data_3FNL # _entry.id 3FNL # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.281 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 3FNL RCSB RCSB050811 WWPDB D_1000050811 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 2Z5Z . unspecified PDB 2O86 . unspecified PDB 2GJM . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 3FNL _pdbx_database_status.recvd_initial_deposition_date 2008-12-25 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site PDBJ _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 'Sheikh, I.A.' 1 'Vikram, G.' 2 'Singh, N.' 3 'Sinha, M.' 4 'Bhushan, A.' 5 'Sharma, S.' 6 'Kaur, P.' 7 'Singh, T.P.' 8 # _citation.id primary _citation.title 'Crystal Structure of the Complex of Buffalo Lactoperoxidase with Salicylhydroxamic Acid at 2.48 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 'Sheikh, I.A.' 1 primary 'Vikram, G.' 2 primary 'Singh, N.' 3 primary 'Sinha, M.' 4 primary 'Bhushan, A.' 5 primary 'Sharma, S.' 6 primary 'Kaur, P.' 7 primary 'Singh, T.P.' 8 # _cell.entry_id 3FNL _cell.length_a 54.479 _cell.length_b 80.632 _cell.length_c 78.121 _cell.angle_alpha 90.00 _cell.angle_beta 102.75 _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 3FNL _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 67817.188 1 1.11.1.7 ? ? ? 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 'IODIDE ION' 126.904 8 ? ? ? ? 6 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE' 616.487 1 ? ? ? ? 7 non-polymer syn 'THIOCYANATE ION' 58.082 1 ? ? ? ? 8 non-polymer syn 'SALICYLHYDROXAMIC ACID' 153.135 1 ? ? ? ? 9 water nat water 18.015 316 ? ? ? ? # _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 KIVGYLDEDGVLDQNRSLLFMQWGQIVDHDLDFAPETELGSNEHSKTQCEEYCIQGDNCFPIMFPKNDPKLKTQGKCMPF FRAGFVCPTPPYQSLAREQINAVTSFLDASLVYGSEP(SEP)LASRLQNLSSPLGLMAVNQEAWDHGLAYLPFNNRKPSP CEFINTTARVPCFLAGDFRASEQILLATAHTLLLREHNRLARELKKLNPQWDGEKLYQEARKILGAFVQIITFRDYLPIV LGSEMQKWIPPYQGYNNSVDPRISNVFTFAFRFGHMEVPSTVSRLDENYQPWGPEAELPLHTLFFNTWRIIKDGGIDPLV RGLLAKKSKLMNQDKMVTSELRNKLFQPTHKIHGFDLAAINLQRCRDHGMPGYNSWRGFCGLSQPKTLKGLQTVLKNKIL AKKLMDLYKTPDNIDIWIGGNAEPMVERGRVGPLLACLLGRQFQQIRDGDRFWWENPGVFTEKQRDSLQKMSFSRLICDN THITKVPLHAFQANNYPHDFVDCSAVDKLDLSPWASREN ; _entity_poly.pdbx_seq_one_letter_code_can ;SWEVGCGAPVPLVKCDENSPYRTITGDCNNRRSPALGAANRALARWLPAEYEDGLALPFGWTQRKTRNGFRVPLAREVSN KIVGYLDEDGVLDQNRSLLFMQWGQIVDHDLDFAPETELGSNEHSKTQCEEYCIQGDNCFPIMFPKNDPKLKTQGKCMPF FRAGFVCPTPPYQSLAREQINAVTSFLDASLVYGSEPSLASRLQNLSSPLGLMAVNQEAWDHGLAYLPFNNRKPSPCEFI NTTARVPCFLAGDFRASEQILLATAHTLLLREHNRLARELKKLNPQWDGEKLYQEARKILGAFVQIITFRDYLPIVLGSE MQKWIPPYQGYNNSVDPRISNVFTFAFRFGHMEVPSTVSRLDENYQPWGPEAELPLHTLFFNTWRIIKDGGIDPLVRGLL AKKSKLMNQDKMVTSELRNKLFQPTHKIHGFDLAAINLQRCRDHGMPGYNSWRGFCGLSQPKTLKGLQTVLKNKILAKKL MDLYKTPDNIDIWIGGNAEPMVERGRVGPLLACLLGRQFQQIRDGDRFWWENPGVFTEKQRDSLQKMSFSRLICDNTHIT KVPLHAFQANNYPHDFVDCSAVDKLDLSPWASREN ; _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 ASP 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 GLN 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 ARG 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 GLN n 1 287 TRP n 1 288 ASP 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 VAL 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 MET n 1 548 SER n 1 549 PHE n 1 550 SER n 1 551 ARG n 1 552 LEU n 1 553 ILE n 1 554 CYS n 1 555 ASP n 1 556 ASN n 1 557 THR n 1 558 HIS n 1 559 ILE n 1 560 THR n 1 561 LYS n 1 562 VAL n 1 563 PRO n 1 564 LEU n 1 565 HIS n 1 566 ALA n 1 567 PHE n 1 568 GLN n 1 569 ALA n 1 570 ASN n 1 571 ASN n 1 572 TYR n 1 573 PRO n 1 574 HIS n 1 575 ASP n 1 576 PHE n 1 577 VAL n 1 578 ASP n 1 579 CYS n 1 580 SER n 1 581 ALA n 1 582 VAL n 1 583 ASP n 1 584 LYS n 1 585 LEU n 1 586 ASP n 1 587 LEU n 1 588 SER n 1 589 PRO n 1 590 TRP n 1 591 ALA n 1 592 SER n 1 593 ARG n 1 594 GLU n 1 595 ASN n # _entity_src_nat.entity_id 1 _entity_src_nat.pdbx_src_id 1 _entity_src_nat.pdbx_alt_source_flag sample _entity_src_nat.pdbx_beg_seq_num ? _entity_src_nat.pdbx_end_seq_num ? _entity_src_nat.common_name 'Domestic water buffalo' _entity_src_nat.pdbx_organism_scientific 'Bubalus bubalis' _entity_src_nat.pdbx_ncbi_taxonomy_id 89462 _entity_src_nat.genus ? _entity_src_nat.species ? _entity_src_nat.strain ? _entity_src_nat.tissue ? _entity_src_nat.tissue_fraction ? _entity_src_nat.pdbx_secretion ? _entity_src_nat.pdbx_fragment ? _entity_src_nat.pdbx_variant ? _entity_src_nat.pdbx_cell_line ? _entity_src_nat.pdbx_atcc ? _entity_src_nat.pdbx_cellular_location ? _entity_src_nat.pdbx_organ ? _entity_src_nat.pdbx_organelle ? _entity_src_nat.pdbx_cell ? _entity_src_nat.pdbx_plasmid_name ? _entity_src_nat.pdbx_plasmid_details ? _entity_src_nat.details ? # _struct_ref.id 1 _struct_ref.db_name PDB _struct_ref.db_code 3FNL _struct_ref.pdbx_db_accession 3FNL _struct_ref.entity_id 1 _struct_ref.pdbx_db_isoform ? _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_align_begin ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 3FNL _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 3FNL _struct_ref_seq.db_align_beg 1 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 595 _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 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CA non-polymer . 'CALCIUM ION' ? 'Ca 2' 40.078 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 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 SHA non-polymer . 'SALICYLHYDROXAMIC ACID' ? 'C7 H7 N O3' 153.135 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 3FNL _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.47 _exptl_crystal.density_percent_sol 50.16 _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 290 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 8.2 _exptl_crystal_grow.pdbx_details 'TRIS HCL, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 290K' _exptl_crystal_grow.pdbx_pH_range . # _diffrn.id 1 _diffrn.ambient_temp 300 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector 'IMAGE PLATE' _diffrn_detector.type MARRESEARCH _diffrn_detector.pdbx_collection_date 2008-09-25 _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 1.5418 _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 1.5418 # _reflns.entry_id 3FNL _reflns.observed_criterion_sigma_I 0.0 _reflns.observed_criterion_sigma_F 0.0 _reflns.d_resolution_low 20.0 _reflns.d_resolution_high 2.48 _reflns.number_obs 22068 _reflns.number_all 22068 _reflns.percent_possible_obs 92.3 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value 0.114 _reflns.pdbx_netI_over_sigmaI 5.8 _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 2.48 _reflns_shell.d_res_low 2.57 _reflns_shell.percent_possible_all 91.2 _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value 0.371 _reflns_shell.meanI_over_sigI_obs 1.2 _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 3FNL _refine.ls_number_reflns_obs 21419 _refine.ls_number_reflns_all 21419 _refine.pdbx_ls_sigma_I 0.0 _refine.pdbx_ls_sigma_F 0.0 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 20.00 _refine.ls_d_res_high 2.48 _refine.ls_percent_reflns_obs 99.18 _refine.ls_R_factor_obs 0.20239 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.20003 _refine.ls_R_factor_R_free 0.24001 _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 1191 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.941 _refine.correlation_coeff_Fo_to_Fc_free 0.912 _refine.B_iso_mean 38.606 _refine.aniso_B[1][1] 0.22 _refine.aniso_B[2][2] -1.83 _refine.aniso_B[3][3] 1.66 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.11 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' _refine.pdbx_starting_model 2Z5Z _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 1.216 _refine.pdbx_overall_ESU_R_Free 0.305 _refine.overall_SU_ML 0.216 _refine.overall_SU_B 9.750 _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_overall_phase_error ? _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 4770 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 200 _refine_hist.number_atoms_solvent 316 _refine_hist.number_atoms_total 5286 _refine_hist.d_res_high 2.48 _refine_hist.d_res_low 20.00 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.011 0.022 ? 5111 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.442 2.016 ? 6964 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.910 5.000 ? 594 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 37.349 23.817 ? 241 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 19.454 15.018 ? 824 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 16.509 15.000 ? 38 'X-RAY DIFFRACTION' ? r_chiral_restr 0.093 0.200 ? 746 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.004 0.020 ? 3889 'X-RAY DIFFRACTION' ? r_nbd_refined 0.229 0.200 ? 2459 'X-RAY DIFFRACTION' ? r_nbtor_refined 0.311 0.200 ? 3423 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined 0.157 0.200 ? 315 'X-RAY DIFFRACTION' ? r_metal_ion_refined 0.083 0.200 ? 4 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined 0.431 0.200 ? 64 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined 0.422 0.200 ? 9 'X-RAY DIFFRACTION' ? r_mcbond_it 0.632 1.500 ? 2977 'X-RAY DIFFRACTION' ? r_mcangle_it 1.209 2.000 ? 4803 'X-RAY DIFFRACTION' ? r_scbond_it 1.527 3.000 ? 2134 'X-RAY DIFFRACTION' ? r_scangle_it 2.618 4.500 ? 2161 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 2.480 _refine_ls_shell.d_res_low 2.543 _refine_ls_shell.number_reflns_R_work 1625 _refine_ls_shell.R_factor_R_work 0.274 _refine_ls_shell.percent_reflns_obs 100.00 _refine_ls_shell.R_factor_R_free 0.340 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 75 _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 3FNL _struct.title 'Crystal Structure of the Complex of Buffalo Lactoperoxidase with Salicylhydroxamic Acid at 2.48 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 3FNL _struct_keywords.pdbx_keywords OXIDOREDUCTASE _struct_keywords.text 'LACTOPEROXIDASE, BUFFALO, SALICYLHYDROXAMIC ACID, Peroxidase, 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 5 ? O N N 5 ? P N N 5 ? Q N N 5 ? R N N 5 ? S N N 5 ? T N N 5 ? U N N 6 ? V N N 7 ? W N N 8 ? X N N 9 ? # _struct_biol.id 1 _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 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 HIS A 124 ? CYS A 133 ? HIS A 124 CYS A 133 1 ? 10 HELX_P HELX_P4 4 ASP A 148 ? GLN A 154 ? ASP A 148 GLN A 154 1 ? 7 HELX_P HELX_P5 5 ALA A 189 ? GLY A 194 ? ALA A 189 GLY A 194 1 ? 6 HELX_P HELX_P6 6 GLU A 196 ? GLN A 204 ? GLU A 196 GLN A 204 1 ? 9 HELX_P HELX_P7 7 SER A 235 ? ILE A 240 ? SER A 235 ILE A 240 1 ? 6 HELX_P HELX_P8 8 GLN A 259 ? ASN A 284 ? GLN A 259 ASN A 284 1 ? 26 HELX_P HELX_P9 9 ASP A 288 ? ASP A 311 ? ASP A 288 ASP A 311 1 ? 24 HELX_P HELX_P10 10 LEU A 313 ? GLY A 318 ? LEU A 313 GLY A 318 1 ? 6 HELX_P HELX_P11 11 GLU A 320 ? ILE A 325 ? GLU A 320 ILE A 325 1 ? 6 HELX_P HELX_P12 12 VAL A 342 ? PHE A 347 ? VAL A 342 PHE A 347 1 ? 6 HELX_P HELX_P13 13 ARG A 348 ? VAL A 354 ? ARG A 348 VAL A 354 5 ? 7 HELX_P HELX_P14 14 HIS A 377 ? PHE A 380 ? HIS A 377 PHE A 380 5 ? 4 HELX_P HELX_P15 15 THR A 383 ? LYS A 388 ? THR A 383 LYS A 388 1 ? 6 HELX_P HELX_P16 16 ILE A 392 ? LYS A 402 ? ILE A 392 LYS A 402 1 ? 11 HELX_P HELX_P17 17 THR A 414 ? ASN A 419 ? THR A 414 ASN A 419 1 ? 6 HELX_P HELX_P18 18 ASP A 432 ? HIS A 444 ? ASP A 432 HIS A 444 1 ? 13 HELX_P HELX_P19 19 GLY A 448 ? CYS A 456 ? GLY A 448 CYS A 456 1 ? 9 HELX_P HELX_P20 20 THR A 463 ? LYS A 472 ? THR A 463 LYS A 472 1 ? 10 HELX_P HELX_P21 21 ASN A 473 ? LYS A 485 ? ASN A 473 LYS A 485 1 ? 13 HELX_P HELX_P22 22 THR A 486 ? ILE A 490 ? THR A 486 ILE A 490 5 ? 5 HELX_P HELX_P23 23 ASP A 491 ? GLU A 499 ? ASP A 491 GLU A 499 1 ? 9 HELX_P HELX_P24 24 GLY A 508 ? GLY A 525 ? GLY A 508 GLY A 525 1 ? 18 HELX_P HELX_P25 25 THR A 537 ? GLN A 545 ? THR A 537 GLN A 545 1 ? 9 HELX_P HELX_P26 26 SER A 548 ? THR A 557 ? SER A 548 THR A 557 1 ? 10 HELX_P HELX_P27 27 SER A 580 ? VAL A 582 ? SER A 580 VAL A 582 5 ? 3 HELX_P HELX_P28 28 LEU A 587 ? ALA A 591 ? LEU A 587 ALA A 591 5 ? 5 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 6 SG ? ? ? 1_555 A CYS 167 SG ? ? A CYS 6 A CYS 167 1_555 ? ? ? ? ? ? ? 2.009 ? disulf2 disulf ? ? A CYS 15 SG ? ? ? 1_555 A CYS 28 SG ? ? A CYS 15 A CYS 28 1_555 ? ? ? ? ? ? ? 2.016 ? disulf3 disulf ? ? A CYS 129 SG ? ? ? 1_555 A CYS 139 SG ? ? A CYS 129 A CYS 139 1_555 ? ? ? ? ? ? ? 2.031 ? disulf4 disulf ? ? A CYS 133 SG ? ? ? 1_555 A CYS 157 SG ? ? A CYS 133 A CYS 157 1_555 ? ? ? ? ? ? ? 2.018 ? disulf5 disulf ? ? A CYS 237 SG ? ? ? 1_555 A CYS 248 SG ? ? A CYS 237 A CYS 248 1_555 ? ? ? ? ? ? ? 2.020 ? disulf6 disulf ? ? A CYS 456 SG ? ? ? 1_555 A CYS 513 SG ? ? A CYS 456 A CYS 513 1_555 ? ? ? ? ? ? ? 2.020 ? disulf7 disulf ? ? A CYS 554 SG ? ? ? 1_555 A CYS 579 SG ? ? A CYS 554 A CYS 579 1_555 ? ? ? ? ? ? ? 2.014 ? covale1 covale ? ? A PRO 197 C ? ? ? 1_555 A SEP 198 N ? ? A PRO 197 A SEP 198 1_555 ? ? ? ? ? ? ? 1.328 ? covale2 covale ? ? A SEP 198 C ? ? ? 1_555 A LEU 199 N ? ? A SEP 198 A LEU 199 1_555 ? ? ? ? ? ? ? 1.336 ? covale3 covale ? ? A ASN 95 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 95 A NAG 596 1_555 ? ? ? ? ? ? ? 1.456 ? metalc1 metalc ? ? A ASP 110 O ? ? ? 1_555 L CA . CA ? ? A ASP 110 A CA 606 1_555 ? ? ? ? ? ? ? 2.296 ? metalc2 metalc ? ? A ASP 110 OD1 ? ? ? 1_555 L CA . CA ? ? A ASP 110 A CA 606 1_555 ? ? ? ? ? ? ? 2.334 ? metalc3 metalc ? ? A THR 184 O ? ? ? 1_555 L CA . CA ? ? A THR 184 A CA 606 1_555 ? ? ? ? ? ? ? 2.564 ? metalc4 metalc ? ? A THR 184 OG1 ? ? ? 1_555 L CA . CA ? ? A THR 184 A CA 606 1_555 ? ? ? ? ? ? ? 2.543 ? metalc5 metalc ? ? A PHE 186 O ? ? ? 1_555 L CA . CA ? ? A PHE 186 A CA 606 1_555 ? ? ? ? ? ? ? 2.363 ? metalc6 metalc ? ? A ASP 188 OD1 ? ? ? 1_555 L CA . CA ? ? A ASP 188 A CA 606 1_555 ? ? ? ? ? ? ? 2.468 ? metalc7 metalc ? ? A SER 190 OG ? ? ? 1_555 L CA . CA ? ? A SER 190 A CA 606 1_555 ? ? ? ? ? ? ? 2.384 ? covale4 covale ? ? A ASN 205 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 205 A NAG 599 1_555 ? ? ? ? ? ? ? 1.441 ? covale5 covale ? ? A ASN 241 ND2 ? ? ? 1_555 G NAG . C1 ? ? A ASN 241 A NAG 601 1_555 ? ? ? ? ? ? ? 1.441 ? covale6 covale ? ? A ASN 332 ND2 ? ? ? 1_555 J NAG . C1 ? ? A ASN 332 A NAG 604 1_555 ? ? ? ? ? ? ? 1.452 ? metalc8 metalc ? ? A HIS 351 NE2 ? ? ? 1_555 U HEM . FE ? ? A HIS 351 A HEM 615 1_555 ? ? ? ? ? ? ? 2.076 ? covale7 covale ? ? B NAG . O4 ? ? ? 1_555 C NAG . C1 ? ? A NAG 596 A NAG 597 1_555 ? ? ? ? ? ? ? 1.459 ? covale8 covale ? ? C NAG . O4 ? ? ? 1_555 D MAN . C1 ? ? A NAG 597 A MAN 598 1_555 ? ? ? ? ? ? ? 1.447 ? covale9 covale ? ? E NAG . O4 ? ? ? 1_555 F NAG . C1 ? ? A NAG 599 A NAG 600 1_555 ? ? ? ? ? ? ? 1.446 ? covale10 covale ? ? G NAG . O4 ? ? ? 1_555 H NAG . C1 ? ? A NAG 601 A NAG 602 1_555 ? ? ? ? ? ? ? 1.441 ? covale11 covale ? ? H NAG . O4 ? ? ? 1_555 I MAN . C1 ? ? A NAG 602 A MAN 603 1_555 ? ? ? ? ? ? ? 1.457 ? covale12 covale ? ? J NAG . O4 ? ? ? 1_555 K NAG . C1 ? ? A NAG 604 A NAG 605 1_555 ? ? ? ? ? ? ? 1.457 ? metalc9 metalc ? ? U HEM . FE ? ? ? 1_555 W SHA . O9 ? ? A HEM 615 A SHA 617 1_555 ? ? ? ? ? ? ? 2.716 ? # 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 0.47 2 TYR 572 A . ? TYR 572 A PRO 573 A ? PRO 573 A 1 1.38 # 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 ? PRO A 563 ? LYS A 561 PRO A 563 F 2 PHE A 576 ? ASP A 578 ? PHE A 576 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 ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 596' AC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 597' AC3 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE MAN A 598' AC4 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG A 599' AC5 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 600' AC6 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 601' AC7 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 602' AC8 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE MAN A 603' AC9 Software ? ? ? ? 4 '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 ? ? ? ? 2 'BINDING SITE FOR RESIDUE IOD A 607' BC4 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE IOD A 608' BC5 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE IOD A 609' BC6 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE IOD A 610' BC7 Software ? ? ? ? 3 '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 ? ? ? ? 1 'BINDING SITE FOR RESIDUE IOD A 614' CC2 Software ? ? ? ? 21 'BINDING SITE FOR RESIDUE HEM A 615' CC3 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE SCN A 616' CC4 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE SHA A 617' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 3 ASN A 95 ? ASN A 95 . ? 1_555 ? 2 AC1 3 ARG A 504 ? ARG A 504 . ? 1_555 ? 3 AC1 3 NAG C . ? NAG A 597 . ? 1_555 ? 4 AC2 3 ARG A 504 ? ARG A 504 . ? 1_555 ? 5 AC2 3 NAG B . ? NAG A 596 . ? 1_555 ? 6 AC2 3 MAN D . ? MAN A 598 . ? 1_555 ? 7 AC3 2 NAG C . ? NAG A 597 . ? 1_555 ? 8 AC3 2 HOH X . ? HOH A 735 . ? 1_555 ? 9 AC4 7 ASN A 205 ? ASN A 205 . ? 1_555 ? 10 AC4 7 SER A 208 ? SER A 208 . ? 1_555 ? 11 AC4 7 ALA A 214 ? ALA A 214 . ? 1_555 ? 12 AC4 7 VAL A 215 ? VAL A 215 . ? 1_555 ? 13 AC4 7 GLN A 217 ? GLN A 217 . ? 1_555 ? 14 AC4 7 NAG F . ? NAG A 600 . ? 1_555 ? 15 AC4 7 HOH X . ? HOH A 921 . ? 1_555 ? 16 AC5 3 NAG E . ? NAG A 599 . ? 1_555 ? 17 AC5 3 HOH X . ? HOH A 916 . ? 1_555 ? 18 AC5 3 HOH X . ? HOH A 927 . ? 1_555 ? 19 AC6 5 ASN A 241 ? ASN A 241 . ? 1_555 ? 20 AC6 5 ALA A 244 ? ALA A 244 . ? 1_555 ? 21 AC6 5 TRP A 384 ? TRP A 384 . ? 1_555 ? 22 AC6 5 LYS A 388 ? LYS A 388 . ? 1_555 ? 23 AC6 5 NAG H . ? NAG A 602 . ? 1_555 ? 24 AC7 3 NAG G . ? NAG A 601 . ? 1_555 ? 25 AC7 3 MAN I . ? MAN A 603 . ? 1_555 ? 26 AC7 3 HOH X . ? HOH A 917 . ? 1_555 ? 27 AC8 1 NAG H . ? NAG A 602 . ? 1_555 ? 28 AC9 4 ASN A 332 ? ASN A 332 . ? 1_555 ? 29 AC9 4 VAL A 335 ? VAL A 335 . ? 1_555 ? 30 AC9 4 NAG K . ? NAG A 605 . ? 1_555 ? 31 AC9 4 HOH X . ? HOH A 809 . ? 1_555 ? 32 BC1 1 NAG J . ? NAG A 604 . ? 1_555 ? 33 BC2 5 ASP A 110 ? ASP A 110 . ? 1_555 ? 34 BC2 5 THR A 184 ? THR A 184 . ? 1_555 ? 35 BC2 5 PHE A 186 ? PHE A 186 . ? 1_555 ? 36 BC2 5 ASP A 188 ? ASP A 188 . ? 1_555 ? 37 BC2 5 SER A 190 ? SER A 190 . ? 1_555 ? 38 BC3 2 PHE A 309 ? PHE A 309 . ? 1_555 ? 39 BC3 2 TRP A 530 ? TRP A 530 . ? 1_555 ? 40 BC4 1 ASN A 80 ? ASN A 80 . ? 1_555 ? 41 BC5 3 HIS A 565 ? HIS A 565 . ? 1_555 ? 42 BC5 3 ALA A 566 ? ALA A 566 . ? 1_555 ? 43 BC5 3 PHE A 567 ? PHE A 567 . ? 1_555 ? 44 BC6 2 GLU A 363 ? GLU A 363 . ? 1_555 ? 45 BC6 2 ARG A 397 ? ARG A 397 . ? 1_555 ? 46 BC7 3 TRP A 46 ? TRP A 46 . ? 1_555 ? 47 BC7 3 VAL A 342 ? VAL A 342 . ? 1_555 ? 48 BC7 3 TRP A 452 ? TRP A 452 . ? 1_555 ? 49 BC8 2 LYS A 462 ? LYS A 462 . ? 1_555 ? 50 BC8 2 THR A 463 ? THR A 463 . ? 1_555 ? 51 BC9 1 PHE A 229 ? PHE A 229 . ? 1_555 ? 52 CC1 1 ARG A 504 ? ARG A 504 . ? 1_555 ? 53 CC2 21 MET A 101 ? MET A 101 . ? 1_555 ? 54 CC2 21 GLY A 104 ? GLY A 104 . ? 1_555 ? 55 CC2 21 GLN A 105 ? GLN A 105 . ? 1_555 ? 56 CC2 21 ASP A 108 ? ASP A 108 . ? 1_555 ? 57 CC2 21 ASP A 112 ? ASP A 112 . ? 1_555 ? 58 CC2 21 PHE A 113 ? PHE A 113 . ? 1_555 ? 59 CC2 21 ALA A 114 ? ALA A 114 . ? 1_555 ? 60 CC2 21 GLU A 258 ? GLU A 258 . ? 1_555 ? 61 CC2 21 THR A 344 ? THR A 344 . ? 1_555 ? 62 CC2 21 PHE A 347 ? PHE A 347 . ? 1_555 ? 63 CC2 21 ARG A 348 ? ARG A 348 . ? 1_555 ? 64 CC2 21 GLY A 350 ? GLY A 350 . ? 1_555 ? 65 CC2 21 HIS A 351 ? HIS A 351 . ? 1_555 ? 66 CC2 21 VAL A 354 ? VAL A 354 . ? 1_555 ? 67 CC2 21 LEU A 417 ? LEU A 417 . ? 1_555 ? 68 CC2 21 ILE A 436 ? ILE A 436 . ? 1_555 ? 69 CC2 21 ARG A 440 ? ARG A 440 . ? 1_555 ? 70 CC2 21 SHA W . ? SHA A 617 . ? 1_555 ? 71 CC2 21 HOH X . ? HOH A 664 . ? 1_555 ? 72 CC2 21 HOH X . ? HOH A 673 . ? 1_555 ? 73 CC2 21 HOH X . ? HOH A 864 . ? 1_555 ? 74 CC3 1 ARG A 202 ? ARG A 202 . ? 1_555 ? 75 CC4 6 GLN A 105 ? GLN A 105 . ? 1_555 ? 76 CC4 6 HIS A 109 ? HIS A 109 . ? 1_555 ? 77 CC4 6 ARG A 255 ? ARG A 255 . ? 1_555 ? 78 CC4 6 GLU A 258 ? GLU A 258 . ? 1_555 ? 79 CC4 6 HEM U . ? HEM A 615 . ? 1_555 ? 80 CC4 6 HOH X . ? HOH A 673 . ? 1_555 ? # _database_PDB_matrix.entry_id 3FNL _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 3FNL _atom_sites.fract_transf_matrix[1][1] 0.018356 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.004153 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.012402 _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] 0.013124 _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 ? 2.363 -34.481 33.483 1.00 86.29 ? 1 SER A N 1 ATOM 2 C CA . SER A 1 1 ? 1.865 -33.454 34.444 1.00 86.20 ? 1 SER A CA 1 ATOM 3 C C . SER A 1 1 ? 2.585 -32.122 34.234 1.00 86.12 ? 1 SER A C 1 ATOM 4 O O . SER A 1 1 ? 3.760 -32.001 34.540 1.00 86.20 ? 1 SER A O 1 ATOM 5 C CB . SER A 1 1 ? 1.987 -34.002 35.867 1.00 86.16 ? 1 SER A CB 1 ATOM 6 O OG . SER A 1 1 ? 1.235 -35.193 36.016 1.00 86.20 ? 1 SER A OG 1 ATOM 7 N N . TRP A 1 2 ? 1.854 -31.130 33.701 1.00 85.82 ? 2 TRP A N 1 ATOM 8 C CA . TRP A 1 2 ? 2.340 -29.786 33.321 1.00 85.61 ? 2 TRP A CA 1 ATOM 9 C C . TRP A 1 2 ? 1.684 -28.620 34.068 1.00 85.16 ? 2 TRP A C 1 ATOM 10 O O . TRP A 1 2 ? 2.043 -27.456 33.879 1.00 84.98 ? 2 TRP A O 1 ATOM 11 C CB . TRP A 1 2 ? 2.054 -29.601 31.824 1.00 85.69 ? 2 TRP A CB 1 ATOM 12 C CG . TRP A 1 2 ? 3.163 -29.885 30.890 1.00 86.40 ? 2 TRP A CG 1 ATOM 13 C CD1 . TRP A 1 2 ? 4.266 -29.094 30.666 1.00 86.80 ? 2 TRP A CD1 1 ATOM 14 C CD2 . TRP A 1 2 ? 3.297 -31.017 30.009 1.00 87.10 ? 2 TRP A CD2 1 ATOM 15 N NE1 . TRP A 1 2 ? 5.085 -29.674 29.712 1.00 86.77 ? 2 TRP A NE1 1 ATOM 16 C CE2 . TRP A 1 2 ? 4.516 -30.854 29.294 1.00 87.10 ? 2 TRP A CE2 1 ATOM 17 C CE3 . TRP A 1 2 ? 2.509 -32.157 29.760 1.00 87.29 ? 2 TRP A CE3 1 ATOM 18 C CZ2 . TRP A 1 2 ? 4.969 -31.793 28.344 1.00 87.34 ? 2 TRP A CZ2 1 ATOM 19 C CZ3 . TRP A 1 2 ? 2.961 -33.094 28.810 1.00 87.53 ? 2 TRP A CZ3 1 ATOM 20 C CH2 . TRP A 1 2 ? 4.181 -32.900 28.118 1.00 87.28 ? 2 TRP A CH2 1 ATOM 21 N N . GLU A 1 3 ? 0.685 -28.929 34.919 1.00 84.71 ? 3 GLU A N 1 ATOM 22 C CA . GLU A 1 3 ? -0.230 -27.982 35.632 1.00 84.23 ? 3 GLU A CA 1 ATOM 23 C C . GLU A 1 3 ? -1.026 -27.394 34.464 1.00 83.58 ? 3 GLU A C 1 ATOM 24 O O . GLU A 1 3 ? -1.905 -26.552 34.628 1.00 83.54 ? 3 GLU A O 1 ATOM 25 C CB . GLU A 1 3 ? 0.478 -26.895 36.490 1.00 84.32 ? 3 GLU A CB 1 ATOM 26 C CG . GLU A 1 3 ? 1.668 -27.343 37.378 1.00 84.80 ? 3 GLU A CG 1 ATOM 27 C CD . GLU A 1 3 ? 1.314 -27.826 38.775 1.00 85.25 ? 3 GLU A CD 1 ATOM 28 O OE1 . GLU A 1 3 ? 0.122 -27.906 39.085 1.00 85.56 ? 3 GLU A OE1 1 ATOM 29 O OE2 . GLU A 1 3 ? 2.257 -28.118 39.536 1.00 85.41 ? 3 GLU A OE2 1 ATOM 30 N N . VAL A 1 4 ? -0.697 -27.898 33.300 1.00 82.79 ? 4 VAL A N 1 ATOM 31 C CA . VAL A 1 4 ? -1.227 -27.447 32.002 1.00 82.19 ? 4 VAL A CA 1 ATOM 32 C C . VAL A 1 4 ? -2.578 -26.655 31.948 1.00 81.44 ? 4 VAL A C 1 ATOM 33 O O . VAL A 1 4 ? -2.690 -25.781 31.100 1.00 81.10 ? 4 VAL A O 1 ATOM 34 C CB . VAL A 1 4 ? -1.367 -28.633 31.007 1.00 82.33 ? 4 VAL A CB 1 ATOM 35 C CG1 . VAL A 1 4 ? -0.813 -28.231 29.638 1.00 82.44 ? 4 VAL A CG1 1 ATOM 36 C CG2 . VAL A 1 4 ? -0.639 -29.869 31.534 1.00 82.45 ? 4 VAL A CG2 1 ATOM 37 N N . GLY A 1 5 ? -3.563 -26.857 32.813 1.00 80.89 ? 5 GLY A N 1 ATOM 38 C CA . GLY A 1 5 ? -4.856 -26.201 32.665 1.00 80.20 ? 5 GLY A CA 1 ATOM 39 C C . GLY A 1 5 ? -5.103 -24.689 32.852 1.00 79.67 ? 5 GLY A C 1 ATOM 40 O O . GLY A 1 5 ? -5.802 -24.083 32.055 1.00 79.32 ? 5 GLY A O 1 ATOM 41 N N . CYS A 1 6 ? -4.537 -24.049 33.891 1.00 79.26 ? 6 CYS A N 1 ATOM 42 C CA . CYS A 1 6 ? -4.886 -22.649 34.244 1.00 78.68 ? 6 CYS A CA 1 ATOM 43 C C . CYS A 1 6 ? -5.084 -21.753 33.029 1.00 79.04 ? 6 CYS A C 1 ATOM 44 O O . CYS A 1 6 ? -4.128 -21.230 32.455 1.00 78.92 ? 6 CYS A O 1 ATOM 45 C CB . CYS A 1 6 ? -3.925 -21.991 35.261 1.00 78.03 ? 6 CYS A CB 1 ATOM 46 S SG . CYS A 1 6 ? -4.577 -20.436 36.053 1.00 76.01 ? 6 CYS A SG 1 ATOM 47 N N . GLY A 1 7 ? -6.351 -21.640 32.636 1.00 79.49 ? 7 GLY A N 1 ATOM 48 C CA . GLY A 1 7 ? -6.824 -20.693 31.628 1.00 79.85 ? 7 GLY A CA 1 ATOM 49 C C . GLY A 1 7 ? -8.023 -19.992 32.245 1.00 80.12 ? 7 GLY A C 1 ATOM 50 O O . GLY A 1 7 ? -9.095 -19.893 31.630 1.00 80.19 ? 7 GLY A O 1 ATOM 51 N N . ALA A 1 8 ? -7.827 -19.536 33.486 1.00 80.23 ? 8 ALA A N 1 ATOM 52 C CA . ALA A 1 8 ? -8.853 -18.882 34.303 1.00 80.31 ? 8 ALA A CA 1 ATOM 53 C C . ALA A 1 8 ? -8.957 -17.371 33.959 1.00 80.23 ? 8 ALA A C 1 ATOM 54 O O . ALA A 1 8 ? -8.802 -17.020 32.786 1.00 80.44 ? 8 ALA A O 1 ATOM 55 C CB . ALA A 1 8 ? -8.547 -19.126 35.787 1.00 80.28 ? 8 ALA A CB 1 ATOM 56 N N . PRO A 1 9 ? -9.338 -16.471 34.838 1.00 80.01 ? 9 PRO A N 1 ATOM 57 C CA . PRO A 1 9 ? -9.347 -15.029 34.553 1.00 79.69 ? 9 PRO A CA 1 ATOM 58 C C . PRO A 1 9 ? -8.563 -14.557 33.316 1.00 79.24 ? 9 PRO A C 1 ATOM 59 O O . PRO A 1 9 ? -7.407 -14.131 33.413 1.00 79.31 ? 9 PRO A O 1 ATOM 60 C CB . PRO A 1 9 ? -8.794 -14.433 35.852 1.00 79.83 ? 9 PRO A CB 1 ATOM 61 C CG . PRO A 1 9 ? -9.381 -15.362 36.941 1.00 79.94 ? 9 PRO A CG 1 ATOM 62 C CD . PRO A 1 9 ? -9.758 -16.695 36.236 1.00 79.97 ? 9 PRO A CD 1 ATOM 63 N N . VAL A 1 10 ? -9.246 -14.672 32.166 1.00 78.71 ? 10 VAL A N 1 ATOM 64 C CA . VAL A 1 10 ? -8.816 -14.230 30.842 1.00 77.79 ? 10 VAL A CA 1 ATOM 65 C C . VAL A 1 10 ? -10.108 -14.246 30.012 1.00 77.10 ? 10 VAL A C 1 ATOM 66 O O . VAL A 1 10 ? -11.025 -15.029 30.305 1.00 77.22 ? 10 VAL A O 1 ATOM 67 C CB . VAL A 1 10 ? -7.769 -15.165 30.176 1.00 77.80 ? 10 VAL A CB 1 ATOM 68 C CG1 . VAL A 1 10 ? -6.485 -15.221 30.985 1.00 77.91 ? 10 VAL A CG1 1 ATOM 69 C CG2 . VAL A 1 10 ? -8.334 -16.580 29.953 1.00 77.82 ? 10 VAL A CG2 1 ATOM 70 N N . PRO A 1 11 ? -10.208 -13.373 28.990 1.00 76.31 ? 11 PRO A N 1 ATOM 71 C CA . PRO A 1 11 ? -11.449 -13.321 28.209 1.00 75.53 ? 11 PRO A CA 1 ATOM 72 C C . PRO A 1 11 ? -11.489 -14.384 27.103 1.00 74.72 ? 11 PRO A C 1 ATOM 73 O O . PRO A 1 11 ? -10.543 -14.494 26.307 1.00 74.71 ? 11 PRO A O 1 ATOM 74 C CB . PRO A 1 11 ? -11.423 -11.912 27.600 1.00 75.50 ? 11 PRO A CB 1 ATOM 75 C CG . PRO A 1 11 ? -10.094 -11.281 28.031 1.00 75.94 ? 11 PRO A CG 1 ATOM 76 C CD . PRO A 1 11 ? -9.223 -12.393 28.502 1.00 76.22 ? 11 PRO A CD 1 ATOM 77 N N . LEU A 1 12 ? -12.575 -15.152 27.049 1.00 73.65 ? 12 LEU A N 1 ATOM 78 C CA . LEU A 1 12 ? -12.683 -16.228 26.055 1.00 72.69 ? 12 LEU A CA 1 ATOM 79 C C . LEU A 1 12 ? -13.980 -16.197 25.230 1.00 71.72 ? 12 LEU A C 1 ATOM 80 O O . LEU A 1 12 ? -15.068 -15.876 25.741 1.00 71.84 ? 12 LEU A O 1 ATOM 81 C CB . LEU A 1 12 ? -12.441 -17.602 26.716 1.00 72.80 ? 12 LEU A CB 1 ATOM 82 C CG . LEU A 1 12 ? -13.079 -18.913 26.219 1.00 73.05 ? 12 LEU A CG 1 ATOM 83 C CD1 . LEU A 1 12 ? -12.068 -20.074 26.224 1.00 72.69 ? 12 LEU A CD1 1 ATOM 84 C CD2 . LEU A 1 12 ? -14.320 -19.255 27.058 1.00 73.19 ? 12 LEU A CD2 1 ATOM 85 N N . VAL A 1 13 ? -13.835 -16.523 23.945 1.00 70.04 ? 13 VAL A N 1 ATOM 86 C CA . VAL A 1 13 ? -14.973 -16.696 23.039 1.00 68.33 ? 13 VAL A CA 1 ATOM 87 C C . VAL A 1 13 ? -14.754 -17.878 22.082 1.00 66.68 ? 13 VAL A C 1 ATOM 88 O O . VAL A 1 13 ? -13.926 -18.758 22.336 1.00 66.52 ? 13 VAL A O 1 ATOM 89 C CB . VAL A 1 13 ? -15.322 -15.401 22.241 1.00 68.75 ? 13 VAL A CB 1 ATOM 90 C CG1 . VAL A 1 13 ? -16.082 -14.399 23.122 1.00 68.62 ? 13 VAL A CG1 1 ATOM 91 C CG2 . VAL A 1 13 ? -14.068 -14.780 21.569 1.00 68.68 ? 13 VAL A CG2 1 ATOM 92 N N . LYS A 1 14 ? -15.498 -17.890 20.983 1.00 64.40 ? 14 LYS A N 1 ATOM 93 C CA . LYS A 1 14 ? -15.513 -19.038 20.097 1.00 62.37 ? 14 LYS A CA 1 ATOM 94 C C . LYS A 1 14 ? -14.968 -18.647 18.723 1.00 60.55 ? 14 LYS A C 1 ATOM 95 O O . LYS A 1 14 ? -15.193 -17.526 18.246 1.00 60.49 ? 14 LYS A O 1 ATOM 96 C CB . LYS A 1 14 ? -16.936 -19.608 20.001 1.00 62.87 ? 14 LYS A CB 1 ATOM 97 C CG . LYS A 1 14 ? -17.640 -19.871 21.380 1.00 63.30 ? 14 LYS A CG 1 ATOM 98 C CD . LYS A 1 14 ? -19.103 -19.357 21.384 1.00 65.15 ? 14 LYS A CD 1 ATOM 99 C CE . LYS A 1 14 ? -19.730 -19.582 22.880 1.00 65.81 ? 14 LYS A CE 1 ATOM 100 N NZ . LYS A 1 14 ? -21.237 -19.106 22.793 1.00 65.65 ? 14 LYS A NZ 1 ATOM 101 N N . CYS A 1 15 ? -14.252 -19.576 18.095 1.00 58.02 ? 15 CYS A N 1 ATOM 102 C CA . CYS A 1 15 ? -13.497 -19.282 16.878 1.00 55.50 ? 15 CYS A CA 1 ATOM 103 C C . CYS A 1 15 ? -14.352 -19.163 15.612 1.00 55.90 ? 15 CYS A C 1 ATOM 104 O O . CYS A 1 15 ? -14.967 -20.141 15.172 1.00 55.47 ? 15 CYS A O 1 ATOM 105 C CB . CYS A 1 15 ? -12.357 -20.291 16.705 1.00 54.29 ? 15 CYS A CB 1 ATOM 106 S SG . CYS A 1 15 ? -10.986 -19.980 17.862 1.00 46.79 ? 15 CYS A SG 1 ATOM 107 N N . ASP A 1 16 ? -14.378 -17.959 15.032 1.00 56.28 ? 16 ASP A N 1 ATOM 108 C CA . ASP A 1 16 ? -15.132 -17.717 13.795 1.00 57.01 ? 16 ASP A CA 1 ATOM 109 C C . ASP A 1 16 ? -14.879 -18.808 12.745 1.00 56.80 ? 16 ASP A C 1 ATOM 110 O O . ASP A 1 16 ? -15.779 -19.119 11.961 1.00 57.06 ? 16 ASP A O 1 ATOM 111 C CB . ASP A 1 16 ? -14.851 -16.315 13.210 1.00 57.59 ? 16 ASP A CB 1 ATOM 112 C CG . ASP A 1 16 ? -15.911 -15.248 13.617 1.00 59.09 ? 16 ASP A CG 1 ATOM 113 O OD1 . ASP A 1 16 ? -16.957 -15.596 14.221 1.00 61.06 ? 16 ASP A OD1 1 ATOM 114 O OD2 . ASP A 1 16 ? -15.697 -14.046 13.312 1.00 59.58 ? 16 ASP A OD2 1 ATOM 115 N N . GLU A 1 17 ? -13.677 -19.392 12.756 1.00 56.46 ? 17 GLU A N 1 ATOM 116 C CA . GLU A 1 17 ? -13.302 -20.508 11.862 1.00 56.52 ? 17 GLU A CA 1 ATOM 117 C C . GLU A 1 17 ? -13.513 -20.156 10.388 1.00 55.87 ? 17 GLU A C 1 ATOM 118 O O . GLU A 1 17 ? -14.654 -20.015 9.930 1.00 55.99 ? 17 GLU A O 1 ATOM 119 C CB . GLU A 1 17 ? -14.071 -21.803 12.207 1.00 56.78 ? 17 GLU A CB 1 ATOM 120 C CG . GLU A 1 17 ? -13.565 -22.583 13.435 1.00 58.53 ? 17 GLU A CG 1 ATOM 121 C CD . GLU A 1 17 ? -12.882 -23.914 13.085 1.00 60.70 ? 17 GLU A CD 1 ATOM 122 O OE1 . GLU A 1 17 ? -13.429 -24.682 12.252 1.00 60.76 ? 17 GLU A OE1 1 ATOM 123 O OE2 . GLU A 1 17 ? -11.805 -24.204 13.666 1.00 61.10 ? 17 GLU A OE2 1 ATOM 124 N N . ASN A 1 18 ? -12.412 -20.019 9.653 1.00 54.81 ? 18 ASN A N 1 ATOM 125 C CA . ASN A 1 18 ? -12.448 -19.643 8.228 1.00 53.79 ? 18 ASN A CA 1 ATOM 126 C C . ASN A 1 18 ? -12.695 -18.139 7.989 1.00 52.23 ? 18 ASN A C 1 ATOM 127 O O . ASN A 1 18 ? -12.585 -17.662 6.859 1.00 52.24 ? 18 ASN A O 1 ATOM 128 C CB . ASN A 1 18 ? -13.446 -20.513 7.430 1.00 54.29 ? 18 ASN A CB 1 ATOM 129 C CG . ASN A 1 18 ? -12.794 -21.216 6.223 1.00 56.38 ? 18 ASN A CG 1 ATOM 130 O OD1 . ASN A 1 18 ? -12.698 -22.447 6.191 1.00 58.46 ? 18 ASN A OD1 1 ATOM 131 N ND2 . ASN A 1 18 ? -12.346 -20.435 5.232 1.00 57.36 ? 18 ASN A ND2 1 ATOM 132 N N . SER A 1 19 ? -13.013 -17.396 9.051 1.00 50.39 ? 19 SER A N 1 ATOM 133 C CA . SER A 1 19 ? -13.043 -15.930 8.985 1.00 48.47 ? 19 SER A CA 1 ATOM 134 C C . SER A 1 19 ? -11.699 -15.366 8.517 1.00 46.83 ? 19 SER A C 1 ATOM 135 O O . SER A 1 19 ? -10.647 -15.752 9.033 1.00 46.79 ? 19 SER A O 1 ATOM 136 C CB . SER A 1 19 ? -13.386 -15.327 10.344 1.00 48.57 ? 19 SER A CB 1 ATOM 137 O OG . SER A 1 19 ? -13.113 -13.930 10.360 1.00 48.56 ? 19 SER A OG 1 ATOM 138 N N . PRO A 1 20 ? -11.732 -14.452 7.536 1.00 45.04 ? 20 PRO A N 1 ATOM 139 C CA . PRO A 1 20 ? -10.519 -13.874 6.970 1.00 43.49 ? 20 PRO A CA 1 ATOM 140 C C . PRO A 1 20 ? -9.928 -12.722 7.809 1.00 41.97 ? 20 PRO A C 1 ATOM 141 O O . PRO A 1 20 ? -8.999 -12.038 7.358 1.00 41.99 ? 20 PRO A O 1 ATOM 142 C CB . PRO A 1 20 ? -10.986 -13.356 5.599 1.00 43.42 ? 20 PRO A CB 1 ATOM 143 C CG . PRO A 1 20 ? -12.461 -13.713 5.500 1.00 44.37 ? 20 PRO A CG 1 ATOM 144 C CD . PRO A 1 20 ? -12.934 -13.916 6.882 1.00 44.70 ? 20 PRO A CD 1 ATOM 145 N N . TYR A 1 21 ? -10.446 -12.506 9.014 1.00 39.74 ? 21 TYR A N 1 ATOM 146 C CA . TYR A 1 21 ? -9.959 -11.406 9.830 1.00 37.81 ? 21 TYR A CA 1 ATOM 147 C C . TYR A 1 21 ? -9.469 -11.856 11.203 1.00 36.57 ? 21 TYR A C 1 ATOM 148 O O . TYR A 1 21 ? -10.051 -12.769 11.810 1.00 36.48 ? 21 TYR A O 1 ATOM 149 C CB . TYR A 1 21 ? -11.048 -10.344 9.961 1.00 37.75 ? 21 TYR A CB 1 ATOM 150 C CG . TYR A 1 21 ? -11.590 -9.871 8.625 1.00 38.25 ? 21 TYR A CG 1 ATOM 151 C CD1 . TYR A 1 21 ? -10.729 -9.426 7.618 1.00 36.94 ? 21 TYR A CD1 1 ATOM 152 C CD2 . TYR A 1 21 ? -12.965 -9.857 8.371 1.00 39.06 ? 21 TYR A CD2 1 ATOM 153 C CE1 . TYR A 1 21 ? -11.204 -9.001 6.402 1.00 38.45 ? 21 TYR A CE1 1 ATOM 154 C CE2 . TYR A 1 21 ? -13.462 -9.416 7.141 1.00 39.66 ? 21 TYR A CE2 1 ATOM 155 C CZ . TYR A 1 21 ? -12.571 -8.988 6.158 1.00 39.91 ? 21 TYR A CZ 1 ATOM 156 O OH . TYR A 1 21 ? -13.039 -8.541 4.935 1.00 38.88 ? 21 TYR A OH 1 ATOM 157 N N . ARG A 1 22 ? -8.398 -11.222 11.687 1.00 34.84 ? 22 ARG A N 1 ATOM 158 C CA . ARG A 1 22 ? -7.890 -11.495 13.037 1.00 33.12 ? 22 ARG A CA 1 ATOM 159 C C . ARG A 1 22 ? -8.972 -11.198 14.053 1.00 32.55 ? 22 ARG A C 1 ATOM 160 O O . ARG A 1 22 ? -9.813 -10.317 13.838 1.00 32.43 ? 22 ARG A O 1 ATOM 161 C CB . ARG A 1 22 ? -6.701 -10.613 13.394 1.00 32.56 ? 22 ARG A CB 1 ATOM 162 C CG . ARG A 1 22 ? -5.512 -10.668 12.478 1.00 32.24 ? 22 ARG A CG 1 ATOM 163 C CD . ARG A 1 22 ? -4.416 -9.785 13.072 1.00 30.67 ? 22 ARG A CD 1 ATOM 164 N NE . ARG A 1 22 ? -3.190 -9.729 12.278 1.00 30.24 ? 22 ARG A NE 1 ATOM 165 C CZ . ARG A 1 22 ? -2.182 -10.584 12.393 1.00 29.39 ? 22 ARG A CZ 1 ATOM 166 N NH1 . ARG A 1 22 ? -2.245 -11.587 13.253 1.00 29.43 ? 22 ARG A NH1 1 ATOM 167 N NH2 . ARG A 1 22 ? -1.110 -10.443 11.635 1.00 30.58 ? 22 ARG A NH2 1 ATOM 168 N N . THR A 1 23 ? -8.956 -11.925 15.161 1.00 31.50 ? 23 THR A N 1 ATOM 169 C CA . THR A 1 23 ? -9.768 -11.522 16.291 1.00 31.39 ? 23 THR A CA 1 ATOM 170 C C . THR A 1 23 ? -9.074 -10.322 16.939 1.00 31.26 ? 23 THR A C 1 ATOM 171 O O . THR A 1 23 ? -7.891 -10.063 16.695 1.00 31.19 ? 23 THR A O 1 ATOM 172 C CB . THR A 1 23 ? -9.974 -12.669 17.324 1.00 31.36 ? 23 THR A CB 1 ATOM 173 O OG1 . THR A 1 23 ? -8.704 -13.201 17.704 1.00 31.36 ? 23 THR A OG1 1 ATOM 174 C CG2 . THR A 1 23 ? -10.828 -13.798 16.736 1.00 31.05 ? 23 THR A CG2 1 ATOM 175 N N . ILE A 1 24 ? -9.818 -9.580 17.745 1.00 31.03 ? 24 ILE A N 1 ATOM 176 C CA . ILE A 1 24 ? -9.261 -8.446 18.474 1.00 30.65 ? 24 ILE A CA 1 ATOM 177 C C . ILE A 1 24 ? -8.274 -8.904 19.565 1.00 30.38 ? 24 ILE A C 1 ATOM 178 O O . ILE A 1 24 ? -7.225 -8.275 19.761 1.00 30.22 ? 24 ILE A O 1 ATOM 179 C CB . ILE A 1 24 ? -10.400 -7.560 19.044 1.00 30.73 ? 24 ILE A CB 1 ATOM 180 C CG1 . ILE A 1 24 ? -10.930 -6.600 17.960 1.00 30.53 ? 24 ILE A CG1 1 ATOM 181 C CG2 . ILE A 1 24 ? -9.972 -6.843 20.323 1.00 30.66 ? 24 ILE A CG2 1 ATOM 182 C CD1 . ILE A 1 24 ? -9.893 -5.634 17.353 1.00 30.74 ? 24 ILE A CD1 1 ATOM 183 N N . THR A 1 25 ? -8.606 -10.010 20.234 1.00 29.93 ? 25 THR A N 1 ATOM 184 C CA . THR A 1 25 ? -7.807 -10.545 21.351 1.00 29.60 ? 25 THR A CA 1 ATOM 185 C C . THR A 1 25 ? -6.629 -11.426 20.929 1.00 30.01 ? 25 THR A C 1 ATOM 186 O O . THR A 1 25 ? -5.739 -11.691 21.742 1.00 29.93 ? 25 THR A O 1 ATOM 187 C CB . THR A 1 25 ? -8.655 -11.384 22.314 1.00 29.23 ? 25 THR A CB 1 ATOM 188 O OG1 . THR A 1 25 ? -9.019 -12.604 21.665 1.00 28.19 ? 25 THR A OG1 1 ATOM 189 C CG2 . THR A 1 25 ? -9.900 -10.635 22.744 1.00 28.31 ? 25 THR A CG2 1 ATOM 190 N N . GLY A 1 26 ? -6.632 -11.890 19.677 1.00 30.02 ? 26 GLY A N 1 ATOM 191 C CA . GLY A 1 26 ? -5.534 -12.696 19.163 1.00 30.08 ? 26 GLY A CA 1 ATOM 192 C C . GLY A 1 26 ? -5.806 -14.177 19.252 1.00 30.57 ? 26 GLY A C 1 ATOM 193 O O . GLY A 1 26 ? -5.031 -14.998 18.734 1.00 30.60 ? 26 GLY A O 1 ATOM 194 N N . ASP A 1 27 ? -6.912 -14.520 19.911 1.00 31.02 ? 27 ASP A N 1 ATOM 195 C CA . ASP A 1 27 ? -7.441 -15.881 19.916 1.00 31.27 ? 27 ASP A CA 1 ATOM 196 C C . ASP A 1 27 ? -7.802 -16.312 18.501 1.00 31.58 ? 27 ASP A C 1 ATOM 197 O O . ASP A 1 27 ? -8.040 -15.465 17.650 1.00 31.36 ? 27 ASP A O 1 ATOM 198 C CB . ASP A 1 27 ? -8.692 -15.936 20.779 1.00 31.49 ? 27 ASP A CB 1 ATOM 199 C CG . ASP A 1 27 ? -8.388 -15.868 22.251 1.00 31.19 ? 27 ASP A CG 1 ATOM 200 O OD1 . ASP A 1 27 ? -7.868 -16.841 22.823 1.00 33.04 ? 27 ASP A OD1 1 ATOM 201 O OD2 . ASP A 1 27 ? -8.704 -14.842 22.856 1.00 32.11 ? 27 ASP A OD2 1 ATOM 202 N N . CYS A 1 28 ? -7.682 -17.677 18.283 1.00 32.24 ? 28 CYS A N 1 ATOM 203 C CA . CYS A 1 28 ? -8.031 -18.290 16.991 1.00 33.27 ? 28 CYS A CA 1 ATOM 204 C C . CYS A 1 28 ? -7.024 -18.099 15.862 1.00 33.45 ? 28 CYS A C 1 ATOM 205 O O . CYS A 1 28 ? -7.353 -18.323 14.698 1.00 33.44 ? 28 CYS A O 1 ATOM 206 C CB . CYS A 1 28 ? -9.413 -17.821 16.509 1.00 33.87 ? 28 CYS A CB 1 ATOM 207 S SG . CYS A 1 28 ? -10.722 -17.986 17.723 1.00 35.85 ? 28 CYS A SG 1 ATOM 208 N N . ASN A 1 29 ? -5.808 -17.670 16.190 1.00 33.94 ? 29 ASN A N 1 ATOM 209 C CA . ASN A 1 29 ? -4.755 -17.566 15.186 1.00 34.19 ? 29 ASN A CA 1 ATOM 210 C C . ASN A 1 29 ? -4.278 -18.974 14.856 1.00 35.09 ? 29 ASN A C 1 ATOM 211 O O . ASN A 1 29 ? -4.377 -19.422 13.710 1.00 35.18 ? 29 ASN A O 1 ATOM 212 C CB . ASN A 1 29 ? -3.604 -16.690 15.681 1.00 33.53 ? 29 ASN A CB 1 ATOM 213 C CG . ASN A 1 29 ? -2.625 -16.323 14.574 1.00 32.70 ? 29 ASN A CG 1 ATOM 214 O OD1 . ASN A 1 29 ? -1.944 -17.183 14.017 1.00 30.62 ? 29 ASN A OD1 1 ATOM 215 N ND2 . ASN A 1 29 ? -2.536 -15.029 14.265 1.00 31.96 ? 29 ASN A ND2 1 ATOM 216 N N . ASN A 1 30 ? -3.789 -19.660 15.888 1.00 36.00 ? 30 ASN A N 1 ATOM 217 C CA . ASN A 1 30 ? -3.405 -21.056 15.832 1.00 36.75 ? 30 ASN A CA 1 ATOM 218 C C . ASN A 1 30 ? -4.662 -21.890 15.984 1.00 37.36 ? 30 ASN A C 1 ATOM 219 O O . ASN A 1 30 ? -5.366 -21.761 16.975 1.00 37.27 ? 30 ASN A O 1 ATOM 220 C CB . ASN A 1 30 ? -2.422 -21.337 16.971 1.00 36.86 ? 30 ASN A CB 1 ATOM 221 C CG . ASN A 1 30 ? -1.743 -22.679 16.843 1.00 37.39 ? 30 ASN A CG 1 ATOM 222 O OD1 . ASN A 1 30 ? -2.341 -23.711 17.140 1.00 38.26 ? 30 ASN A OD1 1 ATOM 223 N ND2 . ASN A 1 30 ? -0.480 -22.675 16.412 1.00 37.22 ? 30 ASN A ND2 1 ATOM 224 N N . ARG A 1 31 ? -4.955 -22.731 14.996 1.00 38.52 ? 31 ARG A N 1 ATOM 225 C CA . ARG A 1 31 ? -6.212 -23.507 14.985 1.00 39.76 ? 31 ARG A CA 1 ATOM 226 C C . ARG A 1 31 ? -6.271 -24.645 16.024 1.00 39.96 ? 31 ARG A C 1 ATOM 227 O O . ARG A 1 31 ? -7.303 -24.855 16.676 1.00 40.03 ? 31 ARG A O 1 ATOM 228 C CB . ARG A 1 31 ? -6.498 -24.071 13.587 1.00 39.88 ? 31 ARG A CB 1 ATOM 229 C CG . ARG A 1 31 ? -7.099 -23.093 12.604 1.00 41.08 ? 31 ARG A CG 1 ATOM 230 C CD . ARG A 1 31 ? -7.409 -23.804 11.285 1.00 44.09 ? 31 ARG A CD 1 ATOM 231 N NE . ARG A 1 31 ? -8.077 -22.941 10.300 1.00 46.08 ? 31 ARG A NE 1 ATOM 232 C CZ . ARG A 1 31 ? -7.570 -22.611 9.109 1.00 46.84 ? 31 ARG A CZ 1 ATOM 233 N NH1 . ARG A 1 31 ? -6.376 -23.063 8.733 1.00 46.79 ? 31 ARG A NH1 1 ATOM 234 N NH2 . ARG A 1 31 ? -8.263 -21.827 8.287 1.00 47.29 ? 31 ARG A NH2 1 ATOM 235 N N . ARG A 1 32 ? -5.173 -25.383 16.168 1.00 40.07 ? 32 ARG A N 1 ATOM 236 C CA . ARG A 1 32 ? -5.156 -26.503 17.101 1.00 40.43 ? 32 ARG A CA 1 ATOM 237 C C . ARG A 1 32 ? -4.954 -26.077 18.554 1.00 39.79 ? 32 ARG A C 1 ATOM 238 O O . ARG A 1 32 ? -5.287 -26.818 19.472 1.00 39.79 ? 32 ARG A O 1 ATOM 239 C CB . ARG A 1 32 ? -4.130 -27.564 16.678 1.00 40.65 ? 32 ARG A CB 1 ATOM 240 C CG . ARG A 1 32 ? -2.625 -27.199 16.899 1.00 43.40 ? 32 ARG A CG 1 ATOM 241 C CD . ARG A 1 32 ? -1.883 -28.559 17.251 1.00 47.38 ? 32 ARG A CD 1 ATOM 242 N NE . ARG A 1 32 ? -1.636 -29.530 16.128 1.00 50.58 ? 32 ARG A NE 1 ATOM 243 C CZ . ARG A 1 32 ? -2.558 -29.933 15.212 1.00 52.17 ? 32 ARG A CZ 1 ATOM 244 N NH1 . ARG A 1 32 ? -2.204 -30.863 14.255 1.00 52.67 ? 32 ARG A NH1 1 ATOM 245 N NH2 . ARG A 1 32 ? -3.806 -29.402 15.190 1.00 53.13 ? 32 ARG A NH2 1 ATOM 246 N N . SER A 1 33 ? -4.407 -24.879 18.742 1.00 39.20 ? 33 SER A N 1 ATOM 247 C CA . SER A 1 33 ? -4.178 -24.316 20.065 1.00 38.70 ? 33 SER A CA 1 ATOM 248 C C . SER A 1 33 ? -4.582 -22.826 20.092 1.00 37.89 ? 33 SER A C 1 ATOM 249 O O . SER A 1 33 ? -3.731 -21.944 20.011 1.00 38.41 ? 33 SER A O 1 ATOM 250 C CB . SER A 1 33 ? -2.716 -24.515 20.462 1.00 38.78 ? 33 SER A CB 1 ATOM 251 O OG . SER A 1 33 ? -2.591 -24.554 21.874 1.00 40.29 ? 33 SER A OG 1 ATOM 252 N N . PRO A 1 34 ? -5.893 -22.549 20.203 1.00 36.90 ? 34 PRO A N 1 ATOM 253 C CA . PRO A 1 34 ? -6.503 -21.230 19.976 1.00 36.14 ? 34 PRO A CA 1 ATOM 254 C C . PRO A 1 34 ? -6.030 -20.054 20.839 1.00 35.48 ? 34 PRO A C 1 ATOM 255 O O . PRO A 1 34 ? -6.145 -18.913 20.402 1.00 35.28 ? 34 PRO A O 1 ATOM 256 C CB . PRO A 1 34 ? -7.989 -21.492 20.227 1.00 35.87 ? 34 PRO A CB 1 ATOM 257 C CG . PRO A 1 34 ? -8.142 -22.971 20.009 1.00 36.22 ? 34 PRO A CG 1 ATOM 258 C CD . PRO A 1 34 ? -6.909 -23.554 20.562 1.00 36.57 ? 34 PRO A CD 1 ATOM 259 N N . ALA A 1 35 ? -5.522 -20.301 22.041 1.00 34.86 ? 35 ALA A N 1 ATOM 260 C CA . ALA A 1 35 ? -5.094 -19.181 22.898 1.00 33.95 ? 35 ALA A CA 1 ATOM 261 C C . ALA A 1 35 ? -3.629 -18.729 22.689 1.00 33.44 ? 35 ALA A C 1 ATOM 262 O O . ALA A 1 35 ? -3.184 -17.758 23.306 1.00 33.47 ? 35 ALA A O 1 ATOM 263 C CB . ALA A 1 35 ? -5.373 -19.484 24.360 1.00 33.58 ? 35 ALA A CB 1 ATOM 264 N N . LEU A 1 36 ? -2.891 -19.412 21.811 1.00 32.65 ? 36 LEU A N 1 ATOM 265 C CA . LEU A 1 36 ? -1.489 -19.065 21.565 1.00 32.00 ? 36 LEU A CA 1 ATOM 266 C C . LEU A 1 36 ? -1.359 -17.673 20.971 1.00 31.25 ? 36 LEU A C 1 ATOM 267 O O . LEU A 1 36 ? -1.801 -17.438 19.846 1.00 30.85 ? 36 LEU A O 1 ATOM 268 C CB . LEU A 1 36 ? -0.833 -20.059 20.607 1.00 32.08 ? 36 LEU A CB 1 ATOM 269 C CG . LEU A 1 36 ? -0.280 -21.404 21.095 1.00 32.85 ? 36 LEU A CG 1 ATOM 270 C CD1 . LEU A 1 36 ? 0.334 -22.123 19.884 1.00 32.22 ? 36 LEU A CD1 1 ATOM 271 C CD2 . LEU A 1 36 ? 0.744 -21.244 22.249 1.00 32.22 ? 36 LEU A CD2 1 ATOM 272 N N . GLY A 1 37 ? -0.750 -16.760 21.727 1.00 30.65 ? 37 GLY A N 1 ATOM 273 C CA . GLY A 1 37 ? -0.494 -15.396 21.243 1.00 30.04 ? 37 GLY A CA 1 ATOM 274 C C . GLY A 1 37 ? -1.560 -14.384 21.612 1.00 29.58 ? 37 GLY A C 1 ATOM 275 O O . GLY A 1 37 ? -1.468 -13.217 21.249 1.00 29.55 ? 37 GLY A O 1 ATOM 276 N N . ALA A 1 38 ? -2.568 -14.832 22.356 1.00 29.34 ? 38 ALA A N 1 ATOM 277 C CA . ALA A 1 38 ? -3.687 -13.986 22.740 1.00 28.91 ? 38 ALA A CA 1 ATOM 278 C C . ALA A 1 38 ? -3.320 -13.072 23.893 1.00 28.56 ? 38 ALA A C 1 ATOM 279 O O . ALA A 1 38 ? -2.543 -13.445 24.769 1.00 28.55 ? 38 ALA A O 1 ATOM 280 C CB . ALA A 1 38 ? -4.907 -14.840 23.101 1.00 28.65 ? 38 ALA A CB 1 ATOM 281 N N . ALA A 1 39 ? -3.893 -11.873 23.874 1.00 28.60 ? 39 ALA A N 1 ATOM 282 C CA . ALA A 1 39 ? -3.817 -10.932 24.979 1.00 29.05 ? 39 ALA A CA 1 ATOM 283 C C . ALA A 1 39 ? -4.437 -11.483 26.250 1.00 29.41 ? 39 ALA A C 1 ATOM 284 O O . ALA A 1 39 ? -5.271 -12.388 26.194 1.00 29.79 ? 39 ALA A O 1 ATOM 285 C CB . ALA A 1 39 ? -4.483 -9.632 24.600 1.00 28.95 ? 39 ALA A CB 1 ATOM 286 N N . ASN A 1 40 ? -3.802 -10.961 27.393 1.00 30.11 ? 40 ASN A N 1 ATOM 287 C CA . ASN A 1 40 ? -4.158 -11.362 28.760 1.00 31.01 ? 40 ASN A CA 1 ATOM 288 C C . ASN A 1 40 ? -3.785 -12.776 29.156 1.00 31.03 ? 40 ASN A C 1 ATOM 289 O O . ASN A 1 40 ? -4.540 -13.448 29.837 1.00 31.21 ? 40 ASN A O 1 ATOM 290 C CB . ASN A 1 40 ? -5.630 -11.091 29.050 1.00 31.09 ? 40 ASN A CB 1 ATOM 291 C CG . ASN A 1 40 ? -5.881 -9.649 29.376 1.00 34.38 ? 40 ASN A CG 1 ATOM 292 O OD1 . ASN A 1 40 ? -5.352 -9.120 30.360 1.00 37.48 ? 40 ASN A OD1 1 ATOM 293 N ND2 . ASN A 1 40 ? -6.686 -8.983 28.545 1.00 38.34 ? 40 ASN A ND2 1 ATOM 294 N N . ARG A 1 41 ? -2.614 -13.223 28.724 1.00 31.16 ? 41 ARG A N 1 ATOM 295 C CA . ARG A 1 41 ? -2.088 -14.521 29.130 1.00 31.15 ? 41 ARG A CA 1 ATOM 296 C C . ARG A 1 41 ? -0.658 -14.318 29.589 1.00 30.66 ? 41 ARG A C 1 ATOM 297 O O . ARG A 1 41 ? -0.072 -13.245 29.394 1.00 30.75 ? 41 ARG A O 1 ATOM 298 C CB . ARG A 1 41 ? -2.124 -15.528 27.977 1.00 31.59 ? 41 ARG A CB 1 ATOM 299 C CG . ARG A 1 41 ? -3.468 -15.682 27.291 1.00 33.11 ? 41 ARG A CG 1 ATOM 300 C CD . ARG A 1 41 ? -4.281 -16.819 27.840 1.00 35.65 ? 41 ARG A CD 1 ATOM 301 N NE . ARG A 1 41 ? -5.601 -16.844 27.212 1.00 40.45 ? 41 ARG A NE 1 ATOM 302 C CZ . ARG A 1 41 ? -6.507 -17.814 27.359 1.00 42.14 ? 41 ARG A CZ 1 ATOM 303 N NH1 . ARG A 1 41 ? -6.254 -18.875 28.124 1.00 41.41 ? 41 ARG A NH1 1 ATOM 304 N NH2 . ARG A 1 41 ? -7.678 -17.718 26.730 1.00 43.49 ? 41 ARG A NH2 1 ATOM 305 N N . ALA A 1 42 ? -0.095 -15.353 30.196 1.00 29.61 ? 42 ALA A N 1 ATOM 306 C CA . ALA A 1 42 ? 1.244 -15.274 30.738 1.00 28.90 ? 42 ALA A CA 1 ATOM 307 C C . ALA A 1 42 ? 2.243 -14.997 29.624 1.00 28.41 ? 42 ALA A C 1 ATOM 308 O O . ALA A 1 42 ? 2.103 -15.531 28.526 1.00 28.90 ? 42 ALA A O 1 ATOM 309 C CB . ALA A 1 42 ? 1.583 -16.570 31.445 1.00 28.73 ? 42 ALA A CB 1 ATOM 310 N N . LEU A 1 43 ? 3.235 -14.152 29.894 1.00 27.87 ? 43 LEU A N 1 ATOM 311 C CA . LEU A 1 43 ? 4.424 -14.079 29.041 1.00 27.06 ? 43 LEU A CA 1 ATOM 312 C C . LEU A 1 43 ? 5.008 -15.489 29.010 1.00 26.74 ? 43 LEU A C 1 ATOM 313 O O . LEU A 1 43 ? 5.009 -16.172 30.039 1.00 27.05 ? 43 LEU A O 1 ATOM 314 C CB . LEU A 1 43 ? 5.481 -13.122 29.623 1.00 26.96 ? 43 LEU A CB 1 ATOM 315 C CG . LEU A 1 43 ? 5.623 -11.596 29.422 1.00 25.79 ? 43 LEU A CG 1 ATOM 316 C CD1 . LEU A 1 43 ? 5.060 -11.077 28.077 1.00 23.84 ? 43 LEU A CD1 1 ATOM 317 C CD2 . LEU A 1 43 ? 5.078 -10.816 30.590 1.00 21.90 ? 43 LEU A CD2 1 ATOM 318 N N . ALA A 1 44 ? 5.473 -15.940 27.847 1.00 25.92 ? 44 ALA A N 1 ATOM 319 C CA . ALA A 1 44 ? 6.182 -17.218 27.758 1.00 25.08 ? 44 ALA A CA 1 ATOM 320 C C . ALA A 1 44 ? 7.512 -17.213 28.551 1.00 25.04 ? 44 ALA A C 1 ATOM 321 O O . ALA A 1 44 ? 8.144 -16.168 28.727 1.00 24.67 ? 44 ALA A O 1 ATOM 322 C CB . ALA A 1 44 ? 6.429 -17.565 26.309 1.00 25.09 ? 44 ALA A CB 1 ATOM 323 N N . ARG A 1 45 ? 7.929 -18.381 29.030 1.00 24.96 ? 45 ARG A N 1 ATOM 324 C CA . ARG A 1 45 ? 9.224 -18.509 29.696 1.00 25.03 ? 45 ARG A CA 1 ATOM 325 C C . ARG A 1 45 ? 10.145 -19.353 28.857 1.00 24.97 ? 45 ARG A C 1 ATOM 326 O O . ARG A 1 45 ? 9.930 -20.548 28.759 1.00 25.35 ? 45 ARG A O 1 ATOM 327 C CB . ARG A 1 45 ? 9.083 -19.177 31.069 1.00 25.01 ? 45 ARG A CB 1 ATOM 328 C CG . ARG A 1 45 ? 8.445 -18.310 32.128 1.00 25.84 ? 45 ARG A CG 1 ATOM 329 C CD . ARG A 1 45 ? 9.463 -17.542 32.953 1.00 26.30 ? 45 ARG A CD 1 ATOM 330 N NE . ARG A 1 45 ? 8.768 -16.693 33.922 1.00 26.07 ? 45 ARG A NE 1 ATOM 331 C CZ . ARG A 1 45 ? 9.330 -15.718 34.629 1.00 26.15 ? 45 ARG A CZ 1 ATOM 332 N NH1 . ARG A 1 45 ? 10.629 -15.436 34.515 1.00 26.65 ? 45 ARG A NH1 1 ATOM 333 N NH2 . ARG A 1 45 ? 8.580 -15.023 35.464 1.00 25.43 ? 45 ARG A NH2 1 ATOM 334 N N . TRP A 1 46 ? 11.161 -18.741 28.253 1.00 24.94 ? 46 TRP A N 1 ATOM 335 C CA . TRP A 1 46 ? 12.180 -19.503 27.547 1.00 24.86 ? 46 TRP A CA 1 ATOM 336 C C . TRP A 1 46 ? 13.095 -20.229 28.534 1.00 25.19 ? 46 TRP A C 1 ATOM 337 O O . TRP A 1 46 ? 13.691 -21.266 28.206 1.00 25.61 ? 46 TRP A O 1 ATOM 338 C CB . TRP A 1 46 ? 12.994 -18.623 26.595 1.00 24.45 ? 46 TRP A CB 1 ATOM 339 C CG . TRP A 1 46 ? 12.206 -18.104 25.426 1.00 24.54 ? 46 TRP A CG 1 ATOM 340 C CD1 . TRP A 1 46 ? 10.964 -18.507 25.029 1.00 24.98 ? 46 TRP A CD1 1 ATOM 341 C CD2 . TRP A 1 46 ? 12.620 -17.103 24.489 1.00 24.26 ? 46 TRP A CD2 1 ATOM 342 N NE1 . TRP A 1 46 ? 10.573 -17.806 23.914 1.00 26.14 ? 46 TRP A NE1 1 ATOM 343 C CE2 . TRP A 1 46 ? 11.570 -16.938 23.564 1.00 24.61 ? 46 TRP A CE2 1 ATOM 344 C CE3 . TRP A 1 46 ? 13.780 -16.322 24.349 1.00 25.16 ? 46 TRP A CE3 1 ATOM 345 C CZ2 . TRP A 1 46 ? 11.633 -16.024 22.512 1.00 27.17 ? 46 TRP A CZ2 1 ATOM 346 C CZ3 . TRP A 1 46 ? 13.853 -15.419 23.311 1.00 26.37 ? 46 TRP A CZ3 1 ATOM 347 C CH2 . TRP A 1 46 ? 12.780 -15.268 22.401 1.00 28.16 ? 46 TRP A CH2 1 ATOM 348 N N . LEU A 1 47 ? 13.194 -19.689 29.739 1.00 24.81 ? 47 LEU A N 1 ATOM 349 C CA . LEU A 1 47 ? 13.964 -20.307 30.797 1.00 25.37 ? 47 LEU A CA 1 ATOM 350 C C . LEU A 1 47 ? 13.184 -20.190 32.097 1.00 25.49 ? 47 LEU A C 1 ATOM 351 O O . LEU A 1 47 ? 12.379 -19.255 32.245 1.00 25.64 ? 47 LEU A O 1 ATOM 352 C CB . LEU A 1 47 ? 15.332 -19.626 30.941 1.00 25.27 ? 47 LEU A CB 1 ATOM 353 C CG . LEU A 1 47 ? 16.512 -20.061 30.073 1.00 25.34 ? 47 LEU A CG 1 ATOM 354 C CD1 . LEU A 1 47 ? 17.636 -19.021 30.194 1.00 25.02 ? 47 LEU A CD1 1 ATOM 355 C CD2 . LEU A 1 47 ? 16.998 -21.468 30.459 1.00 24.34 ? 47 LEU A CD2 1 ATOM 356 N N . PRO A 1 48 ? 13.415 -21.128 33.042 1.00 25.23 ? 48 PRO A N 1 ATOM 357 C CA . PRO A 1 48 ? 12.734 -21.071 34.334 1.00 25.23 ? 48 PRO A CA 1 ATOM 358 C C . PRO A 1 48 ? 13.039 -19.788 35.080 1.00 25.07 ? 48 PRO A C 1 ATOM 359 O O . PRO A 1 48 ? 14.153 -19.284 34.995 1.00 25.13 ? 48 PRO A O 1 ATOM 360 C CB . PRO A 1 48 ? 13.281 -22.295 35.088 1.00 24.76 ? 48 PRO A CB 1 ATOM 361 C CG . PRO A 1 48 ? 13.741 -23.222 34.029 1.00 24.95 ? 48 PRO A CG 1 ATOM 362 C CD . PRO A 1 48 ? 14.290 -22.311 32.945 1.00 25.63 ? 48 PRO A CD 1 ATOM 363 N N . ALA A 1 49 ? 12.024 -19.256 35.758 1.00 25.24 ? 49 ALA A N 1 ATOM 364 C CA . ALA A 1 49 ? 12.118 -18.011 36.501 1.00 25.73 ? 49 ALA A CA 1 ATOM 365 C C . ALA A 1 49 ? 13.078 -18.179 37.659 1.00 26.17 ? 49 ALA A C 1 ATOM 366 O O . ALA A 1 49 ? 13.205 -19.252 38.212 1.00 26.45 ? 49 ALA A O 1 ATOM 367 C CB . ALA A 1 49 ? 10.744 -17.587 37.006 1.00 25.31 ? 49 ALA A CB 1 ATOM 368 N N . GLU A 1 50 ? 13.777 -17.115 38.012 1.00 27.08 ? 50 GLU A N 1 ATOM 369 C CA . GLU A 1 50 ? 14.671 -17.177 39.147 1.00 27.65 ? 50 GLU A CA 1 ATOM 370 C C . GLU A 1 50 ? 14.218 -16.166 40.161 1.00 27.98 ? 50 GLU A C 1 ATOM 371 O O . GLU A 1 50 ? 14.387 -14.966 39.976 1.00 28.28 ? 50 GLU A O 1 ATOM 372 C CB . GLU A 1 50 ? 16.120 -16.970 38.723 1.00 27.70 ? 50 GLU A CB 1 ATOM 373 C CG . GLU A 1 50 ? 16.525 -17.927 37.583 1.00 29.25 ? 50 GLU A CG 1 ATOM 374 C CD . GLU A 1 50 ? 18.019 -18.112 37.441 1.00 29.12 ? 50 GLU A CD 1 ATOM 375 O OE1 . GLU A 1 50 ? 18.795 -17.299 37.991 1.00 26.69 ? 50 GLU A OE1 1 ATOM 376 O OE2 . GLU A 1 50 ? 18.401 -19.089 36.765 1.00 31.08 ? 50 GLU A OE2 1 ATOM 377 N N . TYR A 1 51 ? 13.588 -16.683 41.211 1.00 28.31 ? 51 TYR A N 1 ATOM 378 C CA . TYR A 1 51 ? 13.078 -15.896 42.307 1.00 28.23 ? 51 TYR A CA 1 ATOM 379 C C . TYR A 1 51 ? 13.872 -16.217 43.562 1.00 28.49 ? 51 TYR A C 1 ATOM 380 O O . TYR A 1 51 ? 14.446 -17.284 43.670 1.00 28.69 ? 51 TYR A O 1 ATOM 381 C CB . TYR A 1 51 ? 11.611 -16.235 42.523 1.00 28.25 ? 51 TYR A CB 1 ATOM 382 C CG . TYR A 1 51 ? 10.679 -15.612 41.518 1.00 27.21 ? 51 TYR A CG 1 ATOM 383 C CD1 . TYR A 1 51 ? 9.929 -16.391 40.656 1.00 26.05 ? 51 TYR A CD1 1 ATOM 384 C CD2 . TYR A 1 51 ? 10.536 -14.241 41.445 1.00 26.75 ? 51 TYR A CD2 1 ATOM 385 C CE1 . TYR A 1 51 ? 9.076 -15.809 39.745 1.00 25.75 ? 51 TYR A CE1 1 ATOM 386 C CE2 . TYR A 1 51 ? 9.691 -13.662 40.546 1.00 25.28 ? 51 TYR A CE2 1 ATOM 387 C CZ . TYR A 1 51 ? 8.966 -14.440 39.702 1.00 25.62 ? 51 TYR A CZ 1 ATOM 388 O OH . TYR A 1 51 ? 8.123 -13.822 38.800 1.00 28.80 ? 51 TYR A OH 1 ATOM 389 N N . GLU A 1 52 ? 13.894 -15.286 44.505 1.00 28.69 ? 52 GLU A N 1 ATOM 390 C CA . GLU A 1 52 ? 14.597 -15.446 45.773 1.00 29.33 ? 52 GLU A CA 1 ATOM 391 C C . GLU A 1 52 ? 14.193 -16.704 46.549 1.00 29.63 ? 52 GLU A C 1 ATOM 392 O O . GLU A 1 52 ? 15.043 -17.388 47.115 1.00 29.60 ? 52 GLU A O 1 ATOM 393 C CB . GLU A 1 52 ? 14.314 -14.228 46.632 1.00 29.22 ? 52 GLU A CB 1 ATOM 394 C CG . GLU A 1 52 ? 15.221 -14.026 47.803 1.00 30.18 ? 52 GLU A CG 1 ATOM 395 C CD . GLU A 1 52 ? 14.759 -12.858 48.626 1.00 31.15 ? 52 GLU A CD 1 ATOM 396 O OE1 . GLU A 1 52 ? 13.775 -13.011 49.364 1.00 29.50 ? 52 GLU A OE1 1 ATOM 397 O OE2 . GLU A 1 52 ? 15.368 -11.778 48.515 1.00 33.51 ? 52 GLU A OE2 1 ATOM 398 N N . ASP A 1 53 ? 12.892 -16.978 46.595 1.00 30.09 ? 53 ASP A N 1 ATOM 399 C CA . ASP A 1 53 ? 12.360 -18.111 47.343 1.00 30.61 ? 53 ASP A CA 1 ATOM 400 C C . ASP A 1 53 ? 11.854 -19.162 46.375 1.00 30.87 ? 53 ASP A C 1 ATOM 401 O O . ASP A 1 53 ? 10.950 -19.942 46.690 1.00 30.73 ? 53 ASP A O 1 ATOM 402 C CB . ASP A 1 53 ? 11.255 -17.673 48.313 1.00 30.35 ? 53 ASP A CB 1 ATOM 403 C CG . ASP A 1 53 ? 9.985 -17.223 47.609 1.00 31.46 ? 53 ASP A CG 1 ATOM 404 O OD1 . ASP A 1 53 ? 10.010 -16.992 46.379 1.00 31.74 ? 53 ASP A OD1 1 ATOM 405 O OD2 . ASP A 1 53 ? 8.949 -17.097 48.302 1.00 31.04 ? 53 ASP A OD2 1 ATOM 406 N N . GLY A 1 54 ? 12.445 -19.157 45.183 1.00 31.08 ? 54 GLY A N 1 ATOM 407 C CA . GLY A 1 54 ? 12.113 -20.126 44.166 1.00 31.29 ? 54 GLY A CA 1 ATOM 408 C C . GLY A 1 54 ? 10.829 -19.805 43.436 1.00 31.66 ? 54 GLY A C 1 ATOM 409 O O . GLY A 1 54 ? 10.689 -20.173 42.269 1.00 32.09 ? 54 GLY A O 1 ATOM 410 N N . LEU A 1 55 ? 9.915 -19.085 44.093 1.00 31.43 ? 55 LEU A N 1 ATOM 411 C CA . LEU A 1 55 ? 8.523 -19.042 43.650 1.00 31.34 ? 55 LEU A CA 1 ATOM 412 C C . LEU A 1 55 ? 7.947 -17.707 43.196 1.00 31.16 ? 55 LEU A C 1 ATOM 413 O O . LEU A 1 55 ? 7.152 -17.673 42.254 1.00 30.87 ? 55 LEU A O 1 ATOM 414 C CB . LEU A 1 55 ? 7.624 -19.642 44.726 1.00 31.80 ? 55 LEU A CB 1 ATOM 415 C CG . LEU A 1 55 ? 7.517 -21.163 44.774 1.00 32.05 ? 55 LEU A CG 1 ATOM 416 C CD1 . LEU A 1 55 ? 6.685 -21.548 45.978 1.00 33.44 ? 55 LEU A CD1 1 ATOM 417 C CD2 . LEU A 1 55 ? 6.875 -21.674 43.501 1.00 32.24 ? 55 LEU A CD2 1 ATOM 418 N N . ALA A 1 56 ? 8.329 -16.615 43.860 1.00 30.97 ? 56 ALA A N 1 ATOM 419 C CA . ALA A 1 56 ? 7.708 -15.319 43.590 1.00 30.47 ? 56 ALA A CA 1 ATOM 420 C C . ALA A 1 56 ? 8.529 -14.093 44.018 1.00 30.39 ? 56 ALA A C 1 ATOM 421 O O . ALA A 1 56 ? 8.383 -13.011 43.444 1.00 29.82 ? 56 ALA A O 1 ATOM 422 C CB . ALA A 1 56 ? 6.303 -15.275 44.201 1.00 30.15 ? 56 ALA A CB 1 ATOM 423 N N . LEU A 1 57 ? 9.258 -14.274 45.173 1.00 30.70 ? 57 LEU A N 1 ATOM 424 C CA . LEU A 1 57 ? 9.951 -13.136 45.761 1.00 30.92 ? 57 LEU A CA 1 ATOM 425 C C . LEU A 1 57 ? 11.153 -12.757 44.922 1.00 30.67 ? 57 LEU A C 1 ATOM 426 O O . LEU A 1 57 ? 11.970 -13.608 44.588 1.00 30.97 ? 57 LEU A O 1 ATOM 427 C CB . LEU A 1 57 ? 10.360 -13.390 47.219 1.00 31.37 ? 57 LEU A CB 1 ATOM 428 C CG . LEU A 1 57 ? 9.398 -12.980 48.352 1.00 32.31 ? 57 LEU A CG 1 ATOM 429 C CD1 . LEU A 1 57 ? 8.257 -12.074 47.876 1.00 32.81 ? 57 LEU A CD1 1 ATOM 430 C CD2 . LEU A 1 57 ? 8.829 -14.186 49.053 1.00 32.82 ? 57 LEU A CD2 1 ATOM 431 N N . PRO A 1 58 ? 11.260 -11.473 44.557 1.00 30.65 ? 58 PRO A N 1 ATOM 432 C CA . PRO A 1 58 ? 12.362 -11.088 43.684 1.00 30.53 ? 58 PRO A CA 1 ATOM 433 C C . PRO A 1 58 ? 13.670 -10.999 44.463 1.00 30.47 ? 58 PRO A C 1 ATOM 434 O O . PRO A 1 58 ? 13.652 -10.853 45.697 1.00 30.25 ? 58 PRO A O 1 ATOM 435 C CB . PRO A 1 58 ? 11.935 -9.715 43.165 1.00 30.43 ? 58 PRO A CB 1 ATOM 436 C CG . PRO A 1 58 ? 11.026 -9.180 44.208 1.00 30.62 ? 58 PRO A CG 1 ATOM 437 C CD . PRO A 1 58 ? 10.405 -10.331 44.929 1.00 30.28 ? 58 PRO A CD 1 ATOM 438 N N . PHE A 1 59 ? 14.786 -11.105 43.742 1.00 30.48 ? 59 PHE A N 1 ATOM 439 C CA . PHE A 1 59 ? 16.114 -10.976 44.332 1.00 30.39 ? 59 PHE A CA 1 ATOM 440 C C . PHE A 1 59 ? 16.308 -9.529 44.801 1.00 30.98 ? 59 PHE A C 1 ATOM 441 O O . PHE A 1 59 ? 15.946 -8.590 44.097 1.00 30.44 ? 59 PHE A O 1 ATOM 442 C CB . PHE A 1 59 ? 17.192 -11.410 43.333 1.00 29.89 ? 59 PHE A CB 1 ATOM 443 C CG . PHE A 1 59 ? 17.427 -12.904 43.291 1.00 28.89 ? 59 PHE A CG 1 ATOM 444 C CD1 . PHE A 1 59 ? 17.010 -13.660 42.191 1.00 27.59 ? 59 PHE A CD1 1 ATOM 445 C CD2 . PHE A 1 59 ? 18.087 -13.561 44.357 1.00 28.39 ? 59 PHE A CD2 1 ATOM 446 C CE1 . PHE A 1 59 ? 17.234 -15.061 42.150 1.00 27.55 ? 59 PHE A CE1 1 ATOM 447 C CE2 . PHE A 1 59 ? 18.321 -14.956 44.333 1.00 26.94 ? 59 PHE A CE2 1 ATOM 448 C CZ . PHE A 1 59 ? 17.892 -15.711 43.223 1.00 27.58 ? 59 PHE A CZ 1 ATOM 449 N N . GLY A 1 60 ? 16.836 -9.359 46.011 1.00 31.75 ? 60 GLY A N 1 ATOM 450 C CA . GLY A 1 60 ? 16.941 -8.030 46.611 1.00 32.98 ? 60 GLY A CA 1 ATOM 451 C C . GLY A 1 60 ? 15.878 -7.754 47.662 1.00 34.00 ? 60 GLY A C 1 ATOM 452 O O . GLY A 1 60 ? 16.054 -6.869 48.499 1.00 34.38 ? 60 GLY A O 1 ATOM 453 N N . TRP A 1 61 ? 14.793 -8.529 47.631 1.00 34.70 ? 61 TRP A N 1 ATOM 454 C CA . TRP A 1 61 ? 13.647 -8.360 48.533 1.00 35.34 ? 61 TRP A CA 1 ATOM 455 C C . TRP A 1 61 ? 14.020 -8.576 50.002 1.00 36.61 ? 61 TRP A C 1 ATOM 456 O O . TRP A 1 61 ? 13.744 -7.721 50.838 1.00 36.84 ? 61 TRP A O 1 ATOM 457 C CB . TRP A 1 61 ? 12.510 -9.300 48.112 1.00 34.87 ? 61 TRP A CB 1 ATOM 458 C CG . TRP A 1 61 ? 11.262 -9.201 48.939 1.00 33.66 ? 61 TRP A CG 1 ATOM 459 C CD1 . TRP A 1 61 ? 11.015 -9.817 50.135 1.00 31.92 ? 61 TRP A CD1 1 ATOM 460 C CD2 . TRP A 1 61 ? 10.077 -8.459 48.621 1.00 32.49 ? 61 TRP A CD2 1 ATOM 461 N NE1 . TRP A 1 61 ? 9.758 -9.494 50.586 1.00 31.30 ? 61 TRP A NE1 1 ATOM 462 C CE2 . TRP A 1 61 ? 9.160 -8.663 49.676 1.00 31.70 ? 61 TRP A CE2 1 ATOM 463 C CE3 . TRP A 1 61 ? 9.705 -7.634 47.553 1.00 31.77 ? 61 TRP A CE3 1 ATOM 464 C CZ2 . TRP A 1 61 ? 7.894 -8.080 49.689 1.00 31.75 ? 61 TRP A CZ2 1 ATOM 465 C CZ3 . TRP A 1 61 ? 8.441 -7.051 47.569 1.00 31.78 ? 61 TRP A CZ3 1 ATOM 466 C CH2 . TRP A 1 61 ? 7.555 -7.275 48.630 1.00 31.54 ? 61 TRP A CH2 1 ATOM 467 N N . THR A 1 62 ? 14.634 -9.717 50.311 1.00 38.12 ? 62 THR A N 1 ATOM 468 C CA . THR A 1 62 ? 15.088 -10.013 51.661 1.00 39.86 ? 62 THR A CA 1 ATOM 469 C C . THR A 1 62 ? 16.561 -9.620 51.792 1.00 41.53 ? 62 THR A C 1 ATOM 470 O O . THR A 1 62 ? 17.439 -10.216 51.151 1.00 41.48 ? 62 THR A O 1 ATOM 471 C CB . THR A 1 62 ? 14.907 -11.495 51.987 1.00 39.90 ? 62 THR A CB 1 ATOM 472 O OG1 . THR A 1 62 ? 13.623 -11.923 51.527 1.00 39.15 ? 62 THR A OG1 1 ATOM 473 C CG2 . THR A 1 62 ? 15.047 -11.758 53.502 1.00 40.19 ? 62 THR A CG2 1 ATOM 474 N N . GLN A 1 63 ? 16.822 -8.631 52.644 1.00 43.42 ? 63 GLN A N 1 ATOM 475 C CA . GLN A 1 63 ? 18.120 -7.937 52.691 1.00 45.29 ? 63 GLN A CA 1 ATOM 476 C C . GLN A 1 63 ? 19.306 -8.827 53.112 1.00 45.68 ? 63 GLN A C 1 ATOM 477 O O . GLN A 1 63 ? 20.453 -8.367 53.157 1.00 46.49 ? 63 GLN A O 1 ATOM 478 C CB . GLN A 1 63 ? 18.027 -6.715 53.633 1.00 45.70 ? 63 GLN A CB 1 ATOM 479 C CG . GLN A 1 63 ? 16.603 -6.109 53.796 1.00 48.37 ? 63 GLN A CG 1 ATOM 480 C CD . GLN A 1 63 ? 16.083 -5.413 52.523 1.00 51.15 ? 63 GLN A CD 1 ATOM 481 O OE1 . GLN A 1 63 ? 16.850 -4.767 51.792 1.00 53.04 ? 63 GLN A OE1 1 ATOM 482 N NE2 . GLN A 1 63 ? 14.775 -5.534 52.266 1.00 51.79 ? 63 GLN A NE2 1 ATOM 483 N N . ARG A 1 64 ? 19.029 -10.093 53.419 1.00 45.87 ? 64 ARG A N 1 ATOM 484 C CA . ARG A 1 64 ? 20.036 -10.988 53.986 1.00 45.73 ? 64 ARG A CA 1 ATOM 485 C C . ARG A 1 64 ? 20.210 -12.229 53.114 1.00 44.83 ? 64 ARG A C 1 ATOM 486 O O . ARG A 1 64 ? 21.119 -13.025 53.336 1.00 45.13 ? 64 ARG A O 1 ATOM 487 C CB . ARG A 1 64 ? 19.603 -11.420 55.392 1.00 46.37 ? 64 ARG A CB 1 ATOM 488 C CG . ARG A 1 64 ? 18.436 -12.413 55.356 1.00 49.11 ? 64 ARG A CG 1 ATOM 489 C CD . ARG A 1 64 ? 17.635 -12.458 56.640 1.00 53.28 ? 64 ARG A CD 1 ATOM 490 N NE . ARG A 1 64 ? 16.474 -13.337 56.477 1.00 55.70 ? 64 ARG A NE 1 ATOM 491 C CZ . ARG A 1 64 ? 16.494 -14.663 56.621 1.00 56.56 ? 64 ARG A CZ 1 ATOM 492 N NH1 . ARG A 1 64 ? 17.617 -15.299 56.936 1.00 56.88 ? 64 ARG A NH1 1 ATOM 493 N NH2 . ARG A 1 64 ? 15.380 -15.359 56.448 1.00 57.89 ? 64 ARG A NH2 1 ATOM 494 N N . LYS A 1 65 ? 19.306 -12.420 52.158 1.00 43.54 ? 65 LYS A N 1 ATOM 495 C CA . LYS A 1 65 ? 19.437 -13.513 51.208 1.00 42.07 ? 65 LYS A CA 1 ATOM 496 C C . LYS A 1 65 ? 20.281 -13.029 50.030 1.00 40.39 ? 65 LYS A C 1 ATOM 497 O O . LYS A 1 65 ? 20.047 -11.950 49.487 1.00 40.63 ? 65 LYS A O 1 ATOM 498 C CB . LYS A 1 65 ? 18.063 -14.019 50.740 1.00 42.47 ? 65 LYS A CB 1 ATOM 499 C CG . LYS A 1 65 ? 17.205 -14.674 51.823 1.00 43.51 ? 65 LYS A CG 1 ATOM 500 C CD . LYS A 1 65 ? 16.203 -15.637 51.193 1.00 47.00 ? 65 LYS A CD 1 ATOM 501 C CE . LYS A 1 65 ? 14.778 -15.461 51.762 1.00 48.87 ? 65 LYS A CE 1 ATOM 502 N NZ . LYS A 1 65 ? 13.685 -15.994 50.842 1.00 48.29 ? 65 LYS A NZ 1 ATOM 503 N N . THR A 1 66 ? 21.266 -13.823 49.650 1.00 38.13 ? 66 THR A N 1 ATOM 504 C CA . THR A 1 66 ? 22.145 -13.465 48.556 1.00 36.56 ? 66 THR A CA 1 ATOM 505 C C . THR A 1 66 ? 21.684 -14.077 47.242 1.00 35.08 ? 66 THR A C 1 ATOM 506 O O . THR A 1 66 ? 20.854 -14.974 47.228 1.00 34.77 ? 66 THR A O 1 ATOM 507 C CB . THR A 1 66 ? 23.585 -13.961 48.809 1.00 36.73 ? 66 THR A CB 1 ATOM 508 O OG1 . THR A 1 66 ? 23.600 -15.399 48.855 1.00 36.80 ? 66 THR A OG1 1 ATOM 509 C CG2 . THR A 1 66 ? 24.138 -13.385 50.109 1.00 36.96 ? 66 THR A CG2 1 ATOM 510 N N . ARG A 1 67 ? 22.232 -13.567 46.143 1.00 33.50 ? 67 ARG A N 1 ATOM 511 C CA . ARG A 1 67 ? 22.160 -14.238 44.866 1.00 32.10 ? 67 ARG A CA 1 ATOM 512 C C . ARG A 1 67 ? 23.550 -14.763 44.562 1.00 31.34 ? 67 ARG A C 1 ATOM 513 O O . ARG A 1 67 ? 24.471 -13.982 44.333 1.00 31.01 ? 67 ARG A O 1 ATOM 514 C CB . ARG A 1 67 ? 21.683 -13.287 43.762 1.00 31.78 ? 67 ARG A CB 1 ATOM 515 C CG . ARG A 1 67 ? 21.327 -14.016 42.476 1.00 31.24 ? 67 ARG A CG 1 ATOM 516 C CD . ARG A 1 67 ? 21.036 -13.088 41.332 1.00 30.55 ? 67 ARG A CD 1 ATOM 517 N NE . ARG A 1 67 ? 20.339 -13.825 40.282 1.00 31.72 ? 67 ARG A NE 1 ATOM 518 C CZ . ARG A 1 67 ? 19.478 -13.292 39.413 1.00 31.14 ? 67 ARG A CZ 1 ATOM 519 N NH1 . ARG A 1 67 ? 19.198 -11.992 39.432 1.00 30.51 ? 67 ARG A NH1 1 ATOM 520 N NH2 . ARG A 1 67 ? 18.900 -14.070 38.512 1.00 30.31 ? 67 ARG A NH2 1 ATOM 521 N N . ASN A 1 68 ? 23.703 -16.083 44.577 1.00 30.67 ? 68 ASN A N 1 ATOM 522 C CA . ASN A 1 68 ? 25.006 -16.716 44.365 1.00 30.41 ? 68 ASN A CA 1 ATOM 523 C C . ASN A 1 68 ? 26.114 -16.298 45.352 1.00 30.27 ? 68 ASN A C 1 ATOM 524 O O . ASN A 1 68 ? 27.275 -16.152 44.954 1.00 30.08 ? 68 ASN A O 1 ATOM 525 C CB . ASN A 1 68 ? 25.493 -16.484 42.922 1.00 30.75 ? 68 ASN A CB 1 ATOM 526 C CG . ASN A 1 68 ? 24.566 -17.097 41.880 1.00 30.80 ? 68 ASN A CG 1 ATOM 527 O OD1 . ASN A 1 68 ? 24.186 -18.261 41.978 1.00 31.32 ? 68 ASN A OD1 1 ATOM 528 N ND2 . ASN A 1 68 ? 24.196 -16.305 40.878 1.00 30.34 ? 68 ASN A ND2 1 ATOM 529 N N . GLY A 1 69 ? 25.766 -16.115 46.625 1.00 30.02 ? 69 GLY A N 1 ATOM 530 C CA . GLY A 1 69 ? 26.742 -15.692 47.635 1.00 30.29 ? 69 GLY A CA 1 ATOM 531 C C . GLY A 1 69 ? 26.887 -14.186 47.845 1.00 30.92 ? 69 GLY A C 1 ATOM 532 O O . GLY A 1 69 ? 27.577 -13.751 48.775 1.00 30.68 ? 69 GLY A O 1 ATOM 533 N N . PHE A 1 70 ? 26.239 -13.384 46.990 1.00 31.38 ? 70 PHE A N 1 ATOM 534 C CA . PHE A 1 70 ? 26.403 -11.925 47.020 1.00 31.51 ? 70 PHE A CA 1 ATOM 535 C C . PHE A 1 70 ? 25.084 -11.164 47.069 1.00 31.75 ? 70 PHE A C 1 ATOM 536 O O . PHE A 1 70 ? 24.072 -11.605 46.515 1.00 31.52 ? 70 PHE A O 1 ATOM 537 C CB . PHE A 1 70 ? 27.192 -11.422 45.807 1.00 31.45 ? 70 PHE A CB 1 ATOM 538 C CG . PHE A 1 70 ? 28.512 -12.109 45.589 1.00 32.48 ? 70 PHE A CG 1 ATOM 539 C CD1 . PHE A 1 70 ? 28.661 -13.040 44.559 1.00 32.07 ? 70 PHE A CD1 1 ATOM 540 C CD2 . PHE A 1 70 ? 29.618 -11.808 46.394 1.00 33.16 ? 70 PHE A CD2 1 ATOM 541 C CE1 . PHE A 1 70 ? 29.878 -13.663 44.340 1.00 32.17 ? 70 PHE A CE1 1 ATOM 542 C CE2 . PHE A 1 70 ? 30.846 -12.437 46.182 1.00 32.43 ? 70 PHE A CE2 1 ATOM 543 C CZ . PHE A 1 70 ? 30.970 -13.369 45.151 1.00 32.28 ? 70 PHE A CZ 1 ATOM 544 N N . ARG A 1 71 ? 25.120 -10.007 47.734 1.00 31.95 ? 71 ARG A N 1 ATOM 545 C CA . ARG A 1 71 ? 24.022 -9.057 47.716 1.00 32.15 ? 71 ARG A CA 1 ATOM 546 C C . ARG A 1 71 ? 23.915 -8.452 46.331 1.00 31.00 ? 71 ARG A C 1 ATOM 547 O O . ARG A 1 71 ? 24.913 -8.029 45.760 1.00 30.81 ? 71 ARG A O 1 ATOM 548 C CB . ARG A 1 71 ? 24.256 -7.939 48.735 1.00 32.96 ? 71 ARG A CB 1 ATOM 549 C CG . ARG A 1 71 ? 23.800 -8.270 50.152 1.00 36.69 ? 71 ARG A CG 1 ATOM 550 C CD . ARG A 1 71 ? 24.476 -7.348 51.166 1.00 42.27 ? 71 ARG A CD 1 ATOM 551 N NE . ARG A 1 71 ? 24.212 -7.772 52.541 1.00 46.63 ? 71 ARG A NE 1 ATOM 552 C CZ . ARG A 1 71 ? 23.168 -7.371 53.267 1.00 49.45 ? 71 ARG A CZ 1 ATOM 553 N NH1 . ARG A 1 71 ? 22.274 -6.521 52.754 1.00 50.07 ? 71 ARG A NH1 1 ATOM 554 N NH2 . ARG A 1 71 ? 23.017 -7.814 54.514 1.00 50.45 ? 71 ARG A NH2 1 ATOM 555 N N . VAL A 1 72 ? 22.703 -8.420 45.787 1.00 30.20 ? 72 VAL A N 1 ATOM 556 C CA . VAL A 1 72 ? 22.477 -7.705 44.545 1.00 29.62 ? 72 VAL A CA 1 ATOM 557 C C . VAL A 1 72 ? 22.494 -6.208 44.853 1.00 29.12 ? 72 VAL A C 1 ATOM 558 O O . VAL A 1 72 ? 21.890 -5.776 45.837 1.00 29.45 ? 72 VAL A O 1 ATOM 559 C CB . VAL A 1 72 ? 21.160 -8.126 43.835 1.00 29.55 ? 72 VAL A CB 1 ATOM 560 C CG1 . VAL A 1 72 ? 21.315 -9.494 43.227 1.00 29.35 ? 72 VAL A CG1 1 ATOM 561 C CG2 . VAL A 1 72 ? 19.980 -8.081 44.785 1.00 29.42 ? 72 VAL A CG2 1 ATOM 562 N N . PRO A 1 73 ? 23.195 -5.417 44.024 1.00 28.52 ? 73 PRO A N 1 ATOM 563 C CA . PRO A 1 73 ? 23.311 -3.984 44.257 1.00 28.05 ? 73 PRO A CA 1 ATOM 564 C C . PRO A 1 73 ? 21.971 -3.295 44.063 1.00 27.91 ? 73 PRO A C 1 ATOM 565 O O . PRO A 1 73 ? 21.113 -3.812 43.336 1.00 27.80 ? 73 PRO A O 1 ATOM 566 C CB . PRO A 1 73 ? 24.296 -3.542 43.182 1.00 28.11 ? 73 PRO A CB 1 ATOM 567 C CG . PRO A 1 73 ? 24.126 -4.556 42.083 1.00 28.29 ? 73 PRO A CG 1 ATOM 568 C CD . PRO A 1 73 ? 23.907 -5.835 42.801 1.00 28.51 ? 73 PRO A CD 1 ATOM 569 N N . LEU A 1 74 ? 21.787 -2.154 44.723 1.00 27.53 ? 74 LEU A N 1 ATOM 570 C CA . LEU A 1 74 ? 20.546 -1.383 44.607 1.00 27.50 ? 74 LEU A CA 1 ATOM 571 C C . LEU A 1 74 ? 20.368 -0.853 43.190 1.00 27.21 ? 74 LEU A C 1 ATOM 572 O O . LEU A 1 74 ? 21.301 -0.309 42.605 1.00 26.93 ? 74 LEU A O 1 ATOM 573 C CB . LEU A 1 74 ? 20.541 -0.201 45.586 1.00 27.42 ? 74 LEU A CB 1 ATOM 574 C CG . LEU A 1 74 ? 20.446 -0.452 47.087 1.00 27.33 ? 74 LEU A CG 1 ATOM 575 C CD1 . LEU A 1 74 ? 21.047 0.729 47.837 1.00 27.87 ? 74 LEU A CD1 1 ATOM 576 C CD2 . LEU A 1 74 ? 18.992 -0.673 47.472 1.00 26.75 ? 74 LEU A CD2 1 ATOM 577 N N . ALA A 1 75 ? 19.164 -0.993 42.652 1.00 27.28 ? 75 ALA A N 1 ATOM 578 C CA . ALA A 1 75 ? 18.883 -0.580 41.273 1.00 27.41 ? 75 ALA A CA 1 ATOM 579 C C . ALA A 1 75 ? 19.330 0.851 40.975 1.00 27.65 ? 75 ALA A C 1 ATOM 580 O O . ALA A 1 75 ? 19.959 1.107 39.960 1.00 27.49 ? 75 ALA A O 1 ATOM 581 C CB . ALA A 1 75 ? 17.414 -0.756 40.964 1.00 27.27 ? 75 ALA A CB 1 ATOM 582 N N . ARG A 1 76 ? 19.002 1.781 41.864 1.00 28.49 ? 76 ARG A N 1 ATOM 583 C CA . ARG A 1 76 ? 19.400 3.190 41.710 1.00 29.14 ? 76 ARG A CA 1 ATOM 584 C C . ARG A 1 76 ? 20.927 3.428 41.802 1.00 29.97 ? 76 ARG A C 1 ATOM 585 O O . ARG A 1 76 ? 21.441 4.384 41.198 1.00 30.10 ? 76 ARG A O 1 ATOM 586 C CB . ARG A 1 76 ? 18.620 4.074 42.696 1.00 28.66 ? 76 ARG A CB 1 ATOM 587 C CG . ARG A 1 76 ? 19.052 5.526 42.782 1.00 28.40 ? 76 ARG A CG 1 ATOM 588 C CD . ARG A 1 76 ? 18.513 6.380 41.634 1.00 28.70 ? 76 ARG A CD 1 ATOM 589 N NE . ARG A 1 76 ? 18.885 7.786 41.799 1.00 26.51 ? 76 ARG A NE 1 ATOM 590 C CZ . ARG A 1 76 ? 18.748 8.722 40.870 1.00 25.05 ? 76 ARG A CZ 1 ATOM 591 N NH1 . ARG A 1 76 ? 18.254 8.417 39.679 1.00 24.73 ? 76 ARG A NH1 1 ATOM 592 N NH2 . ARG A 1 76 ? 19.115 9.969 41.138 1.00 24.92 ? 76 ARG A NH2 1 ATOM 593 N N . GLU A 1 77 ? 21.655 2.576 42.532 1.00 30.65 ? 77 GLU A N 1 ATOM 594 C CA . GLU A 1 77 ? 23.115 2.717 42.570 1.00 31.46 ? 77 GLU A CA 1 ATOM 595 C C . GLU A 1 77 ? 23.766 2.236 41.272 1.00 31.44 ? 77 GLU A C 1 ATOM 596 O O . GLU A 1 77 ? 24.717 2.852 40.796 1.00 32.07 ? 77 GLU A O 1 ATOM 597 C CB . GLU A 1 77 ? 23.759 2.040 43.783 1.00 31.63 ? 77 GLU A CB 1 ATOM 598 C CG . GLU A 1 77 ? 25.219 2.479 43.958 1.00 34.40 ? 77 GLU A CG 1 ATOM 599 C CD . GLU A 1 77 ? 25.941 1.857 45.154 1.00 38.12 ? 77 GLU A CD 1 ATOM 600 O OE1 . GLU A 1 77 ? 25.268 1.332 46.073 1.00 39.43 ? 77 GLU A OE1 1 ATOM 601 O OE2 . GLU A 1 77 ? 27.201 1.908 45.171 1.00 39.00 ? 77 GLU A OE2 1 ATOM 602 N N . VAL A 1 78 ? 23.263 1.143 40.698 1.00 31.25 ? 78 VAL A N 1 ATOM 603 C CA . VAL A 1 78 ? 23.689 0.732 39.357 1.00 30.82 ? 78 VAL A CA 1 ATOM 604 C C . VAL A 1 78 ? 23.396 1.886 38.403 1.00 30.50 ? 78 VAL A C 1 ATOM 605 O O . VAL A 1 78 ? 24.201 2.193 37.527 1.00 30.79 ? 78 VAL A O 1 ATOM 606 C CB . VAL A 1 78 ? 23.016 -0.612 38.867 1.00 31.11 ? 78 VAL A CB 1 ATOM 607 C CG1 . VAL A 1 78 ? 23.283 -0.860 37.375 1.00 30.09 ? 78 VAL A CG1 1 ATOM 608 C CG2 . VAL A 1 78 ? 23.493 -1.801 39.692 1.00 29.65 ? 78 VAL A CG2 1 ATOM 609 N N . SER A 1 79 ? 22.268 2.557 38.612 1.00 29.93 ? 79 SER A N 1 ATOM 610 C CA . SER A 1 79 ? 21.921 3.723 37.792 1.00 29.62 ? 79 SER A CA 1 ATOM 611 C C . SER A 1 79 ? 22.947 4.860 37.893 1.00 30.05 ? 79 SER A C 1 ATOM 612 O O . SER A 1 79 ? 23.585 5.206 36.897 1.00 30.78 ? 79 SER A O 1 ATOM 613 C CB . SER A 1 79 ? 20.518 4.222 38.100 1.00 28.92 ? 79 SER A CB 1 ATOM 614 O OG . SER A 1 79 ? 20.110 5.114 37.091 1.00 26.55 ? 79 SER A OG 1 ATOM 615 N N . ASN A 1 80 ? 23.107 5.430 39.084 1.00 30.05 ? 80 ASN A N 1 ATOM 616 C CA . ASN A 1 80 ? 24.146 6.437 39.350 1.00 30.05 ? 80 ASN A CA 1 ATOM 617 C C . ASN A 1 80 ? 25.558 6.109 38.847 1.00 30.13 ? 80 ASN A C 1 ATOM 618 O O . ASN A 1 80 ? 26.260 6.986 38.369 1.00 30.44 ? 80 ASN A O 1 ATOM 619 C CB . ASN A 1 80 ? 24.217 6.719 40.854 1.00 29.95 ? 80 ASN A CB 1 ATOM 620 C CG . ASN A 1 80 ? 22.909 7.222 41.411 1.00 30.17 ? 80 ASN A CG 1 ATOM 621 O OD1 . ASN A 1 80 ? 21.999 7.547 40.653 1.00 32.26 ? 80 ASN A OD1 1 ATOM 622 N ND2 . ASN A 1 80 ? 22.800 7.288 42.736 1.00 28.29 ? 80 ASN A ND2 1 ATOM 623 N N . LYS A 1 81 ? 25.978 4.855 38.964 1.00 30.54 ? 81 LYS A N 1 ATOM 624 C CA . LYS A 1 81 ? 27.379 4.492 38.715 1.00 31.04 ? 81 LYS A CA 1 ATOM 625 C C . LYS A 1 81 ? 27.697 4.194 37.253 1.00 30.76 ? 81 LYS A C 1 ATOM 626 O O . LYS A 1 81 ? 28.812 4.448 36.795 1.00 30.94 ? 81 LYS A O 1 ATOM 627 C CB . LYS A 1 81 ? 27.798 3.283 39.573 1.00 31.56 ? 81 LYS A CB 1 ATOM 628 C CG . LYS A 1 81 ? 28.643 3.607 40.790 1.00 33.48 ? 81 LYS A CG 1 ATOM 629 C CD . LYS A 1 81 ? 27.815 3.837 42.039 1.00 35.98 ? 81 LYS A CD 1 ATOM 630 C CE . LYS A 1 81 ? 28.687 4.361 43.205 1.00 37.89 ? 81 LYS A CE 1 ATOM 631 N NZ . LYS A 1 81 ? 29.273 3.255 44.046 1.00 38.40 ? 81 LYS A NZ 1 ATOM 632 N N . ILE A 1 82 ? 26.723 3.645 36.534 1.00 30.40 ? 82 ILE A N 1 ATOM 633 C CA . ILE A 1 82 ? 26.958 3.112 35.196 1.00 30.01 ? 82 ILE A CA 1 ATOM 634 C C . ILE A 1 82 ? 26.189 3.873 34.117 1.00 29.36 ? 82 ILE A C 1 ATOM 635 O O . ILE A 1 82 ? 26.741 4.166 33.043 1.00 29.03 ? 82 ILE A O 1 ATOM 636 C CB . ILE A 1 82 ? 26.523 1.612 35.108 1.00 30.53 ? 82 ILE A CB 1 ATOM 637 C CG1 . ILE A 1 82 ? 26.974 0.809 36.348 1.00 31.57 ? 82 ILE A CG1 1 ATOM 638 C CG2 . ILE A 1 82 ? 26.938 0.960 33.748 1.00 30.34 ? 82 ILE A CG2 1 ATOM 639 C CD1 . ILE A 1 82 ? 28.442 0.408 36.354 1.00 33.69 ? 82 ILE A CD1 1 ATOM 640 N N . VAL A 1 83 ? 24.919 4.172 34.410 1.00 28.19 ? 83 VAL A N 1 ATOM 641 C CA . VAL A 1 83 ? 23.947 4.626 33.401 1.00 27.43 ? 83 VAL A CA 1 ATOM 642 C C . VAL A 1 83 ? 23.955 6.128 33.134 1.00 26.93 ? 83 VAL A C 1 ATOM 643 O O . VAL A 1 83 ? 23.652 6.563 32.029 1.00 27.16 ? 83 VAL A O 1 ATOM 644 C CB . VAL A 1 83 ? 22.492 4.198 33.776 1.00 27.28 ? 83 VAL A CB 1 ATOM 645 C CG1 . VAL A 1 83 ? 21.555 4.446 32.617 1.00 27.15 ? 83 VAL A CG1 1 ATOM 646 C CG2 . VAL A 1 83 ? 22.438 2.723 34.174 1.00 26.73 ? 83 VAL A CG2 1 ATOM 647 N N . GLY A 1 84 ? 24.298 6.914 34.150 1.00 26.63 ? 84 GLY A N 1 ATOM 648 C CA . GLY A 1 84 ? 24.205 8.372 34.084 1.00 25.65 ? 84 GLY A CA 1 ATOM 649 C C . GLY A 1 84 ? 25.395 9.023 33.421 1.00 25.33 ? 84 GLY A C 1 ATOM 650 O O . GLY A 1 84 ? 26.473 8.425 33.353 1.00 25.23 ? 84 GLY A O 1 ATOM 651 N N . TYR A 1 85 ? 25.172 10.240 32.919 1.00 24.88 ? 85 TYR A N 1 ATOM 652 C CA . TYR A 1 85 ? 26.208 11.118 32.361 1.00 25.09 ? 85 TYR A CA 1 ATOM 653 C C . TYR A 1 85 ? 25.652 12.549 32.275 1.00 25.64 ? 85 TYR A C 1 ATOM 654 O O . TYR A 1 85 ? 24.435 12.752 32.319 1.00 25.13 ? 85 TYR A O 1 ATOM 655 C CB . TYR A 1 85 ? 26.647 10.642 30.975 1.00 24.60 ? 85 TYR A CB 1 ATOM 656 C CG . TYR A 1 85 ? 25.567 10.770 29.922 1.00 24.45 ? 85 TYR A CG 1 ATOM 657 C CD1 . TYR A 1 85 ? 25.485 11.918 29.115 1.00 24.17 ? 85 TYR A CD1 1 ATOM 658 C CD2 . TYR A 1 85 ? 24.615 9.751 29.733 1.00 23.17 ? 85 TYR A CD2 1 ATOM 659 C CE1 . TYR A 1 85 ? 24.500 12.043 28.146 1.00 24.11 ? 85 TYR A CE1 1 ATOM 660 C CE2 . TYR A 1 85 ? 23.618 9.866 28.750 1.00 22.29 ? 85 TYR A CE2 1 ATOM 661 C CZ . TYR A 1 85 ? 23.572 11.010 27.966 1.00 23.44 ? 85 TYR A CZ 1 ATOM 662 O OH . TYR A 1 85 ? 22.604 11.146 27.003 1.00 23.29 ? 85 TYR A OH 1 ATOM 663 N N . LEU A 1 86 ? 26.539 13.526 32.104 1.00 26.76 ? 86 LEU A N 1 ATOM 664 C CA . LEU A 1 86 ? 26.154 14.939 32.153 1.00 28.13 ? 86 LEU A CA 1 ATOM 665 C C . LEU A 1 86 ? 26.240 15.673 30.819 1.00 28.92 ? 86 LEU A C 1 ATOM 666 O O . LEU A 1 86 ? 25.536 16.661 30.627 1.00 29.45 ? 86 LEU A O 1 ATOM 667 C CB . LEU A 1 86 ? 26.984 15.702 33.202 1.00 27.49 ? 86 LEU A CB 1 ATOM 668 C CG . LEU A 1 86 ? 26.984 15.167 34.640 1.00 28.97 ? 86 LEU A CG 1 ATOM 669 C CD1 . LEU A 1 86 ? 28.124 15.768 35.468 1.00 29.97 ? 86 LEU A CD1 1 ATOM 670 C CD2 . LEU A 1 86 ? 25.641 15.341 35.366 1.00 29.75 ? 86 LEU A CD2 1 ATOM 671 N N . ASP A 1 87 ? 27.101 15.215 29.914 1.00 30.05 ? 87 ASP A N 1 ATOM 672 C CA . ASP A 1 87 ? 27.416 15.974 28.691 1.00 31.23 ? 87 ASP A CA 1 ATOM 673 C C . ASP A 1 87 ? 26.631 15.431 27.486 1.00 31.57 ? 87 ASP A C 1 ATOM 674 O O . ASP A 1 87 ? 26.930 14.349 26.984 1.00 31.87 ? 87 ASP A O 1 ATOM 675 C CB . ASP A 1 87 ? 28.928 15.900 28.434 1.00 31.59 ? 87 ASP A CB 1 ATOM 676 C CG . ASP A 1 87 ? 29.423 16.897 27.378 1.00 33.31 ? 87 ASP A CG 1 ATOM 677 O OD1 . ASP A 1 87 ? 28.634 17.416 26.551 1.00 34.75 ? 87 ASP A OD1 1 ATOM 678 O OD2 . ASP A 1 87 ? 30.647 17.143 27.370 1.00 36.14 ? 87 ASP A OD2 1 ATOM 679 N N . GLU A 1 88 ? 25.631 16.180 27.029 1.00 32.04 ? 88 GLU A N 1 ATOM 680 C CA . GLU A 1 88 ? 24.801 15.747 25.896 1.00 32.59 ? 88 GLU A CA 1 ATOM 681 C C . GLU A 1 88 ? 25.493 15.933 24.539 1.00 32.93 ? 88 GLU A C 1 ATOM 682 O O . GLU A 1 88 ? 25.050 15.376 23.540 1.00 33.47 ? 88 GLU A O 1 ATOM 683 C CB . GLU A 1 88 ? 23.424 16.444 25.880 1.00 32.48 ? 88 GLU A CB 1 ATOM 684 C CG . GLU A 1 88 ? 22.455 16.056 27.006 1.00 33.12 ? 88 GLU A CG 1 ATOM 685 C CD . GLU A 1 88 ? 22.099 14.558 27.052 1.00 35.17 ? 88 GLU A CD 1 ATOM 686 O OE1 . GLU A 1 88 ? 22.424 13.816 26.094 1.00 35.88 ? 88 GLU A OE1 1 ATOM 687 O OE2 . GLU A 1 88 ? 21.492 14.118 28.058 1.00 34.68 ? 88 GLU A OE2 1 ATOM 688 N N . ASP A 1 89 ? 26.573 16.711 24.507 1.00 33.28 ? 89 ASP A N 1 ATOM 689 C CA . ASP A 1 89 ? 27.312 16.958 23.281 1.00 33.55 ? 89 ASP A CA 1 ATOM 690 C C . ASP A 1 89 ? 27.974 15.675 22.805 1.00 32.98 ? 89 ASP A C 1 ATOM 691 O O . ASP A 1 89 ? 28.566 14.944 23.593 1.00 33.06 ? 89 ASP A O 1 ATOM 692 C CB . ASP A 1 89 ? 28.354 18.070 23.495 1.00 34.28 ? 89 ASP A CB 1 ATOM 693 C CG . ASP A 1 89 ? 29.330 18.213 22.316 1.00 36.82 ? 89 ASP A CG 1 ATOM 694 O OD1 . ASP A 1 89 ? 28.874 18.264 21.146 1.00 39.88 ? 89 ASP A OD1 1 ATOM 695 O OD2 . ASP A 1 89 ? 30.561 18.280 22.557 1.00 40.02 ? 89 ASP A OD2 1 ATOM 696 N N . GLY A 1 90 ? 27.844 15.395 21.512 1.00 32.46 ? 90 GLY A N 1 ATOM 697 C CA . GLY A 1 90 ? 28.549 14.277 20.886 1.00 31.45 ? 90 GLY A CA 1 ATOM 698 C C . GLY A 1 90 ? 27.782 12.972 20.884 1.00 31.00 ? 90 GLY A C 1 ATOM 699 O O . GLY A 1 90 ? 28.283 11.953 20.389 1.00 30.97 ? 90 GLY A O 1 ATOM 700 N N . VAL A 1 91 ? 26.556 13.005 21.404 1.00 30.14 ? 91 VAL A N 1 ATOM 701 C CA . VAL A 1 91 ? 25.814 11.773 21.680 1.00 29.79 ? 91 VAL A CA 1 ATOM 702 C C . VAL A 1 91 ? 24.860 11.290 20.551 1.00 29.45 ? 91 VAL A C 1 ATOM 703 O O . VAL A 1 91 ? 24.341 10.165 20.616 1.00 28.91 ? 91 VAL A O 1 ATOM 704 C CB . VAL A 1 91 ? 25.070 11.869 23.061 1.00 29.90 ? 91 VAL A CB 1 ATOM 705 C CG1 . VAL A 1 91 ? 23.601 12.279 22.892 1.00 29.17 ? 91 VAL A CG1 1 ATOM 706 C CG2 . VAL A 1 91 ? 25.175 10.554 23.819 1.00 30.11 ? 91 VAL A CG2 1 ATOM 707 N N . LEU A 1 92 ? 24.640 12.127 19.532 1.00 28.95 ? 92 LEU A N 1 ATOM 708 C CA . LEU A 1 92 ? 23.652 11.810 18.498 1.00 29.01 ? 92 LEU A CA 1 ATOM 709 C C . LEU A 1 92 ? 24.119 10.713 17.544 1.00 29.11 ? 92 LEU A C 1 ATOM 710 O O . LEU A 1 92 ? 25.315 10.558 17.268 1.00 29.07 ? 92 LEU A O 1 ATOM 711 C CB . LEU A 1 92 ? 23.179 13.061 17.739 1.00 28.77 ? 92 LEU A CB 1 ATOM 712 C CG . LEU A 1 92 ? 22.588 14.202 18.580 1.00 29.19 ? 92 LEU A CG 1 ATOM 713 C CD1 . LEU A 1 92 ? 22.092 15.331 17.695 1.00 29.37 ? 92 LEU A CD1 1 ATOM 714 C CD2 . LEU A 1 92 ? 21.471 13.734 19.524 1.00 30.31 ? 92 LEU A CD2 1 ATOM 715 N N . ASP A 1 93 ? 23.163 9.927 17.081 1.00 29.44 ? 93 ASP A N 1 ATOM 716 C CA . ASP A 1 93 ? 23.449 8.847 16.164 1.00 30.39 ? 93 ASP A CA 1 ATOM 717 C C . ASP A 1 93 ? 23.537 9.451 14.768 1.00 30.99 ? 93 ASP A C 1 ATOM 718 O O . ASP A 1 93 ? 22.539 9.869 14.187 1.00 30.84 ? 93 ASP A O 1 ATOM 719 C CB . ASP A 1 93 ? 22.364 7.772 16.240 1.00 29.93 ? 93 ASP A CB 1 ATOM 720 C CG . ASP A 1 93 ? 22.724 6.523 15.476 1.00 30.83 ? 93 ASP A CG 1 ATOM 721 O OD1 . ASP A 1 93 ? 23.502 6.614 14.498 1.00 31.58 ? 93 ASP A OD1 1 ATOM 722 O OD2 . ASP A 1 93 ? 22.213 5.438 15.844 1.00 31.30 ? 93 ASP A OD2 1 ATOM 723 N N . GLN A 1 94 ? 24.760 9.493 14.260 1.00 31.94 ? 94 GLN A N 1 ATOM 724 C CA . GLN A 1 94 ? 25.094 10.077 12.972 1.00 33.14 ? 94 GLN A CA 1 ATOM 725 C C . GLN A 1 94 ? 24.367 9.464 11.759 1.00 33.64 ? 94 GLN A C 1 ATOM 726 O O . GLN A 1 94 ? 24.321 10.087 10.704 1.00 33.80 ? 94 GLN A O 1 ATOM 727 C CB . GLN A 1 94 ? 26.617 10.011 12.798 1.00 33.25 ? 94 GLN A CB 1 ATOM 728 C CG . GLN A 1 94 ? 27.288 11.307 12.376 1.00 34.88 ? 94 GLN A CG 1 ATOM 729 C CD . GLN A 1 94 ? 26.809 12.528 13.155 1.00 37.09 ? 94 GLN A CD 1 ATOM 730 O OE1 . GLN A 1 94 ? 26.363 12.425 14.299 1.00 37.25 ? 94 GLN A OE1 1 ATOM 731 N NE2 . GLN A 1 94 ? 26.905 13.699 12.526 1.00 39.15 ? 94 GLN A NE2 1 ATOM 732 N N . ASN A 1 95 ? 23.798 8.263 11.903 1.00 34.42 ? 95 ASN A N 1 ATOM 733 C CA . ASN A 1 95 ? 23.092 7.612 10.783 1.00 35.32 ? 95 ASN A CA 1 ATOM 734 C C . ASN A 1 95 ? 21.724 6.988 11.147 1.00 34.24 ? 95 ASN A C 1 ATOM 735 O O . ASN A 1 95 ? 21.288 6.000 10.536 1.00 34.41 ? 95 ASN A O 1 ATOM 736 C CB . ASN A 1 95 ? 24.015 6.613 10.037 1.00 36.34 ? 95 ASN A CB 1 ATOM 737 C CG . ASN A 1 95 ? 23.570 6.356 8.579 1.00 41.56 ? 95 ASN A CG 1 ATOM 738 O OD1 . ASN A 1 95 ? 22.903 7.197 7.961 1.00 43.54 ? 95 ASN A OD1 1 ATOM 739 N ND2 . ASN A 1 95 ? 23.939 5.174 8.039 1.00 49.63 ? 95 ASN A ND2 1 ATOM 740 N N . ARG A 1 96 ? 21.053 7.564 12.143 1.00 32.93 ? 96 ARG A N 1 ATOM 741 C CA . ARG A 1 96 ? 19.673 7.200 12.464 1.00 31.64 ? 96 ARG A CA 1 ATOM 742 C C . ARG A 1 96 ? 18.823 8.432 12.808 1.00 30.76 ? 96 ARG A C 1 ATOM 743 O O . ARG A 1 96 ? 19.193 9.231 13.669 1.00 31.43 ? 96 ARG A O 1 ATOM 744 C CB . ARG A 1 96 ? 19.630 6.211 13.633 1.00 31.78 ? 96 ARG A CB 1 ATOM 745 C CG . ARG A 1 96 ? 20.345 4.894 13.404 1.00 32.33 ? 96 ARG A CG 1 ATOM 746 C CD . ARG A 1 96 ? 19.569 3.948 12.484 1.00 33.30 ? 96 ARG A CD 1 ATOM 747 N NE . ARG A 1 96 ? 20.223 2.642 12.395 1.00 33.89 ? 96 ARG A NE 1 ATOM 748 C CZ . ARG A 1 96 ? 21.280 2.371 11.628 1.00 34.26 ? 96 ARG A CZ 1 ATOM 749 N NH1 . ARG A 1 96 ? 21.828 3.304 10.853 1.00 34.66 ? 96 ARG A NH1 1 ATOM 750 N NH2 . ARG A 1 96 ? 21.797 1.154 11.640 1.00 33.86 ? 96 ARG A NH2 1 ATOM 751 N N . SER A 1 97 ? 17.680 8.573 12.149 1.00 29.18 ? 97 SER A N 1 ATOM 752 C CA . SER A 1 97 ? 16.739 9.657 12.421 1.00 27.82 ? 97 SER A CA 1 ATOM 753 C C . SER A 1 97 ? 16.024 9.432 13.747 1.00 27.34 ? 97 SER A C 1 ATOM 754 O O . SER A 1 97 ? 16.004 8.320 14.258 1.00 27.37 ? 97 SER A O 1 ATOM 755 C CB . SER A 1 97 ? 15.695 9.734 11.307 1.00 27.40 ? 97 SER A CB 1 ATOM 756 O OG . SER A 1 97 ? 14.960 8.519 11.231 1.00 26.59 ? 97 SER A OG 1 ATOM 757 N N . LEU A 1 98 ? 15.412 10.480 14.291 1.00 26.89 ? 98 LEU A N 1 ATOM 758 C CA . LEU A 1 98 ? 14.650 10.352 15.533 1.00 26.38 ? 98 LEU A CA 1 ATOM 759 C C . LEU A 1 98 ? 13.491 9.349 15.405 1.00 26.55 ? 98 LEU A C 1 ATOM 760 O O . LEU A 1 98 ? 13.064 8.759 16.397 1.00 26.32 ? 98 LEU A O 1 ATOM 761 C CB . LEU A 1 98 ? 14.169 11.720 16.041 1.00 25.76 ? 98 LEU A CB 1 ATOM 762 C CG . LEU A 1 98 ? 13.494 11.715 17.426 1.00 25.03 ? 98 LEU A CG 1 ATOM 763 C CD1 . LEU A 1 98 ? 14.393 11.153 18.522 1.00 22.88 ? 98 LEU A CD1 1 ATOM 764 C CD2 . LEU A 1 98 ? 13.031 13.074 17.787 1.00 23.83 ? 98 LEU A CD2 1 ATOM 765 N N . LEU A 1 99 ? 13.031 9.122 14.172 1.00 26.77 ? 99 LEU A N 1 ATOM 766 C CA . LEU A 1 99 ? 11.976 8.148 13.890 1.00 26.56 ? 99 LEU A CA 1 ATOM 767 C C . LEU A 1 99 ? 12.424 6.698 14.115 1.00 26.40 ? 99 LEU A C 1 ATOM 768 O O . LEU A 1 99 ? 11.588 5.820 14.367 1.00 26.45 ? 99 LEU A O 1 ATOM 769 C CB . LEU A 1 99 ? 11.460 8.335 12.461 1.00 26.39 ? 99 LEU A CB 1 ATOM 770 C CG . LEU A 1 99 ? 10.469 7.316 11.897 1.00 27.48 ? 99 LEU A CG 1 ATOM 771 C CD1 . LEU A 1 99 ? 9.110 7.417 12.589 1.00 27.63 ? 99 LEU A CD1 1 ATOM 772 C CD2 . LEU A 1 99 ? 10.328 7.562 10.419 1.00 30.10 ? 99 LEU A CD2 1 ATOM 773 N N . PHE A 1 100 ? 13.730 6.446 14.006 1.00 26.18 ? 100 PHE A N 1 ATOM 774 C CA . PHE A 1 100 ? 14.296 5.134 14.323 1.00 26.03 ? 100 PHE A CA 1 ATOM 775 C C . PHE A 1 100 ? 13.892 4.738 15.751 1.00 26.10 ? 100 PHE A C 1 ATOM 776 O O . PHE A 1 100 ? 13.231 3.716 15.960 1.00 26.10 ? 100 PHE A O 1 ATOM 777 C CB . PHE A 1 100 ? 15.811 5.148 14.133 1.00 25.96 ? 100 PHE A CB 1 ATOM 778 C CG . PHE A 1 100 ? 16.506 3.855 14.529 1.00 27.90 ? 100 PHE A CG 1 ATOM 779 C CD1 . PHE A 1 100 ? 16.356 2.695 13.761 1.00 29.21 ? 100 PHE A CD1 1 ATOM 780 C CD2 . PHE A 1 100 ? 17.350 3.814 15.651 1.00 27.38 ? 100 PHE A CD2 1 ATOM 781 C CE1 . PHE A 1 100 ? 17.018 1.510 14.118 1.00 29.48 ? 100 PHE A CE1 1 ATOM 782 C CE2 . PHE A 1 100 ? 18.010 2.646 16.016 1.00 27.79 ? 100 PHE A CE2 1 ATOM 783 C CZ . PHE A 1 100 ? 17.841 1.489 15.257 1.00 30.15 ? 100 PHE A CZ 1 ATOM 784 N N . MET A 1 101 ? 14.241 5.576 16.726 1.00 26.27 ? 101 MET A N 1 ATOM 785 C CA . MET A 1 101 ? 13.794 5.371 18.090 1.00 25.99 ? 101 MET A CA 1 ATOM 786 C C . MET A 1 101 ? 12.275 5.248 18.148 1.00 25.65 ? 101 MET A C 1 ATOM 787 O O . MET A 1 101 ? 11.747 4.343 18.773 1.00 25.60 ? 101 MET A O 1 ATOM 788 C CB . MET A 1 101 ? 14.206 6.528 18.981 1.00 26.15 ? 101 MET A CB 1 ATOM 789 C CG . MET A 1 101 ? 13.637 6.366 20.373 1.00 28.80 ? 101 MET A CG 1 ATOM 790 S SD . MET A 1 101 ? 12.605 7.739 20.883 1.00 35.80 ? 101 MET A SD 1 ATOM 791 C CE . MET A 1 101 ? 10.927 7.170 20.546 1.00 35.87 ? 101 MET A CE 1 ATOM 792 N N . GLN A 1 102 ? 11.573 6.171 17.502 1.00 25.45 ? 102 GLN A N 1 ATOM 793 C CA . GLN A 1 102 ? 10.134 6.259 17.682 1.00 25.11 ? 102 GLN A CA 1 ATOM 794 C C . GLN A 1 102 ? 9.390 5.046 17.160 1.00 24.53 ? 102 GLN A C 1 ATOM 795 O O . GLN A 1 102 ? 8.381 4.643 17.743 1.00 24.72 ? 102 GLN A O 1 ATOM 796 C CB . GLN A 1 102 ? 9.573 7.552 17.080 1.00 25.96 ? 102 GLN A CB 1 ATOM 797 C CG . GLN A 1 102 ? 8.147 7.836 17.494 1.00 26.82 ? 102 GLN A CG 1 ATOM 798 C CD . GLN A 1 102 ? 7.993 7.780 18.996 1.00 28.59 ? 102 GLN A CD 1 ATOM 799 O OE1 . GLN A 1 102 ? 8.501 8.646 19.717 1.00 29.04 ? 102 GLN A OE1 1 ATOM 800 N NE2 . GLN A 1 102 ? 7.304 6.751 19.481 1.00 28.16 ? 102 GLN A NE2 1 ATOM 801 N N . TRP A 1 103 ? 9.892 4.451 16.080 1.00 23.59 ? 103 TRP A N 1 ATOM 802 C CA . TRP A 1 103 ? 9.243 3.265 15.540 1.00 22.47 ? 103 TRP A CA 1 ATOM 803 C C . TRP A 1 103 ? 9.411 2.058 16.462 1.00 21.82 ? 103 TRP A C 1 ATOM 804 O O . TRP A 1 103 ? 8.474 1.282 16.650 1.00 21.75 ? 103 TRP A O 1 ATOM 805 C CB . TRP A 1 103 ? 9.693 2.952 14.111 1.00 22.09 ? 103 TRP A CB 1 ATOM 806 C CG . TRP A 1 103 ? 8.845 1.879 13.521 1.00 22.47 ? 103 TRP A CG 1 ATOM 807 C CD1 . TRP A 1 103 ? 9.190 0.579 13.342 1.00 23.51 ? 103 TRP A CD1 1 ATOM 808 C CD2 . TRP A 1 103 ? 7.480 1.995 13.098 1.00 23.45 ? 103 TRP A CD2 1 ATOM 809 N NE1 . TRP A 1 103 ? 8.141 -0.119 12.801 1.00 24.13 ? 103 TRP A NE1 1 ATOM 810 C CE2 . TRP A 1 103 ? 7.074 0.725 12.654 1.00 23.81 ? 103 TRP A CE2 1 ATOM 811 C CE3 . TRP A 1 103 ? 6.564 3.056 13.044 1.00 24.46 ? 103 TRP A CE3 1 ATOM 812 C CZ2 . TRP A 1 103 ? 5.790 0.478 12.152 1.00 25.16 ? 103 TRP A CZ2 1 ATOM 813 C CZ3 . TRP A 1 103 ? 5.291 2.812 12.546 1.00 25.01 ? 103 TRP A CZ3 1 ATOM 814 C CH2 . TRP A 1 103 ? 4.917 1.532 12.099 1.00 25.17 ? 103 TRP A CH2 1 ATOM 815 N N . GLY A 1 104 ? 10.602 1.902 17.031 1.00 21.36 ? 104 GLY A N 1 ATOM 816 C CA . GLY A 1 104 ? 10.850 0.860 18.024 1.00 20.79 ? 104 GLY A CA 1 ATOM 817 C C . GLY A 1 104 ? 9.802 0.805 19.126 1.00 20.63 ? 104 GLY A C 1 ATOM 818 O O . GLY A 1 104 ? 9.318 -0.273 19.484 1.00 19.77 ? 104 GLY A O 1 ATOM 819 N N . GLN A 1 105 ? 9.440 1.980 19.640 1.00 21.12 ? 105 GLN A N 1 ATOM 820 C CA . GLN A 1 105 ? 8.472 2.103 20.723 1.00 21.62 ? 105 GLN A CA 1 ATOM 821 C C . GLN A 1 105 ? 7.050 1.727 20.270 1.00 21.84 ? 105 GLN A C 1 ATOM 822 O O . GLN A 1 105 ? 6.272 1.185 21.056 1.00 21.11 ? 105 GLN A O 1 ATOM 823 C CB . GLN A 1 105 ? 8.517 3.520 21.334 1.00 21.58 ? 105 GLN A CB 1 ATOM 824 C CG . GLN A 1 105 ? 7.799 3.628 22.705 1.00 22.06 ? 105 GLN A CG 1 ATOM 825 C CD . GLN A 1 105 ? 7.738 5.042 23.253 1.00 22.05 ? 105 GLN A CD 1 ATOM 826 O OE1 . GLN A 1 105 ? 7.801 6.022 22.507 1.00 23.53 ? 105 GLN A OE1 1 ATOM 827 N NE2 . GLN A 1 105 ? 7.623 5.154 24.569 1.00 19.28 ? 105 GLN A NE2 1 ATOM 828 N N . ILE A 1 106 ? 6.727 1.997 19.005 1.00 22.56 ? 106 ILE A N 1 ATOM 829 C CA . ILE A 1 106 ? 5.438 1.594 18.435 1.00 23.47 ? 106 ILE A CA 1 ATOM 830 C C . ILE A 1 106 ? 5.332 0.080 18.340 1.00 23.80 ? 106 ILE A C 1 ATOM 831 O O . ILE A 1 106 ? 4.343 -0.515 18.781 1.00 23.98 ? 106 ILE A O 1 ATOM 832 C CB . ILE A 1 106 ? 5.166 2.257 17.052 1.00 23.65 ? 106 ILE A CB 1 ATOM 833 C CG1 . ILE A 1 106 ? 4.518 3.621 17.255 1.00 24.62 ? 106 ILE A CG1 1 ATOM 834 C CG2 . ILE A 1 106 ? 4.212 1.405 16.189 1.00 24.06 ? 106 ILE A CG2 1 ATOM 835 C CD1 . ILE A 1 106 ? 5.525 4.681 17.578 1.00 29.66 ? 106 ILE A CD1 1 ATOM 836 N N . VAL A 1 107 ? 6.364 -0.531 17.774 1.00 24.40 ? 107 VAL A N 1 ATOM 837 C CA . VAL A 1 107 ? 6.448 -1.978 17.663 1.00 24.95 ? 107 VAL A CA 1 ATOM 838 C C . VAL A 1 107 ? 6.402 -2.610 19.049 1.00 25.32 ? 107 VAL A C 1 ATOM 839 O O . VAL A 1 107 ? 5.588 -3.514 19.305 1.00 25.39 ? 107 VAL A O 1 ATOM 840 C CB . VAL A 1 107 ? 7.702 -2.412 16.880 1.00 24.65 ? 107 VAL A CB 1 ATOM 841 C CG1 . VAL A 1 107 ? 7.954 -3.895 17.029 1.00 24.98 ? 107 VAL A CG1 1 ATOM 842 C CG2 . VAL A 1 107 ? 7.526 -2.070 15.416 1.00 25.48 ? 107 VAL A CG2 1 ATOM 843 N N . ASP A 1 108 ? 7.244 -2.123 19.957 1.00 25.90 ? 108 ASP A N 1 ATOM 844 C CA . ASP A 1 108 ? 7.223 -2.652 21.313 1.00 26.30 ? 108 ASP A CA 1 ATOM 845 C C . ASP A 1 108 ? 5.829 -2.694 21.922 1.00 26.05 ? 108 ASP A C 1 ATOM 846 O O . ASP A 1 108 ? 5.458 -3.693 22.539 1.00 26.14 ? 108 ASP A O 1 ATOM 847 C CB . ASP A 1 108 ? 8.093 -1.866 22.267 1.00 26.92 ? 108 ASP A CB 1 ATOM 848 C CG . ASP A 1 108 ? 8.307 -2.397 23.646 1.00 28.25 ? 108 ASP A CG 1 ATOM 849 O OD1 . ASP A 1 108 ? 7.470 -2.230 24.550 1.00 28.74 ? 108 ASP A OD1 1 ATOM 850 O OD2 . ASP A 1 108 ? 9.309 -3.106 23.798 1.00 35.22 ? 108 ASP A OD2 1 ATOM 851 N N . HIS A 1 109 ? 5.086 -1.600 21.752 1.00 25.92 ? 109 HIS A N 1 ATOM 852 C CA . HIS A 1 109 ? 3.767 -1.430 22.353 1.00 26.19 ? 109 HIS A CA 1 ATOM 853 C C . HIS A 1 109 ? 2.683 -2.285 21.702 1.00 26.79 ? 109 HIS A C 1 ATOM 854 O O . HIS A 1 109 ? 1.653 -2.583 22.326 1.00 26.86 ? 109 HIS A O 1 ATOM 855 C CB . HIS A 1 109 ? 3.367 0.046 22.363 1.00 25.91 ? 109 HIS A CB 1 ATOM 856 C CG . HIS A 1 109 ? 4.091 0.864 23.387 1.00 25.71 ? 109 HIS A CG 1 ATOM 857 N ND1 . HIS A 1 109 ? 3.718 2.151 23.708 1.00 26.74 ? 109 HIS A ND1 1 ATOM 858 C CD2 . HIS A 1 109 ? 5.161 0.579 24.168 1.00 25.05 ? 109 HIS A CD2 1 ATOM 859 C CE1 . HIS A 1 109 ? 4.532 2.628 24.633 1.00 25.55 ? 109 HIS A CE1 1 ATOM 860 N NE2 . HIS A 1 109 ? 5.410 1.688 24.936 1.00 25.65 ? 109 HIS A NE2 1 ATOM 861 N N . ASP A 1 110 ? 2.928 -2.681 20.455 1.00 27.30 ? 110 ASP A N 1 ATOM 862 C CA . ASP A 1 110 ? 2.100 -3.660 19.759 1.00 27.58 ? 110 ASP A CA 1 ATOM 863 C C . ASP A 1 110 ? 2.312 -5.082 20.311 1.00 27.48 ? 110 ASP A C 1 ATOM 864 O O . ASP A 1 110 ? 1.421 -5.920 20.244 1.00 27.12 ? 110 ASP A O 1 ATOM 865 C CB . ASP A 1 110 ? 2.460 -3.631 18.275 1.00 28.02 ? 110 ASP A CB 1 ATOM 866 C CG . ASP A 1 110 ? 1.387 -4.235 17.385 1.00 29.91 ? 110 ASP A CG 1 ATOM 867 O OD1 . ASP A 1 110 ? 0.897 -5.352 17.668 1.00 30.29 ? 110 ASP A OD1 1 ATOM 868 O OD2 . ASP A 1 110 ? 1.056 -3.584 16.370 1.00 32.54 ? 110 ASP A OD2 1 ATOM 869 N N . LEU A 1 111 ? 3.490 -5.358 20.861 1.00 27.60 ? 111 LEU A N 1 ATOM 870 C CA . LEU A 1 111 ? 3.836 -6.742 21.198 1.00 27.50 ? 111 LEU A CA 1 ATOM 871 C C . LEU A 1 111 ? 3.671 -7.107 22.662 1.00 27.68 ? 111 LEU A C 1 ATOM 872 O O . LEU A 1 111 ? 3.266 -8.223 22.956 1.00 27.62 ? 111 LEU A O 1 ATOM 873 C CB . LEU A 1 111 ? 5.254 -7.078 20.724 1.00 27.31 ? 111 LEU A CB 1 ATOM 874 C CG . LEU A 1 111 ? 5.527 -6.858 19.231 1.00 27.04 ? 111 LEU A CG 1 ATOM 875 C CD1 . LEU A 1 111 ? 7.042 -6.929 18.943 1.00 26.71 ? 111 LEU A CD1 1 ATOM 876 C CD2 . LEU A 1 111 ? 4.716 -7.825 18.357 1.00 24.05 ? 111 LEU A CD2 1 ATOM 877 N N . ASP A 1 112 ? 3.991 -6.183 23.574 1.00 28.27 ? 112 ASP A N 1 ATOM 878 C CA . ASP A 1 112 ? 3.953 -6.490 25.021 1.00 28.80 ? 112 ASP A CA 1 ATOM 879 C C . ASP A 1 112 ? 3.538 -5.349 25.950 1.00 29.35 ? 112 ASP A C 1 ATOM 880 O O . ASP A 1 112 ? 3.832 -4.185 25.692 1.00 29.04 ? 112 ASP A O 1 ATOM 881 C CB . ASP A 1 112 ? 5.277 -7.125 25.506 1.00 28.49 ? 112 ASP A CB 1 ATOM 882 C CG . ASP A 1 112 ? 6.507 -6.387 24.997 1.00 28.21 ? 112 ASP A CG 1 ATOM 883 O OD1 . ASP A 1 112 ? 6.962 -6.696 23.882 1.00 28.39 ? 112 ASP A OD1 1 ATOM 884 O OD2 . ASP A 1 112 ? 7.020 -5.500 25.711 1.00 24.59 ? 112 ASP A OD2 1 ATOM 885 N N . PHE A 1 113 ? 2.831 -5.705 27.022 1.00 30.41 ? 113 PHE A N 1 ATOM 886 C CA . PHE A 1 113 ? 2.491 -4.785 28.104 1.00 31.53 ? 113 PHE A CA 1 ATOM 887 C C . PHE A 1 113 ? 2.278 -5.605 29.357 1.00 32.69 ? 113 PHE A C 1 ATOM 888 O O . PHE A 1 113 ? 1.346 -6.399 29.431 1.00 32.48 ? 113 PHE A O 1 ATOM 889 C CB . PHE A 1 113 ? 1.224 -3.978 27.782 1.00 31.66 ? 113 PHE A CB 1 ATOM 890 C CG . PHE A 1 113 ? 0.865 -2.921 28.828 1.00 31.46 ? 113 PHE A CG 1 ATOM 891 C CD1 . PHE A 1 113 ? 1.829 -2.377 29.670 1.00 30.25 ? 113 PHE A CD1 1 ATOM 892 C CD2 . PHE A 1 113 ? -0.444 -2.457 28.939 1.00 30.98 ? 113 PHE A CD2 1 ATOM 893 C CE1 . PHE A 1 113 ? 1.485 -1.415 30.615 1.00 31.15 ? 113 PHE A CE1 1 ATOM 894 C CE2 . PHE A 1 113 ? -0.789 -1.485 29.869 1.00 31.09 ? 113 PHE A CE2 1 ATOM 895 C CZ . PHE A 1 113 ? 0.171 -0.959 30.710 1.00 30.27 ? 113 PHE A CZ 1 ATOM 896 N N . ALA A 1 114 ? 3.157 -5.421 30.336 1.00 34.44 ? 114 ALA A N 1 ATOM 897 C CA . ALA A 1 114 ? 2.972 -6.034 31.641 1.00 36.17 ? 114 ALA A CA 1 ATOM 898 C C . ALA A 1 114 ? 2.565 -4.967 32.653 1.00 37.66 ? 114 ALA A C 1 ATOM 899 O O . ALA A 1 114 ? 3.430 -4.361 33.283 1.00 38.10 ? 114 ALA A O 1 ATOM 900 C CB . ALA A 1 114 ? 4.236 -6.756 32.086 1.00 35.80 ? 114 ALA A CB 1 ATOM 901 N N . PRO A 1 115 ? 1.246 -4.754 32.828 1.00 39.40 ? 115 PRO A N 1 ATOM 902 C CA . PRO A 1 115 ? 0.702 -3.691 33.676 1.00 41.11 ? 115 PRO A CA 1 ATOM 903 C C . PRO A 1 115 ? 0.997 -3.921 35.143 1.00 43.04 ? 115 PRO A C 1 ATOM 904 O O . PRO A 1 115 ? 1.217 -5.060 35.559 1.00 42.91 ? 115 PRO A O 1 ATOM 905 C CB . PRO A 1 115 ? -0.818 -3.811 33.473 1.00 40.91 ? 115 PRO A CB 1 ATOM 906 C CG . PRO A 1 115 ? -0.992 -4.643 32.251 1.00 40.46 ? 115 PRO A CG 1 ATOM 907 C CD . PRO A 1 115 ? 0.170 -5.575 32.235 1.00 39.64 ? 115 PRO A CD 1 ATOM 908 N N . GLU A 1 116 ? 0.967 -2.841 35.920 1.00 45.91 ? 116 GLU A N 1 ATOM 909 C CA . GLU A 1 116 ? 1.161 -2.911 37.362 1.00 48.93 ? 116 GLU A CA 1 ATOM 910 C C . GLU A 1 116 ? -0.037 -3.520 38.061 1.00 51.22 ? 116 GLU A C 1 ATOM 911 O O . GLU A 1 116 ? -1.143 -3.550 37.510 1.00 51.36 ? 116 GLU A O 1 ATOM 912 C CB . GLU A 1 116 ? 1.413 -1.526 37.930 1.00 48.84 ? 116 GLU A CB 1 ATOM 913 C CG . GLU A 1 116 ? 2.840 -1.028 37.747 1.00 49.53 ? 116 GLU A CG 1 ATOM 914 C CD . GLU A 1 116 ? 3.012 0.397 38.269 1.00 50.52 ? 116 GLU A CD 1 ATOM 915 O OE1 . GLU A 1 116 ? 1.998 1.026 38.679 1.00 50.18 ? 116 GLU A OE1 1 ATOM 916 O OE2 . GLU A 1 116 ? 4.168 0.888 38.272 1.00 50.80 ? 116 GLU A OE2 1 ATOM 917 N N . THR A 1 117 ? 0.203 -4.029 39.268 1.00 54.52 ? 117 THR A N 1 ATOM 918 C CA . THR A 1 117 ? -0.861 -4.490 40.157 1.00 57.78 ? 117 THR A CA 1 ATOM 919 C C . THR A 1 117 ? -1.593 -3.287 40.752 1.00 60.14 ? 117 THR A C 1 ATOM 920 O O . THR A 1 117 ? -0.975 -2.252 41.047 1.00 60.32 ? 117 THR A O 1 ATOM 921 C CB . THR A 1 117 ? -0.318 -5.340 41.322 1.00 57.69 ? 117 THR A CB 1 ATOM 922 O OG1 . THR A 1 117 ? 0.876 -4.733 41.845 1.00 58.28 ? 117 THR A OG1 1 ATOM 923 C CG2 . THR A 1 117 ? -0.029 -6.778 40.875 1.00 57.78 ? 117 THR A CG2 1 ATOM 924 N N . GLU A 1 118 ? -2.908 -3.434 40.930 1.00 63.20 ? 118 GLU A N 1 ATOM 925 C CA . GLU A 1 118 ? -3.728 -2.386 41.533 1.00 66.13 ? 118 GLU A CA 1 ATOM 926 C C . GLU A 1 118 ? -4.009 -2.666 43.018 1.00 67.60 ? 118 GLU A C 1 ATOM 927 O O . GLU A 1 118 ? -3.258 -2.213 43.891 1.00 67.91 ? 118 GLU A O 1 ATOM 928 C CB . GLU A 1 118 ? -5.028 -2.164 40.740 1.00 66.30 ? 118 GLU A CB 1 ATOM 929 C CG . GLU A 1 118 ? -5.614 -0.752 40.908 1.00 68.53 ? 118 GLU A CG 1 ATOM 930 C CD . GLU A 1 118 ? -7.075 -0.636 40.474 1.00 70.60 ? 118 GLU A CD 1 ATOM 931 O OE1 . GLU A 1 118 ? -7.495 0.481 40.085 1.00 70.97 ? 118 GLU A OE1 1 ATOM 932 O OE2 . GLU A 1 118 ? -7.806 -1.657 40.528 1.00 71.44 ? 118 GLU A OE2 1 ATOM 933 N N . LEU A 1 119 ? -5.069 -3.433 43.288 1.00 69.69 ? 119 LEU A N 1 ATOM 934 C CA . LEU A 1 119 ? -5.627 -3.605 44.646 1.00 71.61 ? 119 LEU A CA 1 ATOM 935 C C . LEU A 1 119 ? -5.889 -2.272 45.375 1.00 72.72 ? 119 LEU A C 1 ATOM 936 O O . LEU A 1 119 ? -5.673 -2.156 46.593 1.00 72.96 ? 119 LEU A O 1 ATOM 937 C CB . LEU A 1 119 ? -4.781 -4.568 45.502 1.00 71.77 ? 119 LEU A CB 1 ATOM 938 C CG . LEU A 1 119 ? -4.840 -6.074 45.179 1.00 72.79 ? 119 LEU A CG 1 ATOM 939 C CD1 . LEU A 1 119 ? -3.841 -6.436 44.038 1.00 73.29 ? 119 LEU A CD1 1 ATOM 940 C CD2 . LEU A 1 119 ? -4.595 -6.948 46.457 1.00 73.02 ? 119 LEU A CD2 1 ATOM 941 N N . GLY A 1 120 ? -6.369 -1.279 44.617 1.00 74.01 ? 120 GLY A N 1 ATOM 942 C CA . GLY A 1 120 ? -6.662 0.053 45.155 1.00 75.44 ? 120 GLY A CA 1 ATOM 943 C C . GLY A 1 120 ? -7.400 0.972 44.190 1.00 76.54 ? 120 GLY A C 1 ATOM 944 O O . GLY A 1 120 ? -6.775 1.743 43.444 1.00 76.58 ? 120 GLY A O 1 ATOM 945 N N . SER A 1 121 ? -8.746 0.928 44.264 1.00 77.64 ? 121 SER A N 1 ATOM 946 C CA . SER A 1 121 ? -9.624 1.878 43.560 1.00 78.59 ? 121 SER A CA 1 ATOM 947 C C . SER A 1 121 ? -9.758 3.018 44.573 1.00 79.21 ? 121 SER A C 1 ATOM 948 O O . SER A 1 121 ? -10.588 3.928 44.447 1.00 79.64 ? 121 SER A O 1 ATOM 949 C CB . SER A 1 121 ? -11.014 1.300 43.234 1.00 78.49 ? 121 SER A CB 1 ATOM 950 O OG . SER A 1 121 ? -10.907 0.088 42.519 1.00 78.74 ? 121 SER A OG 1 ATOM 951 N N . ASN A 1 122 ? -8.898 2.930 45.586 1.00 79.81 ? 122 ASN A N 1 ATOM 952 C CA . ASN A 1 122 ? -8.879 3.719 46.807 1.00 80.27 ? 122 ASN A CA 1 ATOM 953 C C . ASN A 1 122 ? -8.290 2.752 47.838 1.00 80.37 ? 122 ASN A C 1 ATOM 954 O O . ASN A 1 122 ? -8.828 1.649 48.049 1.00 80.52 ? 122 ASN A O 1 ATOM 955 C CB . ASN A 1 122 ? -10.273 4.188 47.235 1.00 80.45 ? 122 ASN A CB 1 ATOM 956 C CG . ASN A 1 122 ? -10.227 5.433 48.120 1.00 81.03 ? 122 ASN A CG 1 ATOM 957 O OD1 . ASN A 1 122 ? -9.304 6.254 48.013 1.00 82.30 ? 122 ASN A OD1 1 ATOM 958 N ND2 . ASN A 1 122 ? -11.238 5.586 48.989 1.00 81.18 ? 122 ASN A ND2 1 ATOM 959 N N . GLU A 1 123 ? -7.168 3.145 48.442 1.00 80.29 ? 123 GLU A N 1 ATOM 960 C CA . GLU A 1 123 ? -6.476 2.304 49.422 1.00 80.19 ? 123 GLU A CA 1 ATOM 961 C C . GLU A 1 123 ? -5.279 3.042 50.000 1.00 79.71 ? 123 GLU A C 1 ATOM 962 O O . GLU A 1 123 ? -4.662 3.876 49.325 1.00 79.70 ? 123 GLU A O 1 ATOM 963 C CB . GLU A 1 123 ? -6.017 0.975 48.782 1.00 80.49 ? 123 GLU A CB 1 ATOM 964 C CG . GLU A 1 123 ? -5.535 -0.106 49.772 1.00 81.43 ? 123 GLU A CG 1 ATOM 965 C CD . GLU A 1 123 ? -6.675 -0.832 50.505 1.00 82.58 ? 123 GLU A CD 1 ATOM 966 O OE1 . GLU A 1 123 ? -7.690 -0.193 50.881 1.00 82.68 ? 123 GLU A OE1 1 ATOM 967 O OE2 . GLU A 1 123 ? -6.546 -2.058 50.717 1.00 83.55 ? 123 GLU A OE2 1 ATOM 968 N N . HIS A 1 124 ? -4.954 2.723 51.250 1.00 79.07 ? 124 HIS A N 1 ATOM 969 C CA . HIS A 1 124 ? -3.748 3.243 51.887 1.00 78.43 ? 124 HIS A CA 1 ATOM 970 C C . HIS A 1 124 ? -2.466 2.555 51.389 1.00 77.67 ? 124 HIS A C 1 ATOM 971 O O . HIS A 1 124 ? -1.369 2.889 51.846 1.00 77.57 ? 124 HIS A O 1 ATOM 972 C CB . HIS A 1 124 ? -3.853 3.155 53.416 1.00 78.66 ? 124 HIS A CB 1 ATOM 973 C CG . HIS A 1 124 ? -4.551 4.327 54.039 1.00 79.49 ? 124 HIS A CG 1 ATOM 974 N ND1 . HIS A 1 124 ? -5.267 4.230 55.220 1.00 80.44 ? 124 HIS A ND1 1 ATOM 975 C CD2 . HIS A 1 124 ? -4.646 5.622 53.642 1.00 79.94 ? 124 HIS A CD2 1 ATOM 976 C CE1 . HIS A 1 124 ? -5.768 5.414 55.527 1.00 80.22 ? 124 HIS A CE1 1 ATOM 977 N NE2 . HIS A 1 124 ? -5.408 6.275 54.584 1.00 80.12 ? 124 HIS A NE2 1 ATOM 978 N N . SER A 1 125 ? -2.608 1.605 50.458 1.00 76.53 ? 125 SER A N 1 ATOM 979 C CA . SER A 1 125 ? -1.447 0.920 49.870 1.00 75.32 ? 125 SER A CA 1 ATOM 980 C C . SER A 1 125 ? -0.766 1.762 48.785 1.00 74.35 ? 125 SER A C 1 ATOM 981 O O . SER A 1 125 ? 0.470 1.817 48.719 1.00 74.20 ? 125 SER A O 1 ATOM 982 C CB . SER A 1 125 ? -1.822 -0.462 49.315 1.00 75.35 ? 125 SER A CB 1 ATOM 983 O OG . SER A 1 125 ? -0.651 -1.187 48.943 1.00 75.15 ? 125 SER A OG 1 ATOM 984 N N . LYS A 1 126 ? -1.563 2.415 47.938 1.00 72.96 ? 126 LYS A N 1 ATOM 985 C CA . LYS A 1 126 ? -1.003 3.314 46.931 1.00 71.86 ? 126 LYS A CA 1 ATOM 986 C C . LYS A 1 126 ? -0.528 4.636 47.564 1.00 70.75 ? 126 LYS A C 1 ATOM 987 O O . LYS A 1 126 ? -0.341 5.645 46.871 1.00 70.85 ? 126 LYS A O 1 ATOM 988 C CB . LYS A 1 126 ? -1.979 3.530 45.758 1.00 72.15 ? 126 LYS A CB 1 ATOM 989 C CG . LYS A 1 126 ? -3.332 4.156 46.114 1.00 72.79 ? 126 LYS A CG 1 ATOM 990 C CD . LYS A 1 126 ? -4.201 4.305 44.866 1.00 73.70 ? 126 LYS A CD 1 ATOM 991 C CE . LYS A 1 126 ? -5.603 4.817 45.210 1.00 73.97 ? 126 LYS A CE 1 ATOM 992 N NZ . LYS A 1 126 ? -6.515 4.814 44.016 1.00 73.76 ? 126 LYS A NZ 1 ATOM 993 N N . THR A 1 127 ? -0.322 4.606 48.883 1.00 69.07 ? 127 THR A N 1 ATOM 994 C CA . THR A 1 127 ? 0.163 5.758 49.641 1.00 67.26 ? 127 THR A CA 1 ATOM 995 C C . THR A 1 127 ? 1.074 5.336 50.803 1.00 65.83 ? 127 THR A C 1 ATOM 996 O O . THR A 1 127 ? 1.975 6.084 51.183 1.00 65.58 ? 127 THR A O 1 ATOM 997 C CB . THR A 1 127 ? -1.021 6.680 50.083 1.00 67.60 ? 127 THR A CB 1 ATOM 998 O OG1 . THR A 1 127 ? -1.567 7.328 48.922 1.00 67.75 ? 127 THR A OG1 1 ATOM 999 C CG2 . THR A 1 127 ? -0.587 7.755 51.089 1.00 67.36 ? 127 THR A CG2 1 ATOM 1000 N N . GLN A 1 128 ? 0.865 4.131 51.344 1.00 64.16 ? 128 GLN A N 1 ATOM 1001 C CA . GLN A 1 128 ? 1.816 3.552 52.314 1.00 62.46 ? 128 GLN A CA 1 ATOM 1002 C C . GLN A 1 128 ? 3.127 3.197 51.621 1.00 60.63 ? 128 GLN A C 1 ATOM 1003 O O . GLN A 1 128 ? 4.173 3.070 52.267 1.00 60.40 ? 128 GLN A O 1 ATOM 1004 C CB . GLN A 1 128 ? 1.241 2.305 52.991 1.00 62.95 ? 128 GLN A CB 1 ATOM 1005 C CG . GLN A 1 128 ? 1.987 1.872 54.262 1.00 64.85 ? 128 GLN A CG 1 ATOM 1006 C CD . GLN A 1 128 ? 1.717 0.417 54.655 1.00 67.65 ? 128 GLN A CD 1 ATOM 1007 O OE1 . GLN A 1 128 ? 1.786 -0.493 53.818 1.00 68.53 ? 128 GLN A OE1 1 ATOM 1008 N NE2 . GLN A 1 128 ? 1.418 0.193 55.938 1.00 67.93 ? 128 GLN A NE2 1 ATOM 1009 N N . CYS A 1 129 ? 3.050 3.035 50.300 1.00 58.38 ? 129 CYS A N 1 ATOM 1010 C CA . CYS A 1 129 ? 4.215 2.749 49.470 1.00 55.69 ? 129 CYS A CA 1 ATOM 1011 C C . CYS A 1 129 ? 5.015 4.009 49.141 1.00 55.52 ? 129 CYS A C 1 ATOM 1012 O O . CYS A 1 129 ? 6.240 4.024 49.312 1.00 55.21 ? 129 CYS A O 1 ATOM 1013 C CB . CYS A 1 129 ? 3.809 2.016 48.185 1.00 54.88 ? 129 CYS A CB 1 ATOM 1014 S SG . CYS A 1 129 ? 5.203 1.290 47.297 1.00 48.31 ? 129 CYS A SG 1 ATOM 1015 N N . GLU A 1 130 ? 4.329 5.055 48.675 1.00 55.07 ? 130 GLU A N 1 ATOM 1016 C CA . GLU A 1 130 ? 5.003 6.313 48.345 1.00 54.99 ? 130 GLU A CA 1 ATOM 1017 C C . GLU A 1 130 ? 5.427 7.095 49.587 1.00 54.42 ? 130 GLU A C 1 ATOM 1018 O O . GLU A 1 130 ? 6.509 7.683 49.601 1.00 54.11 ? 130 GLU A O 1 ATOM 1019 C CB . GLU A 1 130 ? 4.161 7.197 47.405 1.00 55.24 ? 130 GLU A CB 1 ATOM 1020 C CG . GLU A 1 130 ? 4.922 8.454 46.904 1.00 56.74 ? 130 GLU A CG 1 ATOM 1021 C CD . GLU A 1 130 ? 4.330 9.095 45.649 1.00 58.77 ? 130 GLU A CD 1 ATOM 1022 O OE1 . GLU A 1 130 ? 3.220 8.690 45.234 1.00 59.53 ? 130 GLU A OE1 1 ATOM 1023 O OE2 . GLU A 1 130 ? 4.981 10.014 45.079 1.00 59.09 ? 130 GLU A OE2 1 ATOM 1024 N N . GLU A 1 131 ? 4.587 7.089 50.621 1.00 54.09 ? 131 GLU A N 1 ATOM 1025 C CA . GLU A 1 131 ? 4.842 7.898 51.821 1.00 53.82 ? 131 GLU A CA 1 ATOM 1026 C C . GLU A 1 131 ? 5.943 7.388 52.764 1.00 53.22 ? 131 GLU A C 1 ATOM 1027 O O . GLU A 1 131 ? 6.731 8.181 53.294 1.00 53.05 ? 131 GLU A O 1 ATOM 1028 C CB . GLU A 1 131 ? 3.555 8.159 52.620 1.00 54.13 ? 131 GLU A CB 1 ATOM 1029 C CG . GLU A 1 131 ? 2.589 9.181 52.011 1.00 55.50 ? 131 GLU A CG 1 ATOM 1030 C CD . GLU A 1 131 ? 3.255 10.474 51.563 1.00 57.60 ? 131 GLU A CD 1 ATOM 1031 O OE1 . GLU A 1 131 ? 2.734 11.081 50.603 1.00 58.60 ? 131 GLU A OE1 1 ATOM 1032 O OE2 . GLU A 1 131 ? 4.289 10.880 52.152 1.00 58.80 ? 131 GLU A OE2 1 ATOM 1033 N N . TYR A 1 132 ? 6.003 6.080 52.987 1.00 52.21 ? 132 TYR A N 1 ATOM 1034 C CA . TYR A 1 132 ? 6.919 5.580 54.000 1.00 51.30 ? 132 TYR A CA 1 ATOM 1035 C C . TYR A 1 132 ? 7.904 4.523 53.498 1.00 50.03 ? 132 TYR A C 1 ATOM 1036 O O . TYR A 1 132 ? 8.765 4.059 54.257 1.00 49.88 ? 132 TYR A O 1 ATOM 1037 C CB . TYR A 1 132 ? 6.137 5.129 55.245 1.00 52.01 ? 132 TYR A CB 1 ATOM 1038 C CG . TYR A 1 132 ? 5.267 6.237 55.828 1.00 53.51 ? 132 TYR A CG 1 ATOM 1039 C CD1 . TYR A 1 132 ? 3.879 6.243 55.632 1.00 55.00 ? 132 TYR A CD1 1 ATOM 1040 C CD2 . TYR A 1 132 ? 5.840 7.297 56.549 1.00 54.98 ? 132 TYR A CD2 1 ATOM 1041 C CE1 . TYR A 1 132 ? 3.070 7.275 56.160 1.00 55.78 ? 132 TYR A CE1 1 ATOM 1042 C CE2 . TYR A 1 132 ? 5.051 8.334 57.073 1.00 56.03 ? 132 TYR A CE2 1 ATOM 1043 C CZ . TYR A 1 132 ? 3.669 8.316 56.878 1.00 56.71 ? 132 TYR A CZ 1 ATOM 1044 O OH . TYR A 1 132 ? 2.900 9.340 57.400 1.00 57.24 ? 132 TYR A OH 1 ATOM 1045 N N . CYS A 1 133 ? 7.792 4.174 52.213 1.00 48.39 ? 133 CYS A N 1 ATOM 1046 C CA . CYS A 1 133 ? 8.739 3.268 51.544 1.00 46.62 ? 133 CYS A CA 1 ATOM 1047 C C . CYS A 1 133 ? 8.783 1.887 52.178 1.00 46.42 ? 133 CYS A C 1 ATOM 1048 O O . CYS A 1 133 ? 9.805 1.196 52.113 1.00 46.28 ? 133 CYS A O 1 ATOM 1049 C CB . CYS A 1 133 ? 10.150 3.869 51.526 1.00 46.00 ? 133 CYS A CB 1 ATOM 1050 S SG . CYS A 1 133 ? 10.240 5.446 50.676 1.00 43.01 ? 133 CYS A SG 1 ATOM 1051 N N . ILE A 1 134 ? 7.677 1.491 52.800 1.00 46.03 ? 134 ILE A N 1 ATOM 1052 C CA . ILE A 1 134 ? 7.617 0.197 53.464 1.00 45.84 ? 134 ILE A CA 1 ATOM 1053 C C . ILE A 1 134 ? 7.411 -0.883 52.417 1.00 45.03 ? 134 ILE A C 1 ATOM 1054 O O . ILE A 1 134 ? 6.427 -0.874 51.663 1.00 44.56 ? 134 ILE A O 1 ATOM 1055 C CB . ILE A 1 134 ? 6.511 0.114 54.556 1.00 46.09 ? 134 ILE A CB 1 ATOM 1056 C CG1 . ILE A 1 134 ? 6.580 1.329 55.498 1.00 46.83 ? 134 ILE A CG1 1 ATOM 1057 C CG2 . ILE A 1 134 ? 6.684 -1.159 55.375 1.00 46.20 ? 134 ILE A CG2 1 ATOM 1058 C CD1 . ILE A 1 134 ? 5.258 1.630 56.222 1.00 47.62 ? 134 ILE A CD1 1 ATOM 1059 N N . GLN A 1 135 ? 8.371 -1.799 52.373 1.00 44.35 ? 135 GLN A N 1 ATOM 1060 C CA . GLN A 1 135 ? 8.289 -2.965 51.511 1.00 43.62 ? 135 GLN A CA 1 ATOM 1061 C C . GLN A 1 135 ? 7.201 -3.886 52.040 1.00 43.00 ? 135 GLN A C 1 ATOM 1062 O O . GLN A 1 135 ? 7.068 -4.071 53.254 1.00 42.58 ? 135 GLN A O 1 ATOM 1063 C CB . GLN A 1 135 ? 9.618 -3.698 51.497 1.00 43.48 ? 135 GLN A CB 1 ATOM 1064 C CG . GLN A 1 135 ? 9.777 -4.653 50.356 1.00 43.93 ? 135 GLN A CG 1 ATOM 1065 C CD . GLN A 1 135 ? 11.214 -5.030 50.169 1.00 45.06 ? 135 GLN A CD 1 ATOM 1066 O OE1 . GLN A 1 135 ? 12.065 -4.173 49.917 1.00 46.34 ? 135 GLN A OE1 1 ATOM 1067 N NE2 . GLN A 1 135 ? 11.510 -6.312 50.313 1.00 46.35 ? 135 GLN A NE2 1 ATOM 1068 N N . GLY A 1 136 ? 6.456 -4.370 51.173 1.00 47.72 ? 136 GLY A N 1 ATOM 1069 C CA . GLY A 1 136 ? 5.403 -5.254 51.595 1.00 47.70 ? 136 GLY A CA 1 ATOM 1070 C C . GLY A 1 136 ? 4.361 -5.472 50.523 1.00 48.00 ? 136 GLY A C 1 ATOM 1071 O O . GLY A 1 136 ? 3.952 -4.529 49.837 1.00 47.45 ? 136 GLY A O 1 ATOM 1072 N N . ASP A 1 137 ? 3.920 -6.734 50.411 1.00 48.56 ? 137 ASP A N 1 ATOM 1073 C CA . ASP A 1 137 ? 2.964 -7.152 49.392 1.00 48.44 ? 137 ASP A CA 1 ATOM 1074 C C . ASP A 1 137 ? 3.483 -6.657 48.063 1.00 47.90 ? 137 ASP A C 1 ATOM 1075 O O . ASP A 1 137 ? 4.634 -6.888 47.738 1.00 48.52 ? 137 ASP A O 1 ATOM 1076 C CB . ASP A 1 137 ? 1.566 -6.614 49.684 1.00 49.07 ? 137 ASP A CB 1 ATOM 1077 C CG . ASP A 1 137 ? 0.919 -7.282 50.908 1.00 50.99 ? 137 ASP A CG 1 ATOM 1078 O OD1 . ASP A 1 137 ? 1.298 -8.436 51.283 1.00 48.47 ? 137 ASP A OD1 1 ATOM 1079 O OD2 . ASP A 1 137 ? 0.014 -6.690 51.548 1.00 53.15 ? 137 ASP A OD2 1 ATOM 1080 N N . ASN A 1 138 ? 2.694 -5.933 47.295 1.00 46.82 ? 138 ASN A N 1 ATOM 1081 C CA . ASN A 1 138 ? 3.217 -5.566 45.992 1.00 45.44 ? 138 ASN A CA 1 ATOM 1082 C C . ASN A 1 138 ? 3.986 -4.247 45.956 1.00 44.55 ? 138 ASN A C 1 ATOM 1083 O O . ASN A 1 138 ? 4.237 -3.692 44.875 1.00 45.17 ? 138 ASN A O 1 ATOM 1084 C CB . ASN A 1 138 ? 2.116 -5.657 44.930 1.00 45.54 ? 138 ASN A CB 1 ATOM 1085 C CG . ASN A 1 138 ? 1.601 -7.128 44.705 1.00 46.35 ? 138 ASN A CG 1 ATOM 1086 O OD1 . ASN A 1 138 ? 2.309 -8.124 44.928 1.00 41.28 ? 138 ASN A OD1 1 ATOM 1087 N ND2 . ASN A 1 138 ? 0.366 -7.236 44.250 1.00 47.11 ? 138 ASN A ND2 1 ATOM 1088 N N . CYS A 1 139 ? 4.251 -3.616 47.093 1.00 36.35 ? 139 CYS A N 1 ATOM 1089 C CA . CYS A 1 139 ? 5.135 -2.458 47.180 1.00 36.18 ? 139 CYS A CA 1 ATOM 1090 C C . CYS A 1 139 ? 6.577 -2.922 47.303 1.00 34.72 ? 139 CYS A C 1 ATOM 1091 O O . CYS A 1 139 ? 6.972 -3.525 48.303 1.00 34.53 ? 139 CYS A O 1 ATOM 1092 C CB . CYS A 1 139 ? 4.755 -1.531 48.333 1.00 36.94 ? 139 CYS A CB 1 ATOM 1093 S SG . CYS A 1 139 ? 5.903 -0.127 48.572 1.00 41.48 ? 139 CYS A SG 1 ATOM 1094 N N . PHE A 1 140 ? 7.352 -2.627 46.263 1.00 33.51 ? 140 PHE A N 1 ATOM 1095 C CA . PHE A 1 140 ? 8.745 -3.049 46.140 1.00 32.02 ? 140 PHE A CA 1 ATOM 1096 C C . PHE A 1 140 ? 9.585 -1.794 45.810 1.00 31.72 ? 140 PHE A C 1 ATOM 1097 O O . PHE A 1 140 ? 9.968 -1.557 44.645 1.00 31.46 ? 140 PHE A O 1 ATOM 1098 C CB . PHE A 1 140 ? 8.832 -4.145 45.075 1.00 31.25 ? 140 PHE A CB 1 ATOM 1099 C CG . PHE A 1 140 ? 10.198 -4.721 44.883 1.00 30.32 ? 140 PHE A CG 1 ATOM 1100 C CD1 . PHE A 1 140 ? 11.076 -4.874 45.957 1.00 30.05 ? 140 PHE A CD1 1 ATOM 1101 C CD2 . PHE A 1 140 ? 10.603 -5.145 43.619 1.00 29.08 ? 140 PHE A CD2 1 ATOM 1102 C CE1 . PHE A 1 140 ? 12.337 -5.415 45.768 1.00 29.33 ? 140 PHE A CE1 1 ATOM 1103 C CE2 . PHE A 1 140 ? 11.859 -5.696 43.420 1.00 28.48 ? 140 PHE A CE2 1 ATOM 1104 C CZ . PHE A 1 140 ? 12.727 -5.832 44.495 1.00 28.56 ? 140 PHE A CZ 1 ATOM 1105 N N . PRO A 1 141 ? 9.860 -0.974 46.845 1.00 30.99 ? 141 PRO A N 1 ATOM 1106 C CA . PRO A 1 141 ? 10.367 0.389 46.663 1.00 30.35 ? 141 PRO A CA 1 ATOM 1107 C C . PRO A 1 141 ? 11.815 0.417 46.172 1.00 29.69 ? 141 PRO A C 1 ATOM 1108 O O . PRO A 1 141 ? 12.587 -0.492 46.461 1.00 28.96 ? 141 PRO A O 1 ATOM 1109 C CB . PRO A 1 141 ? 10.266 1.015 48.074 1.00 30.60 ? 141 PRO A CB 1 ATOM 1110 C CG . PRO A 1 141 ? 9.593 0.004 48.945 1.00 30.84 ? 141 PRO A CG 1 ATOM 1111 C CD . PRO A 1 141 ? 9.736 -1.330 48.270 1.00 31.06 ? 141 PRO A CD 1 ATOM 1112 N N . ILE A 1 142 ? 12.161 1.452 45.413 1.00 29.31 ? 142 ILE A N 1 ATOM 1113 C CA . ILE A 1 142 ? 13.519 1.635 44.953 1.00 29.27 ? 142 ILE A CA 1 ATOM 1114 C C . ILE A 1 142 ? 14.175 2.560 45.967 1.00 29.70 ? 142 ILE A C 1 ATOM 1115 O O . ILE A 1 142 ? 13.906 3.741 45.967 1.00 29.79 ? 142 ILE A O 1 ATOM 1116 C CB . ILE A 1 142 ? 13.556 2.205 43.489 1.00 29.28 ? 142 ILE A CB 1 ATOM 1117 C CG1 . ILE A 1 142 ? 12.994 1.176 42.491 1.00 28.62 ? 142 ILE A CG1 1 ATOM 1118 C CG2 . ILE A 1 142 ? 14.982 2.606 43.066 1.00 28.24 ? 142 ILE A CG2 1 ATOM 1119 C CD1 . ILE A 1 142 ? 12.540 1.757 41.177 1.00 25.80 ? 142 ILE A CD1 1 ATOM 1120 N N . MET A 1 143 ? 14.997 2.002 46.851 1.00 30.61 ? 143 MET A N 1 ATOM 1121 C CA . MET A 1 143 ? 15.688 2.763 47.888 1.00 32.06 ? 143 MET A CA 1 ATOM 1122 C C . MET A 1 143 ? 16.834 3.590 47.313 1.00 32.92 ? 143 MET A C 1 ATOM 1123 O O . MET A 1 143 ? 17.538 3.133 46.415 1.00 33.18 ? 143 MET A O 1 ATOM 1124 C CB . MET A 1 143 ? 16.258 1.832 48.979 1.00 32.20 ? 143 MET A CB 1 ATOM 1125 C CG . MET A 1 143 ? 15.260 0.939 49.728 1.00 32.41 ? 143 MET A CG 1 ATOM 1126 S SD . MET A 1 143 ? 13.745 1.744 50.322 1.00 34.86 ? 143 MET A SD 1 ATOM 1127 C CE . MET A 1 143 ? 14.378 3.128 51.274 1.00 33.69 ? 143 MET A CE 1 ATOM 1128 N N . PHE A 1 144 ? 17.026 4.800 47.839 1.00 33.94 ? 144 PHE A N 1 ATOM 1129 C CA . PHE A 1 144 ? 18.159 5.642 47.442 1.00 34.65 ? 144 PHE A CA 1 ATOM 1130 C C . PHE A 1 144 ? 19.417 5.248 48.203 1.00 35.36 ? 144 PHE A C 1 ATOM 1131 O O . PHE A 1 144 ? 19.359 5.035 49.412 1.00 35.22 ? 144 PHE A O 1 ATOM 1132 C CB . PHE A 1 144 ? 17.879 7.125 47.686 1.00 34.49 ? 144 PHE A CB 1 ATOM 1133 C CG . PHE A 1 144 ? 16.786 7.692 46.836 1.00 34.05 ? 144 PHE A CG 1 ATOM 1134 C CD1 . PHE A 1 144 ? 15.986 8.715 47.321 1.00 33.61 ? 144 PHE A CD1 1 ATOM 1135 C CD2 . PHE A 1 144 ? 16.553 7.209 45.555 1.00 34.66 ? 144 PHE A CD2 1 ATOM 1136 C CE1 . PHE A 1 144 ? 14.964 9.246 46.549 1.00 33.18 ? 144 PHE A CE1 1 ATOM 1137 C CE2 . PHE A 1 144 ? 15.537 7.734 44.779 1.00 34.58 ? 144 PHE A CE2 1 ATOM 1138 C CZ . PHE A 1 144 ? 14.741 8.760 45.277 1.00 33.59 ? 144 PHE A CZ 1 ATOM 1139 N N . PRO A 1 145 ? 20.556 5.139 47.489 1.00 36.25 ? 145 PRO A N 1 ATOM 1140 C CA . PRO A 1 145 ? 21.858 4.884 48.111 1.00 37.05 ? 145 PRO A CA 1 ATOM 1141 C C . PRO A 1 145 ? 22.330 6.067 48.934 1.00 38.32 ? 145 PRO A C 1 ATOM 1142 O O . PRO A 1 145 ? 21.745 7.156 48.851 1.00 38.28 ? 145 PRO A O 1 ATOM 1143 C CB . PRO A 1 145 ? 22.790 4.707 46.915 1.00 36.71 ? 145 PRO A CB 1 ATOM 1144 C CG . PRO A 1 145 ? 22.106 5.415 45.792 1.00 36.68 ? 145 PRO A CG 1 ATOM 1145 C CD . PRO A 1 145 ? 20.656 5.225 46.019 1.00 36.14 ? 145 PRO A CD 1 ATOM 1146 N N . LYS A 1 146 ? 23.377 5.842 49.727 1.00 39.72 ? 146 LYS A N 1 ATOM 1147 C CA . LYS A 1 146 ? 24.078 6.924 50.417 1.00 40.87 ? 146 LYS A CA 1 ATOM 1148 C C . LYS A 1 146 ? 24.704 7.825 49.346 1.00 41.08 ? 146 LYS A C 1 ATOM 1149 O O . LYS A 1 146 ? 25.243 7.322 48.333 1.00 41.07 ? 146 LYS A O 1 ATOM 1150 C CB . LYS A 1 146 ? 25.126 6.344 51.386 1.00 41.26 ? 146 LYS A CB 1 ATOM 1151 C CG . LYS A 1 146 ? 26.464 7.116 51.512 1.00 43.30 ? 146 LYS A CG 1 ATOM 1152 C CD . LYS A 1 146 ? 27.517 6.352 52.339 1.00 45.96 ? 146 LYS A CD 1 ATOM 1153 C CE . LYS A 1 146 ? 27.197 6.390 53.852 1.00 48.33 ? 146 LYS A CE 1 ATOM 1154 N NZ . LYS A 1 146 ? 28.256 5.760 54.724 1.00 48.39 ? 146 LYS A NZ 1 ATOM 1155 N N . ASN A 1 147 ? 24.614 9.145 49.560 1.00 41.01 ? 147 ASN A N 1 ATOM 1156 C CA . ASN A 1 147 ? 25.200 10.135 48.639 1.00 41.18 ? 147 ASN A CA 1 ATOM 1157 C C . ASN A 1 147 ? 24.376 10.389 47.344 1.00 40.36 ? 147 ASN A C 1 ATOM 1158 O O . ASN A 1 147 ? 24.895 11.002 46.401 1.00 40.46 ? 147 ASN A O 1 ATOM 1159 C CB . ASN A 1 147 ? 26.675 9.791 48.247 1.00 41.66 ? 147 ASN A CB 1 ATOM 1160 C CG . ASN A 1 147 ? 27.648 9.677 49.482 1.00 43.49 ? 147 ASN A CG 1 ATOM 1161 O OD1 . ASN A 1 147 ? 27.516 10.399 50.486 1.00 45.30 ? 147 ASN A OD1 1 ATOM 1162 N ND2 . ASN A 1 147 ? 28.641 8.777 49.374 1.00 44.41 ? 147 ASN A ND2 1 ATOM 1163 N N . ASP A 1 148 ? 23.126 9.913 47.281 1.00 39.07 ? 148 ASP A N 1 ATOM 1164 C CA . ASP A 1 148 ? 22.269 10.209 46.126 1.00 38.00 ? 148 ASP A CA 1 ATOM 1165 C C . ASP A 1 148 ? 21.625 11.565 46.333 1.00 37.44 ? 148 ASP A C 1 ATOM 1166 O O . ASP A 1 148 ? 20.969 11.792 47.350 1.00 37.16 ? 148 ASP A O 1 ATOM 1167 C CB . ASP A 1 148 ? 21.180 9.139 45.901 1.00 38.05 ? 148 ASP A CB 1 ATOM 1168 C CG . ASP A 1 148 ? 20.429 9.316 44.557 1.00 37.48 ? 148 ASP A CG 1 ATOM 1169 O OD1 . ASP A 1 148 ? 19.809 10.373 44.310 1.00 36.31 ? 148 ASP A OD1 1 ATOM 1170 O OD2 . ASP A 1 148 ? 20.453 8.378 43.734 1.00 38.91 ? 148 ASP A OD2 1 ATOM 1171 N N . PRO A 1 149 ? 21.793 12.476 45.359 1.00 37.01 ? 149 PRO A N 1 ATOM 1172 C CA . PRO A 1 149 ? 21.204 13.800 45.526 1.00 36.49 ? 149 PRO A CA 1 ATOM 1173 C C . PRO A 1 149 ? 19.707 13.740 45.849 1.00 36.18 ? 149 PRO A C 1 ATOM 1174 O O . PRO A 1 149 ? 19.245 14.530 46.684 1.00 36.80 ? 149 PRO A O 1 ATOM 1175 C CB . PRO A 1 149 ? 21.443 14.472 44.175 1.00 36.36 ? 149 PRO A CB 1 ATOM 1176 C CG . PRO A 1 149 ? 22.613 13.760 43.602 1.00 36.82 ? 149 PRO A CG 1 ATOM 1177 C CD . PRO A 1 149 ? 22.518 12.342 44.081 1.00 36.80 ? 149 PRO A CD 1 ATOM 1178 N N . LYS A 1 150 ? 18.963 12.812 45.233 1.00 35.18 ? 150 LYS A N 1 ATOM 1179 C CA . LYS A 1 150 ? 17.505 12.761 45.418 1.00 34.21 ? 150 LYS A CA 1 ATOM 1180 C C . LYS A 1 150 ? 17.029 12.522 46.857 1.00 34.25 ? 150 LYS A C 1 ATOM 1181 O O . LYS A 1 150 ? 15.870 12.778 47.180 1.00 33.56 ? 150 LYS A O 1 ATOM 1182 C CB . LYS A 1 150 ? 16.874 11.756 44.463 1.00 33.99 ? 150 LYS A CB 1 ATOM 1183 C CG . LYS A 1 150 ? 16.632 12.326 43.078 1.00 32.92 ? 150 LYS A CG 1 ATOM 1184 C CD . LYS A 1 150 ? 16.082 11.276 42.138 1.00 30.77 ? 150 LYS A CD 1 ATOM 1185 C CE . LYS A 1 150 ? 16.098 11.777 40.712 1.00 29.70 ? 150 LYS A CE 1 ATOM 1186 N NZ . LYS A 1 150 ? 14.908 12.625 40.458 1.00 26.61 ? 150 LYS A NZ 1 ATOM 1187 N N . LEU A 1 151 ? 17.925 12.021 47.708 1.00 34.71 ? 151 LEU A N 1 ATOM 1188 C CA . LEU A 1 151 ? 17.692 11.940 49.156 1.00 35.30 ? 151 LEU A CA 1 ATOM 1189 C C . LEU A 1 151 ? 17.341 13.308 49.738 1.00 35.88 ? 151 LEU A C 1 ATOM 1190 O O . LEU A 1 151 ? 16.330 13.472 50.431 1.00 36.33 ? 151 LEU A O 1 ATOM 1191 C CB . LEU A 1 151 ? 18.941 11.413 49.866 1.00 35.01 ? 151 LEU A CB 1 ATOM 1192 C CG . LEU A 1 151 ? 19.053 9.938 50.271 1.00 35.44 ? 151 LEU A CG 1 ATOM 1193 C CD1 . LEU A 1 151 ? 20.435 9.689 50.858 1.00 35.58 ? 151 LEU A CD1 1 ATOM 1194 C CD2 . LEU A 1 151 ? 17.980 9.533 51.277 1.00 33.33 ? 151 LEU A CD2 1 ATOM 1195 N N . LYS A 1 152 ? 18.191 14.284 49.434 1.00 36.40 ? 152 LYS A N 1 ATOM 1196 C CA . LYS A 1 152 ? 18.090 15.629 49.956 1.00 36.93 ? 152 LYS A CA 1 ATOM 1197 C C . LYS A 1 152 ? 16.788 16.331 49.584 1.00 37.17 ? 152 LYS A C 1 ATOM 1198 O O . LYS A 1 152 ? 16.320 17.172 50.343 1.00 37.72 ? 152 LYS A O 1 ATOM 1199 C CB . LYS A 1 152 ? 19.299 16.452 49.500 1.00 37.19 ? 152 LYS A CB 1 ATOM 1200 C CG . LYS A 1 152 ? 20.638 15.850 49.950 1.00 38.34 ? 152 LYS A CG 1 ATOM 1201 C CD . LYS A 1 152 ? 21.859 16.619 49.436 1.00 39.19 ? 152 LYS A CD 1 ATOM 1202 C CE . LYS A 1 152 ? 23.082 16.398 50.347 1.00 39.26 ? 152 LYS A CE 1 ATOM 1203 N NZ . LYS A 1 152 ? 24.202 17.377 50.076 1.00 40.13 ? 152 LYS A NZ 1 ATOM 1204 N N . THR A 1 153 ? 16.194 15.986 48.441 1.00 37.37 ? 153 THR A N 1 ATOM 1205 C CA . THR A 1 153 ? 15.036 16.743 47.923 1.00 37.12 ? 153 THR A CA 1 ATOM 1206 C C . THR A 1 153 ? 13.710 15.971 47.787 1.00 37.67 ? 153 THR A C 1 ATOM 1207 O O . THR A 1 153 ? 12.656 16.597 47.631 1.00 37.61 ? 153 THR A O 1 ATOM 1208 C CB . THR A 1 153 ? 15.329 17.335 46.543 1.00 36.94 ? 153 THR A CB 1 ATOM 1209 O OG1 . THR A 1 153 ? 15.387 16.267 45.596 1.00 36.02 ? 153 THR A OG1 1 ATOM 1210 C CG2 . THR A 1 153 ? 16.653 18.086 46.534 1.00 36.08 ? 153 THR A CG2 1 ATOM 1211 N N . GLN A 1 154 ? 13.860 14.606 47.539 1.00 37.82 ? 154 GLN A N 1 ATOM 1212 C CA . GLN A 1 154 ? 12.708 13.776 47.170 1.00 38.03 ? 154 GLN A CA 1 ATOM 1213 C C . GLN A 1 154 ? 12.191 12.875 48.278 1.00 38.15 ? 154 GLN A C 1 ATOM 1214 O O . GLN A 1 154 ? 10.980 12.710 48.412 1.00 38.83 ? 154 GLN A O 1 ATOM 1215 C CB . GLN A 1 154 ? 12.995 12.929 45.926 1.00 38.27 ? 154 GLN A CB 1 ATOM 1216 C CG . GLN A 1 154 ? 12.799 13.666 44.611 1.00 38.80 ? 154 GLN A CG 1 ATOM 1217 C CD . GLN A 1 154 ? 12.668 12.732 43.420 1.00 39.96 ? 154 GLN A CD 1 ATOM 1218 O OE1 . GLN A 1 154 ? 13.104 13.064 42.328 1.00 41.27 ? 154 GLN A OE1 1 ATOM 1219 N NE2 . GLN A 1 154 ? 12.059 11.568 43.624 1.00 39.42 ? 154 GLN A NE2 1 ATOM 1220 N N . GLY A 1 155 ? 13.093 12.273 49.047 1.00 37.84 ? 155 GLY A N 1 ATOM 1221 C CA . GLY A 1 155 ? 12.700 11.404 50.149 1.00 37.84 ? 155 GLY A CA 1 ATOM 1222 C C . GLY A 1 155 ? 13.586 10.179 50.300 1.00 38.00 ? 155 GLY A C 1 ATOM 1223 O O . GLY A 1 155 ? 14.775 10.216 49.987 1.00 37.98 ? 155 GLY A O 1 ATOM 1224 N N . LYS A 1 156 ? 13.006 9.080 50.770 1.00 37.93 ? 156 LYS A N 1 ATOM 1225 C CA . LYS A 1 156 ? 13.792 7.888 51.073 1.00 37.67 ? 156 LYS A CA 1 ATOM 1226 C C . LYS A 1 156 ? 13.829 6.900 49.906 1.00 36.81 ? 156 LYS A C 1 ATOM 1227 O O . LYS A 1 156 ? 14.775 6.115 49.783 1.00 36.69 ? 156 LYS A O 1 ATOM 1228 C CB . LYS A 1 156 ? 13.264 7.208 52.342 1.00 38.01 ? 156 LYS A CB 1 ATOM 1229 C CG . LYS A 1 156 ? 13.458 8.008 53.624 1.00 40.50 ? 156 LYS A CG 1 ATOM 1230 C CD . LYS A 1 156 ? 14.730 7.584 54.385 1.00 45.21 ? 156 LYS A CD 1 ATOM 1231 C CE . LYS A 1 156 ? 15.865 8.635 54.265 1.00 47.63 ? 156 LYS A CE 1 ATOM 1232 N NZ . LYS A 1 156 ? 17.204 8.130 54.800 1.00 48.46 ? 156 LYS A NZ 1 ATOM 1233 N N . CYS A 1 157 ? 12.813 6.940 49.048 1.00 35.79 ? 157 CYS A N 1 ATOM 1234 C CA . CYS A 1 157 ? 12.723 5.979 47.952 1.00 35.25 ? 157 CYS A CA 1 ATOM 1235 C C . CYS A 1 157 ? 11.935 6.481 46.756 1.00 34.72 ? 157 CYS A C 1 ATOM 1236 O O . CYS A 1 157 ? 11.334 7.551 46.791 1.00 34.28 ? 157 CYS A O 1 ATOM 1237 C CB . CYS A 1 157 ? 12.053 4.700 48.440 1.00 35.23 ? 157 CYS A CB 1 ATOM 1238 S SG . CYS A 1 157 ? 10.319 4.939 48.724 1.00 36.06 ? 157 CYS A SG 1 ATOM 1239 N N . MET A 1 158 ? 11.939 5.682 45.697 1.00 34.24 ? 158 MET A N 1 ATOM 1240 C CA . MET A 1 158 ? 10.996 5.865 44.615 1.00 34.13 ? 158 MET A CA 1 ATOM 1241 C C . MET A 1 158 ? 9.987 4.722 44.708 1.00 33.85 ? 158 MET A C 1 ATOM 1242 O O . MET A 1 158 ? 10.378 3.551 44.797 1.00 34.00 ? 158 MET A O 1 ATOM 1243 C CB . MET A 1 158 ? 11.701 5.857 43.261 1.00 34.09 ? 158 MET A CB 1 ATOM 1244 C CG . MET A 1 158 ? 12.509 7.097 42.949 1.00 35.14 ? 158 MET A CG 1 ATOM 1245 S SD . MET A 1 158 ? 13.215 7.024 41.279 1.00 37.57 ? 158 MET A SD 1 ATOM 1246 C CE . MET A 1 158 ? 14.749 6.178 41.585 1.00 36.62 ? 158 MET A CE 1 ATOM 1247 N N . PRO A 1 159 ? 8.686 5.053 44.730 1.00 33.42 ? 159 PRO A N 1 ATOM 1248 C CA . PRO A 1 159 ? 7.665 4.011 44.741 1.00 33.28 ? 159 PRO A CA 1 ATOM 1249 C C . PRO A 1 159 ? 7.684 3.154 43.467 1.00 33.17 ? 159 PRO A C 1 ATOM 1250 O O . PRO A 1 159 ? 7.972 3.641 42.375 1.00 33.02 ? 159 PRO A O 1 ATOM 1251 C CB . PRO A 1 159 ? 6.357 4.796 44.842 1.00 33.25 ? 159 PRO A CB 1 ATOM 1252 C CG . PRO A 1 159 ? 6.685 6.152 44.311 1.00 33.08 ? 159 PRO A CG 1 ATOM 1253 C CD . PRO A 1 159 ? 8.095 6.401 44.752 1.00 33.24 ? 159 PRO A CD 1 ATOM 1254 N N . PHE A 1 160 ? 7.376 1.877 43.644 1.00 33.13 ? 160 PHE A N 1 ATOM 1255 C CA . PHE A 1 160 ? 7.407 0.886 42.593 1.00 32.75 ? 160 PHE A CA 1 ATOM 1256 C C . PHE A 1 160 ? 6.467 -0.232 43.011 1.00 33.12 ? 160 PHE A C 1 ATOM 1257 O O . PHE A 1 160 ? 6.510 -0.701 44.152 1.00 33.09 ? 160 PHE A O 1 ATOM 1258 C CB . PHE A 1 160 ? 8.828 0.355 42.446 1.00 32.65 ? 160 PHE A CB 1 ATOM 1259 C CG . PHE A 1 160 ? 8.992 -0.683 41.378 1.00 30.95 ? 160 PHE A CG 1 ATOM 1260 C CD1 . PHE A 1 160 ? 8.701 -2.018 41.633 1.00 30.26 ? 160 PHE A CD1 1 ATOM 1261 C CD2 . PHE A 1 160 ? 9.475 -0.331 40.130 1.00 29.39 ? 160 PHE A CD2 1 ATOM 1262 C CE1 . PHE A 1 160 ? 8.870 -2.977 40.645 1.00 30.10 ? 160 PHE A CE1 1 ATOM 1263 C CE2 . PHE A 1 160 ? 9.654 -1.280 39.146 1.00 28.50 ? 160 PHE A CE2 1 ATOM 1264 C CZ . PHE A 1 160 ? 9.361 -2.604 39.401 1.00 28.50 ? 160 PHE A CZ 1 ATOM 1265 N N . PHE A 1 161 ? 5.614 -0.642 42.080 1.00 33.67 ? 161 PHE A N 1 ATOM 1266 C CA . PHE A 1 161 ? 4.610 -1.673 42.320 1.00 34.10 ? 161 PHE A CA 1 ATOM 1267 C C . PHE A 1 161 ? 4.841 -2.834 41.386 1.00 33.75 ? 161 PHE A C 1 ATOM 1268 O O . PHE A 1 161 ? 5.090 -2.636 40.192 1.00 33.85 ? 161 PHE A O 1 ATOM 1269 C CB . PHE A 1 161 ? 3.209 -1.106 42.109 1.00 34.35 ? 161 PHE A CB 1 ATOM 1270 C CG . PHE A 1 161 ? 2.925 0.078 42.966 1.00 36.59 ? 161 PHE A CG 1 ATOM 1271 C CD1 . PHE A 1 161 ? 3.126 1.369 42.476 1.00 38.15 ? 161 PHE A CD1 1 ATOM 1272 C CD2 . PHE A 1 161 ? 2.498 -0.093 44.283 1.00 38.16 ? 161 PHE A CD2 1 ATOM 1273 C CE1 . PHE A 1 161 ? 2.893 2.472 43.279 1.00 39.39 ? 161 PHE A CE1 1 ATOM 1274 C CE2 . PHE A 1 161 ? 2.258 1.002 45.093 1.00 38.83 ? 161 PHE A CE2 1 ATOM 1275 C CZ . PHE A 1 161 ? 2.457 2.286 44.594 1.00 39.70 ? 161 PHE A CZ 1 ATOM 1276 N N . ARG A 1 162 ? 4.750 -4.040 41.935 1.00 33.39 ? 162 ARG A N 1 ATOM 1277 C CA . ARG A 1 162 ? 5.038 -5.251 41.187 1.00 33.22 ? 162 ARG A CA 1 ATOM 1278 C C . ARG A 1 162 ? 4.033 -5.509 40.069 1.00 33.67 ? 162 ARG A C 1 ATOM 1279 O O . ARG A 1 162 ? 2.868 -5.124 40.172 1.00 33.51 ? 162 ARG A O 1 ATOM 1280 C CB . ARG A 1 162 ? 5.105 -6.440 42.126 1.00 32.95 ? 162 ARG A CB 1 ATOM 1281 C CG . ARG A 1 162 ? 6.183 -6.340 43.154 1.00 31.32 ? 162 ARG A CG 1 ATOM 1282 C CD . ARG A 1 162 ? 6.394 -7.690 43.786 1.00 31.04 ? 162 ARG A CD 1 ATOM 1283 N NE . ARG A 1 162 ? 7.027 -8.610 42.853 1.00 30.05 ? 162 ARG A NE 1 ATOM 1284 C CZ . ARG A 1 162 ? 7.229 -9.899 43.087 1.00 30.15 ? 162 ARG A CZ 1 ATOM 1285 N NH1 . ARG A 1 162 ? 6.841 -10.449 44.229 1.00 30.26 ? 162 ARG A NH1 1 ATOM 1286 N NH2 . ARG A 1 162 ? 7.824 -10.640 42.173 1.00 30.44 ? 162 ARG A NH2 1 ATOM 1287 N N . ALA A 1 163 ? 4.503 -6.166 39.008 1.00 34.21 ? 163 ALA A N 1 ATOM 1288 C CA . ALA A 1 163 ? 3.713 -6.375 37.794 1.00 34.77 ? 163 ALA A CA 1 ATOM 1289 C C . ALA A 1 163 ? 2.592 -7.349 38.050 1.00 35.33 ? 163 ALA A C 1 ATOM 1290 O O . ALA A 1 163 ? 2.684 -8.170 38.956 1.00 35.62 ? 163 ALA A O 1 ATOM 1291 C CB . ALA A 1 163 ? 4.600 -6.878 36.670 1.00 34.41 ? 163 ALA A CB 1 ATOM 1292 N N . GLY A 1 164 ? 1.529 -7.258 37.256 1.00 36.42 ? 164 GLY A N 1 ATOM 1293 C CA . GLY A 1 164 ? 0.413 -8.190 37.357 1.00 37.71 ? 164 GLY A CA 1 ATOM 1294 C C . GLY A 1 164 ? 0.840 -9.609 37.043 1.00 39.08 ? 164 GLY A C 1 ATOM 1295 O O . GLY A 1 164 ? 1.857 -9.824 36.385 1.00 38.58 ? 164 GLY A O 1 ATOM 1296 N N . PHE A 1 165 ? 0.066 -10.580 37.522 1.00 40.91 ? 165 PHE A N 1 ATOM 1297 C CA . PHE A 1 165 ? 0.378 -11.991 37.299 1.00 42.90 ? 165 PHE A CA 1 ATOM 1298 C C . PHE A 1 165 ? -0.855 -12.855 37.031 1.00 44.91 ? 165 PHE A C 1 ATOM 1299 O O . PHE A 1 165 ? -1.945 -12.569 37.535 1.00 44.48 ? 165 PHE A O 1 ATOM 1300 C CB . PHE A 1 165 ? 1.229 -12.560 38.443 1.00 42.53 ? 165 PHE A CB 1 ATOM 1301 C CG . PHE A 1 165 ? 0.618 -12.411 39.806 1.00 41.04 ? 165 PHE A CG 1 ATOM 1302 C CD1 . PHE A 1 165 ? 0.614 -11.178 40.456 1.00 39.49 ? 165 PHE A CD1 1 ATOM 1303 C CD2 . PHE A 1 165 ? 0.074 -13.518 40.459 1.00 40.41 ? 165 PHE A CD2 1 ATOM 1304 C CE1 . PHE A 1 165 ? 0.047 -11.042 41.733 1.00 38.35 ? 165 PHE A CE1 1 ATOM 1305 C CE2 . PHE A 1 165 ? -0.487 -13.394 41.735 1.00 39.36 ? 165 PHE A CE2 1 ATOM 1306 C CZ . PHE A 1 165 ? -0.499 -12.157 42.371 1.00 38.42 ? 165 PHE A CZ 1 ATOM 1307 N N . VAL A 1 166 ? -0.658 -13.905 36.229 1.00 47.90 ? 166 VAL A N 1 ATOM 1308 C CA . VAL A 1 166 ? -1.745 -14.769 35.741 1.00 51.00 ? 166 VAL A CA 1 ATOM 1309 C C . VAL A 1 166 ? -2.391 -15.646 36.800 1.00 53.89 ? 166 VAL A C 1 ATOM 1310 O O . VAL A 1 166 ? -2.132 -15.498 38.001 1.00 53.69 ? 166 VAL A O 1 ATOM 1311 C CB . VAL A 1 166 ? -1.338 -15.674 34.541 1.00 50.56 ? 166 VAL A CB 1 ATOM 1312 C CG1 . VAL A 1 166 ? -1.600 -14.975 33.217 1.00 49.95 ? 166 VAL A CG1 1 ATOM 1313 C CG2 . VAL A 1 166 ? 0.090 -16.180 34.672 1.00 50.20 ? 166 VAL A CG2 1 ATOM 1314 N N . CYS A 1 167 ? -3.209 -16.593 36.323 1.00 57.96 ? 167 CYS A N 1 ATOM 1315 C CA . CYS A 1 167 ? -4.308 -17.135 37.111 1.00 61.87 ? 167 CYS A CA 1 ATOM 1316 C C . CYS A 1 167 ? -4.905 -15.856 37.772 1.00 63.33 ? 167 CYS A C 1 ATOM 1317 O O . CYS A 1 167 ? -4.955 -14.790 37.118 1.00 63.82 ? 167 CYS A O 1 ATOM 1318 C CB . CYS A 1 167 ? -3.829 -18.211 38.115 1.00 62.49 ? 167 CYS A CB 1 ATOM 1319 S SG . CYS A 1 167 ? -3.263 -19.865 37.461 1.00 67.84 ? 167 CYS A SG 1 ATOM 1320 N N . PRO A 1 168 ? -5.355 -15.951 39.040 1.00 64.76 ? 168 PRO A N 1 ATOM 1321 C CA . PRO A 1 168 ? -5.904 -14.912 39.918 1.00 65.66 ? 168 PRO A CA 1 ATOM 1322 C C . PRO A 1 168 ? -5.284 -13.509 39.959 1.00 66.85 ? 168 PRO A C 1 ATOM 1323 O O . PRO A 1 168 ? -4.788 -12.964 38.973 1.00 66.85 ? 168 PRO A O 1 ATOM 1324 C CB . PRO A 1 168 ? -5.656 -15.510 41.297 1.00 65.60 ? 168 PRO A CB 1 ATOM 1325 C CG . PRO A 1 168 ? -5.801 -16.940 41.097 1.00 65.58 ? 168 PRO A CG 1 ATOM 1326 C CD . PRO A 1 168 ? -5.368 -17.264 39.719 1.00 64.99 ? 168 PRO A CD 1 ATOM 1327 N N . THR A 1 169 ? -5.413 -12.935 41.152 1.00 68.28 ? 169 THR A N 1 ATOM 1328 C CA . THR A 1 169 ? -4.757 -11.722 41.608 1.00 69.52 ? 169 THR A CA 1 ATOM 1329 C C . THR A 1 169 ? -4.473 -12.096 43.089 1.00 70.31 ? 169 THR A C 1 ATOM 1330 O O . THR A 1 169 ? -3.780 -13.098 43.310 1.00 70.52 ? 169 THR A O 1 ATOM 1331 C CB . THR A 1 169 ? -5.633 -10.464 41.365 1.00 69.53 ? 169 THR A CB 1 ATOM 1332 O OG1 . THR A 1 169 ? -6.227 -10.552 40.061 1.00 70.00 ? 169 THR A OG1 1 ATOM 1333 C CG2 . THR A 1 169 ? -4.795 -9.180 41.446 1.00 69.63 ? 169 THR A CG2 1 ATOM 1334 N N . PRO A 1 170 ? -5.111 -11.444 44.092 1.00 71.05 ? 170 PRO A N 1 ATOM 1335 C CA . PRO A 1 170 ? -4.653 -11.438 45.501 1.00 71.59 ? 170 PRO A CA 1 ATOM 1336 C C . PRO A 1 170 ? -3.318 -12.150 45.869 1.00 71.95 ? 170 PRO A C 1 ATOM 1337 O O . PRO A 1 170 ? -2.518 -12.453 44.982 1.00 71.93 ? 170 PRO A O 1 ATOM 1338 C CB . PRO A 1 170 ? -5.891 -12.051 46.235 1.00 71.58 ? 170 PRO A CB 1 ATOM 1339 C CG . PRO A 1 170 ? -7.119 -11.537 45.335 1.00 71.40 ? 170 PRO A CG 1 ATOM 1340 C CD . PRO A 1 170 ? -6.489 -10.908 44.042 1.00 71.31 ? 170 PRO A CD 1 ATOM 1341 N N . PRO A 1 171 ? -3.043 -12.359 47.178 1.00 72.36 ? 171 PRO A N 1 ATOM 1342 C CA . PRO A 1 171 ? -1.824 -13.130 47.522 1.00 72.45 ? 171 PRO A CA 1 ATOM 1343 C C . PRO A 1 171 ? -1.820 -14.536 46.893 1.00 72.52 ? 171 PRO A C 1 ATOM 1344 O O . PRO A 1 171 ? -2.782 -15.293 47.093 1.00 72.68 ? 171 PRO A O 1 ATOM 1345 C CB . PRO A 1 171 ? -1.890 -13.225 49.056 1.00 72.54 ? 171 PRO A CB 1 ATOM 1346 C CG . PRO A 1 171 ? -2.762 -12.063 49.478 1.00 72.51 ? 171 PRO A CG 1 ATOM 1347 C CD . PRO A 1 171 ? -3.770 -11.898 48.384 1.00 72.33 ? 171 PRO A CD 1 ATOM 1348 N N . TYR A 1 172 ? -0.791 -14.778 46.093 1.00 72.48 ? 172 TYR A N 1 ATOM 1349 C CA . TYR A 1 172 ? -0.792 -16.086 45.450 1.00 72.35 ? 172 TYR A CA 1 ATOM 1350 C C . TYR A 1 172 ? 0.470 -16.894 45.568 1.00 71.69 ? 172 TYR A C 1 ATOM 1351 O O . TYR A 1 172 ? 1.568 -16.424 45.914 1.00 71.83 ? 172 TYR A O 1 ATOM 1352 C CB . TYR A 1 172 ? -1.250 -15.998 44.003 1.00 72.65 ? 172 TYR A CB 1 ATOM 1353 C CG . TYR A 1 172 ? -2.366 -17.010 43.782 1.00 74.16 ? 172 TYR A CG 1 ATOM 1354 C CD1 . TYR A 1 172 ? -3.653 -16.695 44.240 1.00 75.50 ? 172 TYR A CD1 1 ATOM 1355 C CD2 . TYR A 1 172 ? -2.154 -18.254 43.164 1.00 75.74 ? 172 TYR A CD2 1 ATOM 1356 C CE1 . TYR A 1 172 ? -4.706 -17.584 44.074 1.00 76.55 ? 172 TYR A CE1 1 ATOM 1357 C CE2 . TYR A 1 172 ? -3.199 -19.150 42.982 1.00 76.74 ? 172 TYR A CE2 1 ATOM 1358 C CZ . TYR A 1 172 ? -4.476 -18.809 43.442 1.00 77.47 ? 172 TYR A CZ 1 ATOM 1359 O OH . TYR A 1 172 ? -5.522 -19.688 43.257 1.00 78.53 ? 172 TYR A OH 1 ATOM 1360 N N . GLN A 1 173 ? 0.210 -18.132 45.254 1.00 80.64 ? 173 GLN A N 1 ATOM 1361 C CA . GLN A 1 173 ? 1.171 -19.202 45.571 1.00 79.63 ? 173 GLN A CA 1 ATOM 1362 C C . GLN A 1 173 ? 1.685 -20.227 44.509 1.00 77.94 ? 173 GLN A C 1 ATOM 1363 O O . GLN A 1 173 ? 2.480 -19.885 43.628 1.00 77.90 ? 173 GLN A O 1 ATOM 1364 C CB . GLN A 1 173 ? 0.593 -20.009 46.774 1.00 80.15 ? 173 GLN A CB 1 ATOM 1365 C CG . GLN A 1 173 ? -0.780 -20.729 46.483 1.00 81.60 ? 173 GLN A CG 1 ATOM 1366 C CD . GLN A 1 173 ? -1.456 -21.367 47.722 1.00 83.56 ? 173 GLN A CD 1 ATOM 1367 O OE1 . GLN A 1 173 ? -0.838 -22.161 48.450 1.00 83.47 ? 173 GLN A OE1 1 ATOM 1368 N NE2 . GLN A 1 173 ? -2.732 -21.028 47.942 1.00 82.96 ? 173 GLN A NE2 1 ATOM 1369 N N . SER A 1 174 ? 1.263 -21.489 44.709 1.00 75.58 ? 174 SER A N 1 ATOM 1370 C CA . SER A 1 174 ? 1.650 -22.743 43.993 1.00 73.04 ? 174 SER A CA 1 ATOM 1371 C C . SER A 1 174 ? 2.926 -22.790 43.117 1.00 70.61 ? 174 SER A C 1 ATOM 1372 O O . SER A 1 174 ? 3.977 -23.312 43.522 1.00 70.42 ? 174 SER A O 1 ATOM 1373 C CB . SER A 1 174 ? 0.473 -23.264 43.143 1.00 73.57 ? 174 SER A CB 1 ATOM 1374 O OG . SER A 1 174 ? -0.761 -23.215 43.836 1.00 74.45 ? 174 SER A OG 1 ATOM 1375 N N . LEU A 1 175 ? 2.757 -22.273 41.895 1.00 67.21 ? 175 LEU A N 1 ATOM 1376 C CA . LEU A 1 175 ? 3.714 -22.233 40.788 1.00 63.28 ? 175 LEU A CA 1 ATOM 1377 C C . LEU A 1 175 ? 4.544 -20.980 40.869 1.00 59.82 ? 175 LEU A C 1 ATOM 1378 O O . LEU A 1 175 ? 4.288 -20.111 41.688 1.00 59.89 ? 175 LEU A O 1 ATOM 1379 C CB . LEU A 1 175 ? 2.897 -22.117 39.506 1.00 63.93 ? 175 LEU A CB 1 ATOM 1380 C CG . LEU A 1 175 ? 3.244 -22.913 38.270 1.00 65.43 ? 175 LEU A CG 1 ATOM 1381 C CD1 . LEU A 1 175 ? 1.947 -23.278 37.589 1.00 65.98 ? 175 LEU A CD1 1 ATOM 1382 C CD2 . LEU A 1 175 ? 4.138 -22.086 37.340 1.00 68.20 ? 175 LEU A CD2 1 ATOM 1383 N N . ALA A 1 176 ? 5.505 -21.017 39.992 1.00 50.66 ? 176 ALA A N 1 ATOM 1384 C CA . ALA A 1 176 ? 6.222 -19.740 40.035 1.00 47.57 ? 176 ALA A CA 1 ATOM 1385 C C . ALA A 1 176 ? 5.368 -18.605 39.449 1.00 45.16 ? 176 ALA A C 1 ATOM 1386 O O . ALA A 1 176 ? 4.496 -18.837 38.618 1.00 44.89 ? 176 ALA A O 1 ATOM 1387 C CB . ALA A 1 176 ? 7.564 -19.845 39.330 1.00 47.56 ? 176 ALA A CB 1 ATOM 1388 N N . ARG A 1 177 ? 5.616 -17.387 39.908 1.00 42.32 ? 177 ARG A N 1 ATOM 1389 C CA . ARG A 1 177 ? 4.834 -16.209 39.518 1.00 39.87 ? 177 ARG A CA 1 ATOM 1390 C C . ARG A 1 177 ? 5.056 -15.840 38.049 1.00 38.16 ? 177 ARG A C 1 ATOM 1391 O O . ARG A 1 177 ? 6.192 -15.563 37.642 1.00 37.87 ? 177 ARG A O 1 ATOM 1392 C CB . ARG A 1 177 ? 5.235 -15.044 40.422 1.00 39.80 ? 177 ARG A CB 1 ATOM 1393 C CG . ARG A 1 177 ? 4.507 -13.743 40.229 1.00 38.99 ? 177 ARG A CG 1 ATOM 1394 C CD . ARG A 1 177 ? 5.055 -12.834 41.270 1.00 39.17 ? 177 ARG A CD 1 ATOM 1395 N NE . ARG A 1 177 ? 4.396 -11.539 41.357 1.00 38.65 ? 177 ARG A NE 1 ATOM 1396 C CZ . ARG A 1 177 ? 3.491 -11.217 42.271 1.00 38.58 ? 177 ARG A CZ 1 ATOM 1397 N NH1 . ARG A 1 177 ? 3.091 -12.100 43.178 1.00 38.07 ? 177 ARG A NH1 1 ATOM 1398 N NH2 . ARG A 1 177 ? 2.977 -9.999 42.268 1.00 40.03 ? 177 ARG A NH2 1 ATOM 1399 N N . GLU A 1 178 ? 3.981 -15.850 37.257 1.00 35.91 ? 178 GLU A N 1 ATOM 1400 C CA . GLU A 1 178 ? 4.081 -15.530 35.819 1.00 33.91 ? 178 GLU A CA 1 ATOM 1401 C C . GLU A 1 178 ? 3.364 -14.220 35.484 1.00 32.31 ? 178 GLU A C 1 ATOM 1402 O O . GLU A 1 178 ? 2.163 -14.094 35.700 1.00 31.85 ? 178 GLU A O 1 ATOM 1403 C CB . GLU A 1 178 ? 3.552 -16.672 34.923 1.00 33.52 ? 178 GLU A CB 1 ATOM 1404 C CG . GLU A 1 178 ? 4.032 -18.100 35.237 1.00 34.30 ? 178 GLU A CG 1 ATOM 1405 C CD . GLU A 1 178 ? 5.515 -18.364 34.948 1.00 36.34 ? 178 GLU A CD 1 ATOM 1406 O OE1 . GLU A 1 178 ? 6.164 -17.526 34.286 1.00 38.53 ? 178 GLU A OE1 1 ATOM 1407 O OE2 . GLU A 1 178 ? 6.036 -19.428 35.377 1.00 36.58 ? 178 GLU A OE2 1 ATOM 1408 N N . GLN A 1 179 ? 4.110 -13.254 34.952 1.00 30.81 ? 179 GLN A N 1 ATOM 1409 C CA . GLN A 1 179 ? 3.548 -11.957 34.566 1.00 29.50 ? 179 GLN A CA 1 ATOM 1410 C C . GLN A 1 179 ? 2.653 -12.054 33.354 1.00 29.14 ? 179 GLN A C 1 ATOM 1411 O O . GLN A 1 179 ? 2.787 -12.963 32.543 1.00 29.06 ? 179 GLN A O 1 ATOM 1412 C CB . GLN A 1 179 ? 4.645 -10.917 34.333 1.00 28.66 ? 179 GLN A CB 1 ATOM 1413 C CG . GLN A 1 179 ? 5.275 -10.431 35.629 1.00 27.49 ? 179 GLN A CG 1 ATOM 1414 C CD . GLN A 1 179 ? 6.199 -11.473 36.276 1.00 26.32 ? 179 GLN A CD 1 ATOM 1415 O OE1 . GLN A 1 179 ? 6.848 -12.263 35.583 1.00 26.73 ? 179 GLN A OE1 1 ATOM 1416 N NE2 . GLN A 1 179 ? 6.258 -11.473 37.603 1.00 25.45 ? 179 GLN A NE2 1 ATOM 1417 N N . ILE A 1 180 ? 1.741 -11.099 33.251 1.00 29.07 ? 180 ILE A N 1 ATOM 1418 C CA . ILE A 1 180 ? 0.738 -11.038 32.185 1.00 29.26 ? 180 ILE A CA 1 ATOM 1419 C C . ILE A 1 180 ? 1.222 -10.183 31.014 1.00 28.54 ? 180 ILE A C 1 ATOM 1420 O O . ILE A 1 180 ? 1.950 -9.213 31.197 1.00 28.29 ? 180 ILE A O 1 ATOM 1421 C CB . ILE A 1 180 ? -0.612 -10.467 32.736 1.00 29.35 ? 180 ILE A CB 1 ATOM 1422 C CG1 . ILE A 1 180 ? -1.265 -11.457 33.697 1.00 30.49 ? 180 ILE A CG1 1 ATOM 1423 C CG2 . ILE A 1 180 ? -1.606 -10.162 31.624 1.00 30.08 ? 180 ILE A CG2 1 ATOM 1424 C CD1 . ILE A 1 180 ? -2.172 -10.798 34.738 1.00 33.59 ? 180 ILE A CD1 1 ATOM 1425 N N . ASN A 1 181 ? 0.815 -10.570 29.810 1.00 28.37 ? 181 ASN A N 1 ATOM 1426 C CA . ASN A 1 181 ? 0.916 -9.711 28.639 1.00 27.88 ? 181 ASN A CA 1 ATOM 1427 C C . ASN A 1 181 ? -0.507 -9.303 28.266 1.00 27.61 ? 181 ASN A C 1 ATOM 1428 O O . ASN A 1 181 ? -1.293 -10.116 27.779 1.00 27.32 ? 181 ASN A O 1 ATOM 1429 C CB . ASN A 1 181 ? 1.628 -10.456 27.501 1.00 27.90 ? 181 ASN A CB 1 ATOM 1430 C CG . ASN A 1 181 ? 1.934 -9.571 26.293 1.00 28.02 ? 181 ASN A CG 1 ATOM 1431 O OD1 . ASN A 1 181 ? 1.662 -8.370 26.289 1.00 29.10 ? 181 ASN A OD1 1 ATOM 1432 N ND2 . ASN A 1 181 ? 2.493 -10.179 25.251 1.00 27.48 ? 181 ASN A ND2 1 ATOM 1433 N N . ALA A 1 182 ? -0.832 -8.041 28.527 1.00 27.73 ? 182 ALA A N 1 ATOM 1434 C CA . ALA A 1 182 ? -2.181 -7.491 28.295 1.00 27.97 ? 182 ALA A CA 1 ATOM 1435 C C . ALA A 1 182 ? -2.465 -7.121 26.828 1.00 28.06 ? 182 ALA A C 1 ATOM 1436 O O . ALA A 1 182 ? -3.493 -6.512 26.506 1.00 28.01 ? 182 ALA A O 1 ATOM 1437 C CB . ALA A 1 182 ? -2.420 -6.293 29.210 1.00 27.71 ? 182 ALA A CB 1 ATOM 1438 N N . VAL A 1 183 ? -1.549 -7.505 25.946 1.00 28.33 ? 183 VAL A N 1 ATOM 1439 C CA . VAL A 1 183 ? -1.603 -7.125 24.538 1.00 28.64 ? 183 VAL A CA 1 ATOM 1440 C C . VAL A 1 183 ? -1.411 -8.398 23.682 1.00 28.18 ? 183 VAL A C 1 ATOM 1441 O O . VAL A 1 183 ? -0.964 -9.423 24.190 1.00 27.73 ? 183 VAL A O 1 ATOM 1442 C CB . VAL A 1 183 ? -0.555 -5.990 24.266 1.00 29.20 ? 183 VAL A CB 1 ATOM 1443 C CG1 . VAL A 1 183 ? -0.388 -5.706 22.804 1.00 30.63 ? 183 VAL A CG1 1 ATOM 1444 C CG2 . VAL A 1 183 ? -0.968 -4.696 24.978 1.00 29.55 ? 183 VAL A CG2 1 ATOM 1445 N N . THR A 1 184 ? -1.786 -8.359 22.408 1.00 28.08 ? 184 THR A N 1 ATOM 1446 C CA . THR A 1 184 ? -1.596 -9.532 21.545 1.00 27.89 ? 184 THR A CA 1 ATOM 1447 C C . THR A 1 184 ? -0.145 -9.630 21.104 1.00 27.73 ? 184 THR A C 1 ATOM 1448 O O . THR A 1 184 ? 0.501 -8.617 20.853 1.00 27.97 ? 184 THR A O 1 ATOM 1449 C CB . THR A 1 184 ? -2.526 -9.537 20.310 1.00 27.79 ? 184 THR A CB 1 ATOM 1450 O OG1 . THR A 1 184 ? -2.129 -8.511 19.402 1.00 28.64 ? 184 THR A OG1 1 ATOM 1451 C CG2 . THR A 1 184 ? -3.969 -9.303 20.710 1.00 27.86 ? 184 THR A CG2 1 ATOM 1452 N N . SER A 1 185 ? 0.359 -10.857 21.029 1.00 28.01 ? 185 SER A N 1 ATOM 1453 C CA . SER A 1 185 ? 1.741 -11.141 20.645 1.00 27.75 ? 185 SER A CA 1 ATOM 1454 C C . SER A 1 185 ? 2.015 -10.928 19.163 1.00 27.92 ? 185 SER A C 1 ATOM 1455 O O . SER A 1 185 ? 3.161 -10.761 18.770 1.00 28.62 ? 185 SER A O 1 ATOM 1456 C CB . SER A 1 185 ? 2.112 -12.570 21.035 1.00 28.02 ? 185 SER A CB 1 ATOM 1457 O OG . SER A 1 185 ? 2.283 -12.691 22.432 1.00 26.72 ? 185 SER A OG 1 ATOM 1458 N N . PHE A 1 186 ? 0.971 -10.919 18.343 1.00 27.77 ? 186 PHE A N 1 ATOM 1459 C CA . PHE A 1 186 ? 1.118 -10.696 16.900 1.00 27.49 ? 186 PHE A CA 1 ATOM 1460 C C . PHE A 1 186 ? 1.356 -9.226 16.554 1.00 28.33 ? 186 PHE A C 1 ATOM 1461 O O . PHE A 1 186 ? 0.775 -8.321 17.187 1.00 28.35 ? 186 PHE A O 1 ATOM 1462 C CB . PHE A 1 186 ? -0.106 -11.253 16.163 1.00 26.75 ? 186 PHE A CB 1 ATOM 1463 C CG . PHE A 1 186 ? -0.437 -12.655 16.575 1.00 24.52 ? 186 PHE A CG 1 ATOM 1464 C CD1 . PHE A 1 186 ? -1.459 -12.903 17.485 1.00 22.17 ? 186 PHE A CD1 1 ATOM 1465 C CD2 . PHE A 1 186 ? 0.326 -13.721 16.116 1.00 21.32 ? 186 PHE A CD2 1 ATOM 1466 C CE1 . PHE A 1 186 ? -1.732 -14.191 17.902 1.00 20.73 ? 186 PHE A CE1 1 ATOM 1467 C CE2 . PHE A 1 186 ? 0.053 -15.011 16.525 1.00 20.71 ? 186 PHE A CE2 1 ATOM 1468 C CZ . PHE A 1 186 ? -0.970 -15.246 17.421 1.00 20.44 ? 186 PHE A CZ 1 ATOM 1469 N N . LEU A 1 187 ? 2.251 -8.995 15.588 1.00 28.50 ? 187 LEU A N 1 ATOM 1470 C CA . LEU A 1 187 ? 2.396 -7.685 14.977 1.00 28.70 ? 187 LEU A CA 1 ATOM 1471 C C . LEU A 1 187 ? 1.124 -7.445 14.193 1.00 28.77 ? 187 LEU A C 1 ATOM 1472 O O . LEU A 1 187 ? 1.012 -7.880 13.037 1.00 28.83 ? 187 LEU A O 1 ATOM 1473 C CB . LEU A 1 187 ? 3.580 -7.651 14.016 1.00 29.21 ? 187 LEU A CB 1 ATOM 1474 C CG . LEU A 1 187 ? 4.704 -6.645 14.254 1.00 29.76 ? 187 LEU A CG 1 ATOM 1475 C CD1 . LEU A 1 187 ? 5.571 -6.481 13.006 1.00 28.93 ? 187 LEU A CD1 1 ATOM 1476 C CD2 . LEU A 1 187 ? 4.120 -5.328 14.665 1.00 30.73 ? 187 LEU A CD2 1 ATOM 1477 N N . ASP A 1 188 ? 0.171 -6.759 14.819 1.00 28.45 ? 188 ASP A N 1 ATOM 1478 C CA . ASP A 1 188 ? -1.182 -6.683 14.279 1.00 28.24 ? 188 ASP A CA 1 ATOM 1479 C C . ASP A 1 188 ? -1.860 -5.329 14.484 1.00 27.89 ? 188 ASP A C 1 ATOM 1480 O O . ASP A 1 188 ? -3.081 -5.218 14.326 1.00 27.58 ? 188 ASP A O 1 ATOM 1481 C CB . ASP A 1 188 ? -2.044 -7.812 14.866 1.00 28.32 ? 188 ASP A CB 1 ATOM 1482 C CG . ASP A 1 188 ? -2.234 -7.696 16.375 1.00 28.36 ? 188 ASP A CG 1 ATOM 1483 O OD1 . ASP A 1 188 ? -1.621 -6.815 16.997 1.00 28.75 ? 188 ASP A OD1 1 ATOM 1484 O OD2 . ASP A 1 188 ? -2.995 -8.497 16.954 1.00 29.73 ? 188 ASP A OD2 1 ATOM 1485 N N . ALA A 1 189 ? -1.068 -4.311 14.819 1.00 27.39 ? 189 ALA A N 1 ATOM 1486 C CA . ALA A 1 189 ? -1.588 -2.953 15.052 1.00 27.62 ? 189 ALA A CA 1 ATOM 1487 C C . ALA A 1 189 ? -2.607 -2.908 16.200 1.00 27.77 ? 189 ALA A C 1 ATOM 1488 O O . ALA A 1 189 ? -3.528 -2.075 16.206 1.00 27.80 ? 189 ALA A O 1 ATOM 1489 C CB . ALA A 1 189 ? -2.180 -2.356 13.771 1.00 27.24 ? 189 ALA A CB 1 ATOM 1490 N N . SER A 1 190 ? -2.435 -3.819 17.162 1.00 27.61 ? 190 SER A N 1 ATOM 1491 C CA . SER A 1 190 ? -3.274 -3.857 18.359 1.00 27.51 ? 190 SER A CA 1 ATOM 1492 C C . SER A 1 190 ? -3.200 -2.545 19.138 1.00 27.53 ? 190 SER A C 1 ATOM 1493 O O . SER A 1 190 ? -4.071 -2.252 19.951 1.00 28.02 ? 190 SER A O 1 ATOM 1494 C CB . SER A 1 190 ? -2.902 -5.040 19.266 1.00 27.65 ? 190 SER A CB 1 ATOM 1495 O OG . SER A 1 190 ? -1.491 -5.144 19.477 1.00 26.01 ? 190 SER A OG 1 ATOM 1496 N N . LEU A 1 191 ? -2.163 -1.756 18.880 1.00 27.35 ? 191 LEU A N 1 ATOM 1497 C CA . LEU A 1 191 ? -1.996 -0.488 19.566 1.00 27.42 ? 191 LEU A CA 1 ATOM 1498 C C . LEU A 1 191 ? -2.919 0.581 18.988 1.00 27.44 ? 191 LEU A C 1 ATOM 1499 O O . LEU A 1 191 ? -3.131 1.600 19.622 1.00 27.43 ? 191 LEU A O 1 ATOM 1500 C CB . LEU A 1 191 ? -0.519 -0.045 19.568 1.00 27.46 ? 191 LEU A CB 1 ATOM 1501 C CG . LEU A 1 191 ? 0.122 0.672 18.382 1.00 27.64 ? 191 LEU A CG 1 ATOM 1502 C CD1 . LEU A 1 191 ? 1.424 1.247 18.833 1.00 27.63 ? 191 LEU A CD1 1 ATOM 1503 C CD2 . LEU A 1 191 ? 0.335 -0.253 17.197 1.00 29.32 ? 191 LEU A CD2 1 ATOM 1504 N N . VAL A 1 192 ? -3.472 0.321 17.797 1.00 27.69 ? 192 VAL A N 1 ATOM 1505 C CA . VAL A 1 192 ? -4.410 1.223 17.119 1.00 27.91 ? 192 VAL A CA 1 ATOM 1506 C C . VAL A 1 192 ? -5.844 0.791 17.408 1.00 28.19 ? 192 VAL A C 1 ATOM 1507 O O . VAL A 1 192 ? -6.719 1.624 17.684 1.00 28.48 ? 192 VAL A O 1 ATOM 1508 C CB . VAL A 1 192 ? -4.214 1.215 15.579 1.00 28.02 ? 192 VAL A CB 1 ATOM 1509 C CG1 . VAL A 1 192 ? -5.234 2.108 14.878 1.00 28.17 ? 192 VAL A CG1 1 ATOM 1510 C CG2 . VAL A 1 192 ? -2.825 1.639 15.218 1.00 28.60 ? 192 VAL A CG2 1 ATOM 1511 N N . TYR A 1 193 ? -6.086 -0.516 17.359 1.00 28.09 ? 193 TYR A N 1 ATOM 1512 C CA . TYR A 1 193 ? -7.453 -1.023 17.456 1.00 27.65 ? 193 TYR A CA 1 ATOM 1513 C C . TYR A 1 193 ? -7.889 -1.512 18.839 1.00 27.69 ? 193 TYR A C 1 ATOM 1514 O O . TYR A 1 193 ? -9.084 -1.654 19.080 1.00 28.06 ? 193 TYR A O 1 ATOM 1515 C CB . TYR A 1 193 ? -7.690 -2.082 16.388 1.00 27.04 ? 193 TYR A CB 1 ATOM 1516 C CG . TYR A 1 193 ? -7.433 -1.538 15.012 1.00 26.94 ? 193 TYR A CG 1 ATOM 1517 C CD1 . TYR A 1 193 ? -6.234 -1.811 14.346 1.00 26.82 ? 193 TYR A CD1 1 ATOM 1518 C CD2 . TYR A 1 193 ? -8.376 -0.716 14.382 1.00 25.52 ? 193 TYR A CD2 1 ATOM 1519 C CE1 . TYR A 1 193 ? -5.995 -1.298 13.082 1.00 25.98 ? 193 TYR A CE1 1 ATOM 1520 C CE2 . TYR A 1 193 ? -8.142 -0.195 13.139 1.00 23.85 ? 193 TYR A CE2 1 ATOM 1521 C CZ . TYR A 1 193 ? -6.961 -0.490 12.489 1.00 25.85 ? 193 TYR A CZ 1 ATOM 1522 O OH . TYR A 1 193 ? -6.735 0.034 11.241 1.00 27.03 ? 193 TYR A OH 1 ATOM 1523 N N . GLY A 1 194 ? -6.939 -1.753 19.738 1.00 27.38 ? 194 GLY A N 1 ATOM 1524 C CA . GLY A 1 194 ? -7.256 -2.271 21.064 1.00 27.50 ? 194 GLY A CA 1 ATOM 1525 C C . GLY A 1 194 ? -6.977 -3.751 21.090 1.00 27.70 ? 194 GLY A C 1 ATOM 1526 O O . GLY A 1 194 ? -6.781 -4.346 20.034 1.00 27.91 ? 194 GLY A O 1 ATOM 1527 N N . SER A 1 195 ? -6.955 -4.338 22.289 1.00 27.94 ? 195 SER A N 1 ATOM 1528 C CA . SER A 1 195 ? -6.686 -5.774 22.500 1.00 28.64 ? 195 SER A CA 1 ATOM 1529 C C . SER A 1 195 ? -7.857 -6.463 23.170 1.00 29.26 ? 195 SER A C 1 ATOM 1530 O O . SER A 1 195 ? -7.842 -7.677 23.390 1.00 28.43 ? 195 SER A O 1 ATOM 1531 C CB . SER A 1 195 ? -5.434 -5.986 23.374 1.00 28.12 ? 195 SER A CB 1 ATOM 1532 O OG . SER A 1 195 ? -4.260 -5.980 22.593 1.00 27.55 ? 195 SER A OG 1 ATOM 1533 N N . GLU A 1 196 ? -8.852 -5.659 23.511 1.00 30.77 ? 196 GLU A N 1 ATOM 1534 C CA . GLU A 1 196 ? -10.064 -6.120 24.162 1.00 33.03 ? 196 GLU A CA 1 ATOM 1535 C C . GLU A 1 196 ? -11.269 -5.729 23.319 1.00 33.74 ? 196 GLU A C 1 ATOM 1536 O O . GLU A 1 196 ? -11.277 -4.639 22.713 1.00 33.70 ? 196 GLU A O 1 ATOM 1537 C CB . GLU A 1 196 ? -10.183 -5.480 25.533 1.00 33.27 ? 196 GLU A CB 1 ATOM 1538 C CG . GLU A 1 196 ? -9.148 -5.967 26.529 1.00 37.38 ? 196 GLU A CG 1 ATOM 1539 C CD . GLU A 1 196 ? -9.131 -5.130 27.784 1.00 41.98 ? 196 GLU A CD 1 ATOM 1540 O OE1 . GLU A 1 196 ? -8.805 -3.914 27.701 1.00 44.73 ? 196 GLU A OE1 1 ATOM 1541 O OE2 . GLU A 1 196 ? -9.449 -5.690 28.853 1.00 44.42 ? 196 GLU A OE2 1 ATOM 1542 N N . PRO A 1 197 ? -12.296 -6.607 23.274 1.00 34.43 ? 197 PRO A N 1 ATOM 1543 C CA . PRO A 1 197 ? -13.496 -6.298 22.498 1.00 34.84 ? 197 PRO A CA 1 ATOM 1544 C C . PRO A 1 197 ? -14.158 -5.038 23.050 1.00 35.19 ? 197 PRO A C 1 ATOM 1545 O O . PRO A 1 197 ? -14.676 -4.214 22.300 1.00 35.00 ? 197 PRO A O 1 ATOM 1546 C CB . PRO A 1 197 ? -14.388 -7.525 22.737 1.00 35.02 ? 197 PRO A CB 1 ATOM 1547 C CG . PRO A 1 197 ? -13.459 -8.605 23.129 1.00 34.66 ? 197 PRO A CG 1 ATOM 1548 C CD . PRO A 1 197 ? -12.407 -7.919 23.936 1.00 34.17 ? 197 PRO A CD 1 HETATM 1549 N N . SEP A 1 198 ? -14.109 -4.912 24.371 1.00 35.73 ? 198 SEP A N 1 HETATM 1550 C CA . SEP A 1 198 ? -14.604 -3.763 25.101 1.00 36.51 ? 198 SEP A CA 1 HETATM 1551 C CB . SEP A 1 198 ? -14.192 -3.931 26.571 1.00 36.53 ? 198 SEP A CB 1 HETATM 1552 O OG . SEP A 1 198 ? -14.737 -5.154 27.119 1.00 41.00 ? 198 SEP A OG 1 HETATM 1553 C C . SEP A 1 198 ? -14.064 -2.451 24.480 1.00 36.76 ? 198 SEP A C 1 HETATM 1554 O O . SEP A 1 198 ? -14.829 -1.633 23.934 1.00 36.71 ? 198 SEP A O 1 HETATM 1555 P P . SEP A 1 198 ? -13.785 -6.492 27.352 1.00 37.18 ? 198 SEP A P 1 HETATM 1556 O O1P . SEP A 1 198 ? -13.406 -6.701 28.894 1.00 40.01 ? 198 SEP A O1P 1 HETATM 1557 O O2P . SEP A 1 198 ? -12.487 -6.362 26.435 1.00 42.81 ? 198 SEP A O2P 1 HETATM 1558 O O3P . SEP A 1 198 ? -14.593 -7.769 26.882 1.00 41.98 ? 198 SEP A O3P 1 ATOM 1559 N N . LEU A 1 199 ? -12.740 -2.282 24.525 1.00 36.58 ? 199 LEU A N 1 ATOM 1560 C CA . LEU A 1 199 ? -12.087 -1.069 24.059 1.00 36.16 ? 199 LEU A CA 1 ATOM 1561 C C . LEU A 1 199 ? -12.182 -0.902 22.544 1.00 36.22 ? 199 LEU A C 1 ATOM 1562 O O . LEU A 1 199 ? -12.409 0.210 22.062 1.00 35.78 ? 199 LEU A O 1 ATOM 1563 C CB . LEU A 1 199 ? -10.632 -1.042 24.539 1.00 36.03 ? 199 LEU A CB 1 ATOM 1564 C CG . LEU A 1 199 ? -9.636 0.015 24.062 1.00 35.41 ? 199 LEU A CG 1 ATOM 1565 C CD1 . LEU A 1 199 ? -10.055 1.413 24.490 1.00 35.26 ? 199 LEU A CD1 1 ATOM 1566 C CD2 . LEU A 1 199 ? -8.248 -0.322 24.609 1.00 35.63 ? 199 LEU A CD2 1 ATOM 1567 N N . ALA A 1 200 ? -12.022 -2.004 21.807 1.00 36.20 ? 200 ALA A N 1 ATOM 1568 C CA . ALA A 1 200 ? -12.075 -1.981 20.342 1.00 36.69 ? 200 ALA A CA 1 ATOM 1569 C C . ALA A 1 200 ? -13.330 -1.289 19.829 1.00 37.41 ? 200 ALA A C 1 ATOM 1570 O O . ALA A 1 200 ? -13.267 -0.490 18.884 1.00 37.40 ? 200 ALA A O 1 ATOM 1571 C CB . ALA A 1 200 ? -11.979 -3.395 19.773 1.00 36.65 ? 200 ALA A CB 1 ATOM 1572 N N . SER A 1 201 ? -14.461 -1.590 20.465 1.00 37.99 ? 201 SER A N 1 ATOM 1573 C CA . SER A 1 201 ? -15.736 -0.992 20.093 1.00 38.87 ? 201 SER A CA 1 ATOM 1574 C C . SER A 1 201 ? -15.796 0.514 20.396 1.00 39.13 ? 201 SER A C 1 ATOM 1575 O O . SER A 1 201 ? -16.158 1.301 19.520 1.00 39.45 ? 201 SER A O 1 ATOM 1576 C CB . SER A 1 201 ? -16.895 -1.739 20.755 1.00 38.89 ? 201 SER A CB 1 ATOM 1577 O OG . SER A 1 201 ? -18.037 -0.906 20.827 1.00 40.25 ? 201 SER A OG 1 ATOM 1578 N N . ARG A 1 202 ? -15.416 0.899 21.647 1.00 38.66 ? 202 ARG A N 1 ATOM 1579 C CA . ARG A 1 202 ? -15.365 2.311 22.034 1.00 39.02 ? 202 ARG A CA 1 ATOM 1580 C C . ARG A 1 202 ? -14.631 3.132 20.997 1.00 39.03 ? 202 ARG A C 1 ATOM 1581 O O . ARG A 1 202 ? -15.064 4.220 20.620 1.00 39.87 ? 202 ARG A O 1 ATOM 1582 C CB . ARG A 1 202 ? -14.677 2.556 23.402 1.00 39.18 ? 202 ARG A CB 1 ATOM 1583 C CG . ARG A 1 202 ? -15.374 3.698 24.156 1.00 41.01 ? 202 ARG A CG 1 ATOM 1584 C CD . ARG A 1 202 ? -14.449 4.607 24.961 1.00 44.44 ? 202 ARG A CD 1 ATOM 1585 N NE . ARG A 1 202 ? -14.344 4.157 26.349 1.00 47.91 ? 202 ARG A NE 1 ATOM 1586 C CZ . ARG A 1 202 ? -13.728 4.771 27.364 1.00 49.79 ? 202 ARG A CZ 1 ATOM 1587 N NH1 . ARG A 1 202 ? -13.153 5.957 27.172 1.00 49.98 ? 202 ARG A NH1 1 ATOM 1588 N NH2 . ARG A 1 202 ? -13.695 4.200 28.551 1.00 49.49 ? 202 ARG A NH2 1 ATOM 1589 N N . LEU A 1 203 ? -13.481 2.603 20.550 1.00 39.60 ? 203 LEU A N 1 ATOM 1590 C CA . LEU A 1 203 ? -12.616 3.278 19.587 1.00 39.34 ? 203 LEU A CA 1 ATOM 1591 C C . LEU A 1 203 ? -13.294 3.552 18.249 1.00 39.59 ? 203 LEU A C 1 ATOM 1592 O O . LEU A 1 203 ? -12.940 4.502 17.564 1.00 39.42 ? 203 LEU A O 1 ATOM 1593 C CB . LEU A 1 203 ? -11.337 2.459 19.373 1.00 38.92 ? 203 LEU A CB 1 ATOM 1594 C CG . LEU A 1 203 ? -10.079 2.692 20.223 1.00 37.72 ? 203 LEU A CG 1 ATOM 1595 C CD1 . LEU A 1 203 ? -10.257 3.615 21.414 1.00 35.86 ? 203 LEU A CD1 1 ATOM 1596 C CD2 . LEU A 1 203 ? -9.554 1.354 20.655 1.00 36.96 ? 203 LEU A CD2 1 ATOM 1597 N N . GLN A 1 204 ? -14.260 2.710 17.887 1.00 40.47 ? 204 GLN A N 1 ATOM 1598 C CA . GLN A 1 204 ? -14.910 2.775 16.575 1.00 41.25 ? 204 GLN A CA 1 ATOM 1599 C C . GLN A 1 204 ? -15.975 3.865 16.490 1.00 41.80 ? 204 GLN A C 1 ATOM 1600 O O . GLN A 1 204 ? -16.552 4.266 17.499 1.00 41.47 ? 204 GLN A O 1 ATOM 1601 C CB . GLN A 1 204 ? -15.567 1.439 16.230 1.00 41.36 ? 204 GLN A CB 1 ATOM 1602 C CG . GLN A 1 204 ? -14.633 0.311 15.862 1.00 41.17 ? 204 GLN A CG 1 ATOM 1603 C CD . GLN A 1 204 ? -15.383 -0.857 15.221 1.00 41.03 ? 204 GLN A CD 1 ATOM 1604 O OE1 . GLN A 1 204 ? -15.883 -0.748 14.101 1.00 40.08 ? 204 GLN A OE1 1 ATOM 1605 N NE2 . GLN A 1 204 ? -15.460 -1.977 15.932 1.00 40.89 ? 204 GLN A NE2 1 ATOM 1606 N N . ASN A 1 205 ? -16.222 4.324 15.264 1.00 42.94 ? 205 ASN A N 1 ATOM 1607 C CA . ASN A 1 205 ? -17.329 5.231 14.956 1.00 44.40 ? 205 ASN A CA 1 ATOM 1608 C C . ASN A 1 205 ? -18.521 4.420 14.446 1.00 44.30 ? 205 ASN A C 1 ATOM 1609 O O . ASN A 1 205 ? -18.602 4.046 13.261 1.00 44.32 ? 205 ASN A O 1 ATOM 1610 C CB . ASN A 1 205 ? -16.889 6.295 13.929 1.00 45.02 ? 205 ASN A CB 1 ATOM 1611 C CG . ASN A 1 205 ? -17.948 7.375 13.692 1.00 47.50 ? 205 ASN A CG 1 ATOM 1612 O OD1 . ASN A 1 205 ? -19.152 7.142 13.841 1.00 49.07 ? 205 ASN A OD1 1 ATOM 1613 N ND2 . ASN A 1 205 ? -17.486 8.568 13.302 1.00 50.76 ? 205 ASN A ND2 1 ATOM 1614 N N . LEU A 1 206 ? -19.448 4.134 15.344 1.00 44.68 ? 206 LEU A N 1 ATOM 1615 C CA . LEU A 1 206 ? -20.600 3.315 15.008 1.00 45.05 ? 206 LEU A CA 1 ATOM 1616 C C . LEU A 1 206 ? -21.870 4.155 14.780 1.00 45.49 ? 206 LEU A C 1 ATOM 1617 O O . LEU A 1 206 ? -22.974 3.620 14.706 1.00 45.48 ? 206 LEU A O 1 ATOM 1618 C CB . LEU A 1 206 ? -20.807 2.261 16.098 1.00 44.97 ? 206 LEU A CB 1 ATOM 1619 C CG . LEU A 1 206 ? -19.666 1.271 16.339 1.00 44.22 ? 206 LEU A CG 1 ATOM 1620 C CD1 . LEU A 1 206 ? -20.016 0.339 17.495 1.00 43.18 ? 206 LEU A CD1 1 ATOM 1621 C CD2 . LEU A 1 206 ? -19.358 0.483 15.073 1.00 43.20 ? 206 LEU A CD2 1 ATOM 1622 N N . SER A 1 207 ? -21.695 5.473 14.672 1.00 45.98 ? 207 SER A N 1 ATOM 1623 C CA . SER A 1 207 ? -22.784 6.393 14.359 1.00 46.40 ? 207 SER A CA 1 ATOM 1624 C C . SER A 1 207 ? -23.113 6.337 12.871 1.00 46.76 ? 207 SER A C 1 ATOM 1625 O O . SER A 1 207 ? -24.232 6.685 12.468 1.00 47.18 ? 207 SER A O 1 ATOM 1626 C CB . SER A 1 207 ? -22.400 7.836 14.715 1.00 46.42 ? 207 SER A CB 1 ATOM 1627 O OG . SER A 1 207 ? -21.849 7.939 16.016 1.00 46.41 ? 207 SER A OG 1 ATOM 1628 N N . SER A 1 208 ? -22.131 5.922 12.063 1.00 46.74 ? 208 SER A N 1 ATOM 1629 C CA . SER A 1 208 ? -22.254 5.895 10.600 1.00 46.69 ? 208 SER A CA 1 ATOM 1630 C C . SER A 1 208 ? -21.629 4.624 10.005 1.00 46.31 ? 208 SER A C 1 ATOM 1631 O O . SER A 1 208 ? -20.709 4.069 10.588 1.00 46.32 ? 208 SER A O 1 ATOM 1632 C CB . SER A 1 208 ? -21.613 7.145 9.997 1.00 46.74 ? 208 SER A CB 1 ATOM 1633 O OG . SER A 1 208 ? -20.232 7.203 10.295 1.00 47.87 ? 208 SER A OG 1 ATOM 1634 N N . PRO A 1 209 ? -22.130 4.161 8.839 1.00 46.04 ? 209 PRO A N 1 ATOM 1635 C CA . PRO A 1 209 ? -21.724 2.862 8.295 1.00 45.55 ? 209 PRO A CA 1 ATOM 1636 C C . PRO A 1 209 ? -20.453 2.921 7.439 1.00 45.14 ? 209 PRO A C 1 ATOM 1637 O O . PRO A 1 209 ? -20.352 2.219 6.417 1.00 45.33 ? 209 PRO A O 1 ATOM 1638 C CB . PRO A 1 209 ? -22.917 2.497 7.411 1.00 45.69 ? 209 PRO A CB 1 ATOM 1639 C CG . PRO A 1 209 ? -23.351 3.817 6.848 1.00 45.59 ? 209 PRO A CG 1 ATOM 1640 C CD . PRO A 1 209 ? -23.114 4.827 7.957 1.00 46.18 ? 209 PRO A CD 1 ATOM 1641 N N . LEU A 1 210 ? -19.493 3.742 7.850 1.00 44.35 ? 210 LEU A N 1 ATOM 1642 C CA . LEU A 1 210 ? -18.335 4.023 7.004 1.00 43.76 ? 210 LEU A CA 1 ATOM 1643 C C . LEU A 1 210 ? -17.061 3.315 7.473 1.00 43.12 ? 210 LEU A C 1 ATOM 1644 O O . LEU A 1 210 ? -16.035 3.363 6.794 1.00 43.10 ? 210 LEU A O 1 ATOM 1645 C CB . LEU A 1 210 ? -18.123 5.548 6.869 1.00 44.21 ? 210 LEU A CB 1 ATOM 1646 C CG . LEU A 1 210 ? -19.337 6.418 6.472 1.00 44.04 ? 210 LEU A CG 1 ATOM 1647 C CD1 . LEU A 1 210 ? -19.206 7.837 7.023 1.00 43.73 ? 210 LEU A CD1 1 ATOM 1648 C CD2 . LEU A 1 210 ? -19.590 6.431 4.963 1.00 43.58 ? 210 LEU A CD2 1 ATOM 1649 N N . GLY A 1 211 ? -17.140 2.657 8.630 1.00 42.64 ? 211 GLY A N 1 ATOM 1650 C CA . GLY A 1 211 ? -16.029 1.873 9.175 1.00 41.93 ? 211 GLY A CA 1 ATOM 1651 C C . GLY A 1 211 ? -14.886 2.726 9.693 1.00 41.52 ? 211 GLY A C 1 ATOM 1652 O O . GLY A 1 211 ? -13.726 2.309 9.686 1.00 41.46 ? 211 GLY A O 1 ATOM 1653 N N . LEU A 1 212 ? -15.224 3.931 10.134 1.00 41.08 ? 212 LEU A N 1 ATOM 1654 C CA . LEU A 1 212 ? -14.243 4.872 10.630 1.00 40.53 ? 212 LEU A CA 1 ATOM 1655 C C . LEU A 1 212 ? -13.997 4.672 12.128 1.00 40.39 ? 212 LEU A C 1 ATOM 1656 O O . LEU A 1 212 ? -14.835 4.116 12.853 1.00 39.77 ? 212 LEU A O 1 ATOM 1657 C CB . LEU A 1 212 ? -14.690 6.315 10.340 1.00 40.57 ? 212 LEU A CB 1 ATOM 1658 C CG . LEU A 1 212 ? -14.903 6.747 8.877 1.00 40.80 ? 212 LEU A CG 1 ATOM 1659 C CD1 . LEU A 1 212 ? -15.430 8.172 8.800 1.00 39.77 ? 212 LEU A CD1 1 ATOM 1660 C CD2 . LEU A 1 212 ? -13.642 6.596 8.015 1.00 40.77 ? 212 LEU A CD2 1 ATOM 1661 N N . MET A 1 213 ? -12.822 5.116 12.565 1.00 40.25 ? 213 MET A N 1 ATOM 1662 C CA . MET A 1 213 ? -12.479 5.175 13.967 1.00 40.14 ? 213 MET A CA 1 ATOM 1663 C C . MET A 1 213 ? -12.955 6.521 14.489 1.00 40.07 ? 213 MET A C 1 ATOM 1664 O O . MET A 1 213 ? -12.971 7.501 13.752 1.00 39.97 ? 213 MET A O 1 ATOM 1665 C CB . MET A 1 213 ? -10.962 5.044 14.145 1.00 40.35 ? 213 MET A CB 1 ATOM 1666 C CG . MET A 1 213 ? -10.355 3.695 13.701 1.00 40.24 ? 213 MET A CG 1 ATOM 1667 S SD . MET A 1 213 ? -10.712 2.361 14.866 1.00 39.16 ? 213 MET A SD 1 ATOM 1668 C CE . MET A 1 213 ? -9.655 2.832 16.241 1.00 40.35 ? 213 MET A CE 1 ATOM 1669 N N . ALA A 1 214 ? -13.347 6.554 15.760 1.00 40.32 ? 214 ALA A N 1 ATOM 1670 C CA . ALA A 1 214 ? -13.761 7.781 16.431 1.00 40.41 ? 214 ALA A CA 1 ATOM 1671 C C . ALA A 1 214 ? -12.648 8.812 16.380 1.00 40.68 ? 214 ALA A C 1 ATOM 1672 O O . ALA A 1 214 ? -11.475 8.490 16.579 1.00 40.51 ? 214 ALA A O 1 ATOM 1673 C CB . ALA A 1 214 ? -14.151 7.498 17.872 1.00 40.24 ? 214 ALA A CB 1 ATOM 1674 N N . VAL A 1 215 ? -13.024 10.050 16.084 1.00 41.02 ? 215 VAL A N 1 ATOM 1675 C CA . VAL A 1 215 ? -12.080 11.162 16.072 1.00 41.16 ? 215 VAL A CA 1 ATOM 1676 C C . VAL A 1 215 ? -12.512 12.234 17.081 1.00 41.64 ? 215 VAL A C 1 ATOM 1677 O O . VAL A 1 215 ? -13.704 12.388 17.371 1.00 41.74 ? 215 VAL A O 1 ATOM 1678 C CB . VAL A 1 215 ? -11.913 11.766 14.651 1.00 41.21 ? 215 VAL A CB 1 ATOM 1679 C CG1 . VAL A 1 215 ? -11.425 10.697 13.664 1.00 40.47 ? 215 VAL A CG1 1 ATOM 1680 C CG2 . VAL A 1 215 ? -13.212 12.399 14.154 1.00 40.76 ? 215 VAL A CG2 1 ATOM 1681 N N . ASN A 1 216 ? -11.539 12.951 17.635 1.00 41.87 ? 216 ASN A N 1 ATOM 1682 C CA . ASN A 1 216 ? -11.818 14.093 18.496 1.00 42.22 ? 216 ASN A CA 1 ATOM 1683 C C . ASN A 1 216 ? -12.806 15.047 17.805 1.00 42.60 ? 216 ASN A C 1 ATOM 1684 O O . ASN A 1 216 ? -12.740 15.261 16.584 1.00 42.00 ? 216 ASN A O 1 ATOM 1685 C CB . ASN A 1 216 ? -10.506 14.811 18.826 1.00 42.06 ? 216 ASN A CB 1 ATOM 1686 C CG . ASN A 1 216 ? -10.568 15.585 20.118 1.00 42.63 ? 216 ASN A CG 1 ATOM 1687 O OD1 . ASN A 1 216 ? -11.224 16.623 20.204 1.00 44.30 ? 216 ASN A OD1 1 ATOM 1688 N ND2 . ASN A 1 216 ? -9.856 15.104 21.131 1.00 43.22 ? 216 ASN A ND2 1 ATOM 1689 N N . GLN A 1 217 ? -13.797 15.510 18.665 1.00 43.37 ? 217 GLN A N 1 ATOM 1690 C CA . GLN A 1 217 ? -14.794 16.458 18.168 1.00 44.19 ? 217 GLN A CA 1 ATOM 1691 C C . GLN A 1 217 ? -14.512 17.886 18.632 1.00 44.48 ? 217 GLN A C 1 ATOM 1692 O O . GLN A 1 217 ? -14.927 18.838 17.973 1.00 44.40 ? 217 GLN A O 1 ATOM 1693 C CB . GLN A 1 217 ? -16.219 16.020 18.534 1.00 44.28 ? 217 GLN A CB 1 ATOM 1694 C CG . GLN A 1 217 ? -16.674 14.690 17.886 1.00 45.19 ? 217 GLN A CG 1 ATOM 1695 C CD . GLN A 1 217 ? -16.730 14.724 16.345 1.00 47.02 ? 217 GLN A CD 1 ATOM 1696 O OE1 . GLN A 1 217 ? -17.028 15.755 15.730 1.00 47.06 ? 217 GLN A OE1 1 ATOM 1697 N NE2 . GLN A 1 217 ? -16.458 13.582 15.725 1.00 46.92 ? 217 GLN A NE2 1 ATOM 1698 N N . GLU A 1 218 ? -13.787 18.026 19.744 1.00 44.87 ? 218 GLU A N 1 ATOM 1699 C CA . GLU A 1 218 ? -13.469 19.342 20.311 1.00 45.45 ? 218 GLU A CA 1 ATOM 1700 C C . GLU A 1 218 ? -12.374 20.133 19.582 1.00 45.34 ? 218 GLU A C 1 ATOM 1701 O O . GLU A 1 218 ? -12.333 21.361 19.704 1.00 45.51 ? 218 GLU A O 1 ATOM 1702 C CB . GLU A 1 218 ? -13.096 19.220 21.793 1.00 45.79 ? 218 GLU A CB 1 ATOM 1703 C CG . GLU A 1 218 ? -14.246 19.498 22.772 1.00 47.63 ? 218 GLU A CG 1 ATOM 1704 C CD . GLU A 1 218 ? -15.332 18.429 22.745 1.00 49.60 ? 218 GLU A CD 1 ATOM 1705 O OE1 . GLU A 1 218 ? -14.990 17.225 22.670 1.00 50.17 ? 218 GLU A OE1 1 ATOM 1706 O OE2 . GLU A 1 218 ? -16.529 18.795 22.807 1.00 49.90 ? 218 GLU A OE2 1 ATOM 1707 N N . ALA A 1 219 ? -11.490 19.443 18.846 1.00 45.06 ? 219 ALA A N 1 ATOM 1708 C CA . ALA A 1 219 ? -10.311 20.083 18.221 1.00 44.46 ? 219 ALA A CA 1 ATOM 1709 C C . ALA A 1 219 ? -9.860 19.429 16.915 1.00 44.25 ? 219 ALA A C 1 ATOM 1710 O O . ALA A 1 219 ? -9.959 18.210 16.755 1.00 43.96 ? 219 ALA A O 1 ATOM 1711 C CB . ALA A 1 219 ? -9.148 20.138 19.201 1.00 44.52 ? 219 ALA A CB 1 ATOM 1712 N N . TRP A 1 220 ? -9.354 20.259 16.000 1.00 43.83 ? 220 TRP A N 1 ATOM 1713 C CA . TRP A 1 220 ? -8.904 19.816 14.681 1.00 43.79 ? 220 TRP A CA 1 ATOM 1714 C C . TRP A 1 220 ? -7.479 20.282 14.341 1.00 43.32 ? 220 TRP A C 1 ATOM 1715 O O . TRP A 1 220 ? -6.955 21.215 14.949 1.00 43.47 ? 220 TRP A O 1 ATOM 1716 C CB . TRP A 1 220 ? -9.926 20.222 13.607 1.00 44.17 ? 220 TRP A CB 1 ATOM 1717 C CG . TRP A 1 220 ? -11.194 19.397 13.721 1.00 45.81 ? 220 TRP A CG 1 ATOM 1718 C CD1 . TRP A 1 220 ? -12.247 19.617 14.572 1.00 46.49 ? 220 TRP A CD1 1 ATOM 1719 C CD2 . TRP A 1 220 ? -11.508 18.195 12.995 1.00 46.70 ? 220 TRP A CD2 1 ATOM 1720 N NE1 . TRP A 1 220 ? -13.200 18.632 14.412 1.00 47.22 ? 220 TRP A NE1 1 ATOM 1721 C CE2 . TRP A 1 220 ? -12.773 17.748 13.454 1.00 47.29 ? 220 TRP A CE2 1 ATOM 1722 C CE3 . TRP A 1 220 ? -10.847 17.455 11.999 1.00 47.56 ? 220 TRP A CE3 1 ATOM 1723 C CZ2 . TRP A 1 220 ? -13.397 16.595 12.943 1.00 47.99 ? 220 TRP A CZ2 1 ATOM 1724 C CZ3 . TRP A 1 220 ? -11.470 16.305 11.491 1.00 47.80 ? 220 TRP A CZ3 1 ATOM 1725 C CH2 . TRP A 1 220 ? -12.731 15.891 11.967 1.00 47.49 ? 220 TRP A CH2 1 ATOM 1726 N N . ASP A 1 221 ? -6.847 19.599 13.397 1.00 42.81 ? 221 ASP A N 1 ATOM 1727 C CA . ASP A 1 221 ? -5.495 19.919 12.967 1.00 42.77 ? 221 ASP A CA 1 ATOM 1728 C C . ASP A 1 221 ? -5.560 20.239 11.486 1.00 42.73 ? 221 ASP A C 1 ATOM 1729 O O . ASP A 1 221 ? -5.388 19.352 10.639 1.00 42.17 ? 221 ASP A O 1 ATOM 1730 C CB . ASP A 1 221 ? -4.569 18.723 13.233 1.00 43.09 ? 221 ASP A CB 1 ATOM 1731 C CG . ASP A 1 221 ? -3.121 18.979 12.836 1.00 43.17 ? 221 ASP A CG 1 ATOM 1732 O OD1 . ASP A 1 221 ? -2.745 20.139 12.571 1.00 44.67 ? 221 ASP A OD1 1 ATOM 1733 O OD2 . ASP A 1 221 ? -2.344 18.004 12.797 1.00 42.68 ? 221 ASP A OD2 1 ATOM 1734 N N . HIS A 1 222 ? -5.832 21.512 11.189 1.00 42.94 ? 222 HIS A N 1 ATOM 1735 C CA . HIS A 1 222 ? -6.060 21.988 9.818 1.00 43.31 ? 222 HIS A CA 1 ATOM 1736 C C . HIS A 1 222 ? -7.012 21.089 9.034 1.00 42.93 ? 222 HIS A C 1 ATOM 1737 O O . HIS A 1 222 ? -6.716 20.721 7.896 1.00 43.16 ? 222 HIS A O 1 ATOM 1738 C CB . HIS A 1 222 ? -4.750 22.117 9.038 1.00 43.61 ? 222 HIS A CB 1 ATOM 1739 C CG . HIS A 1 222 ? -3.724 22.973 9.707 1.00 45.57 ? 222 HIS A CG 1 ATOM 1740 N ND1 . HIS A 1 222 ? -2.554 22.456 10.229 1.00 47.40 ? 222 HIS A ND1 1 ATOM 1741 C CD2 . HIS A 1 222 ? -3.680 24.312 9.925 1.00 46.89 ? 222 HIS A CD2 1 ATOM 1742 C CE1 . HIS A 1 222 ? -1.837 23.438 10.748 1.00 48.78 ? 222 HIS A CE1 1 ATOM 1743 N NE2 . HIS A 1 222 ? -2.496 24.575 10.575 1.00 48.52 ? 222 HIS A NE2 1 ATOM 1744 N N . GLY A 1 223 ? -8.143 20.732 9.642 1.00 42.53 ? 223 GLY A N 1 ATOM 1745 C CA . GLY A 1 223 ? -9.123 19.862 8.993 1.00 42.31 ? 223 GLY A CA 1 ATOM 1746 C C . GLY A 1 223 ? -8.709 18.403 8.935 1.00 42.31 ? 223 GLY A C 1 ATOM 1747 O O . GLY A 1 223 ? -9.376 17.592 8.290 1.00 42.54 ? 223 GLY A O 1 ATOM 1748 N N . LEU A 1 224 ? -7.590 18.074 9.594 1.00 42.09 ? 224 LEU A N 1 ATOM 1749 C CA . LEU A 1 224 ? -7.153 16.686 9.771 1.00 41.14 ? 224 LEU A CA 1 ATOM 1750 C C . LEU A 1 224 ? -7.446 16.278 11.210 1.00 40.30 ? 224 LEU A C 1 ATOM 1751 O O . LEU A 1 224 ? -7.504 17.128 12.091 1.00 40.13 ? 224 LEU A O 1 ATOM 1752 C CB . LEU A 1 224 ? -5.667 16.523 9.418 1.00 41.39 ? 224 LEU A CB 1 ATOM 1753 C CG . LEU A 1 224 ? -5.264 16.753 7.948 1.00 42.08 ? 224 LEU A CG 1 ATOM 1754 C CD1 . LEU A 1 224 ? -3.765 16.817 7.772 1.00 42.93 ? 224 LEU A CD1 1 ATOM 1755 C CD2 . LEU A 1 224 ? -5.838 15.711 7.006 1.00 42.50 ? 224 LEU A CD2 1 ATOM 1756 N N . ALA A 1 225 ? -7.642 14.983 11.436 1.00 39.34 ? 225 ALA A N 1 ATOM 1757 C CA . ALA A 1 225 ? -8.150 14.469 12.712 1.00 38.60 ? 225 ALA A CA 1 ATOM 1758 C C . ALA A 1 225 ? -7.142 14.390 13.860 1.00 38.00 ? 225 ALA A C 1 ATOM 1759 O O . ALA A 1 225 ? -5.936 14.338 13.649 1.00 37.97 ? 225 ALA A O 1 ATOM 1760 C CB . ALA A 1 225 ? -8.771 13.096 12.486 1.00 38.86 ? 225 ALA A CB 1 ATOM 1761 N N . TYR A 1 226 ? -7.661 14.385 15.077 1.00 37.48 ? 226 TYR A N 1 ATOM 1762 C CA . TYR A 1 226 ? -6.892 14.026 16.256 1.00 37.82 ? 226 TYR A CA 1 ATOM 1763 C C . TYR A 1 226 ? -7.518 12.769 16.868 1.00 37.85 ? 226 TYR A C 1 ATOM 1764 O O . TYR A 1 226 ? -8.622 12.372 16.490 1.00 37.83 ? 226 TYR A O 1 ATOM 1765 C CB . TYR A 1 226 ? -6.948 15.135 17.310 1.00 37.85 ? 226 TYR A CB 1 ATOM 1766 C CG . TYR A 1 226 ? -6.129 16.384 17.045 1.00 38.96 ? 226 TYR A CG 1 ATOM 1767 C CD1 . TYR A 1 226 ? -6.719 17.652 17.135 1.00 39.02 ? 226 TYR A CD1 1 ATOM 1768 C CD2 . TYR A 1 226 ? -4.754 16.311 16.749 1.00 40.11 ? 226 TYR A CD2 1 ATOM 1769 C CE1 . TYR A 1 226 ? -5.979 18.805 16.921 1.00 39.58 ? 226 TYR A CE1 1 ATOM 1770 C CE2 . TYR A 1 226 ? -4.004 17.467 16.534 1.00 39.60 ? 226 TYR A CE2 1 ATOM 1771 C CZ . TYR A 1 226 ? -4.630 18.701 16.620 1.00 40.79 ? 226 TYR A CZ 1 ATOM 1772 O OH . TYR A 1 226 ? -3.908 19.847 16.400 1.00 44.23 ? 226 TYR A OH 1 ATOM 1773 N N . LEU A 1 227 ? -6.823 12.159 17.828 1.00 37.93 ? 227 LEU A N 1 ATOM 1774 C CA . LEU A 1 227 ? -7.389 11.063 18.610 1.00 38.06 ? 227 LEU A CA 1 ATOM 1775 C C . LEU A 1 227 ? -8.416 11.642 19.575 1.00 37.96 ? 227 LEU A C 1 ATOM 1776 O O . LEU A 1 227 ? -8.252 12.766 20.050 1.00 37.64 ? 227 LEU A O 1 ATOM 1777 C CB . LEU A 1 227 ? -6.291 10.320 19.389 1.00 38.19 ? 227 LEU A CB 1 ATOM 1778 C CG . LEU A 1 227 ? -5.215 9.544 18.606 1.00 39.20 ? 227 LEU A CG 1 ATOM 1779 C CD1 . LEU A 1 227 ? -3.912 9.445 19.388 1.00 38.92 ? 227 LEU A CD1 1 ATOM 1780 C CD2 . LEU A 1 227 ? -5.692 8.162 18.210 1.00 40.19 ? 227 LEU A CD2 1 ATOM 1781 N N . PRO A 1 228 ? -9.480 10.883 19.873 1.00 38.17 ? 228 PRO A N 1 ATOM 1782 C CA . PRO A 1 228 ? -10.447 11.342 20.871 1.00 38.83 ? 228 PRO A CA 1 ATOM 1783 C C . PRO A 1 228 ? -9.775 11.596 22.217 1.00 39.58 ? 228 PRO A C 1 ATOM 1784 O O . PRO A 1 228 ? -8.716 11.016 22.497 1.00 39.60 ? 228 PRO A O 1 ATOM 1785 C CB . PRO A 1 228 ? -11.401 10.156 21.002 1.00 38.95 ? 228 PRO A CB 1 ATOM 1786 C CG . PRO A 1 228 ? -11.246 9.399 19.719 1.00 38.60 ? 228 PRO A CG 1 ATOM 1787 C CD . PRO A 1 228 ? -9.836 9.572 19.307 1.00 38.11 ? 228 PRO A CD 1 ATOM 1788 N N . PHE A 1 229 ? -10.365 12.457 23.039 1.00 40.35 ? 229 PHE A N 1 ATOM 1789 C CA . PHE A 1 229 ? -9.873 12.622 24.398 1.00 41.88 ? 229 PHE A CA 1 ATOM 1790 C C . PHE A 1 229 ? -10.341 11.456 25.252 1.00 43.00 ? 229 PHE A C 1 ATOM 1791 O O . PHE A 1 229 ? -11.266 10.746 24.880 1.00 43.27 ? 229 PHE A O 1 ATOM 1792 C CB . PHE A 1 229 ? -10.331 13.942 25.015 1.00 41.64 ? 229 PHE A CB 1 ATOM 1793 C CG . PHE A 1 229 ? -9.680 15.158 24.412 1.00 42.02 ? 229 PHE A CG 1 ATOM 1794 C CD1 . PHE A 1 229 ? -8.296 15.208 24.218 1.00 41.00 ? 229 PHE A CD1 1 ATOM 1795 C CD2 . PHE A 1 229 ? -10.452 16.272 24.057 1.00 41.87 ? 229 PHE A CD2 1 ATOM 1796 C CE1 . PHE A 1 229 ? -7.698 16.330 23.667 1.00 40.56 ? 229 PHE A CE1 1 ATOM 1797 C CE2 . PHE A 1 229 ? -9.859 17.405 23.506 1.00 40.87 ? 229 PHE A CE2 1 ATOM 1798 C CZ . PHE A 1 229 ? -8.482 17.437 23.315 1.00 40.78 ? 229 PHE A CZ 1 ATOM 1799 N N . ASN A 1 230 ? -9.691 11.255 26.391 1.00 44.62 ? 230 ASN A N 1 ATOM 1800 C CA . ASN A 1 230 ? -10.111 10.226 27.319 1.00 46.06 ? 230 ASN A CA 1 ATOM 1801 C C . ASN A 1 230 ? -11.070 10.731 28.392 1.00 47.30 ? 230 ASN A C 1 ATOM 1802 O O . ASN A 1 230 ? -10.841 11.769 29.014 1.00 47.06 ? 230 ASN A O 1 ATOM 1803 C CB . ASN A 1 230 ? -8.909 9.545 27.973 1.00 45.83 ? 230 ASN A CB 1 ATOM 1804 C CG . ASN A 1 230 ? -9.297 8.270 28.719 1.00 46.03 ? 230 ASN A CG 1 ATOM 1805 O OD1 . ASN A 1 230 ? -10.467 8.068 29.090 1.00 45.15 ? 230 ASN A OD1 1 ATOM 1806 N ND2 . ASN A 1 230 ? -8.312 7.405 28.953 1.00 45.32 ? 230 ASN A ND2 1 ATOM 1807 N N . ASN A 1 231 ? -12.142 9.959 28.587 1.00 49.32 ? 231 ASN A N 1 ATOM 1808 C CA . ASN A 1 231 ? -13.088 10.090 29.703 1.00 50.85 ? 231 ASN A CA 1 ATOM 1809 C C . ASN A 1 231 ? -12.371 10.301 31.040 1.00 51.15 ? 231 ASN A C 1 ATOM 1810 O O . ASN A 1 231 ? -12.710 11.214 31.792 1.00 51.31 ? 231 ASN A O 1 ATOM 1811 C CB . ASN A 1 231 ? -13.961 8.814 29.791 1.00 51.38 ? 231 ASN A CB 1 ATOM 1812 C CG . ASN A 1 231 ? -15.471 9.111 29.866 1.00 53.09 ? 231 ASN A CG 1 ATOM 1813 O OD1 . ASN A 1 231 ? -15.931 9.908 30.688 1.00 54.84 ? 231 ASN A OD1 1 ATOM 1814 N ND2 . ASN A 1 231 ? -16.245 8.443 29.011 1.00 54.58 ? 231 ASN A ND2 1 ATOM 1815 N N . ARG A 1 232 ? -11.364 9.458 31.295 1.00 51.55 ? 232 ARG A N 1 ATOM 1816 C CA . ARG A 1 232 ? -10.702 9.303 32.602 1.00 51.91 ? 232 ARG A CA 1 ATOM 1817 C C . ARG A 1 232 ? -10.347 10.582 33.349 1.00 51.96 ? 232 ARG A C 1 ATOM 1818 O O . ARG A 1 232 ? -9.595 11.432 32.855 1.00 52.60 ? 232 ARG A O 1 ATOM 1819 C CB . ARG A 1 232 ? -9.438 8.431 32.474 1.00 52.24 ? 232 ARG A CB 1 ATOM 1820 C CG . ARG A 1 232 ? -8.260 9.112 31.744 1.00 52.85 ? 232 ARG A CG 1 ATOM 1821 C CD . ARG A 1 232 ? -6.899 8.532 32.139 1.00 53.67 ? 232 ARG A CD 1 ATOM 1822 N NE . ARG A 1 232 ? -5.871 8.842 31.144 1.00 53.04 ? 232 ARG A NE 1 ATOM 1823 C CZ . ARG A 1 232 ? -4.695 8.234 31.063 1.00 53.07 ? 232 ARG A CZ 1 ATOM 1824 N NH1 . ARG A 1 232 ? -4.364 7.275 31.915 1.00 54.65 ? 232 ARG A NH1 1 ATOM 1825 N NH2 . ARG A 1 232 ? -3.843 8.581 30.122 1.00 54.30 ? 232 ARG A NH2 1 ATOM 1826 N N . LYS A 1 233 ? -10.901 10.708 34.547 1.00 51.59 ? 233 LYS A N 1 ATOM 1827 C CA . LYS A 1 233 ? -10.471 11.716 35.501 1.00 51.00 ? 233 LYS A CA 1 ATOM 1828 C C . LYS A 1 233 ? -10.227 10.965 36.806 1.00 50.85 ? 233 LYS A C 1 ATOM 1829 O O . LYS A 1 233 ? -10.999 10.062 37.140 1.00 51.08 ? 233 LYS A O 1 ATOM 1830 C CB . LYS A 1 233 ? -11.518 12.826 35.637 1.00 50.97 ? 233 LYS A CB 1 ATOM 1831 C CG . LYS A 1 233 ? -11.520 13.781 34.433 1.00 50.60 ? 233 LYS A CG 1 ATOM 1832 C CD . LYS A 1 233 ? -12.478 14.957 34.588 1.00 49.69 ? 233 LYS A CD 1 ATOM 1833 C CE . LYS A 1 233 ? -12.041 16.109 33.667 1.00 49.00 ? 233 LYS A CE 1 ATOM 1834 N NZ . LYS A 1 233 ? -13.089 17.138 33.361 1.00 47.52 ? 233 LYS A NZ 1 ATOM 1835 N N . PRO A 1 234 ? -9.119 11.270 37.513 1.00 50.57 ? 234 PRO A N 1 ATOM 1836 C CA . PRO A 1 234 ? -8.089 12.265 37.190 1.00 50.18 ? 234 PRO A CA 1 ATOM 1837 C C . PRO A 1 234 ? -7.334 11.938 35.893 1.00 49.69 ? 234 PRO A C 1 ATOM 1838 O O . PRO A 1 234 ? -7.264 10.773 35.478 1.00 49.89 ? 234 PRO A O 1 ATOM 1839 C CB . PRO A 1 234 ? -7.139 12.184 38.391 1.00 50.15 ? 234 PRO A CB 1 ATOM 1840 C CG . PRO A 1 234 ? -7.324 10.789 38.913 1.00 50.53 ? 234 PRO A CG 1 ATOM 1841 C CD . PRO A 1 234 ? -8.796 10.547 38.760 1.00 50.51 ? 234 PRO A CD 1 ATOM 1842 N N . SER A 1 235 ? -6.786 12.976 35.268 1.00 48.60 ? 235 SER A N 1 ATOM 1843 C CA . SER A 1 235 ? -6.068 12.858 34.012 1.00 47.38 ? 235 SER A CA 1 ATOM 1844 C C . SER A 1 235 ? -4.666 13.461 34.190 1.00 46.26 ? 235 SER A C 1 ATOM 1845 O O . SER A 1 235 ? -4.535 14.625 34.574 1.00 46.03 ? 235 SER A O 1 ATOM 1846 C CB . SER A 1 235 ? -6.856 13.577 32.920 1.00 47.50 ? 235 SER A CB 1 ATOM 1847 O OG . SER A 1 235 ? -6.154 13.591 31.695 1.00 49.00 ? 235 SER A OG 1 ATOM 1848 N N . PRO A 1 236 ? -3.608 12.659 33.947 1.00 45.12 ? 236 PRO A N 1 ATOM 1849 C CA . PRO A 1 236 ? -2.246 13.146 34.195 1.00 43.98 ? 236 PRO A CA 1 ATOM 1850 C C . PRO A 1 236 ? -1.826 14.227 33.195 1.00 43.04 ? 236 PRO A C 1 ATOM 1851 O O . PRO A 1 236 ? -1.038 15.114 33.540 1.00 42.90 ? 236 PRO A O 1 ATOM 1852 C CB . PRO A 1 236 ? -1.378 11.893 34.036 1.00 43.71 ? 236 PRO A CB 1 ATOM 1853 C CG . PRO A 1 236 ? -2.318 10.753 33.987 1.00 44.53 ? 236 PRO A CG 1 ATOM 1854 C CD . PRO A 1 236 ? -3.604 11.274 33.449 1.00 44.99 ? 236 PRO A CD 1 ATOM 1855 N N . CYS A 1 237 ? -2.365 14.149 31.978 1.00 41.93 ? 237 CYS A N 1 ATOM 1856 C CA . CYS A 1 237 ? -2.109 15.122 30.928 1.00 40.83 ? 237 CYS A CA 1 ATOM 1857 C C . CYS A 1 237 ? -2.736 16.466 31.275 1.00 41.56 ? 237 CYS A C 1 ATOM 1858 O O . CYS A 1 237 ? -2.326 17.512 30.772 1.00 41.57 ? 237 CYS A O 1 ATOM 1859 C CB . CYS A 1 237 ? -2.678 14.620 29.609 1.00 40.38 ? 237 CYS A CB 1 ATOM 1860 S SG . CYS A 1 237 ? -1.944 13.089 28.998 1.00 35.85 ? 237 CYS A SG 1 ATOM 1861 N N . GLU A 1 238 ? -3.739 16.419 32.139 1.00 42.10 ? 238 GLU A N 1 ATOM 1862 C CA . GLU A 1 238 ? -4.429 17.593 32.606 1.00 42.89 ? 238 GLU A CA 1 ATOM 1863 C C . GLU A 1 238 ? -3.556 18.178 33.709 1.00 43.12 ? 238 GLU A C 1 ATOM 1864 O O . GLU A 1 238 ? -3.285 19.378 33.726 1.00 43.28 ? 238 GLU A O 1 ATOM 1865 C CB . GLU A 1 238 ? -5.791 17.164 33.148 1.00 43.18 ? 238 GLU A CB 1 ATOM 1866 C CG . GLU A 1 238 ? -7.008 17.945 32.586 1.00 45.47 ? 238 GLU A CG 1 ATOM 1867 C CD . GLU A 1 238 ? -8.325 17.231 32.956 1.00 48.19 ? 238 GLU A CD 1 ATOM 1868 O OE1 . GLU A 1 238 ? -8.888 16.499 32.090 1.00 48.90 ? 238 GLU A OE1 1 ATOM 1869 O OE2 . GLU A 1 238 ? -8.803 17.411 34.110 1.00 49.84 ? 238 GLU A OE2 1 ATOM 1870 N N . PHE A 1 239 ? -3.085 17.304 34.600 1.00 43.46 ? 239 PHE A N 1 ATOM 1871 C CA . PHE A 1 239 ? -2.263 17.661 35.768 1.00 43.63 ? 239 PHE A CA 1 ATOM 1872 C C . PHE A 1 239 ? -0.935 18.334 35.402 1.00 43.63 ? 239 PHE A C 1 ATOM 1873 O O . PHE A 1 239 ? -0.285 18.956 36.244 1.00 43.30 ? 239 PHE A O 1 ATOM 1874 C CB . PHE A 1 239 ? -2.000 16.401 36.604 1.00 43.81 ? 239 PHE A CB 1 ATOM 1875 C CG . PHE A 1 239 ? -0.981 16.587 37.699 1.00 44.62 ? 239 PHE A CG 1 ATOM 1876 C CD1 . PHE A 1 239 ? -1.354 17.098 38.939 1.00 45.70 ? 239 PHE A CD1 1 ATOM 1877 C CD2 . PHE A 1 239 ? 0.352 16.236 37.494 1.00 45.88 ? 239 PHE A CD2 1 ATOM 1878 C CE1 . PHE A 1 239 ? -0.410 17.268 39.962 1.00 46.34 ? 239 PHE A CE1 1 ATOM 1879 C CE2 . PHE A 1 239 ? 1.304 16.410 38.502 1.00 46.38 ? 239 PHE A CE2 1 ATOM 1880 C CZ . PHE A 1 239 ? 0.917 16.922 39.741 1.00 46.86 ? 239 PHE A CZ 1 ATOM 1881 N N . ILE A 1 240 ? -0.554 18.207 34.139 1.00 43.84 ? 240 ILE A N 1 ATOM 1882 C CA . ILE A 1 240 ? 0.740 18.656 33.653 1.00 44.26 ? 240 ILE A CA 1 ATOM 1883 C C . ILE A 1 240 ? 0.743 20.176 33.389 1.00 44.43 ? 240 ILE A C 1 ATOM 1884 O O . ILE A 1 240 ? 1.782 20.841 33.450 1.00 43.98 ? 240 ILE A O 1 ATOM 1885 C CB . ILE A 1 240 ? 1.148 17.790 32.415 1.00 44.47 ? 240 ILE A CB 1 ATOM 1886 C CG1 . ILE A 1 240 ? 2.434 17.017 32.697 1.00 45.27 ? 240 ILE A CG1 1 ATOM 1887 C CG2 . ILE A 1 240 ? 1.129 18.558 31.072 1.00 44.08 ? 240 ILE A CG2 1 ATOM 1888 C CD1 . ILE A 1 240 ? 3.554 17.894 33.169 1.00 47.65 ? 240 ILE A CD1 1 ATOM 1889 N N . ASN A 1 241 ? -0.445 20.701 33.105 1.00 44.87 ? 241 ASN A N 1 ATOM 1890 C CA . ASN A 1 241 ? -0.691 22.123 32.945 1.00 45.35 ? 241 ASN A CA 1 ATOM 1891 C C . ASN A 1 241 ? -2.155 22.355 33.267 1.00 45.18 ? 241 ASN A C 1 ATOM 1892 O O . ASN A 1 241 ? -3.011 22.253 32.377 1.00 45.20 ? 241 ASN A O 1 ATOM 1893 C CB . ASN A 1 241 ? -0.400 22.554 31.507 1.00 45.92 ? 241 ASN A CB 1 ATOM 1894 C CG . ASN A 1 241 ? -0.510 24.056 31.307 1.00 47.36 ? 241 ASN A CG 1 ATOM 1895 O OD1 . ASN A 1 241 ? -1.452 24.697 31.787 1.00 48.90 ? 241 ASN A OD1 1 ATOM 1896 N ND2 . ASN A 1 241 ? 0.462 24.622 30.584 1.00 48.65 ? 241 ASN A ND2 1 ATOM 1897 N N . THR A 1 242 ? -2.443 22.643 34.537 1.00 44.81 ? 242 THR A N 1 ATOM 1898 C CA . THR A 1 242 ? -3.827 22.829 34.998 1.00 44.54 ? 242 THR A CA 1 ATOM 1899 C C . THR A 1 242 ? -4.552 24.026 34.385 1.00 44.02 ? 242 THR A C 1 ATOM 1900 O O . THR A 1 242 ? -5.774 24.073 34.382 1.00 44.00 ? 242 THR A O 1 ATOM 1901 C CB . THR A 1 242 ? -3.928 22.915 36.530 1.00 44.77 ? 242 THR A CB 1 ATOM 1902 O OG1 . THR A 1 242 ? -2.707 23.462 37.061 1.00 44.57 ? 242 THR A OG1 1 ATOM 1903 C CG2 . THR A 1 242 ? -4.173 21.511 37.112 1.00 45.36 ? 242 THR A CG2 1 ATOM 1904 N N . THR A 1 243 ? -3.801 24.983 33.858 1.00 43.47 ? 243 THR A N 1 ATOM 1905 C CA . THR A 1 243 ? -4.396 26.104 33.139 1.00 43.26 ? 243 THR A CA 1 ATOM 1906 C C . THR A 1 243 ? -4.961 25.636 31.787 1.00 42.90 ? 243 THR A C 1 ATOM 1907 O O . THR A 1 243 ? -6.076 26.000 31.417 1.00 42.78 ? 243 THR A O 1 ATOM 1908 C CB . THR A 1 243 ? -3.369 27.252 32.966 1.00 43.34 ? 243 THR A CB 1 ATOM 1909 O OG1 . THR A 1 243 ? -2.844 27.608 34.259 1.00 43.53 ? 243 THR A OG1 1 ATOM 1910 C CG2 . THR A 1 243 ? -3.998 28.476 32.308 1.00 43.17 ? 243 THR A CG2 1 ATOM 1911 N N . ALA A 1 244 ? -4.201 24.804 31.076 1.00 42.31 ? 244 ALA A N 1 ATOM 1912 C CA . ALA A 1 244 ? -4.600 24.352 29.749 1.00 41.82 ? 244 ALA A CA 1 ATOM 1913 C C . ALA A 1 244 ? -5.664 23.248 29.778 1.00 41.58 ? 244 ALA A C 1 ATOM 1914 O O . ALA A 1 244 ? -6.550 23.212 28.915 1.00 41.70 ? 244 ALA A O 1 ATOM 1915 C CB . ALA A 1 244 ? -3.386 23.924 28.946 1.00 41.74 ? 244 ALA A CB 1 ATOM 1916 N N . ARG A 1 245 ? -5.578 22.361 30.771 1.00 41.04 ? 245 ARG A N 1 ATOM 1917 C CA . ARG A 1 245 ? -6.547 21.272 30.954 1.00 40.69 ? 245 ARG A CA 1 ATOM 1918 C C . ARG A 1 245 ? -6.855 20.529 29.674 1.00 39.89 ? 245 ARG A C 1 ATOM 1919 O O . ARG A 1 245 ? -8.001 20.550 29.207 1.00 39.94 ? 245 ARG A O 1 ATOM 1920 C CB . ARG A 1 245 ? -7.874 21.793 31.491 1.00 41.00 ? 245 ARG A CB 1 ATOM 1921 C CG . ARG A 1 245 ? -7.938 21.964 32.970 1.00 42.57 ? 245 ARG A CG 1 ATOM 1922 C CD . ARG A 1 245 ? -9.090 22.874 33.293 1.00 43.63 ? 245 ARG A CD 1 ATOM 1923 N NE . ARG A 1 245 ? -8.695 24.282 33.327 1.00 45.94 ? 245 ARG A NE 1 ATOM 1924 C CZ . ARG A 1 245 ? -8.227 24.908 34.410 1.00 46.62 ? 245 ARG A CZ 1 ATOM 1925 N NH1 . ARG A 1 245 ? -7.909 26.200 34.344 1.00 46.40 ? 245 ARG A NH1 1 ATOM 1926 N NH2 . ARG A 1 245 ? -8.074 24.244 35.563 1.00 45.80 ? 245 ARG A NH2 1 ATOM 1927 N N . VAL A 1 246 ? -5.839 19.884 29.113 1.00 38.68 ? 246 VAL A N 1 ATOM 1928 C CA . VAL A 1 246 ? -6.027 19.007 27.961 1.00 37.67 ? 246 VAL A CA 1 ATOM 1929 C C . VAL A 1 246 ? -5.777 17.558 28.392 1.00 36.89 ? 246 VAL A C 1 ATOM 1930 O O . VAL A 1 246 ? -4.663 17.217 28.794 1.00 37.03 ? 246 VAL A O 1 ATOM 1931 C CB . VAL A 1 246 ? -5.133 19.409 26.757 1.00 37.58 ? 246 VAL A CB 1 ATOM 1932 C CG1 . VAL A 1 246 ? -5.452 18.548 25.542 1.00 36.90 ? 246 VAL A CG1 1 ATOM 1933 C CG2 . VAL A 1 246 ? -5.318 20.880 26.423 1.00 36.98 ? 246 VAL A CG2 1 ATOM 1934 N N . PRO A 1 247 ? -6.831 16.718 28.351 1.00 36.24 ? 247 PRO A N 1 ATOM 1935 C CA . PRO A 1 247 ? -6.718 15.297 28.691 1.00 35.70 ? 247 PRO A CA 1 ATOM 1936 C C . PRO A 1 247 ? -5.823 14.498 27.758 1.00 35.19 ? 247 PRO A C 1 ATOM 1937 O O . PRO A 1 247 ? -5.462 14.963 26.671 1.00 35.14 ? 247 PRO A O 1 ATOM 1938 C CB . PRO A 1 247 ? -8.166 14.790 28.598 1.00 35.32 ? 247 PRO A CB 1 ATOM 1939 C CG . PRO A 1 247 ? -8.887 15.780 27.801 1.00 35.73 ? 247 PRO A CG 1 ATOM 1940 C CD . PRO A 1 247 ? -8.225 17.093 28.035 1.00 36.13 ? 247 PRO A CD 1 ATOM 1941 N N . CYS A 1 248 ? -5.472 13.296 28.198 1.00 34.77 ? 248 CYS A N 1 ATOM 1942 C CA . CYS A 1 248 ? -4.719 12.369 27.380 1.00 34.38 ? 248 CYS A CA 1 ATOM 1943 C C . CYS A 1 248 ? -5.578 11.889 26.217 1.00 34.16 ? 248 CYS A C 1 ATOM 1944 O O . CYS A 1 248 ? -6.792 12.110 26.198 1.00 34.00 ? 248 CYS A O 1 ATOM 1945 C CB . CYS A 1 248 ? -4.238 11.193 28.228 1.00 34.52 ? 248 CYS A CB 1 ATOM 1946 S SG . CYS A 1 248 ? -3.198 11.653 29.665 1.00 34.20 ? 248 CYS A SG 1 ATOM 1947 N N . PHE A 1 249 ? -4.945 11.261 25.234 1.00 33.88 ? 249 PHE A N 1 ATOM 1948 C CA . PHE A 1 249 ? -5.678 10.735 24.097 1.00 33.73 ? 249 PHE A CA 1 ATOM 1949 C C . PHE A 1 249 ? -6.149 9.317 24.369 1.00 33.69 ? 249 PHE A C 1 ATOM 1950 O O . PHE A 1 249 ? -5.584 8.601 25.194 1.00 33.40 ? 249 PHE A O 1 ATOM 1951 C CB . PHE A 1 249 ? -4.826 10.759 22.833 1.00 33.67 ? 249 PHE A CB 1 ATOM 1952 C CG . PHE A 1 249 ? -4.474 12.137 22.350 1.00 33.99 ? 249 PHE A CG 1 ATOM 1953 C CD1 . PHE A 1 249 ? -5.460 13.021 21.929 1.00 34.80 ? 249 PHE A CD1 1 ATOM 1954 C CD2 . PHE A 1 249 ? -3.151 12.533 22.272 1.00 34.26 ? 249 PHE A CD2 1 ATOM 1955 C CE1 . PHE A 1 249 ? -5.128 14.286 21.456 1.00 34.72 ? 249 PHE A CE1 1 ATOM 1956 C CE2 . PHE A 1 249 ? -2.807 13.796 21.807 1.00 34.96 ? 249 PHE A CE2 1 ATOM 1957 C CZ . PHE A 1 249 ? -3.795 14.672 21.395 1.00 34.89 ? 249 PHE A CZ 1 ATOM 1958 N N . LEU A 1 250 ? -7.202 8.921 23.665 1.00 33.97 ? 250 LEU A N 1 ATOM 1959 C CA . LEU A 1 250 ? -7.738 7.579 23.776 1.00 33.90 ? 250 LEU A CA 1 ATOM 1960 C C . LEU A 1 250 ? -7.356 6.792 22.539 1.00 33.80 ? 250 LEU A C 1 ATOM 1961 O O . LEU A 1 250 ? -7.830 7.069 21.429 1.00 34.14 ? 250 LEU A O 1 ATOM 1962 C CB . LEU A 1 250 ? -9.253 7.622 23.937 1.00 33.90 ? 250 LEU A CB 1 ATOM 1963 C CG . LEU A 1 250 ? -9.919 6.272 24.163 1.00 35.68 ? 250 LEU A CG 1 ATOM 1964 C CD1 . LEU A 1 250 ? -9.661 5.743 25.590 1.00 36.78 ? 250 LEU A CD1 1 ATOM 1965 C CD2 . LEU A 1 250 ? -11.404 6.379 23.868 1.00 36.40 ? 250 LEU A CD2 1 ATOM 1966 N N . ALA A 1 251 ? -6.489 5.810 22.737 1.00 33.53 ? 251 ALA A N 1 ATOM 1967 C CA . ALA A 1 251 ? -6.046 4.967 21.658 1.00 33.00 ? 251 ALA A CA 1 ATOM 1968 C C . ALA A 1 251 ? -6.245 3.504 22.031 1.00 32.99 ? 251 ALA A C 1 ATOM 1969 O O . ALA A 1 251 ? -6.688 3.196 23.140 1.00 32.42 ? 251 ALA A O 1 ATOM 1970 C CB . ALA A 1 251 ? -4.594 5.254 21.362 1.00 33.16 ? 251 ALA A CB 1 ATOM 1971 N N . GLY A 1 252 ? -5.906 2.614 21.093 1.00 33.12 ? 252 GLY A N 1 ATOM 1972 C CA . GLY A 1 252 ? -5.960 1.168 21.293 1.00 32.86 ? 252 GLY A CA 1 ATOM 1973 C C . GLY A 1 252 ? -5.032 0.651 22.376 1.00 32.98 ? 252 GLY A C 1 ATOM 1974 O O . GLY A 1 252 ? -5.252 -0.441 22.903 1.00 33.06 ? 252 GLY A O 1 ATOM 1975 N N . ASP A 1 253 ? -3.997 1.430 22.697 1.00 32.75 ? 253 ASP A N 1 ATOM 1976 C CA . ASP A 1 253 ? -3.068 1.107 23.768 1.00 32.58 ? 253 ASP A CA 1 ATOM 1977 C C . ASP A 1 253 ? -3.044 2.229 24.790 1.00 32.74 ? 253 ASP A C 1 ATOM 1978 O O . ASP A 1 253 ? -3.092 3.405 24.427 1.00 32.44 ? 253 ASP A O 1 ATOM 1979 C CB . ASP A 1 253 ? -1.660 0.872 23.214 1.00 32.63 ? 253 ASP A CB 1 ATOM 1980 C CG . ASP A 1 253 ? -0.677 0.392 24.284 1.00 32.61 ? 253 ASP A CG 1 ATOM 1981 O OD1 . ASP A 1 253 ? -0.554 -0.844 24.477 1.00 31.97 ? 253 ASP A OD1 1 ATOM 1982 O OD2 . ASP A 1 253 ? -0.044 1.252 24.941 1.00 31.58 ? 253 ASP A OD2 1 ATOM 1983 N N . PHE A 1 254 ? -2.937 1.862 26.067 1.00 32.99 ? 254 PHE A N 1 ATOM 1984 C CA . PHE A 1 254 ? -3.038 2.838 27.145 1.00 33.75 ? 254 PHE A CA 1 ATOM 1985 C C . PHE A 1 254 ? -1.813 3.761 27.311 1.00 32.78 ? 254 PHE A C 1 ATOM 1986 O O . PHE A 1 254 ? -1.919 4.820 27.924 1.00 32.92 ? 254 PHE A O 1 ATOM 1987 C CB . PHE A 1 254 ? -3.449 2.159 28.470 1.00 34.75 ? 254 PHE A CB 1 ATOM 1988 C CG . PHE A 1 254 ? -4.942 1.796 28.545 1.00 39.06 ? 254 PHE A CG 1 ATOM 1989 C CD1 . PHE A 1 254 ? -5.359 0.458 28.496 1.00 41.48 ? 254 PHE A CD1 1 ATOM 1990 C CD2 . PHE A 1 254 ? -5.928 2.800 28.661 1.00 42.50 ? 254 PHE A CD2 1 ATOM 1991 C CE1 . PHE A 1 254 ? -6.724 0.122 28.566 1.00 43.16 ? 254 PHE A CE1 1 ATOM 1992 C CE2 . PHE A 1 254 ? -7.304 2.480 28.725 1.00 43.64 ? 254 PHE A CE2 1 ATOM 1993 C CZ . PHE A 1 254 ? -7.702 1.139 28.679 1.00 44.22 ? 254 PHE A CZ 1 ATOM 1994 N N . ARG A 1 255 ? -0.669 3.393 26.738 1.00 31.55 ? 255 ARG A N 1 ATOM 1995 C CA . ARG A 1 255 ? 0.569 4.171 26.945 1.00 30.24 ? 255 ARG A CA 1 ATOM 1996 C C . ARG A 1 255 ? 0.706 5.358 25.986 1.00 29.72 ? 255 ARG A C 1 ATOM 1997 O O . ARG A 1 255 ? 1.633 6.172 26.113 1.00 29.51 ? 255 ARG A O 1 ATOM 1998 C CB . ARG A 1 255 ? 1.806 3.268 26.867 1.00 29.67 ? 255 ARG A CB 1 ATOM 1999 C CG . ARG A 1 255 ? 1.825 2.152 27.886 1.00 28.09 ? 255 ARG A CG 1 ATOM 2000 C CD . ARG A 1 255 ? 2.718 1.000 27.434 1.00 26.15 ? 255 ARG A CD 1 ATOM 2001 N NE . ARG A 1 255 ? 2.158 0.181 26.347 1.00 23.59 ? 255 ARG A NE 1 ATOM 2002 C CZ . ARG A 1 255 ? 2.563 -1.056 26.061 1.00 21.58 ? 255 ARG A CZ 1 ATOM 2003 N NH1 . ARG A 1 255 ? 3.531 -1.616 26.776 1.00 21.50 ? 255 ARG A NH1 1 ATOM 2004 N NH2 . ARG A 1 255 ? 1.996 -1.741 25.073 1.00 19.23 ? 255 ARG A NH2 1 ATOM 2005 N N . ALA A 1 256 ? -0.248 5.463 25.063 1.00 29.22 ? 256 ALA A N 1 ATOM 2006 C CA . ALA A 1 256 ? -0.204 6.397 23.923 1.00 28.43 ? 256 ALA A CA 1 ATOM 2007 C C . ALA A 1 256 ? 0.252 7.827 24.206 1.00 27.98 ? 256 ALA A C 1 ATOM 2008 O O . ALA A 1 256 ? 0.886 8.442 23.355 1.00 27.98 ? 256 ALA A O 1 ATOM 2009 C CB . ALA A 1 256 ? -1.547 6.408 23.217 1.00 28.40 ? 256 ALA A CB 1 ATOM 2010 N N . SER A 1 257 ? -0.074 8.358 25.380 1.00 27.68 ? 257 SER A N 1 ATOM 2011 C CA . SER A 1 257 ? 0.258 9.746 25.718 1.00 28.03 ? 257 SER A CA 1 ATOM 2012 C C . SER A 1 257 ? 1.541 9.881 26.549 1.00 27.89 ? 257 SER A C 1 ATOM 2013 O O . SER A 1 257 ? 1.862 10.966 27.019 1.00 27.98 ? 257 SER A O 1 ATOM 2014 C CB . SER A 1 257 ? -0.915 10.421 26.454 1.00 27.95 ? 257 SER A CB 1 ATOM 2015 O OG . SER A 1 257 ? -2.106 10.358 25.677 1.00 29.26 ? 257 SER A OG 1 ATOM 2016 N N . GLU A 1 258 ? 2.270 8.784 26.729 1.00 27.65 ? 258 GLU A N 1 ATOM 2017 C CA . GLU A 1 258 ? 3.490 8.797 27.544 1.00 27.24 ? 258 GLU A CA 1 ATOM 2018 C C . GLU A 1 258 ? 4.427 9.954 27.185 1.00 26.29 ? 258 GLU A C 1 ATOM 2019 O O . GLU A 1 258 ? 5.004 10.605 28.066 1.00 26.31 ? 258 GLU A O 1 ATOM 2020 C CB . GLU A 1 258 ? 4.354 7.547 27.704 1.00 27.39 ? 258 GLU A CB 1 ATOM 2021 C CG . GLU A 1 258 ? 5.574 7.525 28.606 1.00 28.22 ? 258 GLU A CG 1 ATOM 2022 C CD . GLU A 1 258 ? 6.889 7.656 27.862 1.00 29.25 ? 258 GLU A CD 1 ATOM 2023 O OE1 . GLU A 1 258 ? 6.914 7.485 26.626 1.00 29.67 ? 258 GLU A OE1 1 ATOM 2024 O OE2 . GLU A 1 258 ? 7.918 7.936 28.518 1.00 33.53 ? 258 GLU A OE2 1 ATOM 2025 N N . GLN A 1 259 ? 4.582 10.199 25.897 1.00 24.80 ? 259 GLN A N 1 ATOM 2026 C CA . GLN A 1 259 ? 5.360 11.322 25.452 1.00 24.66 ? 259 GLN A CA 1 ATOM 2027 C C . GLN A 1 259 ? 4.802 11.812 24.123 1.00 25.19 ? 259 GLN A C 1 ATOM 2028 O O . GLN A 1 259 ? 4.180 11.047 23.375 1.00 25.66 ? 259 GLN A O 1 ATOM 2029 C CB . GLN A 1 259 ? 6.857 10.976 25.400 1.00 24.16 ? 259 GLN A CB 1 ATOM 2030 C CG . GLN A 1 259 ? 7.223 9.738 24.609 1.00 22.09 ? 259 GLN A CG 1 ATOM 2031 C CD . GLN A 1 259 ? 7.672 10.084 23.212 1.00 21.27 ? 259 GLN A CD 1 ATOM 2032 O OE1 . GLN A 1 259 ? 7.839 9.202 22.349 1.00 19.76 ? 259 GLN A OE1 1 ATOM 2033 N NE2 . GLN A 1 259 ? 7.881 11.377 22.973 1.00 18.96 ? 259 GLN A NE2 1 ATOM 2034 N N . ILE A 1 260 ? 5.006 13.092 23.847 1.00 25.44 ? 260 ILE A N 1 ATOM 2035 C CA . ILE A 1 260 ? 4.347 13.785 22.738 1.00 25.84 ? 260 ILE A CA 1 ATOM 2036 C C . ILE A 1 260 ? 4.587 13.153 21.353 1.00 26.12 ? 260 ILE A C 1 ATOM 2037 O O . ILE A 1 260 ? 3.681 13.090 20.514 1.00 26.65 ? 260 ILE A O 1 ATOM 2038 C CB . ILE A 1 260 ? 4.716 15.287 22.757 1.00 25.78 ? 260 ILE A CB 1 ATOM 2039 C CG1 . ILE A 1 260 ? 3.695 16.106 21.966 1.00 25.95 ? 260 ILE A CG1 1 ATOM 2040 C CG2 . ILE A 1 260 ? 6.166 15.510 22.310 1.00 25.42 ? 260 ILE A CG2 1 ATOM 2041 C CD1 . ILE A 1 260 ? 3.871 17.624 22.112 1.00 26.04 ? 260 ILE A CD1 1 ATOM 2042 N N . LEU A 1 261 ? 5.800 12.672 21.135 1.00 26.17 ? 261 LEU A N 1 ATOM 2043 C CA . LEU A 1 261 ? 6.191 12.096 19.868 1.00 26.26 ? 261 LEU A CA 1 ATOM 2044 C C . LEU A 1 261 ? 5.610 10.703 19.648 1.00 26.86 ? 261 LEU A C 1 ATOM 2045 O O . LEU A 1 261 ? 5.668 10.164 18.530 1.00 27.00 ? 261 LEU A O 1 ATOM 2046 C CB . LEU A 1 261 ? 7.705 12.025 19.807 1.00 26.01 ? 261 LEU A CB 1 ATOM 2047 C CG . LEU A 1 261 ? 8.513 12.862 18.831 1.00 25.36 ? 261 LEU A CG 1 ATOM 2048 C CD1 . LEU A 1 261 ? 7.853 14.153 18.423 1.00 24.82 ? 261 LEU A CD1 1 ATOM 2049 C CD2 . LEU A 1 261 ? 9.869 13.087 19.451 1.00 25.45 ? 261 LEU A CD2 1 ATOM 2050 N N . LEU A 1 262 ? 5.074 10.111 20.709 1.00 26.84 ? 262 LEU A N 1 ATOM 2051 C CA . LEU A 1 262 ? 4.436 8.809 20.610 1.00 27.14 ? 262 LEU A CA 1 ATOM 2052 C C . LEU A 1 262 ? 2.965 9.019 20.282 1.00 27.76 ? 262 LEU A C 1 ATOM 2053 O O . LEU A 1 262 ? 2.371 8.274 19.486 1.00 27.73 ? 262 LEU A O 1 ATOM 2054 C CB . LEU A 1 262 ? 4.607 8.033 21.917 1.00 26.89 ? 262 LEU A CB 1 ATOM 2055 C CG . LEU A 1 262 ? 3.805 6.753 22.143 1.00 26.66 ? 262 LEU A CG 1 ATOM 2056 C CD1 . LEU A 1 262 ? 4.075 5.704 21.043 1.00 26.57 ? 262 LEU A CD1 1 ATOM 2057 C CD2 . LEU A 1 262 ? 4.109 6.204 23.532 1.00 25.49 ? 262 LEU A CD2 1 ATOM 2058 N N . ALA A 1 263 ? 2.381 10.036 20.912 1.00 28.02 ? 263 ALA A N 1 ATOM 2059 C CA . ALA A 1 263 ? 1.026 10.450 20.598 1.00 28.57 ? 263 ALA A CA 1 ATOM 2060 C C . ALA A 1 263 ? 0.945 10.875 19.120 1.00 28.84 ? 263 ALA A C 1 ATOM 2061 O O . ALA A 1 263 ? -0.044 10.608 18.436 1.00 28.97 ? 263 ALA A O 1 ATOM 2062 C CB . ALA A 1 263 ? 0.600 11.580 21.515 1.00 28.34 ? 263 ALA A CB 1 ATOM 2063 N N . THR A 1 264 ? 2.001 11.525 18.642 1.00 28.91 ? 264 THR A N 1 ATOM 2064 C CA . THR A 1 264 ? 2.129 11.902 17.241 1.00 29.19 ? 264 THR A CA 1 ATOM 2065 C C . THR A 1 264 ? 2.029 10.676 16.309 1.00 29.18 ? 264 THR A C 1 ATOM 2066 O O . THR A 1 264 ? 1.223 10.667 15.382 1.00 29.63 ? 264 THR A O 1 ATOM 2067 C CB . THR A 1 264 ? 3.441 12.696 17.022 1.00 29.40 ? 264 THR A CB 1 ATOM 2068 O OG1 . THR A 1 264 ? 3.402 13.877 17.827 1.00 29.52 ? 264 THR A OG1 1 ATOM 2069 C CG2 . THR A 1 264 ? 3.621 13.100 15.570 1.00 28.54 ? 264 THR A CG2 1 ATOM 2070 N N . ALA A 1 265 ? 2.833 9.650 16.565 1.00 28.91 ? 265 ALA A N 1 ATOM 2071 C CA . ALA A 1 265 ? 2.783 8.421 15.783 1.00 29.06 ? 265 ALA A CA 1 ATOM 2072 C C . ALA A 1 265 ? 1.397 7.768 15.824 1.00 29.14 ? 265 ALA A C 1 ATOM 2073 O O . ALA A 1 265 ? 0.867 7.370 14.780 1.00 29.02 ? 265 ALA A O 1 ATOM 2074 C CB . ALA A 1 265 ? 3.868 7.443 16.247 1.00 29.10 ? 265 ALA A CB 1 ATOM 2075 N N . HIS A 1 266 ? 0.804 7.681 17.014 1.00 29.31 ? 266 HIS A N 1 ATOM 2076 C CA . HIS A 1 266 ? -0.566 7.172 17.152 1.00 29.98 ? 266 HIS A CA 1 ATOM 2077 C C . HIS A 1 266 ? -1.561 7.891 16.240 1.00 30.41 ? 266 HIS A C 1 ATOM 2078 O O . HIS A 1 266 ? -2.373 7.234 15.572 1.00 30.36 ? 266 HIS A O 1 ATOM 2079 C CB . HIS A 1 266 ? -1.059 7.227 18.605 1.00 29.95 ? 266 HIS A CB 1 ATOM 2080 C CG . HIS A 1 266 ? -0.794 5.973 19.384 1.00 30.11 ? 266 HIS A CG 1 ATOM 2081 N ND1 . HIS A 1 266 ? -1.557 4.834 19.244 1.00 29.10 ? 266 HIS A ND1 1 ATOM 2082 C CD2 . HIS A 1 266 ? 0.152 5.682 20.311 1.00 29.28 ? 266 HIS A CD2 1 ATOM 2083 C CE1 . HIS A 1 266 ? -1.097 3.899 20.057 1.00 28.50 ? 266 HIS A CE1 1 ATOM 2084 N NE2 . HIS A 1 266 ? -0.062 4.388 20.717 1.00 28.24 ? 266 HIS A NE2 1 ATOM 2085 N N . THR A 1 267 ? -1.488 9.224 16.205 1.00 30.80 ? 267 THR A N 1 ATOM 2086 C CA . THR A 1 267 ? -2.417 10.009 15.387 1.00 31.74 ? 267 THR A CA 1 ATOM 2087 C C . THR A 1 267 ? -2.198 9.897 13.868 1.00 32.55 ? 267 THR A C 1 ATOM 2088 O O . THR A 1 267 ? -3.165 9.980 13.095 1.00 32.77 ? 267 THR A O 1 ATOM 2089 C CB . THR A 1 267 ? -2.622 11.495 15.874 1.00 31.73 ? 267 THR A CB 1 ATOM 2090 O OG1 . THR A 1 267 ? -2.967 12.323 14.757 1.00 32.09 ? 267 THR A OG1 1 ATOM 2091 C CG2 . THR A 1 267 ? -1.415 12.049 16.538 1.00 30.91 ? 267 THR A CG2 1 ATOM 2092 N N . LEU A 1 268 ? -0.950 9.701 13.443 1.00 33.21 ? 268 LEU A N 1 ATOM 2093 C CA . LEU A 1 268 ? -0.680 9.344 12.050 1.00 34.25 ? 268 LEU A CA 1 ATOM 2094 C C . LEU A 1 268 ? -1.383 8.040 11.664 1.00 34.80 ? 268 LEU A C 1 ATOM 2095 O O . LEU A 1 268 ? -1.957 7.947 10.576 1.00 34.96 ? 268 LEU A O 1 ATOM 2096 C CB . LEU A 1 268 ? 0.828 9.231 11.792 1.00 34.44 ? 268 LEU A CB 1 ATOM 2097 C CG . LEU A 1 268 ? 1.641 10.419 11.237 1.00 35.68 ? 268 LEU A CG 1 ATOM 2098 C CD1 . LEU A 1 268 ? 1.142 11.783 11.687 1.00 37.23 ? 268 LEU A CD1 1 ATOM 2099 C CD2 . LEU A 1 268 ? 3.132 10.267 11.576 1.00 36.57 ? 268 LEU A CD2 1 ATOM 2100 N N . LEU A 1 269 ? -1.345 7.050 12.565 1.00 35.38 ? 269 LEU A N 1 ATOM 2101 C CA . LEU A 1 269 ? -1.934 5.717 12.328 1.00 35.77 ? 269 LEU A CA 1 ATOM 2102 C C . LEU A 1 269 ? -3.462 5.703 12.268 1.00 36.06 ? 269 LEU A C 1 ATOM 2103 O O . LEU A 1 269 ? -4.039 5.054 11.394 1.00 35.94 ? 269 LEU A O 1 ATOM 2104 C CB . LEU A 1 269 ? -1.424 4.686 13.349 1.00 35.60 ? 269 LEU A CB 1 ATOM 2105 C CG . LEU A 1 269 ? 0.070 4.325 13.272 1.00 36.02 ? 269 LEU A CG 1 ATOM 2106 C CD1 . LEU A 1 269 ? 0.458 3.380 14.412 1.00 36.07 ? 269 LEU A CD1 1 ATOM 2107 C CD2 . LEU A 1 269 ? 0.478 3.739 11.906 1.00 35.18 ? 269 LEU A CD2 1 ATOM 2108 N N . LEU A 1 270 ? -4.110 6.407 13.196 1.00 36.44 ? 270 LEU A N 1 ATOM 2109 C CA . LEU A 1 270 ? -5.565 6.576 13.162 1.00 36.70 ? 270 LEU A CA 1 ATOM 2110 C C . LEU A 1 270 ? -5.968 7.218 11.840 1.00 36.77 ? 270 LEU A C 1 ATOM 2111 O O . LEU A 1 270 ? -6.873 6.741 11.144 1.00 37.02 ? 270 LEU A O 1 ATOM 2112 C CB . LEU A 1 270 ? -6.025 7.474 14.307 1.00 36.94 ? 270 LEU A CB 1 ATOM 2113 C CG . LEU A 1 270 ? -7.533 7.542 14.558 1.00 37.63 ? 270 LEU A CG 1 ATOM 2114 C CD1 . LEU A 1 270 ? -7.931 6.494 15.574 1.00 38.06 ? 270 LEU A CD1 1 ATOM 2115 C CD2 . LEU A 1 270 ? -7.920 8.917 15.061 1.00 38.59 ? 270 LEU A CD2 1 ATOM 2116 N N . ARG A 1 271 ? -5.276 8.303 11.503 1.00 36.62 ? 271 ARG A N 1 ATOM 2117 C CA . ARG A 1 271 ? -5.520 9.023 10.267 1.00 36.33 ? 271 ARG A CA 1 ATOM 2118 C C . ARG A 1 271 ? -5.439 8.104 9.051 1.00 36.18 ? 271 ARG A C 1 ATOM 2119 O O . ARG A 1 271 ? -6.244 8.239 8.125 1.00 36.36 ? 271 ARG A O 1 ATOM 2120 C CB . ARG A 1 271 ? -4.551 10.197 10.126 1.00 36.31 ? 271 ARG A CB 1 ATOM 2121 C CG . ARG A 1 271 ? -4.938 11.431 10.930 1.00 35.15 ? 271 ARG A CG 1 ATOM 2122 C CD . ARG A 1 271 ? -3.936 12.554 10.685 1.00 34.17 ? 271 ARG A CD 1 ATOM 2123 N NE . ARG A 1 271 ? -4.062 13.630 11.670 1.00 33.34 ? 271 ARG A NE 1 ATOM 2124 C CZ . ARG A 1 271 ? -3.325 14.737 11.686 1.00 32.26 ? 271 ARG A CZ 1 ATOM 2125 N NH1 . ARG A 1 271 ? -2.393 14.950 10.767 1.00 33.21 ? 271 ARG A NH1 1 ATOM 2126 N NH2 . ARG A 1 271 ? -3.525 15.639 12.624 1.00 32.96 ? 271 ARG A NH2 1 ATOM 2127 N N . GLU A 1 272 ? -4.491 7.167 9.068 1.00 35.64 ? 272 GLU A N 1 ATOM 2128 C CA . GLU A 1 272 ? -4.323 6.225 7.959 1.00 35.40 ? 272 GLU A CA 1 ATOM 2129 C C . GLU A 1 272 ? -5.502 5.268 7.812 1.00 35.11 ? 272 GLU A C 1 ATOM 2130 O O . GLU A 1 272 ? -5.913 4.961 6.689 1.00 34.67 ? 272 GLU A O 1 ATOM 2131 C CB . GLU A 1 272 ? -3.013 5.431 8.097 1.00 35.61 ? 272 GLU A CB 1 ATOM 2132 C CG . GLU A 1 272 ? -2.746 4.395 6.982 1.00 35.69 ? 272 GLU A CG 1 ATOM 2133 C CD . GLU A 1 272 ? -2.750 4.973 5.558 1.00 36.32 ? 272 GLU A CD 1 ATOM 2134 O OE1 . GLU A 1 272 ? -2.972 6.183 5.376 1.00 36.88 ? 272 GLU A OE1 1 ATOM 2135 O OE2 . GLU A 1 272 ? -2.516 4.205 4.603 1.00 37.52 ? 272 GLU A OE2 1 ATOM 2136 N N . HIS A 1 273 ? -6.031 4.792 8.937 1.00 34.86 ? 273 HIS A N 1 ATOM 2137 C CA . HIS A 1 273 ? -7.188 3.905 8.909 1.00 35.02 ? 273 HIS A CA 1 ATOM 2138 C C . HIS A 1 273 ? -8.381 4.545 8.207 1.00 34.81 ? 273 HIS A C 1 ATOM 2139 O O . HIS A 1 273 ? -8.980 3.967 7.300 1.00 34.28 ? 273 HIS A O 1 ATOM 2140 C CB . HIS A 1 273 ? -7.620 3.494 10.313 1.00 35.07 ? 273 HIS A CB 1 ATOM 2141 C CG . HIS A 1 273 ? -8.920 2.747 10.333 1.00 35.47 ? 273 HIS A CG 1 ATOM 2142 N ND1 . HIS A 1 273 ? -8.986 1.376 10.462 1.00 34.98 ? 273 HIS A ND1 1 ATOM 2143 C CD2 . HIS A 1 273 ? -10.201 3.177 10.200 1.00 35.76 ? 273 HIS A CD2 1 ATOM 2144 C CE1 . HIS A 1 273 ? -10.251 0.995 10.431 1.00 34.93 ? 273 HIS A CE1 1 ATOM 2145 N NE2 . HIS A 1 273 ? -11.008 2.069 10.275 1.00 35.62 ? 273 HIS A NE2 1 ATOM 2146 N N . ASN A 1 274 ? -8.729 5.734 8.680 1.00 35.16 ? 274 ASN A N 1 ATOM 2147 C CA . ASN A 1 274 ? -9.841 6.494 8.163 1.00 35.24 ? 274 ASN A CA 1 ATOM 2148 C C . ASN A 1 274 ? -9.676 6.816 6.684 1.00 35.78 ? 274 ASN A C 1 ATOM 2149 O O . ASN A 1 274 ? -10.620 6.678 5.904 1.00 35.80 ? 274 ASN A O 1 ATOM 2150 C CB . ASN A 1 274 ? -10.015 7.754 8.998 1.00 35.02 ? 274 ASN A CB 1 ATOM 2151 C CG . ASN A 1 274 ? -10.687 7.473 10.316 1.00 34.88 ? 274 ASN A CG 1 ATOM 2152 O OD1 . ASN A 1 274 ? -11.007 6.322 10.635 1.00 35.02 ? 274 ASN A OD1 1 ATOM 2153 N ND2 . ASN A 1 274 ? -10.926 8.521 11.088 1.00 34.39 ? 274 ASN A ND2 1 ATOM 2154 N N . ARG A 1 275 ? -8.468 7.214 6.300 1.00 36.05 ? 275 ARG A N 1 ATOM 2155 C CA . ARG A 1 275 ? -8.142 7.414 4.904 1.00 36.59 ? 275 ARG A CA 1 ATOM 2156 C C . ARG A 1 275 ? -8.403 6.150 4.099 1.00 37.35 ? 275 ARG A C 1 ATOM 2157 O O . ARG A 1 275 ? -8.970 6.226 3.008 1.00 37.94 ? 275 ARG A O 1 ATOM 2158 C CB . ARG A 1 275 ? -6.678 7.805 4.756 1.00 36.59 ? 275 ARG A CB 1 ATOM 2159 C CG . ARG A 1 275 ? -6.328 8.343 3.399 1.00 36.19 ? 275 ARG A CG 1 ATOM 2160 C CD . ARG A 1 275 ? -4.837 8.561 3.274 1.00 35.72 ? 275 ARG A CD 1 ATOM 2161 N NE . ARG A 1 275 ? -4.119 7.298 3.191 1.00 36.01 ? 275 ARG A NE 1 ATOM 2162 C CZ . ARG A 1 275 ? -4.054 6.545 2.100 1.00 37.01 ? 275 ARG A CZ 1 ATOM 2163 N NH1 . ARG A 1 275 ? -4.670 6.931 0.992 1.00 37.68 ? 275 ARG A NH1 1 ATOM 2164 N NH2 . ARG A 1 275 ? -3.374 5.405 2.114 1.00 37.63 ? 275 ARG A NH2 1 ATOM 2165 N N . LEU A 1 276 ? -7.984 4.997 4.633 1.00 37.96 ? 276 LEU A N 1 ATOM 2166 C CA . LEU A 1 276 ? -8.119 3.722 3.931 1.00 38.29 ? 276 LEU A CA 1 ATOM 2167 C C . LEU A 1 276 ? -9.575 3.378 3.761 1.00 39.44 ? 276 LEU A C 1 ATOM 2168 O O . LEU A 1 276 ? -9.979 2.953 2.687 1.00 39.64 ? 276 LEU A O 1 ATOM 2169 C CB . LEU A 1 276 ? -7.421 2.574 4.664 1.00 37.94 ? 276 LEU A CB 1 ATOM 2170 C CG . LEU A 1 276 ? -6.055 1.962 4.307 1.00 36.50 ? 276 LEU A CG 1 ATOM 2171 C CD1 . LEU A 1 276 ? -5.454 2.489 3.031 1.00 34.61 ? 276 LEU A CD1 1 ATOM 2172 C CD2 . LEU A 1 276 ? -5.087 2.121 5.455 1.00 36.72 ? 276 LEU A CD2 1 ATOM 2173 N N . ALA A 1 277 ? -10.356 3.574 4.824 1.00 40.81 ? 277 ALA A N 1 ATOM 2174 C CA . ALA A 1 277 ? -11.786 3.271 4.813 1.00 42.15 ? 277 ALA A CA 1 ATOM 2175 C C . ALA A 1 277 ? -12.554 4.112 3.795 1.00 43.09 ? 277 ALA A C 1 ATOM 2176 O O . ALA A 1 277 ? -13.402 3.585 3.077 1.00 43.71 ? 277 ALA A O 1 ATOM 2177 C CB . ALA A 1 277 ? -12.385 3.432 6.205 1.00 42.03 ? 277 ALA A CB 1 ATOM 2178 N N . ARG A 1 278 ? -12.260 5.409 3.731 1.00 44.28 ? 278 ARG A N 1 ATOM 2179 C CA . ARG A 1 278 ? -12.893 6.301 2.751 1.00 45.47 ? 278 ARG A CA 1 ATOM 2180 C C . ARG A 1 278 ? -12.593 5.844 1.327 1.00 46.00 ? 278 ARG A C 1 ATOM 2181 O O . ARG A 1 278 ? -13.504 5.547 0.538 1.00 45.93 ? 278 ARG A O 1 ATOM 2182 C CB . ARG A 1 278 ? -12.422 7.738 2.944 1.00 45.46 ? 278 ARG A CB 1 ATOM 2183 C CG . ARG A 1 278 ? -13.271 8.511 3.930 1.00 47.34 ? 278 ARG A CG 1 ATOM 2184 C CD . ARG A 1 278 ? -12.819 9.959 4.016 1.00 49.91 ? 278 ARG A CD 1 ATOM 2185 N NE . ARG A 1 278 ? -11.575 10.058 4.774 1.00 52.10 ? 278 ARG A NE 1 ATOM 2186 C CZ . ARG A 1 278 ? -11.510 10.159 6.102 1.00 53.45 ? 278 ARG A CZ 1 ATOM 2187 N NH1 . ARG A 1 278 ? -12.621 10.183 6.844 1.00 52.84 ? 278 ARG A NH1 1 ATOM 2188 N NH2 . ARG A 1 278 ? -10.322 10.240 6.687 1.00 54.58 ? 278 ARG A NH2 1 ATOM 2189 N N . GLU A 1 279 ? -11.303 5.764 1.027 1.00 46.65 ? 279 GLU A N 1 ATOM 2190 C CA . GLU A 1 279 ? -10.834 5.297 -0.259 1.00 47.32 ? 279 GLU A CA 1 ATOM 2191 C C . GLU A 1 279 ? -11.465 3.959 -0.652 1.00 47.59 ? 279 GLU A C 1 ATOM 2192 O O . GLU A 1 279 ? -11.764 3.724 -1.833 1.00 47.61 ? 279 GLU A O 1 ATOM 2193 C CB . GLU A 1 279 ? -9.302 5.204 -0.243 1.00 47.31 ? 279 GLU A CB 1 ATOM 2194 C CG . GLU A 1 279 ? -8.600 6.563 -0.372 1.00 48.46 ? 279 GLU A CG 1 ATOM 2195 C CD . GLU A 1 279 ? -9.112 7.389 -1.565 1.00 50.28 ? 279 GLU A CD 1 ATOM 2196 O OE1 . GLU A 1 279 ? -9.276 6.817 -2.674 1.00 50.91 ? 279 GLU A OE1 1 ATOM 2197 O OE2 . GLU A 1 279 ? -9.356 8.609 -1.388 1.00 50.31 ? 279 GLU A OE2 1 ATOM 2198 N N . LEU A 1 280 ? -11.676 3.102 0.350 1.00 48.00 ? 280 LEU A N 1 ATOM 2199 C CA . LEU A 1 280 ? -12.161 1.738 0.151 1.00 48.43 ? 280 LEU A CA 1 ATOM 2200 C C . LEU A 1 280 ? -13.650 1.750 -0.179 1.00 48.96 ? 280 LEU A C 1 ATOM 2201 O O . LEU A 1 280 ? -14.111 1.002 -1.048 1.00 48.91 ? 280 LEU A O 1 ATOM 2202 C CB . LEU A 1 280 ? -11.914 0.932 1.426 1.00 48.21 ? 280 LEU A CB 1 ATOM 2203 C CG . LEU A 1 280 ? -11.307 -0.473 1.464 1.00 47.88 ? 280 LEU A CG 1 ATOM 2204 C CD1 . LEU A 1 280 ? -10.154 -0.671 0.473 1.00 47.20 ? 280 LEU A CD1 1 ATOM 2205 C CD2 . LEU A 1 280 ? -10.847 -0.749 2.901 1.00 46.46 ? 280 LEU A CD2 1 ATOM 2206 N N . LYS A 1 281 ? -14.390 2.607 0.525 1.00 49.56 ? 281 LYS A N 1 ATOM 2207 C CA . LYS A 1 281 ? -15.813 2.826 0.271 1.00 50.24 ? 281 LYS A CA 1 ATOM 2208 C C . LYS A 1 281 ? -16.056 3.353 -1.154 1.00 50.59 ? 281 LYS A C 1 ATOM 2209 O O . LYS A 1 281 ? -17.064 3.013 -1.774 1.00 50.54 ? 281 LYS A O 1 ATOM 2210 C CB . LYS A 1 281 ? -16.376 3.788 1.323 1.00 50.42 ? 281 LYS A CB 1 ATOM 2211 C CG . LYS A 1 281 ? -17.754 4.363 1.042 1.00 51.06 ? 281 LYS A CG 1 ATOM 2212 C CD . LYS A 1 281 ? -18.888 3.380 1.327 1.00 52.84 ? 281 LYS A CD 1 ATOM 2213 C CE . LYS A 1 281 ? -20.238 4.127 1.249 1.00 54.16 ? 281 LYS A CE 1 ATOM 2214 N NZ . LYS A 1 281 ? -21.404 3.291 1.718 1.00 56.64 ? 281 LYS A NZ 1 ATOM 2215 N N . LYS A 1 282 ? -15.128 4.173 -1.660 1.00 50.92 ? 282 LYS A N 1 ATOM 2216 C CA . LYS A 1 282 ? -15.182 4.686 -3.036 1.00 51.26 ? 282 LYS A CA 1 ATOM 2217 C C . LYS A 1 282 ? -15.139 3.575 -4.072 1.00 51.48 ? 282 LYS A C 1 ATOM 2218 O O . LYS A 1 282 ? -15.942 3.561 -5.012 1.00 51.92 ? 282 LYS A O 1 ATOM 2219 C CB . LYS A 1 282 ? -14.036 5.657 -3.317 1.00 51.18 ? 282 LYS A CB 1 ATOM 2220 C CG . LYS A 1 282 ? -14.402 7.110 -3.157 1.00 51.56 ? 282 LYS A CG 1 ATOM 2221 C CD . LYS A 1 282 ? -13.380 8.008 -3.840 1.00 52.19 ? 282 LYS A CD 1 ATOM 2222 C CE . LYS A 1 282 ? -13.561 9.457 -3.398 1.00 53.30 ? 282 LYS A CE 1 ATOM 2223 N NZ . LYS A 1 282 ? -13.301 9.671 -1.934 1.00 53.56 ? 282 LYS A NZ 1 ATOM 2224 N N . LEU A 1 283 ? -14.191 2.657 -3.911 1.00 51.46 ? 283 LEU A N 1 ATOM 2225 C CA . LEU A 1 283 ? -14.071 1.534 -4.833 1.00 51.43 ? 283 LEU A CA 1 ATOM 2226 C C . LEU A 1 283 ? -15.204 0.527 -4.669 1.00 51.18 ? 283 LEU A C 1 ATOM 2227 O O . LEU A 1 283 ? -15.696 -0.014 -5.661 1.00 51.29 ? 283 LEU A O 1 ATOM 2228 C CB . LEU A 1 283 ? -12.707 0.844 -4.718 1.00 51.58 ? 283 LEU A CB 1 ATOM 2229 C CG . LEU A 1 283 ? -11.639 1.369 -5.682 1.00 52.09 ? 283 LEU A CG 1 ATOM 2230 C CD1 . LEU A 1 283 ? -10.697 2.336 -4.972 1.00 53.39 ? 283 LEU A CD1 1 ATOM 2231 C CD2 . LEU A 1 283 ? -10.853 0.216 -6.289 1.00 52.94 ? 283 LEU A CD2 1 ATOM 2232 N N . ASN A 1 284 ? -15.626 0.294 -3.427 1.00 50.69 ? 284 ASN A N 1 ATOM 2233 C CA . ASN A 1 284 ? -16.629 -0.727 -3.149 1.00 50.33 ? 284 ASN A CA 1 ATOM 2234 C C . ASN A 1 284 ? -17.850 -0.204 -2.376 1.00 50.12 ? 284 ASN A C 1 ATOM 2235 O O . ASN A 1 284 ? -18.010 -0.494 -1.179 1.00 50.14 ? 284 ASN A O 1 ATOM 2236 C CB . ASN A 1 284 ? -15.987 -1.914 -2.438 1.00 50.18 ? 284 ASN A CB 1 ATOM 2237 C CG . ASN A 1 284 ? -14.778 -2.439 -3.175 1.00 50.79 ? 284 ASN A CG 1 ATOM 2238 O OD1 . ASN A 1 284 ? -14.892 -2.973 -4.282 1.00 51.08 ? 284 ASN A OD1 1 ATOM 2239 N ND2 . ASN A 1 284 ? -13.600 -2.287 -2.561 1.00 52.13 ? 284 ASN A ND2 1 ATOM 2240 N N . PRO A 1 285 ? -18.730 0.551 -3.072 1.00 49.63 ? 285 PRO A N 1 ATOM 2241 C CA . PRO A 1 285 ? -19.864 1.217 -2.431 1.00 49.14 ? 285 PRO A CA 1 ATOM 2242 C C . PRO A 1 285 ? -20.821 0.297 -1.692 1.00 48.80 ? 285 PRO A C 1 ATOM 2243 O O . PRO A 1 285 ? -21.550 0.767 -0.825 1.00 48.42 ? 285 PRO A O 1 ATOM 2244 C CB . PRO A 1 285 ? -20.576 1.900 -3.604 1.00 49.34 ? 285 PRO A CB 1 ATOM 2245 C CG . PRO A 1 285 ? -19.491 2.083 -4.645 1.00 49.36 ? 285 PRO A CG 1 ATOM 2246 C CD . PRO A 1 285 ? -18.688 0.829 -4.523 1.00 49.41 ? 285 PRO A CD 1 ATOM 2247 N N . GLN A 1 286 ? -20.808 -0.998 -2.009 1.00 48.93 ? 286 GLN A N 1 ATOM 2248 C CA . GLN A 1 286 ? -21.761 -1.945 -1.390 1.00 49.04 ? 286 GLN A CA 1 ATOM 2249 C C . GLN A 1 286 ? -21.322 -2.416 -0.007 1.00 48.91 ? 286 GLN A C 1 ATOM 2250 O O . GLN A 1 286 ? -22.142 -2.918 0.774 1.00 48.79 ? 286 GLN A O 1 ATOM 2251 C CB . GLN A 1 286 ? -21.991 -3.177 -2.274 1.00 49.07 ? 286 GLN A CB 1 ATOM 2252 C CG . GLN A 1 286 ? -21.341 -3.115 -3.636 1.00 50.01 ? 286 GLN A CG 1 ATOM 2253 C CD . GLN A 1 286 ? -19.886 -3.538 -3.596 1.00 50.28 ? 286 GLN A CD 1 ATOM 2254 O OE1 . GLN A 1 286 ? -19.541 -4.558 -2.996 1.00 50.99 ? 286 GLN A OE1 1 ATOM 2255 N NE2 . GLN A 1 286 ? -19.027 -2.765 -4.247 1.00 49.91 ? 286 GLN A NE2 1 ATOM 2256 N N . TRP A 1 287 ? -20.028 -2.252 0.275 1.00 48.79 ? 287 TRP A N 1 ATOM 2257 C CA . TRP A 1 287 ? -19.391 -2.770 1.482 1.00 48.43 ? 287 TRP A CA 1 ATOM 2258 C C . TRP A 1 287 ? -19.941 -2.231 2.809 1.00 48.37 ? 287 TRP A C 1 ATOM 2259 O O . TRP A 1 287 ? -20.345 -1.065 2.907 1.00 48.15 ? 287 TRP A O 1 ATOM 2260 C CB . TRP A 1 287 ? -17.877 -2.565 1.395 1.00 48.47 ? 287 TRP A CB 1 ATOM 2261 C CG . TRP A 1 287 ? -17.136 -3.688 0.724 1.00 48.44 ? 287 TRP A CG 1 ATOM 2262 C CD1 . TRP A 1 287 ? -17.679 -4.763 0.079 1.00 48.34 ? 287 TRP A CD1 1 ATOM 2263 C CD2 . TRP A 1 287 ? -15.712 -3.835 0.616 1.00 48.37 ? 287 TRP A CD2 1 ATOM 2264 N NE1 . TRP A 1 287 ? -16.685 -5.577 -0.409 1.00 48.08 ? 287 TRP A NE1 1 ATOM 2265 C CE2 . TRP A 1 287 ? -15.469 -5.027 -0.100 1.00 48.01 ? 287 TRP A CE2 1 ATOM 2266 C CE3 . TRP A 1 287 ? -14.618 -3.079 1.064 1.00 48.33 ? 287 TRP A CE3 1 ATOM 2267 C CZ2 . TRP A 1 287 ? -14.178 -5.481 -0.383 1.00 48.27 ? 287 TRP A CZ2 1 ATOM 2268 C CZ3 . TRP A 1 287 ? -13.335 -3.532 0.781 1.00 48.25 ? 287 TRP A CZ3 1 ATOM 2269 C CH2 . TRP A 1 287 ? -13.127 -4.721 0.061 1.00 48.22 ? 287 TRP A CH2 1 ATOM 2270 N N . ASP A 1 288 ? -19.920 -3.117 3.814 1.00 48.40 ? 288 ASP A N 1 ATOM 2271 C CA . ASP A 1 288 ? -20.364 -2.884 5.202 1.00 48.24 ? 288 ASP A CA 1 ATOM 2272 C C . ASP A 1 288 ? -19.558 -1.850 5.997 1.00 47.13 ? 288 ASP A C 1 ATOM 2273 O O . ASP A 1 288 ? -18.400 -1.578 5.690 1.00 46.89 ? 288 ASP A O 1 ATOM 2274 C CB . ASP A 1 288 ? -20.165 -4.187 5.977 1.00 49.02 ? 288 ASP A CB 1 ATOM 2275 C CG . ASP A 1 288 ? -21.344 -5.075 5.931 1.00 51.11 ? 288 ASP A CG 1 ATOM 2276 O OD1 . ASP A 1 288 ? -22.331 -4.731 6.606 1.00 54.61 ? 288 ASP A OD1 1 ATOM 2277 O OD2 . ASP A 1 288 ? -21.275 -6.126 5.254 1.00 53.62 ? 288 ASP A OD2 1 ATOM 2278 N N . GLY A 1 289 ? -20.158 -1.342 7.069 1.00 46.06 ? 289 GLY A N 1 ATOM 2279 C CA . GLY A 1 289 ? -19.402 -0.671 8.125 1.00 45.19 ? 289 GLY A CA 1 ATOM 2280 C C . GLY A 1 289 ? -18.285 -1.579 8.640 1.00 44.40 ? 289 GLY A C 1 ATOM 2281 O O . GLY A 1 289 ? -17.114 -1.176 8.680 1.00 44.71 ? 289 GLY A O 1 ATOM 2282 N N . GLU A 1 290 ? -18.647 -2.811 8.998 1.00 42.99 ? 290 GLU A N 1 ATOM 2283 C CA . GLU A 1 290 ? -17.710 -3.817 9.478 1.00 41.72 ? 290 GLU A CA 1 ATOM 2284 C C . GLU A 1 290 ? -16.669 -4.193 8.428 1.00 40.84 ? 290 GLU A C 1 ATOM 2285 O O . GLU A 1 290 ? -15.479 -4.234 8.719 1.00 40.87 ? 290 GLU A O 1 ATOM 2286 C CB . GLU A 1 290 ? -18.468 -5.063 9.913 1.00 41.89 ? 290 GLU A CB 1 ATOM 2287 C CG . GLU A 1 290 ? -17.618 -6.177 10.516 1.00 42.35 ? 290 GLU A CG 1 ATOM 2288 C CD . GLU A 1 290 ? -17.155 -5.873 11.924 1.00 43.07 ? 290 GLU A CD 1 ATOM 2289 O OE1 . GLU A 1 290 ? -17.729 -4.964 12.559 1.00 42.03 ? 290 GLU A OE1 1 ATOM 2290 O OE2 . GLU A 1 290 ? -16.209 -6.550 12.392 1.00 44.53 ? 290 GLU A OE2 1 ATOM 2291 N N . LYS A 1 291 ? -17.122 -4.473 7.213 1.00 39.81 ? 291 LYS A N 1 ATOM 2292 C CA . LYS A 1 291 ? -16.230 -4.859 6.117 1.00 38.83 ? 291 LYS A CA 1 ATOM 2293 C C . LYS A 1 291 ? -15.235 -3.750 5.810 1.00 38.03 ? 291 LYS A C 1 ATOM 2294 O O . LYS A 1 291 ? -14.063 -4.010 5.540 1.00 37.47 ? 291 LYS A O 1 ATOM 2295 C CB . LYS A 1 291 ? -17.042 -5.200 4.866 1.00 39.02 ? 291 LYS A CB 1 ATOM 2296 C CG . LYS A 1 291 ? -16.230 -5.574 3.656 1.00 39.14 ? 291 LYS A CG 1 ATOM 2297 C CD . LYS A 1 291 ? -15.980 -7.055 3.613 1.00 40.87 ? 291 LYS A CD 1 ATOM 2298 C CE . LYS A 1 291 ? -15.718 -7.507 2.190 1.00 41.65 ? 291 LYS A CE 1 ATOM 2299 N NZ . LYS A 1 291 ? -15.127 -8.865 2.168 1.00 43.16 ? 291 LYS A NZ 1 ATOM 2300 N N . LEU A 1 292 ? -15.704 -2.509 5.858 1.00 37.35 ? 292 LEU A N 1 ATOM 2301 C CA . LEU A 1 292 ? -14.799 -1.380 5.707 1.00 36.78 ? 292 LEU A CA 1 ATOM 2302 C C . LEU A 1 292 ? -13.749 -1.370 6.822 1.00 36.09 ? 292 LEU A C 1 ATOM 2303 O O . LEU A 1 292 ? -12.569 -1.198 6.548 1.00 35.55 ? 292 LEU A O 1 ATOM 2304 C CB . LEU A 1 292 ? -15.560 -0.044 5.615 1.00 36.86 ? 292 LEU A CB 1 ATOM 2305 C CG . LEU A 1 292 ? -15.953 0.438 4.203 1.00 37.03 ? 292 LEU A CG 1 ATOM 2306 C CD1 . LEU A 1 292 ? -14.883 0.145 3.157 1.00 37.30 ? 292 LEU A CD1 1 ATOM 2307 C CD2 . LEU A 1 292 ? -17.246 -0.132 3.740 1.00 36.20 ? 292 LEU A CD2 1 ATOM 2308 N N . TYR A 1 293 ? -14.194 -1.598 8.058 1.00 35.58 ? 293 TYR A N 1 ATOM 2309 C CA . TYR A 1 293 ? -13.330 -1.579 9.231 1.00 35.21 ? 293 TYR A CA 1 ATOM 2310 C C . TYR A 1 293 ? -12.231 -2.632 9.169 1.00 35.08 ? 293 TYR A C 1 ATOM 2311 O O . TYR A 1 293 ? -11.041 -2.296 9.224 1.00 34.76 ? 293 TYR A O 1 ATOM 2312 C CB . TYR A 1 293 ? -14.165 -1.780 10.488 1.00 35.04 ? 293 TYR A CB 1 ATOM 2313 C CG . TYR A 1 293 ? -13.378 -1.986 11.773 1.00 34.51 ? 293 TYR A CG 1 ATOM 2314 C CD1 . TYR A 1 293 ? -12.840 -0.894 12.476 1.00 33.98 ? 293 TYR A CD1 1 ATOM 2315 C CD2 . TYR A 1 293 ? -13.215 -3.263 12.310 1.00 33.67 ? 293 TYR A CD2 1 ATOM 2316 C CE1 . TYR A 1 293 ? -12.148 -1.075 13.675 1.00 33.19 ? 293 TYR A CE1 1 ATOM 2317 C CE2 . TYR A 1 293 ? -12.525 -3.461 13.509 1.00 33.73 ? 293 TYR A CE2 1 ATOM 2318 C CZ . TYR A 1 293 ? -11.993 -2.363 14.189 1.00 33.52 ? 293 TYR A CZ 1 ATOM 2319 O OH . TYR A 1 293 ? -11.312 -2.565 15.371 1.00 31.16 ? 293 TYR A OH 1 ATOM 2320 N N . GLN A 1 294 ? -12.644 -3.893 9.047 1.00 34.91 ? 294 GLN A N 1 ATOM 2321 C CA . GLN A 1 294 ? -11.730 -5.035 9.003 1.00 34.94 ? 294 GLN A CA 1 ATOM 2322 C C . GLN A 1 294 ? -10.744 -4.941 7.839 1.00 35.07 ? 294 GLN A C 1 ATOM 2323 O O . GLN A 1 294 ? -9.557 -5.209 8.012 1.00 35.30 ? 294 GLN A O 1 ATOM 2324 C CB . GLN A 1 294 ? -12.506 -6.359 8.936 1.00 34.88 ? 294 GLN A CB 1 ATOM 2325 C CG . GLN A 1 294 ? -13.474 -6.624 10.121 1.00 34.16 ? 294 GLN A CG 1 ATOM 2326 C CD . GLN A 1 294 ? -12.780 -7.028 11.431 1.00 32.75 ? 294 GLN A CD 1 ATOM 2327 O OE1 . GLN A 1 294 ? -11.566 -7.226 11.486 1.00 30.42 ? 294 GLN A OE1 1 ATOM 2328 N NE2 . GLN A 1 294 ? -13.569 -7.147 12.493 1.00 32.36 ? 294 GLN A NE2 1 ATOM 2329 N N . GLU A 1 295 ? -11.229 -4.544 6.666 1.00 35.06 ? 295 GLU A N 1 ATOM 2330 C CA . GLU A 1 295 ? -10.369 -4.448 5.487 1.00 35.42 ? 295 GLU A CA 1 ATOM 2331 C C . GLU A 1 295 ? -9.301 -3.360 5.605 1.00 35.33 ? 295 GLU A C 1 ATOM 2332 O O . GLU A 1 295 ? -8.152 -3.578 5.204 1.00 35.66 ? 295 GLU A O 1 ATOM 2333 C CB . GLU A 1 295 ? -11.186 -4.273 4.205 1.00 35.46 ? 295 GLU A CB 1 ATOM 2334 C CG . GLU A 1 295 ? -11.930 -5.536 3.766 1.00 36.13 ? 295 GLU A CG 1 ATOM 2335 C CD . GLU A 1 295 ? -11.039 -6.595 3.135 1.00 35.76 ? 295 GLU A CD 1 ATOM 2336 O OE1 . GLU A 1 295 ? -10.087 -6.241 2.409 1.00 36.32 ? 295 GLU A OE1 1 ATOM 2337 O OE2 . GLU A 1 295 ? -11.314 -7.791 3.346 1.00 35.05 ? 295 GLU A OE2 1 ATOM 2338 N N . ALA A 1 296 ? -9.672 -2.202 6.145 1.00 34.77 ? 296 ALA A N 1 ATOM 2339 C CA . ALA A 1 296 ? -8.700 -1.148 6.434 1.00 34.81 ? 296 ALA A CA 1 ATOM 2340 C C . ALA A 1 296 ? -7.711 -1.623 7.513 1.00 34.94 ? 296 ALA A C 1 ATOM 2341 O O . ALA A 1 296 ? -6.487 -1.487 7.354 1.00 34.72 ? 296 ALA A O 1 ATOM 2342 C CB . ALA A 1 296 ? -9.404 0.129 6.862 1.00 34.70 ? 296 ALA A CB 1 ATOM 2343 N N . ARG A 1 297 ? -8.264 -2.206 8.582 1.00 34.91 ? 297 ARG A N 1 ATOM 2344 C CA . ARG A 1 297 ? -7.508 -2.802 9.688 1.00 34.86 ? 297 ARG A CA 1 ATOM 2345 C C . ARG A 1 297 ? -6.459 -3.832 9.251 1.00 34.81 ? 297 ARG A C 1 ATOM 2346 O O . ARG A 1 297 ? -5.331 -3.843 9.758 1.00 35.04 ? 297 ARG A O 1 ATOM 2347 C CB . ARG A 1 297 ? -8.478 -3.439 10.685 1.00 34.79 ? 297 ARG A CB 1 ATOM 2348 C CG . ARG A 1 297 ? -7.822 -4.280 11.756 1.00 35.26 ? 297 ARG A CG 1 ATOM 2349 C CD . ARG A 1 297 ? -8.750 -4.488 12.918 1.00 35.78 ? 297 ARG A CD 1 ATOM 2350 N NE . ARG A 1 297 ? -8.152 -5.375 13.914 1.00 36.11 ? 297 ARG A NE 1 ATOM 2351 C CZ . ARG A 1 297 ? -8.383 -6.683 14.004 1.00 36.29 ? 297 ARG A CZ 1 ATOM 2352 N NH1 . ARG A 1 297 ? -9.210 -7.291 13.161 1.00 35.13 ? 297 ARG A NH1 1 ATOM 2353 N NH2 . ARG A 1 297 ? -7.786 -7.387 14.954 1.00 36.60 ? 297 ARG A NH2 1 ATOM 2354 N N . LYS A 1 298 ? -6.841 -4.692 8.315 1.00 34.86 ? 298 LYS A N 1 ATOM 2355 C CA . LYS A 1 298 ? -5.951 -5.721 7.805 1.00 34.64 ? 298 LYS A CA 1 ATOM 2356 C C . LYS A 1 298 ? -4.833 -5.081 6.985 1.00 34.67 ? 298 LYS A C 1 ATOM 2357 O O . LYS A 1 298 ? -3.676 -5.485 7.104 1.00 35.18 ? 298 LYS A O 1 ATOM 2358 C CB . LYS A 1 298 ? -6.753 -6.726 6.986 1.00 34.62 ? 298 LYS A CB 1 ATOM 2359 C CG . LYS A 1 298 ? -5.984 -7.896 6.428 1.00 34.95 ? 298 LYS A CG 1 ATOM 2360 C CD . LYS A 1 298 ? -6.951 -8.882 5.767 1.00 35.51 ? 298 LYS A CD 1 ATOM 2361 C CE . LYS A 1 298 ? -6.240 -9.786 4.770 1.00 33.56 ? 298 LYS A CE 1 ATOM 2362 N NZ . LYS A 1 298 ? -6.977 -11.065 4.610 1.00 33.29 ? 298 LYS A NZ 1 ATOM 2363 N N . ILE A 1 299 ? -5.167 -4.078 6.173 1.00 34.50 ? 299 ILE A N 1 ATOM 2364 C CA . ILE A 1 299 ? -4.136 -3.314 5.450 1.00 34.65 ? 299 ILE A CA 1 ATOM 2365 C C . ILE A 1 299 ? -3.095 -2.672 6.408 1.00 34.14 ? 299 ILE A C 1 ATOM 2366 O O . ILE A 1 299 ? -1.893 -2.802 6.184 1.00 33.89 ? 299 ILE A O 1 ATOM 2367 C CB . ILE A 1 299 ? -4.744 -2.247 4.495 1.00 34.59 ? 299 ILE A CB 1 ATOM 2368 C CG1 . ILE A 1 299 ? -5.307 -2.906 3.231 1.00 34.96 ? 299 ILE A CG1 1 ATOM 2369 C CG2 . ILE A 1 299 ? -3.697 -1.210 4.089 1.00 34.72 ? 299 ILE A CG2 1 ATOM 2370 C CD1 . ILE A 1 299 ? -6.340 -2.031 2.502 1.00 33.60 ? 299 ILE A CD1 1 ATOM 2371 N N . LEU A 1 300 ? -3.579 -2.012 7.463 1.00 33.66 ? 300 LEU A N 1 ATOM 2372 C CA . LEU A 1 300 ? -2.736 -1.359 8.465 1.00 33.28 ? 300 LEU A CA 1 ATOM 2373 C C . LEU A 1 300 ? -1.774 -2.322 9.173 1.00 33.02 ? 300 LEU A C 1 ATOM 2374 O O . LEU A 1 300 ? -0.595 -1.992 9.384 1.00 32.28 ? 300 LEU A O 1 ATOM 2375 C CB . LEU A 1 300 ? -3.600 -0.629 9.502 1.00 33.09 ? 300 LEU A CB 1 ATOM 2376 C CG . LEU A 1 300 ? -2.843 0.448 10.290 1.00 33.91 ? 300 LEU A CG 1 ATOM 2377 C CD1 . LEU A 1 300 ? -2.418 1.574 9.374 1.00 35.07 ? 300 LEU A CD1 1 ATOM 2378 C CD2 . LEU A 1 300 ? -3.662 1.004 11.430 1.00 35.29 ? 300 LEU A CD2 1 ATOM 2379 N N . GLY A 1 301 ? -2.289 -3.499 9.543 1.00 32.56 ? 301 GLY A N 1 ATOM 2380 C CA . GLY A 1 301 ? -1.472 -4.539 10.172 1.00 32.35 ? 301 GLY A CA 1 ATOM 2381 C C . GLY A 1 301 ? -0.342 -4.969 9.245 1.00 32.22 ? 301 GLY A C 1 ATOM 2382 O O . GLY A 1 301 ? 0.786 -5.221 9.686 1.00 32.20 ? 301 GLY A O 1 ATOM 2383 N N . ALA A 1 302 ? -0.664 -5.030 7.953 1.00 32.00 ? 302 ALA A N 1 ATOM 2384 C CA . ALA A 1 302 ? 0.281 -5.376 6.907 1.00 31.47 ? 302 ALA A CA 1 ATOM 2385 C C . ALA A 1 302 ? 1.331 -4.282 6.800 1.00 31.25 ? 302 ALA A C 1 ATOM 2386 O O . ALA A 1 302 ? 2.506 -4.557 6.557 1.00 31.92 ? 302 ALA A O 1 ATOM 2387 C CB . ALA A 1 302 ? -0.446 -5.551 5.587 1.00 31.25 ? 302 ALA A CB 1 ATOM 2388 N N . PHE A 1 303 ? 0.908 -3.039 6.998 1.00 30.33 ? 303 PHE A N 1 ATOM 2389 C CA . PHE A 1 303 ? 1.824 -1.923 6.942 1.00 29.56 ? 303 PHE A CA 1 ATOM 2390 C C . PHE A 1 303 ? 2.858 -2.025 8.069 1.00 29.30 ? 303 PHE A C 1 ATOM 2391 O O . PHE A 1 303 ? 4.061 -2.043 7.810 1.00 29.19 ? 303 PHE A O 1 ATOM 2392 C CB . PHE A 1 303 ? 1.069 -0.587 6.984 1.00 29.28 ? 303 PHE A CB 1 ATOM 2393 C CG . PHE A 1 303 ? 1.962 0.606 7.195 1.00 28.20 ? 303 PHE A CG 1 ATOM 2394 C CD1 . PHE A 1 303 ? 2.599 1.206 6.124 1.00 28.26 ? 303 PHE A CD1 1 ATOM 2395 C CD2 . PHE A 1 303 ? 2.172 1.121 8.472 1.00 27.44 ? 303 PHE A CD2 1 ATOM 2396 C CE1 . PHE A 1 303 ? 3.430 2.305 6.319 1.00 28.39 ? 303 PHE A CE1 1 ATOM 2397 C CE2 . PHE A 1 303 ? 2.991 2.210 8.671 1.00 26.76 ? 303 PHE A CE2 1 ATOM 2398 C CZ . PHE A 1 303 ? 3.626 2.797 7.595 1.00 28.01 ? 303 PHE A CZ 1 ATOM 2399 N N . VAL A 1 304 ? 2.375 -2.103 9.307 1.00 29.16 ? 304 VAL A N 1 ATOM 2400 C CA . VAL A 1 304 ? 3.237 -2.182 10.491 1.00 28.99 ? 304 VAL A CA 1 ATOM 2401 C C . VAL A 1 304 ? 4.233 -3.350 10.367 1.00 29.05 ? 304 VAL A C 1 ATOM 2402 O O . VAL A 1 304 ? 5.395 -3.228 10.763 1.00 28.64 ? 304 VAL A O 1 ATOM 2403 C CB . VAL A 1 304 ? 2.393 -2.292 11.783 1.00 28.99 ? 304 VAL A CB 1 ATOM 2404 C CG1 . VAL A 1 304 ? 3.278 -2.445 13.019 1.00 28.94 ? 304 VAL A CG1 1 ATOM 2405 C CG2 . VAL A 1 304 ? 1.491 -1.072 11.936 1.00 29.25 ? 304 VAL A CG2 1 ATOM 2406 N N . GLN A 1 305 ? 3.773 -4.456 9.777 1.00 28.86 ? 305 GLN A N 1 ATOM 2407 C CA . GLN A 1 305 ? 4.612 -5.626 9.544 1.00 28.98 ? 305 GLN A CA 1 ATOM 2408 C C . GLN A 1 305 ? 5.710 -5.364 8.526 1.00 28.86 ? 305 GLN A C 1 ATOM 2409 O O . GLN A 1 305 ? 6.867 -5.706 8.754 1.00 29.18 ? 305 GLN A O 1 ATOM 2410 C CB . GLN A 1 305 ? 3.759 -6.823 9.124 1.00 28.81 ? 305 GLN A CB 1 ATOM 2411 C CG . GLN A 1 305 ? 2.969 -7.434 10.280 1.00 29.86 ? 305 GLN A CG 1 ATOM 2412 C CD . GLN A 1 305 ? 2.186 -8.660 9.871 1.00 30.61 ? 305 GLN A CD 1 ATOM 2413 O OE1 . GLN A 1 305 ? 2.037 -8.928 8.680 1.00 31.50 ? 305 GLN A OE1 1 ATOM 2414 N NE2 . GLN A 1 305 ? 1.671 -9.410 10.855 1.00 29.33 ? 305 GLN A NE2 1 ATOM 2415 N N . ILE A 1 306 ? 5.346 -4.734 7.413 1.00 29.05 ? 306 ILE A N 1 ATOM 2416 C CA . ILE A 1 306 ? 6.286 -4.480 6.312 1.00 28.72 ? 306 ILE A CA 1 ATOM 2417 C C . ILE A 1 306 ? 7.380 -3.497 6.729 1.00 28.19 ? 306 ILE A C 1 ATOM 2418 O O . ILE A 1 306 ? 8.556 -3.820 6.638 1.00 28.34 ? 306 ILE A O 1 ATOM 2419 C CB . ILE A 1 306 ? 5.549 -4.063 4.988 1.00 28.89 ? 306 ILE A CB 1 ATOM 2420 C CG1 . ILE A 1 306 ? 4.751 -5.253 4.438 1.00 28.55 ? 306 ILE A CG1 1 ATOM 2421 C CG2 . ILE A 1 306 ? 6.534 -3.533 3.938 1.00 27.82 ? 306 ILE A CG2 1 ATOM 2422 C CD1 . ILE A 1 306 ? 3.878 -4.915 3.235 1.00 29.43 ? 306 ILE A CD1 1 ATOM 2423 N N . ILE A 1 307 ? 7.003 -2.325 7.221 1.00 27.72 ? 307 ILE A N 1 ATOM 2424 C CA . ILE A 1 307 ? 8.003 -1.374 7.694 1.00 27.86 ? 307 ILE A CA 1 ATOM 2425 C C . ILE A 1 307 ? 8.941 -1.990 8.739 1.00 27.69 ? 307 ILE A C 1 ATOM 2426 O O . ILE A 1 307 ? 10.171 -1.808 8.669 1.00 27.21 ? 307 ILE A O 1 ATOM 2427 C CB . ILE A 1 307 ? 7.391 -0.052 8.258 1.00 27.82 ? 307 ILE A CB 1 ATOM 2428 C CG1 . ILE A 1 307 ? 6.304 0.519 7.336 1.00 28.81 ? 307 ILE A CG1 1 ATOM 2429 C CG2 . ILE A 1 307 ? 8.494 0.997 8.460 1.00 28.39 ? 307 ILE A CG2 1 ATOM 2430 C CD1 . ILE A 1 307 ? 6.750 0.828 5.898 1.00 28.96 ? 307 ILE A CD1 1 ATOM 2431 N N . THR A 1 308 ? 8.361 -2.716 9.694 1.00 27.62 ? 308 THR A N 1 ATOM 2432 C CA . THR A 1 308 ? 9.138 -3.356 10.755 1.00 28.10 ? 308 THR A CA 1 ATOM 2433 C C . THR A 1 308 ? 10.146 -4.375 10.208 1.00 28.39 ? 308 THR A C 1 ATOM 2434 O O . THR A 1 308 ? 11.325 -4.339 10.575 1.00 28.52 ? 308 THR A O 1 ATOM 2435 C CB . THR A 1 308 ? 8.226 -4.038 11.807 1.00 28.04 ? 308 THR A CB 1 ATOM 2436 O OG1 . THR A 1 308 ? 7.393 -3.049 12.423 1.00 27.63 ? 308 THR A OG1 1 ATOM 2437 C CG2 . THR A 1 308 ? 9.061 -4.754 12.887 1.00 28.18 ? 308 THR A CG2 1 ATOM 2438 N N . PHE A 1 309 ? 9.689 -5.271 9.336 1.00 28.46 ? 309 PHE A N 1 ATOM 2439 C CA . PHE A 1 309 ? 10.555 -6.343 8.850 1.00 28.80 ? 309 PHE A CA 1 ATOM 2440 C C . PHE A 1 309 ? 11.428 -5.955 7.660 1.00 29.54 ? 309 PHE A C 1 ATOM 2441 O O . PHE A 1 309 ? 12.553 -6.459 7.533 1.00 29.36 ? 309 PHE A O 1 ATOM 2442 C CB . PHE A 1 309 ? 9.762 -7.627 8.596 1.00 28.24 ? 309 PHE A CB 1 ATOM 2443 C CG . PHE A 1 309 ? 9.628 -8.503 9.824 1.00 28.00 ? 309 PHE A CG 1 ATOM 2444 C CD1 . PHE A 1 309 ? 8.822 -8.116 10.891 1.00 26.03 ? 309 PHE A CD1 1 ATOM 2445 C CD2 . PHE A 1 309 ? 10.329 -9.705 9.922 1.00 26.14 ? 309 PHE A CD2 1 ATOM 2446 C CE1 . PHE A 1 309 ? 8.696 -8.925 12.020 1.00 25.12 ? 309 PHE A CE1 1 ATOM 2447 C CE2 . PHE A 1 309 ? 10.213 -10.511 11.046 1.00 25.12 ? 309 PHE A CE2 1 ATOM 2448 C CZ . PHE A 1 309 ? 9.394 -10.123 12.096 1.00 24.41 ? 309 PHE A CZ 1 ATOM 2449 N N . ARG A 1 310 ? 10.931 -5.045 6.817 1.00 29.78 ? 310 ARG A N 1 ATOM 2450 C CA . ARG A 1 310 ? 11.721 -4.566 5.685 1.00 30.44 ? 310 ARG A CA 1 ATOM 2451 C C . ARG A 1 310 ? 12.656 -3.394 5.999 1.00 30.65 ? 310 ARG A C 1 ATOM 2452 O O . ARG A 1 310 ? 13.796 -3.383 5.530 1.00 30.77 ? 310 ARG A O 1 ATOM 2453 C CB . ARG A 1 310 ? 10.843 -4.221 4.480 1.00 30.44 ? 310 ARG A CB 1 ATOM 2454 C CG . ARG A 1 310 ? 11.634 -3.633 3.309 1.00 30.54 ? 310 ARG A CG 1 ATOM 2455 C CD . ARG A 1 310 ? 10.725 -2.948 2.318 1.00 30.20 ? 310 ARG A CD 1 ATOM 2456 N NE . ARG A 1 310 ? 10.274 -1.644 2.792 1.00 29.09 ? 310 ARG A NE 1 ATOM 2457 C CZ . ARG A 1 310 ? 9.144 -1.065 2.407 1.00 27.10 ? 310 ARG A CZ 1 ATOM 2458 N NH1 . ARG A 1 310 ? 8.346 -1.686 1.551 1.00 25.22 ? 310 ARG A NH1 1 ATOM 2459 N NH2 . ARG A 1 310 ? 8.806 0.125 2.892 1.00 25.74 ? 310 ARG A NH2 1 ATOM 2460 N N . ASP A 1 311 ? 12.183 -2.413 6.770 1.00 30.99 ? 311 ASP A N 1 ATOM 2461 C CA . ASP A 1 311 ? 12.952 -1.166 6.980 1.00 31.15 ? 311 ASP A CA 1 ATOM 2462 C C . ASP A 1 311 ? 13.631 -1.027 8.346 1.00 31.33 ? 311 ASP A C 1 ATOM 2463 O O . ASP A 1 311 ? 14.676 -0.392 8.455 1.00 31.88 ? 311 ASP A O 1 ATOM 2464 C CB . ASP A 1 311 ? 12.078 0.079 6.762 1.00 30.92 ? 311 ASP A CB 1 ATOM 2465 C CG . ASP A 1 311 ? 11.371 0.089 5.416 1.00 30.70 ? 311 ASP A CG 1 ATOM 2466 O OD1 . ASP A 1 311 ? 11.936 -0.411 4.414 1.00 30.88 ? 311 ASP A OD1 1 ATOM 2467 O OD2 . ASP A 1 311 ? 10.241 0.615 5.361 1.00 28.98 ? 311 ASP A OD2 1 ATOM 2468 N N . TYR A 1 312 ? 13.029 -1.592 9.385 1.00 31.06 ? 312 TYR A N 1 ATOM 2469 C CA . TYR A 1 312 ? 13.459 -1.309 10.742 1.00 30.95 ? 312 TYR A CA 1 ATOM 2470 C C . TYR A 1 312 ? 14.410 -2.363 11.314 1.00 31.34 ? 312 TYR A C 1 ATOM 2471 O O . TYR A 1 312 ? 15.474 -2.022 11.846 1.00 31.77 ? 312 TYR A O 1 ATOM 2472 C CB . TYR A 1 312 ? 12.242 -1.101 11.654 1.00 30.81 ? 312 TYR A CB 1 ATOM 2473 C CG . TYR A 1 312 ? 12.591 -0.990 13.113 1.00 30.26 ? 312 TYR A CG 1 ATOM 2474 C CD1 . TYR A 1 312 ? 13.135 0.189 13.632 1.00 29.66 ? 312 TYR A CD1 1 ATOM 2475 C CD2 . TYR A 1 312 ? 12.391 -2.069 13.978 1.00 28.75 ? 312 TYR A CD2 1 ATOM 2476 C CE1 . TYR A 1 312 ? 13.467 0.291 14.984 1.00 29.86 ? 312 TYR A CE1 1 ATOM 2477 C CE2 . TYR A 1 312 ? 12.712 -1.979 15.323 1.00 29.14 ? 312 TYR A CE2 1 ATOM 2478 C CZ . TYR A 1 312 ? 13.253 -0.798 15.823 1.00 29.94 ? 312 TYR A CZ 1 ATOM 2479 O OH . TYR A 1 312 ? 13.588 -0.714 17.155 1.00 30.11 ? 312 TYR A OH 1 ATOM 2480 N N . LEU A 1 313 ? 14.029 -3.636 11.214 1.00 31.19 ? 313 LEU A N 1 ATOM 2481 C CA . LEU A 1 313 ? 14.836 -4.717 11.775 1.00 30.98 ? 313 LEU A CA 1 ATOM 2482 C C . LEU A 1 313 ? 16.225 -4.870 11.157 1.00 31.25 ? 313 LEU A C 1 ATOM 2483 O O . LEU A 1 313 ? 17.189 -5.071 11.899 1.00 31.59 ? 313 LEU A O 1 ATOM 2484 C CB . LEU A 1 313 ? 14.091 -6.051 11.753 1.00 30.79 ? 313 LEU A CB 1 ATOM 2485 C CG . LEU A 1 313 ? 13.087 -6.235 12.881 1.00 30.73 ? 313 LEU A CG 1 ATOM 2486 C CD1 . LEU A 1 313 ? 12.526 -7.653 12.873 1.00 30.59 ? 313 LEU A CD1 1 ATOM 2487 C CD2 . LEU A 1 313 ? 13.712 -5.906 14.235 1.00 30.30 ? 313 LEU A CD2 1 ATOM 2488 N N . PRO A 1 314 ? 16.344 -4.793 9.809 1.00 31.20 ? 314 PRO A N 1 ATOM 2489 C CA . PRO A 1 314 ? 17.689 -4.923 9.240 1.00 31.26 ? 314 PRO A CA 1 ATOM 2490 C C . PRO A 1 314 ? 18.723 -3.954 9.814 1.00 31.34 ? 314 PRO A C 1 ATOM 2491 O O . PRO A 1 314 ? 19.906 -4.258 9.786 1.00 31.78 ? 314 PRO A O 1 ATOM 2492 C CB . PRO A 1 314 ? 17.466 -4.653 7.747 1.00 30.86 ? 314 PRO A CB 1 ATOM 2493 C CG . PRO A 1 314 ? 16.079 -5.097 7.505 1.00 31.31 ? 314 PRO A CG 1 ATOM 2494 C CD . PRO A 1 314 ? 15.328 -4.658 8.741 1.00 31.01 ? 314 PRO A CD 1 ATOM 2495 N N . ILE A 1 315 ? 18.285 -2.812 10.333 1.00 31.43 ? 315 ILE A N 1 ATOM 2496 C CA . ILE A 1 315 ? 19.217 -1.815 10.867 1.00 31.47 ? 315 ILE A CA 1 ATOM 2497 C C . ILE A 1 315 ? 19.321 -1.830 12.399 1.00 31.79 ? 315 ILE A C 1 ATOM 2498 O O . ILE A 1 315 ? 20.040 -1.020 12.977 1.00 32.40 ? 315 ILE A O 1 ATOM 2499 C CB . ILE A 1 315 ? 18.932 -0.373 10.331 1.00 31.09 ? 315 ILE A CB 1 ATOM 2500 C CG1 . ILE A 1 315 ? 17.471 0.030 10.577 1.00 31.65 ? 315 ILE A CG1 1 ATOM 2501 C CG2 . ILE A 1 315 ? 19.229 -0.306 8.864 1.00 30.65 ? 315 ILE A CG2 1 ATOM 2502 C CD1 . ILE A 1 315 ? 17.146 1.480 10.262 1.00 30.84 ? 315 ILE A CD1 1 ATOM 2503 N N . VAL A 1 316 ? 18.604 -2.740 13.055 1.00 31.74 ? 316 VAL A N 1 ATOM 2504 C CA . VAL A 1 316 ? 18.822 -2.989 14.477 1.00 31.49 ? 316 VAL A CA 1 ATOM 2505 C C . VAL A 1 316 ? 19.757 -4.192 14.577 1.00 32.17 ? 316 VAL A C 1 ATOM 2506 O O . VAL A 1 316 ? 20.753 -4.174 15.305 1.00 32.38 ? 316 VAL A O 1 ATOM 2507 C CB . VAL A 1 316 ? 17.504 -3.307 15.249 1.00 31.38 ? 316 VAL A CB 1 ATOM 2508 C CG1 . VAL A 1 316 ? 17.795 -3.547 16.712 1.00 30.11 ? 316 VAL A CG1 1 ATOM 2509 C CG2 . VAL A 1 316 ? 16.483 -2.202 15.081 1.00 30.03 ? 316 VAL A CG2 1 ATOM 2510 N N . LEU A 1 317 ? 19.434 -5.234 13.820 1.00 32.86 ? 317 LEU A N 1 ATOM 2511 C CA . LEU A 1 317 ? 20.164 -6.490 13.886 1.00 33.66 ? 317 LEU A CA 1 ATOM 2512 C C . LEU A 1 317 ? 21.488 -6.427 13.154 1.00 34.40 ? 317 LEU A C 1 ATOM 2513 O O . LEU A 1 317 ? 22.444 -7.104 13.539 1.00 34.83 ? 317 LEU A O 1 ATOM 2514 C CB . LEU A 1 317 ? 19.307 -7.615 13.333 1.00 33.46 ? 317 LEU A CB 1 ATOM 2515 C CG . LEU A 1 317 ? 18.368 -8.334 14.309 1.00 34.44 ? 317 LEU A CG 1 ATOM 2516 C CD1 . LEU A 1 317 ? 18.266 -7.672 15.688 1.00 33.14 ? 317 LEU A CD1 1 ATOM 2517 C CD2 . LEU A 1 317 ? 17.003 -8.476 13.677 1.00 34.39 ? 317 LEU A CD2 1 ATOM 2518 N N . GLY A 1 318 ? 21.540 -5.612 12.104 1.00 35.05 ? 318 GLY A N 1 ATOM 2519 C CA . GLY A 1 318 ? 22.734 -5.476 11.291 1.00 35.87 ? 318 GLY A CA 1 ATOM 2520 C C . GLY A 1 318 ? 23.019 -6.772 10.570 1.00 36.80 ? 318 GLY A C 1 ATOM 2521 O O . GLY A 1 318 ? 22.131 -7.359 9.944 1.00 37.15 ? 318 GLY A O 1 ATOM 2522 N N . SER A 1 319 ? 24.256 -7.229 10.692 1.00 37.38 ? 319 SER A N 1 ATOM 2523 C CA . SER A 1 319 ? 24.726 -8.418 10.008 1.00 38.36 ? 319 SER A CA 1 ATOM 2524 C C . SER A 1 319 ? 24.166 -9.718 10.604 1.00 38.43 ? 319 SER A C 1 ATOM 2525 O O . SER A 1 319 ? 24.176 -10.758 9.938 1.00 38.50 ? 319 SER A O 1 ATOM 2526 C CB . SER A 1 319 ? 26.260 -8.434 10.015 1.00 38.54 ? 319 SER A CB 1 ATOM 2527 O OG . SER A 1 319 ? 26.757 -8.277 11.341 1.00 40.24 ? 319 SER A OG 1 ATOM 2528 N N . GLU A 1 320 ? 23.682 -9.647 11.845 1.00 38.52 ? 320 GLU A N 1 ATOM 2529 C CA . GLU A 1 320 ? 23.099 -10.796 12.550 1.00 38.53 ? 320 GLU A CA 1 ATOM 2530 C C . GLU A 1 320 ? 21.671 -11.089 12.099 1.00 38.71 ? 320 GLU A C 1 ATOM 2531 O O . GLU A 1 320 ? 21.089 -12.105 12.488 1.00 38.57 ? 320 GLU A O 1 ATOM 2532 C CB . GLU A 1 320 ? 23.098 -10.554 14.064 1.00 38.56 ? 320 GLU A CB 1 ATOM 2533 C CG . GLU A 1 320 ? 24.467 -10.271 14.673 1.00 39.36 ? 320 GLU A CG 1 ATOM 2534 C CD . GLU A 1 320 ? 25.230 -11.522 15.066 1.00 39.80 ? 320 GLU A CD 1 ATOM 2535 O OE1 . GLU A 1 320 ? 24.607 -12.518 15.495 1.00 39.38 ? 320 GLU A OE1 1 ATOM 2536 O OE2 . GLU A 1 320 ? 26.472 -11.489 14.966 1.00 40.75 ? 320 GLU A OE2 1 ATOM 2537 N N . MET A 1 321 ? 21.109 -10.186 11.294 1.00 39.14 ? 321 MET A N 1 ATOM 2538 C CA . MET A 1 321 ? 19.762 -10.327 10.752 1.00 39.49 ? 321 MET A CA 1 ATOM 2539 C C . MET A 1 321 ? 19.611 -11.670 10.047 1.00 40.44 ? 321 MET A C 1 ATOM 2540 O O . MET A 1 321 ? 18.719 -12.451 10.390 1.00 40.86 ? 321 MET A O 1 ATOM 2541 C CB . MET A 1 321 ? 19.469 -9.172 9.792 1.00 39.22 ? 321 MET A CB 1 ATOM 2542 C CG . MET A 1 321 ? 18.154 -9.260 9.025 1.00 39.13 ? 321 MET A CG 1 ATOM 2543 S SD . MET A 1 321 ? 16.704 -8.625 9.893 1.00 38.25 ? 321 MET A SD 1 ATOM 2544 C CE . MET A 1 321 ? 15.462 -8.973 8.655 1.00 38.81 ? 321 MET A CE 1 ATOM 2545 N N . GLN A 1 322 ? 20.502 -11.939 9.090 1.00 41.10 ? 322 GLN A N 1 ATOM 2546 C CA . GLN A 1 322 ? 20.496 -13.178 8.296 1.00 42.11 ? 322 GLN A CA 1 ATOM 2547 C C . GLN A 1 322 ? 20.574 -14.456 9.139 1.00 41.58 ? 322 GLN A C 1 ATOM 2548 O O . GLN A 1 322 ? 19.958 -15.459 8.790 1.00 41.91 ? 322 GLN A O 1 ATOM 2549 C CB . GLN A 1 322 ? 21.657 -13.179 7.280 1.00 42.79 ? 322 GLN A CB 1 ATOM 2550 C CG . GLN A 1 322 ? 21.496 -12.218 6.083 1.00 45.68 ? 322 GLN A CG 1 ATOM 2551 C CD . GLN A 1 322 ? 22.498 -12.517 4.961 1.00 50.39 ? 322 GLN A CD 1 ATOM 2552 O OE1 . GLN A 1 322 ? 23.703 -12.222 5.087 1.00 52.94 ? 322 GLN A OE1 1 ATOM 2553 N NE2 . GLN A 1 322 ? 21.998 -13.107 3.853 1.00 51.57 ? 322 GLN A NE2 1 ATOM 2554 N N . LYS A 1 323 ? 21.336 -14.403 10.232 1.00 41.22 ? 323 LYS A N 1 ATOM 2555 C CA . LYS A 1 323 ? 21.585 -15.546 11.121 1.00 40.64 ? 323 LYS A CA 1 ATOM 2556 C C . LYS A 1 323 ? 20.364 -15.952 11.961 1.00 40.06 ? 323 LYS A C 1 ATOM 2557 O O . LYS A 1 323 ? 20.232 -17.124 12.326 1.00 40.15 ? 323 LYS A O 1 ATOM 2558 C CB . LYS A 1 323 ? 22.831 -15.267 12.002 1.00 41.08 ? 323 LYS A CB 1 ATOM 2559 C CG . LYS A 1 323 ? 22.926 -16.053 13.324 1.00 42.78 ? 323 LYS A CG 1 ATOM 2560 C CD . LYS A 1 323 ? 24.371 -16.452 13.802 1.00 46.45 ? 323 LYS A CD 1 ATOM 2561 C CE . LYS A 1 323 ? 25.418 -15.268 13.774 1.00 49.44 ? 323 LYS A CE 1 ATOM 2562 N NZ . LYS A 1 323 ? 26.286 -15.303 12.477 1.00 52.11 ? 323 LYS A NZ 1 ATOM 2563 N N . TRP A 1 324 ? 19.478 -14.995 12.259 1.00 39.43 ? 324 TRP A N 1 ATOM 2564 C CA . TRP A 1 324 ? 18.316 -15.224 13.143 1.00 38.46 ? 324 TRP A CA 1 ATOM 2565 C C . TRP A 1 324 ? 16.963 -15.182 12.429 1.00 38.27 ? 324 TRP A C 1 ATOM 2566 O O . TRP A 1 324 ? 16.064 -15.931 12.783 1.00 38.10 ? 324 TRP A O 1 ATOM 2567 C CB . TRP A 1 324 ? 18.293 -14.225 14.310 1.00 38.21 ? 324 TRP A CB 1 ATOM 2568 C CG . TRP A 1 324 ? 19.484 -14.272 15.165 1.00 36.89 ? 324 TRP A CG 1 ATOM 2569 C CD1 . TRP A 1 324 ? 20.448 -13.316 15.275 1.00 35.46 ? 324 TRP A CD1 1 ATOM 2570 C CD2 . TRP A 1 324 ? 19.863 -15.333 16.044 1.00 36.71 ? 324 TRP A CD2 1 ATOM 2571 N NE1 . TRP A 1 324 ? 21.412 -13.716 16.164 1.00 35.56 ? 324 TRP A NE1 1 ATOM 2572 C CE2 . TRP A 1 324 ? 21.080 -14.955 16.650 1.00 36.41 ? 324 TRP A CE2 1 ATOM 2573 C CE3 . TRP A 1 324 ? 19.297 -16.572 16.374 1.00 37.12 ? 324 TRP A CE3 1 ATOM 2574 C CZ2 . TRP A 1 324 ? 21.748 -15.776 17.569 1.00 36.66 ? 324 TRP A CZ2 1 ATOM 2575 C CZ3 . TRP A 1 324 ? 19.963 -17.391 17.295 1.00 36.75 ? 324 TRP A CZ3 1 ATOM 2576 C CH2 . TRP A 1 324 ? 21.173 -16.985 17.879 1.00 36.80 ? 324 TRP A CH2 1 ATOM 2577 N N . ILE A 1 325 ? 16.817 -14.285 11.456 1.00 38.26 ? 325 ILE A N 1 ATOM 2578 C CA . ILE A 1 325 ? 15.597 -14.181 10.655 1.00 38.29 ? 325 ILE A CA 1 ATOM 2579 C C . ILE A 1 325 ? 15.853 -14.558 9.190 1.00 38.36 ? 325 ILE A C 1 ATOM 2580 O O . ILE A 1 325 ? 16.027 -13.674 8.352 1.00 38.54 ? 325 ILE A O 1 ATOM 2581 C CB . ILE A 1 325 ? 14.972 -12.752 10.719 1.00 38.19 ? 325 ILE A CB 1 ATOM 2582 C CG1 . ILE A 1 325 ? 14.472 -12.416 12.123 1.00 38.16 ? 325 ILE A CG1 1 ATOM 2583 C CG2 . ILE A 1 325 ? 13.785 -12.632 9.779 1.00 37.76 ? 325 ILE A CG2 1 ATOM 2584 C CD1 . ILE A 1 325 ? 15.488 -11.821 13.008 1.00 38.91 ? 325 ILE A CD1 1 ATOM 2585 N N . PRO A 1 326 ? 15.870 -15.866 8.872 1.00 38.51 ? 326 PRO A N 1 ATOM 2586 C CA . PRO A 1 326 ? 16.063 -16.289 7.485 1.00 38.81 ? 326 PRO A CA 1 ATOM 2587 C C . PRO A 1 326 ? 14.839 -15.936 6.640 1.00 39.29 ? 326 PRO A C 1 ATOM 2588 O O . PRO A 1 326 ? 13.772 -15.691 7.212 1.00 39.41 ? 326 PRO A O 1 ATOM 2589 C CB . PRO A 1 326 ? 16.200 -17.812 7.602 1.00 38.78 ? 326 PRO A CB 1 ATOM 2590 C CG . PRO A 1 326 ? 15.492 -18.177 8.844 1.00 38.50 ? 326 PRO A CG 1 ATOM 2591 C CD . PRO A 1 326 ? 15.703 -17.018 9.777 1.00 38.63 ? 326 PRO A CD 1 ATOM 2592 N N . PRO A 1 327 ? 14.971 -15.933 5.291 1.00 39.69 ? 327 PRO A N 1 ATOM 2593 C CA . PRO A 1 327 ? 13.851 -15.519 4.440 1.00 39.82 ? 327 PRO A CA 1 ATOM 2594 C C . PRO A 1 327 ? 12.629 -16.382 4.699 1.00 39.62 ? 327 PRO A C 1 ATOM 2595 O O . PRO A 1 327 ? 12.763 -17.577 4.965 1.00 39.15 ? 327 PRO A O 1 ATOM 2596 C CB . PRO A 1 327 ? 14.374 -15.764 3.019 1.00 40.05 ? 327 PRO A CB 1 ATOM 2597 C CG . PRO A 1 327 ? 15.861 -15.710 3.150 1.00 40.07 ? 327 PRO A CG 1 ATOM 2598 C CD . PRO A 1 327 ? 16.134 -16.349 4.479 1.00 39.93 ? 327 PRO A CD 1 ATOM 2599 N N . TYR A 1 328 ? 11.456 -15.758 4.637 1.00 39.66 ? 328 TYR A N 1 ATOM 2600 C CA . TYR A 1 328 ? 10.194 -16.406 4.970 1.00 39.93 ? 328 TYR A CA 1 ATOM 2601 C C . TYR A 1 328 ? 9.962 -17.633 4.081 1.00 40.33 ? 328 TYR A C 1 ATOM 2602 O O . TYR A 1 328 ? 10.269 -17.606 2.878 1.00 40.46 ? 328 TYR A O 1 ATOM 2603 C CB . TYR A 1 328 ? 9.059 -15.383 4.838 1.00 39.97 ? 328 TYR A CB 1 ATOM 2604 C CG . TYR A 1 328 ? 7.673 -15.819 5.284 1.00 39.47 ? 328 TYR A CG 1 ATOM 2605 C CD1 . TYR A 1 328 ? 7.405 -16.118 6.615 1.00 39.15 ? 328 TYR A CD1 1 ATOM 2606 C CD2 . TYR A 1 328 ? 6.618 -15.878 4.377 1.00 39.58 ? 328 TYR A CD2 1 ATOM 2607 C CE1 . TYR A 1 328 ? 6.134 -16.495 7.034 1.00 38.42 ? 328 TYR A CE1 1 ATOM 2608 C CE2 . TYR A 1 328 ? 5.335 -16.249 4.788 1.00 39.41 ? 328 TYR A CE2 1 ATOM 2609 C CZ . TYR A 1 328 ? 5.105 -16.553 6.119 1.00 38.20 ? 328 TYR A CZ 1 ATOM 2610 O OH . TYR A 1 328 ? 3.853 -16.924 6.527 1.00 36.26 ? 328 TYR A OH 1 ATOM 2611 N N . GLN A 1 329 ? 9.455 -18.707 4.695 1.00 40.52 ? 329 GLN A N 1 ATOM 2612 C CA . GLN A 1 329 ? 9.151 -19.969 4.007 1.00 40.67 ? 329 GLN A CA 1 ATOM 2613 C C . GLN A 1 329 ? 7.714 -20.463 4.209 1.00 39.97 ? 329 GLN A C 1 ATOM 2614 O O . GLN A 1 329 ? 7.382 -21.583 3.821 1.00 40.18 ? 329 GLN A O 1 ATOM 2615 C CB . GLN A 1 329 ? 10.120 -21.067 4.448 1.00 41.23 ? 329 GLN A CB 1 ATOM 2616 C CG . GLN A 1 329 ? 11.440 -21.132 3.676 1.00 44.04 ? 329 GLN A CG 1 ATOM 2617 C CD . GLN A 1 329 ? 12.053 -22.528 3.737 1.00 48.05 ? 329 GLN A CD 1 ATOM 2618 O OE1 . GLN A 1 329 ? 11.482 -23.495 3.210 1.00 50.84 ? 329 GLN A OE1 1 ATOM 2619 N NE2 . GLN A 1 329 ? 13.208 -22.644 4.385 1.00 48.58 ? 329 GLN A NE2 1 ATOM 2620 N N . GLY A 1 330 ? 6.864 -19.637 4.814 1.00 39.36 ? 330 GLY A N 1 ATOM 2621 C CA . GLY A 1 330 ? 5.473 -20.019 5.069 1.00 38.46 ? 330 GLY A CA 1 ATOM 2622 C C . GLY A 1 330 ? 5.109 -20.168 6.541 1.00 37.95 ? 330 GLY A C 1 ATOM 2623 O O . GLY A 1 330 ? 5.974 -20.302 7.414 1.00 37.83 ? 330 GLY A O 1 ATOM 2624 N N . TYR A 1 331 ? 3.811 -20.138 6.810 1.00 37.31 ? 331 TYR A N 1 ATOM 2625 C CA . TYR A 1 331 ? 3.299 -20.265 8.153 1.00 36.79 ? 331 TYR A CA 1 ATOM 2626 C C . TYR A 1 331 ? 3.668 -21.641 8.690 1.00 37.51 ? 331 TYR A C 1 ATOM 2627 O O . TYR A 1 331 ? 3.504 -22.648 7.995 1.00 38.04 ? 331 TYR A O 1 ATOM 2628 C CB . TYR A 1 331 ? 1.792 -20.037 8.140 1.00 35.95 ? 331 TYR A CB 1 ATOM 2629 C CG . TYR A 1 331 ? 1.063 -20.443 9.396 1.00 35.22 ? 331 TYR A CG 1 ATOM 2630 C CD1 . TYR A 1 331 ? 1.393 -19.878 10.632 1.00 34.12 ? 331 TYR A CD1 1 ATOM 2631 C CD2 . TYR A 1 331 ? 0.021 -21.381 9.348 1.00 33.64 ? 331 TYR A CD2 1 ATOM 2632 C CE1 . TYR A 1 331 ? 0.729 -20.248 11.783 1.00 33.99 ? 331 TYR A CE1 1 ATOM 2633 C CE2 . TYR A 1 331 ? -0.654 -21.755 10.496 1.00 33.46 ? 331 TYR A CE2 1 ATOM 2634 C CZ . TYR A 1 331 ? -0.297 -21.179 11.713 1.00 34.04 ? 331 TYR A CZ 1 ATOM 2635 O OH . TYR A 1 331 ? -0.951 -21.533 12.865 1.00 32.70 ? 331 TYR A OH 1 ATOM 2636 N N . ASN A 1 332 ? 4.206 -21.671 9.909 1.00 37.83 ? 332 ASN A N 1 ATOM 2637 C CA . ASN A 1 332 ? 4.574 -22.911 10.571 1.00 38.25 ? 332 ASN A CA 1 ATOM 2638 C C . ASN A 1 332 ? 3.767 -23.047 11.851 1.00 37.66 ? 332 ASN A C 1 ATOM 2639 O O . ASN A 1 332 ? 4.041 -22.347 12.833 1.00 37.98 ? 332 ASN A O 1 ATOM 2640 C CB . ASN A 1 332 ? 6.085 -22.926 10.856 1.00 39.07 ? 332 ASN A CB 1 ATOM 2641 C CG . ASN A 1 332 ? 6.569 -24.245 11.451 1.00 42.18 ? 332 ASN A CG 1 ATOM 2642 O OD1 . ASN A 1 332 ? 5.824 -24.924 12.174 1.00 41.21 ? 332 ASN A OD1 1 ATOM 2643 N ND2 . ASN A 1 332 ? 7.841 -24.598 11.171 1.00 48.90 ? 332 ASN A ND2 1 ATOM 2644 N N . ASN A 1 333 ? 2.778 -23.946 11.844 1.00 36.93 ? 333 ASN A N 1 ATOM 2645 C CA . ASN A 1 333 ? 1.828 -24.079 12.969 1.00 36.03 ? 333 ASN A CA 1 ATOM 2646 C C . ASN A 1 333 ? 2.417 -24.615 14.285 1.00 35.52 ? 333 ASN A C 1 ATOM 2647 O O . ASN A 1 333 ? 1.723 -24.677 15.295 1.00 34.97 ? 333 ASN A O 1 ATOM 2648 C CB . ASN A 1 333 ? 0.563 -24.861 12.556 1.00 35.81 ? 333 ASN A CB 1 ATOM 2649 C CG . ASN A 1 333 ? 0.793 -26.373 12.438 1.00 36.08 ? 333 ASN A CG 1 ATOM 2650 O OD1 . ASN A 1 333 ? 0.246 -27.018 11.554 1.00 35.67 ? 333 ASN A OD1 1 ATOM 2651 N ND2 . ASN A 1 333 ? 1.577 -26.942 13.344 1.00 38.63 ? 333 ASN A ND2 1 ATOM 2652 N N . SER A 1 334 ? 3.694 -24.989 14.257 1.00 35.48 ? 334 SER A N 1 ATOM 2653 C CA . SER A 1 334 ? 4.380 -25.564 15.415 1.00 35.69 ? 334 SER A CA 1 ATOM 2654 C C . SER A 1 334 ? 5.225 -24.564 16.177 1.00 35.42 ? 334 SER A C 1 ATOM 2655 O O . SER A 1 334 ? 5.658 -24.837 17.301 1.00 35.78 ? 334 SER A O 1 ATOM 2656 C CB . SER A 1 334 ? 5.253 -26.736 14.984 1.00 35.66 ? 334 SER A CB 1 ATOM 2657 O OG . SER A 1 334 ? 4.461 -27.904 14.925 1.00 37.22 ? 334 SER A OG 1 ATOM 2658 N N . VAL A 1 335 ? 5.467 -23.419 15.540 1.00 34.88 ? 335 VAL A N 1 ATOM 2659 C CA . VAL A 1 335 ? 6.212 -22.314 16.106 1.00 34.01 ? 335 VAL A CA 1 ATOM 2660 C C . VAL A 1 335 ? 5.347 -21.608 17.129 1.00 33.72 ? 335 VAL A C 1 ATOM 2661 O O . VAL A 1 335 ? 4.187 -21.313 16.865 1.00 34.21 ? 335 VAL A O 1 ATOM 2662 C CB . VAL A 1 335 ? 6.628 -21.342 14.993 1.00 34.15 ? 335 VAL A CB 1 ATOM 2663 C CG1 . VAL A 1 335 ? 7.172 -20.017 15.550 1.00 33.25 ? 335 VAL A CG1 1 ATOM 2664 C CG2 . VAL A 1 335 ? 7.656 -22.013 14.086 1.00 34.90 ? 335 VAL A CG2 1 ATOM 2665 N N . ASP A 1 336 ? 5.918 -21.348 18.302 1.00 33.18 ? 336 ASP A N 1 ATOM 2666 C CA . ASP A 1 336 ? 5.222 -20.684 19.405 1.00 32.12 ? 336 ASP A CA 1 ATOM 2667 C C . ASP A 1 336 ? 5.333 -19.145 19.268 1.00 31.26 ? 336 ASP A C 1 ATOM 2668 O O . ASP A 1 336 ? 6.415 -18.568 19.432 1.00 30.76 ? 336 ASP A O 1 ATOM 2669 C CB . ASP A 1 336 ? 5.812 -21.213 20.713 1.00 32.21 ? 336 ASP A CB 1 ATOM 2670 C CG . ASP A 1 336 ? 5.332 -20.470 21.947 1.00 33.52 ? 336 ASP A CG 1 ATOM 2671 O OD1 . ASP A 1 336 ? 4.373 -19.671 21.905 1.00 33.57 ? 336 ASP A OD1 1 ATOM 2672 O OD2 . ASP A 1 336 ? 5.940 -20.719 23.005 1.00 36.65 ? 336 ASP A OD2 1 ATOM 2673 N N . PRO A 1 337 ? 4.201 -18.471 18.975 1.00 30.71 ? 337 PRO A N 1 ATOM 2674 C CA . PRO A 1 337 ? 4.228 -17.030 18.685 1.00 29.98 ? 337 PRO A CA 1 ATOM 2675 C C . PRO A 1 337 ? 4.200 -16.110 19.912 1.00 29.45 ? 337 PRO A C 1 ATOM 2676 O O . PRO A 1 337 ? 4.242 -14.893 19.745 1.00 29.69 ? 337 PRO A O 1 ATOM 2677 C CB . PRO A 1 337 ? 2.955 -16.826 17.854 1.00 30.03 ? 337 PRO A CB 1 ATOM 2678 C CG . PRO A 1 337 ? 2.003 -17.877 18.366 1.00 30.15 ? 337 PRO A CG 1 ATOM 2679 C CD . PRO A 1 337 ? 2.827 -19.022 18.917 1.00 30.40 ? 337 PRO A CD 1 ATOM 2680 N N . ARG A 1 338 ? 4.125 -16.668 21.120 1.00 28.51 ? 338 ARG A N 1 ATOM 2681 C CA . ARG A 1 338 ? 4.019 -15.856 22.349 1.00 27.82 ? 338 ARG A CA 1 ATOM 2682 C C . ARG A 1 338 ? 5.269 -15.016 22.641 1.00 26.86 ? 338 ARG A C 1 ATOM 2683 O O . ARG A 1 338 ? 6.390 -15.474 22.453 1.00 26.76 ? 338 ARG A O 1 ATOM 2684 C CB . ARG A 1 338 ? 3.729 -16.737 23.564 1.00 27.93 ? 338 ARG A CB 1 ATOM 2685 C CG . ARG A 1 338 ? 2.284 -17.172 23.717 1.00 28.21 ? 338 ARG A CG 1 ATOM 2686 C CD . ARG A 1 338 ? 2.175 -18.191 24.828 1.00 28.06 ? 338 ARG A CD 1 ATOM 2687 N NE . ARG A 1 338 ? 3.185 -19.238 24.657 1.00 29.61 ? 338 ARG A NE 1 ATOM 2688 C CZ . ARG A 1 338 ? 3.686 -19.969 25.647 1.00 29.66 ? 338 ARG A CZ 1 ATOM 2689 N NH1 . ARG A 1 338 ? 3.268 -19.776 26.892 1.00 29.69 ? 338 ARG A NH1 1 ATOM 2690 N NH2 . ARG A 1 338 ? 4.606 -20.893 25.394 1.00 28.78 ? 338 ARG A NH2 1 ATOM 2691 N N . ILE A 1 339 ? 5.065 -13.787 23.103 1.00 25.39 ? 339 ILE A N 1 ATOM 2692 C CA . ILE A 1 339 ? 6.181 -12.961 23.528 1.00 24.37 ? 339 ILE A CA 1 ATOM 2693 C C . ILE A 1 339 ? 6.748 -13.522 24.835 1.00 24.25 ? 339 ILE A C 1 ATOM 2694 O O . ILE A 1 339 ? 6.002 -13.806 25.782 1.00 23.49 ? 339 ILE A O 1 ATOM 2695 C CB . ILE A 1 339 ? 5.777 -11.463 23.681 1.00 23.99 ? 339 ILE A CB 1 ATOM 2696 C CG1 . ILE A 1 339 ? 5.219 -10.902 22.361 1.00 24.26 ? 339 ILE A CG1 1 ATOM 2697 C CG2 . ILE A 1 339 ? 6.938 -10.628 24.190 1.00 22.58 ? 339 ILE A CG2 1 ATOM 2698 C CD1 . ILE A 1 339 ? 6.154 -10.989 21.145 1.00 22.14 ? 339 ILE A CD1 1 ATOM 2699 N N . SER A 1 340 ? 8.066 -13.714 24.858 1.00 24.10 ? 340 SER A N 1 ATOM 2700 C CA . SER A 1 340 ? 8.746 -14.220 26.051 1.00 24.10 ? 340 SER A CA 1 ATOM 2701 C C . SER A 1 340 ? 8.939 -13.110 27.074 1.00 24.59 ? 340 SER A C 1 ATOM 2702 O O . SER A 1 340 ? 8.933 -11.917 26.727 1.00 24.30 ? 340 SER A O 1 ATOM 2703 C CB . SER A 1 340 ? 10.083 -14.869 25.695 1.00 23.75 ? 340 SER A CB 1 ATOM 2704 O OG . SER A 1 340 ? 11.024 -13.931 25.197 1.00 22.52 ? 340 SER A OG 1 ATOM 2705 N N . ASN A 1 341 ? 9.092 -13.503 28.338 1.00 25.22 ? 341 ASN A N 1 ATOM 2706 C CA . ASN A 1 341 ? 9.300 -12.541 29.406 1.00 25.38 ? 341 ASN A CA 1 ATOM 2707 C C . ASN A 1 341 ? 10.578 -11.716 29.188 1.00 25.71 ? 341 ASN A C 1 ATOM 2708 O O . ASN A 1 341 ? 10.563 -10.501 29.337 1.00 26.41 ? 341 ASN A O 1 ATOM 2709 C CB . ASN A 1 341 ? 9.312 -13.258 30.752 1.00 25.50 ? 341 ASN A CB 1 ATOM 2710 C CG . ASN A 1 341 ? 8.803 -12.384 31.901 1.00 25.91 ? 341 ASN A CG 1 ATOM 2711 O OD1 . ASN A 1 341 ? 9.240 -11.239 32.090 1.00 24.30 ? 341 ASN A OD1 1 ATOM 2712 N ND2 . ASN A 1 341 ? 7.878 -12.937 32.683 1.00 23.98 ? 341 ASN A ND2 1 ATOM 2713 N N . VAL A 1 342 ? 11.672 -12.367 28.793 1.00 25.93 ? 342 VAL A N 1 ATOM 2714 C CA . VAL A 1 342 ? 12.957 -11.675 28.586 1.00 25.37 ? 342 VAL A CA 1 ATOM 2715 C C . VAL A 1 342 ? 12.910 -10.696 27.403 1.00 25.21 ? 342 VAL A C 1 ATOM 2716 O O . VAL A 1 342 ? 13.616 -9.695 27.393 1.00 25.62 ? 342 VAL A O 1 ATOM 2717 C CB . VAL A 1 342 ? 14.129 -12.678 28.427 1.00 24.93 ? 342 VAL A CB 1 ATOM 2718 C CG1 . VAL A 1 342 ? 13.937 -13.532 27.203 1.00 26.03 ? 342 VAL A CG1 1 ATOM 2719 C CG2 . VAL A 1 342 ? 15.475 -11.961 28.361 1.00 25.28 ? 342 VAL A CG2 1 ATOM 2720 N N . PHE A 1 343 ? 12.075 -10.972 26.410 1.00 24.96 ? 343 PHE A N 1 ATOM 2721 C CA . PHE A 1 343 ? 11.944 -10.050 25.290 1.00 24.86 ? 343 PHE A CA 1 ATOM 2722 C C . PHE A 1 343 ? 11.544 -8.649 25.748 1.00 24.70 ? 343 PHE A C 1 ATOM 2723 O O . PHE A 1 343 ? 12.068 -7.668 25.231 1.00 24.96 ? 343 PHE A O 1 ATOM 2724 C CB . PHE A 1 343 ? 10.942 -10.559 24.257 1.00 24.69 ? 343 PHE A CB 1 ATOM 2725 C CG . PHE A 1 343 ? 10.778 -9.646 23.084 1.00 24.45 ? 343 PHE A CG 1 ATOM 2726 C CD1 . PHE A 1 343 ? 11.734 -9.609 22.083 1.00 24.02 ? 343 PHE A CD1 1 ATOM 2727 C CD2 . PHE A 1 343 ? 9.667 -8.814 22.983 1.00 24.09 ? 343 PHE A CD2 1 ATOM 2728 C CE1 . PHE A 1 343 ? 11.581 -8.768 20.978 1.00 25.32 ? 343 PHE A CE1 1 ATOM 2729 C CE2 . PHE A 1 343 ? 9.499 -7.979 21.892 1.00 24.03 ? 343 PHE A CE2 1 ATOM 2730 C CZ . PHE A 1 343 ? 10.468 -7.953 20.880 1.00 25.03 ? 343 PHE A CZ 1 ATOM 2731 N N . THR A 1 344 ? 10.627 -8.556 26.713 1.00 24.46 ? 344 THR A N 1 ATOM 2732 C CA . THR A 1 344 ? 10.165 -7.251 27.207 1.00 24.19 ? 344 THR A CA 1 ATOM 2733 C C . THR A 1 344 ? 11.253 -6.475 27.953 1.00 23.64 ? 344 THR A C 1 ATOM 2734 O O . THR A 1 344 ? 11.061 -5.317 28.306 1.00 23.76 ? 344 THR A O 1 ATOM 2735 C CB . THR A 1 344 ? 8.926 -7.365 28.113 1.00 24.33 ? 344 THR A CB 1 ATOM 2736 O OG1 . THR A 1 344 ? 9.334 -7.743 29.433 1.00 25.86 ? 344 THR A OG1 1 ATOM 2737 C CG2 . THR A 1 344 ? 7.955 -8.375 27.570 1.00 23.71 ? 344 THR A CG2 1 ATOM 2738 N N . PHE A 1 345 ? 12.386 -7.121 28.200 1.00 22.91 ? 345 PHE A N 1 ATOM 2739 C CA . PHE A 1 345 ? 13.537 -6.422 28.748 1.00 22.21 ? 345 PHE A CA 1 ATOM 2740 C C . PHE A 1 345 ? 14.611 -6.189 27.714 1.00 22.03 ? 345 PHE A C 1 ATOM 2741 O O . PHE A 1 345 ? 15.296 -5.165 27.771 1.00 22.10 ? 345 PHE A O 1 ATOM 2742 C CB . PHE A 1 345 ? 14.101 -7.140 29.971 1.00 22.11 ? 345 PHE A CB 1 ATOM 2743 C CG . PHE A 1 345 ? 13.183 -7.114 31.131 1.00 21.66 ? 345 PHE A CG 1 ATOM 2744 C CD1 . PHE A 1 345 ? 12.421 -8.239 31.458 1.00 21.43 ? 345 PHE A CD1 1 ATOM 2745 C CD2 . PHE A 1 345 ? 13.023 -5.945 31.875 1.00 22.12 ? 345 PHE A CD2 1 ATOM 2746 C CE1 . PHE A 1 345 ? 11.528 -8.216 32.538 1.00 22.40 ? 345 PHE A CE1 1 ATOM 2747 C CE2 . PHE A 1 345 ? 12.138 -5.912 32.957 1.00 22.69 ? 345 PHE A CE2 1 ATOM 2748 C CZ . PHE A 1 345 ? 11.391 -7.060 33.293 1.00 21.92 ? 345 PHE A CZ 1 ATOM 2749 N N . ALA A 1 346 ? 14.764 -7.128 26.778 1.00 21.51 ? 346 ALA A N 1 ATOM 2750 C CA . ALA A 1 346 ? 15.697 -6.948 25.681 1.00 21.46 ? 346 ALA A CA 1 ATOM 2751 C C . ALA A 1 346 ? 15.263 -5.785 24.787 1.00 21.49 ? 346 ALA A C 1 ATOM 2752 O O . ALA A 1 346 ? 16.099 -5.014 24.310 1.00 21.48 ? 346 ALA A O 1 ATOM 2753 C CB . ALA A 1 346 ? 15.854 -8.232 24.878 1.00 21.32 ? 346 ALA A CB 1 ATOM 2754 N N . PHE A 1 347 ? 13.961 -5.626 24.596 1.00 21.61 ? 347 PHE A N 1 ATOM 2755 C CA . PHE A 1 347 ? 13.456 -4.576 23.720 1.00 22.46 ? 347 PHE A CA 1 ATOM 2756 C C . PHE A 1 347 ? 13.599 -3.183 24.359 1.00 22.81 ? 347 PHE A C 1 ATOM 2757 O O . PHE A 1 347 ? 13.355 -2.153 23.709 1.00 23.52 ? 347 PHE A O 1 ATOM 2758 C CB . PHE A 1 347 ? 12.008 -4.864 23.323 1.00 22.51 ? 347 PHE A CB 1 ATOM 2759 C CG . PHE A 1 347 ? 11.623 -4.337 21.963 1.00 24.89 ? 347 PHE A CG 1 ATOM 2760 C CD1 . PHE A 1 347 ? 12.451 -3.470 21.255 1.00 27.97 ? 347 PHE A CD1 1 ATOM 2761 C CD2 . PHE A 1 347 ? 10.405 -4.696 21.392 1.00 26.23 ? 347 PHE A CD2 1 ATOM 2762 C CE1 . PHE A 1 347 ? 12.085 -2.985 19.995 1.00 28.67 ? 347 PHE A CE1 1 ATOM 2763 C CE2 . PHE A 1 347 ? 10.031 -4.224 20.146 1.00 26.70 ? 347 PHE A CE2 1 ATOM 2764 C CZ . PHE A 1 347 ? 10.873 -3.363 19.444 1.00 28.32 ? 347 PHE A CZ 1 ATOM 2765 N N . ARG A 1 348 ? 14.027 -3.140 25.618 1.00 22.86 ? 348 ARG A N 1 ATOM 2766 C CA . ARG A 1 348 ? 14.255 -1.871 26.304 1.00 22.75 ? 348 ARG A CA 1 ATOM 2767 C C . ARG A 1 348 ? 15.594 -1.217 25.925 1.00 23.11 ? 348 ARG A C 1 ATOM 2768 O O . ARG A 1 348 ? 16.007 -0.234 26.550 1.00 23.12 ? 348 ARG A O 1 ATOM 2769 C CB . ARG A 1 348 ? 14.115 -2.030 27.826 1.00 22.80 ? 348 ARG A CB 1 ATOM 2770 C CG . ARG A 1 348 ? 12.736 -2.550 28.266 1.00 22.82 ? 348 ARG A CG 1 ATOM 2771 C CD . ARG A 1 348 ? 12.537 -2.523 29.780 1.00 22.64 ? 348 ARG A CD 1 ATOM 2772 N NE . ARG A 1 348 ? 11.303 -3.204 30.187 1.00 22.00 ? 348 ARG A NE 1 ATOM 2773 C CZ . ARG A 1 348 ? 10.593 -2.920 31.275 1.00 21.76 ? 348 ARG A CZ 1 ATOM 2774 N NH1 . ARG A 1 348 ? 10.955 -1.945 32.097 1.00 21.49 ? 348 ARG A NH1 1 ATOM 2775 N NH2 . ARG A 1 348 ? 9.496 -3.610 31.535 1.00 23.47 ? 348 ARG A NH2 1 ATOM 2776 N N . PHE A 1 349 ? 16.255 -1.733 24.886 1.00 23.27 ? 349 PHE A N 1 ATOM 2777 C CA . PHE A 1 349 ? 17.488 -1.111 24.388 1.00 23.55 ? 349 PHE A CA 1 ATOM 2778 C C . PHE A 1 349 ? 17.200 0.289 23.863 1.00 24.26 ? 349 PHE A C 1 ATOM 2779 O O . PHE A 1 349 ? 18.057 1.181 23.926 1.00 24.49 ? 349 PHE A O 1 ATOM 2780 C CB . PHE A 1 349 ? 18.146 -1.959 23.298 1.00 23.34 ? 349 PHE A CB 1 ATOM 2781 C CG . PHE A 1 349 ? 17.417 -1.946 21.975 1.00 22.94 ? 349 PHE A CG 1 ATOM 2782 C CD1 . PHE A 1 349 ? 17.719 -0.995 21.005 1.00 21.73 ? 349 PHE A CD1 1 ATOM 2783 C CD2 . PHE A 1 349 ? 16.443 -2.899 21.690 1.00 23.02 ? 349 PHE A CD2 1 ATOM 2784 C CE1 . PHE A 1 349 ? 17.055 -0.985 19.781 1.00 22.04 ? 349 PHE A CE1 1 ATOM 2785 C CE2 . PHE A 1 349 ? 15.783 -2.894 20.457 1.00 22.69 ? 349 PHE A CE2 1 ATOM 2786 C CZ . PHE A 1 349 ? 16.092 -1.941 19.509 1.00 21.70 ? 349 PHE A CZ 1 ATOM 2787 N N . GLY A 1 350 ? 15.985 0.472 23.350 1.00 24.82 ? 350 GLY A N 1 ATOM 2788 C CA . GLY A 1 350 ? 15.537 1.758 22.836 1.00 25.71 ? 350 GLY A CA 1 ATOM 2789 C C . GLY A 1 350 ? 15.565 2.901 23.833 1.00 26.46 ? 350 GLY A C 1 ATOM 2790 O O . GLY A 1 350 ? 15.587 4.065 23.433 1.00 27.01 ? 350 GLY A O 1 ATOM 2791 N N . HIS A 1 351 ? 15.563 2.583 25.129 1.00 27.01 ? 351 HIS A N 1 ATOM 2792 C CA . HIS A 1 351 ? 15.715 3.604 26.165 1.00 27.26 ? 351 HIS A CA 1 ATOM 2793 C C . HIS A 1 351 ? 17.041 4.353 26.065 1.00 27.35 ? 351 HIS A C 1 ATOM 2794 O O . HIS A 1 351 ? 17.109 5.546 26.380 1.00 27.89 ? 351 HIS A O 1 ATOM 2795 C CB . HIS A 1 351 ? 15.502 3.011 27.557 1.00 27.41 ? 351 HIS A CB 1 ATOM 2796 C CG . HIS A 1 351 ? 14.091 2.567 27.798 1.00 28.74 ? 351 HIS A CG 1 ATOM 2797 N ND1 . HIS A 1 351 ? 13.728 1.770 28.862 1.00 29.02 ? 351 HIS A ND1 1 ATOM 2798 C CD2 . HIS A 1 351 ? 12.955 2.798 27.095 1.00 28.26 ? 351 HIS A CD2 1 ATOM 2799 C CE1 . HIS A 1 351 ? 12.427 1.542 28.814 1.00 29.35 ? 351 HIS A CE1 1 ATOM 2800 N NE2 . HIS A 1 351 ? 11.936 2.150 27.749 1.00 29.40 ? 351 HIS A NE2 1 ATOM 2801 N N . MET A 1 352 ? 18.081 3.673 25.585 1.00 26.89 ? 352 MET A N 1 ATOM 2802 C CA . MET A 1 352 ? 19.397 4.305 25.460 1.00 26.63 ? 352 MET A CA 1 ATOM 2803 C C . MET A 1 352 ? 19.499 5.109 24.165 1.00 26.35 ? 352 MET A C 1 ATOM 2804 O O . MET A 1 352 ? 20.542 5.699 23.859 1.00 26.14 ? 352 MET A O 1 ATOM 2805 C CB . MET A 1 352 ? 20.521 3.267 25.594 1.00 26.58 ? 352 MET A CB 1 ATOM 2806 C CG . MET A 1 352 ? 20.250 2.276 26.719 1.00 27.64 ? 352 MET A CG 1 ATOM 2807 S SD . MET A 1 352 ? 21.715 1.625 27.500 1.00 30.96 ? 352 MET A SD 1 ATOM 2808 C CE . MET A 1 352 ? 21.032 0.875 28.964 1.00 27.13 ? 352 MET A CE 1 ATOM 2809 N N . GLU A 1 353 ? 18.383 5.151 23.437 1.00 25.90 ? 353 GLU A N 1 ATOM 2810 C CA . GLU A 1 353 ? 18.303 5.821 22.141 1.00 25.58 ? 353 GLU A CA 1 ATOM 2811 C C . GLU A 1 353 ? 17.539 7.127 22.185 1.00 25.15 ? 353 GLU A C 1 ATOM 2812 O O . GLU A 1 353 ? 17.458 7.833 21.179 1.00 25.62 ? 353 GLU A O 1 ATOM 2813 C CB . GLU A 1 353 ? 17.684 4.898 21.086 1.00 25.28 ? 353 GLU A CB 1 ATOM 2814 C CG . GLU A 1 353 ? 18.605 3.774 20.696 1.00 25.07 ? 353 GLU A CG 1 ATOM 2815 C CD . GLU A 1 353 ? 18.037 2.867 19.625 1.00 23.73 ? 353 GLU A CD 1 ATOM 2816 O OE1 . GLU A 1 353 ? 16.885 3.072 19.175 1.00 22.64 ? 353 GLU A OE1 1 ATOM 2817 O OE2 . GLU A 1 353 ? 18.767 1.937 19.238 1.00 21.92 ? 353 GLU A OE2 1 ATOM 2818 N N . VAL A 1 354 ? 16.986 7.449 23.342 1.00 24.57 ? 354 VAL A N 1 ATOM 2819 C CA . VAL A 1 354 ? 16.216 8.665 23.492 1.00 24.18 ? 354 VAL A CA 1 ATOM 2820 C C . VAL A 1 354 ? 17.146 9.865 23.755 1.00 24.06 ? 354 VAL A C 1 ATOM 2821 O O . VAL A 1 354 ? 17.903 9.849 24.739 1.00 23.91 ? 354 VAL A O 1 ATOM 2822 C CB . VAL A 1 354 ? 15.141 8.503 24.604 1.00 24.45 ? 354 VAL A CB 1 ATOM 2823 C CG1 . VAL A 1 354 ? 14.288 9.764 24.730 1.00 24.83 ? 354 VAL A CG1 1 ATOM 2824 C CG2 . VAL A 1 354 ? 14.229 7.292 24.299 1.00 23.69 ? 354 VAL A CG2 1 ATOM 2825 N N . PRO A 1 355 ? 17.095 10.901 22.879 1.00 23.80 ? 355 PRO A N 1 ATOM 2826 C CA . PRO A 1 355 ? 17.868 12.133 23.076 1.00 24.29 ? 355 PRO A CA 1 ATOM 2827 C C . PRO A 1 355 ? 17.188 13.034 24.107 1.00 24.95 ? 355 PRO A C 1 ATOM 2828 O O . PRO A 1 355 ? 16.095 12.713 24.585 1.00 25.36 ? 355 PRO A O 1 ATOM 2829 C CB . PRO A 1 355 ? 17.865 12.791 21.687 1.00 23.70 ? 355 PRO A CB 1 ATOM 2830 C CG . PRO A 1 355 ? 16.657 12.307 21.032 1.00 23.55 ? 355 PRO A CG 1 ATOM 2831 C CD . PRO A 1 355 ? 16.271 10.973 21.659 1.00 23.83 ? 355 PRO A CD 1 ATOM 2832 N N . SER A 1 356 ? 17.813 14.152 24.458 1.00 25.46 ? 356 SER A N 1 ATOM 2833 C CA . SER A 1 356 ? 17.315 14.938 25.593 1.00 25.67 ? 356 SER A CA 1 ATOM 2834 C C . SER A 1 356 ? 16.325 16.044 25.230 1.00 25.96 ? 356 SER A C 1 ATOM 2835 O O . SER A 1 356 ? 15.705 16.646 26.107 1.00 26.19 ? 356 SER A O 1 ATOM 2836 C CB . SER A 1 356 ? 18.479 15.483 26.424 1.00 25.28 ? 356 SER A CB 1 ATOM 2837 O OG . SER A 1 356 ? 19.238 16.419 25.700 1.00 24.99 ? 356 SER A OG 1 ATOM 2838 N N . THR A 1 357 ? 16.163 16.311 23.944 1.00 26.70 ? 357 THR A N 1 ATOM 2839 C CA . THR A 1 357 ? 15.284 17.397 23.521 1.00 27.67 ? 357 THR A CA 1 ATOM 2840 C C . THR A 1 357 ? 14.412 16.979 22.349 1.00 28.09 ? 357 THR A C 1 ATOM 2841 O O . THR A 1 357 ? 14.767 16.056 21.626 1.00 27.69 ? 357 THR A O 1 ATOM 2842 C CB . THR A 1 357 ? 16.077 18.646 23.106 1.00 27.55 ? 357 THR A CB 1 ATOM 2843 O OG1 . THR A 1 357 ? 16.769 18.377 21.876 1.00 29.17 ? 357 THR A OG1 1 ATOM 2844 C CG2 . THR A 1 357 ? 17.075 19.064 24.184 1.00 26.38 ? 357 THR A CG2 1 ATOM 2845 N N . VAL A 1 358 ? 13.278 17.663 22.184 1.00 29.31 ? 358 VAL A N 1 ATOM 2846 C CA . VAL A 1 358 ? 12.409 17.502 21.016 1.00 30.51 ? 358 VAL A CA 1 ATOM 2847 C C . VAL A 1 358 ? 12.172 18.827 20.276 1.00 31.40 ? 358 VAL A C 1 ATOM 2848 O O . VAL A 1 358 ? 11.866 19.861 20.890 1.00 31.47 ? 358 VAL A O 1 ATOM 2849 C CB . VAL A 1 358 ? 11.054 16.867 21.387 1.00 30.62 ? 358 VAL A CB 1 ATOM 2850 C CG1 . VAL A 1 358 ? 10.202 16.675 20.138 1.00 30.75 ? 358 VAL A CG1 1 ATOM 2851 C CG2 . VAL A 1 358 ? 11.262 15.536 22.107 1.00 30.85 ? 358 VAL A CG2 1 ATOM 2852 N N . SER A 1 359 ? 12.301 18.777 18.951 1.00 32.49 ? 359 SER A N 1 ATOM 2853 C CA . SER A 1 359 ? 12.237 19.965 18.108 1.00 33.26 ? 359 SER A CA 1 ATOM 2854 C C . SER A 1 359 ? 10.945 20.048 17.327 1.00 34.13 ? 359 SER A C 1 ATOM 2855 O O . SER A 1 359 ? 10.364 19.032 16.918 1.00 33.96 ? 359 SER A O 1 ATOM 2856 C CB . SER A 1 359 ? 13.407 19.997 17.112 1.00 33.51 ? 359 SER A CB 1 ATOM 2857 O OG . SER A 1 359 ? 14.571 20.605 17.654 1.00 33.92 ? 359 SER A OG 1 ATOM 2858 N N . ARG A 1 360 ? 10.513 21.286 17.124 1.00 35.29 ? 360 ARG A N 1 ATOM 2859 C CA . ARG A 1 360 ? 9.429 21.607 16.220 1.00 36.56 ? 360 ARG A CA 1 ATOM 2860 C C . ARG A 1 360 ? 10.017 22.367 15.026 1.00 37.36 ? 360 ARG A C 1 ATOM 2861 O O . ARG A 1 360 ? 10.808 23.293 15.204 1.00 37.36 ? 360 ARG A O 1 ATOM 2862 C CB . ARG A 1 360 ? 8.368 22.454 16.935 1.00 36.59 ? 360 ARG A CB 1 ATOM 2863 C CG . ARG A 1 360 ? 7.226 21.668 17.586 1.00 36.43 ? 360 ARG A CG 1 ATOM 2864 C CD . ARG A 1 360 ? 7.457 21.374 19.064 1.00 35.82 ? 360 ARG A CD 1 ATOM 2865 N NE . ARG A 1 360 ? 7.960 22.532 19.793 1.00 36.58 ? 360 ARG A NE 1 ATOM 2866 C CZ . ARG A 1 360 ? 7.217 23.536 20.259 1.00 36.73 ? 360 ARG A CZ 1 ATOM 2867 N NH1 . ARG A 1 360 ? 5.894 23.556 20.084 1.00 36.90 ? 360 ARG A NH1 1 ATOM 2868 N NH2 . ARG A 1 360 ? 7.811 24.536 20.897 1.00 33.88 ? 360 ARG A NH2 1 ATOM 2869 N N . LEU A 1 361 ? 9.646 21.965 13.814 1.00 38.50 ? 361 LEU A N 1 ATOM 2870 C CA . LEU A 1 361 ? 10.184 22.593 12.610 1.00 39.91 ? 361 LEU A CA 1 ATOM 2871 C C . LEU A 1 361 ? 9.082 23.194 11.738 1.00 41.25 ? 361 LEU A C 1 ATOM 2872 O O . LEU A 1 361 ? 7.991 22.624 11.634 1.00 41.71 ? 361 LEU A O 1 ATOM 2873 C CB . LEU A 1 361 ? 11.043 21.600 11.803 1.00 39.59 ? 361 LEU A CB 1 ATOM 2874 C CG . LEU A 1 361 ? 12.217 20.897 12.519 1.00 39.34 ? 361 LEU A CG 1 ATOM 2875 C CD1 . LEU A 1 361 ? 13.053 20.080 11.551 1.00 38.05 ? 361 LEU A CD1 1 ATOM 2876 C CD2 . LEU A 1 361 ? 13.115 21.885 13.273 1.00 39.24 ? 361 LEU A CD2 1 ATOM 2877 N N . ASP A 1 362 ? 9.373 24.345 11.123 1.00 42.65 ? 362 ASP A N 1 ATOM 2878 C CA . ASP A 1 362 ? 8.439 25.002 10.206 1.00 43.93 ? 362 ASP A CA 1 ATOM 2879 C C . ASP A 1 362 ? 8.572 24.422 8.809 1.00 44.75 ? 362 ASP A C 1 ATOM 2880 O O . ASP A 1 362 ? 9.290 23.442 8.610 1.00 45.22 ? 362 ASP A O 1 ATOM 2881 C CB . ASP A 1 362 ? 8.594 26.537 10.212 1.00 44.16 ? 362 ASP A CB 1 ATOM 2882 C CG . ASP A 1 362 ? 9.907 27.020 9.585 1.00 45.17 ? 362 ASP A CG 1 ATOM 2883 O OD1 . ASP A 1 362 ? 10.632 26.218 8.942 1.00 45.42 ? 362 ASP A OD1 1 ATOM 2884 O OD2 . ASP A 1 362 ? 10.208 28.231 9.736 1.00 46.76 ? 362 ASP A OD2 1 ATOM 2885 N N . GLU A 1 363 ? 7.899 25.034 7.840 1.00 45.59 ? 363 GLU A N 1 ATOM 2886 C CA . GLU A 1 363 ? 7.773 24.441 6.513 1.00 46.59 ? 363 GLU A CA 1 ATOM 2887 C C . GLU A 1 363 ? 9.081 24.365 5.715 1.00 46.92 ? 363 GLU A C 1 ATOM 2888 O O . GLU A 1 363 ? 9.215 23.536 4.815 1.00 47.03 ? 363 GLU A O 1 ATOM 2889 C CB . GLU A 1 363 ? 6.667 25.135 5.720 1.00 46.96 ? 363 GLU A CB 1 ATOM 2890 C CG . GLU A 1 363 ? 5.303 25.042 6.399 1.00 48.18 ? 363 GLU A CG 1 ATOM 2891 C CD . GLU A 1 363 ? 4.162 25.409 5.475 1.00 50.61 ? 363 GLU A CD 1 ATOM 2892 O OE1 . GLU A 1 363 ? 4.287 25.189 4.248 1.00 52.28 ? 363 GLU A OE1 1 ATOM 2893 O OE2 . GLU A 1 363 ? 3.137 25.922 5.971 1.00 51.49 ? 363 GLU A OE2 1 ATOM 2894 N N . ASN A 1 364 ? 10.037 25.228 6.040 1.00 47.44 ? 364 ASN A N 1 ATOM 2895 C CA . ASN A 1 364 ? 11.390 25.107 5.482 1.00 48.17 ? 364 ASN A CA 1 ATOM 2896 C C . ASN A 1 364 ? 12.295 24.244 6.370 1.00 48.41 ? 364 ASN A C 1 ATOM 2897 O O . ASN A 1 364 ? 13.517 24.184 6.149 1.00 48.85 ? 364 ASN A O 1 ATOM 2898 C CB . ASN A 1 364 ? 12.055 26.486 5.299 1.00 48.26 ? 364 ASN A CB 1 ATOM 2899 C CG . ASN A 1 364 ? 11.403 27.328 4.207 1.00 48.63 ? 364 ASN A CG 1 ATOM 2900 O OD1 . ASN A 1 364 ? 11.753 28.494 4.049 1.00 49.37 ? 364 ASN A OD1 1 ATOM 2901 N ND2 . ASN A 1 364 ? 10.470 26.752 3.447 1.00 49.35 ? 364 ASN A ND2 1 ATOM 2902 N N . TYR A 1 365 ? 11.702 23.588 7.370 1.00 48.28 ? 365 TYR A N 1 ATOM 2903 C CA . TYR A 1 365 ? 12.450 22.802 8.357 1.00 48.74 ? 365 TYR A CA 1 ATOM 2904 C C . TYR A 1 365 ? 13.369 23.679 9.213 1.00 49.00 ? 365 TYR A C 1 ATOM 2905 O O . TYR A 1 365 ? 14.434 23.244 9.641 1.00 49.12 ? 365 TYR A O 1 ATOM 2906 C CB . TYR A 1 365 ? 13.237 21.656 7.696 1.00 48.61 ? 365 TYR A CB 1 ATOM 2907 C CG . TYR A 1 365 ? 12.381 20.479 7.282 1.00 48.51 ? 365 TYR A CG 1 ATOM 2908 C CD1 . TYR A 1 365 ? 12.334 19.317 8.055 1.00 47.83 ? 365 TYR A CD1 1 ATOM 2909 C CD2 . TYR A 1 365 ? 11.608 20.532 6.125 1.00 48.21 ? 365 TYR A CD2 1 ATOM 2910 C CE1 . TYR A 1 365 ? 11.548 18.236 7.679 1.00 47.36 ? 365 TYR A CE1 1 ATOM 2911 C CE2 . TYR A 1 365 ? 10.815 19.456 5.744 1.00 48.15 ? 365 TYR A CE2 1 ATOM 2912 C CZ . TYR A 1 365 ? 10.792 18.318 6.526 1.00 47.71 ? 365 TYR A CZ 1 ATOM 2913 O OH . TYR A 1 365 ? 10.008 17.267 6.145 1.00 47.85 ? 365 TYR A OH 1 ATOM 2914 N N . GLN A 1 366 ? 12.943 24.915 9.451 1.00 49.46 ? 366 GLN A N 1 ATOM 2915 C CA . GLN A 1 366 ? 13.657 25.835 10.340 1.00 49.86 ? 366 GLN A CA 1 ATOM 2916 C C . GLN A 1 366 ? 12.995 25.814 11.718 1.00 49.50 ? 366 GLN A C 1 ATOM 2917 O O . GLN A 1 366 ? 11.802 25.514 11.819 1.00 49.33 ? 366 GLN A O 1 ATOM 2918 C CB . GLN A 1 366 ? 13.646 27.262 9.775 1.00 50.01 ? 366 GLN A CB 1 ATOM 2919 C CG . GLN A 1 366 ? 14.141 27.390 8.339 1.00 51.54 ? 366 GLN A CG 1 ATOM 2920 C CD . GLN A 1 366 ? 15.528 26.800 8.125 1.00 52.93 ? 366 GLN A CD 1 ATOM 2921 O OE1 . GLN A 1 366 ? 16.470 27.111 8.859 1.00 54.28 ? 366 GLN A OE1 1 ATOM 2922 N NE2 . GLN A 1 366 ? 15.660 25.952 7.104 1.00 53.46 ? 366 GLN A NE2 1 ATOM 2923 N N . PRO A 1 367 ? 13.768 26.104 12.784 1.00 49.23 ? 367 PRO A N 1 ATOM 2924 C CA . PRO A 1 367 ? 13.175 26.198 14.111 1.00 49.31 ? 367 PRO A CA 1 ATOM 2925 C C . PRO A 1 367 ? 11.837 26.926 14.098 1.00 49.44 ? 367 PRO A C 1 ATOM 2926 O O . PRO A 1 367 ? 11.759 28.070 13.682 1.00 49.60 ? 367 PRO A O 1 ATOM 2927 C CB . PRO A 1 367 ? 14.219 26.983 14.900 1.00 49.18 ? 367 PRO A CB 1 ATOM 2928 C CG . PRO A 1 367 ? 15.512 26.563 14.295 1.00 49.12 ? 367 PRO A CG 1 ATOM 2929 C CD . PRO A 1 367 ? 15.230 26.317 12.824 1.00 49.27 ? 367 PRO A CD 1 ATOM 2930 N N . TRP A 1 368 ? 10.795 26.226 14.527 1.00 49.82 ? 368 TRP A N 1 ATOM 2931 C CA . TRP A 1 368 ? 9.435 26.743 14.580 1.00 50.22 ? 368 TRP A CA 1 ATOM 2932 C C . TRP A 1 368 ? 9.230 27.548 15.860 1.00 50.23 ? 368 TRP A C 1 ATOM 2933 O O . TRP A 1 368 ? 8.997 26.980 16.934 1.00 50.28 ? 368 TRP A O 1 ATOM 2934 C CB . TRP A 1 368 ? 8.464 25.562 14.542 1.00 50.22 ? 368 TRP A CB 1 ATOM 2935 C CG . TRP A 1 368 ? 7.028 25.890 14.300 1.00 50.71 ? 368 TRP A CG 1 ATOM 2936 C CD1 . TRP A 1 368 ? 6.420 26.081 13.089 1.00 51.70 ? 368 TRP A CD1 1 ATOM 2937 C CD2 . TRP A 1 368 ? 5.999 26.000 15.284 1.00 50.48 ? 368 TRP A CD2 1 ATOM 2938 N NE1 . TRP A 1 368 ? 5.077 26.322 13.263 1.00 51.00 ? 368 TRP A NE1 1 ATOM 2939 C CE2 . TRP A 1 368 ? 4.795 26.280 14.602 1.00 51.11 ? 368 TRP A CE2 1 ATOM 2940 C CE3 . TRP A 1 368 ? 5.978 25.900 16.676 1.00 51.29 ? 368 TRP A CE3 1 ATOM 2941 C CZ2 . TRP A 1 368 ? 3.582 26.466 15.268 1.00 51.80 ? 368 TRP A CZ2 1 ATOM 2942 C CZ3 . TRP A 1 368 ? 4.775 26.080 17.335 1.00 52.29 ? 368 TRP A CZ3 1 ATOM 2943 C CH2 . TRP A 1 368 ? 3.593 26.366 16.629 1.00 52.28 ? 368 TRP A CH2 1 ATOM 2944 N N . GLY A 1 369 ? 9.321 28.870 15.739 1.00 50.22 ? 369 GLY A N 1 ATOM 2945 C CA . GLY A 1 369 ? 9.111 29.769 16.879 1.00 50.20 ? 369 GLY A CA 1 ATOM 2946 C C . GLY A 1 369 ? 10.366 30.011 17.705 1.00 49.92 ? 369 GLY A C 1 ATOM 2947 O O . GLY A 1 369 ? 11.459 29.607 17.306 1.00 50.35 ? 369 GLY A O 1 ATOM 2948 N N . PRO A 1 370 ? 10.218 30.663 18.873 1.00 49.66 ? 370 PRO A N 1 ATOM 2949 C CA . PRO A 1 370 ? 11.393 30.970 19.689 1.00 49.20 ? 370 PRO A CA 1 ATOM 2950 C C . PRO A 1 370 ? 11.712 29.849 20.688 1.00 48.62 ? 370 PRO A C 1 ATOM 2951 O O . PRO A 1 370 ? 12.786 29.840 21.308 1.00 48.66 ? 370 PRO A O 1 ATOM 2952 C CB . PRO A 1 370 ? 10.964 32.236 20.427 1.00 49.44 ? 370 PRO A CB 1 ATOM 2953 C CG . PRO A 1 370 ? 9.452 32.077 20.600 1.00 49.51 ? 370 PRO A CG 1 ATOM 2954 C CD . PRO A 1 370 ? 8.966 31.135 19.504 1.00 49.63 ? 370 PRO A CD 1 ATOM 2955 N N . GLU A 1 371 ? 10.773 28.920 20.840 1.00 47.52 ? 371 GLU A N 1 ATOM 2956 C CA . GLU A 1 371 ? 10.913 27.820 21.785 1.00 46.54 ? 371 GLU A CA 1 ATOM 2957 C C . GLU A 1 371 ? 10.693 26.506 21.031 1.00 45.33 ? 371 GLU A C 1 ATOM 2958 O O . GLU A 1 371 ? 9.964 25.617 21.479 1.00 45.32 ? 371 GLU A O 1 ATOM 2959 C CB . GLU A 1 371 ? 9.971 28.020 22.995 1.00 46.67 ? 371 GLU A CB 1 ATOM 2960 C CG . GLU A 1 371 ? 10.387 29.231 23.886 1.00 47.66 ? 371 GLU A CG 1 ATOM 2961 C CD . GLU A 1 371 ? 9.311 29.716 24.879 1.00 49.08 ? 371 GLU A CD 1 ATOM 2962 O OE1 . GLU A 1 371 ? 8.107 29.394 24.707 1.00 50.15 ? 371 GLU A OE1 1 ATOM 2963 O OE2 . GLU A 1 371 ? 9.680 30.450 25.832 1.00 48.58 ? 371 GLU A OE2 1 ATOM 2964 N N . ALA A 1 372 ? 11.354 26.405 19.876 1.00 43.78 ? 372 ALA A N 1 ATOM 2965 C CA . ALA A 1 372 ? 11.245 25.245 18.984 1.00 42.36 ? 372 ALA A CA 1 ATOM 2966 C C . ALA A 1 372 ? 11.737 23.943 19.630 1.00 41.27 ? 372 ALA A C 1 ATOM 2967 O O . ALA A 1 372 ? 11.126 22.891 19.454 1.00 41.08 ? 372 ALA A O 1 ATOM 2968 C CB . ALA A 1 372 ? 12.011 25.512 17.689 1.00 42.44 ? 372 ALA A CB 1 ATOM 2969 N N . GLU A 1 373 ? 12.835 24.035 20.384 1.00 39.67 ? 373 GLU A N 1 ATOM 2970 C CA . GLU A 1 373 ? 13.459 22.880 21.005 1.00 38.36 ? 373 GLU A CA 1 ATOM 2971 C C . GLU A 1 373 ? 13.206 22.862 22.507 1.00 36.89 ? 373 GLU A C 1 ATOM 2972 O O . GLU A 1 373 ? 13.473 23.862 23.187 1.00 37.01 ? 373 GLU A O 1 ATOM 2973 C CB . GLU A 1 373 ? 14.954 22.891 20.713 1.00 38.68 ? 373 GLU A CB 1 ATOM 2974 C CG . GLU A 1 373 ? 15.748 21.881 21.527 1.00 40.61 ? 373 GLU A CG 1 ATOM 2975 C CD . GLU A 1 373 ? 17.196 21.833 21.118 1.00 43.19 ? 373 GLU A CD 1 ATOM 2976 O OE1 . GLU A 1 373 ? 18.024 21.338 21.906 1.00 45.61 ? 373 GLU A OE1 1 ATOM 2977 O OE2 . GLU A 1 373 ? 17.520 22.283 20.004 1.00 46.27 ? 373 GLU A OE2 1 ATOM 2978 N N . LEU A 1 374 ? 12.711 21.724 23.011 1.00 34.79 ? 374 LEU A N 1 ATOM 2979 C CA . LEU A 1 374 ? 12.260 21.576 24.412 1.00 32.99 ? 374 LEU A CA 1 ATOM 2980 C C . LEU A 1 374 ? 12.878 20.362 25.119 1.00 31.92 ? 374 LEU A C 1 ATOM 2981 O O . LEU A 1 374 ? 13.120 19.348 24.478 1.00 31.01 ? 374 LEU A O 1 ATOM 2982 C CB . LEU A 1 374 ? 10.734 21.444 24.466 1.00 33.02 ? 374 LEU A CB 1 ATOM 2983 C CG . LEU A 1 374 ? 9.849 22.492 23.778 1.00 32.63 ? 374 LEU A CG 1 ATOM 2984 C CD1 . LEU A 1 374 ? 8.495 21.896 23.454 1.00 33.03 ? 374 LEU A CD1 1 ATOM 2985 C CD2 . LEU A 1 374 ? 9.693 23.727 24.620 1.00 32.11 ? 374 LEU A CD2 1 ATOM 2986 N N . PRO A 1 375 ? 13.155 20.468 26.443 1.00 31.39 ? 375 PRO A N 1 ATOM 2987 C CA . PRO A 1 375 ? 13.616 19.286 27.197 1.00 30.95 ? 375 PRO A CA 1 ATOM 2988 C C . PRO A 1 375 ? 12.565 18.176 27.199 1.00 30.60 ? 375 PRO A C 1 ATOM 2989 O O . PRO A 1 375 ? 11.369 18.441 27.367 1.00 30.14 ? 375 PRO A O 1 ATOM 2990 C CB . PRO A 1 375 ? 13.852 19.826 28.621 1.00 30.61 ? 375 PRO A CB 1 ATOM 2991 C CG . PRO A 1 375 ? 14.023 21.285 28.450 1.00 30.75 ? 375 PRO A CG 1 ATOM 2992 C CD . PRO A 1 375 ? 13.112 21.665 27.303 1.00 31.23 ? 375 PRO A CD 1 ATOM 2993 N N . LEU A 1 376 ? 13.013 16.940 26.998 1.00 30.34 ? 376 LEU A N 1 ATOM 2994 C CA . LEU A 1 376 ? 12.081 15.841 26.837 1.00 30.31 ? 376 LEU A CA 1 ATOM 2995 C C . LEU A 1 376 ? 11.180 15.713 28.052 1.00 30.38 ? 376 LEU A C 1 ATOM 2996 O O . LEU A 1 376 ? 10.007 15.378 27.903 1.00 30.51 ? 376 LEU A O 1 ATOM 2997 C CB . LEU A 1 376 ? 12.811 14.537 26.548 1.00 30.37 ? 376 LEU A CB 1 ATOM 2998 C CG . LEU A 1 376 ? 12.011 13.249 26.718 1.00 30.18 ? 376 LEU A CG 1 ATOM 2999 C CD1 . LEU A 1 376 ? 11.083 12.976 25.527 1.00 28.90 ? 376 LEU A CD1 1 ATOM 3000 C CD2 . LEU A 1 376 ? 12.995 12.110 26.974 1.00 30.36 ? 376 LEU A CD2 1 ATOM 3001 N N . HIS A 1 377 ? 11.708 16.025 29.238 1.00 30.54 ? 377 HIS A N 1 ATOM 3002 C CA . HIS A 1 377 ? 10.942 15.857 30.479 1.00 30.65 ? 377 HIS A CA 1 ATOM 3003 C C . HIS A 1 377 ? 9.672 16.710 30.589 1.00 30.88 ? 377 HIS A C 1 ATOM 3004 O O . HIS A 1 377 ? 8.745 16.333 31.309 1.00 31.65 ? 377 HIS A O 1 ATOM 3005 C CB . HIS A 1 377 ? 11.822 15.961 31.723 1.00 30.30 ? 377 HIS A CB 1 ATOM 3006 C CG . HIS A 1 377 ? 11.974 17.350 32.265 1.00 31.06 ? 377 HIS A CG 1 ATOM 3007 N ND1 . HIS A 1 377 ? 13.016 18.183 31.907 1.00 31.48 ? 377 HIS A ND1 1 ATOM 3008 C CD2 . HIS A 1 377 ? 11.243 18.035 33.176 1.00 31.05 ? 377 HIS A CD2 1 ATOM 3009 C CE1 . HIS A 1 377 ? 12.906 19.327 32.560 1.00 30.73 ? 377 HIS A CE1 1 ATOM 3010 N NE2 . HIS A 1 377 ? 11.840 19.263 33.338 1.00 30.81 ? 377 HIS A NE2 1 ATOM 3011 N N . THR A 1 378 ? 9.610 17.830 29.866 1.00 30.61 ? 378 THR A N 1 ATOM 3012 C CA . THR A 1 378 ? 8.386 18.631 29.841 1.00 30.52 ? 378 THR A CA 1 ATOM 3013 C C . THR A 1 378 ? 7.352 18.059 28.892 1.00 30.89 ? 378 THR A C 1 ATOM 3014 O O . THR A 1 378 ? 6.300 18.658 28.703 1.00 31.60 ? 378 THR A O 1 ATOM 3015 C CB . THR A 1 378 ? 8.615 20.090 29.397 1.00 30.39 ? 378 THR A CB 1 ATOM 3016 O OG1 . THR A 1 378 ? 8.894 20.130 27.988 1.00 28.32 ? 378 THR A OG1 1 ATOM 3017 C CG2 . THR A 1 378 ? 9.733 20.755 30.203 1.00 30.70 ? 378 THR A CG2 1 ATOM 3018 N N . LEU A 1 379 ? 7.646 16.918 28.281 1.00 31.08 ? 379 LEU A N 1 ATOM 3019 C CA . LEU A 1 379 ? 6.756 16.372 27.259 1.00 31.15 ? 379 LEU A CA 1 ATOM 3020 C C . LEU A 1 379 ? 6.128 15.048 27.631 1.00 31.00 ? 379 LEU A C 1 ATOM 3021 O O . LEU A 1 379 ? 5.339 14.504 26.857 1.00 30.97 ? 379 LEU A O 1 ATOM 3022 C CB . LEU A 1 379 ? 7.458 16.274 25.904 1.00 31.11 ? 379 LEU A CB 1 ATOM 3023 C CG . LEU A 1 379 ? 7.891 17.651 25.404 1.00 31.84 ? 379 LEU A CG 1 ATOM 3024 C CD1 . LEU A 1 379 ? 8.772 17.483 24.187 1.00 33.64 ? 379 LEU A CD1 1 ATOM 3025 C CD2 . LEU A 1 379 ? 6.685 18.556 25.106 1.00 30.66 ? 379 LEU A CD2 1 ATOM 3026 N N . PHE A 1 380 ? 6.473 14.524 28.807 1.00 31.00 ? 380 PHE A N 1 ATOM 3027 C CA . PHE A 1 380 ? 5.813 13.325 29.284 1.00 31.03 ? 380 PHE A CA 1 ATOM 3028 C C . PHE A 1 380 ? 4.362 13.694 29.536 1.00 31.50 ? 380 PHE A C 1 ATOM 3029 O O . PHE A 1 380 ? 4.088 14.711 30.171 1.00 31.75 ? 380 PHE A O 1 ATOM 3030 C CB . PHE A 1 380 ? 6.454 12.788 30.552 1.00 30.29 ? 380 PHE A CB 1 ATOM 3031 C CG . PHE A 1 380 ? 7.920 12.506 30.425 1.00 29.89 ? 380 PHE A CG 1 ATOM 3032 C CD1 . PHE A 1 380 ? 8.426 11.853 29.312 1.00 29.90 ? 380 PHE A CD1 1 ATOM 3033 C CD2 . PHE A 1 380 ? 8.799 12.869 31.451 1.00 28.42 ? 380 PHE A CD2 1 ATOM 3034 C CE1 . PHE A 1 380 ? 9.791 11.587 29.212 1.00 30.03 ? 380 PHE A CE1 1 ATOM 3035 C CE2 . PHE A 1 380 ? 10.139 12.606 31.361 1.00 27.94 ? 380 PHE A CE2 1 ATOM 3036 C CZ . PHE A 1 380 ? 10.644 11.963 30.233 1.00 28.44 ? 380 PHE A CZ 1 ATOM 3037 N N . PHE A 1 381 ? 3.448 12.896 28.988 1.00 31.86 ? 381 PHE A N 1 ATOM 3038 C CA . PHE A 1 381 ? 2.002 13.080 29.174 1.00 32.68 ? 381 PHE A CA 1 ATOM 3039 C C . PHE A 1 381 ? 1.506 14.473 28.793 1.00 33.29 ? 381 PHE A C 1 ATOM 3040 O O . PHE A 1 381 ? 0.519 14.967 29.337 1.00 33.78 ? 381 PHE A O 1 ATOM 3041 C CB . PHE A 1 381 ? 1.581 12.682 30.596 1.00 32.48 ? 381 PHE A CB 1 ATOM 3042 C CG . PHE A 1 381 ? 1.787 11.229 30.879 1.00 32.29 ? 381 PHE A CG 1 ATOM 3043 C CD1 . PHE A 1 381 ? 0.842 10.293 30.473 1.00 31.67 ? 381 PHE A CD1 1 ATOM 3044 C CD2 . PHE A 1 381 ? 2.946 10.790 31.493 1.00 31.31 ? 381 PHE A CD2 1 ATOM 3045 C CE1 . PHE A 1 381 ? 1.037 8.944 30.704 1.00 31.99 ? 381 PHE A CE1 1 ATOM 3046 C CE2 . PHE A 1 381 ? 3.147 9.443 31.731 1.00 32.22 ? 381 PHE A CE2 1 ATOM 3047 C CZ . PHE A 1 381 ? 2.186 8.517 31.338 1.00 32.13 ? 381 PHE A CZ 1 ATOM 3048 N N . ASN A 1 382 ? 2.201 15.083 27.836 1.00 33.44 ? 382 ASN A N 1 ATOM 3049 C CA . ASN A 1 382 ? 1.905 16.419 27.391 1.00 33.49 ? 382 ASN A CA 1 ATOM 3050 C C . ASN A 1 382 ? 1.141 16.342 26.080 1.00 33.90 ? 382 ASN A C 1 ATOM 3051 O O . ASN A 1 382 ? 1.709 16.037 25.038 1.00 34.19 ? 382 ASN A O 1 ATOM 3052 C CB . ASN A 1 382 ? 3.214 17.207 27.250 1.00 33.32 ? 382 ASN A CB 1 ATOM 3053 C CG . ASN A 1 382 ? 2.998 18.667 26.925 1.00 33.34 ? 382 ASN A CG 1 ATOM 3054 O OD1 . ASN A 1 382 ? 2.154 19.016 26.097 1.00 32.97 ? 382 ASN A OD1 1 ATOM 3055 N ND2 . ASN A 1 382 ? 3.775 19.536 27.570 1.00 32.37 ? 382 ASN A ND2 1 ATOM 3056 N N . THR A 1 383 ? -0.160 16.603 26.149 1.00 34.33 ? 383 THR A N 1 ATOM 3057 C CA . THR A 1 383 ? -1.010 16.678 24.962 1.00 34.70 ? 383 THR A CA 1 ATOM 3058 C C . THR A 1 383 ? -1.278 18.136 24.560 1.00 35.11 ? 383 THR A C 1 ATOM 3059 O O . THR A 1 383 ? -1.555 18.418 23.394 1.00 34.93 ? 383 THR A O 1 ATOM 3060 C CB . THR A 1 383 ? -2.356 15.998 25.191 1.00 34.59 ? 383 THR A CB 1 ATOM 3061 O OG1 . THR A 1 383 ? -2.987 16.588 26.330 1.00 35.26 ? 383 THR A OG1 1 ATOM 3062 C CG2 . THR A 1 383 ? -2.183 14.505 25.442 1.00 34.82 ? 383 THR A CG2 1 ATOM 3063 N N . TRP A 1 384 ? -1.173 19.059 25.517 1.00 35.50 ? 384 TRP A N 1 ATOM 3064 C CA . TRP A 1 384 ? -1.511 20.463 25.267 1.00 35.96 ? 384 TRP A CA 1 ATOM 3065 C C . TRP A 1 384 ? -0.623 21.114 24.219 1.00 36.74 ? 384 TRP A C 1 ATOM 3066 O O . TRP A 1 384 ? -1.043 22.051 23.542 1.00 37.01 ? 384 TRP A O 1 ATOM 3067 C CB . TRP A 1 384 ? -1.552 21.282 26.563 1.00 35.55 ? 384 TRP A CB 1 ATOM 3068 C CG . TRP A 1 384 ? -0.235 21.705 27.161 1.00 34.96 ? 384 TRP A CG 1 ATOM 3069 C CD1 . TRP A 1 384 ? 0.400 21.125 28.213 1.00 34.24 ? 384 TRP A CD1 1 ATOM 3070 C CD2 . TRP A 1 384 ? 0.562 22.844 26.792 1.00 34.94 ? 384 TRP A CD2 1 ATOM 3071 N NE1 . TRP A 1 384 ? 1.558 21.807 28.508 1.00 34.81 ? 384 TRP A NE1 1 ATOM 3072 C CE2 . TRP A 1 384 ? 1.679 22.866 27.649 1.00 34.82 ? 384 TRP A CE2 1 ATOM 3073 C CE3 . TRP A 1 384 ? 0.448 23.836 25.807 1.00 36.55 ? 384 TRP A CE3 1 ATOM 3074 C CZ2 . TRP A 1 384 ? 2.679 23.838 27.552 1.00 35.63 ? 384 TRP A CZ2 1 ATOM 3075 C CZ3 . TRP A 1 384 ? 1.450 24.807 25.709 1.00 36.06 ? 384 TRP A CZ3 1 ATOM 3076 C CH2 . TRP A 1 384 ? 2.544 24.798 26.578 1.00 35.93 ? 384 TRP A CH2 1 ATOM 3077 N N . ARG A 1 385 ? 0.590 20.591 24.071 1.00 37.52 ? 385 ARG A N 1 ATOM 3078 C CA . ARG A 1 385 ? 1.545 21.112 23.109 1.00 37.80 ? 385 ARG A CA 1 ATOM 3079 C C . ARG A 1 385 ? 1.170 20.733 21.689 1.00 38.60 ? 385 ARG A C 1 ATOM 3080 O O . ARG A 1 385 ? 1.590 21.393 20.750 1.00 39.08 ? 385 ARG A O 1 ATOM 3081 C CB . ARG A 1 385 ? 2.941 20.599 23.426 1.00 37.90 ? 385 ARG A CB 1 ATOM 3082 C CG . ARG A 1 385 ? 3.637 21.317 24.537 1.00 37.38 ? 385 ARG A CG 1 ATOM 3083 C CD . ARG A 1 385 ? 4.349 22.531 24.012 1.00 37.32 ? 385 ARG A CD 1 ATOM 3084 N NE . ARG A 1 385 ? 5.176 23.124 25.055 1.00 37.32 ? 385 ARG A NE 1 ATOM 3085 C CZ . ARG A 1 385 ? 5.705 24.340 24.988 1.00 36.87 ? 385 ARG A CZ 1 ATOM 3086 N NH1 . ARG A 1 385 ? 5.495 25.094 23.922 1.00 36.36 ? 385 ARG A NH1 1 ATOM 3087 N NH2 . ARG A 1 385 ? 6.454 24.793 25.987 1.00 37.21 ? 385 ARG A NH2 1 ATOM 3088 N N . ILE A 1 386 ? 0.402 19.663 21.515 1.00 39.40 ? 386 ILE A N 1 ATOM 3089 C CA . ILE A 1 386 ? -0.068 19.327 20.184 1.00 40.21 ? 386 ILE A CA 1 ATOM 3090 C C . ILE A 1 386 ? -1.260 20.208 19.853 1.00 41.12 ? 386 ILE A C 1 ATOM 3091 O O . ILE A 1 386 ? -1.204 20.994 18.914 1.00 41.42 ? 386 ILE A O 1 ATOM 3092 C CB . ILE A 1 386 ? -0.452 17.845 20.019 1.00 40.01 ? 386 ILE A CB 1 ATOM 3093 C CG1 . ILE A 1 386 ? 0.726 16.934 20.367 1.00 40.20 ? 386 ILE A CG1 1 ATOM 3094 C CG2 . ILE A 1 386 ? -0.892 17.569 18.571 1.00 40.20 ? 386 ILE A CG2 1 ATOM 3095 C CD1 . ILE A 1 386 ? 0.358 15.458 20.526 1.00 40.22 ? 386 ILE A CD1 1 ATOM 3096 N N . ILE A 1 387 ? -2.325 20.077 20.639 1.00 42.20 ? 387 ILE A N 1 ATOM 3097 C CA . ILE A 1 387 ? -3.591 20.760 20.380 1.00 43.23 ? 387 ILE A CA 1 ATOM 3098 C C . ILE A 1 387 ? -3.452 22.278 20.310 1.00 43.54 ? 387 ILE A C 1 ATOM 3099 O O . ILE A 1 387 ? -4.065 22.918 19.446 1.00 43.42 ? 387 ILE A O 1 ATOM 3100 C CB . ILE A 1 387 ? -4.662 20.391 21.446 1.00 43.60 ? 387 ILE A CB 1 ATOM 3101 C CG1 . ILE A 1 387 ? -4.977 18.896 21.389 1.00 44.25 ? 387 ILE A CG1 1 ATOM 3102 C CG2 . ILE A 1 387 ? -5.970 21.189 21.242 1.00 43.82 ? 387 ILE A CG2 1 ATOM 3103 C CD1 . ILE A 1 387 ? -4.173 18.067 22.339 1.00 46.91 ? 387 ILE A CD1 1 ATOM 3104 N N . LYS A 1 388 ? -2.629 22.834 21.205 1.00 43.95 ? 388 LYS A N 1 ATOM 3105 C CA . LYS A 1 388 ? -2.553 24.284 21.407 1.00 44.11 ? 388 LYS A CA 1 ATOM 3106 C C . LYS A 1 388 ? -1.249 24.964 20.951 1.00 43.91 ? 388 LYS A C 1 ATOM 3107 O O . LYS A 1 388 ? -0.954 26.080 21.376 1.00 44.29 ? 388 LYS A O 1 ATOM 3108 C CB . LYS A 1 388 ? -2.857 24.617 22.877 1.00 44.30 ? 388 LYS A CB 1 ATOM 3109 C CG . LYS A 1 388 ? -4.355 24.590 23.234 1.00 45.94 ? 388 LYS A CG 1 ATOM 3110 C CD . LYS A 1 388 ? -4.612 25.138 24.637 1.00 49.11 ? 388 LYS A CD 1 ATOM 3111 C CE . LYS A 1 388 ? -6.018 25.759 24.783 1.00 51.22 ? 388 LYS A CE 1 ATOM 3112 N NZ . LYS A 1 388 ? -6.068 27.272 24.639 1.00 51.81 ? 388 LYS A NZ 1 ATOM 3113 N N . ASP A 1 389 ? -0.494 24.324 20.063 1.00 43.51 ? 389 ASP A N 1 ATOM 3114 C CA . ASP A 1 389 ? 0.853 24.793 19.725 1.00 43.14 ? 389 ASP A CA 1 ATOM 3115 C C . ASP A 1 389 ? 1.367 24.261 18.370 1.00 42.65 ? 389 ASP A C 1 ATOM 3116 O O . ASP A 1 389 ? 2.546 23.947 18.233 1.00 42.88 ? 389 ASP A O 1 ATOM 3117 C CB . ASP A 1 389 ? 1.822 24.400 20.861 1.00 43.36 ? 389 ASP A CB 1 ATOM 3118 C CG . ASP A 1 389 ? 3.004 25.375 21.028 1.00 44.18 ? 389 ASP A CG 1 ATOM 3119 O OD1 . ASP A 1 389 ? 2.930 26.535 20.561 1.00 45.95 ? 389 ASP A OD1 1 ATOM 3120 O OD2 . ASP A 1 389 ? 4.013 24.974 21.654 1.00 43.96 ? 389 ASP A OD2 1 ATOM 3121 N N . GLY A 1 390 ? 0.481 24.138 17.382 1.00 41.99 ? 390 GLY A N 1 ATOM 3122 C CA . GLY A 1 390 ? 0.888 23.848 16.007 1.00 41.01 ? 390 GLY A CA 1 ATOM 3123 C C . GLY A 1 390 ? 0.462 22.516 15.401 1.00 40.74 ? 390 GLY A C 1 ATOM 3124 O O . GLY A 1 390 ? 0.756 22.241 14.234 1.00 40.59 ? 390 GLY A O 1 ATOM 3125 N N . GLY A 1 391 ? -0.217 21.677 16.180 1.00 40.37 ? 391 GLY A N 1 ATOM 3126 C CA . GLY A 1 391 ? -0.625 20.358 15.694 1.00 40.00 ? 391 GLY A CA 1 ATOM 3127 C C . GLY A 1 391 ? 0.527 19.389 15.472 1.00 39.76 ? 391 GLY A C 1 ATOM 3128 O O . GLY A 1 391 ? 1.533 19.440 16.182 1.00 39.87 ? 391 GLY A O 1 ATOM 3129 N N . ILE A 1 392 ? 0.382 18.538 14.453 1.00 39.51 ? 392 ILE A N 1 ATOM 3130 C CA . ILE A 1 392 ? 1.229 17.351 14.226 1.00 39.39 ? 392 ILE A CA 1 ATOM 3131 C C . ILE A 1 392 ? 2.448 17.581 13.316 1.00 39.28 ? 392 ILE A C 1 ATOM 3132 O O . ILE A 1 392 ? 3.519 16.995 13.520 1.00 39.14 ? 392 ILE A O 1 ATOM 3133 C CB . ILE A 1 392 ? 0.346 16.187 13.671 1.00 39.34 ? 392 ILE A CB 1 ATOM 3134 C CG1 . ILE A 1 392 ? -0.313 15.422 14.814 1.00 39.79 ? 392 ILE A CG1 1 ATOM 3135 C CG2 . ILE A 1 392 ? 1.116 15.231 12.790 1.00 39.54 ? 392 ILE A CG2 1 ATOM 3136 C CD1 . ILE A 1 392 ? 0.642 15.006 15.894 1.00 41.44 ? 392 ILE A CD1 1 ATOM 3137 N N . ASP A 1 393 ? 2.274 18.434 12.315 1.00 38.87 ? 393 ASP A N 1 ATOM 3138 C CA . ASP A 1 393 ? 3.284 18.632 11.290 1.00 38.71 ? 393 ASP A CA 1 ATOM 3139 C C . ASP A 1 393 ? 4.652 19.112 11.808 1.00 38.25 ? 393 ASP A C 1 ATOM 3140 O O . ASP A 1 393 ? 5.674 18.514 11.456 1.00 38.04 ? 393 ASP A O 1 ATOM 3141 C CB . ASP A 1 393 ? 2.743 19.533 10.176 1.00 38.84 ? 393 ASP A CB 1 ATOM 3142 C CG . ASP A 1 393 ? 1.591 18.890 9.414 1.00 39.57 ? 393 ASP A CG 1 ATOM 3143 O OD1 . ASP A 1 393 ? 1.018 17.890 9.898 1.00 39.56 ? 393 ASP A OD1 1 ATOM 3144 O OD2 . ASP A 1 393 ? 1.260 19.390 8.320 1.00 41.03 ? 393 ASP A OD2 1 ATOM 3145 N N . PRO A 1 394 ? 4.682 20.180 12.644 1.00 37.69 ? 394 PRO A N 1 ATOM 3146 C CA . PRO A 1 394 ? 5.985 20.654 13.166 1.00 37.21 ? 394 PRO A CA 1 ATOM 3147 C C . PRO A 1 394 ? 6.741 19.581 13.970 1.00 36.51 ? 394 PRO A C 1 ATOM 3148 O O . PRO A 1 394 ? 7.967 19.657 14.130 1.00 36.23 ? 394 PRO A O 1 ATOM 3149 C CB . PRO A 1 394 ? 5.595 21.813 14.092 1.00 37.30 ? 394 PRO A CB 1 ATOM 3150 C CG . PRO A 1 394 ? 4.233 22.224 13.640 1.00 37.61 ? 394 PRO A CG 1 ATOM 3151 C CD . PRO A 1 394 ? 3.563 21.003 13.140 1.00 37.30 ? 394 PRO A CD 1 ATOM 3152 N N . LEU A 1 395 ? 5.989 18.594 14.446 1.00 35.56 ? 395 LEU A N 1 ATOM 3153 C CA . LEU A 1 395 ? 6.479 17.570 15.353 1.00 34.74 ? 395 LEU A CA 1 ATOM 3154 C C . LEU A 1 395 ? 6.958 16.360 14.539 1.00 34.05 ? 395 LEU A C 1 ATOM 3155 O O . LEU A 1 395 ? 7.895 15.674 14.946 1.00 34.25 ? 395 LEU A O 1 ATOM 3156 C CB . LEU A 1 395 ? 5.342 17.189 16.311 1.00 34.67 ? 395 LEU A CB 1 ATOM 3157 C CG . LEU A 1 395 ? 5.450 17.012 17.827 1.00 34.18 ? 395 LEU A CG 1 ATOM 3158 C CD1 . LEU A 1 395 ? 6.460 17.917 18.501 1.00 33.68 ? 395 LEU A CD1 1 ATOM 3159 C CD2 . LEU A 1 395 ? 4.069 17.247 18.412 1.00 33.34 ? 395 LEU A CD2 1 ATOM 3160 N N . VAL A 1 396 ? 6.324 16.130 13.382 1.00 33.06 ? 396 VAL A N 1 ATOM 3161 C CA . VAL A 1 396 ? 6.720 15.069 12.428 1.00 31.85 ? 396 VAL A CA 1 ATOM 3162 C C . VAL A 1 396 ? 7.971 15.441 11.625 1.00 30.86 ? 396 VAL A C 1 ATOM 3163 O O . VAL A 1 396 ? 8.797 14.584 11.306 1.00 30.81 ? 396 VAL A O 1 ATOM 3164 C CB . VAL A 1 396 ? 5.560 14.696 11.463 1.00 31.78 ? 396 VAL A CB 1 ATOM 3165 C CG1 . VAL A 1 396 ? 6.022 13.745 10.380 1.00 31.24 ? 396 VAL A CG1 1 ATOM 3166 C CG2 . VAL A 1 396 ? 4.413 14.068 12.233 1.00 32.09 ? 396 VAL A CG2 1 ATOM 3167 N N . ARG A 1 397 ? 8.123 16.716 11.316 1.00 29.98 ? 397 ARG A N 1 ATOM 3168 C CA . ARG A 1 397 ? 9.312 17.178 10.623 1.00 29.97 ? 397 ARG A CA 1 ATOM 3169 C C . ARG A 1 397 ? 10.553 16.957 11.477 1.00 29.63 ? 397 ARG A C 1 ATOM 3170 O O . ARG A 1 397 ? 11.602 16.601 10.964 1.00 29.23 ? 397 ARG A O 1 ATOM 3171 C CB . ARG A 1 397 ? 9.185 18.654 10.280 1.00 30.19 ? 397 ARG A CB 1 ATOM 3172 C CG . ARG A 1 397 ? 8.163 18.967 9.213 1.00 31.86 ? 397 ARG A CG 1 ATOM 3173 C CD . ARG A 1 397 ? 8.041 20.473 9.031 1.00 33.33 ? 397 ARG A CD 1 ATOM 3174 N NE . ARG A 1 397 ? 7.070 20.806 8.002 1.00 33.91 ? 397 ARG A NE 1 ATOM 3175 C CZ . ARG A 1 397 ? 5.902 21.387 8.252 1.00 34.81 ? 397 ARG A CZ 1 ATOM 3176 N NH1 . ARG A 1 397 ? 5.569 21.710 9.500 1.00 34.43 ? 397 ARG A NH1 1 ATOM 3177 N NH2 . ARG A 1 397 ? 5.080 21.659 7.249 1.00 34.04 ? 397 ARG A NH2 1 ATOM 3178 N N . GLY A 1 398 ? 10.425 17.183 12.783 1.00 29.79 ? 398 GLY A N 1 ATOM 3179 C CA . GLY A 1 398 ? 11.494 16.883 13.738 1.00 30.10 ? 398 GLY A CA 1 ATOM 3180 C C . GLY A 1 398 ? 11.921 15.423 13.682 1.00 30.14 ? 398 GLY A C 1 ATOM 3181 O O . GLY A 1 398 ? 13.105 15.116 13.734 1.00 30.14 ? 398 GLY A O 1 ATOM 3182 N N . LEU A 1 399 ? 10.952 14.523 13.550 1.00 30.20 ? 399 LEU A N 1 ATOM 3183 C CA . LEU A 1 399 ? 11.232 13.092 13.476 1.00 30.37 ? 399 LEU A CA 1 ATOM 3184 C C . LEU A 1 399 ? 12.081 12.692 12.257 1.00 30.49 ? 399 LEU A C 1 ATOM 3185 O O . LEU A 1 399 ? 12.843 11.713 12.308 1.00 30.72 ? 399 LEU A O 1 ATOM 3186 C CB . LEU A 1 399 ? 9.922 12.295 13.495 1.00 30.24 ? 399 LEU A CB 1 ATOM 3187 C CG . LEU A 1 399 ? 9.257 11.994 14.838 1.00 30.58 ? 399 LEU A CG 1 ATOM 3188 C CD1 . LEU A 1 399 ? 7.879 11.399 14.582 1.00 30.76 ? 399 LEU A CD1 1 ATOM 3189 C CD2 . LEU A 1 399 ? 10.109 11.048 15.707 1.00 29.00 ? 399 LEU A CD2 1 ATOM 3190 N N . LEU A 1 400 ? 11.939 13.442 11.167 1.00 30.42 ? 400 LEU A N 1 ATOM 3191 C CA . LEU A 1 400 ? 12.678 13.172 9.942 1.00 30.17 ? 400 LEU A CA 1 ATOM 3192 C C . LEU A 1 400 ? 14.050 13.860 9.944 1.00 30.50 ? 400 LEU A C 1 ATOM 3193 O O . LEU A 1 400 ? 15.028 13.296 9.440 1.00 30.73 ? 400 LEU A O 1 ATOM 3194 C CB . LEU A 1 400 ? 11.853 13.588 8.720 1.00 30.00 ? 400 LEU A CB 1 ATOM 3195 C CG . LEU A 1 400 ? 10.451 12.951 8.568 1.00 30.25 ? 400 LEU A CG 1 ATOM 3196 C CD1 . LEU A 1 400 ? 9.619 13.640 7.496 1.00 29.44 ? 400 LEU A CD1 1 ATOM 3197 C CD2 . LEU A 1 400 ? 10.531 11.460 8.274 1.00 29.21 ? 400 LEU A CD2 1 ATOM 3198 N N . ALA A 1 401 ? 14.130 15.054 10.540 1.00 30.43 ? 401 ALA A N 1 ATOM 3199 C CA . ALA A 1 401 ? 15.311 15.914 10.412 1.00 30.28 ? 401 ALA A CA 1 ATOM 3200 C C . ALA A 1 401 ? 16.316 15.825 11.573 1.00 30.52 ? 401 ALA A C 1 ATOM 3201 O O . ALA A 1 401 ? 17.476 16.183 11.413 1.00 30.54 ? 401 ALA A O 1 ATOM 3202 C CB . ALA A 1 401 ? 14.883 17.351 10.173 1.00 30.22 ? 401 ALA A CB 1 ATOM 3203 N N . LYS A 1 402 ? 15.872 15.349 12.735 1.00 31.04 ? 402 LYS A N 1 ATOM 3204 C CA . LYS A 1 402 ? 16.755 15.160 13.898 1.00 30.92 ? 402 LYS A CA 1 ATOM 3205 C C . LYS A 1 402 ? 17.166 13.699 13.987 1.00 30.80 ? 402 LYS A C 1 ATOM 3206 O O . LYS A 1 402 ? 16.606 12.855 13.270 1.00 30.91 ? 402 LYS A O 1 ATOM 3207 C CB . LYS A 1 402 ? 16.063 15.594 15.191 1.00 30.69 ? 402 LYS A CB 1 ATOM 3208 C CG . LYS A 1 402 ? 15.524 17.008 15.147 1.00 31.64 ? 402 LYS A CG 1 ATOM 3209 C CD . LYS A 1 402 ? 16.647 18.029 15.165 1.00 32.70 ? 402 LYS A CD 1 ATOM 3210 C CE . LYS A 1 402 ? 16.195 19.326 14.517 1.00 33.88 ? 402 LYS A CE 1 ATOM 3211 N NZ . LYS A 1 402 ? 17.078 20.460 14.940 1.00 35.52 ? 402 LYS A NZ 1 ATOM 3212 N N . LYS A 1 403 ? 18.126 13.413 14.869 1.00 30.20 ? 403 LYS A N 1 ATOM 3213 C CA . LYS A 1 403 ? 18.713 12.083 15.005 1.00 29.86 ? 403 LYS A CA 1 ATOM 3214 C C . LYS A 1 403 ? 18.338 11.423 16.330 1.00 29.54 ? 403 LYS A C 1 ATOM 3215 O O . LYS A 1 403 ? 18.044 12.121 17.303 1.00 29.55 ? 403 LYS A O 1 ATOM 3216 C CB . LYS A 1 403 ? 20.234 12.180 14.948 1.00 30.14 ? 403 LYS A CB 1 ATOM 3217 C CG . LYS A 1 403 ? 20.818 12.785 13.669 1.00 31.74 ? 403 LYS A CG 1 ATOM 3218 C CD . LYS A 1 403 ? 22.184 13.464 13.957 1.00 33.62 ? 403 LYS A CD 1 ATOM 3219 C CE . LYS A 1 403 ? 22.985 13.790 12.696 1.00 33.22 ? 403 LYS A CE 1 ATOM 3220 N NZ . LYS A 1 403 ? 22.115 14.321 11.593 1.00 35.47 ? 403 LYS A NZ 1 ATOM 3221 N N . SER A 1 404 ? 18.357 10.081 16.364 1.00 28.46 ? 404 SER A N 1 ATOM 3222 C CA . SER A 1 404 ? 18.273 9.331 17.615 1.00 27.38 ? 404 SER A CA 1 ATOM 3223 C C . SER A 1 404 ? 19.549 9.581 18.412 1.00 26.71 ? 404 SER A C 1 ATOM 3224 O O . SER A 1 404 ? 20.566 9.987 17.854 1.00 25.52 ? 404 SER A O 1 ATOM 3225 C CB . SER A 1 404 ? 18.157 7.821 17.362 1.00 27.04 ? 404 SER A CB 1 ATOM 3226 O OG . SER A 1 404 ? 16.940 7.483 16.718 1.00 27.67 ? 404 SER A OG 1 ATOM 3227 N N . LYS A 1 405 ? 19.485 9.331 19.721 1.00 26.36 ? 405 LYS A N 1 ATOM 3228 C CA . LYS A 1 405 ? 20.695 9.200 20.520 1.00 25.74 ? 405 LYS A CA 1 ATOM 3229 C C . LYS A 1 405 ? 21.303 7.862 20.179 1.00 25.97 ? 405 LYS A C 1 ATOM 3230 O O . LYS A 1 405 ? 20.584 6.896 19.938 1.00 24.89 ? 405 LYS A O 1 ATOM 3231 C CB . LYS A 1 405 ? 20.416 9.288 22.026 1.00 25.35 ? 405 LYS A CB 1 ATOM 3232 C CG . LYS A 1 405 ? 21.673 9.120 22.885 1.00 24.18 ? 405 LYS A CG 1 ATOM 3233 C CD . LYS A 1 405 ? 21.389 9.082 24.377 1.00 22.35 ? 405 LYS A CD 1 ATOM 3234 C CE . LYS A 1 405 ? 22.561 8.466 25.139 1.00 21.34 ? 405 LYS A CE 1 ATOM 3235 N NZ . LYS A 1 405 ? 22.835 7.053 24.752 1.00 20.77 ? 405 LYS A NZ 1 ATOM 3236 N N . LEU A 1 406 ? 22.634 7.835 20.131 1.00 27.02 ? 406 LEU A N 1 ATOM 3237 C CA . LEU A 1 406 ? 23.403 6.621 19.935 1.00 28.19 ? 406 LEU A CA 1 ATOM 3238 C C . LEU A 1 406 ? 23.767 5.976 21.271 1.00 29.33 ? 406 LEU A C 1 ATOM 3239 O O . LEU A 1 406 ? 24.269 6.655 22.189 1.00 29.85 ? 406 LEU A O 1 ATOM 3240 C CB . LEU A 1 406 ? 24.695 6.953 19.183 1.00 28.18 ? 406 LEU A CB 1 ATOM 3241 C CG . LEU A 1 406 ? 25.637 5.783 18.851 1.00 28.21 ? 406 LEU A CG 1 ATOM 3242 C CD1 . LEU A 1 406 ? 25.035 4.933 17.730 1.00 28.16 ? 406 LEU A CD1 1 ATOM 3243 C CD2 . LEU A 1 406 ? 27.061 6.244 18.492 1.00 27.35 ? 406 LEU A CD2 1 ATOM 3244 N N . MET A 1 407 ? 23.555 4.662 21.372 1.00 30.40 ? 407 MET A N 1 ATOM 3245 C CA . MET A 1 407 ? 24.022 3.912 22.534 1.00 31.17 ? 407 MET A CA 1 ATOM 3246 C C . MET A 1 407 ? 25.519 4.100 22.625 1.00 31.15 ? 407 MET A C 1 ATOM 3247 O O . MET A 1 407 ? 26.227 4.000 21.623 1.00 31.11 ? 407 MET A O 1 ATOM 3248 C CB . MET A 1 407 ? 23.702 2.429 22.409 1.00 31.77 ? 407 MET A CB 1 ATOM 3249 C CG . MET A 1 407 ? 23.335 1.735 23.729 1.00 34.51 ? 407 MET A CG 1 ATOM 3250 S SD . MET A 1 407 ? 24.579 1.827 25.037 1.00 42.13 ? 407 MET A SD 1 ATOM 3251 C CE . MET A 1 407 ? 25.969 0.975 24.257 1.00 38.14 ? 407 MET A CE 1 ATOM 3252 N N . ASN A 1 408 ? 25.985 4.377 23.836 1.00 31.14 ? 408 ASN A N 1 ATOM 3253 C CA . ASN A 1 408 ? 27.378 4.669 24.104 1.00 31.36 ? 408 ASN A CA 1 ATOM 3254 C C . ASN A 1 408 ? 27.691 4.125 25.503 1.00 30.87 ? 408 ASN A C 1 ATOM 3255 O O . ASN A 1 408 ? 26.928 4.345 26.440 1.00 29.96 ? 408 ASN A O 1 ATOM 3256 C CB . ASN A 1 408 ? 27.548 6.180 24.033 1.00 31.78 ? 408 ASN A CB 1 ATOM 3257 C CG . ASN A 1 408 ? 28.992 6.624 23.955 1.00 34.25 ? 408 ASN A CG 1 ATOM 3258 O OD1 . ASN A 1 408 ? 29.851 6.163 24.707 1.00 37.53 ? 408 ASN A OD1 1 ATOM 3259 N ND2 . ASN A 1 408 ? 29.254 7.582 23.069 1.00 36.63 ? 408 ASN A ND2 1 ATOM 3260 N N . GLN A 1 409 ? 28.798 3.407 25.649 1.00 30.71 ? 409 GLN A N 1 ATOM 3261 C CA . GLN A 1 409 ? 29.096 2.740 26.922 1.00 31.31 ? 409 GLN A CA 1 ATOM 3262 C C . GLN A 1 409 ? 29.351 3.690 28.099 1.00 32.13 ? 409 GLN A C 1 ATOM 3263 O O . GLN A 1 409 ? 29.202 3.291 29.263 1.00 31.73 ? 409 GLN A O 1 ATOM 3264 C CB . GLN A 1 409 ? 30.267 1.772 26.768 1.00 30.95 ? 409 GLN A CB 1 ATOM 3265 C CG . GLN A 1 409 ? 29.932 0.491 26.012 1.00 30.76 ? 409 GLN A CG 1 ATOM 3266 C CD . GLN A 1 409 ? 31.175 -0.345 25.756 1.00 30.36 ? 409 GLN A CD 1 ATOM 3267 O OE1 . GLN A 1 409 ? 32.260 0.199 25.575 1.00 32.56 ? 409 GLN A OE1 1 ATOM 3268 N NE2 . GLN A 1 409 ? 31.029 -1.664 25.761 1.00 27.43 ? 409 GLN A NE2 1 ATOM 3269 N N . ASP A 1 410 ? 29.730 4.934 27.789 1.00 33.08 ? 410 ASP A N 1 ATOM 3270 C CA . ASP A 1 410 ? 29.980 5.974 28.802 1.00 34.31 ? 410 ASP A CA 1 ATOM 3271 C C . ASP A 1 410 ? 28.803 6.937 28.974 1.00 34.25 ? 410 ASP A C 1 ATOM 3272 O O . ASP A 1 410 ? 28.788 7.748 29.902 1.00 34.98 ? 410 ASP A O 1 ATOM 3273 C CB . ASP A 1 410 ? 31.253 6.771 28.472 1.00 34.56 ? 410 ASP A CB 1 ATOM 3274 C CG . ASP A 1 410 ? 32.500 5.890 28.408 1.00 37.67 ? 410 ASP A CG 1 ATOM 3275 O OD1 . ASP A 1 410 ? 32.668 4.994 29.277 1.00 39.73 ? 410 ASP A OD1 1 ATOM 3276 O OD2 . ASP A 1 410 ? 33.321 6.091 27.480 1.00 41.15 ? 410 ASP A OD2 1 ATOM 3277 N N . LYS A 1 411 ? 27.829 6.859 28.071 1.00 33.93 ? 411 LYS A N 1 ATOM 3278 C CA . LYS A 1 411 ? 26.645 7.714 28.125 1.00 33.26 ? 411 LYS A CA 1 ATOM 3279 C C . LYS A 1 411 ? 25.432 6.891 27.731 1.00 32.32 ? 411 LYS A C 1 ATOM 3280 O O . LYS A 1 411 ? 25.094 6.829 26.554 1.00 32.47 ? 411 LYS A O 1 ATOM 3281 C CB . LYS A 1 411 ? 26.772 8.908 27.170 1.00 33.70 ? 411 LYS A CB 1 ATOM 3282 C CG . LYS A 1 411 ? 28.060 9.738 27.274 1.00 35.27 ? 411 LYS A CG 1 ATOM 3283 C CD . LYS A 1 411 ? 27.871 11.054 26.539 1.00 37.28 ? 411 LYS A CD 1 ATOM 3284 C CE . LYS A 1 411 ? 29.161 11.568 25.968 1.00 38.30 ? 411 LYS A CE 1 ATOM 3285 N NZ . LYS A 1 411 ? 30.095 11.932 27.058 1.00 40.51 ? 411 LYS A NZ 1 ATOM 3286 N N . MET A 1 412 ? 24.774 6.266 28.708 1.00 31.07 ? 412 MET A N 1 ATOM 3287 C CA . MET A 1 412 ? 23.716 5.304 28.402 1.00 29.62 ? 412 MET A CA 1 ATOM 3288 C C . MET A 1 412 ? 22.308 5.902 28.262 1.00 28.96 ? 412 MET A C 1 ATOM 3289 O O . MET A 1 412 ? 21.742 5.918 27.168 1.00 28.60 ? 412 MET A O 1 ATOM 3290 C CB . MET A 1 412 ? 23.750 4.159 29.410 1.00 29.62 ? 412 MET A CB 1 ATOM 3291 C CG . MET A 1 412 ? 25.048 3.387 29.370 1.00 28.93 ? 412 MET A CG 1 ATOM 3292 S SD . MET A 1 412 ? 24.920 1.802 30.206 1.00 29.60 ? 412 MET A SD 1 ATOM 3293 C CE . MET A 1 412 ? 26.547 1.129 29.882 1.00 27.32 ? 412 MET A CE 1 ATOM 3294 N N . VAL A 1 413 ? 21.749 6.396 29.364 1.00 27.96 ? 413 VAL A N 1 ATOM 3295 C CA . VAL A 1 413 ? 20.410 6.969 29.342 1.00 27.09 ? 413 VAL A CA 1 ATOM 3296 C C . VAL A 1 413 ? 20.471 8.424 29.795 1.00 26.70 ? 413 VAL A C 1 ATOM 3297 O O . VAL A 1 413 ? 21.098 8.744 30.808 1.00 27.08 ? 413 VAL A O 1 ATOM 3298 C CB . VAL A 1 413 ? 19.414 6.156 30.225 1.00 27.32 ? 413 VAL A CB 1 ATOM 3299 C CG1 . VAL A 1 413 ? 18.047 6.812 30.257 1.00 26.49 ? 413 VAL A CG1 1 ATOM 3300 C CG2 . VAL A 1 413 ? 19.287 4.704 29.730 1.00 27.23 ? 413 VAL A CG2 1 ATOM 3301 N N . THR A 1 414 ? 19.824 9.302 29.036 1.00 25.70 ? 414 THR A N 1 ATOM 3302 C CA . THR A 1 414 ? 19.837 10.722 29.332 1.00 24.87 ? 414 THR A CA 1 ATOM 3303 C C . THR A 1 414 ? 19.147 11.009 30.659 1.00 24.66 ? 414 THR A C 1 ATOM 3304 O O . THR A 1 414 ? 18.203 10.310 31.039 1.00 23.63 ? 414 THR A O 1 ATOM 3305 C CB . THR A 1 414 ? 19.192 11.553 28.188 1.00 24.86 ? 414 THR A CB 1 ATOM 3306 O OG1 . THR A 1 414 ? 19.356 12.941 28.472 1.00 25.36 ? 414 THR A OG1 1 ATOM 3307 C CG2 . THR A 1 414 ? 17.690 11.252 28.027 1.00 23.94 ? 414 THR A CG2 1 ATOM 3308 N N . SER A 1 415 ? 19.617 12.046 31.352 1.00 24.72 ? 415 SER A N 1 ATOM 3309 C CA . SER A 1 415 ? 19.051 12.453 32.642 1.00 25.03 ? 415 SER A CA 1 ATOM 3310 C C . SER A 1 415 ? 17.582 12.799 32.568 1.00 25.16 ? 415 SER A C 1 ATOM 3311 O O . SER A 1 415 ? 16.891 12.756 33.583 1.00 25.44 ? 415 SER A O 1 ATOM 3312 C CB . SER A 1 415 ? 19.794 13.646 33.205 1.00 24.55 ? 415 SER A CB 1 ATOM 3313 O OG . SER A 1 415 ? 21.017 13.232 33.760 1.00 26.53 ? 415 SER A OG 1 ATOM 3314 N N . GLU A 1 416 ? 17.118 13.161 31.373 1.00 25.54 ? 416 GLU A N 1 ATOM 3315 C CA . GLU A 1 416 ? 15.697 13.421 31.125 1.00 25.72 ? 416 GLU A CA 1 ATOM 3316 C C . GLU A 1 416 ? 14.830 12.214 31.516 1.00 25.15 ? 416 GLU A C 1 ATOM 3317 O O . GLU A 1 416 ? 13.751 12.376 32.082 1.00 25.40 ? 416 GLU A O 1 ATOM 3318 C CB . GLU A 1 416 ? 15.460 13.835 29.661 1.00 25.82 ? 416 GLU A CB 1 ATOM 3319 C CG . GLU A 1 416 ? 16.116 15.161 29.262 1.00 26.96 ? 416 GLU A CG 1 ATOM 3320 C CD . GLU A 1 416 ? 15.636 16.342 30.100 1.00 29.83 ? 416 GLU A CD 1 ATOM 3321 O OE1 . GLU A 1 416 ? 14.415 16.608 30.131 1.00 31.15 ? 416 GLU A OE1 1 ATOM 3322 O OE2 . GLU A 1 416 ? 16.481 17.020 30.730 1.00 32.11 ? 416 GLU A OE2 1 ATOM 3323 N N . LEU A 1 417 ? 15.322 11.015 31.236 1.00 24.75 ? 417 LEU A N 1 ATOM 3324 C CA . LEU A 1 417 ? 14.650 9.789 31.635 1.00 24.57 ? 417 LEU A CA 1 ATOM 3325 C C . LEU A 1 417 ? 15.175 9.266 32.964 1.00 24.88 ? 417 LEU A C 1 ATOM 3326 O O . LEU A 1 417 ? 14.451 8.614 33.716 1.00 24.49 ? 417 LEU A O 1 ATOM 3327 C CB . LEU A 1 417 ? 14.832 8.712 30.572 1.00 23.90 ? 417 LEU A CB 1 ATOM 3328 C CG . LEU A 1 417 ? 14.090 8.880 29.257 1.00 23.87 ? 417 LEU A CG 1 ATOM 3329 C CD1 . LEU A 1 417 ? 14.529 7.807 28.277 1.00 24.79 ? 417 LEU A CD1 1 ATOM 3330 C CD2 . LEU A 1 417 ? 12.598 8.800 29.476 1.00 24.76 ? 417 LEU A CD2 1 ATOM 3331 N N . ARG A 1 418 ? 16.442 9.543 33.248 1.00 25.63 ? 418 ARG A N 1 ATOM 3332 C CA . ARG A 1 418 ? 17.097 8.948 34.408 1.00 26.02 ? 418 ARG A CA 1 ATOM 3333 C C . ARG A 1 418 ? 16.839 9.687 35.719 1.00 26.47 ? 418 ARG A C 1 ATOM 3334 O O . ARG A 1 418 ? 16.979 9.109 36.795 1.00 26.45 ? 418 ARG A O 1 ATOM 3335 C CB . ARG A 1 418 ? 18.595 8.772 34.166 1.00 25.87 ? 418 ARG A CB 1 ATOM 3336 C CG . ARG A 1 418 ? 19.177 7.641 34.987 1.00 26.42 ? 418 ARG A CG 1 ATOM 3337 C CD . ARG A 1 418 ? 20.673 7.637 34.903 1.00 28.69 ? 418 ARG A CD 1 ATOM 3338 N NE . ARG A 1 418 ? 21.305 8.708 35.685 1.00 29.29 ? 418 ARG A NE 1 ATOM 3339 C CZ . ARG A 1 418 ? 21.518 8.664 36.996 1.00 30.06 ? 418 ARG A CZ 1 ATOM 3340 N NH1 . ARG A 1 418 ? 21.125 7.619 37.705 1.00 30.91 ? 418 ARG A NH1 1 ATOM 3341 N NH2 . ARG A 1 418 ? 22.116 9.680 37.604 1.00 32.42 ? 418 ARG A NH2 1 ATOM 3342 N N . ASN A 1 419 ? 16.458 10.955 35.637 1.00 27.12 ? 419 ASN A N 1 ATOM 3343 C CA . ASN A 1 419 ? 16.230 11.748 36.850 1.00 28.16 ? 419 ASN A CA 1 ATOM 3344 C C . ASN A 1 419 ? 14.862 12.412 36.877 1.00 29.10 ? 419 ASN A C 1 ATOM 3345 O O . ASN A 1 419 ? 14.346 12.699 37.957 1.00 29.24 ? 419 ASN A O 1 ATOM 3346 C CB . ASN A 1 419 ? 17.309 12.839 37.032 1.00 27.82 ? 419 ASN A CB 1 ATOM 3347 C CG . ASN A 1 419 ? 18.630 12.297 37.553 1.00 26.77 ? 419 ASN A CG 1 ATOM 3348 O OD1 . ASN A 1 419 ? 18.668 11.458 38.436 1.00 27.07 ? 419 ASN A OD1 1 ATOM 3349 N ND2 . ASN A 1 419 ? 19.725 12.807 37.014 1.00 26.72 ? 419 ASN A ND2 1 ATOM 3350 N N . LYS A 1 420 ? 14.283 12.674 35.703 1.00 30.05 ? 420 LYS A N 1 ATOM 3351 C CA . LYS A 1 420 ? 13.081 13.517 35.636 1.00 31.00 ? 420 LYS A CA 1 ATOM 3352 C C . LYS A 1 420 ? 11.839 12.855 35.016 1.00 31.02 ? 420 LYS A C 1 ATOM 3353 O O . LYS A 1 420 ? 10.947 13.544 34.511 1.00 30.75 ? 420 LYS A O 1 ATOM 3354 C CB . LYS A 1 420 ? 13.393 14.839 34.914 1.00 31.50 ? 420 LYS A CB 1 ATOM 3355 C CG . LYS A 1 420 ? 14.764 15.448 35.208 1.00 33.61 ? 420 LYS A CG 1 ATOM 3356 C CD . LYS A 1 420 ? 14.635 16.932 35.540 1.00 37.07 ? 420 LYS A CD 1 ATOM 3357 C CE . LYS A 1 420 ? 15.918 17.695 35.258 1.00 38.17 ? 420 LYS A CE 1 ATOM 3358 N NZ . LYS A 1 420 ? 15.978 18.034 33.800 1.00 40.93 ? 420 LYS A NZ 1 ATOM 3359 N N . LEU A 1 421 ? 11.777 11.524 35.060 1.00 31.56 ? 421 LEU A N 1 ATOM 3360 C CA . LEU A 1 421 ? 10.638 10.792 34.494 1.00 31.51 ? 421 LEU A CA 1 ATOM 3361 C C . LEU A 1 421 ? 9.380 11.020 35.322 1.00 32.09 ? 421 LEU A C 1 ATOM 3362 O O . LEU A 1 421 ? 9.409 10.969 36.555 1.00 31.76 ? 421 LEU A O 1 ATOM 3363 C CB . LEU A 1 421 ? 10.935 9.295 34.345 1.00 31.05 ? 421 LEU A CB 1 ATOM 3364 C CG . LEU A 1 421 ? 9.859 8.415 33.689 1.00 30.33 ? 421 LEU A CG 1 ATOM 3365 C CD1 . LEU A 1 421 ? 9.887 8.501 32.166 1.00 29.88 ? 421 LEU A CD1 1 ATOM 3366 C CD2 . LEU A 1 421 ? 10.025 6.980 34.137 1.00 28.73 ? 421 LEU A CD2 1 ATOM 3367 N N . PHE A 1 422 ? 8.282 11.284 34.622 1.00 32.93 ? 422 PHE A N 1 ATOM 3368 C CA . PHE A 1 422 ? 6.993 11.481 35.249 1.00 33.94 ? 422 PHE A CA 1 ATOM 3369 C C . PHE A 1 422 ? 6.166 10.195 35.130 1.00 34.97 ? 422 PHE A C 1 ATOM 3370 O O . PHE A 1 422 ? 5.957 9.683 34.028 1.00 35.09 ? 422 PHE A O 1 ATOM 3371 C CB . PHE A 1 422 ? 6.286 12.663 34.577 1.00 33.66 ? 422 PHE A CB 1 ATOM 3372 C CG . PHE A 1 422 ? 4.949 13.000 35.178 1.00 33.41 ? 422 PHE A CG 1 ATOM 3373 C CD1 . PHE A 1 422 ? 4.857 13.890 36.250 1.00 33.68 ? 422 PHE A CD1 1 ATOM 3374 C CD2 . PHE A 1 422 ? 3.784 12.436 34.673 1.00 32.54 ? 422 PHE A CD2 1 ATOM 3375 C CE1 . PHE A 1 422 ? 3.627 14.202 36.809 1.00 32.87 ? 422 PHE A CE1 1 ATOM 3376 C CE2 . PHE A 1 422 ? 2.553 12.739 35.226 1.00 32.52 ? 422 PHE A CE2 1 ATOM 3377 C CZ . PHE A 1 422 ? 2.471 13.625 36.291 1.00 33.12 ? 422 PHE A CZ 1 ATOM 3378 N N . GLN A 1 423 ? 5.720 9.672 36.267 1.00 36.54 ? 423 GLN A N 1 ATOM 3379 C CA . GLN A 1 423 ? 4.850 8.489 36.313 1.00 38.15 ? 423 GLN A CA 1 ATOM 3380 C C . GLN A 1 423 ? 3.405 8.927 36.499 1.00 39.44 ? 423 GLN A C 1 ATOM 3381 O O . GLN A 1 423 ? 3.123 9.669 37.438 1.00 39.55 ? 423 GLN A O 1 ATOM 3382 C CB . GLN A 1 423 ? 5.253 7.562 37.462 1.00 37.95 ? 423 GLN A CB 1 ATOM 3383 C CG . GLN A 1 423 ? 6.587 6.854 37.261 1.00 37.80 ? 423 GLN A CG 1 ATOM 3384 C CD . GLN A 1 423 ? 6.466 5.485 36.616 1.00 37.39 ? 423 GLN A CD 1 ATOM 3385 O OE1 . GLN A 1 423 ? 6.875 4.484 37.204 1.00 37.81 ? 423 GLN A OE1 1 ATOM 3386 N NE2 . GLN A 1 423 ? 5.904 5.431 35.409 1.00 37.17 ? 423 GLN A NE2 1 ATOM 3387 N N . PRO A 1 424 ? 2.484 8.435 35.636 1.00 40.91 ? 424 PRO A N 1 ATOM 3388 C CA . PRO A 1 424 ? 1.085 8.895 35.529 1.00 42.36 ? 424 PRO A CA 1 ATOM 3389 C C . PRO A 1 424 ? 0.290 8.850 36.833 1.00 43.65 ? 424 PRO A C 1 ATOM 3390 O O . PRO A 1 424 ? -0.731 9.533 36.959 1.00 44.33 ? 424 PRO A O 1 ATOM 3391 C CB . PRO A 1 424 ? 0.466 7.911 34.523 1.00 42.34 ? 424 PRO A CB 1 ATOM 3392 C CG . PRO A 1 424 ? 1.386 6.711 34.543 1.00 41.54 ? 424 PRO A CG 1 ATOM 3393 C CD . PRO A 1 424 ? 2.741 7.323 34.704 1.00 40.90 ? 424 PRO A CD 1 ATOM 3394 N N . THR A 1 425 ? 0.763 8.057 37.789 1.00 45.10 ? 425 THR A N 1 ATOM 3395 C CA . THR A 1 425 ? 0.112 7.885 39.085 1.00 46.32 ? 425 THR A CA 1 ATOM 3396 C C . THR A 1 425 ? 0.565 8.942 40.087 1.00 46.67 ? 425 THR A C 1 ATOM 3397 O O . THR A 1 425 ? -0.257 9.619 40.716 1.00 47.45 ? 425 THR A O 1 ATOM 3398 C CB . THR A 1 425 ? 0.436 6.495 39.630 1.00 46.68 ? 425 THR A CB 1 ATOM 3399 O OG1 . THR A 1 425 ? -0.179 5.514 38.784 1.00 47.28 ? 425 THR A OG1 1 ATOM 3400 C CG2 . THR A 1 425 ? -0.056 6.331 41.079 1.00 47.95 ? 425 THR A CG2 1 ATOM 3401 N N . HIS A 1 426 ? 1.883 9.079 40.209 1.00 46.86 ? 426 HIS A N 1 ATOM 3402 C CA . HIS A 1 426 ? 2.515 9.968 41.179 1.00 46.84 ? 426 HIS A CA 1 ATOM 3403 C C . HIS A 1 426 ? 2.694 11.366 40.594 1.00 46.54 ? 426 HIS A C 1 ATOM 3404 O O . HIS A 1 426 ? 2.317 11.596 39.445 1.00 46.70 ? 426 HIS A O 1 ATOM 3405 C CB . HIS A 1 426 ? 3.831 9.335 41.628 1.00 46.93 ? 426 HIS A CB 1 ATOM 3406 C CG . HIS A 1 426 ? 3.707 7.861 41.869 1.00 47.16 ? 426 HIS A CG 1 ATOM 3407 N ND1 . HIS A 1 426 ? 3.141 7.340 43.015 1.00 47.62 ? 426 HIS A ND1 1 ATOM 3408 C CD2 . HIS A 1 426 ? 4.016 6.800 41.086 1.00 47.84 ? 426 HIS A CD2 1 ATOM 3409 C CE1 . HIS A 1 426 ? 3.136 6.020 42.941 1.00 48.65 ? 426 HIS A CE1 1 ATOM 3410 N NE2 . HIS A 1 426 ? 3.664 5.666 41.781 1.00 49.02 ? 426 HIS A NE2 1 ATOM 3411 N N . LYS A 1 427 ? 3.249 12.298 41.367 1.00 46.02 ? 427 LYS A N 1 ATOM 3412 C CA . LYS A 1 427 ? 3.115 13.724 41.016 1.00 45.83 ? 427 LYS A CA 1 ATOM 3413 C C . LYS A 1 427 ? 4.357 14.488 40.527 1.00 44.79 ? 427 LYS A C 1 ATOM 3414 O O . LYS A 1 427 ? 4.209 15.482 39.819 1.00 44.60 ? 427 LYS A O 1 ATOM 3415 C CB . LYS A 1 427 ? 2.417 14.490 42.143 1.00 46.23 ? 427 LYS A CB 1 ATOM 3416 C CG . LYS A 1 427 ? 0.895 14.403 42.066 1.00 48.65 ? 427 LYS A CG 1 ATOM 3417 C CD . LYS A 1 427 ? 0.203 14.626 43.420 1.00 52.19 ? 427 LYS A CD 1 ATOM 3418 C CE . LYS A 1 427 ? 0.441 13.441 44.358 1.00 54.44 ? 427 LYS A CE 1 ATOM 3419 N NZ . LYS A 1 427 ? -0.830 12.930 44.953 1.00 55.78 ? 427 LYS A NZ 1 ATOM 3420 N N . ILE A 1 428 ? 5.556 14.039 40.899 1.00 43.54 ? 428 ILE A N 1 ATOM 3421 C CA . ILE A 1 428 ? 6.799 14.727 40.512 1.00 42.39 ? 428 ILE A CA 1 ATOM 3422 C C . ILE A 1 428 ? 7.402 14.241 39.193 1.00 41.12 ? 428 ILE A C 1 ATOM 3423 O O . ILE A 1 428 ? 7.163 13.112 38.762 1.00 41.31 ? 428 ILE A O 1 ATOM 3424 C CB . ILE A 1 428 ? 7.921 14.623 41.593 1.00 42.62 ? 428 ILE A CB 1 ATOM 3425 C CG1 . ILE A 1 428 ? 7.889 13.253 42.303 1.00 43.64 ? 428 ILE A CG1 1 ATOM 3426 C CG2 . ILE A 1 428 ? 7.851 15.809 42.570 1.00 42.52 ? 428 ILE A CG2 1 ATOM 3427 C CD1 . ILE A 1 428 ? 6.991 13.194 43.569 1.00 47.31 ? 428 ILE A CD1 1 ATOM 3428 N N . HIS A 1 429 ? 8.187 15.113 38.570 1.00 39.29 ? 429 HIS A N 1 ATOM 3429 C CA . HIS A 1 429 ? 9.082 14.735 37.486 1.00 37.70 ? 429 HIS A CA 1 ATOM 3430 C C . HIS A 1 429 ? 10.415 14.321 38.117 1.00 36.58 ? 429 HIS A C 1 ATOM 3431 O O . HIS A 1 429 ? 11.414 15.051 38.045 1.00 36.63 ? 429 HIS A O 1 ATOM 3432 C CB . HIS A 1 429 ? 9.283 15.909 36.524 1.00 37.66 ? 429 HIS A CB 1 ATOM 3433 C CG . HIS A 1 429 ? 8.068 16.240 35.717 1.00 37.99 ? 429 HIS A CG 1 ATOM 3434 N ND1 . HIS A 1 429 ? 6.923 16.760 36.276 1.00 38.51 ? 429 HIS A ND1 1 ATOM 3435 C CD2 . HIS A 1 429 ? 7.819 16.120 34.390 1.00 38.29 ? 429 HIS A CD2 1 ATOM 3436 C CE1 . HIS A 1 429 ? 6.017 16.938 35.331 1.00 38.99 ? 429 HIS A CE1 1 ATOM 3437 N NE2 . HIS A 1 429 ? 6.532 16.551 34.178 1.00 37.58 ? 429 HIS A NE2 1 ATOM 3438 N N . GLY A 1 430 ? 10.428 13.152 38.750 1.00 34.66 ? 430 GLY A N 1 ATOM 3439 C CA . GLY A 1 430 ? 11.590 12.758 39.517 1.00 32.64 ? 430 GLY A CA 1 ATOM 3440 C C . GLY A 1 430 ? 11.909 11.284 39.570 1.00 31.30 ? 430 GLY A C 1 ATOM 3441 O O . GLY A 1 430 ? 12.699 10.853 40.417 1.00 31.32 ? 430 GLY A O 1 ATOM 3442 N N . PHE A 1 431 ? 11.305 10.515 38.671 1.00 29.90 ? 431 PHE A N 1 ATOM 3443 C CA . PHE A 1 431 ? 11.564 9.078 38.584 1.00 28.97 ? 431 PHE A CA 1 ATOM 3444 C C . PHE A 1 431 ? 12.791 8.769 37.733 1.00 28.18 ? 431 PHE A C 1 ATOM 3445 O O . PHE A 1 431 ? 13.332 9.662 37.068 1.00 28.03 ? 431 PHE A O 1 ATOM 3446 C CB . PHE A 1 431 ? 10.332 8.331 38.062 1.00 28.76 ? 431 PHE A CB 1 ATOM 3447 C CG . PHE A 1 431 ? 9.282 8.102 39.110 1.00 28.42 ? 431 PHE A CG 1 ATOM 3448 C CD1 . PHE A 1 431 ? 8.255 9.024 39.300 1.00 27.93 ? 431 PHE A CD1 1 ATOM 3449 C CD2 . PHE A 1 431 ? 9.317 6.958 39.914 1.00 27.20 ? 431 PHE A CD2 1 ATOM 3450 C CE1 . PHE A 1 431 ? 7.289 8.815 40.276 1.00 26.63 ? 431 PHE A CE1 1 ATOM 3451 C CE2 . PHE A 1 431 ? 8.348 6.738 40.880 1.00 25.78 ? 431 PHE A CE2 1 ATOM 3452 C CZ . PHE A 1 431 ? 7.341 7.668 41.063 1.00 26.43 ? 431 PHE A CZ 1 ATOM 3453 N N . ASP A 1 432 ? 13.221 7.507 37.777 1.00 26.95 ? 432 ASP A N 1 ATOM 3454 C CA . ASP A 1 432 ? 14.384 7.022 37.027 1.00 26.28 ? 432 ASP A CA 1 ATOM 3455 C C . ASP A 1 432 ? 14.036 5.763 36.237 1.00 26.30 ? 432 ASP A C 1 ATOM 3456 O O . ASP A 1 432 ? 13.884 4.678 36.806 1.00 26.06 ? 432 ASP A O 1 ATOM 3457 C CB . ASP A 1 432 ? 15.559 6.740 37.977 1.00 25.79 ? 432 ASP A CB 1 ATOM 3458 C CG . ASP A 1 432 ? 16.747 6.074 37.287 1.00 25.09 ? 432 ASP A CG 1 ATOM 3459 O OD1 . ASP A 1 432 ? 16.683 5.724 36.096 1.00 24.66 ? 432 ASP A OD1 1 ATOM 3460 O OD2 . ASP A 1 432 ? 17.775 5.893 37.957 1.00 25.74 ? 432 ASP A OD2 1 ATOM 3461 N N . LEU A 1 433 ? 13.935 5.913 34.918 1.00 26.31 ? 433 LEU A N 1 ATOM 3462 C CA . LEU A 1 433 ? 13.641 4.783 34.041 1.00 25.82 ? 433 LEU A CA 1 ATOM 3463 C C . LEU A 1 433 ? 14.667 3.639 34.152 1.00 25.20 ? 433 LEU A C 1 ATOM 3464 O O . LEU A 1 433 ? 14.286 2.463 34.170 1.00 25.20 ? 433 LEU A O 1 ATOM 3465 C CB . LEU A 1 433 ? 13.473 5.249 32.589 1.00 26.06 ? 433 LEU A CB 1 ATOM 3466 C CG . LEU A 1 433 ? 13.061 4.195 31.555 1.00 26.87 ? 433 LEU A CG 1 ATOM 3467 C CD1 . LEU A 1 433 ? 11.892 3.381 32.061 1.00 29.13 ? 433 LEU A CD1 1 ATOM 3468 C CD2 . LEU A 1 433 ? 12.704 4.853 30.239 1.00 27.19 ? 433 LEU A CD2 1 ATOM 3469 N N . ALA A 1 434 ? 15.951 3.977 34.243 1.00 24.29 ? 434 ALA A N 1 ATOM 3470 C CA . ALA A 1 434 ? 17.003 2.952 34.304 1.00 23.81 ? 434 ALA A CA 1 ATOM 3471 C C . ALA A 1 434 ? 16.878 2.064 35.540 1.00 23.75 ? 434 ALA A C 1 ATOM 3472 O O . ALA A 1 434 ? 16.905 0.842 35.418 1.00 23.29 ? 434 ALA A O 1 ATOM 3473 C CB . ALA A 1 434 ? 18.401 3.571 34.214 1.00 22.79 ? 434 ALA A CB 1 ATOM 3474 N N . ALA A 1 435 ? 16.745 2.687 36.718 1.00 23.56 ? 435 ALA A N 1 ATOM 3475 C CA . ALA A 1 435 ? 16.602 1.962 37.977 1.00 23.37 ? 435 ALA A CA 1 ATOM 3476 C C . ALA A 1 435 ? 15.342 1.092 37.963 1.00 23.79 ? 435 ALA A C 1 ATOM 3477 O O . ALA A 1 435 ? 15.373 -0.056 38.433 1.00 23.89 ? 435 ALA A O 1 ATOM 3478 C CB . ALA A 1 435 ? 16.556 2.923 39.135 1.00 22.99 ? 435 ALA A CB 1 ATOM 3479 N N . ILE A 1 436 ? 14.249 1.654 37.427 1.00 23.60 ? 436 ILE A N 1 ATOM 3480 C CA . ILE A 1 436 ? 12.982 0.963 37.280 1.00 23.87 ? 436 ILE A CA 1 ATOM 3481 C C . ILE A 1 436 ? 13.135 -0.281 36.408 1.00 24.14 ? 436 ILE A C 1 ATOM 3482 O O . ILE A 1 436 ? 12.715 -1.367 36.819 1.00 24.19 ? 436 ILE A O 1 ATOM 3483 C CB . ILE A 1 436 ? 11.861 1.874 36.690 1.00 24.26 ? 436 ILE A CB 1 ATOM 3484 C CG1 . ILE A 1 436 ? 11.306 2.817 37.757 1.00 24.01 ? 436 ILE A CG1 1 ATOM 3485 C CG2 . ILE A 1 436 ? 10.704 1.019 36.097 1.00 23.93 ? 436 ILE A CG2 1 ATOM 3486 C CD1 . ILE A 1 436 ? 10.529 3.984 37.183 1.00 24.97 ? 436 ILE A CD1 1 ATOM 3487 N N . ASN A 1 437 ? 13.725 -0.128 35.219 1.00 23.83 ? 437 ASN A N 1 ATOM 3488 C CA . ASN A 1 437 ? 13.998 -1.272 34.368 1.00 23.70 ? 437 ASN A CA 1 ATOM 3489 C C . ASN A 1 437 ? 14.709 -2.356 35.144 1.00 23.85 ? 437 ASN A C 1 ATOM 3490 O O . ASN A 1 437 ? 14.407 -3.531 34.969 1.00 24.86 ? 437 ASN A O 1 ATOM 3491 C CB . ASN A 1 437 ? 14.876 -0.901 33.180 1.00 24.08 ? 437 ASN A CB 1 ATOM 3492 C CG . ASN A 1 437 ? 14.149 -0.091 32.121 1.00 24.87 ? 437 ASN A CG 1 ATOM 3493 O OD1 . ASN A 1 437 ? 12.925 -0.170 31.950 1.00 23.44 ? 437 ASN A OD1 1 ATOM 3494 N ND2 . ASN A 1 437 ? 14.926 0.695 31.387 1.00 25.50 ? 437 ASN A ND2 1 ATOM 3495 N N . LEU A 1 438 ? 15.658 -1.974 35.993 1.00 23.60 ? 438 LEU A N 1 ATOM 3496 C CA . LEU A 1 438 ? 16.458 -2.951 36.723 1.00 23.56 ? 438 LEU A CA 1 ATOM 3497 C C . LEU A 1 438 ? 15.657 -3.633 37.805 1.00 23.46 ? 438 LEU A C 1 ATOM 3498 O O . LEU A 1 438 ? 15.736 -4.849 37.970 1.00 23.11 ? 438 LEU A O 1 ATOM 3499 C CB . LEU A 1 438 ? 17.700 -2.314 37.332 1.00 23.51 ? 438 LEU A CB 1 ATOM 3500 C CG . LEU A 1 438 ? 18.860 -2.023 36.389 1.00 23.84 ? 438 LEU A CG 1 ATOM 3501 C CD1 . LEU A 1 438 ? 19.910 -1.271 37.177 1.00 23.54 ? 438 LEU A CD1 1 ATOM 3502 C CD2 . LEU A 1 438 ? 19.448 -3.290 35.744 1.00 23.86 ? 438 LEU A CD2 1 ATOM 3503 N N . GLN A 1 439 ? 14.902 -2.831 38.551 1.00 23.54 ? 439 GLN A N 1 ATOM 3504 C CA . GLN A 1 439 ? 13.968 -3.342 39.539 1.00 23.51 ? 439 GLN A CA 1 ATOM 3505 C C . GLN A 1 439 ? 12.973 -4.301 38.864 1.00 23.19 ? 439 GLN A C 1 ATOM 3506 O O . GLN A 1 439 ? 12.655 -5.344 39.419 1.00 23.42 ? 439 GLN A O 1 ATOM 3507 C CB . GLN A 1 439 ? 13.244 -2.183 40.235 1.00 23.70 ? 439 GLN A CB 1 ATOM 3508 C CG . GLN A 1 439 ? 12.563 -2.524 41.564 1.00 24.47 ? 439 GLN A CG 1 ATOM 3509 C CD . GLN A 1 439 ? 13.533 -2.554 42.747 1.00 26.77 ? 439 GLN A CD 1 ATOM 3510 O OE1 . GLN A 1 439 ? 14.746 -2.647 42.568 1.00 27.34 ? 439 GLN A OE1 1 ATOM 3511 N NE2 . GLN A 1 439 ? 12.992 -2.491 43.965 1.00 27.46 ? 439 GLN A NE2 1 ATOM 3512 N N . ARG A 1 440 ? 12.533 -3.963 37.655 1.00 22.62 ? 440 ARG A N 1 ATOM 3513 C CA . ARG A 1 440 ? 11.564 -4.767 36.928 1.00 22.85 ? 440 ARG A CA 1 ATOM 3514 C C . ARG A 1 440 ? 12.110 -6.124 36.472 1.00 23.69 ? 440 ARG A C 1 ATOM 3515 O O . ARG A 1 440 ? 11.373 -7.103 36.474 1.00 24.03 ? 440 ARG A O 1 ATOM 3516 C CB . ARG A 1 440 ? 10.966 -3.990 35.755 1.00 22.22 ? 440 ARG A CB 1 ATOM 3517 C CG . ARG A 1 440 ? 9.744 -4.637 35.133 1.00 21.45 ? 440 ARG A CG 1 ATOM 3518 C CD . ARG A 1 440 ? 8.501 -4.499 35.998 1.00 20.81 ? 440 ARG A CD 1 ATOM 3519 N NE . ARG A 1 440 ? 8.047 -3.122 36.118 1.00 19.29 ? 440 ARG A NE 1 ATOM 3520 C CZ . ARG A 1 440 ? 7.208 -2.700 37.059 1.00 22.16 ? 440 ARG A CZ 1 ATOM 3521 N NH1 . ARG A 1 440 ? 6.735 -3.550 37.980 1.00 21.21 ? 440 ARG A NH1 1 ATOM 3522 N NH2 . ARG A 1 440 ? 6.858 -1.420 37.105 1.00 21.41 ? 440 ARG A NH2 1 ATOM 3523 N N . CYS A 1 441 ? 13.383 -6.175 36.080 1.00 24.41 ? 441 CYS A N 1 ATOM 3524 C CA . CYS A 1 441 ? 14.080 -7.442 35.833 1.00 25.49 ? 441 CYS A CA 1 ATOM 3525 C C . CYS A 1 441 ? 13.925 -8.382 37.015 1.00 24.68 ? 441 CYS A C 1 ATOM 3526 O O . CYS A 1 441 ? 13.598 -9.544 36.863 1.00 25.01 ? 441 CYS A O 1 ATOM 3527 C CB . CYS A 1 441 ? 15.590 -7.219 35.639 1.00 25.89 ? 441 CYS A CB 1 ATOM 3528 S SG . CYS A 1 441 ? 16.117 -6.779 33.997 1.00 30.53 ? 441 CYS A SG 1 ATOM 3529 N N . ARG A 1 442 ? 14.206 -7.866 38.196 1.00 24.50 ? 442 ARG A N 1 ATOM 3530 C CA . ARG A 1 442 ? 14.123 -8.637 39.406 1.00 24.51 ? 442 ARG A CA 1 ATOM 3531 C C . ARG A 1 442 ? 12.671 -9.051 39.686 1.00 24.56 ? 442 ARG A C 1 ATOM 3532 O O . ARG A 1 442 ? 12.408 -10.211 39.961 1.00 24.54 ? 442 ARG A O 1 ATOM 3533 C CB . ARG A 1 442 ? 14.782 -7.851 40.540 1.00 24.48 ? 442 ARG A CB 1 ATOM 3534 C CG . ARG A 1 442 ? 16.283 -7.658 40.282 1.00 24.57 ? 442 ARG A CG 1 ATOM 3535 C CD . ARG A 1 442 ? 16.868 -6.474 41.004 1.00 24.86 ? 442 ARG A CD 1 ATOM 3536 N NE . ARG A 1 442 ? 18.276 -6.291 40.666 1.00 25.20 ? 442 ARG A NE 1 ATOM 3537 C CZ . ARG A 1 442 ? 19.107 -5.466 41.301 1.00 26.41 ? 442 ARG A CZ 1 ATOM 3538 N NH1 . ARG A 1 442 ? 18.683 -4.740 42.323 1.00 26.37 ? 442 ARG A NH1 1 ATOM 3539 N NH2 . ARG A 1 442 ? 20.376 -5.375 40.928 1.00 27.54 ? 442 ARG A NH2 1 ATOM 3540 N N . ASP A 1 443 ? 11.741 -8.102 39.549 1.00 24.65 ? 443 ASP A N 1 ATOM 3541 C CA . ASP A 1 443 ? 10.292 -8.338 39.665 1.00 24.60 ? 443 ASP A CA 1 ATOM 3542 C C . ASP A 1 443 ? 9.833 -9.507 38.761 1.00 24.45 ? 443 ASP A C 1 ATOM 3543 O O . ASP A 1 443 ? 9.080 -10.374 39.194 1.00 24.66 ? 443 ASP A O 1 ATOM 3544 C CB . ASP A 1 443 ? 9.535 -7.028 39.334 1.00 24.23 ? 443 ASP A CB 1 ATOM 3545 C CG . ASP A 1 443 ? 7.998 -7.138 39.518 1.00 25.41 ? 443 ASP A CG 1 ATOM 3546 O OD1 . ASP A 1 443 ? 7.511 -8.069 40.205 1.00 24.81 ? 443 ASP A OD1 1 ATOM 3547 O OD2 . ASP A 1 443 ? 7.271 -6.259 38.976 1.00 25.31 ? 443 ASP A OD2 1 ATOM 3548 N N . HIS A 1 444 ? 10.306 -9.537 37.520 1.00 23.82 ? 444 HIS A N 1 ATOM 3549 C CA . HIS A 1 444 ? 9.898 -10.562 36.569 1.00 23.91 ? 444 HIS A CA 1 ATOM 3550 C C . HIS A 1 444 ? 10.644 -11.895 36.719 1.00 24.38 ? 444 HIS A C 1 ATOM 3551 O O . HIS A 1 444 ? 10.359 -12.848 36.004 1.00 24.29 ? 444 HIS A O 1 ATOM 3552 C CB . HIS A 1 444 ? 10.030 -10.033 35.143 1.00 23.86 ? 444 HIS A CB 1 ATOM 3553 C CG . HIS A 1 444 ? 8.893 -9.153 34.717 1.00 23.17 ? 444 HIS A CG 1 ATOM 3554 N ND1 . HIS A 1 444 ? 8.108 -9.434 33.621 1.00 22.71 ? 444 HIS A ND1 1 ATOM 3555 C CD2 . HIS A 1 444 ? 8.397 -8.013 35.251 1.00 21.91 ? 444 HIS A CD2 1 ATOM 3556 C CE1 . HIS A 1 444 ? 7.192 -8.492 33.483 1.00 21.84 ? 444 HIS A CE1 1 ATOM 3557 N NE2 . HIS A 1 444 ? 7.346 -7.619 34.461 1.00 22.49 ? 444 HIS A NE2 1 ATOM 3558 N N . GLY A 1 445 ? 11.591 -11.953 37.656 1.00 24.75 ? 445 GLY A N 1 ATOM 3559 C CA . GLY A 1 445 ? 12.306 -13.188 37.962 1.00 24.62 ? 445 GLY A CA 1 ATOM 3560 C C . GLY A 1 445 ? 13.267 -13.621 36.873 1.00 24.49 ? 445 GLY A C 1 ATOM 3561 O O . GLY A 1 445 ? 13.314 -14.788 36.507 1.00 25.32 ? 445 GLY A O 1 ATOM 3562 N N . MET A 1 446 ? 14.056 -12.685 36.376 1.00 24.34 ? 446 MET A N 1 ATOM 3563 C CA . MET A 1 446 ? 14.936 -12.942 35.237 1.00 24.31 ? 446 MET A CA 1 ATOM 3564 C C . MET A 1 446 ? 16.226 -13.685 35.585 1.00 24.30 ? 446 MET A C 1 ATOM 3565 O O . MET A 1 446 ? 16.948 -13.314 36.532 1.00 23.77 ? 446 MET A O 1 ATOM 3566 C CB . MET A 1 446 ? 15.285 -11.629 34.533 1.00 24.29 ? 446 MET A CB 1 ATOM 3567 C CG . MET A 1 446 ? 14.127 -11.020 33.743 1.00 25.60 ? 446 MET A CG 1 ATOM 3568 S SD . MET A 1 446 ? 13.817 -11.912 32.214 1.00 28.20 ? 446 MET A SD 1 ATOM 3569 C CE . MET A 1 446 ? 12.431 -12.959 32.643 1.00 27.86 ? 446 MET A CE 1 ATOM 3570 N N . PRO A 1 447 ? 16.541 -14.737 34.806 1.00 24.03 ? 447 PRO A N 1 ATOM 3571 C CA . PRO A 1 447 ? 17.884 -15.289 34.916 1.00 23.73 ? 447 PRO A CA 1 ATOM 3572 C C . PRO A 1 447 ? 18.927 -14.188 34.666 1.00 24.05 ? 447 PRO A C 1 ATOM 3573 O O . PRO A 1 447 ? 18.650 -13.205 33.967 1.00 23.88 ? 447 PRO A O 1 ATOM 3574 C CB . PRO A 1 447 ? 17.918 -16.337 33.807 1.00 23.33 ? 447 PRO A CB 1 ATOM 3575 C CG . PRO A 1 447 ? 16.488 -16.723 33.614 1.00 23.54 ? 447 PRO A CG 1 ATOM 3576 C CD . PRO A 1 447 ? 15.712 -15.470 33.834 1.00 23.53 ? 447 PRO A CD 1 ATOM 3577 N N . GLY A 1 448 ? 20.115 -14.354 35.236 1.00 24.60 ? 448 GLY A N 1 ATOM 3578 C CA . GLY A 1 448 ? 21.204 -13.400 35.046 1.00 24.54 ? 448 GLY A CA 1 ATOM 3579 C C . GLY A 1 448 ? 21.835 -13.435 33.672 1.00 24.56 ? 448 GLY A C 1 ATOM 3580 O O . GLY A 1 448 ? 21.448 -14.215 32.813 1.00 24.97 ? 448 GLY A O 1 ATOM 3581 N N . TYR A 1 449 ? 22.828 -12.577 33.487 1.00 24.81 ? 449 TYR A N 1 ATOM 3582 C CA . TYR A 1 449 ? 23.488 -12.351 32.206 1.00 24.89 ? 449 TYR A CA 1 ATOM 3583 C C . TYR A 1 449 ? 24.128 -13.617 31.599 1.00 25.07 ? 449 TYR A C 1 ATOM 3584 O O . TYR A 1 449 ? 23.978 -13.873 30.406 1.00 25.20 ? 449 TYR A O 1 ATOM 3585 C CB . TYR A 1 449 ? 24.504 -11.199 32.380 1.00 24.85 ? 449 TYR A CB 1 ATOM 3586 C CG . TYR A 1 449 ? 25.383 -10.834 31.188 1.00 25.74 ? 449 TYR A CG 1 ATOM 3587 C CD1 . TYR A 1 449 ? 24.854 -10.171 30.072 1.00 26.36 ? 449 TYR A CD1 1 ATOM 3588 C CD2 . TYR A 1 449 ? 26.754 -11.103 31.202 1.00 24.31 ? 449 TYR A CD2 1 ATOM 3589 C CE1 . TYR A 1 449 ? 25.660 -9.819 28.995 1.00 25.95 ? 449 TYR A CE1 1 ATOM 3590 C CE2 . TYR A 1 449 ? 27.568 -10.744 30.130 1.00 24.95 ? 449 TYR A CE2 1 ATOM 3591 C CZ . TYR A 1 449 ? 27.012 -10.105 29.031 1.00 26.96 ? 449 TYR A CZ 1 ATOM 3592 O OH . TYR A 1 449 ? 27.810 -9.757 27.962 1.00 28.59 ? 449 TYR A OH 1 ATOM 3593 N N . ASN A 1 450 ? 24.829 -14.414 32.405 1.00 25.06 ? 450 ASN A N 1 ATOM 3594 C CA . ASN A 1 450 ? 25.506 -15.579 31.854 1.00 25.12 ? 450 ASN A CA 1 ATOM 3595 C C . ASN A 1 450 ? 24.546 -16.713 31.458 1.00 25.34 ? 450 ASN A C 1 ATOM 3596 O O . ASN A 1 450 ? 24.855 -17.519 30.569 1.00 25.29 ? 450 ASN A O 1 ATOM 3597 C CB . ASN A 1 450 ? 26.648 -16.055 32.767 1.00 25.28 ? 450 ASN A CB 1 ATOM 3598 C CG . ASN A 1 450 ? 27.945 -15.271 32.550 1.00 25.25 ? 450 ASN A CG 1 ATOM 3599 O OD1 . ASN A 1 450 ? 28.205 -14.743 31.460 1.00 26.58 ? 450 ASN A OD1 1 ATOM 3600 N ND2 . ASN A 1 450 ? 28.766 -15.196 33.592 1.00 23.61 ? 450 ASN A ND2 1 ATOM 3601 N N . SER A 1 451 ? 23.387 -16.764 32.109 1.00 25.11 ? 451 SER A N 1 ATOM 3602 C CA . SER A 1 451 ? 22.296 -17.647 31.685 1.00 25.31 ? 451 SER A CA 1 ATOM 3603 C C . SER A 1 451 ? 21.847 -17.363 30.248 1.00 25.25 ? 451 SER A C 1 ATOM 3604 O O . SER A 1 451 ? 21.615 -18.283 29.465 1.00 25.69 ? 451 SER A O 1 ATOM 3605 C CB . SER A 1 451 ? 21.100 -17.496 32.619 1.00 25.35 ? 451 SER A CB 1 ATOM 3606 O OG . SER A 1 451 ? 21.345 -18.114 33.862 1.00 26.13 ? 451 SER A OG 1 ATOM 3607 N N . TRP A 1 452 ? 21.714 -16.087 29.911 1.00 25.12 ? 452 TRP A N 1 ATOM 3608 C CA . TRP A 1 452 ? 21.312 -15.690 28.571 1.00 25.05 ? 452 TRP A CA 1 ATOM 3609 C C . TRP A 1 452 ? 22.471 -15.820 27.573 1.00 25.43 ? 452 TRP A C 1 ATOM 3610 O O . TRP A 1 452 ? 22.270 -16.271 26.438 1.00 25.84 ? 452 TRP A O 1 ATOM 3611 C CB . TRP A 1 452 ? 20.665 -14.299 28.597 1.00 24.98 ? 452 TRP A CB 1 ATOM 3612 C CG . TRP A 1 452 ? 19.375 -14.329 29.402 1.00 24.22 ? 452 TRP A CG 1 ATOM 3613 C CD1 . TRP A 1 452 ? 19.145 -13.773 30.645 1.00 22.35 ? 452 TRP A CD1 1 ATOM 3614 C CD2 . TRP A 1 452 ? 18.170 -15.014 29.040 1.00 22.27 ? 452 TRP A CD2 1 ATOM 3615 N NE1 . TRP A 1 452 ? 17.858 -14.053 31.053 1.00 21.37 ? 452 TRP A NE1 1 ATOM 3616 C CE2 . TRP A 1 452 ? 17.244 -14.818 30.092 1.00 22.33 ? 452 TRP A CE2 1 ATOM 3617 C CE3 . TRP A 1 452 ? 17.788 -15.785 27.929 1.00 23.08 ? 452 TRP A CE3 1 ATOM 3618 C CZ2 . TRP A 1 452 ? 15.947 -15.364 30.062 1.00 24.10 ? 452 TRP A CZ2 1 ATOM 3619 C CZ3 . TRP A 1 452 ? 16.496 -16.329 27.895 1.00 24.02 ? 452 TRP A CZ3 1 ATOM 3620 C CH2 . TRP A 1 452 ? 15.592 -16.113 28.959 1.00 24.15 ? 452 TRP A CH2 1 ATOM 3621 N N . ARG A 1 453 ? 23.686 -15.463 27.993 1.00 25.10 ? 453 ARG A N 1 ATOM 3622 C CA . ARG A 1 453 ? 24.854 -15.738 27.158 1.00 25.00 ? 453 ARG A CA 1 ATOM 3623 C C . ARG A 1 453 ? 24.885 -17.236 26.799 1.00 24.56 ? 453 ARG A C 1 ATOM 3624 O O . ARG A 1 453 ? 24.991 -17.592 25.628 1.00 24.46 ? 453 ARG A O 1 ATOM 3625 C CB . ARG A 1 453 ? 26.166 -15.298 27.833 1.00 25.17 ? 453 ARG A CB 1 ATOM 3626 C CG . ARG A 1 453 ? 26.340 -13.798 28.032 1.00 25.27 ? 453 ARG A CG 1 ATOM 3627 C CD . ARG A 1 453 ? 26.836 -13.093 26.784 1.00 26.58 ? 453 ARG A CD 1 ATOM 3628 N NE . ARG A 1 453 ? 28.171 -13.538 26.370 1.00 26.66 ? 453 ARG A NE 1 ATOM 3629 C CZ . ARG A 1 453 ? 28.887 -12.964 25.401 1.00 25.61 ? 453 ARG A CZ 1 ATOM 3630 N NH1 . ARG A 1 453 ? 28.423 -11.911 24.747 1.00 26.55 ? 453 ARG A NH1 1 ATOM 3631 N NH2 . ARG A 1 453 ? 30.074 -13.436 25.087 1.00 26.78 ? 453 ARG A NH2 1 ATOM 3632 N N . GLY A 1 454 ? 24.771 -18.096 27.805 1.00 24.14 ? 454 GLY A N 1 ATOM 3633 C CA . GLY A 1 454 ? 24.687 -19.532 27.585 1.00 24.62 ? 454 GLY A CA 1 ATOM 3634 C C . GLY A 1 454 ? 23.574 -19.901 26.614 1.00 25.38 ? 454 GLY A C 1 ATOM 3635 O O . GLY A 1 454 ? 23.821 -20.606 25.647 1.00 25.50 ? 454 GLY A O 1 ATOM 3636 N N . PHE A 1 455 ? 22.365 -19.391 26.857 1.00 25.59 ? 455 PHE A N 1 ATOM 3637 C CA . PHE A 1 455 ? 21.196 -19.604 25.992 1.00 26.24 ? 455 PHE A CA 1 ATOM 3638 C C . PHE A 1 455 ? 21.443 -19.290 24.508 1.00 26.72 ? 455 PHE A C 1 ATOM 3639 O O . PHE A 1 455 ? 20.908 -19.962 23.616 1.00 27.13 ? 455 PHE A O 1 ATOM 3640 C CB . PHE A 1 455 ? 20.028 -18.760 26.518 1.00 26.51 ? 455 PHE A CB 1 ATOM 3641 C CG . PHE A 1 455 ? 18.744 -18.908 25.737 1.00 26.89 ? 455 PHE A CG 1 ATOM 3642 C CD1 . PHE A 1 455 ? 17.888 -19.984 25.968 1.00 26.70 ? 455 PHE A CD1 1 ATOM 3643 C CD2 . PHE A 1 455 ? 18.370 -17.941 24.798 1.00 26.55 ? 455 PHE A CD2 1 ATOM 3644 C CE1 . PHE A 1 455 ? 16.694 -20.111 25.252 1.00 26.38 ? 455 PHE A CE1 1 ATOM 3645 C CE2 . PHE A 1 455 ? 17.187 -18.059 24.082 1.00 25.51 ? 455 PHE A CE2 1 ATOM 3646 C CZ . PHE A 1 455 ? 16.347 -19.146 24.306 1.00 26.36 ? 455 PHE A CZ 1 ATOM 3647 N N . CYS A 1 456 ? 22.249 -18.268 24.250 1.00 26.83 ? 456 CYS A N 1 ATOM 3648 C CA . CYS A 1 456 ? 22.522 -17.822 22.890 1.00 26.46 ? 456 CYS A CA 1 ATOM 3649 C C . CYS A 1 456 ? 23.805 -18.435 22.327 1.00 27.00 ? 456 CYS A C 1 ATOM 3650 O O . CYS A 1 456 ? 24.306 -18.005 21.286 1.00 26.76 ? 456 CYS A O 1 ATOM 3651 C CB . CYS A 1 456 ? 22.575 -16.294 22.853 1.00 26.49 ? 456 CYS A CB 1 ATOM 3652 S SG . CYS A 1 456 ? 20.945 -15.524 23.021 1.00 24.63 ? 456 CYS A SG 1 ATOM 3653 N N . GLY A 1 457 ? 24.327 -19.447 23.018 1.00 27.42 ? 457 GLY A N 1 ATOM 3654 C CA . GLY A 1 457 ? 25.564 -20.112 22.616 1.00 27.84 ? 457 GLY A CA 1 ATOM 3655 C C . GLY A 1 457 ? 26.780 -19.205 22.561 1.00 28.28 ? 457 GLY A C 1 ATOM 3656 O O . GLY A 1 457 ? 27.610 -19.361 21.681 1.00 28.86 ? 457 GLY A O 1 ATOM 3657 N N . LEU A 1 458 ? 26.877 -18.257 23.490 1.00 28.63 ? 458 LEU A N 1 ATOM 3658 C CA . LEU A 1 458 ? 27.997 -17.319 23.561 1.00 29.33 ? 458 LEU A CA 1 ATOM 3659 C C . LEU A 1 458 ? 28.757 -17.516 24.860 1.00 29.62 ? 458 LEU A C 1 ATOM 3660 O O . LEU A 1 458 ? 28.170 -17.925 25.856 1.00 29.29 ? 458 LEU A O 1 ATOM 3661 C CB . LEU A 1 458 ? 27.515 -15.861 23.520 1.00 29.31 ? 458 LEU A CB 1 ATOM 3662 C CG . LEU A 1 458 ? 26.614 -15.337 22.405 1.00 29.69 ? 458 LEU A CG 1 ATOM 3663 C CD1 . LEU A 1 458 ? 25.779 -14.139 22.884 1.00 29.14 ? 458 LEU A CD1 1 ATOM 3664 C CD2 . LEU A 1 458 ? 27.379 -15.029 21.137 1.00 29.11 ? 458 LEU A CD2 1 ATOM 3665 N N . SER A 1 459 ? 30.047 -17.169 24.849 1.00 30.14 ? 459 SER A N 1 ATOM 3666 C CA . SER A 1 459 ? 30.921 -17.314 26.014 1.00 30.92 ? 459 SER A CA 1 ATOM 3667 C C . SER A 1 459 ? 30.350 -16.692 27.293 1.00 31.32 ? 459 SER A C 1 ATOM 3668 O O . SER A 1 459 ? 29.655 -15.678 27.247 1.00 31.76 ? 459 SER A O 1 ATOM 3669 C CB . SER A 1 459 ? 32.294 -16.712 25.717 1.00 30.95 ? 459 SER A CB 1 ATOM 3670 O OG . SER A 1 459 ? 32.179 -15.320 25.474 1.00 31.42 ? 459 SER A OG 1 ATOM 3671 N N . GLN A 1 460 ? 30.651 -17.310 28.428 1.00 31.79 ? 460 GLN A N 1 ATOM 3672 C CA . GLN A 1 460 ? 30.160 -16.848 29.722 1.00 32.27 ? 460 GLN A CA 1 ATOM 3673 C C . GLN A 1 460 ? 31.341 -16.448 30.599 1.00 33.06 ? 460 GLN A C 1 ATOM 3674 O O . GLN A 1 460 ? 31.922 -17.298 31.275 1.00 33.36 ? 460 GLN A O 1 ATOM 3675 C CB . GLN A 1 460 ? 29.329 -17.948 30.402 1.00 32.22 ? 460 GLN A CB 1 ATOM 3676 C CG . GLN A 1 460 ? 28.250 -18.589 29.490 1.00 31.41 ? 460 GLN A CG 1 ATOM 3677 C CD . GLN A 1 460 ? 27.584 -19.801 30.113 1.00 30.72 ? 460 GLN A CD 1 ATOM 3678 O OE1 . GLN A 1 460 ? 26.818 -19.685 31.068 1.00 31.64 ? 460 GLN A OE1 1 ATOM 3679 N NE2 . GLN A 1 460 ? 27.866 -20.971 29.568 1.00 30.98 ? 460 GLN A NE2 1 ATOM 3680 N N . PRO A 1 461 ? 31.712 -15.153 30.584 1.00 33.61 ? 461 PRO A N 1 ATOM 3681 C CA . PRO A 1 461 ? 32.845 -14.684 31.398 1.00 34.15 ? 461 PRO A CA 1 ATOM 3682 C C . PRO A 1 461 ? 32.600 -14.906 32.893 1.00 34.62 ? 461 PRO A C 1 ATOM 3683 O O . PRO A 1 461 ? 31.480 -14.686 33.373 1.00 34.56 ? 461 PRO A O 1 ATOM 3684 C CB . PRO A 1 461 ? 32.910 -13.183 31.086 1.00 33.95 ? 461 PRO A CB 1 ATOM 3685 C CG . PRO A 1 461 ? 31.535 -12.830 30.598 1.00 33.82 ? 461 PRO A CG 1 ATOM 3686 C CD . PRO A 1 461 ? 31.082 -14.047 29.840 1.00 33.78 ? 461 PRO A CD 1 ATOM 3687 N N . LYS A 1 462 ? 33.637 -15.347 33.606 1.00 34.89 ? 462 LYS A N 1 ATOM 3688 C CA . LYS A 1 462 ? 33.559 -15.585 35.050 1.00 35.44 ? 462 LYS A CA 1 ATOM 3689 C C . LYS A 1 462 ? 34.451 -14.631 35.850 1.00 35.69 ? 462 LYS A C 1 ATOM 3690 O O . LYS A 1 462 ? 34.297 -14.491 37.069 1.00 35.60 ? 462 LYS A O 1 ATOM 3691 C CB . LYS A 1 462 ? 33.941 -17.033 35.373 1.00 35.77 ? 462 LYS A CB 1 ATOM 3692 C CG . LYS A 1 462 ? 33.043 -18.101 34.743 1.00 36.93 ? 462 LYS A CG 1 ATOM 3693 C CD . LYS A 1 462 ? 31.619 -18.018 35.262 1.00 38.94 ? 462 LYS A CD 1 ATOM 3694 C CE . LYS A 1 462 ? 30.816 -19.241 34.843 1.00 41.98 ? 462 LYS A CE 1 ATOM 3695 N NZ . LYS A 1 462 ? 29.327 -18.937 34.915 1.00 42.74 ? 462 LYS A NZ 1 ATOM 3696 N N . THR A 1 463 ? 35.374 -13.967 35.157 1.00 35.83 ? 463 THR A N 1 ATOM 3697 C CA . THR A 1 463 ? 36.370 -13.125 35.809 1.00 35.71 ? 463 THR A CA 1 ATOM 3698 C C . THR A 1 463 ? 36.340 -11.709 35.247 1.00 36.11 ? 463 THR A C 1 ATOM 3699 O O . THR A 1 463 ? 35.754 -11.478 34.162 1.00 36.18 ? 463 THR A O 1 ATOM 3700 C CB . THR A 1 463 ? 37.795 -13.716 35.649 1.00 35.75 ? 463 THR A CB 1 ATOM 3701 O OG1 . THR A 1 463 ? 38.100 -13.889 34.260 1.00 34.93 ? 463 THR A OG1 1 ATOM 3702 C CG2 . THR A 1 463 ? 37.898 -15.062 36.349 1.00 35.42 ? 463 THR A CG2 1 ATOM 3703 N N . LEU A 1 464 ? 36.959 -10.772 35.987 1.00 35.97 ? 464 LEU A N 1 ATOM 3704 C CA . LEU A 1 464 ? 37.098 -9.379 35.556 1.00 35.89 ? 464 LEU A CA 1 ATOM 3705 C C . LEU A 1 464 ? 37.573 -9.331 34.113 1.00 36.31 ? 464 LEU A C 1 ATOM 3706 O O . LEU A 1 464 ? 36.988 -8.631 33.276 1.00 36.80 ? 464 LEU A O 1 ATOM 3707 C CB . LEU A 1 464 ? 38.120 -8.634 36.411 1.00 35.61 ? 464 LEU A CB 1 ATOM 3708 C CG . LEU A 1 464 ? 38.006 -7.103 36.583 1.00 36.23 ? 464 LEU A CG 1 ATOM 3709 C CD1 . LEU A 1 464 ? 39.355 -6.443 36.896 1.00 34.27 ? 464 LEU A CD1 1 ATOM 3710 C CD2 . LEU A 1 464 ? 37.351 -6.389 35.400 1.00 36.82 ? 464 LEU A CD2 1 ATOM 3711 N N . LYS A 1 465 ? 38.625 -10.098 33.832 1.00 36.16 ? 465 LYS A N 1 ATOM 3712 C CA . LYS A 1 465 ? 39.322 -10.021 32.568 1.00 36.40 ? 465 LYS A CA 1 ATOM 3713 C C . LYS A 1 465 ? 38.500 -10.596 31.435 1.00 35.89 ? 465 LYS A C 1 ATOM 3714 O O . LYS A 1 465 ? 38.593 -10.133 30.298 1.00 36.17 ? 465 LYS A O 1 ATOM 3715 C CB . LYS A 1 465 ? 40.680 -10.723 32.667 1.00 36.85 ? 465 LYS A CB 1 ATOM 3716 C CG . LYS A 1 465 ? 41.787 -9.976 31.934 1.00 38.37 ? 465 LYS A CG 1 ATOM 3717 C CD . LYS A 1 465 ? 43.166 -10.380 32.423 1.00 40.71 ? 465 LYS A CD 1 ATOM 3718 C CE . LYS A 1 465 ? 44.025 -9.149 32.647 1.00 41.74 ? 465 LYS A CE 1 ATOM 3719 N NZ . LYS A 1 465 ? 45.423 -9.407 32.233 1.00 44.41 ? 465 LYS A NZ 1 ATOM 3720 N N . GLY A 1 466 ? 37.711 -11.618 31.750 1.00 35.66 ? 466 GLY A N 1 ATOM 3721 C CA . GLY A 1 466 ? 36.764 -12.193 30.800 1.00 35.11 ? 466 GLY A CA 1 ATOM 3722 C C . GLY A 1 466 ? 35.706 -11.172 30.431 1.00 34.72 ? 466 GLY A C 1 ATOM 3723 O O . GLY A 1 466 ? 35.406 -10.982 29.252 1.00 34.58 ? 466 GLY A O 1 ATOM 3724 N N . LEU A 1 467 ? 35.156 -10.500 31.443 1.00 34.24 ? 467 LEU A N 1 ATOM 3725 C CA . LEU A 1 467 ? 34.179 -9.449 31.209 1.00 33.87 ? 467 LEU A CA 1 ATOM 3726 C C . LEU A 1 467 ? 34.744 -8.273 30.412 1.00 33.78 ? 467 LEU A C 1 ATOM 3727 O O . LEU A 1 467 ? 34.032 -7.682 29.610 1.00 33.81 ? 467 LEU A O 1 ATOM 3728 C CB . LEU A 1 467 ? 33.550 -8.973 32.520 1.00 34.02 ? 467 LEU A CB 1 ATOM 3729 C CG . LEU A 1 467 ? 32.302 -8.098 32.335 1.00 33.67 ? 467 LEU A CG 1 ATOM 3730 C CD1 . LEU A 1 467 ? 31.132 -8.852 31.670 1.00 31.90 ? 467 LEU A CD1 1 ATOM 3731 C CD2 . LEU A 1 467 ? 31.884 -7.512 33.656 1.00 33.66 ? 467 LEU A CD2 1 ATOM 3732 N N . GLN A 1 468 ? 36.018 -7.947 30.617 1.00 34.03 ? 468 GLN A N 1 ATOM 3733 C CA . GLN A 1 468 ? 36.682 -6.884 29.847 1.00 34.26 ? 468 GLN A CA 1 ATOM 3734 C C . GLN A 1 468 ? 36.757 -7.213 28.359 1.00 33.93 ? 468 GLN A C 1 ATOM 3735 O O . GLN A 1 468 ? 36.560 -6.329 27.519 1.00 34.17 ? 468 GLN A O 1 ATOM 3736 C CB . GLN A 1 468 ? 38.092 -6.599 30.372 1.00 34.49 ? 468 GLN A CB 1 ATOM 3737 C CG . GLN A 1 468 ? 38.138 -5.977 31.751 1.00 36.13 ? 468 GLN A CG 1 ATOM 3738 C CD . GLN A 1 468 ? 39.560 -5.840 32.300 1.00 38.32 ? 468 GLN A CD 1 ATOM 3739 O OE1 . GLN A 1 468 ? 39.758 -5.329 33.407 1.00 39.47 ? 468 GLN A OE1 1 ATOM 3740 N NE2 . GLN A 1 468 ? 40.550 -6.279 31.523 1.00 38.90 ? 468 GLN A NE2 1 ATOM 3741 N N . THR A 1 469 ? 37.046 -8.474 28.044 1.00 33.26 ? 469 THR A N 1 ATOM 3742 C CA . THR A 1 469 ? 37.110 -8.939 26.658 1.00 32.87 ? 469 THR A CA 1 ATOM 3743 C C . THR A 1 469 ? 35.743 -8.928 25.967 1.00 32.51 ? 469 THR A C 1 ATOM 3744 O O . THR A 1 469 ? 35.629 -8.466 24.823 1.00 33.15 ? 469 THR A O 1 ATOM 3745 C CB . THR A 1 469 ? 37.755 -10.332 26.551 1.00 33.10 ? 469 THR A CB 1 ATOM 3746 O OG1 . THR A 1 469 ? 39.020 -10.307 27.214 1.00 33.64 ? 469 THR A OG1 1 ATOM 3747 C CG2 . THR A 1 469 ? 37.985 -10.727 25.087 1.00 33.93 ? 469 THR A CG2 1 ATOM 3748 N N . VAL A 1 470 ? 34.713 -9.437 26.640 1.00 31.20 ? 470 VAL A N 1 ATOM 3749 C CA . VAL A 1 470 ? 33.368 -9.403 26.071 1.00 30.43 ? 470 VAL A CA 1 ATOM 3750 C C . VAL A 1 470 ? 32.883 -7.958 25.842 1.00 29.83 ? 470 VAL A C 1 ATOM 3751 O O . VAL A 1 470 ? 32.459 -7.609 24.740 1.00 29.76 ? 470 VAL A O 1 ATOM 3752 C CB . VAL A 1 470 ? 32.362 -10.222 26.914 1.00 30.62 ? 470 VAL A CB 1 ATOM 3753 C CG1 . VAL A 1 470 ? 30.951 -10.010 26.420 1.00 30.65 ? 470 VAL A CG1 1 ATOM 3754 C CG2 . VAL A 1 470 ? 32.712 -11.708 26.850 1.00 30.99 ? 470 VAL A CG2 1 ATOM 3755 N N . LEU A 1 471 ? 32.986 -7.116 26.868 1.00 29.06 ? 471 LEU A N 1 ATOM 3756 C CA . LEU A 1 471 ? 32.534 -5.729 26.771 1.00 28.39 ? 471 LEU A CA 1 ATOM 3757 C C . LEU A 1 471 ? 33.474 -4.838 25.961 1.00 28.44 ? 471 LEU A C 1 ATOM 3758 O O . LEU A 1 471 ? 33.083 -3.755 25.540 1.00 27.79 ? 471 LEU A O 1 ATOM 3759 C CB . LEU A 1 471 ? 32.337 -5.149 28.165 1.00 28.15 ? 471 LEU A CB 1 ATOM 3760 C CG . LEU A 1 471 ? 30.974 -5.322 28.845 1.00 27.95 ? 471 LEU A CG 1 ATOM 3761 C CD1 . LEU A 1 471 ? 30.222 -6.596 28.449 1.00 26.79 ? 471 LEU A CD1 1 ATOM 3762 C CD2 . LEU A 1 471 ? 31.168 -5.243 30.340 1.00 26.40 ? 471 LEU A CD2 1 ATOM 3763 N N . LYS A 1 472 ? 34.698 -5.318 25.733 1.00 28.85 ? 472 LYS A N 1 ATOM 3764 C CA . LYS A 1 472 ? 35.760 -4.546 25.093 1.00 29.46 ? 472 LYS A CA 1 ATOM 3765 C C . LYS A 1 472 ? 35.944 -3.192 25.767 1.00 29.17 ? 472 LYS A C 1 ATOM 3766 O O . LYS A 1 472 ? 36.165 -2.188 25.095 1.00 28.75 ? 472 LYS A O 1 ATOM 3767 C CB . LYS A 1 472 ? 35.513 -4.390 23.586 1.00 29.89 ? 472 LYS A CB 1 ATOM 3768 C CG . LYS A 1 472 ? 35.816 -5.648 22.794 1.00 32.24 ? 472 LYS A CG 1 ATOM 3769 C CD . LYS A 1 472 ? 35.482 -5.469 21.327 1.00 35.24 ? 472 LYS A CD 1 ATOM 3770 C CE . LYS A 1 472 ? 35.968 -6.662 20.518 1.00 37.54 ? 472 LYS A CE 1 ATOM 3771 N NZ . LYS A 1 472 ? 35.219 -7.904 20.874 1.00 40.27 ? 472 LYS A NZ 1 ATOM 3772 N N . ASN A 1 473 ? 35.859 -3.192 27.098 1.00 29.29 ? 473 ASN A N 1 ATOM 3773 C CA . ASN A 1 473 ? 35.932 -1.980 27.908 1.00 30.01 ? 473 ASN A CA 1 ATOM 3774 C C . ASN A 1 473 ? 36.410 -2.311 29.335 1.00 30.93 ? 473 ASN A C 1 ATOM 3775 O O . ASN A 1 473 ? 35.706 -2.986 30.087 1.00 31.26 ? 473 ASN A O 1 ATOM 3776 C CB . ASN A 1 473 ? 34.560 -1.297 27.920 1.00 29.57 ? 473 ASN A CB 1 ATOM 3777 C CG . ASN A 1 473 ? 34.609 0.128 28.435 1.00 29.80 ? 473 ASN A CG 1 ATOM 3778 O OD1 . ASN A 1 473 ? 35.306 0.433 29.404 1.00 30.64 ? 473 ASN A OD1 1 ATOM 3779 N ND2 . ASN A 1 473 ? 33.831 1.006 27.810 1.00 29.01 ? 473 ASN A ND2 1 ATOM 3780 N N . LYS A 1 474 ? 37.605 -1.846 29.704 1.00 31.91 ? 474 LYS A N 1 ATOM 3781 C CA . LYS A 1 474 ? 38.171 -2.132 31.033 1.00 33.20 ? 474 LYS A CA 1 ATOM 3782 C C . LYS A 1 474 ? 37.392 -1.455 32.143 1.00 33.68 ? 474 LYS A C 1 ATOM 3783 O O . LYS A 1 474 ? 37.082 -2.089 33.148 1.00 34.15 ? 474 LYS A O 1 ATOM 3784 C CB . LYS A 1 474 ? 39.649 -1.720 31.151 1.00 33.04 ? 474 LYS A CB 1 ATOM 3785 C CG . LYS A 1 474 ? 40.664 -2.738 30.630 1.00 35.18 ? 474 LYS A CG 1 ATOM 3786 C CD . LYS A 1 474 ? 42.108 -2.260 30.871 1.00 37.68 ? 474 LYS A CD 1 ATOM 3787 C CE . LYS A 1 474 ? 43.110 -2.957 29.929 1.00 39.43 ? 474 LYS A CE 1 ATOM 3788 N NZ . LYS A 1 474 ? 44.526 -2.933 30.457 1.00 40.05 ? 474 LYS A NZ 1 ATOM 3789 N N . ILE A 1 475 ? 37.082 -0.174 31.956 1.00 34.22 ? 475 ILE A N 1 ATOM 3790 C CA . ILE A 1 475 ? 36.443 0.629 33.004 1.00 34.85 ? 475 ILE A CA 1 ATOM 3791 C C . ILE A 1 475 ? 35.007 0.183 33.305 1.00 34.63 ? 475 ILE A C 1 ATOM 3792 O O . ILE A 1 475 ? 34.676 -0.104 34.458 1.00 34.91 ? 475 ILE A O 1 ATOM 3793 C CB . ILE A 1 475 ? 36.535 2.158 32.692 1.00 35.11 ? 475 ILE A CB 1 ATOM 3794 C CG1 . ILE A 1 475 ? 38.000 2.608 32.613 1.00 36.00 ? 475 ILE A CG1 1 ATOM 3795 C CG2 . ILE A 1 475 ? 35.821 2.977 33.736 1.00 35.44 ? 475 ILE A CG2 1 ATOM 3796 C CD1 . ILE A 1 475 ? 38.861 2.172 33.805 1.00 38.81 ? 475 ILE A CD1 1 ATOM 3797 N N . LEU A 1 476 ? 34.172 0.108 32.268 1.00 34.51 ? 476 LEU A N 1 ATOM 3798 C CA . LEU A 1 476 ? 32.808 -0.419 32.396 1.00 34.29 ? 476 LEU A CA 1 ATOM 3799 C C . LEU A 1 476 ? 32.794 -1.765 33.111 1.00 34.17 ? 476 LEU A C 1 ATOM 3800 O O . LEU A 1 476 ? 32.016 -1.973 34.034 1.00 34.23 ? 476 LEU A O 1 ATOM 3801 C CB . LEU A 1 476 ? 32.131 -0.545 31.024 1.00 33.93 ? 476 LEU A CB 1 ATOM 3802 C CG . LEU A 1 476 ? 30.696 -1.089 31.018 1.00 33.84 ? 476 LEU A CG 1 ATOM 3803 C CD1 . LEU A 1 476 ? 29.810 -0.291 31.965 1.00 33.75 ? 476 LEU A CD1 1 ATOM 3804 C CD2 . LEU A 1 476 ? 30.106 -1.091 29.622 1.00 32.34 ? 476 LEU A CD2 1 ATOM 3805 N N . ALA A 1 477 ? 33.676 -2.664 32.691 1.00 34.40 ? 477 ALA A N 1 ATOM 3806 C CA . ALA A 1 477 ? 33.753 -3.997 33.277 1.00 34.73 ? 477 ALA A CA 1 ATOM 3807 C C . ALA A 1 477 ? 34.103 -3.967 34.763 1.00 34.96 ? 477 ALA A C 1 ATOM 3808 O O . ALA A 1 477 ? 33.637 -4.811 35.528 1.00 34.62 ? 477 ALA A O 1 ATOM 3809 C CB . ALA A 1 477 ? 34.733 -4.841 32.518 1.00 34.54 ? 477 ALA A CB 1 ATOM 3810 N N . LYS A 1 478 ? 34.897 -2.975 35.162 1.00 35.57 ? 478 LYS A N 1 ATOM 3811 C CA . LYS A 1 478 ? 35.349 -2.848 36.544 1.00 36.45 ? 478 LYS A CA 1 ATOM 3812 C C . LYS A 1 478 ? 34.233 -2.354 37.451 1.00 36.50 ? 478 LYS A C 1 ATOM 3813 O O . LYS A 1 478 ? 34.067 -2.841 38.580 1.00 36.43 ? 478 LYS A O 1 ATOM 3814 C CB . LYS A 1 478 ? 36.544 -1.905 36.613 1.00 37.11 ? 478 LYS A CB 1 ATOM 3815 C CG . LYS A 1 478 ? 37.166 -1.742 37.999 1.00 38.85 ? 478 LYS A CG 1 ATOM 3816 C CD . LYS A 1 478 ? 38.613 -1.259 37.875 1.00 44.32 ? 478 LYS A CD 1 ATOM 3817 C CE . LYS A 1 478 ? 38.747 -0.074 36.897 1.00 46.39 ? 478 LYS A CE 1 ATOM 3818 N NZ . LYS A 1 478 ? 39.935 -0.217 35.985 1.00 48.58 ? 478 LYS A NZ 1 ATOM 3819 N N . LYS A 1 479 ? 33.467 -1.391 36.949 1.00 36.58 ? 479 LYS A N 1 ATOM 3820 C CA . LYS A 1 479 ? 32.346 -0.843 37.698 1.00 36.71 ? 479 LYS A CA 1 ATOM 3821 C C . LYS A 1 479 ? 31.304 -1.934 37.924 1.00 36.57 ? 479 LYS A C 1 ATOM 3822 O O . LYS A 1 479 ? 30.886 -2.170 39.058 1.00 36.72 ? 479 LYS A O 1 ATOM 3823 C CB . LYS A 1 479 ? 31.735 0.349 36.968 1.00 36.56 ? 479 LYS A CB 1 ATOM 3824 C CG . LYS A 1 479 ? 32.655 1.536 36.820 1.00 37.16 ? 479 LYS A CG 1 ATOM 3825 C CD . LYS A 1 479 ? 31.925 2.629 36.087 1.00 39.13 ? 479 LYS A CD 1 ATOM 3826 C CE . LYS A 1 479 ? 32.794 3.842 35.824 1.00 39.53 ? 479 LYS A CE 1 ATOM 3827 N NZ . LYS A 1 479 ? 32.004 4.806 34.991 1.00 40.39 ? 479 LYS A NZ 1 ATOM 3828 N N . LEU A 1 480 ? 30.916 -2.610 36.841 1.00 36.15 ? 480 LEU A N 1 ATOM 3829 C CA . LEU A 1 480 ? 29.980 -3.737 36.898 1.00 35.90 ? 480 LEU A CA 1 ATOM 3830 C C . LEU A 1 480 ? 30.385 -4.803 37.927 1.00 35.94 ? 480 LEU A C 1 ATOM 3831 O O . LEU A 1 480 ? 29.555 -5.303 38.687 1.00 35.86 ? 480 LEU A O 1 ATOM 3832 C CB . LEU A 1 480 ? 29.868 -4.366 35.516 1.00 35.74 ? 480 LEU A CB 1 ATOM 3833 C CG . LEU A 1 480 ? 28.648 -4.175 34.609 1.00 35.94 ? 480 LEU A CG 1 ATOM 3834 C CD1 . LEU A 1 480 ? 27.816 -2.942 34.880 1.00 35.33 ? 480 LEU A CD1 1 ATOM 3835 C CD2 . LEU A 1 480 ? 29.097 -4.241 33.155 1.00 36.07 ? 480 LEU A CD2 1 ATOM 3836 N N . MET A 1 481 ? 31.677 -5.122 37.957 1.00 36.00 ? 481 MET A N 1 ATOM 3837 C CA . MET A 1 481 ? 32.216 -6.154 38.832 1.00 35.66 ? 481 MET A CA 1 ATOM 3838 C C . MET A 1 481 ? 32.239 -5.702 40.284 1.00 35.60 ? 481 MET A C 1 ATOM 3839 O O . MET A 1 481 ? 32.040 -6.516 41.176 1.00 35.75 ? 481 MET A O 1 ATOM 3840 C CB . MET A 1 481 ? 33.606 -6.543 38.348 1.00 35.64 ? 481 MET A CB 1 ATOM 3841 C CG . MET A 1 481 ? 34.067 -7.943 38.700 1.00 36.94 ? 481 MET A CG 1 ATOM 3842 S SD . MET A 1 481 ? 33.143 -9.336 38.002 1.00 37.83 ? 481 MET A SD 1 ATOM 3843 C CE . MET A 1 481 ? 32.527 -8.657 36.479 1.00 38.62 ? 481 MET A CE 1 ATOM 3844 N N . ASP A 1 482 ? 32.468 -4.408 40.521 1.00 35.49 ? 482 ASP A N 1 ATOM 3845 C CA . ASP A 1 482 ? 32.433 -3.846 41.875 1.00 34.94 ? 482 ASP A CA 1 ATOM 3846 C C . ASP A 1 482 ? 31.014 -3.796 42.439 1.00 34.60 ? 482 ASP A C 1 ATOM 3847 O O . ASP A 1 482 ? 30.817 -3.922 43.650 1.00 34.78 ? 482 ASP A O 1 ATOM 3848 C CB . ASP A 1 482 ? 33.061 -2.447 41.913 1.00 35.39 ? 482 ASP A CB 1 ATOM 3849 C CG . ASP A 1 482 ? 34.595 -2.471 41.808 1.00 36.98 ? 482 ASP A CG 1 ATOM 3850 O OD1 . ASP A 1 482 ? 35.201 -3.564 41.900 1.00 39.36 ? 482 ASP A OD1 1 ATOM 3851 O OD2 . ASP A 1 482 ? 35.204 -1.390 41.612 1.00 37.42 ? 482 ASP A OD2 1 ATOM 3852 N N . LEU A 1 483 ? 30.023 -3.605 41.571 1.00 33.79 ? 483 LEU A N 1 ATOM 3853 C CA . LEU A 1 483 ? 28.632 -3.590 42.024 1.00 33.01 ? 483 LEU A CA 1 ATOM 3854 C C . LEU A 1 483 ? 28.021 -4.989 42.158 1.00 32.41 ? 483 LEU A C 1 ATOM 3855 O O . LEU A 1 483 ? 27.240 -5.246 43.071 1.00 31.84 ? 483 LEU A O 1 ATOM 3856 C CB . LEU A 1 483 ? 27.766 -2.717 41.119 1.00 32.78 ? 483 LEU A CB 1 ATOM 3857 C CG . LEU A 1 483 ? 27.894 -1.220 41.399 1.00 32.92 ? 483 LEU A CG 1 ATOM 3858 C CD1 . LEU A 1 483 ? 27.233 -0.379 40.301 1.00 32.54 ? 483 LEU A CD1 1 ATOM 3859 C CD2 . LEU A 1 483 ? 27.323 -0.887 42.756 1.00 32.72 ? 483 LEU A CD2 1 ATOM 3860 N N . TYR A 1 484 ? 28.481 -5.837 41.350 1.00 32.48 ? 484 TYR A N 1 ATOM 3861 C CA . TYR A 1 484 ? 27.840 -7.145 41.256 1.00 32.30 ? 484 TYR A CA 1 ATOM 3862 C C . TYR A 1 484 ? 28.661 -8.371 41.770 1.00 32.21 ? 484 TYR A C 1 ATOM 3863 O O . TYR A 1 484 ? 28.097 -9.423 42.008 1.00 31.98 ? 484 TYR A O 1 ATOM 3864 C CB . TYR A 1 484 ? 27.463 -7.392 39.785 1.00 32.19 ? 484 TYR A CB 1 ATOM 3865 C CG . TYR A 1 484 ? 26.263 -6.658 39.219 1.00 30.74 ? 484 TYR A CG 1 ATOM 3866 C CD1 . TYR A 1 484 ? 24.984 -7.047 39.560 1.00 30.35 ? 484 TYR A CD1 1 ATOM 3867 C CD2 . TYR A 1 484 ? 26.412 -5.607 38.316 1.00 29.91 ? 484 TYR A CD2 1 ATOM 3868 C CE1 . TYR A 1 484 ? 23.887 -6.412 39.045 1.00 29.46 ? 484 TYR A CE1 1 ATOM 3869 C CE2 . TYR A 1 484 ? 25.308 -4.950 37.796 1.00 29.06 ? 484 TYR A CE2 1 ATOM 3870 C CZ . TYR A 1 484 ? 24.048 -5.375 38.169 1.00 28.69 ? 484 TYR A CZ 1 ATOM 3871 O OH . TYR A 1 484 ? 22.926 -4.787 37.681 1.00 26.24 ? 484 TYR A OH 1 ATOM 3872 N N . LYS A 1 485 ? 29.981 -8.236 41.902 1.00 32.16 ? 485 LYS A N 1 ATOM 3873 C CA . LYS A 1 485 ? 30.867 -9.298 42.415 1.00 32.60 ? 485 LYS A CA 1 ATOM 3874 C C . LYS A 1 485 ? 31.082 -10.512 41.480 1.00 32.07 ? 485 LYS A C 1 ATOM 3875 O O . LYS A 1 485 ? 32.106 -11.214 41.560 1.00 32.75 ? 485 LYS A O 1 ATOM 3876 C CB . LYS A 1 485 ? 30.415 -9.788 43.815 1.00 32.66 ? 485 LYS A CB 1 ATOM 3877 C CG . LYS A 1 485 ? 30.215 -8.683 44.853 1.00 35.38 ? 485 LYS A CG 1 ATOM 3878 C CD . LYS A 1 485 ? 31.448 -7.768 44.960 1.00 40.25 ? 485 LYS A CD 1 ATOM 3879 C CE . LYS A 1 485 ? 31.317 -6.731 46.091 1.00 42.46 ? 485 LYS A CE 1 ATOM 3880 N NZ . LYS A 1 485 ? 29.901 -6.248 46.338 1.00 42.03 ? 485 LYS A NZ 1 ATOM 3881 N N . THR A 1 486 ? 30.137 -10.778 40.605 1.00 30.28 ? 486 THR A N 1 ATOM 3882 C CA . THR A 1 486 ? 30.325 -11.873 39.686 1.00 29.59 ? 486 THR A CA 1 ATOM 3883 C C . THR A 1 486 ? 29.468 -11.617 38.468 1.00 29.31 ? 486 THR A C 1 ATOM 3884 O O . THR A 1 486 ? 28.400 -11.061 38.595 1.00 29.51 ? 486 THR A O 1 ATOM 3885 C CB . THR A 1 486 ? 29.921 -13.151 40.355 1.00 29.36 ? 486 THR A CB 1 ATOM 3886 O OG1 . THR A 1 486 ? 29.863 -14.177 39.366 1.00 28.91 ? 486 THR A OG1 1 ATOM 3887 C CG2 . THR A 1 486 ? 28.487 -13.047 40.875 1.00 30.50 ? 486 THR A CG2 1 ATOM 3888 N N . PRO A 1 487 ? 29.694 -11.840 37.259 1.00 29.71 ? 487 PRO A N 1 ATOM 3889 C CA . PRO A 1 487 ? 28.882 -11.605 36.065 1.00 29.84 ? 487 PRO A CA 1 ATOM 3890 C C . PRO A 1 487 ? 27.600 -12.443 36.027 1.00 29.91 ? 487 PRO A C 1 ATOM 3891 O O . PRO A 1 487 ? 26.665 -12.109 35.291 1.00 30.55 ? 487 PRO A O 1 ATOM 3892 C CB . PRO A 1 487 ? 29.821 -11.979 34.907 1.00 29.98 ? 487 PRO A CB 1 ATOM 3893 C CG . PRO A 1 487 ? 31.198 -12.010 35.496 1.00 29.57 ? 487 PRO A CG 1 ATOM 3894 C CD . PRO A 1 487 ? 31.011 -12.411 36.933 1.00 29.65 ? 487 PRO A CD 1 ATOM 3895 N N . ASP A 1 488 ? 27.549 -13.512 36.822 1.00 29.64 ? 488 ASP A N 1 ATOM 3896 C CA . ASP A 1 488 ? 26.362 -14.366 36.896 1.00 29.35 ? 488 ASP A CA 1 ATOM 3897 C C . ASP A 1 488 ? 25.180 -13.592 37.442 1.00 28.67 ? 488 ASP A C 1 ATOM 3898 O O . ASP A 1 488 ? 24.029 -13.918 37.150 1.00 29.09 ? 488 ASP A O 1 ATOM 3899 C CB . ASP A 1 488 ? 26.617 -15.587 37.785 1.00 29.83 ? 488 ASP A CB 1 ATOM 3900 C CG . ASP A 1 488 ? 27.572 -16.587 37.159 1.00 30.47 ? 488 ASP A CG 1 ATOM 3901 O OD1 . ASP A 1 488 ? 27.969 -16.425 35.982 1.00 31.81 ? 488 ASP A OD1 1 ATOM 3902 O OD2 . ASP A 1 488 ? 27.924 -17.553 37.859 1.00 33.52 ? 488 ASP A OD2 1 ATOM 3903 N N . ASN A 1 489 ? 25.484 -12.566 38.232 1.00 27.58 ? 489 ASN A N 1 ATOM 3904 C CA . ASN A 1 489 ? 24.483 -11.710 38.843 1.00 26.38 ? 489 ASN A CA 1 ATOM 3905 C C . ASN A 1 489 ? 24.057 -10.482 38.017 1.00 26.30 ? 489 ASN A C 1 ATOM 3906 O O . ASN A 1 489 ? 23.066 -9.837 38.377 1.00 26.01 ? 489 ASN A O 1 ATOM 3907 C CB . ASN A 1 489 ? 24.965 -11.264 40.220 1.00 25.96 ? 489 ASN A CB 1 ATOM 3908 C CG . ASN A 1 489 ? 24.848 -12.351 41.256 1.00 25.39 ? 489 ASN A CG 1 ATOM 3909 O OD1 . ASN A 1 489 ? 24.601 -13.511 40.933 1.00 26.27 ? 489 ASN A OD1 1 ATOM 3910 N ND2 . ASN A 1 489 ? 25.020 -11.984 42.514 1.00 24.19 ? 489 ASN A ND2 1 ATOM 3911 N N . ILE A 1 490 ? 24.792 -10.156 36.940 1.00 25.81 ? 490 ILE A N 1 ATOM 3912 C CA . ILE A 1 490 ? 24.503 -8.958 36.141 1.00 25.60 ? 490 ILE A CA 1 ATOM 3913 C C . ILE A 1 490 ? 23.071 -9.072 35.604 1.00 25.34 ? 490 ILE A C 1 ATOM 3914 O O . ILE A 1 490 ? 22.743 -10.008 34.869 1.00 25.11 ? 490 ILE A O 1 ATOM 3915 C CB . ILE A 1 490 ? 25.484 -8.747 34.915 1.00 26.29 ? 490 ILE A CB 1 ATOM 3916 C CG1 . ILE A 1 490 ? 26.913 -8.321 35.280 1.00 26.44 ? 490 ILE A CG1 1 ATOM 3917 C CG2 . ILE A 1 490 ? 25.000 -7.615 34.021 1.00 25.46 ? 490 ILE A CG2 1 ATOM 3918 C CD1 . ILE A 1 490 ? 27.436 -8.833 36.531 1.00 30.85 ? 490 ILE A CD1 1 ATOM 3919 N N . ASP A 1 491 ? 22.224 -8.121 35.990 1.00 24.85 ? 491 ASP A N 1 ATOM 3920 C CA . ASP A 1 491 ? 20.878 -7.991 35.436 1.00 24.58 ? 491 ASP A CA 1 ATOM 3921 C C . ASP A 1 491 ? 20.906 -7.948 33.895 1.00 24.47 ? 491 ASP A C 1 ATOM 3922 O O . ASP A 1 491 ? 21.735 -7.233 33.303 1.00 24.21 ? 491 ASP A O 1 ATOM 3923 C CB . ASP A 1 491 ? 20.193 -6.740 36.010 1.00 24.24 ? 491 ASP A CB 1 ATOM 3924 C CG . ASP A 1 491 ? 20.002 -6.814 37.541 1.00 23.60 ? 491 ASP A CG 1 ATOM 3925 O OD1 . ASP A 1 491 ? 19.281 -7.710 38.029 1.00 21.59 ? 491 ASP A OD1 1 ATOM 3926 O OD2 . ASP A 1 491 ? 20.584 -5.970 38.256 1.00 21.46 ? 491 ASP A OD2 1 ATOM 3927 N N . ILE A 1 492 ? 20.028 -8.738 33.263 1.00 24.23 ? 492 ILE A N 1 ATOM 3928 C CA . ILE A 1 492 ? 19.951 -8.832 31.782 1.00 24.11 ? 492 ILE A CA 1 ATOM 3929 C C . ILE A 1 492 ? 19.878 -7.469 31.065 1.00 24.24 ? 492 ILE A C 1 ATOM 3930 O O . ILE A 1 492 ? 20.561 -7.249 30.052 1.00 24.03 ? 492 ILE A O 1 ATOM 3931 C CB . ILE A 1 492 ? 18.822 -9.817 31.278 1.00 23.89 ? 492 ILE A CB 1 ATOM 3932 C CG1 . ILE A 1 492 ? 18.811 -9.936 29.751 1.00 23.68 ? 492 ILE A CG1 1 ATOM 3933 C CG2 . ILE A 1 492 ? 17.432 -9.406 31.752 1.00 23.40 ? 492 ILE A CG2 1 ATOM 3934 C CD1 . ILE A 1 492 ? 20.043 -10.569 29.147 1.00 22.93 ? 492 ILE A CD1 1 ATOM 3935 N N . TRP A 1 493 ? 19.080 -6.551 31.599 1.00 24.57 ? 493 TRP A N 1 ATOM 3936 C CA . TRP A 1 493 ? 18.912 -5.253 30.946 1.00 25.07 ? 493 TRP A CA 1 ATOM 3937 C C . TRP A 1 493 ? 20.221 -4.481 30.825 1.00 25.51 ? 493 TRP A C 1 ATOM 3938 O O . TRP A 1 493 ? 20.535 -3.976 29.753 1.00 26.14 ? 493 TRP A O 1 ATOM 3939 C CB . TRP A 1 493 ? 17.843 -4.379 31.624 1.00 24.72 ? 493 TRP A CB 1 ATOM 3940 C CG . TRP A 1 493 ? 17.682 -3.053 30.904 1.00 24.20 ? 493 TRP A CG 1 ATOM 3941 C CD1 . TRP A 1 493 ? 17.120 -2.844 29.670 1.00 23.06 ? 493 TRP A CD1 1 ATOM 3942 C CD2 . TRP A 1 493 ? 18.132 -1.773 31.358 1.00 23.54 ? 493 TRP A CD2 1 ATOM 3943 N NE1 . TRP A 1 493 ? 17.190 -1.516 29.336 1.00 22.31 ? 493 TRP A NE1 1 ATOM 3944 C CE2 . TRP A 1 493 ? 17.799 -0.836 30.360 1.00 23.47 ? 493 TRP A CE2 1 ATOM 3945 C CE3 . TRP A 1 493 ? 18.782 -1.324 32.521 1.00 23.84 ? 493 TRP A CE3 1 ATOM 3946 C CZ2 . TRP A 1 493 ? 18.075 0.526 30.497 1.00 23.81 ? 493 TRP A CZ2 1 ATOM 3947 C CZ3 . TRP A 1 493 ? 19.067 0.023 32.649 1.00 22.80 ? 493 TRP A CZ3 1 ATOM 3948 C CH2 . TRP A 1 493 ? 18.714 0.931 31.643 1.00 23.50 ? 493 TRP A CH2 1 ATOM 3949 N N . ILE A 1 494 ? 20.969 -4.379 31.923 1.00 25.79 ? 494 ILE A N 1 ATOM 3950 C CA . ILE A 1 494 ? 22.250 -3.681 31.903 1.00 25.86 ? 494 ILE A CA 1 ATOM 3951 C C . ILE A 1 494 ? 23.337 -4.514 31.232 1.00 26.25 ? 494 ILE A C 1 ATOM 3952 O O . ILE A 1 494 ? 24.229 -3.960 30.615 1.00 27.10 ? 494 ILE A O 1 ATOM 3953 C CB . ILE A 1 494 ? 22.714 -3.209 33.320 1.00 25.66 ? 494 ILE A CB 1 ATOM 3954 C CG1 . ILE A 1 494 ? 23.733 -2.067 33.207 1.00 25.18 ? 494 ILE A CG1 1 ATOM 3955 C CG2 . ILE A 1 494 ? 23.315 -4.343 34.129 1.00 24.52 ? 494 ILE A CG2 1 ATOM 3956 C CD1 . ILE A 1 494 ? 23.181 -0.795 32.629 1.00 25.21 ? 494 ILE A CD1 1 ATOM 3957 N N . GLY A 1 495 ? 23.265 -5.837 31.349 1.00 26.31 ? 495 GLY A N 1 ATOM 3958 C CA . GLY A 1 495 ? 24.248 -6.703 30.694 1.00 26.01 ? 495 GLY A CA 1 ATOM 3959 C C . GLY A 1 495 ? 24.129 -6.691 29.176 1.00 25.55 ? 495 GLY A C 1 ATOM 3960 O O . GLY A 1 495 ? 25.113 -6.470 28.472 1.00 25.57 ? 495 GLY A O 1 ATOM 3961 N N . GLY A 1 496 ? 22.920 -6.933 28.678 1.00 24.88 ? 496 GLY A N 1 ATOM 3962 C CA . GLY A 1 496 ? 22.656 -6.922 27.245 1.00 24.21 ? 496 GLY A CA 1 ATOM 3963 C C . GLY A 1 496 ? 23.017 -5.607 26.586 1.00 23.81 ? 496 GLY A C 1 ATOM 3964 O O . GLY A 1 496 ? 23.578 -5.585 25.495 1.00 23.23 ? 496 GLY A O 1 ATOM 3965 N N . ASN A 1 497 ? 22.718 -4.503 27.263 1.00 23.95 ? 497 ASN A N 1 ATOM 3966 C CA . ASN A 1 497 ? 22.991 -3.173 26.701 1.00 24.18 ? 497 ASN A CA 1 ATOM 3967 C C . ASN A 1 497 ? 24.437 -2.672 26.837 1.00 24.60 ? 497 ASN A C 1 ATOM 3968 O O . ASN A 1 497 ? 24.830 -1.728 26.154 1.00 24.70 ? 497 ASN A O 1 ATOM 3969 C CB . ASN A 1 497 ? 22.013 -2.158 27.272 1.00 23.59 ? 497 ASN A CB 1 ATOM 3970 C CG . ASN A 1 497 ? 20.640 -2.311 26.691 1.00 23.96 ? 497 ASN A CG 1 ATOM 3971 O OD1 . ASN A 1 497 ? 19.681 -2.619 27.393 1.00 23.34 ? 497 ASN A OD1 1 ATOM 3972 N ND2 . ASN A 1 497 ? 20.541 -2.138 25.377 1.00 24.60 ? 497 ASN A ND2 1 ATOM 3973 N N . ALA A 1 498 ? 25.230 -3.298 27.704 1.00 24.76 ? 498 ALA A N 1 ATOM 3974 C CA . ALA A 1 498 ? 26.620 -2.884 27.856 1.00 25.09 ? 498 ALA A CA 1 ATOM 3975 C C . ALA A 1 498 ? 27.534 -3.434 26.748 1.00 25.54 ? 498 ALA A C 1 ATOM 3976 O O . ALA A 1 498 ? 28.665 -2.976 26.598 1.00 25.70 ? 498 ALA A O 1 ATOM 3977 C CB . ALA A 1 498 ? 27.141 -3.254 29.231 1.00 25.01 ? 498 ALA A CB 1 ATOM 3978 N N . GLU A 1 499 ? 27.033 -4.392 25.964 1.00 25.86 ? 499 GLU A N 1 ATOM 3979 C CA . GLU A 1 499 ? 27.820 -5.045 24.915 1.00 26.05 ? 499 GLU A CA 1 ATOM 3980 C C . GLU A 1 499 ? 28.061 -4.129 23.714 1.00 27.01 ? 499 GLU A C 1 ATOM 3981 O O . GLU A 1 499 ? 27.164 -3.407 23.302 1.00 27.54 ? 499 GLU A O 1 ATOM 3982 C CB . GLU A 1 499 ? 27.157 -6.349 24.467 1.00 25.48 ? 499 GLU A CB 1 ATOM 3983 C CG . GLU A 1 499 ? 27.183 -7.441 25.530 1.00 24.17 ? 499 GLU A CG 1 ATOM 3984 C CD . GLU A 1 499 ? 26.669 -8.791 25.036 1.00 23.83 ? 499 GLU A CD 1 ATOM 3985 O OE1 . GLU A 1 499 ? 26.184 -8.874 23.887 1.00 24.06 ? 499 GLU A OE1 1 ATOM 3986 O OE2 . GLU A 1 499 ? 26.746 -9.780 25.804 1.00 22.94 ? 499 GLU A OE2 1 ATOM 3987 N N . PRO A 1 500 ? 29.280 -4.150 23.146 1.00 27.62 ? 500 PRO A N 1 ATOM 3988 C CA . PRO A 1 500 ? 29.469 -3.345 21.943 1.00 28.10 ? 500 PRO A CA 1 ATOM 3989 C C . PRO A 1 500 ? 28.565 -3.830 20.810 1.00 28.77 ? 500 PRO A C 1 ATOM 3990 O O . PRO A 1 500 ? 28.227 -5.002 20.750 1.00 28.97 ? 500 PRO A O 1 ATOM 3991 C CB . PRO A 1 500 ? 30.942 -3.565 21.595 1.00 28.29 ? 500 PRO A CB 1 ATOM 3992 C CG . PRO A 1 500 ? 31.318 -4.855 22.278 1.00 28.33 ? 500 PRO A CG 1 ATOM 3993 C CD . PRO A 1 500 ? 30.505 -4.869 23.538 1.00 27.40 ? 500 PRO A CD 1 ATOM 3994 N N . MET A 1 501 ? 28.184 -2.915 19.927 1.00 29.43 ? 501 MET A N 1 ATOM 3995 C CA . MET A 1 501 ? 27.271 -3.188 18.831 1.00 29.78 ? 501 MET A CA 1 ATOM 3996 C C . MET A 1 501 ? 27.855 -4.069 17.736 1.00 29.73 ? 501 MET A C 1 ATOM 3997 O O . MET A 1 501 ? 29.009 -3.922 17.359 1.00 29.86 ? 501 MET A O 1 ATOM 3998 C CB . MET A 1 501 ? 26.805 -1.864 18.228 1.00 30.18 ? 501 MET A CB 1 ATOM 3999 C CG . MET A 1 501 ? 25.780 -1.159 19.072 1.00 31.94 ? 501 MET A CG 1 ATOM 4000 S SD . MET A 1 501 ? 25.664 0.610 18.694 1.00 37.84 ? 501 MET A SD 1 ATOM 4001 C CE . MET A 1 501 ? 24.276 1.022 19.725 1.00 34.80 ? 501 MET A CE 1 ATOM 4002 N N . VAL A 1 502 ? 27.038 -4.987 17.231 1.00 30.21 ? 502 VAL A N 1 ATOM 4003 C CA . VAL A 1 502 ? 27.354 -5.729 16.023 1.00 30.79 ? 502 VAL A CA 1 ATOM 4004 C C . VAL A 1 502 ? 27.496 -4.771 14.815 1.00 31.85 ? 502 VAL A C 1 ATOM 4005 O O . VAL A 1 502 ? 27.004 -3.642 14.832 1.00 31.20 ? 502 VAL A O 1 ATOM 4006 C CB . VAL A 1 502 ? 26.292 -6.832 15.715 1.00 31.05 ? 502 VAL A CB 1 ATOM 4007 C CG1 . VAL A 1 502 ? 26.079 -7.766 16.911 1.00 29.81 ? 502 VAL A CG1 1 ATOM 4008 C CG2 . VAL A 1 502 ? 24.951 -6.220 15.228 1.00 30.40 ? 502 VAL A CG2 1 ATOM 4009 N N . GLU A 1 503 ? 28.194 -5.246 13.788 1.00 33.27 ? 503 GLU A N 1 ATOM 4010 C CA . GLU A 1 503 ? 28.441 -4.523 12.543 1.00 34.79 ? 503 GLU A CA 1 ATOM 4011 C C . GLU A 1 503 ? 27.126 -4.130 11.854 1.00 34.62 ? 503 GLU A C 1 ATOM 4012 O O . GLU A 1 503 ? 26.240 -4.966 11.692 1.00 34.80 ? 503 GLU A O 1 ATOM 4013 C CB . GLU A 1 503 ? 29.252 -5.440 11.625 1.00 35.47 ? 503 GLU A CB 1 ATOM 4014 C CG . GLU A 1 503 ? 30.390 -4.791 10.860 1.00 39.78 ? 503 GLU A CG 1 ATOM 4015 C CD . GLU A 1 503 ? 31.169 -5.828 10.042 1.00 45.65 ? 503 GLU A CD 1 ATOM 4016 O OE1 . GLU A 1 503 ? 31.997 -6.561 10.634 1.00 46.61 ? 503 GLU A OE1 1 ATOM 4017 O OE2 . GLU A 1 503 ? 30.935 -5.934 8.812 1.00 48.30 ? 503 GLU A OE2 1 ATOM 4018 N N . ARG A 1 504 ? 27.014 -2.855 11.469 1.00 34.75 ? 504 ARG A N 1 ATOM 4019 C CA . ARG A 1 504 ? 25.817 -2.268 10.809 1.00 34.94 ? 504 ARG A CA 1 ATOM 4020 C C . ARG A 1 504 ? 24.520 -2.356 11.643 1.00 34.06 ? 504 ARG A C 1 ATOM 4021 O O . ARG A 1 504 ? 23.421 -2.135 11.116 1.00 34.07 ? 504 ARG A O 1 ATOM 4022 C CB . ARG A 1 504 ? 25.598 -2.831 9.381 1.00 35.23 ? 504 ARG A CB 1 ATOM 4023 C CG . ARG A 1 504 ? 26.880 -2.972 8.527 1.00 38.19 ? 504 ARG A CG 1 ATOM 4024 C CD . ARG A 1 504 ? 26.960 -2.020 7.320 1.00 43.81 ? 504 ARG A CD 1 ATOM 4025 N NE . ARG A 1 504 ? 27.112 -0.595 7.656 1.00 47.31 ? 504 ARG A NE 1 ATOM 4026 C CZ . ARG A 1 504 ? 27.382 0.367 6.768 1.00 48.42 ? 504 ARG A CZ 1 ATOM 4027 N NH1 . ARG A 1 504 ? 27.558 0.065 5.487 1.00 49.94 ? 504 ARG A NH1 1 ATOM 4028 N NH2 . ARG A 1 504 ? 27.496 1.631 7.158 1.00 48.09 ? 504 ARG A NH2 1 ATOM 4029 N N . GLY A 1 505 ? 24.655 -2.666 12.936 1.00 32.91 ? 505 GLY A N 1 ATOM 4030 C CA . GLY A 1 505 ? 23.499 -2.837 13.833 1.00 31.71 ? 505 GLY A CA 1 ATOM 4031 C C . GLY A 1 505 ? 23.479 -1.829 14.961 1.00 30.91 ? 505 GLY A C 1 ATOM 4032 O O . GLY A 1 505 ? 24.316 -0.926 14.999 1.00 30.71 ? 505 GLY A O 1 ATOM 4033 N N . ARG A 1 506 ? 22.532 -1.977 15.887 1.00 30.13 ? 506 ARG A N 1 ATOM 4034 C CA . ARG A 1 506 ? 22.424 -1.047 17.026 1.00 29.12 ? 506 ARG A CA 1 ATOM 4035 C C . ARG A 1 506 ? 22.226 -1.750 18.375 1.00 28.49 ? 506 ARG A C 1 ATOM 4036 O O . ARG A 1 506 ? 21.892 -1.118 19.395 1.00 28.20 ? 506 ARG A O 1 ATOM 4037 C CB . ARG A 1 506 ? 21.345 0.015 16.772 1.00 29.20 ? 506 ARG A CB 1 ATOM 4038 C CG . ARG A 1 506 ? 21.714 1.071 15.706 1.00 29.91 ? 506 ARG A CG 1 ATOM 4039 C CD . ARG A 1 506 ? 22.901 1.932 16.147 1.00 30.11 ? 506 ARG A CD 1 ATOM 4040 N NE . ARG A 1 506 ? 23.231 2.968 15.170 1.00 30.81 ? 506 ARG A NE 1 ATOM 4041 C CZ . ARG A 1 506 ? 24.093 2.826 14.164 1.00 30.18 ? 506 ARG A CZ 1 ATOM 4042 N NH1 . ARG A 1 506 ? 24.735 1.687 13.968 1.00 30.78 ? 506 ARG A NH1 1 ATOM 4043 N NH2 . ARG A 1 506 ? 24.310 3.833 13.343 1.00 30.29 ? 506 ARG A NH2 1 ATOM 4044 N N . VAL A 1 507 ? 22.449 -3.064 18.366 1.00 27.39 ? 507 VAL A N 1 ATOM 4045 C CA . VAL A 1 507 ? 22.528 -3.866 19.583 1.00 26.50 ? 507 VAL A CA 1 ATOM 4046 C C . VAL A 1 507 ? 23.721 -4.809 19.487 1.00 25.94 ? 507 VAL A C 1 ATOM 4047 O O . VAL A 1 507 ? 24.241 -5.031 18.407 1.00 25.26 ? 507 VAL A O 1 ATOM 4048 C CB . VAL A 1 507 ? 21.234 -4.687 19.822 1.00 26.54 ? 507 VAL A CB 1 ATOM 4049 C CG1 . VAL A 1 507 ? 20.022 -3.769 20.005 1.00 26.67 ? 507 VAL A CG1 1 ATOM 4050 C CG2 . VAL A 1 507 ? 20.996 -5.695 18.688 1.00 25.76 ? 507 VAL A CG2 1 ATOM 4051 N N . GLY A 1 508 ? 24.135 -5.375 20.616 1.00 26.09 ? 508 GLY A N 1 ATOM 4052 C CA . GLY A 1 508 ? 25.203 -6.381 20.640 1.00 26.28 ? 508 GLY A CA 1 ATOM 4053 C C . GLY A 1 508 ? 24.742 -7.800 20.313 1.00 26.71 ? 508 GLY A C 1 ATOM 4054 O O . GLY A 1 508 ? 23.586 -8.018 19.919 1.00 25.97 ? 508 GLY A O 1 ATOM 4055 N N . PRO A 1 509 ? 25.658 -8.778 20.463 1.00 27.06 ? 509 PRO A N 1 ATOM 4056 C CA . PRO A 1 509 ? 25.419 -10.198 20.155 1.00 27.13 ? 509 PRO A CA 1 ATOM 4057 C C . PRO A 1 509 ? 24.293 -10.840 20.984 1.00 27.43 ? 509 PRO A C 1 ATOM 4058 O O . PRO A 1 509 ? 23.435 -11.548 20.428 1.00 27.67 ? 509 PRO A O 1 ATOM 4059 C CB . PRO A 1 509 ? 26.770 -10.871 20.476 1.00 27.19 ? 509 PRO A CB 1 ATOM 4060 C CG . PRO A 1 509 ? 27.780 -9.755 20.537 1.00 26.86 ? 509 PRO A CG 1 ATOM 4061 C CD . PRO A 1 509 ? 27.031 -8.532 20.952 1.00 27.06 ? 509 PRO A CD 1 ATOM 4062 N N . LEU A 1 510 ? 24.296 -10.613 22.297 1.00 27.43 ? 510 LEU A N 1 ATOM 4063 C CA . LEU A 1 510 ? 23.265 -11.202 23.150 1.00 27.49 ? 510 LEU A CA 1 ATOM 4064 C C . LEU A 1 510 ? 21.896 -10.647 22.799 1.00 27.41 ? 510 LEU A C 1 ATOM 4065 O O . LEU A 1 510 ? 20.948 -11.409 22.641 1.00 28.37 ? 510 LEU A O 1 ATOM 4066 C CB . LEU A 1 510 ? 23.555 -11.026 24.645 1.00 27.33 ? 510 LEU A CB 1 ATOM 4067 C CG . LEU A 1 510 ? 22.469 -11.523 25.617 1.00 27.44 ? 510 LEU A CG 1 ATOM 4068 C CD1 . LEU A 1 510 ? 22.166 -13.014 25.443 1.00 27.54 ? 510 LEU A CD1 1 ATOM 4069 C CD2 . LEU A 1 510 ? 22.851 -11.234 27.061 1.00 25.87 ? 510 LEU A CD2 1 ATOM 4070 N N . LEU A 1 511 ? 21.800 -9.333 22.658 1.00 26.91 ? 511 LEU A N 1 ATOM 4071 C CA . LEU A 1 511 ? 20.544 -8.691 22.275 1.00 26.17 ? 511 LEU A CA 1 ATOM 4072 C C . LEU A 1 511 ? 20.031 -9.100 20.886 1.00 25.98 ? 511 LEU A C 1 ATOM 4073 O O . LEU A 1 511 ? 18.838 -9.311 20.703 1.00 25.86 ? 511 LEU A O 1 ATOM 4074 C CB . LEU A 1 511 ? 20.672 -7.177 22.396 1.00 25.57 ? 511 LEU A CB 1 ATOM 4075 C CG . LEU A 1 511 ? 19.974 -6.467 23.561 1.00 25.55 ? 511 LEU A CG 1 ATOM 4076 C CD1 . LEU A 1 511 ? 19.901 -7.272 24.846 1.00 25.01 ? 511 LEU A CD1 1 ATOM 4077 C CD2 . LEU A 1 511 ? 20.638 -5.137 23.825 1.00 25.12 ? 511 LEU A CD2 1 ATOM 4078 N N . ALA A 1 512 ? 20.939 -9.231 19.923 1.00 25.93 ? 512 ALA A N 1 ATOM 4079 C CA . ALA A 1 512 ? 20.583 -9.653 18.565 1.00 25.54 ? 512 ALA A CA 1 ATOM 4080 C C . ALA A 1 512 ? 19.951 -11.040 18.552 1.00 25.62 ? 512 ALA A C 1 ATOM 4081 O O . ALA A 1 512 ? 19.014 -11.290 17.806 1.00 25.43 ? 512 ALA A O 1 ATOM 4082 C CB . ALA A 1 512 ? 21.796 -9.616 17.657 1.00 25.18 ? 512 ALA A CB 1 ATOM 4083 N N . CYS A 1 513 ? 20.475 -11.929 19.394 1.00 25.99 ? 513 CYS A N 1 ATOM 4084 C CA . CYS A 1 513 ? 19.941 -13.275 19.552 1.00 26.08 ? 513 CYS A CA 1 ATOM 4085 C C . CYS A 1 513 ? 18.536 -13.294 20.159 1.00 25.88 ? 513 CYS A C 1 ATOM 4086 O O . CYS A 1 513 ? 17.629 -13.913 19.614 1.00 25.96 ? 513 CYS A O 1 ATOM 4087 C CB . CYS A 1 513 ? 20.917 -14.121 20.374 1.00 26.28 ? 513 CYS A CB 1 ATOM 4088 S SG . CYS A 1 513 ? 20.240 -15.626 21.131 1.00 26.93 ? 513 CYS A SG 1 ATOM 4089 N N . LEU A 1 514 ? 18.367 -12.608 21.281 1.00 26.15 ? 514 LEU A N 1 ATOM 4090 C CA . LEU A 1 514 ? 17.073 -12.511 21.965 1.00 26.40 ? 514 LEU A CA 1 ATOM 4091 C C . LEU A 1 514 ? 15.991 -11.869 21.080 1.00 26.36 ? 514 LEU A C 1 ATOM 4092 O O . LEU A 1 514 ? 14.941 -12.463 20.874 1.00 26.41 ? 514 LEU A O 1 ATOM 4093 C CB . LEU A 1 514 ? 17.227 -11.787 23.307 1.00 26.18 ? 514 LEU A CB 1 ATOM 4094 C CG . LEU A 1 514 ? 18.103 -12.552 24.312 1.00 26.95 ? 514 LEU A CG 1 ATOM 4095 C CD1 . LEU A 1 514 ? 18.292 -11.786 25.611 1.00 27.70 ? 514 LEU A CD1 1 ATOM 4096 C CD2 . LEU A 1 514 ? 17.526 -13.926 24.601 1.00 27.02 ? 514 LEU A CD2 1 ATOM 4097 N N . LEU A 1 515 ? 16.280 -10.699 20.519 1.00 26.42 ? 515 LEU A N 1 ATOM 4098 C CA . LEU A 1 515 ? 15.359 -10.018 19.610 1.00 26.75 ? 515 LEU A CA 1 ATOM 4099 C C . LEU A 1 515 ? 15.108 -10.821 18.340 1.00 26.88 ? 515 LEU A C 1 ATOM 4100 O O . LEU A 1 515 ? 13.962 -11.062 17.971 1.00 26.97 ? 515 LEU A O 1 ATOM 4101 C CB . LEU A 1 515 ? 15.901 -8.639 19.232 1.00 26.87 ? 515 LEU A CB 1 ATOM 4102 C CG . LEU A 1 515 ? 16.055 -7.591 20.339 1.00 27.57 ? 515 LEU A CG 1 ATOM 4103 C CD1 . LEU A 1 515 ? 16.913 -6.422 19.851 1.00 27.51 ? 515 LEU A CD1 1 ATOM 4104 C CD2 . LEU A 1 515 ? 14.679 -7.115 20.819 1.00 28.25 ? 515 LEU A CD2 1 ATOM 4105 N N . GLY A 1 516 ? 16.190 -11.223 17.677 1.00 27.20 ? 516 GLY A N 1 ATOM 4106 C CA . GLY A 1 516 ? 16.120 -12.020 16.454 1.00 27.46 ? 516 GLY A CA 1 ATOM 4107 C C . GLY A 1 516 ? 15.263 -13.259 16.583 1.00 27.86 ? 516 GLY A C 1 ATOM 4108 O O . GLY A 1 516 ? 14.394 -13.487 15.753 1.00 27.61 ? 516 GLY A O 1 ATOM 4109 N N . ARG A 1 517 ? 15.504 -14.051 17.629 1.00 28.68 ? 517 ARG A N 1 ATOM 4110 C CA . ARG A 1 517 ? 14.671 -15.216 17.940 1.00 29.87 ? 517 ARG A CA 1 ATOM 4111 C C . ARG A 1 517 ? 13.193 -14.873 18.043 1.00 29.82 ? 517 ARG A C 1 ATOM 4112 O O . ARG A 1 517 ? 12.376 -15.519 17.395 1.00 29.53 ? 517 ARG A O 1 ATOM 4113 C CB . ARG A 1 517 ? 15.095 -15.868 19.245 1.00 30.36 ? 517 ARG A CB 1 ATOM 4114 C CG . ARG A 1 517 ? 16.118 -16.950 19.098 1.00 33.60 ? 517 ARG A CG 1 ATOM 4115 C CD . ARG A 1 517 ? 16.206 -17.752 20.402 1.00 38.12 ? 517 ARG A CD 1 ATOM 4116 N NE . ARG A 1 517 ? 17.544 -18.310 20.593 1.00 41.77 ? 517 ARG A NE 1 ATOM 4117 C CZ . ARG A 1 517 ? 17.866 -19.588 20.406 1.00 44.06 ? 517 ARG A CZ 1 ATOM 4118 N NH1 . ARG A 1 517 ? 16.940 -20.468 20.018 1.00 44.41 ? 517 ARG A NH1 1 ATOM 4119 N NH2 . ARG A 1 517 ? 19.121 -19.984 20.617 1.00 44.97 ? 517 ARG A NH2 1 ATOM 4120 N N . GLN A 1 518 ? 12.865 -13.867 18.863 1.00 29.81 ? 518 GLN A N 1 ATOM 4121 C CA . GLN A 1 518 ? 11.477 -13.460 19.090 1.00 29.57 ? 518 GLN A CA 1 ATOM 4122 C C . GLN A 1 518 ? 10.780 -13.081 17.794 1.00 29.74 ? 518 GLN A C 1 ATOM 4123 O O . GLN A 1 518 ? 9.656 -13.522 17.540 1.00 29.41 ? 518 GLN A O 1 ATOM 4124 C CB . GLN A 1 518 ? 11.388 -12.290 20.068 1.00 29.55 ? 518 GLN A CB 1 ATOM 4125 C CG . GLN A 1 518 ? 9.968 -11.997 20.563 1.00 29.28 ? 518 GLN A CG 1 ATOM 4126 C CD . GLN A 1 518 ? 9.405 -13.112 21.428 1.00 30.22 ? 518 GLN A CD 1 ATOM 4127 O OE1 . GLN A 1 518 ? 9.770 -13.260 22.596 1.00 29.90 ? 518 GLN A OE1 1 ATOM 4128 N NE2 . GLN A 1 518 ? 8.504 -13.903 20.856 1.00 30.14 ? 518 GLN A NE2 1 ATOM 4129 N N . PHE A 1 519 ? 11.455 -12.270 16.982 1.00 29.64 ? 519 PHE A N 1 ATOM 4130 C CA . PHE A 1 519 ? 10.866 -11.785 15.738 1.00 30.13 ? 519 PHE A CA 1 ATOM 4131 C C . PHE A 1 519 ? 10.629 -12.887 14.703 1.00 30.46 ? 519 PHE A C 1 ATOM 4132 O O . PHE A 1 519 ? 9.575 -12.924 14.066 1.00 30.27 ? 519 PHE A O 1 ATOM 4133 C CB . PHE A 1 519 ? 11.678 -10.633 15.160 1.00 29.62 ? 519 PHE A CB 1 ATOM 4134 C CG . PHE A 1 519 ? 11.375 -9.307 15.801 1.00 29.95 ? 519 PHE A CG 1 ATOM 4135 C CD1 . PHE A 1 519 ? 10.158 -8.656 15.547 1.00 28.77 ? 519 PHE A CD1 1 ATOM 4136 C CD2 . PHE A 1 519 ? 12.300 -8.703 16.666 1.00 29.07 ? 519 PHE A CD2 1 ATOM 4137 C CE1 . PHE A 1 519 ? 9.874 -7.426 16.140 1.00 28.34 ? 519 PHE A CE1 1 ATOM 4138 C CE2 . PHE A 1 519 ? 12.020 -7.471 17.266 1.00 28.07 ? 519 PHE A CE2 1 ATOM 4139 C CZ . PHE A 1 519 ? 10.809 -6.830 16.996 1.00 28.41 ? 519 PHE A CZ 1 ATOM 4140 N N . GLN A 1 520 ? 11.610 -13.782 14.563 1.00 30.89 ? 520 GLN A N 1 ATOM 4141 C CA . GLN A 1 520 ? 11.490 -14.964 13.716 1.00 31.26 ? 520 GLN A CA 1 ATOM 4142 C C . GLN A 1 520 ? 10.241 -15.740 14.091 1.00 31.26 ? 520 GLN A C 1 ATOM 4143 O O . GLN A 1 520 ? 9.454 -16.120 13.228 1.00 31.33 ? 520 GLN A O 1 ATOM 4144 C CB . GLN A 1 520 ? 12.728 -15.853 13.864 1.00 31.38 ? 520 GLN A CB 1 ATOM 4145 C CG . GLN A 1 520 ? 12.678 -17.169 13.062 1.00 32.58 ? 520 GLN A CG 1 ATOM 4146 C CD . GLN A 1 520 ? 12.237 -18.368 13.900 1.00 33.73 ? 520 GLN A CD 1 ATOM 4147 O OE1 . GLN A 1 520 ? 11.311 -19.089 13.521 1.00 34.96 ? 520 GLN A OE1 1 ATOM 4148 N NE2 . GLN A 1 520 ? 12.894 -18.581 15.048 1.00 33.33 ? 520 GLN A NE2 1 ATOM 4149 N N . GLN A 1 521 ? 10.063 -15.947 15.390 1.00 31.15 ? 521 GLN A N 1 ATOM 4150 C CA . GLN A 1 521 ? 8.931 -16.681 15.908 1.00 31.41 ? 521 GLN A CA 1 ATOM 4151 C C . GLN A 1 521 ? 7.592 -15.993 15.644 1.00 31.62 ? 521 GLN A C 1 ATOM 4152 O O . GLN A 1 521 ? 6.639 -16.646 15.208 1.00 31.60 ? 521 GLN A O 1 ATOM 4153 C CB . GLN A 1 521 ? 9.113 -16.939 17.396 1.00 31.45 ? 521 GLN A CB 1 ATOM 4154 C CG . GLN A 1 521 ? 10.093 -18.047 17.716 1.00 32.51 ? 521 GLN A CG 1 ATOM 4155 C CD . GLN A 1 521 ? 10.216 -18.278 19.209 1.00 35.57 ? 521 GLN A CD 1 ATOM 4156 O OE1 . GLN A 1 521 ? 9.286 -17.994 19.978 1.00 36.92 ? 521 GLN A OE1 1 ATOM 4157 N NE2 . GLN A 1 521 ? 11.371 -18.782 19.636 1.00 35.87 ? 521 GLN A NE2 1 ATOM 4158 N N . ILE A 1 522 ? 7.510 -14.686 15.899 1.00 31.79 ? 522 ILE A N 1 ATOM 4159 C CA . ILE A 1 522 ? 6.232 -13.983 15.722 1.00 32.21 ? 522 ILE A CA 1 ATOM 4160 C C . ILE A 1 522 ? 5.847 -13.828 14.256 1.00 31.81 ? 522 ILE A C 1 ATOM 4161 O O . ILE A 1 522 ? 4.676 -13.641 13.950 1.00 31.99 ? 522 ILE A O 1 ATOM 4162 C CB . ILE A 1 522 ? 6.128 -12.612 16.465 1.00 32.41 ? 522 ILE A CB 1 ATOM 4163 C CG1 . ILE A 1 522 ? 7.135 -11.610 15.921 1.00 33.56 ? 522 ILE A CG1 1 ATOM 4164 C CG2 . ILE A 1 522 ? 6.263 -12.791 17.967 1.00 32.66 ? 522 ILE A CG2 1 ATOM 4165 C CD1 . ILE A 1 522 ? 6.901 -10.228 16.419 1.00 36.97 ? 522 ILE A CD1 1 ATOM 4166 N N . ARG A 1 523 ? 6.826 -13.911 13.360 1.00 31.62 ? 523 ARG A N 1 ATOM 4167 C CA . ARG A 1 523 ? 6.524 -13.947 11.938 1.00 31.40 ? 523 ARG A CA 1 ATOM 4168 C C . ARG A 1 523 ? 6.117 -15.355 11.492 1.00 31.35 ? 523 ARG A C 1 ATOM 4169 O O . ARG A 1 523 ? 5.082 -15.516 10.838 1.00 32.24 ? 523 ARG A O 1 ATOM 4170 C CB . ARG A 1 523 ? 7.677 -13.403 11.106 1.00 31.18 ? 523 ARG A CB 1 ATOM 4171 C CG . ARG A 1 523 ? 7.573 -13.730 9.617 1.00 31.86 ? 523 ARG A CG 1 ATOM 4172 C CD . ARG A 1 523 ? 8.675 -14.703 9.216 1.00 32.23 ? 523 ARG A CD 1 ATOM 4173 N NE . ARG A 1 523 ? 9.723 -14.041 8.450 1.00 29.56 ? 523 ARG A NE 1 ATOM 4174 C CZ . ARG A 1 523 ? 10.921 -14.553 8.213 1.00 29.31 ? 523 ARG A CZ 1 ATOM 4175 N NH1 . ARG A 1 523 ? 11.264 -15.739 8.696 1.00 27.45 ? 523 ARG A NH1 1 ATOM 4176 N NH2 . ARG A 1 523 ? 11.787 -13.860 7.485 1.00 30.84 ? 523 ARG A NH2 1 ATOM 4177 N N . ASP A 1 524 ? 6.906 -16.360 11.873 1.00 30.48 ? 524 ASP A N 1 ATOM 4178 C CA . ASP A 1 524 ? 6.689 -17.749 11.459 1.00 29.93 ? 524 ASP A CA 1 ATOM 4179 C C . ASP A 1 524 ? 5.454 -18.392 12.093 1.00 30.21 ? 524 ASP A C 1 ATOM 4180 O O . ASP A 1 524 ? 4.883 -19.331 11.532 1.00 30.12 ? 524 ASP A O 1 ATOM 4181 C CB . ASP A 1 524 ? 7.948 -18.606 11.721 1.00 29.37 ? 524 ASP A CB 1 ATOM 4182 C CG . ASP A 1 524 ? 9.083 -18.312 10.731 1.00 29.00 ? 524 ASP A CG 1 ATOM 4183 O OD1 . ASP A 1 524 ? 8.856 -17.567 9.749 1.00 29.76 ? 524 ASP A OD1 1 ATOM 4184 O OD2 . ASP A 1 524 ? 10.212 -18.810 10.922 1.00 27.91 ? 524 ASP A OD2 1 ATOM 4185 N N . GLY A 1 525 ? 5.039 -17.885 13.253 1.00 30.50 ? 525 GLY A N 1 ATOM 4186 C CA . GLY A 1 525 ? 3.901 -18.444 13.979 1.00 30.33 ? 525 GLY A CA 1 ATOM 4187 C C . GLY A 1 525 ? 2.594 -17.711 13.746 1.00 30.68 ? 525 GLY A C 1 ATOM 4188 O O . GLY A 1 525 ? 1.596 -18.005 14.406 1.00 30.72 ? 525 GLY A O 1 ATOM 4189 N N . ASP A 1 526 ? 2.593 -16.779 12.790 1.00 31.15 ? 526 ASP A N 1 ATOM 4190 C CA . ASP A 1 526 ? 1.439 -15.917 12.503 1.00 31.49 ? 526 ASP A CA 1 ATOM 4191 C C . ASP A 1 526 ? 0.665 -16.372 11.270 1.00 31.84 ? 526 ASP A C 1 ATOM 4192 O O . ASP A 1 526 ? 1.082 -16.128 10.128 1.00 31.88 ? 526 ASP A O 1 ATOM 4193 C CB . ASP A 1 526 ? 1.911 -14.469 12.311 1.00 31.60 ? 526 ASP A CB 1 ATOM 4194 C CG . ASP A 1 526 ? 0.765 -13.449 12.280 1.00 32.11 ? 526 ASP A CG 1 ATOM 4195 O OD1 . ASP A 1 526 ? -0.412 -13.793 12.557 1.00 32.55 ? 526 ASP A OD1 1 ATOM 4196 O OD2 . ASP A 1 526 ? 1.063 -12.270 11.992 1.00 32.40 ? 526 ASP A OD2 1 ATOM 4197 N N . ARG A 1 527 ? -0.486 -17.001 11.502 1.00 32.26 ? 527 ARG A N 1 ATOM 4198 C CA . ARG A 1 527 ? -1.353 -17.448 10.404 1.00 32.68 ? 527 ARG A CA 1 ATOM 4199 C C . ARG A 1 527 ? -1.759 -16.289 9.480 1.00 32.94 ? 527 ARG A C 1 ATOM 4200 O O . ARG A 1 527 ? -2.138 -16.505 8.325 1.00 33.22 ? 527 ARG A O 1 ATOM 4201 C CB . ARG A 1 527 ? -2.590 -18.186 10.942 1.00 32.38 ? 527 ARG A CB 1 ATOM 4202 C CG . ARG A 1 527 ? -3.447 -18.817 9.855 1.00 32.08 ? 527 ARG A CG 1 ATOM 4203 C CD . ARG A 1 527 ? -4.361 -19.901 10.383 1.00 31.93 ? 527 ARG A CD 1 ATOM 4204 N NE . ARG A 1 527 ? -5.385 -19.397 11.304 1.00 32.42 ? 527 ARG A NE 1 ATOM 4205 C CZ . ARG A 1 527 ? -6.550 -18.871 10.926 1.00 32.06 ? 527 ARG A CZ 1 ATOM 4206 N NH1 . ARG A 1 527 ? -6.844 -18.762 9.635 1.00 31.61 ? 527 ARG A NH1 1 ATOM 4207 N NH2 . ARG A 1 527 ? -7.422 -18.448 11.840 1.00 31.40 ? 527 ARG A NH2 1 ATOM 4208 N N . PHE A 1 528 ? -1.654 -15.065 9.990 1.00 33.16 ? 528 PHE A N 1 ATOM 4209 C CA . PHE A 1 528 ? -2.068 -13.884 9.239 1.00 33.64 ? 528 PHE A CA 1 ATOM 4210 C C . PHE A 1 528 ? -0.912 -13.010 8.782 1.00 33.89 ? 528 PHE A C 1 ATOM 4211 O O . PHE A 1 528 ? -1.114 -11.862 8.383 1.00 34.30 ? 528 PHE A O 1 ATOM 4212 C CB . PHE A 1 528 ? -3.120 -13.084 10.022 1.00 33.35 ? 528 PHE A CB 1 ATOM 4213 C CG . PHE A 1 528 ? -4.451 -13.774 10.091 1.00 33.76 ? 528 PHE A CG 1 ATOM 4214 C CD1 . PHE A 1 528 ? -4.895 -14.347 11.281 1.00 33.57 ? 528 PHE A CD1 1 ATOM 4215 C CD2 . PHE A 1 528 ? -5.244 -13.897 8.945 1.00 33.12 ? 528 PHE A CD2 1 ATOM 4216 C CE1 . PHE A 1 528 ? -6.125 -15.008 11.333 1.00 34.10 ? 528 PHE A CE1 1 ATOM 4217 C CE2 . PHE A 1 528 ? -6.466 -14.550 8.987 1.00 33.14 ? 528 PHE A CE2 1 ATOM 4218 C CZ . PHE A 1 528 ? -6.910 -15.108 10.182 1.00 33.43 ? 528 PHE A CZ 1 ATOM 4219 N N . TRP A 1 529 ? 0.300 -13.554 8.813 1.00 34.34 ? 529 TRP A N 1 ATOM 4220 C CA . TRP A 1 529 ? 1.436 -12.845 8.247 1.00 34.66 ? 529 TRP A CA 1 ATOM 4221 C C . TRP A 1 529 ? 1.095 -12.470 6.807 1.00 35.14 ? 529 TRP A C 1 ATOM 4222 O O . TRP A 1 529 ? 0.433 -13.230 6.104 1.00 35.39 ? 529 TRP A O 1 ATOM 4223 C CB . TRP A 1 529 ? 2.696 -13.702 8.301 1.00 34.43 ? 529 TRP A CB 1 ATOM 4224 C CG . TRP A 1 529 ? 3.937 -12.972 7.852 1.00 34.44 ? 529 TRP A CG 1 ATOM 4225 C CD1 . TRP A 1 529 ? 4.619 -13.161 6.682 1.00 34.25 ? 529 TRP A CD1 1 ATOM 4226 C CD2 . TRP A 1 529 ? 4.633 -11.935 8.561 1.00 33.21 ? 529 TRP A CD2 1 ATOM 4227 N NE1 . TRP A 1 529 ? 5.704 -12.315 6.625 1.00 35.27 ? 529 TRP A NE1 1 ATOM 4228 C CE2 . TRP A 1 529 ? 5.731 -11.545 7.759 1.00 34.12 ? 529 TRP A CE2 1 ATOM 4229 C CE3 . TRP A 1 529 ? 4.441 -11.305 9.797 1.00 33.18 ? 529 TRP A CE3 1 ATOM 4230 C CZ2 . TRP A 1 529 ? 6.643 -10.549 8.157 1.00 34.50 ? 529 TRP A CZ2 1 ATOM 4231 C CZ3 . TRP A 1 529 ? 5.347 -10.307 10.195 1.00 33.57 ? 529 TRP A CZ3 1 ATOM 4232 C CH2 . TRP A 1 529 ? 6.436 -9.947 9.376 1.00 33.66 ? 529 TRP A CH2 1 ATOM 4233 N N . TRP A 1 530 ? 1.544 -11.298 6.376 1.00 35.78 ? 530 TRP A N 1 ATOM 4234 C CA . TRP A 1 530 ? 1.096 -10.713 5.108 1.00 36.23 ? 530 TRP A CA 1 ATOM 4235 C C . TRP A 1 530 ? 1.516 -11.528 3.866 1.00 36.45 ? 530 TRP A C 1 ATOM 4236 O O . TRP A 1 530 ? 0.772 -11.587 2.873 1.00 36.47 ? 530 TRP A O 1 ATOM 4237 C CB . TRP A 1 530 ? 1.545 -9.246 5.016 1.00 36.18 ? 530 TRP A CB 1 ATOM 4238 C CG . TRP A 1 530 ? 2.997 -9.078 4.725 1.00 36.08 ? 530 TRP A CG 1 ATOM 4239 C CD1 . TRP A 1 530 ? 4.035 -9.152 5.616 1.00 36.19 ? 530 TRP A CD1 1 ATOM 4240 C CD2 . TRP A 1 530 ? 3.580 -8.809 3.447 1.00 36.03 ? 530 TRP A CD2 1 ATOM 4241 N NE1 . TRP A 1 530 ? 5.233 -8.946 4.967 1.00 35.75 ? 530 TRP A NE1 1 ATOM 4242 C CE2 . TRP A 1 530 ? 4.985 -8.733 3.635 1.00 35.56 ? 530 TRP A CE2 1 ATOM 4243 C CE3 . TRP A 1 530 ? 3.056 -8.633 2.156 1.00 34.96 ? 530 TRP A CE3 1 ATOM 4244 C CZ2 . TRP A 1 530 ? 5.871 -8.489 2.578 1.00 34.77 ? 530 TRP A CZ2 1 ATOM 4245 C CZ3 . TRP A 1 530 ? 3.944 -8.396 1.101 1.00 35.24 ? 530 TRP A CZ3 1 ATOM 4246 C CH2 . TRP A 1 530 ? 5.334 -8.322 1.322 1.00 34.84 ? 530 TRP A CH2 1 ATOM 4247 N N . GLU A 1 531 ? 2.693 -12.154 3.932 1.00 36.49 ? 531 GLU A N 1 ATOM 4248 C CA . GLU A 1 531 ? 3.196 -12.983 2.832 1.00 36.64 ? 531 GLU A CA 1 ATOM 4249 C C . GLU A 1 531 ? 2.637 -14.400 2.864 1.00 36.30 ? 531 GLU A C 1 ATOM 4250 O O . GLU A 1 531 ? 2.813 -15.146 1.904 1.00 36.69 ? 531 GLU A O 1 ATOM 4251 C CB . GLU A 1 531 ? 4.718 -13.082 2.838 1.00 36.73 ? 531 GLU A CB 1 ATOM 4252 C CG . GLU A 1 531 ? 5.451 -11.805 3.065 1.00 38.16 ? 531 GLU A CG 1 ATOM 4253 C CD . GLU A 1 531 ? 6.930 -12.038 3.332 1.00 40.87 ? 531 GLU A CD 1 ATOM 4254 O OE1 . GLU A 1 531 ? 7.325 -12.056 4.526 1.00 40.72 ? 531 GLU A OE1 1 ATOM 4255 O OE2 . GLU A 1 531 ? 7.690 -12.220 2.349 1.00 41.59 ? 531 GLU A OE2 1 ATOM 4256 N N . ASN A 1 532 ? 1.986 -14.778 3.960 1.00 35.84 ? 532 ASN A N 1 ATOM 4257 C CA . ASN A 1 532 ? 1.370 -16.100 4.060 1.00 35.62 ? 532 ASN A CA 1 ATOM 4258 C C . ASN A 1 532 ? 0.379 -16.330 2.912 1.00 35.44 ? 532 ASN A C 1 ATOM 4259 O O . ASN A 1 532 ? -0.624 -15.623 2.812 1.00 35.36 ? 532 ASN A O 1 ATOM 4260 C CB . ASN A 1 532 ? 0.680 -16.279 5.416 1.00 35.33 ? 532 ASN A CB 1 ATOM 4261 C CG . ASN A 1 532 ? 0.168 -17.693 5.633 1.00 35.89 ? 532 ASN A CG 1 ATOM 4262 O OD1 . ASN A 1 532 ? 0.727 -18.663 5.097 1.00 34.88 ? 532 ASN A OD1 1 ATOM 4263 N ND2 . ASN A 1 532 ? -0.892 -17.822 6.436 1.00 34.89 ? 532 ASN A ND2 1 ATOM 4264 N N . PRO A 1 533 ? 0.671 -17.305 2.026 1.00 35.44 ? 533 PRO A N 1 ATOM 4265 C CA . PRO A 1 533 ? -0.175 -17.477 0.850 1.00 35.28 ? 533 PRO A CA 1 ATOM 4266 C C . PRO A 1 533 ? -1.653 -17.597 1.222 1.00 35.25 ? 533 PRO A C 1 ATOM 4267 O O . PRO A 1 533 ? -2.002 -18.410 2.082 1.00 35.29 ? 533 PRO A O 1 ATOM 4268 C CB . PRO A 1 533 ? 0.350 -18.779 0.237 1.00 35.29 ? 533 PRO A CB 1 ATOM 4269 C CG . PRO A 1 533 ? 1.796 -18.837 0.661 1.00 34.99 ? 533 PRO A CG 1 ATOM 4270 C CD . PRO A 1 533 ? 1.786 -18.279 2.053 1.00 35.46 ? 533 PRO A CD 1 ATOM 4271 N N . GLY A 1 534 ? -2.497 -16.767 0.606 1.00 34.94 ? 534 GLY A N 1 ATOM 4272 C CA . GLY A 1 534 ? -3.938 -16.838 0.810 1.00 35.17 ? 534 GLY A CA 1 ATOM 4273 C C . GLY A 1 534 ? -4.511 -15.805 1.764 1.00 35.62 ? 534 GLY A C 1 ATOM 4274 O O . GLY A 1 534 ? -5.731 -15.722 1.920 1.00 35.83 ? 534 GLY A O 1 ATOM 4275 N N . VAL A 1 535 ? -3.643 -15.026 2.411 1.00 35.52 ? 535 VAL A N 1 ATOM 4276 C CA . VAL A 1 535 ? -4.079 -13.932 3.274 1.00 35.43 ? 535 VAL A CA 1 ATOM 4277 C C . VAL A 1 535 ? -4.333 -12.660 2.462 1.00 35.85 ? 535 VAL A C 1 ATOM 4278 O O . VAL A 1 535 ? -5.334 -11.977 2.673 1.00 35.57 ? 535 VAL A O 1 ATOM 4279 C CB . VAL A 1 535 ? -3.072 -13.664 4.396 1.00 35.35 ? 535 VAL A CB 1 ATOM 4280 C CG1 . VAL A 1 535 ? -3.360 -12.325 5.077 1.00 34.89 ? 535 VAL A CG1 1 ATOM 4281 C CG2 . VAL A 1 535 ? -3.131 -14.791 5.408 1.00 35.51 ? 535 VAL A CG2 1 ATOM 4282 N N . PHE A 1 536 ? -3.409 -12.331 1.561 1.00 36.36 ? 536 PHE A N 1 ATOM 4283 C CA . PHE A 1 536 ? -3.660 -11.328 0.527 1.00 37.04 ? 536 PHE A CA 1 ATOM 4284 C C . PHE A 1 536 ? -3.480 -12.004 -0.830 1.00 37.51 ? 536 PHE A C 1 ATOM 4285 O O . PHE A 1 536 ? -2.739 -12.981 -0.937 1.00 37.31 ? 536 PHE A O 1 ATOM 4286 C CB . PHE A 1 536 ? -2.688 -10.145 0.634 1.00 36.87 ? 536 PHE A CB 1 ATOM 4287 C CG . PHE A 1 536 ? -2.906 -9.258 1.834 1.00 36.52 ? 536 PHE A CG 1 ATOM 4288 C CD1 . PHE A 1 536 ? -2.038 -9.318 2.929 1.00 36.37 ? 536 PHE A CD1 1 ATOM 4289 C CD2 . PHE A 1 536 ? -3.941 -8.335 1.859 1.00 36.93 ? 536 PHE A CD2 1 ATOM 4290 C CE1 . PHE A 1 536 ? -2.215 -8.494 4.042 1.00 34.95 ? 536 PHE A CE1 1 ATOM 4291 C CE2 . PHE A 1 536 ? -4.127 -7.500 2.975 1.00 36.61 ? 536 PHE A CE2 1 ATOM 4292 C CZ . PHE A 1 536 ? -3.258 -7.591 4.069 1.00 35.52 ? 536 PHE A CZ 1 ATOM 4293 N N . THR A 1 537 ? -4.136 -11.484 -1.866 1.00 38.17 ? 537 THR A N 1 ATOM 4294 C CA . THR A 1 537 ? -3.880 -11.966 -3.232 1.00 38.98 ? 537 THR A CA 1 ATOM 4295 C C . THR A 1 537 ? -2.507 -11.484 -3.711 1.00 40.06 ? 537 THR A C 1 ATOM 4296 O O . THR A 1 537 ? -1.968 -10.509 -3.174 1.00 40.46 ? 537 THR A O 1 ATOM 4297 C CB . THR A 1 537 ? -4.970 -11.522 -4.243 1.00 38.62 ? 537 THR A CB 1 ATOM 4298 O OG1 . THR A 1 537 ? -4.810 -10.134 -4.557 1.00 38.47 ? 537 THR A OG1 1 ATOM 4299 C CG2 . THR A 1 537 ? -6.365 -11.753 -3.698 1.00 37.46 ? 537 THR A CG2 1 ATOM 4300 N N . GLU A 1 538 ? -1.945 -12.169 -4.710 1.00 41.23 ? 538 GLU A N 1 ATOM 4301 C CA . GLU A 1 538 ? -0.674 -11.775 -5.330 1.00 42.16 ? 538 GLU A CA 1 ATOM 4302 C C . GLU A 1 538 ? -0.659 -10.301 -5.737 1.00 42.24 ? 538 GLU A C 1 ATOM 4303 O O . GLU A 1 538 ? 0.328 -9.599 -5.494 1.00 42.17 ? 538 GLU A O 1 ATOM 4304 C CB . GLU A 1 538 ? -0.381 -12.638 -6.562 1.00 42.66 ? 538 GLU A CB 1 ATOM 4305 C CG . GLU A 1 538 ? 0.197 -14.018 -6.259 1.00 45.76 ? 538 GLU A CG 1 ATOM 4306 C CD . GLU A 1 538 ? -0.429 -15.139 -7.101 1.00 50.02 ? 538 GLU A CD 1 ATOM 4307 O OE1 . GLU A 1 538 ? -0.558 -14.992 -8.347 1.00 51.70 ? 538 GLU A OE1 1 ATOM 4308 O OE2 . GLU A 1 538 ? -0.782 -16.188 -6.513 1.00 51.83 ? 538 GLU A OE2 1 ATOM 4309 N N . LYS A 1 539 ? -1.747 -9.844 -6.361 1.00 42.20 ? 539 LYS A N 1 ATOM 4310 C CA . LYS A 1 539 ? -1.860 -8.456 -6.794 1.00 42.50 ? 539 LYS A CA 1 ATOM 4311 C C . LYS A 1 539 ? -1.927 -7.488 -5.616 1.00 42.25 ? 539 LYS A C 1 ATOM 4312 O O . LYS A 1 539 ? -1.369 -6.387 -5.671 1.00 42.13 ? 539 LYS A O 1 ATOM 4313 C CB . LYS A 1 539 ? -3.043 -8.259 -7.748 1.00 42.51 ? 539 LYS A CB 1 ATOM 4314 C CG . LYS A 1 539 ? -2.612 -8.211 -9.229 1.00 44.22 ? 539 LYS A CG 1 ATOM 4315 C CD . LYS A 1 539 ? -3.806 -8.292 -10.204 1.00 46.81 ? 539 LYS A CD 1 ATOM 4316 C CE . LYS A 1 539 ? -4.367 -6.907 -10.563 1.00 47.79 ? 539 LYS A CE 1 ATOM 4317 N NZ . LYS A 1 539 ? -5.867 -6.874 -10.462 1.00 48.78 ? 539 LYS A NZ 1 ATOM 4318 N N . GLN A 1 540 ? -2.601 -7.908 -4.551 1.00 42.21 ? 540 GLN A N 1 ATOM 4319 C CA . GLN A 1 540 ? -2.641 -7.127 -3.320 1.00 41.75 ? 540 GLN A CA 1 ATOM 4320 C C . GLN A 1 540 ? -1.258 -7.024 -2.713 1.00 41.75 ? 540 GLN A C 1 ATOM 4321 O O . GLN A 1 540 ? -0.875 -5.947 -2.262 1.00 41.68 ? 540 GLN A O 1 ATOM 4322 C CB . GLN A 1 540 ? -3.619 -7.725 -2.318 1.00 41.53 ? 540 GLN A CB 1 ATOM 4323 C CG . GLN A 1 540 ? -5.065 -7.391 -2.620 1.00 41.03 ? 540 GLN A CG 1 ATOM 4324 C CD . GLN A 1 540 ? -6.026 -8.167 -1.757 1.00 40.66 ? 540 GLN A CD 1 ATOM 4325 O OE1 . GLN A 1 540 ? -5.616 -8.948 -0.893 1.00 41.15 ? 540 GLN A OE1 1 ATOM 4326 N NE2 . GLN A 1 540 ? -7.318 -7.951 -1.977 1.00 40.73 ? 540 GLN A NE2 1 ATOM 4327 N N . ARG A 1 541 ? -0.512 -8.132 -2.718 1.00 41.78 ? 541 ARG A N 1 ATOM 4328 C CA . ARG A 1 541 ? 0.862 -8.135 -2.189 1.00 42.53 ? 541 ARG A CA 1 ATOM 4329 C C . ARG A 1 541 ? 1.788 -7.165 -2.932 1.00 42.94 ? 541 ARG A C 1 ATOM 4330 O O . ARG A 1 541 ? 2.524 -6.391 -2.308 1.00 43.21 ? 541 ARG A O 1 ATOM 4331 C CB . ARG A 1 541 ? 1.460 -9.547 -2.156 1.00 42.15 ? 541 ARG A CB 1 ATOM 4332 C CG . ARG A 1 541 ? 0.886 -10.419 -1.055 1.00 42.49 ? 541 ARG A CG 1 ATOM 4333 C CD . ARG A 1 541 ? 1.774 -11.622 -0.706 1.00 42.68 ? 541 ARG A CD 1 ATOM 4334 N NE . ARG A 1 541 ? 1.923 -12.590 -1.799 1.00 42.40 ? 541 ARG A NE 1 ATOM 4335 C CZ . ARG A 1 541 ? 1.036 -13.535 -2.118 1.00 41.70 ? 541 ARG A CZ 1 ATOM 4336 N NH1 . ARG A 1 541 ? -0.103 -13.661 -1.448 1.00 39.98 ? 541 ARG A NH1 1 ATOM 4337 N NH2 . ARG A 1 541 ? 1.293 -14.355 -3.129 1.00 41.25 ? 541 ARG A NH2 1 ATOM 4338 N N . ASP A 1 542 ? 1.726 -7.199 -4.260 1.00 43.43 ? 542 ASP A N 1 ATOM 4339 C CA . ASP A 1 542 ? 2.474 -6.275 -5.113 1.00 43.83 ? 542 ASP A CA 1 ATOM 4340 C C . ASP A 1 542 ? 2.201 -4.807 -4.803 1.00 43.44 ? 542 ASP A C 1 ATOM 4341 O O . ASP A 1 542 ? 3.064 -3.942 -4.998 1.00 43.43 ? 542 ASP A O 1 ATOM 4342 C CB . ASP A 1 542 ? 2.175 -6.569 -6.578 1.00 44.11 ? 542 ASP A CB 1 ATOM 4343 C CG . ASP A 1 542 ? 2.952 -7.757 -7.079 1.00 45.98 ? 542 ASP A CG 1 ATOM 4344 O OD1 . ASP A 1 542 ? 4.174 -7.613 -7.313 1.00 47.80 ? 542 ASP A OD1 1 ATOM 4345 O OD2 . ASP A 1 542 ? 2.350 -8.845 -7.206 1.00 48.15 ? 542 ASP A OD2 1 ATOM 4346 N N . SER A 1 543 ? 0.998 -4.543 -4.313 1.00 43.00 ? 543 SER A N 1 ATOM 4347 C CA . SER A 1 543 ? 0.582 -3.197 -3.973 1.00 42.71 ? 543 SER A CA 1 ATOM 4348 C C . SER A 1 543 ? 1.162 -2.798 -2.620 1.00 42.29 ? 543 SER A C 1 ATOM 4349 O O . SER A 1 543 ? 1.547 -1.646 -2.420 1.00 41.96 ? 543 SER A O 1 ATOM 4350 C CB . SER A 1 543 ? -0.940 -3.127 -3.945 1.00 42.61 ? 543 SER A CB 1 ATOM 4351 O OG . SER A 1 543 ? -1.381 -1.953 -4.585 1.00 44.12 ? 543 SER A OG 1 ATOM 4352 N N . LEU A 1 544 ? 1.241 -3.772 -1.711 1.00 42.13 ? 544 LEU A N 1 ATOM 4353 C CA . LEU A 1 544 ? 1.678 -3.547 -0.331 1.00 41.74 ? 544 LEU A CA 1 ATOM 4354 C C . LEU A 1 544 ? 3.184 -3.295 -0.201 1.00 41.83 ? 544 LEU A C 1 ATOM 4355 O O . LEU A 1 544 ? 3.611 -2.582 0.707 1.00 41.68 ? 544 LEU A O 1 ATOM 4356 C CB . LEU A 1 544 ? 1.270 -4.727 0.561 1.00 41.52 ? 544 LEU A CB 1 ATOM 4357 C CG . LEU A 1 544 ? -0.211 -5.027 0.837 1.00 40.81 ? 544 LEU A CG 1 ATOM 4358 C CD1 . LEU A 1 544 ? -0.351 -6.258 1.711 1.00 40.68 ? 544 LEU A CD1 1 ATOM 4359 C CD2 . LEU A 1 544 ? -0.925 -3.866 1.481 1.00 39.38 ? 544 LEU A CD2 1 ATOM 4360 N N . GLN A 1 545 ? 3.975 -3.875 -1.103 1.00 42.08 ? 545 GLN A N 1 ATOM 4361 C CA . GLN A 1 545 ? 5.436 -3.703 -1.096 1.00 42.69 ? 545 GLN A CA 1 ATOM 4362 C C . GLN A 1 545 ? 5.864 -2.279 -1.402 1.00 42.47 ? 545 GLN A C 1 ATOM 4363 O O . GLN A 1 545 ? 6.989 -1.888 -1.105 1.00 42.58 ? 545 GLN A O 1 ATOM 4364 C CB . GLN A 1 545 ? 6.100 -4.634 -2.106 1.00 42.99 ? 545 GLN A CB 1 ATOM 4365 C CG . GLN A 1 545 ? 6.254 -6.079 -1.624 1.00 45.56 ? 545 GLN A CG 1 ATOM 4366 C CD . GLN A 1 545 ? 6.657 -7.014 -2.753 1.00 48.74 ? 545 GLN A CD 1 ATOM 4367 O OE1 . GLN A 1 545 ? 6.097 -8.106 -2.907 1.00 50.26 ? 545 GLN A OE1 1 ATOM 4368 N NE2 . GLN A 1 545 ? 7.634 -6.587 -3.558 1.00 50.56 ? 545 GLN A NE2 1 ATOM 4369 N N . LYS A 1 546 ? 4.966 -1.512 -2.011 1.00 42.23 ? 546 LYS A N 1 ATOM 4370 C CA . LYS A 1 546 ? 5.243 -0.126 -2.362 1.00 41.65 ? 546 LYS A CA 1 ATOM 4371 C C . LYS A 1 546 ? 5.059 0.826 -1.181 1.00 40.71 ? 546 LYS A C 1 ATOM 4372 O O . LYS A 1 546 ? 5.405 2.004 -1.278 1.00 41.28 ? 546 LYS A O 1 ATOM 4373 C CB . LYS A 1 546 ? 4.367 0.300 -3.542 1.00 41.97 ? 546 LYS A CB 1 ATOM 4374 C CG . LYS A 1 546 ? 4.960 -0.050 -4.898 1.00 43.61 ? 546 LYS A CG 1 ATOM 4375 C CD . LYS A 1 546 ? 3.869 -0.338 -5.931 1.00 47.11 ? 546 LYS A CD 1 ATOM 4376 C CE . LYS A 1 546 ? 4.279 0.109 -7.356 1.00 49.08 ? 546 LYS A CE 1 ATOM 4377 N NZ . LYS A 1 546 ? 5.647 -0.347 -7.774 1.00 50.46 ? 546 LYS A NZ 1 ATOM 4378 N N . MET A 1 547 ? 4.506 0.325 -0.077 1.00 39.34 ? 547 MET A N 1 ATOM 4379 C CA . MET A 1 547 ? 4.298 1.135 1.125 1.00 37.91 ? 547 MET A CA 1 ATOM 4380 C C . MET A 1 547 ? 5.617 1.587 1.703 1.00 36.58 ? 547 MET A C 1 ATOM 4381 O O . MET A 1 547 ? 6.609 0.885 1.618 1.00 36.18 ? 547 MET A O 1 ATOM 4382 C CB . MET A 1 547 ? 3.546 0.343 2.192 1.00 38.34 ? 547 MET A CB 1 ATOM 4383 C CG . MET A 1 547 ? 2.029 0.312 2.020 1.00 39.62 ? 547 MET A CG 1 ATOM 4384 S SD . MET A 1 547 ? 1.315 -0.920 3.122 1.00 42.10 ? 547 MET A SD 1 ATOM 4385 C CE . MET A 1 547 ? -0.382 -0.901 2.599 1.00 41.69 ? 547 MET A CE 1 ATOM 4386 N N . SER A 1 548 ? 5.611 2.768 2.300 1.00 35.70 ? 548 SER A N 1 ATOM 4387 C CA . SER A 1 548 ? 6.792 3.337 2.941 1.00 34.91 ? 548 SER A CA 1 ATOM 4388 C C . SER A 1 548 ? 6.318 4.297 4.030 1.00 34.21 ? 548 SER A C 1 ATOM 4389 O O . SER A 1 548 ? 5.202 4.806 3.959 1.00 33.54 ? 548 SER A O 1 ATOM 4390 C CB . SER A 1 548 ? 7.634 4.094 1.916 1.00 34.78 ? 548 SER A CB 1 ATOM 4391 O OG . SER A 1 548 ? 6.878 5.178 1.392 1.00 34.86 ? 548 SER A OG 1 ATOM 4392 N N . PHE A 1 549 ? 7.155 4.554 5.032 1.00 33.55 ? 549 PHE A N 1 ATOM 4393 C CA . PHE A 1 549 ? 6.763 5.505 6.056 1.00 33.12 ? 549 PHE A CA 1 ATOM 4394 C C . PHE A 1 549 ? 6.653 6.913 5.476 1.00 33.23 ? 549 PHE A C 1 ATOM 4395 O O . PHE A 1 549 ? 5.806 7.697 5.903 1.00 33.16 ? 549 PHE A O 1 ATOM 4396 C CB . PHE A 1 549 ? 7.710 5.485 7.248 1.00 33.03 ? 549 PHE A CB 1 ATOM 4397 C CG . PHE A 1 549 ? 7.108 6.066 8.486 1.00 32.42 ? 549 PHE A CG 1 ATOM 4398 C CD1 . PHE A 1 549 ? 6.372 5.268 9.353 1.00 31.39 ? 549 PHE A CD1 1 ATOM 4399 C CD2 . PHE A 1 549 ? 7.244 7.419 8.771 1.00 32.26 ? 549 PHE A CD2 1 ATOM 4400 C CE1 . PHE A 1 549 ? 5.807 5.801 10.491 1.00 30.42 ? 549 PHE A CE1 1 ATOM 4401 C CE2 . PHE A 1 549 ? 6.669 7.960 9.902 1.00 31.07 ? 549 PHE A CE2 1 ATOM 4402 C CZ . PHE A 1 549 ? 5.947 7.147 10.762 1.00 31.27 ? 549 PHE A CZ 1 ATOM 4403 N N . SER A 1 550 ? 7.500 7.223 4.501 1.00 33.33 ? 550 SER A N 1 ATOM 4404 C CA . SER A 1 550 ? 7.431 8.506 3.807 1.00 34.31 ? 550 SER A CA 1 ATOM 4405 C C . SER A 1 550 ? 6.029 8.757 3.244 1.00 34.66 ? 550 SER A C 1 ATOM 4406 O O . SER A 1 550 ? 5.413 9.781 3.561 1.00 34.89 ? 550 SER A O 1 ATOM 4407 C CB . SER A 1 550 ? 8.481 8.577 2.702 1.00 34.40 ? 550 SER A CB 1 ATOM 4408 O OG . SER A 1 550 ? 9.768 8.288 3.230 1.00 35.24 ? 550 SER A OG 1 ATOM 4409 N N . ARG A 1 551 ? 5.509 7.811 2.456 1.00 34.74 ? 551 ARG A N 1 ATOM 4410 C CA . ARG A 1 551 ? 4.169 7.953 1.910 1.00 35.24 ? 551 ARG A CA 1 ATOM 4411 C C . ARG A 1 551 ? 3.126 8.236 2.995 1.00 35.42 ? 551 ARG A C 1 ATOM 4412 O O . ARG A 1 551 ? 2.294 9.148 2.835 1.00 35.51 ? 551 ARG A O 1 ATOM 4413 C CB . ARG A 1 551 ? 3.756 6.730 1.097 1.00 35.79 ? 551 ARG A CB 1 ATOM 4414 C CG . ARG A 1 551 ? 2.415 6.923 0.361 1.00 37.10 ? 551 ARG A CG 1 ATOM 4415 C CD . ARG A 1 551 ? 2.622 7.699 -0.923 1.00 38.95 ? 551 ARG A CD 1 ATOM 4416 N NE . ARG A 1 551 ? 1.768 8.880 -0.984 1.00 40.40 ? 551 ARG A NE 1 ATOM 4417 C CZ . ARG A 1 551 ? 1.999 9.943 -1.760 1.00 39.61 ? 551 ARG A CZ 1 ATOM 4418 N NH1 . ARG A 1 551 ? 3.064 9.990 -2.565 1.00 37.03 ? 551 ARG A NH1 1 ATOM 4419 N NH2 . ARG A 1 551 ? 1.148 10.963 -1.722 1.00 40.23 ? 551 ARG A NH2 1 ATOM 4420 N N . LEU A 1 552 ? 3.175 7.462 4.087 1.00 35.18 ? 552 LEU A N 1 ATOM 4421 C CA . LEU A 1 552 ? 2.249 7.636 5.212 1.00 34.85 ? 552 LEU A CA 1 ATOM 4422 C C . LEU A 1 552 ? 2.153 9.104 5.614 1.00 34.76 ? 552 LEU A C 1 ATOM 4423 O O . LEU A 1 552 ? 1.063 9.622 5.825 1.00 34.38 ? 552 LEU A O 1 ATOM 4424 C CB . LEU A 1 552 ? 2.681 6.791 6.410 1.00 34.84 ? 552 LEU A CB 1 ATOM 4425 C CG . LEU A 1 552 ? 1.670 6.690 7.562 1.00 35.25 ? 552 LEU A CG 1 ATOM 4426 C CD1 . LEU A 1 552 ? 0.675 5.553 7.314 1.00 35.10 ? 552 LEU A CD1 1 ATOM 4427 C CD2 . LEU A 1 552 ? 2.369 6.514 8.910 1.00 34.25 ? 552 LEU A CD2 1 ATOM 4428 N N . ILE A 1 553 ? 3.309 9.765 5.691 1.00 34.91 ? 553 ILE A N 1 ATOM 4429 C CA . ILE A 1 553 ? 3.405 11.190 6.040 1.00 34.91 ? 553 ILE A CA 1 ATOM 4430 C C . ILE A 1 553 ? 2.760 12.077 4.962 1.00 34.94 ? 553 ILE A C 1 ATOM 4431 O O . ILE A 1 553 ? 2.006 13.000 5.284 1.00 34.47 ? 553 ILE A O 1 ATOM 4432 C CB . ILE A 1 553 ? 4.885 11.614 6.274 1.00 34.75 ? 553 ILE A CB 1 ATOM 4433 C CG1 . ILE A 1 553 ? 5.463 10.913 7.503 1.00 34.15 ? 553 ILE A CG1 1 ATOM 4434 C CG2 . ILE A 1 553 ? 5.014 13.113 6.434 1.00 34.59 ? 553 ILE A CG2 1 ATOM 4435 C CD1 . ILE A 1 553 ? 6.974 10.949 7.553 1.00 33.48 ? 553 ILE A CD1 1 ATOM 4436 N N . CYS A 1 554 ? 3.056 11.787 3.694 1.00 34.94 ? 554 CYS A N 1 ATOM 4437 C CA . CYS A 1 554 ? 2.481 12.533 2.571 1.00 35.26 ? 554 CYS A CA 1 ATOM 4438 C C . CYS A 1 554 ? 0.940 12.490 2.581 1.00 35.09 ? 554 CYS A C 1 ATOM 4439 O O . CYS A 1 554 ? 0.288 13.537 2.557 1.00 34.61 ? 554 CYS A O 1 ATOM 4440 C CB . CYS A 1 554 ? 3.022 11.999 1.247 1.00 35.43 ? 554 CYS A CB 1 ATOM 4441 S SG . CYS A 1 554 ? 4.769 12.340 0.927 1.00 36.95 ? 554 CYS A SG 1 ATOM 4442 N N . ASP A 1 555 ? 0.376 11.281 2.656 1.00 34.97 ? 555 ASP A N 1 ATOM 4443 C CA . ASP A 1 555 ? -1.071 11.095 2.681 1.00 35.04 ? 555 ASP A CA 1 ATOM 4444 C C . ASP A 1 555 ? -1.770 11.591 3.951 1.00 34.82 ? 555 ASP A C 1 ATOM 4445 O O . ASP A 1 555 ? -2.983 11.746 3.934 1.00 34.87 ? 555 ASP A O 1 ATOM 4446 C CB . ASP A 1 555 ? -1.447 9.619 2.466 1.00 35.50 ? 555 ASP A CB 1 ATOM 4447 C CG . ASP A 1 555 ? -0.997 9.060 1.109 1.00 36.36 ? 555 ASP A CG 1 ATOM 4448 O OD1 . ASP A 1 555 ? -0.707 9.848 0.165 1.00 37.65 ? 555 ASP A OD1 1 ATOM 4449 O OD2 . ASP A 1 555 ? -0.945 7.807 0.997 1.00 35.50 ? 555 ASP A OD2 1 ATOM 4450 N N . ASN A 1 556 ? -1.040 11.851 5.040 1.00 34.75 ? 556 ASN A N 1 ATOM 4451 C CA . ASN A 1 556 ? -1.698 12.136 6.343 1.00 34.56 ? 556 ASN A CA 1 ATOM 4452 C C . ASN A 1 556 ? -1.439 13.479 7.016 1.00 34.83 ? 556 ASN A C 1 ATOM 4453 O O . ASN A 1 556 ? -1.817 13.694 8.171 1.00 34.71 ? 556 ASN A O 1 ATOM 4454 C CB . ASN A 1 556 ? -1.430 11.010 7.350 1.00 34.31 ? 556 ASN A CB 1 ATOM 4455 C CG . ASN A 1 556 ? -2.056 9.710 6.943 1.00 33.55 ? 556 ASN A CG 1 ATOM 4456 O OD1 . ASN A 1 556 ? -3.255 9.493 7.115 1.00 34.46 ? 556 ASN A OD1 1 ATOM 4457 N ND2 . ASN A 1 556 ? -1.249 8.829 6.400 1.00 33.78 ? 556 ASN A ND2 1 ATOM 4458 N N . THR A 1 557 ? -0.514 14.244 6.471 1.00 35.57 ? 557 THR A N 1 ATOM 4459 C CA . THR A 1 557 ? -0.132 15.523 7.047 1.00 36.33 ? 557 THR A CA 1 ATOM 4460 C C . THR A 1 557 ? -0.002 16.500 5.887 1.00 37.07 ? 557 THR A C 1 ATOM 4461 O O . THR A 1 557 ? -0.404 16.193 4.759 1.00 36.77 ? 557 THR A O 1 ATOM 4462 C CB . THR A 1 557 ? 1.233 15.450 7.806 1.00 36.48 ? 557 THR A CB 1 ATOM 4463 O OG1 . THR A 1 557 ? 2.264 14.979 6.929 1.00 36.17 ? 557 THR A OG1 1 ATOM 4464 C CG2 . THR A 1 557 ? 1.162 14.545 9.037 1.00 36.01 ? 557 THR A CG2 1 ATOM 4465 N N . HIS A 1 558 ? 0.279 17.759 6.198 1.00 37.91 ? 558 HIS A N 1 ATOM 4466 C CA . HIS A 1 558 ? 0.495 18.734 5.141 1.00 39.01 ? 558 HIS A CA 1 ATOM 4467 C C . HIS A 1 558 ? 1.987 18.908 4.788 1.00 39.15 ? 558 HIS A C 1 ATOM 4468 O O . HIS A 1 558 ? 2.367 19.914 4.189 1.00 39.79 ? 558 HIS A O 1 ATOM 4469 C CB . HIS A 1 558 ? -0.194 20.059 5.487 1.00 39.11 ? 558 HIS A CB 1 ATOM 4470 C CG . HIS A 1 558 ? -1.689 19.978 5.454 1.00 41.68 ? 558 HIS A CG 1 ATOM 4471 N ND1 . HIS A 1 558 ? -2.477 20.213 6.564 1.00 44.05 ? 558 HIS A ND1 1 ATOM 4472 C CD2 . HIS A 1 558 ? -2.542 19.663 4.445 1.00 42.78 ? 558 HIS A CD2 1 ATOM 4473 C CE1 . HIS A 1 558 ? -3.750 20.063 6.236 1.00 43.81 ? 558 HIS A CE1 1 ATOM 4474 N NE2 . HIS A 1 558 ? -3.816 19.726 4.958 1.00 43.41 ? 558 HIS A NE2 1 ATOM 4475 N N . ILE A 1 559 ? 2.823 17.933 5.155 1.00 39.15 ? 559 ILE A N 1 ATOM 4476 C CA . ILE A 1 559 ? 4.233 17.919 4.736 1.00 39.20 ? 559 ILE A CA 1 ATOM 4477 C C . ILE A 1 559 ? 4.276 17.505 3.264 1.00 39.75 ? 559 ILE A C 1 ATOM 4478 O O . ILE A 1 559 ? 3.644 16.518 2.866 1.00 39.79 ? 559 ILE A O 1 ATOM 4479 C CB . ILE A 1 559 ? 5.115 16.910 5.555 1.00 38.81 ? 559 ILE A CB 1 ATOM 4480 C CG1 . ILE A 1 559 ? 4.681 16.796 7.026 1.00 38.56 ? 559 ILE A CG1 1 ATOM 4481 C CG2 . ILE A 1 559 ? 6.608 17.207 5.384 1.00 37.95 ? 559 ILE A CG2 1 ATOM 4482 C CD1 . ILE A 1 559 ? 5.310 17.764 7.989 1.00 38.12 ? 559 ILE A CD1 1 ATOM 4483 N N . THR A 1 560 ? 5.035 18.246 2.463 1.00 40.42 ? 560 THR A N 1 ATOM 4484 C CA . THR A 1 560 ? 5.096 18.021 1.007 1.00 41.06 ? 560 THR A CA 1 ATOM 4485 C C . THR A 1 560 ? 6.496 17.589 0.556 1.00 41.42 ? 560 THR A C 1 ATOM 4486 O O . THR A 1 560 ? 6.718 17.258 -0.616 1.00 41.64 ? 560 THR A O 1 ATOM 4487 C CB . THR A 1 560 ? 4.701 19.307 0.239 1.00 41.00 ? 560 THR A CB 1 ATOM 4488 O OG1 . THR A 1 560 ? 5.414 20.427 0.792 1.00 41.47 ? 560 THR A OG1 1 ATOM 4489 C CG2 . THR A 1 560 ? 3.206 19.571 0.353 1.00 40.85 ? 560 THR A CG2 1 ATOM 4490 N N . LYS A 1 561 ? 7.428 17.583 1.505 1.00 41.78 ? 561 LYS A N 1 ATOM 4491 C CA . LYS A 1 561 ? 8.838 17.391 1.223 1.00 42.15 ? 561 LYS A CA 1 ATOM 4492 C C . LYS A 1 561 ? 9.352 16.360 2.261 1.00 42.21 ? 561 LYS A C 1 ATOM 4493 O O . LYS A 1 561 ? 9.427 16.661 3.460 1.00 41.97 ? 561 LYS A O 1 ATOM 4494 C CB . LYS A 1 561 ? 9.540 18.759 1.359 1.00 42.42 ? 561 LYS A CB 1 ATOM 4495 C CG . LYS A 1 561 ? 10.431 19.179 0.090 1.00 44.45 ? 561 LYS A CG 1 ATOM 4496 C CD . LYS A 1 561 ? 9.789 20.336 -0.733 1.00 46.39 ? 561 LYS A CD 1 ATOM 4497 C CE . LYS A 1 561 ? 9.174 19.826 -2.051 1.00 47.70 ? 561 LYS A CE 1 ATOM 4498 N NZ . LYS A 1 561 ? 7.733 20.308 -2.286 1.00 49.58 ? 561 LYS A NZ 1 ATOM 4499 N N . VAL A 1 562 ? 9.665 15.139 1.806 1.00 42.05 ? 562 VAL A N 1 ATOM 4500 C CA . VAL A 1 562 ? 10.095 14.051 2.696 1.00 41.78 ? 562 VAL A CA 1 ATOM 4501 C C . VAL A 1 562 ? 11.334 13.290 2.180 1.00 41.94 ? 562 VAL A C 1 ATOM 4502 O O . VAL A 1 562 ? 11.642 13.356 0.990 1.00 42.28 ? 562 VAL A O 1 ATOM 4503 C CB . VAL A 1 562 ? 8.943 13.054 2.947 1.00 41.74 ? 562 VAL A CB 1 ATOM 4504 C CG1 . VAL A 1 562 ? 7.804 13.739 3.658 1.00 41.51 ? 562 VAL A CG1 1 ATOM 4505 C CG2 . VAL A 1 562 ? 8.452 12.423 1.635 1.00 41.67 ? 562 VAL A CG2 1 ATOM 4506 N N . PRO A 1 563 ? 12.062 12.572 3.069 1.00 42.00 ? 563 PRO A N 1 ATOM 4507 C CA . PRO A 1 563 ? 13.125 11.681 2.569 1.00 41.95 ? 563 PRO A CA 1 ATOM 4508 C C . PRO A 1 563 ? 12.546 10.382 1.998 1.00 41.85 ? 563 PRO A C 1 ATOM 4509 O O . PRO A 1 563 ? 11.383 10.077 2.243 1.00 42.28 ? 563 PRO A O 1 ATOM 4510 C CB . PRO A 1 563 ? 13.943 11.386 3.822 1.00 41.80 ? 563 PRO A CB 1 ATOM 4511 C CG . PRO A 1 563 ? 12.970 11.481 4.926 1.00 41.82 ? 563 PRO A CG 1 ATOM 4512 C CD . PRO A 1 563 ? 11.982 12.542 4.544 1.00 41.82 ? 563 PRO A CD 1 ATOM 4513 N N . LEU A 1 564 ? 13.335 9.635 1.236 1.00 41.61 ? 564 LEU A N 1 ATOM 4514 C CA . LEU A 1 564 ? 12.867 8.367 0.678 1.00 41.59 ? 564 LEU A CA 1 ATOM 4515 C C . LEU A 1 564 ? 13.038 7.248 1.676 1.00 41.57 ? 564 LEU A C 1 ATOM 4516 O O . LEU A 1 564 ? 12.132 6.425 1.875 1.00 41.95 ? 564 LEU A O 1 ATOM 4517 C CB . LEU A 1 564 ? 13.624 8.019 -0.600 1.00 41.78 ? 564 LEU A CB 1 ATOM 4518 C CG . LEU A 1 564 ? 12.922 8.108 -1.962 1.00 42.31 ? 564 LEU A CG 1 ATOM 4519 C CD1 . LEU A 1 564 ? 11.605 8.866 -1.956 1.00 42.01 ? 564 LEU A CD1 1 ATOM 4520 C CD2 . LEU A 1 564 ? 13.880 8.651 -3.026 1.00 43.58 ? 564 LEU A CD2 1 ATOM 4521 N N . HIS A 1 565 ? 14.219 7.219 2.280 1.00 41.16 ? 565 HIS A N 1 ATOM 4522 C CA . HIS A 1 565 ? 14.539 6.318 3.359 1.00 41.08 ? 565 HIS A CA 1 ATOM 4523 C C . HIS A 1 565 ? 14.464 7.143 4.641 1.00 40.66 ? 565 HIS A C 1 ATOM 4524 O O . HIS A 1 565 ? 15.348 7.984 4.897 1.00 41.31 ? 565 HIS A O 1 ATOM 4525 C CB . HIS A 1 565 ? 15.936 5.768 3.131 1.00 41.26 ? 565 HIS A CB 1 ATOM 4526 C CG . HIS A 1 565 ? 16.205 5.414 1.703 1.00 43.27 ? 565 HIS A CG 1 ATOM 4527 N ND1 . HIS A 1 565 ? 15.583 4.355 1.069 1.00 44.48 ? 565 HIS A ND1 1 ATOM 4528 C CD2 . HIS A 1 565 ? 17.006 5.992 0.775 1.00 44.67 ? 565 HIS A CD2 1 ATOM 4529 C CE1 . HIS A 1 565 ? 15.998 4.290 -0.184 1.00 45.42 ? 565 HIS A CE1 1 ATOM 4530 N NE2 . HIS A 1 565 ? 16.866 5.269 -0.387 1.00 45.96 ? 565 HIS A NE2 1 ATOM 4531 N N . ALA A 1 566 ? 13.404 6.927 5.429 1.00 39.53 ? 566 ALA A N 1 ATOM 4532 C CA . ALA A 1 566 ? 13.112 7.818 6.558 1.00 38.50 ? 566 ALA A CA 1 ATOM 4533 C C . ALA A 1 566 ? 13.822 7.480 7.872 1.00 37.96 ? 566 ALA A C 1 ATOM 4534 O O . ALA A 1 566 ? 13.836 8.299 8.790 1.00 37.48 ? 566 ALA A O 1 ATOM 4535 C CB . ALA A 1 566 ? 11.611 7.914 6.777 1.00 38.60 ? 566 ALA A CB 1 ATOM 4536 N N . PHE A 1 567 ? 14.397 6.281 7.958 1.00 37.38 ? 567 PHE A N 1 ATOM 4537 C CA . PHE A 1 567 ? 15.064 5.812 9.184 1.00 37.21 ? 567 PHE A CA 1 ATOM 4538 C C . PHE A 1 567 ? 16.537 6.194 9.286 1.00 36.66 ? 567 PHE A C 1 ATOM 4539 O O . PHE A 1 567 ? 17.092 6.239 10.385 1.00 36.14 ? 567 PHE A O 1 ATOM 4540 C CB . PHE A 1 567 ? 14.919 4.288 9.363 1.00 37.11 ? 567 PHE A CB 1 ATOM 4541 C CG . PHE A 1 567 ? 13.556 3.861 9.779 1.00 37.80 ? 567 PHE A CG 1 ATOM 4542 C CD1 . PHE A 1 567 ? 13.071 4.174 11.037 1.00 38.57 ? 567 PHE A CD1 1 ATOM 4543 C CD2 . PHE A 1 567 ? 12.739 3.153 8.907 1.00 38.32 ? 567 PHE A CD2 1 ATOM 4544 C CE1 . PHE A 1 567 ? 11.778 3.783 11.412 1.00 39.39 ? 567 PHE A CE1 1 ATOM 4545 C CE2 . PHE A 1 567 ? 11.466 2.764 9.282 1.00 37.16 ? 567 PHE A CE2 1 ATOM 4546 C CZ . PHE A 1 567 ? 10.988 3.069 10.530 1.00 36.69 ? 567 PHE A CZ 1 ATOM 4547 N N . GLN A 1 568 ? 17.176 6.421 8.146 1.00 36.47 ? 568 GLN A N 1 ATOM 4548 C CA . GLN A 1 568 ? 18.550 6.897 8.141 1.00 36.86 ? 568 GLN A CA 1 ATOM 4549 C C . GLN A 1 568 ? 18.593 8.412 8.385 1.00 36.86 ? 568 GLN A C 1 ATOM 4550 O O . GLN A 1 568 ? 17.596 9.109 8.191 1.00 36.41 ? 568 GLN A O 1 ATOM 4551 C CB . GLN A 1 568 ? 19.270 6.504 6.835 1.00 37.21 ? 568 GLN A CB 1 ATOM 4552 C CG . GLN A 1 568 ? 18.547 6.891 5.536 1.00 38.23 ? 568 GLN A CG 1 ATOM 4553 C CD . GLN A 1 568 ? 19.376 6.610 4.280 1.00 39.62 ? 568 GLN A CD 1 ATOM 4554 O OE1 . GLN A 1 568 ? 19.511 5.458 3.843 1.00 40.34 ? 568 GLN A OE1 1 ATOM 4555 N NE2 . GLN A 1 568 ? 19.914 7.673 3.682 1.00 39.01 ? 568 GLN A NE2 1 ATOM 4556 N N . ALA A 1 569 ? 19.742 8.911 8.836 1.00 37.25 ? 569 ALA A N 1 ATOM 4557 C CA . ALA A 1 569 ? 19.950 10.353 8.993 1.00 37.73 ? 569 ALA A CA 1 ATOM 4558 C C . ALA A 1 569 ? 19.808 11.085 7.656 1.00 38.15 ? 569 ALA A C 1 ATOM 4559 O O . ALA A 1 569 ? 20.476 10.745 6.667 1.00 38.20 ? 569 ALA A O 1 ATOM 4560 C CB . ALA A 1 569 ? 21.317 10.635 9.610 1.00 37.86 ? 569 ALA A CB 1 ATOM 4561 N N . ASN A 1 570 ? 18.923 12.080 7.637 1.00 38.48 ? 570 ASN A N 1 ATOM 4562 C CA . ASN A 1 570 ? 18.609 12.836 6.421 1.00 38.82 ? 570 ASN A CA 1 ATOM 4563 C C . ASN A 1 570 ? 18.752 14.337 6.617 1.00 39.14 ? 570 ASN A C 1 ATOM 4564 O O . ASN A 1 570 ? 18.191 14.911 7.553 1.00 38.79 ? 570 ASN A O 1 ATOM 4565 C CB . ASN A 1 570 ? 17.189 12.525 5.943 1.00 38.36 ? 570 ASN A CB 1 ATOM 4566 C CG . ASN A 1 570 ? 17.009 11.086 5.555 1.00 38.05 ? 570 ASN A CG 1 ATOM 4567 O OD1 . ASN A 1 570 ? 16.113 10.414 6.059 1.00 37.87 ? 570 ASN A OD1 1 ATOM 4568 N ND2 . ASN A 1 570 ? 17.856 10.596 4.655 1.00 37.36 ? 570 ASN A ND2 1 ATOM 4569 N N . ASN A 1 571 ? 19.500 14.964 5.723 1.00 39.86 ? 571 ASN A N 1 ATOM 4570 C CA . ASN A 1 571 ? 19.722 16.394 5.800 1.00 41.15 ? 571 ASN A CA 1 ATOM 4571 C C . ASN A 1 571 ? 18.786 17.166 4.867 1.00 41.42 ? 571 ASN A C 1 ATOM 4572 O O . ASN A 1 571 ? 18.613 16.800 3.700 1.00 41.53 ? 571 ASN A O 1 ATOM 4573 C CB . ASN A 1 571 ? 21.199 16.712 5.529 1.00 41.19 ? 571 ASN A CB 1 ATOM 4574 C CG . ASN A 1 571 ? 22.109 16.233 6.659 1.00 42.91 ? 571 ASN A CG 1 ATOM 4575 O OD1 . ASN A 1 571 ? 22.372 16.970 7.617 1.00 44.21 ? 571 ASN A OD1 1 ATOM 4576 N ND2 . ASN A 1 571 ? 22.569 14.984 6.566 1.00 43.28 ? 571 ASN A ND2 1 ATOM 4577 N N . TYR A 1 572 ? 18.150 18.202 5.402 1.00 41.94 ? 572 TYR A N 1 ATOM 4578 C CA . TYR A 1 572 ? 17.332 19.094 4.580 1.00 42.95 ? 572 TYR A CA 1 ATOM 4579 C C . TYR A 1 572 ? 18.201 20.215 3.984 1.00 42.75 ? 572 TYR A C 1 ATOM 4580 O O . TYR A 1 572 ? 19.036 20.776 4.696 1.00 42.41 ? 572 TYR A O 1 ATOM 4581 C CB . TYR A 1 572 ? 16.172 19.687 5.391 1.00 43.24 ? 572 TYR A CB 1 ATOM 4582 C CG . TYR A 1 572 ? 15.178 20.442 4.535 1.00 44.68 ? 572 TYR A CG 1 ATOM 4583 C CD1 . TYR A 1 572 ? 14.148 19.770 3.866 1.00 45.79 ? 572 TYR A CD1 1 ATOM 4584 C CD2 . TYR A 1 572 ? 15.279 21.831 4.372 1.00 46.38 ? 572 TYR A CD2 1 ATOM 4585 C CE1 . TYR A 1 572 ? 13.233 20.464 3.057 1.00 46.65 ? 572 TYR A CE1 1 ATOM 4586 C CE2 . TYR A 1 572 ? 14.371 22.534 3.564 1.00 46.60 ? 572 TYR A CE2 1 ATOM 4587 C CZ . TYR A 1 572 ? 13.356 21.843 2.915 1.00 46.66 ? 572 TYR A CZ 1 ATOM 4588 O OH . TYR A 1 572 ? 12.466 22.529 2.130 1.00 46.79 ? 572 TYR A OH 1 ATOM 4589 N N . PRO A 1 573 ? 18.006 20.546 2.684 1.00 42.94 ? 573 PRO A N 1 ATOM 4590 C CA . PRO A 1 573 ? 17.039 19.996 1.731 1.00 43.35 ? 573 PRO A CA 1 ATOM 4591 C C . PRO A 1 573 ? 17.534 18.885 0.794 1.00 44.03 ? 573 PRO A C 1 ATOM 4592 O O . PRO A 1 573 ? 16.735 18.339 0.024 1.00 43.81 ? 573 PRO A O 1 ATOM 4593 C CB . PRO A 1 573 ? 16.653 21.228 0.900 1.00 43.22 ? 573 PRO A CB 1 ATOM 4594 C CG . PRO A 1 573 ? 17.807 22.235 1.097 1.00 42.66 ? 573 PRO A CG 1 ATOM 4595 C CD . PRO A 1 573 ? 18.785 21.632 2.060 1.00 42.88 ? 573 PRO A CD 1 ATOM 4596 N N . HIS A 1 574 ? 18.823 18.552 0.850 1.00 45.02 ? 574 HIS A N 1 ATOM 4597 C CA . HIS A 1 574 ? 19.419 17.646 -0.136 1.00 46.12 ? 574 HIS A CA 1 ATOM 4598 C C . HIS A 1 574 ? 18.750 16.284 -0.179 1.00 45.74 ? 574 HIS A C 1 ATOM 4599 O O . HIS A 1 574 ? 18.412 15.796 -1.253 1.00 46.12 ? 574 HIS A O 1 ATOM 4600 C CB . HIS A 1 574 ? 20.928 17.481 0.087 1.00 47.01 ? 574 HIS A CB 1 ATOM 4601 C CG . HIS A 1 574 ? 21.558 16.421 -0.780 1.00 50.48 ? 574 HIS A CG 1 ATOM 4602 N ND1 . HIS A 1 574 ? 21.318 16.323 -2.140 1.00 52.78 ? 574 HIS A ND1 1 ATOM 4603 C CD2 . HIS A 1 574 ? 22.426 15.420 -0.480 1.00 52.41 ? 574 HIS A CD2 1 ATOM 4604 C CE1 . HIS A 1 574 ? 22.006 15.308 -2.636 1.00 52.92 ? 574 HIS A CE1 1 ATOM 4605 N NE2 . HIS A 1 574 ? 22.687 14.745 -1.651 1.00 53.28 ? 574 HIS A NE2 1 ATOM 4606 N N . ASP A 1 575 ? 18.555 15.683 0.992 1.00 45.45 ? 575 ASP A N 1 ATOM 4607 C CA . ASP A 1 575 ? 18.009 14.333 1.095 1.00 44.97 ? 575 ASP A CA 1 ATOM 4608 C C . ASP A 1 575 ? 16.481 14.272 1.009 1.00 44.48 ? 575 ASP A C 1 ATOM 4609 O O . ASP A 1 575 ? 15.906 13.186 1.066 1.00 44.49 ? 575 ASP A O 1 ATOM 4610 C CB . ASP A 1 575 ? 18.506 13.659 2.381 1.00 45.08 ? 575 ASP A CB 1 ATOM 4611 C CG . ASP A 1 575 ? 20.018 13.437 2.380 1.00 45.54 ? 575 ASP A CG 1 ATOM 4612 O OD1 . ASP A 1 575 ? 20.580 13.091 1.316 1.00 47.11 ? 575 ASP A OD1 1 ATOM 4613 O OD2 . ASP A 1 575 ? 20.646 13.612 3.444 1.00 45.29 ? 575 ASP A OD2 1 ATOM 4614 N N . PHE A 1 576 ? 15.836 15.428 0.856 1.00 43.77 ? 576 PHE A N 1 ATOM 4615 C CA . PHE A 1 576 ? 14.377 15.521 0.842 1.00 43.28 ? 576 PHE A CA 1 ATOM 4616 C C . PHE A 1 576 ? 13.865 15.737 -0.570 1.00 43.53 ? 576 PHE A C 1 ATOM 4617 O O . PHE A 1 576 ? 14.287 16.671 -1.254 1.00 44.14 ? 576 PHE A O 1 ATOM 4618 C CB . PHE A 1 576 ? 13.890 16.655 1.753 1.00 42.76 ? 576 PHE A CB 1 ATOM 4619 C CG . PHE A 1 576 ? 13.934 16.319 3.226 1.00 41.53 ? 576 PHE A CG 1 ATOM 4620 C CD1 . PHE A 1 576 ? 15.156 16.197 3.901 1.00 39.77 ? 576 PHE A CD1 1 ATOM 4621 C CD2 . PHE A 1 576 ? 12.760 16.136 3.944 1.00 39.01 ? 576 PHE A CD2 1 ATOM 4622 C CE1 . PHE A 1 576 ? 15.198 15.882 5.265 1.00 38.33 ? 576 PHE A CE1 1 ATOM 4623 C CE2 . PHE A 1 576 ? 12.802 15.827 5.304 1.00 38.52 ? 576 PHE A CE2 1 ATOM 4624 C CZ . PHE A 1 576 ? 14.027 15.693 5.964 1.00 37.02 ? 576 PHE A CZ 1 ATOM 4625 N N . VAL A 1 577 ? 12.962 14.858 -0.999 1.00 43.37 ? 577 VAL A N 1 ATOM 4626 C CA . VAL A 1 577 ? 12.297 14.970 -2.295 1.00 43.14 ? 577 VAL A CA 1 ATOM 4627 C C . VAL A 1 577 ? 10.814 15.354 -2.109 1.00 42.98 ? 577 VAL A C 1 ATOM 4628 O O . VAL A 1 577 ? 10.277 15.280 -0.999 1.00 42.74 ? 577 VAL A O 1 ATOM 4629 C CB . VAL A 1 577 ? 12.408 13.649 -3.096 1.00 43.13 ? 577 VAL A CB 1 ATOM 4630 C CG1 . VAL A 1 577 ? 13.866 13.308 -3.377 1.00 42.50 ? 577 VAL A CG1 1 ATOM 4631 C CG2 . VAL A 1 577 ? 11.715 12.502 -2.349 1.00 43.60 ? 577 VAL A CG2 1 ATOM 4632 N N . ASP A 1 578 ? 10.170 15.768 -3.199 1.00 42.90 ? 578 ASP A N 1 ATOM 4633 C CA . ASP A 1 578 ? 8.742 16.125 -3.212 1.00 42.87 ? 578 ASP A CA 1 ATOM 4634 C C . ASP A 1 578 ? 7.898 14.864 -3.096 1.00 42.49 ? 578 ASP A C 1 ATOM 4635 O O . ASP A 1 578 ? 8.312 13.803 -3.570 1.00 42.51 ? 578 ASP A O 1 ATOM 4636 C CB . ASP A 1 578 ? 8.396 16.864 -4.516 1.00 42.97 ? 578 ASP A CB 1 ATOM 4637 C CG . ASP A 1 578 ? 6.933 17.259 -4.602 1.00 43.38 ? 578 ASP A CG 1 ATOM 4638 O OD1 . ASP A 1 578 ? 6.172 16.553 -5.300 1.00 43.01 ? 578 ASP A OD1 1 ATOM 4639 O OD2 . ASP A 1 578 ? 6.544 18.271 -3.970 1.00 43.71 ? 578 ASP A OD2 1 ATOM 4640 N N . CYS A 1 579 ? 6.719 14.979 -2.485 1.00 42.14 ? 579 CYS A N 1 ATOM 4641 C CA . CYS A 1 579 ? 5.852 13.816 -2.280 1.00 41.71 ? 579 CYS A CA 1 ATOM 4642 C C . CYS A 1 579 ? 5.514 13.079 -3.570 1.00 42.24 ? 579 CYS A C 1 ATOM 4643 O O . CYS A 1 579 ? 5.375 11.857 -3.562 1.00 42.89 ? 579 CYS A O 1 ATOM 4644 C CB . CYS A 1 579 ? 4.587 14.180 -1.507 1.00 41.01 ? 579 CYS A CB 1 ATOM 4645 S SG . CYS A 1 579 ? 4.837 14.253 0.301 1.00 39.47 ? 579 CYS A SG 1 ATOM 4646 N N . SER A 1 580 ? 5.412 13.805 -4.679 1.00 42.58 ? 580 SER A N 1 ATOM 4647 C CA . SER A 1 580 ? 5.106 13.190 -5.977 1.00 43.09 ? 580 SER A CA 1 ATOM 4648 C C . SER A 1 580 ? 6.051 12.072 -6.357 1.00 42.87 ? 580 SER A C 1 ATOM 4649 O O . SER A 1 580 ? 5.635 11.105 -6.996 1.00 43.17 ? 580 SER A O 1 ATOM 4650 C CB . SER A 1 580 ? 5.114 14.230 -7.085 1.00 43.05 ? 580 SER A CB 1 ATOM 4651 O OG . SER A 1 580 ? 4.273 15.308 -6.718 1.00 45.76 ? 580 SER A OG 1 ATOM 4652 N N . ALA A 1 581 ? 7.316 12.210 -5.966 1.00 42.80 ? 581 ALA A N 1 ATOM 4653 C CA . ALA A 1 581 ? 8.344 11.243 -6.331 1.00 42.75 ? 581 ALA A CA 1 ATOM 4654 C C . ALA A 1 581 ? 8.265 9.974 -5.481 1.00 43.03 ? 581 ALA A C 1 ATOM 4655 O O . ALA A 1 581 ? 9.003 9.004 -5.729 1.00 43.30 ? 581 ALA A O 1 ATOM 4656 C CB . ALA A 1 581 ? 9.734 11.875 -6.239 1.00 42.50 ? 581 ALA A CB 1 ATOM 4657 N N . VAL A 1 582 ? 7.369 9.977 -4.493 1.00 43.10 ? 582 VAL A N 1 ATOM 4658 C CA . VAL A 1 582 ? 7.248 8.860 -3.554 1.00 43.27 ? 582 VAL A CA 1 ATOM 4659 C C . VAL A 1 582 ? 6.122 7.903 -3.955 1.00 43.41 ? 582 VAL A C 1 ATOM 4660 O O . VAL A 1 582 ? 4.963 8.310 -4.056 1.00 43.57 ? 582 VAL A O 1 ATOM 4661 C CB . VAL A 1 582 ? 7.048 9.350 -2.096 1.00 43.04 ? 582 VAL A CB 1 ATOM 4662 C CG1 . VAL A 1 582 ? 7.056 8.174 -1.120 1.00 43.51 ? 582 VAL A CG1 1 ATOM 4663 C CG2 . VAL A 1 582 ? 8.124 10.334 -1.715 1.00 43.26 ? 582 VAL A CG2 1 ATOM 4664 N N . ASP A 1 583 ? 6.481 6.636 -4.171 1.00 43.66 ? 583 ASP A N 1 ATOM 4665 C CA . ASP A 1 583 ? 5.534 5.577 -4.556 1.00 44.03 ? 583 ASP A CA 1 ATOM 4666 C C . ASP A 1 583 ? 4.254 5.603 -3.706 1.00 43.81 ? 583 ASP A C 1 ATOM 4667 O O . ASP A 1 583 ? 4.319 5.682 -2.472 1.00 43.69 ? 583 ASP A O 1 ATOM 4668 C CB . ASP A 1 583 ? 6.209 4.185 -4.451 1.00 44.36 ? 583 ASP A CB 1 ATOM 4669 C CG . ASP A 1 583 ? 6.861 3.713 -5.770 1.00 45.62 ? 583 ASP A CG 1 ATOM 4670 O OD1 . ASP A 1 583 ? 7.763 4.393 -6.310 1.00 46.33 ? 583 ASP A OD1 1 ATOM 4671 O OD2 . ASP A 1 583 ? 6.493 2.624 -6.263 1.00 48.74 ? 583 ASP A OD2 1 ATOM 4672 N N . LYS A 1 584 ? 3.099 5.529 -4.369 1.00 43.77 ? 584 LYS A N 1 ATOM 4673 C CA . LYS A 1 584 ? 1.795 5.461 -3.681 1.00 43.67 ? 584 LYS A CA 1 ATOM 4674 C C . LYS A 1 584 ? 1.283 4.027 -3.534 1.00 43.19 ? 584 LYS A C 1 ATOM 4675 O O . LYS A 1 584 ? 1.554 3.180 -4.385 1.00 42.86 ? 584 LYS A O 1 ATOM 4676 C CB . LYS A 1 584 ? 0.744 6.304 -4.417 1.00 43.72 ? 584 LYS A CB 1 ATOM 4677 C CG . LYS A 1 584 ? 1.052 7.798 -4.457 1.00 45.32 ? 584 LYS A CG 1 ATOM 4678 C CD . LYS A 1 584 ? -0.147 8.638 -4.903 1.00 47.56 ? 584 LYS A CD 1 ATOM 4679 C CE . LYS A 1 584 ? -0.921 9.191 -3.706 1.00 49.36 ? 584 LYS A CE 1 ATOM 4680 N NZ . LYS A 1 584 ? -1.877 10.285 -4.111 1.00 51.09 ? 584 LYS A NZ 1 ATOM 4681 N N . LEU A 1 585 ? 0.545 3.765 -2.452 1.00 42.93 ? 585 LEU A N 1 ATOM 4682 C CA . LEU A 1 585 ? -0.179 2.496 -2.298 1.00 42.53 ? 585 LEU A CA 1 ATOM 4683 C C . LEU A 1 585 ? -1.381 2.457 -3.252 1.00 42.62 ? 585 LEU A C 1 ATOM 4684 O O . LEU A 1 585 ? -2.291 3.283 -3.155 1.00 42.41 ? 585 LEU A O 1 ATOM 4685 C CB . LEU A 1 585 ? -0.631 2.251 -0.843 1.00 41.98 ? 585 LEU A CB 1 ATOM 4686 C CG . LEU A 1 585 ? -1.704 1.160 -0.631 1.00 41.16 ? 585 LEU A CG 1 ATOM 4687 C CD1 . LEU A 1 585 ? -1.198 -0.255 -0.942 1.00 39.58 ? 585 LEU A CD1 1 ATOM 4688 C CD2 . LEU A 1 585 ? -2.341 1.211 0.754 1.00 39.20 ? 585 LEU A CD2 1 ATOM 4689 N N . ASP A 1 586 ? -1.376 1.480 -4.156 1.00 42.83 ? 586 ASP A N 1 ATOM 4690 C CA . ASP A 1 586 ? -2.430 1.345 -5.154 1.00 42.94 ? 586 ASP A CA 1 ATOM 4691 C C . ASP A 1 586 ? -3.542 0.430 -4.668 1.00 42.99 ? 586 ASP A C 1 ATOM 4692 O O . ASP A 1 586 ? -3.401 -0.788 -4.674 1.00 42.97 ? 586 ASP A O 1 ATOM 4693 C CB . ASP A 1 586 ? -1.842 0.809 -6.458 1.00 42.95 ? 586 ASP A CB 1 ATOM 4694 C CG . ASP A 1 586 ? -2.890 0.611 -7.537 1.00 42.61 ? 586 ASP A CG 1 ATOM 4695 O OD1 . ASP A 1 586 ? -3.880 1.385 -7.571 1.00 41.59 ? 586 ASP A OD1 1 ATOM 4696 O OD2 . ASP A 1 586 ? -2.707 -0.318 -8.356 1.00 41.91 ? 586 ASP A OD2 1 ATOM 4697 N N . LEU A 1 587 ? -4.661 1.019 -4.278 1.00 43.35 ? 587 LEU A N 1 ATOM 4698 C CA . LEU A 1 587 ? -5.745 0.251 -3.675 1.00 43.89 ? 587 LEU A CA 1 ATOM 4699 C C . LEU A 1 587 ? -6.697 -0.445 -4.659 1.00 44.32 ? 587 LEU A C 1 ATOM 4700 O O . LEU A 1 587 ? -7.722 -0.981 -4.237 1.00 44.29 ? 587 LEU A O 1 ATOM 4701 C CB . LEU A 1 587 ? -6.533 1.130 -2.690 1.00 43.98 ? 587 LEU A CB 1 ATOM 4702 C CG . LEU A 1 587 ? -5.961 1.272 -1.268 1.00 44.06 ? 587 LEU A CG 1 ATOM 4703 C CD1 . LEU A 1 587 ? -6.485 2.522 -0.575 1.00 44.20 ? 587 LEU A CD1 1 ATOM 4704 C CD2 . LEU A 1 587 ? -6.233 0.034 -0.417 1.00 42.13 ? 587 LEU A CD2 1 ATOM 4705 N N . SER A 1 588 ? -6.363 -0.465 -5.953 1.00 44.77 ? 588 SER A N 1 ATOM 4706 C CA . SER A 1 588 ? -7.276 -1.042 -6.961 1.00 45.33 ? 588 SER A CA 1 ATOM 4707 C C . SER A 1 588 ? -7.435 -2.582 -6.940 1.00 45.57 ? 588 SER A C 1 ATOM 4708 O O . SER A 1 588 ? -8.519 -3.079 -7.276 1.00 45.58 ? 588 SER A O 1 ATOM 4709 C CB . SER A 1 588 ? -6.984 -0.521 -8.382 1.00 45.22 ? 588 SER A CB 1 ATOM 4710 O OG . SER A 1 588 ? -5.806 -1.089 -8.920 1.00 45.94 ? 588 SER A OG 1 ATOM 4711 N N . PRO A 1 589 ? -6.370 -3.339 -6.568 1.00 45.78 ? 589 PRO A N 1 ATOM 4712 C CA . PRO A 1 589 ? -6.506 -4.791 -6.329 1.00 45.91 ? 589 PRO A CA 1 ATOM 4713 C C . PRO A 1 589 ? -7.541 -5.183 -5.264 1.00 46.21 ? 589 PRO A C 1 ATOM 4714 O O . PRO A 1 589 ? -7.821 -6.369 -5.072 1.00 45.93 ? 589 PRO A O 1 ATOM 4715 C CB . PRO A 1 589 ? -5.105 -5.197 -5.869 1.00 45.87 ? 589 PRO A CB 1 ATOM 4716 C CG . PRO A 1 589 ? -4.208 -4.188 -6.507 1.00 45.70 ? 589 PRO A CG 1 ATOM 4717 C CD . PRO A 1 589 ? -4.965 -2.910 -6.417 1.00 45.65 ? 589 PRO A CD 1 ATOM 4718 N N . TRP A 1 590 ? -8.100 -4.194 -4.584 1.00 46.97 ? 590 TRP A N 1 ATOM 4719 C CA . TRP A 1 590 ? -9.110 -4.438 -3.576 1.00 47.99 ? 590 TRP A CA 1 ATOM 4720 C C . TRP A 1 590 ? -10.529 -4.264 -4.131 1.00 49.78 ? 590 TRP A C 1 ATOM 4721 O O . TRP A 1 590 ? -11.492 -4.186 -3.365 1.00 49.97 ? 590 TRP A O 1 ATOM 4722 C CB . TRP A 1 590 ? -8.877 -3.514 -2.370 1.00 47.38 ? 590 TRP A CB 1 ATOM 4723 C CG . TRP A 1 590 ? -7.857 -4.021 -1.367 1.00 44.31 ? 590 TRP A CG 1 ATOM 4724 C CD1 . TRP A 1 590 ? -8.121 -4.632 -0.172 1.00 42.78 ? 590 TRP A CD1 1 ATOM 4725 C CD2 . TRP A 1 590 ? -6.428 -3.950 -1.471 1.00 40.81 ? 590 TRP A CD2 1 ATOM 4726 N NE1 . TRP A 1 590 ? -6.947 -4.947 0.472 1.00 41.05 ? 590 TRP A NE1 1 ATOM 4727 C CE2 . TRP A 1 590 ? -5.893 -4.540 -0.302 1.00 39.87 ? 590 TRP A CE2 1 ATOM 4728 C CE3 . TRP A 1 590 ? -5.549 -3.451 -2.438 1.00 39.62 ? 590 TRP A CE3 1 ATOM 4729 C CZ2 . TRP A 1 590 ? -4.516 -4.644 -0.071 1.00 38.49 ? 590 TRP A CZ2 1 ATOM 4730 C CZ3 . TRP A 1 590 ? -4.169 -3.548 -2.200 1.00 39.79 ? 590 TRP A CZ3 1 ATOM 4731 C CH2 . TRP A 1 590 ? -3.672 -4.140 -1.024 1.00 38.05 ? 590 TRP A CH2 1 ATOM 4732 N N . ALA A 1 591 ? -10.657 -4.216 -5.458 1.00 52.18 ? 591 ALA A N 1 ATOM 4733 C CA . ALA A 1 591 ? -11.966 -4.090 -6.123 1.00 54.52 ? 591 ALA A CA 1 ATOM 4734 C C . ALA A 1 591 ? -12.758 -5.400 -6.111 1.00 56.31 ? 591 ALA A C 1 ATOM 4735 O O . ALA A 1 591 ? -12.172 -6.481 -6.168 1.00 56.42 ? 591 ALA A O 1 ATOM 4736 C CB . ALA A 1 591 ? -11.792 -3.586 -7.546 1.00 54.31 ? 591 ALA A CB 1 ATOM 4737 N N . SER A 1 592 ? -14.089 -5.296 -6.054 1.00 58.99 ? 592 SER A N 1 ATOM 4738 C CA . SER A 1 592 ? -14.962 -6.468 -5.863 1.00 61.50 ? 592 SER A CA 1 ATOM 4739 C C . SER A 1 592 ? -16.169 -6.536 -6.831 1.00 63.23 ? 592 SER A C 1 ATOM 4740 O O . SER A 1 592 ? -17.284 -6.135 -6.485 1.00 63.37 ? 592 SER A O 1 ATOM 4741 C CB . SER A 1 592 ? -15.430 -6.529 -4.402 1.00 61.51 ? 592 SER A CB 1 ATOM 4742 O OG . SER A 1 592 ? -15.737 -7.856 -4.007 1.00 62.04 ? 592 SER A OG 1 ATOM 4743 N N . ARG A 1 593 ? -15.929 -7.071 -8.030 1.00 65.60 ? 593 ARG A N 1 ATOM 4744 C CA . ARG A 1 593 ? -16.950 -7.198 -9.093 1.00 67.92 ? 593 ARG A CA 1 ATOM 4745 C C . ARG A 1 593 ? -18.124 -8.135 -8.743 1.00 68.86 ? 593 ARG A C 1 ATOM 4746 O O . ARG A 1 593 ? -17.954 -9.356 -8.605 1.00 69.06 ? 593 ARG A O 1 ATOM 4747 C CB . ARG A 1 593 ? -16.298 -7.618 -10.422 1.00 68.21 ? 593 ARG A CB 1 ATOM 4748 C CG . ARG A 1 593 ? -15.244 -6.626 -10.941 1.00 70.37 ? 593 ARG A CG 1 ATOM 4749 C CD . ARG A 1 593 ? -14.547 -7.121 -12.216 1.00 73.12 ? 593 ARG A CD 1 ATOM 4750 N NE . ARG A 1 593 ? -14.038 -5.996 -13.018 1.00 74.84 ? 593 ARG A NE 1 ATOM 4751 C CZ . ARG A 1 593 ? -14.684 -5.446 -14.055 1.00 75.27 ? 593 ARG A CZ 1 ATOM 4752 N NH1 . ARG A 1 593 ? -15.870 -5.913 -14.449 1.00 75.28 ? 593 ARG A NH1 1 ATOM 4753 N NH2 . ARG A 1 593 ? -14.138 -4.425 -14.710 1.00 75.84 ? 593 ARG A NH2 1 ATOM 4754 N N . GLU A 1 594 ? -19.312 -7.538 -8.629 1.00 70.24 ? 594 GLU A N 1 ATOM 4755 C CA . GLU A 1 594 ? -20.538 -8.211 -8.160 1.00 71.40 ? 594 GLU A CA 1 ATOM 4756 C C . GLU A 1 594 ? -21.026 -9.352 -9.077 1.00 71.96 ? 594 GLU A C 1 ATOM 4757 O O . GLU A 1 594 ? -20.794 -10.530 -8.766 1.00 72.22 ? 594 GLU A O 1 ATOM 4758 C CB . GLU A 1 594 ? -21.661 -7.177 -7.917 1.00 71.48 ? 594 GLU A CB 1 ATOM 4759 C CG . GLU A 1 594 ? -21.335 -6.114 -6.847 1.00 72.11 ? 594 GLU A CG 1 ATOM 4760 C CD . GLU A 1 594 ? -20.559 -4.903 -7.391 1.00 72.80 ? 594 GLU A CD 1 ATOM 4761 O OE1 . GLU A 1 594 ? -20.559 -3.843 -6.711 1.00 73.51 ? 594 GLU A OE1 1 ATOM 4762 O OE2 . GLU A 1 594 ? -19.947 -4.995 -8.486 1.00 72.21 ? 594 GLU A OE2 1 ATOM 4763 N N . ASN A 1 595 ? -21.686 -9.003 -10.191 1.00 72.46 ? 595 ASN A N 1 ATOM 4764 C CA . ASN A 1 595 ? -22.204 -9.993 -11.155 1.00 72.94 ? 595 ASN A CA 1 ATOM 4765 C C . ASN A 1 595 ? -21.136 -10.995 -11.612 1.00 73.02 ? 595 ASN A C 1 ATOM 4766 O O . ASN A 1 595 ? -20.000 -10.608 -11.949 1.00 73.27 ? 595 ASN A O 1 ATOM 4767 C CB . ASN A 1 595 ? -22.786 -9.293 -12.395 1.00 73.11 ? 595 ASN A CB 1 ATOM 4768 C CG . ASN A 1 595 ? -24.277 -9.012 -12.265 1.00 73.79 ? 595 ASN A CG 1 ATOM 4769 O OD1 . ASN A 1 595 ? -24.696 -8.115 -11.525 1.00 74.86 ? 595 ASN A OD1 1 ATOM 4770 N ND2 . ASN A 1 595 ? -25.084 -9.772 -12.998 1.00 74.17 ? 595 ASN A ND2 1 HETATM 4771 C C1 . NAG B 2 . ? 23.353 4.862 6.743 1.00 59.33 ? 596 NAG A C1 1 HETATM 4772 C C2 . NAG B 2 . ? 24.620 4.288 6.109 1.00 64.66 ? 596 NAG A C2 1 HETATM 4773 C C3 . NAG B 2 . ? 24.346 3.608 4.759 1.00 66.37 ? 596 NAG A C3 1 HETATM 4774 C C4 . NAG B 2 . ? 23.177 2.613 4.789 1.00 68.58 ? 596 NAG A C4 1 HETATM 4775 C C5 . NAG B 2 . ? 21.995 3.265 5.554 1.00 66.71 ? 596 NAG A C5 1 HETATM 4776 C C6 . NAG B 2 . ? 20.777 2.391 5.899 1.00 67.15 ? 596 NAG A C6 1 HETATM 4777 C C7 . NAG B 2 . ? 26.876 5.090 6.486 1.00 65.46 ? 596 NAG A C7 1 HETATM 4778 C C8 . NAG B 2 . ? 28.022 5.716 5.743 1.00 65.73 ? 596 NAG A C8 1 HETATM 4779 N N2 . NAG B 2 . ? 25.655 5.305 5.987 1.00 64.97 ? 596 NAG A N2 1 HETATM 4780 O O3 . NAG B 2 . ? 25.523 2.941 4.357 1.00 67.08 ? 596 NAG A O3 1 HETATM 4781 O O4 . NAG B 2 . ? 22.915 2.279 3.424 1.00 73.77 ? 596 NAG A O4 1 HETATM 4782 O O5 . NAG B 2 . ? 22.433 3.784 6.809 1.00 63.07 ? 596 NAG A O5 1 HETATM 4783 O O6 . NAG B 2 . ? 20.708 1.147 5.212 1.00 68.19 ? 596 NAG A O6 1 HETATM 4784 O O7 . NAG B 2 . ? 27.084 4.412 7.500 1.00 65.51 ? 596 NAG A O7 1 HETATM 4785 C C1 . NAG C 2 . ? 22.534 0.899 3.145 1.00 78.84 ? 597 NAG A C1 1 HETATM 4786 C C2 . NAG C 2 . ? 21.772 0.820 1.808 1.00 81.21 ? 597 NAG A C2 1 HETATM 4787 C C3 . NAG C 2 . ? 22.079 -0.435 0.967 1.00 83.32 ? 597 NAG A C3 1 HETATM 4788 C C4 . NAG C 2 . ? 22.291 -1.703 1.803 1.00 84.86 ? 597 NAG A C4 1 HETATM 4789 C C5 . NAG C 2 . ? 23.091 -1.415 3.094 1.00 83.86 ? 597 NAG A C5 1 HETATM 4790 C C6 . NAG C 2 . ? 24.255 -2.401 3.234 1.00 83.80 ? 597 NAG A C6 1 HETATM 4791 C C7 . NAG C 2 . ? 19.592 1.925 1.688 1.00 82.50 ? 597 NAG A C7 1 HETATM 4792 C C8 . NAG C 2 . ? 18.175 1.946 2.232 1.00 82.30 ? 597 NAG A C8 1 HETATM 4793 N N2 . NAG C 2 . ? 20.340 0.881 2.055 1.00 81.72 ? 597 NAG A N2 1 HETATM 4794 O O3 . NAG C 2 . ? 23.196 -0.207 0.132 1.00 83.67 ? 597 NAG A O3 1 HETATM 4795 O O4 . NAG C 2 . ? 20.996 -2.205 2.115 1.00 88.52 ? 597 NAG A O4 1 HETATM 4796 O O5 . NAG C 2 . ? 23.572 -0.066 3.162 1.00 81.25 ? 597 NAG A O5 1 HETATM 4797 O O6 . NAG C 2 . ? 25.303 -1.831 3.998 1.00 83.80 ? 597 NAG A O6 1 HETATM 4798 O O7 . NAG C 2 . ? 20.011 2.843 0.948 1.00 82.90 ? 597 NAG A O7 1 HETATM 4799 C C1 . MAN D 3 . ? 20.108 -3.182 1.522 1.00 76.93 ? 598 MAN A C1 1 HETATM 4800 C C2 . MAN D 3 . ? 18.811 -3.955 1.845 1.00 77.49 ? 598 MAN A C2 1 HETATM 4801 C C3 . MAN D 3 . ? 18.554 -5.079 0.841 1.00 78.02 ? 598 MAN A C3 1 HETATM 4802 C C4 . MAN D 3 . ? 18.960 -4.628 -0.566 1.00 78.33 ? 598 MAN A C4 1 HETATM 4803 C C5 . MAN D 3 . ? 20.466 -4.342 -0.627 1.00 78.20 ? 598 MAN A C5 1 HETATM 4804 C C6 . MAN D 3 . ? 20.835 -3.359 -1.755 1.00 78.62 ? 598 MAN A C6 1 HETATM 4805 O O2 . MAN D 3 . ? 17.710 -3.072 1.860 1.00 77.38 ? 598 MAN A O2 1 HETATM 4806 O O3 . MAN D 3 . ? 17.197 -5.469 0.882 1.00 78.14 ? 598 MAN A O3 1 HETATM 4807 O O4 . MAN D 3 . ? 18.628 -5.622 -1.512 1.00 78.61 ? 598 MAN A O4 1 HETATM 4808 O O5 . MAN D 3 . ? 20.982 -3.879 0.626 1.00 77.72 ? 598 MAN A O5 1 HETATM 4809 O O6 . MAN D 3 . ? 22.042 -3.827 -2.400 1.00 78.98 ? 598 MAN A O6 1 HETATM 4810 C C1 . NAG E 2 . ? -18.542 9.461 12.898 1.00 54.38 ? 599 NAG A C1 1 HETATM 4811 C C2 . NAG E 2 . ? -18.023 10.716 13.603 1.00 56.27 ? 599 NAG A C2 1 HETATM 4812 C C3 . NAG E 2 . ? -18.717 11.992 13.132 1.00 58.26 ? 599 NAG A C3 1 HETATM 4813 C C4 . NAG E 2 . ? -18.972 12.045 11.619 1.00 60.27 ? 599 NAG A C4 1 HETATM 4814 C C5 . NAG E 2 . ? -19.435 10.673 11.087 1.00 59.34 ? 599 NAG A C5 1 HETATM 4815 C C6 . NAG E 2 . ? -19.536 10.609 9.560 1.00 60.39 ? 599 NAG A C6 1 HETATM 4816 C C7 . NAG E 2 . ? -17.149 10.581 15.886 1.00 55.10 ? 599 NAG A C7 1 HETATM 4817 C C8 . NAG E 2 . ? -17.481 10.602 17.351 1.00 54.39 ? 599 NAG A C8 1 HETATM 4818 N N2 . NAG E 2 . ? -18.189 10.602 15.043 1.00 55.49 ? 599 NAG A N2 1 HETATM 4819 O O3 . NAG E 2 . ? -17.919 13.091 13.525 1.00 58.35 ? 599 NAG A O3 1 HETATM 4820 O O4 . NAG E 2 . ? -19.942 13.050 11.389 1.00 63.75 ? 599 NAG A O4 1 HETATM 4821 O O5 . NAG E 2 . ? -18.540 9.656 11.501 1.00 55.87 ? 599 NAG A O5 1 HETATM 4822 O O6 . NAG E 2 . ? -18.361 11.135 8.965 1.00 61.80 ? 599 NAG A O6 1 HETATM 4823 O O7 . NAG E 2 . ? -15.968 10.553 15.525 1.00 54.97 ? 599 NAG A O7 1 HETATM 4824 C C1 . NAG F 2 . ? -19.610 13.950 10.307 1.00 67.59 ? 600 NAG A C1 1 HETATM 4825 C C2 . NAG F 2 . ? -20.933 14.416 9.672 1.00 69.33 ? 600 NAG A C2 1 HETATM 4826 C C3 . NAG F 2 . ? -21.032 15.924 9.409 1.00 70.72 ? 600 NAG A C3 1 HETATM 4827 C C4 . NAG F 2 . ? -19.704 16.558 8.990 1.00 71.36 ? 600 NAG A C4 1 HETATM 4828 C C5 . NAG F 2 . ? -18.481 16.017 9.751 1.00 71.34 ? 600 NAG A C5 1 HETATM 4829 C C6 . NAG F 2 . ? -17.823 17.204 10.462 1.00 72.57 ? 600 NAG A C6 1 HETATM 4830 C C7 . NAG F 2 . ? -22.378 13.172 8.137 1.00 70.38 ? 600 NAG A C7 1 HETATM 4831 C C8 . NAG F 2 . ? -22.409 12.125 7.031 1.00 70.51 ? 600 NAG A C8 1 HETATM 4832 N N2 . NAG F 2 . ? -21.188 13.716 8.425 1.00 69.77 ? 600 NAG A N2 1 HETATM 4833 O O3 . NAG F 2 . ? -21.527 16.585 10.558 1.00 70.99 ? 600 NAG A O3 1 HETATM 4834 O O4 . NAG F 2 . ? -19.521 16.429 7.595 1.00 72.16 ? 600 NAG A O4 1 HETATM 4835 O O5 . NAG F 2 . ? -18.798 15.026 10.733 1.00 69.04 ? 600 NAG A O5 1 HETATM 4836 O O6 . NAG F 2 . ? -18.728 17.709 11.444 1.00 74.56 ? 600 NAG A O6 1 HETATM 4837 O O7 . NAG F 2 . ? -23.413 13.489 8.728 1.00 70.98 ? 600 NAG A O7 1 HETATM 4838 C C1 . NAG G 2 . ? 0.159 25.957 30.133 1.00 51.41 ? 601 NAG A C1 1 HETATM 4839 C C2 . NAG G 2 . ? 1.585 26.481 29.941 1.00 53.46 ? 601 NAG A C2 1 HETATM 4840 C C3 . NAG G 2 . ? 1.557 27.897 29.372 1.00 54.22 ? 601 NAG A C3 1 HETATM 4841 C C4 . NAG G 2 . ? 0.622 28.040 28.162 1.00 56.80 ? 601 NAG A C4 1 HETATM 4842 C C5 . NAG G 2 . ? -0.665 27.204 28.278 1.00 55.53 ? 601 NAG A C5 1 HETATM 4843 C C6 . NAG G 2 . ? -1.287 26.993 26.901 1.00 55.50 ? 601 NAG A C6 1 HETATM 4844 C C7 . NAG G 2 . ? 3.219 25.472 31.490 1.00 53.98 ? 601 NAG A C7 1 HETATM 4845 C C8 . NAG G 2 . ? 3.657 25.407 32.929 1.00 54.42 ? 601 NAG A C8 1 HETATM 4846 N N2 . NAG G 2 . ? 2.355 26.451 31.179 1.00 53.64 ? 601 NAG A N2 1 HETATM 4847 O O3 . NAG G 2 . ? 2.874 28.260 29.024 1.00 52.03 ? 601 NAG A O3 1 HETATM 4848 O O4 . NAG G 2 . ? 0.280 29.407 28.013 1.00 61.99 ? 601 NAG A O4 1 HETATM 4849 O O5 . NAG G 2 . ? -0.440 25.929 28.856 1.00 53.00 ? 601 NAG A O5 1 HETATM 4850 O O6 . NAG G 2 . ? -2.668 26.718 27.030 1.00 56.68 ? 601 NAG A O6 1 HETATM 4851 O O7 . NAG G 2 . ? 3.652 24.648 30.678 1.00 54.63 ? 601 NAG A O7 1 HETATM 4852 C C1 . NAG H 2 . ? 0.393 29.836 26.642 1.00 66.71 ? 602 NAG A C1 1 HETATM 4853 C C2 . NAG H 2 . ? -0.455 31.081 26.388 1.00 69.30 ? 602 NAG A C2 1 HETATM 4854 C C3 . NAG H 2 . ? -0.198 31.470 24.939 1.00 71.38 ? 602 NAG A C3 1 HETATM 4855 C C4 . NAG H 2 . ? 1.219 32.053 24.863 1.00 72.49 ? 602 NAG A C4 1 HETATM 4856 C C5 . NAG H 2 . ? 2.210 31.291 25.773 1.00 71.43 ? 602 NAG A C5 1 HETATM 4857 C C6 . NAG H 2 . ? 2.685 32.167 26.944 1.00 71.97 ? 602 NAG A C6 1 HETATM 4858 C C7 . NAG H 2 . ? -2.436 31.153 27.852 1.00 69.64 ? 602 NAG A C7 1 HETATM 4859 C C8 . NAG H 2 . ? -3.937 31.128 27.899 1.00 68.89 ? 602 NAG A C8 1 HETATM 4860 N N2 . NAG H 2 . ? -1.874 30.898 26.664 1.00 69.97 ? 602 NAG A N2 1 HETATM 4861 O O3 . NAG H 2 . ? -1.164 32.407 24.514 1.00 72.19 ? 602 NAG A O3 1 HETATM 4862 O O4 . NAG H 2 . ? 1.713 32.105 23.525 1.00 74.77 ? 602 NAG A O4 1 HETATM 4863 O O5 . NAG H 2 . ? 1.743 30.010 26.219 1.00 68.80 ? 602 NAG A O5 1 HETATM 4864 O O6 . NAG H 2 . ? 3.875 31.639 27.497 1.00 72.90 ? 602 NAG A O6 1 HETATM 4865 O O7 . NAG H 2 . ? -1.789 31.389 28.876 1.00 69.82 ? 602 NAG A O7 1 HETATM 4866 C C1 . MAN I 3 . ? 1.720 33.456 22.979 1.00 76.93 ? 603 MAN A C1 1 HETATM 4867 C C2 . MAN I 3 . ? 2.590 34.415 23.821 1.00 77.49 ? 603 MAN A C2 1 HETATM 4868 C C3 . MAN I 3 . ? 2.005 35.827 23.861 1.00 78.02 ? 603 MAN A C3 1 HETATM 4869 C C4 . MAN I 3 . ? 1.402 36.184 22.498 1.00 78.33 ? 603 MAN A C4 1 HETATM 4870 C C5 . MAN I 3 . ? 0.231 35.249 22.166 1.00 78.20 ? 603 MAN A C5 1 HETATM 4871 C C6 . MAN I 3 . ? -0.024 35.139 20.650 1.00 78.62 ? 603 MAN A C6 1 HETATM 4872 O O2 . MAN I 3 . ? 3.903 34.461 23.302 1.00 77.38 ? 603 MAN A O2 1 HETATM 4873 O O3 . MAN I 3 . ? 2.999 36.757 24.240 1.00 78.14 ? 603 MAN A O3 1 HETATM 4874 O O4 . MAN I 3 . ? 0.954 37.523 22.498 1.00 78.61 ? 603 MAN A O4 1 HETATM 4875 O O5 . MAN I 3 . ? 0.396 33.948 22.739 1.00 77.72 ? 603 MAN A O5 1 HETATM 4876 O O6 . MAN I 3 . ? -1.452 35.166 20.418 1.00 78.98 ? 603 MAN A O6 1 HETATM 4877 C C1 . NAG J 2 . ? 8.321 -25.668 12.028 1.00 58.99 ? 604 NAG A C1 1 HETATM 4878 C C2 . NAG J 2 . ? 9.130 -26.683 11.221 1.00 64.88 ? 604 NAG A C2 1 HETATM 4879 C C3 . NAG J 2 . ? 9.945 -27.689 12.055 1.00 66.99 ? 604 NAG A C3 1 HETATM 4880 C C4 . NAG J 2 . ? 10.225 -27.358 13.539 1.00 69.07 ? 604 NAG A C4 1 HETATM 4881 C C5 . NAG J 2 . ? 9.232 -26.314 14.092 1.00 66.25 ? 604 NAG A C5 1 HETATM 4882 C C6 . NAG J 2 . ? 9.619 -25.789 15.481 1.00 66.17 ? 604 NAG A C6 1 HETATM 4883 C C7 . NAG J 2 . ? 8.460 -27.425 8.987 1.00 66.64 ? 604 NAG A C7 1 HETATM 4884 C C8 . NAG J 2 . ? 8.075 -28.692 8.250 1.00 66.85 ? 604 NAG A C8 1 HETATM 4885 N N2 . NAG J 2 . ? 8.248 -27.404 10.312 1.00 65.60 ? 604 NAG A N2 1 HETATM 4886 O O3 . NAG J 2 . ? 11.197 -27.829 11.422 1.00 68.20 ? 604 NAG A O3 1 HETATM 4887 O O4 . NAG J 2 . ? 10.229 -28.551 14.355 1.00 74.79 ? 604 NAG A O4 1 HETATM 4888 O O5 . NAG J 2 . ? 9.071 -25.253 13.159 1.00 62.28 ? 604 NAG A O5 1 HETATM 4889 O O6 . NAG J 2 . ? 10.979 -25.381 15.518 1.00 66.47 ? 604 NAG A O6 1 HETATM 4890 O O7 . NAG J 2 . ? 8.949 -26.473 8.366 1.00 67.14 ? 604 NAG A O7 1 HETATM 4891 C C1 . NAG K 2 . ? 11.452 -29.302 14.101 1.00 78.92 ? 605 NAG A C1 1 HETATM 4892 C C2 . NAG K 2 . ? 12.307 -29.698 15.316 1.00 80.86 ? 605 NAG A C2 1 HETATM 4893 C C3 . NAG K 2 . ? 13.710 -30.061 14.804 1.00 81.36 ? 605 NAG A C3 1 HETATM 4894 C C4 . NAG K 2 . ? 13.626 -31.075 13.652 1.00 81.53 ? 605 NAG A C4 1 HETATM 4895 C C5 . NAG K 2 . ? 12.556 -30.663 12.624 1.00 81.69 ? 605 NAG A C5 1 HETATM 4896 C C6 . NAG K 2 . ? 12.376 -31.669 11.488 1.00 82.78 ? 605 NAG A C6 1 HETATM 4897 C C7 . NAG K 2 . ? 11.899 -28.930 17.562 1.00 83.86 ? 605 NAG A C7 1 HETATM 4898 C C8 . NAG K 2 . ? 12.790 -28.547 18.711 1.00 84.25 ? 605 NAG A C8 1 HETATM 4899 N N2 . NAG K 2 . ? 12.348 -28.666 16.335 1.00 82.74 ? 605 NAG A N2 1 HETATM 4900 O O3 . NAG K 2 . ? 14.520 -30.575 15.843 1.00 80.89 ? 605 NAG A O3 1 HETATM 4901 O O4 . NAG K 2 . ? 14.882 -31.137 13.016 1.00 82.03 ? 605 NAG A O4 1 HETATM 4902 O O5 . NAG K 2 . ? 11.312 -30.445 13.282 1.00 80.52 ? 605 NAG A O5 1 HETATM 4903 O O6 . NAG K 2 . ? 11.482 -31.127 10.533 1.00 83.79 ? 605 NAG A O6 1 HETATM 4904 O O7 . NAG K 2 . ? 10.809 -29.469 17.770 1.00 84.37 ? 605 NAG A O7 1 HETATM 4905 CA CA . CA L 4 . ? -0.120 -7.020 18.945 1.00 29.25 ? 606 CA A CA 1 HETATM 4906 I I . IOD M 5 . ? 8.690 -8.391 5.179 1.00 93.73 ? 607 IOD A I 1 HETATM 4907 I I . IOD N 5 . ? 25.450 6.528 44.419 1.00 86.86 ? 608 IOD A I 1 HETATM 4908 I I . IOD O 5 . ? 14.694 3.791 5.927 0.50 85.54 ? 609 IOD A I 1 HETATM 4909 I I . IOD P 5 . ? 6.959 20.855 4.534 1.00 72.87 ? 610 IOD A I 1 HETATM 4910 I I . IOD Q 5 . ? 12.028 -15.792 29.819 1.00 30.71 ? 611 IOD A I 1 HETATM 4911 I I . IOD R 5 . ? 36.628 -15.944 32.240 1.00 59.77 ? 612 IOD A I 1 HETATM 4912 I I . IOD S 5 . ? -13.433 13.842 22.090 1.00 72.23 ? 613 IOD A I 1 HETATM 4913 I I . IOD T 5 . ? 25.116 1.647 9.746 0.50 67.97 ? 614 IOD A I 1 HETATM 4914 C CHA . HEM U 6 . ? 8.701 0.058 29.295 1.00 26.91 ? 615 HEM A CHA 1 HETATM 4915 C CHB . HEM U 6 . ? 9.024 4.898 29.136 1.00 27.59 ? 615 HEM A CHB 1 HETATM 4916 C CHC . HEM U 6 . ? 10.856 4.647 24.630 1.00 25.49 ? 615 HEM A CHC 1 HETATM 4917 C CHD . HEM U 6 . ? 10.643 -0.127 24.788 1.00 26.30 ? 615 HEM A CHD 1 HETATM 4918 C C1A . HEM U 6 . ? 8.620 1.383 29.668 1.00 27.56 ? 615 HEM A C1A 1 HETATM 4919 C C2A . HEM U 6 . ? 8.126 1.903 30.930 1.00 28.67 ? 615 HEM A C2A 1 HETATM 4920 C C3A . HEM U 6 . ? 8.205 3.241 30.894 1.00 28.41 ? 615 HEM A C3A 1 HETATM 4921 C C4A . HEM U 6 . ? 8.766 3.618 29.603 1.00 28.04 ? 615 HEM A C4A 1 HETATM 4922 C CMA . HEM U 6 . ? 7.788 4.198 32.037 1.00 27.37 ? 615 HEM A CMA 1 HETATM 4923 C CAA . HEM U 6 . ? 7.596 1.049 32.105 1.00 28.04 ? 615 HEM A CAA 1 HETATM 4924 C CBA . HEM U 6 . ? 8.764 0.680 32.997 1.00 29.04 ? 615 HEM A CBA 1 HETATM 4925 C CGA . HEM U 6 . ? 8.339 -0.377 33.993 1.00 30.53 ? 615 HEM A CGA 1 HETATM 4926 O O1A . HEM U 6 . ? 7.367 -0.139 34.748 1.00 30.74 ? 615 HEM A O1A 1 HETATM 4927 O O2A . HEM U 6 . ? 8.972 -1.468 34.047 1.00 31.86 ? 615 HEM A O2A 1 HETATM 4928 C C1B . HEM U 6 . ? 9.523 5.258 27.890 1.00 26.84 ? 615 HEM A C1B 1 HETATM 4929 C C2B . HEM U 6 . ? 9.723 6.610 27.367 1.00 26.42 ? 615 HEM A C2B 1 HETATM 4930 C C3B . HEM U 6 . ? 10.224 6.527 26.127 1.00 25.92 ? 615 HEM A C3B 1 HETATM 4931 C C4B . HEM U 6 . ? 10.358 5.127 25.820 1.00 26.23 ? 615 HEM A C4B 1 HETATM 4932 C CMB . HEM U 6 . ? 9.429 7.920 28.112 1.00 24.27 ? 615 HEM A CMB 1 HETATM 4933 C CAB . HEM U 6 . ? 10.616 7.671 25.149 1.00 26.33 ? 615 HEM A CAB 1 HETATM 4934 C CBB . HEM U 6 . ? 10.861 8.928 25.567 1.00 27.45 ? 615 HEM A CBB 1 HETATM 4935 C C1C . HEM U 6 . ? 11.010 3.332 24.293 1.00 26.38 ? 615 HEM A C1C 1 HETATM 4936 C C2C . HEM U 6 . ? 11.662 2.827 23.093 1.00 26.42 ? 615 HEM A C2C 1 HETATM 4937 C C3C . HEM U 6 . ? 11.603 1.489 23.128 1.00 25.31 ? 615 HEM A C3C 1 HETATM 4938 C C4C . HEM U 6 . ? 10.917 1.136 24.357 1.00 25.35 ? 615 HEM A C4C 1 HETATM 4939 C CMC . HEM U 6 . ? 12.304 3.706 21.999 1.00 24.43 ? 615 HEM A CMC 1 HETATM 4940 C CAC . HEM U 6 . ? 12.151 0.481 22.080 1.00 26.03 ? 615 HEM A CAC 1 HETATM 4941 C CBC . HEM U 6 . ? 12.668 0.866 20.905 1.00 24.90 ? 615 HEM A CBC 1 HETATM 4942 C C1D . HEM U 6 . ? 10.026 -0.494 25.959 1.00 25.78 ? 615 HEM A C1D 1 HETATM 4943 C C2D . HEM U 6 . ? 9.599 -1.831 26.207 1.00 25.55 ? 615 HEM A C2D 1 HETATM 4944 C C3D . HEM U 6 . ? 8.989 -1.819 27.608 1.00 26.95 ? 615 HEM A C3D 1 HETATM 4945 C C4D . HEM U 6 . ? 9.118 -0.440 28.069 1.00 27.34 ? 615 HEM A C4D 1 HETATM 4946 C CMD . HEM U 6 . ? 9.767 -2.989 25.223 1.00 22.89 ? 615 HEM A CMD 1 HETATM 4947 C CAD . HEM U 6 . ? 8.340 -3.010 28.349 1.00 26.24 ? 615 HEM A CAD 1 HETATM 4948 C CBD . HEM U 6 . ? 6.819 -2.815 28.234 1.00 25.36 ? 615 HEM A CBD 1 HETATM 4949 C CGD . HEM U 6 . ? 6.073 -3.997 28.812 1.00 25.57 ? 615 HEM A CGD 1 HETATM 4950 O O1D . HEM U 6 . ? 6.159 -5.121 28.251 1.00 25.04 ? 615 HEM A O1D 1 HETATM 4951 O O2D . HEM U 6 . ? 5.392 -3.836 29.852 1.00 26.31 ? 615 HEM A O2D 1 HETATM 4952 N NA . HEM U 6 . ? 8.999 2.455 28.894 1.00 27.33 ? 615 HEM A NA 1 HETATM 4953 N NB . HEM U 6 . ? 9.917 4.382 26.904 1.00 26.28 ? 615 HEM A NB 1 HETATM 4954 N NC . HEM U 6 . ? 10.562 2.269 25.048 1.00 25.70 ? 615 HEM A NC 1 HETATM 4955 N ND . HEM U 6 . ? 9.736 0.297 27.064 1.00 26.79 ? 615 HEM A ND 1 HETATM 4956 FE FE . HEM U 6 . ? 9.965 2.315 27.117 1.00 27.70 ? 615 HEM A FE 1 HETATM 4957 S S . SCN V 7 . ? -12.648 0.969 28.017 1.00 35.19 ? 616 SCN A S 1 HETATM 4958 C C . SCN V 7 . ? -14.369 0.520 27.763 1.00 33.81 ? 616 SCN A C 1 HETATM 4959 N N . SCN V 7 . ? -15.489 0.162 27.641 1.00 33.41 ? 616 SCN A N 1 HETATM 4960 C C1 . SHA W 8 . ? 5.039 3.034 29.132 1.00 27.07 ? 617 SHA A C1 1 HETATM 4961 C C2 . SHA W 8 . ? 4.470 4.111 29.789 1.00 26.23 ? 617 SHA A C2 1 HETATM 4962 C C3 . SHA W 8 . ? 3.674 3.917 30.928 1.00 27.01 ? 617 SHA A C3 1 HETATM 4963 C C4 . SHA W 8 . ? 3.434 2.629 31.427 1.00 27.90 ? 617 SHA A C4 1 HETATM 4964 C C5 . SHA W 8 . ? 3.972 1.500 30.802 1.00 28.55 ? 617 SHA A C5 1 HETATM 4965 C C6 . SHA W 8 . ? 4.774 1.669 29.663 1.00 28.14 ? 617 SHA A C6 1 HETATM 4966 O O6 . SHA W 8 . ? 5.297 0.583 29.045 1.00 28.85 ? 617 SHA A O6 1 HETATM 4967 C C7 . SHA W 8 . ? 5.886 3.262 27.902 1.00 29.10 ? 617 SHA A C7 1 HETATM 4968 O O7 . SHA W 8 . ? 5.947 4.387 27.413 1.00 30.21 ? 617 SHA A O7 1 HETATM 4969 N N8 . SHA W 8 . ? 6.550 2.247 27.322 1.00 27.34 ? 617 SHA A N8 1 HETATM 4970 O O9 . SHA W 8 . ? 7.401 2.511 26.242 1.00 29.50 ? 617 SHA A O9 1 HETATM 4971 O O . HOH X 9 . ? 1.221 3.073 23.056 1.00 25.04 ? 618 HOH A O 1 HETATM 4972 O O . HOH X 9 . ? -3.550 5.040 17.379 1.00 29.72 ? 619 HOH A O 1 HETATM 4973 O O . HOH X 9 . ? -6.018 4.284 18.311 1.00 28.99 ? 620 HOH A O 1 HETATM 4974 O O . HOH X 9 . ? -8.135 6.002 18.719 1.00 25.35 ? 621 HOH A O 1 HETATM 4975 O O . HOH X 9 . ? -10.772 6.340 17.743 1.00 38.45 ? 622 HOH A O 1 HETATM 4976 O O . HOH X 9 . ? 14.744 11.079 8.025 1.00 32.26 ? 623 HOH A O 1 HETATM 4977 O O . HOH X 9 . ? 32.349 3.667 32.092 1.00 36.99 ? 624 HOH A O 1 HETATM 4978 O O . HOH X 9 . ? -15.828 1.645 12.672 1.00 29.70 ? 625 HOH A O 1 HETATM 4979 O O . HOH X 9 . ? 20.457 14.471 23.937 1.00 29.17 ? 626 HOH A O 1 HETATM 4980 O O . HOH X 9 . ? -16.004 11.110 6.781 1.00 42.18 ? 627 HOH A O 1 HETATM 4981 O O . HOH X 9 . ? 30.709 -11.673 22.716 1.00 19.09 ? 628 HOH A O 1 HETATM 4982 O O . HOH X 9 . ? -1.626 -18.177 30.294 1.00 32.20 ? 629 HOH A O 1 HETATM 4983 O O . HOH X 9 . ? 6.059 4.365 -0.989 1.00 48.10 ? 630 HOH A O 1 HETATM 4984 O O . HOH X 9 . ? -7.456 22.306 37.572 1.00 55.32 ? 631 HOH A O 1 HETATM 4985 O O . HOH X 9 . ? 6.080 19.608 32.436 1.00 38.00 ? 632 HOH A O 1 HETATM 4986 O O . HOH X 9 . ? 17.288 -9.011 55.500 1.00 47.56 ? 633 HOH A O 1 HETATM 4987 O O . HOH X 9 . ? 25.157 -9.248 43.282 1.00 45.75 ? 634 HOH A O 1 HETATM 4988 O O . HOH X 9 . ? -3.330 -2.919 22.657 1.00 42.42 ? 635 HOH A O 1 HETATM 4989 O O . HOH X 9 . ? 5.925 -0.364 39.424 1.00 54.45 ? 636 HOH A O 1 HETATM 4990 O O . HOH X 9 . ? -7.639 -8.944 26.092 1.00 53.29 ? 637 HOH A O 1 HETATM 4991 O O . HOH X 9 . ? 20.427 -15.484 5.069 1.00 45.55 ? 638 HOH A O 1 HETATM 4992 O O . HOH X 9 . ? -11.081 -0.695 17.181 1.00 28.45 ? 639 HOH A O 1 HETATM 4993 O O . HOH X 9 . ? -4.684 -7.976 10.520 1.00 26.00 ? 640 HOH A O 1 HETATM 4994 O O . HOH X 9 . ? -4.387 -5.414 11.844 1.00 26.21 ? 641 HOH A O 1 HETATM 4995 O O . HOH X 9 . ? 1.864 -0.090 49.586 1.00 49.86 ? 642 HOH A O 1 HETATM 4996 O O . HOH X 9 . ? 20.780 -9.725 39.939 1.00 26.49 ? 643 HOH A O 1 HETATM 4997 O O . HOH X 9 . ? -4.928 -10.433 16.495 1.00 28.07 ? 644 HOH A O 1 HETATM 4998 O O . HOH X 9 . ? -1.100 -7.764 10.955 1.00 26.24 ? 645 HOH A O 1 HETATM 4999 O O . HOH X 9 . ? 30.589 3.207 23.681 1.00 35.85 ? 646 HOH A O 1 HETATM 5000 O O . HOH X 9 . ? 9.099 -8.267 -2.207 1.00 37.99 ? 647 HOH A O 1 HETATM 5001 O O . HOH X 9 . ? -7.792 12.718 9.187 1.00 35.71 ? 648 HOH A O 1 HETATM 5002 O O . HOH X 9 . ? 24.282 14.894 47.784 1.00 40.50 ? 649 HOH A O 1 HETATM 5003 O O . HOH X 9 . ? 5.574 -20.656 28.833 1.00 24.32 ? 650 HOH A O 1 HETATM 5004 O O . HOH X 9 . ? 23.156 19.232 5.662 1.00 52.05 ? 651 HOH A O 1 HETATM 5005 O O . HOH X 9 . ? 16.848 5.317 51.127 1.00 29.55 ? 652 HOH A O 1 HETATM 5006 O O . HOH X 9 . ? 6.165 -15.198 32.526 1.00 29.61 ? 653 HOH A O 1 HETATM 5007 O O . HOH X 9 . ? -11.260 -24.331 5.454 1.00 44.83 ? 654 HOH A O 1 HETATM 5008 O O . HOH X 9 . ? 7.724 -18.129 23.095 1.00 23.74 ? 655 HOH A O 1 HETATM 5009 O O . HOH X 9 . ? -15.010 7.280 24.923 1.00 31.85 ? 656 HOH A O 1 HETATM 5010 O O . HOH X 9 . ? 3.458 -16.903 9.224 1.00 23.12 ? 657 HOH A O 1 HETATM 5011 O O . HOH X 9 . ? 17.979 -11.822 47.818 1.00 43.45 ? 658 HOH A O 1 HETATM 5012 O O . HOH X 9 . ? 8.376 -20.921 23.721 1.00 34.06 ? 659 HOH A O 1 HETATM 5013 O O . HOH X 9 . ? -12.822 9.070 39.402 1.00 48.09 ? 660 HOH A O 1 HETATM 5014 O O . HOH X 9 . ? -0.591 -19.484 14.723 1.00 34.97 ? 661 HOH A O 1 HETATM 5015 O O . HOH X 9 . ? 28.764 11.930 52.477 1.00 30.16 ? 662 HOH A O 1 HETATM 5016 O O . HOH X 9 . ? -6.677 28.334 27.111 1.00 47.43 ? 663 HOH A O 1 HETATM 5017 O O . HOH X 9 . ? 7.234 -5.723 30.962 1.00 27.39 ? 664 HOH A O 1 HETATM 5018 O O . HOH X 9 . ? 20.776 0.967 20.592 1.00 25.69 ? 665 HOH A O 1 HETATM 5019 O O . HOH X 9 . ? 13.474 -19.837 17.622 1.00 29.83 ? 666 HOH A O 1 HETATM 5020 O O . HOH X 9 . ? 18.802 8.013 26.640 1.00 24.24 ? 667 HOH A O 1 HETATM 5021 O O . HOH X 9 . ? 27.180 -19.670 33.922 1.00 62.19 ? 668 HOH A O 1 HETATM 5022 O O . HOH X 9 . ? 15.674 -1.043 46.709 1.00 34.71 ? 669 HOH A O 1 HETATM 5023 O O . HOH X 9 . ? 0.846 24.274 12.677 1.00 52.91 ? 670 HOH A O 1 HETATM 5024 O O . HOH X 9 . ? -4.639 -11.556 36.728 1.00 31.28 ? 671 HOH A O 1 HETATM 5025 O O . HOH X 9 . ? 3.518 15.816 -9.564 1.00 34.94 ? 672 HOH A O 1 HETATM 5026 O O . HOH X 9 . ? 5.583 -1.409 30.754 1.00 27.16 ? 673 HOH A O 1 HETATM 5027 O O . HOH X 9 . ? -5.962 -6.282 18.211 1.00 29.97 ? 674 HOH A O 1 HETATM 5028 O O . HOH X 9 . ? -5.632 -5.233 27.411 1.00 54.81 ? 675 HOH A O 1 HETATM 5029 O O . HOH X 9 . ? 5.771 16.755 31.365 1.00 28.70 ? 676 HOH A O 1 HETATM 5030 O O . HOH X 9 . ? 4.322 11.454 48.317 1.00 44.48 ? 677 HOH A O 1 HETATM 5031 O O . HOH X 9 . ? 9.663 29.610 2.207 1.00 27.77 ? 678 HOH A O 1 HETATM 5032 O O . HOH X 9 . ? 17.601 12.689 10.443 1.00 29.89 ? 679 HOH A O 1 HETATM 5033 O O . HOH X 9 . ? 14.677 1.876 17.835 1.00 25.62 ? 680 HOH A O 1 HETATM 5034 O O . HOH X 9 . ? 8.953 -22.206 18.796 1.00 30.48 ? 681 HOH A O 1 HETATM 5035 O O . HOH X 9 . ? 3.324 -12.916 25.375 1.00 31.99 ? 682 HOH A O 1 HETATM 5036 O O . HOH X 9 . ? 29.565 3.885 32.085 1.00 31.13 ? 683 HOH A O 1 HETATM 5037 O O . HOH X 9 . ? 24.393 -16.039 19.628 1.00 43.35 ? 684 HOH A O 1 HETATM 5038 O O . HOH X 9 . ? -0.867 1.482 38.388 1.00 45.74 ? 685 HOH A O 1 HETATM 5039 O O . HOH X 9 . ? 22.584 -15.609 38.609 1.00 50.11 ? 686 HOH A O 1 HETATM 5040 O O . HOH X 9 . ? -4.806 -26.117 36.294 1.00 36.54 ? 687 HOH A O 1 HETATM 5041 O O . HOH X 9 . ? 16.783 -2.033 44.098 1.00 23.58 ? 688 HOH A O 1 HETATM 5042 O O . HOH X 9 . ? 14.666 -18.637 49.938 1.00 35.90 ? 689 HOH A O 1 HETATM 5043 O O . HOH X 9 . ? 12.770 -16.518 33.054 1.00 27.16 ? 690 HOH A O 1 HETATM 5044 O O . HOH X 9 . ? 4.603 28.190 7.345 1.00 61.13 ? 691 HOH A O 1 HETATM 5045 O O . HOH X 9 . ? -2.190 -9.018 45.262 1.00 53.57 ? 692 HOH A O 1 HETATM 5046 O O . HOH X 9 . ? 14.182 -11.940 40.745 1.00 16.89 ? 693 HOH A O 1 HETATM 5047 O O . HOH X 9 . ? -13.883 9.106 33.381 1.00 58.25 ? 694 HOH A O 1 HETATM 5048 O O . HOH X 9 . ? 16.152 -11.909 38.796 1.00 25.31 ? 695 HOH A O 1 HETATM 5049 O O . HOH X 9 . ? 15.793 19.484 31.534 1.00 33.37 ? 696 HOH A O 1 HETATM 5050 O O . HOH X 9 . ? -7.260 -14.155 15.640 1.00 30.88 ? 697 HOH A O 1 HETATM 5051 O O . HOH X 9 . ? -19.122 5.270 17.678 1.00 53.90 ? 698 HOH A O 1 HETATM 5052 O O . HOH X 9 . ? 9.068 -20.294 35.462 1.00 33.07 ? 699 HOH A O 1 HETATM 5053 O O . HOH X 9 . ? 0.975 16.426 2.308 1.00 41.89 ? 700 HOH A O 1 HETATM 5054 O O . HOH X 9 . ? -1.634 17.852 28.157 1.00 19.50 ? 701 HOH A O 1 HETATM 5055 O O . HOH X 9 . ? 9.344 3.265 5.572 1.00 28.68 ? 702 HOH A O 1 HETATM 5056 O O . HOH X 9 . ? -0.387 -29.426 11.605 1.00 50.34 ? 703 HOH A O 1 HETATM 5057 O O . HOH X 9 . ? -4.045 13.272 18.343 1.00 41.72 ? 704 HOH A O 1 HETATM 5058 O O . HOH X 9 . ? 2.405 21.704 8.131 1.00 31.56 ? 705 HOH A O 1 HETATM 5059 O O . HOH X 9 . ? -18.788 1.549 10.686 1.00 41.63 ? 706 HOH A O 1 HETATM 5060 O O . HOH X 9 . ? 23.887 -7.259 23.548 1.00 26.93 ? 707 HOH A O 1 HETATM 5061 O O . HOH X 9 . ? -9.014 21.394 36.145 1.00 52.04 ? 708 HOH A O 1 HETATM 5062 O O . HOH X 9 . ? 22.090 3.200 19.325 1.00 29.80 ? 709 HOH A O 1 HETATM 5063 O O . HOH X 9 . ? -7.066 -9.505 9.660 1.00 36.49 ? 710 HOH A O 1 HETATM 5064 O O . HOH X 9 . ? 2.038 12.922 24.876 1.00 34.56 ? 711 HOH A O 1 HETATM 5065 O O . HOH X 9 . ? 21.671 -16.709 50.908 1.00 37.27 ? 712 HOH A O 1 HETATM 5066 O O . HOH X 9 . ? -7.621 -11.493 26.079 1.00 51.29 ? 713 HOH A O 1 HETATM 5067 O O . HOH X 9 . ? -20.747 9.525 17.892 1.00 45.03 ? 714 HOH A O 1 HETATM 5068 O O . HOH X 9 . ? 18.568 -2.907 53.852 1.00 49.71 ? 715 HOH A O 1 HETATM 5069 O O . HOH X 9 . ? 31.366 -15.481 22.406 1.00 23.05 ? 716 HOH A O 1 HETATM 5070 O O . HOH X 9 . ? 36.569 -6.178 40.533 1.00 42.36 ? 717 HOH A O 1 HETATM 5071 O O . HOH X 9 . ? -4.331 -2.970 51.721 1.00 43.60 ? 718 HOH A O 1 HETATM 5072 O O . HOH X 9 . ? 16.053 18.445 19.108 1.00 22.87 ? 719 HOH A O 1 HETATM 5073 O O . HOH X 9 . ? 18.839 -10.609 34.918 1.00 20.56 ? 720 HOH A O 1 HETATM 5074 O O . HOH X 9 . ? 21.073 -22.575 23.329 1.00 36.49 ? 721 HOH A O 1 HETATM 5075 O O . HOH X 9 . ? 23.253 -13.641 54.125 1.00 41.72 ? 722 HOH A O 1 HETATM 5076 O O . HOH X 9 . ? 15.359 15.862 18.652 1.00 25.04 ? 723 HOH A O 1 HETATM 5077 O O . HOH X 9 . ? 22.253 16.242 21.921 1.00 32.55 ? 724 HOH A O 1 HETATM 5078 O O . HOH X 9 . ? 6.245 11.060 49.832 1.00 39.62 ? 725 HOH A O 1 HETATM 5079 O O . HOH X 9 . ? -1.011 -3.860 -7.330 1.00 42.93 ? 726 HOH A O 1 HETATM 5080 O O . HOH X 9 . ? -7.350 4.936 -2.721 1.00 39.92 ? 727 HOH A O 1 HETATM 5081 O O . HOH X 9 . ? 20.508 4.871 17.729 1.00 26.88 ? 728 HOH A O 1 HETATM 5082 O O . HOH X 9 . ? 5.540 -9.463 46.554 1.00 34.88 ? 729 HOH A O 1 HETATM 5083 O O . HOH X 9 . ? -3.814 -18.487 3.932 1.00 56.77 ? 730 HOH A O 1 HETATM 5084 O O . HOH X 9 . ? 24.391 -1.279 46.366 1.00 37.87 ? 731 HOH A O 1 HETATM 5085 O O . HOH X 9 . ? -15.376 -10.113 4.381 1.00 45.51 ? 732 HOH A O 1 HETATM 5086 O O . HOH X 9 . ? 32.518 -19.787 28.271 1.00 24.40 ? 733 HOH A O 1 HETATM 5087 O O . HOH X 9 . ? -4.307 -23.008 23.860 1.00 39.64 ? 734 HOH A O 1 HETATM 5088 O O . HOH X 9 . ? 21.863 -0.838 -2.942 1.00 68.88 ? 735 HOH A O 1 HETATM 5089 O O . HOH X 9 . ? 2.782 3.973 2.680 1.00 38.53 ? 736 HOH A O 1 HETATM 5090 O O . HOH X 9 . ? 14.284 -11.934 6.818 1.00 36.66 ? 737 HOH A O 1 HETATM 5091 O O . HOH X 9 . ? 12.243 -19.232 50.792 1.00 39.54 ? 738 HOH A O 1 HETATM 5092 O O . HOH X 9 . ? -13.916 -14.597 29.374 1.00 44.83 ? 739 HOH A O 1 HETATM 5093 O O . HOH X 9 . ? 7.209 -16.271 46.991 1.00 49.61 ? 740 HOH A O 1 HETATM 5094 O O . HOH X 9 . ? 21.819 10.398 32.854 1.00 24.61 ? 741 HOH A O 1 HETATM 5095 O O . HOH X 9 . ? -0.550 -15.688 24.791 1.00 35.44 ? 742 HOH A O 1 HETATM 5096 O O . HOH X 9 . ? -5.048 -16.941 47.157 1.00 40.63 ? 743 HOH A O 1 HETATM 5097 O O . HOH X 9 . ? 2.941 -23.168 46.913 1.00 80.11 ? 744 HOH A O 1 HETATM 5098 O O . HOH X 9 . ? 18.903 25.996 7.749 1.00 39.32 ? 745 HOH A O 1 HETATM 5099 O O . HOH X 9 . ? 9.627 9.104 48.151 1.00 32.21 ? 746 HOH A O 1 HETATM 5100 O O . HOH X 9 . ? -8.658 -14.883 13.335 1.00 47.88 ? 747 HOH A O 1 HETATM 5101 O O . HOH X 9 . ? -2.805 -7.858 8.588 1.00 32.91 ? 748 HOH A O 1 HETATM 5102 O O . HOH X 9 . ? 1.918 -7.045 53.647 1.00 44.06 ? 749 HOH A O 1 HETATM 5103 O O . HOH X 9 . ? 2.194 10.750 44.266 1.00 43.90 ? 750 HOH A O 1 HETATM 5104 O O . HOH X 9 . ? -10.244 -8.113 0.622 1.00 37.77 ? 751 HOH A O 1 HETATM 5105 O O . HOH X 9 . ? -3.825 12.068 -5.009 1.00 35.24 ? 752 HOH A O 1 HETATM 5106 O O . HOH X 9 . ? 17.693 1.359 44.291 1.00 32.94 ? 753 HOH A O 1 HETATM 5107 O O . HOH X 9 . ? -11.759 16.875 30.839 1.00 46.07 ? 754 HOH A O 1 HETATM 5108 O O . HOH X 9 . ? -6.879 2.251 -7.278 1.00 41.94 ? 755 HOH A O 1 HETATM 5109 O O . HOH X 9 . ? -0.958 -3.183 21.527 1.00 18.62 ? 756 HOH A O 1 HETATM 5110 O O . HOH X 9 . ? -10.675 11.007 9.287 1.00 39.23 ? 757 HOH A O 1 HETATM 5111 O O . HOH X 9 . ? -15.697 -8.949 11.330 1.00 33.15 ? 758 HOH A O 1 HETATM 5112 O O . HOH X 9 . ? 30.291 5.541 56.326 1.00 42.52 ? 759 HOH A O 1 HETATM 5113 O O . HOH X 9 . ? 29.510 -3.448 45.829 1.00 51.12 ? 760 HOH A O 1 HETATM 5114 O O . HOH X 9 . ? 0.149 -12.060 23.834 1.00 35.57 ? 761 HOH A O 1 HETATM 5115 O O . HOH X 9 . ? 18.298 18.216 29.447 1.00 46.60 ? 762 HOH A O 1 HETATM 5116 O O . HOH X 9 . ? 28.402 6.793 8.987 1.00 58.76 ? 763 HOH A O 1 HETATM 5117 O O . HOH X 9 . ? -5.617 7.079 27.660 1.00 30.05 ? 764 HOH A O 1 HETATM 5118 O O . HOH X 9 . ? 31.255 16.878 20.072 1.00 32.30 ? 765 HOH A O 1 HETATM 5119 O O . HOH X 9 . ? -19.995 -6.028 2.798 1.00 44.35 ? 766 HOH A O 1 HETATM 5120 O O . HOH X 9 . ? -5.079 -3.850 -10.158 1.00 58.47 ? 767 HOH A O 1 HETATM 5121 O O . HOH X 9 . ? 16.956 -1.860 50.920 1.00 57.09 ? 768 HOH A O 1 HETATM 5122 O O . HOH X 9 . ? 4.665 -8.786 51.781 1.00 53.62 ? 769 HOH A O 1 HETATM 5123 O O . HOH X 9 . ? 34.247 -5.933 11.019 1.00 70.48 ? 770 HOH A O 1 HETATM 5124 O O . HOH X 9 . ? 4.283 20.483 34.117 1.00 39.01 ? 771 HOH A O 1 HETATM 5125 O O . HOH X 9 . ? -5.583 -5.507 15.704 1.00 30.62 ? 772 HOH A O 1 HETATM 5126 O O . HOH X 9 . ? -2.446 11.743 37.581 1.00 30.23 ? 773 HOH A O 1 HETATM 5127 O O . HOH X 9 . ? 1.447 -17.086 -8.135 1.00 52.85 ? 774 HOH A O 1 HETATM 5128 O O . HOH X 9 . ? -16.885 -17.753 10.098 1.00 43.72 ? 775 HOH A O 1 HETATM 5129 O O . HOH X 9 . ? 4.791 -18.960 30.702 1.00 29.04 ? 776 HOH A O 1 HETATM 5130 O O . HOH X 9 . ? 29.924 6.165 33.802 1.00 40.86 ? 777 HOH A O 1 HETATM 5131 O O . HOH X 9 . ? -14.569 11.587 19.648 1.00 45.65 ? 778 HOH A O 1 HETATM 5132 O O . HOH X 9 . ? -17.252 -2.914 14.160 1.00 48.19 ? 779 HOH A O 1 HETATM 5133 O O . HOH X 9 . ? 21.119 -0.442 23.115 1.00 46.96 ? 780 HOH A O 1 HETATM 5134 O O . HOH X 9 . ? 19.269 -3.963 51.049 1.00 48.25 ? 781 HOH A O 1 HETATM 5135 O O . HOH X 9 . ? 6.188 -4.740 33.574 1.00 50.99 ? 782 HOH A O 1 HETATM 5136 O O . HOH X 9 . ? 6.671 22.218 27.507 1.00 34.15 ? 783 HOH A O 1 HETATM 5137 O O . HOH X 9 . ? 23.945 -13.421 18.014 1.00 44.70 ? 784 HOH A O 1 HETATM 5138 O O . HOH X 9 . ? -4.210 -12.555 15.030 1.00 40.35 ? 785 HOH A O 1 HETATM 5139 O O . HOH X 9 . ? -0.776 5.839 3.253 1.00 42.88 ? 786 HOH A O 1 HETATM 5140 O O . HOH X 9 . ? -2.758 -1.324 26.684 1.00 42.37 ? 787 HOH A O 1 HETATM 5141 O O . HOH X 9 . ? 30.042 8.902 32.065 1.00 34.38 ? 788 HOH A O 1 HETATM 5142 O O . HOH X 9 . ? 33.322 -19.387 31.012 1.00 40.07 ? 789 HOH A O 1 HETATM 5143 O O . HOH X 9 . ? -8.520 -20.411 28.769 1.00 44.85 ? 790 HOH A O 1 HETATM 5144 O O . HOH X 9 . ? -7.025 11.637 30.176 1.00 53.94 ? 791 HOH A O 1 HETATM 5145 O O . HOH X 9 . ? 1.395 9.896 55.240 1.00 40.51 ? 792 HOH A O 1 HETATM 5146 O O . HOH X 9 . ? 5.610 -34.278 36.013 1.00 52.15 ? 793 HOH A O 1 HETATM 5147 O O . HOH X 9 . ? 26.028 14.596 18.730 1.00 27.95 ? 794 HOH A O 1 HETATM 5148 O O . HOH X 9 . ? -5.927 -12.640 34.767 1.00 40.83 ? 795 HOH A O 1 HETATM 5149 O O . HOH X 9 . ? 22.343 13.226 30.454 1.00 24.95 ? 796 HOH A O 1 HETATM 5150 O O . HOH X 9 . ? -0.248 -16.315 -3.913 1.00 40.23 ? 797 HOH A O 1 HETATM 5151 O O . HOH X 9 . ? 0.249 20.483 12.226 1.00 27.38 ? 798 HOH A O 1 HETATM 5152 O O . HOH X 9 . ? -17.042 -1.270 12.179 1.00 44.93 ? 799 HOH A O 1 HETATM 5153 O O . HOH X 9 . ? 9.739 23.403 2.056 1.00 62.57 ? 800 HOH A O 1 HETATM 5154 O O . HOH X 9 . ? 18.785 -19.294 40.527 1.00 51.71 ? 801 HOH A O 1 HETATM 5155 O O . HOH X 9 . ? 23.865 3.172 50.343 1.00 49.26 ? 802 HOH A O 1 HETATM 5156 O O . HOH X 9 . ? 4.465 21.273 19.789 1.00 51.23 ? 803 HOH A O 1 HETATM 5157 O O . HOH X 9 . ? 1.216 -17.398 41.594 1.00 46.80 ? 804 HOH A O 1 HETATM 5158 O O . HOH X 9 . ? 13.192 -19.875 41.029 1.00 47.03 ? 805 HOH A O 1 HETATM 5159 O O . HOH X 9 . ? 5.370 -9.522 39.395 1.00 35.59 ? 806 HOH A O 1 HETATM 5160 O O . HOH X 9 . ? 20.648 -16.916 36.251 1.00 28.55 ? 807 HOH A O 1 HETATM 5161 O O . HOH X 9 . ? -5.251 5.502 25.264 1.00 38.48 ? 808 HOH A O 1 HETATM 5162 O O . HOH X 9 . ? 10.533 -22.757 16.681 1.00 49.56 ? 809 HOH A O 1 HETATM 5163 O O . HOH X 9 . ? -2.487 -25.708 37.595 1.00 79.38 ? 810 HOH A O 1 HETATM 5164 O O . HOH X 9 . ? -2.356 -31.313 11.305 1.00 57.84 ? 811 HOH A O 1 HETATM 5165 O O . HOH X 9 . ? 29.757 -1.502 11.530 1.00 45.15 ? 812 HOH A O 1 HETATM 5166 O O . HOH X 9 . ? 11.352 -13.058 4.104 1.00 63.82 ? 813 HOH A O 1 HETATM 5167 O O . HOH X 9 . ? 7.910 -23.668 2.801 1.00 57.37 ? 814 HOH A O 1 HETATM 5168 O O . HOH X 9 . ? -8.165 22.685 26.657 1.00 74.59 ? 815 HOH A O 1 HETATM 5169 O O . HOH X 9 . ? -2.464 23.123 13.576 1.00 49.27 ? 816 HOH A O 1 HETATM 5170 O O . HOH X 9 . ? -14.117 12.650 29.793 1.00 54.93 ? 817 HOH A O 1 HETATM 5171 O O . HOH X 9 . ? -17.793 -7.565 -2.168 1.00 44.80 ? 818 HOH A O 1 HETATM 5172 O O . HOH X 9 . ? -3.829 -22.580 49.906 1.00 61.84 ? 819 HOH A O 1 HETATM 5173 O O . HOH X 9 . ? 19.554 16.175 15.684 1.00 33.40 ? 820 HOH A O 1 HETATM 5174 O O . HOH X 9 . ? 15.993 9.430 2.391 1.00 44.49 ? 821 HOH A O 1 HETATM 5175 O O . HOH X 9 . ? 10.053 16.032 16.439 1.00 38.80 ? 822 HOH A O 1 HETATM 5176 O O . HOH X 9 . ? -3.817 22.170 3.068 1.00 51.32 ? 823 HOH A O 1 HETATM 5177 O O . HOH X 9 . ? 2.794 -11.414 13.973 1.00 31.34 ? 824 HOH A O 1 HETATM 5178 O O . HOH X 9 . ? -15.490 9.327 20.532 1.00 58.00 ? 825 HOH A O 1 HETATM 5179 O O . HOH X 9 . ? -14.343 -4.108 17.081 1.00 42.86 ? 826 HOH A O 1 HETATM 5180 O O . HOH X 9 . ? 3.864 17.708 -3.554 1.00 46.55 ? 827 HOH A O 1 HETATM 5181 O O . HOH X 9 . ? -9.304 -7.188 10.091 1.00 39.01 ? 828 HOH A O 1 HETATM 5182 O O . HOH X 9 . ? 29.961 12.400 23.251 1.00 49.34 ? 829 HOH A O 1 HETATM 5183 O O . HOH X 9 . ? -0.209 -7.814 47.110 1.00 64.49 ? 830 HOH A O 1 HETATM 5184 O O . HOH X 9 . ? -24.672 8.616 17.082 1.00 48.68 ? 831 HOH A O 1 HETATM 5185 O O . HOH X 9 . ? -16.207 -7.599 8.188 1.00 42.69 ? 832 HOH A O 1 HETATM 5186 O O . HOH X 9 . ? -12.580 -10.334 18.804 1.00 33.40 ? 833 HOH A O 1 HETATM 5187 O O . HOH X 9 . ? 15.633 -0.230 5.837 1.00 35.49 ? 834 HOH A O 1 HETATM 5188 O O . HOH X 9 . ? 26.591 6.097 31.182 1.00 20.26 ? 835 HOH A O 1 HETATM 5189 O O . HOH X 9 . ? 10.673 5.577 4.301 1.00 44.55 ? 836 HOH A O 1 HETATM 5190 O O . HOH X 9 . ? 17.591 14.517 18.377 1.00 28.91 ? 837 HOH A O 1 HETATM 5191 O O . HOH X 9 . ? -6.452 6.281 49.613 1.00 57.20 ? 838 HOH A O 1 HETATM 5192 O O . HOH X 9 . ? 0.878 -17.938 28.094 1.00 33.01 ? 839 HOH A O 1 HETATM 5193 O O . HOH X 9 . ? 12.699 16.525 17.639 1.00 35.95 ? 840 HOH A O 1 HETATM 5194 O O . HOH X 9 . ? -7.522 10.642 7.300 1.00 40.90 ? 841 HOH A O 1 HETATM 5195 O O . HOH X 9 . ? 17.457 -9.599 37.117 1.00 24.86 ? 842 HOH A O 1 HETATM 5196 O O . HOH X 9 . ? 9.265 -22.464 33.479 1.00 30.03 ? 843 HOH A O 1 HETATM 5197 O O . HOH X 9 . ? -3.951 -18.421 18.781 1.00 33.62 ? 844 HOH A O 1 HETATM 5198 O O . HOH X 9 . ? 15.471 -17.611 15.145 1.00 31.31 ? 845 HOH A O 1 HETATM 5199 O O . HOH X 9 . ? 9.526 20.401 34.565 1.00 41.32 ? 846 HOH A O 1 HETATM 5200 O O . HOH X 9 . ? -10.792 15.673 14.928 1.00 36.64 ? 847 HOH A O 1 HETATM 5201 O O . HOH X 9 . ? 23.825 -15.503 34.796 1.00 35.86 ? 848 HOH A O 1 HETATM 5202 O O . HOH X 9 . ? 2.186 -24.817 9.163 1.00 58.79 ? 849 HOH A O 1 HETATM 5203 O O . HOH X 9 . ? -14.564 -15.587 16.440 1.00 56.34 ? 850 HOH A O 1 HETATM 5204 O O . HOH X 9 . ? 3.189 21.053 30.841 1.00 35.75 ? 851 HOH A O 1 HETATM 5205 O O . HOH X 9 . ? -7.633 -5.993 3.161 1.00 43.39 ? 852 HOH A O 1 HETATM 5206 O O . HOH X 9 . ? 16.690 -20.267 35.100 1.00 31.32 ? 853 HOH A O 1 HETATM 5207 O O . HOH X 9 . ? 1.025 0.214 -4.442 1.00 60.05 ? 854 HOH A O 1 HETATM 5208 O O . HOH X 9 . ? 21.286 -19.391 37.672 1.00 48.25 ? 855 HOH A O 1 HETATM 5209 O O . HOH X 9 . ? 15.724 23.104 16.489 1.00 29.27 ? 856 HOH A O 1 HETATM 5210 O O . HOH X 9 . ? -15.534 -5.303 19.251 1.00 41.84 ? 857 HOH A O 1 HETATM 5211 O O . HOH X 9 . ? 19.030 16.202 31.529 1.00 50.99 ? 858 HOH A O 1 HETATM 5212 O O . HOH X 9 . ? -3.048 20.085 30.218 1.00 33.29 ? 859 HOH A O 1 HETATM 5213 O O . HOH X 9 . ? -17.254 -21.260 13.485 1.00 44.99 ? 860 HOH A O 1 HETATM 5214 O O . HOH X 9 . ? 10.793 -22.225 31.075 1.00 42.50 ? 861 HOH A O 1 HETATM 5215 O O . HOH X 9 . ? 15.824 10.870 -0.075 1.00 39.45 ? 862 HOH A O 1 HETATM 5216 O O . HOH X 9 . ? 2.071 -21.037 15.224 1.00 34.23 ? 863 HOH A O 1 HETATM 5217 O O . HOH X 9 . ? 5.243 -1.530 33.714 1.00 62.37 ? 864 HOH A O 1 HETATM 5218 O O . HOH X 9 . ? 18.968 15.247 35.961 1.00 62.59 ? 865 HOH A O 1 HETATM 5219 O O . HOH X 9 . ? 29.331 -7.762 14.288 1.00 42.27 ? 866 HOH A O 1 HETATM 5220 O O . HOH X 9 . ? -14.732 -7.661 19.570 1.00 45.56 ? 867 HOH A O 1 HETATM 5221 O O . HOH X 9 . ? 1.219 -14.566 26.263 1.00 29.51 ? 868 HOH A O 1 HETATM 5222 O O . HOH X 9 . ? 20.756 16.435 13.290 1.00 61.02 ? 869 HOH A O 1 HETATM 5223 O O . HOH X 9 . ? -18.957 5.122 -1.986 1.00 55.61 ? 870 HOH A O 1 HETATM 5224 O O . HOH X 9 . ? 1.254 -16.550 38.782 1.00 29.25 ? 871 HOH A O 1 HETATM 5225 O O . HOH X 9 . ? -0.925 -13.024 1.548 1.00 37.94 ? 872 HOH A O 1 HETATM 5226 O O . HOH X 9 . ? -6.478 7.757 43.759 1.00 84.44 ? 873 HOH A O 1 HETATM 5227 O O . HOH X 9 . ? 4.401 -11.365 49.002 1.00 58.36 ? 874 HOH A O 1 HETATM 5228 O O . HOH X 9 . ? 21.613 -18.103 44.468 1.00 39.17 ? 875 HOH A O 1 HETATM 5229 O O . HOH X 9 . ? 11.169 16.489 50.212 1.00 54.81 ? 876 HOH A O 1 HETATM 5230 O O . HOH X 9 . ? -2.233 -9.203 39.219 1.00 39.37 ? 877 HOH A O 1 HETATM 5231 O O . HOH X 9 . ? -4.065 12.072 1.385 1.00 49.23 ? 878 HOH A O 1 HETATM 5232 O O . HOH X 9 . ? 14.619 -11.458 56.830 1.00 63.36 ? 879 HOH A O 1 HETATM 5233 O O . HOH X 9 . ? -8.873 -22.595 33.597 1.00 50.98 ? 880 HOH A O 1 HETATM 5234 O O . HOH X 9 . ? 21.732 -20.833 34.114 1.00 45.85 ? 881 HOH A O 1 HETATM 5235 O O . HOH X 9 . ? 0.242 3.527 2.295 1.00 46.16 ? 882 HOH A O 1 HETATM 5236 O O . HOH X 9 . ? 22.540 13.143 49.580 1.00 56.48 ? 883 HOH A O 1 HETATM 5237 O O . HOH X 9 . ? 17.750 19.951 11.835 1.00 56.35 ? 884 HOH A O 1 HETATM 5238 O O . HOH X 9 . ? 27.894 9.922 18.790 1.00 38.91 ? 885 HOH A O 1 HETATM 5239 O O . HOH X 9 . ? -15.359 7.759 0.712 1.00 45.99 ? 886 HOH A O 1 HETATM 5240 O O . HOH X 9 . ? 14.136 -7.738 5.410 1.00 61.12 ? 887 HOH A O 1 HETATM 5241 O O . HOH X 9 . ? 30.363 12.257 18.189 1.00 55.08 ? 888 HOH A O 1 HETATM 5242 O O . HOH X 9 . ? 24.270 -3.775 23.063 1.00 32.13 ? 889 HOH A O 1 HETATM 5243 O O . HOH X 9 . ? 40.618 -11.415 36.135 1.00 41.02 ? 890 HOH A O 1 HETATM 5244 O O . HOH X 9 . ? 37.733 -2.577 40.889 1.00 58.25 ? 891 HOH A O 1 HETATM 5245 O O . HOH X 9 . ? -3.303 -23.025 12.775 1.00 40.12 ? 892 HOH A O 1 HETATM 5246 O O . HOH X 9 . ? 29.102 17.316 18.699 1.00 49.06 ? 893 HOH A O 1 HETATM 5247 O O . HOH X 9 . ? 12.225 18.156 37.234 1.00 61.07 ? 894 HOH A O 1 HETATM 5248 O O . HOH X 9 . ? -6.259 -3.169 24.921 1.00 44.42 ? 895 HOH A O 1 HETATM 5249 O O . HOH X 9 . ? -1.292 -18.122 25.687 1.00 60.11 ? 896 HOH A O 1 HETATM 5250 O O . HOH X 9 . ? -4.355 5.307 29.098 1.00 59.65 ? 897 HOH A O 1 HETATM 5251 O O . HOH X 9 . ? 0.867 20.560 38.856 1.00 51.77 ? 898 HOH A O 1 HETATM 5252 O O . HOH X 9 . ? 0.198 23.850 35.892 1.00 56.74 ? 899 HOH A O 1 HETATM 5253 O O . HOH X 9 . ? 29.538 -0.035 20.371 1.00 34.62 ? 900 HOH A O 1 HETATM 5254 O O . HOH X 9 . ? 8.732 17.491 40.008 1.00 50.28 ? 901 HOH A O 1 HETATM 5255 O O . HOH X 9 . ? -0.804 6.349 -1.631 1.00 54.78 ? 902 HOH A O 1 HETATM 5256 O O . HOH X 9 . ? 20.648 16.409 29.638 1.00 50.06 ? 903 HOH A O 1 HETATM 5257 O O . HOH X 9 . ? 22.915 16.466 31.070 1.00 48.15 ? 904 HOH A O 1 HETATM 5258 O O . HOH X 9 . ? 27.525 -1.008 14.479 1.00 40.24 ? 905 HOH A O 1 HETATM 5259 O O . HOH X 9 . ? -21.012 1.499 3.747 1.00 61.44 ? 906 HOH A O 1 HETATM 5260 O O . HOH X 9 . ? -0.862 22.384 38.180 1.00 67.56 ? 907 HOH A O 1 HETATM 5261 O O . HOH X 9 . ? 27.319 7.430 14.980 1.00 42.97 ? 908 HOH A O 1 HETATM 5262 O O . HOH X 9 . ? 26.618 -3.389 45.367 1.00 57.59 ? 909 HOH A O 1 HETATM 5263 O O . HOH X 9 . ? 24.207 12.635 9.785 1.00 52.14 ? 910 HOH A O 1 HETATM 5264 O O . HOH X 9 . ? 14.103 -7.426 54.162 1.00 56.22 ? 911 HOH A O 1 HETATM 5265 O O . HOH X 9 . ? -3.199 8.037 26.265 1.00 42.42 ? 912 HOH A O 1 HETATM 5266 O O . HOH X 9 . ? 17.662 -4.246 26.866 1.00 37.57 ? 913 HOH A O 1 HETATM 5267 O O . HOH X 9 . ? 28.407 -17.048 40.782 1.00 52.49 ? 914 HOH A O 1 HETATM 5268 O O . HOH X 9 . ? -6.897 -6.991 30.799 1.00 51.39 ? 915 HOH A O 1 HETATM 5269 O O . HOH X 9 . ? -19.367 19.401 7.729 1.00 52.00 ? 916 HOH A O 1 HETATM 5270 O O . HOH X 9 . ? -1.019 33.179 30.707 1.00 59.62 ? 917 HOH A O 1 HETATM 5271 O O . HOH X 9 . ? -0.111 30.646 31.431 1.00 45.10 ? 918 HOH A O 1 HETATM 5272 O O . HOH X 9 . ? 34.744 3.667 30.047 1.00 39.29 ? 919 HOH A O 1 HETATM 5273 O O . HOH X 9 . ? -6.526 2.805 25.704 1.00 44.79 ? 920 HOH A O 1 HETATM 5274 O O . HOH X 9 . ? -14.952 9.330 13.336 1.00 43.74 ? 921 HOH A O 1 HETATM 5275 O O . HOH X 9 . ? 23.055 10.550 40.542 1.00 45.98 ? 922 HOH A O 1 HETATM 5276 O O . HOH X 9 . ? 8.751 -3.370 -0.310 1.00 52.11 ? 923 HOH A O 1 HETATM 5277 O O . HOH X 9 . ? -1.362 17.479 10.447 1.00 45.48 ? 924 HOH A O 1 HETATM 5278 O O . HOH X 9 . ? -4.539 -6.557 32.188 1.00 50.06 ? 925 HOH A O 1 HETATM 5279 O O . HOH X 9 . ? 31.803 4.117 44.496 1.00 59.56 ? 926 HOH A O 1 HETATM 5280 O O . HOH X 9 . ? -19.646 13.899 6.526 1.00 59.00 ? 927 HOH A O 1 HETATM 5281 O O . HOH X 9 . ? 10.762 -0.944 53.268 1.00 63.07 ? 928 HOH A O 1 HETATM 5282 O O . HOH X 9 . ? -12.930 -13.093 13.825 1.00 47.62 ? 929 HOH A O 1 HETATM 5283 O O . HOH X 9 . ? -4.118 -18.255 30.807 1.00 48.76 ? 930 HOH A O 1 HETATM 5284 O O . HOH X 9 . ? 5.260 11.223 38.343 1.00 46.27 ? 931 HOH A O 1 HETATM 5285 O O . HOH X 9 . ? -17.797 4.112 10.804 1.00 49.33 ? 932 HOH A O 1 HETATM 5286 O O . HOH X 9 . ? 5.384 6.568 32.511 1.00 50.01 ? 933 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 ASP 89 89 89 ASP ASP 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 GLN 204 204 204 GLN GLN 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 ARG 232 232 232 ARG ARG 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 GLN 286 286 286 GLN GLN A . n A 1 287 TRP 287 287 287 TRP TRP A . n A 1 288 ASP 288 288 288 ASP ASP A . n A 1 289 GLY 289 289 289 GLY GLY A . n A 1 290 GLU 290 290 290 GLU GLU A . n A 1 291 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 VAL 304 304 304 VAL VAL 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 MET 547 547 547 MET MET A . n A 1 548 SER 548 548 548 SER SER A . n A 1 549 PHE 549 549 549 PHE PHE A . n A 1 550 SER 550 550 550 SER SER A . n A 1 551 ARG 551 551 551 ARG ARG A . n A 1 552 LEU 552 552 552 LEU LEU A . n A 1 553 ILE 553 553 553 ILE ILE A . n A 1 554 CYS 554 554 554 CYS CYS A . n A 1 555 ASP 555 555 555 ASP ASP A . n A 1 556 ASN 556 556 556 ASN ASN A . n A 1 557 THR 557 557 557 THR THR A . n A 1 558 HIS 558 558 558 HIS HIS A . n A 1 559 ILE 559 559 559 ILE ILE A . n A 1 560 THR 560 560 560 THR THR A . n A 1 561 LYS 561 561 561 LYS LYS A . n A 1 562 VAL 562 562 562 VAL VAL A . n A 1 563 PRO 563 563 563 PRO PRO A . n A 1 564 LEU 564 564 564 LEU LEU A . n A 1 565 HIS 565 565 565 HIS HIS A . n A 1 566 ALA 566 566 566 ALA ALA A . n A 1 567 PHE 567 567 567 PHE PHE A . n A 1 568 GLN 568 568 568 GLN GLN A . n A 1 569 ALA 569 569 569 ALA ALA A . n A 1 570 ASN 570 570 570 ASN ASN A . n A 1 571 ASN 571 571 571 ASN ASN A . n A 1 572 TYR 572 572 572 TYR TYR A . n A 1 573 PRO 573 573 573 PRO PRO A . n A 1 574 HIS 574 574 574 HIS HIS A . n A 1 575 ASP 575 575 575 ASP ASP A . n A 1 576 PHE 576 576 576 PHE PHE A . n A 1 577 VAL 577 577 577 VAL VAL A . n A 1 578 ASP 578 578 578 ASP ASP A . n A 1 579 CYS 579 579 579 CYS CYS A . n A 1 580 SER 580 580 580 SER SER A . n A 1 581 ALA 581 581 581 ALA ALA A . n A 1 582 VAL 582 582 582 VAL VAL A . n A 1 583 ASP 583 583 583 ASP ASP A . n A 1 584 LYS 584 584 584 LYS LYS A . n A 1 585 LEU 585 585 585 LEU LEU A . n A 1 586 ASP 586 586 586 ASP ASP A . n A 1 587 LEU 587 587 587 LEU LEU A . n A 1 588 SER 588 588 588 SER SER A . n A 1 589 PRO 589 589 589 PRO PRO A . n A 1 590 TRP 590 590 590 TRP TRP A . n A 1 591 ALA 591 591 591 ALA ALA A . n A 1 592 SER 592 592 592 SER SER A . n A 1 593 ARG 593 593 593 ARG ARG A . n A 1 594 GLU 594 594 594 GLU GLU A . n A 1 595 ASN 595 595 595 ASN ASN A . n # 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 241 A ASN 241 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 332 A ASN 332 ? ASN 'GLYCOSYLATION SITE' 5 A SEP 198 A SEP 198 ? SER PHOSPHOSERINE # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 O ? A ASP 110 ? A ASP 110 ? 1_555 CA ? L CA . ? A CA 606 ? 1_555 OD1 ? A ASP 110 ? A ASP 110 ? 1_555 71.0 ? 2 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 73.4 ? 3 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_555 138.3 ? 4 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_555 135.2 ? 5 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_555 149.5 ? 6 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 72.1 ? 7 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_555 115.5 ? 8 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 79.7 ? 9 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 96.8 ? 10 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 96.3 ? 11 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_555 144.6 ? 12 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 76.9 ? 13 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_555 141.8 ? 14 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 73.1 ? 15 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 71.9 ? 16 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 83.3 ? 17 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 79.1 ? 18 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_555 117.6 ? 19 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 88.1 ? 20 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_555 144.8 ? 21 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 76.2 ? 22 NE2 ? A HIS 351 ? A HIS 351 ? 1_555 FE ? U HEM . ? A HEM 615 ? 1_555 NA ? U HEM . ? A HEM 615 ? 1_555 101.0 ? 23 NE2 ? A HIS 351 ? A HIS 351 ? 1_555 FE ? U HEM . ? A HEM 615 ? 1_555 NB ? U HEM . ? A HEM 615 ? 1_555 97.6 ? 24 NA ? U HEM . ? A HEM 615 ? 1_555 FE ? U HEM . ? A HEM 615 ? 1_555 NB ? U HEM . ? A HEM 615 ? 1_555 90.6 ? 25 NE2 ? A HIS 351 ? A HIS 351 ? 1_555 FE ? U HEM . ? A HEM 615 ? 1_555 NC ? U HEM . ? A HEM 615 ? 1_555 91.6 ? 26 NA ? U HEM . ? A HEM 615 ? 1_555 FE ? U HEM . ? A HEM 615 ? 1_555 NC ? U HEM . ? A HEM 615 ? 1_555 167.3 ? 27 NB ? U HEM . ? A HEM 615 ? 1_555 FE ? U HEM . ? A HEM 615 ? 1_555 NC ? U HEM . ? A HEM 615 ? 1_555 85.9 ? 28 NE2 ? A HIS 351 ? A HIS 351 ? 1_555 FE ? U HEM . ? A HEM 615 ? 1_555 ND ? U HEM . ? A HEM 615 ? 1_555 92.1 ? 29 NA ? U HEM . ? A HEM 615 ? 1_555 FE ? U HEM . ? A HEM 615 ? 1_555 ND ? U HEM . ? A HEM 615 ? 1_555 92.2 ? 30 NB ? U HEM . ? A HEM 615 ? 1_555 FE ? U HEM . ? A HEM 615 ? 1_555 ND ? U HEM . ? A HEM 615 ? 1_555 169.3 ? 31 NC ? U HEM . ? A HEM 615 ? 1_555 FE ? U HEM . ? A HEM 615 ? 1_555 ND ? U HEM . ? A HEM 615 ? 1_555 89.1 ? 32 NE2 ? A HIS 351 ? A HIS 351 ? 1_555 FE ? U HEM . ? A HEM 615 ? 1_555 O9 ? W SHA . ? A SHA 617 ? 1_555 178.9 ? 33 NA ? U HEM . ? A HEM 615 ? 1_555 FE ? U HEM . ? A HEM 615 ? 1_555 O9 ? W SHA . ? A SHA 617 ? 1_555 80.1 ? 34 NB ? U HEM . ? A HEM 615 ? 1_555 FE ? U HEM . ? A HEM 615 ? 1_555 O9 ? W SHA . ? A SHA 617 ? 1_555 82.7 ? 35 NC ? U HEM . ? A HEM 615 ? 1_555 FE ? U HEM . ? A HEM 615 ? 1_555 O9 ? W SHA . ? A SHA 617 ? 1_555 87.3 ? 36 ND ? U HEM . ? A HEM 615 ? 1_555 FE ? U HEM . ? A HEM 615 ? 1_555 O9 ? W SHA . ? A SHA 617 ? 1_555 87.5 ? # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2009-01-27 2 'Structure model' 1 1 2011-07-13 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Non-polymer description' 2 2 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal DENZO 'data reduction' . ? 1 MOLREP phasing . ? 2 REFMAC refinement 5.2.0019 ? 3 AUTOMAR 'data reduction' . ? 4 SCALEPACK 'data scaling' . ? 5 # _pdbx_entry_details.sequence_details ;A SEQUENCE DATABASE REFERENCE FOR THIS PROTEIN DOES NOT CURRENTLY EXIST IN THE UNIPROT. THIS SEQUENCE WILL BE DEPOSITED IN THE UNIPROT. ; _pdbx_entry_details.entry_id 3FNL _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ? # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 OD2 A ASP 108 ? ? CMD A HEM 615 ? ? 1.50 2 1 OE2 A GLU 258 ? ? CMB A HEM 615 ? ? 1.56 # 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 CYS 167 ? ? N A PRO 168 ? ? CA A PRO 168 ? ? 129.62 119.30 10.32 1.50 Y 2 1 N A GLU 258 ? ? CA A GLU 258 ? ? CB A GLU 258 ? ? 121.41 110.60 10.81 1.80 N 3 1 C A THR 486 ? ? N A PRO 487 ? ? CA A PRO 487 ? ? 131.33 119.30 12.03 1.50 Y # 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 VAL A 4 ? ? -20.70 -31.64 2 1 CYS A 6 ? ? -39.22 94.90 3 1 ALA A 8 ? ? -83.55 -151.04 4 1 PRO A 9 ? ? -15.13 83.12 5 1 GLU A 17 ? ? 55.35 111.21 6 1 ASN A 18 ? ? 77.73 -8.30 7 1 ALA A 56 ? ? -159.20 -35.25 8 1 GLU A 118 ? ? -99.70 -86.69 9 1 ASN A 122 ? ? 149.37 121.06 10 1 GLU A 123 ? ? -176.68 149.87 11 1 THR A 127 ? ? -145.62 -28.46 12 1 ASP A 137 ? ? 50.64 -126.67 13 1 VAL A 166 ? ? -69.88 -168.80 14 1 CYS A 167 ? ? 42.48 -142.69 15 1 PRO A 168 ? ? -40.79 -149.47 16 1 THR A 169 ? ? -142.49 -112.87 17 1 PRO A 170 ? ? 3.55 -167.53 18 1 GLN A 173 ? ? -127.95 -111.88 19 1 SER A 174 ? ? 16.61 -80.97 20 1 LEU A 187 ? ? -67.94 94.90 21 1 ASP A 188 ? ? -143.32 15.54 22 1 PRO A 209 ? ? -86.42 38.06 23 1 ASP A 389 ? ? -159.57 36.65 24 1 LYS A 485 ? ? 70.83 -25.62 25 1 ARG A 504 ? ? 59.78 14.01 26 1 PRO A 589 ? ? -57.38 -6.50 27 1 GLU A 594 ? ? -63.89 -78.50 # 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 'IODIDE ION' IOD 6 'PROTOPORPHYRIN IX CONTAINING FE' HEM 7 'THIOCYANATE ION' SCN 8 'SALICYLHYDROXAMIC ACID' SHA 9 water HOH # 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 5 NAG NAG A . H 2 NAG 2 602 6 NAG NAG A . I 3 MAN 3 603 9 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 1 CA CA A . M 5 IOD 1 607 1 IOD IOD A . N 5 IOD 1 608 2 IOD IOD A . O 5 IOD 1 609 3 IOD IOD A . P 5 IOD 1 610 4 IOD IOD A . Q 5 IOD 1 611 5 IOD IOD A . R 5 IOD 1 612 6 IOD IOD A . S 5 IOD 1 613 7 IOD IOD A . T 5 IOD 1 614 8 IOD IOD A . U 6 HEM 1 615 605 HEM HEM A . V 7 SCN 1 616 615 SCN SCN A . W 8 SHA 1 617 6 SHA SHA A . X 9 HOH 1 618 2 HOH HOH A . X 9 HOH 2 619 3 HOH HOH A . X 9 HOH 3 620 4 HOH HOH A . X 9 HOH 4 621 5 HOH HOH A . X 9 HOH 5 622 6 HOH HOH A . X 9 HOH 6 623 7 HOH HOH A . X 9 HOH 7 624 8 HOH HOH A . X 9 HOH 8 625 9 HOH HOH A . X 9 HOH 9 626 10 HOH HOH A . X 9 HOH 10 627 11 HOH HOH A . X 9 HOH 11 628 12 HOH HOH A . X 9 HOH 12 629 13 HOH HOH A . X 9 HOH 13 630 14 HOH HOH A . X 9 HOH 14 631 15 HOH HOH A . X 9 HOH 15 632 16 HOH HOH A . X 9 HOH 16 633 17 HOH HOH A . X 9 HOH 17 634 18 HOH HOH A . X 9 HOH 18 635 19 HOH HOH A . X 9 HOH 19 636 20 HOH HOH A . X 9 HOH 20 637 21 HOH HOH A . X 9 HOH 21 638 22 HOH HOH A . X 9 HOH 22 639 23 HOH HOH A . X 9 HOH 23 640 24 HOH HOH A . X 9 HOH 24 641 25 HOH HOH A . X 9 HOH 25 642 26 HOH HOH A . X 9 HOH 26 643 27 HOH HOH A . X 9 HOH 27 644 28 HOH HOH A . X 9 HOH 28 645 29 HOH HOH A . X 9 HOH 29 646 30 HOH HOH A . X 9 HOH 30 647 31 HOH HOH A . X 9 HOH 31 648 32 HOH HOH A . X 9 HOH 32 649 33 HOH HOH A . X 9 HOH 33 650 34 HOH HOH A . X 9 HOH 34 651 36 HOH HOH A . X 9 HOH 35 652 37 HOH HOH A . X 9 HOH 36 653 38 HOH HOH A . X 9 HOH 37 654 39 HOH HOH A . X 9 HOH 38 655 40 HOH HOH A . X 9 HOH 39 656 41 HOH HOH A . X 9 HOH 40 657 42 HOH HOH A . X 9 HOH 41 658 43 HOH HOH A . X 9 HOH 42 659 44 HOH HOH A . X 9 HOH 43 660 45 HOH HOH A . X 9 HOH 44 661 46 HOH HOH A . X 9 HOH 45 662 47 HOH HOH A . X 9 HOH 46 663 48 HOH HOH A . X 9 HOH 47 664 49 HOH HOH A . X 9 HOH 48 665 50 HOH HOH A . X 9 HOH 49 666 51 HOH HOH A . X 9 HOH 50 667 52 HOH HOH A . X 9 HOH 51 668 53 HOH HOH A . X 9 HOH 52 669 54 HOH HOH A . X 9 HOH 53 670 55 HOH HOH A . X 9 HOH 54 671 56 HOH HOH A . X 9 HOH 55 672 57 HOH HOH A . X 9 HOH 56 673 58 HOH HOH A . X 9 HOH 57 674 59 HOH HOH A . X 9 HOH 58 675 60 HOH HOH A . X 9 HOH 59 676 61 HOH HOH A . X 9 HOH 60 677 62 HOH HOH A . X 9 HOH 61 678 63 HOH HOH A . X 9 HOH 62 679 64 HOH HOH A . X 9 HOH 63 680 65 HOH HOH A . X 9 HOH 64 681 66 HOH HOH A . X 9 HOH 65 682 67 HOH HOH A . X 9 HOH 66 683 68 HOH HOH A . X 9 HOH 67 684 69 HOH HOH A . X 9 HOH 68 685 70 HOH HOH A . X 9 HOH 69 686 71 HOH HOH A . X 9 HOH 70 687 72 HOH HOH A . X 9 HOH 71 688 73 HOH HOH A . X 9 HOH 72 689 74 HOH HOH A . X 9 HOH 73 690 75 HOH HOH A . X 9 HOH 74 691 76 HOH HOH A . X 9 HOH 75 692 77 HOH HOH A . X 9 HOH 76 693 79 HOH HOH A . X 9 HOH 77 694 80 HOH HOH A . X 9 HOH 78 695 81 HOH HOH A . X 9 HOH 79 696 82 HOH HOH A . X 9 HOH 80 697 83 HOH HOH A . X 9 HOH 81 698 84 HOH HOH A . X 9 HOH 82 699 85 HOH HOH A . X 9 HOH 83 700 87 HOH HOH A . X 9 HOH 84 701 88 HOH HOH A . X 9 HOH 85 702 89 HOH HOH A . X 9 HOH 86 703 90 HOH HOH A . X 9 HOH 87 704 91 HOH HOH A . X 9 HOH 88 705 92 HOH HOH A . X 9 HOH 89 706 93 HOH HOH A . X 9 HOH 90 707 94 HOH HOH A . X 9 HOH 91 708 95 HOH HOH A . X 9 HOH 92 709 96 HOH HOH A . X 9 HOH 93 710 97 HOH HOH A . X 9 HOH 94 711 98 HOH HOH A . X 9 HOH 95 712 99 HOH HOH A . X 9 HOH 96 713 100 HOH HOH A . X 9 HOH 97 714 101 HOH HOH A . X 9 HOH 98 715 102 HOH HOH A . X 9 HOH 99 716 103 HOH HOH A . X 9 HOH 100 717 104 HOH HOH A . X 9 HOH 101 718 105 HOH HOH A . X 9 HOH 102 719 106 HOH HOH A . X 9 HOH 103 720 107 HOH HOH A . X 9 HOH 104 721 109 HOH HOH A . X 9 HOH 105 722 110 HOH HOH A . X 9 HOH 106 723 111 HOH HOH A . X 9 HOH 107 724 112 HOH HOH A . X 9 HOH 108 725 113 HOH HOH A . X 9 HOH 109 726 114 HOH HOH A . X 9 HOH 110 727 115 HOH HOH A . X 9 HOH 111 728 116 HOH HOH A . X 9 HOH 112 729 117 HOH HOH A . X 9 HOH 113 730 118 HOH HOH A . X 9 HOH 114 731 119 HOH HOH A . X 9 HOH 115 732 120 HOH HOH A . X 9 HOH 116 733 121 HOH HOH A . X 9 HOH 117 734 122 HOH HOH A . X 9 HOH 118 735 123 HOH HOH A . X 9 HOH 119 736 124 HOH HOH A . X 9 HOH 120 737 125 HOH HOH A . X 9 HOH 121 738 126 HOH HOH A . X 9 HOH 122 739 127 HOH HOH A . X 9 HOH 123 740 128 HOH HOH A . X 9 HOH 124 741 130 HOH HOH A . X 9 HOH 125 742 131 HOH HOH A . X 9 HOH 126 743 132 HOH HOH A . X 9 HOH 127 744 133 HOH HOH A . X 9 HOH 128 745 134 HOH HOH A . X 9 HOH 129 746 135 HOH HOH A . X 9 HOH 130 747 136 HOH HOH A . X 9 HOH 131 748 137 HOH HOH A . X 9 HOH 132 749 138 HOH HOH A . X 9 HOH 133 750 139 HOH HOH A . X 9 HOH 134 751 140 HOH HOH A . X 9 HOH 135 752 141 HOH HOH A . X 9 HOH 136 753 142 HOH HOH A . X 9 HOH 137 754 143 HOH HOH A . X 9 HOH 138 755 144 HOH HOH A . X 9 HOH 139 756 145 HOH HOH A . X 9 HOH 140 757 146 HOH HOH A . X 9 HOH 141 758 147 HOH HOH A . X 9 HOH 142 759 148 HOH HOH A . X 9 HOH 143 760 149 HOH HOH A . X 9 HOH 144 761 150 HOH HOH A . X 9 HOH 145 762 151 HOH HOH A . X 9 HOH 146 763 152 HOH HOH A . X 9 HOH 147 764 153 HOH HOH A . X 9 HOH 148 765 154 HOH HOH A . X 9 HOH 149 766 155 HOH HOH A . X 9 HOH 150 767 156 HOH HOH A . X 9 HOH 151 768 157 HOH HOH A . X 9 HOH 152 769 158 HOH HOH A . X 9 HOH 153 770 159 HOH HOH A . X 9 HOH 154 771 160 HOH HOH A . X 9 HOH 155 772 162 HOH HOH A . X 9 HOH 156 773 163 HOH HOH A . X 9 HOH 157 774 164 HOH HOH A . X 9 HOH 158 775 165 HOH HOH A . X 9 HOH 159 776 166 HOH HOH A . X 9 HOH 160 777 167 HOH HOH A . X 9 HOH 161 778 168 HOH HOH A . X 9 HOH 162 779 169 HOH HOH A . X 9 HOH 163 780 170 HOH HOH A . X 9 HOH 164 781 171 HOH HOH A . X 9 HOH 165 782 172 HOH HOH A . X 9 HOH 166 783 173 HOH HOH A . X 9 HOH 167 784 174 HOH HOH A . X 9 HOH 168 785 175 HOH HOH A . X 9 HOH 169 786 176 HOH HOH A . X 9 HOH 170 787 177 HOH HOH A . X 9 HOH 171 788 178 HOH HOH A . X 9 HOH 172 789 179 HOH HOH A . X 9 HOH 173 790 180 HOH HOH A . X 9 HOH 174 791 181 HOH HOH A . X 9 HOH 175 792 182 HOH HOH A . X 9 HOH 176 793 183 HOH HOH A . X 9 HOH 177 794 184 HOH HOH A . X 9 HOH 178 795 185 HOH HOH A . X 9 HOH 179 796 186 HOH HOH A . X 9 HOH 180 797 187 HOH HOH A . X 9 HOH 181 798 188 HOH HOH A . X 9 HOH 182 799 189 HOH HOH A . X 9 HOH 183 800 190 HOH HOH A . X 9 HOH 184 801 191 HOH HOH A . X 9 HOH 185 802 192 HOH HOH A . X 9 HOH 186 803 193 HOH HOH A . X 9 HOH 187 804 194 HOH HOH A . X 9 HOH 188 805 195 HOH HOH A . X 9 HOH 189 806 196 HOH HOH A . X 9 HOH 190 807 197 HOH HOH A . X 9 HOH 191 808 198 HOH HOH A . X 9 HOH 192 809 199 HOH HOH A . X 9 HOH 193 810 200 HOH HOH A . X 9 HOH 194 811 202 HOH HOH A . X 9 HOH 195 812 203 HOH HOH A . X 9 HOH 196 813 205 HOH HOH A . X 9 HOH 197 814 206 HOH HOH A . X 9 HOH 198 815 208 HOH HOH A . X 9 HOH 199 816 209 HOH HOH A . X 9 HOH 200 817 210 HOH HOH A . X 9 HOH 201 818 211 HOH HOH A . X 9 HOH 202 819 214 HOH HOH A . X 9 HOH 203 820 215 HOH HOH A . X 9 HOH 204 821 216 HOH HOH A . X 9 HOH 205 822 220 HOH HOH A . X 9 HOH 206 823 221 HOH HOH A . X 9 HOH 207 824 222 HOH HOH A . X 9 HOH 208 825 223 HOH HOH A . X 9 HOH 209 826 227 HOH HOH A . X 9 HOH 210 827 229 HOH HOH A . X 9 HOH 211 828 230 HOH HOH A . X 9 HOH 212 829 231 HOH HOH A . X 9 HOH 213 830 235 HOH HOH A . X 9 HOH 214 831 237 HOH HOH A . X 9 HOH 215 832 239 HOH HOH A . X 9 HOH 216 833 240 HOH HOH A . X 9 HOH 217 834 241 HOH HOH A . X 9 HOH 218 835 242 HOH HOH A . X 9 HOH 219 836 243 HOH HOH A . X 9 HOH 220 837 245 HOH HOH A . X 9 HOH 221 838 246 HOH HOH A . X 9 HOH 222 839 247 HOH HOH A . X 9 HOH 223 840 248 HOH HOH A . X 9 HOH 224 841 249 HOH HOH A . X 9 HOH 225 842 250 HOH HOH A . X 9 HOH 226 843 251 HOH HOH A . X 9 HOH 227 844 252 HOH HOH A . X 9 HOH 228 845 254 HOH HOH A . X 9 HOH 229 846 255 HOH HOH A . X 9 HOH 230 847 256 HOH HOH A . X 9 HOH 231 848 257 HOH HOH A . X 9 HOH 232 849 258 HOH HOH A . X 9 HOH 233 850 259 HOH HOH A . X 9 HOH 234 851 260 HOH HOH A . X 9 HOH 235 852 261 HOH HOH A . X 9 HOH 236 853 262 HOH HOH A . X 9 HOH 237 854 263 HOH HOH A . X 9 HOH 238 855 264 HOH HOH A . X 9 HOH 239 856 265 HOH HOH A . X 9 HOH 240 857 266 HOH HOH A . X 9 HOH 241 858 267 HOH HOH A . X 9 HOH 242 859 268 HOH HOH A . X 9 HOH 243 860 269 HOH HOH A . X 9 HOH 244 861 270 HOH HOH A . X 9 HOH 245 862 271 HOH HOH A . X 9 HOH 246 863 272 HOH HOH A . X 9 HOH 247 864 273 HOH HOH A . X 9 HOH 248 865 274 HOH HOH A . X 9 HOH 249 866 275 HOH HOH A . X 9 HOH 250 867 276 HOH HOH A . X 9 HOH 251 868 277 HOH HOH A . X 9 HOH 252 869 278 HOH HOH A . X 9 HOH 253 870 279 HOH HOH A . X 9 HOH 254 871 280 HOH HOH A . X 9 HOH 255 872 281 HOH HOH A . X 9 HOH 256 873 282 HOH HOH A . X 9 HOH 257 874 283 HOH HOH A . X 9 HOH 258 875 284 HOH HOH A . X 9 HOH 259 876 285 HOH HOH A . X 9 HOH 260 877 286 HOH HOH A . X 9 HOH 261 878 287 HOH HOH A . X 9 HOH 262 879 288 HOH HOH A . X 9 HOH 263 880 289 HOH HOH A . X 9 HOH 264 881 290 HOH HOH A . X 9 HOH 265 882 291 HOH HOH A . X 9 HOH 266 883 292 HOH HOH A . X 9 HOH 267 884 293 HOH HOH A . X 9 HOH 268 885 294 HOH HOH A . X 9 HOH 269 886 295 HOH HOH A . X 9 HOH 270 887 296 HOH HOH A . X 9 HOH 271 888 297 HOH HOH A . X 9 HOH 272 889 298 HOH HOH A . X 9 HOH 273 890 299 HOH HOH A . X 9 HOH 274 891 300 HOH HOH A . X 9 HOH 275 892 301 HOH HOH A . X 9 HOH 276 893 302 HOH HOH A . X 9 HOH 277 894 303 HOH HOH A . X 9 HOH 278 895 304 HOH HOH A . X 9 HOH 279 896 306 HOH HOH A . X 9 HOH 280 897 307 HOH HOH A . X 9 HOH 281 898 308 HOH HOH A . X 9 HOH 282 899 309 HOH HOH A . X 9 HOH 283 900 310 HOH HOH A . X 9 HOH 284 901 311 HOH HOH A . X 9 HOH 285 902 313 HOH HOH A . X 9 HOH 286 903 314 HOH HOH A . X 9 HOH 287 904 315 HOH HOH A . X 9 HOH 288 905 316 HOH HOH A . X 9 HOH 289 906 317 HOH HOH A . X 9 HOH 290 907 319 HOH HOH A . X 9 HOH 291 908 320 HOH HOH A . X 9 HOH 292 909 321 HOH HOH A . X 9 HOH 293 910 322 HOH HOH A . X 9 HOH 294 911 323 HOH HOH A . X 9 HOH 295 912 324 HOH HOH A . X 9 HOH 296 913 325 HOH HOH A . X 9 HOH 297 914 326 HOH HOH A . X 9 HOH 298 915 327 HOH HOH A . X 9 HOH 299 916 328 HOH HOH A . X 9 HOH 300 917 329 HOH HOH A . X 9 HOH 301 918 330 HOH HOH A . X 9 HOH 302 919 331 HOH HOH A . X 9 HOH 303 920 332 HOH HOH A . X 9 HOH 304 921 333 HOH HOH A . X 9 HOH 305 922 334 HOH HOH A . X 9 HOH 306 923 335 HOH HOH A . X 9 HOH 307 924 336 HOH HOH A . X 9 HOH 308 925 337 HOH HOH A . X 9 HOH 309 926 338 HOH HOH A . X 9 HOH 310 927 339 HOH HOH A . X 9 HOH 311 928 340 HOH HOH A . X 9 HOH 312 929 341 HOH HOH A . X 9 HOH 313 930 342 HOH HOH A . X 9 HOH 314 931 343 HOH HOH A . X 9 HOH 315 932 344 HOH HOH A . X 9 HOH 316 933 345 HOH HOH A . #