data_2PUM # _entry.id 2PUM # _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 2PUM RCSB RCSB042788 WWPDB D_1000042788 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 2NQX 'Crystal Structure of bovine lactoperoxidase with iodide ions at 2.9A resolution' unspecified PDB 2PT3 'Crystal structure of bovine lactoperoxidase at 2.34 A resolution reveals multiple anion binding sites' unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 2PUM _pdbx_database_status.recvd_initial_deposition_date 2007-05-09 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_cs ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Singh, A.K.' 1 'Singh, N.' 2 'Sharma, S.' 3 'Kaur, P.' 4 'Singh, T.P.' 5 # _citation.id primary _citation.title 'Crystal structure of bovine lactoperoxidase complex with catechol and iodide at 2.7 A resolution' _citation.journal_abbrev 'To be Published' _citation.journal_volume ? _citation.page_first ? _citation.page_last ? _citation.year ? _citation.journal_id_ASTM ? _citation.country ? _citation.journal_id_ISSN ? _citation.journal_id_CSD 0353 _citation.book_publisher ? _citation.pdbx_database_id_PubMed ? _citation.pdbx_database_id_DOI ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Singh, A.K.' 1 primary 'Singh, N.' 2 primary 'Sharma, S.' 3 primary 'Kaur, P.' 4 primary 'Singh, T.P.' 5 # _cell.entry_id 2PUM _cell.length_a 54.422 _cell.length_b 80.489 _cell.length_c 77.321 _cell.angle_alpha 90.00 _cell.angle_beta 102.60 _cell.angle_gamma 90.00 _cell.Z_PDB 2 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 2PUM _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 _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer nat Lactoperoxidase 67853.281 1 1.11.1.7 ? Lactoperoxidase ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 8 ? ? ? ? 3 non-polymer man ALPHA-D-MANNOSE 180.156 2 ? ? ? ? 4 non-polymer syn 'CALCIUM ION' 40.078 1 ? ? ? ? 5 non-polymer syn 'THIOCYANATE ION' 58.082 1 ? ? ? ? 6 non-polymer syn 'IODIDE ION' 126.904 10 ? ? ? ? 7 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE' 616.487 1 ? ? ? ? 8 non-polymer syn CATECHOL 110.111 1 ? ? ? ? 9 water nat water 18.015 281 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name LPO # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer yes _entity_poly.pdbx_seq_one_letter_code ;SWEVGCGAPVPLVKCDENSPYRTITGDCNNRRSPALGAANRALARWLPAEYEDGLALPFGWTQRKTRNGFRVPLAREVSN KIVGYLDEEGVLDQNRSLLFMQWGQIVDHDLDFAPETELGSNEHSKTQCEEYCIQGDNCFPIMFPKNDPKLKTQGKCMPF FRAGFVCPTPPYQSLAREQINAVTSFLDASLVYGSEP(SEP)LASRLRNLSSPLGLMAVNQEAWDHGLAYLPFNNKKPSP CEFINTTARVPCFLAGDFRASEQILLATAHTLLLREHNRLARELKKLNPHWNGEKLYQEARKILGAFIQIITFRDYLPIV LGSEMQKWIPPYQGYNNSVDPRISNVFTFAFRFGHMEVPSTVSRLDENYQPWGPEAELPLHTLFFNTWRIIKDGGIDPLV RGLLAKKSKLMNQDKMVTSELRNKLFQPTHKIHGFDLAAINLQRCRDHGMPGYNSWRGFCGLSQPKTLKGLQTVLKNKIL AKKLMDLYKTPDNIDIWIGGNAEPMVERGRVGPLLACLLGRQFQQIRDGDRFWWENPGVFTEKQRDSLQKVSFSRLICDN THITKVPLHAFQANNYPHDFVDCSTVDKLDLSPWASREN ; _entity_poly.pdbx_seq_one_letter_code_can ;SWEVGCGAPVPLVKCDENSPYRTITGDCNNRRSPALGAANRALARWLPAEYEDGLALPFGWTQRKTRNGFRVPLAREVSN KIVGYLDEEGVLDQNRSLLFMQWGQIVDHDLDFAPETELGSNEHSKTQCEEYCIQGDNCFPIMFPKNDPKLKTQGKCMPF FRAGFVCPTPPYQSLAREQINAVTSFLDASLVYGSEPSLASRLRNLSSPLGLMAVNQEAWDHGLAYLPFNNKKPSPCEFI NTTARVPCFLAGDFRASEQILLATAHTLLLREHNRLARELKKLNPHWNGEKLYQEARKILGAFIQIITFRDYLPIVLGSE MQKWIPPYQGYNNSVDPRISNVFTFAFRFGHMEVPSTVSRLDENYQPWGPEAELPLHTLFFNTWRIIKDGGIDPLVRGLL AKKSKLMNQDKMVTSELRNKLFQPTHKIHGFDLAAINLQRCRDHGMPGYNSWRGFCGLSQPKTLKGLQTVLKNKILAKKL MDLYKTPDNIDIWIGGNAEPMVERGRVGPLLACLLGRQFQQIRDGDRFWWENPGVFTEKQRDSLQKVSFSRLICDNTHIT KVPLHAFQANNYPHDFVDCSTVDKLDLSPWASREN ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 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 LYS n 1 15 CYS n 1 16 ASP n 1 17 GLU n 1 18 ASN 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 LEU 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 ASN n 1 123 GLU n 1 124 HIS n 1 125 SER n 1 126 LYS n 1 127 THR 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 ILE n 1 135 GLN n 1 136 GLY n 1 137 ASP n 1 138 ASN 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 GLU 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 SEP 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 LEU n 1 228 PRO n 1 229 PHE n 1 230 ASN n 1 231 ASN n 1 232 LYS 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 ARG n 1 246 VAL n 1 247 PRO n 1 248 CYS n 1 249 PHE n 1 250 LEU n 1 251 ALA n 1 252 GLY n 1 253 ASP n 1 254 PHE 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 ALA 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 LYS n 1 283 LEU n 1 284 ASN n 1 285 PRO n 1 286 HIS n 1 287 TRP n 1 288 ASN n 1 289 GLY n 1 290 GLU n 1 291 LYS 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 LYS 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 ASP 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 ILE 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 THR n 1 470 VAL n 1 471 LEU n 1 472 LYS n 1 473 ASN n 1 474 LYS n 1 475 ILE n 1 476 LEU n 1 477 ALA n 1 478 LYS n 1 479 LYS n 1 480 LEU n 1 481 MET 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 THR 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 ? _entity_src_nat.pdbx_end_seq_num ? _entity_src_nat.common_name cattle _entity_src_nat.pdbx_organism_scientific 'Bos taurus' _entity_src_nat.pdbx_ncbi_taxonomy_id 9913 _entity_src_nat.genus Bos _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.id 1 _struct_ref.db_name UNP _struct_ref.db_code PERL_BOVIN _struct_ref.pdbx_db_accession P80025 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;SWEVGCGAPVPLVKCDENSPYRTITGDCNNRRSPALGAANRALARWLPAEYEDGLALPFGWTQRKTRNGFRVPLAREVSN KIVGYLDEEGVLDQNRSLLFMQWGQIVDHDLDFAPETELGSNEHSKTQCEEYCIQGDNCFPIMFPKNDPKLKTQGKCMPF FRAGFVCPTPPYQSLAREQINAVTSFLDASLVYGSEPSLASRLRNLSSPLGLMAVNQEAWDHGLAYLPFNNKKPSPCEFI NTTARVPCFLAGDFRASEQILLATAHTLLLREHNRLARELKKLNPHWNGEKLYQEARKILGAFIQIITFRDYLPIVLGSE MQKWIPPYQGYNNSVDPRISNVFTFAFRFGHMEVPSTVSRLDENYQPWGPEAELPLHTLFFNTWRIIKDGGIDPLVRGLL AKKSKLMNQDKMVTSELRNKLFQPTHKIHGFDLAAINLQRCRDHGMPGYNSWRGFCGLSQPKTLKGLQTVLKNKILAKKL MDLYKTPDNIDIWIGGNAEPMVERGRVGPLLACLLGRQFQQIRDGDRFWWENPGVFTEKQRDSLQKVSFSRLICDNTHIT KVPLHAFQANNYPHDFVDCSTVDKLDLSPWASREN ; _struct_ref.pdbx_align_begin 118 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 2PUM _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 1 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 595 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession P80025 _struct_ref_seq.db_align_beg 118 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 712 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 1 _struct_ref_seq.pdbx_auth_seq_align_end 595 # _struct_ref_seq_dif.align_id 1 _struct_ref_seq_dif.pdbx_pdb_id_code 2PUM _struct_ref_seq_dif.mon_id SEP _struct_ref_seq_dif.pdbx_pdb_strand_id A _struct_ref_seq_dif.seq_num 198 _struct_ref_seq_dif.pdbx_pdb_ins_code ? _struct_ref_seq_dif.pdbx_seq_db_name UNP _struct_ref_seq_dif.pdbx_seq_db_accession_code P80025 _struct_ref_seq_dif.db_mon_id SER _struct_ref_seq_dif.pdbx_seq_db_seq_num 315 _struct_ref_seq_dif.details 'MODIFIED RESIDUE' _struct_ref_seq_dif.pdbx_auth_seq_num 198 _struct_ref_seq_dif.pdbx_ordinal 1 # 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 CAQ non-polymer . CATECHOL 1,2-DIHYDROXYBENZENE 'C6 H6 O2' 110.111 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 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 IOD non-polymer . 'IODIDE ION' ? 'I -1' 126.904 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SCN non-polymer . 'THIOCYANATE ION' ? 'C N S -1' 58.082 SEP 'L-peptide linking' n PHOSPHOSERINE PHOSPHONOSERINE 'C3 H8 N O6 P' 185.072 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.entry_id 2PUM _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.43 _exptl_crystal.density_percent_sol 49.47 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 298 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 6.8 _exptl_crystal_grow.pdbx_details 'Tris-HCl, Ammonium Iodide, Catechol, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K' _exptl_crystal_grow.pdbx_pH_range . # _diffrn.id 1 _diffrn.ambient_temp 292 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector 'IMAGE PLATE' _diffrn_detector.type 'MAR scanner 345 mm plate' _diffrn_detector.pdbx_collection_date 2007-03-05 _diffrn_detector.details Mirror # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator Graphite _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.54132 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source 'ROTATING ANODE' _diffrn_source.type 'RIGAKU RU300' _diffrn_source.pdbx_synchrotron_site ? _diffrn_source.pdbx_synchrotron_beamline ? _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1.54132 # _reflns.entry_id 2PUM _reflns.observed_criterion_sigma_F 0 _reflns.observed_criterion_sigma_I 0 _reflns.d_resolution_high 2.7 _reflns.d_resolution_low 74.54 _reflns.number_all 17885 _reflns.number_obs 16961 _reflns.percent_possible_obs 99.4 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy ? _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 2.7 _reflns_shell.d_res_low 2.8 _reflns_shell.percent_possible_all 97.5 _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.pdbx_redundancy ? _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 2PUM _refine.ls_number_reflns_obs 16961 _refine.ls_number_reflns_all 17885 _refine.pdbx_ls_sigma_I 0 _refine.pdbx_ls_sigma_F 0 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 24.93 _refine.ls_d_res_high 2.70 _refine.ls_percent_reflns_obs 99.23 _refine.ls_R_factor_obs 0.1666 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.16463 _refine.ls_R_factor_R_free 0.20283 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.1 _refine.ls_number_reflns_R_free 912 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.945 _refine.correlation_coeff_Fo_to_Fc_free 0.909 _refine.B_iso_mean 41.896 _refine.aniso_B[1][1] -0.67 _refine.aniso_B[2][2] -0.67 _refine.aniso_B[3][3] 0.93 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] -0.95 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details 'BABINET MODEL WITH MASK' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.40 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details ? _refine.pdbx_starting_model 2NQX _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 ? _refine.pdbx_overall_ESU_R_Free 0.311 _refine.overall_SU_ML 0.233 _refine.overall_SU_B 11.374 _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_overall_phase_error ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _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 4774 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 199 _refine_hist.number_atoms_solvent 281 _refine_hist.number_atoms_total 5254 _refine_hist.d_res_high 2.70 _refine_hist.d_res_low 24.93 # 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 0.016 0.021 ? 5120 'X-RAY DIFFRACTION' ? r_bond_other_d ? ? ? ? 'X-RAY DIFFRACTION' ? r_angle_refined_deg 2.046 2.009 ? 6980 'X-RAY DIFFRACTION' ? r_angle_other_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.452 3.000 ? 596 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 22.134 15.000 ? 895 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_chiral_restr 0.138 0.200 ? 751 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.009 0.020 ? 3891 'X-RAY DIFFRACTION' ? r_gen_planes_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_refined 0.265 0.300 ? 2581 '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 0.171 0.500 ? 429 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined 0.173 0.500 ? 5 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined 0.259 0.300 ? 31 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined 0.256 0.500 ? 11 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it 0.930 1.500 ? 2980 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it 1.755 2.000 ? 4814 'X-RAY DIFFRACTION' ? r_scbond_it 2.271 3.000 ? 2140 'X-RAY DIFFRACTION' ? r_scangle_it 3.878 4.500 ? 2165 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 2.700 _refine_ls_shell.d_res_low 2.770 _refine_ls_shell.number_reflns_R_work 1201 _refine_ls_shell.R_factor_R_work 0.223 _refine_ls_shell.percent_reflns_obs ? _refine_ls_shell.R_factor_R_free 0.274 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 66 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' # _struct.entry_id 2PUM _struct.title 'Crystal structure of bovine lactoperoxidase complex with catechol and iodide at 2.7 A resolution' _struct.pdbx_descriptor 'Lactoperoxidase (E.C.1.11.1.7)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 2PUM _struct_keywords.pdbx_keywords OXIDOREDUCTASE _struct_keywords.text 'Heme, Anion Binding, 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 2 ? C N N 2 ? D N N 3 ? E N N 2 ? F N N 2 ? G N N 2 ? H N N 2 ? I N N 3 ? J N N 2 ? K N N 2 ? L N N 4 ? M N N 5 ? N N N 6 ? O N N 6 ? P N N 6 ? Q N N 6 ? R N N 6 ? S N N 6 ? T N N 6 ? U N N 6 ? V N N 6 ? W N N 6 ? X N N 7 ? Y N N 8 ? Z N N 9 ? # _struct_biol.id 1 # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 LEU A 74 ? VAL A 83 ? LEU A 74 VAL A 83 1 ? 10 HELX_P HELX_P2 2 LEU A 98 ? ASP A 112 ? LEU A 98 ASP A 112 1 ? 15 HELX_P HELX_P3 3 PRO A 149 ? GLN A 154 ? PRO A 149 GLN A 154 1 ? 6 HELX_P HELX_P4 4 ALA A 189 ? GLY A 194 ? ALA A 189 GLY A 194 1 ? 6 HELX_P HELX_P5 5 SEP A 198 ? LEU A 203 ? SEP A 198 LEU A 203 1 ? 6 HELX_P HELX_P6 6 SER A 235 ? ILE A 240 ? SER A 235 ILE A 240 1 ? 6 HELX_P HELX_P7 7 GLN A 259 ? ASN A 284 ? GLN A 259 ASN A 284 1 ? 26 HELX_P HELX_P8 8 ASN A 288 ? TYR A 312 ? ASN A 288 TYR A 312 1 ? 25 HELX_P HELX_P9 9 LEU A 313 ? GLY A 318 ? LEU A 313 GLY A 318 1 ? 6 HELX_P HELX_P10 10 GLU A 320 ? ILE A 325 ? GLU A 320 ILE A 325 1 ? 6 HELX_P HELX_P11 11 VAL A 342 ? PHE A 347 ? VAL A 342 PHE A 347 1 ? 6 HELX_P HELX_P12 12 ARG A 348 ? VAL A 354 ? ARG A 348 VAL A 354 5 ? 7 HELX_P HELX_P13 13 HIS A 377 ? PHE A 380 ? HIS A 377 PHE A 380 5 ? 4 HELX_P HELX_P14 14 THR A 383 ? LYS A 388 ? THR A 383 LYS A 388 1 ? 6 HELX_P HELX_P15 15 ILE A 392 ? LYS A 402 ? ILE A 392 LYS A 402 1 ? 11 HELX_P HELX_P16 16 THR A 414 ? ASN A 419 ? THR A 414 ASN A 419 1 ? 6 HELX_P HELX_P17 17 ASP A 432 ? HIS A 444 ? ASP A 432 HIS A 444 1 ? 13 HELX_P HELX_P18 18 GLY A 448 ? CYS A 456 ? GLY A 448 CYS A 456 1 ? 9 HELX_P HELX_P19 19 THR A 463 ? LYS A 472 ? THR A 463 LYS A 472 1 ? 10 HELX_P HELX_P20 20 ASN A 473 ? LYS A 485 ? ASN A 473 LYS A 485 1 ? 13 HELX_P HELX_P21 21 THR A 486 ? ILE A 490 ? THR A 486 ILE A 490 5 ? 5 HELX_P HELX_P22 22 ASP A 491 ? GLU A 499 ? ASP A 491 GLU A 499 1 ? 9 HELX_P HELX_P23 23 GLY A 508 ? GLY A 525 ? GLY A 508 GLY A 525 1 ? 18 HELX_P HELX_P24 24 THR A 537 ? GLN A 545 ? THR A 537 GLN A 545 1 ? 9 HELX_P HELX_P25 25 SER A 548 ? THR A 557 ? SER A 548 THR A 557 1 ? 10 # _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 ? ? ? ? ? ? ? 2.190 ? disulf2 disulf ? ? A CYS 15 SG ? ? ? 1_555 A CYS 28 SG ? ? A CYS 15 A CYS 28 1_555 ? ? ? ? ? ? ? 2.033 ? disulf3 disulf ? ? A CYS 129 SG ? ? ? 1_555 A CYS 139 SG ? ? A CYS 129 A CYS 139 1_555 ? ? ? ? ? ? ? 1.974 ? disulf4 disulf ? ? A CYS 133 SG ? ? ? 1_555 A CYS 157 SG ? ? A CYS 133 A CYS 157 1_555 ? ? ? ? ? ? ? 2.019 ? disulf5 disulf ? ? A CYS 237 SG ? ? ? 1_555 A CYS 248 SG ? ? A CYS 237 A CYS 248 1_555 ? ? ? ? ? ? ? 2.213 ? disulf6 disulf ? ? A CYS 456 SG ? ? ? 1_555 A CYS 513 SG ? ? A CYS 456 A CYS 513 1_555 ? ? ? ? ? ? ? 2.029 ? disulf7 disulf ? ? A CYS 554 SG ? ? ? 1_555 A CYS 579 SG ? ? A CYS 554 A CYS 579 1_555 ? ? ? ? ? ? ? 1.994 ? covale1 covale ? ? A ASN 95 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 95 A NAG 596 1_555 ? ? ? ? ? ? ? 1.468 ? covale2 covale ? ? A ASN 205 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 205 A NAG 599 1_555 ? ? ? ? ? ? ? 1.445 ? covale3 covale ? ? A ASN 332 ND2 ? ? ? 1_555 J NAG . C1 ? ? A ASN 332 A NAG 604 1_555 ? ? ? ? ? ? ? 1.458 ? covale4 covale ? ? B NAG . O4 ? ? ? 1_555 C NAG . C1 ? ? A NAG 596 A NAG 597 1_555 ? ? ? ? ? ? ? 1.416 ? covale5 covale ? ? C NAG . O4 ? ? ? 1_555 D MAN . C1 ? ? A NAG 597 A MAN 598 1_555 ? ? ? ? ? ? ? 1.469 ? covale6 covale ? ? E NAG . O4 ? ? ? 1_555 F NAG . C1 ? ? A NAG 599 A NAG 600 1_555 ? ? ? ? ? ? ? 1.443 ? covale7 covale ? ? J NAG . O4 ? ? ? 1_555 K NAG . C1 ? ? A NAG 604 A NAG 605 1_555 ? ? ? ? ? ? ? 1.448 ? metalc1 metalc ? ? A HIS 351 NE2 ? ? ? 1_555 X HEM . FE ? ? A HIS 351 A HEM 618 1_555 ? ? ? ? ? ? ? 2.192 ? metalc2 metalc ? ? X HEM . FE ? ? ? 1_555 Z HOH . O ? ? A HEM 618 A HOH 649 1_555 ? ? ? ? ? ? ? 2.529 ? covale8 covale ? ? A ASP 108 OD2 ? ? ? 1_555 X HEM . CMD ? ? A ASP 108 A HEM 618 1_555 ? ? ? ? ? ? ? 1.536 ? covale9 covale ? ? A GLU 258 OE2 ? ? ? 1_555 X HEM . CMB ? ? A GLU 258 A HEM 618 1_555 ? ? ? ? ? ? ? 1.570 ? metalc3 metalc ? ? A ASP 110 O ? ? ? 1_555 L CA . CA ? ? A ASP 110 A CA 606 1_555 ? ? ? ? ? ? ? 2.172 ? metalc4 metalc ? ? A ASP 110 OD1 ? ? ? 1_555 L CA . CA ? ? A ASP 110 A CA 606 1_555 ? ? ? ? ? ? ? 2.096 ? metalc5 metalc ? ? A THR 184 O ? ? ? 1_555 L CA . CA ? ? A THR 184 A CA 606 1_555 ? ? ? ? ? ? ? 2.580 ? metalc6 metalc ? ? A THR 184 OG1 ? ? ? 1_555 L CA . CA ? ? A THR 184 A CA 606 1_555 ? ? ? ? ? ? ? 2.587 ? metalc7 metalc ? ? A PHE 186 O ? ? ? 1_555 L CA . CA ? ? A PHE 186 A CA 606 1_555 ? ? ? ? ? ? ? 2.428 ? metalc8 metalc ? ? A ASP 188 OD1 ? ? ? 1_555 L CA . CA ? ? A ASP 188 A CA 606 1_555 ? ? ? ? ? ? ? 2.310 ? metalc9 metalc ? ? A SER 190 OG ? ? ? 1_555 L CA . CA ? ? A SER 190 A CA 606 1_555 ? ? ? ? ? ? ? 2.313 ? covale10 covale ? ? A ASN 241 ND2 ? ? ? 1_555 G NAG . C1 ? ? A ASN 241 A NAG 601 1_555 ? ? ? ? ? ? ? 1.475 ? covale11 covale ? ? G NAG . O4 ? ? ? 1_555 H NAG . C1 ? ? A NAG 601 A NAG 602 1_555 ? ? ? ? ? ? ? 1.426 ? covale12 covale ? ? H NAG . O4 ? ? ? 1_555 I MAN . C1 ? ? A NAG 602 A MAN 603 1_555 ? ? ? ? ? ? ? 1.466 ? covale13 covale ? ? A PRO 197 C ? ? ? 1_555 A SEP 198 N ? ? A PRO 197 A SEP 198 1_555 ? ? ? ? ? ? ? 1.308 ? covale14 covale ? ? A SEP 198 C ? ? ? 1_555 A LEU 199 N ? ? A SEP 198 A LEU 199 1_555 ? ? ? ? ? ? ? 1.316 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 LYS 233 A . ? LYS 233 A PRO 234 A ? PRO 234 A 1 2.18 2 TYR 572 A . ? TYR 572 A PRO 573 A ? PRO 573 A 1 2.01 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 2 ? B ? 2 ? C ? 2 ? D ? 2 ? E ? 2 ? F ? 2 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel B 1 2 ? anti-parallel C 1 2 ? anti-parallel D 1 2 ? anti-parallel E 1 2 ? anti-parallel F 1 2 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 ARG A 41 ? ALA A 42 ? ARG A 41 ALA A 42 A 2 ILE A 180 ? ASN A 181 ? ILE A 180 ASN A 181 B 1 LEU A 92 ? SER A 97 ? LEU A 92 SER A 97 B 2 LYS A 403 ? LYS A 405 ? LYS A 403 LYS A 405 C 1 ILE A 142 ? MET A 143 ? ILE A 142 MET A 143 C 2 CYS A 157 ? MET A 158 ? CYS A 157 MET A 158 D 1 THR A 357 ? SER A 359 ? THR A 357 SER A 359 D 2 GLU A 373 ? PRO A 375 ? GLU A 373 PRO A 375 E 1 LEU A 421 ? PHE A 422 ? LEU A 421 PHE A 422 E 2 HIS A 429 ? PHE A 431 ? HIS A 429 PHE A 431 F 1 LYS A 561 ? VAL A 562 ? LYS A 561 VAL A 562 F 2 VAL A 577 ? ASP A 578 ? VAL A 577 ASP A 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 A 1 2 N ARG A 41 ? N ARG A 41 O ASN A 181 ? O ASN A 181 B 1 2 N ASP A 93 ? N ASP A 93 O SER A 404 ? O SER A 404 C 1 2 N ILE A 142 ? N ILE A 142 O MET A 158 ? O MET A 158 D 1 2 N VAL A 358 ? N VAL A 358 O LEU A 374 ? O LEU A 374 E 1 2 N LEU A 421 ? N LEU A 421 O PHE A 431 ? O PHE A 431 F 1 2 N VAL A 562 ? N VAL A 562 O VAL A 577 ? O VAL A 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 ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 596' AC2 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG A 597' AC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE MAN A 598' AC4 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG A 599' AC5 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG A 600' AC6 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 601' AC7 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 602' AC8 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE MAN A 603' AC9 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 604' BC1 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG A 605' BC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CA A 606' BC3 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE SCN A 607' BC4 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE IOD A 608' BC5 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE IOD A 609' BC6 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE IOD A 610' BC7 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE IOD A 611' BC8 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE IOD A 612' BC9 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE IOD A 613' CC1 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE IOD A 615' CC2 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE IOD A 616' CC3 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE IOD A 617' CC4 Software ? ? ? ? 23 'BINDING SITE FOR RESIDUE HEM A 618' CC5 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE CAQ A 619' # 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 4 ASN A 95 ? ASN A 95 . ? 1_555 ? 2 AC1 4 ILE A 315 ? ILE A 315 . ? 1_555 ? 3 AC1 4 ARG A 504 ? ARG A 504 . ? 1_555 ? 4 AC1 4 NAG C . ? NAG A 597 . ? 1_555 ? 5 AC2 7 HIS A 565 ? HIS A 565 . ? 1_555 ? 6 AC2 7 GLN A 568 ? GLN A 568 . ? 1_555 ? 7 AC2 7 NAG B . ? NAG A 596 . ? 1_555 ? 8 AC2 7 MAN D . ? MAN A 598 . ? 1_555 ? 9 AC2 7 HOH Z . ? HOH A 648 . ? 1_555 ? 10 AC2 7 HOH Z . ? HOH A 842 . ? 1_555 ? 11 AC2 7 HOH Z . ? HOH A 861 . ? 1_555 ? 12 AC3 4 NAG C . ? NAG A 597 . ? 1_555 ? 13 AC3 4 HOH Z . ? HOH A 807 . ? 1_555 ? 14 AC3 4 HOH Z . ? HOH A 813 . ? 1_555 ? 15 AC3 4 HOH Z . ? HOH A 861 . ? 1_555 ? 16 AC4 7 ASN A 205 ? ASN A 205 . ? 1_555 ? 17 AC4 7 SER A 208 ? SER A 208 . ? 1_555 ? 18 AC4 7 ALA A 214 ? ALA A 214 . ? 1_555 ? 19 AC4 7 VAL A 215 ? VAL A 215 . ? 1_555 ? 20 AC4 7 GLN A 217 ? GLN A 217 . ? 1_555 ? 21 AC4 7 NAG F . ? NAG A 600 . ? 1_555 ? 22 AC4 7 HOH Z . ? HOH A 726 . ? 1_555 ? 23 AC5 1 NAG E . ? NAG A 599 . ? 1_555 ? 24 AC6 4 ASN A 241 ? ASN A 241 . ? 1_555 ? 25 AC6 4 ALA A 244 ? ALA A 244 . ? 1_555 ? 26 AC6 4 TRP A 384 ? TRP A 384 . ? 1_555 ? 27 AC6 4 NAG H . ? NAG A 602 . ? 1_555 ? 28 AC7 3 NAG G . ? NAG A 601 . ? 1_555 ? 29 AC7 3 MAN I . ? MAN A 603 . ? 1_555 ? 30 AC7 3 HOH Z . ? HOH A 676 . ? 1_555 ? 31 AC8 2 NAG H . ? NAG A 602 . ? 1_555 ? 32 AC8 2 HOH Z . ? HOH A 793 . ? 1_555 ? 33 AC9 3 ASN A 332 ? ASN A 332 . ? 1_555 ? 34 AC9 3 VAL A 335 ? VAL A 335 . ? 1_555 ? 35 AC9 3 NAG K . ? NAG A 605 . ? 1_555 ? 36 BC1 1 NAG J . ? NAG A 604 . ? 1_555 ? 37 BC2 5 ASP A 110 ? ASP A 110 . ? 1_555 ? 38 BC2 5 THR A 184 ? THR A 184 . ? 1_555 ? 39 BC2 5 PHE A 186 ? PHE A 186 . ? 1_555 ? 40 BC2 5 ASP A 188 ? ASP A 188 . ? 1_555 ? 41 BC2 5 SER A 190 ? SER A 190 . ? 1_555 ? 42 BC3 3 ARG A 202 ? ARG A 202 . ? 1_555 ? 43 BC3 3 ASN A 473 ? ASN A 473 . ? 1_455 ? 44 BC3 3 LYS A 474 ? LYS A 474 . ? 1_455 ? 45 BC4 3 ARG A 255 ? ARG A 255 . ? 1_555 ? 46 BC4 3 HEM X . ? HEM A 618 . ? 1_555 ? 47 BC4 3 HOH Z . ? HOH A 638 . ? 1_555 ? 48 BC5 2 ARG A 31 ? ARG A 31 . ? 1_555 ? 49 BC5 2 HOH Z . ? HOH A 723 . ? 1_555 ? 50 BC6 2 TRP A 46 ? TRP A 46 . ? 1_555 ? 51 BC6 2 VAL A 342 ? VAL A 342 . ? 1_555 ? 52 BC7 2 ASN A 80 ? ASN A 80 . ? 1_555 ? 53 BC7 2 PRO A 145 ? PRO A 145 . ? 1_555 ? 54 BC8 2 ARG A 96 ? ARG A 96 . ? 1_555 ? 55 BC8 2 ARG A 504 ? ARG A 504 . ? 1_555 ? 56 BC9 1 PHE A 229 ? PHE A 229 . ? 1_555 ? 57 CC1 2 GLU A 363 ? GLU A 363 . ? 1_555 ? 58 CC1 2 ARG A 397 ? ARG A 397 . ? 1_555 ? 59 CC2 2 LYS A 462 ? LYS A 462 . ? 1_555 ? 60 CC2 2 THR A 463 ? THR A 463 . ? 1_555 ? 61 CC3 2 HIS A 565 ? HIS A 565 . ? 1_555 ? 62 CC3 2 PHE A 567 ? PHE A 567 . ? 1_555 ? 63 CC4 23 MET A 101 ? MET A 101 . ? 1_555 ? 64 CC4 23 GLY A 104 ? GLY A 104 . ? 1_555 ? 65 CC4 23 GLN A 105 ? GLN A 105 . ? 1_555 ? 66 CC4 23 ASP A 108 ? ASP A 108 . ? 1_555 ? 67 CC4 23 ASP A 112 ? ASP A 112 . ? 1_555 ? 68 CC4 23 PHE A 113 ? PHE A 113 . ? 1_555 ? 69 CC4 23 ALA A 114 ? ALA A 114 . ? 1_555 ? 70 CC4 23 ARG A 255 ? ARG A 255 . ? 1_555 ? 71 CC4 23 GLU A 258 ? GLU A 258 . ? 1_555 ? 72 CC4 23 THR A 344 ? THR A 344 . ? 1_555 ? 73 CC4 23 PHE A 347 ? PHE A 347 . ? 1_555 ? 74 CC4 23 ARG A 348 ? ARG A 348 . ? 1_555 ? 75 CC4 23 GLY A 350 ? GLY A 350 . ? 1_555 ? 76 CC4 23 HIS A 351 ? HIS A 351 . ? 1_555 ? 77 CC4 23 VAL A 354 ? VAL A 354 . ? 1_555 ? 78 CC4 23 PHE A 380 ? PHE A 380 . ? 1_555 ? 79 CC4 23 LEU A 417 ? LEU A 417 . ? 1_555 ? 80 CC4 23 ILE A 436 ? ILE A 436 . ? 1_555 ? 81 CC4 23 ARG A 440 ? ARG A 440 . ? 1_555 ? 82 CC4 23 IOD N . ? IOD A 608 . ? 1_555 ? 83 CC4 23 HOH Z . ? HOH A 649 . ? 1_555 ? 84 CC4 23 HOH Z . ? HOH A 721 . ? 1_555 ? 85 CC4 23 HOH Z . ? HOH A 890 . ? 1_555 ? 86 CC5 3 GLU A 118 ? GLU A 118 . ? 1_555 ? 87 CC5 3 LYS A 232 ? LYS A 232 . ? 1_555 ? 88 CC5 3 HOH Z . ? HOH A 734 . ? 1_555 ? # _database_PDB_matrix.entry_id 2PUM _database_PDB_matrix.origx[1][1] 1.000000 _database_PDB_matrix.origx[1][2] 0.000000 _database_PDB_matrix.origx[1][3] 0.000000 _database_PDB_matrix.origx[2][1] 0.000000 _database_PDB_matrix.origx[2][2] 1.000000 _database_PDB_matrix.origx[2][3] 0.000000 _database_PDB_matrix.origx[3][1] 0.000000 _database_PDB_matrix.origx[3][2] 0.000000 _database_PDB_matrix.origx[3][3] 1.000000 _database_PDB_matrix.origx_vector[1] 0.00000 _database_PDB_matrix.origx_vector[2] 0.00000 _database_PDB_matrix.origx_vector[3] 0.00000 # _atom_sites.entry_id 2PUM _atom_sites.fract_transf_matrix[1][1] 0.018375 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.004107 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.012424 _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] 0.013252 _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 I N O P 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 ? 5.512 -24.058 31.518 1.00 104.37 ? 1 SER A N 1 ATOM 2 C CA . SER A 1 1 ? 4.483 -24.835 30.940 1.00 104.31 ? 1 SER A CA 1 ATOM 3 C C . SER A 1 1 ? 4.306 -26.145 31.629 1.00 104.39 ? 1 SER A C 1 ATOM 4 O O . SER A 1 1 ? 5.148 -26.690 32.340 1.00 104.50 ? 1 SER A O 1 ATOM 5 C CB . SER A 1 1 ? 4.722 -25.077 29.451 1.00 104.23 ? 1 SER A CB 1 ATOM 6 O OG . SER A 1 1 ? 3.711 -25.903 28.914 1.00 103.93 ? 1 SER A OG 1 ATOM 7 N N . TRP A 1 2 ? 3.126 -26.597 31.322 1.00 104.25 ? 2 TRP A N 1 ATOM 8 C CA . TRP A 1 2 ? 2.637 -27.840 31.732 1.00 104.00 ? 2 TRP A CA 1 ATOM 9 C C . TRP A 1 2 ? 2.359 -28.035 33.303 1.00 103.32 ? 2 TRP A C 1 ATOM 10 O O . TRP A 1 2 ? 3.095 -28.751 33.988 1.00 103.26 ? 2 TRP A O 1 ATOM 11 C CB . TRP A 1 2 ? 3.577 -28.923 31.116 1.00 104.33 ? 2 TRP A CB 1 ATOM 12 C CG . TRP A 1 2 ? 2.832 -30.181 30.730 1.00 105.78 ? 2 TRP A CG 1 ATOM 13 C CD1 . TRP A 1 2 ? 2.181 -30.939 31.649 1.00 106.55 ? 2 TRP A CD1 1 ATOM 14 C CD2 . TRP A 1 2 ? 2.657 -30.823 29.450 1.00 107.61 ? 2 TRP A CD2 1 ATOM 15 N NE1 . TRP A 1 2 ? 1.573 -31.995 31.044 1.00 107.53 ? 2 TRP A NE1 1 ATOM 16 C CE2 . TRP A 1 2 ? 1.830 -31.939 29.698 1.00 108.05 ? 2 TRP A CE2 1 ATOM 17 C CE3 . TRP A 1 2 ? 3.067 -30.575 28.125 1.00 108.43 ? 2 TRP A CE3 1 ATOM 18 C CZ2 . TRP A 1 2 ? 1.400 -32.806 28.682 1.00 108.85 ? 2 TRP A CZ2 1 ATOM 19 C CZ3 . TRP A 1 2 ? 2.634 -31.443 27.111 1.00 108.90 ? 2 TRP A CZ3 1 ATOM 20 C CH2 . TRP A 1 2 ? 1.810 -32.541 27.402 1.00 109.19 ? 2 TRP A CH2 1 ATOM 21 N N . GLU A 1 3 ? 1.223 -27.436 33.784 1.00 102.42 ? 3 GLU A N 1 ATOM 22 C CA . GLU A 1 3 ? 0.422 -27.444 35.088 1.00 101.30 ? 3 GLU A CA 1 ATOM 23 C C . GLU A 1 3 ? -0.708 -26.708 34.469 1.00 100.12 ? 3 GLU A C 1 ATOM 24 O O . GLU A 1 3 ? -1.499 -25.892 34.975 1.00 100.21 ? 3 GLU A O 1 ATOM 25 C CB . GLU A 1 3 ? 0.967 -26.847 36.418 1.00 101.48 ? 3 GLU A CB 1 ATOM 26 C CG . GLU A 1 3 ? 0.262 -27.516 37.645 1.00 102.76 ? 3 GLU A CG 1 ATOM 27 C CD . GLU A 1 3 ? 0.881 -27.277 39.030 1.00 103.92 ? 3 GLU A CD 1 ATOM 28 O OE1 . GLU A 1 3 ? 1.073 -26.096 39.388 1.00 104.73 ? 3 GLU A OE1 1 ATOM 29 O OE2 . GLU A 1 3 ? 1.177 -28.268 39.745 1.00 103.67 ? 3 GLU A OE2 1 ATOM 30 N N . VAL A 1 4 ? -0.598 -27.189 33.259 1.00 98.41 ? 4 VAL A N 1 ATOM 31 C CA . VAL A 1 4 ? -1.158 -27.059 31.927 1.00 96.51 ? 4 VAL A CA 1 ATOM 32 C C . VAL A 1 4 ? -2.328 -26.188 31.604 1.00 95.21 ? 4 VAL A C 1 ATOM 33 O O . VAL A 1 4 ? -2.451 -25.673 30.498 1.00 95.01 ? 4 VAL A O 1 ATOM 34 C CB . VAL A 1 4 ? -1.386 -28.502 31.428 1.00 96.52 ? 4 VAL A CB 1 ATOM 35 C CG1 . VAL A 1 4 ? -0.489 -28.807 30.256 1.00 96.45 ? 4 VAL A CG1 1 ATOM 36 C CG2 . VAL A 1 4 ? -1.095 -29.492 32.569 1.00 96.51 ? 4 VAL A CG2 1 ATOM 37 N N . GLY A 1 5 ? -3.205 -26.053 32.562 1.00 93.78 ? 5 GLY A N 1 ATOM 38 C CA . GLY A 1 5 ? -4.358 -25.251 32.338 1.00 92.24 ? 5 GLY A CA 1 ATOM 39 C C . GLY A 1 5 ? -4.609 -24.398 33.542 1.00 91.20 ? 5 GLY A C 1 ATOM 40 O O . GLY A 1 5 ? -5.245 -24.836 34.500 1.00 91.70 ? 5 GLY A O 1 ATOM 41 N N . CYS A 1 6 ? -4.119 -23.184 33.527 1.00 89.67 ? 6 CYS A N 1 ATOM 42 C CA . CYS A 1 6 ? -4.424 -22.277 34.596 1.00 88.00 ? 6 CYS A CA 1 ATOM 43 C C . CYS A 1 6 ? -4.786 -21.001 33.947 1.00 88.27 ? 6 CYS A C 1 ATOM 44 O O . CYS A 1 6 ? -4.390 -20.738 32.822 1.00 88.37 ? 6 CYS A O 1 ATOM 45 C CB . CYS A 1 6 ? -3.269 -22.073 35.589 1.00 87.33 ? 6 CYS A CB 1 ATOM 46 S SG . CYS A 1 6 ? -3.750 -21.224 37.128 1.00 82.97 ? 6 CYS A SG 1 ATOM 47 N N . GLY A 1 7 ? -5.568 -20.201 34.665 1.00 88.19 ? 7 GLY A N 1 ATOM 48 C CA . GLY A 1 7 ? -5.800 -18.900 34.054 1.00 88.33 ? 7 GLY A CA 1 ATOM 49 C C . GLY A 1 7 ? -7.197 -18.393 33.856 1.00 88.22 ? 7 GLY A C 1 ATOM 50 O O . GLY A 1 7 ? -7.892 -18.743 32.909 1.00 88.35 ? 7 GLY A O 1 ATOM 51 N N . ALA A 1 8 ? -7.596 -17.557 34.781 1.00 87.93 ? 8 ALA A N 1 ATOM 52 C CA . ALA A 1 8 ? -8.950 -17.056 34.702 1.00 87.51 ? 8 ALA A CA 1 ATOM 53 C C . ALA A 1 8 ? -9.006 -15.766 33.880 1.00 87.09 ? 8 ALA A C 1 ATOM 54 O O . ALA A 1 8 ? -10.082 -15.347 33.452 1.00 87.29 ? 8 ALA A O 1 ATOM 55 C CB . ALA A 1 8 ? -9.503 -16.827 36.106 1.00 87.56 ? 8 ALA A CB 1 ATOM 56 N N . PRO A 1 9 ? -7.850 -15.158 33.666 1.00 86.37 ? 9 PRO A N 1 ATOM 57 C CA . PRO A 1 9 ? -7.773 -13.857 32.935 1.00 85.78 ? 9 PRO A CA 1 ATOM 58 C C . PRO A 1 9 ? -8.475 -13.793 31.690 1.00 85.15 ? 9 PRO A C 1 ATOM 59 O O . PRO A 1 9 ? -9.180 -12.857 31.300 1.00 85.10 ? 9 PRO A O 1 ATOM 60 C CB . PRO A 1 9 ? -6.303 -13.586 32.877 1.00 85.75 ? 9 PRO A CB 1 ATOM 61 C CG . PRO A 1 9 ? -5.855 -14.047 34.228 1.00 86.28 ? 9 PRO A CG 1 ATOM 62 C CD . PRO A 1 9 ? -6.802 -15.107 34.704 1.00 86.51 ? 9 PRO A CD 1 ATOM 63 N N . VAL A 1 10 ? -8.258 -14.856 31.149 1.00 84.20 ? 10 VAL A N 1 ATOM 64 C CA . VAL A 1 10 ? -8.695 -15.049 29.890 1.00 83.23 ? 10 VAL A CA 1 ATOM 65 C C . VAL A 1 10 ? -10.139 -14.665 29.532 1.00 82.36 ? 10 VAL A C 1 ATOM 66 O O . VAL A 1 10 ? -11.092 -15.208 30.086 1.00 82.45 ? 10 VAL A O 1 ATOM 67 C CB . VAL A 1 10 ? -8.481 -16.530 29.557 1.00 83.42 ? 10 VAL A CB 1 ATOM 68 C CG1 . VAL A 1 10 ? -7.299 -17.087 30.332 1.00 83.54 ? 10 VAL A CG1 1 ATOM 69 C CG2 . VAL A 1 10 ? -9.752 -17.320 29.846 1.00 83.27 ? 10 VAL A CG2 1 ATOM 70 N N . PRO A 1 11 ? -10.306 -13.712 28.590 1.00 81.36 ? 11 PRO A N 1 ATOM 71 C CA . PRO A 1 11 ? -11.629 -13.533 27.979 1.00 80.54 ? 11 PRO A CA 1 ATOM 72 C C . PRO A 1 11 ? -12.094 -14.850 27.386 1.00 79.60 ? 11 PRO A C 1 ATOM 73 O O . PRO A 1 11 ? -11.274 -15.562 26.824 1.00 79.46 ? 11 PRO A O 1 ATOM 74 C CB . PRO A 1 11 ? -11.425 -12.356 27.038 1.00 80.63 ? 11 PRO A CB 1 ATOM 75 C CG . PRO A 1 11 ? -10.518 -11.496 27.861 1.00 80.90 ? 11 PRO A CG 1 ATOM 76 C CD . PRO A 1 11 ? -9.792 -12.373 28.851 1.00 81.32 ? 11 PRO A CD 1 ATOM 77 N N . LEU A 1 12 ? -13.374 -15.222 27.463 1.00 78.29 ? 12 LEU A N 1 ATOM 78 C CA . LEU A 1 12 ? -13.773 -16.522 26.899 1.00 77.01 ? 12 LEU A CA 1 ATOM 79 C C . LEU A 1 12 ? -14.784 -16.508 25.721 1.00 75.60 ? 12 LEU A C 1 ATOM 80 O O . LEU A 1 12 ? -15.969 -16.209 25.914 1.00 74.89 ? 12 LEU A O 1 ATOM 81 C CB . LEU A 1 12 ? -14.243 -17.460 28.023 1.00 77.41 ? 12 LEU A CB 1 ATOM 82 C CG . LEU A 1 12 ? -14.123 -18.973 27.800 1.00 77.90 ? 12 LEU A CG 1 ATOM 83 C CD1 . LEU A 1 12 ? -12.812 -19.339 27.099 1.00 78.68 ? 12 LEU A CD1 1 ATOM 84 C CD2 . LEU A 1 12 ? -14.257 -19.718 29.128 1.00 78.59 ? 12 LEU A CD2 1 ATOM 85 N N . VAL A 1 13 ? -14.291 -16.858 24.518 1.00 73.95 ? 13 VAL A N 1 ATOM 86 C CA . VAL A 1 13 ? -15.098 -16.924 23.281 1.00 72.17 ? 13 VAL A CA 1 ATOM 87 C C . VAL A 1 13 ? -14.578 -17.836 22.130 1.00 70.54 ? 13 VAL A C 1 ATOM 88 O O . VAL A 1 13 ? -13.472 -18.383 22.168 1.00 70.49 ? 13 VAL A O 1 ATOM 89 C CB . VAL A 1 13 ? -15.363 -15.543 22.696 1.00 72.28 ? 13 VAL A CB 1 ATOM 90 C CG1 . VAL A 1 13 ? -16.651 -14.968 23.271 1.00 72.73 ? 13 VAL A CG1 1 ATOM 91 C CG2 . VAL A 1 13 ? -14.171 -14.626 22.949 1.00 72.93 ? 13 VAL A CG2 1 ATOM 92 N N . LYS A 1 14 ? -15.409 -17.902 21.091 1.00 68.14 ? 14 LYS A N 1 ATOM 93 C CA . LYS A 1 14 ? -15.344 -18.829 19.957 1.00 65.52 ? 14 LYS A CA 1 ATOM 94 C C . LYS A 1 14 ? -14.673 -18.429 18.604 1.00 63.28 ? 14 LYS A C 1 ATOM 95 O O . LYS A 1 14 ? -14.690 -17.261 18.188 1.00 63.16 ? 14 LYS A O 1 ATOM 96 C CB . LYS A 1 14 ? -16.793 -19.192 19.673 1.00 65.81 ? 14 LYS A CB 1 ATOM 97 C CG . LYS A 1 14 ? -16.974 -20.259 18.655 1.00 67.28 ? 14 LYS A CG 1 ATOM 98 C CD . LYS A 1 14 ? -17.405 -21.543 19.318 1.00 70.06 ? 14 LYS A CD 1 ATOM 99 C CE . LYS A 1 14 ? -18.201 -22.395 18.361 1.00 70.69 ? 14 LYS A CE 1 ATOM 100 N NZ . LYS A 1 14 ? -17.689 -23.781 18.360 1.00 71.54 ? 14 LYS A NZ 1 ATOM 101 N N . CYS A 1 15 ? -14.149 -19.441 17.904 1.00 60.18 ? 15 CYS A N 1 ATOM 102 C CA . CYS A 1 15 ? -13.444 -19.285 16.623 1.00 57.19 ? 15 CYS A CA 1 ATOM 103 C C . CYS A 1 15 ? -14.275 -19.581 15.361 1.00 57.98 ? 15 CYS A C 1 ATOM 104 O O . CYS A 1 15 ? -15.012 -20.565 15.318 1.00 58.17 ? 15 CYS A O 1 ATOM 105 C CB . CYS A 1 15 ? -12.223 -20.210 16.604 1.00 55.59 ? 15 CYS A CB 1 ATOM 106 S SG . CYS A 1 15 ? -11.079 -19.978 17.981 1.00 46.07 ? 15 CYS A SG 1 ATOM 107 N N . ASP A 1 16 ? -14.127 -18.755 14.322 1.00 58.24 ? 16 ASP A N 1 ATOM 108 C CA . ASP A 1 16 ? -14.827 -18.981 13.053 1.00 58.62 ? 16 ASP A CA 1 ATOM 109 C C . ASP A 1 16 ? -14.098 -19.985 12.171 1.00 58.63 ? 16 ASP A C 1 ATOM 110 O O . ASP A 1 16 ? -14.732 -20.807 11.508 1.00 58.87 ? 16 ASP A O 1 ATOM 111 C CB . ASP A 1 16 ? -15.012 -17.688 12.288 1.00 58.98 ? 16 ASP A CB 1 ATOM 112 C CG . ASP A 1 16 ? -15.616 -17.908 10.920 1.00 60.46 ? 16 ASP A CG 1 ATOM 113 O OD1 . ASP A 1 16 ? -15.321 -18.950 10.276 1.00 61.73 ? 16 ASP A OD1 1 ATOM 114 O OD2 . ASP A 1 16 ? -16.400 -17.075 10.414 1.00 62.92 ? 16 ASP A OD2 1 ATOM 115 N N . GLU A 1 17 ? -12.770 -19.907 12.144 1.00 58.51 ? 17 GLU A N 1 ATOM 116 C CA . GLU A 1 17 ? -11.953 -20.878 11.387 1.00 58.34 ? 17 GLU A CA 1 ATOM 117 C C . GLU A 1 17 ? -12.020 -20.697 9.886 1.00 57.63 ? 17 GLU A C 1 ATOM 118 O O . GLU A 1 17 ? -11.359 -21.420 9.125 1.00 58.70 ? 17 GLU A O 1 ATOM 119 C CB . GLU A 1 17 ? -12.353 -22.318 11.711 1.00 58.52 ? 17 GLU A CB 1 ATOM 120 C CG . GLU A 1 17 ? -11.369 -23.088 12.566 1.00 60.29 ? 17 GLU A CG 1 ATOM 121 C CD . GLU A 1 17 ? -12.105 -23.893 13.603 1.00 62.85 ? 17 GLU A CD 1 ATOM 122 O OE1 . GLU A 1 17 ? -12.473 -25.058 13.325 1.00 64.74 ? 17 GLU A OE1 1 ATOM 123 O OE2 . GLU A 1 17 ? -12.356 -23.332 14.686 1.00 64.21 ? 17 GLU A OE2 1 ATOM 124 N N . ASN A 1 18 ? -12.840 -19.761 9.446 1.00 55.87 ? 18 ASN A N 1 ATOM 125 C CA . ASN A 1 18 ? -12.884 -19.454 8.036 1.00 54.40 ? 18 ASN A CA 1 ATOM 126 C C . ASN A 1 18 ? -12.992 -17.959 7.851 1.00 52.34 ? 18 ASN A C 1 ATOM 127 O O . ASN A 1 18 ? -13.222 -17.475 6.756 1.00 52.64 ? 18 ASN A O 1 ATOM 128 C CB . ASN A 1 18 ? -14.004 -20.223 7.334 1.00 55.48 ? 18 ASN A CB 1 ATOM 129 C CG . ASN A 1 18 ? -13.589 -21.654 6.982 1.00 57.67 ? 18 ASN A CG 1 ATOM 130 O OD1 . ASN A 1 18 ? -13.903 -22.614 7.711 1.00 60.00 ? 18 ASN A OD1 1 ATOM 131 N ND2 . ASN A 1 18 ? -12.863 -21.800 5.866 1.00 59.68 ? 18 ASN A ND2 1 ATOM 132 N N . SER A 1 19 ? -12.827 -17.229 8.948 1.00 49.47 ? 19 SER A N 1 ATOM 133 C CA . SER A 1 19 ? -12.817 -15.786 8.907 1.00 46.21 ? 19 SER A CA 1 ATOM 134 C C . SER A 1 19 ? -11.520 -15.329 8.274 1.00 43.69 ? 19 SER A C 1 ATOM 135 O O . SER A 1 19 ? -10.445 -15.831 8.582 1.00 43.90 ? 19 SER A O 1 ATOM 136 C CB . SER A 1 19 ? -12.893 -15.219 10.318 1.00 46.32 ? 19 SER A CB 1 ATOM 137 O OG . SER A 1 19 ? -12.937 -13.802 10.284 1.00 48.03 ? 19 SER A OG 1 ATOM 138 N N . PRO A 1 20 ? -11.617 -14.386 7.361 1.00 41.06 ? 20 PRO A N 1 ATOM 139 C CA . PRO A 1 20 ? -10.428 -13.782 6.765 1.00 38.77 ? 20 PRO A CA 1 ATOM 140 C C . PRO A 1 20 ? -9.777 -12.714 7.691 1.00 36.70 ? 20 PRO A C 1 ATOM 141 O O . PRO A 1 20 ? -8.838 -12.013 7.257 1.00 36.97 ? 20 PRO A O 1 ATOM 142 C CB . PRO A 1 20 ? -10.988 -13.096 5.527 1.00 38.88 ? 20 PRO A CB 1 ATOM 143 C CG . PRO A 1 20 ? -12.423 -13.559 5.441 1.00 40.22 ? 20 PRO A CG 1 ATOM 144 C CD . PRO A 1 20 ? -12.864 -13.845 6.811 1.00 40.60 ? 20 PRO A CD 1 ATOM 145 N N . TYR A 1 21 ? -10.242 -12.593 8.934 1.00 32.96 ? 21 TYR A N 1 ATOM 146 C CA . TYR A 1 21 ? -9.748 -11.544 9.799 1.00 30.29 ? 21 TYR A CA 1 ATOM 147 C C . TYR A 1 21 ? -9.258 -12.012 11.193 1.00 28.75 ? 21 TYR A C 1 ATOM 148 O O . TYR A 1 21 ? -9.806 -12.960 11.787 1.00 28.02 ? 21 TYR A O 1 ATOM 149 C CB . TYR A 1 21 ? -10.815 -10.477 9.914 1.00 30.08 ? 21 TYR A CB 1 ATOM 150 C CG . TYR A 1 21 ? -11.324 -9.964 8.584 1.00 31.65 ? 21 TYR A CG 1 ATOM 151 C CD1 . TYR A 1 21 ? -10.456 -9.470 7.612 1.00 31.79 ? 21 TYR A CD1 1 ATOM 152 C CD2 . TYR A 1 21 ? -12.687 -9.942 8.302 1.00 33.65 ? 21 TYR A CD2 1 ATOM 153 C CE1 . TYR A 1 21 ? -10.936 -8.984 6.405 1.00 32.05 ? 21 TYR A CE1 1 ATOM 154 C CE2 . TYR A 1 21 ? -13.184 -9.452 7.088 1.00 32.84 ? 21 TYR A CE2 1 ATOM 155 C CZ . TYR A 1 21 ? -12.308 -8.976 6.143 1.00 33.42 ? 21 TYR A CZ 1 ATOM 156 O OH . TYR A 1 21 ? -12.796 -8.496 4.937 1.00 31.10 ? 21 TYR A OH 1 ATOM 157 N N . ARG A 1 22 ? -8.215 -11.359 11.709 1.00 26.42 ? 22 ARG A N 1 ATOM 158 C CA . ARG A 1 22 ? -7.647 -11.754 12.999 1.00 24.41 ? 22 ARG A CA 1 ATOM 159 C C . ARG A 1 22 ? -8.667 -11.404 14.019 1.00 23.35 ? 22 ARG A C 1 ATOM 160 O O . ARG A 1 22 ? -9.433 -10.502 13.787 1.00 23.78 ? 22 ARG A O 1 ATOM 161 C CB . ARG A 1 22 ? -6.436 -10.922 13.356 1.00 23.76 ? 22 ARG A CB 1 ATOM 162 C CG . ARG A 1 22 ? -5.255 -10.949 12.443 1.00 23.73 ? 22 ARG A CG 1 ATOM 163 C CD . ARG A 1 22 ? -4.182 -9.972 12.914 1.00 21.66 ? 22 ARG A CD 1 ATOM 164 N NE . ARG A 1 22 ? -2.998 -9.898 12.067 1.00 20.82 ? 22 ARG A NE 1 ATOM 165 C CZ . ARG A 1 22 ? -1.984 -10.745 12.121 1.00 21.23 ? 22 ARG A CZ 1 ATOM 166 N NH1 . ARG A 1 22 ? -1.989 -11.767 12.962 1.00 22.97 ? 22 ARG A NH1 1 ATOM 167 N NH2 . ARG A 1 22 ? -0.956 -10.583 11.323 1.00 22.36 ? 22 ARG A NH2 1 ATOM 168 N N . THR A 1 23 ? -8.710 -12.103 15.140 1.00 22.48 ? 23 THR A N 1 ATOM 169 C CA . THR A 1 23 ? -9.536 -11.610 16.245 1.00 22.35 ? 23 THR A CA 1 ATOM 170 C C . THR A 1 23 ? -8.876 -10.343 16.831 1.00 22.26 ? 23 THR A C 1 ATOM 171 O O . THR A 1 23 ? -7.767 -9.968 16.469 1.00 22.14 ? 23 THR A O 1 ATOM 172 C CB . THR A 1 23 ? -9.661 -12.633 17.382 1.00 22.08 ? 23 THR A CB 1 ATOM 173 O OG1 . THR A 1 23 ? -8.382 -13.221 17.619 1.00 23.11 ? 23 THR A OG1 1 ATOM 174 C CG2 . THR A 1 23 ? -10.508 -13.822 16.973 1.00 22.16 ? 23 THR A CG2 1 ATOM 175 N N . ILE A 1 24 ? -9.559 -9.688 17.756 1.00 22.00 ? 24 ILE A N 1 ATOM 176 C CA . ILE A 1 24 ? -8.996 -8.533 18.424 1.00 20.88 ? 24 ILE A CA 1 ATOM 177 C C . ILE A 1 24 ? -8.018 -9.020 19.492 1.00 20.77 ? 24 ILE A C 1 ATOM 178 O O . ILE A 1 24 ? -7.004 -8.384 19.783 1.00 19.73 ? 24 ILE A O 1 ATOM 179 C CB . ILE A 1 24 ? -10.124 -7.730 19.048 1.00 20.42 ? 24 ILE A CB 1 ATOM 180 C CG1 . ILE A 1 24 ? -10.693 -6.743 18.037 1.00 21.14 ? 24 ILE A CG1 1 ATOM 181 C CG2 . ILE A 1 24 ? -9.636 -6.993 20.237 1.00 20.97 ? 24 ILE A CG2 1 ATOM 182 C CD1 . ILE A 1 24 ? -9.655 -5.970 17.232 1.00 19.49 ? 24 ILE A CD1 1 ATOM 183 N N . THR A 1 25 ? -8.315 -10.192 20.037 1.00 20.98 ? 25 THR A N 1 ATOM 184 C CA . THR A 1 25 ? -7.566 -10.700 21.167 1.00 21.47 ? 25 THR A CA 1 ATOM 185 C C . THR A 1 25 ? -6.385 -11.547 20.781 1.00 21.50 ? 25 THR A C 1 ATOM 186 O O . THR A 1 25 ? -5.467 -11.706 21.567 1.00 21.97 ? 25 THR A O 1 ATOM 187 C CB . THR A 1 25 ? -8.468 -11.510 22.077 1.00 21.44 ? 25 THR A CB 1 ATOM 188 O OG1 . THR A 1 25 ? -8.883 -12.693 21.394 1.00 21.52 ? 25 THR A OG1 1 ATOM 189 C CG2 . THR A 1 25 ? -9.744 -10.765 22.328 1.00 21.57 ? 25 THR A CG2 1 ATOM 190 N N . GLY A 1 26 ? -6.388 -12.071 19.571 1.00 21.82 ? 26 GLY A N 1 ATOM 191 C CA . GLY A 1 26 ? -5.285 -12.892 19.137 1.00 22.62 ? 26 GLY A CA 1 ATOM 192 C C . GLY A 1 26 ? -5.688 -14.338 19.112 1.00 23.39 ? 26 GLY A C 1 ATOM 193 O O . GLY A 1 26 ? -5.067 -15.179 18.466 1.00 25.22 ? 26 GLY A O 1 ATOM 194 N N . ASP A 1 27 ? -6.733 -14.644 19.845 1.00 23.64 ? 27 ASP A N 1 ATOM 195 C CA . ASP A 1 27 ? -7.326 -15.966 19.794 1.00 23.33 ? 27 ASP A CA 1 ATOM 196 C C . ASP A 1 27 ? -7.607 -16.391 18.371 1.00 23.37 ? 27 ASP A C 1 ATOM 197 O O . ASP A 1 27 ? -7.905 -15.558 17.521 1.00 22.26 ? 27 ASP A O 1 ATOM 198 C CB . ASP A 1 27 ? -8.648 -15.914 20.546 1.00 23.23 ? 27 ASP A CB 1 ATOM 199 C CG . ASP A 1 27 ? -8.443 -15.857 22.003 1.00 21.79 ? 27 ASP A CG 1 ATOM 200 O OD1 . ASP A 1 27 ? -7.797 -16.763 22.521 1.00 23.04 ? 27 ASP A OD1 1 ATOM 201 O OD2 . ASP A 1 27 ? -8.832 -14.942 22.721 1.00 22.78 ? 27 ASP A OD2 1 ATOM 202 N N . CYS A 1 28 ? -7.509 -17.698 18.142 1.00 24.07 ? 28 CYS A N 1 ATOM 203 C CA . CYS A 1 28 ? -7.873 -18.326 16.880 1.00 25.19 ? 28 CYS A CA 1 ATOM 204 C C . CYS A 1 28 ? -6.895 -18.171 15.761 1.00 25.05 ? 28 CYS A C 1 ATOM 205 O O . CYS A 1 28 ? -7.243 -18.450 14.644 1.00 25.86 ? 28 CYS A O 1 ATOM 206 C CB . CYS A 1 28 ? -9.256 -17.864 16.413 1.00 25.60 ? 28 CYS A CB 1 ATOM 207 S SG . CYS A 1 28 ? -10.513 -18.047 17.690 1.00 29.34 ? 28 CYS A SG 1 ATOM 208 N N . ASN A 1 29 ? -5.690 -17.688 16.063 1.00 25.57 ? 29 ASN A N 1 ATOM 209 C CA . ASN A 1 29 ? -4.681 -17.576 15.013 1.00 25.72 ? 29 ASN A CA 1 ATOM 210 C C . ASN A 1 29 ? -4.216 -18.993 14.705 1.00 26.55 ? 29 ASN A C 1 ATOM 211 O O . ASN A 1 29 ? -4.111 -19.375 13.531 1.00 26.56 ? 29 ASN A O 1 ATOM 212 C CB . ASN A 1 29 ? -3.479 -16.756 15.465 1.00 25.28 ? 29 ASN A CB 1 ATOM 213 C CG . ASN A 1 29 ? -2.471 -16.498 14.355 1.00 24.47 ? 29 ASN A CG 1 ATOM 214 O OD1 . ASN A 1 29 ? -1.766 -17.394 13.894 1.00 22.09 ? 29 ASN A OD1 1 ATOM 215 N ND2 . ASN A 1 29 ? -2.394 -15.252 13.913 1.00 25.27 ? 29 ASN A ND2 1 ATOM 216 N N . ASN A 1 30 ? -3.927 -19.741 15.800 1.00 27.72 ? 30 ASN A N 1 ATOM 217 C CA . ASN A 1 30 ? -3.479 -21.139 15.802 1.00 28.46 ? 30 ASN A CA 1 ATOM 218 C C . ASN A 1 30 ? -4.673 -22.074 15.983 1.00 29.22 ? 30 ASN A C 1 ATOM 219 O O . ASN A 1 30 ? -5.469 -21.943 16.902 1.00 28.74 ? 30 ASN A O 1 ATOM 220 C CB . ASN A 1 30 ? -2.474 -21.396 16.898 1.00 27.84 ? 30 ASN A CB 1 ATOM 221 C CG . ASN A 1 30 ? -1.764 -22.707 16.635 1.00 27.71 ? 30 ASN A CG 1 ATOM 222 O OD1 . ASN A 1 30 ? -2.397 -23.771 16.549 1.00 29.44 ? 30 ASN A OD1 1 ATOM 223 N ND2 . ASN A 1 30 ? -0.440 -22.632 16.508 1.00 26.29 ? 30 ASN A ND2 1 ATOM 224 N N . ARG A 1 31 ? -4.744 -22.993 15.072 1.00 30.53 ? 31 ARG A N 1 ATOM 225 C CA . ARG A 1 31 ? -5.900 -23.864 14.983 1.00 32.09 ? 31 ARG A CA 1 ATOM 226 C C . ARG A 1 31 ? -5.908 -24.985 15.988 1.00 32.44 ? 31 ARG A C 1 ATOM 227 O O . ARG A 1 31 ? -6.960 -25.254 16.572 1.00 32.99 ? 31 ARG A O 1 ATOM 228 C CB . ARG A 1 31 ? -5.994 -24.456 13.580 1.00 32.33 ? 31 ARG A CB 1 ATOM 229 C CG . ARG A 1 31 ? -6.575 -23.463 12.605 1.00 32.54 ? 31 ARG A CG 1 ATOM 230 C CD . ARG A 1 31 ? -6.641 -24.011 11.200 1.00 36.70 ? 31 ARG A CD 1 ATOM 231 N NE . ARG A 1 31 ? -7.355 -23.058 10.358 1.00 40.18 ? 31 ARG A NE 1 ATOM 232 C CZ . ARG A 1 31 ? -7.127 -22.850 9.075 1.00 40.70 ? 31 ARG A CZ 1 ATOM 233 N NH1 . ARG A 1 31 ? -6.173 -23.520 8.427 1.00 43.69 ? 31 ARG A NH1 1 ATOM 234 N NH2 . ARG A 1 31 ? -7.851 -21.951 8.435 1.00 40.21 ? 31 ARG A NH2 1 ATOM 235 N N . ARG A 1 32 ? -4.787 -25.608 16.227 1.00 32.69 ? 32 ARG A N 1 ATOM 236 C CA . ARG A 1 32 ? -4.971 -26.665 17.180 1.00 34.22 ? 32 ARG A CA 1 ATOM 237 C C . ARG A 1 32 ? -4.781 -26.119 18.608 1.00 33.56 ? 32 ARG A C 1 ATOM 238 O O . ARG A 1 32 ? -5.128 -26.802 19.569 1.00 34.25 ? 32 ARG A O 1 ATOM 239 C CB . ARG A 1 32 ? -4.062 -27.880 16.931 1.00 35.39 ? 32 ARG A CB 1 ATOM 240 C CG . ARG A 1 32 ? -2.626 -27.578 16.571 1.00 39.31 ? 32 ARG A CG 1 ATOM 241 C CD . ARG A 1 32 ? -2.030 -28.719 15.765 1.00 47.52 ? 32 ARG A CD 1 ATOM 242 N NE . ARG A 1 32 ? -1.798 -29.912 16.575 1.00 52.20 ? 32 ARG A NE 1 ATOM 243 C CZ . ARG A 1 32 ? -0.790 -30.001 17.446 1.00 56.58 ? 32 ARG A CZ 1 ATOM 244 N NH1 . ARG A 1 32 ? 0.030 -28.959 17.616 1.00 58.64 ? 32 ARG A NH1 1 ATOM 245 N NH2 . ARG A 1 32 ? -0.593 -31.124 18.143 1.00 57.34 ? 32 ARG A NH2 1 ATOM 246 N N . SER A 1 33 ? -4.249 -24.918 18.742 1.00 32.97 ? 33 SER A N 1 ATOM 247 C CA . SER A 1 33 ? -3.993 -24.350 20.049 1.00 32.17 ? 33 SER A CA 1 ATOM 248 C C . SER A 1 33 ? -4.420 -22.873 19.973 1.00 31.39 ? 33 SER A C 1 ATOM 249 O O . SER A 1 33 ? -3.588 -21.974 19.889 1.00 31.94 ? 33 SER A O 1 ATOM 250 C CB . SER A 1 33 ? -2.515 -24.515 20.374 1.00 32.09 ? 33 SER A CB 1 ATOM 251 O OG . SER A 1 33 ? -2.228 -24.073 21.691 1.00 34.41 ? 33 SER A OG 1 ATOM 252 N N . PRO A 1 34 ? -5.716 -22.667 20.005 1.00 30.31 ? 34 PRO A N 1 ATOM 253 C CA . PRO A 1 34 ? -6.313 -21.367 19.681 1.00 29.45 ? 34 PRO A CA 1 ATOM 254 C C . PRO A 1 34 ? -5.951 -20.173 20.549 1.00 28.48 ? 34 PRO A C 1 ATOM 255 O O . PRO A 1 34 ? -6.235 -19.069 20.136 1.00 29.65 ? 34 PRO A O 1 ATOM 256 C CB . PRO A 1 34 ? -7.814 -21.642 19.806 1.00 29.57 ? 34 PRO A CB 1 ATOM 257 C CG . PRO A 1 34 ? -7.946 -23.130 19.790 1.00 29.41 ? 34 PRO A CG 1 ATOM 258 C CD . PRO A 1 34 ? -6.711 -23.674 20.388 1.00 30.25 ? 34 PRO A CD 1 ATOM 259 N N . ALA A 1 35 ? -5.382 -20.369 21.722 1.00 27.23 ? 35 ALA A N 1 ATOM 260 C CA . ALA A 1 35 ? -5.049 -19.263 22.610 1.00 25.42 ? 35 ALA A CA 1 ATOM 261 C C . ALA A 1 35 ? -3.564 -18.815 22.497 1.00 24.79 ? 35 ALA A C 1 ATOM 262 O O . ALA A 1 35 ? -3.152 -17.770 23.032 1.00 23.98 ? 35 ALA A O 1 ATOM 263 C CB . ALA A 1 35 ? -5.397 -19.651 24.030 1.00 25.48 ? 35 ALA A CB 1 ATOM 264 N N . LEU A 1 36 ? -2.762 -19.607 21.795 1.00 24.00 ? 36 LEU A N 1 ATOM 265 C CA . LEU A 1 36 ? -1.346 -19.303 21.599 1.00 23.40 ? 36 LEU A CA 1 ATOM 266 C C . LEU A 1 36 ? -1.173 -17.962 20.901 1.00 23.03 ? 36 LEU A C 1 ATOM 267 O O . LEU A 1 36 ? -1.568 -17.811 19.759 1.00 23.18 ? 36 LEU A O 1 ATOM 268 C CB . LEU A 1 36 ? -0.695 -20.392 20.755 1.00 23.31 ? 36 LEU A CB 1 ATOM 269 C CG . LEU A 1 36 ? 0.643 -20.938 21.248 1.00 23.35 ? 36 LEU A CG 1 ATOM 270 C CD1 . LEU A 1 36 ? 0.535 -21.325 22.696 1.00 21.88 ? 36 LEU A CD1 1 ATOM 271 C CD2 . LEU A 1 36 ? 1.050 -22.138 20.444 1.00 25.96 ? 36 LEU A CD2 1 ATOM 272 N N . GLY A 1 37 ? -0.589 -16.984 21.587 1.00 22.61 ? 37 GLY A N 1 ATOM 273 C CA . GLY A 1 37 ? -0.402 -15.663 21.014 1.00 21.68 ? 37 GLY A CA 1 ATOM 274 C C . GLY A 1 37 ? -1.459 -14.619 21.373 1.00 21.33 ? 37 GLY A C 1 ATOM 275 O O . GLY A 1 37 ? -1.347 -13.464 20.988 1.00 21.53 ? 37 GLY A O 1 ATOM 276 N N . ALA A 1 38 ? -2.484 -15.019 22.120 1.00 21.15 ? 38 ALA A N 1 ATOM 277 C CA . ALA A 1 38 ? -3.548 -14.116 22.574 1.00 20.09 ? 38 ALA A CA 1 ATOM 278 C C . ALA A 1 38 ? -3.085 -13.155 23.644 1.00 19.97 ? 38 ALA A C 1 ATOM 279 O O . ALA A 1 38 ? -2.124 -13.393 24.345 1.00 19.55 ? 38 ALA A O 1 ATOM 280 C CB . ALA A 1 38 ? -4.723 -14.905 23.101 1.00 19.71 ? 38 ALA A CB 1 ATOM 281 N N . ALA A 1 39 ? -3.797 -12.056 23.774 1.00 20.59 ? 39 ALA A N 1 ATOM 282 C CA . ALA A 1 39 ? -3.498 -11.099 24.813 1.00 20.88 ? 39 ALA A CA 1 ATOM 283 C C . ALA A 1 39 ? -4.004 -11.659 26.139 1.00 21.29 ? 39 ALA A C 1 ATOM 284 O O . ALA A 1 39 ? -4.707 -12.652 26.143 1.00 21.66 ? 39 ALA A O 1 ATOM 285 C CB . ALA A 1 39 ? -4.174 -9.841 24.507 1.00 21.06 ? 39 ALA A CB 1 ATOM 286 N N . ASN A 1 40 ? -3.641 -11.024 27.254 1.00 21.43 ? 40 ASN A N 1 ATOM 287 C CA . ASN A 1 40 ? -4.037 -11.459 28.585 1.00 21.49 ? 40 ASN A CA 1 ATOM 288 C C . ASN A 1 40 ? -3.646 -12.863 28.986 1.00 21.28 ? 40 ASN A C 1 ATOM 289 O O . ASN A 1 40 ? -4.400 -13.570 29.677 1.00 21.36 ? 40 ASN A O 1 ATOM 290 C CB . ASN A 1 40 ? -5.506 -11.235 28.799 1.00 21.72 ? 40 ASN A CB 1 ATOM 291 C CG . ASN A 1 40 ? -5.829 -9.797 28.835 1.00 25.29 ? 40 ASN A CG 1 ATOM 292 O OD1 . ASN A 1 40 ? -5.371 -9.068 29.734 1.00 29.82 ? 40 ASN A OD1 1 ATOM 293 N ND2 . ASN A 1 40 ? -6.587 -9.337 27.832 1.00 27.41 ? 40 ASN A ND2 1 ATOM 294 N N . ARG A 1 41 ? -2.452 -13.268 28.576 1.00 20.55 ? 41 ARG A N 1 ATOM 295 C CA . ARG A 1 41 ? -1.917 -14.540 29.014 1.00 19.84 ? 41 ARG A CA 1 ATOM 296 C C . ARG A 1 41 ? -0.456 -14.384 29.341 1.00 19.34 ? 41 ARG A C 1 ATOM 297 O O . ARG A 1 41 ? 0.173 -13.332 29.097 1.00 19.42 ? 41 ARG A O 1 ATOM 298 C CB . ARG A 1 41 ? -2.159 -15.622 27.979 1.00 20.50 ? 41 ARG A CB 1 ATOM 299 C CG . ARG A 1 41 ? -3.585 -16.101 28.038 1.00 23.22 ? 41 ARG A CG 1 ATOM 300 C CD . ARG A 1 41 ? -4.003 -16.961 26.916 1.00 29.00 ? 41 ARG A CD 1 ATOM 301 N NE . ARG A 1 41 ? -5.427 -17.234 27.016 1.00 35.21 ? 41 ARG A NE 1 ATOM 302 C CZ . ARG A 1 41 ? -5.930 -18.383 27.427 1.00 37.98 ? 41 ARG A CZ 1 ATOM 303 N NH1 . ARG A 1 41 ? -5.111 -19.372 27.778 1.00 40.37 ? 41 ARG A NH1 1 ATOM 304 N NH2 . ARG A 1 41 ? -7.249 -18.550 27.470 1.00 39.07 ? 41 ARG A NH2 1 ATOM 305 N N . ALA A 1 42 ? 0.106 -15.428 29.910 1.00 18.03 ? 42 ALA A N 1 ATOM 306 C CA . ALA A 1 42 ? 1.485 -15.349 30.326 1.00 16.96 ? 42 ALA A CA 1 ATOM 307 C C . ALA A 1 42 ? 2.475 -15.106 29.199 1.00 16.70 ? 42 ALA A C 1 ATOM 308 O O . ALA A 1 42 ? 2.348 -15.635 28.105 1.00 17.18 ? 42 ALA A O 1 ATOM 309 C CB . ALA A 1 42 ? 1.846 -16.602 31.045 1.00 16.47 ? 42 ALA A CB 1 ATOM 310 N N . LEU A 1 43 ? 3.486 -14.309 29.495 1.00 16.17 ? 43 LEU A N 1 ATOM 311 C CA . LEU A 1 43 ? 4.625 -14.174 28.618 1.00 15.06 ? 43 LEU A CA 1 ATOM 312 C C . LEU A 1 43 ? 5.225 -15.561 28.594 1.00 15.54 ? 43 LEU A C 1 ATOM 313 O O . LEU A 1 43 ? 5.141 -16.275 29.591 1.00 16.96 ? 43 LEU A O 1 ATOM 314 C CB . LEU A 1 43 ? 5.591 -13.193 29.251 1.00 14.39 ? 43 LEU A CB 1 ATOM 315 C CG . LEU A 1 43 ? 5.143 -11.730 29.225 1.00 11.82 ? 43 LEU A CG 1 ATOM 316 C CD1 . LEU A 1 43 ? 5.845 -10.914 30.268 1.00 6.98 ? 43 LEU A CD1 1 ATOM 317 C CD2 . LEU A 1 43 ? 5.406 -11.168 27.813 1.00 9.85 ? 43 LEU A CD2 1 ATOM 318 N N . ALA A 1 44 ? 5.800 -15.980 27.479 1.00 15.45 ? 44 ALA A N 1 ATOM 319 C CA . ALA A 1 44 ? 6.420 -17.304 27.414 1.00 15.41 ? 44 ALA A CA 1 ATOM 320 C C . ALA A 1 44 ? 7.749 -17.335 28.213 1.00 15.20 ? 44 ALA A C 1 ATOM 321 O O . ALA A 1 44 ? 8.336 -16.303 28.475 1.00 14.54 ? 44 ALA A O 1 ATOM 322 C CB . ALA A 1 44 ? 6.661 -17.703 25.975 1.00 15.50 ? 44 ALA A CB 1 ATOM 323 N N . ARG A 1 45 ? 8.205 -18.518 28.609 1.00 15.13 ? 45 ARG A N 1 ATOM 324 C CA . ARG A 1 45 ? 9.439 -18.627 29.364 1.00 15.07 ? 45 ARG A CA 1 ATOM 325 C C . ARG A 1 45 ? 10.393 -19.446 28.592 1.00 14.93 ? 45 ARG A C 1 ATOM 326 O O . ARG A 1 45 ? 10.264 -20.662 28.608 1.00 16.13 ? 45 ARG A O 1 ATOM 327 C CB . ARG A 1 45 ? 9.226 -19.351 30.684 1.00 14.84 ? 45 ARG A CB 1 ATOM 328 C CG . ARG A 1 45 ? 8.711 -18.492 31.814 1.00 14.33 ? 45 ARG A CG 1 ATOM 329 C CD . ARG A 1 45 ? 9.732 -17.657 32.521 1.00 14.95 ? 45 ARG A CD 1 ATOM 330 N NE . ARG A 1 45 ? 9.039 -16.895 33.578 1.00 18.48 ? 45 ARG A NE 1 ATOM 331 C CZ . ARG A 1 45 ? 9.565 -15.890 34.276 1.00 15.30 ? 45 ARG A CZ 1 ATOM 332 N NH1 . ARG A 1 45 ? 10.805 -15.494 34.053 1.00 15.28 ? 45 ARG A NH1 1 ATOM 333 N NH2 . ARG A 1 45 ? 8.848 -15.298 35.207 1.00 13.50 ? 45 ARG A NH2 1 ATOM 334 N N . TRP A 1 46 ? 11.342 -18.801 27.926 1.00 14.49 ? 46 TRP A N 1 ATOM 335 C CA . TRP A 1 46 ? 12.355 -19.530 27.202 1.00 14.54 ? 46 TRP A CA 1 ATOM 336 C C . TRP A 1 46 ? 13.278 -20.317 28.167 1.00 15.71 ? 46 TRP A C 1 ATOM 337 O O . TRP A 1 46 ? 13.853 -21.344 27.788 1.00 16.10 ? 46 TRP A O 1 ATOM 338 C CB . TRP A 1 46 ? 13.156 -18.604 26.284 1.00 14.25 ? 46 TRP A CB 1 ATOM 339 C CG . TRP A 1 46 ? 12.378 -18.161 25.070 1.00 12.29 ? 46 TRP A CG 1 ATOM 340 C CD1 . TRP A 1 46 ? 11.160 -18.589 24.714 1.00 11.50 ? 46 TRP A CD1 1 ATOM 341 C CD2 . TRP A 1 46 ? 12.760 -17.183 24.118 1.00 11.68 ? 46 TRP A CD2 1 ATOM 342 N NE1 . TRP A 1 46 ? 10.732 -17.936 23.592 1.00 14.15 ? 46 TRP A NE1 1 ATOM 343 C CE2 . TRP A 1 46 ? 11.708 -17.059 23.203 1.00 14.92 ? 46 TRP A CE2 1 ATOM 344 C CE3 . TRP A 1 46 ? 13.882 -16.365 23.960 1.00 15.97 ? 46 TRP A CE3 1 ATOM 345 C CZ2 . TRP A 1 46 ? 11.759 -16.191 22.091 1.00 15.77 ? 46 TRP A CZ2 1 ATOM 346 C CZ3 . TRP A 1 46 ? 13.947 -15.498 22.872 1.00 16.93 ? 46 TRP A CZ3 1 ATOM 347 C CH2 . TRP A 1 46 ? 12.884 -15.419 21.944 1.00 17.01 ? 46 TRP A CH2 1 ATOM 348 N N . LEU A 1 47 ? 13.429 -19.822 29.399 1.00 16.11 ? 47 LEU A N 1 ATOM 349 C CA . LEU A 1 47 ? 14.182 -20.521 30.440 1.00 16.34 ? 47 LEU A CA 1 ATOM 350 C C . LEU A 1 47 ? 13.419 -20.367 31.739 1.00 16.52 ? 47 LEU A C 1 ATOM 351 O O . LEU A 1 47 ? 12.565 -19.513 31.869 1.00 17.53 ? 47 LEU A O 1 ATOM 352 C CB . LEU A 1 47 ? 15.574 -19.960 30.625 1.00 16.15 ? 47 LEU A CB 1 ATOM 353 C CG . LEU A 1 47 ? 16.680 -20.052 29.603 1.00 15.48 ? 47 LEU A CG 1 ATOM 354 C CD1 . LEU A 1 47 ? 17.793 -19.075 30.123 1.00 16.50 ? 47 LEU A CD1 1 ATOM 355 C CD2 . LEU A 1 47 ? 17.155 -21.455 29.507 1.00 13.25 ? 47 LEU A CD2 1 ATOM 356 N N . PRO A 1 48 ? 13.688 -21.218 32.697 1.00 16.47 ? 48 PRO A N 1 ATOM 357 C CA . PRO A 1 48 ? 12.939 -21.167 33.960 1.00 16.19 ? 48 PRO A CA 1 ATOM 358 C C . PRO A 1 48 ? 13.217 -19.907 34.751 1.00 15.80 ? 48 PRO A C 1 ATOM 359 O O . PRO A 1 48 ? 14.335 -19.405 34.820 1.00 14.85 ? 48 PRO A O 1 ATOM 360 C CB . PRO A 1 48 ? 13.424 -22.411 34.709 1.00 16.10 ? 48 PRO A CB 1 ATOM 361 C CG . PRO A 1 48 ? 13.972 -23.326 33.565 1.00 16.17 ? 48 PRO A CG 1 ATOM 362 C CD . PRO A 1 48 ? 14.631 -22.344 32.618 1.00 16.57 ? 48 PRO A CD 1 ATOM 363 N N . ALA A 1 49 ? 12.158 -19.373 35.319 1.00 15.70 ? 49 ALA A N 1 ATOM 364 C CA . ALA A 1 49 ? 12.298 -18.203 36.149 1.00 16.14 ? 49 ALA A CA 1 ATOM 365 C C . ALA A 1 49 ? 13.320 -18.412 37.270 1.00 16.39 ? 49 ALA A C 1 ATOM 366 O O . ALA A 1 49 ? 13.495 -19.487 37.779 1.00 16.49 ? 49 ALA A O 1 ATOM 367 C CB . ALA A 1 49 ? 10.949 -17.808 36.721 1.00 15.26 ? 49 ALA A CB 1 ATOM 368 N N . GLU A 1 50 ? 14.017 -17.358 37.638 1.00 17.53 ? 50 GLU A N 1 ATOM 369 C CA . GLU A 1 50 ? 14.929 -17.443 38.748 1.00 18.58 ? 50 GLU A CA 1 ATOM 370 C C . GLU A 1 50 ? 14.530 -16.432 39.758 1.00 19.22 ? 50 GLU A C 1 ATOM 371 O O . GLU A 1 50 ? 14.755 -15.237 39.557 1.00 20.42 ? 50 GLU A O 1 ATOM 372 C CB . GLU A 1 50 ? 16.356 -17.214 38.298 1.00 19.17 ? 50 GLU A CB 1 ATOM 373 C CG . GLU A 1 50 ? 16.850 -18.359 37.419 1.00 20.21 ? 50 GLU A CG 1 ATOM 374 C CD . GLU A 1 50 ? 18.328 -18.273 37.162 1.00 22.40 ? 50 GLU A CD 1 ATOM 375 O OE1 . GLU A 1 50 ? 19.013 -17.537 37.903 1.00 25.79 ? 50 GLU A OE1 1 ATOM 376 O OE2 . GLU A 1 50 ? 18.809 -18.935 36.227 1.00 26.45 ? 50 GLU A OE2 1 ATOM 377 N N . TYR A 1 51 ? 13.906 -16.926 40.832 1.00 19.56 ? 51 TYR A N 1 ATOM 378 C CA . TYR A 1 51 ? 13.370 -16.122 41.922 1.00 19.18 ? 51 TYR A CA 1 ATOM 379 C C . TYR A 1 51 ? 14.131 -16.453 43.190 1.00 19.85 ? 51 TYR A C 1 ATOM 380 O O . TYR A 1 51 ? 14.635 -17.554 43.320 1.00 20.10 ? 51 TYR A O 1 ATOM 381 C CB . TYR A 1 51 ? 11.902 -16.462 42.103 1.00 18.95 ? 51 TYR A CB 1 ATOM 382 C CG . TYR A 1 51 ? 10.968 -15.805 41.106 1.00 17.14 ? 51 TYR A CG 1 ATOM 383 C CD1 . TYR A 1 51 ? 10.871 -14.428 41.029 1.00 16.03 ? 51 TYR A CD1 1 ATOM 384 C CD2 . TYR A 1 51 ? 10.167 -16.560 40.255 1.00 14.70 ? 51 TYR A CD2 1 ATOM 385 C CE1 . TYR A 1 51 ? 10.017 -13.823 40.123 1.00 14.38 ? 51 TYR A CE1 1 ATOM 386 C CE2 . TYR A 1 51 ? 9.306 -15.947 39.351 1.00 12.29 ? 51 TYR A CE2 1 ATOM 387 C CZ . TYR A 1 51 ? 9.245 -14.591 39.299 1.00 13.14 ? 51 TYR A CZ 1 ATOM 388 O OH . TYR A 1 51 ? 8.418 -13.966 38.407 1.00 17.86 ? 51 TYR A OH 1 ATOM 389 N N . GLU A 1 52 ? 14.213 -15.500 44.123 1.00 20.56 ? 52 GLU A N 1 ATOM 390 C CA . GLU A 1 52 ? 14.950 -15.653 45.399 1.00 21.11 ? 52 GLU A CA 1 ATOM 391 C C . GLU A 1 52 ? 14.514 -16.914 46.162 1.00 21.94 ? 52 GLU A C 1 ATOM 392 O O . GLU A 1 52 ? 15.345 -17.642 46.711 1.00 21.99 ? 52 GLU A O 1 ATOM 393 C CB . GLU A 1 52 ? 14.752 -14.395 46.260 1.00 20.68 ? 52 GLU A CB 1 ATOM 394 C CG . GLU A 1 52 ? 15.543 -14.259 47.553 1.00 21.99 ? 52 GLU A CG 1 ATOM 395 C CD . GLU A 1 52 ? 15.200 -12.968 48.338 1.00 24.06 ? 52 GLU A CD 1 ATOM 396 O OE1 . GLU A 1 52 ? 14.141 -12.902 49.003 1.00 20.94 ? 52 GLU A OE1 1 ATOM 397 O OE2 . GLU A 1 52 ? 16.004 -11.991 48.308 1.00 24.70 ? 52 GLU A OE2 1 ATOM 398 N N . ASP A 1 53 ? 13.208 -17.165 46.193 1.00 22.44 ? 53 ASP A N 1 ATOM 399 C CA . ASP A 1 53 ? 12.698 -18.313 46.890 1.00 23.54 ? 53 ASP A CA 1 ATOM 400 C C . ASP A 1 53 ? 12.217 -19.344 45.888 1.00 24.39 ? 53 ASP A C 1 ATOM 401 O O . ASP A 1 53 ? 11.394 -20.218 46.198 1.00 24.63 ? 53 ASP A O 1 ATOM 402 C CB . ASP A 1 53 ? 11.612 -17.928 47.884 1.00 23.35 ? 53 ASP A CB 1 ATOM 403 C CG . ASP A 1 53 ? 10.339 -17.444 47.213 1.00 25.44 ? 53 ASP A CG 1 ATOM 404 O OD1 . ASP A 1 53 ? 10.315 -17.289 45.973 1.00 25.20 ? 53 ASP A OD1 1 ATOM 405 O OD2 . ASP A 1 53 ? 9.292 -17.210 47.866 1.00 27.59 ? 53 ASP A OD2 1 ATOM 406 N N . GLY A 1 54 ? 12.756 -19.235 44.678 1.00 24.90 ? 54 GLY A N 1 ATOM 407 C CA . GLY A 1 54 ? 12.443 -20.172 43.615 1.00 25.16 ? 54 GLY A CA 1 ATOM 408 C C . GLY A 1 54 ? 11.052 -20.106 43.015 1.00 25.47 ? 54 GLY A C 1 ATOM 409 O O . GLY A 1 54 ? 10.853 -20.715 41.973 1.00 26.28 ? 54 GLY A O 1 ATOM 410 N N . LEU A 1 55 ? 10.116 -19.375 43.639 1.00 25.38 ? 55 LEU A N 1 ATOM 411 C CA . LEU A 1 55 ? 8.701 -19.311 43.215 1.00 24.65 ? 55 LEU A CA 1 ATOM 412 C C . LEU A 1 55 ? 8.173 -17.967 42.768 1.00 24.26 ? 55 LEU A C 1 ATOM 413 O O . LEU A 1 55 ? 7.481 -17.871 41.747 1.00 24.47 ? 55 LEU A O 1 ATOM 414 C CB . LEU A 1 55 ? 7.837 -19.694 44.385 1.00 24.97 ? 55 LEU A CB 1 ATOM 415 C CG . LEU A 1 55 ? 7.156 -21.052 44.478 1.00 25.97 ? 55 LEU A CG 1 ATOM 416 C CD1 . LEU A 1 55 ? 7.604 -22.056 43.424 1.00 22.81 ? 55 LEU A CD1 1 ATOM 417 C CD2 . LEU A 1 55 ? 7.366 -21.528 45.914 1.00 25.54 ? 55 LEU A CD2 1 ATOM 418 N N . ALA A 1 56 ? 8.466 -16.928 43.541 1.00 23.61 ? 56 ALA A N 1 ATOM 419 C CA . ALA A 1 56 ? 7.922 -15.633 43.227 1.00 23.68 ? 56 ALA A CA 1 ATOM 420 C C . ALA A 1 56 ? 8.638 -14.401 43.835 1.00 24.52 ? 56 ALA A C 1 ATOM 421 O O . ALA A 1 56 ? 8.435 -13.270 43.371 1.00 23.91 ? 56 ALA A O 1 ATOM 422 C CB . ALA A 1 56 ? 6.472 -15.629 43.567 1.00 22.94 ? 56 ALA A CB 1 ATOM 423 N N . LEU A 1 57 ? 9.459 -14.595 44.863 1.00 25.54 ? 57 LEU A N 1 ATOM 424 C CA . LEU A 1 57 ? 10.123 -13.449 45.485 1.00 26.60 ? 57 LEU A CA 1 ATOM 425 C C . LEU A 1 57 ? 11.332 -13.074 44.648 1.00 27.56 ? 57 LEU A C 1 ATOM 426 O O . LEU A 1 57 ? 12.144 -13.927 44.265 1.00 27.95 ? 57 LEU A O 1 ATOM 427 C CB . LEU A 1 57 ? 10.545 -13.726 46.933 1.00 27.04 ? 57 LEU A CB 1 ATOM 428 C CG . LEU A 1 57 ? 9.731 -13.345 48.198 1.00 26.30 ? 57 LEU A CG 1 ATOM 429 C CD1 . LEU A 1 57 ? 8.697 -12.232 47.976 1.00 23.81 ? 57 LEU A CD1 1 ATOM 430 C CD2 . LEU A 1 57 ? 9.052 -14.553 48.718 1.00 27.31 ? 57 LEU A CD2 1 ATOM 431 N N . PRO A 1 58 ? 11.449 -11.795 44.336 1.00 27.90 ? 58 PRO A N 1 ATOM 432 C CA . PRO A 1 58 ? 12.519 -11.338 43.447 1.00 28.15 ? 58 PRO A CA 1 ATOM 433 C C . PRO A 1 58 ? 13.826 -11.296 44.196 1.00 28.41 ? 58 PRO A C 1 ATOM 434 O O . PRO A 1 58 ? 13.790 -11.265 45.419 1.00 29.35 ? 58 PRO A O 1 ATOM 435 C CB . PRO A 1 58 ? 12.091 -9.909 43.087 1.00 27.73 ? 58 PRO A CB 1 ATOM 436 C CG . PRO A 1 58 ? 10.736 -9.759 43.639 1.00 27.77 ? 58 PRO A CG 1 ATOM 437 C CD . PRO A 1 58 ? 10.575 -10.705 44.780 1.00 27.59 ? 58 PRO A CD 1 ATOM 438 N N . PHE A 1 59 ? 14.946 -11.274 43.483 1.00 28.52 ? 59 PHE A N 1 ATOM 439 C CA . PHE A 1 59 ? 16.254 -11.095 44.099 1.00 28.45 ? 59 PHE A CA 1 ATOM 440 C C . PHE A 1 59 ? 16.398 -9.649 44.530 1.00 29.29 ? 59 PHE A C 1 ATOM 441 O O . PHE A 1 59 ? 16.011 -8.752 43.796 1.00 29.66 ? 59 PHE A O 1 ATOM 442 C CB . PHE A 1 59 ? 17.322 -11.466 43.108 1.00 27.75 ? 59 PHE A CB 1 ATOM 443 C CG . PHE A 1 59 ? 17.582 -12.913 43.063 1.00 25.86 ? 59 PHE A CG 1 ATOM 444 C CD1 . PHE A 1 59 ? 17.066 -13.692 42.060 1.00 24.57 ? 59 PHE A CD1 1 ATOM 445 C CD2 . PHE A 1 59 ? 18.343 -13.513 44.039 1.00 25.45 ? 59 PHE A CD2 1 ATOM 446 C CE1 . PHE A 1 59 ? 17.321 -15.065 42.038 1.00 24.68 ? 59 PHE A CE1 1 ATOM 447 C CE2 . PHE A 1 59 ? 18.600 -14.887 44.006 1.00 24.56 ? 59 PHE A CE2 1 ATOM 448 C CZ . PHE A 1 59 ? 18.100 -15.649 42.999 1.00 21.57 ? 59 PHE A CZ 1 ATOM 449 N N . GLY A 1 60 ? 16.937 -9.428 45.726 1.00 30.15 ? 60 GLY A N 1 ATOM 450 C CA . GLY A 1 60 ? 17.021 -8.098 46.306 1.00 31.22 ? 60 GLY A CA 1 ATOM 451 C C . GLY A 1 60 ? 15.915 -7.876 47.337 1.00 32.38 ? 60 GLY A C 1 ATOM 452 O O . GLY A 1 60 ? 15.941 -6.913 48.101 1.00 32.80 ? 60 GLY A O 1 ATOM 453 N N . TRP A 1 61 ? 14.945 -8.787 47.374 1.00 33.41 ? 61 TRP A N 1 ATOM 454 C CA . TRP A 1 61 ? 13.807 -8.684 48.276 1.00 33.70 ? 61 TRP A CA 1 ATOM 455 C C . TRP A 1 61 ? 14.260 -8.909 49.686 1.00 34.82 ? 61 TRP A C 1 ATOM 456 O O . TRP A 1 61 ? 14.168 -8.024 50.497 1.00 35.10 ? 61 TRP A O 1 ATOM 457 C CB . TRP A 1 61 ? 12.739 -9.711 47.897 1.00 33.27 ? 61 TRP A CB 1 ATOM 458 C CG . TRP A 1 61 ? 11.465 -9.616 48.691 1.00 31.16 ? 61 TRP A CG 1 ATOM 459 C CD1 . TRP A 1 61 ? 11.195 -10.243 49.849 1.00 27.56 ? 61 TRP A CD1 1 ATOM 460 C CD2 . TRP A 1 61 ? 10.290 -8.852 48.365 1.00 29.45 ? 61 TRP A CD2 1 ATOM 461 N NE1 . TRP A 1 61 ? 9.935 -9.918 50.284 1.00 28.77 ? 61 TRP A NE1 1 ATOM 462 C CE2 . TRP A 1 61 ? 9.353 -9.070 49.386 1.00 27.75 ? 61 TRP A CE2 1 ATOM 463 C CE3 . TRP A 1 61 ? 9.943 -8.009 47.318 1.00 28.86 ? 61 TRP A CE3 1 ATOM 464 C CZ2 . TRP A 1 61 ? 8.096 -8.495 49.393 1.00 27.35 ? 61 TRP A CZ2 1 ATOM 465 C CZ3 . TRP A 1 61 ? 8.670 -7.435 47.323 1.00 31.39 ? 61 TRP A CZ3 1 ATOM 466 C CH2 . TRP A 1 61 ? 7.768 -7.687 48.359 1.00 29.66 ? 61 TRP A CH2 1 ATOM 467 N N . THR A 1 62 ? 14.746 -10.106 49.984 1.00 36.91 ? 62 THR A N 1 ATOM 468 C CA . THR A 1 62 ? 15.179 -10.414 51.340 1.00 38.47 ? 62 THR A CA 1 ATOM 469 C C . THR A 1 62 ? 16.610 -9.974 51.455 1.00 40.95 ? 62 THR A C 1 ATOM 470 O O . THR A 1 62 ? 17.483 -10.441 50.733 1.00 41.92 ? 62 THR A O 1 ATOM 471 C CB . THR A 1 62 ? 15.053 -11.874 51.614 1.00 38.09 ? 62 THR A CB 1 ATOM 472 O OG1 . THR A 1 62 ? 13.689 -12.273 51.404 1.00 35.71 ? 62 THR A OG1 1 ATOM 473 C CG2 . THR A 1 62 ? 15.365 -12.143 53.078 1.00 37.17 ? 62 THR A CG2 1 ATOM 474 N N . GLN A 1 63 ? 16.859 -9.084 52.392 1.00 43.45 ? 63 GLN A N 1 ATOM 475 C CA . GLN A 1 63 ? 18.122 -8.382 52.425 1.00 45.52 ? 63 GLN A CA 1 ATOM 476 C C . GLN A 1 63 ? 19.358 -9.288 52.641 1.00 45.61 ? 63 GLN A C 1 ATOM 477 O O . GLN A 1 63 ? 20.460 -8.967 52.204 1.00 46.26 ? 63 GLN A O 1 ATOM 478 C CB . GLN A 1 63 ? 17.999 -7.232 53.430 1.00 46.36 ? 63 GLN A CB 1 ATOM 479 C CG . GLN A 1 63 ? 16.563 -6.595 53.466 1.00 50.93 ? 63 GLN A CG 1 ATOM 480 C CD . GLN A 1 63 ? 16.310 -5.574 52.348 1.00 55.82 ? 63 GLN A CD 1 ATOM 481 O OE1 . GLN A 1 63 ? 17.151 -5.398 51.451 1.00 57.57 ? 63 GLN A OE1 1 ATOM 482 N NE2 . GLN A 1 63 ? 15.159 -4.889 52.414 1.00 58.19 ? 63 GLN A NE2 1 ATOM 483 N N . ARG A 1 64 ? 19.174 -10.448 53.250 1.00 44.96 ? 64 ARG A N 1 ATOM 484 C CA . ARG A 1 64 ? 20.320 -11.297 53.504 1.00 44.68 ? 64 ARG A CA 1 ATOM 485 C C . ARG A 1 64 ? 20.425 -12.543 52.619 1.00 43.41 ? 64 ARG A C 1 ATOM 486 O O . ARG A 1 64 ? 21.333 -13.339 52.794 1.00 43.56 ? 64 ARG A O 1 ATOM 487 C CB . ARG A 1 64 ? 20.335 -11.695 54.972 1.00 45.65 ? 64 ARG A CB 1 ATOM 488 C CG . ARG A 1 64 ? 18.962 -12.109 55.503 1.00 48.90 ? 64 ARG A CG 1 ATOM 489 C CD . ARG A 1 64 ? 18.389 -13.341 54.836 1.00 53.96 ? 64 ARG A CD 1 ATOM 490 N NE . ARG A 1 64 ? 18.468 -14.536 55.672 1.00 59.55 ? 64 ARG A NE 1 ATOM 491 C CZ . ARG A 1 64 ? 17.407 -15.145 56.196 1.00 61.46 ? 64 ARG A CZ 1 ATOM 492 N NH1 . ARG A 1 64 ? 16.190 -14.665 55.970 1.00 63.03 ? 64 ARG A NH1 1 ATOM 493 N NH2 . ARG A 1 64 ? 17.560 -16.231 56.944 1.00 62.37 ? 64 ARG A NH2 1 ATOM 494 N N . LYS A 1 65 ? 19.489 -12.737 51.697 1.00 41.54 ? 65 LYS A N 1 ATOM 495 C CA . LYS A 1 65 ? 19.584 -13.847 50.752 1.00 39.26 ? 65 LYS A CA 1 ATOM 496 C C . LYS A 1 65 ? 20.448 -13.355 49.594 1.00 37.08 ? 65 LYS A C 1 ATOM 497 O O . LYS A 1 65 ? 20.180 -12.322 49.018 1.00 37.77 ? 65 LYS A O 1 ATOM 498 C CB . LYS A 1 65 ? 18.194 -14.236 50.210 1.00 39.81 ? 65 LYS A CB 1 ATOM 499 C CG . LYS A 1 65 ? 17.232 -14.936 51.176 1.00 41.14 ? 65 LYS A CG 1 ATOM 500 C CD . LYS A 1 65 ? 17.601 -16.416 51.412 1.00 44.97 ? 65 LYS A CD 1 ATOM 501 C CE . LYS A 1 65 ? 16.375 -17.322 51.755 1.00 47.74 ? 65 LYS A CE 1 ATOM 502 N NZ . LYS A 1 65 ? 15.282 -17.431 50.679 1.00 48.30 ? 65 LYS A NZ 1 ATOM 503 N N . THR A 1 66 ? 21.486 -14.071 49.232 1.00 34.36 ? 66 THR A N 1 ATOM 504 C CA . THR A 1 66 ? 22.300 -13.609 48.122 1.00 31.89 ? 66 THR A CA 1 ATOM 505 C C . THR A 1 66 ? 21.906 -14.280 46.828 1.00 30.35 ? 66 THR A C 1 ATOM 506 O O . THR A 1 66 ? 21.075 -15.169 46.811 1.00 30.32 ? 66 THR A O 1 ATOM 507 C CB . THR A 1 66 ? 23.772 -13.940 48.332 1.00 32.22 ? 66 THR A CB 1 ATOM 508 O OG1 . THR A 1 66 ? 23.954 -15.352 48.138 1.00 30.27 ? 66 THR A OG1 1 ATOM 509 C CG2 . THR A 1 66 ? 24.202 -13.636 49.774 1.00 31.54 ? 66 THR A CG2 1 ATOM 510 N N . ARG A 1 67 ? 22.510 -13.835 45.728 1.00 27.94 ? 67 ARG A N 1 ATOM 511 C CA . ARG A 1 67 ? 22.341 -14.523 44.467 1.00 25.16 ? 67 ARG A CA 1 ATOM 512 C C . ARG A 1 67 ? 23.719 -15.046 44.185 1.00 23.79 ? 67 ARG A C 1 ATOM 513 O O . ARG A 1 67 ? 24.659 -14.282 44.089 1.00 23.34 ? 67 ARG A O 1 ATOM 514 C CB . ARG A 1 67 ? 21.912 -13.542 43.393 1.00 25.37 ? 67 ARG A CB 1 ATOM 515 C CG . ARG A 1 67 ? 21.694 -14.172 42.049 1.00 25.01 ? 67 ARG A CG 1 ATOM 516 C CD . ARG A 1 67 ? 21.272 -13.224 40.955 1.00 22.69 ? 67 ARG A CD 1 ATOM 517 N NE . ARG A 1 67 ? 20.454 -13.965 40.014 1.00 24.17 ? 67 ARG A NE 1 ATOM 518 C CZ . ARG A 1 67 ? 19.692 -13.427 39.094 1.00 24.14 ? 67 ARG A CZ 1 ATOM 519 N NH1 . ARG A 1 67 ? 19.657 -12.128 38.955 1.00 26.58 ? 67 ARG A NH1 1 ATOM 520 N NH2 . ARG A 1 67 ? 18.979 -14.190 38.289 1.00 24.18 ? 67 ARG A NH2 1 ATOM 521 N N . ASN A 1 68 ? 23.879 -16.354 44.124 1.00 22.11 ? 68 ASN A N 1 ATOM 522 C CA . ASN A 1 68 ? 25.211 -16.902 43.884 1.00 21.21 ? 68 ASN A CA 1 ATOM 523 C C . ASN A 1 68 ? 26.307 -16.534 44.915 1.00 20.67 ? 68 ASN A C 1 ATOM 524 O O . ASN A 1 68 ? 27.486 -16.573 44.606 1.00 20.47 ? 68 ASN A O 1 ATOM 525 C CB . ASN A 1 68 ? 25.707 -16.503 42.496 1.00 20.80 ? 68 ASN A CB 1 ATOM 526 C CG . ASN A 1 68 ? 24.838 -17.035 41.393 1.00 21.39 ? 68 ASN A CG 1 ATOM 527 O OD1 . ASN A 1 68 ? 24.498 -18.215 41.382 1.00 21.96 ? 68 ASN A OD1 1 ATOM 528 N ND2 . ASN A 1 68 ? 24.494 -16.168 40.422 1.00 21.16 ? 68 ASN A ND2 1 ATOM 529 N N . GLY A 1 69 ? 25.938 -16.181 46.126 1.00 20.10 ? 69 GLY A N 1 ATOM 530 C CA . GLY A 1 69 ? 26.948 -15.840 47.097 1.00 20.96 ? 69 GLY A CA 1 ATOM 531 C C . GLY A 1 69 ? 27.099 -14.339 47.320 1.00 21.51 ? 69 GLY A C 1 ATOM 532 O O . GLY A 1 69 ? 27.726 -13.904 48.278 1.00 21.47 ? 69 GLY A O 1 ATOM 533 N N . PHE A 1 70 ? 26.548 -13.531 46.427 1.00 21.73 ? 70 PHE A N 1 ATOM 534 C CA . PHE A 1 70 ? 26.665 -12.090 46.601 1.00 21.69 ? 70 PHE A CA 1 ATOM 535 C C . PHE A 1 70 ? 25.305 -11.370 46.599 1.00 22.79 ? 70 PHE A C 1 ATOM 536 O O . PHE A 1 70 ? 24.252 -11.875 46.109 1.00 21.89 ? 70 PHE A O 1 ATOM 537 C CB . PHE A 1 70 ? 27.606 -11.452 45.569 1.00 20.34 ? 70 PHE A CB 1 ATOM 538 C CG . PHE A 1 70 ? 28.920 -12.155 45.428 1.00 21.52 ? 70 PHE A CG 1 ATOM 539 C CD1 . PHE A 1 70 ? 29.137 -13.072 44.369 1.00 20.24 ? 70 PHE A CD1 1 ATOM 540 C CD2 . PHE A 1 70 ? 29.948 -11.927 46.332 1.00 19.87 ? 70 PHE A CD2 1 ATOM 541 C CE1 . PHE A 1 70 ? 30.319 -13.712 44.225 1.00 15.95 ? 70 PHE A CE1 1 ATOM 542 C CE2 . PHE A 1 70 ? 31.156 -12.605 46.197 1.00 17.17 ? 70 PHE A CE2 1 ATOM 543 C CZ . PHE A 1 70 ? 31.328 -13.500 45.146 1.00 17.24 ? 70 PHE A CZ 1 ATOM 544 N N . ARG A 1 71 ? 25.369 -10.190 47.207 1.00 23.81 ? 71 ARG A N 1 ATOM 545 C CA . ARG A 1 71 ? 24.295 -9.240 47.278 1.00 25.14 ? 71 ARG A CA 1 ATOM 546 C C . ARG A 1 71 ? 24.113 -8.647 45.912 1.00 24.60 ? 71 ARG A C 1 ATOM 547 O O . ARG A 1 71 ? 25.089 -8.229 45.295 1.00 24.65 ? 71 ARG A O 1 ATOM 548 C CB . ARG A 1 71 ? 24.744 -8.124 48.216 1.00 26.48 ? 71 ARG A CB 1 ATOM 549 C CG . ARG A 1 71 ? 24.227 -8.236 49.639 1.00 31.08 ? 71 ARG A CG 1 ATOM 550 C CD . ARG A 1 71 ? 25.128 -7.625 50.714 1.00 39.76 ? 71 ARG A CD 1 ATOM 551 N NE . ARG A 1 71 ? 24.315 -7.200 51.856 1.00 47.82 ? 71 ARG A NE 1 ATOM 552 C CZ . ARG A 1 71 ? 23.289 -7.901 52.359 1.00 50.84 ? 71 ARG A CZ 1 ATOM 553 N NH1 . ARG A 1 71 ? 22.960 -9.092 51.840 1.00 52.79 ? 71 ARG A NH1 1 ATOM 554 N NH2 . ARG A 1 71 ? 22.602 -7.417 53.395 1.00 51.19 ? 71 ARG A NH2 1 ATOM 555 N N . VAL A 1 72 ? 22.888 -8.613 45.407 1.00 24.44 ? 72 VAL A N 1 ATOM 556 C CA . VAL A 1 72 ? 22.685 -7.926 44.138 1.00 24.39 ? 72 VAL A CA 1 ATOM 557 C C . VAL A 1 72 ? 22.762 -6.437 44.442 1.00 24.15 ? 72 VAL A C 1 ATOM 558 O O . VAL A 1 72 ? 22.234 -5.983 45.462 1.00 25.43 ? 72 VAL A O 1 ATOM 559 C CB . VAL A 1 72 ? 21.316 -8.212 43.540 1.00 24.32 ? 72 VAL A CB 1 ATOM 560 C CG1 . VAL A 1 72 ? 21.310 -9.581 42.874 1.00 24.95 ? 72 VAL A CG1 1 ATOM 561 C CG2 . VAL A 1 72 ? 20.270 -8.125 44.595 1.00 24.63 ? 72 VAL A CG2 1 ATOM 562 N N . PRO A 1 73 ? 23.438 -5.675 43.603 1.00 23.06 ? 73 PRO A N 1 ATOM 563 C CA . PRO A 1 73 ? 23.522 -4.227 43.801 1.00 22.02 ? 73 PRO A CA 1 ATOM 564 C C . PRO A 1 73 ? 22.188 -3.543 43.555 1.00 21.46 ? 73 PRO A C 1 ATOM 565 O O . PRO A 1 73 ? 21.367 -4.024 42.779 1.00 21.18 ? 73 PRO A O 1 ATOM 566 C CB . PRO A 1 73 ? 24.543 -3.802 42.749 1.00 22.07 ? 73 PRO A CB 1 ATOM 567 C CG . PRO A 1 73 ? 24.428 -4.859 41.697 1.00 22.50 ? 73 PRO A CG 1 ATOM 568 C CD . PRO A 1 73 ? 24.237 -6.129 42.455 1.00 23.18 ? 73 PRO A CD 1 ATOM 569 N N . LEU A 1 74 ? 21.985 -2.420 44.233 1.00 20.97 ? 74 LEU A N 1 ATOM 570 C CA . LEU A 1 74 ? 20.771 -1.609 44.136 1.00 19.98 ? 74 LEU A CA 1 ATOM 571 C C . LEU A 1 74 ? 20.518 -1.190 42.704 1.00 19.45 ? 74 LEU A C 1 ATOM 572 O O . LEU A 1 74 ? 21.432 -0.882 41.985 1.00 19.31 ? 74 LEU A O 1 ATOM 573 C CB . LEU A 1 74 ? 20.909 -0.373 45.053 1.00 19.83 ? 74 LEU A CB 1 ATOM 574 C CG . LEU A 1 74 ? 20.202 -0.192 46.434 1.00 19.80 ? 74 LEU A CG 1 ATOM 575 C CD1 . LEU A 1 74 ? 19.674 -1.457 47.095 1.00 19.70 ? 74 LEU A CD1 1 ATOM 576 C CD2 . LEU A 1 74 ? 21.037 0.554 47.411 1.00 17.08 ? 74 LEU A CD2 1 ATOM 577 N N . ALA A 1 75 ? 19.265 -1.197 42.282 1.00 19.59 ? 75 ALA A N 1 ATOM 578 C CA . ALA A 1 75 ? 18.918 -0.772 40.943 1.00 19.49 ? 75 ALA A CA 1 ATOM 579 C C . ALA A 1 75 ? 19.480 0.617 40.664 1.00 19.54 ? 75 ALA A C 1 ATOM 580 O O . ALA A 1 75 ? 20.240 0.833 39.752 1.00 19.29 ? 75 ALA A O 1 ATOM 581 C CB . ALA A 1 75 ? 17.454 -0.752 40.823 1.00 19.99 ? 75 ALA A CB 1 ATOM 582 N N . ARG A 1 76 ? 19.121 1.554 41.498 1.00 20.00 ? 76 ARG A N 1 ATOM 583 C CA . ARG A 1 76 ? 19.562 2.933 41.334 1.00 21.19 ? 76 ARG A CA 1 ATOM 584 C C . ARG A 1 76 ? 21.090 3.185 41.460 1.00 21.05 ? 76 ARG A C 1 ATOM 585 O O . ARG A 1 76 ? 21.632 4.154 40.868 1.00 20.44 ? 76 ARG A O 1 ATOM 586 C CB . ARG A 1 76 ? 18.770 3.834 42.297 1.00 21.03 ? 76 ARG A CB 1 ATOM 587 C CG . ARG A 1 76 ? 19.226 5.295 42.333 1.00 22.98 ? 76 ARG A CG 1 ATOM 588 C CD . ARG A 1 76 ? 18.768 6.176 41.182 1.00 22.78 ? 76 ARG A CD 1 ATOM 589 N NE . ARG A 1 76 ? 19.192 7.537 41.450 1.00 22.29 ? 76 ARG A NE 1 ATOM 590 C CZ . ARG A 1 76 ? 19.057 8.567 40.619 1.00 23.49 ? 76 ARG A CZ 1 ATOM 591 N NH1 . ARG A 1 76 ? 18.475 8.415 39.428 1.00 22.55 ? 76 ARG A NH1 1 ATOM 592 N NH2 . ARG A 1 76 ? 19.525 9.758 40.991 1.00 21.32 ? 76 ARG A NH2 1 ATOM 593 N N . GLU A 1 77 ? 21.791 2.334 42.202 1.00 20.84 ? 77 GLU A N 1 ATOM 594 C CA . GLU A 1 77 ? 23.237 2.537 42.301 1.00 21.58 ? 77 GLU A CA 1 ATOM 595 C C . GLU A 1 77 ? 23.919 2.133 40.988 1.00 20.88 ? 77 GLU A C 1 ATOM 596 O O . GLU A 1 77 ? 24.828 2.812 40.532 1.00 20.85 ? 77 GLU A O 1 ATOM 597 C CB . GLU A 1 77 ? 23.868 1.821 43.491 1.00 22.04 ? 77 GLU A CB 1 ATOM 598 C CG . GLU A 1 77 ? 25.162 2.503 43.924 1.00 26.00 ? 77 GLU A CG 1 ATOM 599 C CD . GLU A 1 77 ? 26.117 1.572 44.669 1.00 32.85 ? 77 GLU A CD 1 ATOM 600 O OE1 . GLU A 1 77 ? 25.620 0.670 45.418 1.00 32.81 ? 77 GLU A OE1 1 ATOM 601 O OE2 . GLU A 1 77 ? 27.368 1.745 44.491 1.00 33.86 ? 77 GLU A OE2 1 ATOM 602 N N . VAL A 1 78 ? 23.441 1.043 40.388 1.00 19.77 ? 78 VAL A N 1 ATOM 603 C CA . VAL A 1 78 ? 23.895 0.589 39.085 1.00 18.66 ? 78 VAL A CA 1 ATOM 604 C C . VAL A 1 78 ? 23.599 1.686 38.101 1.00 18.80 ? 78 VAL A C 1 ATOM 605 O O . VAL A 1 78 ? 24.376 1.935 37.186 1.00 19.56 ? 78 VAL A O 1 ATOM 606 C CB . VAL A 1 78 ? 23.142 -0.722 38.613 1.00 19.12 ? 78 VAL A CB 1 ATOM 607 C CG1 . VAL A 1 78 ? 23.470 -1.066 37.115 1.00 17.08 ? 78 VAL A CG1 1 ATOM 608 C CG2 . VAL A 1 78 ? 23.412 -1.928 39.561 1.00 16.21 ? 78 VAL A CG2 1 ATOM 609 N N . SER A 1 79 ? 22.458 2.343 38.282 1.00 19.02 ? 79 SER A N 1 ATOM 610 C CA . SER A 1 79 ? 22.081 3.479 37.440 1.00 18.80 ? 79 SER A CA 1 ATOM 611 C C . SER A 1 79 ? 23.093 4.613 37.575 1.00 19.66 ? 79 SER A C 1 ATOM 612 O O . SER A 1 79 ? 23.659 5.049 36.578 1.00 19.87 ? 79 SER A O 1 ATOM 613 C CB . SER A 1 79 ? 20.667 3.985 37.747 1.00 18.18 ? 79 SER A CB 1 ATOM 614 O OG . SER A 1 79 ? 20.271 4.983 36.804 1.00 14.33 ? 79 SER A OG 1 ATOM 615 N N . ASN A 1 80 ? 23.347 5.065 38.800 1.00 20.42 ? 80 ASN A N 1 ATOM 616 C CA . ASN A 1 80 ? 24.310 6.163 39.009 1.00 21.07 ? 80 ASN A CA 1 ATOM 617 C C . ASN A 1 80 ? 25.760 5.855 38.535 1.00 22.08 ? 80 ASN A C 1 ATOM 618 O O . ASN A 1 80 ? 26.460 6.721 38.038 1.00 23.16 ? 80 ASN A O 1 ATOM 619 C CB . ASN A 1 80 ? 24.352 6.591 40.486 1.00 19.88 ? 80 ASN A CB 1 ATOM 620 C CG . ASN A 1 80 ? 23.018 7.078 40.987 1.00 19.06 ? 80 ASN A CG 1 ATOM 621 O OD1 . ASN A 1 80 ? 22.120 7.304 40.190 1.00 21.92 ? 80 ASN A OD1 1 ATOM 622 N ND2 . ASN A 1 80 ? 22.873 7.244 42.304 1.00 13.93 ? 80 ASN A ND2 1 ATOM 623 N N . LYS A 1 81 ? 26.233 4.638 38.666 1.00 22.16 ? 81 LYS A N 1 ATOM 624 C CA . LYS A 1 81 ? 27.645 4.434 38.372 1.00 22.86 ? 81 LYS A CA 1 ATOM 625 C C . LYS A 1 81 ? 27.929 4.059 36.936 1.00 22.96 ? 81 LYS A C 1 ATOM 626 O O . LYS A 1 81 ? 29.027 4.290 36.423 1.00 24.11 ? 81 LYS A O 1 ATOM 627 C CB . LYS A 1 81 ? 28.207 3.333 39.284 1.00 23.25 ? 81 LYS A CB 1 ATOM 628 C CG . LYS A 1 81 ? 27.828 3.521 40.712 1.00 24.43 ? 81 LYS A CG 1 ATOM 629 C CD . LYS A 1 81 ? 28.978 3.271 41.590 1.00 27.96 ? 81 LYS A CD 1 ATOM 630 C CE . LYS A 1 81 ? 28.813 4.063 42.873 1.00 32.01 ? 81 LYS A CE 1 ATOM 631 N NZ . LYS A 1 81 ? 29.753 3.592 43.944 1.00 34.46 ? 81 LYS A NZ 1 ATOM 632 N N . ILE A 1 82 ? 26.938 3.442 36.306 1.00 22.26 ? 82 ILE A N 1 ATOM 633 C CA . ILE A 1 82 ? 27.106 2.895 34.976 1.00 21.10 ? 82 ILE A CA 1 ATOM 634 C C . ILE A 1 82 ? 26.273 3.620 33.940 1.00 20.37 ? 82 ILE A C 1 ATOM 635 O O . ILE A 1 82 ? 26.761 3.969 32.862 1.00 19.89 ? 82 ILE A O 1 ATOM 636 C CB . ILE A 1 82 ? 26.789 1.345 34.992 1.00 21.83 ? 82 ILE A CB 1 ATOM 637 C CG1 . ILE A 1 82 ? 27.883 0.596 35.762 1.00 22.30 ? 82 ILE A CG1 1 ATOM 638 C CG2 . ILE A 1 82 ? 26.705 0.752 33.562 1.00 20.45 ? 82 ILE A CG2 1 ATOM 639 C CD1 . ILE A 1 82 ? 27.374 -0.452 36.681 1.00 25.15 ? 82 ILE A CD1 1 ATOM 640 N N . VAL A 1 83 ? 25.017 3.857 34.260 1.00 19.23 ? 83 VAL A N 1 ATOM 641 C CA . VAL A 1 83 ? 24.131 4.355 33.238 1.00 19.10 ? 83 VAL A CA 1 ATOM 642 C C . VAL A 1 83 ? 24.186 5.834 32.872 1.00 19.46 ? 83 VAL A C 1 ATOM 643 O O . VAL A 1 83 ? 24.015 6.198 31.701 1.00 19.65 ? 83 VAL A O 1 ATOM 644 C CB . VAL A 1 83 ? 22.682 4.006 33.531 1.00 19.41 ? 83 VAL A CB 1 ATOM 645 C CG1 . VAL A 1 83 ? 21.858 4.441 32.343 1.00 20.62 ? 83 VAL A CG1 1 ATOM 646 C CG2 . VAL A 1 83 ? 22.518 2.510 33.763 1.00 17.25 ? 83 VAL A CG2 1 ATOM 647 N N . GLY A 1 84 ? 24.426 6.696 33.856 1.00 19.37 ? 84 GLY A N 1 ATOM 648 C CA . GLY A 1 84 ? 24.350 8.122 33.635 1.00 18.11 ? 84 GLY A CA 1 ATOM 649 C C . GLY A 1 84 ? 25.550 8.785 33.041 1.00 17.98 ? 84 GLY A C 1 ATOM 650 O O . GLY A 1 84 ? 26.640 8.239 33.031 1.00 17.65 ? 84 GLY A O 1 ATOM 651 N N . TYR A 1 85 ? 25.315 9.992 32.549 1.00 18.38 ? 85 TYR A N 1 ATOM 652 C CA . TYR A 1 85 ? 26.343 10.855 32.000 1.00 19.48 ? 85 TYR A CA 1 ATOM 653 C C . TYR A 1 85 ? 25.835 12.327 31.973 1.00 21.40 ? 85 TYR A C 1 ATOM 654 O O . TYR A 1 85 ? 24.647 12.600 32.140 1.00 21.42 ? 85 TYR A O 1 ATOM 655 C CB . TYR A 1 85 ? 26.732 10.387 30.602 1.00 18.59 ? 85 TYR A CB 1 ATOM 656 C CG . TYR A 1 85 ? 25.629 10.542 29.576 1.00 18.87 ? 85 TYR A CG 1 ATOM 657 C CD1 . TYR A 1 85 ? 25.565 11.692 28.769 1.00 17.17 ? 85 TYR A CD1 1 ATOM 658 C CD2 . TYR A 1 85 ? 24.653 9.530 29.394 1.00 16.87 ? 85 TYR A CD2 1 ATOM 659 C CE1 . TYR A 1 85 ? 24.562 11.853 27.852 1.00 16.45 ? 85 TYR A CE1 1 ATOM 660 C CE2 . TYR A 1 85 ? 23.662 9.669 28.451 1.00 15.32 ? 85 TYR A CE2 1 ATOM 661 C CZ . TYR A 1 85 ? 23.625 10.838 27.687 1.00 17.02 ? 85 TYR A CZ 1 ATOM 662 O OH . TYR A 1 85 ? 22.644 11.017 26.756 1.00 18.05 ? 85 TYR A OH 1 ATOM 663 N N . LEU A 1 86 ? 26.719 13.278 31.702 1.00 22.84 ? 86 LEU A N 1 ATOM 664 C CA . LEU A 1 86 ? 26.313 14.654 31.815 1.00 24.10 ? 86 LEU A CA 1 ATOM 665 C C . LEU A 1 86 ? 26.302 15.338 30.493 1.00 25.19 ? 86 LEU A C 1 ATOM 666 O O . LEU A 1 86 ? 25.533 16.276 30.258 1.00 25.49 ? 86 LEU A O 1 ATOM 667 C CB . LEU A 1 86 ? 27.282 15.419 32.723 1.00 24.10 ? 86 LEU A CB 1 ATOM 668 C CG . LEU A 1 86 ? 27.222 15.140 34.226 1.00 25.98 ? 86 LEU A CG 1 ATOM 669 C CD1 . LEU A 1 86 ? 28.139 16.105 34.947 1.00 28.75 ? 86 LEU A CD1 1 ATOM 670 C CD2 . LEU A 1 86 ? 25.797 15.253 34.780 1.00 29.43 ? 86 LEU A CD2 1 ATOM 671 N N . ASP A 1 87 ? 27.159 14.882 29.606 1.00 26.10 ? 87 ASP A N 1 ATOM 672 C CA . ASP A 1 87 ? 27.373 15.662 28.411 1.00 26.86 ? 87 ASP A CA 1 ATOM 673 C C . ASP A 1 87 ? 26.670 15.121 27.197 1.00 26.60 ? 87 ASP A C 1 ATOM 674 O O . ASP A 1 87 ? 27.086 14.119 26.630 1.00 26.43 ? 87 ASP A O 1 ATOM 675 C CB . ASP A 1 87 ? 28.869 15.747 28.153 1.00 27.19 ? 87 ASP A CB 1 ATOM 676 C CG . ASP A 1 87 ? 29.210 16.666 26.991 1.00 30.82 ? 87 ASP A CG 1 ATOM 677 O OD1 . ASP A 1 87 ? 28.287 17.388 26.464 1.00 30.51 ? 87 ASP A OD1 1 ATOM 678 O OD2 . ASP A 1 87 ? 30.401 16.718 26.560 1.00 33.45 ? 87 ASP A OD2 1 ATOM 679 N N . GLU A 1 88 ? 25.639 15.821 26.764 1.00 26.73 ? 88 GLU A N 1 ATOM 680 C CA . GLU A 1 88 ? 24.919 15.389 25.598 1.00 27.52 ? 88 GLU A CA 1 ATOM 681 C C . GLU A 1 88 ? 25.706 15.620 24.308 1.00 28.02 ? 88 GLU A C 1 ATOM 682 O O . GLU A 1 88 ? 25.334 15.118 23.240 1.00 28.37 ? 88 GLU A O 1 ATOM 683 C CB . GLU A 1 88 ? 23.561 16.063 25.511 1.00 27.35 ? 88 GLU A CB 1 ATOM 684 C CG . GLU A 1 88 ? 22.561 15.691 26.588 1.00 28.91 ? 88 GLU A CG 1 ATOM 685 C CD . GLU A 1 88 ? 22.301 14.196 26.711 1.00 34.12 ? 88 GLU A CD 1 ATOM 686 O OE1 . GLU A 1 88 ? 22.711 13.406 25.800 1.00 33.83 ? 88 GLU A OE1 1 ATOM 687 O OE2 . GLU A 1 88 ? 21.668 13.806 27.736 1.00 34.56 ? 88 GLU A OE2 1 ATOM 688 N N . GLU A 1 89 ? 26.807 16.353 24.380 1.00 28.36 ? 89 GLU A N 1 ATOM 689 C CA . GLU A 1 89 ? 27.526 16.641 23.145 1.00 28.52 ? 89 GLU A CA 1 ATOM 690 C C . GLU A 1 89 ? 28.104 15.372 22.621 1.00 26.71 ? 89 GLU A C 1 ATOM 691 O O . GLU A 1 89 ? 28.593 14.562 23.385 1.00 26.79 ? 89 GLU A O 1 ATOM 692 C CB . GLU A 1 89 ? 28.620 17.708 23.349 1.00 30.05 ? 89 GLU A CB 1 ATOM 693 C CG . GLU A 1 89 ? 28.974 18.503 22.087 1.00 35.50 ? 89 GLU A CG 1 ATOM 694 C CD . GLU A 1 89 ? 30.305 19.256 22.194 1.00 44.21 ? 89 GLU A CD 1 ATOM 695 O OE1 . GLU A 1 89 ? 31.351 18.595 22.470 1.00 49.36 ? 89 GLU A OE1 1 ATOM 696 O OE2 . GLU A 1 89 ? 30.327 20.509 22.006 1.00 45.99 ? 89 GLU A OE2 1 ATOM 697 N N . GLY A 1 90 ? 27.997 15.184 21.316 1.00 25.87 ? 90 GLY A N 1 ATOM 698 C CA . GLY A 1 90 ? 28.587 14.052 20.618 1.00 24.39 ? 90 GLY A CA 1 ATOM 699 C C . GLY A 1 90 ? 27.842 12.763 20.726 1.00 23.63 ? 90 GLY A C 1 ATOM 700 O O . GLY A 1 90 ? 28.341 11.734 20.323 1.00 24.91 ? 90 GLY A O 1 ATOM 701 N N . VAL A 1 91 ? 26.618 12.812 21.219 1.00 23.00 ? 91 VAL A N 1 ATOM 702 C CA . VAL A 1 91 ? 25.902 11.602 21.570 1.00 21.66 ? 91 VAL A CA 1 ATOM 703 C C . VAL A 1 91 ? 24.948 11.095 20.492 1.00 21.69 ? 91 VAL A C 1 ATOM 704 O O . VAL A 1 91 ? 24.519 9.947 20.558 1.00 21.14 ? 91 VAL A O 1 ATOM 705 C CB . VAL A 1 91 ? 25.206 11.808 22.937 1.00 21.78 ? 91 VAL A CB 1 ATOM 706 C CG1 . VAL A 1 91 ? 23.729 12.170 22.784 1.00 22.24 ? 91 VAL A CG1 1 ATOM 707 C CG2 . VAL A 1 91 ? 25.370 10.589 23.788 1.00 21.84 ? 91 VAL A CG2 1 ATOM 708 N N . LEU A 1 92 ? 24.663 11.943 19.488 1.00 21.86 ? 92 LEU A N 1 ATOM 709 C CA . LEU A 1 92 ? 23.750 11.639 18.381 1.00 21.78 ? 92 LEU A CA 1 ATOM 710 C C . LEU A 1 92 ? 24.257 10.630 17.341 1.00 22.58 ? 92 LEU A C 1 ATOM 711 O O . LEU A 1 92 ? 25.431 10.581 16.988 1.00 21.90 ? 92 LEU A O 1 ATOM 712 C CB . LEU A 1 92 ? 23.285 12.915 17.692 1.00 21.96 ? 92 LEU A CB 1 ATOM 713 C CG . LEU A 1 92 ? 22.592 13.922 18.624 1.00 21.04 ? 92 LEU A CG 1 ATOM 714 C CD1 . LEU A 1 92 ? 22.149 15.071 17.818 1.00 20.24 ? 92 LEU A CD1 1 ATOM 715 C CD2 . LEU A 1 92 ? 21.407 13.280 19.317 1.00 21.60 ? 92 LEU A CD2 1 ATOM 716 N N . ASP A 1 93 ? 23.332 9.794 16.889 1.00 23.24 ? 93 ASP A N 1 ATOM 717 C CA . ASP A 1 93 ? 23.632 8.765 15.933 1.00 23.46 ? 93 ASP A CA 1 ATOM 718 C C . ASP A 1 93 ? 23.717 9.398 14.541 1.00 24.47 ? 93 ASP A C 1 ATOM 719 O O . ASP A 1 93 ? 22.688 9.710 13.926 1.00 24.49 ? 93 ASP A O 1 ATOM 720 C CB . ASP A 1 93 ? 22.501 7.743 15.945 1.00 23.14 ? 93 ASP A CB 1 ATOM 721 C CG . ASP A 1 93 ? 22.875 6.438 15.286 1.00 22.97 ? 93 ASP A CG 1 ATOM 722 O OD1 . ASP A 1 93 ? 23.716 6.444 14.358 1.00 21.84 ? 93 ASP A OD1 1 ATOM 723 O OD2 . ASP A 1 93 ? 22.352 5.344 15.616 1.00 21.96 ? 93 ASP A OD2 1 ATOM 724 N N . GLN A 1 94 ? 24.937 9.587 14.046 1.00 24.74 ? 94 GLN A N 1 ATOM 725 C CA . GLN A 1 94 ? 25.127 10.030 12.679 1.00 25.48 ? 94 GLN A CA 1 ATOM 726 C C . GLN A 1 94 ? 24.295 9.274 11.582 1.00 25.16 ? 94 GLN A C 1 ATOM 727 O O . GLN A 1 94 ? 24.055 9.806 10.520 1.00 24.84 ? 94 GLN A O 1 ATOM 728 C CB . GLN A 1 94 ? 26.616 9.999 12.349 1.00 25.69 ? 94 GLN A CB 1 ATOM 729 C CG . GLN A 1 94 ? 27.468 10.949 13.179 1.00 30.00 ? 94 GLN A CG 1 ATOM 730 C CD . GLN A 1 94 ? 26.790 12.320 13.415 1.00 35.86 ? 94 GLN A CD 1 ATOM 731 O OE1 . GLN A 1 94 ? 26.815 13.221 12.543 1.00 39.35 ? 94 GLN A OE1 1 ATOM 732 N NE2 . GLN A 1 94 ? 26.204 12.482 14.597 1.00 35.90 ? 94 GLN A NE2 1 ATOM 733 N N . ASN A 1 95 ? 23.830 8.047 11.804 1.00 25.64 ? 95 ASN A N 1 ATOM 734 C CA . ASN A 1 95 ? 23.137 7.357 10.695 1.00 25.76 ? 95 ASN A CA 1 ATOM 735 C C . ASN A 1 95 ? 21.772 6.758 11.025 1.00 24.65 ? 95 ASN A C 1 ATOM 736 O O . ASN A 1 95 ? 21.298 5.818 10.386 1.00 25.37 ? 95 ASN A O 1 ATOM 737 C CB . ASN A 1 95 ? 24.060 6.371 9.941 1.00 26.53 ? 95 ASN A CB 1 ATOM 738 C CG . ASN A 1 95 ? 23.618 6.174 8.509 1.00 31.20 ? 95 ASN A CG 1 ATOM 739 O OD1 . ASN A 1 95 ? 22.955 7.053 7.970 1.00 34.01 ? 95 ASN A OD1 1 ATOM 740 N ND2 . ASN A 1 95 ? 23.952 5.018 7.895 1.00 38.16 ? 95 ASN A ND2 1 ATOM 741 N N . ARG A 1 96 ? 21.114 7.396 11.961 1.00 23.41 ? 96 ARG A N 1 ATOM 742 C CA . ARG A 1 96 ? 19.775 7.018 12.343 1.00 21.20 ? 96 ARG A CA 1 ATOM 743 C C . ARG A 1 96 ? 18.993 8.251 12.766 1.00 20.94 ? 96 ARG A C 1 ATOM 744 O O . ARG A 1 96 ? 19.396 8.989 13.670 1.00 20.98 ? 96 ARG A O 1 ATOM 745 C CB . ARG A 1 96 ? 19.785 5.993 13.486 1.00 21.28 ? 96 ARG A CB 1 ATOM 746 C CG . ARG A 1 96 ? 20.563 4.722 13.168 1.00 20.45 ? 96 ARG A CG 1 ATOM 747 C CD . ARG A 1 96 ? 19.913 3.920 12.030 1.00 22.20 ? 96 ARG A CD 1 ATOM 748 N NE . ARG A 1 96 ? 20.359 2.517 11.960 1.00 24.74 ? 96 ARG A NE 1 ATOM 749 C CZ . ARG A 1 96 ? 21.474 2.116 11.390 1.00 26.78 ? 96 ARG A CZ 1 ATOM 750 N NH1 . ARG A 1 96 ? 22.273 3.008 10.840 1.00 28.03 ? 96 ARG A NH1 1 ATOM 751 N NH2 . ARG A 1 96 ? 21.790 0.830 11.367 1.00 27.74 ? 96 ARG A NH2 1 ATOM 752 N N . SER A 1 97 ? 17.869 8.445 12.098 1.00 19.79 ? 97 SER A N 1 ATOM 753 C CA . SER A 1 97 ? 16.972 9.548 12.396 1.00 18.43 ? 97 SER A CA 1 ATOM 754 C C . SER A 1 97 ? 16.210 9.280 13.672 1.00 17.14 ? 97 SER A C 1 ATOM 755 O O . SER A 1 97 ? 16.151 8.132 14.109 1.00 18.16 ? 97 SER A O 1 ATOM 756 C CB . SER A 1 97 ? 15.966 9.626 11.267 1.00 18.83 ? 97 SER A CB 1 ATOM 757 O OG . SER A 1 97 ? 15.004 8.583 11.381 1.00 20.36 ? 97 SER A OG 1 ATOM 758 N N . LEU A 1 98 ? 15.580 10.305 14.242 1.00 15.56 ? 98 LEU A N 1 ATOM 759 C CA . LEU A 1 98 ? 14.752 10.148 15.444 1.00 14.79 ? 98 LEU A CA 1 ATOM 760 C C . LEU A 1 98 ? 13.638 9.099 15.253 1.00 14.92 ? 98 LEU A C 1 ATOM 761 O O . LEU A 1 98 ? 13.166 8.450 16.186 1.00 14.07 ? 98 LEU A O 1 ATOM 762 C CB . LEU A 1 98 ? 14.091 11.468 15.816 1.00 13.71 ? 98 LEU A CB 1 ATOM 763 C CG . LEU A 1 98 ? 14.077 11.856 17.297 1.00 12.83 ? 98 LEU A CG 1 ATOM 764 C CD1 . LEU A 1 98 ? 13.026 12.891 17.535 1.00 13.34 ? 98 LEU A CD1 1 ATOM 765 C CD2 . LEU A 1 98 ? 13.891 10.731 18.276 1.00 10.48 ? 98 LEU A CD2 1 ATOM 766 N N . LEU A 1 99 ? 13.207 8.961 14.014 1.00 15.37 ? 99 LEU A N 1 ATOM 767 C CA . LEU A 1 99 ? 12.155 8.045 13.726 1.00 15.66 ? 99 LEU A CA 1 ATOM 768 C C . LEU A 1 99 ? 12.621 6.595 13.988 1.00 16.28 ? 99 LEU A C 1 ATOM 769 O O . LEU A 1 99 ? 11.800 5.750 14.307 1.00 17.92 ? 99 LEU A O 1 ATOM 770 C CB . LEU A 1 99 ? 11.709 8.270 12.305 1.00 14.80 ? 99 LEU A CB 1 ATOM 771 C CG . LEU A 1 99 ? 10.748 7.232 11.788 1.00 15.00 ? 99 LEU A CG 1 ATOM 772 C CD1 . LEU A 1 99 ? 9.426 7.407 12.496 1.00 16.61 ? 99 LEU A CD1 1 ATOM 773 C CD2 . LEU A 1 99 ? 10.634 7.401 10.296 1.00 11.45 ? 99 LEU A CD2 1 ATOM 774 N N . PHE A 1 100 ? 13.923 6.323 13.894 1.00 15.86 ? 100 PHE A N 1 ATOM 775 C CA . PHE A 1 100 ? 14.460 5.002 14.190 1.00 15.93 ? 100 PHE A CA 1 ATOM 776 C C . PHE A 1 100 ? 14.132 4.643 15.638 1.00 16.01 ? 100 PHE A C 1 ATOM 777 O O . PHE A 1 100 ? 13.560 3.617 15.901 1.00 16.29 ? 100 PHE A O 1 ATOM 778 C CB . PHE A 1 100 ? 15.968 5.009 13.954 1.00 16.20 ? 100 PHE A CB 1 ATOM 779 C CG . PHE A 1 100 ? 16.665 3.737 14.364 1.00 16.33 ? 100 PHE A CG 1 ATOM 780 C CD1 . PHE A 1 100 ? 16.555 2.588 13.595 1.00 19.83 ? 100 PHE A CD1 1 ATOM 781 C CD2 . PHE A 1 100 ? 17.470 3.713 15.492 1.00 15.12 ? 100 PHE A CD2 1 ATOM 782 C CE1 . PHE A 1 100 ? 17.233 1.399 13.977 1.00 21.80 ? 100 PHE A CE1 1 ATOM 783 C CE2 . PHE A 1 100 ? 18.144 2.573 15.873 1.00 17.66 ? 100 PHE A CE2 1 ATOM 784 C CZ . PHE A 1 100 ? 18.028 1.395 15.125 1.00 19.64 ? 100 PHE A CZ 1 ATOM 785 N N . MET A 1 101 ? 14.490 5.508 16.580 1.00 15.96 ? 101 MET A N 1 ATOM 786 C CA . MET A 1 101 ? 14.124 5.306 17.971 1.00 15.22 ? 101 MET A CA 1 ATOM 787 C C . MET A 1 101 ? 12.633 5.086 18.105 1.00 15.35 ? 101 MET A C 1 ATOM 788 O O . MET A 1 101 ? 12.202 4.250 18.869 1.00 15.96 ? 101 MET A O 1 ATOM 789 C CB . MET A 1 101 ? 14.468 6.559 18.781 1.00 14.45 ? 101 MET A CB 1 ATOM 790 C CG . MET A 1 101 ? 14.067 6.468 20.219 1.00 13.28 ? 101 MET A CG 1 ATOM 791 S SD . MET A 1 101 ? 12.373 6.998 20.588 1.00 16.93 ? 101 MET A SD 1 ATOM 792 C CE . MET A 1 101 ? 12.386 8.784 20.177 1.00 14.43 ? 101 MET A CE 1 ATOM 793 N N . GLN A 1 102 ? 11.851 5.852 17.363 1.00 15.26 ? 102 GLN A N 1 ATOM 794 C CA . GLN A 1 102 ? 10.415 5.877 17.525 1.00 15.96 ? 102 GLN A CA 1 ATOM 795 C C . GLN A 1 102 ? 9.633 4.709 16.932 1.00 16.36 ? 102 GLN A C 1 ATOM 796 O O . GLN A 1 102 ? 8.592 4.303 17.503 1.00 16.82 ? 102 GLN A O 1 ATOM 797 C CB . GLN A 1 102 ? 9.850 7.199 16.990 1.00 16.91 ? 102 GLN A CB 1 ATOM 798 C CG . GLN A 1 102 ? 8.371 7.428 17.306 1.00 16.66 ? 102 GLN A CG 1 ATOM 799 C CD . GLN A 1 102 ? 8.150 7.501 18.780 1.00 20.12 ? 102 GLN A CD 1 ATOM 800 O OE1 . GLN A 1 102 ? 8.608 8.461 19.457 1.00 24.27 ? 102 GLN A OE1 1 ATOM 801 N NE2 . GLN A 1 102 ? 7.478 6.501 19.313 1.00 16.87 ? 102 GLN A NE2 1 ATOM 802 N N . TRP A 1 103 ? 10.081 4.173 15.796 1.00 15.86 ? 103 TRP A N 1 ATOM 803 C CA . TRP A 1 103 ? 9.377 3.020 15.255 1.00 15.79 ? 103 TRP A CA 1 ATOM 804 C C . TRP A 1 103 ? 9.529 1.852 16.210 1.00 16.16 ? 103 TRP A C 1 ATOM 805 O O . TRP A 1 103 ? 8.637 1.004 16.322 1.00 17.22 ? 103 TRP A O 1 ATOM 806 C CB . TRP A 1 103 ? 9.831 2.625 13.859 1.00 15.12 ? 103 TRP A CB 1 ATOM 807 C CG . TRP A 1 103 ? 8.956 1.531 13.250 1.00 15.50 ? 103 TRP A CG 1 ATOM 808 C CD1 . TRP A 1 103 ? 9.257 0.202 13.158 1.00 16.72 ? 103 TRP A CD1 1 ATOM 809 C CD2 . TRP A 1 103 ? 7.642 1.675 12.690 1.00 16.01 ? 103 TRP A CD2 1 ATOM 810 N NE1 . TRP A 1 103 ? 8.227 -0.479 12.551 1.00 16.53 ? 103 TRP A NE1 1 ATOM 811 C CE2 . TRP A 1 103 ? 7.219 0.400 12.270 1.00 15.75 ? 103 TRP A CE2 1 ATOM 812 C CE3 . TRP A 1 103 ? 6.773 2.754 12.510 1.00 18.16 ? 103 TRP A CE3 1 ATOM 813 C CZ2 . TRP A 1 103 ? 5.984 0.176 11.668 1.00 17.13 ? 103 TRP A CZ2 1 ATOM 814 C CZ3 . TRP A 1 103 ? 5.535 2.525 11.906 1.00 19.71 ? 103 TRP A CZ3 1 ATOM 815 C CH2 . TRP A 1 103 ? 5.152 1.240 11.501 1.00 18.32 ? 103 TRP A CH2 1 ATOM 816 N N . GLY A 1 104 ? 10.650 1.823 16.912 1.00 15.41 ? 104 GLY A N 1 ATOM 817 C CA . GLY A 1 104 ? 10.910 0.751 17.820 1.00 15.54 ? 104 GLY A CA 1 ATOM 818 C C . GLY A 1 104 ? 9.917 0.724 18.945 1.00 15.98 ? 104 GLY A C 1 ATOM 819 O O . GLY A 1 104 ? 9.521 -0.336 19.356 1.00 16.26 ? 104 GLY A O 1 ATOM 820 N N . GLN A 1 105 ? 9.539 1.885 19.462 1.00 16.29 ? 105 GLN A N 1 ATOM 821 C CA . GLN A 1 105 ? 8.561 1.949 20.534 1.00 16.16 ? 105 GLN A CA 1 ATOM 822 C C . GLN A 1 105 ? 7.159 1.564 20.019 1.00 16.47 ? 105 GLN A C 1 ATOM 823 O O . GLN A 1 105 ? 6.342 1.037 20.749 1.00 15.71 ? 105 GLN A O 1 ATOM 824 C CB . GLN A 1 105 ? 8.575 3.343 21.173 1.00 16.05 ? 105 GLN A CB 1 ATOM 825 C CG . GLN A 1 105 ? 8.043 3.375 22.611 1.00 16.32 ? 105 GLN A CG 1 ATOM 826 C CD . GLN A 1 105 ? 7.870 4.782 23.102 1.00 17.77 ? 105 GLN A CD 1 ATOM 827 O OE1 . GLN A 1 105 ? 7.642 5.688 22.305 1.00 18.84 ? 105 GLN A OE1 1 ATOM 828 N NE2 . GLN A 1 105 ? 7.993 4.979 24.395 1.00 17.80 ? 105 GLN A NE2 1 ATOM 829 N N . ILE A 1 106 ? 6.865 1.847 18.761 1.00 17.90 ? 106 ILE A N 1 ATOM 830 C CA . ILE A 1 106 ? 5.589 1.411 18.219 1.00 19.50 ? 106 ILE A CA 1 ATOM 831 C C . ILE A 1 106 ? 5.526 -0.113 18.159 1.00 19.70 ? 106 ILE A C 1 ATOM 832 O O . ILE A 1 106 ? 4.612 -0.739 18.683 1.00 19.66 ? 106 ILE A O 1 ATOM 833 C CB . ILE A 1 106 ? 5.361 2.016 16.852 1.00 20.28 ? 106 ILE A CB 1 ATOM 834 C CG1 . ILE A 1 106 ? 4.721 3.403 17.000 1.00 21.68 ? 106 ILE A CG1 1 ATOM 835 C CG2 . ILE A 1 106 ? 4.426 1.152 15.989 1.00 21.21 ? 106 ILE A CG2 1 ATOM 836 C CD1 . ILE A 1 106 ? 4.971 4.246 15.780 1.00 24.95 ? 106 ILE A CD1 1 ATOM 837 N N . VAL A 1 107 ? 6.531 -0.711 17.536 1.00 20.25 ? 107 VAL A N 1 ATOM 838 C CA . VAL A 1 107 ? 6.612 -2.166 17.417 1.00 19.53 ? 107 VAL A CA 1 ATOM 839 C C . VAL A 1 107 ? 6.555 -2.883 18.769 1.00 18.68 ? 107 VAL A C 1 ATOM 840 O O . VAL A 1 107 ? 5.778 -3.799 18.974 1.00 19.12 ? 107 VAL A O 1 ATOM 841 C CB . VAL A 1 107 ? 7.852 -2.571 16.601 1.00 19.84 ? 107 VAL A CB 1 ATOM 842 C CG1 . VAL A 1 107 ? 7.951 -4.089 16.522 1.00 21.53 ? 107 VAL A CG1 1 ATOM 843 C CG2 . VAL A 1 107 ? 7.778 -1.979 15.196 1.00 18.19 ? 107 VAL A CG2 1 ATOM 844 N N . ASP A 1 108 ? 7.396 -2.470 19.729 1.00 18.41 ? 108 ASP A N 1 ATOM 845 C CA . ASP A 1 108 ? 7.401 -3.062 21.079 1.00 18.49 ? 108 ASP A CA 1 ATOM 846 C C . ASP A 1 108 ? 6.005 -3.032 21.711 1.00 18.49 ? 108 ASP A C 1 ATOM 847 O O . ASP A 1 108 ? 5.574 -4.032 22.297 1.00 17.79 ? 108 ASP A O 1 ATOM 848 C CB . ASP A 1 108 ? 8.400 -2.319 22.026 1.00 18.21 ? 108 ASP A CB 1 ATOM 849 C CG . ASP A 1 108 ? 8.283 -2.664 23.517 1.00 20.27 ? 108 ASP A CG 1 ATOM 850 O OD1 . ASP A 1 108 ? 7.147 -2.576 24.059 1.00 21.64 ? 108 ASP A OD1 1 ATOM 851 O OD2 . ASP A 1 108 ? 9.329 -3.010 24.121 1.00 15.18 ? 108 ASP A OD2 1 ATOM 852 N N . HIS A 1 109 ? 5.283 -1.900 21.595 1.00 17.90 ? 109 HIS A N 1 ATOM 853 C CA . HIS A 1 109 ? 3.976 -1.708 22.216 1.00 17.09 ? 109 HIS A CA 1 ATOM 854 C C . HIS A 1 109 ? 2.902 -2.523 21.535 1.00 17.03 ? 109 HIS A C 1 ATOM 855 O O . HIS A 1 109 ? 1.852 -2.782 22.118 1.00 17.29 ? 109 HIS A O 1 ATOM 856 C CB . HIS A 1 109 ? 3.575 -0.256 22.308 1.00 15.82 ? 109 HIS A CB 1 ATOM 857 C CG . HIS A 1 109 ? 4.416 0.529 23.355 1.00 18.14 ? 109 HIS A CG 1 ATOM 858 N ND1 . HIS A 1 109 ? 4.029 1.755 23.862 1.00 17.50 ? 109 HIS A ND1 1 ATOM 859 C CD2 . HIS A 1 109 ? 5.620 0.252 23.927 1.00 19.89 ? 109 HIS A CD2 1 ATOM 860 C CE1 . HIS A 1 109 ? 4.941 2.181 24.721 1.00 18.25 ? 109 HIS A CE1 1 ATOM 861 N NE2 . HIS A 1 109 ? 5.917 1.289 24.781 1.00 18.29 ? 109 HIS A NE2 1 ATOM 862 N N . ASP A 1 110 ? 3.115 -2.921 20.266 1.00 16.65 ? 110 ASP A N 1 ATOM 863 C CA . ASP A 1 110 ? 2.182 -3.771 19.503 1.00 17.52 ? 110 ASP A CA 1 ATOM 864 C C . ASP A 1 110 ? 2.413 -5.190 19.996 1.00 17.79 ? 110 ASP A C 1 ATOM 865 O O . ASP A 1 110 ? 1.529 -6.038 19.899 1.00 17.33 ? 110 ASP A O 1 ATOM 866 C CB . ASP A 1 110 ? 2.400 -3.731 17.986 1.00 17.70 ? 110 ASP A CB 1 ATOM 867 C CG . ASP A 1 110 ? 1.344 -4.436 17.105 1.00 19.24 ? 110 ASP A CG 1 ATOM 868 O OD1 . ASP A 1 110 ? 1.060 -5.621 17.364 1.00 17.98 ? 110 ASP A OD1 1 ATOM 869 O OD2 . ASP A 1 110 ? 0.812 -3.793 16.167 1.00 24.75 ? 110 ASP A OD2 1 ATOM 870 N N . LEU A 1 111 ? 3.577 -5.443 20.532 1.00 18.40 ? 111 LEU A N 1 ATOM 871 C CA . LEU A 1 111 ? 3.967 -6.787 20.878 1.00 18.63 ? 111 LEU A CA 1 ATOM 872 C C . LEU A 1 111 ? 3.823 -7.237 22.319 1.00 18.29 ? 111 LEU A C 1 ATOM 873 O O . LEU A 1 111 ? 3.476 -8.394 22.567 1.00 19.01 ? 111 LEU A O 1 ATOM 874 C CB . LEU A 1 111 ? 5.424 -6.993 20.476 1.00 18.19 ? 111 LEU A CB 1 ATOM 875 C CG . LEU A 1 111 ? 5.693 -6.970 18.984 1.00 18.03 ? 111 LEU A CG 1 ATOM 876 C CD1 . LEU A 1 111 ? 7.188 -7.027 18.717 1.00 17.89 ? 111 LEU A CD1 1 ATOM 877 C CD2 . LEU A 1 111 ? 4.969 -8.126 18.301 1.00 16.13 ? 111 LEU A CD2 1 ATOM 878 N N . ASP A 1 112 ? 4.069 -6.358 23.270 1.00 18.35 ? 112 ASP A N 1 ATOM 879 C CA . ASP A 1 112 ? 4.053 -6.797 24.663 1.00 18.33 ? 112 ASP A CA 1 ATOM 880 C C . ASP A 1 112 ? 3.802 -5.673 25.625 1.00 18.17 ? 112 ASP A C 1 ATOM 881 O O . ASP A 1 112 ? 4.228 -4.588 25.400 1.00 18.06 ? 112 ASP A O 1 ATOM 882 C CB . ASP A 1 112 ? 5.384 -7.482 25.010 1.00 18.66 ? 112 ASP A CB 1 ATOM 883 C CG . ASP A 1 112 ? 6.614 -6.590 24.736 1.00 17.90 ? 112 ASP A CG 1 ATOM 884 O OD1 . ASP A 1 112 ? 7.247 -6.751 23.676 1.00 16.91 ? 112 ASP A OD1 1 ATOM 885 O OD2 . ASP A 1 112 ? 7.031 -5.724 25.537 1.00 14.90 ? 112 ASP A OD2 1 ATOM 886 N N . PHE A 1 113 ? 3.076 -5.951 26.692 1.00 19.24 ? 113 PHE A N 1 ATOM 887 C CA . PHE A 1 113 ? 2.816 -4.985 27.748 1.00 19.37 ? 113 PHE A CA 1 ATOM 888 C C . PHE A 1 113 ? 2.501 -5.732 29.027 1.00 20.12 ? 113 PHE A C 1 ATOM 889 O O . PHE A 1 113 ? 1.478 -6.385 29.126 1.00 19.25 ? 113 PHE A O 1 ATOM 890 C CB . PHE A 1 113 ? 1.619 -4.157 27.357 1.00 19.95 ? 113 PHE A CB 1 ATOM 891 C CG . PHE A 1 113 ? 1.193 -3.157 28.393 1.00 20.08 ? 113 PHE A CG 1 ATOM 892 C CD1 . PHE A 1 113 ? 2.120 -2.450 29.124 1.00 19.12 ? 113 PHE A CD1 1 ATOM 893 C CD2 . PHE A 1 113 ? -0.155 -2.930 28.631 1.00 17.98 ? 113 PHE A CD2 1 ATOM 894 C CE1 . PHE A 1 113 ? 1.698 -1.560 30.066 1.00 21.70 ? 113 PHE A CE1 1 ATOM 895 C CE2 . PHE A 1 113 ? -0.567 -2.004 29.574 1.00 19.25 ? 113 PHE A CE2 1 ATOM 896 C CZ . PHE A 1 113 ? 0.337 -1.321 30.276 1.00 19.68 ? 113 PHE A CZ 1 ATOM 897 N N . ALA A 1 114 ? 3.386 -5.657 30.009 1.00 21.86 ? 114 ALA A N 1 ATOM 898 C CA . ALA A 1 114 ? 3.129 -6.307 31.289 1.00 23.81 ? 114 ALA A CA 1 ATOM 899 C C . ALA A 1 114 ? 2.703 -5.245 32.271 1.00 26.01 ? 114 ALA A C 1 ATOM 900 O O . ALA A 1 114 ? 3.527 -4.626 32.925 1.00 26.35 ? 114 ALA A O 1 ATOM 901 C CB . ALA A 1 114 ? 4.371 -6.995 31.775 1.00 23.27 ? 114 ALA A CB 1 ATOM 902 N N . PRO A 1 115 ? 1.417 -5.052 32.433 1.00 28.58 ? 115 PRO A N 1 ATOM 903 C CA . PRO A 1 115 ? 0.945 -3.950 33.261 1.00 31.42 ? 115 PRO A CA 1 ATOM 904 C C . PRO A 1 115 ? 1.181 -4.218 34.747 1.00 34.27 ? 115 PRO A C 1 ATOM 905 O O . PRO A 1 115 ? 1.300 -5.338 35.161 1.00 33.66 ? 115 PRO A O 1 ATOM 906 C CB . PRO A 1 115 ? -0.545 -3.899 32.942 1.00 31.25 ? 115 PRO A CB 1 ATOM 907 C CG . PRO A 1 115 ? -0.880 -5.308 32.610 1.00 30.05 ? 115 PRO A CG 1 ATOM 908 C CD . PRO A 1 115 ? 0.327 -5.907 31.951 1.00 28.85 ? 115 PRO A CD 1 ATOM 909 N N . GLU A 1 116 ? 1.263 -3.172 35.545 1.00 38.71 ? 116 GLU A N 1 ATOM 910 C CA . GLU A 1 116 ? 1.470 -3.324 36.977 1.00 43.25 ? 116 GLU A CA 1 ATOM 911 C C . GLU A 1 116 ? 0.226 -3.829 37.666 1.00 46.69 ? 116 GLU A C 1 ATOM 912 O O . GLU A 1 116 ? -0.880 -3.708 37.169 1.00 47.09 ? 116 GLU A O 1 ATOM 913 C CB . GLU A 1 116 ? 1.848 -2.000 37.608 1.00 42.90 ? 116 GLU A CB 1 ATOM 914 C CG . GLU A 1 116 ? 3.249 -1.527 37.276 1.00 44.21 ? 116 GLU A CG 1 ATOM 915 C CD . GLU A 1 116 ? 3.574 -0.220 37.975 1.00 47.10 ? 116 GLU A CD 1 ATOM 916 O OE1 . GLU A 1 116 ? 2.659 0.597 38.182 1.00 47.06 ? 116 GLU A OE1 1 ATOM 917 O OE2 . GLU A 1 116 ? 4.770 -0.011 38.297 1.00 48.41 ? 116 GLU A OE2 1 ATOM 918 N N . THR A 1 117 ? 0.450 -4.390 38.821 1.00 51.41 ? 117 THR A N 1 ATOM 919 C CA . THR A 1 117 ? -0.618 -4.845 39.663 1.00 55.49 ? 117 THR A CA 1 ATOM 920 C C . THR A 1 117 ? -1.318 -3.629 40.180 1.00 59.17 ? 117 THR A C 1 ATOM 921 O O . THR A 1 117 ? -0.637 -2.773 40.754 1.00 59.54 ? 117 THR A O 1 ATOM 922 C CB . THR A 1 117 ? -0.101 -5.631 40.874 1.00 55.11 ? 117 THR A CB 1 ATOM 923 O OG1 . THR A 1 117 ? 1.266 -5.312 41.100 1.00 54.98 ? 117 THR A OG1 1 ATOM 924 C CG2 . THR A 1 117 ? -0.261 -7.120 40.643 1.00 54.44 ? 117 THR A CG2 1 ATOM 925 N N . GLU A 1 118 ? -2.598 -3.455 40.019 1.00 63.13 ? 118 GLU A N 1 ATOM 926 C CA A GLU A 1 118 ? -3.142 -2.234 40.625 0.50 67.32 ? 118 GLU A CA 1 ATOM 927 C CA B GLU A 1 118 ? -3.182 -2.205 40.584 0.50 67.32 ? 118 GLU A CA 1 ATOM 928 C C . GLU A 1 118 ? -3.778 -2.562 41.976 1.00 69.79 ? 118 GLU A C 1 ATOM 929 O O . GLU A 1 118 ? -3.859 -1.711 42.853 1.00 70.31 ? 118 GLU A O 1 ATOM 930 C CB A GLU A 1 118 ? -4.191 -1.560 39.719 0.50 67.26 ? 118 GLU A CB 1 ATOM 931 C CB B GLU A 1 118 ? -4.505 -2.748 39.988 0.50 67.26 ? 118 GLU A CB 1 ATOM 932 C CG A GLU A 1 118 ? -5.615 -2.074 39.948 0.50 68.83 ? 118 GLU A CG 1 ATOM 933 C CG B GLU A 1 118 ? -4.682 -2.452 38.497 0.50 68.83 ? 118 GLU A CG 1 ATOM 934 C CD A GLU A 1 118 ? -6.596 -1.028 40.408 0.50 70.17 ? 118 GLU A CD 1 ATOM 935 C CD B GLU A 1 118 ? -5.952 -3.026 37.825 0.50 70.17 ? 118 GLU A CD 1 ATOM 936 O OE1 A GLU A 1 118 ? -6.802 -0.059 39.653 0.50 71.39 ? 118 GLU A OE1 1 ATOM 937 O OE1 B GLU A 1 118 ? -6.750 -2.216 37.309 0.50 71.39 ? 118 GLU A OE1 1 ATOM 938 O OE2 A GLU A 1 118 ? -7.141 -1.167 41.516 0.50 71.30 ? 118 GLU A OE2 1 ATOM 939 O OE2 B GLU A 1 118 ? -6.125 -4.257 37.837 0.50 71.30 ? 118 GLU A OE2 1 ATOM 940 N N . LEU A 1 119 ? -4.855 -3.330 42.105 1.00 72.79 ? 119 LEU A N 1 ATOM 941 C CA . LEU A 1 119 ? -5.319 -4.031 43.293 1.00 75.69 ? 119 LEU A CA 1 ATOM 942 C C . LEU A 1 119 ? -6.003 -3.072 44.263 1.00 77.44 ? 119 LEU A C 1 ATOM 943 O O . LEU A 1 119 ? -5.990 -3.244 45.491 1.00 78.05 ? 119 LEU A O 1 ATOM 944 C CB . LEU A 1 119 ? -4.154 -4.745 43.989 1.00 75.91 ? 119 LEU A CB 1 ATOM 945 C CG . LEU A 1 119 ? -4.037 -6.270 43.891 1.00 77.00 ? 119 LEU A CG 1 ATOM 946 C CD1 . LEU A 1 119 ? -2.975 -6.675 42.895 1.00 77.50 ? 119 LEU A CD1 1 ATOM 947 C CD2 . LEU A 1 119 ? -3.749 -6.869 45.260 1.00 78.53 ? 119 LEU A CD2 1 ATOM 948 N N . GLY A 1 120 ? -6.641 -2.070 43.665 1.00 79.22 ? 120 GLY A N 1 ATOM 949 C CA . GLY A 1 120 ? -7.428 -1.148 44.453 1.00 81.48 ? 120 GLY A CA 1 ATOM 950 C C . GLY A 1 120 ? -7.273 0.331 44.209 1.00 82.81 ? 120 GLY A C 1 ATOM 951 O O . GLY A 1 120 ? -6.176 0.882 44.224 1.00 83.09 ? 120 GLY A O 1 ATOM 952 N N . SER A 1 121 ? -8.410 0.923 43.970 1.00 83.99 ? 121 SER A N 1 ATOM 953 C CA . SER A 1 121 ? -8.575 2.356 43.865 1.00 84.89 ? 121 SER A CA 1 ATOM 954 C C . SER A 1 121 ? -9.085 2.739 45.239 1.00 85.43 ? 121 SER A C 1 ATOM 955 O O . SER A 1 121 ? -10.147 3.350 45.385 1.00 85.79 ? 121 SER A O 1 ATOM 956 C CB . SER A 1 121 ? -9.583 2.740 42.784 1.00 85.01 ? 121 SER A CB 1 ATOM 957 O OG . SER A 1 121 ? -9.181 3.934 42.130 1.00 84.83 ? 121 SER A OG 1 ATOM 958 N N . ASN A 1 122 ? -8.308 2.371 46.250 1.00 85.93 ? 122 ASN A N 1 ATOM 959 C CA . ASN A 1 122 ? -8.726 2.553 47.630 1.00 86.36 ? 122 ASN A CA 1 ATOM 960 C C . ASN A 1 122 ? -7.558 2.872 48.540 1.00 86.43 ? 122 ASN A C 1 ATOM 961 O O . ASN A 1 122 ? -7.423 3.966 49.104 1.00 86.64 ? 122 ASN A O 1 ATOM 962 C CB . ASN A 1 122 ? -9.338 1.213 48.098 1.00 86.61 ? 122 ASN A CB 1 ATOM 963 C CG . ASN A 1 122 ? -10.263 1.342 49.302 1.00 86.58 ? 122 ASN A CG 1 ATOM 964 O OD1 . ASN A 1 122 ? -10.536 2.437 49.795 1.00 87.34 ? 122 ASN A OD1 1 ATOM 965 N ND2 . ASN A 1 122 ? -10.762 0.203 49.770 1.00 87.09 ? 122 ASN A ND2 1 ATOM 966 N N . GLU A 1 123 ? -6.703 1.866 48.618 1.00 86.38 ? 123 GLU A N 1 ATOM 967 C CA . GLU A 1 123 ? -5.629 1.732 49.580 1.00 86.02 ? 123 GLU A CA 1 ATOM 968 C C . GLU A 1 123 ? -4.492 2.723 49.751 1.00 85.50 ? 123 GLU A C 1 ATOM 969 O O . GLU A 1 123 ? -3.897 3.251 48.808 1.00 85.49 ? 123 GLU A O 1 ATOM 970 C CB . GLU A 1 123 ? -5.030 0.329 49.391 1.00 86.13 ? 123 GLU A CB 1 ATOM 971 C CG . GLU A 1 123 ? -4.500 -0.298 50.671 1.00 86.72 ? 123 GLU A CG 1 ATOM 972 C CD . GLU A 1 123 ? -5.141 -1.637 50.986 1.00 87.07 ? 123 GLU A CD 1 ATOM 973 O OE1 . GLU A 1 123 ? -6.390 -1.739 50.890 1.00 87.34 ? 123 GLU A OE1 1 ATOM 974 O OE2 . GLU A 1 123 ? -4.394 -2.579 51.340 1.00 86.51 ? 123 GLU A OE2 1 ATOM 975 N N . HIS A 1 124 ? -4.201 2.953 51.021 1.00 84.87 ? 124 HIS A N 1 ATOM 976 C CA . HIS A 1 124 ? -2.963 3.576 51.338 1.00 84.13 ? 124 HIS A CA 1 ATOM 977 C C . HIS A 1 124 ? -2.052 2.375 51.161 1.00 83.10 ? 124 HIS A C 1 ATOM 978 O O . HIS A 1 124 ? -1.643 1.737 52.126 1.00 83.17 ? 124 HIS A O 1 ATOM 979 C CB . HIS A 1 124 ? -2.917 4.111 52.767 1.00 84.57 ? 124 HIS A CB 1 ATOM 980 C CG . HIS A 1 124 ? -3.987 5.117 53.053 1.00 85.81 ? 124 HIS A CG 1 ATOM 981 N ND1 . HIS A 1 124 ? -5.101 4.812 53.803 1.00 87.28 ? 124 HIS A ND1 1 ATOM 982 C CD2 . HIS A 1 124 ? -4.131 6.406 52.663 1.00 86.52 ? 124 HIS A CD2 1 ATOM 983 C CE1 . HIS A 1 124 ? -5.884 5.875 53.872 1.00 88.44 ? 124 HIS A CE1 1 ATOM 984 N NE2 . HIS A 1 124 ? -5.319 6.854 53.186 1.00 87.98 ? 124 HIS A NE2 1 ATOM 985 N N . SER A 1 125 ? -1.838 2.019 49.899 1.00 81.68 ? 125 SER A N 1 ATOM 986 C CA . SER A 1 125 ? -0.885 0.998 49.494 1.00 80.23 ? 125 SER A CA 1 ATOM 987 C C . SER A 1 125 ? -0.327 1.589 48.257 1.00 79.00 ? 125 SER A C 1 ATOM 988 O O . SER A 1 125 ? 0.726 1.182 47.783 1.00 79.14 ? 125 SER A O 1 ATOM 989 C CB . SER A 1 125 ? -1.492 -0.348 49.128 1.00 80.42 ? 125 SER A CB 1 ATOM 990 O OG . SER A 1 125 ? -0.515 -1.119 48.434 1.00 80.99 ? 125 SER A OG 1 ATOM 991 N N . LYS A 1 126 ? -1.050 2.529 47.685 1.00 77.10 ? 126 LYS A N 1 ATOM 992 C CA . LYS A 1 126 ? -0.427 3.238 46.604 1.00 75.49 ? 126 LYS A CA 1 ATOM 993 C C . LYS A 1 126 ? 0.204 4.433 47.303 1.00 73.82 ? 126 LYS A C 1 ATOM 994 O O . LYS A 1 126 ? 0.847 5.278 46.684 1.00 74.10 ? 126 LYS A O 1 ATOM 995 C CB . LYS A 1 126 ? -1.453 3.648 45.551 1.00 76.08 ? 126 LYS A CB 1 ATOM 996 C CG . LYS A 1 126 ? -2.541 2.600 45.296 1.00 76.81 ? 126 LYS A CG 1 ATOM 997 C CD . LYS A 1 126 ? -3.624 3.133 44.362 1.00 78.12 ? 126 LYS A CD 1 ATOM 998 C CE . LYS A 1 126 ? -4.746 3.828 45.138 1.00 79.26 ? 126 LYS A CE 1 ATOM 999 N NZ . LYS A 1 126 ? -5.795 4.386 44.222 1.00 79.44 ? 126 LYS A NZ 1 ATOM 1000 N N . THR A 1 127 ? 0.021 4.459 48.622 1.00 71.29 ? 127 THR A N 1 ATOM 1001 C CA . THR A 1 127 ? 0.492 5.528 49.474 1.00 68.43 ? 127 THR A CA 1 ATOM 1002 C C . THR A 1 127 ? 1.376 4.976 50.597 1.00 66.36 ? 127 THR A C 1 ATOM 1003 O O . THR A 1 127 ? 2.362 5.603 50.967 1.00 66.20 ? 127 THR A O 1 ATOM 1004 C CB . THR A 1 127 ? -0.731 6.310 49.989 1.00 68.93 ? 127 THR A CB 1 ATOM 1005 O OG1 . THR A 1 127 ? -1.007 7.399 49.090 1.00 69.08 ? 127 THR A OG1 1 ATOM 1006 C CG2 . THR A 1 127 ? -0.458 6.966 51.342 1.00 69.02 ? 127 THR A CG2 1 ATOM 1007 N N . GLN A 1 128 ? 1.047 3.800 51.127 1.00 63.82 ? 128 GLN A N 1 ATOM 1008 C CA . GLN A 1 128 ? 1.908 3.152 52.127 1.00 61.51 ? 128 GLN A CA 1 ATOM 1009 C C . GLN A 1 128 ? 3.259 2.843 51.457 1.00 59.38 ? 128 GLN A C 1 ATOM 1010 O O . GLN A 1 128 ? 4.288 2.702 52.119 1.00 59.10 ? 128 GLN A O 1 ATOM 1011 C CB . GLN A 1 128 ? 1.249 1.869 52.694 1.00 61.80 ? 128 GLN A CB 1 ATOM 1012 C CG . GLN A 1 128 ? 2.148 0.984 53.605 1.00 63.45 ? 128 GLN A CG 1 ATOM 1013 C CD . GLN A 1 128 ? 1.376 0.031 54.583 1.00 65.63 ? 128 GLN A CD 1 ATOM 1014 O OE1 . GLN A 1 128 ? 1.377 -1.192 54.397 1.00 66.62 ? 128 GLN A OE1 1 ATOM 1015 N NE2 . GLN A 1 128 ? 0.765 0.588 55.636 1.00 65.87 ? 128 GLN A NE2 1 ATOM 1016 N N . CYS A 1 129 ? 3.230 2.743 50.128 1.00 56.74 ? 129 CYS A N 1 ATOM 1017 C CA . CYS A 1 129 ? 4.417 2.490 49.321 1.00 53.74 ? 129 CYS A CA 1 ATOM 1018 C C . CYS A 1 129 ? 5.078 3.810 48.961 1.00 53.69 ? 129 CYS A C 1 ATOM 1019 O O . CYS A 1 129 ? 6.269 3.996 49.146 1.00 53.38 ? 129 CYS A O 1 ATOM 1020 C CB . CYS A 1 129 ? 4.035 1.737 48.048 1.00 53.01 ? 129 CYS A CB 1 ATOM 1021 S SG . CYS A 1 129 ? 5.454 1.149 47.106 1.00 45.93 ? 129 CYS A SG 1 ATOM 1022 N N . GLU A 1 130 ? 4.283 4.722 48.421 1.00 53.50 ? 130 GLU A N 1 ATOM 1023 C CA . GLU A 1 130 ? 4.734 6.067 48.109 1.00 53.46 ? 130 GLU A CA 1 ATOM 1024 C C . GLU A 1 130 ? 5.473 6.737 49.266 1.00 52.50 ? 130 GLU A C 1 ATOM 1025 O O . GLU A 1 130 ? 6.626 7.116 49.135 1.00 52.43 ? 130 GLU A O 1 ATOM 1026 C CB . GLU A 1 130 ? 3.524 6.951 47.770 1.00 53.99 ? 130 GLU A CB 1 ATOM 1027 C CG . GLU A 1 130 ? 3.269 7.220 46.297 1.00 56.59 ? 130 GLU A CG 1 ATOM 1028 C CD . GLU A 1 130 ? 4.046 8.415 45.745 1.00 60.99 ? 130 GLU A CD 1 ATOM 1029 O OE1 . GLU A 1 130 ? 3.401 9.379 45.249 1.00 62.81 ? 130 GLU A OE1 1 ATOM 1030 O OE2 . GLU A 1 130 ? 5.306 8.388 45.777 1.00 63.12 ? 130 GLU A OE2 1 ATOM 1031 N N . GLU A 1 131 ? 4.793 6.890 50.392 1.00 51.84 ? 131 GLU A N 1 ATOM 1032 C CA . GLU A 1 131 ? 5.299 7.740 51.474 1.00 51.97 ? 131 GLU A CA 1 ATOM 1033 C C . GLU A 1 131 ? 6.362 7.106 52.367 1.00 51.43 ? 131 GLU A C 1 ATOM 1034 O O . GLU A 1 131 ? 7.392 7.713 52.687 1.00 51.54 ? 131 GLU A O 1 ATOM 1035 C CB . GLU A 1 131 ? 4.131 8.215 52.360 1.00 52.35 ? 131 GLU A CB 1 ATOM 1036 C CG . GLU A 1 131 ? 2.869 8.608 51.601 1.00 53.00 ? 131 GLU A CG 1 ATOM 1037 C CD . GLU A 1 131 ? 2.734 10.106 51.412 1.00 55.02 ? 131 GLU A CD 1 ATOM 1038 O OE1 . GLU A 1 131 ? 1.614 10.554 51.068 1.00 56.82 ? 131 GLU A OE1 1 ATOM 1039 O OE2 . GLU A 1 131 ? 3.733 10.837 51.618 1.00 54.22 ? 131 GLU A OE2 1 ATOM 1040 N N . TYR A 1 132 ? 6.133 5.863 52.741 1.00 50.00 ? 132 TYR A N 1 ATOM 1041 C CA . TYR A 1 132 ? 6.978 5.288 53.748 1.00 48.97 ? 132 TYR A CA 1 ATOM 1042 C C . TYR A 1 132 ? 8.031 4.295 53.237 1.00 46.95 ? 132 TYR A C 1 ATOM 1043 O O . TYR A 1 132 ? 8.856 3.805 54.017 1.00 46.66 ? 132 TYR A O 1 ATOM 1044 C CB . TYR A 1 132 ? 6.063 4.722 54.849 1.00 50.35 ? 132 TYR A CB 1 ATOM 1045 C CG . TYR A 1 132 ? 4.986 5.723 55.263 1.00 53.06 ? 132 TYR A CG 1 ATOM 1046 C CD1 . TYR A 1 132 ? 3.658 5.538 54.922 1.00 56.26 ? 132 TYR A CD1 1 ATOM 1047 C CD2 . TYR A 1 132 ? 5.319 6.873 55.971 1.00 57.39 ? 132 TYR A CD2 1 ATOM 1048 C CE1 . TYR A 1 132 ? 2.674 6.469 55.294 1.00 59.46 ? 132 TYR A CE1 1 ATOM 1049 C CE2 . TYR A 1 132 ? 4.354 7.808 56.344 1.00 59.84 ? 132 TYR A CE2 1 ATOM 1050 C CZ . TYR A 1 132 ? 3.034 7.602 56.007 1.00 61.15 ? 132 TYR A CZ 1 ATOM 1051 O OH . TYR A 1 132 ? 2.086 8.543 56.381 1.00 64.67 ? 132 TYR A OH 1 ATOM 1052 N N . CYS A 1 133 ? 8.018 4.021 51.933 1.00 44.35 ? 133 CYS A N 1 ATOM 1053 C CA . CYS A 1 133 ? 8.984 3.099 51.313 1.00 41.80 ? 133 CYS A CA 1 ATOM 1054 C C . CYS A 1 133 ? 9.038 1.741 51.974 1.00 41.71 ? 133 CYS A C 1 ATOM 1055 O O . CYS A 1 133 ? 10.104 1.144 52.105 1.00 41.82 ? 133 CYS A O 1 ATOM 1056 C CB . CYS A 1 133 ? 10.393 3.704 51.308 1.00 40.73 ? 133 CYS A CB 1 ATOM 1057 S SG . CYS A 1 133 ? 10.512 5.206 50.322 1.00 36.66 ? 133 CYS A SG 1 ATOM 1058 N N . ILE A 1 134 ? 7.895 1.241 52.407 1.00 41.68 ? 134 ILE A N 1 ATOM 1059 C CA . ILE A 1 134 ? 7.888 -0.046 53.084 1.00 41.39 ? 134 ILE A CA 1 ATOM 1060 C C . ILE A 1 134 ? 7.648 -1.157 52.082 1.00 41.04 ? 134 ILE A C 1 ATOM 1061 O O . ILE A 1 134 ? 6.577 -1.252 51.451 1.00 41.09 ? 134 ILE A O 1 ATOM 1062 C CB . ILE A 1 134 ? 6.853 -0.074 54.238 1.00 41.73 ? 134 ILE A CB 1 ATOM 1063 C CG1 . ILE A 1 134 ? 7.332 0.800 55.402 1.00 41.24 ? 134 ILE A CG1 1 ATOM 1064 C CG2 . ILE A 1 134 ? 6.644 -1.484 54.723 1.00 41.10 ? 134 ILE A CG2 1 ATOM 1065 C CD1 . ILE A 1 134 ? 6.198 1.408 56.185 1.00 41.19 ? 134 ILE A CD1 1 ATOM 1066 N N . GLN A 1 135 ? 8.677 -1.975 51.925 1.00 40.14 ? 135 GLN A N 1 ATOM 1067 C CA . GLN A 1 135 ? 8.626 -3.104 51.013 1.00 39.31 ? 135 GLN A CA 1 ATOM 1068 C C . GLN A 1 135 ? 7.647 -4.129 51.521 1.00 38.56 ? 135 GLN A C 1 ATOM 1069 O O . GLN A 1 135 ? 7.643 -4.480 52.694 1.00 37.88 ? 135 GLN A O 1 ATOM 1070 C CB . GLN A 1 135 ? 10.008 -3.752 50.853 1.00 39.23 ? 135 GLN A CB 1 ATOM 1071 C CG . GLN A 1 135 ? 10.071 -4.731 49.711 1.00 39.90 ? 135 GLN A CG 1 ATOM 1072 C CD . GLN A 1 135 ? 11.326 -5.583 49.721 1.00 40.90 ? 135 GLN A CD 1 ATOM 1073 O OE1 . GLN A 1 135 ? 12.296 -5.292 49.031 1.00 42.01 ? 135 GLN A OE1 1 ATOM 1074 N NE2 . GLN A 1 135 ? 11.299 -6.644 50.486 1.00 41.71 ? 135 GLN A NE2 1 ATOM 1075 N N . GLY A 1 136 ? 6.815 -4.610 50.615 1.00 38.25 ? 136 GLY A N 1 ATOM 1076 C CA . GLY A 1 136 ? 5.848 -5.601 50.973 1.00 37.70 ? 136 GLY A CA 1 ATOM 1077 C C . GLY A 1 136 ? 4.784 -5.769 49.931 1.00 38.01 ? 136 GLY A C 1 ATOM 1078 O O . GLY A 1 136 ? 4.398 -4.829 49.232 1.00 37.35 ? 136 GLY A O 1 ATOM 1079 N N . ASP A 1 137 ? 4.288 -6.998 49.851 1.00 38.84 ? 137 ASP A N 1 ATOM 1080 C CA . ASP A 1 137 ? 3.301 -7.338 48.870 1.00 39.21 ? 137 ASP A CA 1 ATOM 1081 C C . ASP A 1 137 ? 3.797 -6.799 47.554 1.00 38.67 ? 137 ASP A C 1 ATOM 1082 O O . ASP A 1 137 ? 4.961 -6.950 47.205 1.00 38.56 ? 137 ASP A O 1 ATOM 1083 C CB . ASP A 1 137 ? 1.972 -6.709 49.240 1.00 39.98 ? 137 ASP A CB 1 ATOM 1084 C CG . ASP A 1 137 ? 1.366 -7.338 50.472 1.00 43.27 ? 137 ASP A CG 1 ATOM 1085 O OD1 . ASP A 1 137 ? 1.639 -8.548 50.694 1.00 47.53 ? 137 ASP A OD1 1 ATOM 1086 O OD2 . ASP A 1 137 ? 0.613 -6.703 51.263 1.00 46.03 ? 137 ASP A OD2 1 ATOM 1087 N N . ASN A 1 138 ? 2.923 -6.130 46.838 1.00 38.06 ? 138 ASN A N 1 ATOM 1088 C CA . ASN A 1 138 ? 3.301 -5.631 45.547 1.00 37.65 ? 138 ASN A CA 1 ATOM 1089 C C . ASN A 1 138 ? 4.049 -4.319 45.566 1.00 36.33 ? 138 ASN A C 1 ATOM 1090 O O . ASN A 1 138 ? 4.275 -3.731 44.516 1.00 37.18 ? 138 ASN A O 1 ATOM 1091 C CB . ASN A 1 138 ? 2.083 -5.611 44.637 1.00 38.15 ? 138 ASN A CB 1 ATOM 1092 C CG . ASN A 1 138 ? 1.452 -6.995 44.515 1.00 42.29 ? 138 ASN A CG 1 ATOM 1093 O OD1 . ASN A 1 138 ? 2.088 -7.947 44.011 1.00 45.52 ? 138 ASN A OD1 1 ATOM 1094 N ND2 . ASN A 1 138 ? 0.206 -7.134 45.009 1.00 45.66 ? 138 ASN A ND2 1 ATOM 1095 N N . CYS A 1 139 ? 4.434 -3.852 46.749 1.00 34.34 ? 139 CYS A N 1 ATOM 1096 C CA . CYS A 1 139 ? 5.266 -2.656 46.832 1.00 32.71 ? 139 CYS A CA 1 ATOM 1097 C C . CYS A 1 139 ? 6.669 -3.173 46.962 1.00 30.70 ? 139 CYS A C 1 ATOM 1098 O O . CYS A 1 139 ? 6.964 -3.967 47.844 1.00 31.23 ? 139 CYS A O 1 ATOM 1099 C CB . CYS A 1 139 ? 4.898 -1.746 48.003 1.00 33.54 ? 139 CYS A CB 1 ATOM 1100 S SG . CYS A 1 139 ? 6.061 -0.357 48.228 1.00 37.83 ? 139 CYS A SG 1 ATOM 1101 N N . PHE A 1 140 ? 7.554 -2.744 46.075 1.00 28.61 ? 140 PHE A N 1 ATOM 1102 C CA . PHE A 1 140 ? 8.911 -3.307 46.000 1.00 26.18 ? 140 PHE A CA 1 ATOM 1103 C C . PHE A 1 140 ? 9.862 -2.187 45.583 1.00 25.17 ? 140 PHE A C 1 ATOM 1104 O O . PHE A 1 140 ? 10.398 -2.175 44.464 1.00 25.99 ? 140 PHE A O 1 ATOM 1105 C CB . PHE A 1 140 ? 8.900 -4.418 44.957 1.00 25.48 ? 140 PHE A CB 1 ATOM 1106 C CG . PHE A 1 140 ? 10.248 -4.976 44.643 1.00 25.08 ? 140 PHE A CG 1 ATOM 1107 C CD1 . PHE A 1 140 ? 11.074 -5.440 45.641 1.00 24.56 ? 140 PHE A CD1 1 ATOM 1108 C CD2 . PHE A 1 140 ? 10.690 -5.044 43.346 1.00 24.11 ? 140 PHE A CD2 1 ATOM 1109 C CE1 . PHE A 1 140 ? 12.315 -5.941 45.340 1.00 24.51 ? 140 PHE A CE1 1 ATOM 1110 C CE2 . PHE A 1 140 ? 11.931 -5.570 43.047 1.00 23.33 ? 140 PHE A CE2 1 ATOM 1111 C CZ . PHE A 1 140 ? 12.743 -6.007 44.033 1.00 22.75 ? 140 PHE A CZ 1 ATOM 1112 N N . PRO A 1 141 ? 10.096 -1.260 46.505 1.00 23.35 ? 141 PRO A N 1 ATOM 1113 C CA . PRO A 1 141 ? 10.568 0.075 46.133 1.00 21.97 ? 141 PRO A CA 1 ATOM 1114 C C . PRO A 1 141 ? 12.014 0.188 45.802 1.00 21.06 ? 141 PRO A C 1 ATOM 1115 O O . PRO A 1 141 ? 12.761 -0.634 46.226 1.00 19.76 ? 141 PRO A O 1 ATOM 1116 C CB . PRO A 1 141 ? 10.201 0.913 47.346 1.00 21.96 ? 141 PRO A CB 1 ATOM 1117 C CG . PRO A 1 141 ? 10.254 -0.058 48.478 1.00 22.02 ? 141 PRO A CG 1 ATOM 1118 C CD . PRO A 1 141 ? 9.912 -1.405 47.954 1.00 22.75 ? 141 PRO A CD 1 ATOM 1119 N N . ILE A 1 142 ? 12.380 1.197 45.016 1.00 21.54 ? 142 ILE A N 1 ATOM 1120 C CA . ILE A 1 142 ? 13.755 1.378 44.612 1.00 21.72 ? 142 ILE A CA 1 ATOM 1121 C C . ILE A 1 142 ? 14.350 2.324 45.615 1.00 22.39 ? 142 ILE A C 1 ATOM 1122 O O . ILE A 1 142 ? 14.052 3.519 45.604 1.00 22.19 ? 142 ILE A O 1 ATOM 1123 C CB . ILE A 1 142 ? 13.835 1.923 43.164 1.00 22.07 ? 142 ILE A CB 1 ATOM 1124 C CG1 . ILE A 1 142 ? 13.489 0.816 42.148 1.00 21.38 ? 142 ILE A CG1 1 ATOM 1125 C CG2 . ILE A 1 142 ? 15.212 2.488 42.841 1.00 20.62 ? 142 ILE A CG2 1 ATOM 1126 C CD1 . ILE A 1 142 ? 12.814 1.319 40.853 1.00 18.09 ? 142 ILE A CD1 1 ATOM 1127 N N . MET A 1 143 ? 15.140 1.747 46.520 1.00 23.15 ? 143 MET A N 1 ATOM 1128 C CA . MET A 1 143 ? 15.851 2.477 47.551 1.00 24.57 ? 143 MET A CA 1 ATOM 1129 C C . MET A 1 143 ? 16.982 3.263 46.941 1.00 25.32 ? 143 MET A C 1 ATOM 1130 O O . MET A 1 143 ? 17.586 2.808 45.975 1.00 26.37 ? 143 MET A O 1 ATOM 1131 C CB . MET A 1 143 ? 16.441 1.509 48.565 1.00 24.84 ? 143 MET A CB 1 ATOM 1132 C CG . MET A 1 143 ? 15.416 0.612 49.217 1.00 25.68 ? 143 MET A CG 1 ATOM 1133 S SD . MET A 1 143 ? 14.022 1.552 49.844 1.00 31.62 ? 143 MET A SD 1 ATOM 1134 C CE . MET A 1 143 ? 14.899 2.840 50.763 1.00 28.00 ? 143 MET A CE 1 ATOM 1135 N N . PHE A 1 144 ? 17.287 4.425 47.509 1.00 25.75 ? 144 PHE A N 1 ATOM 1136 C CA . PHE A 1 144 ? 18.400 5.239 47.051 1.00 26.10 ? 144 PHE A CA 1 ATOM 1137 C C . PHE A 1 144 ? 19.691 4.907 47.762 1.00 27.33 ? 144 PHE A C 1 ATOM 1138 O O . PHE A 1 144 ? 19.678 4.490 48.905 1.00 27.17 ? 144 PHE A O 1 ATOM 1139 C CB . PHE A 1 144 ? 18.128 6.711 47.318 1.00 25.87 ? 144 PHE A CB 1 ATOM 1140 C CG . PHE A 1 144 ? 17.027 7.296 46.478 1.00 26.07 ? 144 PHE A CG 1 ATOM 1141 C CD1 . PHE A 1 144 ? 16.198 8.287 46.983 1.00 24.35 ? 144 PHE A CD1 1 ATOM 1142 C CD2 . PHE A 1 144 ? 16.810 6.853 45.175 1.00 26.84 ? 144 PHE A CD2 1 ATOM 1143 C CE1 . PHE A 1 144 ? 15.191 8.814 46.230 1.00 21.91 ? 144 PHE A CE1 1 ATOM 1144 C CE2 . PHE A 1 144 ? 15.781 7.398 44.413 1.00 23.52 ? 144 PHE A CE2 1 ATOM 1145 C CZ . PHE A 1 144 ? 14.991 8.371 44.946 1.00 22.01 ? 144 PHE A CZ 1 ATOM 1146 N N . PRO A 1 145 ? 20.772 4.880 46.997 1.00 29.11 ? 145 PRO A N 1 ATOM 1147 C CA . PRO A 1 145 ? 22.156 4.821 47.446 1.00 29.72 ? 145 PRO A CA 1 ATOM 1148 C C . PRO A 1 145 ? 22.577 5.905 48.388 1.00 31.30 ? 145 PRO A C 1 ATOM 1149 O O . PRO A 1 145 ? 21.972 6.974 48.367 1.00 31.07 ? 145 PRO A O 1 ATOM 1150 C CB . PRO A 1 145 ? 22.928 4.952 46.141 1.00 28.80 ? 145 PRO A CB 1 ATOM 1151 C CG . PRO A 1 145 ? 22.092 4.331 45.175 1.00 29.34 ? 145 PRO A CG 1 ATOM 1152 C CD . PRO A 1 145 ? 20.665 4.372 45.622 1.00 29.82 ? 145 PRO A CD 1 ATOM 1153 N N . LYS A 1 146 ? 23.585 5.637 49.222 1.00 33.04 ? 146 LYS A N 1 ATOM 1154 C CA . LYS A 1 146 ? 24.168 6.742 49.965 1.00 34.91 ? 146 LYS A CA 1 ATOM 1155 C C . LYS A 1 146 ? 24.957 7.559 48.906 1.00 35.62 ? 146 LYS A C 1 ATOM 1156 O O . LYS A 1 146 ? 25.552 6.988 47.975 1.00 35.62 ? 146 LYS A O 1 ATOM 1157 C CB . LYS A 1 146 ? 25.005 6.264 51.143 1.00 35.46 ? 146 LYS A CB 1 ATOM 1158 C CG . LYS A 1 146 ? 26.499 6.327 50.927 1.00 37.79 ? 146 LYS A CG 1 ATOM 1159 C CD . LYS A 1 146 ? 27.173 6.946 52.144 1.00 42.59 ? 146 LYS A CD 1 ATOM 1160 C CE . LYS A 1 146 ? 28.473 7.628 51.778 1.00 44.27 ? 146 LYS A CE 1 ATOM 1161 N NZ . LYS A 1 146 ? 29.462 7.531 52.897 1.00 47.43 ? 146 LYS A NZ 1 ATOM 1162 N N . ASN A 1 147 ? 24.903 8.886 49.031 1.00 36.15 ? 147 ASN A N 1 ATOM 1163 C CA . ASN A 1 147 ? 25.471 9.872 48.064 1.00 37.02 ? 147 ASN A CA 1 ATOM 1164 C C . ASN A 1 147 ? 24.550 10.196 46.892 1.00 36.23 ? 147 ASN A C 1 ATOM 1165 O O . ASN A 1 147 ? 24.934 10.979 46.028 1.00 36.68 ? 147 ASN A O 1 ATOM 1166 C CB . ASN A 1 147 ? 26.885 9.562 47.521 1.00 37.62 ? 147 ASN A CB 1 ATOM 1167 C CG . ASN A 1 147 ? 27.822 9.086 48.594 1.00 40.34 ? 147 ASN A CG 1 ATOM 1168 O OD1 . ASN A 1 147 ? 28.330 7.955 48.532 1.00 43.87 ? 147 ASN A OD1 1 ATOM 1169 N ND2 . ASN A 1 147 ? 28.049 9.927 49.601 1.00 41.28 ? 147 ASN A ND2 1 ATOM 1170 N N . ASP A 1 148 ? 23.368 9.584 46.841 1.00 34.83 ? 148 ASP A N 1 ATOM 1171 C CA . ASP A 1 148 ? 22.431 9.915 45.781 1.00 33.29 ? 148 ASP A CA 1 ATOM 1172 C C . ASP A 1 148 ? 21.797 11.239 46.082 1.00 32.91 ? 148 ASP A C 1 ATOM 1173 O O . ASP A 1 148 ? 21.259 11.416 47.157 1.00 32.98 ? 148 ASP A O 1 ATOM 1174 C CB . ASP A 1 148 ? 21.313 8.891 45.682 1.00 33.06 ? 148 ASP A CB 1 ATOM 1175 C CG . ASP A 1 148 ? 20.607 8.931 44.344 1.00 31.90 ? 148 ASP A CG 1 ATOM 1176 O OD1 . ASP A 1 148 ? 19.979 9.948 43.987 1.00 28.38 ? 148 ASP A OD1 1 ATOM 1177 O OD2 . ASP A 1 148 ? 20.657 7.962 43.570 1.00 35.46 ? 148 ASP A OD2 1 ATOM 1178 N N . PRO A 1 149 ? 21.994 12.231 45.234 1.00 32.39 ? 149 PRO A N 1 ATOM 1179 C CA . PRO A 1 149 ? 21.298 13.496 45.373 1.00 32.01 ? 149 PRO A CA 1 ATOM 1180 C C . PRO A 1 149 ? 19.798 13.406 45.637 1.00 31.96 ? 149 PRO A C 1 ATOM 1181 O O . PRO A 1 149 ? 19.326 14.192 46.472 1.00 33.01 ? 149 PRO A O 1 ATOM 1182 C CB . PRO A 1 149 ? 21.680 14.232 44.102 1.00 32.00 ? 149 PRO A CB 1 ATOM 1183 C CG . PRO A 1 149 ? 23.083 13.788 43.882 1.00 32.47 ? 149 PRO A CG 1 ATOM 1184 C CD . PRO A 1 149 ? 23.192 12.384 44.403 1.00 32.42 ? 149 PRO A CD 1 ATOM 1185 N N . LYS A 1 150 ? 19.080 12.476 45.010 1.00 30.63 ? 150 LYS A N 1 ATOM 1186 C CA . LYS A 1 150 ? 17.635 12.387 45.180 1.00 30.19 ? 150 LYS A CA 1 ATOM 1187 C C . LYS A 1 150 ? 17.182 12.239 46.645 1.00 30.56 ? 150 LYS A C 1 ATOM 1188 O O . LYS A 1 150 ? 16.026 12.520 46.999 1.00 29.43 ? 150 LYS A O 1 ATOM 1189 C CB . LYS A 1 150 ? 17.102 11.244 44.353 1.00 30.59 ? 150 LYS A CB 1 ATOM 1190 C CG . LYS A 1 150 ? 17.364 11.395 42.879 1.00 30.14 ? 150 LYS A CG 1 ATOM 1191 C CD . LYS A 1 150 ? 16.157 11.936 42.166 1.00 29.04 ? 150 LYS A CD 1 ATOM 1192 C CE . LYS A 1 150 ? 16.283 11.777 40.657 1.00 26.46 ? 150 LYS A CE 1 ATOM 1193 N NZ . LYS A 1 150 ? 15.009 12.065 39.970 1.00 25.31 ? 150 LYS A NZ 1 ATOM 1194 N N . LEU A 1 151 ? 18.108 11.788 47.487 1.00 31.21 ? 151 LEU A N 1 ATOM 1195 C CA . LEU A 1 151 ? 17.893 11.669 48.918 1.00 31.90 ? 151 LEU A CA 1 ATOM 1196 C C . LEU A 1 151 ? 17.582 13.031 49.514 1.00 32.65 ? 151 LEU A C 1 ATOM 1197 O O . LEU A 1 151 ? 16.646 13.196 50.306 1.00 32.45 ? 151 LEU A O 1 ATOM 1198 C CB . LEU A 1 151 ? 19.159 11.130 49.565 1.00 31.33 ? 151 LEU A CB 1 ATOM 1199 C CG . LEU A 1 151 ? 19.125 9.645 49.916 1.00 32.62 ? 151 LEU A CG 1 ATOM 1200 C CD1 . LEU A 1 151 ? 20.495 9.184 50.339 1.00 33.26 ? 151 LEU A CD1 1 ATOM 1201 C CD2 . LEU A 1 151 ? 18.080 9.330 51.008 1.00 32.35 ? 151 LEU A CD2 1 ATOM 1202 N N . LYS A 1 152 ? 18.400 14.001 49.135 1.00 33.64 ? 152 LYS A N 1 ATOM 1203 C CA . LYS A 1 152 ? 18.263 15.345 49.644 1.00 35.25 ? 152 LYS A CA 1 ATOM 1204 C C . LYS A 1 152 ? 16.987 15.985 49.160 1.00 35.91 ? 152 LYS A C 1 ATOM 1205 O O . LYS A 1 152 ? 16.381 16.811 49.844 1.00 37.46 ? 152 LYS A O 1 ATOM 1206 C CB . LYS A 1 152 ? 19.446 16.209 49.197 1.00 35.15 ? 152 LYS A CB 1 ATOM 1207 C CG . LYS A 1 152 ? 20.771 15.844 49.870 1.00 36.38 ? 152 LYS A CG 1 ATOM 1208 C CD . LYS A 1 152 ? 21.956 16.493 49.172 1.00 37.60 ? 152 LYS A CD 1 ATOM 1209 C CE . LYS A 1 152 ? 23.280 16.080 49.843 1.00 39.59 ? 152 LYS A CE 1 ATOM 1210 N NZ . LYS A 1 152 ? 24.481 16.948 49.474 1.00 41.91 ? 152 LYS A NZ 1 ATOM 1211 N N . THR A 1 153 ? 16.532 15.557 48.008 1.00 36.16 ? 153 THR A N 1 ATOM 1212 C CA . THR A 1 153 ? 15.485 16.289 47.331 1.00 36.11 ? 153 THR A CA 1 ATOM 1213 C C . THR A 1 153 ? 14.135 15.617 47.131 1.00 36.34 ? 153 THR A C 1 ATOM 1214 O O . THR A 1 153 ? 13.134 16.312 46.945 1.00 36.51 ? 153 THR A O 1 ATOM 1215 C CB . THR A 1 153 ? 16.073 16.709 45.997 1.00 35.85 ? 153 THR A CB 1 ATOM 1216 O OG1 . THR A 1 153 ? 16.278 18.122 46.035 1.00 36.61 ? 153 THR A OG1 1 ATOM 1217 C CG2 . THR A 1 153 ? 15.117 16.488 44.864 1.00 35.84 ? 153 THR A CG2 1 ATOM 1218 N N . GLN A 1 154 ? 14.100 14.286 47.206 1.00 36.40 ? 154 GLN A N 1 ATOM 1219 C CA . GLN A 1 154 ? 12.904 13.562 46.842 1.00 36.83 ? 154 GLN A CA 1 ATOM 1220 C C . GLN A 1 154 ? 12.354 12.702 47.937 1.00 36.74 ? 154 GLN A C 1 ATOM 1221 O O . GLN A 1 154 ? 11.139 12.599 48.089 1.00 38.05 ? 154 GLN A O 1 ATOM 1222 C CB . GLN A 1 154 ? 13.172 12.663 45.628 1.00 37.47 ? 154 GLN A CB 1 ATOM 1223 C CG . GLN A 1 154 ? 13.106 13.369 44.292 1.00 38.63 ? 154 GLN A CG 1 ATOM 1224 C CD . GLN A 1 154 ? 12.872 12.424 43.134 1.00 40.72 ? 154 GLN A CD 1 ATOM 1225 O OE1 . GLN A 1 154 ? 13.216 12.744 42.017 1.00 44.17 ? 154 GLN A OE1 1 ATOM 1226 N NE2 . GLN A 1 154 ? 12.279 11.273 43.395 1.00 41.76 ? 154 GLN A NE2 1 ATOM 1227 N N . GLY A 1 155 ? 13.228 12.049 48.677 1.00 35.75 ? 155 GLY A N 1 ATOM 1228 C CA . GLY A 1 155 ? 12.773 11.152 49.708 1.00 34.79 ? 155 GLY A CA 1 ATOM 1229 C C . GLY A 1 155 ? 13.728 9.990 49.898 1.00 34.53 ? 155 GLY A C 1 ATOM 1230 O O . GLY A 1 155 ? 14.950 10.157 49.782 1.00 34.16 ? 155 GLY A O 1 ATOM 1231 N N . LYS A 1 156 ? 13.186 8.805 50.188 1.00 33.84 ? 156 LYS A N 1 ATOM 1232 C CA . LYS A 1 156 ? 14.034 7.668 50.516 1.00 32.90 ? 156 LYS A CA 1 ATOM 1233 C C . LYS A 1 156 ? 14.088 6.586 49.460 1.00 31.40 ? 156 LYS A C 1 ATOM 1234 O O . LYS A 1 156 ? 14.977 5.741 49.476 1.00 31.23 ? 156 LYS A O 1 ATOM 1235 C CB . LYS A 1 156 ? 13.607 7.073 51.850 1.00 33.69 ? 156 LYS A CB 1 ATOM 1236 C CG . LYS A 1 156 ? 14.016 7.905 53.048 1.00 36.82 ? 156 LYS A CG 1 ATOM 1237 C CD . LYS A 1 156 ? 15.388 7.493 53.569 1.00 40.88 ? 156 LYS A CD 1 ATOM 1238 C CE . LYS A 1 156 ? 15.838 8.369 54.742 1.00 43.02 ? 156 LYS A CE 1 ATOM 1239 N NZ . LYS A 1 156 ? 16.648 7.582 55.735 1.00 45.95 ? 156 LYS A NZ 1 ATOM 1240 N N . CYS A 1 157 ? 13.142 6.610 48.537 1.00 29.69 ? 157 CYS A N 1 ATOM 1241 C CA . CYS A 1 157 ? 13.062 5.577 47.537 1.00 28.12 ? 157 CYS A CA 1 ATOM 1242 C C . CYS A 1 157 ? 12.190 6.075 46.447 1.00 26.90 ? 157 CYS A C 1 ATOM 1243 O O . CYS A 1 157 ? 11.550 7.100 46.581 1.00 25.68 ? 157 CYS A O 1 ATOM 1244 C CB . CYS A 1 157 ? 12.329 4.366 48.101 1.00 28.64 ? 157 CYS A CB 1 ATOM 1245 S SG . CYS A 1 157 ? 10.571 4.747 48.357 1.00 29.14 ? 157 CYS A SG 1 ATOM 1246 N N . MET A 1 158 ? 12.152 5.320 45.353 1.00 25.93 ? 158 MET A N 1 ATOM 1247 C CA . MET A 1 158 ? 11.158 5.579 44.342 1.00 24.58 ? 158 MET A CA 1 ATOM 1248 C C . MET A 1 158 ? 10.143 4.437 44.440 1.00 24.04 ? 158 MET A C 1 ATOM 1249 O O . MET A 1 158 ? 10.524 3.265 44.569 1.00 24.48 ? 158 MET A O 1 ATOM 1250 C CB . MET A 1 158 ? 11.806 5.592 42.989 1.00 24.11 ? 158 MET A CB 1 ATOM 1251 C CG . MET A 1 158 ? 12.591 6.807 42.696 1.00 25.47 ? 158 MET A CG 1 ATOM 1252 S SD . MET A 1 158 ? 13.302 6.695 41.041 1.00 28.12 ? 158 MET A SD 1 ATOM 1253 C CE . MET A 1 158 ? 14.853 5.976 41.428 1.00 27.73 ? 158 MET A CE 1 ATOM 1254 N N . PRO A 1 159 ? 8.862 4.765 44.438 1.00 23.05 ? 159 PRO A N 1 ATOM 1255 C CA . PRO A 1 159 ? 7.810 3.746 44.356 1.00 22.74 ? 159 PRO A CA 1 ATOM 1256 C C . PRO A 1 159 ? 7.902 2.907 43.066 1.00 22.23 ? 159 PRO A C 1 ATOM 1257 O O . PRO A 1 159 ? 8.185 3.384 41.979 1.00 21.44 ? 159 PRO A O 1 ATOM 1258 C CB . PRO A 1 159 ? 6.508 4.567 44.365 1.00 22.67 ? 159 PRO A CB 1 ATOM 1259 C CG . PRO A 1 159 ? 6.917 5.950 43.981 1.00 23.27 ? 159 PRO A CG 1 ATOM 1260 C CD . PRO A 1 159 ? 8.315 6.119 44.567 1.00 23.32 ? 159 PRO A CD 1 ATOM 1261 N N . PHE A 1 160 ? 7.623 1.628 43.227 1.00 22.27 ? 160 PHE A N 1 ATOM 1262 C CA . PHE A 1 160 ? 7.675 0.663 42.162 1.00 22.40 ? 160 PHE A CA 1 ATOM 1263 C C . PHE A 1 160 ? 6.730 -0.432 42.591 1.00 22.96 ? 160 PHE A C 1 ATOM 1264 O O . PHE A 1 160 ? 6.685 -0.807 43.762 1.00 23.13 ? 160 PHE A O 1 ATOM 1265 C CB . PHE A 1 160 ? 9.075 0.102 42.065 1.00 22.15 ? 160 PHE A CB 1 ATOM 1266 C CG . PHE A 1 160 ? 9.241 -0.951 41.038 1.00 22.26 ? 160 PHE A CG 1 ATOM 1267 C CD1 . PHE A 1 160 ? 8.934 -2.283 41.317 1.00 23.89 ? 160 PHE A CD1 1 ATOM 1268 C CD2 . PHE A 1 160 ? 9.756 -0.637 39.809 1.00 22.30 ? 160 PHE A CD2 1 ATOM 1269 C CE1 . PHE A 1 160 ? 9.128 -3.264 40.375 1.00 22.90 ? 160 PHE A CE1 1 ATOM 1270 C CE2 . PHE A 1 160 ? 9.952 -1.614 38.857 1.00 23.43 ? 160 PHE A CE2 1 ATOM 1271 C CZ . PHE A 1 160 ? 9.645 -2.929 39.142 1.00 23.15 ? 160 PHE A CZ 1 ATOM 1272 N N . PHE A 1 161 ? 5.984 -0.955 41.640 1.00 23.28 ? 161 PHE A N 1 ATOM 1273 C CA . PHE A 1 161 ? 4.998 -1.953 41.942 1.00 23.92 ? 161 PHE A CA 1 ATOM 1274 C C . PHE A 1 161 ? 5.187 -3.170 41.083 1.00 23.27 ? 161 PHE A C 1 ATOM 1275 O O . PHE A 1 161 ? 5.387 -3.047 39.881 1.00 23.73 ? 161 PHE A O 1 ATOM 1276 C CB . PHE A 1 161 ? 3.633 -1.344 41.725 1.00 24.71 ? 161 PHE A CB 1 ATOM 1277 C CG . PHE A 1 161 ? 3.274 -0.366 42.780 1.00 28.62 ? 161 PHE A CG 1 ATOM 1278 C CD1 . PHE A 1 161 ? 3.413 0.994 42.560 1.00 28.91 ? 161 PHE A CD1 1 ATOM 1279 C CD2 . PHE A 1 161 ? 2.853 -0.814 44.027 1.00 32.47 ? 161 PHE A CD2 1 ATOM 1280 C CE1 . PHE A 1 161 ? 3.105 1.872 43.526 1.00 30.70 ? 161 PHE A CE1 1 ATOM 1281 C CE2 . PHE A 1 161 ? 2.533 0.101 45.032 1.00 34.29 ? 161 PHE A CE2 1 ATOM 1282 C CZ . PHE A 1 161 ? 2.666 1.434 44.780 1.00 32.59 ? 161 PHE A CZ 1 ATOM 1283 N N . ARG A 1 162 ? 5.113 -4.343 41.690 1.00 22.19 ? 162 ARG A N 1 ATOM 1284 C CA . ARG A 1 162 ? 5.367 -5.545 40.939 1.00 21.99 ? 162 ARG A CA 1 ATOM 1285 C C . ARG A 1 162 ? 4.352 -5.709 39.847 1.00 22.51 ? 162 ARG A C 1 ATOM 1286 O O . ARG A 1 162 ? 3.202 -5.323 39.984 1.00 21.66 ? 162 ARG A O 1 ATOM 1287 C CB . ARG A 1 162 ? 5.366 -6.767 41.829 1.00 22.37 ? 162 ARG A CB 1 ATOM 1288 C CG . ARG A 1 162 ? 6.332 -6.724 42.946 1.00 20.72 ? 162 ARG A CG 1 ATOM 1289 C CD . ARG A 1 162 ? 6.554 -8.067 43.501 1.00 23.04 ? 162 ARG A CD 1 ATOM 1290 N NE . ARG A 1 162 ? 7.366 -8.897 42.615 1.00 24.18 ? 162 ARG A NE 1 ATOM 1291 C CZ . ARG A 1 162 ? 7.469 -10.206 42.749 1.00 21.78 ? 162 ARG A CZ 1 ATOM 1292 N NH1 . ARG A 1 162 ? 6.812 -10.810 43.717 1.00 23.11 ? 162 ARG A NH1 1 ATOM 1293 N NH2 . ARG A 1 162 ? 8.235 -10.907 41.941 1.00 18.69 ? 162 ARG A NH2 1 ATOM 1294 N N . ALA A 1 163 ? 4.815 -6.279 38.751 1.00 23.71 ? 163 ALA A N 1 ATOM 1295 C CA . ALA A 1 163 ? 4.004 -6.493 37.576 1.00 25.61 ? 163 ALA A CA 1 ATOM 1296 C C . ALA A 1 163 ? 2.909 -7.535 37.777 1.00 27.44 ? 163 ALA A C 1 ATOM 1297 O O . ALA A 1 163 ? 2.987 -8.391 38.649 1.00 26.80 ? 163 ALA A O 1 ATOM 1298 C CB . ALA A 1 163 ? 4.897 -6.891 36.408 1.00 25.47 ? 163 ALA A CB 1 ATOM 1299 N N . GLY A 1 164 ? 1.882 -7.463 36.943 1.00 30.05 ? 164 GLY A N 1 ATOM 1300 C CA . GLY A 1 164 ? 0.782 -8.401 37.040 1.00 32.98 ? 164 GLY A CA 1 ATOM 1301 C C . GLY A 1 164 ? 1.212 -9.795 36.668 1.00 35.32 ? 164 GLY A C 1 ATOM 1302 O O . GLY A 1 164 ? 2.133 -9.981 35.870 1.00 35.21 ? 164 GLY A O 1 ATOM 1303 N N . PHE A 1 165 ? 0.536 -10.796 37.250 1.00 37.83 ? 165 PHE A N 1 ATOM 1304 C CA . PHE A 1 165 ? 0.807 -12.221 37.027 1.00 40.27 ? 165 PHE A CA 1 ATOM 1305 C C . PHE A 1 165 ? -0.475 -13.008 36.731 1.00 42.61 ? 165 PHE A C 1 ATOM 1306 O O . PHE A 1 165 ? -1.554 -12.578 37.117 1.00 42.87 ? 165 PHE A O 1 ATOM 1307 C CB . PHE A 1 165 ? 1.581 -12.799 38.199 1.00 39.46 ? 165 PHE A CB 1 ATOM 1308 C CG . PHE A 1 165 ? 0.871 -12.704 39.509 1.00 39.62 ? 165 PHE A CG 1 ATOM 1309 C CD1 . PHE A 1 165 ? 0.792 -11.503 40.204 1.00 38.65 ? 165 PHE A CD1 1 ATOM 1310 C CD2 . PHE A 1 165 ? 0.314 -13.839 40.078 1.00 38.06 ? 165 PHE A CD2 1 ATOM 1311 C CE1 . PHE A 1 165 ? 0.129 -11.443 41.419 1.00 38.73 ? 165 PHE A CE1 1 ATOM 1312 C CE2 . PHE A 1 165 ? -0.332 -13.776 41.284 1.00 38.08 ? 165 PHE A CE2 1 ATOM 1313 C CZ . PHE A 1 165 ? -0.431 -12.575 41.957 1.00 37.35 ? 165 PHE A CZ 1 ATOM 1314 N N . VAL A 1 166 ? -0.321 -14.163 36.062 1.00 46.14 ? 166 VAL A N 1 ATOM 1315 C CA . VAL A 1 166 ? -1.445 -15.005 35.634 1.00 50.15 ? 166 VAL A CA 1 ATOM 1316 C C . VAL A 1 166 ? -2.211 -15.708 36.679 1.00 53.42 ? 166 VAL A C 1 ATOM 1317 O O . VAL A 1 166 ? -1.827 -15.873 37.832 1.00 53.49 ? 166 VAL A O 1 ATOM 1318 C CB . VAL A 1 166 ? -1.022 -16.073 34.572 1.00 49.39 ? 166 VAL A CB 1 ATOM 1319 C CG1 . VAL A 1 166 ? -0.862 -15.439 33.196 1.00 49.99 ? 166 VAL A CG1 1 ATOM 1320 C CG2 . VAL A 1 166 ? 0.281 -16.755 34.975 1.00 49.44 ? 166 VAL A CG2 1 ATOM 1321 N N . CYS A 1 167 ? -3.333 -16.126 36.170 1.00 58.12 ? 167 CYS A N 1 ATOM 1322 C CA . CYS A 1 167 ? -4.307 -16.559 37.019 1.00 62.84 ? 167 CYS A CA 1 ATOM 1323 C C . CYS A 1 167 ? -4.699 -15.231 37.743 1.00 64.46 ? 167 CYS A C 1 ATOM 1324 O O . CYS A 1 167 ? -5.091 -14.269 37.075 1.00 65.03 ? 167 CYS A O 1 ATOM 1325 C CB . CYS A 1 167 ? -3.828 -17.692 37.933 1.00 63.55 ? 167 CYS A CB 1 ATOM 1326 S SG . CYS A 1 167 ? -3.130 -19.125 37.047 1.00 71.53 ? 167 CYS A SG 1 ATOM 1327 N N . PRO A 1 168 ? -4.580 -15.163 39.079 1.00 65.93 ? 168 PRO A N 1 ATOM 1328 C CA . PRO A 1 168 ? -5.046 -13.932 39.840 1.00 67.24 ? 168 PRO A CA 1 ATOM 1329 C C . PRO A 1 168 ? -4.608 -12.510 39.528 1.00 68.62 ? 168 PRO A C 1 ATOM 1330 O O . PRO A 1 168 ? -4.372 -12.043 38.419 1.00 68.36 ? 168 PRO A O 1 ATOM 1331 C CB . PRO A 1 168 ? -4.802 -14.321 41.277 1.00 67.40 ? 168 PRO A CB 1 ATOM 1332 C CG . PRO A 1 168 ? -5.176 -15.780 41.288 1.00 66.66 ? 168 PRO A CG 1 ATOM 1333 C CD . PRO A 1 168 ? -5.004 -16.305 39.894 1.00 65.60 ? 168 PRO A CD 1 ATOM 1334 N N . THR A 1 169 ? -4.529 -11.873 40.722 1.00 70.65 ? 169 THR A N 1 ATOM 1335 C CA . THR A 1 169 ? -4.070 -10.584 41.178 1.00 72.88 ? 169 THR A CA 1 ATOM 1336 C C . THR A 1 169 ? -3.775 -10.880 42.716 1.00 74.59 ? 169 THR A C 1 ATOM 1337 O O . THR A 1 169 ? -2.680 -10.512 43.169 1.00 74.95 ? 169 THR A O 1 ATOM 1338 C CB . THR A 1 169 ? -5.033 -9.443 40.828 1.00 72.56 ? 169 THR A CB 1 ATOM 1339 O OG1 . THR A 1 169 ? -5.831 -9.151 41.992 1.00 73.27 ? 169 THR A OG1 1 ATOM 1340 C CG2 . THR A 1 169 ? -5.919 -9.825 39.660 1.00 72.72 ? 169 THR A CG2 1 ATOM 1341 N N . PRO A 1 170 ? -4.686 -11.538 43.576 1.00 76.05 ? 170 PRO A N 1 ATOM 1342 C CA . PRO A 1 170 ? -4.239 -12.023 44.963 1.00 77.28 ? 170 PRO A CA 1 ATOM 1343 C C . PRO A 1 170 ? -2.998 -12.978 45.011 1.00 78.35 ? 170 PRO A C 1 ATOM 1344 O O . PRO A 1 170 ? -2.693 -13.652 44.036 1.00 78.86 ? 170 PRO A O 1 ATOM 1345 C CB . PRO A 1 170 ? -5.522 -12.518 45.620 1.00 77.35 ? 170 PRO A CB 1 ATOM 1346 C CG . PRO A 1 170 ? -6.517 -11.519 45.147 1.00 77.18 ? 170 PRO A CG 1 ATOM 1347 C CD . PRO A 1 170 ? -5.988 -10.888 43.873 1.00 76.28 ? 170 PRO A CD 1 ATOM 1348 N N . PRO A 1 171 ? -2.266 -13.014 46.204 1.00 79.11 ? 171 PRO A N 1 ATOM 1349 C CA . PRO A 1 171 ? -1.006 -13.821 46.398 1.00 79.52 ? 171 PRO A CA 1 ATOM 1350 C C . PRO A 1 171 ? -1.137 -15.247 46.012 1.00 79.76 ? 171 PRO A C 1 ATOM 1351 O O . PRO A 1 171 ? -1.716 -16.055 46.720 1.00 80.12 ? 171 PRO A O 1 ATOM 1352 C CB . PRO A 1 171 ? -0.578 -13.578 47.828 1.00 79.67 ? 171 PRO A CB 1 ATOM 1353 C CG . PRO A 1 171 ? -0.890 -12.113 47.939 1.00 79.56 ? 171 PRO A CG 1 ATOM 1354 C CD . PRO A 1 171 ? -1.977 -11.758 46.961 1.00 79.34 ? 171 PRO A CD 1 ATOM 1355 N N . TYR A 1 172 ? -0.621 -15.570 44.865 1.00 79.65 ? 172 TYR A N 1 ATOM 1356 C CA . TYR A 1 172 ? -0.996 -16.885 44.444 1.00 79.65 ? 172 TYR A CA 1 ATOM 1357 C C . TYR A 1 172 ? -0.294 -18.087 45.055 1.00 79.00 ? 172 TYR A C 1 ATOM 1358 O O . TYR A 1 172 ? 0.894 -18.066 45.395 1.00 79.24 ? 172 TYR A O 1 ATOM 1359 C CB . TYR A 1 172 ? -0.936 -16.888 42.980 1.00 80.06 ? 172 TYR A CB 1 ATOM 1360 C CG . TYR A 1 172 ? -1.677 -18.060 42.480 1.00 82.55 ? 172 TYR A CG 1 ATOM 1361 C CD1 . TYR A 1 172 ? -2.843 -18.558 43.053 1.00 84.80 ? 172 TYR A CD1 1 ATOM 1362 C CD2 . TYR A 1 172 ? -1.168 -18.718 41.380 1.00 84.19 ? 172 TYR A CD2 1 ATOM 1363 C CE1 . TYR A 1 172 ? -3.445 -19.686 42.523 1.00 86.19 ? 172 TYR A CE1 1 ATOM 1364 C CE2 . TYR A 1 172 ? -1.758 -19.829 40.847 1.00 85.50 ? 172 TYR A CE2 1 ATOM 1365 C CZ . TYR A 1 172 ? -2.906 -20.311 41.418 1.00 86.30 ? 172 TYR A CZ 1 ATOM 1366 O OH . TYR A 1 172 ? -3.539 -21.413 40.874 1.00 87.39 ? 172 TYR A OH 1 ATOM 1367 N N . GLN A 1 173 ? -1.087 -19.178 45.140 1.00 77.76 ? 173 GLN A N 1 ATOM 1368 C CA . GLN A 1 173 ? -0.618 -20.408 45.760 1.00 76.01 ? 173 GLN A CA 1 ATOM 1369 C C . GLN A 1 173 ? 0.327 -21.264 44.893 1.00 74.54 ? 173 GLN A C 1 ATOM 1370 O O . GLN A 1 173 ? 1.508 -21.206 45.246 1.00 74.86 ? 173 GLN A O 1 ATOM 1371 C CB . GLN A 1 173 ? -1.781 -21.154 46.410 1.00 76.22 ? 173 GLN A CB 1 ATOM 1372 C CG . GLN A 1 173 ? -1.624 -21.190 47.950 1.00 76.69 ? 173 GLN A CG 1 ATOM 1373 C CD . GLN A 1 173 ? -2.893 -21.114 48.809 1.00 77.80 ? 173 GLN A CD 1 ATOM 1374 O OE1 . GLN A 1 173 ? -3.733 -20.237 48.647 1.00 78.09 ? 173 GLN A OE1 1 ATOM 1375 N NE2 . GLN A 1 173 ? -3.210 -21.947 49.801 1.00 77.65 ? 173 GLN A NE2 1 ATOM 1376 N N . SER A 1 174 ? 0.076 -22.057 43.852 1.00 71.89 ? 174 SER A N 1 ATOM 1377 C CA . SER A 1 174 ? 1.379 -22.618 43.400 1.00 68.90 ? 174 SER A CA 1 ATOM 1378 C C . SER A 1 174 ? 1.702 -23.113 41.950 1.00 66.09 ? 174 SER A C 1 ATOM 1379 O O . SER A 1 174 ? 0.906 -23.786 41.295 1.00 66.39 ? 174 SER A O 1 ATOM 1380 C CB . SER A 1 174 ? 1.749 -23.763 44.371 1.00 69.43 ? 174 SER A CB 1 ATOM 1381 O OG . SER A 1 174 ? 3.160 -23.892 44.494 1.00 71.76 ? 174 SER A OG 1 ATOM 1382 N N . LEU A 1 175 ? 2.950 -22.702 41.506 1.00 62.35 ? 175 LEU A N 1 ATOM 1383 C CA . LEU A 1 175 ? 3.595 -23.080 40.204 1.00 57.65 ? 175 LEU A CA 1 ATOM 1384 C C . LEU A 1 175 ? 5.043 -22.517 40.041 1.00 54.15 ? 175 LEU A C 1 ATOM 1385 O O . LEU A 1 175 ? 6.036 -23.249 40.051 1.00 54.22 ? 175 LEU A O 1 ATOM 1386 C CB . LEU A 1 175 ? 2.717 -22.567 39.039 1.00 58.05 ? 175 LEU A CB 1 ATOM 1387 C CG . LEU A 1 175 ? 2.547 -23.405 37.737 1.00 58.96 ? 175 LEU A CG 1 ATOM 1388 C CD1 . LEU A 1 175 ? 2.036 -22.522 36.615 1.00 60.61 ? 175 LEU A CD1 1 ATOM 1389 C CD2 . LEU A 1 175 ? 3.850 -24.085 37.358 1.00 59.52 ? 175 LEU A CD2 1 ATOM 1390 N N . ALA A 1 176 ? 5.100 -21.175 39.901 1.00 49.07 ? 176 ALA A N 1 ATOM 1391 C CA . ALA A 1 176 ? 6.241 -20.277 39.693 1.00 44.30 ? 176 ALA A CA 1 ATOM 1392 C C . ALA A 1 176 ? 5.556 -19.099 39.056 1.00 40.72 ? 176 ALA A C 1 ATOM 1393 O O . ALA A 1 176 ? 4.792 -19.260 38.103 1.00 39.53 ? 176 ALA A O 1 ATOM 1394 C CB . ALA A 1 176 ? 7.288 -20.841 38.745 1.00 44.18 ? 176 ALA A CB 1 ATOM 1395 N N . ARG A 1 177 ? 5.822 -17.899 39.561 1.00 36.74 ? 177 ARG A N 1 ATOM 1396 C CA . ARG A 1 177 ? 5.100 -16.728 39.097 1.00 34.04 ? 177 ARG A CA 1 ATOM 1397 C C . ARG A 1 177 ? 5.343 -16.266 37.665 1.00 32.11 ? 177 ARG A C 1 ATOM 1398 O O . ARG A 1 177 ? 6.480 -16.041 37.251 1.00 31.17 ? 177 ARG A O 1 ATOM 1399 C CB . ARG A 1 177 ? 5.372 -15.602 40.079 1.00 34.31 ? 177 ARG A CB 1 ATOM 1400 C CG . ARG A 1 177 ? 5.108 -14.220 39.528 1.00 31.89 ? 177 ARG A CG 1 ATOM 1401 C CD . ARG A 1 177 ? 4.056 -13.495 40.360 1.00 32.54 ? 177 ARG A CD 1 ATOM 1402 N NE . ARG A 1 177 ? 4.465 -12.139 40.688 1.00 31.83 ? 177 ARG A NE 1 ATOM 1403 C CZ . ARG A 1 177 ? 4.050 -11.477 41.751 1.00 30.85 ? 177 ARG A CZ 1 ATOM 1404 N NH1 . ARG A 1 177 ? 3.183 -12.035 42.596 1.00 29.24 ? 177 ARG A NH1 1 ATOM 1405 N NH2 . ARG A 1 177 ? 4.497 -10.251 41.971 1.00 33.98 ? 177 ARG A NH2 1 ATOM 1406 N N . GLU A 1 178 ? 4.269 -16.112 36.890 1.00 30.04 ? 178 GLU A N 1 ATOM 1407 C CA . GLU A 1 178 ? 4.394 -15.719 35.470 1.00 27.80 ? 178 GLU A CA 1 ATOM 1408 C C . GLU A 1 178 ? 3.663 -14.392 35.173 1.00 25.91 ? 178 GLU A C 1 ATOM 1409 O O . GLU A 1 178 ? 2.508 -14.221 35.549 1.00 25.76 ? 178 GLU A O 1 ATOM 1410 C CB . GLU A 1 178 ? 3.864 -16.824 34.570 1.00 27.69 ? 178 GLU A CB 1 ATOM 1411 C CG . GLU A 1 178 ? 4.361 -18.237 34.904 1.00 26.87 ? 178 GLU A CG 1 ATOM 1412 C CD . GLU A 1 178 ? 5.843 -18.435 34.635 1.00 31.37 ? 178 GLU A CD 1 ATOM 1413 O OE1 . GLU A 1 178 ? 6.387 -19.514 34.972 1.00 31.25 ? 178 GLU A OE1 1 ATOM 1414 O OE2 . GLU A 1 178 ? 6.452 -17.492 34.076 1.00 33.24 ? 178 GLU A OE2 1 ATOM 1415 N N . GLN A 1 179 ? 4.348 -13.485 34.491 1.00 24.16 ? 179 GLN A N 1 ATOM 1416 C CA . GLN A 1 179 ? 3.812 -12.139 34.237 1.00 22.10 ? 179 GLN A CA 1 ATOM 1417 C C . GLN A 1 179 ? 2.848 -12.165 33.074 1.00 21.16 ? 179 GLN A C 1 ATOM 1418 O O . GLN A 1 179 ? 2.989 -12.962 32.170 1.00 21.39 ? 179 GLN A O 1 ATOM 1419 C CB . GLN A 1 179 ? 4.947 -11.120 34.042 1.00 21.22 ? 179 GLN A CB 1 ATOM 1420 C CG . GLN A 1 179 ? 5.649 -10.717 35.354 1.00 19.88 ? 179 GLN A CG 1 ATOM 1421 C CD . GLN A 1 179 ? 6.450 -11.869 36.004 1.00 19.75 ? 179 GLN A CD 1 ATOM 1422 O OE1 . GLN A 1 179 ? 7.030 -12.690 35.307 1.00 18.53 ? 179 GLN A OE1 1 ATOM 1423 N NE2 . GLN A 1 179 ? 6.497 -11.899 37.339 1.00 16.63 ? 179 GLN A NE2 1 ATOM 1424 N N . ILE A 1 180 ? 1.832 -11.332 33.122 1.00 20.26 ? 180 ILE A N 1 ATOM 1425 C CA . ILE A 1 180 ? 0.856 -11.304 32.052 1.00 19.75 ? 180 ILE A CA 1 ATOM 1426 C C . ILE A 1 180 ? 1.403 -10.488 30.894 1.00 19.30 ? 180 ILE A C 1 ATOM 1427 O O . ILE A 1 180 ? 2.158 -9.546 31.128 1.00 19.10 ? 180 ILE A O 1 ATOM 1428 C CB . ILE A 1 180 ? -0.404 -10.604 32.533 1.00 19.53 ? 180 ILE A CB 1 ATOM 1429 C CG1 . ILE A 1 180 ? -1.044 -11.370 33.675 1.00 20.86 ? 180 ILE A CG1 1 ATOM 1430 C CG2 . ILE A 1 180 ? -1.403 -10.583 31.455 1.00 21.12 ? 180 ILE A CG2 1 ATOM 1431 C CD1 . ILE A 1 180 ? -2.172 -10.638 34.312 1.00 20.99 ? 180 ILE A CD1 1 ATOM 1432 N N . ASN A 1 181 ? 1.070 -10.874 29.656 1.00 18.22 ? 181 ASN A N 1 ATOM 1433 C CA . ASN A 1 181 ? 1.232 -9.968 28.500 1.00 17.30 ? 181 ASN A CA 1 ATOM 1434 C C . ASN A 1 181 ? -0.204 -9.531 28.185 1.00 16.24 ? 181 ASN A C 1 ATOM 1435 O O . ASN A 1 181 ? -1.067 -10.367 27.949 1.00 16.07 ? 181 ASN A O 1 ATOM 1436 C CB . ASN A 1 181 ? 1.908 -10.657 27.308 1.00 17.29 ? 181 ASN A CB 1 ATOM 1437 C CG . ASN A 1 181 ? 2.133 -9.719 26.102 1.00 20.18 ? 181 ASN A CG 1 ATOM 1438 O OD1 . ASN A 1 181 ? 1.785 -8.528 26.132 1.00 24.26 ? 181 ASN A OD1 1 ATOM 1439 N ND2 . ASN A 1 181 ? 2.720 -10.263 25.031 1.00 19.57 ? 181 ASN A ND2 1 ATOM 1440 N N . ALA A 1 182 ? -0.473 -8.232 28.218 1.00 15.66 ? 182 ALA A N 1 ATOM 1441 C CA . ALA A 1 182 ? -1.838 -7.728 28.043 1.00 15.44 ? 182 ALA A CA 1 ATOM 1442 C C . ALA A 1 182 ? -2.210 -7.380 26.594 1.00 15.82 ? 182 ALA A C 1 ATOM 1443 O O . ALA A 1 182 ? -3.255 -6.782 26.323 1.00 15.83 ? 182 ALA A O 1 ATOM 1444 C CB . ALA A 1 182 ? -2.067 -6.557 28.935 1.00 14.66 ? 182 ALA A CB 1 ATOM 1445 N N . VAL A 1 183 ? -1.357 -7.772 25.658 1.00 16.25 ? 183 VAL A N 1 ATOM 1446 C CA . VAL A 1 183 ? -1.581 -7.433 24.259 1.00 16.82 ? 183 VAL A CA 1 ATOM 1447 C C . VAL A 1 183 ? -1.260 -8.656 23.387 1.00 17.45 ? 183 VAL A C 1 ATOM 1448 O O . VAL A 1 183 ? -0.827 -9.694 23.901 1.00 17.80 ? 183 VAL A O 1 ATOM 1449 C CB . VAL A 1 183 ? -0.786 -6.125 23.830 1.00 16.94 ? 183 VAL A CB 1 ATOM 1450 C CG1 . VAL A 1 183 ? -0.796 -5.080 24.954 1.00 15.10 ? 183 VAL A CG1 1 ATOM 1451 C CG2 . VAL A 1 183 ? 0.662 -6.446 23.457 1.00 16.82 ? 183 VAL A CG2 1 ATOM 1452 N N . THR A 1 184 ? -1.484 -8.558 22.083 1.00 17.35 ? 184 THR A N 1 ATOM 1453 C CA . THR A 1 184 ? -1.310 -9.723 21.252 1.00 18.08 ? 184 THR A CA 1 ATOM 1454 C C . THR A 1 184 ? 0.120 -9.823 20.795 1.00 18.52 ? 184 THR A C 1 ATOM 1455 O O . THR A 1 184 ? 0.679 -8.859 20.334 1.00 18.48 ? 184 THR A O 1 ATOM 1456 C CB . THR A 1 184 ? -2.236 -9.652 20.017 1.00 18.18 ? 184 THR A CB 1 ATOM 1457 O OG1 . THR A 1 184 ? -1.933 -8.465 19.249 1.00 19.38 ? 184 THR A OG1 1 ATOM 1458 C CG2 . THR A 1 184 ? -3.667 -9.466 20.437 1.00 17.10 ? 184 THR A CG2 1 ATOM 1459 N N . SER A 1 185 ? 0.697 -11.015 20.886 1.00 19.32 ? 185 SER A N 1 ATOM 1460 C CA . SER A 1 185 ? 2.054 -11.244 20.428 1.00 19.33 ? 185 SER A CA 1 ATOM 1461 C C . SER A 1 185 ? 2.214 -11.028 18.922 1.00 20.32 ? 185 SER A C 1 ATOM 1462 O O . SER A 1 185 ? 3.318 -10.815 18.450 1.00 21.76 ? 185 SER A O 1 ATOM 1463 C CB . SER A 1 185 ? 2.484 -12.668 20.755 1.00 18.69 ? 185 SER A CB 1 ATOM 1464 O OG . SER A 1 185 ? 2.444 -12.929 22.143 1.00 18.17 ? 185 SER A OG 1 ATOM 1465 N N . PHE A 1 186 ? 1.141 -11.087 18.150 1.00 20.22 ? 186 PHE A N 1 ATOM 1466 C CA . PHE A 1 186 ? 1.282 -10.984 16.703 1.00 20.34 ? 186 PHE A CA 1 ATOM 1467 C C . PHE A 1 186 ? 1.408 -9.523 16.337 1.00 21.31 ? 186 PHE A C 1 ATOM 1468 O O . PHE A 1 186 ? 0.659 -8.699 16.888 1.00 22.94 ? 186 PHE A O 1 ATOM 1469 C CB . PHE A 1 186 ? 0.058 -11.595 15.993 1.00 20.26 ? 186 PHE A CB 1 ATOM 1470 C CG . PHE A 1 186 ? -0.268 -12.984 16.449 1.00 17.95 ? 186 PHE A CG 1 ATOM 1471 C CD1 . PHE A 1 186 ? 0.429 -14.049 15.976 1.00 15.86 ? 186 PHE A CD1 1 ATOM 1472 C CD2 . PHE A 1 186 ? -1.244 -13.203 17.380 1.00 16.50 ? 186 PHE A CD2 1 ATOM 1473 C CE1 . PHE A 1 186 ? 0.154 -15.299 16.414 1.00 16.96 ? 186 PHE A CE1 1 ATOM 1474 C CE2 . PHE A 1 186 ? -1.512 -14.453 17.809 1.00 18.51 ? 186 PHE A CE2 1 ATOM 1475 C CZ . PHE A 1 186 ? -0.806 -15.506 17.328 1.00 17.23 ? 186 PHE A CZ 1 ATOM 1476 N N . LEU A 1 187 ? 2.344 -9.199 15.435 1.00 20.88 ? 187 LEU A N 1 ATOM 1477 C CA . LEU A 1 187 ? 2.540 -7.840 14.919 1.00 19.99 ? 187 LEU A CA 1 ATOM 1478 C C . LEU A 1 187 ? 1.326 -7.537 14.032 1.00 20.03 ? 187 LEU A C 1 ATOM 1479 O O . LEU A 1 187 ? 1.348 -7.787 12.804 1.00 19.74 ? 187 LEU A O 1 ATOM 1480 C CB . LEU A 1 187 ? 3.854 -7.734 14.119 1.00 19.62 ? 187 LEU A CB 1 ATOM 1481 C CG . LEU A 1 187 ? 4.317 -6.321 13.725 1.00 18.09 ? 187 LEU A CG 1 ATOM 1482 C CD1 . LEU A 1 187 ? 4.475 -5.502 14.949 1.00 21.55 ? 187 LEU A CD1 1 ATOM 1483 C CD2 . LEU A 1 187 ? 5.638 -6.365 13.049 1.00 15.46 ? 187 LEU A CD2 1 ATOM 1484 N N . ASP A 1 188 ? 0.295 -7.050 14.658 1.00 19.19 ? 188 ASP A N 1 ATOM 1485 C CA . ASP A 1 188 ? -1.012 -6.894 14.072 1.00 18.43 ? 188 ASP A CA 1 ATOM 1486 C C . ASP A 1 188 ? -1.692 -5.504 14.240 1.00 18.10 ? 188 ASP A C 1 ATOM 1487 O O . ASP A 1 188 ? -2.890 -5.386 14.008 1.00 18.64 ? 188 ASP A O 1 ATOM 1488 C CB . ASP A 1 188 ? -1.907 -8.002 14.661 1.00 18.25 ? 188 ASP A CB 1 ATOM 1489 C CG . ASP A 1 188 ? -2.134 -7.839 16.152 1.00 19.94 ? 188 ASP A CG 1 ATOM 1490 O OD1 . ASP A 1 188 ? -1.352 -7.127 16.810 1.00 24.25 ? 188 ASP A OD1 1 ATOM 1491 O OD2 . ASP A 1 188 ? -3.112 -8.421 16.650 1.00 20.17 ? 188 ASP A OD2 1 ATOM 1492 N N . ALA A 1 189 ? -0.952 -4.479 14.636 1.00 17.46 ? 189 ALA A N 1 ATOM 1493 C CA . ALA A 1 189 ? -1.515 -3.158 14.810 1.00 17.09 ? 189 ALA A CA 1 ATOM 1494 C C . ALA A 1 189 ? -2.489 -3.114 15.989 1.00 17.90 ? 189 ALA A C 1 ATOM 1495 O O . ALA A 1 189 ? -3.466 -2.325 15.996 1.00 18.48 ? 189 ALA A O 1 ATOM 1496 C CB . ALA A 1 189 ? -2.201 -2.723 13.561 1.00 16.64 ? 189 ALA A CB 1 ATOM 1497 N N . SER A 1 190 ? -2.227 -3.948 16.993 1.00 17.17 ? 190 SER A N 1 ATOM 1498 C CA . SER A 1 190 ? -3.102 -3.987 18.138 1.00 16.41 ? 190 SER A CA 1 ATOM 1499 C C . SER A 1 190 ? -2.983 -2.701 18.922 1.00 16.31 ? 190 SER A C 1 ATOM 1500 O O . SER A 1 190 ? -3.776 -2.436 19.806 1.00 17.84 ? 190 SER A O 1 ATOM 1501 C CB . SER A 1 190 ? -2.785 -5.203 19.006 1.00 16.44 ? 190 SER A CB 1 ATOM 1502 O OG . SER A 1 190 ? -1.376 -5.379 19.148 1.00 17.31 ? 190 SER A OG 1 ATOM 1503 N N . LEU A 1 191 ? -2.005 -1.880 18.607 1.00 16.08 ? 191 LEU A N 1 ATOM 1504 C CA . LEU A 1 191 ? -1.822 -0.653 19.357 1.00 16.33 ? 191 LEU A CA 1 ATOM 1505 C C . LEU A 1 191 ? -2.754 0.431 18.821 1.00 16.69 ? 191 LEU A C 1 ATOM 1506 O O . LEU A 1 191 ? -3.050 1.390 19.527 1.00 15.97 ? 191 LEU A O 1 ATOM 1507 C CB . LEU A 1 191 ? -0.357 -0.204 19.372 1.00 16.35 ? 191 LEU A CB 1 ATOM 1508 C CG . LEU A 1 191 ? 0.273 0.343 18.097 1.00 16.38 ? 191 LEU A CG 1 ATOM 1509 C CD1 . LEU A 1 191 ? 1.644 0.806 18.438 1.00 15.73 ? 191 LEU A CD1 1 ATOM 1510 C CD2 . LEU A 1 191 ? 0.321 -0.754 17.030 1.00 17.06 ? 191 LEU A CD2 1 ATOM 1511 N N . VAL A 1 192 ? -3.215 0.251 17.577 1.00 17.20 ? 192 VAL A N 1 ATOM 1512 C CA . VAL A 1 192 ? -4.194 1.153 16.974 1.00 17.67 ? 192 VAL A CA 1 ATOM 1513 C C . VAL A 1 192 ? -5.585 0.648 17.292 1.00 18.77 ? 192 VAL A C 1 ATOM 1514 O O . VAL A 1 192 ? -6.451 1.413 17.695 1.00 20.03 ? 192 VAL A O 1 ATOM 1515 C CB . VAL A 1 192 ? -4.099 1.225 15.422 1.00 16.80 ? 192 VAL A CB 1 ATOM 1516 C CG1 . VAL A 1 192 ? -5.242 1.983 14.856 1.00 16.89 ? 192 VAL A CG1 1 ATOM 1517 C CG2 . VAL A 1 192 ? -2.908 1.929 14.991 1.00 16.84 ? 192 VAL A CG2 1 ATOM 1518 N N . TYR A 1 193 ? -5.809 -0.640 17.120 1.00 19.36 ? 193 TYR A N 1 ATOM 1519 C CA . TYR A 1 193 ? -7.153 -1.163 17.268 1.00 20.94 ? 193 TYR A CA 1 ATOM 1520 C C . TYR A 1 193 ? -7.585 -1.635 18.681 1.00 21.92 ? 193 TYR A C 1 ATOM 1521 O O . TYR A 1 193 ? -8.783 -1.747 18.947 1.00 22.74 ? 193 TYR A O 1 ATOM 1522 C CB . TYR A 1 193 ? -7.414 -2.225 16.186 1.00 20.39 ? 193 TYR A CB 1 ATOM 1523 C CG . TYR A 1 193 ? -7.130 -1.667 14.808 1.00 22.08 ? 193 TYR A CG 1 ATOM 1524 C CD1 . TYR A 1 193 ? -8.056 -0.849 14.158 1.00 20.28 ? 193 TYR A CD1 1 ATOM 1525 C CD2 . TYR A 1 193 ? -5.920 -1.935 14.154 1.00 25.00 ? 193 TYR A CD2 1 ATOM 1526 C CE1 . TYR A 1 193 ? -7.797 -0.315 12.924 1.00 19.66 ? 193 TYR A CE1 1 ATOM 1527 C CE2 . TYR A 1 193 ? -5.661 -1.406 12.879 1.00 23.83 ? 193 TYR A CE2 1 ATOM 1528 C CZ . TYR A 1 193 ? -6.608 -0.592 12.289 1.00 23.56 ? 193 TYR A CZ 1 ATOM 1529 O OH . TYR A 1 193 ? -6.366 -0.078 11.032 1.00 27.26 ? 193 TYR A OH 1 ATOM 1530 N N . GLY A 1 194 ? -6.649 -1.907 19.564 1.00 21.97 ? 194 GLY A N 1 ATOM 1531 C CA . GLY A 1 194 ? -7.019 -2.404 20.888 1.00 22.28 ? 194 GLY A CA 1 ATOM 1532 C C . GLY A 1 194 ? -6.813 -3.904 20.893 1.00 22.72 ? 194 GLY A C 1 ATOM 1533 O O . GLY A 1 194 ? -6.798 -4.533 19.839 1.00 22.51 ? 194 GLY A O 1 ATOM 1534 N N . SER A 1 195 ? -6.653 -4.504 22.078 1.00 23.47 ? 195 SER A N 1 ATOM 1535 C CA . SER A 1 195 ? -6.483 -5.951 22.213 1.00 23.90 ? 195 SER A CA 1 ATOM 1536 C C . SER A 1 195 ? -7.683 -6.528 22.882 1.00 24.24 ? 195 SER A C 1 ATOM 1537 O O . SER A 1 195 ? -7.755 -7.750 23.094 1.00 23.67 ? 195 SER A O 1 ATOM 1538 C CB . SER A 1 195 ? -5.221 -6.293 23.016 1.00 23.50 ? 195 SER A CB 1 ATOM 1539 O OG . SER A 1 195 ? -4.051 -5.944 22.296 1.00 23.71 ? 195 SER A OG 1 ATOM 1540 N N . GLU A 1 196 ? -8.600 -5.678 23.195 1.00 25.06 ? 196 GLU A N 1 ATOM 1541 C CA . GLU A 1 196 ? -9.790 -6.184 23.863 1.00 26.52 ? 196 GLU A CA 1 ATOM 1542 C C . GLU A 1 196 ? -11.099 -5.910 23.158 1.00 26.13 ? 196 GLU A C 1 ATOM 1543 O O . GLU A 1 196 ? -11.268 -4.908 22.449 1.00 25.25 ? 196 GLU A O 1 ATOM 1544 C CB . GLU A 1 196 ? -9.926 -5.606 25.252 1.00 27.44 ? 196 GLU A CB 1 ATOM 1545 C CG . GLU A 1 196 ? -8.812 -5.841 26.231 1.00 32.19 ? 196 GLU A CG 1 ATOM 1546 C CD . GLU A 1 196 ? -9.057 -4.900 27.358 1.00 40.71 ? 196 GLU A CD 1 ATOM 1547 O OE1 . GLU A 1 196 ? -9.030 -3.681 27.121 1.00 41.98 ? 196 GLU A OE1 1 ATOM 1548 O OE2 . GLU A 1 196 ? -9.280 -5.372 28.485 1.00 43.86 ? 196 GLU A OE2 1 ATOM 1549 N N . PRO A 1 197 ? -11.998 -6.854 23.385 1.00 26.32 ? 197 PRO A N 1 ATOM 1550 C CA . PRO A 1 197 ? -13.400 -6.782 22.862 1.00 26.47 ? 197 PRO A CA 1 ATOM 1551 C C . PRO A 1 197 ? -14.273 -5.585 23.226 1.00 26.62 ? 197 PRO A C 1 ATOM 1552 O O . PRO A 1 197 ? -15.111 -5.213 22.407 1.00 26.38 ? 197 PRO A O 1 ATOM 1553 C CB . PRO A 1 197 ? -13.973 -8.146 23.214 1.00 26.67 ? 197 PRO A CB 1 ATOM 1554 C CG . PRO A 1 197 ? -12.819 -9.018 22.972 1.00 26.33 ? 197 PRO A CG 1 ATOM 1555 C CD . PRO A 1 197 ? -11.565 -8.214 23.112 1.00 26.00 ? 197 PRO A CD 1 HETATM 1556 N N . SEP A 1 198 ? -14.137 -4.949 24.361 1.00 26.91 ? 198 SEP A N 1 HETATM 1557 C CA . SEP A 1 198 ? -14.460 -3.809 25.170 1.00 27.14 ? 198 SEP A CA 1 HETATM 1558 C CB . SEP A 1 198 ? -13.916 -4.170 26.560 1.00 27.01 ? 198 SEP A CB 1 HETATM 1559 O OG . SEP A 1 198 ? -14.421 -5.484 26.977 1.00 30.09 ? 198 SEP A OG 1 HETATM 1560 C C . SEP A 1 198 ? -13.815 -2.509 24.580 1.00 27.58 ? 198 SEP A C 1 HETATM 1561 O O . SEP A 1 198 ? -14.475 -1.618 24.025 1.00 27.81 ? 198 SEP A O 1 HETATM 1562 P P . SEP A 1 198 ? -13.601 -6.904 27.000 1.00 20.83 ? 198 SEP A P 1 HETATM 1563 O O1P . SEP A 1 198 ? -14.493 -8.067 26.489 1.00 28.29 ? 198 SEP A O1P 1 HETATM 1564 O O2P . SEP A 1 198 ? -13.237 -7.353 28.468 1.00 26.14 ? 198 SEP A O2P 1 HETATM 1565 O O3P . SEP A 1 198 ? -12.359 -6.848 26.008 1.00 26.32 ? 198 SEP A O3P 1 ATOM 1566 N N . LEU A 1 199 ? -12.512 -2.514 24.394 1.00 27.75 ? 199 LEU A N 1 ATOM 1567 C CA . LEU A 1 199 ? -11.907 -1.296 23.940 1.00 27.19 ? 199 LEU A CA 1 ATOM 1568 C C . LEU A 1 199 ? -12.071 -1.171 22.464 1.00 28.00 ? 199 LEU A C 1 ATOM 1569 O O . LEU A 1 199 ? -12.493 -0.114 21.973 1.00 28.25 ? 199 LEU A O 1 ATOM 1570 C CB . LEU A 1 199 ? -10.439 -1.274 24.335 1.00 27.25 ? 199 LEU A CB 1 ATOM 1571 C CG . LEU A 1 199 ? -9.520 -0.106 23.937 1.00 27.38 ? 199 LEU A CG 1 ATOM 1572 C CD1 . LEU A 1 199 ? -9.865 1.198 24.653 1.00 25.64 ? 199 LEU A CD1 1 ATOM 1573 C CD2 . LEU A 1 199 ? -8.054 -0.477 24.172 1.00 24.47 ? 199 LEU A CD2 1 ATOM 1574 N N . ALA A 1 200 ? -11.787 -2.257 21.751 1.00 27.86 ? 200 ALA A N 1 ATOM 1575 C CA . ALA A 1 200 ? -11.797 -2.192 20.301 1.00 28.40 ? 200 ALA A CA 1 ATOM 1576 C C . ALA A 1 200 ? -13.057 -1.542 19.783 1.00 29.19 ? 200 ALA A C 1 ATOM 1577 O O . ALA A 1 200 ? -13.036 -0.749 18.846 1.00 30.05 ? 200 ALA A O 1 ATOM 1578 C CB . ALA A 1 200 ? -11.630 -3.549 19.708 1.00 28.66 ? 200 ALA A CB 1 ATOM 1579 N N . SER A 1 201 ? -14.171 -1.883 20.397 1.00 29.72 ? 201 SER A N 1 ATOM 1580 C CA . SER A 1 201 ? -15.442 -1.335 19.967 1.00 30.30 ? 201 SER A CA 1 ATOM 1581 C C . SER A 1 201 ? -15.606 0.154 20.346 1.00 30.57 ? 201 SER A C 1 ATOM 1582 O O . SER A 1 201 ? -16.032 0.956 19.521 1.00 31.40 ? 201 SER A O 1 ATOM 1583 C CB . SER A 1 201 ? -16.581 -2.204 20.498 1.00 30.26 ? 201 SER A CB 1 ATOM 1584 O OG . SER A 1 201 ? -17.745 -1.439 20.659 1.00 30.60 ? 201 SER A OG 1 ATOM 1585 N N . ARG A 1 202 ? -15.216 0.537 21.537 1.00 29.83 ? 202 ARG A N 1 ATOM 1586 C CA . ARG A 1 202 ? -15.373 1.904 21.946 1.00 28.97 ? 202 ARG A CA 1 ATOM 1587 C C . ARG A 1 202 ? -14.574 2.870 21.068 1.00 28.51 ? 202 ARG A C 1 ATOM 1588 O O . ARG A 1 202 ? -14.856 4.054 21.030 1.00 29.28 ? 202 ARG A O 1 ATOM 1589 C CB . ARG A 1 202 ? -14.978 2.004 23.419 1.00 29.46 ? 202 ARG A CB 1 ATOM 1590 C CG . ARG A 1 202 ? -14.277 3.270 23.844 1.00 30.21 ? 202 ARG A CG 1 ATOM 1591 C CD . ARG A 1 202 ? -14.218 3.315 25.347 1.00 35.22 ? 202 ARG A CD 1 ATOM 1592 N NE . ARG A 1 202 ? -14.137 4.676 25.788 1.00 40.91 ? 202 ARG A NE 1 ATOM 1593 C CZ . ARG A 1 202 ? -13.713 4.916 26.989 1.00 44.57 ? 202 ARG A CZ 1 ATOM 1594 N NH1 . ARG A 1 202 ? -13.338 3.929 27.777 1.00 45.24 ? 202 ARG A NH1 1 ATOM 1595 N NH2 . ARG A 1 202 ? -13.659 6.156 27.431 1.00 45.85 ? 202 ARG A NH2 1 ATOM 1596 N N . LEU A 1 203 ? -13.603 2.340 20.368 1.00 27.98 ? 203 LEU A N 1 ATOM 1597 C CA . LEU A 1 203 ? -12.728 3.165 19.591 1.00 26.93 ? 203 LEU A CA 1 ATOM 1598 C C . LEU A 1 203 ? -13.297 3.409 18.236 1.00 27.94 ? 203 LEU A C 1 ATOM 1599 O O . LEU A 1 203 ? -12.903 4.331 17.534 1.00 27.20 ? 203 LEU A O 1 ATOM 1600 C CB . LEU A 1 203 ? -11.426 2.427 19.428 1.00 26.50 ? 203 LEU A CB 1 ATOM 1601 C CG . LEU A 1 203 ? -10.133 2.854 20.103 1.00 24.53 ? 203 LEU A CG 1 ATOM 1602 C CD1 . LEU A 1 203 ? -10.338 3.652 21.343 1.00 25.69 ? 203 LEU A CD1 1 ATOM 1603 C CD2 . LEU A 1 203 ? -9.286 1.646 20.369 1.00 25.88 ? 203 LEU A CD2 1 ATOM 1604 N N . ARG A 1 204 ? -14.225 2.565 17.839 1.00 29.51 ? 204 ARG A N 1 ATOM 1605 C CA . ARG A 1 204 ? -14.739 2.702 16.494 1.00 31.32 ? 204 ARG A CA 1 ATOM 1606 C C . ARG A 1 204 ? -15.845 3.740 16.419 1.00 33.18 ? 204 ARG A C 1 ATOM 1607 O O . ARG A 1 204 ? -16.474 4.062 17.427 1.00 33.65 ? 204 ARG A O 1 ATOM 1608 C CB . ARG A 1 204 ? -15.228 1.361 15.977 1.00 30.21 ? 204 ARG A CB 1 ATOM 1609 C CG . ARG A 1 204 ? -14.280 0.220 16.219 1.00 29.82 ? 204 ARG A CG 1 ATOM 1610 C CD . ARG A 1 204 ? -14.881 -1.123 15.797 1.00 28.99 ? 204 ARG A CD 1 ATOM 1611 N NE . ARG A 1 204 ? -15.573 -0.914 14.538 1.00 27.63 ? 204 ARG A NE 1 ATOM 1612 C CZ . ARG A 1 204 ? -16.120 -1.870 13.821 1.00 29.55 ? 204 ARG A CZ 1 ATOM 1613 N NH1 . ARG A 1 204 ? -16.095 -3.136 14.254 1.00 26.55 ? 204 ARG A NH1 1 ATOM 1614 N NH2 . ARG A 1 204 ? -16.708 -1.547 12.669 1.00 28.73 ? 204 ARG A NH2 1 ATOM 1615 N N . ASN A 1 205 ? -16.066 4.262 15.215 1.00 35.46 ? 205 ASN A N 1 ATOM 1616 C CA . ASN A 1 205 ? -17.163 5.185 14.957 1.00 37.64 ? 205 ASN A CA 1 ATOM 1617 C C . ASN A 1 205 ? -18.298 4.376 14.379 1.00 38.87 ? 205 ASN A C 1 ATOM 1618 O O . ASN A 1 205 ? -18.332 4.068 13.178 1.00 39.47 ? 205 ASN A O 1 ATOM 1619 C CB . ASN A 1 205 ? -16.738 6.281 13.967 1.00 38.10 ? 205 ASN A CB 1 ATOM 1620 C CG . ASN A 1 205 ? -17.797 7.344 13.776 1.00 39.07 ? 205 ASN A CG 1 ATOM 1621 O OD1 . ASN A 1 205 ? -18.942 7.152 14.161 1.00 40.07 ? 205 ASN A OD1 1 ATOM 1622 N ND2 . ASN A 1 205 ? -17.404 8.485 13.185 1.00 41.05 ? 205 ASN A ND2 1 ATOM 1623 N N . LEU A 1 206 ? -19.235 4.028 15.242 1.00 40.11 ? 206 LEU A N 1 ATOM 1624 C CA . LEU A 1 206 ? -20.362 3.217 14.839 1.00 41.17 ? 206 LEU A CA 1 ATOM 1625 C C . LEU A 1 206 ? -21.653 4.054 14.652 1.00 42.68 ? 206 LEU A C 1 ATOM 1626 O O . LEU A 1 206 ? -22.761 3.580 14.840 1.00 43.40 ? 206 LEU A O 1 ATOM 1627 C CB . LEU A 1 206 ? -20.538 2.125 15.887 1.00 41.00 ? 206 LEU A CB 1 ATOM 1628 C CG . LEU A 1 206 ? -19.286 1.307 16.260 1.00 39.61 ? 206 LEU A CG 1 ATOM 1629 C CD1 . LEU A 1 206 ? -19.585 0.366 17.386 1.00 38.13 ? 206 LEU A CD1 1 ATOM 1630 C CD2 . LEU A 1 206 ? -18.788 0.519 15.093 1.00 39.00 ? 206 LEU A CD2 1 ATOM 1631 N N . SER A 1 207 ? -21.502 5.324 14.321 1.00 44.02 ? 207 SER A N 1 ATOM 1632 C CA . SER A 1 207 ? -22.644 6.163 14.048 1.00 45.29 ? 207 SER A CA 1 ATOM 1633 C C . SER A 1 207 ? -22.797 6.106 12.550 1.00 46.20 ? 207 SER A C 1 ATOM 1634 O O . SER A 1 207 ? -23.863 5.813 12.046 1.00 47.36 ? 207 SER A O 1 ATOM 1635 C CB . SER A 1 207 ? -22.352 7.562 14.513 1.00 45.23 ? 207 SER A CB 1 ATOM 1636 O OG . SER A 1 207 ? -21.939 7.492 15.859 1.00 45.88 ? 207 SER A OG 1 ATOM 1637 N N . SER A 1 208 ? -21.713 6.378 11.837 1.00 46.67 ? 208 SER A N 1 ATOM 1638 C CA . SER A 1 208 ? -21.666 6.159 10.402 1.00 46.81 ? 208 SER A CA 1 ATOM 1639 C C . SER A 1 208 ? -21.162 4.724 10.112 1.00 46.66 ? 208 SER A C 1 ATOM 1640 O O . SER A 1 208 ? -20.312 4.183 10.806 1.00 46.84 ? 208 SER A O 1 ATOM 1641 C CB . SER A 1 208 ? -20.731 7.175 9.766 1.00 47.14 ? 208 SER A CB 1 ATOM 1642 O OG . SER A 1 208 ? -19.492 7.189 10.447 1.00 48.05 ? 208 SER A OG 1 ATOM 1643 N N . PRO A 1 209 ? -21.684 4.092 9.084 1.00 46.33 ? 209 PRO A N 1 ATOM 1644 C CA . PRO A 1 209 ? -21.237 2.751 8.754 1.00 45.18 ? 209 PRO A CA 1 ATOM 1645 C C . PRO A 1 209 ? -20.240 2.843 7.613 1.00 43.98 ? 209 PRO A C 1 ATOM 1646 O O . PRO A 1 209 ? -20.502 2.308 6.530 1.00 44.49 ? 209 PRO A O 1 ATOM 1647 C CB . PRO A 1 209 ? -22.518 2.087 8.249 1.00 45.49 ? 209 PRO A CB 1 ATOM 1648 C CG . PRO A 1 209 ? -23.420 3.245 7.807 1.00 46.25 ? 209 PRO A CG 1 ATOM 1649 C CD . PRO A 1 209 ? -22.727 4.559 8.155 1.00 46.74 ? 209 PRO A CD 1 ATOM 1650 N N . LEU A 1 210 ? -19.131 3.540 7.848 1.00 42.11 ? 210 LEU A N 1 ATOM 1651 C CA . LEU A 1 210 ? -18.061 3.694 6.869 1.00 39.94 ? 210 LEU A CA 1 ATOM 1652 C C . LEU A 1 210 ? -16.808 3.025 7.405 1.00 38.40 ? 210 LEU A C 1 ATOM 1653 O O . LEU A 1 210 ? -15.753 3.095 6.795 1.00 38.61 ? 210 LEU A O 1 ATOM 1654 C CB . LEU A 1 210 ? -17.787 5.178 6.615 1.00 40.41 ? 210 LEU A CB 1 ATOM 1655 C CG . LEU A 1 210 ? -19.026 6.085 6.576 1.00 40.21 ? 210 LEU A CG 1 ATOM 1656 C CD1 . LEU A 1 210 ? -18.741 7.515 7.029 1.00 39.74 ? 210 LEU A CD1 1 ATOM 1657 C CD2 . LEU A 1 210 ? -19.614 6.078 5.204 1.00 40.00 ? 210 LEU A CD2 1 ATOM 1658 N N . GLY A 1 211 ? -16.939 2.364 8.551 1.00 36.74 ? 211 GLY A N 1 ATOM 1659 C CA . GLY A 1 211 ? -15.852 1.627 9.170 1.00 34.44 ? 211 GLY A CA 1 ATOM 1660 C C . GLY A 1 211 ? -14.737 2.537 9.627 1.00 33.44 ? 211 GLY A C 1 ATOM 1661 O O . GLY A 1 211 ? -13.572 2.162 9.582 1.00 32.62 ? 211 GLY A O 1 ATOM 1662 N N . LEU A 1 212 ? -15.094 3.750 10.047 1.00 32.15 ? 212 LEU A N 1 ATOM 1663 C CA . LEU A 1 212 ? -14.103 4.697 10.502 1.00 30.96 ? 212 LEU A CA 1 ATOM 1664 C C . LEU A 1 212 ? -13.805 4.534 11.994 1.00 30.71 ? 212 LEU A C 1 ATOM 1665 O O . LEU A 1 212 ? -14.602 3.961 12.773 1.00 30.37 ? 212 LEU A O 1 ATOM 1666 C CB . LEU A 1 212 ? -14.560 6.122 10.239 1.00 31.04 ? 212 LEU A CB 1 ATOM 1667 C CG . LEU A 1 212 ? -14.854 6.612 8.807 1.00 31.98 ? 212 LEU A CG 1 ATOM 1668 C CD1 . LEU A 1 212 ? -15.401 8.042 8.842 1.00 27.56 ? 212 LEU A CD1 1 ATOM 1669 C CD2 . LEU A 1 212 ? -13.627 6.493 7.863 1.00 31.26 ? 212 LEU A CD2 1 ATOM 1670 N N . MET A 1 213 ? -12.630 5.020 12.382 1.00 29.86 ? 213 MET A N 1 ATOM 1671 C CA . MET A 1 213 ? -12.257 5.052 13.774 1.00 28.70 ? 213 MET A CA 1 ATOM 1672 C C . MET A 1 213 ? -12.775 6.391 14.234 1.00 28.28 ? 213 MET A C 1 ATOM 1673 O O . MET A 1 213 ? -12.919 7.300 13.445 1.00 29.46 ? 213 MET A O 1 ATOM 1674 C CB . MET A 1 213 ? -10.743 4.965 13.943 1.00 28.61 ? 213 MET A CB 1 ATOM 1675 C CG . MET A 1 213 ? -10.091 3.635 13.554 1.00 27.92 ? 213 MET A CG 1 ATOM 1676 S SD . MET A 1 213 ? -10.510 2.228 14.622 1.00 30.12 ? 213 MET A SD 1 ATOM 1677 C CE . MET A 1 213 ? -9.763 2.664 16.143 1.00 29.73 ? 213 MET A CE 1 ATOM 1678 N N . ALA A 1 214 ? -13.066 6.494 15.513 1.00 27.97 ? 214 ALA A N 1 ATOM 1679 C CA . ALA A 1 214 ? -13.621 7.679 16.128 1.00 27.02 ? 214 ALA A CA 1 ATOM 1680 C C . ALA A 1 214 ? -12.568 8.701 16.171 1.00 26.88 ? 214 ALA A C 1 ATOM 1681 O O . ALA A 1 214 ? -11.450 8.361 16.401 1.00 27.81 ? 214 ALA A O 1 ATOM 1682 C CB . ALA A 1 214 ? -13.999 7.356 17.519 1.00 26.86 ? 214 ALA A CB 1 ATOM 1683 N N . VAL A 1 215 ? -12.907 9.964 15.978 1.00 27.07 ? 215 VAL A N 1 ATOM 1684 C CA . VAL A 1 215 ? -11.903 11.005 16.063 1.00 27.27 ? 215 VAL A CA 1 ATOM 1685 C C . VAL A 1 215 ? -12.290 12.065 17.059 1.00 28.00 ? 215 VAL A C 1 ATOM 1686 O O . VAL A 1 215 ? -13.451 12.159 17.475 1.00 27.99 ? 215 VAL A O 1 ATOM 1687 C CB . VAL A 1 215 ? -11.667 11.674 14.721 1.00 27.05 ? 215 VAL A CB 1 ATOM 1688 C CG1 . VAL A 1 215 ? -11.178 10.646 13.696 1.00 27.64 ? 215 VAL A CG1 1 ATOM 1689 C CG2 . VAL A 1 215 ? -12.930 12.323 14.249 1.00 26.12 ? 215 VAL A CG2 1 ATOM 1690 N N . ASN A 1 216 ? -11.304 12.863 17.452 1.00 28.72 ? 216 ASN A N 1 ATOM 1691 C CA . ASN A 1 216 ? -11.553 13.966 18.355 1.00 29.52 ? 216 ASN A CA 1 ATOM 1692 C C . ASN A 1 216 ? -12.589 14.905 17.734 1.00 31.23 ? 216 ASN A C 1 ATOM 1693 O O . ASN A 1 216 ? -12.623 15.134 16.504 1.00 30.98 ? 216 ASN A O 1 ATOM 1694 C CB . ASN A 1 216 ? -10.259 14.686 18.672 1.00 28.92 ? 216 ASN A CB 1 ATOM 1695 C CG . ASN A 1 216 ? -10.345 15.506 19.926 1.00 27.97 ? 216 ASN A CG 1 ATOM 1696 O OD1 . ASN A 1 216 ? -11.026 16.512 19.940 1.00 30.57 ? 216 ASN A OD1 1 ATOM 1697 N ND2 . ASN A 1 216 ? -9.646 15.091 20.985 1.00 24.29 ? 216 ASN A ND2 1 ATOM 1698 N N . GLN A 1 217 ? -13.457 15.415 18.593 1.00 33.20 ? 217 GLN A N 1 ATOM 1699 C CA . GLN A 1 217 ? -14.546 16.258 18.149 1.00 35.59 ? 217 GLN A CA 1 ATOM 1700 C C . GLN A 1 217 ? -14.325 17.642 18.686 1.00 36.55 ? 217 GLN A C 1 ATOM 1701 O O . GLN A 1 217 ? -14.922 18.584 18.197 1.00 37.21 ? 217 GLN A O 1 ATOM 1702 C CB . GLN A 1 217 ? -15.883 15.719 18.659 1.00 35.84 ? 217 GLN A CB 1 ATOM 1703 C CG . GLN A 1 217 ? -16.396 14.436 17.977 1.00 38.71 ? 217 GLN A CG 1 ATOM 1704 C CD . GLN A 1 217 ? -16.482 14.569 16.454 1.00 41.37 ? 217 GLN A CD 1 ATOM 1705 O OE1 . GLN A 1 217 ? -17.016 15.552 15.943 1.00 44.17 ? 217 GLN A OE1 1 ATOM 1706 N NE2 . GLN A 1 217 ? -15.942 13.593 15.733 1.00 40.08 ? 217 GLN A NE2 1 ATOM 1707 N N . GLU A 1 218 ? -13.474 17.764 19.697 1.00 37.54 ? 218 GLU A N 1 ATOM 1708 C CA . GLU A 1 218 ? -13.247 19.048 20.317 1.00 38.71 ? 218 GLU A CA 1 ATOM 1709 C C . GLU A 1 218 ? -12.130 19.830 19.638 1.00 38.69 ? 218 GLU A C 1 ATOM 1710 O O . GLU A 1 218 ? -12.003 21.031 19.887 1.00 38.84 ? 218 GLU A O 1 ATOM 1711 C CB . GLU A 1 218 ? -12.948 18.881 21.816 1.00 39.31 ? 218 GLU A CB 1 ATOM 1712 C CG . GLU A 1 218 ? -14.087 19.244 22.779 1.00 43.46 ? 218 GLU A CG 1 ATOM 1713 C CD . GLU A 1 218 ? -15.271 18.268 22.733 1.00 49.16 ? 218 GLU A CD 1 ATOM 1714 O OE1 . GLU A 1 218 ? -15.076 17.054 23.023 1.00 50.03 ? 218 GLU A OE1 1 ATOM 1715 O OE2 . GLU A 1 218 ? -16.410 18.717 22.418 1.00 51.40 ? 218 GLU A OE2 1 ATOM 1716 N N . ALA A 1 219 ? -11.339 19.179 18.775 1.00 38.72 ? 219 ALA A N 1 ATOM 1717 C CA . ALA A 1 219 ? -10.164 19.848 18.160 1.00 38.94 ? 219 ALA A CA 1 ATOM 1718 C C . ALA A 1 219 ? -9.616 19.221 16.886 1.00 39.10 ? 219 ALA A C 1 ATOM 1719 O O . ALA A 1 219 ? -9.645 18.008 16.716 1.00 38.29 ? 219 ALA A O 1 ATOM 1720 C CB . ALA A 1 219 ? -9.035 19.996 19.166 1.00 39.36 ? 219 ALA A CB 1 ATOM 1721 N N . TRP A 1 220 ? -9.069 20.072 16.018 1.00 39.89 ? 220 TRP A N 1 ATOM 1722 C CA . TRP A 1 220 ? -8.629 19.664 14.672 1.00 40.77 ? 220 TRP A CA 1 ATOM 1723 C C . TRP A 1 220 ? -7.215 20.106 14.313 1.00 40.42 ? 220 TRP A C 1 ATOM 1724 O O . TRP A 1 220 ? -6.676 20.998 14.946 1.00 41.07 ? 220 TRP A O 1 ATOM 1725 C CB . TRP A 1 220 ? -9.657 20.142 13.641 1.00 41.20 ? 220 TRP A CB 1 ATOM 1726 C CG . TRP A 1 220 ? -10.920 19.351 13.803 1.00 44.32 ? 220 TRP A CG 1 ATOM 1727 C CD1 . TRP A 1 220 ? -11.941 19.594 14.677 1.00 45.84 ? 220 TRP A CD1 1 ATOM 1728 C CD2 . TRP A 1 220 ? -11.252 18.129 13.135 1.00 47.11 ? 220 TRP A CD2 1 ATOM 1729 N NE1 . TRP A 1 220 ? -12.895 18.606 14.576 1.00 46.51 ? 220 TRP A NE1 1 ATOM 1730 C CE2 . TRP A 1 220 ? -12.497 17.697 13.636 1.00 47.17 ? 220 TRP A CE2 1 ATOM 1731 C CE3 . TRP A 1 220 ? -10.621 17.353 12.153 1.00 49.40 ? 220 TRP A CE3 1 ATOM 1732 C CZ2 . TRP A 1 220 ? -13.128 16.538 13.184 1.00 49.72 ? 220 TRP A CZ2 1 ATOM 1733 C CZ3 . TRP A 1 220 ? -11.245 16.193 11.710 1.00 50.70 ? 220 TRP A CZ3 1 ATOM 1734 C CH2 . TRP A 1 220 ? -12.489 15.800 12.225 1.00 50.29 ? 220 TRP A CH2 1 ATOM 1735 N N . ASP A 1 221 ? -6.593 19.465 13.333 1.00 39.95 ? 221 ASP A N 1 ATOM 1736 C CA . ASP A 1 221 ? -5.231 19.817 12.933 1.00 39.77 ? 221 ASP A CA 1 ATOM 1737 C C . ASP A 1 221 ? -5.345 20.126 11.461 1.00 39.62 ? 221 ASP A C 1 ATOM 1738 O O . ASP A 1 221 ? -5.206 19.238 10.622 1.00 39.71 ? 221 ASP A O 1 ATOM 1739 C CB . ASP A 1 221 ? -4.283 18.651 13.227 1.00 40.33 ? 221 ASP A CB 1 ATOM 1740 C CG . ASP A 1 221 ? -2.892 18.830 12.640 1.00 41.40 ? 221 ASP A CG 1 ATOM 1741 O OD1 . ASP A 1 221 ? -2.445 19.981 12.470 1.00 43.83 ? 221 ASP A OD1 1 ATOM 1742 O OD2 . ASP A 1 221 ? -2.164 17.854 12.323 1.00 41.80 ? 221 ASP A OD2 1 ATOM 1743 N N . HIS A 1 222 ? -5.625 21.402 11.170 1.00 39.38 ? 222 HIS A N 1 ATOM 1744 C CA . HIS A 1 222 ? -5.990 21.886 9.835 1.00 39.25 ? 222 HIS A CA 1 ATOM 1745 C C . HIS A 1 222 ? -6.939 20.919 9.162 1.00 38.74 ? 222 HIS A C 1 ATOM 1746 O O . HIS A 1 222 ? -6.634 20.390 8.100 1.00 39.11 ? 222 HIS A O 1 ATOM 1747 C CB . HIS A 1 222 ? -4.793 22.135 8.922 1.00 39.69 ? 222 HIS A CB 1 ATOM 1748 C CG . HIS A 1 222 ? -3.620 22.737 9.618 1.00 42.37 ? 222 HIS A CG 1 ATOM 1749 N ND1 . HIS A 1 222 ? -2.319 22.456 9.257 1.00 45.20 ? 222 HIS A ND1 1 ATOM 1750 C CD2 . HIS A 1 222 ? -3.547 23.579 10.673 1.00 45.44 ? 222 HIS A CD2 1 ATOM 1751 C CE1 . HIS A 1 222 ? -1.494 23.093 10.069 1.00 46.77 ? 222 HIS A CE1 1 ATOM 1752 N NE2 . HIS A 1 222 ? -2.214 23.784 10.937 1.00 46.81 ? 222 HIS A NE2 1 ATOM 1753 N N . GLY A 1 223 ? -8.094 20.697 9.779 1.00 37.87 ? 223 GLY A N 1 ATOM 1754 C CA . GLY A 1 223 ? -9.054 19.761 9.251 1.00 36.56 ? 223 GLY A CA 1 ATOM 1755 C C . GLY A 1 223 ? -8.526 18.347 9.135 1.00 36.27 ? 223 GLY A C 1 ATOM 1756 O O . GLY A 1 223 ? -9.044 17.554 8.337 1.00 37.22 ? 223 GLY A O 1 ATOM 1757 N N . LEU A 1 224 ? -7.469 18.014 9.869 1.00 34.80 ? 224 LEU A N 1 ATOM 1758 C CA . LEU A 1 224 ? -7.091 16.613 9.932 1.00 33.38 ? 224 LEU A CA 1 ATOM 1759 C C . LEU A 1 224 ? -7.403 16.104 11.319 1.00 32.68 ? 224 LEU A C 1 ATOM 1760 O O . LEU A 1 224 ? -7.446 16.885 12.269 1.00 32.43 ? 224 LEU A O 1 ATOM 1761 C CB . LEU A 1 224 ? -5.643 16.384 9.565 1.00 33.42 ? 224 LEU A CB 1 ATOM 1762 C CG . LEU A 1 224 ? -5.335 16.622 8.082 1.00 33.75 ? 224 LEU A CG 1 ATOM 1763 C CD1 . LEU A 1 224 ? -3.867 16.731 7.901 1.00 32.77 ? 224 LEU A CD1 1 ATOM 1764 C CD2 . LEU A 1 224 ? -5.885 15.557 7.147 1.00 34.55 ? 224 LEU A CD2 1 ATOM 1765 N N . ALA A 1 225 ? -7.648 14.798 11.419 1.00 31.82 ? 225 ALA A N 1 ATOM 1766 C CA . ALA A 1 225 ? -7.993 14.135 12.683 1.00 30.59 ? 225 ALA A CA 1 ATOM 1767 C C . ALA A 1 225 ? -6.947 14.115 13.802 1.00 29.77 ? 225 ALA A C 1 ATOM 1768 O O . ALA A 1 225 ? -5.732 14.117 13.594 1.00 28.80 ? 225 ALA A O 1 ATOM 1769 C CB . ALA A 1 225 ? -8.430 12.717 12.403 1.00 31.23 ? 225 ALA A CB 1 ATOM 1770 N N . TYR A 1 226 ? -7.467 14.119 15.008 1.00 29.17 ? 226 TYR A N 1 ATOM 1771 C CA . TYR A 1 226 ? -6.668 13.938 16.195 1.00 29.71 ? 226 TYR A CA 1 ATOM 1772 C C . TYR A 1 226 ? -7.278 12.685 16.846 1.00 29.91 ? 226 TYR A C 1 ATOM 1773 O O . TYR A 1 226 ? -8.381 12.293 16.502 1.00 31.18 ? 226 TYR A O 1 ATOM 1774 C CB . TYR A 1 226 ? -6.871 15.118 17.131 1.00 29.13 ? 226 TYR A CB 1 ATOM 1775 C CG . TYR A 1 226 ? -5.942 16.294 16.949 1.00 29.73 ? 226 TYR A CG 1 ATOM 1776 C CD1 . TYR A 1 226 ? -6.382 17.592 17.234 1.00 29.65 ? 226 TYR A CD1 1 ATOM 1777 C CD2 . TYR A 1 226 ? -4.611 16.116 16.549 1.00 30.72 ? 226 TYR A CD2 1 ATOM 1778 C CE1 . TYR A 1 226 ? -5.558 18.670 17.105 1.00 28.98 ? 226 TYR A CE1 1 ATOM 1779 C CE2 . TYR A 1 226 ? -3.761 17.205 16.414 1.00 29.60 ? 226 TYR A CE2 1 ATOM 1780 C CZ . TYR A 1 226 ? -4.251 18.474 16.698 1.00 30.77 ? 226 TYR A CZ 1 ATOM 1781 O OH . TYR A 1 226 ? -3.433 19.560 16.588 1.00 33.78 ? 226 TYR A OH 1 ATOM 1782 N N . LEU A 1 227 ? -6.597 12.043 17.771 1.00 29.95 ? 227 LEU A N 1 ATOM 1783 C CA . LEU A 1 227 ? -7.246 10.973 18.521 1.00 29.75 ? 227 LEU A CA 1 ATOM 1784 C C . LEU A 1 227 ? -8.336 11.529 19.476 1.00 29.50 ? 227 LEU A C 1 ATOM 1785 O O . LEU A 1 227 ? -8.228 12.645 19.971 1.00 29.20 ? 227 LEU A O 1 ATOM 1786 C CB . LEU A 1 227 ? -6.192 10.206 19.336 1.00 29.19 ? 227 LEU A CB 1 ATOM 1787 C CG . LEU A 1 227 ? -5.140 9.417 18.558 1.00 29.97 ? 227 LEU A CG 1 ATOM 1788 C CD1 . LEU A 1 227 ? -4.064 8.855 19.460 1.00 30.90 ? 227 LEU A CD1 1 ATOM 1789 C CD2 . LEU A 1 227 ? -5.778 8.268 17.768 1.00 30.16 ? 227 LEU A CD2 1 ATOM 1790 N N . PRO A 1 228 ? -9.382 10.753 19.729 1.00 29.65 ? 228 PRO A N 1 ATOM 1791 C CA . PRO A 1 228 ? -10.346 11.103 20.767 1.00 29.97 ? 228 PRO A CA 1 ATOM 1792 C C . PRO A 1 228 ? -9.659 11.307 22.087 1.00 31.31 ? 228 PRO A C 1 ATOM 1793 O O . PRO A 1 228 ? -8.653 10.655 22.357 1.00 31.52 ? 228 PRO A O 1 ATOM 1794 C CB . PRO A 1 228 ? -11.195 9.842 20.874 1.00 30.14 ? 228 PRO A CB 1 ATOM 1795 C CG . PRO A 1 228 ? -10.461 8.803 20.067 1.00 29.27 ? 228 PRO A CG 1 ATOM 1796 C CD . PRO A 1 228 ? -9.775 9.532 19.001 1.00 28.94 ? 228 PRO A CD 1 ATOM 1797 N N . PHE A 1 229 ? -10.178 12.203 22.919 1.00 33.06 ? 229 PHE A N 1 ATOM 1798 C CA . PHE A 1 229 ? -9.623 12.360 24.255 1.00 34.39 ? 229 PHE A CA 1 ATOM 1799 C C . PHE A 1 229 ? -10.031 11.144 25.083 1.00 35.95 ? 229 PHE A C 1 ATOM 1800 O O . PHE A 1 229 ? -11.050 10.537 24.821 1.00 36.34 ? 229 PHE A O 1 ATOM 1801 C CB . PHE A 1 229 ? -10.140 13.640 24.901 1.00 34.22 ? 229 PHE A CB 1 ATOM 1802 C CG . PHE A 1 229 ? -9.516 14.900 24.355 1.00 33.72 ? 229 PHE A CG 1 ATOM 1803 C CD1 . PHE A 1 229 ? -8.123 15.048 24.309 1.00 32.63 ? 229 PHE A CD1 1 ATOM 1804 C CD2 . PHE A 1 229 ? -10.322 15.946 23.889 1.00 32.98 ? 229 PHE A CD2 1 ATOM 1805 C CE1 . PHE A 1 229 ? -7.539 16.211 23.788 1.00 31.97 ? 229 PHE A CE1 1 ATOM 1806 C CE2 . PHE A 1 229 ? -9.758 17.114 23.360 1.00 31.71 ? 229 PHE A CE2 1 ATOM 1807 C CZ . PHE A 1 229 ? -8.355 17.250 23.315 1.00 32.22 ? 229 PHE A CZ 1 ATOM 1808 N N . ASN A 1 230 ? -9.221 10.747 26.049 1.00 38.06 ? 230 ASN A N 1 ATOM 1809 C CA . ASN A 1 230 ? -9.680 9.731 26.965 1.00 40.11 ? 230 ASN A CA 1 ATOM 1810 C C . ASN A 1 230 ? -10.560 10.345 28.043 1.00 42.14 ? 230 ASN A C 1 ATOM 1811 O O . ASN A 1 230 ? -10.260 11.390 28.621 1.00 41.94 ? 230 ASN A O 1 ATOM 1812 C CB . ASN A 1 230 ? -8.548 8.948 27.622 1.00 39.78 ? 230 ASN A CB 1 ATOM 1813 C CG . ASN A 1 230 ? -9.061 7.986 28.716 1.00 40.92 ? 230 ASN A CG 1 ATOM 1814 O OD1 . ASN A 1 230 ? -10.239 7.583 28.727 1.00 40.64 ? 230 ASN A OD1 1 ATOM 1815 N ND2 . ASN A 1 230 ? -8.190 7.642 29.652 1.00 41.88 ? 230 ASN A ND2 1 ATOM 1816 N N . ASN A 1 231 ? -11.666 9.643 28.262 1.00 45.17 ? 231 ASN A N 1 ATOM 1817 C CA . ASN A 1 231 ? -12.672 9.846 29.299 1.00 47.37 ? 231 ASN A CA 1 ATOM 1818 C C . ASN A 1 231 ? -12.156 10.107 30.727 1.00 48.00 ? 231 ASN A C 1 ATOM 1819 O O . ASN A 1 231 ? -12.556 11.061 31.392 1.00 47.90 ? 231 ASN A O 1 ATOM 1820 C CB . ASN A 1 231 ? -13.468 8.525 29.325 1.00 47.89 ? 231 ASN A CB 1 ATOM 1821 C CG . ASN A 1 231 ? -14.659 8.551 30.269 1.00 50.88 ? 231 ASN A CG 1 ATOM 1822 O OD1 . ASN A 1 231 ? -14.514 8.781 31.484 1.00 55.40 ? 231 ASN A OD1 1 ATOM 1823 N ND2 . ASN A 1 231 ? -15.852 8.281 29.720 1.00 52.18 ? 231 ASN A ND2 1 ATOM 1824 N N . LYS A 1 232 ? -11.254 9.232 31.162 1.00 49.00 ? 232 LYS A N 1 ATOM 1825 C CA . LYS A 1 232 ? -10.841 9.088 32.561 1.00 49.96 ? 232 LYS A CA 1 ATOM 1826 C C . LYS A 1 232 ? -10.057 10.169 33.333 1.00 49.43 ? 232 LYS A C 1 ATOM 1827 O O . LYS A 1 232 ? -8.870 10.378 33.123 1.00 49.58 ? 232 LYS A O 1 ATOM 1828 C CB . LYS A 1 232 ? -10.135 7.730 32.703 1.00 50.59 ? 232 LYS A CB 1 ATOM 1829 C CG . LYS A 1 232 ? -10.232 7.112 34.103 1.00 54.39 ? 232 LYS A CG 1 ATOM 1830 C CD . LYS A 1 232 ? -9.944 5.598 34.095 1.00 59.25 ? 232 LYS A CD 1 ATOM 1831 C CE . LYS A 1 232 ? -8.530 5.278 33.594 1.00 62.02 ? 232 LYS A CE 1 ATOM 1832 N NZ . LYS A 1 232 ? -7.516 5.362 34.704 1.00 66.73 ? 232 LYS A NZ 1 ATOM 1833 N N . LYS A 1 233 ? -10.740 10.846 34.249 1.00 49.07 ? 233 LYS A N 1 ATOM 1834 C CA . LYS A 1 233 ? -10.097 11.790 35.164 1.00 48.62 ? 233 LYS A CA 1 ATOM 1835 C C . LYS A 1 233 ? -9.929 10.954 36.411 1.00 47.93 ? 233 LYS A C 1 ATOM 1836 O O . LYS A 1 233 ? -10.790 10.118 36.672 1.00 48.47 ? 233 LYS A O 1 ATOM 1837 C CB . LYS A 1 233 ? -10.997 13.002 35.410 1.00 48.44 ? 233 LYS A CB 1 ATOM 1838 C CG . LYS A 1 233 ? -10.939 13.956 34.248 1.00 49.22 ? 233 LYS A CG 1 ATOM 1839 C CD . LYS A 1 233 ? -12.037 15.022 34.209 1.00 51.80 ? 233 LYS A CD 1 ATOM 1840 C CE . LYS A 1 233 ? -12.162 15.605 32.761 1.00 52.71 ? 233 LYS A CE 1 ATOM 1841 N NZ . LYS A 1 233 ? -12.588 17.035 32.613 1.00 52.83 ? 233 LYS A NZ 1 ATOM 1842 N N . PRO A 1 234 ? -8.839 11.074 37.170 1.00 47.02 ? 234 PRO A N 1 ATOM 1843 C CA . PRO A 1 234 ? -7.710 12.002 36.976 1.00 45.83 ? 234 PRO A CA 1 ATOM 1844 C C . PRO A 1 234 ? -6.876 11.648 35.750 1.00 44.43 ? 234 PRO A C 1 ATOM 1845 O O . PRO A 1 234 ? -6.645 10.473 35.454 1.00 44.39 ? 234 PRO A O 1 ATOM 1846 C CB . PRO A 1 234 ? -6.855 11.758 38.227 1.00 46.05 ? 234 PRO A CB 1 ATOM 1847 C CG . PRO A 1 234 ? -7.196 10.345 38.686 1.00 46.64 ? 234 PRO A CG 1 ATOM 1848 C CD . PRO A 1 234 ? -8.632 10.135 38.292 1.00 47.19 ? 234 PRO A CD 1 ATOM 1849 N N . SER A 1 235 ? -6.401 12.677 35.068 1.00 42.48 ? 235 SER A N 1 ATOM 1850 C CA . SER A 1 235 ? -5.676 12.542 33.823 1.00 40.65 ? 235 SER A CA 1 ATOM 1851 C C . SER A 1 235 ? -4.280 13.149 33.980 1.00 39.27 ? 235 SER A C 1 ATOM 1852 O O . SER A 1 235 ? -4.137 14.298 34.374 1.00 39.24 ? 235 SER A O 1 ATOM 1853 C CB . SER A 1 235 ? -6.465 13.296 32.776 1.00 40.73 ? 235 SER A CB 1 ATOM 1854 O OG . SER A 1 235 ? -5.919 13.133 31.504 1.00 41.63 ? 235 SER A OG 1 ATOM 1855 N N . PRO A 1 236 ? -3.231 12.377 33.711 1.00 37.89 ? 236 PRO A N 1 ATOM 1856 C CA . PRO A 1 236 ? -1.879 12.884 33.935 1.00 36.33 ? 236 PRO A CA 1 ATOM 1857 C C . PRO A 1 236 ? -1.582 13.957 32.932 1.00 35.58 ? 236 PRO A C 1 ATOM 1858 O O . PRO A 1 236 ? -0.796 14.835 33.236 1.00 36.04 ? 236 PRO A O 1 ATOM 1859 C CB . PRO A 1 236 ? -0.993 11.663 33.709 1.00 36.05 ? 236 PRO A CB 1 ATOM 1860 C CG . PRO A 1 236 ? -1.910 10.512 33.731 1.00 36.18 ? 236 PRO A CG 1 ATOM 1861 C CD . PRO A 1 236 ? -3.229 10.995 33.204 1.00 37.42 ? 236 PRO A CD 1 ATOM 1862 N N . CYS A 1 237 ? -2.222 13.924 31.771 1.00 34.71 ? 237 CYS A N 1 ATOM 1863 C CA . CYS A 1 237 ? -1.961 14.932 30.757 1.00 34.03 ? 237 CYS A CA 1 ATOM 1864 C C . CYS A 1 237 ? -2.559 16.249 31.183 1.00 34.13 ? 237 CYS A C 1 ATOM 1865 O O . CYS A 1 237 ? -2.124 17.305 30.754 1.00 34.54 ? 237 CYS A O 1 ATOM 1866 C CB . CYS A 1 237 ? -2.498 14.457 29.401 1.00 33.68 ? 237 CYS A CB 1 ATOM 1867 S SG . CYS A 1 237 ? -1.632 13.003 28.721 1.00 34.11 ? 237 CYS A SG 1 ATOM 1868 N N . GLU A 1 238 ? -3.567 16.109 32.065 1.00 34.47 ? 238 GLU A N 1 ATOM 1869 C CA . GLU A 1 238 ? -4.226 17.248 32.636 1.00 34.27 ? 238 GLU A CA 1 ATOM 1870 C C . GLU A 1 238 ? -3.372 17.823 33.764 1.00 34.86 ? 238 GLU A C 1 ATOM 1871 O O . GLU A 1 238 ? -3.359 19.033 34.009 1.00 35.54 ? 238 GLU A O 1 ATOM 1872 C CB . GLU A 1 238 ? -5.697 16.890 33.087 1.00 34.01 ? 238 GLU A CB 1 ATOM 1873 C CG . GLU A 1 238 ? -6.812 17.039 32.020 1.00 35.29 ? 238 GLU A CG 1 ATOM 1874 C CD . GLU A 1 238 ? -8.238 16.804 32.539 1.00 35.56 ? 238 GLU A CD 1 ATOM 1875 O OE1 . GLU A 1 238 ? -8.941 15.940 31.966 1.00 30.60 ? 238 GLU A OE1 1 ATOM 1876 O OE2 . GLU A 1 238 ? -8.638 17.473 33.503 1.00 35.73 ? 238 GLU A OE2 1 ATOM 1877 N N . PHE A 1 239 ? -2.680 16.922 34.443 1.00 35.35 ? 239 PHE A N 1 ATOM 1878 C CA . PHE A 1 239 ? -1.862 17.293 35.580 1.00 36.03 ? 239 PHE A CA 1 ATOM 1879 C C . PHE A 1 239 ? -0.625 18.127 35.221 1.00 36.32 ? 239 PHE A C 1 ATOM 1880 O O . PHE A 1 239 ? -0.325 19.117 35.907 1.00 36.72 ? 239 PHE A O 1 ATOM 1881 C CB . PHE A 1 239 ? -1.442 16.040 36.343 1.00 35.84 ? 239 PHE A CB 1 ATOM 1882 C CG . PHE A 1 239 ? -0.518 16.249 37.540 1.00 37.00 ? 239 PHE A CG 1 ATOM 1883 C CD1 . PHE A 1 239 ? -1.037 16.470 38.818 1.00 39.37 ? 239 PHE A CD1 1 ATOM 1884 C CD2 . PHE A 1 239 ? 0.869 16.218 37.395 1.00 37.32 ? 239 PHE A CD2 1 ATOM 1885 C CE1 . PHE A 1 239 ? -0.182 16.681 39.895 1.00 38.63 ? 239 PHE A CE1 1 ATOM 1886 C CE2 . PHE A 1 239 ? 1.721 16.418 38.497 1.00 36.33 ? 239 PHE A CE2 1 ATOM 1887 C CZ . PHE A 1 239 ? 1.191 16.655 39.754 1.00 37.34 ? 239 PHE A CZ 1 ATOM 1888 N N . ILE A 1 240 ? 0.088 17.754 34.129 1.00 36.50 ? 240 ILE A N 1 ATOM 1889 C CA . ILE A 1 240 ? 1.347 18.449 33.775 1.00 36.65 ? 240 ILE A CA 1 ATOM 1890 C C . ILE A 1 240 ? 1.125 19.954 33.467 1.00 37.25 ? 240 ILE A C 1 ATOM 1891 O O . ILE A 1 240 ? 2.063 20.732 33.526 1.00 37.68 ? 240 ILE A O 1 ATOM 1892 C CB . ILE A 1 240 ? 2.092 17.691 32.625 1.00 36.36 ? 240 ILE A CB 1 ATOM 1893 C CG1 . ILE A 1 240 ? 1.312 17.765 31.307 1.00 35.69 ? 240 ILE A CG1 1 ATOM 1894 C CG2 . ILE A 1 240 ? 2.314 16.227 33.015 1.00 36.65 ? 240 ILE A CG2 1 ATOM 1895 C CD1 . ILE A 1 240 ? 1.927 18.699 30.289 1.00 34.95 ? 240 ILE A CD1 1 ATOM 1896 N N . ASN A 1 241 ? -0.073 20.358 33.147 1.00 37.49 ? 241 ASN A N 1 ATOM 1897 C CA . ASN A 1 241 ? -0.393 21.746 32.908 1.00 38.33 ? 241 ASN A CA 1 ATOM 1898 C C . ASN A 1 241 ? -1.883 21.838 33.215 1.00 38.39 ? 241 ASN A C 1 ATOM 1899 O O . ASN A 1 241 ? -2.701 21.385 32.435 1.00 39.25 ? 241 ASN A O 1 ATOM 1900 C CB . ASN A 1 241 ? -0.092 22.197 31.461 1.00 38.52 ? 241 ASN A CB 1 ATOM 1901 C CG . ASN A 1 241 ? -0.297 23.683 31.236 1.00 39.60 ? 241 ASN A CG 1 ATOM 1902 O OD1 . ASN A 1 241 ? -1.175 24.276 31.855 1.00 42.06 ? 241 ASN A OD1 1 ATOM 1903 N ND2 . ASN A 1 241 ? 0.504 24.278 30.359 1.00 41.65 ? 241 ASN A ND2 1 ATOM 1904 N N . THR A 1 242 ? -2.239 22.439 34.405 1.00 38.06 ? 242 THR A N 1 ATOM 1905 C CA . THR A 1 242 ? -3.646 22.456 34.802 1.00 37.73 ? 242 THR A CA 1 ATOM 1906 C C . THR A 1 242 ? -4.358 23.666 34.240 1.00 37.09 ? 242 THR A C 1 ATOM 1907 O O . THR A 1 242 ? -5.560 23.821 34.365 1.00 36.93 ? 242 THR A O 1 ATOM 1908 C CB . THR A 1 242 ? -3.818 22.368 36.340 1.00 38.39 ? 242 THR A CB 1 ATOM 1909 O OG1 . THR A 1 242 ? -2.814 23.155 36.999 1.00 38.90 ? 242 THR A OG1 1 ATOM 1910 C CG2 . THR A 1 242 ? -3.574 20.908 36.832 1.00 38.92 ? 242 THR A CG2 1 ATOM 1911 N N . THR A 1 243 ? -3.597 24.520 33.598 1.00 36.43 ? 243 THR A N 1 ATOM 1912 C CA . THR A 1 243 ? -4.141 25.673 32.943 1.00 35.81 ? 243 THR A CA 1 ATOM 1913 C C . THR A 1 243 ? -4.646 25.260 31.584 1.00 35.49 ? 243 THR A C 1 ATOM 1914 O O . THR A 1 243 ? -5.790 25.539 31.238 1.00 36.07 ? 243 THR A O 1 ATOM 1915 C CB . THR A 1 243 ? -3.043 26.693 32.849 1.00 36.04 ? 243 THR A CB 1 ATOM 1916 O OG1 . THR A 1 243 ? -2.851 27.237 34.162 1.00 37.84 ? 243 THR A OG1 1 ATOM 1917 C CG2 . THR A 1 243 ? -3.433 27.920 31.964 1.00 35.86 ? 243 THR A CG2 1 ATOM 1918 N N . ALA A 1 244 ? -3.804 24.580 30.810 1.00 34.75 ? 244 ALA A N 1 ATOM 1919 C CA . ALA A 1 244 ? -4.201 24.103 29.484 1.00 33.73 ? 244 ALA A CA 1 ATOM 1920 C C . ALA A 1 244 ? -5.315 23.069 29.585 1.00 33.23 ? 244 ALA A C 1 ATOM 1921 O O . ALA A 1 244 ? -6.201 23.008 28.747 1.00 31.99 ? 244 ALA A O 1 ATOM 1922 C CB . ALA A 1 244 ? -3.015 23.554 28.731 1.00 33.39 ? 244 ALA A CB 1 ATOM 1923 N N . ARG A 1 245 ? -5.270 22.278 30.646 1.00 33.54 ? 245 ARG A N 1 ATOM 1924 C CA . ARG A 1 245 ? -6.281 21.261 30.886 1.00 34.33 ? 245 ARG A CA 1 ATOM 1925 C C . ARG A 1 245 ? -6.587 20.385 29.690 1.00 33.19 ? 245 ARG A C 1 ATOM 1926 O O . ARG A 1 245 ? -7.766 20.171 29.393 1.00 33.12 ? 245 ARG A O 1 ATOM 1927 C CB . ARG A 1 245 ? -7.605 21.907 31.297 1.00 35.54 ? 245 ARG A CB 1 ATOM 1928 C CG . ARG A 1 245 ? -7.865 22.021 32.790 1.00 40.42 ? 245 ARG A CG 1 ATOM 1929 C CD . ARG A 1 245 ? -9.060 22.936 33.121 1.00 48.40 ? 245 ARG A CD 1 ATOM 1930 N NE . ARG A 1 245 ? -8.761 24.371 32.964 1.00 53.82 ? 245 ARG A NE 1 ATOM 1931 C CZ . ARG A 1 245 ? -8.289 25.151 33.949 1.00 57.01 ? 245 ARG A CZ 1 ATOM 1932 N NH1 . ARG A 1 245 ? -8.049 26.439 33.741 1.00 57.62 ? 245 ARG A NH1 1 ATOM 1933 N NH2 . ARG A 1 245 ? -8.057 24.643 35.155 1.00 58.63 ? 245 ARG A NH2 1 ATOM 1934 N N . VAL A 1 246 ? -5.559 19.882 29.011 1.00 31.88 ? 246 VAL A N 1 ATOM 1935 C CA . VAL A 1 246 ? -5.782 18.948 27.895 1.00 30.61 ? 246 VAL A CA 1 ATOM 1936 C C . VAL A 1 246 ? -5.520 17.498 28.307 1.00 29.41 ? 246 VAL A C 1 ATOM 1937 O O . VAL A 1 246 ? -4.414 17.169 28.702 1.00 28.86 ? 246 VAL A O 1 ATOM 1938 C CB . VAL A 1 246 ? -4.915 19.295 26.662 1.00 30.68 ? 246 VAL A CB 1 ATOM 1939 C CG1 . VAL A 1 246 ? -5.254 18.381 25.502 1.00 30.15 ? 246 VAL A CG1 1 ATOM 1940 C CG2 . VAL A 1 246 ? -5.090 20.741 26.273 1.00 28.40 ? 246 VAL A CG2 1 ATOM 1941 N N . PRO A 1 247 ? -6.547 16.645 28.233 1.00 29.15 ? 247 PRO A N 1 ATOM 1942 C CA . PRO A 1 247 ? -6.420 15.201 28.569 1.00 28.54 ? 247 PRO A CA 1 ATOM 1943 C C . PRO A 1 247 ? -5.608 14.365 27.578 1.00 27.76 ? 247 PRO A C 1 ATOM 1944 O O . PRO A 1 247 ? -5.379 14.776 26.440 1.00 27.26 ? 247 PRO A O 1 ATOM 1945 C CB . PRO A 1 247 ? -7.879 14.687 28.557 1.00 28.24 ? 247 PRO A CB 1 ATOM 1946 C CG . PRO A 1 247 ? -8.647 15.641 27.788 1.00 28.10 ? 247 PRO A CG 1 ATOM 1947 C CD . PRO A 1 247 ? -7.931 17.001 27.853 1.00 29.05 ? 247 PRO A CD 1 ATOM 1948 N N . CYS A 1 248 ? -5.185 13.190 28.038 1.00 27.51 ? 248 CYS A N 1 ATOM 1949 C CA . CYS A 1 248 ? -4.453 12.206 27.226 1.00 27.07 ? 248 CYS A CA 1 ATOM 1950 C C . CYS A 1 248 ? -5.340 11.687 26.125 1.00 25.98 ? 248 CYS A C 1 ATOM 1951 O O . CYS A 1 248 ? -6.561 11.824 26.158 1.00 25.32 ? 248 CYS A O 1 ATOM 1952 C CB . CYS A 1 248 ? -4.010 11.034 28.086 1.00 27.06 ? 248 CYS A CB 1 ATOM 1953 S SG . CYS A 1 248 ? -3.022 11.493 29.550 1.00 31.09 ? 248 CYS A SG 1 ATOM 1954 N N . PHE A 1 249 ? -4.714 11.108 25.125 1.00 25.80 ? 249 PHE A N 1 ATOM 1955 C CA . PHE A 1 249 ? -5.443 10.593 23.974 1.00 25.35 ? 249 PHE A CA 1 ATOM 1956 C C . PHE A 1 249 ? -5.973 9.184 24.266 1.00 24.78 ? 249 PHE A C 1 ATOM 1957 O O . PHE A 1 249 ? -5.371 8.453 25.020 1.00 25.26 ? 249 PHE A O 1 ATOM 1958 C CB . PHE A 1 249 ? -4.525 10.606 22.769 1.00 24.78 ? 249 PHE A CB 1 ATOM 1959 C CG . PHE A 1 249 ? -4.284 11.965 22.211 1.00 25.49 ? 249 PHE A CG 1 ATOM 1960 C CD1 . PHE A 1 249 ? -5.333 12.734 21.751 1.00 29.09 ? 249 PHE A CD1 1 ATOM 1961 C CD2 . PHE A 1 249 ? -3.018 12.481 22.119 1.00 25.55 ? 249 PHE A CD2 1 ATOM 1962 C CE1 . PHE A 1 249 ? -5.108 14.002 21.204 1.00 26.15 ? 249 PHE A CE1 1 ATOM 1963 C CE2 . PHE A 1 249 ? -2.805 13.748 21.594 1.00 24.81 ? 249 PHE A CE2 1 ATOM 1964 C CZ . PHE A 1 249 ? -3.856 14.495 21.136 1.00 23.61 ? 249 PHE A CZ 1 ATOM 1965 N N . LEU A 1 250 ? -7.127 8.834 23.712 1.00 24.73 ? 250 LEU A N 1 ATOM 1966 C CA . LEU A 1 250 ? -7.679 7.477 23.843 1.00 24.32 ? 250 LEU A CA 1 ATOM 1967 C C . LEU A 1 250 ? -7.257 6.639 22.630 1.00 23.70 ? 250 LEU A C 1 ATOM 1968 O O . LEU A 1 250 ? -7.680 6.926 21.522 1.00 24.56 ? 250 LEU A O 1 ATOM 1969 C CB . LEU A 1 250 ? -9.198 7.533 23.914 1.00 24.25 ? 250 LEU A CB 1 ATOM 1970 C CG . LEU A 1 250 ? -9.745 6.136 24.120 1.00 25.50 ? 250 LEU A CG 1 ATOM 1971 C CD1 . LEU A 1 250 ? -9.137 5.576 25.370 1.00 27.72 ? 250 LEU A CD1 1 ATOM 1972 C CD2 . LEU A 1 250 ? -11.246 6.082 24.202 1.00 26.19 ? 250 LEU A CD2 1 ATOM 1973 N N . ALA A 1 251 ? -6.412 5.636 22.824 1.00 22.50 ? 251 ALA A N 1 ATOM 1974 C CA . ALA A 1 251 ? -5.953 4.815 21.711 1.00 21.74 ? 251 ALA A CA 1 ATOM 1975 C C . ALA A 1 251 ? -5.989 3.329 21.997 1.00 21.62 ? 251 ALA A C 1 ATOM 1976 O O . ALA A 1 251 ? -6.323 2.893 23.105 1.00 21.40 ? 251 ALA A O 1 ATOM 1977 C CB . ALA A 1 251 ? -4.587 5.203 21.294 1.00 21.58 ? 251 ALA A CB 1 ATOM 1978 N N . GLY A 1 252 ? -5.652 2.556 20.971 1.00 21.21 ? 252 GLY A N 1 ATOM 1979 C CA . GLY A 1 252 ? -5.703 1.116 21.032 1.00 20.94 ? 252 GLY A CA 1 ATOM 1980 C C . GLY A 1 252 ? -4.835 0.596 22.145 1.00 20.94 ? 252 GLY A C 1 ATOM 1981 O O . GLY A 1 252 ? -5.129 -0.431 22.689 1.00 21.13 ? 252 GLY A O 1 ATOM 1982 N N . ASP A 1 253 ? -3.785 1.323 22.495 1.00 21.09 ? 253 ASP A N 1 ATOM 1983 C CA . ASP A 1 253 ? -2.885 0.927 23.556 1.00 21.62 ? 253 ASP A CA 1 ATOM 1984 C C . ASP A 1 253 ? -2.793 2.007 24.620 1.00 22.84 ? 253 ASP A C 1 ATOM 1985 O O . ASP A 1 253 ? -2.645 3.215 24.327 1.00 23.22 ? 253 ASP A O 1 ATOM 1986 C CB . ASP A 1 253 ? -1.506 0.610 22.956 1.00 22.01 ? 253 ASP A CB 1 ATOM 1987 C CG . ASP A 1 253 ? -0.446 0.264 24.000 1.00 20.30 ? 253 ASP A CG 1 ATOM 1988 O OD1 . ASP A 1 253 ? -0.136 -0.928 24.095 1.00 20.17 ? 253 ASP A OD1 1 ATOM 1989 O OD2 . ASP A 1 253 ? 0.146 1.095 24.734 1.00 15.81 ? 253 ASP A OD2 1 ATOM 1990 N N . PHE A 1 254 ? -2.846 1.576 25.872 1.00 24.06 ? 254 PHE A N 1 ATOM 1991 C CA . PHE A 1 254 ? -2.862 2.527 26.994 1.00 25.49 ? 254 PHE A CA 1 ATOM 1992 C C . PHE A 1 254 ? -1.667 3.514 27.148 1.00 24.17 ? 254 PHE A C 1 ATOM 1993 O O . PHE A 1 254 ? -1.833 4.592 27.721 1.00 24.48 ? 254 PHE A O 1 ATOM 1994 C CB . PHE A 1 254 ? -3.200 1.780 28.308 1.00 26.75 ? 254 PHE A CB 1 ATOM 1995 C CG . PHE A 1 254 ? -4.661 1.304 28.378 1.00 31.20 ? 254 PHE A CG 1 ATOM 1996 C CD1 . PHE A 1 254 ? -4.983 -0.036 28.194 1.00 34.12 ? 254 PHE A CD1 1 ATOM 1997 C CD2 . PHE A 1 254 ? -5.707 2.220 28.603 1.00 35.46 ? 254 PHE A CD2 1 ATOM 1998 C CE1 . PHE A 1 254 ? -6.314 -0.464 28.226 1.00 36.44 ? 254 PHE A CE1 1 ATOM 1999 C CE2 . PHE A 1 254 ? -7.053 1.806 28.641 1.00 37.32 ? 254 PHE A CE2 1 ATOM 2000 C CZ . PHE A 1 254 ? -7.355 0.457 28.455 1.00 37.48 ? 254 PHE A CZ 1 ATOM 2001 N N . ARG A 1 255 ? -0.483 3.162 26.637 1.00 22.33 ? 255 ARG A N 1 ATOM 2002 C CA . ARG A 1 255 ? 0.684 4.019 26.817 1.00 20.23 ? 255 ARG A CA 1 ATOM 2003 C C . ARG A 1 255 ? 0.849 5.116 25.765 1.00 19.67 ? 255 ARG A C 1 ATOM 2004 O O . ARG A 1 255 ? 1.827 5.861 25.823 1.00 19.62 ? 255 ARG A O 1 ATOM 2005 C CB . ARG A 1 255 ? 2.011 3.243 26.859 1.00 20.13 ? 255 ARG A CB 1 ATOM 2006 C CG . ARG A 1 255 ? 2.139 1.997 27.671 1.00 17.22 ? 255 ARG A CG 1 ATOM 2007 C CD . ARG A 1 255 ? 2.009 0.817 26.770 1.00 19.35 ? 255 ARG A CD 1 ATOM 2008 N NE . ARG A 1 255 ? 3.027 -0.201 26.931 1.00 18.78 ? 255 ARG A NE 1 ATOM 2009 C CZ . ARG A 1 255 ? 3.069 -1.294 26.188 1.00 13.89 ? 255 ARG A CZ 1 ATOM 2010 N NH1 . ARG A 1 255 ? 2.157 -1.490 25.250 1.00 9.20 ? 255 ARG A NH1 1 ATOM 2011 N NH2 . ARG A 1 255 ? 4.024 -2.176 26.385 1.00 10.59 ? 255 ARG A NH2 1 ATOM 2012 N N . ALA A 1 256 ? -0.094 5.223 24.834 1.00 18.79 ? 256 ALA A N 1 ATOM 2013 C CA . ALA A 1 256 ? -0.030 6.168 23.705 1.00 17.91 ? 256 ALA A CA 1 ATOM 2014 C C . ALA A 1 256 ? 0.508 7.563 23.993 1.00 17.41 ? 256 ALA A C 1 ATOM 2015 O O . ALA A 1 256 ? 1.265 8.118 23.208 1.00 16.98 ? 256 ALA A O 1 ATOM 2016 C CB . ALA A 1 256 ? -1.400 6.283 23.041 1.00 17.58 ? 256 ALA A CB 1 ATOM 2017 N N . SER A 1 257 ? 0.090 8.148 25.095 1.00 17.67 ? 257 SER A N 1 ATOM 2018 C CA . SER A 1 257 ? 0.524 9.498 25.406 1.00 18.42 ? 257 SER A CA 1 ATOM 2019 C C . SER A 1 257 ? 1.651 9.613 26.404 1.00 18.09 ? 257 SER A C 1 ATOM 2020 O O . SER A 1 257 ? 1.848 10.636 27.042 1.00 19.09 ? 257 SER A O 1 ATOM 2021 C CB . SER A 1 257 ? -0.627 10.463 25.741 1.00 18.57 ? 257 SER A CB 1 ATOM 2022 O OG . SER A 1 257 ? -1.707 9.901 26.444 1.00 21.96 ? 257 SER A OG 1 ATOM 2023 N N . GLU A 1 258 ? 2.477 8.543 26.528 1.00 17.56 ? 258 GLU A N 1 ATOM 2024 C CA . GLU A 1 258 ? 3.668 8.617 27.387 1.00 16.73 ? 258 GLU A CA 1 ATOM 2025 C C . GLU A 1 258 ? 4.584 9.691 26.887 1.00 16.54 ? 258 GLU A C 1 ATOM 2026 O O . GLU A 1 258 ? 5.330 10.259 27.682 1.00 16.60 ? 258 GLU A O 1 ATOM 2027 C CB . GLU A 1 258 ? 4.486 7.288 27.446 1.00 16.90 ? 258 GLU A CB 1 ATOM 2028 C CG . GLU A 1 258 ? 5.750 7.365 28.342 1.00 15.32 ? 258 GLU A CG 1 ATOM 2029 C CD . GLU A 1 258 ? 7.058 7.526 27.620 1.00 14.84 ? 258 GLU A CD 1 ATOM 2030 O OE1 . GLU A 1 258 ? 7.010 7.581 26.384 1.00 14.36 ? 258 GLU A OE1 1 ATOM 2031 O OE2 . GLU A 1 258 ? 8.114 7.609 28.269 1.00 15.22 ? 258 GLU A OE2 1 ATOM 2032 N N . GLN A 1 259 ? 4.559 10.016 25.604 1.00 15.86 ? 259 GLN A N 1 ATOM 2033 C CA . GLN A 1 259 ? 5.427 11.078 25.125 1.00 15.59 ? 259 GLN A CA 1 ATOM 2034 C C . GLN A 1 259 ? 4.936 11.642 23.786 1.00 16.62 ? 259 GLN A C 1 ATOM 2035 O O . GLN A 1 259 ? 4.498 10.910 22.874 1.00 18.05 ? 259 GLN A O 1 ATOM 2036 C CB . GLN A 1 259 ? 6.907 10.687 25.165 1.00 14.59 ? 259 GLN A CB 1 ATOM 2037 C CG . GLN A 1 259 ? 7.304 9.453 24.403 1.00 14.37 ? 259 GLN A CG 1 ATOM 2038 C CD . GLN A 1 259 ? 7.845 9.814 23.017 1.00 14.55 ? 259 GLN A CD 1 ATOM 2039 O OE1 . GLN A 1 259 ? 7.992 11.000 22.717 1.00 15.47 ? 259 GLN A OE1 1 ATOM 2040 N NE2 . GLN A 1 259 ? 8.084 8.817 22.162 1.00 10.80 ? 259 GLN A NE2 1 ATOM 2041 N N . ILE A 1 260 ? 4.926 12.959 23.698 1.00 16.75 ? 260 ILE A N 1 ATOM 2042 C CA . ILE A 1 260 ? 4.442 13.669 22.526 1.00 16.46 ? 260 ILE A CA 1 ATOM 2043 C C . ILE A 1 260 ? 4.788 13.017 21.202 1.00 16.73 ? 260 ILE A C 1 ATOM 2044 O O . ILE A 1 260 ? 3.953 12.978 20.294 1.00 17.41 ? 260 ILE A O 1 ATOM 2045 C CB . ILE A 1 260 ? 4.962 15.074 22.568 1.00 16.50 ? 260 ILE A CB 1 ATOM 2046 C CG1 . ILE A 1 260 ? 4.143 15.977 21.680 1.00 17.29 ? 260 ILE A CG1 1 ATOM 2047 C CG2 . ILE A 1 260 ? 6.443 15.117 22.215 1.00 16.83 ? 260 ILE A CG2 1 ATOM 2048 C CD1 . ILE A 1 260 ? 4.285 17.463 22.051 1.00 20.05 ? 260 ILE A CD1 1 ATOM 2049 N N . LEU A 1 261 ? 5.998 12.487 21.079 1.00 16.57 ? 261 LEU A N 1 ATOM 2050 C CA . LEU A 1 261 ? 6.401 11.856 19.824 1.00 16.63 ? 261 LEU A CA 1 ATOM 2051 C C . LEU A 1 261 ? 5.728 10.510 19.578 1.00 16.73 ? 261 LEU A C 1 ATOM 2052 O O . LEU A 1 261 ? 5.534 10.085 18.428 1.00 16.87 ? 261 LEU A O 1 ATOM 2053 C CB . LEU A 1 261 ? 7.913 11.691 19.761 1.00 16.53 ? 261 LEU A CB 1 ATOM 2054 C CG . LEU A 1 261 ? 8.692 12.581 18.803 1.00 14.87 ? 261 LEU A CG 1 ATOM 2055 C CD1 . LEU A 1 261 ? 8.012 13.901 18.564 1.00 13.79 ? 261 LEU A CD1 1 ATOM 2056 C CD2 . LEU A 1 261 ? 10.084 12.764 19.337 1.00 12.45 ? 261 LEU A CD2 1 ATOM 2057 N N . LEU A 1 262 ? 5.387 9.821 20.656 1.00 16.37 ? 262 LEU A N 1 ATOM 2058 C CA . LEU A 1 262 ? 4.711 8.541 20.502 1.00 15.92 ? 262 LEU A CA 1 ATOM 2059 C C . LEU A 1 262 ? 3.262 8.805 20.166 1.00 15.95 ? 262 LEU A C 1 ATOM 2060 O O . LEU A 1 262 ? 2.714 8.146 19.304 1.00 15.71 ? 262 LEU A O 1 ATOM 2061 C CB . LEU A 1 262 ? 4.860 7.686 21.751 1.00 15.19 ? 262 LEU A CB 1 ATOM 2062 C CG . LEU A 1 262 ? 3.866 6.556 21.936 1.00 13.47 ? 262 LEU A CG 1 ATOM 2063 C CD1 . LEU A 1 262 ? 4.128 5.446 20.920 1.00 13.80 ? 262 LEU A CD1 1 ATOM 2064 C CD2 . LEU A 1 262 ? 3.948 6.009 23.363 1.00 10.12 ? 262 LEU A CD2 1 ATOM 2065 N N . ALA A 1 263 ? 2.652 9.776 20.846 1.00 16.37 ? 263 ALA A N 1 ATOM 2066 C CA . ALA A 1 263 ? 1.268 10.191 20.545 1.00 16.43 ? 263 ALA A CA 1 ATOM 2067 C C . ALA A 1 263 ? 1.192 10.683 19.111 1.00 16.69 ? 263 ALA A C 1 ATOM 2068 O O . ALA A 1 263 ? 0.187 10.492 18.418 1.00 17.13 ? 263 ALA A O 1 ATOM 2069 C CB . ALA A 1 263 ? 0.814 11.274 21.490 1.00 15.78 ? 263 ALA A CB 1 ATOM 2070 N N . THR A 1 264 ? 2.263 11.316 18.654 1.00 17.13 ? 264 THR A N 1 ATOM 2071 C CA . THR A 1 264 ? 2.310 11.747 17.269 1.00 17.89 ? 264 THR A CA 1 ATOM 2072 C C . THR A 1 264 ? 2.161 10.545 16.325 1.00 18.34 ? 264 THR A C 1 ATOM 2073 O O . THR A 1 264 ? 1.260 10.509 15.504 1.00 19.21 ? 264 THR A O 1 ATOM 2074 C CB . THR A 1 264 ? 3.582 12.502 17.021 1.00 17.94 ? 264 THR A CB 1 ATOM 2075 O OG1 . THR A 1 264 ? 3.498 13.767 17.703 1.00 19.36 ? 264 THR A OG1 1 ATOM 2076 C CG2 . THR A 1 264 ? 3.695 12.859 15.541 1.00 16.77 ? 264 THR A CG2 1 ATOM 2077 N N . ALA A 1 265 ? 3.018 9.550 16.479 1.00 18.29 ? 265 ALA A N 1 ATOM 2078 C CA . ALA A 1 265 ? 2.942 8.331 15.706 1.00 18.44 ? 265 ALA A CA 1 ATOM 2079 C C . ALA A 1 265 ? 1.571 7.668 15.714 1.00 19.20 ? 265 ALA A C 1 ATOM 2080 O O . ALA A 1 265 ? 1.088 7.153 14.677 1.00 18.67 ? 265 ALA A O 1 ATOM 2081 C CB . ALA A 1 265 ? 3.947 7.368 16.222 1.00 18.80 ? 265 ALA A CB 1 ATOM 2082 N N . HIS A 1 266 ? 0.937 7.638 16.874 1.00 20.19 ? 266 HIS A N 1 ATOM 2083 C CA . HIS A 1 266 ? -0.373 7.003 16.942 1.00 21.49 ? 266 HIS A CA 1 ATOM 2084 C C . HIS A 1 266 ? -1.343 7.731 16.039 1.00 23.02 ? 266 HIS A C 1 ATOM 2085 O O . HIS A 1 266 ? -2.170 7.106 15.376 1.00 23.90 ? 266 HIS A O 1 ATOM 2086 C CB . HIS A 1 266 ? -0.919 7.005 18.353 1.00 21.10 ? 266 HIS A CB 1 ATOM 2087 C CG . HIS A 1 266 ? -0.569 5.782 19.149 1.00 21.44 ? 266 HIS A CG 1 ATOM 2088 N ND1 . HIS A 1 266 ? -1.379 4.668 19.199 1.00 20.69 ? 266 HIS A ND1 1 ATOM 2089 C CD2 . HIS A 1 266 ? 0.486 5.518 19.960 1.00 21.30 ? 266 HIS A CD2 1 ATOM 2090 C CE1 . HIS A 1 266 ? -0.831 3.768 19.997 1.00 22.23 ? 266 HIS A CE1 1 ATOM 2091 N NE2 . HIS A 1 266 ? 0.297 4.263 20.477 1.00 21.56 ? 266 HIS A NE2 1 ATOM 2092 N N . THR A 1 267 ? -1.235 9.061 16.025 1.00 24.11 ? 267 THR A N 1 ATOM 2093 C CA . THR A 1 267 ? -2.096 9.910 15.220 1.00 24.55 ? 267 THR A CA 1 ATOM 2094 C C . THR A 1 267 ? -1.957 9.609 13.714 1.00 25.57 ? 267 THR A C 1 ATOM 2095 O O . THR A 1 267 ? -2.973 9.546 12.978 1.00 26.07 ? 267 THR A O 1 ATOM 2096 C CB . THR A 1 267 ? -1.792 11.404 15.536 1.00 24.48 ? 267 THR A CB 1 ATOM 2097 O OG1 . THR A 1 267 ? -1.851 11.614 16.953 1.00 24.74 ? 267 THR A OG1 1 ATOM 2098 C CG2 . THR A 1 267 ? -2.899 12.291 15.053 1.00 23.10 ? 267 THR A CG2 1 ATOM 2099 N N . LEU A 1 268 ? -0.718 9.456 13.245 1.00 25.32 ? 268 LEU A N 1 ATOM 2100 C CA . LEU A 1 268 ? -0.508 9.112 11.854 1.00 25.56 ? 268 LEU A CA 1 ATOM 2101 C C . LEU A 1 268 ? -1.207 7.799 11.509 1.00 25.88 ? 268 LEU A C 1 ATOM 2102 O O . LEU A 1 268 ? -1.844 7.693 10.449 1.00 26.02 ? 268 LEU A O 1 ATOM 2103 C CB . LEU A 1 268 ? 0.964 9.013 11.547 1.00 25.67 ? 268 LEU A CB 1 ATOM 2104 C CG . LEU A 1 268 ? 1.624 10.288 11.030 1.00 27.41 ? 268 LEU A CG 1 ATOM 2105 C CD1 . LEU A 1 268 ? 1.277 11.470 11.893 1.00 29.46 ? 268 LEU A CD1 1 ATOM 2106 C CD2 . LEU A 1 268 ? 3.112 10.088 11.050 1.00 30.52 ? 268 LEU A CD2 1 ATOM 2107 N N . LEU A 1 269 ? -1.108 6.812 12.413 1.00 25.86 ? 269 LEU A N 1 ATOM 2108 C CA . LEU A 1 269 ? -1.739 5.499 12.231 1.00 25.22 ? 269 LEU A CA 1 ATOM 2109 C C . LEU A 1 269 ? -3.263 5.523 12.270 1.00 25.30 ? 269 LEU A C 1 ATOM 2110 O O . LEU A 1 269 ? -3.914 4.877 11.479 1.00 24.81 ? 269 LEU A O 1 ATOM 2111 C CB . LEU A 1 269 ? -1.221 4.516 13.259 1.00 25.48 ? 269 LEU A CB 1 ATOM 2112 C CG . LEU A 1 269 ? 0.266 4.167 13.133 1.00 26.52 ? 269 LEU A CG 1 ATOM 2113 C CD1 . LEU A 1 269 ? 0.549 3.180 14.238 1.00 26.74 ? 269 LEU A CD1 1 ATOM 2114 C CD2 . LEU A 1 269 ? 0.644 3.560 11.747 1.00 24.80 ? 269 LEU A CD2 1 ATOM 2115 N N . LEU A 1 270 ? -3.849 6.248 13.202 1.00 25.90 ? 270 LEU A N 1 ATOM 2116 C CA . LEU A 1 270 ? -5.292 6.395 13.181 1.00 26.81 ? 270 LEU A CA 1 ATOM 2117 C C . LEU A 1 270 ? -5.708 7.009 11.848 1.00 27.78 ? 270 LEU A C 1 ATOM 2118 O O . LEU A 1 270 ? -6.629 6.525 11.174 1.00 29.16 ? 270 LEU A O 1 ATOM 2119 C CB . LEU A 1 270 ? -5.728 7.340 14.269 1.00 26.84 ? 270 LEU A CB 1 ATOM 2120 C CG . LEU A 1 270 ? -7.233 7.469 14.419 1.00 27.31 ? 270 LEU A CG 1 ATOM 2121 C CD1 . LEU A 1 270 ? -7.777 6.321 15.255 1.00 27.52 ? 270 LEU A CD1 1 ATOM 2122 C CD2 . LEU A 1 270 ? -7.538 8.784 15.093 1.00 27.27 ? 270 LEU A CD2 1 ATOM 2123 N N . ARG A 1 271 ? -4.998 8.058 11.453 1.00 27.68 ? 271 ARG A N 1 ATOM 2124 C CA . ARG A 1 271 ? -5.308 8.776 10.238 1.00 27.44 ? 271 ARG A CA 1 ATOM 2125 C C . ARG A 1 271 ? -5.238 7.882 9.021 1.00 27.82 ? 271 ARG A C 1 ATOM 2126 O O . ARG A 1 271 ? -6.048 7.985 8.106 1.00 29.14 ? 271 ARG A O 1 ATOM 2127 C CB . ARG A 1 271 ? -4.362 9.966 10.065 1.00 27.45 ? 271 ARG A CB 1 ATOM 2128 C CG . ARG A 1 271 ? -4.720 11.163 10.910 1.00 25.42 ? 271 ARG A CG 1 ATOM 2129 C CD . ARG A 1 271 ? -3.824 12.334 10.626 1.00 24.19 ? 271 ARG A CD 1 ATOM 2130 N NE . ARG A 1 271 ? -3.920 13.367 11.641 1.00 20.18 ? 271 ARG A NE 1 ATOM 2131 C CZ . ARG A 1 271 ? -3.162 14.422 11.649 1.00 17.55 ? 271 ARG A CZ 1 ATOM 2132 N NH1 . ARG A 1 271 ? -2.292 14.565 10.674 1.00 19.89 ? 271 ARG A NH1 1 ATOM 2133 N NH2 . ARG A 1 271 ? -3.277 15.339 12.601 1.00 17.55 ? 271 ARG A NH2 1 ATOM 2134 N N . GLU A 1 272 ? -4.253 7.021 8.955 1.00 27.42 ? 272 GLU A N 1 ATOM 2135 C CA . GLU A 1 272 ? -4.206 6.135 7.814 1.00 26.84 ? 272 GLU A CA 1 ATOM 2136 C C . GLU A 1 272 ? -5.397 5.168 7.843 1.00 26.72 ? 272 GLU A C 1 ATOM 2137 O O . GLU A 1 272 ? -5.850 4.716 6.802 1.00 27.22 ? 272 GLU A O 1 ATOM 2138 C CB . GLU A 1 272 ? -2.896 5.379 7.849 1.00 26.90 ? 272 GLU A CB 1 ATOM 2139 C CG . GLU A 1 272 ? -2.682 4.390 6.746 1.00 28.29 ? 272 GLU A CG 1 ATOM 2140 C CD . GLU A 1 272 ? -2.575 5.028 5.399 1.00 31.37 ? 272 GLU A CD 1 ATOM 2141 O OE1 . GLU A 1 272 ? -2.711 6.257 5.303 1.00 33.33 ? 272 GLU A OE1 1 ATOM 2142 O OE2 . GLU A 1 272 ? -2.333 4.284 4.435 1.00 35.47 ? 272 GLU A OE2 1 ATOM 2143 N N . HIS A 1 273 ? -5.931 4.831 9.008 1.00 26.00 ? 273 HIS A N 1 ATOM 2144 C CA . HIS A 1 273 ? -7.041 3.898 8.966 1.00 26.44 ? 273 HIS A CA 1 ATOM 2145 C C . HIS A 1 273 ? -8.287 4.532 8.314 1.00 26.32 ? 273 HIS A C 1 ATOM 2146 O O . HIS A 1 273 ? -8.942 3.963 7.457 1.00 25.72 ? 273 HIS A O 1 ATOM 2147 C CB . HIS A 1 273 ? -7.432 3.359 10.348 1.00 26.51 ? 273 HIS A CB 1 ATOM 2148 C CG . HIS A 1 273 ? -8.758 2.662 10.337 1.00 27.41 ? 273 HIS A CG 1 ATOM 2149 N ND1 . HIS A 1 273 ? -8.883 1.295 10.211 1.00 28.34 ? 273 HIS A ND1 1 ATOM 2150 C CD2 . HIS A 1 273 ? -10.022 3.154 10.347 1.00 29.02 ? 273 HIS A CD2 1 ATOM 2151 C CE1 . HIS A 1 273 ? -10.165 0.969 10.186 1.00 27.55 ? 273 HIS A CE1 1 ATOM 2152 N NE2 . HIS A 1 273 ? -10.877 2.079 10.269 1.00 28.76 ? 273 HIS A NE2 1 ATOM 2153 N N . ASN A 1 274 ? -8.655 5.689 8.804 1.00 25.89 ? 274 ASN A N 1 ATOM 2154 C CA . ASN A 1 274 ? -9.731 6.391 8.199 1.00 26.29 ? 274 ASN A CA 1 ATOM 2155 C C . ASN A 1 274 ? -9.471 6.677 6.705 1.00 26.85 ? 274 ASN A C 1 ATOM 2156 O O . ASN A 1 274 ? -10.346 6.489 5.872 1.00 27.88 ? 274 ASN A O 1 ATOM 2157 C CB . ASN A 1 274 ? -9.970 7.672 8.988 1.00 25.69 ? 274 ASN A CB 1 ATOM 2158 C CG . ASN A 1 274 ? -10.640 7.400 10.290 1.00 25.08 ? 274 ASN A CG 1 ATOM 2159 O OD1 . ASN A 1 274 ? -11.066 6.275 10.556 1.00 23.31 ? 274 ASN A OD1 1 ATOM 2160 N ND2 . ASN A 1 274 ? -10.741 8.413 11.119 1.00 24.97 ? 274 ASN A ND2 1 ATOM 2161 N N . ARG A 1 275 ? -8.275 7.109 6.352 1.00 26.84 ? 275 ARG A N 1 ATOM 2162 C CA . ARG A 1 275 ? -7.968 7.401 4.957 1.00 27.68 ? 275 ARG A CA 1 ATOM 2163 C C . ARG A 1 275 ? -8.230 6.233 4.039 1.00 27.93 ? 275 ARG A C 1 ATOM 2164 O O . ARG A 1 275 ? -8.652 6.382 2.895 1.00 28.25 ? 275 ARG A O 1 ATOM 2165 C CB . ARG A 1 275 ? -6.479 7.706 4.827 1.00 27.82 ? 275 ARG A CB 1 ATOM 2166 C CG . ARG A 1 275 ? -6.128 8.591 3.675 1.00 27.96 ? 275 ARG A CG 1 ATOM 2167 C CD . ARG A 1 275 ? -4.749 8.363 3.141 1.00 27.61 ? 275 ARG A CD 1 ATOM 2168 N NE . ARG A 1 275 ? -4.784 7.200 2.301 1.00 29.42 ? 275 ARG A NE 1 ATOM 2169 C CZ . ARG A 1 275 ? -3.766 6.424 2.092 1.00 31.04 ? 275 ARG A CZ 1 ATOM 2170 N NH1 . ARG A 1 275 ? -2.608 6.690 2.658 1.00 31.97 ? 275 ARG A NH1 1 ATOM 2171 N NH2 . ARG A 1 275 ? -3.903 5.371 1.314 1.00 32.67 ? 275 ARG A NH2 1 ATOM 2172 N N . LEU A 1 276 ? -7.950 5.069 4.584 1.00 28.46 ? 276 LEU A N 1 ATOM 2173 C CA . LEU A 1 276 ? -7.896 3.816 3.865 1.00 29.22 ? 276 LEU A CA 1 ATOM 2174 C C . LEU A 1 276 ? -9.285 3.289 3.759 1.00 30.06 ? 276 LEU A C 1 ATOM 2175 O O . LEU A 1 276 ? -9.660 2.621 2.798 1.00 29.64 ? 276 LEU A O 1 ATOM 2176 C CB . LEU A 1 276 ? -7.082 2.867 4.737 1.00 29.02 ? 276 LEU A CB 1 ATOM 2177 C CG . LEU A 1 276 ? -5.962 1.939 4.310 1.00 27.87 ? 276 LEU A CG 1 ATOM 2178 C CD1 . LEU A 1 276 ? -5.414 2.248 2.930 1.00 28.11 ? 276 LEU A CD1 1 ATOM 2179 C CD2 . LEU A 1 276 ? -4.889 1.996 5.412 1.00 25.24 ? 276 LEU A CD2 1 ATOM 2180 N N . ALA A 1 277 ? -10.055 3.602 4.782 1.00 31.41 ? 277 ALA A N 1 ATOM 2181 C CA . ALA A 1 277 ? -11.422 3.182 4.819 1.00 33.40 ? 277 ALA A CA 1 ATOM 2182 C C . ALA A 1 277 ? -12.232 4.053 3.859 1.00 35.03 ? 277 ALA A C 1 ATOM 2183 O O . ALA A 1 277 ? -13.058 3.536 3.093 1.00 35.63 ? 277 ALA A O 1 ATOM 2184 C CB . ALA A 1 277 ? -11.968 3.259 6.234 1.00 32.91 ? 277 ALA A CB 1 ATOM 2185 N N . ARG A 1 278 ? -12.002 5.364 3.852 1.00 36.60 ? 278 ARG A N 1 ATOM 2186 C CA . ARG A 1 278 ? -12.818 6.179 2.963 1.00 38.43 ? 278 ARG A CA 1 ATOM 2187 C C . ARG A 1 278 ? -12.465 5.920 1.499 1.00 39.57 ? 278 ARG A C 1 ATOM 2188 O O . ARG A 1 278 ? -13.341 5.833 0.632 1.00 40.33 ? 278 ARG A O 1 ATOM 2189 C CB . ARG A 1 278 ? -12.874 7.637 3.373 1.00 38.30 ? 278 ARG A CB 1 ATOM 2190 C CG . ARG A 1 278 ? -11.631 8.396 3.224 1.00 40.60 ? 278 ARG A CG 1 ATOM 2191 C CD . ARG A 1 278 ? -11.830 9.827 3.654 1.00 44.53 ? 278 ARG A CD 1 ATOM 2192 N NE . ARG A 1 278 ? -12.533 9.958 4.936 1.00 46.93 ? 278 ARG A NE 1 ATOM 2193 C CZ . ARG A 1 278 ? -11.915 10.255 6.083 1.00 48.04 ? 278 ARG A CZ 1 ATOM 2194 N NH1 . ARG A 1 278 ? -10.590 10.409 6.082 1.00 47.35 ? 278 ARG A NH1 1 ATOM 2195 N NH2 . ARG A 1 278 ? -12.604 10.389 7.224 1.00 47.57 ? 278 ARG A NH2 1 ATOM 2196 N N . GLU A 1 279 ? -11.180 5.719 1.250 1.00 40.56 ? 279 GLU A N 1 ATOM 2197 C CA . GLU A 1 279 ? -10.735 5.254 -0.050 1.00 41.63 ? 279 GLU A CA 1 ATOM 2198 C C . GLU A 1 279 ? -11.486 3.965 -0.440 1.00 41.72 ? 279 GLU A C 1 ATOM 2199 O O . GLU A 1 279 ? -11.974 3.859 -1.553 1.00 41.54 ? 279 GLU A O 1 ATOM 2200 C CB . GLU A 1 279 ? -9.210 5.025 -0.041 1.00 41.89 ? 279 GLU A CB 1 ATOM 2201 C CG . GLU A 1 279 ? -8.382 6.073 -0.805 1.00 44.22 ? 279 GLU A CG 1 ATOM 2202 C CD . GLU A 1 279 ? -9.036 7.453 -0.879 1.00 47.40 ? 279 GLU A CD 1 ATOM 2203 O OE1 . GLU A 1 279 ? -9.476 7.852 -1.983 1.00 48.40 ? 279 GLU A OE1 1 ATOM 2204 O OE2 . GLU A 1 279 ? -9.103 8.148 0.161 1.00 48.41 ? 279 GLU A OE2 1 ATOM 2205 N N . LEU A 1 280 ? -11.593 2.997 0.479 1.00 42.51 ? 280 LEU A N 1 ATOM 2206 C CA . LEU A 1 280 ? -12.223 1.683 0.188 1.00 42.53 ? 280 LEU A CA 1 ATOM 2207 C C . LEU A 1 280 ? -13.719 1.789 -0.126 1.00 43.05 ? 280 LEU A C 1 ATOM 2208 O O . LEU A 1 280 ? -14.219 1.132 -1.025 1.00 43.42 ? 280 LEU A O 1 ATOM 2209 C CB . LEU A 1 280 ? -12.004 0.689 1.331 1.00 42.44 ? 280 LEU A CB 1 ATOM 2210 C CG . LEU A 1 280 ? -10.664 -0.026 1.553 1.00 42.15 ? 280 LEU A CG 1 ATOM 2211 C CD1 . LEU A 1 280 ? -10.719 -0.742 2.889 1.00 39.53 ? 280 LEU A CD1 1 ATOM 2212 C CD2 . LEU A 1 280 ? -10.305 -0.995 0.437 1.00 40.96 ? 280 LEU A CD2 1 ATOM 2213 N N . LYS A 1 281 ? -14.438 2.608 0.632 1.00 44.04 ? 281 LYS A N 1 ATOM 2214 C CA . LYS A 1 281 ? -15.844 2.883 0.329 1.00 44.91 ? 281 LYS A CA 1 ATOM 2215 C C . LYS A 1 281 ? -15.952 3.349 -1.132 1.00 45.14 ? 281 LYS A C 1 ATOM 2216 O O . LYS A 1 281 ? -16.783 2.825 -1.877 1.00 44.91 ? 281 LYS A O 1 ATOM 2217 C CB . LYS A 1 281 ? -16.417 3.936 1.286 1.00 44.87 ? 281 LYS A CB 1 ATOM 2218 C CG . LYS A 1 281 ? -17.896 4.285 1.066 1.00 45.17 ? 281 LYS A CG 1 ATOM 2219 C CD . LYS A 1 281 ? -18.791 3.083 1.279 1.00 48.65 ? 281 LYS A CD 1 ATOM 2220 C CE . LYS A 1 281 ? -20.279 3.419 1.405 1.00 51.58 ? 281 LYS A CE 1 ATOM 2221 N NZ . LYS A 1 281 ? -21.058 2.248 1.960 1.00 54.55 ? 281 LYS A NZ 1 ATOM 2222 N N . LYS A 1 282 ? -15.098 4.307 -1.529 1.00 45.22 ? 282 LYS A N 1 ATOM 2223 C CA . LYS A 1 282 ? -15.021 4.768 -2.922 1.00 45.34 ? 282 LYS A CA 1 ATOM 2224 C C . LYS A 1 282 ? -14.958 3.636 -3.935 1.00 45.26 ? 282 LYS A C 1 ATOM 2225 O O . LYS A 1 282 ? -15.596 3.712 -4.986 1.00 45.79 ? 282 LYS A O 1 ATOM 2226 C CB . LYS A 1 282 ? -13.819 5.697 -3.166 1.00 44.90 ? 282 LYS A CB 1 ATOM 2227 C CG . LYS A 1 282 ? -14.169 7.175 -3.091 1.00 45.38 ? 282 LYS A CG 1 ATOM 2228 C CD . LYS A 1 282 ? -12.993 8.064 -3.391 1.00 45.63 ? 282 LYS A CD 1 ATOM 2229 C CE . LYS A 1 282 ? -13.230 9.464 -2.869 1.00 45.93 ? 282 LYS A CE 1 ATOM 2230 N NZ . LYS A 1 282 ? -13.656 9.489 -1.432 1.00 47.51 ? 282 LYS A NZ 1 ATOM 2231 N N . LEU A 1 283 ? -14.197 2.594 -3.627 1.00 44.91 ? 283 LEU A N 1 ATOM 2232 C CA . LEU A 1 283 ? -14.013 1.499 -4.581 1.00 45.17 ? 283 LEU A CA 1 ATOM 2233 C C . LEU A 1 283 ? -15.095 0.424 -4.496 1.00 44.81 ? 283 LEU A C 1 ATOM 2234 O O . LEU A 1 283 ? -15.438 -0.194 -5.493 1.00 45.08 ? 283 LEU A O 1 ATOM 2235 C CB . LEU A 1 283 ? -12.647 0.829 -4.425 1.00 45.39 ? 283 LEU A CB 1 ATOM 2236 C CG . LEU A 1 283 ? -11.347 1.619 -4.296 1.00 46.72 ? 283 LEU A CG 1 ATOM 2237 C CD1 . LEU A 1 283 ? -10.166 0.743 -4.742 1.00 47.63 ? 283 LEU A CD1 1 ATOM 2238 C CD2 . LEU A 1 283 ? -11.379 2.925 -5.087 1.00 49.14 ? 283 LEU A CD2 1 ATOM 2239 N N . ASN A 1 284 ? -15.616 0.187 -3.304 1.00 44.24 ? 284 ASN A N 1 ATOM 2240 C CA . ASN A 1 284 ? -16.625 -0.826 -3.128 1.00 43.70 ? 284 ASN A CA 1 ATOM 2241 C C . ASN A 1 284 ? -17.835 -0.237 -2.385 1.00 43.64 ? 284 ASN A C 1 ATOM 2242 O O . ASN A 1 284 ? -18.011 -0.454 -1.188 1.00 43.67 ? 284 ASN A O 1 ATOM 2243 C CB . ASN A 1 284 ? -16.013 -1.992 -2.372 1.00 43.57 ? 284 ASN A CB 1 ATOM 2244 C CG . ASN A 1 284 ? -14.677 -2.441 -2.956 1.00 44.60 ? 284 ASN A CG 1 ATOM 2245 O OD1 . ASN A 1 284 ? -14.512 -2.568 -4.184 1.00 44.91 ? 284 ASN A OD1 1 ATOM 2246 N ND2 . ASN A 1 284 ? -13.714 -2.711 -2.068 1.00 43.85 ? 284 ASN A ND2 1 ATOM 2247 N N . PRO A 1 285 ? -18.688 0.495 -3.100 1.00 43.47 ? 285 PRO A N 1 ATOM 2248 C CA . PRO A 1 285 ? -19.754 1.252 -2.448 1.00 43.14 ? 285 PRO A CA 1 ATOM 2249 C C . PRO A 1 285 ? -20.691 0.349 -1.698 1.00 43.12 ? 285 PRO A C 1 ATOM 2250 O O . PRO A 1 285 ? -21.246 0.777 -0.692 1.00 42.87 ? 285 PRO A O 1 ATOM 2251 C CB . PRO A 1 285 ? -20.439 1.933 -3.615 1.00 43.00 ? 285 PRO A CB 1 ATOM 2252 C CG . PRO A 1 285 ? -19.358 1.998 -4.633 1.00 42.62 ? 285 PRO A CG 1 ATOM 2253 C CD . PRO A 1 285 ? -18.738 0.646 -4.564 1.00 42.94 ? 285 PRO A CD 1 ATOM 2254 N N . HIS A 1 286 ? -20.826 -0.884 -2.167 1.00 43.36 ? 286 HIS A N 1 ATOM 2255 C CA . HIS A 1 286 ? -21.690 -1.864 -1.520 1.00 44.14 ? 286 HIS A CA 1 ATOM 2256 C C . HIS A 1 286 ? -21.113 -2.354 -0.215 1.00 44.12 ? 286 HIS A C 1 ATOM 2257 O O . HIS A 1 286 ? -21.857 -2.765 0.679 1.00 44.39 ? 286 HIS A O 1 ATOM 2258 C CB . HIS A 1 286 ? -21.940 -3.075 -2.424 1.00 44.60 ? 286 HIS A CB 1 ATOM 2259 C CG . HIS A 1 286 ? -20.691 -3.716 -2.941 1.00 45.88 ? 286 HIS A CG 1 ATOM 2260 N ND1 . HIS A 1 286 ? -19.807 -3.061 -3.776 1.00 46.42 ? 286 HIS A ND1 1 ATOM 2261 C CD2 . HIS A 1 286 ? -20.195 -4.963 -2.767 1.00 47.25 ? 286 HIS A CD2 1 ATOM 2262 C CE1 . HIS A 1 286 ? -18.816 -3.877 -4.087 1.00 47.47 ? 286 HIS A CE1 1 ATOM 2263 N NE2 . HIS A 1 286 ? -19.027 -5.037 -3.487 1.00 48.86 ? 286 HIS A NE2 1 ATOM 2264 N N . TRP A 1 287 ? -19.787 -2.316 -0.110 1.00 43.85 ? 287 TRP A N 1 ATOM 2265 C CA . TRP A 1 287 ? -19.118 -2.774 1.103 1.00 43.08 ? 287 TRP A CA 1 ATOM 2266 C C . TRP A 1 287 ? -19.716 -2.174 2.368 1.00 42.58 ? 287 TRP A C 1 ATOM 2267 O O . TRP A 1 287 ? -20.086 -0.988 2.440 1.00 42.58 ? 287 TRP A O 1 ATOM 2268 C CB . TRP A 1 287 ? -17.596 -2.565 1.057 1.00 43.13 ? 287 TRP A CB 1 ATOM 2269 C CG . TRP A 1 287 ? -16.861 -3.734 0.448 1.00 42.49 ? 287 TRP A CG 1 ATOM 2270 C CD1 . TRP A 1 287 ? -17.413 -4.755 -0.253 1.00 41.60 ? 287 TRP A CD1 1 ATOM 2271 C CD2 . TRP A 1 287 ? -15.448 -3.992 0.486 1.00 41.98 ? 287 TRP A CD2 1 ATOM 2272 N NE1 . TRP A 1 287 ? -16.440 -5.637 -0.655 1.00 42.01 ? 287 TRP A NE1 1 ATOM 2273 C CE2 . TRP A 1 287 ? -15.223 -5.191 -0.222 1.00 40.84 ? 287 TRP A CE2 1 ATOM 2274 C CE3 . TRP A 1 287 ? -14.347 -3.332 1.046 1.00 42.35 ? 287 TRP A CE3 1 ATOM 2275 C CZ2 . TRP A 1 287 ? -13.962 -5.748 -0.384 1.00 39.82 ? 287 TRP A CZ2 1 ATOM 2276 C CZ3 . TRP A 1 287 ? -13.086 -3.897 0.883 1.00 43.91 ? 287 TRP A CZ3 1 ATOM 2277 C CH2 . TRP A 1 287 ? -12.911 -5.099 0.173 1.00 41.12 ? 287 TRP A CH2 1 ATOM 2278 N N . ASN A 1 288 ? -19.772 -3.041 3.360 1.00 41.67 ? 288 ASN A N 1 ATOM 2279 C CA . ASN A 1 288 ? -20.345 -2.845 4.668 1.00 41.32 ? 288 ASN A CA 1 ATOM 2280 C C . ASN A 1 288 ? -19.440 -2.107 5.697 1.00 40.37 ? 288 ASN A C 1 ATOM 2281 O O . ASN A 1 288 ? -18.219 -2.052 5.557 1.00 40.21 ? 288 ASN A O 1 ATOM 2282 C CB . ASN A 1 288 ? -20.558 -4.274 5.123 1.00 41.94 ? 288 ASN A CB 1 ATOM 2283 C CG . ASN A 1 288 ? -21.352 -4.382 6.343 1.00 45.18 ? 288 ASN A CG 1 ATOM 2284 O OD1 . ASN A 1 288 ? -21.966 -3.413 6.786 1.00 49.13 ? 288 ASN A OD1 1 ATOM 2285 N ND2 . ASN A 1 288 ? -21.382 -5.588 6.911 1.00 48.95 ? 288 ASN A ND2 1 ATOM 2286 N N . GLY A 1 289 ? -20.041 -1.554 6.746 1.00 39.36 ? 289 GLY A N 1 ATOM 2287 C CA . GLY A 1 289 ? -19.288 -0.938 7.835 1.00 37.57 ? 289 GLY A CA 1 ATOM 2288 C C . GLY A 1 289 ? -18.229 -1.837 8.472 1.00 36.48 ? 289 GLY A C 1 ATOM 2289 O O . GLY A 1 289 ? -17.098 -1.419 8.682 1.00 36.19 ? 289 GLY A O 1 ATOM 2290 N N . GLU A 1 290 ? -18.608 -3.069 8.791 1.00 35.30 ? 290 GLU A N 1 ATOM 2291 C CA . GLU A 1 290 ? -17.703 -4.040 9.356 1.00 34.35 ? 290 GLU A CA 1 ATOM 2292 C C . GLU A 1 290 ? -16.625 -4.320 8.321 1.00 34.17 ? 290 GLU A C 1 ATOM 2293 O O . GLU A 1 290 ? -15.438 -4.187 8.607 1.00 34.57 ? 290 GLU A O 1 ATOM 2294 C CB . GLU A 1 290 ? -18.480 -5.310 9.689 1.00 34.78 ? 290 GLU A CB 1 ATOM 2295 C CG . GLU A 1 290 ? -17.696 -6.446 10.325 1.00 35.91 ? 290 GLU A CG 1 ATOM 2296 C CD . GLU A 1 290 ? -17.191 -6.060 11.689 1.00 37.35 ? 290 GLU A CD 1 ATOM 2297 O OE1 . GLU A 1 290 ? -17.731 -5.055 12.202 1.00 37.97 ? 290 GLU A OE1 1 ATOM 2298 O OE2 . GLU A 1 290 ? -16.269 -6.736 12.231 1.00 37.87 ? 290 GLU A OE2 1 ATOM 2299 N N . LYS A 1 291 ? -17.016 -4.661 7.092 1.00 33.49 ? 291 LYS A N 1 ATOM 2300 C CA . LYS A 1 291 ? -16.003 -5.000 6.090 1.00 31.92 ? 291 LYS A CA 1 ATOM 2301 C C . LYS A 1 291 ? -15.035 -3.883 5.840 1.00 30.80 ? 291 LYS A C 1 ATOM 2302 O O . LYS A 1 291 ? -13.863 -4.138 5.546 1.00 31.32 ? 291 LYS A O 1 ATOM 2303 C CB . LYS A 1 291 ? -16.606 -5.418 4.756 1.00 32.27 ? 291 LYS A CB 1 ATOM 2304 C CG . LYS A 1 291 ? -15.754 -6.438 4.012 1.00 32.04 ? 291 LYS A CG 1 ATOM 2305 C CD . LYS A 1 291 ? -16.265 -6.654 2.636 1.00 33.78 ? 291 LYS A CD 1 ATOM 2306 C CE . LYS A 1 291 ? -15.847 -8.011 2.164 1.00 36.78 ? 291 LYS A CE 1 ATOM 2307 N NZ . LYS A 1 291 ? -14.369 -8.096 2.075 1.00 41.11 ? 291 LYS A NZ 1 ATOM 2308 N N . LEU A 1 292 ? -15.516 -2.651 5.913 1.00 29.18 ? 292 LEU A N 1 ATOM 2309 C CA . LEU A 1 292 ? -14.635 -1.501 5.752 1.00 27.82 ? 292 LEU A CA 1 ATOM 2310 C C . LEU A 1 292 ? -13.574 -1.540 6.854 1.00 26.87 ? 292 LEU A C 1 ATOM 2311 O O . LEU A 1 292 ? -12.385 -1.438 6.604 1.00 26.04 ? 292 LEU A O 1 ATOM 2312 C CB . LEU A 1 292 ? -15.445 -0.196 5.830 1.00 28.44 ? 292 LEU A CB 1 ATOM 2313 C CG . LEU A 1 292 ? -15.900 0.425 4.502 1.00 29.14 ? 292 LEU A CG 1 ATOM 2314 C CD1 . LEU A 1 292 ? -14.749 0.396 3.480 1.00 30.73 ? 292 LEU A CD1 1 ATOM 2315 C CD2 . LEU A 1 292 ? -17.096 -0.292 3.940 1.00 26.59 ? 292 LEU A CD2 1 ATOM 2316 N N . TYR A 1 293 ? -14.033 -1.712 8.084 1.00 25.96 ? 293 TYR A N 1 ATOM 2317 C CA . TYR A 1 293 ? -13.165 -1.795 9.224 1.00 25.31 ? 293 TYR A CA 1 ATOM 2318 C C . TYR A 1 293 ? -12.198 -2.953 9.084 1.00 25.19 ? 293 TYR A C 1 ATOM 2319 O O . TYR A 1 293 ? -11.002 -2.757 8.983 1.00 25.46 ? 293 TYR A O 1 ATOM 2320 C CB . TYR A 1 293 ? -14.010 -2.004 10.452 1.00 24.92 ? 293 TYR A CB 1 ATOM 2321 C CG . TYR A 1 293 ? -13.232 -2.218 11.723 1.00 26.14 ? 293 TYR A CG 1 ATOM 2322 C CD1 . TYR A 1 293 ? -12.668 -1.134 12.410 1.00 26.02 ? 293 TYR A CD1 1 ATOM 2323 C CD2 . TYR A 1 293 ? -13.091 -3.499 12.273 1.00 25.85 ? 293 TYR A CD2 1 ATOM 2324 C CE1 . TYR A 1 293 ? -11.987 -1.321 13.610 1.00 25.41 ? 293 TYR A CE1 1 ATOM 2325 C CE2 . TYR A 1 293 ? -12.408 -3.693 13.471 1.00 26.00 ? 293 TYR A CE2 1 ATOM 2326 C CZ . TYR A 1 293 ? -11.860 -2.593 14.132 1.00 25.11 ? 293 TYR A CZ 1 ATOM 2327 O OH . TYR A 1 293 ? -11.181 -2.769 15.307 1.00 25.37 ? 293 TYR A OH 1 ATOM 2328 N N . GLN A 1 294 ? -12.702 -4.171 9.063 1.00 24.72 ? 294 GLN A N 1 ATOM 2329 C CA . GLN A 1 294 ? -11.782 -5.283 8.984 1.00 25.26 ? 294 GLN A CA 1 ATOM 2330 C C . GLN A 1 294 ? -10.768 -5.136 7.854 1.00 25.11 ? 294 GLN A C 1 ATOM 2331 O O . GLN A 1 294 ? -9.624 -5.520 8.020 1.00 25.44 ? 294 GLN A O 1 ATOM 2332 C CB . GLN A 1 294 ? -12.521 -6.627 8.900 1.00 25.58 ? 294 GLN A CB 1 ATOM 2333 C CG . GLN A 1 294 ? -13.422 -6.934 10.136 1.00 26.41 ? 294 GLN A CG 1 ATOM 2334 C CD . GLN A 1 294 ? -12.619 -7.102 11.429 1.00 26.12 ? 294 GLN A CD 1 ATOM 2335 O OE1 . GLN A 1 294 ? -11.418 -7.396 11.379 1.00 24.93 ? 294 GLN A OE1 1 ATOM 2336 N NE2 . GLN A 1 294 ? -13.269 -6.878 12.576 1.00 23.92 ? 294 GLN A NE2 1 ATOM 2337 N N . GLU A 1 295 ? -11.182 -4.582 6.692 1.00 24.69 ? 295 GLU A N 1 ATOM 2338 C CA . GLU A 1 295 ? -10.210 -4.531 5.575 1.00 24.50 ? 295 GLU A CA 1 ATOM 2339 C C . GLU A 1 295 ? -9.166 -3.449 5.693 1.00 23.53 ? 295 GLU A C 1 ATOM 2340 O O . GLU A 1 295 ? -8.031 -3.670 5.286 1.00 23.79 ? 295 GLU A O 1 ATOM 2341 C CB . GLU A 1 295 ? -10.934 -4.463 4.235 1.00 25.41 ? 295 GLU A CB 1 ATOM 2342 C CG . GLU A 1 295 ? -11.619 -5.768 3.831 1.00 25.81 ? 295 GLU A CG 1 ATOM 2343 C CD . GLU A 1 295 ? -10.754 -6.739 3.026 1.00 23.52 ? 295 GLU A CD 1 ATOM 2344 O OE1 . GLU A 1 295 ? -9.764 -6.291 2.388 1.00 24.15 ? 295 GLU A OE1 1 ATOM 2345 O OE2 . GLU A 1 295 ? -11.072 -7.963 3.045 1.00 25.50 ? 295 GLU A OE2 1 ATOM 2346 N N . ALA A 1 296 ? -9.516 -2.284 6.218 1.00 22.25 ? 296 ALA A N 1 ATOM 2347 C CA . ALA A 1 296 ? -8.479 -1.267 6.455 1.00 21.45 ? 296 ALA A CA 1 ATOM 2348 C C . ALA A 1 296 ? -7.487 -1.828 7.485 1.00 21.34 ? 296 ALA A C 1 ATOM 2349 O O . ALA A 1 296 ? -6.265 -1.904 7.238 1.00 21.25 ? 296 ALA A O 1 ATOM 2350 C CB . ALA A 1 296 ? -9.080 0.015 6.915 1.00 21.41 ? 296 ALA A CB 1 ATOM 2351 N N . ARG A 1 297 ? -8.053 -2.280 8.605 1.00 20.67 ? 297 ARG A N 1 ATOM 2352 C CA . ARG A 1 297 ? -7.347 -2.964 9.676 1.00 20.35 ? 297 ARG A CA 1 ATOM 2353 C C . ARG A 1 297 ? -6.314 -3.984 9.189 1.00 20.68 ? 297 ARG A C 1 ATOM 2354 O O . ARG A 1 297 ? -5.122 -3.931 9.547 1.00 20.06 ? 297 ARG A O 1 ATOM 2355 C CB . ARG A 1 297 ? -8.378 -3.653 10.542 1.00 19.86 ? 297 ARG A CB 1 ATOM 2356 C CG . ARG A 1 297 ? -7.808 -4.593 11.560 1.00 20.08 ? 297 ARG A CG 1 ATOM 2357 C CD . ARG A 1 297 ? -8.609 -4.678 12.847 1.00 19.40 ? 297 ARG A CD 1 ATOM 2358 N NE . ARG A 1 297 ? -7.937 -5.594 13.741 1.00 21.19 ? 297 ARG A NE 1 ATOM 2359 C CZ . ARG A 1 297 ? -8.215 -6.885 13.829 1.00 22.95 ? 297 ARG A CZ 1 ATOM 2360 N NH1 . ARG A 1 297 ? -9.199 -7.418 13.105 1.00 21.24 ? 297 ARG A NH1 1 ATOM 2361 N NH2 . ARG A 1 297 ? -7.510 -7.645 14.663 1.00 24.00 ? 297 ARG A NH2 1 ATOM 2362 N N . LYS A 1 298 ? -6.788 -4.911 8.372 1.00 21.84 ? 298 LYS A N 1 ATOM 2363 C CA . LYS A 1 298 ? -5.940 -5.923 7.792 1.00 23.02 ? 298 LYS A CA 1 ATOM 2364 C C . LYS A 1 298 ? -4.780 -5.262 7.011 1.00 24.00 ? 298 LYS A C 1 ATOM 2365 O O . LYS A 1 298 ? -3.622 -5.693 7.093 1.00 23.72 ? 298 LYS A O 1 ATOM 2366 C CB . LYS A 1 298 ? -6.793 -6.838 6.925 1.00 22.78 ? 298 LYS A CB 1 ATOM 2367 C CG . LYS A 1 298 ? -6.036 -7.845 6.061 1.00 23.73 ? 298 LYS A CG 1 ATOM 2368 C CD . LYS A 1 298 ? -6.824 -9.156 5.967 1.00 26.32 ? 298 LYS A CD 1 ATOM 2369 C CE . LYS A 1 298 ? -6.523 -9.910 4.691 1.00 27.07 ? 298 LYS A CE 1 ATOM 2370 N NZ . LYS A 1 298 ? -7.277 -11.201 4.677 1.00 29.68 ? 298 LYS A NZ 1 ATOM 2371 N N . ILE A 1 299 ? -5.071 -4.184 6.289 1.00 24.87 ? 299 ILE A N 1 ATOM 2372 C CA . ILE A 1 299 ? -4.000 -3.548 5.549 1.00 26.01 ? 299 ILE A CA 1 ATOM 2373 C C . ILE A 1 299 ? -2.991 -2.859 6.484 1.00 26.18 ? 299 ILE A C 1 ATOM 2374 O O . ILE A 1 299 ? -1.776 -2.991 6.290 1.00 26.47 ? 299 ILE A O 1 ATOM 2375 C CB . ILE A 1 299 ? -4.548 -2.530 4.546 1.00 26.93 ? 299 ILE A CB 1 ATOM 2376 C CG1 . ILE A 1 299 ? -5.015 -3.221 3.260 1.00 25.91 ? 299 ILE A CG1 1 ATOM 2377 C CG2 . ILE A 1 299 ? -3.467 -1.465 4.249 1.00 27.88 ? 299 ILE A CG2 1 ATOM 2378 C CD1 . ILE A 1 299 ? -6.092 -2.448 2.509 1.00 24.63 ? 299 ILE A CD1 1 ATOM 2379 N N . LEU A 1 300 ? -3.488 -2.123 7.481 1.00 25.36 ? 300 LEU A N 1 ATOM 2380 C CA . LEU A 1 300 ? -2.603 -1.421 8.414 1.00 24.73 ? 300 LEU A CA 1 ATOM 2381 C C . LEU A 1 300 ? -1.629 -2.383 9.102 1.00 24.67 ? 300 LEU A C 1 ATOM 2382 O O . LEU A 1 300 ? -0.432 -2.080 9.267 1.00 24.12 ? 300 LEU A O 1 ATOM 2383 C CB . LEU A 1 300 ? -3.414 -0.606 9.428 1.00 24.17 ? 300 LEU A CB 1 ATOM 2384 C CG . LEU A 1 300 ? -2.651 0.539 10.109 1.00 24.02 ? 300 LEU A CG 1 ATOM 2385 C CD1 . LEU A 1 300 ? -2.238 1.661 9.160 1.00 22.64 ? 300 LEU A CD1 1 ATOM 2386 C CD2 . LEU A 1 300 ? -3.502 1.110 11.192 1.00 24.88 ? 300 LEU A CD2 1 ATOM 2387 N N . GLY A 1 301 ? -2.157 -3.548 9.488 1.00 25.02 ? 301 GLY A N 1 ATOM 2388 C CA . GLY A 1 301 ? -1.354 -4.634 10.051 1.00 25.09 ? 301 GLY A CA 1 ATOM 2389 C C . GLY A 1 301 ? -0.253 -5.079 9.103 1.00 25.24 ? 301 GLY A C 1 ATOM 2390 O O . GLY A 1 301 ? 0.898 -5.174 9.507 1.00 25.55 ? 301 GLY A O 1 ATOM 2391 N N . ALA A 1 302 ? -0.591 -5.331 7.836 1.00 25.33 ? 302 ALA A N 1 ATOM 2392 C CA . ALA A 1 302 ? 0.413 -5.684 6.824 1.00 24.69 ? 302 ALA A CA 1 ATOM 2393 C C . ALA A 1 302 ? 1.458 -4.580 6.731 1.00 24.26 ? 302 ALA A C 1 ATOM 2394 O O . ALA A 1 302 ? 2.648 -4.824 6.559 1.00 24.34 ? 302 ALA A O 1 ATOM 2395 C CB . ALA A 1 302 ? -0.253 -5.872 5.474 1.00 24.63 ? 302 ALA A CB 1 ATOM 2396 N N . PHE A 1 303 ? 1.012 -3.348 6.849 1.00 23.65 ? 303 PHE A N 1 ATOM 2397 C CA . PHE A 1 303 ? 1.923 -2.236 6.686 1.00 23.57 ? 303 PHE A CA 1 ATOM 2398 C C . PHE A 1 303 ? 2.976 -2.234 7.826 1.00 23.17 ? 303 PHE A C 1 ATOM 2399 O O . PHE A 1 303 ? 4.185 -2.183 7.597 1.00 22.54 ? 303 PHE A O 1 ATOM 2400 C CB . PHE A 1 303 ? 1.099 -0.950 6.603 1.00 23.70 ? 303 PHE A CB 1 ATOM 2401 C CG . PHE A 1 303 ? 1.890 0.294 6.792 1.00 25.71 ? 303 PHE A CG 1 ATOM 2402 C CD1 . PHE A 1 303 ? 2.423 0.956 5.701 1.00 28.89 ? 303 PHE A CD1 1 ATOM 2403 C CD2 . PHE A 1 303 ? 2.086 0.821 8.059 1.00 25.10 ? 303 PHE A CD2 1 ATOM 2404 C CE1 . PHE A 1 303 ? 3.163 2.107 5.881 1.00 30.44 ? 303 PHE A CE1 1 ATOM 2405 C CE2 . PHE A 1 303 ? 2.818 1.941 8.240 1.00 25.74 ? 303 PHE A CE2 1 ATOM 2406 C CZ . PHE A 1 303 ? 3.370 2.582 7.168 1.00 29.46 ? 303 PHE A CZ 1 ATOM 2407 N N . ILE A 1 304 ? 2.521 -2.333 9.063 1.00 22.73 ? 304 ILE A N 1 ATOM 2408 C CA . ILE A 1 304 ? 3.467 -2.347 10.178 1.00 22.17 ? 304 ILE A CA 1 ATOM 2409 C C . ILE A 1 304 ? 4.452 -3.516 10.112 1.00 21.62 ? 304 ILE A C 1 ATOM 2410 O O . ILE A 1 304 ? 5.617 -3.395 10.484 1.00 21.63 ? 304 ILE A O 1 ATOM 2411 C CB . ILE A 1 304 ? 2.715 -2.318 11.486 1.00 21.93 ? 304 ILE A CB 1 ATOM 2412 C CG1 . ILE A 1 304 ? 2.136 -0.916 11.667 1.00 22.56 ? 304 ILE A CG1 1 ATOM 2413 C CG2 . ILE A 1 304 ? 3.650 -2.603 12.617 1.00 22.87 ? 304 ILE A CG2 1 ATOM 2414 C CD1 . ILE A 1 304 ? 1.285 -0.742 12.911 1.00 22.30 ? 304 ILE A CD1 1 ATOM 2415 N N . GLN A 1 305 ? 3.986 -4.645 9.599 1.00 21.09 ? 305 GLN A N 1 ATOM 2416 C CA . GLN A 1 305 ? 4.823 -5.827 9.475 1.00 20.40 ? 305 GLN A CA 1 ATOM 2417 C C . GLN A 1 305 ? 5.923 -5.578 8.454 1.00 20.03 ? 305 GLN A C 1 ATOM 2418 O O . GLN A 1 305 ? 7.081 -5.955 8.640 1.00 19.53 ? 305 GLN A O 1 ATOM 2419 C CB . GLN A 1 305 ? 3.957 -7.034 9.082 1.00 20.29 ? 305 GLN A CB 1 ATOM 2420 C CG . GLN A 1 305 ? 2.902 -7.430 10.123 1.00 20.50 ? 305 GLN A CG 1 ATOM 2421 C CD . GLN A 1 305 ? 2.294 -8.801 9.828 1.00 22.47 ? 305 GLN A CD 1 ATOM 2422 O OE1 . GLN A 1 305 ? 2.265 -9.222 8.686 1.00 23.62 ? 305 GLN A OE1 1 ATOM 2423 N NE2 . GLN A 1 305 ? 1.834 -9.495 10.850 1.00 21.77 ? 305 GLN A NE2 1 ATOM 2424 N N . ILE A 1 306 ? 5.550 -4.901 7.379 1.00 20.60 ? 306 ILE A N 1 ATOM 2425 C CA . ILE A 1 306 ? 6.484 -4.638 6.266 1.00 20.92 ? 306 ILE A CA 1 ATOM 2426 C C . ILE A 1 306 ? 7.573 -3.663 6.652 1.00 20.52 ? 306 ILE A C 1 ATOM 2427 O O . ILE A 1 306 ? 8.747 -3.964 6.500 1.00 20.42 ? 306 ILE A O 1 ATOM 2428 C CB . ILE A 1 306 ? 5.716 -4.184 4.954 1.00 21.09 ? 306 ILE A CB 1 ATOM 2429 C CG1 . ILE A 1 306 ? 4.934 -5.362 4.349 1.00 21.52 ? 306 ILE A CG1 1 ATOM 2430 C CG2 . ILE A 1 306 ? 6.675 -3.640 3.924 1.00 20.79 ? 306 ILE A CG2 1 ATOM 2431 C CD1 . ILE A 1 306 ? 3.892 -4.953 3.299 1.00 23.24 ? 306 ILE A CD1 1 ATOM 2432 N N . ILE A 1 307 ? 7.179 -2.508 7.185 1.00 20.49 ? 307 ILE A N 1 ATOM 2433 C CA . ILE A 1 307 ? 8.139 -1.482 7.571 1.00 20.19 ? 307 ILE A CA 1 ATOM 2434 C C . ILE A 1 307 ? 9.062 -2.050 8.615 1.00 20.40 ? 307 ILE A C 1 ATOM 2435 O O . ILE A 1 307 ? 10.276 -1.778 8.643 1.00 20.85 ? 307 ILE A O 1 ATOM 2436 C CB . ILE A 1 307 ? 7.413 -0.226 8.080 1.00 20.09 ? 307 ILE A CB 1 ATOM 2437 C CG1 . ILE A 1 307 ? 6.420 0.280 6.994 1.00 21.42 ? 307 ILE A CG1 1 ATOM 2438 C CG2 . ILE A 1 307 ? 8.415 0.850 8.520 1.00 18.32 ? 307 ILE A CG2 1 ATOM 2439 C CD1 . ILE A 1 307 ? 6.920 1.377 6.114 1.00 21.07 ? 307 ILE A CD1 1 ATOM 2440 N N . THR A 1 308 ? 8.483 -2.862 9.474 1.00 19.91 ? 308 THR A N 1 ATOM 2441 C CA . THR A 1 308 ? 9.259 -3.445 10.527 1.00 19.83 ? 308 THR A CA 1 ATOM 2442 C C . THR A 1 308 ? 10.219 -4.444 9.966 1.00 19.85 ? 308 THR A C 1 ATOM 2443 O O . THR A 1 308 ? 11.395 -4.380 10.266 1.00 20.15 ? 308 THR A O 1 ATOM 2444 C CB . THR A 1 308 ? 8.336 -4.083 11.541 1.00 19.93 ? 308 THR A CB 1 ATOM 2445 O OG1 . THR A 1 308 ? 7.595 -3.029 12.181 1.00 19.06 ? 308 THR A OG1 1 ATOM 2446 C CG2 . THR A 1 308 ? 9.142 -4.741 12.678 1.00 18.48 ? 308 THR A CG2 1 ATOM 2447 N N . PHE A 1 309 ? 9.732 -5.352 9.136 1.00 19.82 ? 309 PHE A N 1 ATOM 2448 C CA . PHE A 1 309 ? 10.596 -6.419 8.671 1.00 20.17 ? 309 PHE A CA 1 ATOM 2449 C C . PHE A 1 309 ? 11.518 -6.043 7.508 1.00 20.61 ? 309 PHE A C 1 ATOM 2450 O O . PHE A 1 309 ? 12.655 -6.498 7.434 1.00 20.61 ? 309 PHE A O 1 ATOM 2451 C CB . PHE A 1 309 ? 9.800 -7.666 8.392 1.00 19.87 ? 309 PHE A CB 1 ATOM 2452 C CG . PHE A 1 309 ? 9.663 -8.561 9.581 1.00 19.57 ? 309 PHE A CG 1 ATOM 2453 C CD1 . PHE A 1 309 ? 8.803 -8.226 10.610 1.00 18.92 ? 309 PHE A CD1 1 ATOM 2454 C CD2 . PHE A 1 309 ? 10.423 -9.732 9.689 1.00 17.72 ? 309 PHE A CD2 1 ATOM 2455 C CE1 . PHE A 1 309 ? 8.685 -9.062 11.750 1.00 19.58 ? 309 PHE A CE1 1 ATOM 2456 C CE2 . PHE A 1 309 ? 10.314 -10.591 10.818 1.00 18.03 ? 309 PHE A CE2 1 ATOM 2457 C CZ . PHE A 1 309 ? 9.446 -10.260 11.854 1.00 17.33 ? 309 PHE A CZ 1 ATOM 2458 N N . ARG A 1 310 ? 11.053 -5.149 6.649 1.00 20.87 ? 310 ARG A N 1 ATOM 2459 C CA . ARG A 1 310 ? 11.836 -4.738 5.503 1.00 20.56 ? 310 ARG A CA 1 ATOM 2460 C C . ARG A 1 310 ? 12.782 -3.601 5.813 1.00 20.92 ? 310 ARG A C 1 ATOM 2461 O O . ARG A 1 310 ? 13.938 -3.689 5.446 1.00 21.72 ? 310 ARG A O 1 ATOM 2462 C CB . ARG A 1 310 ? 10.923 -4.387 4.333 1.00 20.42 ? 310 ARG A CB 1 ATOM 2463 C CG . ARG A 1 310 ? 11.647 -4.050 3.059 1.00 20.02 ? 310 ARG A CG 1 ATOM 2464 C CD . ARG A 1 310 ? 10.827 -3.212 2.113 1.00 20.94 ? 310 ARG A CD 1 ATOM 2465 N NE . ARG A 1 310 ? 10.491 -1.916 2.674 1.00 22.27 ? 310 ARG A NE 1 ATOM 2466 C CZ . ARG A 1 310 ? 9.417 -1.238 2.338 1.00 23.88 ? 310 ARG A CZ 1 ATOM 2467 N NH1 . ARG A 1 310 ? 8.583 -1.762 1.442 1.00 23.92 ? 310 ARG A NH1 1 ATOM 2468 N NH2 . ARG A 1 310 ? 9.183 -0.048 2.891 1.00 23.10 ? 310 ARG A NH2 1 ATOM 2469 N N . ASP A 1 311 ? 12.313 -2.552 6.498 1.00 21.32 ? 311 ASP A N 1 ATOM 2470 C CA . ASP A 1 311 ? 13.153 -1.389 6.840 1.00 21.71 ? 311 ASP A CA 1 ATOM 2471 C C . ASP A 1 311 ? 13.813 -1.285 8.237 1.00 22.34 ? 311 ASP A C 1 ATOM 2472 O O . ASP A 1 311 ? 14.869 -0.652 8.369 1.00 23.77 ? 311 ASP A O 1 ATOM 2473 C CB . ASP A 1 311 ? 12.355 -0.101 6.661 1.00 21.46 ? 311 ASP A CB 1 ATOM 2474 C CG . ASP A 1 311 ? 11.652 -0.041 5.349 1.00 21.69 ? 311 ASP A CG 1 ATOM 2475 O OD1 . ASP A 1 311 ? 12.030 -0.811 4.452 1.00 23.77 ? 311 ASP A OD1 1 ATOM 2476 O OD2 . ASP A 1 311 ? 10.715 0.742 5.107 1.00 20.63 ? 311 ASP A OD2 1 ATOM 2477 N N . TYR A 1 312 ? 13.213 -1.858 9.271 1.00 21.68 ? 312 TYR A N 1 ATOM 2478 C CA . TYR A 1 312 ? 13.676 -1.561 10.607 1.00 21.54 ? 312 TYR A CA 1 ATOM 2479 C C . TYR A 1 312 ? 14.621 -2.619 11.171 1.00 22.28 ? 312 TYR A C 1 ATOM 2480 O O . TYR A 1 312 ? 15.724 -2.308 11.670 1.00 22.76 ? 312 TYR A O 1 ATOM 2481 C CB . TYR A 1 312 ? 12.449 -1.332 11.507 1.00 21.90 ? 312 TYR A CB 1 ATOM 2482 C CG . TYR A 1 312 ? 12.760 -1.148 12.957 1.00 19.57 ? 312 TYR A CG 1 ATOM 2483 C CD1 . TYR A 1 312 ? 13.325 0.032 13.426 1.00 17.62 ? 312 TYR A CD1 1 ATOM 2484 C CD2 . TYR A 1 312 ? 12.475 -2.146 13.861 1.00 17.76 ? 312 TYR A CD2 1 ATOM 2485 C CE1 . TYR A 1 312 ? 13.620 0.202 14.771 1.00 17.31 ? 312 TYR A CE1 1 ATOM 2486 C CE2 . TYR A 1 312 ? 12.774 -1.998 15.208 1.00 18.14 ? 312 TYR A CE2 1 ATOM 2487 C CZ . TYR A 1 312 ? 13.351 -0.822 15.662 1.00 18.56 ? 312 TYR A CZ 1 ATOM 2488 O OH . TYR A 1 312 ? 13.651 -0.677 17.009 1.00 20.11 ? 312 TYR A OH 1 ATOM 2489 N N . LEU A 1 313 ? 14.231 -3.879 11.079 1.00 21.58 ? 313 LEU A N 1 ATOM 2490 C CA . LEU A 1 313 ? 15.056 -4.897 11.701 1.00 21.55 ? 313 LEU A CA 1 ATOM 2491 C C . LEU A 1 313 ? 16.455 -5.040 11.102 1.00 21.75 ? 313 LEU A C 1 ATOM 2492 O O . LEU A 1 313 ? 17.396 -5.267 11.842 1.00 21.69 ? 313 LEU A O 1 ATOM 2493 C CB . LEU A 1 313 ? 14.347 -6.255 11.733 1.00 21.85 ? 313 LEU A CB 1 ATOM 2494 C CG . LEU A 1 313 ? 13.146 -6.394 12.654 1.00 20.76 ? 313 LEU A CG 1 ATOM 2495 C CD1 . LEU A 1 313 ? 12.511 -7.787 12.503 1.00 18.78 ? 313 LEU A CD1 1 ATOM 2496 C CD2 . LEU A 1 313 ? 13.567 -6.130 14.074 1.00 20.34 ? 313 LEU A CD2 1 ATOM 2497 N N . PRO A 1 314 ? 16.607 -4.966 9.775 1.00 22.11 ? 314 PRO A N 1 ATOM 2498 C CA . PRO A 1 314 ? 17.939 -5.066 9.177 1.00 21.81 ? 314 PRO A CA 1 ATOM 2499 C C . PRO A 1 314 ? 18.902 -4.008 9.731 1.00 22.16 ? 314 PRO A C 1 ATOM 2500 O O . PRO A 1 314 ? 20.115 -4.248 9.804 1.00 22.42 ? 314 PRO A O 1 ATOM 2501 C CB . PRO A 1 314 ? 17.672 -4.818 7.691 1.00 21.43 ? 314 PRO A CB 1 ATOM 2502 C CG . PRO A 1 314 ? 16.304 -5.252 7.452 1.00 21.00 ? 314 PRO A CG 1 ATOM 2503 C CD . PRO A 1 314 ? 15.570 -4.857 8.725 1.00 22.43 ? 314 PRO A CD 1 ATOM 2504 N N . ILE A 1 315 ? 18.394 -2.851 10.128 1.00 22.06 ? 315 ILE A N 1 ATOM 2505 C CA . ILE A 1 315 ? 19.310 -1.846 10.643 1.00 21.59 ? 315 ILE A CA 1 ATOM 2506 C C . ILE A 1 315 ? 19.359 -1.836 12.175 1.00 21.47 ? 315 ILE A C 1 ATOM 2507 O O . ILE A 1 315 ? 19.946 -0.970 12.761 1.00 21.85 ? 315 ILE A O 1 ATOM 2508 C CB . ILE A 1 315 ? 19.068 -0.452 10.013 1.00 21.33 ? 315 ILE A CB 1 ATOM 2509 C CG1 . ILE A 1 315 ? 17.867 0.247 10.620 1.00 21.54 ? 315 ILE A CG1 1 ATOM 2510 C CG2 . ILE A 1 315 ? 18.854 -0.568 8.531 1.00 21.03 ? 315 ILE A CG2 1 ATOM 2511 C CD1 . ILE A 1 315 ? 17.493 1.513 9.897 1.00 22.15 ? 315 ILE A CD1 1 ATOM 2512 N N . VAL A 1 316 ? 18.718 -2.802 12.815 1.00 21.24 ? 316 VAL A N 1 ATOM 2513 C CA . VAL A 1 316 ? 18.922 -3.037 14.244 1.00 20.41 ? 316 VAL A CA 1 ATOM 2514 C C . VAL A 1 316 ? 19.842 -4.265 14.287 1.00 20.78 ? 316 VAL A C 1 ATOM 2515 O O . VAL A 1 316 ? 20.907 -4.214 14.915 1.00 19.98 ? 316 VAL A O 1 ATOM 2516 C CB . VAL A 1 316 ? 17.615 -3.433 15.022 1.00 20.39 ? 316 VAL A CB 1 ATOM 2517 C CG1 . VAL A 1 316 ? 17.949 -3.905 16.409 1.00 19.12 ? 316 VAL A CG1 1 ATOM 2518 C CG2 . VAL A 1 316 ? 16.611 -2.307 15.070 1.00 20.62 ? 316 VAL A CG2 1 ATOM 2519 N N . LEU A 1 317 ? 19.430 -5.359 13.615 1.00 21.21 ? 317 LEU A N 1 ATOM 2520 C CA . LEU A 1 317 ? 20.157 -6.629 13.650 1.00 22.43 ? 317 LEU A CA 1 ATOM 2521 C C . LEU A 1 317 ? 21.463 -6.627 12.870 1.00 23.26 ? 317 LEU A C 1 ATOM 2522 O O . LEU A 1 317 ? 22.344 -7.417 13.152 1.00 24.36 ? 317 LEU A O 1 ATOM 2523 C CB . LEU A 1 317 ? 19.289 -7.778 13.151 1.00 22.95 ? 317 LEU A CB 1 ATOM 2524 C CG . LEU A 1 317 ? 18.252 -8.443 14.053 1.00 24.24 ? 317 LEU A CG 1 ATOM 2525 C CD1 . LEU A 1 317 ? 18.473 -8.025 15.462 1.00 27.17 ? 317 LEU A CD1 1 ATOM 2526 C CD2 . LEU A 1 317 ? 16.868 -8.047 13.633 1.00 25.28 ? 317 LEU A CD2 1 ATOM 2527 N N . GLY A 1 318 ? 21.584 -5.749 11.879 1.00 24.25 ? 318 GLY A N 1 ATOM 2528 C CA . GLY A 1 318 ? 22.794 -5.624 11.078 1.00 24.68 ? 318 GLY A CA 1 ATOM 2529 C C . GLY A 1 318 ? 23.136 -6.938 10.414 1.00 25.38 ? 318 GLY A C 1 ATOM 2530 O O . GLY A 1 318 ? 22.295 -7.661 9.925 1.00 24.78 ? 318 GLY A O 1 ATOM 2531 N N . SER A 1 319 ? 24.405 -7.243 10.402 1.00 26.66 ? 319 SER A N 1 ATOM 2532 C CA . SER A 1 319 ? 24.868 -8.457 9.787 1.00 28.61 ? 319 SER A CA 1 ATOM 2533 C C . SER A 1 319 ? 24.227 -9.730 10.396 1.00 29.45 ? 319 SER A C 1 ATOM 2534 O O . SER A 1 319 ? 24.179 -10.787 9.732 1.00 29.46 ? 319 SER A O 1 ATOM 2535 C CB . SER A 1 319 ? 26.389 -8.500 9.940 1.00 29.05 ? 319 SER A CB 1 ATOM 2536 O OG . SER A 1 319 ? 26.763 -8.281 11.307 1.00 30.93 ? 319 SER A OG 1 ATOM 2537 N N . GLU A 1 320 ? 23.733 -9.632 11.636 1.00 29.57 ? 320 GLU A N 1 ATOM 2538 C CA . GLU A 1 320 ? 23.159 -10.790 12.307 1.00 30.41 ? 320 GLU A CA 1 ATOM 2539 C C . GLU A 1 320 ? 21.763 -11.177 11.820 1.00 30.32 ? 320 GLU A C 1 ATOM 2540 O O . GLU A 1 320 ? 21.290 -12.270 12.070 1.00 29.92 ? 320 GLU A O 1 ATOM 2541 C CB . GLU A 1 320 ? 23.105 -10.559 13.828 1.00 31.14 ? 320 GLU A CB 1 ATOM 2542 C CG . GLU A 1 320 ? 24.448 -10.359 14.529 1.00 33.28 ? 320 GLU A CG 1 ATOM 2543 C CD . GLU A 1 320 ? 25.111 -11.652 14.980 1.00 35.20 ? 320 GLU A CD 1 ATOM 2544 O OE1 . GLU A 1 320 ? 24.413 -12.595 15.396 1.00 34.49 ? 320 GLU A OE1 1 ATOM 2545 O OE2 . GLU A 1 320 ? 26.357 -11.711 14.938 1.00 39.13 ? 320 GLU A OE2 1 ATOM 2546 N N . MET A 1 321 ? 21.095 -10.249 11.164 1.00 31.24 ? 321 MET A N 1 ATOM 2547 C CA . MET A 1 321 ? 19.749 -10.445 10.667 1.00 31.94 ? 321 MET A CA 1 ATOM 2548 C C . MET A 1 321 ? 19.572 -11.792 9.989 1.00 32.90 ? 321 MET A C 1 ATOM 2549 O O . MET A 1 321 ? 18.825 -12.638 10.426 1.00 32.58 ? 321 MET A O 1 ATOM 2550 C CB . MET A 1 321 ? 19.458 -9.345 9.653 1.00 31.79 ? 321 MET A CB 1 ATOM 2551 C CG . MET A 1 321 ? 18.144 -9.465 8.891 1.00 32.65 ? 321 MET A CG 1 ATOM 2552 S SD . MET A 1 321 ? 16.776 -8.587 9.628 1.00 36.01 ? 321 MET A SD 1 ATOM 2553 C CE . MET A 1 321 ? 15.413 -9.194 8.733 1.00 34.42 ? 321 MET A CE 1 ATOM 2554 N N . GLN A 1 322 ? 20.266 -12.000 8.892 1.00 34.51 ? 322 GLN A N 1 ATOM 2555 C CA . GLN A 1 322 ? 20.030 -13.218 8.154 1.00 36.06 ? 322 GLN A CA 1 ATOM 2556 C C . GLN A 1 322 ? 20.424 -14.491 8.876 1.00 35.44 ? 322 GLN A C 1 ATOM 2557 O O . GLN A 1 322 ? 20.053 -15.567 8.423 1.00 36.85 ? 322 GLN A O 1 ATOM 2558 C CB . GLN A 1 322 ? 20.598 -13.148 6.729 1.00 36.98 ? 322 GLN A CB 1 ATOM 2559 C CG . GLN A 1 322 ? 21.761 -12.188 6.564 1.00 41.89 ? 322 GLN A CG 1 ATOM 2560 C CD . GLN A 1 322 ? 22.619 -12.503 5.333 1.00 47.60 ? 322 GLN A CD 1 ATOM 2561 O OE1 . GLN A 1 322 ? 23.495 -11.705 4.957 1.00 50.78 ? 322 GLN A OE1 1 ATOM 2562 N NE2 . GLN A 1 322 ? 22.384 -13.669 4.713 1.00 48.57 ? 322 GLN A NE2 1 ATOM 2563 N N . LYS A 1 323 ? 21.130 -14.406 9.995 1.00 34.28 ? 323 LYS A N 1 ATOM 2564 C CA . LYS A 1 323 ? 21.437 -15.636 10.724 1.00 33.45 ? 323 LYS A CA 1 ATOM 2565 C C . LYS A 1 323 ? 20.372 -16.041 11.758 1.00 32.29 ? 323 LYS A C 1 ATOM 2566 O O . LYS A 1 323 ? 20.417 -17.151 12.332 1.00 32.51 ? 323 LYS A O 1 ATOM 2567 C CB . LYS A 1 323 ? 22.834 -15.592 11.349 1.00 33.91 ? 323 LYS A CB 1 ATOM 2568 C CG . LYS A 1 323 ? 22.865 -15.435 12.849 1.00 35.60 ? 323 LYS A CG 1 ATOM 2569 C CD . LYS A 1 323 ? 23.953 -16.331 13.526 1.00 38.50 ? 323 LYS A CD 1 ATOM 2570 C CE . LYS A 1 323 ? 25.392 -15.825 13.309 1.00 40.15 ? 323 LYS A CE 1 ATOM 2571 N NZ . LYS A 1 323 ? 25.799 -14.719 14.237 1.00 41.05 ? 323 LYS A NZ 1 ATOM 2572 N N . TRP A 1 324 ? 19.403 -15.158 11.964 1.00 30.79 ? 324 TRP A N 1 ATOM 2573 C CA . TRP A 1 324 ? 18.322 -15.388 12.906 1.00 29.48 ? 324 TRP A CA 1 ATOM 2574 C C . TRP A 1 324 ? 16.993 -15.366 12.225 1.00 29.33 ? 324 TRP A C 1 ATOM 2575 O O . TRP A 1 324 ? 16.069 -16.060 12.617 1.00 29.60 ? 324 TRP A O 1 ATOM 2576 C CB . TRP A 1 324 ? 18.308 -14.309 13.965 1.00 29.36 ? 324 TRP A CB 1 ATOM 2577 C CG . TRP A 1 324 ? 19.515 -14.302 14.771 1.00 27.97 ? 324 TRP A CG 1 ATOM 2578 C CD1 . TRP A 1 324 ? 20.486 -13.350 14.788 1.00 27.98 ? 324 TRP A CD1 1 ATOM 2579 C CD2 . TRP A 1 324 ? 19.913 -15.302 15.693 1.00 26.62 ? 324 TRP A CD2 1 ATOM 2580 N NE1 . TRP A 1 324 ? 21.470 -13.699 15.679 1.00 28.63 ? 324 TRP A NE1 1 ATOM 2581 C CE2 . TRP A 1 324 ? 21.146 -14.904 16.240 1.00 26.55 ? 324 TRP A CE2 1 ATOM 2582 C CE3 . TRP A 1 324 ? 19.354 -16.504 16.116 1.00 26.34 ? 324 TRP A CE3 1 ATOM 2583 C CZ2 . TRP A 1 324 ? 21.823 -15.659 17.174 1.00 26.12 ? 324 TRP A CZ2 1 ATOM 2584 C CZ3 . TRP A 1 324 ? 20.044 -17.265 17.048 1.00 27.13 ? 324 TRP A CZ3 1 ATOM 2585 C CH2 . TRP A 1 324 ? 21.260 -16.834 17.568 1.00 25.37 ? 324 TRP A CH2 1 ATOM 2586 N N . ILE A 1 325 ? 16.884 -14.525 11.216 1.00 29.44 ? 325 ILE A N 1 ATOM 2587 C CA . ILE A 1 325 ? 15.642 -14.358 10.473 1.00 29.38 ? 325 ILE A CA 1 ATOM 2588 C C . ILE A 1 325 ? 15.914 -14.640 9.010 1.00 30.49 ? 325 ILE A C 1 ATOM 2589 O O . ILE A 1 325 ? 16.103 -13.713 8.239 1.00 30.89 ? 325 ILE A O 1 ATOM 2590 C CB . ILE A 1 325 ? 15.130 -12.909 10.613 1.00 28.47 ? 325 ILE A CB 1 ATOM 2591 C CG1 . ILE A 1 325 ? 15.014 -12.518 12.088 1.00 27.32 ? 325 ILE A CG1 1 ATOM 2592 C CG2 . ILE A 1 325 ? 13.827 -12.731 9.880 1.00 27.16 ? 325 ILE A CG2 1 ATOM 2593 C CD1 . ILE A 1 325 ? 14.504 -11.115 12.310 1.00 24.03 ? 325 ILE A CD1 1 ATOM 2594 N N . PRO A 1 326 ? 15.973 -15.918 8.640 1.00 31.32 ? 326 PRO A N 1 ATOM 2595 C CA . PRO A 1 326 ? 16.166 -16.327 7.242 1.00 31.98 ? 326 PRO A CA 1 ATOM 2596 C C . PRO A 1 326 ? 14.950 -15.913 6.415 1.00 32.56 ? 326 PRO A C 1 ATOM 2597 O O . PRO A 1 326 ? 14.004 -15.417 7.001 1.00 33.03 ? 326 PRO A O 1 ATOM 2598 C CB . PRO A 1 326 ? 16.244 -17.863 7.343 1.00 31.98 ? 326 PRO A CB 1 ATOM 2599 C CG . PRO A 1 326 ? 15.596 -18.219 8.636 1.00 30.67 ? 326 PRO A CG 1 ATOM 2600 C CD . PRO A 1 326 ? 15.885 -17.076 9.549 1.00 31.51 ? 326 PRO A CD 1 ATOM 2601 N N . PRO A 1 327 ? 14.892 -16.172 5.119 1.00 32.97 ? 327 PRO A N 1 ATOM 2602 C CA . PRO A 1 327 ? 13.767 -15.637 4.355 1.00 33.16 ? 327 PRO A CA 1 ATOM 2603 C C . PRO A 1 327 ? 12.546 -16.504 4.608 1.00 33.16 ? 327 PRO A C 1 ATOM 2604 O O . PRO A 1 327 ? 12.662 -17.671 4.991 1.00 33.02 ? 327 PRO A O 1 ATOM 2605 C CB . PRO A 1 327 ? 14.227 -15.731 2.907 1.00 33.04 ? 327 PRO A CB 1 ATOM 2606 C CG . PRO A 1 327 ? 15.499 -16.452 2.928 1.00 33.50 ? 327 PRO A CG 1 ATOM 2607 C CD . PRO A 1 327 ? 15.748 -17.036 4.298 1.00 33.20 ? 327 PRO A CD 1 ATOM 2608 N N . TYR A 1 328 ? 11.383 -15.914 4.421 1.00 32.57 ? 328 TYR A N 1 ATOM 2609 C CA . TYR A 1 328 ? 10.162 -16.562 4.807 1.00 32.58 ? 328 TYR A CA 1 ATOM 2610 C C . TYR A 1 328 ? 9.933 -17.783 3.932 1.00 33.04 ? 328 TYR A C 1 ATOM 2611 O O . TYR A 1 328 ? 10.086 -17.714 2.711 1.00 34.33 ? 328 TYR A O 1 ATOM 2612 C CB . TYR A 1 328 ? 9.032 -15.541 4.694 1.00 32.50 ? 328 TYR A CB 1 ATOM 2613 C CG . TYR A 1 328 ? 7.636 -15.979 5.067 1.00 31.85 ? 328 TYR A CG 1 ATOM 2614 C CD1 . TYR A 1 328 ? 7.286 -16.257 6.373 1.00 31.33 ? 328 TYR A CD1 1 ATOM 2615 C CD2 . TYR A 1 328 ? 6.641 -16.032 4.120 1.00 33.30 ? 328 TYR A CD2 1 ATOM 2616 C CE1 . TYR A 1 328 ? 5.987 -16.623 6.707 1.00 28.71 ? 328 TYR A CE1 1 ATOM 2617 C CE2 . TYR A 1 328 ? 5.342 -16.392 4.459 1.00 31.93 ? 328 TYR A CE2 1 ATOM 2618 C CZ . TYR A 1 328 ? 5.036 -16.691 5.745 1.00 27.95 ? 328 TYR A CZ 1 ATOM 2619 O OH . TYR A 1 328 ? 3.764 -17.040 6.049 1.00 26.87 ? 328 TYR A OH 1 ATOM 2620 N N . GLN A 1 329 ? 9.574 -18.904 4.559 1.00 32.51 ? 329 GLN A N 1 ATOM 2621 C CA . GLN A 1 329 ? 9.261 -20.136 3.841 1.00 31.91 ? 329 GLN A CA 1 ATOM 2622 C C . GLN A 1 329 ? 7.819 -20.593 3.941 1.00 30.93 ? 329 GLN A C 1 ATOM 2623 O O . GLN A 1 329 ? 7.498 -21.674 3.440 1.00 31.23 ? 329 GLN A O 1 ATOM 2624 C CB . GLN A 1 329 ? 10.143 -21.266 4.318 1.00 31.94 ? 329 GLN A CB 1 ATOM 2625 C CG . GLN A 1 329 ? 11.557 -21.028 3.923 1.00 36.29 ? 329 GLN A CG 1 ATOM 2626 C CD . GLN A 1 329 ? 12.267 -22.309 3.686 1.00 42.39 ? 329 GLN A CD 1 ATOM 2627 O OE1 . GLN A 1 329 ? 13.126 -22.406 2.794 1.00 45.26 ? 329 GLN A OE1 1 ATOM 2628 N NE2 . GLN A 1 329 ? 11.915 -23.323 4.478 1.00 44.43 ? 329 GLN A NE2 1 ATOM 2629 N N . GLY A 1 330 ? 6.962 -19.774 4.569 1.00 29.83 ? 330 GLY A N 1 ATOM 2630 C CA . GLY A 1 330 ? 5.565 -20.100 4.827 1.00 27.77 ? 330 GLY A CA 1 ATOM 2631 C C . GLY A 1 330 ? 5.206 -20.309 6.294 1.00 26.95 ? 330 GLY A C 1 ATOM 2632 O O . GLY A 1 330 ? 6.033 -20.660 7.120 1.00 27.59 ? 330 GLY A O 1 ATOM 2633 N N . TYR A 1 331 ? 3.953 -20.084 6.629 1.00 25.87 ? 331 TYR A N 1 ATOM 2634 C CA . TYR A 1 331 ? 3.470 -20.295 7.973 1.00 25.02 ? 331 TYR A CA 1 ATOM 2635 C C . TYR A 1 331 ? 3.805 -21.681 8.499 1.00 26.01 ? 331 TYR A C 1 ATOM 2636 O O . TYR A 1 331 ? 3.559 -22.678 7.809 1.00 26.86 ? 331 TYR A O 1 ATOM 2637 C CB . TYR A 1 331 ? 1.973 -20.140 7.951 1.00 23.91 ? 331 TYR A CB 1 ATOM 2638 C CG . TYR A 1 331 ? 1.280 -20.499 9.230 1.00 23.15 ? 331 TYR A CG 1 ATOM 2639 C CD1 . TYR A 1 331 ? 1.714 -19.993 10.465 1.00 22.72 ? 331 TYR A CD1 1 ATOM 2640 C CD2 . TYR A 1 331 ? 0.155 -21.315 9.212 1.00 19.65 ? 331 TYR A CD2 1 ATOM 2641 C CE1 . TYR A 1 331 ? 1.038 -20.330 11.631 1.00 22.35 ? 331 TYR A CE1 1 ATOM 2642 C CE2 . TYR A 1 331 ? -0.499 -21.644 10.350 1.00 18.33 ? 331 TYR A CE2 1 ATOM 2643 C CZ . TYR A 1 331 ? -0.074 -21.150 11.546 1.00 19.67 ? 331 TYR A CZ 1 ATOM 2644 O OH . TYR A 1 331 ? -0.775 -21.490 12.649 1.00 18.57 ? 331 TYR A OH 1 ATOM 2645 N N . ASN A 1 332 ? 4.338 -21.726 9.724 1.00 26.34 ? 332 ASN A N 1 ATOM 2646 C CA . ASN A 1 332 ? 4.702 -22.941 10.430 1.00 27.25 ? 332 ASN A CA 1 ATOM 2647 C C . ASN A 1 332 ? 3.863 -23.119 11.713 1.00 27.40 ? 332 ASN A C 1 ATOM 2648 O O . ASN A 1 332 ? 4.172 -22.543 12.748 1.00 28.07 ? 332 ASN A O 1 ATOM 2649 C CB . ASN A 1 332 ? 6.214 -22.931 10.748 1.00 27.54 ? 332 ASN A CB 1 ATOM 2650 C CG . ASN A 1 332 ? 6.719 -24.264 11.343 1.00 30.52 ? 332 ASN A CG 1 ATOM 2651 O OD1 . ASN A 1 332 ? 5.988 -24.942 12.057 1.00 27.71 ? 332 ASN A OD1 1 ATOM 2652 N ND2 . ASN A 1 332 ? 7.981 -24.622 11.052 1.00 38.64 ? 332 ASN A ND2 1 ATOM 2653 N N . ASN A 1 333 ? 2.819 -23.942 11.660 1.00 27.45 ? 333 ASN A N 1 ATOM 2654 C CA . ASN A 1 333 ? 1.911 -24.109 12.809 1.00 27.19 ? 333 ASN A CA 1 ATOM 2655 C C . ASN A 1 333 ? 2.549 -24.633 14.115 1.00 26.67 ? 333 ASN A C 1 ATOM 2656 O O . ASN A 1 333 ? 1.891 -24.683 15.157 1.00 25.21 ? 333 ASN A O 1 ATOM 2657 C CB . ASN A 1 333 ? 0.642 -24.908 12.415 1.00 26.86 ? 333 ASN A CB 1 ATOM 2658 C CG . ASN A 1 333 ? 0.887 -26.414 12.298 1.00 28.82 ? 333 ASN A CG 1 ATOM 2659 O OD1 . ASN A 1 333 ? 0.585 -27.033 11.279 1.00 29.80 ? 333 ASN A OD1 1 ATOM 2660 N ND2 . ASN A 1 333 ? 1.396 -27.021 13.371 1.00 33.40 ? 333 ASN A ND2 1 ATOM 2661 N N . SER A 1 334 ? 3.830 -24.982 14.043 1.00 26.78 ? 334 SER A N 1 ATOM 2662 C CA . SER A 1 334 ? 4.527 -25.584 15.171 1.00 27.96 ? 334 SER A CA 1 ATOM 2663 C C . SER A 1 334 ? 5.377 -24.630 15.953 1.00 28.08 ? 334 SER A C 1 ATOM 2664 O O . SER A 1 334 ? 5.897 -24.974 17.023 1.00 29.22 ? 334 SER A O 1 ATOM 2665 C CB . SER A 1 334 ? 5.429 -26.703 14.695 1.00 27.79 ? 334 SER A CB 1 ATOM 2666 O OG . SER A 1 334 ? 4.655 -27.871 14.507 1.00 32.06 ? 334 SER A OG 1 ATOM 2667 N N . VAL A 1 335 ? 5.554 -23.455 15.375 1.00 27.29 ? 335 VAL A N 1 ATOM 2668 C CA . VAL A 1 335 ? 6.315 -22.393 15.948 1.00 26.37 ? 335 VAL A CA 1 ATOM 2669 C C . VAL A 1 335 ? 5.475 -21.712 17.005 1.00 26.41 ? 335 VAL A C 1 ATOM 2670 O O . VAL A 1 335 ? 4.268 -21.490 16.820 1.00 26.83 ? 335 VAL A O 1 ATOM 2671 C CB . VAL A 1 335 ? 6.645 -21.444 14.846 1.00 26.86 ? 335 VAL A CB 1 ATOM 2672 C CG1 . VAL A 1 335 ? 7.375 -20.208 15.372 1.00 26.01 ? 335 VAL A CG1 1 ATOM 2673 C CG2 . VAL A 1 335 ? 7.468 -22.211 13.810 1.00 26.21 ? 335 VAL A CG2 1 ATOM 2674 N N . ASP A 1 336 ? 6.106 -21.409 18.137 1.00 26.00 ? 336 ASP A N 1 ATOM 2675 C CA . ASP A 1 336 ? 5.422 -20.774 19.268 1.00 24.91 ? 336 ASP A CA 1 ATOM 2676 C C . ASP A 1 336 ? 5.504 -19.281 19.077 1.00 23.97 ? 336 ASP A C 1 ATOM 2677 O O . ASP A 1 336 ? 6.551 -18.676 19.270 1.00 24.34 ? 336 ASP A O 1 ATOM 2678 C CB . ASP A 1 336 ? 6.104 -21.170 20.576 1.00 24.91 ? 336 ASP A CB 1 ATOM 2679 C CG . ASP A 1 336 ? 5.615 -20.369 21.747 1.00 24.73 ? 336 ASP A CG 1 ATOM 2680 O OD1 . ASP A 1 336 ? 4.562 -19.739 21.604 1.00 25.94 ? 336 ASP A OD1 1 ATOM 2681 O OD2 . ASP A 1 336 ? 6.199 -20.303 22.845 1.00 24.60 ? 336 ASP A OD2 1 ATOM 2682 N N . PRO A 1 337 ? 4.386 -18.688 18.714 1.00 23.10 ? 337 PRO A N 1 ATOM 2683 C CA . PRO A 1 337 ? 4.336 -17.270 18.368 1.00 22.26 ? 337 PRO A CA 1 ATOM 2684 C C . PRO A 1 337 ? 4.407 -16.347 19.563 1.00 22.21 ? 337 PRO A C 1 ATOM 2685 O O . PRO A 1 337 ? 4.464 -15.154 19.339 1.00 22.43 ? 337 PRO A O 1 ATOM 2686 C CB . PRO A 1 337 ? 2.976 -17.122 17.726 1.00 21.51 ? 337 PRO A CB 1 ATOM 2687 C CG . PRO A 1 337 ? 2.191 -18.179 18.286 1.00 22.58 ? 337 PRO A CG 1 ATOM 2688 C CD . PRO A 1 337 ? 3.070 -19.338 18.640 1.00 23.25 ? 337 PRO A CD 1 ATOM 2689 N N . ARG A 1 338 ? 4.454 -16.864 20.789 1.00 22.00 ? 338 ARG A N 1 ATOM 2690 C CA . ARG A 1 338 ? 4.395 -16.005 21.975 1.00 21.28 ? 338 ARG A CA 1 ATOM 2691 C C . ARG A 1 338 ? 5.635 -15.200 22.316 1.00 20.40 ? 338 ARG A C 1 ATOM 2692 O O . ARG A 1 338 ? 6.747 -15.724 22.371 1.00 19.98 ? 338 ARG A O 1 ATOM 2693 C CB . ARG A 1 338 ? 4.073 -16.825 23.232 1.00 21.82 ? 338 ARG A CB 1 ATOM 2694 C CG . ARG A 1 338 ? 2.624 -17.205 23.443 1.00 22.92 ? 338 ARG A CG 1 ATOM 2695 C CD . ARG A 1 338 ? 2.462 -18.296 24.446 1.00 21.94 ? 338 ARG A CD 1 ATOM 2696 N NE . ARG A 1 338 ? 3.568 -19.228 24.359 1.00 21.38 ? 338 ARG A NE 1 ATOM 2697 C CZ . ARG A 1 338 ? 3.907 -20.058 25.333 1.00 22.91 ? 338 ARG A CZ 1 ATOM 2698 N NH1 . ARG A 1 338 ? 3.192 -20.065 26.452 1.00 22.88 ? 338 ARG A NH1 1 ATOM 2699 N NH2 . ARG A 1 338 ? 4.937 -20.891 25.185 1.00 22.23 ? 338 ARG A NH2 1 ATOM 2700 N N . ILE A 1 339 ? 5.402 -13.935 22.628 1.00 18.65 ? 339 ILE A N 1 ATOM 2701 C CA . ILE A 1 339 ? 6.441 -13.127 23.199 1.00 17.86 ? 339 ILE A CA 1 ATOM 2702 C C . ILE A 1 339 ? 6.978 -13.769 24.491 1.00 17.72 ? 339 ILE A C 1 ATOM 2703 O O . ILE A 1 339 ? 6.205 -14.121 25.388 1.00 16.89 ? 339 ILE A O 1 ATOM 2704 C CB . ILE A 1 339 ? 5.933 -11.689 23.483 1.00 17.34 ? 339 ILE A CB 1 ATOM 2705 C CG1 . ILE A 1 339 ? 5.465 -11.005 22.196 1.00 16.97 ? 339 ILE A CG1 1 ATOM 2706 C CG2 . ILE A 1 339 ? 7.037 -10.884 24.050 1.00 16.38 ? 339 ILE A CG2 1 ATOM 2707 C CD1 . ILE A 1 339 ? 6.485 -11.038 21.051 1.00 11.06 ? 339 ILE A CD1 1 ATOM 2708 N N . SER A 1 340 ? 8.305 -13.927 24.562 1.00 17.84 ? 340 SER A N 1 ATOM 2709 C CA . SER A 1 340 ? 8.971 -14.462 25.751 1.00 17.87 ? 340 SER A CA 1 ATOM 2710 C C . SER A 1 340 ? 9.201 -13.350 26.743 1.00 18.42 ? 340 SER A C 1 ATOM 2711 O O . SER A 1 340 ? 9.260 -12.165 26.365 1.00 19.69 ? 340 SER A O 1 ATOM 2712 C CB . SER A 1 340 ? 10.294 -15.138 25.415 1.00 17.60 ? 340 SER A CB 1 ATOM 2713 O OG . SER A 1 340 ? 11.299 -14.221 25.043 1.00 17.99 ? 340 SER A OG 1 ATOM 2714 N N . ASN A 1 341 ? 9.333 -13.721 28.011 1.00 17.70 ? 341 ASN A N 1 ATOM 2715 C CA . ASN A 1 341 ? 9.498 -12.745 29.046 1.00 17.09 ? 341 ASN A CA 1 ATOM 2716 C C . ASN A 1 341 ? 10.758 -11.934 28.837 1.00 16.90 ? 341 ASN A C 1 ATOM 2717 O O . ASN A 1 341 ? 10.728 -10.722 28.998 1.00 17.58 ? 341 ASN A O 1 ATOM 2718 C CB . ASN A 1 341 ? 9.455 -13.413 30.410 1.00 17.47 ? 341 ASN A CB 1 ATOM 2719 C CG . ASN A 1 341 ? 9.096 -12.444 31.563 1.00 17.57 ? 341 ASN A CG 1 ATOM 2720 O OD1 . ASN A 1 341 ? 9.660 -11.359 31.699 1.00 15.41 ? 341 ASN A OD1 1 ATOM 2721 N ND2 . ASN A 1 341 ? 8.178 -12.876 32.412 1.00 17.22 ? 341 ASN A ND2 1 ATOM 2722 N N . VAL A 1 342 ? 11.849 -12.570 28.425 1.00 16.11 ? 342 VAL A N 1 ATOM 2723 C CA . VAL A 1 342 ? 13.125 -11.839 28.238 1.00 14.64 ? 342 VAL A CA 1 ATOM 2724 C C . VAL A 1 342 ? 13.096 -10.819 27.058 1.00 14.34 ? 342 VAL A C 1 ATOM 2725 O O . VAL A 1 342 ? 13.690 -9.758 27.118 1.00 14.05 ? 342 VAL A O 1 ATOM 2726 C CB . VAL A 1 342 ? 14.303 -12.863 28.172 1.00 14.21 ? 342 VAL A CB 1 ATOM 2727 C CG1 . VAL A 1 342 ? 14.108 -13.813 27.030 1.00 13.06 ? 342 VAL A CG1 1 ATOM 2728 C CG2 . VAL A 1 342 ? 15.658 -12.189 28.128 1.00 12.31 ? 342 VAL A CG2 1 ATOM 2729 N N . PHE A 1 343 ? 12.389 -11.137 25.985 1.00 14.32 ? 343 PHE A N 1 ATOM 2730 C CA . PHE A 1 343 ? 12.215 -10.172 24.901 1.00 14.59 ? 343 PHE A CA 1 ATOM 2731 C C . PHE A 1 343 ? 11.784 -8.768 25.407 1.00 15.54 ? 343 PHE A C 1 ATOM 2732 O O . PHE A 1 343 ? 12.291 -7.759 24.921 1.00 16.04 ? 343 PHE A O 1 ATOM 2733 C CB . PHE A 1 343 ? 11.170 -10.677 23.926 1.00 13.62 ? 343 PHE A CB 1 ATOM 2734 C CG . PHE A 1 343 ? 10.950 -9.783 22.761 1.00 11.93 ? 343 PHE A CG 1 ATOM 2735 C CD1 . PHE A 1 343 ? 11.828 -9.790 21.702 1.00 11.38 ? 343 PHE A CD1 1 ATOM 2736 C CD2 . PHE A 1 343 ? 9.841 -8.944 22.701 1.00 9.53 ? 343 PHE A CD2 1 ATOM 2737 C CE1 . PHE A 1 343 ? 11.618 -8.970 20.570 1.00 10.24 ? 343 PHE A CE1 1 ATOM 2738 C CE2 . PHE A 1 343 ? 9.632 -8.140 21.613 1.00 8.59 ? 343 PHE A CE2 1 ATOM 2739 C CZ . PHE A 1 343 ? 10.538 -8.159 20.529 1.00 8.91 ? 343 PHE A CZ 1 ATOM 2740 N N . THR A 1 344 ? 10.852 -8.707 26.369 1.00 15.58 ? 344 THR A N 1 ATOM 2741 C CA . THR A 1 344 ? 10.391 -7.424 26.885 1.00 15.42 ? 344 THR A CA 1 ATOM 2742 C C . THR A 1 344 ? 11.456 -6.622 27.620 1.00 15.52 ? 344 THR A C 1 ATOM 2743 O O . THR A 1 344 ? 11.236 -5.445 27.948 1.00 16.77 ? 344 THR A O 1 ATOM 2744 C CB . THR A 1 344 ? 9.095 -7.507 27.738 1.00 15.24 ? 344 THR A CB 1 ATOM 2745 O OG1 . THR A 1 344 ? 9.415 -7.918 29.075 1.00 14.88 ? 344 THR A OG1 1 ATOM 2746 C CG2 . THR A 1 344 ? 8.135 -8.523 27.172 1.00 13.70 ? 344 THR A CG2 1 ATOM 2747 N N . PHE A 1 345 ? 12.603 -7.225 27.874 1.00 15.02 ? 345 PHE A N 1 ATOM 2748 C CA . PHE A 1 345 ? 13.711 -6.448 28.428 1.00 14.71 ? 345 PHE A CA 1 ATOM 2749 C C . PHE A 1 345 ? 14.735 -6.283 27.342 1.00 15.23 ? 345 PHE A C 1 ATOM 2750 O O . PHE A 1 345 ? 15.449 -5.281 27.312 1.00 15.97 ? 345 PHE A O 1 ATOM 2751 C CB . PHE A 1 345 ? 14.329 -7.091 29.667 1.00 13.87 ? 345 PHE A CB 1 ATOM 2752 C CG . PHE A 1 345 ? 13.373 -7.233 30.797 1.00 14.87 ? 345 PHE A CG 1 ATOM 2753 C CD1 . PHE A 1 345 ? 12.742 -8.453 31.042 1.00 14.39 ? 345 PHE A CD1 1 ATOM 2754 C CD2 . PHE A 1 345 ? 13.045 -6.133 31.594 1.00 14.91 ? 345 PHE A CD2 1 ATOM 2755 C CE1 . PHE A 1 345 ? 11.826 -8.596 32.106 1.00 16.04 ? 345 PHE A CE1 1 ATOM 2756 C CE2 . PHE A 1 345 ? 12.121 -6.266 32.654 1.00 17.33 ? 345 PHE A CE2 1 ATOM 2757 C CZ . PHE A 1 345 ? 11.514 -7.510 32.915 1.00 16.24 ? 345 PHE A CZ 1 ATOM 2758 N N . ALA A 1 346 ? 14.829 -7.255 26.435 1.00 15.09 ? 346 ALA A N 1 ATOM 2759 C CA . ALA A 1 346 ? 15.800 -7.107 25.359 1.00 14.95 ? 346 ALA A CA 1 ATOM 2760 C C . ALA A 1 346 ? 15.391 -5.913 24.525 1.00 15.06 ? 346 ALA A C 1 ATOM 2761 O O . ALA A 1 346 ? 16.203 -5.075 24.176 1.00 14.89 ? 346 ALA A O 1 ATOM 2762 C CB . ALA A 1 346 ? 15.872 -8.358 24.517 1.00 14.49 ? 346 ALA A CB 1 ATOM 2763 N N . PHE A 1 347 ? 14.107 -5.827 24.216 1.00 15.66 ? 347 PHE A N 1 ATOM 2764 C CA . PHE A 1 347 ? 13.598 -4.724 23.412 1.00 15.84 ? 347 PHE A CA 1 ATOM 2765 C C . PHE A 1 347 ? 13.795 -3.387 24.116 1.00 15.79 ? 347 PHE A C 1 ATOM 2766 O O . PHE A 1 347 ? 13.681 -2.339 23.504 1.00 16.87 ? 347 PHE A O 1 ATOM 2767 C CB . PHE A 1 347 ? 12.119 -4.930 23.060 1.00 15.75 ? 347 PHE A CB 1 ATOM 2768 C CG . PHE A 1 347 ? 11.763 -4.438 21.693 1.00 17.85 ? 347 PHE A CG 1 ATOM 2769 C CD1 . PHE A 1 347 ? 12.666 -3.676 20.965 1.00 18.63 ? 347 PHE A CD1 1 ATOM 2770 C CD2 . PHE A 1 347 ? 10.551 -4.745 21.113 1.00 17.96 ? 347 PHE A CD2 1 ATOM 2771 C CE1 . PHE A 1 347 ? 12.380 -3.231 19.707 1.00 17.12 ? 347 PHE A CE1 1 ATOM 2772 C CE2 . PHE A 1 347 ? 10.261 -4.286 19.842 1.00 17.08 ? 347 PHE A CE2 1 ATOM 2773 C CZ . PHE A 1 347 ? 11.196 -3.524 19.146 1.00 17.80 ? 347 PHE A CZ 1 ATOM 2774 N N . ARG A 1 348 ? 14.116 -3.396 25.396 1.00 15.38 ? 348 ARG A N 1 ATOM 2775 C CA . ARG A 1 348 ? 14.320 -2.118 26.063 1.00 15.14 ? 348 ARG A CA 1 ATOM 2776 C C . ARG A 1 348 ? 15.617 -1.395 25.677 1.00 14.46 ? 348 ARG A C 1 ATOM 2777 O O . ARG A 1 348 ? 15.945 -0.368 26.237 1.00 14.93 ? 348 ARG A O 1 ATOM 2778 C CB . ARG A 1 348 ? 14.194 -2.267 27.576 1.00 15.59 ? 348 ARG A CB 1 ATOM 2779 C CG . ARG A 1 348 ? 12.780 -2.591 28.037 1.00 14.66 ? 348 ARG A CG 1 ATOM 2780 C CD . ARG A 1 348 ? 12.716 -2.817 29.513 1.00 15.99 ? 348 ARG A CD 1 ATOM 2781 N NE . ARG A 1 348 ? 11.609 -3.676 29.902 1.00 16.30 ? 348 ARG A NE 1 ATOM 2782 C CZ . ARG A 1 348 ? 10.733 -3.350 30.850 1.00 18.24 ? 348 ARG A CZ 1 ATOM 2783 N NH1 . ARG A 1 348 ? 10.838 -2.194 31.511 1.00 14.38 ? 348 ARG A NH1 1 ATOM 2784 N NH2 . ARG A 1 348 ? 9.757 -4.190 31.149 1.00 19.47 ? 348 ARG A NH2 1 ATOM 2785 N N . PHE A 1 349 ? 16.333 -1.910 24.698 1.00 13.56 ? 349 PHE A N 1 ATOM 2786 C CA . PHE A 1 349 ? 17.575 -1.300 24.281 1.00 13.11 ? 349 PHE A CA 1 ATOM 2787 C C . PHE A 1 349 ? 17.304 0.043 23.697 1.00 12.97 ? 349 PHE A C 1 ATOM 2788 O O . PHE A 1 349 ? 18.161 0.932 23.676 1.00 12.40 ? 349 PHE A O 1 ATOM 2789 C CB . PHE A 1 349 ? 18.260 -2.138 23.244 1.00 12.51 ? 349 PHE A CB 1 ATOM 2790 C CG . PHE A 1 349 ? 17.570 -2.128 21.937 1.00 13.88 ? 349 PHE A CG 1 ATOM 2791 C CD1 . PHE A 1 349 ? 17.904 -1.201 20.977 1.00 9.57 ? 349 PHE A CD1 1 ATOM 2792 C CD2 . PHE A 1 349 ? 16.582 -3.090 21.642 1.00 16.01 ? 349 PHE A CD2 1 ATOM 2793 C CE1 . PHE A 1 349 ? 17.269 -1.207 19.758 1.00 11.37 ? 349 PHE A CE1 1 ATOM 2794 C CE2 . PHE A 1 349 ? 15.943 -3.108 20.400 1.00 13.98 ? 349 PHE A CE2 1 ATOM 2795 C CZ . PHE A 1 349 ? 16.270 -2.165 19.460 1.00 12.03 ? 349 PHE A CZ 1 ATOM 2796 N N . GLY A 1 350 ? 16.085 0.197 23.232 1.00 13.55 ? 350 GLY A N 1 ATOM 2797 C CA . GLY A 1 350 ? 15.671 1.467 22.671 1.00 14.41 ? 350 GLY A CA 1 ATOM 2798 C C . GLY A 1 350 ? 15.790 2.586 23.678 1.00 15.14 ? 350 GLY A C 1 ATOM 2799 O O . GLY A 1 350 ? 15.751 3.738 23.307 1.00 16.32 ? 350 GLY A O 1 ATOM 2800 N N . HIS A 1 351 ? 15.946 2.281 24.959 1.00 15.83 ? 351 HIS A N 1 ATOM 2801 C CA . HIS A 1 351 ? 15.988 3.348 25.953 1.00 16.64 ? 351 HIS A CA 1 ATOM 2802 C C . HIS A 1 351 ? 17.274 4.182 25.863 1.00 17.67 ? 351 HIS A C 1 ATOM 2803 O O . HIS A 1 351 ? 17.335 5.332 26.356 1.00 17.68 ? 351 HIS A O 1 ATOM 2804 C CB . HIS A 1 351 ? 15.756 2.777 27.352 1.00 15.58 ? 351 HIS A CB 1 ATOM 2805 C CG . HIS A 1 351 ? 14.333 2.343 27.584 1.00 17.39 ? 351 HIS A CG 1 ATOM 2806 N ND1 . HIS A 1 351 ? 13.913 1.698 28.733 1.00 15.13 ? 351 HIS A ND1 1 ATOM 2807 C CD2 . HIS A 1 351 ? 13.223 2.491 26.809 1.00 16.86 ? 351 HIS A CD2 1 ATOM 2808 C CE1 . HIS A 1 351 ? 12.616 1.464 28.646 1.00 16.43 ? 351 HIS A CE1 1 ATOM 2809 N NE2 . HIS A 1 351 ? 12.168 1.952 27.497 1.00 15.66 ? 351 HIS A NE2 1 ATOM 2810 N N . MET A 1 352 ? 18.286 3.610 25.208 1.00 17.77 ? 352 MET A N 1 ATOM 2811 C CA . MET A 1 352 ? 19.577 4.247 25.123 1.00 18.48 ? 352 MET A CA 1 ATOM 2812 C C . MET A 1 352 ? 19.595 5.046 23.878 1.00 18.16 ? 352 MET A C 1 ATOM 2813 O O . MET A 1 352 ? 20.536 5.789 23.591 1.00 18.36 ? 352 MET A O 1 ATOM 2814 C CB . MET A 1 352 ? 20.651 3.194 25.107 1.00 18.72 ? 352 MET A CB 1 ATOM 2815 C CG . MET A 1 352 ? 20.276 2.144 26.055 1.00 21.86 ? 352 MET A CG 1 ATOM 2816 S SD . MET A 1 352 ? 21.629 1.626 27.018 1.00 28.97 ? 352 MET A SD 1 ATOM 2817 C CE . MET A 1 352 ? 20.747 0.566 28.192 1.00 25.95 ? 352 MET A CE 1 ATOM 2818 N N . GLU A 1 353 ? 18.512 4.897 23.146 1.00 17.67 ? 353 GLU A N 1 ATOM 2819 C CA . GLU A 1 353 ? 18.369 5.575 21.877 1.00 17.13 ? 353 GLU A CA 1 ATOM 2820 C C . GLU A 1 353 ? 17.612 6.887 21.953 1.00 16.41 ? 353 GLU A C 1 ATOM 2821 O O . GLU A 1 353 ? 17.393 7.529 20.921 1.00 18.09 ? 353 GLU A O 1 ATOM 2822 C CB . GLU A 1 353 ? 17.717 4.623 20.874 1.00 16.47 ? 353 GLU A CB 1 ATOM 2823 C CG . GLU A 1 353 ? 18.721 3.615 20.388 1.00 16.03 ? 353 GLU A CG 1 ATOM 2824 C CD . GLU A 1 353 ? 18.150 2.594 19.441 1.00 16.29 ? 353 GLU A CD 1 ATOM 2825 O OE1 . GLU A 1 353 ? 16.972 2.696 19.048 1.00 13.81 ? 353 GLU A OE1 1 ATOM 2826 O OE2 . GLU A 1 353 ? 18.913 1.665 19.113 1.00 17.51 ? 353 GLU A OE2 1 ATOM 2827 N N . VAL A 1 354 ? 17.247 7.300 23.156 1.00 14.66 ? 354 VAL A N 1 ATOM 2828 C CA . VAL A 1 354 ? 16.414 8.486 23.342 1.00 13.77 ? 354 VAL A CA 1 ATOM 2829 C C . VAL A 1 354 ? 17.235 9.715 23.710 1.00 13.42 ? 354 VAL A C 1 ATOM 2830 O O . VAL A 1 354 ? 17.914 9.698 24.728 1.00 12.25 ? 354 VAL A O 1 ATOM 2831 C CB . VAL A 1 354 ? 15.359 8.205 24.439 1.00 14.16 ? 354 VAL A CB 1 ATOM 2832 C CG1 . VAL A 1 354 ? 14.555 9.419 24.750 1.00 13.38 ? 354 VAL A CG1 1 ATOM 2833 C CG2 . VAL A 1 354 ? 14.448 7.031 24.037 1.00 13.27 ? 354 VAL A CG2 1 ATOM 2834 N N . PRO A 1 355 ? 17.166 10.762 22.875 1.00 13.82 ? 355 PRO A N 1 ATOM 2835 C CA . PRO A 1 355 ? 17.921 12.020 23.039 1.00 14.39 ? 355 PRO A CA 1 ATOM 2836 C C . PRO A 1 355 ? 17.340 12.960 24.080 1.00 15.22 ? 355 PRO A C 1 ATOM 2837 O O . PRO A 1 355 ? 16.196 12.790 24.538 1.00 15.67 ? 355 PRO A O 1 ATOM 2838 C CB . PRO A 1 355 ? 17.792 12.693 21.698 1.00 13.30 ? 355 PRO A CB 1 ATOM 2839 C CG . PRO A 1 355 ? 17.085 11.762 20.872 1.00 14.43 ? 355 PRO A CG 1 ATOM 2840 C CD . PRO A 1 355 ? 16.319 10.807 21.689 1.00 14.45 ? 355 PRO A CD 1 ATOM 2841 N N . SER A 1 356 ? 18.122 13.953 24.480 1.00 15.78 ? 356 SER A N 1 ATOM 2842 C CA . SER A 1 356 ? 17.627 14.815 25.547 1.00 16.64 ? 356 SER A CA 1 ATOM 2843 C C . SER A 1 356 ? 16.569 15.823 25.138 1.00 16.25 ? 356 SER A C 1 ATOM 2844 O O . SER A 1 356 ? 15.816 16.245 25.970 1.00 16.06 ? 356 SER A O 1 ATOM 2845 C CB . SER A 1 356 ? 18.762 15.462 26.353 1.00 16.42 ? 356 SER A CB 1 ATOM 2846 O OG . SER A 1 356 ? 19.650 16.199 25.543 1.00 19.76 ? 356 SER A OG 1 ATOM 2847 N N . THR A 1 357 ? 16.463 16.152 23.861 1.00 17.16 ? 357 THR A N 1 ATOM 2848 C CA . THR A 1 357 ? 15.501 17.170 23.421 1.00 18.75 ? 357 THR A CA 1 ATOM 2849 C C . THR A 1 357 ? 14.595 16.761 22.240 1.00 19.86 ? 357 THR A C 1 ATOM 2850 O O . THR A 1 357 ? 14.886 15.788 21.538 1.00 19.64 ? 357 THR A O 1 ATOM 2851 C CB . THR A 1 357 ? 16.245 18.424 23.018 1.00 18.06 ? 357 THR A CB 1 ATOM 2852 O OG1 . THR A 1 357 ? 17.081 18.115 21.891 1.00 19.95 ? 357 THR A OG1 1 ATOM 2853 C CG2 . THR A 1 357 ? 17.206 18.807 24.069 1.00 17.04 ? 357 THR A CG2 1 ATOM 2854 N N . VAL A 1 358 ? 13.508 17.512 22.045 1.00 20.71 ? 358 VAL A N 1 ATOM 2855 C CA . VAL A 1 358 ? 12.645 17.342 20.878 1.00 22.62 ? 358 VAL A CA 1 ATOM 2856 C C . VAL A 1 358 ? 12.345 18.708 20.167 1.00 23.64 ? 358 VAL A C 1 ATOM 2857 O O . VAL A 1 358 ? 12.071 19.732 20.806 1.00 22.72 ? 358 VAL A O 1 ATOM 2858 C CB . VAL A 1 358 ? 11.327 16.653 21.214 1.00 22.71 ? 358 VAL A CB 1 ATOM 2859 C CG1 . VAL A 1 358 ? 10.630 16.265 19.954 1.00 23.31 ? 358 VAL A CG1 1 ATOM 2860 C CG2 . VAL A 1 358 ? 11.548 15.430 22.041 1.00 23.87 ? 358 VAL A CG2 1 ATOM 2861 N N . SER A 1 359 ? 12.408 18.696 18.838 1.00 24.77 ? 359 SER A N 1 ATOM 2862 C CA . SER A 1 359 ? 12.273 19.904 18.047 1.00 25.57 ? 359 SER A CA 1 ATOM 2863 C C . SER A 1 359 ? 11.012 19.908 17.240 1.00 26.90 ? 359 SER A C 1 ATOM 2864 O O . SER A 1 359 ? 10.512 18.854 16.797 1.00 26.72 ? 359 SER A O 1 ATOM 2865 C CB . SER A 1 359 ? 13.397 20.015 17.034 1.00 25.16 ? 359 SER A CB 1 ATOM 2866 O OG . SER A 1 359 ? 14.647 20.047 17.653 1.00 25.17 ? 359 SER A OG 1 ATOM 2867 N N . ARG A 1 360 ? 10.512 21.125 17.067 1.00 28.03 ? 360 ARG A N 1 ATOM 2868 C CA . ARG A 1 360 ? 9.437 21.399 16.148 1.00 29.41 ? 360 ARG A CA 1 ATOM 2869 C C . ARG A 1 360 ? 10.096 22.220 15.044 1.00 30.53 ? 360 ARG A C 1 ATOM 2870 O O . ARG A 1 360 ? 10.852 23.148 15.326 1.00 30.40 ? 360 ARG A O 1 ATOM 2871 C CB . ARG A 1 360 ? 8.329 22.208 16.802 1.00 29.60 ? 360 ARG A CB 1 ATOM 2872 C CG . ARG A 1 360 ? 7.470 21.395 17.717 1.00 27.89 ? 360 ARG A CG 1 ATOM 2873 C CD . ARG A 1 360 ? 7.992 21.411 19.060 1.00 24.59 ? 360 ARG A CD 1 ATOM 2874 N NE . ARG A 1 360 ? 7.267 22.387 19.846 1.00 26.68 ? 360 ARG A NE 1 ATOM 2875 C CZ . ARG A 1 360 ? 7.714 23.581 20.198 1.00 26.52 ? 360 ARG A CZ 1 ATOM 2876 N NH1 . ARG A 1 360 ? 8.898 24.012 19.813 1.00 26.76 ? 360 ARG A NH1 1 ATOM 2877 N NH2 . ARG A 1 360 ? 6.958 24.350 20.952 1.00 29.98 ? 360 ARG A NH2 1 ATOM 2878 N N . LEU A 1 361 ? 9.835 21.855 13.796 1.00 31.45 ? 361 LEU A N 1 ATOM 2879 C CA . LEU A 1 361 ? 10.408 22.563 12.673 1.00 32.75 ? 361 LEU A CA 1 ATOM 2880 C C . LEU A 1 361 ? 9.273 23.154 11.826 1.00 34.08 ? 361 LEU A C 1 ATOM 2881 O O . LEU A 1 361 ? 8.169 22.602 11.795 1.00 34.46 ? 361 LEU A O 1 ATOM 2882 C CB . LEU A 1 361 ? 11.271 21.611 11.840 1.00 32.28 ? 361 LEU A CB 1 ATOM 2883 C CG . LEU A 1 361 ? 12.419 20.898 12.551 1.00 31.74 ? 361 LEU A CG 1 ATOM 2884 C CD1 . LEU A 1 361 ? 13.366 20.187 11.572 1.00 30.09 ? 361 LEU A CD1 1 ATOM 2885 C CD2 . LEU A 1 361 ? 13.180 21.889 13.364 1.00 32.60 ? 361 LEU A CD2 1 ATOM 2886 N N . ASP A 1 362 ? 9.532 24.275 11.159 1.00 35.61 ? 362 ASP A N 1 ATOM 2887 C CA . ASP A 1 362 ? 8.533 24.884 10.289 1.00 37.69 ? 362 ASP A CA 1 ATOM 2888 C C . ASP A 1 362 ? 8.677 24.324 8.896 1.00 39.45 ? 362 ASP A C 1 ATOM 2889 O O . ASP A 1 362 ? 9.549 23.495 8.643 1.00 40.70 ? 362 ASP A O 1 ATOM 2890 C CB . ASP A 1 362 ? 8.701 26.391 10.214 1.00 37.64 ? 362 ASP A CB 1 ATOM 2891 C CG . ASP A 1 362 ? 9.982 26.802 9.512 1.00 37.51 ? 362 ASP A CG 1 ATOM 2892 O OD1 . ASP A 1 362 ? 10.533 26.004 8.743 1.00 34.84 ? 362 ASP A OD1 1 ATOM 2893 O OD2 . ASP A 1 362 ? 10.508 27.926 9.678 1.00 40.91 ? 362 ASP A OD2 1 ATOM 2894 N N . GLU A 1 363 ? 7.862 24.807 7.972 1.00 40.56 ? 363 GLU A N 1 ATOM 2895 C CA . GLU A 1 363 ? 7.835 24.253 6.624 1.00 41.85 ? 363 GLU A CA 1 ATOM 2896 C C . GLU A 1 363 ? 9.136 24.268 5.817 1.00 42.31 ? 363 GLU A C 1 ATOM 2897 O O . GLU A 1 363 ? 9.261 23.581 4.810 1.00 42.97 ? 363 GLU A O 1 ATOM 2898 C CB . GLU A 1 363 ? 6.703 24.899 5.859 1.00 42.31 ? 363 GLU A CB 1 ATOM 2899 C CG . GLU A 1 363 ? 5.513 25.196 6.751 1.00 43.55 ? 363 GLU A CG 1 ATOM 2900 C CD . GLU A 1 363 ? 4.294 25.522 5.927 1.00 46.64 ? 363 GLU A CD 1 ATOM 2901 O OE1 . GLU A 1 363 ? 3.915 24.667 5.104 1.00 46.79 ? 363 GLU A OE1 1 ATOM 2902 O OE2 . GLU A 1 363 ? 3.734 26.637 6.081 1.00 48.55 ? 363 GLU A OE2 1 ATOM 2903 N N . ASN A 1 364 ? 10.095 25.072 6.236 1.00 42.84 ? 364 ASN A N 1 ATOM 2904 C CA . ASN A 1 364 ? 11.402 25.063 5.592 1.00 43.30 ? 364 ASN A CA 1 ATOM 2905 C C . ASN A 1 364 ? 12.353 24.251 6.448 1.00 42.98 ? 364 ASN A C 1 ATOM 2906 O O . ASN A 1 364 ? 13.574 24.326 6.302 1.00 43.67 ? 364 ASN A O 1 ATOM 2907 C CB . ASN A 1 364 ? 11.949 26.489 5.452 1.00 44.13 ? 364 ASN A CB 1 ATOM 2908 C CG . ASN A 1 364 ? 11.379 27.218 4.271 1.00 44.16 ? 364 ASN A CG 1 ATOM 2909 O OD1 . ASN A 1 364 ? 11.862 28.285 3.905 1.00 48.43 ? 364 ASN A OD1 1 ATOM 2910 N ND2 . ASN A 1 364 ? 10.345 26.658 3.669 1.00 44.02 ? 364 ASN A ND2 1 ATOM 2911 N N . TYR A 1 365 ? 11.779 23.511 7.385 1.00 42.59 ? 365 TYR A N 1 ATOM 2912 C CA . TYR A 1 365 ? 12.560 22.673 8.294 1.00 42.13 ? 365 TYR A CA 1 ATOM 2913 C C . TYR A 1 365 ? 13.438 23.500 9.233 1.00 43.27 ? 365 TYR A C 1 ATOM 2914 O O . TYR A 1 365 ? 14.456 23.026 9.755 1.00 43.67 ? 365 TYR A O 1 ATOM 2915 C CB . TYR A 1 365 ? 13.367 21.661 7.519 1.00 40.95 ? 365 TYR A CB 1 ATOM 2916 C CG . TYR A 1 365 ? 12.553 20.453 7.222 1.00 37.28 ? 365 TYR A CG 1 ATOM 2917 C CD1 . TYR A 1 365 ? 12.647 19.318 8.010 1.00 35.32 ? 365 TYR A CD1 1 ATOM 2918 C CD2 . TYR A 1 365 ? 11.707 20.445 6.150 1.00 34.20 ? 365 TYR A CD2 1 ATOM 2919 C CE1 . TYR A 1 365 ? 11.917 18.196 7.738 1.00 33.85 ? 365 TYR A CE1 1 ATOM 2920 C CE2 . TYR A 1 365 ? 10.959 19.330 5.860 1.00 34.18 ? 365 TYR A CE2 1 ATOM 2921 C CZ . TYR A 1 365 ? 11.061 18.225 6.639 1.00 32.27 ? 365 TYR A CZ 1 ATOM 2922 O OH . TYR A 1 365 ? 10.305 17.108 6.335 1.00 32.36 ? 365 TYR A OH 1 ATOM 2923 N N . GLN A 1 366 ? 12.984 24.713 9.454 1.00 44.69 ? 366 GLN A N 1 ATOM 2924 C CA . GLN A 1 366 ? 13.684 25.625 10.340 1.00 46.20 ? 366 GLN A CA 1 ATOM 2925 C C . GLN A 1 366 ? 13.039 25.651 11.765 1.00 46.11 ? 366 GLN A C 1 ATOM 2926 O O . GLN A 1 366 ? 11.852 25.342 11.938 1.00 45.24 ? 366 GLN A O 1 ATOM 2927 C CB . GLN A 1 366 ? 13.681 27.042 9.723 1.00 46.83 ? 366 GLN A CB 1 ATOM 2928 C CG . GLN A 1 366 ? 14.649 27.311 8.605 1.00 50.32 ? 366 GLN A CG 1 ATOM 2929 C CD . GLN A 1 366 ? 16.043 27.656 9.082 1.00 55.90 ? 366 GLN A CD 1 ATOM 2930 O OE1 . GLN A 1 366 ? 16.194 28.415 10.036 1.00 57.95 ? 366 GLN A OE1 1 ATOM 2931 N NE2 . GLN A 1 366 ? 17.179 27.220 8.570 1.00 58.23 ? 366 GLN A NE2 1 ATOM 2932 N N . PRO A 1 367 ? 13.920 26.065 12.792 1.00 46.71 ? 367 PRO A N 1 ATOM 2933 C CA . PRO A 1 367 ? 13.482 26.192 14.213 1.00 47.25 ? 367 PRO A CA 1 ATOM 2934 C C . PRO A 1 367 ? 12.159 26.895 14.261 1.00 47.68 ? 367 PRO A C 1 ATOM 2935 O O . PRO A 1 367 ? 12.059 28.061 13.831 1.00 48.24 ? 367 PRO A O 1 ATOM 2936 C CB . PRO A 1 367 ? 14.701 26.739 14.914 1.00 47.33 ? 367 PRO A CB 1 ATOM 2937 C CG . PRO A 1 367 ? 15.796 25.984 14.212 1.00 47.06 ? 367 PRO A CG 1 ATOM 2938 C CD . PRO A 1 367 ? 15.324 25.643 12.835 1.00 46.97 ? 367 PRO A CD 1 ATOM 2939 N N . TRP A 1 368 ? 11.133 26.243 14.763 1.00 47.94 ? 368 TRP A N 1 ATOM 2940 C CA . TRP A 1 368 ? 9.761 26.741 14.708 1.00 48.17 ? 368 TRP A CA 1 ATOM 2941 C C . TRP A 1 368 ? 9.275 27.584 15.868 1.00 48.17 ? 368 TRP A C 1 ATOM 2942 O O . TRP A 1 368 ? 8.606 27.099 16.791 1.00 47.86 ? 368 TRP A O 1 ATOM 2943 C CB . TRP A 1 368 ? 8.904 25.499 14.522 1.00 48.31 ? 368 TRP A CB 1 ATOM 2944 C CG . TRP A 1 368 ? 7.448 25.771 14.347 1.00 50.08 ? 368 TRP A CG 1 ATOM 2945 C CD1 . TRP A 1 368 ? 6.811 26.055 13.183 1.00 51.46 ? 368 TRP A CD1 1 ATOM 2946 C CD2 . TRP A 1 368 ? 6.432 25.775 15.370 1.00 50.69 ? 368 TRP A CD2 1 ATOM 2947 N NE1 . TRP A 1 368 ? 5.467 26.240 13.414 1.00 52.85 ? 368 TRP A NE1 1 ATOM 2948 C CE2 . TRP A 1 368 ? 5.211 26.074 14.749 1.00 51.22 ? 368 TRP A CE2 1 ATOM 2949 C CE3 . TRP A 1 368 ? 6.438 25.561 16.749 1.00 51.27 ? 368 TRP A CE3 1 ATOM 2950 C CZ2 . TRP A 1 368 ? 4.010 26.166 15.453 1.00 51.94 ? 368 TRP A CZ2 1 ATOM 2951 C CZ3 . TRP A 1 368 ? 5.248 25.638 17.445 1.00 51.72 ? 368 TRP A CZ3 1 ATOM 2952 C CH2 . TRP A 1 368 ? 4.051 25.945 16.799 1.00 52.22 ? 368 TRP A CH2 1 ATOM 2953 N N . GLY A 1 369 ? 9.627 28.870 15.847 1.00 47.85 ? 369 GLY A N 1 ATOM 2954 C CA . GLY A 1 369 ? 9.313 29.749 16.936 1.00 47.41 ? 369 GLY A CA 1 ATOM 2955 C C . GLY A 1 369 ? 10.599 29.888 17.747 1.00 47.03 ? 369 GLY A C 1 ATOM 2956 O O . GLY A 1 369 ? 11.665 29.478 17.294 1.00 47.46 ? 369 GLY A O 1 ATOM 2957 N N . PRO A 1 370 ? 10.514 30.452 18.913 1.00 46.19 ? 370 PRO A N 1 ATOM 2958 C CA . PRO A 1 370 ? 11.662 30.638 19.804 1.00 45.20 ? 370 PRO A CA 1 ATOM 2959 C C . PRO A 1 370 ? 11.876 29.529 20.822 1.00 43.72 ? 370 PRO A C 1 ATOM 2960 O O . PRO A 1 370 ? 12.964 29.399 21.386 1.00 43.39 ? 370 PRO A O 1 ATOM 2961 C CB . PRO A 1 370 ? 11.314 31.954 20.522 1.00 45.33 ? 370 PRO A CB 1 ATOM 2962 C CG . PRO A 1 370 ? 9.844 31.968 20.573 1.00 45.63 ? 370 PRO A CG 1 ATOM 2963 C CD . PRO A 1 370 ? 9.325 31.174 19.390 1.00 46.39 ? 370 PRO A CD 1 ATOM 2964 N N . GLU A 1 371 ? 10.836 28.756 21.079 1.00 42.07 ? 371 GLU A N 1 ATOM 2965 C CA . GLU A 1 371 ? 10.941 27.693 22.064 1.00 40.82 ? 371 GLU A CA 1 ATOM 2966 C C . GLU A 1 371 ? 10.808 26.363 21.300 1.00 39.01 ? 371 GLU A C 1 ATOM 2967 O O . GLU A 1 371 ? 9.983 25.511 21.609 1.00 38.22 ? 371 GLU A O 1 ATOM 2968 C CB . GLU A 1 371 ? 9.902 27.937 23.172 1.00 40.88 ? 371 GLU A CB 1 ATOM 2969 C CG . GLU A 1 371 ? 10.097 29.313 23.819 1.00 43.39 ? 371 GLU A CG 1 ATOM 2970 C CD . GLU A 1 371 ? 9.135 29.660 24.968 1.00 47.70 ? 371 GLU A CD 1 ATOM 2971 O OE1 . GLU A 1 371 ? 7.926 29.297 24.889 1.00 49.69 ? 371 GLU A OE1 1 ATOM 2972 O OE2 . GLU A 1 371 ? 9.584 30.328 25.956 1.00 46.51 ? 371 GLU A OE2 1 ATOM 2973 N N . ALA A 1 372 ? 11.671 26.221 20.291 1.00 37.37 ? 372 ALA A N 1 ATOM 2974 C CA . ALA A 1 372 ? 11.595 25.149 19.300 1.00 35.91 ? 372 ALA A CA 1 ATOM 2975 C C . ALA A 1 372 ? 12.131 23.803 19.777 1.00 34.99 ? 372 ALA A C 1 ATOM 2976 O O . ALA A 1 372 ? 11.634 22.721 19.398 1.00 34.95 ? 372 ALA A O 1 ATOM 2977 C CB . ALA A 1 372 ? 12.319 25.572 18.066 1.00 36.18 ? 372 ALA A CB 1 ATOM 2978 N N . GLU A 1 373 ? 13.154 23.889 20.610 1.00 33.02 ? 373 GLU A N 1 ATOM 2979 C CA . GLU A 1 373 ? 13.750 22.730 21.172 1.00 31.27 ? 373 GLU A CA 1 ATOM 2980 C C . GLU A 1 373 ? 13.282 22.620 22.586 1.00 29.64 ? 373 GLU A C 1 ATOM 2981 O O . GLU A 1 373 ? 13.353 23.582 23.341 1.00 30.04 ? 373 GLU A O 1 ATOM 2982 C CB . GLU A 1 373 ? 15.225 22.903 21.171 1.00 31.87 ? 373 GLU A CB 1 ATOM 2983 C CG . GLU A 1 373 ? 15.938 21.675 20.689 1.00 34.81 ? 373 GLU A CG 1 ATOM 2984 C CD . GLU A 1 373 ? 17.423 21.843 20.812 1.00 38.92 ? 373 GLU A CD 1 ATOM 2985 O OE1 . GLU A 1 373 ? 17.860 22.502 21.778 1.00 39.66 ? 373 GLU A OE1 1 ATOM 2986 O OE2 . GLU A 1 373 ? 18.149 21.328 19.944 1.00 43.17 ? 373 GLU A OE2 1 ATOM 2987 N N . LEU A 1 374 ? 12.805 21.442 22.959 1.00 27.06 ? 374 LEU A N 1 ATOM 2988 C CA . LEU A 1 374 ? 12.305 21.248 24.303 1.00 24.34 ? 374 LEU A CA 1 ATOM 2989 C C . LEU A 1 374 ? 13.046 20.107 24.988 1.00 22.69 ? 374 LEU A C 1 ATOM 2990 O O . LEU A 1 374 ? 13.543 19.214 24.333 1.00 22.58 ? 374 LEU A O 1 ATOM 2991 C CB . LEU A 1 374 ? 10.798 20.988 24.249 1.00 23.99 ? 374 LEU A CB 1 ATOM 2992 C CG . LEU A 1 374 ? 9.871 22.101 23.748 1.00 23.01 ? 374 LEU A CG 1 ATOM 2993 C CD1 . LEU A 1 374 ? 8.459 21.760 24.090 1.00 26.05 ? 374 LEU A CD1 1 ATOM 2994 C CD2 . LEU A 1 374 ? 10.142 23.458 24.324 1.00 22.87 ? 374 LEU A CD2 1 ATOM 2995 N N . PRO A 1 375 ? 13.219 20.162 26.297 1.00 21.47 ? 375 PRO A N 1 ATOM 2996 C CA . PRO A 1 375 ? 13.796 19.009 26.998 1.00 20.47 ? 375 PRO A CA 1 ATOM 2997 C C . PRO A 1 375 ? 12.746 17.886 27.086 1.00 20.10 ? 375 PRO A C 1 ATOM 2998 O O . PRO A 1 375 ? 11.548 18.092 27.343 1.00 18.70 ? 375 PRO A O 1 ATOM 2999 C CB . PRO A 1 375 ? 14.120 19.552 28.387 1.00 19.54 ? 375 PRO A CB 1 ATOM 3000 C CG . PRO A 1 375 ? 14.008 20.967 28.267 1.00 19.24 ? 375 PRO A CG 1 ATOM 3001 C CD . PRO A 1 375 ? 12.966 21.284 27.216 1.00 20.82 ? 375 PRO A CD 1 ATOM 3002 N N . LEU A 1 376 ? 13.233 16.676 26.867 1.00 20.04 ? 376 LEU A N 1 ATOM 3003 C CA . LEU A 1 376 ? 12.371 15.532 26.767 1.00 20.02 ? 376 LEU A CA 1 ATOM 3004 C C . LEU A 1 376 ? 11.463 15.487 27.946 1.00 21.14 ? 376 LEU A C 1 ATOM 3005 O O . LEU A 1 376 ? 10.299 15.115 27.818 1.00 21.89 ? 376 LEU A O 1 ATOM 3006 C CB . LEU A 1 376 ? 13.204 14.275 26.747 1.00 19.48 ? 376 LEU A CB 1 ATOM 3007 C CG . LEU A 1 376 ? 12.772 12.992 26.036 1.00 18.08 ? 376 LEU A CG 1 ATOM 3008 C CD1 . LEU A 1 376 ? 13.048 11.892 27.013 1.00 17.87 ? 376 LEU A CD1 1 ATOM 3009 C CD2 . LEU A 1 376 ? 11.334 12.958 25.601 1.00 14.22 ? 376 LEU A CD2 1 ATOM 3010 N N . HIS A 1 377 ? 11.964 15.906 29.099 1.00 21.82 ? 377 HIS A N 1 ATOM 3011 C CA . HIS A 1 377 ? 11.195 15.652 30.292 1.00 22.42 ? 377 HIS A CA 1 ATOM 3012 C C . HIS A 1 377 ? 9.900 16.451 30.403 1.00 22.57 ? 377 HIS A C 1 ATOM 3013 O O . HIS A 1 377 ? 9.021 16.091 31.166 1.00 24.26 ? 377 HIS A O 1 ATOM 3014 C CB . HIS A 1 377 ? 12.059 15.749 31.530 1.00 22.59 ? 377 HIS A CB 1 ATOM 3015 C CG . HIS A 1 377 ? 12.151 17.126 32.089 1.00 21.97 ? 377 HIS A CG 1 ATOM 3016 N ND1 . HIS A 1 377 ? 13.231 17.948 31.855 1.00 20.85 ? 377 HIS A ND1 1 ATOM 3017 C CD2 . HIS A 1 377 ? 11.319 17.810 32.903 1.00 22.08 ? 377 HIS A CD2 1 ATOM 3018 C CE1 . HIS A 1 377 ? 13.046 19.097 32.475 1.00 21.06 ? 377 HIS A CE1 1 ATOM 3019 N NE2 . HIS A 1 377 ? 11.897 19.035 33.126 1.00 24.41 ? 377 HIS A NE2 1 ATOM 3020 N N . THR A 1 378 ? 9.751 17.499 29.616 1.00 22.10 ? 378 THR A N 1 ATOM 3021 C CA . THR A 1 378 ? 8.501 18.246 29.623 1.00 21.00 ? 378 THR A CA 1 ATOM 3022 C C . THR A 1 378 ? 7.533 17.663 28.628 1.00 21.45 ? 378 THR A C 1 ATOM 3023 O O . THR A 1 378 ? 6.459 18.225 28.408 1.00 21.95 ? 378 THR A O 1 ATOM 3024 C CB . THR A 1 378 ? 8.711 19.712 29.234 1.00 20.69 ? 378 THR A CB 1 ATOM 3025 O OG1 . THR A 1 378 ? 9.066 19.778 27.852 1.00 18.89 ? 378 THR A OG1 1 ATOM 3026 C CG2 . THR A 1 378 ? 9.883 20.343 30.000 1.00 19.60 ? 378 THR A CG2 1 ATOM 3027 N N . LEU A 1 379 ? 7.896 16.550 28.002 1.00 21.38 ? 379 LEU A N 1 ATOM 3028 C CA . LEU A 1 379 ? 6.984 15.938 27.032 1.00 20.87 ? 379 LEU A CA 1 ATOM 3029 C C . LEU A 1 379 ? 6.314 14.624 27.479 1.00 20.46 ? 379 LEU A C 1 ATOM 3030 O O . LEU A 1 379 ? 5.497 14.070 26.753 1.00 20.18 ? 379 LEU A O 1 ATOM 3031 C CB . LEU A 1 379 ? 7.636 15.827 25.669 1.00 20.66 ? 379 LEU A CB 1 ATOM 3032 C CG . LEU A 1 379 ? 8.166 17.184 25.206 1.00 21.61 ? 379 LEU A CG 1 ATOM 3033 C CD1 . LEU A 1 379 ? 9.014 17.011 23.956 1.00 23.61 ? 379 LEU A CD1 1 ATOM 3034 C CD2 . LEU A 1 379 ? 7.049 18.160 24.938 1.00 19.19 ? 379 LEU A CD2 1 ATOM 3035 N N . PHE A 1 380 ? 6.638 14.129 28.672 1.00 20.29 ? 380 PHE A N 1 ATOM 3036 C CA . PHE A 1 380 ? 5.948 12.961 29.193 1.00 19.82 ? 380 PHE A CA 1 ATOM 3037 C C . PHE A 1 380 ? 4.494 13.355 29.445 1.00 20.83 ? 380 PHE A C 1 ATOM 3038 O O . PHE A 1 380 ? 4.223 14.371 30.093 1.00 20.85 ? 380 PHE A O 1 ATOM 3039 C CB . PHE A 1 380 ? 6.624 12.451 30.453 1.00 19.04 ? 380 PHE A CB 1 ATOM 3040 C CG . PHE A 1 380 ? 8.088 12.171 30.269 1.00 17.72 ? 380 PHE A CG 1 ATOM 3041 C CD1 . PHE A 1 380 ? 8.537 11.567 29.127 1.00 15.45 ? 380 PHE A CD1 1 ATOM 3042 C CD2 . PHE A 1 380 ? 9.015 12.556 31.222 1.00 16.16 ? 380 PHE A CD2 1 ATOM 3043 C CE1 . PHE A 1 380 ? 9.864 11.324 28.946 1.00 14.14 ? 380 PHE A CE1 1 ATOM 3044 C CE2 . PHE A 1 380 ? 10.336 12.331 31.021 1.00 15.89 ? 380 PHE A CE2 1 ATOM 3045 C CZ . PHE A 1 380 ? 10.753 11.697 29.875 1.00 13.93 ? 380 PHE A CZ 1 ATOM 3046 N N . PHE A 1 381 ? 3.564 12.586 28.871 1.00 21.54 ? 381 PHE A N 1 ATOM 3047 C CA . PHE A 1 381 ? 2.136 12.857 29.013 1.00 22.29 ? 381 PHE A CA 1 ATOM 3048 C C . PHE A 1 381 ? 1.805 14.306 28.744 1.00 23.18 ? 381 PHE A C 1 ATOM 3049 O O . PHE A 1 381 ? 1.035 14.926 29.474 1.00 23.52 ? 381 PHE A O 1 ATOM 3050 C CB . PHE A 1 381 ? 1.655 12.457 30.398 1.00 22.05 ? 381 PHE A CB 1 ATOM 3051 C CG . PHE A 1 381 ? 1.933 11.063 30.690 1.00 21.52 ? 381 PHE A CG 1 ATOM 3052 C CD1 . PHE A 1 381 ? 1.059 10.076 30.261 1.00 18.34 ? 381 PHE A CD1 1 ATOM 3053 C CD2 . PHE A 1 381 ? 3.127 10.710 31.288 1.00 20.88 ? 381 PHE A CD2 1 ATOM 3054 C CE1 . PHE A 1 381 ? 1.332 8.770 30.472 1.00 14.95 ? 381 PHE A CE1 1 ATOM 3055 C CE2 . PHE A 1 381 ? 3.403 9.389 31.515 1.00 20.30 ? 381 PHE A CE2 1 ATOM 3056 C CZ . PHE A 1 381 ? 2.495 8.420 31.102 1.00 18.42 ? 381 PHE A CZ 1 ATOM 3057 N N . ASN A 1 382 ? 2.404 14.841 27.694 1.00 23.72 ? 382 ASN A N 1 ATOM 3058 C CA . ASN A 1 382 ? 2.165 16.198 27.291 1.00 24.49 ? 382 ASN A CA 1 ATOM 3059 C C . ASN A 1 382 ? 1.398 16.095 25.987 1.00 24.97 ? 382 ASN A C 1 ATOM 3060 O O . ASN A 1 382 ? 1.970 15.710 24.981 1.00 26.42 ? 382 ASN A O 1 ATOM 3061 C CB . ASN A 1 382 ? 3.507 16.941 27.146 1.00 24.17 ? 382 ASN A CB 1 ATOM 3062 C CG . ASN A 1 382 ? 3.349 18.384 26.678 1.00 25.94 ? 382 ASN A CG 1 ATOM 3063 O OD1 . ASN A 1 382 ? 2.518 18.691 25.804 1.00 25.84 ? 382 ASN A OD1 1 ATOM 3064 N ND2 . ASN A 1 382 ? 4.179 19.279 27.233 1.00 26.31 ? 382 ASN A ND2 1 ATOM 3065 N N . THR A 1 383 ? 0.092 16.354 26.009 1.00 25.11 ? 383 THR A N 1 ATOM 3066 C CA . THR A 1 383 ? -0.706 16.400 24.788 1.00 25.31 ? 383 THR A CA 1 ATOM 3067 C C . THR A 1 383 ? -1.053 17.838 24.447 1.00 25.91 ? 383 THR A C 1 ATOM 3068 O O . THR A 1 383 ? -1.531 18.115 23.363 1.00 26.30 ? 383 THR A O 1 ATOM 3069 C CB . THR A 1 383 ? -2.034 15.723 24.994 1.00 25.47 ? 383 THR A CB 1 ATOM 3070 O OG1 . THR A 1 383 ? -2.586 16.220 26.207 1.00 26.80 ? 383 THR A OG1 1 ATOM 3071 C CG2 . THR A 1 383 ? -1.904 14.199 25.232 1.00 24.53 ? 383 THR A CG2 1 ATOM 3072 N N . TRP A 1 384 ? -0.828 18.764 25.362 1.00 26.12 ? 384 TRP A N 1 ATOM 3073 C CA . TRP A 1 384 ? -1.242 20.129 25.108 1.00 26.79 ? 384 TRP A CA 1 ATOM 3074 C C . TRP A 1 384 ? -0.407 20.832 24.073 1.00 27.57 ? 384 TRP A C 1 ATOM 3075 O O . TRP A 1 384 ? -0.900 21.743 23.377 1.00 28.22 ? 384 TRP A O 1 ATOM 3076 C CB . TRP A 1 384 ? -1.349 20.953 26.400 1.00 26.47 ? 384 TRP A CB 1 ATOM 3077 C CG . TRP A 1 384 ? -0.075 21.418 27.042 1.00 25.79 ? 384 TRP A CG 1 ATOM 3078 C CD1 . TRP A 1 384 ? 0.538 20.876 28.131 1.00 24.56 ? 384 TRP A CD1 1 ATOM 3079 C CD2 . TRP A 1 384 ? 0.673 22.573 26.704 1.00 24.12 ? 384 TRP A CD2 1 ATOM 3080 N NE1 . TRP A 1 384 ? 1.645 21.611 28.470 1.00 24.38 ? 384 TRP A NE1 1 ATOM 3081 C CE2 . TRP A 1 384 ? 1.753 22.655 27.595 1.00 25.45 ? 384 TRP A CE2 1 ATOM 3082 C CE3 . TRP A 1 384 ? 0.547 23.544 25.734 1.00 25.22 ? 384 TRP A CE3 1 ATOM 3083 C CZ2 . TRP A 1 384 ? 2.697 23.659 27.527 1.00 26.06 ? 384 TRP A CZ2 1 ATOM 3084 C CZ3 . TRP A 1 384 ? 1.489 24.523 25.652 1.00 26.01 ? 384 TRP A CZ3 1 ATOM 3085 C CH2 . TRP A 1 384 ? 2.543 24.585 26.545 1.00 27.70 ? 384 TRP A CH2 1 ATOM 3086 N N . ARG A 1 385 ? 0.846 20.409 23.962 1.00 28.18 ? 385 ARG A N 1 ATOM 3087 C CA . ARG A 1 385 ? 1.775 20.998 23.006 1.00 28.64 ? 385 ARG A CA 1 ATOM 3088 C C . ARG A 1 385 ? 1.376 20.517 21.629 1.00 29.56 ? 385 ARG A C 1 ATOM 3089 O O . ARG A 1 385 ? 1.753 21.100 20.621 1.00 29.90 ? 385 ARG A O 1 ATOM 3090 C CB . ARG A 1 385 ? 3.210 20.584 23.321 1.00 28.58 ? 385 ARG A CB 1 ATOM 3091 C CG . ARG A 1 385 ? 3.890 21.349 24.401 1.00 27.21 ? 385 ARG A CG 1 ATOM 3092 C CD . ARG A 1 385 ? 4.662 22.531 23.891 1.00 29.31 ? 385 ARG A CD 1 ATOM 3093 N NE . ARG A 1 385 ? 5.465 23.104 24.964 1.00 31.62 ? 385 ARG A NE 1 ATOM 3094 C CZ . ARG A 1 385 ? 5.974 24.324 24.972 1.00 32.07 ? 385 ARG A CZ 1 ATOM 3095 N NH1 . ARG A 1 385 ? 5.775 25.144 23.939 1.00 32.42 ? 385 ARG A NH1 1 ATOM 3096 N NH2 . ARG A 1 385 ? 6.699 24.715 26.016 1.00 30.66 ? 385 ARG A NH2 1 ATOM 3097 N N . ILE A 1 386 ? 0.621 19.434 21.556 1.00 30.57 ? 386 ILE A N 1 ATOM 3098 C CA . ILE A 1 386 ? 0.129 19.063 20.241 1.00 31.77 ? 386 ILE A CA 1 ATOM 3099 C C . ILE A 1 386 ? -1.041 19.978 19.864 1.00 33.10 ? 386 ILE A C 1 ATOM 3100 O O . ILE A 1 386 ? -0.970 20.736 18.900 1.00 34.43 ? 386 ILE A O 1 ATOM 3101 C CB . ILE A 1 386 ? -0.290 17.607 20.144 1.00 31.00 ? 386 ILE A CB 1 ATOM 3102 C CG1 . ILE A 1 386 ? 0.933 16.688 20.164 1.00 30.66 ? 386 ILE A CG1 1 ATOM 3103 C CG2 . ILE A 1 386 ? -0.966 17.397 18.828 1.00 31.46 ? 386 ILE A CG2 1 ATOM 3104 C CD1 . ILE A 1 386 ? 0.577 15.189 20.174 1.00 27.73 ? 386 ILE A CD1 1 ATOM 3105 N N . ILE A 1 387 ? -2.087 19.943 20.672 1.00 33.84 ? 387 ILE A N 1 ATOM 3106 C CA . ILE A 1 387 ? -3.321 20.620 20.366 1.00 34.16 ? 387 ILE A CA 1 ATOM 3107 C C . ILE A 1 387 ? -3.234 22.098 20.477 1.00 35.54 ? 387 ILE A C 1 ATOM 3108 O O . ILE A 1 387 ? -3.882 22.787 19.718 1.00 36.29 ? 387 ILE A O 1 ATOM 3109 C CB . ILE A 1 387 ? -4.403 20.071 21.277 1.00 34.13 ? 387 ILE A CB 1 ATOM 3110 C CG1 . ILE A 1 387 ? -4.774 18.687 20.760 1.00 33.59 ? 387 ILE A CG1 1 ATOM 3111 C CG2 . ILE A 1 387 ? -5.592 21.006 21.363 1.00 31.46 ? 387 ILE A CG2 1 ATOM 3112 C CD1 . ILE A 1 387 ? -5.155 17.803 21.813 1.00 35.52 ? 387 ILE A CD1 1 ATOM 3113 N N . LYS A 1 388 ? -2.441 22.600 21.413 1.00 37.09 ? 388 LYS A N 1 ATOM 3114 C CA . LYS A 1 388 ? -2.302 24.045 21.546 1.00 38.63 ? 388 LYS A CA 1 ATOM 3115 C C . LYS A 1 388 ? -0.944 24.539 21.077 1.00 39.20 ? 388 LYS A C 1 ATOM 3116 O O . LYS A 1 388 ? -0.461 25.533 21.588 1.00 40.10 ? 388 LYS A O 1 ATOM 3117 C CB . LYS A 1 388 ? -2.555 24.501 22.979 1.00 38.90 ? 388 LYS A CB 1 ATOM 3118 C CG . LYS A 1 388 ? -3.932 24.135 23.503 1.00 40.61 ? 388 LYS A CG 1 ATOM 3119 C CD . LYS A 1 388 ? -4.990 24.980 22.872 1.00 43.10 ? 388 LYS A CD 1 ATOM 3120 C CE . LYS A 1 388 ? -4.710 26.467 23.095 1.00 44.55 ? 388 LYS A CE 1 ATOM 3121 N NZ . LYS A 1 388 ? -5.631 27.361 22.304 1.00 46.23 ? 388 LYS A NZ 1 ATOM 3122 N N . ASP A 1 389 ? -0.312 23.813 20.155 1.00 39.50 ? 389 ASP A N 1 ATOM 3123 C CA . ASP A 1 389 ? 0.910 24.272 19.500 1.00 39.20 ? 389 ASP A CA 1 ATOM 3124 C C . ASP A 1 389 ? 1.104 23.679 18.118 1.00 39.18 ? 389 ASP A C 1 ATOM 3125 O O . ASP A 1 389 ? 2.048 22.920 17.892 1.00 40.50 ? 389 ASP A O 1 ATOM 3126 C CB . ASP A 1 389 ? 2.162 23.960 20.284 1.00 39.78 ? 389 ASP A CB 1 ATOM 3127 C CG . ASP A 1 389 ? 2.636 25.113 21.104 1.00 42.23 ? 389 ASP A CG 1 ATOM 3128 O OD1 . ASP A 1 389 ? 2.455 26.276 20.692 1.00 44.98 ? 389 ASP A OD1 1 ATOM 3129 O OD2 . ASP A 1 389 ? 3.230 24.950 22.186 1.00 45.95 ? 389 ASP A OD2 1 ATOM 3130 N N . GLY A 1 390 ? 0.189 23.984 17.209 1.00 38.11 ? 390 GLY A N 1 ATOM 3131 C CA . GLY A 1 390 ? 0.423 23.766 15.795 1.00 35.48 ? 390 GLY A CA 1 ATOM 3132 C C . GLY A 1 390 ? 0.357 22.372 15.242 1.00 33.89 ? 390 GLY A C 1 ATOM 3133 O O . GLY A 1 390 ? 0.827 22.137 14.130 1.00 33.87 ? 390 GLY A O 1 ATOM 3134 N N . GLY A 1 391 ? -0.200 21.451 16.015 1.00 31.98 ? 391 GLY A N 1 ATOM 3135 C CA . GLY A 1 391 ? -0.462 20.126 15.503 1.00 30.63 ? 391 GLY A CA 1 ATOM 3136 C C . GLY A 1 391 ? 0.747 19.236 15.422 1.00 29.52 ? 391 GLY A C 1 ATOM 3137 O O . GLY A 1 391 ? 1.746 19.496 16.067 1.00 29.66 ? 391 GLY A O 1 ATOM 3138 N N . ILE A 1 392 ? 0.681 18.203 14.600 1.00 28.41 ? 392 ILE A N 1 ATOM 3139 C CA . ILE A 1 392 ? 1.773 17.256 14.578 1.00 27.86 ? 392 ILE A CA 1 ATOM 3140 C C . ILE A 1 392 ? 2.768 17.498 13.459 1.00 27.65 ? 392 ILE A C 1 ATOM 3141 O O . ILE A 1 392 ? 3.877 16.976 13.479 1.00 27.35 ? 392 ILE A O 1 ATOM 3142 C CB . ILE A 1 392 ? 1.247 15.811 14.530 1.00 27.38 ? 392 ILE A CB 1 ATOM 3143 C CG1 . ILE A 1 392 ? 0.544 15.563 13.212 1.00 27.34 ? 392 ILE A CG1 1 ATOM 3144 C CG2 . ILE A 1 392 ? 0.318 15.547 15.683 1.00 26.90 ? 392 ILE A CG2 1 ATOM 3145 C CD1 . ILE A 1 392 ? 0.178 14.153 12.991 1.00 27.12 ? 392 ILE A CD1 1 ATOM 3146 N N . ASP A 1 393 ? 2.386 18.296 12.470 1.00 27.66 ? 393 ASP A N 1 ATOM 3147 C CA . ASP A 1 393 ? 3.315 18.549 11.366 1.00 26.31 ? 393 ASP A CA 1 ATOM 3148 C C . ASP A 1 393 ? 4.684 18.995 11.857 1.00 25.02 ? 393 ASP A C 1 ATOM 3149 O O . ASP A 1 393 ? 5.682 18.411 11.463 1.00 25.30 ? 393 ASP A O 1 ATOM 3150 C CB . ASP A 1 393 ? 2.718 19.493 10.360 1.00 26.38 ? 393 ASP A CB 1 ATOM 3151 C CG . ASP A 1 393 ? 1.674 18.809 9.489 1.00 29.38 ? 393 ASP A CG 1 ATOM 3152 O OD1 . ASP A 1 393 ? 1.297 17.626 9.744 1.00 29.44 ? 393 ASP A OD1 1 ATOM 3153 O OD2 . ASP A 1 393 ? 1.165 19.390 8.511 1.00 33.53 ? 393 ASP A OD2 1 ATOM 3154 N N . PRO A 1 394 ? 4.761 19.995 12.733 1.00 23.69 ? 394 PRO A N 1 ATOM 3155 C CA . PRO A 1 394 ? 6.076 20.393 13.272 1.00 22.94 ? 394 PRO A CA 1 ATOM 3156 C C . PRO A 1 394 ? 6.881 19.247 13.990 1.00 22.31 ? 394 PRO A C 1 ATOM 3157 O O . PRO A 1 394 ? 8.098 19.157 13.842 1.00 21.53 ? 394 PRO A O 1 ATOM 3158 C CB . PRO A 1 394 ? 5.730 21.540 14.233 1.00 23.25 ? 394 PRO A CB 1 ATOM 3159 C CG . PRO A 1 394 ? 4.313 22.028 13.800 1.00 22.18 ? 394 PRO A CG 1 ATOM 3160 C CD . PRO A 1 394 ? 3.650 20.826 13.254 1.00 23.18 ? 394 PRO A CD 1 ATOM 3161 N N . LEU A 1 395 ? 6.212 18.377 14.740 1.00 21.49 ? 395 LEU A N 1 ATOM 3162 C CA . LEU A 1 395 ? 6.904 17.262 15.373 1.00 21.02 ? 395 LEU A CA 1 ATOM 3163 C C . LEU A 1 395 ? 7.296 16.200 14.349 1.00 20.90 ? 395 LEU A C 1 ATOM 3164 O O . LEU A 1 395 ? 8.362 15.549 14.463 1.00 20.90 ? 395 LEU A O 1 ATOM 3165 C CB . LEU A 1 395 ? 6.041 16.613 16.458 1.00 20.99 ? 395 LEU A CB 1 ATOM 3166 C CG . LEU A 1 395 ? 5.702 17.443 17.692 1.00 20.94 ? 395 LEU A CG 1 ATOM 3167 C CD1 . LEU A 1 395 ? 4.475 16.914 18.387 1.00 19.72 ? 395 LEU A CD1 1 ATOM 3168 C CD2 . LEU A 1 395 ? 6.875 17.472 18.635 1.00 21.71 ? 395 LEU A CD2 1 ATOM 3169 N N . VAL A 1 396 ? 6.437 16.011 13.360 1.00 20.37 ? 396 VAL A N 1 ATOM 3170 C CA . VAL A 1 396 ? 6.706 15.022 12.357 1.00 20.77 ? 396 VAL A CA 1 ATOM 3171 C C . VAL A 1 396 ? 7.946 15.420 11.568 1.00 21.34 ? 396 VAL A C 1 ATOM 3172 O O . VAL A 1 396 ? 8.743 14.572 11.190 1.00 22.63 ? 396 VAL A O 1 ATOM 3173 C CB . VAL A 1 396 ? 5.497 14.761 11.443 1.00 20.86 ? 396 VAL A CB 1 ATOM 3174 C CG1 . VAL A 1 396 ? 5.841 13.754 10.387 1.00 18.21 ? 396 VAL A CG1 1 ATOM 3175 C CG2 . VAL A 1 396 ? 4.323 14.262 12.267 1.00 21.84 ? 396 VAL A CG2 1 ATOM 3176 N N . ARG A 1 397 ? 8.177 16.692 11.331 1.00 21.39 ? 397 ARG A N 1 ATOM 3177 C CA . ARG A 1 397 ? 9.379 16.976 10.565 1.00 22.01 ? 397 ARG A CA 1 ATOM 3178 C C . ARG A 1 397 ? 10.603 16.780 11.476 1.00 22.03 ? 397 ARG A C 1 ATOM 3179 O O . ARG A 1 397 ? 11.641 16.314 11.031 1.00 22.22 ? 397 ARG A O 1 ATOM 3180 C CB . ARG A 1 397 ? 9.369 18.367 9.938 1.00 22.76 ? 397 ARG A CB 1 ATOM 3181 C CG . ARG A 1 397 ? 8.084 18.818 9.269 1.00 24.11 ? 397 ARG A CG 1 ATOM 3182 C CD . ARG A 1 397 ? 8.014 20.361 9.090 1.00 26.65 ? 397 ARG A CD 1 ATOM 3183 N NE . ARG A 1 397 ? 7.040 20.759 8.074 1.00 26.44 ? 397 ARG A NE 1 ATOM 3184 C CZ . ARG A 1 397 ? 5.874 21.338 8.326 1.00 26.14 ? 397 ARG A CZ 1 ATOM 3185 N NH1 . ARG A 1 397 ? 5.504 21.637 9.572 1.00 23.11 ? 397 ARG A NH1 1 ATOM 3186 N NH2 . ARG A 1 397 ? 5.075 21.641 7.311 1.00 28.22 ? 397 ARG A NH2 1 ATOM 3187 N N . GLY A 1 398 ? 10.482 17.145 12.749 1.00 22.09 ? 398 GLY A N 1 ATOM 3188 C CA . GLY A 1 398 ? 11.521 16.844 13.728 1.00 22.19 ? 398 GLY A CA 1 ATOM 3189 C C . GLY A 1 398 ? 11.909 15.362 13.707 1.00 22.76 ? 398 GLY A C 1 ATOM 3190 O O . GLY A 1 398 ? 13.088 15.042 13.802 1.00 22.33 ? 398 GLY A O 1 ATOM 3191 N N . LEU A 1 399 ? 10.917 14.467 13.575 1.00 22.98 ? 399 LEU A N 1 ATOM 3192 C CA . LEU A 1 399 ? 11.154 13.018 13.500 1.00 23.14 ? 399 LEU A CA 1 ATOM 3193 C C . LEU A 1 399 ? 12.080 12.632 12.341 1.00 23.69 ? 399 LEU A C 1 ATOM 3194 O O . LEU A 1 399 ? 12.895 11.704 12.455 1.00 23.36 ? 399 LEU A O 1 ATOM 3195 C CB . LEU A 1 399 ? 9.822 12.247 13.372 1.00 22.67 ? 399 LEU A CB 1 ATOM 3196 C CG . LEU A 1 399 ? 9.070 11.802 14.642 1.00 22.50 ? 399 LEU A CG 1 ATOM 3197 C CD1 . LEU A 1 399 ? 7.740 11.120 14.283 1.00 19.70 ? 399 LEU A CD1 1 ATOM 3198 C CD2 . LEU A 1 399 ? 9.935 10.906 15.578 1.00 20.09 ? 399 LEU A CD2 1 ATOM 3199 N N . LEU A 1 400 ? 11.952 13.343 11.218 1.00 24.05 ? 400 LEU A N 1 ATOM 3200 C CA . LEU A 1 400 ? 12.749 13.013 10.044 1.00 23.99 ? 400 LEU A CA 1 ATOM 3201 C C . LEU A 1 400 ? 14.092 13.719 9.994 1.00 23.60 ? 400 LEU A C 1 ATOM 3202 O O . LEU A 1 400 ? 15.060 13.157 9.479 1.00 23.51 ? 400 LEU A O 1 ATOM 3203 C CB . LEU A 1 400 ? 11.977 13.366 8.788 1.00 23.86 ? 400 LEU A CB 1 ATOM 3204 C CG . LEU A 1 400 ? 10.674 12.609 8.618 1.00 26.08 ? 400 LEU A CG 1 ATOM 3205 C CD1 . LEU A 1 400 ? 9.779 13.335 7.627 1.00 27.35 ? 400 LEU A CD1 1 ATOM 3206 C CD2 . LEU A 1 400 ? 10.921 11.164 8.178 1.00 26.49 ? 400 LEU A CD2 1 ATOM 3207 N N . ALA A 1 401 ? 14.137 14.943 10.524 1.00 23.11 ? 401 ALA A N 1 ATOM 3208 C CA . ALA A 1 401 ? 15.303 15.824 10.387 1.00 22.76 ? 401 ALA A CA 1 ATOM 3209 C C . ALA A 1 401 ? 16.328 15.673 11.482 1.00 22.62 ? 401 ALA A C 1 ATOM 3210 O O . ALA A 1 401 ? 17.479 16.005 11.282 1.00 22.82 ? 401 ALA A O 1 ATOM 3211 C CB . ALA A 1 401 ? 14.866 17.280 10.299 1.00 22.13 ? 401 ALA A CB 1 ATOM 3212 N N . LYS A 1 402 ? 15.901 15.178 12.641 1.00 22.57 ? 402 LYS A N 1 ATOM 3213 C CA . LYS A 1 402 ? 16.765 15.058 13.811 1.00 22.23 ? 402 LYS A CA 1 ATOM 3214 C C . LYS A 1 402 ? 17.242 13.629 13.959 1.00 21.87 ? 402 LYS A C 1 ATOM 3215 O O . LYS A 1 402 ? 16.692 12.758 13.335 1.00 21.79 ? 402 LYS A O 1 ATOM 3216 C CB . LYS A 1 402 ? 15.973 15.472 15.021 1.00 22.16 ? 402 LYS A CB 1 ATOM 3217 C CG . LYS A 1 402 ? 15.540 16.916 14.905 1.00 24.80 ? 402 LYS A CG 1 ATOM 3218 C CD . LYS A 1 402 ? 16.699 17.815 15.233 1.00 27.16 ? 402 LYS A CD 1 ATOM 3219 C CE . LYS A 1 402 ? 16.531 19.153 14.595 1.00 27.70 ? 402 LYS A CE 1 ATOM 3220 N NZ . LYS A 1 402 ? 17.500 20.109 15.220 1.00 32.04 ? 402 LYS A NZ 1 ATOM 3221 N N . LYS A 1 403 ? 18.257 13.381 14.780 1.00 21.25 ? 403 LYS A N 1 ATOM 3222 C CA . LYS A 1 403 ? 18.812 12.044 14.868 1.00 21.17 ? 403 LYS A CA 1 ATOM 3223 C C . LYS A 1 403 ? 18.473 11.331 16.169 1.00 20.96 ? 403 LYS A C 1 ATOM 3224 O O . LYS A 1 403 ? 18.147 11.956 17.168 1.00 21.19 ? 403 LYS A O 1 ATOM 3225 C CB . LYS A 1 403 ? 20.329 12.102 14.734 1.00 21.19 ? 403 LYS A CB 1 ATOM 3226 C CG . LYS A 1 403 ? 20.869 12.580 13.397 1.00 22.13 ? 403 LYS A CG 1 ATOM 3227 C CD . LYS A 1 403 ? 22.376 12.887 13.497 1.00 25.07 ? 403 LYS A CD 1 ATOM 3228 C CE . LYS A 1 403 ? 22.826 13.934 12.497 1.00 27.29 ? 403 LYS A CE 1 ATOM 3229 N NZ . LYS A 1 403 ? 22.588 13.452 11.093 1.00 32.44 ? 403 LYS A NZ 1 ATOM 3230 N N . SER A 1 404 ? 18.544 10.010 16.139 1.00 20.27 ? 404 SER A N 1 ATOM 3231 C CA . SER A 1 404 ? 18.413 9.230 17.347 1.00 19.27 ? 404 SER A CA 1 ATOM 3232 C C . SER A 1 404 ? 19.670 9.486 18.172 1.00 18.86 ? 404 SER A C 1 ATOM 3233 O O . SER A 1 404 ? 20.650 10.044 17.677 1.00 18.06 ? 404 SER A O 1 ATOM 3234 C CB . SER A 1 404 ? 18.361 7.728 17.006 1.00 19.07 ? 404 SER A CB 1 ATOM 3235 O OG . SER A 1 404 ? 17.068 7.294 16.583 1.00 19.30 ? 404 SER A OG 1 ATOM 3236 N N . LYS A 1 405 ? 19.634 9.052 19.439 1.00 18.92 ? 405 LYS A N 1 ATOM 3237 C CA . LYS A 1 405 ? 20.832 8.989 20.282 1.00 17.32 ? 405 LYS A CA 1 ATOM 3238 C C . LYS A 1 405 ? 21.501 7.653 19.992 1.00 16.95 ? 405 LYS A C 1 ATOM 3239 O O . LYS A 1 405 ? 20.824 6.654 19.786 1.00 16.14 ? 405 LYS A O 1 ATOM 3240 C CB . LYS A 1 405 ? 20.484 9.063 21.766 1.00 16.45 ? 405 LYS A CB 1 ATOM 3241 C CG . LYS A 1 405 ? 21.687 8.895 22.673 1.00 13.95 ? 405 LYS A CG 1 ATOM 3242 C CD . LYS A 1 405 ? 21.262 8.729 24.101 1.00 11.93 ? 405 LYS A CD 1 ATOM 3243 C CE . LYS A 1 405 ? 22.429 8.271 24.941 1.00 12.12 ? 405 LYS A CE 1 ATOM 3244 N NZ . LYS A 1 405 ? 22.953 6.983 24.404 1.00 12.68 ? 405 LYS A NZ 1 ATOM 3245 N N . LEU A 1 406 ? 22.822 7.667 19.946 1.00 17.03 ? 406 LEU A N 1 ATOM 3246 C CA . LEU A 1 406 ? 23.612 6.471 19.799 1.00 18.11 ? 406 LEU A CA 1 ATOM 3247 C C . LEU A 1 406 ? 23.940 5.805 21.165 1.00 19.78 ? 406 LEU A C 1 ATOM 3248 O O . LEU A 1 406 ? 24.380 6.463 22.135 1.00 20.13 ? 406 LEU A O 1 ATOM 3249 C CB . LEU A 1 406 ? 24.906 6.814 19.058 1.00 17.31 ? 406 LEU A CB 1 ATOM 3250 C CG . LEU A 1 406 ? 25.798 5.636 18.637 1.00 16.29 ? 406 LEU A CG 1 ATOM 3251 C CD1 . LEU A 1 406 ? 25.255 4.915 17.379 1.00 16.56 ? 406 LEU A CD1 1 ATOM 3252 C CD2 . LEU A 1 406 ? 27.200 6.046 18.431 1.00 11.26 ? 406 LEU A CD2 1 ATOM 3253 N N . MET A 1 407 ? 23.701 4.502 21.246 1.00 21.49 ? 407 MET A N 1 ATOM 3254 C CA . MET A 1 407 ? 24.096 3.747 22.419 1.00 23.61 ? 407 MET A CA 1 ATOM 3255 C C . MET A 1 407 ? 25.562 3.959 22.463 1.00 24.19 ? 407 MET A C 1 ATOM 3256 O O . MET A 1 407 ? 26.227 3.962 21.431 1.00 24.46 ? 407 MET A O 1 ATOM 3257 C CB . MET A 1 407 ? 23.833 2.261 22.259 1.00 23.43 ? 407 MET A CB 1 ATOM 3258 C CG . MET A 1 407 ? 23.596 1.546 23.585 1.00 28.26 ? 407 MET A CG 1 ATOM 3259 S SD . MET A 1 407 ? 25.022 1.340 24.682 1.00 36.51 ? 407 MET A SD 1 ATOM 3260 C CE . MET A 1 407 ? 26.237 0.793 23.458 1.00 35.46 ? 407 MET A CE 1 ATOM 3261 N N . ASN A 1 408 ? 26.073 4.095 23.666 1.00 25.24 ? 408 ASN A N 1 ATOM 3262 C CA . ASN A 1 408 ? 27.465 4.396 23.866 1.00 26.69 ? 408 ASN A CA 1 ATOM 3263 C C . ASN A 1 408 ? 27.841 3.948 25.289 1.00 26.69 ? 408 ASN A C 1 ATOM 3264 O O . ASN A 1 408 ? 27.241 4.388 26.257 1.00 26.70 ? 408 ASN A O 1 ATOM 3265 C CB . ASN A 1 408 ? 27.585 5.892 23.656 1.00 27.67 ? 408 ASN A CB 1 ATOM 3266 C CG . ASN A 1 408 ? 28.967 6.408 23.849 1.00 31.35 ? 408 ASN A CG 1 ATOM 3267 O OD1 . ASN A 1 408 ? 29.634 6.104 24.852 1.00 38.04 ? 408 ASN A OD1 1 ATOM 3268 N ND2 . ASN A 1 408 ? 29.407 7.238 22.918 1.00 33.02 ? 408 ASN A ND2 1 ATOM 3269 N N . GLN A 1 409 ? 28.810 3.045 25.409 1.00 26.63 ? 409 GLN A N 1 ATOM 3270 C CA . GLN A 1 409 ? 29.166 2.444 26.697 1.00 26.33 ? 409 GLN A CA 1 ATOM 3271 C C . GLN A 1 409 ? 29.423 3.400 27.845 1.00 27.56 ? 409 GLN A C 1 ATOM 3272 O O . GLN A 1 409 ? 29.292 3.002 29.006 1.00 27.11 ? 409 GLN A O 1 ATOM 3273 C CB . GLN A 1 409 ? 30.366 1.530 26.552 1.00 25.89 ? 409 GLN A CB 1 ATOM 3274 C CG . GLN A 1 409 ? 30.092 0.243 25.840 1.00 25.09 ? 409 GLN A CG 1 ATOM 3275 C CD . GLN A 1 409 ? 31.374 -0.507 25.542 1.00 27.64 ? 409 GLN A CD 1 ATOM 3276 O OE1 . GLN A 1 409 ? 32.443 0.098 25.434 1.00 26.74 ? 409 GLN A OE1 1 ATOM 3277 N NE2 . GLN A 1 409 ? 31.285 -1.833 25.435 1.00 28.86 ? 409 GLN A NE2 1 ATOM 3278 N N . ASP A 1 410 ? 29.806 4.643 27.526 1.00 29.05 ? 410 ASP A N 1 ATOM 3279 C CA . ASP A 1 410 ? 30.053 5.677 28.540 1.00 30.50 ? 410 ASP A CA 1 ATOM 3280 C C . ASP A 1 410 ? 28.836 6.550 28.764 1.00 30.39 ? 410 ASP A C 1 ATOM 3281 O O . ASP A 1 410 ? 28.626 7.008 29.869 1.00 32.69 ? 410 ASP A O 1 ATOM 3282 C CB . ASP A 1 410 ? 31.211 6.588 28.147 1.00 31.01 ? 410 ASP A CB 1 ATOM 3283 C CG . ASP A 1 410 ? 32.467 5.821 27.798 1.00 36.05 ? 410 ASP A CG 1 ATOM 3284 O OD1 . ASP A 1 410 ? 32.752 4.759 28.407 1.00 41.43 ? 410 ASP A OD1 1 ATOM 3285 O OD2 . ASP A 1 410 ? 33.249 6.202 26.905 1.00 42.13 ? 410 ASP A OD2 1 ATOM 3286 N N . LYS A 1 411 ? 28.047 6.803 27.725 1.00 29.39 ? 411 LYS A N 1 ATOM 3287 C CA . LYS A 1 411 ? 26.845 7.650 27.824 1.00 28.05 ? 411 LYS A CA 1 ATOM 3288 C C . LYS A 1 411 ? 25.633 6.828 27.487 1.00 26.54 ? 411 LYS A C 1 ATOM 3289 O O . LYS A 1 411 ? 25.319 6.638 26.351 1.00 26.97 ? 411 LYS A O 1 ATOM 3290 C CB . LYS A 1 411 ? 26.984 8.817 26.859 1.00 28.65 ? 411 LYS A CB 1 ATOM 3291 C CG . LYS A 1 411 ? 28.296 9.586 27.113 1.00 29.25 ? 411 LYS A CG 1 ATOM 3292 C CD . LYS A 1 411 ? 28.527 10.648 26.095 1.00 30.17 ? 411 LYS A CD 1 ATOM 3293 C CE . LYS A 1 411 ? 29.504 11.700 26.567 1.00 31.73 ? 411 LYS A CE 1 ATOM 3294 N NZ . LYS A 1 411 ? 29.496 12.851 25.587 1.00 35.33 ? 411 LYS A NZ 1 ATOM 3295 N N . MET A 1 412 ? 24.911 6.382 28.487 1.00 24.71 ? 412 MET A N 1 ATOM 3296 C CA . MET A 1 412 ? 24.043 5.243 28.274 1.00 22.52 ? 412 MET A CA 1 ATOM 3297 C C . MET A 1 412 ? 22.551 5.547 28.214 1.00 21.83 ? 412 MET A C 1 ATOM 3298 O O . MET A 1 412 ? 21.869 5.099 27.314 1.00 22.29 ? 412 MET A O 1 ATOM 3299 C CB . MET A 1 412 ? 24.413 4.227 29.346 1.00 22.49 ? 412 MET A CB 1 ATOM 3300 C CG . MET A 1 412 ? 23.983 2.831 29.128 1.00 22.13 ? 412 MET A CG 1 ATOM 3301 S SD . MET A 1 412 ? 24.952 1.640 30.144 1.00 21.76 ? 412 MET A SD 1 ATOM 3302 C CE . MET A 1 412 ? 26.164 1.384 29.279 1.00 16.35 ? 412 MET A CE 1 ATOM 3303 N N . VAL A 1 413 ? 22.031 6.300 29.168 1.00 20.42 ? 413 VAL A N 1 ATOM 3304 C CA . VAL A 1 413 ? 20.636 6.695 29.134 1.00 18.52 ? 413 VAL A CA 1 ATOM 3305 C C . VAL A 1 413 ? 20.596 8.145 29.599 1.00 18.16 ? 413 VAL A C 1 ATOM 3306 O O . VAL A 1 413 ? 21.203 8.503 30.626 1.00 17.68 ? 413 VAL A O 1 ATOM 3307 C CB . VAL A 1 413 ? 19.727 5.860 30.092 1.00 18.95 ? 413 VAL A CB 1 ATOM 3308 C CG1 . VAL A 1 413 ? 18.324 6.491 30.129 1.00 17.92 ? 413 VAL A CG1 1 ATOM 3309 C CG2 . VAL A 1 413 ? 19.654 4.362 29.714 1.00 16.50 ? 413 VAL A CG2 1 ATOM 3310 N N . THR A 1 414 ? 19.856 8.968 28.870 1.00 16.97 ? 414 THR A N 1 ATOM 3311 C CA . THR A 1 414 ? 19.845 10.397 29.131 1.00 15.93 ? 414 THR A CA 1 ATOM 3312 C C . THR A 1 414 ? 19.141 10.749 30.409 1.00 16.72 ? 414 THR A C 1 ATOM 3313 O O . THR A 1 414 ? 18.151 10.099 30.794 1.00 15.87 ? 414 THR A O 1 ATOM 3314 C CB . THR A 1 414 ? 19.224 11.160 27.978 1.00 15.66 ? 414 THR A CB 1 ATOM 3315 O OG1 . THR A 1 414 ? 19.193 12.533 28.328 1.00 13.55 ? 414 THR A OG1 1 ATOM 3316 C CG2 . THR A 1 414 ? 17.748 10.831 27.811 1.00 13.73 ? 414 THR A CG2 1 ATOM 3317 N N . SER A 1 415 ? 19.636 11.812 31.044 1.00 17.19 ? 415 SER A N 1 ATOM 3318 C CA . SER A 1 415 ? 19.112 12.247 32.324 1.00 17.98 ? 415 SER A CA 1 ATOM 3319 C C . SER A 1 415 ? 17.655 12.572 32.245 1.00 18.50 ? 415 SER A C 1 ATOM 3320 O O . SER A 1 415 ? 16.901 12.421 33.246 1.00 19.27 ? 415 SER A O 1 ATOM 3321 C CB . SER A 1 415 ? 19.865 13.432 32.837 1.00 17.90 ? 415 SER A CB 1 ATOM 3322 O OG . SER A 1 415 ? 21.122 13.004 33.360 1.00 20.92 ? 415 SER A OG 1 ATOM 3323 N N . GLU A 1 416 ? 17.242 12.984 31.054 1.00 18.08 ? 416 GLU A N 1 ATOM 3324 C CA . GLU A 1 416 ? 15.841 13.220 30.818 1.00 18.10 ? 416 GLU A CA 1 ATOM 3325 C C . GLU A 1 416 ? 15.018 11.982 31.224 1.00 18.01 ? 416 GLU A C 1 ATOM 3326 O O . GLU A 1 416 ? 13.895 12.115 31.741 1.00 18.78 ? 416 GLU A O 1 ATOM 3327 C CB . GLU A 1 416 ? 15.626 13.594 29.363 1.00 18.22 ? 416 GLU A CB 1 ATOM 3328 C CG . GLU A 1 416 ? 16.219 14.946 28.999 1.00 19.38 ? 416 GLU A CG 1 ATOM 3329 C CD . GLU A 1 416 ? 15.809 16.041 29.974 1.00 23.55 ? 416 GLU A CD 1 ATOM 3330 O OE1 . GLU A 1 416 ? 16.712 16.646 30.588 1.00 27.00 ? 416 GLU A OE1 1 ATOM 3331 O OE2 . GLU A 1 416 ? 14.591 16.318 30.135 1.00 24.40 ? 416 GLU A OE2 1 ATOM 3332 N N . LEU A 1 417 ? 15.578 10.785 31.042 1.00 17.07 ? 417 LEU A N 1 ATOM 3333 C CA . LEU A 1 417 ? 14.863 9.585 31.434 1.00 16.51 ? 417 LEU A CA 1 ATOM 3334 C C . LEU A 1 417 ? 15.369 9.031 32.731 1.00 17.27 ? 417 LEU A C 1 ATOM 3335 O O . LEU A 1 417 ? 14.629 8.350 33.428 1.00 17.24 ? 417 LEU A O 1 ATOM 3336 C CB . LEU A 1 417 ? 15.014 8.484 30.388 1.00 16.16 ? 417 LEU A CB 1 ATOM 3337 C CG . LEU A 1 417 ? 14.329 8.646 29.057 1.00 14.25 ? 417 LEU A CG 1 ATOM 3338 C CD1 . LEU A 1 417 ? 14.895 7.680 28.145 1.00 15.95 ? 417 LEU A CD1 1 ATOM 3339 C CD2 . LEU A 1 417 ? 12.888 8.388 29.243 1.00 13.01 ? 417 LEU A CD2 1 ATOM 3340 N N . ARG A 1 418 ? 16.641 9.280 33.051 1.00 18.48 ? 418 ARG A N 1 ATOM 3341 C CA . ARG A 1 418 ? 17.261 8.658 34.237 1.00 19.27 ? 418 ARG A CA 1 ATOM 3342 C C . ARG A 1 418 ? 17.031 9.395 35.540 1.00 20.21 ? 418 ARG A C 1 ATOM 3343 O O . ARG A 1 418 ? 17.262 8.863 36.622 1.00 20.97 ? 418 ARG A O 1 ATOM 3344 C CB . ARG A 1 418 ? 18.759 8.505 34.030 1.00 19.21 ? 418 ARG A CB 1 ATOM 3345 C CG . ARG A 1 418 ? 19.307 7.265 34.651 1.00 17.68 ? 418 ARG A CG 1 ATOM 3346 C CD . ARG A 1 418 ? 20.813 7.191 34.602 1.00 17.90 ? 418 ARG A CD 1 ATOM 3347 N NE . ARG A 1 418 ? 21.421 8.326 35.279 1.00 15.90 ? 418 ARG A NE 1 ATOM 3348 C CZ . ARG A 1 418 ? 21.542 8.408 36.585 1.00 18.20 ? 418 ARG A CZ 1 ATOM 3349 N NH1 . ARG A 1 418 ? 21.118 7.403 37.366 1.00 18.85 ? 418 ARG A NH1 1 ATOM 3350 N NH2 . ARG A 1 418 ? 22.112 9.473 37.106 1.00 18.98 ? 418 ARG A NH2 1 ATOM 3351 N N . ASN A 1 419 ? 16.594 10.639 35.437 1.00 21.21 ? 419 ASN A N 1 ATOM 3352 C CA . ASN A 1 419 ? 16.386 11.458 36.619 1.00 21.60 ? 419 ASN A CA 1 ATOM 3353 C C . ASN A 1 419 ? 15.049 12.138 36.667 1.00 22.37 ? 419 ASN A C 1 ATOM 3354 O O . ASN A 1 419 ? 14.551 12.423 37.746 1.00 22.53 ? 419 ASN A O 1 ATOM 3355 C CB . ASN A 1 419 ? 17.501 12.505 36.748 1.00 20.77 ? 419 ASN A CB 1 ATOM 3356 C CG . ASN A 1 419 ? 18.709 11.948 37.451 1.00 20.80 ? 419 ASN A CG 1 ATOM 3357 O OD1 . ASN A 1 419 ? 18.566 11.282 38.475 1.00 22.44 ? 419 ASN A OD1 1 ATOM 3358 N ND2 . ASN A 1 419 ? 19.895 12.163 36.893 1.00 18.69 ? 419 ASN A ND2 1 ATOM 3359 N N . LYS A 1 420 ? 14.465 12.380 35.497 1.00 23.58 ? 420 LYS A N 1 ATOM 3360 C CA . LYS A 1 420 ? 13.331 13.277 35.388 1.00 23.65 ? 420 LYS A CA 1 ATOM 3361 C C . LYS A 1 420 ? 12.115 12.595 34.782 1.00 23.95 ? 420 LYS A C 1 ATOM 3362 O O . LYS A 1 420 ? 11.232 13.266 34.266 1.00 24.75 ? 420 LYS A O 1 ATOM 3363 C CB . LYS A 1 420 ? 13.740 14.486 34.533 1.00 24.17 ? 420 LYS A CB 1 ATOM 3364 C CG . LYS A 1 420 ? 15.162 15.127 34.827 1.00 25.01 ? 420 LYS A CG 1 ATOM 3365 C CD . LYS A 1 420 ? 15.092 16.376 35.698 1.00 27.51 ? 420 LYS A CD 1 ATOM 3366 C CE . LYS A 1 420 ? 16.236 17.359 35.423 1.00 29.12 ? 420 LYS A CE 1 ATOM 3367 N NZ . LYS A 1 420 ? 16.356 17.675 33.967 1.00 30.63 ? 420 LYS A NZ 1 ATOM 3368 N N . LEU A 1 421 ? 12.044 11.266 34.848 1.00 23.42 ? 421 LEU A N 1 ATOM 3369 C CA . LEU A 1 421 ? 10.901 10.575 34.278 1.00 22.76 ? 421 LEU A CA 1 ATOM 3370 C C . LEU A 1 421 ? 9.635 10.842 35.114 1.00 23.81 ? 421 LEU A C 1 ATOM 3371 O O . LEU A 1 421 ? 9.654 10.853 36.345 1.00 22.99 ? 421 LEU A O 1 ATOM 3372 C CB . LEU A 1 421 ? 11.179 9.067 34.129 1.00 22.05 ? 421 LEU A CB 1 ATOM 3373 C CG . LEU A 1 421 ? 10.053 8.141 33.629 1.00 19.75 ? 421 LEU A CG 1 ATOM 3374 C CD1 . LEU A 1 421 ? 9.798 8.367 32.202 1.00 16.79 ? 421 LEU A CD1 1 ATOM 3375 C CD2 . LEU A 1 421 ? 10.345 6.691 33.839 1.00 16.55 ? 421 LEU A CD2 1 ATOM 3376 N N . PHE A 1 422 ? 8.543 11.096 34.412 1.00 25.14 ? 422 PHE A N 1 ATOM 3377 C CA . PHE A 1 422 ? 7.258 11.329 35.021 1.00 26.57 ? 422 PHE A CA 1 ATOM 3378 C C . PHE A 1 422 ? 6.468 10.044 34.883 1.00 27.36 ? 422 PHE A C 1 ATOM 3379 O O . PHE A 1 422 ? 6.298 9.551 33.775 1.00 27.32 ? 422 PHE A O 1 ATOM 3380 C CB . PHE A 1 422 ? 6.535 12.490 34.310 1.00 26.09 ? 422 PHE A CB 1 ATOM 3381 C CG . PHE A 1 422 ? 5.196 12.802 34.896 1.00 27.52 ? 422 PHE A CG 1 ATOM 3382 C CD1 . PHE A 1 422 ? 5.060 13.790 35.869 1.00 30.15 ? 422 PHE A CD1 1 ATOM 3383 C CD2 . PHE A 1 422 ? 4.069 12.088 34.507 1.00 27.75 ? 422 PHE A CD2 1 ATOM 3384 C CE1 . PHE A 1 422 ? 3.821 14.065 36.425 1.00 29.90 ? 422 PHE A CE1 1 ATOM 3385 C CE2 . PHE A 1 422 ? 2.835 12.341 35.057 1.00 26.51 ? 422 PHE A CE2 1 ATOM 3386 C CZ . PHE A 1 422 ? 2.705 13.325 36.018 1.00 29.14 ? 422 PHE A CZ 1 ATOM 3387 N N . GLN A 1 423 ? 5.974 9.518 36.004 1.00 29.62 ? 423 GLN A N 1 ATOM 3388 C CA . GLN A 1 423 ? 5.176 8.260 36.055 1.00 31.09 ? 423 GLN A CA 1 ATOM 3389 C C . GLN A 1 423 ? 3.713 8.684 36.246 1.00 32.98 ? 423 GLN A C 1 ATOM 3390 O O . GLN A 1 423 ? 3.408 9.506 37.128 1.00 32.40 ? 423 GLN A O 1 ATOM 3391 C CB . GLN A 1 423 ? 5.627 7.427 37.238 1.00 30.78 ? 423 GLN A CB 1 ATOM 3392 C CG . GLN A 1 423 ? 6.904 6.686 37.003 1.00 30.87 ? 423 GLN A CG 1 ATOM 3393 C CD . GLN A 1 423 ? 6.620 5.244 36.556 1.00 30.60 ? 423 GLN A CD 1 ATOM 3394 O OE1 . GLN A 1 423 ? 6.928 4.273 37.262 1.00 28.98 ? 423 GLN A OE1 1 ATOM 3395 N NE2 . GLN A 1 423 ? 5.994 5.118 35.401 1.00 30.43 ? 423 GLN A NE2 1 ATOM 3396 N N . PRO A 1 424 ? 2.820 8.105 35.445 1.00 34.86 ? 424 PRO A N 1 ATOM 3397 C CA . PRO A 1 424 ? 1.412 8.509 35.327 1.00 36.77 ? 424 PRO A CA 1 ATOM 3398 C C . PRO A 1 424 ? 0.602 8.471 36.611 1.00 38.84 ? 424 PRO A C 1 ATOM 3399 O O . PRO A 1 424 ? -0.537 8.954 36.631 1.00 39.22 ? 424 PRO A O 1 ATOM 3400 C CB . PRO A 1 424 ? 0.853 7.464 34.373 1.00 36.46 ? 424 PRO A CB 1 ATOM 3401 C CG . PRO A 1 424 ? 1.740 6.332 34.559 1.00 35.80 ? 424 PRO A CG 1 ATOM 3402 C CD . PRO A 1 424 ? 3.098 6.947 34.600 1.00 35.30 ? 424 PRO A CD 1 ATOM 3403 N N . THR A 1 425 ? 1.210 7.952 37.669 1.00 41.19 ? 425 THR A N 1 ATOM 3404 C CA . THR A 1 425 ? 0.539 7.747 38.930 1.00 43.74 ? 425 THR A CA 1 ATOM 3405 C C . THR A 1 425 ? 1.002 8.685 40.039 1.00 44.51 ? 425 THR A C 1 ATOM 3406 O O . THR A 1 425 ? 0.284 8.928 40.989 1.00 45.80 ? 425 THR A O 1 ATOM 3407 C CB . THR A 1 425 ? 0.841 6.325 39.313 1.00 44.54 ? 425 THR A CB 1 ATOM 3408 O OG1 . THR A 1 425 ? 0.677 5.500 38.140 1.00 46.82 ? 425 THR A OG1 1 ATOM 3409 C CG2 . THR A 1 425 ? -0.166 5.779 40.359 1.00 46.14 ? 425 THR A CG2 1 ATOM 3410 N N . HIS A 1 426 ? 2.198 9.233 39.907 1.00 45.16 ? 426 HIS A N 1 ATOM 3411 C CA . HIS A 1 426 ? 2.780 10.068 40.952 1.00 44.93 ? 426 HIS A CA 1 ATOM 3412 C C . HIS A 1 426 ? 3.016 11.463 40.393 1.00 44.44 ? 426 HIS A C 1 ATOM 3413 O O . HIS A 1 426 ? 2.847 11.678 39.196 1.00 44.40 ? 426 HIS A O 1 ATOM 3414 C CB . HIS A 1 426 ? 4.065 9.430 41.463 1.00 45.31 ? 426 HIS A CB 1 ATOM 3415 C CG . HIS A 1 426 ? 3.884 8.001 41.859 1.00 46.53 ? 426 HIS A CG 1 ATOM 3416 N ND1 . HIS A 1 426 ? 3.582 7.008 40.950 1.00 47.45 ? 426 HIS A ND1 1 ATOM 3417 C CD2 . HIS A 1 426 ? 3.916 7.403 43.071 1.00 47.35 ? 426 HIS A CD2 1 ATOM 3418 C CE1 . HIS A 1 426 ? 3.460 5.855 41.582 1.00 47.49 ? 426 HIS A CE1 1 ATOM 3419 N NE2 . HIS A 1 426 ? 3.658 6.066 42.870 1.00 48.76 ? 426 HIS A NE2 1 ATOM 3420 N N . LYS A 1 427 ? 3.432 12.393 41.246 1.00 43.20 ? 427 LYS A N 1 ATOM 3421 C CA . LYS A 1 427 ? 3.370 13.800 40.896 1.00 42.16 ? 427 LYS A CA 1 ATOM 3422 C C . LYS A 1 427 ? 4.629 14.366 40.272 1.00 40.92 ? 427 LYS A C 1 ATOM 3423 O O . LYS A 1 427 ? 4.566 15.267 39.457 1.00 41.14 ? 427 LYS A O 1 ATOM 3424 C CB . LYS A 1 427 ? 3.021 14.604 42.149 1.00 43.11 ? 427 LYS A CB 1 ATOM 3425 C CG . LYS A 1 427 ? 1.560 14.519 42.591 1.00 45.10 ? 427 LYS A CG 1 ATOM 3426 C CD . LYS A 1 427 ? 1.446 14.400 44.126 1.00 48.47 ? 427 LYS A CD 1 ATOM 3427 C CE . LYS A 1 427 ? 0.272 15.226 44.707 1.00 50.24 ? 427 LYS A CE 1 ATOM 3428 N NZ . LYS A 1 427 ? -0.935 15.303 43.812 1.00 49.33 ? 427 LYS A NZ 1 ATOM 3429 N N . ILE A 1 428 ? 5.776 13.825 40.639 1.00 39.08 ? 428 ILE A N 1 ATOM 3430 C CA . ILE A 1 428 ? 7.032 14.431 40.256 1.00 37.11 ? 428 ILE A CA 1 ATOM 3431 C C . ILE A 1 428 ? 7.649 13.914 38.995 1.00 35.95 ? 428 ILE A C 1 ATOM 3432 O O . ILE A 1 428 ? 7.552 12.740 38.663 1.00 36.55 ? 428 ILE A O 1 ATOM 3433 C CB . ILE A 1 428 ? 8.063 14.204 41.357 1.00 37.21 ? 428 ILE A CB 1 ATOM 3434 C CG1 . ILE A 1 428 ? 8.046 12.735 41.813 1.00 37.22 ? 428 ILE A CG1 1 ATOM 3435 C CG2 . ILE A 1 428 ? 7.808 15.103 42.505 1.00 38.09 ? 428 ILE A CG2 1 ATOM 3436 C CD1 . ILE A 1 428 ? 9.321 12.299 42.503 1.00 38.09 ? 428 ILE A CD1 1 ATOM 3437 N N . HIS A 1 429 ? 8.305 14.814 38.294 1.00 34.19 ? 429 HIS A N 1 ATOM 3438 C CA . HIS A 1 429 ? 9.242 14.383 37.278 1.00 33.07 ? 429 HIS A CA 1 ATOM 3439 C C . HIS A 1 429 ? 10.506 14.008 38.053 1.00 32.09 ? 429 HIS A C 1 ATOM 3440 O O . HIS A 1 429 ? 11.315 14.887 38.381 1.00 32.95 ? 429 HIS A O 1 ATOM 3441 C CB . HIS A 1 429 ? 9.525 15.485 36.271 1.00 32.73 ? 429 HIS A CB 1 ATOM 3442 C CG . HIS A 1 429 ? 8.334 15.852 35.454 1.00 33.55 ? 429 HIS A CG 1 ATOM 3443 N ND1 . HIS A 1 429 ? 7.301 16.607 35.962 1.00 34.87 ? 429 HIS A ND1 1 ATOM 3444 C CD2 . HIS A 1 429 ? 7.989 15.546 34.181 1.00 33.31 ? 429 HIS A CD2 1 ATOM 3445 C CE1 . HIS A 1 429 ? 6.376 16.761 35.032 1.00 33.47 ? 429 HIS A CE1 1 ATOM 3446 N NE2 . HIS A 1 429 ? 6.771 16.128 33.941 1.00 32.37 ? 429 HIS A NE2 1 ATOM 3447 N N . GLY A 1 430 ? 10.678 12.723 38.383 1.00 29.73 ? 430 GLY A N 1 ATOM 3448 C CA . GLY A 1 430 ? 11.826 12.362 39.183 1.00 27.78 ? 430 GLY A CA 1 ATOM 3449 C C . GLY A 1 430 ? 12.070 10.895 39.323 1.00 26.60 ? 430 GLY A C 1 ATOM 3450 O O . GLY A 1 430 ? 12.563 10.421 40.330 1.00 27.41 ? 430 GLY A O 1 ATOM 3451 N N . PHE A 1 431 ? 11.709 10.161 38.297 1.00 25.43 ? 431 PHE A N 1 ATOM 3452 C CA . PHE A 1 431 ? 11.857 8.725 38.312 1.00 23.98 ? 431 PHE A CA 1 ATOM 3453 C C . PHE A 1 431 ? 13.004 8.345 37.384 1.00 23.03 ? 431 PHE A C 1 ATOM 3454 O O . PHE A 1 431 ? 13.375 9.081 36.474 1.00 23.46 ? 431 PHE A O 1 ATOM 3455 C CB . PHE A 1 431 ? 10.579 8.089 37.820 1.00 23.92 ? 431 PHE A CB 1 ATOM 3456 C CG . PHE A 1 431 ? 9.511 8.009 38.848 1.00 25.71 ? 431 PHE A CG 1 ATOM 3457 C CD1 . PHE A 1 431 ? 8.521 8.977 38.915 1.00 26.96 ? 431 PHE A CD1 1 ATOM 3458 C CD2 . PHE A 1 431 ? 9.460 6.927 39.720 1.00 25.89 ? 431 PHE A CD2 1 ATOM 3459 C CE1 . PHE A 1 431 ? 7.524 8.898 39.852 1.00 28.08 ? 431 PHE A CE1 1 ATOM 3460 C CE2 . PHE A 1 431 ? 8.469 6.817 40.651 1.00 25.05 ? 431 PHE A CE2 1 ATOM 3461 C CZ . PHE A 1 431 ? 7.495 7.806 40.733 1.00 28.67 ? 431 PHE A CZ 1 ATOM 3462 N N . ASP A 1 432 ? 13.588 7.204 37.648 1.00 21.77 ? 432 ASP A N 1 ATOM 3463 C CA . ASP A 1 432 ? 14.680 6.658 36.853 1.00 20.52 ? 432 ASP A CA 1 ATOM 3464 C C . ASP A 1 432 ? 14.299 5.382 36.052 1.00 20.38 ? 432 ASP A C 1 ATOM 3465 O O . ASP A 1 432 ? 14.235 4.255 36.585 1.00 20.57 ? 432 ASP A O 1 ATOM 3466 C CB . ASP A 1 432 ? 15.848 6.337 37.777 1.00 20.15 ? 432 ASP A CB 1 ATOM 3467 C CG . ASP A 1 432 ? 17.042 5.811 37.042 1.00 19.02 ? 432 ASP A CG 1 ATOM 3468 O OD1 . ASP A 1 432 ? 16.913 5.454 35.861 1.00 17.88 ? 432 ASP A OD1 1 ATOM 3469 O OD2 . ASP A 1 432 ? 18.159 5.716 37.568 1.00 21.41 ? 432 ASP A OD2 1 ATOM 3470 N N . LEU A 1 433 ? 14.070 5.579 34.758 1.00 19.86 ? 433 LEU A N 1 ATOM 3471 C CA . LEU A 1 433 ? 13.765 4.484 33.851 1.00 19.22 ? 433 LEU A CA 1 ATOM 3472 C C . LEU A 1 433 ? 14.793 3.349 33.916 1.00 18.48 ? 433 LEU A C 1 ATOM 3473 O O . LEU A 1 433 ? 14.413 2.185 33.798 1.00 18.83 ? 433 LEU A O 1 ATOM 3474 C CB . LEU A 1 433 ? 13.558 4.990 32.406 1.00 19.35 ? 433 LEU A CB 1 ATOM 3475 C CG . LEU A 1 433 ? 13.114 3.968 31.334 1.00 20.14 ? 433 LEU A CG 1 ATOM 3476 C CD1 . LEU A 1 433 ? 11.984 3.033 31.788 1.00 22.16 ? 433 LEU A CD1 1 ATOM 3477 C CD2 . LEU A 1 433 ? 12.729 4.643 30.055 1.00 18.47 ? 433 LEU A CD2 1 ATOM 3478 N N . ALA A 1 434 ? 16.064 3.697 34.121 1.00 17.60 ? 434 ALA A N 1 ATOM 3479 C CA . ALA A 1 434 ? 17.169 2.744 34.153 1.00 16.86 ? 434 ALA A CA 1 ATOM 3480 C C . ALA A 1 434 ? 17.009 1.795 35.341 1.00 17.16 ? 434 ALA A C 1 ATOM 3481 O O . ALA A 1 434 ? 16.810 0.584 35.151 1.00 17.11 ? 434 ALA A O 1 ATOM 3482 C CB . ALA A 1 434 ? 18.489 3.485 34.191 1.00 16.03 ? 434 ALA A CB 1 ATOM 3483 N N . ALA A 1 435 ? 17.086 2.355 36.557 1.00 17.10 ? 435 ALA A N 1 ATOM 3484 C CA . ALA A 1 435 ? 16.732 1.653 37.811 1.00 16.59 ? 435 ALA A CA 1 ATOM 3485 C C . ALA A 1 435 ? 15.417 0.849 37.730 1.00 16.37 ? 435 ALA A C 1 ATOM 3486 O O . ALA A 1 435 ? 15.364 -0.322 38.167 1.00 14.84 ? 435 ALA A O 1 ATOM 3487 C CB . ALA A 1 435 ? 16.651 2.631 38.972 1.00 16.70 ? 435 ALA A CB 1 ATOM 3488 N N . ILE A 1 436 ? 14.353 1.494 37.229 1.00 16.19 ? 436 ILE A N 1 ATOM 3489 C CA . ILE A 1 436 ? 13.077 0.789 37.005 1.00 16.56 ? 436 ILE A CA 1 ATOM 3490 C C . ILE A 1 436 ? 13.301 -0.474 36.150 1.00 17.04 ? 436 ILE A C 1 ATOM 3491 O O . ILE A 1 436 ? 12.976 -1.618 36.571 1.00 17.62 ? 436 ILE A O 1 ATOM 3492 C CB . ILE A 1 436 ? 12.035 1.672 36.329 1.00 16.56 ? 436 ILE A CB 1 ATOM 3493 C CG1 . ILE A 1 436 ? 11.395 2.598 37.341 1.00 16.02 ? 436 ILE A CG1 1 ATOM 3494 C CG2 . ILE A 1 436 ? 10.908 0.843 35.813 1.00 17.28 ? 436 ILE A CG2 1 ATOM 3495 C CD1 . ILE A 1 436 ? 10.867 3.897 36.701 1.00 16.42 ? 436 ILE A CD1 1 ATOM 3496 N N . ASN A 1 437 ? 13.790 -0.283 34.947 1.00 16.73 ? 437 ASN A N 1 ATOM 3497 C CA . ASN A 1 437 ? 14.061 -1.414 34.103 1.00 16.10 ? 437 ASN A CA 1 ATOM 3498 C C . ASN A 1 437 ? 14.875 -2.438 34.913 1.00 15.80 ? 437 ASN A C 1 ATOM 3499 O O . ASN A 1 437 ? 14.578 -3.645 34.821 1.00 16.48 ? 437 ASN A O 1 ATOM 3500 C CB . ASN A 1 437 ? 14.847 -0.993 32.855 1.00 16.02 ? 437 ASN A CB 1 ATOM 3501 C CG . ASN A 1 437 ? 14.067 -0.354 31.674 1.00 18.90 ? 437 ASN A CG 1 ATOM 3502 O OD1 . ASN A 1 437 ? 14.606 -0.224 30.580 1.00 22.88 ? 437 ASN A OD1 1 ATOM 3503 N ND2 . ASN A 1 437 ? 12.835 0.032 31.932 1.00 17.63 ? 437 ASN A ND2 1 ATOM 3504 N N . LEU A 1 438 ? 15.904 -2.024 35.724 1.00 15.24 ? 438 LEU A N 1 ATOM 3505 C CA . LEU A 1 438 ? 16.619 -3.020 36.510 1.00 15.26 ? 438 LEU A CA 1 ATOM 3506 C C . LEU A 1 438 ? 15.749 -3.694 37.585 1.00 15.48 ? 438 LEU A C 1 ATOM 3507 O O . LEU A 1 438 ? 15.794 -4.904 37.783 1.00 15.32 ? 438 LEU A O 1 ATOM 3508 C CB . LEU A 1 438 ? 17.917 -2.491 37.112 1.00 14.85 ? 438 LEU A CB 1 ATOM 3509 C CG . LEU A 1 438 ? 19.040 -2.234 36.113 1.00 15.36 ? 438 LEU A CG 1 ATOM 3510 C CD1 . LEU A 1 438 ? 20.159 -1.571 36.877 1.00 14.89 ? 438 LEU A CD1 1 ATOM 3511 C CD2 . LEU A 1 438 ? 19.527 -3.467 35.372 1.00 15.58 ? 438 LEU A CD2 1 ATOM 3512 N N . GLN A 1 439 ? 14.951 -2.909 38.277 1.00 16.02 ? 439 GLN A N 1 ATOM 3513 C CA . GLN A 1 439 ? 14.142 -3.469 39.328 1.00 16.49 ? 439 GLN A CA 1 ATOM 3514 C C . GLN A 1 439 ? 13.175 -4.466 38.704 1.00 16.69 ? 439 GLN A C 1 ATOM 3515 O O . GLN A 1 439 ? 12.762 -5.446 39.335 1.00 16.57 ? 439 GLN A O 1 ATOM 3516 C CB . GLN A 1 439 ? 13.379 -2.349 40.022 1.00 16.30 ? 439 GLN A CB 1 ATOM 3517 C CG . GLN A 1 439 ? 12.689 -2.796 41.261 1.00 16.46 ? 439 GLN A CG 1 ATOM 3518 C CD . GLN A 1 439 ? 13.607 -2.868 42.470 1.00 17.98 ? 439 GLN A CD 1 ATOM 3519 O OE1 . GLN A 1 439 ? 14.822 -3.040 42.339 1.00 19.15 ? 439 GLN A OE1 1 ATOM 3520 N NE2 . GLN A 1 439 ? 13.016 -2.757 43.661 1.00 17.43 ? 439 GLN A NE2 1 ATOM 3521 N N . ARG A 1 440 ? 12.826 -4.189 37.455 1.00 16.53 ? 440 ARG A N 1 ATOM 3522 C CA . ARG A 1 440 ? 11.867 -4.994 36.739 1.00 16.79 ? 440 ARG A CA 1 ATOM 3523 C C . ARG A 1 440 ? 12.416 -6.298 36.210 1.00 18.05 ? 440 ARG A C 1 ATOM 3524 O O . ARG A 1 440 ? 11.618 -7.166 35.973 1.00 19.41 ? 440 ARG A O 1 ATOM 3525 C CB . ARG A 1 440 ? 11.225 -4.251 35.585 1.00 16.20 ? 440 ARG A CB 1 ATOM 3526 C CG . ARG A 1 440 ? 10.026 -4.936 35.000 1.00 15.84 ? 440 ARG A CG 1 ATOM 3527 C CD . ARG A 1 440 ? 8.755 -4.806 35.795 1.00 14.38 ? 440 ARG A CD 1 ATOM 3528 N NE . ARG A 1 440 ? 8.308 -3.427 35.893 1.00 13.83 ? 440 ARG A NE 1 ATOM 3529 C CZ . ARG A 1 440 ? 7.471 -3.003 36.821 1.00 12.99 ? 440 ARG A CZ 1 ATOM 3530 N NH1 . ARG A 1 440 ? 7.009 -3.882 37.722 1.00 9.51 ? 440 ARG A NH1 1 ATOM 3531 N NH2 . ARG A 1 440 ? 7.109 -1.727 36.854 1.00 8.81 ? 440 ARG A NH2 1 ATOM 3532 N N . CYS A 1 441 ? 13.728 -6.445 35.981 1.00 18.55 ? 441 CYS A N 1 ATOM 3533 C CA . CYS A 1 441 ? 14.309 -7.729 35.588 1.00 18.81 ? 441 CYS A CA 1 ATOM 3534 C C . CYS A 1 441 ? 14.128 -8.606 36.753 1.00 18.39 ? 441 CYS A C 1 ATOM 3535 O O . CYS A 1 441 ? 13.813 -9.761 36.623 1.00 18.27 ? 441 CYS A O 1 ATOM 3536 C CB . CYS A 1 441 ? 15.816 -7.672 35.430 1.00 19.44 ? 441 CYS A CB 1 ATOM 3537 S SG . CYS A 1 441 ? 16.335 -7.100 33.832 1.00 22.48 ? 441 CYS A SG 1 ATOM 3538 N N . ARG A 1 442 ? 14.372 -8.035 37.914 1.00 18.19 ? 442 ARG A N 1 ATOM 3539 C CA . ARG A 1 442 ? 14.339 -8.795 39.122 1.00 17.38 ? 442 ARG A CA 1 ATOM 3540 C C . ARG A 1 442 ? 12.916 -9.223 39.415 1.00 17.72 ? 442 ARG A C 1 ATOM 3541 O O . ARG A 1 442 ? 12.675 -10.373 39.781 1.00 18.04 ? 442 ARG A O 1 ATOM 3542 C CB . ARG A 1 442 ? 14.974 -7.968 40.215 1.00 17.15 ? 442 ARG A CB 1 ATOM 3543 C CG . ARG A 1 442 ? 16.500 -7.919 40.103 1.00 16.16 ? 442 ARG A CG 1 ATOM 3544 C CD . ARG A 1 442 ? 17.131 -6.777 40.826 1.00 15.56 ? 442 ARG A CD 1 ATOM 3545 N NE . ARG A 1 442 ? 18.477 -6.513 40.333 1.00 17.85 ? 442 ARG A NE 1 ATOM 3546 C CZ . ARG A 1 442 ? 19.303 -5.661 40.913 1.00 17.28 ? 442 ARG A CZ 1 ATOM 3547 N NH1 . ARG A 1 442 ? 18.906 -5.032 41.997 1.00 13.89 ? 442 ARG A NH1 1 ATOM 3548 N NH2 . ARG A 1 442 ? 20.526 -5.462 40.434 1.00 19.21 ? 442 ARG A NH2 1 ATOM 3549 N N . ASP A 1 443 ? 11.973 -8.311 39.182 1.00 17.57 ? 443 ASP A N 1 ATOM 3550 C CA . ASP A 1 443 ? 10.532 -8.551 39.381 1.00 16.99 ? 443 ASP A CA 1 ATOM 3551 C C . ASP A 1 443 ? 10.063 -9.747 38.511 1.00 16.54 ? 443 ASP A C 1 ATOM 3552 O O . ASP A 1 443 ? 9.297 -10.591 38.942 1.00 15.87 ? 443 ASP A O 1 ATOM 3553 C CB . ASP A 1 443 ? 9.760 -7.235 39.084 1.00 16.58 ? 443 ASP A CB 1 ATOM 3554 C CG . ASP A 1 443 ? 8.223 -7.384 39.132 1.00 18.76 ? 443 ASP A CG 1 ATOM 3555 O OD1 . ASP A 1 443 ? 7.710 -8.373 39.716 1.00 20.33 ? 443 ASP A OD1 1 ATOM 3556 O OD2 . ASP A 1 443 ? 7.433 -6.542 38.607 1.00 18.76 ? 443 ASP A OD2 1 ATOM 3557 N N . HIS A 1 444 ? 10.579 -9.827 37.291 1.00 16.02 ? 444 HIS A N 1 ATOM 3558 C CA . HIS A 1 444 ? 10.192 -10.862 36.346 1.00 15.01 ? 444 HIS A CA 1 ATOM 3559 C C . HIS A 1 444 ? 10.956 -12.198 36.442 1.00 15.05 ? 444 HIS A C 1 ATOM 3560 O O . HIS A 1 444 ? 10.843 -13.044 35.566 1.00 13.78 ? 444 HIS A O 1 ATOM 3561 C CB . HIS A 1 444 ? 10.359 -10.302 34.949 1.00 14.79 ? 444 HIS A CB 1 ATOM 3562 C CG . HIS A 1 444 ? 9.240 -9.403 34.531 1.00 15.81 ? 444 HIS A CG 1 ATOM 3563 N ND1 . HIS A 1 444 ? 8.423 -9.688 33.458 1.00 14.48 ? 444 HIS A ND1 1 ATOM 3564 C CD2 . HIS A 1 444 ? 8.783 -8.237 35.057 1.00 15.76 ? 444 HIS A CD2 1 ATOM 3565 C CE1 . HIS A 1 444 ? 7.520 -8.729 33.335 1.00 15.00 ? 444 HIS A CE1 1 ATOM 3566 N NE2 . HIS A 1 444 ? 7.712 -7.842 34.296 1.00 13.97 ? 444 HIS A NE2 1 ATOM 3567 N N . GLY A 1 445 ? 11.746 -12.350 37.492 1.00 16.09 ? 445 GLY A N 1 ATOM 3568 C CA . GLY A 1 445 ? 12.568 -13.527 37.654 1.00 17.39 ? 445 GLY A CA 1 ATOM 3569 C C . GLY A 1 445 ? 13.541 -13.870 36.545 1.00 17.93 ? 445 GLY A C 1 ATOM 3570 O O . GLY A 1 445 ? 13.802 -15.057 36.317 1.00 18.76 ? 445 GLY A O 1 ATOM 3571 N N . MET A 1 446 ? 14.093 -12.876 35.864 1.00 17.87 ? 446 MET A N 1 ATOM 3572 C CA . MET A 1 446 ? 15.045 -13.152 34.796 1.00 18.05 ? 446 MET A CA 1 ATOM 3573 C C . MET A 1 446 ? 16.300 -13.873 35.273 1.00 17.99 ? 446 MET A C 1 ATOM 3574 O O . MET A 1 446 ? 16.826 -13.569 36.347 1.00 18.87 ? 446 MET A O 1 ATOM 3575 C CB . MET A 1 446 ? 15.483 -11.823 34.162 1.00 18.36 ? 446 MET A CB 1 ATOM 3576 C CG . MET A 1 446 ? 14.410 -11.137 33.341 1.00 18.04 ? 446 MET A CG 1 ATOM 3577 S SD . MET A 1 446 ? 14.077 -12.152 31.897 1.00 21.59 ? 446 MET A SD 1 ATOM 3578 C CE . MET A 1 446 ? 12.520 -13.056 32.246 1.00 21.87 ? 446 MET A CE 1 ATOM 3579 N N . PRO A 1 447 ? 16.752 -14.855 34.506 1.00 16.85 ? 447 PRO A N 1 ATOM 3580 C CA . PRO A 1 447 ? 18.085 -15.414 34.664 1.00 15.92 ? 447 PRO A CA 1 ATOM 3581 C C . PRO A 1 447 ? 19.090 -14.303 34.460 1.00 16.10 ? 447 PRO A C 1 ATOM 3582 O O . PRO A 1 447 ? 18.804 -13.349 33.756 1.00 16.68 ? 447 PRO A O 1 ATOM 3583 C CB . PRO A 1 447 ? 18.195 -16.333 33.475 1.00 15.35 ? 447 PRO A CB 1 ATOM 3584 C CG . PRO A 1 447 ? 16.831 -16.771 33.260 1.00 16.12 ? 447 PRO A CG 1 ATOM 3585 C CD . PRO A 1 447 ? 15.960 -15.584 33.519 1.00 16.77 ? 447 PRO A CD 1 ATOM 3586 N N . GLY A 1 448 ? 20.266 -14.439 35.048 1.00 15.88 ? 448 GLY A N 1 ATOM 3587 C CA . GLY A 1 448 ? 21.315 -13.471 34.883 1.00 15.10 ? 448 GLY A CA 1 ATOM 3588 C C . GLY A 1 448 ? 21.935 -13.569 33.519 1.00 15.23 ? 448 GLY A C 1 ATOM 3589 O O . GLY A 1 448 ? 21.511 -14.354 32.687 1.00 14.77 ? 448 GLY A O 1 ATOM 3590 N N . TYR A 1 449 ? 22.995 -12.793 33.328 1.00 15.47 ? 449 TYR A N 1 ATOM 3591 C CA . TYR A 1 449 ? 23.584 -12.569 32.014 1.00 15.63 ? 449 TYR A CA 1 ATOM 3592 C C . TYR A 1 449 ? 24.289 -13.798 31.402 1.00 15.64 ? 449 TYR A C 1 ATOM 3593 O O . TYR A 1 449 ? 24.158 -14.057 30.196 1.00 15.44 ? 449 TYR A O 1 ATOM 3594 C CB . TYR A 1 449 ? 24.470 -11.303 32.105 1.00 15.68 ? 449 TYR A CB 1 ATOM 3595 C CG . TYR A 1 449 ? 25.400 -11.004 30.939 1.00 17.02 ? 449 TYR A CG 1 ATOM 3596 C CD1 . TYR A 1 449 ? 24.975 -10.233 29.869 1.00 16.42 ? 449 TYR A CD1 1 ATOM 3597 C CD2 . TYR A 1 449 ? 26.722 -11.454 30.934 1.00 15.92 ? 449 TYR A CD2 1 ATOM 3598 C CE1 . TYR A 1 449 ? 25.820 -9.962 28.809 1.00 18.04 ? 449 TYR A CE1 1 ATOM 3599 C CE2 . TYR A 1 449 ? 27.570 -11.166 29.872 1.00 16.42 ? 449 TYR A CE2 1 ATOM 3600 C CZ . TYR A 1 449 ? 27.104 -10.420 28.817 1.00 17.65 ? 449 TYR A CZ 1 ATOM 3601 O OH . TYR A 1 449 ? 27.916 -10.124 27.754 1.00 19.08 ? 449 TYR A OH 1 ATOM 3602 N N . ASN A 1 450 ? 25.011 -14.567 32.212 1.00 15.40 ? 450 ASN A N 1 ATOM 3603 C CA . ASN A 1 450 ? 25.695 -15.737 31.661 1.00 15.51 ? 450 ASN A CA 1 ATOM 3604 C C . ASN A 1 450 ? 24.745 -16.828 31.232 1.00 15.99 ? 450 ASN A C 1 ATOM 3605 O O . ASN A 1 450 ? 25.052 -17.589 30.309 1.00 16.66 ? 450 ASN A O 1 ATOM 3606 C CB . ASN A 1 450 ? 26.809 -16.270 32.558 1.00 14.83 ? 450 ASN A CB 1 ATOM 3607 C CG . ASN A 1 450 ? 28.132 -15.522 32.354 1.00 13.66 ? 450 ASN A CG 1 ATOM 3608 O OD1 . ASN A 1 450 ? 28.363 -14.911 31.295 1.00 10.93 ? 450 ASN A OD1 1 ATOM 3609 N ND2 . ASN A 1 450 ? 29.004 -15.561 33.372 1.00 10.96 ? 450 ASN A ND2 1 ATOM 3610 N N . SER A 1 451 ? 23.577 -16.894 31.858 1.00 16.31 ? 451 SER A N 1 ATOM 3611 C CA . SER A 1 451 ? 22.575 -17.871 31.426 1.00 16.44 ? 451 SER A CA 1 ATOM 3612 C C . SER A 1 451 ? 22.150 -17.539 30.019 1.00 16.97 ? 451 SER A C 1 ATOM 3613 O O . SER A 1 451 ? 21.878 -18.432 29.226 1.00 18.07 ? 451 SER A O 1 ATOM 3614 C CB . SER A 1 451 ? 21.330 -17.860 32.319 1.00 16.66 ? 451 SER A CB 1 ATOM 3615 O OG . SER A 1 451 ? 21.570 -18.411 33.602 1.00 15.15 ? 451 SER A OG 1 ATOM 3616 N N . TRP A 1 452 ? 22.075 -16.253 29.702 1.00 17.32 ? 452 TRP A N 1 ATOM 3617 C CA . TRP A 1 452 ? 21.626 -15.828 28.373 1.00 17.83 ? 452 TRP A CA 1 ATOM 3618 C C . TRP A 1 452 ? 22.730 -15.936 27.328 1.00 18.26 ? 452 TRP A C 1 ATOM 3619 O O . TRP A 1 452 ? 22.455 -16.244 26.160 1.00 19.82 ? 452 TRP A O 1 ATOM 3620 C CB . TRP A 1 452 ? 20.981 -14.440 28.409 1.00 18.19 ? 452 TRP A CB 1 ATOM 3621 C CG . TRP A 1 452 ? 19.658 -14.480 29.160 1.00 18.42 ? 452 TRP A CG 1 ATOM 3622 C CD1 . TRP A 1 452 ? 19.365 -13.916 30.366 1.00 15.64 ? 452 TRP A CD1 1 ATOM 3623 C CD2 . TRP A 1 452 ? 18.485 -15.193 28.753 1.00 19.28 ? 452 TRP A CD2 1 ATOM 3624 N NE1 . TRP A 1 452 ? 18.072 -14.214 30.717 1.00 15.86 ? 452 TRP A NE1 1 ATOM 3625 C CE2 . TRP A 1 452 ? 17.509 -14.992 29.741 1.00 16.78 ? 452 TRP A CE2 1 ATOM 3626 C CE3 . TRP A 1 452 ? 18.156 -15.968 27.623 1.00 19.48 ? 452 TRP A CE3 1 ATOM 3627 C CZ2 . TRP A 1 452 ? 16.247 -15.547 29.660 1.00 18.36 ? 452 TRP A CZ2 1 ATOM 3628 C CZ3 . TRP A 1 452 ? 16.900 -16.519 27.537 1.00 20.19 ? 452 TRP A CZ3 1 ATOM 3629 C CH2 . TRP A 1 452 ? 15.960 -16.321 28.560 1.00 21.19 ? 452 TRP A CH2 1 ATOM 3630 N N . ARG A 1 453 ? 23.982 -15.722 27.719 1.00 16.89 ? 453 ARG A N 1 ATOM 3631 C CA . ARG A 1 453 ? 25.044 -15.937 26.757 1.00 16.14 ? 453 ARG A CA 1 ATOM 3632 C C . ARG A 1 453 ? 25.058 -17.423 26.394 1.00 15.93 ? 453 ARG A C 1 ATOM 3633 O O . ARG A 1 453 ? 25.289 -17.791 25.253 1.00 15.06 ? 453 ARG A O 1 ATOM 3634 C CB . ARG A 1 453 ? 26.376 -15.584 27.380 1.00 16.28 ? 453 ARG A CB 1 ATOM 3635 C CG . ARG A 1 453 ? 26.494 -14.162 27.772 1.00 16.90 ? 453 ARG A CG 1 ATOM 3636 C CD . ARG A 1 453 ? 27.000 -13.315 26.636 1.00 17.66 ? 453 ARG A CD 1 ATOM 3637 N NE . ARG A 1 453 ? 28.293 -13.784 26.133 1.00 15.44 ? 453 ARG A NE 1 ATOM 3638 C CZ . ARG A 1 453 ? 28.949 -13.212 25.132 1.00 14.57 ? 453 ARG A CZ 1 ATOM 3639 N NH1 . ARG A 1 453 ? 28.447 -12.133 24.507 1.00 8.79 ? 453 ARG A NH1 1 ATOM 3640 N NH2 . ARG A 1 453 ? 30.110 -13.731 24.764 1.00 12.93 ? 453 ARG A NH2 1 ATOM 3641 N N . GLY A 1 454 ? 24.855 -18.267 27.411 1.00 15.84 ? 454 GLY A N 1 ATOM 3642 C CA . GLY A 1 454 ? 24.799 -19.700 27.236 1.00 15.87 ? 454 GLY A CA 1 ATOM 3643 C C . GLY A 1 454 ? 23.690 -20.099 26.282 1.00 15.70 ? 454 GLY A C 1 ATOM 3644 O O . GLY A 1 454 ? 23.884 -20.848 25.349 1.00 14.33 ? 454 GLY A O 1 ATOM 3645 N N . PHE A 1 455 ? 22.507 -19.575 26.545 1.00 16.50 ? 455 PHE A N 1 ATOM 3646 C CA . PHE A 1 455 ? 21.343 -19.808 25.695 1.00 17.05 ? 455 PHE A CA 1 ATOM 3647 C C . PHE A 1 455 ? 21.597 -19.451 24.246 1.00 17.42 ? 455 PHE A C 1 ATOM 3648 O O . PHE A 1 455 ? 21.158 -20.135 23.355 1.00 18.53 ? 455 PHE A O 1 ATOM 3649 C CB . PHE A 1 455 ? 20.186 -18.968 26.219 1.00 16.89 ? 455 PHE A CB 1 ATOM 3650 C CG . PHE A 1 455 ? 18.922 -19.072 25.413 1.00 13.79 ? 455 PHE A CG 1 ATOM 3651 C CD1 . PHE A 1 455 ? 18.053 -20.125 25.605 1.00 11.64 ? 455 PHE A CD1 1 ATOM 3652 C CD2 . PHE A 1 455 ? 18.569 -18.064 24.534 1.00 7.82 ? 455 PHE A CD2 1 ATOM 3653 C CE1 . PHE A 1 455 ? 16.851 -20.199 24.894 1.00 12.17 ? 455 PHE A CE1 1 ATOM 3654 C CE2 . PHE A 1 455 ? 17.391 -18.137 23.834 1.00 9.26 ? 455 PHE A CE2 1 ATOM 3655 C CZ . PHE A 1 455 ? 16.533 -19.199 24.001 1.00 11.27 ? 455 PHE A CZ 1 ATOM 3656 N N . CYS A 1 456 ? 22.295 -18.369 24.006 1.00 17.91 ? 456 CYS A N 1 ATOM 3657 C CA . CYS A 1 456 ? 22.542 -17.956 22.643 1.00 18.20 ? 456 CYS A CA 1 ATOM 3658 C C . CYS A 1 456 ? 23.844 -18.536 22.168 1.00 18.46 ? 456 CYS A C 1 ATOM 3659 O O . CYS A 1 456 ? 24.432 -18.061 21.208 1.00 18.57 ? 456 CYS A O 1 ATOM 3660 C CB . CYS A 1 456 ? 22.581 -16.437 22.590 1.00 18.27 ? 456 CYS A CB 1 ATOM 3661 S SG . CYS A 1 456 ? 20.920 -15.743 22.668 1.00 18.93 ? 456 CYS A SG 1 ATOM 3662 N N . GLY A 1 457 ? 24.315 -19.562 22.862 1.00 18.77 ? 457 GLY A N 1 ATOM 3663 C CA . GLY A 1 457 ? 25.543 -20.219 22.463 1.00 18.99 ? 457 GLY A CA 1 ATOM 3664 C C . GLY A 1 457 ? 26.768 -19.318 22.419 1.00 19.51 ? 457 GLY A C 1 ATOM 3665 O O . GLY A 1 457 ? 27.618 -19.525 21.583 1.00 20.18 ? 457 GLY A O 1 ATOM 3666 N N . LEU A 1 458 ? 26.879 -18.343 23.322 1.00 19.60 ? 458 LEU A N 1 ATOM 3667 C CA . LEU A 1 458 ? 28.026 -17.444 23.353 1.00 19.75 ? 458 LEU A CA 1 ATOM 3668 C C . LEU A 1 458 ? 28.793 -17.678 24.611 1.00 19.71 ? 458 LEU A C 1 ATOM 3669 O O . LEU A 1 458 ? 28.218 -18.039 25.607 1.00 20.46 ? 458 LEU A O 1 ATOM 3670 C CB . LEU A 1 458 ? 27.584 -15.980 23.388 1.00 20.17 ? 458 LEU A CB 1 ATOM 3671 C CG . LEU A 1 458 ? 26.792 -15.489 22.186 1.00 22.53 ? 458 LEU A CG 1 ATOM 3672 C CD1 . LEU A 1 458 ? 26.029 -14.208 22.507 1.00 24.92 ? 458 LEU A CD1 1 ATOM 3673 C CD2 . LEU A 1 458 ? 27.682 -15.330 20.955 1.00 22.54 ? 458 LEU A CD2 1 ATOM 3674 N N . SER A 1 459 ? 30.081 -17.409 24.573 1.00 19.44 ? 459 SER A N 1 ATOM 3675 C CA . SER A 1 459 ? 30.941 -17.561 25.723 1.00 20.82 ? 459 SER A CA 1 ATOM 3676 C C . SER A 1 459 ? 30.422 -16.888 27.007 1.00 21.35 ? 459 SER A C 1 ATOM 3677 O O . SER A 1 459 ? 29.769 -15.841 26.949 1.00 22.05 ? 459 SER A O 1 ATOM 3678 C CB . SER A 1 459 ? 32.263 -16.914 25.385 1.00 20.75 ? 459 SER A CB 1 ATOM 3679 O OG . SER A 1 459 ? 32.043 -15.516 25.374 1.00 23.15 ? 459 SER A OG 1 ATOM 3680 N N . GLN A 1 460 ? 30.791 -17.453 28.157 1.00 21.41 ? 460 GLN A N 1 ATOM 3681 C CA . GLN A 1 460 ? 30.358 -16.982 29.453 1.00 21.67 ? 460 GLN A CA 1 ATOM 3682 C C . GLN A 1 460 ? 31.535 -16.618 30.319 1.00 21.81 ? 460 GLN A C 1 ATOM 3683 O O . GLN A 1 460 ? 32.077 -17.456 30.998 1.00 22.41 ? 460 GLN A O 1 ATOM 3684 C CB . GLN A 1 460 ? 29.551 -18.083 30.151 1.00 21.80 ? 460 GLN A CB 1 ATOM 3685 C CG . GLN A 1 460 ? 28.290 -18.538 29.350 1.00 24.00 ? 460 GLN A CG 1 ATOM 3686 C CD . GLN A 1 460 ? 27.745 -19.930 29.730 1.00 24.07 ? 460 GLN A CD 1 ATOM 3687 O OE1 . GLN A 1 460 ? 26.802 -20.066 30.529 1.00 23.10 ? 460 GLN A OE1 1 ATOM 3688 N NE2 . GLN A 1 460 ? 28.333 -20.957 29.141 1.00 26.39 ? 460 GLN A NE2 1 ATOM 3689 N N . PRO A 1 461 ? 31.892 -15.350 30.350 1.00 22.49 ? 461 PRO A N 1 ATOM 3690 C CA . PRO A 1 461 ? 33.043 -14.887 31.128 1.00 23.30 ? 461 PRO A CA 1 ATOM 3691 C C . PRO A 1 461 ? 32.833 -15.080 32.618 1.00 24.48 ? 461 PRO A C 1 ATOM 3692 O O . PRO A 1 461 ? 31.743 -14.902 33.145 1.00 24.41 ? 461 PRO A O 1 ATOM 3693 C CB . PRO A 1 461 ? 33.087 -13.393 30.812 1.00 23.07 ? 461 PRO A CB 1 ATOM 3694 C CG . PRO A 1 461 ? 31.672 -13.068 30.485 1.00 22.31 ? 461 PRO A CG 1 ATOM 3695 C CD . PRO A 1 461 ? 31.203 -14.234 29.678 1.00 22.40 ? 461 PRO A CD 1 ATOM 3696 N N . LYS A 1 462 ? 33.896 -15.436 33.310 1.00 26.11 ? 462 LYS A N 1 ATOM 3697 C CA . LYS A 1 462 ? 33.773 -15.697 34.734 1.00 27.83 ? 462 LYS A CA 1 ATOM 3698 C C . LYS A 1 462 ? 34.739 -14.819 35.486 1.00 28.45 ? 462 LYS A C 1 ATOM 3699 O O . LYS A 1 462 ? 34.794 -14.909 36.707 1.00 28.91 ? 462 LYS A O 1 ATOM 3700 C CB . LYS A 1 462 ? 34.041 -17.174 35.070 1.00 27.57 ? 462 LYS A CB 1 ATOM 3701 C CG . LYS A 1 462 ? 33.158 -18.174 34.319 1.00 30.08 ? 462 LYS A CG 1 ATOM 3702 C CD . LYS A 1 462 ? 31.720 -18.214 34.852 1.00 34.81 ? 462 LYS A CD 1 ATOM 3703 C CE . LYS A 1 462 ? 30.956 -19.467 34.366 1.00 38.94 ? 462 LYS A CE 1 ATOM 3704 N NZ . LYS A 1 462 ? 29.440 -19.435 34.549 1.00 41.26 ? 462 LYS A NZ 1 ATOM 3705 N N . THR A 1 463 ? 35.478 -13.961 34.766 1.00 28.54 ? 463 THR A N 1 ATOM 3706 C CA . THR A 1 463 ? 36.490 -13.112 35.402 1.00 28.21 ? 463 THR A CA 1 ATOM 3707 C C . THR A 1 463 ? 36.490 -11.757 34.798 1.00 28.22 ? 463 THR A C 1 ATOM 3708 O O . THR A 1 463 ? 36.030 -11.581 33.687 1.00 27.56 ? 463 THR A O 1 ATOM 3709 C CB . THR A 1 463 ? 37.869 -13.683 35.108 1.00 28.58 ? 463 THR A CB 1 ATOM 3710 O OG1 . THR A 1 463 ? 37.982 -13.850 33.686 1.00 28.44 ? 463 THR A OG1 1 ATOM 3711 C CG2 . THR A 1 463 ? 38.034 -15.097 35.690 1.00 26.65 ? 463 THR A CG2 1 ATOM 3712 N N . LEU A 1 464 ? 37.052 -10.805 35.539 1.00 28.27 ? 464 LEU A N 1 ATOM 3713 C CA . LEU A 1 464 ? 37.230 -9.464 35.060 1.00 28.16 ? 464 LEU A CA 1 ATOM 3714 C C . LEU A 1 464 ? 37.857 -9.520 33.656 1.00 28.18 ? 464 LEU A C 1 ATOM 3715 O O . LEU A 1 464 ? 37.381 -8.878 32.727 1.00 29.28 ? 464 LEU A O 1 ATOM 3716 C CB . LEU A 1 464 ? 38.135 -8.688 36.020 1.00 27.87 ? 464 LEU A CB 1 ATOM 3717 C CG . LEU A 1 464 ? 37.951 -7.143 36.158 1.00 29.41 ? 464 LEU A CG 1 ATOM 3718 C CD1 . LEU A 1 464 ? 39.200 -6.399 36.693 1.00 27.84 ? 464 LEU A CD1 1 ATOM 3719 C CD2 . LEU A 1 464 ? 37.483 -6.458 34.870 1.00 31.60 ? 464 LEU A CD2 1 ATOM 3720 N N . LYS A 1 465 ? 38.923 -10.281 33.490 1.00 27.28 ? 465 LYS A N 1 ATOM 3721 C CA . LYS A 1 465 ? 39.587 -10.296 32.211 1.00 27.10 ? 465 LYS A CA 1 ATOM 3722 C C . LYS A 1 465 ? 38.627 -10.832 31.192 1.00 26.45 ? 465 LYS A C 1 ATOM 3723 O O . LYS A 1 465 ? 38.552 -10.325 30.073 1.00 26.76 ? 465 LYS A O 1 ATOM 3724 C CB . LYS A 1 465 ? 40.857 -11.170 32.254 1.00 27.71 ? 465 LYS A CB 1 ATOM 3725 C CG . LYS A 1 465 ? 42.201 -10.400 32.317 1.00 29.58 ? 465 LYS A CG 1 ATOM 3726 C CD . LYS A 1 465 ? 42.418 -9.560 31.057 1.00 32.65 ? 465 LYS A CD 1 ATOM 3727 C CE . LYS A 1 465 ? 43.882 -9.647 30.623 1.00 35.71 ? 465 LYS A CE 1 ATOM 3728 N NZ . LYS A 1 465 ? 44.831 -9.840 31.795 1.00 36.71 ? 465 LYS A NZ 1 ATOM 3729 N N . GLY A 1 466 ? 37.906 -11.883 31.564 1.00 25.67 ? 466 GLY A N 1 ATOM 3730 C CA . GLY A 1 466 ? 36.908 -12.438 30.676 1.00 24.43 ? 466 GLY A CA 1 ATOM 3731 C C . GLY A 1 466 ? 35.960 -11.333 30.221 1.00 23.95 ? 466 GLY A C 1 ATOM 3732 O O . GLY A 1 466 ? 35.723 -11.169 29.015 1.00 23.74 ? 466 GLY A O 1 ATOM 3733 N N . LEU A 1 467 ? 35.481 -10.528 31.179 1.00 23.18 ? 467 LEU A N 1 ATOM 3734 C CA . LEU A 1 467 ? 34.452 -9.540 30.924 1.00 22.37 ? 467 LEU A CA 1 ATOM 3735 C C . LEU A 1 467 ? 34.899 -8.398 30.032 1.00 23.18 ? 467 LEU A C 1 ATOM 3736 O O . LEU A 1 467 ? 34.122 -7.932 29.155 1.00 23.30 ? 467 LEU A O 1 ATOM 3737 C CB . LEU A 1 467 ? 33.875 -9.063 32.228 1.00 21.93 ? 467 LEU A CB 1 ATOM 3738 C CG . LEU A 1 467 ? 32.592 -8.227 32.197 1.00 21.86 ? 467 LEU A CG 1 ATOM 3739 C CD1 . LEU A 1 467 ? 31.372 -9.001 31.649 1.00 16.63 ? 467 LEU A CD1 1 ATOM 3740 C CD2 . LEU A 1 467 ? 32.356 -7.648 33.612 1.00 20.01 ? 467 LEU A CD2 1 ATOM 3741 N N . GLN A 1 468 ? 36.158 -7.983 30.211 1.00 23.54 ? 468 GLN A N 1 ATOM 3742 C CA . GLN A 1 468 ? 36.726 -6.898 29.417 1.00 24.06 ? 468 GLN A CA 1 ATOM 3743 C C . GLN A 1 468 ? 36.759 -7.307 27.965 1.00 23.70 ? 468 GLN A C 1 ATOM 3744 O O . GLN A 1 468 ? 36.550 -6.490 27.075 1.00 24.05 ? 468 GLN A O 1 ATOM 3745 C CB . GLN A 1 468 ? 38.152 -6.594 29.841 1.00 24.02 ? 468 GLN A CB 1 ATOM 3746 C CG . GLN A 1 468 ? 38.368 -6.651 31.334 1.00 28.23 ? 468 GLN A CG 1 ATOM 3747 C CD . GLN A 1 468 ? 39.692 -6.022 31.766 1.00 32.12 ? 468 GLN A CD 1 ATOM 3748 O OE1 . GLN A 1 468 ? 39.762 -5.395 32.823 1.00 33.16 ? 468 GLN A OE1 1 ATOM 3749 N NE2 . GLN A 1 468 ? 40.732 -6.181 30.948 1.00 31.31 ? 468 GLN A NE2 1 ATOM 3750 N N . THR A 1 469 ? 37.050 -8.576 27.734 1.00 23.13 ? 469 THR A N 1 ATOM 3751 C CA . THR A 1 469 ? 37.235 -9.062 26.382 1.00 22.77 ? 469 THR A CA 1 ATOM 3752 C C . THR A 1 469 ? 35.937 -9.092 25.640 1.00 23.27 ? 469 THR A C 1 ATOM 3753 O O . THR A 1 469 ? 35.859 -8.680 24.459 1.00 24.13 ? 469 THR A O 1 ATOM 3754 C CB . THR A 1 469 ? 37.821 -10.437 26.417 1.00 22.60 ? 469 THR A CB 1 ATOM 3755 O OG1 . THR A 1 469 ? 39.002 -10.404 27.231 1.00 22.20 ? 469 THR A OG1 1 ATOM 3756 C CG2 . THR A 1 469 ? 38.315 -10.787 25.056 1.00 21.77 ? 469 THR A CG2 1 ATOM 3757 N N . VAL A 1 470 ? 34.919 -9.611 26.319 1.00 22.37 ? 470 VAL A N 1 ATOM 3758 C CA . VAL A 1 470 ? 33.605 -9.575 25.766 1.00 21.47 ? 470 VAL A CA 1 ATOM 3759 C C . VAL A 1 470 ? 33.195 -8.117 25.595 1.00 21.25 ? 470 VAL A C 1 ATOM 3760 O O . VAL A 1 470 ? 33.069 -7.650 24.491 1.00 21.30 ? 470 VAL A O 1 ATOM 3761 C CB . VAL A 1 470 ? 32.656 -10.375 26.638 1.00 21.88 ? 470 VAL A CB 1 ATOM 3762 C CG1 . VAL A 1 470 ? 31.199 -10.054 26.322 1.00 22.00 ? 470 VAL A CG1 1 ATOM 3763 C CG2 . VAL A 1 470 ? 32.914 -11.835 26.420 1.00 22.09 ? 470 VAL A CG2 1 ATOM 3764 N N . LEU A 1 471 ? 33.078 -7.356 26.671 1.00 21.39 ? 471 LEU A N 1 ATOM 3765 C CA . LEU A 1 471 ? 32.618 -5.983 26.545 1.00 21.04 ? 471 LEU A CA 1 ATOM 3766 C C . LEU A 1 471 ? 33.533 -5.051 25.742 1.00 22.27 ? 471 LEU A C 1 ATOM 3767 O O . LEU A 1 471 ? 33.101 -3.997 25.237 1.00 22.89 ? 471 LEU A O 1 ATOM 3768 C CB . LEU A 1 471 ? 32.395 -5.437 27.921 1.00 20.40 ? 471 LEU A CB 1 ATOM 3769 C CG . LEU A 1 471 ? 30.993 -5.587 28.501 1.00 19.72 ? 471 LEU A CG 1 ATOM 3770 C CD1 . LEU A 1 471 ? 30.331 -6.859 28.134 1.00 17.21 ? 471 LEU A CD1 1 ATOM 3771 C CD2 . LEU A 1 471 ? 31.136 -5.472 30.012 1.00 18.06 ? 471 LEU A CD2 1 ATOM 3772 N N . LYS A 1 472 ? 34.790 -5.465 25.603 1.00 22.96 ? 472 LYS A N 1 ATOM 3773 C CA . LYS A 1 472 ? 35.822 -4.704 24.919 1.00 23.04 ? 472 LYS A CA 1 ATOM 3774 C C . LYS A 1 472 ? 36.059 -3.355 25.528 1.00 23.42 ? 472 LYS A C 1 ATOM 3775 O O . LYS A 1 472 ? 36.306 -2.388 24.823 1.00 22.97 ? 472 LYS A O 1 ATOM 3776 C CB . LYS A 1 472 ? 35.535 -4.614 23.451 1.00 23.37 ? 472 LYS A CB 1 ATOM 3777 C CG . LYS A 1 472 ? 36.062 -5.841 22.824 1.00 24.09 ? 472 LYS A CG 1 ATOM 3778 C CD . LYS A 1 472 ? 35.717 -5.936 21.399 1.00 26.31 ? 472 LYS A CD 1 ATOM 3779 C CE . LYS A 1 472 ? 36.735 -6.859 20.757 1.00 27.78 ? 472 LYS A CE 1 ATOM 3780 N NZ . LYS A 1 472 ? 36.066 -7.813 19.867 1.00 33.26 ? 472 LYS A NZ 1 ATOM 3781 N N . ASN A 1 473 ? 36.057 -3.340 26.861 1.00 23.94 ? 473 ASN A N 1 ATOM 3782 C CA . ASN A 1 473 ? 36.167 -2.135 27.656 1.00 24.05 ? 473 ASN A CA 1 ATOM 3783 C C . ASN A 1 473 ? 36.598 -2.448 29.124 1.00 24.98 ? 473 ASN A C 1 ATOM 3784 O O . ASN A 1 473 ? 35.841 -3.012 29.918 1.00 25.15 ? 473 ASN A O 1 ATOM 3785 C CB . ASN A 1 473 ? 34.815 -1.478 27.611 1.00 23.58 ? 473 ASN A CB 1 ATOM 3786 C CG . ASN A 1 473 ? 34.802 -0.147 28.234 1.00 23.47 ? 473 ASN A CG 1 ATOM 3787 O OD1 . ASN A 1 473 ? 35.473 0.091 29.241 1.00 23.68 ? 473 ASN A OD1 1 ATOM 3788 N ND2 . ASN A 1 473 ? 34.004 0.749 27.664 1.00 23.89 ? 473 ASN A ND2 1 ATOM 3789 N N . LYS A 1 474 ? 37.826 -2.092 29.479 1.00 25.56 ? 474 LYS A N 1 ATOM 3790 C CA . LYS A 1 474 ? 38.315 -2.300 30.826 1.00 26.53 ? 474 LYS A CA 1 ATOM 3791 C C . LYS A 1 474 ? 37.469 -1.527 31.838 1.00 27.17 ? 474 LYS A C 1 ATOM 3792 O O . LYS A 1 474 ? 36.917 -2.108 32.777 1.00 27.71 ? 474 LYS A O 1 ATOM 3793 C CB . LYS A 1 474 ? 39.770 -1.843 30.928 1.00 26.63 ? 474 LYS A CB 1 ATOM 3794 C CG . LYS A 1 474 ? 40.814 -2.947 30.777 1.00 28.49 ? 474 LYS A CG 1 ATOM 3795 C CD . LYS A 1 474 ? 42.157 -2.360 30.388 1.00 32.59 ? 474 LYS A CD 1 ATOM 3796 C CE . LYS A 1 474 ? 43.072 -3.405 29.691 1.00 36.34 ? 474 LYS A CE 1 ATOM 3797 N NZ . LYS A 1 474 ? 44.530 -3.012 29.595 1.00 36.92 ? 474 LYS A NZ 1 ATOM 3798 N N . ILE A 1 475 ? 37.359 -0.212 31.649 1.00 27.05 ? 475 ILE A N 1 ATOM 3799 C CA . ILE A 1 475 ? 36.635 0.597 32.622 1.00 26.23 ? 475 ILE A CA 1 ATOM 3800 C C . ILE A 1 475 ? 35.247 0.045 32.934 1.00 25.74 ? 475 ILE A C 1 ATOM 3801 O O . ILE A 1 475 ? 34.986 -0.342 34.071 1.00 26.12 ? 475 ILE A O 1 ATOM 3802 C CB . ILE A 1 475 ? 36.615 2.084 32.239 1.00 25.82 ? 475 ILE A CB 1 ATOM 3803 C CG1 . ILE A 1 475 ? 38.027 2.645 32.266 1.00 27.65 ? 475 ILE A CG1 1 ATOM 3804 C CG2 . ILE A 1 475 ? 35.855 2.844 33.235 1.00 23.99 ? 475 ILE A CG2 1 ATOM 3805 C CD1 . ILE A 1 475 ? 38.215 3.952 31.376 1.00 31.74 ? 475 ILE A CD1 1 ATOM 3806 N N . LEU A 1 476 ? 34.378 -0.038 31.931 1.00 25.10 ? 476 LEU A N 1 ATOM 3807 C CA . LEU A 1 476 ? 33.035 -0.583 32.129 1.00 24.26 ? 476 LEU A CA 1 ATOM 3808 C C . LEU A 1 476 ? 33.079 -1.967 32.802 1.00 23.69 ? 476 LEU A C 1 ATOM 3809 O O . LEU A 1 476 ? 32.394 -2.215 33.784 1.00 23.56 ? 476 LEU A O 1 ATOM 3810 C CB . LEU A 1 476 ? 32.287 -0.654 30.806 1.00 24.39 ? 476 LEU A CB 1 ATOM 3811 C CG . LEU A 1 476 ? 30.863 -1.228 30.901 1.00 24.61 ? 476 LEU A CG 1 ATOM 3812 C CD1 . LEU A 1 476 ? 30.008 -0.444 31.877 1.00 21.30 ? 476 LEU A CD1 1 ATOM 3813 C CD2 . LEU A 1 476 ? 30.190 -1.342 29.523 1.00 25.29 ? 476 LEU A CD2 1 ATOM 3814 N N . ALA A 1 477 ? 33.921 -2.855 32.321 1.00 23.25 ? 477 ALA A N 1 ATOM 3815 C CA . ALA A 1 477 ? 33.985 -4.168 32.951 1.00 23.62 ? 477 ALA A CA 1 ATOM 3816 C C . ALA A 1 477 ? 34.306 -4.152 34.450 1.00 24.28 ? 477 ALA A C 1 ATOM 3817 O O . ALA A 1 477 ? 33.837 -5.022 35.192 1.00 24.30 ? 477 ALA A O 1 ATOM 3818 C CB . ALA A 1 477 ? 34.927 -5.086 32.202 1.00 23.11 ? 477 ALA A CB 1 ATOM 3819 N N . LYS A 1 478 ? 35.053 -3.156 34.927 1.00 25.21 ? 478 LYS A N 1 ATOM 3820 C CA . LYS A 1 478 ? 35.392 -3.188 36.346 1.00 26.25 ? 478 LYS A CA 1 ATOM 3821 C C . LYS A 1 478 ? 34.300 -2.625 37.211 1.00 26.16 ? 478 LYS A C 1 ATOM 3822 O O . LYS A 1 478 ? 34.117 -3.067 38.341 1.00 26.92 ? 478 LYS A O 1 ATOM 3823 C CB . LYS A 1 478 ? 36.814 -2.710 36.697 1.00 26.72 ? 478 LYS A CB 1 ATOM 3824 C CG . LYS A 1 478 ? 37.075 -1.281 36.601 1.00 29.23 ? 478 LYS A CG 1 ATOM 3825 C CD . LYS A 1 478 ? 38.575 -1.019 36.497 1.00 34.81 ? 478 LYS A CD 1 ATOM 3826 C CE . LYS A 1 478 ? 39.167 -1.617 35.223 1.00 35.89 ? 478 LYS A CE 1 ATOM 3827 N NZ . LYS A 1 478 ? 40.644 -1.849 35.300 1.00 36.62 ? 478 LYS A NZ 1 ATOM 3828 N N . LYS A 1 479 ? 33.543 -1.686 36.648 1.00 26.26 ? 479 LYS A N 1 ATOM 3829 C CA . LYS A 1 479 ? 32.416 -1.085 37.355 1.00 26.62 ? 479 LYS A CA 1 ATOM 3830 C C . LYS A 1 479 ? 31.375 -2.178 37.577 1.00 26.47 ? 479 LYS A C 1 ATOM 3831 O O . LYS A 1 479 ? 30.800 -2.281 38.643 1.00 26.34 ? 479 LYS A O 1 ATOM 3832 C CB . LYS A 1 479 ? 31.807 0.064 36.555 1.00 26.59 ? 479 LYS A CB 1 ATOM 3833 C CG . LYS A 1 479 ? 32.766 1.151 36.271 1.00 27.58 ? 479 LYS A CG 1 ATOM 3834 C CD . LYS A 1 479 ? 32.018 2.353 35.709 1.00 30.11 ? 479 LYS A CD 1 ATOM 3835 C CE . LYS A 1 479 ? 32.814 3.624 35.877 1.00 32.58 ? 479 LYS A CE 1 ATOM 3836 N NZ . LYS A 1 479 ? 32.052 4.865 35.483 1.00 37.78 ? 479 LYS A NZ 1 ATOM 3837 N N . LEU A 1 480 ? 31.143 -2.981 36.553 1.00 26.53 ? 480 LEU A N 1 ATOM 3838 C CA . LEU A 1 480 ? 30.162 -4.025 36.644 1.00 26.78 ? 480 LEU A CA 1 ATOM 3839 C C . LEU A 1 480 ? 30.542 -5.062 37.714 1.00 26.80 ? 480 LEU A C 1 ATOM 3840 O O . LEU A 1 480 ? 29.668 -5.528 38.455 1.00 26.46 ? 480 LEU A O 1 ATOM 3841 C CB . LEU A 1 480 ? 30.044 -4.730 35.297 1.00 26.96 ? 480 LEU A CB 1 ATOM 3842 C CG . LEU A 1 480 ? 28.886 -4.335 34.394 1.00 27.40 ? 480 LEU A CG 1 ATOM 3843 C CD1 . LEU A 1 480 ? 28.439 -3.005 34.795 1.00 29.16 ? 480 LEU A CD1 1 ATOM 3844 C CD2 . LEU A 1 480 ? 29.298 -4.354 32.956 1.00 27.83 ? 480 LEU A CD2 1 ATOM 3845 N N . MET A 1 481 ? 31.845 -5.383 37.812 1.00 26.48 ? 481 MET A N 1 ATOM 3846 C CA . MET A 1 481 ? 32.343 -6.454 38.708 1.00 25.64 ? 481 MET A CA 1 ATOM 3847 C C . MET A 1 481 ? 32.339 -6.032 40.122 1.00 25.07 ? 481 MET A C 1 ATOM 3848 O O . MET A 1 481 ? 32.070 -6.859 41.016 1.00 24.38 ? 481 MET A O 1 ATOM 3849 C CB . MET A 1 481 ? 33.746 -6.919 38.321 1.00 25.64 ? 481 MET A CB 1 ATOM 3850 C CG . MET A 1 481 ? 33.775 -7.638 37.002 1.00 26.54 ? 481 MET A CG 1 ATOM 3851 S SD . MET A 1 481 ? 32.919 -9.247 37.103 1.00 28.09 ? 481 MET A SD 1 ATOM 3852 C CE . MET A 1 481 ? 33.984 -10.095 38.094 1.00 16.73 ? 481 MET A CE 1 ATOM 3853 N N . ASP A 1 482 ? 32.658 -4.748 40.320 1.00 25.11 ? 482 ASP A N 1 ATOM 3854 C CA . ASP A 1 482 ? 32.596 -4.129 41.647 1.00 25.52 ? 482 ASP A CA 1 ATOM 3855 C C . ASP A 1 482 ? 31.173 -4.158 42.171 1.00 24.84 ? 482 ASP A C 1 ATOM 3856 O O . ASP A 1 482 ? 30.944 -4.366 43.366 1.00 24.36 ? 482 ASP A O 1 ATOM 3857 C CB . ASP A 1 482 ? 33.058 -2.682 41.606 1.00 25.91 ? 482 ASP A CB 1 ATOM 3858 C CG . ASP A 1 482 ? 34.529 -2.567 41.399 1.00 28.85 ? 482 ASP A CG 1 ATOM 3859 O OD1 . ASP A 1 482 ? 35.245 -3.542 41.739 1.00 31.61 ? 482 ASP A OD1 1 ATOM 3860 O OD2 . ASP A 1 482 ? 35.057 -1.554 40.874 1.00 33.02 ? 482 ASP A OD2 1 ATOM 3861 N N . LEU A 1 483 ? 30.223 -3.940 41.264 1.00 23.95 ? 483 LEU A N 1 ATOM 3862 C CA . LEU A 1 483 ? 28.842 -3.880 41.644 1.00 23.33 ? 483 LEU A CA 1 ATOM 3863 C C . LEU A 1 483 ? 28.194 -5.255 41.759 1.00 23.07 ? 483 LEU A C 1 ATOM 3864 O O . LEU A 1 483 ? 27.405 -5.498 42.645 1.00 23.29 ? 483 LEU A O 1 ATOM 3865 C CB . LEU A 1 483 ? 28.082 -3.015 40.662 1.00 22.53 ? 483 LEU A CB 1 ATOM 3866 C CG . LEU A 1 483 ? 28.124 -1.536 40.999 1.00 24.00 ? 483 LEU A CG 1 ATOM 3867 C CD1 . LEU A 1 483 ? 27.438 -0.701 39.926 1.00 26.65 ? 483 LEU A CD1 1 ATOM 3868 C CD2 . LEU A 1 483 ? 27.465 -1.301 42.320 1.00 25.26 ? 483 LEU A CD2 1 ATOM 3869 N N . TYR A 1 484 ? 28.540 -6.143 40.858 1.00 23.19 ? 484 TYR A N 1 ATOM 3870 C CA . TYR A 1 484 ? 27.860 -7.409 40.740 1.00 24.09 ? 484 TYR A CA 1 ATOM 3871 C C . TYR A 1 484 ? 28.681 -8.537 41.305 1.00 24.61 ? 484 TYR A C 1 ATOM 3872 O O . TYR A 1 484 ? 28.138 -9.505 41.816 1.00 24.80 ? 484 TYR A O 1 ATOM 3873 C CB . TYR A 1 484 ? 27.495 -7.668 39.272 1.00 24.10 ? 484 TYR A CB 1 ATOM 3874 C CG . TYR A 1 484 ? 26.277 -6.904 38.767 1.00 23.29 ? 484 TYR A CG 1 ATOM 3875 C CD1 . TYR A 1 484 ? 26.410 -5.681 38.102 1.00 21.64 ? 484 TYR A CD1 1 ATOM 3876 C CD2 . TYR A 1 484 ? 24.985 -7.415 38.953 1.00 24.62 ? 484 TYR A CD2 1 ATOM 3877 C CE1 . TYR A 1 484 ? 25.285 -4.995 37.637 1.00 20.73 ? 484 TYR A CE1 1 ATOM 3878 C CE2 . TYR A 1 484 ? 23.864 -6.734 38.470 1.00 22.28 ? 484 TYR A CE2 1 ATOM 3879 C CZ . TYR A 1 484 ? 24.029 -5.547 37.831 1.00 19.04 ? 484 TYR A CZ 1 ATOM 3880 O OH . TYR A 1 484 ? 22.915 -4.934 37.379 1.00 21.09 ? 484 TYR A OH 1 ATOM 3881 N N . LYS A 1 485 ? 29.993 -8.409 41.219 1.00 25.45 ? 485 LYS A N 1 ATOM 3882 C CA . LYS A 1 485 ? 30.882 -9.359 41.859 1.00 26.27 ? 485 LYS A CA 1 ATOM 3883 C C . LYS A 1 485 ? 30.944 -10.674 41.177 1.00 26.45 ? 485 LYS A C 1 ATOM 3884 O O . LYS A 1 485 ? 31.636 -11.526 41.681 1.00 29.59 ? 485 LYS A O 1 ATOM 3885 C CB . LYS A 1 485 ? 30.433 -9.717 43.272 1.00 26.32 ? 485 LYS A CB 1 ATOM 3886 C CG . LYS A 1 485 ? 30.390 -8.607 44.226 1.00 29.61 ? 485 LYS A CG 1 ATOM 3887 C CD . LYS A 1 485 ? 31.672 -7.817 44.171 1.00 35.02 ? 485 LYS A CD 1 ATOM 3888 C CE . LYS A 1 485 ? 31.742 -6.749 45.277 1.00 34.13 ? 485 LYS A CE 1 ATOM 3889 N NZ . LYS A 1 485 ? 33.103 -6.097 45.293 1.00 37.29 ? 485 LYS A NZ 1 ATOM 3890 N N . THR A 1 486 ? 30.092 -10.927 40.200 1.00 25.31 ? 486 THR A N 1 ATOM 3891 C CA . THR A 1 486 ? 30.261 -12.063 39.291 1.00 24.34 ? 486 THR A CA 1 ATOM 3892 C C . THR A 1 486 ? 29.417 -11.752 38.079 1.00 23.98 ? 486 THR A C 1 ATOM 3893 O O . THR A 1 486 ? 28.332 -11.198 38.218 1.00 24.24 ? 486 THR A O 1 ATOM 3894 C CB . THR A 1 486 ? 29.867 -13.446 39.852 1.00 23.82 ? 486 THR A CB 1 ATOM 3895 O OG1 . THR A 1 486 ? 30.011 -14.403 38.789 1.00 26.08 ? 486 THR A OG1 1 ATOM 3896 C CG2 . THR A 1 486 ? 28.414 -13.519 40.138 1.00 22.15 ? 486 THR A CG2 1 ATOM 3897 N N . PRO A 1 487 ? 29.923 -12.040 36.886 1.00 23.62 ? 487 PRO A N 1 ATOM 3898 C CA . PRO A 1 487 ? 29.128 -11.801 35.677 1.00 23.79 ? 487 PRO A CA 1 ATOM 3899 C C . PRO A 1 487 ? 27.814 -12.582 35.695 1.00 23.65 ? 487 PRO A C 1 ATOM 3900 O O . PRO A 1 487 ? 26.839 -12.119 35.115 1.00 24.33 ? 487 PRO A O 1 ATOM 3901 C CB . PRO A 1 487 ? 30.040 -12.292 34.551 1.00 24.09 ? 487 PRO A CB 1 ATOM 3902 C CG . PRO A 1 487 ? 31.430 -12.159 35.118 1.00 24.19 ? 487 PRO A CG 1 ATOM 3903 C CD . PRO A 1 487 ? 31.288 -12.507 36.576 1.00 23.39 ? 487 PRO A CD 1 ATOM 3904 N N . ASP A 1 488 ? 27.792 -13.756 36.336 1.00 23.00 ? 488 ASP A N 1 ATOM 3905 C CA . ASP A 1 488 ? 26.567 -14.538 36.458 1.00 21.75 ? 488 ASP A CA 1 ATOM 3906 C C . ASP A 1 488 ? 25.453 -13.710 37.095 1.00 20.43 ? 488 ASP A C 1 ATOM 3907 O O . ASP A 1 488 ? 24.279 -13.966 36.870 1.00 20.17 ? 488 ASP A O 1 ATOM 3908 C CB . ASP A 1 488 ? 26.817 -15.757 37.315 1.00 22.41 ? 488 ASP A CB 1 ATOM 3909 C CG . ASP A 1 488 ? 27.828 -16.692 36.706 1.00 24.99 ? 488 ASP A CG 1 ATOM 3910 O OD1 . ASP A 1 488 ? 28.043 -16.629 35.470 1.00 25.21 ? 488 ASP A OD1 1 ATOM 3911 O OD2 . ASP A 1 488 ? 28.441 -17.546 37.393 1.00 28.17 ? 488 ASP A OD2 1 ATOM 3912 N N . ASN A 1 489 ? 25.815 -12.697 37.868 1.00 19.00 ? 489 ASN A N 1 ATOM 3913 C CA . ASN A 1 489 ? 24.808 -11.890 38.527 1.00 17.81 ? 489 ASN A CA 1 ATOM 3914 C C . ASN A 1 489 ? 24.331 -10.626 37.815 1.00 18.13 ? 489 ASN A C 1 ATOM 3915 O O . ASN A 1 489 ? 23.406 -9.965 38.304 1.00 17.46 ? 489 ASN A O 1 ATOM 3916 C CB . ASN A 1 489 ? 25.315 -11.503 39.871 1.00 17.53 ? 489 ASN A CB 1 ATOM 3917 C CG . ASN A 1 489 ? 25.122 -12.581 40.876 1.00 16.69 ? 489 ASN A CG 1 ATOM 3918 O OD1 . ASN A 1 489 ? 24.614 -13.654 40.571 1.00 17.25 ? 489 ASN A OD1 1 ATOM 3919 N ND2 . ASN A 1 489 ? 25.511 -12.300 42.100 1.00 15.13 ? 489 ASN A ND2 1 ATOM 3920 N N . ILE A 1 490 ? 24.958 -10.303 36.680 1.00 17.32 ? 490 ILE A N 1 ATOM 3921 C CA . ILE A 1 490 ? 24.592 -9.141 35.884 1.00 16.64 ? 490 ILE A CA 1 ATOM 3922 C C . ILE A 1 490 ? 23.179 -9.177 35.325 1.00 16.03 ? 490 ILE A C 1 ATOM 3923 O O . ILE A 1 490 ? 22.863 -10.025 34.516 1.00 15.76 ? 490 ILE A O 1 ATOM 3924 C CB . ILE A 1 490 ? 25.622 -8.846 34.753 1.00 17.43 ? 490 ILE A CB 1 ATOM 3925 C CG1 . ILE A 1 490 ? 27.012 -8.638 35.364 1.00 17.93 ? 490 ILE A CG1 1 ATOM 3926 C CG2 . ILE A 1 490 ? 25.218 -7.576 33.946 1.00 14.78 ? 490 ILE A CG2 1 ATOM 3927 C CD1 . ILE A 1 490 ? 28.130 -8.575 34.359 1.00 17.49 ? 490 ILE A CD1 1 ATOM 3928 N N . ASP A 1 491 ? 22.350 -8.207 35.729 1.00 15.62 ? 491 ASP A N 1 ATOM 3929 C CA . ASP A 1 491 ? 20.978 -8.116 35.218 1.00 14.60 ? 491 ASP A CA 1 ATOM 3930 C C . ASP A 1 491 ? 20.981 -8.036 33.649 1.00 15.53 ? 491 ASP A C 1 ATOM 3931 O O . ASP A 1 491 ? 21.749 -7.264 33.035 1.00 14.02 ? 491 ASP A O 1 ATOM 3932 C CB . ASP A 1 491 ? 20.127 -6.992 35.857 1.00 14.18 ? 491 ASP A CB 1 ATOM 3933 C CG . ASP A 1 491 ? 20.123 -6.981 37.424 1.00 13.17 ? 491 ASP A CG 1 ATOM 3934 O OD1 . ASP A 1 491 ? 19.364 -7.701 38.107 1.00 11.46 ? 491 ASP A OD1 1 ATOM 3935 O OD2 . ASP A 1 491 ? 20.805 -6.193 38.075 1.00 14.75 ? 491 ASP A OD2 1 ATOM 3936 N N . ILE A 1 492 ? 20.107 -8.834 33.015 1.00 16.17 ? 492 ILE A N 1 ATOM 3937 C CA . ILE A 1 492 ? 20.132 -8.990 31.563 1.00 17.25 ? 492 ILE A CA 1 ATOM 3938 C C . ILE A 1 492 ? 20.071 -7.697 30.771 1.00 17.90 ? 492 ILE A C 1 ATOM 3939 O O . ILE A 1 492 ? 20.790 -7.528 29.774 1.00 17.91 ? 492 ILE A O 1 ATOM 3940 C CB . ILE A 1 492 ? 19.103 -10.021 31.046 1.00 17.20 ? 492 ILE A CB 1 ATOM 3941 C CG1 . ILE A 1 492 ? 19.293 -10.224 29.556 1.00 17.32 ? 492 ILE A CG1 1 ATOM 3942 C CG2 . ILE A 1 492 ? 17.675 -9.561 31.273 1.00 18.90 ? 492 ILE A CG2 1 ATOM 3943 C CD1 . ILE A 1 492 ? 20.664 -10.680 29.203 1.00 17.07 ? 492 ILE A CD1 1 ATOM 3944 N N . TRP A 1 493 ? 19.215 -6.782 31.206 1.00 18.10 ? 493 TRP A N 1 ATOM 3945 C CA . TRP A 1 493 ? 19.073 -5.505 30.511 1.00 17.84 ? 493 TRP A CA 1 ATOM 3946 C C . TRP A 1 493 ? 20.377 -4.740 30.364 1.00 18.32 ? 493 TRP A C 1 ATOM 3947 O O . TRP A 1 493 ? 20.673 -4.145 29.335 1.00 18.84 ? 493 TRP A O 1 ATOM 3948 C CB . TRP A 1 493 ? 18.095 -4.607 31.261 1.00 17.55 ? 493 TRP A CB 1 ATOM 3949 C CG . TRP A 1 493 ? 17.875 -3.310 30.561 1.00 15.81 ? 493 TRP A CG 1 ATOM 3950 C CD1 . TRP A 1 493 ? 17.253 -3.119 29.364 1.00 13.45 ? 493 TRP A CD1 1 ATOM 3951 C CD2 . TRP A 1 493 ? 18.304 -2.024 31.003 1.00 14.02 ? 493 TRP A CD2 1 ATOM 3952 N NE1 . TRP A 1 493 ? 17.267 -1.788 29.037 1.00 13.36 ? 493 TRP A NE1 1 ATOM 3953 C CE2 . TRP A 1 493 ? 17.895 -1.092 30.039 1.00 13.79 ? 493 TRP A CE2 1 ATOM 3954 C CE3 . TRP A 1 493 ? 18.957 -1.551 32.158 1.00 14.04 ? 493 TRP A CE3 1 ATOM 3955 C CZ2 . TRP A 1 493 ? 18.120 0.284 30.188 1.00 12.61 ? 493 TRP A CZ2 1 ATOM 3956 C CZ3 . TRP A 1 493 ? 19.218 -0.191 32.277 1.00 9.89 ? 493 TRP A CZ3 1 ATOM 3957 C CH2 . TRP A 1 493 ? 18.800 0.703 31.303 1.00 9.58 ? 493 TRP A CH2 1 ATOM 3958 N N . ILE A 1 494 ? 21.169 -4.723 31.411 1.00 19.08 ? 494 ILE A N 1 ATOM 3959 C CA . ILE A 1 494 ? 22.379 -3.936 31.333 1.00 19.44 ? 494 ILE A CA 1 ATOM 3960 C C . ILE A 1 494 ? 23.517 -4.781 30.821 1.00 19.85 ? 494 ILE A C 1 ATOM 3961 O O . ILE A 1 494 ? 24.395 -4.270 30.181 1.00 20.61 ? 494 ILE A O 1 ATOM 3962 C CB . ILE A 1 494 ? 22.678 -3.197 32.665 1.00 19.98 ? 494 ILE A CB 1 ATOM 3963 C CG1 . ILE A 1 494 ? 23.361 -1.866 32.369 1.00 18.72 ? 494 ILE A CG1 1 ATOM 3964 C CG2 . ILE A 1 494 ? 23.437 -4.084 33.656 1.00 17.94 ? 494 ILE A CG2 1 ATOM 3965 C CD1 . ILE A 1 494 ? 24.398 -1.581 33.348 1.00 21.15 ? 494 ILE A CD1 1 ATOM 3966 N N . GLY A 1 495 ? 23.477 -6.085 31.058 1.00 20.35 ? 495 GLY A N 1 ATOM 3967 C CA . GLY A 1 495 ? 24.435 -6.972 30.418 1.00 19.86 ? 495 GLY A CA 1 ATOM 3968 C C . GLY A 1 495 ? 24.277 -6.877 28.906 1.00 19.62 ? 495 GLY A C 1 ATOM 3969 O O . GLY A 1 495 ? 25.243 -6.659 28.167 1.00 19.57 ? 495 GLY A O 1 ATOM 3970 N N . GLY A 1 496 ? 23.049 -7.023 28.434 1.00 19.54 ? 496 GLY A N 1 ATOM 3971 C CA . GLY A 1 496 ? 22.775 -7.018 27.001 1.00 19.36 ? 496 GLY A CA 1 ATOM 3972 C C . GLY A 1 496 ? 23.163 -5.729 26.307 1.00 19.40 ? 496 GLY A C 1 ATOM 3973 O O . GLY A 1 496 ? 23.727 -5.723 25.210 1.00 19.00 ? 496 GLY A O 1 ATOM 3974 N N . ASN A 1 497 ? 22.892 -4.620 26.972 1.00 19.61 ? 497 ASN A N 1 ATOM 3975 C CA . ASN A 1 497 ? 23.191 -3.330 26.386 1.00 19.74 ? 497 ASN A CA 1 ATOM 3976 C C . ASN A 1 497 ? 24.628 -2.882 26.512 1.00 20.22 ? 497 ASN A C 1 ATOM 3977 O O . ASN A 1 497 ? 25.070 -2.043 25.743 1.00 21.25 ? 497 ASN A O 1 ATOM 3978 C CB . ASN A 1 497 ? 22.271 -2.283 26.950 1.00 19.62 ? 497 ASN A CB 1 ATOM 3979 C CG . ASN A 1 497 ? 20.886 -2.427 26.422 1.00 18.72 ? 497 ASN A CG 1 ATOM 3980 O OD1 . ASN A 1 497 ? 19.954 -2.751 27.148 1.00 15.31 ? 497 ASN A OD1 1 ATOM 3981 N ND2 . ASN A 1 497 ? 20.745 -2.226 25.127 1.00 19.88 ? 497 ASN A ND2 1 ATOM 3982 N N . ALA A 1 498 ? 25.384 -3.453 27.436 1.00 20.36 ? 498 ALA A N 1 ATOM 3983 C CA . ALA A 1 498 ? 26.795 -3.079 27.558 1.00 20.83 ? 498 ALA A CA 1 ATOM 3984 C C . ALA A 1 498 ? 27.722 -3.656 26.450 1.00 21.21 ? 498 ALA A C 1 ATOM 3985 O O . ALA A 1 498 ? 28.879 -3.273 26.348 1.00 22.64 ? 498 ALA A O 1 ATOM 3986 C CB . ALA A 1 498 ? 27.330 -3.412 28.985 1.00 20.37 ? 498 ALA A CB 1 ATOM 3987 N N . GLU A 1 499 ? 27.229 -4.577 25.628 1.00 20.92 ? 499 GLU A N 1 ATOM 3988 C CA . GLU A 1 499 ? 28.071 -5.215 24.627 1.00 19.76 ? 499 GLU A CA 1 ATOM 3989 C C . GLU A 1 499 ? 28.240 -4.298 23.450 1.00 19.59 ? 499 GLU A C 1 ATOM 3990 O O . GLU A 1 499 ? 27.328 -3.596 23.116 1.00 19.94 ? 499 GLU A O 1 ATOM 3991 C CB . GLU A 1 499 ? 27.423 -6.519 24.178 1.00 19.30 ? 499 GLU A CB 1 ATOM 3992 C CG . GLU A 1 499 ? 27.356 -7.555 25.281 1.00 18.63 ? 499 GLU A CG 1 ATOM 3993 C CD . GLU A 1 499 ? 26.763 -8.886 24.831 1.00 19.33 ? 499 GLU A CD 1 ATOM 3994 O OE1 . GLU A 1 499 ? 26.179 -8.954 23.714 1.00 20.32 ? 499 GLU A OE1 1 ATOM 3995 O OE2 . GLU A 1 499 ? 26.886 -9.866 25.606 1.00 14.68 ? 499 GLU A OE2 1 ATOM 3996 N N . PRO A 1 500 ? 29.391 -4.307 22.789 1.00 19.77 ? 500 PRO A N 1 ATOM 3997 C CA . PRO A 1 500 ? 29.568 -3.452 21.616 1.00 19.26 ? 500 PRO A CA 1 ATOM 3998 C C . PRO A 1 500 ? 28.604 -3.881 20.526 1.00 19.78 ? 500 PRO A C 1 ATOM 3999 O O . PRO A 1 500 ? 28.042 -4.978 20.589 1.00 19.00 ? 500 PRO A O 1 ATOM 4000 C CB . PRO A 1 500 ? 30.988 -3.736 21.189 1.00 18.33 ? 500 PRO A CB 1 ATOM 4001 C CG . PRO A 1 500 ? 31.604 -4.260 22.391 1.00 19.77 ? 500 PRO A CG 1 ATOM 4002 C CD . PRO A 1 500 ? 30.593 -5.117 23.053 1.00 19.72 ? 500 PRO A CD 1 ATOM 4003 N N . MET A 1 501 ? 28.453 -3.037 19.513 1.00 20.17 ? 501 MET A N 1 ATOM 4004 C CA . MET A 1 501 ? 27.506 -3.333 18.495 1.00 20.93 ? 501 MET A CA 1 ATOM 4005 C C . MET A 1 501 ? 28.079 -4.238 17.437 1.00 21.13 ? 501 MET A C 1 ATOM 4006 O O . MET A 1 501 ? 29.257 -4.198 17.166 1.00 21.01 ? 501 MET A O 1 ATOM 4007 C CB . MET A 1 501 ? 26.979 -2.059 17.909 1.00 21.07 ? 501 MET A CB 1 ATOM 4008 C CG . MET A 1 501 ? 26.069 -1.336 18.839 1.00 24.83 ? 501 MET A CG 1 ATOM 4009 S SD . MET A 1 501 ? 25.802 0.386 18.285 1.00 33.74 ? 501 MET A SD 1 ATOM 4010 C CE . MET A 1 501 ? 24.627 0.984 19.566 1.00 27.35 ? 501 MET A CE 1 ATOM 4011 N N . VAL A 1 502 ? 27.208 -5.082 16.884 1.00 22.25 ? 502 VAL A N 1 ATOM 4012 C CA . VAL A 1 502 ? 27.504 -5.922 15.753 1.00 22.76 ? 502 VAL A CA 1 ATOM 4013 C C . VAL A 1 502 ? 27.574 -4.999 14.518 1.00 24.18 ? 502 VAL A C 1 ATOM 4014 O O . VAL A 1 502 ? 27.169 -3.837 14.552 1.00 23.80 ? 502 VAL A O 1 ATOM 4015 C CB . VAL A 1 502 ? 26.436 -7.003 15.591 1.00 22.31 ? 502 VAL A CB 1 ATOM 4016 C CG1 . VAL A 1 502 ? 26.276 -7.723 16.874 1.00 22.03 ? 502 VAL A CG1 1 ATOM 4017 C CG2 . VAL A 1 502 ? 25.084 -6.390 15.142 1.00 22.46 ? 502 VAL A CG2 1 ATOM 4018 N N . GLU A 1 503 ? 28.115 -5.536 13.438 1.00 25.81 ? 503 GLU A N 1 ATOM 4019 C CA . GLU A 1 503 ? 28.374 -4.798 12.224 1.00 27.11 ? 503 GLU A CA 1 ATOM 4020 C C . GLU A 1 503 ? 27.053 -4.368 11.646 1.00 27.02 ? 503 GLU A C 1 ATOM 4021 O O . GLU A 1 503 ? 26.180 -5.208 11.401 1.00 27.36 ? 503 GLU A O 1 ATOM 4022 C CB . GLU A 1 503 ? 29.060 -5.767 11.260 1.00 27.88 ? 503 GLU A CB 1 ATOM 4023 C CG . GLU A 1 503 ? 30.096 -5.159 10.335 1.00 33.21 ? 503 GLU A CG 1 ATOM 4024 C CD . GLU A 1 503 ? 31.057 -6.227 9.835 1.00 40.04 ? 503 GLU A CD 1 ATOM 4025 O OE1 . GLU A 1 503 ? 31.931 -6.636 10.640 1.00 42.55 ? 503 GLU A OE1 1 ATOM 4026 O OE2 . GLU A 1 503 ? 30.927 -6.684 8.657 1.00 43.96 ? 503 GLU A OE2 1 ATOM 4027 N N . ARG A 1 504 ? 26.920 -3.063 11.402 1.00 26.96 ? 504 ARG A N 1 ATOM 4028 C CA . ARG A 1 504 ? 25.735 -2.439 10.799 1.00 26.53 ? 504 ARG A CA 1 ATOM 4029 C C . ARG A 1 504 ? 24.504 -2.453 11.671 1.00 25.50 ? 504 ARG A C 1 ATOM 4030 O O . ARG A 1 504 ? 23.451 -2.055 11.217 1.00 25.83 ? 504 ARG A O 1 ATOM 4031 C CB . ARG A 1 504 ? 25.364 -3.118 9.495 1.00 27.70 ? 504 ARG A CB 1 ATOM 4032 C CG . ARG A 1 504 ? 26.335 -2.914 8.372 1.00 32.28 ? 504 ARG A CG 1 ATOM 4033 C CD . ARG A 1 504 ? 26.313 -1.524 7.810 1.00 44.58 ? 504 ARG A CD 1 ATOM 4034 N NE . ARG A 1 504 ? 27.409 -1.272 6.867 1.00 53.61 ? 504 ARG A NE 1 ATOM 4035 C CZ . ARG A 1 504 ? 27.687 -0.080 6.349 1.00 57.22 ? 504 ARG A CZ 1 ATOM 4036 N NH1 . ARG A 1 504 ? 26.957 0.989 6.678 1.00 56.75 ? 504 ARG A NH1 1 ATOM 4037 N NH2 . ARG A 1 504 ? 28.704 0.034 5.500 1.00 60.99 ? 504 ARG A NH2 1 ATOM 4038 N N . GLY A 1 505 ? 24.624 -2.919 12.909 1.00 24.02 ? 505 GLY A N 1 ATOM 4039 C CA . GLY A 1 505 ? 23.472 -3.068 13.762 1.00 22.06 ? 505 GLY A CA 1 ATOM 4040 C C . GLY A 1 505 ? 23.415 -2.021 14.832 1.00 21.23 ? 505 GLY A C 1 ATOM 4041 O O . GLY A 1 505 ? 24.171 -1.083 14.778 1.00 22.17 ? 505 GLY A O 1 ATOM 4042 N N . ARG A 1 506 ? 22.514 -2.145 15.796 1.00 19.95 ? 506 ARG A N 1 ATOM 4043 C CA . ARG A 1 506 ? 22.480 -1.169 16.865 1.00 18.64 ? 506 ARG A CA 1 ATOM 4044 C C . ARG A 1 506 ? 22.376 -1.853 18.219 1.00 18.19 ? 506 ARG A C 1 ATOM 4045 O O . ARG A 1 506 ? 22.135 -1.216 19.253 1.00 17.32 ? 506 ARG A O 1 ATOM 4046 C CB . ARG A 1 506 ? 21.390 -0.144 16.629 1.00 18.44 ? 506 ARG A CB 1 ATOM 4047 C CG . ARG A 1 506 ? 21.785 0.897 15.631 1.00 18.76 ? 506 ARG A CG 1 ATOM 4048 C CD . ARG A 1 506 ? 23.004 1.668 16.037 1.00 21.30 ? 506 ARG A CD 1 ATOM 4049 N NE . ARG A 1 506 ? 23.299 2.784 15.140 1.00 24.48 ? 506 ARG A NE 1 ATOM 4050 C CZ . ARG A 1 506 ? 24.106 2.718 14.092 1.00 25.72 ? 506 ARG A CZ 1 ATOM 4051 N NH1 . ARG A 1 506 ? 24.681 1.574 13.757 1.00 26.81 ? 506 ARG A NH1 1 ATOM 4052 N NH2 . ARG A 1 506 ? 24.302 3.791 13.346 1.00 26.07 ? 506 ARG A NH2 1 ATOM 4053 N N . VAL A 1 507 ? 22.576 -3.168 18.181 1.00 17.84 ? 507 VAL A N 1 ATOM 4054 C CA . VAL A 1 507 ? 22.620 -3.986 19.377 1.00 18.19 ? 507 VAL A CA 1 ATOM 4055 C C . VAL A 1 507 ? 23.804 -4.952 19.284 1.00 17.98 ? 507 VAL A C 1 ATOM 4056 O O . VAL A 1 507 ? 24.334 -5.170 18.211 1.00 18.28 ? 507 VAL A O 1 ATOM 4057 C CB . VAL A 1 507 ? 21.324 -4.762 19.562 1.00 18.89 ? 507 VAL A CB 1 ATOM 4058 C CG1 . VAL A 1 507 ? 20.083 -3.813 19.433 1.00 18.08 ? 507 VAL A CG1 1 ATOM 4059 C CG2 . VAL A 1 507 ? 21.263 -5.890 18.587 1.00 19.25 ? 507 VAL A CG2 1 ATOM 4060 N N . GLY A 1 508 ? 24.254 -5.502 20.399 1.00 17.84 ? 508 GLY A N 1 ATOM 4061 C CA . GLY A 1 508 ? 25.323 -6.491 20.354 1.00 18.56 ? 508 GLY A CA 1 ATOM 4062 C C . GLY A 1 508 ? 24.886 -7.920 20.046 1.00 18.98 ? 508 GLY A C 1 ATOM 4063 O O . GLY A 1 508 ? 23.716 -8.186 19.779 1.00 18.87 ? 508 GLY A O 1 ATOM 4064 N N . PRO A 1 509 ? 25.832 -8.851 20.071 1.00 19.42 ? 509 PRO A N 1 ATOM 4065 C CA . PRO A 1 509 ? 25.538 -10.273 19.775 1.00 19.34 ? 509 PRO A CA 1 ATOM 4066 C C . PRO A 1 509 ? 24.434 -10.885 20.646 1.00 19.12 ? 509 PRO A C 1 ATOM 4067 O O . PRO A 1 509 ? 23.590 -11.627 20.119 1.00 19.87 ? 509 PRO A O 1 ATOM 4068 C CB . PRO A 1 509 ? 26.850 -10.987 20.104 1.00 19.34 ? 509 PRO A CB 1 ATOM 4069 C CG . PRO A 1 509 ? 27.891 -9.917 20.036 1.00 20.08 ? 509 PRO A CG 1 ATOM 4070 C CD . PRO A 1 509 ? 27.238 -8.617 20.431 1.00 19.06 ? 509 PRO A CD 1 ATOM 4071 N N . LEU A 1 510 ? 24.440 -10.596 21.947 1.00 18.54 ? 510 LEU A N 1 ATOM 4072 C CA . LEU A 1 510 ? 23.455 -11.193 22.855 1.00 17.94 ? 510 LEU A CA 1 ATOM 4073 C C . LEU A 1 510 ? 22.060 -10.708 22.507 1.00 18.17 ? 510 LEU A C 1 ATOM 4074 O O . LEU A 1 510 ? 21.167 -11.519 22.273 1.00 19.76 ? 510 LEU A O 1 ATOM 4075 C CB . LEU A 1 510 ? 23.764 -10.922 24.324 1.00 16.85 ? 510 LEU A CB 1 ATOM 4076 C CG . LEU A 1 510 ? 22.745 -11.567 25.280 1.00 14.39 ? 510 LEU A CG 1 ATOM 4077 C CD1 . LEU A 1 510 ? 22.693 -13.050 25.158 1.00 13.02 ? 510 LEU A CD1 1 ATOM 4078 C CD2 . LEU A 1 510 ? 23.010 -11.247 26.735 1.00 11.64 ? 510 LEU A CD2 1 ATOM 4079 N N . LEU A 1 511 ? 21.887 -9.398 22.436 1.00 17.15 ? 511 LEU A N 1 ATOM 4080 C CA . LEU A 1 511 ? 20.623 -8.823 22.036 1.00 16.43 ? 511 LEU A CA 1 ATOM 4081 C C . LEU A 1 511 ? 20.140 -9.296 20.643 1.00 16.00 ? 511 LEU A C 1 ATOM 4082 O O . LEU A 1 511 ? 18.981 -9.638 20.465 1.00 15.80 ? 511 LEU A O 1 ATOM 4083 C CB . LEU A 1 511 ? 20.717 -7.295 22.133 1.00 16.30 ? 511 LEU A CB 1 ATOM 4084 C CG . LEU A 1 511 ? 20.042 -6.749 23.412 1.00 16.54 ? 511 LEU A CG 1 ATOM 4085 C CD1 . LEU A 1 511 ? 20.088 -7.700 24.571 1.00 15.69 ? 511 LEU A CD1 1 ATOM 4086 C CD2 . LEU A 1 511 ? 20.546 -5.405 23.858 1.00 17.22 ? 511 LEU A CD2 1 ATOM 4087 N N . ALA A 1 512 ? 21.035 -9.347 19.670 1.00 16.54 ? 512 ALA A N 1 ATOM 4088 C CA . ALA A 1 512 ? 20.688 -9.747 18.294 1.00 17.00 ? 512 ALA A CA 1 ATOM 4089 C C . ALA A 1 512 ? 20.140 -11.169 18.231 1.00 18.07 ? 512 ALA A C 1 ATOM 4090 O O . ALA A 1 512 ? 19.243 -11.466 17.454 1.00 18.59 ? 512 ALA A O 1 ATOM 4091 C CB . ALA A 1 512 ? 21.872 -9.583 17.386 1.00 16.35 ? 512 ALA A CB 1 ATOM 4092 N N . CYS A 1 513 ? 20.679 -12.051 19.072 1.00 18.60 ? 513 CYS A N 1 ATOM 4093 C CA . CYS A 1 513 ? 20.136 -13.395 19.208 1.00 17.68 ? 513 CYS A CA 1 ATOM 4094 C C . CYS A 1 513 ? 18.751 -13.369 19.834 1.00 17.15 ? 513 CYS A C 1 ATOM 4095 O O . CYS A 1 513 ? 17.827 -13.984 19.311 1.00 16.90 ? 513 CYS A O 1 ATOM 4096 C CB . CYS A 1 513 ? 21.086 -14.242 20.041 1.00 18.18 ? 513 CYS A CB 1 ATOM 4097 S SG . CYS A 1 513 ? 20.416 -15.775 20.703 1.00 17.77 ? 513 CYS A SG 1 ATOM 4098 N N . LEU A 1 514 ? 18.596 -12.679 20.964 1.00 16.95 ? 514 LEU A N 1 ATOM 4099 C CA . LEU A 1 514 ? 17.270 -12.578 21.623 1.00 16.92 ? 514 LEU A CA 1 ATOM 4100 C C . LEU A 1 514 ? 16.219 -11.829 20.768 1.00 17.19 ? 514 LEU A C 1 ATOM 4101 O O . LEU A 1 514 ? 15.161 -12.375 20.430 1.00 16.82 ? 514 LEU A O 1 ATOM 4102 C CB . LEU A 1 514 ? 17.393 -11.989 23.020 1.00 17.07 ? 514 LEU A CB 1 ATOM 4103 C CG . LEU A 1 514 ? 18.220 -12.736 24.093 1.00 16.58 ? 514 LEU A CG 1 ATOM 4104 C CD1 . LEU A 1 514 ? 17.938 -12.174 25.436 1.00 15.57 ? 514 LEU A CD1 1 ATOM 4105 C CD2 . LEU A 1 514 ? 17.921 -14.203 24.119 1.00 16.58 ? 514 LEU A CD2 1 ATOM 4106 N N . LEU A 1 515 ? 16.534 -10.611 20.352 1.00 17.32 ? 515 LEU A N 1 ATOM 4107 C CA . LEU A 1 515 ? 15.663 -9.956 19.398 1.00 17.92 ? 515 LEU A CA 1 ATOM 4108 C C . LEU A 1 515 ? 15.406 -10.871 18.221 1.00 17.79 ? 515 LEU A C 1 ATOM 4109 O O . LEU A 1 515 ? 14.276 -11.161 17.927 1.00 18.71 ? 515 LEU A O 1 ATOM 4110 C CB . LEU A 1 515 ? 16.267 -8.639 18.917 1.00 18.26 ? 515 LEU A CB 1 ATOM 4111 C CG . LEU A 1 515 ? 16.299 -7.659 20.088 1.00 18.66 ? 515 LEU A CG 1 ATOM 4112 C CD1 . LEU A 1 515 ? 17.322 -6.571 19.896 1.00 16.79 ? 515 LEU A CD1 1 ATOM 4113 C CD2 . LEU A 1 515 ? 14.881 -7.095 20.222 1.00 20.54 ? 515 LEU A CD2 1 ATOM 4114 N N . GLY A 1 516 ? 16.458 -11.334 17.559 1.00 18.25 ? 516 GLY A N 1 ATOM 4115 C CA . GLY A 1 516 ? 16.353 -12.195 16.381 1.00 17.91 ? 516 GLY A CA 1 ATOM 4116 C C . GLY A 1 516 ? 15.409 -13.374 16.485 1.00 18.57 ? 516 GLY A C 1 ATOM 4117 O O . GLY A 1 516 ? 14.483 -13.530 15.678 1.00 18.47 ? 516 GLY A O 1 ATOM 4118 N N . ARG A 1 517 ? 15.631 -14.226 17.474 1.00 18.77 ? 517 ARG A N 1 ATOM 4119 C CA . ARG A 1 517 ? 14.724 -15.339 17.668 1.00 19.55 ? 517 ARG A CA 1 ATOM 4120 C C . ARG A 1 517 ? 13.254 -14.969 17.835 1.00 18.90 ? 517 ARG A C 1 ATOM 4121 O O . ARG A 1 517 ? 12.395 -15.603 17.217 1.00 20.02 ? 517 ARG A O 1 ATOM 4122 C CB . ARG A 1 517 ? 15.106 -16.109 18.881 1.00 20.83 ? 517 ARG A CB 1 ATOM 4123 C CG . ARG A 1 517 ? 16.300 -16.959 18.739 1.00 25.06 ? 517 ARG A CG 1 ATOM 4124 C CD . ARG A 1 517 ? 16.525 -17.655 20.047 1.00 32.96 ? 517 ARG A CD 1 ATOM 4125 N NE . ARG A 1 517 ? 17.795 -18.347 20.110 1.00 39.16 ? 517 ARG A NE 1 ATOM 4126 C CZ . ARG A 1 517 ? 17.911 -19.612 20.460 1.00 42.22 ? 517 ARG A CZ 1 ATOM 4127 N NH1 . ARG A 1 517 ? 16.818 -20.317 20.779 1.00 43.04 ? 517 ARG A NH1 1 ATOM 4128 N NH2 . ARG A 1 517 ? 19.121 -20.160 20.486 1.00 44.60 ? 517 ARG A NH2 1 ATOM 4129 N N . GLN A 1 518 ? 12.946 -13.996 18.691 1.00 17.73 ? 518 GLN A N 1 ATOM 4130 C CA . GLN A 1 518 ? 11.559 -13.564 18.863 1.00 16.45 ? 518 GLN A CA 1 ATOM 4131 C C . GLN A 1 518 ? 10.917 -13.188 17.546 1.00 16.64 ? 518 GLN A C 1 ATOM 4132 O O . GLN A 1 518 ? 9.833 -13.714 17.205 1.00 16.79 ? 518 GLN A O 1 ATOM 4133 C CB . GLN A 1 518 ? 11.428 -12.384 19.813 1.00 15.66 ? 518 GLN A CB 1 ATOM 4134 C CG . GLN A 1 518 ? 10.020 -12.152 20.248 1.00 13.89 ? 518 GLN A CG 1 ATOM 4135 C CD . GLN A 1 518 ? 9.507 -13.287 21.090 1.00 14.34 ? 518 GLN A CD 1 ATOM 4136 O OE1 . GLN A 1 518 ? 9.929 -13.442 22.241 1.00 13.81 ? 518 GLN A OE1 1 ATOM 4137 N NE2 . GLN A 1 518 ? 8.629 -14.120 20.519 1.00 13.57 ? 518 GLN A NE2 1 ATOM 4138 N N . PHE A 1 519 ? 11.592 -12.333 16.777 1.00 15.97 ? 519 PHE A N 1 ATOM 4139 C CA . PHE A 1 519 ? 10.995 -11.863 15.528 1.00 16.44 ? 519 PHE A CA 1 ATOM 4140 C C . PHE A 1 519 ? 10.790 -12.984 14.516 1.00 17.71 ? 519 PHE A C 1 ATOM 4141 O O . PHE A 1 519 ? 9.740 -13.085 13.888 1.00 18.86 ? 519 PHE A O 1 ATOM 4142 C CB . PHE A 1 519 ? 11.764 -10.693 14.971 1.00 15.80 ? 519 PHE A CB 1 ATOM 4143 C CG . PHE A 1 519 ? 11.515 -9.402 15.715 1.00 14.53 ? 519 PHE A CG 1 ATOM 4144 C CD1 . PHE A 1 519 ? 10.303 -8.701 15.554 1.00 12.96 ? 519 PHE A CD1 1 ATOM 4145 C CD2 . PHE A 1 519 ? 12.484 -8.870 16.550 1.00 11.85 ? 519 PHE A CD2 1 ATOM 4146 C CE1 . PHE A 1 519 ? 10.075 -7.512 16.214 1.00 12.50 ? 519 PHE A CE1 1 ATOM 4147 C CE2 . PHE A 1 519 ? 12.255 -7.647 17.235 1.00 12.57 ? 519 PHE A CE2 1 ATOM 4148 C CZ . PHE A 1 519 ? 11.069 -6.975 17.082 1.00 10.30 ? 519 PHE A CZ 1 ATOM 4149 N N . GLN A 1 520 ? 11.766 -13.865 14.400 1.00 19.02 ? 520 GLN A N 1 ATOM 4150 C CA . GLN A 1 520 ? 11.609 -15.031 13.563 1.00 20.59 ? 520 GLN A CA 1 ATOM 4151 C C . GLN A 1 520 ? 10.340 -15.783 13.919 1.00 21.24 ? 520 GLN A C 1 ATOM 4152 O O . GLN A 1 520 ? 9.538 -16.144 13.043 1.00 21.14 ? 520 GLN A O 1 ATOM 4153 C CB . GLN A 1 520 ? 12.795 -15.974 13.740 1.00 21.39 ? 520 GLN A CB 1 ATOM 4154 C CG . GLN A 1 520 ? 12.670 -17.274 12.942 1.00 21.41 ? 520 GLN A CG 1 ATOM 4155 C CD . GLN A 1 520 ? 12.360 -18.441 13.852 1.00 24.07 ? 520 GLN A CD 1 ATOM 4156 O OE1 . GLN A 1 520 ? 11.387 -19.172 13.638 1.00 26.12 ? 520 GLN A OE1 1 ATOM 4157 N NE2 . GLN A 1 520 ? 13.176 -18.615 14.889 1.00 22.95 ? 520 GLN A NE2 1 ATOM 4158 N N . GLN A 1 521 ? 10.152 -16.003 15.217 1.00 21.43 ? 521 GLN A N 1 ATOM 4159 C CA . GLN A 1 521 ? 9.002 -16.758 15.680 1.00 21.27 ? 521 GLN A CA 1 ATOM 4160 C C . GLN A 1 521 ? 7.693 -16.021 15.486 1.00 21.49 ? 521 GLN A C 1 ATOM 4161 O O . GLN A 1 521 ? 6.715 -16.623 15.084 1.00 21.37 ? 521 GLN A O 1 ATOM 4162 C CB . GLN A 1 521 ? 9.166 -17.080 17.143 1.00 21.69 ? 521 GLN A CB 1 ATOM 4163 C CG . GLN A 1 521 ? 10.100 -18.201 17.443 1.00 21.92 ? 521 GLN A CG 1 ATOM 4164 C CD . GLN A 1 521 ? 10.264 -18.378 18.913 1.00 25.96 ? 521 GLN A CD 1 ATOM 4165 O OE1 . GLN A 1 521 ? 9.325 -18.080 19.706 1.00 27.88 ? 521 GLN A OE1 1 ATOM 4166 N NE2 . GLN A 1 521 ? 11.458 -18.822 19.320 1.00 26.01 ? 521 GLN A NE2 1 ATOM 4167 N N . ILE A 1 522 ? 7.642 -14.722 15.777 1.00 21.76 ? 522 ILE A N 1 ATOM 4168 C CA . ILE A 1 522 ? 6.352 -14.033 15.605 1.00 22.32 ? 522 ILE A CA 1 ATOM 4169 C C . ILE A 1 522 ? 5.957 -13.969 14.151 1.00 22.31 ? 522 ILE A C 1 ATOM 4170 O O . ILE A 1 522 ? 4.777 -13.951 13.834 1.00 21.92 ? 522 ILE A O 1 ATOM 4171 C CB . ILE A 1 522 ? 6.268 -12.614 16.251 1.00 22.80 ? 522 ILE A CB 1 ATOM 4172 C CG1 . ILE A 1 522 ? 7.223 -11.624 15.601 1.00 22.63 ? 522 ILE A CG1 1 ATOM 4173 C CG2 . ILE A 1 522 ? 6.504 -12.689 17.748 1.00 22.63 ? 522 ILE A CG2 1 ATOM 4174 C CD1 . ILE A 1 522 ? 7.426 -10.419 16.477 1.00 23.83 ? 522 ILE A CD1 1 ATOM 4175 N N . ARG A 1 523 ? 6.946 -13.952 13.265 1.00 21.80 ? 523 ARG A N 1 ATOM 4176 C CA . ARG A 1 523 ? 6.607 -14.007 11.866 1.00 21.65 ? 523 ARG A CA 1 ATOM 4177 C C . ARG A 1 523 ? 6.265 -15.453 11.412 1.00 21.83 ? 523 ARG A C 1 ATOM 4178 O O . ARG A 1 523 ? 5.263 -15.639 10.745 1.00 22.18 ? 523 ARG A O 1 ATOM 4179 C CB . ARG A 1 523 ? 7.700 -13.338 11.027 1.00 21.68 ? 523 ARG A CB 1 ATOM 4180 C CG . ARG A 1 523 ? 7.744 -13.728 9.563 1.00 21.55 ? 523 ARG A CG 1 ATOM 4181 C CD . ARG A 1 523 ? 8.805 -14.795 9.291 1.00 21.46 ? 523 ARG A CD 1 ATOM 4182 N NE . ARG A 1 523 ? 9.846 -14.273 8.425 1.00 19.00 ? 523 ARG A NE 1 ATOM 4183 C CZ . ARG A 1 523 ? 10.965 -14.909 8.131 1.00 18.87 ? 523 ARG A CZ 1 ATOM 4184 N NH1 . ARG A 1 523 ? 11.232 -16.097 8.630 1.00 17.09 ? 523 ARG A NH1 1 ATOM 4185 N NH2 . ARG A 1 523 ? 11.832 -14.352 7.313 1.00 21.95 ? 523 ARG A NH2 1 ATOM 4186 N N . ASP A 1 524 ? 7.061 -16.465 11.785 1.00 21.09 ? 524 ASP A N 1 ATOM 4187 C CA . ASP A 1 524 ? 6.814 -17.828 11.294 1.00 20.59 ? 524 ASP A CA 1 ATOM 4188 C C . ASP A 1 524 ? 5.582 -18.422 11.936 1.00 20.43 ? 524 ASP A C 1 ATOM 4189 O O . ASP A 1 524 ? 4.960 -19.363 11.392 1.00 19.52 ? 524 ASP A O 1 ATOM 4190 C CB . ASP A 1 524 ? 8.012 -18.769 11.524 1.00 19.85 ? 524 ASP A CB 1 ATOM 4191 C CG . ASP A 1 524 ? 9.171 -18.438 10.645 1.00 21.73 ? 524 ASP A CG 1 ATOM 4192 O OD1 . ASP A 1 524 ? 8.999 -17.569 9.740 1.00 23.92 ? 524 ASP A OD1 1 ATOM 4193 O OD2 . ASP A 1 524 ? 10.301 -18.956 10.794 1.00 22.70 ? 524 ASP A OD2 1 ATOM 4194 N N . GLY A 1 525 ? 5.224 -17.862 13.089 1.00 19.86 ? 525 GLY A N 1 ATOM 4195 C CA . GLY A 1 525 ? 4.120 -18.401 13.850 1.00 19.51 ? 525 GLY A CA 1 ATOM 4196 C C . GLY A 1 525 ? 2.817 -17.705 13.565 1.00 19.99 ? 525 GLY A C 1 ATOM 4197 O O . GLY A 1 525 ? 1.817 -18.042 14.160 1.00 19.86 ? 525 GLY A O 1 ATOM 4198 N N . ASP A 1 526 ? 2.805 -16.751 12.647 1.00 20.86 ? 526 ASP A N 1 ATOM 4199 C CA . ASP A 1 526 ? 1.602 -15.941 12.421 1.00 22.38 ? 526 ASP A CA 1 ATOM 4200 C C . ASP A 1 526 ? 0.807 -16.384 11.197 1.00 23.47 ? 526 ASP A C 1 ATOM 4201 O O . ASP A 1 526 ? 1.290 -16.273 10.065 1.00 24.13 ? 526 ASP A O 1 ATOM 4202 C CB . ASP A 1 526 ? 2.015 -14.471 12.330 1.00 22.19 ? 526 ASP A CB 1 ATOM 4203 C CG . ASP A 1 526 ? 0.870 -13.528 12.084 1.00 22.56 ? 526 ASP A CG 1 ATOM 4204 O OD1 . ASP A 1 526 ? -0.334 -13.871 12.259 1.00 21.73 ? 526 ASP A OD1 1 ATOM 4205 O OD2 . ASP A 1 526 ? 1.134 -12.364 11.709 1.00 25.13 ? 526 ASP A OD2 1 ATOM 4206 N N . ARG A 1 527 ? -0.404 -16.909 11.422 1.00 24.30 ? 527 ARG A N 1 ATOM 4207 C CA . ARG A 1 527 ? -1.221 -17.415 10.313 1.00 24.73 ? 527 ARG A CA 1 ATOM 4208 C C . ARG A 1 527 ? -1.545 -16.298 9.384 1.00 24.65 ? 527 ARG A C 1 ATOM 4209 O O . ARG A 1 527 ? -1.830 -16.527 8.221 1.00 25.46 ? 527 ARG A O 1 ATOM 4210 C CB . ARG A 1 527 ? -2.541 -17.988 10.787 1.00 25.04 ? 527 ARG A CB 1 ATOM 4211 C CG . ARG A 1 527 ? -2.919 -19.310 10.119 1.00 26.11 ? 527 ARG A CG 1 ATOM 4212 C CD . ARG A 1 527 ? -4.382 -19.466 9.732 1.00 24.71 ? 527 ARG A CD 1 ATOM 4213 N NE . ARG A 1 527 ? -5.289 -19.371 10.861 1.00 27.03 ? 527 ARG A NE 1 ATOM 4214 C CZ . ARG A 1 527 ? -6.551 -18.996 10.747 1.00 28.96 ? 527 ARG A CZ 1 ATOM 4215 N NH1 . ARG A 1 527 ? -7.015 -18.707 9.543 1.00 30.43 ? 527 ARG A NH1 1 ATOM 4216 N NH2 . ARG A 1 527 ? -7.349 -18.903 11.816 1.00 29.43 ? 527 ARG A NH2 1 ATOM 4217 N N . PHE A 1 528 ? -1.486 -15.081 9.905 1.00 24.39 ? 528 PHE A N 1 ATOM 4218 C CA . PHE A 1 528 ? -1.883 -13.908 9.140 1.00 24.08 ? 528 PHE A CA 1 ATOM 4219 C C . PHE A 1 528 ? -0.711 -13.044 8.698 1.00 23.24 ? 528 PHE A C 1 ATOM 4220 O O . PHE A 1 528 ? -0.894 -11.914 8.299 1.00 23.44 ? 528 PHE A O 1 ATOM 4221 C CB . PHE A 1 528 ? -2.974 -13.103 9.870 1.00 24.15 ? 528 PHE A CB 1 ATOM 4222 C CG . PHE A 1 528 ? -4.319 -13.805 9.896 1.00 25.33 ? 528 PHE A CG 1 ATOM 4223 C CD1 . PHE A 1 528 ? -4.722 -14.547 11.022 1.00 26.46 ? 528 PHE A CD1 1 ATOM 4224 C CD2 . PHE A 1 528 ? -5.170 -13.760 8.791 1.00 23.45 ? 528 PHE A CD2 1 ATOM 4225 C CE1 . PHE A 1 528 ? -5.967 -15.213 11.049 1.00 24.98 ? 528 PHE A CE1 1 ATOM 4226 C CE2 . PHE A 1 528 ? -6.407 -14.413 8.821 1.00 23.38 ? 528 PHE A CE2 1 ATOM 4227 C CZ . PHE A 1 528 ? -6.805 -15.145 9.954 1.00 22.86 ? 528 PHE A CZ 1 ATOM 4228 N N . TRP A 1 529 ? 0.491 -13.577 8.760 1.00 22.58 ? 529 TRP A N 1 ATOM 4229 C CA . TRP A 1 529 ? 1.618 -12.885 8.177 1.00 22.87 ? 529 TRP A CA 1 ATOM 4230 C C . TRP A 1 529 ? 1.285 -12.511 6.711 1.00 23.68 ? 529 TRP A C 1 ATOM 4231 O O . TRP A 1 529 ? 0.812 -13.321 5.932 1.00 23.85 ? 529 TRP A O 1 ATOM 4232 C CB . TRP A 1 529 ? 2.890 -13.739 8.297 1.00 22.70 ? 529 TRP A CB 1 ATOM 4233 C CG . TRP A 1 529 ? 4.057 -13.063 7.754 1.00 22.14 ? 529 TRP A CG 1 ATOM 4234 C CD1 . TRP A 1 529 ? 4.649 -13.284 6.545 1.00 21.81 ? 529 TRP A CD1 1 ATOM 4235 C CD2 . TRP A 1 529 ? 4.761 -11.990 8.362 1.00 22.37 ? 529 TRP A CD2 1 ATOM 4236 N NE1 . TRP A 1 529 ? 5.701 -12.420 6.373 1.00 23.77 ? 529 TRP A NE1 1 ATOM 4237 C CE2 . TRP A 1 529 ? 5.789 -11.609 7.477 1.00 23.24 ? 529 TRP A CE2 1 ATOM 4238 C CE3 . TRP A 1 529 ? 4.645 -11.321 9.586 1.00 23.88 ? 529 TRP A CE3 1 ATOM 4239 C CZ2 . TRP A 1 529 ? 6.692 -10.589 7.770 1.00 25.07 ? 529 TRP A CZ2 1 ATOM 4240 C CZ3 . TRP A 1 529 ? 5.550 -10.305 9.885 1.00 26.14 ? 529 TRP A CZ3 1 ATOM 4241 C CH2 . TRP A 1 529 ? 6.567 -9.952 8.974 1.00 26.17 ? 529 TRP A CH2 1 ATOM 4242 N N . TRP A 1 530 ? 1.527 -11.265 6.336 1.00 25.42 ? 530 TRP A N 1 ATOM 4243 C CA . TRP A 1 530 ? 1.108 -10.740 5.023 1.00 26.96 ? 530 TRP A CA 1 ATOM 4244 C C . TRP A 1 530 ? 1.556 -11.552 3.767 1.00 28.16 ? 530 TRP A C 1 ATOM 4245 O O . TRP A 1 530 ? 0.833 -11.592 2.756 1.00 28.05 ? 530 TRP A O 1 ATOM 4246 C CB . TRP A 1 530 ? 1.524 -9.278 4.899 1.00 26.59 ? 530 TRP A CB 1 ATOM 4247 C CG . TRP A 1 530 ? 2.928 -9.142 4.527 1.00 27.00 ? 530 TRP A CG 1 ATOM 4248 C CD1 . TRP A 1 530 ? 4.012 -9.257 5.352 1.00 27.79 ? 530 TRP A CD1 1 ATOM 4249 C CD2 . TRP A 1 530 ? 3.438 -8.912 3.218 1.00 26.44 ? 530 TRP A CD2 1 ATOM 4250 N NE1 . TRP A 1 530 ? 5.171 -9.098 4.630 1.00 28.47 ? 530 TRP A NE1 1 ATOM 4251 C CE2 . TRP A 1 530 ? 4.844 -8.882 3.315 1.00 27.46 ? 530 TRP A CE2 1 ATOM 4252 C CE3 . TRP A 1 530 ? 2.850 -8.745 1.963 1.00 27.37 ? 530 TRP A CE3 1 ATOM 4253 C CZ2 . TRP A 1 530 ? 5.663 -8.693 2.213 1.00 25.77 ? 530 TRP A CZ2 1 ATOM 4254 C CZ3 . TRP A 1 530 ? 3.663 -8.547 0.872 1.00 26.86 ? 530 TRP A CZ3 1 ATOM 4255 C CH2 . TRP A 1 530 ? 5.054 -8.507 1.006 1.00 25.97 ? 530 TRP A CH2 1 ATOM 4256 N N . GLU A 1 531 ? 2.728 -12.177 3.831 1.00 28.89 ? 531 GLU A N 1 ATOM 4257 C CA . GLU A 1 531 ? 3.208 -13.001 2.725 1.00 30.85 ? 531 GLU A CA 1 ATOM 4258 C C . GLU A 1 531 ? 2.629 -14.430 2.720 1.00 31.00 ? 531 GLU A C 1 ATOM 4259 O O . GLU A 1 531 ? 2.870 -15.229 1.796 1.00 31.58 ? 531 GLU A O 1 ATOM 4260 C CB . GLU A 1 531 ? 4.726 -13.137 2.781 1.00 31.41 ? 531 GLU A CB 1 ATOM 4261 C CG . GLU A 1 531 ? 5.500 -11.833 2.661 1.00 35.34 ? 531 GLU A CG 1 ATOM 4262 C CD . GLU A 1 531 ? 6.998 -12.066 2.702 1.00 40.59 ? 531 GLU A CD 1 ATOM 4263 O OE1 . GLU A 1 531 ? 7.569 -12.092 3.835 1.00 40.80 ? 531 GLU A OE1 1 ATOM 4264 O OE2 . GLU A 1 531 ? 7.585 -12.258 1.605 1.00 40.67 ? 531 GLU A OE2 1 ATOM 4265 N N . ASN A 1 532 ? 1.914 -14.790 3.770 1.00 31.16 ? 532 ASN A N 1 ATOM 4266 C CA . ASN A 1 532 ? 1.360 -16.128 3.826 1.00 31.00 ? 532 ASN A CA 1 ATOM 4267 C C . ASN A 1 532 ? 0.365 -16.308 2.685 1.00 30.53 ? 532 ASN A C 1 ATOM 4268 O O . ASN A 1 532 ? -0.569 -15.513 2.550 1.00 30.73 ? 532 ASN A O 1 ATOM 4269 C CB . ASN A 1 532 ? 0.678 -16.347 5.168 1.00 31.23 ? 532 ASN A CB 1 ATOM 4270 C CG . ASN A 1 532 ? 0.287 -17.783 5.382 1.00 32.63 ? 532 ASN A CG 1 ATOM 4271 O OD1 . ASN A 1 532 ? 0.915 -18.697 4.818 1.00 31.70 ? 532 ASN A OD1 1 ATOM 4272 N ND2 . ASN A 1 532 ? -0.750 -18.007 6.213 1.00 34.04 ? 532 ASN A ND2 1 ATOM 4273 N N . PRO A 1 533 ? 0.594 -17.303 1.828 1.00 29.98 ? 533 PRO A N 1 ATOM 4274 C CA . PRO A 1 533 ? -0.330 -17.582 0.724 1.00 29.06 ? 533 PRO A CA 1 ATOM 4275 C C . PRO A 1 533 ? -1.796 -17.610 1.159 1.00 28.70 ? 533 PRO A C 1 ATOM 4276 O O . PRO A 1 533 ? -2.149 -18.232 2.157 1.00 28.32 ? 533 PRO A O 1 ATOM 4277 C CB . PRO A 1 533 ? 0.155 -18.922 0.223 1.00 29.28 ? 533 PRO A CB 1 ATOM 4278 C CG . PRO A 1 533 ? 1.649 -18.817 0.424 1.00 28.77 ? 533 PRO A CG 1 ATOM 4279 C CD . PRO A 1 533 ? 1.780 -18.179 1.785 1.00 29.37 ? 533 PRO A CD 1 ATOM 4280 N N . GLY A 1 534 ? -2.632 -16.868 0.437 1.00 28.19 ? 534 GLY A N 1 ATOM 4281 C CA . GLY A 1 534 ? -4.055 -16.844 0.719 1.00 28.07 ? 534 GLY A CA 1 ATOM 4282 C C . GLY A 1 534 ? -4.592 -15.778 1.674 1.00 28.40 ? 534 GLY A C 1 ATOM 4283 O O . GLY A 1 534 ? -5.811 -15.636 1.798 1.00 27.36 ? 534 GLY A O 1 ATOM 4284 N N . VAL A 1 535 ? -3.703 -15.040 2.345 1.00 28.80 ? 535 VAL A N 1 ATOM 4285 C CA . VAL A 1 535 ? -4.079 -13.980 3.275 1.00 29.03 ? 535 VAL A CA 1 ATOM 4286 C C . VAL A 1 535 ? -4.420 -12.733 2.462 1.00 28.83 ? 535 VAL A C 1 ATOM 4287 O O . VAL A 1 535 ? -5.481 -12.131 2.628 1.00 28.36 ? 535 VAL A O 1 ATOM 4288 C CB . VAL A 1 535 ? -2.920 -13.682 4.239 1.00 29.17 ? 535 VAL A CB 1 ATOM 4289 C CG1 . VAL A 1 535 ? -3.131 -12.362 4.957 1.00 29.77 ? 535 VAL A CG1 1 ATOM 4290 C CG2 . VAL A 1 535 ? -2.772 -14.804 5.261 1.00 30.84 ? 535 VAL A CG2 1 ATOM 4291 N N . PHE A 1 536 ? -3.496 -12.369 1.580 1.00 28.93 ? 536 PHE A N 1 ATOM 4292 C CA . PHE A 1 536 ? -3.728 -11.338 0.581 1.00 29.32 ? 536 PHE A CA 1 ATOM 4293 C C . PHE A 1 536 ? -3.622 -12.014 -0.775 1.00 28.96 ? 536 PHE A C 1 ATOM 4294 O O . PHE A 1 536 ? -3.218 -13.150 -0.835 1.00 29.00 ? 536 PHE A O 1 ATOM 4295 C CB . PHE A 1 536 ? -2.663 -10.247 0.679 1.00 29.45 ? 536 PHE A CB 1 ATOM 4296 C CG . PHE A 1 536 ? -2.794 -9.391 1.874 1.00 29.58 ? 536 PHE A CG 1 ATOM 4297 C CD1 . PHE A 1 536 ? -1.992 -9.573 2.985 1.00 30.55 ? 536 PHE A CD1 1 ATOM 4298 C CD2 . PHE A 1 536 ? -3.717 -8.384 1.889 1.00 30.80 ? 536 PHE A CD2 1 ATOM 4299 C CE1 . PHE A 1 536 ? -2.114 -8.754 4.089 1.00 27.73 ? 536 PHE A CE1 1 ATOM 4300 C CE2 . PHE A 1 536 ? -3.825 -7.558 2.988 1.00 30.05 ? 536 PHE A CE2 1 ATOM 4301 C CZ . PHE A 1 536 ? -3.024 -7.766 4.093 1.00 28.29 ? 536 PHE A CZ 1 ATOM 4302 N N . THR A 1 537 ? -3.987 -11.330 -1.853 1.00 29.42 ? 537 THR A N 1 ATOM 4303 C CA . THR A 1 537 ? -3.772 -11.902 -3.180 1.00 30.50 ? 537 THR A CA 1 ATOM 4304 C C . THR A 1 537 ? -2.454 -11.391 -3.733 1.00 31.69 ? 537 THR A C 1 ATOM 4305 O O . THR A 1 537 ? -2.047 -10.282 -3.414 1.00 32.41 ? 537 THR A O 1 ATOM 4306 C CB . THR A 1 537 ? -4.897 -11.567 -4.181 1.00 30.11 ? 537 THR A CB 1 ATOM 4307 O OG1 . THR A 1 537 ? -4.817 -10.183 -4.536 1.00 29.70 ? 537 THR A OG1 1 ATOM 4308 C CG2 . THR A 1 537 ? -6.276 -11.759 -3.576 1.00 28.52 ? 537 THR A CG2 1 ATOM 4309 N N . GLU A 1 538 ? -1.803 -12.215 -4.551 1.00 32.80 ? 538 GLU A N 1 ATOM 4310 C CA . GLU A 1 538 ? -0.564 -11.917 -5.245 1.00 33.97 ? 538 GLU A CA 1 ATOM 4311 C C . GLU A 1 538 ? -0.515 -10.468 -5.681 1.00 34.01 ? 538 GLU A C 1 ATOM 4312 O O . GLU A 1 538 ? 0.534 -9.821 -5.617 1.00 33.56 ? 538 GLU A O 1 ATOM 4313 C CB . GLU A 1 538 ? -0.557 -12.750 -6.521 1.00 35.08 ? 538 GLU A CB 1 ATOM 4314 C CG . GLU A 1 538 ? 0.742 -13.437 -6.928 1.00 40.40 ? 538 GLU A CG 1 ATOM 4315 C CD . GLU A 1 538 ? 0.476 -14.712 -7.768 1.00 50.46 ? 538 GLU A CD 1 ATOM 4316 O OE1 . GLU A 1 538 ? 0.017 -14.576 -8.953 1.00 52.39 ? 538 GLU A OE1 1 ATOM 4317 O OE2 . GLU A 1 538 ? 0.702 -15.863 -7.247 1.00 52.61 ? 538 GLU A OE2 1 ATOM 4318 N N . LYS A 1 539 ? -1.654 -9.968 -6.154 1.00 34.48 ? 539 LYS A N 1 ATOM 4319 C CA . LYS A 1 539 ? -1.749 -8.617 -6.692 1.00 35.32 ? 539 LYS A CA 1 ATOM 4320 C C . LYS A 1 539 ? -1.810 -7.589 -5.580 1.00 35.62 ? 539 LYS A C 1 ATOM 4321 O O . LYS A 1 539 ? -1.233 -6.490 -5.701 1.00 35.93 ? 539 LYS A O 1 ATOM 4322 C CB . LYS A 1 539 ? -2.954 -8.475 -7.624 1.00 35.27 ? 539 LYS A CB 1 ATOM 4323 C CG . LYS A 1 539 ? -2.558 -7.937 -8.990 1.00 38.35 ? 539 LYS A CG 1 ATOM 4324 C CD . LYS A 1 539 ? -3.582 -8.262 -10.086 1.00 44.36 ? 539 LYS A CD 1 ATOM 4325 C CE . LYS A 1 539 ? -3.387 -7.364 -11.347 1.00 46.66 ? 539 LYS A CE 1 ATOM 4326 N NZ . LYS A 1 539 ? -3.715 -5.898 -11.096 1.00 48.94 ? 539 LYS A NZ 1 ATOM 4327 N N . GLN A 1 540 ? -2.516 -7.946 -4.509 1.00 35.41 ? 540 GLN A N 1 ATOM 4328 C CA . GLN A 1 540 ? -2.565 -7.120 -3.318 1.00 35.11 ? 540 GLN A CA 1 ATOM 4329 C C . GLN A 1 540 ? -1.153 -7.070 -2.751 1.00 34.88 ? 540 GLN A C 1 ATOM 4330 O O . GLN A 1 540 ? -0.639 -5.999 -2.407 1.00 34.86 ? 540 GLN A O 1 ATOM 4331 C CB . GLN A 1 540 ? -3.543 -7.714 -2.294 1.00 35.45 ? 540 GLN A CB 1 ATOM 4332 C CG . GLN A 1 540 ? -4.945 -7.888 -2.843 1.00 35.45 ? 540 GLN A CG 1 ATOM 4333 C CD . GLN A 1 540 ? -5.979 -8.196 -1.795 1.00 36.61 ? 540 GLN A CD 1 ATOM 4334 O OE1 . GLN A 1 540 ? -5.915 -9.229 -1.111 1.00 38.49 ? 540 GLN A OE1 1 ATOM 4335 N NE2 . GLN A 1 540 ? -6.966 -7.318 -1.683 1.00 36.90 ? 540 GLN A NE2 1 ATOM 4336 N N . ARG A 1 541 ? -0.512 -8.225 -2.688 1.00 34.35 ? 541 ARG A N 1 ATOM 4337 C CA . ARG A 1 541 ? 0.848 -8.303 -2.179 1.00 34.74 ? 541 ARG A CA 1 ATOM 4338 C C . ARG A 1 541 ? 1.832 -7.448 -2.936 1.00 35.92 ? 541 ARG A C 1 ATOM 4339 O O . ARG A 1 541 ? 2.745 -6.873 -2.347 1.00 36.65 ? 541 ARG A O 1 ATOM 4340 C CB . ARG A 1 541 ? 1.337 -9.739 -2.200 1.00 34.28 ? 541 ARG A CB 1 ATOM 4341 C CG . ARG A 1 541 ? 0.810 -10.546 -1.080 1.00 33.01 ? 541 ARG A CG 1 ATOM 4342 C CD . ARG A 1 541 ? 1.748 -11.610 -0.620 1.00 32.40 ? 541 ARG A CD 1 ATOM 4343 N NE . ARG A 1 541 ? 1.923 -12.631 -1.644 1.00 32.67 ? 541 ARG A NE 1 ATOM 4344 C CZ . ARG A 1 541 ? 1.036 -13.573 -1.929 1.00 31.99 ? 541 ARG A CZ 1 ATOM 4345 N NH1 . ARG A 1 541 ? -0.129 -13.665 -1.287 1.00 29.70 ? 541 ARG A NH1 1 ATOM 4346 N NH2 . ARG A 1 541 ? 1.318 -14.421 -2.887 1.00 34.18 ? 541 ARG A NH2 1 ATOM 4347 N N . ASP A 1 542 ? 1.678 -7.412 -4.254 1.00 37.38 ? 542 ASP A N 1 ATOM 4348 C CA . ASP A 1 542 ? 2.492 -6.576 -5.135 1.00 38.44 ? 542 ASP A CA 1 ATOM 4349 C C . ASP A 1 542 ? 2.350 -5.074 -4.834 1.00 38.04 ? 542 ASP A C 1 ATOM 4350 O O . ASP A 1 542 ? 3.284 -4.277 -5.031 1.00 38.13 ? 542 ASP A O 1 ATOM 4351 C CB . ASP A 1 542 ? 2.079 -6.822 -6.585 1.00 39.41 ? 542 ASP A CB 1 ATOM 4352 C CG . ASP A 1 542 ? 2.889 -7.920 -7.242 1.00 42.94 ? 542 ASP A CG 1 ATOM 4353 O OD1 . ASP A 1 542 ? 4.139 -7.794 -7.256 1.00 48.15 ? 542 ASP A OD1 1 ATOM 4354 O OD2 . ASP A 1 542 ? 2.374 -8.933 -7.785 1.00 46.26 ? 542 ASP A OD2 1 ATOM 4355 N N . SER A 1 543 ? 1.178 -4.702 -4.351 1.00 37.66 ? 543 SER A N 1 ATOM 4356 C CA . SER A 1 543 ? 0.855 -3.311 -4.120 1.00 38.10 ? 543 SER A CA 1 ATOM 4357 C C . SER A 1 543 ? 1.297 -2.878 -2.725 1.00 38.12 ? 543 SER A C 1 ATOM 4358 O O . SER A 1 543 ? 1.503 -1.689 -2.453 1.00 37.50 ? 543 SER A O 1 ATOM 4359 C CB . SER A 1 543 ? -0.648 -3.131 -4.308 1.00 37.88 ? 543 SER A CB 1 ATOM 4360 O OG . SER A 1 543 ? -1.051 -1.820 -3.988 1.00 40.79 ? 543 SER A OG 1 ATOM 4361 N N . LEU A 1 544 ? 1.459 -3.869 -1.849 1.00 38.27 ? 544 LEU A N 1 ATOM 4362 C CA . LEU A 1 544 ? 1.887 -3.618 -0.477 1.00 38.00 ? 544 LEU A CA 1 ATOM 4363 C C . LEU A 1 544 ? 3.418 -3.506 -0.321 1.00 38.63 ? 544 LEU A C 1 ATOM 4364 O O . LEU A 1 544 ? 3.911 -2.935 0.667 1.00 38.60 ? 544 LEU A O 1 ATOM 4365 C CB . LEU A 1 544 ? 1.346 -4.702 0.435 1.00 37.34 ? 544 LEU A CB 1 ATOM 4366 C CG . LEU A 1 544 ? -0.142 -4.604 0.743 1.00 35.11 ? 544 LEU A CG 1 ATOM 4367 C CD1 . LEU A 1 544 ? -0.696 -5.956 1.109 1.00 33.29 ? 544 LEU A CD1 1 ATOM 4368 C CD2 . LEU A 1 544 ? -0.343 -3.670 1.884 1.00 34.98 ? 544 LEU A CD2 1 ATOM 4369 N N . GLN A 1 545 ? 4.162 -4.037 -1.294 1.00 38.61 ? 545 GLN A N 1 ATOM 4370 C CA . GLN A 1 545 ? 5.619 -3.951 -1.262 1.00 39.06 ? 545 GLN A CA 1 ATOM 4371 C C . GLN A 1 545 ? 6.095 -2.550 -1.563 1.00 38.88 ? 545 GLN A C 1 ATOM 4372 O O . GLN A 1 545 ? 7.275 -2.258 -1.432 1.00 39.58 ? 545 GLN A O 1 ATOM 4373 C CB . GLN A 1 545 ? 6.239 -4.911 -2.265 1.00 39.28 ? 545 GLN A CB 1 ATOM 4374 C CG . GLN A 1 545 ? 6.324 -6.332 -1.743 1.00 42.60 ? 545 GLN A CG 1 ATOM 4375 C CD . GLN A 1 545 ? 6.598 -7.338 -2.842 1.00 45.88 ? 545 GLN A CD 1 ATOM 4376 O OE1 . GLN A 1 545 ? 6.255 -8.523 -2.732 1.00 46.10 ? 545 GLN A OE1 1 ATOM 4377 N NE2 . GLN A 1 545 ? 7.209 -6.862 -3.919 1.00 49.92 ? 545 GLN A NE2 1 ATOM 4378 N N . LYS A 1 546 ? 5.169 -1.699 -1.989 1.00 38.38 ? 546 LYS A N 1 ATOM 4379 C CA . LYS A 1 546 ? 5.433 -0.310 -2.319 1.00 37.68 ? 546 LYS A CA 1 ATOM 4380 C C . LYS A 1 546 ? 5.217 0.628 -1.128 1.00 36.94 ? 546 LYS A C 1 ATOM 4381 O O . LYS A 1 546 ? 5.473 1.833 -1.251 1.00 38.01 ? 546 LYS A O 1 ATOM 4382 C CB . LYS A 1 546 ? 4.499 0.155 -3.451 1.00 37.95 ? 546 LYS A CB 1 ATOM 4383 C CG . LYS A 1 546 ? 5.030 -0.066 -4.858 1.00 40.60 ? 546 LYS A CG 1 ATOM 4384 C CD . LYS A 1 546 ? 4.041 0.454 -5.927 1.00 44.22 ? 546 LYS A CD 1 ATOM 4385 C CE . LYS A 1 546 ? 4.419 -0.042 -7.371 1.00 47.95 ? 546 LYS A CE 1 ATOM 4386 N NZ . LYS A 1 546 ? 3.982 -1.474 -7.722 1.00 48.21 ? 546 LYS A NZ 1 ATOM 4387 N N . VAL A 1 547 ? 4.718 0.128 0.004 1.00 34.79 ? 547 VAL A N 1 ATOM 4388 C CA . VAL A 1 547 ? 4.445 1.017 1.140 1.00 32.84 ? 547 VAL A CA 1 ATOM 4389 C C . VAL A 1 547 ? 5.752 1.565 1.674 1.00 31.52 ? 547 VAL A C 1 ATOM 4390 O O . VAL A 1 547 ? 6.804 0.944 1.571 1.00 31.26 ? 547 VAL A O 1 ATOM 4391 C CB . VAL A 1 547 ? 3.634 0.328 2.297 1.00 33.13 ? 547 VAL A CB 1 ATOM 4392 C CG1 . VAL A 1 547 ? 2.324 -0.279 1.789 1.00 33.69 ? 547 VAL A CG1 1 ATOM 4393 C CG2 . VAL A 1 547 ? 4.461 -0.722 3.022 1.00 31.51 ? 547 VAL A CG2 1 ATOM 4394 N N . SER A 1 548 ? 5.689 2.745 2.233 1.00 30.33 ? 548 SER A N 1 ATOM 4395 C CA . SER A 1 548 ? 6.876 3.332 2.800 1.00 29.85 ? 548 SER A CA 1 ATOM 4396 C C . SER A 1 548 ? 6.396 4.303 3.855 1.00 29.04 ? 548 SER A C 1 ATOM 4397 O O . SER A 1 548 ? 5.306 4.828 3.754 1.00 29.41 ? 548 SER A O 1 ATOM 4398 C CB . SER A 1 548 ? 7.674 4.049 1.721 1.00 29.98 ? 548 SER A CB 1 ATOM 4399 O OG . SER A 1 548 ? 7.053 5.281 1.374 1.00 30.46 ? 548 SER A OG 1 ATOM 4400 N N . PHE A 1 549 ? 7.189 4.523 4.881 1.00 28.09 ? 549 PHE A N 1 ATOM 4401 C CA . PHE A 1 549 ? 6.774 5.444 5.903 1.00 27.64 ? 549 PHE A CA 1 ATOM 4402 C C . PHE A 1 549 ? 6.707 6.849 5.347 1.00 26.95 ? 549 PHE A C 1 ATOM 4403 O O . PHE A 1 549 ? 5.918 7.642 5.807 1.00 26.69 ? 549 PHE A O 1 ATOM 4404 C CB . PHE A 1 549 ? 7.674 5.357 7.136 1.00 28.09 ? 549 PHE A CB 1 ATOM 4405 C CG . PHE A 1 549 ? 7.083 6.004 8.349 1.00 28.13 ? 549 PHE A CG 1 ATOM 4406 C CD1 . PHE A 1 549 ? 6.237 5.324 9.149 1.00 27.48 ? 549 PHE A CD1 1 ATOM 4407 C CD2 . PHE A 1 549 ? 7.380 7.316 8.672 1.00 29.24 ? 549 PHE A CD2 1 ATOM 4408 C CE1 . PHE A 1 549 ? 5.706 5.928 10.249 1.00 30.35 ? 549 PHE A CE1 1 ATOM 4409 C CE2 . PHE A 1 549 ? 6.837 7.916 9.770 1.00 28.10 ? 549 PHE A CE2 1 ATOM 4410 C CZ . PHE A 1 549 ? 6.006 7.227 10.554 1.00 28.41 ? 549 PHE A CZ 1 ATOM 4411 N N . SER A 1 550 ? 7.499 7.158 4.336 1.00 27.10 ? 550 SER A N 1 ATOM 4412 C CA . SER A 1 550 ? 7.403 8.487 3.702 1.00 27.66 ? 550 SER A CA 1 ATOM 4413 C C . SER A 1 550 ? 6.018 8.715 3.084 1.00 27.20 ? 550 SER A C 1 ATOM 4414 O O . SER A 1 550 ? 5.378 9.751 3.262 1.00 26.79 ? 550 SER A O 1 ATOM 4415 C CB . SER A 1 550 ? 8.460 8.638 2.621 1.00 27.88 ? 550 SER A CB 1 ATOM 4416 O OG . SER A 1 550 ? 9.695 8.111 3.063 1.00 30.88 ? 550 SER A OG 1 ATOM 4417 N N . ARG A 1 551 ? 5.542 7.734 2.344 1.00 27.43 ? 551 ARG A N 1 ATOM 4418 C CA . ARG A 1 551 ? 4.219 7.872 1.788 1.00 27.29 ? 551 ARG A CA 1 ATOM 4419 C C . ARG A 1 551 ? 3.280 8.148 2.942 1.00 27.30 ? 551 ARG A C 1 ATOM 4420 O O . ARG A 1 551 ? 2.486 9.095 2.896 1.00 27.56 ? 551 ARG A O 1 ATOM 4421 C CB . ARG A 1 551 ? 3.805 6.585 1.100 1.00 27.40 ? 551 ARG A CB 1 ATOM 4422 C CG . ARG A 1 551 ? 2.536 6.680 0.292 1.00 27.43 ? 551 ARG A CG 1 ATOM 4423 C CD . ARG A 1 551 ? 2.668 7.514 -0.928 1.00 28.36 ? 551 ARG A CD 1 ATOM 4424 N NE . ARG A 1 551 ? 1.882 8.731 -0.778 1.00 30.62 ? 551 ARG A NE 1 ATOM 4425 C CZ . ARG A 1 551 ? 2.031 9.829 -1.508 1.00 29.37 ? 551 ARG A CZ 1 ATOM 4426 N NH1 . ARG A 1 551 ? 2.948 9.903 -2.480 1.00 30.51 ? 551 ARG A NH1 1 ATOM 4427 N NH2 . ARG A 1 551 ? 1.243 10.851 -1.260 1.00 28.73 ? 551 ARG A NH2 1 ATOM 4428 N N . LEU A 1 552 ? 3.372 7.328 3.989 1.00 26.65 ? 552 LEU A N 1 ATOM 4429 C CA . LEU A 1 552 ? 2.428 7.450 5.079 1.00 26.38 ? 552 LEU A CA 1 ATOM 4430 C C . LEU A 1 552 ? 2.373 8.868 5.535 1.00 26.74 ? 552 LEU A C 1 ATOM 4431 O O . LEU A 1 552 ? 1.319 9.377 5.849 1.00 26.24 ? 552 LEU A O 1 ATOM 4432 C CB . LEU A 1 552 ? 2.782 6.546 6.227 1.00 26.31 ? 552 LEU A CB 1 ATOM 4433 C CG . LEU A 1 552 ? 1.589 6.522 7.161 1.00 26.10 ? 552 LEU A CG 1 ATOM 4434 C CD1 . LEU A 1 552 ? 1.096 5.109 7.297 1.00 25.84 ? 552 LEU A CD1 1 ATOM 4435 C CD2 . LEU A 1 552 ? 1.966 7.120 8.513 1.00 27.50 ? 552 LEU A CD2 1 ATOM 4436 N N . ILE A 1 553 ? 3.530 9.518 5.539 1.00 27.74 ? 553 ILE A N 1 ATOM 4437 C CA . ILE A 1 553 ? 3.605 10.910 5.940 1.00 28.29 ? 553 ILE A CA 1 ATOM 4438 C C . ILE A 1 553 ? 2.869 11.787 4.954 1.00 28.50 ? 553 ILE A C 1 ATOM 4439 O O . ILE A 1 553 ? 2.014 12.570 5.345 1.00 28.54 ? 553 ILE A O 1 ATOM 4440 C CB . ILE A 1 553 ? 5.047 11.357 6.095 1.00 28.34 ? 553 ILE A CB 1 ATOM 4441 C CG1 . ILE A 1 553 ? 5.660 10.658 7.306 1.00 28.43 ? 553 ILE A CG1 1 ATOM 4442 C CG2 . ILE A 1 553 ? 5.107 12.870 6.271 1.00 27.80 ? 553 ILE A CG2 1 ATOM 4443 C CD1 . ILE A 1 553 ? 7.152 10.943 7.487 1.00 30.43 ? 553 ILE A CD1 1 ATOM 4444 N N . CYS A 1 554 ? 3.179 11.627 3.677 1.00 29.02 ? 554 CYS A N 1 ATOM 4445 C CA . CYS A 1 554 ? 2.561 12.446 2.635 1.00 29.84 ? 554 CYS A CA 1 ATOM 4446 C C . CYS A 1 554 ? 1.043 12.377 2.659 1.00 29.70 ? 554 CYS A C 1 ATOM 4447 O O . CYS A 1 554 ? 0.374 13.376 2.574 1.00 30.58 ? 554 CYS A O 1 ATOM 4448 C CB . CYS A 1 554 ? 3.077 12.027 1.265 1.00 29.64 ? 554 CYS A CB 1 ATOM 4449 S SG . CYS A 1 554 ? 4.840 12.299 1.087 1.00 34.39 ? 554 CYS A SG 1 ATOM 4450 N N . ASP A 1 555 ? 0.489 11.196 2.832 1.00 29.66 ? 555 ASP A N 1 ATOM 4451 C CA . ASP A 1 555 ? -0.936 11.053 2.739 1.00 29.25 ? 555 ASP A CA 1 ATOM 4452 C C . ASP A 1 555 ? -1.677 11.501 3.956 1.00 29.35 ? 555 ASP A C 1 ATOM 4453 O O . ASP A 1 555 ? -2.896 11.587 3.894 1.00 29.82 ? 555 ASP A O 1 ATOM 4454 C CB . ASP A 1 555 ? -1.272 9.593 2.516 1.00 29.77 ? 555 ASP A CB 1 ATOM 4455 C CG . ASP A 1 555 ? -0.744 9.058 1.182 1.00 30.62 ? 555 ASP A CG 1 ATOM 4456 O OD1 . ASP A 1 555 ? -0.481 9.904 0.276 1.00 31.32 ? 555 ASP A OD1 1 ATOM 4457 O OD2 . ASP A 1 555 ? -0.577 7.828 0.959 1.00 29.78 ? 555 ASP A OD2 1 ATOM 4458 N N . ASN A 1 556 ? -0.968 11.792 5.054 1.00 28.98 ? 556 ASN A N 1 ATOM 4459 C CA . ASN A 1 556 ? -1.624 12.015 6.339 1.00 28.40 ? 556 ASN A CA 1 ATOM 4460 C C . ASN A 1 556 ? -1.216 13.271 7.113 1.00 28.52 ? 556 ASN A C 1 ATOM 4461 O O . ASN A 1 556 ? -1.579 13.455 8.286 1.00 27.59 ? 556 ASN A O 1 ATOM 4462 C CB . ASN A 1 556 ? -1.434 10.764 7.217 1.00 28.03 ? 556 ASN A CB 1 ATOM 4463 C CG . ASN A 1 556 ? -2.198 9.533 6.689 1.00 28.47 ? 556 ASN A CG 1 ATOM 4464 O OD1 . ASN A 1 556 ? -3.416 9.443 6.809 1.00 31.45 ? 556 ASN A OD1 1 ATOM 4465 N ND2 . ASN A 1 556 ? -1.483 8.595 6.106 1.00 27.54 ? 556 ASN A ND2 1 ATOM 4466 N N . THR A 1 557 ? -0.457 14.135 6.459 1.00 29.11 ? 557 THR A N 1 ATOM 4467 C CA . THR A 1 557 ? -0.023 15.394 7.067 1.00 30.29 ? 557 THR A CA 1 ATOM 4468 C C . THR A 1 557 ? 0.109 16.407 5.975 1.00 30.93 ? 557 THR A C 1 ATOM 4469 O O . THR A 1 557 ? -0.091 16.089 4.837 1.00 31.04 ? 557 THR A O 1 ATOM 4470 C CB . THR A 1 557 ? 1.384 15.290 7.723 1.00 30.27 ? 557 THR A CB 1 ATOM 4471 O OG1 . THR A 1 557 ? 2.351 14.950 6.716 1.00 29.65 ? 557 THR A OG1 1 ATOM 4472 C CG2 . THR A 1 557 ? 1.448 14.188 8.784 1.00 28.26 ? 557 THR A CG2 1 ATOM 4473 N N . HIS A 1 558 ? 0.495 17.627 6.311 1.00 32.52 ? 558 HIS A N 1 ATOM 4474 C CA . HIS A 1 558 ? 0.717 18.624 5.262 1.00 33.77 ? 558 HIS A CA 1 ATOM 4475 C C . HIS A 1 558 ? 2.196 18.841 5.017 1.00 33.30 ? 558 HIS A C 1 ATOM 4476 O O . HIS A 1 558 ? 2.661 19.970 4.859 1.00 34.55 ? 558 HIS A O 1 ATOM 4477 C CB . HIS A 1 558 ? -0.038 19.929 5.549 1.00 34.08 ? 558 HIS A CB 1 ATOM 4478 C CG . HIS A 1 558 ? -1.529 19.757 5.544 1.00 37.61 ? 558 HIS A CG 1 ATOM 4479 N ND1 . HIS A 1 558 ? -2.320 20.077 6.626 1.00 40.39 ? 558 HIS A ND1 1 ATOM 4480 C CD2 . HIS A 1 558 ? -2.368 19.254 4.598 1.00 40.14 ? 558 HIS A CD2 1 ATOM 4481 C CE1 . HIS A 1 558 ? -3.585 19.796 6.339 1.00 42.22 ? 558 HIS A CE1 1 ATOM 4482 N NE2 . HIS A 1 558 ? -3.641 19.291 5.117 1.00 40.22 ? 558 HIS A NE2 1 ATOM 4483 N N . ILE A 1 559 ? 2.940 17.755 4.995 1.00 32.51 ? 559 ILE A N 1 ATOM 4484 C CA . ILE A 1 559 ? 4.352 17.846 4.698 1.00 32.34 ? 559 ILE A CA 1 ATOM 4485 C C . ILE A 1 559 ? 4.430 17.426 3.252 1.00 32.90 ? 559 ILE A C 1 ATOM 4486 O O . ILE A 1 559 ? 3.713 16.509 2.829 1.00 32.28 ? 559 ILE A O 1 ATOM 4487 C CB . ILE A 1 559 ? 5.181 16.928 5.618 1.00 31.59 ? 559 ILE A CB 1 ATOM 4488 C CG1 . ILE A 1 559 ? 4.762 17.142 7.075 1.00 31.51 ? 559 ILE A CG1 1 ATOM 4489 C CG2 . ILE A 1 559 ? 6.639 17.200 5.444 1.00 30.95 ? 559 ILE A CG2 1 ATOM 4490 C CD1 . ILE A 1 559 ? 5.445 16.268 8.066 1.00 30.88 ? 559 ILE A CD1 1 ATOM 4491 N N . THR A 1 560 ? 5.278 18.108 2.487 1.00 33.47 ? 560 THR A N 1 ATOM 4492 C CA . THR A 1 560 ? 5.392 17.838 1.051 1.00 33.86 ? 560 THR A CA 1 ATOM 4493 C C . THR A 1 560 ? 6.827 17.516 0.684 1.00 34.03 ? 560 THR A C 1 ATOM 4494 O O . THR A 1 560 ? 7.151 17.210 -0.475 1.00 34.45 ? 560 THR A O 1 ATOM 4495 C CB . THR A 1 560 ? 4.902 19.053 0.229 1.00 34.21 ? 560 THR A CB 1 ATOM 4496 O OG1 . THR A 1 560 ? 5.751 20.194 0.461 1.00 35.54 ? 560 THR A OG1 1 ATOM 4497 C CG2 . THR A 1 560 ? 3.523 19.521 0.703 1.00 33.08 ? 560 THR A CG2 1 ATOM 4498 N N . LYS A 1 561 ? 7.700 17.636 1.674 1.00 34.08 ? 561 LYS A N 1 ATOM 4499 C CA . LYS A 1 561 ? 9.078 17.229 1.482 1.00 33.97 ? 561 LYS A CA 1 ATOM 4500 C C . LYS A 1 561 ? 9.383 16.130 2.493 1.00 33.51 ? 561 LYS A C 1 ATOM 4501 O O . LYS A 1 561 ? 9.253 16.327 3.696 1.00 33.12 ? 561 LYS A O 1 ATOM 4502 C CB . LYS A 1 561 ? 10.053 18.386 1.616 1.00 34.08 ? 561 LYS A CB 1 ATOM 4503 C CG . LYS A 1 561 ? 9.408 19.730 1.383 1.00 37.16 ? 561 LYS A CG 1 ATOM 4504 C CD . LYS A 1 561 ? 10.169 20.611 0.397 1.00 38.84 ? 561 LYS A CD 1 ATOM 4505 C CE . LYS A 1 561 ? 9.366 20.769 -0.887 1.00 40.75 ? 561 LYS A CE 1 ATOM 4506 N NZ . LYS A 1 561 ? 9.536 19.628 -1.836 1.00 42.09 ? 561 LYS A NZ 1 ATOM 4507 N N . VAL A 1 562 ? 9.777 14.971 1.979 1.00 33.29 ? 562 VAL A N 1 ATOM 4508 C CA . VAL A 1 562 ? 10.127 13.831 2.801 1.00 33.53 ? 562 VAL A CA 1 ATOM 4509 C C . VAL A 1 562 ? 11.409 13.199 2.265 1.00 33.44 ? 562 VAL A C 1 ATOM 4510 O O . VAL A 1 562 ? 11.814 13.439 1.129 1.00 34.69 ? 562 VAL A O 1 ATOM 4511 C CB . VAL A 1 562 ? 8.971 12.785 2.802 1.00 33.70 ? 562 VAL A CB 1 ATOM 4512 C CG1 . VAL A 1 562 ? 7.728 13.319 3.543 1.00 33.86 ? 562 VAL A CG1 1 ATOM 4513 C CG2 . VAL A 1 562 ? 8.594 12.379 1.381 1.00 34.19 ? 562 VAL A CG2 1 ATOM 4514 N N . PRO A 1 563 ? 12.098 12.431 3.085 1.00 33.00 ? 563 PRO A N 1 ATOM 4515 C CA . PRO A 1 563 ? 13.193 11.605 2.583 1.00 32.70 ? 563 PRO A CA 1 ATOM 4516 C C . PRO A 1 563 ? 12.644 10.268 2.057 1.00 32.65 ? 563 PRO A C 1 ATOM 4517 O O . PRO A 1 563 ? 11.540 9.901 2.440 1.00 32.86 ? 563 PRO A O 1 ATOM 4518 C CB . PRO A 1 563 ? 14.006 11.381 3.833 1.00 32.92 ? 563 PRO A CB 1 ATOM 4519 C CG . PRO A 1 563 ? 12.932 11.195 4.833 1.00 33.44 ? 563 PRO A CG 1 ATOM 4520 C CD . PRO A 1 563 ? 12.004 12.369 4.552 1.00 33.24 ? 563 PRO A CD 1 ATOM 4521 N N . LEU A 1 564 ? 13.384 9.566 1.200 1.00 32.26 ? 564 LEU A N 1 ATOM 4522 C CA . LEU A 1 564 ? 12.894 8.328 0.641 1.00 31.94 ? 564 LEU A CA 1 ATOM 4523 C C . LEU A 1 564 ? 13.089 7.228 1.636 1.00 31.83 ? 564 LEU A C 1 ATOM 4524 O O . LEU A 1 564 ? 12.284 6.301 1.688 1.00 33.12 ? 564 LEU A O 1 ATOM 4525 C CB . LEU A 1 564 ? 13.642 7.941 -0.633 1.00 32.14 ? 564 LEU A CB 1 ATOM 4526 C CG . LEU A 1 564 ? 13.007 8.155 -2.007 1.00 32.48 ? 564 LEU A CG 1 ATOM 4527 C CD1 . LEU A 1 564 ? 11.499 8.429 -1.872 1.00 33.97 ? 564 LEU A CD1 1 ATOM 4528 C CD2 . LEU A 1 564 ? 13.708 9.268 -2.750 1.00 32.89 ? 564 LEU A CD2 1 ATOM 4529 N N . HIS A 1 565 ? 14.207 7.266 2.358 1.00 30.92 ? 565 HIS A N 1 ATOM 4530 C CA . HIS A 1 565 ? 14.530 6.278 3.391 1.00 29.69 ? 565 HIS A CA 1 ATOM 4531 C C . HIS A 1 565 ? 14.485 6.994 4.705 1.00 28.83 ? 565 HIS A C 1 ATOM 4532 O O . HIS A 1 565 ? 15.458 7.598 5.086 1.00 28.78 ? 565 HIS A O 1 ATOM 4533 C CB . HIS A 1 565 ? 15.933 5.773 3.206 1.00 30.04 ? 565 HIS A CB 1 ATOM 4534 C CG . HIS A 1 565 ? 16.226 5.349 1.809 1.00 32.74 ? 565 HIS A CG 1 ATOM 4535 N ND1 . HIS A 1 565 ? 15.565 4.312 1.192 1.00 33.91 ? 565 HIS A ND1 1 ATOM 4536 C CD2 . HIS A 1 565 ? 17.071 5.867 0.889 1.00 35.49 ? 565 HIS A CD2 1 ATOM 4537 C CE1 . HIS A 1 565 ? 16.017 4.186 -0.041 1.00 36.09 ? 565 HIS A CE1 1 ATOM 4538 N NE2 . HIS A 1 565 ? 16.928 5.121 -0.251 1.00 36.72 ? 565 HIS A NE2 1 ATOM 4539 N N . ALA A 1 566 ? 13.371 6.893 5.419 1.00 27.81 ? 566 ALA A N 1 ATOM 4540 C CA . ALA A 1 566 ? 13.167 7.720 6.581 1.00 26.77 ? 566 ALA A CA 1 ATOM 4541 C C . ALA A 1 566 ? 13.975 7.396 7.789 1.00 26.67 ? 566 ALA A C 1 ATOM 4542 O O . ALA A 1 566 ? 14.186 8.284 8.629 1.00 26.72 ? 566 ALA A O 1 ATOM 4543 C CB . ALA A 1 566 ? 11.749 7.759 6.947 1.00 27.07 ? 566 ALA A CB 1 ATOM 4544 N N . PHE A 1 567 ? 14.436 6.154 7.884 1.00 25.90 ? 567 PHE A N 1 ATOM 4545 C CA . PHE A 1 567 ? 15.142 5.696 9.087 1.00 25.84 ? 567 PHE A CA 1 ATOM 4546 C C . PHE A 1 567 ? 16.629 6.058 9.154 1.00 25.65 ? 567 PHE A C 1 ATOM 4547 O O . PHE A 1 567 ? 17.201 6.062 10.232 1.00 25.23 ? 567 PHE A O 1 ATOM 4548 C CB . PHE A 1 567 ? 14.978 4.188 9.314 1.00 25.69 ? 567 PHE A CB 1 ATOM 4549 C CG . PHE A 1 567 ? 13.585 3.758 9.557 1.00 25.63 ? 567 PHE A CG 1 ATOM 4550 C CD1 . PHE A 1 567 ? 13.045 3.810 10.794 1.00 26.44 ? 567 PHE A CD1 1 ATOM 4551 C CD2 . PHE A 1 567 ? 12.812 3.265 8.544 1.00 27.41 ? 567 PHE A CD2 1 ATOM 4552 C CE1 . PHE A 1 567 ? 11.738 3.378 11.018 1.00 25.87 ? 567 PHE A CE1 1 ATOM 4553 C CE2 . PHE A 1 567 ? 11.517 2.857 8.782 1.00 26.98 ? 567 PHE A CE2 1 ATOM 4554 C CZ . PHE A 1 567 ? 10.997 2.903 10.026 1.00 24.35 ? 567 PHE A CZ 1 ATOM 4555 N N . GLN A 1 568 ? 17.262 6.353 8.030 1.00 25.78 ? 568 GLN A N 1 ATOM 4556 C CA . GLN A 1 568 ? 18.652 6.815 8.089 1.00 27.26 ? 568 GLN A CA 1 ATOM 4557 C C . GLN A 1 568 ? 18.689 8.330 8.306 1.00 27.47 ? 568 GLN A C 1 ATOM 4558 O O . GLN A 1 568 ? 17.675 9.008 8.159 1.00 27.07 ? 568 GLN A O 1 ATOM 4559 C CB . GLN A 1 568 ? 19.439 6.422 6.843 1.00 27.48 ? 568 GLN A CB 1 ATOM 4560 C CG . GLN A 1 568 ? 18.609 6.455 5.590 1.00 31.60 ? 568 GLN A CG 1 ATOM 4561 C CD . GLN A 1 568 ? 19.418 6.762 4.356 1.00 36.70 ? 568 GLN A CD 1 ATOM 4562 O OE1 . GLN A 1 568 ? 19.682 5.866 3.523 1.00 38.53 ? 568 GLN A OE1 1 ATOM 4563 N NE2 . GLN A 1 568 ? 19.822 8.036 4.221 1.00 38.46 ? 568 GLN A NE2 1 ATOM 4564 N N . ALA A 1 569 ? 19.836 8.871 8.696 1.00 28.21 ? 569 ALA A N 1 ATOM 4565 C CA . ALA A 1 569 ? 19.898 10.319 8.932 1.00 29.51 ? 569 ALA A CA 1 ATOM 4566 C C . ALA A 1 569 ? 19.838 11.091 7.619 1.00 30.70 ? 569 ALA A C 1 ATOM 4567 O O . ALA A 1 569 ? 20.558 10.763 6.682 1.00 31.51 ? 569 ALA A O 1 ATOM 4568 C CB . ALA A 1 569 ? 21.138 10.692 9.722 1.00 29.07 ? 569 ALA A CB 1 ATOM 4569 N N . ASN A 1 570 ? 18.991 12.111 7.555 1.00 31.97 ? 570 ASN A N 1 ATOM 4570 C CA . ASN A 1 570 ? 18.760 12.847 6.329 1.00 33.70 ? 570 ASN A CA 1 ATOM 4571 C C . ASN A 1 570 ? 18.833 14.343 6.497 1.00 35.22 ? 570 ASN A C 1 ATOM 4572 O O . ASN A 1 570 ? 18.089 14.917 7.294 1.00 34.93 ? 570 ASN A O 1 ATOM 4573 C CB . ASN A 1 570 ? 17.375 12.519 5.832 1.00 33.63 ? 570 ASN A CB 1 ATOM 4574 C CG . ASN A 1 570 ? 17.235 11.092 5.467 1.00 35.12 ? 570 ASN A CG 1 ATOM 4575 O OD1 . ASN A 1 570 ? 16.424 10.358 6.051 1.00 34.74 ? 570 ASN A OD1 1 ATOM 4576 N ND2 . ASN A 1 570 ? 18.028 10.665 4.482 1.00 36.72 ? 570 ASN A ND2 1 ATOM 4577 N N . ASN A 1 571 ? 19.692 14.993 5.720 1.00 37.35 ? 571 ASN A N 1 ATOM 4578 C CA . ASN A 1 571 ? 19.816 16.454 5.810 1.00 39.54 ? 571 ASN A CA 1 ATOM 4579 C C . ASN A 1 571 ? 18.909 17.178 4.846 1.00 39.88 ? 571 ASN A C 1 ATOM 4580 O O . ASN A 1 571 ? 18.876 16.847 3.666 1.00 40.72 ? 571 ASN A O 1 ATOM 4581 C CB . ASN A 1 571 ? 21.271 16.896 5.623 1.00 40.10 ? 571 ASN A CB 1 ATOM 4582 C CG . ASN A 1 571 ? 22.181 16.328 6.703 1.00 43.08 ? 571 ASN A CG 1 ATOM 4583 O OD1 . ASN A 1 571 ? 22.127 16.757 7.853 1.00 45.82 ? 571 ASN A OD1 1 ATOM 4584 N ND2 . ASN A 1 571 ? 22.985 15.318 6.346 1.00 47.66 ? 571 ASN A ND2 1 ATOM 4585 N N . TYR A 1 572 ? 18.140 18.129 5.354 1.00 40.45 ? 572 TYR A N 1 ATOM 4586 C CA . TYR A 1 572 ? 17.281 18.963 4.513 1.00 41.38 ? 572 TYR A CA 1 ATOM 4587 C C . TYR A 1 572 ? 18.147 20.076 3.950 1.00 41.72 ? 572 TYR A C 1 ATOM 4588 O O . TYR A 1 572 ? 18.932 20.659 4.694 1.00 42.30 ? 572 TYR A O 1 ATOM 4589 C CB . TYR A 1 572 ? 16.186 19.588 5.359 1.00 41.57 ? 572 TYR A CB 1 ATOM 4590 C CG . TYR A 1 572 ? 15.223 20.358 4.543 1.00 43.46 ? 572 TYR A CG 1 ATOM 4591 C CD1 . TYR A 1 572 ? 14.247 19.695 3.825 1.00 45.14 ? 572 TYR A CD1 1 ATOM 4592 C CD2 . TYR A 1 572 ? 15.293 21.750 4.456 1.00 44.63 ? 572 TYR A CD2 1 ATOM 4593 C CE1 . TYR A 1 572 ? 13.363 20.382 3.038 1.00 46.72 ? 572 TYR A CE1 1 ATOM 4594 C CE2 . TYR A 1 572 ? 14.402 22.455 3.674 1.00 45.11 ? 572 TYR A CE2 1 ATOM 4595 C CZ . TYR A 1 572 ? 13.440 21.760 2.962 1.00 46.51 ? 572 TYR A CZ 1 ATOM 4596 O OH . TYR A 1 572 ? 12.521 22.410 2.172 1.00 49.39 ? 572 TYR A OH 1 ATOM 4597 N N . PRO A 1 573 ? 18.027 20.408 2.669 1.00 42.04 ? 573 PRO A N 1 ATOM 4598 C CA . PRO A 1 573 ? 17.079 19.808 1.732 1.00 42.46 ? 573 PRO A CA 1 ATOM 4599 C C . PRO A 1 573 ? 17.664 18.734 0.825 1.00 43.19 ? 573 PRO A C 1 ATOM 4600 O O . PRO A 1 573 ? 16.897 18.077 0.116 1.00 43.05 ? 573 PRO A O 1 ATOM 4601 C CB . PRO A 1 573 ? 16.703 21.003 0.848 1.00 42.70 ? 573 PRO A CB 1 ATOM 4602 C CG . PRO A 1 573 ? 17.763 22.108 1.160 1.00 41.33 ? 573 PRO A CG 1 ATOM 4603 C CD . PRO A 1 573 ? 18.805 21.489 2.040 1.00 41.85 ? 573 PRO A CD 1 ATOM 4604 N N . HIS A 1 574 ? 18.978 18.535 0.843 1.00 44.14 ? 574 HIS A N 1 ATOM 4605 C CA . HIS A 1 574 ? 19.594 17.617 -0.113 1.00 45.16 ? 574 HIS A CA 1 ATOM 4606 C C . HIS A 1 574 ? 18.907 16.255 -0.202 1.00 44.23 ? 574 HIS A C 1 ATOM 4607 O O . HIS A 1 574 ? 18.638 15.775 -1.288 1.00 44.54 ? 574 HIS A O 1 ATOM 4608 C CB . HIS A 1 574 ? 21.100 17.478 0.124 1.00 46.23 ? 574 HIS A CB 1 ATOM 4609 C CG . HIS A 1 574 ? 21.708 16.338 -0.634 1.00 51.20 ? 574 HIS A CG 1 ATOM 4610 N ND1 . HIS A 1 574 ? 22.232 16.483 -1.904 1.00 54.83 ? 574 HIS A ND1 1 ATOM 4611 C CD2 . HIS A 1 574 ? 21.832 15.022 -0.324 1.00 54.58 ? 574 HIS A CD2 1 ATOM 4612 C CE1 . HIS A 1 574 ? 22.673 15.310 -2.331 1.00 56.18 ? 574 HIS A CE1 1 ATOM 4613 N NE2 . HIS A 1 574 ? 22.433 14.405 -1.395 1.00 55.37 ? 574 HIS A NE2 1 ATOM 4614 N N . ASP A 1 575 ? 18.595 15.651 0.940 1.00 43.21 ? 575 ASP A N 1 ATOM 4615 C CA . ASP A 1 575 ? 17.983 14.317 0.981 1.00 41.78 ? 575 ASP A CA 1 ATOM 4616 C C . ASP A 1 575 ? 16.461 14.332 0.900 1.00 41.07 ? 575 ASP A C 1 ATOM 4617 O O . ASP A 1 575 ? 15.818 13.308 1.097 1.00 40.50 ? 575 ASP A O 1 ATOM 4618 C CB . ASP A 1 575 ? 18.356 13.630 2.285 1.00 41.58 ? 575 ASP A CB 1 ATOM 4619 C CG . ASP A 1 575 ? 19.829 13.410 2.424 1.00 41.11 ? 575 ASP A CG 1 ATOM 4620 O OD1 . ASP A 1 575 ? 20.505 13.146 1.407 1.00 38.21 ? 575 ASP A OD1 1 ATOM 4621 O OD2 . ASP A 1 575 ? 20.393 13.477 3.534 1.00 42.69 ? 575 ASP A OD2 1 ATOM 4622 N N . PHE A 1 576 ? 15.885 15.493 0.605 1.00 40.57 ? 576 PHE A N 1 ATOM 4623 C CA . PHE A 1 576 ? 14.436 15.653 0.680 1.00 40.04 ? 576 PHE A CA 1 ATOM 4624 C C . PHE A 1 576 ? 13.780 15.844 -0.675 1.00 40.43 ? 576 PHE A C 1 ATOM 4625 O O . PHE A 1 576 ? 14.087 16.774 -1.394 1.00 41.21 ? 576 PHE A O 1 ATOM 4626 C CB . PHE A 1 576 ? 14.092 16.821 1.625 1.00 39.46 ? 576 PHE A CB 1 ATOM 4627 C CG . PHE A 1 576 ? 14.100 16.438 3.082 1.00 36.66 ? 576 PHE A CG 1 ATOM 4628 C CD1 . PHE A 1 576 ? 15.288 16.257 3.764 1.00 32.81 ? 576 PHE A CD1 1 ATOM 4629 C CD2 . PHE A 1 576 ? 12.909 16.235 3.764 1.00 34.07 ? 576 PHE A CD2 1 ATOM 4630 C CE1 . PHE A 1 576 ? 15.279 15.883 5.097 1.00 30.86 ? 576 PHE A CE1 1 ATOM 4631 C CE2 . PHE A 1 576 ? 12.908 15.879 5.091 1.00 31.57 ? 576 PHE A CE2 1 ATOM 4632 C CZ . PHE A 1 576 ? 14.091 15.684 5.754 1.00 28.86 ? 576 PHE A CZ 1 ATOM 4633 N N . VAL A 1 577 ? 12.847 14.977 -1.014 1.00 41.08 ? 577 VAL A N 1 ATOM 4634 C CA . VAL A 1 577 ? 12.182 15.074 -2.302 1.00 41.94 ? 577 VAL A CA 1 ATOM 4635 C C . VAL A 1 577 ? 10.731 15.550 -2.165 1.00 42.71 ? 577 VAL A C 1 ATOM 4636 O O . VAL A 1 577 ? 10.252 15.813 -1.063 1.00 43.60 ? 577 VAL A O 1 ATOM 4637 C CB . VAL A 1 577 ? 12.211 13.731 -3.024 1.00 41.71 ? 577 VAL A CB 1 ATOM 4638 C CG1 . VAL A 1 577 ? 13.627 13.278 -3.245 1.00 39.27 ? 577 VAL A CG1 1 ATOM 4639 C CG2 . VAL A 1 577 ? 11.452 12.704 -2.211 1.00 42.86 ? 577 VAL A CG2 1 ATOM 4640 N N . ASP A 1 578 ? 10.032 15.681 -3.287 1.00 43.73 ? 578 ASP A N 1 ATOM 4641 C CA . ASP A 1 578 ? 8.626 16.099 -3.267 1.00 44.50 ? 578 ASP A CA 1 ATOM 4642 C C . ASP A 1 578 ? 7.715 14.919 -2.978 1.00 44.35 ? 578 ASP A C 1 ATOM 4643 O O . ASP A 1 578 ? 7.877 13.850 -3.567 1.00 44.23 ? 578 ASP A O 1 ATOM 4644 C CB . ASP A 1 578 ? 8.235 16.718 -4.606 1.00 44.59 ? 578 ASP A CB 1 ATOM 4645 C CG . ASP A 1 578 ? 6.992 17.551 -4.503 1.00 46.60 ? 578 ASP A CG 1 ATOM 4646 O OD1 . ASP A 1 578 ? 5.970 17.197 -5.137 1.00 46.97 ? 578 ASP A OD1 1 ATOM 4647 O OD2 . ASP A 1 578 ? 6.950 18.586 -3.796 1.00 50.03 ? 578 ASP A OD2 1 ATOM 4648 N N . CYS A 1 579 ? 6.757 15.109 -2.080 1.00 44.71 ? 579 CYS A N 1 ATOM 4649 C CA . CYS A 1 579 ? 5.810 14.049 -1.745 1.00 45.01 ? 579 CYS A CA 1 ATOM 4650 C C . CYS A 1 579 ? 5.191 13.489 -2.985 1.00 46.18 ? 579 CYS A C 1 ATOM 4651 O O . CYS A 1 579 ? 4.508 12.493 -2.965 1.00 47.17 ? 579 CYS A O 1 ATOM 4652 C CB . CYS A 1 579 ? 4.683 14.625 -0.912 1.00 43.64 ? 579 CYS A CB 1 ATOM 4653 S SG . CYS A 1 579 ? 4.892 14.276 0.833 1.00 42.08 ? 579 CYS A SG 1 ATOM 4654 N N . SER A 1 580 ? 5.503 14.106 -4.094 1.00 47.67 ? 580 SER A N 1 ATOM 4655 C CA . SER A 1 580 ? 4.627 13.997 -5.245 1.00 48.63 ? 580 SER A CA 1 ATOM 4656 C C . SER A 1 580 ? 5.274 13.198 -6.253 1.00 48.62 ? 580 SER A C 1 ATOM 4657 O O . SER A 1 580 ? 5.333 13.593 -7.419 1.00 48.90 ? 580 SER A O 1 ATOM 4658 C CB . SER A 1 580 ? 4.431 15.380 -5.822 1.00 49.00 ? 580 SER A CB 1 ATOM 4659 O OG . SER A 1 580 ? 3.177 15.874 -5.409 1.00 51.21 ? 580 SER A OG 1 ATOM 4660 N N . THR A 1 581 ? 5.654 12.019 -5.797 1.00 48.70 ? 581 THR A N 1 ATOM 4661 C CA . THR A 1 581 ? 6.775 11.365 -6.400 1.00 49.01 ? 581 THR A CA 1 ATOM 4662 C C . THR A 1 581 ? 7.001 10.066 -5.674 1.00 49.32 ? 581 THR A C 1 ATOM 4663 O O . THR A 1 581 ? 7.313 9.046 -6.281 1.00 50.49 ? 581 THR A O 1 ATOM 4664 C CB . THR A 1 581 ? 7.974 12.278 -6.092 1.00 49.03 ? 581 THR A CB 1 ATOM 4665 O OG1 . THR A 1 581 ? 7.815 13.544 -6.758 1.00 50.55 ? 581 THR A OG1 1 ATOM 4666 C CG2 . THR A 1 581 ? 9.266 11.732 -6.639 1.00 47.98 ? 581 THR A CG2 1 ATOM 4667 N N . VAL A 1 582 ? 6.863 10.099 -4.356 1.00 48.78 ? 582 VAL A N 1 ATOM 4668 C CA . VAL A 1 582 ? 6.963 8.878 -3.576 1.00 47.78 ? 582 VAL A CA 1 ATOM 4669 C C . VAL A 1 582 ? 5.886 7.867 -3.999 1.00 46.65 ? 582 VAL A C 1 ATOM 4670 O O . VAL A 1 582 ? 4.713 8.215 -4.112 1.00 45.93 ? 582 VAL A O 1 ATOM 4671 C CB . VAL A 1 582 ? 6.778 9.184 -2.090 1.00 48.39 ? 582 VAL A CB 1 ATOM 4672 C CG1 . VAL A 1 582 ? 7.216 7.993 -1.212 1.00 49.10 ? 582 VAL A CG1 1 ATOM 4673 C CG2 . VAL A 1 582 ? 7.527 10.442 -1.719 1.00 48.27 ? 582 VAL A CG2 1 ATOM 4674 N N . ASP A 1 583 ? 6.303 6.622 -4.225 1.00 45.79 ? 583 ASP A N 1 ATOM 4675 C CA . ASP A 1 583 ? 5.379 5.535 -4.557 1.00 44.99 ? 583 ASP A CA 1 ATOM 4676 C C . ASP A 1 583 ? 4.135 5.602 -3.676 1.00 43.86 ? 583 ASP A C 1 ATOM 4677 O O . ASP A 1 583 ? 4.231 5.711 -2.457 1.00 43.49 ? 583 ASP A O 1 ATOM 4678 C CB . ASP A 1 583 ? 6.060 4.163 -4.369 1.00 45.07 ? 583 ASP A CB 1 ATOM 4679 C CG . ASP A 1 583 ? 6.993 3.797 -5.516 1.00 46.87 ? 583 ASP A CG 1 ATOM 4680 O OD1 . ASP A 1 583 ? 7.648 4.706 -6.094 1.00 48.36 ? 583 ASP A OD1 1 ATOM 4681 O OD2 . ASP A 1 583 ? 7.142 2.612 -5.910 1.00 48.87 ? 583 ASP A OD2 1 ATOM 4682 N N . LYS A 1 584 ? 2.966 5.551 -4.298 1.00 42.84 ? 584 LYS A N 1 ATOM 4683 C CA . LYS A 1 584 ? 1.715 5.464 -3.556 1.00 41.99 ? 584 LYS A CA 1 ATOM 4684 C C . LYS A 1 584 ? 1.238 4.012 -3.465 1.00 40.71 ? 584 LYS A C 1 ATOM 4685 O O . LYS A 1 584 ? 1.527 3.206 -4.330 1.00 40.14 ? 584 LYS A O 1 ATOM 4686 C CB . LYS A 1 584 ? 0.636 6.308 -4.222 1.00 41.91 ? 584 LYS A CB 1 ATOM 4687 C CG . LYS A 1 584 ? 0.894 7.784 -4.110 1.00 44.24 ? 584 LYS A CG 1 ATOM 4688 C CD . LYS A 1 584 ? -0.307 8.583 -4.600 1.00 48.59 ? 584 LYS A CD 1 ATOM 4689 C CE . LYS A 1 584 ? -1.394 8.630 -3.536 1.00 51.30 ? 584 LYS A CE 1 ATOM 4690 N NZ . LYS A 1 584 ? -1.031 9.540 -2.400 1.00 53.49 ? 584 LYS A NZ 1 ATOM 4691 N N . LEU A 1 585 ? 0.507 3.689 -2.410 1.00 39.96 ? 585 LEU A N 1 ATOM 4692 C CA . LEU A 1 585 ? -0.081 2.366 -2.275 1.00 39.57 ? 585 LEU A CA 1 ATOM 4693 C C . LEU A 1 585 ? -1.270 2.239 -3.236 1.00 40.29 ? 585 LEU A C 1 ATOM 4694 O O . LEU A 1 585 ? -2.378 2.691 -2.927 1.00 40.37 ? 585 LEU A O 1 ATOM 4695 C CB . LEU A 1 585 ? -0.532 2.128 -0.818 1.00 39.31 ? 585 LEU A CB 1 ATOM 4696 C CG . LEU A 1 585 ? -1.537 1.003 -0.543 1.00 35.66 ? 585 LEU A CG 1 ATOM 4697 C CD1 . LEU A 1 585 ? -0.915 -0.310 -0.875 1.00 31.01 ? 585 LEU A CD1 1 ATOM 4698 C CD2 . LEU A 1 585 ? -2.025 1.066 0.904 1.00 34.30 ? 585 LEU A CD2 1 ATOM 4699 N N . ASP A 1 586 ? -1.037 1.630 -4.403 1.00 40.77 ? 586 ASP A N 1 ATOM 4700 C CA . ASP A 1 586 ? -2.110 1.454 -5.375 1.00 41.01 ? 586 ASP A CA 1 ATOM 4701 C C . ASP A 1 586 ? -3.145 0.554 -4.757 1.00 41.08 ? 586 ASP A C 1 ATOM 4702 O O . ASP A 1 586 ? -2.870 -0.545 -4.317 1.00 40.88 ? 586 ASP A O 1 ATOM 4703 C CB . ASP A 1 586 ? -1.658 0.928 -6.713 1.00 41.28 ? 586 ASP A CB 1 ATOM 4704 C CG . ASP A 1 586 ? -2.826 0.735 -7.605 1.00 41.67 ? 586 ASP A CG 1 ATOM 4705 O OD1 . ASP A 1 586 ? -3.715 1.609 -7.572 1.00 43.34 ? 586 ASP A OD1 1 ATOM 4706 O OD2 . ASP A 1 586 ? -2.987 -0.268 -8.301 1.00 42.22 ? 586 ASP A OD2 1 ATOM 4707 N N . LEU A 1 587 ? -4.364 1.032 -4.743 1.00 41.69 ? 587 LEU A N 1 ATOM 4708 C CA . LEU A 1 587 ? -5.348 0.434 -3.876 1.00 41.73 ? 587 LEU A CA 1 ATOM 4709 C C . LEU A 1 587 ? -6.541 -0.149 -4.581 1.00 42.11 ? 587 LEU A C 1 ATOM 4710 O O . LEU A 1 587 ? -7.622 -0.324 -4.023 1.00 42.17 ? 587 LEU A O 1 ATOM 4711 C CB . LEU A 1 587 ? -5.789 1.496 -2.911 1.00 41.23 ? 587 LEU A CB 1 ATOM 4712 C CG . LEU A 1 587 ? -5.861 0.898 -1.535 1.00 41.72 ? 587 LEU A CG 1 ATOM 4713 C CD1 . LEU A 1 587 ? -5.830 1.975 -0.522 1.00 41.80 ? 587 LEU A CD1 1 ATOM 4714 C CD2 . LEU A 1 587 ? -7.131 0.139 -1.406 1.00 45.24 ? 587 LEU A CD2 1 ATOM 4715 N N . SER A 1 588 ? -6.310 -0.448 -5.836 1.00 42.79 ? 588 SER A N 1 ATOM 4716 C CA . SER A 1 588 ? -7.322 -1.001 -6.685 1.00 43.60 ? 588 SER A CA 1 ATOM 4717 C C . SER A 1 588 ? -7.397 -2.518 -6.684 1.00 43.23 ? 588 SER A C 1 ATOM 4718 O O . SER A 1 588 ? -8.416 -3.025 -7.122 1.00 43.45 ? 588 SER A O 1 ATOM 4719 C CB . SER A 1 588 ? -7.111 -0.475 -8.107 1.00 44.36 ? 588 SER A CB 1 ATOM 4720 O OG . SER A 1 588 ? -5.748 -0.622 -8.501 1.00 44.75 ? 588 SER A OG 1 ATOM 4721 N N . PRO A 1 589 ? -6.303 -3.250 -6.452 1.00 43.34 ? 589 PRO A N 1 ATOM 4722 C CA . PRO A 1 589 ? -6.361 -4.700 -6.207 1.00 43.64 ? 589 PRO A CA 1 ATOM 4723 C C . PRO A 1 589 ? -7.402 -5.172 -5.198 1.00 44.58 ? 589 PRO A C 1 ATOM 4724 O O . PRO A 1 589 ? -7.599 -6.360 -5.000 1.00 44.45 ? 589 PRO A O 1 ATOM 4725 C CB . PRO A 1 589 ? -4.926 -5.052 -5.822 1.00 43.27 ? 589 PRO A CB 1 ATOM 4726 C CG . PRO A 1 589 ? -4.112 -4.105 -6.604 1.00 42.56 ? 589 PRO A CG 1 ATOM 4727 C CD . PRO A 1 589 ? -4.946 -2.871 -6.880 1.00 42.93 ? 589 PRO A CD 1 ATOM 4728 N N . TRP A 1 590 ? -8.106 -4.223 -4.617 1.00 46.23 ? 590 TRP A N 1 ATOM 4729 C CA . TRP A 1 590 ? -9.077 -4.513 -3.601 1.00 47.99 ? 590 TRP A CA 1 ATOM 4730 C C . TRP A 1 590 ? -10.495 -4.353 -4.107 1.00 51.00 ? 590 TRP A C 1 ATOM 4731 O O . TRP A 1 590 ? -11.428 -4.395 -3.327 1.00 50.92 ? 590 TRP A O 1 ATOM 4732 C CB . TRP A 1 590 ? -8.846 -3.595 -2.414 1.00 47.20 ? 590 TRP A CB 1 ATOM 4733 C CG . TRP A 1 590 ? -7.823 -4.115 -1.440 1.00 43.26 ? 590 TRP A CG 1 ATOM 4734 C CD1 . TRP A 1 590 ? -8.069 -4.778 -0.268 1.00 39.64 ? 590 TRP A CD1 1 ATOM 4735 C CD2 . TRP A 1 590 ? -6.395 -4.007 -1.544 1.00 39.02 ? 590 TRP A CD2 1 ATOM 4736 N NE1 . TRP A 1 590 ? -6.886 -5.070 0.367 1.00 38.24 ? 590 TRP A NE1 1 ATOM 4737 C CE2 . TRP A 1 590 ? -5.842 -4.617 -0.395 1.00 36.68 ? 590 TRP A CE2 1 ATOM 4738 C CE3 . TRP A 1 590 ? -5.529 -3.448 -2.482 1.00 36.90 ? 590 TRP A CE3 1 ATOM 4739 C CZ2 . TRP A 1 590 ? -4.474 -4.705 -0.174 1.00 33.27 ? 590 TRP A CZ2 1 ATOM 4740 C CZ3 . TRP A 1 590 ? -4.156 -3.513 -2.245 1.00 35.88 ? 590 TRP A CZ3 1 ATOM 4741 C CH2 . TRP A 1 590 ? -3.648 -4.136 -1.099 1.00 33.97 ? 590 TRP A CH2 1 ATOM 4742 N N . ALA A 1 591 ? -10.657 -4.178 -5.416 1.00 55.21 ? 591 ALA A N 1 ATOM 4743 C CA . ALA A 1 591 ? -11.986 -4.085 -6.041 1.00 59.01 ? 591 ALA A CA 1 ATOM 4744 C C . ALA A 1 591 ? -12.764 -5.428 -5.992 1.00 61.68 ? 591 ALA A C 1 ATOM 4745 O O . ALA A 1 591 ? -12.151 -6.490 -6.076 1.00 62.19 ? 591 ALA A O 1 ATOM 4746 C CB . ALA A 1 591 ? -11.846 -3.599 -7.467 1.00 58.40 ? 591 ALA A CB 1 ATOM 4747 N N . SER A 1 592 ? -14.099 -5.370 -5.861 1.00 65.25 ? 592 SER A N 1 ATOM 4748 C CA . SER A 1 592 ? -14.965 -6.571 -5.787 1.00 68.52 ? 592 SER A CA 1 ATOM 4749 C C . SER A 1 592 ? -16.220 -6.527 -6.709 1.00 71.08 ? 592 SER A C 1 ATOM 4750 O O . SER A 1 592 ? -17.168 -5.781 -6.451 1.00 71.55 ? 592 SER A O 1 ATOM 4751 C CB . SER A 1 592 ? -15.382 -6.820 -4.329 1.00 68.32 ? 592 SER A CB 1 ATOM 4752 O OG . SER A 1 592 ? -16.278 -7.913 -4.207 1.00 68.32 ? 592 SER A OG 1 ATOM 4753 N N . ARG A 1 593 ? -16.231 -7.344 -7.765 1.00 74.11 ? 593 ARG A N 1 ATOM 4754 C CA . ARG A 1 593 ? -17.336 -7.386 -8.741 1.00 77.18 ? 593 ARG A CA 1 ATOM 4755 C C . ARG A 1 593 ? -18.154 -8.701 -8.634 1.00 78.75 ? 593 ARG A C 1 ATOM 4756 O O . ARG A 1 593 ? -17.625 -9.800 -8.868 1.00 79.06 ? 593 ARG A O 1 ATOM 4757 C CB . ARG A 1 593 ? -16.768 -7.193 -10.155 1.00 77.41 ? 593 ARG A CB 1 ATOM 4758 C CG . ARG A 1 593 ? -15.458 -6.401 -10.215 1.00 79.78 ? 593 ARG A CG 1 ATOM 4759 C CD . ARG A 1 593 ? -14.548 -6.942 -11.321 1.00 83.92 ? 593 ARG A CD 1 ATOM 4760 N NE . ARG A 1 593 ? -15.063 -6.718 -12.671 1.00 86.86 ? 593 ARG A NE 1 ATOM 4761 C CZ . ARG A 1 593 ? -15.689 -7.656 -13.385 1.00 88.29 ? 593 ARG A CZ 1 ATOM 4762 N NH1 . ARG A 1 593 ? -15.865 -8.884 -12.894 1.00 88.83 ? 593 ARG A NH1 1 ATOM 4763 N NH2 . ARG A 1 593 ? -16.144 -7.359 -14.599 1.00 89.15 ? 593 ARG A NH2 1 ATOM 4764 N N . GLU A 1 594 ? -19.446 -8.601 -8.311 1.00 80.71 ? 594 GLU A N 1 ATOM 4765 C CA . GLU A 1 594 ? -20.414 -9.740 -8.101 1.00 82.37 ? 594 GLU A CA 1 ATOM 4766 C C . GLU A 1 594 ? -21.013 -10.528 -9.302 1.00 83.17 ? 594 GLU A C 1 ATOM 4767 O O . GLU A 1 594 ? -21.605 -11.577 -9.083 1.00 83.40 ? 594 GLU A O 1 ATOM 4768 C CB . GLU A 1 594 ? -21.708 -9.222 -7.439 1.00 82.57 ? 594 GLU A CB 1 ATOM 4769 C CG . GLU A 1 594 ? -21.611 -8.359 -6.176 1.00 83.92 ? 594 GLU A CG 1 ATOM 4770 C CD . GLU A 1 594 ? -20.735 -7.137 -6.269 1.00 85.67 ? 594 GLU A CD 1 ATOM 4771 O OE1 . GLU A 1 594 ? -21.083 -6.175 -6.991 1.00 86.05 ? 594 GLU A OE1 1 ATOM 4772 O OE2 . GLU A 1 594 ? -19.666 -7.146 -5.611 1.00 86.49 ? 594 GLU A OE2 1 ATOM 4773 N N . ASN A 1 595 ? -20.862 -10.036 -10.535 1.00 84.08 ? 595 ASN A N 1 ATOM 4774 C CA . ASN A 1 595 ? -21.386 -10.839 -11.630 1.00 84.82 ? 595 ASN A CA 1 ATOM 4775 C C . ASN A 1 595 ? -20.343 -11.886 -12.017 1.00 84.86 ? 595 ASN A C 1 ATOM 4776 O O . ASN A 1 595 ? -20.673 -13.013 -12.392 1.00 84.96 ? 595 ASN A O 1 ATOM 4777 C CB . ASN A 1 595 ? -21.718 -9.968 -12.868 1.00 85.09 ? 595 ASN A CB 1 ATOM 4778 C CG . ASN A 1 595 ? -23.210 -9.594 -12.997 1.00 86.31 ? 595 ASN A CG 1 ATOM 4779 O OD1 . ASN A 1 595 ? -24.072 -10.457 -13.233 1.00 87.81 ? 595 ASN A OD1 1 ATOM 4780 N ND2 . ASN A 1 595 ? -23.501 -8.306 -12.827 1.00 86.95 ? 595 ASN A ND2 1 HETATM 4781 C C1 . NAG B 2 . ? 23.485 4.757 6.528 1.00 47.95 ? 596 NAG A C1 1 HETATM 4782 C C2 . NAG B 2 . ? 24.680 4.257 5.723 1.00 53.93 ? 596 NAG A C2 1 HETATM 4783 C C3 . NAG B 2 . ? 24.224 3.571 4.408 1.00 58.10 ? 596 NAG A C3 1 HETATM 4784 C C4 . NAG B 2 . ? 23.210 2.443 4.641 1.00 61.27 ? 596 NAG A C4 1 HETATM 4785 C C5 . NAG B 2 . ? 22.103 3.099 5.470 1.00 57.59 ? 596 NAG A C5 1 HETATM 4786 C C6 . NAG B 2 . ? 20.892 2.195 5.712 1.00 57.22 ? 596 NAG A C6 1 HETATM 4787 C C7 . NAG B 2 . ? 26.883 5.272 5.985 1.00 52.50 ? 596 NAG A C7 1 HETATM 4788 C C8 . NAG B 2 . ? 27.831 6.347 5.535 1.00 51.97 ? 596 NAG A C8 1 HETATM 4789 N N2 . NAG B 2 . ? 25.629 5.347 5.519 1.00 52.41 ? 596 NAG A N2 1 HETATM 4790 O O3 . NAG B 2 . ? 25.304 3.030 3.665 1.00 59.72 ? 596 NAG A O3 1 HETATM 4791 O O4 . NAG B 2 . ? 22.818 1.914 3.362 1.00 68.93 ? 596 NAG A O4 1 HETATM 4792 O O5 . NAG B 2 . ? 22.641 3.628 6.687 1.00 52.59 ? 596 NAG A O5 1 HETATM 4793 O O6 . NAG B 2 . ? 21.225 1.108 6.537 1.00 58.53 ? 596 NAG A O6 1 HETATM 4794 O O7 . NAG B 2 . ? 27.277 4.378 6.750 1.00 51.79 ? 596 NAG A O7 1 HETATM 4795 C C1 . NAG C 2 . ? 22.190 0.651 3.233 1.00 76.17 ? 597 NAG A C1 1 HETATM 4796 C C2 . NAG C 2 . ? 21.316 0.732 1.969 1.00 79.70 ? 597 NAG A C2 1 HETATM 4797 C C3 . NAG C 2 . ? 21.716 -0.228 0.832 1.00 81.73 ? 597 NAG A C3 1 HETATM 4798 C C4 . NAG C 2 . ? 22.058 -1.663 1.257 1.00 83.60 ? 597 NAG A C4 1 HETATM 4799 C C5 . NAG C 2 . ? 22.527 -1.687 2.723 1.00 82.20 ? 597 NAG A C5 1 HETATM 4800 C C6 . NAG C 2 . ? 23.585 -2.765 2.942 1.00 82.36 ? 597 NAG A C6 1 HETATM 4801 C C7 . NAG C 2 . ? 18.963 1.382 1.686 1.00 82.80 ? 597 NAG A C7 1 HETATM 4802 C C8 . NAG C 2 . ? 18.484 2.615 2.413 1.00 83.06 ? 597 NAG A C8 1 HETATM 4803 N N2 . NAG C 2 . ? 19.893 0.615 2.279 1.00 81.20 ? 597 NAG A N2 1 HETATM 4804 O O3 . NAG C 2 . ? 22.827 0.298 0.133 1.00 82.08 ? 597 NAG A O3 1 HETATM 4805 O O4 . NAG C 2 . ? 20.991 -2.588 0.987 1.00 87.60 ? 597 NAG A O4 1 HETATM 4806 O O5 . NAG C 2 . ? 23.090 -0.439 3.135 1.00 79.40 ? 597 NAG A O5 1 HETATM 4807 O O6 . NAG C 2 . ? 23.541 -3.723 1.911 1.00 83.18 ? 597 NAG A O6 1 HETATM 4808 O O7 . NAG C 2 . ? 18.488 1.116 0.579 1.00 84.10 ? 597 NAG A O7 1 HETATM 4809 C C1 . MAN D 3 . ? 20.679 -2.793 -0.434 1.00 91.26 ? 598 MAN A C1 1 HETATM 4810 C C2 . MAN D 3 . ? 20.339 -4.259 -0.730 1.00 92.46 ? 598 MAN A C2 1 HETATM 4811 C C3 . MAN D 3 . ? 20.280 -4.519 -2.245 1.00 93.15 ? 598 MAN A C3 1 HETATM 4812 C C4 . MAN D 3 . ? 20.121 -3.221 -3.031 1.00 93.12 ? 598 MAN A C4 1 HETATM 4813 C C5 . MAN D 3 . ? 21.314 -2.310 -2.737 1.00 93.07 ? 598 MAN A C5 1 HETATM 4814 C C6 . MAN D 3 . ? 21.082 -0.855 -3.164 1.00 92.83 ? 598 MAN A C6 1 HETATM 4815 O O2 . MAN D 3 . ? 19.141 -4.646 -0.084 1.00 93.22 ? 598 MAN A O2 1 HETATM 4816 O O3 . MAN D 3 . ? 19.245 -5.414 -2.600 1.00 94.19 ? 598 MAN A O3 1 HETATM 4817 O O4 . MAN D 3 . ? 20.038 -3.513 -4.415 1.00 92.77 ? 598 MAN A O4 1 HETATM 4818 O O5 . MAN D 3 . ? 21.682 -2.379 -1.358 1.00 93.29 ? 598 MAN A O5 1 HETATM 4819 O O6 . MAN D 3 . ? 22.289 -0.279 -3.630 1.00 92.23 ? 598 MAN A O6 1 HETATM 4820 C C1 . NAG E 2 . ? -18.470 9.407 12.867 1.00 42.59 ? 599 NAG A C1 1 HETATM 4821 C C2 . NAG E 2 . ? -17.903 10.634 13.564 1.00 43.65 ? 599 NAG A C2 1 HETATM 4822 C C3 . NAG E 2 . ? -18.482 11.966 13.089 1.00 45.68 ? 599 NAG A C3 1 HETATM 4823 C C4 . NAG E 2 . ? -18.738 12.058 11.572 1.00 47.93 ? 599 NAG A C4 1 HETATM 4824 C C5 . NAG E 2 . ? -19.267 10.717 11.053 1.00 46.65 ? 599 NAG A C5 1 HETATM 4825 C C6 . NAG E 2 . ? -19.295 10.661 9.532 1.00 47.08 ? 599 NAG A C6 1 HETATM 4826 C C7 . NAG E 2 . ? -17.043 10.466 15.824 1.00 44.23 ? 599 NAG A C7 1 HETATM 4827 C C8 . NAG E 2 . ? -17.315 10.663 17.289 1.00 45.23 ? 599 NAG A C8 1 HETATM 4828 N N2 . NAG E 2 . ? -18.095 10.541 14.992 1.00 43.70 ? 599 NAG A N2 1 HETATM 4829 O O3 . NAG E 2 . ? -17.572 12.973 13.486 1.00 44.58 ? 599 NAG A O3 1 HETATM 4830 O O4 . NAG E 2 . ? -19.633 13.138 11.290 1.00 49.84 ? 599 NAG A O4 1 HETATM 4831 O O5 . NAG E 2 . ? -18.430 9.667 11.489 1.00 44.27 ? 599 NAG A O5 1 HETATM 4832 O O6 . NAG E 2 . ? -17.986 10.844 9.038 1.00 47.04 ? 599 NAG A O6 1 HETATM 4833 O O7 . NAG E 2 . ? -15.887 10.255 15.455 1.00 42.59 ? 599 NAG A O7 1 HETATM 4834 C C1 . NAG F 2 . ? -19.207 13.887 10.132 1.00 53.75 ? 600 NAG A C1 1 HETATM 4835 C C2 . NAG F 2 . ? -20.355 14.789 9.650 1.00 56.77 ? 600 NAG A C2 1 HETATM 4836 C C3 . NAG F 2 . ? -20.213 16.308 9.802 1.00 57.67 ? 600 NAG A C3 1 HETATM 4837 C C4 . NAG F 2 . ? -18.761 16.742 9.827 1.00 58.55 ? 600 NAG A C4 1 HETATM 4838 C C5 . NAG F 2 . ? -17.884 15.823 10.703 1.00 57.58 ? 600 NAG A C5 1 HETATM 4839 C C6 . NAG F 2 . ? -18.150 15.839 12.227 1.00 59.41 ? 600 NAG A C6 1 HETATM 4840 C C7 . NAG F 2 . ? -21.373 13.466 7.938 1.00 60.78 ? 600 NAG A C7 1 HETATM 4841 C C8 . NAG F 2 . ? -21.212 12.887 6.559 1.00 61.69 ? 600 NAG A C8 1 HETATM 4842 N N2 . NAG F 2 . ? -20.617 14.519 8.247 1.00 58.90 ? 600 NAG A N2 1 HETATM 4843 O O3 . NAG F 2 . ? -20.893 16.809 10.937 1.00 57.34 ? 600 NAG A O3 1 HETATM 4844 O O4 . NAG F 2 . ? -18.326 16.807 8.472 1.00 59.36 ? 600 NAG A O4 1 HETATM 4845 O O5 . NAG F 2 . ? -17.929 14.492 10.233 1.00 54.66 ? 600 NAG A O5 1 HETATM 4846 O O6 . NAG F 2 . ? -18.875 16.944 12.736 1.00 60.71 ? 600 NAG A O6 1 HETATM 4847 O O7 . NAG F 2 . ? -22.167 12.967 8.743 1.00 61.53 ? 600 NAG A O7 1 HETATM 4848 C C1 . NAG G 2 . ? 0.088 25.651 30.017 1.00 44.39 ? 601 NAG A C1 1 HETATM 4849 C C2 . NAG G 2 . ? 1.504 26.204 29.932 1.00 46.43 ? 601 NAG A C2 1 HETATM 4850 C C3 . NAG G 2 . ? 1.557 27.582 29.308 1.00 48.35 ? 601 NAG A C3 1 HETATM 4851 C C4 . NAG G 2 . ? 0.745 27.694 28.047 1.00 52.02 ? 601 NAG A C4 1 HETATM 4852 C C5 . NAG G 2 . ? -0.604 27.048 28.282 1.00 50.04 ? 601 NAG A C5 1 HETATM 4853 C C6 . NAG G 2 . ? -1.428 27.106 27.008 1.00 50.23 ? 601 NAG A C6 1 HETATM 4854 C C7 . NAG G 2 . ? 3.111 25.437 31.554 1.00 46.58 ? 601 NAG A C7 1 HETATM 4855 C C8 . NAG G 2 . ? 3.855 25.662 32.845 1.00 46.76 ? 601 NAG A C8 1 HETATM 4856 N N2 . NAG G 2 . ? 2.119 26.279 31.242 1.00 46.71 ? 601 NAG A N2 1 HETATM 4857 O O3 . NAG G 2 . ? 2.878 27.938 28.985 1.00 47.75 ? 601 NAG A O3 1 HETATM 4858 O O4 . NAG G 2 . ? 0.607 29.078 27.863 1.00 59.89 ? 601 NAG A O4 1 HETATM 4859 O O5 . NAG G 2 . ? -0.424 25.717 28.708 1.00 47.10 ? 601 NAG A O5 1 HETATM 4860 O O6 . NAG G 2 . ? -1.851 25.805 26.680 1.00 54.46 ? 601 NAG A O6 1 HETATM 4861 O O7 . NAG G 2 . ? 3.418 24.501 30.814 1.00 44.40 ? 601 NAG A O7 1 HETATM 4862 C C1 . NAG H 2 . ? 0.690 29.498 26.503 1.00 67.38 ? 602 NAG A C1 1 HETATM 4863 C C2 . NAG H 2 . ? -0.086 30.797 26.416 1.00 71.32 ? 602 NAG A C2 1 HETATM 4864 C C3 . NAG H 2 . ? 0.165 31.449 25.068 1.00 74.58 ? 602 NAG A C3 1 HETATM 4865 C C4 . NAG H 2 . ? 1.638 31.825 24.913 1.00 76.82 ? 602 NAG A C4 1 HETATM 4866 C C5 . NAG H 2 . ? 2.554 30.931 25.786 1.00 75.17 ? 602 NAG A C5 1 HETATM 4867 C C6 . NAG H 2 . ? 3.035 31.618 27.083 1.00 76.08 ? 602 NAG A C6 1 HETATM 4868 C C7 . NAG H 2 . ? -2.160 30.976 27.709 1.00 72.53 ? 602 NAG A C7 1 HETATM 4869 C C8 . NAG H 2 . ? -3.533 30.428 27.966 1.00 72.44 ? 602 NAG A C8 1 HETATM 4870 N N2 . NAG H 2 . ? -1.508 30.555 26.624 1.00 72.27 ? 602 NAG A N2 1 HETATM 4871 O O3 . NAG H 2 . ? -0.632 32.610 25.008 1.00 75.77 ? 602 NAG A O3 1 HETATM 4872 O O4 . NAG H 2 . ? 2.028 31.782 23.538 1.00 82.02 ? 602 NAG A O4 1 HETATM 4873 O O5 . NAG H 2 . ? 2.023 29.634 26.069 1.00 71.21 ? 602 NAG A O5 1 HETATM 4874 O O6 . NAG H 2 . ? 4.405 31.354 27.364 1.00 75.00 ? 602 NAG A O6 1 HETATM 4875 O O7 . NAG H 2 . ? -1.677 31.789 28.490 1.00 73.91 ? 602 NAG A O7 1 HETATM 4876 C C1 . MAN I 3 . ? 1.863 33.055 22.829 1.00 86.75 ? 603 MAN A C1 1 HETATM 4877 C C2 . MAN I 3 . ? 2.521 34.221 23.595 1.00 88.19 ? 603 MAN A C2 1 HETATM 4878 C C3 . MAN I 3 . ? 1.899 35.570 23.263 1.00 89.35 ? 603 MAN A C3 1 HETATM 4879 C C4 . MAN I 3 . ? 1.367 35.486 21.841 1.00 90.18 ? 603 MAN A C4 1 HETATM 4880 C C5 . MAN I 3 . ? 0.142 34.571 21.901 1.00 89.76 ? 603 MAN A C5 1 HETATM 4881 C C6 . MAN I 3 . ? -0.580 34.426 20.553 1.00 91.05 ? 603 MAN A C6 1 HETATM 4882 O O2 . MAN I 3 . ? 3.893 34.287 23.268 1.00 88.81 ? 603 MAN A O2 1 HETATM 4883 O O3 . MAN I 3 . ? 2.830 36.623 23.414 1.00 89.57 ? 603 MAN A O3 1 HETATM 4884 O O4 . MAN I 3 . ? 1.055 36.775 21.351 1.00 91.36 ? 603 MAN A O4 1 HETATM 4885 O O5 . MAN I 3 . ? 0.511 33.294 22.415 1.00 88.43 ? 603 MAN A O5 1 HETATM 4886 O O6 . MAN I 3 . ? -1.995 34.496 20.668 1.00 92.33 ? 603 MAN A O6 1 HETATM 4887 C C1 . NAG J 2 . ? 8.532 -25.613 11.969 1.00 51.79 ? 604 NAG A C1 1 HETATM 4888 C C2 . NAG J 2 . ? 9.572 -26.529 11.323 1.00 59.03 ? 604 NAG A C2 1 HETATM 4889 C C3 . NAG J 2 . ? 10.658 -27.114 12.248 1.00 60.87 ? 604 NAG A C3 1 HETATM 4890 C C4 . NAG J 2 . ? 10.775 -26.574 13.686 1.00 62.57 ? 604 NAG A C4 1 HETATM 4891 C C5 . NAG J 2 . ? 9.524 -25.802 14.119 1.00 59.29 ? 604 NAG A C5 1 HETATM 4892 C C6 . NAG J 2 . ? 9.752 -24.853 15.307 1.00 59.46 ? 604 NAG A C6 1 HETATM 4893 C C7 . NAG J 2 . ? 8.584 -27.634 9.348 1.00 62.89 ? 604 NAG A C7 1 HETATM 4894 C C8 . NAG J 2 . ? 7.863 -28.854 8.864 1.00 63.39 ? 604 NAG A C8 1 HETATM 4895 N N2 . NAG J 2 . ? 8.899 -27.631 10.649 1.00 62.08 ? 604 NAG A N2 1 HETATM 4896 O O3 . NAG J 2 . ? 11.878 -26.819 11.612 1.00 61.71 ? 604 NAG A O3 1 HETATM 4897 O O4 . NAG J 2 . ? 11.148 -27.553 14.674 1.00 67.77 ? 604 NAG A O4 1 HETATM 4898 O O5 . NAG J 2 . ? 9.167 -24.978 13.044 1.00 56.30 ? 604 NAG A O5 1 HETATM 4899 O O6 . NAG J 2 . ? 10.104 -25.502 16.507 1.00 58.50 ? 604 NAG A O6 1 HETATM 4900 O O7 . NAG J 2 . ? 8.848 -26.719 8.560 1.00 63.16 ? 604 NAG A O7 1 HETATM 4901 C C1 . NAG K 2 . ? 11.828 -28.731 14.178 1.00 70.72 ? 605 NAG A C1 1 HETATM 4902 C C2 . NAG K 2 . ? 13.306 -28.783 14.553 1.00 72.18 ? 605 NAG A C2 1 HETATM 4903 C C3 . NAG K 2 . ? 13.862 -30.211 14.450 1.00 72.97 ? 605 NAG A C3 1 HETATM 4904 C C4 . NAG K 2 . ? 13.019 -31.136 13.568 1.00 73.46 ? 605 NAG A C4 1 HETATM 4905 C C5 . NAG K 2 . ? 11.512 -30.944 13.748 1.00 73.89 ? 605 NAG A C5 1 HETATM 4906 C C6 . NAG K 2 . ? 10.829 -32.239 14.182 1.00 75.02 ? 605 NAG A C6 1 HETATM 4907 C C7 . NAG K 2 . ? 15.225 -27.324 14.164 1.00 73.85 ? 605 NAG A C7 1 HETATM 4908 C C8 . NAG K 2 . ? 16.507 -27.706 13.474 1.00 73.26 ? 605 NAG A C8 1 HETATM 4909 N N2 . NAG K 2 . ? 14.097 -27.894 13.716 1.00 73.37 ? 605 NAG A N2 1 HETATM 4910 O O3 . NAG K 2 . ? 14.015 -30.795 15.730 1.00 73.03 ? 605 NAG A O3 1 HETATM 4911 O O4 . NAG K 2 . ? 13.345 -30.926 12.215 1.00 73.56 ? 605 NAG A O4 1 HETATM 4912 O O5 . NAG K 2 . ? 11.262 -29.917 14.678 1.00 72.28 ? 605 NAG A O5 1 HETATM 4913 O O6 . NAG K 2 . ? 9.666 -32.475 13.412 1.00 77.05 ? 605 NAG A O6 1 HETATM 4914 O O7 . NAG K 2 . ? 15.249 -26.520 15.102 1.00 73.38 ? 605 NAG A O7 1 HETATM 4915 CA CA . CA L 4 . ? 0.125 -7.046 18.584 1.00 17.93 ? 606 CA A CA 1 HETATM 4916 S S . SCN M 5 . ? -12.553 0.578 27.597 1.00 20.96 ? 607 SCN A S 1 HETATM 4917 C C . SCN M 5 . ? -14.303 0.205 27.584 1.00 18.31 ? 607 SCN A C 1 HETATM 4918 N N . SCN M 5 . ? -15.449 0.060 27.639 1.00 18.01 ? 607 SCN A N 1 HETATM 4919 I I . IOD N 6 . ? 5.444 3.394 28.460 1.00 65.68 ? 608 IOD A I 1 HETATM 4920 I I . IOD O 6 . ? -3.507 -24.264 10.413 1.00 98.73 ? 609 IOD A I 1 HETATM 4921 I I . IOD P 6 . ? 12.222 -15.931 29.473 1.00 21.16 ? 610 IOD A I 1 HETATM 4922 I I . IOD Q 6 . ? 25.695 6.229 44.087 1.00 86.18 ? 611 IOD A I 1 HETATM 4923 I I . IOD R 6 . ? 25.211 1.692 9.550 1.00 99.45 ? 612 IOD A I 1 HETATM 4924 I I . IOD S 6 . ? -13.229 13.685 22.046 1.00 59.71 ? 613 IOD A I 1 HETATM 4925 I I . IOD T 6 . ? 8.858 -8.353 4.868 1.00 77.79 ? 614 IOD A I 1 HETATM 4926 I I . IOD U 6 . ? 7.146 20.902 4.622 1.00 58.19 ? 615 IOD A I 1 HETATM 4927 I I . IOD V 6 . ? 36.903 -16.133 31.747 1.00 54.05 ? 616 IOD A I 1 HETATM 4928 I I . IOD W 6 . ? 14.934 3.315 5.741 1.00 99.06 ? 617 IOD A I 1 HETATM 4929 C CHA . HEM X 7 . ? 8.594 0.055 28.935 1.00 16.36 ? 618 HEM A CHA 1 HETATM 4930 C CHB . HEM X 7 . ? 9.140 4.829 28.866 1.00 13.93 ? 618 HEM A CHB 1 HETATM 4931 C CHC . HEM X 7 . ? 11.028 4.492 24.465 1.00 17.18 ? 618 HEM A CHC 1 HETATM 4932 C CHD . HEM X 7 . ? 11.024 -0.283 24.747 1.00 16.93 ? 618 HEM A CHD 1 HETATM 4933 C C1A . HEM X 7 . ? 8.652 1.348 29.332 1.00 13.70 ? 618 HEM A C1A 1 HETATM 4934 C C2A . HEM X 7 . ? 8.221 1.846 30.619 1.00 13.25 ? 618 HEM A C2A 1 HETATM 4935 C C3A . HEM X 7 . ? 8.356 3.180 30.573 1.00 11.49 ? 618 HEM A C3A 1 HETATM 4936 C C4A . HEM X 7 . ? 8.868 3.552 29.280 1.00 12.82 ? 618 HEM A C4A 1 HETATM 4937 C CMA . HEM X 7 . ? 8.077 4.148 31.725 1.00 8.38 ? 618 HEM A CMA 1 HETATM 4938 C CAA . HEM X 7 . ? 7.694 1.009 31.827 1.00 12.32 ? 618 HEM A CAA 1 HETATM 4939 C CBA . HEM X 7 . ? 8.819 0.175 32.391 1.00 17.16 ? 618 HEM A CBA 1 HETATM 4940 C CGA . HEM X 7 . ? 8.420 -0.680 33.572 1.00 20.22 ? 618 HEM A CGA 1 HETATM 4941 O O1A . HEM X 7 . ? 7.561 -0.175 34.341 1.00 25.08 ? 618 HEM A O1A 1 HETATM 4942 O O2A . HEM X 7 . ? 8.944 -1.837 33.779 1.00 18.84 ? 618 HEM A O2A 1 HETATM 4943 C C1B . HEM X 7 . ? 9.671 5.169 27.644 1.00 15.29 ? 618 HEM A C1B 1 HETATM 4944 C C2B . HEM X 7 . ? 9.955 6.510 27.174 1.00 14.31 ? 618 HEM A C2B 1 HETATM 4945 C C3B . HEM X 7 . ? 10.438 6.413 25.954 1.00 14.58 ? 618 HEM A C3B 1 HETATM 4946 C C4B . HEM X 7 . ? 10.551 5.009 25.636 1.00 16.37 ? 618 HEM A C4B 1 HETATM 4947 C CMB . HEM X 7 . ? 9.616 7.838 27.875 1.00 12.61 ? 618 HEM A CMB 1 HETATM 4948 C CAB . HEM X 7 . ? 10.856 7.614 25.090 1.00 15.80 ? 618 HEM A CAB 1 HETATM 4949 C CBB . HEM X 7 . ? 11.029 8.835 25.649 1.00 17.32 ? 618 HEM A CBB 1 HETATM 4950 C C1C . HEM X 7 . ? 11.143 3.177 24.148 1.00 16.37 ? 618 HEM A C1C 1 HETATM 4951 C C2C . HEM X 7 . ? 11.629 2.667 22.894 1.00 17.06 ? 618 HEM A C2C 1 HETATM 4952 C C3C . HEM X 7 . ? 11.601 1.315 22.961 1.00 14.98 ? 618 HEM A C3C 1 HETATM 4953 C C4C . HEM X 7 . ? 11.135 0.967 24.262 1.00 13.54 ? 618 HEM A C4C 1 HETATM 4954 C CMC . HEM X 7 . ? 12.023 3.550 21.682 1.00 15.42 ? 618 HEM A CMC 1 HETATM 4955 C CAC . HEM X 7 . ? 12.026 0.308 21.861 1.00 15.16 ? 618 HEM A CAC 1 HETATM 4956 C CBC . HEM X 7 . ? 12.889 0.629 20.884 1.00 11.67 ? 618 HEM A CBC 1 HETATM 4957 C C1D . HEM X 7 . ? 10.305 -0.636 25.858 1.00 18.73 ? 618 HEM A C1D 1 HETATM 4958 C C2D . HEM X 7 . ? 9.910 -1.996 26.150 1.00 18.44 ? 618 HEM A C2D 1 HETATM 4959 C C3D . HEM X 7 . ? 9.150 -1.918 27.464 1.00 18.53 ? 618 HEM A C3D 1 HETATM 4960 C C4D . HEM X 7 . ? 9.169 -0.492 27.818 1.00 18.36 ? 618 HEM A C4D 1 HETATM 4961 C CMD . HEM X 7 . ? 10.229 -3.260 25.340 1.00 20.44 ? 618 HEM A CMD 1 HETATM 4962 C CAD . HEM X 7 . ? 8.485 -3.110 28.201 1.00 18.11 ? 618 HEM A CAD 1 HETATM 4963 C CBD . HEM X 7 . ? 6.998 -3.196 27.777 1.00 15.58 ? 618 HEM A CBD 1 HETATM 4964 C CGD . HEM X 7 . ? 6.305 -4.301 28.531 1.00 17.85 ? 618 HEM A CGD 1 HETATM 4965 O O1D . HEM X 7 . ? 6.386 -5.518 28.156 1.00 18.51 ? 618 HEM A O1D 1 HETATM 4966 O O2D . HEM X 7 . ? 5.670 -3.964 29.551 1.00 18.54 ? 618 HEM A O2D 1 HETATM 4967 N NA . HEM X 7 . ? 9.030 2.403 28.536 1.00 14.71 ? 618 HEM A NA 1 HETATM 4968 N NB . HEM X 7 . ? 10.072 4.265 26.686 1.00 16.52 ? 618 HEM A NB 1 HETATM 4969 N NC . HEM X 7 . ? 10.876 2.111 24.975 1.00 16.78 ? 618 HEM A NC 1 HETATM 4970 N ND . HEM X 7 . ? 9.848 0.233 26.851 1.00 17.44 ? 618 HEM A ND 1 HETATM 4971 FE FE . HEM X 7 . ? 10.071 2.218 26.917 1.00 18.00 ? 618 HEM A FE 1 HETATM 4972 C C1 . CAQ Y 8 . ? -5.052 4.765 36.834 1.00 36.68 ? 619 CAQ A C1 1 HETATM 4973 C C2 . CAQ Y 8 . ? -4.025 3.937 36.425 1.00 36.65 ? 619 CAQ A C2 1 HETATM 4974 C C3 . CAQ Y 8 . ? -4.023 2.568 36.771 1.00 41.75 ? 619 CAQ A C3 1 HETATM 4975 O O3 . CAQ Y 8 . ? -2.957 1.867 36.306 1.00 39.50 ? 619 CAQ A O3 1 HETATM 4976 C C4 . CAQ Y 8 . ? -5.125 1.971 37.588 1.00 39.75 ? 619 CAQ A C4 1 HETATM 4977 O O4 . CAQ Y 8 . ? -5.138 0.660 37.929 1.00 38.50 ? 619 CAQ A O4 1 HETATM 4978 C C5 . CAQ Y 8 . ? -6.110 2.851 37.959 1.00 37.89 ? 619 CAQ A C5 1 HETATM 4979 C C6 . CAQ Y 8 . ? -6.058 4.195 37.586 1.00 37.97 ? 619 CAQ A C6 1 HETATM 4980 O O . HOH Z 9 . ? 43.281 -3.479 34.930 1.00 66.49 ? 620 HOH A O 1 HETATM 4981 O O . HOH Z 9 . ? 19.091 -10.658 34.515 1.00 10.02 ? 621 HOH A O 1 HETATM 4982 O O . HOH Z 9 . ? 34.193 -18.610 30.509 1.00 47.13 ? 622 HOH A O 1 HETATM 4983 O O . HOH Z 9 . ? -4.107 12.739 18.301 1.00 29.64 ? 623 HOH A O 1 HETATM 4984 O O . HOH Z 9 . ? 40.614 -11.989 35.878 1.00 34.72 ? 624 HOH A O 1 HETATM 4985 O O . HOH Z 9 . ? 0.428 20.448 12.179 1.00 16.64 ? 625 HOH A O 1 HETATM 4986 O O . HOH Z 9 . ? 4.691 28.125 7.992 1.00 39.42 ? 626 HOH A O 1 HETATM 4987 O O . HOH Z 9 . ? -15.214 4.707 4.511 1.00 35.70 ? 627 HOH A O 1 HETATM 4988 O O . HOH Z 9 . ? -8.148 21.974 36.350 1.00 32.91 ? 628 HOH A O 1 HETATM 4989 O O . HOH Z 9 . ? 24.891 -1.724 46.278 1.00 22.55 ? 629 HOH A O 1 HETATM 4990 O O . HOH Z 9 . ? 16.000 -1.258 46.600 1.00 26.02 ? 630 HOH A O 1 HETATM 4991 O O . HOH Z 9 . ? 15.864 9.338 2.198 1.00 30.05 ? 631 HOH A O 1 HETATM 4992 O O . HOH Z 9 . ? 29.854 13.133 30.809 1.00 8.98 ? 632 HOH A O 1 HETATM 4993 O O . HOH Z 9 . ? 24.038 -15.765 34.349 1.00 28.97 ? 633 HOH A O 1 HETATM 4994 O O . HOH Z 9 . ? 24.054 -7.655 23.094 1.00 10.55 ? 634 HOH A O 1 HETATM 4995 O O . HOH Z 9 . ? 2.298 4.066 2.410 1.00 24.23 ? 635 HOH A O 1 HETATM 4996 O O . HOH Z 9 . ? 12.879 -19.930 16.998 1.00 40.83 ? 636 HOH A O 1 HETATM 4997 O O . HOH Z 9 . ? 22.482 3.123 19.139 1.00 39.31 ? 637 HOH A O 1 HETATM 4998 O O . HOH Z 9 . ? 3.751 4.575 30.596 1.00 9.50 ? 638 HOH A O 1 HETATM 4999 O O . HOH Z 9 . ? 7.888 -18.145 22.582 1.00 9.11 ? 639 HOH A O 1 HETATM 5000 O O . HOH Z 9 . ? -2.047 11.625 37.593 1.00 15.51 ? 640 HOH A O 1 HETATM 5001 O O . HOH Z 9 . ? 15.455 15.572 18.751 1.00 9.88 ? 641 HOH A O 1 HETATM 5002 O O . HOH Z 9 . ? 14.656 1.770 17.751 1.00 9.87 ? 642 HOH A O 1 HETATM 5003 O O . HOH Z 9 . ? 11.344 -22.944 30.575 1.00 22.19 ? 643 HOH A O 1 HETATM 5004 O O . HOH Z 9 . ? 21.561 -18.200 43.987 1.00 12.04 ? 644 HOH A O 1 HETATM 5005 O O . HOH Z 9 . ? 0.470 -11.963 23.951 1.00 21.18 ? 645 HOH A O 1 HETATM 5006 O O . HOH Z 9 . ? -3.631 -3.012 22.459 1.00 28.66 ? 646 HOH A O 1 HETATM 5007 O O . HOH Z 9 . ? -13.316 -9.699 -11.884 1.00 48.64 ? 647 HOH A O 1 HETATM 5008 O O . HOH Z 9 . ? 24.854 -3.482 -0.790 1.00 46.97 ? 648 HOH A O 1 HETATM 5009 O O . HOH Z 9 . ? 7.672 2.450 26.150 1.00 12.78 ? 649 HOH A O 1 HETATM 5010 O O . HOH Z 9 . ? 16.477 -11.908 38.494 1.00 16.49 ? 650 HOH A O 1 HETATM 5011 O O . HOH Z 9 . ? -23.080 -5.216 -12.800 1.00 52.84 ? 651 HOH A O 1 HETATM 5012 O O . HOH Z 9 . ? 5.857 16.561 31.285 1.00 25.13 ? 652 HOH A O 1 HETATM 5013 O O . HOH Z 9 . ? -7.855 12.893 9.069 1.00 20.02 ? 653 HOH A O 1 HETATM 5014 O O . HOH Z 9 . ? -5.175 8.392 30.945 1.00 11.71 ? 654 HOH A O 1 HETATM 5015 O O . HOH Z 9 . ? -4.588 -18.328 3.502 1.00 55.56 ? 655 HOH A O 1 HETATM 5016 O O . HOH Z 9 . ? 14.287 -19.608 49.664 1.00 32.70 ? 656 HOH A O 1 HETATM 5017 O O . HOH Z 9 . ? -18.278 1.669 10.973 1.00 29.20 ? 657 HOH A O 1 HETATM 5018 O O . HOH Z 9 . ? 37.815 -11.537 38.450 1.00 41.41 ? 658 HOH A O 1 HETATM 5019 O O . HOH Z 9 . ? 6.187 10.482 44.380 1.00 35.88 ? 659 HOH A O 1 HETATM 5020 O O . HOH Z 9 . ? 2.045 -4.479 52.585 1.00 63.09 ? 660 HOH A O 1 HETATM 5021 O O . HOH Z 9 . ? 19.047 7.675 26.444 1.00 17.40 ? 661 HOH A O 1 HETATM 5022 O O . HOH Z 9 . ? 6.270 4.216 -0.811 1.00 36.85 ? 662 HOH A O 1 HETATM 5023 O O . HOH Z 9 . ? 18.953 14.081 40.363 1.00 17.85 ? 663 HOH A O 1 HETATM 5024 O O . HOH Z 9 . ? -5.812 -6.634 17.930 1.00 14.73 ? 664 HOH A O 1 HETATM 5025 O O . HOH Z 9 . ? 31.405 17.085 20.123 1.00 50.21 ? 665 HOH A O 1 HETATM 5026 O O . HOH Z 9 . ? 13.057 16.498 17.622 1.00 19.70 ? 666 HOH A O 1 HETATM 5027 O O . HOH Z 9 . ? 22.502 10.273 32.831 1.00 25.18 ? 667 HOH A O 1 HETATM 5028 O O . HOH Z 9 . ? 30.772 -11.882 22.221 1.00 9.95 ? 668 HOH A O 1 HETATM 5029 O O . HOH Z 9 . ? 15.960 23.006 16.198 1.00 26.87 ? 669 HOH A O 1 HETATM 5030 O O . HOH Z 9 . ? -12.786 -10.481 18.324 1.00 12.84 ? 670 HOH A O 1 HETATM 5031 O O . HOH Z 9 . ? 26.510 5.818 30.948 1.00 15.23 ? 671 HOH A O 1 HETATM 5032 O O . HOH Z 9 . ? 17.674 -9.709 36.708 1.00 16.60 ? 672 HOH A O 1 HETATM 5033 O O . HOH Z 9 . ? -1.371 17.681 28.078 1.00 15.92 ? 673 HOH A O 1 HETATM 5034 O O . HOH Z 9 . ? -8.475 -7.155 9.714 1.00 25.03 ? 674 HOH A O 1 HETATM 5035 O O . HOH Z 9 . ? 17.159 4.616 50.372 1.00 30.33 ? 675 HOH A O 1 HETATM 5036 O O . HOH Z 9 . ? -1.784 28.940 24.176 1.00 30.64 ? 676 HOH A O 1 HETATM 5037 O O . HOH Z 9 . ? 29.378 -7.687 13.606 1.00 28.29 ? 677 HOH A O 1 HETATM 5038 O O . HOH Z 9 . ? -1.766 -18.216 30.603 1.00 12.30 ? 678 HOH A O 1 HETATM 5039 O O . HOH Z 9 . ? 20.658 -0.297 -6.329 1.00 51.86 ? 679 HOH A O 1 HETATM 5040 O O . HOH Z 9 . ? -6.623 -14.225 14.992 1.00 21.80 ? 680 HOH A O 1 HETATM 5041 O O . HOH Z 9 . ? 1.196 0.208 -4.346 1.00 26.07 ? 681 HOH A O 1 HETATM 5042 O O . HOH Z 9 . ? 4.971 -26.157 40.499 1.00 38.22 ? 682 HOH A O 1 HETATM 5043 O O . HOH Z 9 . ? -1.305 35.776 26.107 1.00 50.60 ? 683 HOH A O 1 HETATM 5044 O O . HOH Z 9 . ? -13.011 -16.701 15.124 1.00 59.19 ? 684 HOH A O 1 HETATM 5045 O O . HOH Z 9 . ? -8.505 -15.184 13.100 1.00 18.69 ? 685 HOH A O 1 HETATM 5046 O O . HOH Z 9 . ? 12.943 -16.992 32.664 1.00 16.98 ? 686 HOH A O 1 HETATM 5047 O O . HOH Z 9 . ? 5.840 -20.914 28.914 1.00 25.46 ? 687 HOH A O 1 HETATM 5048 O O . HOH Z 9 . ? 20.540 14.362 23.832 1.00 25.99 ? 688 HOH A O 1 HETATM 5049 O O . HOH Z 9 . ? 14.455 -12.284 40.458 1.00 9.45 ? 689 HOH A O 1 HETATM 5050 O O . HOH Z 9 . ? -7.955 -9.464 25.663 1.00 31.16 ? 690 HOH A O 1 HETATM 5051 O O . HOH Z 9 . ? 9.548 3.057 5.056 1.00 13.79 ? 691 HOH A O 1 HETATM 5052 O O . HOH Z 9 . ? 21.022 19.435 2.663 1.00 50.15 ? 692 HOH A O 1 HETATM 5053 O O . HOH Z 9 . ? 18.274 -12.158 47.410 1.00 27.34 ? 693 HOH A O 1 HETATM 5054 O O . HOH Z 9 . ? -0.419 10.517 53.095 1.00 68.06 ? 694 HOH A O 1 HETATM 5055 O O . HOH Z 9 . ? -3.972 20.684 2.728 1.00 51.45 ? 695 HOH A O 1 HETATM 5056 O O . HOH Z 9 . ? 23.799 -20.598 31.988 1.00 55.43 ? 696 HOH A O 1 HETATM 5057 O O . HOH Z 9 . ? -1.448 -25.334 40.181 1.00 57.52 ? 697 HOH A O 1 HETATM 5058 O O . HOH Z 9 . ? 9.340 16.899 39.827 1.00 37.01 ? 698 HOH A O 1 HETATM 5059 O O . HOH Z 9 . ? 14.776 11.259 7.983 1.00 20.17 ? 699 HOH A O 1 HETATM 5060 O O . HOH Z 9 . ? 9.346 -20.794 35.103 1.00 17.88 ? 700 HOH A O 1 HETATM 5061 O O . HOH Z 9 . ? -0.604 -15.712 24.663 1.00 16.22 ? 701 HOH A O 1 HETATM 5062 O O . HOH Z 9 . ? 17.700 0.904 44.044 1.00 17.30 ? 702 HOH A O 1 HETATM 5063 O O . HOH Z 9 . ? -0.720 -3.562 21.303 1.00 29.10 ? 703 HOH A O 1 HETATM 5064 O O . HOH Z 9 . ? 22.943 -15.792 38.073 1.00 31.90 ? 704 HOH A O 1 HETATM 5065 O O . HOH Z 9 . ? 9.334 -22.225 18.530 1.00 21.02 ? 705 HOH A O 1 HETATM 5066 O O . HOH Z 9 . ? 43.161 0.526 34.983 1.00 40.63 ? 706 HOH A O 1 HETATM 5067 O O . HOH Z 9 . ? 13.311 -8.985 5.659 1.00 48.14 ? 707 HOH A O 1 HETATM 5068 O O . HOH Z 9 . ? -4.443 -12.144 35.919 1.00 43.85 ? 708 HOH A O 1 HETATM 5069 O O . HOH Z 9 . ? 5.587 -9.893 39.108 1.00 10.86 ? 709 HOH A O 1 HETATM 5070 O O . HOH Z 9 . ? -18.388 -15.837 27.092 1.00 53.12 ? 710 HOH A O 1 HETATM 5071 O O . HOH Z 9 . ? 10.261 16.146 16.456 1.00 24.90 ? 711 HOH A O 1 HETATM 5072 O O . HOH Z 9 . ? -6.737 10.426 31.379 1.00 61.80 ? 712 HOH A O 1 HETATM 5073 O O . HOH Z 9 . ? 11.381 -12.644 3.397 1.00 47.10 ? 713 HOH A O 1 HETATM 5074 O O . HOH Z 9 . ? 3.150 -11.372 13.962 1.00 35.09 ? 714 HOH A O 1 HETATM 5075 O O . HOH Z 9 . ? -4.243 -6.550 31.861 1.00 50.14 ? 715 HOH A O 1 HETATM 5076 O O . HOH Z 9 . ? 1.327 3.016 23.112 1.00 18.73 ? 716 HOH A O 1 HETATM 5077 O O . HOH Z 9 . ? 17.823 -4.451 46.279 1.00 46.89 ? 717 HOH A O 1 HETATM 5078 O O . HOH Z 9 . ? -6.411 12.129 2.823 1.00 35.29 ? 718 HOH A O 1 HETATM 5079 O O . HOH Z 9 . ? 3.757 -17.110 8.838 1.00 20.05 ? 719 HOH A O 1 HETATM 5080 O O . HOH Z 9 . ? -20.757 9.074 17.933 1.00 45.77 ? 720 HOH A O 1 HETATM 5081 O O . HOH Z 9 . ? 5.988 -1.907 31.013 1.00 32.85 ? 721 HOH A O 1 HETATM 5082 O O . HOH Z 9 . ? 30.625 -12.886 19.619 1.00 40.89 ? 722 HOH A O 1 HETATM 5083 O O . HOH Z 9 . ? -3.269 -23.131 12.943 1.00 26.72 ? 723 HOH A O 1 HETATM 5084 O O . HOH Z 9 . ? 16.934 -2.072 43.546 1.00 24.05 ? 724 HOH A O 1 HETATM 5085 O O . HOH Z 9 . ? 16.377 18.074 18.854 1.00 15.32 ? 725 HOH A O 1 HETATM 5086 O O . HOH Z 9 . ? -16.176 10.853 6.526 1.00 53.99 ? 726 HOH A O 1 HETATM 5087 O O . HOH Z 9 . ? 5.507 11.203 38.176 1.00 28.69 ? 727 HOH A O 1 HETATM 5088 O O . HOH Z 9 . ? -15.765 -5.228 18.486 1.00 44.76 ? 728 HOH A O 1 HETATM 5089 O O . HOH Z 9 . ? 4.213 -11.603 48.214 1.00 27.69 ? 729 HOH A O 1 HETATM 5090 O O . HOH Z 9 . ? 20.873 -9.870 39.355 1.00 14.99 ? 730 HOH A O 1 HETATM 5091 O O . HOH Z 9 . ? -7.211 -9.459 9.572 1.00 28.68 ? 731 HOH A O 1 HETATM 5092 O O . HOH Z 9 . ? -0.937 -8.029 11.001 1.00 29.87 ? 732 HOH A O 1 HETATM 5093 O O . HOH Z 9 . ? -19.401 6.753 17.817 1.00 50.64 ? 733 HOH A O 1 HETATM 5094 O O . HOH Z 9 . ? -1.250 0.437 34.182 1.00 35.81 ? 734 HOH A O 1 HETATM 5095 O O . HOH Z 9 . ? 29.855 5.835 55.010 1.00 56.56 ? 735 HOH A O 1 HETATM 5096 O O . HOH Z 9 . ? 37.481 0.401 24.713 1.00 37.65 ? 736 HOH A O 1 HETATM 5097 O O . HOH Z 9 . ? 9.003 19.965 34.052 1.00 12.82 ? 737 HOH A O 1 HETATM 5098 O O . HOH Z 9 . ? 34.694 4.043 26.481 1.00 54.47 ? 738 HOH A O 1 HETATM 5099 O O . HOH Z 9 . ? 9.690 -22.665 33.201 1.00 36.71 ? 739 HOH A O 1 HETATM 5100 O O . HOH Z 9 . ? -2.199 -8.290 8.255 1.00 43.31 ? 740 HOH A O 1 HETATM 5101 O O . HOH Z 9 . ? 5.453 -9.758 46.028 1.00 40.67 ? 741 HOH A O 1 HETATM 5102 O O . HOH Z 9 . ? -14.722 -8.255 18.757 1.00 21.51 ? 742 HOH A O 1 HETATM 5103 O O . HOH Z 9 . ? -4.398 -23.244 23.832 1.00 30.49 ? 743 HOH A O 1 HETATM 5104 O O . HOH Z 9 . ? 17.007 -20.423 34.859 1.00 26.70 ? 744 HOH A O 1 HETATM 5105 O O . HOH Z 9 . ? 10.135 0.841 -0.260 1.00 31.52 ? 745 HOH A O 1 HETATM 5106 O O . HOH Z 9 . ? 15.670 18.939 31.642 1.00 30.69 ? 746 HOH A O 1 HETATM 5107 O O . HOH Z 9 . ? 32.084 -19.974 28.727 1.00 29.81 ? 747 HOH A O 1 HETATM 5108 O O . HOH Z 9 . ? 32.246 6.088 23.971 1.00 52.65 ? 748 HOH A O 1 HETATM 5109 O O . HOH Z 9 . ? -7.022 -3.942 24.645 1.00 33.47 ? 749 HOH A O 1 HETATM 5110 O O . HOH Z 9 . ? 20.974 4.952 17.515 1.00 23.39 ? 750 HOH A O 1 HETATM 5111 O O . HOH Z 9 . ? -10.420 4.985 30.380 1.00 32.31 ? 751 HOH A O 1 HETATM 5112 O O . HOH Z 9 . ? 29.599 3.675 31.692 1.00 33.45 ? 752 HOH A O 1 HETATM 5113 O O . HOH Z 9 . ? 22.459 12.874 30.421 1.00 25.50 ? 753 HOH A O 1 HETATM 5114 O O . HOH Z 9 . ? -2.949 19.878 29.978 1.00 18.26 ? 754 HOH A O 1 HETATM 5115 O O . HOH Z 9 . ? -15.910 1.709 12.418 1.00 28.48 ? 755 HOH A O 1 HETATM 5116 O O . HOH Z 9 . ? -10.202 -8.411 0.567 1.00 32.82 ? 756 HOH A O 1 HETATM 5117 O O . HOH Z 9 . ? -8.077 15.096 35.345 1.00 43.82 ? 757 HOH A O 1 HETATM 5118 O O . HOH Z 9 . ? -0.550 -2.602 56.827 1.00 36.07 ? 758 HOH A O 1 HETATM 5119 O O . HOH Z 9 . ? 29.294 -0.017 20.239 1.00 49.28 ? 759 HOH A O 1 HETATM 5120 O O . HOH Z 9 . ? -3.147 4.795 17.218 1.00 17.36 ? 760 HOH A O 1 HETATM 5121 O O . HOH Z 9 . ? -4.706 6.643 -2.719 1.00 46.87 ? 761 HOH A O 1 HETATM 5122 O O . HOH Z 9 . ? 18.021 12.591 10.305 1.00 25.00 ? 762 HOH A O 1 HETATM 5123 O O . HOH Z 9 . ? -5.140 3.942 -4.814 1.00 29.45 ? 763 HOH A O 1 HETATM 5124 O O . HOH Z 9 . ? 3.331 -13.201 25.114 1.00 25.98 ? 764 HOH A O 1 HETATM 5125 O O . HOH Z 9 . ? -4.466 12.103 1.516 1.00 27.45 ? 765 HOH A O 1 HETATM 5126 O O . HOH Z 9 . ? 28.902 2.725 20.718 1.00 34.86 ? 766 HOH A O 1 HETATM 5127 O O . HOH Z 9 . ? -14.811 7.163 24.429 1.00 26.33 ? 767 HOH A O 1 HETATM 5128 O O . HOH Z 9 . ? 26.076 11.339 35.411 1.00 56.50 ? 768 HOH A O 1 HETATM 5129 O O . HOH Z 9 . ? 22.799 8.922 6.422 1.00 28.07 ? 769 HOH A O 1 HETATM 5130 O O . HOH Z 9 . ? 6.754 21.803 27.047 1.00 42.31 ? 770 HOH A O 1 HETATM 5131 O O . HOH Z 9 . ? 4.542 20.955 19.716 1.00 43.61 ? 771 HOH A O 1 HETATM 5132 O O . HOH Z 9 . ? 23.922 2.611 50.292 1.00 32.21 ? 772 HOH A O 1 HETATM 5133 O O . HOH Z 9 . ? 12.711 -2.602 49.043 1.00 32.33 ? 773 HOH A O 1 HETATM 5134 O O . HOH Z 9 . ? 19.290 15.037 35.579 1.00 45.02 ? 774 HOH A O 1 HETATM 5135 O O . HOH Z 9 . ? -23.423 -2.202 -13.339 1.00 56.71 ? 775 HOH A O 1 HETATM 5136 O O . HOH Z 9 . ? 10.164 29.368 1.093 1.00 28.47 ? 776 HOH A O 1 HETATM 5137 O O . HOH Z 9 . ? -10.940 -0.859 17.164 1.00 22.82 ? 777 HOH A O 1 HETATM 5138 O O . HOH Z 9 . ? 10.481 2.698 1.776 1.00 39.72 ? 778 HOH A O 1 HETATM 5139 O O . HOH Z 9 . ? -15.141 7.708 0.671 1.00 24.26 ? 779 HOH A O 1 HETATM 5140 O O . HOH Z 9 . ? -12.471 -14.521 33.939 1.00 40.97 ? 780 HOH A O 1 HETATM 5141 O O . HOH Z 9 . ? -19.967 -6.454 2.747 1.00 25.18 ? 781 HOH A O 1 HETATM 5142 O O . HOH Z 9 . ? -5.840 4.107 18.083 1.00 26.50 ? 782 HOH A O 1 HETATM 5143 O O . HOH Z 9 . ? 16.626 -17.307 60.048 1.00 58.26 ? 783 HOH A O 1 HETATM 5144 O O . HOH Z 9 . ? -5.436 -5.873 15.446 1.00 18.48 ? 784 HOH A O 1 HETATM 5145 O O . HOH Z 9 . ? -7.569 23.337 17.178 1.00 66.51 ? 785 HOH A O 1 HETATM 5146 O O . HOH Z 9 . ? 15.674 -17.992 14.462 1.00 24.28 ? 786 HOH A O 1 HETATM 5147 O O . HOH Z 9 . ? 1.359 -16.514 38.204 1.00 23.93 ? 787 HOH A O 1 HETATM 5148 O O . HOH Z 9 . ? 3.311 23.032 9.889 1.00 28.39 ? 788 HOH A O 1 HETATM 5149 O O . HOH Z 9 . ? 23.176 12.253 35.334 1.00 34.17 ? 789 HOH A O 1 HETATM 5150 O O . HOH Z 9 . ? -21.081 -1.398 10.788 1.00 61.23 ? 790 HOH A O 1 HETATM 5151 O O . HOH Z 9 . ? 20.963 0.051 22.659 1.00 27.76 ? 791 HOH A O 1 HETATM 5152 O O . HOH Z 9 . ? -18.549 -7.797 -2.845 1.00 67.59 ? 792 HOH A O 1 HETATM 5153 O O . HOH Z 9 . ? -0.436 38.768 19.720 1.00 62.93 ? 793 HOH A O 1 HETATM 5154 O O . HOH Z 9 . ? 6.519 11.404 51.450 1.00 47.42 ? 794 HOH A O 1 HETATM 5155 O O . HOH Z 9 . ? -1.015 -13.015 1.350 1.00 18.81 ? 795 HOH A O 1 HETATM 5156 O O . HOH Z 9 . ? 16.178 -5.403 43.697 1.00 31.56 ? 796 HOH A O 1 HETATM 5157 O O . HOH Z 9 . ? 11.769 16.586 -5.031 1.00 54.02 ? 797 HOH A O 1 HETATM 5158 O O . HOH Z 9 . ? -3.874 -18.448 18.192 1.00 42.77 ? 798 HOH A O 1 HETATM 5159 O O . HOH Z 9 . ? 14.896 -19.782 4.031 1.00 48.10 ? 799 HOH A O 1 HETATM 5160 O O . HOH Z 9 . ? -0.533 6.652 3.544 1.00 34.81 ? 800 HOH A O 1 HETATM 5161 O O . HOH Z 9 . ? 25.496 18.192 27.506 1.00 40.39 ? 801 HOH A O 1 HETATM 5162 O O . HOH Z 9 . ? 12.807 -24.770 1.081 1.00 42.68 ? 802 HOH A O 1 HETATM 5163 O O . HOH Z 9 . ? 2.472 21.342 7.704 1.00 26.84 ? 803 HOH A O 1 HETATM 5164 O O . HOH Z 9 . ? -4.924 -18.413 6.511 1.00 63.34 ? 804 HOH A O 1 HETATM 5165 O O . HOH Z 9 . ? 19.966 -6.828 55.410 1.00 38.20 ? 805 HOH A O 1 HETATM 5166 O O . HOH Z 9 . ? -7.162 -4.730 49.560 1.00 51.07 ? 806 HOH A O 1 HETATM 5167 O O . HOH Z 9 . ? 16.764 -4.413 -2.945 1.00 64.98 ? 807 HOH A O 1 HETATM 5168 O O . HOH Z 9 . ? -6.327 -6.563 -10.217 1.00 63.96 ? 808 HOH A O 1 HETATM 5169 O O . HOH Z 9 . ? 31.394 -15.809 22.303 1.00 26.29 ? 809 HOH A O 1 HETATM 5170 O O . HOH Z 9 . ? 26.131 14.343 18.542 1.00 38.81 ? 810 HOH A O 1 HETATM 5171 O O . HOH Z 9 . ? 24.619 13.476 47.925 1.00 54.97 ? 811 HOH A O 1 HETATM 5172 O O . HOH Z 9 . ? 7.075 29.326 7.781 1.00 48.52 ? 812 HOH A O 1 HETATM 5173 O O . HOH Z 9 . ? 24.417 -1.972 -3.472 1.00 57.20 ? 813 HOH A O 1 HETATM 5174 O O . HOH Z 9 . ? -0.139 6.905 45.464 1.00 62.74 ? 814 HOH A O 1 HETATM 5175 O O . HOH Z 9 . ? 30.146 11.709 18.019 1.00 45.08 ? 815 HOH A O 1 HETATM 5176 O O . HOH Z 9 . ? -16.087 -15.071 12.959 1.00 51.71 ? 816 HOH A O 1 HETATM 5177 O O . HOH Z 9 . ? 18.204 13.930 53.134 1.00 44.61 ? 817 HOH A O 1 HETATM 5178 O O . HOH Z 9 . ? -16.827 -9.175 7.431 1.00 31.82 ? 818 HOH A O 1 HETATM 5179 O O . HOH Z 9 . ? 20.967 -17.144 35.907 1.00 29.61 ? 819 HOH A O 1 HETATM 5180 O O . HOH Z 9 . ? -1.124 2.069 55.250 1.00 56.51 ? 820 HOH A O 1 HETATM 5181 O O . HOH Z 9 . ? 6.393 19.388 32.962 1.00 41.86 ? 821 HOH A O 1 HETATM 5182 O O . HOH Z 9 . ? 13.340 -19.037 21.050 1.00 41.33 ? 822 HOH A O 1 HETATM 5183 O O . HOH Z 9 . ? 24.269 -3.894 22.951 1.00 23.59 ? 823 HOH A O 1 HETATM 5184 O O . HOH Z 9 . ? 15.193 -20.985 47.259 1.00 50.54 ? 824 HOH A O 1 HETATM 5185 O O . HOH Z 9 . ? 10.269 9.353 51.078 1.00 53.17 ? 825 HOH A O 1 HETATM 5186 O O . HOH Z 9 . ? 1.412 28.990 20.249 1.00 47.78 ? 826 HOH A O 1 HETATM 5187 O O . HOH Z 9 . ? -11.103 0.611 41.839 1.00 68.45 ? 827 HOH A O 1 HETATM 5188 O O . HOH Z 9 . ? -7.425 -5.888 3.323 1.00 38.74 ? 828 HOH A O 1 HETATM 5189 O O . HOH Z 9 . ? -18.211 5.042 -2.752 1.00 54.55 ? 829 HOH A O 1 HETATM 5190 O O . HOH Z 9 . ? 1.620 -17.439 41.122 1.00 31.57 ? 830 HOH A O 1 HETATM 5191 O O . HOH Z 9 . ? -17.237 -21.756 14.064 1.00 53.78 ? 831 HOH A O 1 HETATM 5192 O O . HOH Z 9 . ? 22.294 -5.331 51.418 1.00 48.73 ? 832 HOH A O 1 HETATM 5193 O O . HOH Z 9 . ? 2.045 -14.806 46.883 1.00 81.46 ? 833 HOH A O 1 HETATM 5194 O O . HOH Z 9 . ? 20.924 -21.112 33.819 1.00 39.98 ? 834 HOH A O 1 HETATM 5195 O O . HOH Z 9 . ? -3.065 -4.623 36.207 1.00 62.94 ? 835 HOH A O 1 HETATM 5196 O O . HOH Z 9 . ? 12.666 29.982 8.542 1.00 56.79 ? 836 HOH A O 1 HETATM 5197 O O . HOH Z 9 . ? 1.153 -11.747 45.679 1.00 47.97 ? 837 HOH A O 1 HETATM 5198 O O . HOH Z 9 . ? 4.693 -9.609 50.868 1.00 55.42 ? 838 HOH A O 1 HETATM 5199 O O . HOH Z 9 . ? 2.723 -29.783 11.202 1.00 42.79 ? 839 HOH A O 1 HETATM 5200 O O . HOH Z 9 . ? 30.101 -1.809 11.534 1.00 28.08 ? 840 HOH A O 1 HETATM 5201 O O . HOH Z 9 . ? 22.824 16.127 30.466 1.00 28.29 ? 841 HOH A O 1 HETATM 5202 O O . HOH Z 9 . ? 25.928 -5.567 1.407 1.00 55.73 ? 842 HOH A O 1 HETATM 5203 O O . HOH Z 9 . ? -9.703 15.473 15.233 1.00 42.27 ? 843 HOH A O 1 HETATM 5204 O O . HOH Z 9 . ? -7.549 -12.189 25.400 1.00 45.62 ? 844 HOH A O 1 HETATM 5205 O O . HOH Z 9 . ? 15.182 -25.664 11.492 1.00 54.13 ? 845 HOH A O 1 HETATM 5206 O O . HOH Z 9 . ? -23.720 -0.768 -4.044 1.00 58.28 ? 846 HOH A O 1 HETATM 5207 O O . HOH Z 9 . ? 11.361 -0.837 52.265 1.00 58.75 ? 847 HOH A O 1 HETATM 5208 O O . HOH Z 9 . ? 25.303 -9.404 42.890 1.00 31.79 ? 848 HOH A O 1 HETATM 5209 O O . HOH Z 9 . ? -5.417 -16.834 45.467 1.00 70.87 ? 849 HOH A O 1 HETATM 5210 O O . HOH Z 9 . ? 30.491 1.799 23.100 1.00 58.08 ? 850 HOH A O 1 HETATM 5211 O O . HOH Z 9 . ? 3.694 18.009 -3.484 1.00 42.39 ? 851 HOH A O 1 HETATM 5212 O O . HOH Z 9 . ? 1.548 -15.171 25.893 1.00 18.30 ? 852 HOH A O 1 HETATM 5213 O O . HOH Z 9 . ? 6.507 -16.657 47.047 1.00 42.22 ? 853 HOH A O 1 HETATM 5214 O O . HOH Z 9 . ? 1.506 -25.746 46.693 1.00 62.49 ? 854 HOH A O 1 HETATM 5215 O O . HOH Z 9 . ? 28.991 9.600 54.497 1.00 57.52 ? 855 HOH A O 1 HETATM 5216 O O . HOH Z 9 . ? -14.411 -4.224 16.758 1.00 42.83 ? 856 HOH A O 1 HETATM 5217 O O . HOH Z 9 . ? 1.410 -23.517 48.771 1.00 54.69 ? 857 HOH A O 1 HETATM 5218 O O . HOH Z 9 . ? -15.427 -10.489 4.565 1.00 73.88 ? 858 HOH A O 1 HETATM 5219 O O . HOH Z 9 . ? -17.715 5.126 10.555 1.00 50.86 ? 859 HOH A O 1 HETATM 5220 O O . HOH Z 9 . ? -7.145 -21.330 28.243 1.00 56.50 ? 860 HOH A O 1 HETATM 5221 O O . HOH Z 9 . ? 22.713 -5.708 0.356 1.00 76.16 ? 861 HOH A O 1 HETATM 5222 O O . HOH Z 9 . ? -14.254 -14.609 29.743 1.00 62.52 ? 862 HOH A O 1 HETATM 5223 O O . HOH Z 9 . ? 18.121 -4.397 26.469 1.00 43.02 ? 863 HOH A O 1 HETATM 5224 O O . HOH Z 9 . ? 6.108 27.432 21.118 1.00 60.76 ? 864 HOH A O 1 HETATM 5225 O O . HOH Z 9 . ? -23.100 -1.186 8.812 1.00 46.88 ? 865 HOH A O 1 HETATM 5226 O O . HOH Z 9 . ? -23.642 -11.633 -6.388 1.00 58.46 ? 866 HOH A O 1 HETATM 5227 O O . HOH Z 9 . ? -0.204 4.354 2.463 1.00 31.07 ? 867 HOH A O 1 HETATM 5228 O O . HOH Z 9 . ? 8.668 -21.068 23.348 1.00 43.32 ? 868 HOH A O 1 HETATM 5229 O O . HOH Z 9 . ? 1.147 16.180 2.170 1.00 28.42 ? 869 HOH A O 1 HETATM 5230 O O . HOH Z 9 . ? -4.936 5.351 24.859 1.00 24.60 ? 870 HOH A O 1 HETATM 5231 O O . HOH Z 9 . ? -12.099 14.104 27.521 1.00 34.64 ? 871 HOH A O 1 HETATM 5232 O O . HOH Z 9 . ? -3.747 22.656 39.783 1.00 42.98 ? 872 HOH A O 1 HETATM 5233 O O . HOH Z 9 . ? 1.186 17.527 43.231 1.00 36.79 ? 873 HOH A O 1 HETATM 5234 O O . HOH Z 9 . ? -2.244 -9.402 39.015 1.00 24.15 ? 874 HOH A O 1 HETATM 5235 O O . HOH Z 9 . ? 14.325 26.208 21.696 1.00 29.67 ? 875 HOH A O 1 HETATM 5236 O O . HOH Z 9 . ? -10.062 -20.603 28.297 1.00 59.57 ? 876 HOH A O 1 HETATM 5237 O O . HOH Z 9 . ? 27.273 4.536 47.331 1.00 38.63 ? 877 HOH A O 1 HETATM 5238 O O . HOH Z 9 . ? -4.322 -12.226 15.215 1.00 39.06 ? 878 HOH A O 1 HETATM 5239 O O . HOH Z 9 . ? 17.522 14.601 18.053 1.00 25.40 ? 879 HOH A O 1 HETATM 5240 O O . HOH Z 9 . ? -19.726 12.092 19.213 1.00 55.95 ? 880 HOH A O 1 HETATM 5241 O O . HOH Z 9 . ? 20.076 16.251 15.511 1.00 46.54 ? 881 HOH A O 1 HETATM 5242 O O . HOH Z 9 . ? -2.230 22.900 13.313 1.00 47.63 ? 882 HOH A O 1 HETATM 5243 O O . HOH Z 9 . ? -4.407 -26.185 36.421 1.00 45.54 ? 883 HOH A O 1 HETATM 5244 O O . HOH Z 9 . ? -9.154 -20.392 30.725 1.00 70.06 ? 884 HOH A O 1 HETATM 5245 O O . HOH Z 9 . ? 23.415 -3.757 -5.513 1.00 55.83 ? 885 HOH A O 1 HETATM 5246 O O . HOH Z 9 . ? 6.202 -15.359 31.941 1.00 31.02 ? 886 HOH A O 1 HETATM 5247 O O . HOH Z 9 . ? 34.110 6.455 34.918 1.00 36.66 ? 887 HOH A O 1 HETATM 5248 O O . HOH Z 9 . ? 16.534 4.400 -3.455 1.00 51.63 ? 888 HOH A O 1 HETATM 5249 O O . HOH Z 9 . ? -13.264 -9.223 -4.687 1.00 40.16 ? 889 HOH A O 1 HETATM 5250 O O . HOH Z 9 . ? 7.635 -6.288 30.010 1.00 29.15 ? 890 HOH A O 1 HETATM 5251 O O . HOH Z 9 . ? -5.684 10.917 5.902 1.00 52.54 ? 891 HOH A O 1 HETATM 5252 O O . HOH Z 9 . ? -0.277 -28.363 42.167 1.00 51.13 ? 892 HOH A O 1 HETATM 5253 O O . HOH Z 9 . ? 25.622 -6.172 7.347 1.00 54.20 ? 893 HOH A O 1 HETATM 5254 O O . HOH Z 9 . ? -9.916 -20.873 13.816 1.00 37.76 ? 894 HOH A O 1 HETATM 5255 O O . HOH Z 9 . ? -1.815 13.523 46.120 1.00 52.24 ? 895 HOH A O 1 HETATM 5256 O O . HOH Z 9 . ? -0.809 -26.107 20.027 1.00 49.54 ? 896 HOH A O 1 HETATM 5257 O O . HOH Z 9 . ? -10.725 -23.964 9.809 1.00 52.26 ? 897 HOH A O 1 HETATM 5258 O O . HOH Z 9 . ? -5.081 -18.814 47.083 1.00 52.76 ? 898 HOH A O 1 HETATM 5259 O O . HOH Z 9 . ? 18.109 18.042 28.595 1.00 43.02 ? 899 HOH A O 1 HETATM 5260 O O . HOH Z 9 . ? 8.393 27.440 19.610 1.00 48.78 ? 900 HOH A O 1 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 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 LYS 14 14 14 LYS LYS 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 ASN 18 18 18 ASN ASN 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 LEU 57 57 57 LEU LEU 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 ASN 122 122 122 ASN ASN 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 THR 127 127 127 THR THR 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 ILE 134 134 134 ILE ILE 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 ASN 138 138 138 ASN ASN 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 GLU 178 178 178 GLU GLU 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 SEP 198 198 198 SEP SEP 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 LEU 227 227 227 LEU LEU 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 LYS 232 232 232 LYS LYS 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 ARG 245 245 245 ARG ARG 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 LEU 250 250 250 LEU LEU 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 PHE 254 254 254 PHE PHE 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 ALA 265 265 265 ALA ALA 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 LYS 282 282 282 LYS LYS 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 ASN 288 288 288 ASN ASN 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 LYS 291 291 291 LYS LYS 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 LYS 403 403 403 LYS LYS 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 ASP 410 410 410 ASP ASP 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 ILE 428 428 428 ILE ILE 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 THR 469 469 469 THR THR 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 ILE 475 475 475 ILE ILE 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 MET 481 481 481 MET MET 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 THR 581 581 581 THR THR 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 # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 NAG 1 596 1 NAG NAG A . C 2 NAG 2 597 2 NAG NAG A . D 3 MAN 3 598 10 MAN MAN A . E 2 NAG 1 599 3 NAG NAG A . F 2 NAG 2 600 4 NAG NAG A . G 2 NAG 1 601 705 NAG NAG A . H 2 NAG 2 602 706 NAG NAG A . I 3 MAN 3 603 709 MAN MAN A . J 2 NAG 1 604 7 NAG NAG A . K 2 NAG 2 605 8 NAG NAG A . L 4 CA 1 606 606 CA CA A . M 5 SCN 1 607 312 SCN SCN A . N 6 IOD 1 608 301 IOD IOD A . O 6 IOD 1 609 302 IOD IOD A . P 6 IOD 1 610 303 IOD IOD A . Q 6 IOD 1 611 304 IOD IOD A . R 6 IOD 1 612 305 IOD IOD A . S 6 IOD 1 613 306 IOD IOD A . T 6 IOD 1 614 307 IOD IOD A . U 6 IOD 1 615 308 IOD IOD A . V 6 IOD 1 616 309 IOD IOD A . W 6 IOD 1 617 310 IOD IOD A . X 7 HEM 1 618 605 HEM HEM A . Y 8 CAQ 1 619 311 CAQ CAQ A . Z 9 HOH 1 620 1 HOH HOH A . Z 9 HOH 2 621 2 HOH HOH A . Z 9 HOH 3 622 3 HOH HOH A . Z 9 HOH 4 623 4 HOH HOH A . Z 9 HOH 5 624 5 HOH HOH A . Z 9 HOH 6 625 6 HOH HOH A . Z 9 HOH 7 626 7 HOH HOH A . Z 9 HOH 8 627 8 HOH HOH A . Z 9 HOH 9 628 9 HOH HOH A . Z 9 HOH 10 629 10 HOH HOH A . Z 9 HOH 11 630 11 HOH HOH A . Z 9 HOH 12 631 12 HOH HOH A . Z 9 HOH 13 632 13 HOH HOH A . Z 9 HOH 14 633 14 HOH HOH A . Z 9 HOH 15 634 15 HOH HOH A . Z 9 HOH 16 635 16 HOH HOH A . Z 9 HOH 17 636 17 HOH HOH A . Z 9 HOH 18 637 18 HOH HOH A . Z 9 HOH 19 638 19 HOH HOH A . Z 9 HOH 20 639 20 HOH HOH A . Z 9 HOH 21 640 21 HOH HOH A . Z 9 HOH 22 641 22 HOH HOH A . Z 9 HOH 23 642 23 HOH HOH A . Z 9 HOH 24 643 24 HOH HOH A . Z 9 HOH 25 644 25 HOH HOH A . Z 9 HOH 26 645 26 HOH HOH A . Z 9 HOH 27 646 27 HOH HOH A . Z 9 HOH 28 647 28 HOH HOH A . Z 9 HOH 29 648 29 HOH HOH A . Z 9 HOH 30 649 30 HOH HOH A . Z 9 HOH 31 650 31 HOH HOH A . Z 9 HOH 32 651 32 HOH HOH A . Z 9 HOH 33 652 33 HOH HOH A . Z 9 HOH 34 653 34 HOH HOH A . Z 9 HOH 35 654 35 HOH HOH A . Z 9 HOH 36 655 36 HOH HOH A . Z 9 HOH 37 656 37 HOH HOH A . Z 9 HOH 38 657 38 HOH HOH A . Z 9 HOH 39 658 39 HOH HOH A . Z 9 HOH 40 659 40 HOH HOH A . Z 9 HOH 41 660 41 HOH HOH A . Z 9 HOH 42 661 42 HOH HOH A . Z 9 HOH 43 662 43 HOH HOH A . Z 9 HOH 44 663 44 HOH HOH A . Z 9 HOH 45 664 45 HOH HOH A . Z 9 HOH 46 665 46 HOH HOH A . Z 9 HOH 47 666 47 HOH HOH A . Z 9 HOH 48 667 48 HOH HOH A . Z 9 HOH 49 668 49 HOH HOH A . Z 9 HOH 50 669 50 HOH HOH A . Z 9 HOH 51 670 51 HOH HOH A . Z 9 HOH 52 671 52 HOH HOH A . Z 9 HOH 53 672 53 HOH HOH A . Z 9 HOH 54 673 54 HOH HOH A . Z 9 HOH 55 674 55 HOH HOH A . Z 9 HOH 56 675 56 HOH HOH A . Z 9 HOH 57 676 57 HOH HOH A . Z 9 HOH 58 677 58 HOH HOH A . Z 9 HOH 59 678 59 HOH HOH A . Z 9 HOH 60 679 60 HOH HOH A . Z 9 HOH 61 680 61 HOH HOH A . Z 9 HOH 62 681 62 HOH HOH A . Z 9 HOH 63 682 63 HOH HOH A . Z 9 HOH 64 683 64 HOH HOH A . Z 9 HOH 65 684 65 HOH HOH A . Z 9 HOH 66 685 66 HOH HOH A . Z 9 HOH 67 686 67 HOH HOH A . Z 9 HOH 68 687 68 HOH HOH A . Z 9 HOH 69 688 69 HOH HOH A . Z 9 HOH 70 689 70 HOH HOH A . Z 9 HOH 71 690 71 HOH HOH A . Z 9 HOH 72 691 72 HOH HOH A . Z 9 HOH 73 692 73 HOH HOH A . Z 9 HOH 74 693 74 HOH HOH A . Z 9 HOH 75 694 75 HOH HOH A . Z 9 HOH 76 695 76 HOH HOH A . Z 9 HOH 77 696 77 HOH HOH A . Z 9 HOH 78 697 78 HOH HOH A . Z 9 HOH 79 698 79 HOH HOH A . Z 9 HOH 80 699 80 HOH HOH A . Z 9 HOH 81 700 81 HOH HOH A . Z 9 HOH 82 701 82 HOH HOH A . Z 9 HOH 83 702 83 HOH HOH A . Z 9 HOH 84 703 84 HOH HOH A . Z 9 HOH 85 704 85 HOH HOH A . Z 9 HOH 86 705 86 HOH HOH A . Z 9 HOH 87 706 87 HOH HOH A . Z 9 HOH 88 707 88 HOH HOH A . Z 9 HOH 89 708 89 HOH HOH A . Z 9 HOH 90 709 90 HOH HOH A . Z 9 HOH 91 710 91 HOH HOH A . Z 9 HOH 92 711 92 HOH HOH A . Z 9 HOH 93 712 93 HOH HOH A . Z 9 HOH 94 713 94 HOH HOH A . Z 9 HOH 95 714 95 HOH HOH A . Z 9 HOH 96 715 96 HOH HOH A . Z 9 HOH 97 716 97 HOH HOH A . Z 9 HOH 98 717 98 HOH HOH A . Z 9 HOH 99 718 99 HOH HOH A . Z 9 HOH 100 719 100 HOH HOH A . Z 9 HOH 101 720 101 HOH HOH A . Z 9 HOH 102 721 102 HOH HOH A . Z 9 HOH 103 722 103 HOH HOH A . Z 9 HOH 104 723 104 HOH HOH A . Z 9 HOH 105 724 105 HOH HOH A . Z 9 HOH 106 725 106 HOH HOH A . Z 9 HOH 107 726 107 HOH HOH A . Z 9 HOH 108 727 108 HOH HOH A . Z 9 HOH 109 728 109 HOH HOH A . Z 9 HOH 110 729 110 HOH HOH A . Z 9 HOH 111 730 111 HOH HOH A . Z 9 HOH 112 731 112 HOH HOH A . Z 9 HOH 113 732 113 HOH HOH A . Z 9 HOH 114 733 114 HOH HOH A . Z 9 HOH 115 734 115 HOH HOH A . Z 9 HOH 116 735 116 HOH HOH A . Z 9 HOH 117 736 117 HOH HOH A . Z 9 HOH 118 737 118 HOH HOH A . Z 9 HOH 119 738 119 HOH HOH A . Z 9 HOH 120 739 120 HOH HOH A . Z 9 HOH 121 740 121 HOH HOH A . Z 9 HOH 122 741 122 HOH HOH A . Z 9 HOH 123 742 123 HOH HOH A . Z 9 HOH 124 743 124 HOH HOH A . Z 9 HOH 125 744 125 HOH HOH A . Z 9 HOH 126 745 126 HOH HOH A . Z 9 HOH 127 746 127 HOH HOH A . Z 9 HOH 128 747 128 HOH HOH A . Z 9 HOH 129 748 129 HOH HOH A . Z 9 HOH 130 749 130 HOH HOH A . Z 9 HOH 131 750 131 HOH HOH A . Z 9 HOH 132 751 132 HOH HOH A . Z 9 HOH 133 752 133 HOH HOH A . Z 9 HOH 134 753 134 HOH HOH A . Z 9 HOH 135 754 135 HOH HOH A . Z 9 HOH 136 755 136 HOH HOH A . Z 9 HOH 137 756 137 HOH HOH A . Z 9 HOH 138 757 138 HOH HOH A . Z 9 HOH 139 758 139 HOH HOH A . Z 9 HOH 140 759 140 HOH HOH A . Z 9 HOH 141 760 141 HOH HOH A . Z 9 HOH 142 761 142 HOH HOH A . Z 9 HOH 143 762 143 HOH HOH A . Z 9 HOH 144 763 144 HOH HOH A . Z 9 HOH 145 764 145 HOH HOH A . Z 9 HOH 146 765 146 HOH HOH A . Z 9 HOH 147 766 147 HOH HOH A . Z 9 HOH 148 767 148 HOH HOH A . Z 9 HOH 149 768 149 HOH HOH A . Z 9 HOH 150 769 150 HOH HOH A . Z 9 HOH 151 770 151 HOH HOH A . Z 9 HOH 152 771 152 HOH HOH A . Z 9 HOH 153 772 153 HOH HOH A . Z 9 HOH 154 773 154 HOH HOH A . Z 9 HOH 155 774 155 HOH HOH A . Z 9 HOH 156 775 156 HOH HOH A . Z 9 HOH 157 776 157 HOH HOH A . Z 9 HOH 158 777 158 HOH HOH A . Z 9 HOH 159 778 159 HOH HOH A . Z 9 HOH 160 779 160 HOH HOH A . Z 9 HOH 161 780 161 HOH HOH A . Z 9 HOH 162 781 162 HOH HOH A . Z 9 HOH 163 782 163 HOH HOH A . Z 9 HOH 164 783 164 HOH HOH A . Z 9 HOH 165 784 165 HOH HOH A . Z 9 HOH 166 785 166 HOH HOH A . Z 9 HOH 167 786 167 HOH HOH A . Z 9 HOH 168 787 168 HOH HOH A . Z 9 HOH 169 788 169 HOH HOH A . Z 9 HOH 170 789 170 HOH HOH A . Z 9 HOH 171 790 171 HOH HOH A . Z 9 HOH 172 791 172 HOH HOH A . Z 9 HOH 173 792 173 HOH HOH A . Z 9 HOH 174 793 174 HOH HOH A . Z 9 HOH 175 794 175 HOH HOH A . Z 9 HOH 176 795 176 HOH HOH A . Z 9 HOH 177 796 177 HOH HOH A . Z 9 HOH 178 797 178 HOH HOH A . Z 9 HOH 179 798 179 HOH HOH A . Z 9 HOH 180 799 180 HOH HOH A . Z 9 HOH 181 800 181 HOH HOH A . Z 9 HOH 182 801 182 HOH HOH A . Z 9 HOH 183 802 183 HOH HOH A . Z 9 HOH 184 803 184 HOH HOH A . Z 9 HOH 185 804 185 HOH HOH A . Z 9 HOH 186 805 186 HOH HOH A . Z 9 HOH 187 806 187 HOH HOH A . Z 9 HOH 188 807 188 HOH HOH A . Z 9 HOH 189 808 189 HOH HOH A . Z 9 HOH 190 809 190 HOH HOH A . Z 9 HOH 191 810 191 HOH HOH A . Z 9 HOH 192 811 192 HOH HOH A . Z 9 HOH 193 812 193 HOH HOH A . Z 9 HOH 194 813 194 HOH HOH A . Z 9 HOH 195 814 195 HOH HOH A . Z 9 HOH 196 815 196 HOH HOH A . Z 9 HOH 197 816 197 HOH HOH A . Z 9 HOH 198 817 198 HOH HOH A . Z 9 HOH 199 818 199 HOH HOH A . Z 9 HOH 200 819 200 HOH HOH A . Z 9 HOH 201 820 201 HOH HOH A . Z 9 HOH 202 821 202 HOH HOH A . Z 9 HOH 203 822 203 HOH HOH A . Z 9 HOH 204 823 204 HOH HOH A . Z 9 HOH 205 824 205 HOH HOH A . Z 9 HOH 206 825 206 HOH HOH A . Z 9 HOH 207 826 207 HOH HOH A . Z 9 HOH 208 827 208 HOH HOH A . Z 9 HOH 209 828 209 HOH HOH A . Z 9 HOH 210 829 210 HOH HOH A . Z 9 HOH 211 830 211 HOH HOH A . Z 9 HOH 212 831 212 HOH HOH A . Z 9 HOH 213 832 213 HOH HOH A . Z 9 HOH 214 833 214 HOH HOH A . Z 9 HOH 215 834 215 HOH HOH A . Z 9 HOH 216 835 216 HOH HOH A . Z 9 HOH 217 836 217 HOH HOH A . Z 9 HOH 218 837 218 HOH HOH A . Z 9 HOH 219 838 219 HOH HOH A . Z 9 HOH 220 839 220 HOH HOH A . Z 9 HOH 221 840 221 HOH HOH A . Z 9 HOH 222 841 222 HOH HOH A . Z 9 HOH 223 842 223 HOH HOH A . Z 9 HOH 224 843 224 HOH HOH A . Z 9 HOH 225 844 225 HOH HOH A . Z 9 HOH 226 845 226 HOH HOH A . Z 9 HOH 227 846 227 HOH HOH A . Z 9 HOH 228 847 228 HOH HOH A . Z 9 HOH 229 848 229 HOH HOH A . Z 9 HOH 230 849 230 HOH HOH A . Z 9 HOH 231 850 231 HOH HOH A . Z 9 HOH 232 851 232 HOH HOH A . Z 9 HOH 233 852 233 HOH HOH A . Z 9 HOH 234 853 234 HOH HOH A . Z 9 HOH 235 854 235 HOH HOH A . Z 9 HOH 236 855 236 HOH HOH A . Z 9 HOH 237 856 237 HOH HOH A . Z 9 HOH 238 857 238 HOH HOH A . Z 9 HOH 239 858 239 HOH HOH A . Z 9 HOH 240 859 240 HOH HOH A . Z 9 HOH 241 860 241 HOH HOH A . Z 9 HOH 242 861 242 HOH HOH A . Z 9 HOH 243 862 243 HOH HOH A . Z 9 HOH 244 863 244 HOH HOH A . Z 9 HOH 245 864 245 HOH HOH A . Z 9 HOH 246 865 246 HOH HOH A . Z 9 HOH 247 866 247 HOH HOH A . Z 9 HOH 248 867 248 HOH HOH A . Z 9 HOH 249 868 249 HOH HOH A . Z 9 HOH 250 869 250 HOH HOH A . Z 9 HOH 251 870 251 HOH HOH A . Z 9 HOH 252 871 252 HOH HOH A . Z 9 HOH 253 872 253 HOH HOH A . Z 9 HOH 254 873 254 HOH HOH A . Z 9 HOH 255 874 255 HOH HOH A . Z 9 HOH 256 875 256 HOH HOH A . Z 9 HOH 257 876 257 HOH HOH A . Z 9 HOH 258 877 258 HOH HOH A . Z 9 HOH 259 878 259 HOH HOH A . Z 9 HOH 260 879 260 HOH HOH A . Z 9 HOH 261 880 261 HOH HOH A . Z 9 HOH 262 881 262 HOH HOH A . Z 9 HOH 263 882 263 HOH HOH A . Z 9 HOH 264 883 264 HOH HOH A . Z 9 HOH 265 884 265 HOH HOH A . Z 9 HOH 266 885 266 HOH HOH A . Z 9 HOH 267 886 267 HOH HOH A . Z 9 HOH 268 887 268 HOH HOH A . Z 9 HOH 269 888 269 HOH HOH A . Z 9 HOH 270 889 270 HOH HOH A . Z 9 HOH 271 890 271 HOH HOH A . Z 9 HOH 272 891 272 HOH HOH A . Z 9 HOH 273 892 273 HOH HOH A . Z 9 HOH 274 893 274 HOH HOH A . Z 9 HOH 275 894 275 HOH HOH A . Z 9 HOH 276 895 276 HOH HOH A . Z 9 HOH 277 896 277 HOH HOH A . Z 9 HOH 278 897 278 HOH HOH A . Z 9 HOH 279 898 279 HOH HOH A . Z 9 HOH 280 899 280 HOH HOH A . Z 9 HOH 281 900 281 HOH HOH A . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 95 A ASN 95 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 205 A ASN 205 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 332 A ASN 332 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 241 A ASN 241 ? ASN 'GLYCOSYLATION SITE' 5 A SEP 198 A SEP 198 ? SER PHOSPHOSERINE # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_defined_assembly _pdbx_struct_assembly.method_details ? _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 NE2 ? A HIS 351 ? A HIS 351 ? 1_555 FE ? X HEM . ? A HEM 618 ? 1_555 NA ? X HEM . ? A HEM 618 ? 1_555 107.8 ? 2 NE2 ? A HIS 351 ? A HIS 351 ? 1_555 FE ? X HEM . ? A HEM 618 ? 1_555 NB ? X HEM . ? A HEM 618 ? 1_555 98.6 ? 3 NA ? X HEM . ? A HEM 618 ? 1_555 FE ? X HEM . ? A HEM 618 ? 1_555 NB ? X HEM . ? A HEM 618 ? 1_555 89.9 ? 4 NE2 ? A HIS 351 ? A HIS 351 ? 1_555 FE ? X HEM . ? A HEM 618 ? 1_555 NC ? X HEM . ? A HEM 618 ? 1_555 82.7 ? 5 NA ? X HEM . ? A HEM 618 ? 1_555 FE ? X HEM . ? A HEM 618 ? 1_555 NC ? X HEM . ? A HEM 618 ? 1_555 169.5 ? 6 NB ? X HEM . ? A HEM 618 ? 1_555 FE ? X HEM . ? A HEM 618 ? 1_555 NC ? X HEM . ? A HEM 618 ? 1_555 87.0 ? 7 NE2 ? A HIS 351 ? A HIS 351 ? 1_555 FE ? X HEM . ? A HEM 618 ? 1_555 ND ? X HEM . ? A HEM 618 ? 1_555 89.7 ? 8 NA ? X HEM . ? A HEM 618 ? 1_555 FE ? X HEM . ? A HEM 618 ? 1_555 ND ? X HEM . ? A HEM 618 ? 1_555 93.6 ? 9 NB ? X HEM . ? A HEM 618 ? 1_555 FE ? X HEM . ? A HEM 618 ? 1_555 ND ? X HEM . ? A HEM 618 ? 1_555 169.5 ? 10 NC ? X HEM . ? A HEM 618 ? 1_555 FE ? X HEM . ? A HEM 618 ? 1_555 ND ? X HEM . ? A HEM 618 ? 1_555 87.8 ? 11 NE2 ? A HIS 351 ? A HIS 351 ? 1_555 FE ? X HEM . ? A HEM 618 ? 1_555 O ? Z HOH . ? A HOH 649 ? 1_555 177.2 ? 12 NA ? X HEM . ? A HEM 618 ? 1_555 FE ? X HEM . ? A HEM 618 ? 1_555 O ? Z HOH . ? A HOH 649 ? 1_555 74.6 ? 13 NB ? X HEM . ? A HEM 618 ? 1_555 FE ? X HEM . ? A HEM 618 ? 1_555 O ? Z HOH . ? A HOH 649 ? 1_555 82.8 ? 14 NC ? X HEM . ? A HEM 618 ? 1_555 FE ? X HEM . ? A HEM 618 ? 1_555 O ? Z HOH . ? A HOH 649 ? 1_555 95.0 ? 15 ND ? X HEM . ? A HEM 618 ? 1_555 FE ? X HEM . ? A HEM 618 ? 1_555 O ? Z HOH . ? A HOH 649 ? 1_555 88.6 ? 16 O ? A ASP 110 ? A ASP 110 ? 1_555 CA ? L CA . ? A CA 606 ? 1_555 OD1 ? A ASP 110 ? A ASP 110 ? 1_555 75.4 ? 17 O ? A ASP 110 ? A ASP 110 ? 1_555 CA ? L CA . ? A CA 606 ? 1_555 O ? A THR 184 ? A THR 184 ? 1_555 77.1 ? 18 OD1 ? A ASP 110 ? A ASP 110 ? 1_555 CA ? L CA . ? A CA 606 ? 1_555 O ? A THR 184 ? A THR 184 ? 1_555 141.0 ? 19 O ? A ASP 110 ? A ASP 110 ? 1_555 CA ? L CA . ? A CA 606 ? 1_555 OG1 ? A THR 184 ? A THR 184 ? 1_555 127.8 ? 20 OD1 ? A ASP 110 ? A ASP 110 ? 1_555 CA ? L CA . ? A CA 606 ? 1_555 OG1 ? A THR 184 ? A THR 184 ? 1_555 151.3 ? 21 O ? A THR 184 ? A THR 184 ? 1_555 CA ? L CA . ? A CA 606 ? 1_555 OG1 ? A THR 184 ? A THR 184 ? 1_555 67.1 ? 22 O ? A ASP 110 ? A ASP 110 ? 1_555 CA ? L CA . ? A CA 606 ? 1_555 O ? A PHE 186 ? A PHE 186 ? 1_555 126.6 ? 23 OD1 ? A ASP 110 ? A ASP 110 ? 1_555 CA ? L CA . ? A CA 606 ? 1_555 O ? A PHE 186 ? A PHE 186 ? 1_555 87.6 ? 24 O ? A THR 184 ? A THR 184 ? 1_555 CA ? L CA . ? A CA 606 ? 1_555 O ? A PHE 186 ? A PHE 186 ? 1_555 87.0 ? 25 OG1 ? A THR 184 ? A THR 184 ? 1_555 CA ? L CA . ? A CA 606 ? 1_555 O ? A PHE 186 ? A PHE 186 ? 1_555 88.9 ? 26 O ? A ASP 110 ? A ASP 110 ? 1_555 CA ? L CA . ? A CA 606 ? 1_555 OD1 ? A ASP 188 ? A ASP 188 ? 1_555 153.5 ? 27 OD1 ? A ASP 110 ? A ASP 110 ? 1_555 CA ? L CA . ? A CA 606 ? 1_555 OD1 ? A ASP 188 ? A ASP 188 ? 1_555 82.1 ? 28 O ? A THR 184 ? A THR 184 ? 1_555 CA ? L CA . ? A CA 606 ? 1_555 OD1 ? A ASP 188 ? A ASP 188 ? 1_555 129.3 ? 29 OG1 ? A THR 184 ? A THR 184 ? 1_555 CA ? L CA . ? A CA 606 ? 1_555 OD1 ? A ASP 188 ? A ASP 188 ? 1_555 70.7 ? 30 O ? A PHE 186 ? A PHE 186 ? 1_555 CA ? L CA . ? A CA 606 ? 1_555 OD1 ? A ASP 188 ? A ASP 188 ? 1_555 65.2 ? 31 O ? A ASP 110 ? A ASP 110 ? 1_555 CA ? L CA . ? A CA 606 ? 1_555 OG ? A SER 190 ? A SER 190 ? 1_555 86.4 ? 32 OD1 ? A ASP 110 ? A ASP 110 ? 1_555 CA ? L CA . ? A CA 606 ? 1_555 OG ? A SER 190 ? A SER 190 ? 1_555 86.6 ? 33 O ? A THR 184 ? A THR 184 ? 1_555 CA ? L CA . ? A CA 606 ? 1_555 OG ? A SER 190 ? A SER 190 ? 1_555 118.7 ? 34 OG1 ? A THR 184 ? A THR 184 ? 1_555 CA ? L CA . ? A CA 606 ? 1_555 OG ? A SER 190 ? A SER 190 ? 1_555 79.4 ? 35 O ? A PHE 186 ? A PHE 186 ? 1_555 CA ? L CA . ? A CA 606 ? 1_555 OG ? A SER 190 ? A SER 190 ? 1_555 143.5 ? 36 OD1 ? A ASP 188 ? A ASP 188 ? 1_555 CA ? L CA . ? A CA 606 ? 1_555 OG ? A SER 190 ? A SER 190 ? 1_555 78.3 ? # 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 2007-05-22 2 'Structure model' 1 1 2008-05-01 3 'Structure model' 1 2 2011-07-13 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Version format compliance' 2 3 'Structure model' 'Non-polymer description' 3 3 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.0 ? 1 MAR345dtb 'data collection' . ? 2 DENZO 'data reduction' . ? 3 SCALEPACK 'data scaling' . ? 4 AMoRE phasing . ? 5 # 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 C A TRP 2 ? ? N A GLU 3 ? ? CA A GLU 3 ? ? 136.90 121.70 15.20 2.50 Y 2 1 N A GLU 3 ? ? CA A GLU 3 ? ? CB A GLU 3 ? ? 122.88 110.60 12.28 1.80 N 3 1 N A GLU 3 ? ? CA A GLU 3 ? ? C A GLU 3 ? ? 92.32 111.00 -18.68 2.70 N 4 1 CA A GLU 3 ? ? C A GLU 3 ? ? N A VAL 4 ? ? 98.02 117.20 -19.18 2.20 Y 5 1 C A GLU 3 ? ? N A VAL 4 ? ? CA A VAL 4 ? ? 141.69 121.70 19.99 2.50 Y 6 1 CB A ASP 27 ? ? CG A ASP 27 ? ? OD2 A ASP 27 ? ? 124.33 118.30 6.03 0.90 N 7 1 CB A GLU 118 ? B CA A GLU 118 ? B C A GLU 118 ? ? 86.37 110.40 -24.03 2.00 N 8 1 N A GLU 118 ? ? CA A GLU 118 ? B CB A GLU 118 ? B 83.96 110.60 -26.64 1.80 N 9 1 O A GLU 118 ? ? C A GLU 118 ? ? N A LEU 119 ? ? 106.17 122.70 -16.53 1.60 Y 10 1 CA A PRO 170 ? ? N A PRO 170 ? ? CD A PRO 170 ? ? 102.28 111.70 -9.42 1.40 N 11 1 CA A PRO 171 ? ? N A PRO 171 ? ? CD A PRO 171 ? ? 102.88 111.70 -8.82 1.40 N 12 1 CA A GLN 173 ? ? C A GLN 173 ? ? N A SER 174 ? ? 130.86 117.20 13.66 2.20 Y 13 1 C A GLU 196 ? ? N A PRO 197 ? ? CD A PRO 197 ? ? 115.66 128.40 -12.74 2.10 Y 14 1 C A PRO 197 ? ? N A SEP 198 ? ? CA A SEP 198 ? ? 148.45 121.70 26.75 2.50 Y 15 1 CB A ASP 253 ? ? CG A ASP 253 ? ? OD2 A ASP 253 ? ? 125.19 118.30 6.89 0.90 N 16 1 CB A ASP 336 ? ? CG A ASP 336 ? ? OD2 A ASP 336 ? ? 124.30 118.30 6.00 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 ? ? 67.28 76.09 2 1 GLU A 3 ? ? -169.62 32.25 3 1 VAL A 4 ? ? -5.23 -31.58 4 1 GLU A 17 ? ? 72.89 -3.52 5 1 ALA A 56 ? ? -160.09 -17.48 6 1 GLU A 118 ? ? -98.54 -65.49 7 1 GLU A 118 ? ? -96.85 -69.20 8 1 LEU A 119 ? ? 77.48 32.36 9 1 SER A 121 ? ? -98.32 56.19 10 1 ASN A 122 ? ? -145.91 -64.85 11 1 SER A 125 ? ? -141.49 -19.66 12 1 ASP A 137 ? ? 47.82 -132.84 13 1 ASN A 147 ? ? 84.34 -0.29 14 1 CYS A 167 ? ? 67.37 -121.20 15 1 PRO A 168 ? ? -53.51 -144.80 16 1 THR A 169 ? ? -157.55 -48.77 17 1 PRO A 171 ? ? -51.50 102.26 18 1 GLN A 173 ? ? -77.36 -75.60 19 1 LEU A 175 ? ? -176.57 -68.68 20 1 ALA A 176 ? ? 156.72 130.68 21 1 GLU A 371 ? ? -113.61 54.51 22 1 ASP A 389 ? ? -153.29 63.02 23 1 PRO A 424 ? ? -58.21 -6.54 24 1 ASN A 473 ? ? -161.44 109.23 25 1 LYS A 485 ? ? 73.45 -8.80 26 1 HIS A 558 ? ? -104.15 42.18 27 1 CYS A 579 ? ? -51.52 -5.81 28 1 SER A 580 ? ? -109.80 54.61 29 1 THR A 581 ? ? 178.90 -40.51 30 1 PRO A 589 ? ? -47.50 -2.38 # loop_ _pdbx_validate_main_chain_plane.id _pdbx_validate_main_chain_plane.PDB_model_num _pdbx_validate_main_chain_plane.auth_comp_id _pdbx_validate_main_chain_plane.auth_asym_id _pdbx_validate_main_chain_plane.auth_seq_id _pdbx_validate_main_chain_plane.PDB_ins_code _pdbx_validate_main_chain_plane.label_alt_id _pdbx_validate_main_chain_plane.improper_torsion_angle 1 1 GLU A 118 ? A 21.52 2 1 GLU A 118 ? B 22.67 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 ALPHA-D-MANNOSE MAN 4 'CALCIUM ION' CA 5 'THIOCYANATE ION' SCN 6 'IODIDE ION' IOD 7 'PROTOPORPHYRIN IX CONTAINING FE' HEM 8 CATECHOL CAQ 9 water HOH #