data_5FF1 # _entry.id 5FF1 # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.279 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 5FF1 WWPDB D_1000216476 # _pdbx_database_related.db_name PDB _pdbx_database_related.details . _pdbx_database_related.db_id 4QJQ _pdbx_database_related.content_type 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 5FF1 _pdbx_database_status.recvd_initial_deposition_date 2015-12-17 _pdbx_database_status.SG_entry N _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site PDBJ _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 'Singh, R.P.' 1 'Singh, A.' 2 'Sirohi, H.' 3 'Singh, A.K.' 4 'Kaur, P.' 5 'Sharma, S.' 6 'Singh, T.P.' 7 # _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 NE _citation.database_id_Medline ? _citation.details ? _citation.id primary _citation.journal_abbrev 'Febs Open Bio' _citation.journal_id_ASTM ? _citation.journal_id_CSD ? _citation.journal_id_ISSN 2211-5463 _citation.journal_full ? _citation.journal_issue ? _citation.journal_volume 6 _citation.language ? _citation.page_first 640 _citation.page_last 650 _citation.title ;Dual binding mode of antithyroid drug methimazole to mammalian heme peroxidases - structural determination of the lactoperoxidase-methimazole complex at 1.97 angstrom resolution. ; _citation.year 2016 _citation.database_id_CSD ? _citation.pdbx_database_id_DOI 10.1002/2211-5463.12051 _citation.pdbx_database_id_PubMed 27398304 _citation.unpublished_flag ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Singh, R.P.' 1 primary 'Singh, A.' 2 primary 'Sirohi, H.V.' 3 primary 'Singh, A.K.' 4 primary 'Kaur, P.' 5 primary 'Sharma, S.' 6 primary 'Singh, T.P.' 7 # _cell.entry_id 5FF1 _cell.length_a 80.310 _cell.length_b 93.020 _cell.length_c 81.530 _cell.angle_alpha 90.00 _cell.angle_beta 89.97 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _cell.pdbx_unique_axis ? # _symmetry.entry_id 5FF1 _symmetry.space_group_name_H-M 'P 1 21 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 4 # 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 nat Lactoperoxidase 67529.781 2 ? ? 'UNP RESIDUES 118-712' ? 2 non-polymer syn 1-METHYL-1,3-DIHYDRO-2H-IMIDAZOLE-2-THIONE 114.169 4 ? ? ? ? 3 non-polymer syn N-ACETYL-D-GLUCOSAMINE 221.208 9 ? ? ? ? 4 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE' 616.487 2 ? ? ? ? 5 non-polymer syn 'CALCIUM ION' 40.078 2 ? ? ? ? 6 non-polymer syn 'NITRATE ION' 62.005 9 ? ? ? ? 7 non-polymer syn GLYCEROL 92.094 8 ? ? ? ? 8 water nat water 18.015 775 ? ? ? ? # _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 ;SWEVGCGAPVPLVTCDEQSPYRTITGDCNNRRSPALGAANRALARWLPAEYEDGLAVPFGWTQRKTRNGFRVPLAREVSN KIVGYLDEEGVLDQNRSLLFMQWGQIVDHDLDFAPETELGSSEHSKVQCEEYCVQGDECFPIMFPKNDPKLKTQGKCMPF FRAGFVCPTPPYQSLARDQINAVTSFLDASLVYGSEPSLASRLRNLSSPLGLMAVNQEAWDHGLAYPPFNNVKPSPCEFI NTTAHVPCFQAGDSRASEQILLATVHTLLLREHNRLARELKRLNPHWDGEMLYQEARKILGAFIQIITFRDYLPIVLGSE MQKWIPPYQGYNNSVDPRISNVFTFAFRFGHMEVPSTVSRLDENYQPWGPEAELPLHTLFFNTWRIIKDGGIDPLVRGLL AKNSKLMNQNKMVTSELRNKLFQPTHKVHGFDLAAINLQRCRDHGMPGYNSWRGFCGLSQPKTLKGLQAVLKNKVLAKKL LDLYKTPDNIDIWIGGNAEPMVERGRVGPLLACLLGRQFQQIRDGDRFWWENPGVFTEKQRDSLQKVSFSRLICDNTHIT KVPLHAFQANNYPHDFVDCSAVDKLDLSPWASREN ; _entity_poly.pdbx_seq_one_letter_code_can ;SWEVGCGAPVPLVTCDEQSPYRTITGDCNNRRSPALGAANRALARWLPAEYEDGLAVPFGWTQRKTRNGFRVPLAREVSN KIVGYLDEEGVLDQNRSLLFMQWGQIVDHDLDFAPETELGSSEHSKVQCEEYCVQGDECFPIMFPKNDPKLKTQGKCMPF FRAGFVCPTPPYQSLARDQINAVTSFLDASLVYGSEPSLASRLRNLSSPLGLMAVNQEAWDHGLAYPPFNNVKPSPCEFI NTTAHVPCFQAGDSRASEQILLATVHTLLLREHNRLARELKRLNPHWDGEMLYQEARKILGAFIQIITFRDYLPIVLGSE MQKWIPPYQGYNNSVDPRISNVFTFAFRFGHMEVPSTVSRLDENYQPWGPEAELPLHTLFFNTWRIIKDGGIDPLVRGLL AKNSKLMNQNKMVTSELRNKLFQPTHKVHGFDLAAINLQRCRDHGMPGYNSWRGFCGLSQPKTLKGLQAVLKNKVLAKKL LDLYKTPDNIDIWIGGNAEPMVERGRVGPLLACLLGRQFQQIRDGDRFWWENPGVFTEKQRDSLQKVSFSRLICDNTHIT KVPLHAFQANNYPHDFVDCSAVDKLDLSPWASREN ; _entity_poly.pdbx_strand_id A,B _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 SER n 1 2 TRP n 1 3 GLU n 1 4 VAL n 1 5 GLY n 1 6 CYS n 1 7 GLY n 1 8 ALA n 1 9 PRO n 1 10 VAL n 1 11 PRO n 1 12 LEU n 1 13 VAL n 1 14 THR n 1 15 CYS n 1 16 ASP n 1 17 GLU n 1 18 GLN n 1 19 SER n 1 20 PRO n 1 21 TYR n 1 22 ARG n 1 23 THR n 1 24 ILE n 1 25 THR n 1 26 GLY n 1 27 ASP n 1 28 CYS n 1 29 ASN n 1 30 ASN n 1 31 ARG n 1 32 ARG n 1 33 SER n 1 34 PRO n 1 35 ALA n 1 36 LEU n 1 37 GLY n 1 38 ALA n 1 39 ALA n 1 40 ASN n 1 41 ARG n 1 42 ALA n 1 43 LEU n 1 44 ALA n 1 45 ARG n 1 46 TRP n 1 47 LEU n 1 48 PRO n 1 49 ALA n 1 50 GLU n 1 51 TYR n 1 52 GLU n 1 53 ASP n 1 54 GLY n 1 55 LEU n 1 56 ALA n 1 57 VAL n 1 58 PRO n 1 59 PHE n 1 60 GLY n 1 61 TRP n 1 62 THR n 1 63 GLN n 1 64 ARG n 1 65 LYS n 1 66 THR n 1 67 ARG n 1 68 ASN n 1 69 GLY n 1 70 PHE n 1 71 ARG n 1 72 VAL n 1 73 PRO n 1 74 LEU n 1 75 ALA n 1 76 ARG n 1 77 GLU n 1 78 VAL n 1 79 SER n 1 80 ASN n 1 81 LYS n 1 82 ILE n 1 83 VAL n 1 84 GLY n 1 85 TYR n 1 86 LEU n 1 87 ASP n 1 88 GLU n 1 89 GLU n 1 90 GLY n 1 91 VAL n 1 92 LEU n 1 93 ASP n 1 94 GLN n 1 95 ASN n 1 96 ARG n 1 97 SER n 1 98 LEU n 1 99 LEU n 1 100 PHE n 1 101 MET n 1 102 GLN n 1 103 TRP n 1 104 GLY n 1 105 GLN n 1 106 ILE n 1 107 VAL n 1 108 ASP n 1 109 HIS n 1 110 ASP n 1 111 LEU n 1 112 ASP n 1 113 PHE n 1 114 ALA n 1 115 PRO n 1 116 GLU n 1 117 THR n 1 118 GLU n 1 119 LEU n 1 120 GLY n 1 121 SER n 1 122 SER n 1 123 GLU n 1 124 HIS n 1 125 SER n 1 126 LYS n 1 127 VAL n 1 128 GLN n 1 129 CYS n 1 130 GLU n 1 131 GLU n 1 132 TYR n 1 133 CYS n 1 134 VAL n 1 135 GLN n 1 136 GLY n 1 137 ASP n 1 138 GLU n 1 139 CYS n 1 140 PHE n 1 141 PRO n 1 142 ILE n 1 143 MET n 1 144 PHE n 1 145 PRO n 1 146 LYS n 1 147 ASN n 1 148 ASP n 1 149 PRO n 1 150 LYS n 1 151 LEU n 1 152 LYS n 1 153 THR n 1 154 GLN n 1 155 GLY n 1 156 LYS n 1 157 CYS n 1 158 MET n 1 159 PRO n 1 160 PHE n 1 161 PHE n 1 162 ARG n 1 163 ALA n 1 164 GLY n 1 165 PHE n 1 166 VAL n 1 167 CYS n 1 168 PRO n 1 169 THR n 1 170 PRO n 1 171 PRO n 1 172 TYR n 1 173 GLN n 1 174 SER n 1 175 LEU n 1 176 ALA n 1 177 ARG n 1 178 ASP n 1 179 GLN n 1 180 ILE n 1 181 ASN n 1 182 ALA n 1 183 VAL n 1 184 THR n 1 185 SER n 1 186 PHE n 1 187 LEU n 1 188 ASP n 1 189 ALA n 1 190 SER n 1 191 LEU n 1 192 VAL n 1 193 TYR n 1 194 GLY n 1 195 SER n 1 196 GLU n 1 197 PRO n 1 198 SER n 1 199 LEU n 1 200 ALA n 1 201 SER n 1 202 ARG n 1 203 LEU n 1 204 ARG n 1 205 ASN n 1 206 LEU n 1 207 SER n 1 208 SER n 1 209 PRO n 1 210 LEU n 1 211 GLY n 1 212 LEU n 1 213 MET n 1 214 ALA n 1 215 VAL n 1 216 ASN n 1 217 GLN n 1 218 GLU n 1 219 ALA n 1 220 TRP n 1 221 ASP n 1 222 HIS n 1 223 GLY n 1 224 LEU n 1 225 ALA n 1 226 TYR n 1 227 PRO n 1 228 PRO n 1 229 PHE n 1 230 ASN n 1 231 ASN n 1 232 VAL n 1 233 LYS n 1 234 PRO n 1 235 SER n 1 236 PRO n 1 237 CYS n 1 238 GLU n 1 239 PHE n 1 240 ILE n 1 241 ASN n 1 242 THR n 1 243 THR n 1 244 ALA n 1 245 HIS n 1 246 VAL n 1 247 PRO n 1 248 CYS n 1 249 PHE n 1 250 GLN n 1 251 ALA n 1 252 GLY n 1 253 ASP n 1 254 SER n 1 255 ARG n 1 256 ALA n 1 257 SER n 1 258 GLU n 1 259 GLN n 1 260 ILE n 1 261 LEU n 1 262 LEU n 1 263 ALA n 1 264 THR n 1 265 VAL n 1 266 HIS n 1 267 THR n 1 268 LEU n 1 269 LEU n 1 270 LEU n 1 271 ARG n 1 272 GLU n 1 273 HIS n 1 274 ASN n 1 275 ARG n 1 276 LEU n 1 277 ALA n 1 278 ARG n 1 279 GLU n 1 280 LEU n 1 281 LYS n 1 282 ARG n 1 283 LEU n 1 284 ASN n 1 285 PRO n 1 286 HIS n 1 287 TRP n 1 288 ASP n 1 289 GLY n 1 290 GLU n 1 291 MET n 1 292 LEU n 1 293 TYR n 1 294 GLN n 1 295 GLU n 1 296 ALA n 1 297 ARG n 1 298 LYS n 1 299 ILE n 1 300 LEU n 1 301 GLY n 1 302 ALA n 1 303 PHE n 1 304 ILE n 1 305 GLN n 1 306 ILE n 1 307 ILE n 1 308 THR n 1 309 PHE n 1 310 ARG n 1 311 ASP n 1 312 TYR n 1 313 LEU n 1 314 PRO n 1 315 ILE n 1 316 VAL n 1 317 LEU n 1 318 GLY n 1 319 SER n 1 320 GLU n 1 321 MET n 1 322 GLN n 1 323 LYS n 1 324 TRP n 1 325 ILE n 1 326 PRO n 1 327 PRO n 1 328 TYR n 1 329 GLN n 1 330 GLY n 1 331 TYR n 1 332 ASN n 1 333 ASN n 1 334 SER n 1 335 VAL n 1 336 ASP n 1 337 PRO n 1 338 ARG n 1 339 ILE n 1 340 SER n 1 341 ASN n 1 342 VAL n 1 343 PHE n 1 344 THR n 1 345 PHE n 1 346 ALA n 1 347 PHE n 1 348 ARG n 1 349 PHE n 1 350 GLY n 1 351 HIS n 1 352 MET n 1 353 GLU n 1 354 VAL n 1 355 PRO n 1 356 SER n 1 357 THR n 1 358 VAL n 1 359 SER n 1 360 ARG n 1 361 LEU n 1 362 ASP n 1 363 GLU n 1 364 ASN n 1 365 TYR n 1 366 GLN n 1 367 PRO n 1 368 TRP n 1 369 GLY n 1 370 PRO n 1 371 GLU n 1 372 ALA n 1 373 GLU n 1 374 LEU n 1 375 PRO n 1 376 LEU n 1 377 HIS n 1 378 THR n 1 379 LEU n 1 380 PHE n 1 381 PHE n 1 382 ASN n 1 383 THR n 1 384 TRP n 1 385 ARG n 1 386 ILE n 1 387 ILE n 1 388 LYS n 1 389 ASP n 1 390 GLY n 1 391 GLY n 1 392 ILE n 1 393 ASP n 1 394 PRO n 1 395 LEU n 1 396 VAL n 1 397 ARG n 1 398 GLY n 1 399 LEU n 1 400 LEU n 1 401 ALA n 1 402 LYS n 1 403 ASN n 1 404 SER n 1 405 LYS n 1 406 LEU n 1 407 MET n 1 408 ASN n 1 409 GLN n 1 410 ASN n 1 411 LYS n 1 412 MET n 1 413 VAL n 1 414 THR n 1 415 SER n 1 416 GLU n 1 417 LEU n 1 418 ARG n 1 419 ASN n 1 420 LYS n 1 421 LEU n 1 422 PHE n 1 423 GLN n 1 424 PRO n 1 425 THR n 1 426 HIS n 1 427 LYS n 1 428 VAL n 1 429 HIS n 1 430 GLY n 1 431 PHE n 1 432 ASP n 1 433 LEU n 1 434 ALA n 1 435 ALA n 1 436 ILE n 1 437 ASN n 1 438 LEU n 1 439 GLN n 1 440 ARG n 1 441 CYS n 1 442 ARG n 1 443 ASP n 1 444 HIS n 1 445 GLY n 1 446 MET n 1 447 PRO n 1 448 GLY n 1 449 TYR n 1 450 ASN n 1 451 SER n 1 452 TRP n 1 453 ARG n 1 454 GLY n 1 455 PHE n 1 456 CYS n 1 457 GLY n 1 458 LEU n 1 459 SER n 1 460 GLN n 1 461 PRO n 1 462 LYS n 1 463 THR n 1 464 LEU n 1 465 LYS n 1 466 GLY n 1 467 LEU n 1 468 GLN n 1 469 ALA n 1 470 VAL n 1 471 LEU n 1 472 LYS n 1 473 ASN n 1 474 LYS n 1 475 VAL n 1 476 LEU n 1 477 ALA n 1 478 LYS n 1 479 LYS n 1 480 LEU n 1 481 LEU n 1 482 ASP n 1 483 LEU n 1 484 TYR n 1 485 LYS n 1 486 THR n 1 487 PRO n 1 488 ASP n 1 489 ASN n 1 490 ILE n 1 491 ASP n 1 492 ILE n 1 493 TRP n 1 494 ILE n 1 495 GLY n 1 496 GLY n 1 497 ASN n 1 498 ALA n 1 499 GLU n 1 500 PRO n 1 501 MET n 1 502 VAL n 1 503 GLU n 1 504 ARG n 1 505 GLY n 1 506 ARG n 1 507 VAL n 1 508 GLY n 1 509 PRO n 1 510 LEU n 1 511 LEU n 1 512 ALA n 1 513 CYS n 1 514 LEU n 1 515 LEU n 1 516 GLY n 1 517 ARG n 1 518 GLN n 1 519 PHE n 1 520 GLN n 1 521 GLN n 1 522 ILE n 1 523 ARG n 1 524 ASP n 1 525 GLY n 1 526 ASP n 1 527 ARG n 1 528 PHE n 1 529 TRP n 1 530 TRP n 1 531 GLU n 1 532 ASN n 1 533 PRO n 1 534 GLY n 1 535 VAL n 1 536 PHE n 1 537 THR n 1 538 GLU n 1 539 LYS n 1 540 GLN n 1 541 ARG n 1 542 ASP n 1 543 SER n 1 544 LEU n 1 545 GLN n 1 546 LYS n 1 547 VAL n 1 548 SER n 1 549 PHE n 1 550 SER n 1 551 ARG n 1 552 LEU n 1 553 ILE n 1 554 CYS n 1 555 ASP n 1 556 ASN n 1 557 THR n 1 558 HIS n 1 559 ILE n 1 560 THR n 1 561 LYS n 1 562 VAL n 1 563 PRO n 1 564 LEU n 1 565 HIS n 1 566 ALA n 1 567 PHE n 1 568 GLN n 1 569 ALA n 1 570 ASN n 1 571 ASN n 1 572 TYR n 1 573 PRO n 1 574 HIS n 1 575 ASP n 1 576 PHE n 1 577 VAL n 1 578 ASP n 1 579 CYS n 1 580 SER n 1 581 ALA n 1 582 VAL n 1 583 ASP n 1 584 LYS n 1 585 LEU n 1 586 ASP n 1 587 LEU n 1 588 SER n 1 589 PRO n 1 590 TRP n 1 591 ALA n 1 592 SER n 1 593 ARG n 1 594 GLU n 1 595 ASN n # _entity_src_nat.entity_id 1 _entity_src_nat.pdbx_src_id 1 _entity_src_nat.pdbx_alt_source_flag sample _entity_src_nat.pdbx_beg_seq_num 1 _entity_src_nat.pdbx_end_seq_num 595 _entity_src_nat.common_name Goat _entity_src_nat.pdbx_organism_scientific 'Capra hircus' _entity_src_nat.pdbx_ncbi_taxonomy_id 9925 _entity_src_nat.genus ? _entity_src_nat.species ? _entity_src_nat.strain ? _entity_src_nat.tissue ? _entity_src_nat.tissue_fraction ? _entity_src_nat.pdbx_secretion ? _entity_src_nat.pdbx_fragment ? _entity_src_nat.pdbx_variant ? _entity_src_nat.pdbx_cell_line ? _entity_src_nat.pdbx_atcc ? _entity_src_nat.pdbx_cellular_location ? _entity_src_nat.pdbx_organ ? _entity_src_nat.pdbx_organelle ? _entity_src_nat.pdbx_cell ? _entity_src_nat.pdbx_plasmid_name ? _entity_src_nat.pdbx_plasmid_details ? _entity_src_nat.details ? # _struct_ref.db_code A3F9D6_CAPHI _struct_ref.db_name UNP _struct_ref.details ? _struct_ref.entity_id 1 _struct_ref.id 1 _struct_ref.seq_align ? _struct_ref.seq_dif ? _struct_ref.pdbx_db_accession A3F9D6 _struct_ref.pdbx_db_isoform ? _struct_ref.pdbx_seq_one_letter_code ;SWEVGCGAPVPLVTCDEQSPYRTITGDCNNRRSPALGAANRALARWLPAEYEDGLAVPFGWTQRKTRNGFRVPLAREVSN KIVGYLDEEGVLDQNRSLLFMQWGQIVDHDLDFAPETELGSSEHSKVQCEEYCVQGDECFPIMFPKNDPKLKTQGKCMPF FRAGFVCPTPPYQSLARDQINAVTSFLDASLVYGSEPSLASRLRNLSSPLGLMAVNQEAWDHGLAYPPFNNVKPSPCEFI NTTAHVPCFQAGDSRASEQILLATVHTLLLREHNRLARELKRLNPHWDGEMLYQEARKILGAFIQIITFRDYLPIVLGSE MQKWIPPYQGYNNSVDPRISNVFTFAFRFGHMEVPSTVSRLDENYQPWGPEAELPLHTLFFNTWRIIKDGGIDPLVRGLL AKNSKLMNQNKMVTSELRNKLFQPTHKVHGFDLAAINLQRCRDHGMPGYNSWRGFCGLSQPKTLKGLQAVLKNKVLAKKL LDLYKTPDNIDIWIGGNAEPMVERGRVGPLLACLLGRQFQQIRDGDRFWWENPGVFTEKQRDSLQKVSFSRLICDNTHIT KVPLHAFQANNYPHDFVDCSAVDKLDLSPWASREN ; _struct_ref.pdbx_align_begin 118 _struct_ref.pdbx_align_end ? # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.pdbx_db_align_beg_ins_code _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_db_align_end_ins_code _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 5FF1 A 1 ? 595 ? A3F9D6 118 ? 712 ? 1 595 2 1 5FF1 B 1 ? 595 ? A3F9D6 118 ? 712 ? 1 595 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CA non-polymer . 'CALCIUM ION' ? 'Ca 2' 40.078 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 GOL non-polymer . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 92.094 HEM non-polymer . 'PROTOPORPHYRIN IX CONTAINING FE' HEME 'C34 H32 Fe N4 O4' 616.487 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 MMZ non-polymer . 1-METHYL-1,3-DIHYDRO-2H-IMIDAZOLE-2-THIONE METHIMAZOLE 'C4 H6 N2 S' 114.169 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 NO3 non-polymer . 'NITRATE ION' ? 'N O3 -1' 62.005 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 5FF1 _exptl.crystals_number ? _exptl.details ? _exptl.method 'X-RAY DIFFRACTION' _exptl.method_details ? # _exptl_crystal.colour ? _exptl_crystal.density_diffrn ? _exptl_crystal.density_Matthews 2.25 _exptl_crystal.density_method ? _exptl_crystal.density_percent_sol 45.45 _exptl_crystal.description ? _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, HANGING DROP' _exptl_crystal_grow.method_ref ? _exptl_crystal_grow.pH ? _exptl_crystal_grow.pressure ? _exptl_crystal_grow.pressure_esd ? _exptl_crystal_grow.seeding ? _exptl_crystal_grow.seeding_ref ? _exptl_crystal_grow.temp 298 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.temp_esd ? _exptl_crystal_grow.time ? _exptl_crystal_grow.pdbx_details 'Sodium nitrate, PEG' _exptl_crystal_grow.pdbx_pH_range ? # _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 ? _diffrn_detector.detector CCD _diffrn_detector.diffrn_id 1 _diffrn_detector.type MARRESEARCH _diffrn_detector.area_resol_mean ? _diffrn_detector.dtime ? _diffrn_detector.pdbx_frames_total ? _diffrn_detector.pdbx_collection_time_total ? _diffrn_detector.pdbx_collection_date 2015-11-12 # _diffrn_radiation.collimation ? _diffrn_radiation.diffrn_id 1 _diffrn_radiation.filter_edge ? _diffrn_radiation.inhomogeneity ? _diffrn_radiation.monochromator graphite _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 0.97 _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 'ESRF BEAMLINE BM14' _diffrn_source.voltage ? _diffrn_source.take-off_angle ? _diffrn_source.pdbx_wavelength_list 0.97 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_synchrotron_beamline BM14 _diffrn_source.pdbx_synchrotron_site ESRF # _reflns.B_iso_Wilson_estimate ? _reflns.entry_id 5FF1 _reflns.data_reduction_details ? _reflns.data_reduction_method ? _reflns.d_resolution_high 1.97 _reflns.d_resolution_low 40.43 _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 78463 _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 93.8 _reflns.R_free_details ? _reflns.Rmerge_F_all ? _reflns.Rmerge_F_obs ? _reflns.Friedel_coverage ? _reflns.number_gt ? _reflns.threshold_expression ? _reflns.pdbx_redundancy 4 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rmerge_I_all ? _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_av_sigmaI ? _reflns.pdbx_netI_over_sigmaI 7.2 _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 ? _reflns.pdbx_R_split ? # _reflns_shell.d_res_high 1.966 _reflns_shell.d_res_low 2.017 _reflns_shell.meanI_over_sigI_all ? _reflns_shell.meanI_over_sigI_obs 2.1 _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 ? _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 ? _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 ? _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.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 5FF1 _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 78463 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 40.43 _refine.ls_d_res_high 1.97 _refine.ls_percent_reflns_obs 94.84 _refine.ls_R_factor_obs 0.17819 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.17675 _refine.ls_R_factor_R_free 0.22586 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 3.0 _refine.ls_number_reflns_R_free 2415 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.956 _refine.correlation_coeff_Fo_to_Fc_free 0.928 _refine.B_iso_mean 32.345 _refine.aniso_B[1][1] 0.21 _refine.aniso_B[2][2] 1.12 _refine.aniso_B[3][3] -1.33 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.38 _refine.aniso_B[2][3] -0.00 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' _refine.pdbx_starting_model 4OEK _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.194 _refine.pdbx_overall_ESU_R_Free 0.168 _refine.overall_SU_ML ? _refine.pdbx_overall_phase_error ? _refine.overall_SU_B ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 9507 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 326 _refine_hist.number_atoms_solvent 775 _refine_hist.number_atoms_total 10608 _refine_hist.d_res_high 1.97 _refine_hist.d_res_low 40.43 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.017 0.019 ? 10109 'X-RAY DIFFRACTION' ? r_bond_other_d 0.000 0.020 ? 9433 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.850 1.987 ? 13751 'X-RAY DIFFRACTION' ? r_angle_other_deg 3.554 3.003 ? 21602 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 7.403 5.000 ? 1188 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 37.880 23.750 ? 480 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 15.377 15.000 ? 1610 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 19.329 15.000 ? 76 'X-RAY DIFFRACTION' ? r_chiral_restr 0.125 0.200 ? 1453 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.011 0.021 ? 11441 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.020 0.020 ? 2421 'X-RAY DIFFRACTION' ? r_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it 3.048 3.092 ? 4758 'X-RAY DIFFRACTION' ? r_mcbond_other 3.046 3.090 ? 4757 'X-RAY DIFFRACTION' ? r_mcangle_it 4.624 4.623 ? 5944 'X-RAY DIFFRACTION' ? r_mcangle_other 4.624 4.625 ? 5945 'X-RAY DIFFRACTION' ? r_scbond_it 3.256 3.338 ? 5351 'X-RAY DIFFRACTION' ? r_scbond_other 3.256 3.338 ? 5352 'X-RAY DIFFRACTION' ? r_scangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_other 5.049 4.924 ? 7808 'X-RAY DIFFRACTION' ? r_long_range_B_refined 8.399 25.170 ? 12550 'X-RAY DIFFRACTION' ? r_long_range_B_other 8.399 25.170 ? 12551 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # loop_ _refine_ls_restr_ncs.pdbx_refine_id _refine_ls_restr_ncs.dom_id _refine_ls_restr_ncs.pdbx_ens_id _refine_ls_restr_ncs.pdbx_ordinal _refine_ls_restr_ncs.ncs_model_details _refine_ls_restr_ncs.rms_dev_position _refine_ls_restr_ncs.weight_position _refine_ls_restr_ncs.rms_dev_B_iso _refine_ls_restr_ncs.weight_B_iso _refine_ls_restr_ncs.pdbx_auth_asym_id _refine_ls_restr_ncs.pdbx_number _refine_ls_restr_ncs.pdbx_type 'X-RAY DIFFRACTION' 1 1 1 ? 0.10 0.05 ? ? A 3815 'interatomic distance' 'X-RAY DIFFRACTION' 2 1 2 ? 0.10 0.05 ? ? B 3815 'interatomic distance' # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.966 _refine_ls_shell.d_res_low 2.017 _refine_ls_shell.number_reflns_R_work 5009 _refine_ls_shell.R_factor_R_work 0.270 _refine_ls_shell.percent_reflns_obs 81.95 _refine_ls_shell.R_factor_R_free 0.332 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 145 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.R_factor_obs ? _refine_ls_shell.number_reflns_obs ? # loop_ _struct_ncs_dom.id _struct_ncs_dom.details _struct_ncs_dom.pdbx_ens_id 1 A 1 2 B 1 # loop_ _struct_ncs_dom_lim.dom_id _struct_ncs_dom_lim.beg_auth_asym_id _struct_ncs_dom_lim.beg_auth_seq_id _struct_ncs_dom_lim.end_auth_asym_id _struct_ncs_dom_lim.end_auth_seq_id _struct_ncs_dom_lim.pdbx_component_id _struct_ncs_dom_lim.pdbx_refine_code _struct_ncs_dom_lim.beg_label_asym_id _struct_ncs_dom_lim.beg_label_comp_id _struct_ncs_dom_lim.beg_label_seq_id _struct_ncs_dom_lim.beg_label_alt_id _struct_ncs_dom_lim.end_label_asym_id _struct_ncs_dom_lim.end_label_comp_id _struct_ncs_dom_lim.end_label_seq_id _struct_ncs_dom_lim.end_label_alt_id _struct_ncs_dom_lim.pdbx_ens_id _struct_ncs_dom_lim.selection_details 1 A 1 A 595 0 0 ? ? ? ? ? ? ? ? 1 ? 2 B 1 B 595 0 0 ? ? ? ? ? ? ? ? 1 ? # _struct_ncs_ens.id 1 _struct_ncs_ens.details ? # _struct.entry_id 5FF1 _struct.title ;Two way mode of binding of antithyroid drug methimazole to mammalian heme peroxidases: Structure of the complex of lactoperoxidase with methimazole at 1.97 Angstrom resolution ; _struct.pdbx_descriptor Lactoperoxidase _struct.pdbx_model_details ? _struct.pdbx_formula_weight ? _struct.pdbx_formula_weight_method ? _struct.pdbx_model_type_details ? _struct.pdbx_CASP_flag ? # _struct_keywords.entry_id 5FF1 _struct_keywords.text 'Inhibitor, peroxidase, OXIDOREDUCTASE' _struct_keywords.pdbx_keywords OXIDOREDUCTASE # 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 1 ? C N N 2 ? D N N 2 ? E N N 3 ? F N N 3 ? G N N 3 ? H N N 3 ? I N N 4 ? J N N 5 ? K N N 6 ? L N N 6 ? M N N 6 ? N N N 6 ? O N N 6 ? P N N 7 ? Q N N 7 ? R N N 7 ? S N N 7 ? T N N 2 ? U N N 3 ? V N N 3 ? W N N 3 ? X N N 3 ? Y N N 3 ? Z N N 4 ? AA N N 5 ? BA N N 6 ? CA N N 6 ? DA N N 6 ? EA N N 6 ? FA N N 2 ? GA N N 7 ? HA N N 7 ? IA N N 7 ? JA N N 7 ? KA N N 8 ? LA 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 LEU A 74 ? VAL A 83 ? LEU A 74 VAL A 83 1 ? 10 HELX_P HELX_P2 AA2 LEU A 98 ? ASP A 112 ? LEU A 98 ASP A 112 1 ? 15 HELX_P HELX_P3 AA3 SER A 122 ? GLU A 131 ? SER A 122 GLU A 131 1 ? 10 HELX_P HELX_P4 AA4 ASP A 148 ? THR A 153 ? ASP A 148 THR A 153 5 ? 6 HELX_P HELX_P5 AA5 ALA A 189 ? GLY A 194 ? ALA A 189 GLY A 194 1 ? 6 HELX_P HELX_P6 AA6 GLU A 196 ? ARG A 204 ? GLU A 196 ARG A 204 1 ? 9 HELX_P HELX_P7 AA7 SER A 235 ? ILE A 240 ? SER A 235 ILE A 240 1 ? 6 HELX_P HELX_P8 AA8 GLN A 259 ? ASN A 284 ? GLN A 259 ASN A 284 1 ? 26 HELX_P HELX_P9 AA9 ASP A 288 ? ASP A 311 ? ASP A 288 ASP A 311 1 ? 24 HELX_P HELX_P10 AB1 ASP A 311 ? GLY A 318 ? ASP A 311 GLY A 318 1 ? 8 HELX_P HELX_P11 AB2 GLU A 320 ? ILE A 325 ? GLU A 320 ILE A 325 1 ? 6 HELX_P HELX_P12 AB3 SER A 340 ? PHE A 347 ? SER A 340 PHE A 347 1 ? 8 HELX_P HELX_P13 AB4 ARG A 348 ? VAL A 354 ? ARG A 348 VAL A 354 5 ? 7 HELX_P HELX_P14 AB5 HIS A 377 ? PHE A 380 ? HIS A 377 PHE A 380 5 ? 4 HELX_P HELX_P15 AB6 THR A 383 ? LYS A 388 ? THR A 383 LYS A 388 1 ? 6 HELX_P HELX_P16 AB7 ILE A 392 ? LYS A 402 ? ILE A 392 LYS A 402 1 ? 11 HELX_P HELX_P17 AB8 THR A 414 ? ASN A 419 ? THR A 414 ASN A 419 1 ? 6 HELX_P HELX_P18 AB9 ASP A 432 ? HIS A 444 ? ASP A 432 HIS A 444 1 ? 13 HELX_P HELX_P19 AC1 GLY A 448 ? CYS A 456 ? GLY A 448 CYS A 456 1 ? 9 HELX_P HELX_P20 AC2 THR A 463 ? LYS A 472 ? THR A 463 LYS A 472 1 ? 10 HELX_P HELX_P21 AC3 ASN A 473 ? LYS A 485 ? ASN A 473 LYS A 485 1 ? 13 HELX_P HELX_P22 AC4 THR A 486 ? ILE A 490 ? THR A 486 ILE A 490 5 ? 5 HELX_P HELX_P23 AC5 ASP A 491 ? GLU A 499 ? ASP A 491 GLU A 499 1 ? 9 HELX_P HELX_P24 AC6 GLY A 508 ? GLY A 525 ? GLY A 508 GLY A 525 1 ? 18 HELX_P HELX_P25 AC7 THR A 537 ? GLN A 545 ? THR A 537 GLN A 545 1 ? 9 HELX_P HELX_P26 AC8 SER A 548 ? THR A 557 ? SER A 548 THR A 557 1 ? 10 HELX_P HELX_P27 AC9 SER A 580 ? VAL A 582 ? SER A 580 VAL A 582 5 ? 3 HELX_P HELX_P28 AD1 LEU A 587 ? ALA A 591 ? LEU A 587 ALA A 591 5 ? 5 HELX_P HELX_P29 AD2 LEU B 74 ? VAL B 83 ? LEU B 74 VAL B 83 1 ? 10 HELX_P HELX_P30 AD3 LEU B 98 ? ASP B 112 ? LEU B 98 ASP B 112 1 ? 15 HELX_P HELX_P31 AD4 SER B 122 ? GLU B 131 ? SER B 122 GLU B 131 1 ? 10 HELX_P HELX_P32 AD5 ASP B 148 ? THR B 153 ? ASP B 148 THR B 153 5 ? 6 HELX_P HELX_P33 AD6 ALA B 189 ? GLY B 194 ? ALA B 189 GLY B 194 1 ? 6 HELX_P HELX_P34 AD7 GLU B 196 ? ARG B 204 ? GLU B 196 ARG B 204 1 ? 9 HELX_P HELX_P35 AD8 SER B 235 ? ILE B 240 ? SER B 235 ILE B 240 1 ? 6 HELX_P HELX_P36 AD9 GLN B 259 ? ASN B 284 ? GLN B 259 ASN B 284 1 ? 26 HELX_P HELX_P37 AE1 ASP B 288 ? ASP B 311 ? ASP B 288 ASP B 311 1 ? 24 HELX_P HELX_P38 AE2 ASP B 311 ? GLY B 318 ? ASP B 311 GLY B 318 1 ? 8 HELX_P HELX_P39 AE3 GLU B 320 ? ILE B 325 ? GLU B 320 ILE B 325 1 ? 6 HELX_P HELX_P40 AE4 VAL B 342 ? PHE B 347 ? VAL B 342 PHE B 347 1 ? 6 HELX_P HELX_P41 AE5 ARG B 348 ? VAL B 354 ? ARG B 348 VAL B 354 5 ? 7 HELX_P HELX_P42 AE6 HIS B 377 ? PHE B 380 ? HIS B 377 PHE B 380 5 ? 4 HELX_P HELX_P43 AE7 THR B 383 ? LYS B 388 ? THR B 383 LYS B 388 1 ? 6 HELX_P HELX_P44 AE8 ILE B 392 ? LYS B 402 ? ILE B 392 LYS B 402 1 ? 11 HELX_P HELX_P45 AE9 THR B 414 ? ASN B 419 ? THR B 414 ASN B 419 1 ? 6 HELX_P HELX_P46 AF1 ASP B 432 ? HIS B 444 ? ASP B 432 HIS B 444 1 ? 13 HELX_P HELX_P47 AF2 GLY B 448 ? CYS B 456 ? GLY B 448 CYS B 456 1 ? 9 HELX_P HELX_P48 AF3 THR B 463 ? LYS B 472 ? THR B 463 LYS B 472 1 ? 10 HELX_P HELX_P49 AF4 ASN B 473 ? LYS B 485 ? ASN B 473 LYS B 485 1 ? 13 HELX_P HELX_P50 AF5 THR B 486 ? ILE B 490 ? THR B 486 ILE B 490 5 ? 5 HELX_P HELX_P51 AF6 ASP B 491 ? GLU B 499 ? ASP B 491 GLU B 499 1 ? 9 HELX_P HELX_P52 AF7 GLY B 508 ? GLY B 525 ? GLY B 508 GLY B 525 1 ? 18 HELX_P HELX_P53 AF8 THR B 537 ? GLN B 545 ? THR B 537 GLN B 545 1 ? 9 HELX_P HELX_P54 AF9 SER B 548 ? THR B 557 ? SER B 548 THR B 557 1 ? 10 HELX_P HELX_P55 AG1 SER B 580 ? VAL B 582 ? SER B 580 VAL B 582 5 ? 3 HELX_P HELX_P56 AG2 LEU B 587 ? ALA B 591 ? LEU B 587 ALA B 591 5 ? 5 # _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 6 SG ? ? ? 1_555 A CYS 167 SG ? ? A CYS 6 A CYS 167 1_555 ? ? ? ? ? ? ? 2.034 ? disulf2 disulf ? ? A CYS 15 SG ? ? ? 1_555 A CYS 28 SG ? ? A CYS 15 A CYS 28 1_555 ? ? ? ? ? ? ? 2.025 ? disulf3 disulf ? ? A CYS 129 SG ? ? ? 1_555 A CYS 139 SG ? ? A CYS 129 A CYS 139 1_555 ? ? ? ? ? ? ? 2.016 ? disulf4 disulf ? ? A CYS 133 SG ? ? ? 1_555 A CYS 157 SG ? ? A CYS 133 A CYS 157 1_555 ? ? ? ? ? ? ? 2.009 ? disulf5 disulf ? ? A CYS 237 SG ? ? ? 1_555 A CYS 248 SG ? ? A CYS 237 A CYS 248 1_555 ? ? ? ? ? ? ? 2.005 ? disulf6 disulf ? ? A CYS 456 SG ? ? ? 1_555 A CYS 513 SG ? ? A CYS 456 A CYS 513 1_555 ? ? ? ? ? ? ? 1.978 ? disulf7 disulf ? ? A CYS 554 SG ? ? ? 1_555 A CYS 579 SG ? ? A CYS 554 A CYS 579 1_555 ? ? ? ? ? ? ? 2.053 ? disulf8 disulf ? ? B CYS 6 SG ? ? ? 1_555 B CYS 167 SG ? ? B CYS 6 B CYS 167 1_555 ? ? ? ? ? ? ? 2.040 ? disulf9 disulf ? ? B CYS 15 SG ? ? ? 1_555 B CYS 28 SG ? ? B CYS 15 B CYS 28 1_555 ? ? ? ? ? ? ? 2.040 ? disulf10 disulf ? ? B CYS 129 SG ? ? ? 1_555 B CYS 139 SG ? ? B CYS 129 B CYS 139 1_555 ? ? ? ? ? ? ? 2.028 ? disulf11 disulf ? ? B CYS 133 SG ? ? ? 1_555 B CYS 157 SG ? ? B CYS 133 B CYS 157 1_555 ? ? ? ? ? ? ? 2.028 ? disulf12 disulf ? ? B CYS 237 SG ? ? ? 1_555 B CYS 248 SG ? ? B CYS 237 B CYS 248 1_555 ? ? ? ? ? ? ? 2.038 ? disulf13 disulf ? ? B CYS 456 SG ? ? ? 1_555 B CYS 513 SG ? ? B CYS 456 B CYS 513 1_555 ? ? ? ? ? ? ? 2.025 ? disulf14 disulf ? ? B CYS 554 SG ? ? ? 1_555 B CYS 579 SG ? ? B CYS 554 B CYS 579 1_555 ? ? ? ? ? ? ? 2.051 ? covale1 covale one ? A ASN 95 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 95 A NAG 604 1_555 ? ? ? ? ? ? ? 1.431 ? metalc1 metalc ? ? A ASP 110 O ? ? ? 1_555 J CA . CA ? ? A ASP 110 A CA 608 1_555 ? ? ? ? ? ? ? 2.508 ? metalc2 metalc ? ? A ASP 110 OD1 ? ? ? 1_555 J CA . CA ? ? A ASP 110 A CA 608 1_555 ? ? ? ? ? ? ? 2.352 ? metalc3 metalc ? ? A THR 184 O ? ? ? 1_555 J CA . CA ? ? A THR 184 A CA 608 1_555 ? ? ? ? ? ? ? 2.443 ? metalc4 metalc ? ? A THR 184 OG1 ? ? ? 1_555 J CA . CA ? ? A THR 184 A CA 608 1_555 ? ? ? ? ? ? ? 2.367 ? metalc5 metalc ? ? A PHE 186 O ? ? ? 1_555 J CA . CA ? ? A PHE 186 A CA 608 1_555 ? ? ? ? ? ? ? 2.241 ? metalc6 metalc ? ? A ASP 188 OD1 ? ? ? 1_555 J CA . CA ? ? A ASP 188 A CA 608 1_555 ? ? ? ? ? ? ? 2.452 ? metalc7 metalc ? ? A SER 190 OG ? ? ? 1_555 J CA . CA ? ? A SER 190 A CA 608 1_555 ? ? ? ? ? ? ? 2.367 ? covale2 covale one ? A ASN 205 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 205 A NAG 606 1_555 ? ? ? ? ? ? ? 1.471 ? covale3 covale one ? A ASN 241 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 241 A NAG 603 1_555 ? ? ? ? ? ? ? 1.446 ? covale4 covale one ? A ASN 332 ND2 ? ? ? 1_555 G NAG . C1 ? ? A ASN 332 A NAG 605 1_555 ? ? ? ? ? ? ? 1.482 ? metalc8 metalc ? ? A HIS 351 NE2 ? ? ? 1_555 I HEM . FE ? ? A HIS 351 A HEM 607 1_555 ? ? ? ? ? ? ? 2.148 ? covale5 covale one ? B ASN 95 ND2 ? ? ? 1_555 U NAG . C1 ? ? B ASN 95 B NAG 602 1_555 ? ? ? ? ? ? ? 1.447 ? metalc9 metalc ? ? B ASP 110 O ? ? ? 1_555 AA CA . CA ? ? B ASP 110 B CA 608 1_555 ? ? ? ? ? ? ? 2.437 ? metalc10 metalc ? ? B ASP 110 OD1 ? ? ? 1_555 AA CA . CA ? ? B ASP 110 B CA 608 1_555 ? ? ? ? ? ? ? 2.299 ? metalc11 metalc ? ? B THR 184 O ? ? ? 1_555 AA CA . CA ? ? B THR 184 B CA 608 1_555 ? ? ? ? ? ? ? 2.396 ? metalc12 metalc ? ? B THR 184 OG1 ? ? ? 1_555 AA CA . CA ? ? B THR 184 B CA 608 1_555 ? ? ? ? ? ? ? 2.475 ? metalc13 metalc ? ? B PHE 186 O ? ? ? 1_555 AA CA . CA ? ? B PHE 186 B CA 608 1_555 ? ? ? ? ? ? ? 2.240 ? metalc14 metalc ? ? B ASP 188 OD1 ? ? ? 1_555 AA CA . CA ? ? B ASP 188 B CA 608 1_555 ? ? ? ? ? ? ? 2.594 ? metalc15 metalc ? ? B SER 190 OG ? ? ? 1_555 AA CA . CA ? ? B SER 190 B CA 608 1_555 ? ? ? ? ? ? ? 2.369 ? covale6 covale one ? B ASN 205 ND2 ? ? ? 1_555 X NAG . C1 ? ? B ASN 205 B NAG 605 1_555 ? ? ? ? ? ? ? 1.476 ? covale7 covale one ? B ASN 241 ND2 ? ? ? 1_555 V NAG . C1 ? ? B ASN 241 B NAG 603 1_555 ? ? ? ? ? ? ? 1.433 ? covale8 covale one ? B ASN 332 ND2 ? ? ? 1_555 W NAG . C1 ? ? B ASN 332 B NAG 604 1_555 ? ? ? ? ? ? ? 1.469 ? metalc16 metalc ? ? B HIS 351 NE2 ? ? ? 1_555 Z HEM . FE ? ? B HIS 351 B HEM 607 1_555 ? ? ? ? ? ? ? 2.129 ? covale9 covale none ? C MMZ . N1 ? ? ? 1_555 D MMZ . C2 ? ? A MMZ 601 A MMZ 602 1_555 ? ? ? ? ? ? ? 1.466 ? covale10 covale none ? C MMZ . C1A ? ? ? 1_555 D MMZ . S2 ? ? A MMZ 601 A MMZ 602 1_555 ? ? ? ? ? ? ? 1.743 ? covale11 covale none ? C MMZ . C2 ? ? ? 1_555 D MMZ . N1 ? ? A MMZ 601 A MMZ 602 1_555 ? ? ? ? ? ? ? 1.456 ? covale12 covale none ? C MMZ . C2 ? ? ? 1_555 D MMZ . C2 ? ? A MMZ 601 A MMZ 602 1_555 ? ? ? ? ? ? ? 1.635 ? covale13 covale none ? C MMZ . S2 ? ? ? 1_555 D MMZ . C1A ? ? A MMZ 601 A MMZ 602 1_555 ? ? ? ? ? ? ? 1.649 ? covale14 covale none ? C MMZ . N3 ? ? ? 1_555 D MMZ . C2 ? ? A MMZ 601 A MMZ 602 1_555 ? ? ? ? ? ? ? 1.222 ? covale15 covale none ? C MMZ . N3 ? ? ? 1_555 D MMZ . C3A ? ? A MMZ 601 A MMZ 602 1_555 ? ? ? ? ? ? ? 1.487 ? covale16 covale none ? C MMZ . N3 ? ? ? 1_555 D MMZ . C4 ? ? A MMZ 601 A MMZ 602 1_555 ? ? ? ? ? ? ? 1.365 ? covale17 covale none ? C MMZ . C3A ? ? ? 1_555 D MMZ . N3 ? ? A MMZ 601 A MMZ 602 1_555 ? ? ? ? ? ? ? 1.438 ? covale18 covale none ? C MMZ . C4 ? ? ? 1_555 D MMZ . N3 ? ? A MMZ 601 A MMZ 602 1_555 ? ? ? ? ? ? ? 1.437 ? metalc17 metalc ? ? D MMZ . S2 ? ? ? 1_555 I HEM . FE ? ? A MMZ 602 A HEM 607 1_555 ? ? ? ? ? ? ? 2.415 ? covale19 covale none ? T MMZ . N1 ? ? ? 1_555 FA MMZ . C2 ? ? B MMZ 601 B MMZ 613 1_555 ? ? ? ? ? ? ? 1.548 ? covale20 covale none ? T MMZ . C1A ? ? ? 1_555 FA MMZ . S2 ? ? B MMZ 601 B MMZ 613 1_555 ? ? ? ? ? ? ? 1.784 ? covale21 covale none ? T MMZ . C2 ? ? ? 1_555 FA MMZ . C1A ? ? B MMZ 601 B MMZ 613 1_555 ? ? ? ? ? ? ? 1.182 ? metalc18 metalc ? ? T MMZ . S2 ? ? ? 1_555 Z HEM . FE ? ? B MMZ 601 B HEM 607 1_555 ? ? ? ? ? ? ? 2.665 ? covale22 covale none ? T MMZ . N3 ? ? ? 1_555 FA MMZ . C2 ? ? B MMZ 601 B MMZ 613 1_555 ? ? ? ? ? ? ? 1.307 ? covale23 covale none ? T MMZ . N3 ? ? ? 1_555 FA MMZ . C4 ? ? B MMZ 601 B MMZ 613 1_555 ? ? ? ? ? ? ? 1.325 ? covale24 covale none ? T MMZ . N3 ? ? ? 1_555 FA MMZ . C3A ? ? B MMZ 601 B MMZ 613 1_555 ? ? ? ? ? ? ? 1.471 ? covale25 covale none ? T MMZ . C3A ? ? ? 1_555 FA MMZ . N3 ? ? B MMZ 601 B MMZ 613 1_555 ? ? ? ? ? ? ? 1.408 ? covale26 covale none ? T MMZ . C4 ? ? ? 1_555 FA MMZ . N3 ? ? B MMZ 601 B MMZ 613 1_555 ? ? ? ? ? ? ? 1.496 ? covale27 covale both ? X NAG . O4 ? ? ? 1_555 Y NAG . C1 ? ? B NAG 605 B NAG 606 1_555 ? ? ? ? ? ? ? 1.437 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 PRO 170 A . ? PRO 170 A PRO 171 A ? PRO 171 A 1 -4.12 2 LYS 233 A . ? LYS 233 A PRO 234 A ? PRO 234 A 1 -3.67 3 TYR 572 A . ? TYR 572 A PRO 573 A ? PRO 573 A 1 -2.62 4 TRP 2 B . ? TRP 2 B GLU 3 B ? GLU 3 B 1 -2.93 5 LYS 233 B . ? LYS 233 B PRO 234 B ? PRO 234 B 1 -3.69 6 TYR 572 B . ? TYR 572 B PRO 573 B ? PRO 573 B 1 -9.59 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA1 ? 2 ? AA2 ? 2 ? AA3 ? 2 ? AA4 ? 2 ? AA5 ? 2 ? AA6 ? 2 ? AA7 ? 2 ? AA8 ? 2 ? AA9 ? 2 ? AB1 ? 2 ? AB2 ? 2 ? AB3 ? 2 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense AA1 1 2 ? anti-parallel AA2 1 2 ? anti-parallel AA3 1 2 ? anti-parallel AA4 1 2 ? anti-parallel AA5 1 2 ? anti-parallel AA6 1 2 ? anti-parallel AA7 1 2 ? anti-parallel AA8 1 2 ? anti-parallel AA9 1 2 ? anti-parallel AB1 1 2 ? anti-parallel AB2 1 2 ? anti-parallel AB3 1 2 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id AA1 1 ARG A 41 ? ALA A 42 ? ARG A 41 ALA A 42 AA1 2 ILE A 180 ? ASN A 181 ? ILE A 180 ASN A 181 AA2 1 LEU A 92 ? SER A 97 ? LEU A 92 SER A 97 AA2 2 ASN A 403 ? LYS A 405 ? ASN A 403 LYS A 405 AA3 1 ILE A 142 ? MET A 143 ? ILE A 142 MET A 143 AA3 2 CYS A 157 ? MET A 158 ? CYS A 157 MET A 158 AA4 1 THR A 357 ? SER A 359 ? THR A 357 SER A 359 AA4 2 GLU A 373 ? PRO A 375 ? GLU A 373 PRO A 375 AA5 1 LEU A 421 ? PHE A 422 ? LEU A 421 PHE A 422 AA5 2 HIS A 429 ? PHE A 431 ? HIS A 429 PHE A 431 AA6 1 LYS A 561 ? VAL A 562 ? LYS A 561 VAL A 562 AA6 2 VAL A 577 ? ASP A 578 ? VAL A 577 ASP A 578 AA7 1 ARG B 41 ? ALA B 42 ? ARG B 41 ALA B 42 AA7 2 ILE B 180 ? ASN B 181 ? ILE B 180 ASN B 181 AA8 1 LEU B 92 ? SER B 97 ? LEU B 92 SER B 97 AA8 2 ASN B 403 ? LYS B 405 ? ASN B 403 LYS B 405 AA9 1 ILE B 142 ? MET B 143 ? ILE B 142 MET B 143 AA9 2 CYS B 157 ? MET B 158 ? CYS B 157 MET B 158 AB1 1 THR B 357 ? SER B 359 ? THR B 357 SER B 359 AB1 2 GLU B 373 ? PRO B 375 ? GLU B 373 PRO B 375 AB2 1 LEU B 421 ? PHE B 422 ? LEU B 421 PHE B 422 AB2 2 HIS B 429 ? PHE B 431 ? HIS B 429 PHE B 431 AB3 1 LYS B 561 ? VAL B 562 ? LYS B 561 VAL B 562 AB3 2 VAL B 577 ? ASP B 578 ? VAL B 577 ASP B 578 # 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 ARG A 41 ? N ARG A 41 O ASN A 181 ? O ASN A 181 AA2 1 2 N ASP A 93 ? N ASP A 93 O SER A 404 ? O SER A 404 AA3 1 2 N ILE A 142 ? N ILE A 142 O MET A 158 ? O MET A 158 AA4 1 2 N VAL A 358 ? N VAL A 358 O LEU A 374 ? O LEU A 374 AA5 1 2 N LEU A 421 ? N LEU A 421 O PHE A 431 ? O PHE A 431 AA6 1 2 N VAL A 562 ? N VAL A 562 O VAL A 577 ? O VAL A 577 AA7 1 2 N ARG B 41 ? N ARG B 41 O ASN B 181 ? O ASN B 181 AA8 1 2 N ASP B 93 ? N ASP B 93 O SER B 404 ? O SER B 404 AA9 1 2 N ILE B 142 ? N ILE B 142 O MET B 158 ? O MET B 158 AB1 1 2 N VAL B 358 ? N VAL B 358 O LEU B 374 ? O LEU B 374 AB2 1 2 N LEU B 421 ? N LEU B 421 O PHE B 431 ? O PHE B 431 AB3 1 2 N VAL B 562 ? N VAL B 562 O VAL B 577 ? O VAL B 577 # 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 HEM 607 ? 22 'binding site for residue HEM A 607' AC2 Software A CA 608 ? 5 'binding site for residue CA A 608' AC3 Software A NO3 609 ? 10 'binding site for residue NO3 A 609' AC4 Software A NO3 610 ? 4 'binding site for residue NO3 A 610' AC5 Software A NO3 611 ? 6 'binding site for residue NO3 A 611' AC6 Software A NO3 612 ? 6 'binding site for residue NO3 A 612' AC7 Software A NO3 613 ? 3 'binding site for residue NO3 A 613' AC8 Software A GOL 614 ? 8 'binding site for residue GOL A 614' AC9 Software A GOL 615 ? 4 'binding site for residue GOL A 615' AD1 Software A GOL 616 ? 5 'binding site for residue GOL A 616' AD2 Software A GOL 617 ? 9 'binding site for residue GOL A 617' AD3 Software B HEM 607 ? 22 'binding site for residue HEM B 607' AD4 Software B CA 608 ? 5 'binding site for residue CA B 608' AD5 Software B NO3 609 ? 10 'binding site for residue NO3 B 609' AD6 Software B NO3 610 ? 6 'binding site for residue NO3 B 610' AD7 Software B NO3 611 ? 5 'binding site for residue NO3 B 611' AD8 Software B NO3 612 ? 5 'binding site for residue NO3 B 612' AD9 Software B GOL 614 ? 6 'binding site for residue GOL B 614' AE1 Software B GOL 615 ? 9 'binding site for residue GOL B 615' AE2 Software B GOL 616 ? 4 'binding site for residue GOL B 616' AE3 Software B GOL 617 ? 5 'binding site for residue GOL B 617' AE4 Software A NAG 604 ? 2 'binding site for Mono-Saccharide NAG A 604 bound to ASN A 95' AE5 Software A NAG 606 ? 11 'binding site for Mono-Saccharide NAG A 606 bound to ASN A 205' AE6 Software A NAG 603 ? 5 'binding site for Mono-Saccharide NAG A 603 bound to ASN A 241' AE7 Software A NAG 605 ? 3 'binding site for Mono-Saccharide NAG A 605 bound to ASN A 332' AE8 Software B NAG 602 ? 2 'binding site for Mono-Saccharide NAG B 602 bound to ASN B 95' AE9 Software B ASN 205 ? 9 'binding site for Poly-Saccharide residues NAG B 605 through NAG B 606 bound to ASN B 205' AF1 Software B NAG 603 ? 5 'binding site for Mono-Saccharide NAG B 603 bound to ASN B 241' AF2 Software B NAG 604 ? 3 'binding site for Mono-Saccharide NAG B 604 bound to ASN B 332' AF3 Software A MMZ 601 ? 7 'binding site for residues MMZ A 601 and MMZ A 602' AF4 Software A MMZ 601 ? 7 'binding site for residues MMZ A 601 and MMZ A 602' AF5 Software A MMZ 601 ? 7 'binding site for residues MMZ A 601 and MMZ A 602' AF6 Software A MMZ 601 ? 7 'binding site for residues MMZ A 601 and MMZ A 602' AF7 Software A MMZ 601 ? 7 'binding site for residues MMZ A 601 and MMZ A 602' AF8 Software A MMZ 601 ? 7 'binding site for residues MMZ A 601 and MMZ A 602' AF9 Software A MMZ 601 ? 7 'binding site for residues MMZ A 601 and MMZ A 602' AG1 Software A MMZ 601 ? 7 'binding site for residues MMZ A 601 and MMZ A 602' AG2 Software A MMZ 601 ? 7 'binding site for residues MMZ A 601 and MMZ A 602' AG3 Software A MMZ 601 ? 7 'binding site for residues MMZ A 601 and MMZ A 602' AG4 Software B MMZ 601 ? 8 'binding site for residues MMZ B 601 and MMZ B 613' AG5 Software B MMZ 601 ? 8 'binding site for residues MMZ B 601 and MMZ B 613' AG6 Software B MMZ 601 ? 8 'binding site for residues MMZ B 601 and MMZ B 613' AG7 Software B MMZ 601 ? 8 'binding site for residues MMZ B 601 and MMZ B 613' AG8 Software B MMZ 601 ? 8 'binding site for residues MMZ B 601 and MMZ B 613' AG9 Software B MMZ 601 ? 8 'binding site for residues MMZ B 601 and MMZ B 613' AH1 Software B MMZ 601 ? 8 'binding site for residues MMZ B 601 and MMZ B 613' AH2 Software B MMZ 601 ? 8 'binding site for residues MMZ B 601 and MMZ B 613' # 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 22 MET A 101 ? MET A 101 . ? 1_555 ? 2 AC1 22 GLY A 104 ? GLY A 104 . ? 1_555 ? 3 AC1 22 GLN A 105 ? GLN A 105 . ? 1_555 ? 4 AC1 22 ASP A 108 ? ASP A 108 . ? 1_555 ? 5 AC1 22 ASP A 112 ? ASP A 112 . ? 1_555 ? 6 AC1 22 PHE A 113 ? PHE A 113 . ? 1_555 ? 7 AC1 22 ALA A 114 ? ALA A 114 . ? 1_555 ? 8 AC1 22 ARG A 255 ? ARG A 255 . ? 1_555 ? 9 AC1 22 GLU A 258 ? GLU A 258 . ? 1_555 ? 10 AC1 22 GLN A 259 ? GLN A 259 . ? 1_555 ? 11 AC1 22 THR A 344 ? THR A 344 . ? 1_555 ? 12 AC1 22 PHE A 347 ? PHE A 347 . ? 1_555 ? 13 AC1 22 ARG A 348 ? ARG A 348 . ? 1_555 ? 14 AC1 22 GLY A 350 ? GLY A 350 . ? 1_555 ? 15 AC1 22 HIS A 351 ? HIS A 351 . ? 1_555 ? 16 AC1 22 GLN A 423 ? GLN A 423 . ? 1_555 ? 17 AC1 22 ILE A 436 ? ILE A 436 . ? 1_555 ? 18 AC1 22 ARG A 440 ? ARG A 440 . ? 1_555 ? 19 AC1 22 MMZ C . ? MMZ A 601 . ? 1_555 ? 20 AC1 22 MMZ D . ? MMZ A 602 . ? 1_555 ? 21 AC1 22 HOH KA . ? HOH A 703 . ? 1_555 ? 22 AC1 22 HOH KA . ? HOH A 817 . ? 1_555 ? 23 AC2 5 ASP A 110 ? ASP A 110 . ? 1_555 ? 24 AC2 5 THR A 184 ? THR A 184 . ? 1_555 ? 25 AC2 5 PHE A 186 ? PHE A 186 . ? 1_555 ? 26 AC2 5 ASP A 188 ? ASP A 188 . ? 1_555 ? 27 AC2 5 SER A 190 ? SER A 190 . ? 1_555 ? 28 AC3 10 ALA A 44 ? ALA A 44 . ? 1_555 ? 29 AC3 10 ARG A 45 ? ARG A 45 . ? 1_555 ? 30 AC3 10 TRP A 46 ? TRP A 46 . ? 1_555 ? 31 AC3 10 LEU A 47 ? LEU A 47 . ? 1_555 ? 32 AC3 10 SER A 340 ? SER A 340 . ? 1_555 ? 33 AC3 10 ASN A 341 ? ASN A 341 . ? 1_555 ? 34 AC3 10 VAL A 342 ? VAL A 342 . ? 1_555 ? 35 AC3 10 MET A 446 ? MET A 446 . ? 1_555 ? 36 AC3 10 TRP A 452 ? TRP A 452 . ? 1_555 ? 37 AC3 10 HOH KA . ? HOH A 802 . ? 1_555 ? 38 AC4 4 ASN A 241 ? ASN A 241 . ? 1_555 ? 39 AC4 4 THR A 242 ? THR A 242 . ? 1_555 ? 40 AC4 4 THR A 243 ? THR A 243 . ? 1_555 ? 41 AC4 4 HOH KA . ? HOH A 858 . ? 1_555 ? 42 AC5 6 LEU A 92 ? LEU A 92 . ? 1_555 ? 43 AC5 6 LYS A 402 ? LYS A 402 . ? 1_555 ? 44 AC5 6 ASN A 403 ? ASN A 403 . ? 1_555 ? 45 AC5 6 HOH KA . ? HOH A 779 . ? 1_555 ? 46 AC5 6 HOH KA . ? HOH A 820 . ? 1_555 ? 47 AC5 6 HOH KA . ? HOH A 979 . ? 1_555 ? 48 AC6 6 ILE A 306 ? ILE A 306 . ? 1_555 ? 49 AC6 6 PHE A 309 ? PHE A 309 . ? 1_555 ? 50 AC6 6 ARG A 310 ? ARG A 310 . ? 1_555 ? 51 AC6 6 TRP A 529 ? TRP A 529 . ? 1_555 ? 52 AC6 6 TRP A 530 ? TRP A 530 . ? 1_555 ? 53 AC6 6 GLU A 531 ? GLU A 531 . ? 1_555 ? 54 AC7 3 ASN A 408 ? ASN A 408 . ? 1_555 ? 55 AC7 3 ASN A 410 ? ASN A 410 . ? 1_555 ? 56 AC7 3 LYS A 411 ? LYS A 411 . ? 1_555 ? 57 AC8 8 GLU A 52 ? GLU A 52 . ? 1_555 ? 58 AC8 8 PHE A 59 ? PHE A 59 . ? 1_555 ? 59 AC8 8 GLY A 60 ? GLY A 60 . ? 1_555 ? 60 AC8 8 TRP A 61 ? TRP A 61 . ? 1_555 ? 61 AC8 8 THR A 62 ? THR A 62 . ? 1_555 ? 62 AC8 8 LYS A 65 ? LYS A 65 . ? 1_555 ? 63 AC8 8 ARG A 71 ? ARG A 71 . ? 1_555 ? 64 AC8 8 VAL A 72 ? VAL A 72 . ? 1_555 ? 65 AC9 4 GLU A 52 ? GLU A 52 . ? 1_555 ? 66 AC9 4 LYS A 65 ? LYS A 65 . ? 1_555 ? 67 AC9 4 THR A 66 ? THR A 66 . ? 1_555 ? 68 AC9 4 HOH KA . ? HOH A 708 . ? 1_555 ? 69 AD1 5 ALA A 56 ? ALA A 56 . ? 1_555 ? 70 AD1 5 TRP A 61 ? TRP A 61 . ? 1_555 ? 71 AD1 5 ASP A 137 ? ASP A 137 . ? 1_555 ? 72 AD1 5 ARG A 162 ? ARG A 162 . ? 1_555 ? 73 AD1 5 HOH KA . ? HOH A 755 . ? 1_555 ? 74 AD2 9 GLU A 116 ? GLU A 116 . ? 1_555 ? 75 AD2 9 GLU A 118 ? GLU A 118 . ? 1_555 ? 76 AD2 9 PRO A 159 ? PRO A 159 . ? 1_555 ? 77 AD2 9 PHE A 160 ? PHE A 160 . ? 1_555 ? 78 AD2 9 PHE A 161 ? PHE A 161 . ? 1_555 ? 79 AD2 9 GLN A 423 ? GLN A 423 . ? 1_555 ? 80 AD2 9 HIS A 426 ? HIS A 426 . ? 1_555 ? 81 AD2 9 PHE A 431 ? PHE A 431 . ? 1_555 ? 82 AD2 9 ILE A 436 ? ILE A 436 . ? 1_555 ? 83 AD3 22 MET B 101 ? MET B 101 . ? 1_555 ? 84 AD3 22 GLY B 104 ? GLY B 104 . ? 1_555 ? 85 AD3 22 GLN B 105 ? GLN B 105 . ? 1_555 ? 86 AD3 22 ASP B 108 ? ASP B 108 . ? 1_555 ? 87 AD3 22 ASP B 112 ? ASP B 112 . ? 1_555 ? 88 AD3 22 PHE B 113 ? PHE B 113 . ? 1_555 ? 89 AD3 22 ALA B 114 ? ALA B 114 . ? 1_555 ? 90 AD3 22 ARG B 255 ? ARG B 255 . ? 1_555 ? 91 AD3 22 GLU B 258 ? GLU B 258 . ? 1_555 ? 92 AD3 22 GLN B 259 ? GLN B 259 . ? 1_555 ? 93 AD3 22 THR B 344 ? THR B 344 . ? 1_555 ? 94 AD3 22 PHE B 347 ? PHE B 347 . ? 1_555 ? 95 AD3 22 ARG B 348 ? ARG B 348 . ? 1_555 ? 96 AD3 22 GLY B 350 ? GLY B 350 . ? 1_555 ? 97 AD3 22 HIS B 351 ? HIS B 351 . ? 1_555 ? 98 AD3 22 LEU B 433 ? LEU B 433 . ? 1_555 ? 99 AD3 22 ILE B 436 ? ILE B 436 . ? 1_555 ? 100 AD3 22 ARG B 440 ? ARG B 440 . ? 1_555 ? 101 AD3 22 MMZ T . ? MMZ B 601 . ? 1_555 ? 102 AD3 22 MMZ FA . ? MMZ B 613 . ? 1_555 ? 103 AD3 22 HOH LA . ? HOH B 726 . ? 1_555 ? 104 AD3 22 HOH LA . ? HOH B 735 . ? 1_555 ? 105 AD4 5 ASP B 110 ? ASP B 110 . ? 1_555 ? 106 AD4 5 THR B 184 ? THR B 184 . ? 1_555 ? 107 AD4 5 PHE B 186 ? PHE B 186 . ? 1_555 ? 108 AD4 5 ASP B 188 ? ASP B 188 . ? 1_555 ? 109 AD4 5 SER B 190 ? SER B 190 . ? 1_555 ? 110 AD5 10 ALA B 44 ? ALA B 44 . ? 1_555 ? 111 AD5 10 ARG B 45 ? ARG B 45 . ? 1_555 ? 112 AD5 10 TRP B 46 ? TRP B 46 . ? 1_555 ? 113 AD5 10 LEU B 47 ? LEU B 47 . ? 1_555 ? 114 AD5 10 SER B 340 ? SER B 340 . ? 1_555 ? 115 AD5 10 ASN B 341 ? ASN B 341 . ? 1_555 ? 116 AD5 10 VAL B 342 ? VAL B 342 . ? 1_555 ? 117 AD5 10 MET B 446 ? MET B 446 . ? 1_555 ? 118 AD5 10 TRP B 452 ? TRP B 452 . ? 1_555 ? 119 AD5 10 HOH LA . ? HOH B 706 . ? 1_555 ? 120 AD6 6 ARG B 76 ? ARG B 76 . ? 1_555 ? 121 AD6 6 PRO B 149 ? PRO B 149 . ? 1_555 ? 122 AD6 6 LYS B 150 ? LYS B 150 . ? 1_555 ? 123 AD6 6 ASN B 419 ? ASN B 419 . ? 1_555 ? 124 AD6 6 HOH LA . ? HOH B 788 . ? 1_555 ? 125 AD6 6 HOH LA . ? HOH B 864 . ? 1_555 ? 126 AD7 5 ASP B 311 ? ASP B 311 . ? 1_555 ? 127 AD7 5 HIS B 565 ? HIS B 565 . ? 1_555 ? 128 AD7 5 ALA B 566 ? ALA B 566 . ? 1_555 ? 129 AD7 5 PHE B 567 ? PHE B 567 . ? 1_555 ? 130 AD7 5 HOH LA . ? HOH B 867 . ? 1_555 ? 131 AD8 5 LEU B 92 ? LEU B 92 . ? 1_555 ? 132 AD8 5 LYS B 402 ? LYS B 402 . ? 1_555 ? 133 AD8 5 ASN B 403 ? ASN B 403 . ? 1_555 ? 134 AD8 5 HOH LA . ? HOH B 709 . ? 1_555 ? 135 AD8 5 HOH LA . ? HOH B 785 . ? 1_555 ? 136 AD9 6 ALA B 56 ? ALA B 56 . ? 1_555 ? 137 AD9 6 VAL B 57 ? VAL B 57 . ? 1_555 ? 138 AD9 6 TRP B 61 ? TRP B 61 . ? 1_555 ? 139 AD9 6 ASP B 137 ? ASP B 137 . ? 1_555 ? 140 AD9 6 ARG B 162 ? ARG B 162 . ? 1_555 ? 141 AD9 6 HOH LA . ? HOH B 897 . ? 1_555 ? 142 AE1 9 GLU B 52 ? GLU B 52 . ? 1_555 ? 143 AE1 9 PHE B 59 ? PHE B 59 . ? 1_555 ? 144 AE1 9 GLY B 60 ? GLY B 60 . ? 1_555 ? 145 AE1 9 TRP B 61 ? TRP B 61 . ? 1_555 ? 146 AE1 9 THR B 62 ? THR B 62 . ? 1_555 ? 147 AE1 9 LYS B 65 ? LYS B 65 . ? 1_555 ? 148 AE1 9 THR B 66 ? THR B 66 . ? 1_555 ? 149 AE1 9 ARG B 71 ? ARG B 71 . ? 1_555 ? 150 AE1 9 VAL B 72 ? VAL B 72 . ? 1_555 ? 151 AE2 4 GLU B 52 ? GLU B 52 . ? 1_555 ? 152 AE2 4 PHE B 59 ? PHE B 59 . ? 1_555 ? 153 AE2 4 LYS B 65 ? LYS B 65 . ? 1_555 ? 154 AE2 4 THR B 66 ? THR B 66 . ? 1_555 ? 155 AE3 5 ASN B 532 ? ASN B 532 . ? 1_555 ? 156 AE3 5 PRO B 533 ? PRO B 533 . ? 1_555 ? 157 AE3 5 GLY B 534 ? GLY B 534 . ? 1_555 ? 158 AE3 5 HOH LA . ? HOH B 718 . ? 1_555 ? 159 AE3 5 HOH LA . ? HOH B 873 . ? 1_555 ? 160 AE4 2 ASN A 95 ? ASN A 95 . ? 1_555 ? 161 AE4 2 HOH KA . ? HOH A 707 . ? 1_555 ? 162 AE5 11 ASN A 205 ? ASN A 205 . ? 1_555 ? 163 AE5 11 SER A 208 ? SER A 208 . ? 1_555 ? 164 AE5 11 LEU A 210 ? LEU A 210 . ? 1_555 ? 165 AE5 11 ALA A 214 ? ALA A 214 . ? 1_555 ? 166 AE5 11 VAL A 215 ? VAL A 215 . ? 1_555 ? 167 AE5 11 GLN A 217 ? GLN A 217 . ? 1_555 ? 168 AE5 11 HOH KA . ? HOH A 706 . ? 1_555 ? 169 AE5 11 HOH KA . ? HOH A 732 . ? 1_555 ? 170 AE5 11 HOH KA . ? HOH A 735 . ? 1_555 ? 171 AE5 11 HOH KA . ? HOH A 801 . ? 1_555 ? 172 AE5 11 HOH KA . ? HOH A 991 . ? 1_555 ? 173 AE6 5 ASN A 241 ? ASN A 241 . ? 1_555 ? 174 AE6 5 ALA A 244 ? ALA A 244 . ? 1_555 ? 175 AE6 5 TRP A 384 ? TRP A 384 . ? 1_555 ? 176 AE6 5 HOH KA . ? HOH A 714 . ? 1_555 ? 177 AE6 5 HOH KA . ? HOH A 758 . ? 1_555 ? 178 AE7 3 ASN A 332 ? ASN A 332 . ? 1_555 ? 179 AE7 3 SER A 334 ? SER A 334 . ? 1_555 ? 180 AE7 3 HOH KA . ? HOH A 880 . ? 1_555 ? 181 AE8 2 ASN B 95 ? ASN B 95 . ? 1_555 ? 182 AE8 2 HOH LA . ? HOH B 702 . ? 1_555 ? 183 AE9 9 ASN B 205 ? ASN B 205 . ? 1_555 ? 184 AE9 9 SER B 208 ? SER B 208 . ? 1_555 ? 185 AE9 9 LEU B 210 ? LEU B 210 . ? 1_555 ? 186 AE9 9 ALA B 214 ? ALA B 214 . ? 1_555 ? 187 AE9 9 VAL B 215 ? VAL B 215 . ? 1_555 ? 188 AE9 9 GLN B 217 ? GLN B 217 . ? 1_555 ? 189 AE9 9 TRP B 220 ? TRP B 220 . ? 1_555 ? 190 AE9 9 HOH LA . ? HOH B 756 . ? 1_555 ? 191 AE9 9 HOH LA . ? HOH B 896 . ? 1_555 ? 192 AF1 5 ASN B 241 ? ASN B 241 . ? 1_555 ? 193 AF1 5 ALA B 244 ? ALA B 244 . ? 1_555 ? 194 AF1 5 TRP B 384 ? TRP B 384 . ? 1_555 ? 195 AF1 5 HOH LA . ? HOH B 710 . ? 1_555 ? 196 AF1 5 HOH LA . ? HOH B 947 . ? 1_555 ? 197 AF2 3 ASN B 332 ? ASN B 332 . ? 1_555 ? 198 AF2 3 SER B 334 ? SER B 334 . ? 1_555 ? 199 AF2 3 HOH LA . ? HOH B 795 . ? 1_555 ? 200 AF3 7 GLN A 105 ? GLN A 105 . ? 1_555 ? 201 AF3 7 HIS A 109 ? HIS A 109 . ? 1_555 ? 202 AF3 7 ARG A 255 ? ARG A 255 . ? 1_555 ? 203 AF3 7 GLU A 258 ? GLU A 258 . ? 1_555 ? 204 AF3 7 HEM I . ? HEM A 607 . ? 1_555 ? 205 AF3 7 HOH KA . ? HOH A 701 . ? 1_555 ? 206 AF3 7 HOH KA . ? HOH A 1084 . ? 1_555 ? 207 AF4 7 GLN A 105 ? GLN A 105 . ? 1_555 ? 208 AF4 7 HIS A 109 ? HIS A 109 . ? 1_555 ? 209 AF4 7 ARG A 255 ? ARG A 255 . ? 1_555 ? 210 AF4 7 GLU A 258 ? GLU A 258 . ? 1_555 ? 211 AF4 7 HEM I . ? HEM A 607 . ? 1_555 ? 212 AF4 7 HOH KA . ? HOH A 701 . ? 1_555 ? 213 AF4 7 HOH KA . ? HOH A 1084 . ? 1_555 ? 214 AF5 7 GLN A 105 ? GLN A 105 . ? 1_555 ? 215 AF5 7 HIS A 109 ? HIS A 109 . ? 1_555 ? 216 AF5 7 ARG A 255 ? ARG A 255 . ? 1_555 ? 217 AF5 7 GLU A 258 ? GLU A 258 . ? 1_555 ? 218 AF5 7 HEM I . ? HEM A 607 . ? 1_555 ? 219 AF5 7 HOH KA . ? HOH A 701 . ? 1_555 ? 220 AF5 7 HOH KA . ? HOH A 1084 . ? 1_555 ? 221 AF6 7 GLN A 105 ? GLN A 105 . ? 1_555 ? 222 AF6 7 HIS A 109 ? HIS A 109 . ? 1_555 ? 223 AF6 7 ARG A 255 ? ARG A 255 . ? 1_555 ? 224 AF6 7 GLU A 258 ? GLU A 258 . ? 1_555 ? 225 AF6 7 HEM I . ? HEM A 607 . ? 1_555 ? 226 AF6 7 HOH KA . ? HOH A 701 . ? 1_555 ? 227 AF6 7 HOH KA . ? HOH A 1084 . ? 1_555 ? 228 AF7 7 GLN A 105 ? GLN A 105 . ? 1_555 ? 229 AF7 7 HIS A 109 ? HIS A 109 . ? 1_555 ? 230 AF7 7 ARG A 255 ? ARG A 255 . ? 1_555 ? 231 AF7 7 GLU A 258 ? GLU A 258 . ? 1_555 ? 232 AF7 7 HEM I . ? HEM A 607 . ? 1_555 ? 233 AF7 7 HOH KA . ? HOH A 701 . ? 1_555 ? 234 AF7 7 HOH KA . ? HOH A 1084 . ? 1_555 ? 235 AF8 7 GLN A 105 ? GLN A 105 . ? 1_555 ? 236 AF8 7 HIS A 109 ? HIS A 109 . ? 1_555 ? 237 AF8 7 ARG A 255 ? ARG A 255 . ? 1_555 ? 238 AF8 7 GLU A 258 ? GLU A 258 . ? 1_555 ? 239 AF8 7 HEM I . ? HEM A 607 . ? 1_555 ? 240 AF8 7 HOH KA . ? HOH A 701 . ? 1_555 ? 241 AF8 7 HOH KA . ? HOH A 1084 . ? 1_555 ? 242 AF9 7 GLN A 105 ? GLN A 105 . ? 1_555 ? 243 AF9 7 HIS A 109 ? HIS A 109 . ? 1_555 ? 244 AF9 7 ARG A 255 ? ARG A 255 . ? 1_555 ? 245 AF9 7 GLU A 258 ? GLU A 258 . ? 1_555 ? 246 AF9 7 HEM I . ? HEM A 607 . ? 1_555 ? 247 AF9 7 HOH KA . ? HOH A 701 . ? 1_555 ? 248 AF9 7 HOH KA . ? HOH A 1084 . ? 1_555 ? 249 AG1 7 GLN A 105 ? GLN A 105 . ? 1_555 ? 250 AG1 7 HIS A 109 ? HIS A 109 . ? 1_555 ? 251 AG1 7 ARG A 255 ? ARG A 255 . ? 1_555 ? 252 AG1 7 GLU A 258 ? GLU A 258 . ? 1_555 ? 253 AG1 7 HEM I . ? HEM A 607 . ? 1_555 ? 254 AG1 7 HOH KA . ? HOH A 701 . ? 1_555 ? 255 AG1 7 HOH KA . ? HOH A 1084 . ? 1_555 ? 256 AG2 7 GLN A 105 ? GLN A 105 . ? 1_555 ? 257 AG2 7 HIS A 109 ? HIS A 109 . ? 1_555 ? 258 AG2 7 ARG A 255 ? ARG A 255 . ? 1_555 ? 259 AG2 7 GLU A 258 ? GLU A 258 . ? 1_555 ? 260 AG2 7 HEM I . ? HEM A 607 . ? 1_555 ? 261 AG2 7 HOH KA . ? HOH A 701 . ? 1_555 ? 262 AG2 7 HOH KA . ? HOH A 1084 . ? 1_555 ? 263 AG3 7 GLN A 105 ? GLN A 105 . ? 1_555 ? 264 AG3 7 HIS A 109 ? HIS A 109 . ? 1_555 ? 265 AG3 7 ARG A 255 ? ARG A 255 . ? 1_555 ? 266 AG3 7 GLU A 258 ? GLU A 258 . ? 1_555 ? 267 AG3 7 HEM I . ? HEM A 607 . ? 1_555 ? 268 AG3 7 HOH KA . ? HOH A 701 . ? 1_555 ? 269 AG3 7 HOH KA . ? HOH A 1084 . ? 1_555 ? 270 AG4 8 GLN B 105 ? GLN B 105 . ? 1_555 ? 271 AG4 8 HIS B 109 ? HIS B 109 . ? 1_555 ? 272 AG4 8 ARG B 255 ? ARG B 255 . ? 1_555 ? 273 AG4 8 GLU B 258 ? GLU B 258 . ? 1_555 ? 274 AG4 8 HEM Z . ? HEM B 607 . ? 1_555 ? 275 AG4 8 HOH LA . ? HOH B 701 . ? 1_555 ? 276 AG4 8 HOH LA . ? HOH B 1033 . ? 1_555 ? 277 AG4 8 HOH LA . ? HOH B 1042 . ? 1_555 ? 278 AG5 8 GLN B 105 ? GLN B 105 . ? 1_555 ? 279 AG5 8 HIS B 109 ? HIS B 109 . ? 1_555 ? 280 AG5 8 ARG B 255 ? ARG B 255 . ? 1_555 ? 281 AG5 8 GLU B 258 ? GLU B 258 . ? 1_555 ? 282 AG5 8 HEM Z . ? HEM B 607 . ? 1_555 ? 283 AG5 8 HOH LA . ? HOH B 701 . ? 1_555 ? 284 AG5 8 HOH LA . ? HOH B 1033 . ? 1_555 ? 285 AG5 8 HOH LA . ? HOH B 1042 . ? 1_555 ? 286 AG6 8 GLN B 105 ? GLN B 105 . ? 1_555 ? 287 AG6 8 HIS B 109 ? HIS B 109 . ? 1_555 ? 288 AG6 8 ARG B 255 ? ARG B 255 . ? 1_555 ? 289 AG6 8 GLU B 258 ? GLU B 258 . ? 1_555 ? 290 AG6 8 HEM Z . ? HEM B 607 . ? 1_555 ? 291 AG6 8 HOH LA . ? HOH B 701 . ? 1_555 ? 292 AG6 8 HOH LA . ? HOH B 1033 . ? 1_555 ? 293 AG6 8 HOH LA . ? HOH B 1042 . ? 1_555 ? 294 AG7 8 GLN B 105 ? GLN B 105 . ? 1_555 ? 295 AG7 8 HIS B 109 ? HIS B 109 . ? 1_555 ? 296 AG7 8 ARG B 255 ? ARG B 255 . ? 1_555 ? 297 AG7 8 GLU B 258 ? GLU B 258 . ? 1_555 ? 298 AG7 8 HEM Z . ? HEM B 607 . ? 1_555 ? 299 AG7 8 HOH LA . ? HOH B 701 . ? 1_555 ? 300 AG7 8 HOH LA . ? HOH B 1033 . ? 1_555 ? 301 AG7 8 HOH LA . ? HOH B 1042 . ? 1_555 ? 302 AG8 8 GLN B 105 ? GLN B 105 . ? 1_555 ? 303 AG8 8 HIS B 109 ? HIS B 109 . ? 1_555 ? 304 AG8 8 ARG B 255 ? ARG B 255 . ? 1_555 ? 305 AG8 8 GLU B 258 ? GLU B 258 . ? 1_555 ? 306 AG8 8 HEM Z . ? HEM B 607 . ? 1_555 ? 307 AG8 8 HOH LA . ? HOH B 701 . ? 1_555 ? 308 AG8 8 HOH LA . ? HOH B 1033 . ? 1_555 ? 309 AG8 8 HOH LA . ? HOH B 1042 . ? 1_555 ? 310 AG9 8 GLN B 105 ? GLN B 105 . ? 1_555 ? 311 AG9 8 HIS B 109 ? HIS B 109 . ? 1_555 ? 312 AG9 8 ARG B 255 ? ARG B 255 . ? 1_555 ? 313 AG9 8 GLU B 258 ? GLU B 258 . ? 1_555 ? 314 AG9 8 HEM Z . ? HEM B 607 . ? 1_555 ? 315 AG9 8 HOH LA . ? HOH B 701 . ? 1_555 ? 316 AG9 8 HOH LA . ? HOH B 1033 . ? 1_555 ? 317 AG9 8 HOH LA . ? HOH B 1042 . ? 1_555 ? 318 AH1 8 GLN B 105 ? GLN B 105 . ? 1_555 ? 319 AH1 8 HIS B 109 ? HIS B 109 . ? 1_555 ? 320 AH1 8 ARG B 255 ? ARG B 255 . ? 1_555 ? 321 AH1 8 GLU B 258 ? GLU B 258 . ? 1_555 ? 322 AH1 8 HEM Z . ? HEM B 607 . ? 1_555 ? 323 AH1 8 HOH LA . ? HOH B 701 . ? 1_555 ? 324 AH1 8 HOH LA . ? HOH B 1033 . ? 1_555 ? 325 AH1 8 HOH LA . ? HOH B 1042 . ? 1_555 ? 326 AH2 8 GLN B 105 ? GLN B 105 . ? 1_555 ? 327 AH2 8 HIS B 109 ? HIS B 109 . ? 1_555 ? 328 AH2 8 ARG B 255 ? ARG B 255 . ? 1_555 ? 329 AH2 8 GLU B 258 ? GLU B 258 . ? 1_555 ? 330 AH2 8 HEM Z . ? HEM B 607 . ? 1_555 ? 331 AH2 8 HOH LA . ? HOH B 701 . ? 1_555 ? 332 AH2 8 HOH LA . ? HOH B 1033 . ? 1_555 ? 333 AH2 8 HOH LA . ? HOH B 1042 . ? 1_555 ? # _atom_sites.entry_id 5FF1 _atom_sites.fract_transf_matrix[1][1] 0.012452 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] -0.000007 _atom_sites.fract_transf_matrix[2][1] -0.000000 _atom_sites.fract_transf_matrix[2][2] 0.010750 _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] 0.012265 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C CA FE 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 . SER A 1 1 ? -12.172 18.854 9.516 1.00 99.63 ? 1 SER A N 1 ATOM 2 C CA . SER A 1 1 ? -11.497 19.614 10.602 1.00 102.81 ? 1 SER A CA 1 ATOM 3 C C . SER A 1 1 ? -12.498 20.426 11.422 1.00 115.20 ? 1 SER A C 1 ATOM 4 O O . SER A 1 1 ? -13.198 21.287 10.884 1.00 121.52 ? 1 SER A O 1 ATOM 5 C CB . SER A 1 1 ? -10.438 20.565 10.027 1.00 96.61 ? 1 SER A CB 1 ATOM 6 O OG . SER A 1 1 ? -9.399 19.858 9.389 1.00 94.82 ? 1 SER A OG 1 ATOM 7 N N . TRP A 1 2 ? -12.585 20.119 12.715 1.00 124.30 ? 2 TRP A N 1 ATOM 8 C CA . TRP A 1 2 ? -13.073 21.076 13.710 1.00 127.59 ? 2 TRP A CA 1 ATOM 9 C C . TRP A 1 2 ? -11.805 21.602 14.424 1.00 127.02 ? 2 TRP A C 1 ATOM 10 O O . TRP A 1 2 ? -10.695 21.342 13.954 1.00 124.31 ? 2 TRP A O 1 ATOM 11 C CB . TRP A 1 2 ? -14.108 20.434 14.646 1.00 130.10 ? 2 TRP A CB 1 ATOM 12 C CG . TRP A 1 2 ? -15.444 20.092 13.980 1.00 138.66 ? 2 TRP A CG 1 ATOM 13 C CD1 . TRP A 1 2 ? -15.884 18.844 13.615 1.00 137.53 ? 2 TRP A CD1 1 ATOM 14 C CD2 . TRP A 1 2 ? -16.501 21.009 13.617 1.00 143.48 ? 2 TRP A CD2 1 ATOM 15 N NE1 . TRP A 1 2 ? -17.138 18.930 13.047 1.00 142.43 ? 2 TRP A NE1 1 ATOM 16 C CE2 . TRP A 1 2 ? -17.540 20.242 13.035 1.00 142.44 ? 2 TRP A CE2 1 ATOM 17 C CE3 . TRP A 1 2 ? -16.667 22.400 13.724 1.00 137.70 ? 2 TRP A CE3 1 ATOM 18 C CZ2 . TRP A 1 2 ? -18.732 20.822 12.563 1.00 136.03 ? 2 TRP A CZ2 1 ATOM 19 C CZ3 . TRP A 1 2 ? -17.852 22.973 13.254 1.00 135.44 ? 2 TRP A CZ3 1 ATOM 20 C CH2 . TRP A 1 2 ? -18.867 22.182 12.681 1.00 131.91 ? 2 TRP A CH2 1 ATOM 21 N N . GLU A 1 3 ? -11.941 22.337 15.533 1.00 131.19 ? 3 GLU A N 1 ATOM 22 C CA . GLU A 1 3 ? -10.838 23.203 16.021 1.00 124.04 ? 3 GLU A CA 1 ATOM 23 C C . GLU A 1 3 ? -10.504 23.127 17.544 1.00 121.88 ? 3 GLU A C 1 ATOM 24 O O . GLU A 1 3 ? -10.360 24.153 18.223 1.00 128.91 ? 3 GLU A O 1 ATOM 25 C CB . GLU A 1 3 ? -11.110 24.659 15.568 1.00 118.28 ? 3 GLU A CB 1 ATOM 26 C CG . GLU A 1 3 ? -11.362 24.804 14.065 1.00 116.69 ? 3 GLU A CG 1 ATOM 27 C CD . GLU A 1 3 ? -11.919 26.157 13.652 1.00 113.56 ? 3 GLU A CD 1 ATOM 28 O OE1 . GLU A 1 3 ? -11.143 27.130 13.641 1.00 114.36 ? 3 GLU A OE1 1 ATOM 29 O OE2 . GLU A 1 3 ? -13.123 26.246 13.309 1.00 99.98 ? 3 GLU A OE2 1 ATOM 30 N N . VAL A 1 4 ? -10.352 21.907 18.064 1.00 116.36 ? 4 VAL A N 1 ATOM 31 C CA . VAL A 1 4 ? -9.774 21.692 19.414 1.00 112.51 ? 4 VAL A CA 1 ATOM 32 C C . VAL A 1 4 ? -8.243 21.552 19.312 1.00 119.41 ? 4 VAL A C 1 ATOM 33 O O . VAL A 1 4 ? -7.746 20.629 18.664 1.00 128.75 ? 4 VAL A O 1 ATOM 34 C CB . VAL A 1 4 ? -10.406 20.453 20.132 1.00 103.85 ? 4 VAL A CB 1 ATOM 35 C CG1 . VAL A 1 4 ? -9.442 19.773 21.113 1.00 96.04 ? 4 VAL A CG1 1 ATOM 36 C CG2 . VAL A 1 4 ? -11.694 20.855 20.845 1.00 98.82 ? 4 VAL A CG2 1 ATOM 37 N N . GLY A 1 5 ? -7.497 22.468 19.938 1.00 121.73 ? 5 GLY A N 1 ATOM 38 C CA . GLY A 1 5 ? -6.035 22.332 20.046 1.00 115.11 ? 5 GLY A CA 1 ATOM 39 C C . GLY A 1 5 ? -5.617 20.944 20.536 1.00 111.46 ? 5 GLY A C 1 ATOM 40 O O . GLY A 1 5 ? -6.160 20.429 21.519 1.00 107.64 ? 5 GLY A O 1 ATOM 41 N N . CYS A 1 6 ? -4.667 20.333 19.824 1.00 109.61 ? 6 CYS A N 1 ATOM 42 C CA . CYS A 1 6 ? -4.129 18.986 20.138 1.00 101.17 ? 6 CYS A CA 1 ATOM 43 C C . CYS A 1 6 ? -2.877 19.015 21.022 1.00 112.13 ? 6 CYS A C 1 ATOM 44 O O . CYS A 1 6 ? -2.310 20.078 21.281 1.00 121.21 ? 6 CYS A O 1 ATOM 45 C CB . CYS A 1 6 ? -3.766 18.258 18.834 1.00 87.76 ? 6 CYS A CB 1 ATOM 46 S SG . CYS A 1 6 ? -3.471 19.358 17.431 1.00 73.12 ? 6 CYS A SG 1 ATOM 47 N N . GLY A 1 7 ? -2.437 17.840 21.470 1.00 110.63 ? 7 GLY A N 1 ATOM 48 C CA . GLY A 1 7 ? -1.103 17.714 22.064 1.00 116.00 ? 7 GLY A CA 1 ATOM 49 C C . GLY A 1 7 ? -0.056 18.025 21.000 1.00 121.35 ? 7 GLY A C 1 ATOM 50 O O . GLY A 1 7 ? -0.174 17.546 19.879 1.00 118.93 ? 7 GLY A O 1 ATOM 51 N N . ALA A 1 8 ? 0.962 18.826 21.333 1.00 132.82 ? 8 ALA A N 1 ATOM 52 C CA . ALA A 1 8 ? 1.933 19.321 20.328 1.00 136.34 ? 8 ALA A CA 1 ATOM 53 C C . ALA A 1 8 ? 3.359 19.581 20.878 1.00 138.59 ? 8 ALA A C 1 ATOM 54 O O . ALA A 1 8 ? 3.576 20.576 21.567 1.00 139.93 ? 8 ALA A O 1 ATOM 55 C CB . ALA A 1 8 ? 1.393 20.590 19.670 1.00 130.59 ? 8 ALA A CB 1 ATOM 56 N N . PRO A 1 9 ? 4.329 18.685 20.573 1.00 138.91 ? 9 PRO A N 1 ATOM 57 C CA . PRO A 1 9 ? 5.781 18.874 20.848 1.00 141.09 ? 9 PRO A CA 1 ATOM 58 C C . PRO A 1 9 ? 6.567 19.658 19.753 1.00 142.33 ? 9 PRO A C 1 ATOM 59 O O . PRO A 1 9 ? 5.981 20.507 19.090 1.00 145.99 ? 9 PRO A O 1 ATOM 60 C CB . PRO A 1 9 ? 6.304 17.432 20.970 1.00 134.82 ? 9 PRO A CB 1 ATOM 61 C CG . PRO A 1 9 ? 5.097 16.546 21.023 1.00 130.11 ? 9 PRO A CG 1 ATOM 62 C CD . PRO A 1 9 ? 4.023 17.272 20.282 1.00 128.75 ? 9 PRO A CD 1 ATOM 63 N N . VAL A 1 10 ? 7.826 19.438 19.575 1.00 148.06 ? 10 VAL A N 1 ATOM 64 C CA . VAL A 1 10 ? 8.700 20.139 18.578 1.00 141.79 ? 10 VAL A CA 1 ATOM 65 C C . VAL A 1 10 ? 9.798 19.200 17.971 1.00 138.90 ? 10 VAL A C 1 ATOM 66 O O . VAL A 1 10 ? 10.822 18.990 18.610 1.00 139.49 ? 10 VAL A O 1 ATOM 67 C CB . VAL A 1 10 ? 9.395 21.413 19.169 1.00 132.49 ? 10 VAL A CB 1 ATOM 68 C CG1 . VAL A 1 10 ? 8.571 22.678 18.941 1.00 129.97 ? 10 VAL A CG1 1 ATOM 69 C CG2 . VAL A 1 10 ? 9.710 21.248 20.641 1.00 126.48 ? 10 VAL A CG2 1 ATOM 70 N N . PRO A 1 11 ? 9.572 18.635 16.746 1.00 131.70 ? 11 PRO A N 1 ATOM 71 C CA . PRO A 1 11 ? 10.492 17.647 16.050 1.00 129.54 ? 11 PRO A CA 1 ATOM 72 C C . PRO A 1 11 ? 11.928 17.972 15.398 1.00 122.26 ? 11 PRO A C 1 ATOM 73 O O . PRO A 1 11 ? 12.832 18.333 16.143 1.00 124.81 ? 11 PRO A O 1 ATOM 74 C CB . PRO A 1 11 ? 9.552 17.002 15.022 1.00 127.50 ? 11 PRO A CB 1 ATOM 75 C CG . PRO A 1 11 ? 8.178 17.148 15.591 1.00 121.67 ? 11 PRO A CG 1 ATOM 76 C CD . PRO A 1 11 ? 8.190 18.515 16.217 1.00 126.20 ? 11 PRO A CD 1 ATOM 77 N N . LEU A 1 12 ? 12.133 17.825 14.074 1.00 122.64 ? 12 LEU A N 1 ATOM 78 C CA . LEU A 1 12 ? 13.454 17.326 13.444 1.00 127.50 ? 12 LEU A CA 1 ATOM 79 C C . LEU A 1 12 ? 14.826 18.092 13.638 1.00 137.19 ? 12 LEU A C 1 ATOM 80 O O . LEU A 1 12 ? 14.864 19.222 14.132 1.00 150.83 ? 12 LEU A O 1 ATOM 81 C CB . LEU A 1 12 ? 13.236 16.994 11.925 1.00 113.33 ? 12 LEU A CB 1 ATOM 82 C CG . LEU A 1 12 ? 14.088 15.943 11.154 1.00 100.79 ? 12 LEU A CG 1 ATOM 83 C CD1 . LEU A 1 12 ? 14.614 14.783 12.003 1.00 93.35 ? 12 LEU A CD1 1 ATOM 84 C CD2 . LEU A 1 12 ? 13.322 15.394 9.949 1.00 91.26 ? 12 LEU A CD2 1 ATOM 85 N N . VAL A 1 13 ? 15.936 17.438 13.234 1.00 131.49 ? 13 VAL A N 1 ATOM 86 C CA . VAL A 1 13 ? 17.337 17.842 13.545 1.00 127.44 ? 13 VAL A CA 1 ATOM 87 C C . VAL A 1 13 ? 18.284 17.761 12.315 1.00 122.51 ? 13 VAL A C 1 ATOM 88 O O . VAL A 1 13 ? 18.008 17.012 11.372 1.00 111.79 ? 13 VAL A O 1 ATOM 89 C CB . VAL A 1 13 ? 17.918 16.934 14.666 1.00 122.81 ? 13 VAL A CB 1 ATOM 90 C CG1 . VAL A 1 13 ? 19.417 17.143 14.875 1.00 118.72 ? 13 VAL A CG1 1 ATOM 91 C CG2 . VAL A 1 13 ? 17.172 17.154 15.977 1.00 119.55 ? 13 VAL A CG2 1 ATOM 92 N N . THR A 1 14 ? 19.399 18.517 12.363 1.00 116.08 ? 14 THR A N 1 ATOM 93 C CA . THR A 1 14 ? 20.505 18.499 11.355 1.00 105.29 ? 14 THR A CA 1 ATOM 94 C C . THR A 1 14 ? 21.699 17.631 11.856 1.00 99.37 ? 14 THR A C 1 ATOM 95 O O . THR A 1 14 ? 22.093 17.770 13.015 1.00 110.46 ? 14 THR A O 1 ATOM 96 C CB . THR A 1 14 ? 20.970 19.958 11.031 1.00 100.32 ? 14 THR A CB 1 ATOM 97 O OG1 . THR A 1 14 ? 21.753 19.978 9.837 1.00 99.26 ? 14 THR A OG1 1 ATOM 98 C CG2 . THR A 1 14 ? 21.786 20.604 12.176 1.00 94.50 ? 14 THR A CG2 1 ATOM 99 N N . CYS A 1 15 ? 22.270 16.756 11.007 1.00 79.55 ? 15 CYS A N 1 ATOM 100 C CA . CYS A 1 15 ? 23.014 15.561 11.498 1.00 69.97 ? 15 CYS A CA 1 ATOM 101 C C . CYS A 1 15 ? 24.536 15.550 11.503 1.00 73.24 ? 15 CYS A C 1 ATOM 102 O O . CYS A 1 15 ? 25.149 15.372 10.455 1.00 71.53 ? 15 CYS A O 1 ATOM 103 C CB . CYS A 1 15 ? 22.578 14.319 10.717 1.00 61.33 ? 15 CYS A CB 1 ATOM 104 S SG . CYS A 1 15 ? 20.884 13.789 11.037 1.00 55.19 ? 15 CYS A SG 1 ATOM 105 N N . ASP A 1 16 ? 25.126 15.644 12.701 1.00 74.25 ? 16 ASP A N 1 ATOM 106 C CA . ASP A 1 16 ? 26.555 15.360 12.931 1.00 73.41 ? 16 ASP A CA 1 ATOM 107 C C . ASP A 1 16 ? 26.998 14.110 12.210 1.00 74.71 ? 16 ASP A C 1 ATOM 108 O O . ASP A 1 16 ? 26.253 13.140 12.128 1.00 78.61 ? 16 ASP A O 1 ATOM 109 C CB . ASP A 1 16 ? 26.826 15.158 14.414 1.00 76.31 ? 16 ASP A CB 1 ATOM 110 C CG . ASP A 1 16 ? 28.222 15.592 14.828 1.00 76.21 ? 16 ASP A CG 1 ATOM 111 O OD1 . ASP A 1 16 ? 29.177 15.197 14.146 1.00 75.87 ? 16 ASP A OD1 1 ATOM 112 O OD2 . ASP A 1 16 ? 28.367 16.305 15.850 1.00 74.46 ? 16 ASP A OD2 1 ATOM 113 N N . GLU A 1 17 ? 28.213 14.129 11.680 1.00 75.26 ? 17 GLU A N 1 ATOM 114 C CA . GLU A 1 17 ? 28.674 13.022 10.868 1.00 71.03 ? 17 GLU A CA 1 ATOM 115 C C . GLU A 1 17 ? 29.213 11.863 11.674 1.00 72.69 ? 17 GLU A C 1 ATOM 116 O O . GLU A 1 17 ? 28.524 10.862 11.848 1.00 81.22 ? 17 GLU A O 1 ATOM 117 C CB . GLU A 1 17 ? 29.691 13.474 9.799 1.00 67.50 ? 17 GLU A CB 1 ATOM 118 C CG . GLU A 1 17 ? 30.018 12.399 8.760 1.00 65.75 ? 17 GLU A CG 1 ATOM 119 C CD . GLU A 1 17 ? 28.845 12.068 7.839 1.00 63.52 ? 17 GLU A CD 1 ATOM 120 O OE1 . GLU A 1 17 ? 28.581 10.866 7.602 1.00 58.38 ? 17 GLU A OE1 1 ATOM 121 O OE2 . GLU A 1 17 ? 28.182 13.016 7.353 1.00 59.90 ? 17 GLU A OE2 1 ATOM 122 N N . GLN A 1 18 ? 30.444 11.983 12.157 1.00 72.95 ? 18 GLN A N 1 ATOM 123 C CA . GLN A 1 18 ? 31.067 10.892 12.903 1.00 74.57 ? 18 GLN A CA 1 ATOM 124 C C . GLN A 1 18 ? 30.832 11.069 14.378 1.00 69.94 ? 18 GLN A C 1 ATOM 125 O O . GLN A 1 18 ? 31.594 10.497 15.150 1.00 73.88 ? 18 GLN A O 1 ATOM 126 C CB . GLN A 1 18 ? 32.588 10.800 12.686 1.00 74.54 ? 18 GLN A CB 1 ATOM 127 C CG . GLN A 1 18 ? 33.054 10.600 11.259 1.00 71.56 ? 18 GLN A CG 1 ATOM 128 C CD . GLN A 1 18 ? 33.812 11.816 10.792 1.00 72.14 ? 18 GLN A CD 1 ATOM 129 O OE1 . GLN A 1 18 ? 33.214 12.868 10.610 1.00 62.46 ? 18 GLN A OE1 1 ATOM 130 N NE2 . GLN A 1 18 ? 35.135 11.691 10.623 1.00 74.96 ? 18 GLN A NE2 1 ATOM 131 N N . SER A 1 19 ? 29.815 11.827 14.798 1.00 61.47 ? 19 SER A N 1 ATOM 132 C CA . SER A 1 19 ? 29.537 11.860 16.238 1.00 61.28 ? 19 SER A CA 1 ATOM 133 C C . SER A 1 19 ? 29.441 10.424 16.697 1.00 50.81 ? 19 SER A C 1 ATOM 134 O O . SER A 1 19 ? 28.693 9.621 16.146 1.00 51.84 ? 19 SER A O 1 ATOM 135 C CB . SER A 1 19 ? 28.266 12.583 16.627 1.00 62.93 ? 19 SER A CB 1 ATOM 136 O OG . SER A 1 19 ? 28.019 12.350 18.014 1.00 70.97 ? 19 SER A OG 1 ATOM 137 N N . PRO A 1 20 ? 30.267 10.079 17.659 1.00 43.23 ? 20 PRO A N 1 ATOM 138 C CA . PRO A 1 20 ? 30.256 8.740 18.186 1.00 40.60 ? 20 PRO A CA 1 ATOM 139 C C . PRO A 1 20 ? 29.163 8.582 19.291 1.00 37.74 ? 20 PRO A C 1 ATOM 140 O O . PRO A 1 20 ? 29.074 7.526 19.920 1.00 36.24 ? 20 PRO A O 1 ATOM 141 C CB . PRO A 1 20 ? 31.640 8.648 18.800 1.00 42.19 ? 20 PRO A CB 1 ATOM 142 C CG . PRO A 1 20 ? 31.863 10.032 19.344 1.00 41.42 ? 20 PRO A CG 1 ATOM 143 C CD . PRO A 1 20 ? 31.204 10.965 18.380 1.00 41.64 ? 20 PRO A CD 1 ATOM 144 N N . TYR A 1 21 ? 28.360 9.610 19.508 1.00 34.03 ? 21 TYR A N 1 ATOM 145 C CA . TYR A 1 21 ? 27.350 9.617 20.571 1.00 33.69 ? 21 TYR A CA 1 ATOM 146 C C . TYR A 1 21 ? 25.946 9.851 20.059 1.00 35.32 ? 21 TYR A C 1 ATOM 147 O O . TYR A 1 21 ? 25.752 10.586 19.137 1.00 38.28 ? 21 TYR A O 1 ATOM 148 C CB . TYR A 1 21 ? 27.656 10.690 21.610 1.00 31.60 ? 21 TYR A CB 1 ATOM 149 C CG . TYR A 1 21 ? 29.050 10.636 22.148 1.00 32.32 ? 21 TYR A CG 1 ATOM 150 C CD1 . TYR A 1 21 ? 29.548 9.488 22.655 1.00 30.70 ? 21 TYR A CD1 1 ATOM 151 C CD2 . TYR A 1 21 ? 29.879 11.725 22.094 1.00 33.21 ? 21 TYR A CD2 1 ATOM 152 C CE1 . TYR A 1 21 ? 30.813 9.407 23.118 1.00 33.40 ? 21 TYR A CE1 1 ATOM 153 C CE2 . TYR A 1 21 ? 31.160 11.648 22.557 1.00 33.56 ? 21 TYR A CE2 1 ATOM 154 C CZ . TYR A 1 21 ? 31.627 10.469 23.052 1.00 34.42 ? 21 TYR A CZ 1 ATOM 155 O OH . TYR A 1 21 ? 32.883 10.334 23.549 1.00 32.78 ? 21 TYR A OH 1 ATOM 156 N N . ARG A 1 22 ? 24.957 9.263 20.714 1.00 31.96 ? 22 ARG A N 1 ATOM 157 C CA . ARG A 1 22 ? 23.559 9.555 20.406 1.00 25.07 ? 22 ARG A CA 1 ATOM 158 C C . ARG A 1 22 ? 23.174 10.998 20.662 1.00 24.22 ? 22 ARG A C 1 ATOM 159 O O . ARG A 1 22 ? 23.667 11.603 21.572 1.00 25.19 ? 22 ARG A O 1 ATOM 160 C CB . ARG A 1 22 ? 22.684 8.753 21.316 1.00 23.30 ? 22 ARG A CB 1 ATOM 161 C CG . ARG A 1 22 ? 22.894 7.260 21.247 1.00 21.96 ? 22 ARG A CG 1 ATOM 162 C CD . ARG A 1 22 ? 21.942 6.621 22.242 1.00 19.52 ? 22 ARG A CD 1 ATOM 163 N NE . ARG A 1 22 ? 22.054 5.189 22.291 1.00 18.23 ? 22 ARG A NE 1 ATOM 164 C CZ . ARG A 1 22 ? 21.447 4.353 21.494 1.00 18.53 ? 22 ARG A CZ 1 ATOM 165 N NH1 . ARG A 1 22 ? 20.634 4.772 20.525 1.00 22.05 ? 22 ARG A NH1 1 ATOM 166 N NH2 . ARG A 1 22 ? 21.631 3.055 21.668 1.00 19.54 ? 22 ARG A NH2 1 ATOM 167 N N . THR A 1 23 ? 22.245 11.525 19.880 1.00 20.95 ? 23 THR A N 1 ATOM 168 C CA . THR A 1 23 ? 21.560 12.730 20.251 1.00 22.81 ? 23 THR A CA 1 ATOM 169 C C . THR A 1 23 ? 20.634 12.363 21.453 1.00 24.45 ? 23 THR A C 1 ATOM 170 O O . THR A 1 23 ? 20.394 11.168 21.738 1.00 20.03 ? 23 THR A O 1 ATOM 171 C CB . THR A 1 23 ? 20.691 13.244 19.092 1.00 24.32 ? 23 THR A CB 1 ATOM 172 O OG1 . THR A 1 23 ? 19.734 12.234 18.733 1.00 23.97 ? 23 THR A OG1 1 ATOM 173 C CG2 . THR A 1 23 ? 21.566 13.566 17.835 1.00 25.48 ? 23 THR A CG2 1 ATOM 174 N N . ILE A 1 24 ? 20.166 13.392 22.144 1.00 25.48 ? 24 ILE A N 1 ATOM 175 C CA . ILE A 1 24 ? 19.212 13.230 23.260 1.00 25.99 ? 24 ILE A CA 1 ATOM 176 C C . ILE A 1 24 ? 17.842 12.777 22.764 1.00 24.13 ? 24 ILE A C 1 ATOM 177 O O . ILE A 1 24 ? 17.256 11.846 23.331 1.00 25.37 ? 24 ILE A O 1 ATOM 178 C CB . ILE A 1 24 ? 19.139 14.484 24.125 1.00 25.74 ? 24 ILE A CB 1 ATOM 179 C CG1 . ILE A 1 24 ? 20.321 14.474 25.127 1.00 29.45 ? 24 ILE A CG1 1 ATOM 180 C CG2 . ILE A 1 24 ? 17.822 14.552 24.926 1.00 27.18 ? 24 ILE A CG2 1 ATOM 181 C CD1 . ILE A 1 24 ? 20.379 13.294 26.093 1.00 31.18 ? 24 ILE A CD1 1 ATOM 182 N N . THR A 1 25 ? 17.379 13.413 21.694 1.00 23.61 ? 25 THR A N 1 ATOM 183 C CA . THR A 1 25 ? 16.012 13.219 21.124 1.00 23.59 ? 25 THR A CA 1 ATOM 184 C C . THR A 1 25 ? 15.902 11.976 20.262 1.00 24.18 ? 25 THR A C 1 ATOM 185 O O . THR A 1 25 ? 14.818 11.641 19.802 1.00 26.21 ? 25 THR A O 1 ATOM 186 C CB . THR A 1 25 ? 15.643 14.346 20.144 1.00 22.74 ? 25 THR A CB 1 ATOM 187 O OG1 . THR A 1 25 ? 16.564 14.282 19.051 1.00 25.54 ? 25 THR A OG1 1 ATOM 188 C CG2 . THR A 1 25 ? 15.736 15.656 20.785 1.00 23.13 ? 25 THR A CG2 1 ATOM 189 N N . GLY A 1 26 ? 17.023 11.350 19.959 1.00 22.89 ? 26 GLY A N 1 ATOM 190 C CA . GLY A 1 26 ? 17.054 10.202 19.090 1.00 22.31 ? 26 GLY A CA 1 ATOM 191 C C . GLY A 1 26 ? 17.166 10.478 17.598 1.00 24.87 ? 26 GLY A C 1 ATOM 192 O O . GLY A 1 26 ? 17.374 9.546 16.799 1.00 24.82 ? 26 GLY A O 1 ATOM 193 N N . ASP A 1 27 ? 17.076 11.742 17.213 1.00 26.15 ? 27 ASP A N 1 ATOM 194 C CA . ASP A 1 27 ? 17.259 12.129 15.805 1.00 27.01 ? 27 ASP A CA 1 ATOM 195 C C . ASP A 1 27 ? 18.637 11.749 15.283 1.00 27.21 ? 27 ASP A C 1 ATOM 196 O O . ASP A 1 27 ? 19.575 11.568 16.043 1.00 27.71 ? 27 ASP A O 1 ATOM 197 C CB . ASP A 1 27 ? 17.039 13.657 15.612 1.00 26.66 ? 27 ASP A CB 1 ATOM 198 C CG . ASP A 1 27 ? 15.599 14.077 15.812 1.00 29.68 ? 27 ASP A CG 1 ATOM 199 O OD1 . ASP A 1 27 ? 14.757 13.845 14.926 1.00 28.57 ? 27 ASP A OD1 1 ATOM 200 O OD2 . ASP A 1 27 ? 15.287 14.654 16.873 1.00 37.32 ? 27 ASP A OD2 1 ATOM 201 N N . CYS A 1 28 ? 18.742 11.628 13.963 1.00 27.07 ? 28 CYS A N 1 ATOM 202 C CA . CYS A 1 28 ? 19.990 11.317 13.280 1.00 26.70 ? 28 CYS A CA 1 ATOM 203 C C . CYS A 1 28 ? 20.519 9.920 13.521 1.00 26.40 ? 28 CYS A C 1 ATOM 204 O O . CYS A 1 28 ? 21.596 9.585 13.054 1.00 25.83 ? 28 CYS A O 1 ATOM 205 C CB . CYS A 1 28 ? 21.046 12.375 13.591 1.00 29.32 ? 28 CYS A CB 1 ATOM 206 S SG . CYS A 1 28 ? 20.567 14.022 13.023 1.00 42.07 ? 28 CYS A SG 1 ATOM 207 N N . ASN A 1 29 ? 19.801 9.081 14.268 1.00 27.47 ? 29 ASN A N 1 ATOM 208 C CA . ASN A 1 29 ? 20.243 7.697 14.429 1.00 26.33 ? 29 ASN A CA 1 ATOM 209 C C . ASN A 1 29 ? 20.200 6.960 13.128 1.00 27.37 ? 29 ASN A C 1 ATOM 210 O O . ASN A 1 29 ? 21.140 6.276 12.777 1.00 29.37 ? 29 ASN A O 1 ATOM 211 C CB . ASN A 1 29 ? 19.340 6.954 15.422 1.00 27.64 ? 29 ASN A CB 1 ATOM 212 C CG . ASN A 1 29 ? 19.874 5.589 15.810 1.00 24.66 ? 29 ASN A CG 1 ATOM 213 O OD1 . ASN A 1 29 ? 20.018 4.694 14.983 1.00 24.83 ? 29 ASN A OD1 1 ATOM 214 N ND2 . ASN A 1 29 ? 20.025 5.373 17.128 1.00 27.38 ? 29 ASN A ND2 1 ATOM 215 N N . ASN A 1 30 ? 19.074 7.069 12.433 1.00 27.67 ? 30 ASN A N 1 ATOM 216 C CA . ASN A 1 30 ? 18.955 6.650 11.047 1.00 28.52 ? 30 ASN A CA 1 ATOM 217 C C . ASN A 1 30 ? 19.295 7.798 10.094 1.00 29.71 ? 30 ASN A C 1 ATOM 218 O O . ASN A 1 30 ? 18.575 8.832 10.013 1.00 26.87 ? 30 ASN A O 1 ATOM 219 C CB . ASN A 1 30 ? 17.552 6.173 10.747 1.00 31.02 ? 30 ASN A CB 1 ATOM 220 C CG . ASN A 1 30 ? 17.462 5.433 9.423 1.00 31.05 ? 30 ASN A CG 1 ATOM 221 O OD1 . ASN A 1 30 ? 17.469 6.037 8.343 1.00 30.75 ? 30 ASN A OD1 1 ATOM 222 N ND2 . ASN A 1 30 ? 17.345 4.125 9.499 1.00 30.93 ? 30 ASN A ND2 1 ATOM 223 N N . ARG A 1 31 ? 20.361 7.592 9.321 1.00 30.87 ? 31 ARG A N 1 ATOM 224 C CA . ARG A 1 31 ? 20.920 8.660 8.471 1.00 34.86 ? 31 ARG A CA 1 ATOM 225 C C . ARG A 1 31 ? 19.988 8.945 7.285 1.00 35.42 ? 31 ARG A C 1 ATOM 226 O O . ARG A 1 31 ? 19.625 10.102 7.017 1.00 33.81 ? 31 ARG A O 1 ATOM 227 C CB . ARG A 1 31 ? 22.329 8.243 7.984 1.00 42.46 ? 31 ARG A CB 1 ATOM 228 C CG . ARG A 1 31 ? 23.265 7.575 9.018 1.00 47.68 ? 31 ARG A CG 1 ATOM 229 C CD . ARG A 1 31 ? 24.376 8.434 9.698 1.00 50.72 ? 31 ARG A CD 1 ATOM 230 N NE . ARG A 1 31 ? 24.564 9.795 9.179 1.00 55.49 ? 31 ARG A NE 1 ATOM 231 C CZ . ARG A 1 31 ? 25.415 10.669 9.721 1.00 66.54 ? 31 ARG A CZ 1 ATOM 232 N NH1 . ARG A 1 31 ? 26.167 10.323 10.785 1.00 65.09 ? 31 ARG A NH1 1 ATOM 233 N NH2 . ARG A 1 31 ? 25.513 11.892 9.199 1.00 67.13 ? 31 ARG A NH2 1 ATOM 234 N N . ARG A 1 32 ? 19.521 7.885 6.633 1.00 35.68 ? 32 ARG A N 1 ATOM 235 C CA . ARG A 1 32 ? 18.579 8.034 5.532 1.00 41.26 ? 32 ARG A CA 1 ATOM 236 C C . ARG A 1 32 ? 17.288 8.742 5.986 1.00 39.96 ? 32 ARG A C 1 ATOM 237 O O . ARG A 1 32 ? 16.828 9.669 5.333 1.00 40.95 ? 32 ARG A O 1 ATOM 238 C CB . ARG A 1 32 ? 18.281 6.672 4.903 1.00 49.96 ? 32 ARG A CB 1 ATOM 239 C CG . ARG A 1 32 ? 17.571 6.823 3.559 1.00 56.44 ? 32 ARG A CG 1 ATOM 240 C CD . ARG A 1 32 ? 16.790 5.590 3.139 1.00 63.11 ? 32 ARG A CD 1 ATOM 241 N NE . ARG A 1 32 ? 17.628 4.479 2.688 1.00 68.04 ? 32 ARG A NE 1 ATOM 242 C CZ . ARG A 1 32 ? 17.575 3.231 3.151 1.00 72.06 ? 32 ARG A CZ 1 ATOM 243 N NH1 . ARG A 1 32 ? 16.726 2.862 4.119 1.00 71.19 ? 32 ARG A NH1 1 ATOM 244 N NH2 . ARG A 1 32 ? 18.399 2.333 2.630 1.00 74.15 ? 32 ARG A NH2 1 ATOM 245 N N . SER A 1 33 ? 16.728 8.350 7.133 1.00 38.30 ? 33 SER A N 1 ATOM 246 C CA . SER A 1 33 ? 15.529 9.027 7.648 1.00 34.85 ? 33 SER A CA 1 ATOM 247 C C . SER A 1 33 ? 15.686 9.449 9.135 1.00 35.81 ? 33 SER A C 1 ATOM 248 O O . SER A 1 33 ? 15.429 8.666 10.053 1.00 31.53 ? 33 SER A O 1 ATOM 249 C CB . SER A 1 33 ? 14.307 8.154 7.432 1.00 36.49 ? 33 SER A CB 1 ATOM 250 O OG . SER A 1 33 ? 13.151 8.924 7.725 1.00 43.43 ? 33 SER A OG 1 ATOM 251 N N . PRO A 1 34 ? 16.135 10.685 9.365 1.00 31.63 ? 34 PRO A N 1 ATOM 252 C CA . PRO A 1 34 ? 16.735 11.017 10.645 1.00 31.56 ? 34 PRO A CA 1 ATOM 253 C C . PRO A 1 34 ? 15.787 11.077 11.872 1.00 31.13 ? 34 PRO A C 1 ATOM 254 O O . PRO A 1 34 ? 16.257 10.943 13.026 1.00 30.43 ? 34 PRO A O 1 ATOM 255 C CB . PRO A 1 34 ? 17.383 12.389 10.366 1.00 35.63 ? 34 PRO A CB 1 ATOM 256 C CG . PRO A 1 34 ? 16.704 12.927 9.148 1.00 33.51 ? 34 PRO A CG 1 ATOM 257 C CD . PRO A 1 34 ? 16.339 11.737 8.341 1.00 32.99 ? 34 PRO A CD 1 ATOM 258 N N . ALA A 1 35 ? 14.501 11.300 11.625 1.00 28.19 ? 35 ALA A N 1 ATOM 259 C CA . ALA A 1 35 ? 13.474 11.311 12.665 1.00 27.55 ? 35 ALA A CA 1 ATOM 260 C C . ALA A 1 35 ? 12.986 9.929 13.123 1.00 27.30 ? 35 ALA A C 1 ATOM 261 O O . ALA A 1 35 ? 12.314 9.854 14.126 1.00 23.71 ? 35 ALA A O 1 ATOM 262 C CB . ALA A 1 35 ? 12.288 12.099 12.208 1.00 28.69 ? 35 ALA A CB 1 ATOM 263 N N . LEU A 1 36 ? 13.302 8.865 12.391 1.00 25.94 ? 36 LEU A N 1 ATOM 264 C CA . LEU A 1 36 ? 12.920 7.542 12.801 1.00 24.16 ? 36 LEU A CA 1 ATOM 265 C C . LEU A 1 36 ? 13.418 7.191 14.194 1.00 24.62 ? 36 LEU A C 1 ATOM 266 O O . LEU A 1 36 ? 14.670 7.081 14.455 1.00 19.55 ? 36 LEU A O 1 ATOM 267 C CB . LEU A 1 36 ? 13.434 6.480 11.841 1.00 26.41 ? 36 LEU A CB 1 ATOM 268 C CG . LEU A 1 36 ? 12.686 6.278 10.543 1.00 30.11 ? 36 LEU A CG 1 ATOM 269 C CD1 . LEU A 1 36 ? 13.214 5.002 9.941 1.00 33.40 ? 36 LEU A CD1 1 ATOM 270 C CD2 . LEU A 1 36 ? 11.188 6.203 10.704 1.00 30.53 ? 36 LEU A CD2 1 ATOM 271 N N . GLY A 1 37 ? 12.456 6.981 15.100 1.00 23.20 ? 37 GLY A N 1 ATOM 272 C CA . GLY A 1 37 ? 12.829 6.544 16.421 1.00 22.68 ? 37 GLY A CA 1 ATOM 273 C C . GLY A 1 37 ? 13.023 7.707 17.328 1.00 24.52 ? 37 GLY A C 1 ATOM 274 O O . GLY A 1 37 ? 13.168 7.500 18.546 1.00 21.74 ? 37 GLY A O 1 ATOM 275 N N . ALA A 1 38 ? 13.003 8.935 16.778 1.00 21.55 ? 38 ALA A N 1 ATOM 276 C CA . ALA A 1 38 ? 13.145 10.111 17.621 1.00 20.88 ? 38 ALA A CA 1 ATOM 277 C C . ALA A 1 38 ? 11.948 10.257 18.525 1.00 22.13 ? 38 ALA A C 1 ATOM 278 O O . ALA A 1 38 ? 10.846 9.774 18.196 1.00 18.04 ? 38 ALA A O 1 ATOM 279 C CB . ALA A 1 38 ? 13.268 11.356 16.806 1.00 22.08 ? 38 ALA A CB 1 ATOM 280 N N . ALA A 1 39 ? 12.139 10.997 19.609 1.00 21.74 ? 39 ALA A N 1 ATOM 281 C CA . ALA A 1 39 ? 11.066 11.354 20.558 1.00 21.42 ? 39 ALA A CA 1 ATOM 282 C C . ALA A 1 39 ? 10.139 12.392 19.971 1.00 23.01 ? 39 ALA A C 1 ATOM 283 O O . ALA A 1 39 ? 10.521 13.127 19.043 1.00 21.98 ? 39 ALA A O 1 ATOM 284 C CB . ALA A 1 39 ? 11.649 11.905 21.848 1.00 22.03 ? 39 ALA A CB 1 ATOM 285 N N . ASN A 1 40 ? 8.938 12.463 20.558 1.00 24.49 ? 40 ASN A N 1 ATOM 286 C CA . ASN A 1 40 ? 7.850 13.375 20.210 1.00 29.77 ? 40 ASN A CA 1 ATOM 287 C C . ASN A 1 40 ? 7.350 13.336 18.780 1.00 29.36 ? 40 ASN A C 1 ATOM 288 O O . ASN A 1 40 ? 7.036 14.361 18.194 1.00 26.74 ? 40 ASN A O 1 ATOM 289 C CB . ASN A 1 40 ? 8.160 14.796 20.672 1.00 35.15 ? 40 ASN A CB 1 ATOM 290 C CG . ASN A 1 40 ? 8.092 14.904 22.221 1.00 41.80 ? 40 ASN A CG 1 ATOM 291 O OD1 . ASN A 1 40 ? 7.029 14.693 22.840 1.00 45.46 ? 40 ASN A OD1 1 ATOM 292 N ND2 . ASN A 1 40 ? 9.239 15.118 22.847 1.00 45.51 ? 40 ASN A ND2 1 ATOM 293 N N . ARG A 1 41 ? 7.253 12.118 18.282 1.00 27.08 ? 41 ARG A N 1 ATOM 294 C CA . ARG A 1 41 ? 6.618 11.774 17.018 1.00 27.69 ? 41 ARG A CA 1 ATOM 295 C C . ARG A 1 41 ? 5.532 10.707 17.244 1.00 26.84 ? 41 ARG A C 1 ATOM 296 O O . ARG A 1 41 ? 5.420 10.095 18.306 1.00 24.57 ? 41 ARG A O 1 ATOM 297 C CB . ARG A 1 41 ? 7.643 11.153 16.039 1.00 33.45 ? 41 ARG A CB 1 ATOM 298 C CG . ARG A 1 41 ? 9.004 11.880 15.963 1.00 39.24 ? 41 ARG A CG 1 ATOM 299 C CD . ARG A 1 41 ? 8.808 13.324 15.547 1.00 45.97 ? 41 ARG A CD 1 ATOM 300 N NE . ARG A 1 41 ? 9.742 13.715 14.492 1.00 60.89 ? 41 ARG A NE 1 ATOM 301 C CZ . ARG A 1 41 ? 9.400 14.370 13.387 1.00 69.56 ? 41 ARG A CZ 1 ATOM 302 N NH1 . ARG A 1 41 ? 8.134 14.722 13.155 1.00 74.88 ? 41 ARG A NH1 1 ATOM 303 N NH2 . ARG A 1 41 ? 10.331 14.708 12.501 1.00 74.74 ? 41 ARG A NH2 1 ATOM 304 N N . ALA A 1 42 ? 4.769 10.473 16.204 1.00 21.16 ? 42 ALA A N 1 ATOM 305 C CA . ALA A 1 42 ? 3.745 9.487 16.237 1.00 21.48 ? 42 ALA A CA 1 ATOM 306 C C . ALA A 1 42 ? 4.249 8.090 16.497 1.00 19.22 ? 42 ALA A C 1 ATOM 307 O O . ALA A 1 42 ? 5.233 7.655 15.920 1.00 18.74 ? 42 ALA A O 1 ATOM 308 C CB . ALA A 1 42 ? 3.057 9.503 14.903 1.00 21.44 ? 42 ALA A CB 1 ATOM 309 N N . LEU A 1 43 ? 3.529 7.345 17.340 1.00 18.43 ? 43 LEU A N 1 ATOM 310 C CA . LEU A 1 43 ? 3.814 5.939 17.493 1.00 15.07 ? 43 LEU A CA 1 ATOM 311 C C . LEU A 1 43 ? 3.568 5.360 16.140 1.00 16.49 ? 43 LEU A C 1 ATOM 312 O O . LEU A 1 43 ? 2.638 5.738 15.433 1.00 15.41 ? 43 LEU A O 1 ATOM 313 C CB . LEU A 1 43 ? 2.859 5.308 18.561 1.00 14.68 ? 43 LEU A CB 1 ATOM 314 C CG . LEU A 1 43 ? 3.198 5.660 20.006 1.00 14.01 ? 43 LEU A CG 1 ATOM 315 C CD1 . LEU A 1 43 ? 1.973 5.679 20.918 1.00 13.63 ? 43 LEU A CD1 1 ATOM 316 C CD2 . LEU A 1 43 ? 4.329 4.727 20.489 1.00 13.41 ? 43 LEU A CD2 1 ATOM 317 N N . ALA A 1 44 ? 4.352 4.367 15.792 1.00 21.43 ? 44 ALA A N 1 ATOM 318 C CA . ALA A 1 44 ? 4.134 3.665 14.563 1.00 20.73 ? 44 ALA A CA 1 ATOM 319 C C . ALA A 1 44 ? 2.853 2.837 14.644 1.00 23.02 ? 44 ALA A C 1 ATOM 320 O O . ALA A 1 44 ? 2.439 2.343 15.732 1.00 22.11 ? 44 ALA A O 1 ATOM 321 C CB . ALA A 1 44 ? 5.322 2.745 14.278 1.00 22.64 ? 44 ALA A CB 1 ATOM 322 N N . ARG A 1 45 ? 2.221 2.692 13.491 1.00 19.88 ? 45 ARG A N 1 ATOM 323 C CA . ARG A 1 45 ? 1.110 1.789 13.312 1.00 20.49 ? 45 ARG A CA 1 ATOM 324 C C . ARG A 1 45 ? 1.467 0.616 12.417 1.00 22.01 ? 45 ARG A C 1 ATOM 325 O O . ARG A 1 45 ? 1.608 0.762 11.191 1.00 19.55 ? 45 ARG A O 1 ATOM 326 C CB . ARG A 1 45 ? -0.072 2.522 12.741 1.00 22.63 ? 45 ARG A CB 1 ATOM 327 C CG . ARG A 1 45 ? -0.705 3.484 13.774 1.00 22.71 ? 45 ARG A CG 1 ATOM 328 C CD . ARG A 1 45 ? -2.174 3.484 13.809 1.00 20.35 ? 45 ARG A CD 1 ATOM 329 N NE . ARG A 1 45 ? -2.656 4.486 14.746 1.00 19.70 ? 45 ARG A NE 1 ATOM 330 C CZ . ARG A 1 45 ? -3.391 4.234 15.858 1.00 17.84 ? 45 ARG A CZ 1 ATOM 331 N NH1 . ARG A 1 45 ? -3.761 2.978 16.180 1.00 16.65 ? 45 ARG A NH1 1 ATOM 332 N NH2 . ARG A 1 45 ? -3.795 5.237 16.615 1.00 15.91 ? 45 ARG A NH2 1 ATOM 333 N N . TRP A 1 46 ? 1.561 -0.557 13.023 1.00 18.13 ? 46 TRP A N 1 ATOM 334 C CA . TRP A 1 46 ? 1.686 -1.799 12.246 1.00 19.83 ? 46 TRP A CA 1 ATOM 335 C C . TRP A 1 46 ? 0.429 -2.208 11.458 1.00 20.31 ? 46 TRP A C 1 ATOM 336 O O . TRP A 1 46 ? 0.503 -2.972 10.441 1.00 21.06 ? 46 TRP A O 1 ATOM 337 C CB . TRP A 1 46 ? 2.103 -2.926 13.169 1.00 18.61 ? 46 TRP A CB 1 ATOM 338 C CG . TRP A 1 46 ? 3.503 -2.737 13.746 1.00 18.68 ? 46 TRP A CG 1 ATOM 339 C CD1 . TRP A 1 46 ? 4.475 -1.848 13.355 1.00 20.06 ? 46 TRP A CD1 1 ATOM 340 C CD2 . TRP A 1 46 ? 4.105 -3.524 14.772 1.00 17.69 ? 46 TRP A CD2 1 ATOM 341 N NE1 . TRP A 1 46 ? 5.630 -2.030 14.108 1.00 17.41 ? 46 TRP A NE1 1 ATOM 342 C CE2 . TRP A 1 46 ? 5.432 -3.066 14.951 1.00 18.11 ? 46 TRP A CE2 1 ATOM 343 C CE3 . TRP A 1 46 ? 3.666 -4.589 15.525 1.00 18.99 ? 46 TRP A CE3 1 ATOM 344 C CZ2 . TRP A 1 46 ? 6.281 -3.596 15.918 1.00 19.78 ? 46 TRP A CZ2 1 ATOM 345 C CZ3 . TRP A 1 46 ? 4.535 -5.102 16.522 1.00 20.48 ? 46 TRP A CZ3 1 ATOM 346 C CH2 . TRP A 1 46 ? 5.806 -4.611 16.681 1.00 19.74 ? 46 TRP A CH2 1 ATOM 347 N N . LEU A 1 47 ? -0.727 -1.841 12.024 1.00 19.45 ? 47 LEU A N 1 ATOM 348 C CA . LEU A 1 47 ? -2.031 -2.050 11.429 1.00 16.80 ? 47 LEU A CA 1 ATOM 349 C C . LEU A 1 47 ? -2.732 -0.718 11.413 1.00 16.83 ? 47 LEU A C 1 ATOM 350 O O . LEU A 1 47 ? -2.436 0.133 12.230 1.00 15.69 ? 47 LEU A O 1 ATOM 351 C CB . LEU A 1 47 ? -2.880 -3.060 12.182 1.00 16.95 ? 47 LEU A CB 1 ATOM 352 C CG . LEU A 1 47 ? -2.583 -4.541 11.955 1.00 16.93 ? 47 LEU A CG 1 ATOM 353 C CD1 . LEU A 1 47 ? -3.511 -5.405 12.814 1.00 17.51 ? 47 LEU A CD1 1 ATOM 354 C CD2 . LEU A 1 47 ? -2.611 -4.967 10.502 1.00 15.47 ? 47 LEU A CD2 1 ATOM 355 N N . PRO A 1 48 ? -3.690 -0.525 10.462 1.00 16.83 ? 48 PRO A N 1 ATOM 356 C CA . PRO A 1 48 ? -4.520 0.677 10.475 1.00 16.04 ? 48 PRO A CA 1 ATOM 357 C C . PRO A 1 48 ? -5.334 0.794 11.767 1.00 16.76 ? 48 PRO A C 1 ATOM 358 O O . PRO A 1 48 ? -5.835 -0.205 12.302 1.00 15.28 ? 48 PRO A O 1 ATOM 359 C CB . PRO A 1 48 ? -5.436 0.521 9.220 1.00 16.67 ? 48 PRO A CB 1 ATOM 360 C CG . PRO A 1 48 ? -4.717 -0.513 8.377 1.00 18.00 ? 48 PRO A CG 1 ATOM 361 C CD . PRO A 1 48 ? -4.036 -1.418 9.341 1.00 17.28 ? 48 PRO A CD 1 ATOM 362 N N . ALA A 1 49 ? -5.507 2.046 12.188 1.00 15.27 ? 49 ALA A N 1 ATOM 363 C CA . ALA A 1 49 ? -6.209 2.409 13.406 1.00 15.48 ? 49 ALA A CA 1 ATOM 364 C C . ALA A 1 49 ? -7.631 2.025 13.233 1.00 14.98 ? 49 ALA A C 1 ATOM 365 O O . ALA A 1 49 ? -8.142 2.010 12.111 1.00 14.08 ? 49 ALA A O 1 ATOM 366 C CB . ALA A 1 49 ? -6.062 3.907 13.650 1.00 14.92 ? 49 ALA A CB 1 ATOM 367 N N . GLU A 1 50 ? -8.310 1.729 14.338 1.00 15.27 ? 50 GLU A N 1 ATOM 368 C CA . GLU A 1 50 ? -9.701 1.336 14.299 1.00 14.35 ? 50 GLU A CA 1 ATOM 369 C C . GLU A 1 50 ? -10.389 2.200 15.334 1.00 16.76 ? 50 GLU A C 1 ATOM 370 O O . GLU A 1 50 ? -10.139 2.057 16.548 1.00 18.49 ? 50 GLU A O 1 ATOM 371 C CB . GLU A 1 50 ? -9.858 -0.139 14.616 1.00 16.26 ? 50 GLU A CB 1 ATOM 372 C CG . GLU A 1 50 ? -9.154 -1.004 13.614 1.00 17.23 ? 50 GLU A CG 1 ATOM 373 C CD . GLU A 1 50 ? -9.584 -2.472 13.600 1.00 18.30 ? 50 GLU A CD 1 ATOM 374 O OE1 . GLU A 1 50 ? -10.559 -2.878 14.272 1.00 18.21 ? 50 GLU A OE1 1 ATOM 375 O OE2 . GLU A 1 50 ? -8.880 -3.207 12.890 1.00 19.65 ? 50 GLU A OE2 1 ATOM 376 N N . TYR A 1 51 ? -11.194 3.138 14.804 1.00 18.04 ? 51 TYR A N 1 ATOM 377 C CA . TYR A 1 51 ? -11.982 4.065 15.490 1.00 17.13 ? 51 TYR A CA 1 ATOM 378 C C . TYR A 1 51 ? -13.416 3.933 14.991 1.00 19.77 ? 51 TYR A C 1 ATOM 379 O O . TYR A 1 51 ? -13.677 3.561 13.855 1.00 20.18 ? 51 TYR A O 1 ATOM 380 C CB . TYR A 1 51 ? -11.481 5.460 15.229 1.00 17.96 ? 51 TYR A CB 1 ATOM 381 C CG . TYR A 1 51 ? -10.142 5.815 15.905 1.00 18.15 ? 51 TYR A CG 1 ATOM 382 C CD1 . TYR A 1 51 ? -10.043 6.002 17.252 1.00 19.03 ? 51 TYR A CD1 1 ATOM 383 C CD2 . TYR A 1 51 ? -9.018 6.053 15.155 1.00 18.80 ? 51 TYR A CD2 1 ATOM 384 C CE1 . TYR A 1 51 ? -8.845 6.386 17.840 1.00 18.41 ? 51 TYR A CE1 1 ATOM 385 C CE2 . TYR A 1 51 ? -7.823 6.434 15.729 1.00 19.63 ? 51 TYR A CE2 1 ATOM 386 C CZ . TYR A 1 51 ? -7.730 6.572 17.083 1.00 19.35 ? 51 TYR A CZ 1 ATOM 387 O OH . TYR A 1 51 ? -6.503 6.944 17.647 1.00 21.37 ? 51 TYR A OH 1 ATOM 388 N N . GLU A 1 52 ? -14.337 4.299 15.868 1.00 20.43 ? 52 GLU A N 1 ATOM 389 C CA . GLU A 1 52 ? -15.755 4.332 15.625 1.00 19.97 ? 52 GLU A CA 1 ATOM 390 C C . GLU A 1 52 ? -16.159 5.056 14.370 1.00 22.23 ? 52 GLU A C 1 ATOM 391 O O . GLU A 1 52 ? -17.038 4.587 13.651 1.00 22.78 ? 52 GLU A O 1 ATOM 392 C CB . GLU A 1 52 ? -16.434 5.003 16.802 1.00 23.12 ? 52 GLU A CB 1 ATOM 393 C CG . GLU A 1 52 ? -17.880 4.592 17.000 1.00 23.59 ? 52 GLU A CG 1 ATOM 394 C CD . GLU A 1 52 ? -18.565 5.393 18.078 1.00 24.05 ? 52 GLU A CD 1 ATOM 395 O OE1 . GLU A 1 52 ? -18.948 6.555 17.816 1.00 22.65 ? 52 GLU A OE1 1 ATOM 396 O OE2 . GLU A 1 52 ? -18.689 4.880 19.204 1.00 24.82 ? 52 GLU A OE2 1 ATOM 397 N N . ASP A 1 53 ? -15.516 6.176 14.090 1.00 22.78 ? 53 ASP A N 1 ATOM 398 C CA . ASP A 1 53 ? -15.717 6.917 12.853 1.00 22.41 ? 53 ASP A CA 1 ATOM 399 C C . ASP A 1 53 ? -14.548 6.844 11.899 1.00 25.40 ? 53 ASP A C 1 ATOM 400 O O . ASP A 1 53 ? -14.389 7.717 11.040 1.00 26.42 ? 53 ASP A O 1 ATOM 401 C CB . ASP A 1 53 ? -15.953 8.379 13.194 1.00 22.85 ? 53 ASP A CB 1 ATOM 402 C CG . ASP A 1 53 ? -14.705 9.060 13.720 1.00 22.31 ? 53 ASP A CG 1 ATOM 403 O OD1 . ASP A 1 53 ? -13.776 8.369 14.113 1.00 22.93 ? 53 ASP A OD1 1 ATOM 404 O OD2 . ASP A 1 53 ? -14.662 10.315 13.728 1.00 26.36 ? 53 ASP A OD2 1 ATOM 405 N N . GLY A 1 54 ? -13.684 5.844 12.036 1.00 23.54 ? 54 GLY A N 1 ATOM 406 C CA . GLY A 1 54 ? -12.475 5.772 11.207 1.00 22.75 ? 54 GLY A CA 1 ATOM 407 C C . GLY A 1 54 ? -11.374 6.775 11.461 1.00 22.76 ? 54 GLY A C 1 ATOM 408 O O . GLY A 1 54 ? -10.285 6.617 10.961 1.00 20.41 ? 54 GLY A O 1 ATOM 409 N N . LEU A 1 55 ? -11.618 7.820 12.235 1.00 21.24 ? 55 LEU A N 1 ATOM 410 C CA . LEU A 1 55 ? -10.580 8.835 12.405 1.00 20.91 ? 55 LEU A CA 1 ATOM 411 C C . LEU A 1 55 ? -10.061 9.035 13.833 1.00 20.69 ? 55 LEU A C 1 ATOM 412 O O . LEU A 1 55 ? -8.866 9.161 14.037 1.00 16.15 ? 55 LEU A O 1 ATOM 413 C CB . LEU A 1 55 ? -11.109 10.205 12.009 1.00 22.04 ? 55 LEU A CB 1 ATOM 414 C CG . LEU A 1 55 ? -11.374 10.341 10.525 1.00 27.75 ? 55 LEU A CG 1 ATOM 415 C CD1 . LEU A 1 55 ? -12.175 11.614 10.328 1.00 28.05 ? 55 LEU A CD1 1 ATOM 416 C CD2 . LEU A 1 55 ? -10.057 10.412 9.784 1.00 27.50 ? 55 LEU A CD2 1 ATOM 417 N N . ALA A 1 56 ? -10.982 9.199 14.789 1.00 19.82 ? 56 ALA A N 1 ATOM 418 C CA . ALA A 1 56 ? -10.524 9.547 16.114 1.00 20.40 ? 56 ALA A CA 1 ATOM 419 C C . ALA A 1 56 ? -11.443 9.081 17.220 1.00 20.76 ? 56 ALA A C 1 ATOM 420 O O . ALA A 1 56 ? -11.012 9.065 18.382 1.00 21.74 ? 56 ALA A O 1 ATOM 421 C CB . ALA A 1 56 ? -10.344 11.083 16.174 1.00 21.41 ? 56 ALA A CB 1 ATOM 422 N N . VAL A 1 57 ? -12.698 8.779 16.901 1.00 19.31 ? 57 VAL A N 1 ATOM 423 C CA . VAL A 1 57 ? -13.696 8.496 17.931 1.00 18.81 ? 57 VAL A CA 1 ATOM 424 C C . VAL A 1 57 ? -13.470 7.051 18.445 1.00 18.52 ? 57 VAL A C 1 ATOM 425 O O . VAL A 1 57 ? -13.445 6.065 17.660 1.00 18.52 ? 57 VAL A O 1 ATOM 426 C CB . VAL A 1 57 ? -15.142 8.652 17.416 1.00 18.57 ? 57 VAL A CB 1 ATOM 427 C CG1 . VAL A 1 57 ? -16.117 8.302 18.520 1.00 18.81 ? 57 VAL A CG1 1 ATOM 428 C CG2 . VAL A 1 57 ? -15.447 10.057 16.895 1.00 18.69 ? 57 VAL A CG2 1 ATOM 429 N N . PRO A 1 58 ? -13.309 6.893 19.758 1.00 19.02 ? 58 PRO A N 1 ATOM 430 C CA . PRO A 1 58 ? -13.042 5.535 20.224 1.00 18.15 ? 58 PRO A CA 1 ATOM 431 C C . PRO A 1 58 ? -14.224 4.642 20.177 1.00 15.68 ? 58 PRO A C 1 ATOM 432 O O . PRO A 1 58 ? -15.353 5.052 20.503 1.00 16.60 ? 58 PRO A O 1 ATOM 433 C CB . PRO A 1 58 ? -12.589 5.708 21.704 1.00 19.12 ? 58 PRO A CB 1 ATOM 434 C CG . PRO A 1 58 ? -12.510 7.187 21.948 1.00 22.59 ? 58 PRO A CG 1 ATOM 435 C CD . PRO A 1 58 ? -13.283 7.879 20.846 1.00 20.58 ? 58 PRO A CD 1 ATOM 436 N N . PHE A 1 59 ? -14.002 3.378 19.840 1.00 14.97 ? 59 PHE A N 1 ATOM 437 C CA . PHE A 1 59 ? -15.009 2.373 20.138 1.00 14.01 ? 59 PHE A CA 1 ATOM 438 C C . PHE A 1 59 ? -15.386 2.443 21.637 1.00 15.51 ? 59 PHE A C 1 ATOM 439 O O . PHE A 1 59 ? -14.506 2.542 22.494 1.00 15.29 ? 59 PHE A O 1 ATOM 440 C CB . PHE A 1 59 ? -14.527 0.975 19.717 1.00 12.80 ? 59 PHE A CB 1 ATOM 441 C CG . PHE A 1 59 ? -14.610 0.767 18.248 1.00 13.22 ? 59 PHE A CG 1 ATOM 442 C CD1 . PHE A 1 59 ? -15.847 0.834 17.603 1.00 12.99 ? 59 PHE A CD1 1 ATOM 443 C CD2 . PHE A 1 59 ? -13.485 0.648 17.490 1.00 13.10 ? 59 PHE A CD2 1 ATOM 444 C CE1 . PHE A 1 59 ? -15.971 0.707 16.245 1.00 13.33 ? 59 PHE A CE1 1 ATOM 445 C CE2 . PHE A 1 59 ? -13.577 0.489 16.133 1.00 14.05 ? 59 PHE A CE2 1 ATOM 446 C CZ . PHE A 1 59 ? -14.801 0.549 15.492 1.00 15.08 ? 59 PHE A CZ 1 ATOM 447 N N . GLY A 1 60 ? -16.681 2.481 21.903 1.00 16.12 ? 60 GLY A N 1 ATOM 448 C CA . GLY A 1 60 ? -17.247 2.641 23.258 1.00 18.31 ? 60 GLY A CA 1 ATOM 449 C C . GLY A 1 60 ? -17.851 4.029 23.477 1.00 18.77 ? 60 GLY A C 1 ATOM 450 O O . GLY A 1 60 ? -18.536 4.256 24.444 1.00 20.75 ? 60 GLY A O 1 ATOM 451 N N . TRP A 1 61 ? -17.595 4.954 22.551 1.00 18.63 ? 61 TRP A N 1 ATOM 452 C CA . TRP A 1 61 ? -17.982 6.323 22.719 1.00 19.24 ? 61 TRP A CA 1 ATOM 453 C C . TRP A 1 61 ? -19.464 6.539 22.608 1.00 20.39 ? 61 TRP A C 1 ATOM 454 O O . TRP A 1 61 ? -20.055 7.169 23.468 1.00 19.50 ? 61 TRP A O 1 ATOM 455 C CB . TRP A 1 61 ? -17.261 7.210 21.706 1.00 17.80 ? 61 TRP A CB 1 ATOM 456 C CG . TRP A 1 61 ? -17.434 8.661 21.883 1.00 17.17 ? 61 TRP A CG 1 ATOM 457 C CD1 . TRP A 1 61 ? -18.426 9.450 21.341 1.00 17.85 ? 61 TRP A CD1 1 ATOM 458 C CD2 . TRP A 1 61 ? -16.588 9.546 22.631 1.00 17.86 ? 61 TRP A CD2 1 ATOM 459 N NE1 . TRP A 1 61 ? -18.215 10.785 21.698 1.00 18.40 ? 61 TRP A NE1 1 ATOM 460 C CE2 . TRP A 1 61 ? -17.115 10.852 22.506 1.00 19.10 ? 61 TRP A CE2 1 ATOM 461 C CE3 . TRP A 1 61 ? -15.478 9.353 23.446 1.00 18.76 ? 61 TRP A CE3 1 ATOM 462 C CZ2 . TRP A 1 61 ? -16.526 11.962 23.115 1.00 20.93 ? 61 TRP A CZ2 1 ATOM 463 C CZ3 . TRP A 1 61 ? -14.868 10.464 24.030 1.00 20.30 ? 61 TRP A CZ3 1 ATOM 464 C CH2 . TRP A 1 61 ? -15.403 11.761 23.860 1.00 18.83 ? 61 TRP A CH2 1 ATOM 465 N N . THR A 1 62 ? -20.063 6.013 21.554 1.00 24.24 ? 62 THR A N 1 ATOM 466 C CA . THR A 1 62 ? -21.443 6.397 21.208 1.00 22.79 ? 62 THR A CA 1 ATOM 467 C C . THR A 1 62 ? -22.377 5.251 21.452 1.00 25.56 ? 62 THR A C 1 ATOM 468 O O . THR A 1 62 ? -22.172 4.153 20.957 1.00 25.83 ? 62 THR A O 1 ATOM 469 C CB . THR A 1 62 ? -21.538 6.802 19.730 1.00 20.98 ? 62 THR A CB 1 ATOM 470 O OG1 . THR A 1 62 ? -20.617 7.863 19.470 1.00 19.13 ? 62 THR A OG1 1 ATOM 471 C CG2 . THR A 1 62 ? -22.946 7.210 19.370 1.00 22.48 ? 62 THR A CG2 1 ATOM 472 N N . GLN A 1 63 ? -23.431 5.499 22.184 1.00 32.37 ? 63 GLN A N 1 ATOM 473 C CA . GLN A 1 63 ? -24.296 4.450 22.630 1.00 39.02 ? 63 GLN A CA 1 ATOM 474 C C . GLN A 1 63 ? -25.055 3.583 21.620 1.00 40.50 ? 63 GLN A C 1 ATOM 475 O O . GLN A 1 63 ? -25.045 2.391 21.642 1.00 46.57 ? 63 GLN A O 1 ATOM 476 C CB . GLN A 1 63 ? -25.296 5.072 23.601 1.00 49.96 ? 63 GLN A CB 1 ATOM 477 C CG . GLN A 1 63 ? -24.811 5.135 25.028 1.00 55.07 ? 63 GLN A CG 1 ATOM 478 C CD . GLN A 1 63 ? -25.775 4.462 25.991 1.00 69.81 ? 63 GLN A CD 1 ATOM 479 O OE1 . GLN A 1 63 ? -26.994 4.601 25.885 1.00 73.08 ? 63 GLN A OE1 1 ATOM 480 N NE2 . GLN A 1 63 ? -25.225 3.722 26.938 1.00 73.11 ? 63 GLN A NE2 1 ATOM 481 N N . ARG A 1 64 ? -25.683 4.144 20.629 1.00 34.45 ? 64 ARG A N 1 ATOM 482 C CA . ARG A 1 64 ? -26.430 3.271 19.719 1.00 39.07 ? 64 ARG A CA 1 ATOM 483 C C . ARG A 1 64 ? -25.583 2.677 18.536 1.00 34.02 ? 64 ARG A C 1 ATOM 484 O O . ARG A 1 64 ? -26.120 1.939 17.667 1.00 30.82 ? 64 ARG A O 1 ATOM 485 C CB . ARG A 1 64 ? -27.658 4.010 19.213 1.00 44.00 ? 64 ARG A CB 1 ATOM 486 C CG . ARG A 1 64 ? -28.614 4.424 20.319 1.00 53.02 ? 64 ARG A CG 1 ATOM 487 C CD . ARG A 1 64 ? -29.099 3.300 21.218 1.00 59.50 ? 64 ARG A CD 1 ATOM 488 N NE . ARG A 1 64 ? -30.370 3.753 21.792 1.00 62.04 ? 64 ARG A NE 1 ATOM 489 C CZ . ARG A 1 64 ? -31.413 2.987 22.089 1.00 68.50 ? 64 ARG A CZ 1 ATOM 490 N NH1 . ARG A 1 64 ? -32.507 3.551 22.600 1.00 75.94 ? 64 ARG A NH1 1 ATOM 491 N NH2 . ARG A 1 64 ? -31.404 1.685 21.868 1.00 69.01 ? 64 ARG A NH2 1 ATOM 492 N N . LYS A 1 65 ? -24.277 2.962 18.542 1.00 25.59 ? 65 LYS A N 1 ATOM 493 C CA . LYS A 1 65 ? -23.342 2.418 17.539 1.00 22.69 ? 65 LYS A CA 1 ATOM 494 C C . LYS A 1 65 ? -22.786 1.113 18.094 1.00 21.44 ? 65 LYS A C 1 ATOM 495 O O . LYS A 1 65 ? -23.129 0.723 19.215 1.00 24.96 ? 65 LYS A O 1 ATOM 496 C CB . LYS A 1 65 ? -22.277 3.433 17.188 1.00 22.14 ? 65 LYS A CB 1 ATOM 497 C CG . LYS A 1 65 ? -22.817 4.557 16.287 1.00 26.20 ? 65 LYS A CG 1 ATOM 498 C CD . LYS A 1 65 ? -21.749 5.604 16.021 1.00 28.09 ? 65 LYS A CD 1 ATOM 499 C CE . LYS A 1 65 ? -22.224 6.849 15.302 1.00 30.16 ? 65 LYS A CE 1 ATOM 500 N NZ . LYS A 1 65 ? -22.801 6.457 13.973 1.00 37.65 ? 65 LYS A NZ 1 ATOM 501 N N . THR A 1 66 ? -22.005 0.415 17.299 1.00 20.18 ? 66 THR A N 1 ATOM 502 C CA . THR A 1 66 ? -21.534 -0.918 17.629 1.00 20.75 ? 66 THR A CA 1 ATOM 503 C C . THR A 1 66 ? -20.176 -1.092 17.017 1.00 21.42 ? 66 THR A C 1 ATOM 504 O O . THR A 1 66 ? -19.753 -0.273 16.178 1.00 19.34 ? 66 THR A O 1 ATOM 505 C CB . THR A 1 66 ? -22.467 -2.023 17.094 1.00 22.19 ? 66 THR A CB 1 ATOM 506 O OG1 . THR A 1 66 ? -22.447 -2.024 15.651 1.00 22.59 ? 66 THR A OG1 1 ATOM 507 C CG2 . THR A 1 66 ? -23.886 -1.839 17.644 1.00 22.26 ? 66 THR A CG2 1 ATOM 508 N N . ARG A 1 67 ? -19.468 -2.101 17.520 1.00 18.84 ? 67 ARG A N 1 ATOM 509 C CA . ARG A 1 67 ? -18.251 -2.541 16.940 1.00 18.35 ? 67 ARG A CA 1 ATOM 510 C C . ARG A 1 67 ? -18.557 -3.903 16.379 1.00 18.84 ? 67 ARG A C 1 ATOM 511 O O . ARG A 1 67 ? -18.948 -4.815 17.125 1.00 16.98 ? 67 ARG A O 1 ATOM 512 C CB . ARG A 1 67 ? -17.130 -2.567 18.011 1.00 17.68 ? 67 ARG A CB 1 ATOM 513 C CG . ARG A 1 67 ? -15.789 -2.936 17.388 1.00 18.46 ? 67 ARG A CG 1 ATOM 514 C CD . ARG A 1 67 ? -14.685 -3.124 18.418 1.00 17.64 ? 67 ARG A CD 1 ATOM 515 N NE . ARG A 1 67 ? -13.423 -3.100 17.735 1.00 18.61 ? 67 ARG A NE 1 ATOM 516 C CZ . ARG A 1 67 ? -12.260 -2.656 18.213 1.00 17.61 ? 67 ARG A CZ 1 ATOM 517 N NH1 . ARG A 1 67 ? -12.101 -2.211 19.460 1.00 19.63 ? 67 ARG A NH1 1 ATOM 518 N NH2 . ARG A 1 67 ? -11.242 -2.628 17.396 1.00 15.68 ? 67 ARG A NH2 1 ATOM 519 N N . ASN A 1 68 ? -18.452 -4.052 15.049 1.00 20.59 ? 68 ASN A N 1 ATOM 520 C CA . ASN A 1 68 ? -18.865 -5.311 14.378 1.00 18.30 ? 68 ASN A CA 1 ATOM 521 C C . ASN A 1 68 ? -20.272 -5.802 14.822 1.00 17.56 ? 68 ASN A C 1 ATOM 522 O O . ASN A 1 68 ? -20.612 -7.011 14.889 1.00 17.64 ? 68 ASN A O 1 ATOM 523 C CB . ASN A 1 68 ? -17.797 -6.362 14.642 1.00 19.86 ? 68 ASN A CB 1 ATOM 524 C CG . ASN A 1 68 ? -16.456 -6.013 14.039 1.00 21.41 ? 68 ASN A CG 1 ATOM 525 O OD1 . ASN A 1 68 ? -16.382 -5.591 12.889 1.00 19.29 ? 68 ASN A OD1 1 ATOM 526 N ND2 . ASN A 1 68 ? -15.372 -6.122 14.840 1.00 20.80 ? 68 ASN A ND2 1 ATOM 527 N N . GLY A 1 69 ? -21.121 -4.867 15.159 1.00 15.42 ? 69 GLY A N 1 ATOM 528 C CA . GLY A 1 69 ? -22.523 -5.246 15.468 1.00 17.71 ? 69 GLY A CA 1 ATOM 529 C C . GLY A 1 69 ? -22.887 -5.497 16.919 1.00 17.40 ? 69 GLY A C 1 ATOM 530 O O . GLY A 1 69 ? -24.060 -5.700 17.232 1.00 16.94 ? 69 GLY A O 1 ATOM 531 N N . PHE A 1 70 ? -21.894 -5.388 17.805 1.00 16.56 ? 70 PHE A N 1 ATOM 532 C CA . PHE A 1 70 ? -22.110 -5.582 19.221 1.00 18.03 ? 70 PHE A CA 1 ATOM 533 C C . PHE A 1 70 ? -21.627 -4.351 19.985 1.00 19.59 ? 70 PHE A C 1 ATOM 534 O O . PHE A 1 70 ? -20.661 -3.709 19.580 1.00 18.91 ? 70 PHE A O 1 ATOM 535 C CB . PHE A 1 70 ? -21.348 -6.822 19.692 1.00 17.78 ? 70 PHE A CB 1 ATOM 536 C CG . PHE A 1 70 ? -21.711 -8.042 18.907 1.00 18.64 ? 70 PHE A CG 1 ATOM 537 C CD1 . PHE A 1 70 ? -22.946 -8.644 19.104 1.00 17.66 ? 70 PHE A CD1 1 ATOM 538 C CD2 . PHE A 1 70 ? -20.891 -8.505 17.896 1.00 19.13 ? 70 PHE A CD2 1 ATOM 539 C CE1 . PHE A 1 70 ? -23.362 -9.712 18.322 1.00 20.47 ? 70 PHE A CE1 1 ATOM 540 C CE2 . PHE A 1 70 ? -21.283 -9.609 17.149 1.00 20.40 ? 70 PHE A CE2 1 ATOM 541 C CZ . PHE A 1 70 ? -22.523 -10.198 17.355 1.00 21.62 ? 70 PHE A CZ 1 ATOM 542 N N . ARG A 1 71 ? -22.249 -4.047 21.099 1.00 19.45 ? 71 ARG A N 1 ATOM 543 C CA . ARG A 1 71 ? -21.718 -3.077 22.022 1.00 23.06 ? 71 ARG A CA 1 ATOM 544 C C . ARG A 1 71 ? -20.418 -3.564 22.654 1.00 19.94 ? 71 ARG A C 1 ATOM 545 O O . ARG A 1 71 ? -20.243 -4.706 22.836 1.00 17.15 ? 71 ARG A O 1 ATOM 546 C CB . ARG A 1 71 ? -22.710 -2.791 23.120 1.00 27.87 ? 71 ARG A CB 1 ATOM 547 C CG . ARG A 1 71 ? -24.053 -2.402 22.603 1.00 34.08 ? 71 ARG A CG 1 ATOM 548 C CD . ARG A 1 71 ? -24.044 -0.941 22.275 1.00 43.53 ? 71 ARG A CD 1 ATOM 549 N NE . ARG A 1 71 ? -24.826 -0.249 23.247 1.00 51.06 ? 71 ARG A NE 1 ATOM 550 C CZ . ARG A 1 71 ? -24.458 0.859 23.839 1.00 62.15 ? 71 ARG A CZ 1 ATOM 551 N NH1 . ARG A 1 71 ? -23.305 1.400 23.524 1.00 67.41 ? 71 ARG A NH1 1 ATOM 552 N NH2 . ARG A 1 71 ? -25.257 1.417 24.744 1.00 61.98 ? 71 ARG A NH2 1 ATOM 553 N N . VAL A 1 72 ? -19.517 -2.668 22.949 1.00 20.10 ? 72 VAL A N 1 ATOM 554 C CA . VAL A 1 72 ? -18.307 -3.080 23.661 1.00 19.79 ? 72 VAL A CA 1 ATOM 555 C C . VAL A 1 72 ? -18.528 -2.940 25.161 1.00 17.83 ? 72 VAL A C 1 ATOM 556 O O . VAL A 1 72 ? -19.218 -2.024 25.586 1.00 17.74 ? 72 VAL A O 1 ATOM 557 C CB . VAL A 1 72 ? -17.000 -2.359 23.216 1.00 23.38 ? 72 VAL A CB 1 ATOM 558 C CG1 . VAL A 1 72 ? -16.875 -2.405 21.701 1.00 25.74 ? 72 VAL A CG1 1 ATOM 559 C CG2 . VAL A 1 72 ? -16.948 -0.961 23.703 1.00 23.32 ? 72 VAL A CG2 1 ATOM 560 N N . PRO A 1 73 ? -18.070 -3.931 25.946 1.00 17.90 ? 73 PRO A N 1 ATOM 561 C CA . PRO A 1 73 ? -18.327 -3.957 27.363 1.00 18.37 ? 73 PRO A CA 1 ATOM 562 C C . PRO A 1 73 ? -17.576 -2.841 28.123 1.00 19.14 ? 73 PRO A C 1 ATOM 563 O O . PRO A 1 73 ? -16.506 -2.396 27.722 1.00 16.92 ? 73 PRO A O 1 ATOM 564 C CB . PRO A 1 73 ? -17.870 -5.326 27.754 1.00 17.64 ? 73 PRO A CB 1 ATOM 565 C CG . PRO A 1 73 ? -16.772 -5.630 26.800 1.00 18.02 ? 73 PRO A CG 1 ATOM 566 C CD . PRO A 1 73 ? -17.295 -5.091 25.510 1.00 17.96 ? 73 PRO A CD 1 ATOM 567 N N . LEU A 1 74 ? -18.180 -2.351 29.186 1.00 20.31 ? 74 LEU A N 1 ATOM 568 C CA . LEU A 1 74 ? -17.565 -1.312 30.007 1.00 20.19 ? 74 LEU A CA 1 ATOM 569 C C . LEU A 1 74 ? -16.212 -1.840 30.459 1.00 18.38 ? 74 LEU A C 1 ATOM 570 O O . LEU A 1 74 ? -16.089 -2.989 30.878 1.00 15.91 ? 74 LEU A O 1 ATOM 571 C CB . LEU A 1 74 ? -18.412 -0.968 31.226 1.00 22.23 ? 74 LEU A CB 1 ATOM 572 C CG . LEU A 1 74 ? -19.744 -0.236 31.076 1.00 25.54 ? 74 LEU A CG 1 ATOM 573 C CD1 . LEU A 1 74 ? -20.381 0.003 32.437 1.00 27.67 ? 74 LEU A CD1 1 ATOM 574 C CD2 . LEU A 1 74 ? -19.522 1.082 30.391 1.00 29.06 ? 74 LEU A CD2 1 ATOM 575 N N . ALA A 1 75 ? -15.180 -1.025 30.310 1.00 16.92 ? 75 ALA A N 1 ATOM 576 C CA . ALA A 1 75 ? -13.835 -1.411 30.766 1.00 16.40 ? 75 ALA A CA 1 ATOM 577 C C . ALA A 1 75 ? -13.813 -1.922 32.229 1.00 16.05 ? 75 ALA A C 1 ATOM 578 O O . ALA A 1 75 ? -13.104 -2.887 32.575 1.00 19.47 ? 75 ALA A O 1 ATOM 579 C CB . ALA A 1 75 ? -12.939 -0.219 30.648 1.00 16.64 ? 75 ALA A CB 1 ATOM 580 N N . ARG A 1 76 ? -14.571 -1.269 33.081 1.00 17.04 ? 76 ARG A N 1 ATOM 581 C CA . ARG A 1 76 ? -14.597 -1.601 34.535 1.00 17.32 ? 76 ARG A CA 1 ATOM 582 C C . ARG A 1 76 ? -15.338 -2.899 34.790 1.00 17.37 ? 76 ARG A C 1 ATOM 583 O O . ARG A 1 76 ? -14.938 -3.637 35.715 1.00 16.88 ? 76 ARG A O 1 ATOM 584 C CB . ARG A 1 76 ? -15.241 -0.463 35.334 1.00 17.47 ? 76 ARG A CB 1 ATOM 585 C CG . ARG A 1 76 ? -15.471 -0.755 36.826 1.00 17.15 ? 76 ARG A CG 1 ATOM 586 C CD . ARG A 1 76 ? -14.187 -1.013 37.607 1.00 16.23 ? 76 ARG A CD 1 ATOM 587 N NE . ARG A 1 76 ? -14.504 -1.200 39.038 1.00 16.49 ? 76 ARG A NE 1 ATOM 588 C CZ . ARG A 1 76 ? -13.642 -1.462 39.998 1.00 16.57 ? 76 ARG A CZ 1 ATOM 589 N NH1 . ARG A 1 76 ? -12.327 -1.590 39.761 1.00 15.41 ? 76 ARG A NH1 1 ATOM 590 N NH2 . ARG A 1 76 ? -14.108 -1.658 41.226 1.00 17.21 ? 76 ARG A NH2 1 ATOM 591 N N . GLU A 1 77 ? -16.309 -3.251 33.934 1.00 16.26 ? 77 GLU A N 1 ATOM 592 C CA . GLU A 1 77 ? -16.968 -4.577 34.041 1.00 18.18 ? 77 GLU A CA 1 ATOM 593 C C . GLU A 1 77 ? -16.108 -5.708 33.650 1.00 14.94 ? 77 GLU A C 1 ATOM 594 O O . GLU A 1 77 ? -16.114 -6.773 34.294 1.00 18.45 ? 77 GLU A O 1 ATOM 595 C CB . GLU A 1 77 ? -18.256 -4.603 33.228 1.00 20.14 ? 77 GLU A CB 1 ATOM 596 C CG . GLU A 1 77 ? -19.093 -5.860 33.305 1.00 24.54 ? 77 GLU A CG 1 ATOM 597 C CD . GLU A 1 77 ? -20.500 -5.622 32.751 1.00 28.18 ? 77 GLU A CD 1 ATOM 598 O OE1 . GLU A 1 77 ? -20.856 -4.472 32.312 1.00 27.96 ? 77 GLU A OE1 1 ATOM 599 O OE2 . GLU A 1 77 ? -21.267 -6.581 32.816 1.00 30.78 ? 77 GLU A OE2 1 ATOM 600 N N . VAL A 1 78 ? -15.299 -5.509 32.613 1.00 14.42 ? 78 VAL A N 1 ATOM 601 C CA . VAL A 1 78 ? -14.315 -6.503 32.252 1.00 13.83 ? 78 VAL A CA 1 ATOM 602 C C . VAL A 1 78 ? -13.357 -6.719 33.381 1.00 12.85 ? 78 VAL A C 1 ATOM 603 O O . VAL A 1 78 ? -12.958 -7.870 33.733 1.00 13.11 ? 78 VAL A O 1 ATOM 604 C CB . VAL A 1 78 ? -13.563 -6.058 30.923 1.00 14.15 ? 78 VAL A CB 1 ATOM 605 C CG1 . VAL A 1 78 ? -12.485 -7.019 30.550 1.00 12.68 ? 78 VAL A CG1 1 ATOM 606 C CG2 . VAL A 1 78 ? -14.532 -5.936 29.743 1.00 14.39 ? 78 VAL A CG2 1 ATOM 607 N N . SER A 1 79 ? -12.833 -5.600 33.865 1.00 12.69 ? 79 SER A N 1 ATOM 608 C CA . SER A 1 79 ? -11.910 -5.622 35.050 1.00 15.16 ? 79 SER A CA 1 ATOM 609 C C . SER A 1 79 ? -12.511 -6.461 36.210 1.00 16.24 ? 79 SER A C 1 ATOM 610 O O . SER A 1 79 ? -11.885 -7.418 36.637 1.00 20.04 ? 79 SER A O 1 ATOM 611 C CB . SER A 1 79 ? -11.582 -4.199 35.546 1.00 13.40 ? 79 SER A CB 1 ATOM 612 O OG . SER A 1 79 ? -10.631 -4.189 36.581 1.00 14.70 ? 79 SER A OG 1 ATOM 613 N N . ASN A 1 80 ? -13.709 -6.127 36.641 1.00 17.27 ? 80 ASN A N 1 ATOM 614 C CA . ASN A 1 80 ? -14.364 -6.803 37.746 1.00 18.54 ? 80 ASN A CA 1 ATOM 615 C C . ASN A 1 80 ? -14.570 -8.311 37.478 1.00 19.46 ? 80 ASN A C 1 ATOM 616 O O . ASN A 1 80 ? -14.216 -9.113 38.277 1.00 21.51 ? 80 ASN A O 1 ATOM 617 C CB . ASN A 1 80 ? -15.758 -6.272 37.999 1.00 16.91 ? 80 ASN A CB 1 ATOM 618 C CG . ASN A 1 80 ? -15.767 -4.858 38.534 1.00 19.92 ? 80 ASN A CG 1 ATOM 619 O OD1 . ASN A 1 80 ? -14.747 -4.338 38.978 1.00 19.12 ? 80 ASN A OD1 1 ATOM 620 N ND2 . ASN A 1 80 ? -16.910 -4.185 38.386 1.00 18.80 ? 80 ASN A ND2 1 ATOM 621 N N . LYS A 1 81 ? -15.073 -8.668 36.309 1.00 20.16 ? 81 LYS A N 1 ATOM 622 C CA . LYS A 1 81 ? -15.487 -10.064 36.035 1.00 20.45 ? 81 LYS A CA 1 ATOM 623 C C . LYS A 1 81 ? -14.397 -10.938 35.590 1.00 20.40 ? 81 LYS A C 1 ATOM 624 O O . LYS A 1 81 ? -14.464 -12.160 35.788 1.00 21.45 ? 81 LYS A O 1 ATOM 625 C CB . LYS A 1 81 ? -16.574 -10.095 34.981 1.00 21.76 ? 81 LYS A CB 1 ATOM 626 C CG . LYS A 1 81 ? -17.816 -9.390 35.539 1.00 28.59 ? 81 LYS A CG 1 ATOM 627 C CD . LYS A 1 81 ? -18.976 -9.405 34.563 1.00 29.59 ? 81 LYS A CD 1 ATOM 628 C CE . LYS A 1 81 ? -20.250 -8.869 35.240 1.00 29.93 ? 81 LYS A CE 1 ATOM 629 N NZ . LYS A 1 81 ? -21.335 -8.940 34.217 1.00 30.43 ? 81 LYS A NZ 1 ATOM 630 N N . ILE A 1 82 ? -13.412 -10.371 34.912 1.00 20.60 ? 82 ILE A N 1 ATOM 631 C CA . ILE A 1 82 ? -12.300 -11.189 34.433 1.00 21.83 ? 82 ILE A CA 1 ATOM 632 C C . ILE A 1 82 ? -10.974 -10.987 35.140 1.00 22.55 ? 82 ILE A C 1 ATOM 633 O O . ILE A 1 82 ? -10.257 -11.951 35.415 1.00 23.23 ? 82 ILE A O 1 ATOM 634 C CB . ILE A 1 82 ? -12.118 -10.985 32.940 1.00 24.06 ? 82 ILE A CB 1 ATOM 635 C CG1 . ILE A 1 82 ? -13.288 -11.633 32.186 1.00 28.47 ? 82 ILE A CG1 1 ATOM 636 C CG2 . ILE A 1 82 ? -10.813 -11.638 32.461 1.00 22.81 ? 82 ILE A CG2 1 ATOM 637 C CD1 . ILE A 1 82 ? -13.623 -10.854 30.955 1.00 31.30 ? 82 ILE A CD1 1 ATOM 638 N N . VAL A 1 83 ? -10.644 -9.747 35.433 1.00 20.20 ? 83 VAL A N 1 ATOM 639 C CA . VAL A 1 83 ? -9.271 -9.379 35.811 1.00 19.78 ? 83 VAL A CA 1 ATOM 640 C C . VAL A 1 83 ? -9.008 -9.433 37.336 1.00 18.59 ? 83 VAL A C 1 ATOM 641 O O . VAL A 1 83 ? -7.861 -9.500 37.770 1.00 21.10 ? 83 VAL A O 1 ATOM 642 C CB . VAL A 1 83 ? -8.988 -7.952 35.231 1.00 18.56 ? 83 VAL A CB 1 ATOM 643 C CG1 . VAL A 1 83 ? -7.567 -7.531 35.509 1.00 19.98 ? 83 VAL A CG1 1 ATOM 644 C CG2 . VAL A 1 83 ? -9.241 -7.908 33.735 1.00 17.27 ? 83 VAL A CG2 1 ATOM 645 N N . GLY A 1 84 ? -10.067 -9.392 38.171 1.00 18.47 ? 84 GLY A N 1 ATOM 646 C CA . GLY A 1 84 ? -9.945 -9.230 39.608 1.00 17.95 ? 84 GLY A CA 1 ATOM 647 C C . GLY A 1 84 ? -9.848 -10.538 40.379 1.00 19.08 ? 84 GLY A C 1 ATOM 648 O O . GLY A 1 84 ? -10.261 -11.611 39.882 1.00 22.23 ? 84 GLY A O 1 ATOM 649 N N . TYR A 1 85 ? -9.221 -10.492 41.560 1.00 21.18 ? 85 TYR A N 1 ATOM 650 C CA . TYR A 1 85 ? -9.236 -11.610 42.509 1.00 21.76 ? 85 TYR A CA 1 ATOM 651 C C . TYR A 1 85 ? -8.997 -11.099 43.891 1.00 23.59 ? 85 TYR A C 1 ATOM 652 O O . TYR A 1 85 ? -8.518 -9.952 44.101 1.00 22.54 ? 85 TYR A O 1 ATOM 653 C CB . TYR A 1 85 ? -8.142 -12.634 42.122 1.00 20.93 ? 85 TYR A CB 1 ATOM 654 C CG . TYR A 1 85 ? -6.739 -12.079 42.281 1.00 21.30 ? 85 TYR A CG 1 ATOM 655 C CD1 . TYR A 1 85 ? -6.154 -11.271 41.306 1.00 19.06 ? 85 TYR A CD1 1 ATOM 656 C CD2 . TYR A 1 85 ? -5.991 -12.407 43.390 1.00 21.86 ? 85 TYR A CD2 1 ATOM 657 C CE1 . TYR A 1 85 ? -4.913 -10.758 41.479 1.00 21.10 ? 85 TYR A CE1 1 ATOM 658 C CE2 . TYR A 1 85 ? -4.739 -11.933 43.562 1.00 20.59 ? 85 TYR A CE2 1 ATOM 659 C CZ . TYR A 1 85 ? -4.195 -11.123 42.606 1.00 21.90 ? 85 TYR A CZ 1 ATOM 660 O OH . TYR A 1 85 ? -2.992 -10.632 42.820 1.00 19.93 ? 85 TYR A OH 1 ATOM 661 N N . LEU A 1 86 ? -9.255 -11.976 44.861 1.00 26.87 ? 86 LEU A N 1 ATOM 662 C CA . LEU A 1 86 ? -9.135 -11.620 46.299 1.00 27.66 ? 86 LEU A CA 1 ATOM 663 C C . LEU A 1 86 ? -7.946 -12.272 46.965 1.00 25.50 ? 86 LEU A C 1 ATOM 664 O O . LEU A 1 86 ? -7.302 -11.677 47.785 1.00 29.90 ? 86 LEU A O 1 ATOM 665 C CB . LEU A 1 86 ? -10.394 -12.103 47.013 1.00 29.66 ? 86 LEU A CB 1 ATOM 666 C CG . LEU A 1 86 ? -11.131 -11.238 47.987 1.00 35.28 ? 86 LEU A CG 1 ATOM 667 C CD1 . LEU A 1 86 ? -11.339 -9.861 47.371 1.00 37.87 ? 86 LEU A CD1 1 ATOM 668 C CD2 . LEU A 1 86 ? -12.464 -11.920 48.325 1.00 36.72 ? 86 LEU A CD2 1 ATOM 669 N N . ASP A 1 87 ? -7.662 -13.513 46.624 1.00 24.52 ? 87 ASP A N 1 ATOM 670 C CA . ASP A 1 87 ? -6.756 -14.321 47.403 1.00 23.80 ? 87 ASP A CA 1 ATOM 671 C C . ASP A 1 87 ? -5.362 -14.338 46.763 1.00 23.75 ? 87 ASP A C 1 ATOM 672 O O . ASP A 1 87 ? -5.174 -14.855 45.700 1.00 25.26 ? 87 ASP A O 1 ATOM 673 C CB . ASP A 1 87 ? -7.339 -15.705 47.538 1.00 26.08 ? 87 ASP A CB 1 ATOM 674 C CG . ASP A 1 87 ? -6.510 -16.632 48.444 1.00 26.46 ? 87 ASP A CG 1 ATOM 675 O OD1 . ASP A 1 87 ? -5.536 -16.185 49.075 1.00 25.70 ? 87 ASP A OD1 1 ATOM 676 O OD2 . ASP A 1 87 ? -6.884 -17.829 48.538 1.00 34.12 ? 87 ASP A OD2 1 ATOM 677 N N . GLU A 1 88 ? -4.416 -13.704 47.436 1.00 23.65 ? 88 GLU A N 1 ATOM 678 C CA . GLU A 1 88 ? -3.031 -13.599 47.016 1.00 23.48 ? 88 GLU A CA 1 ATOM 679 C C . GLU A 1 88 ? -2.240 -14.856 47.315 1.00 24.15 ? 88 GLU A C 1 ATOM 680 O O . GLU A 1 88 ? -1.095 -15.007 46.884 1.00 25.10 ? 88 GLU A O 1 ATOM 681 C CB . GLU A 1 88 ? -2.394 -12.404 47.723 1.00 21.68 ? 88 GLU A CB 1 ATOM 682 C CG . GLU A 1 88 ? -3.118 -11.070 47.498 1.00 22.64 ? 88 GLU A CG 1 ATOM 683 C CD . GLU A 1 88 ? -2.946 -10.441 46.102 1.00 24.18 ? 88 GLU A CD 1 ATOM 684 O OE1 . GLU A 1 88 ? -2.133 -10.948 45.304 1.00 20.77 ? 88 GLU A OE1 1 ATOM 685 O OE2 . GLU A 1 88 ? -3.569 -9.367 45.835 1.00 21.58 ? 88 GLU A OE2 1 ATOM 686 N N . GLU A 1 89 ? -2.814 -15.758 48.094 1.00 24.43 ? 89 GLU A N 1 ATOM 687 C CA . GLU A 1 89 ? -2.077 -16.955 48.429 1.00 25.87 ? 89 GLU A CA 1 ATOM 688 C C . GLU A 1 89 ? -1.818 -17.751 47.170 1.00 21.24 ? 89 GLU A C 1 ATOM 689 O O . GLU A 1 89 ? -2.644 -18.024 46.428 1.00 21.82 ? 89 GLU A O 1 ATOM 690 C CB . GLU A 1 89 ? -2.768 -17.804 49.526 1.00 32.08 ? 89 GLU A CB 1 ATOM 691 C CG . GLU A 1 89 ? -2.041 -19.085 49.902 1.00 39.98 ? 89 GLU A CG 1 ATOM 692 C CD . GLU A 1 89 ? -0.794 -18.825 50.717 1.00 51.87 ? 89 GLU A CD 1 ATOM 693 O OE1 . GLU A 1 89 ? -0.932 -18.422 51.870 1.00 66.75 ? 89 GLU A OE1 1 ATOM 694 O OE2 . GLU A 1 89 ? 0.344 -19.003 50.230 1.00 63.62 ? 89 GLU A OE2 1 ATOM 695 N N . GLY A 1 90 ? -0.602 -18.121 46.981 1.00 25.10 ? 90 GLY A N 1 ATOM 696 C CA . GLY A 1 90 ? -0.181 -18.955 45.842 1.00 25.76 ? 90 GLY A CA 1 ATOM 697 C C . GLY A 1 90 ? 0.046 -18.206 44.536 1.00 27.99 ? 90 GLY A C 1 ATOM 698 O O . GLY A 1 90 ? 0.341 -18.857 43.536 1.00 27.55 ? 90 GLY A O 1 ATOM 699 N N . VAL A 1 91 ? -0.089 -16.859 44.515 1.00 29.08 ? 91 VAL A N 1 ATOM 700 C CA . VAL A 1 91 ? -0.020 -16.100 43.220 1.00 29.15 ? 91 VAL A CA 1 ATOM 701 C C . VAL A 1 91 ? 1.400 -15.771 42.816 1.00 27.80 ? 91 VAL A C 1 ATOM 702 O O . VAL A 1 91 ? 1.583 -15.250 41.747 1.00 26.02 ? 91 VAL A O 1 ATOM 703 C CB . VAL A 1 91 ? -0.754 -14.742 43.175 1.00 31.35 ? 91 VAL A CB 1 ATOM 704 C CG1 . VAL A 1 91 ? -2.211 -14.939 43.410 1.00 39.66 ? 91 VAL A CG1 1 ATOM 705 C CG2 . VAL A 1 91 ? -0.163 -13.752 44.138 1.00 30.20 ? 91 VAL A CG2 1 ATOM 706 N N . LEU A 1 92 ? 2.398 -16.020 43.651 1.00 24.05 ? 92 LEU A N 1 ATOM 707 C CA . LEU A 1 92 ? 3.722 -15.537 43.345 1.00 24.37 ? 92 LEU A CA 1 ATOM 708 C C . LEU A 1 92 ? 4.393 -16.420 42.314 1.00 25.56 ? 92 LEU A C 1 ATOM 709 O O . LEU A 1 92 ? 4.002 -17.571 42.137 1.00 26.60 ? 92 LEU A O 1 ATOM 710 C CB . LEU A 1 92 ? 4.589 -15.435 44.603 1.00 25.67 ? 92 LEU A CB 1 ATOM 711 C CG . LEU A 1 92 ? 4.067 -14.386 45.618 1.00 26.34 ? 92 LEU A CG 1 ATOM 712 C CD1 . LEU A 1 92 ? 4.965 -14.357 46.849 1.00 27.94 ? 92 LEU A CD1 1 ATOM 713 C CD2 . LEU A 1 92 ? 3.983 -13.018 44.995 1.00 27.12 ? 92 LEU A CD2 1 ATOM 714 N N . ASP A 1 93 ? 5.384 -15.851 41.628 1.00 24.21 ? 93 ASP A N 1 ATOM 715 C CA . ASP A 1 93 ? 6.149 -16.508 40.570 1.00 22.06 ? 93 ASP A CA 1 ATOM 716 C C . ASP A 1 93 ? 7.310 -17.126 41.262 1.00 23.62 ? 93 ASP A C 1 ATOM 717 O O . ASP A 1 93 ? 8.260 -16.451 41.669 1.00 25.15 ? 93 ASP A O 1 ATOM 718 C CB . ASP A 1 93 ? 6.648 -15.487 39.551 1.00 21.05 ? 93 ASP A CB 1 ATOM 719 C CG . ASP A 1 93 ? 7.274 -16.151 38.339 1.00 22.16 ? 93 ASP A CG 1 ATOM 720 O OD1 . ASP A 1 93 ? 7.680 -17.343 38.431 1.00 22.30 ? 93 ASP A OD1 1 ATOM 721 O OD2 . ASP A 1 93 ? 7.314 -15.485 37.297 1.00 20.88 ? 93 ASP A OD2 1 ATOM 722 N N . GLN A 1 94 ? 7.238 -18.437 41.384 1.00 27.75 ? 94 GLN A N 1 ATOM 723 C CA . GLN A 1 94 ? 8.210 -19.181 42.160 1.00 35.77 ? 94 GLN A CA 1 ATOM 724 C C . GLN A 1 94 ? 9.606 -19.126 41.538 1.00 35.05 ? 94 GLN A C 1 ATOM 725 O O . GLN A 1 94 ? 10.551 -19.513 42.196 1.00 37.52 ? 94 GLN A O 1 ATOM 726 C CB . GLN A 1 94 ? 7.771 -20.657 42.281 1.00 38.90 ? 94 GLN A CB 1 ATOM 727 C CG . GLN A 1 94 ? 6.427 -20.833 42.962 1.00 43.48 ? 94 GLN A CG 1 ATOM 728 C CD . GLN A 1 94 ? 6.423 -20.178 44.332 1.00 42.02 ? 94 GLN A CD 1 ATOM 729 O OE1 . GLN A 1 94 ? 5.584 -19.346 44.598 1.00 42.61 ? 94 GLN A OE1 1 ATOM 730 N NE2 . GLN A 1 94 ? 7.394 -20.511 45.175 1.00 43.03 ? 94 GLN A NE2 1 ATOM 731 N N . ASN A 1 95 ? 9.753 -18.644 40.303 1.00 32.27 ? 95 ASN A N 1 ATOM 732 C CA . ASN A 1 95 ? 11.066 -18.638 39.696 1.00 33.37 ? 95 ASN A CA 1 ATOM 733 C C . ASN A 1 95 ? 11.488 -17.303 39.160 1.00 32.45 ? 95 ASN A C 1 ATOM 734 O O . ASN A 1 95 ? 12.389 -17.248 38.327 1.00 31.94 ? 95 ASN A O 1 ATOM 735 C CB . ASN A 1 95 ? 11.124 -19.689 38.581 1.00 40.83 ? 95 ASN A CB 1 ATOM 736 C CG . ASN A 1 95 ? 12.535 -20.058 38.219 1.00 51.82 ? 95 ASN A CG 1 ATOM 737 O OD1 . ASN A 1 95 ? 13.491 -19.799 38.983 1.00 62.83 ? 95 ASN A OD1 1 ATOM 738 N ND2 . ASN A 1 95 ? 12.693 -20.653 37.055 1.00 60.69 ? 95 ASN A ND2 1 ATOM 739 N N . ARG A 1 96 ? 10.871 -16.228 39.659 1.00 29.41 ? 96 ARG A N 1 ATOM 740 C CA . ARG A 1 96 ? 11.246 -14.865 39.305 1.00 25.98 ? 96 ARG A CA 1 ATOM 741 C C . ARG A 1 96 ? 11.230 -13.917 40.489 1.00 23.51 ? 96 ARG A C 1 ATOM 742 O O . ARG A 1 96 ? 10.193 -13.737 41.133 1.00 21.27 ? 96 ARG A O 1 ATOM 743 C CB . ARG A 1 96 ? 10.274 -14.339 38.265 1.00 27.14 ? 96 ARG A CB 1 ATOM 744 C CG . ARG A 1 96 ? 10.222 -15.058 36.927 1.00 30.81 ? 96 ARG A CG 1 ATOM 745 C CD . ARG A 1 96 ? 11.459 -14.942 36.091 1.00 34.80 ? 96 ARG A CD 1 ATOM 746 N NE . ARG A 1 96 ? 11.122 -15.519 34.784 1.00 38.65 ? 96 ARG A NE 1 ATOM 747 C CZ . ARG A 1 96 ? 11.211 -16.806 34.470 1.00 39.13 ? 96 ARG A CZ 1 ATOM 748 N NH1 . ARG A 1 96 ? 11.715 -17.656 35.353 1.00 40.37 ? 96 ARG A NH1 1 ATOM 749 N NH2 . ARG A 1 96 ? 10.826 -17.222 33.237 1.00 39.90 ? 96 ARG A NH2 1 ATOM 750 N N . SER A 1 97 ? 12.360 -13.284 40.753 1.00 25.12 ? 97 SER A N 1 ATOM 751 C CA . SER A 1 97 ? 12.429 -12.236 41.763 1.00 23.27 ? 97 SER A CA 1 ATOM 752 C C . SER A 1 97 ? 11.592 -11.043 41.324 1.00 22.82 ? 97 SER A C 1 ATOM 753 O O . SER A 1 97 ? 11.171 -10.919 40.161 1.00 24.14 ? 97 SER A O 1 ATOM 754 C CB . SER A 1 97 ? 13.852 -11.786 42.002 1.00 22.64 ? 97 SER A CB 1 ATOM 755 O OG . SER A 1 97 ? 14.407 -11.169 40.843 1.00 24.31 ? 97 SER A OG 1 ATOM 756 N N . LEU A 1 98 ? 11.288 -10.219 42.295 1.00 19.92 ? 98 LEU A N 1 ATOM 757 C CA . LEU A 1 98 ? 10.511 -9.031 42.075 1.00 19.33 ? 98 LEU A CA 1 ATOM 758 C C . LEU A 1 98 ? 11.225 -8.097 41.059 1.00 19.10 ? 98 LEU A C 1 ATOM 759 O O . LEU A 1 98 ? 10.596 -7.290 40.420 1.00 19.32 ? 98 LEU A O 1 ATOM 760 C CB . LEU A 1 98 ? 10.313 -8.355 43.389 1.00 19.61 ? 98 LEU A CB 1 ATOM 761 C CG . LEU A 1 98 ? 9.437 -7.113 43.408 1.00 18.46 ? 98 LEU A CG 1 ATOM 762 C CD1 . LEU A 1 98 ? 8.125 -7.431 42.812 1.00 16.91 ? 98 LEU A CD1 1 ATOM 763 C CD2 . LEU A 1 98 ? 9.265 -6.697 44.874 1.00 22.00 ? 98 LEU A CD2 1 ATOM 764 N N . LEU A 1 99 ? 12.540 -8.246 40.943 1.00 20.03 ? 99 LEU A N 1 ATOM 765 C CA . LEU A 1 99 ? 13.342 -7.460 39.993 1.00 21.01 ? 99 LEU A CA 1 ATOM 766 C C . LEU A 1 99 ? 12.947 -7.673 38.563 1.00 19.16 ? 99 LEU A C 1 ATOM 767 O O . LEU A 1 99 ? 13.096 -6.750 37.736 1.00 20.31 ? 99 LEU A O 1 ATOM 768 C CB . LEU A 1 99 ? 14.833 -7.762 40.166 1.00 23.62 ? 99 LEU A CB 1 ATOM 769 C CG . LEU A 1 99 ? 15.795 -7.103 39.161 1.00 26.38 ? 99 LEU A CG 1 ATOM 770 C CD1 . LEU A 1 99 ? 15.951 -5.616 39.488 1.00 27.42 ? 99 LEU A CD1 1 ATOM 771 C CD2 . LEU A 1 99 ? 17.135 -7.795 39.148 1.00 27.72 ? 99 LEU A CD2 1 ATOM 772 N N . PHE A 1 100 ? 12.500 -8.885 38.266 1.00 17.54 ? 100 PHE A N 1 ATOM 773 C CA . PHE A 1 100 ? 11.964 -9.215 36.973 1.00 17.63 ? 100 PHE A CA 1 ATOM 774 C C . PHE A 1 100 ? 10.819 -8.306 36.588 1.00 18.45 ? 100 PHE A C 1 ATOM 775 O O . PHE A 1 100 ? 10.837 -7.729 35.487 1.00 17.56 ? 100 PHE A O 1 ATOM 776 C CB . PHE A 1 100 ? 11.477 -10.627 36.958 1.00 18.27 ? 100 PHE A CB 1 ATOM 777 C CG . PHE A 1 100 ? 10.772 -11.022 35.675 1.00 18.55 ? 100 PHE A CG 1 ATOM 778 C CD1 . PHE A 1 100 ? 11.433 -10.999 34.454 1.00 18.68 ? 100 PHE A CD1 1 ATOM 779 C CD2 . PHE A 1 100 ? 9.470 -11.493 35.710 1.00 19.60 ? 100 PHE A CD2 1 ATOM 780 C CE1 . PHE A 1 100 ? 10.764 -11.399 33.280 1.00 19.16 ? 100 PHE A CE1 1 ATOM 781 C CE2 . PHE A 1 100 ? 8.789 -11.884 34.532 1.00 19.95 ? 100 PHE A CE2 1 ATOM 782 C CZ . PHE A 1 100 ? 9.451 -11.823 33.318 1.00 17.28 ? 100 PHE A CZ 1 ATOM 783 N N . MET A 1 101 ? 9.818 -8.167 37.462 1.00 16.10 ? 101 MET A N 1 ATOM 784 C CA . MET A 1 101 ? 8.739 -7.199 37.194 1.00 16.46 ? 101 MET A CA 1 ATOM 785 C C . MET A 1 101 ? 9.354 -5.822 37.005 1.00 16.95 ? 101 MET A C 1 ATOM 786 O O . MET A 1 101 ? 8.987 -5.062 36.076 1.00 18.42 ? 101 MET A O 1 ATOM 787 C CB . MET A 1 101 ? 7.684 -7.197 38.360 1.00 15.76 ? 101 MET A CB 1 ATOM 788 C CG . MET A 1 101 ? 6.613 -6.116 38.356 1.00 15.25 ? 101 MET A CG 1 ATOM 789 S SD . MET A 1 101 ? 7.167 -4.476 38.795 1.00 18.17 ? 101 MET A SD 1 ATOM 790 C CE . MET A 1 101 ? 7.448 -4.563 40.553 1.00 21.62 ? 101 MET A CE 1 ATOM 791 N N . GLN A 1 102 ? 10.271 -5.486 37.885 1.00 14.47 ? 102 GLN A N 1 ATOM 792 C CA . GLN A 1 102 ? 10.692 -4.109 37.995 1.00 14.37 ? 102 GLN A CA 1 ATOM 793 C C . GLN A 1 102 ? 11.544 -3.688 36.825 1.00 14.61 ? 102 GLN A C 1 ATOM 794 O O . GLN A 1 102 ? 11.502 -2.533 36.437 1.00 14.59 ? 102 GLN A O 1 ATOM 795 C CB . GLN A 1 102 ? 11.500 -3.883 39.278 1.00 14.80 ? 102 GLN A CB 1 ATOM 796 C CG . GLN A 1 102 ? 11.776 -2.383 39.536 1.00 16.25 ? 102 GLN A CG 1 ATOM 797 C CD . GLN A 1 102 ? 10.486 -1.602 39.613 1.00 18.60 ? 102 GLN A CD 1 ATOM 798 O OE1 . GLN A 1 102 ? 9.683 -1.813 40.550 1.00 21.72 ? 102 GLN A OE1 1 ATOM 799 N NE2 . GLN A 1 102 ? 10.219 -0.756 38.604 1.00 20.05 ? 102 GLN A NE2 1 ATOM 800 N N . TRP A 1 103 ? 12.372 -4.605 36.311 1.00 14.18 ? 103 TRP A N 1 ATOM 801 C CA . TRP A 1 103 ? 13.197 -4.305 35.144 1.00 15.37 ? 103 TRP A CA 1 ATOM 802 C C . TRP A 1 103 ? 12.264 -4.070 33.900 1.00 15.30 ? 103 TRP A C 1 ATOM 803 O O . TRP A 1 103 ? 12.502 -3.240 33.069 1.00 17.22 ? 103 TRP A O 1 ATOM 804 C CB . TRP A 1 103 ? 14.234 -5.420 34.858 1.00 14.18 ? 103 TRP A CB 1 ATOM 805 C CG . TRP A 1 103 ? 15.216 -4.965 33.794 1.00 16.30 ? 103 TRP A CG 1 ATOM 806 C CD1 . TRP A 1 103 ? 15.306 -5.411 32.464 1.00 17.89 ? 103 TRP A CD1 1 ATOM 807 C CD2 . TRP A 1 103 ? 16.204 -3.967 33.923 1.00 17.65 ? 103 TRP A CD2 1 ATOM 808 N NE1 . TRP A 1 103 ? 16.258 -4.722 31.797 1.00 15.77 ? 103 TRP A NE1 1 ATOM 809 C CE2 . TRP A 1 103 ? 16.839 -3.834 32.659 1.00 17.33 ? 103 TRP A CE2 1 ATOM 810 C CE3 . TRP A 1 103 ? 16.614 -3.139 34.983 1.00 19.24 ? 103 TRP A CE3 1 ATOM 811 C CZ2 . TRP A 1 103 ? 17.851 -2.937 32.441 1.00 16.86 ? 103 TRP A CZ2 1 ATOM 812 C CZ3 . TRP A 1 103 ? 17.598 -2.216 34.761 1.00 20.05 ? 103 TRP A CZ3 1 ATOM 813 C CH2 . TRP A 1 103 ? 18.234 -2.146 33.501 1.00 18.69 ? 103 TRP A CH2 1 ATOM 814 N N . GLY A 1 104 ? 11.231 -4.845 33.786 1.00 15.18 ? 104 GLY A N 1 ATOM 815 C CA . GLY A 1 104 ? 10.233 -4.569 32.786 1.00 15.44 ? 104 GLY A CA 1 ATOM 816 C C . GLY A 1 104 ? 9.690 -3.163 32.759 1.00 14.86 ? 104 GLY A C 1 ATOM 817 O O . GLY A 1 104 ? 9.564 -2.591 31.697 1.00 15.52 ? 104 GLY A O 1 ATOM 818 N N . GLN A 1 105 ? 9.316 -2.612 33.915 1.00 13.90 ? 105 GLN A N 1 ATOM 819 C CA . GLN A 1 105 ? 8.736 -1.297 33.931 1.00 14.01 ? 105 GLN A CA 1 ATOM 820 C C . GLN A 1 105 ? 9.812 -0.284 33.523 1.00 14.36 ? 105 GLN A C 1 ATOM 821 O O . GLN A 1 105 ? 9.563 0.703 32.826 1.00 14.09 ? 105 GLN A O 1 ATOM 822 C CB . GLN A 1 105 ? 8.134 -0.992 35.320 1.00 13.08 ? 105 GLN A CB 1 ATOM 823 C CG . GLN A 1 105 ? 7.493 0.374 35.378 1.00 13.31 ? 105 GLN A CG 1 ATOM 824 C CD . GLN A 1 105 ? 6.921 0.685 36.780 1.00 13.35 ? 105 GLN A CD 1 ATOM 825 O OE1 . GLN A 1 105 ? 7.569 0.367 37.843 1.00 12.96 ? 105 GLN A OE1 1 ATOM 826 N NE2 . GLN A 1 105 ? 5.816 1.384 36.812 1.00 11.18 ? 105 GLN A NE2 1 ATOM 827 N N . ILE A 1 106 ? 11.014 -0.525 33.997 1.00 16.82 ? 106 ILE A N 1 ATOM 828 C CA . ILE A 1 106 ? 12.213 0.247 33.582 1.00 15.76 ? 106 ILE A CA 1 ATOM 829 C C . ILE A 1 106 ? 12.442 0.286 32.044 1.00 16.30 ? 106 ILE A C 1 ATOM 830 O O . ILE A 1 106 ? 12.548 1.359 31.484 1.00 15.97 ? 106 ILE A O 1 ATOM 831 C CB . ILE A 1 106 ? 13.445 -0.212 34.356 1.00 17.99 ? 106 ILE A CB 1 ATOM 832 C CG1 . ILE A 1 106 ? 13.343 0.394 35.763 1.00 17.69 ? 106 ILE A CG1 1 ATOM 833 C CG2 . ILE A 1 106 ? 14.769 0.108 33.626 1.00 16.67 ? 106 ILE A CG2 1 ATOM 834 C CD1 . ILE A 1 106 ? 13.803 1.816 35.857 1.00 16.78 ? 106 ILE A CD1 1 ATOM 835 N N . VAL A 1 107 ? 12.516 -0.864 31.418 1.00 17.09 ? 107 VAL A N 1 ATOM 836 C CA . VAL A 1 107 ? 12.712 -0.950 29.975 1.00 18.52 ? 107 VAL A CA 1 ATOM 837 C C . VAL A 1 107 ? 11.505 -0.294 29.245 1.00 16.55 ? 107 VAL A C 1 ATOM 838 O O . VAL A 1 107 ? 11.679 0.513 28.319 1.00 14.84 ? 107 VAL A O 1 ATOM 839 C CB . VAL A 1 107 ? 12.818 -2.408 29.521 1.00 19.33 ? 107 VAL A CB 1 ATOM 840 C CG1 . VAL A 1 107 ? 12.863 -2.488 27.980 1.00 21.01 ? 107 VAL A CG1 1 ATOM 841 C CG2 . VAL A 1 107 ? 14.034 -3.089 30.124 1.00 18.14 ? 107 VAL A CG2 1 ATOM 842 N N . ASP A 1 108 ? 10.299 -0.547 29.754 1.00 13.60 ? 108 ASP A N 1 ATOM 843 C CA . ASP A 1 108 ? 9.138 0.035 29.173 1.00 13.34 ? 108 ASP A CA 1 ATOM 844 C C . ASP A 1 108 ? 9.256 1.559 29.133 1.00 14.22 ? 108 ASP A C 1 ATOM 845 O O . ASP A 1 108 ? 8.881 2.150 28.146 1.00 12.98 ? 108 ASP A O 1 ATOM 846 C CB . ASP A 1 108 ? 7.882 -0.363 29.968 1.00 14.77 ? 108 ASP A CB 1 ATOM 847 C CG . ASP A 1 108 ? 6.650 0.244 29.446 1.00 15.99 ? 108 ASP A CG 1 ATOM 848 O OD1 . ASP A 1 108 ? 6.449 1.474 29.623 1.00 14.60 ? 108 ASP A OD1 1 ATOM 849 O OD2 . ASP A 1 108 ? 5.824 -0.536 28.880 1.00 18.12 ? 108 ASP A OD2 1 ATOM 850 N N . HIS A 1 109 ? 9.785 2.185 30.184 1.00 13.95 ? 109 HIS A N 1 ATOM 851 C CA . HIS A 1 109 ? 9.849 3.659 30.264 1.00 14.83 ? 109 HIS A CA 1 ATOM 852 C C . HIS A 1 109 ? 10.981 4.251 29.424 1.00 14.93 ? 109 HIS A C 1 ATOM 853 O O . HIS A 1 109 ? 10.914 5.425 29.046 1.00 14.38 ? 109 HIS A O 1 ATOM 854 C CB . HIS A 1 109 ? 9.994 4.105 31.738 1.00 15.06 ? 109 HIS A CB 1 ATOM 855 C CG . HIS A 1 109 ? 8.744 3.874 32.504 1.00 16.32 ? 109 HIS A CG 1 ATOM 856 N ND1 . HIS A 1 109 ? 8.537 4.313 33.786 1.00 18.57 ? 109 HIS A ND1 1 ATOM 857 C CD2 . HIS A 1 109 ? 7.630 3.210 32.144 1.00 16.30 ? 109 HIS A CD2 1 ATOM 858 C CE1 . HIS A 1 109 ? 7.324 3.970 34.173 1.00 15.99 ? 109 HIS A CE1 1 ATOM 859 N NE2 . HIS A 1 109 ? 6.757 3.282 33.193 1.00 16.64 ? 109 HIS A NE2 1 ATOM 860 N N . ASP A 1 110 ? 12.002 3.445 29.177 1.00 14.42 ? 110 ASP A N 1 ATOM 861 C CA . ASP A 1 110 ? 13.076 3.801 28.224 1.00 16.03 ? 110 ASP A CA 1 ATOM 862 C C . ASP A 1 110 ? 12.423 3.897 26.833 1.00 16.46 ? 110 ASP A C 1 ATOM 863 O O . ASP A 1 110 ? 12.596 4.917 26.100 1.00 19.60 ? 110 ASP A O 1 ATOM 864 C CB . ASP A 1 110 ? 14.183 2.738 28.253 1.00 17.57 ? 110 ASP A CB 1 ATOM 865 C CG . ASP A 1 110 ? 15.508 3.221 27.642 1.00 19.85 ? 110 ASP A CG 1 ATOM 866 O OD1 . ASP A 1 110 ? 15.492 3.811 26.515 1.00 20.68 ? 110 ASP A OD1 1 ATOM 867 O OD2 . ASP A 1 110 ? 16.554 2.999 28.307 1.00 18.46 ? 110 ASP A OD2 1 ATOM 868 N N . LEU A 1 111 ? 11.555 2.950 26.517 1.00 15.11 ? 111 LEU A N 1 ATOM 869 C CA . LEU A 1 111 ? 10.969 2.851 25.152 1.00 14.76 ? 111 LEU A CA 1 ATOM 870 C C . LEU A 1 111 ? 9.757 3.650 24.791 1.00 16.45 ? 111 LEU A C 1 ATOM 871 O O . LEU A 1 111 ? 9.660 4.075 23.633 1.00 13.83 ? 111 LEU A O 1 ATOM 872 C CB . LEU A 1 111 ? 10.660 1.410 24.808 1.00 13.66 ? 111 LEU A CB 1 ATOM 873 C CG . LEU A 1 111 ? 11.823 0.452 25.017 1.00 14.33 ? 111 LEU A CG 1 ATOM 874 C CD1 . LEU A 1 111 ? 11.367 -0.939 24.783 1.00 13.79 ? 111 LEU A CD1 1 ATOM 875 C CD2 . LEU A 1 111 ? 12.977 0.807 24.067 1.00 14.21 ? 111 LEU A CD2 1 ATOM 876 N N . ASP A 1 112 ? 8.789 3.823 25.713 1.00 16.34 ? 112 ASP A N 1 ATOM 877 C CA . ASP A 1 112 ? 7.561 4.510 25.315 1.00 16.78 ? 112 ASP A CA 1 ATOM 878 C C . ASP A 1 112 ? 6.855 5.293 26.430 1.00 18.52 ? 112 ASP A C 1 ATOM 879 O O . ASP A 1 112 ? 6.815 4.869 27.583 1.00 17.49 ? 112 ASP A O 1 ATOM 880 C CB . ASP A 1 112 ? 6.616 3.573 24.591 1.00 17.56 ? 112 ASP A CB 1 ATOM 881 C CG . ASP A 1 112 ? 6.345 2.239 25.340 1.00 18.58 ? 112 ASP A CG 1 ATOM 882 O OD1 . ASP A 1 112 ? 5.295 2.098 26.062 1.00 20.79 ? 112 ASP A OD1 1 ATOM 883 O OD2 . ASP A 1 112 ? 7.110 1.296 25.086 1.00 19.72 ? 112 ASP A OD2 1 ATOM 884 N N . PHE A 1 113 ? 6.312 6.425 26.046 1.00 18.41 ? 113 PHE A N 1 ATOM 885 C CA . PHE A 1 113 ? 5.383 7.214 26.850 1.00 19.26 ? 113 PHE A CA 1 ATOM 886 C C . PHE A 1 113 ? 4.425 8.011 25.950 1.00 19.54 ? 113 PHE A C 1 ATOM 887 O O . PHE A 1 113 ? 4.842 8.935 25.257 1.00 18.76 ? 113 PHE A O 1 ATOM 888 C CB . PHE A 1 113 ? 6.141 8.171 27.752 1.00 20.86 ? 113 PHE A CB 1 ATOM 889 C CG . PHE A 1 113 ? 5.287 8.983 28.670 1.00 23.22 ? 113 PHE A CG 1 ATOM 890 C CD1 . PHE A 1 113 ? 4.151 8.477 29.222 1.00 24.89 ? 113 PHE A CD1 1 ATOM 891 C CD2 . PHE A 1 113 ? 5.693 10.234 29.055 1.00 26.93 ? 113 PHE A CD2 1 ATOM 892 C CE1 . PHE A 1 113 ? 3.394 9.220 30.109 1.00 27.12 ? 113 PHE A CE1 1 ATOM 893 C CE2 . PHE A 1 113 ? 4.944 11.006 29.927 1.00 28.40 ? 113 PHE A CE2 1 ATOM 894 C CZ . PHE A 1 113 ? 3.790 10.495 30.474 1.00 27.73 ? 113 PHE A CZ 1 ATOM 895 N N . ALA A 1 114 ? 3.155 7.656 25.981 1.00 18.55 ? 114 ALA A N 1 ATOM 896 C CA . ALA A 1 114 ? 2.099 8.410 25.318 1.00 20.60 ? 114 ALA A CA 1 ATOM 897 C C . ALA A 1 114 ? 1.464 9.328 26.318 1.00 22.52 ? 114 ALA A C 1 ATOM 898 O O . ALA A 1 114 ? 0.622 8.887 27.069 1.00 24.67 ? 114 ALA A O 1 ATOM 899 C CB . ALA A 1 114 ? 1.056 7.503 24.699 1.00 18.99 ? 114 ALA A CB 1 ATOM 900 N N . PRO A 1 115 ? 1.886 10.600 26.342 1.00 23.92 ? 115 PRO A N 1 ATOM 901 C CA . PRO A 1 115 ? 1.364 11.512 27.318 1.00 26.66 ? 115 PRO A CA 1 ATOM 902 C C . PRO A 1 115 ? -0.107 11.796 27.104 1.00 29.43 ? 115 PRO A C 1 ATOM 903 O O . PRO A 1 115 ? -0.640 11.701 26.013 1.00 27.55 ? 115 PRO A O 1 ATOM 904 C CB . PRO A 1 115 ? 2.175 12.790 27.082 1.00 27.04 ? 115 PRO A CB 1 ATOM 905 C CG . PRO A 1 115 ? 2.513 12.750 25.641 1.00 30.21 ? 115 PRO A CG 1 ATOM 906 C CD . PRO A 1 115 ? 2.769 11.274 25.380 1.00 27.83 ? 115 PRO A CD 1 ATOM 907 N N . GLU A 1 116 ? -0.700 12.257 28.173 1.00 36.05 ? 116 GLU A N 1 ATOM 908 C CA . GLU A 1 116 ? -2.111 12.415 28.293 1.00 39.17 ? 116 GLU A CA 1 ATOM 909 C C . GLU A 1 116 ? -2.398 13.901 28.355 1.00 41.66 ? 116 GLU A C 1 ATOM 910 O O . GLU A 1 116 ? -1.471 14.723 28.309 1.00 41.25 ? 116 GLU A O 1 ATOM 911 C CB . GLU A 1 116 ? -2.455 11.730 29.575 1.00 43.31 ? 116 GLU A CB 1 ATOM 912 C CG . GLU A 1 116 ? -3.822 11.223 29.727 1.00 42.50 ? 116 GLU A CG 1 ATOM 913 C CD . GLU A 1 116 ? -4.182 11.232 31.184 1.00 45.30 ? 116 GLU A CD 1 ATOM 914 O OE1 . GLU A 1 116 ? -4.185 12.363 31.770 1.00 36.75 ? 116 GLU A OE1 1 ATOM 915 O OE2 . GLU A 1 116 ? -4.462 10.114 31.710 1.00 42.35 ? 116 GLU A OE2 1 ATOM 916 N N . THR A 1 117 ? -3.672 14.255 28.388 1.00 41.99 ? 117 THR A N 1 ATOM 917 C CA . THR A 1 117 ? -4.032 15.648 28.247 1.00 42.18 ? 117 THR A CA 1 ATOM 918 C C . THR A 1 117 ? -4.649 16.253 29.481 1.00 43.47 ? 117 THR A C 1 ATOM 919 O O . THR A 1 117 ? -5.037 17.419 29.424 1.00 49.52 ? 117 THR A O 1 ATOM 920 C CB . THR A 1 117 ? -4.961 15.841 27.026 1.00 40.26 ? 117 THR A CB 1 ATOM 921 O OG1 . THR A 1 117 ? -6.107 14.984 27.126 1.00 31.26 ? 117 THR A OG1 1 ATOM 922 C CG2 . THR A 1 117 ? -4.192 15.526 25.743 1.00 37.65 ? 117 THR A CG2 1 ATOM 923 N N . GLU A 1 118 ? -4.721 15.531 30.607 1.00 51.40 ? 118 GLU A N 1 ATOM 924 C CA . GLU A 1 118 ? -5.410 16.102 31.801 1.00 60.10 ? 118 GLU A CA 1 ATOM 925 C C . GLU A 1 118 ? -4.741 17.375 32.336 1.00 60.76 ? 118 GLU A C 1 ATOM 926 O O . GLU A 1 118 ? -5.384 18.430 32.373 1.00 52.43 ? 118 GLU A O 1 ATOM 927 C CB . GLU A 1 118 ? -5.626 15.103 32.958 1.00 58.22 ? 118 GLU A CB 1 ATOM 928 C CG . GLU A 1 118 ? -6.208 15.769 34.228 1.00 56.15 ? 118 GLU A CG 1 ATOM 929 C CD . GLU A 1 118 ? -7.236 14.929 35.016 1.00 57.87 ? 118 GLU A CD 1 ATOM 930 O OE1 . GLU A 1 118 ? -7.102 13.678 35.079 1.00 50.38 ? 118 GLU A OE1 1 ATOM 931 O OE2 . GLU A 1 118 ? -8.192 15.534 35.606 1.00 52.91 ? 118 GLU A OE2 1 ATOM 932 N N . LEU A 1 119 ? -3.481 17.278 32.758 1.00 70.58 ? 119 LEU A N 1 ATOM 933 C CA . LEU A 1 119 ? -2.754 18.441 33.309 1.00 73.89 ? 119 LEU A CA 1 ATOM 934 C C . LEU A 1 119 ? -3.014 19.703 32.471 1.00 73.26 ? 119 LEU A C 1 ATOM 935 O O . LEU A 1 119 ? -3.465 20.727 33.000 1.00 73.99 ? 119 LEU A O 1 ATOM 936 C CB . LEU A 1 119 ? -1.254 18.160 33.398 1.00 74.41 ? 119 LEU A CB 1 ATOM 937 C CG . LEU A 1 119 ? -0.425 19.295 34.027 1.00 78.96 ? 119 LEU A CG 1 ATOM 938 C CD1 . LEU A 1 119 ? -0.385 19.155 35.549 1.00 79.62 ? 119 LEU A CD1 1 ATOM 939 C CD2 . LEU A 1 119 ? 0.981 19.350 33.425 1.00 79.91 ? 119 LEU A CD2 1 ATOM 940 N N . GLY A 1 120 ? -2.783 19.604 31.161 1.00 65.73 ? 120 GLY A N 1 ATOM 941 C CA . GLY A 1 120 ? -3.004 20.732 30.254 1.00 69.57 ? 120 GLY A CA 1 ATOM 942 C C . GLY A 1 120 ? -4.450 21.146 29.970 1.00 70.85 ? 120 GLY A C 1 ATOM 943 O O . GLY A 1 120 ? -4.666 22.169 29.315 1.00 74.78 ? 120 GLY A O 1 ATOM 944 N N . SER A 1 121 ? -5.431 20.355 30.431 1.00 64.46 ? 121 SER A N 1 ATOM 945 C CA . SER A 1 121 ? -6.872 20.654 30.245 1.00 60.50 ? 121 SER A CA 1 ATOM 946 C C . SER A 1 121 ? -7.336 21.780 31.182 1.00 60.60 ? 121 SER A C 1 ATOM 947 O O . SER A 1 121 ? -6.700 22.015 32.215 1.00 51.59 ? 121 SER A O 1 ATOM 948 C CB . SER A 1 121 ? -7.742 19.409 30.531 1.00 53.34 ? 121 SER A CB 1 ATOM 949 O OG . SER A 1 121 ? -7.632 18.441 29.522 1.00 45.84 ? 121 SER A OG 1 ATOM 950 N N . SER A 1 122 ? -8.457 22.433 30.828 1.00 63.04 ? 122 SER A N 1 ATOM 951 C CA . SER A 1 122 ? -9.092 23.482 31.659 1.00 61.30 ? 122 SER A CA 1 ATOM 952 C C . SER A 1 122 ? -9.689 22.928 32.948 1.00 59.87 ? 122 SER A C 1 ATOM 953 O O . SER A 1 122 ? -10.145 21.787 32.993 1.00 59.20 ? 122 SER A O 1 ATOM 954 C CB . SER A 1 122 ? -10.212 24.181 30.889 1.00 57.91 ? 122 SER A CB 1 ATOM 955 O OG . SER A 1 122 ? -11.382 23.386 30.871 1.00 53.49 ? 122 SER A OG 1 ATOM 956 N N . GLU A 1 123 ? -9.768 23.755 33.963 1.00 60.39 ? 123 GLU A N 1 ATOM 957 C CA . GLU A 1 123 ? -10.291 23.281 35.219 1.00 60.58 ? 123 GLU A CA 1 ATOM 958 C C . GLU A 1 123 ? -11.711 22.812 35.047 1.00 58.45 ? 123 GLU A C 1 ATOM 959 O O . GLU A 1 123 ? -12.137 21.859 35.664 1.00 63.86 ? 123 GLU A O 1 ATOM 960 C CB . GLU A 1 123 ? -10.229 24.368 36.258 1.00 62.99 ? 123 GLU A CB 1 ATOM 961 C CG . GLU A 1 123 ? -10.737 23.925 37.606 1.00 61.19 ? 123 GLU A CG 1 ATOM 962 C CD . GLU A 1 123 ? -9.889 22.838 38.206 1.00 60.39 ? 123 GLU A CD 1 ATOM 963 O OE1 . GLU A 1 123 ? -8.822 22.543 37.674 1.00 51.86 ? 123 GLU A OE1 1 ATOM 964 O OE2 . GLU A 1 123 ? -10.306 22.298 39.228 1.00 66.27 ? 123 GLU A OE2 1 ATOM 965 N N . HIS A 1 124 ? -12.460 23.505 34.226 1.00 55.16 ? 124 HIS A N 1 ATOM 966 C CA . HIS A 1 124 ? -13.830 23.114 33.935 1.00 59.97 ? 124 HIS A CA 1 ATOM 967 C C . HIS A 1 124 ? -13.911 21.674 33.397 1.00 54.13 ? 124 HIS A C 1 ATOM 968 O O . HIS A 1 124 ? -14.720 20.869 33.886 1.00 46.40 ? 124 HIS A O 1 ATOM 969 C CB . HIS A 1 124 ? -14.489 24.070 32.936 1.00 65.68 ? 124 HIS A CB 1 ATOM 970 C CG . HIS A 1 124 ? -15.950 23.778 32.735 1.00 72.78 ? 124 HIS A CG 1 ATOM 971 N ND1 . HIS A 1 124 ? -16.488 23.368 31.531 1.00 72.14 ? 124 HIS A ND1 1 ATOM 972 C CD2 . HIS A 1 124 ? -16.975 23.788 33.622 1.00 74.94 ? 124 HIS A CD2 1 ATOM 973 C CE1 . HIS A 1 124 ? -17.787 23.165 31.680 1.00 74.81 ? 124 HIS A CE1 1 ATOM 974 N NE2 . HIS A 1 124 ? -18.107 23.414 32.939 1.00 75.39 ? 124 HIS A NE2 1 ATOM 975 N N . SER A 1 125 ? -13.065 21.368 32.410 1.00 49.48 ? 125 SER A N 1 ATOM 976 C CA . SER A 1 125 ? -13.058 20.064 31.768 1.00 48.90 ? 125 SER A CA 1 ATOM 977 C C . SER A 1 125 ? -12.745 18.997 32.806 1.00 45.98 ? 125 SER A C 1 ATOM 978 O O . SER A 1 125 ? -13.450 17.964 32.914 1.00 41.36 ? 125 SER A O 1 ATOM 979 C CB . SER A 1 125 ? -12.061 20.033 30.603 1.00 53.33 ? 125 SER A CB 1 ATOM 980 O OG . SER A 1 125 ? -12.178 18.833 29.840 1.00 53.42 ? 125 SER A OG 1 ATOM 981 N N . LYS A 1 126 ? -11.759 19.279 33.647 1.00 42.70 ? 126 LYS A N 1 ATOM 982 C CA . LYS A 1 126 ? -11.382 18.350 34.700 1.00 37.54 ? 126 LYS A CA 1 ATOM 983 C C . LYS A 1 126 ? -12.549 18.114 35.657 1.00 38.57 ? 126 LYS A C 1 ATOM 984 O O . LYS A 1 126 ? -12.765 16.990 36.110 1.00 36.17 ? 126 LYS A O 1 ATOM 985 C CB . LYS A 1 126 ? -10.168 18.875 35.469 1.00 42.50 ? 126 LYS A CB 1 ATOM 986 C CG . LYS A 1 126 ? -8.900 18.972 34.637 1.00 42.84 ? 126 LYS A CG 1 ATOM 987 C CD . LYS A 1 126 ? -8.072 20.184 35.033 1.00 44.18 ? 126 LYS A CD 1 ATOM 988 C CE . LYS A 1 126 ? -6.581 19.860 35.041 1.00 48.24 ? 126 LYS A CE 1 ATOM 989 N NZ . LYS A 1 126 ? -5.795 20.836 34.237 1.00 49.75 ? 126 LYS A NZ 1 ATOM 990 N N . VAL A 1 127 ? -13.298 19.169 35.968 1.00 36.57 ? 127 VAL A N 1 ATOM 991 C CA . VAL A 1 127 ? -14.396 19.047 36.903 1.00 36.70 ? 127 VAL A CA 1 ATOM 992 C C . VAL A 1 127 ? -15.539 18.315 36.269 1.00 34.34 ? 127 VAL A C 1 ATOM 993 O O . VAL A 1 127 ? -16.100 17.404 36.878 1.00 32.41 ? 127 VAL A O 1 ATOM 994 C CB . VAL A 1 127 ? -14.815 20.442 37.500 1.00 44.28 ? 127 VAL A CB 1 ATOM 995 C CG1 . VAL A 1 127 ? -16.281 20.458 37.956 1.00 44.29 ? 127 VAL A CG1 1 ATOM 996 C CG2 . VAL A 1 127 ? -13.870 20.806 38.668 1.00 37.09 ? 127 VAL A CG2 1 ATOM 997 N N . GLN A 1 128 ? -15.830 18.633 35.022 1.00 33.65 ? 128 GLN A N 1 ATOM 998 C CA . GLN A 1 128 ? -16.871 17.907 34.326 1.00 41.49 ? 128 GLN A CA 1 ATOM 999 C C . GLN A 1 128 ? -16.568 16.408 34.289 1.00 35.58 ? 128 GLN A C 1 ATOM 1000 O O . GLN A 1 128 ? -17.486 15.593 34.321 1.00 39.14 ? 128 GLN A O 1 ATOM 1001 C CB . GLN A 1 128 ? -17.029 18.396 32.889 1.00 43.79 ? 128 GLN A CB 1 ATOM 1002 C CG . GLN A 1 128 ? -17.650 19.791 32.803 1.00 48.84 ? 128 GLN A CG 1 ATOM 1003 C CD . GLN A 1 128 ? -19.014 19.908 33.472 1.00 56.17 ? 128 GLN A CD 1 ATOM 1004 O OE1 . GLN A 1 128 ? -19.107 20.192 34.674 1.00 62.93 ? 128 GLN A OE1 1 ATOM 1005 N NE2 . GLN A 1 128 ? -20.076 19.743 32.695 1.00 57.88 ? 128 GLN A NE2 1 ATOM 1006 N N . CYS A 1 129 ? -15.296 16.074 34.172 1.00 30.64 ? 129 CYS A N 1 ATOM 1007 C CA . CYS A 1 129 ? -14.903 14.703 33.954 1.00 26.46 ? 129 CYS A CA 1 ATOM 1008 C C . CYS A 1 129 ? -14.936 13.993 35.280 1.00 28.57 ? 129 CYS A C 1 ATOM 1009 O O . CYS A 1 129 ? -15.542 12.921 35.371 1.00 25.82 ? 129 CYS A O 1 ATOM 1010 C CB . CYS A 1 129 ? -13.510 14.618 33.316 1.00 26.34 ? 129 CYS A CB 1 ATOM 1011 S SG . CYS A 1 129 ? -13.274 13.103 32.429 1.00 23.98 ? 129 CYS A SG 1 ATOM 1012 N N . GLU A 1 130 ? -14.291 14.567 36.313 1.00 28.91 ? 130 GLU A N 1 ATOM 1013 C CA . GLU A 1 130 ? -14.249 13.858 37.577 1.00 33.06 ? 130 GLU A CA 1 ATOM 1014 C C . GLU A 1 130 ? -15.590 13.965 38.308 1.00 30.92 ? 130 GLU A C 1 ATOM 1015 O O . GLU A 1 130 ? -16.132 12.948 38.747 1.00 30.04 ? 130 GLU A O 1 ATOM 1016 C CB . GLU A 1 130 ? -13.088 14.259 38.498 1.00 32.81 ? 130 GLU A CB 1 ATOM 1017 C CG . GLU A 1 130 ? -13.042 13.390 39.776 1.00 34.85 ? 130 GLU A CG 1 ATOM 1018 C CD . GLU A 1 130 ? -11.641 13.234 40.428 1.00 38.04 ? 130 GLU A CD 1 ATOM 1019 O OE1 . GLU A 1 130 ? -10.827 14.192 40.350 1.00 35.01 ? 130 GLU A OE1 1 ATOM 1020 O OE2 . GLU A 1 130 ? -11.362 12.148 41.033 1.00 35.14 ? 130 GLU A OE2 1 ATOM 1021 N N . GLU A 1 131 ? -16.050 15.177 38.539 1.00 31.81 ? 131 GLU A N 1 ATOM 1022 C CA . GLU A 1 131 ? -17.264 15.436 39.306 1.00 39.05 ? 131 GLU A CA 1 ATOM 1023 C C . GLU A 1 131 ? -18.537 14.968 38.659 1.00 33.77 ? 131 GLU A C 1 ATOM 1024 O O . GLU A 1 131 ? -19.398 14.485 39.320 1.00 34.31 ? 131 GLU A O 1 ATOM 1025 C CB . GLU A 1 131 ? -17.382 16.899 39.744 1.00 41.96 ? 131 GLU A CB 1 ATOM 1026 C CG . GLU A 1 131 ? -16.062 17.498 40.182 1.00 49.82 ? 131 GLU A CG 1 ATOM 1027 C CD . GLU A 1 131 ? -16.149 18.596 41.228 1.00 55.76 ? 131 GLU A CD 1 ATOM 1028 O OE1 . GLU A 1 131 ? -15.213 18.700 42.035 1.00 63.54 ? 131 GLU A OE1 1 ATOM 1029 O OE2 . GLU A 1 131 ? -17.111 19.357 41.236 1.00 58.34 ? 131 GLU A OE2 1 ATOM 1030 N N . TYR A 1 132 ? -18.646 15.143 37.367 1.00 28.56 ? 132 TYR A N 1 ATOM 1031 C CA . TYR A 1 132 ? -19.915 14.884 36.695 1.00 28.98 ? 132 TYR A CA 1 ATOM 1032 C C . TYR A 1 132 ? -19.879 13.725 35.701 1.00 26.85 ? 132 TYR A C 1 ATOM 1033 O O . TYR A 1 132 ? -20.886 13.375 35.173 1.00 25.96 ? 132 TYR A O 1 ATOM 1034 C CB . TYR A 1 132 ? -20.394 16.153 36.013 1.00 31.00 ? 132 TYR A CB 1 ATOM 1035 C CG . TYR A 1 132 ? -20.702 17.186 37.053 1.00 34.98 ? 132 TYR A CG 1 ATOM 1036 C CD1 . TYR A 1 132 ? -21.848 17.067 37.844 1.00 36.07 ? 132 TYR A CD1 1 ATOM 1037 C CD2 . TYR A 1 132 ? -19.836 18.250 37.286 1.00 36.34 ? 132 TYR A CD2 1 ATOM 1038 C CE1 . TYR A 1 132 ? -22.113 17.972 38.851 1.00 41.57 ? 132 TYR A CE1 1 ATOM 1039 C CE2 . TYR A 1 132 ? -20.108 19.192 38.267 1.00 44.46 ? 132 TYR A CE2 1 ATOM 1040 C CZ . TYR A 1 132 ? -21.256 19.040 39.050 1.00 42.63 ? 132 TYR A CZ 1 ATOM 1041 O OH . TYR A 1 132 ? -21.538 19.965 40.031 1.00 43.02 ? 132 TYR A OH 1 ATOM 1042 N N . CYS A 1 133 ? -18.730 13.113 35.477 1.00 23.99 ? 133 CYS A N 1 ATOM 1043 C CA . CYS A 1 133 ? -18.684 11.926 34.617 1.00 24.33 ? 133 CYS A CA 1 ATOM 1044 C C . CYS A 1 133 ? -19.292 12.206 33.233 1.00 23.07 ? 133 CYS A C 1 ATOM 1045 O O . CYS A 1 133 ? -19.859 11.342 32.628 1.00 24.96 ? 133 CYS A O 1 ATOM 1046 C CB . CYS A 1 133 ? -19.339 10.713 35.318 1.00 22.72 ? 133 CYS A CB 1 ATOM 1047 S SG . CYS A 1 133 ? -18.495 10.253 36.864 1.00 26.52 ? 133 CYS A SG 1 ATOM 1048 N N . VAL A 1 134 ? -19.049 13.399 32.720 1.00 24.29 ? 134 VAL A N 1 ATOM 1049 C CA . VAL A 1 134 ? -19.586 13.849 31.480 1.00 24.73 ? 134 VAL A CA 1 ATOM 1050 C C . VAL A 1 134 ? -18.636 13.633 30.326 1.00 24.03 ? 134 VAL A C 1 ATOM 1051 O O . VAL A 1 134 ? -17.583 14.262 30.241 1.00 26.71 ? 134 VAL A O 1 ATOM 1052 C CB . VAL A 1 134 ? -19.946 15.324 31.569 1.00 30.47 ? 134 VAL A CB 1 ATOM 1053 C CG1 . VAL A 1 134 ? -20.282 15.870 30.182 1.00 33.48 ? 134 VAL A CG1 1 ATOM 1054 C CG2 . VAL A 1 134 ? -21.155 15.489 32.511 1.00 30.84 ? 134 VAL A CG2 1 ATOM 1055 N N . GLN A 1 135 ? -19.015 12.722 29.448 1.00 22.08 ? 135 GLN A N 1 ATOM 1056 C CA . GLN A 1 135 ? -18.226 12.400 28.257 1.00 23.75 ? 135 GLN A CA 1 ATOM 1057 C C . GLN A 1 135 ? -18.203 13.514 27.244 1.00 24.66 ? 135 GLN A C 1 ATOM 1058 O O . GLN A 1 135 ? -19.223 14.033 26.917 1.00 27.14 ? 135 GLN A O 1 ATOM 1059 C CB . GLN A 1 135 ? -18.746 11.131 27.623 1.00 22.36 ? 135 GLN A CB 1 ATOM 1060 C CG . GLN A 1 135 ? -17.889 10.732 26.452 1.00 24.47 ? 135 GLN A CG 1 ATOM 1061 C CD . GLN A 1 135 ? -18.298 9.384 25.917 1.00 22.51 ? 135 GLN A CD 1 ATOM 1062 O OE1 . GLN A 1 135 ? -17.968 8.353 26.486 1.00 23.24 ? 135 GLN A OE1 1 ATOM 1063 N NE2 . GLN A 1 135 ? -19.113 9.410 24.872 1.00 22.63 ? 135 GLN A NE2 1 ATOM 1064 N N . GLY A 1 136 ? -17.022 13.894 26.756 1.00 26.26 ? 136 GLY A N 1 ATOM 1065 C CA . GLY A 1 136 ? -16.919 14.944 25.718 1.00 22.98 ? 136 GLY A CA 1 ATOM 1066 C C . GLY A 1 136 ? -15.521 15.452 25.595 1.00 22.71 ? 136 GLY A C 1 ATOM 1067 O O . GLY A 1 136 ? -14.801 15.542 26.618 1.00 21.85 ? 136 GLY A O 1 ATOM 1068 N N . ASP A 1 137 ? -15.087 15.797 24.356 1.00 23.89 ? 137 ASP A N 1 ATOM 1069 C CA . ASP A 1 137 ? -13.745 16.304 24.154 1.00 26.98 ? 137 ASP A CA 1 ATOM 1070 C C . ASP A 1 137 ? -12.668 15.326 24.731 1.00 27.30 ? 137 ASP A C 1 ATOM 1071 O O . ASP A 1 137 ? -12.620 14.195 24.281 1.00 27.53 ? 137 ASP A O 1 ATOM 1072 C CB . ASP A 1 137 ? -13.613 17.691 24.772 1.00 28.93 ? 137 ASP A CB 1 ATOM 1073 C CG . ASP A 1 137 ? -14.377 18.760 23.999 1.00 33.65 ? 137 ASP A CG 1 ATOM 1074 O OD1 . ASP A 1 137 ? -14.792 18.547 22.842 1.00 39.56 ? 137 ASP A OD1 1 ATOM 1075 O OD2 . ASP A 1 137 ? -14.489 19.861 24.527 1.00 38.01 ? 137 ASP A OD2 1 ATOM 1076 N N . GLU A 1 138 ? -11.769 15.630 25.498 1.00 26.33 ? 138 GLU A N 1 ATOM 1077 C CA . GLU A 1 138 ? -10.726 14.757 26.058 1.00 28.18 ? 138 GLU A CA 1 ATOM 1078 C C . GLU A 1 138 ? -11.206 13.849 27.178 1.00 23.18 ? 138 GLU A C 1 ATOM 1079 O O . GLU A 1 138 ? -10.534 12.915 27.489 1.00 23.19 ? 138 GLU A O 1 ATOM 1080 C CB . GLU A 1 138 ? -9.521 15.552 26.596 1.00 33.63 ? 138 GLU A CB 1 ATOM 1081 C CG . GLU A 1 138 ? -8.689 16.265 25.547 1.00 37.92 ? 138 GLU A CG 1 ATOM 1082 C CD . GLU A 1 138 ? -8.481 15.421 24.325 1.00 40.23 ? 138 GLU A CD 1 ATOM 1083 O OE1 . GLU A 1 138 ? -7.444 14.726 24.205 1.00 60.83 ? 138 GLU A OE1 1 ATOM 1084 O OE2 . GLU A 1 138 ? -9.371 15.446 23.448 1.00 52.18 ? 138 GLU A OE2 1 ATOM 1085 N N . CYS A 1 139 ? -12.342 14.139 27.780 1.00 21.59 ? 139 CYS A N 1 ATOM 1086 C CA . CYS A 1 139 ? -12.914 13.276 28.834 1.00 22.47 ? 139 CYS A CA 1 ATOM 1087 C C . CYS A 1 139 ? -13.672 12.043 28.320 1.00 20.33 ? 139 CYS A C 1 ATOM 1088 O O . CYS A 1 139 ? -14.722 12.184 27.684 1.00 19.84 ? 139 CYS A O 1 ATOM 1089 C CB . CYS A 1 139 ? -13.838 14.134 29.707 1.00 22.59 ? 139 CYS A CB 1 ATOM 1090 S SG . CYS A 1 139 ? -14.663 13.206 30.972 1.00 25.67 ? 139 CYS A SG 1 ATOM 1091 N N . PHE A 1 140 ? -13.153 10.846 28.593 1.00 18.22 ? 140 PHE A N 1 ATOM 1092 C CA . PHE A 1 140 ? -13.718 9.589 28.123 1.00 19.03 ? 140 PHE A CA 1 ATOM 1093 C C . PHE A 1 140 ? -13.827 8.731 29.368 1.00 20.58 ? 140 PHE A C 1 ATOM 1094 O O . PHE A 1 140 ? -13.019 7.834 29.599 1.00 19.00 ? 140 PHE A O 1 ATOM 1095 C CB . PHE A 1 140 ? -12.780 8.966 27.047 1.00 19.09 ? 140 PHE A CB 1 ATOM 1096 C CG . PHE A 1 140 ? -13.253 7.660 26.422 1.00 18.60 ? 140 PHE A CG 1 ATOM 1097 C CD1 . PHE A 1 140 ? -14.573 7.365 26.237 1.00 19.79 ? 140 PHE A CD1 1 ATOM 1098 C CD2 . PHE A 1 140 ? -12.311 6.746 25.946 1.00 18.82 ? 140 PHE A CD2 1 ATOM 1099 C CE1 . PHE A 1 140 ? -14.947 6.164 25.648 1.00 18.20 ? 140 PHE A CE1 1 ATOM 1100 C CE2 . PHE A 1 140 ? -12.676 5.561 25.345 1.00 18.19 ? 140 PHE A CE2 1 ATOM 1101 C CZ . PHE A 1 140 ? -13.994 5.267 25.179 1.00 16.30 ? 140 PHE A CZ 1 ATOM 1102 N N . PRO A 1 141 ? -14.822 9.054 30.221 1.00 19.48 ? 141 PRO A N 1 ATOM 1103 C CA . PRO A 1 141 ? -14.811 8.544 31.570 1.00 18.12 ? 141 PRO A CA 1 ATOM 1104 C C . PRO A 1 141 ? -15.065 7.050 31.636 1.00 17.84 ? 141 PRO A C 1 ATOM 1105 O O . PRO A 1 141 ? -15.698 6.460 30.760 1.00 18.29 ? 141 PRO A O 1 ATOM 1106 C CB . PRO A 1 141 ? -15.906 9.360 32.275 1.00 18.78 ? 141 PRO A CB 1 ATOM 1107 C CG . PRO A 1 141 ? -16.829 9.801 31.197 1.00 18.86 ? 141 PRO A CG 1 ATOM 1108 C CD . PRO A 1 141 ? -15.930 10.006 29.978 1.00 19.07 ? 141 PRO A CD 1 ATOM 1109 N N . ILE A 1 142 ? -14.534 6.416 32.652 1.00 16.22 ? 142 ILE A N 1 ATOM 1110 C CA . ILE A 1 142 ? -14.668 4.965 32.822 1.00 15.79 ? 142 ILE A CA 1 ATOM 1111 C C . ILE A 1 142 ? -15.872 4.795 33.766 1.00 19.27 ? 142 ILE A C 1 ATOM 1112 O O . ILE A 1 142 ? -15.746 4.977 34.979 1.00 20.23 ? 142 ILE A O 1 ATOM 1113 C CB . ILE A 1 142 ? -13.374 4.367 33.429 1.00 15.29 ? 142 ILE A CB 1 ATOM 1114 C CG1 . ILE A 1 142 ? -12.261 4.317 32.333 1.00 15.57 ? 142 ILE A CG1 1 ATOM 1115 C CG2 . ILE A 1 142 ? -13.550 2.962 34.006 1.00 13.02 ? 142 ILE A CG2 1 ATOM 1116 C CD1 . ILE A 1 142 ? -10.871 4.404 32.924 1.00 16.03 ? 142 ILE A CD1 1 ATOM 1117 N N . MET A 1 143 ? -17.014 4.430 33.205 1.00 18.10 ? 143 MET A N 1 ATOM 1118 C CA . MET A 1 143 ? -18.243 4.311 33.956 1.00 20.72 ? 143 MET A CA 1 ATOM 1119 C C . MET A 1 143 ? -18.297 3.017 34.754 1.00 16.77 ? 143 MET A C 1 ATOM 1120 O O . MET A 1 143 ? -17.863 1.993 34.307 1.00 17.78 ? 143 MET A O 1 ATOM 1121 C CB . MET A 1 143 ? -19.475 4.436 33.030 1.00 20.41 ? 143 MET A CB 1 ATOM 1122 C CG . MET A 1 143 ? -19.495 5.703 32.192 1.00 19.48 ? 143 MET A CG 1 ATOM 1123 S SD . MET A 1 143 ? -19.526 7.291 33.055 1.00 21.87 ? 143 MET A SD 1 ATOM 1124 C CE . MET A 1 143 ? -21.046 7.202 34.011 1.00 21.21 ? 143 MET A CE 1 ATOM 1125 N N . PHE A 1 144 ? -18.798 3.093 35.978 1.00 20.97 ? 144 PHE A N 1 ATOM 1126 C CA . PHE A 1 144 ? -19.002 1.886 36.807 1.00 20.62 ? 144 PHE A CA 1 ATOM 1127 C C . PHE A 1 144 ? -20.231 1.135 36.341 1.00 22.39 ? 144 PHE A C 1 ATOM 1128 O O . PHE A 1 144 ? -21.238 1.764 36.044 1.00 22.52 ? 144 PHE A O 1 ATOM 1129 C CB . PHE A 1 144 ? -19.149 2.235 38.274 1.00 21.38 ? 144 PHE A CB 1 ATOM 1130 C CG . PHE A 1 144 ? -18.008 2.990 38.837 1.00 22.72 ? 144 PHE A CG 1 ATOM 1131 C CD1 . PHE A 1 144 ? -16.723 2.761 38.396 1.00 26.37 ? 144 PHE A CD1 1 ATOM 1132 C CD2 . PHE A 1 144 ? -18.204 3.896 39.844 1.00 22.20 ? 144 PHE A CD2 1 ATOM 1133 C CE1 . PHE A 1 144 ? -15.667 3.500 38.902 1.00 26.53 ? 144 PHE A CE1 1 ATOM 1134 C CE2 . PHE A 1 144 ? -17.157 4.625 40.356 1.00 24.75 ? 144 PHE A CE2 1 ATOM 1135 C CZ . PHE A 1 144 ? -15.888 4.414 39.907 1.00 25.13 ? 144 PHE A CZ 1 ATOM 1136 N N . PRO A 1 145 ? -20.130 -0.205 36.218 1.00 23.39 ? 145 PRO A N 1 ATOM 1137 C CA . PRO A 1 145 ? -21.275 -1.008 35.955 1.00 24.26 ? 145 PRO A CA 1 ATOM 1138 C C . PRO A 1 145 ? -22.107 -1.174 37.225 1.00 28.32 ? 145 PRO A C 1 ATOM 1139 O O . PRO A 1 145 ? -21.607 -0.963 38.368 1.00 23.47 ? 145 PRO A O 1 ATOM 1140 C CB . PRO A 1 145 ? -20.687 -2.347 35.630 1.00 24.16 ? 145 PRO A CB 1 ATOM 1141 C CG . PRO A 1 145 ? -19.481 -2.409 36.519 1.00 23.01 ? 145 PRO A CG 1 ATOM 1142 C CD . PRO A 1 145 ? -18.942 -1.031 36.469 1.00 21.82 ? 145 PRO A CD 1 ATOM 1143 N N . LYS A 1 146 ? -23.375 -1.525 37.024 1.00 28.90 ? 146 LYS A N 1 ATOM 1144 C CA . LYS A 1 146 ? -24.258 -1.792 38.165 1.00 36.20 ? 146 LYS A CA 1 ATOM 1145 C C . LYS A 1 146 ? -23.654 -2.751 39.210 1.00 33.31 ? 146 LYS A C 1 ATOM 1146 O O . LYS A 1 146 ? -22.878 -3.682 38.916 1.00 33.12 ? 146 LYS A O 1 ATOM 1147 C CB . LYS A 1 146 ? -25.629 -2.304 37.718 1.00 40.30 ? 146 LYS A CB 1 ATOM 1148 C CG . LYS A 1 146 ? -25.665 -3.768 37.391 1.00 46.73 ? 146 LYS A CG 1 ATOM 1149 C CD . LYS A 1 146 ? -26.967 -4.111 36.670 1.00 51.40 ? 146 LYS A CD 1 ATOM 1150 C CE . LYS A 1 146 ? -27.374 -5.576 36.933 1.00 56.92 ? 146 LYS A CE 1 ATOM 1151 N NZ . LYS A 1 146 ? -28.611 -5.736 37.768 1.00 63.18 ? 146 LYS A NZ 1 ATOM 1152 N N . ASN A 1 147 ? -24.000 -2.510 40.451 1.00 34.33 ? 147 ASN A N 1 ATOM 1153 C CA . ASN A 1 147 ? -23.452 -3.326 41.562 1.00 34.18 ? 147 ASN A CA 1 ATOM 1154 C C . ASN A 1 147 ? -21.943 -3.147 41.857 1.00 29.53 ? 147 ASN A C 1 ATOM 1155 O O . ASN A 1 147 ? -21.436 -3.858 42.699 1.00 25.68 ? 147 ASN A O 1 ATOM 1156 C CB . ASN A 1 147 ? -23.684 -4.846 41.355 1.00 36.05 ? 147 ASN A CB 1 ATOM 1157 C CG . ASN A 1 147 ? -25.140 -5.199 41.122 1.00 41.62 ? 147 ASN A CG 1 ATOM 1158 O OD1 . ASN A 1 147 ? -25.476 -5.907 40.162 1.00 48.12 ? 147 ASN A OD1 1 ATOM 1159 N ND2 . ASN A 1 147 ? -26.006 -4.691 41.972 1.00 36.48 ? 147 ASN A ND2 1 ATOM 1160 N N . ASP A 1 148 ? -21.232 -2.259 41.162 1.00 26.95 ? 148 ASP A N 1 ATOM 1161 C CA . ASP A 1 148 ? -19.828 -2.015 41.501 1.00 23.67 ? 148 ASP A CA 1 ATOM 1162 C C . ASP A 1 148 ? -19.734 -1.420 42.901 1.00 22.37 ? 148 ASP A C 1 ATOM 1163 O O . ASP A 1 148 ? -20.336 -0.366 43.182 1.00 21.77 ? 148 ASP A O 1 ATOM 1164 C CB . ASP A 1 148 ? -19.204 -1.064 40.482 1.00 23.39 ? 148 ASP A CB 1 ATOM 1165 C CG . ASP A 1 148 ? -17.658 -1.112 40.476 1.00 26.56 ? 148 ASP A CG 1 ATOM 1166 O OD1 . ASP A 1 148 ? -17.047 -0.924 41.569 1.00 21.20 ? 148 ASP A OD1 1 ATOM 1167 O OD2 . ASP A 1 148 ? -17.099 -1.372 39.369 1.00 22.79 ? 148 ASP A OD2 1 ATOM 1168 N N . PRO A 1 149 ? -18.891 -2.007 43.742 1.00 24.18 ? 149 PRO A N 1 ATOM 1169 C CA . PRO A 1 149 ? -18.711 -1.469 45.104 1.00 24.41 ? 149 PRO A CA 1 ATOM 1170 C C . PRO A 1 149 ? -18.370 -0.030 45.113 1.00 23.16 ? 149 PRO A C 1 ATOM 1171 O O . PRO A 1 149 ? -18.821 0.722 45.980 1.00 26.67 ? 149 PRO A O 1 ATOM 1172 C CB . PRO A 1 149 ? -17.534 -2.280 45.637 1.00 24.40 ? 149 PRO A CB 1 ATOM 1173 C CG . PRO A 1 149 ? -17.695 -3.567 44.972 1.00 25.25 ? 149 PRO A CG 1 ATOM 1174 C CD . PRO A 1 149 ? -18.075 -3.222 43.556 1.00 23.93 ? 149 PRO A CD 1 ATOM 1175 N N . LYS A 1 150 ? -17.656 0.411 44.112 1.00 20.96 ? 150 LYS A N 1 ATOM 1176 C CA . LYS A 1 150 ? -17.248 1.807 44.082 1.00 20.42 ? 150 LYS A CA 1 ATOM 1177 C C . LYS A 1 150 ? -18.363 2.823 43.889 1.00 19.35 ? 150 LYS A C 1 ATOM 1178 O O . LYS A 1 150 ? -18.162 4.007 44.123 1.00 20.71 ? 150 LYS A O 1 ATOM 1179 C CB . LYS A 1 150 ? -16.166 2.031 42.986 1.00 19.49 ? 150 LYS A CB 1 ATOM 1180 C CG . LYS A 1 150 ? -14.840 1.358 43.221 1.00 20.52 ? 150 LYS A CG 1 ATOM 1181 C CD . LYS A 1 150 ? -13.846 1.710 42.090 1.00 23.25 ? 150 LYS A CD 1 ATOM 1182 C CE . LYS A 1 150 ? -12.437 1.237 42.397 1.00 23.96 ? 150 LYS A CE 1 ATOM 1183 N NZ . LYS A 1 150 ? -11.970 1.781 43.677 1.00 22.61 ? 150 LYS A NZ 1 ATOM 1184 N N . LEU A 1 151 ? -19.514 2.381 43.407 1.00 22.07 ? 151 LEU A N 1 ATOM 1185 C CA . LEU A 1 151 ? -20.697 3.206 43.407 1.00 24.47 ? 151 LEU A CA 1 ATOM 1186 C C . LEU A 1 151 ? -21.025 3.724 44.819 1.00 26.46 ? 151 LEU A C 1 ATOM 1187 O O . LEU A 1 151 ? -21.632 4.787 44.950 1.00 28.52 ? 151 LEU A O 1 ATOM 1188 C CB . LEU A 1 151 ? -21.951 2.457 42.881 1.00 24.45 ? 151 LEU A CB 1 ATOM 1189 C CG . LEU A 1 151 ? -21.862 2.046 41.429 1.00 25.41 ? 151 LEU A CG 1 ATOM 1190 C CD1 . LEU A 1 151 ? -22.882 0.941 41.106 1.00 25.04 ? 151 LEU A CD1 1 ATOM 1191 C CD2 . LEU A 1 151 ? -22.064 3.308 40.606 1.00 25.24 ? 151 LEU A CD2 1 ATOM 1192 N N . LYS A 1 152 ? -20.652 2.970 45.855 1.00 29.31 ? 152 LYS A N 1 ATOM 1193 C CA . LYS A 1 152 ? -20.967 3.378 47.240 1.00 31.54 ? 152 LYS A CA 1 ATOM 1194 C C . LYS A 1 152 ? -19.972 4.334 47.841 1.00 36.43 ? 152 LYS A C 1 ATOM 1195 O O . LYS A 1 152 ? -20.284 4.986 48.855 1.00 40.59 ? 152 LYS A O 1 ATOM 1196 C CB . LYS A 1 152 ? -21.124 2.173 48.141 1.00 32.04 ? 152 LYS A CB 1 ATOM 1197 C CG . LYS A 1 152 ? -22.377 1.397 47.876 1.00 35.46 ? 152 LYS A CG 1 ATOM 1198 C CD . LYS A 1 152 ? -22.098 -0.082 48.004 1.00 46.14 ? 152 LYS A CD 1 ATOM 1199 C CE . LYS A 1 152 ? -23.354 -0.943 47.906 1.00 47.73 ? 152 LYS A CE 1 ATOM 1200 N NZ . LYS A 1 152 ? -23.637 -1.639 49.206 1.00 51.06 ? 152 LYS A NZ 1 ATOM 1201 N N . THR A 1 153 ? -18.801 4.474 47.226 1.00 32.61 ? 153 THR A N 1 ATOM 1202 C CA . THR A 1 153 ? -17.774 5.372 47.752 1.00 33.60 ? 153 THR A CA 1 ATOM 1203 C C . THR A 1 153 ? -17.166 6.385 46.800 1.00 36.78 ? 153 THR A C 1 ATOM 1204 O O . THR A 1 153 ? -16.549 7.329 47.279 1.00 36.58 ? 153 THR A O 1 ATOM 1205 C CB . THR A 1 153 ? -16.622 4.557 48.278 1.00 37.68 ? 153 THR A CB 1 ATOM 1206 O OG1 . THR A 1 153 ? -16.220 3.619 47.275 1.00 39.97 ? 153 THR A OG1 1 ATOM 1207 C CG2 . THR A 1 153 ? -17.076 3.804 49.513 1.00 40.24 ? 153 THR A CG2 1 ATOM 1208 N N . GLN A 1 154 ? -17.332 6.222 45.476 1.00 31.22 ? 154 GLN A N 1 ATOM 1209 C CA . GLN A 1 154 ? -16.637 7.073 44.516 1.00 29.59 ? 154 GLN A CA 1 ATOM 1210 C C . GLN A 1 154 ? -17.491 7.624 43.434 1.00 31.05 ? 154 GLN A C 1 ATOM 1211 O O . GLN A 1 154 ? -16.950 8.054 42.432 1.00 36.70 ? 154 GLN A O 1 ATOM 1212 C CB . GLN A 1 154 ? -15.525 6.278 43.788 1.00 29.82 ? 154 GLN A CB 1 ATOM 1213 C CG . GLN A 1 154 ? -14.320 5.939 44.629 1.00 29.63 ? 154 GLN A CG 1 ATOM 1214 C CD . GLN A 1 154 ? -13.347 5.063 43.875 1.00 25.20 ? 154 GLN A CD 1 ATOM 1215 O OE1 . GLN A 1 154 ? -12.892 4.066 44.405 1.00 25.37 ? 154 GLN A OE1 1 ATOM 1216 N NE2 . GLN A 1 154 ? -13.033 5.423 42.659 1.00 23.15 ? 154 GLN A NE2 1 ATOM 1217 N N . GLY A 1 155 ? -18.805 7.570 43.544 1.00 27.16 ? 155 GLY A N 1 ATOM 1218 C CA . GLY A 1 155 ? -19.626 8.130 42.458 1.00 28.89 ? 155 GLY A CA 1 ATOM 1219 C C . GLY A 1 155 ? -19.863 7.166 41.311 1.00 26.77 ? 155 GLY A C 1 ATOM 1220 O O . GLY A 1 155 ? -19.914 5.960 41.508 1.00 24.21 ? 155 GLY A O 1 ATOM 1221 N N . LYS A 1 156 ? -20.036 7.717 40.117 1.00 31.94 ? 156 LYS A N 1 ATOM 1222 C CA . LYS A 1 156 ? -20.502 6.960 38.955 1.00 31.82 ? 156 LYS A CA 1 ATOM 1223 C C . LYS A 1 156 ? -19.368 6.489 38.017 1.00 28.09 ? 156 LYS A C 1 ATOM 1224 O O . LYS A 1 156 ? -19.578 5.627 37.164 1.00 30.07 ? 156 LYS A O 1 ATOM 1225 C CB . LYS A 1 156 ? -21.479 7.814 38.155 1.00 36.59 ? 156 LYS A CB 1 ATOM 1226 C CG . LYS A 1 156 ? -22.802 8.085 38.865 1.00 43.23 ? 156 LYS A CG 1 ATOM 1227 C CD . LYS A 1 156 ? -23.610 6.794 39.084 1.00 48.35 ? 156 LYS A CD 1 ATOM 1228 C CE . LYS A 1 156 ? -24.883 7.029 39.924 1.00 54.87 ? 156 LYS A CE 1 ATOM 1229 N NZ . LYS A 1 156 ? -25.124 5.957 40.951 1.00 55.15 ? 156 LYS A NZ 1 ATOM 1230 N N . CYS A 1 157 ? -18.197 7.076 38.151 1.00 24.29 ? 157 CYS A N 1 ATOM 1231 C CA . CYS A 1 157 ? -17.118 6.809 37.210 1.00 20.85 ? 157 CYS A CA 1 ATOM 1232 C C . CYS A 1 157 ? -15.786 7.119 37.836 1.00 23.30 ? 157 CYS A C 1 ATOM 1233 O O . CYS A 1 157 ? -15.735 7.695 38.923 1.00 23.74 ? 157 CYS A O 1 ATOM 1234 C CB . CYS A 1 157 ? -17.316 7.666 35.981 1.00 19.06 ? 157 CYS A CB 1 ATOM 1235 S SG . CYS A 1 157 ? -16.838 9.398 36.116 1.00 21.71 ? 157 CYS A SG 1 ATOM 1236 N N . MET A 1 158 ? -14.732 6.741 37.111 1.00 20.21 ? 158 MET A N 1 ATOM 1237 C CA . MET A 1 158 ? -13.407 7.253 37.262 1.00 22.35 ? 158 MET A CA 1 ATOM 1238 C C . MET A 1 158 ? -13.110 8.130 36.059 1.00 20.92 ? 158 MET A C 1 ATOM 1239 O O . MET A 1 158 ? -13.398 7.725 34.920 1.00 19.70 ? 158 MET A O 1 ATOM 1240 C CB . MET A 1 158 ? -12.433 6.073 37.158 1.00 23.14 ? 158 MET A CB 1 ATOM 1241 C CG . MET A 1 158 ? -12.437 5.181 38.349 1.00 26.49 ? 158 MET A CG 1 ATOM 1242 S SD . MET A 1 158 ? -11.628 3.664 37.839 1.00 28.61 ? 158 MET A SD 1 ATOM 1243 C CE . MET A 1 158 ? -11.991 2.621 39.174 1.00 28.45 ? 158 MET A CE 1 ATOM 1244 N N . PRO A 1 159 ? -12.562 9.313 36.271 1.00 19.89 ? 159 PRO A N 1 ATOM 1245 C CA . PRO A 1 159 ? -12.250 10.131 35.145 1.00 20.32 ? 159 PRO A CA 1 ATOM 1246 C C . PRO A 1 159 ? -11.071 9.599 34.397 1.00 17.68 ? 159 PRO A C 1 ATOM 1247 O O . PRO A 1 159 ? -10.241 8.865 34.963 1.00 15.80 ? 159 PRO A O 1 ATOM 1248 C CB . PRO A 1 159 ? -11.865 11.473 35.767 1.00 20.74 ? 159 PRO A CB 1 ATOM 1249 C CG . PRO A 1 159 ? -11.281 11.077 37.066 1.00 22.62 ? 159 PRO A CG 1 ATOM 1250 C CD . PRO A 1 159 ? -12.158 9.945 37.540 1.00 24.86 ? 159 PRO A CD 1 ATOM 1251 N N . PHE A 1 160 ? -11.021 9.962 33.125 1.00 17.49 ? 160 PHE A N 1 ATOM 1252 C CA . PHE A 1 160 ? -10.027 9.454 32.191 1.00 14.65 ? 160 PHE A CA 1 ATOM 1253 C C . PHE A 1 160 ? -9.906 10.441 31.069 1.00 16.12 ? 160 PHE A C 1 ATOM 1254 O O . PHE A 1 160 ? -10.899 10.779 30.415 1.00 15.70 ? 160 PHE A O 1 ATOM 1255 C CB . PHE A 1 160 ? -10.529 8.110 31.636 1.00 14.50 ? 160 PHE A CB 1 ATOM 1256 C CG . PHE A 1 160 ? -9.669 7.484 30.509 1.00 15.60 ? 160 PHE A CG 1 ATOM 1257 C CD1 . PHE A 1 160 ? -9.781 7.924 29.166 1.00 15.86 ? 160 PHE A CD1 1 ATOM 1258 C CD2 . PHE A 1 160 ? -8.750 6.485 30.791 1.00 15.38 ? 160 PHE A CD2 1 ATOM 1259 C CE1 . PHE A 1 160 ? -8.983 7.346 28.162 1.00 13.10 ? 160 PHE A CE1 1 ATOM 1260 C CE2 . PHE A 1 160 ? -7.943 5.908 29.799 1.00 14.98 ? 160 PHE A CE2 1 ATOM 1261 C CZ . PHE A 1 160 ? -8.079 6.335 28.481 1.00 13.86 ? 160 PHE A CZ 1 ATOM 1262 N N . PHE A 1 161 ? -8.675 10.852 30.778 1.00 18.51 ? 161 PHE A N 1 ATOM 1263 C CA . PHE A 1 161 ? -8.402 11.777 29.717 1.00 20.85 ? 161 PHE A CA 1 ATOM 1264 C C . PHE A 1 161 ? -7.612 11.115 28.594 1.00 19.71 ? 161 PHE A C 1 ATOM 1265 O O . PHE A 1 161 ? -6.621 10.437 28.831 1.00 18.27 ? 161 PHE A O 1 ATOM 1266 C CB . PHE A 1 161 ? -7.637 12.995 30.258 1.00 23.84 ? 161 PHE A CB 1 ATOM 1267 C CG . PHE A 1 161 ? -8.519 13.946 30.964 1.00 30.56 ? 161 PHE A CG 1 ATOM 1268 C CD1 . PHE A 1 161 ? -8.893 13.700 32.253 1.00 33.80 ? 161 PHE A CD1 1 ATOM 1269 C CD2 . PHE A 1 161 ? -9.030 15.059 30.303 1.00 33.43 ? 161 PHE A CD2 1 ATOM 1270 C CE1 . PHE A 1 161 ? -9.773 14.541 32.918 1.00 36.12 ? 161 PHE A CE1 1 ATOM 1271 C CE2 . PHE A 1 161 ? -9.886 15.923 30.974 1.00 39.63 ? 161 PHE A CE2 1 ATOM 1272 C CZ . PHE A 1 161 ? -10.267 15.661 32.280 1.00 35.10 ? 161 PHE A CZ 1 ATOM 1273 N N . ARG A 1 162 ? -8.055 11.383 27.364 1.00 17.80 ? 162 ARG A N 1 ATOM 1274 C CA . ARG A 1 162 ? -7.444 10.821 26.167 1.00 18.15 ? 162 ARG A CA 1 ATOM 1275 C C . ARG A 1 162 ? -6.002 11.176 25.955 1.00 18.39 ? 162 ARG A C 1 ATOM 1276 O O . ARG A 1 162 ? -5.530 12.240 26.364 1.00 17.68 ? 162 ARG A O 1 ATOM 1277 C CB . ARG A 1 162 ? -8.292 11.251 24.944 1.00 19.07 ? 162 ARG A CB 1 ATOM 1278 C CG . ARG A 1 162 ? -9.717 10.712 25.005 1.00 18.86 ? 162 ARG A CG 1 ATOM 1279 C CD . ARG A 1 162 ? -10.408 10.739 23.586 1.00 19.64 ? 162 ARG A CD 1 ATOM 1280 N NE . ARG A 1 162 ? -9.718 9.870 22.628 1.00 19.22 ? 162 ARG A NE 1 ATOM 1281 C CZ . ARG A 1 162 ? -10.001 9.815 21.329 1.00 19.16 ? 162 ARG A CZ 1 ATOM 1282 N NH1 . ARG A 1 162 ? -10.908 10.640 20.806 1.00 19.69 ? 162 ARG A NH1 1 ATOM 1283 N NH2 . ARG A 1 162 ? -9.350 8.970 20.553 1.00 19.82 ? 162 ARG A NH2 1 ATOM 1284 N N . ALA A 1 163 ? -5.280 10.276 25.288 1.00 19.58 ? 163 ALA A N 1 ATOM 1285 C CA . ALA A 1 163 ? -3.848 10.496 25.042 1.00 21.44 ? 163 ALA A CA 1 ATOM 1286 C C . ALA A 1 163 ? -3.645 11.629 24.048 1.00 20.92 ? 163 ALA A C 1 ATOM 1287 O O . ALA A 1 163 ? -4.484 11.858 23.176 1.00 20.39 ? 163 ALA A O 1 ATOM 1288 C CB . ALA A 1 163 ? -3.174 9.230 24.557 1.00 22.38 ? 163 ALA A CB 1 ATOM 1289 N N . GLY A 1 164 ? -2.532 12.346 24.216 1.00 22.86 ? 164 GLY A N 1 ATOM 1290 C CA . GLY A 1 164 ? -2.138 13.411 23.306 1.00 22.03 ? 164 GLY A CA 1 ATOM 1291 C C . GLY A 1 164 ? -1.870 12.821 21.937 1.00 24.79 ? 164 GLY A C 1 ATOM 1292 O O . GLY A 1 164 ? -1.677 11.607 21.782 1.00 24.72 ? 164 GLY A O 1 ATOM 1293 N N . PHE A 1 165 ? -1.888 13.630 20.956 1.00 23.95 ? 165 PHE A N 1 ATOM 1294 C CA . PHE A 1 165 ? -1.766 13.066 19.596 1.00 26.33 ? 165 PHE A CA 1 ATOM 1295 C C . PHE A 1 165 ? -1.187 14.069 18.610 1.00 25.97 ? 165 PHE A C 1 ATOM 1296 O O . PHE A 1 165 ? -1.086 15.231 18.909 1.00 19.92 ? 165 PHE A O 1 ATOM 1297 C CB . PHE A 1 165 ? -3.114 12.604 19.091 1.00 24.37 ? 165 PHE A CB 1 ATOM 1298 C CG . PHE A 1 165 ? -4.133 13.688 19.051 1.00 25.22 ? 165 PHE A CG 1 ATOM 1299 C CD1 . PHE A 1 165 ? -4.854 14.012 20.183 1.00 29.12 ? 165 PHE A CD1 1 ATOM 1300 C CD2 . PHE A 1 165 ? -4.382 14.383 17.879 1.00 29.04 ? 165 PHE A CD2 1 ATOM 1301 C CE1 . PHE A 1 165 ? -5.798 15.025 20.176 1.00 28.38 ? 165 PHE A CE1 1 ATOM 1302 C CE2 . PHE A 1 165 ? -5.335 15.381 17.852 1.00 29.72 ? 165 PHE A CE2 1 ATOM 1303 C CZ . PHE A 1 165 ? -6.056 15.696 18.990 1.00 30.47 ? 165 PHE A CZ 1 ATOM 1304 N N . VAL A 1 166 ? -0.773 13.583 17.449 1.00 27.07 ? 166 VAL A N 1 ATOM 1305 C CA . VAL A 1 166 ? -0.117 14.451 16.470 1.00 31.88 ? 166 VAL A CA 1 ATOM 1306 C C . VAL A 1 166 ? -1.145 15.373 15.830 1.00 31.80 ? 166 VAL A C 1 ATOM 1307 O O . VAL A 1 166 ? -2.167 14.897 15.405 1.00 34.34 ? 166 VAL A O 1 ATOM 1308 C CB . VAL A 1 166 ? 0.552 13.639 15.351 1.00 31.86 ? 166 VAL A CB 1 ATOM 1309 C CG1 . VAL A 1 166 ? 1.086 14.573 14.254 1.00 32.92 ? 166 VAL A CG1 1 ATOM 1310 C CG2 . VAL A 1 166 ? 1.630 12.790 15.915 1.00 30.48 ? 166 VAL A CG2 1 ATOM 1311 N N . CYS A 1 167 ? -0.833 16.655 15.720 1.00 35.23 ? 167 CYS A N 1 ATOM 1312 C CA . CYS A 1 167 ? -1.784 17.679 15.225 1.00 44.03 ? 167 CYS A CA 1 ATOM 1313 C C . CYS A 1 167 ? -2.140 17.527 13.765 1.00 36.04 ? 167 CYS A C 1 ATOM 1314 O O . CYS A 1 167 ? -1.285 17.208 13.018 1.00 31.41 ? 167 CYS A O 1 ATOM 1315 C CB . CYS A 1 167 ? -1.216 19.085 15.476 1.00 48.80 ? 167 CYS A CB 1 ATOM 1316 S SG . CYS A 1 167 ? -1.456 19.532 17.215 1.00 58.29 ? 167 CYS A SG 1 ATOM 1317 N N . PRO A 1 168 ? -3.442 17.668 13.393 1.00 42.56 ? 168 PRO A N 1 ATOM 1318 C CA . PRO A 1 168 ? -3.794 17.709 11.979 1.00 43.75 ? 168 PRO A CA 1 ATOM 1319 C C . PRO A 1 168 ? -3.127 18.927 11.394 1.00 48.69 ? 168 PRO A C 1 ATOM 1320 O O . PRO A 1 168 ? -3.301 20.052 11.897 1.00 48.08 ? 168 PRO A O 1 ATOM 1321 C CB . PRO A 1 168 ? -5.321 17.891 11.963 1.00 47.01 ? 168 PRO A CB 1 ATOM 1322 C CG . PRO A 1 168 ? -5.803 17.521 13.335 1.00 46.50 ? 168 PRO A CG 1 ATOM 1323 C CD . PRO A 1 168 ? -4.637 17.750 14.266 1.00 45.87 ? 168 PRO A CD 1 ATOM 1324 N N . THR A 1 169 ? -2.382 18.694 10.287 1.00 49.09 ? 169 THR A N 1 ATOM 1325 C CA . THR A 1 169 ? -1.665 19.790 9.664 1.00 52.92 ? 169 THR A CA 1 ATOM 1326 C C . THR A 1 169 ? -2.179 20.031 8.218 1.00 55.59 ? 169 THR A C 1 ATOM 1327 O O . THR A 1 169 ? -2.925 19.229 7.676 1.00 45.46 ? 169 THR A O 1 ATOM 1328 C CB . THR A 1 169 ? -0.143 19.511 9.746 1.00 50.08 ? 169 THR A CB 1 ATOM 1329 O OG1 . THR A 1 169 ? 0.173 18.182 9.304 1.00 44.81 ? 169 THR A OG1 1 ATOM 1330 C CG2 . THR A 1 169 ? 0.339 19.679 11.204 1.00 48.02 ? 169 THR A CG2 1 ATOM 1331 N N . PRO A 1 170 ? -1.841 21.171 7.604 1.00 60.13 ? 170 PRO A N 1 ATOM 1332 C CA . PRO A 1 170 ? -1.838 20.955 6.172 1.00 61.64 ? 170 PRO A CA 1 ATOM 1333 C C . PRO A 1 170 ? -0.925 19.750 5.785 1.00 67.76 ? 170 PRO A C 1 ATOM 1334 O O . PRO A 1 170 ? -0.113 19.278 6.602 1.00 65.40 ? 170 PRO A O 1 ATOM 1335 C CB . PRO A 1 170 ? -1.376 22.290 5.636 1.00 64.29 ? 170 PRO A CB 1 ATOM 1336 C CG . PRO A 1 170 ? -1.986 23.273 6.598 1.00 62.97 ? 170 PRO A CG 1 ATOM 1337 C CD . PRO A 1 170 ? -2.074 22.585 7.937 1.00 60.67 ? 170 PRO A CD 1 ATOM 1338 N N . PRO A 1 171 ? -1.165 19.141 4.616 1.00 79.43 ? 171 PRO A N 1 ATOM 1339 C CA . PRO A 1 171 ? -2.235 19.367 3.619 1.00 72.29 ? 171 PRO A CA 1 ATOM 1340 C C . PRO A 1 171 ? -3.681 19.443 4.158 1.00 73.09 ? 171 PRO A C 1 ATOM 1341 O O . PRO A 1 171 ? -4.517 20.005 3.481 1.00 76.18 ? 171 PRO A O 1 ATOM 1342 C CB . PRO A 1 171 ? -2.114 18.159 2.681 1.00 74.03 ? 171 PRO A CB 1 ATOM 1343 C CG . PRO A 1 171 ? -0.764 17.567 2.938 1.00 78.63 ? 171 PRO A CG 1 ATOM 1344 C CD . PRO A 1 171 ? -0.366 17.930 4.333 1.00 78.62 ? 171 PRO A CD 1 ATOM 1345 N N . TYR A 1 172 ? -3.920 18.888 5.342 1.00 71.16 ? 172 TYR A N 1 ATOM 1346 C CA . TYR A 1 172 ? -5.240 18.726 5.948 1.00 67.58 ? 172 TYR A CA 1 ATOM 1347 C C . TYR A 1 172 ? -5.975 17.458 5.638 1.00 54.84 ? 172 TYR A C 1 ATOM 1348 O O . TYR A 1 172 ? -7.071 17.281 6.062 1.00 55.23 ? 172 TYR A O 1 ATOM 1349 C CB . TYR A 1 172 ? -6.141 19.931 5.731 1.00 78.32 ? 172 TYR A CB 1 ATOM 1350 C CG . TYR A 1 172 ? -6.104 20.788 6.966 1.00 94.07 ? 172 TYR A CG 1 ATOM 1351 C CD1 . TYR A 1 172 ? -6.120 20.212 8.231 1.00 95.71 ? 172 TYR A CD1 1 ATOM 1352 C CD2 . TYR A 1 172 ? -5.960 22.149 6.876 1.00 105.70 ? 172 TYR A CD2 1 ATOM 1353 C CE1 . TYR A 1 172 ? -6.032 20.983 9.366 1.00 101.81 ? 172 TYR A CE1 1 ATOM 1354 C CE2 . TYR A 1 172 ? -5.865 22.930 8.005 1.00 108.88 ? 172 TYR A CE2 1 ATOM 1355 C CZ . TYR A 1 172 ? -5.909 22.353 9.244 1.00 109.16 ? 172 TYR A CZ 1 ATOM 1356 O OH . TYR A 1 172 ? -5.805 23.172 10.340 1.00 103.51 ? 172 TYR A OH 1 ATOM 1357 N N . GLN A 1 173 ? -5.321 16.578 4.919 1.00 50.67 ? 173 GLN A N 1 ATOM 1358 C CA . GLN A 1 173 ? -5.879 15.321 4.476 1.00 51.00 ? 173 GLN A CA 1 ATOM 1359 C C . GLN A 1 173 ? -6.436 14.546 5.676 1.00 48.05 ? 173 GLN A C 1 ATOM 1360 O O . GLN A 1 173 ? -5.885 14.648 6.733 1.00 46.83 ? 173 GLN A O 1 ATOM 1361 C CB . GLN A 1 173 ? -4.739 14.545 3.834 1.00 55.94 ? 173 GLN A CB 1 ATOM 1362 C CG . GLN A 1 173 ? -5.043 13.152 3.317 1.00 65.30 ? 173 GLN A CG 1 ATOM 1363 C CD . GLN A 1 173 ? -3.797 12.431 2.832 1.00 69.28 ? 173 GLN A CD 1 ATOM 1364 O OE1 . GLN A 1 173 ? -2.777 13.048 2.609 1.00 68.57 ? 173 GLN A OE1 1 ATOM 1365 N NE2 . GLN A 1 173 ? -3.886 11.124 2.659 1.00 72.36 ? 173 GLN A NE2 1 ATOM 1366 N N . SER A 1 174 ? -7.567 13.850 5.513 1.00 46.78 ? 174 SER A N 1 ATOM 1367 C CA . SER A 1 174 ? -8.229 13.104 6.612 1.00 44.89 ? 174 SER A CA 1 ATOM 1368 C C . SER A 1 174 ? -7.409 11.891 6.920 1.00 39.31 ? 174 SER A C 1 ATOM 1369 O O . SER A 1 174 ? -7.222 11.026 6.072 1.00 36.90 ? 174 SER A O 1 ATOM 1370 C CB . SER A 1 174 ? -9.673 12.655 6.277 1.00 46.43 ? 174 SER A CB 1 ATOM 1371 O OG . SER A 1 174 ? -10.648 13.503 6.909 1.00 48.06 ? 174 SER A OG 1 ATOM 1372 N N . LEU A 1 175 ? -6.894 11.842 8.138 1.00 32.26 ? 175 LEU A N 1 ATOM 1373 C CA . LEU A 1 175 ? -6.039 10.731 8.535 1.00 32.49 ? 175 LEU A CA 1 ATOM 1374 C C . LEU A 1 175 ? -6.378 10.350 9.975 1.00 24.97 ? 175 LEU A C 1 ATOM 1375 O O . LEU A 1 175 ? -6.755 11.172 10.741 1.00 21.82 ? 175 LEU A O 1 ATOM 1376 C CB . LEU A 1 175 ? -4.551 11.123 8.456 1.00 31.78 ? 175 LEU A CB 1 ATOM 1377 C CG . LEU A 1 175 ? -3.861 11.268 7.089 1.00 31.86 ? 175 LEU A CG 1 ATOM 1378 C CD1 . LEU A 1 175 ? -2.539 12.026 7.229 1.00 30.15 ? 175 LEU A CD1 1 ATOM 1379 C CD2 . LEU A 1 175 ? -3.662 9.898 6.446 1.00 32.52 ? 175 LEU A CD2 1 ATOM 1380 N N . ALA A 1 176 ? -6.248 9.077 10.291 1.00 23.24 ? 176 ALA A N 1 ATOM 1381 C CA . ALA A 1 176 ? -6.579 8.602 11.606 1.00 22.65 ? 176 ALA A CA 1 ATOM 1382 C C . ALA A 1 176 ? -5.596 9.224 12.632 1.00 20.91 ? 176 ALA A C 1 ATOM 1383 O O . ALA A 1 176 ? -4.454 9.412 12.368 1.00 17.60 ? 176 ALA A O 1 ATOM 1384 C CB . ALA A 1 176 ? -6.540 7.095 11.623 1.00 22.56 ? 176 ALA A CB 1 ATOM 1385 N N . ARG A 1 177 ? -6.122 9.577 13.790 1.00 19.60 ? 177 ARG A N 1 ATOM 1386 C CA . ARG A 1 177 ? -5.343 10.006 14.912 1.00 18.52 ? 177 ARG A CA 1 ATOM 1387 C C . ARG A 1 177 ? -4.244 9.048 15.353 1.00 19.32 ? 177 ARG A C 1 ATOM 1388 O O . ARG A 1 177 ? -4.471 7.853 15.550 1.00 19.13 ? 177 ARG A O 1 ATOM 1389 C CB . ARG A 1 177 ? -6.338 10.182 16.040 1.00 19.35 ? 177 ARG A CB 1 ATOM 1390 C CG . ARG A 1 177 ? -5.744 10.641 17.346 1.00 20.86 ? 177 ARG A CG 1 ATOM 1391 C CD . ARG A 1 177 ? -6.771 11.640 17.763 1.00 24.52 ? 177 ARG A CD 1 ATOM 1392 N NE . ARG A 1 177 ? -7.104 11.561 19.081 1.00 26.98 ? 177 ARG A NE 1 ATOM 1393 C CZ . ARG A 1 177 ? -7.922 12.395 19.692 1.00 24.97 ? 177 ARG A CZ 1 ATOM 1394 N NH1 . ARG A 1 177 ? -8.555 13.437 19.121 1.00 25.30 ? 177 ARG A NH1 1 ATOM 1395 N NH2 . ARG A 1 177 ? -8.042 12.153 20.946 1.00 21.00 ? 177 ARG A NH2 1 ATOM 1396 N N . ASP A 1 178 ? -3.048 9.609 15.506 1.00 20.16 ? 178 ASP A N 1 ATOM 1397 C CA . ASP A 1 178 ? -1.880 8.946 16.029 1.00 19.71 ? 178 ASP A CA 1 ATOM 1398 C C . ASP A 1 178 ? -1.412 9.520 17.337 1.00 19.04 ? 178 ASP A C 1 ATOM 1399 O O . ASP A 1 178 ? -1.022 10.692 17.412 1.00 18.68 ? 178 ASP A O 1 ATOM 1400 C CB . ASP A 1 178 ? -0.681 9.025 15.047 1.00 20.11 ? 178 ASP A CB 1 ATOM 1401 C CG . ASP A 1 178 ? -0.800 8.114 13.891 1.00 20.20 ? 178 ASP A CG 1 ATOM 1402 O OD1 . ASP A 1 178 ? -1.248 6.919 14.008 1.00 19.91 ? 178 ASP A OD1 1 ATOM 1403 O OD2 . ASP A 1 178 ? -0.434 8.629 12.825 1.00 20.09 ? 178 ASP A OD2 1 ATOM 1404 N N . GLN A 1 179 ? -1.326 8.667 18.356 1.00 18.64 ? 179 GLN A N 1 ATOM 1405 C CA . GLN A 1 179 ? -0.769 9.099 19.652 1.00 16.64 ? 179 GLN A CA 1 ATOM 1406 C C . GLN A 1 179 ? 0.757 9.242 19.551 1.00 17.52 ? 179 GLN A C 1 ATOM 1407 O O . GLN A 1 179 ? 1.388 8.720 18.686 1.00 16.42 ? 179 GLN A O 1 ATOM 1408 C CB . GLN A 1 179 ? -1.135 8.121 20.778 1.00 16.33 ? 179 GLN A CB 1 ATOM 1409 C CG . GLN A 1 179 ? -2.644 8.124 21.128 1.00 15.92 ? 179 GLN A CG 1 ATOM 1410 C CD . GLN A 1 179 ? -3.519 7.474 20.055 1.00 15.47 ? 179 GLN A CD 1 ATOM 1411 O OE1 . GLN A 1 179 ? -3.082 6.604 19.364 1.00 18.03 ? 179 GLN A OE1 1 ATOM 1412 N NE2 . GLN A 1 179 ? -4.731 7.959 19.896 1.00 15.34 ? 179 GLN A NE2 1 ATOM 1413 N N . ILE A 1 180 ? 1.294 10.052 20.422 1.00 17.45 ? 180 ILE A N 1 ATOM 1414 C CA . ILE A 1 180 ? 2.714 10.401 20.454 1.00 21.51 ? 180 ILE A CA 1 ATOM 1415 C C . ILE A 1 180 ? 3.509 9.466 21.353 1.00 19.02 ? 180 ILE A C 1 ATOM 1416 O O . ILE A 1 180 ? 3.029 9.004 22.375 1.00 21.32 ? 180 ILE A O 1 ATOM 1417 C CB . ILE A 1 180 ? 2.828 11.852 20.984 1.00 20.08 ? 180 ILE A CB 1 ATOM 1418 C CG1 . ILE A 1 180 ? 2.064 12.751 20.007 1.00 26.02 ? 180 ILE A CG1 1 ATOM 1419 C CG2 . ILE A 1 180 ? 4.276 12.256 21.155 1.00 20.38 ? 180 ILE A CG2 1 ATOM 1420 C CD1 . ILE A 1 180 ? 2.034 14.247 20.279 1.00 28.23 ? 180 ILE A CD1 1 ATOM 1421 N N . ASN A 1 181 ? 4.721 9.168 20.949 1.00 19.74 ? 181 ASN A N 1 ATOM 1422 C CA . ASN A 1 181 ? 5.726 8.662 21.845 1.00 17.94 ? 181 ASN A CA 1 ATOM 1423 C C . ASN A 1 181 ? 6.679 9.803 22.256 1.00 18.71 ? 181 ASN A C 1 ATOM 1424 O O . ASN A 1 181 ? 7.585 10.217 21.506 1.00 17.86 ? 181 ASN A O 1 ATOM 1425 C CB . ASN A 1 181 ? 6.506 7.503 21.229 1.00 18.75 ? 181 ASN A CB 1 ATOM 1426 C CG . ASN A 1 181 ? 7.371 6.761 22.250 1.00 19.74 ? 181 ASN A CG 1 ATOM 1427 O OD1 . ASN A 1 181 ? 7.446 7.187 23.411 1.00 18.86 ? 181 ASN A OD1 1 ATOM 1428 N ND2 . ASN A 1 181 ? 8.125 5.735 21.794 1.00 17.08 ? 181 ASN A ND2 1 ATOM 1429 N N . ALA A 1 182 ? 6.569 10.193 23.507 1.00 15.91 ? 182 ALA A N 1 ATOM 1430 C CA . ALA A 1 182 ? 7.395 11.263 24.056 1.00 17.74 ? 182 ALA A CA 1 ATOM 1431 C C . ALA A 1 182 ? 8.819 10.883 24.472 1.00 18.10 ? 182 ALA A C 1 ATOM 1432 O O . ALA A 1 182 ? 9.564 11.758 24.845 1.00 18.23 ? 182 ALA A O 1 ATOM 1433 C CB . ALA A 1 182 ? 6.673 11.967 25.203 1.00 17.10 ? 182 ALA A CB 1 ATOM 1434 N N . VAL A 1 183 ? 9.215 9.612 24.388 1.00 17.75 ? 183 VAL A N 1 ATOM 1435 C CA . VAL A 1 183 ? 10.561 9.280 24.616 1.00 18.56 ? 183 VAL A CA 1 ATOM 1436 C C . VAL A 1 183 ? 11.149 8.624 23.401 1.00 17.87 ? 183 VAL A C 1 ATOM 1437 O O . VAL A 1 183 ? 10.446 8.303 22.448 1.00 17.78 ? 183 VAL A O 1 ATOM 1438 C CB . VAL A 1 183 ? 10.774 8.427 25.905 1.00 19.25 ? 183 VAL A CB 1 ATOM 1439 C CG1 . VAL A 1 183 ? 10.120 9.092 27.123 1.00 19.04 ? 183 VAL A CG1 1 ATOM 1440 C CG2 . VAL A 1 183 ? 10.274 7.027 25.714 1.00 19.09 ? 183 VAL A CG2 1 ATOM 1441 N N . THR A 1 184 ? 12.449 8.352 23.469 1.00 17.59 ? 184 THR A N 1 ATOM 1442 C CA . THR A 1 184 ? 13.211 7.811 22.301 1.00 17.36 ? 184 THR A CA 1 ATOM 1443 C C . THR A 1 184 ? 12.936 6.309 22.199 1.00 18.62 ? 184 THR A C 1 ATOM 1444 O O . THR A 1 184 ? 12.983 5.606 23.220 1.00 18.61 ? 184 THR A O 1 ATOM 1445 C CB . THR A 1 184 ? 14.721 8.024 22.483 1.00 17.68 ? 184 THR A CB 1 ATOM 1446 O OG1 . THR A 1 184 ? 15.215 7.293 23.639 1.00 17.45 ? 184 THR A OG1 1 ATOM 1447 C CG2 . THR A 1 184 ? 15.035 9.492 22.652 1.00 20.04 ? 184 THR A CG2 1 ATOM 1448 N N . SER A 1 185 ? 12.666 5.826 20.992 1.00 17.57 ? 185 SER A N 1 ATOM 1449 C CA . SER A 1 185 ? 12.326 4.425 20.771 1.00 18.64 ? 185 SER A CA 1 ATOM 1450 C C . SER A 1 185 ? 13.477 3.475 20.985 1.00 18.36 ? 185 SER A C 1 ATOM 1451 O O . SER A 1 185 ? 13.305 2.247 21.160 1.00 20.27 ? 185 SER A O 1 ATOM 1452 C CB . SER A 1 185 ? 11.813 4.194 19.343 1.00 19.04 ? 185 SER A CB 1 ATOM 1453 O OG . SER A 1 185 ? 10.647 4.906 19.101 1.00 18.00 ? 185 SER A OG 1 ATOM 1454 N N . PHE A 1 186 ? 14.681 4.032 20.919 1.00 20.47 ? 186 PHE A N 1 ATOM 1455 C CA . PHE A 1 186 ? 15.897 3.306 21.144 1.00 19.26 ? 186 PHE A CA 1 ATOM 1456 C C . PHE A 1 186 ? 15.978 2.991 22.659 1.00 19.25 ? 186 PHE A C 1 ATOM 1457 O O . PHE A 1 186 ? 15.510 3.738 23.508 1.00 21.56 ? 186 PHE A O 1 ATOM 1458 C CB . PHE A 1 186 ? 17.131 4.127 20.644 1.00 20.29 ? 186 PHE A CB 1 ATOM 1459 C CG . PHE A 1 186 ? 17.078 4.432 19.167 1.00 20.31 ? 186 PHE A CG 1 ATOM 1460 C CD1 . PHE A 1 186 ? 17.163 3.386 18.246 1.00 20.90 ? 186 PHE A CD1 1 ATOM 1461 C CD2 . PHE A 1 186 ? 16.800 5.689 18.713 1.00 20.82 ? 186 PHE A CD2 1 ATOM 1462 C CE1 . PHE A 1 186 ? 17.018 3.646 16.910 1.00 23.49 ? 186 PHE A CE1 1 ATOM 1463 C CE2 . PHE A 1 186 ? 16.644 5.969 17.347 1.00 20.98 ? 186 PHE A CE2 1 ATOM 1464 C CZ . PHE A 1 186 ? 16.755 4.933 16.454 1.00 20.72 ? 186 PHE A CZ 1 ATOM 1465 N N . LEU A 1 187 ? 16.633 1.866 22.949 1.00 18.57 ? 187 LEU A N 1 ATOM 1466 C CA . LEU A 1 187 ? 16.913 1.419 24.264 1.00 18.04 ? 187 LEU A CA 1 ATOM 1467 C C . LEU A 1 187 ? 18.224 2.038 24.621 1.00 18.18 ? 187 LEU A C 1 ATOM 1468 O O . LEU A 1 187 ? 19.323 1.445 24.370 1.00 19.16 ? 187 LEU A O 1 ATOM 1469 C CB . LEU A 1 187 ? 16.931 -0.112 24.277 1.00 17.69 ? 187 LEU A CB 1 ATOM 1470 C CG . LEU A 1 187 ? 17.073 -0.688 25.689 1.00 17.72 ? 187 LEU A CG 1 ATOM 1471 C CD1 . LEU A 1 187 ? 15.912 -0.255 26.608 1.00 16.36 ? 187 LEU A CD1 1 ATOM 1472 C CD2 . LEU A 1 187 ? 17.071 -2.215 25.646 1.00 18.93 ? 187 LEU A CD2 1 ATOM 1473 N N . ASP A 1 188 ? 18.148 3.247 25.182 1.00 20.50 ? 188 ASP A N 1 ATOM 1474 C CA . ASP A 1 188 ? 19.292 4.128 25.228 1.00 19.42 ? 188 ASP A CA 1 ATOM 1475 C C . ASP A 1 188 ? 19.440 4.895 26.515 1.00 21.35 ? 188 ASP A C 1 ATOM 1476 O O . ASP A 1 188 ? 20.044 5.964 26.546 1.00 20.45 ? 188 ASP A O 1 ATOM 1477 C CB . ASP A 1 188 ? 19.178 5.117 24.051 1.00 20.18 ? 188 ASP A CB 1 ATOM 1478 C CG . ASP A 1 188 ? 17.960 6.018 24.151 1.00 18.45 ? 188 ASP A CG 1 ATOM 1479 O OD1 . ASP A 1 188 ? 17.144 5.832 25.068 1.00 16.79 ? 188 ASP A OD1 1 ATOM 1480 O OD2 . ASP A 1 188 ? 17.852 6.943 23.311 1.00 18.92 ? 188 ASP A OD2 1 ATOM 1481 N N . ALA A 1 189 ? 18.861 4.369 27.587 1.00 21.45 ? 189 ALA A N 1 ATOM 1482 C CA . ALA A 1 189 ? 18.852 5.060 28.872 1.00 19.48 ? 189 ALA A CA 1 ATOM 1483 C C . ALA A 1 189 ? 18.193 6.412 28.856 1.00 19.54 ? 189 ALA A C 1 ATOM 1484 O O . ALA A 1 189 ? 18.531 7.285 29.657 1.00 20.71 ? 189 ALA A O 1 ATOM 1485 C CB . ALA A 1 189 ? 20.240 5.137 29.416 1.00 22.20 ? 189 ALA A CB 1 ATOM 1486 N N . SER A 1 190 ? 17.249 6.636 27.946 1.00 16.87 ? 190 SER A N 1 ATOM 1487 C CA . SER A 1 190 ? 16.568 7.938 27.973 1.00 16.74 ? 190 SER A CA 1 ATOM 1488 C C . SER A 1 190 ? 15.824 8.194 29.285 1.00 15.22 ? 190 SER A C 1 ATOM 1489 O O . SER A 1 190 ? 15.479 9.303 29.588 1.00 14.82 ? 190 SER A O 1 ATOM 1490 C CB . SER A 1 190 ? 15.580 8.056 26.824 1.00 16.79 ? 190 SER A CB 1 ATOM 1491 O OG . SER A 1 190 ? 14.788 6.882 26.676 1.00 18.90 ? 190 SER A OG 1 ATOM 1492 N N . LEU A 1 191 ? 15.500 7.144 30.033 1.00 15.37 ? 191 LEU A N 1 ATOM 1493 C CA . LEU A 1 191 ? 14.751 7.330 31.255 1.00 18.08 ? 191 LEU A CA 1 ATOM 1494 C C . LEU A 1 191 ? 15.640 7.968 32.312 1.00 21.04 ? 191 LEU A C 1 ATOM 1495 O O . LEU A 1 191 ? 15.127 8.576 33.296 1.00 20.24 ? 191 LEU A O 1 ATOM 1496 C CB . LEU A 1 191 ? 14.113 6.000 31.740 1.00 18.11 ? 191 LEU A CB 1 ATOM 1497 C CG . LEU A 1 191 ? 14.994 5.022 32.519 1.00 19.25 ? 191 LEU A CG 1 ATOM 1498 C CD1 . LEU A 1 191 ? 14.102 3.931 33.097 1.00 19.80 ? 191 LEU A CD1 1 ATOM 1499 C CD2 . LEU A 1 191 ? 16.122 4.397 31.716 1.00 18.91 ? 191 LEU A CD2 1 ATOM 1500 N N . VAL A 1 192 ? 16.968 7.913 32.086 1.00 17.55 ? 192 VAL A N 1 ATOM 1501 C CA . VAL A 1 192 ? 17.946 8.558 33.014 1.00 18.58 ? 192 VAL A CA 1 ATOM 1502 C C . VAL A 1 192 ? 18.296 9.964 32.533 1.00 18.40 ? 192 VAL A C 1 ATOM 1503 O O . VAL A 1 192 ? 18.380 10.908 33.317 1.00 16.58 ? 192 VAL A O 1 ATOM 1504 C CB . VAL A 1 192 ? 19.222 7.712 33.109 1.00 18.88 ? 192 VAL A CB 1 ATOM 1505 C CG1 . VAL A 1 192 ? 20.282 8.371 33.974 1.00 19.43 ? 192 VAL A CG1 1 ATOM 1506 C CG2 . VAL A 1 192 ? 18.909 6.310 33.587 1.00 16.22 ? 192 VAL A CG2 1 ATOM 1507 N N . TYR A 1 193 ? 18.507 10.103 31.217 1.00 21.31 ? 193 TYR A N 1 ATOM 1508 C CA . TYR A 1 193 ? 19.117 11.325 30.653 1.00 22.24 ? 193 TYR A CA 1 ATOM 1509 C C . TYR A 1 193 ? 18.103 12.325 30.167 1.00 23.46 ? 193 TYR A C 1 ATOM 1510 O O . TYR A 1 193 ? 18.434 13.521 30.034 1.00 21.73 ? 193 TYR A O 1 ATOM 1511 C CB . TYR A 1 193 ? 20.132 10.976 29.521 1.00 20.52 ? 193 TYR A CB 1 ATOM 1512 C CG . TYR A 1 193 ? 21.232 10.185 30.074 1.00 19.97 ? 193 TYR A CG 1 ATOM 1513 C CD1 . TYR A 1 193 ? 22.094 10.747 30.991 1.00 18.65 ? 193 TYR A CD1 1 ATOM 1514 C CD2 . TYR A 1 193 ? 21.346 8.843 29.811 1.00 18.28 ? 193 TYR A CD2 1 ATOM 1515 C CE1 . TYR A 1 193 ? 23.086 10.001 31.607 1.00 17.72 ? 193 TYR A CE1 1 ATOM 1516 C CE2 . TYR A 1 193 ? 22.335 8.100 30.405 1.00 19.49 ? 193 TYR A CE2 1 ATOM 1517 C CZ . TYR A 1 193 ? 23.223 8.710 31.324 1.00 19.31 ? 193 TYR A CZ 1 ATOM 1518 O OH . TYR A 1 193 ? 24.244 7.971 31.923 1.00 18.36 ? 193 TYR A OH 1 ATOM 1519 N N . GLY A 1 194 ? 16.889 11.850 29.888 1.00 21.32 ? 194 GLY A N 1 ATOM 1520 C CA . GLY A 1 194 ? 15.880 12.657 29.229 1.00 21.26 ? 194 GLY A CA 1 ATOM 1521 C C . GLY A 1 194 ? 15.863 12.359 27.727 1.00 24.01 ? 194 GLY A C 1 ATOM 1522 O O . GLY A 1 194 ? 16.817 11.787 27.177 1.00 22.73 ? 194 GLY A O 1 ATOM 1523 N N . SER A 1 195 ? 14.749 12.690 27.083 1.00 23.22 ? 195 SER A N 1 ATOM 1524 C CA . SER A 1 195 ? 14.540 12.523 25.630 1.00 22.71 ? 195 SER A CA 1 ATOM 1525 C C . SER A 1 195 ? 14.356 13.879 24.926 1.00 24.32 ? 195 SER A C 1 ATOM 1526 O O . SER A 1 195 ? 14.039 13.959 23.725 1.00 20.95 ? 195 SER A O 1 ATOM 1527 C CB . SER A 1 195 ? 13.290 11.726 25.391 1.00 22.11 ? 195 SER A CB 1 ATOM 1528 O OG . SER A 1 195 ? 13.412 10.414 25.862 1.00 20.69 ? 195 SER A OG 1 ATOM 1529 N N . GLU A 1 196 ? 14.516 14.913 25.706 1.00 24.38 ? 196 GLU A N 1 ATOM 1530 C CA . GLU A 1 196 ? 14.325 16.295 25.282 1.00 28.69 ? 196 GLU A CA 1 ATOM 1531 C C . GLU A 1 196 ? 15.561 17.107 25.777 1.00 30.92 ? 196 GLU A C 1 ATOM 1532 O O . GLU A 1 196 ? 16.036 16.911 26.922 1.00 31.37 ? 196 GLU A O 1 ATOM 1533 C CB . GLU A 1 196 ? 13.077 16.769 25.959 1.00 32.51 ? 196 GLU A CB 1 ATOM 1534 C CG . GLU A 1 196 ? 12.577 18.109 25.539 1.00 36.31 ? 196 GLU A CG 1 ATOM 1535 C CD . GLU A 1 196 ? 13.369 19.245 26.133 1.00 35.77 ? 196 GLU A CD 1 ATOM 1536 O OE1 . GLU A 1 196 ? 13.463 19.335 27.386 1.00 32.68 ? 196 GLU A OE1 1 ATOM 1537 O OE2 . GLU A 1 196 ? 13.857 20.087 25.324 1.00 37.93 ? 196 GLU A OE2 1 ATOM 1538 N N . PRO A 1 197 ? 16.127 17.976 24.920 1.00 27.50 ? 197 PRO A N 1 ATOM 1539 C CA . PRO A 1 197 ? 17.421 18.585 25.282 1.00 28.18 ? 197 PRO A CA 1 ATOM 1540 C C . PRO A 1 197 ? 17.479 19.559 26.486 1.00 25.96 ? 197 PRO A C 1 ATOM 1541 O O . PRO A 1 197 ? 18.470 19.530 27.224 1.00 25.83 ? 197 PRO A O 1 ATOM 1542 C CB . PRO A 1 197 ? 17.836 19.309 23.995 1.00 28.56 ? 197 PRO A CB 1 ATOM 1543 C CG . PRO A 1 197 ? 16.591 19.354 23.138 1.00 31.83 ? 197 PRO A CG 1 ATOM 1544 C CD . PRO A 1 197 ? 15.819 18.145 23.499 1.00 27.63 ? 197 PRO A CD 1 ATOM 1545 N N . SER A 1 198 ? 16.503 20.433 26.691 1.00 26.68 ? 198 SER A N 1 ATOM 1546 C CA . SER A 1 198 ? 16.594 21.315 27.859 1.00 28.16 ? 198 SER A CA 1 ATOM 1547 C C . SER A 1 198 ? 16.498 20.518 29.157 1.00 28.08 ? 198 SER A C 1 ATOM 1548 O O . SER A 1 198 ? 17.194 20.818 30.113 1.00 28.57 ? 198 SER A O 1 ATOM 1549 C CB . SER A 1 198 ? 15.598 22.459 27.854 1.00 33.16 ? 198 SER A CB 1 ATOM 1550 O OG . SER A 1 198 ? 14.288 22.001 27.838 1.00 37.28 ? 198 SER A OG 1 ATOM 1551 N N . LEU A 1 199 ? 15.645 19.490 29.198 1.00 28.08 ? 199 LEU A N 1 ATOM 1552 C CA . LEU A 1 199 ? 15.602 18.624 30.375 1.00 26.10 ? 199 LEU A CA 1 ATOM 1553 C C . LEU A 1 199 ? 16.940 17.945 30.581 1.00 27.76 ? 199 LEU A C 1 ATOM 1554 O O . LEU A 1 199 ? 17.485 17.955 31.699 1.00 25.48 ? 199 LEU A O 1 ATOM 1555 C CB . LEU A 1 199 ? 14.487 17.573 30.286 1.00 28.37 ? 199 LEU A CB 1 ATOM 1556 C CG . LEU A 1 199 ? 14.459 16.549 31.432 1.00 28.05 ? 199 LEU A CG 1 ATOM 1557 C CD1 . LEU A 1 199 ? 14.237 17.226 32.786 1.00 27.28 ? 199 LEU A CD1 1 ATOM 1558 C CD2 . LEU A 1 199 ? 13.395 15.489 31.184 1.00 29.66 ? 199 LEU A CD2 1 ATOM 1559 N N . ALA A 1 200 ? 17.504 17.367 29.514 1.00 22.93 ? 200 ALA A N 1 ATOM 1560 C CA . ALA A 1 200 ? 18.736 16.649 29.682 1.00 24.50 ? 200 ALA A CA 1 ATOM 1561 C C . ALA A 1 200 ? 19.798 17.567 30.271 1.00 23.73 ? 200 ALA A C 1 ATOM 1562 O O . ALA A 1 200 ? 20.641 17.147 31.052 1.00 22.85 ? 200 ALA A O 1 ATOM 1563 C CB . ALA A 1 200 ? 19.207 16.019 28.355 1.00 26.27 ? 200 ALA A CB 1 ATOM 1564 N N . SER A 1 201 ? 19.803 18.812 29.858 1.00 23.70 ? 201 SER A N 1 ATOM 1565 C CA . SER A 1 201 ? 20.790 19.740 30.361 1.00 24.01 ? 201 SER A CA 1 ATOM 1566 C C . SER A 1 201 ? 20.503 20.060 31.838 1.00 24.71 ? 201 SER A C 1 ATOM 1567 O O . SER A 1 201 ? 21.413 20.036 32.685 1.00 27.89 ? 201 SER A O 1 ATOM 1568 C CB . SER A 1 201 ? 20.796 21.012 29.476 1.00 25.95 ? 201 SER A CB 1 ATOM 1569 O OG . SER A 1 201 ? 21.348 22.131 30.162 1.00 33.20 ? 201 SER A OG 1 ATOM 1570 N N . ARG A 1 202 ? 19.266 20.298 32.187 1.00 26.37 ? 202 ARG A N 1 ATOM 1571 C CA . ARG A 1 202 ? 18.938 20.605 33.546 1.00 27.23 ? 202 ARG A CA 1 ATOM 1572 C C . ARG A 1 202 ? 19.304 19.496 34.497 1.00 26.12 ? 202 ARG A C 1 ATOM 1573 O O . ARG A 1 202 ? 19.582 19.753 35.610 1.00 27.74 ? 202 ARG A O 1 ATOM 1574 C CB . ARG A 1 202 ? 17.485 20.917 33.674 1.00 35.52 ? 202 ARG A CB 1 ATOM 1575 C CG . ARG A 1 202 ? 17.187 22.356 33.438 1.00 43.01 ? 202 ARG A CG 1 ATOM 1576 C CD . ARG A 1 202 ? 15.749 22.669 33.754 1.00 53.98 ? 202 ARG A CD 1 ATOM 1577 N NE . ARG A 1 202 ? 14.950 22.784 32.555 1.00 61.17 ? 202 ARG A NE 1 ATOM 1578 C CZ . ARG A 1 202 ? 14.048 21.881 32.183 1.00 69.45 ? 202 ARG A CZ 1 ATOM 1579 N NH1 . ARG A 1 202 ? 13.358 22.031 31.070 1.00 73.49 ? 202 ARG A NH1 1 ATOM 1580 N NH2 . ARG A 1 202 ? 13.845 20.815 32.936 1.00 62.90 ? 202 ARG A NH2 1 ATOM 1581 N N . LEU A 1 203 ? 19.315 18.268 34.025 1.00 24.12 ? 203 LEU A N 1 ATOM 1582 C CA . LEU A 1 203 ? 19.636 17.097 34.863 1.00 23.74 ? 203 LEU A CA 1 ATOM 1583 C C . LEU A 1 203 ? 21.122 16.934 35.124 1.00 25.21 ? 203 LEU A C 1 ATOM 1584 O O . LEU A 1 203 ? 21.516 16.190 36.015 1.00 23.29 ? 203 LEU A O 1 ATOM 1585 C CB . LEU A 1 203 ? 19.086 15.810 34.214 1.00 24.42 ? 203 LEU A CB 1 ATOM 1586 C CG . LEU A 1 203 ? 17.560 15.561 34.196 1.00 24.96 ? 203 LEU A CG 1 ATOM 1587 C CD1 . LEU A 1 203 ? 17.204 14.329 33.372 1.00 24.05 ? 203 LEU A CD1 1 ATOM 1588 C CD2 . LEU A 1 203 ? 17.008 15.365 35.611 1.00 26.88 ? 203 LEU A CD2 1 ATOM 1589 N N . ARG A 1 204 ? 21.932 17.584 34.317 1.00 25.45 ? 204 ARG A N 1 ATOM 1590 C CA . ARG A 1 204 ? 23.354 17.471 34.371 1.00 25.09 ? 204 ARG A CA 1 ATOM 1591 C C . ARG A 1 204 ? 23.927 18.382 35.443 1.00 26.04 ? 204 ARG A C 1 ATOM 1592 O O . ARG A 1 204 ? 23.358 19.386 35.742 1.00 23.97 ? 204 ARG A O 1 ATOM 1593 C CB . ARG A 1 204 ? 23.961 17.851 33.024 1.00 25.19 ? 204 ARG A CB 1 ATOM 1594 C CG . ARG A 1 204 ? 23.963 16.766 31.986 1.00 24.88 ? 204 ARG A CG 1 ATOM 1595 C CD . ARG A 1 204 ? 24.584 17.242 30.703 1.00 26.56 ? 204 ARG A CD 1 ATOM 1596 N NE . ARG A 1 204 ? 26.012 17.297 30.779 1.00 28.50 ? 204 ARG A NE 1 ATOM 1597 C CZ . ARG A 1 204 ? 26.820 17.674 29.798 1.00 34.51 ? 204 ARG A CZ 1 ATOM 1598 N NH1 . ARG A 1 204 ? 26.365 18.045 28.638 1.00 30.54 ? 204 ARG A NH1 1 ATOM 1599 N NH2 . ARG A 1 204 ? 28.109 17.685 30.015 1.00 39.13 ? 204 ARG A NH2 1 ATOM 1600 N N . ASN A 1 205 ? 25.043 17.972 36.015 1.00 27.52 ? 205 ASN A N 1 ATOM 1601 C CA . ASN A 1 205 ? 25.804 18.862 36.870 1.00 30.51 ? 205 ASN A CA 1 ATOM 1602 C C . ASN A 1 205 ? 26.807 19.607 35.961 1.00 28.96 ? 205 ASN A C 1 ATOM 1603 O O . ASN A 1 205 ? 27.859 19.074 35.608 1.00 27.49 ? 205 ASN A O 1 ATOM 1604 C CB . ASN A 1 205 ? 26.540 18.090 37.968 1.00 30.48 ? 205 ASN A CB 1 ATOM 1605 C CG . ASN A 1 205 ? 27.202 19.014 38.980 1.00 30.92 ? 205 ASN A CG 1 ATOM 1606 O OD1 . ASN A 1 205 ? 27.299 20.246 38.769 1.00 31.80 ? 205 ASN A OD1 1 ATOM 1607 N ND2 . ASN A 1 205 ? 27.653 18.437 40.099 1.00 31.59 ? 205 ASN A ND2 1 ATOM 1608 N N . LEU A 1 206 ? 26.429 20.799 35.546 1.00 31.39 ? 206 LEU A N 1 ATOM 1609 C CA . LEU A 1 206 ? 27.280 21.637 34.745 1.00 40.33 ? 206 LEU A CA 1 ATOM 1610 C C . LEU A 1 206 ? 28.120 22.588 35.601 1.00 42.21 ? 206 LEU A C 1 ATOM 1611 O O . LEU A 1 206 ? 28.772 23.447 35.062 1.00 40.81 ? 206 LEU A O 1 ATOM 1612 C CB . LEU A 1 206 ? 26.439 22.461 33.777 1.00 40.58 ? 206 LEU A CB 1 ATOM 1613 C CG . LEU A 1 206 ? 25.628 21.618 32.801 1.00 41.75 ? 206 LEU A CG 1 ATOM 1614 C CD1 . LEU A 1 206 ? 24.791 22.485 31.875 1.00 40.35 ? 206 LEU A CD1 1 ATOM 1615 C CD2 . LEU A 1 206 ? 26.507 20.680 31.998 1.00 41.84 ? 206 LEU A CD2 1 ATOM 1616 N N . SER A 1 207 ? 28.048 22.469 36.919 1.00 42.85 ? 207 SER A N 1 ATOM 1617 C CA . SER A 1 207 ? 28.825 23.316 37.800 1.00 45.89 ? 207 SER A CA 1 ATOM 1618 C C . SER A 1 207 ? 30.243 22.845 37.948 1.00 50.41 ? 207 SER A C 1 ATOM 1619 O O . SER A 1 207 ? 31.097 23.592 38.438 1.00 52.22 ? 207 SER A O 1 ATOM 1620 C CB . SER A 1 207 ? 28.218 23.370 39.191 1.00 47.28 ? 207 SER A CB 1 ATOM 1621 O OG . SER A 1 207 ? 27.095 24.221 39.178 1.00 55.23 ? 207 SER A OG 1 ATOM 1622 N N . SER A 1 208 ? 30.479 21.594 37.581 1.00 46.83 ? 208 SER A N 1 ATOM 1623 C CA . SER A 1 208 ? 31.790 21.017 37.625 1.00 46.64 ? 208 SER A CA 1 ATOM 1624 C C . SER A 1 208 ? 32.000 20.460 36.230 1.00 40.67 ? 208 SER A C 1 ATOM 1625 O O . SER A 1 208 ? 31.056 20.045 35.593 1.00 41.06 ? 208 SER A O 1 ATOM 1626 C CB . SER A 1 208 ? 31.868 19.923 38.704 1.00 44.70 ? 208 SER A CB 1 ATOM 1627 O OG . SER A 1 208 ? 30.924 18.889 38.493 1.00 40.42 ? 208 SER A OG 1 ATOM 1628 N N . PRO A 1 209 ? 33.230 20.505 35.718 1.00 39.92 ? 209 PRO A N 1 ATOM 1629 C CA . PRO A 1 209 ? 33.507 19.893 34.427 1.00 36.74 ? 209 PRO A CA 1 ATOM 1630 C C . PRO A 1 209 ? 33.757 18.377 34.542 1.00 33.72 ? 209 PRO A C 1 ATOM 1631 O O . PRO A 1 209 ? 34.627 17.852 33.874 1.00 34.63 ? 209 PRO A O 1 ATOM 1632 C CB . PRO A 1 209 ? 34.767 20.644 33.967 1.00 41.77 ? 209 PRO A CB 1 ATOM 1633 C CG . PRO A 1 209 ? 35.486 20.938 35.250 1.00 38.62 ? 209 PRO A CG 1 ATOM 1634 C CD . PRO A 1 209 ? 34.393 21.250 36.239 1.00 40.06 ? 209 PRO A CD 1 ATOM 1635 N N . LEU A 1 210 ? 32.988 17.669 35.367 1.00 31.67 ? 210 LEU A N 1 ATOM 1636 C CA . LEU A 1 210 ? 33.291 16.282 35.674 1.00 31.17 ? 210 LEU A CA 1 ATOM 1637 C C . LEU A 1 210 ? 32.292 15.315 35.037 1.00 31.24 ? 210 LEU A C 1 ATOM 1638 O O . LEU A 1 210 ? 32.299 14.123 35.345 1.00 33.34 ? 210 LEU A O 1 ATOM 1639 C CB . LEU A 1 210 ? 33.296 16.119 37.207 1.00 34.94 ? 210 LEU A CB 1 ATOM 1640 C CG . LEU A 1 210 ? 34.294 17.028 37.948 1.00 36.84 ? 210 LEU A CG 1 ATOM 1641 C CD1 . LEU A 1 210 ? 34.262 16.831 39.461 1.00 34.98 ? 210 LEU A CD1 1 ATOM 1642 C CD2 . LEU A 1 210 ? 35.692 16.731 37.410 1.00 38.39 ? 210 LEU A CD2 1 ATOM 1643 N N . GLY A 1 211 ? 31.439 15.847 34.165 1.00 31.08 ? 211 GLY A N 1 ATOM 1644 C CA . GLY A 1 211 ? 30.407 15.070 33.454 1.00 33.74 ? 211 GLY A CA 1 ATOM 1645 C C . GLY A 1 211 ? 29.370 14.359 34.341 1.00 32.61 ? 211 GLY A C 1 ATOM 1646 O O . GLY A 1 211 ? 28.813 13.341 33.948 1.00 31.42 ? 211 GLY A O 1 ATOM 1647 N N . LEU A 1 212 ? 29.146 14.875 35.550 1.00 30.06 ? 212 LEU A N 1 ATOM 1648 C CA . LEU A 1 212 ? 28.266 14.213 36.507 1.00 27.92 ? 212 LEU A CA 1 ATOM 1649 C C . LEU A 1 212 ? 26.821 14.567 36.184 1.00 25.60 ? 212 LEU A C 1 ATOM 1650 O O . LEU A 1 212 ? 26.570 15.571 35.582 1.00 20.85 ? 212 LEU A O 1 ATOM 1651 C CB . LEU A 1 212 ? 28.583 14.640 37.933 1.00 25.53 ? 212 LEU A CB 1 ATOM 1652 C CG . LEU A 1 212 ? 30.028 14.370 38.398 1.00 24.91 ? 212 LEU A CG 1 ATOM 1653 C CD1 . LEU A 1 212 ? 30.354 15.177 39.651 1.00 24.98 ? 212 LEU A CD1 1 ATOM 1654 C CD2 . LEU A 1 212 ? 30.314 12.887 38.603 1.00 27.37 ? 212 LEU A CD2 1 ATOM 1655 N N . MET A 1 213 ? 25.896 13.749 36.637 1.00 25.94 ? 213 MET A N 1 ATOM 1656 C CA . MET A 1 213 ? 24.503 14.148 36.689 1.00 25.73 ? 213 MET A CA 1 ATOM 1657 C C . MET A 1 213 ? 24.281 14.803 38.052 1.00 25.46 ? 213 MET A C 1 ATOM 1658 O O . MET A 1 213 ? 24.846 14.370 39.074 1.00 28.83 ? 213 MET A O 1 ATOM 1659 C CB . MET A 1 213 ? 23.621 12.919 36.549 1.00 23.71 ? 213 MET A CB 1 ATOM 1660 C CG . MET A 1 213 ? 23.668 12.219 35.199 1.00 21.74 ? 213 MET A CG 1 ATOM 1661 S SD . MET A 1 213 ? 22.850 13.206 33.964 1.00 22.83 ? 213 MET A SD 1 ATOM 1662 C CE . MET A 1 213 ? 21.128 12.839 34.293 1.00 23.33 ? 213 MET A CE 1 ATOM 1663 N N . ALA A 1 214 ? 23.413 15.799 38.066 1.00 23.05 ? 214 ALA A N 1 ATOM 1664 C CA . ALA A 1 214 ? 22.988 16.451 39.297 1.00 24.38 ? 214 ALA A CA 1 ATOM 1665 C C . ALA A 1 214 ? 22.394 15.479 40.287 1.00 25.20 ? 214 ALA A C 1 ATOM 1666 O O . ALA A 1 214 ? 21.679 14.520 39.877 1.00 22.69 ? 214 ALA A O 1 ATOM 1667 C CB . ALA A 1 214 ? 21.943 17.513 38.972 1.00 25.48 ? 214 ALA A CB 1 ATOM 1668 N N . VAL A 1 215 ? 22.685 15.705 41.576 1.00 23.34 ? 215 VAL A N 1 ATOM 1669 C CA . VAL A 1 215 ? 22.134 14.861 42.651 1.00 23.32 ? 215 VAL A CA 1 ATOM 1670 C C . VAL A 1 215 ? 21.491 15.723 43.714 1.00 24.48 ? 215 VAL A C 1 ATOM 1671 O O . VAL A 1 215 ? 21.701 16.926 43.772 1.00 22.27 ? 215 VAL A O 1 ATOM 1672 C CB . VAL A 1 215 ? 23.168 13.915 43.273 1.00 23.97 ? 215 VAL A CB 1 ATOM 1673 C CG1 . VAL A 1 215 ? 23.781 13.038 42.190 1.00 24.36 ? 215 VAL A CG1 1 ATOM 1674 C CG2 . VAL A 1 215 ? 24.257 14.662 44.050 1.00 27.45 ? 215 VAL A CG2 1 ATOM 1675 N N . ASN A 1 216 ? 20.634 15.106 44.524 1.00 24.80 ? 216 ASN A N 1 ATOM 1676 C CA . ASN A 1 216 ? 19.914 15.843 45.585 1.00 24.34 ? 216 ASN A CA 1 ATOM 1677 C C . ASN A 1 216 ? 20.931 16.472 46.547 1.00 26.28 ? 216 ASN A C 1 ATOM 1678 O O . ASN A 1 216 ? 21.951 15.832 46.913 1.00 22.59 ? 216 ASN A O 1 ATOM 1679 C CB . ASN A 1 216 ? 19.059 14.873 46.360 1.00 26.20 ? 216 ASN A CB 1 ATOM 1680 C CG . ASN A 1 216 ? 17.868 15.513 47.005 1.00 27.30 ? 216 ASN A CG 1 ATOM 1681 O OD1 . ASN A 1 216 ? 17.996 16.175 48.026 1.00 27.54 ? 216 ASN A OD1 1 ATOM 1682 N ND2 . ASN A 1 216 ? 16.692 15.278 46.447 1.00 26.99 ? 216 ASN A ND2 1 ATOM 1683 N N . GLN A 1 217 ? 20.656 17.721 46.924 1.00 25.60 ? 217 GLN A N 1 ATOM 1684 C CA . GLN A 1 217 ? 21.480 18.471 47.890 1.00 28.68 ? 217 GLN A CA 1 ATOM 1685 C C . GLN A 1 217 ? 20.822 18.562 49.278 1.00 29.80 ? 217 GLN A C 1 ATOM 1686 O O . GLN A 1 217 ? 21.380 19.132 50.196 1.00 29.68 ? 217 GLN A O 1 ATOM 1687 C CB . GLN A 1 217 ? 21.730 19.887 47.378 1.00 31.89 ? 217 GLN A CB 1 ATOM 1688 C CG . GLN A 1 217 ? 22.481 19.955 46.066 1.00 34.81 ? 217 GLN A CG 1 ATOM 1689 C CD . GLN A 1 217 ? 23.824 19.266 46.106 1.00 39.33 ? 217 GLN A CD 1 ATOM 1690 O OE1 . GLN A 1 217 ? 24.738 19.683 46.840 1.00 45.64 ? 217 GLN A OE1 1 ATOM 1691 N NE2 . GLN A 1 217 ? 23.980 18.203 45.298 1.00 42.90 ? 217 GLN A NE2 1 ATOM 1692 N N . GLU A 1 218 ? 19.649 17.963 49.435 1.00 29.93 ? 218 GLU A N 1 ATOM 1693 C CA . GLU A 1 218 ? 18.929 18.009 50.671 1.00 32.57 ? 218 GLU A CA 1 ATOM 1694 C C . GLU A 1 218 ? 18.990 16.672 51.395 1.00 34.91 ? 218 GLU A C 1 ATOM 1695 O O . GLU A 1 218 ? 18.884 16.650 52.603 1.00 37.56 ? 218 GLU A O 1 ATOM 1696 C CB . GLU A 1 218 ? 17.479 18.371 50.390 1.00 37.32 ? 218 GLU A CB 1 ATOM 1697 C CG . GLU A 1 218 ? 17.325 19.744 49.772 1.00 45.48 ? 218 GLU A CG 1 ATOM 1698 C CD . GLU A 1 218 ? 15.881 20.104 49.475 1.00 51.44 ? 218 GLU A CD 1 ATOM 1699 O OE1 . GLU A 1 218 ? 14.991 19.618 50.210 1.00 56.74 ? 218 GLU A OE1 1 ATOM 1700 O OE2 . GLU A 1 218 ? 15.638 20.857 48.499 1.00 53.22 ? 218 GLU A OE2 1 ATOM 1701 N N . ALA A 1 219 ? 19.214 15.579 50.675 1.00 29.30 ? 219 ALA A N 1 ATOM 1702 C CA . ALA A 1 219 ? 19.245 14.249 51.279 1.00 29.88 ? 219 ALA A CA 1 ATOM 1703 C C . ALA A 1 219 ? 20.236 13.326 50.613 1.00 29.52 ? 219 ALA A C 1 ATOM 1704 O O . ALA A 1 219 ? 20.517 13.466 49.428 1.00 28.57 ? 219 ALA A O 1 ATOM 1705 C CB . ALA A 1 219 ? 17.875 13.645 51.236 1.00 30.26 ? 219 ALA A CB 1 ATOM 1706 N N . TRP A 1 220 ? 20.748 12.379 51.403 1.00 26.04 ? 220 TRP A N 1 ATOM 1707 C CA . TRP A 1 220 ? 21.719 11.422 51.025 1.00 24.86 ? 220 TRP A CA 1 ATOM 1708 C C . TRP A 1 220 ? 21.306 10.130 51.723 1.00 25.20 ? 220 TRP A C 1 ATOM 1709 O O . TRP A 1 220 ? 20.626 10.176 52.715 1.00 23.38 ? 220 TRP A O 1 ATOM 1710 C CB . TRP A 1 220 ? 23.095 11.913 51.504 1.00 27.76 ? 220 TRP A CB 1 ATOM 1711 C CG . TRP A 1 220 ? 23.516 13.190 50.808 1.00 31.25 ? 220 TRP A CG 1 ATOM 1712 C CD1 . TRP A 1 220 ? 23.204 14.480 51.178 1.00 33.84 ? 220 TRP A CD1 1 ATOM 1713 C CD2 . TRP A 1 220 ? 24.283 13.286 49.618 1.00 34.78 ? 220 TRP A CD2 1 ATOM 1714 N NE1 . TRP A 1 220 ? 23.758 15.363 50.289 1.00 37.86 ? 220 TRP A NE1 1 ATOM 1715 C CE2 . TRP A 1 220 ? 24.423 14.658 49.317 1.00 41.06 ? 220 TRP A CE2 1 ATOM 1716 C CE3 . TRP A 1 220 ? 24.892 12.336 48.770 1.00 44.36 ? 220 TRP A CE3 1 ATOM 1717 C CZ2 . TRP A 1 220 ? 25.130 15.122 48.170 1.00 43.18 ? 220 TRP A CZ2 1 ATOM 1718 C CZ3 . TRP A 1 220 ? 25.624 12.793 47.635 1.00 42.26 ? 220 TRP A CZ3 1 ATOM 1719 C CH2 . TRP A 1 220 ? 25.724 14.172 47.357 1.00 45.14 ? 220 TRP A CH2 1 ATOM 1720 N N . ASP A 1 221 ? 21.799 8.998 51.260 1.00 22.29 ? 221 ASP A N 1 ATOM 1721 C CA . ASP A 1 221 ? 21.406 7.634 51.724 1.00 24.60 ? 221 ASP A CA 1 ATOM 1722 C C . ASP A 1 221 ? 22.699 7.028 52.225 1.00 25.71 ? 221 ASP A C 1 ATOM 1723 O O . ASP A 1 221 ? 23.426 6.355 51.459 1.00 24.92 ? 221 ASP A O 1 ATOM 1724 C CB . ASP A 1 221 ? 20.859 6.861 50.503 1.00 22.61 ? 221 ASP A CB 1 ATOM 1725 C CG . ASP A 1 221 ? 20.409 5.442 50.805 1.00 24.80 ? 221 ASP A CG 1 ATOM 1726 O OD1 . ASP A 1 221 ? 20.426 4.956 51.969 1.00 24.19 ? 221 ASP A OD1 1 ATOM 1727 O OD2 . ASP A 1 221 ? 19.961 4.764 49.840 1.00 27.74 ? 221 ASP A OD2 1 ATOM 1728 N N . HIS A 1 222 ? 23.079 7.326 53.471 1.00 28.03 ? 222 HIS A N 1 ATOM 1729 C CA . HIS A 1 222 ? 24.349 6.813 54.005 1.00 27.05 ? 222 HIS A CA 1 ATOM 1730 C C . HIS A 1 222 ? 25.507 7.298 53.143 1.00 26.62 ? 222 HIS A C 1 ATOM 1731 O O . HIS A 1 222 ? 26.377 6.530 52.721 1.00 25.62 ? 222 HIS A O 1 ATOM 1732 C CB . HIS A 1 222 ? 24.346 5.269 54.129 1.00 27.96 ? 222 HIS A CB 1 ATOM 1733 C CG . HIS A 1 222 ? 23.222 4.719 54.947 1.00 30.33 ? 222 HIS A CG 1 ATOM 1734 N ND1 . HIS A 1 222 ? 22.191 3.987 54.397 1.00 33.45 ? 222 HIS A ND1 1 ATOM 1735 C CD2 . HIS A 1 222 ? 22.953 4.806 56.273 1.00 31.03 ? 222 HIS A CD2 1 ATOM 1736 C CE1 . HIS A 1 222 ? 21.328 3.660 55.341 1.00 31.67 ? 222 HIS A CE1 1 ATOM 1737 N NE2 . HIS A 1 222 ? 21.758 4.162 56.484 1.00 33.90 ? 222 HIS A NE2 1 ATOM 1738 N N . GLY A 1 223 ? 25.495 8.588 52.826 1.00 25.98 ? 223 GLY A N 1 ATOM 1739 C CA . GLY A 1 223 ? 26.487 9.092 51.893 1.00 28.25 ? 223 GLY A CA 1 ATOM 1740 C C . GLY A 1 223 ? 26.307 8.823 50.394 1.00 29.07 ? 223 GLY A C 1 ATOM 1741 O O . GLY A 1 223 ? 27.061 9.368 49.601 1.00 30.21 ? 223 GLY A O 1 ATOM 1742 N N . LEU A 1 224 ? 25.322 8.036 49.968 1.00 26.26 ? 224 LEU A N 1 ATOM 1743 C CA . LEU A 1 224 ? 25.114 7.834 48.531 1.00 25.46 ? 224 LEU A CA 1 ATOM 1744 C C . LEU A 1 224 ? 24.004 8.728 48.001 1.00 25.50 ? 224 LEU A C 1 ATOM 1745 O O . LEU A 1 224 ? 23.120 9.161 48.722 1.00 26.38 ? 224 LEU A O 1 ATOM 1746 C CB . LEU A 1 224 ? 24.840 6.347 48.264 1.00 28.90 ? 224 LEU A CB 1 ATOM 1747 C CG . LEU A 1 224 ? 25.834 5.334 48.835 1.00 29.58 ? 224 LEU A CG 1 ATOM 1748 C CD1 . LEU A 1 224 ? 25.468 3.876 48.557 1.00 30.03 ? 224 LEU A CD1 1 ATOM 1749 C CD2 . LEU A 1 224 ? 27.209 5.611 48.256 1.00 30.83 ? 224 LEU A CD2 1 ATOM 1750 N N . ALA A 1 225 ? 24.033 8.993 46.701 1.00 27.80 ? 225 ALA A N 1 ATOM 1751 C CA . ALA A 1 225 ? 23.198 10.034 46.107 1.00 23.01 ? 225 ALA A CA 1 ATOM 1752 C C . ALA A 1 225 ? 21.759 9.655 45.922 1.00 21.58 ? 225 ALA A C 1 ATOM 1753 O O . ALA A 1 225 ? 21.398 8.472 45.750 1.00 20.73 ? 225 ALA A O 1 ATOM 1754 C CB . ALA A 1 225 ? 23.792 10.507 44.774 1.00 24.27 ? 225 ALA A CB 1 ATOM 1755 N N . TYR A 1 226 ? 20.917 10.689 45.917 1.00 19.09 ? 226 TYR A N 1 ATOM 1756 C CA . TYR A 1 226 ? 19.554 10.537 45.424 1.00 19.83 ? 226 TYR A CA 1 ATOM 1757 C C . TYR A 1 226 ? 19.377 11.419 44.214 1.00 21.50 ? 226 TYR A C 1 ATOM 1758 O O . TYR A 1 226 ? 20.119 12.400 44.038 1.00 19.37 ? 226 TYR A O 1 ATOM 1759 C CB . TYR A 1 226 ? 18.544 10.982 46.474 1.00 19.81 ? 226 TYR A CB 1 ATOM 1760 C CG . TYR A 1 226 ? 18.344 10.065 47.637 1.00 18.81 ? 226 TYR A CG 1 ATOM 1761 C CD1 . TYR A 1 226 ? 17.927 8.769 47.451 1.00 19.60 ? 226 TYR A CD1 1 ATOM 1762 C CD2 . TYR A 1 226 ? 18.535 10.513 48.974 1.00 20.46 ? 226 TYR A CD2 1 ATOM 1763 C CE1 . TYR A 1 226 ? 17.702 7.932 48.519 1.00 19.47 ? 226 TYR A CE1 1 ATOM 1764 C CE2 . TYR A 1 226 ? 18.325 9.661 50.053 1.00 20.84 ? 226 TYR A CE2 1 ATOM 1765 C CZ . TYR A 1 226 ? 17.925 8.360 49.813 1.00 19.08 ? 226 TYR A CZ 1 ATOM 1766 O OH . TYR A 1 226 ? 17.635 7.484 50.851 1.00 24.08 ? 226 TYR A OH 1 ATOM 1767 N N . PRO A 1 227 ? 18.317 11.189 43.444 1.00 20.70 ? 227 PRO A N 1 ATOM 1768 C CA . PRO A 1 227 ? 18.062 12.129 42.398 1.00 20.47 ? 227 PRO A CA 1 ATOM 1769 C C . PRO A 1 227 ? 17.676 13.484 42.978 1.00 23.58 ? 227 PRO A C 1 ATOM 1770 O O . PRO A 1 227 ? 17.191 13.539 44.088 1.00 20.51 ? 227 PRO A O 1 ATOM 1771 C CB . PRO A 1 227 ? 16.856 11.523 41.693 1.00 21.09 ? 227 PRO A CB 1 ATOM 1772 C CG . PRO A 1 227 ? 16.952 10.095 41.965 1.00 20.69 ? 227 PRO A CG 1 ATOM 1773 C CD . PRO A 1 227 ? 17.441 10.019 43.359 1.00 23.48 ? 227 PRO A CD 1 ATOM 1774 N N . PRO A 1 228 ? 17.860 14.569 42.192 1.00 23.80 ? 228 PRO A N 1 ATOM 1775 C CA . PRO A 1 228 ? 17.294 15.798 42.665 1.00 24.28 ? 228 PRO A CA 1 ATOM 1776 C C . PRO A 1 228 ? 15.798 15.731 42.858 1.00 23.55 ? 228 PRO A C 1 ATOM 1777 O O . PRO A 1 228 ? 15.129 14.813 42.307 1.00 24.35 ? 228 PRO A O 1 ATOM 1778 C CB . PRO A 1 228 ? 17.659 16.818 41.573 1.00 24.19 ? 228 PRO A CB 1 ATOM 1779 C CG . PRO A 1 228 ? 18.680 16.148 40.715 1.00 23.38 ? 228 PRO A CG 1 ATOM 1780 C CD . PRO A 1 228 ? 18.391 14.689 40.830 1.00 23.53 ? 228 PRO A CD 1 ATOM 1781 N N . PHE A 1 229 ? 15.276 16.653 43.664 1.00 23.52 ? 229 PHE A N 1 ATOM 1782 C CA . PHE A 1 229 ? 13.822 16.806 43.809 1.00 23.25 ? 229 PHE A CA 1 ATOM 1783 C C . PHE A 1 229 ? 13.266 17.600 42.659 1.00 24.16 ? 229 PHE A C 1 ATOM 1784 O O . PHE A 1 229 ? 13.889 18.534 42.143 1.00 25.29 ? 229 PHE A O 1 ATOM 1785 C CB . PHE A 1 229 ? 13.425 17.464 45.099 1.00 23.68 ? 229 PHE A CB 1 ATOM 1786 C CG . PHE A 1 229 ? 13.575 16.585 46.308 1.00 26.41 ? 229 PHE A CG 1 ATOM 1787 C CD1 . PHE A 1 229 ? 13.210 15.203 46.275 1.00 26.48 ? 229 PHE A CD1 1 ATOM 1788 C CD2 . PHE A 1 229 ? 14.049 17.120 47.505 1.00 24.34 ? 229 PHE A CD2 1 ATOM 1789 C CE1 . PHE A 1 229 ? 13.357 14.413 47.389 1.00 24.19 ? 229 PHE A CE1 1 ATOM 1790 C CE2 . PHE A 1 229 ? 14.165 16.316 48.627 1.00 24.05 ? 229 PHE A CE2 1 ATOM 1791 C CZ . PHE A 1 229 ? 13.819 14.976 48.591 1.00 23.24 ? 229 PHE A CZ 1 ATOM 1792 N N . ASN A 1 230 ? 12.105 17.197 42.195 1.00 26.06 ? 230 ASN A N 1 ATOM 1793 C CA . ASN A 1 230 ? 11.369 18.073 41.348 1.00 28.88 ? 230 ASN A CA 1 ATOM 1794 C C . ASN A 1 230 ? 10.582 19.107 42.213 1.00 31.29 ? 230 ASN A C 1 ATOM 1795 O O . ASN A 1 230 ? 9.615 18.754 42.868 1.00 31.77 ? 230 ASN A O 1 ATOM 1796 C CB . ASN A 1 230 ? 10.450 17.295 40.470 1.00 29.96 ? 230 ASN A CB 1 ATOM 1797 C CG . ASN A 1 230 ? 9.703 18.223 39.581 1.00 34.78 ? 230 ASN A CG 1 ATOM 1798 O OD1 . ASN A 1 230 ? 10.220 19.291 39.263 1.00 41.58 ? 230 ASN A OD1 1 ATOM 1799 N ND2 . ASN A 1 230 ? 8.475 17.892 39.241 1.00 38.74 ? 230 ASN A ND2 1 ATOM 1800 N N . ASN A 1 231 ? 10.975 20.374 42.186 1.00 31.78 ? 231 ASN A N 1 ATOM 1801 C CA . ASN A 1 231 ? 10.497 21.333 43.207 1.00 35.76 ? 231 ASN A CA 1 ATOM 1802 C C . ASN A 1 231 ? 9.315 22.193 42.774 1.00 39.74 ? 231 ASN A C 1 ATOM 1803 O O . ASN A 1 231 ? 9.150 23.283 43.232 1.00 43.60 ? 231 ASN A O 1 ATOM 1804 C CB . ASN A 1 231 ? 11.655 22.194 43.758 1.00 35.91 ? 231 ASN A CB 1 ATOM 1805 C CG . ASN A 1 231 ? 12.606 21.408 44.686 1.00 37.02 ? 231 ASN A CG 1 ATOM 1806 O OD1 . ASN A 1 231 ? 12.170 20.670 45.571 1.00 38.51 ? 231 ASN A OD1 1 ATOM 1807 N ND2 . ASN A 1 231 ? 13.890 21.548 44.460 1.00 36.34 ? 231 ASN A ND2 1 ATOM 1808 N N . VAL A 1 232 ? 8.470 21.673 41.890 1.00 45.97 ? 232 VAL A N 1 ATOM 1809 C CA . VAL A 1 232 ? 7.146 22.254 41.645 1.00 44.52 ? 232 VAL A CA 1 ATOM 1810 C C . VAL A 1 232 ? 6.219 22.134 42.849 1.00 46.25 ? 232 VAL A C 1 ATOM 1811 O O . VAL A 1 232 ? 6.281 21.157 43.593 1.00 48.18 ? 232 VAL A O 1 ATOM 1812 C CB . VAL A 1 232 ? 6.397 21.527 40.510 1.00 41.26 ? 232 VAL A CB 1 ATOM 1813 C CG1 . VAL A 1 232 ? 7.242 21.555 39.237 1.00 44.47 ? 232 VAL A CG1 1 ATOM 1814 C CG2 . VAL A 1 232 ? 6.048 20.102 40.937 1.00 38.37 ? 232 VAL A CG2 1 ATOM 1815 N N . LYS A 1 233 ? 5.354 23.125 43.012 1.00 46.81 ? 233 LYS A N 1 ATOM 1816 C CA . LYS A 1 233 ? 4.147 22.939 43.792 1.00 51.14 ? 233 LYS A CA 1 ATOM 1817 C C . LYS A 1 233 ? 2.966 23.025 42.819 1.00 47.64 ? 233 LYS A C 1 ATOM 1818 O O . LYS A 1 233 ? 2.973 23.859 41.934 1.00 56.26 ? 233 LYS A O 1 ATOM 1819 C CB . LYS A 1 233 ? 4.020 24.020 44.877 1.00 50.97 ? 233 LYS A CB 1 ATOM 1820 C CG . LYS A 1 233 ? 5.175 24.135 45.871 1.00 52.62 ? 233 LYS A CG 1 ATOM 1821 C CD . LYS A 1 233 ? 5.139 23.032 46.935 1.00 54.04 ? 233 LYS A CD 1 ATOM 1822 C CE . LYS A 1 233 ? 6.526 22.640 47.443 1.00 55.28 ? 233 LYS A CE 1 ATOM 1823 N NZ . LYS A 1 233 ? 6.915 23.199 48.770 1.00 56.59 ? 233 LYS A NZ 1 ATOM 1824 N N . PRO A 1 234 ? 1.950 22.163 42.958 1.00 51.02 ? 234 PRO A N 1 ATOM 1825 C CA . PRO A 1 234 ? 1.796 21.057 43.880 1.00 44.96 ? 234 PRO A CA 1 ATOM 1826 C C . PRO A 1 234 ? 2.483 19.806 43.330 1.00 43.47 ? 234 PRO A C 1 ATOM 1827 O O . PRO A 1 234 ? 2.749 19.710 42.142 1.00 45.22 ? 234 PRO A O 1 ATOM 1828 C CB . PRO A 1 234 ? 0.286 20.861 43.944 1.00 46.76 ? 234 PRO A CB 1 ATOM 1829 C CG . PRO A 1 234 ? -0.225 21.338 42.631 1.00 48.76 ? 234 PRO A CG 1 ATOM 1830 C CD . PRO A 1 234 ? 0.805 22.252 42.024 1.00 48.85 ? 234 PRO A CD 1 ATOM 1831 N N . SER A 1 235 ? 2.784 18.880 44.233 1.00 37.70 ? 235 SER A N 1 ATOM 1832 C CA . SER A 1 235 ? 3.450 17.588 43.953 1.00 29.35 ? 235 SER A CA 1 ATOM 1833 C C . SER A 1 235 ? 2.581 16.448 44.465 1.00 28.49 ? 235 SER A C 1 ATOM 1834 O O . SER A 1 235 ? 2.112 16.504 45.623 1.00 30.21 ? 235 SER A O 1 ATOM 1835 C CB . SER A 1 235 ? 4.794 17.626 44.697 1.00 27.40 ? 235 SER A CB 1 ATOM 1836 O OG . SER A 1 235 ? 5.377 16.346 44.907 1.00 25.40 ? 235 SER A OG 1 ATOM 1837 N N . PRO A 1 236 ? 2.361 15.383 43.644 1.00 23.34 ? 236 PRO A N 1 ATOM 1838 C CA . PRO A 1 236 ? 1.612 14.279 44.207 1.00 23.72 ? 236 PRO A CA 1 ATOM 1839 C C . PRO A 1 236 ? 2.372 13.565 45.315 1.00 24.81 ? 236 PRO A C 1 ATOM 1840 O O . PRO A 1 236 ? 1.730 12.952 46.174 1.00 24.45 ? 236 PRO A O 1 ATOM 1841 C CB . PRO A 1 236 ? 1.435 13.326 43.021 1.00 23.78 ? 236 PRO A CB 1 ATOM 1842 C CG . PRO A 1 236 ? 2.610 13.608 42.162 1.00 24.67 ? 236 PRO A CG 1 ATOM 1843 C CD . PRO A 1 236 ? 2.789 15.095 42.254 1.00 23.27 ? 236 PRO A CD 1 ATOM 1844 N N . CYS A 1 237 ? 3.714 13.548 45.225 1.00 21.62 ? 237 CYS A N 1 ATOM 1845 C CA . CYS A 1 237 ? 4.522 12.809 46.186 1.00 21.71 ? 237 CYS A CA 1 ATOM 1846 C C . CYS A 1 237 ? 4.461 13.522 47.561 1.00 21.48 ? 237 CYS A C 1 ATOM 1847 O O . CYS A 1 237 ? 4.540 12.873 48.600 1.00 21.00 ? 237 CYS A O 1 ATOM 1848 C CB . CYS A 1 237 ? 5.963 12.669 45.736 1.00 20.74 ? 237 CYS A CB 1 ATOM 1849 S SG . CYS A 1 237 ? 6.227 11.795 44.207 1.00 20.34 ? 237 CYS A SG 1 ATOM 1850 N N . GLU A 1 238 ? 4.293 14.838 47.543 1.00 20.02 ? 238 GLU A N 1 ATOM 1851 C CA . GLU A 1 238 ? 4.033 15.583 48.740 1.00 22.56 ? 238 GLU A CA 1 ATOM 1852 C C . GLU A 1 238 ? 2.594 15.348 49.231 1.00 24.05 ? 238 GLU A C 1 ATOM 1853 O O . GLU A 1 238 ? 2.347 15.210 50.417 1.00 22.25 ? 238 GLU A O 1 ATOM 1854 C CB . GLU A 1 238 ? 4.254 17.102 48.493 1.00 26.40 ? 238 GLU A CB 1 ATOM 1855 C CG . GLU A 1 238 ? 5.698 17.453 48.331 1.00 26.67 ? 238 GLU A CG 1 ATOM 1856 C CD . GLU A 1 238 ? 5.951 18.932 48.169 1.00 31.41 ? 238 GLU A CD 1 ATOM 1857 O OE1 . GLU A 1 238 ? 7.112 19.339 47.984 1.00 33.17 ? 238 GLU A OE1 1 ATOM 1858 O OE2 . GLU A 1 238 ? 5.006 19.700 48.208 1.00 30.73 ? 238 GLU A OE2 1 ATOM 1859 N N . PHE A 1 239 ? 1.637 15.343 48.296 1.00 24.75 ? 239 PHE A N 1 ATOM 1860 C CA . PHE A 1 239 ? 0.231 15.161 48.621 1.00 23.45 ? 239 PHE A CA 1 ATOM 1861 C C . PHE A 1 239 ? -0.039 13.916 49.420 1.00 22.35 ? 239 PHE A C 1 ATOM 1862 O O . PHE A 1 239 ? -0.852 13.915 50.330 1.00 21.80 ? 239 PHE A O 1 ATOM 1863 C CB . PHE A 1 239 ? -0.642 15.164 47.342 1.00 24.62 ? 239 PHE A CB 1 ATOM 1864 C CG . PHE A 1 239 ? -2.137 15.000 47.623 1.00 26.75 ? 239 PHE A CG 1 ATOM 1865 C CD1 . PHE A 1 239 ? -2.930 16.107 47.869 1.00 25.97 ? 239 PHE A CD1 1 ATOM 1866 C CD2 . PHE A 1 239 ? -2.739 13.748 47.615 1.00 29.10 ? 239 PHE A CD2 1 ATOM 1867 C CE1 . PHE A 1 239 ? -4.281 15.971 48.106 1.00 26.98 ? 239 PHE A CE1 1 ATOM 1868 C CE2 . PHE A 1 239 ? -4.096 13.587 47.890 1.00 30.83 ? 239 PHE A CE2 1 ATOM 1869 C CZ . PHE A 1 239 ? -4.877 14.714 48.117 1.00 30.08 ? 239 PHE A CZ 1 ATOM 1870 N N . ILE A 1 240 ? 0.626 12.822 49.131 1.00 22.10 ? 240 ILE A N 1 ATOM 1871 C CA . ILE A 1 240 ? 0.313 11.592 49.862 1.00 20.67 ? 240 ILE A CA 1 ATOM 1872 C C . ILE A 1 240 ? 0.784 11.573 51.344 1.00 22.82 ? 240 ILE A C 1 ATOM 1873 O O . ILE A 1 240 ? 0.402 10.702 52.102 1.00 22.86 ? 240 ILE A O 1 ATOM 1874 C CB . ILE A 1 240 ? 0.761 10.343 49.095 1.00 23.51 ? 240 ILE A CB 1 ATOM 1875 C CG1 . ILE A 1 240 ? 2.239 10.376 48.787 1.00 22.99 ? 240 ILE A CG1 1 ATOM 1876 C CG2 . ILE A 1 240 ? -0.039 10.215 47.820 1.00 23.27 ? 240 ILE A CG2 1 ATOM 1877 C CD1 . ILE A 1 240 ? 2.984 9.254 49.388 1.00 22.53 ? 240 ILE A CD1 1 ATOM 1878 N N . ASN A 1 241 ? 1.567 12.553 51.737 1.00 21.47 ? 241 ASN A N 1 ATOM 1879 C CA . ASN A 1 241 ? 1.942 12.748 53.123 1.00 23.77 ? 241 ASN A CA 1 ATOM 1880 C C . ASN A 1 241 ? 2.471 14.155 53.263 1.00 23.09 ? 241 ASN A C 1 ATOM 1881 O O . ASN A 1 241 ? 3.654 14.424 53.075 1.00 23.40 ? 241 ASN A O 1 ATOM 1882 C CB . ASN A 1 241 ? 2.973 11.751 53.612 1.00 25.43 ? 241 ASN A CB 1 ATOM 1883 C CG . ASN A 1 241 ? 3.218 11.894 55.110 1.00 28.06 ? 241 ASN A CG 1 ATOM 1884 O OD1 . ASN A 1 241 ? 3.059 12.968 55.665 1.00 27.72 ? 241 ASN A OD1 1 ATOM 1885 N ND2 . ASN A 1 241 ? 3.604 10.826 55.751 1.00 29.76 ? 241 ASN A ND2 1 ATOM 1886 N N . THR A 1 242 ? 1.565 15.064 53.587 1.00 27.42 ? 242 THR A N 1 ATOM 1887 C CA . THR A 1 242 ? 1.889 16.500 53.668 1.00 27.51 ? 242 THR A CA 1 ATOM 1888 C C . THR A 1 242 ? 2.798 16.830 54.873 1.00 28.34 ? 242 THR A C 1 ATOM 1889 O O . THR A 1 242 ? 3.516 17.822 54.859 1.00 31.76 ? 242 THR A O 1 ATOM 1890 C CB . THR A 1 242 ? 0.593 17.351 53.670 1.00 30.40 ? 242 THR A CB 1 ATOM 1891 O OG1 . THR A 1 242 ? -0.333 16.806 54.623 1.00 34.36 ? 242 THR A OG1 1 ATOM 1892 C CG2 . THR A 1 242 ? -0.101 17.324 52.283 1.00 30.01 ? 242 THR A CG2 1 ATOM 1893 N N . THR A 1 243 ? 2.740 16.021 55.922 1.00 28.75 ? 243 THR A N 1 ATOM 1894 C CA . THR A 1 243 ? 3.624 16.194 57.052 1.00 27.26 ? 243 THR A CA 1 ATOM 1895 C C . THR A 1 243 ? 5.074 15.914 56.664 1.00 27.51 ? 243 THR A C 1 ATOM 1896 O O . THR A 1 243 ? 5.967 16.677 57.020 1.00 26.80 ? 243 THR A O 1 ATOM 1897 C CB . THR A 1 243 ? 3.233 15.239 58.152 1.00 27.95 ? 243 THR A CB 1 ATOM 1898 O OG1 . THR A 1 243 ? 1.882 15.488 58.542 1.00 31.73 ? 243 THR A OG1 1 ATOM 1899 C CG2 . THR A 1 243 ? 4.142 15.398 59.358 1.00 29.29 ? 243 THR A CG2 1 ATOM 1900 N N . ALA A 1 244 ? 5.317 14.813 55.950 1.00 26.31 ? 244 ALA A N 1 ATOM 1901 C CA . ALA A 1 244 ? 6.662 14.580 55.420 1.00 26.45 ? 244 ALA A CA 1 ATOM 1902 C C . ALA A 1 244 ? 7.017 15.566 54.287 1.00 24.69 ? 244 ALA A C 1 ATOM 1903 O O . ALA A 1 244 ? 8.172 16.012 54.205 1.00 21.51 ? 244 ALA A O 1 ATOM 1904 C CB . ALA A 1 244 ? 6.848 13.157 54.990 1.00 29.93 ? 244 ALA A CB 1 ATOM 1905 N N . HIS A 1 245 ? 6.047 15.919 53.432 1.00 24.87 ? 245 HIS A N 1 ATOM 1906 C CA . HIS A 1 245 ? 6.231 16.800 52.260 1.00 24.33 ? 245 HIS A CA 1 ATOM 1907 C C . HIS A 1 245 ? 7.542 16.536 51.497 1.00 24.32 ? 245 HIS A C 1 ATOM 1908 O O . HIS A 1 245 ? 8.307 17.420 51.274 1.00 28.78 ? 245 HIS A O 1 ATOM 1909 C CB . HIS A 1 245 ? 6.001 18.311 52.574 1.00 29.52 ? 245 HIS A CB 1 ATOM 1910 C CG . HIS A 1 245 ? 6.894 18.866 53.640 1.00 31.92 ? 245 HIS A CG 1 ATOM 1911 N ND1 . HIS A 1 245 ? 8.141 19.393 53.376 1.00 34.07 ? 245 HIS A ND1 1 ATOM 1912 C CD2 . HIS A 1 245 ? 6.715 18.975 54.980 1.00 32.54 ? 245 HIS A CD2 1 ATOM 1913 C CE1 . HIS A 1 245 ? 8.709 19.759 54.510 1.00 35.74 ? 245 HIS A CE1 1 ATOM 1914 N NE2 . HIS A 1 245 ? 7.854 19.534 55.492 1.00 37.65 ? 245 HIS A NE2 1 ATOM 1915 N N . VAL A 1 246 ? 7.801 15.274 51.134 1.00 25.55 ? 246 VAL A N 1 ATOM 1916 C CA . VAL A 1 246 ? 8.959 14.933 50.292 1.00 22.09 ? 246 VAL A CA 1 ATOM 1917 C C . VAL A 1 246 ? 8.558 14.871 48.814 1.00 20.15 ? 246 VAL A C 1 ATOM 1918 O O . VAL A 1 246 ? 7.694 14.061 48.445 1.00 19.40 ? 246 VAL A O 1 ATOM 1919 C CB . VAL A 1 246 ? 9.470 13.571 50.672 1.00 21.47 ? 246 VAL A CB 1 ATOM 1920 C CG1 . VAL A 1 246 ? 10.727 13.252 49.885 1.00 21.01 ? 246 VAL A CG1 1 ATOM 1921 C CG2 . VAL A 1 246 ? 9.707 13.502 52.195 1.00 23.93 ? 246 VAL A CG2 1 ATOM 1922 N N . PRO A 1 247 ? 9.137 15.744 47.982 1.00 21.78 ? 247 PRO A N 1 ATOM 1923 C CA . PRO A 1 247 ? 8.742 15.827 46.575 1.00 21.18 ? 247 PRO A CA 1 ATOM 1924 C C . PRO A 1 247 ? 9.108 14.577 45.796 1.00 19.01 ? 247 PRO A C 1 ATOM 1925 O O . PRO A 1 247 ? 9.772 13.666 46.305 1.00 23.02 ? 247 PRO A O 1 ATOM 1926 C CB . PRO A 1 247 ? 9.491 17.075 46.053 1.00 22.95 ? 247 PRO A CB 1 ATOM 1927 C CG . PRO A 1 247 ? 9.972 17.789 47.256 1.00 22.48 ? 247 PRO A CG 1 ATOM 1928 C CD . PRO A 1 247 ? 10.157 16.752 48.310 1.00 23.77 ? 247 PRO A CD 1 ATOM 1929 N N . CYS A 1 248 ? 8.554 14.475 44.620 1.00 19.57 ? 248 CYS A N 1 ATOM 1930 C CA . CYS A 1 248 ? 8.960 13.484 43.685 1.00 19.02 ? 248 CYS A CA 1 ATOM 1931 C C . CYS A 1 248 ? 10.396 13.808 43.234 1.00 18.56 ? 248 CYS A C 1 ATOM 1932 O O . CYS A 1 248 ? 10.889 14.948 43.314 1.00 17.26 ? 248 CYS A O 1 ATOM 1933 C CB . CYS A 1 248 ? 8.033 13.463 42.463 1.00 22.74 ? 248 CYS A CB 1 ATOM 1934 S SG . CYS A 1 248 ? 6.286 13.260 42.840 1.00 20.43 ? 248 CYS A SG 1 ATOM 1935 N N . PHE A 1 249 ? 11.025 12.785 42.712 1.00 19.56 ? 249 PHE A N 1 ATOM 1936 C CA . PHE A 1 249 ? 12.349 12.887 42.116 1.00 18.95 ? 249 PHE A CA 1 ATOM 1937 C C . PHE A 1 249 ? 12.263 13.485 40.743 1.00 22.09 ? 249 PHE A C 1 ATOM 1938 O O . PHE A 1 249 ? 11.192 13.424 40.140 1.00 20.56 ? 249 PHE A O 1 ATOM 1939 C CB . PHE A 1 249 ? 12.984 11.503 42.022 1.00 20.90 ? 249 PHE A CB 1 ATOM 1940 C CG . PHE A 1 249 ? 13.444 10.967 43.346 1.00 22.19 ? 249 PHE A CG 1 ATOM 1941 C CD1 . PHE A 1 249 ? 14.102 11.822 44.274 1.00 23.42 ? 249 PHE A CD1 1 ATOM 1942 C CD2 . PHE A 1 249 ? 13.224 9.672 43.715 1.00 22.78 ? 249 PHE A CD2 1 ATOM 1943 C CE1 . PHE A 1 249 ? 14.512 11.350 45.512 1.00 23.52 ? 249 PHE A CE1 1 ATOM 1944 C CE2 . PHE A 1 249 ? 13.674 9.189 44.968 1.00 24.30 ? 249 PHE A CE2 1 ATOM 1945 C CZ . PHE A 1 249 ? 14.306 10.037 45.859 1.00 23.92 ? 249 PHE A CZ 1 ATOM 1946 N N . GLN A 1 250 ? 13.367 14.128 40.306 1.00 22.21 ? 250 GLN A N 1 ATOM 1947 C CA . GLN A 1 250 ? 13.541 14.606 38.963 1.00 25.30 ? 250 GLN A CA 1 ATOM 1948 C C . GLN A 1 250 ? 14.472 13.692 38.224 1.00 22.14 ? 250 GLN A C 1 ATOM 1949 O O . GLN A 1 250 ? 15.590 13.538 38.596 1.00 24.44 ? 250 GLN A O 1 ATOM 1950 C CB . GLN A 1 250 ? 14.106 16.039 38.979 1.00 32.87 ? 250 GLN A CB 1 ATOM 1951 C CG . GLN A 1 250 ? 14.168 16.639 37.592 1.00 36.45 ? 250 GLN A CG 1 ATOM 1952 C CD . GLN A 1 250 ? 14.622 18.059 37.631 1.00 41.40 ? 250 GLN A CD 1 ATOM 1953 O OE1 . GLN A 1 250 ? 13.827 18.958 37.445 1.00 48.47 ? 250 GLN A OE1 1 ATOM 1954 N NE2 . GLN A 1 250 ? 15.903 18.276 37.928 1.00 46.70 ? 250 GLN A NE2 1 ATOM 1955 N N . ALA A 1 251 ? 13.989 13.029 37.183 1.00 19.84 ? 251 ALA A N 1 ATOM 1956 C CA . ALA A 1 251 ? 14.824 12.126 36.391 1.00 19.75 ? 251 ALA A CA 1 ATOM 1957 C C . ALA A 1 251 ? 14.543 12.308 34.873 1.00 20.66 ? 251 ALA A C 1 ATOM 1958 O O . ALA A 1 251 ? 13.713 13.151 34.485 1.00 19.71 ? 251 ALA A O 1 ATOM 1959 C CB . ALA A 1 251 ? 14.571 10.692 36.840 1.00 19.52 ? 251 ALA A CB 1 ATOM 1960 N N . GLY A 1 252 ? 15.187 11.508 34.030 1.00 20.35 ? 252 GLY A N 1 ATOM 1961 C CA . GLY A 1 252 ? 15.008 11.637 32.589 1.00 20.04 ? 252 GLY A CA 1 ATOM 1962 C C . GLY A 1 252 ? 13.631 11.276 32.099 1.00 20.01 ? 252 GLY A C 1 ATOM 1963 O O . GLY A 1 252 ? 13.193 11.727 31.024 1.00 21.13 ? 252 GLY A O 1 ATOM 1964 N N . ASP A 1 253 ? 12.909 10.521 32.912 1.00 20.71 ? 253 ASP A N 1 ATOM 1965 C CA . ASP A 1 253 ? 11.523 10.237 32.654 1.00 21.03 ? 253 ASP A CA 1 ATOM 1966 C C . ASP A 1 253 ? 10.600 10.715 33.777 1.00 21.34 ? 253 ASP A C 1 ATOM 1967 O O . ASP A 1 253 ? 10.872 10.479 34.948 1.00 21.26 ? 253 ASP A O 1 ATOM 1968 C CB . ASP A 1 253 ? 11.381 8.738 32.424 1.00 22.48 ? 253 ASP A CB 1 ATOM 1969 C CG . ASP A 1 253 ? 9.926 8.334 32.088 1.00 24.48 ? 253 ASP A CG 1 ATOM 1970 O OD1 . ASP A 1 253 ? 9.509 8.479 30.898 1.00 24.43 ? 253 ASP A OD1 1 ATOM 1971 O OD2 . ASP A 1 253 ? 9.226 7.912 33.033 1.00 24.31 ? 253 ASP A OD2 1 ATOM 1972 N N . SER A 1 254 ? 9.465 11.325 33.418 1.00 20.39 ? 254 SER A N 1 ATOM 1973 C CA . SER A 1 254 ? 8.591 11.931 34.415 1.00 18.96 ? 254 SER A CA 1 ATOM 1974 C C . SER A 1 254 ? 7.827 10.924 35.269 1.00 17.45 ? 254 SER A C 1 ATOM 1975 O O . SER A 1 254 ? 7.185 11.296 36.232 1.00 16.12 ? 254 SER A O 1 ATOM 1976 C CB . SER A 1 254 ? 7.562 12.825 33.719 1.00 19.72 ? 254 SER A CB 1 ATOM 1977 O OG . SER A 1 254 ? 6.702 11.994 32.882 1.00 20.14 ? 254 SER A OG 1 ATOM 1978 N N . ARG A 1 255 ? 7.861 9.651 34.940 1.00 16.75 ? 255 ARG A N 1 ATOM 1979 C CA . ARG A 1 255 ? 7.129 8.703 35.727 1.00 16.84 ? 255 ARG A CA 1 ATOM 1980 C C . ARG A 1 255 ? 7.949 8.094 36.861 1.00 16.53 ? 255 ARG A C 1 ATOM 1981 O O . ARG A 1 255 ? 7.503 7.138 37.510 1.00 15.00 ? 255 ARG A O 1 ATOM 1982 C CB . ARG A 1 255 ? 6.612 7.598 34.821 1.00 18.37 ? 255 ARG A CB 1 ATOM 1983 C CG . ARG A 1 255 ? 5.678 8.127 33.746 1.00 19.52 ? 255 ARG A CG 1 ATOM 1984 C CD . ARG A 1 255 ? 5.511 7.137 32.601 1.00 20.70 ? 255 ARG A CD 1 ATOM 1985 N NE . ARG A 1 255 ? 6.736 7.052 31.736 1.00 19.43 ? 255 ARG A NE 1 ATOM 1986 C CZ . ARG A 1 255 ? 6.843 6.254 30.673 1.00 18.02 ? 255 ARG A CZ 1 ATOM 1987 N NH1 . ARG A 1 255 ? 5.798 5.573 30.247 1.00 16.91 ? 255 ARG A NH1 1 ATOM 1988 N NH2 . ARG A 1 255 ? 7.960 6.261 29.946 1.00 17.71 ? 255 ARG A NH2 1 ATOM 1989 N N . ALA A 1 256 ? 9.142 8.612 37.099 1.00 16.66 ? 256 ALA A N 1 ATOM 1990 C CA . ALA A 1 256 ? 10.161 7.912 37.945 1.00 17.11 ? 256 ALA A CA 1 ATOM 1991 C C . ALA A 1 256 ? 9.727 7.586 39.368 1.00 17.20 ? 256 ALA A C 1 ATOM 1992 O O . ALA A 1 256 ? 10.193 6.642 39.984 1.00 16.92 ? 256 ALA A O 1 ATOM 1993 C CB . ALA A 1 256 ? 11.470 8.714 37.989 1.00 17.89 ? 256 ALA A CB 1 ATOM 1994 N N . SER A 1 257 ? 8.857 8.395 39.895 1.00 19.15 ? 257 SER A N 1 ATOM 1995 C CA . SER A 1 257 ? 8.373 8.228 41.262 1.00 17.75 ? 257 SER A CA 1 ATOM 1996 C C . SER A 1 257 ? 7.035 7.548 41.365 1.00 19.34 ? 257 SER A C 1 ATOM 1997 O O . SER A 1 257 ? 6.450 7.535 42.454 1.00 18.45 ? 257 SER A O 1 ATOM 1998 C CB . SER A 1 257 ? 8.247 9.613 41.895 1.00 18.74 ? 257 SER A CB 1 ATOM 1999 O OG . SER A 1 257 ? 9.504 10.271 41.842 1.00 19.66 ? 257 SER A OG 1 ATOM 2000 N N . GLU A 1 258 ? 6.488 7.011 40.268 1.00 17.08 ? 258 GLU A N 1 ATOM 2001 C CA . GLU A 1 258 ? 5.167 6.418 40.322 1.00 18.64 ? 258 GLU A CA 1 ATOM 2002 C C . GLU A 1 258 ? 5.008 5.335 41.341 1.00 18.02 ? 258 GLU A C 1 ATOM 2003 O O . GLU A 1 258 ? 3.902 5.128 41.850 1.00 19.28 ? 258 GLU A O 1 ATOM 2004 C CB . GLU A 1 258 ? 4.781 5.844 38.966 1.00 15.85 ? 258 GLU A CB 1 ATOM 2005 C CG . GLU A 1 258 ? 3.416 5.258 38.896 1.00 14.85 ? 258 GLU A CG 1 ATOM 2006 C CD . GLU A 1 258 ? 3.365 3.729 39.102 1.00 14.00 ? 258 GLU A CD 1 ATOM 2007 O OE1 . GLU A 1 258 ? 4.414 3.089 39.107 1.00 13.38 ? 258 GLU A OE1 1 ATOM 2008 O OE2 . GLU A 1 258 ? 2.236 3.148 39.236 1.00 13.86 ? 258 GLU A OE2 1 ATOM 2009 N N . GLN A 1 259 ? 6.078 4.601 41.567 1.00 18.19 ? 259 GLN A N 1 ATOM 2010 C CA . GLN A 1 259 ? 6.157 3.766 42.758 1.00 18.43 ? 259 GLN A CA 1 ATOM 2011 C C . GLN A 1 259 ? 7.565 3.545 43.236 1.00 19.08 ? 259 GLN A C 1 ATOM 2012 O O . GLN A 1 259 ? 8.574 3.741 42.542 1.00 16.43 ? 259 GLN A O 1 ATOM 2013 C CB . GLN A 1 259 ? 5.394 2.449 42.610 1.00 18.35 ? 259 GLN A CB 1 ATOM 2014 C CG . GLN A 1 259 ? 5.835 1.496 41.477 1.00 17.45 ? 259 GLN A CG 1 ATOM 2015 C CD . GLN A 1 259 ? 6.930 0.535 41.774 1.00 18.03 ? 259 GLN A CD 1 ATOM 2016 O OE1 . GLN A 1 259 ? 7.372 0.336 42.956 1.00 16.06 ? 259 GLN A OE1 1 ATOM 2017 N NE2 . GLN A 1 259 ? 7.426 -0.116 40.689 1.00 17.67 ? 259 GLN A NE2 1 ATOM 2018 N N . ILE A 1 260 ? 7.662 3.132 44.492 1.00 20.61 ? 260 ILE A N 1 ATOM 2019 C CA . ILE A 1 260 ? 8.927 3.300 45.229 1.00 19.92 ? 260 ILE A CA 1 ATOM 2020 C C . ILE A 1 260 ? 10.044 2.444 44.636 1.00 17.61 ? 260 ILE A C 1 ATOM 2021 O O . ILE A 1 260 ? 11.159 2.808 44.632 1.00 17.56 ? 260 ILE A O 1 ATOM 2022 C CB . ILE A 1 260 ? 8.663 2.957 46.691 1.00 21.83 ? 260 ILE A CB 1 ATOM 2023 C CG1 . ILE A 1 260 ? 9.622 3.652 47.584 1.00 24.58 ? 260 ILE A CG1 1 ATOM 2024 C CG2 . ILE A 1 260 ? 8.615 1.449 46.908 1.00 20.46 ? 260 ILE A CG2 1 ATOM 2025 C CD1 . ILE A 1 260 ? 9.411 3.336 49.058 1.00 28.39 ? 260 ILE A CD1 1 ATOM 2026 N N . LEU A 1 261 ? 9.738 1.285 44.110 1.00 19.70 ? 261 LEU A N 1 ATOM 2027 C CA . LEU A 1 261 ? 10.786 0.432 43.531 1.00 18.81 ? 261 LEU A CA 1 ATOM 2028 C C . LEU A 1 261 ? 11.225 0.852 42.167 1.00 18.21 ? 261 LEU A C 1 ATOM 2029 O O . LEU A 1 261 ? 12.386 0.557 41.760 1.00 16.67 ? 261 LEU A O 1 ATOM 2030 C CB . LEU A 1 261 ? 10.350 -1.029 43.460 1.00 18.14 ? 261 LEU A CB 1 ATOM 2031 C CG . LEU A 1 261 ? 10.113 -1.638 44.853 1.00 18.03 ? 261 LEU A CG 1 ATOM 2032 C CD1 . LEU A 1 261 ? 9.732 -3.081 44.617 1.00 16.73 ? 261 LEU A CD1 1 ATOM 2033 C CD2 . LEU A 1 261 ? 11.364 -1.581 45.754 1.00 19.99 ? 261 LEU A CD2 1 ATOM 2034 N N . LEU A 1 262 ? 10.364 1.588 41.473 1.00 17.72 ? 262 LEU A N 1 ATOM 2035 C CA . LEU A 1 262 ? 10.804 2.247 40.260 1.00 16.92 ? 262 LEU A CA 1 ATOM 2036 C C . LEU A 1 262 ? 11.797 3.337 40.597 1.00 16.69 ? 262 LEU A C 1 ATOM 2037 O O . LEU A 1 262 ? 12.838 3.447 39.934 1.00 16.45 ? 262 LEU A O 1 ATOM 2038 C CB . LEU A 1 262 ? 9.658 2.806 39.474 1.00 15.36 ? 262 LEU A CB 1 ATOM 2039 C CG . LEU A 1 262 ? 9.920 3.619 38.210 1.00 16.09 ? 262 LEU A CG 1 ATOM 2040 C CD1 . LEU A 1 262 ? 10.493 2.751 37.118 1.00 15.93 ? 262 LEU A CD1 1 ATOM 2041 C CD2 . LEU A 1 262 ? 8.585 4.167 37.756 1.00 14.67 ? 262 LEU A CD2 1 ATOM 2042 N N . ALA A 1 263 ? 11.450 4.204 41.535 1.00 16.92 ? 263 ALA A N 1 ATOM 2043 C CA . ALA A 1 263 ? 12.387 5.241 41.998 1.00 16.32 ? 263 ALA A CA 1 ATOM 2044 C C . ALA A 1 263 ? 13.681 4.637 42.506 1.00 16.20 ? 263 ALA A C 1 ATOM 2045 O O . ALA A 1 263 ? 14.720 5.207 42.311 1.00 17.53 ? 263 ALA A O 1 ATOM 2046 C CB . ALA A 1 263 ? 11.748 6.076 43.100 1.00 17.17 ? 263 ALA A CB 1 ATOM 2047 N N . THR A 1 264 ? 13.627 3.467 43.126 1.00 16.04 ? 264 THR A N 1 ATOM 2048 C CA . THR A 1 264 ? 14.821 2.780 43.610 1.00 16.05 ? 264 THR A CA 1 ATOM 2049 C C . THR A 1 264 ? 15.714 2.424 42.434 1.00 18.11 ? 264 THR A C 1 ATOM 2050 O O . THR A 1 264 ? 16.946 2.676 42.496 1.00 17.02 ? 264 THR A O 1 ATOM 2051 C CB . THR A 1 264 ? 14.401 1.547 44.389 1.00 18.40 ? 264 THR A CB 1 ATOM 2052 O OG1 . THR A 1 264 ? 13.753 1.951 45.606 1.00 19.12 ? 264 THR A OG1 1 ATOM 2053 C CG2 . THR A 1 264 ? 15.579 0.543 44.655 1.00 16.65 ? 264 THR A CG2 1 ATOM 2054 N N . VAL A 1 265 ? 15.139 1.916 41.338 1.00 18.00 ? 265 VAL A N 1 ATOM 2055 C CA . VAL A 1 265 ? 16.011 1.532 40.213 1.00 17.90 ? 265 VAL A CA 1 ATOM 2056 C C . VAL A 1 265 ? 16.556 2.767 39.486 1.00 18.78 ? 265 VAL A C 1 ATOM 2057 O O . VAL A 1 265 ? 17.735 2.803 39.142 1.00 20.13 ? 265 VAL A O 1 ATOM 2058 C CB . VAL A 1 265 ? 15.413 0.437 39.292 1.00 18.31 ? 265 VAL A CB 1 ATOM 2059 C CG1 . VAL A 1 265 ? 16.401 0.112 38.117 1.00 18.32 ? 265 VAL A CG1 1 ATOM 2060 C CG2 . VAL A 1 265 ? 15.199 -0.819 40.119 1.00 18.34 ? 265 VAL A CG2 1 ATOM 2061 N N . HIS A 1 266 ? 15.754 3.794 39.317 1.00 17.45 ? 266 HIS A N 1 ATOM 2062 C CA . HIS A 1 266 ? 16.224 5.081 38.803 1.00 17.86 ? 266 HIS A CA 1 ATOM 2063 C C . HIS A 1 266 ? 17.420 5.615 39.586 1.00 20.79 ? 266 HIS A C 1 ATOM 2064 O O . HIS A 1 266 ? 18.359 6.176 39.009 1.00 20.97 ? 266 HIS A O 1 ATOM 2065 C CB . HIS A 1 266 ? 15.149 6.157 38.801 1.00 17.10 ? 266 HIS A CB 1 ATOM 2066 C CG . HIS A 1 266 ? 14.330 6.233 37.538 1.00 18.09 ? 266 HIS A CG 1 ATOM 2067 N ND1 . HIS A 1 266 ? 14.747 6.894 36.398 1.00 17.09 ? 266 HIS A ND1 1 ATOM 2068 C CD2 . HIS A 1 266 ? 13.094 5.746 37.260 1.00 18.12 ? 266 HIS A CD2 1 ATOM 2069 C CE1 . HIS A 1 266 ? 13.786 6.818 35.483 1.00 18.69 ? 266 HIS A CE1 1 ATOM 2070 N NE2 . HIS A 1 266 ? 12.770 6.134 35.987 1.00 17.61 ? 266 HIS A NE2 1 ATOM 2071 N N . THR A 1 267 ? 17.315 5.504 40.916 1.00 18.77 ? 267 THR A N 1 ATOM 2072 C CA . THR A 1 267 ? 18.398 5.904 41.811 1.00 18.54 ? 267 THR A CA 1 ATOM 2073 C C . THR A 1 267 ? 19.698 5.094 41.561 1.00 18.80 ? 267 THR A C 1 ATOM 2074 O O . THR A 1 267 ? 20.782 5.682 41.441 1.00 17.83 ? 267 THR A O 1 ATOM 2075 C CB . THR A 1 267 ? 17.931 5.822 43.263 1.00 16.70 ? 267 THR A CB 1 ATOM 2076 O OG1 . THR A 1 267 ? 16.921 6.825 43.491 1.00 16.02 ? 267 THR A OG1 1 ATOM 2077 C CG2 . THR A 1 267 ? 19.101 6.118 44.227 1.00 16.31 ? 267 THR A CG2 1 ATOM 2078 N N . LEU A 1 268 ? 19.574 3.764 41.402 1.00 18.39 ? 268 LEU A N 1 ATOM 2079 C CA . LEU A 1 268 ? 20.724 2.958 41.079 1.00 19.21 ? 268 LEU A CA 1 ATOM 2080 C C . LEU A 1 268 ? 21.409 3.363 39.776 1.00 21.44 ? 268 LEU A C 1 ATOM 2081 O O . LEU A 1 268 ? 22.672 3.407 39.668 1.00 18.21 ? 268 LEU A O 1 ATOM 2082 C CB . LEU A 1 268 ? 20.344 1.493 40.997 1.00 19.76 ? 268 LEU A CB 1 ATOM 2083 C CG . LEU A 1 268 ? 19.805 0.840 42.270 1.00 18.54 ? 268 LEU A CG 1 ATOM 2084 C CD1 . LEU A 1 268 ? 19.288 -0.539 41.994 1.00 19.70 ? 268 LEU A CD1 1 ATOM 2085 C CD2 . LEU A 1 268 ? 20.897 0.785 43.325 1.00 19.78 ? 268 LEU A CD2 1 ATOM 2086 N N . LEU A 1 269 ? 20.580 3.633 38.762 1.00 21.07 ? 269 LEU A N 1 ATOM 2087 C CA . LEU A 1 269 ? 21.081 3.976 37.449 1.00 20.04 ? 269 LEU A CA 1 ATOM 2088 C C . LEU A 1 269 ? 21.798 5.322 37.481 1.00 21.34 ? 269 LEU A C 1 ATOM 2089 O O . LEU A 1 269 ? 22.880 5.475 36.902 1.00 16.63 ? 269 LEU A O 1 ATOM 2090 C CB . LEU A 1 269 ? 19.924 4.001 36.425 1.00 19.81 ? 269 LEU A CB 1 ATOM 2091 C CG . LEU A 1 269 ? 19.340 2.635 36.141 1.00 19.10 ? 269 LEU A CG 1 ATOM 2092 C CD1 . LEU A 1 269 ? 18.062 2.804 35.319 1.00 20.95 ? 269 LEU A CD1 1 ATOM 2093 C CD2 . LEU A 1 269 ? 20.333 1.794 35.385 1.00 21.32 ? 269 LEU A CD2 1 ATOM 2094 N N . LEU A 1 270 ? 21.196 6.304 38.159 1.00 20.86 ? 270 LEU A N 1 ATOM 2095 C CA . LEU A 1 270 ? 21.859 7.594 38.353 1.00 18.96 ? 270 LEU A CA 1 ATOM 2096 C C . LEU A 1 270 ? 23.223 7.503 39.103 1.00 21.59 ? 270 LEU A C 1 ATOM 2097 O O . LEU A 1 270 ? 24.241 8.115 38.703 1.00 18.00 ? 270 LEU A O 1 ATOM 2098 C CB . LEU A 1 270 ? 20.936 8.487 39.135 1.00 21.76 ? 270 LEU A CB 1 ATOM 2099 C CG . LEU A 1 270 ? 21.379 9.935 39.258 1.00 22.69 ? 270 LEU A CG 1 ATOM 2100 C CD1 . LEU A 1 270 ? 21.227 10.648 37.942 1.00 24.22 ? 270 LEU A CD1 1 ATOM 2101 C CD2 . LEU A 1 270 ? 20.592 10.622 40.361 1.00 24.20 ? 270 LEU A CD2 1 ATOM 2102 N N . ARG A 1 271 ? 23.235 6.728 40.172 1.00 19.68 ? 271 ARG A N 1 ATOM 2103 C CA . ARG A 1 271 ? 24.448 6.518 40.935 1.00 21.96 ? 271 ARG A CA 1 ATOM 2104 C C . ARG A 1 271 ? 25.496 5.925 39.992 1.00 21.71 ? 271 ARG A C 1 ATOM 2105 O O . ARG A 1 271 ? 26.624 6.372 40.015 1.00 19.65 ? 271 ARG A O 1 ATOM 2106 C CB . ARG A 1 271 ? 24.233 5.601 42.138 1.00 20.67 ? 271 ARG A CB 1 ATOM 2107 C CG . ARG A 1 271 ? 23.516 6.278 43.282 1.00 20.90 ? 271 ARG A CG 1 ATOM 2108 C CD . ARG A 1 271 ? 23.250 5.330 44.400 1.00 20.94 ? 271 ARG A CD 1 ATOM 2109 N NE . ARG A 1 271 ? 22.373 5.972 45.398 1.00 21.13 ? 271 ARG A NE 1 ATOM 2110 C CZ . ARG A 1 271 ? 21.885 5.383 46.486 1.00 21.07 ? 271 ARG A CZ 1 ATOM 2111 N NH1 . ARG A 1 271 ? 22.158 4.134 46.745 1.00 20.98 ? 271 ARG A NH1 1 ATOM 2112 N NH2 . ARG A 1 271 ? 21.086 6.075 47.316 1.00 19.14 ? 271 ARG A NH2 1 ATOM 2113 N N . GLU A 1 272 ? 25.102 4.955 39.173 1.00 22.31 ? 272 GLU A N 1 ATOM 2114 C CA . GLU A 1 272 ? 26.026 4.304 38.268 1.00 22.21 ? 272 GLU A CA 1 ATOM 2115 C C . GLU A 1 272 ? 26.595 5.259 37.278 1.00 24.74 ? 272 GLU A C 1 ATOM 2116 O O . GLU A 1 272 ? 27.783 5.191 37.011 1.00 24.34 ? 272 GLU A O 1 ATOM 2117 C CB . GLU A 1 272 ? 25.377 3.147 37.546 1.00 25.43 ? 272 GLU A CB 1 ATOM 2118 C CG . GLU A 1 272 ? 26.261 2.497 36.458 1.00 26.01 ? 272 GLU A CG 1 ATOM 2119 C CD . GLU A 1 272 ? 27.474 1.750 36.998 1.00 29.49 ? 272 GLU A CD 1 ATOM 2120 O OE1 . GLU A 1 272 ? 27.570 1.502 38.224 1.00 28.21 ? 272 GLU A OE1 1 ATOM 2121 O OE2 . GLU A 1 272 ? 28.370 1.367 36.168 1.00 29.34 ? 272 GLU A OE2 1 ATOM 2122 N N . HIS A 1 273 ? 25.799 6.181 36.727 1.00 24.87 ? 273 HIS A N 1 ATOM 2123 C CA . HIS A 1 273 ? 26.382 7.189 35.841 1.00 25.92 ? 273 HIS A CA 1 ATOM 2124 C C . HIS A 1 273 ? 27.516 7.958 36.483 1.00 29.05 ? 273 HIS A C 1 ATOM 2125 O O . HIS A 1 273 ? 28.590 8.159 35.862 1.00 29.67 ? 273 HIS A O 1 ATOM 2126 C CB . HIS A 1 273 ? 25.388 8.217 35.361 1.00 26.58 ? 273 HIS A CB 1 ATOM 2127 C CG . HIS A 1 273 ? 26.024 9.342 34.600 1.00 28.06 ? 273 HIS A CG 1 ATOM 2128 N ND1 . HIS A 1 273 ? 26.058 9.383 33.226 1.00 29.69 ? 273 HIS A ND1 1 ATOM 2129 C CD2 . HIS A 1 273 ? 26.686 10.445 35.022 1.00 29.70 ? 273 HIS A CD2 1 ATOM 2130 C CE1 . HIS A 1 273 ? 26.657 10.492 32.836 1.00 31.78 ? 273 HIS A CE1 1 ATOM 2131 N NE2 . HIS A 1 273 ? 27.075 11.140 33.906 1.00 30.99 ? 273 HIS A NE2 1 ATOM 2132 N N . ASN A 1 274 ? 27.278 8.473 37.691 1.00 27.22 ? 274 ASN A N 1 ATOM 2133 C CA . ASN A 1 274 ? 28.323 9.220 38.390 1.00 26.32 ? 274 ASN A CA 1 ATOM 2134 C C . ASN A 1 274 ? 29.524 8.347 38.752 1.00 25.78 ? 274 ASN A C 1 ATOM 2135 O O . ASN A 1 274 ? 30.642 8.804 38.652 1.00 28.93 ? 274 ASN A O 1 ATOM 2136 C CB . ASN A 1 274 ? 27.750 9.947 39.592 1.00 25.58 ? 274 ASN A CB 1 ATOM 2137 C CG . ASN A 1 274 ? 26.903 11.102 39.167 1.00 26.44 ? 274 ASN A CG 1 ATOM 2138 O OD1 . ASN A 1 274 ? 26.894 11.418 37.989 1.00 26.14 ? 274 ASN A OD1 1 ATOM 2139 N ND2 . ASN A 1 274 ? 26.189 11.759 40.103 1.00 24.96 ? 274 ASN A ND2 1 ATOM 2140 N N . ARG A 1 275 ? 29.302 7.077 39.074 1.00 25.75 ? 275 ARG A N 1 ATOM 2141 C CA . ARG A 1 275 ? 30.393 6.173 39.348 1.00 28.21 ? 275 ARG A CA 1 ATOM 2142 C C . ARG A 1 275 ? 31.292 6.095 38.126 1.00 26.93 ? 275 ARG A C 1 ATOM 2143 O O . ARG A 1 275 ? 32.502 6.208 38.232 1.00 27.50 ? 275 ARG A O 1 ATOM 2144 C CB . ARG A 1 275 ? 29.887 4.783 39.702 1.00 30.81 ? 275 ARG A CB 1 ATOM 2145 C CG . ARG A 1 275 ? 30.905 3.911 40.392 1.00 29.45 ? 275 ARG A CG 1 ATOM 2146 C CD . ARG A 1 275 ? 30.368 2.510 40.574 1.00 29.46 ? 275 ARG A CD 1 ATOM 2147 N NE . ARG A 1 275 ? 30.096 1.873 39.272 1.00 30.35 ? 275 ARG A NE 1 ATOM 2148 C CZ . ARG A 1 275 ? 31.034 1.374 38.480 1.00 28.53 ? 275 ARG A CZ 1 ATOM 2149 N NH1 . ARG A 1 275 ? 32.274 1.361 38.883 1.00 27.66 ? 275 ARG A NH1 1 ATOM 2150 N NH2 . ARG A 1 275 ? 30.734 0.868 37.302 1.00 25.61 ? 275 ARG A NH2 1 ATOM 2151 N N . LEU A 1 276 ? 30.676 5.862 36.984 1.00 26.11 ? 276 LEU A N 1 ATOM 2152 C CA . LEU A 1 276 ? 31.364 5.765 35.704 1.00 25.11 ? 276 LEU A CA 1 ATOM 2153 C C . LEU A 1 276 ? 32.112 7.023 35.351 1.00 28.94 ? 276 LEU A C 1 ATOM 2154 O O . LEU A 1 276 ? 33.244 6.961 34.868 1.00 28.53 ? 276 LEU A O 1 ATOM 2155 C CB . LEU A 1 276 ? 30.370 5.419 34.590 1.00 21.96 ? 276 LEU A CB 1 ATOM 2156 C CG . LEU A 1 276 ? 29.772 4.034 34.605 1.00 21.02 ? 276 LEU A CG 1 ATOM 2157 C CD1 . LEU A 1 276 ? 28.608 3.961 33.613 1.00 21.76 ? 276 LEU A CD1 1 ATOM 2158 C CD2 . LEU A 1 276 ? 30.766 2.913 34.310 1.00 23.60 ? 276 LEU A CD2 1 ATOM 2159 N N . ALA A 1 277 ? 31.512 8.180 35.593 1.00 30.14 ? 277 ALA A N 1 ATOM 2160 C CA . ALA A 1 277 ? 32.134 9.448 35.219 1.00 32.26 ? 277 ALA A CA 1 ATOM 2161 C C . ALA A 1 277 ? 33.341 9.734 36.099 1.00 39.08 ? 277 ALA A C 1 ATOM 2162 O O . ALA A 1 277 ? 34.282 10.415 35.670 1.00 36.00 ? 277 ALA A O 1 ATOM 2163 C CB . ALA A 1 277 ? 31.146 10.591 35.289 1.00 31.47 ? 277 ALA A CB 1 ATOM 2164 N N . ARG A 1 278 ? 33.327 9.203 37.319 1.00 36.03 ? 278 ARG A N 1 ATOM 2165 C CA . ARG A 1 278 ? 34.411 9.466 38.231 1.00 35.58 ? 278 ARG A CA 1 ATOM 2166 C C . ARG A 1 278 ? 35.549 8.554 37.901 1.00 35.06 ? 278 ARG A C 1 ATOM 2167 O O . ARG A 1 278 ? 36.693 8.957 37.981 1.00 33.93 ? 278 ARG A O 1 ATOM 2168 C CB . ARG A 1 278 ? 34.001 9.243 39.672 1.00 36.53 ? 278 ARG A CB 1 ATOM 2169 C CG . ARG A 1 278 ? 33.138 10.367 40.168 1.00 36.85 ? 278 ARG A CG 1 ATOM 2170 C CD . ARG A 1 278 ? 32.805 10.190 41.628 1.00 39.14 ? 278 ARG A CD 1 ATOM 2171 N NE . ARG A 1 278 ? 31.735 11.134 41.930 1.00 44.26 ? 278 ARG A NE 1 ATOM 2172 C CZ . ARG A 1 278 ? 30.486 10.786 42.215 1.00 45.04 ? 278 ARG A CZ 1 ATOM 2173 N NH1 . ARG A 1 278 ? 30.127 9.496 42.325 1.00 42.19 ? 278 ARG A NH1 1 ATOM 2174 N NH2 . ARG A 1 278 ? 29.598 11.740 42.409 1.00 48.50 ? 278 ARG A NH2 1 ATOM 2175 N N . GLU A 1 279 ? 35.223 7.318 37.546 1.00 34.33 ? 279 GLU A N 1 ATOM 2176 C CA . GLU A 1 279 ? 36.229 6.368 37.165 1.00 34.19 ? 279 GLU A CA 1 ATOM 2177 C C . GLU A 1 279 ? 36.888 6.705 35.840 1.00 36.49 ? 279 GLU A C 1 ATOM 2178 O O . GLU A 1 279 ? 38.086 6.449 35.668 1.00 38.41 ? 279 GLU A O 1 ATOM 2179 C CB . GLU A 1 279 ? 35.675 4.961 37.190 1.00 39.01 ? 279 GLU A CB 1 ATOM 2180 C CG . GLU A 1 279 ? 36.616 3.941 37.791 1.00 50.57 ? 279 GLU A CG 1 ATOM 2181 C CD . GLU A 1 279 ? 37.149 4.338 39.166 1.00 52.34 ? 279 GLU A CD 1 ATOM 2182 O OE1 . GLU A 1 279 ? 37.702 5.450 39.315 1.00 51.11 ? 279 GLU A OE1 1 ATOM 2183 O OE2 . GLU A 1 279 ? 37.029 3.524 40.112 1.00 60.65 ? 279 GLU A OE2 1 ATOM 2184 N N . LEU A 1 280 ? 36.145 7.302 34.914 1.00 35.56 ? 280 LEU A N 1 ATOM 2185 C CA . LEU A 1 280 ? 36.710 7.767 33.643 1.00 38.49 ? 280 LEU A CA 1 ATOM 2186 C C . LEU A 1 280 ? 37.534 9.055 33.807 1.00 41.18 ? 280 LEU A C 1 ATOM 2187 O O . LEU A 1 280 ? 38.474 9.288 33.063 1.00 36.88 ? 280 LEU A O 1 ATOM 2188 C CB . LEU A 1 280 ? 35.607 8.007 32.583 1.00 37.96 ? 280 LEU A CB 1 ATOM 2189 C CG . LEU A 1 280 ? 34.713 6.799 32.197 1.00 38.98 ? 280 LEU A CG 1 ATOM 2190 C CD1 . LEU A 1 280 ? 33.454 7.224 31.420 1.00 37.17 ? 280 LEU A CD1 1 ATOM 2191 C CD2 . LEU A 1 280 ? 35.499 5.736 31.443 1.00 42.35 ? 280 LEU A CD2 1 ATOM 2192 N N . LYS A 1 281 ? 37.139 9.932 34.719 1.00 41.75 ? 281 LYS A N 1 ATOM 2193 C CA . LYS A 1 281 ? 37.884 11.153 34.941 1.00 41.39 ? 281 LYS A CA 1 ATOM 2194 C C . LYS A 1 281 ? 39.231 10.813 35.602 1.00 47.29 ? 281 LYS A C 1 ATOM 2195 O O . LYS A 1 281 ? 40.244 11.482 35.404 1.00 48.91 ? 281 LYS A O 1 ATOM 2196 C CB . LYS A 1 281 ? 37.060 12.111 35.768 1.00 43.98 ? 281 LYS A CB 1 ATOM 2197 C CG . LYS A 1 281 ? 37.817 13.269 36.344 1.00 42.49 ? 281 LYS A CG 1 ATOM 2198 C CD . LYS A 1 281 ? 38.495 14.083 35.273 1.00 42.53 ? 281 LYS A CD 1 ATOM 2199 C CE . LYS A 1 281 ? 39.420 15.086 35.934 1.00 42.88 ? 281 LYS A CE 1 ATOM 2200 N NZ . LYS A 1 281 ? 39.454 16.346 35.151 1.00 43.31 ? 281 LYS A NZ 1 ATOM 2201 N N . ARG A 1 282 ? 39.253 9.739 36.360 1.00 47.78 ? 282 ARG A N 1 ATOM 2202 C CA . ARG A 1 282 ? 40.490 9.261 36.902 1.00 46.52 ? 282 ARG A CA 1 ATOM 2203 C C . ARG A 1 282 ? 41.368 8.720 35.787 1.00 47.51 ? 282 ARG A C 1 ATOM 2204 O O . ARG A 1 282 ? 42.554 9.059 35.713 1.00 45.71 ? 282 ARG A O 1 ATOM 2205 C CB . ARG A 1 282 ? 40.217 8.196 37.949 1.00 45.18 ? 282 ARG A CB 1 ATOM 2206 C CG . ARG A 1 282 ? 41.406 7.344 38.309 1.00 49.76 ? 282 ARG A CG 1 ATOM 2207 C CD . ARG A 1 282 ? 40.951 6.036 38.897 1.00 51.42 ? 282 ARG A CD 1 ATOM 2208 N NE . ARG A 1 282 ? 41.833 4.937 38.533 1.00 58.21 ? 282 ARG A NE 1 ATOM 2209 C CZ . ARG A 1 282 ? 41.428 3.748 38.088 1.00 62.33 ? 282 ARG A CZ 1 ATOM 2210 N NH1 . ARG A 1 282 ? 40.130 3.475 37.939 1.00 66.09 ? 282 ARG A NH1 1 ATOM 2211 N NH2 . ARG A 1 282 ? 42.325 2.812 37.796 1.00 63.27 ? 282 ARG A NH2 1 ATOM 2212 N N . LEU A 1 283 ? 40.816 7.852 34.945 1.00 45.85 ? 283 LEU A N 1 ATOM 2213 C CA . LEU A 1 283 ? 41.596 7.229 33.878 1.00 46.18 ? 283 LEU A CA 1 ATOM 2214 C C . LEU A 1 283 ? 41.992 8.230 32.785 1.00 46.43 ? 283 LEU A C 1 ATOM 2215 O O . LEU A 1 283 ? 42.981 8.028 32.078 1.00 46.20 ? 283 LEU A O 1 ATOM 2216 C CB . LEU A 1 283 ? 40.801 6.122 33.197 1.00 47.15 ? 283 LEU A CB 1 ATOM 2217 C CG . LEU A 1 283 ? 40.318 4.904 33.944 1.00 43.40 ? 283 LEU A CG 1 ATOM 2218 C CD1 . LEU A 1 283 ? 39.531 4.058 32.967 1.00 43.72 ? 283 LEU A CD1 1 ATOM 2219 C CD2 . LEU A 1 283 ? 41.457 4.114 34.547 1.00 47.11 ? 283 LEU A CD2 1 ATOM 2220 N N . ASN A 1 284 ? 41.186 9.266 32.593 1.00 42.13 ? 284 ASN A N 1 ATOM 2221 C CA . ASN A 1 284 ? 41.422 10.210 31.540 1.00 38.80 ? 284 ASN A CA 1 ATOM 2222 C C . ASN A 1 284 ? 41.268 11.588 32.096 1.00 38.05 ? 284 ASN A C 1 ATOM 2223 O O . ASN A 1 284 ? 40.419 12.342 31.634 1.00 38.97 ? 284 ASN A O 1 ATOM 2224 C CB . ASN A 1 284 ? 40.488 9.983 30.344 1.00 41.01 ? 284 ASN A CB 1 ATOM 2225 C CG . ASN A 1 284 ? 40.559 8.566 29.817 1.00 49.01 ? 284 ASN A CG 1 ATOM 2226 O OD1 . ASN A 1 284 ? 41.634 8.067 29.504 1.00 53.21 ? 284 ASN A OD1 1 ATOM 2227 N ND2 . ASN A 1 284 ? 39.413 7.896 29.722 1.00 48.28 ? 284 ASN A ND2 1 ATOM 2228 N N . PRO A 1 285 ? 42.185 11.986 33.015 1.00 41.94 ? 285 PRO A N 1 ATOM 2229 C CA . PRO A 1 285 ? 42.179 13.345 33.613 1.00 40.38 ? 285 PRO A CA 1 ATOM 2230 C C . PRO A 1 285 ? 42.036 14.486 32.633 1.00 39.90 ? 285 PRO A C 1 ATOM 2231 O O . PRO A 1 285 ? 41.503 15.541 32.992 1.00 42.85 ? 285 PRO A O 1 ATOM 2232 C CB . PRO A 1 285 ? 43.533 13.412 34.346 1.00 42.83 ? 285 PRO A CB 1 ATOM 2233 C CG . PRO A 1 285 ? 43.878 12.005 34.631 1.00 42.74 ? 285 PRO A CG 1 ATOM 2234 C CD . PRO A 1 285 ? 43.373 11.226 33.441 1.00 43.45 ? 285 PRO A CD 1 ATOM 2235 N N . HIS A 1 286 ? 42.472 14.271 31.397 1.00 36.98 ? 286 HIS A N 1 ATOM 2236 C CA . HIS A 1 286 ? 42.402 15.274 30.335 1.00 41.60 ? 286 HIS A CA 1 ATOM 2237 C C . HIS A 1 286 ? 41.023 15.475 29.713 1.00 41.46 ? 286 HIS A C 1 ATOM 2238 O O . HIS A 1 286 ? 40.727 16.579 29.242 1.00 42.85 ? 286 HIS A O 1 ATOM 2239 C CB . HIS A 1 286 ? 43.390 14.938 29.206 1.00 40.24 ? 286 HIS A CB 1 ATOM 2240 C CG . HIS A 1 286 ? 43.273 13.545 28.667 1.00 39.88 ? 286 HIS A CG 1 ATOM 2241 N ND1 . HIS A 1 286 ? 42.763 13.268 27.410 1.00 37.21 ? 286 HIS A ND1 1 ATOM 2242 C CD2 . HIS A 1 286 ? 43.664 12.352 29.185 1.00 42.67 ? 286 HIS A CD2 1 ATOM 2243 C CE1 . HIS A 1 286 ? 42.814 11.964 27.191 1.00 39.82 ? 286 HIS A CE1 1 ATOM 2244 N NE2 . HIS A 1 286 ? 43.377 11.387 28.243 1.00 43.79 ? 286 HIS A NE2 1 ATOM 2245 N N . TRP A 1 287 ? 40.184 14.434 29.730 1.00 42.63 ? 287 TRP A N 1 ATOM 2246 C CA . TRP A 1 287 ? 38.809 14.541 29.194 1.00 40.37 ? 287 TRP A CA 1 ATOM 2247 C C . TRP A 1 287 ? 38.076 15.616 29.895 1.00 37.67 ? 287 TRP A C 1 ATOM 2248 O O . TRP A 1 287 ? 38.157 15.715 31.112 1.00 33.96 ? 287 TRP A O 1 ATOM 2249 C CB . TRP A 1 287 ? 38.024 13.261 29.380 1.00 38.73 ? 287 TRP A CB 1 ATOM 2250 C CG . TRP A 1 287 ? 38.396 12.226 28.441 1.00 39.02 ? 287 TRP A CG 1 ATOM 2251 C CD1 . TRP A 1 287 ? 39.377 12.300 27.492 1.00 37.97 ? 287 TRP A CD1 1 ATOM 2252 C CD2 . TRP A 1 287 ? 37.831 10.916 28.344 1.00 38.60 ? 287 TRP A CD2 1 ATOM 2253 N NE1 . TRP A 1 287 ? 39.428 11.118 26.793 1.00 41.36 ? 287 TRP A NE1 1 ATOM 2254 C CE2 . TRP A 1 287 ? 38.507 10.245 27.308 1.00 39.49 ? 287 TRP A CE2 1 ATOM 2255 C CE3 . TRP A 1 287 ? 36.817 10.243 29.031 1.00 39.65 ? 287 TRP A CE3 1 ATOM 2256 C CZ2 . TRP A 1 287 ? 38.176 8.938 26.908 1.00 42.88 ? 287 TRP A CZ2 1 ATOM 2257 C CZ3 . TRP A 1 287 ? 36.492 8.945 28.650 1.00 38.07 ? 287 TRP A CZ3 1 ATOM 2258 C CH2 . TRP A 1 287 ? 37.164 8.304 27.597 1.00 43.25 ? 287 TRP A CH2 1 ATOM 2259 N N . ASP A 1 288 ? 37.360 16.418 29.113 1.00 36.44 ? 288 ASP A N 1 ATOM 2260 C CA . ASP A 1 288 ? 36.546 17.477 29.655 1.00 38.23 ? 288 ASP A CA 1 ATOM 2261 C C . ASP A 1 288 ? 35.125 16.969 30.084 1.00 39.17 ? 288 ASP A C 1 ATOM 2262 O O . ASP A 1 288 ? 34.806 15.779 29.954 1.00 34.51 ? 288 ASP A O 1 ATOM 2263 C CB . ASP A 1 288 ? 36.451 18.626 28.633 1.00 42.28 ? 288 ASP A CB 1 ATOM 2264 C CG . ASP A 1 288 ? 35.735 18.233 27.357 1.00 44.32 ? 288 ASP A CG 1 ATOM 2265 O OD1 . ASP A 1 288 ? 35.468 17.022 27.123 1.00 49.21 ? 288 ASP A OD1 1 ATOM 2266 O OD2 . ASP A 1 288 ? 35.412 19.154 26.585 1.00 50.56 ? 288 ASP A OD2 1 ATOM 2267 N N . GLY A 1 289 ? 34.310 17.899 30.584 1.00 35.79 ? 289 GLY A N 1 ATOM 2268 C CA . GLY A 1 289 ? 32.980 17.603 31.150 1.00 40.37 ? 289 GLY A CA 1 ATOM 2269 C C . GLY A 1 289 ? 32.045 16.872 30.193 1.00 36.39 ? 289 GLY A C 1 ATOM 2270 O O . GLY A 1 289 ? 31.446 15.874 30.575 1.00 35.75 ? 289 GLY A O 1 ATOM 2271 N N . GLU A 1 290 ? 31.989 17.352 28.952 1.00 30.14 ? 290 GLU A N 1 ATOM 2272 C CA . GLU A 1 290 ? 31.145 16.756 27.913 1.00 32.59 ? 290 GLU A CA 1 ATOM 2273 C C . GLU A 1 290 ? 31.475 15.319 27.606 1.00 31.06 ? 290 GLU A C 1 ATOM 2274 O O . GLU A 1 290 ? 30.592 14.457 27.350 1.00 30.57 ? 290 GLU A O 1 ATOM 2275 C CB . GLU A 1 290 ? 31.282 17.560 26.607 1.00 34.64 ? 290 GLU A CB 1 ATOM 2276 C CG . GLU A 1 290 ? 30.324 17.071 25.511 1.00 36.41 ? 290 GLU A CG 1 ATOM 2277 C CD . GLU A 1 290 ? 28.847 17.359 25.821 1.00 36.81 ? 290 GLU A CD 1 ATOM 2278 O OE1 . GLU A 1 290 ? 28.538 18.194 26.706 1.00 37.33 ? 290 GLU A OE1 1 ATOM 2279 O OE2 . GLU A 1 290 ? 27.989 16.774 25.151 1.00 37.00 ? 290 GLU A OE2 1 ATOM 2280 N N . MET A 1 291 ? 32.775 15.061 27.545 1.00 32.31 ? 291 MET A N 1 ATOM 2281 C CA . MET A 1 291 ? 33.225 13.807 27.080 1.00 31.60 ? 291 MET A CA 1 ATOM 2282 C C . MET A 1 291 ? 32.971 12.767 28.155 1.00 28.59 ? 291 MET A C 1 ATOM 2283 O O . MET A 1 291 ? 32.640 11.633 27.864 1.00 30.03 ? 291 MET A O 1 ATOM 2284 C CB . MET A 1 291 ? 34.714 13.855 26.755 1.00 35.22 ? 291 MET A CB 1 ATOM 2285 C CG . MET A 1 291 ? 35.181 12.515 26.235 1.00 42.25 ? 291 MET A CG 1 ATOM 2286 S SD . MET A 1 291 ? 36.535 12.657 25.051 1.00 53.77 ? 291 MET A SD 1 ATOM 2287 C CE . MET A 1 291 ? 36.745 10.918 24.693 1.00 52.81 ? 291 MET A CE 1 ATOM 2288 N N . LEU A 1 292 ? 33.204 13.166 29.388 1.00 28.21 ? 292 LEU A N 1 ATOM 2289 C CA . LEU A 1 292 ? 32.932 12.333 30.556 1.00 31.97 ? 292 LEU A CA 1 ATOM 2290 C C . LEU A 1 292 ? 31.433 11.958 30.605 1.00 26.88 ? 292 LEU A C 1 ATOM 2291 O O . LEU A 1 292 ? 31.102 10.789 30.709 1.00 24.19 ? 292 LEU A O 1 ATOM 2292 C CB . LEU A 1 292 ? 33.381 13.052 31.847 1.00 31.47 ? 292 LEU A CB 1 ATOM 2293 C CG . LEU A 1 292 ? 34.924 13.045 32.021 1.00 35.37 ? 292 LEU A CG 1 ATOM 2294 C CD1 . LEU A 1 292 ? 35.355 14.124 33.010 1.00 34.18 ? 292 LEU A CD1 1 ATOM 2295 C CD2 . LEU A 1 292 ? 35.455 11.685 32.434 1.00 32.91 ? 292 LEU A CD2 1 ATOM 2296 N N . TYR A 1 293 ? 30.578 12.964 30.471 1.00 26.47 ? 293 TYR A N 1 ATOM 2297 C CA . TYR A 1 293 ? 29.117 12.745 30.479 1.00 28.33 ? 293 TYR A CA 1 ATOM 2298 C C . TYR A 1 293 ? 28.741 11.762 29.386 1.00 30.43 ? 293 TYR A C 1 ATOM 2299 O O . TYR A 1 293 ? 28.212 10.676 29.661 1.00 31.86 ? 293 TYR A O 1 ATOM 2300 C CB . TYR A 1 293 ? 28.405 14.057 30.253 1.00 27.72 ? 293 TYR A CB 1 ATOM 2301 C CG . TYR A 1 293 ? 26.929 13.931 29.914 1.00 30.95 ? 293 TYR A CG 1 ATOM 2302 C CD1 . TYR A 1 293 ? 25.967 13.760 30.905 1.00 30.58 ? 293 TYR A CD1 1 ATOM 2303 C CD2 . TYR A 1 293 ? 26.487 14.005 28.580 1.00 28.86 ? 293 TYR A CD2 1 ATOM 2304 C CE1 . TYR A 1 293 ? 24.609 13.663 30.584 1.00 30.38 ? 293 TYR A CE1 1 ATOM 2305 C CE2 . TYR A 1 293 ? 25.160 13.893 28.244 1.00 28.59 ? 293 TYR A CE2 1 ATOM 2306 C CZ . TYR A 1 293 ? 24.214 13.710 29.250 1.00 29.48 ? 293 TYR A CZ 1 ATOM 2307 O OH . TYR A 1 293 ? 22.902 13.633 28.917 1.00 24.56 ? 293 TYR A OH 1 ATOM 2308 N N . GLN A 1 294 ? 29.099 12.111 28.144 1.00 29.55 ? 294 GLN A N 1 ATOM 2309 C CA . GLN A 1 294 ? 28.733 11.294 26.992 1.00 27.52 ? 294 GLN A CA 1 ATOM 2310 C C . GLN A 1 294 ? 29.237 9.874 27.130 1.00 27.61 ? 294 GLN A C 1 ATOM 2311 O O . GLN A 1 294 ? 28.541 8.910 26.757 1.00 29.37 ? 294 GLN A O 1 ATOM 2312 C CB . GLN A 1 294 ? 29.224 11.923 25.676 1.00 26.53 ? 294 GLN A CB 1 ATOM 2313 C CG . GLN A 1 294 ? 28.561 13.278 25.335 1.00 27.69 ? 294 GLN A CG 1 ATOM 2314 C CD . GLN A 1 294 ? 27.062 13.208 25.104 1.00 27.40 ? 294 GLN A CD 1 ATOM 2315 O OE1 . GLN A 1 294 ? 26.471 12.134 24.900 1.00 29.07 ? 294 GLN A OE1 1 ATOM 2316 N NE2 . GLN A 1 294 ? 26.449 14.353 25.088 1.00 27.35 ? 294 GLN A NE2 1 ATOM 2317 N N . GLU A 1 295 ? 30.489 9.716 27.527 1.00 28.34 ? 295 GLU A N 1 ATOM 2318 C CA . GLU A 1 295 ? 31.082 8.392 27.629 1.00 28.77 ? 295 GLU A CA 1 ATOM 2319 C C . GLU A 1 295 ? 30.422 7.562 28.726 1.00 27.39 ? 295 GLU A C 1 ATOM 2320 O O . GLU A 1 295 ? 30.142 6.434 28.526 1.00 33.93 ? 295 GLU A O 1 ATOM 2321 C CB . GLU A 1 295 ? 32.632 8.382 27.764 1.00 29.67 ? 295 GLU A CB 1 ATOM 2322 C CG . GLU A 1 295 ? 33.495 8.737 26.536 1.00 27.56 ? 295 GLU A CG 1 ATOM 2323 C CD . GLU A 1 295 ? 33.593 7.681 25.431 1.00 30.03 ? 295 GLU A CD 1 ATOM 2324 O OE1 . GLU A 1 295 ? 33.595 6.495 25.717 1.00 30.75 ? 295 GLU A OE1 1 ATOM 2325 O OE2 . GLU A 1 295 ? 33.703 8.049 24.270 1.00 29.09 ? 295 GLU A OE2 1 ATOM 2326 N N . ALA A 1 296 ? 30.152 8.158 29.869 1.00 29.20 ? 296 ALA A N 1 ATOM 2327 C CA . ALA A 1 296 ? 29.323 7.508 30.918 1.00 27.64 ? 296 ALA A CA 1 ATOM 2328 C C . ALA A 1 296 ? 27.935 7.106 30.416 1.00 22.73 ? 296 ALA A C 1 ATOM 2329 O O . ALA A 1 296 ? 27.532 5.957 30.557 1.00 24.64 ? 296 ALA A O 1 ATOM 2330 C CB . ALA A 1 296 ? 29.187 8.465 32.093 1.00 25.39 ? 296 ALA A CB 1 ATOM 2331 N N . ARG A 1 297 ? 27.242 8.062 29.806 1.00 22.45 ? 297 ARG A N 1 ATOM 2332 C CA . ARG A 1 297 ? 25.944 7.847 29.143 1.00 23.29 ? 297 ARG A CA 1 ATOM 2333 C C . ARG A 1 297 ? 25.957 6.655 28.181 1.00 25.83 ? 297 ARG A C 1 ATOM 2334 O O . ARG A 1 297 ? 25.096 5.781 28.226 1.00 22.65 ? 297 ARG A O 1 ATOM 2335 C CB . ARG A 1 297 ? 25.558 9.076 28.431 1.00 24.69 ? 297 ARG A CB 1 ATOM 2336 C CG . ARG A 1 297 ? 24.307 8.976 27.561 1.00 25.98 ? 297 ARG A CG 1 ATOM 2337 C CD . ARG A 1 297 ? 23.841 10.336 27.156 1.00 26.78 ? 297 ARG A CD 1 ATOM 2338 N NE . ARG A 1 297 ? 22.722 10.199 26.251 1.00 27.65 ? 297 ARG A NE 1 ATOM 2339 C CZ . ARG A 1 297 ? 22.691 10.578 24.974 1.00 27.12 ? 297 ARG A CZ 1 ATOM 2340 N NH1 . ARG A 1 297 ? 23.723 11.204 24.399 1.00 24.64 ? 297 ARG A NH1 1 ATOM 2341 N NH2 . ARG A 1 297 ? 21.574 10.370 24.282 1.00 28.75 ? 297 ARG A NH2 1 ATOM 2342 N N . LYS A 1 298 ? 26.985 6.593 27.350 1.00 25.93 ? 298 LYS A N 1 ATOM 2343 C CA . LYS A 1 298 ? 27.103 5.540 26.383 1.00 27.29 ? 298 LYS A CA 1 ATOM 2344 C C . LYS A 1 298 ? 27.260 4.185 27.050 1.00 23.84 ? 298 LYS A C 1 ATOM 2345 O O . LYS A 1 298 ? 26.649 3.226 26.630 1.00 24.28 ? 298 LYS A O 1 ATOM 2346 C CB . LYS A 1 298 ? 28.269 5.866 25.450 1.00 30.24 ? 298 LYS A CB 1 ATOM 2347 C CG . LYS A 1 298 ? 28.412 4.991 24.237 1.00 33.23 ? 298 LYS A CG 1 ATOM 2348 C CD . LYS A 1 298 ? 29.291 5.695 23.184 1.00 36.24 ? 298 LYS A CD 1 ATOM 2349 C CE . LYS A 1 298 ? 30.112 4.714 22.354 1.00 40.12 ? 298 LYS A CE 1 ATOM 2350 N NZ . LYS A 1 298 ? 30.734 5.452 21.211 1.00 41.28 ? 298 LYS A NZ 1 ATOM 2351 N N . ILE A 1 299 ? 28.058 4.105 28.108 1.00 24.32 ? 299 ILE A N 1 ATOM 2352 C CA . ILE A 1 299 ? 28.206 2.866 28.838 1.00 23.41 ? 299 ILE A CA 1 ATOM 2353 C C . ILE A 1 299 ? 26.916 2.402 29.569 1.00 21.38 ? 299 ILE A C 1 ATOM 2354 O O . ILE A 1 299 ? 26.563 1.201 29.562 1.00 20.97 ? 299 ILE A O 1 ATOM 2355 C CB . ILE A 1 299 ? 29.370 2.989 29.907 1.00 27.54 ? 299 ILE A CB 1 ATOM 2356 C CG1 . ILE A 1 299 ? 30.717 3.128 29.200 1.00 30.90 ? 299 ILE A CG1 1 ATOM 2357 C CG2 . ILE A 1 299 ? 29.334 1.825 30.892 1.00 23.25 ? 299 ILE A CG2 1 ATOM 2358 C CD1 . ILE A 1 299 ? 31.861 3.593 30.096 1.00 30.19 ? 299 ILE A CD1 1 ATOM 2359 N N . LEU A 1 300 ? 26.204 3.358 30.163 1.00 22.94 ? 300 LEU A N 1 ATOM 2360 C CA . LEU A 1 300 ? 24.929 3.067 30.884 1.00 21.51 ? 300 LEU A CA 1 ATOM 2361 C C . LEU A 1 300 ? 23.856 2.560 29.905 1.00 20.16 ? 300 LEU A C 1 ATOM 2362 O O . LEU A 1 300 ? 23.162 1.492 30.127 1.00 16.22 ? 300 LEU A O 1 ATOM 2363 C CB . LEU A 1 300 ? 24.434 4.295 31.618 1.00 22.14 ? 300 LEU A CB 1 ATOM 2364 C CG . LEU A 1 300 ? 23.369 3.922 32.676 1.00 25.59 ? 300 LEU A CG 1 ATOM 2365 C CD1 . LEU A 1 300 ? 23.938 3.005 33.736 1.00 26.58 ? 300 LEU A CD1 1 ATOM 2366 C CD2 . LEU A 1 300 ? 22.805 5.171 33.332 1.00 26.93 ? 300 LEU A CD2 1 ATOM 2367 N N . GLY A 1 301 ? 23.762 3.284 28.786 1.00 19.78 ? 301 GLY A N 1 ATOM 2368 C CA . GLY A 1 301 ? 23.008 2.778 27.639 1.00 20.16 ? 301 GLY A CA 1 ATOM 2369 C C . GLY A 1 301 ? 23.295 1.310 27.285 1.00 21.06 ? 301 GLY A C 1 ATOM 2370 O O . GLY A 1 301 ? 22.378 0.506 27.060 1.00 20.99 ? 301 GLY A O 1 ATOM 2371 N N . ALA A 1 302 ? 24.573 0.935 27.203 1.00 24.22 ? 302 ALA A N 1 ATOM 2372 C CA . ALA A 1 302 ? 24.938 -0.439 26.830 1.00 21.49 ? 302 ALA A CA 1 ATOM 2373 C C . ALA A 1 302 ? 24.590 -1.420 27.904 1.00 19.66 ? 302 ALA A C 1 ATOM 2374 O O . ALA A 1 302 ? 24.142 -2.535 27.642 1.00 22.59 ? 302 ALA A O 1 ATOM 2375 C CB . ALA A 1 302 ? 26.431 -0.519 26.543 1.00 23.17 ? 302 ALA A CB 1 ATOM 2376 N N . PHE A 1 303 ? 24.845 -1.028 29.138 1.00 23.48 ? 303 PHE A N 1 ATOM 2377 C CA . PHE A 1 303 ? 24.438 -1.816 30.313 1.00 20.93 ? 303 PHE A CA 1 ATOM 2378 C C . PHE A 1 303 ? 22.933 -2.185 30.204 1.00 18.75 ? 303 PHE A C 1 ATOM 2379 O O . PHE A 1 303 ? 22.534 -3.326 30.351 1.00 17.05 ? 303 PHE A O 1 ATOM 2380 C CB . PHE A 1 303 ? 24.689 -1.040 31.612 1.00 21.21 ? 303 PHE A CB 1 ATOM 2381 C CG . PHE A 1 303 ? 24.051 -1.696 32.848 1.00 20.98 ? 303 PHE A CG 1 ATOM 2382 C CD1 . PHE A 1 303 ? 24.736 -2.657 33.572 1.00 21.36 ? 303 PHE A CD1 1 ATOM 2383 C CD2 . PHE A 1 303 ? 22.773 -1.352 33.263 1.00 24.09 ? 303 PHE A CD2 1 ATOM 2384 C CE1 . PHE A 1 303 ? 24.201 -3.226 34.698 1.00 22.34 ? 303 PHE A CE1 1 ATOM 2385 C CE2 . PHE A 1 303 ? 22.194 -1.967 34.362 1.00 22.29 ? 303 PHE A CE2 1 ATOM 2386 C CZ . PHE A 1 303 ? 22.903 -2.901 35.080 1.00 20.97 ? 303 PHE A CZ 1 ATOM 2387 N N . ILE A 1 304 ? 22.108 -1.198 29.870 1.00 19.05 ? 304 ILE A N 1 ATOM 2388 C CA . ILE A 1 304 ? 20.625 -1.447 29.777 1.00 19.06 ? 304 ILE A CA 1 ATOM 2389 C C . ILE A 1 304 ? 20.314 -2.454 28.662 1.00 21.24 ? 304 ILE A C 1 ATOM 2390 O O . ILE A 1 304 ? 19.522 -3.411 28.842 1.00 19.00 ? 304 ILE A O 1 ATOM 2391 C CB . ILE A 1 304 ? 19.828 -0.136 29.652 1.00 18.67 ? 304 ILE A CB 1 ATOM 2392 C CG1 . ILE A 1 304 ? 19.932 0.621 30.981 1.00 17.45 ? 304 ILE A CG1 1 ATOM 2393 C CG2 . ILE A 1 304 ? 18.347 -0.386 29.390 1.00 17.73 ? 304 ILE A CG2 1 ATOM 2394 C CD1 . ILE A 1 304 ? 19.345 2.011 31.001 1.00 19.00 ? 304 ILE A CD1 1 ATOM 2395 N N . GLN A 1 305 ? 20.989 -2.280 27.523 1.00 21.46 ? 305 GLN A N 1 ATOM 2396 C CA . GLN A 1 305 ? 20.772 -3.195 26.407 1.00 17.97 ? 305 GLN A CA 1 ATOM 2397 C C . GLN A 1 305 ? 21.189 -4.575 26.732 1.00 16.86 ? 305 GLN A C 1 ATOM 2398 O O . GLN A 1 305 ? 20.484 -5.503 26.438 1.00 19.71 ? 305 GLN A O 1 ATOM 2399 C CB . GLN A 1 305 ? 21.506 -2.714 25.162 1.00 18.59 ? 305 GLN A CB 1 ATOM 2400 C CG . GLN A 1 305 ? 21.022 -1.375 24.687 1.00 17.99 ? 305 GLN A CG 1 ATOM 2401 C CD . GLN A 1 305 ? 21.735 -0.932 23.413 1.00 19.32 ? 305 GLN A CD 1 ATOM 2402 O OE1 . GLN A 1 305 ? 22.779 -1.471 23.051 1.00 20.83 ? 305 GLN A OE1 1 ATOM 2403 N NE2 . GLN A 1 305 ? 21.214 0.115 22.770 1.00 20.58 ? 305 GLN A NE2 1 ATOM 2404 N N . ILE A 1 306 ? 22.277 -4.734 27.464 1.00 21.27 ? 306 ILE A N 1 ATOM 2405 C CA . ILE A 1 306 ? 22.794 -6.074 27.747 1.00 21.35 ? 306 ILE A CA 1 ATOM 2406 C C . ILE A 1 306 ? 21.953 -6.860 28.737 1.00 21.78 ? 306 ILE A C 1 ATOM 2407 O O . ILE A 1 306 ? 21.542 -7.999 28.474 1.00 24.86 ? 306 ILE A O 1 ATOM 2408 C CB . ILE A 1 306 ? 24.262 -6.011 28.163 1.00 22.91 ? 306 ILE A CB 1 ATOM 2409 C CG1 . ILE A 1 306 ? 25.090 -5.582 26.934 1.00 22.95 ? 306 ILE A CG1 1 ATOM 2410 C CG2 . ILE A 1 306 ? 24.708 -7.367 28.751 1.00 22.64 ? 306 ILE A CG2 1 ATOM 2411 C CD1 . ILE A 1 306 ? 26.446 -5.057 27.308 1.00 23.09 ? 306 ILE A CD1 1 ATOM 2412 N N . ILE A 1 307 ? 21.607 -6.207 29.829 1.00 22.70 ? 307 ILE A N 1 ATOM 2413 C CA . ILE A 1 307 ? 20.726 -6.798 30.798 1.00 21.26 ? 307 ILE A CA 1 ATOM 2414 C C . ILE A 1 307 ? 19.373 -7.113 30.148 1.00 18.95 ? 307 ILE A C 1 ATOM 2415 O O . ILE A 1 307 ? 18.802 -8.196 30.299 1.00 23.72 ? 307 ILE A O 1 ATOM 2416 C CB . ILE A 1 307 ? 20.522 -5.860 32.009 1.00 22.83 ? 307 ILE A CB 1 ATOM 2417 C CG1 . ILE A 1 307 ? 21.830 -5.467 32.667 1.00 26.13 ? 307 ILE A CG1 1 ATOM 2418 C CG2 . ILE A 1 307 ? 19.595 -6.530 33.030 1.00 23.75 ? 307 ILE A CG2 1 ATOM 2419 C CD1 . ILE A 1 307 ? 22.568 -6.645 33.307 1.00 27.73 ? 307 ILE A CD1 1 ATOM 2420 N N . THR A 1 308 ? 18.852 -6.192 29.384 1.00 20.98 ? 308 THR A N 1 ATOM 2421 C CA . THR A 1 308 ? 17.565 -6.455 28.717 1.00 18.26 ? 308 THR A CA 1 ATOM 2422 C C . THR A 1 308 ? 17.604 -7.650 27.768 1.00 19.44 ? 308 THR A C 1 ATOM 2423 O O . THR A 1 308 ? 16.772 -8.579 27.896 1.00 20.47 ? 308 THR A O 1 ATOM 2424 C CB . THR A 1 308 ? 17.069 -5.220 27.999 1.00 19.76 ? 308 THR A CB 1 ATOM 2425 O OG1 . THR A 1 308 ? 16.997 -4.142 28.937 1.00 22.09 ? 308 THR A OG1 1 ATOM 2426 C CG2 . THR A 1 308 ? 15.716 -5.445 27.397 1.00 19.18 ? 308 THR A CG2 1 ATOM 2427 N N . PHE A 1 309 ? 18.578 -7.667 26.838 1.00 20.92 ? 309 PHE A N 1 ATOM 2428 C CA . PHE A 1 309 ? 18.607 -8.729 25.813 1.00 22.41 ? 309 PHE A CA 1 ATOM 2429 C C . PHE A 1 309 ? 19.215 -10.066 26.292 1.00 20.34 ? 309 PHE A C 1 ATOM 2430 O O . PHE A 1 309 ? 18.709 -11.077 25.946 1.00 23.28 ? 309 PHE A O 1 ATOM 2431 C CB . PHE A 1 309 ? 19.239 -8.218 24.507 1.00 22.04 ? 309 PHE A CB 1 ATOM 2432 C CG . PHE A 1 309 ? 18.295 -7.405 23.664 1.00 21.30 ? 309 PHE A CG 1 ATOM 2433 C CD1 . PHE A 1 309 ? 17.931 -6.133 24.042 1.00 19.80 ? 309 PHE A CD1 1 ATOM 2434 C CD2 . PHE A 1 309 ? 17.725 -7.933 22.525 1.00 21.27 ? 309 PHE A CD2 1 ATOM 2435 C CE1 . PHE A 1 309 ? 17.067 -5.378 23.258 1.00 20.10 ? 309 PHE A CE1 1 ATOM 2436 C CE2 . PHE A 1 309 ? 16.826 -7.187 21.730 1.00 19.06 ? 309 PHE A CE2 1 ATOM 2437 C CZ . PHE A 1 309 ? 16.515 -5.903 22.076 1.00 19.18 ? 309 PHE A CZ 1 ATOM 2438 N N . ARG A 1 310 ? 20.249 -10.057 27.127 1.00 22.10 ? 310 ARG A N 1 ATOM 2439 C CA . ARG A 1 310 ? 20.896 -11.283 27.628 1.00 20.27 ? 310 ARG A CA 1 ATOM 2440 C C . ARG A 1 310 ? 20.079 -11.897 28.732 1.00 20.77 ? 310 ARG A C 1 ATOM 2441 O O . ARG A 1 310 ? 19.840 -13.108 28.741 1.00 19.81 ? 310 ARG A O 1 ATOM 2442 C CB . ARG A 1 310 ? 22.349 -10.984 28.098 1.00 23.20 ? 310 ARG A CB 1 ATOM 2443 C CG . ARG A 1 310 ? 23.174 -12.205 28.584 1.00 26.69 ? 310 ARG A CG 1 ATOM 2444 C CD . ARG A 1 310 ? 24.465 -11.797 29.292 1.00 29.83 ? 310 ARG A CD 1 ATOM 2445 N NE . ARG A 1 310 ? 24.150 -11.190 30.588 1.00 30.46 ? 310 ARG A NE 1 ATOM 2446 C CZ . ARG A 1 310 ? 24.875 -10.270 31.201 1.00 28.90 ? 310 ARG A CZ 1 ATOM 2447 N NH1 . ARG A 1 310 ? 26.023 -9.858 30.735 1.00 31.10 ? 310 ARG A NH1 1 ATOM 2448 N NH2 . ARG A 1 310 ? 24.444 -9.752 32.332 1.00 29.76 ? 310 ARG A NH2 1 ATOM 2449 N N . ASP A 1 311 ? 19.563 -11.088 29.653 1.00 20.89 ? 311 ASP A N 1 ATOM 2450 C CA . ASP A 1 311 ? 18.943 -11.682 30.908 1.00 23.06 ? 311 ASP A CA 1 ATOM 2451 C C . ASP A 1 311 ? 17.416 -11.645 30.864 1.00 21.34 ? 311 ASP A C 1 ATOM 2452 O O . ASP A 1 311 ? 16.760 -12.612 31.160 1.00 23.58 ? 311 ASP A O 1 ATOM 2453 C CB . ASP A 1 311 ? 19.457 -10.964 32.184 1.00 23.85 ? 311 ASP A CB 1 ATOM 2454 C CG . ASP A 1 311 ? 20.965 -10.918 32.261 1.00 26.07 ? 311 ASP A CG 1 ATOM 2455 O OD1 . ASP A 1 311 ? 21.558 -11.886 31.796 1.00 29.12 ? 311 ASP A OD1 1 ATOM 2456 O OD2 . ASP A 1 311 ? 21.579 -9.915 32.700 1.00 27.58 ? 311 ASP A OD2 1 ATOM 2457 N N . TYR A 1 312 ? 16.853 -10.508 30.468 1.00 22.22 ? 312 TYR A N 1 ATOM 2458 C CA . TYR A 1 312 ? 15.404 -10.250 30.643 1.00 19.86 ? 312 TYR A CA 1 ATOM 2459 C C . TYR A 1 312 ? 14.510 -10.882 29.570 1.00 19.81 ? 312 TYR A C 1 ATOM 2460 O O . TYR A 1 312 ? 13.611 -11.650 29.896 1.00 18.20 ? 312 TYR A O 1 ATOM 2461 C CB . TYR A 1 312 ? 15.163 -8.739 30.769 1.00 20.35 ? 312 TYR A CB 1 ATOM 2462 C CG . TYR A 1 312 ? 13.671 -8.396 30.900 1.00 20.16 ? 312 TYR A CG 1 ATOM 2463 C CD1 . TYR A 1 312 ? 12.985 -8.618 32.093 1.00 17.57 ? 312 TYR A CD1 1 ATOM 2464 C CD2 . TYR A 1 312 ? 12.967 -7.828 29.818 1.00 18.13 ? 312 TYR A CD2 1 ATOM 2465 C CE1 . TYR A 1 312 ? 11.609 -8.314 32.218 1.00 18.29 ? 312 TYR A CE1 1 ATOM 2466 C CE2 . TYR A 1 312 ? 11.627 -7.447 29.944 1.00 17.97 ? 312 TYR A CE2 1 ATOM 2467 C CZ . TYR A 1 312 ? 10.936 -7.738 31.115 1.00 18.68 ? 312 TYR A CZ 1 ATOM 2468 O OH . TYR A 1 312 ? 9.627 -7.425 31.176 1.00 17.45 ? 312 TYR A OH 1 ATOM 2469 N N . LEU A 1 313 ? 14.762 -10.608 28.305 1.00 18.31 ? 313 LEU A N 1 ATOM 2470 C CA . LEU A 1 313 ? 13.855 -11.102 27.249 1.00 19.17 ? 313 LEU A CA 1 ATOM 2471 C C . LEU A 1 313 ? 13.816 -12.624 27.167 1.00 20.28 ? 313 LEU A C 1 ATOM 2472 O O . LEU A 1 313 ? 12.718 -13.214 26.929 1.00 19.65 ? 313 LEU A O 1 ATOM 2473 C CB . LEU A 1 313 ? 14.228 -10.512 25.915 1.00 20.36 ? 313 LEU A CB 1 ATOM 2474 C CG . LEU A 1 313 ? 14.132 -8.998 25.817 1.00 23.07 ? 313 LEU A CG 1 ATOM 2475 C CD1 . LEU A 1 313 ? 14.754 -8.552 24.502 1.00 23.07 ? 313 LEU A CD1 1 ATOM 2476 C CD2 . LEU A 1 313 ? 12.682 -8.573 25.876 1.00 24.49 ? 313 LEU A CD2 1 ATOM 2477 N N . PRO A 1 314 ? 14.957 -13.293 27.443 1.00 21.11 ? 314 PRO A N 1 ATOM 2478 C CA . PRO A 1 314 ? 14.864 -14.762 27.345 1.00 20.22 ? 314 PRO A CA 1 ATOM 2479 C C . PRO A 1 314 ? 13.883 -15.300 28.372 1.00 23.18 ? 314 PRO A C 1 ATOM 2480 O O . PRO A 1 314 ? 13.240 -16.342 28.166 1.00 20.82 ? 314 PRO A O 1 ATOM 2481 C CB . PRO A 1 314 ? 16.278 -15.219 27.620 1.00 21.99 ? 314 PRO A CB 1 ATOM 2482 C CG . PRO A 1 314 ? 17.114 -14.118 27.088 1.00 22.16 ? 314 PRO A CG 1 ATOM 2483 C CD . PRO A 1 314 ? 16.369 -12.831 27.420 1.00 20.51 ? 314 PRO A CD 1 ATOM 2484 N N . ILE A 1 315 ? 13.678 -14.562 29.450 1.00 24.36 ? 315 ILE A N 1 ATOM 2485 C CA . ILE A 1 315 ? 12.762 -15.107 30.433 1.00 23.92 ? 315 ILE A CA 1 ATOM 2486 C C . ILE A 1 315 ? 11.370 -14.619 30.253 1.00 24.08 ? 315 ILE A C 1 ATOM 2487 O O . ILE A 1 315 ? 10.457 -15.248 30.742 1.00 25.73 ? 315 ILE A O 1 ATOM 2488 C CB . ILE A 1 315 ? 13.319 -15.061 31.865 1.00 27.66 ? 315 ILE A CB 1 ATOM 2489 C CG1 . ILE A 1 315 ? 13.717 -13.690 32.355 1.00 25.03 ? 315 ILE A CG1 1 ATOM 2490 C CG2 . ILE A 1 315 ? 14.579 -15.924 31.913 1.00 29.10 ? 315 ILE A CG2 1 ATOM 2491 C CD1 . ILE A 1 315 ? 14.568 -13.710 33.631 1.00 24.02 ? 315 ILE A CD1 1 ATOM 2492 N N . VAL A 1 316 ? 11.189 -13.586 29.436 1.00 21.01 ? 316 VAL A N 1 ATOM 2493 C CA . VAL A 1 316 ? 9.853 -13.214 28.946 1.00 19.21 ? 316 VAL A CA 1 ATOM 2494 C C . VAL A 1 316 ? 9.416 -14.110 27.785 1.00 19.44 ? 316 VAL A C 1 ATOM 2495 O O . VAL A 1 316 ? 8.279 -14.664 27.764 1.00 18.76 ? 316 VAL A O 1 ATOM 2496 C CB . VAL A 1 316 ? 9.839 -11.733 28.545 1.00 18.61 ? 316 VAL A CB 1 ATOM 2497 C CG1 . VAL A 1 316 ? 8.539 -11.329 27.906 1.00 20.31 ? 316 VAL A CG1 1 ATOM 2498 C CG2 . VAL A 1 316 ? 10.133 -10.876 29.749 1.00 21.22 ? 316 VAL A CG2 1 ATOM 2499 N N . LEU A 1 317 ? 10.291 -14.261 26.802 1.00 20.54 ? 317 LEU A N 1 ATOM 2500 C CA . LEU A 1 317 ? 9.931 -14.950 25.570 1.00 21.21 ? 317 LEU A CA 1 ATOM 2501 C C . LEU A 1 317 ? 10.119 -16.446 25.594 1.00 23.78 ? 317 LEU A C 1 ATOM 2502 O O . LEU A 1 317 ? 9.561 -17.124 24.726 1.00 23.01 ? 317 LEU A O 1 ATOM 2503 C CB . LEU A 1 317 ? 10.689 -14.350 24.385 1.00 21.65 ? 317 LEU A CB 1 ATOM 2504 C CG . LEU A 1 317 ? 10.330 -12.869 24.147 1.00 22.00 ? 317 LEU A CG 1 ATOM 2505 C CD1 . LEU A 1 317 ? 11.185 -12.278 23.041 1.00 21.33 ? 317 LEU A CD1 1 ATOM 2506 C CD2 . LEU A 1 317 ? 8.855 -12.636 23.917 1.00 22.22 ? 317 LEU A CD2 1 ATOM 2507 N N . GLY A 1 318 ? 10.863 -17.000 26.562 1.00 27.42 ? 318 GLY A N 1 ATOM 2508 C CA . GLY A 1 318 ? 11.009 -18.469 26.651 1.00 26.79 ? 318 GLY A CA 1 ATOM 2509 C C . GLY A 1 318 ? 11.456 -19.068 25.310 1.00 29.21 ? 318 GLY A C 1 ATOM 2510 O O . GLY A 1 318 ? 12.393 -18.559 24.652 1.00 27.28 ? 318 GLY A O 1 ATOM 2511 N N . SER A 1 319 ? 10.727 -20.090 24.872 1.00 32.07 ? 319 SER A N 1 ATOM 2512 C CA . SER A 1 319 ? 11.014 -20.825 23.618 1.00 32.29 ? 319 SER A CA 1 ATOM 2513 C C . SER A 1 319 ? 10.891 -19.984 22.363 1.00 33.94 ? 319 SER A C 1 ATOM 2514 O O . SER A 1 319 ? 11.373 -20.399 21.314 1.00 37.13 ? 319 SER A O 1 ATOM 2515 C CB . SER A 1 319 ? 10.067 -22.016 23.471 1.00 32.17 ? 319 SER A CB 1 ATOM 2516 O OG . SER A 1 319 ? 8.717 -21.584 23.497 1.00 26.72 ? 319 SER A OG 1 ATOM 2517 N N . GLU A 1 320 ? 10.287 -18.802 22.465 1.00 28.59 ? 320 GLU A N 1 ATOM 2518 C CA . GLU A 1 320 ? 10.118 -17.929 21.323 1.00 31.62 ? 320 GLU A CA 1 ATOM 2519 C C . GLU A 1 320 ? 11.232 -16.938 21.159 1.00 27.09 ? 320 GLU A C 1 ATOM 2520 O O . GLU A 1 320 ? 11.276 -16.232 20.160 1.00 32.10 ? 320 GLU A O 1 ATOM 2521 C CB . GLU A 1 320 ? 8.797 -17.174 21.399 1.00 33.58 ? 320 GLU A CB 1 ATOM 2522 C CG . GLU A 1 320 ? 7.602 -18.032 21.683 1.00 36.89 ? 320 GLU A CG 1 ATOM 2523 C CD . GLU A 1 320 ? 7.043 -18.616 20.425 1.00 41.43 ? 320 GLU A CD 1 ATOM 2524 O OE1 . GLU A 1 320 ? 6.286 -17.906 19.706 1.00 40.52 ? 320 GLU A OE1 1 ATOM 2525 O OE2 . GLU A 1 320 ? 7.423 -19.772 20.173 1.00 38.04 ? 320 GLU A OE2 1 ATOM 2526 N N . MET A 1 321 ? 12.157 -16.891 22.108 1.00 27.27 ? 321 MET A N 1 ATOM 2527 C CA . MET A 1 321 ? 13.248 -15.913 22.097 1.00 26.96 ? 321 MET A CA 1 ATOM 2528 C C . MET A 1 321 ? 13.988 -15.962 20.733 1.00 29.25 ? 321 MET A C 1 ATOM 2529 O O . MET A 1 321 ? 14.009 -14.992 19.998 1.00 24.90 ? 321 MET A O 1 ATOM 2530 C CB . MET A 1 321 ? 14.206 -16.204 23.234 1.00 27.72 ? 321 MET A CB 1 ATOM 2531 C CG . MET A 1 321 ? 15.413 -15.278 23.358 1.00 24.05 ? 321 MET A CG 1 ATOM 2532 S SD . MET A 1 321 ? 15.035 -13.564 23.766 1.00 25.38 ? 321 MET A SD 1 ATOM 2533 C CE . MET A 1 321 ? 16.529 -12.821 23.190 1.00 23.83 ? 321 MET A CE 1 ATOM 2534 N N . GLN A 1 322 ? 14.536 -17.128 20.400 1.00 31.37 ? 322 GLN A N 1 ATOM 2535 C CA . GLN A 1 322 ? 15.327 -17.327 19.187 1.00 38.56 ? 322 GLN A CA 1 ATOM 2536 C C . GLN A 1 322 ? 14.503 -17.029 17.928 1.00 37.90 ? 322 GLN A C 1 ATOM 2537 O O . GLN A 1 322 ? 14.980 -16.409 17.021 1.00 39.46 ? 322 GLN A O 1 ATOM 2538 C CB . GLN A 1 322 ? 15.884 -18.755 19.107 1.00 50.63 ? 322 GLN A CB 1 ATOM 2539 C CG . GLN A 1 322 ? 16.284 -19.416 20.418 1.00 65.86 ? 322 GLN A CG 1 ATOM 2540 C CD . GLN A 1 322 ? 15.137 -20.141 21.146 1.00 72.65 ? 322 GLN A CD 1 ATOM 2541 O OE1 . GLN A 1 322 ? 14.391 -19.544 21.852 1.00 77.38 ? 322 GLN A OE1 1 ATOM 2542 N NE2 . GLN A 1 322 ? 15.066 -21.459 20.992 1.00 70.96 ? 322 GLN A NE2 1 ATOM 2543 N N . LYS A 1 323 ? 13.265 -17.461 17.917 1.00 30.49 ? 323 LYS A N 1 ATOM 2544 C CA . LYS A 1 323 ? 12.356 -17.213 16.808 1.00 32.10 ? 323 LYS A CA 1 ATOM 2545 C C . LYS A 1 323 ? 12.230 -15.723 16.476 1.00 35.95 ? 323 LYS A C 1 ATOM 2546 O O . LYS A 1 323 ? 12.293 -15.368 15.296 1.00 30.67 ? 323 LYS A O 1 ATOM 2547 C CB . LYS A 1 323 ? 10.973 -17.792 17.092 1.00 33.77 ? 323 LYS A CB 1 ATOM 2548 C CG . LYS A 1 323 ? 9.866 -17.268 16.197 1.00 35.71 ? 323 LYS A CG 1 ATOM 2549 C CD . LYS A 1 323 ? 8.639 -18.131 16.259 1.00 41.23 ? 323 LYS A CD 1 ATOM 2550 C CE . LYS A 1 323 ? 7.573 -17.539 15.346 1.00 47.59 ? 323 LYS A CE 1 ATOM 2551 N NZ . LYS A 1 323 ? 6.760 -18.611 14.709 1.00 53.18 ? 323 LYS A NZ 1 ATOM 2552 N N . TRP A 1 324 ? 12.049 -14.837 17.472 1.00 33.97 ? 324 TRP A N 1 ATOM 2553 C CA . TRP A 1 324 ? 11.845 -13.421 17.123 1.00 30.09 ? 324 TRP A CA 1 ATOM 2554 C C . TRP A 1 324 ? 13.121 -12.667 17.160 1.00 29.88 ? 324 TRP A C 1 ATOM 2555 O O . TRP A 1 324 ? 13.245 -11.649 16.506 1.00 32.07 ? 324 TRP A O 1 ATOM 2556 C CB . TRP A 1 324 ? 10.763 -12.729 18.003 1.00 29.48 ? 324 TRP A CB 1 ATOM 2557 C CG . TRP A 1 324 ? 9.510 -13.433 17.914 1.00 26.79 ? 324 TRP A CG 1 ATOM 2558 C CD1 . TRP A 1 324 ? 9.034 -14.389 18.776 1.00 30.26 ? 324 TRP A CD1 1 ATOM 2559 C CD2 . TRP A 1 324 ? 8.570 -13.342 16.881 1.00 26.18 ? 324 TRP A CD2 1 ATOM 2560 N NE1 . TRP A 1 324 ? 7.840 -14.884 18.330 1.00 26.81 ? 324 TRP A NE1 1 ATOM 2561 C CE2 . TRP A 1 324 ? 7.545 -14.274 17.150 1.00 25.65 ? 324 TRP A CE2 1 ATOM 2562 C CE3 . TRP A 1 324 ? 8.484 -12.577 15.720 1.00 27.99 ? 324 TRP A CE3 1 ATOM 2563 C CZ2 . TRP A 1 324 ? 6.471 -14.436 16.311 1.00 26.58 ? 324 TRP A CZ2 1 ATOM 2564 C CZ3 . TRP A 1 324 ? 7.437 -12.758 14.912 1.00 27.06 ? 324 TRP A CZ3 1 ATOM 2565 C CH2 . TRP A 1 324 ? 6.433 -13.682 15.196 1.00 24.17 ? 324 TRP A CH2 1 ATOM 2566 N N . ILE A 1 325 ? 14.076 -13.122 17.956 1.00 29.67 ? 325 ILE A N 1 ATOM 2567 C CA . ILE A 1 325 ? 15.298 -12.356 18.151 1.00 32.37 ? 325 ILE A CA 1 ATOM 2568 C C . ILE A 1 325 ? 16.473 -13.322 17.972 1.00 33.52 ? 325 ILE A C 1 ATOM 2569 O O . ILE A 1 325 ? 17.128 -13.745 18.930 1.00 32.62 ? 325 ILE A O 1 ATOM 2570 C CB . ILE A 1 325 ? 15.373 -11.610 19.518 1.00 34.01 ? 325 ILE A CB 1 ATOM 2571 C CG1 . ILE A 1 325 ? 14.067 -10.874 19.835 1.00 33.91 ? 325 ILE A CG1 1 ATOM 2572 C CG2 . ILE A 1 325 ? 16.498 -10.573 19.497 1.00 34.44 ? 325 ILE A CG2 1 ATOM 2573 C CD1 . ILE A 1 325 ? 14.039 -10.205 21.196 1.00 29.26 ? 325 ILE A CD1 1 ATOM 2574 N N . PRO A 1 326 ? 16.732 -13.671 16.718 1.00 36.80 ? 326 PRO A N 1 ATOM 2575 C CA . PRO A 1 326 ? 17.905 -14.480 16.398 1.00 40.25 ? 326 PRO A CA 1 ATOM 2576 C C . PRO A 1 326 ? 19.204 -13.714 16.613 1.00 37.74 ? 326 PRO A C 1 ATOM 2577 O O . PRO A 1 326 ? 19.168 -12.465 16.761 1.00 37.92 ? 326 PRO A O 1 ATOM 2578 C CB . PRO A 1 326 ? 17.684 -14.823 14.915 1.00 38.74 ? 326 PRO A CB 1 ATOM 2579 C CG . PRO A 1 326 ? 16.988 -13.648 14.389 1.00 40.04 ? 326 PRO A CG 1 ATOM 2580 C CD . PRO A 1 326 ? 16.085 -13.159 15.499 1.00 37.15 ? 326 PRO A CD 1 ATOM 2581 N N . PRO A 1 327 ? 20.342 -14.431 16.667 1.00 38.99 ? 327 PRO A N 1 ATOM 2582 C CA . PRO A 1 327 ? 21.636 -13.817 16.969 1.00 36.04 ? 327 PRO A CA 1 ATOM 2583 C C . PRO A 1 327 ? 21.840 -12.634 16.067 1.00 33.10 ? 327 PRO A C 1 ATOM 2584 O O . PRO A 1 327 ? 21.370 -12.659 14.934 1.00 31.20 ? 327 PRO A O 1 ATOM 2585 C CB . PRO A 1 327 ? 22.643 -14.918 16.704 1.00 38.15 ? 327 PRO A CB 1 ATOM 2586 C CG . PRO A 1 327 ? 21.862 -16.168 16.993 1.00 42.06 ? 327 PRO A CG 1 ATOM 2587 C CD . PRO A 1 327 ? 20.483 -15.890 16.468 1.00 41.22 ? 327 PRO A CD 1 ATOM 2588 N N . TYR A 1 328 ? 22.453 -11.582 16.615 1.00 28.41 ? 328 TYR A N 1 ATOM 2589 C CA . TYR A 1 328 ? 22.543 -10.304 15.942 1.00 29.94 ? 328 TYR A CA 1 ATOM 2590 C C . TYR A 1 328 ? 23.418 -10.483 14.717 1.00 38.17 ? 328 TYR A C 1 ATOM 2591 O O . TYR A 1 328 ? 24.378 -11.238 14.795 1.00 37.24 ? 328 TYR A O 1 ATOM 2592 C CB . TYR A 1 328 ? 23.252 -9.374 16.880 1.00 27.92 ? 328 TYR A CB 1 ATOM 2593 C CG . TYR A 1 328 ? 23.451 -7.995 16.421 1.00 28.35 ? 328 TYR A CG 1 ATOM 2594 C CD1 . TYR A 1 328 ? 22.375 -7.217 16.011 1.00 28.69 ? 328 TYR A CD1 1 ATOM 2595 C CD2 . TYR A 1 328 ? 24.696 -7.401 16.468 1.00 28.55 ? 328 TYR A CD2 1 ATOM 2596 C CE1 . TYR A 1 328 ? 22.547 -5.910 15.634 1.00 29.31 ? 328 TYR A CE1 1 ATOM 2597 C CE2 . TYR A 1 328 ? 24.873 -6.080 16.062 1.00 27.27 ? 328 TYR A CE2 1 ATOM 2598 C CZ . TYR A 1 328 ? 23.790 -5.352 15.668 1.00 25.81 ? 328 TYR A CZ 1 ATOM 2599 O OH . TYR A 1 328 ? 23.915 -4.033 15.313 1.00 28.52 ? 328 TYR A OH 1 ATOM 2600 N N . GLN A 1 329 ? 23.118 -9.765 13.651 1.00 36.40 ? 329 GLN A N 1 ATOM 2601 C CA . GLN A 1 329 ? 23.929 -9.744 12.442 1.00 37.05 ? 329 GLN A CA 1 ATOM 2602 C C . GLN A 1 329 ? 24.220 -8.321 12.035 1.00 36.38 ? 329 GLN A C 1 ATOM 2603 O O . GLN A 1 329 ? 24.534 -8.081 10.889 1.00 43.49 ? 329 GLN A O 1 ATOM 2604 C CB . GLN A 1 329 ? 23.175 -10.359 11.251 1.00 39.42 ? 329 GLN A CB 1 ATOM 2605 C CG . GLN A 1 329 ? 22.514 -11.711 11.462 1.00 42.61 ? 329 GLN A CG 1 ATOM 2606 C CD . GLN A 1 329 ? 23.481 -12.826 11.810 1.00 50.64 ? 329 GLN A CD 1 ATOM 2607 O OE1 . GLN A 1 329 ? 23.074 -13.873 12.330 1.00 58.51 ? 329 GLN A OE1 1 ATOM 2608 N NE2 . GLN A 1 329 ? 24.771 -12.606 11.555 1.00 50.92 ? 329 GLN A NE2 1 ATOM 2609 N N . GLY A 1 330 ? 24.084 -7.350 12.919 1.00 32.91 ? 330 GLY A N 1 ATOM 2610 C CA . GLY A 1 330 ? 24.531 -5.989 12.603 1.00 31.14 ? 330 GLY A CA 1 ATOM 2611 C C . GLY A 1 330 ? 23.405 -5.047 12.255 1.00 30.33 ? 330 GLY A C 1 ATOM 2612 O O . GLY A 1 330 ? 22.268 -5.454 12.065 1.00 28.37 ? 330 GLY A O 1 ATOM 2613 N N . TYR A 1 331 ? 23.752 -3.779 12.179 1.00 28.21 ? 331 TYR A N 1 ATOM 2614 C CA . TYR A 1 331 ? 22.795 -2.749 12.033 1.00 29.99 ? 331 TYR A CA 1 ATOM 2615 C C . TYR A 1 331 ? 22.216 -2.891 10.669 1.00 32.72 ? 331 TYR A C 1 ATOM 2616 O O . TYR A 1 331 ? 22.950 -3.063 9.692 1.00 30.55 ? 331 TYR A O 1 ATOM 2617 C CB . TYR A 1 331 ? 23.471 -1.425 12.219 1.00 28.81 ? 331 TYR A CB 1 ATOM 2618 C CG . TYR A 1 331 ? 22.655 -0.227 11.829 1.00 32.20 ? 331 TYR A CG 1 ATOM 2619 C CD1 . TYR A 1 331 ? 21.442 0.064 12.433 1.00 31.52 ? 331 TYR A CD1 1 ATOM 2620 C CD2 . TYR A 1 331 ? 23.142 0.692 10.900 1.00 34.54 ? 331 TYR A CD2 1 ATOM 2621 C CE1 . TYR A 1 331 ? 20.719 1.200 12.075 1.00 29.87 ? 331 TYR A CE1 1 ATOM 2622 C CE2 . TYR A 1 331 ? 22.411 1.808 10.539 1.00 35.13 ? 331 TYR A CE2 1 ATOM 2623 C CZ . TYR A 1 331 ? 21.210 2.082 11.160 1.00 30.45 ? 331 TYR A CZ 1 ATOM 2624 O OH . TYR A 1 331 ? 20.460 3.214 10.779 1.00 27.45 ? 331 TYR A OH 1 ATOM 2625 N N . ASN A 1 332 ? 20.890 -2.885 10.595 1.00 30.03 ? 332 ASN A N 1 ATOM 2626 C CA . ASN A 1 332 ? 20.203 -2.805 9.298 1.00 29.09 ? 332 ASN A CA 1 ATOM 2627 C C . ASN A 1 332 ? 19.419 -1.526 9.291 1.00 27.74 ? 332 ASN A C 1 ATOM 2628 O O . ASN A 1 332 ? 18.383 -1.417 9.938 1.00 31.02 ? 332 ASN A O 1 ATOM 2629 C CB . ASN A 1 332 ? 19.380 -4.087 9.026 1.00 30.11 ? 332 ASN A CB 1 ATOM 2630 C CG . ASN A 1 332 ? 18.581 -4.018 7.741 1.00 34.67 ? 332 ASN A CG 1 ATOM 2631 O OD1 . ASN A 1 332 ? 18.500 -2.972 7.132 1.00 37.22 ? 332 ASN A OD1 1 ATOM 2632 N ND2 . ASN A 1 332 ? 17.939 -5.134 7.357 1.00 41.28 ? 332 ASN A ND2 1 ATOM 2633 N N . ASN A 1 333 ? 19.885 -0.546 8.531 1.00 26.26 ? 333 ASN A N 1 ATOM 2634 C CA . ASN A 1 333 ? 19.152 0.704 8.394 1.00 25.89 ? 333 ASN A CA 1 ATOM 2635 C C . ASN A 1 333 ? 17.860 0.642 7.580 1.00 24.86 ? 333 ASN A C 1 ATOM 2636 O O . ASN A 1 333 ? 17.258 1.660 7.372 1.00 21.57 ? 333 ASN A O 1 ATOM 2637 C CB . ASN A 1 333 ? 20.034 1.806 7.851 1.00 31.13 ? 333 ASN A CB 1 ATOM 2638 C CG . ASN A 1 333 ? 20.191 1.762 6.333 1.00 32.23 ? 333 ASN A CG 1 ATOM 2639 O OD1 . ASN A 1 333 ? 20.212 0.718 5.715 1.00 40.87 ? 333 ASN A OD1 1 ATOM 2640 N ND2 . ASN A 1 333 ? 20.258 2.899 5.752 1.00 33.64 ? 333 ASN A ND2 1 ATOM 2641 N N . SER A 1 334 ? 17.440 -0.530 7.109 1.00 22.66 ? 334 SER A N 1 ATOM 2642 C CA . SER A 1 334 ? 16.067 -0.645 6.552 1.00 27.35 ? 334 SER A CA 1 ATOM 2643 C C . SER A 1 334 ? 15.023 -1.048 7.617 1.00 25.34 ? 334 SER A C 1 ATOM 2644 O O . SER A 1 334 ? 13.847 -1.123 7.313 1.00 24.41 ? 334 SER A O 1 ATOM 2645 C CB . SER A 1 334 ? 16.004 -1.727 5.493 1.00 25.91 ? 334 SER A CB 1 ATOM 2646 O OG . SER A 1 334 ? 16.903 -1.414 4.462 1.00 28.54 ? 334 SER A OG 1 ATOM 2647 N N . VAL A 1 335 ? 15.485 -1.356 8.828 1.00 25.06 ? 335 VAL A N 1 ATOM 2648 C CA . VAL A 1 335 ? 14.588 -1.721 9.896 1.00 26.01 ? 335 VAL A CA 1 ATOM 2649 C C . VAL A 1 335 ? 13.958 -0.434 10.490 1.00 23.89 ? 335 VAL A C 1 ATOM 2650 O O . VAL A 1 335 ? 14.617 0.590 10.618 1.00 21.64 ? 335 VAL A O 1 ATOM 2651 C CB . VAL A 1 335 ? 15.276 -2.613 10.914 1.00 24.37 ? 335 VAL A CB 1 ATOM 2652 C CG1 . VAL A 1 335 ? 14.351 -2.810 12.126 1.00 28.66 ? 335 VAL A CG1 1 ATOM 2653 C CG2 . VAL A 1 335 ? 15.619 -3.967 10.288 1.00 23.88 ? 335 VAL A CG2 1 ATOM 2654 N N . ASP A 1 336 ? 12.647 -0.473 10.704 1.00 24.39 ? 336 ASP A N 1 ATOM 2655 C CA . ASP A 1 336 ? 11.929 0.590 11.416 1.00 24.30 ? 336 ASP A CA 1 ATOM 2656 C C . ASP A 1 336 ? 12.173 0.415 12.940 1.00 23.32 ? 336 ASP A C 1 ATOM 2657 O O . ASP A 1 336 ? 11.728 -0.532 13.539 1.00 23.29 ? 336 ASP A O 1 ATOM 2658 C CB . ASP A 1 336 ? 10.445 0.496 11.111 1.00 23.72 ? 336 ASP A CB 1 ATOM 2659 C CG . ASP A 1 336 ? 9.644 1.593 11.760 1.00 24.21 ? 336 ASP A CG 1 ATOM 2660 O OD1 . ASP A 1 336 ? 10.181 2.543 12.416 1.00 24.27 ? 336 ASP A OD1 1 ATOM 2661 O OD2 . ASP A 1 336 ? 8.427 1.546 11.596 1.00 24.04 ? 336 ASP A OD2 1 ATOM 2662 N N . PRO A 1 337 ? 12.904 1.332 13.557 1.00 21.88 ? 337 PRO A N 1 ATOM 2663 C CA . PRO A 1 337 ? 13.166 1.209 14.955 1.00 22.22 ? 337 PRO A CA 1 ATOM 2664 C C . PRO A 1 337 ? 12.043 1.819 15.862 1.00 23.06 ? 337 PRO A C 1 ATOM 2665 O O . PRO A 1 337 ? 12.139 1.763 17.094 1.00 20.73 ? 337 PRO A O 1 ATOM 2666 C CB . PRO A 1 337 ? 14.410 2.037 15.101 1.00 22.77 ? 337 PRO A CB 1 ATOM 2667 C CG . PRO A 1 337 ? 14.202 3.141 14.196 1.00 21.83 ? 337 PRO A CG 1 ATOM 2668 C CD . PRO A 1 337 ? 13.574 2.511 12.996 1.00 23.56 ? 337 PRO A CD 1 ATOM 2669 N N . ARG A 1 338 ? 10.995 2.383 15.260 1.00 20.76 ? 338 ARG A N 1 ATOM 2670 C CA . ARG A 1 338 ? 10.007 3.047 16.036 1.00 19.44 ? 338 ARG A CA 1 ATOM 2671 C C . ARG A 1 338 ? 9.248 2.041 16.879 1.00 18.30 ? 338 ARG A C 1 ATOM 2672 O O . ARG A 1 338 ? 8.933 0.910 16.443 1.00 18.62 ? 338 ARG A O 1 ATOM 2673 C CB . ARG A 1 338 ? 9.061 3.809 15.142 1.00 21.53 ? 338 ARG A CB 1 ATOM 2674 C CG . ARG A 1 338 ? 9.645 5.034 14.510 1.00 19.99 ? 338 ARG A CG 1 ATOM 2675 C CD . ARG A 1 338 ? 8.667 5.618 13.509 1.00 20.79 ? 338 ARG A CD 1 ATOM 2676 N NE . ARG A 1 338 ? 8.306 4.598 12.550 1.00 20.55 ? 338 ARG A NE 1 ATOM 2677 C CZ . ARG A 1 338 ? 7.214 4.611 11.816 1.00 19.08 ? 338 ARG A CZ 1 ATOM 2678 N NH1 . ARG A 1 338 ? 6.358 5.597 11.863 1.00 25.02 ? 338 ARG A NH1 1 ATOM 2679 N NH2 . ARG A 1 338 ? 6.957 3.588 11.068 1.00 20.57 ? 338 ARG A NH2 1 ATOM 2680 N N . ILE A 1 339 ? 8.883 2.472 18.063 1.00 20.27 ? 339 ILE A N 1 ATOM 2681 C CA . ILE A 1 339 ? 7.890 1.694 18.916 1.00 19.49 ? 339 ILE A CA 1 ATOM 2682 C C . ILE A 1 339 ? 6.533 1.802 18.312 1.00 18.57 ? 339 ILE A C 1 ATOM 2683 O O . ILE A 1 339 ? 6.102 2.868 17.945 1.00 18.91 ? 339 ILE A O 1 ATOM 2684 C CB . ILE A 1 339 ? 7.805 2.192 20.346 1.00 17.97 ? 339 ILE A CB 1 ATOM 2685 C CG1 . ILE A 1 339 ? 9.182 2.132 20.976 1.00 17.68 ? 339 ILE A CG1 1 ATOM 2686 C CG2 . ILE A 1 339 ? 6.784 1.388 21.163 1.00 18.24 ? 339 ILE A CG2 1 ATOM 2687 C CD1 . ILE A 1 339 ? 9.856 0.747 20.956 1.00 17.88 ? 339 ILE A CD1 1 ATOM 2688 N N . SER A 1 340 ? 5.827 0.676 18.228 1.00 16.62 ? 340 SER A N 1 ATOM 2689 C CA . SER A 1 340 ? 4.494 0.707 17.677 1.00 15.49 ? 340 SER A CA 1 ATOM 2690 C C . SER A 1 340 ? 3.499 1.019 18.765 1.00 16.67 ? 340 SER A C 1 ATOM 2691 O O . SER A 1 340 ? 3.769 0.770 19.946 1.00 15.70 ? 340 SER A O 1 ATOM 2692 C CB . SER A 1 340 ? 4.176 -0.654 17.077 1.00 15.48 ? 340 SER A CB 1 ATOM 2693 O OG . SER A 1 340 ? 4.352 -1.698 18.032 1.00 16.20 ? 340 SER A OG 1 ATOM 2694 N N . ASN A 1 341 ? 2.326 1.472 18.354 1.00 15.34 ? 341 ASN A N 1 ATOM 2695 C CA . ASN A 1 341 ? 1.269 1.838 19.258 1.00 16.02 ? 341 ASN A CA 1 ATOM 2696 C C . ASN A 1 341 ? 0.839 0.552 20.011 1.00 16.37 ? 341 ASN A C 1 ATOM 2697 O O . ASN A 1 341 ? 0.694 0.568 21.280 1.00 16.23 ? 341 ASN A O 1 ATOM 2698 C CB . ASN A 1 341 ? 0.150 2.514 18.458 1.00 16.86 ? 341 ASN A CB 1 ATOM 2699 C CG . ASN A 1 341 ? -0.764 3.386 19.297 1.00 17.14 ? 341 ASN A CG 1 ATOM 2700 O OD1 . ASN A 1 341 ? -1.055 3.053 20.414 1.00 18.19 ? 341 ASN A OD1 1 ATOM 2701 N ND2 . ASN A 1 341 ? -1.255 4.504 18.724 1.00 17.31 ? 341 ASN A ND2 1 ATOM 2702 N N . VAL A 1 342 ? 0.682 -0.573 19.289 1.00 15.85 ? 342 VAL A N 1 ATOM 2703 C CA . VAL A 1 342 ? 0.306 -1.807 19.943 1.00 15.40 ? 342 VAL A CA 1 ATOM 2704 C C . VAL A 1 342 ? 1.282 -2.340 21.030 1.00 15.79 ? 342 VAL A C 1 ATOM 2705 O O . VAL A 1 342 ? 0.841 -2.926 22.063 1.00 14.08 ? 342 VAL A O 1 ATOM 2706 C CB . VAL A 1 342 ? -0.092 -2.923 18.944 1.00 15.95 ? 342 VAL A CB 1 ATOM 2707 C CG1 . VAL A 1 342 ? 1.087 -3.424 18.163 1.00 14.58 ? 342 VAL A CG1 1 ATOM 2708 C CG2 . VAL A 1 342 ? -0.770 -4.044 19.723 1.00 16.60 ? 342 VAL A CG2 1 ATOM 2709 N N . PHE A 1 343 ? 2.563 -2.139 20.812 1.00 14.92 ? 343 PHE A N 1 ATOM 2710 C CA . PHE A 1 343 ? 3.563 -2.572 21.741 1.00 15.39 ? 343 PHE A CA 1 ATOM 2711 C C . PHE A 1 343 ? 3.394 -1.861 23.111 1.00 15.55 ? 343 PHE A C 1 ATOM 2712 O O . PHE A 1 343 ? 3.721 -2.442 24.175 1.00 16.37 ? 343 PHE A O 1 ATOM 2713 C CB . PHE A 1 343 ? 4.944 -2.309 21.188 1.00 13.95 ? 343 PHE A CB 1 ATOM 2714 C CG . PHE A 1 343 ? 6.032 -2.631 22.131 1.00 13.59 ? 343 PHE A CG 1 ATOM 2715 C CD1 . PHE A 1 343 ? 6.508 -1.658 23.001 1.00 12.85 ? 343 PHE A CD1 1 ATOM 2716 C CD2 . PHE A 1 343 ? 6.620 -3.887 22.131 1.00 12.89 ? 343 PHE A CD2 1 ATOM 2717 C CE1 . PHE A 1 343 ? 7.559 -1.925 23.856 1.00 13.44 ? 343 PHE A CE1 1 ATOM 2718 C CE2 . PHE A 1 343 ? 7.617 -4.184 23.041 1.00 13.51 ? 343 PHE A CE2 1 ATOM 2719 C CZ . PHE A 1 343 ? 8.089 -3.202 23.896 1.00 14.56 ? 343 PHE A CZ 1 ATOM 2720 N N . THR A 1 344 ? 3.002 -0.599 23.082 1.00 15.93 ? 344 THR A N 1 ATOM 2721 C CA . THR A 1 344 ? 2.765 0.099 24.339 1.00 15.03 ? 344 THR A CA 1 ATOM 2722 C C . THR A 1 344 ? 1.613 -0.539 25.166 1.00 16.70 ? 344 THR A C 1 ATOM 2723 O O . THR A 1 344 ? 1.562 -0.335 26.355 1.00 14.66 ? 344 THR A O 1 ATOM 2724 C CB . THR A 1 344 ? 2.492 1.582 24.158 1.00 16.69 ? 344 THR A CB 1 ATOM 2725 O OG1 . THR A 1 344 ? 1.131 1.794 23.782 1.00 13.58 ? 344 THR A OG1 1 ATOM 2726 C CG2 . THR A 1 344 ? 3.504 2.197 23.163 1.00 14.87 ? 344 THR A CG2 1 ATOM 2727 N N . PHE A 1 345 ? 0.714 -1.326 24.541 1.00 13.97 ? 345 PHE A N 1 ATOM 2728 C CA . PHE A 1 345 ? -0.276 -2.134 25.266 1.00 13.16 ? 345 PHE A CA 1 ATOM 2729 C C . PHE A 1 345 ? 0.257 -3.536 25.560 1.00 14.05 ? 345 PHE A C 1 ATOM 2730 O O . PHE A 1 345 ? 0.027 -4.088 26.679 1.00 15.05 ? 345 PHE A O 1 ATOM 2731 C CB . PHE A 1 345 ? -1.615 -2.155 24.527 1.00 12.49 ? 345 PHE A CB 1 ATOM 2732 C CG . PHE A 1 345 ? -2.207 -0.787 24.408 1.00 12.77 ? 345 PHE A CG 1 ATOM 2733 C CD1 . PHE A 1 345 ? -2.744 -0.180 25.504 1.00 11.44 ? 345 PHE A CD1 1 ATOM 2734 C CD2 . PHE A 1 345 ? -2.039 -0.033 23.215 1.00 12.91 ? 345 PHE A CD2 1 ATOM 2735 C CE1 . PHE A 1 345 ? -3.176 1.130 25.441 1.00 11.59 ? 345 PHE A CE1 1 ATOM 2736 C CE2 . PHE A 1 345 ? -2.484 1.271 23.129 1.00 12.90 ? 345 PHE A CE2 1 ATOM 2737 C CZ . PHE A 1 345 ? -3.058 1.855 24.246 1.00 13.96 ? 345 PHE A CZ 1 ATOM 2738 N N . ALA A 1 346 ? 0.996 -4.121 24.600 1.00 14.26 ? 346 ALA A N 1 ATOM 2739 C CA . ALA A 1 346 ? 1.562 -5.442 24.782 1.00 14.02 ? 346 ALA A CA 1 ATOM 2740 C C . ALA A 1 346 ? 2.497 -5.534 25.949 1.00 12.64 ? 346 ALA A C 1 ATOM 2741 O O . ALA A 1 346 ? 2.471 -6.548 26.700 1.00 13.01 ? 346 ALA A O 1 ATOM 2742 C CB . ALA A 1 346 ? 2.310 -5.842 23.511 1.00 15.89 ? 346 ALA A CB 1 ATOM 2743 N N . PHE A 1 347 ? 3.316 -4.504 26.140 1.00 12.54 ? 347 PHE A N 1 ATOM 2744 C CA . PHE A 1 347 ? 4.287 -4.470 27.226 1.00 13.22 ? 347 PHE A CA 1 ATOM 2745 C C . PHE A 1 347 ? 3.668 -4.255 28.638 1.00 13.68 ? 347 PHE A C 1 ATOM 2746 O O . PHE A 1 347 ? 4.389 -4.369 29.649 1.00 13.64 ? 347 PHE A O 1 ATOM 2747 C CB . PHE A 1 347 ? 5.342 -3.421 26.964 1.00 14.28 ? 347 PHE A CB 1 ATOM 2748 C CG . PHE A 1 347 ? 6.686 -3.664 27.592 1.00 15.01 ? 347 PHE A CG 1 ATOM 2749 C CD1 . PHE A 1 347 ? 6.973 -4.695 28.482 1.00 15.73 ? 347 PHE A CD1 1 ATOM 2750 C CD2 . PHE A 1 347 ? 7.741 -2.808 27.231 1.00 15.58 ? 347 PHE A CD2 1 ATOM 2751 C CE1 . PHE A 1 347 ? 8.275 -4.885 28.991 1.00 14.20 ? 347 PHE A CE1 1 ATOM 2752 C CE2 . PHE A 1 347 ? 9.030 -2.942 27.734 1.00 13.98 ? 347 PHE A CE2 1 ATOM 2753 C CZ . PHE A 1 347 ? 9.312 -3.999 28.626 1.00 15.05 ? 347 PHE A CZ 1 ATOM 2754 N N . ARG A 1 348 ? 2.389 -3.981 28.694 1.00 13.85 ? 348 ARG A N 1 ATOM 2755 C CA . ARG A 1 348 ? 1.625 -3.920 29.974 1.00 14.42 ? 348 ARG A CA 1 ATOM 2756 C C . ARG A 1 348 ? 1.227 -5.261 30.535 1.00 15.34 ? 348 ARG A C 1 ATOM 2757 O O . ARG A 1 348 ? 0.474 -5.348 31.551 1.00 15.65 ? 348 ARG A O 1 ATOM 2758 C CB . ARG A 1 348 ? 0.376 -3.059 29.824 1.00 15.22 ? 348 ARG A CB 1 ATOM 2759 C CG . ARG A 1 348 ? 0.672 -1.647 29.289 1.00 16.58 ? 348 ARG A CG 1 ATOM 2760 C CD . ARG A 1 348 ? -0.588 -0.853 29.139 1.00 17.76 ? 348 ARG A CD 1 ATOM 2761 N NE . ARG A 1 348 ? -0.384 0.377 28.409 1.00 18.32 ? 348 ARG A NE 1 ATOM 2762 C CZ . ARG A 1 348 ? -1.083 1.496 28.541 1.00 15.80 ? 348 ARG A CZ 1 ATOM 2763 N NH1 . ARG A 1 348 ? -2.077 1.622 29.420 1.00 16.55 ? 348 ARG A NH1 1 ATOM 2764 N NH2 . ARG A 1 348 ? -0.734 2.534 27.794 1.00 14.49 ? 348 ARG A NH2 1 ATOM 2765 N N . PHE A 1 349 ? 1.680 -6.333 29.888 1.00 16.22 ? 349 PHE A N 1 ATOM 2766 C CA . PHE A 1 349 ? 1.687 -7.605 30.534 1.00 15.58 ? 349 PHE A CA 1 ATOM 2767 C C . PHE A 1 349 ? 2.283 -7.505 31.960 1.00 16.09 ? 349 PHE A C 1 ATOM 2768 O O . PHE A 1 349 ? 1.909 -8.278 32.828 1.00 17.28 ? 349 PHE A O 1 ATOM 2769 C CB . PHE A 1 349 ? 2.405 -8.655 29.687 1.00 16.65 ? 349 PHE A CB 1 ATOM 2770 C CG . PHE A 1 349 ? 3.908 -8.587 29.699 1.00 17.30 ? 349 PHE A CG 1 ATOM 2771 C CD1 . PHE A 1 349 ? 4.657 -9.057 30.812 1.00 17.74 ? 349 PHE A CD1 1 ATOM 2772 C CD2 . PHE A 1 349 ? 4.593 -8.055 28.617 1.00 17.07 ? 349 PHE A CD2 1 ATOM 2773 C CE1 . PHE A 1 349 ? 6.020 -9.039 30.787 1.00 17.64 ? 349 PHE A CE1 1 ATOM 2774 C CE2 . PHE A 1 349 ? 5.962 -8.012 28.606 1.00 17.36 ? 349 PHE A CE2 1 ATOM 2775 C CZ . PHE A 1 349 ? 6.698 -8.499 29.708 1.00 17.96 ? 349 PHE A CZ 1 ATOM 2776 N N . GLY A 1 350 ? 3.197 -6.585 32.140 1.00 15.55 ? 350 GLY A N 1 ATOM 2777 C CA . GLY A 1 350 ? 3.834 -6.305 33.429 1.00 16.73 ? 350 GLY A CA 1 ATOM 2778 C C . GLY A 1 350 ? 2.838 -6.098 34.551 1.00 16.82 ? 350 GLY A C 1 ATOM 2779 O O . GLY A 1 350 ? 3.132 -6.366 35.699 1.00 14.84 ? 350 GLY A O 1 ATOM 2780 N N . HIS A 1 351 ? 1.675 -5.582 34.221 1.00 16.61 ? 351 HIS A N 1 ATOM 2781 C CA . HIS A 1 351 ? 0.700 -5.246 35.236 1.00 16.09 ? 351 HIS A CA 1 ATOM 2782 C C . HIS A 1 351 ? 0.208 -6.463 35.969 1.00 16.69 ? 351 HIS A C 1 ATOM 2783 O O . HIS A 1 351 ? -0.173 -6.350 37.094 1.00 17.32 ? 351 HIS A O 1 ATOM 2784 C CB . HIS A 1 351 ? -0.416 -4.444 34.623 1.00 16.00 ? 351 HIS A CB 1 ATOM 2785 C CG . HIS A 1 351 ? 0.050 -3.114 34.137 1.00 18.20 ? 351 HIS A CG 1 ATOM 2786 N ND1 . HIS A 1 351 ? -0.706 -2.324 33.319 1.00 19.88 ? 351 HIS A ND1 1 ATOM 2787 C CD2 . HIS A 1 351 ? 1.197 -2.433 34.356 1.00 20.35 ? 351 HIS A CD2 1 ATOM 2788 C CE1 . HIS A 1 351 ? -0.063 -1.197 33.066 1.00 18.83 ? 351 HIS A CE1 1 ATOM 2789 N NE2 . HIS A 1 351 ? 1.093 -1.222 33.703 1.00 21.31 ? 351 HIS A NE2 1 ATOM 2790 N N . MET A 1 352 ? 0.289 -7.621 35.353 1.00 16.44 ? 352 MET A N 1 ATOM 2791 C CA . MET A 1 352 ? -0.103 -8.872 35.998 1.00 18.08 ? 352 MET A CA 1 ATOM 2792 C C . MET A 1 352 ? 1.017 -9.542 36.791 1.00 16.68 ? 352 MET A C 1 ATOM 2793 O O . MET A 1 352 ? 0.789 -10.550 37.440 1.00 18.46 ? 352 MET A O 1 ATOM 2794 C CB . MET A 1 352 ? -0.696 -9.815 34.960 1.00 19.88 ? 352 MET A CB 1 ATOM 2795 C CG . MET A 1 352 ? -1.741 -9.098 34.111 1.00 22.43 ? 352 MET A CG 1 ATOM 2796 S SD . MET A 1 352 ? -2.810 -10.267 33.320 1.00 24.77 ? 352 MET A SD 1 ATOM 2797 C CE . MET A 1 352 ? -3.869 -9.041 32.554 1.00 20.30 ? 352 MET A CE 1 ATOM 2798 N N . GLU A 1 353 ? 2.215 -8.952 36.774 1.00 15.66 ? 353 GLU A N 1 ATOM 2799 C CA . GLU A 1 353 ? 3.390 -9.485 37.491 1.00 16.20 ? 353 GLU A CA 1 ATOM 2800 C C . GLU A 1 353 ? 3.686 -8.709 38.777 1.00 16.24 ? 353 GLU A C 1 ATOM 2801 O O . GLU A 1 353 ? 4.737 -8.928 39.469 1.00 16.46 ? 353 GLU A O 1 ATOM 2802 C CB . GLU A 1 353 ? 4.654 -9.401 36.581 1.00 15.27 ? 353 GLU A CB 1 ATOM 2803 C CG . GLU A 1 353 ? 4.520 -10.268 35.376 1.00 13.77 ? 353 GLU A CG 1 ATOM 2804 C CD . GLU A 1 353 ? 5.667 -10.109 34.393 1.00 15.60 ? 353 GLU A CD 1 ATOM 2805 O OE1 . GLU A 1 353 ? 6.576 -9.284 34.623 1.00 14.49 ? 353 GLU A OE1 1 ATOM 2806 O OE2 . GLU A 1 353 ? 5.666 -10.874 33.384 1.00 17.98 ? 353 GLU A OE2 1 ATOM 2807 N N . VAL A 1 354 ? 2.840 -7.741 39.073 1.00 15.91 ? 354 VAL A N 1 ATOM 2808 C CA . VAL A 1 354 ? 3.056 -6.868 40.213 1.00 16.58 ? 354 VAL A CA 1 ATOM 2809 C C . VAL A 1 354 ? 2.286 -7.431 41.433 1.00 15.66 ? 354 VAL A C 1 ATOM 2810 O O . VAL A 1 354 ? 1.091 -7.512 41.390 1.00 17.39 ? 354 VAL A O 1 ATOM 2811 C CB . VAL A 1 354 ? 2.528 -5.441 39.916 1.00 16.82 ? 354 VAL A CB 1 ATOM 2812 C CG1 . VAL A 1 354 ? 2.645 -4.587 41.168 1.00 17.66 ? 354 VAL A CG1 1 ATOM 2813 C CG2 . VAL A 1 354 ? 3.266 -4.775 38.755 1.00 15.71 ? 354 VAL A CG2 1 ATOM 2814 N N . PRO A 1 355 ? 2.998 -7.775 42.545 1.00 17.73 ? 355 PRO A N 1 ATOM 2815 C CA . PRO A 1 355 ? 2.340 -8.355 43.692 1.00 16.98 ? 355 PRO A CA 1 ATOM 2816 C C . PRO A 1 355 ? 1.768 -7.289 44.622 1.00 16.46 ? 355 PRO A C 1 ATOM 2817 O O . PRO A 1 355 ? 1.994 -6.106 44.416 1.00 16.99 ? 355 PRO A O 1 ATOM 2818 C CB . PRO A 1 355 ? 3.482 -9.158 44.331 1.00 16.42 ? 355 PRO A CB 1 ATOM 2819 C CG . PRO A 1 355 ? 4.647 -8.300 44.092 1.00 16.75 ? 355 PRO A CG 1 ATOM 2820 C CD . PRO A 1 355 ? 4.432 -7.617 42.790 1.00 16.46 ? 355 PRO A CD 1 ATOM 2821 N N . SER A 1 356 ? 1.100 -7.706 45.703 1.00 17.47 ? 356 SER A N 1 ATOM 2822 C CA . SER A 1 356 ? 0.291 -6.790 46.498 1.00 17.23 ? 356 SER A CA 1 ATOM 2823 C C . SER A 1 356 ? 1.055 -6.026 47.525 1.00 18.55 ? 356 SER A C 1 ATOM 2824 O O . SER A 1 356 ? 0.542 -5.043 48.034 1.00 16.71 ? 356 SER A O 1 ATOM 2825 C CB . SER A 1 356 ? -0.853 -7.573 47.205 1.00 18.69 ? 356 SER A CB 1 ATOM 2826 O OG . SER A 1 356 ? -0.289 -8.497 48.120 1.00 18.54 ? 356 SER A OG 1 ATOM 2827 N N . THR A 1 357 ? 2.283 -6.467 47.828 1.00 17.35 ? 357 THR A N 1 ATOM 2828 C CA . THR A 1 357 ? 3.100 -5.847 48.837 1.00 18.87 ? 357 THR A CA 1 ATOM 2829 C C . THR A 1 357 ? 4.523 -5.630 48.367 1.00 17.96 ? 357 THR A C 1 ATOM 2830 O O . THR A 1 357 ? 4.986 -6.278 47.438 1.00 19.01 ? 357 THR A O 1 ATOM 2831 C CB . THR A 1 357 ? 3.175 -6.677 50.162 1.00 20.19 ? 357 THR A CB 1 ATOM 2832 O OG1 . THR A 1 357 ? 4.007 -7.831 49.976 1.00 20.92 ? 357 THR A OG1 1 ATOM 2833 C CG2 . THR A 1 357 ? 1.755 -7.147 50.572 1.00 19.75 ? 357 THR A CG2 1 ATOM 2834 N N . VAL A 1 358 ? 5.228 -4.731 49.067 1.00 18.16 ? 358 VAL A N 1 ATOM 2835 C CA . VAL A 1 358 ? 6.673 -4.490 48.928 1.00 17.48 ? 358 VAL A CA 1 ATOM 2836 C C . VAL A 1 358 ? 7.339 -4.537 50.339 1.00 20.00 ? 358 VAL A C 1 ATOM 2837 O O . VAL A 1 358 ? 6.780 -3.968 51.315 1.00 19.15 ? 358 VAL A O 1 ATOM 2838 C CB . VAL A 1 358 ? 6.929 -3.082 48.358 1.00 17.54 ? 358 VAL A CB 1 ATOM 2839 C CG1 . VAL A 1 358 ? 8.361 -2.669 48.523 1.00 18.35 ? 358 VAL A CG1 1 ATOM 2840 C CG2 . VAL A 1 358 ? 6.488 -3.010 46.899 1.00 19.25 ? 358 VAL A CG2 1 ATOM 2841 N N . SER A 1 359 ? 8.526 -5.152 50.446 1.00 17.26 ? 359 SER A N 1 ATOM 2842 C CA . SER A 1 359 ? 9.156 -5.346 51.759 1.00 16.58 ? 359 SER A CA 1 ATOM 2843 C C . SER A 1 359 ? 10.452 -4.619 51.833 1.00 18.01 ? 359 SER A C 1 ATOM 2844 O O . SER A 1 359 ? 11.176 -4.481 50.841 1.00 20.77 ? 359 SER A O 1 ATOM 2845 C CB . SER A 1 359 ? 9.414 -6.815 52.072 1.00 16.16 ? 359 SER A CB 1 ATOM 2846 O OG . SER A 1 359 ? 8.231 -7.538 52.334 1.00 13.94 ? 359 SER A OG 1 ATOM 2847 N N . ARG A 1 360 ? 10.753 -4.150 53.038 1.00 18.93 ? 360 ARG A N 1 ATOM 2848 C CA . ARG A 1 360 ? 12.096 -3.691 53.392 1.00 20.28 ? 360 ARG A CA 1 ATOM 2849 C C . ARG A 1 360 ? 12.736 -4.830 54.220 1.00 21.63 ? 360 ARG A C 1 ATOM 2850 O O . ARG A 1 360 ? 12.099 -5.368 55.146 1.00 22.14 ? 360 ARG A O 1 ATOM 2851 C CB . ARG A 1 360 ? 12.009 -2.405 54.193 1.00 19.64 ? 360 ARG A CB 1 ATOM 2852 C CG . ARG A 1 360 ? 11.506 -1.199 53.382 1.00 21.70 ? 360 ARG A CG 1 ATOM 2853 C CD . ARG A 1 360 ? 9.982 -1.103 53.345 1.00 21.03 ? 360 ARG A CD 1 ATOM 2854 N NE . ARG A 1 360 ? 9.486 -0.775 54.683 1.00 22.42 ? 360 ARG A NE 1 ATOM 2855 C CZ . ARG A 1 360 ? 9.589 0.429 55.272 1.00 23.55 ? 360 ARG A CZ 1 ATOM 2856 N NH1 . ARG A 1 360 ? 10.133 1.458 54.656 1.00 22.02 ? 360 ARG A NH1 1 ATOM 2857 N NH2 . ARG A 1 360 ? 9.151 0.599 56.539 1.00 26.33 ? 360 ARG A NH2 1 ATOM 2858 N N . LEU A 1 361 ? 13.960 -5.222 53.862 1.00 21.92 ? 361 LEU A N 1 ATOM 2859 C CA . LEU A 1 361 ? 14.660 -6.340 54.455 1.00 21.15 ? 361 LEU A CA 1 ATOM 2860 C C . LEU A 1 361 ? 15.988 -5.841 55.016 1.00 20.32 ? 361 LEU A C 1 ATOM 2861 O O . LEU A 1 361 ? 16.590 -4.937 54.446 1.00 21.37 ? 361 LEU A O 1 ATOM 2862 C CB . LEU A 1 361 ? 14.892 -7.444 53.435 1.00 21.46 ? 361 LEU A CB 1 ATOM 2863 C CG . LEU A 1 361 ? 13.635 -8.077 52.803 1.00 21.44 ? 361 LEU A CG 1 ATOM 2864 C CD1 . LEU A 1 361 ? 14.054 -9.193 51.892 1.00 21.46 ? 361 LEU A CD1 1 ATOM 2865 C CD2 . LEU A 1 361 ? 12.675 -8.569 53.861 1.00 22.12 ? 361 LEU A CD2 1 ATOM 2866 N N . ASP A 1 362 ? 16.403 -6.345 56.186 1.00 23.88 ? 362 ASP A N 1 ATOM 2867 C CA . ASP A 1 362 ? 17.647 -5.851 56.799 1.00 24.61 ? 362 ASP A CA 1 ATOM 2868 C C . ASP A 1 362 ? 18.801 -6.644 56.219 1.00 28.73 ? 362 ASP A C 1 ATOM 2869 O O . ASP A 1 362 ? 18.614 -7.460 55.300 1.00 23.86 ? 362 ASP A O 1 ATOM 2870 C CB . ASP A 1 362 ? 17.651 -5.906 58.349 1.00 27.29 ? 362 ASP A CB 1 ATOM 2871 C CG . ASP A 1 362 ? 17.598 -7.312 58.893 1.00 33.08 ? 362 ASP A CG 1 ATOM 2872 O OD1 . ASP A 1 362 ? 17.877 -8.291 58.134 1.00 31.00 ? 362 ASP A OD1 1 ATOM 2873 O OD2 . ASP A 1 362 ? 17.169 -7.428 60.070 1.00 34.60 ? 362 ASP A OD2 1 ATOM 2874 N N . GLU A 1 363 ? 19.989 -6.426 56.786 1.00 29.82 ? 363 GLU A N 1 ATOM 2875 C CA . GLU A 1 363 ? 21.165 -7.070 56.278 1.00 34.53 ? 363 GLU A CA 1 ATOM 2876 C C . GLU A 1 363 ? 21.242 -8.554 56.519 1.00 31.45 ? 363 GLU A C 1 ATOM 2877 O O . GLU A 1 363 ? 22.086 -9.160 55.937 1.00 31.07 ? 363 GLU A O 1 ATOM 2878 C CB . GLU A 1 363 ? 22.507 -6.350 56.553 1.00 34.99 ? 363 GLU A CB 1 ATOM 2879 C CG . GLU A 1 363 ? 22.684 -5.616 57.845 1.00 39.03 ? 363 GLU A CG 1 ATOM 2880 C CD . GLU A 1 363 ? 21.893 -4.334 58.012 1.00 35.47 ? 363 GLU A CD 1 ATOM 2881 O OE1 . GLU A 1 363 ? 22.418 -3.197 57.855 1.00 31.05 ? 363 GLU A OE1 1 ATOM 2882 O OE2 . GLU A 1 363 ? 20.725 -4.513 58.393 1.00 37.52 ? 363 GLU A OE2 1 ATOM 2883 N N . ASN A 1 364 ? 20.320 -9.163 57.248 1.00 29.08 ? 364 ASN A N 1 ATOM 2884 C CA . ASN A 1 364 ? 20.218 -10.597 57.169 1.00 28.69 ? 364 ASN A CA 1 ATOM 2885 C C . ASN A 1 364 ? 19.069 -11.024 56.317 1.00 29.12 ? 364 ASN A C 1 ATOM 2886 O O . ASN A 1 364 ? 18.676 -12.171 56.393 1.00 29.01 ? 364 ASN A O 1 ATOM 2887 C CB . ASN A 1 364 ? 20.071 -11.193 58.554 1.00 31.30 ? 364 ASN A CB 1 ATOM 2888 C CG . ASN A 1 364 ? 21.266 -10.891 59.414 1.00 31.44 ? 364 ASN A CG 1 ATOM 2889 O OD1 . ASN A 1 364 ? 22.424 -10.991 58.993 1.00 33.12 ? 364 ASN A OD1 1 ATOM 2890 N ND2 . ASN A 1 364 ? 20.991 -10.458 60.597 1.00 32.95 ? 364 ASN A ND2 1 ATOM 2891 N N . TYR A 1 365 ? 18.546 -10.105 55.492 1.00 27.49 ? 365 TYR A N 1 ATOM 2892 C CA . TYR A 1 365 ? 17.357 -10.345 54.688 1.00 26.98 ? 365 TYR A CA 1 ATOM 2893 C C . TYR A 1 365 ? 16.127 -10.764 55.515 1.00 29.79 ? 365 TYR A C 1 ATOM 2894 O O . TYR A 1 365 ? 15.258 -11.513 55.042 1.00 28.52 ? 365 TYR A O 1 ATOM 2895 C CB . TYR A 1 365 ? 17.670 -11.339 53.561 1.00 27.34 ? 365 TYR A CB 1 ATOM 2896 C CG . TYR A 1 365 ? 18.514 -10.710 52.457 1.00 29.52 ? 365 TYR A CG 1 ATOM 2897 C CD1 . TYR A 1 365 ? 19.844 -10.418 52.646 1.00 29.25 ? 365 TYR A CD1 1 ATOM 2898 C CD2 . TYR A 1 365 ? 17.944 -10.370 51.239 1.00 32.07 ? 365 TYR A CD2 1 ATOM 2899 C CE1 . TYR A 1 365 ? 20.613 -9.835 51.656 1.00 31.66 ? 365 TYR A CE1 1 ATOM 2900 C CE2 . TYR A 1 365 ? 18.692 -9.786 50.254 1.00 29.53 ? 365 TYR A CE2 1 ATOM 2901 C CZ . TYR A 1 365 ? 20.031 -9.517 50.445 1.00 32.95 ? 365 TYR A CZ 1 ATOM 2902 O OH . TYR A 1 365 ? 20.792 -8.933 49.410 1.00 27.43 ? 365 TYR A OH 1 ATOM 2903 N N . GLN A 1 366 ? 16.024 -10.234 56.731 1.00 29.02 ? 366 GLN A N 1 ATOM 2904 C CA . GLN A 1 366 ? 14.866 -10.438 57.553 1.00 30.09 ? 366 GLN A CA 1 ATOM 2905 C C . GLN A 1 366 ? 14.070 -9.124 57.497 1.00 30.46 ? 366 GLN A C 1 ATOM 2906 O O . GLN A 1 366 ? 14.634 -8.082 57.182 1.00 26.61 ? 366 GLN A O 1 ATOM 2907 C CB . GLN A 1 366 ? 15.271 -10.711 58.997 1.00 31.09 ? 366 GLN A CB 1 ATOM 2908 C CG . GLN A 1 366 ? 16.073 -11.962 59.197 1.00 35.81 ? 366 GLN A CG 1 ATOM 2909 C CD . GLN A 1 366 ? 15.287 -13.190 58.804 1.00 41.20 ? 366 GLN A CD 1 ATOM 2910 O OE1 . GLN A 1 366 ? 14.128 -13.353 59.193 1.00 44.14 ? 366 GLN A OE1 1 ATOM 2911 N NE2 . GLN A 1 366 ? 15.892 -14.048 57.990 1.00 47.82 ? 366 GLN A NE2 1 ATOM 2912 N N . PRO A 1 367 ? 12.772 -9.173 57.845 1.00 32.07 ? 367 PRO A N 1 ATOM 2913 C CA . PRO A 1 367 ? 11.960 -7.958 57.904 1.00 30.85 ? 367 PRO A CA 1 ATOM 2914 C C . PRO A 1 367 ? 12.622 -6.838 58.689 1.00 32.69 ? 367 PRO A C 1 ATOM 2915 O O . PRO A 1 367 ? 13.158 -7.047 59.771 1.00 35.00 ? 367 PRO A O 1 ATOM 2916 C CB . PRO A 1 367 ? 10.725 -8.404 58.631 1.00 33.00 ? 367 PRO A CB 1 ATOM 2917 C CG . PRO A 1 367 ? 10.599 -9.834 58.305 1.00 31.78 ? 367 PRO A CG 1 ATOM 2918 C CD . PRO A 1 367 ? 12.011 -10.356 58.267 1.00 30.61 ? 367 PRO A CD 1 ATOM 2919 N N . TRP A 1 368 ? 12.608 -5.661 58.097 1.00 29.25 ? 368 TRP A N 1 ATOM 2920 C CA . TRP A 1 368 ? 13.336 -4.536 58.573 1.00 29.19 ? 368 TRP A CA 1 ATOM 2921 C C . TRP A 1 368 ? 12.335 -3.660 59.268 1.00 29.90 ? 368 TRP A C 1 ATOM 2922 O O . TRP A 1 368 ? 11.551 -2.961 58.622 1.00 25.33 ? 368 TRP A O 1 ATOM 2923 C CB . TRP A 1 368 ? 13.964 -3.794 57.394 1.00 30.13 ? 368 TRP A CB 1 ATOM 2924 C CG . TRP A 1 368 ? 14.723 -2.610 57.768 1.00 30.60 ? 368 TRP A CG 1 ATOM 2925 C CD1 . TRP A 1 368 ? 15.989 -2.581 58.266 1.00 30.18 ? 368 TRP A CD1 1 ATOM 2926 C CD2 . TRP A 1 368 ? 14.281 -1.257 57.715 1.00 28.63 ? 368 TRP A CD2 1 ATOM 2927 N NE1 . TRP A 1 368 ? 16.366 -1.290 58.499 1.00 30.21 ? 368 TRP A NE1 1 ATOM 2928 C CE2 . TRP A 1 368 ? 15.332 -0.457 58.187 1.00 28.92 ? 368 TRP A CE2 1 ATOM 2929 C CE3 . TRP A 1 368 ? 13.112 -0.644 57.317 1.00 27.23 ? 368 TRP A CE3 1 ATOM 2930 C CZ2 . TRP A 1 368 ? 15.235 0.925 58.275 1.00 28.35 ? 368 TRP A CZ2 1 ATOM 2931 C CZ3 . TRP A 1 368 ? 13.029 0.729 57.396 1.00 26.67 ? 368 TRP A CZ3 1 ATOM 2932 C CH2 . TRP A 1 368 ? 14.065 1.492 57.865 1.00 25.33 ? 368 TRP A CH2 1 ATOM 2933 N N . GLY A 1 369 ? 12.327 -3.756 60.599 1.00 32.87 ? 369 GLY A N 1 ATOM 2934 C CA . GLY A 1 369 ? 11.410 -2.981 61.432 1.00 29.88 ? 369 GLY A CA 1 ATOM 2935 C C . GLY A 1 369 ? 10.004 -3.511 61.671 1.00 27.81 ? 369 GLY A C 1 ATOM 2936 O O . GLY A 1 369 ? 9.591 -4.590 61.197 1.00 30.83 ? 369 GLY A O 1 ATOM 2937 N N . PRO A 1 370 ? 9.226 -2.717 62.406 1.00 27.45 ? 370 PRO A N 1 ATOM 2938 C CA . PRO A 1 370 ? 7.870 -3.096 62.681 1.00 27.76 ? 370 PRO A CA 1 ATOM 2939 C C . PRO A 1 370 ? 6.938 -2.855 61.476 1.00 29.97 ? 370 PRO A C 1 ATOM 2940 O O . PRO A 1 370 ? 5.876 -3.448 61.443 1.00 30.78 ? 370 PRO A O 1 ATOM 2941 C CB . PRO A 1 370 ? 7.484 -2.176 63.829 1.00 25.84 ? 370 PRO A CB 1 ATOM 2942 C CG . PRO A 1 370 ? 8.310 -0.944 63.622 1.00 26.57 ? 370 PRO A CG 1 ATOM 2943 C CD . PRO A 1 370 ? 9.479 -1.298 62.736 1.00 25.09 ? 370 PRO A CD 1 ATOM 2944 N N . GLU A 1 371 ? 7.328 -2.003 60.512 1.00 28.30 ? 371 GLU A N 1 ATOM 2945 C CA . GLU A 1 371 ? 6.512 -1.781 59.279 1.00 27.30 ? 371 GLU A CA 1 ATOM 2946 C C . GLU A 1 371 ? 7.265 -2.337 58.059 1.00 25.41 ? 371 GLU A C 1 ATOM 2947 O O . GLU A 1 371 ? 7.534 -1.630 57.094 1.00 29.28 ? 371 GLU A O 1 ATOM 2948 C CB . GLU A 1 371 ? 6.294 -0.267 59.120 1.00 24.88 ? 371 GLU A CB 1 ATOM 2949 C CG . GLU A 1 371 ? 5.387 0.308 60.201 1.00 27.93 ? 371 GLU A CG 1 ATOM 2950 C CD . GLU A 1 371 ? 5.437 1.798 60.279 1.00 30.18 ? 371 GLU A CD 1 ATOM 2951 O OE1 . GLU A 1 371 ? 4.995 2.324 61.298 1.00 31.67 ? 371 GLU A OE1 1 ATOM 2952 O OE2 . GLU A 1 371 ? 5.975 2.467 59.368 1.00 37.19 ? 371 GLU A OE2 1 ATOM 2953 N N . ALA A 1 372 ? 7.661 -3.595 58.135 1.00 25.85 ? 372 ALA A N 1 ATOM 2954 C CA . ALA A 1 372 ? 8.644 -4.099 57.193 1.00 25.50 ? 372 ALA A CA 1 ATOM 2955 C C . ALA A 1 372 ? 7.926 -4.239 55.833 1.00 24.66 ? 372 ALA A C 1 ATOM 2956 O O . ALA A 1 372 ? 8.449 -3.806 54.812 1.00 22.22 ? 372 ALA A O 1 ATOM 2957 C CB . ALA A 1 372 ? 9.203 -5.446 57.623 1.00 24.01 ? 372 ALA A CB 1 ATOM 2958 N N . GLU A 1 373 ? 6.780 -4.931 55.873 1.00 24.19 ? 373 GLU A N 1 ATOM 2959 C CA . GLU A 1 373 ? 5.956 -5.185 54.704 1.00 23.46 ? 373 GLU A CA 1 ATOM 2960 C C . GLU A 1 373 ? 4.835 -4.142 54.520 1.00 23.33 ? 373 GLU A C 1 ATOM 2961 O O . GLU A 1 373 ? 3.900 -4.032 55.336 1.00 20.51 ? 373 GLU A O 1 ATOM 2962 C CB . GLU A 1 373 ? 5.348 -6.551 54.761 1.00 23.68 ? 373 GLU A CB 1 ATOM 2963 C CG . GLU A 1 373 ? 4.721 -6.954 53.464 1.00 28.49 ? 373 GLU A CG 1 ATOM 2964 C CD . GLU A 1 373 ? 4.033 -8.307 53.543 1.00 30.69 ? 373 GLU A CD 1 ATOM 2965 O OE1 . GLU A 1 373 ? 4.639 -9.306 53.205 1.00 36.08 ? 373 GLU A OE1 1 ATOM 2966 O OE2 . GLU A 1 373 ? 2.872 -8.365 53.965 1.00 34.03 ? 373 GLU A OE2 1 ATOM 2967 N N . LEU A 1 374 ? 4.892 -3.475 53.365 1.00 20.04 ? 374 LEU A N 1 ATOM 2968 C CA . LEU A 1 374 ? 3.992 -2.386 53.008 1.00 19.01 ? 374 LEU A CA 1 ATOM 2969 C C . LEU A 1 374 ? 3.030 -2.813 51.863 1.00 19.26 ? 374 LEU A C 1 ATOM 2970 O O . LEU A 1 374 ? 3.447 -3.484 50.902 1.00 20.50 ? 374 LEU A O 1 ATOM 2971 C CB . LEU A 1 374 ? 4.805 -1.147 52.649 1.00 17.27 ? 374 LEU A CB 1 ATOM 2972 C CG . LEU A 1 374 ? 5.817 -0.651 53.712 1.00 19.20 ? 374 LEU A CG 1 ATOM 2973 C CD1 . LEU A 1 374 ? 6.590 0.523 53.127 1.00 19.92 ? 374 LEU A CD1 1 ATOM 2974 C CD2 . LEU A 1 374 ? 5.189 -0.202 55.022 1.00 18.90 ? 374 LEU A CD2 1 ATOM 2975 N N . PRO A 1 375 ? 1.746 -2.439 51.988 1.00 17.44 ? 375 PRO A N 1 ATOM 2976 C CA . PRO A 1 375 ? 0.839 -2.585 50.854 1.00 17.85 ? 375 PRO A CA 1 ATOM 2977 C C . PRO A 1 375 ? 1.289 -1.690 49.697 1.00 16.23 ? 375 PRO A C 1 ATOM 2978 O O . PRO A 1 375 ? 1.584 -0.514 49.865 1.00 14.98 ? 375 PRO A O 1 ATOM 2979 C CB . PRO A 1 375 ? -0.529 -2.183 51.403 1.00 18.55 ? 375 PRO A CB 1 ATOM 2980 C CG . PRO A 1 375 ? -0.332 -1.896 52.863 1.00 18.43 ? 375 PRO A CG 1 ATOM 2981 C CD . PRO A 1 375 ? 1.148 -1.663 53.092 1.00 18.74 ? 375 PRO A CD 1 ATOM 2982 N N . LEU A 1 376 ? 1.322 -2.281 48.517 1.00 18.43 ? 376 LEU A N 1 ATOM 2983 C CA . LEU A 1 376 ? 1.679 -1.546 47.284 1.00 18.57 ? 376 LEU A CA 1 ATOM 2984 C C . LEU A 1 376 ? 0.979 -0.213 47.129 1.00 16.64 ? 376 LEU A C 1 ATOM 2985 O O . LEU A 1 376 ? 1.623 0.805 46.759 1.00 17.89 ? 376 LEU A O 1 ATOM 2986 C CB . LEU A 1 376 ? 1.368 -2.418 46.082 1.00 19.34 ? 376 LEU A CB 1 ATOM 2987 C CG . LEU A 1 376 ? 1.709 -1.701 44.746 1.00 21.59 ? 376 LEU A CG 1 ATOM 2988 C CD1 . LEU A 1 376 ? 3.175 -1.465 44.618 1.00 20.63 ? 376 LEU A CD1 1 ATOM 2989 C CD2 . LEU A 1 376 ? 1.164 -2.494 43.540 1.00 22.99 ? 376 LEU A CD2 1 ATOM 2990 N N . HIS A 1 377 ? -0.296 -0.131 47.527 1.00 15.47 ? 377 HIS A N 1 ATOM 2991 C CA . HIS A 1 377 ? -1.070 1.056 47.205 1.00 15.66 ? 377 HIS A CA 1 ATOM 2992 C C . HIS A 1 377 ? -0.571 2.215 47.940 1.00 14.76 ? 377 HIS A C 1 ATOM 2993 O O . HIS A 1 377 ? -0.826 3.334 47.536 1.00 16.24 ? 377 HIS A O 1 ATOM 2994 C CB . HIS A 1 377 ? -2.615 0.899 47.336 1.00 18.41 ? 377 HIS A CB 1 ATOM 2995 C CG . HIS A 1 377 ? -3.121 0.956 48.739 1.00 18.44 ? 377 HIS A CG 1 ATOM 2996 N ND1 . HIS A 1 377 ? -3.121 -0.138 49.581 1.00 20.53 ? 377 HIS A ND1 1 ATOM 2997 C CD2 . HIS A 1 377 ? -3.619 1.985 49.450 1.00 22.28 ? 377 HIS A CD2 1 ATOM 2998 C CE1 . HIS A 1 377 ? -3.583 0.230 50.765 1.00 22.12 ? 377 HIS A CE1 1 ATOM 2999 N NE2 . HIS A 1 377 ? -3.905 1.509 50.702 1.00 23.25 ? 377 HIS A NE2 1 ATOM 3000 N N . THR A 1 378 ? 0.148 2.000 49.035 1.00 14.15 ? 378 THR A N 1 ATOM 3001 C CA . THR A 1 378 ? 0.622 3.127 49.807 1.00 15.26 ? 378 THR A CA 1 ATOM 3002 C C . THR A 1 378 ? 1.923 3.654 49.234 1.00 15.66 ? 378 THR A C 1 ATOM 3003 O O . THR A 1 378 ? 2.506 4.553 49.774 1.00 18.48 ? 378 THR A O 1 ATOM 3004 C CB . THR A 1 378 ? 0.882 2.769 51.317 1.00 15.59 ? 378 THR A CB 1 ATOM 3005 O OG1 . THR A 1 378 ? 1.958 1.832 51.425 1.00 12.91 ? 378 THR A OG1 1 ATOM 3006 C CG2 . THR A 1 378 ? -0.384 2.130 51.994 1.00 14.89 ? 378 THR A CG2 1 ATOM 3007 N N . LEU A 1 379 ? 2.417 3.051 48.180 1.00 16.76 ? 379 LEU A N 1 ATOM 3008 C CA . LEU A 1 379 ? 3.747 3.356 47.688 1.00 15.68 ? 379 LEU A CA 1 ATOM 3009 C C . LEU A 1 379 ? 3.711 4.145 46.359 1.00 16.18 ? 379 LEU A C 1 ATOM 3010 O O . LEU A 1 379 ? 4.771 4.476 45.818 1.00 15.29 ? 379 LEU A O 1 ATOM 3011 C CB . LEU A 1 379 ? 4.464 2.055 47.515 1.00 17.03 ? 379 LEU A CB 1 ATOM 3012 C CG . LEU A 1 379 ? 4.688 1.366 48.868 1.00 17.52 ? 379 LEU A CG 1 ATOM 3013 C CD1 . LEU A 1 379 ? 5.221 0.009 48.624 1.00 18.45 ? 379 LEU A CD1 1 ATOM 3014 C CD2 . LEU A 1 379 ? 5.590 2.176 49.760 1.00 17.94 ? 379 LEU A CD2 1 ATOM 3015 N N . PHE A 1 380 ? 2.513 4.397 45.846 1.00 14.91 ? 380 PHE A N 1 ATOM 3016 C CA . PHE A 1 380 ? 2.372 5.186 44.614 1.00 15.83 ? 380 PHE A CA 1 ATOM 3017 C C . PHE A 1 380 ? 2.716 6.644 44.872 1.00 15.89 ? 380 PHE A C 1 ATOM 3018 O O . PHE A 1 380 ? 2.275 7.230 45.878 1.00 15.29 ? 380 PHE A O 1 ATOM 3019 C CB . PHE A 1 380 ? 0.929 5.122 44.041 1.00 15.18 ? 380 PHE A CB 1 ATOM 3020 C CG . PHE A 1 380 ? 0.441 3.759 43.757 1.00 14.22 ? 380 PHE A CG 1 ATOM 3021 C CD1 . PHE A 1 380 ? 1.196 2.853 43.038 1.00 14.36 ? 380 PHE A CD1 1 ATOM 3022 C CD2 . PHE A 1 380 ? -0.843 3.365 44.158 1.00 15.52 ? 380 PHE A CD2 1 ATOM 3023 C CE1 . PHE A 1 380 ? 0.719 1.554 42.794 1.00 14.29 ? 380 PHE A CE1 1 ATOM 3024 C CE2 . PHE A 1 380 ? -1.321 2.078 43.913 1.00 14.66 ? 380 PHE A CE2 1 ATOM 3025 C CZ . PHE A 1 380 ? -0.553 1.172 43.215 1.00 14.61 ? 380 PHE A CZ 1 ATOM 3026 N N . PHE A 1 381 ? 3.643 7.197 44.079 1.00 15.20 ? 381 PHE A N 1 ATOM 3027 C CA . PHE A 1 381 ? 4.145 8.539 44.303 1.00 16.55 ? 381 PHE A CA 1 ATOM 3028 C C . PHE A 1 381 ? 4.770 8.752 45.688 1.00 18.87 ? 381 PHE A C 1 ATOM 3029 O O . PHE A 1 381 ? 4.803 9.877 46.229 1.00 20.06 ? 381 PHE A O 1 ATOM 3030 C CB . PHE A 1 381 ? 3.138 9.574 43.888 1.00 16.97 ? 381 PHE A CB 1 ATOM 3031 C CG . PHE A 1 381 ? 2.790 9.406 42.453 1.00 21.00 ? 381 PHE A CG 1 ATOM 3032 C CD1 . PHE A 1 381 ? 1.777 8.576 42.073 1.00 19.90 ? 381 PHE A CD1 1 ATOM 3033 C CD2 . PHE A 1 381 ? 3.630 9.949 41.478 1.00 22.94 ? 381 PHE A CD2 1 ATOM 3034 C CE1 . PHE A 1 381 ? 1.556 8.313 40.708 1.00 24.85 ? 381 PHE A CE1 1 ATOM 3035 C CE2 . PHE A 1 381 ? 3.388 9.758 40.113 1.00 23.58 ? 381 PHE A CE2 1 ATOM 3036 C CZ . PHE A 1 381 ? 2.345 8.933 39.737 1.00 24.32 ? 381 PHE A CZ 1 ATOM 3037 N N . ASN A 1 382 ? 5.389 7.686 46.176 1.00 17.52 ? 382 ASN A N 1 ATOM 3038 C CA . ASN A 1 382 ? 5.910 7.696 47.545 1.00 18.57 ? 382 ASN A CA 1 ATOM 3039 C C . ASN A 1 382 ? 7.439 7.725 47.486 1.00 17.34 ? 382 ASN A C 1 ATOM 3040 O O . ASN A 1 382 ? 8.114 6.699 47.173 1.00 13.24 ? 382 ASN A O 1 ATOM 3041 C CB . ASN A 1 382 ? 5.389 6.465 48.320 1.00 18.42 ? 382 ASN A CB 1 ATOM 3042 C CG . ASN A 1 382 ? 5.726 6.520 49.821 1.00 20.48 ? 382 ASN A CG 1 ATOM 3043 O OD1 . ASN A 1 382 ? 6.738 7.070 50.200 1.00 15.90 ? 382 ASN A OD1 1 ATOM 3044 N ND2 . ASN A 1 382 ? 4.809 6.040 50.659 1.00 20.10 ? 382 ASN A ND2 1 ATOM 3045 N N . THR A 1 383 ? 7.978 8.919 47.749 1.00 16.24 ? 383 THR A N 1 ATOM 3046 C CA . THR A 1 383 ? 9.381 9.094 48.030 1.00 17.16 ? 383 THR A CA 1 ATOM 3047 C C . THR A 1 383 ? 9.753 9.187 49.516 1.00 17.13 ? 383 THR A C 1 ATOM 3048 O O . THR A 1 383 ? 10.922 8.971 49.899 1.00 16.85 ? 383 THR A O 1 ATOM 3049 C CB . THR A 1 383 ? 9.950 10.313 47.288 1.00 17.90 ? 383 THR A CB 1 ATOM 3050 O OG1 . THR A 1 383 ? 9.129 11.443 47.536 1.00 20.19 ? 383 THR A OG1 1 ATOM 3051 C CG2 . THR A 1 383 ? 9.994 10.005 45.796 1.00 18.85 ? 383 THR A CG2 1 ATOM 3052 N N . TRP A 1 384 ? 8.793 9.541 50.375 1.00 19.87 ? 384 TRP A N 1 ATOM 3053 C CA . TRP A 1 384 ? 9.168 9.736 51.771 1.00 19.63 ? 384 TRP A CA 1 ATOM 3054 C C . TRP A 1 384 ? 9.565 8.448 52.426 1.00 20.31 ? 384 TRP A C 1 ATOM 3055 O O . TRP A 1 384 ? 10.418 8.451 53.343 1.00 20.31 ? 384 TRP A O 1 ATOM 3056 C CB . TRP A 1 384 ? 8.071 10.459 52.536 1.00 21.70 ? 384 TRP A CB 1 ATOM 3057 C CG . TRP A 1 384 ? 6.853 9.655 52.810 1.00 20.82 ? 384 TRP A CG 1 ATOM 3058 C CD1 . TRP A 1 384 ? 5.724 9.648 52.073 1.00 21.24 ? 384 TRP A CD1 1 ATOM 3059 C CD2 . TRP A 1 384 ? 6.615 8.799 53.932 1.00 22.67 ? 384 TRP A CD2 1 ATOM 3060 N NE1 . TRP A 1 384 ? 4.779 8.781 52.648 1.00 22.78 ? 384 TRP A NE1 1 ATOM 3061 C CE2 . TRP A 1 384 ? 5.313 8.255 53.785 1.00 21.19 ? 384 TRP A CE2 1 ATOM 3062 C CE3 . TRP A 1 384 ? 7.376 8.413 55.031 1.00 22.29 ? 384 TRP A CE3 1 ATOM 3063 C CZ2 . TRP A 1 384 ? 4.753 7.378 54.720 1.00 23.32 ? 384 TRP A CZ2 1 ATOM 3064 C CZ3 . TRP A 1 384 ? 6.819 7.530 55.948 1.00 22.87 ? 384 TRP A CZ3 1 ATOM 3065 C CH2 . TRP A 1 384 ? 5.535 7.017 55.787 1.00 23.45 ? 384 TRP A CH2 1 ATOM 3066 N N . ARG A 1 385 ? 8.956 7.332 52.025 1.00 17.37 ? 385 ARG A N 1 ATOM 3067 C CA . ARG A 1 385 ? 9.423 6.036 52.562 1.00 19.30 ? 385 ARG A CA 1 ATOM 3068 C C . ARG A 1 385 ? 10.891 5.713 52.230 1.00 21.43 ? 385 ARG A C 1 ATOM 3069 O O . ARG A 1 385 ? 11.506 4.894 52.924 1.00 23.13 ? 385 ARG A O 1 ATOM 3070 C CB . ARG A 1 385 ? 8.541 4.913 52.053 1.00 18.01 ? 385 ARG A CB 1 ATOM 3071 C CG . ARG A 1 385 ? 7.204 4.854 52.770 1.00 18.73 ? 385 ARG A CG 1 ATOM 3072 C CD . ARG A 1 385 ? 7.380 4.229 54.166 1.00 18.68 ? 385 ARG A CD 1 ATOM 3073 N NE . ARG A 1 385 ? 6.070 3.876 54.718 1.00 18.41 ? 385 ARG A NE 1 ATOM 3074 C CZ . ARG A 1 385 ? 5.836 3.477 55.951 1.00 19.87 ? 385 ARG A CZ 1 ATOM 3075 N NH1 . ARG A 1 385 ? 6.825 3.402 56.844 1.00 22.46 ? 385 ARG A NH1 1 ATOM 3076 N NH2 . ARG A 1 385 ? 4.592 3.227 56.305 1.00 21.38 ? 385 ARG A NH2 1 ATOM 3077 N N . ILE A 1 386 ? 11.407 6.298 51.137 1.00 20.75 ? 386 ILE A N 1 ATOM 3078 C CA . ILE A 1 386 ? 12.821 6.188 50.814 1.00 21.42 ? 386 ILE A CA 1 ATOM 3079 C C . ILE A 1 386 ? 13.614 7.145 51.687 1.00 22.47 ? 386 ILE A C 1 ATOM 3080 O O . ILE A 1 386 ? 14.406 6.704 52.524 1.00 25.57 ? 386 ILE A O 1 ATOM 3081 C CB . ILE A 1 386 ? 13.138 6.521 49.343 1.00 21.41 ? 386 ILE A CB 1 ATOM 3082 C CG1 . ILE A 1 386 ? 12.427 5.553 48.395 1.00 19.28 ? 386 ILE A CG1 1 ATOM 3083 C CG2 . ILE A 1 386 ? 14.657 6.457 49.134 1.00 24.30 ? 386 ILE A CG2 1 ATOM 3084 C CD1 . ILE A 1 386 ? 12.498 5.934 46.916 1.00 18.32 ? 386 ILE A CD1 1 ATOM 3085 N N . ILE A 1 387 ? 13.325 8.445 51.543 1.00 21.06 ? 387 ILE A N 1 ATOM 3086 C CA . ILE A 1 387 ? 14.113 9.487 52.142 1.00 23.63 ? 387 ILE A CA 1 ATOM 3087 C C . ILE A 1 387 ? 14.023 9.487 53.663 1.00 24.37 ? 387 ILE A C 1 ATOM 3088 O O . ILE A 1 387 ? 15.035 9.663 54.318 1.00 27.13 ? 387 ILE A O 1 ATOM 3089 C CB . ILE A 1 387 ? 13.676 10.870 51.660 1.00 23.79 ? 387 ILE A CB 1 ATOM 3090 C CG1 . ILE A 1 387 ? 13.785 10.986 50.123 1.00 26.89 ? 387 ILE A CG1 1 ATOM 3091 C CG2 . ILE A 1 387 ? 14.492 11.961 52.350 1.00 26.79 ? 387 ILE A CG2 1 ATOM 3092 C CD1 . ILE A 1 387 ? 15.154 11.195 49.577 1.00 25.85 ? 387 ILE A CD1 1 ATOM 3093 N N . LYS A 1 388 ? 12.843 9.240 54.226 1.00 23.66 ? 388 LYS A N 1 ATOM 3094 C CA . LYS A 1 388 ? 12.719 9.255 55.695 1.00 25.47 ? 388 LYS A CA 1 ATOM 3095 C C . LYS A 1 388 ? 12.677 7.923 56.361 1.00 24.89 ? 388 LYS A C 1 ATOM 3096 O O . LYS A 1 388 ? 12.567 7.879 57.576 1.00 22.24 ? 388 LYS A O 1 ATOM 3097 C CB . LYS A 1 388 ? 11.443 9.891 56.108 1.00 29.41 ? 388 LYS A CB 1 ATOM 3098 C CG . LYS A 1 388 ? 11.196 11.219 55.485 1.00 31.20 ? 388 LYS A CG 1 ATOM 3099 C CD . LYS A 1 388 ? 11.921 12.301 56.187 1.00 34.41 ? 388 LYS A CD 1 ATOM 3100 C CE . LYS A 1 388 ? 11.252 13.620 55.852 1.00 38.94 ? 388 LYS A CE 1 ATOM 3101 N NZ . LYS A 1 388 ? 12.257 14.719 55.855 1.00 41.54 ? 388 LYS A NZ 1 ATOM 3102 N N . ASP A 1 389 ? 12.747 6.840 55.609 1.00 21.09 ? 389 ASP A N 1 ATOM 3103 C CA . ASP A 1 389 ? 12.524 5.559 56.224 1.00 22.69 ? 389 ASP A CA 1 ATOM 3104 C C . ASP A 1 389 ? 13.426 4.445 55.643 1.00 21.19 ? 389 ASP A C 1 ATOM 3105 O O . ASP A 1 389 ? 12.981 3.356 55.336 1.00 21.94 ? 389 ASP A O 1 ATOM 3106 C CB . ASP A 1 389 ? 11.022 5.223 56.166 1.00 21.14 ? 389 ASP A CB 1 ATOM 3107 C CG . ASP A 1 389 ? 10.622 4.055 57.088 1.00 21.21 ? 389 ASP A CG 1 ATOM 3108 O OD1 . ASP A 1 389 ? 11.220 3.863 58.142 1.00 22.32 ? 389 ASP A OD1 1 ATOM 3109 O OD2 . ASP A 1 389 ? 9.661 3.339 56.784 1.00 20.76 ? 389 ASP A OD2 1 ATOM 3110 N N . GLY A 1 390 ? 14.717 4.714 55.601 1.00 21.43 ? 390 GLY A N 1 ATOM 3111 C CA . GLY A 1 390 ? 15.744 3.639 55.477 1.00 20.30 ? 390 GLY A CA 1 ATOM 3112 C C . GLY A 1 390 ? 16.605 3.674 54.207 1.00 20.63 ? 390 GLY A C 1 ATOM 3113 O O . GLY A 1 390 ? 17.557 2.869 54.048 1.00 22.68 ? 390 GLY A O 1 ATOM 3114 N N . GLY A 1 391 ? 16.267 4.583 53.309 1.00 21.80 ? 391 GLY A N 1 ATOM 3115 C CA . GLY A 1 391 ? 16.854 4.662 51.961 1.00 22.12 ? 391 GLY A CA 1 ATOM 3116 C C . GLY A 1 391 ? 16.621 3.447 51.117 1.00 22.25 ? 391 GLY A C 1 ATOM 3117 O O . GLY A 1 391 ? 15.731 2.628 51.424 1.00 22.02 ? 391 GLY A O 1 ATOM 3118 N N . ILE A 1 392 ? 17.437 3.258 50.078 1.00 21.15 ? 392 ILE A N 1 ATOM 3119 C CA . ILE A 1 392 ? 17.124 2.182 49.149 1.00 19.55 ? 392 ILE A CA 1 ATOM 3120 C C . ILE A 1 392 ? 17.672 0.794 49.487 1.00 19.99 ? 392 ILE A C 1 ATOM 3121 O O . ILE A 1 392 ? 17.157 -0.204 48.953 1.00 19.06 ? 392 ILE A O 1 ATOM 3122 C CB . ILE A 1 392 ? 17.460 2.519 47.699 1.00 22.23 ? 392 ILE A CB 1 ATOM 3123 C CG1 . ILE A 1 392 ? 18.963 2.474 47.410 1.00 23.89 ? 392 ILE A CG1 1 ATOM 3124 C CG2 . ILE A 1 392 ? 16.838 3.833 47.285 1.00 22.26 ? 392 ILE A CG2 1 ATOM 3125 C CD1 . ILE A 1 392 ? 19.212 2.399 45.904 1.00 24.06 ? 392 ILE A CD1 1 ATOM 3126 N N . ASP A 1 393 ? 18.651 0.674 50.397 1.00 21.14 ? 393 ASP A N 1 ATOM 3127 C CA . ASP A 1 393 ? 19.220 -0.656 50.637 1.00 21.17 ? 393 ASP A CA 1 ATOM 3128 C C . ASP A 1 393 ? 18.187 -1.679 51.024 1.00 20.98 ? 393 ASP A C 1 ATOM 3129 O O . ASP A 1 393 ? 18.210 -2.815 50.498 1.00 22.90 ? 393 ASP A O 1 ATOM 3130 C CB . ASP A 1 393 ? 20.401 -0.612 51.661 1.00 24.22 ? 393 ASP A CB 1 ATOM 3131 C CG . ASP A 1 393 ? 21.675 0.003 51.074 1.00 26.19 ? 393 ASP A CG 1 ATOM 3132 O OD1 . ASP A 1 393 ? 21.688 0.438 49.894 1.00 26.61 ? 393 ASP A OD1 1 ATOM 3133 O OD2 . ASP A 1 393 ? 22.639 0.180 51.828 1.00 32.17 ? 393 ASP A OD2 1 ATOM 3134 N N . PRO A 1 394 ? 17.249 -1.340 51.964 1.00 20.32 ? 394 PRO A N 1 ATOM 3135 C CA . PRO A 1 394 ? 16.264 -2.394 52.318 1.00 21.36 ? 394 PRO A CA 1 ATOM 3136 C C . PRO A 1 394 ? 15.295 -2.762 51.224 1.00 18.17 ? 394 PRO A C 1 ATOM 3137 O O . PRO A 1 394 ? 14.778 -3.925 51.164 1.00 19.46 ? 394 PRO A O 1 ATOM 3138 C CB . PRO A 1 394 ? 15.465 -1.767 53.488 1.00 22.04 ? 394 PRO A CB 1 ATOM 3139 C CG . PRO A 1 394 ? 16.415 -0.808 54.074 1.00 22.23 ? 394 PRO A CG 1 ATOM 3140 C CD . PRO A 1 394 ? 17.233 -0.249 52.922 1.00 20.93 ? 394 PRO A CD 1 ATOM 3141 N N . LEU A 1 395 ? 15.047 -1.803 50.348 1.00 18.49 ? 395 LEU A N 1 ATOM 3142 C CA . LEU A 1 395 ? 14.157 -2.064 49.156 1.00 17.48 ? 395 LEU A CA 1 ATOM 3143 C C . LEU A 1 395 ? 14.864 -2.916 48.128 1.00 17.07 ? 395 LEU A C 1 ATOM 3144 O O . LEU A 1 395 ? 14.273 -3.815 47.556 1.00 19.10 ? 395 LEU A O 1 ATOM 3145 C CB . LEU A 1 395 ? 13.761 -0.733 48.528 1.00 15.70 ? 395 LEU A CB 1 ATOM 3146 C CG . LEU A 1 395 ? 12.827 0.078 49.414 1.00 15.83 ? 395 LEU A CG 1 ATOM 3147 C CD1 . LEU A 1 395 ? 12.707 1.524 48.981 1.00 15.11 ? 395 LEU A CD1 1 ATOM 3148 C CD2 . LEU A 1 395 ? 11.468 -0.557 49.537 1.00 16.12 ? 395 LEU A CD2 1 ATOM 3149 N N . VAL A 1 396 ? 16.136 -2.620 47.906 1.00 19.09 ? 396 VAL A N 1 ATOM 3150 C CA . VAL A 1 396 ? 16.979 -3.382 46.973 1.00 19.41 ? 396 VAL A CA 1 ATOM 3151 C C . VAL A 1 396 ? 17.021 -4.833 47.452 1.00 19.71 ? 396 VAL A C 1 ATOM 3152 O O . VAL A 1 396 ? 16.960 -5.726 46.638 1.00 20.85 ? 396 VAL A O 1 ATOM 3153 C CB . VAL A 1 396 ? 18.368 -2.739 46.831 1.00 19.48 ? 396 VAL A CB 1 ATOM 3154 C CG1 . VAL A 1 396 ? 19.297 -3.612 45.998 1.00 20.75 ? 396 VAL A CG1 1 ATOM 3155 C CG2 . VAL A 1 396 ? 18.246 -1.346 46.220 1.00 20.76 ? 396 VAL A CG2 1 ATOM 3156 N N . ARG A 1 397 ? 17.055 -5.082 48.781 1.00 22.42 ? 397 ARG A N 1 ATOM 3157 C CA . ARG A 1 397 ? 17.180 -6.474 49.275 1.00 21.59 ? 397 ARG A CA 1 ATOM 3158 C C . ARG A 1 397 ? 15.884 -7.174 49.018 1.00 21.31 ? 397 ARG A C 1 ATOM 3159 O O . ARG A 1 397 ? 15.872 -8.359 48.615 1.00 19.18 ? 397 ARG A O 1 ATOM 3160 C CB . ARG A 1 397 ? 17.464 -6.511 50.766 1.00 23.51 ? 397 ARG A CB 1 ATOM 3161 C CG . ARG A 1 397 ? 18.842 -6.071 51.142 1.00 26.05 ? 397 ARG A CG 1 ATOM 3162 C CD . ARG A 1 397 ? 19.150 -6.410 52.604 1.00 28.54 ? 397 ARG A CD 1 ATOM 3163 N NE . ARG A 1 397 ? 20.344 -5.684 52.941 1.00 28.55 ? 397 ARG A NE 1 ATOM 3164 C CZ . ARG A 1 397 ? 20.407 -4.447 53.426 1.00 29.27 ? 397 ARG A CZ 1 ATOM 3165 N NH1 . ARG A 1 397 ? 19.328 -3.779 53.812 1.00 25.67 ? 397 ARG A NH1 1 ATOM 3166 N NH2 . ARG A 1 397 ? 21.602 -3.896 53.623 1.00 29.00 ? 397 ARG A NH2 1 ATOM 3167 N N . GLY A 1 398 ? 14.781 -6.447 49.209 1.00 19.68 ? 398 GLY A N 1 ATOM 3168 C CA . GLY A 1 398 ? 13.478 -6.985 48.815 1.00 20.82 ? 398 GLY A CA 1 ATOM 3169 C C . GLY A 1 398 ? 13.358 -7.323 47.328 1.00 21.02 ? 398 GLY A C 1 ATOM 3170 O O . GLY A 1 398 ? 12.782 -8.341 46.977 1.00 20.83 ? 398 GLY A O 1 ATOM 3171 N N . LEU A 1 399 ? 13.897 -6.466 46.463 1.00 22.17 ? 399 LEU A N 1 ATOM 3172 C CA . LEU A 1 399 ? 13.899 -6.770 45.020 1.00 24.10 ? 399 LEU A CA 1 ATOM 3173 C C . LEU A 1 399 ? 14.506 -8.115 44.690 1.00 25.00 ? 399 LEU A C 1 ATOM 3174 O O . LEU A 1 399 ? 14.074 -8.796 43.744 1.00 24.86 ? 399 LEU A O 1 ATOM 3175 C CB . LEU A 1 399 ? 14.585 -5.677 44.226 1.00 25.66 ? 399 LEU A CB 1 ATOM 3176 C CG . LEU A 1 399 ? 13.642 -4.517 43.916 1.00 27.49 ? 399 LEU A CG 1 ATOM 3177 C CD1 . LEU A 1 399 ? 14.387 -3.224 43.603 1.00 29.59 ? 399 LEU A CD1 1 ATOM 3178 C CD2 . LEU A 1 399 ? 12.708 -4.910 42.798 1.00 26.98 ? 399 LEU A CD2 1 ATOM 3179 N N . LEU A 1 400 ? 15.487 -8.520 45.497 1.00 23.23 ? 400 LEU A N 1 ATOM 3180 C CA . LEU A 1 400 ? 16.280 -9.706 45.221 1.00 21.14 ? 400 LEU A CA 1 ATOM 3181 C C . LEU A 1 400 ? 15.686 -10.929 45.877 1.00 22.87 ? 400 LEU A C 1 ATOM 3182 O O . LEU A 1 400 ? 15.605 -12.032 45.285 1.00 19.73 ? 400 LEU A O 1 ATOM 3183 C CB . LEU A 1 400 ? 17.727 -9.482 45.664 1.00 23.04 ? 400 LEU A CB 1 ATOM 3184 C CG . LEU A 1 400 ? 18.629 -8.464 44.952 1.00 22.45 ? 400 LEU A CG 1 ATOM 3185 C CD1 . LEU A 1 400 ? 19.836 -8.173 45.846 1.00 23.66 ? 400 LEU A CD1 1 ATOM 3186 C CD2 . LEU A 1 400 ? 19.064 -8.909 43.563 1.00 22.23 ? 400 LEU A CD2 1 ATOM 3187 N N . ALA A 1 401 ? 15.163 -10.755 47.080 1.00 22.34 ? 401 ALA A N 1 ATOM 3188 C CA . ALA A 1 401 ? 14.708 -11.934 47.829 1.00 22.12 ? 401 ALA A CA 1 ATOM 3189 C C . ALA A 1 401 ? 13.255 -12.164 47.719 1.00 23.18 ? 401 ALA A C 1 ATOM 3190 O O . ALA A 1 401 ? 12.808 -13.287 47.971 1.00 24.74 ? 401 ALA A O 1 ATOM 3191 C CB . ALA A 1 401 ? 15.118 -11.791 49.318 1.00 21.54 ? 401 ALA A CB 1 ATOM 3192 N N . LYS A 1 402 ? 12.463 -11.142 47.355 1.00 20.87 ? 402 LYS A N 1 ATOM 3193 C CA . LYS A 1 402 ? 11.041 -11.387 47.121 1.00 21.40 ? 402 LYS A CA 1 ATOM 3194 C C . LYS A 1 402 ? 10.754 -11.751 45.645 1.00 20.76 ? 402 LYS A C 1 ATOM 3195 O O . LYS A 1 402 ? 11.629 -11.601 44.801 1.00 23.78 ? 402 LYS A O 1 ATOM 3196 C CB . LYS A 1 402 ? 10.212 -10.179 47.549 1.00 23.26 ? 402 LYS A CB 1 ATOM 3197 C CG . LYS A 1 402 ? 10.370 -9.889 49.030 1.00 24.19 ? 402 LYS A CG 1 ATOM 3198 C CD . LYS A 1 402 ? 9.720 -10.927 49.920 1.00 24.44 ? 402 LYS A CD 1 ATOM 3199 C CE . LYS A 1 402 ? 10.048 -10.621 51.372 1.00 25.71 ? 402 LYS A CE 1 ATOM 3200 N NZ . LYS A 1 402 ? 9.323 -11.563 52.243 1.00 28.52 ? 402 LYS A NZ 1 ATOM 3201 N N . ASN A 1 403 ? 9.573 -12.290 45.385 1.00 19.71 ? 403 ASN A N 1 ATOM 3202 C CA . ASN A 1 403 ? 9.150 -12.714 44.078 1.00 21.31 ? 403 ASN A CA 1 ATOM 3203 C C . ASN A 1 403 ? 8.234 -11.714 43.320 1.00 20.81 ? 403 ASN A C 1 ATOM 3204 O O . ASN A 1 403 ? 7.501 -10.954 43.951 1.00 18.94 ? 403 ASN A O 1 ATOM 3205 C CB . ASN A 1 403 ? 8.369 -14.027 44.236 1.00 23.62 ? 403 ASN A CB 1 ATOM 3206 C CG . ASN A 1 403 ? 9.219 -15.152 44.779 1.00 27.67 ? 403 ASN A CG 1 ATOM 3207 O OD1 . ASN A 1 403 ? 10.432 -15.032 44.900 1.00 38.68 ? 403 ASN A OD1 1 ATOM 3208 N ND2 . ASN A 1 403 ? 8.593 -16.293 45.067 1.00 32.60 ? 403 ASN A ND2 1 ATOM 3209 N N . SER A 1 404 ? 8.270 -11.758 41.978 1.00 20.36 ? 404 SER A N 1 ATOM 3210 C CA . SER A 1 404 ? 7.202 -11.142 41.147 1.00 18.34 ? 404 SER A CA 1 ATOM 3211 C C . SER A 1 404 ? 5.934 -11.952 41.350 1.00 20.11 ? 404 SER A C 1 ATOM 3212 O O . SER A 1 404 ? 5.999 -13.153 41.749 1.00 22.24 ? 404 SER A O 1 ATOM 3213 C CB . SER A 1 404 ? 7.552 -11.118 39.679 1.00 17.51 ? 404 SER A CB 1 ATOM 3214 O OG . SER A 1 404 ? 8.718 -10.348 39.384 1.00 17.50 ? 404 SER A OG 1 ATOM 3215 N N . LYS A 1 405 ? 4.782 -11.318 41.134 1.00 18.44 ? 405 LYS A N 1 ATOM 3216 C CA . LYS A 1 405 ? 3.548 -12.044 40.938 1.00 18.09 ? 405 LYS A CA 1 ATOM 3217 C C . LYS A 1 405 ? 3.587 -12.842 39.615 1.00 19.66 ? 405 LYS A C 1 ATOM 3218 O O . LYS A 1 405 ? 4.166 -12.432 38.631 1.00 18.49 ? 405 LYS A O 1 ATOM 3219 C CB . LYS A 1 405 ? 2.385 -11.079 40.923 1.00 18.43 ? 405 LYS A CB 1 ATOM 3220 C CG . LYS A 1 405 ? 1.020 -11.709 40.780 1.00 18.09 ? 405 LYS A CG 1 ATOM 3221 C CD . LYS A 1 405 ? -0.061 -10.659 40.576 1.00 19.24 ? 405 LYS A CD 1 ATOM 3222 C CE . LYS A 1 405 ? -1.343 -11.235 40.073 1.00 19.29 ? 405 LYS A CE 1 ATOM 3223 N NZ . LYS A 1 405 ? -1.212 -11.929 38.743 1.00 21.06 ? 405 LYS A NZ 1 ATOM 3224 N N . LEU A 1 406 ? 2.920 -13.973 39.614 1.00 23.23 ? 406 LEU A N 1 ATOM 3225 C CA . LEU A 1 406 ? 2.770 -14.785 38.411 1.00 22.57 ? 406 LEU A CA 1 ATOM 3226 C C . LEU A 1 406 ? 1.460 -14.460 37.797 1.00 23.15 ? 406 LEU A C 1 ATOM 3227 O O . LEU A 1 406 ? 0.415 -14.476 38.466 1.00 21.61 ? 406 LEU A O 1 ATOM 3228 C CB . LEU A 1 406 ? 2.794 -16.289 38.730 1.00 25.34 ? 406 LEU A CB 1 ATOM 3229 C CG . LEU A 1 406 ? 2.869 -17.210 37.510 1.00 26.57 ? 406 LEU A CG 1 ATOM 3230 C CD1 . LEU A 1 406 ? 4.178 -17.003 36.788 1.00 29.68 ? 406 LEU A CD1 1 ATOM 3231 C CD2 . LEU A 1 406 ? 2.727 -18.669 37.921 1.00 27.51 ? 406 LEU A CD2 1 ATOM 3232 N N . MET A 1 407 ? 1.459 -14.171 36.497 1.00 23.28 ? 407 MET A N 1 ATOM 3233 C CA . MET A 1 407 ? 0.161 -14.023 35.830 1.00 21.76 ? 407 MET A CA 1 ATOM 3234 C C . MET A 1 407 ? -0.621 -15.320 35.970 1.00 22.53 ? 407 MET A C 1 ATOM 3235 O O . MET A 1 407 ? -0.072 -16.381 35.772 1.00 20.53 ? 407 MET A O 1 ATOM 3236 C CB . MET A 1 407 ? 0.322 -13.641 34.363 1.00 24.22 ? 407 MET A CB 1 ATOM 3237 C CG . MET A 1 407 ? -1.008 -13.400 33.675 1.00 24.00 ? 407 MET A CG 1 ATOM 3238 S SD . MET A 1 407 ? -1.628 -14.968 33.199 1.00 32.68 ? 407 MET A SD 1 ATOM 3239 C CE . MET A 1 407 ? -3.287 -14.483 32.679 1.00 31.40 ? 407 MET A CE 1 ATOM 3240 N N . ASN A 1 408 ? -1.904 -15.238 36.310 1.00 22.04 ? 408 ASN A N 1 ATOM 3241 C CA . ASN A 1 408 ? -2.727 -16.435 36.426 1.00 27.32 ? 408 ASN A CA 1 ATOM 3242 C C . ASN A 1 408 ? -4.022 -16.103 35.754 1.00 21.41 ? 408 ASN A C 1 ATOM 3243 O O . ASN A 1 408 ? -4.488 -14.978 35.936 1.00 20.04 ? 408 ASN A O 1 ATOM 3244 C CB . ASN A 1 408 ? -2.970 -16.749 37.895 1.00 31.89 ? 408 ASN A CB 1 ATOM 3245 C CG . ASN A 1 408 ? -3.596 -18.081 38.097 1.00 37.88 ? 408 ASN A CG 1 ATOM 3246 O OD1 . ASN A 1 408 ? -4.776 -18.268 37.762 1.00 34.14 ? 408 ASN A OD1 1 ATOM 3247 N ND2 . ASN A 1 408 ? -2.820 -19.048 38.657 1.00 42.36 ? 408 ASN A ND2 1 ATOM 3248 N N . GLN A 1 409 ? -4.597 -17.025 34.978 1.00 20.43 ? 409 GLN A N 1 ATOM 3249 C CA . GLN A 1 409 ? -5.871 -16.737 34.246 1.00 20.36 ? 409 GLN A CA 1 ATOM 3250 C C . GLN A 1 409 ? -7.076 -16.433 35.167 1.00 22.50 ? 409 GLN A C 1 ATOM 3251 O O . GLN A 1 409 ? -7.972 -15.731 34.758 1.00 21.69 ? 409 GLN A O 1 ATOM 3252 C CB . GLN A 1 409 ? -6.247 -17.868 33.330 1.00 20.33 ? 409 GLN A CB 1 ATOM 3253 C CG . GLN A 1 409 ? -5.360 -17.986 32.100 1.00 19.66 ? 409 GLN A CG 1 ATOM 3254 C CD . GLN A 1 409 ? -5.840 -19.135 31.217 1.00 21.35 ? 409 GLN A CD 1 ATOM 3255 O OE1 . GLN A 1 409 ? -6.132 -20.244 31.713 1.00 19.81 ? 409 GLN A OE1 1 ATOM 3256 N NE2 . GLN A 1 409 ? -5.857 -18.917 29.907 1.00 19.34 ? 409 GLN A NE2 1 ATOM 3257 N N . ASN A 1 410 ? -7.085 -16.858 36.428 1.00 23.30 ? 410 ASN A N 1 ATOM 3258 C CA . ASN A 1 410 ? -8.152 -16.337 37.338 1.00 28.70 ? 410 ASN A CA 1 ATOM 3259 C C . ASN A 1 410 ? -7.626 -15.489 38.527 1.00 26.57 ? 410 ASN A C 1 ATOM 3260 O O . ASN A 1 410 ? -8.372 -15.225 39.485 1.00 25.50 ? 410 ASN A O 1 ATOM 3261 C CB . ASN A 1 410 ? -9.119 -17.444 37.723 1.00 35.89 ? 410 ASN A CB 1 ATOM 3262 C CG . ASN A 1 410 ? -8.408 -18.701 37.947 1.00 41.98 ? 410 ASN A CG 1 ATOM 3263 O OD1 . ASN A 1 410 ? -8.534 -19.686 37.195 1.00 42.07 ? 410 ASN A OD1 1 ATOM 3264 N ND2 . ASN A 1 410 ? -7.501 -18.627 38.884 1.00 44.64 ? 410 ASN A ND2 1 ATOM 3265 N N . LYS A 1 411 ? -6.367 -15.036 38.419 1.00 20.68 ? 411 LYS A N 1 ATOM 3266 C CA . LYS A 1 411 ? -5.804 -14.017 39.325 1.00 18.86 ? 411 LYS A CA 1 ATOM 3267 C C . LYS A 1 411 ? -4.846 -13.119 38.516 1.00 18.29 ? 411 LYS A C 1 ATOM 3268 O O . LYS A 1 411 ? -3.617 -13.276 38.566 1.00 14.83 ? 411 LYS A O 1 ATOM 3269 C CB . LYS A 1 411 ? -5.078 -14.643 40.521 1.00 18.88 ? 411 LYS A CB 1 ATOM 3270 C CG . LYS A 1 411 ? -5.936 -15.590 41.366 1.00 19.47 ? 411 LYS A CG 1 ATOM 3271 C CD . LYS A 1 411 ? -5.116 -16.102 42.537 1.00 20.03 ? 411 LYS A CD 1 ATOM 3272 C CE . LYS A 1 411 ? -5.922 -16.998 43.462 1.00 19.79 ? 411 LYS A CE 1 ATOM 3273 N NZ . LYS A 1 411 ? -5.020 -17.375 44.584 1.00 25.38 ? 411 LYS A NZ 1 ATOM 3274 N N . MET A 1 412 ? -5.434 -12.156 37.806 1.00 18.06 ? 412 MET A N 1 ATOM 3275 C CA . MET A 1 412 ? -4.702 -11.363 36.828 1.00 16.30 ? 412 MET A CA 1 ATOM 3276 C C . MET A 1 412 ? -4.017 -10.136 37.415 1.00 16.44 ? 412 MET A C 1 ATOM 3277 O O . MET A 1 412 ? -2.807 -10.049 37.361 1.00 17.42 ? 412 MET A O 1 ATOM 3278 C CB . MET A 1 412 ? -5.664 -10.976 35.683 1.00 17.39 ? 412 MET A CB 1 ATOM 3279 C CG . MET A 1 412 ? -5.996 -12.141 34.738 1.00 17.56 ? 412 MET A CG 1 ATOM 3280 S SD . MET A 1 412 ? -6.860 -11.532 33.258 1.00 19.37 ? 412 MET A SD 1 ATOM 3281 C CE . MET A 1 412 ? -7.169 -13.059 32.355 1.00 19.71 ? 412 MET A CE 1 ATOM 3282 N N . VAL A 1 413 ? -4.778 -9.182 37.958 1.00 15.07 ? 413 VAL A N 1 ATOM 3283 C CA . VAL A 1 413 ? -4.212 -7.983 38.485 1.00 15.29 ? 413 VAL A CA 1 ATOM 3284 C C . VAL A 1 413 ? -4.645 -7.798 39.944 1.00 16.02 ? 413 VAL A C 1 ATOM 3285 O O . VAL A 1 413 ? -5.835 -7.722 40.222 1.00 16.57 ? 413 VAL A O 1 ATOM 3286 C CB . VAL A 1 413 ? -4.635 -6.730 37.660 1.00 15.25 ? 413 VAL A CB 1 ATOM 3287 C CG1 . VAL A 1 413 ? -4.097 -5.453 38.278 1.00 14.30 ? 413 VAL A CG1 1 ATOM 3288 C CG2 . VAL A 1 413 ? -4.120 -6.861 36.189 1.00 15.66 ? 413 VAL A CG2 1 ATOM 3289 N N . THR A 1 414 ? -3.654 -7.676 40.814 1.00 19.15 ? 414 THR A N 1 ATOM 3290 C CA . THR A 1 414 ? -3.883 -7.357 42.238 1.00 19.77 ? 414 THR A CA 1 ATOM 3291 C C . THR A 1 414 ? -4.734 -6.089 42.467 1.00 18.90 ? 414 THR A C 1 ATOM 3292 O O . THR A 1 414 ? -4.596 -5.023 41.794 1.00 16.91 ? 414 THR A O 1 ATOM 3293 C CB . THR A 1 414 ? -2.561 -7.189 43.039 1.00 19.73 ? 414 THR A CB 1 ATOM 3294 O OG1 . THR A 1 414 ? -2.874 -6.954 44.402 1.00 20.52 ? 414 THR A OG1 1 ATOM 3295 C CG2 . THR A 1 414 ? -1.727 -5.986 42.574 1.00 21.72 ? 414 THR A CG2 1 ATOM 3296 N N . SER A 1 415 ? -5.597 -6.199 43.445 1.00 18.36 ? 415 SER A N 1 ATOM 3297 C CA . SER A 1 415 ? -6.471 -5.108 43.789 1.00 17.84 ? 415 SER A CA 1 ATOM 3298 C C . SER A 1 415 ? -5.746 -3.869 44.245 1.00 15.82 ? 415 SER A C 1 ATOM 3299 O O . SER A 1 415 ? -6.349 -2.802 44.195 1.00 16.99 ? 415 SER A O 1 ATOM 3300 C CB . SER A 1 415 ? -7.507 -5.534 44.857 1.00 20.46 ? 415 SER A CB 1 ATOM 3301 O OG . SER A 1 415 ? -8.336 -6.497 44.276 1.00 26.58 ? 415 SER A OG 1 ATOM 3302 N N . GLU A 1 416 ? -4.482 -3.970 44.676 1.00 16.73 ? 416 GLU A N 1 ATOM 3303 C CA . GLU A 1 416 ? -3.670 -2.783 44.914 1.00 16.31 ? 416 GLU A CA 1 ATOM 3304 C C . GLU A 1 416 ? -3.594 -1.845 43.697 1.00 16.41 ? 416 GLU A C 1 ATOM 3305 O O . GLU A 1 416 ? -3.466 -0.610 43.844 1.00 15.42 ? 416 GLU A O 1 ATOM 3306 C CB . GLU A 1 416 ? -2.266 -3.152 45.375 1.00 17.70 ? 416 GLU A CB 1 ATOM 3307 C CG . GLU A 1 416 ? -2.209 -3.978 46.658 1.00 18.00 ? 416 GLU A CG 1 ATOM 3308 C CD . GLU A 1 416 ? -2.709 -3.190 47.876 1.00 19.76 ? 416 GLU A CD 1 ATOM 3309 O OE1 . GLU A 1 416 ? -2.209 -2.074 48.185 1.00 17.47 ? 416 GLU A OE1 1 ATOM 3310 O OE2 . GLU A 1 416 ? -3.662 -3.654 48.493 1.00 21.95 ? 416 GLU A OE2 1 ATOM 3311 N N . LEU A 1 417 ? -3.692 -2.444 42.517 1.00 16.25 ? 417 LEU A N 1 ATOM 3312 C CA . LEU A 1 417 ? -3.685 -1.727 41.263 1.00 16.01 ? 417 LEU A CA 1 ATOM 3313 C C . LEU A 1 417 ? -5.060 -1.639 40.613 1.00 16.11 ? 417 LEU A C 1 ATOM 3314 O O . LEU A 1 417 ? -5.339 -0.680 39.917 1.00 17.80 ? 417 LEU A O 1 ATOM 3315 C CB . LEU A 1 417 ? -2.777 -2.429 40.266 1.00 15.91 ? 417 LEU A CB 1 ATOM 3316 C CG . LEU A 1 417 ? -1.291 -2.362 40.450 1.00 16.91 ? 417 LEU A CG 1 ATOM 3317 C CD1 . LEU A 1 417 ? -0.592 -3.374 39.531 1.00 17.74 ? 417 LEU A CD1 1 ATOM 3318 C CD2 . LEU A 1 417 ? -0.727 -0.987 40.219 1.00 15.65 ? 417 LEU A CD2 1 ATOM 3319 N N . ARG A 1 418 ? -5.910 -2.651 40.838 1.00 15.35 ? 418 ARG A N 1 ATOM 3320 C CA . ARG A 1 418 ? -7.178 -2.728 40.166 1.00 15.58 ? 418 ARG A CA 1 ATOM 3321 C C . ARG A 1 418 ? -8.246 -1.955 40.918 1.00 16.98 ? 418 ARG A C 1 ATOM 3322 O O . ARG A 1 418 ? -9.222 -1.558 40.340 1.00 16.27 ? 418 ARG A O 1 ATOM 3323 C CB . ARG A 1 418 ? -7.604 -4.167 39.993 1.00 15.66 ? 418 ARG A CB 1 ATOM 3324 C CG . ARG A 1 418 ? -8.588 -4.391 38.868 1.00 16.09 ? 418 ARG A CG 1 ATOM 3325 C CD . ARG A 1 418 ? -9.102 -5.796 38.923 1.00 17.23 ? 418 ARG A CD 1 ATOM 3326 N NE . ARG A 1 418 ? -9.974 -5.966 40.074 1.00 18.24 ? 418 ARG A NE 1 ATOM 3327 C CZ . ARG A 1 418 ? -11.246 -5.651 40.127 1.00 17.45 ? 418 ARG A CZ 1 ATOM 3328 N NH1 . ARG A 1 418 ? -11.846 -5.008 39.129 1.00 18.53 ? 418 ARG A NH1 1 ATOM 3329 N NH2 . ARG A 1 418 ? -11.914 -5.873 41.261 1.00 16.42 ? 418 ARG A NH2 1 ATOM 3330 N N . ASN A 1 419 ? -8.029 -1.705 42.213 1.00 17.25 ? 419 ASN A N 1 ATOM 3331 C CA . ASN A 1 419 ? -8.950 -0.908 42.946 1.00 17.66 ? 419 ASN A CA 1 ATOM 3332 C C . ASN A 1 419 ? -8.344 0.276 43.628 1.00 18.04 ? 419 ASN A C 1 ATOM 3333 O O . ASN A 1 419 ? -9.072 1.228 43.924 1.00 17.22 ? 419 ASN A O 1 ATOM 3334 C CB . ASN A 1 419 ? -9.681 -1.737 43.974 1.00 16.46 ? 419 ASN A CB 1 ATOM 3335 C CG . ASN A 1 419 ? -10.766 -2.576 43.358 1.00 18.54 ? 419 ASN A CG 1 ATOM 3336 O OD1 . ASN A 1 419 ? -11.500 -2.157 42.466 1.00 17.46 ? 419 ASN A OD1 1 ATOM 3337 N ND2 . ASN A 1 419 ? -10.863 -3.761 43.825 1.00 20.35 ? 419 ASN A ND2 1 ATOM 3338 N N . LYS A 1 420 ? -7.036 0.243 43.892 1.00 19.27 ? 420 LYS A N 1 ATOM 3339 C CA . LYS A 1 420 ? -6.457 1.355 44.732 1.00 18.68 ? 420 LYS A CA 1 ATOM 3340 C C . LYS A 1 420 ? -5.389 2.236 44.097 1.00 19.41 ? 420 LYS A C 1 ATOM 3341 O O . LYS A 1 420 ? -4.602 2.882 44.802 1.00 16.69 ? 420 LYS A O 1 ATOM 3342 C CB . LYS A 1 420 ? -5.947 0.737 46.036 1.00 17.79 ? 420 LYS A CB 1 ATOM 3343 C CG . LYS A 1 420 ? -7.076 -0.042 46.739 1.00 20.16 ? 420 LYS A CG 1 ATOM 3344 C CD . LYS A 1 420 ? -6.603 -0.671 48.022 1.00 23.93 ? 420 LYS A CD 1 ATOM 3345 C CE . LYS A 1 420 ? -7.775 -1.258 48.780 1.00 27.35 ? 420 LYS A CE 1 ATOM 3346 N NZ . LYS A 1 420 ? -7.292 -1.718 50.091 1.00 31.99 ? 420 LYS A NZ 1 ATOM 3347 N N . LEU A 1 421 ? -5.368 2.295 42.779 1.00 17.43 ? 421 LEU A N 1 ATOM 3348 C CA . LEU A 1 421 ? -4.375 3.074 42.108 1.00 15.22 ? 421 LEU A CA 1 ATOM 3349 C C . LEU A 1 421 ? -4.571 4.538 42.422 1.00 17.11 ? 421 LEU A C 1 ATOM 3350 O O . LEU A 1 421 ? -5.680 5.037 42.428 1.00 18.63 ? 421 LEU A O 1 ATOM 3351 C CB . LEU A 1 421 ? -4.461 2.859 40.605 1.00 16.38 ? 421 LEU A CB 1 ATOM 3352 C CG . LEU A 1 421 ? -3.413 3.598 39.696 1.00 14.60 ? 421 LEU A CG 1 ATOM 3353 C CD1 . LEU A 1 421 ? -2.098 2.957 39.890 1.00 16.46 ? 421 LEU A CD1 1 ATOM 3354 C CD2 . LEU A 1 421 ? -3.863 3.601 38.252 1.00 15.45 ? 421 LEU A CD2 1 ATOM 3355 N N . PHE A 1 422 ? -3.482 5.239 42.669 1.00 16.93 ? 422 PHE A N 1 ATOM 3356 C CA . PHE A 1 422 ? -3.474 6.665 42.881 1.00 19.05 ? 422 PHE A CA 1 ATOM 3357 C C . PHE A 1 422 ? -2.927 7.324 41.605 1.00 21.87 ? 422 PHE A C 1 ATOM 3358 O O . PHE A 1 422 ? -1.924 6.876 41.072 1.00 21.41 ? 422 PHE A O 1 ATOM 3359 C CB . PHE A 1 422 ? -2.551 7.025 43.996 1.00 20.89 ? 422 PHE A CB 1 ATOM 3360 C CG . PHE A 1 422 ? -2.531 8.481 44.291 1.00 23.34 ? 422 PHE A CG 1 ATOM 3361 C CD1 . PHE A 1 422 ? -3.439 9.021 45.181 1.00 23.99 ? 422 PHE A CD1 1 ATOM 3362 C CD2 . PHE A 1 422 ? -1.596 9.336 43.688 1.00 24.08 ? 422 PHE A CD2 1 ATOM 3363 C CE1 . PHE A 1 422 ? -3.412 10.399 45.474 1.00 24.73 ? 422 PHE A CE1 1 ATOM 3364 C CE2 . PHE A 1 422 ? -1.597 10.685 43.955 1.00 24.55 ? 422 PHE A CE2 1 ATOM 3365 C CZ . PHE A 1 422 ? -2.532 11.220 44.833 1.00 25.29 ? 422 PHE A CZ 1 ATOM 3366 N N . GLN A 1 423 ? -3.605 8.329 41.091 1.00 23.32 ? 423 GLN A N 1 ATOM 3367 C CA . GLN A 1 423 ? -3.201 8.997 39.893 1.00 23.56 ? 423 GLN A CA 1 ATOM 3368 C C . GLN A 1 423 ? -2.823 10.403 40.256 1.00 22.69 ? 423 GLN A C 1 ATOM 3369 O O . GLN A 1 423 ? -3.486 11.008 41.018 1.00 20.01 ? 423 GLN A O 1 ATOM 3370 C CB . GLN A 1 423 ? -4.356 9.002 38.925 1.00 27.92 ? 423 GLN A CB 1 ATOM 3371 C CG . GLN A 1 423 ? -4.680 7.638 38.398 1.00 30.22 ? 423 GLN A CG 1 ATOM 3372 C CD . GLN A 1 423 ? -3.981 7.381 37.103 1.00 33.77 ? 423 GLN A CD 1 ATOM 3373 O OE1 . GLN A 1 423 ? -4.545 7.584 36.088 1.00 46.77 ? 423 GLN A OE1 1 ATOM 3374 N NE2 . GLN A 1 423 ? -2.743 7.001 37.145 1.00 35.38 ? 423 GLN A NE2 1 ATOM 3375 N N . PRO A 1 424 ? -1.744 10.909 39.686 1.00 25.41 ? 424 PRO A N 1 ATOM 3376 C CA . PRO A 1 424 ? -1.134 12.124 40.191 1.00 26.54 ? 424 PRO A CA 1 ATOM 3377 C C . PRO A 1 424 ? -1.980 13.364 40.127 1.00 29.24 ? 424 PRO A C 1 ATOM 3378 O O . PRO A 1 424 ? -1.751 14.248 40.948 1.00 33.70 ? 424 PRO A O 1 ATOM 3379 C CB . PRO A 1 424 ? 0.150 12.267 39.375 1.00 29.46 ? 424 PRO A CB 1 ATOM 3380 C CG . PRO A 1 424 ? 0.067 11.266 38.284 1.00 29.20 ? 424 PRO A CG 1 ATOM 3381 C CD . PRO A 1 424 ? -0.913 10.227 38.694 1.00 25.89 ? 424 PRO A CD 1 ATOM 3382 N N . THR A 1 425 ? -2.973 13.453 39.227 1.00 31.13 ? 425 THR A N 1 ATOM 3383 C CA . THR A 1 425 ? -3.790 14.660 39.189 1.00 34.37 ? 425 THR A CA 1 ATOM 3384 C C . THR A 1 425 ? -5.066 14.537 40.022 1.00 35.81 ? 425 THR A C 1 ATOM 3385 O O . THR A 1 425 ? -5.850 15.474 40.057 1.00 40.41 ? 425 THR A O 1 ATOM 3386 C CB . THR A 1 425 ? -4.129 15.107 37.739 1.00 36.43 ? 425 THR A CB 1 ATOM 3387 O OG1 . THR A 1 425 ? -5.031 14.191 37.161 1.00 36.52 ? 425 THR A OG1 1 ATOM 3388 C CG2 . THR A 1 425 ? -2.866 15.160 36.861 1.00 37.67 ? 425 THR A CG2 1 ATOM 3389 N N . HIS A 1 426 ? -5.247 13.417 40.715 1.00 34.61 ? 426 HIS A N 1 ATOM 3390 C CA . HIS A 1 426 ? -6.433 13.183 41.533 1.00 32.39 ? 426 HIS A CA 1 ATOM 3391 C C . HIS A 1 426 ? -6.084 12.893 43.004 1.00 33.15 ? 426 HIS A C 1 ATOM 3392 O O . HIS A 1 426 ? -4.922 12.914 43.383 1.00 38.06 ? 426 HIS A O 1 ATOM 3393 C CB . HIS A 1 426 ? -7.250 12.050 40.897 1.00 33.60 ? 426 HIS A CB 1 ATOM 3394 C CG . HIS A 1 426 ? -7.597 12.335 39.478 1.00 32.49 ? 426 HIS A CG 1 ATOM 3395 N ND1 . HIS A 1 426 ? -8.648 13.153 39.129 1.00 30.13 ? 426 HIS A ND1 1 ATOM 3396 C CD2 . HIS A 1 426 ? -6.940 12.062 38.337 1.00 31.54 ? 426 HIS A CD2 1 ATOM 3397 C CE1 . HIS A 1 426 ? -8.666 13.310 37.832 1.00 28.92 ? 426 HIS A CE1 1 ATOM 3398 N NE2 . HIS A 1 426 ? -7.637 12.662 37.326 1.00 31.91 ? 426 HIS A NE2 1 ATOM 3399 N N . LYS A 1 427 ? -7.091 12.632 43.815 1.00 29.56 ? 427 LYS A N 1 ATOM 3400 C CA . LYS A 1 427 ? -6.864 12.677 45.241 1.00 32.25 ? 427 LYS A CA 1 ATOM 3401 C C . LYS A 1 427 ? -7.056 11.338 45.939 1.00 29.44 ? 427 LYS A C 1 ATOM 3402 O O . LYS A 1 427 ? -6.805 11.229 47.124 1.00 30.65 ? 427 LYS A O 1 ATOM 3403 C CB . LYS A 1 427 ? -7.796 13.730 45.852 1.00 35.66 ? 427 LYS A CB 1 ATOM 3404 C CG . LYS A 1 427 ? -7.485 15.175 45.483 1.00 41.56 ? 427 LYS A CG 1 ATOM 3405 C CD . LYS A 1 427 ? -8.679 16.075 45.812 1.00 48.05 ? 427 LYS A CD 1 ATOM 3406 C CE . LYS A 1 427 ? -8.497 17.510 45.311 1.00 53.10 ? 427 LYS A CE 1 ATOM 3407 N NZ . LYS A 1 427 ? -7.372 18.191 46.018 1.00 56.96 ? 427 LYS A NZ 1 ATOM 3408 N N . VAL A 1 428 ? -7.498 10.325 45.203 1.00 26.16 ? 428 VAL A N 1 ATOM 3409 C CA . VAL A 1 428 ? -7.932 9.052 45.793 1.00 26.01 ? 428 VAL A CA 1 ATOM 3410 C C . VAL A 1 428 ? -7.096 7.870 45.348 1.00 25.77 ? 428 VAL A C 1 ATOM 3411 O O . VAL A 1 428 ? -6.568 7.822 44.223 1.00 26.68 ? 428 VAL A O 1 ATOM 3412 C CB . VAL A 1 428 ? -9.465 8.786 45.572 1.00 30.94 ? 428 VAL A CB 1 ATOM 3413 C CG1 . VAL A 1 428 ? -10.295 9.921 46.213 1.00 33.50 ? 428 VAL A CG1 1 ATOM 3414 C CG2 . VAL A 1 428 ? -9.874 8.661 44.105 1.00 31.50 ? 428 VAL A CG2 1 ATOM 3415 N N . HIS A 1 429 ? -6.933 6.945 46.277 1.00 20.43 ? 429 HIS A N 1 ATOM 3416 C CA . HIS A 1 429 ? -6.430 5.651 45.970 1.00 22.97 ? 429 HIS A CA 1 ATOM 3417 C C . HIS A 1 429 ? -7.637 4.809 45.595 1.00 24.47 ? 429 HIS A C 1 ATOM 3418 O O . HIS A 1 429 ? -8.036 3.892 46.329 1.00 22.45 ? 429 HIS A O 1 ATOM 3419 C CB . HIS A 1 429 ? -5.740 5.065 47.185 1.00 24.58 ? 429 HIS A CB 1 ATOM 3420 C CG . HIS A 1 429 ? -4.396 5.660 47.443 1.00 22.90 ? 429 HIS A CG 1 ATOM 3421 N ND1 . HIS A 1 429 ? -4.213 6.943 47.902 1.00 20.28 ? 429 HIS A ND1 1 ATOM 3422 C CD2 . HIS A 1 429 ? -3.163 5.127 47.298 1.00 23.34 ? 429 HIS A CD2 1 ATOM 3423 C CE1 . HIS A 1 429 ? -2.922 7.168 48.059 1.00 24.47 ? 429 HIS A CE1 1 ATOM 3424 N NE2 . HIS A 1 429 ? -2.260 6.076 47.704 1.00 24.56 ? 429 HIS A NE2 1 ATOM 3425 N N . GLY A 1 430 ? -8.211 5.100 44.419 1.00 22.25 ? 430 GLY A N 1 ATOM 3426 C CA . GLY A 1 430 ? -9.331 4.318 43.980 1.00 22.00 ? 430 GLY A CA 1 ATOM 3427 C C . GLY A 1 430 ? -9.467 4.116 42.501 1.00 20.43 ? 430 GLY A C 1 ATOM 3428 O O . GLY A 1 430 ? -10.586 3.884 42.047 1.00 19.68 ? 430 GLY A O 1 ATOM 3429 N N . PHE A 1 431 ? -8.357 4.191 41.731 1.00 17.55 ? 431 PHE A N 1 ATOM 3430 C CA . PHE A 1 431 ? -8.439 3.949 40.305 1.00 18.28 ? 431 PHE A CA 1 ATOM 3431 C C . PHE A 1 431 ? -8.161 2.464 39.995 1.00 17.32 ? 431 PHE A C 1 ATOM 3432 O O . PHE A 1 431 ? -7.659 1.679 40.848 1.00 13.56 ? 431 PHE A O 1 ATOM 3433 C CB . PHE A 1 431 ? -7.487 4.891 39.575 1.00 20.28 ? 431 PHE A CB 1 ATOM 3434 C CG . PHE A 1 431 ? -7.962 6.300 39.517 1.00 21.77 ? 431 PHE A CG 1 ATOM 3435 C CD1 . PHE A 1 431 ? -7.717 7.174 40.571 1.00 22.54 ? 431 PHE A CD1 1 ATOM 3436 C CD2 . PHE A 1 431 ? -8.668 6.777 38.379 1.00 23.30 ? 431 PHE A CD2 1 ATOM 3437 C CE1 . PHE A 1 431 ? -8.171 8.502 40.508 1.00 21.69 ? 431 PHE A CE1 1 ATOM 3438 C CE2 . PHE A 1 431 ? -9.098 8.089 38.310 1.00 25.09 ? 431 PHE A CE2 1 ATOM 3439 C CZ . PHE A 1 431 ? -8.828 8.964 39.375 1.00 23.62 ? 431 PHE A CZ 1 ATOM 3440 N N . ASP A 1 432 ? -8.479 2.086 38.766 1.00 17.09 ? 432 ASP A N 1 ATOM 3441 C CA . ASP A 1 432 ? -8.355 0.668 38.331 1.00 16.26 ? 432 ASP A CA 1 ATOM 3442 C C . ASP A 1 432 ? -7.438 0.661 37.106 1.00 14.95 ? 432 ASP A C 1 ATOM 3443 O O . ASP A 1 432 ? -7.868 1.011 36.013 1.00 14.27 ? 432 ASP A O 1 ATOM 3444 C CB . ASP A 1 432 ? -9.709 0.146 37.950 1.00 15.98 ? 432 ASP A CB 1 ATOM 3445 C CG . ASP A 1 432 ? -9.688 -1.255 37.406 1.00 16.40 ? 432 ASP A CG 1 ATOM 3446 O OD1 . ASP A 1 432 ? -8.618 -1.777 37.022 1.00 15.34 ? 432 ASP A OD1 1 ATOM 3447 O OD2 . ASP A 1 432 ? -10.757 -1.829 37.422 1.00 16.73 ? 432 ASP A OD2 1 ATOM 3448 N N . LEU A 1 433 ? -6.188 0.294 37.289 1.00 15.70 ? 433 LEU A N 1 ATOM 3449 C CA . LEU A 1 433 ? -5.259 0.206 36.139 1.00 14.55 ? 433 LEU A CA 1 ATOM 3450 C C . LEU A 1 433 ? -5.740 -0.680 34.998 1.00 16.75 ? 433 LEU A C 1 ATOM 3451 O O . LEU A 1 433 ? -5.434 -0.382 33.763 1.00 18.43 ? 433 LEU A O 1 ATOM 3452 C CB . LEU A 1 433 ? -3.852 -0.197 36.609 1.00 15.38 ? 433 LEU A CB 1 ATOM 3453 C CG . LEU A 1 433 ? -2.744 -0.187 35.542 1.00 13.96 ? 433 LEU A CG 1 ATOM 3454 C CD1 . LEU A 1 433 ? -2.643 1.182 34.913 1.00 13.82 ? 433 LEU A CD1 1 ATOM 3455 C CD2 . LEU A 1 433 ? -1.446 -0.589 36.224 1.00 14.99 ? 433 LEU A CD2 1 ATOM 3456 N N . ALA A 1 434 ? -6.398 -1.816 35.326 1.00 17.81 ? 434 ALA A N 1 ATOM 3457 C CA . ALA A 1 434 ? -6.885 -2.687 34.290 1.00 18.15 ? 434 ALA A CA 1 ATOM 3458 C C . ALA A 1 434 ? -7.964 -2.012 33.417 1.00 19.68 ? 434 ALA A C 1 ATOM 3459 O O . ALA A 1 434 ? -7.926 -2.077 32.173 1.00 17.85 ? 434 ALA A O 1 ATOM 3460 C CB . ALA A 1 434 ? -7.359 -4.013 34.829 1.00 19.40 ? 434 ALA A CB 1 ATOM 3461 N N . ALA A 1 435 ? -8.921 -1.356 34.050 1.00 19.58 ? 435 ALA A N 1 ATOM 3462 C CA . ALA A 1 435 ? -9.920 -0.628 33.330 1.00 19.69 ? 435 ALA A CA 1 ATOM 3463 C C . ALA A 1 435 ? -9.293 0.463 32.479 1.00 17.73 ? 435 ALA A C 1 ATOM 3464 O O . ALA A 1 435 ? -9.750 0.708 31.352 1.00 16.64 ? 435 ALA A O 1 ATOM 3465 C CB . ALA A 1 435 ? -10.929 0.015 34.309 1.00 22.44 ? 435 ALA A CB 1 ATOM 3466 N N . ILE A 1 436 ? -8.335 1.142 33.041 1.00 14.89 ? 436 ILE A N 1 ATOM 3467 C CA . ILE A 1 436 ? -7.664 2.238 32.367 1.00 16.34 ? 436 ILE A CA 1 ATOM 3468 C C . ILE A 1 436 ? -6.913 1.733 31.116 1.00 15.38 ? 436 ILE A C 1 ATOM 3469 O O . ILE A 1 436 ? -6.982 2.332 30.042 1.00 15.67 ? 436 ILE A O 1 ATOM 3470 C CB . ILE A 1 436 ? -6.681 2.936 33.279 1.00 16.81 ? 436 ILE A CB 1 ATOM 3471 C CG1 . ILE A 1 436 ? -7.402 3.784 34.320 1.00 19.23 ? 436 ILE A CG1 1 ATOM 3472 C CG2 . ILE A 1 436 ? -5.748 3.823 32.488 1.00 17.25 ? 436 ILE A CG2 1 ATOM 3473 C CD1 . ILE A 1 436 ? -6.448 4.315 35.394 1.00 17.60 ? 436 ILE A CD1 1 ATOM 3474 N N . ASN A 1 437 ? -6.269 0.592 31.250 1.00 15.88 ? 437 ASN A N 1 ATOM 3475 C CA . ASN A 1 437 ? -5.595 -0.043 30.122 1.00 15.82 ? 437 ASN A CA 1 ATOM 3476 C C . ASN A 1 437 ? -6.593 -0.363 28.989 1.00 15.25 ? 437 ASN A C 1 ATOM 3477 O O . ASN A 1 437 ? -6.313 -0.169 27.792 1.00 15.55 ? 437 ASN A O 1 ATOM 3478 C CB . ASN A 1 437 ? -4.931 -1.330 30.526 1.00 14.91 ? 437 ASN A CB 1 ATOM 3479 C CG . ASN A 1 437 ? -3.713 -1.163 31.397 1.00 14.43 ? 437 ASN A CG 1 ATOM 3480 O OD1 . ASN A 1 437 ? -3.037 -0.159 31.418 1.00 16.02 ? 437 ASN A OD1 1 ATOM 3481 N ND2 . ASN A 1 437 ? -3.323 -2.272 32.008 1.00 15.15 ? 437 ASN A ND2 1 ATOM 3482 N N . LEU A 1 438 ? -7.736 -0.939 29.356 1.00 14.49 ? 438 LEU A N 1 ATOM 3483 C CA . LEU A 1 438 ? -8.766 -1.261 28.377 1.00 13.79 ? 438 LEU A CA 1 ATOM 3484 C C . LEU A 1 438 ? -9.321 -0.028 27.724 1.00 14.25 ? 438 LEU A C 1 ATOM 3485 O O . LEU A 1 438 ? -9.513 0.003 26.499 1.00 15.61 ? 438 LEU A O 1 ATOM 3486 C CB . LEU A 1 438 ? -9.836 -2.108 28.993 1.00 13.50 ? 438 LEU A CB 1 ATOM 3487 C CG . LEU A 1 438 ? -9.425 -3.511 29.428 1.00 16.07 ? 438 LEU A CG 1 ATOM 3488 C CD1 . LEU A 1 438 ? -10.554 -4.102 30.283 1.00 18.04 ? 438 LEU A CD1 1 ATOM 3489 C CD2 . LEU A 1 438 ? -9.136 -4.429 28.241 1.00 16.69 ? 438 LEU A CD2 1 ATOM 3490 N N . GLN A 1 439 ? -9.598 0.999 28.532 1.00 14.28 ? 439 GLN A N 1 ATOM 3491 C CA . GLN A 1 439 ? -10.137 2.224 28.021 1.00 15.41 ? 439 GLN A CA 1 ATOM 3492 C C . GLN A 1 439 ? -9.138 2.837 27.046 1.00 16.51 ? 439 GLN A C 1 ATOM 3493 O O . GLN A 1 439 ? -9.508 3.439 25.993 1.00 15.97 ? 439 GLN A O 1 ATOM 3494 C CB . GLN A 1 439 ? -10.509 3.173 29.173 1.00 15.91 ? 439 GLN A CB 1 ATOM 3495 C CG . GLN A 1 439 ? -11.346 4.378 28.721 1.00 16.04 ? 439 GLN A CG 1 ATOM 3496 C CD . GLN A 1 439 ? -12.842 4.093 28.641 1.00 17.37 ? 439 GLN A CD 1 ATOM 3497 O OE1 . GLN A 1 439 ? -13.294 2.974 28.390 1.00 17.51 ? 439 GLN A OE1 1 ATOM 3498 N NE2 . GLN A 1 439 ? -13.626 5.139 28.823 1.00 17.93 ? 439 GLN A NE2 1 ATOM 3499 N N . ARG A 1 440 ? -7.869 2.722 27.416 1.00 15.91 ? 440 ARG A N 1 ATOM 3500 C CA . ARG A 1 440 ? -6.777 3.300 26.684 1.00 15.41 ? 440 ARG A CA 1 ATOM 3501 C C . ARG A 1 440 ? -6.541 2.634 25.323 1.00 16.45 ? 440 ARG A C 1 ATOM 3502 O O . ARG A 1 440 ? -6.203 3.328 24.340 1.00 15.46 ? 440 ARG A O 1 ATOM 3503 C CB . ARG A 1 440 ? -5.487 3.236 27.496 1.00 15.04 ? 440 ARG A CB 1 ATOM 3504 C CG . ARG A 1 440 ? -4.363 4.048 26.868 1.00 14.83 ? 440 ARG A CG 1 ATOM 3505 C CD . ARG A 1 440 ? -4.528 5.554 26.992 1.00 15.97 ? 440 ARG A CD 1 ATOM 3506 N NE . ARG A 1 440 ? -4.443 6.064 28.360 1.00 15.19 ? 440 ARG A NE 1 ATOM 3507 C CZ . ARG A 1 440 ? -4.847 7.278 28.730 1.00 19.01 ? 440 ARG A CZ 1 ATOM 3508 N NH1 . ARG A 1 440 ? -5.511 8.120 27.876 1.00 18.32 ? 440 ARG A NH1 1 ATOM 3509 N NH2 . ARG A 1 440 ? -4.673 7.644 30.012 1.00 18.00 ? 440 ARG A NH2 1 ATOM 3510 N N . CYS A 1 441 ? -6.664 1.303 25.283 1.00 14.46 ? 441 CYS A N 1 ATOM 3511 C CA . CYS A 1 441 ? -6.667 0.581 24.014 1.00 14.95 ? 441 CYS A CA 1 ATOM 3512 C C . CYS A 1 441 ? -7.630 1.214 22.986 1.00 14.22 ? 441 CYS A C 1 ATOM 3513 O O . CYS A 1 441 ? -7.334 1.366 21.797 1.00 14.38 ? 441 CYS A O 1 ATOM 3514 C CB . CYS A 1 441 ? -7.088 -0.900 24.205 1.00 13.81 ? 441 CYS A CB 1 ATOM 3515 S SG . CYS A 1 441 ? -5.846 -1.978 24.978 1.00 15.67 ? 441 CYS A SG 1 ATOM 3516 N N . ARG A 1 442 ? -8.808 1.550 23.463 1.00 15.44 ? 442 ARG A N 1 ATOM 3517 C CA . ARG A 1 442 ? -9.891 2.121 22.663 1.00 14.58 ? 442 ARG A CA 1 ATOM 3518 C C . ARG A 1 442 ? -9.580 3.588 22.245 1.00 16.36 ? 442 ARG A C 1 ATOM 3519 O O . ARG A 1 442 ? -9.759 3.983 21.062 1.00 15.39 ? 442 ARG A O 1 ATOM 3520 C CB . ARG A 1 442 ? -11.149 2.089 23.462 1.00 14.79 ? 442 ARG A CB 1 ATOM 3521 C CG . ARG A 1 442 ? -11.593 0.671 23.761 1.00 13.99 ? 442 ARG A CG 1 ATOM 3522 C CD . ARG A 1 442 ? -12.756 0.504 24.729 1.00 13.93 ? 442 ARG A CD 1 ATOM 3523 N NE . ARG A 1 442 ? -13.049 -0.892 25.027 1.00 13.18 ? 442 ARG A NE 1 ATOM 3524 C CZ . ARG A 1 442 ? -13.983 -1.322 25.876 1.00 15.15 ? 442 ARG A CZ 1 ATOM 3525 N NH1 . ARG A 1 442 ? -14.752 -0.477 26.545 1.00 15.34 ? 442 ARG A NH1 1 ATOM 3526 N NH2 . ARG A 1 442 ? -14.171 -2.629 26.053 1.00 13.72 ? 442 ARG A NH2 1 ATOM 3527 N N . ASP A 1 443 ? -9.078 4.349 23.217 1.00 16.30 ? 443 ASP A N 1 ATOM 3528 C CA . ASP A 1 443 ? -8.526 5.701 23.011 1.00 17.23 ? 443 ASP A CA 1 ATOM 3529 C C . ASP A 1 443 ? -7.499 5.693 21.854 1.00 16.09 ? 443 ASP A C 1 ATOM 3530 O O . ASP A 1 443 ? -7.540 6.544 20.945 1.00 16.47 ? 443 ASP A O 1 ATOM 3531 C CB . ASP A 1 443 ? -7.862 6.171 24.309 1.00 16.89 ? 443 ASP A CB 1 ATOM 3532 C CG . ASP A 1 443 ? -7.266 7.544 24.200 1.00 16.96 ? 443 ASP A CG 1 ATOM 3533 O OD1 . ASP A 1 443 ? -7.643 8.304 23.249 1.00 17.27 ? 443 ASP A OD1 1 ATOM 3534 O OD2 . ASP A 1 443 ? -6.431 7.878 25.094 1.00 15.62 ? 443 ASP A OD2 1 ATOM 3535 N N . HIS A 1 444 ? -6.647 4.674 21.844 1.00 16.85 ? 444 HIS A N 1 ATOM 3536 C CA . HIS A 1 444 ? -5.545 4.639 20.888 1.00 16.66 ? 444 HIS A CA 1 ATOM 3537 C C . HIS A 1 444 ? -5.923 3.974 19.560 1.00 16.17 ? 444 HIS A C 1 ATOM 3538 O O . HIS A 1 444 ? -5.055 3.766 18.707 1.00 19.61 ? 444 HIS A O 1 ATOM 3539 C CB . HIS A 1 444 ? -4.357 3.903 21.468 1.00 15.35 ? 444 HIS A CB 1 ATOM 3540 C CG . HIS A 1 444 ? -3.481 4.707 22.364 1.00 14.10 ? 444 HIS A CG 1 ATOM 3541 N ND1 . HIS A 1 444 ? -2.121 4.631 22.325 1.00 15.41 ? 444 HIS A ND1 1 ATOM 3542 C CD2 . HIS A 1 444 ? -3.775 5.488 23.422 1.00 15.44 ? 444 HIS A CD2 1 ATOM 3543 C CE1 . HIS A 1 444 ? -1.604 5.439 23.243 1.00 15.41 ? 444 HIS A CE1 1 ATOM 3544 N NE2 . HIS A 1 444 ? -2.594 5.943 23.945 1.00 14.56 ? 444 HIS A NE2 1 ATOM 3545 N N . GLY A 1 445 ? -7.150 3.614 19.376 1.00 15.15 ? 445 GLY A N 1 ATOM 3546 C CA . GLY A 1 445 ? -7.549 3.039 18.124 1.00 16.44 ? 445 GLY A CA 1 ATOM 3547 C C . GLY A 1 445 ? -7.054 1.632 17.849 1.00 16.14 ? 445 GLY A C 1 ATOM 3548 O O . GLY A 1 445 ? -6.819 1.219 16.690 1.00 15.21 ? 445 GLY A O 1 ATOM 3549 N N . MET A 1 446 ? -6.889 0.866 18.915 1.00 16.03 ? 446 MET A N 1 ATOM 3550 C CA . MET A 1 446 ? -6.453 -0.519 18.732 1.00 16.62 ? 446 MET A CA 1 ATOM 3551 C C . MET A 1 446 ? -7.425 -1.391 17.958 1.00 16.17 ? 446 MET A C 1 ATOM 3552 O O . MET A 1 446 ? -8.616 -1.566 18.317 1.00 17.71 ? 446 MET A O 1 ATOM 3553 C CB . MET A 1 446 ? -6.100 -1.166 20.073 1.00 15.59 ? 446 MET A CB 1 ATOM 3554 C CG . MET A 1 446 ? -4.859 -0.586 20.713 1.00 15.83 ? 446 MET A CG 1 ATOM 3555 S SD . MET A 1 446 ? -3.369 -0.916 19.721 1.00 15.39 ? 446 MET A SD 1 ATOM 3556 C CE . MET A 1 446 ? -3.151 0.733 19.066 1.00 17.72 ? 446 MET A CE 1 ATOM 3557 N N . PRO A 1 447 ? -6.920 -1.978 16.853 1.00 16.15 ? 447 PRO A N 1 ATOM 3558 C CA . PRO A 1 447 ? -7.513 -3.190 16.360 1.00 15.76 ? 447 PRO A CA 1 ATOM 3559 C C . PRO A 1 447 ? -7.646 -4.244 17.474 1.00 14.43 ? 447 PRO A C 1 ATOM 3560 O O . PRO A 1 447 ? -6.890 -4.231 18.462 1.00 13.69 ? 447 PRO A O 1 ATOM 3561 C CB . PRO A 1 447 ? -6.474 -3.700 15.316 1.00 16.68 ? 447 PRO A CB 1 ATOM 3562 C CG . PRO A 1 447 ? -5.647 -2.517 14.993 1.00 17.75 ? 447 PRO A CG 1 ATOM 3563 C CD . PRO A 1 447 ? -5.583 -1.768 16.288 1.00 17.86 ? 447 PRO A CD 1 ATOM 3564 N N . GLY A 1 448 ? -8.600 -5.136 17.269 1.00 15.59 ? 448 GLY A N 1 ATOM 3565 C CA . GLY A 1 448 ? -8.978 -6.095 18.247 1.00 15.57 ? 448 GLY A CA 1 ATOM 3566 C C . GLY A 1 448 ? -8.046 -7.291 18.223 1.00 17.44 ? 448 GLY A C 1 ATOM 3567 O O . GLY A 1 448 ? -7.156 -7.383 17.419 1.00 15.74 ? 448 GLY A O 1 ATOM 3568 N N . TYR A 1 449 ? -8.291 -8.184 19.183 1.00 18.50 ? 449 TYR A N 1 ATOM 3569 C CA . TYR A 1 449 ? -7.576 -9.438 19.384 1.00 16.30 ? 449 TYR A CA 1 ATOM 3570 C C . TYR A 1 449 ? -7.323 -10.267 18.136 1.00 15.81 ? 449 TYR A C 1 ATOM 3571 O O . TYR A 1 449 ? -6.157 -10.626 17.843 1.00 17.35 ? 449 TYR A O 1 ATOM 3572 C CB . TYR A 1 449 ? -8.367 -10.271 20.380 1.00 16.81 ? 449 TYR A CB 1 ATOM 3573 C CG . TYR A 1 449 ? -7.748 -11.578 20.707 1.00 16.20 ? 449 TYR A CG 1 ATOM 3574 C CD1 . TYR A 1 449 ? -6.529 -11.655 21.358 1.00 16.32 ? 449 TYR A CD1 1 ATOM 3575 C CD2 . TYR A 1 449 ? -8.415 -12.768 20.401 1.00 17.05 ? 449 TYR A CD2 1 ATOM 3576 C CE1 . TYR A 1 449 ? -5.946 -12.907 21.660 1.00 16.45 ? 449 TYR A CE1 1 ATOM 3577 C CE2 . TYR A 1 449 ? -7.838 -14.023 20.658 1.00 15.62 ? 449 TYR A CE2 1 ATOM 3578 C CZ . TYR A 1 449 ? -6.654 -14.097 21.314 1.00 17.84 ? 449 TYR A CZ 1 ATOM 3579 O OH . TYR A 1 449 ? -6.109 -15.339 21.587 1.00 21.11 ? 449 TYR A OH 1 ATOM 3580 N N . ASN A 1 450 ? -8.355 -10.558 17.387 1.00 17.27 ? 450 ASN A N 1 ATOM 3581 C CA . ASN A 1 450 ? -8.169 -11.350 16.149 1.00 18.78 ? 450 ASN A CA 1 ATOM 3582 C C . ASN A 1 450 ? -7.383 -10.659 15.053 1.00 18.18 ? 450 ASN A C 1 ATOM 3583 O O . ASN A 1 450 ? -6.687 -11.356 14.322 1.00 18.94 ? 450 ASN A O 1 ATOM 3584 C CB . ASN A 1 450 ? -9.498 -11.916 15.595 1.00 19.67 ? 450 ASN A CB 1 ATOM 3585 C CG . ASN A 1 450 ? -9.917 -13.212 16.290 1.00 20.71 ? 450 ASN A CG 1 ATOM 3586 O OD1 . ASN A 1 450 ? -9.062 -13.963 16.787 1.00 21.95 ? 450 ASN A OD1 1 ATOM 3587 N ND2 . ASN A 1 450 ? -11.199 -13.487 16.314 1.00 20.43 ? 450 ASN A ND2 1 ATOM 3588 N N . SER A 1 451 ? -7.460 -9.325 14.940 1.00 17.17 ? 451 SER A N 1 ATOM 3589 C CA . SER A 1 451 ? -6.632 -8.626 13.987 1.00 16.29 ? 451 SER A CA 1 ATOM 3590 C C . SER A 1 451 ? -5.208 -8.847 14.306 1.00 16.21 ? 451 SER A C 1 ATOM 3591 O O . SER A 1 451 ? -4.346 -9.073 13.424 1.00 17.24 ? 451 SER A O 1 ATOM 3592 C CB . SER A 1 451 ? -6.911 -7.102 14.039 1.00 17.27 ? 451 SER A CB 1 ATOM 3593 O OG . SER A 1 451 ? -8.177 -6.813 13.501 1.00 16.69 ? 451 SER A OG 1 ATOM 3594 N N . TRP A 1 452 ? -4.868 -8.734 15.583 1.00 16.75 ? 452 TRP A N 1 ATOM 3595 C CA . TRP A 1 452 ? -3.479 -8.986 15.960 1.00 15.80 ? 452 TRP A CA 1 ATOM 3596 C C . TRP A 1 452 ? -3.085 -10.504 15.814 1.00 15.11 ? 452 TRP A C 1 ATOM 3597 O O . TRP A 1 452 ? -1.956 -10.822 15.387 1.00 12.94 ? 452 TRP A O 1 ATOM 3598 C CB . TRP A 1 452 ? -3.137 -8.379 17.338 1.00 15.89 ? 452 TRP A CB 1 ATOM 3599 C CG . TRP A 1 452 ? -3.223 -6.912 17.317 1.00 15.69 ? 452 TRP A CG 1 ATOM 3600 C CD1 . TRP A 1 452 ? -4.167 -6.142 17.918 1.00 15.78 ? 452 TRP A CD1 1 ATOM 3601 C CD2 . TRP A 1 452 ? -2.381 -6.016 16.573 1.00 15.12 ? 452 TRP A CD2 1 ATOM 3602 N NE1 . TRP A 1 452 ? -3.912 -4.799 17.641 1.00 15.04 ? 452 TRP A NE1 1 ATOM 3603 C CE2 . TRP A 1 452 ? -2.830 -4.715 16.811 1.00 13.67 ? 452 TRP A CE2 1 ATOM 3604 C CE3 . TRP A 1 452 ? -1.255 -6.203 15.747 1.00 16.00 ? 452 TRP A CE3 1 ATOM 3605 C CZ2 . TRP A 1 452 ? -2.245 -3.611 16.218 1.00 15.47 ? 452 TRP A CZ2 1 ATOM 3606 C CZ3 . TRP A 1 452 ? -0.680 -5.093 15.137 1.00 15.55 ? 452 TRP A CZ3 1 ATOM 3607 C CH2 . TRP A 1 452 ? -1.155 -3.816 15.403 1.00 14.87 ? 452 TRP A CH2 1 ATOM 3608 N N . ARG A 1 453 ? -3.996 -11.404 16.158 1.00 15.69 ? 453 ARG A N 1 ATOM 3609 C CA . ARG A 1 453 ? -3.726 -12.834 15.960 1.00 17.58 ? 453 ARG A CA 1 ATOM 3610 C C . ARG A 1 453 ? -3.312 -13.066 14.492 1.00 17.98 ? 453 ARG A C 1 ATOM 3611 O O . ARG A 1 453 ? -2.225 -13.620 14.234 1.00 21.15 ? 453 ARG A O 1 ATOM 3612 C CB . ARG A 1 453 ? -4.911 -13.659 16.322 1.00 18.51 ? 453 ARG A CB 1 ATOM 3613 C CG . ARG A 1 453 ? -5.221 -13.773 17.828 1.00 17.78 ? 453 ARG A CG 1 ATOM 3614 C CD . ARG A 1 453 ? -4.313 -14.785 18.478 1.00 18.30 ? 453 ARG A CD 1 ATOM 3615 N NE . ARG A 1 453 ? -4.631 -16.152 18.133 1.00 18.78 ? 453 ARG A NE 1 ATOM 3616 C CZ . ARG A 1 453 ? -4.082 -17.202 18.742 1.00 18.89 ? 453 ARG A CZ 1 ATOM 3617 N NH1 . ARG A 1 453 ? -3.166 -17.088 19.710 1.00 21.23 ? 453 ARG A NH1 1 ATOM 3618 N NH2 . ARG A 1 453 ? -4.367 -18.357 18.309 1.00 19.28 ? 453 ARG A NH2 1 ATOM 3619 N N . GLY A 1 454 ? -4.073 -12.491 13.570 1.00 19.18 ? 454 GLY A N 1 ATOM 3620 C CA . GLY A 1 454 ? -3.843 -12.712 12.122 1.00 21.15 ? 454 GLY A CA 1 ATOM 3621 C C . GLY A 1 454 ? -2.534 -12.062 11.679 1.00 19.91 ? 454 GLY A C 1 ATOM 3622 O O . GLY A 1 454 ? -1.817 -12.604 10.919 1.00 20.34 ? 454 GLY A O 1 ATOM 3623 N N . PHE A 1 455 ? -2.207 -10.918 12.220 1.00 20.49 ? 455 PHE A N 1 ATOM 3624 C CA . PHE A 1 455 ? -0.953 -10.226 11.908 1.00 19.72 ? 455 PHE A CA 1 ATOM 3625 C C . PHE A 1 455 ? 0.212 -11.112 12.274 1.00 20.90 ? 455 PHE A C 1 ATOM 3626 O O . PHE A 1 455 ? 1.243 -11.038 11.633 1.00 18.83 ? 455 PHE A O 1 ATOM 3627 C CB . PHE A 1 455 ? -0.935 -8.889 12.672 1.00 19.78 ? 455 PHE A CB 1 ATOM 3628 C CG . PHE A 1 455 ? 0.373 -8.122 12.599 1.00 21.32 ? 455 PHE A CG 1 ATOM 3629 C CD1 . PHE A 1 455 ? 0.572 -7.187 11.610 1.00 19.57 ? 455 PHE A CD1 1 ATOM 3630 C CD2 . PHE A 1 455 ? 1.358 -8.296 13.563 1.00 20.28 ? 455 PHE A CD2 1 ATOM 3631 C CE1 . PHE A 1 455 ? 1.760 -6.496 11.542 1.00 19.41 ? 455 PHE A CE1 1 ATOM 3632 C CE2 . PHE A 1 455 ? 2.546 -7.584 13.499 1.00 19.81 ? 455 PHE A CE2 1 ATOM 3633 C CZ . PHE A 1 455 ? 2.742 -6.675 12.499 1.00 19.70 ? 455 PHE A CZ 1 ATOM 3634 N N . CYS A 1 456 ? 0.038 -11.875 13.344 1.00 19.22 ? 456 CYS A N 1 ATOM 3635 C CA . CYS A 1 456 ? 1.086 -12.706 13.894 1.00 19.91 ? 456 CYS A CA 1 ATOM 3636 C C . CYS A 1 456 ? 1.009 -14.119 13.332 1.00 20.17 ? 456 CYS A C 1 ATOM 3637 O O . CYS A 1 456 ? 1.734 -14.978 13.796 1.00 23.53 ? 456 CYS A O 1 ATOM 3638 C CB . CYS A 1 456 ? 0.926 -12.763 15.416 1.00 20.09 ? 456 CYS A CB 1 ATOM 3639 S SG . CYS A 1 456 ? 1.599 -11.260 16.203 1.00 20.88 ? 456 CYS A SG 1 ATOM 3640 N N . GLY A 1 457 ? 0.151 -14.335 12.348 1.00 20.80 ? 457 GLY A N 1 ATOM 3641 C CA . GLY A 1 457 ? 0.069 -15.612 11.681 1.00 24.81 ? 457 GLY A CA 1 ATOM 3642 C C . GLY A 1 457 ? -0.577 -16.691 12.538 1.00 26.18 ? 457 GLY A C 1 ATOM 3643 O O . GLY A 1 457 ? -0.201 -17.869 12.422 1.00 27.26 ? 457 GLY A O 1 ATOM 3644 N N . LEU A 1 458 ? -1.479 -16.277 13.466 1.00 26.00 ? 458 LEU A N 1 ATOM 3645 C CA . LEU A 1 458 ? -2.094 -17.169 14.416 1.00 22.10 ? 458 LEU A CA 1 ATOM 3646 C C . LEU A 1 458 ? -3.563 -17.313 14.111 1.00 23.10 ? 458 LEU A C 1 ATOM 3647 O O . LEU A 1 458 ? -4.186 -16.448 13.515 1.00 19.81 ? 458 LEU A O 1 ATOM 3648 C CB . LEU A 1 458 ? -1.899 -16.652 15.859 1.00 22.40 ? 458 LEU A CB 1 ATOM 3649 C CG . LEU A 1 458 ? -0.472 -16.459 16.355 1.00 22.30 ? 458 LEU A CG 1 ATOM 3650 C CD1 . LEU A 1 458 ? -0.431 -15.681 17.654 1.00 24.54 ? 458 LEU A CD1 1 ATOM 3651 C CD2 . LEU A 1 458 ? 0.221 -17.789 16.569 1.00 22.27 ? 458 LEU A CD2 1 ATOM 3652 N N . SER A 1 459 ? -4.145 -18.424 14.505 1.00 24.15 ? 459 SER A N 1 ATOM 3653 C CA . SER A 1 459 ? -5.553 -18.630 14.292 1.00 25.47 ? 459 SER A CA 1 ATOM 3654 C C . SER A 1 459 ? -6.417 -17.569 14.971 1.00 24.14 ? 459 SER A C 1 ATOM 3655 O O . SER A 1 459 ? -6.069 -17.017 16.017 1.00 25.81 ? 459 SER A O 1 ATOM 3656 C CB . SER A 1 459 ? -5.982 -20.062 14.725 1.00 26.52 ? 459 SER A CB 1 ATOM 3657 O OG . SER A 1 459 ? -6.120 -20.138 16.136 1.00 29.08 ? 459 SER A OG 1 ATOM 3658 N N . GLN A 1 460 ? -7.549 -17.309 14.357 1.00 21.09 ? 460 GLN A N 1 ATOM 3659 C CA . GLN A 1 460 ? -8.479 -16.341 14.788 1.00 22.41 ? 460 GLN A CA 1 ATOM 3660 C C . GLN A 1 460 ? -9.765 -17.022 15.252 1.00 23.35 ? 460 GLN A C 1 ATOM 3661 O O . GLN A 1 460 ? -10.677 -17.244 14.453 1.00 21.25 ? 460 GLN A O 1 ATOM 3662 C CB . GLN A 1 460 ? -8.750 -15.405 13.605 1.00 27.09 ? 460 GLN A CB 1 ATOM 3663 C CG . GLN A 1 460 ? -7.571 -14.497 13.304 1.00 29.29 ? 460 GLN A CG 1 ATOM 3664 C CD . GLN A 1 460 ? -7.729 -13.747 11.990 1.00 32.24 ? 460 GLN A CD 1 ATOM 3665 O OE1 . GLN A 1 460 ? -8.536 -12.806 11.906 1.00 43.01 ? 460 GLN A OE1 1 ATOM 3666 N NE2 . GLN A 1 460 ? -6.991 -14.135 10.984 1.00 33.14 ? 460 GLN A NE2 1 ATOM 3667 N N . PRO A 1 461 ? -9.870 -17.369 16.555 1.00 22.14 ? 461 PRO A N 1 ATOM 3668 C CA . PRO A 1 461 ? -11.143 -18.045 16.906 1.00 22.88 ? 461 PRO A CA 1 ATOM 3669 C C . PRO A 1 461 ? -12.370 -17.170 16.704 1.00 25.97 ? 461 PRO A C 1 ATOM 3670 O O . PRO A 1 461 ? -12.342 -15.923 16.936 1.00 24.64 ? 461 PRO A O 1 ATOM 3671 C CB . PRO A 1 461 ? -10.978 -18.365 18.397 1.00 22.44 ? 461 PRO A CB 1 ATOM 3672 C CG . PRO A 1 461 ? -9.992 -17.306 18.877 1.00 22.20 ? 461 PRO A CG 1 ATOM 3673 C CD . PRO A 1 461 ? -9.013 -17.157 17.730 1.00 20.58 ? 461 PRO A CD 1 ATOM 3674 N N . LYS A 1 462 ? -13.475 -17.820 16.323 1.00 26.71 ? 462 LYS A N 1 ATOM 3675 C CA . LYS A 1 462 ? -14.741 -17.128 16.149 1.00 26.52 ? 462 LYS A CA 1 ATOM 3676 C C . LYS A 1 462 ? -15.815 -17.578 17.095 1.00 29.38 ? 462 LYS A C 1 ATOM 3677 O O . LYS A 1 462 ? -16.775 -16.862 17.274 1.00 26.62 ? 462 LYS A O 1 ATOM 3678 C CB . LYS A 1 462 ? -15.276 -17.245 14.703 1.00 28.75 ? 462 LYS A CB 1 ATOM 3679 C CG . LYS A 1 462 ? -14.251 -16.851 13.664 1.00 29.07 ? 462 LYS A CG 1 ATOM 3680 C CD . LYS A 1 462 ? -13.989 -15.339 13.634 1.00 27.93 ? 462 LYS A CD 1 ATOM 3681 C CE . LYS A 1 462 ? -12.873 -14.994 12.645 1.00 28.81 ? 462 LYS A CE 1 ATOM 3682 N NZ . LYS A 1 462 ? -12.532 -13.553 12.554 1.00 29.71 ? 462 LYS A NZ 1 ATOM 3683 N N . THR A 1 463 ? -15.706 -18.765 17.689 1.00 27.70 ? 463 THR A N 1 ATOM 3684 C CA . THR A 1 463 ? -16.796 -19.256 18.497 1.00 25.73 ? 463 THR A CA 1 ATOM 3685 C C . THR A 1 463 ? -16.259 -19.519 19.912 1.00 28.15 ? 463 THR A C 1 ATOM 3686 O O . THR A 1 463 ? -15.060 -19.563 20.109 1.00 28.94 ? 463 THR A O 1 ATOM 3687 C CB . THR A 1 463 ? -17.268 -20.591 17.945 1.00 25.59 ? 463 THR A CB 1 ATOM 3688 O OG1 . THR A 1 463 ? -16.142 -21.483 17.932 1.00 25.69 ? 463 THR A OG1 1 ATOM 3689 C CG2 . THR A 1 463 ? -17.842 -20.428 16.503 1.00 25.03 ? 463 THR A CG2 1 ATOM 3690 N N . LEU A 1 464 ? -17.155 -19.780 20.853 1.00 30.35 ? 464 LEU A N 1 ATOM 3691 C CA . LEU A 1 464 ? -16.780 -20.229 22.186 1.00 29.38 ? 464 LEU A CA 1 ATOM 3692 C C . LEU A 1 464 ? -15.824 -21.371 22.111 1.00 29.38 ? 464 LEU A C 1 ATOM 3693 O O . LEU A 1 464 ? -14.763 -21.358 22.729 1.00 29.61 ? 464 LEU A O 1 ATOM 3694 C CB . LEU A 1 464 ? -18.016 -20.625 22.988 1.00 30.86 ? 464 LEU A CB 1 ATOM 3695 C CG . LEU A 1 464 ? -17.755 -21.013 24.464 1.00 33.08 ? 464 LEU A CG 1 ATOM 3696 C CD1 . LEU A 1 464 ? -17.035 -19.915 25.259 1.00 30.89 ? 464 LEU A CD1 1 ATOM 3697 C CD2 . LEU A 1 464 ? -19.099 -21.340 25.131 1.00 34.69 ? 464 LEU A CD2 1 ATOM 3698 N N . LYS A 1 465 ? -16.149 -22.360 21.297 1.00 32.68 ? 465 LYS A N 1 ATOM 3699 C CA . LYS A 1 465 ? -15.322 -23.532 21.179 1.00 32.18 ? 465 LYS A CA 1 ATOM 3700 C C . LYS A 1 465 ? -13.900 -23.240 20.717 1.00 32.08 ? 465 LYS A C 1 ATOM 3701 O O . LYS A 1 465 ? -12.941 -23.723 21.282 1.00 32.67 ? 465 LYS A O 1 ATOM 3702 C CB . LYS A 1 465 ? -15.964 -24.507 20.191 1.00 38.05 ? 465 LYS A CB 1 ATOM 3703 C CG . LYS A 1 465 ? -15.618 -25.933 20.514 1.00 42.24 ? 465 LYS A CG 1 ATOM 3704 C CD . LYS A 1 465 ? -16.190 -26.938 19.514 1.00 49.15 ? 465 LYS A CD 1 ATOM 3705 C CE . LYS A 1 465 ? -15.833 -28.372 19.909 1.00 53.12 ? 465 LYS A CE 1 ATOM 3706 N NZ . LYS A 1 465 ? -15.244 -29.130 18.764 1.00 54.73 ? 465 LYS A NZ 1 ATOM 3707 N N . GLY A 1 466 ? -13.752 -22.443 19.666 1.00 31.24 ? 466 GLY A N 1 ATOM 3708 C CA . GLY A 1 466 ? -12.407 -22.022 19.234 1.00 25.62 ? 466 GLY A CA 1 ATOM 3709 C C . GLY A 1 466 ? -11.640 -21.188 20.289 1.00 21.74 ? 466 GLY A C 1 ATOM 3710 O O . GLY A 1 466 ? -10.463 -21.348 20.452 1.00 21.96 ? 466 GLY A O 1 ATOM 3711 N N . LEU A 1 467 ? -12.310 -20.324 21.000 1.00 21.76 ? 467 LEU A N 1 ATOM 3712 C CA . LEU A 1 467 ? -11.615 -19.484 21.964 1.00 25.26 ? 467 LEU A CA 1 ATOM 3713 C C . LEU A 1 467 ? -11.177 -20.318 23.190 1.00 25.58 ? 467 LEU A C 1 ATOM 3714 O O . LEU A 1 467 ? -10.064 -20.171 23.704 1.00 23.74 ? 467 LEU A O 1 ATOM 3715 C CB . LEU A 1 467 ? -12.490 -18.312 22.352 1.00 25.77 ? 467 LEU A CB 1 ATOM 3716 C CG . LEU A 1 467 ? -11.884 -17.299 23.320 1.00 26.69 ? 467 LEU A CG 1 ATOM 3717 C CD1 . LEU A 1 467 ? -10.709 -16.543 22.695 1.00 26.57 ? 467 LEU A CD1 1 ATOM 3718 C CD2 . LEU A 1 467 ? -12.972 -16.326 23.794 1.00 24.43 ? 467 LEU A CD2 1 ATOM 3719 N N . GLN A 1 468 ? -12.039 -21.236 23.613 1.00 29.90 ? 468 GLN A N 1 ATOM 3720 C CA . GLN A 1 468 ? -11.688 -22.165 24.681 1.00 31.46 ? 468 GLN A CA 1 ATOM 3721 C C . GLN A 1 468 ? -10.364 -22.865 24.370 1.00 29.37 ? 468 GLN A C 1 ATOM 3722 O O . GLN A 1 468 ? -9.474 -22.935 25.218 1.00 30.68 ? 468 GLN A O 1 ATOM 3723 C CB . GLN A 1 468 ? -12.798 -23.198 24.880 1.00 36.59 ? 468 GLN A CB 1 ATOM 3724 C CG . GLN A 1 468 ? -14.143 -22.600 25.260 1.00 43.18 ? 468 GLN A CG 1 ATOM 3725 C CD . GLN A 1 468 ? -15.223 -23.648 25.461 1.00 52.13 ? 468 GLN A CD 1 ATOM 3726 O OE1 . GLN A 1 468 ? -16.305 -23.348 25.966 1.00 60.38 ? 468 GLN A OE1 1 ATOM 3727 N NE2 . GLN A 1 468 ? -14.936 -24.884 25.066 1.00 47.68 ? 468 GLN A NE2 1 ATOM 3728 N N . ALA A 1 469 ? -10.243 -23.380 23.149 1.00 27.64 ? 469 ALA A N 1 ATOM 3729 C CA . ALA A 1 469 ? -9.028 -24.049 22.703 1.00 26.91 ? 469 ALA A CA 1 ATOM 3730 C C . ALA A 1 469 ? -7.825 -23.152 22.696 1.00 25.18 ? 469 ALA A C 1 ATOM 3731 O O . ALA A 1 469 ? -6.710 -23.590 23.064 1.00 29.01 ? 469 ALA A O 1 ATOM 3732 C CB . ALA A 1 469 ? -9.226 -24.659 21.306 1.00 29.36 ? 469 ALA A CB 1 ATOM 3733 N N . VAL A 1 470 ? -7.958 -21.891 22.291 1.00 23.07 ? 470 VAL A N 1 ATOM 3734 C CA . VAL A 1 470 ? -6.745 -21.010 22.296 1.00 21.28 ? 470 VAL A CA 1 ATOM 3735 C C . VAL A 1 470 ? -6.284 -20.660 23.721 1.00 18.84 ? 470 VAL A C 1 ATOM 3736 O O . VAL A 1 470 ? -5.110 -20.557 24.022 1.00 19.52 ? 470 VAL A O 1 ATOM 3737 C CB . VAL A 1 470 ? -7.040 -19.722 21.484 1.00 22.44 ? 470 VAL A CB 1 ATOM 3738 C CG1 . VAL A 1 470 ? -5.916 -18.690 21.634 1.00 20.57 ? 470 VAL A CG1 1 ATOM 3739 C CG2 . VAL A 1 470 ? -7.233 -20.100 20.010 1.00 23.35 ? 470 VAL A CG2 1 ATOM 3740 N N . LEU A 1 471 ? -7.240 -20.466 24.608 1.00 21.18 ? 471 LEU A N 1 ATOM 3741 C CA . LEU A 1 471 ? -6.984 -20.009 25.982 1.00 21.47 ? 471 LEU A CA 1 ATOM 3742 C C . LEU A 1 471 ? -6.830 -21.184 26.945 1.00 23.27 ? 471 LEU A C 1 ATOM 3743 O O . LEU A 1 471 ? -6.331 -21.021 28.061 1.00 19.40 ? 471 LEU A O 1 ATOM 3744 C CB . LEU A 1 471 ? -8.099 -19.149 26.482 1.00 20.88 ? 471 LEU A CB 1 ATOM 3745 C CG . LEU A 1 471 ? -8.388 -17.882 25.672 1.00 20.99 ? 471 LEU A CG 1 ATOM 3746 C CD1 . LEU A 1 471 ? -9.499 -17.127 26.390 1.00 21.51 ? 471 LEU A CD1 1 ATOM 3747 C CD2 . LEU A 1 471 ? -7.130 -17.026 25.492 1.00 18.54 ? 471 LEU A CD2 1 ATOM 3748 N N . LYS A 1 472 ? -7.194 -22.367 26.464 1.00 28.45 ? 472 LYS A N 1 ATOM 3749 C CA . LYS A 1 472 ? -7.113 -23.608 27.260 1.00 29.44 ? 472 LYS A CA 1 ATOM 3750 C C . LYS A 1 472 ? -7.873 -23.432 28.561 1.00 28.40 ? 472 LYS A C 1 ATOM 3751 O O . LYS A 1 472 ? -7.408 -23.824 29.613 1.00 29.77 ? 472 LYS A O 1 ATOM 3752 C CB . LYS A 1 472 ? -5.660 -23.962 27.509 1.00 29.37 ? 472 LYS A CB 1 ATOM 3753 C CG . LYS A 1 472 ? -5.021 -24.319 26.206 1.00 35.06 ? 472 LYS A CG 1 ATOM 3754 C CD . LYS A 1 472 ? -3.669 -24.952 26.337 1.00 37.06 ? 472 LYS A CD 1 ATOM 3755 C CE . LYS A 1 472 ? -3.378 -25.755 25.071 1.00 41.46 ? 472 LYS A CE 1 ATOM 3756 N NZ . LYS A 1 472 ? -2.116 -26.506 25.227 1.00 43.49 ? 472 LYS A NZ 1 ATOM 3757 N N . ASN A 1 473 ? -9.027 -22.805 28.468 1.00 29.06 ? 473 ASN A N 1 ATOM 3758 C CA . ASN A 1 473 ? -9.794 -22.436 29.627 1.00 29.23 ? 473 ASN A CA 1 ATOM 3759 C C . ASN A 1 473 ? -11.179 -22.057 29.165 1.00 28.38 ? 473 ASN A C 1 ATOM 3760 O O . ASN A 1 473 ? -11.396 -21.030 28.532 1.00 27.66 ? 473 ASN A O 1 ATOM 3761 C CB . ASN A 1 473 ? -9.117 -21.294 30.344 1.00 28.83 ? 473 ASN A CB 1 ATOM 3762 C CG . ASN A 1 473 ? -9.802 -20.896 31.601 1.00 26.44 ? 473 ASN A CG 1 ATOM 3763 O OD1 . ASN A 1 473 ? -11.014 -21.001 31.741 1.00 22.68 ? 473 ASN A OD1 1 ATOM 3764 N ND2 . ASN A 1 473 ? -9.029 -20.267 32.480 1.00 24.94 ? 473 ASN A ND2 1 ATOM 3765 N N . LYS A 1 474 ? -12.160 -22.873 29.566 1.00 32.51 ? 474 LYS A N 1 ATOM 3766 C CA . LYS A 1 474 ? -13.501 -22.808 29.021 1.00 31.84 ? 474 LYS A CA 1 ATOM 3767 C C . LYS A 1 474 ? -14.257 -21.667 29.673 1.00 29.26 ? 474 LYS A C 1 ATOM 3768 O O . LYS A 1 474 ? -15.021 -20.976 29.028 1.00 30.47 ? 474 LYS A O 1 ATOM 3769 C CB . LYS A 1 474 ? -14.197 -24.149 29.249 1.00 40.31 ? 474 LYS A CB 1 ATOM 3770 C CG . LYS A 1 474 ? -15.591 -24.287 28.647 1.00 48.71 ? 474 LYS A CG 1 ATOM 3771 C CD . LYS A 1 474 ? -15.790 -25.682 28.046 1.00 54.94 ? 474 LYS A CD 1 ATOM 3772 C CE . LYS A 1 474 ? -17.241 -26.128 28.154 1.00 62.57 ? 474 LYS A CE 1 ATOM 3773 N NZ . LYS A 1 474 ? -17.493 -27.489 27.566 1.00 60.44 ? 474 LYS A NZ 1 ATOM 3774 N N . VAL A 1 475 ? -14.037 -21.484 30.955 1.00 28.14 ? 475 VAL A N 1 ATOM 3775 C CA . VAL A 1 475 ? -14.740 -20.496 31.760 1.00 27.07 ? 475 VAL A CA 1 ATOM 3776 C C . VAL A 1 475 ? -14.273 -19.106 31.389 1.00 26.97 ? 475 VAL A C 1 ATOM 3777 O O . VAL A 1 475 ? -15.075 -18.164 31.331 1.00 25.08 ? 475 VAL A O 1 ATOM 3778 C CB . VAL A 1 475 ? -14.454 -20.721 33.287 1.00 28.90 ? 475 VAL A CB 1 ATOM 3779 C CG1 . VAL A 1 475 ? -15.003 -19.594 34.140 1.00 26.79 ? 475 VAL A CG1 1 ATOM 3780 C CG2 . VAL A 1 475 ? -15.041 -22.068 33.752 1.00 31.07 ? 475 VAL A CG2 1 ATOM 3781 N N . LEU A 1 476 ? -12.969 -18.948 31.221 1.00 26.48 ? 476 LEU A N 1 ATOM 3782 C CA . LEU A 1 476 ? -12.425 -17.619 30.908 1.00 23.28 ? 476 LEU A CA 1 ATOM 3783 C C . LEU A 1 476 ? -13.007 -17.215 29.535 1.00 23.07 ? 476 LEU A C 1 ATOM 3784 O O . LEU A 1 476 ? -13.470 -16.110 29.354 1.00 21.18 ? 476 LEU A O 1 ATOM 3785 C CB . LEU A 1 476 ? -10.882 -17.619 30.944 1.00 22.52 ? 476 LEU A CB 1 ATOM 3786 C CG . LEU A 1 476 ? -10.227 -16.352 30.396 1.00 20.27 ? 476 LEU A CG 1 ATOM 3787 C CD1 . LEU A 1 476 ? -10.735 -15.065 31.063 1.00 23.30 ? 476 LEU A CD1 1 ATOM 3788 C CD2 . LEU A 1 476 ? -8.719 -16.462 30.502 1.00 22.54 ? 476 LEU A CD2 1 ATOM 3789 N N . ALA A 1 477 ? -13.075 -18.176 28.620 1.00 23.82 ? 477 ALA A N 1 ATOM 3790 C CA . ALA A 1 477 ? -13.522 -17.940 27.283 1.00 21.21 ? 477 ALA A CA 1 ATOM 3791 C C . ALA A 1 477 ? -14.980 -17.611 27.264 1.00 23.78 ? 477 ALA A C 1 ATOM 3792 O O . ALA A 1 477 ? -15.427 -16.647 26.597 1.00 24.38 ? 477 ALA A O 1 ATOM 3793 C CB . ALA A 1 477 ? -13.156 -19.112 26.405 1.00 23.31 ? 477 ALA A CB 1 ATOM 3794 N N . LYS A 1 478 ? -15.733 -18.334 28.092 1.00 25.65 ? 478 LYS A N 1 ATOM 3795 C CA . LYS A 1 478 ? -17.116 -18.044 28.346 1.00 25.28 ? 478 LYS A CA 1 ATOM 3796 C C . LYS A 1 478 ? -17.326 -16.623 28.859 1.00 24.73 ? 478 LYS A C 1 ATOM 3797 O O . LYS A 1 478 ? -18.123 -15.871 28.317 1.00 23.56 ? 478 LYS A O 1 ATOM 3798 C CB . LYS A 1 478 ? -17.664 -19.101 29.315 1.00 29.60 ? 478 LYS A CB 1 ATOM 3799 C CG . LYS A 1 478 ? -19.133 -18.978 29.688 1.00 36.52 ? 478 LYS A CG 1 ATOM 3800 C CD . LYS A 1 478 ? -20.044 -19.034 28.480 1.00 42.04 ? 478 LYS A CD 1 ATOM 3801 C CE . LYS A 1 478 ? -21.484 -18.721 28.876 1.00 52.22 ? 478 LYS A CE 1 ATOM 3802 N NZ . LYS A 1 478 ? -22.316 -18.694 27.636 1.00 57.95 ? 478 LYS A NZ 1 ATOM 3803 N N . LYS A 1 479 ? -16.602 -16.240 29.895 1.00 21.85 ? 479 LYS A N 1 ATOM 3804 C CA . LYS A 1 479 ? -16.776 -14.908 30.436 1.00 23.82 ? 479 LYS A CA 1 ATOM 3805 C C . LYS A 1 479 ? -16.387 -13.845 29.394 1.00 21.45 ? 479 LYS A C 1 ATOM 3806 O O . LYS A 1 479 ? -16.976 -12.797 29.370 1.00 22.18 ? 479 LYS A O 1 ATOM 3807 C CB . LYS A 1 479 ? -15.938 -14.705 31.689 1.00 23.43 ? 479 LYS A CB 1 ATOM 3808 C CG . LYS A 1 479 ? -16.345 -15.579 32.886 1.00 27.73 ? 479 LYS A CG 1 ATOM 3809 C CD . LYS A 1 479 ? -15.459 -15.258 34.077 1.00 30.94 ? 479 LYS A CD 1 ATOM 3810 C CE . LYS A 1 479 ? -15.769 -16.135 35.276 1.00 37.83 ? 479 LYS A CE 1 ATOM 3811 N NZ . LYS A 1 479 ? -14.572 -16.227 36.184 1.00 40.79 ? 479 LYS A NZ 1 ATOM 3812 N N . LEU A 1 480 ? -15.341 -14.090 28.614 1.00 21.75 ? 480 LEU A N 1 ATOM 3813 C CA . LEU A 1 480 ? -14.962 -13.111 27.624 1.00 22.10 ? 480 LEU A CA 1 ATOM 3814 C C . LEU A 1 480 ? -16.085 -12.967 26.544 1.00 23.42 ? 480 LEU A C 1 ATOM 3815 O O . LEU A 1 480 ? -16.507 -11.858 26.200 1.00 23.53 ? 480 LEU A O 1 ATOM 3816 C CB . LEU A 1 480 ? -13.629 -13.495 27.023 1.00 20.13 ? 480 LEU A CB 1 ATOM 3817 C CG . LEU A 1 480 ? -12.416 -13.156 27.900 1.00 19.59 ? 480 LEU A CG 1 ATOM 3818 C CD1 . LEU A 1 480 ? -11.196 -13.854 27.343 1.00 19.00 ? 480 LEU A CD1 1 ATOM 3819 C CD2 . LEU A 1 480 ? -12.202 -11.615 27.985 1.00 20.02 ? 480 LEU A CD2 1 ATOM 3820 N N . LEU A 1 481 ? -16.605 -14.088 26.060 1.00 24.13 ? 481 LEU A N 1 ATOM 3821 C CA . LEU A 1 481 ? -17.673 -13.978 25.058 1.00 24.45 ? 481 LEU A CA 1 ATOM 3822 C C . LEU A 1 481 ? -18.947 -13.447 25.609 1.00 23.79 ? 481 LEU A C 1 ATOM 3823 O O . LEU A 1 481 ? -19.650 -12.723 24.909 1.00 21.77 ? 481 LEU A O 1 ATOM 3824 C CB . LEU A 1 481 ? -17.919 -15.297 24.358 1.00 27.15 ? 481 LEU A CB 1 ATOM 3825 C CG . LEU A 1 481 ? -16.719 -15.614 23.481 1.00 29.48 ? 481 LEU A CG 1 ATOM 3826 C CD1 . LEU A 1 481 ? -17.057 -16.869 22.711 1.00 30.25 ? 481 LEU A CD1 1 ATOM 3827 C CD2 . LEU A 1 481 ? -16.369 -14.493 22.526 1.00 31.97 ? 481 LEU A CD2 1 ATOM 3828 N N . ASP A 1 482 ? -19.274 -13.730 26.869 1.00 22.12 ? 482 ASP A N 1 ATOM 3829 C CA . ASP A 1 482 ? -20.443 -13.073 27.435 1.00 23.14 ? 482 ASP A CA 1 ATOM 3830 C C . ASP A 1 482 ? -20.283 -11.543 27.434 1.00 23.67 ? 482 ASP A C 1 ATOM 3831 O O . ASP A 1 482 ? -21.228 -10.815 27.221 1.00 21.77 ? 482 ASP A O 1 ATOM 3832 C CB . ASP A 1 482 ? -20.688 -13.534 28.862 1.00 27.06 ? 482 ASP A CB 1 ATOM 3833 C CG . ASP A 1 482 ? -21.256 -14.943 28.950 1.00 33.05 ? 482 ASP A CG 1 ATOM 3834 O OD1 . ASP A 1 482 ? -21.651 -15.537 27.924 1.00 32.59 ? 482 ASP A OD1 1 ATOM 3835 O OD2 . ASP A 1 482 ? -21.316 -15.472 30.082 1.00 37.01 ? 482 ASP A OD2 1 ATOM 3836 N N . LEU A 1 483 ? -19.079 -11.050 27.696 1.00 22.26 ? 483 LEU A N 1 ATOM 3837 C CA . LEU A 1 483 ? -18.849 -9.613 27.663 1.00 22.31 ? 483 LEU A CA 1 ATOM 3838 C C . LEU A 1 483 ? -18.671 -9.022 26.240 1.00 20.19 ? 483 LEU A C 1 ATOM 3839 O O . LEU A 1 483 ? -19.181 -7.962 25.949 1.00 17.61 ? 483 LEU A O 1 ATOM 3840 C CB . LEU A 1 483 ? -17.616 -9.352 28.504 1.00 24.52 ? 483 LEU A CB 1 ATOM 3841 C CG . LEU A 1 483 ? -17.970 -9.475 30.001 1.00 25.81 ? 483 LEU A CG 1 ATOM 3842 C CD1 . LEU A 1 483 ? -16.691 -9.482 30.827 1.00 28.02 ? 483 LEU A CD1 1 ATOM 3843 C CD2 . LEU A 1 483 ? -18.882 -8.361 30.414 1.00 24.87 ? 483 LEU A CD2 1 ATOM 3844 N N . TYR A 1 484 ? -17.914 -9.689 25.382 1.00 17.05 ? 484 TYR A N 1 ATOM 3845 C CA . TYR A 1 484 ? -17.429 -9.133 24.106 1.00 17.52 ? 484 TYR A CA 1 ATOM 3846 C C . TYR A 1 484 ? -18.178 -9.545 22.809 1.00 18.92 ? 484 TYR A C 1 ATOM 3847 O O . TYR A 1 484 ? -18.172 -8.941 21.814 1.00 16.58 ? 484 TYR A O 1 ATOM 3848 C CB . TYR A 1 484 ? -15.975 -9.524 23.955 1.00 15.63 ? 484 TYR A CB 1 ATOM 3849 C CG . TYR A 1 484 ? -15.063 -8.620 24.697 1.00 16.76 ? 484 TYR A CG 1 ATOM 3850 C CD1 . TYR A 1 484 ? -14.832 -7.315 24.267 1.00 13.65 ? 484 TYR A CD1 1 ATOM 3851 C CD2 . TYR A 1 484 ? -14.444 -9.044 25.833 1.00 15.02 ? 484 TYR A CD2 1 ATOM 3852 C CE1 . TYR A 1 484 ? -13.986 -6.505 24.949 1.00 14.16 ? 484 TYR A CE1 1 ATOM 3853 C CE2 . TYR A 1 484 ? -13.622 -8.231 26.514 1.00 15.27 ? 484 TYR A CE2 1 ATOM 3854 C CZ . TYR A 1 484 ? -13.375 -6.970 26.068 1.00 14.03 ? 484 TYR A CZ 1 ATOM 3855 O OH . TYR A 1 484 ? -12.567 -6.223 26.779 1.00 13.89 ? 484 TYR A OH 1 ATOM 3856 N N . LYS A 1 485 ? -18.700 -10.711 22.893 1.00 19.82 ? 485 LYS A N 1 ATOM 3857 C CA . LYS A 1 485 ? -19.698 -11.340 21.948 1.00 23.11 ? 485 LYS A CA 1 ATOM 3858 C C . LYS A 1 485 ? -19.076 -12.052 20.746 1.00 22.25 ? 485 LYS A C 1 ATOM 3859 O O . LYS A 1 485 ? -19.620 -13.027 20.200 1.00 21.52 ? 485 LYS A O 1 ATOM 3860 C CB . LYS A 1 485 ? -20.702 -10.316 21.398 1.00 24.58 ? 485 LYS A CB 1 ATOM 3861 C CG . LYS A 1 485 ? -21.623 -9.665 22.420 1.00 32.33 ? 485 LYS A CG 1 ATOM 3862 C CD . LYS A 1 485 ? -22.610 -10.698 22.990 1.00 36.35 ? 485 LYS A CD 1 ATOM 3863 C CE . LYS A 1 485 ? -23.668 -10.193 23.960 1.00 40.89 ? 485 LYS A CE 1 ATOM 3864 N NZ . LYS A 1 485 ? -23.117 -9.805 25.283 1.00 42.17 ? 485 LYS A NZ 1 ATOM 3865 N N . THR A 1 486 ? -17.938 -11.510 20.411 1.00 18.94 ? 486 THR A N 1 ATOM 3866 C CA . THR A 1 486 ? -17.122 -12.127 19.357 1.00 18.51 ? 486 THR A CA 1 ATOM 3867 C C . THR A 1 486 ? -15.715 -11.907 19.778 1.00 18.02 ? 486 THR A C 1 ATOM 3868 O O . THR A 1 486 ? -15.419 -10.833 20.321 1.00 18.41 ? 486 THR A O 1 ATOM 3869 C CB . THR A 1 486 ? -17.327 -11.520 17.951 1.00 16.74 ? 486 THR A CB 1 ATOM 3870 O OG1 . THR A 1 486 ? -16.193 -11.850 17.148 1.00 18.14 ? 486 THR A OG1 1 ATOM 3871 C CG2 . THR A 1 486 ? -17.398 -10.044 18.019 1.00 17.59 ? 486 THR A CG2 1 ATOM 3872 N N . PRO A 1 487 ? -14.819 -12.875 19.502 1.00 19.45 ? 487 PRO A N 1 ATOM 3873 C CA . PRO A 1 487 ? -13.436 -12.608 19.890 1.00 18.83 ? 487 PRO A CA 1 ATOM 3874 C C . PRO A 1 487 ? -12.801 -11.409 19.143 1.00 20.44 ? 487 PRO A C 1 ATOM 3875 O O . PRO A 1 487 ? -11.716 -10.920 19.540 1.00 16.81 ? 487 PRO A O 1 ATOM 3876 C CB . PRO A 1 487 ? -12.741 -13.897 19.581 1.00 19.04 ? 487 PRO A CB 1 ATOM 3877 C CG . PRO A 1 487 ? -13.824 -14.959 19.737 1.00 19.33 ? 487 PRO A CG 1 ATOM 3878 C CD . PRO A 1 487 ? -15.034 -14.307 19.168 1.00 19.55 ? 487 PRO A CD 1 ATOM 3879 N N . ASP A 1 488 ? -13.474 -10.931 18.095 1.00 17.02 ? 488 ASP A N 1 ATOM 3880 C CA . ASP A 1 488 ? -12.925 -9.861 17.232 1.00 16.58 ? 488 ASP A CA 1 ATOM 3881 C C . ASP A 1 488 ? -12.899 -8.596 18.013 1.00 14.41 ? 488 ASP A C 1 ATOM 3882 O O . ASP A 1 488 ? -12.059 -7.748 17.766 1.00 14.66 ? 488 ASP A O 1 ATOM 3883 C CB . ASP A 1 488 ? -13.819 -9.578 15.987 1.00 16.04 ? 488 ASP A CB 1 ATOM 3884 C CG . ASP A 1 488 ? -13.770 -10.681 14.926 1.00 17.85 ? 488 ASP A CG 1 ATOM 3885 O OD1 . ASP A 1 488 ? -12.827 -11.502 14.930 1.00 16.83 ? 488 ASP A OD1 1 ATOM 3886 O OD2 . ASP A 1 488 ? -14.686 -10.657 14.023 1.00 16.82 ? 488 ASP A OD2 1 ATOM 3887 N N . ASN A 1 489 ? -13.845 -8.474 18.938 1.00 13.01 ? 489 ASN A N 1 ATOM 3888 C CA . ASN A 1 489 ? -13.992 -7.278 19.745 1.00 12.94 ? 489 ASN A CA 1 ATOM 3889 C C . ASN A 1 489 ? -13.195 -7.276 21.021 1.00 14.02 ? 489 ASN A C 1 ATOM 3890 O O . ASN A 1 489 ? -13.173 -6.244 21.698 1.00 12.67 ? 489 ASN A O 1 ATOM 3891 C CB . ASN A 1 489 ? -15.422 -7.028 20.042 1.00 13.57 ? 489 ASN A CB 1 ATOM 3892 C CG . ASN A 1 489 ? -16.190 -6.546 18.784 1.00 14.51 ? 489 ASN A CG 1 ATOM 3893 O OD1 . ASN A 1 489 ? -15.627 -6.524 17.687 1.00 13.41 ? 489 ASN A OD1 1 ATOM 3894 N ND2 . ASN A 1 489 ? -17.418 -6.124 18.968 1.00 12.76 ? 489 ASN A ND2 1 ATOM 3895 N N . ILE A 1 490 ? -12.548 -8.418 21.355 1.00 14.93 ? 490 ILE A N 1 ATOM 3896 C CA . ILE A 1 490 ? -11.698 -8.446 22.600 1.00 15.35 ? 490 ILE A CA 1 ATOM 3897 C C . ILE A 1 490 ? -10.525 -7.457 22.501 1.00 17.97 ? 490 ILE A C 1 ATOM 3898 O O . ILE A 1 490 ? -9.713 -7.535 21.577 1.00 16.07 ? 490 ILE A O 1 ATOM 3899 C CB . ILE A 1 490 ? -11.194 -9.852 22.983 1.00 15.86 ? 490 ILE A CB 1 ATOM 3900 C CG1 . ILE A 1 490 ? -12.342 -10.837 23.206 1.00 17.84 ? 490 ILE A CG1 1 ATOM 3901 C CG2 . ILE A 1 490 ? -10.393 -9.788 24.279 1.00 17.96 ? 490 ILE A CG2 1 ATOM 3902 C CD1 . ILE A 1 490 ? -11.882 -12.285 23.262 1.00 18.60 ? 490 ILE A CD1 1 ATOM 3903 N N . ASP A 1 491 ? -10.427 -6.536 23.498 1.00 17.98 ? 491 ASP A N 1 ATOM 3904 C CA . ASP A 1 491 ? -9.381 -5.545 23.516 1.00 17.19 ? 491 ASP A CA 1 ATOM 3905 C C . ASP A 1 491 ? -8.029 -6.209 23.673 1.00 17.77 ? 491 ASP A C 1 ATOM 3906 O O . ASP A 1 491 ? -7.902 -7.228 24.401 1.00 15.63 ? 491 ASP A O 1 ATOM 3907 C CB . ASP A 1 491 ? -9.595 -4.508 24.623 1.00 18.43 ? 491 ASP A CB 1 ATOM 3908 C CG . ASP A 1 491 ? -10.968 -3.774 24.530 1.00 18.12 ? 491 ASP A CG 1 ATOM 3909 O OD1 . ASP A 1 491 ? -11.099 -2.879 23.681 1.00 19.22 ? 491 ASP A OD1 1 ATOM 3910 O OD2 . ASP A 1 491 ? -11.855 -4.025 25.403 1.00 19.09 ? 491 ASP A OD2 1 ATOM 3911 N N . ILE A 1 492 ? -7.030 -5.678 22.948 1.00 15.32 ? 492 ILE A N 1 ATOM 3912 C CA . ILE A 1 492 ? -5.766 -6.347 22.797 1.00 14.87 ? 492 ILE A CA 1 ATOM 3913 C C . ILE A 1 492 ? -5.086 -6.624 24.158 1.00 16.05 ? 492 ILE A C 1 ATOM 3914 O O . ILE A 1 492 ? -4.527 -7.709 24.395 1.00 13.86 ? 492 ILE A O 1 ATOM 3915 C CB . ILE A 1 492 ? -4.842 -5.628 21.788 1.00 14.01 ? 492 ILE A CB 1 ATOM 3916 C CG1 . ILE A 1 492 ? -3.515 -6.321 21.549 1.00 13.82 ? 492 ILE A CG1 1 ATOM 3917 C CG2 . ILE A 1 492 ? -4.545 -4.213 22.177 1.00 14.18 ? 492 ILE A CG2 1 ATOM 3918 C CD1 . ILE A 1 492 ? -3.657 -7.740 21.097 1.00 16.15 ? 492 ILE A CD1 1 ATOM 3919 N N . TRP A 1 493 ? -5.069 -5.614 25.023 1.00 15.71 ? 493 TRP A N 1 ATOM 3920 C CA . TRP A 1 493 ? -4.478 -5.807 26.328 1.00 14.92 ? 493 TRP A CA 1 ATOM 3921 C C . TRP A 1 493 ? -5.008 -7.070 27.035 1.00 14.90 ? 493 TRP A C 1 ATOM 3922 O O . TRP A 1 493 ? -4.218 -7.841 27.531 1.00 16.96 ? 493 TRP A O 1 ATOM 3923 C CB . TRP A 1 493 ? -4.670 -4.602 27.239 1.00 14.77 ? 493 TRP A CB 1 ATOM 3924 C CG . TRP A 1 493 ? -3.994 -4.857 28.572 1.00 15.75 ? 493 TRP A CG 1 ATOM 3925 C CD1 . TRP A 1 493 ? -2.684 -4.889 28.794 1.00 15.80 ? 493 TRP A CD1 1 ATOM 3926 C CD2 . TRP A 1 493 ? -4.630 -5.181 29.811 1.00 16.30 ? 493 TRP A CD2 1 ATOM 3927 N NE1 . TRP A 1 493 ? -2.411 -5.100 30.120 1.00 17.36 ? 493 TRP A NE1 1 ATOM 3928 C CE2 . TRP A 1 493 ? -3.604 -5.331 30.768 1.00 19.81 ? 493 TRP A CE2 1 ATOM 3929 C CE3 . TRP A 1 493 ? -5.949 -5.410 30.191 1.00 19.33 ? 493 TRP A CE3 1 ATOM 3930 C CZ2 . TRP A 1 493 ? -3.859 -5.685 32.110 1.00 20.40 ? 493 TRP A CZ2 1 ATOM 3931 C CZ3 . TRP A 1 493 ? -6.232 -5.683 31.572 1.00 19.39 ? 493 TRP A CZ3 1 ATOM 3932 C CH2 . TRP A 1 493 ? -5.183 -5.798 32.492 1.00 19.72 ? 493 TRP A CH2 1 ATOM 3933 N N . ILE A 1 494 ? -6.308 -7.244 27.143 1.00 15.51 ? 494 ILE A N 1 ATOM 3934 C CA . ILE A 1 494 ? -6.833 -8.437 27.854 1.00 16.97 ? 494 ILE A CA 1 ATOM 3935 C C . ILE A 1 494 ? -6.741 -9.704 27.050 1.00 20.68 ? 494 ILE A C 1 ATOM 3936 O O . ILE A 1 494 ? -6.448 -10.795 27.597 1.00 17.93 ? 494 ILE A O 1 ATOM 3937 C CB . ILE A 1 494 ? -8.242 -8.213 28.438 1.00 17.97 ? 494 ILE A CB 1 ATOM 3938 C CG1 . ILE A 1 494 ? -8.628 -9.357 29.385 1.00 18.94 ? 494 ILE A CG1 1 ATOM 3939 C CG2 . ILE A 1 494 ? -9.356 -8.046 27.357 1.00 17.78 ? 494 ILE A CG2 1 ATOM 3940 C CD1 . ILE A 1 494 ? -7.613 -9.602 30.497 1.00 20.23 ? 494 ILE A CD1 1 ATOM 3941 N N . GLY A 1 495 ? -6.907 -9.615 25.731 1.00 20.04 ? 495 GLY A N 1 ATOM 3942 C CA . GLY A 1 495 ? -6.796 -10.859 24.904 1.00 19.70 ? 495 GLY A CA 1 ATOM 3943 C C . GLY A 1 495 ? -5.446 -11.472 24.896 1.00 19.03 ? 495 GLY A C 1 ATOM 3944 O O . GLY A 1 495 ? -5.280 -12.676 25.068 1.00 18.26 ? 495 GLY A O 1 ATOM 3945 N N . GLY A 1 496 ? -4.440 -10.625 24.692 1.00 18.26 ? 496 GLY A N 1 ATOM 3946 C CA . GLY A 1 496 ? -3.096 -11.068 24.734 1.00 18.05 ? 496 GLY A CA 1 ATOM 3947 C C . GLY A 1 496 ? -2.682 -11.634 26.102 1.00 19.16 ? 496 GLY A C 1 ATOM 3948 O O . GLY A 1 496 ? -1.972 -12.644 26.158 1.00 16.53 ? 496 GLY A O 1 ATOM 3949 N N . ASN A 1 497 ? -3.099 -10.975 27.192 1.00 18.33 ? 497 ASN A N 1 ATOM 3950 C CA . ASN A 1 497 ? -2.717 -11.435 28.527 1.00 17.48 ? 497 ASN A CA 1 ATOM 3951 C C . ASN A 1 497 ? -3.505 -12.657 28.964 1.00 19.50 ? 497 ASN A C 1 ATOM 3952 O O . ASN A 1 497 ? -3.097 -13.351 29.879 1.00 20.80 ? 497 ASN A O 1 ATOM 3953 C CB . ASN A 1 497 ? -2.818 -10.266 29.553 1.00 17.54 ? 497 ASN A CB 1 ATOM 3954 C CG . ASN A 1 497 ? -1.655 -9.316 29.427 1.00 16.84 ? 497 ASN A CG 1 ATOM 3955 O OD1 . ASN A 1 497 ? -0.571 -9.743 29.580 1.00 20.12 ? 497 ASN A OD1 1 ATOM 3956 N ND2 . ASN A 1 497 ? -1.868 -8.059 29.133 1.00 16.84 ? 497 ASN A ND2 1 ATOM 3957 N N . ALA A 1 498 ? -4.631 -12.936 28.311 1.00 19.24 ? 498 ALA A N 1 ATOM 3958 C CA . ALA A 1 498 ? -5.433 -14.107 28.634 1.00 21.07 ? 498 ALA A CA 1 ATOM 3959 C C . ALA A 1 498 ? -4.836 -15.432 28.162 1.00 21.44 ? 498 ALA A C 1 ATOM 3960 O O . ALA A 1 498 ? -5.224 -16.481 28.628 1.00 18.77 ? 498 ALA A O 1 ATOM 3961 C CB . ALA A 1 498 ? -6.845 -13.941 28.045 1.00 19.15 ? 498 ALA A CB 1 ATOM 3962 N N . GLU A 1 499 ? -3.901 -15.380 27.204 1.00 22.02 ? 499 GLU A N 1 ATOM 3963 C CA . GLU A 1 499 ? -3.401 -16.590 26.598 1.00 20.80 ? 499 GLU A CA 1 ATOM 3964 C C . GLU A 1 499 ? -2.398 -17.268 27.532 1.00 21.85 ? 499 GLU A C 1 ATOM 3965 O O . GLU A 1 499 ? -1.529 -16.594 28.144 1.00 18.53 ? 499 GLU A O 1 ATOM 3966 C CB . GLU A 1 499 ? -2.675 -16.285 25.281 1.00 19.62 ? 499 GLU A CB 1 ATOM 3967 C CG . GLU A 1 499 ? -3.571 -15.760 24.175 1.00 19.73 ? 499 GLU A CG 1 ATOM 3968 C CD . GLU A 1 499 ? -2.839 -15.509 22.858 1.00 18.18 ? 499 GLU A CD 1 ATOM 3969 O OE1 . GLU A 1 499 ? -1.599 -15.568 22.829 1.00 20.86 ? 499 GLU A OE1 1 ATOM 3970 O OE2 . GLU A 1 499 ? -3.525 -15.228 21.849 1.00 16.90 ? 499 GLU A OE2 1 ATOM 3971 N N . PRO A 1 500 ? -2.429 -18.584 27.572 1.00 23.13 ? 500 PRO A N 1 ATOM 3972 C CA . PRO A 1 500 ? -1.458 -19.257 28.362 1.00 23.78 ? 500 PRO A CA 1 ATOM 3973 C C . PRO A 1 500 ? -0.093 -18.994 27.831 1.00 25.67 ? 500 PRO A C 1 ATOM 3974 O O . PRO A 1 500 ? 0.122 -18.775 26.620 1.00 22.53 ? 500 PRO A O 1 ATOM 3975 C CB . PRO A 1 500 ? -1.799 -20.750 28.229 1.00 26.87 ? 500 PRO A CB 1 ATOM 3976 C CG . PRO A 1 500 ? -3.033 -20.827 27.454 1.00 26.33 ? 500 PRO A CG 1 ATOM 3977 C CD . PRO A 1 500 ? -3.315 -19.493 26.845 1.00 25.14 ? 500 PRO A CD 1 ATOM 3978 N N . MET A 1 501 ? 0.840 -19.019 28.761 1.00 26.83 ? 501 MET A N 1 ATOM 3979 C CA . MET A 1 501 ? 2.179 -18.639 28.524 1.00 26.11 ? 501 MET A CA 1 ATOM 3980 C C . MET A 1 501 ? 2.910 -19.653 27.653 1.00 28.23 ? 501 MET A C 1 ATOM 3981 O O . MET A 1 501 ? 2.646 -20.838 27.749 1.00 26.56 ? 501 MET A O 1 ATOM 3982 C CB . MET A 1 501 ? 2.879 -18.600 29.879 1.00 30.06 ? 501 MET A CB 1 ATOM 3983 C CG . MET A 1 501 ? 2.374 -17.510 30.790 1.00 27.83 ? 501 MET A CG 1 ATOM 3984 S SD . MET A 1 501 ? 3.230 -17.568 32.371 1.00 29.85 ? 501 MET A SD 1 ATOM 3985 C CE . MET A 1 501 ? 2.507 -16.080 33.017 1.00 30.45 ? 501 MET A CE 1 ATOM 3986 N N . VAL A 1 502 ? 3.866 -19.184 26.857 1.00 23.61 ? 502 VAL A N 1 ATOM 3987 C CA . VAL A 1 502 ? 4.657 -20.087 26.078 1.00 26.10 ? 502 VAL A CA 1 ATOM 3988 C C . VAL A 1 502 ? 5.682 -20.788 26.988 1.00 31.18 ? 502 VAL A C 1 ATOM 3989 O O . VAL A 1 502 ? 6.036 -20.297 28.099 1.00 24.83 ? 502 VAL A O 1 ATOM 3990 C CB . VAL A 1 502 ? 5.434 -19.373 24.972 1.00 25.20 ? 502 VAL A CB 1 ATOM 3991 C CG1 . VAL A 1 502 ? 4.495 -18.642 24.009 1.00 23.80 ? 502 VAL A CG1 1 ATOM 3992 C CG2 . VAL A 1 502 ? 6.474 -18.419 25.548 1.00 25.62 ? 502 VAL A CG2 1 ATOM 3993 N N . GLU A 1 503 ? 6.193 -21.921 26.523 1.00 32.80 ? 503 GLU A N 1 ATOM 3994 C CA . GLU A 1 503 ? 7.097 -22.699 27.328 1.00 37.47 ? 503 GLU A CA 1 ATOM 3995 C C . GLU A 1 503 ? 8.311 -21.932 27.708 1.00 32.01 ? 503 GLU A C 1 ATOM 3996 O O . GLU A 1 503 ? 8.938 -21.325 26.881 1.00 27.68 ? 503 GLU A O 1 ATOM 3997 C CB . GLU A 1 503 ? 7.486 -24.020 26.680 1.00 45.55 ? 503 GLU A CB 1 ATOM 3998 C CG . GLU A 1 503 ? 7.162 -25.186 27.578 1.00 52.70 ? 503 GLU A CG 1 ATOM 3999 C CD . GLU A 1 503 ? 8.112 -26.324 27.435 1.00 62.57 ? 503 GLU A CD 1 ATOM 4000 O OE1 . GLU A 1 503 ? 7.775 -27.263 26.718 1.00 66.42 ? 503 GLU A OE1 1 ATOM 4001 O OE2 . GLU A 1 503 ? 9.204 -26.262 28.027 1.00 72.27 ? 503 GLU A OE2 1 ATOM 4002 N N . ARG A 1 504 ? 8.591 -21.945 28.999 1.00 29.06 ? 504 ARG A N 1 ATOM 4003 C CA . ARG A 1 504 ? 9.734 -21.248 29.559 1.00 30.24 ? 504 ARG A CA 1 ATOM 4004 C C . ARG A 1 504 ? 9.648 -19.700 29.552 1.00 25.79 ? 504 ARG A C 1 ATOM 4005 O O . ARG A 1 504 ? 10.563 -19.072 29.948 1.00 24.92 ? 504 ARG A O 1 ATOM 4006 C CB . ARG A 1 504 ? 11.032 -21.718 28.868 1.00 38.24 ? 504 ARG A CB 1 ATOM 4007 C CG . ARG A 1 504 ? 11.670 -23.035 29.317 1.00 40.73 ? 504 ARG A CG 1 ATOM 4008 C CD . ARG A 1 504 ? 12.866 -23.400 28.442 1.00 43.78 ? 504 ARG A CD 1 ATOM 4009 N NE . ARG A 1 504 ? 12.408 -24.240 27.365 1.00 46.05 ? 504 ARG A NE 1 ATOM 4010 C CZ . ARG A 1 504 ? 12.549 -24.025 26.070 1.00 52.86 ? 504 ARG A CZ 1 ATOM 4011 N NH1 . ARG A 1 504 ? 13.234 -23.001 25.606 1.00 57.94 ? 504 ARG A NH1 1 ATOM 4012 N NH2 . ARG A 1 504 ? 11.991 -24.877 25.227 1.00 52.99 ? 504 ARG A NH2 1 ATOM 4013 N N . GLY A 1 505 ? 8.549 -19.115 29.120 1.00 24.23 ? 505 GLY A N 1 ATOM 4014 C CA . GLY A 1 505 ? 8.448 -17.655 29.100 1.00 27.40 ? 505 GLY A CA 1 ATOM 4015 C C . GLY A 1 505 ? 7.326 -17.219 30.052 1.00 25.49 ? 505 GLY A C 1 ATOM 4016 O O . GLY A 1 505 ? 6.791 -18.027 30.846 1.00 21.99 ? 505 GLY A O 1 ATOM 4017 N N . ARG A 1 506 ? 6.981 -15.929 29.972 1.00 22.60 ? 506 ARG A N 1 ATOM 4018 C CA . ARG A 1 506 ? 5.983 -15.367 30.873 1.00 21.18 ? 506 ARG A CA 1 ATOM 4019 C C . ARG A 1 506 ? 4.869 -14.635 30.116 1.00 23.53 ? 506 ARG A C 1 ATOM 4020 O O . ARG A 1 506 ? 4.124 -13.816 30.709 1.00 20.66 ? 506 ARG A O 1 ATOM 4021 C CB . ARG A 1 506 ? 6.681 -14.436 31.879 1.00 20.70 ? 506 ARG A CB 1 ATOM 4022 C CG . ARG A 1 506 ? 7.492 -15.165 32.908 1.00 20.95 ? 506 ARG A CG 1 ATOM 4023 C CD . ARG A 1 506 ? 6.570 -15.950 33.841 1.00 21.79 ? 506 ARG A CD 1 ATOM 4024 N NE . ARG A 1 506 ? 7.296 -16.654 34.907 1.00 22.88 ? 506 ARG A NE 1 ATOM 4025 C CZ . ARG A 1 506 ? 7.662 -17.939 34.853 1.00 25.98 ? 506 ARG A CZ 1 ATOM 4026 N NH1 . ARG A 1 506 ? 7.441 -18.659 33.776 1.00 24.41 ? 506 ARG A NH1 1 ATOM 4027 N NH2 . ARG A 1 506 ? 8.340 -18.489 35.853 1.00 26.44 ? 506 ARG A NH2 1 ATOM 4028 N N . VAL A 1 507 ? 4.813 -14.868 28.796 1.00 20.47 ? 507 VAL A N 1 ATOM 4029 C CA . VAL A 1 507 ? 3.708 -14.367 27.936 1.00 18.75 ? 507 VAL A CA 1 ATOM 4030 C C . VAL A 1 507 ? 3.307 -15.454 26.959 1.00 17.35 ? 507 VAL A C 1 ATOM 4031 O O . VAL A 1 507 ? 4.056 -16.417 26.711 1.00 15.84 ? 507 VAL A O 1 ATOM 4032 C CB . VAL A 1 507 ? 4.036 -13.057 27.173 1.00 18.42 ? 507 VAL A CB 1 ATOM 4033 C CG1 . VAL A 1 507 ? 4.417 -11.921 28.105 1.00 18.94 ? 507 VAL A CG1 1 ATOM 4034 C CG2 . VAL A 1 507 ? 5.151 -13.261 26.156 1.00 18.21 ? 507 VAL A CG2 1 ATOM 4035 N N . GLY A 1 508 ? 2.116 -15.311 26.408 1.00 17.92 ? 508 GLY A N 1 ATOM 4036 C CA . GLY A 1 508 ? 1.579 -16.271 25.436 1.00 18.40 ? 508 GLY A CA 1 ATOM 4037 C C . GLY A 1 508 ? 2.059 -15.992 24.013 1.00 21.34 ? 508 GLY A C 1 ATOM 4038 O O . GLY A 1 508 ? 2.793 -15.022 23.782 1.00 21.59 ? 508 GLY A O 1 ATOM 4039 N N . PRO A 1 509 ? 1.578 -16.802 23.052 1.00 22.14 ? 509 PRO A N 1 ATOM 4040 C CA . PRO A 1 509 ? 1.917 -16.663 21.626 1.00 21.51 ? 509 PRO A CA 1 ATOM 4041 C C . PRO A 1 509 ? 1.694 -15.279 21.038 1.00 20.84 ? 509 PRO A C 1 ATOM 4042 O O . PRO A 1 509 ? 2.578 -14.749 20.414 1.00 21.23 ? 509 PRO A O 1 ATOM 4043 C CB . PRO A 1 509 ? 1.003 -17.653 20.933 1.00 20.28 ? 509 PRO A CB 1 ATOM 4044 C CG . PRO A 1 509 ? 0.594 -18.624 21.976 1.00 21.66 ? 509 PRO A CG 1 ATOM 4045 C CD . PRO A 1 509 ? 0.581 -17.876 23.276 1.00 20.89 ? 509 PRO A CD 1 ATOM 4046 N N . LEU A 1 510 ? 0.535 -14.698 21.241 1.00 20.02 ? 510 LEU A N 1 ATOM 4047 C CA . LEU A 1 510 ? 0.318 -13.417 20.584 1.00 21.19 ? 510 LEU A CA 1 ATOM 4048 C C . LEU A 1 510 ? 1.312 -12.396 21.102 1.00 19.53 ? 510 LEU A C 1 ATOM 4049 O O . LEU A 1 510 ? 1.954 -11.658 20.355 1.00 18.61 ? 510 LEU A O 1 ATOM 4050 C CB . LEU A 1 510 ? -1.132 -12.940 20.783 1.00 19.28 ? 510 LEU A CB 1 ATOM 4051 C CG . LEU A 1 510 ? -1.513 -11.563 20.191 1.00 17.68 ? 510 LEU A CG 1 ATOM 4052 C CD1 . LEU A 1 510 ? -1.191 -11.539 18.705 1.00 18.56 ? 510 LEU A CD1 1 ATOM 4053 C CD2 . LEU A 1 510 ? -2.969 -11.280 20.413 1.00 17.62 ? 510 LEU A CD2 1 ATOM 4054 N N . LEU A 1 511 ? 1.380 -12.265 22.405 1.00 18.47 ? 511 LEU A N 1 ATOM 4055 C CA . LEU A 1 511 ? 2.298 -11.285 22.940 1.00 16.99 ? 511 LEU A CA 1 ATOM 4056 C C . LEU A 1 511 ? 3.771 -11.521 22.585 1.00 16.97 ? 511 LEU A C 1 ATOM 4057 O O . LEU A 1 511 ? 4.550 -10.570 22.380 1.00 17.13 ? 511 LEU A O 1 ATOM 4058 C CB . LEU A 1 511 ? 2.102 -11.212 24.456 1.00 17.91 ? 511 LEU A CB 1 ATOM 4059 C CG . LEU A 1 511 ? 0.795 -10.555 24.917 1.00 15.55 ? 511 LEU A CG 1 ATOM 4060 C CD1 . LEU A 1 511 ? 0.703 -10.632 26.455 1.00 16.95 ? 511 LEU A CD1 1 ATOM 4061 C CD2 . LEU A 1 511 ? 0.626 -9.114 24.538 1.00 17.56 ? 511 LEU A CD2 1 ATOM 4062 N N . ALA A 1 512 ? 4.180 -12.774 22.542 1.00 16.52 ? 512 ALA A N 1 ATOM 4063 C CA . ALA A 1 512 ? 5.515 -13.133 22.175 1.00 17.41 ? 512 ALA A CA 1 ATOM 4064 C C . ALA A 1 512 ? 5.865 -12.577 20.804 1.00 18.32 ? 512 ALA A C 1 ATOM 4065 O O . ALA A 1 512 ? 6.946 -12.047 20.610 1.00 18.49 ? 512 ALA A O 1 ATOM 4066 C CB . ALA A 1 512 ? 5.682 -14.652 22.197 1.00 15.68 ? 512 ALA A CB 1 ATOM 4067 N N . CYS A 1 513 ? 4.889 -12.655 19.895 1.00 21.81 ? 513 CYS A N 1 ATOM 4068 C CA . CYS A 1 513 ? 5.034 -12.115 18.570 1.00 21.03 ? 513 CYS A CA 1 ATOM 4069 C C . CYS A 1 513 ? 5.150 -10.596 18.593 1.00 18.56 ? 513 CYS A C 1 ATOM 4070 O O . CYS A 1 513 ? 6.030 -10.043 17.965 1.00 18.60 ? 513 CYS A O 1 ATOM 4071 C CB . CYS A 1 513 ? 3.827 -12.560 17.701 1.00 20.82 ? 513 CYS A CB 1 ATOM 4072 S SG . CYS A 1 513 ? 3.543 -11.623 16.158 1.00 21.38 ? 513 CYS A SG 1 ATOM 4073 N N . LEU A 1 514 ? 4.231 -9.902 19.249 1.00 18.14 ? 514 LEU A N 1 ATOM 4074 C CA . LEU A 1 514 ? 4.250 -8.416 19.218 1.00 18.28 ? 514 LEU A CA 1 ATOM 4075 C C . LEU A 1 514 ? 5.432 -7.874 19.924 1.00 17.74 ? 514 LEU A C 1 ATOM 4076 O O . LEU A 1 514 ? 6.102 -6.986 19.421 1.00 20.54 ? 514 LEU A O 1 ATOM 4077 C CB . LEU A 1 514 ? 2.959 -7.795 19.825 1.00 17.79 ? 514 LEU A CB 1 ATOM 4078 C CG . LEU A 1 514 ? 1.710 -8.292 19.142 1.00 16.78 ? 514 LEU A CG 1 ATOM 4079 C CD1 . LEU A 1 514 ? 0.451 -7.950 19.946 1.00 18.40 ? 514 LEU A CD1 1 ATOM 4080 C CD2 . LEU A 1 514 ? 1.579 -7.711 17.717 1.00 18.45 ? 514 LEU A CD2 1 ATOM 4081 N N . LEU A 1 515 ? 5.753 -8.418 21.102 1.00 17.29 ? 515 LEU A N 1 ATOM 4082 C CA . LEU A 1 515 ? 6.923 -7.989 21.820 1.00 17.62 ? 515 LEU A CA 1 ATOM 4083 C C . LEU A 1 515 ? 8.204 -8.383 21.049 1.00 18.00 ? 515 LEU A C 1 ATOM 4084 O O . LEU A 1 515 ? 9.163 -7.601 20.986 1.00 17.15 ? 515 LEU A O 1 ATOM 4085 C CB . LEU A 1 515 ? 6.950 -8.614 23.228 1.00 16.48 ? 515 LEU A CB 1 ATOM 4086 C CG . LEU A 1 515 ? 5.758 -8.292 24.139 1.00 15.42 ? 515 LEU A CG 1 ATOM 4087 C CD1 . LEU A 1 515 ? 5.717 -9.334 25.239 1.00 19.22 ? 515 LEU A CD1 1 ATOM 4088 C CD2 . LEU A 1 515 ? 5.930 -6.943 24.769 1.00 17.02 ? 515 LEU A CD2 1 ATOM 4089 N N . GLY A 1 516 ? 8.243 -9.630 20.578 1.00 19.36 ? 516 GLY A N 1 ATOM 4090 C CA . GLY A 1 516 ? 9.484 -10.184 19.949 1.00 19.10 ? 516 GLY A CA 1 ATOM 4091 C C . GLY A 1 516 ? 9.854 -9.375 18.734 1.00 19.27 ? 516 GLY A C 1 ATOM 4092 O O . GLY A 1 516 ? 11.006 -8.930 18.594 1.00 19.36 ? 516 GLY A O 1 ATOM 4093 N N . ARG A 1 517 ? 8.865 -9.077 17.894 1.00 19.91 ? 517 ARG A N 1 ATOM 4094 C CA . ARG A 1 517 ? 9.061 -8.209 16.738 1.00 22.87 ? 517 ARG A CA 1 ATOM 4095 C C . ARG A 1 517 ? 9.621 -6.873 17.138 1.00 21.85 ? 517 ARG A C 1 ATOM 4096 O O . ARG A 1 517 ? 10.584 -6.442 16.582 1.00 21.11 ? 517 ARG A O 1 ATOM 4097 C CB . ARG A 1 517 ? 7.788 -7.942 15.971 1.00 25.50 ? 517 ARG A CB 1 ATOM 4098 C CG . ARG A 1 517 ? 7.201 -9.133 15.328 1.00 32.53 ? 517 ARG A CG 1 ATOM 4099 C CD . ARG A 1 517 ? 5.974 -8.723 14.558 1.00 41.16 ? 517 ARG A CD 1 ATOM 4100 N NE . ARG A 1 517 ? 6.331 -8.714 13.181 1.00 47.22 ? 517 ARG A NE 1 ATOM 4101 C CZ . ARG A 1 517 ? 5.832 -9.555 12.303 1.00 54.80 ? 517 ARG A CZ 1 ATOM 4102 N NH1 . ARG A 1 517 ? 4.892 -10.423 12.636 1.00 52.40 ? 517 ARG A NH1 1 ATOM 4103 N NH2 . ARG A 1 517 ? 6.265 -9.501 11.089 1.00 63.90 ? 517 ARG A NH2 1 ATOM 4104 N N . GLN A 1 518 ? 8.980 -6.240 18.103 1.00 18.65 ? 518 GLN A N 1 ATOM 4105 C CA . GLN A 1 518 ? 9.459 -4.900 18.524 1.00 16.87 ? 518 GLN A CA 1 ATOM 4106 C C . GLN A 1 518 ? 10.901 -4.916 19.027 1.00 17.09 ? 518 GLN A C 1 ATOM 4107 O O . GLN A 1 518 ? 11.725 -4.079 18.652 1.00 18.09 ? 518 GLN A O 1 ATOM 4108 C CB . GLN A 1 518 ? 8.536 -4.279 19.559 1.00 16.49 ? 518 GLN A CB 1 ATOM 4109 C CG . GLN A 1 518 ? 8.838 -2.829 19.836 1.00 17.73 ? 518 GLN A CG 1 ATOM 4110 C CD . GLN A 1 518 ? 8.351 -1.934 18.703 1.00 18.32 ? 518 GLN A CD 1 ATOM 4111 O OE1 . GLN A 1 518 ? 7.156 -1.719 18.549 1.00 21.55 ? 518 GLN A OE1 1 ATOM 4112 N NE2 . GLN A 1 518 ? 9.283 -1.393 17.919 1.00 19.41 ? 518 GLN A NE2 1 ATOM 4113 N N . PHE A 1 519 ? 11.234 -5.840 19.902 1.00 16.52 ? 519 PHE A N 1 ATOM 4114 C CA . PHE A 1 519 ? 12.548 -5.853 20.425 1.00 18.82 ? 519 PHE A CA 1 ATOM 4115 C C . PHE A 1 519 ? 13.623 -6.161 19.305 1.00 20.33 ? 519 PHE A C 1 ATOM 4116 O O . PHE A 1 519 ? 14.715 -5.579 19.307 1.00 20.33 ? 519 PHE A O 1 ATOM 4117 C CB . PHE A 1 519 ? 12.623 -6.788 21.625 1.00 18.67 ? 519 PHE A CB 1 ATOM 4118 C CG . PHE A 1 519 ? 12.139 -6.128 22.923 1.00 18.78 ? 519 PHE A CG 1 ATOM 4119 C CD1 . PHE A 1 519 ? 12.934 -5.233 23.578 1.00 19.31 ? 519 PHE A CD1 1 ATOM 4120 C CD2 . PHE A 1 519 ? 10.925 -6.462 23.491 1.00 18.77 ? 519 PHE A CD2 1 ATOM 4121 C CE1 . PHE A 1 519 ? 12.513 -4.645 24.770 1.00 20.16 ? 519 PHE A CE1 1 ATOM 4122 C CE2 . PHE A 1 519 ? 10.510 -5.905 24.698 1.00 19.31 ? 519 PHE A CE2 1 ATOM 4123 C CZ . PHE A 1 519 ? 11.310 -5.010 25.345 1.00 17.92 ? 519 PHE A CZ 1 ATOM 4124 N N . GLN A 1 520 ? 13.274 -7.046 18.393 1.00 22.39 ? 520 GLN A N 1 ATOM 4125 C CA . GLN A 1 520 ? 14.139 -7.346 17.220 1.00 23.94 ? 520 GLN A CA 1 ATOM 4126 C C . GLN A 1 520 ? 14.465 -6.061 16.489 1.00 22.94 ? 520 GLN A C 1 ATOM 4127 O O . GLN A 1 520 ? 15.640 -5.771 16.220 1.00 22.04 ? 520 GLN A O 1 ATOM 4128 C CB . GLN A 1 520 ? 13.487 -8.344 16.311 1.00 24.22 ? 520 GLN A CB 1 ATOM 4129 C CG . GLN A 1 520 ? 14.188 -8.564 14.936 1.00 27.76 ? 520 GLN A CG 1 ATOM 4130 C CD . GLN A 1 520 ? 13.407 -7.921 13.806 1.00 30.26 ? 520 GLN A CD 1 ATOM 4131 O OE1 . GLN A 1 520 ? 12.302 -8.338 13.522 1.00 34.22 ? 520 GLN A OE1 1 ATOM 4132 N NE2 . GLN A 1 520 ? 13.972 -6.884 13.177 1.00 29.46 ? 520 GLN A NE2 1 ATOM 4133 N N . GLN A 1 521 ? 13.433 -5.276 16.232 1.00 22.36 ? 521 GLN A N 1 ATOM 4134 C CA . GLN A 1 521 ? 13.566 -4.002 15.528 1.00 22.01 ? 521 GLN A CA 1 ATOM 4135 C C . GLN A 1 521 ? 14.314 -2.893 16.246 1.00 24.39 ? 521 GLN A C 1 ATOM 4136 O O . GLN A 1 521 ? 15.099 -2.161 15.627 1.00 22.54 ? 521 GLN A O 1 ATOM 4137 C CB . GLN A 1 521 ? 12.207 -3.466 15.153 1.00 21.47 ? 521 GLN A CB 1 ATOM 4138 C CG . GLN A 1 521 ? 11.524 -4.364 14.187 1.00 23.17 ? 521 GLN A CG 1 ATOM 4139 C CD . GLN A 1 521 ? 10.149 -3.892 13.793 1.00 24.27 ? 521 GLN A CD 1 ATOM 4140 O OE1 . GLN A 1 521 ? 9.337 -4.699 13.435 1.00 27.81 ? 521 GLN A OE1 1 ATOM 4141 N NE2 . GLN A 1 521 ? 9.873 -2.609 13.909 1.00 25.44 ? 521 GLN A NE2 1 ATOM 4142 N N . ILE A 1 522 ? 14.111 -2.770 17.557 1.00 24.99 ? 522 ILE A N 1 ATOM 4143 C CA . ILE A 1 522 ? 14.873 -1.781 18.282 1.00 24.96 ? 522 ILE A CA 1 ATOM 4144 C C . ILE A 1 522 ? 16.361 -2.201 18.370 1.00 22.71 ? 522 ILE A C 1 ATOM 4145 O O . ILE A 1 522 ? 17.208 -1.349 18.454 1.00 25.82 ? 522 ILE A O 1 ATOM 4146 C CB . ILE A 1 522 ? 14.295 -1.382 19.675 1.00 25.65 ? 522 ILE A CB 1 ATOM 4147 C CG1 . ILE A 1 522 ? 14.566 -2.418 20.736 1.00 27.54 ? 522 ILE A CG1 1 ATOM 4148 C CG2 . ILE A 1 522 ? 12.803 -1.114 19.598 1.00 28.62 ? 522 ILE A CG2 1 ATOM 4149 C CD1 . ILE A 1 522 ? 14.042 -1.932 22.082 1.00 33.40 ? 522 ILE A CD1 1 ATOM 4150 N N . ARG A 1 523 ? 16.677 -3.481 18.409 1.00 23.72 ? 523 ARG A N 1 ATOM 4151 C CA . ARG A 1 523 ? 18.069 -3.872 18.259 1.00 25.79 ? 523 ARG A CA 1 ATOM 4152 C C . ARG A 1 523 ? 18.548 -3.645 16.823 1.00 25.02 ? 523 ARG A C 1 ATOM 4153 O O . ARG A 1 523 ? 19.451 -2.874 16.614 1.00 23.15 ? 523 ARG A O 1 ATOM 4154 C CB . ARG A 1 523 ? 18.318 -5.310 18.655 1.00 26.96 ? 523 ARG A CB 1 ATOM 4155 C CG . ARG A 1 523 ? 19.768 -5.752 18.323 1.00 29.06 ? 523 ARG A CG 1 ATOM 4156 C CD . ARG A 1 523 ? 19.925 -7.238 18.487 1.00 29.31 ? 523 ARG A CD 1 ATOM 4157 N NE . ARG A 1 523 ? 19.209 -7.915 17.438 1.00 28.61 ? 523 ARG A NE 1 ATOM 4158 C CZ . ARG A 1 523 ? 19.115 -9.239 17.323 1.00 28.82 ? 523 ARG A CZ 1 ATOM 4159 N NH1 . ARG A 1 523 ? 19.734 -10.053 18.168 1.00 27.36 ? 523 ARG A NH1 1 ATOM 4160 N NH2 . ARG A 1 523 ? 18.434 -9.732 16.301 1.00 30.05 ? 523 ARG A NH2 1 ATOM 4161 N N . ASP A 1 524 ? 17.934 -4.342 15.841 1.00 21.56 ? 524 ASP A N 1 ATOM 4162 C CA . ASP A 1 524 ? 18.459 -4.307 14.441 1.00 20.05 ? 524 ASP A CA 1 ATOM 4163 C C . ASP A 1 524 ? 18.446 -2.903 13.801 1.00 20.91 ? 524 ASP A C 1 ATOM 4164 O O . ASP A 1 524 ? 19.203 -2.631 12.852 1.00 23.63 ? 524 ASP A O 1 ATOM 4165 C CB . ASP A 1 524 ? 17.722 -5.292 13.553 1.00 18.01 ? 524 ASP A CB 1 ATOM 4166 C CG . ASP A 1 524 ? 17.849 -6.660 14.044 1.00 17.79 ? 524 ASP A CG 1 ATOM 4167 O OD1 . ASP A 1 524 ? 18.690 -6.854 14.933 1.00 20.81 ? 524 ASP A OD1 1 ATOM 4168 O OD2 . ASP A 1 524 ? 17.131 -7.535 13.572 1.00 18.34 ? 524 ASP A OD2 1 ATOM 4169 N N . GLY A 1 525 ? 17.666 -1.998 14.338 1.00 20.05 ? 525 GLY A N 1 ATOM 4170 C CA . GLY A 1 525 ? 17.466 -0.697 13.726 1.00 19.79 ? 525 GLY A CA 1 ATOM 4171 C C . GLY A 1 525 ? 18.143 0.425 14.417 1.00 18.94 ? 525 GLY A C 1 ATOM 4172 O O . GLY A 1 525 ? 17.916 1.588 14.125 1.00 21.15 ? 525 GLY A O 1 ATOM 4173 N N . ASP A 1 526 ? 19.000 0.088 15.354 1.00 20.03 ? 526 ASP A N 1 ATOM 4174 C CA . ASP A 1 526 ? 19.658 1.079 16.159 1.00 21.65 ? 526 ASP A CA 1 ATOM 4175 C C . ASP A 1 526 ? 21.150 1.144 15.696 1.00 20.87 ? 526 ASP A C 1 ATOM 4176 O O . ASP A 1 526 ? 21.886 0.173 15.873 1.00 21.24 ? 526 ASP A O 1 ATOM 4177 C CB . ASP A 1 526 ? 19.553 0.613 17.621 1.00 21.43 ? 526 ASP A CB 1 ATOM 4178 C CG . ASP A 1 526 ? 20.201 1.537 18.582 1.00 21.82 ? 526 ASP A CG 1 ATOM 4179 O OD1 . ASP A 1 526 ? 20.646 2.673 18.203 1.00 23.42 ? 526 ASP A OD1 1 ATOM 4180 O OD2 . ASP A 1 526 ? 20.265 1.140 19.771 1.00 21.04 ? 526 ASP A OD2 1 ATOM 4181 N N . ARG A 1 527 ? 21.565 2.287 15.159 1.00 22.64 ? 527 ARG A N 1 ATOM 4182 C CA . ARG A 1 527 ? 22.958 2.451 14.671 1.00 24.03 ? 527 ARG A CA 1 ATOM 4183 C C . ARG A 1 527 ? 23.940 2.366 15.834 1.00 29.21 ? 527 ARG A C 1 ATOM 4184 O O . ARG A 1 527 ? 25.132 2.043 15.656 1.00 25.16 ? 527 ARG A O 1 ATOM 4185 C CB . ARG A 1 527 ? 23.105 3.776 13.964 1.00 26.20 ? 527 ARG A CB 1 ATOM 4186 C CG . ARG A 1 527 ? 24.489 4.005 13.346 1.00 27.61 ? 527 ARG A CG 1 ATOM 4187 C CD . ARG A 1 527 ? 24.397 4.958 12.188 1.00 28.19 ? 527 ARG A CD 1 ATOM 4188 N NE . ARG A 1 527 ? 24.024 6.316 12.596 1.00 28.65 ? 527 ARG A NE 1 ATOM 4189 C CZ . ARG A 1 527 ? 24.863 7.177 13.159 1.00 29.09 ? 527 ARG A CZ 1 ATOM 4190 N NH1 . ARG A 1 527 ? 26.121 6.824 13.378 1.00 34.59 ? 527 ARG A NH1 1 ATOM 4191 N NH2 . ARG A 1 527 ? 24.480 8.408 13.473 1.00 28.24 ? 527 ARG A NH2 1 ATOM 4192 N N . PHE A 1 528 ? 23.460 2.667 17.046 1.00 27.94 ? 528 PHE A N 1 ATOM 4193 C CA . PHE A 1 528 ? 24.338 2.698 18.216 1.00 26.07 ? 528 PHE A CA 1 ATOM 4194 C C . PHE A 1 528 ? 24.085 1.505 19.114 1.00 24.74 ? 528 PHE A C 1 ATOM 4195 O O . PHE A 1 528 ? 24.442 1.556 20.285 1.00 25.13 ? 528 PHE A O 1 ATOM 4196 C CB . PHE A 1 528 ? 24.136 3.990 19.006 1.00 26.12 ? 528 PHE A CB 1 ATOM 4197 C CG . PHE A 1 528 ? 24.511 5.228 18.266 1.00 26.02 ? 528 PHE A CG 1 ATOM 4198 C CD1 . PHE A 1 528 ? 25.790 5.742 18.369 1.00 28.74 ? 528 PHE A CD1 1 ATOM 4199 C CD2 . PHE A 1 528 ? 23.579 5.927 17.531 1.00 30.71 ? 528 PHE A CD2 1 ATOM 4200 C CE1 . PHE A 1 528 ? 26.141 6.922 17.717 1.00 31.88 ? 528 PHE A CE1 1 ATOM 4201 C CE2 . PHE A 1 528 ? 23.914 7.114 16.873 1.00 29.27 ? 528 PHE A CE2 1 ATOM 4202 C CZ . PHE A 1 528 ? 25.183 7.622 16.986 1.00 30.45 ? 528 PHE A CZ 1 ATOM 4203 N N . TRP A 1 529 ? 23.468 0.444 18.586 1.00 25.04 ? 529 TRP A N 1 ATOM 4204 C CA . TRP A 1 529 ? 23.402 -0.821 19.324 1.00 24.84 ? 529 TRP A CA 1 ATOM 4205 C C . TRP A 1 529 ? 24.817 -1.157 19.802 1.00 30.36 ? 529 TRP A C 1 ATOM 4206 O O . TRP A 1 529 ? 25.804 -0.949 19.063 1.00 31.54 ? 529 TRP A O 1 ATOM 4207 C CB . TRP A 1 529 ? 22.831 -1.938 18.463 1.00 25.64 ? 529 TRP A CB 1 ATOM 4208 C CG . TRP A 1 529 ? 22.627 -3.221 19.177 1.00 27.08 ? 529 TRP A CG 1 ATOM 4209 C CD1 . TRP A 1 529 ? 23.336 -4.370 19.030 1.00 27.71 ? 529 TRP A CD1 1 ATOM 4210 C CD2 . TRP A 1 529 ? 21.694 -3.464 20.228 1.00 25.97 ? 529 TRP A CD2 1 ATOM 4211 N NE1 . TRP A 1 529 ? 22.868 -5.325 19.895 1.00 32.12 ? 529 TRP A NE1 1 ATOM 4212 C CE2 . TRP A 1 529 ? 21.869 -4.781 20.646 1.00 28.23 ? 529 TRP A CE2 1 ATOM 4213 C CE3 . TRP A 1 529 ? 20.702 -2.692 20.832 1.00 26.47 ? 529 TRP A CE3 1 ATOM 4214 C CZ2 . TRP A 1 529 ? 21.096 -5.355 21.637 1.00 30.58 ? 529 TRP A CZ2 1 ATOM 4215 C CZ3 . TRP A 1 529 ? 19.943 -3.265 21.825 1.00 25.39 ? 529 TRP A CZ3 1 ATOM 4216 C CH2 . TRP A 1 529 ? 20.144 -4.572 22.210 1.00 27.17 ? 529 TRP A CH2 1 ATOM 4217 N N . TRP A 1 530 ? 24.938 -1.681 21.019 1.00 29.74 ? 530 TRP A N 1 ATOM 4218 C CA . TRP A 1 530 ? 26.250 -1.835 21.645 1.00 29.84 ? 530 TRP A CA 1 ATOM 4219 C C . TRP A 1 530 ? 27.149 -2.835 20.899 1.00 31.19 ? 530 TRP A C 1 ATOM 4220 O O . TRP A 1 530 ? 28.362 -2.674 20.878 1.00 33.77 ? 530 TRP A O 1 ATOM 4221 C CB . TRP A 1 530 ? 26.144 -2.237 23.126 1.00 27.81 ? 530 TRP A CB 1 ATOM 4222 C CG . TRP A 1 530 ? 25.821 -3.619 23.308 1.00 24.17 ? 530 TRP A CG 1 ATOM 4223 C CD1 . TRP A 1 530 ? 24.582 -4.192 23.223 1.00 25.04 ? 530 TRP A CD1 1 ATOM 4224 C CD2 . TRP A 1 530 ? 26.726 -4.666 23.612 1.00 27.97 ? 530 TRP A CD2 1 ATOM 4225 N NE1 . TRP A 1 530 ? 24.674 -5.558 23.425 1.00 24.20 ? 530 TRP A NE1 1 ATOM 4226 C CE2 . TRP A 1 530 ? 25.980 -5.867 23.696 1.00 26.52 ? 530 TRP A CE2 1 ATOM 4227 C CE3 . TRP A 1 530 ? 28.102 -4.723 23.784 1.00 27.63 ? 530 TRP A CE3 1 ATOM 4228 C CZ2 . TRP A 1 530 ? 26.576 -7.096 23.956 1.00 31.67 ? 530 TRP A CZ2 1 ATOM 4229 C CZ3 . TRP A 1 530 ? 28.684 -5.956 24.089 1.00 29.04 ? 530 TRP A CZ3 1 ATOM 4230 C CH2 . TRP A 1 530 ? 27.941 -7.112 24.154 1.00 28.52 ? 530 TRP A CH2 1 ATOM 4231 N N . GLU A 1 531 ? 26.556 -3.867 20.327 1.00 29.54 ? 531 GLU A N 1 ATOM 4232 C CA . GLU A 1 531 ? 27.303 -4.813 19.514 1.00 32.08 ? 531 GLU A CA 1 ATOM 4233 C C . GLU A 1 531 ? 27.566 -4.349 18.070 1.00 30.14 ? 531 GLU A C 1 ATOM 4234 O O . GLU A 1 531 ? 28.147 -5.104 17.306 1.00 29.00 ? 531 GLU A O 1 ATOM 4235 C CB . GLU A 1 531 ? 26.621 -6.180 19.429 1.00 34.55 ? 531 GLU A CB 1 ATOM 4236 C CG . GLU A 1 531 ? 25.868 -6.651 20.650 1.00 40.51 ? 531 GLU A CG 1 ATOM 4237 C CD . GLU A 1 531 ? 25.158 -7.993 20.466 1.00 39.52 ? 531 GLU A CD 1 ATOM 4238 O OE1 . GLU A 1 531 ? 23.886 -8.022 20.427 1.00 42.32 ? 531 GLU A OE1 1 ATOM 4239 O OE2 . GLU A 1 531 ? 25.879 -9.001 20.401 1.00 37.73 ? 531 GLU A OE2 1 ATOM 4240 N N . ASN A 1 532 ? 27.056 -3.195 17.648 1.00 29.24 ? 532 ASN A N 1 ATOM 4241 C CA . ASN A 1 532 ? 27.263 -2.795 16.276 1.00 27.22 ? 532 ASN A CA 1 ATOM 4242 C C . ASN A 1 532 ? 28.739 -2.373 16.047 1.00 29.78 ? 532 ASN A C 1 ATOM 4243 O O . ASN A 1 532 ? 29.215 -1.435 16.695 1.00 30.90 ? 532 ASN A O 1 ATOM 4244 C CB . ASN A 1 532 ? 26.380 -1.628 15.839 1.00 27.69 ? 532 ASN A CB 1 ATOM 4245 C CG . ASN A 1 532 ? 26.466 -1.396 14.330 1.00 28.38 ? 532 ASN A CG 1 ATOM 4246 O OD1 . ASN A 1 532 ? 26.688 -2.344 13.581 1.00 27.73 ? 532 ASN A OD1 1 ATOM 4247 N ND2 . ASN A 1 532 ? 26.310 -0.170 13.885 1.00 27.21 ? 532 ASN A ND2 1 ATOM 4248 N N . PRO A 1 533 ? 29.448 -3.046 15.107 1.00 32.83 ? 533 PRO A N 1 ATOM 4249 C CA . PRO A 1 533 ? 30.862 -2.702 14.922 1.00 31.77 ? 533 PRO A CA 1 ATOM 4250 C C . PRO A 1 533 ? 31.073 -1.194 14.820 1.00 29.86 ? 533 PRO A C 1 ATOM 4251 O O . PRO A 1 533 ? 30.303 -0.524 14.146 1.00 29.20 ? 533 PRO A O 1 ATOM 4252 C CB . PRO A 1 533 ? 31.208 -3.442 13.628 1.00 33.85 ? 533 PRO A CB 1 ATOM 4253 C CG . PRO A 1 533 ? 30.390 -4.720 13.727 1.00 32.74 ? 533 PRO A CG 1 ATOM 4254 C CD . PRO A 1 533 ? 29.095 -4.293 14.389 1.00 31.04 ? 533 PRO A CD 1 ATOM 4255 N N . GLY A 1 534 ? 32.061 -0.663 15.563 1.00 30.68 ? 534 GLY A N 1 ATOM 4256 C CA . GLY A 1 534 ? 32.376 0.775 15.532 1.00 31.14 ? 534 GLY A CA 1 ATOM 4257 C C . GLY A 1 534 ? 31.797 1.593 16.683 1.00 36.37 ? 534 GLY A C 1 ATOM 4258 O O . GLY A 1 534 ? 32.250 2.703 16.944 1.00 32.99 ? 534 GLY A O 1 ATOM 4259 N N . VAL A 1 535 ? 30.773 1.064 17.363 1.00 37.90 ? 535 VAL A N 1 ATOM 4260 C CA . VAL A 1 535 ? 30.165 1.815 18.444 1.00 32.46 ? 535 VAL A CA 1 ATOM 4261 C C . VAL A 1 535 ? 31.092 1.797 19.644 1.00 31.27 ? 535 VAL A C 1 ATOM 4262 O O . VAL A 1 535 ? 31.395 2.868 20.232 1.00 29.27 ? 535 VAL A O 1 ATOM 4263 C CB . VAL A 1 535 ? 28.779 1.219 18.798 1.00 34.19 ? 535 VAL A CB 1 ATOM 4264 C CG1 . VAL A 1 535 ? 28.213 1.883 20.055 1.00 31.81 ? 535 VAL A CG1 1 ATOM 4265 C CG2 . VAL A 1 535 ? 27.831 1.393 17.628 1.00 33.17 ? 535 VAL A CG2 1 ATOM 4266 N N . PHE A 1 536 ? 31.500 0.569 20.012 1.00 33.35 ? 536 PHE A N 1 ATOM 4267 C CA . PHE A 1 536 ? 32.556 0.278 20.989 1.00 37.85 ? 536 PHE A CA 1 ATOM 4268 C C . PHE A 1 536 ? 33.708 -0.551 20.349 1.00 41.56 ? 536 PHE A C 1 ATOM 4269 O O . PHE A 1 536 ? 33.479 -1.376 19.425 1.00 31.90 ? 536 PHE A O 1 ATOM 4270 C CB . PHE A 1 536 ? 31.988 -0.574 22.113 1.00 40.52 ? 536 PHE A CB 1 ATOM 4271 C CG . PHE A 1 536 ? 31.008 0.161 23.009 1.00 44.12 ? 536 PHE A CG 1 ATOM 4272 C CD1 . PHE A 1 536 ? 31.451 1.168 23.889 1.00 45.63 ? 536 PHE A CD1 1 ATOM 4273 C CD2 . PHE A 1 536 ? 29.644 -0.146 22.984 1.00 41.50 ? 536 PHE A CD2 1 ATOM 4274 C CE1 . PHE A 1 536 ? 30.540 1.848 24.715 1.00 41.08 ? 536 PHE A CE1 1 ATOM 4275 C CE2 . PHE A 1 536 ? 28.742 0.534 23.806 1.00 38.12 ? 536 PHE A CE2 1 ATOM 4276 C CZ . PHE A 1 536 ? 29.191 1.520 24.670 1.00 37.37 ? 536 PHE A CZ 1 ATOM 4277 N N . THR A 1 537 ? 34.928 -0.368 20.876 1.00 38.23 ? 537 THR A N 1 ATOM 4278 C CA . THR A 1 537 ? 36.074 -1.136 20.415 1.00 34.31 ? 537 THR A CA 1 ATOM 4279 C C . THR A 1 537 ? 35.789 -2.512 20.897 1.00 37.03 ? 537 THR A C 1 ATOM 4280 O O . THR A 1 537 ? 34.950 -2.699 21.782 1.00 38.66 ? 537 THR A O 1 ATOM 4281 C CB . THR A 1 537 ? 37.366 -0.695 21.099 1.00 33.38 ? 537 THR A CB 1 ATOM 4282 O OG1 . THR A 1 537 ? 37.374 -1.178 22.463 1.00 32.47 ? 537 THR A OG1 1 ATOM 4283 C CG2 . THR A 1 537 ? 37.510 0.825 21.063 1.00 36.09 ? 537 THR A CG2 1 ATOM 4284 N N . GLU A 1 538 ? 36.513 -3.501 20.389 1.00 34.82 ? 538 GLU A N 1 ATOM 4285 C CA . GLU A 1 538 ? 36.273 -4.907 20.795 1.00 35.60 ? 538 GLU A CA 1 ATOM 4286 C C . GLU A 1 538 ? 36.672 -5.217 22.235 1.00 38.38 ? 538 GLU A C 1 ATOM 4287 O O . GLU A 1 538 ? 36.067 -6.063 22.868 1.00 38.78 ? 538 GLU A O 1 ATOM 4288 C CB . GLU A 1 538 ? 37.037 -5.857 19.878 1.00 37.09 ? 538 GLU A CB 1 ATOM 4289 C CG . GLU A 1 538 ? 36.837 -7.321 20.196 1.00 37.40 ? 538 GLU A CG 1 ATOM 4290 C CD . GLU A 1 538 ? 37.511 -8.196 19.167 1.00 44.15 ? 538 GLU A CD 1 ATOM 4291 O OE1 . GLU A 1 538 ? 37.900 -7.651 18.114 1.00 49.09 ? 538 GLU A OE1 1 ATOM 4292 O OE2 . GLU A 1 538 ? 37.663 -9.417 19.408 1.00 50.92 ? 538 GLU A OE2 1 ATOM 4293 N N . LYS A 1 539 ? 37.706 -4.545 22.727 1.00 42.56 ? 539 LYS A N 1 ATOM 4294 C CA . LYS A 1 539 ? 38.075 -4.659 24.144 1.00 50.32 ? 539 LYS A CA 1 ATOM 4295 C C . LYS A 1 539 ? 36.947 -4.134 25.045 1.00 45.10 ? 539 LYS A C 1 ATOM 4296 O O . LYS A 1 539 ? 36.598 -4.789 26.025 1.00 43.54 ? 539 LYS A O 1 ATOM 4297 C CB . LYS A 1 539 ? 39.408 -3.964 24.502 1.00 59.45 ? 539 LYS A CB 1 ATOM 4298 C CG . LYS A 1 539 ? 40.417 -4.923 25.159 1.00 68.27 ? 539 LYS A CG 1 ATOM 4299 C CD . LYS A 1 539 ? 41.669 -4.243 25.734 1.00 76.78 ? 539 LYS A CD 1 ATOM 4300 C CE . LYS A 1 539 ? 42.332 -5.052 26.858 1.00 75.58 ? 539 LYS A CE 1 ATOM 4301 N NZ . LYS A 1 539 ? 43.567 -4.401 27.382 1.00 70.63 ? 539 LYS A NZ 1 ATOM 4302 N N . GLN A 1 540 ? 36.400 -2.964 24.697 1.00 42.99 ? 540 GLN A N 1 ATOM 4303 C CA . GLN A 1 540 ? 35.208 -2.397 25.387 1.00 37.83 ? 540 GLN A CA 1 ATOM 4304 C C . GLN A 1 540 ? 34.050 -3.414 25.396 1.00 38.10 ? 540 GLN A C 1 ATOM 4305 O O . GLN A 1 540 ? 33.527 -3.811 26.461 1.00 29.04 ? 540 GLN A O 1 ATOM 4306 C CB . GLN A 1 540 ? 34.827 -1.073 24.745 1.00 35.38 ? 540 GLN A CB 1 ATOM 4307 C CG . GLN A 1 540 ? 35.856 -0.017 25.076 1.00 31.59 ? 540 GLN A CG 1 ATOM 4308 C CD . GLN A 1 540 ? 35.640 1.247 24.299 1.00 33.74 ? 540 GLN A CD 1 ATOM 4309 O OE1 . GLN A 1 540 ? 34.952 1.260 23.278 1.00 31.55 ? 540 GLN A OE1 1 ATOM 4310 N NE2 . GLN A 1 540 ? 36.197 2.343 24.796 1.00 34.78 ? 540 GLN A NE2 1 ATOM 4311 N N . ARG A 1 541 ? 33.718 -3.940 24.237 1.00 35.82 ? 541 ARG A N 1 ATOM 4312 C CA . ARG A 1 541 ? 32.743 -4.986 24.217 1.00 33.76 ? 541 ARG A CA 1 ATOM 4313 C C . ARG A 1 541 ? 33.034 -6.163 25.123 1.00 35.26 ? 541 ARG A C 1 ATOM 4314 O O . ARG A 1 541 ? 32.110 -6.613 25.804 1.00 33.16 ? 541 ARG A O 1 ATOM 4315 C CB . ARG A 1 541 ? 32.419 -5.474 22.803 1.00 35.51 ? 541 ARG A CB 1 ATOM 4316 C CG . ARG A 1 541 ? 31.814 -4.374 21.943 1.00 37.04 ? 541 ARG A CG 1 ATOM 4317 C CD . ARG A 1 541 ? 31.146 -5.004 20.709 1.00 39.56 ? 541 ARG A CD 1 ATOM 4318 N NE . ARG A 1 541 ? 32.077 -5.857 19.917 1.00 39.93 ? 541 ARG A NE 1 ATOM 4319 C CZ . ARG A 1 541 ? 32.919 -5.407 18.991 1.00 39.29 ? 541 ARG A CZ 1 ATOM 4320 N NH1 . ARG A 1 541 ? 32.972 -4.096 18.674 1.00 35.53 ? 541 ARG A NH1 1 ATOM 4321 N NH2 . ARG A 1 541 ? 33.716 -6.281 18.380 1.00 43.11 ? 541 ARG A NH2 1 ATOM 4322 N N . ASP A 1 542 ? 34.276 -6.661 25.191 1.00 35.73 ? 542 ASP A N 1 ATOM 4323 C CA . ASP A 1 542 ? 34.526 -7.871 26.040 1.00 37.67 ? 542 ASP A CA 1 ATOM 4324 C C . ASP A 1 542 ? 34.342 -7.562 27.539 1.00 32.38 ? 542 ASP A C 1 ATOM 4325 O O . ASP A 1 542 ? 33.974 -8.438 28.303 1.00 27.80 ? 542 ASP A O 1 ATOM 4326 C CB . ASP A 1 542 ? 35.923 -8.497 25.883 1.00 44.05 ? 542 ASP A CB 1 ATOM 4327 C CG . ASP A 1 542 ? 36.239 -8.885 24.483 1.00 50.03 ? 542 ASP A CG 1 ATOM 4328 O OD1 . ASP A 1 542 ? 35.473 -9.740 23.962 1.00 43.75 ? 542 ASP A OD1 1 ATOM 4329 O OD2 . ASP A 1 542 ? 37.252 -8.351 23.949 1.00 49.60 ? 542 ASP A OD2 1 ATOM 4330 N N . SER A 1 543 ? 34.626 -6.337 27.949 1.00 35.09 ? 543 SER A N 1 ATOM 4331 C CA . SER A 1 543 ? 34.343 -5.908 29.323 1.00 41.19 ? 543 SER A CA 1 ATOM 4332 C C . SER A 1 543 ? 32.818 -5.833 29.590 1.00 37.84 ? 543 SER A C 1 ATOM 4333 O O . SER A 1 543 ? 32.293 -6.331 30.603 1.00 35.02 ? 543 SER A O 1 ATOM 4334 C CB . SER A 1 543 ? 34.982 -4.518 29.554 1.00 46.82 ? 543 SER A CB 1 ATOM 4335 O OG . SER A 1 543 ? 36.320 -4.630 29.995 1.00 50.90 ? 543 SER A OG 1 ATOM 4336 N N . LEU A 1 544 ? 32.112 -5.213 28.650 1.00 31.71 ? 544 LEU A N 1 ATOM 4337 C CA . LEU A 1 544 ? 30.702 -4.993 28.803 1.00 30.80 ? 544 LEU A CA 1 ATOM 4338 C C . LEU A 1 544 ? 30.000 -6.266 28.986 1.00 32.69 ? 544 LEU A C 1 ATOM 4339 O O . LEU A 1 544 ? 29.065 -6.335 29.794 1.00 32.19 ? 544 LEU A O 1 ATOM 4340 C CB . LEU A 1 544 ? 30.128 -4.269 27.605 1.00 32.35 ? 544 LEU A CB 1 ATOM 4341 C CG . LEU A 1 544 ? 30.522 -2.810 27.571 1.00 31.10 ? 544 LEU A CG 1 ATOM 4342 C CD1 . LEU A 1 544 ? 30.146 -2.246 26.221 1.00 32.82 ? 544 LEU A CD1 1 ATOM 4343 C CD2 . LEU A 1 544 ? 29.881 -1.982 28.703 1.00 29.21 ? 544 LEU A CD2 1 ATOM 4344 N N . GLN A 1 545 ? 30.468 -7.320 28.328 1.00 31.19 ? 545 GLN A N 1 ATOM 4345 C CA . GLN A 1 545 ? 29.790 -8.610 28.472 1.00 35.69 ? 545 GLN A CA 1 ATOM 4346 C C . GLN A 1 545 ? 29.628 -9.087 29.911 1.00 33.46 ? 545 GLN A C 1 ATOM 4347 O O . GLN A 1 545 ? 28.828 -9.975 30.186 1.00 32.83 ? 545 GLN A O 1 ATOM 4348 C CB . GLN A 1 545 ? 30.521 -9.703 27.662 1.00 45.65 ? 545 GLN A CB 1 ATOM 4349 C CG . GLN A 1 545 ? 29.667 -10.933 27.313 1.00 54.34 ? 545 GLN A CG 1 ATOM 4350 C CD . GLN A 1 545 ? 28.552 -10.667 26.296 1.00 61.94 ? 545 GLN A CD 1 ATOM 4351 O OE1 . GLN A 1 545 ? 27.348 -10.812 26.594 1.00 64.51 ? 545 GLN A OE1 1 ATOM 4352 N NE2 . GLN A 1 545 ? 28.954 -10.326 25.070 1.00 62.96 ? 545 GLN A NE2 1 ATOM 4353 N N . LYS A 1 546 ? 30.441 -8.557 30.829 1.00 37.90 ? 546 LYS A N 1 ATOM 4354 C CA . LYS A 1 546 ? 30.488 -9.060 32.200 1.00 39.08 ? 546 LYS A CA 1 ATOM 4355 C C . LYS A 1 546 ? 29.512 -8.312 33.116 1.00 34.08 ? 546 LYS A C 1 ATOM 4356 O O . LYS A 1 546 ? 29.399 -8.662 34.311 1.00 36.19 ? 546 LYS A O 1 ATOM 4357 C CB . LYS A 1 546 ? 31.880 -8.830 32.799 1.00 42.03 ? 546 LYS A CB 1 ATOM 4358 C CG . LYS A 1 546 ? 33.055 -9.395 32.007 1.00 49.15 ? 546 LYS A CG 1 ATOM 4359 C CD . LYS A 1 546 ? 33.150 -10.890 32.252 1.00 48.67 ? 546 LYS A CD 1 ATOM 4360 C CE . LYS A 1 546 ? 34.462 -11.487 31.746 1.00 53.30 ? 546 LYS A CE 1 ATOM 4361 N NZ . LYS A 1 546 ? 34.304 -12.944 31.527 1.00 53.40 ? 546 LYS A NZ 1 ATOM 4362 N N . VAL A 1 547 ? 28.859 -7.262 32.608 1.00 30.39 ? 547 VAL A N 1 ATOM 4363 C CA . VAL A 1 547 ? 27.953 -6.485 33.466 1.00 28.13 ? 547 VAL A CA 1 ATOM 4364 C C . VAL A 1 547 ? 26.874 -7.371 33.987 1.00 27.66 ? 547 VAL A C 1 ATOM 4365 O O . VAL A 1 547 ? 26.568 -8.384 33.376 1.00 28.09 ? 547 VAL A O 1 ATOM 4366 C CB . VAL A 1 547 ? 27.352 -5.235 32.810 1.00 27.70 ? 547 VAL A CB 1 ATOM 4367 C CG1 . VAL A 1 547 ? 28.472 -4.276 32.438 1.00 28.04 ? 547 VAL A CG1 1 ATOM 4368 C CG2 . VAL A 1 547 ? 26.482 -5.553 31.639 1.00 28.01 ? 547 VAL A CG2 1 ATOM 4369 N N . SER A 1 548 ? 26.323 -7.031 35.151 1.00 25.59 ? 548 SER A N 1 ATOM 4370 C CA . SER A 1 548 ? 25.163 -7.744 35.665 1.00 23.67 ? 548 SER A CA 1 ATOM 4371 C C . SER A 1 548 ? 24.372 -6.801 36.562 1.00 22.06 ? 548 SER A C 1 ATOM 4372 O O . SER A 1 548 ? 24.905 -5.810 37.057 1.00 20.78 ? 548 SER A O 1 ATOM 4373 C CB . SER A 1 548 ? 25.562 -8.986 36.504 1.00 22.24 ? 548 SER A CB 1 ATOM 4374 O OG . SER A 1 548 ? 26.330 -8.593 37.641 1.00 22.39 ? 548 SER A OG 1 ATOM 4375 N N . PHE A 1 549 ? 23.125 -7.146 36.816 1.00 21.39 ? 549 PHE A N 1 ATOM 4376 C CA . PHE A 1 549 ? 22.374 -6.328 37.765 1.00 22.18 ? 549 PHE A CA 1 ATOM 4377 C C . PHE A 1 549 ? 22.992 -6.461 39.154 1.00 23.22 ? 549 PHE A C 1 ATOM 4378 O O . PHE A 1 549 ? 22.999 -5.486 39.910 1.00 25.12 ? 549 PHE A O 1 ATOM 4379 C CB . PHE A 1 549 ? 20.880 -6.687 37.853 1.00 20.64 ? 549 PHE A CB 1 ATOM 4380 C CG . PHE A 1 549 ? 20.033 -5.526 38.390 1.00 21.86 ? 549 PHE A CG 1 ATOM 4381 C CD1 . PHE A 1 549 ? 19.550 -4.554 37.507 1.00 22.30 ? 549 PHE A CD1 1 ATOM 4382 C CD2 . PHE A 1 549 ? 19.822 -5.337 39.736 1.00 22.40 ? 549 PHE A CD2 1 ATOM 4383 C CE1 . PHE A 1 549 ? 18.806 -3.468 37.961 1.00 23.57 ? 549 PHE A CE1 1 ATOM 4384 C CE2 . PHE A 1 549 ? 19.077 -4.234 40.195 1.00 23.78 ? 549 PHE A CE2 1 ATOM 4385 C CZ . PHE A 1 549 ? 18.567 -3.307 39.298 1.00 23.75 ? 549 PHE A CZ 1 ATOM 4386 N N . SER A 1 550 ? 23.450 -7.668 39.510 1.00 22.16 ? 550 SER A N 1 ATOM 4387 C CA . SER A 1 550 ? 24.018 -7.851 40.844 1.00 22.18 ? 550 SER A CA 1 ATOM 4388 C C . SER A 1 550 ? 25.162 -6.915 41.074 1.00 20.91 ? 550 SER A C 1 ATOM 4389 O O . SER A 1 550 ? 25.316 -6.399 42.157 1.00 26.12 ? 550 SER A O 1 ATOM 4390 C CB . SER A 1 550 ? 24.409 -9.312 41.089 1.00 25.24 ? 550 SER A CB 1 ATOM 4391 O OG . SER A 1 550 ? 23.286 -10.161 40.992 1.00 27.52 ? 550 SER A OG 1 ATOM 4392 N N . ARG A 1 551 ? 26.005 -6.721 40.071 1.00 20.80 ? 551 ARG A N 1 ATOM 4393 C CA . ARG A 1 551 ? 27.161 -5.862 40.222 1.00 22.22 ? 551 ARG A CA 1 ATOM 4394 C C . ARG A 1 551 ? 26.763 -4.415 40.300 1.00 20.74 ? 551 ARG A C 1 ATOM 4395 O O . ARG A 1 551 ? 27.346 -3.614 41.047 1.00 22.47 ? 551 ARG A O 1 ATOM 4396 C CB . ARG A 1 551 ? 28.147 -6.104 39.046 1.00 21.45 ? 551 ARG A CB 1 ATOM 4397 C CG . ARG A 1 551 ? 29.173 -4.993 38.826 1.00 22.37 ? 551 ARG A CG 1 ATOM 4398 C CD . ARG A 1 551 ? 30.119 -4.717 40.015 1.00 25.03 ? 551 ARG A CD 1 ATOM 4399 N NE . ARG A 1 551 ? 30.609 -5.929 40.711 1.00 26.76 ? 551 ARG A NE 1 ATOM 4400 C CZ . ARG A 1 551 ? 31.301 -5.910 41.856 1.00 27.28 ? 551 ARG A CZ 1 ATOM 4401 N NH1 . ARG A 1 551 ? 31.666 -7.056 42.420 1.00 25.57 ? 551 ARG A NH1 1 ATOM 4402 N NH2 . ARG A 1 551 ? 31.648 -4.741 42.435 1.00 26.47 ? 551 ARG A NH2 1 ATOM 4403 N N . LEU A 1 552 ? 25.758 -4.046 39.527 1.00 21.16 ? 552 LEU A N 1 ATOM 4404 C CA . LEU A 1 552 ? 25.212 -2.698 39.681 1.00 22.70 ? 552 LEU A CA 1 ATOM 4405 C C . LEU A 1 552 ? 24.828 -2.400 41.151 1.00 21.84 ? 552 LEU A C 1 ATOM 4406 O O . LEU A 1 552 ? 25.029 -1.309 41.660 1.00 20.65 ? 552 LEU A O 1 ATOM 4407 C CB . LEU A 1 552 ? 23.982 -2.540 38.761 1.00 24.14 ? 552 LEU A CB 1 ATOM 4408 C CG . LEU A 1 552 ? 23.327 -1.150 38.816 1.00 23.80 ? 552 LEU A CG 1 ATOM 4409 C CD1 . LEU A 1 552 ? 24.048 -0.237 37.842 1.00 24.33 ? 552 LEU A CD1 1 ATOM 4410 C CD2 . LEU A 1 552 ? 21.839 -1.263 38.520 1.00 23.19 ? 552 LEU A CD2 1 ATOM 4411 N N . ILE A 1 553 ? 24.212 -3.356 41.803 1.00 23.06 ? 553 ILE A N 1 ATOM 4412 C CA . ILE A 1 553 ? 23.809 -3.170 43.198 1.00 25.11 ? 553 ILE A CA 1 ATOM 4413 C C . ILE A 1 553 ? 25.042 -3.092 44.102 1.00 27.63 ? 553 ILE A C 1 ATOM 4414 O O . ILE A 1 553 ? 25.157 -2.179 44.916 1.00 24.36 ? 553 ILE A O 1 ATOM 4415 C CB . ILE A 1 553 ? 22.915 -4.330 43.660 1.00 26.08 ? 553 ILE A CB 1 ATOM 4416 C CG1 . ILE A 1 553 ? 21.527 -4.216 43.042 1.00 21.85 ? 553 ILE A CG1 1 ATOM 4417 C CG2 . ILE A 1 553 ? 22.811 -4.389 45.198 1.00 26.06 ? 553 ILE A CG2 1 ATOM 4418 C CD1 . ILE A 1 553 ? 20.756 -5.514 43.063 1.00 23.15 ? 553 ILE A CD1 1 ATOM 4419 N N . CYS A 1 554 ? 25.978 -4.019 43.879 1.00 28.25 ? 554 CYS A N 1 ATOM 4420 C CA . CYS A 1 554 ? 27.212 -4.064 44.652 1.00 27.16 ? 554 CYS A CA 1 ATOM 4421 C C . CYS A 1 554 ? 27.879 -2.723 44.575 1.00 24.62 ? 554 CYS A C 1 ATOM 4422 O O . CYS A 1 554 ? 28.315 -2.213 45.595 1.00 21.94 ? 554 CYS A O 1 ATOM 4423 C CB . CYS A 1 554 ? 28.158 -5.182 44.197 1.00 25.48 ? 554 CYS A CB 1 ATOM 4424 S SG . CYS A 1 554 ? 27.558 -6.852 44.548 1.00 30.63 ? 554 CYS A SG 1 ATOM 4425 N N . ASP A 1 555 ? 27.914 -2.125 43.385 1.00 27.15 ? 555 ASP A N 1 ATOM 4426 C CA . ASP A 1 555 ? 28.655 -0.894 43.172 1.00 23.98 ? 555 ASP A CA 1 ATOM 4427 C C . ASP A 1 555 ? 27.954 0.356 43.620 1.00 24.94 ? 555 ASP A C 1 ATOM 4428 O O . ASP A 1 555 ? 28.600 1.407 43.714 1.00 22.98 ? 555 ASP A O 1 ATOM 4429 C CB . ASP A 1 555 ? 29.006 -0.671 41.697 1.00 27.89 ? 555 ASP A CB 1 ATOM 4430 C CG . ASP A 1 555 ? 30.110 -1.609 41.156 1.00 31.66 ? 555 ASP A CG 1 ATOM 4431 O OD1 . ASP A 1 555 ? 30.843 -2.238 41.930 1.00 30.03 ? 555 ASP A OD1 1 ATOM 4432 O OD2 . ASP A 1 555 ? 30.221 -1.728 39.920 1.00 31.14 ? 555 ASP A OD2 1 ATOM 4433 N N . ASN A 1 556 ? 26.639 0.313 43.839 1.00 25.96 ? 556 ASN A N 1 ATOM 4434 C CA . ASN A 1 556 ? 25.904 1.559 44.044 1.00 23.04 ? 556 ASN A CA 1 ATOM 4435 C C . ASN A 1 556 ? 24.990 1.532 45.266 1.00 24.67 ? 556 ASN A C 1 ATOM 4436 O O . ASN A 1 556 ? 24.112 2.385 45.407 1.00 24.98 ? 556 ASN A O 1 ATOM 4437 C CB . ASN A 1 556 ? 25.065 1.831 42.802 1.00 25.72 ? 556 ASN A CB 1 ATOM 4438 C CG . ASN A 1 556 ? 25.909 2.069 41.573 1.00 26.83 ? 556 ASN A CG 1 ATOM 4439 O OD1 . ASN A 1 556 ? 26.516 3.115 41.452 1.00 24.70 ? 556 ASN A OD1 1 ATOM 4440 N ND2 . ASN A 1 556 ? 25.935 1.104 40.662 1.00 26.54 ? 556 ASN A ND2 1 ATOM 4441 N N . THR A 1 557 ? 25.136 0.514 46.102 1.00 24.99 ? 557 THR A N 1 ATOM 4442 C CA . THR A 1 557 ? 24.459 0.483 47.399 1.00 22.04 ? 557 THR A CA 1 ATOM 4443 C C . THR A 1 557 ? 25.462 0.068 48.513 1.00 23.87 ? 557 THR A C 1 ATOM 4444 O O . THR A 1 557 ? 26.653 0.019 48.263 1.00 22.70 ? 557 THR A O 1 ATOM 4445 C CB . THR A 1 557 ? 23.328 -0.491 47.363 1.00 20.11 ? 557 THR A CB 1 ATOM 4446 O OG1 . THR A 1 557 ? 23.837 -1.840 47.249 1.00 19.43 ? 557 THR A OG1 1 ATOM 4447 C CG2 . THR A 1 557 ? 22.436 -0.216 46.161 1.00 22.05 ? 557 THR A CG2 1 ATOM 4448 N N . HIS A 1 558 ? 24.974 -0.213 49.723 1.00 23.20 ? 558 HIS A N 1 ATOM 4449 C CA . HIS A 1 558 ? 25.768 -0.953 50.728 1.00 25.24 ? 558 HIS A CA 1 ATOM 4450 C C . HIS A 1 558 ? 25.236 -2.363 50.958 1.00 26.36 ? 558 HIS A C 1 ATOM 4451 O O . HIS A 1 558 ? 25.317 -2.909 52.060 1.00 26.65 ? 558 HIS A O 1 ATOM 4452 C CB . HIS A 1 558 ? 25.875 -0.147 52.014 1.00 25.52 ? 558 HIS A CB 1 ATOM 4453 C CG . HIS A 1 558 ? 26.613 1.145 51.848 1.00 25.75 ? 558 HIS A CG 1 ATOM 4454 N ND1 . HIS A 1 558 ? 26.153 2.353 52.320 1.00 28.48 ? 558 HIS A ND1 1 ATOM 4455 C CD2 . HIS A 1 558 ? 27.796 1.419 51.259 1.00 30.12 ? 558 HIS A CD2 1 ATOM 4456 C CE1 . HIS A 1 558 ? 27.013 3.309 52.035 1.00 25.06 ? 558 HIS A CE1 1 ATOM 4457 N NE2 . HIS A 1 558 ? 28.016 2.768 51.382 1.00 25.58 ? 558 HIS A NE2 1 ATOM 4458 N N . ILE A 1 559 ? 24.583 -2.925 49.935 1.00 25.60 ? 559 ILE A N 1 ATOM 4459 C CA . ILE A 1 559 ? 24.136 -4.312 50.004 1.00 24.13 ? 559 ILE A CA 1 ATOM 4460 C C . ILE A 1 559 ? 25.415 -5.064 49.635 1.00 29.76 ? 559 ILE A C 1 ATOM 4461 O O . ILE A 1 559 ? 26.004 -4.764 48.591 1.00 26.23 ? 559 ILE A O 1 ATOM 4462 C CB . ILE A 1 559 ? 23.088 -4.622 48.952 1.00 25.88 ? 559 ILE A CB 1 ATOM 4463 C CG1 . ILE A 1 559 ? 21.903 -3.716 49.139 1.00 26.78 ? 559 ILE A CG1 1 ATOM 4464 C CG2 . ILE A 1 559 ? 22.667 -6.104 48.987 1.00 23.04 ? 559 ILE A CG2 1 ATOM 4465 C CD1 . ILE A 1 559 ? 21.320 -3.794 50.486 1.00 31.74 ? 559 ILE A CD1 1 ATOM 4466 N N . THR A 1 560 ? 25.855 -5.990 50.482 1.00 30.28 ? 560 THR A N 1 ATOM 4467 C CA . THR A 1 560 ? 27.191 -6.631 50.325 1.00 32.87 ? 560 THR A CA 1 ATOM 4468 C C . THR A 1 560 ? 27.059 -8.092 49.933 1.00 32.00 ? 560 THR A C 1 ATOM 4469 O O . THR A 1 560 ? 28.060 -8.719 49.546 1.00 30.23 ? 560 THR A O 1 ATOM 4470 C CB . THR A 1 560 ? 27.998 -6.555 51.662 1.00 33.35 ? 560 THR A CB 1 ATOM 4471 O OG1 . THR A 1 560 ? 27.132 -6.945 52.743 1.00 36.81 ? 560 THR A OG1 1 ATOM 4472 C CG2 . THR A 1 560 ? 28.486 -5.117 51.898 1.00 32.69 ? 560 THR A CG2 1 ATOM 4473 N N . LYS A 1 561 ? 25.831 -8.626 50.025 1.00 34.53 ? 561 LYS A N 1 ATOM 4474 C CA . LYS A 1 561 ? 25.512 -9.986 49.663 1.00 34.54 ? 561 LYS A CA 1 ATOM 4475 C C . LYS A 1 561 ? 24.438 -9.967 48.565 1.00 33.16 ? 561 LYS A C 1 ATOM 4476 O O . LYS A 1 561 ? 23.407 -9.345 48.727 1.00 30.12 ? 561 LYS A O 1 ATOM 4477 C CB . LYS A 1 561 ? 24.973 -10.762 50.882 1.00 41.24 ? 561 LYS A CB 1 ATOM 4478 C CG . LYS A 1 561 ? 25.871 -10.749 52.134 1.00 42.01 ? 561 LYS A CG 1 ATOM 4479 C CD . LYS A 1 561 ? 27.259 -11.300 51.850 1.00 49.59 ? 561 LYS A CD 1 ATOM 4480 C CE . LYS A 1 561 ? 28.167 -11.349 53.087 1.00 58.70 ? 561 LYS A CE 1 ATOM 4481 N NZ . LYS A 1 561 ? 29.535 -11.821 52.707 1.00 62.52 ? 561 LYS A NZ 1 ATOM 4482 N N . VAL A 1 562 ? 24.691 -10.668 47.461 1.00 32.10 ? 562 VAL A N 1 ATOM 4483 C CA . VAL A 1 562 ? 23.812 -10.687 46.287 1.00 32.23 ? 562 VAL A CA 1 ATOM 4484 C C . VAL A 1 562 ? 23.836 -12.061 45.605 1.00 31.84 ? 562 VAL A C 1 ATOM 4485 O O . VAL A 1 562 ? 24.798 -12.793 45.762 1.00 31.28 ? 562 VAL A O 1 ATOM 4486 C CB . VAL A 1 562 ? 24.259 -9.625 45.243 1.00 30.54 ? 562 VAL A CB 1 ATOM 4487 C CG1 . VAL A 1 562 ? 24.193 -8.226 45.828 1.00 31.07 ? 562 VAL A CG1 1 ATOM 4488 C CG2 . VAL A 1 562 ? 25.672 -9.861 44.777 1.00 29.43 ? 562 VAL A CG2 1 ATOM 4489 N N . PRO A 1 563 ? 22.800 -12.386 44.817 1.00 31.00 ? 563 PRO A N 1 ATOM 4490 C CA . PRO A 1 563 ? 22.912 -13.563 44.030 1.00 29.83 ? 563 PRO A CA 1 ATOM 4491 C C . PRO A 1 563 ? 23.694 -13.339 42.770 1.00 30.25 ? 563 PRO A C 1 ATOM 4492 O O . PRO A 1 563 ? 24.032 -12.198 42.417 1.00 30.89 ? 563 PRO A O 1 ATOM 4493 C CB . PRO A 1 563 ? 21.465 -13.915 43.727 1.00 31.63 ? 563 PRO A CB 1 ATOM 4494 C CG . PRO A 1 563 ? 20.691 -12.642 43.893 1.00 33.78 ? 563 PRO A CG 1 ATOM 4495 C CD . PRO A 1 563 ? 21.608 -11.599 44.425 1.00 32.22 ? 563 PRO A CD 1 ATOM 4496 N N . LEU A 1 564 ? 24.006 -14.419 42.078 1.00 32.83 ? 564 LEU A N 1 ATOM 4497 C CA . LEU A 1 564 ? 24.601 -14.298 40.761 1.00 36.43 ? 564 LEU A CA 1 ATOM 4498 C C . LEU A 1 564 ? 23.556 -13.966 39.705 1.00 34.11 ? 564 LEU A C 1 ATOM 4499 O O . LEU A 1 564 ? 23.822 -13.190 38.793 1.00 36.66 ? 564 LEU A O 1 ATOM 4500 C CB . LEU A 1 564 ? 25.324 -15.574 40.386 1.00 35.93 ? 564 LEU A CB 1 ATOM 4501 C CG . LEU A 1 564 ? 26.510 -15.877 41.324 1.00 37.38 ? 564 LEU A CG 1 ATOM 4502 C CD1 . LEU A 1 564 ? 27.047 -17.262 41.017 1.00 37.64 ? 564 LEU A CD1 1 ATOM 4503 C CD2 . LEU A 1 564 ? 27.595 -14.816 41.203 1.00 34.25 ? 564 LEU A CD2 1 ATOM 4504 N N . HIS A 1 565 ? 22.397 -14.575 39.801 1.00 33.85 ? 565 HIS A N 1 ATOM 4505 C CA . HIS A 1 565 ? 21.391 -14.429 38.754 1.00 33.87 ? 565 HIS A CA 1 ATOM 4506 C C . HIS A 1 565 ? 20.194 -13.709 39.366 1.00 30.63 ? 565 HIS A C 1 ATOM 4507 O O . HIS A 1 565 ? 19.254 -14.338 39.846 1.00 27.96 ? 565 HIS A O 1 ATOM 4508 C CB . HIS A 1 565 ? 21.035 -15.786 38.164 1.00 38.94 ? 565 HIS A CB 1 ATOM 4509 C CG . HIS A 1 565 ? 22.231 -16.609 37.824 1.00 43.10 ? 565 HIS A CG 1 ATOM 4510 N ND1 . HIS A 1 565 ? 23.126 -16.241 36.844 1.00 45.53 ? 565 HIS A ND1 1 ATOM 4511 C CD2 . HIS A 1 565 ? 22.710 -17.759 38.356 1.00 46.95 ? 565 HIS A CD2 1 ATOM 4512 C CE1 . HIS A 1 565 ? 24.114 -17.118 36.792 1.00 43.57 ? 565 HIS A CE1 1 ATOM 4513 N NE2 . HIS A 1 565 ? 23.881 -18.056 37.691 1.00 47.78 ? 565 HIS A NE2 1 ATOM 4514 N N . ALA A 1 566 ? 20.288 -12.369 39.381 1.00 23.85 ? 566 ALA A N 1 ATOM 4515 C CA . ALA A 1 566 ? 19.348 -11.522 40.082 1.00 25.94 ? 566 ALA A CA 1 ATOM 4516 C C . ALA A 1 566 ? 17.895 -11.596 39.647 1.00 26.34 ? 566 ALA A C 1 ATOM 4517 O O . ALA A 1 566 ? 17.010 -11.273 40.466 1.00 23.68 ? 566 ALA A O 1 ATOM 4518 C CB . ALA A 1 566 ? 19.798 -10.092 40.064 1.00 25.53 ? 566 ALA A CB 1 ATOM 4519 N N . PHE A 1 567 ? 17.623 -12.049 38.416 1.00 24.15 ? 567 PHE A N 1 ATOM 4520 C CA . PHE A 1 567 ? 16.249 -12.225 37.939 1.00 22.78 ? 567 PHE A CA 1 ATOM 4521 C C . PHE A 1 567 ? 15.561 -13.516 38.360 1.00 25.45 ? 567 PHE A C 1 ATOM 4522 O O . PHE A 1 567 ? 14.350 -13.592 38.361 1.00 26.11 ? 567 PHE A O 1 ATOM 4523 C CB . PHE A 1 567 ? 16.177 -12.117 36.423 1.00 25.33 ? 567 PHE A CB 1 ATOM 4524 C CG . PHE A 1 567 ? 16.351 -10.734 35.923 1.00 29.35 ? 567 PHE A CG 1 ATOM 4525 C CD1 . PHE A 1 567 ? 15.397 -9.784 36.167 1.00 33.03 ? 567 PHE A CD1 1 ATOM 4526 C CD2 . PHE A 1 567 ? 17.491 -10.347 35.289 1.00 32.96 ? 567 PHE A CD2 1 ATOM 4527 C CE1 . PHE A 1 567 ? 15.556 -8.475 35.744 1.00 37.15 ? 567 PHE A CE1 1 ATOM 4528 C CE2 . PHE A 1 567 ? 17.639 -9.032 34.851 1.00 38.33 ? 567 PHE A CE2 1 ATOM 4529 C CZ . PHE A 1 567 ? 16.684 -8.085 35.092 1.00 31.23 ? 567 PHE A CZ 1 ATOM 4530 N N . GLN A 1 568 ? 16.340 -14.488 38.758 1.00 30.34 ? 568 GLN A N 1 ATOM 4531 C CA . GLN A 1 568 ? 15.840 -15.738 39.231 1.00 34.01 ? 568 GLN A CA 1 ATOM 4532 C C . GLN A 1 568 ? 15.376 -15.551 40.640 1.00 30.50 ? 568 GLN A C 1 ATOM 4533 O O . GLN A 1 568 ? 15.791 -14.664 41.304 1.00 28.86 ? 568 GLN A O 1 ATOM 4534 C CB . GLN A 1 568 ? 16.942 -16.797 39.197 1.00 40.24 ? 568 GLN A CB 1 ATOM 4535 C CG . GLN A 1 568 ? 17.180 -17.487 37.861 1.00 46.08 ? 568 GLN A CG 1 ATOM 4536 C CD . GLN A 1 568 ? 18.402 -18.416 37.875 1.00 57.92 ? 568 GLN A CD 1 ATOM 4537 O OE1 . GLN A 1 568 ? 18.976 -18.714 36.833 1.00 67.77 ? 568 GLN A OE1 1 ATOM 4538 N NE2 . GLN A 1 568 ? 18.810 -18.859 39.048 1.00 57.16 ? 568 GLN A NE2 1 ATOM 4539 N N . ALA A 1 569 ? 14.475 -16.396 41.065 1.00 32.04 ? 569 ALA A N 1 ATOM 4540 C CA . ALA A 1 569 ? 14.078 -16.453 42.455 1.00 35.42 ? 569 ALA A CA 1 ATOM 4541 C C . ALA A 1 569 ? 15.288 -16.984 43.172 1.00 37.52 ? 569 ALA A C 1 ATOM 4542 O O . ALA A 1 569 ? 15.869 -17.957 42.730 1.00 45.25 ? 569 ALA A O 1 ATOM 4543 C CB . ALA A 1 569 ? 12.895 -17.400 42.622 1.00 36.10 ? 569 ALA A CB 1 ATOM 4544 N N . ASN A 1 570 ? 15.646 -16.330 44.268 1.00 32.00 ? 570 ASN A N 1 ATOM 4545 C CA . ASN A 1 570 ? 16.861 -16.564 45.042 1.00 34.01 ? 570 ASN A CA 1 ATOM 4546 C C . ASN A 1 570 ? 16.553 -16.349 46.529 1.00 35.61 ? 570 ASN A C 1 ATOM 4547 O O . ASN A 1 570 ? 15.924 -15.341 46.898 1.00 32.37 ? 570 ASN A O 1 ATOM 4548 C CB . ASN A 1 570 ? 17.920 -15.539 44.721 1.00 31.42 ? 570 ASN A CB 1 ATOM 4549 C CG . ASN A 1 570 ? 18.599 -15.759 43.397 1.00 32.18 ? 570 ASN A CG 1 ATOM 4550 O OD1 . ASN A 1 570 ? 19.218 -16.820 43.155 1.00 31.80 ? 570 ASN A OD1 1 ATOM 4551 N ND2 . ASN A 1 570 ? 18.549 -14.734 42.549 1.00 29.76 ? 570 ASN A ND2 1 ATOM 4552 N N . ASN A 1 571 ? 16.997 -17.292 47.360 1.00 40.58 ? 571 ASN A N 1 ATOM 4553 C CA . ASN A 1 571 ? 16.647 -17.323 48.773 1.00 42.65 ? 571 ASN A CA 1 ATOM 4554 C C . ASN A 1 571 ? 17.900 -17.170 49.556 1.00 38.27 ? 571 ASN A C 1 ATOM 4555 O O . ASN A 1 571 ? 18.889 -17.807 49.227 1.00 41.94 ? 571 ASN A O 1 ATOM 4556 C CB . ASN A 1 571 ? 15.936 -18.631 49.108 1.00 48.84 ? 571 ASN A CB 1 ATOM 4557 C CG . ASN A 1 571 ? 14.643 -18.792 48.323 1.00 50.40 ? 571 ASN A CG 1 ATOM 4558 O OD1 . ASN A 1 571 ? 13.574 -18.364 48.733 1.00 47.30 ? 571 ASN A OD1 1 ATOM 4559 N ND2 . ASN A 1 571 ? 14.759 -19.359 47.157 1.00 56.58 ? 571 ASN A ND2 1 ATOM 4560 N N . TYR A 1 572 ? 17.869 -16.266 50.540 1.00 36.92 ? 572 TYR A N 1 ATOM 4561 C CA . TYR A 1 572 ? 19.034 -15.934 51.379 1.00 38.31 ? 572 TYR A CA 1 ATOM 4562 C C . TYR A 1 572 ? 19.134 -16.928 52.540 1.00 37.60 ? 572 TYR A C 1 ATOM 4563 O O . TYR A 1 572 ? 18.112 -17.304 53.092 1.00 39.18 ? 572 TYR A O 1 ATOM 4564 C CB . TYR A 1 572 ? 18.894 -14.531 51.968 1.00 37.85 ? 572 TYR A CB 1 ATOM 4565 C CG . TYR A 1 572 ? 20.086 -14.117 52.784 1.00 39.31 ? 572 TYR A CG 1 ATOM 4566 C CD1 . TYR A 1 572 ? 21.212 -13.637 52.152 1.00 37.17 ? 572 TYR A CD1 1 ATOM 4567 C CD2 . TYR A 1 572 ? 20.104 -14.246 54.191 1.00 38.97 ? 572 TYR A CD2 1 ATOM 4568 C CE1 . TYR A 1 572 ? 22.321 -13.256 52.860 1.00 36.58 ? 572 TYR A CE1 1 ATOM 4569 C CE2 . TYR A 1 572 ? 21.213 -13.849 54.916 1.00 39.64 ? 572 TYR A CE2 1 ATOM 4570 C CZ . TYR A 1 572 ? 22.322 -13.351 54.247 1.00 38.27 ? 572 TYR A CZ 1 ATOM 4571 O OH . TYR A 1 572 ? 23.453 -12.970 54.900 1.00 37.76 ? 572 TYR A OH 1 ATOM 4572 N N . PRO A 1 573 ? 20.341 -17.390 52.881 1.00 37.13 ? 573 PRO A N 1 ATOM 4573 C CA . PRO A 1 573 ? 21.656 -17.155 52.299 1.00 39.29 ? 573 PRO A CA 1 ATOM 4574 C C . PRO A 1 573 ? 22.115 -18.126 51.215 1.00 36.36 ? 573 PRO A C 1 ATOM 4575 O O . PRO A 1 573 ? 23.132 -17.864 50.585 1.00 35.69 ? 573 PRO A O 1 ATOM 4576 C CB . PRO A 1 573 ? 22.578 -17.316 53.503 1.00 40.08 ? 573 PRO A CB 1 ATOM 4577 C CG . PRO A 1 573 ? 21.919 -18.398 54.285 1.00 40.07 ? 573 PRO A CG 1 ATOM 4578 C CD . PRO A 1 573 ? 20.455 -18.106 54.175 1.00 40.04 ? 573 PRO A CD 1 ATOM 4579 N N . HIS A 1 574 ? 21.412 -19.231 50.998 1.00 42.44 ? 574 HIS A N 1 ATOM 4580 C CA . HIS A 1 574 ? 21.937 -20.272 50.111 1.00 41.27 ? 574 HIS A CA 1 ATOM 4581 C C . HIS A 1 574 ? 22.279 -19.769 48.701 1.00 42.13 ? 574 HIS A C 1 ATOM 4582 O O . HIS A 1 574 ? 23.264 -20.208 48.086 1.00 42.99 ? 574 HIS A O 1 ATOM 4583 C CB . HIS A 1 574 ? 20.908 -21.407 49.998 1.00 45.56 ? 574 HIS A CB 1 ATOM 4584 C CG . HIS A 1 574 ? 21.385 -22.553 49.154 1.00 57.53 ? 574 HIS A CG 1 ATOM 4585 N ND1 . HIS A 1 574 ? 21.137 -22.626 47.799 1.00 58.11 ? 574 HIS A ND1 1 ATOM 4586 C CD2 . HIS A 1 574 ? 22.107 -23.658 49.466 1.00 56.69 ? 574 HIS A CD2 1 ATOM 4587 C CE1 . HIS A 1 574 ? 21.691 -23.722 47.313 1.00 57.09 ? 574 HIS A CE1 1 ATOM 4588 N NE2 . HIS A 1 574 ? 22.285 -24.364 48.304 1.00 56.85 ? 574 HIS A NE2 1 ATOM 4589 N N . ASP A 1 575 ? 21.466 -18.859 48.181 1.00 40.32 ? 575 ASP A N 1 ATOM 4590 C CA . ASP A 1 575 ? 21.670 -18.368 46.797 1.00 39.02 ? 575 ASP A CA 1 ATOM 4591 C C . ASP A 1 575 ? 22.459 -17.084 46.710 1.00 34.53 ? 575 ASP A C 1 ATOM 4592 O O . ASP A 1 575 ? 22.548 -16.461 45.656 1.00 38.40 ? 575 ASP A O 1 ATOM 4593 C CB . ASP A 1 575 ? 20.310 -18.217 46.107 1.00 39.25 ? 575 ASP A CB 1 ATOM 4594 C CG . ASP A 1 575 ? 19.593 -19.545 45.977 1.00 39.32 ? 575 ASP A CG 1 ATOM 4595 O OD1 . ASP A 1 575 ? 20.270 -20.527 45.614 1.00 41.04 ? 575 ASP A OD1 1 ATOM 4596 O OD2 . ASP A 1 575 ? 18.381 -19.611 46.230 1.00 38.70 ? 575 ASP A OD2 1 ATOM 4597 N N . PHE A 1 576 ? 23.089 -16.697 47.807 1.00 31.18 ? 576 PHE A N 1 ATOM 4598 C CA . PHE A 1 576 ? 23.669 -15.371 47.874 1.00 31.62 ? 576 PHE A CA 1 ATOM 4599 C C . PHE A 1 576 ? 25.148 -15.455 48.098 1.00 35.10 ? 576 PHE A C 1 ATOM 4600 O O . PHE A 1 576 ? 25.612 -16.319 48.830 1.00 44.28 ? 576 PHE A O 1 ATOM 4601 C CB . PHE A 1 576 ? 22.989 -14.570 48.990 1.00 32.43 ? 576 PHE A CB 1 ATOM 4602 C CG . PHE A 1 576 ? 21.663 -13.958 48.580 1.00 32.52 ? 576 PHE A CG 1 ATOM 4603 C CD1 . PHE A 1 576 ? 20.529 -14.721 48.457 1.00 29.69 ? 576 PHE A CD1 1 ATOM 4604 C CD2 . PHE A 1 576 ? 21.561 -12.599 48.334 1.00 32.05 ? 576 PHE A CD2 1 ATOM 4605 C CE1 . PHE A 1 576 ? 19.314 -14.182 48.083 1.00 30.93 ? 576 PHE A CE1 1 ATOM 4606 C CE2 . PHE A 1 576 ? 20.350 -12.061 47.944 1.00 31.54 ? 576 PHE A CE2 1 ATOM 4607 C CZ . PHE A 1 576 ? 19.220 -12.849 47.838 1.00 28.45 ? 576 PHE A CZ 1 ATOM 4608 N N . VAL A 1 577 ? 25.897 -14.566 47.460 1.00 34.85 ? 577 VAL A N 1 ATOM 4609 C CA . VAL A 1 577 ? 27.331 -14.597 47.557 1.00 33.50 ? 577 VAL A CA 1 ATOM 4610 C C . VAL A 1 577 ? 27.815 -13.232 47.820 1.00 36.26 ? 577 VAL A C 1 ATOM 4611 O O . VAL A 1 577 ? 27.092 -12.263 47.624 1.00 35.73 ? 577 VAL A O 1 ATOM 4612 C CB . VAL A 1 577 ? 28.013 -15.167 46.281 1.00 34.77 ? 577 VAL A CB 1 ATOM 4613 C CG1 . VAL A 1 577 ? 27.427 -16.558 45.942 1.00 32.90 ? 577 VAL A CG1 1 ATOM 4614 C CG2 . VAL A 1 577 ? 27.941 -14.214 45.105 1.00 32.90 ? 577 VAL A CG2 1 ATOM 4615 N N . ASP A 1 578 ? 29.035 -13.154 48.320 1.00 35.38 ? 578 ASP A N 1 ATOM 4616 C CA . ASP A 1 578 ? 29.642 -11.894 48.582 1.00 34.92 ? 578 ASP A CA 1 ATOM 4617 C C . ASP A 1 578 ? 29.928 -11.212 47.243 1.00 34.93 ? 578 ASP A C 1 ATOM 4618 O O . ASP A 1 578 ? 30.235 -11.886 46.266 1.00 38.59 ? 578 ASP A O 1 ATOM 4619 C CB . ASP A 1 578 ? 30.931 -12.122 49.356 1.00 41.06 ? 578 ASP A CB 1 ATOM 4620 C CG . ASP A 1 578 ? 31.518 -10.840 49.848 1.00 41.26 ? 578 ASP A CG 1 ATOM 4621 O OD1 . ASP A 1 578 ? 31.030 -10.356 50.901 1.00 42.47 ? 578 ASP A OD1 1 ATOM 4622 O OD2 . ASP A 1 578 ? 32.451 -10.326 49.169 1.00 41.26 ? 578 ASP A OD2 1 ATOM 4623 N N . CYS A 1 579 ? 29.885 -9.881 47.238 1.00 33.43 ? 579 CYS A N 1 ATOM 4624 C CA . CYS A 1 579 ? 30.120 -9.074 46.055 1.00 30.95 ? 579 CYS A CA 1 ATOM 4625 C C . CYS A 1 579 ? 31.494 -9.240 45.382 1.00 35.35 ? 579 CYS A C 1 ATOM 4626 O O . CYS A 1 579 ? 31.645 -8.948 44.187 1.00 35.51 ? 579 CYS A O 1 ATOM 4627 C CB . CYS A 1 579 ? 29.845 -7.599 46.357 1.00 30.64 ? 579 CYS A CB 1 ATOM 4628 S SG . CYS A 1 579 ? 28.079 -7.107 46.517 1.00 30.86 ? 579 CYS A SG 1 ATOM 4629 N N . SER A 1 580 ? 32.506 -9.681 46.108 1.00 33.78 ? 580 SER A N 1 ATOM 4630 C CA . SER A 1 580 ? 33.794 -9.973 45.480 1.00 35.66 ? 580 SER A CA 1 ATOM 4631 C C . SER A 1 580 ? 33.608 -11.129 44.493 1.00 33.23 ? 580 SER A C 1 ATOM 4632 O O . SER A 1 580 ? 34.326 -11.234 43.541 1.00 35.21 ? 580 SER A O 1 ATOM 4633 C CB . SER A 1 580 ? 34.846 -10.343 46.532 1.00 36.55 ? 580 SER A CB 1 ATOM 4634 O OG . SER A 1 580 ? 34.348 -11.421 47.309 1.00 37.80 ? 580 SER A OG 1 ATOM 4635 N N . ALA A 1 581 ? 32.627 -11.984 44.700 1.00 34.48 ? 581 ALA A N 1 ATOM 4636 C CA . ALA A 1 581 ? 32.388 -13.054 43.748 1.00 34.00 ? 581 ALA A CA 1 ATOM 4637 C C . ALA A 1 581 ? 31.705 -12.615 42.449 1.00 37.68 ? 581 ALA A C 1 ATOM 4638 O O . ALA A 1 581 ? 31.378 -13.475 41.614 1.00 41.18 ? 581 ALA A O 1 ATOM 4639 C CB . ALA A 1 581 ? 31.549 -14.146 44.395 1.00 33.58 ? 581 ALA A CB 1 ATOM 4640 N N . VAL A 1 582 ? 31.407 -11.325 42.261 1.00 36.41 ? 582 VAL A N 1 ATOM 4641 C CA . VAL A 1 582 ? 30.673 -10.922 41.052 1.00 34.76 ? 582 VAL A CA 1 ATOM 4642 C C . VAL A 1 582 ? 31.558 -10.073 40.150 1.00 32.68 ? 582 VAL A C 1 ATOM 4643 O O . VAL A 1 582 ? 32.131 -9.102 40.593 1.00 34.44 ? 582 VAL A O 1 ATOM 4644 C CB . VAL A 1 582 ? 29.390 -10.133 41.371 1.00 32.48 ? 582 VAL A CB 1 ATOM 4645 C CG1 . VAL A 1 582 ? 28.633 -9.876 40.098 1.00 32.37 ? 582 VAL A CG1 1 ATOM 4646 C CG2 . VAL A 1 582 ? 28.504 -10.866 42.332 1.00 34.96 ? 582 VAL A CG2 1 ATOM 4647 N N . ASP A 1 583 ? 31.590 -10.401 38.855 1.00 33.51 ? 583 ASP A N 1 ATOM 4648 C CA . ASP A 1 583 ? 32.443 -9.709 37.921 1.00 33.14 ? 583 ASP A CA 1 ATOM 4649 C C . ASP A 1 583 ? 32.214 -8.223 38.024 1.00 34.11 ? 583 ASP A C 1 ATOM 4650 O O . ASP A 1 583 ? 31.086 -7.782 38.276 1.00 36.59 ? 583 ASP A O 1 ATOM 4651 C CB . ASP A 1 583 ? 32.137 -10.124 36.468 1.00 39.63 ? 583 ASP A CB 1 ATOM 4652 C CG . ASP A 1 583 ? 32.339 -11.613 36.198 1.00 42.42 ? 583 ASP A CG 1 ATOM 4653 O OD1 . ASP A 1 583 ? 32.975 -12.318 36.988 1.00 42.56 ? 583 ASP A OD1 1 ATOM 4654 O OD2 . ASP A 1 583 ? 31.832 -12.096 35.168 1.00 52.57 ? 583 ASP A OD2 1 ATOM 4655 N N . LYS A 1 584 ? 33.254 -7.447 37.749 1.00 33.05 ? 584 LYS A N 1 ATOM 4656 C CA . LYS A 1 584 ? 33.144 -5.996 37.623 1.00 34.95 ? 584 LYS A CA 1 ATOM 4657 C C . LYS A 1 584 ? 33.270 -5.576 36.168 1.00 38.00 ? 584 LYS A C 1 ATOM 4658 O O . LYS A 1 584 ? 33.742 -6.317 35.304 1.00 36.86 ? 584 LYS A O 1 ATOM 4659 C CB . LYS A 1 584 ? 34.238 -5.306 38.410 1.00 37.56 ? 584 LYS A CB 1 ATOM 4660 C CG . LYS A 1 584 ? 34.408 -5.879 39.799 1.00 38.48 ? 584 LYS A CG 1 ATOM 4661 C CD . LYS A 1 584 ? 35.366 -5.061 40.627 1.00 38.28 ? 584 LYS A CD 1 ATOM 4662 C CE . LYS A 1 584 ? 35.289 -5.571 42.063 1.00 38.56 ? 584 LYS A CE 1 ATOM 4663 N NZ . LYS A 1 584 ? 36.413 -5.016 42.854 1.00 42.85 ? 584 LYS A NZ 1 ATOM 4664 N N . LEU A 1 585 ? 32.826 -4.365 35.903 1.00 29.67 ? 585 LEU A N 1 ATOM 4665 C CA . LEU A 1 585 ? 33.049 -3.768 34.646 1.00 32.17 ? 585 LEU A CA 1 ATOM 4666 C C . LEU A 1 585 ? 34.486 -3.275 34.664 1.00 32.25 ? 585 LEU A C 1 ATOM 4667 O O . LEU A 1 585 ? 34.826 -2.404 35.458 1.00 31.53 ? 585 LEU A O 1 ATOM 4668 C CB . LEU A 1 585 ? 32.106 -2.563 34.466 1.00 30.26 ? 585 LEU A CB 1 ATOM 4669 C CG . LEU A 1 585 ? 32.357 -1.743 33.222 1.00 32.65 ? 585 LEU A CG 1 ATOM 4670 C CD1 . LEU A 1 585 ? 32.293 -2.632 31.992 1.00 36.87 ? 585 LEU A CD1 1 ATOM 4671 C CD2 . LEU A 1 585 ? 31.319 -0.643 33.114 1.00 31.92 ? 585 LEU A CD2 1 ATOM 4672 N N . ASP A 1 586 ? 35.319 -3.829 33.801 1.00 32.79 ? 586 ASP A N 1 ATOM 4673 C CA . ASP A 1 586 ? 36.713 -3.429 33.744 1.00 29.86 ? 586 ASP A CA 1 ATOM 4674 C C . ASP A 1 586 ? 36.828 -2.282 32.815 1.00 27.26 ? 586 ASP A C 1 ATOM 4675 O O . ASP A 1 586 ? 36.609 -2.456 31.624 1.00 30.64 ? 586 ASP A O 1 ATOM 4676 C CB . ASP A 1 586 ? 37.579 -4.615 33.289 1.00 31.13 ? 586 ASP A CB 1 ATOM 4677 C CG . ASP A 1 586 ? 39.036 -4.212 32.916 1.00 29.96 ? 586 ASP A CG 1 ATOM 4678 O OD1 . ASP A 1 586 ? 39.427 -3.004 32.926 1.00 31.98 ? 586 ASP A OD1 1 ATOM 4679 O OD2 . ASP A 1 586 ? 39.775 -5.149 32.573 1.00 35.92 ? 586 ASP A OD2 1 ATOM 4680 N N . LEU A 1 587 ? 37.149 -1.092 33.331 1.00 25.94 ? 587 LEU A N 1 ATOM 4681 C CA . LEU A 1 587 ? 37.186 0.105 32.493 1.00 29.39 ? 587 LEU A CA 1 ATOM 4682 C C . LEU A 1 587 ? 38.562 0.461 31.869 1.00 28.78 ? 587 LEU A C 1 ATOM 4683 O O . LEU A 1 587 ? 38.730 1.546 31.306 1.00 30.38 ? 587 LEU A O 1 ATOM 4684 C CB . LEU A 1 587 ? 36.690 1.324 33.263 1.00 31.24 ? 587 LEU A CB 1 ATOM 4685 C CG . LEU A 1 587 ? 35.236 1.285 33.788 1.00 36.71 ? 587 LEU A CG 1 ATOM 4686 C CD1 . LEU A 1 587 ? 34.935 2.471 34.673 1.00 32.02 ? 587 LEU A CD1 1 ATOM 4687 C CD2 . LEU A 1 587 ? 34.220 1.227 32.635 1.00 35.62 ? 587 LEU A CD2 1 ATOM 4688 N N . SER A 1 588 ? 39.550 -0.400 31.969 1.00 33.52 ? 588 SER A N 1 ATOM 4689 C CA . SER A 1 588 ? 40.855 0.016 31.376 1.00 35.48 ? 588 SER A CA 1 ATOM 4690 C C . SER A 1 588 ? 40.713 0.327 29.876 1.00 34.68 ? 588 SER A C 1 ATOM 4691 O O . SER A 1 588 ? 41.268 1.336 29.414 1.00 37.34 ? 588 SER A O 1 ATOM 4692 C CB . SER A 1 588 ? 41.963 -0.996 31.664 1.00 36.00 ? 588 SER A CB 1 ATOM 4693 O OG . SER A 1 588 ? 41.507 -2.324 31.687 1.00 34.56 ? 588 SER A OG 1 ATOM 4694 N N . PRO A 1 589 ? 39.872 -0.450 29.139 1.00 35.26 ? 589 PRO A N 1 ATOM 4695 C CA . PRO A 1 589 ? 39.687 -0.168 27.735 1.00 36.82 ? 589 PRO A CA 1 ATOM 4696 C C . PRO A 1 589 ? 39.197 1.221 27.377 1.00 40.00 ? 589 PRO A C 1 ATOM 4697 O O . PRO A 1 589 ? 39.143 1.535 26.195 1.00 42.46 ? 589 PRO A O 1 ATOM 4698 C CB . PRO A 1 589 ? 38.665 -1.216 27.306 1.00 38.46 ? 589 PRO A CB 1 ATOM 4699 C CG . PRO A 1 589 ? 39.009 -2.389 28.136 1.00 38.57 ? 589 PRO A CG 1 ATOM 4700 C CD . PRO A 1 589 ? 39.400 -1.803 29.465 1.00 33.09 ? 589 PRO A CD 1 ATOM 4701 N N . TRP A 1 590 ? 38.830 2.030 28.367 1.00 35.38 ? 590 TRP A N 1 ATOM 4702 C CA . TRP A 1 590 ? 38.387 3.384 28.122 1.00 33.01 ? 590 TRP A CA 1 ATOM 4703 C C . TRP A 1 590 ? 39.531 4.344 28.374 1.00 38.41 ? 590 TRP A C 1 ATOM 4704 O O . TRP A 1 590 ? 39.404 5.543 28.138 1.00 34.23 ? 590 TRP A O 1 ATOM 4705 C CB . TRP A 1 590 ? 37.179 3.724 29.016 1.00 30.99 ? 590 TRP A CB 1 ATOM 4706 C CG . TRP A 1 590 ? 35.894 3.174 28.435 1.00 27.23 ? 590 TRP A CG 1 ATOM 4707 C CD1 . TRP A 1 590 ? 34.970 3.868 27.668 1.00 29.56 ? 590 TRP A CD1 1 ATOM 4708 C CD2 . TRP A 1 590 ? 35.420 1.834 28.504 1.00 25.15 ? 590 TRP A CD2 1 ATOM 4709 N NE1 . TRP A 1 590 ? 33.941 3.017 27.287 1.00 27.72 ? 590 TRP A NE1 1 ATOM 4710 C CE2 . TRP A 1 590 ? 34.203 1.770 27.797 1.00 24.59 ? 590 TRP A CE2 1 ATOM 4711 C CE3 . TRP A 1 590 ? 35.888 0.695 29.104 1.00 26.68 ? 590 TRP A CE3 1 ATOM 4712 C CZ2 . TRP A 1 590 ? 33.465 0.622 27.697 1.00 26.75 ? 590 TRP A CZ2 1 ATOM 4713 C CZ3 . TRP A 1 590 ? 35.153 -0.455 29.012 1.00 27.62 ? 590 TRP A CZ3 1 ATOM 4714 C CH2 . TRP A 1 590 ? 33.937 -0.486 28.315 1.00 30.00 ? 590 TRP A CH2 1 ATOM 4715 N N . ALA A 1 591 ? 40.662 3.797 28.819 1.00 43.87 ? 591 ALA A N 1 ATOM 4716 C CA . ALA A 1 591 ? 41.909 4.589 28.990 1.00 51.56 ? 591 ALA A CA 1 ATOM 4717 C C . ALA A 1 591 ? 42.352 5.226 27.668 1.00 45.69 ? 591 ALA A C 1 ATOM 4718 O O . ALA A 1 591 ? 42.765 4.531 26.771 1.00 52.08 ? 591 ALA A O 1 ATOM 4719 C CB . ALA A 1 591 ? 43.012 3.691 29.543 1.00 50.54 ? 591 ALA A CB 1 ATOM 4720 N N . SER A 1 592 ? 42.236 6.538 27.569 1.00 53.49 ? 592 SER A N 1 ATOM 4721 C CA . SER A 1 592 ? 42.534 7.321 26.372 1.00 59.68 ? 592 SER A CA 1 ATOM 4722 C C . SER A 1 592 ? 43.802 8.105 26.593 1.00 65.67 ? 592 SER A C 1 ATOM 4723 O O . SER A 1 592 ? 43.761 9.171 27.204 1.00 57.25 ? 592 SER A O 1 ATOM 4724 C CB . SER A 1 592 ? 41.453 8.372 26.113 1.00 62.02 ? 592 SER A CB 1 ATOM 4725 O OG . SER A 1 592 ? 41.971 9.430 25.284 1.00 59.45 ? 592 SER A OG 1 ATOM 4726 N N . ARG A 1 593 ? 44.922 7.629 26.073 1.00 72.56 ? 593 ARG A N 1 ATOM 4727 C CA . ARG A 1 593 ? 46.163 8.366 26.290 1.00 85.45 ? 593 ARG A CA 1 ATOM 4728 C C . ARG A 1 593 ? 46.464 9.234 25.049 1.00 93.00 ? 593 ARG A C 1 ATOM 4729 O O . ARG A 1 593 ? 45.623 9.327 24.145 1.00 94.10 ? 593 ARG A O 1 ATOM 4730 C CB . ARG A 1 593 ? 47.275 7.409 26.772 1.00 88.40 ? 593 ARG A CB 1 ATOM 4731 C CG . ARG A 1 593 ? 46.946 6.789 28.151 1.00 87.58 ? 593 ARG A CG 1 ATOM 4732 C CD . ARG A 1 593 ? 47.806 7.397 29.257 1.00 90.25 ? 593 ARG A CD 1 ATOM 4733 N NE . ARG A 1 593 ? 47.351 7.074 30.612 1.00 89.74 ? 593 ARG A NE 1 ATOM 4734 C CZ . ARG A 1 593 ? 47.923 7.533 31.728 1.00 89.95 ? 593 ARG A CZ 1 ATOM 4735 N NH1 . ARG A 1 593 ? 48.979 8.337 31.673 1.00 93.36 ? 593 ARG A NH1 1 ATOM 4736 N NH2 . ARG A 1 593 ? 47.443 7.182 32.914 1.00 93.05 ? 593 ARG A NH2 1 ATOM 4737 N N . GLU A 1 594 ? 47.598 9.936 25.054 1.00 102.85 ? 594 GLU A N 1 ATOM 4738 C CA . GLU A 1 594 ? 47.980 10.878 23.978 1.00 106.07 ? 594 GLU A CA 1 ATOM 4739 C C . GLU A 1 594 ? 48.785 10.220 22.845 1.00 107.32 ? 594 GLU A C 1 ATOM 4740 O O . GLU A 1 594 ? 48.550 10.506 21.666 1.00 103.64 ? 594 GLU A O 1 ATOM 4741 C CB . GLU A 1 594 ? 48.801 12.061 24.537 1.00 103.96 ? 594 GLU A CB 1 ATOM 4742 C CG . GLU A 1 594 ? 48.314 12.699 25.855 1.00 96.25 ? 594 GLU A CG 1 ATOM 4743 C CD . GLU A 1 594 ? 46.825 13.016 25.909 1.00 89.57 ? 594 GLU A CD 1 ATOM 4744 O OE1 . GLU A 1 594 ? 46.503 14.147 26.327 1.00 80.90 ? 594 GLU A OE1 1 ATOM 4745 O OE2 . GLU A 1 594 ? 45.977 12.157 25.572 1.00 84.36 ? 594 GLU A OE2 1 ATOM 4746 N N . ASN A 1 595 ? 49.746 9.368 23.212 1.00 102.08 ? 595 ASN A N 1 ATOM 4747 C CA . ASN A 1 595 ? 50.605 8.673 22.246 1.00 95.21 ? 595 ASN A CA 1 ATOM 4748 C C . ASN A 1 595 ? 49.882 7.607 21.417 1.00 91.67 ? 595 ASN A C 1 ATOM 4749 O O . ASN A 1 595 ? 49.282 7.883 20.376 1.00 80.08 ? 595 ASN A O 1 ATOM 4750 C CB . ASN A 1 595 ? 51.767 8.002 22.976 1.00 90.98 ? 595 ASN A CB 1 ATOM 4751 C CG . ASN A 1 595 ? 52.719 8.992 23.606 1.00 87.67 ? 595 ASN A CG 1 ATOM 4752 O OD1 . ASN A 1 595 ? 52.981 10.056 23.058 1.00 85.34 ? 595 ASN A OD1 1 ATOM 4753 N ND2 . ASN A 1 595 ? 53.257 8.635 24.761 1.00 87.92 ? 595 ASN A ND2 1 ATOM 4754 O OXT . ASN A 1 595 ? 49.904 6.426 21.764 1.00 89.83 ? 595 ASN A OXT 1 ATOM 4755 N N . SER B 1 1 ? 21.423 36.051 36.221 1.00 139.80 ? 1 SER B N 1 ATOM 4756 C CA . SER B 1 1 ? 22.481 35.440 37.090 1.00 137.67 ? 1 SER B CA 1 ATOM 4757 C C . SER B 1 1 ? 22.066 35.371 38.575 1.00 139.69 ? 1 SER B C 1 ATOM 4758 O O . SER B 1 1 ? 22.623 36.070 39.429 1.00 137.08 ? 1 SER B O 1 ATOM 4759 C CB . SER B 1 1 ? 23.813 36.191 36.937 1.00 134.92 ? 1 SER B CB 1 ATOM 4760 O OG . SER B 1 1 ? 23.658 37.579 37.173 1.00 129.84 ? 1 SER B OG 1 ATOM 4761 N N . TRP B 1 2 ? 21.066 34.537 38.860 1.00 142.90 ? 2 TRP B N 1 ATOM 4762 C CA . TRP B 1 2 ? 20.779 34.074 40.225 1.00 138.55 ? 2 TRP B CA 1 ATOM 4763 C C . TRP B 1 2 ? 19.852 32.835 40.213 1.00 137.96 ? 2 TRP B C 1 ATOM 4764 O O . TRP B 1 2 ? 18.709 32.953 40.655 1.00 135.00 ? 2 TRP B O 1 ATOM 4765 C CB . TRP B 1 2 ? 20.172 35.197 41.105 1.00 130.47 ? 2 TRP B CB 1 ATOM 4766 C CG . TRP B 1 2 ? 20.200 34.864 42.578 1.00 128.17 ? 2 TRP B CG 1 ATOM 4767 C CD1 . TRP B 1 2 ? 19.137 34.521 43.357 1.00 131.02 ? 2 TRP B CD1 1 ATOM 4768 C CD2 . TRP B 1 2 ? 21.359 34.814 43.419 1.00 130.59 ? 2 TRP B CD2 1 ATOM 4769 N NE1 . TRP B 1 2 ? 19.559 34.271 44.647 1.00 133.84 ? 2 TRP B NE1 1 ATOM 4770 C CE2 . TRP B 1 2 ? 20.917 34.441 44.713 1.00 132.60 ? 2 TRP B CE2 1 ATOM 4771 C CE3 . TRP B 1 2 ? 22.726 35.052 43.214 1.00 128.18 ? 2 TRP B CE3 1 ATOM 4772 C CZ2 . TRP B 1 2 ? 21.794 34.305 45.800 1.00 128.21 ? 2 TRP B CZ2 1 ATOM 4773 C CZ3 . TRP B 1 2 ? 23.599 34.914 44.292 1.00 126.32 ? 2 TRP B CZ3 1 ATOM 4774 C CH2 . TRP B 1 2 ? 23.127 34.541 45.568 1.00 127.71 ? 2 TRP B CH2 1 ATOM 4775 N N . GLU B 1 3 ? 20.288 31.656 39.722 1.00 135.30 ? 3 GLU B N 1 ATOM 4776 C CA . GLU B 1 3 ? 21.613 31.372 39.093 1.00 120.01 ? 3 GLU B CA 1 ATOM 4777 C C . GLU B 1 3 ? 21.595 30.250 38.008 1.00 110.02 ? 3 GLU B C 1 ATOM 4778 O O . GLU B 1 3 ? 22.663 29.801 37.556 1.00 90.73 ? 3 GLU B O 1 ATOM 4779 C CB . GLU B 1 3 ? 22.610 30.941 40.187 1.00 112.27 ? 3 GLU B CB 1 ATOM 4780 C CG . GLU B 1 3 ? 23.753 31.912 40.413 1.00 108.17 ? 3 GLU B CG 1 ATOM 4781 C CD . GLU B 1 3 ? 24.619 31.517 41.580 1.00 103.15 ? 3 GLU B CD 1 ATOM 4782 O OE1 . GLU B 1 3 ? 25.388 30.545 41.436 1.00 96.93 ? 3 GLU B OE1 1 ATOM 4783 O OE2 . GLU B 1 3 ? 24.531 32.185 42.636 1.00 104.46 ? 3 GLU B OE2 1 ATOM 4784 N N . VAL B 1 4 ? 20.403 29.866 37.536 1.00 107.23 ? 4 VAL B N 1 ATOM 4785 C CA . VAL B 1 4 ? 20.147 28.499 37.041 1.00 105.04 ? 4 VAL B CA 1 ATOM 4786 C C . VAL B 1 4 ? 21.413 27.915 36.420 1.00 105.33 ? 4 VAL B C 1 ATOM 4787 O O . VAL B 1 4 ? 22.177 28.623 35.748 1.00 103.75 ? 4 VAL B O 1 ATOM 4788 C CB . VAL B 1 4 ? 18.960 28.442 36.033 1.00 107.71 ? 4 VAL B CB 1 ATOM 4789 C CG1 . VAL B 1 4 ? 18.879 27.082 35.333 1.00 101.69 ? 4 VAL B CG1 1 ATOM 4790 C CG2 . VAL B 1 4 ? 17.634 28.758 36.730 1.00 103.37 ? 4 VAL B CG2 1 ATOM 4791 N N . GLY B 1 5 ? 21.631 26.627 36.674 1.00 102.87 ? 5 GLY B N 1 ATOM 4792 C CA . GLY B 1 5 ? 22.770 25.895 36.157 1.00 98.56 ? 5 GLY B CA 1 ATOM 4793 C C . GLY B 1 5 ? 22.363 25.339 34.827 1.00 97.00 ? 5 GLY B C 1 ATOM 4794 O O . GLY B 1 5 ? 22.174 24.142 34.687 1.00 89.49 ? 5 GLY B O 1 ATOM 4795 N N . CYS B 1 6 ? 22.190 26.228 33.858 1.00 102.80 ? 6 CYS B N 1 ATOM 4796 C CA . CYS B 1 6 ? 21.849 25.822 32.510 1.00 112.37 ? 6 CYS B CA 1 ATOM 4797 C C . CYS B 1 6 ? 22.726 26.512 31.454 1.00 118.89 ? 6 CYS B C 1 ATOM 4798 O O . CYS B 1 6 ? 23.430 27.482 31.744 1.00 100.83 ? 6 CYS B O 1 ATOM 4799 C CB . CYS B 1 6 ? 20.374 26.076 32.214 1.00 107.09 ? 6 CYS B CB 1 ATOM 4800 S SG . CYS B 1 6 ? 19.830 25.066 30.825 1.00 102.87 ? 6 CYS B SG 1 ATOM 4801 N N . GLY B 1 7 ? 22.662 25.980 30.234 1.00 134.67 ? 7 GLY B N 1 ATOM 4802 C CA . GLY B 1 7 ? 23.475 26.426 29.099 1.00 143.60 ? 7 GLY B CA 1 ATOM 4803 C C . GLY B 1 7 ? 24.576 25.402 28.826 1.00 158.19 ? 7 GLY B C 1 ATOM 4804 O O . GLY B 1 7 ? 25.553 25.342 29.572 1.00 173.58 ? 7 GLY B O 1 ATOM 4805 N N . ALA B 1 8 ? 24.426 24.589 27.774 1.00 161.63 ? 8 ALA B N 1 ATOM 4806 C CA . ALA B 1 8 ? 25.384 23.497 27.480 1.00 158.12 ? 8 ALA B CA 1 ATOM 4807 C C . ALA B 1 8 ? 25.667 23.277 25.975 1.00 160.94 ? 8 ALA B C 1 ATOM 4808 O O . ALA B 1 8 ? 24.791 22.789 25.261 1.00 159.62 ? 8 ALA B O 1 ATOM 4809 C CB . ALA B 1 8 ? 24.900 22.194 28.114 1.00 150.75 ? 8 ALA B CB 1 ATOM 4810 N N . PRO B 1 9 ? 26.882 23.640 25.492 1.00 164.56 ? 9 PRO B N 1 ATOM 4811 C CA . PRO B 1 9 ? 27.370 23.249 24.156 1.00 165.37 ? 9 PRO B CA 1 ATOM 4812 C C . PRO B 1 9 ? 28.222 21.951 24.183 1.00 167.05 ? 9 PRO B C 1 ATOM 4813 O O . PRO B 1 9 ? 27.908 21.026 24.937 1.00 165.62 ? 9 PRO B O 1 ATOM 4814 C CB . PRO B 1 9 ? 28.214 24.467 23.714 1.00 158.45 ? 9 PRO B CB 1 ATOM 4815 C CG . PRO B 1 9 ? 28.269 25.400 24.886 1.00 157.50 ? 9 PRO B CG 1 ATOM 4816 C CD . PRO B 1 9 ? 27.768 24.654 26.086 1.00 159.50 ? 9 PRO B CD 1 ATOM 4817 N N . VAL B 1 10 ? 29.241 21.866 23.323 1.00 163.09 ? 10 VAL B N 1 ATOM 4818 C CA . VAL B 1 10 ? 30.306 20.863 23.427 1.00 155.66 ? 10 VAL B CA 1 ATOM 4819 C C . VAL B 1 10 ? 31.693 21.548 23.475 1.00 168.42 ? 10 VAL B C 1 ATOM 4820 O O . VAL B 1 10 ? 32.233 21.907 22.427 1.00 183.06 ? 10 VAL B O 1 ATOM 4821 C CB . VAL B 1 10 ? 30.237 19.902 22.212 1.00 138.18 ? 10 VAL B CB 1 ATOM 4822 C CG1 . VAL B 1 10 ? 31.309 18.826 22.302 1.00 133.73 ? 10 VAL B CG1 1 ATOM 4823 C CG2 . VAL B 1 10 ? 28.851 19.293 22.096 1.00 128.71 ? 10 VAL B CG2 1 ATOM 4824 N N . PRO B 1 11 ? 32.271 21.746 24.690 1.00 166.06 ? 11 PRO B N 1 ATOM 4825 C CA . PRO B 1 11 ? 33.607 22.355 24.813 1.00 159.41 ? 11 PRO B CA 1 ATOM 4826 C C . PRO B 1 11 ? 34.701 21.480 24.196 1.00 169.28 ? 11 PRO B C 1 ATOM 4827 O O . PRO B 1 11 ? 34.525 20.269 24.064 1.00 176.85 ? 11 PRO B O 1 ATOM 4828 C CB . PRO B 1 11 ? 33.786 22.526 26.328 1.00 146.98 ? 11 PRO B CB 1 ATOM 4829 C CG . PRO B 1 11 ? 32.391 22.603 26.839 1.00 145.31 ? 11 PRO B CG 1 ATOM 4830 C CD . PRO B 1 11 ? 31.655 21.589 26.014 1.00 155.65 ? 11 PRO B CD 1 ATOM 4831 N N . LEU B 1 12 ? 35.813 22.103 23.813 1.00 168.39 ? 12 LEU B N 1 ATOM 4832 C CA . LEU B 1 12 ? 36.789 21.484 22.907 1.00 162.66 ? 12 LEU B CA 1 ATOM 4833 C C . LEU B 1 12 ? 38.284 21.648 23.288 1.00 161.50 ? 12 LEU B C 1 ATOM 4834 O O . LEU B 1 12 ? 39.127 20.986 22.683 1.00 163.34 ? 12 LEU B O 1 ATOM 4835 C CB . LEU B 1 12 ? 36.546 22.056 21.491 1.00 153.47 ? 12 LEU B CB 1 ATOM 4836 C CG . LEU B 1 12 ? 35.806 21.320 20.340 1.00 143.09 ? 12 LEU B CG 1 ATOM 4837 C CD1 . LEU B 1 12 ? 35.021 20.082 20.767 1.00 137.93 ? 12 LEU B CD1 1 ATOM 4838 C CD2 . LEU B 1 12 ? 34.892 22.296 19.601 1.00 132.54 ? 12 LEU B CD2 1 ATOM 4839 N N . VAL B 1 13 ? 38.598 22.481 24.294 1.00 157.91 ? 13 VAL B N 1 ATOM 4840 C CA . VAL B 1 13 ? 39.966 23.008 24.544 1.00 148.76 ? 13 VAL B CA 1 ATOM 4841 C C . VAL B 1 13 ? 40.381 22.942 26.050 1.00 147.31 ? 13 VAL B C 1 ATOM 4842 O O . VAL B 1 13 ? 39.511 23.046 26.923 1.00 156.60 ? 13 VAL B O 1 ATOM 4843 C CB . VAL B 1 13 ? 40.043 24.473 24.003 1.00 138.55 ? 13 VAL B CB 1 ATOM 4844 C CG1 . VAL B 1 13 ? 41.328 25.180 24.416 1.00 135.12 ? 13 VAL B CG1 1 ATOM 4845 C CG2 . VAL B 1 13 ? 39.890 24.501 22.480 1.00 131.72 ? 13 VAL B CG2 1 ATOM 4846 N N . THR B 1 14 ? 41.681 22.717 26.338 1.00 135.59 ? 14 THR B N 1 ATOM 4847 C CA . THR B 1 14 ? 42.304 22.923 27.695 1.00 120.30 ? 14 THR B CA 1 ATOM 4848 C C . THR B 1 14 ? 43.283 24.126 27.687 1.00 109.36 ? 14 THR B C 1 ATOM 4849 O O . THR B 1 14 ? 43.990 24.342 26.697 1.00 109.24 ? 14 THR B O 1 ATOM 4850 C CB . THR B 1 14 ? 43.027 21.659 28.205 1.00 116.83 ? 14 THR B CB 1 ATOM 4851 O OG1 . THR B 1 14 ? 42.132 20.547 28.126 1.00 114.75 ? 14 THR B OG1 1 ATOM 4852 C CG2 . THR B 1 14 ? 43.489 21.821 29.664 1.00 116.22 ? 14 THR B CG2 1 ATOM 4853 N N . CYS B 1 15 ? 43.355 24.896 28.778 1.00 94.24 ? 15 CYS B N 1 ATOM 4854 C CA . CYS B 1 15 ? 43.947 26.242 28.679 1.00 89.72 ? 15 CYS B CA 1 ATOM 4855 C C . CYS B 1 15 ? 45.441 26.269 28.802 1.00 90.35 ? 15 CYS B C 1 ATOM 4856 O O . CYS B 1 15 ? 45.993 26.977 29.667 1.00 89.47 ? 15 CYS B O 1 ATOM 4857 C CB . CYS B 1 15 ? 43.388 27.218 29.704 1.00 88.31 ? 15 CYS B CB 1 ATOM 4858 S SG . CYS B 1 15 ? 41.704 27.761 29.424 1.00 88.05 ? 15 CYS B SG 1 ATOM 4859 N N . ASP B 1 16 ? 46.087 25.564 27.876 1.00 90.06 ? 16 ASP B N 1 ATOM 4860 C CA . ASP B 1 16 ? 47.530 25.404 27.902 1.00 84.22 ? 16 ASP B CA 1 ATOM 4861 C C . ASP B 1 16 ? 48.111 26.786 28.251 1.00 80.66 ? 16 ASP B C 1 ATOM 4862 O O . ASP B 1 16 ? 47.920 27.759 27.517 1.00 72.36 ? 16 ASP B O 1 ATOM 4863 C CB . ASP B 1 16 ? 48.065 24.810 26.582 1.00 79.03 ? 16 ASP B CB 1 ATOM 4864 C CG . ASP B 1 16 ? 48.417 25.871 25.567 1.00 79.96 ? 16 ASP B CG 1 ATOM 4865 O OD1 . ASP B 1 16 ? 47.506 26.394 24.897 1.00 73.55 ? 16 ASP B OD1 1 ATOM 4866 O OD2 . ASP B 1 16 ? 49.609 26.205 25.448 1.00 73.92 ? 16 ASP B OD2 1 ATOM 4867 N N . GLU B 1 17 ? 48.766 26.864 29.414 1.00 82.45 ? 17 GLU B N 1 ATOM 4868 C CA . GLU B 1 17 ? 49.104 28.146 30.047 1.00 74.93 ? 17 GLU B CA 1 ATOM 4869 C C . GLU B 1 17 ? 49.469 29.060 28.935 1.00 68.95 ? 17 GLU B C 1 ATOM 4870 O O . GLU B 1 17 ? 48.673 29.893 28.511 1.00 60.19 ? 17 GLU B O 1 ATOM 4871 C CB . GLU B 1 17 ? 50.301 28.020 31.011 1.00 74.11 ? 17 GLU B CB 1 ATOM 4872 C CG . GLU B 1 17 ? 50.752 29.350 31.613 1.00 67.71 ? 17 GLU B CG 1 ATOM 4873 C CD . GLU B 1 17 ? 49.763 29.906 32.642 1.00 70.58 ? 17 GLU B CD 1 ATOM 4874 O OE1 . GLU B 1 17 ? 49.510 31.128 32.658 1.00 59.09 ? 17 GLU B OE1 1 ATOM 4875 O OE2 . GLU B 1 17 ? 49.215 29.117 33.448 1.00 71.61 ? 17 GLU B OE2 1 ATOM 4876 N N . GLN B 1 18 ? 50.644 28.807 28.388 1.00 73.96 ? 18 GLN B N 1 ATOM 4877 C CA . GLN B 1 18 ? 51.362 29.832 27.695 1.00 75.05 ? 18 GLN B CA 1 ATOM 4878 C C . GLN B 1 18 ? 51.163 29.838 26.182 1.00 73.55 ? 18 GLN B C 1 ATOM 4879 O O . GLN B 1 18 ? 51.905 30.543 25.498 1.00 70.20 ? 18 GLN B O 1 ATOM 4880 C CB . GLN B 1 18 ? 52.853 29.697 28.024 1.00 77.07 ? 18 GLN B CB 1 ATOM 4881 C CG . GLN B 1 18 ? 53.596 31.015 28.117 1.00 77.00 ? 18 GLN B CG 1 ATOM 4882 C CD . GLN B 1 18 ? 54.329 31.165 29.431 1.00 76.75 ? 18 GLN B CD 1 ATOM 4883 O OE1 . GLN B 1 18 ? 54.138 32.139 30.166 1.00 75.13 ? 18 GLN B OE1 1 ATOM 4884 N NE2 . GLN B 1 18 ? 55.161 30.186 29.749 1.00 76.98 ? 18 GLN B NE2 1 ATOM 4885 N N . SER B 1 19 ? 50.176 29.118 25.632 1.00 72.74 ? 19 SER B N 1 ATOM 4886 C CA . SER B 1 19 ? 49.977 29.244 24.184 1.00 68.04 ? 19 SER B CA 1 ATOM 4887 C C . SER B 1 19 ? 49.899 30.737 23.877 1.00 59.16 ? 19 SER B C 1 ATOM 4888 O O . SER B 1 19 ? 49.079 31.436 24.486 1.00 59.92 ? 19 SER B O 1 ATOM 4889 C CB . SER B 1 19 ? 48.714 28.619 23.671 1.00 67.98 ? 19 SER B CB 1 ATOM 4890 O OG . SER B 1 19 ? 48.521 28.922 22.315 1.00 67.85 ? 19 SER B OG 1 ATOM 4891 N N . PRO B 1 20 ? 50.772 31.227 22.964 1.00 51.96 ? 20 PRO B N 1 ATOM 4892 C CA . PRO B 1 20 ? 50.822 32.615 22.500 1.00 49.15 ? 20 PRO B CA 1 ATOM 4893 C C . PRO B 1 20 ? 49.817 32.846 21.335 1.00 49.33 ? 20 PRO B C 1 ATOM 4894 O O . PRO B 1 20 ? 49.779 33.931 20.721 1.00 44.35 ? 20 PRO B O 1 ATOM 4895 C CB . PRO B 1 20 ? 52.233 32.725 21.961 1.00 47.60 ? 20 PRO B CB 1 ATOM 4896 C CG . PRO B 1 20 ? 52.445 31.376 21.325 1.00 46.33 ? 20 PRO B CG 1 ATOM 4897 C CD . PRO B 1 20 ? 51.727 30.386 22.206 1.00 47.64 ? 20 PRO B CD 1 ATOM 4898 N N . TYR B 1 21 ? 49.041 31.811 21.018 1.00 54.38 ? 21 TYR B N 1 ATOM 4899 C CA . TYR B 1 21 ? 48.055 31.893 19.939 1.00 50.89 ? 21 TYR B CA 1 ATOM 4900 C C . TYR B 1 21 ? 46.656 31.664 20.480 1.00 48.65 ? 21 TYR B C 1 ATOM 4901 O O . TYR B 1 21 ? 46.466 30.965 21.465 1.00 43.67 ? 21 TYR B O 1 ATOM 4902 C CB . TYR B 1 21 ? 48.372 30.844 18.878 1.00 50.84 ? 21 TYR B CB 1 ATOM 4903 C CG . TYR B 1 21 ? 49.824 30.867 18.460 1.00 50.91 ? 21 TYR B CG 1 ATOM 4904 C CD1 . TYR B 1 21 ? 50.399 32.040 18.016 1.00 52.80 ? 21 TYR B CD1 1 ATOM 4905 C CD2 . TYR B 1 21 ? 50.616 29.722 18.525 1.00 52.79 ? 21 TYR B CD2 1 ATOM 4906 C CE1 . TYR B 1 21 ? 51.719 32.105 17.644 1.00 56.37 ? 21 TYR B CE1 1 ATOM 4907 C CE2 . TYR B 1 21 ? 51.950 29.765 18.136 1.00 56.97 ? 21 TYR B CE2 1 ATOM 4908 C CZ . TYR B 1 21 ? 52.500 30.964 17.708 1.00 54.60 ? 21 TYR B CZ 1 ATOM 4909 O OH . TYR B 1 21 ? 53.816 31.044 17.318 1.00 52.44 ? 21 TYR B OH 1 ATOM 4910 N N . ARG B 1 22 ? 45.675 32.239 19.799 1.00 45.22 ? 22 ARG B N 1 ATOM 4911 C CA . ARG B 1 22 ? 44.312 32.014 20.144 1.00 37.41 ? 22 ARG B CA 1 ATOM 4912 C C . ARG B 1 22 ? 43.919 30.597 19.881 1.00 36.35 ? 22 ARG B C 1 ATOM 4913 O O . ARG B 1 22 ? 44.412 29.993 18.935 1.00 36.09 ? 22 ARG B O 1 ATOM 4914 C CB . ARG B 1 22 ? 43.438 32.870 19.242 1.00 37.57 ? 22 ARG B CB 1 ATOM 4915 C CG . ARG B 1 22 ? 43.682 34.360 19.349 1.00 34.36 ? 22 ARG B CG 1 ATOM 4916 C CD . ARG B 1 22 ? 42.771 35.044 18.376 1.00 30.52 ? 22 ARG B CD 1 ATOM 4917 N NE . ARG B 1 22 ? 42.900 36.483 18.373 1.00 27.78 ? 22 ARG B NE 1 ATOM 4918 C CZ . ARG B 1 22 ? 42.240 37.315 19.156 1.00 24.86 ? 22 ARG B CZ 1 ATOM 4919 N NH1 . ARG B 1 22 ? 41.415 36.868 20.094 1.00 29.63 ? 22 ARG B NH1 1 ATOM 4920 N NH2 . ARG B 1 22 ? 42.425 38.610 18.999 1.00 23.48 ? 22 ARG B NH2 1 ATOM 4921 N N . THR B 1 23 ? 42.952 30.092 20.623 1.00 34.48 ? 23 THR B N 1 ATOM 4922 C CA . THR B 1 23 ? 42.277 28.877 20.216 1.00 37.05 ? 23 THR B CA 1 ATOM 4923 C C . THR B 1 23 ? 41.360 29.243 19.038 1.00 37.20 ? 23 THR B C 1 ATOM 4924 O O . THR B 1 23 ? 41.126 30.429 18.767 1.00 38.61 ? 23 THR B O 1 ATOM 4925 C CB . THR B 1 23 ? 41.417 28.323 21.367 1.00 43.30 ? 23 THR B CB 1 ATOM 4926 O OG1 . THR B 1 23 ? 40.462 29.328 21.746 1.00 43.00 ? 23 THR B OG1 1 ATOM 4927 C CG2 . THR B 1 23 ? 42.302 27.989 22.596 1.00 41.28 ? 23 THR B CG2 1 ATOM 4928 N N . ILE B 1 24 ? 40.868 28.222 18.348 1.00 39.74 ? 24 ILE B N 1 ATOM 4929 C CA . ILE B 1 24 ? 39.935 28.395 17.246 1.00 40.71 ? 24 ILE B CA 1 ATOM 4930 C C . ILE B 1 24 ? 38.546 28.813 17.742 1.00 41.97 ? 24 ILE B C 1 ATOM 4931 O O . ILE B 1 24 ? 37.960 29.757 17.206 1.00 49.22 ? 24 ILE B O 1 ATOM 4932 C CB . ILE B 1 24 ? 39.878 27.147 16.355 1.00 39.75 ? 24 ILE B CB 1 ATOM 4933 C CG1 . ILE B 1 24 ? 41.078 27.170 15.368 1.00 38.86 ? 24 ILE B CG1 1 ATOM 4934 C CG2 . ILE B 1 24 ? 38.566 27.080 15.558 1.00 41.19 ? 24 ILE B CG2 1 ATOM 4935 C CD1 . ILE B 1 24 ? 41.130 28.367 14.420 1.00 40.86 ? 24 ILE B CD1 1 ATOM 4936 N N . THR B 1 25 ? 38.090 28.172 18.817 1.00 43.04 ? 25 THR B N 1 ATOM 4937 C CA . THR B 1 25 ? 36.751 28.395 19.397 1.00 37.65 ? 25 THR B CA 1 ATOM 4938 C C . THR B 1 25 ? 36.636 29.625 20.267 1.00 30.83 ? 25 THR B C 1 ATOM 4939 O O . THR B 1 25 ? 35.559 29.930 20.749 1.00 31.23 ? 25 THR B O 1 ATOM 4940 C CB . THR B 1 25 ? 36.378 27.254 20.341 1.00 38.52 ? 25 THR B CB 1 ATOM 4941 O OG1 . THR B 1 25 ? 37.298 27.279 21.426 1.00 41.05 ? 25 THR B OG1 1 ATOM 4942 C CG2 . THR B 1 25 ? 36.455 25.919 19.640 1.00 40.59 ? 25 THR B CG2 1 ATOM 4943 N N . GLY B 1 26 ? 37.744 30.286 20.519 1.00 30.22 ? 26 GLY B N 1 ATOM 4944 C CA . GLY B 1 26 ? 37.822 31.428 21.427 1.00 27.17 ? 26 GLY B CA 1 ATOM 4945 C C . GLY B 1 26 ? 37.975 31.131 22.909 1.00 32.87 ? 26 GLY B C 1 ATOM 4946 O O . GLY B 1 26 ? 38.167 32.066 23.720 1.00 35.32 ? 26 GLY B O 1 ATOM 4947 N N . ASP B 1 27 ? 37.874 29.855 23.282 1.00 38.71 ? 27 ASP B N 1 ATOM 4948 C CA . ASP B 1 27 ? 38.038 29.443 24.698 1.00 43.89 ? 27 ASP B CA 1 ATOM 4949 C C . ASP B 1 27 ? 39.416 29.783 25.232 1.00 43.52 ? 27 ASP B C 1 ATOM 4950 O O . ASP B 1 27 ? 40.354 29.987 24.466 1.00 46.23 ? 27 ASP B O 1 ATOM 4951 C CB . ASP B 1 27 ? 37.794 27.928 24.862 1.00 45.23 ? 27 ASP B CB 1 ATOM 4952 C CG . ASP B 1 27 ? 36.332 27.536 24.654 1.00 45.60 ? 27 ASP B CG 1 ATOM 4953 O OD1 . ASP B 1 27 ? 35.512 27.767 25.561 1.00 44.65 ? 27 ASP B OD1 1 ATOM 4954 O OD2 . ASP B 1 27 ? 36.008 26.955 23.595 1.00 48.02 ? 27 ASP B OD2 1 ATOM 4955 N N . CYS B 1 28 ? 39.518 29.891 26.552 1.00 48.48 ? 28 CYS B N 1 ATOM 4956 C CA . CYS B 1 28 ? 40.770 30.225 27.246 1.00 47.23 ? 28 CYS B CA 1 ATOM 4957 C C . CYS B 1 28 ? 41.291 31.643 27.023 1.00 48.07 ? 28 CYS B C 1 ATOM 4958 O O . CYS B 1 28 ? 42.329 31.996 27.558 1.00 54.77 ? 28 CYS B O 1 ATOM 4959 C CB . CYS B 1 28 ? 41.840 29.190 26.902 1.00 52.61 ? 28 CYS B CB 1 ATOM 4960 S SG . CYS B 1 28 ? 41.339 27.547 27.428 1.00 62.41 ? 28 CYS B SG 1 ATOM 4961 N N . ASN B 1 29 ? 40.590 32.483 26.257 1.00 44.35 ? 29 ASN B N 1 ATOM 4962 C CA . ASN B 1 29 ? 41.019 33.884 26.117 1.00 40.93 ? 29 ASN B CA 1 ATOM 4963 C C . ASN B 1 29 ? 40.992 34.589 27.458 1.00 41.13 ? 29 ASN B C 1 ATOM 4964 O O . ASN B 1 29 ? 41.920 35.301 27.806 1.00 43.39 ? 29 ASN B O 1 ATOM 4965 C CB . ASN B 1 29 ? 40.106 34.635 25.140 1.00 42.01 ? 29 ASN B CB 1 ATOM 4966 C CG . ASN B 1 29 ? 40.622 36.014 24.765 1.00 40.27 ? 29 ASN B CG 1 ATOM 4967 O OD1 . ASN B 1 29 ? 40.776 36.911 25.609 1.00 44.26 ? 29 ASN B OD1 1 ATOM 4968 N ND2 . ASN B 1 29 ? 40.808 36.226 23.461 1.00 44.18 ? 29 ASN B ND2 1 ATOM 4969 N N . ASN B 1 30 ? 39.876 34.451 28.168 1.00 43.67 ? 30 ASN B N 1 ATOM 4970 C CA . ASN B 1 30 ? 39.764 34.887 29.565 1.00 45.54 ? 30 ASN B CA 1 ATOM 4971 C C . ASN B 1 30 ? 40.120 33.722 30.501 1.00 51.61 ? 30 ASN B C 1 ATOM 4972 O O . ASN B 1 30 ? 39.429 32.678 30.525 1.00 49.48 ? 30 ASN B O 1 ATOM 4973 C CB . ASN B 1 30 ? 38.358 35.393 29.861 1.00 47.14 ? 30 ASN B CB 1 ATOM 4974 C CG . ASN B 1 30 ? 38.269 36.102 31.183 1.00 40.97 ? 30 ASN B CG 1 ATOM 4975 O OD1 . ASN B 1 30 ? 38.295 35.469 32.233 1.00 53.46 ? 30 ASN B OD1 1 ATOM 4976 N ND2 . ASN B 1 30 ? 38.164 37.410 31.150 1.00 40.06 ? 30 ASN B ND2 1 ATOM 4977 N N . ARG B 1 31 ? 41.187 33.908 31.285 1.00 53.88 ? 31 ARG B N 1 ATOM 4978 C CA . ARG B 1 31 ? 41.735 32.806 32.111 1.00 53.75 ? 31 ARG B CA 1 ATOM 4979 C C . ARG B 1 31 ? 40.810 32.512 33.299 1.00 54.89 ? 31 ARG B C 1 ATOM 4980 O O . ARG B 1 31 ? 40.468 31.356 33.559 1.00 49.49 ? 31 ARG B O 1 ATOM 4981 C CB . ARG B 1 31 ? 43.154 33.133 32.602 1.00 58.67 ? 31 ARG B CB 1 ATOM 4982 C CG . ARG B 1 31 ? 44.023 31.898 32.904 1.00 66.40 ? 31 ARG B CG 1 ATOM 4983 C CD . ARG B 1 31 ? 44.692 31.304 31.684 1.00 63.24 ? 31 ARG B CD 1 ATOM 4984 N NE . ARG B 1 31 ? 45.633 32.242 31.088 1.00 59.25 ? 31 ARG B NE 1 ATOM 4985 C CZ . ARG B 1 31 ? 46.710 31.914 30.383 1.00 60.87 ? 31 ARG B CZ 1 ATOM 4986 N NH1 . ARG B 1 31 ? 47.306 32.858 29.641 1.00 60.67 ? 31 ARG B NH1 1 ATOM 4987 N NH2 . ARG B 1 31 ? 47.191 30.666 30.416 1.00 60.02 ? 31 ARG B NH2 1 ATOM 4988 N N . ARG B 1 32 ? 40.363 33.574 33.980 1.00 56.94 ? 32 ARG B N 1 ATOM 4989 C CA . ARG B 1 32 ? 39.405 33.444 35.092 1.00 57.07 ? 32 ARG B CA 1 ATOM 4990 C C . ARG B 1 32 ? 38.125 32.744 34.627 1.00 53.95 ? 32 ARG B C 1 ATOM 4991 O O . ARG B 1 32 ? 37.664 31.810 35.259 1.00 52.45 ? 32 ARG B O 1 ATOM 4992 C CB . ARG B 1 32 ? 39.113 34.837 35.686 1.00 65.18 ? 32 ARG B CB 1 ATOM 4993 C CG . ARG B 1 32 ? 38.408 34.892 37.042 1.00 72.71 ? 32 ARG B CG 1 ATOM 4994 C CD . ARG B 1 32 ? 38.551 36.282 37.672 1.00 78.63 ? 32 ARG B CD 1 ATOM 4995 N NE . ARG B 1 32 ? 37.999 37.381 36.858 1.00 83.03 ? 32 ARG B NE 1 ATOM 4996 C CZ . ARG B 1 32 ? 38.339 38.668 36.995 1.00 81.23 ? 32 ARG B CZ 1 ATOM 4997 N NH1 . ARG B 1 32 ? 37.790 39.593 36.209 1.00 79.87 ? 32 ARG B NH1 1 ATOM 4998 N NH2 . ARG B 1 32 ? 39.247 39.046 37.897 1.00 81.14 ? 32 ARG B NH2 1 ATOM 4999 N N . SER B 1 33 ? 37.564 33.149 33.479 1.00 59.58 ? 33 SER B N 1 ATOM 5000 C CA . SER B 1 33 ? 36.364 32.485 32.930 1.00 45.00 ? 33 SER B CA 1 ATOM 5001 C C . SER B 1 33 ? 36.544 32.089 31.444 1.00 49.76 ? 33 SER B C 1 ATOM 5002 O O . SER B 1 33 ? 36.266 32.878 30.528 1.00 43.89 ? 33 SER B O 1 ATOM 5003 C CB . SER B 1 33 ? 35.134 33.355 33.151 1.00 46.28 ? 33 SER B CB 1 ATOM 5004 O OG . SER B 1 33 ? 33.982 32.575 32.863 1.00 55.10 ? 33 SER B OG 1 ATOM 5005 N N . PRO B 1 34 ? 37.020 30.857 31.204 1.00 46.33 ? 34 PRO B N 1 ATOM 5006 C CA . PRO B 1 34 ? 37.566 30.488 29.897 1.00 48.42 ? 34 PRO B CA 1 ATOM 5007 C C . PRO B 1 34 ? 36.596 30.449 28.679 1.00 46.01 ? 34 PRO B C 1 ATOM 5008 O O . PRO B 1 34 ? 37.048 30.590 27.517 1.00 43.27 ? 34 PRO B O 1 ATOM 5009 C CB . PRO B 1 34 ? 38.183 29.099 30.152 1.00 53.33 ? 34 PRO B CB 1 ATOM 5010 C CG . PRO B 1 34 ? 37.500 28.569 31.372 1.00 49.91 ? 34 PRO B CG 1 ATOM 5011 C CD . PRO B 1 34 ? 37.180 29.776 32.201 1.00 48.20 ? 34 PRO B CD 1 ATOM 5012 N N . ALA B 1 35 ? 35.309 30.258 28.941 1.00 41.73 ? 35 ALA B N 1 ATOM 5013 C CA . ALA B 1 35 ? 34.294 30.253 27.889 1.00 38.14 ? 35 ALA B CA 1 ATOM 5014 C C . ALA B 1 35 ? 33.817 31.635 27.464 1.00 33.55 ? 35 ALA B C 1 ATOM 5015 O O . ALA B 1 35 ? 33.135 31.751 26.458 1.00 40.61 ? 35 ALA B O 1 ATOM 5016 C CB . ALA B 1 35 ? 33.108 29.453 28.342 1.00 42.40 ? 35 ALA B CB 1 ATOM 5017 N N . LEU B 1 36 ? 34.154 32.666 28.178 1.00 34.68 ? 36 LEU B N 1 ATOM 5018 C CA . LEU B 1 36 ? 33.741 33.975 27.761 1.00 37.57 ? 36 LEU B CA 1 ATOM 5019 C C . LEU B 1 36 ? 34.204 34.357 26.378 1.00 38.72 ? 36 LEU B C 1 ATOM 5020 O O . LEU B 1 36 ? 35.383 34.393 26.111 1.00 32.29 ? 36 LEU B O 1 ATOM 5021 C CB . LEU B 1 36 ? 34.216 35.004 28.730 1.00 37.03 ? 36 LEU B CB 1 ATOM 5022 C CG . LEU B 1 36 ? 33.514 35.026 30.052 1.00 42.90 ? 36 LEU B CG 1 ATOM 5023 C CD1 . LEU B 1 36 ? 33.695 36.411 30.609 1.00 43.85 ? 36 LEU B CD1 1 ATOM 5024 C CD2 . LEU B 1 36 ? 32.029 34.675 29.934 1.00 46.94 ? 36 LEU B CD2 1 ATOM 5025 N N . GLY B 1 37 ? 33.265 34.674 25.504 1.00 37.83 ? 37 GLY B N 1 ATOM 5026 C CA . GLY B 1 37 ? 33.634 35.133 24.175 1.00 31.92 ? 37 GLY B CA 1 ATOM 5027 C C . GLY B 1 37 ? 33.832 33.961 23.246 1.00 31.57 ? 37 GLY B C 1 ATOM 5028 O O . GLY B 1 37 ? 33.964 34.172 22.045 1.00 37.03 ? 37 GLY B O 1 ATOM 5029 N N . ALA B 1 38 ? 33.824 32.732 23.763 1.00 30.50 ? 38 ALA B N 1 ATOM 5030 C CA . ALA B 1 38 ? 33.943 31.537 22.927 1.00 30.16 ? 38 ALA B CA 1 ATOM 5031 C C . ALA B 1 38 ? 32.735 31.421 22.059 1.00 32.80 ? 38 ALA B C 1 ATOM 5032 O O . ALA B 1 38 ? 31.674 31.955 22.401 1.00 34.42 ? 38 ALA B O 1 ATOM 5033 C CB . ALA B 1 38 ? 34.046 30.279 23.758 1.00 31.36 ? 38 ALA B CB 1 ATOM 5034 N N . ALA B 1 39 ? 32.889 30.651 20.988 1.00 33.61 ? 39 ALA B N 1 ATOM 5035 C CA . ALA B 1 39 ? 31.813 30.361 20.055 1.00 32.48 ? 39 ALA B CA 1 ATOM 5036 C C . ALA B 1 39 ? 30.845 29.374 20.645 1.00 35.06 ? 39 ALA B C 1 ATOM 5037 O O . ALA B 1 39 ? 31.211 28.619 21.553 1.00 35.78 ? 39 ALA B O 1 ATOM 5038 C CB . ALA B 1 39 ? 32.370 29.804 18.740 1.00 29.17 ? 39 ALA B CB 1 ATOM 5039 N N . ASN B 1 40 ? 29.657 29.328 20.041 1.00 32.94 ? 40 ASN B N 1 ATOM 5040 C CA . ASN B 1 40 ? 28.537 28.437 20.380 1.00 37.50 ? 40 ASN B CA 1 ATOM 5041 C C . ASN B 1 40 ? 28.046 28.495 21.814 1.00 39.82 ? 40 ASN B C 1 ATOM 5042 O O . ASN B 1 40 ? 27.691 27.466 22.403 1.00 44.04 ? 40 ASN B O 1 ATOM 5043 C CB . ASN B 1 40 ? 28.813 26.977 19.980 1.00 42.50 ? 40 ASN B CB 1 ATOM 5044 C CG . ASN B 1 40 ? 28.665 26.728 18.475 1.00 45.85 ? 40 ASN B CG 1 ATOM 5045 O OD1 . ASN B 1 40 ? 27.705 27.169 17.823 1.00 46.28 ? 40 ASN B OD1 1 ATOM 5046 N ND2 . ASN B 1 40 ? 29.594 25.972 17.930 1.00 47.09 ? 40 ASN B ND2 1 ATOM 5047 N N . ARG B 1 41 ? 27.959 29.701 22.346 1.00 40.33 ? 41 ARG B N 1 ATOM 5048 C CA . ARG B 1 41 ? 27.291 29.992 23.601 1.00 34.91 ? 41 ARG B CA 1 ATOM 5049 C C . ARG B 1 41 ? 26.276 31.106 23.426 1.00 36.89 ? 41 ARG B C 1 ATOM 5050 O O . ARG B 1 41 ? 26.184 31.675 22.379 1.00 36.87 ? 41 ARG B O 1 ATOM 5051 C CB . ARG B 1 41 ? 28.217 30.431 24.699 1.00 41.05 ? 41 ARG B CB 1 ATOM 5052 C CG . ARG B 1 41 ? 29.667 30.378 24.416 1.00 49.57 ? 41 ARG B CG 1 ATOM 5053 C CD . ARG B 1 41 ? 30.216 29.097 24.948 1.00 50.43 ? 41 ARG B CD 1 ATOM 5054 N NE . ARG B 1 41 ? 29.994 28.856 26.357 1.00 61.06 ? 41 ARG B NE 1 ATOM 5055 C CZ . ARG B 1 41 ? 29.703 29.742 27.309 1.00 63.49 ? 41 ARG B CZ 1 ATOM 5056 N NH1 . ARG B 1 41 ? 29.546 29.290 28.542 1.00 60.29 ? 41 ARG B NH1 1 ATOM 5057 N NH2 . ARG B 1 41 ? 29.610 31.049 27.069 1.00 58.57 ? 41 ARG B NH2 1 ATOM 5058 N N . ALA B 1 42 ? 25.500 31.374 24.459 1.00 26.89 ? 42 ALA B N 1 ATOM 5059 C CA . ALA B 1 42 ? 24.547 32.405 24.423 1.00 25.36 ? 42 ALA B CA 1 ATOM 5060 C C . ALA B 1 42 ? 25.070 33.798 24.104 1.00 23.71 ? 42 ALA B C 1 ATOM 5061 O O . ALA B 1 42 ? 26.026 34.240 24.673 1.00 19.68 ? 42 ALA B O 1 ATOM 5062 C CB . ALA B 1 42 ? 23.831 32.466 25.768 1.00 23.64 ? 42 ALA B CB 1 ATOM 5063 N N . LEU B 1 43 ? 24.336 34.558 23.276 1.00 25.56 ? 43 LEU B N 1 ATOM 5064 C CA . LEU B 1 43 ? 24.576 35.981 23.147 1.00 21.36 ? 43 LEU B CA 1 ATOM 5065 C C . LEU B 1 43 ? 24.316 36.600 24.492 1.00 22.12 ? 43 LEU B C 1 ATOM 5066 O O . LEU B 1 43 ? 23.439 36.186 25.220 1.00 25.36 ? 43 LEU B O 1 ATOM 5067 C CB . LEU B 1 43 ? 23.619 36.629 22.120 1.00 20.68 ? 43 LEU B CB 1 ATOM 5068 C CG . LEU B 1 43 ? 23.990 36.250 20.659 1.00 21.43 ? 43 LEU B CG 1 ATOM 5069 C CD1 . LEU B 1 43 ? 22.750 36.274 19.764 1.00 19.44 ? 43 LEU B CD1 1 ATOM 5070 C CD2 . LEU B 1 43 ? 25.113 37.179 20.195 1.00 19.63 ? 43 LEU B CD2 1 ATOM 5071 N N . ALA B 1 44 ? 25.068 37.622 24.812 1.00 23.77 ? 44 ALA B N 1 ATOM 5072 C CA . ALA B 1 44 ? 24.906 38.287 26.076 1.00 24.08 ? 44 ALA B CA 1 ATOM 5073 C C . ALA B 1 44 ? 23.670 39.151 26.030 1.00 25.24 ? 44 ALA B C 1 ATOM 5074 O O . ALA B 1 44 ? 23.240 39.602 24.956 1.00 23.70 ? 44 ALA B O 1 ATOM 5075 C CB . ALA B 1 44 ? 26.117 39.134 26.376 1.00 24.60 ? 44 ALA B CB 1 ATOM 5076 N N . ARG B 1 45 ? 23.060 39.292 27.195 1.00 26.05 ? 45 ARG B N 1 ATOM 5077 C CA . ARG B 1 45 ? 21.943 40.178 27.375 1.00 24.59 ? 45 ARG B CA 1 ATOM 5078 C C . ARG B 1 45 ? 22.270 41.331 28.250 1.00 25.54 ? 45 ARG B C 1 ATOM 5079 O O . ARG B 1 45 ? 22.404 41.179 29.451 1.00 25.19 ? 45 ARG B O 1 ATOM 5080 C CB . ARG B 1 45 ? 20.767 39.415 27.951 1.00 25.57 ? 45 ARG B CB 1 ATOM 5081 C CG . ARG B 1 45 ? 20.101 38.508 26.900 1.00 28.49 ? 45 ARG B CG 1 ATOM 5082 C CD . ARG B 1 45 ? 18.588 38.551 26.873 1.00 23.60 ? 45 ARG B CD 1 ATOM 5083 N NE . ARG B 1 45 ? 18.066 37.548 25.936 1.00 23.95 ? 45 ARG B NE 1 ATOM 5084 C CZ . ARG B 1 45 ? 17.357 37.808 24.810 1.00 22.03 ? 45 ARG B CZ 1 ATOM 5085 N NH1 . ARG B 1 45 ? 16.999 39.046 24.499 1.00 20.19 ? 45 ARG B NH1 1 ATOM 5086 N NH2 . ARG B 1 45 ? 16.936 36.815 24.054 1.00 20.12 ? 45 ARG B NH2 1 ATOM 5087 N N . TRP B 1 46 ? 22.321 42.513 27.661 1.00 22.97 ? 46 TRP B N 1 ATOM 5088 C CA . TRP B 1 46 ? 22.487 43.729 28.418 1.00 24.52 ? 46 TRP B CA 1 ATOM 5089 C C . TRP B 1 46 ? 21.202 44.209 29.175 1.00 24.23 ? 46 TRP B C 1 ATOM 5090 O O . TRP B 1 46 ? 21.274 44.944 30.215 1.00 23.63 ? 46 TRP B O 1 ATOM 5091 C CB . TRP B 1 46 ? 22.974 44.837 27.509 1.00 23.42 ? 46 TRP B CB 1 ATOM 5092 C CG . TRP B 1 46 ? 24.324 44.644 26.953 1.00 21.84 ? 46 TRP B CG 1 ATOM 5093 C CD1 . TRP B 1 46 ? 25.268 43.715 27.331 1.00 24.22 ? 46 TRP B CD1 1 ATOM 5094 C CD2 . TRP B 1 46 ? 24.937 45.421 25.933 1.00 21.84 ? 46 TRP B CD2 1 ATOM 5095 N NE1 . TRP B 1 46 ? 26.439 43.899 26.617 1.00 22.58 ? 46 TRP B NE1 1 ATOM 5096 C CE2 . TRP B 1 46 ? 26.254 44.906 25.729 1.00 23.22 ? 46 TRP B CE2 1 ATOM 5097 C CE3 . TRP B 1 46 ? 24.515 46.511 25.165 1.00 22.20 ? 46 TRP B CE3 1 ATOM 5098 C CZ2 . TRP B 1 46 ? 27.129 45.439 24.789 1.00 21.74 ? 46 TRP B CZ2 1 ATOM 5099 C CZ3 . TRP B 1 46 ? 25.379 47.035 24.215 1.00 23.54 ? 46 TRP B CZ3 1 ATOM 5100 C CH2 . TRP B 1 46 ? 26.676 46.501 24.042 1.00 23.85 ? 46 TRP B CH2 1 ATOM 5101 N N . LEU B 1 47 ? 20.046 43.826 28.628 1.00 25.02 ? 47 LEU B N 1 ATOM 5102 C CA . LEU B 1 47 ? 18.746 44.048 29.235 1.00 20.78 ? 47 LEU B CA 1 ATOM 5103 C C . LEU B 1 47 ? 18.076 42.719 29.294 1.00 21.14 ? 47 LEU B C 1 ATOM 5104 O O . LEU B 1 47 ? 18.399 41.818 28.512 1.00 22.79 ? 47 LEU B O 1 ATOM 5105 C CB . LEU B 1 47 ? 17.899 45.057 28.463 1.00 23.71 ? 47 LEU B CB 1 ATOM 5106 C CG . LEU B 1 47 ? 18.251 46.530 28.664 1.00 24.81 ? 47 LEU B CG 1 ATOM 5107 C CD1 . LEU B 1 47 ? 17.345 47.417 27.842 1.00 26.77 ? 47 LEU B CD1 1 ATOM 5108 C CD2 . LEU B 1 47 ? 18.161 46.972 30.136 1.00 28.21 ? 47 LEU B CD2 1 ATOM 5109 N N . PRO B 1 48 ? 17.158 42.538 30.256 1.00 19.23 ? 48 PRO B N 1 ATOM 5110 C CA . PRO B 1 48 ? 16.342 41.344 30.223 1.00 19.87 ? 48 PRO B CA 1 ATOM 5111 C C . PRO B 1 48 ? 15.484 41.220 28.932 1.00 18.83 ? 48 PRO B C 1 ATOM 5112 O O . PRO B 1 48 ? 14.987 42.217 28.392 1.00 16.96 ? 48 PRO B O 1 ATOM 5113 C CB . PRO B 1 48 ? 15.398 41.500 31.466 1.00 21.04 ? 48 PRO B CB 1 ATOM 5114 C CG . PRO B 1 48 ? 16.046 42.544 32.309 1.00 23.11 ? 48 PRO B CG 1 ATOM 5115 C CD . PRO B 1 48 ? 16.747 43.452 31.337 1.00 21.52 ? 48 PRO B CD 1 ATOM 5116 N N . ALA B 1 49 ? 15.320 39.988 28.501 1.00 18.03 ? 49 ALA B N 1 ATOM 5117 C CA . ALA B 1 49 ? 14.602 39.598 27.298 1.00 20.92 ? 49 ALA B CA 1 ATOM 5118 C C . ALA B 1 49 ? 13.139 39.918 27.431 1.00 24.07 ? 49 ALA B C 1 ATOM 5119 O O . ALA B 1 49 ? 12.605 39.952 28.550 1.00 24.09 ? 49 ALA B O 1 ATOM 5120 C CB . ALA B 1 49 ? 14.760 38.099 27.076 1.00 22.03 ? 49 ALA B CB 1 ATOM 5121 N N . GLU B 1 50 ? 12.475 40.205 26.310 1.00 24.20 ? 50 GLU B N 1 ATOM 5122 C CA . GLU B 1 50 ? 11.088 40.616 26.345 1.00 21.11 ? 50 GLU B CA 1 ATOM 5123 C C . GLU B 1 50 ? 10.398 39.756 25.334 1.00 22.99 ? 50 GLU B C 1 ATOM 5124 O O . GLU B 1 50 ? 10.627 39.885 24.128 1.00 19.36 ? 50 GLU B O 1 ATOM 5125 C CB . GLU B 1 50 ? 10.945 42.084 26.044 1.00 22.40 ? 50 GLU B CB 1 ATOM 5126 C CG . GLU B 1 50 ? 11.622 42.932 27.107 1.00 23.54 ? 50 GLU B CG 1 ATOM 5127 C CD . GLU B 1 50 ? 11.239 44.409 27.089 1.00 25.22 ? 50 GLU B CD 1 ATOM 5128 O OE1 . GLU B 1 50 ? 10.291 44.849 26.395 1.00 22.40 ? 50 GLU B OE1 1 ATOM 5129 O OE2 . GLU B 1 50 ? 11.947 45.158 27.788 1.00 25.41 ? 50 GLU B OE2 1 ATOM 5130 N N . TYR B 1 51 ? 9.590 38.846 25.882 1.00 21.51 ? 51 TYR B N 1 ATOM 5131 C CA . TYR B 1 51 ? 8.805 37.923 25.161 1.00 22.89 ? 51 TYR B CA 1 ATOM 5132 C C . TYR B 1 51 ? 7.379 38.044 25.631 1.00 26.29 ? 51 TYR B C 1 ATOM 5133 O O . TYR B 1 51 ? 7.109 38.468 26.761 1.00 28.57 ? 51 TYR B O 1 ATOM 5134 C CB . TYR B 1 51 ? 9.301 36.534 25.419 1.00 22.47 ? 51 TYR B CB 1 ATOM 5135 C CG . TYR B 1 51 ? 10.636 36.183 24.753 1.00 22.95 ? 51 TYR B CG 1 ATOM 5136 C CD1 . TYR B 1 51 ? 10.739 36.054 23.386 1.00 26.17 ? 51 TYR B CD1 1 ATOM 5137 C CD2 . TYR B 1 51 ? 11.754 35.945 25.507 1.00 24.96 ? 51 TYR B CD2 1 ATOM 5138 C CE1 . TYR B 1 51 ? 11.936 35.712 22.783 1.00 25.12 ? 51 TYR B CE1 1 ATOM 5139 C CE2 . TYR B 1 51 ? 12.958 35.580 24.931 1.00 28.07 ? 51 TYR B CE2 1 ATOM 5140 C CZ . TYR B 1 51 ? 13.054 35.469 23.563 1.00 27.81 ? 51 TYR B CZ 1 ATOM 5141 O OH . TYR B 1 51 ? 14.266 35.124 23.003 1.00 25.61 ? 51 TYR B OH 1 ATOM 5142 N N . GLU B 1 52 ? 6.472 37.608 24.781 1.00 25.12 ? 52 GLU B N 1 ATOM 5143 C CA . GLU B 1 52 ? 5.052 37.619 25.010 1.00 25.56 ? 52 GLU B CA 1 ATOM 5144 C C . GLU B 1 52 ? 4.690 36.948 26.315 1.00 23.12 ? 52 GLU B C 1 ATOM 5145 O O . GLU B 1 52 ? 3.889 37.420 27.034 1.00 22.24 ? 52 GLU B O 1 ATOM 5146 C CB . GLU B 1 52 ? 4.342 36.934 23.866 1.00 28.92 ? 52 GLU B CB 1 ATOM 5147 C CG . GLU B 1 52 ? 2.962 37.446 23.591 1.00 28.24 ? 52 GLU B CG 1 ATOM 5148 C CD . GLU B 1 52 ? 2.242 36.644 22.556 1.00 27.98 ? 52 GLU B CD 1 ATOM 5149 O OE1 . GLU B 1 52 ? 1.863 35.542 22.852 1.00 30.58 ? 52 GLU B OE1 1 ATOM 5150 O OE2 . GLU B 1 52 ? 2.041 37.128 21.468 1.00 26.33 ? 52 GLU B OE2 1 ATOM 5151 N N . ASP B 1 53 ? 5.323 35.835 26.570 1.00 23.86 ? 53 ASP B N 1 ATOM 5152 C CA . ASP B 1 53 ? 5.090 35.070 27.787 1.00 23.49 ? 53 ASP B CA 1 ATOM 5153 C C . ASP B 1 53 ? 6.254 35.175 28.761 1.00 26.21 ? 53 ASP B C 1 ATOM 5154 O O . ASP B 1 53 ? 6.459 34.279 29.566 1.00 24.97 ? 53 ASP B O 1 ATOM 5155 C CB . ASP B 1 53 ? 4.868 33.606 27.451 1.00 21.12 ? 53 ASP B CB 1 ATOM 5156 C CG . ASP B 1 53 ? 6.088 32.934 26.889 1.00 22.63 ? 53 ASP B CG 1 ATOM 5157 O OD1 . ASP B 1 53 ? 7.047 33.627 26.500 1.00 29.21 ? 53 ASP B OD1 1 ATOM 5158 O OD2 . ASP B 1 53 ? 6.157 31.680 26.876 1.00 20.70 ? 53 ASP B OD2 1 ATOM 5159 N N . GLY B 1 54 ? 7.095 36.202 28.642 1.00 26.74 ? 54 GLY B N 1 ATOM 5160 C CA . GLY B 1 54 ? 8.301 36.260 29.468 1.00 26.46 ? 54 GLY B CA 1 ATOM 5161 C C . GLY B 1 54 ? 9.415 35.235 29.189 1.00 26.72 ? 54 GLY B C 1 ATOM 5162 O O . GLY B 1 54 ? 10.479 35.369 29.721 1.00 26.76 ? 54 GLY B O 1 ATOM 5163 N N . LEU B 1 55 ? 9.203 34.217 28.379 1.00 26.56 ? 55 LEU B N 1 ATOM 5164 C CA . LEU B 1 55 ? 10.230 33.200 28.220 1.00 27.05 ? 55 LEU B CA 1 ATOM 5165 C C . LEU B 1 55 ? 10.745 32.985 26.794 1.00 26.27 ? 55 LEU B C 1 ATOM 5166 O O . LEU B 1 55 ? 11.940 32.875 26.590 1.00 23.27 ? 55 LEU B O 1 ATOM 5167 C CB . LEU B 1 55 ? 9.697 31.852 28.667 1.00 27.89 ? 55 LEU B CB 1 ATOM 5168 C CG . LEU B 1 55 ? 9.422 31.692 30.163 1.00 31.01 ? 55 LEU B CG 1 ATOM 5169 C CD1 . LEU B 1 55 ? 8.629 30.421 30.387 1.00 33.23 ? 55 LEU B CD1 1 ATOM 5170 C CD2 . LEU B 1 55 ? 10.752 31.601 30.900 1.00 33.16 ? 55 LEU B CD2 1 ATOM 5171 N N . ALA B 1 56 ? 9.841 32.840 25.838 1.00 24.22 ? 56 ALA B N 1 ATOM 5172 C CA . ALA B 1 56 ? 10.263 32.462 24.526 1.00 25.68 ? 56 ALA B CA 1 ATOM 5173 C C . ALA B 1 56 ? 9.321 32.895 23.386 1.00 24.93 ? 56 ALA B C 1 ATOM 5174 O O . ALA B 1 56 ? 9.752 32.895 22.241 1.00 20.31 ? 56 ALA B O 1 ATOM 5175 C CB . ALA B 1 56 ? 10.479 30.940 24.468 1.00 24.94 ? 56 ALA B CB 1 ATOM 5176 N N . VAL B 1 57 ? 8.071 33.235 23.700 1.00 26.06 ? 57 VAL B N 1 ATOM 5177 C CA . VAL B 1 57 ? 7.066 33.527 22.696 1.00 24.27 ? 57 VAL B CA 1 ATOM 5178 C C . VAL B 1 57 ? 7.222 34.983 22.181 1.00 22.99 ? 57 VAL B C 1 ATOM 5179 O O . VAL B 1 57 ? 7.294 35.938 22.972 1.00 22.04 ? 57 VAL B O 1 ATOM 5180 C CB . VAL B 1 57 ? 5.614 33.364 23.229 1.00 24.70 ? 57 VAL B CB 1 ATOM 5181 C CG1 . VAL B 1 57 ? 4.619 33.718 22.129 1.00 23.23 ? 57 VAL B CG1 1 ATOM 5182 C CG2 . VAL B 1 57 ? 5.349 31.946 23.709 1.00 27.06 ? 57 VAL B CG2 1 ATOM 5183 N N . PRO B 1 58 ? 7.324 35.154 20.850 1.00 20.44 ? 58 PRO B N 1 ATOM 5184 C CA . PRO B 1 58 ? 7.691 36.497 20.416 1.00 17.73 ? 58 PRO B CA 1 ATOM 5185 C C . PRO B 1 58 ? 6.514 37.420 20.479 1.00 17.26 ? 58 PRO B C 1 ATOM 5186 O O . PRO B 1 58 ? 5.400 37.012 20.162 1.00 19.59 ? 58 PRO B O 1 ATOM 5187 C CB . PRO B 1 58 ? 8.161 36.310 18.959 1.00 18.72 ? 58 PRO B CB 1 ATOM 5188 C CG . PRO B 1 58 ? 8.256 34.852 18.712 1.00 21.72 ? 58 PRO B CG 1 ATOM 5189 C CD . PRO B 1 58 ? 7.489 34.139 19.798 1.00 20.29 ? 58 PRO B CD 1 ATOM 5190 N N . PHE B 1 59 ? 6.745 38.662 20.849 1.00 17.55 ? 59 PHE B N 1 ATOM 5191 C CA . PHE B 1 59 ? 5.761 39.683 20.524 1.00 17.16 ? 59 PHE B CA 1 ATOM 5192 C C . PHE B 1 59 ? 5.407 39.596 19.027 1.00 17.37 ? 59 PHE B C 1 ATOM 5193 O O . PHE B 1 59 ? 6.291 39.494 18.155 1.00 16.20 ? 59 PHE B O 1 ATOM 5194 C CB . PHE B 1 59 ? 6.225 41.054 20.938 1.00 17.99 ? 59 PHE B CB 1 ATOM 5195 C CG . PHE B 1 59 ? 6.135 41.264 22.424 1.00 18.52 ? 59 PHE B CG 1 ATOM 5196 C CD1 . PHE B 1 59 ? 4.915 41.211 23.059 1.00 19.22 ? 59 PHE B CD1 1 ATOM 5197 C CD2 . PHE B 1 59 ? 7.293 41.400 23.195 1.00 19.60 ? 59 PHE B CD2 1 ATOM 5198 C CE1 . PHE B 1 59 ? 4.813 41.364 24.424 1.00 20.06 ? 59 PHE B CE1 1 ATOM 5199 C CE2 . PHE B 1 59 ? 7.219 41.553 24.575 1.00 18.89 ? 59 PHE B CE2 1 ATOM 5200 C CZ . PHE B 1 59 ? 5.985 41.577 25.186 1.00 21.49 ? 59 PHE B CZ 1 ATOM 5201 N N . GLY B 1 60 ? 4.110 39.548 18.763 1.00 18.52 ? 60 GLY B N 1 ATOM 5202 C CA . GLY B 1 60 ? 3.556 39.400 17.417 1.00 22.02 ? 60 GLY B CA 1 ATOM 5203 C C . GLY B 1 60 ? 2.921 38.033 17.216 1.00 24.25 ? 60 GLY B C 1 ATOM 5204 O O . GLY B 1 60 ? 2.244 37.796 16.218 1.00 23.02 ? 60 GLY B O 1 ATOM 5205 N N . TRP B 1 61 ? 3.168 37.114 18.145 1.00 22.30 ? 61 TRP B N 1 ATOM 5206 C CA . TRP B 1 61 ? 2.757 35.744 17.931 1.00 23.82 ? 61 TRP B CA 1 ATOM 5207 C C . TRP B 1 61 ? 1.257 35.568 18.047 1.00 23.93 ? 61 TRP B C 1 ATOM 5208 O O . TRP B 1 61 ? 0.658 34.882 17.220 1.00 21.91 ? 61 TRP B O 1 ATOM 5209 C CB . TRP B 1 61 ? 3.473 34.841 18.931 1.00 22.04 ? 61 TRP B CB 1 ATOM 5210 C CG . TRP B 1 61 ? 3.301 33.378 18.752 1.00 18.72 ? 61 TRP B CG 1 ATOM 5211 C CD1 . TRP B 1 61 ? 2.307 32.564 19.337 1.00 19.47 ? 61 TRP B CD1 1 ATOM 5212 C CD2 . TRP B 1 61 ? 4.130 32.503 17.997 1.00 16.55 ? 61 TRP B CD2 1 ATOM 5213 N NE1 . TRP B 1 61 ? 2.520 31.280 18.970 1.00 17.73 ? 61 TRP B NE1 1 ATOM 5214 C CE2 . TRP B 1 61 ? 3.626 31.201 18.166 1.00 18.02 ? 61 TRP B CE2 1 ATOM 5215 C CE3 . TRP B 1 61 ? 5.267 32.687 17.197 1.00 17.47 ? 61 TRP B CE3 1 ATOM 5216 C CZ2 . TRP B 1 61 ? 4.224 30.088 17.578 1.00 18.21 ? 61 TRP B CZ2 1 ATOM 5217 C CZ3 . TRP B 1 61 ? 5.887 31.605 16.676 1.00 17.34 ? 61 TRP B CZ3 1 ATOM 5218 C CH2 . TRP B 1 61 ? 5.312 30.300 16.802 1.00 18.78 ? 61 TRP B CH2 1 ATOM 5219 N N . THR B 1 62 ? 0.665 36.122 19.104 1.00 26.64 ? 62 THR B N 1 ATOM 5220 C CA . THR B 1 62 ? -0.711 35.722 19.495 1.00 26.69 ? 62 THR B CA 1 ATOM 5221 C C . THR B 1 62 ? -1.681 36.833 19.237 1.00 28.61 ? 62 THR B C 1 ATOM 5222 O O . THR B 1 62 ? -1.463 37.907 19.730 1.00 22.02 ? 62 THR B O 1 ATOM 5223 C CB . THR B 1 62 ? -0.769 35.306 20.979 1.00 26.87 ? 62 THR B CB 1 ATOM 5224 O OG1 . THR B 1 62 ? 0.147 34.225 21.229 1.00 23.66 ? 62 THR B OG1 1 ATOM 5225 C CG2 . THR B 1 62 ? -2.185 34.869 21.373 1.00 28.23 ? 62 THR B CG2 1 ATOM 5226 N N . GLN B 1 63 ? -2.764 36.572 18.513 1.00 31.71 ? 63 GLN B N 1 ATOM 5227 C CA . GLN B 1 63 ? -3.710 37.597 18.076 1.00 41.75 ? 63 GLN B CA 1 ATOM 5228 C C . GLN B 1 63 ? -4.352 38.500 19.161 1.00 45.61 ? 63 GLN B C 1 ATOM 5229 O O . GLN B 1 63 ? -4.286 39.712 19.093 1.00 47.39 ? 63 GLN B O 1 ATOM 5230 C CB . GLN B 1 63 ? -4.835 37.014 17.213 1.00 49.58 ? 63 GLN B CB 1 ATOM 5231 C CG . GLN B 1 63 ? -4.427 36.347 15.920 1.00 57.14 ? 63 GLN B CG 1 ATOM 5232 C CD . GLN B 1 63 ? -5.610 36.186 14.980 1.00 64.25 ? 63 GLN B CD 1 ATOM 5233 O OE1 . GLN B 1 63 ? -6.468 35.388 15.219 1.00 61.59 ? 63 GLN B OE1 1 ATOM 5234 N NE2 . GLN B 1 63 ? -5.648 36.966 13.935 1.00 66.80 ? 63 GLN B NE2 1 ATOM 5235 N N . ARG B 1 64 ? -4.987 37.944 20.151 1.00 36.79 ? 64 ARG B N 1 ATOM 5236 C CA . ARG B 1 64 ? -5.671 38.865 21.073 1.00 38.08 ? 64 ARG B CA 1 ATOM 5237 C C . ARG B 1 64 ? -4.799 39.403 22.246 1.00 34.70 ? 64 ARG B C 1 ATOM 5238 O O . ARG B 1 64 ? -5.271 40.162 23.120 1.00 31.93 ? 64 ARG B O 1 ATOM 5239 C CB . ARG B 1 64 ? -6.935 38.192 21.575 1.00 43.46 ? 64 ARG B CB 1 ATOM 5240 C CG . ARG B 1 64 ? -7.954 37.916 20.462 1.00 51.42 ? 64 ARG B CG 1 ATOM 5241 C CD . ARG B 1 64 ? -8.201 39.174 19.597 1.00 53.37 ? 64 ARG B CD 1 ATOM 5242 N NE . ARG B 1 64 ? -9.605 39.529 19.329 1.00 61.02 ? 64 ARG B NE 1 ATOM 5243 C CZ . ARG B 1 64 ? -10.509 38.768 18.711 1.00 60.60 ? 64 ARG B CZ 1 ATOM 5244 N NH1 . ARG B 1 64 ? -10.209 37.556 18.275 1.00 61.30 ? 64 ARG B NH1 1 ATOM 5245 N NH2 . ARG B 1 64 ? -11.740 39.231 18.546 1.00 60.27 ? 64 ARG B NH2 1 ATOM 5246 N N . LYS B 1 65 ? -3.518 39.043 22.240 1.00 30.42 ? 65 LYS B N 1 ATOM 5247 C CA . LYS B 1 65 ? -2.567 39.609 23.191 1.00 30.33 ? 65 LYS B CA 1 ATOM 5248 C C . LYS B 1 65 ? -2.019 40.919 22.632 1.00 26.73 ? 65 LYS B C 1 ATOM 5249 O O . LYS B 1 65 ? -2.307 41.278 21.492 1.00 27.09 ? 65 LYS B O 1 ATOM 5250 C CB . LYS B 1 65 ? -1.477 38.611 23.515 1.00 28.80 ? 65 LYS B CB 1 ATOM 5251 C CG . LYS B 1 65 ? -1.979 37.507 24.448 1.00 32.45 ? 65 LYS B CG 1 ATOM 5252 C CD . LYS B 1 65 ? -0.881 36.480 24.704 1.00 35.54 ? 65 LYS B CD 1 ATOM 5253 C CE . LYS B 1 65 ? -1.356 35.244 25.446 1.00 37.34 ? 65 LYS B CE 1 ATOM 5254 N NZ . LYS B 1 65 ? -1.880 35.641 26.780 1.00 40.71 ? 65 LYS B NZ 1 ATOM 5255 N N . THR B 1 66 ? -1.239 41.609 23.435 1.00 20.66 ? 66 THR B N 1 ATOM 5256 C CA . THR B 1 66 ? -0.750 42.941 23.114 1.00 22.28 ? 66 THR B CA 1 ATOM 5257 C C . THR B 1 66 ? 0.588 43.118 23.703 1.00 23.66 ? 66 THR B C 1 ATOM 5258 O O . THR B 1 66 ? 1.033 42.267 24.522 1.00 22.12 ? 66 THR B O 1 ATOM 5259 C CB . THR B 1 66 ? -1.669 44.017 23.668 1.00 23.68 ? 66 THR B CB 1 ATOM 5260 O OG1 . THR B 1 66 ? -1.683 43.978 25.105 1.00 26.73 ? 66 THR B OG1 1 ATOM 5261 C CG2 . THR B 1 66 ? -3.079 43.813 23.117 1.00 22.24 ? 66 THR B CG2 1 ATOM 5262 N N . ARG B 1 67 ? 1.316 44.094 23.167 1.00 21.80 ? 67 ARG B N 1 ATOM 5263 C CA . ARG B 1 67 ? 2.530 44.506 23.747 1.00 21.16 ? 67 ARG B CA 1 ATOM 5264 C C . ARG B 1 67 ? 2.235 45.872 24.307 1.00 22.45 ? 67 ARG B C 1 ATOM 5265 O O . ARG B 1 67 ? 1.859 46.804 23.562 1.00 19.89 ? 67 ARG B O 1 ATOM 5266 C CB . ARG B 1 67 ? 3.656 44.567 22.676 1.00 21.65 ? 67 ARG B CB 1 ATOM 5267 C CG . ARG B 1 67 ? 4.994 44.948 23.300 1.00 21.32 ? 67 ARG B CG 1 ATOM 5268 C CD . ARG B 1 67 ? 6.120 45.172 22.284 1.00 21.87 ? 67 ARG B CD 1 ATOM 5269 N NE . ARG B 1 67 ? 7.368 45.189 22.955 1.00 21.40 ? 67 ARG B NE 1 ATOM 5270 C CZ . ARG B 1 67 ? 8.524 44.711 22.501 1.00 20.40 ? 67 ARG B CZ 1 ATOM 5271 N NH1 . ARG B 1 67 ? 8.682 44.237 21.263 1.00 19.02 ? 67 ARG B NH1 1 ATOM 5272 N NH2 . ARG B 1 67 ? 9.542 44.675 23.350 1.00 20.60 ? 67 ARG B NH2 1 ATOM 5273 N N . ASN B 1 68 ? 2.360 46.012 25.623 1.00 23.78 ? 68 ASN B N 1 ATOM 5274 C CA . ASN B 1 68 ? 1.946 47.236 26.300 1.00 21.06 ? 68 ASN B CA 1 ATOM 5275 C C . ASN B 1 68 ? 0.565 47.738 25.923 1.00 21.04 ? 68 ASN B C 1 ATOM 5276 O O . ASN B 1 68 ? 0.264 48.969 25.895 1.00 21.42 ? 68 ASN B O 1 ATOM 5277 C CB . ASN B 1 68 ? 2.973 48.313 26.058 1.00 22.25 ? 68 ASN B CB 1 ATOM 5278 C CG . ASN B 1 68 ? 4.318 47.952 26.630 1.00 25.86 ? 68 ASN B CG 1 ATOM 5279 O OD1 . ASN B 1 68 ? 4.432 47.507 27.791 1.00 22.93 ? 68 ASN B OD1 1 ATOM 5280 N ND2 . ASN B 1 68 ? 5.367 48.109 25.809 1.00 21.73 ? 68 ASN B ND2 1 ATOM 5281 N N . GLY B 1 69 ? -0.319 46.816 25.598 1.00 21.22 ? 69 GLY B N 1 ATOM 5282 C CA . GLY B 1 69 ? -1.687 47.222 25.306 1.00 23.43 ? 69 GLY B CA 1 ATOM 5283 C C . GLY B 1 69 ? -2.044 47.441 23.837 1.00 25.44 ? 69 GLY B C 1 ATOM 5284 O O . GLY B 1 69 ? -3.226 47.740 23.528 1.00 21.33 ? 69 GLY B O 1 ATOM 5285 N N . PHE B 1 70 ? -1.053 47.299 22.939 1.00 22.33 ? 70 PHE B N 1 ATOM 5286 C CA . PHE B 1 70 ? -1.286 47.513 21.518 1.00 23.39 ? 70 PHE B CA 1 ATOM 5287 C C . PHE B 1 70 ? -0.797 46.316 20.723 1.00 21.47 ? 70 PHE B C 1 ATOM 5288 O O . PHE B 1 70 ? 0.136 45.681 21.101 1.00 21.23 ? 70 PHE B O 1 ATOM 5289 C CB . PHE B 1 70 ? -0.570 48.793 21.083 1.00 22.14 ? 70 PHE B CB 1 ATOM 5290 C CG . PHE B 1 70 ? -0.960 49.975 21.888 1.00 23.04 ? 70 PHE B CG 1 ATOM 5291 C CD1 . PHE B 1 70 ? -2.156 50.603 21.657 1.00 23.76 ? 70 PHE B CD1 1 ATOM 5292 C CD2 . PHE B 1 70 ? -0.131 50.475 22.866 1.00 25.53 ? 70 PHE B CD2 1 ATOM 5293 C CE1 . PHE B 1 70 ? -2.563 51.695 22.406 1.00 26.22 ? 70 PHE B CE1 1 ATOM 5294 C CE2 . PHE B 1 70 ? -0.516 51.563 23.632 1.00 26.27 ? 70 PHE B CE2 1 ATOM 5295 C CZ . PHE B 1 70 ? -1.734 52.179 23.405 1.00 28.83 ? 70 PHE B CZ 1 ATOM 5296 N N . ARG B 1 71 ? -1.414 46.053 19.593 1.00 23.87 ? 71 ARG B N 1 ATOM 5297 C CA . ARG B 1 71 ? -0.929 45.019 18.658 1.00 24.21 ? 71 ARG B CA 1 ATOM 5298 C C . ARG B 1 71 ? 0.340 45.572 18.028 1.00 19.05 ? 71 ARG B C 1 ATOM 5299 O O . ARG B 1 71 ? 0.466 46.764 17.940 1.00 16.71 ? 71 ARG B O 1 ATOM 5300 C CB . ARG B 1 71 ? -1.983 44.771 17.570 1.00 29.79 ? 71 ARG B CB 1 ATOM 5301 C CG . ARG B 1 71 ? -3.282 44.236 18.130 1.00 36.21 ? 71 ARG B CG 1 ATOM 5302 C CD . ARG B 1 71 ? -3.143 42.785 18.606 1.00 42.14 ? 71 ARG B CD 1 ATOM 5303 N NE . ARG B 1 71 ? -3.819 41.852 17.698 1.00 51.11 ? 71 ARG B NE 1 ATOM 5304 C CZ . ARG B 1 71 ? -3.238 40.883 16.980 1.00 57.95 ? 71 ARG B CZ 1 ATOM 5305 N NH1 . ARG B 1 71 ? -1.923 40.678 17.009 1.00 66.84 ? 71 ARG B NH1 1 ATOM 5306 N NH2 . ARG B 1 71 ? -4.009 40.095 16.226 1.00 65.51 ? 71 ARG B NH2 1 ATOM 5307 N N . VAL B 1 72 ? 1.313 44.715 17.734 1.00 18.08 ? 72 VAL B N 1 ATOM 5308 C CA . VAL B 1 72 ? 2.511 45.127 17.023 1.00 19.46 ? 72 VAL B CA 1 ATOM 5309 C C . VAL B 1 72 ? 2.291 44.986 15.534 1.00 17.35 ? 72 VAL B C 1 ATOM 5310 O O . VAL B 1 72 ? 1.615 44.044 15.102 1.00 15.57 ? 72 VAL B O 1 ATOM 5311 C CB . VAL B 1 72 ? 3.809 44.400 17.469 1.00 24.58 ? 72 VAL B CB 1 ATOM 5312 C CG1 . VAL B 1 72 ? 3.943 44.478 18.993 1.00 24.96 ? 72 VAL B CG1 1 ATOM 5313 C CG2 . VAL B 1 72 ? 3.864 42.983 16.979 1.00 23.43 ? 72 VAL B CG2 1 ATOM 5314 N N . PRO B 1 73 ? 2.721 45.983 14.775 1.00 17.25 ? 73 PRO B N 1 ATOM 5315 C CA . PRO B 1 73 ? 2.466 45.986 13.347 1.00 17.95 ? 73 PRO B CA 1 ATOM 5316 C C . PRO B 1 73 ? 3.202 44.860 12.607 1.00 17.19 ? 73 PRO B C 1 ATOM 5317 O O . PRO B 1 73 ? 4.307 44.441 12.976 1.00 17.02 ? 73 PRO B O 1 ATOM 5318 C CB . PRO B 1 73 ? 2.911 47.366 12.948 1.00 16.65 ? 73 PRO B CB 1 ATOM 5319 C CG . PRO B 1 73 ? 4.027 47.675 13.897 1.00 18.12 ? 73 PRO B CG 1 ATOM 5320 C CD . PRO B 1 73 ? 3.532 47.147 15.184 1.00 18.18 ? 73 PRO B CD 1 ATOM 5321 N N . LEU B 1 74 ? 2.599 44.363 11.553 1.00 18.36 ? 74 LEU B N 1 ATOM 5322 C CA . LEU B 1 74 ? 3.242 43.334 10.739 1.00 17.66 ? 74 LEU B CA 1 ATOM 5323 C C . LEU B 1 74 ? 4.610 43.859 10.252 1.00 16.34 ? 74 LEU B C 1 ATOM 5324 O O . LEU B 1 74 ? 4.718 44.977 9.821 1.00 16.02 ? 74 LEU B O 1 ATOM 5325 C CB . LEU B 1 74 ? 2.367 43.004 9.512 1.00 21.87 ? 74 LEU B CB 1 ATOM 5326 C CG . LEU B 1 74 ? 1.040 42.291 9.642 1.00 24.03 ? 74 LEU B CG 1 ATOM 5327 C CD1 . LEU B 1 74 ? 0.408 42.060 8.267 1.00 25.29 ? 74 LEU B CD1 1 ATOM 5328 C CD2 . LEU B 1 74 ? 1.289 40.974 10.330 1.00 27.95 ? 74 LEU B CD2 1 ATOM 5329 N N . ALA B 1 75 ? 5.648 43.069 10.386 1.00 17.23 ? 75 ALA B N 1 ATOM 5330 C CA . ALA B 1 75 ? 6.995 43.464 9.926 1.00 16.69 ? 75 ALA B CA 1 ATOM 5331 C C . ALA B 1 75 ? 7.007 43.968 8.482 1.00 15.96 ? 75 ALA B C 1 ATOM 5332 O O . ALA B 1 75 ? 7.690 44.932 8.148 1.00 17.37 ? 75 ALA B O 1 ATOM 5333 C CB . ALA B 1 75 ? 7.889 42.271 10.037 1.00 17.71 ? 75 ALA B CB 1 ATOM 5334 N N . ARG B 1 76 ? 6.241 43.298 7.616 1.00 16.80 ? 76 ARG B N 1 ATOM 5335 C CA . ARG B 1 76 ? 6.210 43.623 6.193 1.00 15.71 ? 76 ARG B CA 1 ATOM 5336 C C . ARG B 1 76 ? 5.489 44.933 5.939 1.00 14.92 ? 76 ARG B C 1 ATOM 5337 O O . ARG B 1 76 ? 5.855 45.626 5.005 1.00 13.87 ? 76 ARG B O 1 ATOM 5338 C CB . ARG B 1 76 ? 5.567 42.461 5.368 1.00 15.53 ? 76 ARG B CB 1 ATOM 5339 C CG . ARG B 1 76 ? 5.334 42.791 3.896 1.00 15.47 ? 76 ARG B CG 1 ATOM 5340 C CD . ARG B 1 76 ? 6.638 43.005 3.097 1.00 14.12 ? 76 ARG B CD 1 ATOM 5341 N NE . ARG B 1 76 ? 6.316 43.178 1.689 1.00 13.86 ? 76 ARG B NE 1 ATOM 5342 C CZ . ARG B 1 76 ? 7.181 43.479 0.720 1.00 12.65 ? 76 ARG B CZ 1 ATOM 5343 N NH1 . ARG B 1 76 ? 8.469 43.580 0.949 1.00 11.91 ? 76 ARG B NH1 1 ATOM 5344 N NH2 . ARG B 1 76 ? 6.709 43.642 -0.507 1.00 13.62 ? 76 ARG B NH2 1 ATOM 5345 N N . GLU B 1 77 ? 4.475 45.263 6.767 1.00 13.71 ? 77 GLU B N 1 ATOM 5346 C CA . GLU B 1 77 ? 3.819 46.594 6.656 1.00 16.30 ? 77 GLU B CA 1 ATOM 5347 C C . GLU B 1 77 ? 4.689 47.750 7.044 1.00 14.98 ? 77 GLU B C 1 ATOM 5348 O O . GLU B 1 77 ? 4.714 48.771 6.356 1.00 17.87 ? 77 GLU B O 1 ATOM 5349 C CB . GLU B 1 77 ? 2.512 46.593 7.481 1.00 19.31 ? 77 GLU B CB 1 ATOM 5350 C CG . GLU B 1 77 ? 1.682 47.851 7.411 1.00 23.49 ? 77 GLU B CG 1 ATOM 5351 C CD . GLU B 1 77 ? 0.288 47.633 7.985 1.00 27.93 ? 77 GLU B CD 1 ATOM 5352 O OE1 . GLU B 1 77 ? -0.061 46.508 8.443 1.00 32.23 ? 77 GLU B OE1 1 ATOM 5353 O OE2 . GLU B 1 77 ? -0.479 48.587 7.939 1.00 33.38 ? 77 GLU B OE2 1 ATOM 5354 N N . VAL B 1 78 ? 5.485 47.590 8.105 1.00 14.63 ? 78 VAL B N 1 ATOM 5355 C CA . VAL B 1 78 ? 6.499 48.561 8.452 1.00 14.19 ? 78 VAL B CA 1 ATOM 5356 C C . VAL B 1 78 ? 7.484 48.737 7.301 1.00 14.45 ? 78 VAL B C 1 ATOM 5357 O O . VAL B 1 78 ? 7.872 49.862 6.940 1.00 13.87 ? 78 VAL B O 1 ATOM 5358 C CB . VAL B 1 78 ? 7.240 48.133 9.759 1.00 14.14 ? 78 VAL B CB 1 ATOM 5359 C CG1 . VAL B 1 78 ? 8.302 49.055 10.166 1.00 13.09 ? 78 VAL B CG1 1 ATOM 5360 C CG2 . VAL B 1 78 ? 6.244 47.941 10.944 1.00 15.66 ? 78 VAL B CG2 1 ATOM 5361 N N . SER B 1 79 ? 8.005 47.608 6.828 1.00 14.72 ? 79 SER B N 1 ATOM 5362 C CA . SER B 1 79 ? 8.899 47.637 5.669 1.00 15.11 ? 79 SER B CA 1 ATOM 5363 C C . SER B 1 79 ? 8.284 48.467 4.555 1.00 14.91 ? 79 SER B C 1 ATOM 5364 O O . SER B 1 79 ? 8.909 49.379 4.083 1.00 18.37 ? 79 SER B O 1 ATOM 5365 C CB . SER B 1 79 ? 9.209 46.188 5.158 1.00 13.98 ? 79 SER B CB 1 ATOM 5366 O OG . SER B 1 79 ? 10.160 46.184 4.104 1.00 14.53 ? 79 SER B OG 1 ATOM 5367 N N . ASN B 1 80 ? 7.078 48.115 4.111 1.00 16.05 ? 80 ASN B N 1 ATOM 5368 C CA . ASN B 1 80 ? 6.455 48.793 2.981 1.00 17.13 ? 80 ASN B CA 1 ATOM 5369 C C . ASN B 1 80 ? 6.287 50.283 3.248 1.00 19.33 ? 80 ASN B C 1 ATOM 5370 O O . ASN B 1 80 ? 6.644 51.094 2.438 1.00 18.90 ? 80 ASN B O 1 ATOM 5371 C CB . ASN B 1 80 ? 5.053 48.255 2.695 1.00 16.48 ? 80 ASN B CB 1 ATOM 5372 C CG . ASN B 1 80 ? 5.034 46.839 2.168 1.00 15.37 ? 80 ASN B CG 1 ATOM 5373 O OD1 . ASN B 1 80 ? 6.021 46.334 1.677 1.00 12.49 ? 80 ASN B OD1 1 ATOM 5374 N ND2 . ASN B 1 80 ? 3.863 46.191 2.270 1.00 14.68 ? 80 ASN B ND2 1 ATOM 5375 N N . LYS B 1 81 ? 5.753 50.643 4.412 1.00 21.17 ? 81 LYS B N 1 ATOM 5376 C CA . LYS B 1 81 ? 5.296 52.055 4.657 1.00 19.22 ? 81 LYS B CA 1 ATOM 5377 C C . LYS B 1 81 ? 6.409 52.963 5.077 1.00 18.58 ? 81 LYS B C 1 ATOM 5378 O O . LYS B 1 81 ? 6.323 54.174 4.861 1.00 18.34 ? 81 LYS B O 1 ATOM 5379 C CB . LYS B 1 81 ? 4.219 52.079 5.721 1.00 21.06 ? 81 LYS B CB 1 ATOM 5380 C CG . LYS B 1 81 ? 2.960 51.375 5.181 1.00 27.13 ? 81 LYS B CG 1 ATOM 5381 C CD . LYS B 1 81 ? 1.808 51.387 6.159 1.00 30.09 ? 81 LYS B CD 1 ATOM 5382 C CE . LYS B 1 81 ? 0.533 50.870 5.504 1.00 32.74 ? 81 LYS B CE 1 ATOM 5383 N NZ . LYS B 1 81 ? -0.530 50.969 6.532 1.00 31.04 ? 81 LYS B NZ 1 ATOM 5384 N N . ILE B 1 82 ? 7.409 52.398 5.746 1.00 17.98 ? 82 ILE B N 1 ATOM 5385 C CA . ILE B 1 82 ? 8.527 53.196 6.231 1.00 19.16 ? 82 ILE B CA 1 ATOM 5386 C C . ILE B 1 82 ? 9.845 52.997 5.511 1.00 19.94 ? 82 ILE B C 1 ATOM 5387 O O . ILE B 1 82 ? 10.530 53.977 5.227 1.00 23.14 ? 82 ILE B O 1 ATOM 5388 C CB . ILE B 1 82 ? 8.707 53.010 7.740 1.00 19.47 ? 82 ILE B CB 1 ATOM 5389 C CG1 . ILE B 1 82 ? 7.510 53.666 8.504 1.00 22.31 ? 82 ILE B CG1 1 ATOM 5390 C CG2 . ILE B 1 82 ? 9.983 53.648 8.209 1.00 18.99 ? 82 ILE B CG2 1 ATOM 5391 C CD1 . ILE B 1 82 ? 7.169 52.889 9.750 1.00 26.04 ? 82 ILE B CD1 1 ATOM 5392 N N . VAL B 1 83 ? 10.192 51.750 5.222 1.00 19.56 ? 83 VAL B N 1 ATOM 5393 C CA . VAL B 1 83 ? 11.548 51.363 4.870 1.00 18.75 ? 83 VAL B CA 1 ATOM 5394 C C . VAL B 1 83 ? 11.831 51.447 3.334 1.00 18.43 ? 83 VAL B C 1 ATOM 5395 O O . VAL B 1 83 ? 12.970 51.512 2.922 1.00 20.06 ? 83 VAL B O 1 ATOM 5396 C CB . VAL B 1 83 ? 11.817 49.939 5.448 1.00 20.20 ? 83 VAL B CB 1 ATOM 5397 C CG1 . VAL B 1 83 ? 13.241 49.487 5.197 1.00 20.05 ? 83 VAL B CG1 1 ATOM 5398 C CG2 . VAL B 1 83 ? 11.565 49.902 6.969 1.00 20.77 ? 83 VAL B CG2 1 ATOM 5399 N N . GLY B 1 84 ? 10.792 51.419 2.517 1.00 18.22 ? 84 GLY B N 1 ATOM 5400 C CA . GLY B 1 84 ? 10.915 51.209 1.082 1.00 18.89 ? 84 GLY B CA 1 ATOM 5401 C C . GLY B 1 84 ? 11.026 52.526 0.360 1.00 20.90 ? 84 GLY B C 1 ATOM 5402 O O . GLY B 1 84 ? 10.584 53.587 0.872 1.00 23.10 ? 84 GLY B O 1 ATOM 5403 N N . TYR B 1 85 ? 11.621 52.486 -0.810 1.00 21.04 ? 85 TYR B N 1 ATOM 5404 C CA . TYR B 1 85 ? 11.604 53.628 -1.699 1.00 21.26 ? 85 TYR B CA 1 ATOM 5405 C C . TYR B 1 85 ? 11.843 53.179 -3.121 1.00 25.08 ? 85 TYR B C 1 ATOM 5406 O O . TYR B 1 85 ? 12.273 52.000 -3.389 1.00 22.29 ? 85 TYR B O 1 ATOM 5407 C CB . TYR B 1 85 ? 12.712 54.611 -1.296 1.00 19.22 ? 85 TYR B CB 1 ATOM 5408 C CG . TYR B 1 85 ? 14.097 54.076 -1.489 1.00 18.03 ? 85 TYR B CG 1 ATOM 5409 C CD1 . TYR B 1 85 ? 14.701 53.241 -0.517 1.00 15.84 ? 85 TYR B CD1 1 ATOM 5410 C CD2 . TYR B 1 85 ? 14.836 54.415 -2.626 1.00 17.93 ? 85 TYR B CD2 1 ATOM 5411 C CE1 . TYR B 1 85 ? 15.941 52.751 -0.705 1.00 16.15 ? 85 TYR B CE1 1 ATOM 5412 C CE2 . TYR B 1 85 ? 16.104 53.924 -2.807 1.00 18.29 ? 85 TYR B CE2 1 ATOM 5413 C CZ . TYR B 1 85 ? 16.635 53.067 -1.863 1.00 16.84 ? 85 TYR B CZ 1 ATOM 5414 O OH . TYR B 1 85 ? 17.861 52.579 -2.086 1.00 15.70 ? 85 TYR B OH 1 ATOM 5415 N N . LEU B 1 86 ? 11.551 54.085 -4.056 1.00 22.75 ? 86 LEU B N 1 ATOM 5416 C CA . LEU B 1 86 ? 11.576 53.721 -5.481 1.00 25.07 ? 86 LEU B CA 1 ATOM 5417 C C . LEU B 1 86 ? 12.774 54.276 -6.185 1.00 23.70 ? 86 LEU B C 1 ATOM 5418 O O . LEU B 1 86 ? 13.327 53.666 -7.047 1.00 23.48 ? 86 LEU B O 1 ATOM 5419 C CB . LEU B 1 86 ? 10.305 54.272 -6.129 1.00 29.93 ? 86 LEU B CB 1 ATOM 5420 C CG . LEU B 1 86 ? 9.459 53.431 -7.045 1.00 32.46 ? 86 LEU B CG 1 ATOM 5421 C CD1 . LEU B 1 86 ? 9.228 52.063 -6.417 1.00 36.51 ? 86 LEU B CD1 1 ATOM 5422 C CD2 . LEU B 1 86 ? 8.149 54.165 -7.274 1.00 32.80 ? 86 LEU B CD2 1 ATOM 5423 N N . ASP B 1 87 ? 13.176 55.474 -5.826 1.00 24.81 ? 87 ASP B N 1 ATOM 5424 C CA . ASP B 1 87 ? 14.095 56.253 -6.647 1.00 24.11 ? 87 ASP B CA 1 ATOM 5425 C C . ASP B 1 87 ? 15.479 56.271 -6.024 1.00 22.26 ? 87 ASP B C 1 ATOM 5426 O O . ASP B 1 87 ? 15.683 56.826 -4.950 1.00 26.64 ? 87 ASP B O 1 ATOM 5427 C CB . ASP B 1 87 ? 13.497 57.674 -6.760 1.00 25.14 ? 87 ASP B CB 1 ATOM 5428 C CG . ASP B 1 87 ? 14.300 58.620 -7.708 1.00 25.71 ? 87 ASP B CG 1 ATOM 5429 O OD1 . ASP B 1 87 ? 15.309 58.187 -8.316 1.00 29.54 ? 87 ASP B OD1 1 ATOM 5430 O OD2 . ASP B 1 87 ? 13.926 59.814 -7.781 1.00 26.72 ? 87 ASP B OD2 1 ATOM 5431 N N . GLU B 1 88 ? 16.419 55.652 -6.703 1.00 20.21 ? 88 GLU B N 1 ATOM 5432 C CA . GLU B 1 88 ? 17.785 55.531 -6.293 1.00 21.94 ? 88 GLU B CA 1 ATOM 5433 C C . GLU B 1 88 ? 18.610 56.787 -6.583 1.00 23.57 ? 88 GLU B C 1 ATOM 5434 O O . GLU B 1 88 ? 19.734 56.977 -6.117 1.00 22.30 ? 88 GLU B O 1 ATOM 5435 C CB . GLU B 1 88 ? 18.408 54.357 -7.029 1.00 21.51 ? 88 GLU B CB 1 ATOM 5436 C CG . GLU B 1 88 ? 17.719 53.016 -6.793 1.00 22.46 ? 88 GLU B CG 1 ATOM 5437 C CD . GLU B 1 88 ? 17.899 52.412 -5.376 1.00 22.36 ? 88 GLU B CD 1 ATOM 5438 O OE1 . GLU B 1 88 ? 18.737 52.911 -4.599 1.00 22.70 ? 88 GLU B OE1 1 ATOM 5439 O OE2 . GLU B 1 88 ? 17.215 51.398 -5.090 1.00 19.68 ? 88 GLU B OE2 1 ATOM 5440 N N . GLU B 1 89 ? 18.002 57.706 -7.282 1.00 28.88 ? 89 GLU B N 1 ATOM 5441 C CA . GLU B 1 89 ? 18.658 58.911 -7.639 1.00 30.30 ? 89 GLU B CA 1 ATOM 5442 C C . GLU B 1 89 ? 18.948 59.731 -6.392 1.00 27.29 ? 89 GLU B C 1 ATOM 5443 O O . GLU B 1 89 ? 18.060 60.007 -5.604 1.00 29.26 ? 89 GLU B O 1 ATOM 5444 C CB . GLU B 1 89 ? 17.758 59.610 -8.672 1.00 35.68 ? 89 GLU B CB 1 ATOM 5445 C CG . GLU B 1 89 ? 18.535 60.090 -9.837 1.00 43.94 ? 89 GLU B CG 1 ATOM 5446 C CD . GLU B 1 89 ? 19.566 61.028 -9.371 1.00 47.08 ? 89 GLU B CD 1 ATOM 5447 O OE1 . GLU B 1 89 ? 19.169 61.928 -8.622 1.00 52.24 ? 89 GLU B OE1 1 ATOM 5448 O OE2 . GLU B 1 89 ? 20.746 60.810 -9.709 1.00 56.72 ? 89 GLU B OE2 1 ATOM 5449 N N . GLY B 1 90 ? 20.202 60.117 -6.232 1.00 24.39 ? 90 GLY B N 1 ATOM 5450 C CA . GLY B 1 90 ? 20.653 60.964 -5.114 1.00 27.93 ? 90 GLY B CA 1 ATOM 5451 C C . GLY B 1 90 ? 20.905 60.220 -3.803 1.00 26.30 ? 90 GLY B C 1 ATOM 5452 O O . GLY B 1 90 ? 21.219 60.847 -2.817 1.00 23.91 ? 90 GLY B O 1 ATOM 5453 N N . VAL B 1 91 ? 20.730 58.885 -3.791 1.00 26.42 ? 91 VAL B N 1 ATOM 5454 C CA . VAL B 1 91 ? 20.733 58.085 -2.543 1.00 23.41 ? 91 VAL B CA 1 ATOM 5455 C C . VAL B 1 91 ? 22.135 57.741 -2.086 1.00 21.61 ? 91 VAL B C 1 ATOM 5456 O O . VAL B 1 91 ? 22.325 57.204 -1.002 1.00 23.44 ? 91 VAL B O 1 ATOM 5457 C CB . VAL B 1 91 ? 19.874 56.784 -2.718 1.00 22.89 ? 91 VAL B CB 1 ATOM 5458 C CG1 . VAL B 1 91 ? 20.717 55.629 -3.292 1.00 22.19 ? 91 VAL B CG1 1 ATOM 5459 C CG2 . VAL B 1 91 ? 19.246 56.377 -1.424 1.00 23.75 ? 91 VAL B CG2 1 ATOM 5460 N N . LEU B 1 92 ? 23.142 57.988 -2.919 1.00 20.60 ? 92 LEU B N 1 ATOM 5461 C CA . LEU B 1 92 ? 24.481 57.475 -2.603 1.00 21.61 ? 92 LEU B CA 1 ATOM 5462 C C . LEU B 1 92 ? 25.144 58.345 -1.570 1.00 21.69 ? 92 LEU B C 1 ATOM 5463 O O . LEU B 1 92 ? 24.739 59.489 -1.389 1.00 21.68 ? 92 LEU B O 1 ATOM 5464 C CB . LEU B 1 92 ? 25.367 57.388 -3.862 1.00 25.26 ? 92 LEU B CB 1 ATOM 5465 C CG . LEU B 1 92 ? 24.831 56.370 -4.907 1.00 25.25 ? 92 LEU B CG 1 ATOM 5466 C CD1 . LEU B 1 92 ? 25.729 56.338 -6.127 1.00 27.69 ? 92 LEU B CD1 1 ATOM 5467 C CD2 . LEU B 1 92 ? 24.756 54.961 -4.309 1.00 25.01 ? 92 LEU B CD2 1 ATOM 5468 N N . ASP B 1 93 ? 26.117 57.761 -0.868 1.00 24.77 ? 93 ASP B N 1 ATOM 5469 C CA . ASP B 1 93 ? 26.912 58.405 0.165 1.00 21.41 ? 93 ASP B CA 1 ATOM 5470 C C . ASP B 1 93 ? 28.073 59.037 -0.527 1.00 25.51 ? 93 ASP B C 1 ATOM 5471 O O . ASP B 1 93 ? 29.047 58.375 -0.923 1.00 22.90 ? 93 ASP B O 1 ATOM 5472 C CB . ASP B 1 93 ? 27.416 57.403 1.173 1.00 20.90 ? 93 ASP B CB 1 ATOM 5473 C CG . ASP B 1 93 ? 28.017 58.054 2.381 1.00 22.45 ? 93 ASP B CG 1 ATOM 5474 O OD1 . ASP B 1 93 ? 28.477 59.247 2.301 1.00 22.29 ? 93 ASP B OD1 1 ATOM 5475 O OD2 . ASP B 1 93 ? 28.075 57.362 3.433 1.00 23.30 ? 93 ASP B OD2 1 ATOM 5476 N N . GLN B 1 94 ? 27.989 60.355 -0.630 1.00 30.00 ? 94 GLN B N 1 ATOM 5477 C CA . GLN B 1 94 ? 28.957 61.112 -1.362 1.00 34.95 ? 94 GLN B CA 1 ATOM 5478 C C . GLN B 1 94 ? 30.339 61.115 -0.727 1.00 30.71 ? 94 GLN B C 1 ATOM 5479 O O . GLN B 1 94 ? 31.282 61.538 -1.360 1.00 30.75 ? 94 GLN B O 1 ATOM 5480 C CB . GLN B 1 94 ? 28.465 62.567 -1.508 1.00 41.30 ? 94 GLN B CB 1 ATOM 5481 C CG . GLN B 1 94 ? 27.110 62.715 -2.185 1.00 45.44 ? 94 GLN B CG 1 ATOM 5482 C CD . GLN B 1 94 ? 26.966 61.978 -3.521 1.00 49.76 ? 94 GLN B CD 1 ATOM 5483 O OE1 . GLN B 1 94 ? 27.901 61.869 -4.316 1.00 53.17 ? 94 GLN B OE1 1 ATOM 5484 N NE2 . GLN B 1 94 ? 25.770 61.460 -3.752 1.00 50.49 ? 94 GLN B NE2 1 ATOM 5485 N N . ASN B 1 95 ? 30.496 60.613 0.484 1.00 30.27 ? 95 ASN B N 1 ATOM 5486 C CA . ASN B 1 95 ? 31.837 60.594 1.082 1.00 35.53 ? 95 ASN B CA 1 ATOM 5487 C C . ASN B 1 95 ? 32.284 59.251 1.615 1.00 33.67 ? 95 ASN B C 1 ATOM 5488 O O . ASN B 1 95 ? 33.160 59.184 2.455 1.00 36.77 ? 95 ASN B O 1 ATOM 5489 C CB . ASN B 1 95 ? 31.921 61.639 2.194 1.00 39.38 ? 95 ASN B CB 1 ATOM 5490 C CG . ASN B 1 95 ? 33.347 61.975 2.549 1.00 49.11 ? 95 ASN B CG 1 ATOM 5491 O OD1 . ASN B 1 95 ? 34.294 61.714 1.769 1.00 50.21 ? 95 ASN B OD1 1 ATOM 5492 N ND2 . ASN B 1 95 ? 33.528 62.524 3.766 1.00 60.53 ? 95 ASN B ND2 1 ATOM 5493 N N . ARG B 1 96 ? 31.676 58.176 1.120 1.00 33.69 ? 96 ARG B N 1 ATOM 5494 C CA . ARG B 1 96 ? 32.051 56.798 1.485 1.00 31.36 ? 96 ARG B CA 1 ATOM 5495 C C . ARG B 1 96 ? 32.019 55.839 0.276 1.00 25.76 ? 96 ARG B C 1 ATOM 5496 O O . ARG B 1 96 ? 30.980 55.668 -0.367 1.00 25.11 ? 96 ARG B O 1 ATOM 5497 C CB . ARG B 1 96 ? 31.081 56.244 2.516 1.00 32.94 ? 96 ARG B CB 1 ATOM 5498 C CG . ARG B 1 96 ? 31.022 56.978 3.834 1.00 36.42 ? 96 ARG B CG 1 ATOM 5499 C CD . ARG B 1 96 ? 32.274 56.841 4.681 1.00 40.64 ? 96 ARG B CD 1 ATOM 5500 N NE . ARG B 1 96 ? 31.974 57.399 6.010 1.00 42.21 ? 96 ARG B NE 1 ATOM 5501 C CZ . ARG B 1 96 ? 32.024 58.691 6.310 1.00 44.39 ? 96 ARG B CZ 1 ATOM 5502 N NH1 . ARG B 1 96 ? 32.461 59.554 5.398 1.00 42.74 ? 96 ARG B NH1 1 ATOM 5503 N NH2 . ARG B 1 96 ? 31.673 59.113 7.548 1.00 45.08 ? 96 ARG B NH2 1 ATOM 5504 N N . SER B 1 97 ? 33.143 55.219 -0.003 1.00 22.99 ? 97 SER B N 1 ATOM 5505 C CA . SER B 1 97 ? 33.197 54.184 -0.995 1.00 24.01 ? 97 SER B CA 1 ATOM 5506 C C . SER B 1 97 ? 32.345 52.975 -0.576 1.00 24.04 ? 97 SER B C 1 ATOM 5507 O O . SER B 1 97 ? 31.970 52.811 0.600 1.00 22.70 ? 97 SER B O 1 ATOM 5508 C CB . SER B 1 97 ? 34.630 53.717 -1.219 1.00 23.31 ? 97 SER B CB 1 ATOM 5509 O OG . SER B 1 97 ? 35.166 53.078 -0.070 1.00 22.96 ? 97 SER B OG 1 ATOM 5510 N N . LEU B 1 98 ? 32.103 52.102 -1.546 1.00 22.39 ? 98 LEU B N 1 ATOM 5511 C CA . LEU B 1 98 ? 31.320 50.906 -1.341 1.00 21.50 ? 98 LEU B CA 1 ATOM 5512 C C . LEU B 1 98 ? 32.016 49.975 -0.350 1.00 22.58 ? 98 LEU B C 1 ATOM 5513 O O . LEU B 1 98 ? 31.383 49.196 0.330 1.00 22.07 ? 98 LEU B O 1 ATOM 5514 C CB . LEU B 1 98 ? 31.120 50.240 -2.679 1.00 20.52 ? 98 LEU B CB 1 ATOM 5515 C CG . LEU B 1 98 ? 30.228 49.008 -2.692 1.00 19.07 ? 98 LEU B CG 1 ATOM 5516 C CD1 . LEU B 1 98 ? 28.917 49.342 -2.072 1.00 18.61 ? 98 LEU B CD1 1 ATOM 5517 C CD2 . LEU B 1 98 ? 30.032 48.587 -4.138 1.00 20.12 ? 98 LEU B CD2 1 ATOM 5518 N N . LEU B 1 99 ? 33.339 50.121 -0.235 1.00 23.15 ? 99 LEU B N 1 ATOM 5519 C CA . LEU B 1 99 ? 34.117 49.363 0.726 1.00 22.29 ? 99 LEU B CA 1 ATOM 5520 C C . LEU B 1 99 ? 33.748 49.560 2.202 1.00 20.97 ? 99 LEU B C 1 ATOM 5521 O O . LEU B 1 99 ? 33.898 48.642 3.009 1.00 23.58 ? 99 LEU B O 1 ATOM 5522 C CB . LEU B 1 99 ? 35.606 49.678 0.562 1.00 23.84 ? 99 LEU B CB 1 ATOM 5523 C CG . LEU B 1 99 ? 36.556 49.013 1.547 1.00 25.19 ? 99 LEU B CG 1 ATOM 5524 C CD1 . LEU B 1 99 ? 36.740 47.536 1.247 1.00 28.44 ? 99 LEU B CD1 1 ATOM 5525 C CD2 . LEU B 1 99 ? 37.926 49.727 1.556 1.00 27.54 ? 99 LEU B CD2 1 ATOM 5526 N N . PHE B 1 100 ? 33.353 50.768 2.532 1.00 20.43 ? 100 PHE B N 1 ATOM 5527 C CA . PHE B 1 100 ? 32.821 51.093 3.818 1.00 19.80 ? 100 PHE B CA 1 ATOM 5528 C C . PHE B 1 100 ? 31.658 50.152 4.178 1.00 19.66 ? 100 PHE B C 1 ATOM 5529 O O . PHE B 1 100 ? 31.676 49.614 5.260 1.00 19.06 ? 100 PHE B O 1 ATOM 5530 C CB . PHE B 1 100 ? 32.288 52.526 3.817 1.00 19.70 ? 100 PHE B CB 1 ATOM 5531 C CG . PHE B 1 100 ? 31.600 52.941 5.090 1.00 19.16 ? 100 PHE B CG 1 ATOM 5532 C CD1 . PHE B 1 100 ? 32.264 52.872 6.324 1.00 21.32 ? 100 PHE B CD1 1 ATOM 5533 C CD2 . PHE B 1 100 ? 30.328 53.427 5.065 1.00 19.89 ? 100 PHE B CD2 1 ATOM 5534 C CE1 . PHE B 1 100 ? 31.595 53.241 7.491 1.00 20.64 ? 100 PHE B CE1 1 ATOM 5535 C CE2 . PHE B 1 100 ? 29.668 53.800 6.234 1.00 20.98 ? 100 PHE B CE2 1 ATOM 5536 C CZ . PHE B 1 100 ? 30.306 53.689 7.457 1.00 18.21 ? 100 PHE B CZ 1 ATOM 5537 N N . MET B 1 101 ? 30.657 50.028 3.294 1.00 17.55 ? 101 MET B N 1 ATOM 5538 C CA . MET B 1 101 ? 29.560 49.083 3.548 1.00 16.63 ? 101 MET B CA 1 ATOM 5539 C C . MET B 1 101 ? 30.167 47.703 3.695 1.00 17.47 ? 101 MET B C 1 ATOM 5540 O O . MET B 1 101 ? 29.821 46.954 4.608 1.00 18.49 ? 101 MET B O 1 ATOM 5541 C CB . MET B 1 101 ? 28.503 49.137 2.399 1.00 16.27 ? 101 MET B CB 1 ATOM 5542 C CG . MET B 1 101 ? 27.422 48.046 2.345 1.00 16.47 ? 101 MET B CG 1 ATOM 5543 S SD . MET B 1 101 ? 27.991 46.369 1.967 1.00 15.87 ? 101 MET B SD 1 ATOM 5544 C CE . MET B 1 101 ? 28.234 46.451 0.170 1.00 17.98 ? 101 MET B CE 1 ATOM 5545 N N . GLN B 1 102 ? 31.112 47.341 2.796 1.00 17.59 ? 102 GLN B N 1 ATOM 5546 C CA . GLN B 1 102 ? 31.522 45.996 2.710 1.00 15.61 ? 102 GLN B CA 1 ATOM 5547 C C . GLN B 1 102 ? 32.347 45.569 3.915 1.00 16.57 ? 102 GLN B C 1 ATOM 5548 O O . GLN B 1 102 ? 32.314 44.410 4.305 1.00 18.12 ? 102 GLN B O 1 ATOM 5549 C CB . GLN B 1 102 ? 32.327 45.743 1.447 1.00 15.26 ? 102 GLN B CB 1 ATOM 5550 C CG . GLN B 1 102 ? 32.591 44.288 1.206 1.00 16.26 ? 102 GLN B CG 1 ATOM 5551 C CD . GLN B 1 102 ? 31.303 43.486 1.131 1.00 17.71 ? 102 GLN B CD 1 ATOM 5552 O OE1 . GLN B 1 102 ? 30.487 43.690 0.170 1.00 17.18 ? 102 GLN B OE1 1 ATOM 5553 N NE2 . GLN B 1 102 ? 31.062 42.642 2.131 1.00 15.21 ? 102 GLN B NE2 1 ATOM 5554 N N . TRP B 1 103 ? 33.213 46.460 4.400 1.00 15.37 ? 103 TRP B N 1 ATOM 5555 C CA . TRP B 1 103 ? 33.987 46.159 5.579 1.00 14.89 ? 103 TRP B CA 1 ATOM 5556 C C . TRP B 1 103 ? 33.095 45.941 6.799 1.00 14.43 ? 103 TRP B C 1 ATOM 5557 O O . TRP B 1 103 ? 33.350 45.067 7.647 1.00 15.05 ? 103 TRP B O 1 ATOM 5558 C CB . TRP B 1 103 ? 35.027 47.294 5.888 1.00 16.67 ? 103 TRP B CB 1 ATOM 5559 C CG . TRP B 1 103 ? 36.069 46.831 6.972 1.00 18.47 ? 103 TRP B CG 1 ATOM 5560 C CD1 . TRP B 1 103 ? 36.168 47.276 8.269 1.00 20.91 ? 103 TRP B CD1 1 ATOM 5561 C CD2 . TRP B 1 103 ? 37.016 45.788 6.841 1.00 22.65 ? 103 TRP B CD2 1 ATOM 5562 N NE1 . TRP B 1 103 ? 37.118 46.556 8.948 1.00 22.31 ? 103 TRP B NE1 1 ATOM 5563 C CE2 . TRP B 1 103 ? 37.666 45.644 8.093 1.00 22.16 ? 103 TRP B CE2 1 ATOM 5564 C CE3 . TRP B 1 103 ? 37.403 44.943 5.771 1.00 23.44 ? 103 TRP B CE3 1 ATOM 5565 C CZ2 . TRP B 1 103 ? 38.675 44.735 8.301 1.00 22.64 ? 103 TRP B CZ2 1 ATOM 5566 C CZ3 . TRP B 1 103 ? 38.384 44.049 5.981 1.00 23.43 ? 103 TRP B CZ3 1 ATOM 5567 C CH2 . TRP B 1 103 ? 39.023 43.944 7.252 1.00 23.42 ? 103 TRP B CH2 1 ATOM 5568 N N . GLY B 1 104 ? 32.039 46.718 6.904 1.00 15.76 ? 104 GLY B N 1 ATOM 5569 C CA . GLY B 1 104 ? 31.058 46.462 7.970 1.00 15.78 ? 104 GLY B CA 1 ATOM 5570 C C . GLY B 1 104 ? 30.520 45.059 7.980 1.00 15.43 ? 104 GLY B C 1 ATOM 5571 O O . GLY B 1 104 ? 30.446 44.434 9.044 1.00 16.40 ? 104 GLY B O 1 ATOM 5572 N N . GLN B 1 105 ? 30.135 44.534 6.820 1.00 13.86 ? 105 GLN B N 1 ATOM 5573 C CA . GLN B 1 105 ? 29.573 43.167 6.799 1.00 14.64 ? 105 GLN B CA 1 ATOM 5574 C C . GLN B 1 105 ? 30.640 42.171 7.227 1.00 15.27 ? 105 GLN B C 1 ATOM 5575 O O . GLN B 1 105 ? 30.373 41.167 7.901 1.00 17.34 ? 105 GLN B O 1 ATOM 5576 C CB . GLN B 1 105 ? 28.956 42.868 5.398 1.00 14.33 ? 105 GLN B CB 1 ATOM 5577 C CG . GLN B 1 105 ? 28.296 41.504 5.302 1.00 15.43 ? 105 GLN B CG 1 ATOM 5578 C CD . GLN B 1 105 ? 27.753 41.206 3.911 1.00 17.72 ? 105 GLN B CD 1 ATOM 5579 O OE1 . GLN B 1 105 ? 28.361 41.576 2.866 1.00 16.29 ? 105 GLN B OE1 1 ATOM 5580 N NE2 . GLN B 1 105 ? 26.609 40.534 3.865 1.00 15.72 ? 105 GLN B NE2 1 ATOM 5581 N N . ILE B 1 106 ? 31.844 42.382 6.739 1.00 16.30 ? 106 ILE B N 1 ATOM 5582 C CA . ILE B 1 106 ? 33.014 41.585 7.133 1.00 15.79 ? 106 ILE B CA 1 ATOM 5583 C C . ILE B 1 106 ? 33.260 41.546 8.656 1.00 15.81 ? 106 ILE B C 1 ATOM 5584 O O . ILE B 1 106 ? 33.361 40.428 9.223 1.00 14.02 ? 106 ILE B O 1 ATOM 5585 C CB . ILE B 1 106 ? 34.257 42.021 6.346 1.00 16.78 ? 106 ILE B CB 1 ATOM 5586 C CG1 . ILE B 1 106 ? 34.159 41.444 4.938 1.00 17.90 ? 106 ILE B CG1 1 ATOM 5587 C CG2 . ILE B 1 106 ? 35.575 41.695 7.063 1.00 19.19 ? 106 ILE B CG2 1 ATOM 5588 C CD1 . ILE B 1 106 ? 34.599 40.016 4.837 1.00 19.15 ? 106 ILE B CD1 1 ATOM 5589 N N . VAL B 1 107 ? 33.312 42.701 9.279 1.00 15.41 ? 107 VAL B N 1 ATOM 5590 C CA . VAL B 1 107 ? 33.526 42.768 10.731 1.00 18.24 ? 107 VAL B CA 1 ATOM 5591 C C . VAL B 1 107 ? 32.353 42.110 11.440 1.00 16.94 ? 107 VAL B C 1 ATOM 5592 O O . VAL B 1 107 ? 32.516 41.297 12.367 1.00 16.44 ? 107 VAL B O 1 ATOM 5593 C CB . VAL B 1 107 ? 33.659 44.209 11.213 1.00 20.23 ? 107 VAL B CB 1 ATOM 5594 C CG1 . VAL B 1 107 ? 33.702 44.298 12.728 1.00 22.00 ? 107 VAL B CG1 1 ATOM 5595 C CG2 . VAL B 1 107 ? 34.908 44.893 10.604 1.00 21.13 ? 107 VAL B CG2 1 ATOM 5596 N N . ASP B 1 108 ? 31.160 42.396 10.952 1.00 18.47 ? 108 ASP B N 1 ATOM 5597 C CA . ASP B 1 108 ? 29.964 41.820 11.550 1.00 17.74 ? 108 ASP B CA 1 ATOM 5598 C C . ASP B 1 108 ? 30.105 40.306 11.586 1.00 18.24 ? 108 ASP B C 1 ATOM 5599 O O . ASP B 1 108 ? 29.736 39.707 12.576 1.00 19.41 ? 108 ASP B O 1 ATOM 5600 C CB . ASP B 1 108 ? 28.936 42.233 10.741 1.00 18.06 ? 108 ASP B CB 1 ATOM 5601 C CG . ASP B 1 108 ? 27.689 41.597 11.228 1.00 17.54 ? 108 ASP B CG 1 ATOM 5602 O OD1 . ASP B 1 108 ? 27.489 40.421 11.063 1.00 17.38 ? 108 ASP B OD1 1 ATOM 5603 O OD2 . ASP B 1 108 ? 26.823 42.303 11.771 1.00 21.83 ? 108 ASP B OD2 1 ATOM 5604 N N . HIS B 1 109 ? 30.632 39.680 10.512 1.00 17.26 ? 109 HIS B N 1 ATOM 5605 C CA . HIS B 1 109 ? 30.684 38.213 10.427 1.00 16.01 ? 109 HIS B CA 1 ATOM 5606 C C . HIS B 1 109 ? 31.811 37.565 11.226 1.00 16.75 ? 109 HIS B C 1 ATOM 5607 O O . HIS B 1 109 ? 31.718 36.412 11.602 1.00 18.42 ? 109 HIS B O 1 ATOM 5608 C CB . HIS B 1 109 ? 30.787 37.758 8.982 1.00 16.83 ? 109 HIS B CB 1 ATOM 5609 C CG . HIS B 1 109 ? 29.523 37.985 8.234 1.00 17.27 ? 109 HIS B CG 1 ATOM 5610 N ND1 . HIS B 1 109 ? 29.325 37.577 6.929 1.00 17.87 ? 109 HIS B ND1 1 ATOM 5611 C CD2 . HIS B 1 109 ? 28.429 38.688 8.589 1.00 17.47 ? 109 HIS B CD2 1 ATOM 5612 C CE1 . HIS B 1 109 ? 28.121 37.955 6.543 1.00 18.01 ? 109 HIS B CE1 1 ATOM 5613 N NE2 . HIS B 1 109 ? 27.556 38.639 7.535 1.00 18.19 ? 109 HIS B NE2 1 ATOM 5614 N N . ASP B 1 110 ? 32.835 38.344 11.505 1.00 18.63 ? 110 ASP B N 1 ATOM 5615 C CA . ASP B 1 110 ? 33.878 37.965 12.458 1.00 19.26 ? 110 ASP B CA 1 ATOM 5616 C C . ASP B 1 110 ? 33.203 37.848 13.827 1.00 18.26 ? 110 ASP B C 1 ATOM 5617 O O . ASP B 1 110 ? 33.394 36.892 14.529 1.00 19.92 ? 110 ASP B O 1 ATOM 5618 C CB . ASP B 1 110 ? 34.999 39.019 12.446 1.00 19.80 ? 110 ASP B CB 1 ATOM 5619 C CG . ASP B 1 110 ? 36.328 38.499 13.039 1.00 20.98 ? 110 ASP B CG 1 ATOM 5620 O OD1 . ASP B 1 110 ? 36.311 37.890 14.149 1.00 23.40 ? 110 ASP B OD1 1 ATOM 5621 O OD2 . ASP B 1 110 ? 37.371 38.754 12.385 1.00 22.09 ? 110 ASP B OD2 1 ATOM 5622 N N . LEU B 1 111 ? 32.337 38.788 14.149 1.00 21.04 ? 111 LEU B N 1 ATOM 5623 C CA . LEU B 1 111 ? 31.803 38.919 15.513 1.00 17.60 ? 111 LEU B CA 1 ATOM 5624 C C . LEU B 1 111 ? 30.596 38.153 15.888 1.00 19.77 ? 111 LEU B C 1 ATOM 5625 O O . LEU B 1 111 ? 30.490 37.765 17.051 1.00 19.91 ? 111 LEU B O 1 ATOM 5626 C CB . LEU B 1 111 ? 31.520 40.358 15.832 1.00 17.54 ? 111 LEU B CB 1 ATOM 5627 C CG . LEU B 1 111 ? 32.673 41.318 15.670 1.00 16.98 ? 111 LEU B CG 1 ATOM 5628 C CD1 . LEU B 1 111 ? 32.195 42.740 15.907 1.00 15.54 ? 111 LEU B CD1 1 ATOM 5629 C CD2 . LEU B 1 111 ? 33.810 40.966 16.620 1.00 16.22 ? 111 LEU B CD2 1 ATOM 5630 N N . ASP B 1 112 ? 29.628 37.981 14.980 1.00 18.93 ? 112 ASP B N 1 ATOM 5631 C CA . ASP B 1 112 ? 28.376 37.319 15.371 1.00 18.55 ? 112 ASP B CA 1 ATOM 5632 C C . ASP B 1 112 ? 27.623 36.565 14.292 1.00 18.21 ? 112 ASP B C 1 ATOM 5633 O O . ASP B 1 112 ? 27.577 36.973 13.151 1.00 18.36 ? 112 ASP B O 1 ATOM 5634 C CB . ASP B 1 112 ? 27.439 38.277 16.098 1.00 18.81 ? 112 ASP B CB 1 ATOM 5635 C CG . ASP B 1 112 ? 27.204 39.597 15.399 1.00 18.92 ? 112 ASP B CG 1 ATOM 5636 O OD1 . ASP B 1 112 ? 27.985 40.533 15.622 1.00 19.57 ? 112 ASP B OD1 1 ATOM 5637 O OD2 . ASP B 1 112 ? 26.148 39.784 14.692 1.00 23.13 ? 112 ASP B OD2 1 ATOM 5638 N N . PHE B 1 113 ? 27.079 35.426 14.671 1.00 19.50 ? 113 PHE B N 1 ATOM 5639 C CA . PHE B 1 113 ? 26.135 34.666 13.852 1.00 20.47 ? 113 PHE B CA 1 ATOM 5640 C C . PHE B 1 113 ? 25.180 33.902 14.741 1.00 18.95 ? 113 PHE B C 1 ATOM 5641 O O . PHE B 1 113 ? 25.630 32.991 15.471 1.00 18.42 ? 113 PHE B O 1 ATOM 5642 C CB . PHE B 1 113 ? 26.874 33.679 12.936 1.00 23.02 ? 113 PHE B CB 1 ATOM 5643 C CG . PHE B 1 113 ? 25.976 32.907 11.989 1.00 26.81 ? 113 PHE B CG 1 ATOM 5644 C CD1 . PHE B 1 113 ? 24.819 33.434 11.499 1.00 26.99 ? 113 PHE B CD1 1 ATOM 5645 C CD2 . PHE B 1 113 ? 26.320 31.641 11.624 1.00 33.93 ? 113 PHE B CD2 1 ATOM 5646 C CE1 . PHE B 1 113 ? 23.991 32.705 10.657 1.00 29.63 ? 113 PHE B CE1 1 ATOM 5647 C CE2 . PHE B 1 113 ? 25.525 30.885 10.776 1.00 36.47 ? 113 PHE B CE2 1 ATOM 5648 C CZ . PHE B 1 113 ? 24.352 31.412 10.292 1.00 32.89 ? 113 PHE B CZ 1 ATOM 5649 N N . ALA B 1 114 ? 23.908 34.288 14.734 1.00 17.84 ? 114 ALA B N 1 ATOM 5650 C CA . ALA B 1 114 ? 22.829 33.550 15.386 1.00 17.68 ? 114 ALA B CA 1 ATOM 5651 C C . ALA B 1 114 ? 22.162 32.625 14.389 1.00 21.61 ? 114 ALA B C 1 ATOM 5652 O O . ALA B 1 114 ? 21.298 33.073 13.655 1.00 23.73 ? 114 ALA B O 1 ATOM 5653 C CB . ALA B 1 114 ? 21.839 34.452 16.008 1.00 16.65 ? 114 ALA B CB 1 ATOM 5654 N N . PRO B 1 115 ? 22.622 31.355 14.316 1.00 21.44 ? 115 PRO B N 1 ATOM 5655 C CA . PRO B 1 115 ? 22.081 30.432 13.390 1.00 23.52 ? 115 PRO B CA 1 ATOM 5656 C C . PRO B 1 115 ? 20.619 30.138 13.618 1.00 25.26 ? 115 PRO B C 1 ATOM 5657 O O . PRO B 1 115 ? 20.084 30.247 14.726 1.00 25.48 ? 115 PRO B O 1 ATOM 5658 C CB . PRO B 1 115 ? 22.883 29.153 13.635 1.00 27.37 ? 115 PRO B CB 1 ATOM 5659 C CG . PRO B 1 115 ? 23.235 29.202 15.061 1.00 27.76 ? 115 PRO B CG 1 ATOM 5660 C CD . PRO B 1 115 ? 23.519 30.677 15.284 1.00 27.22 ? 115 PRO B CD 1 ATOM 5661 N N . GLU B 1 116 ? 20.014 29.726 12.529 1.00 27.56 ? 116 GLU B N 1 ATOM 5662 C CA . GLU B 1 116 ? 18.606 29.584 12.408 1.00 38.16 ? 116 GLU B CA 1 ATOM 5663 C C . GLU B 1 116 ? 18.309 28.103 12.353 1.00 43.15 ? 116 GLU B C 1 ATOM 5664 O O . GLU B 1 116 ? 19.222 27.261 12.396 1.00 48.42 ? 116 GLU B O 1 ATOM 5665 C CB . GLU B 1 116 ? 18.280 30.279 11.122 1.00 42.02 ? 116 GLU B CB 1 ATOM 5666 C CG . GLU B 1 116 ? 16.913 30.768 10.962 1.00 44.25 ? 116 GLU B CG 1 ATOM 5667 C CD . GLU B 1 116 ? 16.567 30.760 9.507 1.00 47.90 ? 116 GLU B CD 1 ATOM 5668 O OE1 . GLU B 1 116 ? 16.573 29.644 8.928 1.00 42.45 ? 116 GLU B OE1 1 ATOM 5669 O OE2 . GLU B 1 116 ? 16.280 31.861 8.969 1.00 52.51 ? 116 GLU B OE2 1 ATOM 5670 N N . THR B 1 117 ? 17.034 27.752 12.313 1.00 51.04 ? 117 THR B N 1 ATOM 5671 C CA . THR B 1 117 ? 16.657 26.343 12.441 1.00 51.64 ? 117 THR B CA 1 ATOM 5672 C C . THR B 1 117 ? 16.026 25.744 11.182 1.00 52.95 ? 117 THR B C 1 ATOM 5673 O O . THR B 1 117 ? 15.645 24.593 11.222 1.00 66.78 ? 117 THR B O 1 ATOM 5674 C CB . THR B 1 117 ? 15.748 26.142 13.677 1.00 50.37 ? 117 THR B CB 1 ATOM 5675 O OG1 . THR B 1 117 ? 14.617 27.018 13.593 1.00 39.57 ? 117 THR B OG1 1 ATOM 5676 C CG2 . THR B 1 117 ? 16.517 26.450 14.952 1.00 47.35 ? 117 THR B CG2 1 ATOM 5677 N N . GLU B 1 118 ? 15.962 26.470 10.060 1.00 58.09 ? 118 GLU B N 1 ATOM 5678 C CA . GLU B 1 118 ? 15.309 25.926 8.841 1.00 63.80 ? 118 GLU B CA 1 ATOM 5679 C C . GLU B 1 118 ? 16.000 24.683 8.286 1.00 71.45 ? 118 GLU B C 1 ATOM 5680 O O . GLU B 1 118 ? 15.381 23.622 8.225 1.00 74.27 ? 118 GLU B O 1 ATOM 5681 C CB . GLU B 1 118 ? 15.116 26.949 7.706 1.00 57.60 ? 118 GLU B CB 1 ATOM 5682 C CG . GLU B 1 118 ? 14.537 26.304 6.421 1.00 59.65 ? 118 GLU B CG 1 ATOM 5683 C CD . GLU B 1 118 ? 13.430 27.106 5.688 1.00 60.54 ? 118 GLU B CD 1 ATOM 5684 O OE1 . GLU B 1 118 ? 12.582 26.482 4.983 1.00 42.80 ? 118 GLU B OE1 1 ATOM 5685 O OE2 . GLU B 1 118 ? 13.376 28.357 5.805 1.00 59.67 ? 118 GLU B OE2 1 ATOM 5686 N N . LEU B 1 119 ? 17.267 24.813 7.888 1.00 83.67 ? 119 LEU B N 1 ATOM 5687 C CA . LEU B 1 119 ? 18.038 23.676 7.359 1.00 90.18 ? 119 LEU B CA 1 ATOM 5688 C C . LEU B 1 119 ? 17.780 22.402 8.185 1.00 86.83 ? 119 LEU B C 1 ATOM 5689 O O . LEU B 1 119 ? 17.391 21.367 7.629 1.00 79.64 ? 119 LEU B O 1 ATOM 5690 C CB . LEU B 1 119 ? 19.544 23.991 7.322 1.00 93.18 ? 119 LEU B CB 1 ATOM 5691 C CG . LEU B 1 119 ? 20.434 22.885 6.725 1.00 95.62 ? 119 LEU B CG 1 ATOM 5692 C CD1 . LEU B 1 119 ? 20.516 23.021 5.206 1.00 92.07 ? 119 LEU B CD1 1 ATOM 5693 C CD2 . LEU B 1 119 ? 21.821 22.880 7.369 1.00 93.26 ? 119 LEU B CD2 1 ATOM 5694 N N . GLY B 1 120 ? 17.972 22.499 9.501 1.00 79.77 ? 120 GLY B N 1 ATOM 5695 C CA . GLY B 1 120 ? 17.763 21.367 10.404 1.00 85.92 ? 120 GLY B CA 1 ATOM 5696 C C . GLY B 1 120 ? 16.324 20.909 10.619 1.00 84.47 ? 120 GLY B C 1 ATOM 5697 O O . GLY B 1 120 ? 16.109 19.862 11.240 1.00 91.22 ? 120 GLY B O 1 ATOM 5698 N N . SER B 1 121 ? 15.346 21.678 10.121 1.00 75.56 ? 121 SER B N 1 ATOM 5699 C CA . SER B 1 121 ? 13.918 21.339 10.251 1.00 67.93 ? 121 SER B CA 1 ATOM 5700 C C . SER B 1 121 ? 13.500 20.243 9.253 1.00 66.14 ? 121 SER B C 1 ATOM 5701 O O . SER B 1 121 ? 14.148 20.061 8.228 1.00 61.69 ? 121 SER B O 1 ATOM 5702 C CB . SER B 1 121 ? 13.033 22.576 10.027 1.00 62.19 ? 121 SER B CB 1 ATOM 5703 O OG . SER B 1 121 ? 13.121 23.514 11.086 1.00 61.08 ? 121 SER B OG 1 ATOM 5704 N N . SER B 1 122 ? 12.405 19.541 9.568 1.00 61.55 ? 122 SER B N 1 ATOM 5705 C CA . SER B 1 122 ? 11.816 18.519 8.687 1.00 60.56 ? 122 SER B CA 1 ATOM 5706 C C . SER B 1 122 ? 11.221 19.116 7.419 1.00 62.30 ? 122 SER B C 1 ATOM 5707 O O . SER B 1 122 ? 10.727 20.242 7.431 1.00 63.33 ? 122 SER B O 1 ATOM 5708 C CB . SER B 1 122 ? 10.703 17.753 9.415 1.00 59.49 ? 122 SER B CB 1 ATOM 5709 O OG . SER B 1 122 ? 9.511 18.530 9.493 1.00 52.11 ? 122 SER B OG 1 ATOM 5710 N N . GLU B 1 123 ? 11.222 18.336 6.341 1.00 65.74 ? 123 GLU B N 1 ATOM 5711 C CA . GLU B 1 123 ? 10.632 18.779 5.088 1.00 67.93 ? 123 GLU B CA 1 ATOM 5712 C C . GLU B 1 123 ? 9.185 19.222 5.262 1.00 63.87 ? 123 GLU B C 1 ATOM 5713 O O . GLU B 1 123 ? 8.749 20.204 4.654 1.00 57.14 ? 123 GLU B O 1 ATOM 5714 C CB . GLU B 1 123 ? 10.675 17.666 4.047 1.00 72.16 ? 123 GLU B CB 1 ATOM 5715 C CG . GLU B 1 123 ? 10.162 18.107 2.689 1.00 76.87 ? 123 GLU B CG 1 ATOM 5716 C CD . GLU B 1 123 ? 10.830 19.379 2.195 1.00 79.97 ? 123 GLU B CD 1 ATOM 5717 O OE1 . GLU B 1 123 ? 11.963 19.694 2.643 1.00 78.85 ? 123 GLU B OE1 1 ATOM 5718 O OE2 . GLU B 1 123 ? 10.216 20.056 1.343 1.00 88.60 ? 123 GLU B OE2 1 ATOM 5719 N N . HIS B 1 124 ? 8.459 18.480 6.052 1.00 61.86 ? 124 HIS B N 1 ATOM 5720 C CA . HIS B 1 124 ? 7.107 18.820 6.392 1.00 61.88 ? 124 HIS B CA 1 ATOM 5721 C C . HIS B 1 124 ? 6.996 20.230 7.008 1.00 56.55 ? 124 HIS B C 1 ATOM 5722 O O . HIS B 1 124 ? 6.148 20.978 6.587 1.00 55.41 ? 124 HIS B O 1 ATOM 5723 C CB . HIS B 1 124 ? 6.563 17.715 7.288 1.00 66.21 ? 124 HIS B CB 1 ATOM 5724 C CG . HIS B 1 124 ? 5.458 18.144 8.178 1.00 72.91 ? 124 HIS B CG 1 ATOM 5725 N ND1 . HIS B 1 124 ? 4.164 18.252 7.752 1.00 80.78 ? 124 HIS B ND1 1 ATOM 5726 C CD2 . HIS B 1 124 ? 5.473 18.559 9.459 1.00 74.15 ? 124 HIS B CD2 1 ATOM 5727 C CE1 . HIS B 1 124 ? 3.416 18.684 8.748 1.00 85.62 ? 124 HIS B CE1 1 ATOM 5728 N NE2 . HIS B 1 124 ? 4.192 18.888 9.793 1.00 85.37 ? 124 HIS B NE2 1 ATOM 5729 N N . SER B 1 125 ? 7.859 20.562 7.939 1.00 50.05 ? 125 SER B N 1 ATOM 5730 C CA . SER B 1 125 ? 7.763 21.831 8.612 1.00 50.06 ? 125 SER B CA 1 ATOM 5731 C C . SER B 1 125 ? 8.085 22.965 7.673 1.00 40.25 ? 125 SER B C 1 ATOM 5732 O O . SER B 1 125 ? 7.454 23.976 7.669 1.00 41.90 ? 125 SER B O 1 ATOM 5733 C CB . SER B 1 125 ? 8.697 21.824 9.796 1.00 54.15 ? 125 SER B CB 1 ATOM 5734 O OG . SER B 1 125 ? 8.234 22.691 10.780 1.00 63.38 ? 125 SER B OG 1 ATOM 5735 N N . LYS B 1 126 ? 9.074 22.740 6.850 1.00 40.79 ? 126 LYS B N 1 ATOM 5736 C CA . LYS B 1 126 ? 9.436 23.685 5.809 1.00 38.33 ? 126 LYS B CA 1 ATOM 5737 C C . LYS B 1 126 ? 8.273 23.951 4.874 1.00 39.59 ? 126 LYS B C 1 ATOM 5738 O O . LYS B 1 126 ? 7.985 25.113 4.534 1.00 33.89 ? 126 LYS B O 1 ATOM 5739 C CB . LYS B 1 126 ? 10.647 23.176 5.060 1.00 44.64 ? 126 LYS B CB 1 ATOM 5740 C CG . LYS B 1 126 ? 11.914 23.230 5.918 1.00 45.73 ? 126 LYS B CG 1 ATOM 5741 C CD . LYS B 1 126 ? 12.833 22.022 5.742 1.00 52.47 ? 126 LYS B CD 1 ATOM 5742 C CE . LYS B 1 126 ? 13.974 22.314 4.780 1.00 55.17 ? 126 LYS B CE 1 ATOM 5743 N NZ . LYS B 1 126 ? 15.273 21.755 5.238 1.00 57.91 ? 126 LYS B NZ 1 ATOM 5744 N N . VAL B 1 127 ? 7.551 22.885 4.526 1.00 37.76 ? 127 VAL B N 1 ATOM 5745 C CA . VAL B 1 127 ? 6.437 22.993 3.626 1.00 35.29 ? 127 VAL B CA 1 ATOM 5746 C C . VAL B 1 127 ? 5.307 23.711 4.326 1.00 35.79 ? 127 VAL B C 1 ATOM 5747 O O . VAL B 1 127 ? 4.694 24.581 3.729 1.00 38.14 ? 127 VAL B O 1 ATOM 5748 C CB . VAL B 1 127 ? 6.039 21.598 3.008 1.00 37.12 ? 127 VAL B CB 1 ATOM 5749 C CG1 . VAL B 1 127 ? 4.570 21.539 2.577 1.00 32.67 ? 127 VAL B CG1 1 ATOM 5750 C CG2 . VAL B 1 127 ? 6.966 21.253 1.832 1.00 34.88 ? 127 VAL B CG2 1 ATOM 5751 N N . GLN B 1 128 ? 5.046 23.385 5.594 1.00 36.75 ? 128 GLN B N 1 ATOM 5752 C CA . GLN B 1 128 ? 3.995 24.083 6.338 1.00 37.33 ? 128 GLN B CA 1 ATOM 5753 C C . GLN B 1 128 ? 4.250 25.590 6.378 1.00 33.50 ? 128 GLN B C 1 ATOM 5754 O O . GLN B 1 128 ? 3.325 26.393 6.390 1.00 35.52 ? 128 GLN B O 1 ATOM 5755 C CB . GLN B 1 128 ? 3.910 23.606 7.786 1.00 43.38 ? 128 GLN B CB 1 ATOM 5756 C CG . GLN B 1 128 ? 3.470 22.181 8.063 1.00 52.16 ? 128 GLN B CG 1 ATOM 5757 C CD . GLN B 1 128 ? 1.993 22.099 8.397 1.00 58.37 ? 128 GLN B CD 1 ATOM 5758 O OE1 . GLN B 1 128 ? 1.565 22.326 9.550 1.00 60.19 ? 128 GLN B OE1 1 ATOM 5759 N NE2 . GLN B 1 128 ? 1.198 21.794 7.387 1.00 61.60 ? 128 GLN B NE2 1 ATOM 5760 N N . CYS B 1 129 ? 5.522 25.948 6.440 1.00 35.54 ? 129 CYS B N 1 ATOM 5761 C CA . CYS B 1 129 ? 5.896 27.330 6.685 1.00 33.24 ? 129 CYS B CA 1 ATOM 5762 C C . CYS B 1 129 ? 5.827 28.045 5.371 1.00 32.73 ? 129 CYS B C 1 ATOM 5763 O O . CYS B 1 129 ? 5.220 29.099 5.292 1.00 31.29 ? 129 CYS B O 1 ATOM 5764 C CB . CYS B 1 129 ? 7.299 27.424 7.316 1.00 32.00 ? 129 CYS B CB 1 ATOM 5765 S SG . CYS B 1 129 ? 7.532 28.966 8.238 1.00 26.82 ? 129 CYS B SG 1 ATOM 5766 N N . GLU B 1 130 ? 6.437 27.474 4.327 1.00 37.43 ? 130 GLU B N 1 ATOM 5767 C CA . GLU B 1 130 ? 6.466 28.195 3.037 1.00 36.64 ? 130 GLU B CA 1 ATOM 5768 C C . GLU B 1 130 ? 5.152 28.060 2.308 1.00 32.33 ? 130 GLU B C 1 ATOM 5769 O O . GLU B 1 130 ? 4.572 29.060 1.881 1.00 29.41 ? 130 GLU B O 1 ATOM 5770 C CB . GLU B 1 130 ? 7.636 27.789 2.124 1.00 37.63 ? 130 GLU B CB 1 ATOM 5771 C CG . GLU B 1 130 ? 7.690 28.679 0.861 1.00 44.78 ? 130 GLU B CG 1 ATOM 5772 C CD . GLU B 1 130 ? 9.085 28.797 0.193 1.00 48.93 ? 130 GLU B CD 1 ATOM 5773 O OE1 . GLU B 1 130 ? 9.882 27.804 0.245 1.00 44.13 ? 130 GLU B OE1 1 ATOM 5774 O OE2 . GLU B 1 130 ? 9.382 29.892 -0.392 1.00 46.25 ? 130 GLU B OE2 1 ATOM 5775 N N . GLU B 1 131 ? 4.675 26.825 2.143 1.00 32.71 ? 131 GLU B N 1 ATOM 5776 C CA . GLU B 1 131 ? 3.511 26.613 1.305 1.00 34.39 ? 131 GLU B CA 1 ATOM 5777 C C . GLU B 1 131 ? 2.246 27.035 1.990 1.00 29.84 ? 131 GLU B C 1 ATOM 5778 O O . GLU B 1 131 ? 1.318 27.501 1.327 1.00 29.83 ? 131 GLU B O 1 ATOM 5779 C CB . GLU B 1 131 ? 3.355 25.150 0.865 1.00 43.51 ? 131 GLU B CB 1 ATOM 5780 C CG . GLU B 1 131 ? 4.620 24.572 0.250 1.00 49.75 ? 131 GLU B CG 1 ATOM 5781 C CD . GLU B 1 131 ? 4.496 24.233 -1.236 1.00 58.49 ? 131 GLU B CD 1 ATOM 5782 O OE1 . GLU B 1 131 ? 4.850 23.082 -1.658 1.00 56.71 ? 131 GLU B OE1 1 ATOM 5783 O OE2 . GLU B 1 131 ? 4.083 25.172 -1.972 1.00 50.94 ? 131 GLU B OE2 1 ATOM 5784 N N . TYR B 1 132 ? 2.164 26.845 3.310 1.00 27.98 ? 132 TYR B N 1 ATOM 5785 C CA . TYR B 1 132 ? 0.895 27.078 3.992 1.00 28.19 ? 132 TYR B CA 1 ATOM 5786 C C . TYR B 1 132 ? 0.913 28.260 4.940 1.00 30.66 ? 132 TYR B C 1 ATOM 5787 O O . TYR B 1 132 ? -0.101 28.573 5.511 1.00 30.70 ? 132 TYR B O 1 ATOM 5788 C CB . TYR B 1 132 ? 0.424 25.788 4.696 1.00 31.54 ? 132 TYR B CB 1 ATOM 5789 C CG . TYR B 1 132 ? 0.111 24.658 3.707 1.00 31.42 ? 132 TYR B CG 1 ATOM 5790 C CD1 . TYR B 1 132 ? -1.109 24.623 3.009 1.00 35.47 ? 132 TYR B CD1 1 ATOM 5791 C CD2 . TYR B 1 132 ? 0.994 23.615 3.523 1.00 32.75 ? 132 TYR B CD2 1 ATOM 5792 C CE1 . TYR B 1 132 ? -1.399 23.605 2.095 1.00 36.75 ? 132 TYR B CE1 1 ATOM 5793 C CE2 . TYR B 1 132 ? 0.731 22.591 2.619 1.00 35.37 ? 132 TYR B CE2 1 ATOM 5794 C CZ . TYR B 1 132 ? -0.466 22.581 1.906 1.00 40.46 ? 132 TYR B CZ 1 ATOM 5795 O OH . TYR B 1 132 ? -0.708 21.523 1.043 1.00 42.68 ? 132 TYR B OH 1 ATOM 5796 N N . CYS B 1 133 ? 2.050 28.925 5.125 1.00 27.14 ? 133 CYS B N 1 ATOM 5797 C CA . CYS B 1 133 ? 2.075 30.095 6.022 1.00 25.79 ? 133 CYS B CA 1 ATOM 5798 C C . CYS B 1 133 ? 1.450 29.789 7.407 1.00 25.65 ? 133 CYS B C 1 ATOM 5799 O O . CYS B 1 133 ? 0.853 30.638 8.021 1.00 24.71 ? 133 CYS B O 1 ATOM 5800 C CB . CYS B 1 133 ? 1.422 31.317 5.353 1.00 25.89 ? 133 CYS B CB 1 ATOM 5801 S SG . CYS B 1 133 ? 2.297 31.749 3.823 1.00 24.23 ? 133 CYS B SG 1 ATOM 5802 N N . VAL B 1 134 ? 1.754 28.608 7.942 1.00 31.39 ? 134 VAL B N 1 ATOM 5803 C CA . VAL B 1 134 ? 1.196 28.142 9.198 1.00 30.95 ? 134 VAL B CA 1 ATOM 5804 C C . VAL B 1 134 ? 2.140 28.371 10.323 1.00 28.95 ? 134 VAL B C 1 ATOM 5805 O O . VAL B 1 134 ? 3.205 27.722 10.414 1.00 32.31 ? 134 VAL B O 1 ATOM 5806 C CB . VAL B 1 134 ? 0.865 26.640 9.111 1.00 36.99 ? 134 VAL B CB 1 ATOM 5807 C CG1 . VAL B 1 134 ? 0.547 26.081 10.493 1.00 41.93 ? 134 VAL B CG1 1 ATOM 5808 C CG2 . VAL B 1 134 ? -0.345 26.449 8.188 1.00 39.35 ? 134 VAL B CG2 1 ATOM 5809 N N . GLN B 1 135 ? 1.750 29.289 11.203 1.00 23.23 ? 135 GLN B N 1 ATOM 5810 C CA . GLN B 1 135 ? 2.523 29.624 12.376 1.00 22.78 ? 135 GLN B CA 1 ATOM 5811 C C . GLN B 1 135 ? 2.574 28.514 13.425 1.00 22.92 ? 135 GLN B C 1 ATOM 5812 O O . GLN B 1 135 ? 1.573 27.956 13.776 1.00 26.55 ? 135 GLN B O 1 ATOM 5813 C CB . GLN B 1 135 ? 1.995 30.885 13.015 1.00 21.47 ? 135 GLN B CB 1 ATOM 5814 C CG . GLN B 1 135 ? 2.822 31.285 14.184 1.00 22.79 ? 135 GLN B CG 1 ATOM 5815 C CD . GLN B 1 135 ? 2.400 32.601 14.726 1.00 23.15 ? 135 GLN B CD 1 ATOM 5816 O OE1 . GLN B 1 135 ? 2.780 33.668 14.216 1.00 23.97 ? 135 GLN B OE1 1 ATOM 5817 N NE2 . GLN B 1 135 ? 1.655 32.549 15.809 1.00 20.94 ? 135 GLN B NE2 1 ATOM 5818 N N . GLY B 1 136 ? 3.755 28.155 13.879 1.00 25.81 ? 136 GLY B N 1 ATOM 5819 C CA . GLY B 1 136 ? 3.891 27.130 14.907 1.00 25.63 ? 136 GLY B CA 1 ATOM 5820 C C . GLY B 1 136 ? 5.293 26.672 15.011 1.00 23.85 ? 136 GLY B C 1 ATOM 5821 O O . GLY B 1 136 ? 5.991 26.557 13.988 1.00 23.00 ? 136 GLY B O 1 ATOM 5822 N N . ASP B 1 137 ? 5.670 26.301 16.232 1.00 24.62 ? 137 ASP B N 1 ATOM 5823 C CA . ASP B 1 137 ? 7.005 25.835 16.507 1.00 29.36 ? 137 ASP B CA 1 ATOM 5824 C C . ASP B 1 137 ? 8.076 26.829 15.993 1.00 30.76 ? 137 ASP B C 1 ATOM 5825 O O . ASP B 1 137 ? 8.048 27.973 16.397 1.00 30.06 ? 137 ASP B O 1 ATOM 5826 C CB . ASP B 1 137 ? 7.201 24.449 15.926 1.00 33.27 ? 137 ASP B CB 1 ATOM 5827 C CG . ASP B 1 137 ? 6.344 23.415 16.609 1.00 40.26 ? 137 ASP B CG 1 ATOM 5828 O OD1 . ASP B 1 137 ? 5.511 23.744 17.494 1.00 39.44 ? 137 ASP B OD1 1 ATOM 5829 O OD2 . ASP B 1 137 ? 6.515 22.263 16.218 1.00 46.12 ? 137 ASP B OD2 1 ATOM 5830 N N . GLU B 1 138 ? 9.009 26.384 15.151 1.00 29.04 ? 138 GLU B N 1 ATOM 5831 C CA . GLU B 1 138 ? 10.052 27.252 14.598 1.00 32.68 ? 138 GLU B CA 1 ATOM 5832 C C . GLU B 1 138 ? 9.563 28.158 13.462 1.00 27.75 ? 138 GLU B C 1 ATOM 5833 O O . GLU B 1 138 ? 10.235 29.115 13.150 1.00 28.84 ? 138 GLU B O 1 ATOM 5834 C CB . GLU B 1 138 ? 11.250 26.444 14.096 1.00 36.66 ? 138 GLU B CB 1 ATOM 5835 C CG . GLU B 1 138 ? 12.048 25.732 15.163 1.00 43.67 ? 138 GLU B CG 1 ATOM 5836 C CD . GLU B 1 138 ? 12.250 26.585 16.404 1.00 48.51 ? 138 GLU B CD 1 ATOM 5837 O OE1 . GLU B 1 138 ? 13.302 27.255 16.546 1.00 64.47 ? 138 GLU B OE1 1 ATOM 5838 O OE2 . GLU B 1 138 ? 11.352 26.576 17.270 1.00 72.28 ? 138 GLU B OE2 1 ATOM 5839 N N . CYS B 1 139 ? 8.423 27.866 12.861 1.00 23.91 ? 139 CYS B N 1 ATOM 5840 C CA . CYS B 1 139 ? 7.848 28.722 11.796 1.00 22.95 ? 139 CYS B CA 1 ATOM 5841 C C . CYS B 1 139 ? 7.097 29.956 12.316 1.00 20.08 ? 139 CYS B C 1 ATOM 5842 O O . CYS B 1 139 ? 6.047 29.833 12.951 1.00 23.49 ? 139 CYS B O 1 ATOM 5843 C CB . CYS B 1 139 ? 6.946 27.859 10.902 1.00 22.28 ? 139 CYS B CB 1 ATOM 5844 S SG . CYS B 1 139 ? 6.081 28.796 9.645 1.00 24.08 ? 139 CYS B SG 1 ATOM 5845 N N . PHE B 1 140 ? 7.621 31.145 12.059 1.00 20.28 ? 140 PHE B N 1 ATOM 5846 C CA . PHE B 1 140 ? 7.042 32.426 12.565 1.00 19.02 ? 140 PHE B CA 1 ATOM 5847 C C . PHE B 1 140 ? 6.920 33.274 11.309 1.00 21.43 ? 140 PHE B C 1 ATOM 5848 O O . PHE B 1 140 ? 7.732 34.191 11.073 1.00 20.85 ? 140 PHE B O 1 ATOM 5849 C CB . PHE B 1 140 ? 7.967 33.025 13.598 1.00 18.36 ? 140 PHE B CB 1 ATOM 5850 C CG . PHE B 1 140 ? 7.513 34.339 14.228 1.00 18.94 ? 140 PHE B CG 1 ATOM 5851 C CD1 . PHE B 1 140 ? 6.185 34.665 14.423 1.00 18.72 ? 140 PHE B CD1 1 ATOM 5852 C CD2 . PHE B 1 140 ? 8.464 35.258 14.661 1.00 19.89 ? 140 PHE B CD2 1 ATOM 5853 C CE1 . PHE B 1 140 ? 5.826 35.860 14.981 1.00 17.57 ? 140 PHE B CE1 1 ATOM 5854 C CE2 . PHE B 1 140 ? 8.095 36.461 15.288 1.00 17.83 ? 140 PHE B CE2 1 ATOM 5855 C CZ . PHE B 1 140 ? 6.783 36.746 15.444 1.00 17.72 ? 140 PHE B CZ 1 ATOM 5856 N N . PRO B 1 141 ? 5.936 32.941 10.470 1.00 20.64 ? 141 PRO B N 1 ATOM 5857 C CA . PRO B 1 141 ? 5.946 33.462 9.113 1.00 21.04 ? 141 PRO B CA 1 ATOM 5858 C C . PRO B 1 141 ? 5.677 34.960 9.046 1.00 19.61 ? 141 PRO B C 1 ATOM 5859 O O . PRO B 1 141 ? 5.037 35.535 9.918 1.00 19.62 ? 141 PRO B O 1 ATOM 5860 C CB . PRO B 1 141 ? 4.852 32.664 8.403 1.00 23.42 ? 141 PRO B CB 1 ATOM 5861 C CG . PRO B 1 141 ? 3.918 32.207 9.488 1.00 25.14 ? 141 PRO B CG 1 ATOM 5862 C CD . PRO B 1 141 ? 4.835 31.975 10.693 1.00 22.68 ? 141 PRO B CD 1 ATOM 5863 N N . ILE B 1 142 ? 6.229 35.594 8.018 1.00 17.65 ? 142 ILE B N 1 ATOM 5864 C CA . ILE B 1 142 ? 6.062 37.072 7.832 1.00 18.97 ? 142 ILE B CA 1 ATOM 5865 C C . ILE B 1 142 ? 4.882 37.241 6.901 1.00 18.90 ? 142 ILE B C 1 ATOM 5866 O O . ILE B 1 142 ? 5.023 36.995 5.706 1.00 18.96 ? 142 ILE B O 1 ATOM 5867 C CB . ILE B 1 142 ? 7.374 37.680 7.228 1.00 17.96 ? 142 ILE B CB 1 ATOM 5868 C CG1 . ILE B 1 142 ? 8.500 37.717 8.342 1.00 18.32 ? 142 ILE B CG1 1 ATOM 5869 C CG2 . ILE B 1 142 ? 7.155 39.044 6.665 1.00 17.34 ? 142 ILE B CG2 1 ATOM 5870 C CD1 . ILE B 1 142 ? 9.885 37.642 7.758 1.00 19.00 ? 142 ILE B CD1 1 ATOM 5871 N N . MET B 1 143 ? 3.745 37.673 7.438 1.00 18.01 ? 143 MET B N 1 ATOM 5872 C CA . MET B 1 143 ? 2.510 37.758 6.700 1.00 19.26 ? 143 MET B CA 1 ATOM 5873 C C . MET B 1 143 ? 2.440 39.039 5.907 1.00 18.47 ? 143 MET B C 1 ATOM 5874 O O . MET B 1 143 ? 2.920 40.055 6.356 1.00 19.05 ? 143 MET B O 1 ATOM 5875 C CB . MET B 1 143 ? 1.276 37.629 7.638 1.00 19.36 ? 143 MET B CB 1 ATOM 5876 C CG . MET B 1 143 ? 1.241 36.384 8.497 1.00 18.36 ? 143 MET B CG 1 ATOM 5877 S SD . MET B 1 143 ? 1.217 34.815 7.630 1.00 21.34 ? 143 MET B SD 1 ATOM 5878 C CE . MET B 1 143 ? -0.277 34.881 6.689 1.00 21.85 ? 143 MET B CE 1 ATOM 5879 N N . PHE B 1 144 ? 1.935 38.946 4.680 1.00 19.71 ? 144 PHE B N 1 ATOM 5880 C CA . PHE B 1 144 ? 1.763 40.120 3.857 1.00 21.88 ? 144 PHE B CA 1 ATOM 5881 C C . PHE B 1 144 ? 0.541 40.896 4.334 1.00 22.93 ? 144 PHE B C 1 ATOM 5882 O O . PHE B 1 144 ? -0.458 40.306 4.667 1.00 25.72 ? 144 PHE B O 1 ATOM 5883 C CB . PHE B 1 144 ? 1.618 39.787 2.390 1.00 20.59 ? 144 PHE B CB 1 ATOM 5884 C CG . PHE B 1 144 ? 2.774 39.042 1.829 1.00 22.85 ? 144 PHE B CG 1 ATOM 5885 C CD1 . PHE B 1 144 ? 4.060 39.264 2.283 1.00 24.51 ? 144 PHE B CD1 1 ATOM 5886 C CD2 . PHE B 1 144 ? 2.575 38.106 0.852 1.00 20.88 ? 144 PHE B CD2 1 ATOM 5887 C CE1 . PHE B 1 144 ? 5.115 38.550 1.766 1.00 23.43 ? 144 PHE B CE1 1 ATOM 5888 C CE2 . PHE B 1 144 ? 3.625 37.392 0.334 1.00 22.31 ? 144 PHE B CE2 1 ATOM 5889 C CZ . PHE B 1 144 ? 4.900 37.602 0.789 1.00 21.91 ? 144 PHE B CZ 1 ATOM 5890 N N . PRO B 1 145 ? 0.650 42.208 4.405 1.00 21.30 ? 145 PRO B N 1 ATOM 5891 C CA . PRO B 1 145 ? -0.495 43.020 4.702 1.00 22.27 ? 145 PRO B CA 1 ATOM 5892 C C . PRO B 1 145 ? -1.350 43.221 3.454 1.00 25.38 ? 145 PRO B C 1 ATOM 5893 O O . PRO B 1 145 ? -0.872 43.010 2.310 1.00 19.67 ? 145 PRO B O 1 ATOM 5894 C CB . PRO B 1 145 ? 0.107 44.357 5.046 1.00 20.99 ? 145 PRO B CB 1 ATOM 5895 C CG . PRO B 1 145 ? 1.294 44.418 4.156 1.00 21.52 ? 145 PRO B CG 1 ATOM 5896 C CD . PRO B 1 145 ? 1.853 43.013 4.203 1.00 21.02 ? 145 PRO B CD 1 ATOM 5897 N N . LYS B 1 146 ? -2.614 43.576 3.702 1.00 28.03 ? 146 LYS B N 1 ATOM 5898 C CA . LYS B 1 146 ? -3.546 44.039 2.647 1.00 34.28 ? 146 LYS B CA 1 ATOM 5899 C C . LYS B 1 146 ? -2.877 44.860 1.536 1.00 31.69 ? 146 LYS B C 1 ATOM 5900 O O . LYS B 1 146 ? -2.087 45.741 1.797 1.00 30.76 ? 146 LYS B O 1 ATOM 5901 C CB . LYS B 1 146 ? -4.610 44.936 3.308 1.00 40.23 ? 146 LYS B CB 1 ATOM 5902 C CG . LYS B 1 146 ? -5.888 45.065 2.526 1.00 49.29 ? 146 LYS B CG 1 ATOM 5903 C CD . LYS B 1 146 ? -6.887 46.062 3.144 1.00 55.32 ? 146 LYS B CD 1 ATOM 5904 C CE . LYS B 1 146 ? -7.721 46.777 2.092 1.00 56.71 ? 146 LYS B CE 1 ATOM 5905 N NZ . LYS B 1 146 ? -8.033 45.900 0.924 1.00 57.15 ? 146 LYS B NZ 1 ATOM 5906 N N . ASN B 1 147 ? -3.207 44.574 0.292 1.00 33.50 ? 147 ASN B N 1 ATOM 5907 C CA . ASN B 1 147 ? -2.672 45.382 -0.822 1.00 35.75 ? 147 ASN B CA 1 ATOM 5908 C C . ASN B 1 147 ? -1.182 45.204 -1.129 1.00 28.61 ? 147 ASN B C 1 ATOM 5909 O O . ASN B 1 147 ? -0.676 45.903 -2.001 1.00 27.64 ? 147 ASN B O 1 ATOM 5910 C CB . ASN B 1 147 ? -2.888 46.895 -0.637 1.00 37.33 ? 147 ASN B CB 1 ATOM 5911 C CG . ASN B 1 147 ? -4.341 47.277 -0.376 1.00 46.41 ? 147 ASN B CG 1 ATOM 5912 O OD1 . ASN B 1 147 ? -4.631 48.076 0.537 1.00 48.59 ? 147 ASN B OD1 1 ATOM 5913 N ND2 . ASN B 1 147 ? -5.250 46.730 -1.166 1.00 43.97 ? 147 ASN B ND2 1 ATOM 5914 N N . ASP B 1 148 ? -0.472 44.334 -0.428 1.00 25.91 ? 148 ASP B N 1 ATOM 5915 C CA . ASP B 1 148 ? 0.935 44.057 -0.794 1.00 21.97 ? 148 ASP B CA 1 ATOM 5916 C C . ASP B 1 148 ? 1.022 43.444 -2.197 1.00 20.74 ? 148 ASP B C 1 ATOM 5917 O O . ASP B 1 148 ? 0.426 42.394 -2.476 1.00 20.62 ? 148 ASP B O 1 ATOM 5918 C CB . ASP B 1 148 ? 1.549 43.101 0.198 1.00 21.52 ? 148 ASP B CB 1 ATOM 5919 C CG . ASP B 1 148 ? 3.071 43.156 0.211 1.00 20.30 ? 148 ASP B CG 1 ATOM 5920 O OD1 . ASP B 1 148 ? 3.701 42.929 -0.854 1.00 18.66 ? 148 ASP B OD1 1 ATOM 5921 O OD2 . ASP B 1 148 ? 3.663 43.382 1.324 1.00 24.17 ? 148 ASP B OD2 1 ATOM 5922 N N . PRO B 1 149 ? 1.830 44.053 -3.053 1.00 23.12 ? 149 PRO B N 1 ATOM 5923 C CA . PRO B 1 149 ? 2.011 43.502 -4.395 1.00 22.07 ? 149 PRO B CA 1 ATOM 5924 C C . PRO B 1 149 ? 2.364 42.039 -4.375 1.00 20.96 ? 149 PRO B C 1 ATOM 5925 O O . PRO B 1 149 ? 1.953 41.296 -5.266 1.00 18.71 ? 149 PRO B O 1 ATOM 5926 C CB . PRO B 1 149 ? 3.188 44.304 -4.934 1.00 21.54 ? 149 PRO B CB 1 ATOM 5927 C CG . PRO B 1 149 ? 3.008 45.610 -4.288 1.00 22.35 ? 149 PRO B CG 1 ATOM 5928 C CD . PRO B 1 149 ? 2.668 45.255 -2.859 1.00 22.19 ? 149 PRO B CD 1 ATOM 5929 N N . LYS B 1 150 ? 3.106 41.598 -3.359 1.00 19.25 ? 150 LYS B N 1 ATOM 5930 C CA . LYS B 1 150 ? 3.521 40.215 -3.317 1.00 17.58 ? 150 LYS B CA 1 ATOM 5931 C C . LYS B 1 150 ? 2.391 39.210 -3.160 1.00 17.89 ? 150 LYS B C 1 ATOM 5932 O O . LYS B 1 150 ? 2.630 38.012 -3.381 1.00 19.01 ? 150 LYS B O 1 ATOM 5933 C CB . LYS B 1 150 ? 4.604 39.965 -2.208 1.00 16.92 ? 150 LYS B CB 1 ATOM 5934 C CG . LYS B 1 150 ? 5.936 40.602 -2.489 1.00 16.48 ? 150 LYS B CG 1 ATOM 5935 C CD . LYS B 1 150 ? 6.925 40.287 -1.368 1.00 17.33 ? 150 LYS B CD 1 ATOM 5936 C CE . LYS B 1 150 ? 8.316 40.785 -1.696 1.00 17.87 ? 150 LYS B CE 1 ATOM 5937 N NZ . LYS B 1 150 ? 8.772 40.251 -3.015 1.00 19.88 ? 150 LYS B NZ 1 ATOM 5938 N N . LEU B 1 151 ? 1.212 39.658 -2.745 1.00 17.67 ? 151 LEU B N 1 ATOM 5939 C CA . LEU B 1 151 ? 0.032 38.796 -2.696 1.00 21.02 ? 151 LEU B CA 1 ATOM 5940 C C . LEU B 1 151 ? -0.318 38.283 -4.106 1.00 23.58 ? 151 LEU B C 1 ATOM 5941 O O . LEU B 1 151 ? -0.867 37.208 -4.232 1.00 22.82 ? 151 LEU B O 1 ATOM 5942 C CB . LEU B 1 151 ? -1.221 39.544 -2.165 1.00 21.92 ? 151 LEU B CB 1 ATOM 5943 C CG . LEU B 1 151 ? -1.131 39.957 -0.729 1.00 22.53 ? 151 LEU B CG 1 ATOM 5944 C CD1 . LEU B 1 151 ? -2.127 41.074 -0.424 1.00 22.08 ? 151 LEU B CD1 1 ATOM 5945 C CD2 . LEU B 1 151 ? -1.314 38.708 0.126 1.00 24.16 ? 151 LEU B CD2 1 ATOM 5946 N N . LYS B 1 152 ? 0.056 39.027 -5.146 1.00 25.30 ? 152 LYS B N 1 ATOM 5947 C CA . LYS B 1 152 ? -0.225 38.582 -6.522 1.00 27.75 ? 152 LYS B CA 1 ATOM 5948 C C . LYS B 1 152 ? 0.780 37.608 -7.086 1.00 32.28 ? 152 LYS B C 1 ATOM 5949 O O . LYS B 1 152 ? 0.495 36.966 -8.103 1.00 35.60 ? 152 LYS B O 1 ATOM 5950 C CB . LYS B 1 152 ? -0.348 39.782 -7.430 1.00 27.17 ? 152 LYS B CB 1 ATOM 5951 C CG . LYS B 1 152 ? -1.619 40.546 -7.152 1.00 29.82 ? 152 LYS B CG 1 ATOM 5952 C CD . LYS B 1 152 ? -1.360 42.016 -7.327 1.00 36.45 ? 152 LYS B CD 1 ATOM 5953 C CE . LYS B 1 152 ? -2.662 42.806 -7.361 1.00 39.02 ? 152 LYS B CE 1 ATOM 5954 N NZ . LYS B 1 152 ? -3.109 43.077 -8.760 1.00 42.16 ? 152 LYS B NZ 1 ATOM 5955 N N . THR B 1 153 ? 1.959 37.497 -6.469 1.00 32.77 ? 153 THR B N 1 ATOM 5956 C CA . THR B 1 153 ? 2.984 36.607 -6.986 1.00 31.02 ? 153 THR B CA 1 ATOM 5957 C C . THR B 1 153 ? 3.555 35.595 -6.034 1.00 30.14 ? 153 THR B C 1 ATOM 5958 O O . THR B 1 153 ? 4.198 34.658 -6.500 1.00 30.55 ? 153 THR B O 1 ATOM 5959 C CB . THR B 1 153 ? 4.164 37.428 -7.523 1.00 34.51 ? 153 THR B CB 1 ATOM 5960 O OG1 . THR B 1 153 ? 4.578 38.372 -6.532 1.00 32.20 ? 153 THR B OG1 1 ATOM 5961 C CG2 . THR B 1 153 ? 3.719 38.183 -8.767 1.00 34.86 ? 153 THR B CG2 1 ATOM 5962 N N . GLN B 1 154 ? 3.392 35.773 -4.722 1.00 26.07 ? 154 GLN B N 1 ATOM 5963 C CA . GLN B 1 154 ? 4.128 34.942 -3.776 1.00 26.65 ? 154 GLN B CA 1 ATOM 5964 C C . GLN B 1 154 ? 3.271 34.395 -2.675 1.00 25.10 ? 154 GLN B C 1 ATOM 5965 O O . GLN B 1 154 ? 3.806 34.008 -1.678 1.00 26.48 ? 154 GLN B O 1 ATOM 5966 C CB . GLN B 1 154 ? 5.254 35.731 -3.049 1.00 25.56 ? 154 GLN B CB 1 ATOM 5967 C CG . GLN B 1 154 ? 6.451 36.059 -3.883 1.00 25.94 ? 154 GLN B CG 1 ATOM 5968 C CD . GLN B 1 154 ? 7.441 36.931 -3.142 1.00 22.30 ? 154 GLN B CD 1 ATOM 5969 O OE1 . GLN B 1 154 ? 7.889 37.911 -3.663 1.00 22.42 ? 154 GLN B OE1 1 ATOM 5970 N NE2 . GLN B 1 154 ? 7.770 36.568 -1.927 1.00 19.33 ? 154 GLN B NE2 1 ATOM 5971 N N . GLY B 1 155 ? 1.966 34.432 -2.793 1.00 25.98 ? 155 GLY B N 1 ATOM 5972 C CA . GLY B 1 155 ? 1.122 33.889 -1.706 1.00 25.66 ? 155 GLY B CA 1 ATOM 5973 C C . GLY B 1 155 ? 0.924 34.858 -0.567 1.00 24.84 ? 155 GLY B C 1 ATOM 5974 O O . GLY B 1 155 ? 0.888 36.085 -0.772 1.00 24.00 ? 155 GLY B O 1 ATOM 5975 N N . LYS B 1 156 ? 0.751 34.316 0.624 1.00 25.49 ? 156 LYS B N 1 ATOM 5976 C CA . LYS B 1 156 ? 0.262 35.079 1.760 1.00 26.71 ? 156 LYS B CA 1 ATOM 5977 C C . LYS B 1 156 ? 1.391 35.547 2.692 1.00 23.19 ? 156 LYS B C 1 ATOM 5978 O O . LYS B 1 156 ? 1.170 36.405 3.539 1.00 20.19 ? 156 LYS B O 1 ATOM 5979 C CB . LYS B 1 156 ? -0.732 34.236 2.562 1.00 30.48 ? 156 LYS B CB 1 ATOM 5980 C CG . LYS B 1 156 ? -2.039 33.942 1.848 1.00 36.52 ? 156 LYS B CG 1 ATOM 5981 C CD . LYS B 1 156 ? -2.853 35.213 1.577 1.00 42.98 ? 156 LYS B CD 1 ATOM 5982 C CE . LYS B 1 156 ? -4.095 34.962 0.705 1.00 51.55 ? 156 LYS B CE 1 ATOM 5983 N NZ . LYS B 1 156 ? -4.323 36.019 -0.341 1.00 51.31 ? 156 LYS B NZ 1 ATOM 5984 N N . CYS B 1 157 ? 2.571 34.974 2.536 1.00 20.24 ? 157 CYS B N 1 ATOM 5985 C CA . CYS B 1 157 ? 3.653 35.232 3.483 1.00 21.74 ? 157 CYS B CA 1 ATOM 5986 C C . CYS B 1 157 ? 4.990 34.943 2.872 1.00 21.91 ? 157 CYS B C 1 ATOM 5987 O O . CYS B 1 157 ? 5.063 34.402 1.767 1.00 22.29 ? 157 CYS B O 1 ATOM 5988 C CB . CYS B 1 157 ? 3.439 34.390 4.731 1.00 19.47 ? 157 CYS B CB 1 ATOM 5989 S SG . CYS B 1 157 ? 3.955 32.667 4.546 1.00 19.68 ? 157 CYS B SG 1 ATOM 5990 N N . MET B 1 158 ? 6.041 35.282 3.615 1.00 21.05 ? 158 MET B N 1 ATOM 5991 C CA . MET B 1 158 ? 7.360 34.781 3.435 1.00 21.94 ? 158 MET B CA 1 ATOM 5992 C C . MET B 1 158 ? 7.639 33.895 4.611 1.00 22.16 ? 158 MET B C 1 ATOM 5993 O O . MET B 1 158 ? 7.379 34.271 5.759 1.00 19.52 ? 158 MET B O 1 ATOM 5994 C CB . MET B 1 158 ? 8.361 35.968 3.527 1.00 23.37 ? 158 MET B CB 1 ATOM 5995 C CG . MET B 1 158 ? 8.340 36.906 2.323 1.00 25.00 ? 158 MET B CG 1 ATOM 5996 S SD . MET B 1 158 ? 8.946 38.623 2.536 1.00 25.51 ? 158 MET B SD 1 ATOM 5997 C CE . MET B 1 158 ? 10.215 38.163 3.664 1.00 22.90 ? 158 MET B CE 1 ATOM 5998 N N . PRO B 1 159 ? 8.171 32.715 4.366 1.00 21.63 ? 159 PRO B N 1 ATOM 5999 C CA . PRO B 1 159 ? 8.490 31.887 5.513 1.00 21.15 ? 159 PRO B CA 1 ATOM 6000 C C . PRO B 1 159 ? 9.669 32.436 6.284 1.00 20.95 ? 159 PRO B C 1 ATOM 6001 O O . PRO B 1 159 ? 10.581 33.133 5.706 1.00 19.90 ? 159 PRO B O 1 ATOM 6002 C CB . PRO B 1 159 ? 8.894 30.545 4.880 1.00 22.10 ? 159 PRO B CB 1 ATOM 6003 C CG . PRO B 1 159 ? 9.496 30.928 3.592 1.00 23.84 ? 159 PRO B CG 1 ATOM 6004 C CD . PRO B 1 159 ? 8.596 32.084 3.112 1.00 24.36 ? 159 PRO B CD 1 ATOM 6005 N N . PHE B 1 160 ? 9.707 32.079 7.559 1.00 19.23 ? 160 PHE B N 1 ATOM 6006 C CA . PHE B 1 160 ? 10.729 32.572 8.506 1.00 16.41 ? 160 PHE B CA 1 ATOM 6007 C C . PHE B 1 160 ? 10.853 31.582 9.647 1.00 17.15 ? 160 PHE B C 1 ATOM 6008 O O . PHE B 1 160 ? 9.870 31.267 10.289 1.00 15.82 ? 160 PHE B O 1 ATOM 6009 C CB . PHE B 1 160 ? 10.259 33.887 9.043 1.00 17.20 ? 160 PHE B CB 1 ATOM 6010 C CG . PHE B 1 160 ? 11.141 34.461 10.135 1.00 17.95 ? 160 PHE B CG 1 ATOM 6011 C CD1 . PHE B 1 160 ? 10.989 34.069 11.481 1.00 17.14 ? 160 PHE B CD1 1 ATOM 6012 C CD2 . PHE B 1 160 ? 12.001 35.517 9.841 1.00 18.48 ? 160 PHE B CD2 1 ATOM 6013 C CE1 . PHE B 1 160 ? 11.742 34.680 12.498 1.00 18.30 ? 160 PHE B CE1 1 ATOM 6014 C CE2 . PHE B 1 160 ? 12.783 36.094 10.846 1.00 18.90 ? 160 PHE B CE2 1 ATOM 6015 C CZ . PHE B 1 160 ? 12.653 35.674 12.181 1.00 18.33 ? 160 PHE B CZ 1 ATOM 6016 N N . PHE B 1 161 ? 12.071 31.130 9.920 1.00 20.19 ? 161 PHE B N 1 ATOM 6017 C CA . PHE B 1 161 ? 12.352 30.222 10.985 1.00 21.82 ? 161 PHE B CA 1 ATOM 6018 C C . PHE B 1 161 ? 13.152 30.870 12.106 1.00 21.38 ? 161 PHE B C 1 ATOM 6019 O O . PHE B 1 161 ? 14.124 31.566 11.849 1.00 17.52 ? 161 PHE B O 1 ATOM 6020 C CB . PHE B 1 161 ? 13.096 29.013 10.447 1.00 26.65 ? 161 PHE B CB 1 ATOM 6021 C CG . PHE B 1 161 ? 12.195 28.061 9.727 1.00 31.33 ? 161 PHE B CG 1 ATOM 6022 C CD1 . PHE B 1 161 ? 11.831 28.325 8.424 1.00 37.30 ? 161 PHE B CD1 1 ATOM 6023 C CD2 . PHE B 1 161 ? 11.696 26.933 10.366 1.00 35.78 ? 161 PHE B CD2 1 ATOM 6024 C CE1 . PHE B 1 161 ? 10.986 27.478 7.746 1.00 36.38 ? 161 PHE B CE1 1 ATOM 6025 C CE2 . PHE B 1 161 ? 10.861 26.057 9.691 1.00 36.92 ? 161 PHE B CE2 1 ATOM 6026 C CZ . PHE B 1 161 ? 10.498 26.340 8.389 1.00 38.21 ? 161 PHE B CZ 1 ATOM 6027 N N . ARG B 1 162 ? 12.722 30.602 13.348 1.00 18.45 ? 162 ARG B N 1 ATOM 6028 C CA . ARG B 1 162 ? 13.310 31.168 14.535 1.00 17.72 ? 162 ARG B CA 1 ATOM 6029 C C . ARG B 1 162 ? 14.755 30.792 14.769 1.00 17.26 ? 162 ARG B C 1 ATOM 6030 O O . ARG B 1 162 ? 15.219 29.730 14.343 1.00 15.57 ? 162 ARG B O 1 ATOM 6031 C CB . ARG B 1 162 ? 12.440 30.723 15.758 1.00 18.85 ? 162 ARG B CB 1 ATOM 6032 C CG . ARG B 1 162 ? 11.029 31.284 15.700 1.00 20.02 ? 162 ARG B CG 1 ATOM 6033 C CD . ARG B 1 162 ? 10.341 31.257 17.063 1.00 19.84 ? 162 ARG B CD 1 ATOM 6034 N NE . ARG B 1 162 ? 10.998 32.162 18.030 1.00 21.90 ? 162 ARG B NE 1 ATOM 6035 C CZ . ARG B 1 162 ? 10.743 32.204 19.333 1.00 22.65 ? 162 ARG B CZ 1 ATOM 6036 N NH1 . ARG B 1 162 ? 9.828 31.364 19.848 1.00 26.03 ? 162 ARG B NH1 1 ATOM 6037 N NH2 . ARG B 1 162 ? 11.413 33.061 20.125 1.00 23.57 ? 162 ARG B NH2 1 ATOM 6038 N N . ALA B 1 163 ? 15.483 31.683 15.415 1.00 17.33 ? 163 ALA B N 1 ATOM 6039 C CA . ALA B 1 163 ? 16.905 31.485 15.690 1.00 20.68 ? 163 ALA B CA 1 ATOM 6040 C C . ALA B 1 163 ? 17.076 30.386 16.741 1.00 21.99 ? 163 ALA B C 1 ATOM 6041 O O . ALA B 1 163 ? 16.210 30.176 17.580 1.00 22.83 ? 163 ALA B O 1 ATOM 6042 C CB . ALA B 1 163 ? 17.568 32.758 16.177 1.00 21.03 ? 163 ALA B CB 1 ATOM 6043 N N . GLY B 1 164 ? 18.162 29.650 16.599 1.00 23.93 ? 164 GLY B N 1 ATOM 6044 C CA . GLY B 1 164 ? 18.490 28.576 17.509 1.00 27.25 ? 164 GLY B CA 1 ATOM 6045 C C . GLY B 1 164 ? 18.783 29.166 18.886 1.00 27.74 ? 164 GLY B C 1 ATOM 6046 O O . GLY B 1 164 ? 19.046 30.379 19.003 1.00 23.29 ? 164 GLY B O 1 ATOM 6047 N N . PHE B 1 165 ? 18.764 28.336 19.933 1.00 25.03 ? 165 PHE B N 1 ATOM 6048 C CA . PHE B 1 165 ? 19.010 28.893 21.266 1.00 26.96 ? 165 PHE B CA 1 ATOM 6049 C C . PHE B 1 165 ? 19.665 27.900 22.229 1.00 28.06 ? 165 PHE B C 1 ATOM 6050 O O . PHE B 1 165 ? 19.653 26.702 21.965 1.00 23.43 ? 165 PHE B O 1 ATOM 6051 C CB . PHE B 1 165 ? 17.688 29.396 21.812 1.00 27.12 ? 165 PHE B CB 1 ATOM 6052 C CG . PHE B 1 165 ? 16.658 28.347 21.851 1.00 27.27 ? 165 PHE B CG 1 ATOM 6053 C CD1 . PHE B 1 165 ? 15.949 28.014 20.691 1.00 31.57 ? 165 PHE B CD1 1 ATOM 6054 C CD2 . PHE B 1 165 ? 16.447 27.630 22.989 1.00 31.23 ? 165 PHE B CD2 1 ATOM 6055 C CE1 . PHE B 1 165 ? 15.024 27.014 20.682 1.00 28.02 ? 165 PHE B CE1 1 ATOM 6056 C CE2 . PHE B 1 165 ? 15.506 26.622 22.997 1.00 30.75 ? 165 PHE B CE2 1 ATOM 6057 C CZ . PHE B 1 165 ? 14.777 26.329 21.853 1.00 30.58 ? 165 PHE B CZ 1 ATOM 6058 N N . VAL B 1 166 ? 20.235 28.419 23.324 1.00 29.56 ? 166 VAL B N 1 ATOM 6059 C CA . VAL B 1 166 ? 20.978 27.582 24.247 1.00 32.24 ? 166 VAL B CA 1 ATOM 6060 C C . VAL B 1 166 ? 20.093 27.001 25.344 1.00 38.04 ? 166 VAL B C 1 ATOM 6061 O O . VAL B 1 166 ? 18.920 27.367 25.495 1.00 33.73 ? 166 VAL B O 1 ATOM 6062 C CB . VAL B 1 166 ? 22.200 28.303 24.912 1.00 33.17 ? 166 VAL B CB 1 ATOM 6063 C CG1 . VAL B 1 166 ? 23.128 28.910 23.861 1.00 36.53 ? 166 VAL B CG1 1 ATOM 6064 C CG2 . VAL B 1 166 ? 21.799 29.351 25.913 1.00 30.36 ? 166 VAL B CG2 1 ATOM 6065 N N . CYS B 1 167 ? 20.753 26.172 26.156 1.00 53.25 ? 167 CYS B N 1 ATOM 6066 C CA . CYS B 1 167 ? 20.294 25.726 27.497 1.00 63.68 ? 167 CYS B CA 1 ATOM 6067 C C . CYS B 1 167 ? 19.407 24.651 26.983 1.00 64.36 ? 167 CYS B C 1 ATOM 6068 O O . CYS B 1 167 ? 18.217 24.578 27.266 1.00 81.11 ? 167 CYS B O 1 ATOM 6069 C CB . CYS B 1 167 ? 19.620 26.833 28.317 1.00 69.93 ? 167 CYS B CB 1 ATOM 6070 S SG . CYS B 1 167 ? 18.635 26.314 29.741 1.00 90.56 ? 167 CYS B SG 1 ATOM 6071 N N . PRO B 1 168 ? 20.047 23.789 26.205 1.00 57.02 ? 168 PRO B N 1 ATOM 6072 C CA . PRO B 1 168 ? 19.702 23.137 24.988 1.00 49.86 ? 168 PRO B CA 1 ATOM 6073 C C . PRO B 1 168 ? 18.278 23.281 24.569 1.00 45.14 ? 168 PRO B C 1 ATOM 6074 O O . PRO B 1 168 ? 17.462 22.853 25.271 1.00 31.94 ? 168 PRO B O 1 ATOM 6075 C CB . PRO B 1 168 ? 20.083 21.734 25.267 1.00 55.25 ? 168 PRO B CB 1 ATOM 6076 C CG . PRO B 1 168 ? 21.382 21.908 25.990 1.00 64.30 ? 168 PRO B CG 1 ATOM 6077 C CD . PRO B 1 168 ? 21.215 23.155 26.815 1.00 63.08 ? 168 PRO B CD 1 ATOM 6078 N N . THR B 1 169 ? 18.050 24.105 23.535 1.00 53.71 ? 169 THR B N 1 ATOM 6079 C CA . THR B 1 169 ? 17.335 23.720 22.290 1.00 56.14 ? 169 THR B CA 1 ATOM 6080 C C . THR B 1 169 ? 15.863 23.147 22.459 1.00 68.20 ? 169 THR B C 1 ATOM 6081 O O . THR B 1 169 ? 15.433 22.879 23.596 1.00 70.55 ? 169 THR B O 1 ATOM 6082 C CB . THR B 1 169 ? 18.426 22.886 21.547 1.00 54.45 ? 169 THR B CB 1 ATOM 6083 O OG1 . THR B 1 169 ? 19.673 23.508 21.876 1.00 43.50 ? 169 THR B OG1 1 ATOM 6084 C CG2 . THR B 1 169 ? 18.323 22.860 19.980 1.00 57.58 ? 169 THR B CG2 1 ATOM 6085 N N . PRO B 1 170 ? 15.068 22.996 21.350 1.00 85.06 ? 170 PRO B N 1 ATOM 6086 C CA . PRO B 1 170 ? 13.556 22.895 21.368 1.00 100.54 ? 170 PRO B CA 1 ATOM 6087 C C . PRO B 1 170 ? 12.711 22.912 22.726 1.00 120.88 ? 170 PRO B C 1 ATOM 6088 O O . PRO B 1 170 ? 12.725 23.957 23.387 1.00 119.42 ? 170 PRO B O 1 ATOM 6089 C CB . PRO B 1 170 ? 13.304 21.696 20.458 1.00 94.83 ? 170 PRO B CB 1 ATOM 6090 C CG . PRO B 1 170 ? 14.379 21.831 19.413 1.00 86.35 ? 170 PRO B CG 1 ATOM 6091 C CD . PRO B 1 170 ? 15.574 22.516 20.045 1.00 80.10 ? 170 PRO B CD 1 ATOM 6092 N N . PRO B 1 171 ? 11.942 21.838 23.121 1.00 138.39 ? 171 PRO B N 1 ATOM 6093 C CA . PRO B 1 171 ? 10.932 22.202 24.177 1.00 137.98 ? 171 PRO B CA 1 ATOM 6094 C C . PRO B 1 171 ? 11.463 22.941 25.428 1.00 136.28 ? 171 PRO B C 1 ATOM 6095 O O . PRO B 1 171 ? 12.638 22.807 25.778 1.00 131.68 ? 171 PRO B O 1 ATOM 6096 C CB . PRO B 1 171 ? 10.280 20.858 24.559 1.00 132.10 ? 171 PRO B CB 1 ATOM 6097 C CG . PRO B 1 171 ? 10.615 19.910 23.459 1.00 131.38 ? 171 PRO B CG 1 ATOM 6098 C CD . PRO B 1 171 ? 11.899 20.389 22.823 1.00 132.44 ? 171 PRO B CD 1 ATOM 6099 N N . TYR B 1 172 ? 10.574 23.689 26.089 1.00 137.65 ? 172 TYR B N 1 ATOM 6100 C CA . TYR B 1 172 ? 10.955 24.785 27.011 1.00 138.16 ? 172 TYR B CA 1 ATOM 6101 C C . TYR B 1 172 ? 10.844 24.444 28.517 1.00 137.09 ? 172 TYR B C 1 ATOM 6102 O O . TYR B 1 172 ? 10.466 23.323 28.876 1.00 136.63 ? 172 TYR B O 1 ATOM 6103 C CB . TYR B 1 172 ? 10.129 26.053 26.663 1.00 139.74 ? 172 TYR B CB 1 ATOM 6104 C CG . TYR B 1 172 ? 8.841 26.264 27.463 1.00 143.43 ? 172 TYR B CG 1 ATOM 6105 C CD1 . TYR B 1 172 ? 7.851 25.273 27.522 1.00 140.33 ? 172 TYR B CD1 1 ATOM 6106 C CD2 . TYR B 1 172 ? 8.607 27.464 28.150 1.00 138.48 ? 172 TYR B CD2 1 ATOM 6107 C CE1 . TYR B 1 172 ? 6.681 25.462 28.254 1.00 137.79 ? 172 TYR B CE1 1 ATOM 6108 C CE2 . TYR B 1 172 ? 7.436 27.659 28.880 1.00 135.33 ? 172 TYR B CE2 1 ATOM 6109 C CZ . TYR B 1 172 ? 6.476 26.658 28.932 1.00 134.88 ? 172 TYR B CZ 1 ATOM 6110 O OH . TYR B 1 172 ? 5.313 26.847 29.658 1.00 120.44 ? 172 TYR B OH 1 ATOM 6111 N N . GLN B 1 173 ? 11.253 25.391 29.374 1.00 130.85 ? 173 GLN B N 1 ATOM 6112 C CA . GLN B 1 173 ? 10.693 25.542 30.736 1.00 119.35 ? 173 GLN B CA 1 ATOM 6113 C C . GLN B 1 173 ? 10.814 26.989 31.323 1.00 115.81 ? 173 GLN B C 1 ATOM 6114 O O . GLN B 1 173 ? 9.957 27.841 31.033 1.00 107.06 ? 173 GLN B O 1 ATOM 6115 C CB . GLN B 1 173 ? 11.243 24.465 31.699 1.00 109.29 ? 173 GLN B CB 1 ATOM 6116 C CG . GLN B 1 173 ? 10.472 24.338 33.012 1.00 100.50 ? 173 GLN B CG 1 ATOM 6117 C CD . GLN B 1 173 ? 11.263 23.618 34.087 1.00 93.86 ? 173 GLN B CD 1 ATOM 6118 O OE1 . GLN B 1 173 ? 12.292 24.114 34.529 1.00 93.84 ? 173 GLN B OE1 1 ATOM 6119 N NE2 . GLN B 1 173 ? 10.784 22.461 34.522 1.00 87.76 ? 173 GLN B NE2 1 ATOM 6120 N N . SER B 1 174 ? 11.817 27.219 32.155 1.00 109.64 ? 174 SER B N 1 ATOM 6121 C CA . SER B 1 174 ? 12.024 28.512 32.816 1.00 95.79 ? 174 SER B CA 1 ATOM 6122 C C . SER B 1 174 ? 13.120 29.246 32.093 1.00 88.18 ? 174 SER B C 1 ATOM 6123 O O . SER B 1 174 ? 13.529 28.674 31.022 1.00 90.83 ? 174 SER B O 1 ATOM 6124 C CB . SER B 1 174 ? 12.467 28.313 34.251 1.00 91.83 ? 174 SER B CB 1 ATOM 6125 O OG . SER B 1 174 ? 13.811 27.871 34.313 1.00 87.84 ? 174 SER B OG 1 ATOM 6126 N N . LEU B 1 175 ? 13.599 30.394 32.725 1.00 68.97 ? 175 LEU B N 1 ATOM 6127 C CA . LEU B 1 175 ? 14.561 31.393 32.199 1.00 52.63 ? 175 LEU B CA 1 ATOM 6128 C C . LEU B 1 175 ? 14.501 31.770 30.716 1.00 36.93 ? 175 LEU B C 1 ATOM 6129 O O . LEU B 1 175 ? 14.442 31.066 29.808 1.00 34.15 ? 175 LEU B O 1 ATOM 6130 C CB . LEU B 1 175 ? 15.988 31.107 32.607 1.00 50.67 ? 175 LEU B CB 1 ATOM 6131 C CG . LEU B 1 175 ? 16.894 32.136 31.961 1.00 54.68 ? 175 LEU B CG 1 ATOM 6132 C CD1 . LEU B 1 175 ? 16.590 33.550 32.446 1.00 53.26 ? 175 LEU B CD1 1 ATOM 6133 C CD2 . LEU B 1 175 ? 18.344 31.759 32.134 1.00 56.78 ? 175 LEU B CD2 1 ATOM 6134 N N . ALA B 1 176 ? 14.534 33.035 30.421 1.00 34.47 ? 176 ALA B N 1 ATOM 6135 C CA . ALA B 1 176 ? 14.227 33.412 29.062 1.00 29.58 ? 176 ALA B CA 1 ATOM 6136 C C . ALA B 1 176 ? 15.199 32.892 27.991 1.00 27.80 ? 176 ALA B C 1 ATOM 6137 O O . ALA B 1 176 ? 16.356 32.873 28.190 1.00 29.84 ? 176 ALA B O 1 ATOM 6138 C CB . ALA B 1 176 ? 14.069 34.894 28.968 1.00 31.08 ? 176 ALA B CB 1 ATOM 6139 N N . ARG B 1 177 ? 14.661 32.487 26.858 1.00 24.11 ? 177 ARG B N 1 ATOM 6140 C CA . ARG B 1 177 ? 15.397 32.038 25.712 1.00 24.54 ? 177 ARG B CA 1 ATOM 6141 C C . ARG B 1 177 ? 16.493 32.968 25.270 1.00 21.27 ? 177 ARG B C 1 ATOM 6142 O O . ARG B 1 177 ? 16.272 34.177 25.074 1.00 24.74 ? 177 ARG B O 1 ATOM 6143 C CB . ARG B 1 177 ? 14.406 31.841 24.564 1.00 27.02 ? 177 ARG B CB 1 ATOM 6144 C CG . ARG B 1 177 ? 15.104 31.454 23.274 1.00 29.40 ? 177 ARG B CG 1 ATOM 6145 C CD . ARG B 1 177 ? 14.140 31.201 22.116 1.00 31.68 ? 177 ARG B CD 1 ATOM 6146 N NE . ARG B 1 177 ? 13.325 30.029 22.253 1.00 29.43 ? 177 ARG B NE 1 ATOM 6147 C CZ . ARG B 1 177 ? 12.663 29.443 21.245 1.00 31.64 ? 177 ARG B CZ 1 ATOM 6148 N NH1 . ARG B 1 177 ? 11.988 28.349 21.543 1.00 29.27 ? 177 ARG B NH1 1 ATOM 6149 N NH2 . ARG B 1 177 ? 12.741 29.828 19.946 1.00 26.74 ? 177 ARG B NH2 1 ATOM 6150 N N . ASP B 1 178 ? 17.679 32.402 25.142 1.00 21.39 ? 178 ASP B N 1 ATOM 6151 C CA . ASP B 1 178 ? 18.879 33.080 24.658 1.00 23.25 ? 178 ASP B CA 1 ATOM 6152 C C . ASP B 1 178 ? 19.415 32.495 23.370 1.00 21.50 ? 178 ASP B C 1 ATOM 6153 O O . ASP B 1 178 ? 19.829 31.336 23.313 1.00 23.79 ? 178 ASP B O 1 ATOM 6154 C CB . ASP B 1 178 ? 20.029 33.021 25.653 1.00 25.97 ? 178 ASP B CB 1 ATOM 6155 C CG . ASP B 1 178 ? 19.886 33.969 26.807 1.00 26.90 ? 178 ASP B CG 1 ATOM 6156 O OD1 . ASP B 1 178 ? 19.429 35.121 26.713 1.00 27.14 ? 178 ASP B OD1 1 ATOM 6157 O OD2 . ASP B 1 178 ? 20.330 33.550 27.848 1.00 32.09 ? 178 ASP B OD2 1 ATOM 6158 N N . GLN B 1 179 ? 19.463 33.333 22.329 1.00 22.10 ? 179 GLN B N 1 ATOM 6159 C CA . GLN B 1 179 ? 20.045 32.908 21.037 1.00 20.67 ? 179 GLN B CA 1 ATOM 6160 C C . GLN B 1 179 ? 21.537 32.733 21.129 1.00 20.02 ? 179 GLN B C 1 ATOM 6161 O O . GLN B 1 179 ? 22.179 33.258 21.976 1.00 25.19 ? 179 GLN B O 1 ATOM 6162 C CB . GLN B 1 179 ? 19.647 33.869 19.896 1.00 19.47 ? 179 GLN B CB 1 ATOM 6163 C CG . GLN B 1 179 ? 18.139 33.846 19.598 1.00 18.04 ? 179 GLN B CG 1 ATOM 6164 C CD . GLN B 1 179 ? 17.285 34.507 20.647 1.00 18.23 ? 179 GLN B CD 1 ATOM 6165 O OE1 . GLN B 1 179 ? 17.709 35.441 21.296 1.00 20.19 ? 179 GLN B OE1 1 ATOM 6166 N NE2 . GLN B 1 179 ? 16.078 34.019 20.822 1.00 18.91 ? 179 GLN B NE2 1 ATOM 6167 N N . ILE B 1 180 ? 22.066 31.920 20.257 1.00 23.38 ? 180 ILE B N 1 ATOM 6168 C CA . ILE B 1 180 ? 23.478 31.564 20.211 1.00 25.62 ? 180 ILE B CA 1 ATOM 6169 C C . ILE B 1 180 ? 24.308 32.510 19.339 1.00 24.98 ? 180 ILE B C 1 ATOM 6170 O O . ILE B 1 180 ? 23.832 33.007 18.299 1.00 24.80 ? 180 ILE B O 1 ATOM 6171 C CB . ILE B 1 180 ? 23.563 30.122 19.665 1.00 30.06 ? 180 ILE B CB 1 ATOM 6172 C CG1 . ILE B 1 180 ? 22.765 29.207 20.626 1.00 36.48 ? 180 ILE B CG1 1 ATOM 6173 C CG2 . ILE B 1 180 ? 25.005 29.670 19.496 1.00 31.68 ? 180 ILE B CG2 1 ATOM 6174 C CD1 . ILE B 1 180 ? 22.750 27.719 20.356 1.00 40.09 ? 180 ILE B CD1 1 ATOM 6175 N N . ASN B 1 181 ? 25.525 32.770 19.768 1.00 21.41 ? 181 ASN B N 1 ATOM 6176 C CA . ASN B 1 181 ? 26.556 33.233 18.882 1.00 22.83 ? 181 ASN B CA 1 ATOM 6177 C C . ASN B 1 181 ? 27.505 32.119 18.443 1.00 24.11 ? 181 ASN B C 1 ATOM 6178 O O . ASN B 1 181 ? 28.393 31.674 19.209 1.00 24.37 ? 181 ASN B O 1 ATOM 6179 C CB . ASN B 1 181 ? 27.358 34.367 19.499 1.00 22.41 ? 181 ASN B CB 1 ATOM 6180 C CG . ASN B 1 181 ? 28.251 35.067 18.474 1.00 22.45 ? 181 ASN B CG 1 ATOM 6181 O OD1 . ASN B 1 181 ? 28.271 34.681 17.288 1.00 21.32 ? 181 ASN B OD1 1 ATOM 6182 N ND2 . ASN B 1 181 ? 28.973 36.084 18.912 1.00 20.52 ? 181 ASN B ND2 1 ATOM 6183 N N . ALA B 1 182 ? 27.372 31.716 17.203 1.00 20.78 ? 182 ALA B N 1 ATOM 6184 C CA . ALA B 1 182 ? 28.144 30.608 16.660 1.00 24.10 ? 182 ALA B CA 1 ATOM 6185 C C . ALA B 1 182 ? 29.574 30.959 16.234 1.00 25.45 ? 182 ALA B C 1 ATOM 6186 O O . ALA B 1 182 ? 30.297 30.093 15.796 1.00 25.52 ? 182 ALA B O 1 ATOM 6187 C CB . ALA B 1 182 ? 27.381 29.931 15.507 1.00 22.88 ? 182 ALA B CB 1 ATOM 6188 N N . VAL B 1 183 ? 29.998 32.212 16.355 1.00 23.85 ? 183 VAL B N 1 ATOM 6189 C CA . VAL B 1 183 ? 31.373 32.510 16.034 1.00 24.71 ? 183 VAL B CA 1 ATOM 6190 C C . VAL B 1 183 ? 31.977 33.214 17.248 1.00 22.85 ? 183 VAL B C 1 ATOM 6191 O O . VAL B 1 183 ? 31.277 33.517 18.205 1.00 21.98 ? 183 VAL B O 1 ATOM 6192 C CB . VAL B 1 183 ? 31.544 33.370 14.740 1.00 22.87 ? 183 VAL B CB 1 ATOM 6193 C CG1 . VAL B 1 183 ? 30.837 32.740 13.558 1.00 22.58 ? 183 VAL B CG1 1 ATOM 6194 C CG2 . VAL B 1 183 ? 31.077 34.782 14.953 1.00 22.76 ? 183 VAL B CG2 1 ATOM 6195 N N . THR B 1 184 ? 33.261 33.490 17.170 1.00 23.41 ? 184 THR B N 1 ATOM 6196 C CA . THR B 1 184 ? 34.021 33.992 18.313 1.00 23.65 ? 184 THR B CA 1 ATOM 6197 C C . THR B 1 184 ? 33.746 35.477 18.426 1.00 23.21 ? 184 THR B C 1 ATOM 6198 O O . THR B 1 184 ? 33.782 36.178 17.407 1.00 20.84 ? 184 THR B O 1 ATOM 6199 C CB . THR B 1 184 ? 35.541 33.710 18.147 1.00 26.17 ? 184 THR B CB 1 ATOM 6200 O OG1 . THR B 1 184 ? 36.035 34.389 16.983 1.00 27.02 ? 184 THR B OG1 1 ATOM 6201 C CG2 . THR B 1 184 ? 35.812 32.213 17.982 1.00 28.97 ? 184 THR B CG2 1 ATOM 6202 N N . SER B 1 185 ? 33.511 35.965 19.657 1.00 21.57 ? 185 SER B N 1 ATOM 6203 C CA . SER B 1 185 ? 33.171 37.358 19.892 1.00 20.25 ? 185 SER B CA 1 ATOM 6204 C C . SER B 1 185 ? 34.327 38.267 19.671 1.00 20.02 ? 185 SER B C 1 ATOM 6205 O O . SER B 1 185 ? 34.185 39.481 19.526 1.00 20.47 ? 185 SER B O 1 ATOM 6206 C CB . SER B 1 185 ? 32.624 37.562 21.290 1.00 21.81 ? 185 SER B CB 1 ATOM 6207 O OG . SER B 1 185 ? 31.470 36.803 21.538 1.00 21.44 ? 185 SER B OG 1 ATOM 6208 N N . PHE B 1 186 ? 35.510 37.665 19.691 1.00 23.11 ? 186 PHE B N 1 ATOM 6209 C CA . PHE B 1 186 ? 36.736 38.388 19.479 1.00 22.87 ? 186 PHE B CA 1 ATOM 6210 C C . PHE B 1 186 ? 36.834 38.704 17.989 1.00 20.10 ? 186 PHE B C 1 ATOM 6211 O O . PHE B 1 186 ? 36.328 37.960 17.135 1.00 25.06 ? 186 PHE B O 1 ATOM 6212 C CB . PHE B 1 186 ? 37.938 37.563 19.996 1.00 23.12 ? 186 PHE B CB 1 ATOM 6213 C CG . PHE B 1 186 ? 37.845 37.260 21.465 1.00 23.63 ? 186 PHE B CG 1 ATOM 6214 C CD1 . PHE B 1 186 ? 37.919 38.281 22.390 1.00 22.57 ? 186 PHE B CD1 1 ATOM 6215 C CD2 . PHE B 1 186 ? 37.547 35.992 21.900 1.00 23.98 ? 186 PHE B CD2 1 ATOM 6216 C CE1 . PHE B 1 186 ? 37.771 38.036 23.743 1.00 21.27 ? 186 PHE B CE1 1 ATOM 6217 C CE2 . PHE B 1 186 ? 37.403 35.729 23.253 1.00 22.10 ? 186 PHE B CE2 1 ATOM 6218 C CZ . PHE B 1 186 ? 37.533 36.757 24.168 1.00 22.06 ? 186 PHE B CZ 1 ATOM 6219 N N . LEU B 1 187 ? 37.453 39.829 17.726 1.00 20.30 ? 187 LEU B N 1 ATOM 6220 C CA . LEU B 1 187 ? 37.757 40.322 16.411 1.00 20.38 ? 187 LEU B CA 1 ATOM 6221 C C . LEU B 1 187 ? 39.068 39.693 16.029 1.00 21.69 ? 187 LEU B C 1 ATOM 6222 O O . LEU B 1 187 ? 40.145 40.272 16.277 1.00 22.44 ? 187 LEU B O 1 ATOM 6223 C CB . LEU B 1 187 ? 37.782 41.856 16.431 1.00 18.22 ? 187 LEU B CB 1 ATOM 6224 C CG . LEU B 1 187 ? 37.903 42.484 15.043 1.00 17.90 ? 187 LEU B CG 1 ATOM 6225 C CD1 . LEU B 1 187 ? 36.758 42.042 14.096 1.00 18.74 ? 187 LEU B CD1 1 ATOM 6226 C CD2 . LEU B 1 187 ? 37.918 43.981 15.082 1.00 19.39 ? 187 LEU B CD2 1 ATOM 6227 N N . ASP B 1 188 ? 38.975 38.461 15.527 1.00 24.02 ? 188 ASP B N 1 ATOM 6228 C CA . ASP B 1 188 ? 40.114 37.579 15.457 1.00 25.09 ? 188 ASP B CA 1 ATOM 6229 C C . ASP B 1 188 ? 40.244 36.820 14.138 1.00 24.87 ? 188 ASP B C 1 ATOM 6230 O O . ASP B 1 188 ? 40.842 35.734 14.085 1.00 27.60 ? 188 ASP B O 1 ATOM 6231 C CB . ASP B 1 188 ? 39.998 36.570 16.603 1.00 27.56 ? 188 ASP B CB 1 ATOM 6232 C CG . ASP B 1 188 ? 38.785 35.696 16.490 1.00 28.26 ? 188 ASP B CG 1 ATOM 6233 O OD1 . ASP B 1 188 ? 37.987 35.857 15.520 1.00 27.20 ? 188 ASP B OD1 1 ATOM 6234 O OD2 . ASP B 1 188 ? 38.646 34.769 17.337 1.00 30.28 ? 188 ASP B OD2 1 ATOM 6235 N N . ALA B 1 189 ? 39.653 37.357 13.079 1.00 23.91 ? 189 ALA B N 1 ATOM 6236 C CA . ALA B 1 189 ? 39.656 36.688 11.784 1.00 21.91 ? 189 ALA B CA 1 ATOM 6237 C C . ALA B 1 189 ? 39.026 35.311 11.802 1.00 22.54 ? 189 ALA B C 1 ATOM 6238 O O . ALA B 1 189 ? 39.376 34.447 10.989 1.00 19.88 ? 189 ALA B O 1 ATOM 6239 C CB . ALA B 1 189 ? 41.061 36.609 11.234 1.00 24.09 ? 189 ALA B CB 1 ATOM 6240 N N . SER B 1 190 ? 38.065 35.077 12.694 1.00 22.14 ? 190 SER B N 1 ATOM 6241 C CA . SER B 1 190 ? 37.371 33.784 12.665 1.00 22.58 ? 190 SER B CA 1 ATOM 6242 C C . SER B 1 190 ? 36.608 33.571 11.344 1.00 20.65 ? 190 SER B C 1 ATOM 6243 O O . SER B 1 190 ? 36.281 32.468 11.025 1.00 19.23 ? 190 SER B O 1 ATOM 6244 C CB . SER B 1 190 ? 36.380 33.644 13.822 1.00 22.62 ? 190 SER B CB 1 ATOM 6245 O OG . SER B 1 190 ? 35.612 34.836 13.993 1.00 26.43 ? 190 SER B OG 1 ATOM 6246 N N . LEU B 1 191 ? 36.292 34.621 10.618 1.00 20.29 ? 191 LEU B N 1 ATOM 6247 C CA . LEU B 1 191 ? 35.528 34.469 9.411 1.00 21.88 ? 191 LEU B CA 1 ATOM 6248 C C . LEU B 1 191 ? 36.436 33.838 8.318 1.00 26.18 ? 191 LEU B C 1 ATOM 6249 O O . LEU B 1 191 ? 35.922 33.274 7.317 1.00 26.83 ? 191 LEU B O 1 ATOM 6250 C CB . LEU B 1 191 ? 34.953 35.816 8.943 1.00 19.67 ? 191 LEU B CB 1 ATOM 6251 C CG . LEU B 1 191 ? 35.809 36.789 8.151 1.00 20.67 ? 191 LEU B CG 1 ATOM 6252 C CD1 . LEU B 1 191 ? 34.916 37.877 7.558 1.00 21.25 ? 191 LEU B CD1 1 ATOM 6253 C CD2 . LEU B 1 191 ? 36.925 37.401 8.977 1.00 22.10 ? 191 LEU B CD2 1 ATOM 6254 N N . VAL B 1 192 ? 37.761 33.884 8.550 1.00 24.18 ? 192 VAL B N 1 ATOM 6255 C CA . VAL B 1 192 ? 38.749 33.255 7.646 1.00 24.47 ? 192 VAL B CA 1 ATOM 6256 C C . VAL B 1 192 ? 39.113 31.848 8.107 1.00 26.28 ? 192 VAL B C 1 ATOM 6257 O O . VAL B 1 192 ? 39.173 30.907 7.285 1.00 26.29 ? 192 VAL B O 1 ATOM 6258 C CB . VAL B 1 192 ? 40.030 34.106 7.538 1.00 24.78 ? 192 VAL B CB 1 ATOM 6259 C CG1 . VAL B 1 192 ? 41.069 33.465 6.617 1.00 26.53 ? 192 VAL B CG1 1 ATOM 6260 C CG2 . VAL B 1 192 ? 39.701 35.491 7.031 1.00 22.64 ? 192 VAL B CG2 1 ATOM 6261 N N . TYR B 1 193 ? 39.305 31.674 9.411 1.00 29.50 ? 193 TYR B N 1 ATOM 6262 C CA . TYR B 1 193 ? 39.900 30.426 9.945 1.00 30.35 ? 193 TYR B CA 1 ATOM 6263 C C . TYR B 1 193 ? 38.901 29.462 10.421 1.00 30.76 ? 193 TYR B C 1 ATOM 6264 O O . TYR B 1 193 ? 39.198 28.247 10.490 1.00 28.93 ? 193 TYR B O 1 ATOM 6265 C CB . TYR B 1 193 ? 40.903 30.740 11.071 1.00 29.60 ? 193 TYR B CB 1 ATOM 6266 C CG . TYR B 1 193 ? 42.024 31.544 10.496 1.00 28.18 ? 193 TYR B CG 1 ATOM 6267 C CD1 . TYR B 1 193 ? 42.919 30.964 9.566 1.00 25.91 ? 193 TYR B CD1 1 ATOM 6268 C CD2 . TYR B 1 193 ? 42.167 32.884 10.794 1.00 26.01 ? 193 TYR B CD2 1 ATOM 6269 C CE1 . TYR B 1 193 ? 43.913 31.724 8.970 1.00 26.75 ? 193 TYR B CE1 1 ATOM 6270 C CE2 . TYR B 1 193 ? 43.159 33.640 10.177 1.00 26.38 ? 193 TYR B CE2 1 ATOM 6271 C CZ . TYR B 1 193 ? 44.048 33.050 9.290 1.00 25.14 ? 193 TYR B CZ 1 ATOM 6272 O OH . TYR B 1 193 ? 45.054 33.811 8.679 1.00 28.70 ? 193 TYR B OH 1 ATOM 6273 N N . GLY B 1 194 ? 37.697 29.965 10.733 1.00 26.00 ? 194 GLY B N 1 ATOM 6274 C CA . GLY B 1 194 ? 36.670 29.127 11.372 1.00 25.84 ? 194 GLY B CA 1 ATOM 6275 C C . GLY B 1 194 ? 36.651 29.388 12.862 1.00 26.26 ? 194 GLY B C 1 ATOM 6276 O O . GLY B 1 194 ? 37.594 29.955 13.397 1.00 28.73 ? 194 GLY B O 1 ATOM 6277 N N . SER B 1 195 ? 35.533 29.058 13.497 1.00 27.72 ? 195 SER B N 1 ATOM 6278 C CA . SER B 1 195 ? 35.336 29.196 14.929 1.00 29.03 ? 195 SER B CA 1 ATOM 6279 C C . SER B 1 195 ? 35.128 27.815 15.586 1.00 30.57 ? 195 SER B C 1 ATOM 6280 O O . SER B 1 195 ? 34.774 27.710 16.770 1.00 32.73 ? 195 SER B O 1 ATOM 6281 C CB . SER B 1 195 ? 34.086 30.026 15.187 1.00 27.24 ? 195 SER B CB 1 ATOM 6282 O OG . SER B 1 195 ? 34.225 31.338 14.724 1.00 24.91 ? 195 SER B OG 1 ATOM 6283 N N . GLU B 1 196 ? 35.304 26.782 14.783 1.00 37.23 ? 196 GLU B N 1 ATOM 6284 C CA . GLU B 1 196 ? 35.130 25.382 15.154 1.00 42.32 ? 196 GLU B CA 1 ATOM 6285 C C . GLU B 1 196 ? 36.359 24.596 14.627 1.00 45.42 ? 196 GLU B C 1 ATOM 6286 O O . GLU B 1 196 ? 36.803 24.786 13.482 1.00 41.51 ? 196 GLU B O 1 ATOM 6287 C CB . GLU B 1 196 ? 33.870 24.890 14.466 1.00 47.71 ? 196 GLU B CB 1 ATOM 6288 C CG . GLU B 1 196 ? 33.381 23.506 14.846 1.00 49.85 ? 196 GLU B CG 1 ATOM 6289 C CD . GLU B 1 196 ? 34.182 22.394 14.206 1.00 55.44 ? 196 GLU B CD 1 ATOM 6290 O OE1 . GLU B 1 196 ? 34.270 22.369 12.947 1.00 43.92 ? 196 GLU B OE1 1 ATOM 6291 O OE2 . GLU B 1 196 ? 34.708 21.543 14.969 1.00 54.98 ? 196 GLU B OE2 1 ATOM 6292 N N . PRO B 1 197 ? 36.909 23.691 15.442 1.00 49.84 ? 197 PRO B N 1 ATOM 6293 C CA . PRO B 1 197 ? 38.183 23.034 15.037 1.00 45.60 ? 197 PRO B CA 1 ATOM 6294 C C . PRO B 1 197 ? 38.237 22.105 13.801 1.00 40.33 ? 197 PRO B C 1 ATOM 6295 O O . PRO B 1 197 ? 39.158 22.205 13.001 1.00 37.30 ? 197 PRO B O 1 ATOM 6296 C CB . PRO B 1 197 ? 38.594 22.281 16.309 1.00 51.53 ? 197 PRO B CB 1 ATOM 6297 C CG . PRO B 1 197 ? 37.381 22.253 17.194 1.00 50.73 ? 197 PRO B CG 1 ATOM 6298 C CD . PRO B 1 197 ? 36.602 23.484 16.865 1.00 47.54 ? 197 PRO B CD 1 ATOM 6299 N N . SER B 1 198 ? 37.305 21.199 13.584 1.00 40.85 ? 198 SER B N 1 ATOM 6300 C CA . SER B 1 198 ? 37.413 20.387 12.346 1.00 42.65 ? 198 SER B CA 1 ATOM 6301 C C . SER B 1 198 ? 37.279 21.215 11.054 1.00 45.38 ? 198 SER B C 1 ATOM 6302 O O . SER B 1 198 ? 37.965 20.942 10.052 1.00 37.81 ? 198 SER B O 1 ATOM 6303 C CB . SER B 1 198 ? 36.410 19.232 12.301 1.00 45.10 ? 198 SER B CB 1 ATOM 6304 O OG . SER B 1 198 ? 35.102 19.723 12.368 1.00 52.45 ? 198 SER B OG 1 ATOM 6305 N N . LEU B 1 199 ? 36.413 22.239 11.076 1.00 49.01 ? 199 LEU B N 1 ATOM 6306 C CA . LEU B 1 199 ? 36.332 23.176 9.952 1.00 43.55 ? 199 LEU B CA 1 ATOM 6307 C C . LEU B 1 199 ? 37.672 23.858 9.779 1.00 40.41 ? 199 LEU B C 1 ATOM 6308 O O . LEU B 1 199 ? 38.212 23.885 8.658 1.00 39.04 ? 199 LEU B O 1 ATOM 6309 C CB . LEU B 1 199 ? 35.222 24.228 10.130 1.00 43.29 ? 199 LEU B CB 1 ATOM 6310 C CG . LEU B 1 199 ? 35.188 25.303 9.024 1.00 44.30 ? 199 LEU B CG 1 ATOM 6311 C CD1 . LEU B 1 199 ? 34.948 24.674 7.661 1.00 41.31 ? 199 LEU B CD1 1 ATOM 6312 C CD2 . LEU B 1 199 ? 34.143 26.370 9.331 1.00 47.81 ? 199 LEU B CD2 1 ATOM 6313 N N . ALA B 1 200 ? 38.231 24.399 10.867 1.00 42.31 ? 200 ALA B N 1 ATOM 6314 C CA . ALA B 1 200 ? 39.501 25.121 10.739 1.00 40.82 ? 200 ALA B CA 1 ATOM 6315 C C . ALA B 1 200 ? 40.565 24.231 10.110 1.00 43.22 ? 200 ALA B C 1 ATOM 6316 O O . ALA B 1 200 ? 41.370 24.694 9.289 1.00 43.15 ? 200 ALA B O 1 ATOM 6317 C CB . ALA B 1 200 ? 39.974 25.670 12.071 1.00 45.96 ? 200 ALA B CB 1 ATOM 6318 N N . SER B 1 201 ? 40.547 22.941 10.444 1.00 38.40 ? 201 SER B N 1 ATOM 6319 C CA . SER B 1 201 ? 41.556 22.039 9.853 1.00 42.21 ? 201 SER B CA 1 ATOM 6320 C C . SER B 1 201 ? 41.230 21.755 8.398 1.00 38.74 ? 201 SER B C 1 ATOM 6321 O O . SER B 1 201 ? 42.130 21.819 7.552 1.00 40.49 ? 201 SER B O 1 ATOM 6322 C CB . SER B 1 201 ? 41.850 20.765 10.679 1.00 42.37 ? 201 SER B CB 1 ATOM 6323 O OG . SER B 1 201 ? 40.760 20.327 11.453 1.00 45.76 ? 201 SER B OG 1 ATOM 6324 N N . ARG B 1 202 ? 39.952 21.481 8.093 1.00 39.89 ? 202 ARG B N 1 ATOM 6325 C CA . ARG B 1 202 ? 39.565 21.244 6.695 1.00 43.41 ? 202 ARG B CA 1 ATOM 6326 C C . ARG B 1 202 ? 39.985 22.399 5.773 1.00 43.06 ? 202 ARG B C 1 ATOM 6327 O O . ARG B 1 202 ? 40.264 22.171 4.597 1.00 33.11 ? 202 ARG B O 1 ATOM 6328 C CB . ARG B 1 202 ? 38.056 20.989 6.549 1.00 50.21 ? 202 ARG B CB 1 ATOM 6329 C CG . ARG B 1 202 ? 37.691 19.543 6.293 1.00 54.90 ? 202 ARG B CG 1 ATOM 6330 C CD . ARG B 1 202 ? 36.187 19.343 6.109 1.00 60.69 ? 202 ARG B CD 1 ATOM 6331 N NE . ARG B 1 202 ? 35.535 19.115 7.401 1.00 68.69 ? 202 ARG B NE 1 ATOM 6332 C CZ . ARG B 1 202 ? 34.722 19.968 8.029 1.00 73.16 ? 202 ARG B CZ 1 ATOM 6333 N NH1 . ARG B 1 202 ? 34.381 21.133 7.492 1.00 73.72 ? 202 ARG B NH1 1 ATOM 6334 N NH2 . ARG B 1 202 ? 34.223 19.642 9.218 1.00 82.12 ? 202 ARG B NH2 1 ATOM 6335 N N . LEU B 1 203 ? 40.065 23.617 6.323 1.00 41.96 ? 203 LEU B N 1 ATOM 6336 C CA . LEU B 1 203 ? 40.394 24.814 5.548 1.00 42.60 ? 203 LEU B CA 1 ATOM 6337 C C . LEU B 1 203 ? 41.887 24.993 5.318 1.00 44.27 ? 203 LEU B C 1 ATOM 6338 O O . LEU B 1 203 ? 42.312 25.738 4.394 1.00 40.63 ? 203 LEU B O 1 ATOM 6339 C CB . LEU B 1 203 ? 39.830 26.077 6.232 1.00 39.52 ? 203 LEU B CB 1 ATOM 6340 C CG . LEU B 1 203 ? 38.309 26.301 6.259 1.00 36.47 ? 203 LEU B CG 1 ATOM 6341 C CD1 . LEU B 1 203 ? 37.953 27.505 7.120 1.00 38.56 ? 203 LEU B CD1 1 ATOM 6342 C CD2 . LEU B 1 203 ? 37.769 26.531 4.855 1.00 33.25 ? 203 LEU B CD2 1 ATOM 6343 N N . ARG B 1 204 ? 42.684 24.306 6.131 1.00 46.65 ? 204 ARG B N 1 ATOM 6344 C CA . ARG B 1 204 ? 44.146 24.389 6.028 1.00 45.62 ? 204 ARG B CA 1 ATOM 6345 C C . ARG B 1 204 ? 44.699 23.515 4.921 1.00 41.66 ? 204 ARG B C 1 ATOM 6346 O O . ARG B 1 204 ? 44.063 22.518 4.528 1.00 35.25 ? 204 ARG B O 1 ATOM 6347 C CB . ARG B 1 204 ? 44.778 23.972 7.340 1.00 49.36 ? 204 ARG B CB 1 ATOM 6348 C CG . ARG B 1 204 ? 44.724 25.076 8.384 1.00 49.46 ? 204 ARG B CG 1 ATOM 6349 C CD . ARG B 1 204 ? 45.352 24.606 9.660 1.00 49.51 ? 204 ARG B CD 1 ATOM 6350 N NE . ARG B 1 204 ? 46.802 24.519 9.501 1.00 51.05 ? 204 ARG B NE 1 ATOM 6351 C CZ . ARG B 1 204 ? 47.644 24.055 10.432 1.00 53.97 ? 204 ARG B CZ 1 ATOM 6352 N NH1 . ARG B 1 204 ? 47.188 23.627 11.610 1.00 47.07 ? 204 ARG B NH1 1 ATOM 6353 N NH2 . ARG B 1 204 ? 48.954 24.023 10.178 1.00 53.18 ? 204 ARG B NH2 1 ATOM 6354 N N . ASN B 1 205 ? 45.850 23.920 4.375 1.00 44.37 ? 205 ASN B N 1 ATOM 6355 C CA . ASN B 1 205 ? 46.607 23.046 3.472 1.00 44.92 ? 205 ASN B CA 1 ATOM 6356 C C . ASN B 1 205 ? 47.600 22.267 4.351 1.00 46.94 ? 205 ASN B C 1 ATOM 6357 O O . ASN B 1 205 ? 48.664 22.757 4.690 1.00 39.26 ? 205 ASN B O 1 ATOM 6358 C CB . ASN B 1 205 ? 47.355 23.825 2.384 1.00 48.43 ? 205 ASN B CB 1 ATOM 6359 C CG . ASN B 1 205 ? 47.973 22.899 1.325 1.00 48.63 ? 205 ASN B CG 1 ATOM 6360 O OD1 . ASN B 1 205 ? 47.966 21.676 1.482 1.00 44.31 ? 205 ASN B OD1 1 ATOM 6361 N ND2 . ASN B 1 205 ? 48.494 23.492 0.239 1.00 52.01 ? 205 ASN B ND2 1 ATOM 6362 N N . LEU B 1 206 ? 47.203 21.075 4.764 1.00 47.83 ? 206 LEU B N 1 ATOM 6363 C CA . LEU B 1 206 ? 48.083 20.201 5.519 1.00 56.94 ? 206 LEU B CA 1 ATOM 6364 C C . LEU B 1 206 ? 49.069 19.427 4.571 1.00 59.99 ? 206 LEU B C 1 ATOM 6365 O O . LEU B 1 206 ? 50.116 18.948 4.994 1.00 59.57 ? 206 LEU B O 1 ATOM 6366 C CB . LEU B 1 206 ? 47.220 19.333 6.452 1.00 57.33 ? 206 LEU B CB 1 ATOM 6367 C CG . LEU B 1 206 ? 46.361 20.163 7.428 1.00 55.11 ? 206 LEU B CG 1 ATOM 6368 C CD1 . LEU B 1 206 ? 45.486 19.285 8.319 1.00 53.40 ? 206 LEU B CD1 1 ATOM 6369 C CD2 . LEU B 1 206 ? 47.234 21.083 8.282 1.00 56.84 ? 206 LEU B CD2 1 ATOM 6370 N N . SER B 1 207 ? 48.790 19.450 3.263 1.00 63.67 ? 207 SER B N 1 ATOM 6371 C CA . SER B 1 207 ? 49.585 18.737 2.249 1.00 61.24 ? 207 SER B CA 1 ATOM 6372 C C . SER B 1 207 ? 50.936 19.391 1.986 1.00 61.59 ? 207 SER B C 1 ATOM 6373 O O . SER B 1 207 ? 51.738 18.876 1.205 1.00 62.98 ? 207 SER B O 1 ATOM 6374 C CB . SER B 1 207 ? 48.812 18.599 0.935 1.00 58.50 ? 207 SER B CB 1 ATOM 6375 O OG . SER B 1 207 ? 47.792 17.642 1.099 1.00 61.06 ? 207 SER B OG 1 ATOM 6376 N N . SER B 1 208 ? 51.176 20.525 2.625 1.00 61.81 ? 208 SER B N 1 ATOM 6377 C CA . SER B 1 208 ? 52.484 21.125 2.631 1.00 66.60 ? 208 SER B CA 1 ATOM 6378 C C . SER B 1 208 ? 52.761 21.538 4.058 1.00 64.39 ? 208 SER B C 1 ATOM 6379 O O . SER B 1 208 ? 51.838 21.795 4.810 1.00 63.69 ? 208 SER B O 1 ATOM 6380 C CB . SER B 1 208 ? 52.505 22.321 1.692 1.00 66.60 ? 208 SER B CB 1 ATOM 6381 O OG . SER B 1 208 ? 51.525 23.260 2.088 1.00 73.20 ? 208 SER B OG 1 ATOM 6382 N N . PRO B 1 209 ? 54.032 21.533 4.465 1.00 66.77 ? 209 PRO B N 1 ATOM 6383 C CA . PRO B 1 209 ? 54.337 22.044 5.800 1.00 65.09 ? 209 PRO B CA 1 ATOM 6384 C C . PRO B 1 209 ? 54.610 23.535 5.731 1.00 55.34 ? 209 PRO B C 1 ATOM 6385 O O . PRO B 1 209 ? 55.452 24.030 6.447 1.00 48.20 ? 209 PRO B O 1 ATOM 6386 C CB . PRO B 1 209 ? 55.597 21.269 6.193 1.00 66.83 ? 209 PRO B CB 1 ATOM 6387 C CG . PRO B 1 209 ? 56.278 21.030 4.885 1.00 69.66 ? 209 PRO B CG 1 ATOM 6388 C CD . PRO B 1 209 ? 55.170 20.793 3.887 1.00 71.03 ? 209 PRO B CD 1 ATOM 6389 N N . LEU B 1 210 ? 53.868 24.250 4.892 1.00 50.05 ? 210 LEU B N 1 ATOM 6390 C CA . LEU B 1 210 ? 54.138 25.662 4.658 1.00 44.94 ? 210 LEU B CA 1 ATOM 6391 C C . LEU B 1 210 ? 53.114 26.579 5.346 1.00 40.50 ? 210 LEU B C 1 ATOM 6392 O O . LEU B 1 210 ? 53.115 27.778 5.102 1.00 40.84 ? 210 LEU B O 1 ATOM 6393 C CB . LEU B 1 210 ? 54.161 25.907 3.156 1.00 47.67 ? 210 LEU B CB 1 ATOM 6394 C CG . LEU B 1 210 ? 55.172 25.052 2.385 1.00 45.70 ? 210 LEU B CG 1 ATOM 6395 C CD1 . LEU B 1 210 ? 55.159 25.342 0.885 1.00 41.89 ? 210 LEU B CD1 1 ATOM 6396 C CD2 . LEU B 1 210 ? 56.550 25.303 2.955 1.00 48.39 ? 210 LEU B CD2 1 ATOM 6397 N N . GLY B 1 211 ? 52.279 26.008 6.220 1.00 42.28 ? 211 GLY B N 1 ATOM 6398 C CA . GLY B 1 211 ? 51.224 26.751 6.956 1.00 51.08 ? 211 GLY B CA 1 ATOM 6399 C C . GLY B 1 211 ? 50.195 27.496 6.089 1.00 47.80 ? 211 GLY B C 1 ATOM 6400 O O . GLY B 1 211 ? 49.618 28.503 6.518 1.00 54.22 ? 211 GLY B O 1 ATOM 6401 N N . LEU B 1 212 ? 49.974 27.019 4.873 1.00 43.68 ? 212 LEU B N 1 ATOM 6402 C CA . LEU B 1 212 ? 49.089 27.701 3.938 1.00 46.64 ? 212 LEU B CA 1 ATOM 6403 C C . LEU B 1 212 ? 47.654 27.330 4.240 1.00 37.97 ? 212 LEU B C 1 ATOM 6404 O O . LEU B 1 212 ? 47.386 26.294 4.848 1.00 37.50 ? 212 LEU B O 1 ATOM 6405 C CB . LEU B 1 212 ? 49.412 27.313 2.492 1.00 47.80 ? 212 LEU B CB 1 ATOM 6406 C CG . LEU B 1 212 ? 50.856 27.612 2.042 1.00 47.86 ? 212 LEU B CG 1 ATOM 6407 C CD1 . LEU B 1 212 ? 51.184 26.856 0.765 1.00 51.31 ? 212 LEU B CD1 1 ATOM 6408 C CD2 . LEU B 1 212 ? 51.109 29.099 1.878 1.00 48.15 ? 212 LEU B CD2 1 ATOM 6409 N N . MET B 1 213 ? 46.728 28.183 3.803 1.00 35.35 ? 213 MET B N 1 ATOM 6410 C CA . MET B 1 213 ? 45.310 27.793 3.765 1.00 32.33 ? 213 MET B CA 1 ATOM 6411 C C . MET B 1 213 ? 45.052 27.179 2.396 1.00 31.84 ? 213 MET B C 1 ATOM 6412 O O . MET B 1 213 ? 45.649 27.623 1.375 1.00 32.06 ? 213 MET B O 1 ATOM 6413 C CB . MET B 1 213 ? 44.409 29.018 3.933 1.00 31.44 ? 213 MET B CB 1 ATOM 6414 C CG . MET B 1 213 ? 44.475 29.662 5.298 1.00 31.89 ? 213 MET B CG 1 ATOM 6415 S SD . MET B 1 213 ? 43.704 28.616 6.513 1.00 32.92 ? 213 MET B SD 1 ATOM 6416 C CE . MET B 1 213 ? 41.957 28.997 6.265 1.00 36.23 ? 213 MET B CE 1 ATOM 6417 N N . ALA B 1 214 ? 44.191 26.170 2.361 1.00 30.37 ? 214 ALA B N 1 ATOM 6418 C CA . ALA B 1 214 ? 43.784 25.513 1.113 1.00 32.02 ? 214 ALA B CA 1 ATOM 6419 C C . ALA B 1 214 ? 43.178 26.495 0.141 1.00 37.06 ? 214 ALA B C 1 ATOM 6420 O O . ALA B 1 214 ? 42.472 27.445 0.566 1.00 33.56 ? 214 ALA B O 1 ATOM 6421 C CB . ALA B 1 214 ? 42.764 24.447 1.422 1.00 32.49 ? 214 ALA B CB 1 ATOM 6422 N N . VAL B 1 215 ? 43.479 26.298 -1.147 1.00 34.33 ? 215 VAL B N 1 ATOM 6423 C CA . VAL B 1 215 ? 42.927 27.121 -2.212 1.00 34.10 ? 215 VAL B CA 1 ATOM 6424 C C . VAL B 1 215 ? 42.265 26.253 -3.277 1.00 35.47 ? 215 VAL B C 1 ATOM 6425 O O . VAL B 1 215 ? 42.525 25.060 -3.375 1.00 35.55 ? 215 VAL B O 1 ATOM 6426 C CB . VAL B 1 215 ? 43.954 28.113 -2.822 1.00 38.31 ? 215 VAL B CB 1 ATOM 6427 C CG1 . VAL B 1 215 ? 44.543 28.992 -1.716 1.00 39.29 ? 215 VAL B CG1 1 ATOM 6428 C CG2 . VAL B 1 215 ? 45.090 27.409 -3.591 1.00 38.70 ? 215 VAL B CG2 1 ATOM 6429 N N . ASN B 1 216 ? 41.396 26.867 -4.062 1.00 31.89 ? 216 ASN B N 1 ATOM 6430 C CA . ASN B 1 216 ? 40.737 26.175 -5.145 1.00 33.83 ? 216 ASN B CA 1 ATOM 6431 C C . ASN B 1 216 ? 41.788 25.588 -6.116 1.00 34.62 ? 216 ASN B C 1 ATOM 6432 O O . ASN B 1 216 ? 42.778 26.261 -6.474 1.00 28.03 ? 216 ASN B O 1 ATOM 6433 C CB . ASN B 1 216 ? 39.846 27.128 -5.895 1.00 35.80 ? 216 ASN B CB 1 ATOM 6434 C CG . ASN B 1 216 ? 38.672 26.446 -6.521 1.00 37.02 ? 216 ASN B CG 1 ATOM 6435 O OD1 . ASN B 1 216 ? 38.815 25.791 -7.540 1.00 37.19 ? 216 ASN B OD1 1 ATOM 6436 N ND2 . ASN B 1 216 ? 37.470 26.655 -5.946 1.00 36.07 ? 216 ASN B ND2 1 ATOM 6437 N N . GLN B 1 217 ? 41.556 24.339 -6.508 1.00 33.89 ? 217 GLN B N 1 ATOM 6438 C CA . GLN B 1 217 ? 42.405 23.615 -7.463 1.00 39.40 ? 217 GLN B CA 1 ATOM 6439 C C . GLN B 1 217 ? 41.747 23.519 -8.848 1.00 46.75 ? 217 GLN B C 1 ATOM 6440 O O . GLN B 1 217 ? 42.306 22.909 -9.749 1.00 53.40 ? 217 GLN B O 1 ATOM 6441 C CB . GLN B 1 217 ? 42.695 22.197 -6.938 1.00 41.53 ? 217 GLN B CB 1 ATOM 6442 C CG . GLN B 1 217 ? 43.437 22.140 -5.607 1.00 41.47 ? 217 GLN B CG 1 ATOM 6443 C CD . GLN B 1 217 ? 44.773 22.878 -5.648 1.00 47.13 ? 217 GLN B CD 1 ATOM 6444 O OE1 . GLN B 1 217 ? 45.688 22.519 -6.409 1.00 49.22 ? 217 GLN B OE1 1 ATOM 6445 N NE2 . GLN B 1 217 ? 44.897 23.906 -4.839 1.00 49.82 ? 217 GLN B NE2 1 ATOM 6446 N N . GLU B 1 218 ? 40.547 24.082 -9.001 1.00 40.47 ? 218 GLU B N 1 ATOM 6447 C CA . GLU B 1 218 ? 39.810 24.010 -10.227 1.00 38.06 ? 218 GLU B CA 1 ATOM 6448 C C . GLU B 1 218 ? 39.844 25.332 -10.933 1.00 36.47 ? 218 GLU B C 1 ATOM 6449 O O . GLU B 1 218 ? 39.697 25.367 -12.144 1.00 35.24 ? 218 GLU B O 1 ATOM 6450 C CB . GLU B 1 218 ? 38.367 23.625 -9.939 1.00 45.88 ? 218 GLU B CB 1 ATOM 6451 C CG . GLU B 1 218 ? 38.237 22.252 -9.313 1.00 52.58 ? 218 GLU B CG 1 ATOM 6452 C CD . GLU B 1 218 ? 36.798 21.887 -9.010 1.00 55.30 ? 218 GLU B CD 1 ATOM 6453 O OE1 . GLU B 1 218 ? 35.915 22.275 -9.809 1.00 54.31 ? 218 GLU B OE1 1 ATOM 6454 O OE2 . GLU B 1 218 ? 36.559 21.205 -7.981 1.00 57.73 ? 218 GLU B OE2 1 ATOM 6455 N N . ALA B 1 219 ? 40.036 26.430 -10.187 1.00 31.78 ? 219 ALA B N 1 ATOM 6456 C CA . ALA B 1 219 ? 40.041 27.742 -10.784 1.00 34.21 ? 219 ALA B CA 1 ATOM 6457 C C . ALA B 1 219 ? 41.012 28.686 -10.108 1.00 28.54 ? 219 ALA B C 1 ATOM 6458 O O . ALA B 1 219 ? 41.252 28.579 -8.947 1.00 29.80 ? 219 ALA B O 1 ATOM 6459 C CB . ALA B 1 219 ? 38.642 28.339 -10.737 1.00 35.72 ? 219 ALA B CB 1 ATOM 6460 N N . TRP B 1 220 ? 41.482 29.665 -10.879 1.00 30.93 ? 220 TRP B N 1 ATOM 6461 C CA . TRP B 1 220 ? 42.478 30.625 -10.494 1.00 30.11 ? 220 TRP B CA 1 ATOM 6462 C C . TRP B 1 220 ? 42.107 31.928 -11.199 1.00 29.98 ? 220 TRP B C 1 ATOM 6463 O O . TRP B 1 220 ? 41.413 31.882 -12.188 1.00 29.64 ? 220 TRP B O 1 ATOM 6464 C CB . TRP B 1 220 ? 43.846 30.122 -11.001 1.00 32.79 ? 220 TRP B CB 1 ATOM 6465 C CG . TRP B 1 220 ? 44.296 28.849 -10.309 1.00 36.61 ? 220 TRP B CG 1 ATOM 6466 C CD1 . TRP B 1 220 ? 43.997 27.542 -10.664 1.00 36.40 ? 220 TRP B CD1 1 ATOM 6467 C CD2 . TRP B 1 220 ? 45.080 28.771 -9.118 1.00 38.08 ? 220 TRP B CD2 1 ATOM 6468 N NE1 . TRP B 1 220 ? 44.549 26.678 -9.751 1.00 37.94 ? 220 TRP B NE1 1 ATOM 6469 C CE2 . TRP B 1 220 ? 45.232 27.403 -8.807 1.00 39.85 ? 220 TRP B CE2 1 ATOM 6470 C CE3 . TRP B 1 220 ? 45.686 29.743 -8.276 1.00 43.97 ? 220 TRP B CE3 1 ATOM 6471 C CZ2 . TRP B 1 220 ? 45.959 26.971 -7.684 1.00 47.75 ? 220 TRP B CZ2 1 ATOM 6472 C CZ3 . TRP B 1 220 ? 46.409 29.315 -7.158 1.00 45.29 ? 220 TRP B CZ3 1 ATOM 6473 C CH2 . TRP B 1 220 ? 46.542 27.937 -6.871 1.00 51.14 ? 220 TRP B CH2 1 ATOM 6474 N N . ASP B 1 221 ? 42.602 33.065 -10.725 1.00 30.75 ? 221 ASP B N 1 ATOM 6475 C CA . ASP B 1 221 ? 42.183 34.401 -11.161 1.00 30.61 ? 221 ASP B CA 1 ATOM 6476 C C . ASP B 1 221 ? 43.460 35.079 -11.692 1.00 34.13 ? 221 ASP B C 1 ATOM 6477 O O . ASP B 1 221 ? 44.165 35.793 -10.957 1.00 27.30 ? 221 ASP B O 1 ATOM 6478 C CB . ASP B 1 221 ? 41.611 35.148 -9.931 1.00 28.77 ? 221 ASP B CB 1 ATOM 6479 C CG . ASP B 1 221 ? 41.155 36.579 -10.214 1.00 31.17 ? 221 ASP B CG 1 ATOM 6480 O OD1 . ASP B 1 221 ? 41.167 37.065 -11.370 1.00 31.54 ? 221 ASP B OD1 1 ATOM 6481 O OD2 . ASP B 1 221 ? 40.725 37.242 -9.230 1.00 30.95 ? 221 ASP B OD2 1 ATOM 6482 N N . HIS B 1 222 ? 43.802 34.809 -12.948 1.00 35.28 ? 222 HIS B N 1 ATOM 6483 C CA . HIS B 1 222 ? 45.071 35.316 -13.493 1.00 34.05 ? 222 HIS B CA 1 ATOM 6484 C C . HIS B 1 222 ? 46.193 34.834 -12.602 1.00 31.95 ? 222 HIS B C 1 ATOM 6485 O O . HIS B 1 222 ? 47.090 35.606 -12.199 1.00 37.54 ? 222 HIS B O 1 ATOM 6486 C CB . HIS B 1 222 ? 45.072 36.833 -13.623 1.00 34.06 ? 222 HIS B CB 1 ATOM 6487 C CG . HIS B 1 222 ? 43.908 37.361 -14.378 1.00 36.85 ? 222 HIS B CG 1 ATOM 6488 N ND1 . HIS B 1 222 ? 42.889 38.077 -13.788 1.00 42.33 ? 222 HIS B ND1 1 ATOM 6489 C CD2 . HIS B 1 222 ? 43.594 37.280 -15.679 1.00 41.49 ? 222 HIS B CD2 1 ATOM 6490 C CE1 . HIS B 1 222 ? 42.015 38.438 -14.694 1.00 43.18 ? 222 HIS B CE1 1 ATOM 6491 N NE2 . HIS B 1 222 ? 42.418 37.965 -15.857 1.00 42.48 ? 222 HIS B NE2 1 ATOM 6492 N N . GLY B 1 223 ? 46.155 33.543 -12.289 1.00 33.26 ? 223 GLY B N 1 ATOM 6493 C CA . GLY B 1 223 ? 47.123 32.970 -11.393 1.00 34.76 ? 223 GLY B CA 1 ATOM 6494 C C . GLY B 1 223 ? 46.918 33.131 -9.887 1.00 37.76 ? 223 GLY B C 1 ATOM 6495 O O . GLY B 1 223 ? 47.612 32.474 -9.123 1.00 39.34 ? 223 GLY B O 1 ATOM 6496 N N . LEU B 1 224 ? 46.027 34.028 -9.440 1.00 37.41 ? 224 LEU B N 1 ATOM 6497 C CA . LEU B 1 224 ? 45.836 34.267 -7.987 1.00 33.35 ? 224 LEU B CA 1 ATOM 6498 C C . LEU B 1 224 ? 44.710 33.379 -7.451 1.00 32.39 ? 224 LEU B C 1 ATOM 6499 O O . LEU B 1 224 ? 43.842 32.935 -8.205 1.00 34.57 ? 224 LEU B O 1 ATOM 6500 C CB . LEU B 1 224 ? 45.579 35.750 -7.684 1.00 33.93 ? 224 LEU B CB 1 ATOM 6501 C CG . LEU B 1 224 ? 46.575 36.786 -8.237 1.00 36.07 ? 224 LEU B CG 1 ATOM 6502 C CD1 . LEU B 1 224 ? 46.216 38.224 -7.939 1.00 35.08 ? 224 LEU B CD1 1 ATOM 6503 C CD2 . LEU B 1 224 ? 47.960 36.481 -7.675 1.00 38.71 ? 224 LEU B CD2 1 ATOM 6504 N N . ALA B 1 225 ? 44.775 33.070 -6.158 1.00 28.00 ? 225 ALA B N 1 ATOM 6505 C CA . ALA B 1 225 ? 43.944 32.008 -5.573 1.00 28.23 ? 225 ALA B CA 1 ATOM 6506 C C . ALA B 1 225 ? 42.481 32.370 -5.339 1.00 27.58 ? 225 ALA B C 1 ATOM 6507 O O . ALA B 1 225 ? 42.128 33.532 -5.188 1.00 25.52 ? 225 ALA B O 1 ATOM 6508 C CB . ALA B 1 225 ? 44.536 31.518 -4.271 1.00 29.36 ? 225 ALA B CB 1 ATOM 6509 N N . TYR B 1 226 ? 41.650 31.335 -5.333 1.00 28.73 ? 226 TYR B N 1 ATOM 6510 C CA . TYR B 1 226 ? 40.257 31.437 -4.856 1.00 26.66 ? 226 TYR B CA 1 ATOM 6511 C C . TYR B 1 226 ? 40.102 30.522 -3.708 1.00 25.46 ? 226 TYR B C 1 ATOM 6512 O O . TYR B 1 226 ? 40.878 29.582 -3.560 1.00 27.74 ? 226 TYR B O 1 ATOM 6513 C CB . TYR B 1 226 ? 39.250 30.961 -5.916 1.00 24.47 ? 226 TYR B CB 1 ATOM 6514 C CG . TYR B 1 226 ? 39.043 31.904 -7.067 1.00 27.17 ? 226 TYR B CG 1 ATOM 6515 C CD1 . TYR B 1 226 ? 38.663 33.191 -6.857 1.00 25.22 ? 226 TYR B CD1 1 ATOM 6516 C CD2 . TYR B 1 226 ? 39.223 31.479 -8.393 1.00 26.29 ? 226 TYR B CD2 1 ATOM 6517 C CE1 . TYR B 1 226 ? 38.492 34.069 -7.918 1.00 26.35 ? 226 TYR B CE1 1 ATOM 6518 C CE2 . TYR B 1 226 ? 39.034 32.356 -9.453 1.00 27.40 ? 226 TYR B CE2 1 ATOM 6519 C CZ . TYR B 1 226 ? 38.642 33.644 -9.204 1.00 25.68 ? 226 TYR B CZ 1 ATOM 6520 O OH . TYR B 1 226 ? 38.404 34.527 -10.250 1.00 30.11 ? 226 TYR B OH 1 ATOM 6521 N N . PRO B 1 227 ? 39.085 30.765 -2.864 1.00 26.05 ? 227 PRO B N 1 ATOM 6522 C CA . PRO B 1 227 ? 38.817 29.816 -1.852 1.00 25.62 ? 227 PRO B CA 1 ATOM 6523 C C . PRO B 1 227 ? 38.441 28.497 -2.433 1.00 25.42 ? 227 PRO B C 1 ATOM 6524 O O . PRO B 1 227 ? 37.962 28.419 -3.560 1.00 29.46 ? 227 PRO B O 1 ATOM 6525 C CB . PRO B 1 227 ? 37.600 30.401 -1.099 1.00 24.87 ? 227 PRO B CB 1 ATOM 6526 C CG . PRO B 1 227 ? 37.694 31.858 -1.338 1.00 26.09 ? 227 PRO B CG 1 ATOM 6527 C CD . PRO B 1 227 ? 38.189 31.951 -2.765 1.00 29.04 ? 227 PRO B CD 1 ATOM 6528 N N . PRO B 1 228 ? 38.565 27.432 -1.642 1.00 27.90 ? 228 PRO B N 1 ATOM 6529 C CA . PRO B 1 228 ? 38.056 26.167 -2.175 1.00 28.41 ? 228 PRO B CA 1 ATOM 6530 C C . PRO B 1 228 ? 36.529 26.215 -2.352 1.00 32.41 ? 228 PRO B C 1 ATOM 6531 O O . PRO B 1 228 ? 35.864 27.116 -1.775 1.00 24.81 ? 228 PRO B O 1 ATOM 6532 C CB . PRO B 1 228 ? 38.434 25.142 -1.116 1.00 30.03 ? 228 PRO B CB 1 ATOM 6533 C CG . PRO B 1 228 ? 39.454 25.820 -0.246 1.00 30.13 ? 228 PRO B CG 1 ATOM 6534 C CD . PRO B 1 228 ? 39.171 27.279 -0.316 1.00 28.88 ? 228 PRO B CD 1 ATOM 6535 N N . PHE B 1 229 ? 35.992 25.274 -3.148 1.00 28.91 ? 229 PHE B N 1 ATOM 6536 C CA . PHE B 1 229 ? 34.537 25.105 -3.245 1.00 30.25 ? 229 PHE B CA 1 ATOM 6537 C C . PHE B 1 229 ? 34.006 24.322 -2.080 1.00 29.90 ? 229 PHE B C 1 ATOM 6538 O O . PHE B 1 229 ? 34.622 23.387 -1.601 1.00 33.24 ? 229 PHE B O 1 ATOM 6539 C CB . PHE B 1 229 ? 34.096 24.431 -4.556 1.00 29.30 ? 229 PHE B CB 1 ATOM 6540 C CG . PHE B 1 229 ? 34.243 25.306 -5.784 1.00 32.48 ? 229 PHE B CG 1 ATOM 6541 C CD1 . PHE B 1 229 ? 33.940 26.680 -5.747 1.00 30.72 ? 229 PHE B CD1 1 ATOM 6542 C CD2 . PHE B 1 229 ? 34.710 24.766 -6.982 1.00 30.55 ? 229 PHE B CD2 1 ATOM 6543 C CE1 . PHE B 1 229 ? 34.106 27.471 -6.867 1.00 28.90 ? 229 PHE B CE1 1 ATOM 6544 C CE2 . PHE B 1 229 ? 34.840 25.544 -8.111 1.00 29.87 ? 229 PHE B CE2 1 ATOM 6545 C CZ . PHE B 1 229 ? 34.532 26.911 -8.059 1.00 29.50 ? 229 PHE B CZ 1 ATOM 6546 N N . ASN B 1 230 ? 32.840 24.705 -1.605 1.00 34.69 ? 230 ASN B N 1 ATOM 6547 C CA . ASN B 1 230 ? 32.070 23.826 -0.747 1.00 33.57 ? 230 ASN B CA 1 ATOM 6548 C C . ASN B 1 230 ? 31.255 22.883 -1.606 1.00 36.01 ? 230 ASN B C 1 ATOM 6549 O O . ASN B 1 230 ? 30.597 23.326 -2.545 1.00 38.92 ? 230 ASN B O 1 ATOM 6550 C CB . ASN B 1 230 ? 31.149 24.668 0.066 1.00 38.50 ? 230 ASN B CB 1 ATOM 6551 C CG . ASN B 1 230 ? 30.246 23.871 0.956 1.00 39.76 ? 230 ASN B CG 1 ATOM 6552 O OD1 . ASN B 1 230 ? 30.340 22.640 1.076 1.00 53.50 ? 230 ASN B OD1 1 ATOM 6553 N ND2 . ASN B 1 230 ? 29.380 24.576 1.619 1.00 37.30 ? 230 ASN B ND2 1 ATOM 6554 N N . ASN B 1 231 ? 31.249 21.598 -1.298 1.00 43.49 ? 231 ASN B N 1 ATOM 6555 C CA . ASN B 1 231 ? 30.537 20.634 -2.164 1.00 48.76 ? 231 ASN B CA 1 ATOM 6556 C C . ASN B 1 231 ? 29.346 19.922 -1.549 1.00 50.24 ? 231 ASN B C 1 ATOM 6557 O O . ASN B 1 231 ? 28.846 18.937 -2.097 1.00 53.30 ? 231 ASN B O 1 ATOM 6558 C CB . ASN B 1 231 ? 31.531 19.655 -2.789 1.00 50.67 ? 231 ASN B CB 1 ATOM 6559 C CG . ASN B 1 231 ? 32.274 20.284 -3.970 1.00 53.99 ? 231 ASN B CG 1 ATOM 6560 O OD1 . ASN B 1 231 ? 31.660 20.746 -4.964 1.00 54.55 ? 231 ASN B OD1 1 ATOM 6561 N ND2 . ASN B 1 231 ? 33.583 20.345 -3.860 1.00 49.86 ? 231 ASN B ND2 1 ATOM 6562 N N . VAL B 1 232 ? 28.894 20.430 -0.416 1.00 52.10 ? 232 VAL B N 1 ATOM 6563 C CA . VAL B 1 232 ? 27.600 20.068 0.132 1.00 51.57 ? 232 VAL B CA 1 ATOM 6564 C C . VAL B 1 232 ? 26.526 20.325 -0.910 1.00 55.81 ? 232 VAL B C 1 ATOM 6565 O O . VAL B 1 232 ? 26.501 21.404 -1.523 1.00 55.33 ? 232 VAL B O 1 ATOM 6566 C CB . VAL B 1 232 ? 27.240 20.937 1.357 1.00 60.51 ? 232 VAL B CB 1 ATOM 6567 C CG1 . VAL B 1 232 ? 25.795 20.696 1.824 1.00 56.59 ? 232 VAL B CG1 1 ATOM 6568 C CG2 . VAL B 1 232 ? 28.244 20.702 2.499 1.00 63.27 ? 232 VAL B CG2 1 ATOM 6569 N N . LYS B 1 233 ? 25.628 19.350 -1.085 1.00 53.45 ? 233 LYS B N 1 ATOM 6570 C CA . LYS B 1 233 ? 24.499 19.505 -1.995 1.00 51.38 ? 233 LYS B CA 1 ATOM 6571 C C . LYS B 1 233 ? 23.183 19.530 -1.190 1.00 44.94 ? 233 LYS B C 1 ATOM 6572 O O . LYS B 1 233 ? 23.094 18.956 -0.119 1.00 45.58 ? 233 LYS B O 1 ATOM 6573 C CB . LYS B 1 233 ? 24.564 18.487 -3.141 1.00 50.62 ? 233 LYS B CB 1 ATOM 6574 C CG . LYS B 1 233 ? 25.219 19.091 -4.388 1.00 56.20 ? 233 LYS B CG 1 ATOM 6575 C CD . LYS B 1 233 ? 24.564 18.607 -5.691 1.00 64.47 ? 233 LYS B CD 1 ATOM 6576 C CE . LYS B 1 233 ? 24.604 19.634 -6.836 1.00 66.70 ? 233 LYS B CE 1 ATOM 6577 N NZ . LYS B 1 233 ? 25.654 19.435 -7.882 1.00 63.72 ? 233 LYS B NZ 1 ATOM 6578 N N . PRO B 1 234 ? 22.194 20.322 -1.628 1.00 40.53 ? 234 PRO B N 1 ATOM 6579 C CA . PRO B 1 234 ? 22.201 21.256 -2.760 1.00 39.63 ? 234 PRO B CA 1 ATOM 6580 C C . PRO B 1 234 ? 22.852 22.581 -2.420 1.00 30.68 ? 234 PRO B C 1 ATOM 6581 O O . PRO B 1 234 ? 22.879 23.001 -1.279 1.00 34.41 ? 234 PRO B O 1 ATOM 6582 C CB . PRO B 1 234 ? 20.718 21.417 -3.085 1.00 37.44 ? 234 PRO B CB 1 ATOM 6583 C CG . PRO B 1 234 ? 20.007 21.166 -1.795 1.00 38.83 ? 234 PRO B CG 1 ATOM 6584 C CD . PRO B 1 234 ? 20.935 20.421 -0.866 1.00 38.55 ? 234 PRO B CD 1 ATOM 6585 N N . SER B 1 235 ? 23.386 23.232 -3.433 1.00 31.57 ? 235 SER B N 1 ATOM 6586 C CA . SER B 1 235 ? 24.141 24.462 -3.270 1.00 27.94 ? 235 SER B CA 1 ATOM 6587 C C . SER B 1 235 ? 23.258 25.601 -3.778 1.00 29.00 ? 235 SER B C 1 ATOM 6588 O O . SER B 1 235 ? 22.783 25.546 -4.944 1.00 28.36 ? 235 SER B O 1 ATOM 6589 C CB . SER B 1 235 ? 25.419 24.375 -4.072 1.00 27.54 ? 235 SER B CB 1 ATOM 6590 O OG . SER B 1 235 ? 26.044 25.636 -4.303 1.00 31.54 ? 235 SER B OG 1 ATOM 6591 N N . PRO B 1 236 ? 23.057 26.650 -2.949 1.00 26.06 ? 236 PRO B N 1 ATOM 6592 C CA . PRO B 1 236 ? 22.327 27.791 -3.511 1.00 25.19 ? 236 PRO B CA 1 ATOM 6593 C C . PRO B 1 236 ? 23.090 28.494 -4.618 1.00 22.67 ? 236 PRO B C 1 ATOM 6594 O O . PRO B 1 236 ? 22.462 29.075 -5.509 1.00 22.02 ? 236 PRO B O 1 ATOM 6595 C CB . PRO B 1 236 ? 22.154 28.705 -2.328 1.00 25.69 ? 236 PRO B CB 1 ATOM 6596 C CG . PRO B 1 236 ? 23.333 28.415 -1.479 1.00 28.67 ? 236 PRO B CG 1 ATOM 6597 C CD . PRO B 1 236 ? 23.491 26.913 -1.582 1.00 26.67 ? 236 PRO B CD 1 ATOM 6598 N N . CYS B 1 237 ? 24.422 28.474 -4.572 1.00 22.67 ? 237 CYS B N 1 ATOM 6599 C CA . CYS B 1 237 ? 25.222 29.195 -5.548 1.00 23.81 ? 237 CYS B CA 1 ATOM 6600 C C . CYS B 1 237 ? 25.129 28.508 -6.918 1.00 23.17 ? 237 CYS B C 1 ATOM 6601 O O . CYS B 1 237 ? 25.260 29.149 -7.968 1.00 25.90 ? 237 CYS B O 1 ATOM 6602 C CB . CYS B 1 237 ? 26.692 29.326 -5.106 1.00 22.84 ? 237 CYS B CB 1 ATOM 6603 S SG . CYS B 1 237 ? 26.978 30.219 -3.563 1.00 21.43 ? 237 CYS B SG 1 ATOM 6604 N N . GLU B 1 238 ? 24.904 27.205 -6.904 1.00 24.55 ? 238 GLU B N 1 ATOM 6605 C CA . GLU B 1 238 ? 24.630 26.417 -8.120 1.00 24.73 ? 238 GLU B CA 1 ATOM 6606 C C . GLU B 1 238 ? 23.223 26.651 -8.595 1.00 22.31 ? 238 GLU B C 1 ATOM 6607 O O . GLU B 1 238 ? 22.992 26.841 -9.761 1.00 20.49 ? 238 GLU B O 1 ATOM 6608 C CB . GLU B 1 238 ? 24.871 24.925 -7.861 1.00 27.93 ? 238 GLU B CB 1 ATOM 6609 C CG . GLU B 1 238 ? 26.343 24.559 -7.723 1.00 27.98 ? 238 GLU B CG 1 ATOM 6610 C CD . GLU B 1 238 ? 26.611 23.050 -7.631 1.00 33.66 ? 238 GLU B CD 1 ATOM 6611 O OE1 . GLU B 1 238 ? 27.743 22.644 -7.385 1.00 36.93 ? 238 GLU B OE1 1 ATOM 6612 O OE2 . GLU B 1 238 ? 25.690 22.257 -7.754 1.00 39.32 ? 238 GLU B OE2 1 ATOM 6613 N N . PHE B 1 239 ? 22.294 26.681 -7.650 1.00 23.20 ? 239 PHE B N 1 ATOM 6614 C CA . PHE B 1 239 ? 20.928 26.866 -7.959 1.00 24.69 ? 239 PHE B CA 1 ATOM 6615 C C . PHE B 1 239 ? 20.692 28.140 -8.790 1.00 26.07 ? 239 PHE B C 1 ATOM 6616 O O . PHE B 1 239 ? 19.883 28.142 -9.672 1.00 22.03 ? 239 PHE B O 1 ATOM 6617 C CB . PHE B 1 239 ? 20.078 26.861 -6.676 1.00 26.32 ? 239 PHE B CB 1 ATOM 6618 C CG . PHE B 1 239 ? 18.596 26.963 -6.931 1.00 29.09 ? 239 PHE B CG 1 ATOM 6619 C CD1 . PHE B 1 239 ? 17.820 25.811 -7.173 1.00 28.96 ? 239 PHE B CD1 1 ATOM 6620 C CD2 . PHE B 1 239 ? 17.971 28.225 -6.957 1.00 29.73 ? 239 PHE B CD2 1 ATOM 6621 C CE1 . PHE B 1 239 ? 16.462 25.924 -7.433 1.00 31.16 ? 239 PHE B CE1 1 ATOM 6622 C CE2 . PHE B 1 239 ? 16.625 28.352 -7.217 1.00 28.95 ? 239 PHE B CE2 1 ATOM 6623 C CZ . PHE B 1 239 ? 15.853 27.207 -7.448 1.00 32.84 ? 239 PHE B CZ 1 ATOM 6624 N N . ILE B 1 240 ? 21.387 29.227 -8.498 1.00 22.09 ? 240 ILE B N 1 ATOM 6625 C CA . ILE B 1 240 ? 21.082 30.447 -9.206 1.00 21.26 ? 240 ILE B CA 1 ATOM 6626 C C . ILE B 1 240 ? 21.555 30.448 -10.664 1.00 23.26 ? 240 ILE B C 1 ATOM 6627 O O . ILE B 1 240 ? 21.176 31.329 -11.436 1.00 19.03 ? 240 ILE B O 1 ATOM 6628 C CB . ILE B 1 240 ? 21.539 31.681 -8.440 1.00 21.84 ? 240 ILE B CB 1 ATOM 6629 C CG1 . ILE B 1 240 ? 23.019 31.628 -8.091 1.00 22.59 ? 240 ILE B CG1 1 ATOM 6630 C CG2 . ILE B 1 240 ? 20.731 31.804 -7.154 1.00 22.35 ? 240 ILE B CG2 1 ATOM 6631 C CD1 . ILE B 1 240 ? 23.762 32.744 -8.716 1.00 25.32 ? 240 ILE B CD1 1 ATOM 6632 N N . ASN B 1 241 ? 22.312 29.425 -11.072 1.00 22.41 ? 241 ASN B N 1 ATOM 6633 C CA . ASN B 1 241 ? 22.641 29.260 -12.467 1.00 22.41 ? 241 ASN B CA 1 ATOM 6634 C C . ASN B 1 241 ? 23.149 27.850 -12.636 1.00 24.30 ? 241 ASN B C 1 ATOM 6635 O O . ASN B 1 241 ? 24.346 27.579 -12.473 1.00 23.43 ? 241 ASN B O 1 ATOM 6636 C CB . ASN B 1 241 ? 23.676 30.278 -12.980 1.00 24.27 ? 241 ASN B CB 1 ATOM 6637 C CG . ASN B 1 241 ? 23.958 30.107 -14.478 1.00 26.72 ? 241 ASN B CG 1 ATOM 6638 O OD1 . ASN B 1 241 ? 23.776 29.038 -15.024 1.00 28.44 ? 241 ASN B OD1 1 ATOM 6639 N ND2 . ASN B 1 241 ? 24.395 31.163 -15.136 1.00 29.35 ? 241 ASN B ND2 1 ATOM 6640 N N . THR B 1 242 ? 22.219 26.953 -12.961 1.00 26.49 ? 242 THR B N 1 ATOM 6641 C CA . THR B 1 242 ? 22.511 25.532 -13.061 1.00 26.28 ? 242 THR B CA 1 ATOM 6642 C C . THR B 1 242 ? 23.397 25.179 -14.264 1.00 27.36 ? 242 THR B C 1 ATOM 6643 O O . THR B 1 242 ? 24.125 24.196 -14.229 1.00 29.25 ? 242 THR B O 1 ATOM 6644 C CB . THR B 1 242 ? 21.201 24.701 -13.012 1.00 25.19 ? 242 THR B CB 1 ATOM 6645 O OG1 . THR B 1 242 ? 20.280 25.203 -13.959 1.00 28.16 ? 242 THR B OG1 1 ATOM 6646 C CG2 . THR B 1 242 ? 20.524 24.744 -11.620 1.00 25.81 ? 242 THR B CG2 1 ATOM 6647 N N . THR B 1 243 ? 23.383 25.996 -15.300 1.00 27.30 ? 243 THR B N 1 ATOM 6648 C CA . THR B 1 243 ? 24.275 25.828 -16.421 1.00 29.26 ? 243 THR B CA 1 ATOM 6649 C C . THR B 1 243 ? 25.733 26.083 -16.037 1.00 32.11 ? 243 THR B C 1 ATOM 6650 O O . THR B 1 243 ? 26.622 25.300 -16.386 1.00 33.39 ? 243 THR B O 1 ATOM 6651 C CB . THR B 1 243 ? 23.901 26.791 -17.540 1.00 33.46 ? 243 THR B CB 1 ATOM 6652 O OG1 . THR B 1 243 ? 22.544 26.545 -17.925 1.00 37.89 ? 243 THR B OG1 1 ATOM 6653 C CG2 . THR B 1 243 ? 24.804 26.622 -18.714 1.00 32.74 ? 243 THR B CG2 1 ATOM 6654 N N . ALA B 1 244 ? 25.989 27.158 -15.304 1.00 31.58 ? 244 ALA B N 1 ATOM 6655 C CA . ALA B 1 244 ? 27.321 27.364 -14.733 1.00 27.60 ? 244 ALA B CA 1 ATOM 6656 C C . ALA B 1 244 ? 27.669 26.386 -13.605 1.00 27.58 ? 244 ALA B C 1 ATOM 6657 O O . ALA B 1 244 ? 28.809 25.929 -13.518 1.00 27.88 ? 244 ALA B O 1 ATOM 6658 C CB . ALA B 1 244 ? 27.532 28.796 -14.331 1.00 25.87 ? 244 ALA B CB 1 ATOM 6659 N N . HIS B 1 245 ? 26.700 26.048 -12.770 1.00 28.85 ? 245 HIS B N 1 ATOM 6660 C CA . HIS B 1 245 ? 26.847 25.204 -11.605 1.00 31.53 ? 245 HIS B CA 1 ATOM 6661 C C . HIS B 1 245 ? 28.168 25.414 -10.867 1.00 31.64 ? 245 HIS B C 1 ATOM 6662 O O . HIS B 1 245 ? 28.879 24.479 -10.565 1.00 30.58 ? 245 HIS B O 1 ATOM 6663 C CB . HIS B 1 245 ? 26.545 23.684 -11.909 1.00 35.96 ? 245 HIS B CB 1 ATOM 6664 C CG . HIS B 1 245 ? 27.420 23.094 -12.967 1.00 40.37 ? 245 HIS B CG 1 ATOM 6665 N ND1 . HIS B 1 245 ? 28.660 22.557 -12.686 1.00 42.02 ? 245 HIS B ND1 1 ATOM 6666 C CD2 . HIS B 1 245 ? 27.251 22.985 -14.310 1.00 38.73 ? 245 HIS B CD2 1 ATOM 6667 C CE1 . HIS B 1 245 ? 29.225 22.169 -13.818 1.00 41.59 ? 245 HIS B CE1 1 ATOM 6668 N NE2 . HIS B 1 245 ? 28.391 22.421 -14.807 1.00 38.82 ? 245 HIS B NE2 1 ATOM 6669 N N . VAL B 1 246 ? 28.462 26.668 -10.526 1.00 28.61 ? 246 VAL B N 1 ATOM 6670 C CA . VAL B 1 246 ? 29.609 26.995 -9.708 1.00 26.18 ? 246 VAL B CA 1 ATOM 6671 C C . VAL B 1 246 ? 29.196 27.049 -8.231 1.00 26.20 ? 246 VAL B C 1 ATOM 6672 O O . VAL B 1 246 ? 28.380 27.914 -7.856 1.00 23.90 ? 246 VAL B O 1 ATOM 6673 C CB . VAL B 1 246 ? 30.169 28.369 -10.088 1.00 26.47 ? 246 VAL B CB 1 ATOM 6674 C CG1 . VAL B 1 246 ? 31.426 28.690 -9.300 1.00 26.12 ? 246 VAL B CG1 1 ATOM 6675 C CG2 . VAL B 1 246 ? 30.399 28.471 -11.595 1.00 27.40 ? 246 VAL B CG2 1 ATOM 6676 N N . PRO B 1 247 ? 29.795 26.181 -7.380 1.00 27.84 ? 247 PRO B N 1 ATOM 6677 C CA . PRO B 1 247 ? 29.407 26.129 -5.987 1.00 25.65 ? 247 PRO B CA 1 ATOM 6678 C C . PRO B 1 247 ? 29.782 27.359 -5.219 1.00 24.36 ? 247 PRO B C 1 ATOM 6679 O O . PRO B 1 247 ? 30.510 28.247 -5.717 1.00 25.22 ? 247 PRO B O 1 ATOM 6680 C CB . PRO B 1 247 ? 30.144 24.876 -5.433 1.00 27.89 ? 247 PRO B CB 1 ATOM 6681 C CG . PRO B 1 247 ? 30.623 24.139 -6.653 1.00 28.50 ? 247 PRO B CG 1 ATOM 6682 C CD . PRO B 1 247 ? 30.835 25.181 -7.696 1.00 26.70 ? 247 PRO B CD 1 ATOM 6683 N N . CYS B 1 248 ? 29.261 27.441 -4.008 1.00 25.15 ? 248 CYS B N 1 ATOM 6684 C CA . CYS B 1 248 ? 29.703 28.453 -3.079 1.00 25.85 ? 248 CYS B CA 1 ATOM 6685 C C . CYS B 1 248 ? 31.127 28.127 -2.620 1.00 26.37 ? 248 CYS B C 1 ATOM 6686 O O . CYS B 1 248 ? 31.620 26.980 -2.738 1.00 29.53 ? 248 CYS B O 1 ATOM 6687 C CB . CYS B 1 248 ? 28.786 28.502 -1.865 1.00 25.79 ? 248 CYS B CB 1 ATOM 6688 S SG . CYS B 1 248 ? 27.063 28.701 -2.206 1.00 23.77 ? 248 CYS B SG 1 ATOM 6689 N N . PHE B 1 249 ? 31.763 29.148 -2.068 1.00 29.43 ? 249 PHE B N 1 ATOM 6690 C CA . PHE B 1 249 ? 33.082 29.044 -1.504 1.00 26.88 ? 249 PHE B CA 1 ATOM 6691 C C . PHE B 1 249 ? 32.982 28.423 -0.160 1.00 30.50 ? 249 PHE B C 1 ATOM 6692 O O . PHE B 1 249 ? 31.930 28.478 0.447 1.00 31.97 ? 249 PHE B O 1 ATOM 6693 C CB . PHE B 1 249 ? 33.724 30.401 -1.426 1.00 24.35 ? 249 PHE B CB 1 ATOM 6694 C CG . PHE B 1 249 ? 34.149 30.932 -2.768 1.00 24.66 ? 249 PHE B CG 1 ATOM 6695 C CD1 . PHE B 1 249 ? 34.773 30.103 -3.700 1.00 23.78 ? 249 PHE B CD1 1 ATOM 6696 C CD2 . PHE B 1 249 ? 34.010 32.243 -3.095 1.00 22.37 ? 249 PHE B CD2 1 ATOM 6697 C CE1 . PHE B 1 249 ? 35.217 30.596 -4.914 1.00 25.30 ? 249 PHE B CE1 1 ATOM 6698 C CE2 . PHE B 1 249 ? 34.437 32.724 -4.338 1.00 23.34 ? 249 PHE B CE2 1 ATOM 6699 C CZ . PHE B 1 249 ? 35.044 31.905 -5.252 1.00 22.56 ? 249 PHE B CZ 1 ATOM 6700 N N . GLN B 1 250 ? 34.051 27.771 0.280 1.00 31.15 ? 250 GLN B N 1 ATOM 6701 C CA . GLN B 1 250 ? 34.227 27.324 1.651 1.00 33.78 ? 250 GLN B CA 1 ATOM 6702 C C . GLN B 1 250 ? 35.183 28.232 2.370 1.00 31.42 ? 250 GLN B C 1 ATOM 6703 O O . GLN B 1 250 ? 36.284 28.391 1.968 1.00 37.17 ? 250 GLN B O 1 ATOM 6704 C CB . GLN B 1 250 ? 34.770 25.916 1.758 1.00 39.73 ? 250 GLN B CB 1 ATOM 6705 C CG . GLN B 1 250 ? 33.718 24.885 2.062 1.00 45.28 ? 250 GLN B CG 1 ATOM 6706 C CD . GLN B 1 250 ? 33.387 24.807 3.534 1.00 60.50 ? 250 GLN B CD 1 ATOM 6707 O OE1 . GLN B 1 250 ? 34.150 25.250 4.331 1.00 54.52 ? 250 GLN B OE1 1 ATOM 6708 N NE2 . GLN B 1 250 ? 32.239 24.237 3.880 1.00 65.47 ? 250 GLN B NE2 1 ATOM 6709 N N . ALA B 1 251 ? 34.723 28.839 3.428 1.00 32.41 ? 251 ALA B N 1 ATOM 6710 C CA . ALA B 1 251 ? 35.551 29.770 4.209 1.00 28.80 ? 251 ALA B CA 1 ATOM 6711 C C . ALA B 1 251 ? 35.250 29.590 5.692 1.00 25.69 ? 251 ALA B C 1 ATOM 6712 O O . ALA B 1 251 ? 34.477 28.720 6.075 1.00 25.11 ? 251 ALA B O 1 ATOM 6713 C CB . ALA B 1 251 ? 35.313 31.211 3.759 1.00 26.51 ? 251 ALA B CB 1 ATOM 6714 N N . GLY B 1 252 ? 35.880 30.395 6.541 1.00 24.47 ? 252 GLY B N 1 ATOM 6715 C CA . GLY B 1 252 ? 35.720 30.195 8.002 1.00 25.63 ? 252 GLY B CA 1 ATOM 6716 C C . GLY B 1 252 ? 34.330 30.497 8.506 1.00 25.91 ? 252 GLY B C 1 ATOM 6717 O O . GLY B 1 252 ? 33.938 30.081 9.588 1.00 25.06 ? 252 GLY B O 1 ATOM 6718 N N . ASP B 1 253 ? 33.595 31.292 7.724 1.00 25.73 ? 253 ASP B N 1 ATOM 6719 C CA . ASP B 1 253 ? 32.236 31.631 8.068 1.00 22.19 ? 253 ASP B CA 1 ATOM 6720 C C . ASP B 1 253 ? 31.288 31.172 6.965 1.00 22.38 ? 253 ASP B C 1 ATOM 6721 O O . ASP B 1 253 ? 31.589 31.339 5.759 1.00 23.35 ? 253 ASP B O 1 ATOM 6722 C CB . ASP B 1 253 ? 32.138 33.114 8.292 1.00 24.02 ? 253 ASP B CB 1 ATOM 6723 C CG . ASP B 1 253 ? 30.703 33.547 8.600 1.00 24.73 ? 253 ASP B CG 1 ATOM 6724 O OD1 . ASP B 1 253 ? 30.259 33.391 9.781 1.00 24.36 ? 253 ASP B OD1 1 ATOM 6725 O OD2 . ASP B 1 253 ? 30.022 33.970 7.650 1.00 23.79 ? 253 ASP B OD2 1 ATOM 6726 N N . SER B 1 254 ? 30.167 30.575 7.351 1.00 19.86 ? 254 SER B N 1 ATOM 6727 C CA . SER B 1 254 ? 29.277 29.944 6.377 1.00 21.98 ? 254 SER B CA 1 ATOM 6728 C C . SER B 1 254 ? 28.554 30.956 5.447 1.00 20.88 ? 254 SER B C 1 ATOM 6729 O O . SER B 1 254 ? 27.910 30.554 4.517 1.00 19.56 ? 254 SER B O 1 ATOM 6730 C CB . SER B 1 254 ? 28.228 29.045 7.090 1.00 22.14 ? 254 SER B CB 1 ATOM 6731 O OG . SER B 1 254 ? 27.406 29.837 7.924 1.00 26.56 ? 254 SER B OG 1 ATOM 6732 N N . ARG B 1 255 ? 28.636 32.259 5.720 1.00 18.74 ? 255 ARG B N 1 ATOM 6733 C CA . ARG B 1 255 ? 27.886 33.209 4.915 1.00 17.28 ? 255 ARG B CA 1 ATOM 6734 C C . ARG B 1 255 ? 28.708 33.841 3.821 1.00 18.41 ? 255 ARG B C 1 ATOM 6735 O O . ARG B 1 255 ? 28.258 34.785 3.209 1.00 20.46 ? 255 ARG B O 1 ATOM 6736 C CB . ARG B 1 255 ? 27.375 34.301 5.850 1.00 16.87 ? 255 ARG B CB 1 ATOM 6737 C CG . ARG B 1 255 ? 26.479 33.757 6.930 1.00 16.63 ? 255 ARG B CG 1 ATOM 6738 C CD . ARG B 1 255 ? 26.286 34.750 8.089 1.00 17.70 ? 255 ARG B CD 1 ATOM 6739 N NE . ARG B 1 255 ? 27.507 34.833 8.976 1.00 17.61 ? 255 ARG B NE 1 ATOM 6740 C CZ . ARG B 1 255 ? 27.596 35.606 10.058 1.00 17.39 ? 255 ARG B CZ 1 ATOM 6741 N NH1 . ARG B 1 255 ? 26.540 36.344 10.443 1.00 20.68 ? 255 ARG B NH1 1 ATOM 6742 N NH2 . ARG B 1 255 ? 28.710 35.629 10.790 1.00 16.62 ? 255 ARG B NH2 1 ATOM 6743 N N . ALA B 1 256 ? 29.899 33.307 3.556 1.00 17.46 ? 256 ALA B N 1 ATOM 6744 C CA . ALA B 1 256 ? 30.935 33.994 2.753 1.00 16.32 ? 256 ALA B CA 1 ATOM 6745 C C . ALA B 1 256 ? 30.483 34.302 1.346 1.00 16.31 ? 256 ALA B C 1 ATOM 6746 O O . ALA B 1 256 ? 30.945 35.268 0.721 1.00 14.13 ? 256 ALA B O 1 ATOM 6747 C CB . ALA B 1 256 ? 32.237 33.227 2.729 1.00 16.67 ? 256 ALA B CB 1 ATOM 6748 N N . SER B 1 257 ? 29.543 33.515 0.852 1.00 15.19 ? 257 SER B N 1 ATOM 6749 C CA . SER B 1 257 ? 29.116 33.705 -0.516 1.00 15.19 ? 257 SER B CA 1 ATOM 6750 C C . SER B 1 257 ? 27.789 34.430 -0.654 1.00 14.43 ? 257 SER B C 1 ATOM 6751 O O . SER B 1 257 ? 27.245 34.450 -1.736 1.00 16.66 ? 257 SER B O 1 ATOM 6752 C CB . SER B 1 257 ? 28.996 32.311 -1.207 1.00 17.06 ? 257 SER B CB 1 ATOM 6753 O OG . SER B 1 257 ? 30.247 31.638 -1.204 1.00 20.03 ? 257 SER B OG 1 ATOM 6754 N N . GLU B 1 258 ? 27.215 34.932 0.434 1.00 14.36 ? 258 GLU B N 1 ATOM 6755 C CA . GLU B 1 258 ? 25.915 35.561 0.390 1.00 15.37 ? 258 GLU B CA 1 ATOM 6756 C C . GLU B 1 258 ? 25.775 36.641 -0.628 1.00 15.54 ? 258 GLU B C 1 ATOM 6757 O O . GLU B 1 258 ? 24.683 36.834 -1.146 1.00 18.24 ? 258 GLU B O 1 ATOM 6758 C CB . GLU B 1 258 ? 25.533 36.118 1.749 1.00 16.17 ? 258 GLU B CB 1 ATOM 6759 C CG . GLU B 1 258 ? 24.152 36.712 1.829 1.00 16.72 ? 258 GLU B CG 1 ATOM 6760 C CD . GLU B 1 258 ? 24.122 38.236 1.684 1.00 16.04 ? 258 GLU B CD 1 ATOM 6761 O OE1 . GLU B 1 258 ? 25.190 38.842 1.625 1.00 12.97 ? 258 GLU B OE1 1 ATOM 6762 O OE2 . GLU B 1 258 ? 22.993 38.832 1.536 1.00 14.81 ? 258 GLU B OE2 1 ATOM 6763 N N . GLN B 1 259 ? 26.841 37.410 -0.859 1.00 16.96 ? 259 GLN B N 1 ATOM 6764 C CA . GLN B 1 259 ? 26.921 38.210 -2.033 1.00 16.84 ? 259 GLN B CA 1 ATOM 6765 C C . GLN B 1 259 ? 28.341 38.382 -2.550 1.00 16.56 ? 259 GLN B C 1 ATOM 6766 O O . GLN B 1 259 ? 29.309 38.178 -1.856 1.00 17.13 ? 259 GLN B O 1 ATOM 6767 C CB . GLN B 1 259 ? 26.208 39.531 -1.869 1.00 17.16 ? 259 GLN B CB 1 ATOM 6768 C CG . GLN B 1 259 ? 26.614 40.429 -0.733 1.00 17.46 ? 259 GLN B CG 1 ATOM 6769 C CD . GLN B 1 259 ? 27.731 41.387 -1.031 1.00 17.71 ? 259 GLN B CD 1 ATOM 6770 O OE1 . GLN B 1 259 ? 28.158 41.550 -2.178 1.00 16.11 ? 259 GLN B OE1 1 ATOM 6771 N NE2 . GLN B 1 259 ? 28.253 42.009 0.050 1.00 19.64 ? 259 GLN B NE2 1 ATOM 6772 N N . ILE B 1 260 ? 28.443 38.785 -3.796 1.00 17.06 ? 260 ILE B N 1 ATOM 6773 C CA . ILE B 1 260 ? 29.707 38.630 -4.539 1.00 17.13 ? 260 ILE B CA 1 ATOM 6774 C C . ILE B 1 260 ? 30.827 39.502 -3.945 1.00 19.65 ? 260 ILE B C 1 ATOM 6775 O O . ILE B 1 260 ? 31.956 39.124 -3.945 1.00 19.70 ? 260 ILE B O 1 ATOM 6776 C CB . ILE B 1 260 ? 29.444 39.013 -5.997 1.00 18.68 ? 260 ILE B CB 1 ATOM 6777 C CG1 . ILE B 1 260 ? 30.443 38.311 -6.909 1.00 22.12 ? 260 ILE B CG1 1 ATOM 6778 C CG2 . ILE B 1 260 ? 29.418 40.519 -6.209 1.00 19.10 ? 260 ILE B CG2 1 ATOM 6779 C CD1 . ILE B 1 260 ? 30.201 38.611 -8.374 1.00 27.02 ? 260 ILE B CD1 1 ATOM 6780 N N . LEU B 1 261 ? 30.509 40.676 -3.427 1.00 17.32 ? 261 LEU B N 1 ATOM 6781 C CA . LEU B 1 261 ? 31.559 41.510 -2.828 1.00 17.08 ? 261 LEU B CA 1 ATOM 6782 C C . LEU B 1 261 ? 32.050 41.027 -1.466 1.00 17.53 ? 261 LEU B C 1 ATOM 6783 O O . LEU B 1 261 ? 33.183 41.341 -1.072 1.00 19.06 ? 261 LEU B O 1 ATOM 6784 C CB . LEU B 1 261 ? 31.118 42.934 -2.750 1.00 17.17 ? 261 LEU B CB 1 ATOM 6785 C CG . LEU B 1 261 ? 30.888 43.554 -4.135 1.00 16.71 ? 261 LEU B CG 1 ATOM 6786 C CD1 . LEU B 1 261 ? 30.522 44.978 -3.897 1.00 16.05 ? 261 LEU B CD1 1 ATOM 6787 C CD2 . LEU B 1 261 ? 32.115 43.483 -5.056 1.00 17.75 ? 261 LEU B CD2 1 ATOM 6788 N N . LEU B 1 262 ? 31.227 40.253 -0.756 1.00 16.47 ? 262 LEU B N 1 ATOM 6789 C CA . LEU B 1 262 ? 31.626 39.643 0.464 1.00 16.50 ? 262 LEU B CA 1 ATOM 6790 C C . LEU B 1 262 ? 32.558 38.505 0.147 1.00 17.23 ? 262 LEU B C 1 ATOM 6791 O O . LEU B 1 262 ? 33.571 38.402 0.776 1.00 18.92 ? 262 LEU B O 1 ATOM 6792 C CB . LEU B 1 262 ? 30.427 39.084 1.233 1.00 16.30 ? 262 LEU B CB 1 ATOM 6793 C CG . LEU B 1 262 ? 30.679 38.276 2.457 1.00 15.94 ? 262 LEU B CG 1 ATOM 6794 C CD1 . LEU B 1 262 ? 31.266 39.126 3.557 1.00 16.25 ? 262 LEU B CD1 1 ATOM 6795 C CD2 . LEU B 1 262 ? 29.329 37.750 2.913 1.00 15.66 ? 262 LEU B CD2 1 ATOM 6796 N N . ALA B 1 263 ? 32.221 37.695 -0.849 1.00 18.02 ? 263 ALA B N 1 ATOM 6797 C CA . ALA B 1 263 ? 33.107 36.664 -1.327 1.00 17.89 ? 263 ALA B CA 1 ATOM 6798 C C . ALA B 1 263 ? 34.438 37.272 -1.860 1.00 18.11 ? 263 ALA B C 1 ATOM 6799 O O . ALA B 1 263 ? 35.449 36.705 -1.665 1.00 15.38 ? 263 ALA B O 1 ATOM 6800 C CB . ALA B 1 263 ? 32.439 35.852 -2.427 1.00 20.90 ? 263 ALA B CB 1 ATOM 6801 N N . THR B 1 264 ? 34.398 38.453 -2.484 1.00 18.30 ? 264 THR B N 1 ATOM 6802 C CA . THR B 1 264 ? 35.613 39.158 -2.970 1.00 19.08 ? 264 THR B CA 1 ATOM 6803 C C . THR B 1 264 ? 36.500 39.492 -1.785 1.00 22.75 ? 264 THR B C 1 ATOM 6804 O O . THR B 1 264 ? 37.723 39.231 -1.833 1.00 22.77 ? 264 THR B O 1 ATOM 6805 C CB . THR B 1 264 ? 35.178 40.403 -3.711 1.00 20.48 ? 264 THR B CB 1 ATOM 6806 O OG1 . THR B 1 264 ? 34.551 39.999 -4.944 1.00 17.79 ? 264 THR B OG1 1 ATOM 6807 C CG2 . THR B 1 264 ? 36.337 41.358 -3.976 1.00 20.37 ? 264 THR B CG2 1 ATOM 6808 N N . VAL B 1 265 ? 35.916 39.975 -0.672 1.00 19.78 ? 265 VAL B N 1 ATOM 6809 C CA . VAL B 1 265 ? 36.790 40.377 0.444 1.00 19.29 ? 265 VAL B CA 1 ATOM 6810 C C . VAL B 1 265 ? 37.318 39.150 1.151 1.00 18.95 ? 265 VAL B C 1 ATOM 6811 O O . VAL B 1 265 ? 38.500 39.113 1.524 1.00 25.25 ? 265 VAL B O 1 ATOM 6812 C CB . VAL B 1 265 ? 36.221 41.460 1.388 1.00 16.78 ? 265 VAL B CB 1 ATOM 6813 C CG1 . VAL B 1 265 ? 37.195 41.738 2.586 1.00 20.86 ? 265 VAL B CG1 1 ATOM 6814 C CG2 . VAL B 1 265 ? 36.021 42.731 0.607 1.00 16.87 ? 265 VAL B CG2 1 ATOM 6815 N N . HIS B 1 266 ? 36.505 38.108 1.287 1.00 21.42 ? 266 HIS B N 1 ATOM 6816 C CA . HIS B 1 266 ? 36.957 36.836 1.848 1.00 19.71 ? 266 HIS B CA 1 ATOM 6817 C C . HIS B 1 266 ? 38.166 36.290 1.052 1.00 25.54 ? 266 HIS B C 1 ATOM 6818 O O . HIS B 1 266 ? 39.123 35.671 1.641 1.00 19.78 ? 266 HIS B O 1 ATOM 6819 C CB . HIS B 1 266 ? 35.866 35.764 1.863 1.00 21.97 ? 266 HIS B CB 1 ATOM 6820 C CG . HIS B 1 266 ? 35.049 35.683 3.132 1.00 22.55 ? 266 HIS B CG 1 ATOM 6821 N ND1 . HIS B 1 266 ? 35.432 34.945 4.230 1.00 20.78 ? 266 HIS B ND1 1 ATOM 6822 C CD2 . HIS B 1 266 ? 33.782 36.109 3.399 1.00 22.23 ? 266 HIS B CD2 1 ATOM 6823 C CE1 . HIS B 1 266 ? 34.470 34.994 5.150 1.00 21.89 ? 266 HIS B CE1 1 ATOM 6824 N NE2 . HIS B 1 266 ? 33.459 35.703 4.671 1.00 20.85 ? 266 HIS B NE2 1 ATOM 6825 N N . THR B 1 267 ? 38.088 36.472 -0.264 1.00 22.91 ? 267 THR B N 1 ATOM 6826 C CA . THR B 1 267 ? 39.159 36.031 -1.161 1.00 24.41 ? 267 THR B CA 1 ATOM 6827 C C . THR B 1 267 ? 40.449 36.798 -0.884 1.00 23.16 ? 267 THR B C 1 ATOM 6828 O O . THR B 1 267 ? 41.521 36.177 -0.802 1.00 23.57 ? 267 THR B O 1 ATOM 6829 C CB . THR B 1 267 ? 38.713 36.106 -2.637 1.00 20.89 ? 267 THR B CB 1 ATOM 6830 O OG1 . THR B 1 267 ? 37.728 35.116 -2.849 1.00 18.89 ? 267 THR B OG1 1 ATOM 6831 C CG2 . THR B 1 267 ? 39.893 35.821 -3.621 1.00 22.22 ? 267 THR B CG2 1 ATOM 6832 N N . LEU B 1 268 ? 40.358 38.122 -0.728 1.00 19.56 ? 268 LEU B N 1 ATOM 6833 C CA . LEU B 1 268 ? 41.507 38.939 -0.451 1.00 21.23 ? 268 LEU B CA 1 ATOM 6834 C C . LEU B 1 268 ? 42.180 38.542 0.878 1.00 25.22 ? 268 LEU B C 1 ATOM 6835 O O . LEU B 1 268 ? 43.444 38.538 1.012 1.00 25.21 ? 268 LEU B O 1 ATOM 6836 C CB . LEU B 1 268 ? 41.129 40.421 -0.351 1.00 21.07 ? 268 LEU B CB 1 ATOM 6837 C CG . LEU B 1 268 ? 40.589 41.085 -1.598 1.00 21.08 ? 268 LEU B CG 1 ATOM 6838 C CD1 . LEU B 1 268 ? 40.073 42.472 -1.297 1.00 20.17 ? 268 LEU B CD1 1 ATOM 6839 C CD2 . LEU B 1 268 ? 41.669 41.169 -2.664 1.00 23.23 ? 268 LEU B CD2 1 ATOM 6840 N N . LEU B 1 269 ? 41.348 38.250 1.870 1.00 25.25 ? 269 LEU B N 1 ATOM 6841 C CA . LEU B 1 269 ? 41.853 37.913 3.187 1.00 25.70 ? 269 LEU B CA 1 ATOM 6842 C C . LEU B 1 269 ? 42.577 36.577 3.133 1.00 28.82 ? 269 LEU B C 1 ATOM 6843 O O . LEU B 1 269 ? 43.644 36.402 3.742 1.00 27.11 ? 269 LEU B O 1 ATOM 6844 C CB . LEU B 1 269 ? 40.706 37.866 4.235 1.00 22.84 ? 269 LEU B CB 1 ATOM 6845 C CG . LEU B 1 269 ? 40.153 39.246 4.533 1.00 20.73 ? 269 LEU B CG 1 ATOM 6846 C CD1 . LEU B 1 269 ? 38.866 39.064 5.355 1.00 23.33 ? 269 LEU B CD1 1 ATOM 6847 C CD2 . LEU B 1 269 ? 41.157 40.072 5.293 1.00 19.85 ? 269 LEU B CD2 1 ATOM 6848 N N . LEU B 1 270 ? 41.987 35.626 2.438 1.00 27.49 ? 270 LEU B N 1 ATOM 6849 C CA . LEU B 1 270 ? 42.625 34.316 2.262 1.00 26.61 ? 270 LEU B CA 1 ATOM 6850 C C . LEU B 1 270 ? 44.003 34.417 1.510 1.00 27.91 ? 270 LEU B C 1 ATOM 6851 O O . LEU B 1 270 ? 45.007 33.795 1.916 1.00 30.31 ? 270 LEU B O 1 ATOM 6852 C CB . LEU B 1 270 ? 41.721 33.423 1.470 1.00 24.59 ? 270 LEU B CB 1 ATOM 6853 C CG . LEU B 1 270 ? 42.171 31.978 1.305 1.00 24.57 ? 270 LEU B CG 1 ATOM 6854 C CD1 . LEU B 1 270 ? 42.013 31.225 2.620 1.00 28.88 ? 270 LEU B CD1 1 ATOM 6855 C CD2 . LEU B 1 270 ? 41.353 31.322 0.209 1.00 25.40 ? 270 LEU B CD2 1 ATOM 6856 N N . ARG B 1 271 ? 44.010 35.169 0.424 1.00 25.58 ? 271 ARG B N 1 ATOM 6857 C CA . ARG B 1 271 ? 45.225 35.429 -0.372 1.00 27.55 ? 271 ARG B CA 1 ATOM 6858 C C . ARG B 1 271 ? 46.267 36.038 0.580 1.00 34.48 ? 271 ARG B C 1 ATOM 6859 O O . ARG B 1 271 ? 47.384 35.562 0.616 1.00 34.44 ? 271 ARG B O 1 ATOM 6860 C CB . ARG B 1 271 ? 44.983 36.367 -1.515 1.00 26.01 ? 271 ARG B CB 1 ATOM 6861 C CG . ARG B 1 271 ? 44.274 35.692 -2.665 1.00 27.74 ? 271 ARG B CG 1 ATOM 6862 C CD . ARG B 1 271 ? 43.984 36.668 -3.757 1.00 27.56 ? 271 ARG B CD 1 ATOM 6863 N NE . ARG B 1 271 ? 43.132 36.024 -4.771 1.00 25.08 ? 271 ARG B NE 1 ATOM 6864 C CZ . ARG B 1 271 ? 42.650 36.621 -5.843 1.00 24.76 ? 271 ARG B CZ 1 ATOM 6865 N NH1 . ARG B 1 271 ? 42.931 37.896 -6.096 1.00 26.49 ? 271 ARG B NH1 1 ATOM 6866 N NH2 . ARG B 1 271 ? 41.885 35.931 -6.694 1.00 25.62 ? 271 ARG B NH2 1 ATOM 6867 N N . GLU B 1 272 ? 45.869 37.003 1.411 1.00 34.41 ? 272 GLU B N 1 ATOM 6868 C CA . GLU B 1 272 ? 46.807 37.614 2.363 1.00 32.87 ? 272 GLU B CA 1 ATOM 6869 C C . GLU B 1 272 ? 47.369 36.621 3.323 1.00 29.82 ? 272 GLU B C 1 ATOM 6870 O O . GLU B 1 272 ? 48.546 36.709 3.618 1.00 33.63 ? 272 GLU B O 1 ATOM 6871 C CB . GLU B 1 272 ? 46.183 38.754 3.123 1.00 34.63 ? 272 GLU B CB 1 ATOM 6872 C CG . GLU B 1 272 ? 47.053 39.398 4.221 1.00 33.57 ? 272 GLU B CG 1 ATOM 6873 C CD . GLU B 1 272 ? 48.257 40.184 3.692 1.00 37.67 ? 272 GLU B CD 1 ATOM 6874 O OE1 . GLU B 1 272 ? 48.361 40.448 2.468 1.00 30.79 ? 272 GLU B OE1 1 ATOM 6875 O OE2 . GLU B 1 272 ? 49.135 40.533 4.520 1.00 39.73 ? 272 GLU B OE2 1 ATOM 6876 N N . HIS B 1 273 ? 46.591 35.671 3.824 1.00 31.22 ? 273 HIS B N 1 ATOM 6877 C CA . HIS B 1 273 ? 47.173 34.690 4.738 1.00 30.71 ? 273 HIS B CA 1 ATOM 6878 C C . HIS B 1 273 ? 48.334 33.951 4.077 1.00 34.67 ? 273 HIS B C 1 ATOM 6879 O O . HIS B 1 273 ? 49.385 33.711 4.694 1.00 31.80 ? 273 HIS B O 1 ATOM 6880 C CB . HIS B 1 273 ? 46.196 33.644 5.202 1.00 31.06 ? 273 HIS B CB 1 ATOM 6881 C CG . HIS B 1 273 ? 46.847 32.520 5.943 1.00 38.02 ? 273 HIS B CG 1 ATOM 6882 N ND1 . HIS B 1 273 ? 46.893 32.454 7.323 1.00 38.05 ? 273 HIS B ND1 1 ATOM 6883 C CD2 . HIS B 1 273 ? 47.498 31.425 5.495 1.00 40.09 ? 273 HIS B CD2 1 ATOM 6884 C CE1 . HIS B 1 273 ? 47.498 31.343 7.686 1.00 43.86 ? 273 HIS B CE1 1 ATOM 6885 N NE2 . HIS B 1 273 ? 47.883 30.702 6.597 1.00 42.98 ? 273 HIS B NE2 1 ATOM 6886 N N . ASN B 1 274 ? 48.095 33.484 2.871 1.00 34.86 ? 274 ASN B N 1 ATOM 6887 C CA . ASN B 1 274 ? 49.121 32.751 2.168 1.00 35.55 ? 274 ASN B CA 1 ATOM 6888 C C . ASN B 1 274 ? 50.321 33.610 1.821 1.00 33.88 ? 274 ASN B C 1 ATOM 6889 O O . ASN B 1 274 ? 51.427 33.160 1.918 1.00 41.83 ? 274 ASN B O 1 ATOM 6890 C CB . ASN B 1 274 ? 48.514 32.067 0.949 1.00 32.80 ? 274 ASN B CB 1 ATOM 6891 C CG . ASN B 1 274 ? 47.684 30.897 1.350 1.00 34.64 ? 274 ASN B CG 1 ATOM 6892 O OD1 . ASN B 1 274 ? 47.713 30.509 2.515 1.00 37.21 ? 274 ASN B OD1 1 ATOM 6893 N ND2 . ASN B 1 274 ? 46.943 30.311 0.408 1.00 39.84 ? 274 ASN B ND2 1 ATOM 6894 N N . ARG B 1 275 ? 50.098 34.872 1.482 1.00 39.73 ? 275 ARG B N 1 ATOM 6895 C CA . ARG B 1 275 ? 51.195 35.795 1.233 1.00 39.24 ? 275 ARG B CA 1 ATOM 6896 C C . ARG B 1 275 ? 52.078 35.866 2.468 1.00 44.05 ? 275 ARG B C 1 ATOM 6897 O O . ARG B 1 275 ? 53.302 35.766 2.363 1.00 46.30 ? 275 ARG B O 1 ATOM 6898 C CB . ARG B 1 275 ? 50.669 37.177 0.910 1.00 40.29 ? 275 ARG B CB 1 ATOM 6899 C CG . ARG B 1 275 ? 51.665 38.066 0.240 1.00 36.21 ? 275 ARG B CG 1 ATOM 6900 C CD . ARG B 1 275 ? 51.123 39.464 0.095 1.00 35.46 ? 275 ARG B CD 1 ATOM 6901 N NE . ARG B 1 275 ? 50.856 40.061 1.406 1.00 38.08 ? 275 ARG B NE 1 ATOM 6902 C CZ . ARG B 1 275 ? 51.784 40.574 2.201 1.00 42.95 ? 275 ARG B CZ 1 ATOM 6903 N NH1 . ARG B 1 275 ? 53.047 40.570 1.827 1.00 43.47 ? 275 ARG B NH1 1 ATOM 6904 N NH2 . ARG B 1 275 ? 51.477 41.061 3.383 1.00 46.80 ? 275 ARG B NH2 1 ATOM 6905 N N . LEU B 1 276 ? 51.449 36.031 3.627 1.00 37.28 ? 276 LEU B N 1 ATOM 6906 C CA . LEU B 1 276 ? 52.139 36.111 4.900 1.00 39.07 ? 276 LEU B CA 1 ATOM 6907 C C . LEU B 1 276 ? 52.890 34.828 5.260 1.00 41.54 ? 276 LEU B C 1 ATOM 6908 O O . LEU B 1 276 ? 54.020 34.891 5.737 1.00 52.55 ? 276 LEU B O 1 ATOM 6909 C CB . LEU B 1 276 ? 51.160 36.424 6.025 1.00 35.36 ? 276 LEU B CB 1 ATOM 6910 C CG . LEU B 1 276 ? 50.565 37.826 6.044 1.00 32.69 ? 276 LEU B CG 1 ATOM 6911 C CD1 . LEU B 1 276 ? 49.399 37.846 7.043 1.00 37.06 ? 276 LEU B CD1 1 ATOM 6912 C CD2 . LEU B 1 276 ? 51.548 38.920 6.371 1.00 36.66 ? 276 LEU B CD2 1 ATOM 6913 N N . ALA B 1 277 ? 52.287 33.675 5.029 1.00 37.77 ? 277 ALA B N 1 ATOM 6914 C CA . ALA B 1 277 ? 52.933 32.411 5.366 1.00 41.86 ? 277 ALA B CA 1 ATOM 6915 C C . ALA B 1 277 ? 54.161 32.160 4.460 1.00 47.24 ? 277 ALA B C 1 ATOM 6916 O O . ALA B 1 277 ? 55.092 31.459 4.849 1.00 54.91 ? 277 ALA B O 1 ATOM 6917 C CB . ALA B 1 277 ? 51.957 31.268 5.258 1.00 40.76 ? 277 ALA B CB 1 ATOM 6918 N N . ARG B 1 278 ? 54.156 32.740 3.262 1.00 42.16 ? 278 ARG B N 1 ATOM 6919 C CA . ARG B 1 278 ? 55.225 32.496 2.323 1.00 45.67 ? 278 ARG B CA 1 ATOM 6920 C C . ARG B 1 278 ? 56.360 33.396 2.654 1.00 45.54 ? 278 ARG B C 1 ATOM 6921 O O . ARG B 1 278 ? 57.519 32.993 2.564 1.00 44.27 ? 278 ARG B O 1 ATOM 6922 C CB . ARG B 1 278 ? 54.791 32.767 0.890 1.00 42.73 ? 278 ARG B CB 1 ATOM 6923 C CG . ARG B 1 278 ? 53.923 31.656 0.371 1.00 44.42 ? 278 ARG B CG 1 ATOM 6924 C CD . ARG B 1 278 ? 53.607 31.854 -1.102 1.00 48.49 ? 278 ARG B CD 1 ATOM 6925 N NE . ARG B 1 278 ? 52.530 30.930 -1.423 1.00 50.82 ? 278 ARG B NE 1 ATOM 6926 C CZ . ARG B 1 278 ? 51.283 31.289 -1.683 1.00 49.52 ? 278 ARG B CZ 1 ATOM 6927 N NH1 . ARG B 1 278 ? 50.921 32.577 -1.753 1.00 43.80 ? 278 ARG B NH1 1 ATOM 6928 N NH2 . ARG B 1 278 ? 50.394 30.337 -1.906 1.00 57.74 ? 278 ARG B NH2 1 ATOM 6929 N N . GLU B 1 279 ? 56.025 34.610 3.041 1.00 41.63 ? 279 GLU B N 1 ATOM 6930 C CA . GLU B 1 279 ? 57.031 35.558 3.448 1.00 49.37 ? 279 GLU B CA 1 ATOM 6931 C C . GLU B 1 279 ? 57.694 35.190 4.799 1.00 57.43 ? 279 GLU B C 1 ATOM 6932 O O . GLU B 1 279 ? 58.882 35.456 4.984 1.00 59.34 ? 279 GLU B O 1 ATOM 6933 C CB . GLU B 1 279 ? 56.462 36.979 3.456 1.00 47.50 ? 279 GLU B CB 1 ATOM 6934 C CG . GLU B 1 279 ? 57.407 38.027 2.903 1.00 55.83 ? 279 GLU B CG 1 ATOM 6935 C CD . GLU B 1 279 ? 57.969 37.670 1.521 1.00 59.40 ? 279 GLU B CD 1 ATOM 6936 O OE1 . GLU B 1 279 ? 58.516 36.550 1.347 1.00 62.64 ? 279 GLU B OE1 1 ATOM 6937 O OE2 . GLU B 1 279 ? 57.874 38.512 0.604 1.00 56.30 ? 279 GLU B OE2 1 ATOM 6938 N N . LEU B 1 280 ? 56.946 34.556 5.706 1.00 56.70 ? 280 LEU B N 1 ATOM 6939 C CA . LEU B 1 280 ? 57.497 34.062 6.981 1.00 58.52 ? 280 LEU B CA 1 ATOM 6940 C C . LEU B 1 280 ? 58.321 32.798 6.802 1.00 61.96 ? 280 LEU B C 1 ATOM 6941 O O . LEU B 1 280 ? 59.263 32.563 7.542 1.00 71.94 ? 280 LEU B O 1 ATOM 6942 C CB . LEU B 1 280 ? 56.391 33.781 8.027 1.00 52.19 ? 280 LEU B CB 1 ATOM 6943 C CG . LEU B 1 280 ? 55.515 34.990 8.425 1.00 53.85 ? 280 LEU B CG 1 ATOM 6944 C CD1 . LEU B 1 280 ? 54.266 34.534 9.191 1.00 54.45 ? 280 LEU B CD1 1 ATOM 6945 C CD2 . LEU B 1 280 ? 56.287 36.048 9.207 1.00 48.22 ? 280 LEU B CD2 1 ATOM 6946 N N . LYS B 1 281 ? 57.945 31.952 5.859 1.00 63.33 ? 281 LYS B N 1 ATOM 6947 C CA . LYS B 1 281 ? 58.698 30.738 5.626 1.00 66.05 ? 281 LYS B CA 1 ATOM 6948 C C . LYS B 1 281 ? 60.045 31.092 4.991 1.00 67.87 ? 281 LYS B C 1 ATOM 6949 O O . LYS B 1 281 ? 61.055 30.416 5.205 1.00 62.98 ? 281 LYS B O 1 ATOM 6950 C CB . LYS B 1 281 ? 57.884 29.797 4.754 1.00 67.66 ? 281 LYS B CB 1 ATOM 6951 C CG . LYS B 1 281 ? 58.672 28.656 4.160 1.00 66.31 ? 281 LYS B CG 1 ATOM 6952 C CD . LYS B 1 281 ? 59.325 27.798 5.224 1.00 62.89 ? 281 LYS B CD 1 ATOM 6953 C CE . LYS B 1 281 ? 60.249 26.804 4.559 1.00 62.82 ? 281 LYS B CE 1 ATOM 6954 N NZ . LYS B 1 281 ? 60.269 25.518 5.299 1.00 64.95 ? 281 LYS B NZ 1 ATOM 6955 N N . ARG B 1 282 ? 60.054 32.207 4.293 1.00 67.30 ? 282 ARG B N 1 ATOM 6956 C CA . ARG B 1 282 ? 61.276 32.711 3.739 1.00 69.08 ? 282 ARG B CA 1 ATOM 6957 C C . ARG B 1 282 ? 62.134 33.116 4.903 1.00 69.62 ? 282 ARG B C 1 ATOM 6958 O O . ARG B 1 282 ? 63.226 32.615 5.081 1.00 73.85 ? 282 ARG B O 1 ATOM 6959 C CB . ARG B 1 282 ? 61.007 33.879 2.802 1.00 66.31 ? 282 ARG B CB 1 ATOM 6960 C CG . ARG B 1 282 ? 62.185 34.794 2.552 1.00 66.14 ? 282 ARG B CG 1 ATOM 6961 C CD . ARG B 1 282 ? 61.684 36.184 2.312 1.00 63.16 ? 282 ARG B CD 1 ATOM 6962 N NE . ARG B 1 282 ? 62.700 37.207 2.448 1.00 66.76 ? 282 ARG B NE 1 ATOM 6963 C CZ . ARG B 1 282 ? 62.414 38.501 2.554 1.00 77.65 ? 282 ARG B CZ 1 ATOM 6964 N NH1 . ARG B 1 282 ? 61.145 38.909 2.577 1.00 80.59 ? 282 ARG B NH1 1 ATOM 6965 N NH2 . ARG B 1 282 ? 63.368 39.392 2.652 1.00 78.68 ? 282 ARG B NH2 1 ATOM 6966 N N . LEU B 1 283 ? 61.627 34.032 5.696 1.00 66.23 ? 283 LEU B N 1 ATOM 6967 C CA . LEU B 1 283 ? 62.387 34.626 6.802 1.00 60.27 ? 283 LEU B CA 1 ATOM 6968 C C . LEU B 1 283 ? 62.774 33.621 7.879 1.00 54.82 ? 283 LEU B C 1 ATOM 6969 O O . LEU B 1 283 ? 63.772 33.804 8.559 1.00 65.62 ? 283 LEU B O 1 ATOM 6970 C CB . LEU B 1 283 ? 61.576 35.704 7.489 1.00 61.94 ? 283 LEU B CB 1 ATOM 6971 C CG . LEU B 1 283 ? 61.093 36.933 6.742 1.00 65.88 ? 283 LEU B CG 1 ATOM 6972 C CD1 . LEU B 1 283 ? 60.297 37.765 7.730 1.00 65.20 ? 283 LEU B CD1 1 ATOM 6973 C CD2 . LEU B 1 283 ? 62.230 37.743 6.149 1.00 67.61 ? 283 LEU B CD2 1 ATOM 6974 N N . ASN B 1 284 ? 61.979 32.573 8.053 1.00 52.55 ? 284 ASN B N 1 ATOM 6975 C CA . ASN B 1 284 ? 62.209 31.581 9.088 1.00 50.89 ? 284 ASN B CA 1 ATOM 6976 C C . ASN B 1 284 ? 62.066 30.202 8.535 1.00 53.39 ? 284 ASN B C 1 ATOM 6977 O O . ASN B 1 284 ? 61.181 29.458 8.944 1.00 51.65 ? 284 ASN B O 1 ATOM 6978 C CB . ASN B 1 284 ? 61.258 31.777 10.268 1.00 59.13 ? 284 ASN B CB 1 ATOM 6979 C CG . ASN B 1 284 ? 61.327 33.188 10.824 1.00 64.32 ? 284 ASN B CG 1 ATOM 6980 O OD1 . ASN B 1 284 ? 62.401 33.689 11.130 1.00 71.29 ? 284 ASN B OD1 1 ATOM 6981 N ND2 . ASN B 1 284 ? 60.193 33.841 10.933 1.00 68.63 ? 284 ASN B ND2 1 ATOM 6982 N N . PRO B 1 285 ? 62.988 29.819 7.635 1.00 55.40 ? 285 PRO B N 1 ATOM 6983 C CA . PRO B 1 285 ? 62.940 28.501 6.975 1.00 53.79 ? 285 PRO B CA 1 ATOM 6984 C C . PRO B 1 285 ? 62.778 27.327 7.928 1.00 50.90 ? 285 PRO B C 1 ATOM 6985 O O . PRO B 1 285 ? 62.266 26.291 7.529 1.00 54.34 ? 285 PRO B O 1 ATOM 6986 C CB . PRO B 1 285 ? 64.286 28.439 6.231 1.00 61.18 ? 285 PRO B CB 1 ATOM 6987 C CG . PRO B 1 285 ? 64.639 29.870 5.963 1.00 55.76 ? 285 PRO B CG 1 ATOM 6988 C CD . PRO B 1 285 ? 64.148 30.613 7.181 1.00 55.60 ? 285 PRO B CD 1 ATOM 6989 N N . HIS B 1 286 ? 63.211 27.503 9.169 1.00 52.45 ? 286 HIS B N 1 ATOM 6990 C CA . HIS B 1 286 ? 63.131 26.462 10.193 1.00 58.52 ? 286 HIS B CA 1 ATOM 6991 C C . HIS B 1 286 ? 61.739 26.228 10.784 1.00 61.08 ? 286 HIS B C 1 ATOM 6992 O O . HIS B 1 286 ? 61.439 25.103 11.265 1.00 48.18 ? 286 HIS B O 1 ATOM 6993 C CB . HIS B 1 286 ? 64.119 26.730 11.352 1.00 61.83 ? 286 HIS B CB 1 ATOM 6994 C CG . HIS B 1 286 ? 63.962 28.067 12.028 1.00 56.35 ? 286 HIS B CG 1 ATOM 6995 N ND1 . HIS B 1 286 ? 64.361 29.256 11.446 1.00 58.72 ? 286 HIS B ND1 1 ATOM 6996 C CD2 . HIS B 1 286 ? 63.524 28.386 13.273 1.00 50.81 ? 286 HIS B CD2 1 ATOM 6997 C CE1 . HIS B 1 286 ? 64.132 30.255 12.285 1.00 57.55 ? 286 HIS B CE1 1 ATOM 6998 N NE2 . HIS B 1 286 ? 63.619 29.752 13.400 1.00 56.91 ? 286 HIS B NE2 1 ATOM 6999 N N . TRP B 1 287 ? 60.911 27.277 10.779 1.00 59.27 ? 287 TRP B N 1 ATOM 7000 C CA . TRP B 1 287 ? 59.541 27.165 11.314 1.00 56.94 ? 287 TRP B CA 1 ATOM 7001 C C . TRP B 1 287 ? 58.809 26.099 10.577 1.00 53.14 ? 287 TRP B C 1 ATOM 7002 O O . TRP B 1 287 ? 58.897 26.040 9.346 1.00 54.75 ? 287 TRP B O 1 ATOM 7003 C CB . TRP B 1 287 ? 58.776 28.460 11.141 1.00 57.02 ? 287 TRP B CB 1 ATOM 7004 C CG . TRP B 1 287 ? 59.143 29.478 12.128 1.00 60.63 ? 287 TRP B CG 1 ATOM 7005 C CD1 . TRP B 1 287 ? 60.101 29.380 13.093 1.00 59.24 ? 287 TRP B CD1 1 ATOM 7006 C CD2 . TRP B 1 287 ? 58.588 30.781 12.235 1.00 62.42 ? 287 TRP B CD2 1 ATOM 7007 N NE1 . TRP B 1 287 ? 60.169 30.543 13.803 1.00 66.07 ? 287 TRP B NE1 1 ATOM 7008 C CE2 . TRP B 1 287 ? 59.256 31.428 13.292 1.00 65.23 ? 287 TRP B CE2 1 ATOM 7009 C CE3 . TRP B 1 287 ? 57.583 31.466 11.541 1.00 61.86 ? 287 TRP B CE3 1 ATOM 7010 C CZ2 . TRP B 1 287 ? 58.949 32.726 13.684 1.00 66.84 ? 287 TRP B CZ2 1 ATOM 7011 C CZ3 . TRP B 1 287 ? 57.285 32.751 11.917 1.00 65.80 ? 287 TRP B CZ3 1 ATOM 7012 C CH2 . TRP B 1 287 ? 57.964 33.375 12.991 1.00 70.49 ? 287 TRP B CH2 1 ATOM 7013 N N . ASP B 1 288 ? 58.105 25.262 11.327 1.00 48.78 ? 288 ASP B N 1 ATOM 7014 C CA . ASP B 1 288 ? 57.276 24.219 10.745 1.00 54.74 ? 288 ASP B CA 1 ATOM 7015 C C . ASP B 1 288 ? 55.870 24.753 10.322 1.00 53.39 ? 288 ASP B C 1 ATOM 7016 O O . ASP B 1 288 ? 55.565 25.947 10.470 1.00 49.66 ? 288 ASP B O 1 ATOM 7017 C CB . ASP B 1 288 ? 57.161 23.033 11.717 1.00 55.55 ? 288 ASP B CB 1 ATOM 7018 C CG . ASP B 1 288 ? 56.410 23.382 12.990 1.00 58.06 ? 288 ASP B CG 1 ATOM 7019 O OD1 . ASP B 1 288 ? 56.179 24.586 13.266 1.00 61.82 ? 288 ASP B OD1 1 ATOM 7020 O OD2 . ASP B 1 288 ? 56.064 22.428 13.717 1.00 58.83 ? 288 ASP B OD2 1 ATOM 7021 N N . GLY B 1 289 ? 55.071 23.852 9.742 1.00 55.46 ? 289 GLY B N 1 ATOM 7022 C CA . GLY B 1 289 ? 53.769 24.172 9.170 1.00 54.67 ? 289 GLY B CA 1 ATOM 7023 C C . GLY B 1 289 ? 52.820 24.859 10.141 1.00 54.73 ? 289 GLY B C 1 ATOM 7024 O O . GLY B 1 289 ? 52.233 25.874 9.798 1.00 49.93 ? 289 GLY B O 1 ATOM 7025 N N . GLU B 1 290 ? 52.708 24.312 11.354 1.00 54.44 ? 290 GLU B N 1 ATOM 7026 C CA . GLU B 1 290 ? 51.873 24.871 12.424 1.00 56.01 ? 290 GLU B CA 1 ATOM 7027 C C . GLU B 1 290 ? 52.231 26.297 12.809 1.00 57.50 ? 290 GLU B C 1 ATOM 7028 O O . GLU B 1 290 ? 51.361 27.157 13.060 1.00 63.72 ? 290 GLU B O 1 ATOM 7029 C CB . GLU B 1 290 ? 52.005 24.032 13.689 1.00 55.81 ? 290 GLU B CB 1 ATOM 7030 C CG . GLU B 1 290 ? 51.076 24.505 14.808 1.00 58.45 ? 290 GLU B CG 1 ATOM 7031 C CD . GLU B 1 290 ? 49.603 24.275 14.516 1.00 53.45 ? 290 GLU B CD 1 ATOM 7032 O OE1 . GLU B 1 290 ? 49.262 23.479 13.614 1.00 52.39 ? 290 GLU B OE1 1 ATOM 7033 O OE2 . GLU B 1 290 ? 48.783 24.841 15.250 1.00 50.96 ? 290 GLU B OE2 1 ATOM 7034 N N . MET B 1 291 ? 53.523 26.551 12.890 1.00 56.79 ? 291 MET B N 1 ATOM 7035 C CA . MET B 1 291 ? 53.972 27.821 13.380 1.00 53.49 ? 291 MET B CA 1 ATOM 7036 C C . MET B 1 291 ? 53.723 28.887 12.332 1.00 51.72 ? 291 MET B C 1 ATOM 7037 O O . MET B 1 291 ? 53.399 30.026 12.649 1.00 50.55 ? 291 MET B O 1 ATOM 7038 C CB . MET B 1 291 ? 55.450 27.774 13.726 1.00 56.49 ? 291 MET B CB 1 ATOM 7039 C CG . MET B 1 291 ? 55.924 29.100 14.294 1.00 59.48 ? 291 MET B CG 1 ATOM 7040 S SD . MET B 1 291 ? 57.238 28.941 15.505 1.00 68.56 ? 291 MET B SD 1 ATOM 7041 C CE . MET B 1 291 ? 57.483 30.678 15.868 1.00 61.86 ? 291 MET B CE 1 ATOM 7042 N N . LEU B 1 292 ? 53.938 28.514 11.076 1.00 55.08 ? 292 LEU B N 1 ATOM 7043 C CA . LEU B 1 292 ? 53.699 29.408 9.941 1.00 50.92 ? 292 LEU B CA 1 ATOM 7044 C C . LEU B 1 292 ? 52.206 29.795 9.878 1.00 44.14 ? 292 LEU B C 1 ATOM 7045 O O . LEU B 1 292 ? 51.876 30.970 9.805 1.00 44.45 ? 292 LEU B O 1 ATOM 7046 C CB . LEU B 1 292 ? 54.184 28.747 8.645 1.00 45.61 ? 292 LEU B CB 1 ATOM 7047 C CG . LEU B 1 292 ? 55.725 28.755 8.474 1.00 44.64 ? 292 LEU B CG 1 ATOM 7048 C CD1 . LEU B 1 292 ? 56.165 27.716 7.453 1.00 45.83 ? 292 LEU B CD1 1 ATOM 7049 C CD2 . LEU B 1 292 ? 56.245 30.138 8.090 1.00 42.56 ? 292 LEU B CD2 1 ATOM 7050 N N . TYR B 1 293 ? 51.343 28.794 9.979 1.00 42.75 ? 293 TYR B N 1 ATOM 7051 C CA . TYR B 1 293 ? 49.905 29.010 10.001 1.00 46.35 ? 293 TYR B CA 1 ATOM 7052 C C . TYR B 1 293 ? 49.558 29.970 11.121 1.00 46.62 ? 293 TYR B C 1 ATOM 7053 O O . TYR B 1 293 ? 49.027 31.064 10.868 1.00 44.53 ? 293 TYR B O 1 ATOM 7054 C CB . TYR B 1 293 ? 49.178 27.682 10.214 1.00 48.11 ? 293 TYR B CB 1 ATOM 7055 C CG . TYR B 1 293 ? 47.705 27.799 10.573 1.00 50.25 ? 293 TYR B CG 1 ATOM 7056 C CD1 . TYR B 1 293 ? 46.744 27.983 9.585 1.00 50.35 ? 293 TYR B CD1 1 ATOM 7057 C CD2 . TYR B 1 293 ? 47.270 27.704 11.894 1.00 48.98 ? 293 TYR B CD2 1 ATOM 7058 C CE1 . TYR B 1 293 ? 45.399 28.087 9.911 1.00 52.22 ? 293 TYR B CE1 1 ATOM 7059 C CE2 . TYR B 1 293 ? 45.941 27.806 12.230 1.00 52.36 ? 293 TYR B CE2 1 ATOM 7060 C CZ . TYR B 1 293 ? 44.994 28.002 11.231 1.00 49.65 ? 293 TYR B CZ 1 ATOM 7061 O OH . TYR B 1 293 ? 43.667 28.082 11.578 1.00 41.57 ? 293 TYR B OH 1 ATOM 7062 N N . GLN B 1 294 ? 49.891 29.563 12.350 1.00 46.71 ? 294 GLN B N 1 ATOM 7063 C CA . GLN B 1 294 ? 49.528 30.348 13.552 1.00 45.24 ? 294 GLN B CA 1 ATOM 7064 C C . GLN B 1 294 ? 50.035 31.768 13.497 1.00 37.47 ? 294 GLN B C 1 ATOM 7065 O O . GLN B 1 294 ? 49.330 32.714 13.852 1.00 43.31 ? 294 GLN B O 1 ATOM 7066 C CB . GLN B 1 294 ? 50.000 29.670 14.831 1.00 43.26 ? 294 GLN B CB 1 ATOM 7067 C CG . GLN B 1 294 ? 49.349 28.312 15.134 1.00 44.98 ? 294 GLN B CG 1 ATOM 7068 C CD . GLN B 1 294 ? 47.850 28.389 15.411 1.00 44.22 ? 294 GLN B CD 1 ATOM 7069 O OE1 . GLN B 1 294 ? 47.266 29.467 15.585 1.00 50.16 ? 294 GLN B OE1 1 ATOM 7070 N NE2 . GLN B 1 294 ? 47.221 27.248 15.417 1.00 42.42 ? 294 GLN B NE2 1 ATOM 7071 N N . GLU B 1 295 ? 51.237 31.951 12.967 1.00 40.33 ? 295 GLU B N 1 ATOM 7072 C CA . GLU B 1 295 ? 51.844 33.282 12.961 1.00 35.60 ? 295 GLU B CA 1 ATOM 7073 C C . GLU B 1 295 ? 51.212 34.148 11.877 1.00 36.11 ? 295 GLU B C 1 ATOM 7074 O O . GLU B 1 295 ? 51.057 35.353 12.041 1.00 34.31 ? 295 GLU B O 1 ATOM 7075 C CB . GLU B 1 295 ? 53.397 33.222 12.803 1.00 37.85 ? 295 GLU B CB 1 ATOM 7076 C CG . GLU B 1 295 ? 54.235 32.762 14.050 1.00 36.34 ? 295 GLU B CG 1 ATOM 7077 C CD . GLU B 1 295 ? 54.342 33.802 15.179 1.00 35.01 ? 295 GLU B CD 1 ATOM 7078 O OE1 . GLU B 1 295 ? 54.530 35.012 14.876 1.00 31.06 ? 295 GLU B OE1 1 ATOM 7079 O OE2 . GLU B 1 295 ? 54.238 33.394 16.385 1.00 34.55 ? 295 GLU B OE2 1 ATOM 7080 N N . ALA B 1 296 ? 50.882 33.546 10.737 1.00 40.71 ? 296 ALA B N 1 ATOM 7081 C CA . ALA B 1 296 ? 50.116 34.255 9.684 1.00 36.81 ? 296 ALA B CA 1 ATOM 7082 C C . ALA B 1 296 ? 48.725 34.671 10.206 1.00 33.67 ? 296 ALA B C 1 ATOM 7083 O O . ALA B 1 296 ? 48.300 35.819 10.054 1.00 29.45 ? 296 ALA B O 1 ATOM 7084 C CB . ALA B 1 296 ? 49.979 33.348 8.473 1.00 38.55 ? 296 ALA B CB 1 ATOM 7085 N N . ARG B 1 297 ? 48.050 33.713 10.807 1.00 34.96 ? 297 ARG B N 1 ATOM 7086 C CA . ARG B 1 297 ? 46.739 33.901 11.457 1.00 36.60 ? 297 ARG B CA 1 ATOM 7087 C C . ARG B 1 297 ? 46.747 35.055 12.430 1.00 41.01 ? 297 ARG B C 1 ATOM 7088 O O . ARG B 1 297 ? 45.869 35.928 12.407 1.00 41.95 ? 297 ARG B O 1 ATOM 7089 C CB . ARG B 1 297 ? 46.359 32.601 12.154 1.00 38.58 ? 297 ARG B CB 1 ATOM 7090 C CG . ARG B 1 297 ? 45.112 32.685 13.010 1.00 43.06 ? 297 ARG B CG 1 ATOM 7091 C CD . ARG B 1 297 ? 44.635 31.315 13.407 1.00 43.17 ? 297 ARG B CD 1 ATOM 7092 N NE . ARG B 1 297 ? 43.495 31.450 14.310 1.00 45.77 ? 297 ARG B NE 1 ATOM 7093 C CZ . ARG B 1 297 ? 43.451 31.065 15.569 1.00 47.53 ? 297 ARG B CZ 1 ATOM 7094 N NH1 . ARG B 1 297 ? 44.490 30.464 16.139 1.00 46.55 ? 297 ARG B NH1 1 ATOM 7095 N NH2 . ARG B 1 297 ? 42.339 31.271 16.268 1.00 44.70 ? 297 ARG B NH2 1 ATOM 7096 N N . LYS B 1 298 ? 47.775 35.090 13.270 1.00 42.71 ? 298 LYS B N 1 ATOM 7097 C CA . LYS B 1 298 ? 47.882 36.109 14.273 1.00 38.25 ? 298 LYS B CA 1 ATOM 7098 C C . LYS B 1 298 ? 48.038 37.475 13.618 1.00 36.79 ? 298 LYS B C 1 ATOM 7099 O O . LYS B 1 298 ? 47.448 38.465 14.051 1.00 31.92 ? 298 LYS B O 1 ATOM 7100 C CB . LYS B 1 298 ? 49.058 35.763 15.182 1.00 45.30 ? 298 LYS B CB 1 ATOM 7101 C CG . LYS B 1 298 ? 49.213 36.623 16.422 1.00 50.29 ? 298 LYS B CG 1 ATOM 7102 C CD . LYS B 1 298 ? 50.053 35.881 17.479 1.00 52.35 ? 298 LYS B CD 1 ATOM 7103 C CE . LYS B 1 298 ? 50.878 36.812 18.360 1.00 58.04 ? 298 LYS B CE 1 ATOM 7104 N NZ . LYS B 1 298 ? 51.465 36.040 19.503 1.00 57.55 ? 298 LYS B NZ 1 ATOM 7105 N N . ILE B 1 299 ? 48.797 37.558 12.541 1.00 34.83 ? 299 ILE B N 1 ATOM 7106 C CA . ILE B 1 299 ? 48.954 38.837 11.853 1.00 32.42 ? 299 ILE B CA 1 ATOM 7107 C C . ILE B 1 299 ? 47.639 39.327 11.158 1.00 31.56 ? 299 ILE B C 1 ATOM 7108 O O . ILE B 1 299 ? 47.344 40.557 11.113 1.00 28.80 ? 299 ILE B O 1 ATOM 7109 C CB . ILE B 1 299 ? 50.109 38.724 10.786 1.00 35.13 ? 299 ILE B CB 1 ATOM 7110 C CG1 . ILE B 1 299 ? 51.476 38.567 11.506 1.00 42.11 ? 299 ILE B CG1 1 ATOM 7111 C CG2 . ILE B 1 299 ? 50.119 39.922 9.833 1.00 29.12 ? 299 ILE B CG2 1 ATOM 7112 C CD1 . ILE B 1 299 ? 52.632 38.130 10.607 1.00 44.04 ? 299 ILE B CD1 1 ATOM 7113 N N . LEU B 1 300 ? 46.924 38.379 10.549 1.00 29.83 ? 300 LEU B N 1 ATOM 7114 C CA . LEU B 1 300 ? 45.689 38.692 9.787 1.00 30.25 ? 300 LEU B CA 1 ATOM 7115 C C . LEU B 1 300 ? 44.618 39.192 10.761 1.00 25.88 ? 300 LEU B C 1 ATOM 7116 O O . LEU B 1 300 ? 43.998 40.267 10.573 1.00 28.16 ? 300 LEU B O 1 ATOM 7117 C CB . LEU B 1 300 ? 45.206 37.474 9.000 1.00 30.81 ? 300 LEU B CB 1 ATOM 7118 C CG . LEU B 1 300 ? 44.132 37.848 7.954 1.00 30.55 ? 300 LEU B CG 1 ATOM 7119 C CD1 . LEU B 1 300 ? 44.703 38.797 6.934 1.00 32.99 ? 300 LEU B CD1 1 ATOM 7120 C CD2 . LEU B 1 300 ? 43.585 36.636 7.293 1.00 31.86 ? 300 LEU B CD2 1 ATOM 7121 N N . GLY B 1 301 ? 44.518 38.467 11.859 1.00 26.31 ? 301 GLY B N 1 ATOM 7122 C CA . GLY B 1 301 ? 43.793 38.964 13.034 1.00 30.64 ? 301 GLY B CA 1 ATOM 7123 C C . GLY B 1 301 ? 44.075 40.411 13.403 1.00 30.81 ? 301 GLY B C 1 ATOM 7124 O O . GLY B 1 301 ? 43.165 41.218 13.598 1.00 33.66 ? 301 GLY B O 1 ATOM 7125 N N . ALA B 1 302 ? 45.350 40.780 13.478 1.00 34.46 ? 302 ALA B N 1 ATOM 7126 C CA . ALA B 1 302 ? 45.718 42.153 13.850 1.00 29.17 ? 302 ALA B CA 1 ATOM 7127 C C . ALA B 1 302 ? 45.397 43.148 12.781 1.00 29.00 ? 302 ALA B C 1 ATOM 7128 O O . ALA B 1 302 ? 44.971 44.266 13.067 1.00 25.57 ? 302 ALA B O 1 ATOM 7129 C CB . ALA B 1 302 ? 47.207 42.221 14.167 1.00 34.57 ? 302 ALA B CB 1 ATOM 7130 N N . PHE B 1 303 ? 45.650 42.760 11.522 1.00 27.64 ? 303 PHE B N 1 ATOM 7131 C CA . PHE B 1 303 ? 45.240 43.546 10.377 1.00 24.92 ? 303 PHE B CA 1 ATOM 7132 C C . PHE B 1 303 ? 43.742 43.908 10.525 1.00 20.87 ? 303 PHE B C 1 ATOM 7133 O O . PHE B 1 303 ? 43.338 45.070 10.394 1.00 23.56 ? 303 PHE B O 1 ATOM 7134 C CB . PHE B 1 303 ? 45.495 42.796 9.041 1.00 26.92 ? 303 PHE B CB 1 ATOM 7135 C CG . PHE B 1 303 ? 44.872 43.458 7.824 1.00 26.62 ? 303 PHE B CG 1 ATOM 7136 C CD1 . PHE B 1 303 ? 45.563 44.437 7.111 1.00 28.16 ? 303 PHE B CD1 1 ATOM 7137 C CD2 . PHE B 1 303 ? 43.591 43.161 7.431 1.00 27.02 ? 303 PHE B CD2 1 ATOM 7138 C CE1 . PHE B 1 303 ? 44.993 45.077 6.022 1.00 27.74 ? 303 PHE B CE1 1 ATOM 7139 C CE2 . PHE B 1 303 ? 43.009 43.803 6.346 1.00 24.36 ? 303 PHE B CE2 1 ATOM 7140 C CZ . PHE B 1 303 ? 43.691 44.739 5.636 1.00 25.08 ? 303 PHE B CZ 1 ATOM 7141 N N . ILE B 1 304 ? 42.926 42.926 10.817 1.00 24.16 ? 304 ILE B N 1 ATOM 7142 C CA . ILE B 1 304 ? 41.450 43.187 10.923 1.00 24.39 ? 304 ILE B CA 1 ATOM 7143 C C . ILE B 1 304 ? 41.138 44.187 12.036 1.00 24.79 ? 304 ILE B C 1 ATOM 7144 O O . ILE B 1 304 ? 40.352 45.164 11.851 1.00 24.38 ? 304 ILE B O 1 ATOM 7145 C CB . ILE B 1 304 ? 40.638 41.879 11.032 1.00 25.15 ? 304 ILE B CB 1 ATOM 7146 C CG1 . ILE B 1 304 ? 40.746 41.131 9.699 1.00 25.77 ? 304 ILE B CG1 1 ATOM 7147 C CG2 . ILE B 1 304 ? 39.178 42.156 11.325 1.00 26.20 ? 304 ILE B CG2 1 ATOM 7148 C CD1 . ILE B 1 304 ? 40.152 39.747 9.673 1.00 26.89 ? 304 ILE B CD1 1 ATOM 7149 N N . GLN B 1 305 ? 41.802 44.016 13.171 1.00 26.20 ? 305 GLN B N 1 ATOM 7150 C CA . GLN B 1 305 ? 41.568 44.912 14.304 1.00 26.58 ? 305 GLN B CA 1 ATOM 7151 C C . GLN B 1 305 ? 41.941 46.282 13.971 1.00 23.78 ? 305 GLN B C 1 ATOM 7152 O O . GLN B 1 305 ? 41.254 47.233 14.316 1.00 28.24 ? 305 GLN B O 1 ATOM 7153 C CB . GLN B 1 305 ? 42.329 44.445 15.550 1.00 28.82 ? 305 GLN B CB 1 ATOM 7154 C CG . GLN B 1 305 ? 41.858 43.109 15.994 1.00 28.94 ? 305 GLN B CG 1 ATOM 7155 C CD . GLN B 1 305 ? 42.526 42.699 17.286 1.00 29.38 ? 305 GLN B CD 1 ATOM 7156 O OE1 . GLN B 1 305 ? 43.559 43.254 17.674 1.00 30.03 ? 305 GLN B OE1 1 ATOM 7157 N NE2 . GLN B 1 305 ? 41.991 41.687 17.918 1.00 30.44 ? 305 GLN B NE2 1 ATOM 7158 N N . ILE B 1 306 ? 43.048 46.438 13.253 1.00 28.18 ? 306 ILE B N 1 ATOM 7159 C CA . ILE B 1 306 ? 43.539 47.794 12.994 1.00 24.45 ? 306 ILE B CA 1 ATOM 7160 C C . ILE B 1 306 ? 42.709 48.563 12.038 1.00 22.67 ? 306 ILE B C 1 ATOM 7161 O O . ILE B 1 306 ? 42.366 49.733 12.260 1.00 27.10 ? 306 ILE B O 1 ATOM 7162 C CB . ILE B 1 306 ? 45.052 47.753 12.600 1.00 30.85 ? 306 ILE B CB 1 ATOM 7163 C CG1 . ILE B 1 306 ? 45.903 47.298 13.828 1.00 32.65 ? 306 ILE B CG1 1 ATOM 7164 C CG2 . ILE B 1 306 ? 45.496 49.112 12.059 1.00 28.88 ? 306 ILE B CG2 1 ATOM 7165 C CD1 . ILE B 1 306 ? 47.278 46.746 13.464 1.00 35.91 ? 306 ILE B CD1 1 ATOM 7166 N N . ILE B 1 307 ? 42.397 47.932 10.917 1.00 25.39 ? 307 ILE B N 1 ATOM 7167 C CA . ILE B 1 307 ? 41.545 48.587 9.925 1.00 21.23 ? 307 ILE B CA 1 ATOM 7168 C C . ILE B 1 307 ? 40.205 48.911 10.578 1.00 19.72 ? 307 ILE B C 1 ATOM 7169 O O . ILE B 1 307 ? 39.644 49.999 10.449 1.00 17.18 ? 307 ILE B O 1 ATOM 7170 C CB . ILE B 1 307 ? 41.325 47.678 8.694 1.00 23.80 ? 307 ILE B CB 1 ATOM 7171 C CG1 . ILE B 1 307 ? 42.655 47.276 8.054 1.00 25.72 ? 307 ILE B CG1 1 ATOM 7172 C CG2 . ILE B 1 307 ? 40.413 48.384 7.694 1.00 23.48 ? 307 ILE B CG2 1 ATOM 7173 C CD1 . ILE B 1 307 ? 43.376 48.462 7.445 1.00 27.68 ? 307 ILE B CD1 1 ATOM 7174 N N . THR B 1 308 ? 39.704 47.999 11.357 1.00 20.88 ? 308 THR B N 1 ATOM 7175 C CA . THR B 1 308 ? 38.394 48.288 12.016 1.00 22.94 ? 308 THR B CA 1 ATOM 7176 C C . THR B 1 308 ? 38.436 49.466 12.957 1.00 21.67 ? 308 THR B C 1 ATOM 7177 O O . THR B 1 308 ? 37.634 50.413 12.828 1.00 23.34 ? 308 THR B O 1 ATOM 7178 C CB . THR B 1 308 ? 37.909 47.053 12.742 1.00 24.57 ? 308 THR B CB 1 ATOM 7179 O OG1 . THR B 1 308 ? 37.894 45.958 11.827 1.00 22.41 ? 308 THR B OG1 1 ATOM 7180 C CG2 . THR B 1 308 ? 36.523 47.271 13.321 1.00 25.54 ? 308 THR B CG2 1 ATOM 7181 N N . PHE B 1 309 ? 39.378 49.440 13.910 1.00 24.74 ? 309 PHE B N 1 ATOM 7182 C CA . PHE B 1 309 ? 39.448 50.497 14.958 1.00 24.90 ? 309 PHE B CA 1 ATOM 7183 C C . PHE B 1 309 ? 40.078 51.828 14.501 1.00 24.95 ? 309 PHE B C 1 ATOM 7184 O O . PHE B 1 309 ? 39.535 52.889 14.790 1.00 24.83 ? 309 PHE B O 1 ATOM 7185 C CB . PHE B 1 309 ? 40.089 49.957 16.244 1.00 25.55 ? 309 PHE B CB 1 ATOM 7186 C CG . PHE B 1 309 ? 39.134 49.165 17.093 1.00 24.87 ? 309 PHE B CG 1 ATOM 7187 C CD1 . PHE B 1 309 ? 38.741 47.914 16.696 1.00 24.24 ? 309 PHE B CD1 1 ATOM 7188 C CD2 . PHE B 1 309 ? 38.561 49.709 18.234 1.00 24.56 ? 309 PHE B CD2 1 ATOM 7189 C CE1 . PHE B 1 309 ? 37.859 47.166 17.485 1.00 26.04 ? 309 PHE B CE1 1 ATOM 7190 C CE2 . PHE B 1 309 ? 37.671 48.984 19.024 1.00 25.87 ? 309 PHE B CE2 1 ATOM 7191 C CZ . PHE B 1 309 ? 37.327 47.705 18.662 1.00 24.22 ? 309 PHE B CZ 1 ATOM 7192 N N . ARG B 1 310 ? 41.091 51.803 13.664 1.00 27.24 ? 310 ARG B N 1 ATOM 7193 C CA . ARG B 1 310 ? 41.709 53.051 13.194 1.00 27.33 ? 310 ARG B CA 1 ATOM 7194 C C . ARG B 1 310 ? 40.909 53.690 12.081 1.00 27.89 ? 310 ARG B C 1 ATOM 7195 O O . ARG B 1 310 ? 40.676 54.922 12.072 1.00 26.95 ? 310 ARG B O 1 ATOM 7196 C CB . ARG B 1 310 ? 43.164 52.747 12.723 1.00 33.68 ? 310 ARG B CB 1 ATOM 7197 C CG . ARG B 1 310 ? 43.993 53.976 12.265 1.00 37.14 ? 310 ARG B CG 1 ATOM 7198 C CD . ARG B 1 310 ? 45.276 53.551 11.563 1.00 37.73 ? 310 ARG B CD 1 ATOM 7199 N NE . ARG B 1 310 ? 44.960 52.976 10.261 1.00 38.07 ? 310 ARG B NE 1 ATOM 7200 C CZ . ARG B 1 310 ? 45.695 52.075 9.606 1.00 36.87 ? 310 ARG B CZ 1 ATOM 7201 N NH1 . ARG B 1 310 ? 46.820 51.618 10.071 1.00 35.63 ? 310 ARG B NH1 1 ATOM 7202 N NH2 . ARG B 1 310 ? 45.268 51.604 8.453 1.00 40.52 ? 310 ARG B NH2 1 ATOM 7203 N N . ASP B 1 311 ? 40.446 52.901 11.100 1.00 29.83 ? 311 ASP B N 1 ATOM 7204 C CA . ASP B 1 311 ? 39.821 53.518 9.887 1.00 27.25 ? 311 ASP B CA 1 ATOM 7205 C C . ASP B 1 311 ? 38.301 53.488 9.874 1.00 26.73 ? 311 ASP B C 1 ATOM 7206 O O . ASP B 1 311 ? 37.639 54.480 9.584 1.00 26.04 ? 311 ASP B O 1 ATOM 7207 C CB . ASP B 1 311 ? 40.334 52.808 8.618 1.00 31.33 ? 311 ASP B CB 1 ATOM 7208 C CG . ASP B 1 311 ? 41.850 52.773 8.559 1.00 30.14 ? 311 ASP B CG 1 ATOM 7209 O OD1 . ASP B 1 311 ? 42.411 53.768 9.015 1.00 28.12 ? 311 ASP B OD1 1 ATOM 7210 O OD2 . ASP B 1 311 ? 42.449 51.752 8.118 1.00 28.51 ? 311 ASP B OD2 1 ATOM 7211 N N . TYR B 1 312 ? 37.740 52.338 10.226 1.00 24.42 ? 312 TYR B N 1 ATOM 7212 C CA . TYR B 1 312 ? 36.304 52.152 10.101 1.00 21.64 ? 312 TYR B CA 1 ATOM 7213 C C . TYR B 1 312 ? 35.417 52.823 11.172 1.00 18.04 ? 312 TYR B C 1 ATOM 7214 O O . TYR B 1 312 ? 34.491 53.560 10.857 1.00 17.75 ? 312 TYR B O 1 ATOM 7215 C CB . TYR B 1 312 ? 36.020 50.600 10.004 1.00 23.00 ? 312 TYR B CB 1 ATOM 7216 C CG . TYR B 1 312 ? 34.545 50.276 9.874 1.00 22.86 ? 312 TYR B CG 1 ATOM 7217 C CD1 . TYR B 1 312 ? 33.866 50.508 8.693 1.00 21.66 ? 312 TYR B CD1 1 ATOM 7218 C CD2 . TYR B 1 312 ? 33.853 49.655 10.923 1.00 26.88 ? 312 TYR B CD2 1 ATOM 7219 C CE1 . TYR B 1 312 ? 32.504 50.205 8.567 1.00 22.06 ? 312 TYR B CE1 1 ATOM 7220 C CE2 . TYR B 1 312 ? 32.497 49.334 10.815 1.00 22.69 ? 312 TYR B CE2 1 ATOM 7221 C CZ . TYR B 1 312 ? 31.832 49.632 9.648 1.00 22.31 ? 312 TYR B CZ 1 ATOM 7222 O OH . TYR B 1 312 ? 30.536 49.319 9.549 1.00 19.91 ? 312 TYR B OH 1 ATOM 7223 N N . LEU B 1 313 ? 35.650 52.524 12.440 1.00 20.07 ? 313 LEU B N 1 ATOM 7224 C CA . LEU B 1 313 ? 34.735 52.994 13.524 1.00 20.39 ? 313 LEU B CA 1 ATOM 7225 C C . LEU B 1 313 ? 34.690 54.494 13.639 1.00 22.80 ? 313 LEU B C 1 ATOM 7226 O O . LEU B 1 313 ? 33.598 55.089 13.837 1.00 24.39 ? 313 LEU B O 1 ATOM 7227 C CB . LEU B 1 313 ? 35.123 52.361 14.815 1.00 24.16 ? 313 LEU B CB 1 ATOM 7228 C CG . LEU B 1 313 ? 35.022 50.831 14.912 1.00 22.28 ? 313 LEU B CG 1 ATOM 7229 C CD1 . LEU B 1 313 ? 35.627 50.378 16.235 1.00 25.67 ? 313 LEU B CD1 1 ATOM 7230 C CD2 . LEU B 1 313 ? 33.562 50.398 14.868 1.00 21.61 ? 313 LEU B CD2 1 ATOM 7231 N N . PRO B 1 314 ? 35.822 55.160 13.349 1.00 23.47 ? 314 PRO B N 1 ATOM 7232 C CA . PRO B 1 314 ? 35.734 56.649 13.412 1.00 23.22 ? 314 PRO B CA 1 ATOM 7233 C C . PRO B 1 314 ? 34.779 57.179 12.393 1.00 24.00 ? 314 PRO B C 1 ATOM 7234 O O . PRO B 1 314 ? 34.178 58.224 12.598 1.00 24.43 ? 314 PRO B O 1 ATOM 7235 C CB . PRO B 1 314 ? 37.155 57.092 13.148 1.00 23.97 ? 314 PRO B CB 1 ATOM 7236 C CG . PRO B 1 314 ? 38.004 55.951 13.718 1.00 25.42 ? 314 PRO B CG 1 ATOM 7237 C CD . PRO B 1 314 ? 37.226 54.683 13.372 1.00 25.96 ? 314 PRO B CD 1 ATOM 7238 N N . ILE B 1 315 ? 34.574 56.445 11.297 1.00 23.18 ? 315 ILE B N 1 ATOM 7239 C CA . ILE B 1 315 ? 33.657 56.986 10.325 1.00 24.41 ? 315 ILE B CA 1 ATOM 7240 C C . ILE B 1 315 ? 32.224 56.510 10.516 1.00 22.12 ? 315 ILE B C 1 ATOM 7241 O O . ILE B 1 315 ? 31.330 57.146 10.022 1.00 26.69 ? 315 ILE B O 1 ATOM 7242 C CB . ILE B 1 315 ? 34.195 56.961 8.885 1.00 27.67 ? 315 ILE B CB 1 ATOM 7243 C CG1 . ILE B 1 315 ? 34.594 55.573 8.404 1.00 28.38 ? 315 ILE B CG1 1 ATOM 7244 C CG2 . ILE B 1 315 ? 35.437 57.834 8.837 1.00 28.77 ? 315 ILE B CG2 1 ATOM 7245 C CD1 . ILE B 1 315 ? 35.416 55.589 7.108 1.00 28.39 ? 315 ILE B CD1 1 ATOM 7246 N N . VAL B 1 316 ? 32.023 55.484 11.345 1.00 22.50 ? 316 VAL B N 1 ATOM 7247 C CA . VAL B 1 316 ? 30.710 55.111 11.789 1.00 22.50 ? 316 VAL B CA 1 ATOM 7248 C C . VAL B 1 316 ? 30.254 55.976 12.975 1.00 22.84 ? 316 VAL B C 1 ATOM 7249 O O . VAL B 1 316 ? 29.166 56.581 12.960 1.00 23.68 ? 316 VAL B O 1 ATOM 7250 C CB . VAL B 1 316 ? 30.705 53.611 12.180 1.00 23.58 ? 316 VAL B CB 1 ATOM 7251 C CG1 . VAL B 1 316 ? 29.401 53.210 12.808 1.00 21.27 ? 316 VAL B CG1 1 ATOM 7252 C CG2 . VAL B 1 316 ? 30.997 52.756 10.966 1.00 24.54 ? 316 VAL B CG2 1 ATOM 7253 N N . LEU B 1 317 ? 31.118 56.098 13.980 1.00 25.27 ? 317 LEU B N 1 ATOM 7254 C CA . LEU B 1 317 ? 30.762 56.793 15.191 1.00 24.85 ? 317 LEU B CA 1 ATOM 7255 C C . LEU B 1 317 ? 30.959 58.326 15.176 1.00 28.74 ? 317 LEU B C 1 ATOM 7256 O O . LEU B 1 317 ? 30.434 58.987 16.061 1.00 30.29 ? 317 LEU B O 1 ATOM 7257 C CB . LEU B 1 317 ? 31.538 56.197 16.372 1.00 25.07 ? 317 LEU B CB 1 ATOM 7258 C CG . LEU B 1 317 ? 31.205 54.725 16.592 1.00 21.03 ? 317 LEU B CG 1 ATOM 7259 C CD1 . LEU B 1 317 ? 32.048 54.145 17.708 1.00 20.11 ? 317 LEU B CD1 1 ATOM 7260 C CD2 . LEU B 1 317 ? 29.718 54.491 16.800 1.00 21.39 ? 317 LEU B CD2 1 ATOM 7261 N N . GLY B 1 318 ? 31.717 58.876 14.237 1.00 26.18 ? 318 GLY B N 1 ATOM 7262 C CA . GLY B 1 318 ? 31.906 60.314 14.173 1.00 29.61 ? 318 GLY B CA 1 ATOM 7263 C C . GLY B 1 318 ? 32.327 60.921 15.534 1.00 31.24 ? 318 GLY B C 1 ATOM 7264 O O . GLY B 1 318 ? 33.251 60.430 16.188 1.00 28.95 ? 318 GLY B O 1 ATOM 7265 N N . SER B 1 319 ? 31.571 61.934 15.977 1.00 36.97 ? 319 SER B N 1 ATOM 7266 C CA . SER B 1 319 ? 31.866 62.684 17.204 1.00 37.85 ? 319 SER B CA 1 ATOM 7267 C C . SER B 1 319 ? 31.750 61.841 18.455 1.00 43.37 ? 319 SER B C 1 ATOM 7268 O O . SER B 1 319 ? 32.226 62.249 19.511 1.00 44.58 ? 319 SER B O 1 ATOM 7269 C CB . SER B 1 319 ? 30.929 63.868 17.337 1.00 41.25 ? 319 SER B CB 1 ATOM 7270 O OG . SER B 1 319 ? 29.578 63.424 17.346 1.00 40.39 ? 319 SER B OG 1 ATOM 7271 N N . GLU B 1 320 ? 31.157 60.651 18.345 1.00 42.84 ? 320 GLU B N 1 ATOM 7272 C CA . GLU B 1 320 ? 30.969 59.770 19.503 1.00 36.72 ? 320 GLU B CA 1 ATOM 7273 C C . GLU B 1 320 ? 32.088 58.781 19.672 1.00 34.09 ? 320 GLU B C 1 ATOM 7274 O O . GLU B 1 320 ? 32.133 58.050 20.651 1.00 31.97 ? 320 GLU B O 1 ATOM 7275 C CB . GLU B 1 320 ? 29.648 59.029 19.388 1.00 38.29 ? 320 GLU B CB 1 ATOM 7276 C CG . GLU B 1 320 ? 28.451 59.914 19.096 1.00 40.66 ? 320 GLU B CG 1 ATOM 7277 C CD . GLU B 1 320 ? 27.891 60.497 20.352 1.00 47.61 ? 320 GLU B CD 1 ATOM 7278 O OE1 . GLU B 1 320 ? 27.128 59.789 21.054 1.00 53.03 ? 320 GLU B OE1 1 ATOM 7279 O OE2 . GLU B 1 320 ? 28.254 61.639 20.615 1.00 48.19 ? 320 GLU B OE2 1 ATOM 7280 N N . MET B 1 321 ? 33.022 58.762 18.724 1.00 36.62 ? 321 MET B N 1 ATOM 7281 C CA . MET B 1 321 ? 34.099 57.775 18.729 1.00 36.68 ? 321 MET B CA 1 ATOM 7282 C C . MET B 1 321 ? 34.819 57.801 20.090 1.00 39.34 ? 321 MET B C 1 ATOM 7283 O O . MET B 1 321 ? 34.837 56.798 20.819 1.00 36.47 ? 321 MET B O 1 ATOM 7284 C CB . MET B 1 321 ? 35.052 58.047 17.567 1.00 34.78 ? 321 MET B CB 1 ATOM 7285 C CG . MET B 1 321 ? 36.237 57.101 17.438 1.00 33.38 ? 321 MET B CG 1 ATOM 7286 S SD . MET B 1 321 ? 35.868 55.389 17.022 1.00 33.49 ? 321 MET B SD 1 ATOM 7287 C CE . MET B 1 321 ? 37.377 54.602 17.574 1.00 31.69 ? 321 MET B CE 1 ATOM 7288 N N . GLN B 1 322 ? 35.374 58.955 20.444 1.00 47.26 ? 322 GLN B N 1 ATOM 7289 C CA . GLN B 1 322 ? 36.213 59.058 21.669 1.00 50.76 ? 322 GLN B CA 1 ATOM 7290 C C . GLN B 1 322 ? 35.355 58.835 22.929 1.00 45.01 ? 322 GLN B C 1 ATOM 7291 O O . GLN B 1 322 ? 35.808 58.209 23.883 1.00 42.29 ? 322 GLN B O 1 ATOM 7292 C CB . GLN B 1 322 ? 36.945 60.407 21.724 1.00 61.56 ? 322 GLN B CB 1 ATOM 7293 C CG . GLN B 1 322 ? 38.386 60.292 22.233 1.00 72.29 ? 322 GLN B CG 1 ATOM 7294 C CD . GLN B 1 322 ? 39.393 60.208 21.099 1.00 75.90 ? 322 GLN B CD 1 ATOM 7295 O OE1 . GLN B 1 322 ? 39.710 61.216 20.456 1.00 84.36 ? 322 GLN B OE1 1 ATOM 7296 N NE2 . GLN B 1 322 ? 39.907 59.008 20.850 1.00 74.49 ? 322 GLN B NE2 1 ATOM 7297 N N . LYS B 1 323 ? 34.096 59.285 22.898 1.00 35.57 ? 323 LYS B N 1 ATOM 7298 C CA . LYS B 1 323 ? 33.201 59.019 24.003 1.00 35.08 ? 323 LYS B CA 1 ATOM 7299 C C . LYS B 1 323 ? 33.081 57.555 24.354 1.00 39.63 ? 323 LYS B C 1 ATOM 7300 O O . LYS B 1 323 ? 33.138 57.210 25.532 1.00 42.52 ? 323 LYS B O 1 ATOM 7301 C CB . LYS B 1 323 ? 31.820 59.588 23.718 1.00 40.03 ? 323 LYS B CB 1 ATOM 7302 C CG . LYS B 1 323 ? 30.720 59.081 24.618 1.00 39.46 ? 323 LYS B CG 1 ATOM 7303 C CD . LYS B 1 323 ? 29.499 59.979 24.516 1.00 42.50 ? 323 LYS B CD 1 ATOM 7304 C CE . LYS B 1 323 ? 28.403 59.416 25.408 1.00 46.68 ? 323 LYS B CE 1 ATOM 7305 N NZ . LYS B 1 323 ? 27.618 60.505 26.042 1.00 48.36 ? 323 LYS B NZ 1 ATOM 7306 N N . TRP B 1 324 ? 32.887 56.669 23.377 1.00 34.47 ? 324 TRP B N 1 ATOM 7307 C CA . TRP B 1 324 ? 32.661 55.244 23.722 1.00 35.89 ? 324 TRP B CA 1 ATOM 7308 C C . TRP B 1 324 ? 33.957 54.454 23.662 1.00 32.65 ? 324 TRP B C 1 ATOM 7309 O O . TRP B 1 324 ? 34.079 53.444 24.323 1.00 31.48 ? 324 TRP B O 1 ATOM 7310 C CB . TRP B 1 324 ? 31.579 54.560 22.808 1.00 35.78 ? 324 TRP B CB 1 ATOM 7311 C CG . TRP B 1 324 ? 30.308 55.281 22.869 1.00 33.78 ? 324 TRP B CG 1 ATOM 7312 C CD1 . TRP B 1 324 ? 29.872 56.260 22.010 1.00 34.85 ? 324 TRP B CD1 1 ATOM 7313 C CD2 . TRP B 1 324 ? 29.360 55.219 23.911 1.00 30.95 ? 324 TRP B CD2 1 ATOM 7314 N NE1 . TRP B 1 324 ? 28.670 56.765 22.451 1.00 33.85 ? 324 TRP B NE1 1 ATOM 7315 C CE2 . TRP B 1 324 ? 28.347 56.139 23.618 1.00 29.40 ? 324 TRP B CE2 1 ATOM 7316 C CE3 . TRP B 1 324 ? 29.268 54.478 25.075 1.00 33.71 ? 324 TRP B CE3 1 ATOM 7317 C CZ2 . TRP B 1 324 ? 27.250 56.319 24.444 1.00 33.31 ? 324 TRP B CZ2 1 ATOM 7318 C CZ3 . TRP B 1 324 ? 28.173 54.646 25.881 1.00 33.33 ? 324 TRP B CZ3 1 ATOM 7319 C CH2 . TRP B 1 324 ? 27.176 55.560 25.554 1.00 31.04 ? 324 TRP B CH2 1 ATOM 7320 N N . ILE B 1 325 ? 34.917 54.905 22.846 1.00 34.65 ? 325 ILE B N 1 ATOM 7321 C CA . ILE B 1 325 ? 36.139 54.139 22.647 1.00 38.17 ? 325 ILE B CA 1 ATOM 7322 C C . ILE B 1 325 ? 37.311 55.093 22.841 1.00 47.00 ? 325 ILE B C 1 ATOM 7323 O O . ILE B 1 325 ? 37.958 55.527 21.876 1.00 47.80 ? 325 ILE B O 1 ATOM 7324 C CB . ILE B 1 325 ? 36.226 53.409 21.266 1.00 41.25 ? 325 ILE B CB 1 ATOM 7325 C CG1 . ILE B 1 325 ? 34.910 52.670 20.932 1.00 40.87 ? 325 ILE B CG1 1 ATOM 7326 C CG2 . ILE B 1 325 ? 37.356 52.381 21.279 1.00 42.11 ? 325 ILE B CG2 1 ATOM 7327 C CD1 . ILE B 1 325 ? 34.892 52.008 19.569 1.00 38.13 ? 325 ILE B CD1 1 ATOM 7328 N N . PRO B 1 326 ? 37.599 55.409 24.117 1.00 45.77 ? 326 PRO B N 1 ATOM 7329 C CA . PRO B 1 326 ? 38.744 56.244 24.439 1.00 43.24 ? 326 PRO B CA 1 ATOM 7330 C C . PRO B 1 326 ? 40.038 55.451 24.248 1.00 44.09 ? 326 PRO B C 1 ATOM 7331 O O . PRO B 1 326 ? 40.008 54.190 24.102 1.00 40.43 ? 326 PRO B O 1 ATOM 7332 C CB . PRO B 1 326 ? 38.513 56.592 25.910 1.00 41.56 ? 326 PRO B CB 1 ATOM 7333 C CG . PRO B 1 326 ? 37.832 55.381 26.447 1.00 44.52 ? 326 PRO B CG 1 ATOM 7334 C CD . PRO B 1 326 ? 36.930 54.906 25.328 1.00 43.15 ? 326 PRO B CD 1 ATOM 7335 N N . PRO B 1 327 ? 41.188 56.165 24.265 1.00 47.66 ? 327 PRO B N 1 ATOM 7336 C CA . PRO B 1 327 ? 42.469 55.520 23.980 1.00 44.48 ? 327 PRO B CA 1 ATOM 7337 C C . PRO B 1 327 ? 42.666 54.298 24.848 1.00 41.21 ? 327 PRO B C 1 ATOM 7338 O O . PRO B 1 327 ? 42.197 54.259 25.996 1.00 48.30 ? 327 PRO B O 1 ATOM 7339 C CB . PRO B 1 327 ? 43.474 56.621 24.268 1.00 46.58 ? 327 PRO B CB 1 ATOM 7340 C CG . PRO B 1 327 ? 42.728 57.884 23.948 1.00 47.98 ? 327 PRO B CG 1 ATOM 7341 C CD . PRO B 1 327 ? 41.333 57.627 24.422 1.00 46.57 ? 327 PRO B CD 1 ATOM 7342 N N . TYR B 1 328 ? 43.286 53.281 24.276 1.00 38.98 ? 328 TYR B N 1 ATOM 7343 C CA . TYR B 1 328 ? 43.397 51.977 24.913 1.00 37.36 ? 328 TYR B CA 1 ATOM 7344 C C . TYR B 1 328 ? 44.302 52.091 26.121 1.00 42.31 ? 328 TYR B C 1 ATOM 7345 O O . TYR B 1 328 ? 45.238 52.849 26.057 1.00 47.72 ? 328 TYR B O 1 ATOM 7346 C CB . TYR B 1 328 ? 44.084 51.071 23.941 1.00 35.20 ? 328 TYR B CB 1 ATOM 7347 C CG . TYR B 1 328 ? 44.265 49.646 24.369 1.00 33.48 ? 328 TYR B CG 1 ATOM 7348 C CD1 . TYR B 1 328 ? 43.192 48.884 24.777 1.00 30.80 ? 328 TYR B CD1 1 ATOM 7349 C CD2 . TYR B 1 328 ? 45.524 49.032 24.315 1.00 31.48 ? 328 TYR B CD2 1 ATOM 7350 C CE1 . TYR B 1 328 ? 43.374 47.559 25.127 1.00 29.97 ? 328 TYR B CE1 1 ATOM 7351 C CE2 . TYR B 1 328 ? 45.691 47.687 24.649 1.00 28.40 ? 328 TYR B CE2 1 ATOM 7352 C CZ . TYR B 1 328 ? 44.629 46.969 25.049 1.00 27.93 ? 328 TYR B CZ 1 ATOM 7353 O OH . TYR B 1 328 ? 44.766 45.645 25.372 1.00 32.78 ? 328 TYR B OH 1 ATOM 7354 N N . GLN B 1 329 ? 44.038 51.314 27.170 1.00 43.10 ? 329 GLN B N 1 ATOM 7355 C CA . GLN B 1 329 ? 44.843 51.255 28.391 1.00 43.08 ? 329 GLN B CA 1 ATOM 7356 C C . GLN B 1 329 ? 45.138 49.829 28.773 1.00 39.60 ? 329 GLN B C 1 ATOM 7357 O O . GLN B 1 329 ? 45.429 49.550 29.921 1.00 47.88 ? 329 GLN B O 1 ATOM 7358 C CB . GLN B 1 329 ? 44.100 51.863 29.611 1.00 41.77 ? 329 GLN B CB 1 ATOM 7359 C CG . GLN B 1 329 ? 43.456 53.225 29.417 1.00 45.56 ? 329 GLN B CG 1 ATOM 7360 C CD . GLN B 1 329 ? 44.430 54.327 29.084 1.00 54.34 ? 329 GLN B CD 1 ATOM 7361 O OE1 . GLN B 1 329 ? 44.033 55.399 28.599 1.00 63.58 ? 329 GLN B OE1 1 ATOM 7362 N NE2 . GLN B 1 329 ? 45.717 54.085 29.329 1.00 61.31 ? 329 GLN B NE2 1 ATOM 7363 N N . GLY B 1 330 ? 44.997 48.898 27.860 1.00 39.24 ? 330 GLY B N 1 ATOM 7364 C CA . GLY B 1 330 ? 45.413 47.535 28.135 1.00 36.14 ? 330 GLY B CA 1 ATOM 7365 C C . GLY B 1 330 ? 44.261 46.608 28.441 1.00 32.30 ? 330 GLY B C 1 ATOM 7366 O O . GLY B 1 330 ? 43.148 47.022 28.652 1.00 37.83 ? 330 GLY B O 1 ATOM 7367 N N . TYR B 1 331 ? 44.577 45.342 28.492 1.00 30.72 ? 331 TYR B N 1 ATOM 7368 C CA . TYR B 1 331 ? 43.616 44.328 28.664 1.00 36.44 ? 331 TYR B CA 1 ATOM 7369 C C . TYR B 1 331 ? 43.052 44.456 30.047 1.00 40.97 ? 331 TYR B C 1 ATOM 7370 O O . TYR B 1 331 ? 43.800 44.537 31.019 1.00 39.40 ? 331 TYR B O 1 ATOM 7371 C CB . TYR B 1 331 ? 44.289 42.984 28.479 1.00 34.76 ? 331 TYR B CB 1 ATOM 7372 C CG . TYR B 1 331 ? 43.462 41.779 28.853 1.00 38.59 ? 331 TYR B CG 1 ATOM 7373 C CD1 . TYR B 1 331 ? 42.212 41.540 28.272 1.00 38.02 ? 331 TYR B CD1 1 ATOM 7374 C CD2 . TYR B 1 331 ? 43.936 40.851 29.757 1.00 36.60 ? 331 TYR B CD2 1 ATOM 7375 C CE1 . TYR B 1 331 ? 41.488 40.403 28.589 1.00 38.57 ? 331 TYR B CE1 1 ATOM 7376 C CE2 . TYR B 1 331 ? 43.211 39.714 30.072 1.00 40.39 ? 331 TYR B CE2 1 ATOM 7377 C CZ . TYR B 1 331 ? 41.985 39.489 29.483 1.00 39.48 ? 331 TYR B CZ 1 ATOM 7378 O OH . TYR B 1 331 ? 41.252 38.349 29.822 1.00 39.18 ? 331 TYR B OH 1 ATOM 7379 N N . ASN B 1 332 ? 41.729 44.530 30.128 1.00 40.84 ? 332 ASN B N 1 ATOM 7380 C CA . ASN B 1 332 ? 41.043 44.440 31.416 1.00 38.03 ? 332 ASN B CA 1 ATOM 7381 C C . ASN B 1 332 ? 40.224 43.175 31.408 1.00 38.45 ? 332 ASN B C 1 ATOM 7382 O O . ASN B 1 332 ? 39.204 43.083 30.743 1.00 46.08 ? 332 ASN B O 1 ATOM 7383 C CB . ASN B 1 332 ? 40.246 45.716 31.713 1.00 40.02 ? 332 ASN B CB 1 ATOM 7384 C CG . ASN B 1 332 ? 39.440 45.617 32.994 1.00 40.03 ? 332 ASN B CG 1 ATOM 7385 O OD1 . ASN B 1 332 ? 39.340 44.555 33.569 1.00 37.41 ? 332 ASN B OD1 1 ATOM 7386 N ND2 . ASN B 1 332 ? 38.809 46.712 33.408 1.00 47.01 ? 332 ASN B ND2 1 ATOM 7387 N N . ASN B 1 333 ? 40.690 42.166 32.109 1.00 34.96 ? 333 ASN B N 1 ATOM 7388 C CA . ASN B 1 333 ? 39.941 40.945 32.225 1.00 36.30 ? 333 ASN B CA 1 ATOM 7389 C C . ASN B 1 333 ? 38.666 41.018 33.091 1.00 31.40 ? 333 ASN B C 1 ATOM 7390 O O . ASN B 1 333 ? 38.066 39.996 33.300 1.00 27.67 ? 333 ASN B O 1 ATOM 7391 C CB . ASN B 1 333 ? 40.823 39.805 32.730 1.00 39.87 ? 333 ASN B CB 1 ATOM 7392 C CG . ASN B 1 333 ? 40.964 39.786 34.243 1.00 41.05 ? 333 ASN B CG 1 ATOM 7393 O OD1 . ASN B 1 333 ? 40.988 40.816 34.902 1.00 48.53 ? 333 ASN B OD1 1 ATOM 7394 N ND2 . ASN B 1 333 ? 41.045 38.601 34.791 1.00 44.88 ? 333 ASN B ND2 1 ATOM 7395 N N . SER B 1 334 ? 38.257 42.183 33.586 1.00 30.28 ? 334 SER B N 1 ATOM 7396 C CA . SER B 1 334 ? 36.914 42.301 34.142 1.00 39.03 ? 334 SER B CA 1 ATOM 7397 C C . SER B 1 334 ? 35.866 42.651 33.077 1.00 41.28 ? 334 SER B C 1 ATOM 7398 O O . SER B 1 334 ? 34.696 42.670 33.378 1.00 40.25 ? 334 SER B O 1 ATOM 7399 C CB . SER B 1 334 ? 36.847 43.380 35.197 1.00 41.07 ? 334 SER B CB 1 ATOM 7400 O OG . SER B 1 334 ? 37.756 43.085 36.237 1.00 48.41 ? 334 SER B OG 1 ATOM 7401 N N . VAL B 1 335 ? 36.313 42.998 31.876 1.00 39.81 ? 335 VAL B N 1 ATOM 7402 C CA . VAL B 1 335 ? 35.414 43.409 30.820 1.00 40.01 ? 335 VAL B CA 1 ATOM 7403 C C . VAL B 1 335 ? 34.774 42.160 30.226 1.00 33.29 ? 335 VAL B C 1 ATOM 7404 O O . VAL B 1 335 ? 35.419 41.130 30.023 1.00 35.53 ? 335 VAL B O 1 ATOM 7405 C CB . VAL B 1 335 ? 36.112 44.306 29.785 1.00 39.46 ? 335 VAL B CB 1 ATOM 7406 C CG1 . VAL B 1 335 ? 35.182 44.546 28.588 1.00 43.37 ? 335 VAL B CG1 1 ATOM 7407 C CG2 . VAL B 1 335 ? 36.496 45.650 30.423 1.00 39.00 ? 335 VAL B CG2 1 ATOM 7408 N N . ASP B 1 336 ? 33.460 42.209 30.048 1.00 33.44 ? 336 ASP B N 1 ATOM 7409 C CA . ASP B 1 336 ? 32.743 41.129 29.311 1.00 31.35 ? 336 ASP B CA 1 ATOM 7410 C C . ASP B 1 336 ? 33.004 41.296 27.779 1.00 30.83 ? 336 ASP B C 1 ATOM 7411 O O . ASP B 1 336 ? 32.616 42.287 27.187 1.00 29.35 ? 336 ASP B O 1 ATOM 7412 C CB . ASP B 1 336 ? 31.255 41.233 29.613 1.00 30.34 ? 336 ASP B CB 1 ATOM 7413 C CG . ASP B 1 336 ? 30.441 40.141 28.948 1.00 30.58 ? 336 ASP B CG 1 ATOM 7414 O OD1 . ASP B 1 336 ? 30.967 39.227 28.283 1.00 28.07 ? 336 ASP B OD1 1 ATOM 7415 O OD2 . ASP B 1 336 ? 29.228 40.239 29.077 1.00 30.88 ? 336 ASP B OD2 1 ATOM 7416 N N . PRO B 1 337 ? 33.701 40.335 27.153 1.00 32.97 ? 337 PRO B N 1 ATOM 7417 C CA . PRO B 1 337 ? 33.964 40.490 25.726 1.00 36.18 ? 337 PRO B CA 1 ATOM 7418 C C . PRO B 1 337 ? 32.833 39.959 24.794 1.00 35.42 ? 337 PRO B C 1 ATOM 7419 O O . PRO B 1 337 ? 32.956 39.975 23.543 1.00 28.89 ? 337 PRO B O 1 ATOM 7420 C CB . PRO B 1 337 ? 35.196 39.628 25.543 1.00 35.49 ? 337 PRO B CB 1 ATOM 7421 C CG . PRO B 1 337 ? 34.972 38.501 26.464 1.00 37.09 ? 337 PRO B CG 1 ATOM 7422 C CD . PRO B 1 337 ? 34.345 39.136 27.684 1.00 34.75 ? 337 PRO B CD 1 ATOM 7423 N N . ARG B 1 338 ? 31.764 39.459 25.393 1.00 29.20 ? 338 ARG B N 1 ATOM 7424 C CA . ARG B 1 338 ? 30.774 38.773 24.636 1.00 27.07 ? 338 ARG B CA 1 ATOM 7425 C C . ARG B 1 338 ? 30.011 39.760 23.815 1.00 22.13 ? 338 ARG B C 1 ATOM 7426 O O . ARG B 1 338 ? 29.793 40.904 24.209 1.00 24.62 ? 338 ARG B O 1 ATOM 7427 C CB . ARG B 1 338 ? 29.848 38.019 25.539 1.00 27.68 ? 338 ARG B CB 1 ATOM 7428 C CG . ARG B 1 338 ? 30.440 36.758 26.139 1.00 29.01 ? 338 ARG B CG 1 ATOM 7429 C CD . ARG B 1 338 ? 29.475 36.152 27.162 1.00 28.96 ? 338 ARG B CD 1 ATOM 7430 N NE . ARG B 1 338 ? 29.106 37.210 28.083 1.00 30.66 ? 338 ARG B NE 1 ATOM 7431 C CZ . ARG B 1 338 ? 27.999 37.226 28.815 1.00 28.81 ? 338 ARG B CZ 1 ATOM 7432 N NH1 . ARG B 1 338 ? 27.146 36.225 28.789 1.00 28.86 ? 338 ARG B NH1 1 ATOM 7433 N NH2 . ARG B 1 338 ? 27.740 38.269 29.570 1.00 27.23 ? 338 ARG B NH2 1 ATOM 7434 N N . ILE B 1 339 ? 29.649 39.331 22.615 1.00 26.53 ? 339 ILE B N 1 ATOM 7435 C CA . ILE B 1 339 ? 28.750 40.155 21.778 1.00 25.48 ? 339 ILE B CA 1 ATOM 7436 C C . ILE B 1 339 ? 27.366 40.082 22.394 1.00 22.35 ? 339 ILE B C 1 ATOM 7437 O O . ILE B 1 339 ? 26.916 39.019 22.723 1.00 20.64 ? 339 ILE B O 1 ATOM 7438 C CB . ILE B 1 339 ? 28.654 39.656 20.340 1.00 25.34 ? 339 ILE B CB 1 ATOM 7439 C CG1 . ILE B 1 339 ? 30.023 39.704 19.686 1.00 24.86 ? 339 ILE B CG1 1 ATOM 7440 C CG2 . ILE B 1 339 ? 27.647 40.491 19.560 1.00 24.88 ? 339 ILE B CG2 1 ATOM 7441 C CD1 . ILE B 1 339 ? 30.701 41.058 19.697 1.00 24.47 ? 339 ILE B CD1 1 ATOM 7442 N N . SER B 1 340 ? 26.696 41.219 22.510 1.00 19.65 ? 340 SER B N 1 ATOM 7443 C CA . SER B 1 340 ? 25.330 41.215 23.024 1.00 20.46 ? 340 SER B CA 1 ATOM 7444 C C . SER B 1 340 ? 24.328 40.921 21.917 1.00 22.30 ? 340 SER B C 1 ATOM 7445 O O . SER B 1 340 ? 24.616 41.138 20.753 1.00 18.64 ? 340 SER B O 1 ATOM 7446 C CB . SER B 1 340 ? 25.020 42.560 23.596 1.00 21.14 ? 340 SER B CB 1 ATOM 7447 O OG . SER B 1 340 ? 25.194 43.591 22.643 1.00 21.83 ? 340 SER B OG 1 ATOM 7448 N N . ASN B 1 341 ? 23.143 40.450 22.325 1.00 19.79 ? 341 ASN B N 1 ATOM 7449 C CA . ASN B 1 341 ? 22.087 40.121 21.434 1.00 19.40 ? 341 ASN B CA 1 ATOM 7450 C C . ASN B 1 341 ? 21.637 41.417 20.678 1.00 19.38 ? 341 ASN B C 1 ATOM 7451 O O . ASN B 1 341 ? 21.504 41.410 19.429 1.00 18.10 ? 341 ASN B O 1 ATOM 7452 C CB . ASN B 1 341 ? 20.952 39.451 22.234 1.00 20.27 ? 341 ASN B CB 1 ATOM 7453 C CG . ASN B 1 341 ? 20.055 38.594 21.398 1.00 23.02 ? 341 ASN B CG 1 ATOM 7454 O OD1 . ASN B 1 341 ? 19.756 38.940 20.246 1.00 23.87 ? 341 ASN B OD1 1 ATOM 7455 N ND2 . ASN B 1 341 ? 19.555 37.495 21.963 1.00 24.98 ? 341 ASN B ND2 1 ATOM 7456 N N . VAL B 1 342 ? 21.503 42.531 21.399 1.00 18.01 ? 342 VAL B N 1 ATOM 7457 C CA . VAL B 1 342 ? 21.131 43.756 20.752 1.00 18.44 ? 342 VAL B CA 1 ATOM 7458 C C . VAL B 1 342 ? 22.130 44.261 19.665 1.00 17.66 ? 342 VAL B C 1 ATOM 7459 O O . VAL B 1 342 ? 21.698 44.851 18.651 1.00 14.67 ? 342 VAL B O 1 ATOM 7460 C CB . VAL B 1 342 ? 20.762 44.862 21.744 1.00 19.79 ? 342 VAL B CB 1 ATOM 7461 C CG1 . VAL B 1 342 ? 21.958 45.351 22.544 1.00 19.14 ? 342 VAL B CG1 1 ATOM 7462 C CG2 . VAL B 1 342 ? 20.065 45.982 20.996 1.00 20.04 ? 342 VAL B CG2 1 ATOM 7463 N N . PHE B 1 343 ? 23.414 44.034 19.880 1.00 15.84 ? 343 PHE B N 1 ATOM 7464 C CA . PHE B 1 343 ? 24.443 44.507 18.943 1.00 15.98 ? 343 PHE B CA 1 ATOM 7465 C C . PHE B 1 343 ? 24.259 43.835 17.582 1.00 17.44 ? 343 PHE B C 1 ATOM 7466 O O . PHE B 1 343 ? 24.547 44.411 16.535 1.00 19.63 ? 343 PHE B O 1 ATOM 7467 C CB . PHE B 1 343 ? 25.821 44.196 19.463 1.00 15.57 ? 343 PHE B CB 1 ATOM 7468 C CG . PHE B 1 343 ? 26.901 44.495 18.505 1.00 14.38 ? 343 PHE B CG 1 ATOM 7469 C CD1 . PHE B 1 343 ? 27.395 45.753 18.437 1.00 14.02 ? 343 PHE B CD1 1 ATOM 7470 C CD2 . PHE B 1 343 ? 27.486 43.474 17.757 1.00 14.66 ? 343 PHE B CD2 1 ATOM 7471 C CE1 . PHE B 1 343 ? 28.433 46.029 17.568 1.00 14.92 ? 343 PHE B CE1 1 ATOM 7472 C CE2 . PHE B 1 343 ? 28.558 43.718 16.918 1.00 16.07 ? 343 PHE B CE2 1 ATOM 7473 C CZ . PHE B 1 343 ? 29.006 45.035 16.791 1.00 15.43 ? 343 PHE B CZ 1 ATOM 7474 N N . THR B 1 344 ? 23.841 42.589 17.599 1.00 16.84 ? 344 THR B N 1 ATOM 7475 C CA . THR B 1 344 ? 23.621 41.896 16.351 1.00 15.87 ? 344 THR B CA 1 ATOM 7476 C C . THR B 1 344 ? 22.487 42.512 15.548 1.00 15.19 ? 344 THR B C 1 ATOM 7477 O O . THR B 1 344 ? 22.406 42.247 14.385 1.00 14.29 ? 344 THR B O 1 ATOM 7478 C CB . THR B 1 344 ? 23.344 40.414 16.529 1.00 16.30 ? 344 THR B CB 1 ATOM 7479 O OG1 . THR B 1 344 ? 21.970 40.226 16.918 1.00 17.85 ? 344 THR B OG1 1 ATOM 7480 C CG2 . THR B 1 344 ? 24.341 39.770 17.532 1.00 17.63 ? 344 THR B CG2 1 ATOM 7481 N N . PHE B 1 345 ? 21.610 43.295 16.175 1.00 15.91 ? 345 PHE B N 1 ATOM 7482 C CA . PHE B 1 345 ? 20.612 44.081 15.460 1.00 14.57 ? 345 PHE B CA 1 ATOM 7483 C C . PHE B 1 345 ? 21.112 45.481 15.128 1.00 15.44 ? 345 PHE B C 1 ATOM 7484 O O . PHE B 1 345 ? 20.824 46.016 14.051 1.00 12.15 ? 345 PHE B O 1 ATOM 7485 C CB . PHE B 1 345 ? 19.245 44.108 16.201 1.00 14.17 ? 345 PHE B CB 1 ATOM 7486 C CG . PHE B 1 345 ? 18.653 42.755 16.308 1.00 15.43 ? 345 PHE B CG 1 ATOM 7487 C CD1 . PHE B 1 345 ? 18.079 42.162 15.178 1.00 14.74 ? 345 PHE B CD1 1 ATOM 7488 C CD2 . PHE B 1 345 ? 18.833 42.003 17.457 1.00 15.25 ? 345 PHE B CD2 1 ATOM 7489 C CE1 . PHE B 1 345 ? 17.598 40.885 15.240 1.00 14.53 ? 345 PHE B CE1 1 ATOM 7490 C CE2 . PHE B 1 345 ? 18.365 40.701 17.532 1.00 15.64 ? 345 PHE B CE2 1 ATOM 7491 C CZ . PHE B 1 345 ? 17.748 40.140 16.406 1.00 15.32 ? 345 PHE B CZ 1 ATOM 7492 N N . ALA B 1 346 ? 21.840 46.066 16.054 1.00 16.42 ? 346 ALA B N 1 ATOM 7493 C CA . ALA B 1 346 ? 22.410 47.392 15.918 1.00 14.53 ? 346 ALA B CA 1 ATOM 7494 C C . ALA B 1 346 ? 23.359 47.491 14.763 1.00 14.51 ? 346 ALA B C 1 ATOM 7495 O O . ALA B 1 346 ? 23.303 48.455 13.997 1.00 17.43 ? 346 ALA B O 1 ATOM 7496 C CB . ALA B 1 346 ? 23.154 47.756 17.194 1.00 15.27 ? 346 ALA B CB 1 ATOM 7497 N N . PHE B 1 347 ? 24.117 46.444 14.542 1.00 14.57 ? 347 PHE B N 1 ATOM 7498 C CA . PHE B 1 347 ? 25.129 46.412 13.478 1.00 15.00 ? 347 PHE B CA 1 ATOM 7499 C C . PHE B 1 347 ? 24.477 46.189 12.091 1.00 15.04 ? 347 PHE B C 1 ATOM 7500 O O . PHE B 1 347 ? 25.200 46.249 11.078 1.00 15.43 ? 347 PHE B O 1 ATOM 7501 C CB . PHE B 1 347 ? 26.171 45.325 13.742 1.00 14.97 ? 347 PHE B CB 1 ATOM 7502 C CG . PHE B 1 347 ? 27.548 45.547 13.142 1.00 15.69 ? 347 PHE B CG 1 ATOM 7503 C CD1 . PHE B 1 347 ? 27.857 46.583 12.261 1.00 15.71 ? 347 PHE B CD1 1 ATOM 7504 C CD2 . PHE B 1 347 ? 28.571 44.668 13.497 1.00 17.74 ? 347 PHE B CD2 1 ATOM 7505 C CE1 . PHE B 1 347 ? 29.136 46.762 11.776 1.00 16.42 ? 347 PHE B CE1 1 ATOM 7506 C CE2 . PHE B 1 347 ? 29.878 44.823 13.007 1.00 18.05 ? 347 PHE B CE2 1 ATOM 7507 C CZ . PHE B 1 347 ? 30.170 45.856 12.128 1.00 15.98 ? 347 PHE B CZ 1 ATOM 7508 N N . ARG B 1 348 ? 23.161 45.914 12.080 1.00 14.95 ? 348 ARG B N 1 ATOM 7509 C CA . ARG B 1 348 ? 22.373 45.850 10.806 1.00 14.26 ? 348 ARG B CA 1 ATOM 7510 C C . ARG B 1 348 ? 21.993 47.198 10.228 1.00 13.87 ? 348 ARG B C 1 ATOM 7511 O O . ARG B 1 348 ? 21.215 47.296 9.254 1.00 14.90 ? 348 ARG B O 1 ATOM 7512 C CB . ARG B 1 348 ? 21.142 44.978 10.967 1.00 14.54 ? 348 ARG B CB 1 ATOM 7513 C CG . ARG B 1 348 ? 21.457 43.577 11.480 1.00 15.09 ? 348 ARG B CG 1 ATOM 7514 C CD . ARG B 1 348 ? 20.215 42.769 11.591 1.00 15.71 ? 348 ARG B CD 1 ATOM 7515 N NE . ARG B 1 348 ? 20.418 41.519 12.290 1.00 14.15 ? 348 ARG B NE 1 ATOM 7516 C CZ . ARG B 1 348 ? 19.702 40.411 12.141 1.00 16.24 ? 348 ARG B CZ 1 ATOM 7517 N NH1 . ARG B 1 348 ? 18.699 40.311 11.245 1.00 16.96 ? 348 ARG B NH1 1 ATOM 7518 N NH2 . ARG B 1 348 ? 20.028 39.358 12.902 1.00 15.91 ? 348 ARG B NH2 1 ATOM 7519 N N . PHE B 1 349 ? 22.494 48.259 10.833 1.00 15.13 ? 349 PHE B N 1 ATOM 7520 C CA . PHE B 1 349 ? 22.566 49.542 10.185 1.00 14.69 ? 349 PHE B CA 1 ATOM 7521 C C . PHE B 1 349 ? 23.181 49.445 8.803 1.00 14.92 ? 349 PHE B C 1 ATOM 7522 O O . PHE B 1 349 ? 22.761 50.196 7.907 1.00 15.83 ? 349 PHE B O 1 ATOM 7523 C CB . PHE B 1 349 ? 23.282 50.580 11.031 1.00 14.48 ? 349 PHE B CB 1 ATOM 7524 C CG . PHE B 1 349 ? 24.799 50.499 11.024 1.00 14.08 ? 349 PHE B CG 1 ATOM 7525 C CD1 . PHE B 1 349 ? 25.545 50.987 9.933 1.00 15.34 ? 349 PHE B CD1 1 ATOM 7526 C CD2 . PHE B 1 349 ? 25.483 50.016 12.130 1.00 13.78 ? 349 PHE B CD2 1 ATOM 7527 C CE1 . PHE B 1 349 ? 26.922 50.930 9.931 1.00 14.15 ? 349 PHE B CE1 1 ATOM 7528 C CE2 . PHE B 1 349 ? 26.840 49.932 12.122 1.00 13.50 ? 349 PHE B CE2 1 ATOM 7529 C CZ . PHE B 1 349 ? 27.578 50.408 11.020 1.00 14.74 ? 349 PHE B CZ 1 ATOM 7530 N N . GLY B 1 350 ? 24.056 48.460 8.609 1.00 16.10 ? 350 GLY B N 1 ATOM 7531 C CA . GLY B 1 350 ? 24.685 48.183 7.293 1.00 15.97 ? 350 GLY B CA 1 ATOM 7532 C C . GLY B 1 350 ? 23.688 47.994 6.161 1.00 17.23 ? 350 GLY B C 1 ATOM 7533 O O . GLY B 1 350 ? 23.974 48.313 5.018 1.00 18.32 ? 350 GLY B O 1 ATOM 7534 N N . HIS B 1 351 ? 22.513 47.452 6.487 1.00 15.51 ? 351 HIS B N 1 ATOM 7535 C CA . HIS B 1 351 ? 21.558 47.160 5.495 1.00 15.46 ? 351 HIS B CA 1 ATOM 7536 C C . HIS B 1 351 ? 21.051 48.381 4.772 1.00 15.81 ? 351 HIS B C 1 ATOM 7537 O O . HIS B 1 351 ? 20.676 48.271 3.665 1.00 14.82 ? 351 HIS B O 1 ATOM 7538 C CB . HIS B 1 351 ? 20.422 46.381 6.092 1.00 15.53 ? 351 HIS B CB 1 ATOM 7539 C CG . HIS B 1 351 ? 20.867 45.043 6.555 1.00 16.91 ? 351 HIS B CG 1 ATOM 7540 N ND1 . HIS B 1 351 ? 20.109 44.284 7.394 1.00 16.52 ? 351 HIS B ND1 1 ATOM 7541 C CD2 . HIS B 1 351 ? 22.014 44.357 6.333 1.00 17.75 ? 351 HIS B CD2 1 ATOM 7542 C CE1 . HIS B 1 351 ? 20.768 43.177 7.697 1.00 19.52 ? 351 HIS B CE1 1 ATOM 7543 N NE2 . HIS B 1 351 ? 21.940 43.190 7.070 1.00 20.80 ? 351 HIS B NE2 1 ATOM 7544 N N . MET B 1 352 ? 21.100 49.552 5.398 1.00 17.36 ? 352 MET B N 1 ATOM 7545 C CA . MET B 1 352 ? 20.685 50.792 4.758 1.00 18.19 ? 352 MET B CA 1 ATOM 7546 C C . MET B 1 352 ? 21.812 51.467 3.923 1.00 18.25 ? 352 MET B C 1 ATOM 7547 O O . MET B 1 352 ? 21.565 52.487 3.318 1.00 19.39 ? 352 MET B O 1 ATOM 7548 C CB . MET B 1 352 ? 20.109 51.743 5.801 1.00 18.22 ? 352 MET B CB 1 ATOM 7549 C CG . MET B 1 352 ? 19.065 51.048 6.643 1.00 20.87 ? 352 MET B CG 1 ATOM 7550 S SD . MET B 1 352 ? 18.035 52.246 7.435 1.00 21.82 ? 352 MET B SD 1 ATOM 7551 C CE . MET B 1 352 ? 16.930 51.012 8.199 1.00 19.76 ? 352 MET B CE 1 ATOM 7552 N N . GLU B 1 353 ? 23.013 50.897 3.913 1.00 17.81 ? 353 GLU B N 1 ATOM 7553 C CA . GLU B 1 353 ? 24.197 51.417 3.201 1.00 17.34 ? 353 GLU B CA 1 ATOM 7554 C C . GLU B 1 353 ? 24.516 50.619 1.929 1.00 18.98 ? 353 GLU B C 1 ATOM 7555 O O . GLU B 1 353 ? 25.562 50.845 1.265 1.00 17.29 ? 353 GLU B O 1 ATOM 7556 C CB . GLU B 1 353 ? 25.452 51.315 4.089 1.00 15.50 ? 353 GLU B CB 1 ATOM 7557 C CG . GLU B 1 353 ? 25.360 52.219 5.327 1.00 15.11 ? 353 GLU B CG 1 ATOM 7558 C CD . GLU B 1 353 ? 26.537 52.042 6.296 1.00 15.44 ? 353 GLU B CD 1 ATOM 7559 O OE1 . GLU B 1 353 ? 27.411 51.185 6.100 1.00 13.92 ? 353 GLU B OE1 1 ATOM 7560 O OE2 . GLU B 1 353 ? 26.586 52.810 7.304 1.00 15.57 ? 353 GLU B OE2 1 ATOM 7561 N N . VAL B 1 354 ? 23.678 49.632 1.661 1.00 15.38 ? 354 VAL B N 1 ATOM 7562 C CA . VAL B 1 354 ? 23.873 48.758 0.511 1.00 15.33 ? 354 VAL B CA 1 ATOM 7563 C C . VAL B 1 354 ? 23.121 49.352 -0.684 1.00 14.58 ? 354 VAL B C 1 ATOM 7564 O O . VAL B 1 354 ? 21.907 49.479 -0.625 1.00 13.70 ? 354 VAL B O 1 ATOM 7565 C CB . VAL B 1 354 ? 23.313 47.381 0.777 1.00 14.63 ? 354 VAL B CB 1 ATOM 7566 C CG1 . VAL B 1 354 ? 23.407 46.556 -0.499 1.00 16.51 ? 354 VAL B CG1 1 ATOM 7567 C CG2 . VAL B 1 354 ? 24.046 46.693 1.930 1.00 14.03 ? 354 VAL B CG2 1 ATOM 7568 N N . PRO B 1 355 ? 23.844 49.691 -1.778 1.00 14.66 ? 355 PRO B N 1 ATOM 7569 C CA . PRO B 1 355 ? 23.178 50.312 -2.942 1.00 17.04 ? 355 PRO B CA 1 ATOM 7570 C C . PRO B 1 355 ? 22.632 49.268 -3.904 1.00 16.36 ? 355 PRO B C 1 ATOM 7571 O O . PRO B 1 355 ? 22.788 48.075 -3.666 1.00 15.34 ? 355 PRO B O 1 ATOM 7572 C CB . PRO B 1 355 ? 24.318 51.108 -3.587 1.00 16.78 ? 355 PRO B CB 1 ATOM 7573 C CG . PRO B 1 355 ? 25.481 50.234 -3.362 1.00 16.32 ? 355 PRO B CG 1 ATOM 7574 C CD . PRO B 1 355 ? 25.271 49.521 -2.051 1.00 16.03 ? 355 PRO B CD 1 ATOM 7575 N N . SER B 1 356 ? 21.917 49.694 -4.948 1.00 18.53 ? 356 SER B N 1 ATOM 7576 C CA . SER B 1 356 ? 21.087 48.780 -5.742 1.00 16.64 ? 356 SER B CA 1 ATOM 7577 C C . SER B 1 356 ? 21.878 48.024 -6.799 1.00 16.73 ? 356 SER B C 1 ATOM 7578 O O . SER B 1 356 ? 21.345 47.049 -7.360 1.00 17.57 ? 356 SER B O 1 ATOM 7579 C CB . SER B 1 356 ? 19.957 49.543 -6.456 1.00 17.91 ? 356 SER B CB 1 ATOM 7580 O OG . SER B 1 356 ? 20.520 50.460 -7.402 1.00 20.80 ? 356 SER B OG 1 ATOM 7581 N N . THR B 1 357 ? 23.121 48.429 -7.046 1.00 16.93 ? 357 THR B N 1 ATOM 7582 C CA . THR B 1 357 ? 23.983 47.826 -8.072 1.00 18.01 ? 357 THR B CA 1 ATOM 7583 C C . THR B 1 357 ? 25.389 47.620 -7.646 1.00 19.23 ? 357 THR B C 1 ATOM 7584 O O . THR B 1 357 ? 25.874 48.250 -6.690 1.00 20.47 ? 357 THR B O 1 ATOM 7585 C CB . THR B 1 357 ? 24.047 48.673 -9.404 1.00 20.32 ? 357 THR B CB 1 ATOM 7586 O OG1 . THR B 1 357 ? 24.902 49.809 -9.235 1.00 18.52 ? 357 THR B OG1 1 ATOM 7587 C CG2 . THR B 1 357 ? 22.639 49.124 -9.842 1.00 19.45 ? 357 THR B CG2 1 ATOM 7588 N N . VAL B 1 358 ? 26.079 46.759 -8.402 1.00 19.93 ? 358 VAL B N 1 ATOM 7589 C CA . VAL B 1 358 ? 27.496 46.455 -8.213 1.00 18.08 ? 358 VAL B CA 1 ATOM 7590 C C . VAL B 1 358 ? 28.164 46.485 -9.595 1.00 21.27 ? 358 VAL B C 1 ATOM 7591 O O . VAL B 1 358 ? 27.583 45.966 -10.587 1.00 18.05 ? 358 VAL B O 1 ATOM 7592 C CB . VAL B 1 358 ? 27.697 45.063 -7.632 1.00 19.52 ? 358 VAL B CB 1 ATOM 7593 C CG1 . VAL B 1 358 ? 29.154 44.621 -7.767 1.00 19.01 ? 358 VAL B CG1 1 ATOM 7594 C CG2 . VAL B 1 358 ? 27.229 44.983 -6.163 1.00 21.08 ? 358 VAL B CG2 1 ATOM 7595 N N . SER B 1 359 ? 29.346 47.118 -9.696 1.00 22.46 ? 359 SER B N 1 ATOM 7596 C CA . SER B 1 359 ? 29.960 47.333 -11.052 1.00 20.83 ? 359 SER B CA 1 ATOM 7597 C C . SER B 1 359 ? 31.244 46.630 -11.165 1.00 22.88 ? 359 SER B C 1 ATOM 7598 O O . SER B 1 359 ? 31.985 46.431 -10.161 1.00 23.82 ? 359 SER B O 1 ATOM 7599 C CB . SER B 1 359 ? 30.203 48.805 -11.368 1.00 21.03 ? 359 SER B CB 1 ATOM 7600 O OG . SER B 1 359 ? 29.031 49.502 -11.687 1.00 22.26 ? 359 SER B OG 1 ATOM 7601 N N . ARG B 1 360 ? 31.521 46.181 -12.395 1.00 23.95 ? 360 ARG B N 1 ATOM 7602 C CA . ARG B 1 360 ? 32.873 45.684 -12.727 1.00 24.48 ? 360 ARG B CA 1 ATOM 7603 C C . ARG B 1 360 ? 33.526 46.800 -13.545 1.00 25.51 ? 360 ARG B C 1 ATOM 7604 O O . ARG B 1 360 ? 32.911 47.343 -14.472 1.00 22.67 ? 360 ARG B O 1 ATOM 7605 C CB . ARG B 1 360 ? 32.764 44.387 -13.515 1.00 25.40 ? 360 ARG B CB 1 ATOM 7606 C CG . ARG B 1 360 ? 32.271 43.178 -12.700 1.00 25.69 ? 360 ARG B CG 1 ATOM 7607 C CD . ARG B 1 360 ? 30.738 43.061 -12.638 1.00 23.12 ? 360 ARG B CD 1 ATOM 7608 N NE . ARG B 1 360 ? 30.191 42.747 -13.969 1.00 22.21 ? 360 ARG B NE 1 ATOM 7609 C CZ . ARG B 1 360 ? 30.332 41.570 -14.576 1.00 20.60 ? 360 ARG B CZ 1 ATOM 7610 N NH1 . ARG B 1 360 ? 30.900 40.519 -13.962 1.00 21.97 ? 360 ARG B NH1 1 ATOM 7611 N NH2 . ARG B 1 360 ? 29.877 41.425 -15.806 1.00 21.72 ? 360 ARG B NH2 1 ATOM 7612 N N . LEU B 1 361 ? 34.727 47.191 -13.156 1.00 26.75 ? 361 LEU B N 1 ATOM 7613 C CA . LEU B 1 361 ? 35.402 48.329 -13.759 1.00 27.02 ? 361 LEU B CA 1 ATOM 7614 C C . LEU B 1 361 ? 36.727 47.831 -14.328 1.00 24.68 ? 361 LEU B C 1 ATOM 7615 O O . LEU B 1 361 ? 37.356 46.950 -13.755 1.00 23.80 ? 361 LEU B O 1 ATOM 7616 C CB . LEU B 1 361 ? 35.615 49.403 -12.733 1.00 27.49 ? 361 LEU B CB 1 ATOM 7617 C CG . LEU B 1 361 ? 34.385 50.041 -12.098 1.00 26.48 ? 361 LEU B CG 1 ATOM 7618 C CD1 . LEU B 1 361 ? 34.801 51.171 -11.188 1.00 27.18 ? 361 LEU B CD1 1 ATOM 7619 C CD2 . LEU B 1 361 ? 33.433 50.562 -13.148 1.00 26.38 ? 361 LEU B CD2 1 ATOM 7620 N N . ASP B 1 362 ? 37.135 48.347 -15.489 1.00 27.46 ? 362 ASP B N 1 ATOM 7621 C CA . ASP B 1 362 ? 38.416 47.882 -16.086 1.00 30.57 ? 362 ASP B CA 1 ATOM 7622 C C . ASP B 1 362 ? 39.570 48.682 -15.520 1.00 33.89 ? 362 ASP B C 1 ATOM 7623 O O . ASP B 1 362 ? 39.419 49.474 -14.570 1.00 31.26 ? 362 ASP B O 1 ATOM 7624 C CB . ASP B 1 362 ? 38.419 47.933 -17.633 1.00 32.88 ? 362 ASP B CB 1 ATOM 7625 C CG . ASP B 1 362 ? 38.324 49.338 -18.180 1.00 40.74 ? 362 ASP B CG 1 ATOM 7626 O OD1 . ASP B 1 362 ? 38.620 50.337 -17.440 1.00 34.86 ? 362 ASP B OD1 1 ATOM 7627 O OD2 . ASP B 1 362 ? 37.890 49.436 -19.356 1.00 41.18 ? 362 ASP B OD2 1 ATOM 7628 N N . GLU B 1 363 ? 40.715 48.482 -16.146 1.00 36.84 ? 363 GLU B N 1 ATOM 7629 C CA . GLU B 1 363 ? 41.976 49.069 -15.754 1.00 38.97 ? 363 GLU B CA 1 ATOM 7630 C C . GLU B 1 363 ? 41.972 50.581 -15.812 1.00 35.60 ? 363 GLU B C 1 ATOM 7631 O O . GLU B 1 363 ? 42.760 51.173 -15.178 1.00 36.52 ? 363 GLU B O 1 ATOM 7632 C CB . GLU B 1 363 ? 43.158 48.474 -16.575 1.00 43.62 ? 363 GLU B CB 1 ATOM 7633 C CG . GLU B 1 363 ? 43.589 47.046 -16.260 1.00 48.01 ? 363 GLU B CG 1 ATOM 7634 C CD . GLU B 1 363 ? 42.956 45.979 -17.128 1.00 47.61 ? 363 GLU B CD 1 ATOM 7635 O OE1 . GLU B 1 363 ? 43.328 44.837 -17.032 1.00 59.11 ? 363 GLU B OE1 1 ATOM 7636 O OE2 . GLU B 1 363 ? 42.052 46.268 -17.894 1.00 38.48 ? 363 GLU B OE2 1 ATOM 7637 N N . ASN B 1 364 ? 41.079 51.197 -16.555 1.00 31.95 ? 364 ASN B N 1 ATOM 7638 C CA . ASN B 1 364 ? 40.926 52.622 -16.497 1.00 32.48 ? 364 ASN B CA 1 ATOM 7639 C C . ASN B 1 364 ? 39.763 53.031 -15.622 1.00 32.94 ? 364 ASN B C 1 ATOM 7640 O O . ASN B 1 364 ? 39.372 54.200 -15.653 1.00 30.88 ? 364 ASN B O 1 ATOM 7641 C CB . ASN B 1 364 ? 40.737 53.218 -17.875 1.00 36.05 ? 364 ASN B CB 1 ATOM 7642 C CG . ASN B 1 364 ? 41.922 52.975 -18.797 1.00 35.87 ? 364 ASN B CG 1 ATOM 7643 O OD1 . ASN B 1 364 ? 41.759 52.928 -20.003 1.00 39.85 ? 364 ASN B OD1 1 ATOM 7644 N ND2 . ASN B 1 364 ? 43.098 52.838 -18.239 1.00 33.01 ? 364 ASN B ND2 1 ATOM 7645 N N . TYR B 1 365 ? 39.254 52.105 -14.794 1.00 27.98 ? 365 TYR B N 1 ATOM 7646 C CA . TYR B 1 365 ? 38.061 52.347 -13.981 1.00 28.94 ? 365 TYR B CA 1 ATOM 7647 C C . TYR B 1 365 ? 36.837 52.780 -14.793 1.00 29.33 ? 365 TYR B C 1 ATOM 7648 O O . TYR B 1 365 ? 35.969 53.504 -14.326 1.00 32.66 ? 365 TYR B O 1 ATOM 7649 C CB . TYR B 1 365 ? 38.355 53.338 -12.842 1.00 28.02 ? 365 TYR B CB 1 ATOM 7650 C CG . TYR B 1 365 ? 39.183 52.712 -11.759 1.00 28.59 ? 365 TYR B CG 1 ATOM 7651 C CD1 . TYR B 1 365 ? 40.523 52.444 -11.939 1.00 28.24 ? 365 TYR B CD1 1 ATOM 7652 C CD2 . TYR B 1 365 ? 38.628 52.381 -10.529 1.00 29.11 ? 365 TYR B CD2 1 ATOM 7653 C CE1 . TYR B 1 365 ? 41.292 51.855 -10.926 1.00 29.37 ? 365 TYR B CE1 1 ATOM 7654 C CE2 . TYR B 1 365 ? 39.406 51.806 -9.512 1.00 28.57 ? 365 TYR B CE2 1 ATOM 7655 C CZ . TYR B 1 365 ? 40.711 51.509 -9.709 1.00 29.62 ? 365 TYR B CZ 1 ATOM 7656 O OH . TYR B 1 365 ? 41.476 50.956 -8.673 1.00 27.20 ? 365 TYR B OH 1 ATOM 7657 N N . GLN B 1 366 ? 36.749 52.276 -16.014 1.00 31.62 ? 366 GLN B N 1 ATOM 7658 C CA . GLN B 1 366 ? 35.573 52.443 -16.857 1.00 28.57 ? 366 GLN B CA 1 ATOM 7659 C C . GLN B 1 366 ? 34.809 51.116 -16.831 1.00 27.82 ? 366 GLN B C 1 ATOM 7660 O O . GLN B 1 366 ? 35.386 50.090 -16.478 1.00 26.70 ? 366 GLN B O 1 ATOM 7661 C CB . GLN B 1 366 ? 35.993 52.727 -18.300 1.00 32.62 ? 366 GLN B CB 1 ATOM 7662 C CG . GLN B 1 366 ? 36.772 53.990 -18.483 1.00 35.75 ? 366 GLN B CG 1 ATOM 7663 C CD . GLN B 1 366 ? 35.971 55.195 -18.035 1.00 39.84 ? 366 GLN B CD 1 ATOM 7664 O OE1 . GLN B 1 366 ? 34.818 55.351 -18.400 1.00 40.45 ? 366 GLN B OE1 1 ATOM 7665 N NE2 . GLN B 1 366 ? 36.589 56.057 -17.231 1.00 50.36 ? 366 GLN B NE2 1 ATOM 7666 N N . PRO B 1 367 ? 33.536 51.120 -17.267 1.00 31.66 ? 367 PRO B N 1 ATOM 7667 C CA . PRO B 1 367 ? 32.719 49.924 -17.228 1.00 30.35 ? 367 PRO B CA 1 ATOM 7668 C C . PRO B 1 367 ? 33.379 48.818 -17.991 1.00 35.14 ? 367 PRO B C 1 ATOM 7669 O O . PRO B 1 367 ? 33.889 49.022 -19.096 1.00 36.75 ? 367 PRO B O 1 ATOM 7670 C CB . PRO B 1 367 ? 31.480 50.338 -17.946 1.00 31.47 ? 367 PRO B CB 1 ATOM 7671 C CG . PRO B 1 367 ? 31.342 51.777 -17.636 1.00 32.83 ? 367 PRO B CG 1 ATOM 7672 C CD . PRO B 1 367 ? 32.735 52.306 -17.631 1.00 33.22 ? 367 PRO B CD 1 ATOM 7673 N N . TRP B 1 368 ? 33.382 47.652 -17.388 1.00 30.21 ? 368 TRP B N 1 ATOM 7674 C CA . TRP B 1 368 ? 34.095 46.544 -17.877 1.00 28.54 ? 368 TRP B CA 1 ATOM 7675 C C . TRP B 1 368 ? 33.071 45.680 -18.563 1.00 35.12 ? 368 TRP B C 1 ATOM 7676 O O . TRP B 1 368 ? 32.278 44.986 -17.900 1.00 28.04 ? 368 TRP B O 1 ATOM 7677 C CB . TRP B 1 368 ? 34.710 45.786 -16.717 1.00 29.40 ? 368 TRP B CB 1 ATOM 7678 C CG . TRP B 1 368 ? 35.459 44.609 -17.126 1.00 32.62 ? 368 TRP B CG 1 ATOM 7679 C CD1 . TRP B 1 368 ? 36.751 44.583 -17.615 1.00 36.60 ? 368 TRP B CD1 1 ATOM 7680 C CD2 . TRP B 1 368 ? 35.025 43.257 -17.060 1.00 31.77 ? 368 TRP B CD2 1 ATOM 7681 N NE1 . TRP B 1 368 ? 37.132 43.278 -17.851 1.00 37.45 ? 368 TRP B NE1 1 ATOM 7682 C CE2 . TRP B 1 368 ? 36.100 42.454 -17.503 1.00 33.62 ? 368 TRP B CE2 1 ATOM 7683 C CE3 . TRP B 1 368 ? 33.843 42.652 -16.661 1.00 28.99 ? 368 TRP B CE3 1 ATOM 7684 C CZ2 . TRP B 1 368 ? 35.991 41.074 -17.606 1.00 32.38 ? 368 TRP B CZ2 1 ATOM 7685 C CZ3 . TRP B 1 368 ? 33.746 41.290 -16.754 1.00 30.33 ? 368 TRP B CZ3 1 ATOM 7686 C CH2 . TRP B 1 368 ? 34.812 40.512 -17.215 1.00 31.61 ? 368 TRP B CH2 1 ATOM 7687 N N . GLY B 1 369 ? 33.071 45.725 -19.902 1.00 38.26 ? 369 GLY B N 1 ATOM 7688 C CA . GLY B 1 369 ? 32.143 44.922 -20.706 1.00 36.54 ? 369 GLY B CA 1 ATOM 7689 C C . GLY B 1 369 ? 30.738 45.465 -20.896 1.00 38.40 ? 369 GLY B C 1 ATOM 7690 O O . GLY B 1 369 ? 30.352 46.570 -20.426 1.00 40.46 ? 369 GLY B O 1 ATOM 7691 N N . PRO B 1 370 ? 29.934 44.706 -21.626 1.00 34.39 ? 370 PRO B N 1 ATOM 7692 C CA . PRO B 1 370 ? 28.578 45.160 -21.915 1.00 31.57 ? 370 PRO B CA 1 ATOM 7693 C C . PRO B 1 370 ? 27.631 44.884 -20.707 1.00 30.46 ? 370 PRO B C 1 ATOM 7694 O O . PRO B 1 370 ? 26.569 45.484 -20.643 1.00 34.82 ? 370 PRO B O 1 ATOM 7695 C CB . PRO B 1 370 ? 28.183 44.295 -23.112 1.00 29.65 ? 370 PRO B CB 1 ATOM 7696 C CG . PRO B 1 370 ? 28.991 43.047 -22.944 1.00 31.98 ? 370 PRO B CG 1 ATOM 7697 C CD . PRO B 1 370 ? 30.154 43.317 -22.036 1.00 32.47 ? 370 PRO B CD 1 ATOM 7698 N N . GLU B 1 371 ? 28.020 44.024 -19.783 1.00 25.75 ? 371 GLU B N 1 ATOM 7699 C CA . GLU B 1 371 ? 27.262 43.790 -18.564 1.00 23.40 ? 371 GLU B CA 1 ATOM 7700 C C . GLU B 1 371 ? 28.032 44.352 -17.344 1.00 24.94 ? 371 GLU B C 1 ATOM 7701 O O . GLU B 1 371 ? 28.288 43.664 -16.410 1.00 24.63 ? 371 GLU B O 1 ATOM 7702 C CB . GLU B 1 371 ? 27.000 42.293 -18.403 1.00 22.89 ? 371 GLU B CB 1 ATOM 7703 C CG . GLU B 1 371 ? 26.184 41.664 -19.510 1.00 24.33 ? 371 GLU B CG 1 ATOM 7704 C CD . GLU B 1 371 ? 26.249 40.150 -19.571 1.00 23.96 ? 371 GLU B CD 1 ATOM 7705 O OE1 . GLU B 1 371 ? 25.868 39.618 -20.594 1.00 24.32 ? 371 GLU B OE1 1 ATOM 7706 O OE2 . GLU B 1 371 ? 26.604 39.492 -18.618 1.00 22.15 ? 371 GLU B OE2 1 ATOM 7707 N N . ALA B 1 372 ? 28.405 45.616 -17.393 1.00 24.72 ? 372 ALA B N 1 ATOM 7708 C CA . ALA B 1 372 ? 29.388 46.112 -16.440 1.00 23.65 ? 372 ALA B CA 1 ATOM 7709 C C . ALA B 1 372 ? 28.685 46.264 -15.097 1.00 21.88 ? 372 ALA B C 1 ATOM 7710 O O . ALA B 1 372 ? 29.193 45.824 -14.097 1.00 21.42 ? 372 ALA B O 1 ATOM 7711 C CB . ALA B 1 372 ? 29.937 47.463 -16.859 1.00 22.08 ? 372 ALA B CB 1 ATOM 7712 N N . GLU B 1 373 ? 27.542 46.936 -15.145 1.00 24.41 ? 373 GLU B N 1 ATOM 7713 C CA . GLU B 1 373 ? 26.722 47.193 -13.981 1.00 24.99 ? 373 GLU B CA 1 ATOM 7714 C C . GLU B 1 373 ? 25.597 46.160 -13.771 1.00 22.57 ? 373 GLU B C 1 ATOM 7715 O O . GLU B 1 373 ? 24.646 46.072 -14.560 1.00 24.23 ? 373 GLU B O 1 ATOM 7716 C CB . GLU B 1 373 ? 26.131 48.567 -14.041 1.00 25.97 ? 373 GLU B CB 1 ATOM 7717 C CG . GLU B 1 373 ? 25.516 48.965 -12.726 1.00 28.00 ? 373 GLU B CG 1 ATOM 7718 C CD . GLU B 1 373 ? 24.843 50.303 -12.808 1.00 30.25 ? 373 GLU B CD 1 ATOM 7719 O OE1 . GLU B 1 373 ? 25.437 51.319 -12.496 1.00 36.65 ? 373 GLU B OE1 1 ATOM 7720 O OE2 . GLU B 1 373 ? 23.682 50.353 -13.204 1.00 43.30 ? 373 GLU B OE2 1 ATOM 7721 N N . LEU B 1 374 ? 25.708 45.428 -12.653 1.00 18.48 ? 374 LEU B N 1 ATOM 7722 C CA . LEU B 1 374 ? 24.807 44.359 -12.289 1.00 17.49 ? 374 LEU B CA 1 ATOM 7723 C C . LEU B 1 374 ? 23.839 44.754 -11.139 1.00 17.07 ? 374 LEU B C 1 ATOM 7724 O O . LEU B 1 374 ? 24.253 45.429 -10.171 1.00 19.08 ? 374 LEU B O 1 ATOM 7725 C CB . LEU B 1 374 ? 25.599 43.122 -11.924 1.00 17.38 ? 374 LEU B CB 1 ATOM 7726 C CG . LEU B 1 374 ? 26.621 42.648 -12.983 1.00 17.69 ? 374 LEU B CG 1 ATOM 7727 C CD1 . LEU B 1 374 ? 27.365 41.468 -12.399 1.00 18.70 ? 374 LEU B CD1 1 ATOM 7728 C CD2 . LEU B 1 374 ? 25.958 42.205 -14.298 1.00 17.76 ? 374 LEU B CD2 1 ATOM 7729 N N . PRO B 1 375 ? 22.558 44.392 -11.287 1.00 15.73 ? 375 PRO B N 1 ATOM 7730 C CA . PRO B 1 375 ? 21.657 44.563 -10.140 1.00 15.57 ? 375 PRO B CA 1 ATOM 7731 C C . PRO B 1 375 ? 22.088 43.692 -8.996 1.00 14.95 ? 375 PRO B C 1 ATOM 7732 O O . PRO B 1 375 ? 22.403 42.488 -9.173 1.00 13.68 ? 375 PRO B O 1 ATOM 7733 C CB . PRO B 1 375 ? 20.264 44.182 -10.702 1.00 15.06 ? 375 PRO B CB 1 ATOM 7734 C CG . PRO B 1 375 ? 20.458 43.884 -12.197 1.00 14.80 ? 375 PRO B CG 1 ATOM 7735 C CD . PRO B 1 375 ? 21.895 43.646 -12.404 1.00 14.90 ? 375 PRO B CD 1 ATOM 7736 N N . LEU B 1 376 ? 22.091 44.274 -7.811 1.00 15.67 ? 376 LEU B N 1 ATOM 7737 C CA . LEU B 1 376 ? 22.466 43.538 -6.579 1.00 16.08 ? 376 LEU B CA 1 ATOM 7738 C C . LEU B 1 376 ? 21.771 42.195 -6.420 1.00 14.95 ? 376 LEU B C 1 ATOM 7739 O O . LEU B 1 376 ? 22.397 41.190 -6.022 1.00 15.89 ? 376 LEU B O 1 ATOM 7740 C CB . LEU B 1 376 ? 22.160 44.411 -5.371 1.00 18.52 ? 376 LEU B CB 1 ATOM 7741 C CG . LEU B 1 376 ? 22.468 43.706 -4.025 1.00 21.54 ? 376 LEU B CG 1 ATOM 7742 C CD1 . LEU B 1 376 ? 23.930 43.476 -3.881 1.00 21.85 ? 376 LEU B CD1 1 ATOM 7743 C CD2 . LEU B 1 376 ? 21.927 44.493 -2.840 1.00 22.63 ? 376 LEU B CD2 1 ATOM 7744 N N . HIS B 1 377 ? 20.497 42.146 -6.772 1.00 15.80 ? 377 HIS B N 1 ATOM 7745 C CA . HIS B 1 377 ? 19.699 40.960 -6.446 1.00 16.38 ? 377 HIS B CA 1 ATOM 7746 C C . HIS B 1 377 ? 20.211 39.761 -7.206 1.00 15.53 ? 377 HIS B C 1 ATOM 7747 O O . HIS B 1 377 ? 19.999 38.687 -6.781 1.00 16.39 ? 377 HIS B O 1 ATOM 7748 C CB . HIS B 1 377 ? 18.179 41.130 -6.622 1.00 17.04 ? 377 HIS B CB 1 ATOM 7749 C CG . HIS B 1 377 ? 17.699 41.044 -8.041 1.00 16.08 ? 377 HIS B CG 1 ATOM 7750 N ND1 . HIS B 1 377 ? 17.665 42.139 -8.880 1.00 16.24 ? 377 HIS B ND1 1 ATOM 7751 C CD2 . HIS B 1 377 ? 17.233 39.995 -8.754 1.00 16.73 ? 377 HIS B CD2 1 ATOM 7752 C CE1 . HIS B 1 377 ? 17.197 41.752 -10.058 1.00 18.81 ? 377 HIS B CE1 1 ATOM 7753 N NE2 . HIS B 1 377 ? 16.993 40.447 -10.022 1.00 16.76 ? 377 HIS B NE2 1 ATOM 7754 N N . THR B 1 378 ? 20.934 39.995 -8.307 1.00 15.45 ? 378 THR B N 1 ATOM 7755 C CA . THR B 1 378 ? 21.434 38.913 -9.108 1.00 15.02 ? 378 THR B CA 1 ATOM 7756 C C . THR B 1 378 ? 22.725 38.392 -8.565 1.00 15.17 ? 378 THR B C 1 ATOM 7757 O O . THR B 1 378 ? 23.285 37.456 -9.111 1.00 17.45 ? 378 THR B O 1 ATOM 7758 C CB . THR B 1 378 ? 21.666 39.286 -10.592 1.00 14.83 ? 378 THR B CB 1 ATOM 7759 O OG1 . THR B 1 378 ? 22.732 40.225 -10.705 1.00 13.56 ? 378 THR B OG1 1 ATOM 7760 C CG2 . THR B 1 378 ? 20.396 39.874 -11.271 1.00 15.41 ? 378 THR B CG2 1 ATOM 7761 N N . LEU B 1 379 ? 23.203 38.950 -7.471 1.00 15.39 ? 379 LEU B N 1 ATOM 7762 C CA . LEU B 1 379 ? 24.519 38.622 -6.965 1.00 15.20 ? 379 LEU B CA 1 ATOM 7763 C C . LEU B 1 379 ? 24.497 37.832 -5.676 1.00 14.79 ? 379 LEU B C 1 ATOM 7764 O O . LEU B 1 379 ? 25.562 37.504 -5.137 1.00 16.80 ? 379 LEU B O 1 ATOM 7765 C CB . LEU B 1 379 ? 25.264 39.919 -6.788 1.00 15.60 ? 379 LEU B CB 1 ATOM 7766 C CG . LEU B 1 379 ? 25.452 40.608 -8.126 1.00 15.58 ? 379 LEU B CG 1 ATOM 7767 C CD1 . LEU B 1 379 ? 26.026 41.987 -7.900 1.00 17.84 ? 379 LEU B CD1 1 ATOM 7768 C CD2 . LEU B 1 379 ? 26.339 39.782 -9.044 1.00 16.03 ? 379 LEU B CD2 1 ATOM 7769 N N . PHE B 1 380 ? 23.305 37.558 -5.154 1.00 13.94 ? 380 PHE B N 1 ATOM 7770 C CA . PHE B 1 380 ? 23.194 36.789 -3.931 1.00 14.33 ? 380 PHE B CA 1 ATOM 7771 C C . PHE B 1 380 ? 23.611 35.340 -4.232 1.00 15.30 ? 380 PHE B C 1 ATOM 7772 O O . PHE B 1 380 ? 23.139 34.715 -5.195 1.00 15.85 ? 380 PHE B O 1 ATOM 7773 C CB . PHE B 1 380 ? 21.744 36.839 -3.326 1.00 13.83 ? 380 PHE B CB 1 ATOM 7774 C CG . PHE B 1 380 ? 21.234 38.222 -3.039 1.00 14.01 ? 380 PHE B CG 1 ATOM 7775 C CD1 . PHE B 1 380 ? 22.011 39.131 -2.345 1.00 13.30 ? 380 PHE B CD1 1 ATOM 7776 C CD2 . PHE B 1 380 ? 19.947 38.625 -3.466 1.00 14.89 ? 380 PHE B CD2 1 ATOM 7777 C CE1 . PHE B 1 380 ? 21.535 40.452 -2.111 1.00 13.82 ? 380 PHE B CE1 1 ATOM 7778 C CE2 . PHE B 1 380 ? 19.462 39.920 -3.241 1.00 13.37 ? 380 PHE B CE2 1 ATOM 7779 C CZ . PHE B 1 380 ? 20.249 40.820 -2.551 1.00 13.98 ? 380 PHE B CZ 1 ATOM 7780 N N . PHE B 1 381 ? 24.476 34.793 -3.416 1.00 16.54 ? 381 PHE B N 1 ATOM 7781 C CA . PHE B 1 381 ? 24.983 33.399 -3.635 1.00 15.84 ? 381 PHE B CA 1 ATOM 7782 C C . PHE B 1 381 ? 25.592 33.220 -5.020 1.00 17.91 ? 381 PHE B C 1 ATOM 7783 O O . PHE B 1 381 ? 25.573 32.129 -5.572 1.00 18.50 ? 381 PHE B O 1 ATOM 7784 C CB . PHE B 1 381 ? 23.925 32.397 -3.221 1.00 15.97 ? 381 PHE B CB 1 ATOM 7785 C CG . PHE B 1 381 ? 23.561 32.556 -1.785 1.00 16.17 ? 381 PHE B CG 1 ATOM 7786 C CD1 . PHE B 1 381 ? 24.362 32.004 -0.814 1.00 18.24 ? 381 PHE B CD1 1 ATOM 7787 C CD2 . PHE B 1 381 ? 22.511 33.403 -1.395 1.00 17.70 ? 381 PHE B CD2 1 ATOM 7788 C CE1 . PHE B 1 381 ? 24.096 32.178 0.526 1.00 19.29 ? 381 PHE B CE1 1 ATOM 7789 C CE2 . PHE B 1 381 ? 22.271 33.644 -0.047 1.00 18.32 ? 381 PHE B CE2 1 ATOM 7790 C CZ . PHE B 1 381 ? 23.079 33.019 0.914 1.00 19.46 ? 381 PHE B CZ 1 ATOM 7791 N N . ASN B 1 382 ? 26.192 34.313 -5.535 1.00 18.03 ? 382 ASN B N 1 ATOM 7792 C CA . ASN B 1 382 ? 26.719 34.318 -6.865 1.00 19.51 ? 382 ASN B CA 1 ATOM 7793 C C . ASN B 1 382 ? 28.256 34.294 -6.869 1.00 19.18 ? 382 ASN B C 1 ATOM 7794 O O . ASN B 1 382 ? 28.912 35.278 -6.522 1.00 21.28 ? 382 ASN B O 1 ATOM 7795 C CB . ASN B 1 382 ? 26.220 35.522 -7.638 1.00 20.08 ? 382 ASN B CB 1 ATOM 7796 C CG . ASN B 1 382 ? 26.486 35.391 -9.143 1.00 21.01 ? 382 ASN B CG 1 ATOM 7797 O OD1 . ASN B 1 382 ? 27.494 34.858 -9.516 1.00 20.36 ? 382 ASN B OD1 1 ATOM 7798 N ND2 . ASN B 1 382 ? 25.551 35.871 -9.994 1.00 18.86 ? 382 ASN B ND2 1 ATOM 7799 N N . THR B 1 383 ? 28.784 33.106 -7.153 1.00 22.51 ? 383 THR B N 1 ATOM 7800 C CA . THR B 1 383 ? 30.203 32.864 -7.404 1.00 22.21 ? 383 THR B CA 1 ATOM 7801 C C . THR B 1 383 ? 30.562 32.723 -8.894 1.00 22.39 ? 383 THR B C 1 ATOM 7802 O O . THR B 1 383 ? 31.709 32.995 -9.279 1.00 22.48 ? 383 THR B O 1 ATOM 7803 C CB . THR B 1 383 ? 30.701 31.636 -6.658 1.00 24.32 ? 383 THR B CB 1 ATOM 7804 O OG1 . THR B 1 383 ? 29.852 30.521 -6.906 1.00 22.50 ? 383 THR B OG1 1 ATOM 7805 C CG2 . THR B 1 383 ? 30.721 31.926 -5.175 1.00 24.18 ? 383 THR B CG2 1 ATOM 7806 N N . TRP B 1 384 ? 29.601 32.402 -9.746 1.00 21.10 ? 384 TRP B N 1 ATOM 7807 C CA . TRP B 1 384 ? 29.896 32.230 -11.158 1.00 18.68 ? 384 TRP B CA 1 ATOM 7808 C C . TRP B 1 384 ? 30.293 33.538 -11.844 1.00 19.54 ? 384 TRP B C 1 ATOM 7809 O O . TRP B 1 384 ? 31.142 33.528 -12.745 1.00 17.52 ? 384 TRP B O 1 ATOM 7810 C CB . TRP B 1 384 ? 28.770 31.526 -11.896 1.00 18.06 ? 384 TRP B CB 1 ATOM 7811 C CG . TRP B 1 384 ? 27.545 32.326 -12.181 1.00 18.27 ? 384 TRP B CG 1 ATOM 7812 C CD1 . TRP B 1 384 ? 26.395 32.342 -11.451 1.00 16.46 ? 384 TRP B CD1 1 ATOM 7813 C CD2 . TRP B 1 384 ? 27.332 33.207 -13.301 1.00 19.59 ? 384 TRP B CD2 1 ATOM 7814 N NE1 . TRP B 1 384 ? 25.478 33.211 -12.032 1.00 19.39 ? 384 TRP B NE1 1 ATOM 7815 C CE2 . TRP B 1 384 ? 26.035 33.769 -13.155 1.00 20.10 ? 384 TRP B CE2 1 ATOM 7816 C CE3 . TRP B 1 384 ? 28.108 33.581 -14.389 1.00 19.67 ? 384 TRP B CE3 1 ATOM 7817 C CZ2 . TRP B 1 384 ? 25.484 34.631 -14.086 1.00 20.26 ? 384 TRP B CZ2 1 ATOM 7818 C CZ3 . TRP B 1 384 ? 27.566 34.492 -15.299 1.00 20.97 ? 384 TRP B CZ3 1 ATOM 7819 C CH2 . TRP B 1 384 ? 26.269 35.001 -15.133 1.00 21.94 ? 384 TRP B CH2 1 ATOM 7820 N N . ARG B 1 385 ? 29.724 34.670 -11.412 1.00 20.80 ? 385 ARG B N 1 ATOM 7821 C CA . ARG B 1 385 ? 30.188 35.938 -11.913 1.00 22.69 ? 385 ARG B CA 1 ATOM 7822 C C . ARG B 1 385 ? 31.646 36.226 -11.574 1.00 23.99 ? 385 ARG B C 1 ATOM 7823 O O . ARG B 1 385 ? 32.271 37.080 -12.256 1.00 27.54 ? 385 ARG B O 1 ATOM 7824 C CB . ARG B 1 385 ? 29.318 37.072 -11.406 1.00 23.65 ? 385 ARG B CB 1 ATOM 7825 C CG . ARG B 1 385 ? 27.971 37.119 -12.098 1.00 23.06 ? 385 ARG B CG 1 ATOM 7826 C CD . ARG B 1 385 ? 28.119 37.741 -13.502 1.00 22.87 ? 385 ARG B CD 1 ATOM 7827 N NE . ARG B 1 385 ? 26.819 38.072 -14.009 1.00 20.01 ? 385 ARG B NE 1 ATOM 7828 C CZ . ARG B 1 385 ? 26.543 38.454 -15.240 1.00 20.28 ? 385 ARG B CZ 1 ATOM 7829 N NH1 . ARG B 1 385 ? 27.523 38.599 -16.131 1.00 21.89 ? 385 ARG B NH1 1 ATOM 7830 N NH2 . ARG B 1 385 ? 25.302 38.729 -15.565 1.00 19.06 ? 385 ARG B NH2 1 ATOM 7831 N N . ILE B 1 386 ? 32.166 35.625 -10.500 1.00 22.68 ? 386 ILE B N 1 ATOM 7832 C CA . ILE B 1 386 ? 33.574 35.759 -10.184 1.00 24.73 ? 386 ILE B CA 1 ATOM 7833 C C . ILE B 1 386 ? 34.385 34.795 -11.094 1.00 26.66 ? 386 ILE B C 1 ATOM 7834 O O . ILE B 1 386 ? 35.171 35.232 -11.915 1.00 29.21 ? 386 ILE B O 1 ATOM 7835 C CB . ILE B 1 386 ? 33.921 35.411 -8.706 1.00 24.56 ? 386 ILE B CB 1 ATOM 7836 C CG1 . ILE B 1 386 ? 33.189 36.378 -7.738 1.00 26.27 ? 386 ILE B CG1 1 ATOM 7837 C CG2 . ILE B 1 386 ? 35.423 35.496 -8.507 1.00 24.39 ? 386 ILE B CG2 1 ATOM 7838 C CD1 . ILE B 1 386 ? 33.287 35.994 -6.261 1.00 24.61 ? 386 ILE B CD1 1 ATOM 7839 N N . ILE B 1 387 ? 34.122 33.509 -10.941 1.00 25.70 ? 387 ILE B N 1 ATOM 7840 C CA . ILE B 1 387 ? 34.899 32.468 -11.565 1.00 28.67 ? 387 ILE B CA 1 ATOM 7841 C C . ILE B 1 387 ? 34.781 32.493 -13.101 1.00 28.65 ? 387 ILE B C 1 ATOM 7842 O O . ILE B 1 387 ? 35.753 32.271 -13.782 1.00 26.69 ? 387 ILE B O 1 ATOM 7843 C CB . ILE B 1 387 ? 34.434 31.087 -11.083 1.00 30.38 ? 387 ILE B CB 1 ATOM 7844 C CG1 . ILE B 1 387 ? 34.530 30.966 -9.564 1.00 32.44 ? 387 ILE B CG1 1 ATOM 7845 C CG2 . ILE B 1 387 ? 35.214 29.986 -11.794 1.00 33.37 ? 387 ILE B CG2 1 ATOM 7846 C CD1 . ILE B 1 387 ? 35.900 30.755 -9.018 1.00 34.46 ? 387 ILE B CD1 1 ATOM 7847 N N . LYS B 1 388 ? 33.600 32.750 -13.646 1.00 25.12 ? 388 LYS B N 1 ATOM 7848 C CA . LYS B 1 388 ? 33.452 32.738 -15.091 1.00 24.71 ? 388 LYS B CA 1 ATOM 7849 C C . LYS B 1 388 ? 33.447 34.060 -15.709 1.00 26.11 ? 388 LYS B C 1 ATOM 7850 O O . LYS B 1 388 ? 33.256 34.121 -16.913 1.00 29.31 ? 388 LYS B O 1 ATOM 7851 C CB . LYS B 1 388 ? 32.136 32.092 -15.504 1.00 29.24 ? 388 LYS B CB 1 ATOM 7852 C CG . LYS B 1 388 ? 31.871 30.749 -14.868 1.00 30.18 ? 388 LYS B CG 1 ATOM 7853 C CD . LYS B 1 388 ? 32.574 29.641 -15.579 1.00 37.73 ? 388 LYS B CD 1 ATOM 7854 C CE . LYS B 1 388 ? 31.891 28.322 -15.265 1.00 42.88 ? 388 LYS B CE 1 ATOM 7855 N NZ . LYS B 1 388 ? 32.883 27.203 -15.305 1.00 48.31 ? 388 LYS B NZ 1 ATOM 7856 N N . ASP B 1 389 ? 33.537 35.154 -14.954 1.00 23.03 ? 389 ASP B N 1 ATOM 7857 C CA . ASP B 1 389 ? 33.275 36.439 -15.574 1.00 25.00 ? 389 ASP B CA 1 ATOM 7858 C C . ASP B 1 389 ? 34.170 37.556 -14.997 1.00 24.49 ? 389 ASP B C 1 ATOM 7859 O O . ASP B 1 389 ? 33.724 38.642 -14.674 1.00 26.12 ? 389 ASP B O 1 ATOM 7860 C CB . ASP B 1 389 ? 31.757 36.768 -15.542 1.00 24.20 ? 389 ASP B CB 1 ATOM 7861 C CG . ASP B 1 389 ? 31.355 37.976 -16.414 1.00 21.97 ? 389 ASP B CG 1 ATOM 7862 O OD1 . ASP B 1 389 ? 31.955 38.255 -17.456 1.00 26.09 ? 389 ASP B OD1 1 ATOM 7863 O OD2 . ASP B 1 389 ? 30.381 38.697 -16.076 1.00 22.04 ? 389 ASP B OD2 1 ATOM 7864 N N . GLY B 1 390 ? 35.459 37.289 -14.965 1.00 24.89 ? 390 GLY B N 1 ATOM 7865 C CA . GLY B 1 390 ? 36.480 38.381 -14.826 1.00 27.41 ? 390 GLY B CA 1 ATOM 7866 C C . GLY B 1 390 ? 37.358 38.319 -13.585 1.00 27.28 ? 390 GLY B C 1 ATOM 7867 O O . GLY B 1 390 ? 38.272 39.144 -13.430 1.00 33.68 ? 390 GLY B O 1 ATOM 7868 N N . GLY B 1 391 ? 37.074 37.363 -12.697 1.00 24.95 ? 391 GLY B N 1 ATOM 7869 C CA . GLY B 1 391 ? 37.639 37.301 -11.358 1.00 25.97 ? 391 GLY B CA 1 ATOM 7870 C C . GLY B 1 391 ? 37.391 38.517 -10.482 1.00 25.61 ? 391 GLY B C 1 ATOM 7871 O O . GLY B 1 391 ? 36.482 39.330 -10.777 1.00 27.21 ? 391 GLY B O 1 ATOM 7872 N N . ILE B 1 392 ? 38.217 38.731 -9.454 1.00 25.55 ? 392 ILE B N 1 ATOM 7873 C CA . ILE B 1 392 ? 37.894 39.830 -8.498 1.00 25.16 ? 392 ILE B CA 1 ATOM 7874 C C . ILE B 1 392 ? 38.420 41.197 -8.803 1.00 28.06 ? 392 ILE B C 1 ATOM 7875 O O . ILE B 1 392 ? 37.895 42.182 -8.259 1.00 24.35 ? 392 ILE B O 1 ATOM 7876 C CB . ILE B 1 392 ? 38.220 39.476 -7.046 1.00 29.37 ? 392 ILE B CB 1 ATOM 7877 C CG1 . ILE B 1 392 ? 39.714 39.513 -6.754 1.00 29.37 ? 392 ILE B CG1 1 ATOM 7878 C CG2 . ILE B 1 392 ? 37.618 38.137 -6.646 1.00 28.60 ? 392 ILE B CG2 1 ATOM 7879 C CD1 . ILE B 1 392 ? 39.974 39.549 -5.243 1.00 30.12 ? 392 ILE B CD1 1 ATOM 7880 N N . ASP B 1 393 ? 39.425 41.323 -9.690 1.00 24.91 ? 393 ASP B N 1 ATOM 7881 C CA . ASP B 1 393 ? 39.953 42.635 -9.939 1.00 24.14 ? 393 ASP B CA 1 ATOM 7882 C C . ASP B 1 393 ? 38.895 43.676 -10.335 1.00 23.73 ? 393 ASP B C 1 ATOM 7883 O O . ASP B 1 393 ? 38.939 44.812 -9.796 1.00 23.69 ? 393 ASP B O 1 ATOM 7884 C CB . ASP B 1 393 ? 41.131 42.614 -10.950 1.00 27.20 ? 393 ASP B CB 1 ATOM 7885 C CG . ASP B 1 393 ? 42.368 41.949 -10.394 1.00 25.32 ? 393 ASP B CG 1 ATOM 7886 O OD1 . ASP B 1 393 ? 42.404 41.554 -9.228 1.00 28.83 ? 393 ASP B OD1 1 ATOM 7887 O OD2 . ASP B 1 393 ? 43.375 41.847 -11.121 1.00 31.40 ? 393 ASP B OD2 1 ATOM 7888 N N . PRO B 1 394 ? 37.980 43.371 -11.299 1.00 22.07 ? 394 PRO B N 1 ATOM 7889 C CA . PRO B 1 394 ? 37.022 44.415 -11.647 1.00 21.93 ? 394 PRO B CA 1 ATOM 7890 C C . PRO B 1 394 ? 36.028 44.781 -10.508 1.00 22.43 ? 394 PRO B C 1 ATOM 7891 O O . PRO B 1 394 ? 35.496 45.930 -10.475 1.00 18.66 ? 394 PRO B O 1 ATOM 7892 C CB . PRO B 1 394 ? 36.238 43.800 -12.812 1.00 22.31 ? 394 PRO B CB 1 ATOM 7893 C CG . PRO B 1 394 ? 37.173 42.812 -13.408 1.00 23.71 ? 394 PRO B CG 1 ATOM 7894 C CD . PRO B 1 394 ? 37.931 42.250 -12.245 1.00 22.92 ? 394 PRO B CD 1 ATOM 7895 N N . LEU B 1 395 ? 35.778 43.810 -9.634 1.00 20.77 ? 395 LEU B N 1 ATOM 7896 C CA . LEU B 1 395 ? 34.881 44.017 -8.476 1.00 22.38 ? 395 LEU B CA 1 ATOM 7897 C C . LEU B 1 395 ? 35.581 44.862 -7.399 1.00 21.45 ? 395 LEU B C 1 ATOM 7898 O O . LEU B 1 395 ? 34.999 45.770 -6.846 1.00 25.27 ? 395 LEU B O 1 ATOM 7899 C CB . LEU B 1 395 ? 34.521 42.661 -7.863 1.00 20.74 ? 395 LEU B CB 1 ATOM 7900 C CG . LEU B 1 395 ? 33.579 41.865 -8.770 1.00 20.44 ? 395 LEU B CG 1 ATOM 7901 C CD1 . LEU B 1 395 ? 33.466 40.411 -8.308 1.00 21.26 ? 395 LEU B CD1 1 ATOM 7902 C CD2 . LEU B 1 395 ? 32.231 42.515 -8.838 1.00 22.06 ? 395 LEU B CD2 1 ATOM 7903 N N . VAL B 1 396 ? 36.844 44.561 -7.185 1.00 22.82 ? 396 VAL B N 1 ATOM 7904 C CA . VAL B 1 396 ? 37.707 45.325 -6.296 1.00 24.49 ? 396 VAL B CA 1 ATOM 7905 C C . VAL B 1 396 ? 37.768 46.799 -6.754 1.00 25.57 ? 396 VAL B C 1 ATOM 7906 O O . VAL B 1 396 ? 37.694 47.675 -5.926 1.00 28.21 ? 396 VAL B O 1 ATOM 7907 C CB . VAL B 1 396 ? 39.077 44.680 -6.143 1.00 22.77 ? 396 VAL B CB 1 ATOM 7908 C CG1 . VAL B 1 396 ? 40.027 45.545 -5.270 1.00 23.97 ? 396 VAL B CG1 1 ATOM 7909 C CG2 . VAL B 1 396 ? 38.967 43.285 -5.528 1.00 24.33 ? 396 VAL B CG2 1 ATOM 7910 N N . ARG B 1 397 ? 37.796 47.077 -8.058 1.00 25.07 ? 397 ARG B N 1 ATOM 7911 C CA . ARG B 1 397 ? 37.920 48.459 -8.505 1.00 23.37 ? 397 ARG B CA 1 ATOM 7912 C C . ARG B 1 397 ? 36.638 49.136 -8.231 1.00 24.82 ? 397 ARG B C 1 ATOM 7913 O O . ARG B 1 397 ? 36.617 50.318 -7.875 1.00 24.23 ? 397 ARG B O 1 ATOM 7914 C CB . ARG B 1 397 ? 38.203 48.539 -10.020 1.00 26.32 ? 397 ARG B CB 1 ATOM 7915 C CG . ARG B 1 397 ? 39.601 48.076 -10.410 1.00 26.73 ? 397 ARG B CG 1 ATOM 7916 C CD . ARG B 1 397 ? 39.907 48.432 -11.871 1.00 29.88 ? 397 ARG B CD 1 ATOM 7917 N NE . ARG B 1 397 ? 41.119 47.710 -12.218 1.00 31.83 ? 397 ARG B NE 1 ATOM 7918 C CZ . ARG B 1 397 ? 41.184 46.472 -12.723 1.00 33.17 ? 397 ARG B CZ 1 ATOM 7919 N NH1 . ARG B 1 397 ? 40.097 45.797 -13.080 1.00 31.70 ? 397 ARG B NH1 1 ATOM 7920 N NH2 . ARG B 1 397 ? 42.390 45.913 -12.916 1.00 32.85 ? 397 ARG B NH2 1 ATOM 7921 N N . GLY B 1 398 ? 35.522 48.414 -8.476 1.00 21.25 ? 398 GLY B N 1 ATOM 7922 C CA . GLY B 1 398 ? 34.233 48.945 -8.072 1.00 21.24 ? 398 GLY B CA 1 ATOM 7923 C C . GLY B 1 398 ? 34.096 49.261 -6.600 1.00 17.99 ? 398 GLY B C 1 ATOM 7924 O O . GLY B 1 398 ? 33.551 50.288 -6.252 1.00 22.08 ? 398 GLY B O 1 ATOM 7925 N N . LEU B 1 399 ? 34.615 48.413 -5.752 1.00 19.43 ? 399 LEU B N 1 ATOM 7926 C CA . LEU B 1 399 ? 34.657 48.710 -4.298 1.00 23.01 ? 399 LEU B CA 1 ATOM 7927 C C . LEU B 1 399 ? 35.259 50.040 -3.962 1.00 24.16 ? 399 LEU B C 1 ATOM 7928 O O . LEU B 1 399 ? 34.853 50.706 -3.004 1.00 23.44 ? 399 LEU B O 1 ATOM 7929 C CB . LEU B 1 399 ? 35.365 47.611 -3.520 1.00 23.10 ? 399 LEU B CB 1 ATOM 7930 C CG . LEU B 1 399 ? 34.437 46.442 -3.225 1.00 26.04 ? 399 LEU B CG 1 ATOM 7931 C CD1 . LEU B 1 399 ? 35.169 45.148 -2.899 1.00 31.08 ? 399 LEU B CD1 1 ATOM 7932 C CD2 . LEU B 1 399 ? 33.488 46.814 -2.096 1.00 24.48 ? 399 LEU B CD2 1 ATOM 7933 N N . LEU B 1 400 ? 36.190 50.470 -4.800 1.00 24.09 ? 400 LEU B N 1 ATOM 7934 C CA . LEU B 1 400 ? 37.008 51.678 -4.499 1.00 24.79 ? 400 LEU B CA 1 ATOM 7935 C C . LEU B 1 400 ? 36.427 52.902 -5.155 1.00 24.71 ? 400 LEU B C 1 ATOM 7936 O O . LEU B 1 400 ? 36.333 53.974 -4.553 1.00 22.13 ? 400 LEU B O 1 ATOM 7937 C CB . LEU B 1 400 ? 38.457 51.450 -4.945 1.00 25.68 ? 400 LEU B CB 1 ATOM 7938 C CG . LEU B 1 400 ? 39.340 50.406 -4.218 1.00 25.54 ? 400 LEU B CG 1 ATOM 7939 C CD1 . LEU B 1 400 ? 40.562 50.129 -5.110 1.00 24.26 ? 400 LEU B CD1 1 ATOM 7940 C CD2 . LEU B 1 400 ? 39.794 50.862 -2.824 1.00 23.22 ? 400 LEU B CD2 1 ATOM 7941 N N . ALA B 1 401 ? 35.950 52.728 -6.371 1.00 24.33 ? 401 ALA B N 1 ATOM 7942 C CA . ALA B 1 401 ? 35.479 53.881 -7.108 1.00 25.21 ? 401 ALA B CA 1 ATOM 7943 C C . ALA B 1 401 ? 34.022 54.094 -6.993 1.00 23.63 ? 401 ALA B C 1 ATOM 7944 O O . ALA B 1 401 ? 33.549 55.217 -7.246 1.00 24.64 ? 401 ALA B O 1 ATOM 7945 C CB . ALA B 1 401 ? 35.873 53.759 -8.584 1.00 27.28 ? 401 ALA B CB 1 ATOM 7946 N N . LYS B 1 402 ? 33.254 53.064 -6.626 1.00 21.38 ? 402 LYS B N 1 ATOM 7947 C CA . LYS B 1 402 ? 31.821 53.314 -6.365 1.00 23.61 ? 402 LYS B CA 1 ATOM 7948 C C . LYS B 1 402 ? 31.543 53.695 -4.928 1.00 23.96 ? 402 LYS B C 1 ATOM 7949 O O . LYS B 1 402 ? 32.400 53.518 -4.062 1.00 23.88 ? 402 LYS B O 1 ATOM 7950 C CB . LYS B 1 402 ? 30.999 52.104 -6.799 1.00 24.07 ? 402 LYS B CB 1 ATOM 7951 C CG . LYS B 1 402 ? 31.154 51.827 -8.290 1.00 25.40 ? 402 LYS B CG 1 ATOM 7952 C CD . LYS B 1 402 ? 30.494 52.876 -9.164 1.00 26.80 ? 402 LYS B CD 1 ATOM 7953 C CE . LYS B 1 402 ? 30.788 52.555 -10.622 1.00 26.51 ? 402 LYS B CE 1 ATOM 7954 N NZ . LYS B 1 402 ? 30.065 53.491 -11.474 1.00 29.50 ? 402 LYS B NZ 1 ATOM 7955 N N . ASN B 1 403 ? 30.354 54.236 -4.689 1.00 23.09 ? 403 ASN B N 1 ATOM 7956 C CA . ASN B 1 403 ? 29.915 54.659 -3.343 1.00 25.35 ? 403 ASN B CA 1 ATOM 7957 C C . ASN B 1 403 ? 29.005 53.639 -2.595 1.00 24.63 ? 403 ASN B C 1 ATOM 7958 O O . ASN B 1 403 ? 28.315 52.883 -3.215 1.00 23.75 ? 403 ASN B O 1 ATOM 7959 C CB . ASN B 1 403 ? 29.127 55.955 -3.488 1.00 25.75 ? 403 ASN B CB 1 ATOM 7960 C CG . ASN B 1 403 ? 29.983 57.100 -4.036 1.00 32.06 ? 403 ASN B CG 1 ATOM 7961 O OD1 . ASN B 1 403 ? 31.195 56.969 -4.140 1.00 41.22 ? 403 ASN B OD1 1 ATOM 7962 N ND2 . ASN B 1 403 ? 29.368 58.238 -4.337 1.00 35.74 ? 403 ASN B ND2 1 ATOM 7963 N N . SER B 1 404 ? 29.038 53.666 -1.263 1.00 22.54 ? 404 SER B N 1 ATOM 7964 C CA . SER B 1 404 ? 28.003 53.069 -0.438 1.00 20.05 ? 404 SER B CA 1 ATOM 7965 C C . SER B 1 404 ? 26.750 53.865 -0.644 1.00 20.42 ? 404 SER B C 1 ATOM 7966 O O . SER B 1 404 ? 26.772 55.060 -1.040 1.00 21.19 ? 404 SER B O 1 ATOM 7967 C CB . SER B 1 404 ? 28.374 53.046 1.039 1.00 20.01 ? 404 SER B CB 1 ATOM 7968 O OG . SER B 1 404 ? 29.527 52.281 1.343 1.00 16.74 ? 404 SER B OG 1 ATOM 7969 N N . LYS B 1 405 ? 25.609 53.214 -0.421 1.00 18.42 ? 405 LYS B N 1 ATOM 7970 C CA . LYS B 1 405 ? 24.368 53.944 -0.217 1.00 16.93 ? 405 LYS B CA 1 ATOM 7971 C C . LYS B 1 405 ? 24.422 54.753 1.092 1.00 17.28 ? 405 LYS B C 1 ATOM 7972 O O . LYS B 1 405 ? 25.028 54.345 2.089 1.00 16.05 ? 405 LYS B O 1 ATOM 7973 C CB . LYS B 1 405 ? 23.187 52.981 -0.190 1.00 16.78 ? 405 LYS B CB 1 ATOM 7974 C CG . LYS B 1 405 ? 21.825 53.620 -0.005 1.00 17.61 ? 405 LYS B CG 1 ATOM 7975 C CD . LYS B 1 405 ? 20.767 52.571 0.196 1.00 17.25 ? 405 LYS B CD 1 ATOM 7976 C CE . LYS B 1 405 ? 19.451 53.175 0.673 1.00 17.21 ? 405 LYS B CE 1 ATOM 7977 N NZ . LYS B 1 405 ? 19.572 53.863 2.010 1.00 19.28 ? 405 LYS B NZ 1 ATOM 7978 N N . LEU B 1 406 ? 23.699 55.868 1.114 1.00 19.68 ? 406 LEU B N 1 ATOM 7979 C CA . LEU B 1 406 ? 23.538 56.648 2.332 1.00 19.38 ? 406 LEU B CA 1 ATOM 7980 C C . LEU B 1 406 ? 22.249 56.282 2.955 1.00 17.62 ? 406 LEU B C 1 ATOM 7981 O O . LEU B 1 406 ? 21.210 56.354 2.323 1.00 18.34 ? 406 LEU B O 1 ATOM 7982 C CB . LEU B 1 406 ? 23.536 58.186 2.025 1.00 20.65 ? 406 LEU B CB 1 ATOM 7983 C CG . LEU B 1 406 ? 23.652 59.091 3.257 1.00 19.87 ? 406 LEU B CG 1 ATOM 7984 C CD1 . LEU B 1 406 ? 24.989 58.898 3.954 1.00 19.94 ? 406 LEU B CD1 1 ATOM 7985 C CD2 . LEU B 1 406 ? 23.514 60.568 2.904 1.00 23.47 ? 406 LEU B CD2 1 ATOM 7986 N N . MET B 1 407 ? 22.257 56.012 4.242 1.00 18.49 ? 407 MET B N 1 ATOM 7987 C CA . MET B 1 407 ? 20.962 55.959 4.950 1.00 19.00 ? 407 MET B CA 1 ATOM 7988 C C . MET B 1 407 ? 20.185 57.266 4.801 1.00 20.17 ? 407 MET B C 1 ATOM 7989 O O . MET B 1 407 ? 20.711 58.335 5.021 1.00 20.89 ? 407 MET B O 1 ATOM 7990 C CB . MET B 1 407 ? 21.144 55.590 6.401 1.00 20.74 ? 407 MET B CB 1 ATOM 7991 C CG . MET B 1 407 ? 19.832 55.378 7.104 1.00 22.81 ? 407 MET B CG 1 ATOM 7992 S SD . MET B 1 407 ? 19.201 56.998 7.575 1.00 31.37 ? 407 MET B SD 1 ATOM 7993 C CE . MET B 1 407 ? 17.541 56.466 8.058 1.00 37.08 ? 407 MET B CE 1 ATOM 7994 N N . ASN B 1 408 ? 18.951 57.183 4.367 1.00 21.44 ? 408 ASN B N 1 ATOM 7995 C CA . ASN B 1 408 ? 18.102 58.334 4.251 1.00 24.72 ? 408 ASN B CA 1 ATOM 7996 C C . ASN B 1 408 ? 16.813 58.012 4.970 1.00 22.44 ? 408 ASN B C 1 ATOM 7997 O O . ASN B 1 408 ? 16.336 56.933 4.794 1.00 22.90 ? 408 ASN B O 1 ATOM 7998 C CB . ASN B 1 408 ? 17.725 58.562 2.786 1.00 29.02 ? 408 ASN B CB 1 ATOM 7999 C CG . ASN B 1 408 ? 18.685 59.428 2.031 1.00 34.34 ? 408 ASN B CG 1 ATOM 8000 O OD1 . ASN B 1 408 ? 18.349 60.531 1.701 1.00 46.37 ? 408 ASN B OD1 1 ATOM 8001 N ND2 . ASN B 1 408 ? 19.823 58.898 1.661 1.00 35.09 ? 408 ASN B ND2 1 ATOM 8002 N N . GLN B 1 409 ? 16.218 58.959 5.689 1.00 21.14 ? 409 GLN B N 1 ATOM 8003 C CA . GLN B 1 409 ? 14.940 58.684 6.373 1.00 22.99 ? 409 GLN B CA 1 ATOM 8004 C C . GLN B 1 409 ? 13.770 58.349 5.438 1.00 22.88 ? 409 GLN B C 1 ATOM 8005 O O . GLN B 1 409 ? 12.831 57.675 5.845 1.00 20.10 ? 409 GLN B O 1 ATOM 8006 C CB . GLN B 1 409 ? 14.534 59.860 7.305 1.00 22.74 ? 409 GLN B CB 1 ATOM 8007 C CG . GLN B 1 409 ? 15.442 60.008 8.538 1.00 23.33 ? 409 GLN B CG 1 ATOM 8008 C CD . GLN B 1 409 ? 14.997 61.174 9.434 1.00 23.86 ? 409 GLN B CD 1 ATOM 8009 O OE1 . GLN B 1 409 ? 14.643 62.241 8.940 1.00 24.32 ? 409 GLN B OE1 1 ATOM 8010 N NE2 . GLN B 1 409 ? 14.979 60.954 10.730 1.00 23.74 ? 409 GLN B NE2 1 ATOM 8011 N N . ASN B 1 410 ? 13.791 58.861 4.205 1.00 23.37 ? 410 ASN B N 1 ATOM 8012 C CA . ASN B 1 410 ? 12.756 58.481 3.262 1.00 26.29 ? 410 ASN B CA 1 ATOM 8013 C C . ASN B 1 410 ? 13.253 57.506 2.184 1.00 21.18 ? 410 ASN B C 1 ATOM 8014 O O . ASN B 1 410 ? 12.484 57.231 1.269 1.00 21.06 ? 410 ASN B O 1 ATOM 8015 C CB . ASN B 1 410 ? 12.139 59.703 2.589 1.00 28.03 ? 410 ASN B CB 1 ATOM 8016 C CG . ASN B 1 410 ? 13.147 60.436 1.731 1.00 34.40 ? 410 ASN B CG 1 ATOM 8017 O OD1 . ASN B 1 410 ? 14.342 60.211 1.851 1.00 38.47 ? 410 ASN B OD1 1 ATOM 8018 N ND2 . ASN B 1 410 ? 12.674 61.294 0.835 1.00 44.00 ? 410 ASN B ND2 1 ATOM 8019 N N . LYS B 1 411 ? 14.504 57.024 2.301 1.00 17.25 ? 411 LYS B N 1 ATOM 8020 C CA . LYS B 1 411 ? 15.083 56.001 1.387 1.00 17.44 ? 411 LYS B CA 1 ATOM 8021 C C . LYS B 1 411 ? 15.997 55.048 2.168 1.00 15.31 ? 411 LYS B C 1 ATOM 8022 O O . LYS B 1 411 ? 17.184 55.168 2.169 1.00 14.98 ? 411 LYS B O 1 ATOM 8023 C CB . LYS B 1 411 ? 15.853 56.641 0.214 1.00 17.07 ? 411 LYS B CB 1 ATOM 8024 C CG . LYS B 1 411 ? 14.995 57.601 -0.621 1.00 18.03 ? 411 LYS B CG 1 ATOM 8025 C CD . LYS B 1 411 ? 15.819 58.060 -1.793 1.00 19.74 ? 411 LYS B CD 1 ATOM 8026 C CE . LYS B 1 411 ? 14.960 58.940 -2.700 1.00 21.03 ? 411 LYS B CE 1 ATOM 8027 N NZ . LYS B 1 411 ? 15.860 59.334 -3.797 1.00 24.03 ? 411 LYS B NZ 1 ATOM 8028 N N . MET B 1 412 ? 15.370 54.157 2.912 1.00 14.44 ? 412 MET B N 1 ATOM 8029 C CA . MET B 1 412 ? 16.084 53.338 3.872 1.00 13.76 ? 412 MET B CA 1 ATOM 8030 C C . MET B 1 412 ? 16.777 52.095 3.295 1.00 13.53 ? 412 MET B C 1 ATOM 8031 O O . MET B 1 412 ? 18.006 51.980 3.397 1.00 13.23 ? 412 MET B O 1 ATOM 8032 C CB . MET B 1 412 ? 15.134 52.943 5.024 1.00 14.54 ? 412 MET B CB 1 ATOM 8033 C CG . MET B 1 412 ? 14.846 54.124 6.003 1.00 16.50 ? 412 MET B CG 1 ATOM 8034 S SD . MET B 1 412 ? 13.944 53.522 7.438 1.00 17.68 ? 412 MET B SD 1 ATOM 8035 C CE . MET B 1 412 ? 13.665 55.024 8.363 1.00 19.29 ? 412 MET B CE 1 ATOM 8036 N N . VAL B 1 413 ? 16.020 51.175 2.718 1.00 11.86 ? 413 VAL B N 1 ATOM 8037 C CA . VAL B 1 413 ? 16.592 49.927 2.218 1.00 12.52 ? 413 VAL B CA 1 ATOM 8038 C C . VAL B 1 413 ? 16.175 49.704 0.790 1.00 12.49 ? 413 VAL B C 1 ATOM 8039 O O . VAL B 1 413 ? 14.962 49.680 0.498 1.00 12.67 ? 413 VAL B O 1 ATOM 8040 C CB . VAL B 1 413 ? 16.184 48.702 3.070 1.00 13.11 ? 413 VAL B CB 1 ATOM 8041 C CG1 . VAL B 1 413 ? 16.727 47.428 2.459 1.00 13.86 ? 413 VAL B CG1 1 ATOM 8042 C CG2 . VAL B 1 413 ? 16.676 48.838 4.511 1.00 13.61 ? 413 VAL B CG2 1 ATOM 8043 N N . THR B 1 414 ? 17.171 49.600 -0.088 1.00 14.31 ? 414 THR B N 1 ATOM 8044 C CA . THR B 1 414 ? 16.943 49.340 -1.518 1.00 15.94 ? 414 THR B CA 1 ATOM 8045 C C . THR B 1 414 ? 16.047 48.095 -1.747 1.00 14.96 ? 414 THR B C 1 ATOM 8046 O O . THR B 1 414 ? 16.167 47.067 -1.083 1.00 14.86 ? 414 THR B O 1 ATOM 8047 C CB . THR B 1 414 ? 18.265 49.137 -2.318 1.00 17.67 ? 414 THR B CB 1 ATOM 8048 O OG1 . THR B 1 414 ? 17.927 48.917 -3.704 1.00 18.36 ? 414 THR B OG1 1 ATOM 8049 C CG2 . THR B 1 414 ? 19.042 47.962 -1.844 1.00 17.53 ? 414 THR B CG2 1 ATOM 8050 N N . SER B 1 415 ? 15.190 48.189 -2.756 1.00 14.77 ? 415 SER B N 1 ATOM 8051 C CA . SER B 1 415 ? 14.310 47.095 -3.072 1.00 15.28 ? 415 SER B CA 1 ATOM 8052 C C . SER B 1 415 ? 15.049 45.825 -3.501 1.00 14.94 ? 415 SER B C 1 ATOM 8053 O O . SER B 1 415 ? 14.426 44.761 -3.467 1.00 13.26 ? 415 SER B O 1 ATOM 8054 C CB . SER B 1 415 ? 13.280 47.506 -4.153 1.00 15.72 ? 415 SER B CB 1 ATOM 8055 O OG . SER B 1 415 ? 12.481 48.536 -3.595 1.00 21.59 ? 415 SER B OG 1 ATOM 8056 N N . GLU B 1 416 ? 16.304 45.931 -3.946 1.00 14.90 ? 416 GLU B N 1 ATOM 8057 C CA . GLU B 1 416 ? 17.108 44.742 -4.213 1.00 15.84 ? 416 GLU B CA 1 ATOM 8058 C C . GLU B 1 416 ? 17.171 43.810 -2.974 1.00 16.45 ? 416 GLU B C 1 ATOM 8059 O O . GLU B 1 416 ? 17.258 42.571 -3.107 1.00 12.82 ? 416 GLU B O 1 ATOM 8060 C CB . GLU B 1 416 ? 18.514 45.138 -4.662 1.00 17.49 ? 416 GLU B CB 1 ATOM 8061 C CG . GLU B 1 416 ? 18.573 45.974 -5.942 1.00 17.33 ? 416 GLU B CG 1 ATOM 8062 C CD . GLU B 1 416 ? 18.067 45.193 -7.168 1.00 17.82 ? 416 GLU B CD 1 ATOM 8063 O OE1 . GLU B 1 416 ? 18.595 44.108 -7.479 1.00 17.40 ? 416 GLU B OE1 1 ATOM 8064 O OE2 . GLU B 1 416 ? 17.091 45.659 -7.786 1.00 19.81 ? 416 GLU B OE2 1 ATOM 8065 N N . LEU B 1 417 ? 17.113 44.426 -1.775 1.00 15.76 ? 417 LEU B N 1 ATOM 8066 C CA . LEU B 1 417 ? 17.084 43.714 -0.495 1.00 15.41 ? 417 LEU B CA 1 ATOM 8067 C C . LEU B 1 417 ? 15.731 43.630 0.116 1.00 14.96 ? 417 LEU B C 1 ATOM 8068 O O . LEU B 1 417 ? 15.419 42.660 0.795 1.00 15.49 ? 417 LEU B O 1 ATOM 8069 C CB . LEU B 1 417 ? 18.023 44.400 0.508 1.00 14.98 ? 417 LEU B CB 1 ATOM 8070 C CG . LEU B 1 417 ? 19.490 44.372 0.273 1.00 14.72 ? 417 LEU B CG 1 ATOM 8071 C CD1 . LEU B 1 417 ? 20.186 45.357 1.197 1.00 15.40 ? 417 LEU B CD1 1 ATOM 8072 C CD2 . LEU B 1 417 ? 20.074 42.972 0.483 1.00 15.86 ? 417 LEU B CD2 1 ATOM 8073 N N . ARG B 1 418 ? 14.885 44.633 -0.140 1.00 16.14 ? 418 ARG B N 1 ATOM 8074 C CA . ARG B 1 418 ? 13.587 44.703 0.542 1.00 16.24 ? 418 ARG B CA 1 ATOM 8075 C C . ARG B 1 418 ? 12.538 43.886 -0.193 1.00 16.22 ? 418 ARG B C 1 ATOM 8076 O O . ARG B 1 418 ? 11.565 43.487 0.366 1.00 15.25 ? 418 ARG B O 1 ATOM 8077 C CB . ARG B 1 418 ? 13.148 46.150 0.680 1.00 16.89 ? 418 ARG B CB 1 ATOM 8078 C CG . ARG B 1 418 ? 12.144 46.402 1.799 1.00 15.68 ? 418 ARG B CG 1 ATOM 8079 C CD . ARG B 1 418 ? 11.657 47.815 1.760 1.00 16.98 ? 418 ARG B CD 1 ATOM 8080 N NE . ARG B 1 418 ? 10.778 48.049 0.592 1.00 15.04 ? 418 ARG B NE 1 ATOM 8081 C CZ . ARG B 1 418 ? 9.535 47.663 0.531 1.00 14.71 ? 418 ARG B CZ 1 ATOM 8082 N NH1 . ARG B 1 418 ? 8.948 47.049 1.547 1.00 17.48 ? 418 ARG B NH1 1 ATOM 8083 N NH2 . ARG B 1 418 ? 8.847 47.911 -0.563 1.00 15.62 ? 418 ARG B NH2 1 ATOM 8084 N N . ASN B 1 419 ? 12.759 43.632 -1.478 1.00 15.96 ? 419 ASN B N 1 ATOM 8085 C CA . ASN B 1 419 ? 11.832 42.860 -2.228 1.00 14.24 ? 419 ASN B CA 1 ATOM 8086 C C . ASN B 1 419 ? 12.435 41.715 -2.911 1.00 15.66 ? 419 ASN B C 1 ATOM 8087 O O . ASN B 1 419 ? 11.687 40.769 -3.227 1.00 17.40 ? 419 ASN B O 1 ATOM 8088 C CB . ASN B 1 419 ? 11.099 43.707 -3.253 1.00 13.80 ? 419 ASN B CB 1 ATOM 8089 C CG . ASN B 1 419 ? 10.065 44.557 -2.625 1.00 15.35 ? 419 ASN B CG 1 ATOM 8090 O OD1 . ASN B 1 419 ? 9.308 44.137 -1.750 1.00 13.16 ? 419 ASN B OD1 1 ATOM 8091 N ND2 . ASN B 1 419 ? 9.966 45.787 -3.120 1.00 17.01 ? 419 ASN B ND2 1 ATOM 8092 N N . LYS B 1 420 ? 13.755 41.748 -3.163 1.00 15.51 ? 420 LYS B N 1 ATOM 8093 C CA . LYS B 1 420 ? 14.347 40.675 -3.996 1.00 17.22 ? 420 LYS B CA 1 ATOM 8094 C C . LYS B 1 420 ? 15.406 39.777 -3.395 1.00 17.46 ? 420 LYS B C 1 ATOM 8095 O O . LYS B 1 420 ? 16.159 39.121 -4.128 1.00 15.40 ? 420 LYS B O 1 ATOM 8096 C CB . LYS B 1 420 ? 14.855 41.284 -5.316 1.00 17.12 ? 420 LYS B CB 1 ATOM 8097 C CG . LYS B 1 420 ? 13.713 42.049 -6.016 1.00 17.44 ? 420 LYS B CG 1 ATOM 8098 C CD . LYS B 1 420 ? 14.171 42.665 -7.358 1.00 20.68 ? 420 LYS B CD 1 ATOM 8099 C CE . LYS B 1 420 ? 12.994 43.209 -8.129 1.00 25.24 ? 420 LYS B CE 1 ATOM 8100 N NZ . LYS B 1 420 ? 13.427 43.648 -9.452 1.00 28.53 ? 420 LYS B NZ 1 ATOM 8101 N N . LEU B 1 421 ? 15.431 39.706 -2.057 1.00 16.78 ? 421 LEU B N 1 ATOM 8102 C CA . LEU B 1 421 ? 16.407 38.906 -1.404 1.00 15.52 ? 421 LEU B CA 1 ATOM 8103 C C . LEU B 1 421 ? 16.194 37.430 -1.730 1.00 16.13 ? 421 LEU B C 1 ATOM 8104 O O . LEU B 1 421 ? 15.095 36.941 -1.731 1.00 14.55 ? 421 LEU B O 1 ATOM 8105 C CB . LEU B 1 421 ? 16.318 39.122 0.095 1.00 16.94 ? 421 LEU B CB 1 ATOM 8106 C CG . LEU B 1 421 ? 17.375 38.397 0.960 1.00 17.79 ? 421 LEU B CG 1 ATOM 8107 C CD1 . LEU B 1 421 ? 18.709 39.033 0.746 1.00 17.77 ? 421 LEU B CD1 1 ATOM 8108 C CD2 . LEU B 1 421 ? 16.939 38.405 2.447 1.00 17.30 ? 421 LEU B CD2 1 ATOM 8109 N N . PHE B 1 422 ? 17.282 36.743 -1.991 1.00 17.25 ? 422 PHE B N 1 ATOM 8110 C CA . PHE B 1 422 ? 17.295 35.312 -2.188 1.00 17.42 ? 422 PHE B CA 1 ATOM 8111 C C . PHE B 1 422 ? 17.844 34.689 -0.894 1.00 20.82 ? 422 PHE B C 1 ATOM 8112 O O . PHE B 1 422 ? 18.877 35.131 -0.389 1.00 18.69 ? 422 PHE B O 1 ATOM 8113 C CB . PHE B 1 422 ? 18.231 34.977 -3.307 1.00 19.17 ? 422 PHE B CB 1 ATOM 8114 C CG . PHE B 1 422 ? 18.264 33.515 -3.619 1.00 18.85 ? 422 PHE B CG 1 ATOM 8115 C CD1 . PHE B 1 422 ? 17.351 32.990 -4.507 1.00 20.38 ? 422 PHE B CD1 1 ATOM 8116 C CD2 . PHE B 1 422 ? 19.133 32.669 -2.998 1.00 21.78 ? 422 PHE B CD2 1 ATOM 8117 C CE1 . PHE B 1 422 ? 17.375 31.629 -4.801 1.00 21.41 ? 422 PHE B CE1 1 ATOM 8118 C CE2 . PHE B 1 422 ? 19.144 31.321 -3.270 1.00 20.55 ? 422 PHE B CE2 1 ATOM 8119 C CZ . PHE B 1 422 ? 18.234 30.812 -4.156 1.00 19.19 ? 422 PHE B CZ 1 ATOM 8120 N N . GLN B 1 423 ? 17.153 33.705 -0.368 1.00 20.89 ? 423 GLN B N 1 ATOM 8121 C CA . GLN B 1 423 ? 17.554 33.014 0.852 1.00 23.11 ? 423 GLN B CA 1 ATOM 8122 C C . GLN B 1 423 ? 17.950 31.617 0.439 1.00 23.28 ? 423 GLN B C 1 ATOM 8123 O O . GLN B 1 423 ? 17.263 31.010 -0.385 1.00 23.67 ? 423 GLN B O 1 ATOM 8124 C CB . GLN B 1 423 ? 16.368 32.895 1.800 1.00 26.40 ? 423 GLN B CB 1 ATOM 8125 C CG . GLN B 1 423 ? 15.938 34.237 2.350 1.00 27.45 ? 423 GLN B CG 1 ATOM 8126 C CD . GLN B 1 423 ? 16.666 34.562 3.613 1.00 31.03 ? 423 GLN B CD 1 ATOM 8127 O OE1 . GLN B 1 423 ? 16.104 34.436 4.692 1.00 40.50 ? 423 GLN B OE1 1 ATOM 8128 N NE2 . GLN B 1 423 ? 17.945 34.908 3.504 1.00 30.61 ? 423 GLN B NE2 1 ATOM 8129 N N . PRO B 1 424 ? 19.028 31.104 1.028 1.00 25.65 ? 424 PRO B N 1 ATOM 8130 C CA . PRO B 1 424 ? 19.650 29.884 0.506 1.00 30.36 ? 424 PRO B CA 1 ATOM 8131 C C . PRO B 1 424 ? 18.804 28.624 0.567 1.00 35.01 ? 424 PRO B C 1 ATOM 8132 O O . PRO B 1 424 ? 19.015 27.746 -0.274 1.00 46.98 ? 424 PRO B O 1 ATOM 8133 C CB . PRO B 1 424 ? 20.934 29.739 1.319 1.00 27.87 ? 424 PRO B CB 1 ATOM 8134 C CG . PRO B 1 424 ? 20.849 30.734 2.433 1.00 29.32 ? 424 PRO B CG 1 ATOM 8135 C CD . PRO B 1 424 ? 19.882 31.791 2.032 1.00 25.08 ? 424 PRO B CD 1 ATOM 8136 N N . THR B 1 425 ? 17.824 28.536 1.465 1.00 33.02 ? 425 THR B N 1 ATOM 8137 C CA . THR B 1 425 ? 17.020 27.318 1.482 1.00 37.21 ? 425 THR B CA 1 ATOM 8138 C C . THR B 1 425 ? 15.754 27.417 0.624 1.00 36.25 ? 425 THR B C 1 ATOM 8139 O O . THR B 1 425 ? 14.938 26.514 0.653 1.00 39.43 ? 425 THR B O 1 ATOM 8140 C CB . THR B 1 425 ? 16.669 26.914 2.928 1.00 37.21 ? 425 THR B CB 1 ATOM 8141 O OG1 . THR B 1 425 ? 15.762 27.861 3.501 1.00 42.53 ? 425 THR B OG1 1 ATOM 8142 C CG2 . THR B 1 425 ? 17.925 26.901 3.806 1.00 37.01 ? 425 THR B CG2 1 ATOM 8143 N N . HIS B 1 426 ? 15.561 28.544 -0.076 1.00 33.15 ? 426 HIS B N 1 ATOM 8144 C CA . HIS B 1 426 ? 14.354 28.804 -0.885 1.00 29.64 ? 426 HIS B CA 1 ATOM 8145 C C . HIS B 1 426 ? 14.717 29.118 -2.319 1.00 29.12 ? 426 HIS B C 1 ATOM 8146 O O . HIS B 1 426 ? 15.871 29.101 -2.688 1.00 31.19 ? 426 HIS B O 1 ATOM 8147 C CB . HIS B 1 426 ? 13.532 29.923 -0.259 1.00 29.50 ? 426 HIS B CB 1 ATOM 8148 C CG . HIS B 1 426 ? 13.173 29.630 1.154 1.00 31.95 ? 426 HIS B CG 1 ATOM 8149 N ND1 . HIS B 1 426 ? 12.099 28.835 1.495 1.00 33.49 ? 426 HIS B ND1 1 ATOM 8150 C CD2 . HIS B 1 426 ? 13.804 29.930 2.308 1.00 31.28 ? 426 HIS B CD2 1 ATOM 8151 C CE1 . HIS B 1 426 ? 12.063 28.693 2.800 1.00 32.64 ? 426 HIS B CE1 1 ATOM 8152 N NE2 . HIS B 1 426 ? 13.094 29.338 3.314 1.00 31.97 ? 426 HIS B NE2 1 ATOM 8153 N N . LYS B 1 427 ? 13.729 29.296 -3.151 1.00 29.02 ? 427 LYS B N 1 ATOM 8154 C CA . LYS B 1 427 ? 13.937 29.309 -4.569 1.00 28.42 ? 427 LYS B CA 1 ATOM 8155 C C . LYS B 1 427 ? 13.688 30.630 -5.282 1.00 26.51 ? 427 LYS B C 1 ATOM 8156 O O . LYS B 1 427 ? 13.858 30.716 -6.450 1.00 28.67 ? 427 LYS B O 1 ATOM 8157 C CB . LYS B 1 427 ? 13.101 28.237 -5.215 1.00 33.27 ? 427 LYS B CB 1 ATOM 8158 C CG . LYS B 1 427 ? 13.499 26.819 -4.907 1.00 39.45 ? 427 LYS B CG 1 ATOM 8159 C CD . LYS B 1 427 ? 12.288 25.935 -4.952 1.00 51.01 ? 427 LYS B CD 1 ATOM 8160 C CE . LYS B 1 427 ? 12.614 24.461 -4.718 1.00 54.76 ? 427 LYS B CE 1 ATOM 8161 N NZ . LYS B 1 427 ? 13.724 23.924 -5.551 1.00 55.39 ? 427 LYS B NZ 1 ATOM 8162 N N . VAL B 1 428 ? 13.282 31.636 -4.551 1.00 24.35 ? 428 VAL B N 1 ATOM 8163 C CA . VAL B 1 428 ? 12.853 32.915 -5.139 1.00 22.66 ? 428 VAL B CA 1 ATOM 8164 C C . VAL B 1 428 ? 13.690 34.103 -4.672 1.00 20.91 ? 428 VAL B C 1 ATOM 8165 O O . VAL B 1 428 ? 14.250 34.121 -3.548 1.00 22.12 ? 428 VAL B O 1 ATOM 8166 C CB . VAL B 1 428 ? 11.347 33.178 -4.907 1.00 25.32 ? 428 VAL B CB 1 ATOM 8167 C CG1 . VAL B 1 428 ? 10.491 32.071 -5.544 1.00 26.53 ? 428 VAL B CG1 1 ATOM 8168 C CG2 . VAL B 1 428 ? 10.977 33.324 -3.428 1.00 25.84 ? 428 VAL B CG2 1 ATOM 8169 N N . HIS B 1 429 ? 13.837 35.069 -5.577 1.00 18.93 ? 429 HIS B N 1 ATOM 8170 C CA . HIS B 1 429 ? 14.357 36.395 -5.265 1.00 18.27 ? 429 HIS B CA 1 ATOM 8171 C C . HIS B 1 429 ? 13.160 37.270 -4.847 1.00 19.62 ? 429 HIS B C 1 ATOM 8172 O O . HIS B 1 429 ? 12.706 38.176 -5.598 1.00 17.46 ? 429 HIS B O 1 ATOM 8173 C CB . HIS B 1 429 ? 15.061 36.978 -6.498 1.00 17.84 ? 429 HIS B CB 1 ATOM 8174 C CG . HIS B 1 429 ? 16.415 36.387 -6.763 1.00 19.03 ? 429 HIS B CG 1 ATOM 8175 N ND1 . HIS B 1 429 ? 16.610 35.108 -7.236 1.00 18.06 ? 429 HIS B ND1 1 ATOM 8176 C CD2 . HIS B 1 429 ? 17.653 36.915 -6.599 1.00 21.03 ? 429 HIS B CD2 1 ATOM 8177 C CE1 . HIS B 1 429 ? 17.901 34.882 -7.371 1.00 21.90 ? 429 HIS B CE1 1 ATOM 8178 N NE2 . HIS B 1 429 ? 18.561 35.963 -6.979 1.00 21.04 ? 429 HIS B NE2 1 ATOM 8179 N N . GLY B 1 430 ? 12.586 36.963 -3.677 1.00 16.50 ? 430 GLY B N 1 ATOM 8180 C CA . GLY B 1 430 ? 11.432 37.690 -3.267 1.00 16.13 ? 430 GLY B CA 1 ATOM 8181 C C . GLY B 1 430 ? 11.323 37.925 -1.769 1.00 15.16 ? 430 GLY B C 1 ATOM 8182 O O . GLY B 1 430 ? 10.229 38.173 -1.297 1.00 15.05 ? 430 GLY B O 1 ATOM 8183 N N . PHE B 1 431 ? 12.430 37.857 -1.023 1.00 13.57 ? 431 PHE B N 1 ATOM 8184 C CA . PHE B 1 431 ? 12.350 38.100 0.395 1.00 14.21 ? 431 PHE B CA 1 ATOM 8185 C C . PHE B 1 431 ? 12.649 39.562 0.710 1.00 15.15 ? 431 PHE B C 1 ATOM 8186 O O . PHE B 1 431 ? 13.103 40.320 -0.173 1.00 11.60 ? 431 PHE B O 1 ATOM 8187 C CB . PHE B 1 431 ? 13.300 37.129 1.104 1.00 15.45 ? 431 PHE B CB 1 ATOM 8188 C CG . PHE B 1 431 ? 12.784 35.713 1.139 1.00 17.01 ? 431 PHE B CG 1 ATOM 8189 C CD1 . PHE B 1 431 ? 13.061 34.831 0.117 1.00 19.02 ? 431 PHE B CD1 1 ATOM 8190 C CD2 . PHE B 1 431 ? 12.091 35.234 2.275 1.00 20.76 ? 431 PHE B CD2 1 ATOM 8191 C CE1 . PHE B 1 431 ? 12.619 33.498 0.180 1.00 22.57 ? 431 PHE B CE1 1 ATOM 8192 C CE2 . PHE B 1 431 ? 11.681 33.897 2.355 1.00 22.19 ? 431 PHE B CE2 1 ATOM 8193 C CZ . PHE B 1 431 ? 11.956 33.024 1.318 1.00 20.74 ? 431 PHE B CZ 1 ATOM 8194 N N . ASP B 1 432 ? 12.372 39.943 1.961 1.00 14.34 ? 432 ASP B N 1 ATOM 8195 C CA . ASP B 1 432 ? 12.479 41.343 2.394 1.00 14.03 ? 432 ASP B CA 1 ATOM 8196 C C . ASP B 1 432 ? 13.383 41.338 3.630 1.00 14.38 ? 432 ASP B C 1 ATOM 8197 O O . ASP B 1 432 ? 12.925 40.989 4.706 1.00 12.08 ? 432 ASP B O 1 ATOM 8198 C CB . ASP B 1 432 ? 11.098 41.866 2.743 1.00 14.75 ? 432 ASP B CB 1 ATOM 8199 C CG . ASP B 1 432 ? 11.128 43.312 3.266 1.00 14.59 ? 432 ASP B CG 1 ATOM 8200 O OD1 . ASP B 1 432 ? 12.185 43.821 3.667 1.00 16.27 ? 432 ASP B OD1 1 ATOM 8201 O OD2 . ASP B 1 432 ? 10.036 43.876 3.287 1.00 15.21 ? 432 ASP B OD2 1 ATOM 8202 N N . LEU B 1 433 ? 14.658 41.694 3.467 1.00 12.00 ? 433 LEU B N 1 ATOM 8203 C CA . LEU B 1 433 ? 15.556 41.774 4.584 1.00 12.77 ? 433 LEU B CA 1 ATOM 8204 C C . LEU B 1 433 ? 15.089 42.710 5.740 1.00 14.79 ? 433 LEU B C 1 ATOM 8205 O O . LEU B 1 433 ? 15.414 42.454 6.941 1.00 15.42 ? 433 LEU B O 1 ATOM 8206 C CB . LEU B 1 433 ? 16.965 42.205 4.086 1.00 12.37 ? 433 LEU B CB 1 ATOM 8207 C CG . LEU B 1 433 ? 18.063 42.169 5.162 1.00 13.09 ? 433 LEU B CG 1 ATOM 8208 C CD1 . LEU B 1 433 ? 18.162 40.777 5.789 1.00 13.25 ? 433 LEU B CD1 1 ATOM 8209 C CD2 . LEU B 1 433 ? 19.400 42.595 4.475 1.00 13.02 ? 433 LEU B CD2 1 ATOM 8210 N N . ALA B 1 434 ? 14.368 43.785 5.405 1.00 15.09 ? 434 ALA B N 1 ATOM 8211 C CA . ALA B 1 434 ? 13.889 44.673 6.459 1.00 14.86 ? 434 ALA B CA 1 ATOM 8212 C C . ALA B 1 434 ? 12.806 44.030 7.287 1.00 14.08 ? 434 ALA B C 1 ATOM 8213 O O . ALA B 1 434 ? 12.864 44.075 8.510 1.00 15.81 ? 434 ALA B O 1 ATOM 8214 C CB . ALA B 1 434 ? 13.428 46.010 5.908 1.00 13.91 ? 434 ALA B CB 1 ATOM 8215 N N . ALA B 1 435 ? 11.824 43.442 6.645 1.00 15.59 ? 435 ALA B N 1 ATOM 8216 C CA . ALA B 1 435 ? 10.800 42.664 7.345 1.00 15.36 ? 435 ALA B CA 1 ATOM 8217 C C . ALA B 1 435 ? 11.439 41.544 8.185 1.00 14.76 ? 435 ALA B C 1 ATOM 8218 O O . ALA B 1 435 ? 11.027 41.298 9.312 1.00 15.54 ? 435 ALA B O 1 ATOM 8219 C CB . ALA B 1 435 ? 9.833 42.034 6.380 1.00 15.21 ? 435 ALA B CB 1 ATOM 8220 N N . ILE B 1 436 ? 12.422 40.883 7.625 1.00 13.41 ? 436 ILE B N 1 ATOM 8221 C CA . ILE B 1 436 ? 13.092 39.801 8.299 1.00 14.65 ? 436 ILE B CA 1 ATOM 8222 C C . ILE B 1 436 ? 13.796 40.317 9.558 1.00 14.81 ? 436 ILE B C 1 ATOM 8223 O O . ILE B 1 436 ? 13.781 39.689 10.632 1.00 14.33 ? 436 ILE B O 1 ATOM 8224 C CB . ILE B 1 436 ? 14.114 39.081 7.391 1.00 15.56 ? 436 ILE B CB 1 ATOM 8225 C CG1 . ILE B 1 436 ? 13.402 38.232 6.379 1.00 17.72 ? 436 ILE B CG1 1 ATOM 8226 C CG2 . ILE B 1 436 ? 15.017 38.194 8.206 1.00 15.54 ? 436 ILE B CG2 1 ATOM 8227 C CD1 . ILE B 1 436 ? 14.346 37.687 5.299 1.00 16.61 ? 436 ILE B CD1 1 ATOM 8228 N N . ASN B 1 437 ? 14.448 41.470 9.429 1.00 15.15 ? 437 ASN B N 1 ATOM 8229 C CA . ASN B 1 437 ? 15.139 42.042 10.580 1.00 13.79 ? 437 ASN B CA 1 ATOM 8230 C C . ASN B 1 437 ? 14.130 42.370 11.721 1.00 15.00 ? 437 ASN B C 1 ATOM 8231 O O . ASN B 1 437 ? 14.428 42.202 12.941 1.00 14.02 ? 437 ASN B O 1 ATOM 8232 C CB . ASN B 1 437 ? 15.850 43.348 10.220 1.00 12.88 ? 437 ASN B CB 1 ATOM 8233 C CG . ASN B 1 437 ? 17.087 43.173 9.353 1.00 13.09 ? 437 ASN B CG 1 ATOM 8234 O OD1 . ASN B 1 437 ? 17.750 42.158 9.296 1.00 12.19 ? 437 ASN B OD1 1 ATOM 8235 N ND2 . ASN B 1 437 ? 17.444 44.277 8.730 1.00 12.41 ? 437 ASN B ND2 1 ATOM 8236 N N . LEU B 1 438 ? 13.031 42.990 11.336 1.00 14.16 ? 438 LEU B N 1 ATOM 8237 C CA . LEU B 1 438 ? 11.993 43.336 12.302 1.00 16.40 ? 438 LEU B CA 1 ATOM 8238 C C . LEU B 1 438 ? 11.387 42.086 12.949 1.00 17.18 ? 438 LEU B C 1 ATOM 8239 O O . LEU B 1 438 ? 11.281 42.010 14.191 1.00 16.52 ? 438 LEU B O 1 ATOM 8240 C CB . LEU B 1 438 ? 10.928 44.158 11.682 1.00 15.26 ? 438 LEU B CB 1 ATOM 8241 C CG . LEU B 1 438 ? 11.347 45.566 11.273 1.00 14.61 ? 438 LEU B CG 1 ATOM 8242 C CD1 . LEU B 1 438 ? 10.201 46.143 10.444 1.00 16.11 ? 438 LEU B CD1 1 ATOM 8243 C CD2 . LEU B 1 438 ? 11.658 46.452 12.455 1.00 13.58 ? 438 LEU B CD2 1 ATOM 8244 N N . GLN B 1 439 ? 11.101 41.076 12.134 1.00 16.58 ? 439 GLN B N 1 ATOM 8245 C CA . GLN B 1 439 ? 10.602 39.830 12.670 1.00 15.69 ? 439 GLN B CA 1 ATOM 8246 C C . GLN B 1 439 ? 11.642 39.168 13.623 1.00 14.55 ? 439 GLN B C 1 ATOM 8247 O O . GLN B 1 439 ? 11.267 38.567 14.653 1.00 13.55 ? 439 GLN B O 1 ATOM 8248 C CB . GLN B 1 439 ? 10.221 38.854 11.535 1.00 16.52 ? 439 GLN B CB 1 ATOM 8249 C CG . GLN B 1 439 ? 9.403 37.652 11.986 1.00 17.86 ? 439 GLN B CG 1 ATOM 8250 C CD . GLN B 1 439 ? 7.892 37.909 12.056 1.00 15.86 ? 439 GLN B CD 1 ATOM 8251 O OE1 . GLN B 1 439 ? 7.412 39.029 12.259 1.00 17.77 ? 439 GLN B OE1 1 ATOM 8252 N NE2 . GLN B 1 439 ? 7.144 36.880 11.817 1.00 17.36 ? 439 GLN B NE2 1 ATOM 8253 N N . ARG B 1 440 ? 12.904 39.247 13.247 1.00 14.28 ? 440 ARG B N 1 ATOM 8254 C CA . ARG B 1 440 ? 13.991 38.697 14.005 1.00 14.75 ? 440 ARG B CA 1 ATOM 8255 C C . ARG B 1 440 ? 14.228 39.333 15.383 1.00 15.30 ? 440 ARG B C 1 ATOM 8256 O O . ARG B 1 440 ? 14.620 38.632 16.361 1.00 14.79 ? 440 ARG B O 1 ATOM 8257 C CB . ARG B 1 440 ? 15.264 38.739 13.187 1.00 15.51 ? 440 ARG B CB 1 ATOM 8258 C CG . ARG B 1 440 ? 16.406 37.949 13.803 1.00 15.64 ? 440 ARG B CG 1 ATOM 8259 C CD . ARG B 1 440 ? 16.232 36.432 13.675 1.00 17.34 ? 440 ARG B CD 1 ATOM 8260 N NE . ARG B 1 440 ? 16.268 35.909 12.297 1.00 14.29 ? 440 ARG B NE 1 ATOM 8261 C CZ . ARG B 1 440 ? 15.896 34.678 11.955 1.00 17.47 ? 440 ARG B CZ 1 ATOM 8262 N NH1 . ARG B 1 440 ? 15.358 33.826 12.830 1.00 17.00 ? 440 ARG B NH1 1 ATOM 8263 N NH2 . ARG B 1 440 ? 15.999 34.305 10.693 1.00 18.30 ? 440 ARG B NH2 1 ATOM 8264 N N . CYS B 1 441 ? 14.094 40.657 15.439 1.00 13.99 ? 441 CYS B N 1 ATOM 8265 C CA . CYS B 1 441 ? 14.089 41.403 16.682 1.00 14.29 ? 441 CYS B CA 1 ATOM 8266 C C . CYS B 1 441 ? 13.131 40.794 17.697 1.00 14.09 ? 441 CYS B C 1 ATOM 8267 O O . CYS B 1 441 ? 13.442 40.655 18.865 1.00 14.87 ? 441 CYS B O 1 ATOM 8268 C CB . CYS B 1 441 ? 13.694 42.871 16.478 1.00 14.13 ? 441 CYS B CB 1 ATOM 8269 S SG . CYS B 1 441 ? 14.947 43.958 15.716 1.00 14.53 ? 441 CYS B SG 1 ATOM 8270 N N . ARG B 1 442 ? 11.961 40.453 17.216 1.00 15.16 ? 442 ARG B N 1 ATOM 8271 C CA . ARG B 1 442 ? 10.879 39.888 18.049 1.00 16.21 ? 442 ARG B CA 1 ATOM 8272 C C . ARG B 1 442 ? 11.202 38.449 18.442 1.00 17.31 ? 442 ARG B C 1 ATOM 8273 O O . ARG B 1 442 ? 10.999 38.077 19.607 1.00 18.77 ? 442 ARG B O 1 ATOM 8274 C CB . ARG B 1 442 ? 9.614 39.940 17.246 1.00 16.33 ? 442 ARG B CB 1 ATOM 8275 C CG . ARG B 1 442 ? 9.194 41.343 16.922 1.00 15.83 ? 442 ARG B CG 1 ATOM 8276 C CD . ARG B 1 442 ? 8.021 41.485 15.972 1.00 17.25 ? 442 ARG B CD 1 ATOM 8277 N NE . ARG B 1 442 ? 7.708 42.884 15.692 1.00 20.29 ? 442 ARG B NE 1 ATOM 8278 C CZ . ARG B 1 442 ? 6.820 43.320 14.805 1.00 18.20 ? 442 ARG B CZ 1 ATOM 8279 N NH1 . ARG B 1 442 ? 6.060 42.493 14.118 1.00 17.96 ? 442 ARG B NH1 1 ATOM 8280 N NH2 . ARG B 1 442 ? 6.679 44.612 14.618 1.00 16.89 ? 442 ARG B NH2 1 ATOM 8281 N N . ASP B 1 443 ? 11.725 37.669 17.453 1.00 17.10 ? 443 ASP B N 1 ATOM 8282 C CA . ASP B 1 443 ? 12.266 36.307 17.643 1.00 18.98 ? 443 ASP B CA 1 ATOM 8283 C C . ASP B 1 443 ? 13.278 36.301 18.812 1.00 19.05 ? 443 ASP B C 1 ATOM 8284 O O . ASP B 1 443 ? 13.205 35.458 19.705 1.00 20.04 ? 443 ASP B O 1 ATOM 8285 C CB . ASP B 1 443 ? 12.929 35.842 16.353 1.00 18.91 ? 443 ASP B CB 1 ATOM 8286 C CG . ASP B 1 443 ? 13.501 34.449 16.448 1.00 21.45 ? 443 ASP B CG 1 ATOM 8287 O OD1 . ASP B 1 443 ? 13.133 33.701 17.391 1.00 21.40 ? 443 ASP B OD1 1 ATOM 8288 O OD2 . ASP B 1 443 ? 14.304 34.100 15.553 1.00 18.66 ? 443 ASP B OD2 1 ATOM 8289 N N . HIS B 1 444 ? 14.164 37.294 18.820 1.00 17.28 ? 444 HIS B N 1 ATOM 8290 C CA . HIS B 1 444 ? 15.242 37.370 19.765 1.00 17.35 ? 444 HIS B CA 1 ATOM 8291 C C . HIS B 1 444 ? 14.873 38.068 21.085 1.00 18.07 ? 444 HIS B C 1 ATOM 8292 O O . HIS B 1 444 ? 15.735 38.270 21.913 1.00 19.94 ? 444 HIS B O 1 ATOM 8293 C CB . HIS B 1 444 ? 16.440 38.107 19.190 1.00 16.49 ? 444 HIS B CB 1 ATOM 8294 C CG . HIS B 1 444 ? 17.302 37.307 18.273 1.00 15.71 ? 444 HIS B CG 1 ATOM 8295 N ND1 . HIS B 1 444 ? 18.678 37.398 18.300 1.00 19.72 ? 444 HIS B ND1 1 ATOM 8296 C CD2 . HIS B 1 444 ? 17.006 36.525 17.210 1.00 15.87 ? 444 HIS B CD2 1 ATOM 8297 C CE1 . HIS B 1 444 ? 19.189 36.599 17.366 1.00 18.19 ? 444 HIS B CE1 1 ATOM 8298 N NE2 . HIS B 1 444 ? 18.191 36.069 16.687 1.00 15.67 ? 444 HIS B NE2 1 ATOM 8299 N N . GLY B 1 445 ? 13.635 38.461 21.292 1.00 17.36 ? 445 GLY B N 1 ATOM 8300 C CA . GLY B 1 445 ? 13.227 38.986 22.544 1.00 17.58 ? 445 GLY B CA 1 ATOM 8301 C C . GLY B 1 445 ? 13.719 40.372 22.836 1.00 17.50 ? 445 GLY B C 1 ATOM 8302 O O . GLY B 1 445 ? 13.954 40.735 23.996 1.00 18.92 ? 445 GLY B O 1 ATOM 8303 N N . MET B 1 446 ? 13.894 41.156 21.792 1.00 16.67 ? 446 MET B N 1 ATOM 8304 C CA . MET B 1 446 ? 14.325 42.548 21.951 1.00 16.32 ? 446 MET B CA 1 ATOM 8305 C C . MET B 1 446 ? 13.361 43.467 22.717 1.00 15.92 ? 446 MET B C 1 ATOM 8306 O O . MET B 1 446 ? 12.182 43.638 22.371 1.00 16.38 ? 446 MET B O 1 ATOM 8307 C CB . MET B 1 446 ? 14.663 43.170 20.602 1.00 16.61 ? 446 MET B CB 1 ATOM 8308 C CG . MET B 1 446 ? 15.919 42.562 19.959 1.00 18.50 ? 446 MET B CG 1 ATOM 8309 S SD . MET B 1 446 ? 17.444 42.897 20.909 1.00 18.35 ? 446 MET B SD 1 ATOM 8310 C CE . MET B 1 446 ? 17.691 41.268 21.583 1.00 18.96 ? 446 MET B CE 1 ATOM 8311 N N . PRO B 1 447 ? 13.882 44.061 23.773 1.00 17.22 ? 447 PRO B N 1 ATOM 8312 C CA . PRO B 1 447 ? 13.291 45.221 24.319 1.00 18.01 ? 447 PRO B CA 1 ATOM 8313 C C . PRO B 1 447 ? 13.142 46.253 23.225 1.00 19.71 ? 447 PRO B C 1 ATOM 8314 O O . PRO B 1 447 ? 13.883 46.203 22.215 1.00 20.70 ? 447 PRO B O 1 ATOM 8315 C CB . PRO B 1 447 ? 14.328 45.719 25.338 1.00 18.15 ? 447 PRO B CB 1 ATOM 8316 C CG . PRO B 1 447 ? 15.148 44.538 25.643 1.00 19.36 ? 447 PRO B CG 1 ATOM 8317 C CD . PRO B 1 447 ? 15.212 43.780 24.378 1.00 18.55 ? 447 PRO B CD 1 ATOM 8318 N N . GLY B 1 448 ? 12.171 47.156 23.432 1.00 18.97 ? 448 GLY B N 1 ATOM 8319 C CA . GLY B 1 448 ? 11.813 48.097 22.461 1.00 18.55 ? 448 GLY B CA 1 ATOM 8320 C C . GLY B 1 448 ? 12.721 49.296 22.472 1.00 19.45 ? 448 GLY B C 1 ATOM 8321 O O . GLY B 1 448 ? 13.649 49.380 23.279 1.00 18.60 ? 448 GLY B O 1 ATOM 8322 N N . TYR B 1 449 ? 12.436 50.190 21.524 1.00 18.21 ? 449 TYR B N 1 ATOM 8323 C CA . TYR B 1 449 ? 13.196 51.407 21.285 1.00 19.71 ? 449 TYR B CA 1 ATOM 8324 C C . TYR B 1 449 ? 13.483 52.235 22.546 1.00 21.30 ? 449 TYR B C 1 ATOM 8325 O O . TYR B 1 449 ? 14.669 52.590 22.812 1.00 17.17 ? 449 TYR B O 1 ATOM 8326 C CB . TYR B 1 449 ? 12.401 52.262 20.298 1.00 18.59 ? 449 TYR B CB 1 ATOM 8327 C CG . TYR B 1 449 ? 13.027 53.608 19.944 1.00 18.72 ? 449 TYR B CG 1 ATOM 8328 C CD1 . TYR B 1 449 ? 14.272 53.676 19.282 1.00 17.93 ? 449 TYR B CD1 1 ATOM 8329 C CD2 . TYR B 1 449 ? 12.411 54.784 20.284 1.00 17.80 ? 449 TYR B CD2 1 ATOM 8330 C CE1 . TYR B 1 449 ? 14.844 54.903 18.990 1.00 19.86 ? 449 TYR B CE1 1 ATOM 8331 C CE2 . TYR B 1 449 ? 12.989 55.999 20.001 1.00 17.72 ? 449 TYR B CE2 1 ATOM 8332 C CZ . TYR B 1 449 ? 14.179 56.062 19.343 1.00 18.99 ? 449 TYR B CZ 1 ATOM 8333 O OH . TYR B 1 449 ? 14.724 57.318 19.046 1.00 22.37 ? 449 TYR B OH 1 ATOM 8334 N N . ASN B 1 450 ? 12.427 52.549 23.320 1.00 20.31 ? 450 ASN B N 1 ATOM 8335 C CA . ASN B 1 450 ? 12.648 53.381 24.521 1.00 22.29 ? 450 ASN B CA 1 ATOM 8336 C C . ASN B 1 450 ? 13.467 52.708 25.601 1.00 22.03 ? 450 ASN B C 1 ATOM 8337 O O . ASN B 1 450 ? 14.138 53.399 26.323 1.00 22.41 ? 450 ASN B O 1 ATOM 8338 C CB . ASN B 1 450 ? 11.328 53.958 25.081 1.00 22.69 ? 450 ASN B CB 1 ATOM 8339 C CG . ASN B 1 450 ? 10.937 55.226 24.393 1.00 23.03 ? 450 ASN B CG 1 ATOM 8340 O OD1 . ASN B 1 450 ? 11.806 55.956 23.864 1.00 23.73 ? 450 ASN B OD1 1 ATOM 8341 N ND2 . ASN B 1 450 ? 9.632 55.533 24.379 1.00 26.69 ? 450 ASN B ND2 1 ATOM 8342 N N . SER B 1 451 ? 13.381 51.373 25.728 1.00 20.21 ? 451 SER B N 1 ATOM 8343 C CA . SER B 1 451 ? 14.158 50.653 26.693 1.00 21.31 ? 451 SER B CA 1 ATOM 8344 C C . SER B 1 451 ? 15.624 50.867 26.372 1.00 22.07 ? 451 SER B C 1 ATOM 8345 O O . SER B 1 451 ? 16.478 51.072 27.263 1.00 23.26 ? 451 SER B O 1 ATOM 8346 C CB . SER B 1 451 ? 13.869 49.150 26.689 1.00 20.91 ? 451 SER B CB 1 ATOM 8347 O OG . SER B 1 451 ? 12.581 48.825 27.179 1.00 22.97 ? 451 SER B OG 1 ATOM 8348 N N . TRP B 1 452 ? 15.963 50.758 25.093 1.00 22.36 ? 452 TRP B N 1 ATOM 8349 C CA . TRP B 1 452 ? 17.356 50.996 24.698 1.00 19.94 ? 452 TRP B CA 1 ATOM 8350 C C . TRP B 1 452 ? 17.736 52.497 24.785 1.00 20.18 ? 452 TRP B C 1 ATOM 8351 O O . TRP B 1 452 ? 18.871 52.857 25.221 1.00 18.83 ? 452 TRP B O 1 ATOM 8352 C CB . TRP B 1 452 ? 17.648 50.384 23.308 1.00 19.51 ? 452 TRP B CB 1 ATOM 8353 C CG . TRP B 1 452 ? 17.555 48.858 23.341 1.00 15.90 ? 452 TRP B CG 1 ATOM 8354 C CD1 . TRP B 1 452 ? 16.630 48.106 22.740 1.00 14.84 ? 452 TRP B CD1 1 ATOM 8355 C CD2 . TRP B 1 452 ? 18.408 47.988 24.064 1.00 15.21 ? 452 TRP B CD2 1 ATOM 8356 N NE1 . TRP B 1 452 ? 16.821 46.755 23.055 1.00 15.80 ? 452 TRP B NE1 1 ATOM 8357 C CE2 . TRP B 1 452 ? 17.964 46.670 23.824 1.00 15.49 ? 452 TRP B CE2 1 ATOM 8358 C CE3 . TRP B 1 452 ? 19.509 48.190 24.928 1.00 16.29 ? 452 TRP B CE3 1 ATOM 8359 C CZ2 . TRP B 1 452 ? 18.527 45.595 24.443 1.00 16.46 ? 452 TRP B CZ2 1 ATOM 8360 C CZ3 . TRP B 1 452 ? 20.127 47.071 25.478 1.00 14.99 ? 452 TRP B CZ3 1 ATOM 8361 C CH2 . TRP B 1 452 ? 19.629 45.815 25.247 1.00 17.86 ? 452 TRP B CH2 1 ATOM 8362 N N . ARG B 1 453 ? 16.807 53.379 24.473 1.00 19.86 ? 453 ARG B N 1 ATOM 8363 C CA . ARG B 1 453 ? 17.101 54.823 24.698 1.00 22.01 ? 453 ARG B CA 1 ATOM 8364 C C . ARG B 1 453 ? 17.555 55.030 26.168 1.00 24.48 ? 453 ARG B C 1 ATOM 8365 O O . ARG B 1 453 ? 18.628 55.597 26.418 1.00 23.39 ? 453 ARG B O 1 ATOM 8366 C CB . ARG B 1 453 ? 15.925 55.682 24.355 1.00 21.08 ? 453 ARG B CB 1 ATOM 8367 C CG . ARG B 1 453 ? 15.661 55.772 22.846 1.00 22.61 ? 453 ARG B CG 1 ATOM 8368 C CD . ARG B 1 453 ? 16.560 56.787 22.160 1.00 22.93 ? 453 ARG B CD 1 ATOM 8369 N NE . ARG B 1 453 ? 16.204 58.171 22.422 1.00 25.37 ? 453 ARG B NE 1 ATOM 8370 C CZ . ARG B 1 453 ? 16.769 59.224 21.820 1.00 27.13 ? 453 ARG B CZ 1 ATOM 8371 N NH1 . ARG B 1 453 ? 17.716 59.107 20.850 1.00 25.33 ? 453 ARG B NH1 1 ATOM 8372 N NH2 . ARG B 1 453 ? 16.397 60.413 22.188 1.00 27.83 ? 453 ARG B NH2 1 ATOM 8373 N N . GLY B 1 454 ? 16.785 54.462 27.114 1.00 26.56 ? 454 GLY B N 1 ATOM 8374 C CA . GLY B 1 454 ? 17.039 54.693 28.555 1.00 27.14 ? 454 GLY B CA 1 ATOM 8375 C C . GLY B 1 454 ? 18.337 54.044 28.958 1.00 27.35 ? 454 GLY B C 1 ATOM 8376 O O . GLY B 1 454 ? 19.106 54.602 29.682 1.00 26.19 ? 454 GLY B O 1 ATOM 8377 N N . PHE B 1 455 ? 18.591 52.840 28.482 1.00 25.37 ? 455 PHE B N 1 ATOM 8378 C CA . PHE B 1 455 ? 19.851 52.138 28.782 1.00 25.60 ? 455 PHE B CA 1 ATOM 8379 C C . PHE B 1 455 ? 21.044 52.992 28.364 1.00 27.75 ? 455 PHE B C 1 ATOM 8380 O O . PHE B 1 455 ? 22.069 52.923 28.987 1.00 27.33 ? 455 PHE B O 1 ATOM 8381 C CB . PHE B 1 455 ? 19.877 50.839 28.017 1.00 26.12 ? 455 PHE B CB 1 ATOM 8382 C CG . PHE B 1 455 ? 21.158 50.081 28.092 1.00 26.32 ? 455 PHE B CG 1 ATOM 8383 C CD1 . PHE B 1 455 ? 21.344 49.117 29.066 1.00 25.54 ? 455 PHE B CD1 1 ATOM 8384 C CD2 . PHE B 1 455 ? 22.160 50.280 27.134 1.00 26.06 ? 455 PHE B CD2 1 ATOM 8385 C CE1 . PHE B 1 455 ? 22.519 48.386 29.130 1.00 27.34 ? 455 PHE B CE1 1 ATOM 8386 C CE2 . PHE B 1 455 ? 23.330 49.555 27.195 1.00 28.82 ? 455 PHE B CE2 1 ATOM 8387 C CZ . PHE B 1 455 ? 23.528 48.619 28.201 1.00 28.24 ? 455 PHE B CZ 1 ATOM 8388 N N . CYS B 1 456 ? 20.872 53.805 27.324 1.00 24.86 ? 456 CYS B N 1 ATOM 8389 C CA . CYS B 1 456 ? 21.915 54.646 26.793 1.00 25.64 ? 456 CYS B CA 1 ATOM 8390 C C . CYS B 1 456 ? 21.874 56.071 27.355 1.00 29.44 ? 456 CYS B C 1 ATOM 8391 O O . CYS B 1 456 ? 22.593 56.947 26.864 1.00 26.42 ? 456 CYS B O 1 ATOM 8392 C CB . CYS B 1 456 ? 21.763 54.721 25.259 1.00 25.18 ? 456 CYS B CB 1 ATOM 8393 S SG . CYS B 1 456 ? 22.417 53.243 24.469 1.00 26.13 ? 456 CYS B SG 1 ATOM 8394 N N . GLY B 1 457 ? 20.986 56.331 28.313 1.00 29.57 ? 457 GLY B N 1 ATOM 8395 C CA . GLY B 1 457 ? 20.898 57.654 28.924 1.00 30.63 ? 457 GLY B CA 1 ATOM 8396 C C . GLY B 1 457 ? 20.274 58.700 28.017 1.00 32.28 ? 457 GLY B C 1 ATOM 8397 O O . GLY B 1 457 ? 20.584 59.892 28.140 1.00 32.79 ? 457 GLY B O 1 ATOM 8398 N N . LEU B 1 458 ? 19.377 58.279 27.112 1.00 29.11 ? 458 LEU B N 1 ATOM 8399 C CA . LEU B 1 458 ? 18.774 59.188 26.154 1.00 26.32 ? 458 LEU B CA 1 ATOM 8400 C C . LEU B 1 458 ? 17.316 59.373 26.501 1.00 27.23 ? 458 LEU B C 1 ATOM 8401 O O . LEU B 1 458 ? 16.699 58.512 27.126 1.00 26.49 ? 458 LEU B O 1 ATOM 8402 C CB . LEU B 1 458 ? 18.949 58.646 24.729 1.00 26.74 ? 458 LEU B CB 1 ATOM 8403 C CG . LEU B 1 458 ? 20.397 58.433 24.259 1.00 26.25 ? 458 LEU B CG 1 ATOM 8404 C CD1 . LEU B 1 458 ? 20.428 57.653 22.946 1.00 26.11 ? 458 LEU B CD1 1 ATOM 8405 C CD2 . LEU B 1 458 ? 21.103 59.760 24.037 1.00 28.11 ? 458 LEU B CD2 1 ATOM 8406 N N . SER B 1 459 ? 16.753 60.479 26.080 1.00 28.18 ? 459 SER B N 1 ATOM 8407 C CA . SER B 1 459 ? 15.349 60.691 26.290 1.00 30.19 ? 459 SER B CA 1 ATOM 8408 C C . SER B 1 459 ? 14.457 59.614 25.614 1.00 28.37 ? 459 SER B C 1 ATOM 8409 O O . SER B 1 459 ? 14.790 59.060 24.580 1.00 24.75 ? 459 SER B O 1 ATOM 8410 C CB . SER B 1 459 ? 14.935 62.098 25.843 1.00 27.87 ? 459 SER B CB 1 ATOM 8411 O OG . SER B 1 459 ? 14.745 62.166 24.452 1.00 33.00 ? 459 SER B OG 1 ATOM 8412 N N . GLN B 1 460 ? 13.317 59.364 26.250 1.00 26.88 ? 460 GLN B N 1 ATOM 8413 C CA . GLN B 1 460 ? 12.376 58.408 25.834 1.00 25.01 ? 460 GLN B CA 1 ATOM 8414 C C . GLN B 1 460 ? 11.105 59.122 25.392 1.00 28.57 ? 460 GLN B C 1 ATOM 8415 O O . GLN B 1 460 ? 10.174 59.288 26.193 1.00 29.75 ? 460 GLN B O 1 ATOM 8416 C CB . GLN B 1 460 ? 12.114 57.486 27.022 1.00 28.42 ? 460 GLN B CB 1 ATOM 8417 C CG . GLN B 1 460 ? 13.320 56.585 27.319 1.00 29.87 ? 460 GLN B CG 1 ATOM 8418 C CD . GLN B 1 460 ? 13.456 56.140 28.768 1.00 32.27 ? 460 GLN B CD 1 ATOM 8419 O OE1 . GLN B 1 460 ? 13.374 54.980 29.099 1.00 30.97 ? 460 GLN B OE1 1 ATOM 8420 N NE2 . GLN B 1 460 ? 13.769 57.076 29.610 1.00 35.02 ? 460 GLN B NE2 1 ATOM 8421 N N . PRO B 1 461 ? 10.985 59.466 24.099 1.00 26.15 ? 461 PRO B N 1 ATOM 8422 C CA . PRO B 1 461 ? 9.702 60.083 23.722 1.00 26.66 ? 461 PRO B CA 1 ATOM 8423 C C . PRO B 1 461 ? 8.450 59.225 23.916 1.00 31.34 ? 461 PRO B C 1 ATOM 8424 O O . PRO B 1 461 ? 8.464 57.979 23.702 1.00 28.85 ? 461 PRO B O 1 ATOM 8425 C CB . PRO B 1 461 ? 9.884 60.390 22.233 1.00 26.33 ? 461 PRO B CB 1 ATOM 8426 C CG . PRO B 1 461 ? 10.866 59.358 21.780 1.00 25.40 ? 461 PRO B CG 1 ATOM 8427 C CD . PRO B 1 461 ? 11.842 59.222 22.922 1.00 25.53 ? 461 PRO B CD 1 ATOM 8428 N N . LYS B 1 462 ? 7.376 59.893 24.320 1.00 29.68 ? 462 LYS B N 1 ATOM 8429 C CA . LYS B 1 462 ? 6.092 59.203 24.524 1.00 29.88 ? 462 LYS B CA 1 ATOM 8430 C C . LYS B 1 462 ? 5.027 59.665 23.596 1.00 25.96 ? 462 LYS B C 1 ATOM 8431 O O . LYS B 1 462 ? 4.083 58.962 23.409 1.00 30.74 ? 462 LYS B O 1 ATOM 8432 C CB . LYS B 1 462 ? 5.572 59.348 25.964 1.00 29.73 ? 462 LYS B CB 1 ATOM 8433 C CG . LYS B 1 462 ? 6.599 58.947 27.000 1.00 30.17 ? 462 LYS B CG 1 ATOM 8434 C CD . LYS B 1 462 ? 6.825 57.408 27.032 1.00 32.02 ? 462 LYS B CD 1 ATOM 8435 C CE . LYS B 1 462 ? 7.940 57.063 27.993 1.00 31.63 ? 462 LYS B CE 1 ATOM 8436 N NZ . LYS B 1 462 ? 8.267 55.623 28.088 1.00 32.98 ? 462 LYS B NZ 1 ATOM 8437 N N . THR B 1 463 ? 5.170 60.812 22.976 1.00 27.55 ? 463 THR B N 1 ATOM 8438 C CA . THR B 1 463 ? 4.088 61.322 22.172 1.00 27.13 ? 463 THR B CA 1 ATOM 8439 C C . THR B 1 463 ? 4.614 61.551 20.755 1.00 24.93 ? 463 THR B C 1 ATOM 8440 O O . THR B 1 463 ? 5.802 61.573 20.555 1.00 24.45 ? 463 THR B O 1 ATOM 8441 C CB . THR B 1 463 ? 3.663 62.695 22.716 1.00 29.55 ? 463 THR B CB 1 ATOM 8442 O OG1 . THR B 1 463 ? 4.794 63.547 22.680 1.00 30.45 ? 463 THR B OG1 1 ATOM 8443 C CG2 . THR B 1 463 ? 3.113 62.577 24.178 1.00 31.87 ? 463 THR B CG2 1 ATOM 8444 N N . LEU B 1 464 ? 3.718 61.831 19.828 1.00 28.86 ? 464 LEU B N 1 ATOM 8445 C CA . LEU B 1 464 ? 4.086 62.265 18.497 1.00 29.83 ? 464 LEU B CA 1 ATOM 8446 C C . LEU B 1 464 ? 5.063 63.400 18.545 1.00 31.58 ? 464 LEU B C 1 ATOM 8447 O O . LEU B 1 464 ? 6.123 63.365 17.915 1.00 29.84 ? 464 LEU B O 1 ATOM 8448 C CB . LEU B 1 464 ? 2.840 62.678 17.703 1.00 33.91 ? 464 LEU B CB 1 ATOM 8449 C CG . LEU B 1 464 ? 3.086 63.063 16.232 1.00 36.36 ? 464 LEU B CG 1 ATOM 8450 C CD1 . LEU B 1 464 ? 3.817 61.952 15.438 1.00 36.68 ? 464 LEU B CD1 1 ATOM 8451 C CD2 . LEU B 1 464 ? 1.748 63.402 15.578 1.00 36.51 ? 464 LEU B CD2 1 ATOM 8452 N N . LYS B 1 465 ? 4.754 64.402 19.339 1.00 29.70 ? 465 LYS B N 1 ATOM 8453 C CA . LYS B 1 465 ? 5.606 65.581 19.417 1.00 30.67 ? 465 LYS B CA 1 ATOM 8454 C C . LYS B 1 465 ? 7.022 65.274 19.854 1.00 25.56 ? 465 LYS B C 1 ATOM 8455 O O . LYS B 1 465 ? 7.968 65.719 19.256 1.00 28.19 ? 465 LYS B O 1 ATOM 8456 C CB . LYS B 1 465 ? 5.009 66.581 20.392 1.00 35.47 ? 465 LYS B CB 1 ATOM 8457 C CG . LYS B 1 465 ? 5.224 67.997 19.917 1.00 39.40 ? 465 LYS B CG 1 ATOM 8458 C CD . LYS B 1 465 ? 4.039 68.328 19.015 1.00 46.84 ? 465 LYS B CD 1 ATOM 8459 C CE . LYS B 1 465 ? 4.085 69.779 18.534 1.00 52.28 ? 465 LYS B CE 1 ATOM 8460 N NZ . LYS B 1 465 ? 2.791 70.481 18.762 1.00 58.19 ? 465 LYS B NZ 1 ATOM 8461 N N . GLY B 1 466 ? 7.171 64.505 20.921 1.00 23.47 ? 466 GLY B N 1 ATOM 8462 C CA . GLY B 1 466 ? 8.501 64.106 21.366 1.00 23.83 ? 466 GLY B CA 1 ATOM 8463 C C . GLY B 1 466 ? 9.234 63.242 20.306 1.00 23.88 ? 466 GLY B C 1 ATOM 8464 O O . GLY B 1 466 ? 10.420 63.377 20.128 1.00 25.28 ? 466 GLY B O 1 ATOM 8465 N N . LEU B 1 467 ? 8.537 62.348 19.620 1.00 24.48 ? 467 LEU B N 1 ATOM 8466 C CA . LEU B 1 467 ? 9.236 61.472 18.649 1.00 25.65 ? 467 LEU B CA 1 ATOM 8467 C C . LEU B 1 467 ? 9.664 62.298 17.431 1.00 28.20 ? 467 LEU B C 1 ATOM 8468 O O . LEU B 1 467 ? 10.777 62.145 16.896 1.00 31.12 ? 467 LEU B O 1 ATOM 8469 C CB . LEU B 1 467 ? 8.348 60.283 18.293 1.00 24.91 ? 467 LEU B CB 1 ATOM 8470 C CG . LEU B 1 467 ? 8.965 59.263 17.317 1.00 25.50 ? 467 LEU B CG 1 ATOM 8471 C CD1 . LEU B 1 467 ? 10.135 58.524 17.959 1.00 23.18 ? 467 LEU B CD1 1 ATOM 8472 C CD2 . LEU B 1 467 ? 7.858 58.310 16.858 1.00 22.71 ? 467 LEU B CD2 1 ATOM 8473 N N . GLN B 1 468 ? 8.819 63.219 17.011 1.00 29.93 ? 468 GLN B N 1 ATOM 8474 C CA . GLN B 1 468 ? 9.179 64.172 15.943 1.00 32.42 ? 468 GLN B CA 1 ATOM 8475 C C . GLN B 1 468 ? 10.453 64.908 16.219 1.00 30.59 ? 468 GLN B C 1 ATOM 8476 O O . GLN B 1 468 ? 11.299 65.077 15.370 1.00 28.34 ? 468 GLN B O 1 ATOM 8477 C CB . GLN B 1 468 ? 8.085 65.187 15.772 1.00 36.31 ? 468 GLN B CB 1 ATOM 8478 C CG . GLN B 1 468 ? 6.794 64.545 15.307 1.00 41.90 ? 468 GLN B CG 1 ATOM 8479 C CD . GLN B 1 468 ? 5.689 65.531 14.996 1.00 43.69 ? 468 GLN B CD 1 ATOM 8480 O OE1 . GLN B 1 468 ? 4.810 65.249 14.182 1.00 51.65 ? 468 GLN B OE1 1 ATOM 8481 N NE2 . GLN B 1 468 ? 5.714 66.675 15.658 1.00 45.41 ? 468 GLN B NE2 1 ATOM 8482 N N . ALA B 1 469 ? 10.602 65.356 17.447 1.00 35.67 ? 469 ALA B N 1 ATOM 8483 C CA . ALA B 1 469 ? 11.822 66.035 17.858 1.00 30.99 ? 469 ALA B CA 1 ATOM 8484 C C . ALA B 1 469 ? 13.031 65.132 17.851 1.00 29.46 ? 469 ALA B C 1 ATOM 8485 O O . ALA B 1 469 ? 14.117 65.569 17.462 1.00 27.14 ? 469 ALA B O 1 ATOM 8486 C CB . ALA B 1 469 ? 11.639 66.663 19.241 1.00 36.22 ? 469 ALA B CB 1 ATOM 8487 N N . VAL B 1 470 ? 12.903 63.876 18.303 1.00 29.18 ? 470 VAL B N 1 ATOM 8488 C CA . VAL B 1 470 ? 14.100 62.989 18.293 1.00 28.00 ? 470 VAL B CA 1 ATOM 8489 C C . VAL B 1 470 ? 14.532 62.603 16.856 1.00 24.52 ? 470 VAL B C 1 ATOM 8490 O O . VAL B 1 470 ? 15.705 62.500 16.530 1.00 22.66 ? 470 VAL B O 1 ATOM 8491 C CB . VAL B 1 470 ? 13.812 61.715 19.109 1.00 30.79 ? 470 VAL B CB 1 ATOM 8492 C CG1 . VAL B 1 470 ? 14.930 60.706 18.970 1.00 27.55 ? 470 VAL B CG1 1 ATOM 8493 C CG2 . VAL B 1 470 ? 13.596 62.092 20.597 1.00 33.15 ? 470 VAL B CG2 1 ATOM 8494 N N . LEU B 1 471 ? 13.564 62.412 15.996 1.00 24.35 ? 471 LEU B N 1 ATOM 8495 C CA . LEU B 1 471 ? 13.847 61.965 14.648 1.00 24.95 ? 471 LEU B CA 1 ATOM 8496 C C . LEU B 1 471 ? 14.021 63.136 13.712 1.00 26.12 ? 471 LEU B C 1 ATOM 8497 O O . LEU B 1 471 ? 14.492 62.967 12.580 1.00 22.30 ? 471 LEU B O 1 ATOM 8498 C CB . LEU B 1 471 ? 12.713 61.111 14.152 1.00 24.35 ? 471 LEU B CB 1 ATOM 8499 C CG . LEU B 1 471 ? 12.447 59.865 14.952 1.00 24.94 ? 471 LEU B CG 1 ATOM 8500 C CD1 . LEU B 1 471 ? 11.312 59.119 14.241 1.00 24.25 ? 471 LEU B CD1 1 ATOM 8501 C CD2 . LEU B 1 471 ? 13.702 58.990 15.129 1.00 23.63 ? 471 LEU B CD2 1 ATOM 8502 N N . LYS B 1 472 ? 13.634 64.334 14.173 1.00 31.62 ? 472 LYS B N 1 ATOM 8503 C CA . LYS B 1 472 ? 13.683 65.559 13.354 1.00 30.34 ? 472 LYS B CA 1 ATOM 8504 C C . LYS B 1 472 ? 12.917 65.399 12.081 1.00 27.99 ? 472 LYS B C 1 ATOM 8505 O O . LYS B 1 472 ? 13.350 65.836 11.040 1.00 26.58 ? 472 LYS B O 1 ATOM 8506 C CB . LYS B 1 472 ? 15.119 65.917 13.034 1.00 31.10 ? 472 LYS B CB 1 ATOM 8507 C CG . LYS B 1 472 ? 15.835 66.319 14.293 1.00 40.71 ? 472 LYS B CG 1 ATOM 8508 C CD . LYS B 1 472 ? 17.178 66.938 13.979 1.00 47.30 ? 472 LYS B CD 1 ATOM 8509 C CE . LYS B 1 472 ? 17.591 67.889 15.094 1.00 52.67 ? 472 LYS B CE 1 ATOM 8510 N NZ . LYS B 1 472 ? 18.801 68.665 14.683 1.00 52.88 ? 472 LYS B NZ 1 ATOM 8511 N N . ASN B 1 473 ? 11.761 64.783 12.174 1.00 26.90 ? 473 ASN B N 1 ATOM 8512 C CA . ASN B 1 473 ? 10.990 64.475 10.991 1.00 27.08 ? 473 ASN B CA 1 ATOM 8513 C C . ASN B 1 473 ? 9.586 64.102 11.432 1.00 30.84 ? 473 ASN B C 1 ATOM 8514 O O . ASN B 1 473 ? 9.386 63.064 12.095 1.00 26.21 ? 473 ASN B O 1 ATOM 8515 C CB . ASN B 1 473 ? 11.675 63.294 10.300 1.00 26.00 ? 473 ASN B CB 1 ATOM 8516 C CG . ASN B 1 473 ? 10.992 62.855 9.061 1.00 25.50 ? 473 ASN B CG 1 ATOM 8517 O OD1 . ASN B 1 473 ? 9.784 63.010 8.875 1.00 24.72 ? 473 ASN B OD1 1 ATOM 8518 N ND2 . ASN B 1 473 ? 11.768 62.217 8.209 1.00 26.72 ? 473 ASN B ND2 1 ATOM 8519 N N . LYS B 1 474 ? 8.615 64.938 11.039 1.00 30.97 ? 474 LYS B N 1 ATOM 8520 C CA . LYS B 1 474 ? 7.287 64.852 11.615 1.00 34.52 ? 474 LYS B CA 1 ATOM 8521 C C . LYS B 1 474 ? 6.575 63.681 10.971 1.00 27.34 ? 474 LYS B C 1 ATOM 8522 O O . LYS B 1 474 ? 5.818 63.001 11.625 1.00 28.41 ? 474 LYS B O 1 ATOM 8523 C CB . LYS B 1 474 ? 6.423 66.099 11.316 1.00 41.34 ? 474 LYS B CB 1 ATOM 8524 C CG . LYS B 1 474 ? 7.006 67.479 11.609 1.00 48.80 ? 474 LYS B CG 1 ATOM 8525 C CD . LYS B 1 474 ? 6.311 68.527 10.711 1.00 54.03 ? 474 LYS B CD 1 ATOM 8526 C CE . LYS B 1 474 ? 5.048 69.137 11.325 1.00 58.99 ? 474 LYS B CE 1 ATOM 8527 N NZ . LYS B 1 474 ? 5.410 70.203 12.320 1.00 60.44 ? 474 LYS B NZ 1 ATOM 8528 N N . VAL B 1 475 ? 6.766 63.523 9.665 1.00 26.56 ? 475 VAL B N 1 ATOM 8529 C CA . VAL B 1 475 ? 6.028 62.532 8.888 1.00 28.34 ? 475 VAL B CA 1 ATOM 8530 C C . VAL B 1 475 ? 6.491 61.104 9.241 1.00 26.74 ? 475 VAL B C 1 ATOM 8531 O O . VAL B 1 475 ? 5.695 60.192 9.348 1.00 30.10 ? 475 VAL B O 1 ATOM 8532 C CB . VAL B 1 475 ? 6.204 62.782 7.356 1.00 32.45 ? 475 VAL B CB 1 ATOM 8533 C CG1 . VAL B 1 475 ? 5.604 61.651 6.519 1.00 29.08 ? 475 VAL B CG1 1 ATOM 8534 C CG2 . VAL B 1 475 ? 5.586 64.112 6.954 1.00 34.36 ? 475 VAL B CG2 1 ATOM 8535 N N . LEU B 1 476 ? 7.786 60.935 9.408 1.00 27.03 ? 476 LEU B N 1 ATOM 8536 C CA . LEU B 1 476 ? 8.357 59.634 9.760 1.00 29.29 ? 476 LEU B CA 1 ATOM 8537 C C . LEU B 1 476 ? 7.803 59.237 11.149 1.00 27.56 ? 476 LEU B C 1 ATOM 8538 O O . LEU B 1 476 ? 7.324 58.131 11.347 1.00 24.92 ? 476 LEU B O 1 ATOM 8539 C CB . LEU B 1 476 ? 9.910 59.663 9.732 1.00 27.33 ? 476 LEU B CB 1 ATOM 8540 C CG . LEU B 1 476 ? 10.564 58.376 10.255 1.00 27.26 ? 476 LEU B CG 1 ATOM 8541 C CD1 . LEU B 1 476 ? 10.032 57.089 9.605 1.00 26.55 ? 476 LEU B CD1 1 ATOM 8542 C CD2 . LEU B 1 476 ? 12.061 58.467 10.109 1.00 27.60 ? 476 LEU B CD2 1 ATOM 8543 N N . ALA B 1 477 ? 7.770 60.197 12.058 1.00 29.28 ? 477 ALA B N 1 ATOM 8544 C CA . ALA B 1 477 ? 7.322 59.941 13.402 1.00 25.66 ? 477 ALA B CA 1 ATOM 8545 C C . ALA B 1 477 ? 5.841 59.638 13.429 1.00 26.00 ? 477 ALA B C 1 ATOM 8546 O O . ALA B 1 477 ? 5.368 58.682 14.102 1.00 27.78 ? 477 ALA B O 1 ATOM 8547 C CB . ALA B 1 477 ? 7.690 61.116 14.269 1.00 29.78 ? 477 ALA B CB 1 ATOM 8548 N N . LYS B 1 478 ? 5.096 60.382 12.615 1.00 26.17 ? 478 LYS B N 1 ATOM 8549 C CA . LYS B 1 478 ? 3.715 60.106 12.398 1.00 25.19 ? 478 LYS B CA 1 ATOM 8550 C C . LYS B 1 478 ? 3.510 58.652 11.903 1.00 24.04 ? 478 LYS B C 1 ATOM 8551 O O . LYS B 1 478 ? 2.676 57.909 12.434 1.00 24.39 ? 478 LYS B O 1 ATOM 8552 C CB . LYS B 1 478 ? 3.165 61.156 11.416 1.00 28.78 ? 478 LYS B CB 1 ATOM 8553 C CG . LYS B 1 478 ? 1.700 61.059 11.042 1.00 36.06 ? 478 LYS B CG 1 ATOM 8554 C CD . LYS B 1 478 ? 0.785 61.098 12.230 1.00 41.15 ? 478 LYS B CD 1 ATOM 8555 C CE . LYS B 1 478 ? -0.643 60.806 11.828 1.00 46.24 ? 478 LYS B CE 1 ATOM 8556 N NZ . LYS B 1 478 ? -1.466 60.786 13.081 1.00 52.30 ? 478 LYS B NZ 1 ATOM 8557 N N . LYS B 1 479 ? 4.204 58.258 10.845 1.00 20.84 ? 479 LYS B N 1 ATOM 8558 C CA . LYS B 1 479 ? 4.024 56.927 10.290 1.00 20.28 ? 479 LYS B CA 1 ATOM 8559 C C . LYS B 1 479 ? 4.429 55.883 11.308 1.00 18.64 ? 479 LYS B C 1 ATOM 8560 O O . LYS B 1 479 ? 3.810 54.851 11.367 1.00 20.96 ? 479 LYS B O 1 ATOM 8561 C CB . LYS B 1 479 ? 4.842 56.718 9.015 1.00 23.89 ? 479 LYS B CB 1 ATOM 8562 C CG . LYS B 1 479 ? 4.389 57.574 7.855 1.00 28.95 ? 479 LYS B CG 1 ATOM 8563 C CD . LYS B 1 479 ? 5.244 57.267 6.626 1.00 33.35 ? 479 LYS B CD 1 ATOM 8564 C CE . LYS B 1 479 ? 4.836 58.153 5.450 1.00 35.97 ? 479 LYS B CE 1 ATOM 8565 N NZ . LYS B 1 479 ? 5.960 58.266 4.475 1.00 42.07 ? 479 LYS B NZ 1 ATOM 8566 N N . LEU B 1 480 ? 5.480 56.134 12.095 1.00 18.17 ? 480 LEU B N 1 ATOM 8567 C CA . LEU B 1 480 ? 5.873 55.133 13.091 1.00 20.15 ? 480 LEU B CA 1 ATOM 8568 C C . LEU B 1 480 ? 4.733 54.982 14.152 1.00 22.96 ? 480 LEU B C 1 ATOM 8569 O O . LEU B 1 480 ? 4.316 53.864 14.492 1.00 20.34 ? 480 LEU B O 1 ATOM 8570 C CB . LEU B 1 480 ? 7.222 55.488 13.706 1.00 20.80 ? 480 LEU B CB 1 ATOM 8571 C CG . LEU B 1 480 ? 8.432 55.173 12.798 1.00 20.66 ? 480 LEU B CG 1 ATOM 8572 C CD1 . LEU B 1 480 ? 9.656 55.859 13.308 1.00 22.05 ? 480 LEU B CD1 1 ATOM 8573 C CD2 . LEU B 1 480 ? 8.642 53.631 12.722 1.00 22.00 ? 480 LEU B CD2 1 ATOM 8574 N N . LEU B 1 481 ? 4.166 56.104 14.583 1.00 24.93 ? 481 LEU B N 1 ATOM 8575 C CA . LEU B 1 481 ? 3.107 55.993 15.606 1.00 26.93 ? 481 LEU B CA 1 ATOM 8576 C C . LEU B 1 481 ? 1.838 55.441 15.085 1.00 23.46 ? 481 LEU B C 1 ATOM 8577 O O . LEU B 1 481 ? 1.164 54.709 15.772 1.00 23.37 ? 481 LEU B O 1 ATOM 8578 C CB . LEU B 1 481 ? 2.882 57.321 16.312 1.00 30.90 ? 481 LEU B CB 1 ATOM 8579 C CG . LEU B 1 481 ? 4.079 57.643 17.199 1.00 36.59 ? 481 LEU B CG 1 ATOM 8580 C CD1 . LEU B 1 481 ? 3.767 58.907 17.978 1.00 41.30 ? 481 LEU B CD1 1 ATOM 8581 C CD2 . LEU B 1 481 ? 4.442 56.513 18.157 1.00 38.15 ? 481 LEU B CD2 1 ATOM 8582 N N . ASP B 1 482 ? 1.493 55.738 13.854 1.00 23.90 ? 482 ASP B N 1 ATOM 8583 C CA . ASP B 1 482 ? 0.330 55.115 13.285 1.00 22.30 ? 482 ASP B CA 1 ATOM 8584 C C . ASP B 1 482 ? 0.505 53.595 13.297 1.00 22.31 ? 482 ASP B C 1 ATOM 8585 O O . ASP B 1 482 ? -0.460 52.840 13.498 1.00 20.39 ? 482 ASP B O 1 ATOM 8586 C CB . ASP B 1 482 ? 0.096 55.595 11.849 1.00 26.42 ? 482 ASP B CB 1 ATOM 8587 C CG . ASP B 1 482 ? -0.461 57.035 11.769 1.00 29.87 ? 482 ASP B CG 1 ATOM 8588 O OD1 . ASP B 1 482 ? -0.819 57.640 12.799 1.00 36.17 ? 482 ASP B OD1 1 ATOM 8589 O OD2 . ASP B 1 482 ? -0.560 57.551 10.660 1.00 33.03 ? 482 ASP B OD2 1 ATOM 8590 N N . LEU B 1 483 ? 1.726 53.120 13.059 1.00 21.36 ? 483 LEU B N 1 ATOM 8591 C CA . LEU B 1 483 ? 1.943 51.690 13.059 1.00 21.74 ? 483 LEU B CA 1 ATOM 8592 C C . LEU B 1 483 ? 2.130 51.091 14.457 1.00 20.15 ? 483 LEU B C 1 ATOM 8593 O O . LEU B 1 483 ? 1.715 49.952 14.734 1.00 19.06 ? 483 LEU B O 1 ATOM 8594 C CB . LEU B 1 483 ? 3.170 51.420 12.186 1.00 24.70 ? 483 LEU B CB 1 ATOM 8595 C CG . LEU B 1 483 ? 2.843 51.537 10.691 1.00 26.31 ? 483 LEU B CG 1 ATOM 8596 C CD1 . LEU B 1 483 ? 4.107 51.501 9.871 1.00 27.12 ? 483 LEU B CD1 1 ATOM 8597 C CD2 . LEU B 1 483 ? 1.920 50.409 10.284 1.00 27.33 ? 483 LEU B CD2 1 ATOM 8598 N N . TYR B 1 484 ? 2.876 51.802 15.284 1.00 17.79 ? 484 TYR B N 1 ATOM 8599 C CA . TYR B 1 484 ? 3.307 51.253 16.564 1.00 18.53 ? 484 TYR B CA 1 ATOM 8600 C C . TYR B 1 484 ? 2.505 51.713 17.796 1.00 19.40 ? 484 TYR B C 1 ATOM 8601 O O . TYR B 1 484 ? 2.572 51.030 18.830 1.00 18.80 ? 484 TYR B O 1 ATOM 8602 C CB . TYR B 1 484 ? 4.779 51.572 16.825 1.00 17.86 ? 484 TYR B CB 1 ATOM 8603 C CG . TYR B 1 484 ? 5.703 50.655 16.029 1.00 18.56 ? 484 TYR B CG 1 ATOM 8604 C CD1 . TYR B 1 484 ? 5.944 49.375 16.423 1.00 16.86 ? 484 TYR B CD1 1 ATOM 8605 C CD2 . TYR B 1 484 ? 6.355 51.124 14.872 1.00 19.29 ? 484 TYR B CD2 1 ATOM 8606 C CE1 . TYR B 1 484 ? 6.821 48.559 15.709 1.00 18.82 ? 484 TYR B CE1 1 ATOM 8607 C CE2 . TYR B 1 484 ? 7.179 50.295 14.119 1.00 19.32 ? 484 TYR B CE2 1 ATOM 8608 C CZ . TYR B 1 484 ? 7.397 49.010 14.525 1.00 19.43 ? 484 TYR B CZ 1 ATOM 8609 O OH . TYR B 1 484 ? 8.263 48.180 13.830 1.00 19.15 ? 484 TYR B OH 1 ATOM 8610 N N . LYS B 1 485 ? 1.819 52.864 17.666 1.00 20.38 ? 485 LYS B N 1 ATOM 8611 C CA . LYS B 1 485 ? 0.930 53.448 18.708 1.00 22.36 ? 485 LYS B CA 1 ATOM 8612 C C . LYS B 1 485 ? 1.732 54.123 19.825 1.00 25.11 ? 485 LYS B C 1 ATOM 8613 O O . LYS B 1 485 ? 1.430 55.247 20.262 1.00 24.79 ? 485 LYS B O 1 ATOM 8614 C CB . LYS B 1 485 ? -0.041 52.411 19.304 1.00 23.13 ? 485 LYS B CB 1 ATOM 8615 C CG . LYS B 1 485 ? -0.877 51.659 18.294 1.00 25.45 ? 485 LYS B CG 1 ATOM 8616 C CD . LYS B 1 485 ? -1.610 52.591 17.343 1.00 27.01 ? 485 LYS B CD 1 ATOM 8617 C CE . LYS B 1 485 ? -2.287 51.840 16.215 1.00 30.75 ? 485 LYS B CE 1 ATOM 8618 N NZ . LYS B 1 485 ? -2.715 52.780 15.123 1.00 31.22 ? 485 LYS B NZ 1 ATOM 8619 N N . THR B 1 486 ? 2.760 53.470 20.303 1.00 21.48 ? 486 THR B N 1 ATOM 8620 C CA . THR B 1 486 ? 3.626 54.110 21.309 1.00 21.37 ? 486 THR B CA 1 ATOM 8621 C C . THR B 1 486 ? 5.058 53.871 20.918 1.00 20.23 ? 486 THR B C 1 ATOM 8622 O O . THR B 1 486 ? 5.342 52.807 20.394 1.00 17.56 ? 486 THR B O 1 ATOM 8623 C CB . THR B 1 486 ? 3.432 53.505 22.714 1.00 20.27 ? 486 THR B CB 1 ATOM 8624 O OG1 . THR B 1 486 ? 4.523 53.865 23.552 1.00 20.34 ? 486 THR B OG1 1 ATOM 8625 C CG2 . THR B 1 486 ? 3.366 52.026 22.647 1.00 21.72 ? 486 THR B CG2 1 ATOM 8626 N N . PRO B 1 487 ? 5.952 54.855 21.148 1.00 21.62 ? 487 PRO B N 1 ATOM 8627 C CA . PRO B 1 487 ? 7.339 54.584 20.764 1.00 21.83 ? 487 PRO B CA 1 ATOM 8628 C C . PRO B 1 487 ? 7.976 53.434 21.537 1.00 22.00 ? 487 PRO B C 1 ATOM 8629 O O . PRO B 1 487 ? 9.064 52.941 21.169 1.00 20.42 ? 487 PRO B O 1 ATOM 8630 C CB . PRO B 1 487 ? 8.053 55.894 21.097 1.00 21.96 ? 487 PRO B CB 1 ATOM 8631 C CG . PRO B 1 487 ? 6.993 56.939 20.927 1.00 22.38 ? 487 PRO B CG 1 ATOM 8632 C CD . PRO B 1 487 ? 5.764 56.285 21.499 1.00 22.22 ? 487 PRO B CD 1 ATOM 8633 N N . ASP B 1 488 ? 7.324 53.018 22.633 1.00 22.81 ? 488 ASP B N 1 ATOM 8634 C CA . ASP B 1 488 ? 7.858 51.922 23.491 1.00 19.97 ? 488 ASP B CA 1 ATOM 8635 C C . ASP B 1 488 ? 7.901 50.652 22.683 1.00 16.18 ? 488 ASP B C 1 ATOM 8636 O O . ASP B 1 488 ? 8.683 49.778 22.984 1.00 18.35 ? 488 ASP B O 1 ATOM 8637 C CB . ASP B 1 488 ? 6.936 51.633 24.719 1.00 20.88 ? 488 ASP B CB 1 ATOM 8638 C CG . ASP B 1 488 ? 7.010 52.743 25.807 1.00 22.99 ? 488 ASP B CG 1 ATOM 8639 O OD1 . ASP B 1 488 ? 7.937 53.587 25.747 1.00 23.55 ? 488 ASP B OD1 1 ATOM 8640 O OD2 . ASP B 1 488 ? 6.087 52.768 26.692 1.00 23.07 ? 488 ASP B OD2 1 ATOM 8641 N N . ASN B 1 489 ? 6.976 50.530 21.744 1.00 16.18 ? 489 ASN B N 1 ATOM 8642 C CA . ASN B 1 489 ? 6.806 49.308 20.952 1.00 15.91 ? 489 ASN B CA 1 ATOM 8643 C C . ASN B 1 489 ? 7.578 49.300 19.641 1.00 17.17 ? 489 ASN B C 1 ATOM 8644 O O . ASN B 1 489 ? 7.602 48.261 18.975 1.00 18.67 ? 489 ASN B O 1 ATOM 8645 C CB . ASN B 1 489 ? 5.347 49.069 20.645 1.00 15.63 ? 489 ASN B CB 1 ATOM 8646 C CG . ASN B 1 489 ? 4.556 48.608 21.894 1.00 14.61 ? 489 ASN B CG 1 ATOM 8647 O OD1 . ASN B 1 489 ? 5.102 48.561 22.996 1.00 15.24 ? 489 ASN B OD1 1 ATOM 8648 N ND2 . ASN B 1 489 ? 3.347 48.182 21.692 1.00 13.95 ? 489 ASN B ND2 1 ATOM 8649 N N . ILE B 1 490 ? 8.220 50.412 19.310 1.00 17.11 ? 490 ILE B N 1 ATOM 8650 C CA . ILE B 1 490 ? 9.059 50.460 18.066 1.00 19.00 ? 490 ILE B CA 1 ATOM 8651 C C . ILE B 1 490 ? 10.282 49.489 18.161 1.00 20.39 ? 490 ILE B C 1 ATOM 8652 O O . ILE B 1 490 ? 11.097 49.560 19.081 1.00 18.21 ? 490 ILE B O 1 ATOM 8653 C CB . ILE B 1 490 ? 9.560 51.855 17.686 1.00 18.34 ? 490 ILE B CB 1 ATOM 8654 C CG1 . ILE B 1 490 ? 8.422 52.820 17.459 1.00 20.59 ? 490 ILE B CG1 1 ATOM 8655 C CG2 . ILE B 1 490 ? 10.394 51.787 16.385 1.00 18.43 ? 490 ILE B CG2 1 ATOM 8656 C CD1 . ILE B 1 490 ? 8.899 54.275 17.387 1.00 20.83 ? 490 ILE B CD1 1 ATOM 8657 N N . ASP B 1 491 ? 10.347 48.545 17.208 1.00 19.51 ? 491 ASP B N 1 ATOM 8658 C CA . ASP B 1 491 ? 11.388 47.542 17.197 1.00 19.42 ? 491 ASP B CA 1 ATOM 8659 C C . ASP B 1 491 ? 12.755 48.226 17.067 1.00 19.57 ? 491 ASP B C 1 ATOM 8660 O O . ASP B 1 491 ? 12.877 49.230 16.329 1.00 21.58 ? 491 ASP B O 1 ATOM 8661 C CB . ASP B 1 491 ? 11.163 46.524 16.080 1.00 19.16 ? 491 ASP B CB 1 ATOM 8662 C CG . ASP B 1 491 ? 9.817 45.821 16.172 1.00 19.76 ? 491 ASP B CG 1 ATOM 8663 O OD1 . ASP B 1 491 ? 9.713 44.916 17.028 1.00 19.63 ? 491 ASP B OD1 1 ATOM 8664 O OD2 . ASP B 1 491 ? 8.913 46.055 15.288 1.00 17.84 ? 491 ASP B OD2 1 ATOM 8665 N N . ILE B 1 492 ? 13.756 47.703 17.810 1.00 18.96 ? 492 ILE B N 1 ATOM 8666 C CA . ILE B 1 492 ? 15.063 48.336 17.935 1.00 16.10 ? 492 ILE B CA 1 ATOM 8667 C C . ILE B 1 492 ? 15.772 48.570 16.584 1.00 16.26 ? 492 ILE B C 1 ATOM 8668 O O . ILE B 1 492 ? 16.274 49.659 16.317 1.00 15.95 ? 492 ILE B O 1 ATOM 8669 C CB . ILE B 1 492 ? 15.979 47.584 18.927 1.00 14.40 ? 492 ILE B CB 1 ATOM 8670 C CG1 . ILE B 1 492 ? 17.308 48.283 19.167 1.00 14.94 ? 492 ILE B CG1 1 ATOM 8671 C CG2 . ILE B 1 492 ? 16.263 46.175 18.513 1.00 15.24 ? 492 ILE B CG2 1 ATOM 8672 C CD1 . ILE B 1 492 ? 17.162 49.699 19.622 1.00 15.60 ? 492 ILE B CD1 1 ATOM 8673 N N . TRP B 1 493 ? 15.745 47.574 15.706 1.00 17.05 ? 493 TRP B N 1 ATOM 8674 C CA . TRP B 1 493 ? 16.311 47.784 14.378 1.00 15.80 ? 493 TRP B CA 1 ATOM 8675 C C . TRP B 1 493 ? 15.781 49.057 13.695 1.00 15.10 ? 493 TRP B C 1 ATOM 8676 O O . TRP B 1 493 ? 16.573 49.822 13.181 1.00 16.98 ? 493 TRP B O 1 ATOM 8677 C CB . TRP B 1 493 ? 16.121 46.578 13.465 1.00 14.05 ? 493 TRP B CB 1 ATOM 8678 C CG . TRP B 1 493 ? 16.794 46.773 12.166 1.00 13.12 ? 493 TRP B CG 1 ATOM 8679 C CD1 . TRP B 1 493 ? 18.131 46.808 11.950 1.00 12.80 ? 493 TRP B CD1 1 ATOM 8680 C CD2 . TRP B 1 493 ? 16.163 47.172 10.915 1.00 12.55 ? 493 TRP B CD2 1 ATOM 8681 N NE1 . TRP B 1 493 ? 18.393 47.061 10.626 1.00 13.08 ? 493 TRP B NE1 1 ATOM 8682 C CE2 . TRP B 1 493 ? 17.202 47.298 9.956 1.00 13.05 ? 493 TRP B CE2 1 ATOM 8683 C CE3 . TRP B 1 493 ? 14.842 47.336 10.507 1.00 13.70 ? 493 TRP B CE3 1 ATOM 8684 C CZ2 . TRP B 1 493 ? 16.951 47.612 8.621 1.00 12.80 ? 493 TRP B CZ2 1 ATOM 8685 C CZ3 . TRP B 1 493 ? 14.568 47.624 9.149 1.00 13.31 ? 493 TRP B CZ3 1 ATOM 8686 C CH2 . TRP B 1 493 ? 15.625 47.776 8.232 1.00 12.96 ? 493 TRP B CH2 1 ATOM 8687 N N . ILE B 1 494 ? 14.479 49.239 13.590 1.00 17.02 ? 494 ILE B N 1 ATOM 8688 C CA . ILE B 1 494 ? 13.960 50.414 12.851 1.00 16.50 ? 494 ILE B CA 1 ATOM 8689 C C . ILE B 1 494 ? 14.078 51.708 13.670 1.00 17.86 ? 494 ILE B C 1 ATOM 8690 O O . ILE B 1 494 ? 14.371 52.775 13.117 1.00 17.38 ? 494 ILE B O 1 ATOM 8691 C CB . ILE B 1 494 ? 12.576 50.212 12.260 1.00 17.33 ? 494 ILE B CB 1 ATOM 8692 C CG1 . ILE B 1 494 ? 12.193 51.364 11.309 1.00 18.54 ? 494 ILE B CG1 1 ATOM 8693 C CG2 . ILE B 1 494 ? 11.459 50.059 13.331 1.00 19.73 ? 494 ILE B CG2 1 ATOM 8694 C CD1 . ILE B 1 494 ? 13.207 51.588 10.199 1.00 18.52 ? 494 ILE B CD1 1 ATOM 8695 N N . GLY B 1 495 ? 13.829 51.636 14.956 1.00 17.59 ? 495 GLY B N 1 ATOM 8696 C CA . GLY B 1 495 ? 13.989 52.852 15.786 1.00 17.14 ? 495 GLY B CA 1 ATOM 8697 C C . GLY B 1 495 ? 15.393 53.426 15.822 1.00 18.14 ? 495 GLY B C 1 ATOM 8698 O O . GLY B 1 495 ? 15.599 54.619 15.617 1.00 13.98 ? 495 GLY B O 1 ATOM 8699 N N . GLY B 1 496 ? 16.369 52.548 16.003 1.00 18.66 ? 496 GLY B N 1 ATOM 8700 C CA . GLY B 1 496 ? 17.775 52.979 15.929 1.00 20.02 ? 496 GLY B CA 1 ATOM 8701 C C . GLY B 1 496 ? 18.194 53.542 14.592 1.00 19.05 ? 496 GLY B C 1 ATOM 8702 O O . GLY B 1 496 ? 18.853 54.571 14.542 1.00 18.92 ? 496 GLY B O 1 ATOM 8703 N N . ASN B 1 497 ? 17.758 52.896 13.509 1.00 17.50 ? 497 ASN B N 1 ATOM 8704 C CA . ASN B 1 497 ? 18.109 53.359 12.186 1.00 18.25 ? 497 ASN B CA 1 ATOM 8705 C C . ASN B 1 497 ? 17.323 54.601 11.733 1.00 19.20 ? 497 ASN B C 1 ATOM 8706 O O . ASN B 1 497 ? 17.738 55.279 10.822 1.00 18.47 ? 497 ASN B O 1 ATOM 8707 C CB . ASN B 1 497 ? 17.994 52.205 11.179 1.00 18.29 ? 497 ASN B CB 1 ATOM 8708 C CG . ASN B 1 497 ? 19.142 51.253 11.341 1.00 17.43 ? 497 ASN B CG 1 ATOM 8709 O OD1 . ASN B 1 497 ? 20.248 51.667 11.190 1.00 18.20 ? 497 ASN B OD1 1 ATOM 8710 N ND2 . ASN B 1 497 ? 18.907 50.023 11.627 1.00 17.51 ? 497 ASN B ND2 1 ATOM 8711 N N . ALA B 1 498 ? 16.192 54.895 12.371 1.00 18.23 ? 498 ALA B N 1 ATOM 8712 C CA . ALA B 1 498 ? 15.424 56.047 12.035 1.00 18.40 ? 498 ALA B CA 1 ATOM 8713 C C . ALA B 1 498 ? 16.025 57.383 12.489 1.00 21.19 ? 498 ALA B C 1 ATOM 8714 O O . ALA B 1 498 ? 15.603 58.457 12.016 1.00 22.71 ? 498 ALA B O 1 ATOM 8715 C CB . ALA B 1 498 ? 14.004 55.908 12.610 1.00 20.01 ? 498 ALA B CB 1 ATOM 8716 N N . GLU B 1 499 ? 16.948 57.345 13.436 1.00 20.38 ? 499 GLU B N 1 ATOM 8717 C CA . GLU B 1 499 ? 17.446 58.555 14.007 1.00 22.05 ? 499 GLU B CA 1 ATOM 8718 C C . GLU B 1 499 ? 18.447 59.207 13.058 1.00 21.90 ? 499 GLU B C 1 ATOM 8719 O O . GLU B 1 499 ? 19.326 58.551 12.522 1.00 21.10 ? 499 GLU B O 1 ATOM 8720 C CB . GLU B 1 499 ? 18.185 58.261 15.342 1.00 20.50 ? 499 GLU B CB 1 ATOM 8721 C CG . GLU B 1 499 ? 17.289 57.704 16.460 1.00 20.48 ? 499 GLU B CG 1 ATOM 8722 C CD . GLU B 1 499 ? 18.031 57.454 17.779 1.00 20.93 ? 499 GLU B CD 1 ATOM 8723 O OE1 . GLU B 1 499 ? 19.275 57.523 17.797 1.00 22.27 ? 499 GLU B OE1 1 ATOM 8724 O OE2 . GLU B 1 499 ? 17.348 57.186 18.795 1.00 20.57 ? 499 GLU B OE2 1 ATOM 8725 N N . PRO B 1 500 ? 18.379 60.527 12.964 1.00 26.07 ? 500 PRO B N 1 ATOM 8726 C CA . PRO B 1 500 ? 19.419 61.203 12.266 1.00 25.49 ? 500 PRO B CA 1 ATOM 8727 C C . PRO B 1 500 ? 20.796 60.907 12.801 1.00 28.57 ? 500 PRO B C 1 ATOM 8728 O O . PRO B 1 500 ? 21.016 60.700 14.006 1.00 25.79 ? 500 PRO B O 1 ATOM 8729 C CB . PRO B 1 500 ? 19.071 62.698 12.415 1.00 26.43 ? 500 PRO B CB 1 ATOM 8730 C CG . PRO B 1 500 ? 17.808 62.792 13.152 1.00 29.73 ? 500 PRO B CG 1 ATOM 8731 C CD . PRO B 1 500 ? 17.523 61.437 13.761 1.00 26.67 ? 500 PRO B CD 1 ATOM 8732 N N . MET B 1 501 ? 21.740 60.938 11.871 1.00 27.05 ? 501 MET B N 1 ATOM 8733 C CA . MET B 1 501 ? 23.081 60.594 12.125 1.00 27.45 ? 501 MET B CA 1 ATOM 8734 C C . MET B 1 501 ? 23.818 61.588 13.024 1.00 27.91 ? 501 MET B C 1 ATOM 8735 O O . MET B 1 501 ? 23.563 62.759 12.939 1.00 29.23 ? 501 MET B O 1 ATOM 8736 C CB . MET B 1 501 ? 23.794 60.559 10.787 1.00 28.40 ? 501 MET B CB 1 ATOM 8737 C CG . MET B 1 501 ? 23.266 59.470 9.889 1.00 28.99 ? 501 MET B CG 1 ATOM 8738 S SD . MET B 1 501 ? 24.100 59.506 8.283 1.00 33.52 ? 501 MET B SD 1 ATOM 8739 C CE . MET B 1 501 ? 23.355 57.989 7.718 1.00 28.36 ? 501 MET B CE 1 ATOM 8740 N N . VAL B 1 502 ? 24.747 61.106 13.836 1.00 26.03 ? 502 VAL B N 1 ATOM 8741 C CA . VAL B 1 502 ? 25.552 61.993 14.633 1.00 28.74 ? 502 VAL B CA 1 ATOM 8742 C C . VAL B 1 502 ? 26.601 62.680 13.754 1.00 34.84 ? 502 VAL B C 1 ATOM 8743 O O . VAL B 1 502 ? 26.941 62.206 12.612 1.00 28.92 ? 502 VAL B O 1 ATOM 8744 C CB . VAL B 1 502 ? 26.318 61.265 15.731 1.00 28.66 ? 502 VAL B CB 1 ATOM 8745 C CG1 . VAL B 1 502 ? 25.373 60.552 16.694 1.00 27.64 ? 502 VAL B CG1 1 ATOM 8746 C CG2 . VAL B 1 502 ? 27.340 60.300 15.160 1.00 28.85 ? 502 VAL B CG2 1 ATOM 8747 N N . GLU B 1 503 ? 27.122 63.789 14.274 1.00 35.94 ? 503 GLU B N 1 ATOM 8748 C CA . GLU B 1 503 ? 28.093 64.592 13.534 1.00 36.60 ? 503 GLU B CA 1 ATOM 8749 C C . GLU B 1 503 ? 29.295 63.791 13.133 1.00 31.46 ? 503 GLU B C 1 ATOM 8750 O O . GLU B 1 503 ? 29.909 63.134 13.957 1.00 30.49 ? 503 GLU B O 1 ATOM 8751 C CB . GLU B 1 503 ? 28.548 65.831 14.301 1.00 42.97 ? 503 GLU B CB 1 ATOM 8752 C CG . GLU B 1 503 ? 29.054 66.910 13.351 1.00 48.27 ? 503 GLU B CG 1 ATOM 8753 C CD . GLU B 1 503 ? 30.082 67.802 14.027 1.00 62.98 ? 503 GLU B CD 1 ATOM 8754 O OE1 . GLU B 1 503 ? 29.761 68.199 15.152 1.00 61.84 ? 503 GLU B OE1 1 ATOM 8755 O OE2 . GLU B 1 503 ? 31.189 68.093 13.467 1.00 66.44 ? 503 GLU B OE2 1 ATOM 8756 N N . ARG B 1 504 ? 29.573 63.833 11.830 1.00 34.23 ? 504 ARG B N 1 ATOM 8757 C CA . ARG B 1 504 ? 30.696 63.138 11.211 1.00 36.05 ? 504 ARG B CA 1 ATOM 8758 C C . ARG B 1 504 ? 30.588 61.607 11.224 1.00 31.31 ? 504 ARG B C 1 ATOM 8759 O O . ARG B 1 504 ? 31.519 60.948 10.866 1.00 29.72 ? 504 ARG B O 1 ATOM 8760 C CB . ARG B 1 504 ? 32.033 63.587 11.847 1.00 41.56 ? 504 ARG B CB 1 ATOM 8761 C CG . ARG B 1 504 ? 32.448 65.020 11.497 1.00 46.06 ? 504 ARG B CG 1 ATOM 8762 C CD . ARG B 1 504 ? 33.787 65.417 12.142 1.00 47.84 ? 504 ARG B CD 1 ATOM 8763 N NE . ARG B 1 504 ? 33.614 65.720 13.572 1.00 49.48 ? 504 ARG B NE 1 ATOM 8764 C CZ . ARG B 1 504 ? 34.145 65.035 14.584 1.00 54.96 ? 504 ARG B CZ 1 ATOM 8765 N NH1 . ARG B 1 504 ? 34.954 63.994 14.389 1.00 58.70 ? 504 ARG B NH1 1 ATOM 8766 N NH2 . ARG B 1 504 ? 33.878 65.409 15.829 1.00 55.38 ? 504 ARG B NH2 1 ATOM 8767 N N . GLY B 1 505 ? 29.472 61.025 11.659 1.00 32.49 ? 505 GLY B N 1 ATOM 8768 C CA . GLY B 1 505 ? 29.345 59.537 11.663 1.00 28.40 ? 505 GLY B CA 1 ATOM 8769 C C . GLY B 1 505 ? 28.225 59.096 10.687 1.00 26.70 ? 505 GLY B C 1 ATOM 8770 O O . GLY B 1 505 ? 27.724 59.890 9.874 1.00 23.74 ? 505 GLY B O 1 ATOM 8771 N N . ARG B 1 506 ? 27.883 57.815 10.740 1.00 24.37 ? 506 ARG B N 1 ATOM 8772 C CA . ARG B 1 506 ? 26.873 57.255 9.859 1.00 23.52 ? 506 ARG B CA 1 ATOM 8773 C C . ARG B 1 506 ? 25.758 56.530 10.635 1.00 25.84 ? 506 ARG B C 1 ATOM 8774 O O . ARG B 1 506 ? 24.964 55.765 10.064 1.00 24.74 ? 506 ARG B O 1 ATOM 8775 C CB . ARG B 1 506 ? 27.565 56.329 8.888 1.00 22.45 ? 506 ARG B CB 1 ATOM 8776 C CG . ARG B 1 506 ? 28.391 57.081 7.864 1.00 21.83 ? 506 ARG B CG 1 ATOM 8777 C CD . ARG B 1 506 ? 27.471 57.865 6.936 1.00 20.83 ? 506 ARG B CD 1 ATOM 8778 N NE . ARG B 1 506 ? 28.165 58.569 5.870 1.00 22.36 ? 506 ARG B NE 1 ATOM 8779 C CZ . ARG B 1 506 ? 28.493 59.866 5.901 1.00 26.03 ? 506 ARG B CZ 1 ATOM 8780 N NH1 . ARG B 1 506 ? 28.271 60.573 6.981 1.00 24.26 ? 506 ARG B NH1 1 ATOM 8781 N NH2 . ARG B 1 506 ? 29.054 60.462 4.849 1.00 26.66 ? 506 ARG B NH2 1 ATOM 8782 N N . VAL B 1 507 ? 25.713 56.761 11.942 1.00 22.59 ? 507 VAL B N 1 ATOM 8783 C CA . VAL B 1 507 ? 24.608 56.261 12.777 1.00 23.26 ? 507 VAL B CA 1 ATOM 8784 C C . VAL B 1 507 ? 24.191 57.354 13.766 1.00 23.03 ? 507 VAL B C 1 ATOM 8785 O O . VAL B 1 507 ? 24.937 58.309 14.025 1.00 22.28 ? 507 VAL B O 1 ATOM 8786 C CB . VAL B 1 507 ? 24.924 54.962 13.527 1.00 21.02 ? 507 VAL B CB 1 ATOM 8787 C CG1 . VAL B 1 507 ? 25.283 53.825 12.600 1.00 20.96 ? 507 VAL B CG1 1 ATOM 8788 C CG2 . VAL B 1 507 ? 26.021 55.153 14.558 1.00 22.35 ? 507 VAL B CG2 1 ATOM 8789 N N . GLY B 1 508 ? 22.950 57.238 14.250 1.00 24.04 ? 508 GLY B N 1 ATOM 8790 C CA . GLY B 1 508 ? 22.416 58.181 15.230 1.00 23.24 ? 508 GLY B CA 1 ATOM 8791 C C . GLY B 1 508 ? 22.876 57.878 16.650 1.00 22.01 ? 508 GLY B C 1 ATOM 8792 O O . GLY B 1 508 ? 23.677 56.943 16.887 1.00 20.59 ? 508 GLY B O 1 ATOM 8793 N N . PRO B 1 509 ? 22.365 58.671 17.616 1.00 24.32 ? 509 PRO B N 1 ATOM 8794 C CA . PRO B 1 509 ? 22.762 58.596 19.025 1.00 23.53 ? 509 PRO B CA 1 ATOM 8795 C C . PRO B 1 509 ? 22.534 57.229 19.631 1.00 21.79 ? 509 PRO B C 1 ATOM 8796 O O . PRO B 1 509 ? 23.433 56.679 20.246 1.00 21.94 ? 509 PRO B O 1 ATOM 8797 C CB . PRO B 1 509 ? 21.854 59.612 19.701 1.00 25.61 ? 509 PRO B CB 1 ATOM 8798 C CG . PRO B 1 509 ? 21.473 60.590 18.669 1.00 27.69 ? 509 PRO B CG 1 ATOM 8799 C CD . PRO B 1 509 ? 21.436 59.809 17.364 1.00 26.41 ? 509 PRO B CD 1 ATOM 8800 N N . LEU B 1 510 ? 21.376 56.626 19.383 1.00 21.46 ? 510 LEU B N 1 ATOM 8801 C CA . LEU B 1 510 ? 21.137 55.330 20.047 1.00 21.35 ? 510 LEU B CA 1 ATOM 8802 C C . LEU B 1 510 ? 22.124 54.286 19.561 1.00 19.41 ? 510 LEU B C 1 ATOM 8803 O O . LEU B 1 510 ? 22.805 53.597 20.321 1.00 22.76 ? 510 LEU B O 1 ATOM 8804 C CB . LEU B 1 510 ? 19.697 54.880 19.846 1.00 23.55 ? 510 LEU B CB 1 ATOM 8805 C CG . LEU B 1 510 ? 19.303 53.521 20.419 1.00 22.27 ? 510 LEU B CG 1 ATOM 8806 C CD1 . LEU B 1 510 ? 19.675 53.512 21.910 1.00 24.44 ? 510 LEU B CD1 1 ATOM 8807 C CD2 . LEU B 1 510 ? 17.836 53.254 20.236 1.00 25.53 ? 510 LEU B CD2 1 ATOM 8808 N N . LEU B 1 511 ? 22.230 54.146 18.266 1.00 19.85 ? 511 LEU B N 1 ATOM 8809 C CA . LEU B 1 511 ? 23.158 53.133 17.728 1.00 20.21 ? 511 LEU B CA 1 ATOM 8810 C C . LEU B 1 511 ? 24.647 53.374 18.077 1.00 19.63 ? 511 LEU B C 1 ATOM 8811 O O . LEU B 1 511 ? 25.407 52.435 18.304 1.00 19.50 ? 511 LEU B O 1 ATOM 8812 C CB . LEU B 1 511 ? 22.974 53.035 16.226 1.00 19.49 ? 511 LEU B CB 1 ATOM 8813 C CG . LEU B 1 511 ? 21.641 52.439 15.748 1.00 19.56 ? 511 LEU B CG 1 ATOM 8814 C CD1 . LEU B 1 511 ? 21.550 52.523 14.235 1.00 21.46 ? 511 LEU B CD1 1 ATOM 8815 C CD2 . LEU B 1 511 ? 21.434 51.009 16.158 1.00 21.16 ? 511 LEU B CD2 1 ATOM 8816 N N . ALA B 1 512 ? 25.037 54.631 18.109 1.00 18.99 ? 512 ALA B N 1 ATOM 8817 C CA . ALA B 1 512 ? 26.364 54.988 18.518 1.00 22.11 ? 512 ALA B CA 1 ATOM 8818 C C . ALA B 1 512 ? 26.721 54.418 19.883 1.00 20.40 ? 512 ALA B C 1 ATOM 8819 O O . ALA B 1 512 ? 27.846 53.918 20.122 1.00 21.08 ? 512 ALA B O 1 ATOM 8820 C CB . ALA B 1 512 ? 26.511 56.524 18.531 1.00 21.96 ? 512 ALA B CB 1 ATOM 8821 N N . CYS B 1 513 ? 25.763 54.492 20.776 1.00 21.83 ? 513 CYS B N 1 ATOM 8822 C CA . CYS B 1 513 ? 25.933 53.996 22.143 1.00 21.68 ? 513 CYS B CA 1 ATOM 8823 C C . CYS B 1 513 ? 26.025 52.510 22.154 1.00 21.88 ? 513 CYS B C 1 ATOM 8824 O O . CYS B 1 513 ? 26.899 51.937 22.783 1.00 23.70 ? 513 CYS B O 1 ATOM 8825 C CB . CYS B 1 513 ? 24.704 54.484 22.986 1.00 25.23 ? 513 CYS B CB 1 ATOM 8826 S SG . CYS B 1 513 ? 24.419 53.549 24.485 1.00 26.87 ? 513 CYS B SG 1 ATOM 8827 N N . LEU B 1 514 ? 25.105 51.832 21.482 1.00 22.26 ? 514 LEU B N 1 ATOM 8828 C CA . LEU B 1 514 ? 25.100 50.339 21.541 1.00 20.24 ? 514 LEU B CA 1 ATOM 8829 C C . LEU B 1 514 ? 26.332 49.777 20.817 1.00 19.23 ? 514 LEU B C 1 ATOM 8830 O O . LEU B 1 514 ? 26.967 48.891 21.296 1.00 18.80 ? 514 LEU B O 1 ATOM 8831 C CB . LEU B 1 514 ? 23.817 49.745 20.924 1.00 18.97 ? 514 LEU B CB 1 ATOM 8832 C CG . LEU B 1 514 ? 22.519 50.227 21.606 1.00 20.21 ? 514 LEU B CG 1 ATOM 8833 C CD1 . LEU B 1 514 ? 21.272 49.888 20.790 1.00 20.44 ? 514 LEU B CD1 1 ATOM 8834 C CD2 . LEU B 1 514 ? 22.422 49.656 23.006 1.00 20.60 ? 514 LEU B CD2 1 ATOM 8835 N N . LEU B 1 515 ? 26.635 50.298 19.627 1.00 18.63 ? 515 LEU B N 1 ATOM 8836 C CA . LEU B 1 515 ? 27.823 49.853 18.901 1.00 17.64 ? 515 LEU B CA 1 ATOM 8837 C C . LEU B 1 515 ? 29.114 50.230 19.669 1.00 19.15 ? 515 LEU B C 1 ATOM 8838 O O . LEU B 1 515 ? 30.082 49.429 19.740 1.00 22.16 ? 515 LEU B O 1 ATOM 8839 C CB . LEU B 1 515 ? 27.841 50.491 17.516 1.00 17.77 ? 515 LEU B CB 1 ATOM 8840 C CG . LEU B 1 515 ? 26.637 50.174 16.574 1.00 17.53 ? 515 LEU B CG 1 ATOM 8841 C CD1 . LEU B 1 515 ? 26.593 51.209 15.464 1.00 17.66 ? 515 LEU B CD1 1 ATOM 8842 C CD2 . LEU B 1 515 ? 26.806 48.848 15.943 1.00 16.19 ? 515 LEU B CD2 1 ATOM 8843 N N . GLY B 1 516 ? 29.155 51.453 20.166 1.00 20.82 ? 516 GLY B N 1 ATOM 8844 C CA . GLY B 1 516 ? 30.385 52.014 20.782 1.00 25.85 ? 516 GLY B CA 1 ATOM 8845 C C . GLY B 1 516 ? 30.731 51.174 21.995 1.00 25.35 ? 516 GLY B C 1 ATOM 8846 O O . GLY B 1 516 ? 31.846 50.762 22.172 1.00 25.58 ? 516 GLY B O 1 ATOM 8847 N N . ARG B 1 517 ? 29.707 50.841 22.765 1.00 28.72 ? 517 ARG B N 1 ATOM 8848 C CA . ARG B 1 517 ? 29.894 50.047 23.953 1.00 28.77 ? 517 ARG B CA 1 ATOM 8849 C C . ARG B 1 517 ? 30.452 48.709 23.587 1.00 24.01 ? 517 ARG B C 1 ATOM 8850 O O . ARG B 1 517 ? 31.416 48.227 24.194 1.00 21.22 ? 517 ARG B O 1 ATOM 8851 C CB . ARG B 1 517 ? 28.555 49.932 24.691 1.00 31.03 ? 517 ARG B CB 1 ATOM 8852 C CG . ARG B 1 517 ? 28.691 49.831 26.179 1.00 42.20 ? 517 ARG B CG 1 ATOM 8853 C CD . ARG B 1 517 ? 27.323 49.595 26.829 1.00 48.54 ? 517 ARG B CD 1 ATOM 8854 N NE . ARG B 1 517 ? 27.250 48.220 27.325 1.00 52.14 ? 517 ARG B NE 1 ATOM 8855 C CZ . ARG B 1 517 ? 27.267 47.847 28.602 1.00 55.87 ? 517 ARG B CZ 1 ATOM 8856 N NH1 . ARG B 1 517 ? 27.331 48.751 29.570 1.00 59.64 ? 517 ARG B NH1 1 ATOM 8857 N NH2 . ARG B 1 517 ? 27.201 46.546 28.911 1.00 56.87 ? 517 ARG B NH2 1 ATOM 8858 N N . GLN B 1 518 ? 29.824 48.059 22.622 1.00 22.38 ? 518 GLN B N 1 ATOM 8859 C CA . GLN B 1 518 ? 30.288 46.739 22.225 1.00 20.60 ? 518 GLN B CA 1 ATOM 8860 C C . GLN B 1 518 ? 31.735 46.738 21.706 1.00 20.60 ? 518 GLN B C 1 ATOM 8861 O O . GLN B 1 518 ? 32.532 45.915 22.068 1.00 22.10 ? 518 GLN B O 1 ATOM 8862 C CB . GLN B 1 518 ? 29.346 46.119 21.156 1.00 21.30 ? 518 GLN B CB 1 ATOM 8863 C CG . GLN B 1 518 ? 29.672 44.651 20.856 1.00 20.77 ? 518 GLN B CG 1 ATOM 8864 C CD . GLN B 1 518 ? 29.199 43.751 21.976 1.00 23.89 ? 518 GLN B CD 1 ATOM 8865 O OE1 . GLN B 1 518 ? 27.982 43.528 22.125 1.00 20.63 ? 518 GLN B OE1 1 ATOM 8866 N NE2 . GLN B 1 518 ? 30.148 43.213 22.773 1.00 25.77 ? 518 GLN B NE2 1 ATOM 8867 N N . PHE B 1 519 ? 32.067 47.650 20.839 1.00 21.00 ? 519 PHE B N 1 ATOM 8868 C CA . PHE B 1 519 ? 33.406 47.664 20.287 1.00 24.19 ? 519 PHE B CA 1 ATOM 8869 C C . PHE B 1 519 ? 34.482 47.997 21.386 1.00 26.05 ? 519 PHE B C 1 ATOM 8870 O O . PHE B 1 519 ? 35.528 47.357 21.434 1.00 24.78 ? 519 PHE B O 1 ATOM 8871 C CB . PHE B 1 519 ? 33.472 48.608 19.101 1.00 24.33 ? 519 PHE B CB 1 ATOM 8872 C CG . PHE B 1 519 ? 33.005 47.957 17.789 1.00 25.22 ? 519 PHE B CG 1 ATOM 8873 C CD1 . PHE B 1 519 ? 33.786 47.017 17.152 1.00 26.61 ? 519 PHE B CD1 1 ATOM 8874 C CD2 . PHE B 1 519 ? 31.824 48.304 17.204 1.00 26.45 ? 519 PHE B CD2 1 ATOM 8875 C CE1 . PHE B 1 519 ? 33.366 46.421 15.956 1.00 25.39 ? 519 PHE B CE1 1 ATOM 8876 C CE2 . PHE B 1 519 ? 31.389 47.707 16.019 1.00 24.25 ? 519 PHE B CE2 1 ATOM 8877 C CZ . PHE B 1 519 ? 32.165 46.802 15.383 1.00 24.09 ? 519 PHE B CZ 1 ATOM 8878 N N . GLN B 1 520 ? 34.130 48.896 22.310 1.00 27.31 ? 520 GLN B N 1 ATOM 8879 C CA . GLN B 1 520 ? 34.969 49.149 23.501 1.00 28.83 ? 520 GLN B CA 1 ATOM 8880 C C . GLN B 1 520 ? 35.304 47.866 24.202 1.00 30.39 ? 520 GLN B C 1 ATOM 8881 O O . GLN B 1 520 ? 36.482 47.597 24.513 1.00 32.26 ? 520 GLN B O 1 ATOM 8882 C CB . GLN B 1 520 ? 34.292 50.139 24.451 1.00 29.78 ? 520 GLN B CB 1 ATOM 8883 C CG . GLN B 1 520 ? 34.993 50.356 25.816 1.00 34.32 ? 520 GLN B CG 1 ATOM 8884 C CD . GLN B 1 520 ? 34.227 49.704 26.952 1.00 36.50 ? 520 GLN B CD 1 ATOM 8885 O OE1 . GLN B 1 520 ? 33.102 50.107 27.235 1.00 43.54 ? 520 GLN B OE1 1 ATOM 8886 N NE2 . GLN B 1 520 ? 34.801 48.665 27.568 1.00 32.27 ? 520 GLN B NE2 1 ATOM 8887 N N . GLN B 1 521 ? 34.276 47.058 24.463 1.00 27.78 ? 521 GLN B N 1 ATOM 8888 C CA . GLN B 1 521 ? 34.443 45.810 25.170 1.00 24.94 ? 521 GLN B CA 1 ATOM 8889 C C . GLN B 1 521 ? 35.218 44.740 24.457 1.00 30.82 ? 521 GLN B C 1 ATOM 8890 O O . GLN B 1 521 ? 35.912 43.899 25.084 1.00 29.27 ? 521 GLN B O 1 ATOM 8891 C CB . GLN B 1 521 ? 33.067 45.238 25.550 1.00 28.43 ? 521 GLN B CB 1 ATOM 8892 C CG . GLN B 1 521 ? 32.362 46.143 26.545 1.00 29.15 ? 521 GLN B CG 1 ATOM 8893 C CD . GLN B 1 521 ? 30.986 45.678 26.937 1.00 30.79 ? 521 GLN B CD 1 ATOM 8894 O OE1 . GLN B 1 521 ? 30.184 46.494 27.304 1.00 32.54 ? 521 GLN B OE1 1 ATOM 8895 N NE2 . GLN B 1 521 ? 30.704 44.380 26.818 1.00 29.62 ? 521 GLN B NE2 1 ATOM 8896 N N . ILE B 1 522 ? 35.012 44.675 23.152 1.00 28.84 ? 522 ILE B N 1 ATOM 8897 C CA . ILE B 1 522 ? 35.707 43.736 22.299 1.00 30.47 ? 522 ILE B CA 1 ATOM 8898 C C . ILE B 1 522 ? 37.217 43.997 22.362 1.00 25.22 ? 522 ILE B C 1 ATOM 8899 O O . ILE B 1 522 ? 38.017 43.088 22.317 1.00 24.96 ? 522 ILE B O 1 ATOM 8900 C CB . ILE B 1 522 ? 35.179 44.031 20.848 1.00 32.28 ? 522 ILE B CB 1 ATOM 8901 C CG1 . ILE B 1 522 ? 33.896 43.289 20.539 1.00 36.04 ? 522 ILE B CG1 1 ATOM 8902 C CG2 . ILE B 1 522 ? 36.177 43.853 19.723 1.00 36.48 ? 522 ILE B CG2 1 ATOM 8903 C CD1 . ILE B 1 522 ? 33.302 43.868 19.271 1.00 39.43 ? 522 ILE B CD1 1 ATOM 8904 N N . ARG B 1 523 ? 37.579 45.263 22.335 1.00 24.95 ? 523 ARG B N 1 ATOM 8905 C CA . ARG B 1 523 ? 38.957 45.634 22.450 1.00 29.49 ? 523 ARG B CA 1 ATOM 8906 C C . ARG B 1 523 ? 39.446 45.422 23.893 1.00 29.80 ? 523 ARG B C 1 ATOM 8907 O O . ARG B 1 523 ? 40.318 44.590 24.096 1.00 33.05 ? 523 ARG B O 1 ATOM 8908 C CB . ARG B 1 523 ? 39.186 47.076 22.068 1.00 28.86 ? 523 ARG B CB 1 ATOM 8909 C CG . ARG B 1 523 ? 40.614 47.511 22.428 1.00 31.88 ? 523 ARG B CG 1 ATOM 8910 C CD . ARG B 1 523 ? 40.770 48.995 22.265 1.00 30.67 ? 523 ARG B CD 1 ATOM 8911 N NE . ARG B 1 523 ? 40.034 49.660 23.311 1.00 33.91 ? 523 ARG B NE 1 ATOM 8912 C CZ . ARG B 1 523 ? 39.972 50.973 23.478 1.00 35.01 ? 523 ARG B CZ 1 ATOM 8913 N NH1 . ARG B 1 523 ? 40.610 51.782 22.669 1.00 36.36 ? 523 ARG B NH1 1 ATOM 8914 N NH2 . ARG B 1 523 ? 39.260 51.471 24.483 1.00 42.22 ? 523 ARG B NH2 1 ATOM 8915 N N . ASP B 1 524 ? 38.819 46.104 24.867 1.00 31.03 ? 524 ASP B N 1 ATOM 8916 C CA . ASP B 1 524 ? 39.316 46.024 26.277 1.00 27.56 ? 524 ASP B CA 1 ATOM 8917 C C . ASP B 1 524 ? 39.306 44.628 26.884 1.00 29.20 ? 524 ASP B C 1 ATOM 8918 O O . ASP B 1 524 ? 40.068 44.315 27.824 1.00 33.04 ? 524 ASP B O 1 ATOM 8919 C CB . ASP B 1 524 ? 38.572 47.010 27.162 1.00 24.94 ? 524 ASP B CB 1 ATOM 8920 C CG . ASP B 1 524 ? 38.710 48.370 26.683 1.00 24.78 ? 524 ASP B CG 1 ATOM 8921 O OD1 . ASP B 1 524 ? 39.544 48.543 25.778 1.00 30.26 ? 524 ASP B OD1 1 ATOM 8922 O OD2 . ASP B 1 524 ? 37.999 49.289 27.135 1.00 27.22 ? 524 ASP B OD2 1 ATOM 8923 N N . GLY B 1 525 ? 38.472 43.734 26.356 1.00 30.00 ? 525 GLY B N 1 ATOM 8924 C CA . GLY B 1 525 ? 38.264 42.412 26.960 1.00 24.98 ? 525 GLY B CA 1 ATOM 8925 C C . GLY B 1 525 ? 38.923 41.284 26.230 1.00 25.48 ? 525 GLY B C 1 ATOM 8926 O O . GLY B 1 525 ? 38.697 40.092 26.527 1.00 28.38 ? 525 GLY B O 1 ATOM 8927 N N . ASP B 1 526 ? 39.801 41.624 25.296 1.00 29.49 ? 526 ASP B N 1 ATOM 8928 C CA . ASP B 1 526 ? 40.473 40.606 24.482 1.00 32.19 ? 526 ASP B CA 1 ATOM 8929 C C . ASP B 1 526 ? 41.940 40.495 24.956 1.00 36.27 ? 526 ASP B C 1 ATOM 8930 O O . ASP B 1 526 ? 42.708 41.466 24.804 1.00 36.69 ? 526 ASP B O 1 ATOM 8931 C CB . ASP B 1 526 ? 40.389 41.063 23.009 1.00 30.45 ? 526 ASP B CB 1 ATOM 8932 C CG . ASP B 1 526 ? 41.063 40.130 22.053 1.00 32.15 ? 526 ASP B CG 1 ATOM 8933 O OD1 . ASP B 1 526 ? 41.434 38.969 22.428 1.00 32.32 ? 526 ASP B OD1 1 ATOM 8934 O OD2 . ASP B 1 526 ? 41.142 40.541 20.885 1.00 30.55 ? 526 ASP B OD2 1 ATOM 8935 N N . ARG B 1 527 ? 42.333 39.337 25.482 1.00 34.86 ? 527 ARG B N 1 ATOM 8936 C CA . ARG B 1 527 ? 43.722 39.144 25.956 1.00 39.47 ? 527 ARG B CA 1 ATOM 8937 C C . ARG B 1 527 ? 44.742 39.177 24.814 1.00 47.37 ? 527 ARG B C 1 ATOM 8938 O O . ARG B 1 527 ? 45.936 39.506 25.010 1.00 41.62 ? 527 ARG B O 1 ATOM 8939 C CB . ARG B 1 527 ? 43.860 37.796 26.658 1.00 41.44 ? 527 ARG B CB 1 ATOM 8940 C CG . ARG B 1 527 ? 45.248 37.551 27.243 1.00 40.21 ? 527 ARG B CG 1 ATOM 8941 C CD . ARG B 1 527 ? 45.184 36.586 28.418 1.00 37.15 ? 527 ARG B CD 1 ATOM 8942 N NE . ARG B 1 527 ? 44.824 35.230 28.047 1.00 35.20 ? 527 ARG B NE 1 ATOM 8943 C CZ . ARG B 1 527 ? 45.625 34.377 27.430 1.00 42.07 ? 527 ARG B CZ 1 ATOM 8944 N NH1 . ARG B 1 527 ? 46.865 34.738 27.099 1.00 57.05 ? 527 ARG B NH1 1 ATOM 8945 N NH2 . ARG B 1 527 ? 45.208 33.149 27.143 1.00 39.13 ? 527 ARG B NH2 1 ATOM 8946 N N . PHE B 1 528 ? 44.270 38.850 23.611 1.00 44.47 ? 528 PHE B N 1 ATOM 8947 C CA . PHE B 1 528 ? 45.133 38.849 22.445 1.00 40.97 ? 528 PHE B CA 1 ATOM 8948 C C . PHE B 1 528 ? 44.894 40.069 21.558 1.00 38.81 ? 528 PHE B C 1 ATOM 8949 O O . PHE B 1 528 ? 45.249 40.039 20.368 1.00 35.48 ? 528 PHE B O 1 ATOM 8950 C CB . PHE B 1 528 ? 44.911 37.580 21.630 1.00 44.20 ? 528 PHE B CB 1 ATOM 8951 C CG . PHE B 1 528 ? 45.228 36.289 22.350 1.00 43.99 ? 528 PHE B CG 1 ATOM 8952 C CD1 . PHE B 1 528 ? 44.244 35.600 23.048 1.00 47.07 ? 528 PHE B CD1 1 ATOM 8953 C CD2 . PHE B 1 528 ? 46.493 35.710 22.252 1.00 46.53 ? 528 PHE B CD2 1 ATOM 8954 C CE1 . PHE B 1 528 ? 44.520 34.383 23.676 1.00 47.82 ? 528 PHE B CE1 1 ATOM 8955 C CE2 . PHE B 1 528 ? 46.776 34.492 22.880 1.00 48.87 ? 528 PHE B CE2 1 ATOM 8956 C CZ . PHE B 1 528 ? 45.783 33.821 23.582 1.00 47.17 ? 528 PHE B CZ 1 ATOM 8957 N N . TRP B 1 529 ? 44.295 41.132 22.100 1.00 33.74 ? 529 TRP B N 1 ATOM 8958 C CA . TRP B 1 529 ? 44.240 42.394 21.371 1.00 33.01 ? 529 TRP B CA 1 ATOM 8959 C C . TRP B 1 529 ? 45.653 42.717 20.902 1.00 40.96 ? 529 TRP B C 1 ATOM 8960 O O . TRP B 1 529 ? 46.625 42.539 21.647 1.00 49.64 ? 529 TRP B O 1 ATOM 8961 C CB . TRP B 1 529 ? 43.668 43.529 22.210 1.00 26.90 ? 529 TRP B CB 1 ATOM 8962 C CG . TRP B 1 529 ? 43.511 44.862 21.484 1.00 29.46 ? 529 TRP B CG 1 ATOM 8963 C CD1 . TRP B 1 529 ? 44.193 46.032 21.703 1.00 32.27 ? 529 TRP B CD1 1 ATOM 8964 C CD2 . TRP B 1 529 ? 42.548 45.165 20.467 1.00 30.37 ? 529 TRP B CD2 1 ATOM 8965 N NE1 . TRP B 1 529 ? 43.724 47.051 20.855 1.00 30.48 ? 529 TRP B NE1 1 ATOM 8966 C CE2 . TRP B 1 529 ? 42.731 46.513 20.079 1.00 32.76 ? 529 TRP B CE2 1 ATOM 8967 C CE3 . TRP B 1 529 ? 41.542 44.417 19.852 1.00 30.73 ? 529 TRP B CE3 1 ATOM 8968 C CZ2 . TRP B 1 529 ? 41.948 47.108 19.086 1.00 35.21 ? 529 TRP B CZ2 1 ATOM 8969 C CZ3 . TRP B 1 529 ? 40.791 44.993 18.880 1.00 31.29 ? 529 TRP B CZ3 1 ATOM 8970 C CH2 . TRP B 1 529 ? 40.989 46.323 18.504 1.00 34.64 ? 529 TRP B CH2 1 ATOM 8971 N N . TRP B 1 530 ? 45.775 43.227 19.686 1.00 42.08 ? 530 TRP B N 1 ATOM 8972 C CA . TRP B 1 530 ? 47.075 43.395 19.061 1.00 38.44 ? 530 TRP B CA 1 ATOM 8973 C C . TRP B 1 530 ? 47.959 44.409 19.802 1.00 45.05 ? 530 TRP B C 1 ATOM 8974 O O . TRP B 1 530 ? 49.180 44.265 19.831 1.00 40.98 ? 530 TRP B O 1 ATOM 8975 C CB . TRP B 1 530 ? 46.934 43.854 17.622 1.00 32.77 ? 530 TRP B CB 1 ATOM 8976 C CG . TRP B 1 530 ? 46.630 45.280 17.492 1.00 28.83 ? 530 TRP B CG 1 ATOM 8977 C CD1 . TRP B 1 530 ? 45.413 45.874 17.565 1.00 31.58 ? 530 TRP B CD1 1 ATOM 8978 C CD2 . TRP B 1 530 ? 47.555 46.311 17.179 1.00 31.24 ? 530 TRP B CD2 1 ATOM 8979 N NE1 . TRP B 1 530 ? 45.520 47.256 17.368 1.00 29.13 ? 530 TRP B NE1 1 ATOM 8980 C CE2 . TRP B 1 530 ? 46.839 47.535 17.144 1.00 28.69 ? 530 TRP B CE2 1 ATOM 8981 C CE3 . TRP B 1 530 ? 48.948 46.340 17.010 1.00 30.26 ? 530 TRP B CE3 1 ATOM 8982 C CZ2 . TRP B 1 530 ? 47.454 48.749 16.867 1.00 34.03 ? 530 TRP B CZ2 1 ATOM 8983 C CZ3 . TRP B 1 530 ? 49.565 47.575 16.739 1.00 30.97 ? 530 TRP B CZ3 1 ATOM 8984 C CH2 . TRP B 1 530 ? 48.818 48.752 16.664 1.00 31.28 ? 530 TRP B CH2 1 ATOM 8985 N N . GLU B 1 531 ? 47.337 45.441 20.359 1.00 43.26 ? 531 GLU B N 1 ATOM 8986 C CA . GLU B 1 531 ? 48.019 46.455 21.144 1.00 43.45 ? 531 GLU B CA 1 ATOM 8987 C C . GLU B 1 531 ? 48.293 45.986 22.602 1.00 40.29 ? 531 GLU B C 1 ATOM 8988 O O . GLU B 1 531 ? 48.906 46.718 23.367 1.00 42.13 ? 531 GLU B O 1 ATOM 8989 C CB . GLU B 1 531 ? 47.108 47.692 21.169 1.00 43.99 ? 531 GLU B CB 1 ATOM 8990 C CG . GLU B 1 531 ? 47.686 49.030 20.774 1.00 47.47 ? 531 GLU B CG 1 ATOM 8991 C CD . GLU B 1 531 ? 46.621 50.123 20.700 1.00 50.19 ? 531 GLU B CD 1 ATOM 8992 O OE1 . GLU B 1 531 ? 45.384 49.805 20.799 1.00 52.79 ? 531 GLU B OE1 1 ATOM 8993 O OE2 . GLU B 1 531 ? 47.018 51.315 20.530 1.00 43.65 ? 531 GLU B OE2 1 ATOM 8994 N N . ASN B 1 532 ? 47.855 44.795 23.011 1.00 46.11 ? 532 ASN B N 1 ATOM 8995 C CA . ASN B 1 532 ? 48.094 44.370 24.390 1.00 43.67 ? 532 ASN B CA 1 ATOM 8996 C C . ASN B 1 532 ? 49.562 43.972 24.614 1.00 41.75 ? 532 ASN B C 1 ATOM 8997 O O . ASN B 1 532 ? 50.034 42.977 24.019 1.00 32.74 ? 532 ASN B O 1 ATOM 8998 C CB . ASN B 1 532 ? 47.210 43.195 24.840 1.00 42.83 ? 532 ASN B CB 1 ATOM 8999 C CG . ASN B 1 532 ? 47.307 42.959 26.354 1.00 41.19 ? 532 ASN B CG 1 ATOM 9000 O OD1 . ASN B 1 532 ? 47.511 43.905 27.087 1.00 36.56 ? 532 ASN B OD1 1 ATOM 9001 N ND2 . ASN B 1 532 ? 47.149 41.729 26.810 1.00 43.49 ? 532 ASN B ND2 1 ATOM 9002 N N . PRO B 1 533 ? 50.267 44.694 25.519 1.00 41.19 ? 533 PRO B N 1 ATOM 9003 C CA . PRO B 1 533 ? 51.692 44.380 25.709 1.00 37.92 ? 533 PRO B CA 1 ATOM 9004 C C . PRO B 1 533 ? 51.903 42.894 25.849 1.00 37.91 ? 533 PRO B C 1 ATOM 9005 O O . PRO B 1 533 ? 51.106 42.234 26.539 1.00 37.82 ? 533 PRO B O 1 ATOM 9006 C CB . PRO B 1 533 ? 52.031 45.141 26.998 1.00 40.63 ? 533 PRO B CB 1 ATOM 9007 C CG . PRO B 1 533 ? 51.200 46.394 26.900 1.00 41.33 ? 533 PRO B CG 1 ATOM 9008 C CD . PRO B 1 533 ? 49.892 45.915 26.270 1.00 41.36 ? 533 PRO B CD 1 ATOM 9009 N N . GLY B 1 534 ? 52.921 42.370 25.156 1.00 36.29 ? 534 GLY B N 1 ATOM 9010 C CA . GLY B 1 534 ? 53.219 40.953 25.200 1.00 35.46 ? 534 GLY B CA 1 ATOM 9011 C C . GLY B 1 534 ? 52.646 40.066 24.100 1.00 39.65 ? 534 GLY B C 1 ATOM 9012 O O . GLY B 1 534 ? 53.110 38.924 23.913 1.00 43.03 ? 534 GLY B O 1 ATOM 9013 N N . VAL B 1 535 ? 51.619 40.538 23.392 1.00 41.65 ? 535 VAL B N 1 ATOM 9014 C CA . VAL B 1 535 ? 50.993 39.760 22.300 1.00 41.68 ? 535 VAL B CA 1 ATOM 9015 C C . VAL B 1 535 ? 51.934 39.746 21.092 1.00 41.22 ? 535 VAL B C 1 ATOM 9016 O O . VAL B 1 535 ? 52.223 38.673 20.528 1.00 42.07 ? 535 VAL B O 1 ATOM 9017 C CB . VAL B 1 535 ? 49.599 40.357 21.917 1.00 44.69 ? 535 VAL B CB 1 ATOM 9018 C CG1 . VAL B 1 535 ? 49.013 39.688 20.653 1.00 43.72 ? 535 VAL B CG1 1 ATOM 9019 C CG2 . VAL B 1 535 ? 48.632 40.180 23.082 1.00 41.93 ? 535 VAL B CG2 1 ATOM 9020 N N . PHE B 1 536 ? 52.336 40.958 20.716 1.00 43.22 ? 536 PHE B N 1 ATOM 9021 C CA . PHE B 1 536 ? 53.350 41.238 19.727 1.00 51.50 ? 536 PHE B CA 1 ATOM 9022 C C . PHE B 1 536 ? 54.488 42.063 20.373 1.00 54.50 ? 536 PHE B C 1 ATOM 9023 O O . PHE B 1 536 ? 54.258 42.879 21.276 1.00 53.18 ? 536 PHE B O 1 ATOM 9024 C CB . PHE B 1 536 ? 52.760 42.112 18.606 1.00 58.20 ? 536 PHE B CB 1 ATOM 9025 C CG . PHE B 1 536 ? 51.776 41.397 17.709 1.00 61.66 ? 536 PHE B CG 1 ATOM 9026 C CD1 . PHE B 1 536 ? 52.203 40.396 16.839 1.00 59.75 ? 536 PHE B CD1 1 ATOM 9027 C CD2 . PHE B 1 536 ? 50.428 41.739 17.720 1.00 62.69 ? 536 PHE B CD2 1 ATOM 9028 C CE1 . PHE B 1 536 ? 51.304 39.743 16.009 1.00 63.87 ? 536 PHE B CE1 1 ATOM 9029 C CE2 . PHE B 1 536 ? 49.525 41.077 16.899 1.00 63.84 ? 536 PHE B CE2 1 ATOM 9030 C CZ . PHE B 1 536 ? 49.964 40.084 16.038 1.00 61.98 ? 536 PHE B CZ 1 ATOM 9031 N N . THR B 1 537 ? 55.702 41.886 19.859 1.00 49.58 ? 537 THR B N 1 ATOM 9032 C CA . THR B 1 537 ? 56.854 42.662 20.327 1.00 44.25 ? 537 THR B CA 1 ATOM 9033 C C . THR B 1 537 ? 56.586 44.037 19.863 1.00 42.13 ? 537 THR B C 1 ATOM 9034 O O . THR B 1 537 ? 55.742 44.216 18.988 1.00 40.34 ? 537 THR B O 1 ATOM 9035 C CB . THR B 1 537 ? 58.155 42.215 19.659 1.00 44.39 ? 537 THR B CB 1 ATOM 9036 O OG1 . THR B 1 537 ? 58.184 42.697 18.305 1.00 46.69 ? 537 THR B OG1 1 ATOM 9037 C CG2 . THR B 1 537 ? 58.288 40.686 19.689 1.00 45.40 ? 537 THR B CG2 1 ATOM 9038 N N . GLU B 1 538 ? 57.300 45.021 20.404 1.00 39.57 ? 538 GLU B N 1 ATOM 9039 C CA . GLU B 1 538 ? 57.067 46.418 20.009 1.00 43.92 ? 538 GLU B CA 1 ATOM 9040 C C . GLU B 1 538 ? 57.443 46.674 18.570 1.00 51.43 ? 538 GLU B C 1 ATOM 9041 O O . GLU B 1 538 ? 56.884 47.550 17.930 1.00 54.32 ? 538 GLU B O 1 ATOM 9042 C CB . GLU B 1 538 ? 57.858 47.387 20.896 1.00 39.25 ? 538 GLU B CB 1 ATOM 9043 C CG . GLU B 1 538 ? 57.703 48.852 20.527 1.00 43.59 ? 538 GLU B CG 1 ATOM 9044 C CD . GLU B 1 538 ? 58.367 49.763 21.532 1.00 47.72 ? 538 GLU B CD 1 ATOM 9045 O OE1 . GLU B 1 538 ? 58.759 49.257 22.595 1.00 43.14 ? 538 GLU B OE1 1 ATOM 9046 O OE2 . GLU B 1 538 ? 58.506 50.974 21.255 1.00 53.17 ? 538 GLU B OE2 1 ATOM 9047 N N . LYS B 1 539 ? 58.476 45.975 18.110 1.00 62.39 ? 539 LYS B N 1 ATOM 9048 C CA . LYS B 1 539 ? 58.929 46.035 16.722 1.00 66.17 ? 539 LYS B CA 1 ATOM 9049 C C . LYS B 1 539 ? 57.788 45.607 15.780 1.00 54.24 ? 539 LYS B C 1 ATOM 9050 O O . LYS B 1 539 ? 57.419 46.334 14.840 1.00 43.87 ? 539 LYS B O 1 ATOM 9051 C CB . LYS B 1 539 ? 60.150 45.089 16.540 1.00 72.68 ? 539 LYS B CB 1 ATOM 9052 C CG . LYS B 1 539 ? 61.525 45.740 16.689 1.00 75.98 ? 539 LYS B CG 1 ATOM 9053 C CD . LYS B 1 539 ? 62.621 44.842 16.083 1.00 80.14 ? 539 LYS B CD 1 ATOM 9054 C CE . LYS B 1 539 ? 62.967 43.661 16.993 1.00 81.67 ? 539 LYS B CE 1 ATOM 9055 N NZ . LYS B 1 539 ? 63.995 42.749 16.407 1.00 82.97 ? 539 LYS B NZ 1 ATOM 9056 N N . GLN B 1 540 ? 57.230 44.442 16.085 1.00 51.51 ? 540 GLN B N 1 ATOM 9057 C CA . GLN B 1 540 ? 56.043 43.937 15.386 1.00 48.17 ? 540 GLN B CA 1 ATOM 9058 C C . GLN B 1 540 ? 54.908 44.974 15.390 1.00 48.84 ? 540 GLN B C 1 ATOM 9059 O O . GLN B 1 540 ? 54.375 45.391 14.335 1.00 49.59 ? 540 GLN B O 1 ATOM 9060 C CB . GLN B 1 540 ? 55.636 42.624 16.012 1.00 45.36 ? 540 GLN B CB 1 ATOM 9061 C CG . GLN B 1 540 ? 56.647 41.568 15.682 1.00 39.50 ? 540 GLN B CG 1 ATOM 9062 C CD . GLN B 1 540 ? 56.410 40.312 16.454 1.00 40.56 ? 540 GLN B CD 1 ATOM 9063 O OE1 . GLN B 1 540 ? 55.727 40.306 17.471 1.00 41.11 ? 540 GLN B OE1 1 ATOM 9064 N NE2 . GLN B 1 540 ? 56.962 39.216 15.962 1.00 42.82 ? 540 GLN B NE2 1 ATOM 9065 N N . ARG B 1 541 ? 54.573 45.491 16.559 1.00 42.40 ? 541 ARG B N 1 ATOM 9066 C CA . ARG B 1 541 ? 53.580 46.551 16.565 1.00 45.11 ? 541 ARG B CA 1 ATOM 9067 C C . ARG B 1 541 ? 53.881 47.698 15.653 1.00 43.66 ? 541 ARG B C 1 ATOM 9068 O O . ARG B 1 541 ? 52.962 48.204 15.008 1.00 47.04 ? 541 ARG B O 1 ATOM 9069 C CB . ARG B 1 541 ? 53.260 47.040 17.974 1.00 46.10 ? 541 ARG B CB 1 ATOM 9070 C CG . ARG B 1 541 ? 52.614 45.915 18.779 1.00 50.94 ? 541 ARG B CG 1 ATOM 9071 C CD . ARG B 1 541 ? 51.875 46.382 20.022 1.00 52.45 ? 541 ARG B CD 1 ATOM 9072 N NE . ARG B 1 541 ? 52.679 45.984 21.141 1.00 52.38 ? 541 ARG B NE 1 ATOM 9073 C CZ . ARG B 1 541 ? 53.541 46.753 21.759 1.00 48.95 ? 541 ARG B CZ 1 ATOM 9074 N NH1 . ARG B 1 541 ? 54.252 46.211 22.737 1.00 47.81 ? 541 ARG B NH1 1 ATOM 9075 N NH2 . ARG B 1 541 ? 53.676 48.042 21.416 1.00 47.01 ? 541 ARG B NH2 1 ATOM 9076 N N . ASP B 1 542 ? 55.045 48.169 15.663 1.00 44.99 ? 542 ASP B N 1 ATOM 9077 C CA . ASP B 1 542 ? 55.409 49.350 14.893 1.00 45.11 ? 542 ASP B CA 1 ATOM 9078 C C . ASP B 1 542 ? 55.093 49.173 13.414 1.00 42.80 ? 542 ASP B C 1 ATOM 9079 O O . ASP B 1 542 ? 54.549 50.055 12.787 1.00 43.52 ? 542 ASP B O 1 ATOM 9080 C CB . ASP B 1 542 ? 56.881 49.631 15.035 1.00 53.18 ? 542 ASP B CB 1 ATOM 9081 C CG . ASP B 1 542 ? 57.267 49.999 16.456 1.00 54.72 ? 542 ASP B CG 1 ATOM 9082 O OD1 . ASP B 1 542 ? 56.385 50.035 17.332 1.00 54.56 ? 542 ASP B OD1 1 ATOM 9083 O OD2 . ASP B 1 542 ? 58.479 50.244 16.686 1.00 58.97 ? 542 ASP B OD2 1 ATOM 9084 N N . SER B 1 543 ? 55.487 48.010 12.844 1.00 40.16 ? 543 SER B N 1 ATOM 9085 C CA . SER B 1 543 ? 55.196 47.690 11.426 1.00 48.26 ? 543 SER B CA 1 ATOM 9086 C C . SER B 1 543 ? 53.658 47.554 11.178 1.00 53.57 ? 543 SER B C 1 ATOM 9087 O O . SER B 1 543 ? 53.104 48.103 10.192 1.00 45.82 ? 543 SER B O 1 ATOM 9088 C CB . SER B 1 543 ? 55.977 46.481 10.934 1.00 47.96 ? 543 SER B CB 1 ATOM 9089 O OG . SER B 1 543 ? 56.255 45.590 11.982 1.00 53.18 ? 543 SER B OG 1 ATOM 9090 N N . LEU B 1 544 ? 52.963 46.898 12.121 1.00 49.04 ? 544 LEU B N 1 ATOM 9091 C CA . LEU B 1 544 ? 51.519 46.721 11.997 1.00 43.68 ? 544 LEU B CA 1 ATOM 9092 C C . LEU B 1 544 ? 50.798 48.027 11.825 1.00 44.89 ? 544 LEU B C 1 ATOM 9093 O O . LEU B 1 544 ? 49.873 48.103 11.020 1.00 52.65 ? 544 LEU B O 1 ATOM 9094 C CB . LEU B 1 544 ? 50.959 45.952 13.179 1.00 38.11 ? 544 LEU B CB 1 ATOM 9095 C CG . LEU B 1 544 ? 51.345 44.480 13.182 1.00 34.73 ? 544 LEU B CG 1 ATOM 9096 C CD1 . LEU B 1 544 ? 50.948 43.878 14.495 1.00 34.98 ? 544 LEU B CD1 1 ATOM 9097 C CD2 . LEU B 1 544 ? 50.715 43.694 12.037 1.00 36.39 ? 544 LEU B CD2 1 ATOM 9098 N N . GLN B 1 545 ? 51.298 49.098 12.392 1.00 45.23 ? 545 GLN B N 1 ATOM 9099 C CA . GLN B 1 545 ? 50.630 50.371 12.329 1.00 44.88 ? 545 GLN B CA 1 ATOM 9100 C C . GLN B 1 545 ? 50.457 50.890 10.924 1.00 45.09 ? 545 GLN B C 1 ATOM 9101 O O . GLN B 1 545 ? 49.771 51.856 10.720 1.00 47.95 ? 545 GLN B O 1 ATOM 9102 C CB . GLN B 1 545 ? 51.438 51.422 13.041 1.00 52.09 ? 545 GLN B CB 1 ATOM 9103 C CG . GLN B 1 545 ? 50.793 52.029 14.268 1.00 58.54 ? 545 GLN B CG 1 ATOM 9104 C CD . GLN B 1 545 ? 51.460 51.559 15.558 1.00 69.01 ? 545 GLN B CD 1 ATOM 9105 O OE1 . GLN B 1 545 ? 50.934 51.759 16.647 1.00 75.65 ? 545 GLN B OE1 1 ATOM 9106 N NE2 . GLN B 1 545 ? 52.617 50.915 15.429 1.00 61.51 ? 545 GLN B NE2 1 ATOM 9107 N N . LYS B 1 546 ? 51.215 50.356 9.993 1.00 45.26 ? 546 LYS B N 1 ATOM 9108 C CA . LYS B 1 546 ? 51.253 50.871 8.622 1.00 44.26 ? 546 LYS B CA 1 ATOM 9109 C C . LYS B 1 546 ? 50.270 50.168 7.693 1.00 38.53 ? 546 LYS B C 1 ATOM 9110 O O . LYS B 1 546 ? 50.140 50.569 6.532 1.00 31.98 ? 546 LYS B O 1 ATOM 9111 C CB . LYS B 1 546 ? 52.657 50.643 8.004 1.00 54.54 ? 546 LYS B CB 1 ATOM 9112 C CG . LYS B 1 546 ? 53.856 51.158 8.810 1.00 61.31 ? 546 LYS B CG 1 ATOM 9113 C CD . LYS B 1 546 ? 54.074 52.672 8.785 1.00 66.27 ? 546 LYS B CD 1 ATOM 9114 C CE . LYS B 1 546 ? 55.009 53.098 9.918 1.00 71.72 ? 546 LYS B CE 1 ATOM 9115 N NZ . LYS B 1 546 ? 54.467 52.878 11.300 1.00 75.97 ? 546 LYS B NZ 1 ATOM 9116 N N . VAL B 1 547 ? 49.623 49.101 8.162 1.00 38.32 ? 547 VAL B N 1 ATOM 9117 C CA . VAL B 1 547 ? 48.718 48.335 7.283 1.00 34.40 ? 547 VAL B CA 1 ATOM 9118 C C . VAL B 1 547 ? 47.632 49.233 6.760 1.00 34.96 ? 547 VAL B C 1 ATOM 9119 O O . VAL B 1 547 ? 47.339 50.236 7.390 1.00 33.78 ? 547 VAL B O 1 ATOM 9120 C CB . VAL B 1 547 ? 48.157 47.052 7.920 1.00 37.35 ? 547 VAL B CB 1 ATOM 9121 C CG1 . VAL B 1 547 ? 49.284 46.105 8.304 1.00 37.41 ? 547 VAL B CG1 1 ATOM 9122 C CG2 . VAL B 1 547 ? 47.262 47.335 9.116 1.00 39.03 ? 547 VAL B CG2 1 ATOM 9123 N N . SER B 1 548 ? 47.102 48.937 5.563 1.00 32.42 ? 548 SER B N 1 ATOM 9124 C CA . SER B 1 548 ? 45.932 49.626 5.039 1.00 31.21 ? 548 SER B CA 1 ATOM 9125 C C . SER B 1 548 ? 45.135 48.683 4.137 1.00 32.89 ? 548 SER B C 1 ATOM 9126 O O . SER B 1 548 ? 45.658 47.697 3.662 1.00 25.60 ? 548 SER B O 1 ATOM 9127 C CB . SER B 1 548 ? 46.323 50.872 4.251 1.00 34.44 ? 548 SER B CB 1 ATOM 9128 O OG . SER B 1 548 ? 47.113 50.560 3.123 1.00 36.08 ? 548 SER B OG 1 ATOM 9129 N N . PHE B 1 549 ? 43.865 49.005 3.898 1.00 33.51 ? 549 PHE B N 1 ATOM 9130 C CA . PHE B 1 549 ? 43.124 48.217 2.966 1.00 30.44 ? 549 PHE B CA 1 ATOM 9131 C C . PHE B 1 549 ? 43.723 48.376 1.565 1.00 28.96 ? 549 PHE B C 1 ATOM 9132 O O . PHE B 1 549 ? 43.756 47.424 0.820 1.00 28.37 ? 549 PHE B O 1 ATOM 9133 C CB . PHE B 1 549 ? 41.627 48.561 2.918 1.00 31.98 ? 549 PHE B CB 1 ATOM 9134 C CG . PHE B 1 549 ? 40.800 47.412 2.431 1.00 31.59 ? 549 PHE B CG 1 ATOM 9135 C CD1 . PHE B 1 549 ? 40.642 47.181 1.078 1.00 33.10 ? 549 PHE B CD1 1 ATOM 9136 C CD2 . PHE B 1 549 ? 40.265 46.507 3.310 1.00 29.90 ? 549 PHE B CD2 1 ATOM 9137 C CE1 . PHE B 1 549 ? 39.920 46.085 0.622 1.00 33.99 ? 549 PHE B CE1 1 ATOM 9138 C CE2 . PHE B 1 549 ? 39.558 45.397 2.850 1.00 30.84 ? 549 PHE B CE2 1 ATOM 9139 C CZ . PHE B 1 549 ? 39.373 45.198 1.506 1.00 30.46 ? 549 PHE B CZ 1 ATOM 9140 N N . SER B 1 550 ? 44.146 49.585 1.204 1.00 29.88 ? 550 SER B N 1 ATOM 9141 C CA . SER B 1 550 ? 44.743 49.824 -0.130 1.00 30.05 ? 550 SER B CA 1 ATOM 9142 C C . SER B 1 550 ? 45.912 48.916 -0.373 1.00 28.83 ? 550 SER B C 1 ATOM 9143 O O . SER B 1 550 ? 46.050 48.404 -1.451 1.00 31.58 ? 550 SER B O 1 ATOM 9144 C CB . SER B 1 550 ? 45.170 51.264 -0.335 1.00 32.25 ? 550 SER B CB 1 ATOM 9145 O OG . SER B 1 550 ? 44.070 52.124 -0.262 1.00 35.65 ? 550 SER B OG 1 ATOM 9146 N N . ARG B 1 551 ? 46.734 48.676 0.650 1.00 28.24 ? 551 ARG B N 1 ATOM 9147 C CA . ARG B 1 551 ? 47.888 47.830 0.498 1.00 28.33 ? 551 ARG B CA 1 ATOM 9148 C C . ARG B 1 551 ? 47.506 46.374 0.403 1.00 29.17 ? 551 ARG B C 1 ATOM 9149 O O . ARG B 1 551 ? 48.113 45.575 -0.352 1.00 31.23 ? 551 ARG B O 1 ATOM 9150 C CB . ARG B 1 551 ? 48.860 48.055 1.676 1.00 30.40 ? 551 ARG B CB 1 ATOM 9151 C CG . ARG B 1 551 ? 49.902 46.934 1.895 1.00 30.26 ? 551 ARG B CG 1 ATOM 9152 C CD . ARG B 1 551 ? 50.843 46.675 0.681 1.00 32.79 ? 551 ARG B CD 1 ATOM 9153 N NE . ARG B 1 551 ? 51.294 47.888 -0.028 1.00 32.45 ? 551 ARG B NE 1 ATOM 9154 C CZ . ARG B 1 551 ? 52.000 47.868 -1.163 1.00 35.88 ? 551 ARG B CZ 1 ATOM 9155 N NH1 . ARG B 1 551 ? 52.346 49.009 -1.744 1.00 34.35 ? 551 ARG B NH1 1 ATOM 9156 N NH2 . ARG B 1 551 ? 52.335 46.709 -1.738 1.00 36.82 ? 551 ARG B NH2 1 ATOM 9157 N N . LEU B 1 552 ? 46.509 45.982 1.172 1.00 27.62 ? 552 LEU B N 1 ATOM 9158 C CA . LEU B 1 552 ? 45.978 44.620 1.028 1.00 29.01 ? 552 LEU B CA 1 ATOM 9159 C C . LEU B 1 552 ? 45.565 44.323 -0.438 1.00 24.67 ? 552 LEU B C 1 ATOM 9160 O O . LEU B 1 552 ? 45.780 43.247 -0.950 1.00 24.12 ? 552 LEU B O 1 ATOM 9161 C CB . LEU B 1 552 ? 44.766 44.445 1.956 1.00 31.35 ? 552 LEU B CB 1 ATOM 9162 C CG . LEU B 1 552 ? 44.120 43.067 1.901 1.00 32.42 ? 552 LEU B CG 1 ATOM 9163 C CD1 . LEU B 1 552 ? 44.837 42.132 2.843 1.00 31.85 ? 552 LEU B CD1 1 ATOM 9164 C CD2 . LEU B 1 552 ? 42.612 43.176 2.190 1.00 34.49 ? 552 LEU B CD2 1 ATOM 9165 N N . ILE B 1 553 ? 44.915 45.281 -1.081 1.00 28.26 ? 553 ILE B N 1 ATOM 9166 C CA . ILE B 1 553 ? 44.508 45.119 -2.489 1.00 25.58 ? 553 ILE B CA 1 ATOM 9167 C C . ILE B 1 553 ? 45.752 45.056 -3.397 1.00 29.28 ? 553 ILE B C 1 ATOM 9168 O O . ILE B 1 553 ? 45.849 44.171 -4.240 1.00 26.92 ? 553 ILE B O 1 ATOM 9169 C CB . ILE B 1 553 ? 43.622 46.283 -2.923 1.00 24.77 ? 553 ILE B CB 1 ATOM 9170 C CG1 . ILE B 1 553 ? 42.213 46.142 -2.288 1.00 23.63 ? 553 ILE B CG1 1 ATOM 9171 C CG2 . ILE B 1 553 ? 43.511 46.373 -4.455 1.00 24.89 ? 553 ILE B CG2 1 ATOM 9172 C CD1 . ILE B 1 553 ? 41.479 47.445 -2.317 1.00 24.45 ? 553 ILE B CD1 1 ATOM 9173 N N . CYS B 1 554 ? 46.716 45.988 -3.171 1.00 29.22 ? 554 CYS B N 1 ATOM 9174 C CA . CYS B 1 554 ? 47.979 46.031 -3.945 1.00 25.98 ? 554 CYS B CA 1 ATOM 9175 C C . CYS B 1 554 ? 48.652 44.717 -3.889 1.00 27.06 ? 554 CYS B C 1 ATOM 9176 O O . CYS B 1 554 ? 49.029 44.193 -4.919 1.00 27.31 ? 554 CYS B O 1 ATOM 9177 C CB . CYS B 1 554 ? 48.913 47.159 -3.495 1.00 26.47 ? 554 CYS B CB 1 ATOM 9178 S SG . CYS B 1 554 ? 48.284 48.823 -3.878 1.00 33.38 ? 554 CYS B SG 1 ATOM 9179 N N . ASP B 1 555 ? 48.727 44.121 -2.709 1.00 29.96 ? 555 ASP B N 1 ATOM 9180 C CA . ASP B 1 555 ? 49.465 42.884 -2.531 1.00 27.55 ? 555 ASP B CA 1 ATOM 9181 C C . ASP B 1 555 ? 48.748 41.661 -3.014 1.00 29.66 ? 555 ASP B C 1 ATOM 9182 O O . ASP B 1 555 ? 49.376 40.592 -3.111 1.00 26.12 ? 555 ASP B O 1 ATOM 9183 C CB . ASP B 1 555 ? 49.784 42.647 -1.045 1.00 29.92 ? 555 ASP B CB 1 ATOM 9184 C CG . ASP B 1 555 ? 50.880 43.597 -0.464 1.00 32.64 ? 555 ASP B CG 1 ATOM 9185 O OD1 . ASP B 1 555 ? 51.618 44.250 -1.230 1.00 31.15 ? 555 ASP B OD1 1 ATOM 9186 O OD2 . ASP B 1 555 ? 50.978 43.689 0.782 1.00 33.16 ? 555 ASP B OD2 1 ATOM 9187 N N . ASN B 1 556 ? 47.412 41.719 -3.190 1.00 29.85 ? 556 ASN B N 1 ATOM 9188 C CA . ASN B 1 556 ? 46.676 40.454 -3.372 1.00 28.07 ? 556 ASN B CA 1 ATOM 9189 C C . ASN B 1 556 ? 45.735 40.489 -4.579 1.00 27.06 ? 556 ASN B C 1 ATOM 9190 O O . ASN B 1 556 ? 44.883 39.625 -4.727 1.00 25.48 ? 556 ASN B O 1 ATOM 9191 C CB . ASN B 1 556 ? 45.869 40.153 -2.123 1.00 27.88 ? 556 ASN B CB 1 ATOM 9192 C CG . ASN B 1 556 ? 46.706 39.892 -0.939 1.00 29.35 ? 556 ASN B CG 1 ATOM 9193 O OD1 . ASN B 1 556 ? 47.290 38.825 -0.827 1.00 28.46 ? 556 ASN B OD1 1 ATOM 9194 N ND2 . ASN B 1 556 ? 46.707 40.826 0.008 1.00 32.34 ? 556 ASN B ND2 1 ATOM 9195 N N . THR B 1 557 ? 45.868 41.520 -5.413 1.00 27.57 ? 557 THR B N 1 ATOM 9196 C CA . THR B 1 557 ? 45.201 41.551 -6.708 1.00 24.90 ? 557 THR B CA 1 ATOM 9197 C C . THR B 1 557 ? 46.197 41.981 -7.805 1.00 29.10 ? 557 THR B C 1 ATOM 9198 O O . THR B 1 557 ? 47.402 42.069 -7.527 1.00 30.91 ? 557 THR B O 1 ATOM 9199 C CB . THR B 1 557 ? 44.061 42.524 -6.666 1.00 26.77 ? 557 THR B CB 1 ATOM 9200 O OG1 . THR B 1 557 ? 44.542 43.858 -6.563 1.00 22.96 ? 557 THR B OG1 1 ATOM 9201 C CG2 . THR B 1 557 ? 43.166 42.214 -5.444 1.00 25.42 ? 557 THR B CG2 1 ATOM 9202 N N . HIS B 1 558 ? 45.713 42.257 -9.029 1.00 27.33 ? 558 HIS B N 1 ATOM 9203 C CA . HIS B 1 558 ? 46.514 42.975 -10.045 1.00 28.59 ? 558 HIS B CA 1 ATOM 9204 C C . HIS B 1 558 ? 45.931 44.355 -10.278 1.00 31.58 ? 558 HIS B C 1 ATOM 9205 O O . HIS B 1 558 ? 46.047 44.922 -11.373 1.00 29.61 ? 558 HIS B O 1 ATOM 9206 C CB . HIS B 1 558 ? 46.607 42.213 -11.360 1.00 30.54 ? 558 HIS B CB 1 ATOM 9207 C CG . HIS B 1 558 ? 47.272 40.877 -11.245 1.00 31.18 ? 558 HIS B CG 1 ATOM 9208 N ND1 . HIS B 1 558 ? 48.486 40.689 -10.634 1.00 35.82 ? 558 HIS B ND1 1 ATOM 9209 C CD2 . HIS B 1 558 ? 46.915 39.668 -11.722 1.00 35.29 ? 558 HIS B CD2 1 ATOM 9210 C CE1 . HIS B 1 558 ? 48.831 39.412 -10.700 1.00 33.13 ? 558 HIS B CE1 1 ATOM 9211 N NE2 . HIS B 1 558 ? 47.888 38.774 -11.355 1.00 34.48 ? 558 HIS B NE2 1 ATOM 9212 N N . ILE B 1 559 ? 45.280 44.909 -9.250 1.00 31.24 ? 559 ILE B N 1 ATOM 9213 C CA . ILE B 1 559 ? 44.862 46.307 -9.286 1.00 33.27 ? 559 ILE B CA 1 ATOM 9214 C C . ILE B 1 559 ? 46.091 47.080 -8.920 1.00 33.45 ? 559 ILE B C 1 ATOM 9215 O O . ILE B 1 559 ? 46.678 46.770 -7.881 1.00 36.78 ? 559 ILE B O 1 ATOM 9216 C CB . ILE B 1 559 ? 43.815 46.633 -8.217 1.00 32.55 ? 559 ILE B CB 1 ATOM 9217 C CG1 . ILE B 1 559 ? 42.619 45.718 -8.403 1.00 37.70 ? 559 ILE B CG1 1 ATOM 9218 C CG2 . ILE B 1 559 ? 43.393 48.108 -8.267 1.00 30.29 ? 559 ILE B CG2 1 ATOM 9219 C CD1 . ILE B 1 559 ? 42.048 45.804 -9.772 1.00 37.28 ? 559 ILE B CD1 1 ATOM 9220 N N . THR B 1 560 ? 46.489 48.047 -9.757 1.00 33.44 ? 560 THR B N 1 ATOM 9221 C CA . THR B 1 560 ? 47.797 48.705 -9.614 1.00 36.93 ? 560 THR B CA 1 ATOM 9222 C C . THR B 1 560 ? 47.665 50.169 -9.210 1.00 37.57 ? 560 THR B C 1 ATOM 9223 O O . THR B 1 560 ? 48.645 50.784 -8.836 1.00 36.88 ? 560 THR B O 1 ATOM 9224 C CB . THR B 1 560 ? 48.610 48.612 -10.957 1.00 36.37 ? 560 THR B CB 1 ATOM 9225 O OG1 . THR B 1 560 ? 47.748 48.977 -12.056 1.00 40.09 ? 560 THR B OG1 1 ATOM 9226 C CG2 . THR B 1 560 ? 49.148 47.186 -11.166 1.00 33.99 ? 560 THR B CG2 1 ATOM 9227 N N . LYS B 1 561 ? 46.450 50.706 -9.329 1.00 42.41 ? 561 LYS B N 1 ATOM 9228 C CA . LYS B 1 561 ? 46.129 52.064 -8.953 1.00 42.25 ? 561 LYS B CA 1 ATOM 9229 C C . LYS B 1 561 ? 45.091 52.023 -7.826 1.00 41.50 ? 561 LYS B C 1 ATOM 9230 O O . LYS B 1 561 ? 44.063 51.369 -7.965 1.00 43.37 ? 561 LYS B O 1 ATOM 9231 C CB . LYS B 1 561 ? 45.584 52.840 -10.157 1.00 47.41 ? 561 LYS B CB 1 ATOM 9232 C CG . LYS B 1 561 ? 46.474 52.808 -11.415 1.00 52.46 ? 561 LYS B CG 1 ATOM 9233 C CD . LYS B 1 561 ? 47.877 53.354 -11.147 1.00 53.53 ? 561 LYS B CD 1 ATOM 9234 C CE . LYS B 1 561 ? 48.769 53.407 -12.390 1.00 53.57 ? 561 LYS B CE 1 ATOM 9235 N NZ . LYS B 1 561 ? 50.129 53.895 -12.013 1.00 54.41 ? 561 LYS B NZ 1 ATOM 9236 N N . VAL B 1 562 ? 45.388 52.691 -6.706 1.00 35.24 ? 562 VAL B N 1 ATOM 9237 C CA . VAL B 1 562 ? 44.530 52.676 -5.523 1.00 34.23 ? 562 VAL B CA 1 ATOM 9238 C C . VAL B 1 562 ? 44.554 54.025 -4.829 1.00 34.72 ? 562 VAL B C 1 ATOM 9239 O O . VAL B 1 562 ? 45.475 54.813 -5.055 1.00 28.80 ? 562 VAL B O 1 ATOM 9240 C CB . VAL B 1 562 ? 44.983 51.626 -4.497 1.00 33.62 ? 562 VAL B CB 1 ATOM 9241 C CG1 . VAL B 1 562 ? 44.920 50.230 -5.089 1.00 32.04 ? 562 VAL B CG1 1 ATOM 9242 C CG2 . VAL B 1 562 ? 46.384 51.893 -4.048 1.00 36.29 ? 562 VAL B CG2 1 ATOM 9243 N N . PRO B 1 563 ? 43.544 54.299 -3.970 1.00 36.04 ? 563 PRO B N 1 ATOM 9244 C CA . PRO B 1 563 ? 43.612 55.538 -3.231 1.00 36.19 ? 563 PRO B CA 1 ATOM 9245 C C . PRO B 1 563 ? 44.413 55.308 -1.982 1.00 31.67 ? 563 PRO B C 1 ATOM 9246 O O . PRO B 1 563 ? 44.740 54.170 -1.635 1.00 37.06 ? 563 PRO B O 1 ATOM 9247 C CB . PRO B 1 563 ? 42.160 55.884 -2.952 1.00 36.20 ? 563 PRO B CB 1 ATOM 9248 C CG . PRO B 1 563 ? 41.403 54.614 -3.120 1.00 39.38 ? 563 PRO B CG 1 ATOM 9249 C CD . PRO B 1 563 ? 42.316 53.548 -3.640 1.00 36.02 ? 563 PRO B CD 1 ATOM 9250 N N . LEU B 1 564 ? 44.801 56.396 -1.336 1.00 33.90 ? 564 LEU B N 1 ATOM 9251 C CA . LEU B 1 564 ? 45.396 56.259 -0.022 1.00 36.87 ? 564 LEU B CA 1 ATOM 9252 C C . LEU B 1 564 ? 44.345 55.880 1.023 1.00 32.19 ? 564 LEU B C 1 ATOM 9253 O O . LEU B 1 564 ? 44.615 55.098 1.903 1.00 34.54 ? 564 LEU B O 1 ATOM 9254 C CB . LEU B 1 564 ? 46.092 57.552 0.377 1.00 38.01 ? 564 LEU B CB 1 ATOM 9255 C CG . LEU B 1 564 ? 47.242 57.880 -0.590 1.00 41.93 ? 564 LEU B CG 1 ATOM 9256 C CD1 . LEU B 1 564 ? 47.762 59.265 -0.287 1.00 40.87 ? 564 LEU B CD1 1 ATOM 9257 C CD2 . LEU B 1 564 ? 48.344 56.818 -0.496 1.00 40.65 ? 564 LEU B CD2 1 ATOM 9258 N N . HIS B 1 565 ? 43.185 56.500 0.955 1.00 33.37 ? 565 HIS B N 1 ATOM 9259 C CA . HIS B 1 565 ? 42.175 56.341 2.013 1.00 35.54 ? 565 HIS B CA 1 ATOM 9260 C C . HIS B 1 565 ? 40.954 55.643 1.390 1.00 28.10 ? 565 HIS B C 1 ATOM 9261 O O . HIS B 1 565 ? 40.027 56.299 0.935 1.00 27.53 ? 565 HIS B O 1 ATOM 9262 C CB . HIS B 1 565 ? 41.830 57.711 2.626 1.00 39.80 ? 565 HIS B CB 1 ATOM 9263 C CG . HIS B 1 565 ? 43.041 58.497 3.014 1.00 48.14 ? 565 HIS B CG 1 ATOM 9264 N ND1 . HIS B 1 565 ? 43.950 58.048 3.956 1.00 49.48 ? 565 HIS B ND1 1 ATOM 9265 C CD2 . HIS B 1 565 ? 43.542 59.658 2.527 1.00 50.58 ? 565 HIS B CD2 1 ATOM 9266 C CE1 . HIS B 1 565 ? 44.943 58.913 4.054 1.00 51.46 ? 565 HIS B CE1 1 ATOM 9267 N NE2 . HIS B 1 565 ? 44.719 59.899 3.199 1.00 54.90 ? 565 HIS B NE2 1 ATOM 9268 N N . ALA B 1 566 ? 41.023 54.317 1.379 1.00 25.04 ? 566 ALA B N 1 ATOM 9269 C CA . ALA B 1 566 ? 40.095 53.460 0.654 1.00 25.63 ? 566 ALA B CA 1 ATOM 9270 C C . ALA B 1 566 ? 38.627 53.555 1.090 1.00 30.54 ? 566 ALA B C 1 ATOM 9271 O O . ALA B 1 566 ? 37.759 53.193 0.319 1.00 25.33 ? 566 ALA B O 1 ATOM 9272 C CB . ALA B 1 566 ? 40.568 52.032 0.679 1.00 25.25 ? 566 ALA B CB 1 ATOM 9273 N N . PHE B 1 567 ? 38.364 54.026 2.319 1.00 28.04 ? 567 PHE B N 1 ATOM 9274 C CA . PHE B 1 567 ? 36.993 54.137 2.820 1.00 26.43 ? 567 PHE B CA 1 ATOM 9275 C C . PHE B 1 567 ? 36.338 55.433 2.465 1.00 28.48 ? 567 PHE B C 1 ATOM 9276 O O . PHE B 1 567 ? 35.128 55.511 2.434 1.00 29.13 ? 567 PHE B O 1 ATOM 9277 C CB . PHE B 1 567 ? 36.955 53.986 4.326 1.00 27.70 ? 567 PHE B CB 1 ATOM 9278 C CG . PHE B 1 567 ? 37.166 52.586 4.788 1.00 30.04 ? 567 PHE B CG 1 ATOM 9279 C CD1 . PHE B 1 567 ? 36.211 51.656 4.582 1.00 31.68 ? 567 PHE B CD1 1 ATOM 9280 C CD2 . PHE B 1 567 ? 38.291 52.213 5.461 1.00 31.45 ? 567 PHE B CD2 1 ATOM 9281 C CE1 . PHE B 1 567 ? 36.376 50.345 4.995 1.00 35.37 ? 567 PHE B CE1 1 ATOM 9282 C CE2 . PHE B 1 567 ? 38.465 50.908 5.894 1.00 37.23 ? 567 PHE B CE2 1 ATOM 9283 C CZ . PHE B 1 567 ? 37.495 49.964 5.672 1.00 33.79 ? 567 PHE B CZ 1 ATOM 9284 N N . GLN B 1 568 ? 37.114 56.448 2.143 1.00 28.13 ? 568 GLN B N 1 ATOM 9285 C CA . GLN B 1 568 ? 36.515 57.650 1.671 1.00 36.39 ? 568 GLN B CA 1 ATOM 9286 C C . GLN B 1 568 ? 36.074 57.451 0.205 1.00 32.22 ? 568 GLN B C 1 ATOM 9287 O O . GLN B 1 568 ? 36.502 56.515 -0.460 1.00 33.21 ? 568 GLN B O 1 ATOM 9288 C CB . GLN B 1 568 ? 37.428 58.856 1.901 1.00 41.24 ? 568 GLN B CB 1 ATOM 9289 C CG . GLN B 1 568 ? 38.230 59.294 0.711 1.00 48.21 ? 568 GLN B CG 1 ATOM 9290 C CD . GLN B 1 568 ? 39.174 60.438 1.058 1.00 58.62 ? 568 GLN B CD 1 ATOM 9291 O OE1 . GLN B 1 568 ? 39.844 60.423 2.111 1.00 59.43 ? 568 GLN B OE1 1 ATOM 9292 N NE2 . GLN B 1 568 ? 39.245 61.433 0.167 1.00 59.01 ? 568 GLN B NE2 1 ATOM 9293 N N . ALA B 1 569 ? 35.165 58.314 -0.237 1.00 31.01 ? 569 ALA B N 1 ATOM 9294 C CA . ALA B 1 569 ? 34.774 58.402 -1.638 1.00 33.16 ? 569 ALA B CA 1 ATOM 9295 C C . ALA B 1 569 ? 35.966 58.932 -2.378 1.00 34.61 ? 569 ALA B C 1 ATOM 9296 O O . ALA B 1 569 ? 36.552 59.920 -1.960 1.00 43.55 ? 569 ALA B O 1 ATOM 9297 C CB . ALA B 1 569 ? 33.600 59.363 -1.834 1.00 33.08 ? 569 ALA B CB 1 ATOM 9298 N N . ASN B 1 570 ? 36.300 58.276 -3.467 1.00 28.95 ? 570 ASN B N 1 ATOM 9299 C CA . ASN B 1 570 ? 37.518 58.532 -4.246 1.00 31.02 ? 570 ASN B CA 1 ATOM 9300 C C . ASN B 1 570 ? 37.149 58.321 -5.691 1.00 34.90 ? 570 ASN B C 1 ATOM 9301 O O . ASN B 1 570 ? 36.583 57.284 -6.031 1.00 33.08 ? 570 ASN B O 1 ATOM 9302 C CB . ASN B 1 570 ? 38.595 57.498 -3.935 1.00 26.76 ? 570 ASN B CB 1 ATOM 9303 C CG . ASN B 1 570 ? 39.273 57.732 -2.596 1.00 32.86 ? 570 ASN B CG 1 ATOM 9304 O OD1 . ASN B 1 570 ? 39.895 58.786 -2.389 1.00 30.55 ? 570 ASN B OD1 1 ATOM 9305 N ND2 . ASN B 1 570 ? 39.234 56.725 -1.711 1.00 27.93 ? 570 ASN B ND2 1 ATOM 9306 N N . ASN B 1 571 ? 37.553 59.266 -6.534 1.00 36.57 ? 571 ASN B N 1 ATOM 9307 C CA . ASN B 1 571 ? 37.186 59.288 -7.915 1.00 37.56 ? 571 ASN B CA 1 ATOM 9308 C C . ASN B 1 571 ? 38.451 59.204 -8.743 1.00 40.97 ? 571 ASN B C 1 ATOM 9309 O O . ASN B 1 571 ? 39.425 59.876 -8.440 1.00 42.23 ? 571 ASN B O 1 ATOM 9310 C CB . ASN B 1 571 ? 36.425 60.565 -8.192 1.00 36.04 ? 571 ASN B CB 1 ATOM 9311 C CG . ASN B 1 571 ? 35.139 60.643 -7.430 1.00 31.45 ? 571 ASN B CG 1 ATOM 9312 O OD1 . ASN B 1 571 ? 34.396 59.707 -7.434 1.00 38.88 ? 571 ASN B OD1 1 ATOM 9313 N ND2 . ASN B 1 571 ? 34.826 61.787 -6.841 1.00 32.32 ? 571 ASN B ND2 1 ATOM 9314 N N . TYR B 1 572 ? 38.439 58.320 -9.749 1.00 41.22 ? 572 TYR B N 1 ATOM 9315 C CA . TYR B 1 572 ? 39.598 58.014 -10.604 1.00 37.87 ? 572 TYR B CA 1 ATOM 9316 C C . TYR B 1 572 ? 39.695 58.987 -11.757 1.00 37.05 ? 572 TYR B C 1 ATOM 9317 O O . TYR B 1 572 ? 38.666 59.411 -12.264 1.00 32.63 ? 572 TYR B O 1 ATOM 9318 C CB . TYR B 1 572 ? 39.459 56.608 -11.215 1.00 39.81 ? 572 TYR B CB 1 ATOM 9319 C CG . TYR B 1 572 ? 40.641 56.189 -12.006 1.00 38.91 ? 572 TYR B CG 1 ATOM 9320 C CD1 . TYR B 1 572 ? 41.767 55.690 -11.364 1.00 40.07 ? 572 TYR B CD1 1 ATOM 9321 C CD2 . TYR B 1 572 ? 40.656 56.279 -13.410 1.00 40.21 ? 572 TYR B CD2 1 ATOM 9322 C CE1 . TYR B 1 572 ? 42.872 55.273 -12.076 1.00 41.55 ? 572 TYR B CE1 1 ATOM 9323 C CE2 . TYR B 1 572 ? 41.786 55.862 -14.133 1.00 41.04 ? 572 TYR B CE2 1 ATOM 9324 C CZ . TYR B 1 572 ? 42.883 55.369 -13.446 1.00 41.43 ? 572 TYR B CZ 1 ATOM 9325 O OH . TYR B 1 572 ? 44.052 54.973 -14.079 1.00 44.85 ? 572 TYR B OH 1 ATOM 9326 N N . PRO B 1 573 ? 40.922 59.380 -12.171 1.00 35.60 ? 573 PRO B N 1 ATOM 9327 C CA . PRO B 1 573 ? 42.223 59.176 -11.590 1.00 37.45 ? 573 PRO B CA 1 ATOM 9328 C C . PRO B 1 573 ? 42.668 60.168 -10.502 1.00 36.78 ? 573 PRO B C 1 ATOM 9329 O O . PRO B 1 573 ? 43.686 59.907 -9.875 1.00 34.45 ? 573 PRO B O 1 ATOM 9330 C CB . PRO B 1 573 ? 43.141 59.363 -12.799 1.00 40.29 ? 573 PRO B CB 1 ATOM 9331 C CG . PRO B 1 573 ? 42.472 60.447 -13.571 1.00 34.65 ? 573 PRO B CG 1 ATOM 9332 C CD . PRO B 1 573 ? 41.014 60.155 -13.429 1.00 36.59 ? 573 PRO B CD 1 ATOM 9333 N N . HIS B 1 574 ? 41.980 61.295 -10.286 1.00 42.04 ? 574 HIS B N 1 ATOM 9334 C CA . HIS B 1 574 ? 42.566 62.342 -9.425 1.00 43.77 ? 574 HIS B CA 1 ATOM 9335 C C . HIS B 1 574 ? 42.814 61.870 -7.981 1.00 45.58 ? 574 HIS B C 1 ATOM 9336 O O . HIS B 1 574 ? 43.810 62.282 -7.385 1.00 38.11 ? 574 HIS B O 1 ATOM 9337 C CB . HIS B 1 574 ? 41.831 63.669 -9.505 1.00 45.71 ? 574 HIS B CB 1 ATOM 9338 C CG . HIS B 1 574 ? 40.353 63.554 -9.374 1.00 50.63 ? 574 HIS B CG 1 ATOM 9339 N ND1 . HIS B 1 574 ? 39.515 63.436 -10.466 1.00 54.11 ? 574 HIS B ND1 1 ATOM 9340 C CD2 . HIS B 1 574 ? 39.554 63.546 -8.281 1.00 55.81 ? 574 HIS B CD2 1 ATOM 9341 C CE1 . HIS B 1 574 ? 38.263 63.363 -10.049 1.00 53.92 ? 574 HIS B CE1 1 ATOM 9342 N NE2 . HIS B 1 574 ? 38.259 63.431 -8.727 1.00 55.16 ? 574 HIS B NE2 1 ATOM 9343 N N . ASP B 1 575 ? 42.015 60.923 -7.452 1.00 41.19 ? 575 ASP B N 1 ATOM 9344 C CA . ASP B 1 575 ? 42.265 60.396 -6.073 1.00 39.24 ? 575 ASP B CA 1 ATOM 9345 C C . ASP B 1 575 ? 43.091 59.113 -5.978 1.00 39.43 ? 575 ASP B C 1 ATOM 9346 O O . ASP B 1 575 ? 43.198 58.469 -4.910 1.00 39.25 ? 575 ASP B O 1 ATOM 9347 C CB . ASP B 1 575 ? 40.926 60.206 -5.361 1.00 39.99 ? 575 ASP B CB 1 ATOM 9348 C CG . ASP B 1 575 ? 40.206 61.502 -5.200 1.00 42.88 ? 575 ASP B CG 1 ATOM 9349 O OD1 . ASP B 1 575 ? 40.883 62.506 -4.856 1.00 45.45 ? 575 ASP B OD1 1 ATOM 9350 O OD2 . ASP B 1 575 ? 38.986 61.554 -5.425 1.00 41.49 ? 575 ASP B OD2 1 ATOM 9351 N N . PHE B 1 576 ? 43.720 58.739 -7.073 1.00 33.74 ? 576 PHE B N 1 ATOM 9352 C CA . PHE B 1 576 ? 44.289 57.406 -7.133 1.00 36.80 ? 576 PHE B CA 1 ATOM 9353 C C . PHE B 1 576 ? 45.760 57.500 -7.358 1.00 39.18 ? 576 PHE B C 1 ATOM 9354 O O . PHE B 1 576 ? 46.203 58.382 -8.079 1.00 40.25 ? 576 PHE B O 1 ATOM 9355 C CB . PHE B 1 576 ? 43.591 56.616 -8.254 1.00 37.02 ? 576 PHE B CB 1 ATOM 9356 C CG . PHE B 1 576 ? 42.274 55.989 -7.832 1.00 31.01 ? 576 PHE B CG 1 ATOM 9357 C CD1 . PHE B 1 576 ? 41.140 56.758 -7.706 1.00 31.74 ? 576 PHE B CD1 1 ATOM 9358 C CD2 . PHE B 1 576 ? 42.192 54.619 -7.555 1.00 31.38 ? 576 PHE B CD2 1 ATOM 9359 C CE1 . PHE B 1 576 ? 39.929 56.191 -7.311 1.00 32.86 ? 576 PHE B CE1 1 ATOM 9360 C CE2 . PHE B 1 576 ? 40.999 54.049 -7.168 1.00 26.90 ? 576 PHE B CE2 1 ATOM 9361 C CZ . PHE B 1 576 ? 39.864 54.823 -7.059 1.00 25.68 ? 576 PHE B CZ 1 ATOM 9362 N N . VAL B 1 577 ? 46.513 56.619 -6.732 1.00 39.56 ? 577 VAL B N 1 ATOM 9363 C CA . VAL B 1 577 ? 47.948 56.646 -6.851 1.00 40.84 ? 577 VAL B CA 1 ATOM 9364 C C . VAL B 1 577 ? 48.425 55.259 -7.133 1.00 42.22 ? 577 VAL B C 1 ATOM 9365 O O . VAL B 1 577 ? 47.718 54.307 -6.911 1.00 44.97 ? 577 VAL B O 1 ATOM 9366 C CB . VAL B 1 577 ? 48.670 57.200 -5.586 1.00 42.49 ? 577 VAL B CB 1 ATOM 9367 C CG1 . VAL B 1 577 ? 48.090 58.580 -5.226 1.00 43.19 ? 577 VAL B CG1 1 ATOM 9368 C CG2 . VAL B 1 577 ? 48.628 56.231 -4.407 1.00 40.26 ? 577 VAL B CG2 1 ATOM 9369 N N . ASP B 1 578 ? 49.652 55.170 -7.618 1.00 40.55 ? 578 ASP B N 1 ATOM 9370 C CA . ASP B 1 578 ? 50.274 53.926 -7.888 1.00 38.66 ? 578 ASP B CA 1 ATOM 9371 C C . ASP B 1 578 ? 50.578 53.242 -6.579 1.00 36.00 ? 578 ASP B C 1 ATOM 9372 O O . ASP B 1 578 ? 50.871 53.900 -5.593 1.00 34.39 ? 578 ASP B O 1 ATOM 9373 C CB . ASP B 1 578 ? 51.576 54.178 -8.674 1.00 43.32 ? 578 ASP B CB 1 ATOM 9374 C CG . ASP B 1 578 ? 52.183 52.909 -9.186 1.00 44.60 ? 578 ASP B CG 1 ATOM 9375 O OD1 . ASP B 1 578 ? 51.671 52.426 -10.225 1.00 47.08 ? 578 ASP B OD1 1 ATOM 9376 O OD2 . ASP B 1 578 ? 53.114 52.381 -8.516 1.00 44.86 ? 578 ASP B OD2 1 ATOM 9377 N N . CYS B 1 579 ? 50.544 51.917 -6.586 1.00 33.35 ? 579 CYS B N 1 ATOM 9378 C CA . CYS B 1 579 ? 50.760 51.091 -5.388 1.00 37.07 ? 579 CYS B CA 1 ATOM 9379 C C . CYS B 1 579 ? 52.126 51.229 -4.702 1.00 41.84 ? 579 CYS B C 1 ATOM 9380 O O . CYS B 1 579 ? 52.267 50.952 -3.495 1.00 40.10 ? 579 CYS B O 1 ATOM 9381 C CB . CYS B 1 579 ? 50.502 49.598 -5.711 1.00 35.55 ? 579 CYS B CB 1 ATOM 9382 S SG . CYS B 1 579 ? 48.752 49.067 -5.860 1.00 36.81 ? 579 CYS B SG 1 ATOM 9383 N N . SER B 1 580 ? 53.152 51.619 -5.446 1.00 47.86 ? 580 SER B N 1 ATOM 9384 C CA . SER B 1 580 ? 54.446 51.890 -4.824 1.00 47.25 ? 580 SER B CA 1 ATOM 9385 C C . SER B 1 580 ? 54.292 53.057 -3.819 1.00 44.55 ? 580 SER B C 1 ATOM 9386 O O . SER B 1 580 ? 55.032 53.146 -2.870 1.00 43.27 ? 580 SER B O 1 ATOM 9387 C CB . SER B 1 580 ? 55.495 52.251 -5.887 1.00 47.85 ? 580 SER B CB 1 ATOM 9388 O OG . SER B 1 580 ? 55.031 53.352 -6.660 1.00 43.63 ? 580 SER B OG 1 ATOM 9389 N N . ALA B 1 581 ? 53.315 53.931 -4.020 1.00 46.94 ? 581 ALA B N 1 ATOM 9390 C CA . ALA B 1 581 ? 53.077 55.004 -3.077 1.00 46.54 ? 581 ALA B CA 1 ATOM 9391 C C . ALA B 1 581 ? 52.391 54.578 -1.761 1.00 49.62 ? 581 ALA B C 1 ATOM 9392 O O . ALA B 1 581 ? 52.118 55.440 -0.925 1.00 49.94 ? 581 ALA B O 1 ATOM 9393 C CB . ALA B 1 581 ? 52.257 56.115 -3.728 1.00 47.58 ? 581 ALA B CB 1 ATOM 9394 N N . VAL B 1 582 ? 52.110 53.292 -1.554 1.00 48.41 ? 582 VAL B N 1 ATOM 9395 C CA . VAL B 1 582 ? 51.430 52.877 -0.320 1.00 44.14 ? 582 VAL B CA 1 ATOM 9396 C C . VAL B 1 582 ? 52.312 51.999 0.570 1.00 44.39 ? 582 VAL B C 1 ATOM 9397 O O . VAL B 1 582 ? 52.900 51.028 0.093 1.00 40.22 ? 582 VAL B O 1 ATOM 9398 C CB . VAL B 1 582 ? 50.129 52.093 -0.628 1.00 48.30 ? 582 VAL B CB 1 ATOM 9399 C CG1 . VAL B 1 582 ? 49.368 51.822 0.657 1.00 47.48 ? 582 VAL B CG1 1 ATOM 9400 C CG2 . VAL B 1 582 ? 49.231 52.850 -1.599 1.00 42.88 ? 582 VAL B CG2 1 ATOM 9401 N N . ASP B 1 583 ? 52.336 52.292 1.879 1.00 42.59 ? 583 ASP B N 1 ATOM 9402 C CA . ASP B 1 583 ? 53.208 51.588 2.825 1.00 45.12 ? 583 ASP B CA 1 ATOM 9403 C C . ASP B 1 583 ? 52.959 50.120 2.704 1.00 43.39 ? 583 ASP B C 1 ATOM 9404 O O . ASP B 1 583 ? 51.840 49.718 2.404 1.00 42.25 ? 583 ASP B O 1 ATOM 9405 C CB . ASP B 1 583 ? 52.918 51.956 4.305 1.00 51.84 ? 583 ASP B CB 1 ATOM 9406 C CG . ASP B 1 583 ? 53.191 53.425 4.653 1.00 56.99 ? 583 ASP B CG 1 ATOM 9407 O OD1 . ASP B 1 583 ? 53.327 54.288 3.758 1.00 50.76 ? 583 ASP B OD1 1 ATOM 9408 O OD2 . ASP B 1 583 ? 53.217 53.718 5.868 1.00 63.16 ? 583 ASP B OD2 1 ATOM 9409 N N . LYS B 1 584 ? 53.988 49.327 3.000 1.00 39.56 ? 584 LYS B N 1 ATOM 9410 C CA . LYS B 1 584 ? 53.865 47.896 3.132 1.00 37.72 ? 584 LYS B CA 1 ATOM 9411 C C . LYS B 1 584 ? 54.025 47.430 4.582 1.00 42.47 ? 584 LYS B C 1 ATOM 9412 O O . LYS B 1 584 ? 54.512 48.139 5.446 1.00 46.75 ? 584 LYS B O 1 ATOM 9413 C CB . LYS B 1 584 ? 54.931 47.195 2.305 1.00 42.88 ? 584 LYS B CB 1 ATOM 9414 C CG . LYS B 1 584 ? 55.115 47.730 0.892 1.00 47.31 ? 584 LYS B CG 1 ATOM 9415 C CD . LYS B 1 584 ? 56.070 46.805 0.110 1.00 52.20 ? 584 LYS B CD 1 ATOM 9416 C CE . LYS B 1 584 ? 56.208 47.114 -1.370 1.00 56.69 ? 584 LYS B CE 1 ATOM 9417 N NZ . LYS B 1 584 ? 56.544 48.545 -1.650 1.00 57.21 ? 584 LYS B NZ 1 ATOM 9418 N N . LEU B 1 585 ? 53.602 46.213 4.840 1.00 43.79 ? 585 LEU B N 1 ATOM 9419 C CA . LEU B 1 585 ? 53.842 45.593 6.104 1.00 45.20 ? 585 LEU B CA 1 ATOM 9420 C C . LEU B 1 585 ? 55.272 45.110 6.066 1.00 45.37 ? 585 LEU B C 1 ATOM 9421 O O . LEU B 1 585 ? 55.585 44.233 5.274 1.00 41.12 ? 585 LEU B O 1 ATOM 9422 C CB . LEU B 1 585 ? 52.901 44.410 6.290 1.00 42.03 ? 585 LEU B CB 1 ATOM 9423 C CG . LEU B 1 585 ? 53.142 43.560 7.537 1.00 47.84 ? 585 LEU B CG 1 ATOM 9424 C CD1 . LEU B 1 585 ? 53.091 44.422 8.783 1.00 48.88 ? 585 LEU B CD1 1 ATOM 9425 C CD2 . LEU B 1 585 ? 52.099 42.455 7.635 1.00 47.61 ? 585 LEU B CD2 1 ATOM 9426 N N . ASP B 1 586 ? 56.122 45.663 6.939 1.00 48.89 ? 586 ASP B N 1 ATOM 9427 C CA . ASP B 1 586 ? 57.512 45.225 7.068 1.00 43.09 ? 586 ASP B CA 1 ATOM 9428 C C . ASP B 1 586 ? 57.596 44.036 8.001 1.00 41.30 ? 586 ASP B C 1 ATOM 9429 O O . ASP B 1 586 ? 57.388 44.178 9.190 1.00 49.23 ? 586 ASP B O 1 ATOM 9430 C CB . ASP B 1 586 ? 58.362 46.373 7.588 1.00 47.06 ? 586 ASP B CB 1 ATOM 9431 C CG . ASP B 1 586 ? 59.824 45.957 7.944 1.00 48.16 ? 586 ASP B CG 1 ATOM 9432 O OD1 . ASP B 1 586 ? 60.233 44.768 7.786 1.00 45.97 ? 586 ASP B OD1 1 ATOM 9433 O OD2 . ASP B 1 586 ? 60.544 46.874 8.395 1.00 40.72 ? 586 ASP B OD2 1 ATOM 9434 N N . LEU B 1 587 ? 57.914 42.868 7.471 1.00 36.48 ? 587 LEU B N 1 ATOM 9435 C CA . LEU B 1 587 ? 57.948 41.676 8.287 1.00 41.71 ? 587 LEU B CA 1 ATOM 9436 C C . LEU B 1 587 ? 59.321 41.292 8.895 1.00 45.39 ? 587 LEU B C 1 ATOM 9437 O O . LEU B 1 587 ? 59.483 40.174 9.441 1.00 38.34 ? 587 LEU B O 1 ATOM 9438 C CB . LEU B 1 587 ? 57.441 40.492 7.486 1.00 37.83 ? 587 LEU B CB 1 ATOM 9439 C CG . LEU B 1 587 ? 55.998 40.560 6.953 1.00 43.08 ? 587 LEU B CG 1 ATOM 9440 C CD1 . LEU B 1 587 ? 55.707 39.382 6.032 1.00 41.84 ? 587 LEU B CD1 1 ATOM 9441 C CD2 . LEU B 1 587 ? 54.995 40.568 8.096 1.00 40.00 ? 587 LEU B CD2 1 ATOM 9442 N N . SER B 1 588 ? 60.322 42.157 8.813 1.00 49.70 ? 588 SER B N 1 ATOM 9443 C CA . SER B 1 588 ? 61.632 41.726 9.378 1.00 51.14 ? 588 SER B CA 1 ATOM 9444 C C . SER B 1 588 ? 61.491 41.359 10.858 1.00 48.68 ? 588 SER B C 1 ATOM 9445 O O . SER B 1 588 ? 62.025 40.332 11.288 1.00 47.26 ? 588 SER B O 1 ATOM 9446 C CB . SER B 1 588 ? 62.734 42.738 9.121 1.00 50.36 ? 588 SER B CB 1 ATOM 9447 O OG . SER B 1 588 ? 62.245 44.063 9.140 1.00 50.70 ? 588 SER B OG 1 ATOM 9448 N N . PRO B 1 589 ? 60.680 42.130 11.620 1.00 44.77 ? 589 PRO B N 1 ATOM 9449 C CA . PRO B 1 589 ? 60.503 41.793 13.029 1.00 38.45 ? 589 PRO B CA 1 ATOM 9450 C C . PRO B 1 589 ? 60.025 40.423 13.341 1.00 39.24 ? 589 PRO B C 1 ATOM 9451 O O . PRO B 1 589 ? 59.949 40.053 14.511 1.00 42.80 ? 589 PRO B O 1 ATOM 9452 C CB . PRO B 1 589 ? 59.496 42.806 13.488 1.00 38.91 ? 589 PRO B CB 1 ATOM 9453 C CG . PRO B 1 589 ? 59.852 44.027 12.677 1.00 41.59 ? 589 PRO B CG 1 ATOM 9454 C CD . PRO B 1 589 ? 60.213 43.497 11.334 1.00 42.85 ? 589 PRO B CD 1 ATOM 9455 N N . TRP B 1 590 ? 59.641 39.660 12.345 1.00 38.87 ? 590 TRP B N 1 ATOM 9456 C CA . TRP B 1 590 ? 59.182 38.305 12.612 1.00 42.55 ? 590 TRP B CA 1 ATOM 9457 C C . TRP B 1 590 ? 60.323 37.355 12.422 1.00 43.60 ? 590 TRP B C 1 ATOM 9458 O O . TRP B 1 590 ? 60.174 36.158 12.655 1.00 45.08 ? 590 TRP B O 1 ATOM 9459 C CB . TRP B 1 590 ? 57.968 37.957 11.700 1.00 44.32 ? 590 TRP B CB 1 ATOM 9460 C CG . TRP B 1 590 ? 56.649 38.475 12.292 1.00 39.72 ? 590 TRP B CG 1 ATOM 9461 C CD1 . TRP B 1 590 ? 55.757 37.779 13.039 1.00 36.91 ? 590 TRP B CD1 1 ATOM 9462 C CD2 . TRP B 1 590 ? 56.167 39.819 12.244 1.00 34.47 ? 590 TRP B CD2 1 ATOM 9463 N NE1 . TRP B 1 590 ? 54.721 38.604 13.418 1.00 36.15 ? 590 TRP B NE1 1 ATOM 9464 C CE2 . TRP B 1 590 ? 54.960 39.861 12.949 1.00 33.15 ? 590 TRP B CE2 1 ATOM 9465 C CE3 . TRP B 1 590 ? 56.634 40.977 11.663 1.00 35.42 ? 590 TRP B CE3 1 ATOM 9466 C CZ2 . TRP B 1 590 ? 54.225 41.023 13.090 1.00 32.46 ? 590 TRP B CZ2 1 ATOM 9467 C CZ3 . TRP B 1 590 ? 55.907 42.119 11.783 1.00 35.70 ? 590 TRP B CZ3 1 ATOM 9468 C CH2 . TRP B 1 590 ? 54.695 42.131 12.475 1.00 33.95 ? 590 TRP B CH2 1 ATOM 9469 N N . ALA B 1 591 ? 61.450 37.893 11.947 1.00 55.68 ? 591 ALA B N 1 ATOM 9470 C CA . ALA B 1 591 ? 62.675 37.108 11.743 1.00 65.09 ? 591 ALA B CA 1 ATOM 9471 C C . ALA B 1 591 ? 63.118 36.451 13.051 1.00 62.52 ? 591 ALA B C 1 ATOM 9472 O O . ALA B 1 591 ? 63.570 37.123 13.953 1.00 57.29 ? 591 ALA B O 1 ATOM 9473 C CB . ALA B 1 591 ? 63.781 38.000 11.184 1.00 67.63 ? 591 ALA B CB 1 ATOM 9474 N N . SER B 1 592 ? 62.976 35.136 13.144 1.00 71.61 ? 592 SER B N 1 ATOM 9475 C CA . SER B 1 592 ? 63.155 34.422 14.413 1.00 81.67 ? 592 SER B CA 1 ATOM 9476 C C . SER B 1 592 ? 64.598 34.207 14.832 1.00 95.31 ? 592 SER B C 1 ATOM 9477 O O . SER B 1 592 ? 64.915 34.284 16.018 1.00 109.03 ? 592 SER B O 1 ATOM 9478 C CB . SER B 1 592 ? 62.476 33.052 14.343 1.00 84.25 ? 592 SER B CB 1 ATOM 9479 O OG . SER B 1 592 ? 62.726 32.227 15.458 1.00 77.03 ? 592 SER B OG 1 ATOM 9480 N N . ARG B 1 593 ? 65.461 33.919 13.874 1.00 105.00 ? 593 ARG B N 1 ATOM 9481 C CA . ARG B 1 593 ? 66.852 33.593 14.140 1.00 105.95 ? 593 ARG B CA 1 ATOM 9482 C C . ARG B 1 593 ? 67.016 32.322 14.995 1.00 107.29 ? 593 ARG B C 1 ATOM 9483 O O . ARG B 1 593 ? 66.369 31.314 14.734 1.00 97.16 ? 593 ARG B O 1 ATOM 9484 C CB . ARG B 1 593 ? 67.565 34.812 14.738 1.00 106.49 ? 593 ARG B CB 1 ATOM 9485 C CG . ARG B 1 593 ? 67.391 36.107 13.977 1.00 102.55 ? 593 ARG B CG 1 ATOM 9486 C CD . ARG B 1 593 ? 67.606 35.863 12.497 1.00 103.12 ? 593 ARG B CD 1 ATOM 9487 N NE . ARG B 1 593 ? 67.398 37.049 11.683 1.00 108.42 ? 593 ARG B NE 1 ATOM 9488 C CZ . ARG B 1 593 ? 67.438 37.062 10.349 1.00 112.36 ? 593 ARG B CZ 1 ATOM 9489 N NH1 . ARG B 1 593 ? 67.680 35.947 9.665 1.00 111.93 ? 593 ARG B NH1 1 ATOM 9490 N NH2 . ARG B 1 593 ? 67.234 38.197 9.686 1.00 113.46 ? 593 ARG B NH2 1 ATOM 9491 N N . GLU B 1 594 ? 67.873 32.365 16.013 1.00 117.67 ? 594 GLU B N 1 ATOM 9492 C CA . GLU B 1 594 ? 68.361 31.133 16.644 1.00 129.19 ? 594 GLU B CA 1 ATOM 9493 C C . GLU B 1 594 ? 69.134 31.422 17.939 1.00 128.30 ? 594 GLU B C 1 ATOM 9494 O O . GLU B 1 594 ? 69.636 32.533 18.133 1.00 131.04 ? 594 GLU B O 1 ATOM 9495 C CB . GLU B 1 594 ? 69.272 30.384 15.655 1.00 135.13 ? 594 GLU B CB 1 ATOM 9496 C CG . GLU B 1 594 ? 69.744 29.028 16.125 1.00 140.23 ? 594 GLU B CG 1 ATOM 9497 C CD . GLU B 1 594 ? 68.592 28.092 16.423 1.00 143.02 ? 594 GLU B CD 1 ATOM 9498 O OE1 . GLU B 1 594 ? 67.491 28.279 15.852 1.00 147.09 ? 594 GLU B OE1 1 ATOM 9499 O OE2 . GLU B 1 594 ? 68.790 27.173 17.233 1.00 140.59 ? 594 GLU B OE2 1 ATOM 9500 N N . ASN B 1 595 ? 69.219 30.421 18.818 1.00 118.63 ? 595 ASN B N 1 ATOM 9501 C CA . ASN B 1 595 ? 70.076 30.501 20.005 1.00 114.09 ? 595 ASN B CA 1 ATOM 9502 C C . ASN B 1 595 ? 70.330 29.131 20.642 1.00 111.62 ? 595 ASN B C 1 ATOM 9503 O O . ASN B 1 595 ? 69.982 28.876 21.793 1.00 105.01 ? 595 ASN B O 1 ATOM 9504 C CB . ASN B 1 595 ? 69.510 31.503 21.029 1.00 111.96 ? 595 ASN B CB 1 ATOM 9505 C CG . ASN B 1 595 ? 70.598 32.264 21.740 1.00 114.18 ? 595 ASN B CG 1 ATOM 9506 O OD1 . ASN B 1 595 ? 71.658 31.708 22.035 1.00 121.21 ? 595 ASN B OD1 1 ATOM 9507 N ND2 . ASN B 1 595 ? 70.357 33.542 22.008 1.00 111.57 ? 595 ASN B ND2 1 HETATM 9508 N N1 . MMZ C 2 . ? 3.029 4.883 33.673 0.50 41.51 ? 601 MMZ A N1 1 HETATM 9509 C C1A . MMZ C 2 . ? 3.630 3.705 33.398 0.50 37.98 ? 601 MMZ A C1A 1 HETATM 9510 C C2 . MMZ C 2 . ? 3.351 5.263 34.903 0.50 35.59 ? 601 MMZ A C2 1 HETATM 9511 S S2 . MMZ C 2 . ? 2.873 6.644 35.688 0.50 35.24 ? 601 MMZ A S2 1 HETATM 9512 N N3 . MMZ C 2 . ? 4.140 4.304 35.354 0.50 34.86 ? 601 MMZ A N3 1 HETATM 9513 C C3A . MMZ C 2 . ? 4.322 3.342 34.496 0.50 35.47 ? 601 MMZ A C3A 1 HETATM 9514 C C4 . MMZ C 2 . ? 4.781 4.306 36.634 0.50 35.89 ? 601 MMZ A C4 1 HETATM 9515 N N1 . MMZ D 2 . ? 3.033 4.647 33.623 0.50 31.49 ? 602 MMZ A N1 1 HETATM 9516 C C1A . MMZ D 2 . ? 2.970 5.853 34.244 0.50 30.55 ? 602 MMZ A C1A 1 HETATM 9517 C C2 . MMZ D 2 . ? 3.718 3.773 34.338 0.50 28.45 ? 602 MMZ A C2 1 HETATM 9518 S S2 . MMZ D 2 . ? 4.098 2.165 34.066 0.50 31.00 ? 602 MMZ A S2 1 HETATM 9519 N N3 . MMZ D 2 . ? 4.088 4.449 35.383 0.50 29.69 ? 602 MMZ A N3 1 HETATM 9520 C C3A . MMZ D 2 . ? 3.681 5.718 35.387 0.50 29.84 ? 602 MMZ A C3A 1 HETATM 9521 C C4 . MMZ D 2 . ? 4.904 3.780 36.356 0.50 29.77 ? 602 MMZ A C4 1 HETATM 9522 C C1 . NAG E 3 . ? 3.870 10.859 57.172 1.00 33.74 ? 603 NAG A C1 1 HETATM 9523 C C2 . NAG E 3 . ? 3.560 9.645 58.059 1.00 36.78 ? 603 NAG A C2 1 HETATM 9524 C C3 . NAG E 3 . ? 4.195 9.638 59.471 1.00 41.30 ? 603 NAG A C3 1 HETATM 9525 C C4 . NAG E 3 . ? 5.669 10.078 59.380 1.00 40.87 ? 603 NAG A C4 1 HETATM 9526 C C5 . NAG E 3 . ? 5.595 11.391 58.592 1.00 43.19 ? 603 NAG A C5 1 HETATM 9527 C C6 . NAG E 3 . ? 6.832 12.275 58.572 1.00 43.16 ? 603 NAG A C6 1 HETATM 9528 C C7 . NAG E 3 . ? 1.471 8.909 57.139 1.00 31.35 ? 603 NAG A C7 1 HETATM 9529 C C8 . NAG E 3 . ? -0.001 8.860 57.407 1.00 31.12 ? 603 NAG A C8 1 HETATM 9530 N N2 . NAG E 3 . ? 2.143 9.501 58.109 1.00 30.72 ? 603 NAG A N2 1 HETATM 9531 O O3 . NAG E 3 . ? 4.032 8.346 60.019 1.00 38.61 ? 603 NAG A O3 1 HETATM 9532 O O4 . NAG E 3 . ? 6.291 10.281 60.628 1.00 43.72 ? 603 NAG A O4 1 HETATM 9533 O O5 . NAG E 3 . ? 5.231 11.011 57.271 1.00 34.37 ? 603 NAG A O5 1 HETATM 9534 O O6 . NAG E 3 . ? 7.761 11.717 57.689 1.00 49.26 ? 603 NAG A O6 1 HETATM 9535 O O7 . NAG E 3 . ? 1.976 8.411 56.106 1.00 27.34 ? 603 NAG A O7 1 HETATM 9536 C C1 . NAG F 3 . ? 14.008 -21.035 36.640 1.00 61.54 ? 604 NAG A C1 1 HETATM 9537 C C2 . NAG F 3 . ? 14.493 -22.494 36.592 1.00 62.46 ? 604 NAG A C2 1 HETATM 9538 C C3 . NAG F 3 . ? 16.023 -22.406 36.388 1.00 60.37 ? 604 NAG A C3 1 HETATM 9539 C C4 . NAG F 3 . ? 16.228 -21.861 34.982 1.00 58.10 ? 604 NAG A C4 1 HETATM 9540 C C5 . NAG F 3 . ? 15.606 -20.456 35.000 1.00 61.43 ? 604 NAG A C5 1 HETATM 9541 C C6 . NAG F 3 . ? 15.748 -19.709 33.684 1.00 59.63 ? 604 NAG A C6 1 HETATM 9542 C C7 . NAG F 3 . ? 12.808 -23.889 37.778 1.00 58.37 ? 604 NAG A C7 1 HETATM 9543 C C8 . NAG F 3 . ? 12.467 -24.845 38.891 1.00 53.93 ? 604 NAG A C8 1 HETATM 9544 N N2 . NAG F 3 . ? 14.061 -23.398 37.669 1.00 60.52 ? 604 NAG A N2 1 HETATM 9545 O O3 . NAG F 3 . ? 16.737 -23.605 36.549 1.00 59.74 ? 604 NAG A O3 1 HETATM 9546 O O4 . NAG F 3 . ? 17.600 -21.842 34.655 1.00 59.07 ? 604 NAG A O4 1 HETATM 9547 O O5 . NAG F 3 . ? 14.234 -20.482 35.360 1.00 62.98 ? 604 NAG A O5 1 HETATM 9548 O O6 . NAG F 3 . ? 16.487 -18.588 34.079 1.00 56.25 ? 604 NAG A O6 1 HETATM 9549 O O7 . NAG F 3 . ? 11.902 -23.563 37.039 1.00 57.73 ? 604 NAG A O7 1 HETATM 9550 C C1 . NAG G 3 . ? 17.056 -5.181 6.168 1.00 57.05 ? 605 NAG A C1 1 HETATM 9551 C C2 . NAG G 3 . ? 17.551 -6.414 5.429 1.00 64.75 ? 605 NAG A C2 1 HETATM 9552 C C3 . NAG G 3 . ? 16.628 -6.897 4.306 1.00 61.85 ? 605 NAG A C3 1 HETATM 9553 C C4 . NAG G 3 . ? 15.143 -6.961 4.658 1.00 60.66 ? 605 NAG A C4 1 HETATM 9554 C C5 . NAG G 3 . ? 14.696 -5.679 5.389 1.00 58.21 ? 605 NAG A C5 1 HETATM 9555 C C6 . NAG G 3 . ? 13.285 -5.840 6.005 1.00 56.20 ? 605 NAG A C6 1 HETATM 9556 C C7 . NAG G 3 . ? 19.956 -6.900 5.311 1.00 65.73 ? 605 NAG A C7 1 HETATM 9557 C C8 . NAG G 3 . ? 21.303 -6.507 4.756 1.00 62.27 ? 605 NAG A C8 1 HETATM 9558 N N2 . NAG G 3 . ? 18.917 -6.141 4.954 1.00 65.56 ? 605 NAG A N2 1 HETATM 9559 O O3 . NAG G 3 . ? 16.995 -8.226 4.102 1.00 58.58 ? 605 NAG A O3 1 HETATM 9560 O O4 . NAG G 3 . ? 14.381 -7.301 3.484 1.00 64.33 ? 605 NAG A O4 1 HETATM 9561 O O5 . NAG G 3 . ? 15.634 -5.203 6.382 1.00 59.60 ? 605 NAG A O5 1 HETATM 9562 O O6 . NAG G 3 . ? 13.197 -6.683 7.150 1.00 54.26 ? 605 NAG A O6 1 HETATM 9563 O O7 . NAG G 3 . ? 19.830 -7.891 6.043 1.00 65.35 ? 605 NAG A O7 1 HETATM 9564 C C1 . NAG H 3 . ? 28.297 19.214 41.169 1.00 33.63 ? 606 NAG A C1 1 HETATM 9565 C C2 . NAG H 3 . ? 27.425 18.942 42.389 1.00 32.08 ? 606 NAG A C2 1 HETATM 9566 C C3 . NAG H 3 . ? 28.075 19.410 43.683 1.00 32.85 ? 606 NAG A C3 1 HETATM 9567 C C4 . NAG H 3 . ? 29.477 18.850 43.910 1.00 40.00 ? 606 NAG A C4 1 HETATM 9568 C C5 . NAG H 3 . ? 30.270 19.112 42.627 1.00 40.46 ? 606 NAG A C5 1 HETATM 9569 C C6 . NAG H 3 . ? 31.633 18.419 42.597 1.00 38.67 ? 606 NAG A C6 1 HETATM 9570 C C7 . NAG H 3 . ? 25.005 18.748 42.007 1.00 32.05 ? 606 NAG A C7 1 HETATM 9571 C C8 . NAG H 3 . ? 23.699 19.437 41.799 1.00 31.18 ? 606 NAG A C8 1 HETATM 9572 N N2 . NAG H 3 . ? 26.095 19.532 42.186 1.00 32.00 ? 606 NAG A N2 1 HETATM 9573 O O3 . NAG H 3 . ? 27.232 19.128 44.750 1.00 30.85 ? 606 NAG A O3 1 HETATM 9574 O O4 . NAG H 3 . ? 30.122 19.472 45.040 1.00 39.94 ? 606 NAG A O4 1 HETATM 9575 O O5 . NAG H 3 . ? 29.580 18.744 41.428 1.00 36.56 ? 606 NAG A O5 1 HETATM 9576 O O6 . NAG H 3 . ? 32.248 18.842 41.397 1.00 45.03 ? 606 NAG A O6 1 HETATM 9577 O O7 . NAG H 3 . ? 25.018 17.502 41.955 1.00 27.18 ? 606 NAG A O7 1 HETATM 9578 C CHA . HEM I 4 . ? 1.361 2.347 31.656 1.00 16.28 ? 607 HEM A CHA 1 HETATM 9579 C CHB . HEM I 4 . ? 1.294 2.087 36.396 1.00 16.46 ? 607 HEM A CHB 1 HETATM 9580 C CHC . HEM I 4 . ? 4.210 -1.749 36.196 1.00 16.03 ? 607 HEM A CHC 1 HETATM 9581 C CHD . HEM I 4 . ? 4.471 -1.307 31.456 1.00 16.29 ? 607 HEM A CHD 1 HETATM 9582 C C1A . HEM I 4 . ? 1.020 2.540 32.957 1.00 15.80 ? 607 HEM A C1A 1 HETATM 9583 C C2A . HEM I 4 . ? 0.221 3.619 33.378 1.00 16.42 ? 607 HEM A C2A 1 HETATM 9584 C C3A . HEM I 4 . ? 0.217 3.596 34.745 1.00 16.90 ? 607 HEM A C3A 1 HETATM 9585 C C4A . HEM I 4 . ? 0.968 2.455 35.135 1.00 17.43 ? 607 HEM A C4A 1 HETATM 9586 C CMA . HEM I 4 . ? -0.631 4.548 35.605 1.00 17.83 ? 607 HEM A CMA 1 HETATM 9587 C CAA . HEM I 4 . ? -0.546 4.633 32.513 1.00 16.00 ? 607 HEM A CAA 1 HETATM 9588 C CBA . HEM I 4 . ? -1.861 3.982 32.109 1.00 15.50 ? 607 HEM A CBA 1 HETATM 9589 C CGA . HEM I 4 . ? -2.680 4.800 31.116 1.00 16.69 ? 607 HEM A CGA 1 HETATM 9590 O O1A . HEM I 4 . ? -3.103 5.968 31.400 1.00 16.73 ? 607 HEM A O1A 1 HETATM 9591 O O2A . HEM I 4 . ? -2.938 4.333 29.968 1.00 15.28 ? 607 HEM A O2A 1 HETATM 9592 C C1B . HEM I 4 . ? 2.165 1.079 36.746 1.00 16.23 ? 607 HEM A C1B 1 HETATM 9593 C C2B . HEM I 4 . ? 2.477 0.726 38.097 1.00 16.44 ? 607 HEM A C2B 1 HETATM 9594 C C3B . HEM I 4 . ? 3.279 -0.375 38.085 1.00 16.31 ? 607 HEM A C3B 1 HETATM 9595 C C4B . HEM I 4 . ? 3.431 -0.710 36.663 1.00 16.64 ? 607 HEM A C4B 1 HETATM 9596 C CMB . HEM I 4 . ? 1.957 1.409 39.288 1.00 14.77 ? 607 HEM A CMB 1 HETATM 9597 C CAB . HEM I 4 . ? 3.882 -1.144 39.181 1.00 16.27 ? 607 HEM A CAB 1 HETATM 9598 C CBB . HEM I 4 . ? 3.562 -0.997 40.455 1.00 15.42 ? 607 HEM A CBB 1 HETATM 9599 C C1C . HEM I 4 . ? 4.533 -2.021 34.906 1.00 16.01 ? 607 HEM A C1C 1 HETATM 9600 C C2C . HEM I 4 . ? 5.333 -3.046 34.444 1.00 16.28 ? 607 HEM A C2C 1 HETATM 9601 C C3C . HEM I 4 . ? 5.392 -2.916 33.072 1.00 15.36 ? 607 HEM A C3C 1 HETATM 9602 C C4C . HEM I 4 . ? 4.659 -1.770 32.734 1.00 15.88 ? 607 HEM A C4C 1 HETATM 9603 C CMC . HEM I 4 . ? 6.002 -4.086 35.313 1.00 15.36 ? 607 HEM A CMC 1 HETATM 9604 C CAC . HEM I 4 . ? 6.129 -3.756 32.145 1.00 15.63 ? 607 HEM A CAC 1 HETATM 9605 C CBC . HEM I 4 . ? 6.830 -4.873 32.463 1.00 15.72 ? 607 HEM A CBC 1 HETATM 9606 C C1D . HEM I 4 . ? 3.673 -0.203 31.164 1.00 16.76 ? 607 HEM A C1D 1 HETATM 9607 C C2D . HEM I 4 . ? 3.636 0.356 29.805 1.00 16.25 ? 607 HEM A C2D 1 HETATM 9608 C C3D . HEM I 4 . ? 2.780 1.347 29.852 1.00 15.05 ? 607 HEM A C3D 1 HETATM 9609 C C4D . HEM I 4 . ? 2.316 1.423 31.243 1.00 14.82 ? 607 HEM A C4D 1 HETATM 9610 C CMD . HEM I 4 . ? 4.280 -0.103 28.525 1.00 15.49 ? 607 HEM A CMD 1 HETATM 9611 C CAD . HEM I 4 . ? 2.426 2.195 28.651 1.00 14.70 ? 607 HEM A CAD 1 HETATM 9612 C CBD . HEM I 4 . ? 3.404 3.354 28.611 1.00 15.21 ? 607 HEM A CBD 1 HETATM 9613 C CGD . HEM I 4 . ? 3.194 4.349 27.457 1.00 17.34 ? 607 HEM A CGD 1 HETATM 9614 O O1D . HEM I 4 . ? 3.689 4.105 26.292 1.00 19.80 ? 607 HEM A O1D 1 HETATM 9615 O O2D . HEM I 4 . ? 2.590 5.418 27.672 1.00 17.33 ? 607 HEM A O2D 1 HETATM 9616 N NA . HEM I 4 . ? 1.449 1.794 34.053 1.00 17.56 ? 607 HEM A NA 1 HETATM 9617 N NB . HEM I 4 . ? 2.683 0.130 35.989 1.00 18.14 ? 607 HEM A NB 1 HETATM 9618 N NC . HEM I 4 . ? 4.034 -1.322 33.881 1.00 16.54 ? 607 HEM A NC 1 HETATM 9619 N ND . HEM I 4 . ? 2.782 0.418 31.971 1.00 18.23 ? 607 HEM A ND 1 HETATM 9620 FE FE . HEM I 4 . ? 2.663 0.228 33.917 1.00 16.54 ? 607 HEM A FE 1 HETATM 9621 CA CA . CA J 5 . ? 14.750 5.335 24.885 1.00 19.07 ? 608 CA A CA 1 HETATM 9622 N N . NO3 K 6 . ? -0.497 -0.570 15.852 1.00 18.84 ? 609 NO3 A N 1 HETATM 9623 O O1 . NO3 K 6 . ? 0.674 -0.659 15.955 1.00 18.84 ? 609 NO3 A O1 1 HETATM 9624 O O2 . NO3 K 6 . ? -1.114 -0.733 14.667 1.00 19.03 ? 609 NO3 A O2 1 HETATM 9625 O O3 . NO3 K 6 . ? -1.326 -0.371 16.939 1.00 22.89 ? 609 NO3 A O3 1 HETATM 9626 N N . NO3 L 6 . ? -1.022 13.583 55.080 1.00 51.18 ? 610 NO3 A N 1 HETATM 9627 O O1 . NO3 L 6 . ? -0.978 14.385 54.170 1.00 51.75 ? 610 NO3 A O1 1 HETATM 9628 O O2 . NO3 L 6 . ? -1.739 12.421 54.830 1.00 52.69 ? 610 NO3 A O2 1 HETATM 9629 O O3 . NO3 L 6 . ? -0.373 13.779 56.335 1.00 54.83 ? 610 NO3 A O3 1 HETATM 9630 N N . NO3 M 6 . ? 7.381 -13.010 48.525 1.00 40.63 ? 611 NO3 A N 1 HETATM 9631 O O1 . NO3 M 6 . ? 8.083 -13.263 47.550 1.00 36.79 ? 611 NO3 A O1 1 HETATM 9632 O O2 . NO3 M 6 . ? 7.461 -13.883 49.619 1.00 44.71 ? 611 NO3 A O2 1 HETATM 9633 O O3 . NO3 M 6 . ? 6.476 -11.914 48.605 1.00 36.62 ? 611 NO3 A O3 1 HETATM 9634 N N . NO3 N 6 . ? 23.114 -8.844 24.661 1.00 45.47 ? 612 NO3 A N 1 HETATM 9635 O O1 . NO3 N 6 . ? 22.931 -10.043 24.441 1.00 47.20 ? 612 NO3 A O1 1 HETATM 9636 O O2 . NO3 N 6 . ? 22.829 -7.826 23.756 1.00 40.49 ? 612 NO3 A O2 1 HETATM 9637 O O3 . NO3 N 6 . ? 23.662 -8.481 25.877 1.00 53.54 ? 612 NO3 A O3 1 HETATM 9638 N N . NO3 O 6 . ? -5.346 -20.340 40.902 1.00 72.18 ? 613 NO3 A N 1 HETATM 9639 O O1 . NO3 O 6 . ? -5.319 -20.933 41.975 1.00 70.84 ? 613 NO3 A O1 1 HETATM 9640 O O2 . NO3 O 6 . ? -6.065 -20.844 39.791 1.00 65.39 ? 613 NO3 A O2 1 HETATM 9641 O O3 . NO3 O 6 . ? -4.652 -19.130 40.784 1.00 74.38 ? 613 NO3 A O3 1 HETATM 9642 C C1 . GOL P 7 . ? -18.960 1.448 19.601 1.00 30.01 ? 614 GOL A C1 1 HETATM 9643 O O1 . GOL P 7 . ? -18.422 2.737 19.352 1.00 25.62 ? 614 GOL A O1 1 HETATM 9644 C C2 . GOL P 7 . ? -20.045 1.444 20.698 1.00 30.69 ? 614 GOL A C2 1 HETATM 9645 O O2 . GOL P 7 . ? -20.048 2.528 21.671 1.00 31.53 ? 614 GOL A O2 1 HETATM 9646 C C3 . GOL P 7 . ? -19.734 0.152 21.404 1.00 29.62 ? 614 GOL A C3 1 HETATM 9647 O O3 . GOL P 7 . ? -20.658 -0.006 22.460 1.00 32.67 ? 614 GOL A O3 1 HETATM 9648 C C1 . GOL Q 7 . ? -19.054 1.653 13.755 1.00 39.58 ? 615 GOL A C1 1 HETATM 9649 O O1 . GOL Q 7 . ? -19.629 2.948 13.779 1.00 40.51 ? 615 GOL A O1 1 HETATM 9650 C C2 . GOL Q 7 . ? -20.152 0.767 13.169 1.00 42.80 ? 615 GOL A C2 1 HETATM 9651 O O2 . GOL Q 7 . ? -19.810 0.603 11.780 1.00 47.76 ? 615 GOL A O2 1 HETATM 9652 C C3 . GOL Q 7 . ? -21.575 1.316 13.169 1.00 39.58 ? 615 GOL A C3 1 HETATM 9653 O O3 . GOL Q 7 . ? -22.258 1.381 14.406 1.00 35.15 ? 615 GOL A O3 1 HETATM 9654 C C1 . GOL R 7 . ? -13.891 14.508 20.630 1.00 31.12 ? 616 GOL A C1 1 HETATM 9655 O O1 . GOL R 7 . ? -12.739 14.597 19.835 1.00 38.20 ? 616 GOL A O1 1 HETATM 9656 C C2 . GOL R 7 . ? -13.764 13.148 21.264 1.00 26.16 ? 616 GOL A C2 1 HETATM 9657 O O2 . GOL R 7 . ? -12.461 12.930 21.803 1.00 22.37 ? 616 GOL A O2 1 HETATM 9658 C C3 . GOL R 7 . ? -14.088 12.077 20.261 1.00 24.85 ? 616 GOL A C3 1 HETATM 9659 O O3 . GOL R 7 . ? -13.032 11.953 19.261 1.00 24.26 ? 616 GOL A O3 1 HETATM 9660 C C1 . GOL S 7 . ? -7.303 8.519 35.123 1.00 47.29 ? 617 GOL A C1 1 HETATM 9661 O O1 . GOL S 7 . ? -7.584 7.258 34.560 1.00 45.80 ? 617 GOL A O1 1 HETATM 9662 C C2 . GOL S 7 . ? -6.343 9.305 34.220 1.00 51.83 ? 617 GOL A C2 1 HETATM 9663 O O2 . GOL S 7 . ? -6.643 9.314 32.751 1.00 36.58 ? 617 GOL A O2 1 HETATM 9664 C C3 . GOL S 7 . ? -6.435 10.686 34.884 1.00 54.60 ? 617 GOL A C3 1 HETATM 9665 O O3 . GOL S 7 . ? -5.318 11.550 34.576 1.00 58.74 ? 617 GOL A O3 1 HETATM 9666 N N1 . MMZ T 2 . ? 23.986 37.419 6.965 0.50 30.62 ? 601 MMZ B N1 1 HETATM 9667 C C1A . MMZ T 2 . ? 23.816 36.213 6.360 0.50 31.24 ? 601 MMZ B C1A 1 HETATM 9668 C C2 . MMZ T 2 . ? 24.717 38.214 6.190 0.50 28.18 ? 601 MMZ B C2 1 HETATM 9669 S S2 . MMZ T 2 . ? 25.234 39.797 6.324 0.50 27.72 ? 601 MMZ B S2 1 HETATM 9670 N N3 . MMZ T 2 . ? 24.975 37.511 5.149 0.50 27.47 ? 601 MMZ B N3 1 HETATM 9671 C C3A . MMZ T 2 . ? 24.475 36.286 5.182 0.50 28.87 ? 601 MMZ B C3A 1 HETATM 9672 C C4 . MMZ T 2 . ? 25.780 38.163 4.160 0.50 29.20 ? 601 MMZ B C4 1 HETATM 9673 C C1 . NAG U 3 . ? 34.793 62.925 4.342 1.00 61.58 ? 602 NAG B C1 1 HETATM 9674 C C2 . NAG U 3 . ? 35.297 64.385 4.361 1.00 59.26 ? 602 NAG B C2 1 HETATM 9675 C C3 . NAG U 3 . ? 36.424 64.650 5.402 1.00 60.45 ? 602 NAG B C3 1 HETATM 9676 C C4 . NAG U 3 . ? 36.880 63.482 6.290 1.00 64.16 ? 602 NAG B C4 1 HETATM 9677 C C5 . NAG U 3 . ? 36.399 62.152 5.766 1.00 65.15 ? 602 NAG B C5 1 HETATM 9678 C C6 . NAG U 3 . ? 36.577 61.054 6.791 1.00 68.98 ? 602 NAG B C6 1 HETATM 9679 C C7 . NAG U 3 . ? 34.735 65.296 2.093 1.00 48.20 ? 602 NAG B C7 1 HETATM 9680 C C8 . NAG U 3 . ? 35.144 65.395 0.643 1.00 47.14 ? 602 NAG B C8 1 HETATM 9681 N N2 . NAG U 3 . ? 35.567 64.632 2.934 1.00 52.60 ? 602 NAG B N2 1 HETATM 9682 O O3 . NAG U 3 . ? 35.870 65.509 6.374 1.00 60.74 ? 602 NAG B O3 1 HETATM 9683 O O4 . NAG U 3 . ? 38.287 63.456 6.539 1.00 65.74 ? 602 NAG B O4 1 HETATM 9684 O O5 . NAG U 3 . ? 35.009 62.286 5.560 1.00 64.72 ? 602 NAG B O5 1 HETATM 9685 O O6 . NAG U 3 . ? 37.110 59.976 6.069 1.00 73.40 ? 602 NAG B O6 1 HETATM 9686 O O7 . NAG U 3 . ? 33.684 65.866 2.429 1.00 51.53 ? 602 NAG B O7 1 HETATM 9687 C C1 . NAG V 3 . ? 24.726 31.034 -16.524 1.00 30.10 ? 603 NAG B C1 1 HETATM 9688 C C2 . NAG V 3 . ? 24.345 32.229 -17.357 1.00 29.94 ? 603 NAG B C2 1 HETATM 9689 C C3 . NAG V 3 . ? 25.005 32.254 -18.746 1.00 34.83 ? 603 NAG B C3 1 HETATM 9690 C C4 . NAG V 3 . ? 26.481 31.849 -18.741 1.00 39.14 ? 603 NAG B C4 1 HETATM 9691 C C5 . NAG V 3 . ? 26.648 30.607 -17.866 1.00 38.26 ? 603 NAG B C5 1 HETATM 9692 C C6 . NAG V 3 . ? 28.110 30.121 -17.768 1.00 40.91 ? 603 NAG B C6 1 HETATM 9693 C C7 . NAG V 3 . ? 22.230 33.021 -16.511 1.00 26.17 ? 603 NAG B C7 1 HETATM 9694 C C8 . NAG V 3 . ? 20.730 33.162 -16.752 1.00 26.23 ? 603 NAG B C8 1 HETATM 9695 N N2 . NAG V 3 . ? 22.906 32.362 -17.445 1.00 27.12 ? 603 NAG B N2 1 HETATM 9696 O O3 . NAG V 3 . ? 24.950 33.517 -19.356 1.00 31.59 ? 603 NAG B O3 1 HETATM 9697 O O4 . NAG V 3 . ? 26.781 31.534 -20.093 1.00 48.03 ? 603 NAG B O4 1 HETATM 9698 O O5 . NAG V 3 . ? 26.142 30.962 -16.590 1.00 32.33 ? 603 NAG B O5 1 HETATM 9699 O O6 . NAG V 3 . ? 28.947 31.246 -17.461 1.00 41.23 ? 603 NAG B O6 1 HETATM 9700 O O7 . NAG V 3 . ? 22.783 33.557 -15.542 1.00 22.38 ? 603 NAG B O7 1 HETATM 9701 C C1 . NAG W 3 . ? 37.925 46.801 34.578 1.00 60.11 ? 604 NAG B C1 1 HETATM 9702 C C2 . NAG W 3 . ? 38.322 48.147 35.180 1.00 66.14 ? 604 NAG B C2 1 HETATM 9703 C C3 . NAG W 3 . ? 37.464 48.466 36.397 1.00 68.93 ? 604 NAG B C3 1 HETATM 9704 C C4 . NAG W 3 . ? 35.974 48.473 36.043 1.00 69.80 ? 604 NAG B C4 1 HETATM 9705 C C5 . NAG W 3 . ? 35.558 47.239 35.207 1.00 65.25 ? 604 NAG B C5 1 HETATM 9706 C C6 . NAG W 3 . ? 34.165 47.361 34.541 1.00 60.68 ? 604 NAG B C6 1 HETATM 9707 C C7 . NAG W 3 . ? 40.669 48.841 34.951 1.00 67.36 ? 604 NAG B C7 1 HETATM 9708 C C8 . NAG W 3 . ? 42.081 48.609 35.424 1.00 67.74 ? 604 NAG B C8 1 HETATM 9709 N N2 . NAG W 3 . ? 39.735 48.073 35.515 1.00 67.32 ? 604 NAG B N2 1 HETATM 9710 O O3 . NAG W 3 . ? 37.829 49.722 36.925 1.00 68.36 ? 604 NAG B O3 1 HETATM 9711 O O4 . NAG W 3 . ? 35.253 48.572 37.264 1.00 72.66 ? 604 NAG B O4 1 HETATM 9712 O O5 . NAG W 3 . ? 36.533 46.829 34.231 1.00 66.48 ? 604 NAG B O5 1 HETATM 9713 O O6 . NAG W 3 . ? 34.103 48.259 33.437 1.00 57.96 ? 604 NAG B O6 1 HETATM 9714 O O7 . NAG W 3 . ? 40.425 49.703 34.096 1.00 67.01 ? 604 NAG B O7 1 HETATM 9715 C C1 . NAG X 3 . ? 49.123 22.824 -0.917 1.00 55.14 ? 605 NAG B C1 1 HETATM 9716 C C2 . NAG X 3 . ? 48.240 23.103 -2.140 1.00 52.24 ? 605 NAG B C2 1 HETATM 9717 C C3 . NAG X 3 . ? 48.973 22.720 -3.434 1.00 53.06 ? 605 NAG B C3 1 HETATM 9718 C C4 . NAG X 3 . ? 50.341 23.412 -3.578 1.00 56.13 ? 605 NAG B C4 1 HETATM 9719 C C5 . NAG X 3 . ? 51.180 23.191 -2.327 1.00 55.50 ? 605 NAG B C5 1 HETATM 9720 C C6 . NAG X 3 . ? 52.338 24.204 -2.405 1.00 53.03 ? 605 NAG B C6 1 HETATM 9721 C C7 . NAG X 3 . ? 45.792 22.940 -1.571 1.00 55.59 ? 605 NAG B C7 1 HETATM 9722 C C8 . NAG X 3 . ? 44.570 22.073 -1.471 1.00 54.96 ? 605 NAG B C8 1 HETATM 9723 N N2 . NAG X 3 . ? 46.969 22.388 -1.995 1.00 56.73 ? 605 NAG B N2 1 HETATM 9724 O O3 . NAG X 3 . ? 48.195 23.038 -4.563 1.00 47.05 ? 605 NAG B O3 1 HETATM 9725 O O4 . NAG X 3 . ? 51.091 22.871 -4.660 1.00 54.09 ? 605 NAG B O4 1 HETATM 9726 O O5 . NAG X 3 . ? 50.446 23.323 -1.104 1.00 56.72 ? 605 NAG B O5 1 HETATM 9727 O O6 . NAG X 3 . ? 53.102 24.287 -1.222 1.00 48.31 ? 605 NAG B O6 1 HETATM 9728 O O7 . NAG X 3 . ? 45.626 24.104 -1.255 1.00 41.94 ? 605 NAG B O7 1 HETATM 9729 C C1 . NAG Y 3 . ? 51.594 23.835 -5.599 1.00 55.63 ? 606 NAG B C1 1 HETATM 9730 C C2 . NAG Y 3 . ? 52.564 23.106 -6.546 1.00 55.90 ? 606 NAG B C2 1 HETATM 9731 C C3 . NAG Y 3 . ? 52.952 23.897 -7.790 1.00 64.82 ? 606 NAG B C3 1 HETATM 9732 C C4 . NAG Y 3 . ? 51.747 24.605 -8.397 1.00 65.70 ? 606 NAG B C4 1 HETATM 9733 C C5 . NAG Y 3 . ? 51.028 25.371 -7.267 1.00 67.04 ? 606 NAG B C5 1 HETATM 9734 C C6 . NAG Y 3 . ? 49.855 26.256 -7.736 1.00 66.48 ? 606 NAG B C6 1 HETATM 9735 C C7 . NAG Y 3 . ? 53.928 21.741 -5.107 1.00 52.39 ? 606 NAG B C7 1 HETATM 9736 C C8 . NAG Y 3 . ? 55.087 21.669 -4.161 1.00 57.34 ? 606 NAG B C8 1 HETATM 9737 N N2 . NAG Y 3 . ? 53.687 22.909 -5.683 1.00 49.76 ? 606 NAG B N2 1 HETATM 9738 O O3 . NAG Y 3 . ? 53.485 23.044 -8.787 1.00 66.07 ? 606 NAG B O3 1 HETATM 9739 O O4 . NAG Y 3 . ? 52.198 25.416 -9.480 1.00 66.22 ? 606 NAG B O4 1 HETATM 9740 O O5 . NAG Y 3 . ? 50.562 24.448 -6.296 1.00 56.19 ? 606 NAG B O5 1 HETATM 9741 O O6 . NAG Y 3 . ? 49.027 25.588 -8.663 1.00 57.08 ? 606 NAG B O6 1 HETATM 9742 O O7 . NAG Y 3 . ? 53.260 20.739 -5.323 1.00 52.39 ? 606 NAG B O7 1 HETATM 9743 C CHA . HEM Z 4 . ? 22.160 39.574 9.186 1.00 14.89 ? 607 HEM B CHA 1 HETATM 9744 C CHB . HEM Z 4 . ? 22.043 39.841 4.364 1.00 14.72 ? 607 HEM B CHB 1 HETATM 9745 C CHC . HEM Z 4 . ? 25.043 43.574 4.498 1.00 14.15 ? 607 HEM B CHC 1 HETATM 9746 C CHD . HEM Z 4 . ? 25.293 43.204 9.234 1.00 13.42 ? 607 HEM B CHD 1 HETATM 9747 C C1A . HEM Z 4 . ? 21.806 39.362 7.855 1.00 15.70 ? 607 HEM B C1A 1 HETATM 9748 C C2A . HEM Z 4 . ? 20.956 38.325 7.406 1.00 16.39 ? 607 HEM B C2A 1 HETATM 9749 C C3A . HEM Z 4 . ? 20.931 38.398 6.041 1.00 16.08 ? 607 HEM B C3A 1 HETATM 9750 C C4A . HEM Z 4 . ? 21.754 39.470 5.667 1.00 15.89 ? 607 HEM B C4A 1 HETATM 9751 C CMA . HEM Z 4 . ? 20.127 37.483 5.099 1.00 15.40 ? 607 HEM B CMA 1 HETATM 9752 C CAA . HEM Z 4 . ? 20.173 37.312 8.231 1.00 14.67 ? 607 HEM B CAA 1 HETATM 9753 C CBA . HEM Z 4 . ? 18.876 37.970 8.595 1.00 14.77 ? 607 HEM B CBA 1 HETATM 9754 C CGA . HEM Z 4 . ? 18.021 37.147 9.545 1.00 15.50 ? 607 HEM B CGA 1 HETATM 9755 O O1A . HEM Z 4 . ? 17.606 35.993 9.214 1.00 17.40 ? 607 HEM B O1A 1 HETATM 9756 O O2A . HEM Z 4 . ? 17.750 37.623 10.672 1.00 15.42 ? 607 HEM B O2A 1 HETATM 9757 C C1B . HEM Z 4 . ? 22.921 40.844 3.997 1.00 15.46 ? 607 HEM B C1B 1 HETATM 9758 C C2B . HEM Z 4 . ? 23.259 41.183 2.640 1.00 15.46 ? 607 HEM B C2B 1 HETATM 9759 C C3B . HEM Z 4 . ? 24.108 42.252 2.662 1.00 15.52 ? 607 HEM B C3B 1 HETATM 9760 C C4B . HEM Z 4 . ? 24.246 42.567 4.079 1.00 14.22 ? 607 HEM B C4B 1 HETATM 9761 C CMB . HEM Z 4 . ? 22.778 40.492 1.398 1.00 13.98 ? 607 HEM B CMB 1 HETATM 9762 C CAB . HEM Z 4 . ? 24.759 42.998 1.559 1.00 15.26 ? 607 HEM B CAB 1 HETATM 9763 C CBB . HEM Z 4 . ? 24.339 42.941 0.286 1.00 14.69 ? 607 HEM B CBB 1 HETATM 9764 C C1C . HEM Z 4 . ? 25.400 43.845 5.803 1.00 14.49 ? 607 HEM B C1C 1 HETATM 9765 C C2C . HEM Z 4 . ? 26.194 44.917 6.248 1.00 13.28 ? 607 HEM B C2C 1 HETATM 9766 C C3C . HEM Z 4 . ? 26.284 44.819 7.639 1.00 13.70 ? 607 HEM B C3C 1 HETATM 9767 C C4C . HEM Z 4 . ? 25.472 43.689 7.979 1.00 13.61 ? 607 HEM B C4C 1 HETATM 9768 C CMC . HEM Z 4 . ? 26.803 45.972 5.361 1.00 12.05 ? 607 HEM B CMC 1 HETATM 9769 C CAC . HEM Z 4 . ? 27.016 45.693 8.632 1.00 13.13 ? 607 HEM B CAC 1 HETATM 9770 C CBC . HEM Z 4 . ? 27.609 46.849 8.388 1.00 12.82 ? 607 HEM B CBC 1 HETATM 9771 C C1D . HEM Z 4 . ? 24.499 42.128 9.546 1.00 14.25 ? 607 HEM B C1D 1 HETATM 9772 C C2D . HEM Z 4 . ? 24.475 41.637 10.930 1.00 15.08 ? 607 HEM B C2D 1 HETATM 9773 C C3D . HEM Z 4 . ? 23.604 40.610 10.928 1.00 14.49 ? 607 HEM B C3D 1 HETATM 9774 C C4D . HEM Z 4 . ? 23.118 40.503 9.536 1.00 13.24 ? 607 HEM B C4D 1 HETATM 9775 C CMD . HEM Z 4 . ? 25.206 42.158 12.176 1.00 14.10 ? 607 HEM B CMD 1 HETATM 9776 C CAD . HEM Z 4 . ? 23.216 39.738 12.097 1.00 14.79 ? 607 HEM B CAD 1 HETATM 9777 C CBD . HEM Z 4 . ? 24.186 38.565 12.161 1.00 15.50 ? 607 HEM B CBD 1 HETATM 9778 C CGD . HEM Z 4 . ? 23.909 37.589 13.341 1.00 18.95 ? 607 HEM B CGD 1 HETATM 9779 O O1D . HEM Z 4 . ? 24.461 37.789 14.471 1.00 19.95 ? 607 HEM B O1D 1 HETATM 9780 O O2D . HEM Z 4 . ? 23.180 36.569 13.201 1.00 16.50 ? 607 HEM B O2D 1 HETATM 9781 N NA . HEM Z 4 . ? 22.195 40.129 6.756 1.00 16.34 ? 607 HEM B NA 1 HETATM 9782 N NB . HEM Z 4 . ? 23.402 41.777 4.761 1.00 16.96 ? 607 HEM B NB 1 HETATM 9783 N NC . HEM Z 4 . ? 24.854 43.221 6.825 1.00 14.89 ? 607 HEM B NC 1 HETATM 9784 N ND . HEM Z 4 . ? 23.568 41.485 8.791 1.00 15.14 ? 607 HEM B ND 1 HETATM 9785 FE FE . HEM Z 4 . ? 23.437 41.690 6.862 1.00 15.61 ? 607 HEM B FE 1 HETATM 9786 CA CA . CA AA 5 . ? 35.469 36.445 15.726 1.00 25.81 ? 608 CA B CA 1 HETATM 9787 N N . NO3 BA 6 . ? 20.381 42.468 24.824 1.00 29.25 ? 609 NO3 B N 1 HETATM 9788 O O1 . NO3 BA 6 . ? 19.757 42.116 23.829 1.00 32.30 ? 609 NO3 B O1 1 HETATM 9789 O O2 . NO3 BA 6 . ? 19.797 42.676 26.090 1.00 24.76 ? 609 NO3 B O2 1 HETATM 9790 O O3 . NO3 BA 6 . ? 21.716 42.646 24.685 1.00 32.03 ? 609 NO3 B O3 1 HETATM 9791 N N . NO3 CA 6 . ? 6.715 45.069 -4.080 1.00 29.10 ? 610 NO3 B N 1 HETATM 9792 O O1 . NO3 CA 6 . ? 7.063 44.887 -5.233 1.00 25.23 ? 610 NO3 B O1 1 HETATM 9793 O O2 . NO3 CA 6 . ? 6.655 46.348 -3.538 1.00 24.98 ? 610 NO3 B O2 1 HETATM 9794 O O3 . NO3 CA 6 . ? 6.408 43.982 -3.287 1.00 31.22 ? 610 NO3 B O3 1 HETATM 9795 N N . NO3 DA 6 . ? 40.807 54.350 4.908 1.00 62.72 ? 611 NO3 B N 1 HETATM 9796 O O1 . NO3 DA 6 . ? 40.801 53.255 4.363 1.00 61.92 ? 611 NO3 B O1 1 HETATM 9797 O O2 . NO3 DA 6 . ? 41.618 54.480 6.039 1.00 69.96 ? 611 NO3 B O2 1 HETATM 9798 O O3 . NO3 DA 6 . ? 40.036 55.435 4.433 1.00 55.05 ? 611 NO3 B O3 1 HETATM 9799 N N . NO3 EA 6 . ? 28.066 55.021 -7.840 1.00 37.67 ? 612 NO3 B N 1 HETATM 9800 O O1 . NO3 EA 6 . ? 27.467 53.945 -7.887 1.00 42.46 ? 612 NO3 B O1 1 HETATM 9801 O O2 . NO3 EA 6 . ? 29.027 55.291 -6.845 1.00 30.26 ? 612 NO3 B O2 1 HETATM 9802 O O3 . NO3 EA 6 . ? 27.865 55.930 -8.874 1.00 36.30 ? 612 NO3 B O3 1 HETATM 9803 N N1 . MMZ FA 2 . ? 24.012 36.839 6.999 0.50 31.18 ? 613 MMZ B N1 1 HETATM 9804 C C1A . MMZ FA 2 . ? 24.599 38.013 7.349 0.50 28.29 ? 613 MMZ B C1A 1 HETATM 9805 C C2 . MMZ FA 2 . ? 24.312 36.545 5.729 0.50 27.10 ? 613 MMZ B C2 1 HETATM 9806 S S2 . MMZ FA 2 . ? 23.837 35.185 4.902 0.50 25.39 ? 613 MMZ B S2 1 HETATM 9807 N N3 . MMZ FA 2 . ? 25.061 37.558 5.324 0.50 26.07 ? 613 MMZ B N3 1 HETATM 9808 C C3A . MMZ FA 2 . ? 25.232 38.462 6.242 0.50 27.32 ? 613 MMZ B C3A 1 HETATM 9809 C C4 . MMZ FA 2 . ? 25.657 37.743 4.037 0.50 29.35 ? 613 MMZ B C4 1 HETATM 9810 C C1 . GOL GA 7 . ? 7.437 27.624 20.491 1.00 34.16 ? 614 GOL B C1 1 HETATM 9811 O O1 . GOL GA 7 . ? 8.183 26.670 19.753 1.00 39.50 ? 614 GOL B O1 1 HETATM 9812 C C2 . GOL GA 7 . ? 7.099 28.827 19.588 1.00 31.09 ? 614 GOL B C2 1 HETATM 9813 O O2 . GOL GA 7 . ? 8.217 29.326 18.832 1.00 27.20 ? 614 GOL B O2 1 HETATM 9814 C C3 . GOL GA 7 . ? 6.597 29.962 20.426 1.00 28.40 ? 614 GOL B C3 1 HETATM 9815 O O3 . GOL GA 7 . ? 7.620 30.382 21.359 1.00 26.67 ? 614 GOL B O3 1 HETATM 9816 C C1 . GOL HA 7 . ? 1.419 40.400 21.196 1.00 28.08 ? 615 GOL B C1 1 HETATM 9817 O O1 . GOL HA 7 . ? 2.594 39.563 21.316 1.00 24.37 ? 615 GOL B O1 1 HETATM 9818 C C2 . GOL HA 7 . ? 1.274 40.713 19.696 1.00 27.10 ? 615 GOL B C2 1 HETATM 9819 O O2 . GOL HA 7 . ? 0.637 39.618 18.956 1.00 26.19 ? 615 GOL B O2 1 HETATM 9820 C C3 . GOL HA 7 . ? 0.652 42.058 19.471 1.00 26.70 ? 615 GOL B C3 1 HETATM 9821 O O3 . GOL HA 7 . ? 0.510 42.362 18.089 1.00 25.73 ? 615 GOL B O3 1 HETATM 9822 C C1 . GOL IA 7 . ? -1.109 40.057 27.514 1.00 35.67 ? 616 GOL B C1 1 HETATM 9823 O O1 . GOL IA 7 . ? -1.730 40.451 26.329 1.00 33.08 ? 616 GOL B O1 1 HETATM 9824 C C2 . GOL IA 7 . ? 0.254 40.692 27.596 1.00 34.76 ? 616 GOL B C2 1 HETATM 9825 O O2 . GOL IA 7 . ? 0.669 40.979 28.922 1.00 31.61 ? 616 GOL B O2 1 HETATM 9826 C C3 . GOL IA 7 . ? 1.226 39.770 26.927 1.00 35.37 ? 616 GOL B C3 1 HETATM 9827 O O3 . GOL IA 7 . ? 2.325 40.601 26.715 1.00 37.92 ? 616 GOL B O3 1 HETATM 9828 C C1 . GOL JA 7 . ? 48.960 37.731 27.732 1.00 58.21 ? 617 GOL B C1 1 HETATM 9829 O O1 . GOL JA 7 . ? 48.909 38.527 28.925 1.00 59.97 ? 617 GOL B O1 1 HETATM 9830 C C2 . GOL JA 7 . ? 49.504 38.536 26.553 1.00 57.32 ? 617 GOL B C2 1 HETATM 9831 O O2 . GOL JA 7 . ? 50.071 39.811 27.011 1.00 54.92 ? 617 GOL B O2 1 HETATM 9832 C C3 . GOL JA 7 . ? 50.500 37.628 25.807 1.00 56.23 ? 617 GOL B C3 1 HETATM 9833 O O3 . GOL JA 7 . ? 49.978 36.298 25.561 1.00 51.80 ? 617 GOL B O3 1 HETATM 9834 O O . HOH KA 8 . ? 2.847 5.674 31.383 1.00 19.82 ? 701 HOH A O 1 HETATM 9835 O O . HOH KA 8 . ? -13.058 10.317 41.084 1.00 33.74 ? 702 HOH A O 1 HETATM 9836 O O . HOH KA 8 . ? 0.964 5.622 29.563 1.00 24.74 ? 703 HOH A O 1 HETATM 9837 O O . HOH KA 8 . ? -13.231 12.227 14.482 1.00 24.08 ? 704 HOH A O 1 HETATM 9838 O O . HOH KA 8 . ? 28.719 -8.886 36.943 1.00 29.82 ? 705 HOH A O 1 HETATM 9839 O O . HOH KA 8 . ? 26.515 15.796 40.886 1.00 25.89 ? 706 HOH A O 1 HETATM 9840 O O . HOH KA 8 . ? 19.411 -21.437 32.966 1.00 59.47 ? 707 HOH A O 1 HETATM 9841 O O . HOH KA 8 . ? -18.907 0.960 9.462 1.00 31.21 ? 708 HOH A O 1 HETATM 9842 O O . HOH KA 8 . ? 27.972 -3.229 48.292 1.00 31.64 ? 709 HOH A O 1 HETATM 9843 O O . HOH KA 8 . ? 31.904 5.008 17.894 1.00 49.92 ? 710 HOH A O 1 HETATM 9844 O O . HOH KA 8 . ? -16.255 8.115 9.398 1.00 40.79 ? 711 HOH A O 1 HETATM 9845 O O . HOH KA 8 . ? 34.492 20.412 30.678 1.00 44.50 ? 712 HOH A O 1 HETATM 9846 O O . HOH KA 8 . ? -20.631 -14.274 32.195 1.00 48.37 ? 713 HOH A O 1 HETATM 9847 O O . HOH KA 8 . ? 6.986 11.872 62.461 1.00 48.91 ? 714 HOH A O 1 HETATM 9848 O O . HOH KA 8 . ? -11.358 18.076 27.568 1.00 43.04 ? 715 HOH A O 1 HETATM 9849 O O . HOH KA 8 . ? -0.594 -20.373 24.789 1.00 32.49 ? 716 HOH A O 1 HETATM 9850 O O . HOH KA 8 . ? 3.395 1.547 63.105 1.00 28.81 ? 717 HOH A O 1 HETATM 9851 O O . HOH KA 8 . ? 10.166 7.328 19.698 1.00 14.73 ? 718 HOH A O 1 HETATM 9852 O O . HOH KA 8 . ? 17.003 -10.064 13.785 1.00 25.67 ? 719 HOH A O 1 HETATM 9853 O O . HOH KA 8 . ? -0.012 10.344 23.232 1.00 30.20 ? 720 HOH A O 1 HETATM 9854 O O . HOH KA 8 . ? -6.893 -2.323 11.369 1.00 18.42 ? 721 HOH A O 1 HETATM 9855 O O . HOH KA 8 . ? 21.984 2.908 49.358 1.00 20.11 ? 722 HOH A O 1 HETATM 9856 O O . HOH KA 8 . ? -15.497 10.547 39.304 1.00 38.56 ? 723 HOH A O 1 HETATM 9857 O O . HOH KA 8 . ? 8.370 9.399 18.656 1.00 36.56 ? 724 HOH A O 1 HETATM 9858 O O . HOH KA 8 . ? 20.066 8.498 26.281 1.00 20.67 ? 725 HOH A O 1 HETATM 9859 O O . HOH KA 8 . ? 22.014 -2.337 15.244 1.00 23.13 ? 726 HOH A O 1 HETATM 9860 O O . HOH KA 8 . ? -0.833 6.304 38.682 1.00 35.96 ? 727 HOH A O 1 HETATM 9861 O O . HOH KA 8 . ? -20.585 -3.595 29.932 1.00 27.84 ? 728 HOH A O 1 HETATM 9862 O O . HOH KA 8 . ? 8.811 -7.631 33.585 1.00 17.33 ? 729 HOH A O 1 HETATM 9863 O O . HOH KA 8 . ? -6.595 22.971 36.492 1.00 39.69 ? 730 HOH A O 1 HETATM 9864 O O . HOH KA 8 . ? 24.674 -3.869 54.343 1.00 36.04 ? 731 HOH A O 1 HETATM 9865 O O . HOH KA 8 . ? 32.270 19.683 46.415 1.00 37.92 ? 732 HOH A O 1 HETATM 9866 O O . HOH KA 8 . ? 26.327 9.580 25.084 1.00 32.68 ? 733 HOH A O 1 HETATM 9867 O O . HOH KA 8 . ? 17.865 -14.726 32.120 1.00 38.65 ? 734 HOH A O 1 HETATM 9868 O O . HOH KA 8 . ? 27.091 16.646 45.410 1.00 38.37 ? 735 HOH A O 1 HETATM 9869 O O . HOH KA 8 . ? 28.987 -1.543 12.184 1.00 29.54 ? 736 HOH A O 1 HETATM 9870 O O . HOH KA 8 . ? 3.558 -12.419 32.798 1.00 19.01 ? 737 HOH A O 1 HETATM 9871 O O . HOH KA 8 . ? 25.766 18.075 25.090 1.00 36.67 ? 738 HOH A O 1 HETATM 9872 O O . HOH KA 8 . ? 13.677 -13.714 44.951 1.00 29.08 ? 739 HOH A O 1 HETATM 9873 O O . HOH KA 8 . ? -5.581 -5.134 47.589 1.00 33.51 ? 740 HOH A O 1 HETATM 9874 O O . HOH KA 8 . ? -6.801 -18.835 45.775 1.00 43.28 ? 741 HOH A O 1 HETATM 9875 O O . HOH KA 8 . ? 19.726 2.497 52.407 1.00 16.75 ? 742 HOH A O 1 HETATM 9876 O O . HOH KA 8 . ? -19.152 19.012 30.383 1.00 48.47 ? 743 HOH A O 1 HETATM 9877 O O . HOH KA 8 . ? 17.936 0.400 20.651 1.00 23.38 ? 744 HOH A O 1 HETATM 9878 O O . HOH KA 8 . ? 37.407 10.958 39.478 1.00 32.57 ? 745 HOH A O 1 HETATM 9879 O O . HOH KA 8 . ? 6.580 11.318 49.031 1.00 16.46 ? 746 HOH A O 1 HETATM 9880 O O . HOH KA 8 . ? -19.022 5.975 26.494 1.00 24.33 ? 747 HOH A O 1 HETATM 9881 O O . HOH KA 8 . ? -0.240 15.417 26.125 1.00 54.72 ? 748 HOH A O 1 HETATM 9882 O O . HOH KA 8 . ? 13.936 1.756 53.100 1.00 27.79 ? 749 HOH A O 1 HETATM 9883 O O . HOH KA 8 . ? 23.565 -16.752 43.153 1.00 38.79 ? 750 HOH A O 1 HETATM 9884 O O . HOH KA 8 . ? 21.950 13.083 47.284 1.00 21.51 ? 751 HOH A O 1 HETATM 9885 O O . HOH KA 8 . ? -21.857 -14.305 20.606 1.00 33.14 ? 752 HOH A O 1 HETATM 9886 O O . HOH KA 8 . ? -4.785 3.625 51.948 1.00 38.61 ? 753 HOH A O 1 HETATM 9887 O O . HOH KA 8 . ? -4.795 -16.022 11.013 1.00 38.24 ? 754 HOH A O 1 HETATM 9888 O O . HOH KA 8 . ? -13.222 13.367 17.071 1.00 24.23 ? 755 HOH A O 1 HETATM 9889 O O . HOH KA 8 . ? -10.241 -0.170 19.817 1.00 9.67 ? 756 HOH A O 1 HETATM 9890 O O . HOH KA 8 . ? -1.635 17.742 29.721 1.00 55.86 ? 757 HOH A O 1 HETATM 9891 O O . HOH KA 8 . ? 0.694 6.724 54.564 1.00 25.32 ? 758 HOH A O 1 HETATM 9892 O O . HOH KA 8 . ? -14.941 1.987 12.184 1.00 40.81 ? 759 HOH A O 1 HETATM 9893 O O . HOH KA 8 . ? 18.794 3.888 12.687 1.00 25.81 ? 760 HOH A O 1 HETATM 9894 O O . HOH KA 8 . ? 11.425 -2.721 10.126 1.00 29.48 ? 761 HOH A O 1 HETATM 9895 O O . HOH KA 8 . ? -13.156 -3.016 13.923 1.00 34.56 ? 762 HOH A O 1 HETATM 9896 O O . HOH KA 8 . ? -11.053 2.574 19.263 1.00 14.30 ? 763 HOH A O 1 HETATM 9897 O O . HOH KA 8 . ? -5.646 9.715 42.653 1.00 19.82 ? 764 HOH A O 1 HETATM 9898 O O . HOH KA 8 . ? -4.322 -2.535 50.777 1.00 29.89 ? 765 HOH A O 1 HETATM 9899 O O . HOH KA 8 . ? 10.269 16.422 56.103 1.00 45.98 ? 766 HOH A O 1 HETATM 9900 O O . HOH KA 8 . ? -4.833 -7.918 47.630 1.00 27.38 ? 767 HOH A O 1 HETATM 9901 O O . HOH KA 8 . ? 26.027 2.713 22.037 1.00 39.08 ? 768 HOH A O 1 HETATM 9902 O O . HOH KA 8 . ? 3.346 -15.866 15.677 1.00 31.63 ? 769 HOH A O 1 HETATM 9903 O O . HOH KA 8 . ? 7.977 6.569 44.369 1.00 19.62 ? 770 HOH A O 1 HETATM 9904 O O . HOH KA 8 . ? 37.173 17.546 33.273 1.00 33.35 ? 771 HOH A O 1 HETATM 9905 O O . HOH KA 8 . ? 24.093 5.658 23.891 1.00 22.73 ? 772 HOH A O 1 HETATM 9906 O O . HOH KA 8 . ? 12.934 10.101 28.434 1.00 17.13 ? 773 HOH A O 1 HETATM 9907 O O . HOH KA 8 . ? 12.431 -16.046 46.289 1.00 24.65 ? 774 HOH A O 1 HETATM 9908 O O . HOH KA 8 . ? 31.622 4.850 26.318 1.00 37.68 ? 775 HOH A O 1 HETATM 9909 O O . HOH KA 8 . ? 31.730 -2.761 38.015 1.00 40.12 ? 776 HOH A O 1 HETATM 9910 O O . HOH KA 8 . ? -21.276 -6.611 24.348 1.00 39.73 ? 777 HOH A O 1 HETATM 9911 O O . HOH KA 8 . ? 20.678 -8.753 13.531 1.00 29.21 ? 778 HOH A O 1 HETATM 9912 O O . HOH KA 8 . ? 7.536 -16.476 49.106 1.00 44.78 ? 779 HOH A O 1 HETATM 9913 O O . HOH KA 8 . ? -20.449 12.080 38.991 1.00 36.30 ? 780 HOH A O 1 HETATM 9914 O O . HOH KA 8 . ? 22.430 -0.762 54.296 1.00 39.98 ? 781 HOH A O 1 HETATM 9915 O O . HOH KA 8 . ? -5.906 -8.799 44.721 1.00 22.51 ? 782 HOH A O 1 HETATM 9916 O O . HOH KA 8 . ? 33.152 6.133 22.519 1.00 44.15 ? 783 HOH A O 1 HETATM 9917 O O . HOH KA 8 . ? 11.058 12.246 36.919 1.00 25.25 ? 784 HOH A O 1 HETATM 9918 O O . HOH KA 8 . ? -17.857 7.361 28.946 1.00 32.72 ? 785 HOH A O 1 HETATM 9919 O O . HOH KA 8 . ? -10.414 -14.706 34.948 1.00 27.08 ? 786 HOH A O 1 HETATM 9920 O O . HOH KA 8 . ? 9.436 -6.569 48.392 1.00 22.21 ? 787 HOH A O 1 HETATM 9921 O O . HOH KA 8 . ? 18.002 10.258 25.356 1.00 22.90 ? 788 HOH A O 1 HETATM 9922 O O . HOH KA 8 . ? -21.848 4.363 36.598 1.00 32.89 ? 789 HOH A O 1 HETATM 9923 O O . HOH KA 8 . ? -3.023 -18.683 43.410 1.00 42.94 ? 790 HOH A O 1 HETATM 9924 O O . HOH KA 8 . ? -10.145 -5.424 14.934 1.00 15.25 ? 791 HOH A O 1 HETATM 9925 O O . HOH KA 8 . ? 30.249 17.080 36.559 1.00 30.22 ? 792 HOH A O 1 HETATM 9926 O O . HOH KA 8 . ? 22.782 -10.554 38.405 1.00 23.07 ? 793 HOH A O 1 HETATM 9927 O O . HOH KA 8 . ? -18.102 -6.277 21.877 1.00 18.18 ? 794 HOH A O 1 HETATM 9928 O O . HOH KA 8 . ? 1.650 8.361 52.376 1.00 29.19 ? 795 HOH A O 1 HETATM 9929 O O . HOH KA 8 . ? 38.025 -0.371 35.746 1.00 31.95 ? 796 HOH A O 1 HETATM 9930 O O . HOH KA 8 . ? -25.733 -0.480 40.463 1.00 40.66 ? 797 HOH A O 1 HETATM 9931 O O . HOH KA 8 . ? -16.878 -14.260 16.219 1.00 33.34 ? 798 HOH A O 1 HETATM 9932 O O . HOH KA 8 . ? 0.639 3.781 25.502 1.00 17.99 ? 799 HOH A O 1 HETATM 9933 O O . HOH KA 8 . ? -0.099 -6.725 27.417 1.00 37.45 ? 800 HOH A O 1 HETATM 9934 O O . HOH KA 8 . ? 30.479 17.394 46.690 1.00 33.05 ? 801 HOH A O 1 HETATM 9935 O O . HOH KA 8 . ? -3.496 0.475 14.855 1.00 15.90 ? 802 HOH A O 1 HETATM 9936 O O . HOH KA 8 . ? 5.905 -13.214 36.750 1.00 17.97 ? 803 HOH A O 1 HETATM 9937 O O . HOH KA 8 . ? -19.023 23.416 35.456 1.00 45.30 ? 804 HOH A O 1 HETATM 9938 O O . HOH KA 8 . ? 34.233 12.798 36.897 1.00 31.38 ? 805 HOH A O 1 HETATM 9939 O O . HOH KA 8 . ? 0.471 -10.457 45.716 1.00 24.15 ? 806 HOH A O 1 HETATM 9940 O O . HOH KA 8 . ? 2.558 20.119 47.194 1.00 36.20 ? 807 HOH A O 1 HETATM 9941 O O . HOH KA 8 . ? 6.647 -8.270 50.212 1.00 21.32 ? 808 HOH A O 1 HETATM 9942 O O . HOH KA 8 . ? 17.996 12.513 37.973 1.00 18.81 ? 809 HOH A O 1 HETATM 9943 O O . HOH KA 8 . ? 7.407 16.698 43.179 1.00 29.17 ? 810 HOH A O 1 HETATM 9944 O O . HOH KA 8 . ? -13.227 4.060 47.074 1.00 36.96 ? 811 HOH A O 1 HETATM 9945 O O . HOH KA 8 . ? -18.831 7.813 15.437 1.00 16.48 ? 812 HOH A O 1 HETATM 9946 O O . HOH KA 8 . ? 22.390 2.735 24.233 1.00 21.70 ? 813 HOH A O 1 HETATM 9947 O O . HOH KA 8 . ? 18.584 18.554 37.983 1.00 32.70 ? 814 HOH A O 1 HETATM 9948 O O . HOH KA 8 . ? 1.168 -14.287 48.164 1.00 44.11 ? 815 HOH A O 1 HETATM 9949 O O . HOH KA 8 . ? 0.393 11.143 12.300 1.00 28.60 ? 816 HOH A O 1 HETATM 9950 O O . HOH KA 8 . ? -2.996 7.173 33.916 1.00 34.07 ? 817 HOH A O 1 HETATM 9951 O O . HOH KA 8 . ? 16.886 8.336 13.383 1.00 21.36 ? 818 HOH A O 1 HETATM 9952 O O . HOH KA 8 . ? 38.552 -3.234 18.637 1.00 36.22 ? 819 HOH A O 1 HETATM 9953 O O . HOH KA 8 . ? 6.577 -10.219 46.503 1.00 18.01 ? 820 HOH A O 1 HETATM 9954 O O . HOH KA 8 . ? -10.144 -8.433 15.985 1.00 20.34 ? 821 HOH A O 1 HETATM 9955 O O . HOH KA 8 . ? 10.216 6.111 34.908 1.00 15.14 ? 822 HOH A O 1 HETATM 9956 O O . HOH KA 8 . ? 22.310 -0.832 7.367 1.00 39.88 ? 823 HOH A O 1 HETATM 9957 O O . HOH KA 8 . ? 20.109 18.951 42.938 1.00 29.30 ? 824 HOH A O 1 HETATM 9958 O O . HOH KA 8 . ? -25.259 4.329 43.111 1.00 46.77 ? 825 HOH A O 1 HETATM 9959 O O . HOH KA 8 . ? 1.701 -18.560 41.105 1.00 34.93 ? 826 HOH A O 1 HETATM 9960 O O . HOH KA 8 . ? 12.148 14.896 14.899 1.00 47.92 ? 827 HOH A O 1 HETATM 9961 O O . HOH KA 8 . ? 18.928 8.532 21.394 1.00 20.97 ? 828 HOH A O 1 HETATM 9962 O O . HOH KA 8 . ? -6.054 9.987 21.829 1.00 21.87 ? 829 HOH A O 1 HETATM 9963 O O . HOH KA 8 . ? 27.646 12.500 44.138 1.00 39.21 ? 830 HOH A O 1 HETATM 9964 O O . HOH KA 8 . ? 14.669 -17.895 26.455 1.00 37.41 ? 831 HOH A O 1 HETATM 9965 O O . HOH KA 8 . ? 21.708 -9.053 35.497 1.00 24.20 ? 832 HOH A O 1 HETATM 9966 O O . HOH KA 8 . ? 4.306 11.666 34.123 1.00 38.98 ? 833 HOH A O 1 HETATM 9967 O O . HOH KA 8 . ? 11.243 13.995 33.726 1.00 29.71 ? 834 HOH A O 1 HETATM 9968 O O . HOH KA 8 . ? -9.758 12.545 43.194 1.00 40.19 ? 835 HOH A O 1 HETATM 9969 O O . HOH KA 8 . ? 14.802 14.643 54.896 1.00 38.63 ? 836 HOH A O 1 HETATM 9970 O O . HOH KA 8 . ? -2.359 8.982 10.685 1.00 36.65 ? 837 HOH A O 1 HETATM 9971 O O . HOH KA 8 . ? -2.361 15.213 43.419 1.00 45.69 ? 838 HOH A O 1 HETATM 9972 O O . HOH KA 8 . ? 21.089 14.465 30.901 1.00 24.29 ? 839 HOH A O 1 HETATM 9973 O O . HOH KA 8 . ? -9.306 -1.763 21.960 1.00 13.65 ? 840 HOH A O 1 HETATM 9974 O O . HOH KA 8 . ? 12.439 9.609 5.186 1.00 38.91 ? 841 HOH A O 1 HETATM 9975 O O . HOH KA 8 . ? -8.042 -7.664 41.820 1.00 17.35 ? 842 HOH A O 1 HETATM 9976 O O . HOH KA 8 . ? -15.219 2.203 26.376 1.00 17.26 ? 843 HOH A O 1 HETATM 9977 O O . HOH KA 8 . ? 0.526 6.453 47.821 1.00 18.45 ? 844 HOH A O 1 HETATM 9978 O O . HOH KA 8 . ? -0.986 -7.596 39.623 1.00 14.49 ? 845 HOH A O 1 HETATM 9979 O O . HOH KA 8 . ? 11.949 15.314 22.564 1.00 29.34 ? 846 HOH A O 1 HETATM 9980 O O . HOH KA 8 . ? 17.830 8.693 53.293 1.00 28.94 ? 847 HOH A O 1 HETATM 9981 O O . HOH KA 8 . ? 33.773 -11.150 28.028 1.00 42.69 ? 848 HOH A O 1 HETATM 9982 O O . HOH KA 8 . ? 6.245 -10.725 51.507 1.00 35.76 ? 849 HOH A O 1 HETATM 9983 O O . HOH KA 8 . ? -8.401 7.004 48.584 1.00 33.83 ? 850 HOH A O 1 HETATM 9984 O O . HOH KA 8 . ? -21.109 11.059 30.033 1.00 45.72 ? 851 HOH A O 1 HETATM 9985 O O . HOH KA 8 . ? 34.284 -6.355 32.621 1.00 33.91 ? 852 HOH A O 1 HETATM 9986 O O . HOH KA 8 . ? 33.872 -0.082 36.558 1.00 32.06 ? 853 HOH A O 1 HETATM 9987 O O . HOH KA 8 . ? 39.639 -0.689 23.927 1.00 44.60 ? 854 HOH A O 1 HETATM 9988 O O . HOH KA 8 . ? 9.587 11.418 39.184 1.00 21.26 ? 855 HOH A O 1 HETATM 9989 O O . HOH KA 8 . ? 15.006 -17.104 14.368 1.00 53.02 ? 856 HOH A O 1 HETATM 9990 O O . HOH KA 8 . ? 33.889 -2.264 16.847 1.00 43.84 ? 857 HOH A O 1 HETATM 9991 O O . HOH KA 8 . ? -2.890 9.929 54.669 1.00 41.50 ? 858 HOH A O 1 HETATM 9992 O O . HOH KA 8 . ? 17.274 -12.302 43.003 1.00 27.67 ? 859 HOH A O 1 HETATM 9993 O O . HOH KA 8 . ? -12.251 -24.356 31.881 1.00 41.05 ? 860 HOH A O 1 HETATM 9994 O O . HOH KA 8 . ? -17.227 -9.620 13.830 1.00 31.04 ? 861 HOH A O 1 HETATM 9995 O O . HOH KA 8 . ? -13.650 7.588 40.717 1.00 28.61 ? 862 HOH A O 1 HETATM 9996 O O . HOH KA 8 . ? 21.069 2.603 2.014 1.00 50.72 ? 863 HOH A O 1 HETATM 9997 O O . HOH KA 8 . ? -8.048 -3.930 20.944 1.00 15.51 ? 864 HOH A O 1 HETATM 9998 O O . HOH KA 8 . ? -18.068 -0.630 48.262 1.00 33.18 ? 865 HOH A O 1 HETATM 9999 O O . HOH KA 8 . ? 5.490 13.423 51.273 1.00 22.04 ? 866 HOH A O 1 HETATM 10000 O O . HOH KA 8 . ? -16.468 -23.796 16.459 1.00 45.70 ? 867 HOH A O 1 HETATM 10001 O O . HOH KA 8 . ? 21.416 -16.707 41.487 1.00 31.25 ? 868 HOH A O 1 HETATM 10002 O O . HOH KA 8 . ? -0.239 -14.185 27.742 1.00 20.13 ? 869 HOH A O 1 HETATM 10003 O O . HOH KA 8 . ? 21.231 -14.884 27.146 1.00 33.42 ? 870 HOH A O 1 HETATM 10004 O O . HOH KA 8 . ? -0.160 -13.671 24.342 1.00 17.55 ? 871 HOH A O 1 HETATM 10005 O O . HOH KA 8 . ? -2.976 12.388 14.568 1.00 24.92 ? 872 HOH A O 1 HETATM 10006 O O . HOH KA 8 . ? 12.797 7.467 28.505 1.00 18.69 ? 873 HOH A O 1 HETATM 10007 O O . HOH KA 8 . ? 31.514 23.078 41.124 1.00 49.75 ? 874 HOH A O 1 HETATM 10008 O O . HOH KA 8 . ? -12.842 -5.620 15.840 1.00 22.50 ? 875 HOH A O 1 HETATM 10009 O O . HOH KA 8 . ? 24.071 10.423 54.331 1.00 32.59 ? 876 HOH A O 1 HETATM 10010 O O . HOH KA 8 . ? 27.978 -1.235 38.296 1.00 24.43 ? 877 HOH A O 1 HETATM 10011 O O . HOH KA 8 . ? 27.441 16.028 9.040 1.00 58.91 ? 878 HOH A O 1 HETATM 10012 O O . HOH KA 8 . ? -15.535 1.929 29.644 1.00 14.70 ? 879 HOH A O 1 HETATM 10013 O O . HOH KA 8 . ? 12.850 -9.092 8.480 1.00 53.01 ? 880 HOH A O 1 HETATM 10014 O O . HOH KA 8 . ? -16.626 16.828 29.796 1.00 41.18 ? 881 HOH A O 1 HETATM 10015 O O . HOH KA 8 . ? 11.785 -23.054 20.621 1.00 38.03 ? 882 HOH A O 1 HETATM 10016 O O . HOH KA 8 . ? 3.773 -16.273 18.426 1.00 33.38 ? 883 HOH A O 1 HETATM 10017 O O . HOH KA 8 . ? 37.873 15.931 26.266 1.00 38.81 ? 884 HOH A O 1 HETATM 10018 O O . HOH KA 8 . ? 1.423 -10.984 32.420 1.00 20.85 ? 885 HOH A O 1 HETATM 10019 O O . HOH KA 8 . ? -10.943 14.891 36.147 1.00 44.08 ? 886 HOH A O 1 HETATM 10020 O O . HOH KA 8 . ? 10.317 1.741 59.694 1.00 36.68 ? 887 HOH A O 1 HETATM 10021 O O . HOH KA 8 . ? 2.113 -9.578 9.431 1.00 26.63 ? 888 HOH A O 1 HETATM 10022 O O . HOH KA 8 . ? 0.016 5.968 16.341 1.00 23.60 ? 889 HOH A O 1 HETATM 10023 O O . HOH KA 8 . ? 21.775 4.999 9.088 1.00 34.30 ? 890 HOH A O 1 HETATM 10024 O O . HOH KA 8 . ? 18.626 1.323 56.109 1.00 36.39 ? 891 HOH A O 1 HETATM 10025 O O . HOH KA 8 . ? 27.168 0.978 11.490 1.00 26.40 ? 892 HOH A O 1 HETATM 10026 O O . HOH KA 8 . ? -3.341 -19.456 34.426 1.00 23.80 ? 893 HOH A O 1 HETATM 10027 O O . HOH KA 8 . ? 19.977 -1.435 55.184 1.00 34.43 ? 894 HOH A O 1 HETATM 10028 O O . HOH KA 8 . ? 7.329 5.223 18.809 1.00 14.25 ? 895 HOH A O 1 HETATM 10029 O O . HOH KA 8 . ? 20.135 14.287 37.525 1.00 19.36 ? 896 HOH A O 1 HETATM 10030 O O . HOH KA 8 . ? 30.513 -2.136 19.174 1.00 27.15 ? 897 HOH A O 1 HETATM 10031 O O . HOH KA 8 . ? 10.001 -0.760 59.385 1.00 23.61 ? 898 HOH A O 1 HETATM 10032 O O . HOH KA 8 . ? 11.547 -4.512 48.067 1.00 18.44 ? 899 HOH A O 1 HETATM 10033 O O . HOH KA 8 . ? 11.152 -10.697 14.910 1.00 38.49 ? 900 HOH A O 1 HETATM 10034 O O . HOH KA 8 . ? 7.810 7.262 16.941 1.00 20.10 ? 901 HOH A O 1 HETATM 10035 O O . HOH KA 8 . ? 17.400 7.747 36.682 1.00 20.20 ? 902 HOH A O 1 HETATM 10036 O O . HOH KA 8 . ? 6.560 8.400 13.568 1.00 21.43 ? 903 HOH A O 1 HETATM 10037 O O . HOH KA 8 . ? -23.963 -9.325 35.109 1.00 38.56 ? 904 HOH A O 1 HETATM 10038 O O . HOH KA 8 . ? 22.845 5.994 26.439 1.00 22.51 ? 905 HOH A O 1 HETATM 10039 O O . HOH KA 8 . ? -22.785 -8.568 14.043 1.00 18.79 ? 906 HOH A O 1 HETATM 10040 O O . HOH KA 8 . ? -5.523 9.525 48.948 1.00 38.19 ? 907 HOH A O 1 HETATM 10041 O O . HOH KA 8 . ? 15.239 -15.328 50.822 1.00 50.92 ? 908 HOH A O 1 HETATM 10042 O O . HOH KA 8 . ? 27.584 -11.706 23.044 1.00 49.47 ? 909 HOH A O 1 HETATM 10043 O O . HOH KA 8 . ? 22.553 -26.618 46.650 1.00 44.52 ? 910 HOH A O 1 HETATM 10044 O O . HOH KA 8 . ? 27.578 -12.470 28.853 1.00 48.97 ? 911 HOH A O 1 HETATM 10045 O O . HOH KA 8 . ? 25.000 3.112 24.354 1.00 27.02 ? 912 HOH A O 1 HETATM 10046 O O . HOH KA 8 . ? 17.129 1.773 11.077 1.00 34.59 ? 913 HOH A O 1 HETATM 10047 O O . HOH KA 8 . ? -21.345 10.478 18.711 1.00 38.01 ? 914 HOH A O 1 HETATM 10048 O O . HOH KA 8 . ? 27.481 7.264 42.551 1.00 22.94 ? 915 HOH A O 1 HETATM 10049 O O . HOH KA 8 . ? 8.950 -8.666 54.819 1.00 30.48 ? 916 HOH A O 1 HETATM 10050 O O . HOH KA 8 . ? 5.940 -20.675 31.330 1.00 24.16 ? 917 HOH A O 1 HETATM 10051 O O . HOH KA 8 . ? -9.157 -3.589 51.087 1.00 45.58 ? 918 HOH A O 1 HETATM 10052 O O . HOH KA 8 . ? -26.171 6.889 21.074 1.00 46.15 ? 919 HOH A O 1 HETATM 10053 O O . HOH KA 8 . ? 22.765 -13.507 57.756 1.00 37.01 ? 920 HOH A O 1 HETATM 10054 O O . HOH KA 8 . ? 4.039 -9.522 47.714 1.00 30.46 ? 921 HOH A O 1 HETATM 10055 O O . HOH KA 8 . ? 14.695 -8.366 61.740 1.00 40.18 ? 922 HOH A O 1 HETATM 10056 O O . HOH KA 8 . ? 10.037 8.190 15.920 1.00 25.79 ? 923 HOH A O 1 HETATM 10057 O O . HOH KA 8 . ? -20.715 7.270 45.940 1.00 39.58 ? 924 HOH A O 1 HETATM 10058 O O . HOH KA 8 . ? 7.687 -0.010 14.079 1.00 21.83 ? 925 HOH A O 1 HETATM 10059 O O . HOH KA 8 . ? 18.286 -9.780 61.183 1.00 31.72 ? 926 HOH A O 1 HETATM 10060 O O . HOH KA 8 . ? 0.429 6.257 50.670 1.00 27.90 ? 927 HOH A O 1 HETATM 10061 O O . HOH KA 8 . ? 11.466 2.061 52.231 1.00 22.44 ? 928 HOH A O 1 HETATM 10062 O O . HOH KA 8 . ? -8.460 -12.552 37.520 1.00 20.41 ? 929 HOH A O 1 HETATM 10063 O O . HOH KA 8 . ? -5.707 -9.110 10.939 1.00 42.32 ? 930 HOH A O 1 HETATM 10064 O O . HOH KA 8 . ? 30.088 18.251 33.491 1.00 31.71 ? 931 HOH A O 1 HETATM 10065 O O . HOH KA 8 . ? 23.638 18.457 27.959 1.00 41.58 ? 932 HOH A O 1 HETATM 10066 O O . HOH KA 8 . ? -31.231 0.319 24.359 1.00 45.23 ? 933 HOH A O 1 HETATM 10067 O O . HOH KA 8 . ? 27.323 -4.489 35.957 1.00 23.67 ? 934 HOH A O 1 HETATM 10068 O O . HOH KA 8 . ? 31.612 25.324 36.235 1.00 48.00 ? 935 HOH A O 1 HETATM 10069 O O . HOH KA 8 . ? 6.460 -5.869 13.057 1.00 28.39 ? 936 HOH A O 1 HETATM 10070 O O . HOH KA 8 . ? 27.613 -0.314 33.991 1.00 25.94 ? 937 HOH A O 1 HETATM 10071 O O . HOH KA 8 . ? 21.515 -9.607 20.554 1.00 42.08 ? 938 HOH A O 1 HETATM 10072 O O . HOH KA 8 . ? -15.232 -12.519 11.927 1.00 32.72 ? 939 HOH A O 1 HETATM 10073 O O . HOH KA 8 . ? -13.530 -20.664 16.046 1.00 38.06 ? 940 HOH A O 1 HETATM 10074 O O . HOH KA 8 . ? 3.797 3.595 53.005 1.00 18.01 ? 941 HOH A O 1 HETATM 10075 O O . HOH KA 8 . ? 12.891 21.260 40.254 1.00 27.67 ? 942 HOH A O 1 HETATM 10076 O O . HOH KA 8 . ? 12.952 11.501 8.955 1.00 42.39 ? 943 HOH A O 1 HETATM 10077 O O . HOH KA 8 . ? 19.499 22.317 36.884 1.00 41.23 ? 944 HOH A O 1 HETATM 10078 O O . HOH KA 8 . ? 33.245 -6.292 44.685 1.00 45.24 ? 945 HOH A O 1 HETATM 10079 O O . HOH KA 8 . ? -2.447 -19.792 20.327 1.00 23.65 ? 946 HOH A O 1 HETATM 10080 O O . HOH KA 8 . ? -15.867 1.262 32.378 1.00 16.33 ? 947 HOH A O 1 HETATM 10081 O O . HOH KA 8 . ? 21.383 15.970 21.805 1.00 45.15 ? 948 HOH A O 1 HETATM 10082 O O . HOH KA 8 . ? 24.414 22.639 36.442 1.00 42.98 ? 949 HOH A O 1 HETATM 10083 O O . HOH KA 8 . ? -3.066 15.434 51.360 1.00 39.76 ? 950 HOH A O 1 HETATM 10084 O O . HOH KA 8 . ? -13.300 -3.375 21.862 1.00 14.57 ? 951 HOH A O 1 HETATM 10085 O O . HOH KA 8 . ? 2.959 4.130 11.111 1.00 30.55 ? 952 HOH A O 1 HETATM 10086 O O . HOH KA 8 . ? 10.295 20.571 51.870 1.00 45.86 ? 953 HOH A O 1 HETATM 10087 O O . HOH KA 8 . ? -7.912 -6.793 10.633 1.00 35.03 ? 954 HOH A O 1 HETATM 10088 O O . HOH KA 8 . ? 5.032 12.107 13.845 1.00 21.85 ? 955 HOH A O 1 HETATM 10089 O O . HOH KA 8 . ? -2.520 -20.447 15.759 1.00 27.16 ? 956 HOH A O 1 HETATM 10090 O O . HOH KA 8 . ? -8.084 3.931 9.963 1.00 32.26 ? 957 HOH A O 1 HETATM 10091 O O . HOH KA 8 . ? 35.932 -7.462 44.303 1.00 43.61 ? 958 HOH A O 1 HETATM 10092 O O . HOH KA 8 . ? 9.937 8.205 58.713 1.00 37.49 ? 959 HOH A O 1 HETATM 10093 O O . HOH KA 8 . ? 3.912 -14.005 34.989 1.00 16.83 ? 960 HOH A O 1 HETATM 10094 O O . HOH KA 8 . ? -14.729 -4.655 41.846 1.00 27.53 ? 961 HOH A O 1 HETATM 10095 O O . HOH KA 8 . ? -16.944 15.692 22.147 1.00 36.34 ? 962 HOH A O 1 HETATM 10096 O O . HOH KA 8 . ? 0.460 -12.364 30.225 1.00 36.17 ? 963 HOH A O 1 HETATM 10097 O O . HOH KA 8 . ? 7.310 -7.992 47.601 1.00 14.02 ? 964 HOH A O 1 HETATM 10098 O O . HOH KA 8 . ? 17.379 23.701 30.265 1.00 44.32 ? 965 HOH A O 1 HETATM 10099 O O . HOH KA 8 . ? 33.501 -1.989 40.815 1.00 36.52 ? 966 HOH A O 1 HETATM 10100 O O . HOH KA 8 . ? 23.187 3.032 51.854 1.00 26.18 ? 967 HOH A O 1 HETATM 10101 O O . HOH KA 8 . ? -24.030 -1.487 34.205 1.00 34.49 ? 968 HOH A O 1 HETATM 10102 O O . HOH KA 8 . ? 17.735 10.438 36.101 1.00 20.91 ? 969 HOH A O 1 HETATM 10103 O O . HOH KA 8 . ? -8.947 -20.658 16.508 1.00 29.43 ? 970 HOH A O 1 HETATM 10104 O O . HOH KA 8 . ? 10.501 -14.104 51.475 1.00 41.52 ? 971 HOH A O 1 HETATM 10105 O O . HOH KA 8 . ? -2.717 6.225 11.597 1.00 29.75 ? 972 HOH A O 1 HETATM 10106 O O . HOH KA 8 . ? -0.296 -16.999 39.736 1.00 34.88 ? 973 HOH A O 1 HETATM 10107 O O . HOH KA 8 . ? -17.126 3.972 30.255 1.00 17.23 ? 974 HOH A O 1 HETATM 10108 O O . HOH KA 8 . ? -4.946 7.501 8.215 1.00 25.41 ? 975 HOH A O 1 HETATM 10109 O O . HOH KA 8 . ? -10.955 -7.553 43.542 1.00 36.46 ? 976 HOH A O 1 HETATM 10110 O O . HOH KA 8 . ? 25.707 7.433 22.871 1.00 26.61 ? 977 HOH A O 1 HETATM 10111 O O . HOH KA 8 . ? -12.506 -11.647 38.005 1.00 26.97 ? 978 HOH A O 1 HETATM 10112 O O . HOH KA 8 . ? 10.025 -15.134 48.698 1.00 39.00 ? 979 HOH A O 1 HETATM 10113 O O . HOH KA 8 . ? -23.105 6.490 43.066 1.00 43.41 ? 980 HOH A O 1 HETATM 10114 O O . HOH KA 8 . ? -15.123 -7.975 11.724 1.00 41.80 ? 981 HOH A O 1 HETATM 10115 O O . HOH KA 8 . ? 12.326 13.660 28.430 1.00 29.25 ? 982 HOH A O 1 HETATM 10116 O O . HOH KA 8 . ? -9.911 -5.305 11.109 1.00 30.86 ? 983 HOH A O 1 HETATM 10117 O O . HOH KA 8 . ? -17.036 -2.289 13.170 1.00 26.82 ? 984 HOH A O 1 HETATM 10118 O O . HOH KA 8 . ? 6.757 10.667 39.072 1.00 39.56 ? 985 HOH A O 1 HETATM 10119 O O . HOH KA 8 . ? -21.984 -5.457 36.749 1.00 42.84 ? 986 HOH A O 1 HETATM 10120 O O . HOH KA 8 . ? 19.906 12.804 54.189 1.00 34.86 ? 987 HOH A O 1 HETATM 10121 O O . HOH KA 8 . ? -11.219 -18.098 11.690 1.00 47.57 ? 988 HOH A O 1 HETATM 10122 O O . HOH KA 8 . ? -3.961 4.137 10.796 1.00 19.93 ? 989 HOH A O 1 HETATM 10123 O O . HOH KA 8 . ? 27.578 17.240 33.280 1.00 37.62 ? 990 HOH A O 1 HETATM 10124 O O . HOH KA 8 . ? 28.093 21.352 46.495 1.00 41.66 ? 991 HOH A O 1 HETATM 10125 O O . HOH KA 8 . ? 21.042 8.052 55.489 1.00 28.09 ? 992 HOH A O 1 HETATM 10126 O O . HOH KA 8 . ? 21.252 18.883 26.426 1.00 29.20 ? 993 HOH A O 1 HETATM 10127 O O . HOH KA 8 . ? -19.110 -5.920 37.401 1.00 28.46 ? 994 HOH A O 1 HETATM 10128 O O . HOH KA 8 . ? 0.075 -20.092 31.423 1.00 33.10 ? 995 HOH A O 1 HETATM 10129 O O . HOH KA 8 . ? 8.595 11.995 12.070 1.00 48.98 ? 996 HOH A O 1 HETATM 10130 O O . HOH KA 8 . ? 26.377 8.022 45.155 1.00 33.71 ? 997 HOH A O 1 HETATM 10131 O O . HOH KA 8 . ? -11.679 2.563 11.895 1.00 28.83 ? 998 HOH A O 1 HETATM 10132 O O . HOH KA 8 . ? 8.529 11.287 30.593 1.00 54.68 ? 999 HOH A O 1 HETATM 10133 O O . HOH KA 8 . ? 3.174 -17.777 45.933 1.00 27.41 ? 1000 HOH A O 1 HETATM 10134 O O . HOH KA 8 . ? -22.933 -0.994 44.519 1.00 32.83 ? 1001 HOH A O 1 HETATM 10135 O O . HOH KA 8 . ? -23.862 8.384 22.831 1.00 36.41 ? 1002 HOH A O 1 HETATM 10136 O O . HOH KA 8 . ? 20.116 7.561 19.167 1.00 20.08 ? 1003 HOH A O 1 HETATM 10137 O O . HOH KA 8 . ? 16.008 7.112 56.846 1.00 30.91 ? 1004 HOH A O 1 HETATM 10138 O O . HOH KA 8 . ? 10.154 -11.002 55.072 1.00 36.25 ? 1005 HOH A O 1 HETATM 10139 O O . HOH KA 8 . ? 36.756 -3.110 37.650 1.00 51.23 ? 1006 HOH A O 1 HETATM 10140 O O . HOH KA 8 . ? 26.718 8.877 55.568 1.00 46.65 ? 1007 HOH A O 1 HETATM 10141 O O . HOH KA 8 . ? -12.158 -17.065 34.575 1.00 27.27 ? 1008 HOH A O 1 HETATM 10142 O O . HOH KA 8 . ? 10.580 13.242 31.031 1.00 40.40 ? 1009 HOH A O 1 HETATM 10143 O O . HOH KA 8 . ? -21.949 12.745 26.707 1.00 51.22 ? 1010 HOH A O 1 HETATM 10144 O O . HOH KA 8 . ? 33.526 1.261 41.634 1.00 28.73 ? 1011 HOH A O 1 HETATM 10145 O O . HOH KA 8 . ? 38.499 -6.092 28.015 1.00 29.82 ? 1012 HOH A O 1 HETATM 10146 O O . HOH KA 8 . ? 5.514 -23.068 23.781 1.00 36.91 ? 1013 HOH A O 1 HETATM 10147 O O . HOH KA 8 . ? -25.599 4.317 38.422 1.00 59.49 ? 1014 HOH A O 1 HETATM 10148 O O . HOH KA 8 . ? 32.908 20.224 28.479 1.00 50.45 ? 1015 HOH A O 1 HETATM 10149 O O . HOH KA 8 . ? 22.958 -11.479 19.629 1.00 48.33 ? 1016 HOH A O 1 HETATM 10150 O O . HOH KA 8 . ? 14.460 -4.803 62.530 1.00 37.76 ? 1017 HOH A O 1 HETATM 10151 O O . HOH KA 8 . ? 39.937 -3.416 20.946 1.00 39.82 ? 1018 HOH A O 1 HETATM 10152 O O . HOH KA 8 . ? 25.900 10.977 14.378 1.00 34.08 ? 1019 HOH A O 1 HETATM 10153 O O . HOH KA 8 . ? -9.781 -10.022 11.538 1.00 35.31 ? 1020 HOH A O 1 HETATM 10154 O O . HOH KA 8 . ? 21.374 9.581 17.559 1.00 22.69 ? 1021 HOH A O 1 HETATM 10155 O O . HOH KA 8 . ? -13.042 -0.333 45.652 1.00 28.64 ? 1022 HOH A O 1 HETATM 10156 O O . HOH KA 8 . ? -17.903 2.633 26.993 1.00 38.13 ? 1023 HOH A O 1 HETATM 10157 O O . HOH KA 8 . ? 20.777 -1.478 3.617 1.00 41.35 ? 1024 HOH A O 1 HETATM 10158 O O . HOH KA 8 . ? -10.358 14.784 17.002 1.00 50.48 ? 1025 HOH A O 1 HETATM 10159 O O . HOH KA 8 . ? -18.370 -12.187 32.061 1.00 41.50 ? 1026 HOH A O 1 HETATM 10160 O O . HOH KA 8 . ? 26.779 10.386 42.811 1.00 25.59 ? 1027 HOH A O 1 HETATM 10161 O O . HOH KA 8 . ? 32.419 -15.363 36.952 1.00 51.05 ? 1028 HOH A O 1 HETATM 10162 O O . HOH KA 8 . ? 6.390 16.227 40.825 1.00 43.53 ? 1029 HOH A O 1 HETATM 10163 O O . HOH KA 8 . ? -19.013 -22.659 20.129 1.00 30.88 ? 1030 HOH A O 1 HETATM 10164 O O . HOH KA 8 . ? -10.632 -19.167 34.918 1.00 36.09 ? 1031 HOH A O 1 HETATM 10165 O O . HOH KA 8 . ? 34.810 3.830 21.481 1.00 40.73 ? 1032 HOH A O 1 HETATM 10166 O O . HOH KA 8 . ? 6.102 -20.538 39.342 1.00 36.02 ? 1033 HOH A O 1 HETATM 10167 O O . HOH KA 8 . ? 19.119 -13.661 36.169 1.00 31.53 ? 1034 HOH A O 1 HETATM 10168 O O . HOH KA 8 . ? -12.637 -14.176 37.605 1.00 35.61 ? 1035 HOH A O 1 HETATM 10169 O O . HOH KA 8 . ? 23.179 16.059 15.438 1.00 55.54 ? 1036 HOH A O 1 HETATM 10170 O O . HOH KA 8 . ? -5.693 -11.649 9.528 1.00 38.96 ? 1037 HOH A O 1 HETATM 10171 O O . HOH KA 8 . ? 22.377 16.305 27.283 1.00 31.39 ? 1038 HOH A O 1 HETATM 10172 O O . HOH KA 8 . ? 11.870 16.765 36.242 1.00 56.14 ? 1039 HOH A O 1 HETATM 10173 O O . HOH KA 8 . ? -3.199 -21.298 18.039 1.00 44.60 ? 1040 HOH A O 1 HETATM 10174 O O . HOH KA 8 . ? 2.233 6.395 12.352 1.00 32.76 ? 1041 HOH A O 1 HETATM 10175 O O . HOH KA 8 . ? -24.669 4.720 45.897 1.00 54.61 ? 1042 HOH A O 1 HETATM 10176 O O . HOH KA 8 . ? 25.949 22.716 42.276 1.00 29.26 ? 1043 HOH A O 1 HETATM 10177 O O . HOH KA 8 . ? 19.128 6.577 54.395 1.00 45.74 ? 1044 HOH A O 1 HETATM 10178 O O . HOH KA 8 . ? -23.835 1.748 34.181 1.00 45.08 ? 1045 HOH A O 1 HETATM 10179 O O . HOH KA 8 . ? -0.639 -1.728 7.726 1.00 41.97 ? 1046 HOH A O 1 HETATM 10180 O O . HOH KA 8 . ? -9.911 -15.055 44.286 1.00 31.16 ? 1047 HOH A O 1 HETATM 10181 O O . HOH KA 8 . ? -11.783 -13.707 9.431 1.00 36.99 ? 1048 HOH A O 1 HETATM 10182 O O . HOH KA 8 . ? 0.274 11.583 31.165 1.00 45.49 ? 1049 HOH A O 1 HETATM 10183 O O . HOH KA 8 . ? 1.165 12.480 59.435 1.00 41.68 ? 1050 HOH A O 1 HETATM 10184 O O . HOH KA 8 . ? -20.494 12.196 24.014 1.00 27.53 ? 1051 HOH A O 1 HETATM 10185 O O . HOH KA 8 . ? 1.946 17.391 17.184 1.00 36.30 ? 1052 HOH A O 1 HETATM 10186 O O . HOH KA 8 . ? -8.035 12.766 13.240 1.00 41.09 ? 1053 HOH A O 1 HETATM 10187 O O . HOH KA 8 . ? -21.143 -11.320 32.030 1.00 44.36 ? 1054 HOH A O 1 HETATM 10188 O O . HOH KA 8 . ? 17.975 -4.854 61.874 1.00 49.51 ? 1055 HOH A O 1 HETATM 10189 O O . HOH KA 8 . ? 23.335 -6.913 52.659 1.00 36.19 ? 1056 HOH A O 1 HETATM 10190 O O . HOH KA 8 . ? 12.338 -9.419 2.108 1.00 63.59 ? 1057 HOH A O 1 HETATM 10191 O O . HOH KA 8 . ? 16.964 18.811 45.413 1.00 31.51 ? 1058 HOH A O 1 HETATM 10192 O O . HOH KA 8 . ? -0.892 1.085 9.104 1.00 31.20 ? 1059 HOH A O 1 HETATM 10193 O O . HOH KA 8 . ? -9.741 -3.746 46.924 1.00 26.49 ? 1060 HOH A O 1 HETATM 10194 O O . HOH KA 8 . ? 0.241 -20.668 14.151 1.00 53.71 ? 1061 HOH A O 1 HETATM 10195 O O . HOH KA 8 . ? 22.736 -5.581 7.538 1.00 47.10 ? 1062 HOH A O 1 HETATM 10196 O O . HOH KA 8 . ? -23.413 6.816 10.729 1.00 60.92 ? 1063 HOH A O 1 HETATM 10197 O O . HOH KA 8 . ? -1.304 5.749 27.011 1.00 49.11 ? 1064 HOH A O 1 HETATM 10198 O O . HOH KA 8 . ? -14.138 -2.667 44.449 1.00 31.14 ? 1065 HOH A O 1 HETATM 10199 O O . HOH KA 8 . ? 27.291 -11.523 34.269 1.00 45.44 ? 1066 HOH A O 1 HETATM 10200 O O . HOH KA 8 . ? 36.524 -8.120 34.714 1.00 38.24 ? 1067 HOH A O 1 HETATM 10201 O O . HOH KA 8 . ? -7.818 13.622 15.840 1.00 34.10 ? 1068 HOH A O 1 HETATM 10202 O O . HOH KA 8 . ? 9.034 9.407 13.414 1.00 22.21 ? 1069 HOH A O 1 HETATM 10203 O O . HOH KA 8 . ? 4.665 -16.140 12.552 1.00 57.47 ? 1070 HOH A O 1 HETATM 10204 O O . HOH KA 8 . ? 13.141 18.615 21.082 1.00 51.95 ? 1071 HOH A O 1 HETATM 10205 O O . HOH KA 8 . ? 18.206 -20.352 51.490 1.00 50.92 ? 1072 HOH A O 1 HETATM 10206 O O . HOH KA 8 . ? -0.590 17.133 43.489 1.00 35.77 ? 1073 HOH A O 1 HETATM 10207 O O . HOH KA 8 . ? 30.670 4.090 44.281 1.00 47.23 ? 1074 HOH A O 1 HETATM 10208 O O . HOH KA 8 . ? -11.641 -25.805 25.516 1.00 43.33 ? 1075 HOH A O 1 HETATM 10209 O O . HOH KA 8 . ? -22.426 -14.377 23.670 1.00 43.26 ? 1076 HOH A O 1 HETATM 10210 O O . HOH KA 8 . ? 28.530 -2.043 35.592 1.00 27.92 ? 1077 HOH A O 1 HETATM 10211 O O . HOH KA 8 . ? 24.909 1.371 55.401 1.00 40.19 ? 1078 HOH A O 1 HETATM 10212 O O . HOH KA 8 . ? -7.641 18.400 16.002 1.00 52.72 ? 1079 HOH A O 1 HETATM 10213 O O . HOH KA 8 . ? 29.293 2.800 14.055 1.00 48.00 ? 1080 HOH A O 1 HETATM 10214 O O . HOH KA 8 . ? -0.547 8.304 34.766 1.00 43.03 ? 1081 HOH A O 1 HETATM 10215 O O . HOH KA 8 . ? 8.880 15.716 58.693 1.00 39.99 ? 1082 HOH A O 1 HETATM 10216 O O . HOH KA 8 . ? 36.564 0.993 37.732 1.00 49.96 ? 1083 HOH A O 1 HETATM 10217 O O . HOH KA 8 . ? 0.768 7.540 37.008 1.00 35.62 ? 1084 HOH A O 1 HETATM 10218 O O . HOH KA 8 . ? 3.839 10.126 36.652 1.00 48.52 ? 1085 HOH A O 1 HETATM 10219 O O . HOH KA 8 . ? 0.515 18.796 47.851 1.00 35.46 ? 1086 HOH A O 1 HETATM 10220 O O . HOH KA 8 . ? -11.165 -8.750 13.195 1.00 35.11 ? 1087 HOH A O 1 HETATM 10221 O O . HOH KA 8 . ? 34.682 13.179 41.549 1.00 42.05 ? 1088 HOH A O 1 HETATM 10222 O O . HOH KA 8 . ? -18.774 -24.120 17.706 1.00 43.47 ? 1089 HOH A O 1 HETATM 10223 O O . HOH KA 8 . ? 22.571 -22.509 52.360 1.00 49.96 ? 1090 HOH A O 1 HETATM 10224 O O . HOH KA 8 . ? -1.989 4.920 51.318 1.00 39.86 ? 1091 HOH A O 1 HETATM 10225 O O . HOH KA 8 . ? 27.750 15.030 43.119 1.00 32.12 ? 1092 HOH A O 1 HETATM 10226 O O . HOH KA 8 . ? 29.200 -1.725 50.571 1.00 30.31 ? 1093 HOH A O 1 HETATM 10227 O O . HOH KA 8 . ? 1.650 -11.802 47.693 1.00 32.42 ? 1094 HOH A O 1 HETATM 10228 O O . HOH KA 8 . ? -8.368 -5.174 48.661 1.00 36.60 ? 1095 HOH A O 1 HETATM 10229 O O . HOH KA 8 . ? 19.775 -14.279 60.189 1.00 35.36 ? 1096 HOH A O 1 HETATM 10230 O O . HOH KA 8 . ? 11.381 11.015 59.853 1.00 43.28 ? 1097 HOH A O 1 HETATM 10231 O O . HOH KA 8 . ? -8.279 -11.752 7.959 1.00 50.69 ? 1098 HOH A O 1 HETATM 10232 O O . HOH KA 8 . ? -5.400 -23.065 18.890 1.00 49.56 ? 1099 HOH A O 1 HETATM 10233 O O . HOH KA 8 . ? -6.064 -4.698 10.259 1.00 41.38 ? 1100 HOH A O 1 HETATM 10234 O O . HOH KA 8 . ? 5.853 13.787 39.353 1.00 51.21 ? 1101 HOH A O 1 HETATM 10235 O O . HOH KA 8 . ? -5.756 4.819 9.001 1.00 27.05 ? 1102 HOH A O 1 HETATM 10236 O O . HOH KA 8 . ? -22.113 -5.301 27.946 1.00 53.56 ? 1103 HOH A O 1 HETATM 10237 O O . HOH KA 8 . ? 13.079 0.577 61.184 1.00 48.16 ? 1104 HOH A O 1 HETATM 10238 O O . HOH KA 8 . ? -19.207 4.232 28.853 1.00 22.38 ? 1105 HOH A O 1 HETATM 10239 O O . HOH KA 8 . ? -4.936 7.232 5.408 1.00 49.73 ? 1106 HOH A O 1 HETATM 10240 O O . HOH KA 8 . ? -2.343 7.331 8.781 1.00 37.56 ? 1107 HOH A O 1 HETATM 10241 O O . HOH KA 8 . ? -1.349 12.718 10.928 1.00 50.74 ? 1108 HOH A O 1 HETATM 10242 O O . HOH KA 8 . ? 21.334 -15.506 58.208 1.00 46.95 ? 1109 HOH A O 1 HETATM 10243 O O . HOH KA 8 . ? 1.544 -21.832 23.323 1.00 44.53 ? 1110 HOH A O 1 HETATM 10244 O O . HOH KA 8 . ? 19.581 19.589 40.545 1.00 36.34 ? 1111 HOH A O 1 HETATM 10245 O O . HOH KA 8 . ? 35.463 13.487 39.035 1.00 30.96 ? 1112 HOH A O 1 HETATM 10246 O O . HOH KA 8 . ? 3.353 11.706 11.867 1.00 36.74 ? 1113 HOH A O 1 HETATM 10247 O O . HOH KA 8 . ? 1.724 13.984 31.866 1.00 60.18 ? 1114 HOH A O 1 HETATM 10248 O O . HOH KA 8 . ? 37.863 14.845 39.834 1.00 39.74 ? 1115 HOH A O 1 HETATM 10249 O O . HOH LA 8 . ? 23.494 36.448 9.331 1.00 19.63 ? 701 HOH B O 1 HETATM 10250 O O . HOH LA 8 . ? 40.054 63.248 8.291 1.00 42.38 ? 702 HOH B O 1 HETATM 10251 O O . HOH LA 8 . ? 24.066 40.481 -22.098 1.00 31.71 ? 703 HOH B O 1 HETATM 10252 O O . HOH LA 8 . ? 37.831 32.836 26.742 1.00 37.36 ? 704 HOH B O 1 HETATM 10253 O O . HOH LA 8 . ? 45.475 46.821 -12.940 1.00 42.31 ? 705 HOH B O 1 HETATM 10254 O O . HOH LA 8 . ? 17.507 41.655 25.754 1.00 24.35 ? 706 HOH B O 1 HETATM 10255 O O . HOH LA 8 . ? 39.775 37.363 27.888 1.00 33.17 ? 707 HOH B O 1 HETATM 10256 O O . HOH LA 8 . ? 42.738 39.114 -8.648 1.00 22.74 ? 708 HOH B O 1 HETATM 10257 O O . HOH LA 8 . ? 27.188 52.512 -5.819 1.00 24.40 ? 709 HOH B O 1 HETATM 10258 O O . HOH LA 8 . ? 21.962 35.246 -13.838 1.00 20.54 ? 710 HOH B O 1 HETATM 10259 O O . HOH LA 8 . ? 36.931 63.606 -6.573 1.00 43.22 ? 711 HOH B O 1 HETATM 10260 O O . HOH LA 8 . ? 20.048 35.684 2.313 1.00 33.10 ? 712 HOH B O 1 HETATM 10261 O O . HOH LA 8 . ? 22.443 21.618 34.621 1.00 39.46 ? 713 HOH B O 1 HETATM 10262 O O . HOH LA 8 . ? 30.975 34.402 20.869 1.00 29.49 ? 714 HOH B O 1 HETATM 10263 O O . HOH LA 8 . ? 7.572 38.149 -6.174 1.00 29.75 ? 715 HOH B O 1 HETATM 10264 O O . HOH LA 8 . ? 38.691 31.364 15.209 1.00 28.16 ? 716 HOH B O 1 HETATM 10265 O O . HOH LA 8 . ? 52.700 32.922 25.923 1.00 50.99 ? 717 HOH B O 1 HETATM 10266 O O . HOH LA 8 . ? 47.982 40.861 29.355 1.00 33.77 ? 718 HOH B O 1 HETATM 10267 O O . HOH LA 8 . ? 7.726 31.801 -0.719 1.00 30.63 ? 719 HOH B O 1 HETATM 10268 O O . HOH LA 8 . ? 58.190 31.431 0.665 1.00 33.66 ? 720 HOH B O 1 HETATM 10269 O O . HOH LA 8 . ? 34.183 17.744 23.945 1.00 47.65 ? 721 HOH B O 1 HETATM 10270 O O . HOH LA 8 . ? 49.652 50.419 4.032 1.00 35.83 ? 722 HOH B O 1 HETATM 10271 O O . HOH LA 8 . ? 27.270 30.650 -8.439 1.00 22.67 ? 723 HOH B O 1 HETATM 10272 O O . HOH LA 8 . ? 3.714 51.844 26.877 1.00 28.18 ? 724 HOH B O 1 HETATM 10273 O O . HOH LA 8 . ? 42.815 43.998 25.458 1.00 27.41 ? 725 HOH B O 1 HETATM 10274 O O . HOH LA 8 . ? 17.838 34.458 7.184 1.00 34.93 ? 726 HOH B O 1 HETATM 10275 O O . HOH LA 8 . ? 24.588 54.315 7.830 1.00 17.49 ? 727 HOH B O 1 HETATM 10276 O O . HOH LA 8 . ? -0.120 45.790 10.896 1.00 25.88 ? 728 HOH B O 1 HETATM 10277 O O . HOH LA 8 . ? 48.332 25.201 6.958 1.00 47.27 ? 729 HOH B O 1 HETATM 10278 O O . HOH LA 8 . ? 19.053 34.271 13.923 1.00 41.93 ? 730 HOH B O 1 HETATM 10279 O O . HOH LA 8 . ? 17.847 29.637 25.996 1.00 23.60 ? 731 HOH B O 1 HETATM 10280 O O . HOH LA 8 . ? 33.626 31.713 12.256 1.00 25.69 ? 732 HOH B O 1 HETATM 10281 O O . HOH LA 8 . ? 38.460 33.732 -12.693 1.00 40.56 ? 733 HOH B O 1 HETATM 10282 O O . HOH LA 8 . ? 25.448 46.604 30.800 1.00 43.28 ? 734 HOH B O 1 HETATM 10283 O O . HOH LA 8 . ? 21.727 36.220 11.100 1.00 24.39 ? 735 HOH B O 1 HETATM 10284 O O . HOH LA 8 . ? 33.436 28.354 12.162 1.00 44.32 ? 736 HOH B O 1 HETATM 10285 O O . HOH LA 8 . ? 47.896 46.622 4.734 1.00 28.87 ? 737 HOH B O 1 HETATM 10286 O O . HOH LA 8 . ? 14.664 31.844 18.808 1.00 14.54 ? 738 HOH B O 1 HETATM 10287 O O . HOH LA 8 . ? 48.788 42.997 2.401 1.00 29.38 ? 739 HOH B O 1 HETATM 10288 O O . HOH LA 8 . ? 43.055 43.300 -13.239 1.00 27.41 ? 740 HOH B O 1 HETATM 10289 O O . HOH LA 8 . ? 9.763 39.462 21.413 1.00 14.75 ? 741 HOH B O 1 HETATM 10290 O O . HOH LA 8 . ? 48.825 45.435 -7.311 1.00 26.41 ? 742 HOH B O 1 HETATM 10291 O O . HOH LA 8 . ? 11.108 19.733 11.804 1.00 54.32 ? 743 HOH B O 1 HETATM 10292 O O . HOH LA 8 . ? 47.255 32.347 15.364 1.00 27.48 ? 744 HOH B O 1 HETATM 10293 O O . HOH LA 8 . ? 42.845 19.926 5.923 1.00 44.25 ? 745 HOH B O 1 HETATM 10294 O O . HOH LA 8 . ? -1.070 37.814 4.252 1.00 23.88 ? 746 HOH B O 1 HETATM 10295 O O . HOH LA 8 . ? 41.907 27.391 9.789 1.00 31.80 ? 747 HOH B O 1 HETATM 10296 O O . HOH LA 8 . ? 39.583 22.755 -5.891 1.00 41.21 ? 748 HOH B O 1 HETATM 10297 O O . HOH LA 8 . ? 34.461 55.761 -4.256 1.00 26.22 ? 749 HOH B O 1 HETATM 10298 O O . HOH LA 8 . ? 15.005 67.983 17.033 1.00 44.19 ? 750 HOH B O 1 HETATM 10299 O O . HOH LA 8 . ? 6.816 24.776 10.068 1.00 46.75 ? 751 HOH B O 1 HETATM 10300 O O . HOH LA 8 . ? 6.976 34.445 -0.008 1.00 21.84 ? 752 HOH B O 1 HETATM 10301 O O . HOH LA 8 . ? 35.266 60.223 14.530 1.00 38.48 ? 753 HOH B O 1 HETATM 10302 O O . HOH LA 8 . ? 43.471 52.785 2.343 1.00 33.39 ? 754 HOH B O 1 HETATM 10303 O O . HOH LA 8 . ? 19.307 24.284 10.874 1.00 43.35 ? 755 HOH B O 1 HETATM 10304 O O . HOH LA 8 . ? 47.876 25.622 -4.877 1.00 38.67 ? 756 HOH B O 1 HETATM 10305 O O . HOH LA 8 . ? 27.464 50.287 -9.543 1.00 23.12 ? 757 HOH B O 1 HETATM 10306 O O . HOH LA 8 . ? 1.652 36.037 14.274 1.00 19.37 ? 758 HOH B O 1 HETATM 10307 O O . HOH LA 8 . ? 29.138 32.241 21.788 1.00 50.58 ? 759 HOH B O 1 HETATM 10308 O O . HOH LA 8 . ? 36.667 35.494 -16.458 1.00 33.42 ? 760 HOH B O 1 HETATM 10309 O O . HOH LA 8 . ? 6.565 33.516 -6.427 1.00 43.85 ? 761 HOH B O 1 HETATM 10310 O O . HOH LA 8 . ? 13.746 44.228 29.546 1.00 23.82 ? 762 HOH B O 1 HETATM 10311 O O . HOH LA 8 . ? 44.506 58.791 -2.384 1.00 45.27 ? 763 HOH B O 1 HETATM 10312 O O . HOH LA 8 . ? 15.981 50.160 -7.057 1.00 27.00 ? 764 HOH B O 1 HETATM 10313 O O . HOH LA 8 . ? 3.809 56.202 24.531 1.00 29.57 ? 765 HOH B O 1 HETATM 10314 O O . HOH LA 8 . ? 17.516 61.228 6.055 1.00 24.04 ? 766 HOH B O 1 HETATM 10315 O O . HOH LA 8 . ? 27.035 52.752 -10.952 1.00 29.87 ? 767 HOH B O 1 HETATM 10316 O O . HOH LA 8 . ? 32.114 39.868 -11.702 1.00 20.90 ? 768 HOH B O 1 HETATM 10317 O O . HOH LA 8 . ? 30.201 30.538 1.204 1.00 30.60 ? 769 HOH B O 1 HETATM 10318 O O . HOH LA 8 . ? 30.959 35.791 5.855 1.00 15.68 ? 770 HOH B O 1 HETATM 10319 O O . HOH LA 8 . ? 29.567 49.620 7.098 1.00 13.78 ? 771 HOH B O 1 HETATM 10320 O O . HOH LA 8 . ? 20.868 31.430 17.382 1.00 30.49 ? 772 HOH B O 1 HETATM 10321 O O . HOH LA 8 . ? 41.016 27.599 2.784 1.00 35.38 ? 773 HOH B O 1 HETATM 10322 O O . HOH LA 8 . ? 37.861 51.929 26.852 1.00 38.59 ? 774 HOH B O 1 HETATM 10323 O O . HOH LA 8 . ? 10.726 47.476 25.834 1.00 21.50 ? 775 HOH B O 1 HETATM 10324 O O . HOH LA 8 . ? 13.977 25.039 26.326 1.00 51.02 ? 776 HOH B O 1 HETATM 10325 O O . HOH LA 8 . ? 37.804 54.323 -2.359 1.00 29.45 ? 777 HOH B O 1 HETATM 10326 O O . HOH LA 8 . ? 42.840 29.150 -6.883 1.00 25.21 ? 778 HOH B O 1 HETATM 10327 O O . HOH LA 8 . ? 20.911 30.111 10.042 1.00 32.11 ? 779 HOH B O 1 HETATM 10328 O O . HOH LA 8 . ? 44.979 35.988 16.768 1.00 27.35 ? 780 HOH B O 1 HETATM 10329 O O . HOH LA 8 . ? 12.449 63.245 23.607 1.00 35.60 ? 781 HOH B O 1 HETATM 10330 O O . HOH LA 8 . ? 2.696 48.357 18.849 1.00 15.18 ? 782 HOH B O 1 HETATM 10331 O O . HOH LA 8 . ? 16.363 44.599 -10.138 1.00 26.56 ? 783 HOH B O 1 HETATM 10332 O O . HOH LA 8 . ? 11.159 29.626 -2.459 1.00 40.24 ? 784 HOH B O 1 HETATM 10333 O O . HOH LA 8 . ? 30.782 56.865 -8.125 1.00 27.94 ? 785 HOH B O 1 HETATM 10334 O O . HOH LA 8 . ? 28.192 25.407 -2.622 1.00 21.19 ? 786 HOH B O 1 HETATM 10335 O O . HOH LA 8 . ? 12.617 38.334 30.694 1.00 36.36 ? 787 HOH B O 1 HETATM 10336 O O . HOH LA 8 . ? 5.810 46.591 -0.992 1.00 20.29 ? 788 HOH B O 1 HETATM 10337 O O . HOH LA 8 . ? 21.405 38.167 15.281 1.00 17.21 ? 789 HOH B O 1 HETATM 10338 O O . HOH LA 8 . ? 26.750 55.083 4.023 1.00 19.88 ? 790 HOH B O 1 HETATM 10339 O O . HOH LA 8 . ? 40.585 43.529 -14.449 1.00 43.14 ? 791 HOH B O 1 HETATM 10340 O O . HOH LA 8 . ? 40.485 39.647 -11.731 1.00 27.97 ? 792 HOH B O 1 HETATM 10341 O O . HOH LA 8 . ? 12.784 45.923 19.770 1.00 14.58 ? 793 HOH B O 1 HETATM 10342 O O . HOH LA 8 . ? 38.636 41.073 20.047 1.00 28.40 ? 794 HOH B O 1 HETATM 10343 O O . HOH LA 8 . ? 34.872 50.203 31.731 1.00 51.74 ? 795 HOH B O 1 HETATM 10344 O O . HOH LA 8 . ? 4.497 33.874 31.375 1.00 43.52 ? 796 HOH B O 1 HETATM 10345 O O . HOH LA 8 . ? 10.299 56.739 5.821 1.00 22.54 ? 797 HOH B O 1 HETATM 10346 O O . HOH LA 8 . ? 39.686 33.021 19.112 1.00 34.99 ? 798 HOH B O 1 HETATM 10347 O O . HOH LA 8 . ? 52.703 36.941 14.385 1.00 54.90 ? 799 HOH B O 1 HETATM 10348 O O . HOH LA 8 . ? 13.553 25.081 2.882 1.00 42.72 ? 800 HOH B O 1 HETATM 10349 O O . HOH LA 8 . ? 37.791 62.080 -3.020 1.00 46.91 ? 801 HOH B O 1 HETATM 10350 O O . HOH LA 8 . ? 15.440 51.080 29.763 1.00 38.93 ? 802 HOH B O 1 HETATM 10351 O O . HOH LA 8 . ? 36.237 57.158 -10.817 1.00 39.20 ? 803 HOH B O 1 HETATM 10352 O O . HOH LA 8 . ? 18.576 61.609 20.235 1.00 24.22 ? 804 HOH B O 1 HETATM 10353 O O . HOH LA 8 . ? 5.336 40.255 11.005 1.00 13.96 ? 805 HOH B O 1 HETATM 10354 O O . HOH LA 8 . ? 8.933 24.295 12.860 1.00 32.24 ? 806 HOH B O 1 HETATM 10355 O O . HOH LA 8 . ? 5.550 39.838 14.426 1.00 14.00 ? 807 HOH B O 1 HETATM 10356 O O . HOH LA 8 . ? 19.845 49.529 1.155 1.00 16.03 ? 808 HOH B O 1 HETATM 10357 O O . HOH LA 8 . ? 33.296 57.869 -5.748 1.00 41.56 ? 809 HOH B O 1 HETATM 10358 O O . HOH LA 8 . ? 11.534 43.776 18.708 1.00 13.47 ? 810 HOH B O 1 HETATM 10359 O O . HOH LA 8 . ? -2.287 35.710 -2.133 1.00 37.31 ? 811 HOH B O 1 HETATM 10360 O O . HOH LA 8 . ? 30.318 48.564 -7.594 1.00 20.31 ? 812 HOH B O 1 HETATM 10361 O O . HOH LA 8 . ? 28.552 34.469 23.658 1.00 27.33 ? 813 HOH B O 1 HETATM 10362 O O . HOH LA 8 . ? 2.997 34.819 11.747 1.00 27.81 ? 814 HOH B O 1 HETATM 10363 O O . HOH LA 8 . ? 42.070 58.475 -0.763 1.00 31.83 ? 815 HOH B O 1 HETATM 10364 O O . HOH LA 8 . ? 14.786 50.889 -3.942 1.00 17.74 ? 816 HOH B O 1 HETATM 10365 O O . HOH LA 8 . ? 31.815 29.381 3.862 1.00 26.69 ? 817 HOH B O 1 HETATM 10366 O O . HOH LA 8 . ? 19.540 36.774 13.657 1.00 44.47 ? 818 HOH B O 1 HETATM 10367 O O . HOH LA 8 . ? 33.717 34.426 12.062 1.00 26.10 ? 819 HOH B O 1 HETATM 10368 O O . HOH LA 8 . ? 39.492 40.558 -15.431 1.00 30.56 ? 820 HOH B O 1 HETATM 10369 O O . HOH LA 8 . ? 24.602 55.943 5.666 1.00 18.70 ? 821 HOH B O 1 HETATM 10370 O O . HOH LA 8 . ? 35.069 40.702 21.822 1.00 36.63 ? 822 HOH B O 1 HETATM 10371 O O . HOH LA 8 . ? 28.930 63.795 22.177 1.00 56.68 ? 823 HOH B O 1 HETATM 10372 O O . HOH LA 8 . ? 28.045 49.934 -6.746 1.00 17.34 ? 824 HOH B O 1 HETATM 10373 O O . HOH LA 8 . ? 15.271 32.138 -1.942 1.00 16.34 ? 825 HOH B O 1 HETATM 10374 O O . HOH LA 8 . ? 29.005 30.950 9.948 1.00 37.00 ? 826 HOH B O 1 HETATM 10375 O O . HOH LA 8 . ? 28.779 35.570 -3.727 1.00 21.70 ? 827 HOH B O 1 HETATM 10376 O O . HOH LA 8 . ? -10.713 35.165 19.549 1.00 52.58 ? 828 HOH B O 1 HETATM 10377 O O . HOH LA 8 . ? 24.811 58.414 21.890 1.00 37.01 ? 829 HOH B O 1 HETATM 10378 O O . HOH LA 8 . ? 18.193 62.233 24.511 1.00 29.05 ? 830 HOH B O 1 HETATM 10379 O O . HOH LA 8 . ? 22.171 60.464 -0.255 1.00 31.87 ? 831 HOH B O 1 HETATM 10380 O O . HOH LA 8 . ? 4.775 40.777 8.268 1.00 17.30 ? 832 HOH B O 1 HETATM 10381 O O . HOH LA 8 . ? 38.715 29.566 2.541 1.00 22.71 ? 833 HOH B O 1 HETATM 10382 O O . HOH LA 8 . ? 10.698 50.328 24.791 1.00 20.98 ? 834 HOH B O 1 HETATM 10383 O O . HOH LA 8 . ? 21.364 54.113 10.556 1.00 31.19 ? 835 HOH B O 1 HETATM 10384 O O . HOH LA 8 . ? 10.003 27.466 4.874 1.00 42.57 ? 836 HOH B O 1 HETATM 10385 O O . HOH LA 8 . ? 41.811 29.175 32.519 1.00 52.17 ? 837 HOH B O 1 HETATM 10386 O O . HOH LA 8 . ? 12.693 60.794 28.533 1.00 31.80 ? 838 HOH B O 1 HETATM 10387 O O . HOH LA 8 . ? 28.107 36.675 21.858 1.00 18.74 ? 839 HOH B O 1 HETATM 10388 O O . HOH LA 8 . ? 26.104 28.537 -10.559 1.00 18.82 ? 840 HOH B O 1 HETATM 10389 O O . HOH LA 8 . ? 28.516 41.999 26.413 1.00 26.37 ? 841 HOH B O 1 HETATM 10390 O O . HOH LA 8 . ? 10.256 42.005 20.768 1.00 18.25 ? 842 HOH B O 1 HETATM 10391 O O . HOH LA 8 . ? 20.687 55.605 16.371 1.00 15.91 ? 843 HOH B O 1 HETATM 10392 O O . HOH LA 8 . ? 32.032 46.748 -7.403 1.00 19.57 ? 844 HOH B O 1 HETATM 10393 O O . HOH LA 8 . ? -3.209 43.943 6.394 1.00 31.93 ? 845 HOH B O 1 HETATM 10394 O O . HOH LA 8 . ? 23.359 25.057 24.523 1.00 58.12 ? 846 HOH B O 1 HETATM 10395 O O . HOH LA 8 . ? 27.423 33.334 26.902 1.00 26.83 ? 847 HOH B O 1 HETATM 10396 O O . HOH LA 8 . ? 21.320 35.702 -7.226 1.00 15.22 ? 848 HOH B O 1 HETATM 10397 O O . HOH LA 8 . ? 1.116 41.591 13.883 1.00 37.48 ? 849 HOH B O 1 HETATM 10398 O O . HOH LA 8 . ? 34.620 40.293 -12.611 1.00 22.48 ? 850 HOH B O 1 HETATM 10399 O O . HOH LA 8 . ? 43.179 39.190 16.379 1.00 30.17 ? 851 HOH B O 1 HETATM 10400 O O . HOH LA 8 . ? 20.282 62.547 15.963 1.00 38.39 ? 852 HOH B O 1 HETATM 10401 O O . HOH LA 8 . ? 15.353 47.606 -6.799 1.00 25.15 ? 853 HOH B O 1 HETATM 10402 O O . HOH LA 8 . ? 46.960 16.197 3.338 1.00 51.60 ? 854 HOH B O 1 HETATM 10403 O O . HOH LA 8 . ? 48.360 34.510 -1.779 1.00 26.34 ? 855 HOH B O 1 HETATM 10404 O O . HOH LA 8 . ? 41.801 31.852 22.974 1.00 38.60 ? 856 HOH B O 1 HETATM 10405 O O . HOH LA 8 . ? 22.871 51.928 31.471 1.00 29.96 ? 857 HOH B O 1 HETATM 10406 O O . HOH LA 8 . ? -4.975 41.722 -10.340 1.00 37.76 ? 858 HOH B O 1 HETATM 10407 O O . HOH LA 8 . ? 12.659 49.781 -1.098 1.00 17.42 ? 859 HOH B O 1 HETATM 10408 O O . HOH LA 8 . ? 18.537 25.682 19.078 1.00 29.25 ? 860 HOH B O 1 HETATM 10409 O O . HOH LA 8 . ? 30.850 40.277 -19.049 1.00 34.42 ? 861 HOH B O 1 HETATM 10410 O O . HOH LA 8 . ? 5.968 22.068 -4.020 1.00 54.12 ? 862 HOH B O 1 HETATM 10411 O O . HOH LA 8 . ? 21.525 52.462 -4.730 1.00 22.20 ? 863 HOH B O 1 HETATM 10412 O O . HOH LA 8 . ? 7.975 42.165 -4.905 1.00 26.55 ? 864 HOH B O 1 HETATM 10413 O O . HOH LA 8 . ? -0.955 48.766 16.581 1.00 47.21 ? 865 HOH B O 1 HETATM 10414 O O . HOH LA 8 . ? 13.504 50.941 -7.698 1.00 42.09 ? 866 HOH B O 1 HETATM 10415 O O . HOH LA 8 . ? 42.569 51.005 5.386 1.00 26.45 ? 867 HOH B O 1 HETATM 10416 O O . HOH LA 8 . ? 1.966 34.181 25.311 1.00 22.48 ? 868 HOH B O 1 HETATM 10417 O O . HOH LA 8 . ? 8.415 53.536 2.666 1.00 21.26 ? 869 HOH B O 1 HETATM 10418 O O . HOH LA 8 . ? 12.885 49.257 29.945 1.00 33.06 ? 870 HOH B O 1 HETATM 10419 O O . HOH LA 8 . ? 48.365 42.139 6.702 1.00 29.52 ? 871 HOH B O 1 HETATM 10420 O O . HOH LA 8 . ? 31.820 27.957 6.619 1.00 34.28 ? 872 HOH B O 1 HETATM 10421 O O . HOH LA 8 . ? 48.172 38.968 31.609 1.00 55.47 ? 873 HOH B O 1 HETATM 10422 O O . HOH LA 8 . ? 20.765 36.046 24.339 1.00 26.68 ? 874 HOH B O 1 HETATM 10423 O O . HOH LA 8 . ? 8.016 47.742 24.821 1.00 26.37 ? 875 HOH B O 1 HETATM 10424 O O . HOH LA 8 . ? 28.894 63.067 3.771 1.00 39.54 ? 876 HOH B O 1 HETATM 10425 O O . HOH LA 8 . ? 51.699 25.958 23.564 1.00 49.25 ? 877 HOH B O 1 HETATM 10426 O O . HOH LA 8 . ? 13.494 34.330 5.768 1.00 40.99 ? 878 HOH B O 1 HETATM 10427 O O . HOH LA 8 . ? 45.814 38.350 16.355 1.00 29.24 ? 879 HOH B O 1 HETATM 10428 O O . HOH LA 8 . ? 40.694 32.912 14.212 1.00 31.16 ? 880 HOH B O 1 HETATM 10429 O O . HOH LA 8 . ? -1.285 56.039 20.179 1.00 38.81 ? 881 HOH B O 1 HETATM 10430 O O . HOH LA 8 . ? -4.974 42.381 0.006 1.00 41.03 ? 882 HOH B O 1 HETATM 10431 O O . HOH LA 8 . ? 22.550 33.784 -11.764 1.00 32.03 ? 883 HOH B O 1 HETATM 10432 O O . HOH LA 8 . ? 24.942 51.448 -6.925 1.00 28.29 ? 884 HOH B O 1 HETATM 10433 O O . HOH LA 8 . ? 3.658 37.996 10.253 1.00 26.09 ? 885 HOH B O 1 HETATM 10434 O O . HOH LA 8 . ? 7.795 29.492 26.120 1.00 30.15 ? 886 HOH B O 1 HETATM 10435 O O . HOH LA 8 . ? 12.220 54.549 3.022 1.00 19.95 ? 887 HOH B O 1 HETATM 10436 O O . HOH LA 8 . ? -1.972 50.539 26.673 1.00 22.73 ? 888 HOH B O 1 HETATM 10437 O O . HOH LA 8 . ? 38.573 31.339 4.541 1.00 22.54 ? 889 HOH B O 1 HETATM 10438 O O . HOH LA 8 . ? 9.373 39.143 28.700 1.00 27.16 ? 890 HOH B O 1 HETATM 10439 O O . HOH LA 8 . ? 30.797 33.320 24.735 1.00 20.93 ? 891 HOH B O 1 HETATM 10440 O O . HOH LA 8 . ? 29.587 50.682 -14.213 1.00 25.06 ? 892 HOH B O 1 HETATM 10441 O O . HOH LA 8 . ? 54.592 41.952 3.897 1.00 42.52 ? 893 HOH B O 1 HETATM 10442 O O . HOH LA 8 . ? 11.993 57.227 -3.915 1.00 38.27 ? 894 HOH B O 1 HETATM 10443 O O . HOH LA 8 . ? 20.792 62.547 27.122 1.00 51.30 ? 895 HOH B O 1 HETATM 10444 O O . HOH LA 8 . ? 47.400 26.235 -0.400 1.00 26.83 ? 896 HOH B O 1 HETATM 10445 O O . HOH LA 8 . ? 7.510 28.715 23.675 1.00 31.25 ? 897 HOH B O 1 HETATM 10446 O O . HOH LA 8 . ? 26.761 62.554 9.500 1.00 31.80 ? 898 HOH B O 1 HETATM 10447 O O . HOH LA 8 . ? 7.514 45.409 18.809 1.00 16.10 ? 899 HOH B O 1 HETATM 10448 O O . HOH LA 8 . ? -0.869 35.136 14.815 1.00 41.13 ? 900 HOH B O 1 HETATM 10449 O O . HOH LA 8 . ? 25.266 46.693 -4.054 1.00 38.49 ? 901 HOH B O 1 HETATM 10450 O O . HOH LA 8 . ? 20.057 60.980 5.909 1.00 36.28 ? 902 HOH B O 1 HETATM 10451 O O . HOH LA 8 . ? 55.421 50.731 -8.932 1.00 42.22 ? 903 HOH B O 1 HETATM 10452 O O . HOH LA 8 . ? 30.603 42.805 -18.722 1.00 27.19 ? 904 HOH B O 1 HETATM 10453 O O . HOH LA 8 . ? -1.990 43.001 -3.904 1.00 26.66 ? 905 HOH B O 1 HETATM 10454 O O . HOH LA 8 . ? 10.586 61.145 5.813 1.00 40.79 ? 906 HOH B O 1 HETATM 10455 O O . HOH LA 8 . ? 5.487 27.630 -2.511 1.00 45.58 ? 907 HOH B O 1 HETATM 10456 O O . HOH LA 8 . ? 5.859 40.059 28.819 1.00 35.87 ? 908 HOH B O 1 HETATM 10457 O O . HOH LA 8 . ? 25.780 29.533 26.669 1.00 31.85 ? 909 HOH B O 1 HETATM 10458 O O . HOH LA 8 . ? 43.933 39.008 -11.184 1.00 34.05 ? 910 HOH B O 1 HETATM 10459 O O . HOH LA 8 . ? 53.603 48.556 -4.435 1.00 45.41 ? 911 HOH B O 1 HETATM 10460 O O . HOH LA 8 . ? 17.751 60.868 -2.216 1.00 28.81 ? 912 HOH B O 1 HETATM 10461 O O . HOH LA 8 . ? 24.513 38.417 -12.279 1.00 21.21 ? 913 HOH B O 1 HETATM 10462 O O . HOH LA 8 . ? 7.792 55.945 3.080 1.00 28.14 ? 914 HOH B O 1 HETATM 10463 O O . HOH LA 8 . ? 17.598 35.642 28.917 1.00 38.67 ? 915 HOH B O 1 HETATM 10464 O O . HOH LA 8 . ? 48.867 36.965 -2.424 1.00 37.99 ? 916 HOH B O 1 HETATM 10465 O O . HOH LA 8 . ? 12.328 35.071 -8.073 1.00 29.52 ? 917 HOH B O 1 HETATM 10466 O O . HOH LA 8 . ? 22.167 53.011 8.406 1.00 17.79 ? 918 HOH B O 1 HETATM 10467 O O . HOH LA 8 . ? 43.787 35.994 14.454 1.00 44.15 ? 919 HOH B O 1 HETATM 10468 O O . HOH LA 8 . ? 8.423 65.472 8.088 1.00 34.16 ? 920 HOH B O 1 HETATM 10469 O O . HOH LA 8 . ? 54.061 35.867 17.939 1.00 52.56 ? 921 HOH B O 1 HETATM 10470 O O . HOH LA 8 . ? 36.496 62.614 -0.813 1.00 55.22 ? 922 HOH B O 1 HETATM 10471 O O . HOH LA 8 . ? 20.733 55.984 12.794 1.00 16.39 ? 923 HOH B O 1 HETATM 10472 O O . HOH LA 8 . ? 20.908 28.667 -16.726 1.00 44.83 ? 924 HOH B O 1 HETATM 10473 O O . HOH LA 8 . ? 0.359 30.025 16.577 1.00 33.31 ? 925 HOH B O 1 HETATM 10474 O O . HOH LA 8 . ? 28.675 21.983 -17.704 1.00 47.48 ? 926 HOH B O 1 HETATM 10475 O O . HOH LA 8 . ? 9.704 49.668 -2.781 1.00 26.38 ? 927 HOH B O 1 HETATM 10476 O O . HOH LA 8 . ? -1.030 47.481 3.941 1.00 46.13 ? 928 HOH B O 1 HETATM 10477 O O . HOH LA 8 . ? 38.205 33.924 4.107 1.00 34.22 ? 929 HOH B O 1 HETATM 10478 O O . HOH LA 8 . ? 39.327 51.560 -21.008 1.00 57.20 ? 930 HOH B O 1 HETATM 10479 O O . HOH LA 8 . ? 25.205 23.221 0.552 1.00 45.83 ? 931 HOH B O 1 HETATM 10480 O O . HOH LA 8 . ? 15.292 32.454 -8.387 1.00 36.54 ? 932 HOH B O 1 HETATM 10481 O O . HOH LA 8 . ? 0.102 34.633 -5.361 1.00 35.10 ? 933 HOH B O 1 HETATM 10482 O O . HOH LA 8 . ? 4.052 73.141 19.196 1.00 48.77 ? 934 HOH B O 1 HETATM 10483 O O . HOH LA 8 . ? 31.129 52.687 -14.136 1.00 33.74 ? 935 HOH B O 1 HETATM 10484 O O . HOH LA 8 . ? 3.812 44.181 27.469 1.00 29.88 ? 936 HOH B O 1 HETATM 10485 O O . HOH LA 8 . ? 31.499 28.348 9.668 1.00 39.28 ? 937 HOH B O 1 HETATM 10486 O O . HOH LA 8 . ? 1.243 47.886 -0.836 1.00 45.40 ? 938 HOH B O 1 HETATM 10487 O O . HOH LA 8 . ? 7.644 62.825 24.874 1.00 34.39 ? 939 HOH B O 1 HETATM 10488 O O . HOH LA 8 . ? 17.830 26.870 -3.135 1.00 43.66 ? 940 HOH B O 1 HETATM 10489 O O . HOH LA 8 . ? 2.043 64.920 20.522 1.00 33.03 ? 941 HOH B O 1 HETATM 10490 O O . HOH LA 8 . ? 58.610 42.316 4.595 1.00 35.17 ? 942 HOH B O 1 HETATM 10491 O O . HOH LA 8 . ? -2.715 33.698 17.614 1.00 33.82 ? 943 HOH B O 1 HETATM 10492 O O . HOH LA 8 . ? 25.549 54.301 -12.934 1.00 40.38 ? 944 HOH B O 1 HETATM 10493 O O . HOH LA 8 . ? 4.271 24.946 10.949 1.00 31.55 ? 945 HOH B O 1 HETATM 10494 O O . HOH LA 8 . ? 29.084 21.473 -9.827 1.00 34.56 ? 946 HOH B O 1 HETATM 10495 O O . HOH LA 8 . ? 29.906 33.838 -18.700 1.00 41.83 ? 947 HOH B O 1 HETATM 10496 O O . HOH LA 8 . ? 21.159 35.392 -9.757 1.00 26.73 ? 948 HOH B O 1 HETATM 10497 O O . HOH LA 8 . ? 16.691 37.754 30.035 1.00 24.55 ? 949 HOH B O 1 HETATM 10498 O O . HOH LA 8 . ? 20.061 41.028 31.383 1.00 43.43 ? 950 HOH B O 1 HETATM 10499 O O . HOH LA 8 . ? 0.957 31.283 0.464 1.00 39.24 ? 951 HOH B O 1 HETATM 10500 O O . HOH LA 8 . ? -5.199 38.477 1.244 1.00 52.58 ? 952 HOH B O 1 HETATM 10501 O O . HOH LA 8 . ? 53.966 39.603 -0.935 1.00 39.22 ? 953 HOH B O 1 HETATM 10502 O O . HOH LA 8 . ? 24.633 29.966 6.612 1.00 39.63 ? 954 HOH B O 1 HETATM 10503 O O . HOH LA 8 . ? 37.329 23.041 -4.786 1.00 34.69 ? 955 HOH B O 1 HETATM 10504 O O . HOH LA 8 . ? 19.578 28.329 -13.733 1.00 29.31 ? 956 HOH B O 1 HETATM 10505 O O . HOH LA 8 . ? 9.917 67.223 9.439 1.00 38.22 ? 957 HOH B O 1 HETATM 10506 O O . HOH LA 8 . ? 34.640 47.049 -22.197 1.00 32.30 ? 958 HOH B O 1 HETATM 10507 O O . HOH LA 8 . ? 21.092 26.422 10.089 1.00 48.66 ? 959 HOH B O 1 HETATM 10508 O O . HOH LA 8 . ? 1.648 48.015 3.418 1.00 19.81 ? 960 HOH B O 1 HETATM 10509 O O . HOH LA 8 . ? 23.441 59.701 -5.475 1.00 33.43 ? 961 HOH B O 1 HETATM 10510 O O . HOH LA 8 . ? 27.030 61.974 2.084 1.00 37.66 ? 962 HOH B O 1 HETATM 10511 O O . HOH LA 8 . ? 27.435 30.945 1.483 1.00 33.20 ? 963 HOH B O 1 HETATM 10512 O O . HOH LA 8 . ? -12.988 36.590 19.574 1.00 41.20 ? 964 HOH B O 1 HETATM 10513 O O . HOH LA 8 . ? 0.335 25.162 14.294 1.00 41.09 ? 965 HOH B O 1 HETATM 10514 O O . HOH LA 8 . ? 23.548 35.467 28.236 1.00 29.95 ? 966 HOH B O 1 HETATM 10515 O O . HOH LA 8 . ? 40.366 61.158 6.918 1.00 60.28 ? 967 HOH B O 1 HETATM 10516 O O . HOH LA 8 . ? 19.654 34.353 10.918 1.00 52.14 ? 968 HOH B O 1 HETATM 10517 O O . HOH LA 8 . ? 46.938 34.387 -4.319 1.00 42.16 ? 969 HOH B O 1 HETATM 10518 O O . HOH LA 8 . ? 55.212 25.873 -8.763 1.00 57.55 ? 970 HOH B O 1 HETATM 10519 O O . HOH LA 8 . ? 53.137 49.654 -10.190 1.00 51.09 ? 971 HOH B O 1 HETATM 10520 O O . HOH LA 8 . ? 33.888 29.606 31.838 1.00 49.47 ? 972 HOH B O 1 HETATM 10521 O O . HOH LA 8 . ? 67.232 29.779 23.027 1.00 56.81 ? 973 HOH B O 1 HETATM 10522 O O . HOH LA 8 . ? 39.960 29.845 -14.109 1.00 47.04 ? 974 HOH B O 1 HETATM 10523 O O . HOH LA 8 . ? 11.000 45.393 -10.464 1.00 36.46 ? 975 HOH B O 1 HETATM 10524 O O . HOH LA 8 . ? 44.597 27.588 25.196 1.00 38.05 ? 976 HOH B O 1 HETATM 10525 O O . HOH LA 8 . ? 10.738 68.166 15.010 1.00 46.04 ? 977 HOH B O 1 HETATM 10526 O O . HOH LA 8 . ? 36.175 25.903 28.032 1.00 53.71 ? 978 HOH B O 1 HETATM 10527 O O . HOH LA 8 . ? 50.899 41.270 -8.669 1.00 51.64 ? 979 HOH B O 1 HETATM 10528 O O . HOH LA 8 . ? 31.315 62.398 6.239 1.00 48.59 ? 980 HOH B O 1 HETATM 10529 O O . HOH LA 8 . ? 25.250 27.136 34.339 1.00 42.51 ? 981 HOH B O 1 HETATM 10530 O O . HOH LA 8 . ? 25.482 62.191 0.133 1.00 39.55 ? 982 HOH B O 1 HETATM 10531 O O . HOH LA 8 . ? 41.043 33.836 21.360 1.00 28.80 ? 983 HOH B O 1 HETATM 10532 O O . HOH LA 8 . ? 41.053 63.761 4.976 1.00 54.45 ? 984 HOH B O 1 HETATM 10533 O O . HOH LA 8 . ? 25.667 27.071 26.180 1.00 51.84 ? 985 HOH B O 1 HETATM 10534 O O . HOH LA 8 . ? 2.935 39.731 13.764 1.00 29.47 ? 986 HOH B O 1 HETATM 10535 O O . HOH LA 8 . ? 31.403 56.264 -10.597 1.00 36.16 ? 987 HOH B O 1 HETATM 10536 O O . HOH LA 8 . ? 11.042 45.575 -6.133 1.00 23.32 ? 988 HOH B O 1 HETATM 10537 O O . HOH LA 8 . ? 31.951 19.386 0.916 1.00 57.47 ? 989 HOH B O 1 HETATM 10538 O O . HOH LA 8 . ? 37.184 66.200 15.067 1.00 49.94 ? 990 HOH B O 1 HETATM 10539 O O . HOH LA 8 . ? 54.726 37.220 -0.125 1.00 41.07 ? 991 HOH B O 1 HETATM 10540 O O . HOH LA 8 . ? 26.128 21.641 -16.956 1.00 52.28 ? 992 HOH B O 1 HETATM 10541 O O . HOH LA 8 . ? 14.797 43.912 -12.351 1.00 36.56 ? 993 HOH B O 1 HETATM 10542 O O . HOH LA 8 . ? 53.049 44.693 -4.146 1.00 39.23 ? 994 HOH B O 1 HETATM 10543 O O . HOH LA 8 . ? 44.110 48.862 -11.877 1.00 32.40 ? 995 HOH B O 1 HETATM 10544 O O . HOH LA 8 . ? 1.216 35.504 27.679 1.00 48.73 ? 996 HOH B O 1 HETATM 10545 O O . HOH LA 8 . ? 27.108 25.765 -0.346 1.00 34.55 ? 997 HOH B O 1 HETATM 10546 O O . HOH LA 8 . ? 14.127 31.928 5.348 1.00 45.49 ? 998 HOH B O 1 HETATM 10547 O O . HOH LA 8 . ? 16.023 62.216 -0.099 1.00 49.82 ? 999 HOH B O 1 HETATM 10548 O O . HOH LA 8 . ? 22.030 64.618 10.713 1.00 43.45 ? 1000 HOH B O 1 HETATM 10549 O O . HOH LA 8 . ? 5.388 41.460 -7.309 1.00 43.13 ? 1001 HOH B O 1 HETATM 10550 O O . HOH LA 8 . ? 9.394 15.330 6.353 1.00 58.19 ? 1002 HOH B O 1 HETATM 10551 O O . HOH LA 8 . ? 8.697 58.945 6.228 1.00 29.76 ? 1003 HOH B O 1 HETATM 10552 O O . HOH LA 8 . ? 20.370 43.585 33.110 1.00 48.54 ? 1004 HOH B O 1 HETATM 10553 O O . HOH LA 8 . ? 29.273 36.471 -18.288 1.00 39.40 ? 1005 HOH B O 1 HETATM 10554 O O . HOH LA 8 . ? 9.805 39.660 -6.270 1.00 45.67 ? 1006 HOH B O 1 HETATM 10555 O O . HOH LA 8 . ? 21.063 23.608 -7.059 1.00 38.71 ? 1007 HOH B O 1 HETATM 10556 O O . HOH LA 8 . ? 11.537 68.222 12.559 1.00 46.90 ? 1008 HOH B O 1 HETATM 10557 O O . HOH LA 8 . ? 44.167 25.954 14.865 1.00 44.12 ? 1009 HOH B O 1 HETATM 10558 O O . HOH LA 8 . ? 30.545 27.162 3.853 1.00 44.36 ? 1010 HOH B O 1 HETATM 10559 O O . HOH LA 8 . ? 20.703 29.076 30.535 1.00 40.72 ? 1011 HOH B O 1 HETATM 10560 O O . HOH LA 8 . ? 34.543 16.552 11.330 1.00 50.86 ? 1012 HOH B O 1 HETATM 10561 O O . HOH LA 8 . ? 18.501 18.734 5.813 1.00 38.38 ? 1013 HOH B O 1 HETATM 10562 O O . HOH LA 8 . ? 32.296 45.392 30.425 1.00 49.45 ? 1014 HOH B O 1 HETATM 10563 O O . HOH LA 8 . ? 9.742 50.726 27.200 1.00 34.42 ? 1015 HOH B O 1 HETATM 10564 O O . HOH LA 8 . ? 16.242 36.973 -10.083 1.00 55.52 ? 1016 HOH B O 1 HETATM 10565 O O . HOH LA 8 . ? 43.719 50.061 16.586 1.00 35.92 ? 1017 HOH B O 1 HETATM 10566 O O . HOH LA 8 . ? 19.517 24.985 -2.251 1.00 46.42 ? 1018 HOH B O 1 HETATM 10567 O O . HOH LA 8 . ? 51.154 37.657 -3.279 1.00 43.03 ? 1019 HOH B O 1 HETATM 10568 O O . HOH LA 8 . ? 20.223 61.591 8.858 1.00 41.25 ? 1020 HOH B O 1 HETATM 10569 O O . HOH LA 8 . ? 39.745 35.837 -14.247 1.00 45.32 ? 1021 HOH B O 1 HETATM 10570 O O . HOH LA 8 . ? 48.013 53.841 3.663 1.00 55.19 ? 1022 HOH B O 1 HETATM 10571 O O . HOH LA 8 . ? 48.978 37.028 -14.710 1.00 43.27 ? 1023 HOH B O 1 HETATM 10572 O O . HOH LA 8 . ? 65.220 44.480 19.135 1.00 33.42 ? 1024 HOH B O 1 HETATM 10573 O O . HOH LA 8 . ? 5.348 23.317 12.967 1.00 48.42 ? 1025 HOH B O 1 HETATM 10574 O O . HOH LA 8 . ? 24.126 37.485 30.021 1.00 39.18 ? 1026 HOH B O 1 HETATM 10575 O O . HOH LA 8 . ? 2.133 54.084 8.373 1.00 44.94 ? 1027 HOH B O 1 HETATM 10576 O O . HOH LA 8 . ? 47.161 32.374 -2.454 1.00 40.53 ? 1028 HOH B O 1 HETATM 10577 O O . HOH LA 8 . ? 20.745 29.938 -18.892 1.00 50.51 ? 1029 HOH B O 1 HETATM 10578 O O . HOH LA 8 . ? 40.453 66.129 5.622 1.00 52.76 ? 1030 HOH B O 1 HETATM 10579 O O . HOH LA 8 . ? 2.971 31.463 -4.541 1.00 41.56 ? 1031 HOH B O 1 HETATM 10580 O O . HOH LA 8 . ? 48.483 27.365 -2.627 1.00 50.17 ? 1032 HOH B O 1 HETATM 10581 O O . HOH LA 8 . ? 21.486 34.198 3.788 1.00 36.08 ? 1033 HOH B O 1 HETATM 10582 O O . HOH LA 8 . ? 51.104 52.568 -15.243 1.00 35.55 ? 1034 HOH B O 1 HETATM 10583 O O . HOH LA 8 . ? 8.342 51.762 -2.375 1.00 32.33 ? 1035 HOH B O 1 HETATM 10584 O O . HOH LA 8 . ? 2.143 66.175 22.956 1.00 40.08 ? 1036 HOH B O 1 HETATM 10585 O O . HOH LA 8 . ? -1.792 50.041 2.119 1.00 38.67 ? 1037 HOH B O 1 HETATM 10586 O O . HOH LA 8 . ? 23.851 61.375 22.151 1.00 52.08 ? 1038 HOH B O 1 HETATM 10587 O O . HOH LA 8 . ? -1.220 44.938 -5.654 1.00 41.48 ? 1039 HOH B O 1 HETATM 10588 O O . HOH LA 8 . ? 9.815 42.581 -6.622 1.00 43.60 ? 1040 HOH B O 1 HETATM 10589 O O . HOH LA 8 . ? 36.287 36.637 -18.674 1.00 46.15 ? 1041 HOH B O 1 HETATM 10590 O O . HOH LA 8 . ? 24.523 32.387 4.060 1.00 41.29 ? 1042 HOH B O 1 HETATM 10591 O O . HOH LA 8 . ? 19.053 36.355 -10.818 1.00 30.47 ? 1043 HOH B O 1 HETATM 10592 O O . HOH LA 8 . ? 49.233 44.402 5.006 1.00 35.43 ? 1044 HOH B O 1 HETATM 10593 O O . HOH LA 8 . ? 8.600 14.690 8.838 1.00 45.60 ? 1045 HOH B O 1 HETATM 10594 O O . HOH LA 8 . ? 22.780 28.423 9.869 1.00 52.28 ? 1046 HOH B O 1 HETATM 10595 O O . HOH LA 8 . ? 0.089 34.275 11.085 1.00 48.07 ? 1047 HOH B O 1 HETATM 10596 O O . HOH LA 8 . ? 1.499 37.595 12.016 1.00 29.96 ? 1048 HOH B O 1 HETATM 10597 O O . HOH LA 8 . ? 26.770 28.126 1.177 1.00 42.32 ? 1049 HOH B O 1 HETATM 10598 O O . HOH LA 8 . ? 14.852 37.299 31.811 1.00 30.70 ? 1050 HOH B O 1 HETATM 10599 O O . HOH LA 8 . ? 3.836 48.803 -1.429 1.00 29.12 ? 1051 HOH B O 1 HETATM 10600 O O . HOH LA 8 . ? 20.501 32.686 9.214 1.00 48.63 ? 1052 HOH B O 1 HETATM 10601 O O . HOH LA 8 . ? -1.808 30.952 18.651 1.00 52.78 ? 1053 HOH B O 1 HETATM 10602 O O . HOH LA 8 . ? 19.271 38.611 31.458 1.00 44.36 ? 1054 HOH B O 1 HETATM 10603 O O . HOH LA 8 . ? 33.227 41.285 -20.601 1.00 46.48 ? 1055 HOH B O 1 HETATM 10604 O O . HOH LA 8 . ? 16.703 31.544 -10.796 1.00 52.06 ? 1056 HOH B O 1 HETATM 10605 O O . HOH LA 8 . ? 1.386 31.579 25.094 1.00 33.22 ? 1057 HOH B O 1 HETATM 10606 O O . HOH LA 8 . ? 37.703 66.957 17.902 1.00 60.66 ? 1058 HOH B O 1 HETATM 10607 O O . HOH LA 8 . ? -4.432 41.712 -3.252 1.00 48.49 ? 1059 HOH B O 1 HETATM 10608 O O . HOH LA 8 . ? 1.791 55.105 6.050 1.00 47.06 ? 1060 HOH B 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 SER 1 1 1 SER SER A . n A 1 2 TRP 2 2 2 TRP TRP A . n A 1 3 GLU 3 3 3 GLU GLU A . n A 1 4 VAL 4 4 4 VAL VAL A . n A 1 5 GLY 5 5 5 GLY GLY A . n A 1 6 CYS 6 6 6 CYS CYS A . n A 1 7 GLY 7 7 7 GLY GLY A . n A 1 8 ALA 8 8 8 ALA ALA A . n A 1 9 PRO 9 9 9 PRO PRO A . n A 1 10 VAL 10 10 10 VAL VAL A . n A 1 11 PRO 11 11 11 PRO PRO A . n A 1 12 LEU 12 12 12 LEU LEU A . n A 1 13 VAL 13 13 13 VAL VAL A . n A 1 14 THR 14 14 14 THR THR A . n A 1 15 CYS 15 15 15 CYS CYS A . n A 1 16 ASP 16 16 16 ASP ASP A . n A 1 17 GLU 17 17 17 GLU GLU A . n A 1 18 GLN 18 18 18 GLN GLN A . n A 1 19 SER 19 19 19 SER SER A . n A 1 20 PRO 20 20 20 PRO PRO A . n A 1 21 TYR 21 21 21 TYR TYR A . n A 1 22 ARG 22 22 22 ARG ARG A . n A 1 23 THR 23 23 23 THR THR A . n A 1 24 ILE 24 24 24 ILE ILE A . n A 1 25 THR 25 25 25 THR THR A . n A 1 26 GLY 26 26 26 GLY GLY A . n A 1 27 ASP 27 27 27 ASP ASP A . n A 1 28 CYS 28 28 28 CYS CYS A . n A 1 29 ASN 29 29 29 ASN ASN A . n A 1 30 ASN 30 30 30 ASN ASN A . n A 1 31 ARG 31 31 31 ARG ARG A . n A 1 32 ARG 32 32 32 ARG ARG A . n A 1 33 SER 33 33 33 SER SER A . n A 1 34 PRO 34 34 34 PRO PRO A . n A 1 35 ALA 35 35 35 ALA ALA A . n A 1 36 LEU 36 36 36 LEU LEU A . n A 1 37 GLY 37 37 37 GLY GLY A . n A 1 38 ALA 38 38 38 ALA ALA A . n A 1 39 ALA 39 39 39 ALA ALA A . n A 1 40 ASN 40 40 40 ASN ASN A . n A 1 41 ARG 41 41 41 ARG ARG A . n A 1 42 ALA 42 42 42 ALA ALA A . n A 1 43 LEU 43 43 43 LEU LEU A . n A 1 44 ALA 44 44 44 ALA ALA A . n A 1 45 ARG 45 45 45 ARG ARG A . n A 1 46 TRP 46 46 46 TRP TRP A . n A 1 47 LEU 47 47 47 LEU LEU A . n A 1 48 PRO 48 48 48 PRO PRO A . n A 1 49 ALA 49 49 49 ALA ALA A . n A 1 50 GLU 50 50 50 GLU GLU A . n A 1 51 TYR 51 51 51 TYR TYR A . n A 1 52 GLU 52 52 52 GLU GLU A . n A 1 53 ASP 53 53 53 ASP ASP A . n A 1 54 GLY 54 54 54 GLY GLY A . n A 1 55 LEU 55 55 55 LEU LEU A . n A 1 56 ALA 56 56 56 ALA ALA A . n A 1 57 VAL 57 57 57 VAL VAL A . n A 1 58 PRO 58 58 58 PRO PRO A . n A 1 59 PHE 59 59 59 PHE PHE A . n A 1 60 GLY 60 60 60 GLY GLY A . n A 1 61 TRP 61 61 61 TRP TRP A . n A 1 62 THR 62 62 62 THR THR A . n A 1 63 GLN 63 63 63 GLN GLN A . n A 1 64 ARG 64 64 64 ARG ARG A . n A 1 65 LYS 65 65 65 LYS LYS A . n A 1 66 THR 66 66 66 THR THR A . n A 1 67 ARG 67 67 67 ARG ARG A . n A 1 68 ASN 68 68 68 ASN ASN A . n A 1 69 GLY 69 69 69 GLY GLY 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 VAL 72 72 72 VAL VAL A . n A 1 73 PRO 73 73 73 PRO PRO A . n A 1 74 LEU 74 74 74 LEU LEU A . n A 1 75 ALA 75 75 75 ALA ALA A . n A 1 76 ARG 76 76 76 ARG ARG A . n A 1 77 GLU 77 77 77 GLU GLU A . n A 1 78 VAL 78 78 78 VAL VAL A . n A 1 79 SER 79 79 79 SER SER A . n A 1 80 ASN 80 80 80 ASN ASN A . n A 1 81 LYS 81 81 81 LYS LYS A . n A 1 82 ILE 82 82 82 ILE ILE A . n A 1 83 VAL 83 83 83 VAL VAL A . n A 1 84 GLY 84 84 84 GLY GLY A . n A 1 85 TYR 85 85 85 TYR TYR A . n A 1 86 LEU 86 86 86 LEU LEU A . n A 1 87 ASP 87 87 87 ASP ASP A . n A 1 88 GLU 88 88 88 GLU GLU A . n A 1 89 GLU 89 89 89 GLU GLU A . n A 1 90 GLY 90 90 90 GLY GLY A . n A 1 91 VAL 91 91 91 VAL VAL A . n A 1 92 LEU 92 92 92 LEU LEU A . n A 1 93 ASP 93 93 93 ASP ASP A . n A 1 94 GLN 94 94 94 GLN GLN A . n A 1 95 ASN 95 95 95 ASN ASN A . n A 1 96 ARG 96 96 96 ARG ARG A . n A 1 97 SER 97 97 97 SER SER A . n A 1 98 LEU 98 98 98 LEU LEU A . n A 1 99 LEU 99 99 99 LEU LEU A . n A 1 100 PHE 100 100 100 PHE PHE A . n A 1 101 MET 101 101 101 MET MET A . n A 1 102 GLN 102 102 102 GLN GLN A . n A 1 103 TRP 103 103 103 TRP TRP A . n A 1 104 GLY 104 104 104 GLY GLY A . n A 1 105 GLN 105 105 105 GLN GLN A . n A 1 106 ILE 106 106 106 ILE ILE A . n A 1 107 VAL 107 107 107 VAL VAL A . n A 1 108 ASP 108 108 108 ASP ASP A . n A 1 109 HIS 109 109 109 HIS HIS A . n A 1 110 ASP 110 110 110 ASP ASP A . n A 1 111 LEU 111 111 111 LEU LEU A . n A 1 112 ASP 112 112 112 ASP ASP A . n A 1 113 PHE 113 113 113 PHE PHE A . n A 1 114 ALA 114 114 114 ALA ALA A . n A 1 115 PRO 115 115 115 PRO PRO A . n A 1 116 GLU 116 116 116 GLU GLU A . n A 1 117 THR 117 117 117 THR THR A . n A 1 118 GLU 118 118 118 GLU GLU A . n A 1 119 LEU 119 119 119 LEU LEU A . n A 1 120 GLY 120 120 120 GLY GLY A . n A 1 121 SER 121 121 121 SER SER A . n A 1 122 SER 122 122 122 SER SER A . n A 1 123 GLU 123 123 123 GLU GLU A . n A 1 124 HIS 124 124 124 HIS HIS A . n A 1 125 SER 125 125 125 SER SER A . n A 1 126 LYS 126 126 126 LYS LYS A . n A 1 127 VAL 127 127 127 VAL VAL A . n A 1 128 GLN 128 128 128 GLN GLN A . n A 1 129 CYS 129 129 129 CYS CYS A . n A 1 130 GLU 130 130 130 GLU GLU A . n A 1 131 GLU 131 131 131 GLU GLU A . n A 1 132 TYR 132 132 132 TYR TYR A . n A 1 133 CYS 133 133 133 CYS CYS A . n A 1 134 VAL 134 134 134 VAL VAL A . n A 1 135 GLN 135 135 135 GLN GLN A . n A 1 136 GLY 136 136 136 GLY GLY A . n A 1 137 ASP 137 137 137 ASP ASP A . n A 1 138 GLU 138 138 138 GLU GLU A . n A 1 139 CYS 139 139 139 CYS CYS A . n A 1 140 PHE 140 140 140 PHE PHE A . n A 1 141 PRO 141 141 141 PRO PRO A . n A 1 142 ILE 142 142 142 ILE ILE A . n A 1 143 MET 143 143 143 MET MET A . n A 1 144 PHE 144 144 144 PHE PHE A . n A 1 145 PRO 145 145 145 PRO PRO A . n A 1 146 LYS 146 146 146 LYS LYS A . n A 1 147 ASN 147 147 147 ASN ASN A . n A 1 148 ASP 148 148 148 ASP ASP A . n A 1 149 PRO 149 149 149 PRO PRO A . n A 1 150 LYS 150 150 150 LYS LYS A . n A 1 151 LEU 151 151 151 LEU LEU A . n A 1 152 LYS 152 152 152 LYS LYS A . n A 1 153 THR 153 153 153 THR THR A . n A 1 154 GLN 154 154 154 GLN GLN A . n A 1 155 GLY 155 155 155 GLY GLY A . n A 1 156 LYS 156 156 156 LYS LYS A . n A 1 157 CYS 157 157 157 CYS CYS A . n A 1 158 MET 158 158 158 MET MET A . n A 1 159 PRO 159 159 159 PRO PRO A . n A 1 160 PHE 160 160 160 PHE PHE A . n A 1 161 PHE 161 161 161 PHE PHE A . n A 1 162 ARG 162 162 162 ARG ARG A . n A 1 163 ALA 163 163 163 ALA ALA A . n A 1 164 GLY 164 164 164 GLY GLY A . n A 1 165 PHE 165 165 165 PHE PHE A . n A 1 166 VAL 166 166 166 VAL VAL A . n A 1 167 CYS 167 167 167 CYS CYS A . n A 1 168 PRO 168 168 168 PRO PRO A . n A 1 169 THR 169 169 169 THR THR A . n A 1 170 PRO 170 170 170 PRO PRO A . n A 1 171 PRO 171 171 171 PRO PRO A . n A 1 172 TYR 172 172 172 TYR TYR A . n A 1 173 GLN 173 173 173 GLN GLN A . n A 1 174 SER 174 174 174 SER SER A . n A 1 175 LEU 175 175 175 LEU LEU A . n A 1 176 ALA 176 176 176 ALA ALA A . n A 1 177 ARG 177 177 177 ARG ARG A . n A 1 178 ASP 178 178 178 ASP ASP A . n A 1 179 GLN 179 179 179 GLN GLN A . n A 1 180 ILE 180 180 180 ILE ILE A . n A 1 181 ASN 181 181 181 ASN ASN A . n A 1 182 ALA 182 182 182 ALA ALA A . n A 1 183 VAL 183 183 183 VAL VAL A . n A 1 184 THR 184 184 184 THR THR A . n A 1 185 SER 185 185 185 SER SER A . n A 1 186 PHE 186 186 186 PHE PHE A . n A 1 187 LEU 187 187 187 LEU LEU A . n A 1 188 ASP 188 188 188 ASP ASP A . n A 1 189 ALA 189 189 189 ALA ALA A . n A 1 190 SER 190 190 190 SER SER A . n A 1 191 LEU 191 191 191 LEU LEU A . n A 1 192 VAL 192 192 192 VAL VAL A . n A 1 193 TYR 193 193 193 TYR TYR A . n A 1 194 GLY 194 194 194 GLY GLY A . n A 1 195 SER 195 195 195 SER SER A . n A 1 196 GLU 196 196 196 GLU GLU A . n A 1 197 PRO 197 197 197 PRO PRO A . n A 1 198 SER 198 198 198 SER SER A . n A 1 199 LEU 199 199 199 LEU LEU A . n A 1 200 ALA 200 200 200 ALA ALA A . n A 1 201 SER 201 201 201 SER SER A . n A 1 202 ARG 202 202 202 ARG ARG A . n A 1 203 LEU 203 203 203 LEU LEU A . n A 1 204 ARG 204 204 204 ARG ARG A . n A 1 205 ASN 205 205 205 ASN ASN A . n A 1 206 LEU 206 206 206 LEU LEU A . n A 1 207 SER 207 207 207 SER SER A . n A 1 208 SER 208 208 208 SER SER A . n A 1 209 PRO 209 209 209 PRO PRO A . n A 1 210 LEU 210 210 210 LEU LEU A . n A 1 211 GLY 211 211 211 GLY GLY A . n A 1 212 LEU 212 212 212 LEU LEU A . n A 1 213 MET 213 213 213 MET MET A . n A 1 214 ALA 214 214 214 ALA ALA A . n A 1 215 VAL 215 215 215 VAL VAL A . n A 1 216 ASN 216 216 216 ASN ASN A . n A 1 217 GLN 217 217 217 GLN GLN A . n A 1 218 GLU 218 218 218 GLU GLU A . n A 1 219 ALA 219 219 219 ALA ALA A . n A 1 220 TRP 220 220 220 TRP TRP A . n A 1 221 ASP 221 221 221 ASP ASP A . n A 1 222 HIS 222 222 222 HIS HIS A . n A 1 223 GLY 223 223 223 GLY GLY A . n A 1 224 LEU 224 224 224 LEU LEU A . n A 1 225 ALA 225 225 225 ALA ALA A . n A 1 226 TYR 226 226 226 TYR TYR A . n A 1 227 PRO 227 227 227 PRO PRO A . n A 1 228 PRO 228 228 228 PRO PRO A . n A 1 229 PHE 229 229 229 PHE PHE A . n A 1 230 ASN 230 230 230 ASN ASN A . n A 1 231 ASN 231 231 231 ASN ASN A . n A 1 232 VAL 232 232 232 VAL VAL A . n A 1 233 LYS 233 233 233 LYS LYS A . n A 1 234 PRO 234 234 234 PRO PRO A . n A 1 235 SER 235 235 235 SER SER A . n A 1 236 PRO 236 236 236 PRO PRO A . n A 1 237 CYS 237 237 237 CYS CYS A . n A 1 238 GLU 238 238 238 GLU GLU A . n A 1 239 PHE 239 239 239 PHE PHE A . n A 1 240 ILE 240 240 240 ILE ILE A . n A 1 241 ASN 241 241 241 ASN ASN A . n A 1 242 THR 242 242 242 THR THR A . n A 1 243 THR 243 243 243 THR THR A . n A 1 244 ALA 244 244 244 ALA ALA A . n A 1 245 HIS 245 245 245 HIS HIS A . n A 1 246 VAL 246 246 246 VAL VAL A . n A 1 247 PRO 247 247 247 PRO PRO A . n A 1 248 CYS 248 248 248 CYS CYS A . n A 1 249 PHE 249 249 249 PHE PHE A . n A 1 250 GLN 250 250 250 GLN GLN A . n A 1 251 ALA 251 251 251 ALA ALA A . n A 1 252 GLY 252 252 252 GLY GLY A . n A 1 253 ASP 253 253 253 ASP ASP A . n A 1 254 SER 254 254 254 SER SER A . n A 1 255 ARG 255 255 255 ARG ARG A . n A 1 256 ALA 256 256 256 ALA ALA A . n A 1 257 SER 257 257 257 SER SER A . n A 1 258 GLU 258 258 258 GLU GLU A . n A 1 259 GLN 259 259 259 GLN GLN A . n A 1 260 ILE 260 260 260 ILE ILE A . n A 1 261 LEU 261 261 261 LEU LEU A . n A 1 262 LEU 262 262 262 LEU LEU A . n A 1 263 ALA 263 263 263 ALA ALA A . n A 1 264 THR 264 264 264 THR THR A . n A 1 265 VAL 265 265 265 VAL VAL A . n A 1 266 HIS 266 266 266 HIS HIS A . n A 1 267 THR 267 267 267 THR THR A . n A 1 268 LEU 268 268 268 LEU LEU A . n A 1 269 LEU 269 269 269 LEU LEU A . n A 1 270 LEU 270 270 270 LEU LEU A . n A 1 271 ARG 271 271 271 ARG ARG A . n A 1 272 GLU 272 272 272 GLU GLU A . n A 1 273 HIS 273 273 273 HIS HIS A . n A 1 274 ASN 274 274 274 ASN ASN A . n A 1 275 ARG 275 275 275 ARG ARG A . n A 1 276 LEU 276 276 276 LEU LEU A . n A 1 277 ALA 277 277 277 ALA ALA A . n A 1 278 ARG 278 278 278 ARG ARG A . n A 1 279 GLU 279 279 279 GLU GLU A . n A 1 280 LEU 280 280 280 LEU LEU A . n A 1 281 LYS 281 281 281 LYS LYS A . n A 1 282 ARG 282 282 282 ARG ARG A . n A 1 283 LEU 283 283 283 LEU LEU A . n A 1 284 ASN 284 284 284 ASN ASN A . n A 1 285 PRO 285 285 285 PRO PRO A . n A 1 286 HIS 286 286 286 HIS HIS A . n A 1 287 TRP 287 287 287 TRP TRP A . n A 1 288 ASP 288 288 288 ASP ASP A . n A 1 289 GLY 289 289 289 GLY GLY A . n A 1 290 GLU 290 290 290 GLU GLU A . n A 1 291 MET 291 291 291 MET MET A . n A 1 292 LEU 292 292 292 LEU LEU A . n A 1 293 TYR 293 293 293 TYR TYR A . n A 1 294 GLN 294 294 294 GLN GLN A . n A 1 295 GLU 295 295 295 GLU GLU A . n A 1 296 ALA 296 296 296 ALA ALA A . n A 1 297 ARG 297 297 297 ARG ARG A . n A 1 298 LYS 298 298 298 LYS LYS A . n A 1 299 ILE 299 299 299 ILE ILE A . n A 1 300 LEU 300 300 300 LEU LEU A . n A 1 301 GLY 301 301 301 GLY GLY A . n A 1 302 ALA 302 302 302 ALA ALA A . n A 1 303 PHE 303 303 303 PHE PHE A . n A 1 304 ILE 304 304 304 ILE ILE A . n A 1 305 GLN 305 305 305 GLN GLN A . n A 1 306 ILE 306 306 306 ILE ILE A . n A 1 307 ILE 307 307 307 ILE ILE A . n A 1 308 THR 308 308 308 THR THR A . n A 1 309 PHE 309 309 309 PHE PHE A . n A 1 310 ARG 310 310 310 ARG ARG A . n A 1 311 ASP 311 311 311 ASP ASP A . n A 1 312 TYR 312 312 312 TYR TYR A . n A 1 313 LEU 313 313 313 LEU LEU A . n A 1 314 PRO 314 314 314 PRO PRO A . n A 1 315 ILE 315 315 315 ILE ILE A . n A 1 316 VAL 316 316 316 VAL VAL A . n A 1 317 LEU 317 317 317 LEU LEU A . n A 1 318 GLY 318 318 318 GLY GLY A . n A 1 319 SER 319 319 319 SER SER A . n A 1 320 GLU 320 320 320 GLU GLU A . n A 1 321 MET 321 321 321 MET MET A . n A 1 322 GLN 322 322 322 GLN GLN A . n A 1 323 LYS 323 323 323 LYS LYS A . n A 1 324 TRP 324 324 324 TRP TRP A . n A 1 325 ILE 325 325 325 ILE ILE A . n A 1 326 PRO 326 326 326 PRO PRO A . n A 1 327 PRO 327 327 327 PRO PRO A . n A 1 328 TYR 328 328 328 TYR TYR A . n A 1 329 GLN 329 329 329 GLN GLN A . n A 1 330 GLY 330 330 330 GLY GLY A . n A 1 331 TYR 331 331 331 TYR TYR A . n A 1 332 ASN 332 332 332 ASN ASN A . n A 1 333 ASN 333 333 333 ASN ASN A . n A 1 334 SER 334 334 334 SER SER A . n A 1 335 VAL 335 335 335 VAL VAL A . n A 1 336 ASP 336 336 336 ASP ASP A . n A 1 337 PRO 337 337 337 PRO PRO A . n A 1 338 ARG 338 338 338 ARG ARG A . n A 1 339 ILE 339 339 339 ILE ILE A . n A 1 340 SER 340 340 340 SER SER A . n A 1 341 ASN 341 341 341 ASN ASN A . n A 1 342 VAL 342 342 342 VAL VAL A . n A 1 343 PHE 343 343 343 PHE PHE A . n A 1 344 THR 344 344 344 THR THR A . n A 1 345 PHE 345 345 345 PHE PHE A . n A 1 346 ALA 346 346 346 ALA ALA A . n A 1 347 PHE 347 347 347 PHE PHE A . n A 1 348 ARG 348 348 348 ARG ARG A . n A 1 349 PHE 349 349 349 PHE PHE A . n A 1 350 GLY 350 350 350 GLY GLY A . n A 1 351 HIS 351 351 351 HIS HIS A . n A 1 352 MET 352 352 352 MET MET A . n A 1 353 GLU 353 353 353 GLU GLU A . n A 1 354 VAL 354 354 354 VAL VAL A . n A 1 355 PRO 355 355 355 PRO PRO A . n A 1 356 SER 356 356 356 SER SER A . n A 1 357 THR 357 357 357 THR THR A . n A 1 358 VAL 358 358 358 VAL VAL A . n A 1 359 SER 359 359 359 SER SER A . n A 1 360 ARG 360 360 360 ARG ARG A . n A 1 361 LEU 361 361 361 LEU LEU A . n A 1 362 ASP 362 362 362 ASP ASP A . n A 1 363 GLU 363 363 363 GLU GLU A . n A 1 364 ASN 364 364 364 ASN ASN A . n A 1 365 TYR 365 365 365 TYR TYR A . n A 1 366 GLN 366 366 366 GLN GLN A . n A 1 367 PRO 367 367 367 PRO PRO A . n A 1 368 TRP 368 368 368 TRP TRP A . n A 1 369 GLY 369 369 369 GLY GLY A . n A 1 370 PRO 370 370 370 PRO PRO A . n A 1 371 GLU 371 371 371 GLU GLU A . n A 1 372 ALA 372 372 372 ALA ALA A . n A 1 373 GLU 373 373 373 GLU GLU A . n A 1 374 LEU 374 374 374 LEU LEU A . n A 1 375 PRO 375 375 375 PRO PRO A . n A 1 376 LEU 376 376 376 LEU LEU A . n A 1 377 HIS 377 377 377 HIS HIS A . n A 1 378 THR 378 378 378 THR THR A . n A 1 379 LEU 379 379 379 LEU LEU A . n A 1 380 PHE 380 380 380 PHE PHE A . n A 1 381 PHE 381 381 381 PHE PHE A . n A 1 382 ASN 382 382 382 ASN ASN A . n A 1 383 THR 383 383 383 THR THR A . n A 1 384 TRP 384 384 384 TRP TRP A . n A 1 385 ARG 385 385 385 ARG ARG A . n A 1 386 ILE 386 386 386 ILE ILE A . n A 1 387 ILE 387 387 387 ILE ILE A . n A 1 388 LYS 388 388 388 LYS LYS A . n A 1 389 ASP 389 389 389 ASP ASP A . n A 1 390 GLY 390 390 390 GLY GLY A . n A 1 391 GLY 391 391 391 GLY GLY A . n A 1 392 ILE 392 392 392 ILE ILE A . n A 1 393 ASP 393 393 393 ASP ASP A . n A 1 394 PRO 394 394 394 PRO PRO A . n A 1 395 LEU 395 395 395 LEU LEU A . n A 1 396 VAL 396 396 396 VAL VAL A . n A 1 397 ARG 397 397 397 ARG ARG A . n A 1 398 GLY 398 398 398 GLY GLY A . n A 1 399 LEU 399 399 399 LEU LEU A . n A 1 400 LEU 400 400 400 LEU LEU A . n A 1 401 ALA 401 401 401 ALA ALA A . n A 1 402 LYS 402 402 402 LYS LYS A . n A 1 403 ASN 403 403 403 ASN ASN A . n A 1 404 SER 404 404 404 SER SER A . n A 1 405 LYS 405 405 405 LYS LYS A . n A 1 406 LEU 406 406 406 LEU LEU A . n A 1 407 MET 407 407 407 MET MET A . n A 1 408 ASN 408 408 408 ASN ASN A . n A 1 409 GLN 409 409 409 GLN GLN A . n A 1 410 ASN 410 410 410 ASN ASN A . n A 1 411 LYS 411 411 411 LYS LYS A . n A 1 412 MET 412 412 412 MET MET A . n A 1 413 VAL 413 413 413 VAL VAL A . n A 1 414 THR 414 414 414 THR THR A . n A 1 415 SER 415 415 415 SER SER A . n A 1 416 GLU 416 416 416 GLU GLU A . n A 1 417 LEU 417 417 417 LEU LEU A . n A 1 418 ARG 418 418 418 ARG ARG A . n A 1 419 ASN 419 419 419 ASN ASN A . n A 1 420 LYS 420 420 420 LYS LYS A . n A 1 421 LEU 421 421 421 LEU LEU A . n A 1 422 PHE 422 422 422 PHE PHE A . n A 1 423 GLN 423 423 423 GLN GLN A . n A 1 424 PRO 424 424 424 PRO PRO A . n A 1 425 THR 425 425 425 THR THR A . n A 1 426 HIS 426 426 426 HIS HIS A . n A 1 427 LYS 427 427 427 LYS LYS A . n A 1 428 VAL 428 428 428 VAL VAL A . n A 1 429 HIS 429 429 429 HIS HIS A . n A 1 430 GLY 430 430 430 GLY GLY A . n A 1 431 PHE 431 431 431 PHE PHE A . n A 1 432 ASP 432 432 432 ASP ASP A . n A 1 433 LEU 433 433 433 LEU LEU A . n A 1 434 ALA 434 434 434 ALA ALA A . n A 1 435 ALA 435 435 435 ALA ALA A . n A 1 436 ILE 436 436 436 ILE ILE A . n A 1 437 ASN 437 437 437 ASN ASN A . n A 1 438 LEU 438 438 438 LEU LEU A . n A 1 439 GLN 439 439 439 GLN GLN A . n A 1 440 ARG 440 440 440 ARG ARG A . n A 1 441 CYS 441 441 441 CYS CYS A . n A 1 442 ARG 442 442 442 ARG ARG A . n A 1 443 ASP 443 443 443 ASP ASP A . n A 1 444 HIS 444 444 444 HIS HIS A . n A 1 445 GLY 445 445 445 GLY GLY A . n A 1 446 MET 446 446 446 MET MET A . n A 1 447 PRO 447 447 447 PRO PRO A . n A 1 448 GLY 448 448 448 GLY GLY A . n A 1 449 TYR 449 449 449 TYR TYR A . n A 1 450 ASN 450 450 450 ASN ASN A . n A 1 451 SER 451 451 451 SER SER A . n A 1 452 TRP 452 452 452 TRP TRP A . n A 1 453 ARG 453 453 453 ARG ARG A . n A 1 454 GLY 454 454 454 GLY GLY A . n A 1 455 PHE 455 455 455 PHE PHE A . n A 1 456 CYS 456 456 456 CYS CYS A . n A 1 457 GLY 457 457 457 GLY GLY A . n A 1 458 LEU 458 458 458 LEU LEU A . n A 1 459 SER 459 459 459 SER SER A . n A 1 460 GLN 460 460 460 GLN GLN A . n A 1 461 PRO 461 461 461 PRO PRO A . n A 1 462 LYS 462 462 462 LYS LYS A . n A 1 463 THR 463 463 463 THR THR A . n A 1 464 LEU 464 464 464 LEU LEU A . n A 1 465 LYS 465 465 465 LYS LYS A . n A 1 466 GLY 466 466 466 GLY GLY A . n A 1 467 LEU 467 467 467 LEU LEU A . n A 1 468 GLN 468 468 468 GLN GLN A . n A 1 469 ALA 469 469 469 ALA ALA A . n A 1 470 VAL 470 470 470 VAL VAL A . n A 1 471 LEU 471 471 471 LEU LEU A . n A 1 472 LYS 472 472 472 LYS LYS A . n A 1 473 ASN 473 473 473 ASN ASN A . n A 1 474 LYS 474 474 474 LYS LYS A . n A 1 475 VAL 475 475 475 VAL VAL A . n A 1 476 LEU 476 476 476 LEU LEU A . n A 1 477 ALA 477 477 477 ALA ALA A . n A 1 478 LYS 478 478 478 LYS LYS A . n A 1 479 LYS 479 479 479 LYS LYS A . n A 1 480 LEU 480 480 480 LEU LEU A . n A 1 481 LEU 481 481 481 LEU LEU A . n A 1 482 ASP 482 482 482 ASP ASP A . n A 1 483 LEU 483 483 483 LEU LEU A . n A 1 484 TYR 484 484 484 TYR TYR A . n A 1 485 LYS 485 485 485 LYS LYS A . n A 1 486 THR 486 486 486 THR THR A . n A 1 487 PRO 487 487 487 PRO PRO A . n A 1 488 ASP 488 488 488 ASP ASP A . n A 1 489 ASN 489 489 489 ASN ASN A . n A 1 490 ILE 490 490 490 ILE ILE A . n A 1 491 ASP 491 491 491 ASP ASP A . n A 1 492 ILE 492 492 492 ILE ILE A . n A 1 493 TRP 493 493 493 TRP TRP A . n A 1 494 ILE 494 494 494 ILE ILE A . n A 1 495 GLY 495 495 495 GLY GLY A . n A 1 496 GLY 496 496 496 GLY GLY A . n A 1 497 ASN 497 497 497 ASN ASN A . n A 1 498 ALA 498 498 498 ALA ALA A . n A 1 499 GLU 499 499 499 GLU GLU A . n A 1 500 PRO 500 500 500 PRO PRO A . n A 1 501 MET 501 501 501 MET MET A . n A 1 502 VAL 502 502 502 VAL VAL A . n A 1 503 GLU 503 503 503 GLU GLU A . n A 1 504 ARG 504 504 504 ARG ARG A . n A 1 505 GLY 505 505 505 GLY GLY A . n A 1 506 ARG 506 506 506 ARG ARG A . n A 1 507 VAL 507 507 507 VAL VAL A . n A 1 508 GLY 508 508 508 GLY GLY A . n A 1 509 PRO 509 509 509 PRO PRO A . n A 1 510 LEU 510 510 510 LEU LEU A . n A 1 511 LEU 511 511 511 LEU LEU A . n A 1 512 ALA 512 512 512 ALA ALA A . n A 1 513 CYS 513 513 513 CYS CYS A . n A 1 514 LEU 514 514 514 LEU LEU A . n A 1 515 LEU 515 515 515 LEU LEU A . n A 1 516 GLY 516 516 516 GLY GLY A . n A 1 517 ARG 517 517 517 ARG ARG A . n A 1 518 GLN 518 518 518 GLN GLN A . n A 1 519 PHE 519 519 519 PHE PHE A . n A 1 520 GLN 520 520 520 GLN GLN A . n A 1 521 GLN 521 521 521 GLN GLN A . n A 1 522 ILE 522 522 522 ILE ILE A . n A 1 523 ARG 523 523 523 ARG ARG A . n A 1 524 ASP 524 524 524 ASP ASP A . n A 1 525 GLY 525 525 525 GLY GLY A . n A 1 526 ASP 526 526 526 ASP ASP A . n A 1 527 ARG 527 527 527 ARG ARG A . n A 1 528 PHE 528 528 528 PHE PHE A . n A 1 529 TRP 529 529 529 TRP TRP A . n A 1 530 TRP 530 530 530 TRP TRP A . n A 1 531 GLU 531 531 531 GLU GLU A . n A 1 532 ASN 532 532 532 ASN ASN A . n A 1 533 PRO 533 533 533 PRO PRO A . n A 1 534 GLY 534 534 534 GLY GLY A . n A 1 535 VAL 535 535 535 VAL VAL A . n A 1 536 PHE 536 536 536 PHE PHE A . n A 1 537 THR 537 537 537 THR THR A . n A 1 538 GLU 538 538 538 GLU GLU A . n A 1 539 LYS 539 539 539 LYS LYS A . n A 1 540 GLN 540 540 540 GLN GLN A . n A 1 541 ARG 541 541 541 ARG ARG A . n A 1 542 ASP 542 542 542 ASP ASP A . n A 1 543 SER 543 543 543 SER SER A . n A 1 544 LEU 544 544 544 LEU LEU A . n A 1 545 GLN 545 545 545 GLN GLN A . n A 1 546 LYS 546 546 546 LYS LYS A . n A 1 547 VAL 547 547 547 VAL VAL A . n A 1 548 SER 548 548 548 SER SER A . n A 1 549 PHE 549 549 549 PHE PHE A . n A 1 550 SER 550 550 550 SER SER A . n A 1 551 ARG 551 551 551 ARG ARG A . n A 1 552 LEU 552 552 552 LEU LEU A . n A 1 553 ILE 553 553 553 ILE ILE A . n A 1 554 CYS 554 554 554 CYS CYS A . n A 1 555 ASP 555 555 555 ASP ASP A . n A 1 556 ASN 556 556 556 ASN ASN A . n A 1 557 THR 557 557 557 THR THR A . n A 1 558 HIS 558 558 558 HIS HIS A . n A 1 559 ILE 559 559 559 ILE ILE A . n A 1 560 THR 560 560 560 THR THR A . n A 1 561 LYS 561 561 561 LYS LYS A . n A 1 562 VAL 562 562 562 VAL VAL A . n A 1 563 PRO 563 563 563 PRO PRO A . n A 1 564 LEU 564 564 564 LEU LEU A . n A 1 565 HIS 565 565 565 HIS HIS A . n A 1 566 ALA 566 566 566 ALA ALA A . n A 1 567 PHE 567 567 567 PHE PHE A . n A 1 568 GLN 568 568 568 GLN GLN A . n A 1 569 ALA 569 569 569 ALA ALA A . n A 1 570 ASN 570 570 570 ASN ASN A . n A 1 571 ASN 571 571 571 ASN ASN A . n A 1 572 TYR 572 572 572 TYR TYR A . n A 1 573 PRO 573 573 573 PRO PRO A . n A 1 574 HIS 574 574 574 HIS HIS A . n A 1 575 ASP 575 575 575 ASP ASP A . n A 1 576 PHE 576 576 576 PHE PHE A . n A 1 577 VAL 577 577 577 VAL VAL A . n A 1 578 ASP 578 578 578 ASP ASP A . n A 1 579 CYS 579 579 579 CYS CYS A . n A 1 580 SER 580 580 580 SER SER A . n A 1 581 ALA 581 581 581 ALA ALA A . n A 1 582 VAL 582 582 582 VAL VAL A . n A 1 583 ASP 583 583 583 ASP ASP A . n A 1 584 LYS 584 584 584 LYS LYS A . n A 1 585 LEU 585 585 585 LEU LEU A . n A 1 586 ASP 586 586 586 ASP ASP A . n A 1 587 LEU 587 587 587 LEU LEU A . n A 1 588 SER 588 588 588 SER SER A . n A 1 589 PRO 589 589 589 PRO PRO A . n A 1 590 TRP 590 590 590 TRP TRP A . n A 1 591 ALA 591 591 591 ALA ALA A . n A 1 592 SER 592 592 592 SER SER A . n A 1 593 ARG 593 593 593 ARG ARG A . n A 1 594 GLU 594 594 594 GLU GLU A . n A 1 595 ASN 595 595 595 ASN ASN A . n B 1 1 SER 1 1 1 SER SER B . n B 1 2 TRP 2 2 2 TRP TRP B . n B 1 3 GLU 3 3 3 GLU GLU B . n B 1 4 VAL 4 4 4 VAL VAL B . n B 1 5 GLY 5 5 5 GLY GLY B . n B 1 6 CYS 6 6 6 CYS CYS B . n B 1 7 GLY 7 7 7 GLY GLY B . n B 1 8 ALA 8 8 8 ALA ALA B . n B 1 9 PRO 9 9 9 PRO PRO B . n B 1 10 VAL 10 10 10 VAL VAL B . n B 1 11 PRO 11 11 11 PRO PRO B . n B 1 12 LEU 12 12 12 LEU LEU B . n B 1 13 VAL 13 13 13 VAL VAL B . n B 1 14 THR 14 14 14 THR THR B . n B 1 15 CYS 15 15 15 CYS CYS B . n B 1 16 ASP 16 16 16 ASP ASP B . n B 1 17 GLU 17 17 17 GLU GLU B . n B 1 18 GLN 18 18 18 GLN GLN B . n B 1 19 SER 19 19 19 SER SER B . n B 1 20 PRO 20 20 20 PRO PRO B . n B 1 21 TYR 21 21 21 TYR TYR B . n B 1 22 ARG 22 22 22 ARG ARG B . n B 1 23 THR 23 23 23 THR THR B . n B 1 24 ILE 24 24 24 ILE ILE B . n B 1 25 THR 25 25 25 THR THR B . n B 1 26 GLY 26 26 26 GLY GLY B . n B 1 27 ASP 27 27 27 ASP ASP B . n B 1 28 CYS 28 28 28 CYS CYS B . n B 1 29 ASN 29 29 29 ASN ASN B . n B 1 30 ASN 30 30 30 ASN ASN B . n B 1 31 ARG 31 31 31 ARG ARG B . n B 1 32 ARG 32 32 32 ARG ARG B . n B 1 33 SER 33 33 33 SER SER B . n B 1 34 PRO 34 34 34 PRO PRO B . n B 1 35 ALA 35 35 35 ALA ALA B . n B 1 36 LEU 36 36 36 LEU LEU B . n B 1 37 GLY 37 37 37 GLY GLY B . n B 1 38 ALA 38 38 38 ALA ALA B . n B 1 39 ALA 39 39 39 ALA ALA B . n B 1 40 ASN 40 40 40 ASN ASN B . n B 1 41 ARG 41 41 41 ARG ARG B . n B 1 42 ALA 42 42 42 ALA ALA B . n B 1 43 LEU 43 43 43 LEU LEU B . n B 1 44 ALA 44 44 44 ALA ALA B . n B 1 45 ARG 45 45 45 ARG ARG B . n B 1 46 TRP 46 46 46 TRP TRP B . n B 1 47 LEU 47 47 47 LEU LEU B . n B 1 48 PRO 48 48 48 PRO PRO B . n B 1 49 ALA 49 49 49 ALA ALA B . n B 1 50 GLU 50 50 50 GLU GLU B . n B 1 51 TYR 51 51 51 TYR TYR B . n B 1 52 GLU 52 52 52 GLU GLU B . n B 1 53 ASP 53 53 53 ASP ASP B . n B 1 54 GLY 54 54 54 GLY GLY B . n B 1 55 LEU 55 55 55 LEU LEU B . n B 1 56 ALA 56 56 56 ALA ALA B . n B 1 57 VAL 57 57 57 VAL VAL B . n B 1 58 PRO 58 58 58 PRO PRO B . n B 1 59 PHE 59 59 59 PHE PHE B . n B 1 60 GLY 60 60 60 GLY GLY B . n B 1 61 TRP 61 61 61 TRP TRP B . n B 1 62 THR 62 62 62 THR THR B . n B 1 63 GLN 63 63 63 GLN GLN B . n B 1 64 ARG 64 64 64 ARG ARG B . n B 1 65 LYS 65 65 65 LYS LYS B . n B 1 66 THR 66 66 66 THR THR B . n B 1 67 ARG 67 67 67 ARG ARG B . n B 1 68 ASN 68 68 68 ASN ASN B . n B 1 69 GLY 69 69 69 GLY GLY B . n B 1 70 PHE 70 70 70 PHE PHE B . n B 1 71 ARG 71 71 71 ARG ARG B . n B 1 72 VAL 72 72 72 VAL VAL B . n B 1 73 PRO 73 73 73 PRO PRO B . n B 1 74 LEU 74 74 74 LEU LEU B . n B 1 75 ALA 75 75 75 ALA ALA B . n B 1 76 ARG 76 76 76 ARG ARG B . n B 1 77 GLU 77 77 77 GLU GLU B . n B 1 78 VAL 78 78 78 VAL VAL B . n B 1 79 SER 79 79 79 SER SER B . n B 1 80 ASN 80 80 80 ASN ASN B . n B 1 81 LYS 81 81 81 LYS LYS B . n B 1 82 ILE 82 82 82 ILE ILE B . n B 1 83 VAL 83 83 83 VAL VAL B . n B 1 84 GLY 84 84 84 GLY GLY B . n B 1 85 TYR 85 85 85 TYR TYR B . n B 1 86 LEU 86 86 86 LEU LEU B . n B 1 87 ASP 87 87 87 ASP ASP B . n B 1 88 GLU 88 88 88 GLU GLU B . n B 1 89 GLU 89 89 89 GLU GLU B . n B 1 90 GLY 90 90 90 GLY GLY B . n B 1 91 VAL 91 91 91 VAL VAL B . n B 1 92 LEU 92 92 92 LEU LEU B . n B 1 93 ASP 93 93 93 ASP ASP B . n B 1 94 GLN 94 94 94 GLN GLN B . n B 1 95 ASN 95 95 95 ASN ASN B . n B 1 96 ARG 96 96 96 ARG ARG B . n B 1 97 SER 97 97 97 SER SER B . n B 1 98 LEU 98 98 98 LEU LEU B . n B 1 99 LEU 99 99 99 LEU LEU B . n B 1 100 PHE 100 100 100 PHE PHE B . n B 1 101 MET 101 101 101 MET MET B . n B 1 102 GLN 102 102 102 GLN GLN B . n B 1 103 TRP 103 103 103 TRP TRP B . n B 1 104 GLY 104 104 104 GLY GLY B . n B 1 105 GLN 105 105 105 GLN GLN B . n B 1 106 ILE 106 106 106 ILE ILE B . n B 1 107 VAL 107 107 107 VAL VAL B . n B 1 108 ASP 108 108 108 ASP ASP B . n B 1 109 HIS 109 109 109 HIS HIS B . n B 1 110 ASP 110 110 110 ASP ASP B . n B 1 111 LEU 111 111 111 LEU LEU B . n B 1 112 ASP 112 112 112 ASP ASP B . n B 1 113 PHE 113 113 113 PHE PHE B . n B 1 114 ALA 114 114 114 ALA ALA B . n B 1 115 PRO 115 115 115 PRO PRO B . n B 1 116 GLU 116 116 116 GLU GLU B . n B 1 117 THR 117 117 117 THR THR B . n B 1 118 GLU 118 118 118 GLU GLU B . n B 1 119 LEU 119 119 119 LEU LEU B . n B 1 120 GLY 120 120 120 GLY GLY B . n B 1 121 SER 121 121 121 SER SER B . n B 1 122 SER 122 122 122 SER SER B . n B 1 123 GLU 123 123 123 GLU GLU B . n B 1 124 HIS 124 124 124 HIS HIS B . n B 1 125 SER 125 125 125 SER SER B . n B 1 126 LYS 126 126 126 LYS LYS B . n B 1 127 VAL 127 127 127 VAL VAL B . n B 1 128 GLN 128 128 128 GLN GLN B . n B 1 129 CYS 129 129 129 CYS CYS B . n B 1 130 GLU 130 130 130 GLU GLU B . n B 1 131 GLU 131 131 131 GLU GLU B . n B 1 132 TYR 132 132 132 TYR TYR B . n B 1 133 CYS 133 133 133 CYS CYS B . n B 1 134 VAL 134 134 134 VAL VAL B . n B 1 135 GLN 135 135 135 GLN GLN B . n B 1 136 GLY 136 136 136 GLY GLY B . n B 1 137 ASP 137 137 137 ASP ASP B . n B 1 138 GLU 138 138 138 GLU GLU B . n B 1 139 CYS 139 139 139 CYS CYS B . n B 1 140 PHE 140 140 140 PHE PHE B . n B 1 141 PRO 141 141 141 PRO PRO B . n B 1 142 ILE 142 142 142 ILE ILE B . n B 1 143 MET 143 143 143 MET MET B . n B 1 144 PHE 144 144 144 PHE PHE B . n B 1 145 PRO 145 145 145 PRO PRO B . n B 1 146 LYS 146 146 146 LYS LYS B . n B 1 147 ASN 147 147 147 ASN ASN B . n B 1 148 ASP 148 148 148 ASP ASP B . n B 1 149 PRO 149 149 149 PRO PRO B . n B 1 150 LYS 150 150 150 LYS LYS B . n B 1 151 LEU 151 151 151 LEU LEU B . n B 1 152 LYS 152 152 152 LYS LYS B . n B 1 153 THR 153 153 153 THR THR B . n B 1 154 GLN 154 154 154 GLN GLN B . n B 1 155 GLY 155 155 155 GLY GLY B . n B 1 156 LYS 156 156 156 LYS LYS B . n B 1 157 CYS 157 157 157 CYS CYS B . n B 1 158 MET 158 158 158 MET MET B . n B 1 159 PRO 159 159 159 PRO PRO B . n B 1 160 PHE 160 160 160 PHE PHE B . n B 1 161 PHE 161 161 161 PHE PHE B . n B 1 162 ARG 162 162 162 ARG ARG B . n B 1 163 ALA 163 163 163 ALA ALA B . n B 1 164 GLY 164 164 164 GLY GLY B . n B 1 165 PHE 165 165 165 PHE PHE B . n B 1 166 VAL 166 166 166 VAL VAL B . n B 1 167 CYS 167 167 167 CYS CYS B . n B 1 168 PRO 168 168 168 PRO PRO B . n B 1 169 THR 169 169 169 THR THR B . n B 1 170 PRO 170 170 170 PRO PRO B . n B 1 171 PRO 171 171 171 PRO PRO B . n B 1 172 TYR 172 172 172 TYR TYR B . n B 1 173 GLN 173 173 173 GLN GLN B . n B 1 174 SER 174 174 174 SER SER B . n B 1 175 LEU 175 175 175 LEU LEU B . n B 1 176 ALA 176 176 176 ALA ALA B . n B 1 177 ARG 177 177 177 ARG ARG B . n B 1 178 ASP 178 178 178 ASP ASP B . n B 1 179 GLN 179 179 179 GLN GLN B . n B 1 180 ILE 180 180 180 ILE ILE B . n B 1 181 ASN 181 181 181 ASN ASN B . n B 1 182 ALA 182 182 182 ALA ALA B . n B 1 183 VAL 183 183 183 VAL VAL B . n B 1 184 THR 184 184 184 THR THR B . n B 1 185 SER 185 185 185 SER SER B . n B 1 186 PHE 186 186 186 PHE PHE B . n B 1 187 LEU 187 187 187 LEU LEU B . n B 1 188 ASP 188 188 188 ASP ASP B . n B 1 189 ALA 189 189 189 ALA ALA B . n B 1 190 SER 190 190 190 SER SER B . n B 1 191 LEU 191 191 191 LEU LEU B . n B 1 192 VAL 192 192 192 VAL VAL B . n B 1 193 TYR 193 193 193 TYR TYR B . n B 1 194 GLY 194 194 194 GLY GLY B . n B 1 195 SER 195 195 195 SER SER B . n B 1 196 GLU 196 196 196 GLU GLU B . n B 1 197 PRO 197 197 197 PRO PRO B . n B 1 198 SER 198 198 198 SER SER B . n B 1 199 LEU 199 199 199 LEU LEU B . n B 1 200 ALA 200 200 200 ALA ALA B . n B 1 201 SER 201 201 201 SER SER B . n B 1 202 ARG 202 202 202 ARG ARG B . n B 1 203 LEU 203 203 203 LEU LEU B . n B 1 204 ARG 204 204 204 ARG ARG B . n B 1 205 ASN 205 205 205 ASN ASN B . n B 1 206 LEU 206 206 206 LEU LEU B . n B 1 207 SER 207 207 207 SER SER B . n B 1 208 SER 208 208 208 SER SER B . n B 1 209 PRO 209 209 209 PRO PRO B . n B 1 210 LEU 210 210 210 LEU LEU B . n B 1 211 GLY 211 211 211 GLY GLY B . n B 1 212 LEU 212 212 212 LEU LEU B . n B 1 213 MET 213 213 213 MET MET B . n B 1 214 ALA 214 214 214 ALA ALA B . n B 1 215 VAL 215 215 215 VAL VAL B . n B 1 216 ASN 216 216 216 ASN ASN B . n B 1 217 GLN 217 217 217 GLN GLN B . n B 1 218 GLU 218 218 218 GLU GLU B . n B 1 219 ALA 219 219 219 ALA ALA B . n B 1 220 TRP 220 220 220 TRP TRP B . n B 1 221 ASP 221 221 221 ASP ASP B . n B 1 222 HIS 222 222 222 HIS HIS B . n B 1 223 GLY 223 223 223 GLY GLY B . n B 1 224 LEU 224 224 224 LEU LEU B . n B 1 225 ALA 225 225 225 ALA ALA B . n B 1 226 TYR 226 226 226 TYR TYR B . n B 1 227 PRO 227 227 227 PRO PRO B . n B 1 228 PRO 228 228 228 PRO PRO B . n B 1 229 PHE 229 229 229 PHE PHE B . n B 1 230 ASN 230 230 230 ASN ASN B . n B 1 231 ASN 231 231 231 ASN ASN B . n B 1 232 VAL 232 232 232 VAL VAL B . n B 1 233 LYS 233 233 233 LYS LYS B . n B 1 234 PRO 234 234 234 PRO PRO B . n B 1 235 SER 235 235 235 SER SER B . n B 1 236 PRO 236 236 236 PRO PRO B . n B 1 237 CYS 237 237 237 CYS CYS B . n B 1 238 GLU 238 238 238 GLU GLU B . n B 1 239 PHE 239 239 239 PHE PHE B . n B 1 240 ILE 240 240 240 ILE ILE B . n B 1 241 ASN 241 241 241 ASN ASN B . n B 1 242 THR 242 242 242 THR THR B . n B 1 243 THR 243 243 243 THR THR B . n B 1 244 ALA 244 244 244 ALA ALA B . n B 1 245 HIS 245 245 245 HIS HIS B . n B 1 246 VAL 246 246 246 VAL VAL B . n B 1 247 PRO 247 247 247 PRO PRO B . n B 1 248 CYS 248 248 248 CYS CYS B . n B 1 249 PHE 249 249 249 PHE PHE B . n B 1 250 GLN 250 250 250 GLN GLN B . n B 1 251 ALA 251 251 251 ALA ALA B . n B 1 252 GLY 252 252 252 GLY GLY B . n B 1 253 ASP 253 253 253 ASP ASP B . n B 1 254 SER 254 254 254 SER SER B . n B 1 255 ARG 255 255 255 ARG ARG B . n B 1 256 ALA 256 256 256 ALA ALA B . n B 1 257 SER 257 257 257 SER SER B . n B 1 258 GLU 258 258 258 GLU GLU B . n B 1 259 GLN 259 259 259 GLN GLN B . n B 1 260 ILE 260 260 260 ILE ILE B . n B 1 261 LEU 261 261 261 LEU LEU B . n B 1 262 LEU 262 262 262 LEU LEU B . n B 1 263 ALA 263 263 263 ALA ALA B . n B 1 264 THR 264 264 264 THR THR B . n B 1 265 VAL 265 265 265 VAL VAL B . n B 1 266 HIS 266 266 266 HIS HIS B . n B 1 267 THR 267 267 267 THR THR B . n B 1 268 LEU 268 268 268 LEU LEU B . n B 1 269 LEU 269 269 269 LEU LEU B . n B 1 270 LEU 270 270 270 LEU LEU B . n B 1 271 ARG 271 271 271 ARG ARG B . n B 1 272 GLU 272 272 272 GLU GLU B . n B 1 273 HIS 273 273 273 HIS HIS B . n B 1 274 ASN 274 274 274 ASN ASN B . n B 1 275 ARG 275 275 275 ARG ARG B . n B 1 276 LEU 276 276 276 LEU LEU B . n B 1 277 ALA 277 277 277 ALA ALA B . n B 1 278 ARG 278 278 278 ARG ARG B . n B 1 279 GLU 279 279 279 GLU GLU B . n B 1 280 LEU 280 280 280 LEU LEU B . n B 1 281 LYS 281 281 281 LYS LYS B . n B 1 282 ARG 282 282 282 ARG ARG B . n B 1 283 LEU 283 283 283 LEU LEU B . n B 1 284 ASN 284 284 284 ASN ASN B . n B 1 285 PRO 285 285 285 PRO PRO B . n B 1 286 HIS 286 286 286 HIS HIS B . n B 1 287 TRP 287 287 287 TRP TRP B . n B 1 288 ASP 288 288 288 ASP ASP B . n B 1 289 GLY 289 289 289 GLY GLY B . n B 1 290 GLU 290 290 290 GLU GLU B . n B 1 291 MET 291 291 291 MET MET B . n B 1 292 LEU 292 292 292 LEU LEU B . n B 1 293 TYR 293 293 293 TYR TYR B . n B 1 294 GLN 294 294 294 GLN GLN B . n B 1 295 GLU 295 295 295 GLU GLU B . n B 1 296 ALA 296 296 296 ALA ALA B . n B 1 297 ARG 297 297 297 ARG ARG B . n B 1 298 LYS 298 298 298 LYS LYS B . n B 1 299 ILE 299 299 299 ILE ILE B . n B 1 300 LEU 300 300 300 LEU LEU B . n B 1 301 GLY 301 301 301 GLY GLY B . n B 1 302 ALA 302 302 302 ALA ALA B . n B 1 303 PHE 303 303 303 PHE PHE B . n B 1 304 ILE 304 304 304 ILE ILE B . n B 1 305 GLN 305 305 305 GLN GLN B . n B 1 306 ILE 306 306 306 ILE ILE B . n B 1 307 ILE 307 307 307 ILE ILE B . n B 1 308 THR 308 308 308 THR THR B . n B 1 309 PHE 309 309 309 PHE PHE B . n B 1 310 ARG 310 310 310 ARG ARG B . n B 1 311 ASP 311 311 311 ASP ASP B . n B 1 312 TYR 312 312 312 TYR TYR B . n B 1 313 LEU 313 313 313 LEU LEU B . n B 1 314 PRO 314 314 314 PRO PRO B . n B 1 315 ILE 315 315 315 ILE ILE B . n B 1 316 VAL 316 316 316 VAL VAL B . n B 1 317 LEU 317 317 317 LEU LEU B . n B 1 318 GLY 318 318 318 GLY GLY B . n B 1 319 SER 319 319 319 SER SER B . n B 1 320 GLU 320 320 320 GLU GLU B . n B 1 321 MET 321 321 321 MET MET B . n B 1 322 GLN 322 322 322 GLN GLN B . n B 1 323 LYS 323 323 323 LYS LYS B . n B 1 324 TRP 324 324 324 TRP TRP B . n B 1 325 ILE 325 325 325 ILE ILE B . n B 1 326 PRO 326 326 326 PRO PRO B . n B 1 327 PRO 327 327 327 PRO PRO B . n B 1 328 TYR 328 328 328 TYR TYR B . n B 1 329 GLN 329 329 329 GLN GLN B . n B 1 330 GLY 330 330 330 GLY GLY B . n B 1 331 TYR 331 331 331 TYR TYR B . n B 1 332 ASN 332 332 332 ASN ASN B . n B 1 333 ASN 333 333 333 ASN ASN B . n B 1 334 SER 334 334 334 SER SER B . n B 1 335 VAL 335 335 335 VAL VAL B . n B 1 336 ASP 336 336 336 ASP ASP B . n B 1 337 PRO 337 337 337 PRO PRO B . n B 1 338 ARG 338 338 338 ARG ARG B . n B 1 339 ILE 339 339 339 ILE ILE B . n B 1 340 SER 340 340 340 SER SER B . n B 1 341 ASN 341 341 341 ASN ASN B . n B 1 342 VAL 342 342 342 VAL VAL B . n B 1 343 PHE 343 343 343 PHE PHE B . n B 1 344 THR 344 344 344 THR THR B . n B 1 345 PHE 345 345 345 PHE PHE B . n B 1 346 ALA 346 346 346 ALA ALA B . n B 1 347 PHE 347 347 347 PHE PHE B . n B 1 348 ARG 348 348 348 ARG ARG B . n B 1 349 PHE 349 349 349 PHE PHE B . n B 1 350 GLY 350 350 350 GLY GLY B . n B 1 351 HIS 351 351 351 HIS HIS B . n B 1 352 MET 352 352 352 MET MET B . n B 1 353 GLU 353 353 353 GLU GLU B . n B 1 354 VAL 354 354 354 VAL VAL B . n B 1 355 PRO 355 355 355 PRO PRO B . n B 1 356 SER 356 356 356 SER SER B . n B 1 357 THR 357 357 357 THR THR B . n B 1 358 VAL 358 358 358 VAL VAL B . n B 1 359 SER 359 359 359 SER SER B . n B 1 360 ARG 360 360 360 ARG ARG B . n B 1 361 LEU 361 361 361 LEU LEU B . n B 1 362 ASP 362 362 362 ASP ASP B . n B 1 363 GLU 363 363 363 GLU GLU B . n B 1 364 ASN 364 364 364 ASN ASN B . n B 1 365 TYR 365 365 365 TYR TYR B . n B 1 366 GLN 366 366 366 GLN GLN B . n B 1 367 PRO 367 367 367 PRO PRO B . n B 1 368 TRP 368 368 368 TRP TRP B . n B 1 369 GLY 369 369 369 GLY GLY B . n B 1 370 PRO 370 370 370 PRO PRO B . n B 1 371 GLU 371 371 371 GLU GLU B . n B 1 372 ALA 372 372 372 ALA ALA B . n B 1 373 GLU 373 373 373 GLU GLU B . n B 1 374 LEU 374 374 374 LEU LEU B . n B 1 375 PRO 375 375 375 PRO PRO B . n B 1 376 LEU 376 376 376 LEU LEU B . n B 1 377 HIS 377 377 377 HIS HIS B . n B 1 378 THR 378 378 378 THR THR B . n B 1 379 LEU 379 379 379 LEU LEU B . n B 1 380 PHE 380 380 380 PHE PHE B . n B 1 381 PHE 381 381 381 PHE PHE B . n B 1 382 ASN 382 382 382 ASN ASN B . n B 1 383 THR 383 383 383 THR THR B . n B 1 384 TRP 384 384 384 TRP TRP B . n B 1 385 ARG 385 385 385 ARG ARG B . n B 1 386 ILE 386 386 386 ILE ILE B . n B 1 387 ILE 387 387 387 ILE ILE B . n B 1 388 LYS 388 388 388 LYS LYS B . n B 1 389 ASP 389 389 389 ASP ASP B . n B 1 390 GLY 390 390 390 GLY GLY B . n B 1 391 GLY 391 391 391 GLY GLY B . n B 1 392 ILE 392 392 392 ILE ILE B . n B 1 393 ASP 393 393 393 ASP ASP B . n B 1 394 PRO 394 394 394 PRO PRO B . n B 1 395 LEU 395 395 395 LEU LEU B . n B 1 396 VAL 396 396 396 VAL VAL B . n B 1 397 ARG 397 397 397 ARG ARG B . n B 1 398 GLY 398 398 398 GLY GLY B . n B 1 399 LEU 399 399 399 LEU LEU B . n B 1 400 LEU 400 400 400 LEU LEU B . n B 1 401 ALA 401 401 401 ALA ALA B . n B 1 402 LYS 402 402 402 LYS LYS B . n B 1 403 ASN 403 403 403 ASN ASN B . n B 1 404 SER 404 404 404 SER SER B . n B 1 405 LYS 405 405 405 LYS LYS B . n B 1 406 LEU 406 406 406 LEU LEU B . n B 1 407 MET 407 407 407 MET MET B . n B 1 408 ASN 408 408 408 ASN ASN B . n B 1 409 GLN 409 409 409 GLN GLN B . n B 1 410 ASN 410 410 410 ASN ASN B . n B 1 411 LYS 411 411 411 LYS LYS B . n B 1 412 MET 412 412 412 MET MET B . n B 1 413 VAL 413 413 413 VAL VAL B . n B 1 414 THR 414 414 414 THR THR B . n B 1 415 SER 415 415 415 SER SER B . n B 1 416 GLU 416 416 416 GLU GLU B . n B 1 417 LEU 417 417 417 LEU LEU B . n B 1 418 ARG 418 418 418 ARG ARG B . n B 1 419 ASN 419 419 419 ASN ASN B . n B 1 420 LYS 420 420 420 LYS LYS B . n B 1 421 LEU 421 421 421 LEU LEU B . n B 1 422 PHE 422 422 422 PHE PHE B . n B 1 423 GLN 423 423 423 GLN GLN B . n B 1 424 PRO 424 424 424 PRO PRO B . n B 1 425 THR 425 425 425 THR THR B . n B 1 426 HIS 426 426 426 HIS HIS B . n B 1 427 LYS 427 427 427 LYS LYS B . n B 1 428 VAL 428 428 428 VAL VAL B . n B 1 429 HIS 429 429 429 HIS HIS B . n B 1 430 GLY 430 430 430 GLY GLY B . n B 1 431 PHE 431 431 431 PHE PHE B . n B 1 432 ASP 432 432 432 ASP ASP B . n B 1 433 LEU 433 433 433 LEU LEU B . n B 1 434 ALA 434 434 434 ALA ALA B . n B 1 435 ALA 435 435 435 ALA ALA B . n B 1 436 ILE 436 436 436 ILE ILE B . n B 1 437 ASN 437 437 437 ASN ASN B . n B 1 438 LEU 438 438 438 LEU LEU B . n B 1 439 GLN 439 439 439 GLN GLN B . n B 1 440 ARG 440 440 440 ARG ARG B . n B 1 441 CYS 441 441 441 CYS CYS B . n B 1 442 ARG 442 442 442 ARG ARG B . n B 1 443 ASP 443 443 443 ASP ASP B . n B 1 444 HIS 444 444 444 HIS HIS B . n B 1 445 GLY 445 445 445 GLY GLY B . n B 1 446 MET 446 446 446 MET MET B . n B 1 447 PRO 447 447 447 PRO PRO B . n B 1 448 GLY 448 448 448 GLY GLY B . n B 1 449 TYR 449 449 449 TYR TYR B . n B 1 450 ASN 450 450 450 ASN ASN B . n B 1 451 SER 451 451 451 SER SER B . n B 1 452 TRP 452 452 452 TRP TRP B . n B 1 453 ARG 453 453 453 ARG ARG B . n B 1 454 GLY 454 454 454 GLY GLY B . n B 1 455 PHE 455 455 455 PHE PHE B . n B 1 456 CYS 456 456 456 CYS CYS B . n B 1 457 GLY 457 457 457 GLY GLY B . n B 1 458 LEU 458 458 458 LEU LEU B . n B 1 459 SER 459 459 459 SER SER B . n B 1 460 GLN 460 460 460 GLN GLN B . n B 1 461 PRO 461 461 461 PRO PRO B . n B 1 462 LYS 462 462 462 LYS LYS B . n B 1 463 THR 463 463 463 THR THR B . n B 1 464 LEU 464 464 464 LEU LEU B . n B 1 465 LYS 465 465 465 LYS LYS B . n B 1 466 GLY 466 466 466 GLY GLY B . n B 1 467 LEU 467 467 467 LEU LEU B . n B 1 468 GLN 468 468 468 GLN GLN B . n B 1 469 ALA 469 469 469 ALA ALA B . n B 1 470 VAL 470 470 470 VAL VAL B . n B 1 471 LEU 471 471 471 LEU LEU B . n B 1 472 LYS 472 472 472 LYS LYS B . n B 1 473 ASN 473 473 473 ASN ASN B . n B 1 474 LYS 474 474 474 LYS LYS B . n B 1 475 VAL 475 475 475 VAL VAL B . n B 1 476 LEU 476 476 476 LEU LEU B . n B 1 477 ALA 477 477 477 ALA ALA B . n B 1 478 LYS 478 478 478 LYS LYS B . n B 1 479 LYS 479 479 479 LYS LYS B . n B 1 480 LEU 480 480 480 LEU LEU B . n B 1 481 LEU 481 481 481 LEU LEU B . n B 1 482 ASP 482 482 482 ASP ASP B . n B 1 483 LEU 483 483 483 LEU LEU B . n B 1 484 TYR 484 484 484 TYR TYR B . n B 1 485 LYS 485 485 485 LYS LYS B . n B 1 486 THR 486 486 486 THR THR B . n B 1 487 PRO 487 487 487 PRO PRO B . n B 1 488 ASP 488 488 488 ASP ASP B . n B 1 489 ASN 489 489 489 ASN ASN B . n B 1 490 ILE 490 490 490 ILE ILE B . n B 1 491 ASP 491 491 491 ASP ASP B . n B 1 492 ILE 492 492 492 ILE ILE B . n B 1 493 TRP 493 493 493 TRP TRP B . n B 1 494 ILE 494 494 494 ILE ILE B . n B 1 495 GLY 495 495 495 GLY GLY B . n B 1 496 GLY 496 496 496 GLY GLY B . n B 1 497 ASN 497 497 497 ASN ASN B . n B 1 498 ALA 498 498 498 ALA ALA B . n B 1 499 GLU 499 499 499 GLU GLU B . n B 1 500 PRO 500 500 500 PRO PRO B . n B 1 501 MET 501 501 501 MET MET B . n B 1 502 VAL 502 502 502 VAL VAL B . n B 1 503 GLU 503 503 503 GLU GLU B . n B 1 504 ARG 504 504 504 ARG ARG B . n B 1 505 GLY 505 505 505 GLY GLY B . n B 1 506 ARG 506 506 506 ARG ARG B . n B 1 507 VAL 507 507 507 VAL VAL B . n B 1 508 GLY 508 508 508 GLY GLY B . n B 1 509 PRO 509 509 509 PRO PRO B . n B 1 510 LEU 510 510 510 LEU LEU B . n B 1 511 LEU 511 511 511 LEU LEU B . n B 1 512 ALA 512 512 512 ALA ALA B . n B 1 513 CYS 513 513 513 CYS CYS B . n B 1 514 LEU 514 514 514 LEU LEU B . n B 1 515 LEU 515 515 515 LEU LEU B . n B 1 516 GLY 516 516 516 GLY GLY B . n B 1 517 ARG 517 517 517 ARG ARG B . n B 1 518 GLN 518 518 518 GLN GLN B . n B 1 519 PHE 519 519 519 PHE PHE B . n B 1 520 GLN 520 520 520 GLN GLN B . n B 1 521 GLN 521 521 521 GLN GLN B . n B 1 522 ILE 522 522 522 ILE ILE B . n B 1 523 ARG 523 523 523 ARG ARG B . n B 1 524 ASP 524 524 524 ASP ASP B . n B 1 525 GLY 525 525 525 GLY GLY B . n B 1 526 ASP 526 526 526 ASP ASP B . n B 1 527 ARG 527 527 527 ARG ARG B . n B 1 528 PHE 528 528 528 PHE PHE B . n B 1 529 TRP 529 529 529 TRP TRP B . n B 1 530 TRP 530 530 530 TRP TRP B . n B 1 531 GLU 531 531 531 GLU GLU B . n B 1 532 ASN 532 532 532 ASN ASN B . n B 1 533 PRO 533 533 533 PRO PRO B . n B 1 534 GLY 534 534 534 GLY GLY B . n B 1 535 VAL 535 535 535 VAL VAL B . n B 1 536 PHE 536 536 536 PHE PHE B . n B 1 537 THR 537 537 537 THR THR B . n B 1 538 GLU 538 538 538 GLU GLU B . n B 1 539 LYS 539 539 539 LYS LYS B . n B 1 540 GLN 540 540 540 GLN GLN B . n B 1 541 ARG 541 541 541 ARG ARG B . n B 1 542 ASP 542 542 542 ASP ASP B . n B 1 543 SER 543 543 543 SER SER B . n B 1 544 LEU 544 544 544 LEU LEU B . n B 1 545 GLN 545 545 545 GLN GLN B . n B 1 546 LYS 546 546 546 LYS LYS B . n B 1 547 VAL 547 547 547 VAL VAL B . n B 1 548 SER 548 548 548 SER SER B . n B 1 549 PHE 549 549 549 PHE PHE B . n B 1 550 SER 550 550 550 SER SER B . n B 1 551 ARG 551 551 551 ARG ARG B . n B 1 552 LEU 552 552 552 LEU LEU B . n B 1 553 ILE 553 553 553 ILE ILE B . n B 1 554 CYS 554 554 554 CYS CYS B . n B 1 555 ASP 555 555 555 ASP ASP B . n B 1 556 ASN 556 556 556 ASN ASN B . n B 1 557 THR 557 557 557 THR THR B . n B 1 558 HIS 558 558 558 HIS HIS B . n B 1 559 ILE 559 559 559 ILE ILE B . n B 1 560 THR 560 560 560 THR THR B . n B 1 561 LYS 561 561 561 LYS LYS B . n B 1 562 VAL 562 562 562 VAL VAL B . n B 1 563 PRO 563 563 563 PRO PRO B . n B 1 564 LEU 564 564 564 LEU LEU B . n B 1 565 HIS 565 565 565 HIS HIS B . n B 1 566 ALA 566 566 566 ALA ALA B . n B 1 567 PHE 567 567 567 PHE PHE B . n B 1 568 GLN 568 568 568 GLN GLN B . n B 1 569 ALA 569 569 569 ALA ALA B . n B 1 570 ASN 570 570 570 ASN ASN B . n B 1 571 ASN 571 571 571 ASN ASN B . n B 1 572 TYR 572 572 572 TYR TYR B . n B 1 573 PRO 573 573 573 PRO PRO B . n B 1 574 HIS 574 574 574 HIS HIS B . n B 1 575 ASP 575 575 575 ASP ASP B . n B 1 576 PHE 576 576 576 PHE PHE B . n B 1 577 VAL 577 577 577 VAL VAL B . n B 1 578 ASP 578 578 578 ASP ASP B . n B 1 579 CYS 579 579 579 CYS CYS B . n B 1 580 SER 580 580 580 SER SER B . n B 1 581 ALA 581 581 581 ALA ALA B . n B 1 582 VAL 582 582 582 VAL VAL B . n B 1 583 ASP 583 583 583 ASP ASP B . n B 1 584 LYS 584 584 584 LYS LYS B . n B 1 585 LEU 585 585 585 LEU LEU B . n B 1 586 ASP 586 586 586 ASP ASP B . n B 1 587 LEU 587 587 587 LEU LEU B . n B 1 588 SER 588 588 588 SER SER B . n B 1 589 PRO 589 589 589 PRO PRO B . n B 1 590 TRP 590 590 590 TRP TRP B . n B 1 591 ALA 591 591 591 ALA ALA B . n B 1 592 SER 592 592 592 SER SER B . n B 1 593 ARG 593 593 593 ARG ARG B . n B 1 594 GLU 594 594 594 GLU GLU B . n B 1 595 ASN 595 595 595 ASN ASN B . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code C 2 MMZ 1 601 618 MMZ MMZ A . D 2 MMZ 1 602 616 MMZ MMZ A . E 3 NAG 1 603 602 NAG NAG A . F 3 NAG 1 604 603 NAG NAG A . G 3 NAG 1 605 904 NAG NAG A . H 3 NAG 1 606 605 NAG NAG A . I 4 HEM 1 607 601 HEM HEM A . J 5 CA 1 608 606 CA CA A . K 6 NO3 1 609 607 NO3 NO3 A . L 6 NO3 1 610 608 NO3 NO3 A . M 6 NO3 1 611 1609 NO3 NO3 A . N 6 NO3 1 612 1610 NO3 NO3 A . O 6 NO3 1 613 611 NO3 NO3 A . P 7 GOL 1 614 612 GOL GOL A . Q 7 GOL 1 615 1613 GOL GOL A . R 7 GOL 1 616 1614 GOL GOL A . S 7 GOL 1 617 1615 GOL GOL A . T 2 MMZ 1 601 619 MMZ MMZ B . U 3 NAG 1 602 903 NAG NAG B . V 3 NAG 1 603 604 NAG NAG B . W 3 NAG 1 604 606 NAG NAG B . X 3 NAG 1 605 607 NAG NAG B . Y 3 NAG 2 606 608 NAG NAG B . Z 4 HEM 1 607 602 HEM HEM B . AA 5 CA 1 608 601 CA CA B . BA 6 NO3 1 609 609 NO3 NO3 B . CA 6 NO3 1 610 610 NO3 NO3 B . DA 6 NO3 1 611 1611 NO3 NO3 B . EA 6 NO3 1 612 612 NO3 NO3 B . FA 2 MMZ 1 613 620 MMZ MMZ B . GA 7 GOL 1 614 613 GOL GOL B . HA 7 GOL 1 615 614 GOL GOL B . IA 7 GOL 1 616 615 GOL GOL B . JA 7 GOL 1 617 616 GOL GOL B . KA 8 HOH 1 701 1728 HOH HOH A . KA 8 HOH 2 702 1951 HOH HOH A . KA 8 HOH 3 703 1869 HOH HOH A . KA 8 HOH 4 704 940 HOH HOH A . KA 8 HOH 5 705 1836 HOH HOH A . KA 8 HOH 6 706 791 HOH HOH A . KA 8 HOH 7 707 316 HOH HOH A . KA 8 HOH 8 708 52 HOH HOH A . KA 8 HOH 9 709 1858 HOH HOH A . KA 8 HOH 10 710 322 HOH HOH A . KA 8 HOH 11 711 1893 HOH HOH A . KA 8 HOH 12 712 49 HOH HOH A . KA 8 HOH 13 713 355 HOH HOH A . KA 8 HOH 14 714 81 HOH HOH A . KA 8 HOH 15 715 126 HOH HOH A . KA 8 HOH 16 716 1891 HOH HOH A . KA 8 HOH 17 717 767 HOH HOH A . KA 8 HOH 18 718 761 HOH HOH A . KA 8 HOH 19 719 782 HOH HOH A . KA 8 HOH 20 720 345 HOH HOH A . KA 8 HOH 21 721 755 HOH HOH A . KA 8 HOH 22 722 1823 HOH HOH A . KA 8 HOH 23 723 379 HOH HOH A . KA 8 HOH 24 724 1855 HOH HOH A . KA 8 HOH 25 725 1726 HOH HOH A . KA 8 HOH 26 726 1817 HOH HOH A . KA 8 HOH 27 727 343 HOH HOH A . KA 8 HOH 28 728 765 HOH HOH A . KA 8 HOH 29 729 1709 HOH HOH A . KA 8 HOH 30 730 364 HOH HOH A . KA 8 HOH 31 731 914 HOH HOH A . KA 8 HOH 32 732 847 HOH HOH A . KA 8 HOH 33 733 928 HOH HOH A . KA 8 HOH 34 734 321 HOH HOH A . KA 8 HOH 35 735 849 HOH HOH A . KA 8 HOH 36 736 127 HOH HOH A . KA 8 HOH 37 737 388 HOH HOH A . KA 8 HOH 38 738 779 HOH HOH A . KA 8 HOH 39 739 853 HOH HOH A . KA 8 HOH 40 740 906 HOH HOH A . KA 8 HOH 41 741 363 HOH HOH A . KA 8 HOH 42 742 1721 HOH HOH A . KA 8 HOH 43 743 93 HOH HOH A . KA 8 HOH 44 744 1706 HOH HOH A . KA 8 HOH 45 745 769 HOH HOH A . KA 8 HOH 46 746 1710 HOH HOH A . KA 8 HOH 47 747 1838 HOH HOH A . KA 8 HOH 48 748 1982 HOH HOH A . KA 8 HOH 49 749 1720 HOH HOH A . KA 8 HOH 50 750 852 HOH HOH A . KA 8 HOH 51 751 1715 HOH HOH A . KA 8 HOH 52 752 101 HOH HOH A . KA 8 HOH 53 753 1938 HOH HOH A . KA 8 HOH 54 754 122 HOH HOH A . KA 8 HOH 55 755 1793 HOH HOH A . KA 8 HOH 56 756 1713 HOH HOH A . KA 8 HOH 57 757 324 HOH HOH A . KA 8 HOH 58 758 934 HOH HOH A . KA 8 HOH 59 759 38 HOH HOH A . KA 8 HOH 60 760 734 HOH HOH A . KA 8 HOH 61 761 1840 HOH HOH A . KA 8 HOH 62 762 941 HOH HOH A . KA 8 HOH 63 763 1707 HOH HOH A . KA 8 HOH 64 764 1712 HOH HOH A . KA 8 HOH 65 765 740 HOH HOH A . KA 8 HOH 66 766 323 HOH HOH A . KA 8 HOH 67 767 1806 HOH HOH A . KA 8 HOH 68 768 1824 HOH HOH A . KA 8 HOH 69 769 1 HOH HOH A . KA 8 HOH 70 770 1818 HOH HOH A . KA 8 HOH 71 771 882 HOH HOH A . KA 8 HOH 72 772 930 HOH HOH A . KA 8 HOH 73 773 747 HOH HOH A . KA 8 HOH 74 774 845 HOH HOH A . KA 8 HOH 75 775 1888 HOH HOH A . KA 8 HOH 76 776 59 HOH HOH A . KA 8 HOH 77 777 1953 HOH HOH A . KA 8 HOH 78 778 918 HOH HOH A . KA 8 HOH 79 779 1989 HOH HOH A . KA 8 HOH 80 780 36 HOH HOH A . KA 8 HOH 81 781 903 HOH HOH A . KA 8 HOH 82 782 762 HOH HOH A . KA 8 HOH 83 783 332 HOH HOH A . KA 8 HOH 84 784 1867 HOH HOH A . KA 8 HOH 85 785 900 HOH HOH A . KA 8 HOH 86 786 1801 HOH HOH A . KA 8 HOH 87 787 313 HOH HOH A . KA 8 HOH 88 788 744 HOH HOH A . KA 8 HOH 89 789 2 HOH HOH A . KA 8 HOH 90 790 3 HOH HOH A . KA 8 HOH 91 791 1718 HOH HOH A . KA 8 HOH 92 792 326 HOH HOH A . KA 8 HOH 93 793 737 HOH HOH A . KA 8 HOH 94 794 754 HOH HOH A . KA 8 HOH 95 795 784 HOH HOH A . KA 8 HOH 96 796 915 HOH HOH A . KA 8 HOH 97 797 329 HOH HOH A . KA 8 HOH 98 798 775 HOH HOH A . KA 8 HOH 99 799 1722 HOH HOH A . KA 8 HOH 100 800 1794 HOH HOH A . KA 8 HOH 101 801 1826 HOH HOH A . KA 8 HOH 102 802 1714 HOH HOH A . KA 8 HOH 103 803 701 HOH HOH A . KA 8 HOH 104 804 380 HOH HOH A . KA 8 HOH 105 805 916 HOH HOH A . KA 8 HOH 106 806 1798 HOH HOH A . KA 8 HOH 107 807 1979 HOH HOH A . KA 8 HOH 108 808 756 HOH HOH A . KA 8 HOH 109 809 1814 HOH HOH A . KA 8 HOH 110 810 1834 HOH HOH A . KA 8 HOH 111 811 1886 HOH HOH A . KA 8 HOH 112 812 1795 HOH HOH A . KA 8 HOH 113 813 764 HOH HOH A . KA 8 HOH 114 814 971 HOH HOH A . KA 8 HOH 115 815 974 HOH HOH A . KA 8 HOH 116 816 739 HOH HOH A . KA 8 HOH 117 817 937 HOH HOH A . KA 8 HOH 118 818 1716 HOH HOH A . KA 8 HOH 119 819 109 HOH HOH A . KA 8 HOH 120 820 12 HOH HOH A . KA 8 HOH 121 821 1725 HOH HOH A . KA 8 HOH 122 822 1711 HOH HOH A . KA 8 HOH 123 823 917 HOH HOH A . KA 8 HOH 124 824 871 HOH HOH A . KA 8 HOH 125 825 1980 HOH HOH A . KA 8 HOH 126 826 1831 HOH HOH A . KA 8 HOH 127 827 317 HOH HOH A . KA 8 HOH 128 828 758 HOH HOH A . KA 8 HOH 129 829 1704 HOH HOH A . KA 8 HOH 130 830 977 HOH HOH A . KA 8 HOH 131 831 130 HOH HOH A . KA 8 HOH 132 832 1820 HOH HOH A . KA 8 HOH 133 833 1955 HOH HOH A . KA 8 HOH 134 834 1885 HOH HOH A . KA 8 HOH 135 835 1889 HOH HOH A . KA 8 HOH 136 836 1998 HOH HOH A . KA 8 HOH 137 837 106 HOH HOH A . KA 8 HOH 138 838 931 HOH HOH A . KA 8 HOH 139 839 1819 HOH HOH A . KA 8 HOH 140 840 1816 HOH HOH A . KA 8 HOH 141 841 899 HOH HOH A . KA 8 HOH 142 842 741 HOH HOH A . KA 8 HOH 143 843 732 HOH HOH A . KA 8 HOH 144 844 731 HOH HOH A . KA 8 HOH 145 845 1705 HOH HOH A . KA 8 HOH 146 846 1990 HOH HOH A . KA 8 HOH 147 847 848 HOH HOH A . KA 8 HOH 148 848 102 HOH HOH A . KA 8 HOH 149 849 1922 HOH HOH A . KA 8 HOH 150 850 1962 HOH HOH A . KA 8 HOH 151 851 377 HOH HOH A . KA 8 HOH 152 852 1892 HOH HOH A . KA 8 HOH 153 853 1896 HOH HOH A . KA 8 HOH 154 854 1865 HOH HOH A . KA 8 HOH 155 855 735 HOH HOH A . KA 8 HOH 156 856 105 HOH HOH A . KA 8 HOH 157 857 972 HOH HOH A . KA 8 HOH 158 858 374 HOH HOH A . KA 8 HOH 159 859 780 HOH HOH A . KA 8 HOH 160 860 1859 HOH HOH A . KA 8 HOH 161 861 788 HOH HOH A . KA 8 HOH 162 862 772 HOH HOH A . KA 8 HOH 163 863 964 HOH HOH A . KA 8 HOH 164 864 1815 HOH HOH A . KA 8 HOH 165 865 337 HOH HOH A . KA 8 HOH 166 866 1719 HOH HOH A . KA 8 HOH 167 867 125 HOH HOH A . KA 8 HOH 168 868 946 HOH HOH A . KA 8 HOH 169 869 1708 HOH HOH A . KA 8 HOH 170 870 902 HOH HOH A . KA 8 HOH 171 871 1703 HOH HOH A . KA 8 HOH 172 872 743 HOH HOH A . KA 8 HOH 173 873 745 HOH HOH A . KA 8 HOH 174 874 71 HOH HOH A . KA 8 HOH 175 875 768 HOH HOH A . KA 8 HOH 176 876 1843 HOH HOH A . KA 8 HOH 177 877 1833 HOH HOH A . KA 8 HOH 178 878 1956 HOH HOH A . KA 8 HOH 179 879 384 HOH HOH A . KA 8 HOH 180 880 112 HOH HOH A . KA 8 HOH 181 881 967 HOH HOH A . KA 8 HOH 182 882 382 HOH HOH A . KA 8 HOH 183 883 1994 HOH HOH A . KA 8 HOH 184 884 319 HOH HOH A . KA 8 HOH 185 885 89 HOH HOH A . KA 8 HOH 186 886 94 HOH HOH A . KA 8 HOH 187 887 1835 HOH HOH A . KA 8 HOH 188 888 968 HOH HOH A . KA 8 HOH 189 889 1724 HOH HOH A . KA 8 HOH 190 890 320 HOH HOH A . KA 8 HOH 191 891 1799 HOH HOH A . KA 8 HOH 192 892 7 HOH HOH A . KA 8 HOH 193 893 1792 HOH HOH A . KA 8 HOH 194 894 1866 HOH HOH A . KA 8 HOH 195 895 749 HOH HOH A . KA 8 HOH 196 896 1812 HOH HOH A . KA 8 HOH 197 897 777 HOH HOH A . KA 8 HOH 198 898 1830 HOH HOH A . KA 8 HOH 199 899 11 HOH HOH A . KA 8 HOH 200 900 356 HOH HOH A . KA 8 HOH 201 901 1822 HOH HOH A . KA 8 HOH 202 902 1729 HOH HOH A . KA 8 HOH 203 903 738 HOH HOH A . KA 8 HOH 204 904 1809 HOH HOH A . KA 8 HOH 205 905 770 HOH HOH A . KA 8 HOH 206 906 1878 HOH HOH A . KA 8 HOH 207 907 790 HOH HOH A . KA 8 HOH 208 908 759 HOH HOH A . KA 8 HOH 209 909 6 HOH HOH A . KA 8 HOH 210 910 100 HOH HOH A . KA 8 HOH 211 911 114 HOH HOH A . KA 8 HOH 212 912 927 HOH HOH A . KA 8 HOH 213 913 876 HOH HOH A . KA 8 HOH 214 914 1895 HOH HOH A . KA 8 HOH 215 915 748 HOH HOH A . KA 8 HOH 216 916 351 HOH HOH A . KA 8 HOH 217 917 786 HOH HOH A . KA 8 HOH 218 918 1983 HOH HOH A . KA 8 HOH 219 919 315 HOH HOH A . KA 8 HOH 220 920 1947 HOH HOH A . KA 8 HOH 221 921 965 HOH HOH A . KA 8 HOH 222 922 1959 HOH HOH A . KA 8 HOH 223 923 760 HOH HOH A . KA 8 HOH 224 924 912 HOH HOH A . KA 8 HOH 225 925 746 HOH HOH A . KA 8 HOH 226 926 1810 HOH HOH A . KA 8 HOH 227 927 766 HOH HOH A . KA 8 HOH 228 928 1717 HOH HOH A . KA 8 HOH 229 929 1727 HOH HOH A . KA 8 HOH 230 930 787 HOH HOH A . KA 8 HOH 231 931 124 HOH HOH A . KA 8 HOH 232 932 67 HOH HOH A . KA 8 HOH 233 933 34 HOH HOH A . KA 8 HOH 234 934 733 HOH HOH A . KA 8 HOH 235 935 1950 HOH HOH A . KA 8 HOH 236 936 875 HOH HOH A . KA 8 HOH 237 937 877 HOH HOH A . KA 8 HOH 238 938 1949 HOH HOH A . KA 8 HOH 239 939 1800 HOH HOH A . KA 8 HOH 240 940 773 HOH HOH A . KA 8 HOH 241 941 1844 HOH HOH A . KA 8 HOH 242 942 1805 HOH HOH A . KA 8 HOH 243 943 1842 HOH HOH A . KA 8 HOH 244 944 1957 HOH HOH A . KA 8 HOH 245 945 1803 HOH HOH A . KA 8 HOH 246 946 751 HOH HOH A . KA 8 HOH 247 947 1723 HOH HOH A . KA 8 HOH 248 948 1945 HOH HOH A . KA 8 HOH 249 949 113 HOH HOH A . KA 8 HOH 250 950 68 HOH HOH A . KA 8 HOH 251 951 1702 HOH HOH A . KA 8 HOH 252 952 1797 HOH HOH A . KA 8 HOH 253 953 1 HOH HOH A . KA 8 HOH 254 954 789 HOH HOH A . KA 8 HOH 255 955 1821 HOH HOH A . KA 8 HOH 256 956 1841 HOH HOH A . KA 8 HOH 257 957 904 HOH HOH A . KA 8 HOH 258 958 110 HOH HOH A . KA 8 HOH 259 959 1960 HOH HOH A . KA 8 HOH 260 960 87 HOH HOH A . KA 8 HOH 261 961 753 HOH HOH A . KA 8 HOH 262 962 874 HOH HOH A . KA 8 HOH 263 963 1825 HOH HOH A . KA 8 HOH 264 964 314 HOH HOH A . KA 8 HOH 265 965 331 HOH HOH A . KA 8 HOH 266 966 104 HOH HOH A . KA 8 HOH 267 967 1802 HOH HOH A . KA 8 HOH 268 968 846 HOH HOH A . KA 8 HOH 269 969 1813 HOH HOH A . KA 8 HOH 270 970 1857 HOH HOH A . KA 8 HOH 271 971 939 HOH HOH A . KA 8 HOH 272 972 1985 HOH HOH A . KA 8 HOH 273 973 1863 HOH HOH A . KA 8 HOH 274 974 83 HOH HOH A . KA 8 HOH 275 975 771 HOH HOH A . KA 8 HOH 276 976 1868 HOH HOH A . KA 8 HOH 277 977 929 HOH HOH A . KA 8 HOH 278 978 785 HOH HOH A . KA 8 HOH 279 979 1961 HOH HOH A . KA 8 HOH 280 980 1996 HOH HOH A . KA 8 HOH 281 981 1783 HOH HOH A . KA 8 HOH 282 982 1987 HOH HOH A . KA 8 HOH 283 983 909 HOH HOH A . KA 8 HOH 284 984 1837 HOH HOH A . KA 8 HOH 285 985 1808 HOH HOH A . KA 8 HOH 286 986 1829 HOH HOH A . KA 8 HOH 287 987 1944 HOH HOH A . KA 8 HOH 288 988 932 HOH HOH A . KA 8 HOH 289 989 763 HOH HOH A . KA 8 HOH 290 990 1861 HOH HOH A . KA 8 HOH 291 991 35 HOH HOH A . KA 8 HOH 292 992 37 HOH HOH A . KA 8 HOH 293 993 330 HOH HOH A . KA 8 HOH 294 994 1804 HOH HOH A . KA 8 HOH 295 995 1952 HOH HOH A . KA 8 HOH 296 996 1828 HOH HOH A . KA 8 HOH 297 997 783 HOH HOH A . KA 8 HOH 298 998 757 HOH HOH A . KA 8 HOH 299 999 935 HOH HOH A . KA 8 HOH 300 1000 1827 HOH HOH A . KA 8 HOH 301 1001 752 HOH HOH A . KA 8 HOH 302 1002 1796 HOH HOH A . KA 8 HOH 303 1003 742 HOH HOH A . KA 8 HOH 304 1004 1864 HOH HOH A . KA 8 HOH 305 1005 50 HOH HOH A . KA 8 HOH 306 1006 328 HOH HOH A . KA 8 HOH 307 1007 108 HOH HOH A . KA 8 HOH 308 1008 1839 HOH HOH A . KA 8 HOH 309 1009 121 HOH HOH A . KA 8 HOH 310 1010 378 HOH HOH A . KA 8 HOH 311 1011 966 HOH HOH A . KA 8 HOH 312 1012 1870 HOH HOH A . KA 8 HOH 313 1013 1988 HOH HOH A . KA 8 HOH 314 1014 70 HOH HOH A . KA 8 HOH 315 1015 95 HOH HOH A . KA 8 HOH 316 1016 120 HOH HOH A . KA 8 HOH 317 1017 975 HOH HOH A . KA 8 HOH 318 1018 1999 HOH HOH A . KA 8 HOH 319 1019 911 HOH HOH A . KA 8 HOH 320 1020 969 HOH HOH A . KA 8 HOH 321 1021 730 HOH HOH A . KA 8 HOH 322 1022 85 HOH HOH A . KA 8 HOH 323 1023 1992 HOH HOH A . KA 8 HOH 324 1024 901 HOH HOH A . KA 8 HOH 325 1025 98 HOH HOH A . KA 8 HOH 326 1026 91 HOH HOH A . KA 8 HOH 327 1027 774 HOH HOH A . KA 8 HOH 328 1028 339 HOH HOH A . KA 8 HOH 329 1029 116 HOH HOH A . KA 8 HOH 330 1030 872 HOH HOH A . KA 8 HOH 331 1031 325 HOH HOH A . KA 8 HOH 332 1032 938 HOH HOH A . KA 8 HOH 333 1033 781 HOH HOH A . KA 8 HOH 334 1034 358 HOH HOH A . KA 8 HOH 335 1035 1894 HOH HOH A . KA 8 HOH 336 1036 131 HOH HOH A . KA 8 HOH 337 1037 25 HOH HOH A . KA 8 HOH 338 1038 878 HOH HOH A . KA 8 HOH 339 1039 92 HOH HOH A . KA 8 HOH 340 1040 1991 HOH HOH A . KA 8 HOH 341 1041 353 HOH HOH A . KA 8 HOH 342 1042 963 HOH HOH A . KA 8 HOH 343 1043 910 HOH HOH A . KA 8 HOH 344 1044 341 HOH HOH A . KA 8 HOH 345 1045 107 HOH HOH A . KA 8 HOH 346 1046 115 HOH HOH A . KA 8 HOH 347 1047 736 HOH HOH A . KA 8 HOH 348 1048 976 HOH HOH A . KA 8 HOH 349 1049 908 HOH HOH A . KA 8 HOH 350 1050 69 HOH HOH A . KA 8 HOH 351 1051 850 HOH HOH A . KA 8 HOH 352 1052 1981 HOH HOH A . KA 8 HOH 353 1053 1943 HOH HOH A . KA 8 HOH 354 1054 1995 HOH HOH A . KA 8 HOH 355 1055 880 HOH HOH A . KA 8 HOH 356 1056 123 HOH HOH A . KA 8 HOH 357 1057 118 HOH HOH A . KA 8 HOH 358 1058 776 HOH HOH A . KA 8 HOH 359 1059 778 HOH HOH A . KA 8 HOH 360 1060 1884 HOH HOH A . KA 8 HOH 361 1061 132 HOH HOH A . KA 8 HOH 362 1062 1921 HOH HOH A . KA 8 HOH 363 1063 1904 HOH HOH A . KA 8 HOH 364 1064 103 HOH HOH A . KA 8 HOH 365 1065 386 HOH HOH A . KA 8 HOH 366 1066 1948 HOH HOH A . KA 8 HOH 367 1067 973 HOH HOH A . KA 8 HOH 368 1068 1856 HOH HOH A . KA 8 HOH 369 1069 905 HOH HOH A . KA 8 HOH 370 1070 942 HOH HOH A . KA 8 HOH 371 1071 333 HOH HOH A . KA 8 HOH 372 1072 318 HOH HOH A . KA 8 HOH 373 1073 340 HOH HOH A . KA 8 HOH 374 1074 879 HOH HOH A . KA 8 HOH 375 1075 129 HOH HOH A . KA 8 HOH 376 1076 873 HOH HOH A . KA 8 HOH 377 1077 933 HOH HOH A . KA 8 HOH 378 1078 1958 HOH HOH A . KA 8 HOH 379 1079 119 HOH HOH A . KA 8 HOH 380 1080 344 HOH HOH A . KA 8 HOH 381 1081 346 HOH HOH A . KA 8 HOH 382 1082 362 HOH HOH A . KA 8 HOH 383 1083 117 HOH HOH A . KA 8 HOH 384 1084 347 HOH HOH A . KA 8 HOH 385 1085 4 HOH HOH A . KA 8 HOH 386 1086 66 HOH HOH A . KA 8 HOH 387 1087 9 HOH HOH A . KA 8 HOH 388 1088 357 HOH HOH A . KA 8 HOH 389 1089 881 HOH HOH A . KA 8 HOH 390 1090 390 HOH HOH A . KA 8 HOH 391 1091 958 HOH HOH A . KA 8 HOH 392 1092 851 HOH HOH A . KA 8 HOH 393 1093 327 HOH HOH A . KA 8 HOH 394 1094 1811 HOH HOH A . KA 8 HOH 395 1095 919 HOH HOH A . KA 8 HOH 396 1096 72 HOH HOH A . KA 8 HOH 397 1097 1993 HOH HOH A . KA 8 HOH 398 1098 1846 HOH HOH A . KA 8 HOH 399 1099 376 HOH HOH A . KA 8 HOH 400 1100 986 HOH HOH A . KA 8 HOH 401 1101 365 HOH HOH A . KA 8 HOH 402 1102 926 HOH HOH A . KA 8 HOH 403 1103 5 HOH HOH A . KA 8 HOH 404 1104 1897 HOH HOH A . KA 8 HOH 405 1105 1923 HOH HOH A . KA 8 HOH 406 1106 978 HOH HOH A . KA 8 HOH 407 1107 10 HOH HOH A . KA 8 HOH 408 1108 111 HOH HOH A . KA 8 HOH 409 1109 373 HOH HOH A . KA 8 HOH 410 1110 925 HOH HOH A . KA 8 HOH 411 1111 352 HOH HOH A . KA 8 HOH 412 1112 60 HOH HOH A . KA 8 HOH 413 1113 354 HOH HOH A . KA 8 HOH 414 1114 42 HOH HOH A . KA 8 HOH 415 1115 61 HOH HOH A . LA 8 HOH 1 701 984 HOH HOH B . LA 8 HOH 2 702 1936 HOH HOH B . LA 8 HOH 3 703 5 HOH HOH B . LA 8 HOH 4 704 804 HOH HOH B . LA 8 HOH 5 705 841 HOH HOH B . LA 8 HOH 6 706 716 HOH HOH B . LA 8 HOH 7 707 1741 HOH HOH B . LA 8 HOH 8 708 1776 HOH HOH B . LA 8 HOH 9 709 895 HOH HOH B . LA 8 HOH 10 710 800 HOH HOH B . LA 8 HOH 11 711 807 HOH HOH B . LA 8 HOH 12 712 308 HOH HOH B . LA 8 HOH 13 713 954 HOH HOH B . LA 8 HOH 14 714 1770 HOH HOH B . LA 8 HOH 15 715 1852 HOH HOH B . LA 8 HOH 16 716 891 HOH HOH B . LA 8 HOH 17 717 64 HOH HOH B . LA 8 HOH 18 718 1976 HOH HOH B . LA 8 HOH 19 719 1918 HOH HOH B . LA 8 HOH 20 720 1882 HOH HOH B . LA 8 HOH 21 721 1964 HOH HOH B . LA 8 HOH 22 722 1967 HOH HOH B . LA 8 HOH 23 723 717 HOH HOH B . LA 8 HOH 24 724 1732 HOH HOH B . LA 8 HOH 25 725 792 HOH HOH B . LA 8 HOH 26 726 887 HOH HOH B . LA 8 HOH 27 727 1784 HOH HOH B . LA 8 HOH 28 728 996 HOH HOH B . LA 8 HOH 29 729 842 HOH HOH B . LA 8 HOH 30 730 1972 HOH HOH B . LA 8 HOH 31 731 1782 HOH HOH B . LA 8 HOH 32 732 1749 HOH HOH B . LA 8 HOH 33 733 1873 HOH HOH B . LA 8 HOH 34 734 7 HOH HOH B . LA 8 HOH 35 735 793 HOH HOH B . LA 8 HOH 36 736 370 HOH HOH B . LA 8 HOH 37 737 1910 HOH HOH B . LA 8 HOH 38 738 1790 HOH HOH B . LA 8 HOH 39 739 1731 HOH HOH B . LA 8 HOH 40 740 1975 HOH HOH B . LA 8 HOH 41 741 1787 HOH HOH B . LA 8 HOH 42 742 819 HOH HOH B . LA 8 HOH 43 743 62 HOH HOH B . LA 8 HOH 44 744 802 HOH HOH B . LA 8 HOH 45 745 54 HOH HOH B . LA 8 HOH 46 746 810 HOH HOH B . LA 8 HOH 47 747 795 HOH HOH B . LA 8 HOH 48 748 1872 HOH HOH B . LA 8 HOH 49 749 794 HOH HOH B . LA 8 HOH 50 750 24 HOH HOH B . LA 8 HOH 51 751 16 HOH HOH B . LA 8 HOH 52 752 1764 HOH HOH B . LA 8 HOH 53 753 17 HOH HOH B . LA 8 HOH 54 754 1851 HOH HOH B . LA 8 HOH 55 755 808 HOH HOH B . LA 8 HOH 56 756 839 HOH HOH B . LA 8 HOH 57 757 829 HOH HOH B . LA 8 HOH 58 758 1739 HOH HOH B . LA 8 HOH 59 759 837 HOH HOH B . LA 8 HOH 60 760 947 HOH HOH B . LA 8 HOH 61 761 39 HOH HOH B . LA 8 HOH 62 762 1928 HOH HOH B . LA 8 HOH 63 763 1876 HOH HOH B . LA 8 HOH 64 764 1761 HOH HOH B . LA 8 HOH 65 765 1905 HOH HOH B . LA 8 HOH 66 766 985 HOH HOH B . LA 8 HOH 67 767 824 HOH HOH B . LA 8 HOH 68 768 1791 HOH HOH B . LA 8 HOH 69 769 838 HOH HOH B . LA 8 HOH 70 770 710 HOH HOH B . LA 8 HOH 71 771 708 HOH HOH B . LA 8 HOH 72 772 719 HOH HOH B . LA 8 HOH 73 773 1730 HOH HOH B . LA 8 HOH 74 774 861 HOH HOH B . LA 8 HOH 75 775 1735 HOH HOH B . LA 8 HOH 76 776 368 HOH HOH B . LA 8 HOH 77 777 1734 HOH HOH B . LA 8 HOH 78 778 720 HOH HOH B . LA 8 HOH 79 779 1743 HOH HOH B . LA 8 HOH 80 780 990 HOH HOH B . LA 8 HOH 81 781 1933 HOH HOH B . LA 8 HOH 82 782 1733 HOH HOH B . LA 8 HOH 83 783 721 HOH HOH B . LA 8 HOH 84 784 1853 HOH HOH B . LA 8 HOH 85 785 1912 HOH HOH B . LA 8 HOH 86 786 1778 HOH HOH B . LA 8 HOH 87 787 956 HOH HOH B . LA 8 HOH 88 788 806 HOH HOH B . LA 8 HOH 89 789 725 HOH HOH B . LA 8 HOH 90 790 1740 HOH HOH B . LA 8 HOH 91 791 883 HOH HOH B . LA 8 HOH 92 792 722 HOH HOH B . LA 8 HOH 93 793 1789 HOH HOH B . LA 8 HOH 94 794 718 HOH HOH B . LA 8 HOH 95 795 922 HOH HOH B . LA 8 HOH 96 796 1986 HOH HOH B . LA 8 HOH 97 797 1769 HOH HOH B . LA 8 HOH 98 798 1875 HOH HOH B . LA 8 HOH 99 799 1845 HOH HOH B . LA 8 HOH 100 800 22 HOH HOH B . LA 8 HOH 101 801 8 HOH HOH B . LA 8 HOH 102 802 1966 HOH HOH B . LA 8 HOH 103 803 1969 HOH HOH B . LA 8 HOH 104 804 834 HOH HOH B . LA 8 HOH 105 805 1737 HOH HOH B . LA 8 HOH 106 806 835 HOH HOH B . LA 8 HOH 107 807 723 HOH HOH B . LA 8 HOH 108 808 706 HOH HOH B . LA 8 HOH 109 809 1932 HOH HOH B . LA 8 HOH 110 810 703 HOH HOH B . LA 8 HOH 111 811 1767 HOH HOH B . LA 8 HOH 112 812 893 HOH HOH B . LA 8 HOH 113 813 805 HOH HOH B . LA 8 HOH 114 814 823 HOH HOH B . LA 8 HOH 115 815 866 HOH HOH B . LA 8 HOH 116 816 1762 HOH HOH B . LA 8 HOH 117 817 818 HOH HOH B . LA 8 HOH 118 818 1965 HOH HOH B . LA 8 HOH 119 819 1736 HOH HOH B . LA 8 HOH 120 820 825 HOH HOH B . LA 8 HOH 121 821 1785 HOH HOH B . LA 8 HOH 122 822 1742 HOH HOH B . LA 8 HOH 123 823 367 HOH HOH B . LA 8 HOH 124 824 894 HOH HOH B . LA 8 HOH 125 825 713 HOH HOH B . LA 8 HOH 126 826 860 HOH HOH B . LA 8 HOH 127 827 715 HOH HOH B . LA 8 HOH 128 828 924 HOH HOH B . LA 8 HOH 129 829 999 HOH HOH B . LA 8 HOH 130 830 797 HOH HOH B . LA 8 HOH 131 831 1925 HOH HOH B . LA 8 HOH 132 832 1751 HOH HOH B . LA 8 HOH 133 833 724 HOH HOH B . LA 8 HOH 134 834 1738 HOH HOH B . LA 8 HOH 135 835 1744 HOH HOH B . LA 8 HOH 136 836 1974 HOH HOH B . LA 8 HOH 137 837 73 HOH HOH B . LA 8 HOH 138 838 1902 HOH HOH B . LA 8 HOH 139 839 1766 HOH HOH B . LA 8 HOH 140 840 709 HOH HOH B . LA 8 HOH 141 841 854 HOH HOH B . LA 8 HOH 142 842 1788 HOH HOH B . LA 8 HOH 143 843 707 HOH HOH B . LA 8 HOH 144 844 892 HOH HOH B . LA 8 HOH 145 845 865 HOH HOH B . LA 8 HOH 146 846 348 HOH HOH B . LA 8 HOH 147 847 1756 HOH HOH B . LA 8 HOH 148 848 1757 HOH HOH B . LA 8 HOH 149 849 1900 HOH HOH B . LA 8 HOH 150 850 704 HOH HOH B . LA 8 HOH 151 851 803 HOH HOH B . LA 8 HOH 152 852 28 HOH HOH B . LA 8 HOH 153 853 1754 HOH HOH B . LA 8 HOH 154 854 1919 HOH HOH B . LA 8 HOH 155 855 858 HOH HOH B . LA 8 HOH 156 856 366 HOH HOH B . LA 8 HOH 157 857 936 HOH HOH B . LA 8 HOH 158 858 99 HOH HOH B . LA 8 HOH 159 859 727 HOH HOH B . LA 8 HOH 160 860 820 HOH HOH B . LA 8 HOH 161 861 989 HOH HOH B . LA 8 HOH 162 862 51 HOH HOH B . LA 8 HOH 163 863 1771 HOH HOH B . LA 8 HOH 164 864 988 HOH HOH B . LA 8 HOH 165 865 56 HOH HOH B . LA 8 HOH 166 866 1939 HOH HOH B . LA 8 HOH 167 867 728 HOH HOH B . LA 8 HOH 168 868 1755 HOH HOH B . LA 8 HOH 169 869 1745 HOH HOH B . LA 8 HOH 170 870 1917 HOH HOH B . LA 8 HOH 171 871 868 HOH HOH B . LA 8 HOH 172 872 814 HOH HOH B . LA 8 HOH 173 873 1954 HOH HOH B . LA 8 HOH 174 874 705 HOH HOH B . LA 8 HOH 175 875 359 HOH HOH B . LA 8 HOH 176 876 311 HOH HOH B . LA 8 HOH 177 877 955 HOH HOH B . LA 8 HOH 178 878 896 HOH HOH B . LA 8 HOH 179 879 801 HOH HOH B . LA 8 HOH 180 880 890 HOH HOH B . LA 8 HOH 181 881 982 HOH HOH B . LA 8 HOH 182 882 1760 HOH HOH B . LA 8 HOH 183 883 859 HOH HOH B . LA 8 HOH 184 884 815 HOH HOH B . LA 8 HOH 185 885 726 HOH HOH B . LA 8 HOH 186 886 1765 HOH HOH B . LA 8 HOH 187 887 1753 HOH HOH B . LA 8 HOH 188 888 1877 HOH HOH B . LA 8 HOH 189 889 714 HOH HOH B . LA 8 HOH 190 890 1774 HOH HOH B . LA 8 HOH 191 891 1775 HOH HOH B . LA 8 HOH 192 892 1748 HOH HOH B . LA 8 HOH 193 893 822 HOH HOH B . LA 8 HOH 194 894 334 HOH HOH B . LA 8 HOH 195 895 6 HOH HOH B . LA 8 HOH 196 896 1781 HOH HOH B . LA 8 HOH 197 897 1929 HOH HOH B . LA 8 HOH 198 898 817 HOH HOH B . LA 8 HOH 199 899 711 HOH HOH B . LA 8 HOH 200 900 921 HOH HOH B . LA 8 HOH 201 901 813 HOH HOH B . LA 8 HOH 202 902 867 HOH HOH B . LA 8 HOH 203 903 1934 HOH HOH B . LA 8 HOH 204 904 1772 HOH HOH B . LA 8 HOH 205 905 1759 HOH HOH B . LA 8 HOH 206 906 1898 HOH HOH B . LA 8 HOH 207 907 840 HOH HOH B . LA 8 HOH 208 908 1903 HOH HOH B . LA 8 HOH 209 909 913 HOH HOH B . LA 8 HOH 210 910 799 HOH HOH B . LA 8 HOH 211 911 798 HOH HOH B . LA 8 HOH 212 912 1847 HOH HOH B . LA 8 HOH 213 913 796 HOH HOH B . LA 8 HOH 214 914 1871 HOH HOH B . LA 8 HOH 215 915 836 HOH HOH B . LA 8 HOH 216 916 950 HOH HOH B . LA 8 HOH 217 917 1763 HOH HOH B . LA 8 HOH 218 918 1786 HOH HOH B . LA 8 HOH 219 919 1773 HOH HOH B . LA 8 HOH 220 920 302 HOH HOH B . LA 8 HOH 221 921 79 HOH HOH B . LA 8 HOH 222 922 943 HOH HOH B . LA 8 HOH 223 923 712 HOH HOH B . LA 8 HOH 224 924 897 HOH HOH B . LA 8 HOH 225 925 1927 HOH HOH B . LA 8 HOH 226 926 3 HOH HOH B . LA 8 HOH 227 927 991 HOH HOH B . LA 8 HOH 228 928 855 HOH HOH B . LA 8 HOH 229 929 1777 HOH HOH B . LA 8 HOH 230 930 1909 HOH HOH B . LA 8 HOH 231 931 948 HOH HOH B . LA 8 HOH 232 932 369 HOH HOH B . LA 8 HOH 233 933 833 HOH HOH B . LA 8 HOH 234 934 45 HOH HOH B . LA 8 HOH 235 935 864 HOH HOH B . LA 8 HOH 236 936 1701 HOH HOH B . LA 8 HOH 237 937 1849 HOH HOH B . LA 8 HOH 238 938 1915 HOH HOH B . LA 8 HOH 239 939 1780 HOH HOH B . LA 8 HOH 240 940 18 HOH HOH B . LA 8 HOH 241 941 371 HOH HOH B . LA 8 HOH 242 942 821 HOH HOH B . LA 8 HOH 243 943 1750 HOH HOH B . LA 8 HOH 244 944 1926 HOH HOH B . LA 8 HOH 245 945 884 HOH HOH B . LA 8 HOH 246 946 856 HOH HOH B . LA 8 HOH 247 947 827 HOH HOH B . LA 8 HOH 248 948 1747 HOH HOH B . LA 8 HOH 249 949 811 HOH HOH B . LA 8 HOH 250 950 994 HOH HOH B . LA 8 HOH 251 951 843 HOH HOH B . LA 8 HOH 252 952 1963 HOH HOH B . LA 8 HOH 253 953 1881 HOH HOH B . LA 8 HOH 254 954 1941 HOH HOH B . LA 8 HOH 255 955 1911 HOH HOH B . LA 8 HOH 256 956 997 HOH HOH B . LA 8 HOH 257 957 303 HOH HOH B . LA 8 HOH 258 958 826 HOH HOH B . LA 8 HOH 259 959 945 HOH HOH B . LA 8 HOH 260 960 1758 HOH HOH B . LA 8 HOH 261 961 816 HOH HOH B . LA 8 HOH 262 962 1940 HOH HOH B . LA 8 HOH 263 963 1746 HOH HOH B . LA 8 HOH 264 964 29 HOH HOH B . LA 8 HOH 265 965 949 HOH HOH B . LA 8 HOH 266 966 993 HOH HOH B . LA 8 HOH 267 967 31 HOH HOH B . LA 8 HOH 268 968 63 HOH HOH B . LA 8 HOH 269 969 1850 HOH HOH B . LA 8 HOH 270 970 980 HOH HOH B . LA 8 HOH 271 971 957 HOH HOH B . LA 8 HOH 272 972 983 HOH HOH B . LA 8 HOH 273 973 26 HOH HOH B . LA 8 HOH 274 974 23 HOH HOH B . LA 8 HOH 275 975 46 HOH HOH B . LA 8 HOH 276 976 998 HOH HOH B . LA 8 HOH 277 977 907 HOH HOH B . LA 8 HOH 278 978 57 HOH HOH B . LA 8 HOH 279 979 1899 HOH HOH B . LA 8 HOH 280 980 1935 HOH HOH B . LA 8 HOH 281 981 1901 HOH HOH B . LA 8 HOH 282 982 812 HOH HOH B . LA 8 HOH 283 983 863 HOH HOH B . LA 8 HOH 284 984 830 HOH HOH B . LA 8 HOH 285 985 47 HOH HOH B . LA 8 HOH 286 986 1874 HOH HOH B . LA 8 HOH 287 987 1779 HOH HOH B . LA 8 HOH 288 988 1752 HOH HOH B . LA 8 HOH 289 989 1937 HOH HOH B . LA 8 HOH 290 990 1879 HOH HOH B . LA 8 HOH 291 991 77 HOH HOH B . LA 8 HOH 292 992 1968 HOH HOH B . LA 8 HOH 293 993 55 HOH HOH B . LA 8 HOH 294 994 1916 HOH HOH B . LA 8 HOH 295 995 809 HOH HOH B . LA 8 HOH 296 996 78 HOH HOH B . LA 8 HOH 297 997 15 HOH HOH B . LA 8 HOH 298 998 360 HOH HOH B . LA 8 HOH 299 999 1914 HOH HOH B . LA 8 HOH 300 1000 32 HOH HOH B . LA 8 HOH 301 1001 987 HOH HOH B . LA 8 HOH 302 1002 857 HOH HOH B . LA 8 HOH 303 1003 885 HOH HOH B . LA 8 HOH 304 1004 995 HOH HOH B . LA 8 HOH 305 1005 75 HOH HOH B . LA 8 HOH 306 1006 1906 HOH HOH B . LA 8 HOH 307 1007 886 HOH HOH B . LA 8 HOH 308 1008 306 HOH HOH B . LA 8 HOH 309 1009 43 HOH HOH B . LA 8 HOH 310 1010 1931 HOH HOH B . LA 8 HOH 311 1011 342 HOH HOH B . LA 8 HOH 312 1012 97 HOH HOH B . LA 8 HOH 313 1013 981 HOH HOH B . LA 8 HOH 314 1014 27 HOH HOH B . LA 8 HOH 315 1015 1848 HOH HOH B . LA 8 HOH 316 1016 44 HOH HOH B . LA 8 HOH 317 1017 4 HOH HOH B . LA 8 HOH 318 1018 14 HOH HOH B . LA 8 HOH 319 1019 951 HOH HOH B . LA 8 HOH 320 1020 888 HOH HOH B . LA 8 HOH 321 1021 349 HOH HOH B . LA 8 HOH 322 1022 76 HOH HOH B . LA 8 HOH 323 1023 74 HOH HOH B . LA 8 HOH 324 1024 8 HOH HOH B . LA 8 HOH 325 1025 40 HOH HOH B . LA 8 HOH 326 1026 992 HOH HOH B . LA 8 HOH 327 1027 953 HOH HOH B . LA 8 HOH 328 1028 1908 HOH HOH B . LA 8 HOH 329 1029 1033 HOH HOH B . LA 8 HOH 330 1030 1971 HOH HOH B . LA 8 HOH 331 1031 1973 HOH HOH B . LA 8 HOH 332 1032 920 HOH HOH B . LA 8 HOH 333 1033 309 HOH HOH B . LA 8 HOH 334 1034 750 HOH HOH B . LA 8 HOH 335 1035 702 HOH HOH B . LA 8 HOH 336 1036 336 HOH HOH B . LA 8 HOH 337 1037 2 HOH HOH B . LA 8 HOH 338 1038 301 HOH HOH B . LA 8 HOH 339 1039 979 HOH HOH B . LA 8 HOH 340 1040 1930 HOH HOH B . LA 8 HOH 341 1041 21 HOH HOH B . LA 8 HOH 342 1042 889 HOH HOH B . LA 8 HOH 343 1043 304 HOH HOH B . LA 8 HOH 344 1044 305 HOH HOH B . LA 8 HOH 345 1045 53 HOH HOH B . LA 8 HOH 346 1046 13 HOH HOH B . LA 8 HOH 347 1047 20 HOH HOH B . LA 8 HOH 348 1048 1880 HOH HOH B . LA 8 HOH 349 1049 310 HOH HOH B . LA 8 HOH 350 1050 961 HOH HOH B . LA 8 HOH 351 1051 828 HOH HOH B . LA 8 HOH 352 1052 831 HOH HOH B . LA 8 HOH 353 1053 960 HOH HOH B . LA 8 HOH 354 1054 1977 HOH HOH B . LA 8 HOH 355 1055 19 HOH HOH B . LA 8 HOH 356 1056 375 HOH HOH B . LA 8 HOH 357 1057 307 HOH HOH B . LA 8 HOH 358 1058 30 HOH HOH B . LA 8 HOH 359 1059 1768 HOH HOH B . LA 8 HOH 360 1060 959 HOH HOH B . # loop_ _pdbx_struct_assembly.id _pdbx_struct_assembly.details _pdbx_struct_assembly.method_details _pdbx_struct_assembly.oligomeric_details _pdbx_struct_assembly.oligomeric_count 1 author_defined_assembly ? monomeric 1 2 author_defined_assembly ? monomeric 1 # loop_ _pdbx_struct_assembly_gen.assembly_id _pdbx_struct_assembly_gen.oper_expression _pdbx_struct_assembly_gen.asym_id_list 1 1 A,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,KA 2 1 B,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA,JA,LA # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 O ? A ASP 110 ? A ASP 110 ? 1_555 CA ? J CA . ? A CA 608 ? 1_555 OD1 ? A ASP 110 ? A ASP 110 ? 1_555 80.0 ? 2 O ? A ASP 110 ? A ASP 110 ? 1_555 CA ? J CA . ? A CA 608 ? 1_555 O ? A THR 184 ? A THR 184 ? 1_555 74.2 ? 3 OD1 ? A ASP 110 ? A ASP 110 ? 1_555 CA ? J CA . ? A CA 608 ? 1_555 O ? A THR 184 ? A THR 184 ? 1_555 140.6 ? 4 O ? A ASP 110 ? A ASP 110 ? 1_555 CA ? J CA . ? A CA 608 ? 1_555 OG1 ? A THR 184 ? A THR 184 ? 1_555 124.2 ? 5 OD1 ? A ASP 110 ? A ASP 110 ? 1_555 CA ? J CA . ? A CA 608 ? 1_555 OG1 ? A THR 184 ? A THR 184 ? 1_555 147.0 ? 6 O ? A THR 184 ? A THR 184 ? 1_555 CA ? J CA . ? A CA 608 ? 1_555 OG1 ? A THR 184 ? A THR 184 ? 1_555 72.0 ? 7 O ? A ASP 110 ? A ASP 110 ? 1_555 CA ? J CA . ? A CA 608 ? 1_555 O ? A PHE 186 ? A PHE 186 ? 1_555 118.0 ? 8 OD1 ? A ASP 110 ? A ASP 110 ? 1_555 CA ? J CA . ? A CA 608 ? 1_555 O ? A PHE 186 ? A PHE 186 ? 1_555 81.8 ? 9 O ? A THR 184 ? A THR 184 ? 1_555 CA ? J CA . ? A CA 608 ? 1_555 O ? A PHE 186 ? A PHE 186 ? 1_555 84.6 ? 10 OG1 ? A THR 184 ? A THR 184 ? 1_555 CA ? J CA . ? A CA 608 ? 1_555 O ? A PHE 186 ? A PHE 186 ? 1_555 101.5 ? 11 O ? A ASP 110 ? A ASP 110 ? 1_555 CA ? J CA . ? A CA 608 ? 1_555 OD1 ? A ASP 188 ? A ASP 188 ? 1_555 146.7 ? 12 OD1 ? A ASP 110 ? A ASP 110 ? 1_555 CA ? J CA . ? A CA 608 ? 1_555 OD1 ? A ASP 188 ? A ASP 188 ? 1_555 76.8 ? 13 O ? A THR 184 ? A THR 184 ? 1_555 CA ? J CA . ? A CA 608 ? 1_555 OD1 ? A ASP 188 ? A ASP 188 ? 1_555 137.3 ? 14 OG1 ? A THR 184 ? A THR 184 ? 1_555 CA ? J CA . ? A CA 608 ? 1_555 OD1 ? A ASP 188 ? A ASP 188 ? 1_555 71.3 ? 15 O ? A PHE 186 ? A PHE 186 ? 1_555 CA ? J CA . ? A CA 608 ? 1_555 OD1 ? A ASP 188 ? A ASP 188 ? 1_555 81.9 ? 16 O ? A ASP 110 ? A ASP 110 ? 1_555 CA ? J CA . ? A CA 608 ? 1_555 OG ? A SER 190 ? A SER 190 ? 1_555 75.9 ? 17 OD1 ? A ASP 110 ? A ASP 110 ? 1_555 CA ? J CA . ? A CA 608 ? 1_555 OG ? A SER 190 ? A SER 190 ? 1_555 83.9 ? 18 O ? A THR 184 ? A THR 184 ? 1_555 CA ? J CA . ? A CA 608 ? 1_555 OG ? A SER 190 ? A SER 190 ? 1_555 117.1 ? 19 OG1 ? A THR 184 ? A THR 184 ? 1_555 CA ? J CA . ? A CA 608 ? 1_555 OG ? A SER 190 ? A SER 190 ? 1_555 81.6 ? 20 O ? A PHE 186 ? A PHE 186 ? 1_555 CA ? J CA . ? A CA 608 ? 1_555 OG ? A SER 190 ? A SER 190 ? 1_555 157.7 ? 21 OD1 ? A ASP 188 ? A ASP 188 ? 1_555 CA ? J CA . ? A CA 608 ? 1_555 OG ? A SER 190 ? A SER 190 ? 1_555 78.2 ? 22 NE2 ? A HIS 351 ? A HIS 351 ? 1_555 FE ? I HEM . ? A HEM 607 ? 1_555 NA ? I HEM . ? A HEM 607 ? 1_555 95.3 ? 23 NE2 ? A HIS 351 ? A HIS 351 ? 1_555 FE ? I HEM . ? A HEM 607 ? 1_555 NB ? I HEM . ? A HEM 607 ? 1_555 94.3 ? 24 NA ? I HEM . ? A HEM 607 ? 1_555 FE ? I HEM . ? A HEM 607 ? 1_555 NB ? I HEM . ? A HEM 607 ? 1_555 88.6 ? 25 NE2 ? A HIS 351 ? A HIS 351 ? 1_555 FE ? I HEM . ? A HEM 607 ? 1_555 NC ? I HEM . ? A HEM 607 ? 1_555 88.7 ? 26 NA ? I HEM . ? A HEM 607 ? 1_555 FE ? I HEM . ? A HEM 607 ? 1_555 NC ? I HEM . ? A HEM 607 ? 1_555 175.3 ? 27 NB ? I HEM . ? A HEM 607 ? 1_555 FE ? I HEM . ? A HEM 607 ? 1_555 NC ? I HEM . ? A HEM 607 ? 1_555 88.6 ? 28 NE2 ? A HIS 351 ? A HIS 351 ? 1_555 FE ? I HEM . ? A HEM 607 ? 1_555 ND ? I HEM . ? A HEM 607 ? 1_555 90.6 ? 29 NA ? I HEM . ? A HEM 607 ? 1_555 FE ? I HEM . ? A HEM 607 ? 1_555 ND ? I HEM . ? A HEM 607 ? 1_555 91.6 ? 30 NB ? I HEM . ? A HEM 607 ? 1_555 FE ? I HEM . ? A HEM 607 ? 1_555 ND ? I HEM . ? A HEM 607 ? 1_555 175.0 ? 31 NC ? I HEM . ? A HEM 607 ? 1_555 FE ? I HEM . ? A HEM 607 ? 1_555 ND ? I HEM . ? A HEM 607 ? 1_555 90.9 ? 32 NE2 ? A HIS 351 ? A HIS 351 ? 1_555 FE ? I HEM . ? A HEM 607 ? 1_555 S2 ? D MMZ . ? A MMZ 602 ? 1_555 169.1 ? 33 NA ? I HEM . ? A HEM 607 ? 1_555 FE ? I HEM . ? A HEM 607 ? 1_555 S2 ? D MMZ . ? A MMZ 602 ? 1_555 74.1 ? 34 NB ? I HEM . ? A HEM 607 ? 1_555 FE ? I HEM . ? A HEM 607 ? 1_555 S2 ? D MMZ . ? A MMZ 602 ? 1_555 88.3 ? 35 NC ? I HEM . ? A HEM 607 ? 1_555 FE ? I HEM . ? A HEM 607 ? 1_555 S2 ? D MMZ . ? A MMZ 602 ? 1_555 102.0 ? 36 ND ? I HEM . ? A HEM 607 ? 1_555 FE ? I HEM . ? A HEM 607 ? 1_555 S2 ? D MMZ . ? A MMZ 602 ? 1_555 87.0 ? 37 O ? B ASP 110 ? B ASP 110 ? 1_555 CA ? AA CA . ? B CA 608 ? 1_555 OD1 ? B ASP 110 ? B ASP 110 ? 1_555 81.9 ? 38 O ? B ASP 110 ? B ASP 110 ? 1_555 CA ? AA CA . ? B CA 608 ? 1_555 O ? B THR 184 ? B THR 184 ? 1_555 76.4 ? 39 OD1 ? B ASP 110 ? B ASP 110 ? 1_555 CA ? AA CA . ? B CA 608 ? 1_555 O ? B THR 184 ? B THR 184 ? 1_555 144.0 ? 40 O ? B ASP 110 ? B ASP 110 ? 1_555 CA ? AA CA . ? B CA 608 ? 1_555 OG1 ? B THR 184 ? B THR 184 ? 1_555 126.6 ? 41 OD1 ? B ASP 110 ? B ASP 110 ? 1_555 CA ? AA CA . ? B CA 608 ? 1_555 OG1 ? B THR 184 ? B THR 184 ? 1_555 141.9 ? 42 O ? B THR 184 ? B THR 184 ? 1_555 CA ? AA CA . ? B CA 608 ? 1_555 OG1 ? B THR 184 ? B THR 184 ? 1_555 73.3 ? 43 O ? B ASP 110 ? B ASP 110 ? 1_555 CA ? AA CA . ? B CA 608 ? 1_555 O ? B PHE 186 ? B PHE 186 ? 1_555 120.8 ? 44 OD1 ? B ASP 110 ? B ASP 110 ? 1_555 CA ? AA CA . ? B CA 608 ? 1_555 O ? B PHE 186 ? B PHE 186 ? 1_555 82.3 ? 45 O ? B THR 184 ? B THR 184 ? 1_555 CA ? AA CA . ? B CA 608 ? 1_555 O ? B PHE 186 ? B PHE 186 ? 1_555 84.5 ? 46 OG1 ? B THR 184 ? B THR 184 ? 1_555 CA ? AA CA . ? B CA 608 ? 1_555 O ? B PHE 186 ? B PHE 186 ? 1_555 98.9 ? 47 O ? B ASP 110 ? B ASP 110 ? 1_555 CA ? AA CA . ? B CA 608 ? 1_555 OD1 ? B ASP 188 ? B ASP 188 ? 1_555 146.0 ? 48 OD1 ? B ASP 110 ? B ASP 110 ? 1_555 CA ? AA CA . ? B CA 608 ? 1_555 OD1 ? B ASP 188 ? B ASP 188 ? 1_555 74.5 ? 49 O ? B THR 184 ? B THR 184 ? 1_555 CA ? AA CA . ? B CA 608 ? 1_555 OD1 ? B ASP 188 ? B ASP 188 ? 1_555 135.5 ? 50 OG1 ? B THR 184 ? B THR 184 ? 1_555 CA ? AA CA . ? B CA 608 ? 1_555 OD1 ? B ASP 188 ? B ASP 188 ? 1_555 68.3 ? 51 O ? B PHE 186 ? B PHE 186 ? 1_555 CA ? AA CA . ? B CA 608 ? 1_555 OD1 ? B ASP 188 ? B ASP 188 ? 1_555 80.3 ? 52 O ? B ASP 110 ? B ASP 110 ? 1_555 CA ? AA CA . ? B CA 608 ? 1_555 OG ? B SER 190 ? B SER 190 ? 1_555 79.4 ? 53 OD1 ? B ASP 110 ? B ASP 110 ? 1_555 CA ? AA CA . ? B CA 608 ? 1_555 OG ? B SER 190 ? B SER 190 ? 1_555 84.4 ? 54 O ? B THR 184 ? B THR 184 ? 1_555 CA ? AA CA . ? B CA 608 ? 1_555 OG ? B SER 190 ? B SER 190 ? 1_555 118.7 ? 55 OG1 ? B THR 184 ? B THR 184 ? 1_555 CA ? AA CA . ? B CA 608 ? 1_555 OG ? B SER 190 ? B SER 190 ? 1_555 78.1 ? 56 O ? B PHE 186 ? B PHE 186 ? 1_555 CA ? AA CA . ? B CA 608 ? 1_555 OG ? B SER 190 ? B SER 190 ? 1_555 153.7 ? 57 OD1 ? B ASP 188 ? B ASP 188 ? 1_555 CA ? AA CA . ? B CA 608 ? 1_555 OG ? B SER 190 ? B SER 190 ? 1_555 74.3 ? 58 NE2 ? B HIS 351 ? B HIS 351 ? 1_555 FE ? Z HEM . ? B HEM 607 ? 1_555 NA ? Z HEM . ? B HEM 607 ? 1_555 96.8 ? 59 NE2 ? B HIS 351 ? B HIS 351 ? 1_555 FE ? Z HEM . ? B HEM 607 ? 1_555 NB ? Z HEM . ? B HEM 607 ? 1_555 93.3 ? 60 NA ? Z HEM . ? B HEM 607 ? 1_555 FE ? Z HEM . ? B HEM 607 ? 1_555 NB ? Z HEM . ? B HEM 607 ? 1_555 88.2 ? 61 NE2 ? B HIS 351 ? B HIS 351 ? 1_555 FE ? Z HEM . ? B HEM 607 ? 1_555 NC ? Z HEM . ? B HEM 607 ? 1_555 87.8 ? 62 NA ? Z HEM . ? B HEM 607 ? 1_555 FE ? Z HEM . ? B HEM 607 ? 1_555 NC ? Z HEM . ? B HEM 607 ? 1_555 174.1 ? 63 NB ? Z HEM . ? B HEM 607 ? 1_555 FE ? Z HEM . ? B HEM 607 ? 1_555 NC ? Z HEM . ? B HEM 607 ? 1_555 87.9 ? 64 NE2 ? B HIS 351 ? B HIS 351 ? 1_555 FE ? Z HEM . ? B HEM 607 ? 1_555 ND ? Z HEM . ? B HEM 607 ? 1_555 91.4 ? 65 NA ? Z HEM . ? B HEM 607 ? 1_555 FE ? Z HEM . ? B HEM 607 ? 1_555 ND ? Z HEM . ? B HEM 607 ? 1_555 90.7 ? 66 NB ? Z HEM . ? B HEM 607 ? 1_555 FE ? Z HEM . ? B HEM 607 ? 1_555 ND ? Z HEM . ? B HEM 607 ? 1_555 175.3 ? 67 NC ? Z HEM . ? B HEM 607 ? 1_555 FE ? Z HEM . ? B HEM 607 ? 1_555 ND ? Z HEM . ? B HEM 607 ? 1_555 92.8 ? 68 NE2 ? B HIS 351 ? B HIS 351 ? 1_555 FE ? Z HEM . ? B HEM 607 ? 1_555 S2 ? T MMZ . ? B MMZ 601 ? 1_555 173.8 ? 69 NA ? Z HEM . ? B HEM 607 ? 1_555 FE ? Z HEM . ? B HEM 607 ? 1_555 S2 ? T MMZ . ? B MMZ 601 ? 1_555 81.6 ? 70 NB ? Z HEM . ? B HEM 607 ? 1_555 FE ? Z HEM . ? B HEM 607 ? 1_555 S2 ? T MMZ . ? B MMZ 601 ? 1_555 80.7 ? 71 NC ? Z HEM . ? B HEM 607 ? 1_555 FE ? Z HEM . ? B HEM 607 ? 1_555 S2 ? T MMZ . ? B MMZ 601 ? 1_555 93.4 ? 72 ND ? Z HEM . ? B HEM 607 ? 1_555 FE ? Z HEM . ? B HEM 607 ? 1_555 S2 ? T MMZ . ? B MMZ 601 ? 1_555 94.6 ? # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2016-01-13 2 'Structure model' 1 1 2016-07-27 # _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' # 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 ? ? ? 5.7.0032 1 ? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? . 2 ? 'data scaling' ? ? ? ? ? ? ? ? ? ? ? SCALEPACK ? ? ? . 3 ? phasing ? ? ? ? ? ? ? ? ? ? ? AMoRE ? ? ? . 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 OD2 A ASP 108 ? ? CMD A HEM 607 ? ? 1.64 2 1 OD2 B ASP 108 ? ? CMD B HEM 607 ? ? 1.67 3 1 OE2 B GLU 258 ? ? CMB B HEM 607 ? ? 1.68 4 1 OE2 A GLU 258 ? ? CMB A HEM 607 ? ? 1.76 5 1 OE2 A GLU 52 ? ? O1 A GOL 614 ? ? 2.16 # _pdbx_validate_rmsd_bond.id 1 _pdbx_validate_rmsd_bond.PDB_model_num 1 _pdbx_validate_rmsd_bond.auth_atom_id_1 CA _pdbx_validate_rmsd_bond.auth_asym_id_1 B _pdbx_validate_rmsd_bond.auth_comp_id_1 ASP _pdbx_validate_rmsd_bond.auth_seq_id_1 108 _pdbx_validate_rmsd_bond.PDB_ins_code_1 ? _pdbx_validate_rmsd_bond.label_alt_id_1 ? _pdbx_validate_rmsd_bond.auth_atom_id_2 CB _pdbx_validate_rmsd_bond.auth_asym_id_2 B _pdbx_validate_rmsd_bond.auth_comp_id_2 ASP _pdbx_validate_rmsd_bond.auth_seq_id_2 108 _pdbx_validate_rmsd_bond.PDB_ins_code_2 ? _pdbx_validate_rmsd_bond.label_alt_id_2 ? _pdbx_validate_rmsd_bond.bond_value 1.372 _pdbx_validate_rmsd_bond.bond_target_value 1.535 _pdbx_validate_rmsd_bond.bond_deviation -0.163 _pdbx_validate_rmsd_bond.bond_standard_deviation 0.022 _pdbx_validate_rmsd_bond.linker_flag N # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 NE A ARG 67 ? ? CZ A ARG 67 ? ? NH1 A ARG 67 ? ? 123.39 120.30 3.09 0.50 N 2 1 C A THR 169 ? ? N A PRO 170 ? ? CA A PRO 170 ? ? 109.10 119.30 -10.20 1.50 Y 3 1 NE A ARG 177 ? ? CZ A ARG 177 ? ? NH1 A ARG 177 ? ? 125.79 120.30 5.49 0.50 N 4 1 NE A ARG 177 ? ? CZ A ARG 177 ? ? NH2 A ARG 177 ? ? 113.06 120.30 -7.24 0.50 N 5 1 NE B ARG 67 ? ? CZ B ARG 67 ? ? NH2 B ARG 67 ? ? 117.27 120.30 -3.03 0.50 N 6 1 C B CYS 167 ? ? N B PRO 168 ? ? CA B PRO 168 ? ? 133.05 119.30 13.75 1.50 Y 7 1 C B CYS 167 ? ? N B PRO 168 ? ? CD B PRO 168 ? ? 115.00 128.40 -13.40 2.10 Y 8 1 NE B ARG 177 ? ? CZ B ARG 177 ? ? NH1 B ARG 177 ? ? 116.43 120.30 -3.87 0.50 N 9 1 NE B ARG 177 ? ? CZ B ARG 177 ? ? NH2 B ARG 177 ? ? 124.56 120.30 4.26 0.50 N 10 1 CB B ASP 178 ? ? CG B ASP 178 ? ? OD1 B ASP 178 ? ? 124.23 118.30 5.93 0.90 N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 TRP A 2 ? ? -102.48 -169.43 2 1 PRO A 9 ? ? -85.60 -151.87 3 1 PRO A 11 ? ? -71.11 -116.58 4 1 GLU A 17 ? ? -82.76 -78.66 5 1 ALA A 56 ? ? -152.13 -19.19 6 1 ASP A 137 ? ? 54.52 -128.25 7 1 TYR A 172 ? ? 89.73 4.22 8 1 ASP A 188 ? ? -140.43 23.46 9 1 PRO A 209 ? ? -82.67 40.84 10 1 ASN A 241 ? ? -163.05 91.36 11 1 GLU A 371 ? ? -112.46 53.60 12 1 ASP A 389 ? ? -143.38 51.40 13 1 ASN A 473 ? ? -166.28 113.63 14 1 LYS A 485 ? ? 86.32 -29.13 15 1 PRO A 589 ? ? -57.46 -7.35 16 1 ALA A 591 ? ? -58.95 109.85 17 1 TRP B 2 ? ? -163.87 67.28 18 1 GLU B 3 ? ? -149.63 14.32 19 1 VAL B 4 ? ? -31.72 140.64 20 1 PRO B 9 ? ? -93.67 -145.42 21 1 GLU B 17 ? ? -37.80 -73.29 22 1 ALA B 56 ? ? -154.61 -17.87 23 1 ASP B 137 ? ? 52.28 -124.23 24 1 LYS B 146 ? ? -34.88 135.06 25 1 CYS B 167 ? ? 82.31 55.70 26 1 PRO B 168 ? ? -9.95 106.56 27 1 THR B 169 ? ? 56.86 168.62 28 1 PRO B 170 ? ? -1.88 -117.24 29 1 GLN B 173 ? ? -154.81 -98.71 30 1 SER B 174 ? ? -101.81 -169.57 31 1 LEU B 175 ? ? 37.39 133.04 32 1 PRO B 209 ? ? -89.46 37.89 33 1 ASN B 241 ? ? -164.34 92.02 34 1 HIS B 245 ? ? 37.07 52.84 35 1 GLU B 371 ? ? -110.47 54.02 36 1 ASP B 389 ? ? -144.84 50.78 37 1 ASN B 473 ? ? -165.77 114.85 38 1 LYS B 485 ? ? 76.92 -45.49 39 1 PRO B 589 ? ? -56.05 -7.99 40 1 ALA B 591 ? ? -57.67 108.94 41 1 ARG B 593 ? ? 62.02 -134.14 # loop_ _pdbx_validate_peptide_omega.id _pdbx_validate_peptide_omega.PDB_model_num _pdbx_validate_peptide_omega.auth_comp_id_1 _pdbx_validate_peptide_omega.auth_asym_id_1 _pdbx_validate_peptide_omega.auth_seq_id_1 _pdbx_validate_peptide_omega.PDB_ins_code_1 _pdbx_validate_peptide_omega.label_alt_id_1 _pdbx_validate_peptide_omega.auth_comp_id_2 _pdbx_validate_peptide_omega.auth_asym_id_2 _pdbx_validate_peptide_omega.auth_seq_id_2 _pdbx_validate_peptide_omega.PDB_ins_code_2 _pdbx_validate_peptide_omega.label_alt_id_2 _pdbx_validate_peptide_omega.omega 1 1 PRO A 11 ? ? LEU A 12 ? ? -143.88 2 1 CYS B 167 ? ? PRO B 168 ? ? -139.04 3 1 PRO B 168 ? ? THR B 169 ? ? 124.66 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 1-METHYL-1,3-DIHYDRO-2H-IMIDAZOLE-2-THIONE MMZ 3 N-ACETYL-D-GLUCOSAMINE NAG 4 'PROTOPORPHYRIN IX CONTAINING FE' HEM 5 'CALCIUM ION' CA 6 'NITRATE ION' NO3 7 GLYCEROL GOL 8 water HOH #