data_2ADE # _entry.id 2ADE # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.279 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 2ADE RCSB RCSB033764 WWPDB D_1000033764 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 2ADD 'Crystal structure of fructan 1-exohydrolase IIa from Cichorium intybus in complex with sucrose' unspecified PDB 2AEZ 'Crystal structure of fructan 1-exohydrolase IIa (E201Q) from Cichorium intybus in complex with 1-kestose' unspecified PDB 2ADE 'Crystal structure of fructan 1-exohydrolase IIa from Cichorium intybus in complex with fructose' unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 2ADE _pdbx_database_status.recvd_initial_deposition_date 2005-07-20 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_cs ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Verhaest, M.' 1 'Le Roy, K.' 2 'De Ranter, C.J.' 3 'Van Laere, A.' 4 'Van den Ende, W.' 5 'Rabijns, A.' 6 # _citation.id primary _citation.title ;Insights into the fine architecture of the active site of chicory fructan 1-exohydrolase: 1-kestose as substrate vs sucrose as inhibitor. ; _citation.journal_abbrev 'New Phytol' _citation.journal_volume 174 _citation.page_first 90 _citation.page_last 100 _citation.year 2007 _citation.journal_id_ASTM ? _citation.country ? _citation.journal_id_ISSN ? _citation.journal_id_CSD 0353 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 17335500 _citation.pdbx_database_id_DOI 10.1111/j.1469-8137.2007.01988.x # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Verhaest, M.' 1 primary 'Lammens, W.' 2 primary 'Le Roy, K.' 3 primary 'De Ranter, C.J.' 4 primary 'Van Laere, A.' 5 primary 'Rabijns, A.' 6 primary 'Van den Ende, W.' 7 # _cell.entry_id 2ADE _cell.length_a 139.040 _cell.length_b 139.040 _cell.length_c 182.240 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _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 2ADE _symmetry.space_group_name_H-M 'P 41 21 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 92 _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man 'fructan 1-exohydrolase IIa' 61115.965 1 3.2.1.153 ? ? ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? 3 non-polymer man ALPHA-D-MANNOSE 180.156 1 ? ? ? ? 4 non-polymer man FRUCTOSE 180.156 1 ? ? ? ? 5 water nat water 18.015 271 ? ? ? ? # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer no _entity_poly.pdbx_seq_one_letter_code ;QQIEQPYRTGYHFQPPSNWMNDPNGPMLYQGVYHFFYQYNPYAATFGDVIIWGHAVSYDLVNWIHLDPAIYPTQEADSKS CWSGSATILPGNIPAMLYTGSDSKSRQVQDLAWPKNLSDPFLREWVKHPKNPLITPPEGVKDDCFRDPSTAWLGPDGVWR IVVGGDRDNNGMAFLYQSTDFVNWKRYDQPLSSADATGTWECPDFYPVPLNSTNGLDTSVYGGSVRHVMKAGFEGHDWYT IGTYSPDRENFLPQNGLSLTGSTLDLRYDYGQFYASKSFFDDAKNRRVLWAWVPETDSQADDIEKGWAGLQSFPRALWID RNGKQLIQWPVEEIEELRQNQVNLQNKNLKPGSVLEIHGIAASQADVTISFKLEGLKEAEVLDTTLVDPQALCNERGASS RGALGPFGLLAMASKDLKEQSAIFFRVFQNQLGRYSVLMCSDLSRSTVRSNIDTTSYGAFVDIDPRSEEISLRNLIDHSI IESFGAGGKTCITSRIYPKFVNNEEAHLFVFNNGTQNVKISEMSAWSMKNAKFVVDQSVKSAA ; _entity_poly.pdbx_seq_one_letter_code_can ;QQIEQPYRTGYHFQPPSNWMNDPNGPMLYQGVYHFFYQYNPYAATFGDVIIWGHAVSYDLVNWIHLDPAIYPTQEADSKS CWSGSATILPGNIPAMLYTGSDSKSRQVQDLAWPKNLSDPFLREWVKHPKNPLITPPEGVKDDCFRDPSTAWLGPDGVWR IVVGGDRDNNGMAFLYQSTDFVNWKRYDQPLSSADATGTWECPDFYPVPLNSTNGLDTSVYGGSVRHVMKAGFEGHDWYT IGTYSPDRENFLPQNGLSLTGSTLDLRYDYGQFYASKSFFDDAKNRRVLWAWVPETDSQADDIEKGWAGLQSFPRALWID RNGKQLIQWPVEEIEELRQNQVNLQNKNLKPGSVLEIHGIAASQADVTISFKLEGLKEAEVLDTTLVDPQALCNERGASS RGALGPFGLLAMASKDLKEQSAIFFRVFQNQLGRYSVLMCSDLSRSTVRSNIDTTSYGAFVDIDPRSEEISLRNLIDHSI IESFGAGGKTCITSRIYPKFVNNEEAHLFVFNNGTQNVKISEMSAWSMKNAKFVVDQSVKSAA ; _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 GLN n 1 2 GLN n 1 3 ILE n 1 4 GLU n 1 5 GLN n 1 6 PRO n 1 7 TYR n 1 8 ARG n 1 9 THR n 1 10 GLY n 1 11 TYR n 1 12 HIS n 1 13 PHE n 1 14 GLN n 1 15 PRO n 1 16 PRO n 1 17 SER n 1 18 ASN n 1 19 TRP n 1 20 MET n 1 21 ASN n 1 22 ASP n 1 23 PRO n 1 24 ASN n 1 25 GLY n 1 26 PRO n 1 27 MET n 1 28 LEU n 1 29 TYR n 1 30 GLN n 1 31 GLY n 1 32 VAL n 1 33 TYR n 1 34 HIS n 1 35 PHE n 1 36 PHE n 1 37 TYR n 1 38 GLN n 1 39 TYR n 1 40 ASN n 1 41 PRO n 1 42 TYR n 1 43 ALA n 1 44 ALA n 1 45 THR n 1 46 PHE n 1 47 GLY n 1 48 ASP n 1 49 VAL n 1 50 ILE n 1 51 ILE n 1 52 TRP n 1 53 GLY n 1 54 HIS n 1 55 ALA n 1 56 VAL n 1 57 SER n 1 58 TYR n 1 59 ASP n 1 60 LEU n 1 61 VAL n 1 62 ASN n 1 63 TRP n 1 64 ILE n 1 65 HIS n 1 66 LEU n 1 67 ASP n 1 68 PRO n 1 69 ALA n 1 70 ILE n 1 71 TYR n 1 72 PRO n 1 73 THR n 1 74 GLN n 1 75 GLU n 1 76 ALA n 1 77 ASP n 1 78 SER n 1 79 LYS n 1 80 SER n 1 81 CYS n 1 82 TRP n 1 83 SER n 1 84 GLY n 1 85 SER n 1 86 ALA n 1 87 THR n 1 88 ILE n 1 89 LEU n 1 90 PRO n 1 91 GLY n 1 92 ASN n 1 93 ILE n 1 94 PRO n 1 95 ALA n 1 96 MET n 1 97 LEU n 1 98 TYR n 1 99 THR n 1 100 GLY n 1 101 SER n 1 102 ASP n 1 103 SER n 1 104 LYS n 1 105 SER n 1 106 ARG n 1 107 GLN n 1 108 VAL n 1 109 GLN n 1 110 ASP n 1 111 LEU n 1 112 ALA n 1 113 TRP n 1 114 PRO n 1 115 LYS n 1 116 ASN n 1 117 LEU n 1 118 SER n 1 119 ASP n 1 120 PRO n 1 121 PHE n 1 122 LEU n 1 123 ARG n 1 124 GLU n 1 125 TRP n 1 126 VAL n 1 127 LYS n 1 128 HIS n 1 129 PRO n 1 130 LYS n 1 131 ASN n 1 132 PRO n 1 133 LEU n 1 134 ILE n 1 135 THR n 1 136 PRO n 1 137 PRO n 1 138 GLU n 1 139 GLY n 1 140 VAL n 1 141 LYS n 1 142 ASP n 1 143 ASP n 1 144 CYS n 1 145 PHE n 1 146 ARG n 1 147 ASP n 1 148 PRO n 1 149 SER n 1 150 THR n 1 151 ALA n 1 152 TRP n 1 153 LEU n 1 154 GLY n 1 155 PRO n 1 156 ASP n 1 157 GLY n 1 158 VAL n 1 159 TRP n 1 160 ARG n 1 161 ILE n 1 162 VAL n 1 163 VAL n 1 164 GLY n 1 165 GLY n 1 166 ASP n 1 167 ARG n 1 168 ASP n 1 169 ASN n 1 170 ASN n 1 171 GLY n 1 172 MET n 1 173 ALA n 1 174 PHE n 1 175 LEU n 1 176 TYR n 1 177 GLN n 1 178 SER n 1 179 THR n 1 180 ASP n 1 181 PHE n 1 182 VAL n 1 183 ASN n 1 184 TRP n 1 185 LYS n 1 186 ARG n 1 187 TYR n 1 188 ASP n 1 189 GLN n 1 190 PRO n 1 191 LEU n 1 192 SER n 1 193 SER n 1 194 ALA n 1 195 ASP n 1 196 ALA n 1 197 THR n 1 198 GLY n 1 199 THR n 1 200 TRP n 1 201 GLU n 1 202 CYS n 1 203 PRO n 1 204 ASP n 1 205 PHE n 1 206 TYR n 1 207 PRO n 1 208 VAL n 1 209 PRO n 1 210 LEU n 1 211 ASN n 1 212 SER n 1 213 THR n 1 214 ASN n 1 215 GLY n 1 216 LEU n 1 217 ASP n 1 218 THR n 1 219 SER n 1 220 VAL n 1 221 TYR n 1 222 GLY n 1 223 GLY n 1 224 SER n 1 225 VAL n 1 226 ARG n 1 227 HIS n 1 228 VAL n 1 229 MET n 1 230 LYS n 1 231 ALA n 1 232 GLY n 1 233 PHE n 1 234 GLU n 1 235 GLY n 1 236 HIS n 1 237 ASP n 1 238 TRP n 1 239 TYR n 1 240 THR n 1 241 ILE n 1 242 GLY n 1 243 THR n 1 244 TYR n 1 245 SER n 1 246 PRO n 1 247 ASP n 1 248 ARG n 1 249 GLU n 1 250 ASN n 1 251 PHE n 1 252 LEU n 1 253 PRO n 1 254 GLN n 1 255 ASN n 1 256 GLY n 1 257 LEU n 1 258 SER n 1 259 LEU n 1 260 THR n 1 261 GLY n 1 262 SER n 1 263 THR n 1 264 LEU n 1 265 ASP n 1 266 LEU n 1 267 ARG n 1 268 TYR n 1 269 ASP n 1 270 TYR n 1 271 GLY n 1 272 GLN n 1 273 PHE n 1 274 TYR n 1 275 ALA n 1 276 SER n 1 277 LYS n 1 278 SER n 1 279 PHE n 1 280 PHE n 1 281 ASP n 1 282 ASP n 1 283 ALA n 1 284 LYS n 1 285 ASN n 1 286 ARG n 1 287 ARG n 1 288 VAL n 1 289 LEU n 1 290 TRP n 1 291 ALA n 1 292 TRP n 1 293 VAL n 1 294 PRO n 1 295 GLU n 1 296 THR n 1 297 ASP n 1 298 SER n 1 299 GLN n 1 300 ALA n 1 301 ASP n 1 302 ASP n 1 303 ILE n 1 304 GLU n 1 305 LYS n 1 306 GLY n 1 307 TRP n 1 308 ALA n 1 309 GLY n 1 310 LEU n 1 311 GLN n 1 312 SER n 1 313 PHE n 1 314 PRO n 1 315 ARG n 1 316 ALA n 1 317 LEU n 1 318 TRP n 1 319 ILE n 1 320 ASP n 1 321 ARG n 1 322 ASN n 1 323 GLY n 1 324 LYS n 1 325 GLN n 1 326 LEU n 1 327 ILE n 1 328 GLN n 1 329 TRP n 1 330 PRO n 1 331 VAL n 1 332 GLU n 1 333 GLU n 1 334 ILE n 1 335 GLU n 1 336 GLU n 1 337 LEU n 1 338 ARG n 1 339 GLN n 1 340 ASN n 1 341 GLN n 1 342 VAL n 1 343 ASN n 1 344 LEU n 1 345 GLN n 1 346 ASN n 1 347 LYS n 1 348 ASN n 1 349 LEU n 1 350 LYS n 1 351 PRO n 1 352 GLY n 1 353 SER n 1 354 VAL n 1 355 LEU n 1 356 GLU n 1 357 ILE n 1 358 HIS n 1 359 GLY n 1 360 ILE n 1 361 ALA n 1 362 ALA n 1 363 SER n 1 364 GLN n 1 365 ALA n 1 366 ASP n 1 367 VAL n 1 368 THR n 1 369 ILE n 1 370 SER n 1 371 PHE n 1 372 LYS n 1 373 LEU n 1 374 GLU n 1 375 GLY n 1 376 LEU n 1 377 LYS n 1 378 GLU n 1 379 ALA n 1 380 GLU n 1 381 VAL n 1 382 LEU n 1 383 ASP n 1 384 THR n 1 385 THR n 1 386 LEU n 1 387 VAL n 1 388 ASP n 1 389 PRO n 1 390 GLN n 1 391 ALA n 1 392 LEU n 1 393 CYS n 1 394 ASN n 1 395 GLU n 1 396 ARG n 1 397 GLY n 1 398 ALA n 1 399 SER n 1 400 SER n 1 401 ARG n 1 402 GLY n 1 403 ALA n 1 404 LEU n 1 405 GLY n 1 406 PRO n 1 407 PHE n 1 408 GLY n 1 409 LEU n 1 410 LEU n 1 411 ALA n 1 412 MET n 1 413 ALA n 1 414 SER n 1 415 LYS n 1 416 ASP n 1 417 LEU n 1 418 LYS n 1 419 GLU n 1 420 GLN n 1 421 SER n 1 422 ALA n 1 423 ILE n 1 424 PHE n 1 425 PHE n 1 426 ARG n 1 427 VAL n 1 428 PHE n 1 429 GLN n 1 430 ASN n 1 431 GLN n 1 432 LEU n 1 433 GLY n 1 434 ARG n 1 435 TYR n 1 436 SER n 1 437 VAL n 1 438 LEU n 1 439 MET n 1 440 CYS n 1 441 SER n 1 442 ASP n 1 443 LEU n 1 444 SER n 1 445 ARG n 1 446 SER n 1 447 THR n 1 448 VAL n 1 449 ARG n 1 450 SER n 1 451 ASN n 1 452 ILE n 1 453 ASP n 1 454 THR n 1 455 THR n 1 456 SER n 1 457 TYR n 1 458 GLY n 1 459 ALA n 1 460 PHE n 1 461 VAL n 1 462 ASP n 1 463 ILE n 1 464 ASP n 1 465 PRO n 1 466 ARG n 1 467 SER n 1 468 GLU n 1 469 GLU n 1 470 ILE n 1 471 SER n 1 472 LEU n 1 473 ARG n 1 474 ASN n 1 475 LEU n 1 476 ILE n 1 477 ASP n 1 478 HIS n 1 479 SER n 1 480 ILE n 1 481 ILE n 1 482 GLU n 1 483 SER n 1 484 PHE n 1 485 GLY n 1 486 ALA n 1 487 GLY n 1 488 GLY n 1 489 LYS n 1 490 THR n 1 491 CYS n 1 492 ILE n 1 493 THR n 1 494 SER n 1 495 ARG n 1 496 ILE n 1 497 TYR n 1 498 PRO n 1 499 LYS n 1 500 PHE n 1 501 VAL n 1 502 ASN n 1 503 ASN n 1 504 GLU n 1 505 GLU n 1 506 ALA n 1 507 HIS n 1 508 LEU n 1 509 PHE n 1 510 VAL n 1 511 PHE n 1 512 ASN n 1 513 ASN n 1 514 GLY n 1 515 THR n 1 516 GLN n 1 517 ASN n 1 518 VAL n 1 519 LYS n 1 520 ILE n 1 521 SER n 1 522 GLU n 1 523 MET n 1 524 SER n 1 525 ALA n 1 526 TRP n 1 527 SER n 1 528 MET n 1 529 LYS n 1 530 ASN n 1 531 ALA n 1 532 LYS n 1 533 PHE n 1 534 VAL n 1 535 VAL n 1 536 ASP n 1 537 GLN n 1 538 SER n 1 539 VAL n 1 540 LYS n 1 541 SER n 1 542 ALA n 1 543 ALA n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name chicory _entity_src_gen.gene_src_genus Cichorium _entity_src_gen.pdbx_gene_src_gene '1-FEH IIa' _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'Cichorium intybus' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 13427 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name ? _entity_src_gen.pdbx_host_org_scientific_name 'Pichia pastoris' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 4922 _entity_src_gen.host_org_genus Pichia _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type ? _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name ? _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code Q93X60_CICIN _struct_ref.pdbx_db_accession Q93X60 _struct_ref.entity_id 1 _struct_ref.pdbx_align_begin 39 _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 2ADE _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 543 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession Q93X60 _struct_ref_seq.db_align_beg 39 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 581 _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 543 # 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 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 FRU saccharide . FRUCTOSE ? 'C6 H12 O6' 180.156 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 2ADE _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 7.2 _exptl_crystal.density_percent_sol 82 _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 277 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 7.0 _exptl_crystal_grow.pdbx_details 'sodium potassium phosphate, potassium phosphate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K' _exptl_crystal_grow.pdbx_pH_range . # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type MARRESEARCH _diffrn_detector.pdbx_collection_date 2004-12-17 _diffrn_detector.details 'bent mirror' # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'triangular monochromator' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.931 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'ESRF BEAMLINE ID14-3' _diffrn_source.pdbx_synchrotron_site ESRF _diffrn_source.pdbx_synchrotron_beamline ID14-3 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 0.931 # _reflns.entry_id 2ADE _reflns.observed_criterion_sigma_I 2.0 _reflns.observed_criterion_sigma_F 1.41 _reflns.d_resolution_low 30 _reflns.d_resolution_high 2.65 _reflns.number_obs 52450 _reflns.number_all 52790 _reflns.percent_possible_obs 88.1 _reflns.pdbx_Rmerge_I_obs 0.114 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate 36.2 _reflns.pdbx_redundancy 8.0 _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 2.65 _reflns_shell.d_res_low 2.70 _reflns_shell.percent_possible_all 100 _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.pdbx_redundancy ? _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all 2586 _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 2ADE _refine.ls_number_reflns_obs 50307 _refine.ls_number_reflns_all 50307 _refine.pdbx_ls_sigma_I 0.0 _refine.pdbx_ls_sigma_F 0.0 _refine.pdbx_data_cutoff_high_absF 66253.28 _refine.pdbx_data_cutoff_low_absF 0.000000 _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 29.48 _refine.ls_d_res_high 2.65 _refine.ls_percent_reflns_obs 95.9 _refine.ls_R_factor_obs 0.239 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.239 _refine.ls_R_factor_R_free 0.251 _refine.ls_R_factor_R_free_error 0.005 _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.0 _refine.ls_number_reflns_R_free 2531 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean 31.1 _refine.aniso_B[1][1] 4.74 _refine.aniso_B[2][2] 4.74 _refine.aniso_B[3][3] -9.48 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details 'FLAT MODEL' _refine.solvent_model_param_ksol 0.355455 _refine.solvent_model_param_bsol 30.7468 _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details ? _refine.pdbx_starting_model 'PDB ENTRY 1ST8' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model RESTRAINED _refine.pdbx_stereochemistry_target_values 'Engh & Huber' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML ? _refine.overall_SU_B ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_overall_phase_error ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_analyze.entry_id 2ADE _refine_analyze.Luzzati_coordinate_error_obs 0.36 _refine_analyze.Luzzati_sigma_a_obs 0.42 _refine_analyze.Luzzati_d_res_low_obs 5.00 _refine_analyze.Luzzati_coordinate_error_free 0.40 _refine_analyze.Luzzati_sigma_a_free 0.48 _refine_analyze.Luzzati_d_res_low_free ? _refine_analyze.number_disordered_residues ? _refine_analyze.occupancy_sum_hydrogen ? _refine_analyze.occupancy_sum_non_hydrogen ? _refine_analyze.pdbx_Luzzati_d_res_high_obs ? _refine_analyze.pdbx_refine_id 'X-RAY DIFFRACTION' # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 4274 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 79 _refine_hist.number_atoms_solvent 271 _refine_hist.number_atoms_total 4624 _refine_hist.d_res_high 2.65 _refine_hist.d_res_low 29.48 # 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 c_bond_d 0.006 ? ? ? 'X-RAY DIFFRACTION' ? c_bond_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? c_bond_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? c_angle_d ? ? ? ? 'X-RAY DIFFRACTION' ? c_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? c_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? c_angle_deg 1.3 ? ? ? 'X-RAY DIFFRACTION' ? c_angle_deg_na ? ? ? ? 'X-RAY DIFFRACTION' ? c_angle_deg_prot ? ? ? ? 'X-RAY DIFFRACTION' ? c_dihedral_angle_d 25.9 ? ? ? 'X-RAY DIFFRACTION' ? c_dihedral_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? c_dihedral_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? c_improper_angle_d 0.80 ? ? ? 'X-RAY DIFFRACTION' ? c_improper_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? c_improper_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? c_mcbond_it 1.16 1.50 ? ? 'X-RAY DIFFRACTION' ? c_mcangle_it 1.96 2.00 ? ? 'X-RAY DIFFRACTION' ? c_scbond_it 2.10 2.00 ? ? 'X-RAY DIFFRACTION' ? c_scangle_it 3.23 2.50 ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_total_number_of_bins_used 6 _refine_ls_shell.d_res_high 2.65 _refine_ls_shell.d_res_low 2.82 _refine_ls_shell.number_reflns_R_work 7351 _refine_ls_shell.R_factor_R_work 0.321 _refine_ls_shell.percent_reflns_obs 89.9 _refine_ls_shell.R_factor_R_free 0.35 _refine_ls_shell.R_factor_R_free_error 0.018 _refine_ls_shell.percent_reflns_R_free 4.9 _refine_ls_shell.number_reflns_R_free 379 _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' # loop_ _pdbx_xplor_file.serial_no _pdbx_xplor_file.param_file _pdbx_xplor_file.topol_file _pdbx_xplor_file.pdbx_refine_id 1 protein_rep.param protein.top 'X-RAY DIFFRACTION' 2 water_rep.param water.top 'X-RAY DIFFRACTION' 3 carbohydrate.param carbohydrate.top 'X-RAY DIFFRACTION' 4 gol.param gol.top 'X-RAY DIFFRACTION' 5 fruct2.param fruct2.top 'X-RAY DIFFRACTION' # _struct.entry_id 2ADE _struct.title 'Crystal structure of fructan 1-exohydrolase IIa from Cichorium intybus in complex with fructose' _struct.pdbx_descriptor 'fructan 1-exohydrolase IIa (E.C.3.2.1.153)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 2ADE _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'five fold beta propeller, HYDROLASE' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 2 ? D N N 3 ? E N N 2 ? F N N 2 ? G N N 4 ? H N N 5 ? # _struct_biol.id 1 # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 GLN A 74 ? SER A 78 ? GLN A 74 SER A 78 5 ? 5 HELX_P HELX_P2 2 PRO A 246 ? GLU A 249 ? PRO A 246 GLU A 249 5 ? 4 HELX_P HELX_P3 3 SER A 298 ? GLY A 306 ? SER A 298 GLY A 306 1 ? 9 HELX_P HELX_P4 4 GLU A 332 ? GLU A 336 ? GLU A 332 GLU A 336 5 ? 5 HELX_P HELX_P5 5 GLY A 375 ? ALA A 379 ? GLY A 375 ALA A 379 5 ? 5 HELX_P HELX_P6 6 ASP A 388 ? ARG A 396 ? ASP A 388 ARG A 396 1 ? 9 HELX_P HELX_P7 7 LYS A 499 ? ASN A 503 ? LYS A 499 ASN A 503 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 393 SG ? ? ? 1_555 A CYS 440 SG ? ? A CYS 393 A CYS 440 1_555 ? ? ? ? ? ? ? 2.038 ? covale1 covale ? ? A ASN 116 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 116 A NAG 680 1_555 ? ? ? ? ? ? ? 1.451 ? covale2 covale ? ? A ASN 513 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 513 A NAG 650 1_555 ? ? ? ? ? ? ? 1.458 ? covale3 covale ? ? B NAG . O4 ? ? ? 1_555 C NAG . C1 ? ? A NAG 650 A NAG 660 1_555 ? ? ? ? ? ? ? 1.394 ? covale4 covale ? ? C NAG . O4 ? ? ? 1_555 D MAN . C1 ? ? A NAG 660 A MAN 670 1_555 ? ? ? ? ? ? ? 1.400 ? covale5 covale ? ? E NAG . O4 ? ? ? 1_555 F NAG . C1 ? ? A NAG 680 A NAG 690 1_555 ? ? ? ? ? ? ? 1.388 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 ASN 131 A . ? ASN 131 A PRO 132 A ? PRO 132 A 1 -0.01 2 GLY 405 A . ? GLY 405 A PRO 406 A ? PRO 406 A 1 0.06 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 6 ? B ? 4 ? C ? 4 ? D ? 4 ? E ? 4 ? F ? 4 ? G ? 3 ? H ? 4 ? I ? 6 ? J ? 5 ? K ? 6 ? # 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 ? parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel A 4 5 ? anti-parallel A 5 6 ? parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel C 1 2 ? anti-parallel C 2 3 ? anti-parallel C 3 4 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? anti-parallel D 3 4 ? anti-parallel E 1 2 ? anti-parallel E 2 3 ? anti-parallel E 3 4 ? anti-parallel F 1 2 ? anti-parallel F 2 3 ? anti-parallel F 3 4 ? anti-parallel G 1 2 ? anti-parallel G 2 3 ? anti-parallel H 1 2 ? anti-parallel H 2 3 ? anti-parallel H 3 4 ? anti-parallel I 1 2 ? anti-parallel I 2 3 ? anti-parallel I 3 4 ? anti-parallel I 4 5 ? anti-parallel I 5 6 ? anti-parallel J 1 2 ? anti-parallel J 2 3 ? anti-parallel J 3 4 ? anti-parallel J 4 5 ? parallel K 1 2 ? anti-parallel K 2 3 ? anti-parallel K 3 4 ? anti-parallel K 4 5 ? anti-parallel K 5 6 ? 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 TRP A 307 ? ALA A 308 ? TRP A 307 ALA A 308 A 2 ASN A 18 ? TYR A 29 ? ASN A 18 TYR A 29 A 3 VAL A 32 ? ASN A 40 ? VAL A 32 ASN A 40 A 4 ILE A 51 ? SER A 57 ? ILE A 51 SER A 57 A 5 TRP A 63 ? HIS A 65 ? TRP A 63 HIS A 65 A 6 PHE A 533 ? VAL A 535 ? PHE A 533 VAL A 535 B 1 SER A 80 ? LEU A 89 ? SER A 80 LEU A 89 B 2 ILE A 93 ? SER A 101 ? ILE A 93 SER A 101 B 3 GLN A 107 ? PRO A 114 ? GLN A 107 PRO A 114 B 4 TRP A 125 ? LYS A 127 ? TRP A 125 LYS A 127 C 1 PHE A 145 ? ARG A 146 ? PHE A 145 ARG A 146 C 2 TRP A 159 ? ARG A 167 ? TRP A 159 ARG A 167 C 3 ASN A 170 ? SER A 178 ? ASN A 170 SER A 178 C 4 LYS A 185 ? ARG A 186 ? LYS A 185 ARG A 186 D 1 TRP A 152 ? LEU A 153 ? TRP A 152 LEU A 153 D 2 TRP A 159 ? ARG A 167 ? TRP A 159 ARG A 167 D 3 ASN A 170 ? SER A 178 ? ASN A 170 SER A 178 D 4 SER A 192 ? ALA A 194 ? SER A 192 ALA A 194 E 1 GLU A 201 ? PRO A 209 ? GLU A 201 PRO A 209 E 2 VAL A 225 ? PHE A 233 ? VAL A 225 PHE A 233 E 3 HIS A 236 ? SER A 245 ? HIS A 236 SER A 245 E 4 ASN A 250 ? PRO A 253 ? ASN A 250 PRO A 253 F 1 GLU A 201 ? PRO A 209 ? GLU A 201 PRO A 209 F 2 VAL A 225 ? PHE A 233 ? VAL A 225 PHE A 233 F 3 HIS A 236 ? SER A 245 ? HIS A 236 SER A 245 F 4 LEU A 266 ? ARG A 267 ? LEU A 266 ARG A 267 G 1 TYR A 274 ? ASP A 281 ? TYR A 274 ASP A 281 G 2 ARG A 286 ? VAL A 293 ? ARG A 286 VAL A 293 G 3 LEU A 310 ? GLN A 311 ? LEU A 310 GLN A 311 H 1 TYR A 274 ? ASP A 281 ? TYR A 274 ASP A 281 H 2 ARG A 286 ? VAL A 293 ? ARG A 286 VAL A 293 H 3 ARG A 315 ? ILE A 319 ? ARG A 315 ILE A 319 H 4 LEU A 326 ? PRO A 330 ? LEU A 326 PRO A 330 I 1 ARG A 338 ? LEU A 349 ? ARG A 338 LEU A 349 I 2 VAL A 518 ? MET A 528 ? VAL A 518 MET A 528 I 3 GLN A 364 ? LEU A 373 ? GLN A 364 LEU A 373 I 4 ILE A 470 ? ASP A 477 ? ILE A 470 ASP A 477 I 5 ILE A 480 ? GLY A 485 ? ILE A 480 GLY A 485 I 6 THR A 490 ? ARG A 495 ? THR A 490 ARG A 495 J 1 SER A 353 ? GLU A 356 ? SER A 353 GLU A 356 J 2 HIS A 507 ? ASN A 512 ? HIS A 507 ASN A 512 J 3 PHE A 407 ? ALA A 413 ? PHE A 407 ALA A 413 J 4 SER A 421 ? GLN A 429 ? SER A 421 GLN A 429 J 5 GLU A 380 ? VAL A 381 ? GLU A 380 VAL A 381 K 1 SER A 353 ? GLU A 356 ? SER A 353 GLU A 356 K 2 HIS A 507 ? ASN A 512 ? HIS A 507 ASN A 512 K 3 PHE A 407 ? ALA A 413 ? PHE A 407 ALA A 413 K 4 SER A 421 ? GLN A 429 ? SER A 421 GLN A 429 K 5 TYR A 435 ? ASP A 442 ? TYR A 435 ASP A 442 K 6 TYR A 457 ? VAL A 461 ? TYR A 457 VAL A 461 # 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 O ALA A 308 ? O ALA A 308 N ASN A 18 ? N ASN A 18 A 2 3 N ASN A 24 ? N ASN A 24 O PHE A 36 ? O PHE A 36 A 3 4 N TYR A 33 ? N TYR A 33 O SER A 57 ? O SER A 57 A 4 5 N VAL A 56 ? N VAL A 56 O ILE A 64 ? O ILE A 64 A 5 6 N HIS A 65 ? N HIS A 65 O VAL A 534 ? O VAL A 534 B 1 2 N THR A 87 ? N THR A 87 O ALA A 95 ? O ALA A 95 B 2 3 N TYR A 98 ? N TYR A 98 O ASP A 110 ? O ASP A 110 B 3 4 N TRP A 113 ? N TRP A 113 O VAL A 126 ? O VAL A 126 C 1 2 N ARG A 146 ? N ARG A 146 O GLY A 164 ? O GLY A 164 C 2 3 N TRP A 159 ? N TRP A 159 O SER A 178 ? O SER A 178 C 3 4 N GLN A 177 ? N GLN A 177 O LYS A 185 ? O LYS A 185 D 1 2 N TRP A 152 ? N TRP A 152 O ARG A 160 ? O ARG A 160 D 2 3 N TRP A 159 ? N TRP A 159 O SER A 178 ? O SER A 178 D 3 4 N ALA A 173 ? N ALA A 173 O SER A 192 ? O SER A 192 E 1 2 N GLU A 201 ? N GLU A 201 O GLY A 232 ? O GLY A 232 E 2 3 N HIS A 227 ? N HIS A 227 O GLY A 242 ? O GLY A 242 E 3 4 N THR A 243 ? N THR A 243 O LEU A 252 ? O LEU A 252 F 1 2 N GLU A 201 ? N GLU A 201 O GLY A 232 ? O GLY A 232 F 2 3 N HIS A 227 ? N HIS A 227 O GLY A 242 ? O GLY A 242 F 3 4 N TYR A 239 ? N TYR A 239 O LEU A 266 ? O LEU A 266 G 1 2 N ASP A 281 ? N ASP A 281 O ARG A 286 ? O ARG A 286 G 2 3 N VAL A 293 ? N VAL A 293 O LEU A 310 ? O LEU A 310 H 1 2 N ASP A 281 ? N ASP A 281 O ARG A 286 ? O ARG A 286 H 2 3 N LEU A 289 ? N LEU A 289 O ARG A 315 ? O ARG A 315 H 3 4 N TRP A 318 ? N TRP A 318 O ILE A 327 ? O ILE A 327 I 1 2 N LEU A 349 ? N LEU A 349 O VAL A 518 ? O VAL A 518 I 2 3 O SER A 524 ? O SER A 524 N THR A 368 ? N THR A 368 I 3 4 N VAL A 367 ? N VAL A 367 O ASN A 474 ? O ASN A 474 I 4 5 N ARG A 473 ? N ARG A 473 O PHE A 484 ? O PHE A 484 I 5 6 N GLY A 485 ? N GLY A 485 O THR A 490 ? O THR A 490 J 1 2 N LEU A 355 ? N LEU A 355 O VAL A 510 ? O VAL A 510 J 2 3 O PHE A 509 ? O PHE A 509 N LEU A 410 ? N LEU A 410 J 3 4 N LEU A 409 ? N LEU A 409 O ILE A 423 ? O ILE A 423 J 4 5 O GLN A 429 ? O GLN A 429 N GLU A 380 ? N GLU A 380 K 1 2 N LEU A 355 ? N LEU A 355 O VAL A 510 ? O VAL A 510 K 2 3 O PHE A 509 ? O PHE A 509 N LEU A 410 ? N LEU A 410 K 3 4 N LEU A 409 ? N LEU A 409 O ILE A 423 ? O ILE A 423 K 4 5 N ALA A 422 ? N ALA A 422 O ASP A 442 ? O ASP A 442 K 5 6 N MET A 439 ? N MET A 439 O ALA A 459 ? O ALA A 459 # 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 ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 650' AC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 660' AC3 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE MAN A 670' AC4 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 680' AC5 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG A 690' AC6 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE FRU A 800' # 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 6 ALA A 398 ? ALA A 398 . ? 1_555 ? 2 AC1 6 SER A 399 ? SER A 399 . ? 1_555 ? 3 AC1 6 GLN A 420 ? GLN A 420 . ? 1_555 ? 4 AC1 6 ARG A 445 ? ARG A 445 . ? 1_555 ? 5 AC1 6 ASN A 513 ? ASN A 513 . ? 1_555 ? 6 AC1 6 NAG C . ? NAG A 660 . ? 1_555 ? 7 AC2 3 ARG A 445 ? ARG A 445 . ? 1_555 ? 8 AC2 3 NAG B . ? NAG A 650 . ? 1_555 ? 9 AC2 3 MAN D . ? MAN A 670 . ? 1_555 ? 10 AC3 1 NAG C . ? NAG A 660 . ? 1_555 ? 11 AC4 6 ASN A 116 ? ASN A 116 . ? 1_555 ? 12 AC4 6 ASP A 119 ? ASP A 119 . ? 1_555 ? 13 AC4 6 GLU A 234 ? GLU A 234 . ? 4_454 ? 14 AC4 6 NAG F . ? NAG A 690 . ? 1_555 ? 15 AC4 6 HOH H . ? HOH A 1120 . ? 1_555 ? 16 AC4 6 HOH H . ? HOH A 1261 . ? 1_555 ? 17 AC5 1 NAG E . ? NAG A 680 . ? 1_555 ? 18 AC6 9 ASN A 21 ? ASN A 21 . ? 1_555 ? 19 AC6 9 ASP A 22 ? ASP A 22 . ? 1_555 ? 20 AC6 9 GLN A 38 ? GLN A 38 . ? 1_555 ? 21 AC6 9 PHE A 46 ? PHE A 46 . ? 1_555 ? 22 AC6 9 TRP A 82 ? TRP A 82 . ? 1_555 ? 23 AC6 9 SER A 83 ? SER A 83 . ? 1_555 ? 24 AC6 9 ARG A 146 ? ARG A 146 . ? 1_555 ? 25 AC6 9 ASP A 147 ? ASP A 147 . ? 1_555 ? 26 AC6 9 GLU A 201 ? GLU A 201 . ? 1_555 ? # _database_PDB_matrix.entry_id 2ADE _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 2ADE _atom_sites.fract_transf_matrix[1][1] 0.007192 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.007192 _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] 0.005487 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O 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 . GLN A 1 2 ? 42.626 65.118 -13.334 1.00 71.80 ? 2 GLN A N 1 ATOM 2 C CA . GLN A 1 2 ? 41.301 65.761 -13.109 1.00 71.34 ? 2 GLN A CA 1 ATOM 3 C C . GLN A 1 2 ? 40.159 64.886 -13.617 1.00 69.96 ? 2 GLN A C 1 ATOM 4 O O . GLN A 1 2 ? 40.298 64.186 -14.622 1.00 69.19 ? 2 GLN A O 1 ATOM 5 C CB . GLN A 1 2 ? 41.257 67.122 -13.809 1.00 73.19 ? 2 GLN A CB 1 ATOM 6 C CG . GLN A 1 2 ? 41.302 68.316 -12.867 1.00 76.09 ? 2 GLN A CG 1 ATOM 7 C CD . GLN A 1 2 ? 40.003 68.507 -12.100 1.00 78.36 ? 2 GLN A CD 1 ATOM 8 O OE1 . GLN A 1 2 ? 39.890 69.400 -11.260 1.00 78.99 ? 2 GLN A OE1 1 ATOM 9 N NE2 . GLN A 1 2 ? 39.011 67.669 -12.391 1.00 79.89 ? 2 GLN A NE2 1 ATOM 10 N N . ILE A 1 3 ? 39.035 64.921 -12.906 1.00 68.55 ? 3 ILE A N 1 ATOM 11 C CA . ILE A 1 3 ? 37.850 64.156 -13.286 1.00 66.50 ? 3 ILE A CA 1 ATOM 12 C C . ILE A 1 3 ? 36.704 65.126 -13.514 1.00 65.24 ? 3 ILE A C 1 ATOM 13 O O . ILE A 1 3 ? 36.519 66.071 -12.746 1.00 64.83 ? 3 ILE A O 1 ATOM 14 C CB . ILE A 1 3 ? 37.415 63.164 -12.188 1.00 66.50 ? 3 ILE A CB 1 ATOM 15 C CG1 . ILE A 1 3 ? 38.498 62.107 -11.978 1.00 66.05 ? 3 ILE A CG1 1 ATOM 16 C CG2 . ILE A 1 3 ? 36.092 62.507 -12.575 1.00 65.68 ? 3 ILE A CG2 1 ATOM 17 C CD1 . ILE A 1 3 ? 38.125 61.051 -10.960 1.00 66.01 ? 3 ILE A CD1 1 ATOM 18 N N . GLU A 1 4 ? 35.935 64.896 -14.570 1.00 64.25 ? 4 GLU A N 1 ATOM 19 C CA . GLU A 1 4 ? 34.810 65.767 -14.875 1.00 64.73 ? 4 GLU A CA 1 ATOM 20 C C . GLU A 1 4 ? 33.557 65.343 -14.133 1.00 61.70 ? 4 GLU A C 1 ATOM 21 O O . GLU A 1 4 ? 33.080 64.220 -14.300 1.00 62.93 ? 4 GLU A O 1 ATOM 22 C CB . GLU A 1 4 ? 34.522 65.775 -16.379 1.00 69.52 ? 4 GLU A CB 1 ATOM 23 C CG . GLU A 1 4 ? 35.547 66.539 -17.201 1.00 76.93 ? 4 GLU A CG 1 ATOM 24 C CD . GLU A 1 4 ? 35.851 67.913 -16.616 1.00 80.45 ? 4 GLU A CD 1 ATOM 25 O OE1 . GLU A 1 4 ? 34.890 68.653 -16.295 1.00 81.61 ? 4 GLU A OE1 1 ATOM 26 O OE2 . GLU A 1 4 ? 37.052 68.252 -16.481 1.00 81.95 ? 4 GLU A OE2 1 ATOM 27 N N . GLN A 1 5 ? 33.026 66.245 -13.314 1.00 56.07 ? 5 GLN A N 1 ATOM 28 C CA . GLN A 1 5 ? 31.812 65.962 -12.558 1.00 51.06 ? 5 GLN A CA 1 ATOM 29 C C . GLN A 1 5 ? 31.971 64.728 -11.679 1.00 46.16 ? 5 GLN A C 1 ATOM 30 O O . GLN A 1 5 ? 31.241 63.748 -11.821 1.00 45.42 ? 5 GLN A O 1 ATOM 31 C CB . GLN A 1 5 ? 30.652 65.776 -13.528 1.00 51.78 ? 5 GLN A CB 1 ATOM 32 C CG . GLN A 1 5 ? 30.644 66.834 -14.606 1.00 55.19 ? 5 GLN A CG 1 ATOM 33 C CD . GLN A 1 5 ? 29.253 67.212 -15.046 1.00 57.29 ? 5 GLN A CD 1 ATOM 34 O OE1 . GLN A 1 5 ? 28.623 66.513 -15.850 1.00 57.84 ? 5 GLN A OE1 1 ATOM 35 N NE2 . GLN A 1 5 ? 28.754 68.324 -14.510 1.00 56.47 ? 5 GLN A NE2 1 ATOM 36 N N . PRO A 1 6 ? 32.929 64.771 -10.742 1.00 41.62 ? 6 PRO A N 1 ATOM 37 C CA . PRO A 1 6 ? 33.233 63.683 -9.809 1.00 38.82 ? 6 PRO A CA 1 ATOM 38 C C . PRO A 1 6 ? 32.107 63.356 -8.825 1.00 36.63 ? 6 PRO A C 1 ATOM 39 O O . PRO A 1 6 ? 32.191 62.378 -8.080 1.00 35.66 ? 6 PRO A O 1 ATOM 40 C CB . PRO A 1 6 ? 34.479 64.194 -9.100 1.00 39.37 ? 6 PRO A CB 1 ATOM 41 C CG . PRO A 1 6 ? 34.209 65.659 -9.023 1.00 38.60 ? 6 PRO A CG 1 ATOM 42 C CD . PRO A 1 6 ? 33.724 65.968 -10.414 1.00 38.79 ? 6 PRO A CD 1 ATOM 43 N N . TYR A 1 7 ? 31.060 64.175 -8.822 1.00 34.12 ? 7 TYR A N 1 ATOM 44 C CA . TYR A 1 7 ? 29.946 63.951 -7.916 1.00 31.99 ? 7 TYR A CA 1 ATOM 45 C C . TYR A 1 7 ? 28.767 63.213 -8.548 1.00 31.59 ? 7 TYR A C 1 ATOM 46 O O . TYR A 1 7 ? 27.886 62.732 -7.833 1.00 31.98 ? 7 TYR A O 1 ATOM 47 C CB . TYR A 1 7 ? 29.492 65.279 -7.315 1.00 30.94 ? 7 TYR A CB 1 ATOM 48 C CG . TYR A 1 7 ? 30.564 65.923 -6.473 1.00 31.17 ? 7 TYR A CG 1 ATOM 49 C CD1 . TYR A 1 7 ? 31.096 65.259 -5.368 1.00 30.88 ? 7 TYR A CD1 1 ATOM 50 C CD2 . TYR A 1 7 ? 31.074 67.182 -6.794 1.00 31.81 ? 7 TYR A CD2 1 ATOM 51 C CE1 . TYR A 1 7 ? 32.110 65.828 -4.601 1.00 30.96 ? 7 TYR A CE1 1 ATOM 52 C CE2 . TYR A 1 7 ? 32.091 67.764 -6.034 1.00 31.57 ? 7 TYR A CE2 1 ATOM 53 C CZ . TYR A 1 7 ? 32.602 67.080 -4.940 1.00 32.28 ? 7 TYR A CZ 1 ATOM 54 O OH . TYR A 1 7 ? 33.598 67.649 -4.182 1.00 31.81 ? 7 TYR A OH 1 ATOM 55 N N . ARG A 1 8 ? 28.744 63.111 -9.875 1.00 29.55 ? 8 ARG A N 1 ATOM 56 C CA . ARG A 1 8 ? 27.663 62.390 -10.544 1.00 29.07 ? 8 ARG A CA 1 ATOM 57 C C . ARG A 1 8 ? 27.791 60.903 -10.227 1.00 28.35 ? 8 ARG A C 1 ATOM 58 O O . ARG A 1 8 ? 28.896 60.361 -10.178 1.00 29.39 ? 8 ARG A O 1 ATOM 59 C CB . ARG A 1 8 ? 27.712 62.601 -12.059 1.00 26.89 ? 8 ARG A CB 1 ATOM 60 C CG . ARG A 1 8 ? 27.350 64.011 -12.494 1.00 27.99 ? 8 ARG A CG 1 ATOM 61 C CD . ARG A 1 8 ? 27.261 64.118 -14.008 1.00 27.15 ? 8 ARG A CD 1 ATOM 62 N NE . ARG A 1 8 ? 26.117 63.388 -14.551 1.00 28.90 ? 8 ARG A NE 1 ATOM 63 C CZ . ARG A 1 8 ? 24.853 63.777 -14.420 1.00 28.60 ? 8 ARG A CZ 1 ATOM 64 N NH1 . ARG A 1 8 ? 24.566 64.893 -13.766 1.00 30.38 ? 8 ARG A NH1 1 ATOM 65 N NH2 . ARG A 1 8 ? 23.874 63.047 -14.937 1.00 28.45 ? 8 ARG A NH2 1 ATOM 66 N N . THR A 1 9 ? 26.655 60.251 -10.006 1.00 26.48 ? 9 THR A N 1 ATOM 67 C CA . THR A 1 9 ? 26.636 58.830 -9.679 1.00 24.52 ? 9 THR A CA 1 ATOM 68 C C . THR A 1 9 ? 26.860 57.949 -10.902 1.00 24.92 ? 9 THR A C 1 ATOM 69 O O . THR A 1 9 ? 26.696 58.389 -12.043 1.00 26.47 ? 9 THR A O 1 ATOM 70 C CB . THR A 1 9 ? 25.299 58.428 -9.060 1.00 23.82 ? 9 THR A CB 1 ATOM 71 O OG1 . THR A 1 9 ? 24.274 58.517 -10.057 1.00 24.18 ? 9 THR A OG1 1 ATOM 72 C CG2 . THR A 1 9 ? 24.950 59.353 -7.902 1.00 20.99 ? 9 THR A CG2 1 ATOM 73 N N . GLY A 1 10 ? 27.226 56.697 -10.652 1.00 23.86 ? 10 GLY A N 1 ATOM 74 C CA . GLY A 1 10 ? 27.465 55.759 -11.731 1.00 21.42 ? 10 GLY A CA 1 ATOM 75 C C . GLY A 1 10 ? 26.311 54.800 -11.964 1.00 22.53 ? 10 GLY A C 1 ATOM 76 O O . GLY A 1 10 ? 26.183 54.242 -13.060 1.00 22.98 ? 10 GLY A O 1 ATOM 77 N N . TYR A 1 11 ? 25.469 54.588 -10.953 1.00 21.25 ? 11 TYR A N 1 ATOM 78 C CA . TYR A 1 11 ? 24.347 53.678 -11.127 1.00 21.55 ? 11 TYR A CA 1 ATOM 79 C C . TYR A 1 11 ? 23.069 54.109 -10.416 1.00 21.94 ? 11 TYR A C 1 ATOM 80 O O . TYR A 1 11 ? 22.206 53.289 -10.109 1.00 21.78 ? 11 TYR A O 1 ATOM 81 C CB . TYR A 1 11 ? 24.741 52.244 -10.729 1.00 21.27 ? 11 TYR A CB 1 ATOM 82 C CG . TYR A 1 11 ? 25.212 52.082 -9.303 1.00 22.08 ? 11 TYR A CG 1 ATOM 83 C CD1 . TYR A 1 11 ? 24.303 51.892 -8.263 1.00 21.42 ? 11 TYR A CD1 1 ATOM 84 C CD2 . TYR A 1 11 ? 26.571 52.142 -8.991 1.00 22.21 ? 11 TYR A CD2 1 ATOM 85 C CE1 . TYR A 1 11 ? 24.735 51.768 -6.941 1.00 22.91 ? 11 TYR A CE1 1 ATOM 86 C CE2 . TYR A 1 11 ? 27.013 52.022 -7.676 1.00 22.64 ? 11 TYR A CE2 1 ATOM 87 C CZ . TYR A 1 11 ? 26.093 51.838 -6.656 1.00 22.05 ? 11 TYR A CZ 1 ATOM 88 O OH . TYR A 1 11 ? 26.530 51.748 -5.355 1.00 20.49 ? 11 TYR A OH 1 ATOM 89 N N . HIS A 1 12 ? 22.951 55.403 -10.149 1.00 22.25 ? 12 HIS A N 1 ATOM 90 C CA . HIS A 1 12 ? 21.741 55.929 -9.531 1.00 22.06 ? 12 HIS A CA 1 ATOM 91 C C . HIS A 1 12 ? 21.019 56.719 -10.605 1.00 22.39 ? 12 HIS A C 1 ATOM 92 O O . HIS A 1 12 ? 21.655 57.292 -11.487 1.00 23.21 ? 12 HIS A O 1 ATOM 93 C CB . HIS A 1 12 ? 22.065 56.852 -8.363 1.00 21.77 ? 12 HIS A CB 1 ATOM 94 C CG . HIS A 1 12 ? 22.271 56.131 -7.070 1.00 23.57 ? 12 HIS A CG 1 ATOM 95 N ND1 . HIS A 1 12 ? 23.397 55.384 -6.805 1.00 23.12 ? 12 HIS A ND1 1 ATOM 96 C CD2 . HIS A 1 12 ? 21.478 56.021 -5.977 1.00 23.11 ? 12 HIS A CD2 1 ATOM 97 C CE1 . HIS A 1 12 ? 23.290 54.844 -5.603 1.00 24.00 ? 12 HIS A CE1 1 ATOM 98 N NE2 . HIS A 1 12 ? 22.135 55.215 -5.081 1.00 23.98 ? 12 HIS A NE2 1 ATOM 99 N N . PHE A 1 13 ? 19.697 56.757 -10.550 1.00 22.29 ? 13 PHE A N 1 ATOM 100 C CA . PHE A 1 13 ? 18.986 57.504 -11.568 1.00 23.20 ? 13 PHE A CA 1 ATOM 101 C C . PHE A 1 13 ? 19.061 59.003 -11.345 1.00 24.48 ? 13 PHE A C 1 ATOM 102 O O . PHE A 1 13 ? 18.890 59.492 -10.229 1.00 25.56 ? 13 PHE A O 1 ATOM 103 C CB . PHE A 1 13 ? 17.514 57.111 -11.635 1.00 21.82 ? 13 PHE A CB 1 ATOM 104 C CG . PHE A 1 13 ? 16.768 57.830 -12.715 1.00 21.70 ? 13 PHE A CG 1 ATOM 105 C CD1 . PHE A 1 13 ? 16.649 57.273 -13.983 1.00 22.40 ? 13 PHE A CD1 1 ATOM 106 C CD2 . PHE A 1 13 ? 16.272 59.116 -12.498 1.00 20.17 ? 13 PHE A CD2 1 ATOM 107 C CE1 . PHE A 1 13 ? 16.051 57.991 -15.025 1.00 21.79 ? 13 PHE A CE1 1 ATOM 108 C CE2 . PHE A 1 13 ? 15.676 59.842 -13.528 1.00 19.23 ? 13 PHE A CE2 1 ATOM 109 C CZ . PHE A 1 13 ? 15.567 59.281 -14.795 1.00 21.01 ? 13 PHE A CZ 1 ATOM 110 N N . GLN A 1 14 ? 19.316 59.724 -12.427 1.00 26.08 ? 14 GLN A N 1 ATOM 111 C CA . GLN A 1 14 ? 19.372 61.183 -12.424 1.00 26.87 ? 14 GLN A CA 1 ATOM 112 C C . GLN A 1 14 ? 19.361 61.599 -13.887 1.00 27.45 ? 14 GLN A C 1 ATOM 113 O O . GLN A 1 14 ? 19.832 60.860 -14.755 1.00 28.54 ? 14 GLN A O 1 ATOM 114 C CB . GLN A 1 14 ? 20.630 61.709 -11.708 1.00 26.20 ? 14 GLN A CB 1 ATOM 115 C CG . GLN A 1 14 ? 21.962 61.265 -12.290 1.00 27.71 ? 14 GLN A CG 1 ATOM 116 C CD . GLN A 1 14 ? 23.164 61.808 -11.506 1.00 29.29 ? 14 GLN A CD 1 ATOM 117 O OE1 . GLN A 1 14 ? 24.021 61.045 -11.049 1.00 29.90 ? 14 GLN A OE1 1 ATOM 118 N NE2 . GLN A 1 14 ? 23.230 63.129 -11.357 1.00 26.66 ? 14 GLN A NE2 1 ATOM 119 N N . PRO A 1 15 ? 18.798 62.775 -14.189 1.00 27.73 ? 15 PRO A N 1 ATOM 120 C CA . PRO A 1 15 ? 18.752 63.231 -15.582 1.00 27.07 ? 15 PRO A CA 1 ATOM 121 C C . PRO A 1 15 ? 20.126 63.659 -16.087 1.00 26.36 ? 15 PRO A C 1 ATOM 122 O O . PRO A 1 15 ? 21.059 63.834 -15.304 1.00 25.55 ? 15 PRO A O 1 ATOM 123 C CB . PRO A 1 15 ? 17.772 64.394 -15.523 1.00 28.25 ? 15 PRO A CB 1 ATOM 124 C CG . PRO A 1 15 ? 18.073 64.988 -14.177 1.00 28.43 ? 15 PRO A CG 1 ATOM 125 C CD . PRO A 1 15 ? 18.184 63.764 -13.286 1.00 27.05 ? 15 PRO A CD 1 ATOM 126 N N . PRO A 1 16 ? 20.271 63.813 -17.410 1.00 26.49 ? 16 PRO A N 1 ATOM 127 C CA . PRO A 1 16 ? 21.553 64.231 -17.986 1.00 25.84 ? 16 PRO A CA 1 ATOM 128 C C . PRO A 1 16 ? 22.098 65.468 -17.263 1.00 26.66 ? 16 PRO A C 1 ATOM 129 O O . PRO A 1 16 ? 23.310 65.619 -17.097 1.00 26.88 ? 16 PRO A O 1 ATOM 130 C CB . PRO A 1 16 ? 21.193 64.496 -19.441 1.00 24.41 ? 16 PRO A CB 1 ATOM 131 C CG . PRO A 1 16 ? 20.182 63.412 -19.710 1.00 25.42 ? 16 PRO A CG 1 ATOM 132 C CD . PRO A 1 16 ? 19.302 63.475 -18.468 1.00 25.77 ? 16 PRO A CD 1 ATOM 133 N N . SER A 1 17 ? 21.193 66.344 -16.829 1.00 26.20 ? 17 SER A N 1 ATOM 134 C CA . SER A 1 17 ? 21.578 67.544 -16.095 1.00 26.99 ? 17 SER A CA 1 ATOM 135 C C . SER A 1 17 ? 20.369 68.275 -15.514 1.00 26.94 ? 17 SER A C 1 ATOM 136 O O . SER A 1 17 ? 19.225 67.840 -15.666 1.00 25.60 ? 17 SER A O 1 ATOM 137 C CB . SER A 1 17 ? 22.345 68.509 -16.993 1.00 27.64 ? 17 SER A CB 1 ATOM 138 O OG . SER A 1 17 ? 21.453 69.243 -17.811 1.00 31.06 ? 17 SER A OG 1 ATOM 139 N N . ASN A 1 18 ? 20.655 69.395 -14.854 1.00 26.63 ? 18 ASN A N 1 ATOM 140 C CA . ASN A 1 18 ? 19.656 70.254 -14.224 1.00 26.89 ? 18 ASN A CA 1 ATOM 141 C C . ASN A 1 18 ? 19.061 69.723 -12.932 1.00 26.55 ? 18 ASN A C 1 ATOM 142 O O . ASN A 1 18 ? 19.573 68.770 -12.340 1.00 26.84 ? 18 ASN A O 1 ATOM 143 C CB . ASN A 1 18 ? 18.527 70.584 -15.201 1.00 29.60 ? 18 ASN A CB 1 ATOM 144 C CG . ASN A 1 18 ? 19.019 71.346 -16.410 1.00 32.29 ? 18 ASN A CG 1 ATOM 145 O OD1 . ASN A 1 18 ? 19.735 72.344 -16.285 1.00 33.53 ? 18 ASN A OD1 1 ATOM 146 N ND2 . ASN A 1 18 ? 18.640 70.883 -17.591 1.00 33.92 ? 18 ASN A ND2 1 ATOM 147 N N . TRP A 1 19 ? 17.968 70.356 -12.513 1.00 24.70 ? 19 TRP A N 1 ATOM 148 C CA . TRP A 1 19 ? 17.274 70.023 -11.276 1.00 23.84 ? 19 TRP A CA 1 ATOM 149 C C . TRP A 1 19 ? 16.191 68.960 -11.364 1.00 25.36 ? 19 TRP A C 1 ATOM 150 O O . TRP A 1 19 ? 15.351 68.981 -12.261 1.00 26.72 ? 19 TRP A O 1 ATOM 151 C CB . TRP A 1 19 ? 16.665 71.293 -10.678 1.00 21.32 ? 19 TRP A CB 1 ATOM 152 C CG . TRP A 1 19 ? 15.719 71.064 -9.534 1.00 20.28 ? 19 TRP A CG 1 ATOM 153 C CD1 . TRP A 1 19 ? 14.442 70.571 -9.601 1.00 19.80 ? 19 TRP A CD1 1 ATOM 154 C CD2 . TRP A 1 19 ? 15.969 71.341 -8.152 1.00 19.16 ? 19 TRP A CD2 1 ATOM 155 N NE1 . TRP A 1 19 ? 13.885 70.529 -8.343 1.00 19.84 ? 19 TRP A NE1 1 ATOM 156 C CE2 . TRP A 1 19 ? 14.800 70.995 -7.437 1.00 19.12 ? 19 TRP A CE2 1 ATOM 157 C CE3 . TRP A 1 19 ? 17.070 71.852 -7.448 1.00 19.17 ? 19 TRP A CE3 1 ATOM 158 C CZ2 . TRP A 1 19 ? 14.698 71.144 -6.051 1.00 18.94 ? 19 TRP A CZ2 1 ATOM 159 C CZ3 . TRP A 1 19 ? 16.970 72.001 -6.068 1.00 17.84 ? 19 TRP A CZ3 1 ATOM 160 C CH2 . TRP A 1 19 ? 15.790 71.648 -5.386 1.00 18.48 ? 19 TRP A CH2 1 ATOM 161 N N . MET A 1 20 ? 16.208 68.047 -10.399 1.00 25.45 ? 20 MET A N 1 ATOM 162 C CA . MET A 1 20 ? 15.217 66.988 -10.306 1.00 24.74 ? 20 MET A CA 1 ATOM 163 C C . MET A 1 20 ? 14.826 66.778 -8.851 1.00 25.14 ? 20 MET A C 1 ATOM 164 O O . MET A 1 20 ? 15.698 66.727 -7.988 1.00 26.34 ? 20 MET A O 1 ATOM 165 C CB . MET A 1 20 ? 15.774 65.664 -10.842 1.00 22.88 ? 20 MET A CB 1 ATOM 166 C CG . MET A 1 20 ? 14.967 64.444 -10.363 1.00 23.15 ? 20 MET A CG 1 ATOM 167 S SD . MET A 1 20 ? 15.568 62.798 -10.864 1.00 23.83 ? 20 MET A SD 1 ATOM 168 C CE . MET A 1 20 ? 16.968 62.557 -9.754 1.00 22.49 ? 20 MET A CE 1 ATOM 169 N N . ASN A 1 21 ? 13.530 66.693 -8.560 1.00 24.33 ? 21 ASN A N 1 ATOM 170 C CA . ASN A 1 21 ? 13.131 66.381 -7.194 1.00 23.88 ? 21 ASN A CA 1 ATOM 171 C C . ASN A 1 21 ? 12.195 65.162 -7.145 1.00 23.39 ? 21 ASN A C 1 ATOM 172 O O . ASN A 1 21 ? 12.573 64.087 -7.602 1.00 23.38 ? 21 ASN A O 1 ATOM 173 C CB . ASN A 1 21 ? 12.565 67.604 -6.418 1.00 24.21 ? 21 ASN A CB 1 ATOM 174 C CG . ASN A 1 21 ? 11.460 68.354 -7.152 1.00 25.06 ? 21 ASN A CG 1 ATOM 175 O OD1 . ASN A 1 21 ? 11.690 68.973 -8.187 1.00 24.41 ? 21 ASN A OD1 1 ATOM 176 N ND2 . ASN A 1 21 ? 10.255 68.322 -6.591 1.00 22.71 ? 21 ASN A ND2 1 ATOM 177 N N . ASP A 1 22 ? 10.993 65.316 -6.605 1.00 23.68 ? 22 ASP A N 1 ATOM 178 C CA . ASP A 1 22 ? 10.034 64.213 -6.464 1.00 23.78 ? 22 ASP A CA 1 ATOM 179 C C . ASP A 1 22 ? 9.879 63.175 -7.570 1.00 23.67 ? 22 ASP A C 1 ATOM 180 O O . ASP A 1 22 ? 9.720 63.516 -8.741 1.00 25.04 ? 22 ASP A O 1 ATOM 181 C CB . ASP A 1 22 ? 8.643 64.775 -6.221 1.00 24.39 ? 22 ASP A CB 1 ATOM 182 C CG . ASP A 1 22 ? 8.579 65.669 -5.026 1.00 27.26 ? 22 ASP A CG 1 ATOM 183 O OD1 . ASP A 1 22 ? 9.602 66.310 -4.686 1.00 28.27 ? 22 ASP A OD1 1 ATOM 184 O OD2 . ASP A 1 22 ? 7.482 65.741 -4.439 1.00 27.24 ? 22 ASP A OD2 1 ATOM 185 N N . PRO A 1 23 ? 9.911 61.882 -7.210 1.00 24.21 ? 23 PRO A N 1 ATOM 186 C CA . PRO A 1 23 ? 9.737 60.843 -8.234 1.00 24.25 ? 23 PRO A CA 1 ATOM 187 C C . PRO A 1 23 ? 8.228 60.831 -8.570 1.00 23.79 ? 23 PRO A C 1 ATOM 188 O O . PRO A 1 23 ? 7.397 60.990 -7.676 1.00 23.35 ? 23 PRO A O 1 ATOM 189 C CB . PRO A 1 23 ? 10.199 59.573 -7.517 1.00 23.03 ? 23 PRO A CB 1 ATOM 190 C CG . PRO A 1 23 ? 9.890 59.857 -6.075 1.00 21.78 ? 23 PRO A CG 1 ATOM 191 C CD . PRO A 1 23 ? 10.325 61.289 -5.924 1.00 23.36 ? 23 PRO A CD 1 ATOM 192 N N . ASN A 1 24 ? 7.864 60.659 -9.837 1.00 23.91 ? 24 ASN A N 1 ATOM 193 C CA . ASN A 1 24 ? 6.450 60.684 -10.214 1.00 24.59 ? 24 ASN A CA 1 ATOM 194 C C . ASN A 1 24 ? 5.925 59.474 -10.985 1.00 25.28 ? 24 ASN A C 1 ATOM 195 O O . ASN A 1 24 ? 6.659 58.828 -11.736 1.00 23.96 ? 24 ASN A O 1 ATOM 196 C CB . ASN A 1 24 ? 6.160 61.947 -11.034 1.00 24.78 ? 24 ASN A CB 1 ATOM 197 C CG . ASN A 1 24 ? 6.278 63.222 -10.217 1.00 25.70 ? 24 ASN A CG 1 ATOM 198 O OD1 . ASN A 1 24 ? 6.550 64.292 -10.761 1.00 24.60 ? 24 ASN A OD1 1 ATOM 199 N ND2 . ASN A 1 24 ? 6.059 63.119 -8.910 1.00 27.05 ? 24 ASN A ND2 1 ATOM 200 N N . GLY A 1 25 ? 4.635 59.198 -10.792 1.00 24.68 ? 25 GLY A N 1 ATOM 201 C CA . GLY A 1 25 ? 3.954 58.101 -11.464 1.00 24.19 ? 25 GLY A CA 1 ATOM 202 C C . GLY A 1 25 ? 4.709 56.818 -11.781 1.00 24.49 ? 25 GLY A C 1 ATOM 203 O O . GLY A 1 25 ? 4.547 56.283 -12.876 1.00 24.60 ? 25 GLY A O 1 ATOM 204 N N . PRO A 1 26 ? 5.522 56.284 -10.854 1.00 23.80 ? 26 PRO A N 1 ATOM 205 C CA . PRO A 1 26 ? 6.263 55.047 -11.122 1.00 22.90 ? 26 PRO A CA 1 ATOM 206 C C . PRO A 1 26 ? 5.271 53.935 -11.419 1.00 24.54 ? 26 PRO A C 1 ATOM 207 O O . PRO A 1 26 ? 4.184 53.889 -10.834 1.00 24.77 ? 26 PRO A O 1 ATOM 208 C CB . PRO A 1 26 ? 6.992 54.775 -9.808 1.00 23.64 ? 26 PRO A CB 1 ATOM 209 C CG . PRO A 1 26 ? 7.022 56.093 -9.127 1.00 25.71 ? 26 PRO A CG 1 ATOM 210 C CD . PRO A 1 26 ? 5.699 56.704 -9.458 1.00 24.14 ? 26 PRO A CD 1 ATOM 211 N N . MET A 1 27 ? 5.641 53.028 -12.312 1.00 24.54 ? 27 MET A N 1 ATOM 212 C CA . MET A 1 27 ? 4.758 51.926 -12.646 1.00 24.48 ? 27 MET A CA 1 ATOM 213 C C . MET A 1 27 ? 5.436 50.956 -13.591 1.00 24.75 ? 27 MET A C 1 ATOM 214 O O . MET A 1 27 ? 6.507 51.231 -14.129 1.00 25.08 ? 27 MET A O 1 ATOM 215 C CB . MET A 1 27 ? 3.483 52.447 -13.311 1.00 24.41 ? 27 MET A CB 1 ATOM 216 C CG . MET A 1 27 ? 3.744 53.127 -14.654 1.00 26.39 ? 27 MET A CG 1 ATOM 217 S SD . MET A 1 27 ? 2.266 53.323 -15.684 1.00 28.44 ? 27 MET A SD 1 ATOM 218 C CE . MET A 1 27 ? 2.822 54.577 -16.902 1.00 25.67 ? 27 MET A CE 1 ATOM 219 N N . LEU A 1 28 ? 4.795 49.808 -13.772 1.00 25.06 ? 28 LEU A N 1 ATOM 220 C CA . LEU A 1 28 ? 5.262 48.777 -14.680 1.00 24.48 ? 28 LEU A CA 1 ATOM 221 C C . LEU A 1 28 ? 4.105 48.584 -15.648 1.00 25.08 ? 28 LEU A C 1 ATOM 222 O O . LEU A 1 28 ? 3.000 48.233 -15.235 1.00 25.55 ? 28 LEU A O 1 ATOM 223 C CB . LEU A 1 28 ? 5.529 47.473 -13.931 1.00 23.49 ? 28 LEU A CB 1 ATOM 224 C CG . LEU A 1 28 ? 5.722 46.226 -14.805 1.00 23.72 ? 28 LEU A CG 1 ATOM 225 C CD1 . LEU A 1 28 ? 6.959 46.366 -15.695 1.00 22.31 ? 28 LEU A CD1 1 ATOM 226 C CD2 . LEU A 1 28 ? 5.852 45.014 -13.904 1.00 22.00 ? 28 LEU A CD2 1 ATOM 227 N N . TYR A 1 29 ? 4.347 48.839 -16.928 1.00 25.45 ? 29 TYR A N 1 ATOM 228 C CA . TYR A 1 29 ? 3.301 48.685 -17.932 1.00 25.72 ? 29 TYR A CA 1 ATOM 229 C C . TYR A 1 29 ? 3.823 47.933 -19.147 1.00 26.06 ? 29 TYR A C 1 ATOM 230 O O . TYR A 1 29 ? 4.851 48.299 -19.722 1.00 25.12 ? 29 TYR A O 1 ATOM 231 C CB . TYR A 1 29 ? 2.771 50.052 -18.376 1.00 24.76 ? 29 TYR A CB 1 ATOM 232 C CG . TYR A 1 29 ? 1.562 49.962 -19.285 1.00 25.69 ? 29 TYR A CG 1 ATOM 233 C CD1 . TYR A 1 29 ? 0.328 49.535 -18.794 1.00 24.21 ? 29 TYR A CD1 1 ATOM 234 C CD2 . TYR A 1 29 ? 1.654 50.288 -20.643 1.00 25.50 ? 29 TYR A CD2 1 ATOM 235 C CE1 . TYR A 1 29 ? -0.788 49.431 -19.628 1.00 24.57 ? 29 TYR A CE1 1 ATOM 236 C CE2 . TYR A 1 29 ? 0.542 50.189 -21.489 1.00 24.57 ? 29 TYR A CE2 1 ATOM 237 C CZ . TYR A 1 29 ? -0.676 49.760 -20.975 1.00 25.83 ? 29 TYR A CZ 1 ATOM 238 O OH . TYR A 1 29 ? -1.779 49.662 -21.799 1.00 24.27 ? 29 TYR A OH 1 ATOM 239 N N . GLN A 1 30 ? 3.113 46.876 -19.530 1.00 26.02 ? 30 GLN A N 1 ATOM 240 C CA . GLN A 1 30 ? 3.504 46.089 -20.691 1.00 26.24 ? 30 GLN A CA 1 ATOM 241 C C . GLN A 1 30 ? 4.988 45.751 -20.675 1.00 24.93 ? 30 GLN A C 1 ATOM 242 O O . GLN A 1 30 ? 5.682 45.961 -21.670 1.00 24.04 ? 30 GLN A O 1 ATOM 243 C CB . GLN A 1 30 ? 3.183 46.852 -21.978 1.00 28.79 ? 30 GLN A CB 1 ATOM 244 C CG . GLN A 1 30 ? 1.715 47.174 -22.175 1.00 34.02 ? 30 GLN A CG 1 ATOM 245 C CD . GLN A 1 30 ? 0.850 45.930 -22.303 1.00 36.45 ? 30 GLN A CD 1 ATOM 246 O OE1 . GLN A 1 30 ? 0.699 45.166 -21.354 1.00 39.48 ? 30 GLN A OE1 1 ATOM 247 N NE2 . GLN A 1 30 ? 0.278 45.723 -23.483 1.00 37.43 ? 30 GLN A NE2 1 ATOM 248 N N . GLY A 1 31 ? 5.475 45.256 -19.541 1.00 24.34 ? 31 GLY A N 1 ATOM 249 C CA . GLY A 1 31 ? 6.870 44.868 -19.432 1.00 22.77 ? 31 GLY A CA 1 ATOM 250 C C . GLY A 1 31 ? 7.891 45.983 -19.404 1.00 24.12 ? 31 GLY A C 1 ATOM 251 O O . GLY A 1 31 ? 9.094 45.732 -19.483 1.00 24.69 ? 31 GLY A O 1 ATOM 252 N N . VAL A 1 32 ? 7.430 47.220 -19.298 1.00 23.18 ? 32 VAL A N 1 ATOM 253 C CA . VAL A 1 32 ? 8.357 48.340 -19.255 1.00 22.18 ? 32 VAL A CA 1 ATOM 254 C C . VAL A 1 32 ? 8.194 49.115 -17.954 1.00 22.50 ? 32 VAL A C 1 ATOM 255 O O . VAL A 1 32 ? 7.078 49.399 -17.520 1.00 23.00 ? 32 VAL A O 1 ATOM 256 C CB . VAL A 1 32 ? 8.131 49.291 -20.451 1.00 22.40 ? 32 VAL A CB 1 ATOM 257 C CG1 . VAL A 1 32 ? 9.000 50.532 -20.304 1.00 21.25 ? 32 VAL A CG1 1 ATOM 258 C CG2 . VAL A 1 32 ? 8.447 48.568 -21.749 1.00 19.55 ? 32 VAL A CG2 1 ATOM 259 N N . TYR A 1 33 ? 9.311 49.435 -17.318 1.00 21.99 ? 33 TYR A N 1 ATOM 260 C CA . TYR A 1 33 ? 9.262 50.200 -16.081 1.00 21.59 ? 33 TYR A CA 1 ATOM 261 C C . TYR A 1 33 ? 9.310 51.667 -16.467 1.00 20.81 ? 33 TYR A C 1 ATOM 262 O O . TYR A 1 33 ? 10.229 52.118 -17.162 1.00 20.16 ? 33 TYR A O 1 ATOM 263 C CB . TYR A 1 33 ? 10.452 49.862 -15.180 1.00 22.98 ? 33 TYR A CB 1 ATOM 264 C CG . TYR A 1 33 ? 10.373 48.504 -14.528 1.00 22.66 ? 33 TYR A CG 1 ATOM 265 C CD1 . TYR A 1 33 ? 9.544 48.281 -13.424 1.00 23.27 ? 33 TYR A CD1 1 ATOM 266 C CD2 . TYR A 1 33 ? 11.114 47.431 -15.024 1.00 21.90 ? 33 TYR A CD2 1 ATOM 267 C CE1 . TYR A 1 33 ? 9.459 47.017 -12.834 1.00 22.98 ? 33 TYR A CE1 1 ATOM 268 C CE2 . TYR A 1 33 ? 11.034 46.173 -14.443 1.00 20.90 ? 33 TYR A CE2 1 ATOM 269 C CZ . TYR A 1 33 ? 10.208 45.969 -13.354 1.00 21.78 ? 33 TYR A CZ 1 ATOM 270 O OH . TYR A 1 33 ? 10.130 44.708 -12.810 1.00 23.44 ? 33 TYR A OH 1 ATOM 271 N N . HIS A 1 34 ? 8.302 52.406 -16.032 1.00 20.10 ? 34 HIS A N 1 ATOM 272 C CA . HIS A 1 34 ? 8.229 53.822 -16.332 1.00 20.12 ? 34 HIS A CA 1 ATOM 273 C C . HIS A 1 34 ? 8.576 54.615 -15.097 1.00 20.50 ? 34 HIS A C 1 ATOM 274 O O . HIS A 1 34 ? 8.117 54.306 -13.999 1.00 20.26 ? 34 HIS A O 1 ATOM 275 C CB . HIS A 1 34 ? 6.819 54.202 -16.783 1.00 19.96 ? 34 HIS A CB 1 ATOM 276 C CG . HIS A 1 34 ? 6.489 53.763 -18.172 1.00 20.32 ? 34 HIS A CG 1 ATOM 277 N ND1 . HIS A 1 34 ? 6.700 54.565 -19.274 1.00 21.21 ? 34 HIS A ND1 1 ATOM 278 C CD2 . HIS A 1 34 ? 5.983 52.600 -18.644 1.00 21.44 ? 34 HIS A CD2 1 ATOM 279 C CE1 . HIS A 1 34 ? 6.337 53.914 -20.363 1.00 22.98 ? 34 HIS A CE1 1 ATOM 280 N NE2 . HIS A 1 34 ? 5.899 52.717 -20.010 1.00 22.57 ? 34 HIS A NE2 1 ATOM 281 N N . PHE A 1 35 ? 9.404 55.633 -15.280 1.00 21.44 ? 35 PHE A N 1 ATOM 282 C CA . PHE A 1 35 ? 9.774 56.503 -14.183 1.00 20.34 ? 35 PHE A CA 1 ATOM 283 C C . PHE A 1 35 ? 9.603 57.953 -14.631 1.00 20.25 ? 35 PHE A C 1 ATOM 284 O O . PHE A 1 35 ? 9.991 58.320 -15.741 1.00 20.22 ? 35 PHE A O 1 ATOM 285 C CB . PHE A 1 35 ? 11.218 56.268 -13.749 1.00 19.15 ? 35 PHE A CB 1 ATOM 286 C CG . PHE A 1 35 ? 11.614 57.094 -12.561 1.00 20.14 ? 35 PHE A CG 1 ATOM 287 C CD1 . PHE A 1 35 ? 11.023 56.864 -11.319 1.00 17.21 ? 35 PHE A CD1 1 ATOM 288 C CD2 . PHE A 1 35 ? 12.501 58.160 -12.700 1.00 16.63 ? 35 PHE A CD2 1 ATOM 289 C CE1 . PHE A 1 35 ? 11.304 57.685 -10.234 1.00 16.66 ? 35 PHE A CE1 1 ATOM 290 C CE2 . PHE A 1 35 ? 12.784 58.985 -11.620 1.00 16.99 ? 35 PHE A CE2 1 ATOM 291 C CZ . PHE A 1 35 ? 12.182 58.747 -10.384 1.00 15.85 ? 35 PHE A CZ 1 ATOM 292 N N . PHE A 1 36 ? 9.001 58.764 -13.771 1.00 20.08 ? 36 PHE A N 1 ATOM 293 C CA . PHE A 1 36 ? 8.775 60.172 -14.064 1.00 21.35 ? 36 PHE A CA 1 ATOM 294 C C . PHE A 1 36 ? 9.325 60.924 -12.867 1.00 22.93 ? 36 PHE A C 1 ATOM 295 O O . PHE A 1 36 ? 9.551 60.326 -11.816 1.00 22.87 ? 36 PHE A O 1 ATOM 296 C CB . PHE A 1 36 ? 7.278 60.456 -14.210 1.00 20.56 ? 36 PHE A CB 1 ATOM 297 C CG . PHE A 1 36 ? 6.605 59.641 -15.280 1.00 21.68 ? 36 PHE A CG 1 ATOM 298 C CD1 . PHE A 1 36 ? 6.550 60.097 -16.593 1.00 20.39 ? 36 PHE A CD1 1 ATOM 299 C CD2 . PHE A 1 36 ? 6.022 58.412 -14.971 1.00 22.37 ? 36 PHE A CD2 1 ATOM 300 C CE1 . PHE A 1 36 ? 5.918 59.344 -17.587 1.00 20.40 ? 36 PHE A CE1 1 ATOM 301 C CE2 . PHE A 1 36 ? 5.389 57.647 -15.956 1.00 21.64 ? 36 PHE A CE2 1 ATOM 302 C CZ . PHE A 1 36 ? 5.336 58.115 -17.266 1.00 21.64 ? 36 PHE A CZ 1 ATOM 303 N N . TYR A 1 37 ? 9.532 62.228 -13.012 1.00 23.05 ? 37 TYR A N 1 ATOM 304 C CA . TYR A 1 37 ? 10.072 63.013 -11.912 1.00 23.13 ? 37 TYR A CA 1 ATOM 305 C C . TYR A 1 37 ? 9.950 64.516 -12.123 1.00 24.04 ? 37 TYR A C 1 ATOM 306 O O . TYR A 1 37 ? 9.987 64.999 -13.255 1.00 23.07 ? 37 TYR A O 1 ATOM 307 C CB . TYR A 1 37 ? 11.546 62.665 -11.716 1.00 21.13 ? 37 TYR A CB 1 ATOM 308 C CG . TYR A 1 37 ? 12.350 62.808 -12.985 1.00 21.18 ? 37 TYR A CG 1 ATOM 309 C CD1 . TYR A 1 37 ? 12.366 61.794 -13.946 1.00 20.49 ? 37 TYR A CD1 1 ATOM 310 C CD2 . TYR A 1 37 ? 13.075 63.973 -13.242 1.00 20.87 ? 37 TYR A CD2 1 ATOM 311 C CE1 . TYR A 1 37 ? 13.091 61.940 -15.134 1.00 20.38 ? 37 TYR A CE1 1 ATOM 312 C CE2 . TYR A 1 37 ? 13.798 64.130 -14.423 1.00 19.51 ? 37 TYR A CE2 1 ATOM 313 C CZ . TYR A 1 37 ? 13.803 63.112 -15.365 1.00 20.75 ? 37 TYR A CZ 1 ATOM 314 O OH . TYR A 1 37 ? 14.520 63.278 -16.532 1.00 20.40 ? 37 TYR A OH 1 ATOM 315 N N . GLN A 1 38 ? 9.808 65.247 -11.018 1.00 24.64 ? 38 GLN A N 1 ATOM 316 C CA . GLN A 1 38 ? 9.728 66.702 -11.051 1.00 24.13 ? 38 GLN A CA 1 ATOM 317 C C . GLN A 1 38 ? 11.048 67.203 -11.648 1.00 24.75 ? 38 GLN A C 1 ATOM 318 O O . GLN A 1 38 ? 12.131 66.915 -11.127 1.00 23.01 ? 38 GLN A O 1 ATOM 319 C CB . GLN A 1 38 ? 9.536 67.241 -9.630 1.00 22.83 ? 38 GLN A CB 1 ATOM 320 C CG . GLN A 1 38 ? 8.176 66.912 -9.044 1.00 21.37 ? 38 GLN A CG 1 ATOM 321 C CD . GLN A 1 38 ? 7.050 67.651 -9.750 1.00 21.58 ? 38 GLN A CD 1 ATOM 322 O OE1 . GLN A 1 38 ? 6.779 68.819 -9.466 1.00 21.43 ? 38 GLN A OE1 1 ATOM 323 N NE2 . GLN A 1 38 ? 6.401 66.978 -10.691 1.00 23.07 ? 38 GLN A NE2 1 ATOM 324 N N . TYR A 1 39 ? 10.953 67.958 -12.737 1.00 24.79 ? 39 TYR A N 1 ATOM 325 C CA . TYR A 1 39 ? 12.139 68.446 -13.427 1.00 25.74 ? 39 TYR A CA 1 ATOM 326 C C . TYR A 1 39 ? 12.080 69.913 -13.847 1.00 27.16 ? 39 TYR A C 1 ATOM 327 O O . TYR A 1 39 ? 11.026 70.423 -14.236 1.00 28.24 ? 39 TYR A O 1 ATOM 328 C CB . TYR A 1 39 ? 12.360 67.567 -14.658 1.00 24.56 ? 39 TYR A CB 1 ATOM 329 C CG . TYR A 1 39 ? 13.519 67.941 -15.549 1.00 23.95 ? 39 TYR A CG 1 ATOM 330 C CD1 . TYR A 1 39 ? 13.304 68.412 -16.845 1.00 23.31 ? 39 TYR A CD1 1 ATOM 331 C CD2 . TYR A 1 39 ? 14.835 67.751 -15.127 1.00 23.96 ? 39 TYR A CD2 1 ATOM 332 C CE1 . TYR A 1 39 ? 14.373 68.676 -17.702 1.00 23.34 ? 39 TYR A CE1 1 ATOM 333 C CE2 . TYR A 1 39 ? 15.910 68.011 -15.975 1.00 24.05 ? 39 TYR A CE2 1 ATOM 334 C CZ . TYR A 1 39 ? 15.673 68.469 -17.259 1.00 24.13 ? 39 TYR A CZ 1 ATOM 335 O OH . TYR A 1 39 ? 16.737 68.692 -18.102 1.00 25.21 ? 39 TYR A OH 1 ATOM 336 N N . ASN A 1 40 ? 13.218 70.593 -13.752 1.00 28.23 ? 40 ASN A N 1 ATOM 337 C CA . ASN A 1 40 ? 13.314 71.982 -14.182 1.00 30.69 ? 40 ASN A CA 1 ATOM 338 C C . ASN A 1 40 ? 14.210 71.953 -15.413 1.00 31.27 ? 40 ASN A C 1 ATOM 339 O O . ASN A 1 40 ? 15.411 71.700 -15.314 1.00 31.69 ? 40 ASN A O 1 ATOM 340 C CB . ASN A 1 40 ? 13.957 72.870 -13.119 1.00 31.52 ? 40 ASN A CB 1 ATOM 341 C CG . ASN A 1 40 ? 13.947 74.340 -13.517 1.00 32.37 ? 40 ASN A CG 1 ATOM 342 O OD1 . ASN A 1 40 ? 13.731 74.670 -14.688 1.00 29.83 ? 40 ASN A OD1 1 ATOM 343 N ND2 . ASN A 1 40 ? 14.190 75.227 -12.552 1.00 30.79 ? 40 ASN A ND2 1 ATOM 344 N N . PRO A 1 41 ? 13.635 72.209 -16.591 1.00 31.96 ? 41 PRO A N 1 ATOM 345 C CA . PRO A 1 41 ? 14.424 72.191 -17.824 1.00 33.03 ? 41 PRO A CA 1 ATOM 346 C C . PRO A 1 41 ? 15.334 73.402 -17.960 1.00 33.38 ? 41 PRO A C 1 ATOM 347 O O . PRO A 1 41 ? 16.209 73.433 -18.821 1.00 34.51 ? 41 PRO A O 1 ATOM 348 C CB . PRO A 1 41 ? 13.361 72.179 -18.925 1.00 32.57 ? 41 PRO A CB 1 ATOM 349 C CG . PRO A 1 41 ? 12.054 71.862 -18.201 1.00 32.46 ? 41 PRO A CG 1 ATOM 350 C CD . PRO A 1 41 ? 12.225 72.512 -16.875 1.00 30.78 ? 41 PRO A CD 1 ATOM 351 N N . TYR A 1 42 ? 15.142 74.385 -17.093 1.00 32.57 ? 42 TYR A N 1 ATOM 352 C CA . TYR A 1 42 ? 15.908 75.613 -17.194 1.00 33.86 ? 42 TYR A CA 1 ATOM 353 C C . TYR A 1 42 ? 16.997 75.905 -16.174 1.00 33.67 ? 42 TYR A C 1 ATOM 354 O O . TYR A 1 42 ? 17.724 76.881 -16.333 1.00 35.50 ? 42 TYR A O 1 ATOM 355 C CB . TYR A 1 42 ? 14.928 76.778 -17.235 1.00 34.71 ? 42 TYR A CB 1 ATOM 356 C CG . TYR A 1 42 ? 13.812 76.541 -18.217 1.00 37.41 ? 42 TYR A CG 1 ATOM 357 C CD1 . TYR A 1 42 ? 12.483 76.461 -17.794 1.00 38.56 ? 42 TYR A CD1 1 ATOM 358 C CD2 . TYR A 1 42 ? 14.085 76.372 -19.577 1.00 37.81 ? 42 TYR A CD2 1 ATOM 359 C CE1 . TYR A 1 42 ? 11.455 76.220 -18.702 1.00 40.18 ? 42 TYR A CE1 1 ATOM 360 C CE2 . TYR A 1 42 ? 13.068 76.129 -20.491 1.00 39.30 ? 42 TYR A CE2 1 ATOM 361 C CZ . TYR A 1 42 ? 11.755 76.055 -20.053 1.00 40.77 ? 42 TYR A CZ 1 ATOM 362 O OH . TYR A 1 42 ? 10.752 75.825 -20.972 1.00 41.29 ? 42 TYR A OH 1 ATOM 363 N N . ALA A 1 43 ? 17.128 75.088 -15.134 1.00 32.56 ? 43 ALA A N 1 ATOM 364 C CA . ALA A 1 43 ? 18.164 75.351 -14.142 1.00 31.07 ? 43 ALA A CA 1 ATOM 365 C C . ALA A 1 43 ? 18.455 74.178 -13.227 1.00 30.84 ? 43 ALA A C 1 ATOM 366 O O . ALA A 1 43 ? 17.742 73.179 -13.228 1.00 30.46 ? 43 ALA A O 1 ATOM 367 C CB . ALA A 1 43 ? 17.784 76.567 -13.304 1.00 30.55 ? 43 ALA A CB 1 ATOM 368 N N . ALA A 1 44 ? 19.522 74.323 -12.448 1.00 30.94 ? 44 ALA A N 1 ATOM 369 C CA . ALA A 1 44 ? 19.941 73.315 -11.489 1.00 29.99 ? 44 ALA A CA 1 ATOM 370 C C . ALA A 1 44 ? 19.386 73.710 -10.123 1.00 30.12 ? 44 ALA A C 1 ATOM 371 O O . ALA A 1 44 ? 19.983 73.425 -9.085 1.00 30.09 ? 44 ALA A O 1 ATOM 372 C CB . ALA A 1 44 ? 21.462 73.232 -11.440 1.00 29.37 ? 44 ALA A CB 1 ATOM 373 N N . THR A 1 45 ? 18.242 74.385 -10.142 1.00 29.41 ? 45 THR A N 1 ATOM 374 C CA . THR A 1 45 ? 17.567 74.817 -8.925 1.00 30.18 ? 45 THR A CA 1 ATOM 375 C C . THR A 1 45 ? 16.083 74.711 -9.211 1.00 29.93 ? 45 THR A C 1 ATOM 376 O O . THR A 1 45 ? 15.679 74.547 -10.360 1.00 30.50 ? 45 THR A O 1 ATOM 377 C CB . THR A 1 45 ? 17.858 76.295 -8.584 1.00 32.13 ? 45 THR A CB 1 ATOM 378 O OG1 . THR A 1 45 ? 17.214 77.144 -9.546 1.00 29.95 ? 45 THR A OG1 1 ATOM 379 C CG2 . THR A 1 45 ? 19.355 76.568 -8.597 1.00 33.00 ? 45 THR A CG2 1 ATOM 380 N N . PHE A 1 46 ? 15.263 74.802 -8.175 1.00 29.38 ? 46 PHE A N 1 ATOM 381 C CA . PHE A 1 46 ? 13.831 74.739 -8.386 1.00 29.65 ? 46 PHE A CA 1 ATOM 382 C C . PHE A 1 46 ? 13.464 75.990 -9.191 1.00 31.34 ? 46 PHE A C 1 ATOM 383 O O . PHE A 1 46 ? 14.224 76.964 -9.209 1.00 31.18 ? 46 PHE A O 1 ATOM 384 C CB . PHE A 1 46 ? 13.101 74.748 -7.052 1.00 27.68 ? 46 PHE A CB 1 ATOM 385 C CG . PHE A 1 46 ? 11.672 74.322 -7.151 1.00 28.22 ? 46 PHE A CG 1 ATOM 386 C CD1 . PHE A 1 46 ? 11.347 72.990 -7.403 1.00 28.11 ? 46 PHE A CD1 1 ATOM 387 C CD2 . PHE A 1 46 ? 10.646 75.249 -6.999 1.00 26.46 ? 46 PHE A CD2 1 ATOM 388 C CE1 . PHE A 1 46 ? 10.014 72.585 -7.501 1.00 28.34 ? 46 PHE A CE1 1 ATOM 389 C CE2 . PHE A 1 46 ? 9.313 74.861 -7.094 1.00 26.35 ? 46 PHE A CE2 1 ATOM 390 C CZ . PHE A 1 46 ? 8.993 73.524 -7.344 1.00 28.75 ? 46 PHE A CZ 1 ATOM 391 N N . GLY A 1 47 ? 12.312 75.963 -9.859 1.00 32.06 ? 47 GLY A N 1 ATOM 392 C CA . GLY A 1 47 ? 11.903 77.109 -10.655 1.00 31.51 ? 47 GLY A CA 1 ATOM 393 C C . GLY A 1 47 ? 10.404 77.259 -10.805 1.00 31.86 ? 47 GLY A C 1 ATOM 394 O O . GLY A 1 47 ? 9.636 76.433 -10.308 1.00 30.90 ? 47 GLY A O 1 ATOM 395 N N . ASP A 1 48 ? 9.985 78.316 -11.496 1.00 33.15 ? 48 ASP A N 1 ATOM 396 C CA . ASP A 1 48 ? 8.564 78.580 -11.715 1.00 34.36 ? 48 ASP A CA 1 ATOM 397 C C . ASP A 1 48 ? 7.946 77.595 -12.686 1.00 32.69 ? 48 ASP A C 1 ATOM 398 O O . ASP A 1 48 ? 6.727 77.444 -12.732 1.00 32.37 ? 48 ASP A O 1 ATOM 399 C CB . ASP A 1 48 ? 8.346 79.991 -12.256 1.00 37.59 ? 48 ASP A CB 1 ATOM 400 C CG . ASP A 1 48 ? 8.904 81.060 -11.341 1.00 41.68 ? 48 ASP A CG 1 ATOM 401 O OD1 . ASP A 1 48 ? 8.740 80.929 -10.106 1.00 42.50 ? 48 ASP A OD1 1 ATOM 402 O OD2 . ASP A 1 48 ? 9.495 82.034 -11.864 1.00 43.49 ? 48 ASP A OD2 1 ATOM 403 N N . VAL A 1 49 ? 8.785 76.942 -13.476 1.00 30.72 ? 49 VAL A N 1 ATOM 404 C CA . VAL A 1 49 ? 8.292 75.969 -14.435 1.00 29.63 ? 49 VAL A CA 1 ATOM 405 C C . VAL A 1 49 ? 8.877 74.591 -14.155 1.00 29.39 ? 49 VAL A C 1 ATOM 406 O O . VAL A 1 49 ? 10.052 74.334 -14.424 1.00 27.18 ? 49 VAL A O 1 ATOM 407 C CB . VAL A 1 49 ? 8.639 76.379 -15.882 1.00 30.59 ? 49 VAL A CB 1 ATOM 408 C CG1 . VAL A 1 49 ? 8.147 75.316 -16.854 1.00 28.56 ? 49 VAL A CG1 1 ATOM 409 C CG2 . VAL A 1 49 ? 8.004 77.720 -16.208 1.00 29.40 ? 49 VAL A CG2 1 ATOM 410 N N . ILE A 1 50 ? 8.045 73.715 -13.600 1.00 28.32 ? 50 ILE A N 1 ATOM 411 C CA . ILE A 1 50 ? 8.444 72.349 -13.290 1.00 27.94 ? 50 ILE A CA 1 ATOM 412 C C . ILE A 1 50 ? 7.605 71.392 -14.122 1.00 28.68 ? 50 ILE A C 1 ATOM 413 O O . ILE A 1 50 ? 6.383 71.542 -14.220 1.00 28.10 ? 50 ILE A O 1 ATOM 414 C CB . ILE A 1 50 ? 8.223 72.018 -11.809 1.00 28.54 ? 50 ILE A CB 1 ATOM 415 C CG1 . ILE A 1 50 ? 9.145 72.881 -10.942 1.00 29.21 ? 50 ILE A CG1 1 ATOM 416 C CG2 . ILE A 1 50 ? 8.455 70.530 -11.573 1.00 27.07 ? 50 ILE A CG2 1 ATOM 417 C CD1 . ILE A 1 50 ? 10.628 72.648 -11.181 1.00 29.24 ? 50 ILE A CD1 1 ATOM 418 N N . ILE A 1 51 ? 8.261 70.406 -14.719 1.00 27.68 ? 51 ILE A N 1 ATOM 419 C CA . ILE A 1 51 ? 7.556 69.441 -15.544 1.00 26.61 ? 51 ILE A CA 1 ATOM 420 C C . ILE A 1 51 ? 7.982 68.012 -15.211 1.00 27.44 ? 51 ILE A C 1 ATOM 421 O O . ILE A 1 51 ? 8.964 67.799 -14.499 1.00 28.93 ? 51 ILE A O 1 ATOM 422 C CB . ILE A 1 51 ? 7.807 69.723 -17.031 1.00 24.86 ? 51 ILE A CB 1 ATOM 423 C CG1 . ILE A 1 51 ? 9.280 69.498 -17.367 1.00 24.70 ? 51 ILE A CG1 1 ATOM 424 C CG2 . ILE A 1 51 ? 7.436 71.159 -17.343 1.00 24.03 ? 51 ILE A CG2 1 ATOM 425 C CD1 . ILE A 1 51 ? 9.612 69.714 -18.830 1.00 22.04 ? 51 ILE A CD1 1 ATOM 426 N N . TRP A 1 52 ? 7.232 67.043 -15.732 1.00 26.38 ? 52 TRP A N 1 ATOM 427 C CA . TRP A 1 52 ? 7.496 65.624 -15.514 1.00 22.84 ? 52 TRP A CA 1 ATOM 428 C C . TRP A 1 52 ? 8.531 65.048 -16.470 1.00 22.98 ? 52 TRP A C 1 ATOM 429 O O . TRP A 1 52 ? 8.263 64.896 -17.659 1.00 22.55 ? 52 TRP A O 1 ATOM 430 C CB . TRP A 1 52 ? 6.206 64.815 -15.673 1.00 21.25 ? 52 TRP A CB 1 ATOM 431 C CG . TRP A 1 52 ? 5.286 64.858 -14.492 1.00 18.61 ? 52 TRP A CG 1 ATOM 432 C CD1 . TRP A 1 52 ? 4.991 65.943 -13.720 1.00 17.07 ? 52 TRP A CD1 1 ATOM 433 C CD2 . TRP A 1 52 ? 4.523 63.767 -13.961 1.00 16.96 ? 52 TRP A CD2 1 ATOM 434 N NE1 . TRP A 1 52 ? 4.095 65.596 -12.737 1.00 16.09 ? 52 TRP A NE1 1 ATOM 435 C CE2 . TRP A 1 52 ? 3.789 64.266 -12.861 1.00 16.55 ? 52 TRP A CE2 1 ATOM 436 C CE3 . TRP A 1 52 ? 4.387 62.414 -14.310 1.00 15.47 ? 52 TRP A CE3 1 ATOM 437 C CZ2 . TRP A 1 52 ? 2.933 63.460 -12.099 1.00 15.01 ? 52 TRP A CZ2 1 ATOM 438 C CZ3 . TRP A 1 52 ? 3.536 61.613 -13.556 1.00 15.55 ? 52 TRP A CZ3 1 ATOM 439 C CH2 . TRP A 1 52 ? 2.819 62.141 -12.460 1.00 16.26 ? 52 TRP A CH2 1 ATOM 440 N N . GLY A 1 53 ? 9.712 64.731 -15.949 1.00 23.53 ? 53 GLY A N 1 ATOM 441 C CA . GLY A 1 53 ? 10.731 64.114 -16.777 1.00 22.61 ? 53 GLY A CA 1 ATOM 442 C C . GLY A 1 53 ? 10.234 62.696 -17.001 1.00 23.38 ? 53 GLY A C 1 ATOM 443 O O . GLY A 1 53 ? 9.360 62.227 -16.266 1.00 23.06 ? 53 GLY A O 1 ATOM 444 N N . HIS A 1 54 ? 10.776 61.996 -17.991 1.00 23.78 ? 54 HIS A N 1 ATOM 445 C CA . HIS A 1 54 ? 10.317 60.640 -18.279 1.00 22.08 ? 54 HIS A CA 1 ATOM 446 C C . HIS A 1 54 ? 11.464 59.764 -18.780 1.00 22.83 ? 54 HIS A C 1 ATOM 447 O O . HIS A 1 54 ? 12.243 60.170 -19.650 1.00 21.18 ? 54 HIS A O 1 ATOM 448 C CB . HIS A 1 54 ? 9.180 60.726 -19.311 1.00 23.05 ? 54 HIS A CB 1 ATOM 449 C CG . HIS A 1 54 ? 8.551 59.410 -19.667 1.00 23.91 ? 54 HIS A CG 1 ATOM 450 N ND1 . HIS A 1 54 ? 8.453 58.359 -18.784 1.00 25.63 ? 54 HIS A ND1 1 ATOM 451 C CD2 . HIS A 1 54 ? 7.920 59.011 -20.799 1.00 22.48 ? 54 HIS A CD2 1 ATOM 452 C CE1 . HIS A 1 54 ? 7.789 57.366 -19.355 1.00 23.37 ? 54 HIS A CE1 1 ATOM 453 N NE2 . HIS A 1 54 ? 7.453 57.738 -20.575 1.00 23.34 ? 54 HIS A NE2 1 ATOM 454 N N . ALA A 1 55 ? 11.571 58.569 -18.200 1.00 22.81 ? 55 ALA A N 1 ATOM 455 C CA . ALA A 1 55 ? 12.601 57.598 -18.565 1.00 22.55 ? 55 ALA A CA 1 ATOM 456 C C . ALA A 1 55 ? 12.002 56.208 -18.424 1.00 22.36 ? 55 ALA A C 1 ATOM 457 O O . ALA A 1 55 ? 11.087 56.003 -17.625 1.00 21.70 ? 55 ALA A O 1 ATOM 458 C CB . ALA A 1 55 ? 13.815 57.737 -17.654 1.00 21.58 ? 55 ALA A CB 1 ATOM 459 N N . VAL A 1 56 ? 12.507 55.259 -19.203 1.00 21.53 ? 56 VAL A N 1 ATOM 460 C CA . VAL A 1 56 ? 11.997 53.899 -19.140 1.00 21.28 ? 56 VAL A CA 1 ATOM 461 C C . VAL A 1 56 ? 13.106 52.875 -18.935 1.00 21.74 ? 56 VAL A C 1 ATOM 462 O O . VAL A 1 56 ? 14.277 53.139 -19.212 1.00 21.16 ? 56 VAL A O 1 ATOM 463 C CB . VAL A 1 56 ? 11.210 53.542 -20.417 1.00 21.90 ? 56 VAL A CB 1 ATOM 464 C CG1 . VAL A 1 56 ? 9.914 54.339 -20.461 1.00 21.33 ? 56 VAL A CG1 1 ATOM 465 C CG2 . VAL A 1 56 ? 12.056 53.823 -21.657 1.00 20.28 ? 56 VAL A CG2 1 ATOM 466 N N . SER A 1 57 ? 12.730 51.703 -18.443 1.00 21.61 ? 57 SER A N 1 ATOM 467 C CA . SER A 1 57 ? 13.702 50.651 -18.198 1.00 23.20 ? 57 SER A CA 1 ATOM 468 C C . SER A 1 57 ? 13.078 49.262 -18.191 1.00 24.55 ? 57 SER A C 1 ATOM 469 O O . SER A 1 57 ? 11.887 49.096 -17.933 1.00 26.08 ? 57 SER A O 1 ATOM 470 C CB . SER A 1 57 ? 14.402 50.890 -16.860 1.00 20.72 ? 57 SER A CB 1 ATOM 471 O OG . SER A 1 57 ? 15.279 49.821 -16.566 1.00 21.42 ? 57 SER A OG 1 ATOM 472 N N . TYR A 1 58 ? 13.894 48.261 -18.476 1.00 25.07 ? 58 TYR A N 1 ATOM 473 C CA . TYR A 1 58 ? 13.424 46.891 -18.471 1.00 26.02 ? 58 TYR A CA 1 ATOM 474 C C . TYR A 1 58 ? 13.888 46.203 -17.192 1.00 26.15 ? 58 TYR A C 1 ATOM 475 O O . TYR A 1 58 ? 13.419 45.115 -16.868 1.00 27.90 ? 58 TYR A O 1 ATOM 476 C CB . TYR A 1 58 ? 13.982 46.140 -19.674 1.00 25.56 ? 58 TYR A CB 1 ATOM 477 C CG . TYR A 1 58 ? 13.502 46.669 -20.998 1.00 28.25 ? 58 TYR A CG 1 ATOM 478 C CD1 . TYR A 1 58 ? 12.169 46.510 -21.394 1.00 29.85 ? 58 TYR A CD1 1 ATOM 479 C CD2 . TYR A 1 58 ? 14.375 47.324 -21.866 1.00 27.78 ? 58 TYR A CD2 1 ATOM 480 C CE1 . TYR A 1 58 ? 11.722 46.989 -22.625 1.00 29.67 ? 58 TYR A CE1 1 ATOM 481 C CE2 . TYR A 1 58 ? 13.938 47.806 -23.097 1.00 29.01 ? 58 TYR A CE2 1 ATOM 482 C CZ . TYR A 1 58 ? 12.614 47.636 -23.470 1.00 30.77 ? 58 TYR A CZ 1 ATOM 483 O OH . TYR A 1 58 ? 12.184 48.112 -24.691 1.00 34.79 ? 58 TYR A OH 1 ATOM 484 N N . ASP A 1 59 ? 14.795 46.848 -16.460 1.00 24.92 ? 59 ASP A N 1 ATOM 485 C CA . ASP A 1 59 ? 15.344 46.259 -15.242 1.00 24.75 ? 59 ASP A CA 1 ATOM 486 C C . ASP A 1 59 ? 15.467 47.188 -14.029 1.00 25.46 ? 59 ASP A C 1 ATOM 487 O O . ASP A 1 59 ? 15.997 46.782 -12.995 1.00 25.96 ? 59 ASP A O 1 ATOM 488 C CB . ASP A 1 59 ? 16.721 45.682 -15.549 1.00 22.93 ? 59 ASP A CB 1 ATOM 489 C CG . ASP A 1 59 ? 17.610 46.671 -16.289 1.00 25.42 ? 59 ASP A CG 1 ATOM 490 O OD1 . ASP A 1 59 ? 17.575 47.878 -15.960 1.00 23.70 ? 59 ASP A OD1 1 ATOM 491 O OD2 . ASP A 1 59 ? 18.349 46.241 -17.197 1.00 27.00 ? 59 ASP A OD2 1 ATOM 492 N N . LEU A 1 60 ? 14.988 48.423 -14.151 1.00 25.52 ? 60 LEU A N 1 ATOM 493 C CA . LEU A 1 60 ? 15.069 49.404 -13.063 1.00 24.20 ? 60 LEU A CA 1 ATOM 494 C C . LEU A 1 60 ? 16.513 49.830 -12.796 1.00 23.88 ? 60 LEU A C 1 ATOM 495 O O . LEU A 1 60 ? 16.789 50.547 -11.835 1.00 24.00 ? 60 LEU A O 1 ATOM 496 C CB . LEU A 1 60 ? 14.457 48.842 -11.772 1.00 23.95 ? 60 LEU A CB 1 ATOM 497 C CG . LEU A 1 60 ? 12.930 48.721 -11.706 1.00 23.18 ? 60 LEU A CG 1 ATOM 498 C CD1 . LEU A 1 60 ? 12.529 47.944 -10.466 1.00 21.89 ? 60 LEU A CD1 1 ATOM 499 C CD2 . LEU A 1 60 ? 12.305 50.111 -11.692 1.00 24.02 ? 60 LEU A CD2 1 ATOM 500 N N . VAL A 1 61 ? 17.432 49.391 -13.649 1.00 21.55 ? 61 VAL A N 1 ATOM 501 C CA . VAL A 1 61 ? 18.835 49.739 -13.485 1.00 20.42 ? 61 VAL A CA 1 ATOM 502 C C . VAL A 1 61 ? 19.322 50.586 -14.651 1.00 22.33 ? 61 VAL A C 1 ATOM 503 O O . VAL A 1 61 ? 19.857 51.675 -14.459 1.00 23.33 ? 61 VAL A O 1 ATOM 504 C CB . VAL A 1 61 ? 19.722 48.482 -13.401 1.00 19.69 ? 61 VAL A CB 1 ATOM 505 C CG1 . VAL A 1 61 ? 21.187 48.885 -13.326 1.00 18.04 ? 61 VAL A CG1 1 ATOM 506 C CG2 . VAL A 1 61 ? 19.335 47.655 -12.192 1.00 18.36 ? 61 VAL A CG2 1 ATOM 507 N N . ASN A 1 62 ? 19.137 50.075 -15.861 1.00 21.93 ? 62 ASN A N 1 ATOM 508 C CA . ASN A 1 62 ? 19.560 50.776 -17.062 1.00 21.28 ? 62 ASN A CA 1 ATOM 509 C C . ASN A 1 62 ? 18.375 51.542 -17.632 1.00 22.17 ? 62 ASN A C 1 ATOM 510 O O . ASN A 1 62 ? 17.306 50.976 -17.855 1.00 22.18 ? 62 ASN A O 1 ATOM 511 C CB . ASN A 1 62 ? 20.115 49.757 -18.049 1.00 20.43 ? 62 ASN A CB 1 ATOM 512 C CG . ASN A 1 62 ? 21.232 48.933 -17.434 1.00 21.59 ? 62 ASN A CG 1 ATOM 513 O OD1 . ASN A 1 62 ? 22.329 49.441 -17.192 1.00 20.27 ? 62 ASN A OD1 1 ATOM 514 N ND2 . ASN A 1 62 ? 20.946 47.668 -17.140 1.00 19.59 ? 62 ASN A ND2 1 ATOM 515 N N . TRP A 1 63 ? 18.568 52.837 -17.862 1.00 22.33 ? 63 TRP A N 1 ATOM 516 C CA . TRP A 1 63 ? 17.485 53.672 -18.348 1.00 22.13 ? 63 TRP A CA 1 ATOM 517 C C . TRP A 1 63 ? 17.660 54.355 -19.690 1.00 23.92 ? 63 TRP A C 1 ATOM 518 O O . TRP A 1 63 ? 18.772 54.542 -20.186 1.00 24.69 ? 63 TRP A O 1 ATOM 519 C CB . TRP A 1 63 ? 17.160 54.742 -17.301 1.00 22.00 ? 63 TRP A CB 1 ATOM 520 C CG . TRP A 1 63 ? 16.759 54.176 -15.980 1.00 22.07 ? 63 TRP A CG 1 ATOM 521 C CD1 . TRP A 1 63 ? 17.586 53.735 -14.984 1.00 21.08 ? 63 TRP A CD1 1 ATOM 522 C CD2 . TRP A 1 63 ? 15.424 53.932 -15.533 1.00 21.83 ? 63 TRP A CD2 1 ATOM 523 N NE1 . TRP A 1 63 ? 16.845 53.226 -13.942 1.00 21.65 ? 63 TRP A NE1 1 ATOM 524 C CE2 . TRP A 1 63 ? 15.514 53.334 -14.253 1.00 22.13 ? 63 TRP A CE2 1 ATOM 525 C CE3 . TRP A 1 63 ? 14.157 54.157 -16.089 1.00 19.77 ? 63 TRP A CE3 1 ATOM 526 C CZ2 . TRP A 1 63 ? 14.386 52.958 -13.521 1.00 21.20 ? 63 TRP A CZ2 1 ATOM 527 C CZ3 . TRP A 1 63 ? 13.036 53.785 -15.363 1.00 21.36 ? 63 TRP A CZ3 1 ATOM 528 C CH2 . TRP A 1 63 ? 13.158 53.191 -14.090 1.00 22.59 ? 63 TRP A CH2 1 ATOM 529 N N . ILE A 1 64 ? 16.524 54.721 -20.273 1.00 24.47 ? 64 ILE A N 1 ATOM 530 C CA . ILE A 1 64 ? 16.495 55.441 -21.530 1.00 24.40 ? 64 ILE A CA 1 ATOM 531 C C . ILE A 1 64 ? 15.744 56.738 -21.239 1.00 25.47 ? 64 ILE A C 1 ATOM 532 O O . ILE A 1 64 ? 14.571 56.711 -20.840 1.00 25.35 ? 64 ILE A O 1 ATOM 533 C CB . ILE A 1 64 ? 15.747 54.663 -22.616 1.00 24.50 ? 64 ILE A CB 1 ATOM 534 C CG1 . ILE A 1 64 ? 16.459 53.338 -22.897 1.00 23.88 ? 64 ILE A CG1 1 ATOM 535 C CG2 . ILE A 1 64 ? 15.666 55.500 -23.884 1.00 22.29 ? 64 ILE A CG2 1 ATOM 536 C CD1 . ILE A 1 64 ? 15.763 52.484 -23.950 1.00 20.36 ? 64 ILE A CD1 1 ATOM 537 N N . HIS A 1 65 ? 16.431 57.867 -21.405 1.00 25.00 ? 65 HIS A N 1 ATOM 538 C CA . HIS A 1 65 ? 15.830 59.175 -21.159 1.00 24.87 ? 65 HIS A CA 1 ATOM 539 C C . HIS A 1 65 ? 14.968 59.574 -22.347 1.00 25.40 ? 65 HIS A C 1 ATOM 540 O O . HIS A 1 65 ? 15.414 59.532 -23.491 1.00 26.19 ? 65 HIS A O 1 ATOM 541 C CB . HIS A 1 65 ? 16.914 60.231 -20.935 1.00 23.91 ? 65 HIS A CB 1 ATOM 542 C CG . HIS A 1 65 ? 17.703 60.036 -19.677 1.00 25.69 ? 65 HIS A CG 1 ATOM 543 N ND1 . HIS A 1 65 ? 17.133 60.109 -18.423 1.00 25.92 ? 65 HIS A ND1 1 ATOM 544 C CD2 . HIS A 1 65 ? 19.021 59.794 -19.479 1.00 24.56 ? 65 HIS A CD2 1 ATOM 545 C CE1 . HIS A 1 65 ? 18.069 59.921 -17.506 1.00 26.11 ? 65 HIS A CE1 1 ATOM 546 N NE2 . HIS A 1 65 ? 19.222 59.729 -18.121 1.00 24.55 ? 65 HIS A NE2 1 ATOM 547 N N . LEU A 1 66 ? 13.727 59.954 -22.073 1.00 25.48 ? 66 LEU A N 1 ATOM 548 C CA . LEU A 1 66 ? 12.804 60.354 -23.126 1.00 25.44 ? 66 LEU A CA 1 ATOM 549 C C . LEU A 1 66 ? 12.499 61.832 -22.949 1.00 27.30 ? 66 LEU A C 1 ATOM 550 O O . LEU A 1 66 ? 13.112 62.502 -22.120 1.00 28.55 ? 66 LEU A O 1 ATOM 551 C CB . LEU A 1 66 ? 11.511 59.546 -23.018 1.00 23.36 ? 66 LEU A CB 1 ATOM 552 C CG . LEU A 1 66 ? 11.661 58.022 -22.984 1.00 22.45 ? 66 LEU A CG 1 ATOM 553 C CD1 . LEU A 1 66 ? 10.322 57.378 -22.674 1.00 20.87 ? 66 LEU A CD1 1 ATOM 554 C CD2 . LEU A 1 66 ? 12.192 57.528 -24.314 1.00 22.48 ? 66 LEU A CD2 1 ATOM 555 N N . ASP A 1 67 ? 11.564 62.346 -23.736 1.00 28.06 ? 67 ASP A N 1 ATOM 556 C CA . ASP A 1 67 ? 11.185 63.744 -23.603 1.00 28.64 ? 67 ASP A CA 1 ATOM 557 C C . ASP A 1 67 ? 10.183 63.819 -22.470 1.00 27.44 ? 67 ASP A C 1 ATOM 558 O O . ASP A 1 67 ? 9.521 62.835 -22.160 1.00 26.30 ? 67 ASP A O 1 ATOM 559 C CB . ASP A 1 67 ? 10.537 64.265 -24.886 1.00 31.40 ? 67 ASP A CB 1 ATOM 560 C CG . ASP A 1 67 ? 11.527 64.410 -26.019 1.00 33.43 ? 67 ASP A CG 1 ATOM 561 O OD1 . ASP A 1 67 ? 12.575 65.065 -25.813 1.00 32.91 ? 67 ASP A OD1 1 ATOM 562 O OD2 . ASP A 1 67 ? 11.252 63.874 -27.113 1.00 36.32 ? 67 ASP A OD2 1 ATOM 563 N N . PRO A 1 68 ? 10.072 64.984 -21.821 1.00 27.81 ? 68 PRO A N 1 ATOM 564 C CA . PRO A 1 68 ? 9.110 65.097 -20.726 1.00 27.78 ? 68 PRO A CA 1 ATOM 565 C C . PRO A 1 68 ? 7.716 64.668 -21.174 1.00 28.58 ? 68 PRO A C 1 ATOM 566 O O . PRO A 1 68 ? 7.291 64.959 -22.292 1.00 29.33 ? 68 PRO A O 1 ATOM 567 C CB . PRO A 1 68 ? 9.208 66.570 -20.317 1.00 27.50 ? 68 PRO A CB 1 ATOM 568 C CG . PRO A 1 68 ? 9.868 67.238 -21.492 1.00 29.66 ? 68 PRO A CG 1 ATOM 569 C CD . PRO A 1 68 ? 10.850 66.220 -21.970 1.00 27.13 ? 68 PRO A CD 1 ATOM 570 N N . ALA A 1 69 ? 7.024 63.954 -20.292 1.00 29.55 ? 69 ALA A N 1 ATOM 571 C CA . ALA A 1 69 ? 5.699 63.424 -20.581 1.00 29.47 ? 69 ALA A CA 1 ATOM 572 C C . ALA A 1 69 ? 4.555 64.379 -20.268 1.00 29.71 ? 69 ALA A C 1 ATOM 573 O O . ALA A 1 69 ? 3.631 64.534 -21.064 1.00 29.70 ? 69 ALA A O 1 ATOM 574 C CB . ALA A 1 69 ? 5.507 62.118 -19.819 1.00 29.34 ? 69 ALA A CB 1 ATOM 575 N N . ILE A 1 70 ? 4.616 65.008 -19.102 1.00 30.26 ? 70 ILE A N 1 ATOM 576 C CA . ILE A 1 70 ? 3.574 65.931 -18.681 1.00 29.14 ? 70 ILE A CA 1 ATOM 577 C C . ILE A 1 70 ? 4.149 67.324 -18.446 1.00 30.16 ? 70 ILE A C 1 ATOM 578 O O . ILE A 1 70 ? 5.058 67.508 -17.635 1.00 30.40 ? 70 ILE A O 1 ATOM 579 C CB . ILE A 1 70 ? 2.892 65.408 -17.407 1.00 27.84 ? 70 ILE A CB 1 ATOM 580 C CG1 . ILE A 1 70 ? 2.241 64.056 -17.714 1.00 25.41 ? 70 ILE A CG1 1 ATOM 581 C CG2 . ILE A 1 70 ? 1.866 66.409 -16.902 1.00 26.43 ? 70 ILE A CG2 1 ATOM 582 C CD1 . ILE A 1 70 ? 1.628 63.387 -16.519 1.00 26.05 ? 70 ILE A CD1 1 ATOM 583 N N . TYR A 1 71 ? 3.618 68.294 -19.181 1.00 29.23 ? 71 TYR A N 1 ATOM 584 C CA . TYR A 1 71 ? 4.062 69.678 -19.097 1.00 29.47 ? 71 TYR A CA 1 ATOM 585 C C . TYR A 1 71 ? 2.859 70.576 -19.353 1.00 30.83 ? 71 TYR A C 1 ATOM 586 O O . TYR A 1 71 ? 1.946 70.201 -20.085 1.00 30.19 ? 71 TYR A O 1 ATOM 587 C CB . TYR A 1 71 ? 5.151 69.930 -20.144 1.00 29.46 ? 71 TYR A CB 1 ATOM 588 C CG . TYR A 1 71 ? 4.821 69.367 -21.513 1.00 30.82 ? 71 TYR A CG 1 ATOM 589 C CD1 . TYR A 1 71 ? 3.991 70.061 -22.401 1.00 30.24 ? 71 TYR A CD1 1 ATOM 590 C CD2 . TYR A 1 71 ? 5.286 68.102 -21.896 1.00 30.59 ? 71 TYR A CD2 1 ATOM 591 C CE1 . TYR A 1 71 ? 3.625 69.503 -23.636 1.00 30.36 ? 71 TYR A CE1 1 ATOM 592 C CE2 . TYR A 1 71 ? 4.927 67.537 -23.124 1.00 30.50 ? 71 TYR A CE2 1 ATOM 593 C CZ . TYR A 1 71 ? 4.095 68.240 -23.988 1.00 31.99 ? 71 TYR A CZ 1 ATOM 594 O OH . TYR A 1 71 ? 3.715 67.667 -25.186 1.00 32.25 ? 71 TYR A OH 1 ATOM 595 N N . PRO A 1 72 ? 2.836 71.775 -18.750 1.00 31.92 ? 72 PRO A N 1 ATOM 596 C CA . PRO A 1 72 ? 1.707 72.694 -18.944 1.00 31.33 ? 72 PRO A CA 1 ATOM 597 C C . PRO A 1 72 ? 1.211 72.833 -20.387 1.00 31.81 ? 72 PRO A C 1 ATOM 598 O O . PRO A 1 72 ? 1.976 73.195 -21.285 1.00 32.13 ? 72 PRO A O 1 ATOM 599 C CB . PRO A 1 72 ? 2.227 74.018 -18.366 1.00 30.00 ? 72 PRO A CB 1 ATOM 600 C CG . PRO A 1 72 ? 3.717 73.870 -18.397 1.00 30.82 ? 72 PRO A CG 1 ATOM 601 C CD . PRO A 1 72 ? 3.924 72.436 -18.012 1.00 30.23 ? 72 PRO A CD 1 ATOM 602 N N . THR A 1 73 ? -0.072 72.526 -20.595 1.00 30.96 ? 73 THR A N 1 ATOM 603 C CA . THR A 1 73 ? -0.707 72.638 -21.909 1.00 28.96 ? 73 THR A CA 1 ATOM 604 C C . THR A 1 73 ? -2.121 73.193 -21.776 1.00 30.05 ? 73 THR A C 1 ATOM 605 O O . THR A 1 73 ? -2.724 73.603 -22.766 1.00 30.35 ? 73 THR A O 1 ATOM 606 C CB . THR A 1 73 ? -0.820 71.286 -22.644 1.00 27.15 ? 73 THR A CB 1 ATOM 607 O OG1 . THR A 1 73 ? -1.582 70.373 -21.847 1.00 26.53 ? 73 THR A OG1 1 ATOM 608 C CG2 . THR A 1 73 ? 0.546 70.712 -22.935 1.00 24.34 ? 73 THR A CG2 1 ATOM 609 N N . GLN A 1 74 ? -2.663 73.187 -20.561 1.00 30.03 ? 74 GLN A N 1 ATOM 610 C CA . GLN A 1 74 ? -4.003 73.718 -20.345 1.00 30.88 ? 74 GLN A CA 1 ATOM 611 C C . GLN A 1 74 ? -4.069 74.621 -19.116 1.00 31.43 ? 74 GLN A C 1 ATOM 612 O O . GLN A 1 74 ? -3.147 74.660 -18.308 1.00 32.12 ? 74 GLN A O 1 ATOM 613 C CB . GLN A 1 74 ? -5.034 72.581 -20.255 1.00 31.06 ? 74 GLN A CB 1 ATOM 614 C CG . GLN A 1 74 ? -4.722 71.509 -19.243 1.00 34.83 ? 74 GLN A CG 1 ATOM 615 C CD . GLN A 1 74 ? -5.690 70.332 -19.294 1.00 36.19 ? 74 GLN A CD 1 ATOM 616 O OE1 . GLN A 1 74 ? -5.580 69.402 -18.501 1.00 41.92 ? 74 GLN A OE1 1 ATOM 617 N NE2 . GLN A 1 74 ? -6.637 70.368 -20.223 1.00 34.63 ? 74 GLN A NE2 1 ATOM 618 N N . GLU A 1 75 ? -5.157 75.370 -18.992 1.00 30.98 ? 75 GLU A N 1 ATOM 619 C CA . GLU A 1 75 ? -5.316 76.284 -17.875 1.00 31.50 ? 75 GLU A CA 1 ATOM 620 C C . GLU A 1 75 ? -5.144 75.584 -16.534 1.00 31.08 ? 75 GLU A C 1 ATOM 621 O O . GLU A 1 75 ? -4.575 76.152 -15.604 1.00 29.97 ? 75 GLU A O 1 ATOM 622 C CB . GLU A 1 75 ? -6.695 76.948 -17.951 1.00 32.76 ? 75 GLU A CB 1 ATOM 623 C CG . GLU A 1 75 ? -6.960 78.040 -16.908 1.00 34.94 ? 75 GLU A CG 1 ATOM 624 C CD . GLU A 1 75 ? -7.278 77.491 -15.522 1.00 36.76 ? 75 GLU A CD 1 ATOM 625 O OE1 . GLU A 1 75 ? -7.960 76.442 -15.438 1.00 37.95 ? 75 GLU A OE1 1 ATOM 626 O OE2 . GLU A 1 75 ? -6.863 78.119 -14.519 1.00 35.14 ? 75 GLU A OE2 1 ATOM 627 N N . ALA A 1 76 ? -5.627 74.347 -16.446 1.00 31.58 ? 76 ALA A N 1 ATOM 628 C CA . ALA A 1 76 ? -5.556 73.572 -15.210 1.00 31.57 ? 76 ALA A CA 1 ATOM 629 C C . ALA A 1 76 ? -4.139 73.242 -14.736 1.00 32.00 ? 76 ALA A C 1 ATOM 630 O O . ALA A 1 76 ? -3.958 72.722 -13.632 1.00 32.12 ? 76 ALA A O 1 ATOM 631 C CB . ALA A 1 76 ? -6.367 72.290 -15.357 1.00 32.15 ? 76 ALA A CB 1 ATOM 632 N N . ASP A 1 77 ? -3.135 73.542 -15.556 1.00 30.32 ? 77 ASP A N 1 ATOM 633 C CA . ASP A 1 77 ? -1.756 73.278 -15.170 1.00 30.01 ? 77 ASP A CA 1 ATOM 634 C C . ASP A 1 77 ? -0.794 74.177 -15.931 1.00 29.77 ? 77 ASP A C 1 ATOM 635 O O . ASP A 1 77 ? 0.358 73.819 -16.166 1.00 28.36 ? 77 ASP A O 1 ATOM 636 C CB . ASP A 1 77 ? -1.413 71.795 -15.396 1.00 31.51 ? 77 ASP A CB 1 ATOM 637 C CG . ASP A 1 77 ? -1.238 71.429 -16.867 1.00 32.80 ? 77 ASP A CG 1 ATOM 638 O OD1 . ASP A 1 77 ? -1.613 72.221 -17.756 1.00 33.36 ? 77 ASP A OD1 1 ATOM 639 O OD2 . ASP A 1 77 ? -0.722 70.321 -17.130 1.00 32.57 ? 77 ASP A OD2 1 ATOM 640 N N . SER A 1 78 ? -1.278 75.364 -16.285 1.00 30.45 ? 78 SER A N 1 ATOM 641 C CA . SER A 1 78 ? -0.501 76.343 -17.043 1.00 30.49 ? 78 SER A CA 1 ATOM 642 C C . SER A 1 78 ? 0.770 76.857 -16.375 1.00 30.70 ? 78 SER A C 1 ATOM 643 O O . SER A 1 78 ? 1.728 77.228 -17.058 1.00 30.07 ? 78 SER A O 1 ATOM 644 C CB . SER A 1 78 ? -1.393 77.532 -17.408 1.00 31.49 ? 78 SER A CB 1 ATOM 645 O OG . SER A 1 78 ? -2.046 78.053 -16.263 1.00 33.24 ? 78 SER A OG 1 ATOM 646 N N . LYS A 1 79 ? 0.793 76.877 -15.047 1.00 30.82 ? 79 LYS A N 1 ATOM 647 C CA . LYS A 1 79 ? 1.966 77.374 -14.340 1.00 31.31 ? 79 LYS A CA 1 ATOM 648 C C . LYS A 1 79 ? 2.998 76.326 -13.943 1.00 30.28 ? 79 LYS A C 1 ATOM 649 O O . LYS A 1 79 ? 4.140 76.668 -13.642 1.00 29.68 ? 79 LYS A O 1 ATOM 650 C CB . LYS A 1 79 ? 1.532 78.168 -13.112 1.00 33.60 ? 79 LYS A CB 1 ATOM 651 C CG . LYS A 1 79 ? 0.947 79.506 -13.480 1.00 37.07 ? 79 LYS A CG 1 ATOM 652 C CD . LYS A 1 79 ? 0.558 80.304 -12.262 1.00 41.48 ? 79 LYS A CD 1 ATOM 653 C CE . LYS A 1 79 ? 0.351 81.759 -12.639 1.00 43.79 ? 79 LYS A CE 1 ATOM 654 N NZ . LYS A 1 79 ? 1.612 82.332 -13.205 1.00 45.95 ? 79 LYS A NZ 1 ATOM 655 N N . SER A 1 80 ? 2.602 75.056 -13.951 1.00 29.47 ? 80 SER A N 1 ATOM 656 C CA . SER A 1 80 ? 3.499 73.951 -13.597 1.00 28.29 ? 80 SER A CA 1 ATOM 657 C C . SER A 1 80 ? 2.753 72.642 -13.425 1.00 27.17 ? 80 SER A C 1 ATOM 658 O O . SER A 1 80 ? 1.547 72.622 -13.168 1.00 26.92 ? 80 SER A O 1 ATOM 659 C CB . SER A 1 80 ? 4.258 74.235 -12.289 1.00 27.82 ? 80 SER A CB 1 ATOM 660 O OG . SER A 1 80 ? 5.520 74.836 -12.525 1.00 27.03 ? 80 SER A OG 1 ATOM 661 N N . CYS A 1 81 ? 3.489 71.548 -13.562 1.00 26.60 ? 81 CYS A N 1 ATOM 662 C CA . CYS A 1 81 ? 2.926 70.219 -13.390 1.00 26.27 ? 81 CYS A CA 1 ATOM 663 C C . CYS A 1 81 ? 3.678 69.571 -12.231 1.00 26.08 ? 81 CYS A C 1 ATOM 664 O O . CYS A 1 81 ? 4.772 69.035 -12.410 1.00 24.10 ? 81 CYS A O 1 ATOM 665 C CB . CYS A 1 81 ? 3.105 69.393 -14.665 1.00 25.81 ? 81 CYS A CB 1 ATOM 666 S SG . CYS A 1 81 ? 2.204 70.037 -16.088 1.00 27.08 ? 81 CYS A SG 1 ATOM 667 N N . TRP A 1 82 ? 3.097 69.634 -11.038 1.00 25.55 ? 82 TRP A N 1 ATOM 668 C CA . TRP A 1 82 ? 3.745 69.054 -9.877 1.00 26.03 ? 82 TRP A CA 1 ATOM 669 C C . TRP A 1 82 ? 3.447 67.573 -9.660 1.00 25.56 ? 82 TRP A C 1 ATOM 670 O O . TRP A 1 82 ? 2.785 66.938 -10.476 1.00 24.89 ? 82 TRP A O 1 ATOM 671 C CB . TRP A 1 82 ? 3.432 69.892 -8.637 1.00 25.76 ? 82 TRP A CB 1 ATOM 672 C CG . TRP A 1 82 ? 4.027 71.280 -8.761 1.00 27.84 ? 82 TRP A CG 1 ATOM 673 C CD1 . TRP A 1 82 ? 5.228 71.606 -9.335 1.00 27.11 ? 82 TRP A CD1 1 ATOM 674 C CD2 . TRP A 1 82 ? 3.457 72.516 -8.306 1.00 27.65 ? 82 TRP A CD2 1 ATOM 675 N NE1 . TRP A 1 82 ? 5.436 72.961 -9.267 1.00 26.57 ? 82 TRP A NE1 1 ATOM 676 C CE2 . TRP A 1 82 ? 4.366 73.546 -8.640 1.00 27.74 ? 82 TRP A CE2 1 ATOM 677 C CE3 . TRP A 1 82 ? 2.264 72.855 -7.649 1.00 29.07 ? 82 TRP A CE3 1 ATOM 678 C CZ2 . TRP A 1 82 ? 4.120 74.898 -8.339 1.00 28.78 ? 82 TRP A CZ2 1 ATOM 679 C CZ3 . TRP A 1 82 ? 2.019 74.199 -7.348 1.00 29.17 ? 82 TRP A CZ3 1 ATOM 680 C CH2 . TRP A 1 82 ? 2.946 75.202 -7.694 1.00 27.75 ? 82 TRP A CH2 1 ATOM 681 N N . SER A 1 83 ? 3.958 67.031 -8.563 1.00 26.07 ? 83 SER A N 1 ATOM 682 C CA . SER A 1 83 ? 3.831 65.614 -8.249 1.00 26.69 ? 83 SER A CA 1 ATOM 683 C C . SER A 1 83 ? 2.481 64.917 -8.385 1.00 27.08 ? 83 SER A C 1 ATOM 684 O O . SER A 1 83 ? 1.417 65.509 -8.177 1.00 27.46 ? 83 SER A O 1 ATOM 685 C CB . SER A 1 83 ? 4.409 65.357 -6.861 1.00 26.15 ? 83 SER A CB 1 ATOM 686 O OG . SER A 1 83 ? 5.790 65.665 -6.859 1.00 27.52 ? 83 SER A OG 1 ATOM 687 N N . GLY A 1 84 ? 2.559 63.635 -8.742 1.00 26.21 ? 84 GLY A N 1 ATOM 688 C CA . GLY A 1 84 ? 1.380 62.810 -8.921 1.00 26.10 ? 84 GLY A CA 1 ATOM 689 C C . GLY A 1 84 ? 1.720 61.326 -8.973 1.00 25.51 ? 84 GLY A C 1 ATOM 690 O O . GLY A 1 84 ? 2.883 60.936 -8.861 1.00 24.09 ? 84 GLY A O 1 ATOM 691 N N . SER A 1 85 ? 0.699 60.497 -9.168 1.00 24.66 ? 85 SER A N 1 ATOM 692 C CA . SER A 1 85 ? 0.880 59.055 -9.198 1.00 22.42 ? 85 SER A CA 1 ATOM 693 C C . SER A 1 85 ? 0.180 58.378 -10.370 1.00 23.70 ? 85 SER A C 1 ATOM 694 O O . SER A 1 85 ? -0.716 58.946 -11.001 1.00 24.03 ? 85 SER A O 1 ATOM 695 C CB . SER A 1 85 ? 0.363 58.456 -7.890 1.00 21.08 ? 85 SER A CB 1 ATOM 696 O OG . SER A 1 85 ? 0.860 59.182 -6.780 1.00 19.74 ? 85 SER A OG 1 ATOM 697 N N . ALA A 1 86 ? 0.591 57.144 -10.647 1.00 22.72 ? 86 ALA A N 1 ATOM 698 C CA . ALA A 1 86 ? 0.021 56.373 -11.738 1.00 21.36 ? 86 ALA A CA 1 ATOM 699 C C . ALA A 1 86 ? -0.846 55.241 -11.216 1.00 22.07 ? 86 ALA A C 1 ATOM 700 O O . ALA A 1 86 ? -0.515 54.600 -10.219 1.00 22.17 ? 86 ALA A O 1 ATOM 701 C CB . ALA A 1 86 ? 1.135 55.807 -12.600 1.00 21.21 ? 86 ALA A CB 1 ATOM 702 N N . THR A 1 87 ? -1.964 55.008 -11.892 1.00 23.20 ? 87 THR A N 1 ATOM 703 C CA . THR A 1 87 ? -2.878 53.926 -11.539 1.00 23.76 ? 87 THR A CA 1 ATOM 704 C C . THR A 1 87 ? -3.293 53.254 -12.843 1.00 24.55 ? 87 THR A C 1 ATOM 705 O O . THR A 1 87 ? -3.826 53.910 -13.740 1.00 23.89 ? 87 THR A O 1 ATOM 706 C CB . THR A 1 87 ? -4.161 54.440 -10.847 1.00 24.68 ? 87 THR A CB 1 ATOM 707 O OG1 . THR A 1 87 ? -3.817 55.182 -9.669 1.00 25.75 ? 87 THR A OG1 1 ATOM 708 C CG2 . THR A 1 87 ? -5.061 53.265 -10.458 1.00 22.08 ? 87 THR A CG2 1 ATOM 709 N N . ILE A 1 88 ? -3.040 51.956 -12.962 1.00 24.28 ? 88 ILE A N 1 ATOM 710 C CA . ILE A 1 88 ? -3.425 51.250 -14.173 1.00 25.13 ? 88 ILE A CA 1 ATOM 711 C C . ILE A 1 88 ? -4.825 50.691 -13.972 1.00 25.98 ? 88 ILE A C 1 ATOM 712 O O . ILE A 1 88 ? -5.035 49.782 -13.166 1.00 26.89 ? 88 ILE A O 1 ATOM 713 C CB . ILE A 1 88 ? -2.447 50.122 -14.488 1.00 24.38 ? 88 ILE A CB 1 ATOM 714 C CG1 . ILE A 1 88 ? -1.042 50.710 -14.642 1.00 24.19 ? 88 ILE A CG1 1 ATOM 715 C CG2 . ILE A 1 88 ? -2.876 49.407 -15.769 1.00 22.96 ? 88 ILE A CG2 1 ATOM 716 C CD1 . ILE A 1 88 ? 0.045 49.689 -14.873 1.00 24.38 ? 88 ILE A CD1 1 ATOM 717 N N . LEU A 1 89 ? -5.778 51.250 -14.708 1.00 25.70 ? 89 LEU A N 1 ATOM 718 C CA . LEU A 1 89 ? -7.174 50.848 -14.596 1.00 27.15 ? 89 LEU A CA 1 ATOM 719 C C . LEU A 1 89 ? -7.521 49.619 -15.415 1.00 27.94 ? 89 LEU A C 1 ATOM 720 O O . LEU A 1 89 ? -6.853 49.308 -16.402 1.00 27.18 ? 89 LEU A O 1 ATOM 721 C CB . LEU A 1 89 ? -8.090 51.989 -15.052 1.00 26.15 ? 89 LEU A CB 1 ATOM 722 C CG . LEU A 1 89 ? -7.773 53.409 -14.588 1.00 26.69 ? 89 LEU A CG 1 ATOM 723 C CD1 . LEU A 1 89 ? -8.826 54.354 -15.146 1.00 27.78 ? 89 LEU A CD1 1 ATOM 724 C CD2 . LEU A 1 89 ? -7.738 53.473 -13.075 1.00 25.39 ? 89 LEU A CD2 1 ATOM 725 N N . PRO A 1 90 ? -8.583 48.899 -15.007 1.00 28.91 ? 90 PRO A N 1 ATOM 726 C CA . PRO A 1 90 ? -9.026 47.700 -15.727 1.00 27.90 ? 90 PRO A CA 1 ATOM 727 C C . PRO A 1 90 ? -9.145 48.089 -17.197 1.00 27.70 ? 90 PRO A C 1 ATOM 728 O O . PRO A 1 90 ? -9.537 49.212 -17.512 1.00 25.82 ? 90 PRO A O 1 ATOM 729 C CB . PRO A 1 90 ? -10.380 47.404 -15.095 1.00 27.42 ? 90 PRO A CB 1 ATOM 730 C CG . PRO A 1 90 ? -10.161 47.816 -13.667 1.00 28.17 ? 90 PRO A CG 1 ATOM 731 C CD . PRO A 1 90 ? -9.406 49.127 -13.803 1.00 28.40 ? 90 PRO A CD 1 ATOM 732 N N . GLY A 1 91 ? -8.811 47.171 -18.093 1.00 28.21 ? 91 GLY A N 1 ATOM 733 C CA . GLY A 1 91 ? -8.864 47.507 -19.501 1.00 30.08 ? 91 GLY A CA 1 ATOM 734 C C . GLY A 1 91 ? -7.451 47.860 -19.927 1.00 30.28 ? 91 GLY A C 1 ATOM 735 O O . GLY A 1 91 ? -7.188 48.175 -21.087 1.00 30.94 ? 91 GLY A O 1 ATOM 736 N N . ASN A 1 92 ? -6.542 47.819 -18.956 1.00 29.96 ? 92 ASN A N 1 ATOM 737 C CA . ASN A 1 92 ? -5.128 48.083 -19.171 1.00 28.30 ? 92 ASN A CA 1 ATOM 738 C C . ASN A 1 92 ? -4.793 49.499 -19.653 1.00 28.30 ? 92 ASN A C 1 ATOM 739 O O . ASN A 1 92 ? -4.067 49.687 -20.635 1.00 28.30 ? 92 ASN A O 1 ATOM 740 C CB . ASN A 1 92 ? -4.584 47.039 -20.142 1.00 28.56 ? 92 ASN A CB 1 ATOM 741 C CG . ASN A 1 92 ? -3.134 46.741 -19.907 1.00 29.87 ? 92 ASN A CG 1 ATOM 742 O OD1 . ASN A 1 92 ? -2.667 46.755 -18.766 1.00 32.74 ? 92 ASN A OD1 1 ATOM 743 N ND2 . ASN A 1 92 ? -2.406 46.448 -20.977 1.00 31.42 ? 92 ASN A ND2 1 ATOM 744 N N . ILE A 1 93 ? -5.306 50.493 -18.939 1.00 26.32 ? 93 ILE A N 1 ATOM 745 C CA . ILE A 1 93 ? -5.072 51.886 -19.284 1.00 25.72 ? 93 ILE A CA 1 ATOM 746 C C . ILE A 1 93 ? -4.426 52.638 -18.112 1.00 25.48 ? 93 ILE A C 1 ATOM 747 O O . ILE A 1 93 ? -5.048 52.837 -17.068 1.00 25.00 ? 93 ILE A O 1 ATOM 748 C CB . ILE A 1 93 ? -6.409 52.572 -19.682 1.00 26.30 ? 93 ILE A CB 1 ATOM 749 C CG1 . ILE A 1 93 ? -6.212 54.075 -19.850 1.00 27.33 ? 93 ILE A CG1 1 ATOM 750 C CG2 . ILE A 1 93 ? -7.466 52.297 -18.641 1.00 27.33 ? 93 ILE A CG2 1 ATOM 751 C CD1 . ILE A 1 93 ? -5.383 54.445 -21.057 1.00 29.50 ? 93 ILE A CD1 1 ATOM 752 N N . PRO A 1 94 ? -3.154 53.041 -18.260 1.00 24.63 ? 94 PRO A N 1 ATOM 753 C CA . PRO A 1 94 ? -2.511 53.765 -17.159 1.00 22.87 ? 94 PRO A CA 1 ATOM 754 C C . PRO A 1 94 ? -3.057 55.185 -17.035 1.00 22.98 ? 94 PRO A C 1 ATOM 755 O O . PRO A 1 94 ? -2.981 55.971 -17.975 1.00 24.33 ? 94 PRO A O 1 ATOM 756 C CB . PRO A 1 94 ? -1.026 53.721 -17.532 1.00 21.49 ? 94 PRO A CB 1 ATOM 757 C CG . PRO A 1 94 ? -1.046 53.664 -19.019 1.00 22.45 ? 94 PRO A CG 1 ATOM 758 C CD . PRO A 1 94 ? -2.186 52.721 -19.325 1.00 22.68 ? 94 PRO A CD 1 ATOM 759 N N . ALA A 1 95 ? -3.624 55.494 -15.870 1.00 24.24 ? 95 ALA A N 1 ATOM 760 C CA . ALA A 1 95 ? -4.196 56.812 -15.590 1.00 23.16 ? 95 ALA A CA 1 ATOM 761 C C . ALA A 1 95 ? -3.277 57.576 -14.639 1.00 23.87 ? 95 ALA A C 1 ATOM 762 O O . ALA A 1 95 ? -2.884 57.060 -13.590 1.00 25.21 ? 95 ALA A O 1 ATOM 763 C CB . ALA A 1 95 ? -5.577 56.656 -14.969 1.00 22.33 ? 95 ALA A CB 1 ATOM 764 N N . MET A 1 96 ? -2.943 58.808 -15.005 1.00 23.34 ? 96 MET A N 1 ATOM 765 C CA . MET A 1 96 ? -2.050 59.626 -14.194 1.00 23.70 ? 96 MET A CA 1 ATOM 766 C C . MET A 1 96 ? -2.778 60.806 -13.550 1.00 24.35 ? 96 MET A C 1 ATOM 767 O O . MET A 1 96 ? -3.415 61.612 -14.236 1.00 24.43 ? 96 MET A O 1 ATOM 768 C CB . MET A 1 96 ? -0.909 60.145 -15.072 1.00 24.44 ? 96 MET A CB 1 ATOM 769 C CG . MET A 1 96 ? 0.344 60.559 -14.330 1.00 27.79 ? 96 MET A CG 1 ATOM 770 S SD . MET A 1 96 ? 1.299 59.148 -13.698 1.00 27.84 ? 96 MET A SD 1 ATOM 771 C CE . MET A 1 96 ? 2.021 58.488 -15.197 1.00 27.01 ? 96 MET A CE 1 ATOM 772 N N . LEU A 1 97 ? -2.706 60.887 -12.226 1.00 24.23 ? 97 LEU A N 1 ATOM 773 C CA . LEU A 1 97 ? -3.316 61.984 -11.484 1.00 23.38 ? 97 LEU A CA 1 ATOM 774 C C . LEU A 1 97 ? -2.160 62.810 -10.943 1.00 24.25 ? 97 LEU A C 1 ATOM 775 O O . LEU A 1 97 ? -1.256 62.272 -10.307 1.00 23.95 ? 97 LEU A O 1 ATOM 776 C CB . LEU A 1 97 ? -4.159 61.460 -10.325 1.00 21.59 ? 97 LEU A CB 1 ATOM 777 C CG . LEU A 1 97 ? -5.435 60.729 -10.722 1.00 23.47 ? 97 LEU A CG 1 ATOM 778 C CD1 . LEU A 1 97 ? -6.174 60.248 -9.481 1.00 21.55 ? 97 LEU A CD1 1 ATOM 779 C CD2 . LEU A 1 97 ? -6.303 61.679 -11.531 1.00 23.15 ? 97 LEU A CD2 1 ATOM 780 N N . TYR A 1 98 ? -2.176 64.110 -11.203 1.00 24.70 ? 98 TYR A N 1 ATOM 781 C CA . TYR A 1 98 ? -1.101 64.970 -10.736 1.00 24.44 ? 98 TYR A CA 1 ATOM 782 C C . TYR A 1 98 ? -1.640 66.326 -10.338 1.00 24.80 ? 98 TYR A C 1 ATOM 783 O O . TYR A 1 98 ? -2.752 66.706 -10.712 1.00 23.50 ? 98 TYR A O 1 ATOM 784 C CB . TYR A 1 98 ? -0.053 65.147 -11.833 1.00 24.63 ? 98 TYR A CB 1 ATOM 785 C CG . TYR A 1 98 ? -0.567 65.887 -13.049 1.00 26.75 ? 98 TYR A CG 1 ATOM 786 C CD1 . TYR A 1 98 ? -0.336 67.256 -13.210 1.00 27.14 ? 98 TYR A CD1 1 ATOM 787 C CD2 . TYR A 1 98 ? -1.291 65.221 -14.038 1.00 28.05 ? 98 TYR A CD2 1 ATOM 788 C CE1 . TYR A 1 98 ? -0.809 67.946 -14.325 1.00 28.31 ? 98 TYR A CE1 1 ATOM 789 C CE2 . TYR A 1 98 ? -1.772 65.897 -15.160 1.00 31.27 ? 98 TYR A CE2 1 ATOM 790 C CZ . TYR A 1 98 ? -1.526 67.261 -15.298 1.00 31.89 ? 98 TYR A CZ 1 ATOM 791 O OH . TYR A 1 98 ? -1.995 67.930 -16.410 1.00 33.37 ? 98 TYR A OH 1 ATOM 792 N N . THR A 1 99 ? -0.838 67.053 -9.576 1.00 24.93 ? 99 THR A N 1 ATOM 793 C CA . THR A 1 99 ? -1.225 68.374 -9.127 1.00 25.64 ? 99 THR A CA 1 ATOM 794 C C . THR A 1 99 ? -0.710 69.413 -10.101 1.00 26.63 ? 99 THR A C 1 ATOM 795 O O . THR A 1 99 ? 0.485 69.476 -10.386 1.00 26.18 ? 99 THR A O 1 ATOM 796 C CB . THR A 1 99 ? -0.646 68.694 -7.743 1.00 25.57 ? 99 THR A CB 1 ATOM 797 O OG1 . THR A 1 99 ? -1.190 67.792 -6.774 1.00 25.91 ? 99 THR A OG1 1 ATOM 798 C CG2 . THR A 1 99 ? -0.976 70.124 -7.354 1.00 24.72 ? 99 THR A CG2 1 ATOM 799 N N . GLY A 1 100 ? -1.617 70.225 -10.620 1.00 28.41 ? 100 GLY A N 1 ATOM 800 C CA . GLY A 1 100 ? -1.203 71.265 -11.537 1.00 29.75 ? 100 GLY A CA 1 ATOM 801 C C . GLY A 1 100 ? -1.336 72.603 -10.843 1.00 31.03 ? 100 GLY A C 1 ATOM 802 O O . GLY A 1 100 ? -2.065 72.728 -9.852 1.00 30.73 ? 100 GLY A O 1 ATOM 803 N N . SER A 1 101 ? -0.609 73.595 -11.340 1.00 31.31 ? 101 SER A N 1 ATOM 804 C CA . SER A 1 101 ? -0.682 74.946 -10.794 1.00 32.79 ? 101 SER A CA 1 ATOM 805 C C . SER A 1 101 ? -1.408 75.718 -11.900 1.00 33.97 ? 101 SER A C 1 ATOM 806 O O . SER A 1 101 ? -0.819 75.988 -12.951 1.00 34.17 ? 101 SER A O 1 ATOM 807 C CB . SER A 1 101 ? 0.729 75.499 -10.583 1.00 32.18 ? 101 SER A CB 1 ATOM 808 O OG . SER A 1 101 ? 0.705 76.739 -9.899 1.00 34.59 ? 101 SER A OG 1 ATOM 809 N N . ASP A 1 102 ? -2.682 76.049 -11.691 1.00 34.84 ? 102 ASP A N 1 ATOM 810 C CA . ASP A 1 102 ? -3.431 76.754 -12.734 1.00 37.93 ? 102 ASP A CA 1 ATOM 811 C C . ASP A 1 102 ? -3.083 78.232 -12.887 1.00 38.56 ? 102 ASP A C 1 ATOM 812 O O . ASP A 1 102 ? -2.222 78.753 -12.178 1.00 40.53 ? 102 ASP A O 1 ATOM 813 C CB . ASP A 1 102 ? -4.951 76.593 -12.542 1.00 37.76 ? 102 ASP A CB 1 ATOM 814 C CG . ASP A 1 102 ? -5.470 77.256 -11.279 1.00 38.24 ? 102 ASP A CG 1 ATOM 815 O OD1 . ASP A 1 102 ? -4.873 78.254 -10.819 1.00 36.76 ? 102 ASP A OD1 1 ATOM 816 O OD2 . ASP A 1 102 ? -6.503 76.780 -10.760 1.00 37.99 ? 102 ASP A OD2 1 ATOM 817 N N . SER A 1 103 ? -3.750 78.893 -13.827 1.00 38.99 ? 103 SER A N 1 ATOM 818 C CA . SER A 1 103 ? -3.517 80.305 -14.108 1.00 40.41 ? 103 SER A CA 1 ATOM 819 C C . SER A 1 103 ? -3.686 81.214 -12.889 1.00 41.75 ? 103 SER A C 1 ATOM 820 O O . SER A 1 103 ? -3.067 82.274 -12.812 1.00 41.98 ? 103 SER A O 1 ATOM 821 C CB . SER A 1 103 ? -4.448 80.757 -15.224 1.00 39.52 ? 103 SER A CB 1 ATOM 822 O OG . SER A 1 103 ? -5.776 80.362 -14.939 1.00 40.99 ? 103 SER A OG 1 ATOM 823 N N . LYS A 1 104 ? -4.525 80.802 -11.942 1.00 43.05 ? 104 LYS A N 1 ATOM 824 C CA . LYS A 1 104 ? -4.740 81.584 -10.727 1.00 44.14 ? 104 LYS A CA 1 ATOM 825 C C . LYS A 1 104 ? -3.783 81.119 -9.637 1.00 43.76 ? 104 LYS A C 1 ATOM 826 O O . LYS A 1 104 ? -3.967 81.420 -8.456 1.00 43.58 ? 104 LYS A O 1 ATOM 827 C CB . LYS A 1 104 ? -6.183 81.434 -10.239 1.00 46.69 ? 104 LYS A CB 1 ATOM 828 C CG . LYS A 1 104 ? -7.214 82.092 -11.136 1.00 52.17 ? 104 LYS A CG 1 ATOM 829 C CD . LYS A 1 104 ? -8.601 82.040 -10.505 1.00 57.56 ? 104 LYS A CD 1 ATOM 830 C CE . LYS A 1 104 ? -9.645 82.712 -11.397 1.00 60.19 ? 104 LYS A CE 1 ATOM 831 N NZ . LYS A 1 104 ? -11.015 82.668 -10.798 1.00 62.03 ? 104 LYS A NZ 1 ATOM 832 N N . SER A 1 105 ? -2.764 80.371 -10.044 1.00 42.49 ? 105 SER A N 1 ATOM 833 C CA . SER A 1 105 ? -1.762 79.854 -9.122 1.00 41.61 ? 105 SER A CA 1 ATOM 834 C C . SER A 1 105 ? -2.278 78.950 -8.010 1.00 39.33 ? 105 SER A C 1 ATOM 835 O O . SER A 1 105 ? -1.685 78.904 -6.939 1.00 40.06 ? 105 SER A O 1 ATOM 836 C CB . SER A 1 105 ? -0.971 81.008 -8.495 1.00 42.03 ? 105 SER A CB 1 ATOM 837 O OG . SER A 1 105 ? 0.151 81.360 -9.288 1.00 44.55 ? 105 SER A OG 1 ATOM 838 N N . ARG A 1 106 ? -3.374 78.235 -8.228 1.00 36.95 ? 106 ARG A N 1 ATOM 839 C CA . ARG A 1 106 ? -3.841 77.343 -7.175 1.00 36.85 ? 106 ARG A CA 1 ATOM 840 C C . ARG A 1 106 ? -3.603 75.877 -7.541 1.00 35.22 ? 106 ARG A C 1 ATOM 841 O O . ARG A 1 106 ? -3.659 75.490 -8.708 1.00 35.69 ? 106 ARG A O 1 ATOM 842 C CB . ARG A 1 106 ? -5.313 77.586 -6.856 1.00 37.32 ? 106 ARG A CB 1 ATOM 843 C CG . ARG A 1 106 ? -6.194 77.576 -8.045 1.00 41.69 ? 106 ARG A CG 1 ATOM 844 C CD . ARG A 1 106 ? -7.642 77.476 -7.642 1.00 44.07 ? 106 ARG A CD 1 ATOM 845 N NE . ARG A 1 106 ? -8.445 77.123 -8.806 1.00 48.91 ? 106 ARG A NE 1 ATOM 846 C CZ . ARG A 1 106 ? -9.678 76.640 -8.741 1.00 50.22 ? 106 ARG A CZ 1 ATOM 847 N NH1 . ARG A 1 106 ? -10.251 76.457 -7.557 1.00 51.64 ? 106 ARG A NH1 1 ATOM 848 N NH2 . ARG A 1 106 ? -10.326 76.327 -9.857 1.00 49.83 ? 106 ARG A NH2 1 ATOM 849 N N . GLN A 1 107 ? -3.310 75.071 -6.527 1.00 32.47 ? 107 GLN A N 1 ATOM 850 C CA . GLN A 1 107 ? -3.034 73.656 -6.710 1.00 29.71 ? 107 GLN A CA 1 ATOM 851 C C . GLN A 1 107 ? -4.319 72.872 -6.932 1.00 28.92 ? 107 GLN A C 1 ATOM 852 O O . GLN A 1 107 ? -5.202 72.852 -6.076 1.00 28.46 ? 107 GLN A O 1 ATOM 853 C CB . GLN A 1 107 ? -2.280 73.130 -5.486 1.00 28.65 ? 107 GLN A CB 1 ATOM 854 C CG . GLN A 1 107 ? -1.125 74.045 -5.076 1.00 28.37 ? 107 GLN A CG 1 ATOM 855 C CD . GLN A 1 107 ? -0.334 73.531 -3.893 1.00 27.61 ? 107 GLN A CD 1 ATOM 856 O OE1 . GLN A 1 107 ? -0.831 72.751 -3.075 1.00 28.64 ? 107 GLN A OE1 1 ATOM 857 N NE2 . GLN A 1 107 ? 0.902 73.988 -3.782 1.00 26.84 ? 107 GLN A NE2 1 ATOM 858 N N . VAL A 1 108 ? -4.415 72.227 -8.092 1.00 27.86 ? 108 VAL A N 1 ATOM 859 C CA . VAL A 1 108 ? -5.595 71.450 -8.449 1.00 26.35 ? 108 VAL A CA 1 ATOM 860 C C . VAL A 1 108 ? -5.188 70.079 -8.996 1.00 27.30 ? 108 VAL A C 1 ATOM 861 O O . VAL A 1 108 ? -4.089 69.911 -9.531 1.00 27.61 ? 108 VAL A O 1 ATOM 862 C CB . VAL A 1 108 ? -6.439 72.210 -9.500 1.00 25.99 ? 108 VAL A CB 1 ATOM 863 C CG1 . VAL A 1 108 ? -6.890 73.553 -8.927 1.00 22.48 ? 108 VAL A CG1 1 ATOM 864 C CG2 . VAL A 1 108 ? -5.623 72.438 -10.760 1.00 24.26 ? 108 VAL A CG2 1 ATOM 865 N N . GLN A 1 109 ? -6.076 69.099 -8.870 1.00 27.30 ? 109 GLN A N 1 ATOM 866 C CA . GLN A 1 109 ? -5.768 67.748 -9.328 1.00 27.68 ? 109 GLN A CA 1 ATOM 867 C C . GLN A 1 109 ? -6.231 67.473 -10.756 1.00 28.89 ? 109 GLN A C 1 ATOM 868 O O . GLN A 1 109 ? -7.422 67.578 -11.067 1.00 29.21 ? 109 GLN A O 1 ATOM 869 C CB . GLN A 1 109 ? -6.374 66.738 -8.353 1.00 27.82 ? 109 GLN A CB 1 ATOM 870 C CG . GLN A 1 109 ? -6.163 67.139 -6.897 1.00 28.68 ? 109 GLN A CG 1 ATOM 871 C CD . GLN A 1 109 ? -4.753 67.669 -6.635 1.00 29.36 ? 109 GLN A CD 1 ATOM 872 O OE1 . GLN A 1 109 ? -4.572 68.680 -5.949 1.00 28.79 ? 109 GLN A OE1 1 ATOM 873 N NE2 . GLN A 1 109 ? -3.753 66.988 -7.183 1.00 26.58 ? 109 GLN A NE2 1 ATOM 874 N N . ASP A 1 110 ? -5.275 67.112 -11.613 1.00 28.70 ? 110 ASP A N 1 ATOM 875 C CA . ASP A 1 110 ? -5.538 66.838 -13.027 1.00 27.54 ? 110 ASP A CA 1 ATOM 876 C C . ASP A 1 110 ? -5.318 65.381 -13.441 1.00 27.15 ? 110 ASP A C 1 ATOM 877 O O . ASP A 1 110 ? -4.572 64.639 -12.795 1.00 26.08 ? 110 ASP A O 1 ATOM 878 C CB . ASP A 1 110 ? -4.661 67.744 -13.888 1.00 28.44 ? 110 ASP A CB 1 ATOM 879 C CG . ASP A 1 110 ? -4.903 69.214 -13.618 1.00 30.29 ? 110 ASP A CG 1 ATOM 880 O OD1 . ASP A 1 110 ? -3.968 70.015 -13.823 1.00 32.91 ? 110 ASP A OD1 1 ATOM 881 O OD2 . ASP A 1 110 ? -6.031 69.572 -13.212 1.00 30.97 ? 110 ASP A OD2 1 ATOM 882 N N . LEU A 1 111 ? -5.965 64.991 -14.539 1.00 25.94 ? 111 LEU A N 1 ATOM 883 C CA . LEU A 1 111 ? -5.877 63.632 -15.072 1.00 26.07 ? 111 LEU A CA 1 ATOM 884 C C . LEU A 1 111 ? -5.243 63.614 -16.461 1.00 26.64 ? 111 LEU A C 1 ATOM 885 O O . LEU A 1 111 ? -5.468 64.512 -17.275 1.00 27.51 ? 111 LEU A O 1 ATOM 886 C CB . LEU A 1 111 ? -7.277 63.024 -15.180 1.00 26.78 ? 111 LEU A CB 1 ATOM 887 C CG . LEU A 1 111 ? -7.527 61.510 -15.224 1.00 27.32 ? 111 LEU A CG 1 ATOM 888 C CD1 . LEU A 1 111 ? -8.834 61.288 -15.971 1.00 27.10 ? 111 LEU A CD1 1 ATOM 889 C CD2 . LEU A 1 111 ? -6.411 60.754 -15.909 1.00 26.86 ? 111 LEU A CD2 1 ATOM 890 N N . ALA A 1 112 ? -4.458 62.581 -16.730 1.00 26.11 ? 112 ALA A N 1 ATOM 891 C CA . ALA A 1 112 ? -3.826 62.419 -18.032 1.00 26.06 ? 112 ALA A CA 1 ATOM 892 C C . ALA A 1 112 ? -3.588 60.933 -18.255 1.00 25.73 ? 112 ALA A C 1 ATOM 893 O O . ALA A 1 112 ? -3.501 60.164 -17.302 1.00 25.83 ? 112 ALA A O 1 ATOM 894 C CB . ALA A 1 112 ? -2.502 63.180 -18.080 1.00 24.49 ? 112 ALA A CB 1 ATOM 895 N N . TRP A 1 113 ? -3.513 60.520 -19.512 1.00 25.79 ? 113 TRP A N 1 ATOM 896 C CA . TRP A 1 113 ? -3.243 59.124 -19.815 1.00 26.33 ? 113 TRP A CA 1 ATOM 897 C C . TRP A 1 113 ? -2.553 59.084 -21.163 1.00 25.75 ? 113 TRP A C 1 ATOM 898 O O . TRP A 1 113 ? -2.636 60.034 -21.934 1.00 24.29 ? 113 TRP A O 1 ATOM 899 C CB . TRP A 1 113 ? -4.533 58.292 -19.802 1.00 28.40 ? 113 TRP A CB 1 ATOM 900 C CG . TRP A 1 113 ? -5.517 58.630 -20.862 1.00 32.99 ? 113 TRP A CG 1 ATOM 901 C CD1 . TRP A 1 113 ? -5.618 58.063 -22.101 1.00 34.05 ? 113 TRP A CD1 1 ATOM 902 C CD2 . TRP A 1 113 ? -6.547 59.620 -20.789 1.00 35.05 ? 113 TRP A CD2 1 ATOM 903 N NE1 . TRP A 1 113 ? -6.650 58.638 -22.805 1.00 34.54 ? 113 TRP A NE1 1 ATOM 904 C CE2 . TRP A 1 113 ? -7.237 59.598 -22.024 1.00 36.10 ? 113 TRP A CE2 1 ATOM 905 C CE3 . TRP A 1 113 ? -6.956 60.525 -19.800 1.00 34.35 ? 113 TRP A CE3 1 ATOM 906 C CZ2 . TRP A 1 113 ? -8.314 60.450 -22.294 1.00 36.18 ? 113 TRP A CZ2 1 ATOM 907 C CZ3 . TRP A 1 113 ? -8.027 61.372 -20.070 1.00 34.48 ? 113 TRP A CZ3 1 ATOM 908 C CH2 . TRP A 1 113 ? -8.692 61.327 -21.308 1.00 35.33 ? 113 TRP A CH2 1 ATOM 909 N N . PRO A 1 114 ? -1.826 57.997 -21.452 1.00 26.81 ? 114 PRO A N 1 ATOM 910 C CA . PRO A 1 114 ? -1.132 57.907 -22.738 1.00 27.71 ? 114 PRO A CA 1 ATOM 911 C C . PRO A 1 114 ? -2.053 58.028 -23.947 1.00 28.82 ? 114 PRO A C 1 ATOM 912 O O . PRO A 1 114 ? -3.178 57.532 -23.946 1.00 28.26 ? 114 PRO A O 1 ATOM 913 C CB . PRO A 1 114 ? -0.405 56.560 -22.648 1.00 27.72 ? 114 PRO A CB 1 ATOM 914 C CG . PRO A 1 114 ? -1.216 55.784 -21.668 1.00 27.87 ? 114 PRO A CG 1 ATOM 915 C CD . PRO A 1 114 ? -1.597 56.792 -20.638 1.00 26.83 ? 114 PRO A CD 1 ATOM 916 N N . LYS A 1 115 ? -1.564 58.700 -24.978 1.00 29.74 ? 115 LYS A N 1 ATOM 917 C CA . LYS A 1 115 ? -2.347 58.912 -26.181 1.00 31.98 ? 115 LYS A CA 1 ATOM 918 C C . LYS A 1 115 ? -2.126 57.825 -27.235 1.00 32.27 ? 115 LYS A C 1 ATOM 919 O O . LYS A 1 115 ? -2.865 57.746 -28.216 1.00 33.51 ? 115 LYS A O 1 ATOM 920 C CB . LYS A 1 115 ? -1.999 60.276 -26.778 1.00 33.86 ? 115 LYS A CB 1 ATOM 921 C CG . LYS A 1 115 ? -3.067 60.826 -27.698 1.00 38.13 ? 115 LYS A CG 1 ATOM 922 C CD . LYS A 1 115 ? -2.667 62.159 -28.296 1.00 39.39 ? 115 LYS A CD 1 ATOM 923 C CE . LYS A 1 115 ? -1.565 61.992 -29.317 1.00 40.64 ? 115 LYS A CE 1 ATOM 924 N NZ . LYS A 1 115 ? -1.380 63.251 -30.086 1.00 43.10 ? 115 LYS A NZ 1 ATOM 925 N N . ASN A 1 116 ? -1.122 56.983 -27.017 1.00 31.50 ? 116 ASN A N 1 ATOM 926 C CA . ASN A 1 116 ? -0.770 55.930 -27.962 1.00 30.77 ? 116 ASN A CA 1 ATOM 927 C C . ASN A 1 116 ? -0.265 54.685 -27.218 1.00 30.91 ? 116 ASN A C 1 ATOM 928 O O . ASN A 1 116 ? 0.939 54.503 -27.048 1.00 31.22 ? 116 ASN A O 1 ATOM 929 C CB . ASN A 1 116 ? 0.303 56.496 -28.905 1.00 30.97 ? 116 ASN A CB 1 ATOM 930 C CG . ASN A 1 116 ? 0.825 55.486 -29.906 1.00 33.42 ? 116 ASN A CG 1 ATOM 931 O OD1 . ASN A 1 116 ? 0.229 54.428 -30.128 1.00 31.95 ? 116 ASN A OD1 1 ATOM 932 N ND2 . ASN A 1 116 ? 1.952 55.837 -30.526 1.00 36.64 ? 116 ASN A ND2 1 ATOM 933 N N . LEU A 1 117 ? -1.192 53.832 -26.785 1.00 29.56 ? 117 LEU A N 1 ATOM 934 C CA . LEU A 1 117 ? -0.840 52.621 -26.045 1.00 29.87 ? 117 LEU A CA 1 ATOM 935 C C . LEU A 1 117 ? -0.023 51.610 -26.843 1.00 30.95 ? 117 LEU A C 1 ATOM 936 O O . LEU A 1 117 ? 0.416 50.598 -26.298 1.00 31.67 ? 117 LEU A O 1 ATOM 937 C CB . LEU A 1 117 ? -2.103 51.939 -25.506 1.00 29.07 ? 117 LEU A CB 1 ATOM 938 C CG . LEU A 1 117 ? -2.900 52.708 -24.446 1.00 29.66 ? 117 LEU A CG 1 ATOM 939 C CD1 . LEU A 1 117 ? -4.108 51.887 -24.028 1.00 29.01 ? 117 LEU A CD1 1 ATOM 940 C CD2 . LEU A 1 117 ? -2.023 52.997 -23.239 1.00 28.15 ? 117 LEU A CD2 1 ATOM 941 N N . SER A 1 118 ? 0.176 51.877 -28.131 1.00 30.51 ? 118 SER A N 1 ATOM 942 C CA . SER A 1 118 ? 0.964 50.985 -28.979 1.00 30.81 ? 118 SER A CA 1 ATOM 943 C C . SER A 1 118 ? 2.436 51.259 -28.743 1.00 29.62 ? 118 SER A C 1 ATOM 944 O O . SER A 1 118 ? 3.296 50.434 -29.040 1.00 29.39 ? 118 SER A O 1 ATOM 945 C CB . SER A 1 118 ? 0.653 51.227 -30.452 1.00 31.78 ? 118 SER A CB 1 ATOM 946 O OG . SER A 1 118 ? -0.678 50.857 -30.753 1.00 39.23 ? 118 SER A OG 1 ATOM 947 N N . ASP A 1 119 ? 2.712 52.442 -28.213 1.00 27.81 ? 119 ASP A N 1 ATOM 948 C CA . ASP A 1 119 ? 4.069 52.861 -27.929 1.00 26.72 ? 119 ASP A CA 1 ATOM 949 C C . ASP A 1 119 ? 4.554 52.248 -26.613 1.00 26.72 ? 119 ASP A C 1 ATOM 950 O O . ASP A 1 119 ? 4.063 52.590 -25.543 1.00 27.19 ? 119 ASP A O 1 ATOM 951 C CB . ASP A 1 119 ? 4.122 54.388 -27.855 1.00 25.30 ? 119 ASP A CB 1 ATOM 952 C CG . ASP A 1 119 ? 5.512 54.908 -27.569 1.00 26.61 ? 119 ASP A CG 1 ATOM 953 O OD1 . ASP A 1 119 ? 6.450 54.083 -27.512 1.00 26.27 ? 119 ASP A OD1 1 ATOM 954 O OD2 . ASP A 1 119 ? 5.667 56.137 -27.409 1.00 26.78 ? 119 ASP A OD2 1 ATOM 955 N N . PRO A 1 120 ? 5.527 51.330 -26.681 1.00 26.24 ? 120 PRO A N 1 ATOM 956 C CA . PRO A 1 120 ? 6.080 50.668 -25.492 1.00 25.97 ? 120 PRO A CA 1 ATOM 957 C C . PRO A 1 120 ? 6.603 51.670 -24.476 1.00 25.85 ? 120 PRO A C 1 ATOM 958 O O . PRO A 1 120 ? 6.625 51.398 -23.276 1.00 26.13 ? 120 PRO A O 1 ATOM 959 C CB . PRO A 1 120 ? 7.220 49.822 -26.058 1.00 25.05 ? 120 PRO A CB 1 ATOM 960 C CG . PRO A 1 120 ? 6.774 49.532 -27.434 1.00 27.84 ? 120 PRO A CG 1 ATOM 961 C CD . PRO A 1 120 ? 6.203 50.852 -27.897 1.00 26.78 ? 120 PRO A CD 1 ATOM 962 N N . PHE A 1 121 ? 7.024 52.830 -24.967 1.00 24.62 ? 121 PHE A N 1 ATOM 963 C CA . PHE A 1 121 ? 7.572 53.852 -24.098 1.00 24.13 ? 121 PHE A CA 1 ATOM 964 C C . PHE A 1 121 ? 6.584 54.923 -23.640 1.00 24.88 ? 121 PHE A C 1 ATOM 965 O O . PHE A 1 121 ? 6.944 55.797 -22.854 1.00 26.36 ? 121 PHE A O 1 ATOM 966 C CB . PHE A 1 121 ? 8.781 54.497 -24.773 1.00 23.23 ? 121 PHE A CB 1 ATOM 967 C CG . PHE A 1 121 ? 9.948 53.561 -24.949 1.00 23.41 ? 121 PHE A CG 1 ATOM 968 C CD1 . PHE A 1 121 ? 9.920 52.273 -24.411 1.00 23.37 ? 121 PHE A CD1 1 ATOM 969 C CD2 . PHE A 1 121 ? 11.089 53.973 -25.625 1.00 23.09 ? 121 PHE A CD2 1 ATOM 970 C CE1 . PHE A 1 121 ? 11.019 51.412 -24.546 1.00 22.30 ? 121 PHE A CE1 1 ATOM 971 C CE2 . PHE A 1 121 ? 12.194 53.118 -25.763 1.00 22.77 ? 121 PHE A CE2 1 ATOM 972 C CZ . PHE A 1 121 ? 12.157 51.838 -25.222 1.00 20.49 ? 121 PHE A CZ 1 ATOM 973 N N . LEU A 1 122 ? 5.345 54.854 -24.116 1.00 23.59 ? 122 LEU A N 1 ATOM 974 C CA . LEU A 1 122 ? 4.329 55.826 -23.722 1.00 23.79 ? 122 LEU A CA 1 ATOM 975 C C . LEU A 1 122 ? 4.881 57.256 -23.682 1.00 24.51 ? 122 LEU A C 1 ATOM 976 O O . LEU A 1 122 ? 4.883 57.898 -22.630 1.00 24.43 ? 122 LEU A O 1 ATOM 977 C CB . LEU A 1 122 ? 3.782 55.466 -22.338 1.00 22.67 ? 122 LEU A CB 1 ATOM 978 C CG . LEU A 1 122 ? 3.235 54.055 -22.107 1.00 22.29 ? 122 LEU A CG 1 ATOM 979 C CD1 . LEU A 1 122 ? 2.675 53.966 -20.694 1.00 21.72 ? 122 LEU A CD1 1 ATOM 980 C CD2 . LEU A 1 122 ? 2.146 53.733 -23.121 1.00 22.87 ? 122 LEU A CD2 1 ATOM 981 N N . ARG A 1 123 ? 5.338 57.758 -24.824 1.00 24.45 ? 123 ARG A N 1 ATOM 982 C CA . ARG A 1 123 ? 5.904 59.103 -24.876 1.00 27.50 ? 123 ARG A CA 1 ATOM 983 C C . ARG A 1 123 ? 4.869 60.224 -24.848 1.00 27.87 ? 123 ARG A C 1 ATOM 984 O O . ARG A 1 123 ? 5.049 61.228 -24.159 1.00 27.67 ? 123 ARG A O 1 ATOM 985 C CB . ARG A 1 123 ? 6.758 59.268 -26.129 1.00 29.15 ? 123 ARG A CB 1 ATOM 986 C CG . ARG A 1 123 ? 7.742 58.155 -26.370 1.00 31.94 ? 123 ARG A CG 1 ATOM 987 C CD . ARG A 1 123 ? 8.660 58.522 -27.509 1.00 35.15 ? 123 ARG A CD 1 ATOM 988 N NE . ARG A 1 123 ? 9.503 57.402 -27.899 1.00 40.16 ? 123 ARG A NE 1 ATOM 989 C CZ . ARG A 1 123 ? 10.813 57.482 -28.123 1.00 44.50 ? 123 ARG A CZ 1 ATOM 990 N NH1 . ARG A 1 123 ? 11.455 58.646 -27.993 1.00 44.06 ? 123 ARG A NH1 1 ATOM 991 N NH2 . ARG A 1 123 ? 11.484 56.392 -28.480 1.00 44.73 ? 123 ARG A NH2 1 ATOM 992 N N . GLU A 1 124 ? 3.794 60.058 -25.607 1.00 28.24 ? 124 GLU A N 1 ATOM 993 C CA . GLU A 1 124 ? 2.754 61.073 -25.684 1.00 29.40 ? 124 GLU A CA 1 ATOM 994 C C . GLU A 1 124 ? 1.604 60.859 -24.717 1.00 29.31 ? 124 GLU A C 1 ATOM 995 O O . GLU A 1 124 ? 1.041 59.770 -24.628 1.00 30.52 ? 124 GLU A O 1 ATOM 996 C CB . GLU A 1 124 ? 2.196 61.136 -27.103 1.00 32.67 ? 124 GLU A CB 1 ATOM 997 C CG . GLU A 1 124 ? 3.229 61.449 -28.165 1.00 36.85 ? 124 GLU A CG 1 ATOM 998 C CD . GLU A 1 124 ? 3.968 62.738 -27.880 1.00 40.08 ? 124 GLU A CD 1 ATOM 999 O OE1 . GLU A 1 124 ? 3.326 63.698 -27.397 1.00 43.10 ? 124 GLU A OE1 1 ATOM 1000 O OE2 . GLU A 1 124 ? 5.186 62.798 -28.150 1.00 41.97 ? 124 GLU A OE2 1 ATOM 1001 N N . TRP A 1 125 ? 1.243 61.915 -24.003 1.00 28.67 ? 125 TRP A N 1 ATOM 1002 C CA . TRP A 1 125 ? 0.143 61.840 -23.055 1.00 28.06 ? 125 TRP A CA 1 ATOM 1003 C C . TRP A 1 125 ? -0.926 62.873 -23.398 1.00 28.20 ? 125 TRP A C 1 ATOM 1004 O O . TRP A 1 125 ? -0.623 63.965 -23.885 1.00 28.74 ? 125 TRP A O 1 ATOM 1005 C CB . TRP A 1 125 ? 0.658 62.062 -21.633 1.00 26.46 ? 125 TRP A CB 1 ATOM 1006 C CG . TRP A 1 125 ? 1.554 60.954 -21.170 1.00 26.04 ? 125 TRP A CG 1 ATOM 1007 C CD1 . TRP A 1 125 ? 2.806 60.657 -21.636 1.00 26.18 ? 125 TRP A CD1 1 ATOM 1008 C CD2 . TRP A 1 125 ? 1.237 59.946 -20.203 1.00 24.25 ? 125 TRP A CD2 1 ATOM 1009 N NE1 . TRP A 1 125 ? 3.285 59.521 -21.025 1.00 26.50 ? 125 TRP A NE1 1 ATOM 1010 C CE2 . TRP A 1 125 ? 2.342 59.064 -20.140 1.00 25.89 ? 125 TRP A CE2 1 ATOM 1011 C CE3 . TRP A 1 125 ? 0.127 59.699 -19.385 1.00 22.17 ? 125 TRP A CE3 1 ATOM 1012 C CZ2 . TRP A 1 125 ? 2.365 57.952 -19.292 1.00 25.30 ? 125 TRP A CZ2 1 ATOM 1013 C CZ3 . TRP A 1 125 ? 0.149 58.593 -18.541 1.00 22.87 ? 125 TRP A CZ3 1 ATOM 1014 C CH2 . TRP A 1 125 ? 1.262 57.733 -18.502 1.00 24.41 ? 125 TRP A CH2 1 ATOM 1015 N N . VAL A 1 126 ? -2.180 62.515 -23.159 1.00 26.81 ? 126 VAL A N 1 ATOM 1016 C CA . VAL A 1 126 ? -3.284 63.418 -23.433 1.00 26.30 ? 126 VAL A CA 1 ATOM 1017 C C . VAL A 1 126 ? -3.933 63.799 -22.102 1.00 25.77 ? 126 VAL A C 1 ATOM 1018 O O . VAL A 1 126 ? -3.962 63.000 -21.164 1.00 25.15 ? 126 VAL A O 1 ATOM 1019 C CB . VAL A 1 126 ? -4.321 62.747 -24.360 1.00 27.11 ? 126 VAL A CB 1 ATOM 1020 C CG1 . VAL A 1 126 ? -4.919 61.518 -23.680 1.00 28.26 ? 126 VAL A CG1 1 ATOM 1021 C CG2 . VAL A 1 126 ? -5.406 63.743 -24.731 1.00 28.95 ? 126 VAL A CG2 1 ATOM 1022 N N . LYS A 1 127 ? -4.444 65.021 -22.014 1.00 25.12 ? 127 LYS A N 1 ATOM 1023 C CA . LYS A 1 127 ? -5.068 65.480 -20.780 1.00 26.72 ? 127 LYS A CA 1 ATOM 1024 C C . LYS A 1 127 ? -6.582 65.499 -20.851 1.00 26.54 ? 127 LYS A C 1 ATOM 1025 O O . LYS A 1 127 ? -7.152 65.743 -21.908 1.00 25.99 ? 127 LYS A O 1 ATOM 1026 C CB . LYS A 1 127 ? -4.519 66.858 -20.416 1.00 26.23 ? 127 LYS A CB 1 ATOM 1027 C CG . LYS A 1 127 ? -3.048 66.766 -20.056 1.00 26.52 ? 127 LYS A CG 1 ATOM 1028 C CD . LYS A 1 127 ? -2.422 68.101 -19.810 1.00 27.17 ? 127 LYS A CD 1 ATOM 1029 C CE . LYS A 1 127 ? -0.930 67.939 -19.633 1.00 24.87 ? 127 LYS A CE 1 ATOM 1030 N NZ . LYS A 1 127 ? -0.282 69.263 -19.524 1.00 25.34 ? 127 LYS A NZ 1 ATOM 1031 N N . HIS A 1 128 ? -7.233 65.217 -19.725 1.00 27.56 ? 128 HIS A N 1 ATOM 1032 C CA . HIS A 1 128 ? -8.686 65.201 -19.698 1.00 28.51 ? 128 HIS A CA 1 ATOM 1033 C C . HIS A 1 128 ? -9.255 66.597 -19.913 1.00 29.56 ? 128 HIS A C 1 ATOM 1034 O O . HIS A 1 128 ? -8.812 67.566 -19.291 1.00 29.73 ? 128 HIS A O 1 ATOM 1035 C CB . HIS A 1 128 ? -9.213 64.652 -18.382 1.00 29.22 ? 128 HIS A CB 1 ATOM 1036 C CG . HIS A 1 128 ? -10.673 64.332 -18.432 1.00 31.40 ? 128 HIS A CG 1 ATOM 1037 N ND1 . HIS A 1 128 ? -11.150 63.086 -18.778 1.00 31.70 ? 128 HIS A ND1 1 ATOM 1038 C CD2 . HIS A 1 128 ? -11.761 65.121 -18.278 1.00 30.64 ? 128 HIS A CD2 1 ATOM 1039 C CE1 . HIS A 1 128 ? -12.469 63.122 -18.836 1.00 32.44 ? 128 HIS A CE1 1 ATOM 1040 N NE2 . HIS A 1 128 ? -12.865 64.346 -18.538 1.00 33.47 ? 128 HIS A NE2 1 ATOM 1041 N N . PRO A 1 129 ? -10.263 66.716 -20.793 1.00 30.54 ? 129 PRO A N 1 ATOM 1042 C CA . PRO A 1 129 ? -10.882 68.011 -21.086 1.00 29.99 ? 129 PRO A CA 1 ATOM 1043 C C . PRO A 1 129 ? -11.524 68.672 -19.873 1.00 30.54 ? 129 PRO A C 1 ATOM 1044 O O . PRO A 1 129 ? -11.690 69.887 -19.845 1.00 30.58 ? 129 PRO A O 1 ATOM 1045 C CB . PRO A 1 129 ? -11.911 67.667 -22.161 1.00 27.84 ? 129 PRO A CB 1 ATOM 1046 C CG . PRO A 1 129 ? -11.345 66.457 -22.810 1.00 28.16 ? 129 PRO A CG 1 ATOM 1047 C CD . PRO A 1 129 ? -10.857 65.662 -21.631 1.00 28.62 ? 129 PRO A CD 1 ATOM 1048 N N . LYS A 1 130 ? -11.884 67.882 -18.870 1.00 32.16 ? 130 LYS A N 1 ATOM 1049 C CA . LYS A 1 130 ? -12.525 68.446 -17.691 1.00 34.02 ? 130 LYS A CA 1 ATOM 1050 C C . LYS A 1 130 ? -11.598 68.844 -16.542 1.00 33.78 ? 130 LYS A C 1 ATOM 1051 O O . LYS A 1 130 ? -12.071 69.141 -15.445 1.00 35.50 ? 130 LYS A O 1 ATOM 1052 C CB . LYS A 1 130 ? -13.628 67.505 -17.190 1.00 35.31 ? 130 LYS A CB 1 ATOM 1053 C CG . LYS A 1 130 ? -14.948 67.690 -17.937 1.00 40.68 ? 130 LYS A CG 1 ATOM 1054 C CD . LYS A 1 130 ? -16.069 66.764 -17.445 1.00 45.80 ? 130 LYS A CD 1 ATOM 1055 C CE . LYS A 1 130 ? -15.943 65.355 -18.030 1.00 49.50 ? 130 LYS A CE 1 ATOM 1056 N NZ . LYS A 1 130 ? -17.114 64.477 -17.692 1.00 51.40 ? 130 LYS A NZ 1 ATOM 1057 N N . ASN A 1 131 ? -10.288 68.873 -16.779 1.00 32.18 ? 131 ASN A N 1 ATOM 1058 C CA . ASN A 1 131 ? -9.363 69.273 -15.719 1.00 31.55 ? 131 ASN A CA 1 ATOM 1059 C C . ASN A 1 131 ? -9.625 70.733 -15.339 1.00 32.00 ? 131 ASN A C 1 ATOM 1060 O O . ASN A 1 131 ? -9.942 71.559 -16.196 1.00 32.48 ? 131 ASN A O 1 ATOM 1061 C CB . ASN A 1 131 ? -7.898 69.116 -16.157 1.00 29.41 ? 131 ASN A CB 1 ATOM 1062 C CG . ASN A 1 131 ? -7.437 67.664 -16.167 1.00 27.53 ? 131 ASN A CG 1 ATOM 1063 O OD1 . ASN A 1 131 ? -7.979 66.822 -15.455 1.00 25.58 ? 131 ASN A OD1 1 ATOM 1064 N ND2 . ASN A 1 131 ? -6.415 67.374 -16.962 1.00 26.06 ? 131 ASN A ND2 1 ATOM 1065 N N . PRO A 1 132 ? -9.487 71.071 -14.047 1.00 31.82 ? 132 PRO A N 1 ATOM 1066 C CA . PRO A 1 132 ? -9.106 70.162 -12.962 1.00 31.42 ? 132 PRO A CA 1 ATOM 1067 C C . PRO A 1 132 ? -10.251 69.269 -12.496 1.00 31.07 ? 132 PRO A C 1 ATOM 1068 O O . PRO A 1 132 ? -11.415 69.671 -12.509 1.00 31.94 ? 132 PRO A O 1 ATOM 1069 C CB . PRO A 1 132 ? -8.643 71.119 -11.870 1.00 31.85 ? 132 PRO A CB 1 ATOM 1070 C CG . PRO A 1 132 ? -9.587 72.267 -12.047 1.00 31.19 ? 132 PRO A CG 1 ATOM 1071 C CD . PRO A 1 132 ? -9.601 72.454 -13.551 1.00 30.79 ? 132 PRO A CD 1 ATOM 1072 N N . LEU A 1 133 ? -9.912 68.055 -12.081 1.00 29.83 ? 133 LEU A N 1 ATOM 1073 C CA . LEU A 1 133 ? -10.904 67.107 -11.599 1.00 28.21 ? 133 LEU A CA 1 ATOM 1074 C C . LEU A 1 133 ? -11.232 67.364 -10.129 1.00 27.32 ? 133 LEU A C 1 ATOM 1075 O O . LEU A 1 133 ? -12.336 67.081 -9.672 1.00 27.17 ? 133 LEU A O 1 ATOM 1076 C CB . LEU A 1 133 ? -10.388 65.677 -11.785 1.00 28.23 ? 133 LEU A CB 1 ATOM 1077 C CG . LEU A 1 133 ? -10.825 64.931 -13.050 1.00 28.40 ? 133 LEU A CG 1 ATOM 1078 C CD1 . LEU A 1 133 ? -10.708 65.835 -14.259 1.00 25.92 ? 133 LEU A CD1 1 ATOM 1079 C CD2 . LEU A 1 133 ? -9.984 63.674 -13.211 1.00 26.59 ? 133 LEU A CD2 1 ATOM 1080 N N . ILE A 1 134 ? -10.268 67.900 -9.390 1.00 26.84 ? 134 ILE A N 1 ATOM 1081 C CA . ILE A 1 134 ? -10.470 68.196 -7.979 1.00 26.31 ? 134 ILE A CA 1 ATOM 1082 C C . ILE A 1 134 ? -9.798 69.513 -7.626 1.00 28.85 ? 134 ILE A C 1 ATOM 1083 O O . ILE A 1 134 ? -8.676 69.785 -8.060 1.00 29.20 ? 134 ILE A O 1 ATOM 1084 C CB . ILE A 1 134 ? -9.860 67.110 -7.073 1.00 24.90 ? 134 ILE A CB 1 ATOM 1085 C CG1 . ILE A 1 134 ? -10.376 65.733 -7.478 1.00 23.88 ? 134 ILE A CG1 1 ATOM 1086 C CG2 . ILE A 1 134 ? -10.205 67.397 -5.623 1.00 20.18 ? 134 ILE A CG2 1 ATOM 1087 C CD1 . ILE A 1 134 ? -9.757 64.602 -6.693 1.00 24.44 ? 134 ILE A CD1 1 ATOM 1088 N N . THR A 1 135 ? -10.493 70.326 -6.841 1.00 31.30 ? 135 THR A N 1 ATOM 1089 C CA . THR A 1 135 ? -9.966 71.613 -6.396 1.00 33.02 ? 135 THR A CA 1 ATOM 1090 C C . THR A 1 135 ? -9.949 71.637 -4.870 1.00 34.08 ? 135 THR A C 1 ATOM 1091 O O . THR A 1 135 ? -10.627 70.837 -4.223 1.00 34.38 ? 135 THR A O 1 ATOM 1092 C CB . THR A 1 135 ? -10.825 72.781 -6.904 1.00 33.12 ? 135 THR A CB 1 ATOM 1093 O OG1 . THR A 1 135 ? -12.203 72.527 -6.601 1.00 35.04 ? 135 THR A OG1 1 ATOM 1094 C CG2 . THR A 1 135 ? -10.648 72.953 -8.397 1.00 30.81 ? 135 THR A CG2 1 ATOM 1095 N N . PRO A 1 136 ? -9.175 72.558 -4.277 1.00 35.85 ? 136 PRO A N 1 ATOM 1096 C CA . PRO A 1 136 ? -9.072 72.673 -2.816 1.00 36.55 ? 136 PRO A CA 1 ATOM 1097 C C . PRO A 1 136 ? -10.419 72.655 -2.096 1.00 38.23 ? 136 PRO A C 1 ATOM 1098 O O . PRO A 1 136 ? -11.345 73.363 -2.491 1.00 37.16 ? 136 PRO A O 1 ATOM 1099 C CB . PRO A 1 136 ? -8.344 74.002 -2.629 1.00 35.88 ? 136 PRO A CB 1 ATOM 1100 C CG . PRO A 1 136 ? -7.471 74.078 -3.843 1.00 36.50 ? 136 PRO A CG 1 ATOM 1101 C CD . PRO A 1 136 ? -8.407 73.628 -4.941 1.00 35.37 ? 136 PRO A CD 1 ATOM 1102 N N . PRO A 1 137 ? -10.544 71.832 -1.034 1.00 40.68 ? 137 PRO A N 1 ATOM 1103 C CA . PRO A 1 137 ? -11.784 71.731 -0.251 1.00 42.66 ? 137 PRO A CA 1 ATOM 1104 C C . PRO A 1 137 ? -12.104 73.090 0.367 1.00 46.11 ? 137 PRO A C 1 ATOM 1105 O O . PRO A 1 137 ? -11.334 74.040 0.215 1.00 46.58 ? 137 PRO A O 1 ATOM 1106 C CB . PRO A 1 137 ? -11.442 70.689 0.810 1.00 42.21 ? 137 PRO A CB 1 ATOM 1107 C CG . PRO A 1 137 ? -10.445 69.821 0.118 1.00 41.44 ? 137 PRO A CG 1 ATOM 1108 C CD . PRO A 1 137 ? -9.566 70.824 -0.590 1.00 40.44 ? 137 PRO A CD 1 ATOM 1109 N N . GLU A 1 138 ? -13.217 73.183 1.085 1.00 48.97 ? 138 GLU A N 1 ATOM 1110 C CA . GLU A 1 138 ? -13.598 74.461 1.670 1.00 51.17 ? 138 GLU A CA 1 ATOM 1111 C C . GLU A 1 138 ? -12.526 75.201 2.471 1.00 50.75 ? 138 GLU A C 1 ATOM 1112 O O . GLU A 1 138 ? -11.928 76.158 1.971 1.00 52.72 ? 138 GLU A O 1 ATOM 1113 C CB . GLU A 1 138 ? -14.856 74.310 2.526 1.00 55.74 ? 138 GLU A CB 1 ATOM 1114 C CG . GLU A 1 138 ? -15.279 75.621 3.193 1.00 61.79 ? 138 GLU A CG 1 ATOM 1115 C CD . GLU A 1 138 ? -15.314 76.808 2.224 1.00 64.75 ? 138 GLU A CD 1 ATOM 1116 O OE1 . GLU A 1 138 ? -15.365 77.966 2.701 1.00 66.22 ? 138 GLU A OE1 1 ATOM 1117 O OE2 . GLU A 1 138 ? -15.298 76.590 0.991 1.00 65.57 ? 138 GLU A OE2 1 ATOM 1118 N N . GLY A 1 139 ? -12.277 74.777 3.704 1.00 47.65 ? 139 GLY A N 1 ATOM 1119 C CA . GLY A 1 139 ? -11.293 75.481 4.512 1.00 45.87 ? 139 GLY A CA 1 ATOM 1120 C C . GLY A 1 139 ? -9.830 75.180 4.238 1.00 44.66 ? 139 GLY A C 1 ATOM 1121 O O . GLY A 1 139 ? -9.022 75.147 5.170 1.00 46.09 ? 139 GLY A O 1 ATOM 1122 N N . VAL A 1 140 ? -9.477 74.977 2.971 1.00 42.05 ? 140 VAL A N 1 ATOM 1123 C CA . VAL A 1 140 ? -8.100 74.656 2.606 1.00 38.97 ? 140 VAL A CA 1 ATOM 1124 C C . VAL A 1 140 ? -7.517 75.678 1.635 1.00 38.79 ? 140 VAL A C 1 ATOM 1125 O O . VAL A 1 140 ? -8.124 75.980 0.608 1.00 39.19 ? 140 VAL A O 1 ATOM 1126 C CB . VAL A 1 140 ? -8.026 73.251 1.973 1.00 38.45 ? 140 VAL A CB 1 ATOM 1127 C CG1 . VAL A 1 140 ? -6.580 72.854 1.742 1.00 35.77 ? 140 VAL A CG1 1 ATOM 1128 C CG2 . VAL A 1 140 ? -8.730 72.244 2.867 1.00 33.99 ? 140 VAL A CG2 1 ATOM 1129 N N . LYS A 1 141 ? -6.338 76.202 1.960 1.00 39.07 ? 141 LYS A N 1 ATOM 1130 C CA . LYS A 1 141 ? -5.684 77.202 1.119 1.00 39.54 ? 141 LYS A CA 1 ATOM 1131 C C . LYS A 1 141 ? -5.327 76.653 -0.252 1.00 39.34 ? 141 LYS A C 1 ATOM 1132 O O . LYS A 1 141 ? -5.151 75.451 -0.422 1.00 39.87 ? 141 LYS A O 1 ATOM 1133 C CB . LYS A 1 141 ? -4.424 77.725 1.800 1.00 41.40 ? 141 LYS A CB 1 ATOM 1134 C CG . LYS A 1 141 ? -4.683 78.442 3.108 1.00 44.21 ? 141 LYS A CG 1 ATOM 1135 C CD . LYS A 1 141 ? -3.369 78.817 3.774 1.00 50.07 ? 141 LYS A CD 1 ATOM 1136 C CE . LYS A 1 141 ? -3.585 79.435 5.152 1.00 53.27 ? 141 LYS A CE 1 ATOM 1137 N NZ . LYS A 1 141 ? -4.263 80.762 5.080 1.00 55.82 ? 141 LYS A NZ 1 ATOM 1138 N N . ASP A 1 142 ? -5.210 77.546 -1.231 1.00 38.40 ? 142 ASP A N 1 ATOM 1139 C CA . ASP A 1 142 ? -4.891 77.139 -2.592 1.00 37.43 ? 142 ASP A CA 1 ATOM 1140 C C . ASP A 1 142 ? -3.510 76.534 -2.797 1.00 35.62 ? 142 ASP A C 1 ATOM 1141 O O . ASP A 1 142 ? -3.259 75.923 -3.828 1.00 34.72 ? 142 ASP A O 1 ATOM 1142 C CB . ASP A 1 142 ? -5.055 78.313 -3.555 1.00 39.78 ? 142 ASP A CB 1 ATOM 1143 C CG . ASP A 1 142 ? -6.493 78.772 -3.677 1.00 42.10 ? 142 ASP A CG 1 ATOM 1144 O OD1 . ASP A 1 142 ? -7.417 77.928 -3.561 1.00 43.67 ? 142 ASP A OD1 1 ATOM 1145 O OD2 . ASP A 1 142 ? -6.694 79.981 -3.909 1.00 43.37 ? 142 ASP A OD2 1 ATOM 1146 N N . ASP A 1 143 ? -2.611 76.703 -1.838 1.00 34.21 ? 143 ASP A N 1 ATOM 1147 C CA . ASP A 1 143 ? -1.271 76.144 -1.980 1.00 33.40 ? 143 ASP A CA 1 ATOM 1148 C C . ASP A 1 143 ? -0.984 75.085 -0.919 1.00 31.99 ? 143 ASP A C 1 ATOM 1149 O O . ASP A 1 143 ? 0.163 74.873 -0.524 1.00 30.45 ? 143 ASP A O 1 ATOM 1150 C CB . ASP A 1 143 ? -0.231 77.257 -1.905 1.00 34.40 ? 143 ASP A CB 1 ATOM 1151 C CG . ASP A 1 143 ? -0.361 78.084 -0.648 1.00 38.68 ? 143 ASP A CG 1 ATOM 1152 O OD1 . ASP A 1 143 ? 0.473 78.990 -0.447 1.00 42.96 ? 143 ASP A OD1 1 ATOM 1153 O OD2 . ASP A 1 143 ? -1.299 77.835 0.141 1.00 40.32 ? 143 ASP A OD2 1 ATOM 1154 N N . CYS A 1 144 ? -2.042 74.420 -0.469 1.00 30.15 ? 144 CYS A N 1 ATOM 1155 C CA . CYS A 1 144 ? -1.925 73.382 0.542 1.00 30.59 ? 144 CYS A CA 1 ATOM 1156 C C . CYS A 1 144 ? -2.842 72.215 0.190 1.00 29.17 ? 144 CYS A C 1 ATOM 1157 O O . CYS A 1 144 ? -3.535 71.676 1.048 1.00 28.08 ? 144 CYS A O 1 ATOM 1158 C CB . CYS A 1 144 ? -2.301 73.948 1.915 1.00 32.51 ? 144 CYS A CB 1 ATOM 1159 S SG . CYS A 1 144 ? -1.272 75.344 2.444 1.00 36.79 ? 144 CYS A SG 1 ATOM 1160 N N . PHE A 1 145 ? -2.832 71.818 -1.076 1.00 28.36 ? 145 PHE A N 1 ATOM 1161 C CA . PHE A 1 145 ? -3.684 70.728 -1.536 1.00 28.31 ? 145 PHE A CA 1 ATOM 1162 C C . PHE A 1 145 ? -2.992 70.072 -2.730 1.00 28.45 ? 145 PHE A C 1 ATOM 1163 O O . PHE A 1 145 ? -3.187 70.496 -3.871 1.00 29.27 ? 145 PHE A O 1 ATOM 1164 C CB . PHE A 1 145 ? -5.036 71.315 -1.945 1.00 27.02 ? 145 PHE A CB 1 ATOM 1165 C CG . PHE A 1 145 ? -6.051 70.294 -2.342 1.00 27.85 ? 145 PHE A CG 1 ATOM 1166 C CD1 . PHE A 1 145 ? -6.451 69.308 -1.449 1.00 28.26 ? 145 PHE A CD1 1 ATOM 1167 C CD2 . PHE A 1 145 ? -6.622 70.325 -3.612 1.00 28.09 ? 145 PHE A CD2 1 ATOM 1168 C CE1 . PHE A 1 145 ? -7.410 68.362 -1.815 1.00 28.44 ? 145 PHE A CE1 1 ATOM 1169 C CE2 . PHE A 1 145 ? -7.580 69.387 -3.989 1.00 27.79 ? 145 PHE A CE2 1 ATOM 1170 C CZ . PHE A 1 145 ? -7.975 68.401 -3.088 1.00 28.17 ? 145 PHE A CZ 1 ATOM 1171 N N . ARG A 1 146 ? -2.191 69.036 -2.486 1.00 26.51 ? 146 ARG A N 1 ATOM 1172 C CA . ARG A 1 146 ? -1.472 68.412 -3.593 1.00 24.39 ? 146 ARG A CA 1 ATOM 1173 C C . ARG A 1 146 ? -0.976 66.984 -3.402 1.00 23.69 ? 146 ARG A C 1 ATOM 1174 O O . ARG A 1 146 ? -1.129 66.378 -2.338 1.00 20.97 ? 146 ARG A O 1 ATOM 1175 C CB . ARG A 1 146 ? -0.273 69.284 -3.956 1.00 25.75 ? 146 ARG A CB 1 ATOM 1176 C CG . ARG A 1 146 ? 0.700 69.462 -2.799 1.00 26.03 ? 146 ARG A CG 1 ATOM 1177 C CD . ARG A 1 146 ? 1.915 70.273 -3.208 1.00 29.53 ? 146 ARG A CD 1 ATOM 1178 N NE . ARG A 1 146 ? 2.773 70.560 -2.062 1.00 30.80 ? 146 ARG A NE 1 ATOM 1179 C CZ . ARG A 1 146 ? 2.471 71.425 -1.098 1.00 31.56 ? 146 ARG A CZ 1 ATOM 1180 N NH1 . ARG A 1 146 ? 1.331 72.102 -1.137 1.00 32.44 ? 146 ARG A NH1 1 ATOM 1181 N NH2 . ARG A 1 146 ? 3.299 71.600 -0.080 1.00 29.05 ? 146 ARG A NH2 1 ATOM 1182 N N . ASP A 1 147 ? -0.371 66.471 -4.474 1.00 23.36 ? 147 ASP A N 1 ATOM 1183 C CA . ASP A 1 147 ? 0.216 65.134 -4.529 1.00 22.42 ? 147 ASP A CA 1 ATOM 1184 C C . ASP A 1 147 ? -0.754 63.964 -4.415 1.00 22.96 ? 147 ASP A C 1 ATOM 1185 O O . ASP A 1 147 ? -0.722 63.215 -3.437 1.00 24.06 ? 147 ASP A O 1 ATOM 1186 C CB . ASP A 1 147 ? 1.297 64.997 -3.457 1.00 21.45 ? 147 ASP A CB 1 ATOM 1187 C CG . ASP A 1 147 ? 2.245 66.174 -3.441 1.00 21.92 ? 147 ASP A CG 1 ATOM 1188 O OD1 . ASP A 1 147 ? 2.367 66.857 -4.476 1.00 21.35 ? 147 ASP A OD1 1 ATOM 1189 O OD2 . ASP A 1 147 ? 2.877 66.411 -2.394 1.00 23.65 ? 147 ASP A OD2 1 ATOM 1190 N N . PRO A 1 148 ? -1.629 63.783 -5.419 1.00 22.58 ? 148 PRO A N 1 ATOM 1191 C CA . PRO A 1 148 ? -2.585 62.670 -5.373 1.00 21.23 ? 148 PRO A CA 1 ATOM 1192 C C . PRO A 1 148 ? -1.848 61.332 -5.441 1.00 21.25 ? 148 PRO A C 1 ATOM 1193 O O . PRO A 1 148 ? -0.856 61.183 -6.160 1.00 19.16 ? 148 PRO A O 1 ATOM 1194 C CB . PRO A 1 148 ? -3.474 62.927 -6.589 1.00 21.06 ? 148 PRO A CB 1 ATOM 1195 C CG . PRO A 1 148 ? -2.544 63.605 -7.547 1.00 22.24 ? 148 PRO A CG 1 ATOM 1196 C CD . PRO A 1 148 ? -1.768 64.556 -6.666 1.00 21.80 ? 148 PRO A CD 1 ATOM 1197 N N . SER A 1 149 ? -2.337 60.366 -4.678 1.00 21.01 ? 149 SER A N 1 ATOM 1198 C CA . SER A 1 149 ? -1.724 59.044 -4.620 1.00 21.82 ? 149 SER A CA 1 ATOM 1199 C C . SER A 1 149 ? -2.231 58.106 -5.704 1.00 23.73 ? 149 SER A C 1 ATOM 1200 O O . SER A 1 149 ? -3.054 58.474 -6.540 1.00 23.24 ? 149 SER A O 1 ATOM 1201 C CB . SER A 1 149 ? -2.039 58.391 -3.281 1.00 21.94 ? 149 SER A CB 1 ATOM 1202 O OG . SER A 1 149 ? -3.404 57.994 -3.239 1.00 21.34 ? 149 SER A OG 1 ATOM 1203 N N . THR A 1 150 ? -1.722 56.882 -5.679 1.00 23.84 ? 150 THR A N 1 ATOM 1204 C CA . THR A 1 150 ? -2.176 55.861 -6.604 1.00 23.15 ? 150 THR A CA 1 ATOM 1205 C C . THR A 1 150 ? -3.537 55.478 -6.024 1.00 23.07 ? 150 THR A C 1 ATOM 1206 O O . THR A 1 150 ? -3.717 55.481 -4.808 1.00 22.36 ? 150 THR A O 1 ATOM 1207 C CB . THR A 1 150 ? -1.230 54.656 -6.593 1.00 23.55 ? 150 THR A CB 1 ATOM 1208 O OG1 . THR A 1 150 ? -0.028 55.010 -7.283 1.00 25.71 ? 150 THR A OG1 1 ATOM 1209 C CG2 . THR A 1 150 ? -1.875 53.445 -7.260 1.00 21.42 ? 150 THR A CG2 1 ATOM 1210 N N . ALA A 1 151 ? -4.499 55.171 -6.881 1.00 22.48 ? 151 ALA A N 1 ATOM 1211 C CA . ALA A 1 151 ? -5.830 54.826 -6.401 1.00 22.35 ? 151 ALA A CA 1 ATOM 1212 C C . ALA A 1 151 ? -5.972 53.345 -6.110 1.00 23.59 ? 151 ALA A C 1 ATOM 1213 O O . ALA A 1 151 ? -5.204 52.523 -6.618 1.00 23.86 ? 151 ALA A O 1 ATOM 1214 C CB . ALA A 1 151 ? -6.870 55.243 -7.424 1.00 20.33 ? 151 ALA A CB 1 ATOM 1215 N N . TRP A 1 152 ? -6.943 53.013 -5.267 1.00 24.20 ? 152 TRP A N 1 ATOM 1216 C CA . TRP A 1 152 ? -7.228 51.621 -4.966 1.00 26.14 ? 152 TRP A CA 1 ATOM 1217 C C . TRP A 1 152 ? -8.737 51.411 -5.132 1.00 27.20 ? 152 TRP A C 1 ATOM 1218 O O . TRP A 1 152 ? -9.546 52.291 -4.827 1.00 25.94 ? 152 TRP A O 1 ATOM 1219 C CB . TRP A 1 152 ? -6.704 51.219 -3.566 1.00 25.25 ? 152 TRP A CB 1 ATOM 1220 C CG . TRP A 1 152 ? -7.234 51.990 -2.390 1.00 27.39 ? 152 TRP A CG 1 ATOM 1221 C CD1 . TRP A 1 152 ? -8.296 51.651 -1.596 1.00 25.96 ? 152 TRP A CD1 1 ATOM 1222 C CD2 . TRP A 1 152 ? -6.729 53.230 -1.873 1.00 26.99 ? 152 TRP A CD2 1 ATOM 1223 N NE1 . TRP A 1 152 ? -8.483 52.602 -0.621 1.00 26.06 ? 152 TRP A NE1 1 ATOM 1224 C CE2 . TRP A 1 152 ? -7.537 53.584 -0.768 1.00 27.42 ? 152 TRP A CE2 1 ATOM 1225 C CE3 . TRP A 1 152 ? -5.676 54.079 -2.239 1.00 25.12 ? 152 TRP A CE3 1 ATOM 1226 C CZ2 . TRP A 1 152 ? -7.327 54.752 -0.023 1.00 28.40 ? 152 TRP A CZ2 1 ATOM 1227 C CZ3 . TRP A 1 152 ? -5.465 55.242 -1.499 1.00 27.43 ? 152 TRP A CZ3 1 ATOM 1228 C CH2 . TRP A 1 152 ? -6.291 55.567 -0.403 1.00 27.78 ? 152 TRP A CH2 1 ATOM 1229 N N . LEU A 1 153 ? -9.097 50.255 -5.683 1.00 29.58 ? 153 LEU A N 1 ATOM 1230 C CA . LEU A 1 153 ? -10.488 49.911 -5.945 1.00 31.17 ? 153 LEU A CA 1 ATOM 1231 C C . LEU A 1 153 ? -11.029 49.045 -4.821 1.00 33.21 ? 153 LEU A C 1 ATOM 1232 O O . LEU A 1 153 ? -10.520 47.953 -4.563 1.00 33.99 ? 153 LEU A O 1 ATOM 1233 C CB . LEU A 1 153 ? -10.594 49.171 -7.281 1.00 29.11 ? 153 LEU A CB 1 ATOM 1234 C CG . LEU A 1 153 ? -11.986 48.944 -7.874 1.00 29.35 ? 153 LEU A CG 1 ATOM 1235 C CD1 . LEU A 1 153 ? -12.694 50.277 -8.091 1.00 27.61 ? 153 LEU A CD1 1 ATOM 1236 C CD2 . LEU A 1 153 ? -11.842 48.204 -9.193 1.00 28.79 ? 153 LEU A CD2 1 ATOM 1237 N N . GLY A 1 154 ? -12.063 49.545 -4.155 1.00 35.42 ? 154 GLY A N 1 ATOM 1238 C CA . GLY A 1 154 ? -12.655 48.814 -3.052 1.00 37.86 ? 154 GLY A CA 1 ATOM 1239 C C . GLY A 1 154 ? -13.577 47.705 -3.510 1.00 39.09 ? 154 GLY A C 1 ATOM 1240 O O . GLY A 1 154 ? -13.976 47.667 -4.672 1.00 38.59 ? 154 GLY A O 1 ATOM 1241 N N . PRO A 1 155 ? -13.938 46.783 -2.609 1.00 41.21 ? 155 PRO A N 1 ATOM 1242 C CA . PRO A 1 155 ? -14.829 45.679 -2.976 1.00 41.23 ? 155 PRO A CA 1 ATOM 1243 C C . PRO A 1 155 ? -16.141 46.155 -3.610 1.00 41.46 ? 155 PRO A C 1 ATOM 1244 O O . PRO A 1 155 ? -16.750 45.443 -4.412 1.00 41.70 ? 155 PRO A O 1 ATOM 1245 C CB . PRO A 1 155 ? -15.036 44.949 -1.648 1.00 41.46 ? 155 PRO A CB 1 ATOM 1246 C CG . PRO A 1 155 ? -14.848 46.040 -0.616 1.00 42.10 ? 155 PRO A CG 1 ATOM 1247 C CD . PRO A 1 155 ? -13.661 46.784 -1.159 1.00 41.72 ? 155 PRO A CD 1 ATOM 1248 N N . ASP A 1 156 ? -16.560 47.370 -3.260 1.00 40.03 ? 156 ASP A N 1 ATOM 1249 C CA . ASP A 1 156 ? -17.795 47.951 -3.786 1.00 38.35 ? 156 ASP A CA 1 ATOM 1250 C C . ASP A 1 156 ? -17.613 48.569 -5.180 1.00 37.89 ? 156 ASP A C 1 ATOM 1251 O O . ASP A 1 156 ? -18.510 49.247 -5.695 1.00 37.39 ? 156 ASP A O 1 ATOM 1252 C CB . ASP A 1 156 ? -18.309 49.013 -2.815 1.00 37.92 ? 156 ASP A CB 1 ATOM 1253 C CG . ASP A 1 156 ? -17.331 50.157 -2.637 1.00 38.47 ? 156 ASP A CG 1 ATOM 1254 O OD1 . ASP A 1 156 ? -16.130 49.960 -2.916 1.00 38.36 ? 156 ASP A OD1 1 ATOM 1255 O OD2 . ASP A 1 156 ? -17.762 51.249 -2.208 1.00 39.97 ? 156 ASP A OD2 1 ATOM 1256 N N . GLY A 1 157 ? -16.450 48.342 -5.782 1.00 36.53 ? 157 GLY A N 1 ATOM 1257 C CA . GLY A 1 157 ? -16.185 48.876 -7.106 1.00 35.37 ? 157 GLY A CA 1 ATOM 1258 C C . GLY A 1 157 ? -15.992 50.381 -7.147 1.00 35.16 ? 157 GLY A C 1 ATOM 1259 O O . GLY A 1 157 ? -16.203 51.021 -8.182 1.00 34.85 ? 157 GLY A O 1 ATOM 1260 N N . VAL A 1 158 ? -15.590 50.956 -6.022 1.00 34.05 ? 158 VAL A N 1 ATOM 1261 C CA . VAL A 1 158 ? -15.367 52.390 -5.966 1.00 32.83 ? 158 VAL A CA 1 ATOM 1262 C C . VAL A 1 158 ? -13.891 52.688 -5.730 1.00 32.92 ? 158 VAL A C 1 ATOM 1263 O O . VAL A 1 158 ? -13.251 52.083 -4.866 1.00 32.61 ? 158 VAL A O 1 ATOM 1264 C CB . VAL A 1 158 ? -16.201 53.031 -4.850 1.00 32.85 ? 158 VAL A CB 1 ATOM 1265 C CG1 . VAL A 1 158 ? -15.997 54.539 -4.847 1.00 32.46 ? 158 VAL A CG1 1 ATOM 1266 C CG2 . VAL A 1 158 ? -17.660 52.693 -5.051 1.00 30.14 ? 158 VAL A CG2 1 ATOM 1267 N N . TRP A 1 159 ? -13.353 53.616 -6.513 1.00 31.96 ? 159 TRP A N 1 ATOM 1268 C CA . TRP A 1 159 ? -11.953 53.993 -6.393 1.00 30.77 ? 159 TRP A CA 1 ATOM 1269 C C . TRP A 1 159 ? -11.719 54.955 -5.243 1.00 30.88 ? 159 TRP A C 1 ATOM 1270 O O . TRP A 1 159 ? -12.571 55.789 -4.935 1.00 29.98 ? 159 TRP A O 1 ATOM 1271 C CB . TRP A 1 159 ? -11.460 54.669 -7.671 1.00 29.79 ? 159 TRP A CB 1 ATOM 1272 C CG . TRP A 1 159 ? -11.311 53.768 -8.840 1.00 30.83 ? 159 TRP A CG 1 ATOM 1273 C CD1 . TRP A 1 159 ? -12.142 53.679 -9.922 1.00 29.72 ? 159 TRP A CD1 1 ATOM 1274 C CD2 . TRP A 1 159 ? -10.242 52.848 -9.077 1.00 31.07 ? 159 TRP A CD2 1 ATOM 1275 N NE1 . TRP A 1 159 ? -11.650 52.767 -10.822 1.00 29.39 ? 159 TRP A NE1 1 ATOM 1276 C CE2 . TRP A 1 159 ? -10.485 52.239 -10.330 1.00 30.08 ? 159 TRP A CE2 1 ATOM 1277 C CE3 . TRP A 1 159 ? -9.098 52.481 -8.354 1.00 29.57 ? 159 TRP A CE3 1 ATOM 1278 C CZ2 . TRP A 1 159 ? -9.627 51.280 -10.877 1.00 28.85 ? 159 TRP A CZ2 1 ATOM 1279 C CZ3 . TRP A 1 159 ? -8.245 51.528 -8.898 1.00 29.46 ? 159 TRP A CZ3 1 ATOM 1280 C CH2 . TRP A 1 159 ? -8.516 50.938 -10.148 1.00 29.13 ? 159 TRP A CH2 1 ATOM 1281 N N . ARG A 1 160 ? -10.547 54.834 -4.624 1.00 30.38 ? 160 ARG A N 1 ATOM 1282 C CA . ARG A 1 160 ? -10.148 55.709 -3.531 1.00 29.72 ? 160 ARG A CA 1 ATOM 1283 C C . ARG A 1 160 ? -8.743 56.236 -3.780 1.00 29.30 ? 160 ARG A C 1 ATOM 1284 O O . ARG A 1 160 ? -7.881 55.516 -4.290 1.00 29.10 ? 160 ARG A O 1 ATOM 1285 C CB . ARG A 1 160 ? -10.137 54.970 -2.193 1.00 30.96 ? 160 ARG A CB 1 ATOM 1286 C CG . ARG A 1 160 ? -11.439 54.965 -1.423 1.00 32.80 ? 160 ARG A CG 1 ATOM 1287 C CD . ARG A 1 160 ? -12.376 53.882 -1.895 1.00 34.78 ? 160 ARG A CD 1 ATOM 1288 N NE . ARG A 1 160 ? -13.220 53.420 -0.798 1.00 38.04 ? 160 ARG A NE 1 ATOM 1289 C CZ . ARG A 1 160 ? -14.117 52.446 -0.898 1.00 40.04 ? 160 ARG A CZ 1 ATOM 1290 N NH1 . ARG A 1 160 ? -14.302 51.820 -2.053 1.00 40.36 ? 160 ARG A NH1 1 ATOM 1291 N NH2 . ARG A 1 160 ? -14.823 52.091 0.165 1.00 41.56 ? 160 ARG A NH2 1 ATOM 1292 N N . ILE A 1 161 ? -8.525 57.498 -3.431 1.00 28.29 ? 161 ILE A N 1 ATOM 1293 C CA . ILE A 1 161 ? -7.209 58.126 -3.541 1.00 28.11 ? 161 ILE A CA 1 ATOM 1294 C C . ILE A 1 161 ? -7.097 59.119 -2.395 1.00 29.19 ? 161 ILE A C 1 ATOM 1295 O O . ILE A 1 161 ? -8.107 59.520 -1.811 1.00 30.25 ? 161 ILE A O 1 ATOM 1296 C CB . ILE A 1 161 ? -7.004 58.937 -4.854 1.00 27.30 ? 161 ILE A CB 1 ATOM 1297 C CG1 . ILE A 1 161 ? -7.958 60.132 -4.895 1.00 25.88 ? 161 ILE A CG1 1 ATOM 1298 C CG2 . ILE A 1 161 ? -7.184 58.049 -6.054 1.00 27.29 ? 161 ILE A CG2 1 ATOM 1299 C CD1 . ILE A 1 161 ? -7.646 61.111 -6.012 1.00 25.30 ? 161 ILE A CD1 1 ATOM 1300 N N . VAL A 1 162 ? -5.874 59.503 -2.051 1.00 27.71 ? 162 VAL A N 1 ATOM 1301 C CA . VAL A 1 162 ? -5.695 60.504 -1.013 1.00 26.06 ? 162 VAL A CA 1 ATOM 1302 C C . VAL A 1 162 ? -4.906 61.643 -1.642 1.00 26.27 ? 162 VAL A C 1 ATOM 1303 O O . VAL A 1 162 ? -4.149 61.438 -2.596 1.00 25.37 ? 162 VAL A O 1 ATOM 1304 C CB . VAL A 1 162 ? -4.940 59.961 0.243 1.00 24.83 ? 162 VAL A CB 1 ATOM 1305 C CG1 . VAL A 1 162 ? -5.839 59.030 1.032 1.00 22.56 ? 162 VAL A CG1 1 ATOM 1306 C CG2 . VAL A 1 162 ? -3.667 59.253 -0.168 1.00 24.23 ? 162 VAL A CG2 1 ATOM 1307 N N . VAL A 1 163 ? -5.122 62.851 -1.140 1.00 25.84 ? 163 VAL A N 1 ATOM 1308 C CA . VAL A 1 163 ? -4.402 64.011 -1.638 1.00 26.52 ? 163 VAL A CA 1 ATOM 1309 C C . VAL A 1 163 ? -3.820 64.696 -0.414 1.00 27.13 ? 163 VAL A C 1 ATOM 1310 O O . VAL A 1 163 ? -4.481 64.793 0.618 1.00 26.47 ? 163 VAL A O 1 ATOM 1311 C CB . VAL A 1 163 ? -5.335 64.989 -2.393 1.00 25.54 ? 163 VAL A CB 1 ATOM 1312 C CG1 . VAL A 1 163 ? -4.544 66.195 -2.883 1.00 22.80 ? 163 VAL A CG1 1 ATOM 1313 C CG2 . VAL A 1 163 ? -5.985 64.279 -3.568 1.00 23.62 ? 163 VAL A CG2 1 ATOM 1314 N N . GLY A 1 164 ? -2.575 65.145 -0.527 1.00 27.04 ? 164 GLY A N 1 ATOM 1315 C CA . GLY A 1 164 ? -1.933 65.806 0.590 1.00 26.82 ? 164 GLY A CA 1 ATOM 1316 C C . GLY A 1 164 ? -2.421 67.224 0.790 1.00 27.68 ? 164 GLY A C 1 ATOM 1317 O O . GLY A 1 164 ? -3.220 67.746 0.013 1.00 27.36 ? 164 GLY A O 1 ATOM 1318 N N . GLY A 1 165 ? -1.919 67.852 1.843 1.00 29.14 ? 165 GLY A N 1 ATOM 1319 C CA . GLY A 1 165 ? -2.297 69.215 2.154 1.00 31.22 ? 165 GLY A CA 1 ATOM 1320 C C . GLY A 1 165 ? -2.477 69.346 3.649 1.00 32.23 ? 165 GLY A C 1 ATOM 1321 O O . GLY A 1 165 ? -1.983 68.516 4.411 1.00 32.43 ? 165 GLY A O 1 ATOM 1322 N N . ASP A 1 166 ? -3.181 70.386 4.073 1.00 33.52 ? 166 ASP A N 1 ATOM 1323 C CA . ASP A 1 166 ? -3.428 70.595 5.493 1.00 34.58 ? 166 ASP A CA 1 ATOM 1324 C C . ASP A 1 166 ? -4.590 71.544 5.704 1.00 33.42 ? 166 ASP A C 1 ATOM 1325 O O . ASP A 1 166 ? -4.910 72.367 4.846 1.00 31.30 ? 166 ASP A O 1 ATOM 1326 C CB . ASP A 1 166 ? -2.176 71.155 6.182 1.00 35.54 ? 166 ASP A CB 1 ATOM 1327 C CG . ASP A 1 166 ? -1.894 72.599 5.805 1.00 37.63 ? 166 ASP A CG 1 ATOM 1328 O OD1 . ASP A 1 166 ? -2.499 73.509 6.418 1.00 39.16 ? 166 ASP A OD1 1 ATOM 1329 O OD2 . ASP A 1 166 ? -1.075 72.826 4.889 1.00 37.11 ? 166 ASP A OD2 1 ATOM 1330 N N . ARG A 1 167 ? -5.229 71.409 6.853 1.00 34.37 ? 167 ARG A N 1 ATOM 1331 C CA . ARG A 1 167 ? -6.342 72.269 7.202 1.00 36.51 ? 167 ARG A CA 1 ATOM 1332 C C . ARG A 1 167 ? -5.931 72.949 8.504 1.00 37.25 ? 167 ARG A C 1 ATOM 1333 O O . ARG A 1 167 ? -5.899 72.316 9.561 1.00 37.95 ? 167 ARG A O 1 ATOM 1334 C CB . ARG A 1 167 ? -7.604 71.434 7.398 1.00 35.25 ? 167 ARG A CB 1 ATOM 1335 C CG . ARG A 1 167 ? -8.852 72.254 7.627 1.00 36.57 ? 167 ARG A CG 1 ATOM 1336 C CD . ARG A 1 167 ? -10.012 71.354 8.012 1.00 37.62 ? 167 ARG A CD 1 ATOM 1337 N NE . ARG A 1 167 ? -10.446 70.495 6.914 1.00 38.00 ? 167 ARG A NE 1 ATOM 1338 C CZ . ARG A 1 167 ? -11.073 70.937 5.829 1.00 39.17 ? 167 ARG A CZ 1 ATOM 1339 N NH1 . ARG A 1 167 ? -11.339 72.234 5.696 1.00 37.17 ? 167 ARG A NH1 1 ATOM 1340 N NH2 . ARG A 1 167 ? -11.436 70.081 4.878 1.00 38.65 ? 167 ARG A NH2 1 ATOM 1341 N N . ASP A 1 168 ? -5.596 74.233 8.416 1.00 38.00 ? 168 ASP A N 1 ATOM 1342 C CA . ASP A 1 168 ? -5.156 74.997 9.582 1.00 39.30 ? 168 ASP A CA 1 ATOM 1343 C C . ASP A 1 168 ? -3.877 74.394 10.141 1.00 39.13 ? 168 ASP A C 1 ATOM 1344 O O . ASP A 1 168 ? -3.777 74.118 11.337 1.00 38.96 ? 168 ASP A O 1 ATOM 1345 C CB . ASP A 1 168 ? -6.225 75.002 10.677 1.00 39.78 ? 168 ASP A CB 1 ATOM 1346 C CG . ASP A 1 168 ? -7.545 75.574 10.202 1.00 41.97 ? 168 ASP A CG 1 ATOM 1347 O OD1 . ASP A 1 168 ? -7.548 76.696 9.640 1.00 40.31 ? 168 ASP A OD1 1 ATOM 1348 O OD2 . ASP A 1 168 ? -8.578 74.895 10.401 1.00 42.66 ? 168 ASP A OD2 1 ATOM 1349 N N . ASN A 1 169 ? -2.911 74.176 9.257 1.00 38.43 ? 169 ASN A N 1 ATOM 1350 C CA . ASN A 1 169 ? -1.615 73.621 9.624 1.00 37.76 ? 169 ASN A CA 1 ATOM 1351 C C . ASN A 1 169 ? -1.650 72.169 10.115 1.00 36.97 ? 169 ASN A C 1 ATOM 1352 O O . ASN A 1 169 ? -0.642 71.648 10.597 1.00 35.75 ? 169 ASN A O 1 ATOM 1353 C CB . ASN A 1 169 ? -0.951 74.514 10.675 1.00 37.92 ? 169 ASN A CB 1 ATOM 1354 C CG . ASN A 1 169 ? 0.537 74.251 10.807 1.00 39.69 ? 169 ASN A CG 1 ATOM 1355 O OD1 . ASN A 1 169 ? 1.277 74.312 9.820 1.00 41.08 ? 169 ASN A OD1 1 ATOM 1356 N ND2 . ASN A 1 169 ? 0.984 73.960 12.027 1.00 39.79 ? 169 ASN A ND2 1 ATOM 1357 N N . ASN A 1 170 ? -2.800 71.513 9.993 1.00 36.34 ? 170 ASN A N 1 ATOM 1358 C CA . ASN A 1 170 ? -2.898 70.118 10.405 1.00 36.52 ? 170 ASN A CA 1 ATOM 1359 C C . ASN A 1 170 ? -2.795 69.196 9.196 1.00 36.55 ? 170 ASN A C 1 ATOM 1360 O O . ASN A 1 170 ? -3.653 69.215 8.314 1.00 36.59 ? 170 ASN A O 1 ATOM 1361 C CB . ASN A 1 170 ? -4.208 69.858 11.144 1.00 37.07 ? 170 ASN A CB 1 ATOM 1362 C CG . ASN A 1 170 ? -4.292 70.613 12.451 1.00 38.43 ? 170 ASN A CG 1 ATOM 1363 O OD1 . ASN A 1 170 ? -3.388 70.540 13.284 1.00 38.69 ? 170 ASN A OD1 1 ATOM 1364 N ND2 . ASN A 1 170 ? -5.381 71.344 12.639 1.00 38.64 ? 170 ASN A ND2 1 ATOM 1365 N N . GLY A 1 171 ? -1.724 68.402 9.164 1.00 36.68 ? 171 GLY A N 1 ATOM 1366 C CA . GLY A 1 171 ? -1.498 67.470 8.070 1.00 35.24 ? 171 GLY A CA 1 ATOM 1367 C C . GLY A 1 171 ? -2.745 66.701 7.685 1.00 34.42 ? 171 GLY A C 1 ATOM 1368 O O . GLY A 1 171 ? -3.475 66.207 8.544 1.00 34.18 ? 171 GLY A O 1 ATOM 1369 N N . MET A 1 172 ? -2.980 66.580 6.384 1.00 34.22 ? 172 MET A N 1 ATOM 1370 C CA . MET A 1 172 ? -4.169 65.896 5.896 1.00 33.59 ? 172 MET A CA 1 ATOM 1371 C C . MET A 1 172 ? -3.928 64.934 4.743 1.00 31.83 ? 172 MET A C 1 ATOM 1372 O O . MET A 1 172 ? -3.113 65.186 3.856 1.00 31.11 ? 172 MET A O 1 ATOM 1373 C CB . MET A 1 172 ? -5.203 66.925 5.423 1.00 34.74 ? 172 MET A CB 1 ATOM 1374 C CG . MET A 1 172 ? -5.802 67.805 6.499 1.00 34.52 ? 172 MET A CG 1 ATOM 1375 S SD . MET A 1 172 ? -7.049 66.938 7.460 1.00 37.08 ? 172 MET A SD 1 ATOM 1376 C CE . MET A 1 172 ? -6.481 67.247 9.109 1.00 37.87 ? 172 MET A CE 1 ATOM 1377 N N . ALA A 1 173 ? -4.661 63.830 4.772 1.00 30.23 ? 173 ALA A N 1 ATOM 1378 C CA . ALA A 1 173 ? -4.628 62.846 3.703 1.00 28.96 ? 173 ALA A CA 1 ATOM 1379 C C . ALA A 1 173 ? -6.089 62.848 3.245 1.00 29.28 ? 173 ALA A C 1 ATOM 1380 O O . ALA A 1 173 ? -6.859 61.953 3.590 1.00 29.03 ? 173 ALA A O 1 ATOM 1381 C CB . ALA A 1 173 ? -4.235 61.482 4.230 1.00 26.61 ? 173 ALA A CB 1 ATOM 1382 N N . PHE A 1 174 ? -6.470 63.890 2.506 1.00 29.15 ? 174 PHE A N 1 ATOM 1383 C CA . PHE A 1 174 ? -7.836 64.038 2.006 1.00 30.08 ? 174 PHE A CA 1 ATOM 1384 C C . PHE A 1 174 ? -8.227 62.829 1.167 1.00 30.69 ? 174 PHE A C 1 ATOM 1385 O O . PHE A 1 174 ? -7.491 62.427 0.268 1.00 31.75 ? 174 PHE A O 1 ATOM 1386 C CB . PHE A 1 174 ? -7.953 65.310 1.166 1.00 30.92 ? 174 PHE A CB 1 ATOM 1387 C CG . PHE A 1 174 ? -7.625 66.570 1.919 1.00 32.16 ? 174 PHE A CG 1 ATOM 1388 C CD1 . PHE A 1 174 ? -8.435 67.008 2.965 1.00 31.83 ? 174 PHE A CD1 1 ATOM 1389 C CD2 . PHE A 1 174 ? -6.497 67.322 1.583 1.00 33.19 ? 174 PHE A CD2 1 ATOM 1390 C CE1 . PHE A 1 174 ? -8.129 68.177 3.667 1.00 31.78 ? 174 PHE A CE1 1 ATOM 1391 C CE2 . PHE A 1 174 ? -6.179 68.494 2.278 1.00 33.24 ? 174 PHE A CE2 1 ATOM 1392 C CZ . PHE A 1 174 ? -6.997 68.923 3.322 1.00 32.71 ? 174 PHE A CZ 1 ATOM 1393 N N . LEU A 1 175 ? -9.391 62.257 1.464 1.00 29.74 ? 175 LEU A N 1 ATOM 1394 C CA . LEU A 1 175 ? -9.875 61.073 0.763 1.00 30.06 ? 175 LEU A CA 1 ATOM 1395 C C . LEU A 1 175 ? -10.965 61.382 -0.258 1.00 30.87 ? 175 LEU A C 1 ATOM 1396 O O . LEU A 1 175 ? -11.950 62.046 0.058 1.00 32.92 ? 175 LEU A O 1 ATOM 1397 C CB . LEU A 1 175 ? -10.402 60.068 1.789 1.00 29.88 ? 175 LEU A CB 1 ATOM 1398 C CG . LEU A 1 175 ? -10.978 58.740 1.295 1.00 31.08 ? 175 LEU A CG 1 ATOM 1399 C CD1 . LEU A 1 175 ? -9.882 57.895 0.674 1.00 31.60 ? 175 LEU A CD1 1 ATOM 1400 C CD2 . LEU A 1 175 ? -11.595 58.004 2.467 1.00 32.31 ? 175 LEU A CD2 1 ATOM 1401 N N . TYR A 1 176 ? -10.785 60.903 -1.486 1.00 31.01 ? 176 TYR A N 1 ATOM 1402 C CA . TYR A 1 176 ? -11.769 61.111 -2.545 1.00 30.64 ? 176 TYR A CA 1 ATOM 1403 C C . TYR A 1 176 ? -12.207 59.790 -3.157 1.00 31.14 ? 176 TYR A C 1 ATOM 1404 O O . TYR A 1 176 ? -11.452 58.816 -3.171 1.00 29.99 ? 176 TYR A O 1 ATOM 1405 C CB . TYR A 1 176 ? -11.209 62.013 -3.641 1.00 29.97 ? 176 TYR A CB 1 ATOM 1406 C CG . TYR A 1 176 ? -11.042 63.445 -3.209 1.00 29.84 ? 176 TYR A CG 1 ATOM 1407 C CD1 . TYR A 1 176 ? -10.008 63.821 -2.356 1.00 29.70 ? 176 TYR A CD1 1 ATOM 1408 C CD2 . TYR A 1 176 ? -11.938 64.420 -3.631 1.00 29.69 ? 176 TYR A CD2 1 ATOM 1409 C CE1 . TYR A 1 176 ? -9.871 65.138 -1.931 1.00 29.82 ? 176 TYR A CE1 1 ATOM 1410 C CE2 . TYR A 1 176 ? -11.812 65.736 -3.212 1.00 30.15 ? 176 TYR A CE2 1 ATOM 1411 C CZ . TYR A 1 176 ? -10.778 66.090 -2.362 1.00 30.47 ? 176 TYR A CZ 1 ATOM 1412 O OH . TYR A 1 176 ? -10.662 67.396 -1.944 1.00 30.89 ? 176 TYR A OH 1 ATOM 1413 N N . GLN A 1 177 ? -13.434 59.761 -3.662 1.00 32.50 ? 177 GLN A N 1 ATOM 1414 C CA . GLN A 1 177 ? -13.970 58.554 -4.271 1.00 34.45 ? 177 GLN A CA 1 ATOM 1415 C C . GLN A 1 177 ? -14.473 58.790 -5.684 1.00 34.14 ? 177 GLN A C 1 ATOM 1416 O O . GLN A 1 177 ? -14.854 59.905 -6.039 1.00 33.90 ? 177 GLN A O 1 ATOM 1417 C CB . GLN A 1 177 ? -15.093 58.004 -3.406 1.00 36.98 ? 177 GLN A CB 1 ATOM 1418 C CG . GLN A 1 177 ? -14.603 57.297 -2.162 1.00 44.67 ? 177 GLN A CG 1 ATOM 1419 C CD . GLN A 1 177 ? -15.570 57.432 -1.004 1.00 49.58 ? 177 GLN A CD 1 ATOM 1420 O OE1 . GLN A 1 177 ? -15.680 56.533 -0.160 1.00 51.64 ? 177 GLN A OE1 1 ATOM 1421 N NE2 . GLN A 1 177 ? -16.270 58.567 -0.947 1.00 51.41 ? 177 GLN A NE2 1 ATOM 1422 N N . SER A 1 178 ? -14.467 57.729 -6.486 1.00 33.65 ? 178 SER A N 1 ATOM 1423 C CA . SER A 1 178 ? -14.927 57.804 -7.869 1.00 32.83 ? 178 SER A CA 1 ATOM 1424 C C . SER A 1 178 ? -15.160 56.411 -8.444 1.00 33.46 ? 178 SER A C 1 ATOM 1425 O O . SER A 1 178 ? -14.555 55.438 -7.991 1.00 33.90 ? 178 SER A O 1 ATOM 1426 C CB . SER A 1 178 ? -13.890 58.540 -8.723 1.00 31.93 ? 178 SER A CB 1 ATOM 1427 O OG . SER A 1 178 ? -14.275 58.595 -10.083 1.00 31.16 ? 178 SER A OG 1 ATOM 1428 N N . THR A 1 179 ? -16.051 56.315 -9.427 1.00 33.37 ? 179 THR A N 1 ATOM 1429 C CA . THR A 1 179 ? -16.318 55.034 -10.079 1.00 32.73 ? 179 THR A CA 1 ATOM 1430 C C . THR A 1 179 ? -15.775 55.074 -11.500 1.00 32.33 ? 179 THR A C 1 ATOM 1431 O O . THR A 1 179 ? -15.364 54.048 -12.036 1.00 33.51 ? 179 THR A O 1 ATOM 1432 C CB . THR A 1 179 ? -17.826 54.696 -10.143 1.00 31.82 ? 179 THR A CB 1 ATOM 1433 O OG1 . THR A 1 179 ? -18.566 55.881 -10.444 1.00 33.64 ? 179 THR A OG1 1 ATOM 1434 C CG2 . THR A 1 179 ? -18.305 54.111 -8.830 1.00 30.28 ? 179 THR A CG2 1 ATOM 1435 N N . ASP A 1 180 ? -15.757 56.261 -12.099 1.00 31.41 ? 180 ASP A N 1 ATOM 1436 C CA . ASP A 1 180 ? -15.267 56.419 -13.466 1.00 32.09 ? 180 ASP A CA 1 ATOM 1437 C C . ASP A 1 180 ? -13.872 57.042 -13.538 1.00 32.49 ? 180 ASP A C 1 ATOM 1438 O O . ASP A 1 180 ? -13.332 57.249 -14.626 1.00 32.03 ? 180 ASP A O 1 ATOM 1439 C CB . ASP A 1 180 ? -16.238 57.280 -14.273 1.00 32.72 ? 180 ASP A CB 1 ATOM 1440 C CG . ASP A 1 180 ? -16.423 58.663 -13.677 1.00 34.14 ? 180 ASP A CG 1 ATOM 1441 O OD1 . ASP A 1 180 ? -15.695 59.004 -12.717 1.00 34.83 ? 180 ASP A OD1 1 ATOM 1442 O OD2 . ASP A 1 180 ? -17.293 59.411 -14.171 1.00 34.73 ? 180 ASP A OD2 1 ATOM 1443 N N . PHE A 1 181 ? -13.303 57.350 -12.375 1.00 31.98 ? 181 PHE A N 1 ATOM 1444 C CA . PHE A 1 181 ? -11.970 57.945 -12.283 1.00 30.79 ? 181 PHE A CA 1 ATOM 1445 C C . PHE A 1 181 ? -11.922 59.375 -12.827 1.00 31.26 ? 181 PHE A C 1 ATOM 1446 O O . PHE A 1 181 ? -10.848 59.980 -12.916 1.00 30.82 ? 181 PHE A O 1 ATOM 1447 C CB . PHE A 1 181 ? -10.944 57.080 -13.030 1.00 28.64 ? 181 PHE A CB 1 ATOM 1448 C CG . PHE A 1 181 ? -9.630 56.951 -12.314 1.00 27.91 ? 181 PHE A CG 1 ATOM 1449 C CD1 . PHE A 1 181 ? -9.513 56.131 -11.192 1.00 27.83 ? 181 PHE A CD1 1 ATOM 1450 C CD2 . PHE A 1 181 ? -8.520 57.676 -12.731 1.00 26.57 ? 181 PHE A CD2 1 ATOM 1451 C CE1 . PHE A 1 181 ? -8.308 56.041 -10.494 1.00 26.82 ? 181 PHE A CE1 1 ATOM 1452 C CE2 . PHE A 1 181 ? -7.312 57.595 -12.040 1.00 26.26 ? 181 PHE A CE2 1 ATOM 1453 C CZ . PHE A 1 181 ? -7.205 56.776 -10.920 1.00 26.26 ? 181 PHE A CZ 1 ATOM 1454 N N . VAL A 1 182 ? -13.088 59.917 -13.178 1.00 31.02 ? 182 VAL A N 1 ATOM 1455 C CA . VAL A 1 182 ? -13.178 61.273 -13.718 1.00 30.34 ? 182 VAL A CA 1 ATOM 1456 C C . VAL A 1 182 ? -13.924 62.202 -12.765 1.00 30.64 ? 182 VAL A C 1 ATOM 1457 O O . VAL A 1 182 ? -13.527 63.350 -12.572 1.00 29.45 ? 182 VAL A O 1 ATOM 1458 C CB . VAL A 1 182 ? -13.882 61.266 -15.096 1.00 30.13 ? 182 VAL A CB 1 ATOM 1459 C CG1 . VAL A 1 182 ? -13.991 62.681 -15.643 1.00 28.65 ? 182 VAL A CG1 1 ATOM 1460 C CG2 . VAL A 1 182 ? -13.102 60.390 -16.064 1.00 28.51 ? 182 VAL A CG2 1 ATOM 1461 N N . ASN A 1 183 ? -15.003 61.695 -12.177 1.00 32.34 ? 183 ASN A N 1 ATOM 1462 C CA . ASN A 1 183 ? -15.806 62.450 -11.221 1.00 34.67 ? 183 ASN A CA 1 ATOM 1463 C C . ASN A 1 183 ? -15.466 61.981 -9.820 1.00 35.58 ? 183 ASN A C 1 ATOM 1464 O O . ASN A 1 183 ? -15.793 60.856 -9.441 1.00 35.59 ? 183 ASN A O 1 ATOM 1465 C CB . ASN A 1 183 ? -17.289 62.224 -11.480 1.00 38.39 ? 183 ASN A CB 1 ATOM 1466 C CG . ASN A 1 183 ? -17.734 62.807 -12.799 1.00 43.89 ? 183 ASN A CG 1 ATOM 1467 O OD1 . ASN A 1 183 ? -17.912 64.021 -12.924 1.00 47.69 ? 183 ASN A OD1 1 ATOM 1468 N ND2 . ASN A 1 183 ? -17.897 61.950 -13.803 1.00 44.72 ? 183 ASN A ND2 1 ATOM 1469 N N . TRP A 1 184 ? -14.806 62.841 -9.054 1.00 35.72 ? 184 TRP A N 1 ATOM 1470 C CA . TRP A 1 184 ? -14.415 62.505 -7.692 1.00 35.77 ? 184 TRP A CA 1 ATOM 1471 C C . TRP A 1 184 ? -15.195 63.320 -6.671 1.00 37.59 ? 184 TRP A C 1 ATOM 1472 O O . TRP A 1 184 ? -15.490 64.494 -6.899 1.00 38.26 ? 184 TRP A O 1 ATOM 1473 C CB . TRP A 1 184 ? -12.923 62.759 -7.497 1.00 33.63 ? 184 TRP A CB 1 ATOM 1474 C CG . TRP A 1 184 ? -12.052 61.984 -8.416 1.00 31.39 ? 184 TRP A CG 1 ATOM 1475 C CD1 . TRP A 1 184 ? -11.711 62.311 -9.694 1.00 31.41 ? 184 TRP A CD1 1 ATOM 1476 C CD2 . TRP A 1 184 ? -11.403 60.743 -8.130 1.00 31.10 ? 184 TRP A CD2 1 ATOM 1477 N NE1 . TRP A 1 184 ? -10.884 61.349 -10.227 1.00 30.43 ? 184 TRP A NE1 1 ATOM 1478 C CE2 . TRP A 1 184 ? -10.679 60.373 -9.286 1.00 30.30 ? 184 TRP A CE2 1 ATOM 1479 C CE3 . TRP A 1 184 ? -11.365 59.902 -7.007 1.00 28.74 ? 184 TRP A CE3 1 ATOM 1480 C CZ2 . TRP A 1 184 ? -9.920 59.205 -9.352 1.00 29.58 ? 184 TRP A CZ2 1 ATOM 1481 C CZ3 . TRP A 1 184 ? -10.612 58.737 -7.072 1.00 28.19 ? 184 TRP A CZ3 1 ATOM 1482 C CH2 . TRP A 1 184 ? -9.900 58.400 -8.239 1.00 29.63 ? 184 TRP A CH2 1 ATOM 1483 N N . LYS A 1 185 ? -15.527 62.694 -5.546 1.00 39.08 ? 185 LYS A N 1 ATOM 1484 C CA . LYS A 1 185 ? -16.255 63.375 -4.485 1.00 41.64 ? 185 LYS A CA 1 ATOM 1485 C C . LYS A 1 185 ? -15.499 63.179 -3.185 1.00 41.35 ? 185 LYS A C 1 ATOM 1486 O O . LYS A 1 185 ? -15.188 62.051 -2.793 1.00 40.67 ? 185 LYS A O 1 ATOM 1487 C CB . LYS A 1 185 ? -17.677 62.819 -4.361 1.00 44.79 ? 185 LYS A CB 1 ATOM 1488 C CG . LYS A 1 185 ? -18.440 62.816 -5.683 1.00 53.64 ? 185 LYS A CG 1 ATOM 1489 C CD . LYS A 1 185 ? -19.877 62.311 -5.534 1.00 59.94 ? 185 LYS A CD 1 ATOM 1490 C CE . LYS A 1 185 ? -20.791 63.350 -4.879 1.00 63.46 ? 185 LYS A CE 1 ATOM 1491 N NZ . LYS A 1 185 ? -20.971 64.568 -5.729 1.00 64.68 ? 185 LYS A NZ 1 ATOM 1492 N N . ARG A 1 186 ? -15.191 64.290 -2.529 1.00 41.69 ? 186 ARG A N 1 ATOM 1493 C CA . ARG A 1 186 ? -14.456 64.268 -1.275 1.00 42.74 ? 186 ARG A CA 1 ATOM 1494 C C . ARG A 1 186 ? -15.240 63.562 -0.179 1.00 42.10 ? 186 ARG A C 1 ATOM 1495 O O . ARG A 1 186 ? -16.420 63.831 0.021 1.00 41.58 ? 186 ARG A O 1 ATOM 1496 C CB . ARG A 1 186 ? -14.150 65.695 -0.827 1.00 44.06 ? 186 ARG A CB 1 ATOM 1497 C CG . ARG A 1 186 ? -13.008 65.798 0.165 1.00 49.26 ? 186 ARG A CG 1 ATOM 1498 C CD . ARG A 1 186 ? -12.963 67.173 0.805 1.00 51.84 ? 186 ARG A CD 1 ATOM 1499 N NE . ARG A 1 186 ? -13.580 67.153 2.126 1.00 55.85 ? 186 ARG A NE 1 ATOM 1500 C CZ . ARG A 1 186 ? -14.416 68.080 2.582 1.00 56.35 ? 186 ARG A CZ 1 ATOM 1501 N NH1 . ARG A 1 186 ? -14.748 69.119 1.821 1.00 56.50 ? 186 ARG A NH1 1 ATOM 1502 N NH2 . ARG A 1 186 ? -14.919 67.960 3.803 1.00 56.21 ? 186 ARG A NH2 1 ATOM 1503 N N . TYR A 1 187 ? -14.581 62.654 0.526 1.00 42.94 ? 187 TYR A N 1 ATOM 1504 C CA . TYR A 1 187 ? -15.226 61.943 1.618 1.00 43.85 ? 187 TYR A CA 1 ATOM 1505 C C . TYR A 1 187 ? -15.311 62.921 2.786 1.00 45.10 ? 187 TYR A C 1 ATOM 1506 O O . TYR A 1 187 ? -14.457 63.796 2.935 1.00 44.69 ? 187 TYR A O 1 ATOM 1507 C CB . TYR A 1 187 ? -14.395 60.733 2.027 1.00 42.68 ? 187 TYR A CB 1 ATOM 1508 C CG . TYR A 1 187 ? -15.126 59.792 2.948 1.00 41.20 ? 187 TYR A CG 1 ATOM 1509 C CD1 . TYR A 1 187 ? -16.107 58.936 2.457 1.00 40.01 ? 187 TYR A CD1 1 ATOM 1510 C CD2 . TYR A 1 187 ? -14.843 59.763 4.312 1.00 41.76 ? 187 TYR A CD2 1 ATOM 1511 C CE1 . TYR A 1 187 ? -16.790 58.067 3.300 1.00 40.60 ? 187 TYR A CE1 1 ATOM 1512 C CE2 . TYR A 1 187 ? -15.519 58.898 5.169 1.00 42.16 ? 187 TYR A CE2 1 ATOM 1513 C CZ . TYR A 1 187 ? -16.492 58.051 4.656 1.00 42.73 ? 187 TYR A CZ 1 ATOM 1514 O OH . TYR A 1 187 ? -17.155 57.184 5.496 1.00 42.44 ? 187 TYR A OH 1 ATOM 1515 N N . ASP A 1 188 ? -16.335 62.774 3.616 1.00 47.50 ? 188 ASP A N 1 ATOM 1516 C CA . ASP A 1 188 ? -16.520 63.666 4.755 1.00 50.24 ? 188 ASP A CA 1 ATOM 1517 C C . ASP A 1 188 ? -15.266 63.875 5.617 1.00 48.94 ? 188 ASP A C 1 ATOM 1518 O O . ASP A 1 188 ? -14.837 65.010 5.840 1.00 48.68 ? 188 ASP A O 1 ATOM 1519 C CB . ASP A 1 188 ? -17.665 63.156 5.628 1.00 55.01 ? 188 ASP A CB 1 ATOM 1520 C CG . ASP A 1 188 ? -17.856 63.993 6.877 1.00 61.49 ? 188 ASP A CG 1 ATOM 1521 O OD1 . ASP A 1 188 ? -17.937 65.239 6.752 1.00 64.33 ? 188 ASP A OD1 1 ATOM 1522 O OD2 . ASP A 1 188 ? -17.925 63.409 7.985 1.00 64.17 ? 188 ASP A OD2 1 ATOM 1523 N N . GLN A 1 189 ? -14.688 62.780 6.104 1.00 47.69 ? 189 GLN A N 1 ATOM 1524 C CA . GLN A 1 189 ? -13.490 62.841 6.939 1.00 46.46 ? 189 GLN A CA 1 ATOM 1525 C C . GLN A 1 189 ? -12.246 62.396 6.164 1.00 43.84 ? 189 GLN A C 1 ATOM 1526 O O . GLN A 1 189 ? -12.352 61.673 5.177 1.00 44.72 ? 189 GLN A O 1 ATOM 1527 C CB . GLN A 1 189 ? -13.662 61.940 8.169 1.00 49.16 ? 189 GLN A CB 1 ATOM 1528 C CG . GLN A 1 189 ? -14.782 62.350 9.119 1.00 55.11 ? 189 GLN A CG 1 ATOM 1529 C CD . GLN A 1 189 ? -14.583 63.749 9.693 1.00 59.49 ? 189 GLN A CD 1 ATOM 1530 O OE1 . GLN A 1 189 ? -13.537 64.054 10.272 1.00 61.30 ? 189 GLN A OE1 1 ATOM 1531 N NE2 . GLN A 1 189 ? -15.592 64.605 9.539 1.00 60.82 ? 189 GLN A NE2 1 ATOM 1532 N N . PRO A 1 190 ? -11.052 62.846 6.591 1.00 40.87 ? 190 PRO A N 1 ATOM 1533 C CA . PRO A 1 190 ? -9.792 62.475 5.932 1.00 38.26 ? 190 PRO A CA 1 ATOM 1534 C C . PRO A 1 190 ? -9.483 61.016 6.237 1.00 35.89 ? 190 PRO A C 1 ATOM 1535 O O . PRO A 1 190 ? -10.022 60.459 7.192 1.00 36.11 ? 190 PRO A O 1 ATOM 1536 C CB . PRO A 1 190 ? -8.769 63.398 6.587 1.00 37.67 ? 190 PRO A CB 1 ATOM 1537 C CG . PRO A 1 190 ? -9.569 64.578 6.958 1.00 40.22 ? 190 PRO A CG 1 ATOM 1538 C CD . PRO A 1 190 ? -10.829 63.966 7.515 1.00 39.69 ? 190 PRO A CD 1 ATOM 1539 N N . LEU A 1 191 ? -8.624 60.395 5.436 1.00 33.36 ? 191 LEU A N 1 ATOM 1540 C CA . LEU A 1 191 ? -8.271 59.006 5.692 1.00 31.68 ? 191 LEU A CA 1 ATOM 1541 C C . LEU A 1 191 ? -7.463 58.989 6.981 1.00 31.64 ? 191 LEU A C 1 ATOM 1542 O O . LEU A 1 191 ? -7.606 58.091 7.810 1.00 31.31 ? 191 LEU A O 1 ATOM 1543 C CB . LEU A 1 191 ? -7.439 58.424 4.544 1.00 30.65 ? 191 LEU A CB 1 ATOM 1544 C CG . LEU A 1 191 ? -7.092 56.939 4.717 1.00 29.32 ? 191 LEU A CG 1 ATOM 1545 C CD1 . LEU A 1 191 ? -8.370 56.132 4.820 1.00 29.00 ? 191 LEU A CD1 1 ATOM 1546 C CD2 . LEU A 1 191 ? -6.244 56.450 3.556 1.00 29.30 ? 191 LEU A CD2 1 ATOM 1547 N N . SER A 1 192 ? -6.616 60.001 7.140 1.00 31.39 ? 192 SER A N 1 ATOM 1548 C CA . SER A 1 192 ? -5.782 60.133 8.325 1.00 30.43 ? 192 SER A CA 1 ATOM 1549 C C . SER A 1 192 ? -5.270 61.568 8.403 1.00 30.60 ? 192 SER A C 1 ATOM 1550 O O . SER A 1 192 ? -5.422 62.337 7.451 1.00 30.55 ? 192 SER A O 1 ATOM 1551 C CB . SER A 1 192 ? -4.613 59.155 8.259 1.00 29.91 ? 192 SER A CB 1 ATOM 1552 O OG . SER A 1 192 ? -3.845 59.220 9.444 1.00 31.10 ? 192 SER A OG 1 ATOM 1553 N N . SER A 1 193 ? -4.665 61.930 9.531 1.00 29.55 ? 193 SER A N 1 ATOM 1554 C CA . SER A 1 193 ? -4.164 63.287 9.708 1.00 30.80 ? 193 SER A CA 1 ATOM 1555 C C . SER A 1 193 ? -3.354 63.423 10.988 1.00 31.42 ? 193 SER A C 1 ATOM 1556 O O . SER A 1 193 ? -3.288 62.495 11.787 1.00 31.84 ? 193 SER A O 1 ATOM 1557 C CB . SER A 1 193 ? -5.338 64.259 9.763 1.00 31.86 ? 193 SER A CB 1 ATOM 1558 O OG . SER A 1 193 ? -6.169 63.962 10.876 1.00 32.83 ? 193 SER A OG 1 ATOM 1559 N N . ALA A 1 194 ? -2.744 64.589 11.180 1.00 32.04 ? 194 ALA A N 1 ATOM 1560 C CA . ALA A 1 194 ? -1.941 64.854 12.372 1.00 33.67 ? 194 ALA A CA 1 ATOM 1561 C C . ALA A 1 194 ? -1.906 66.350 12.655 1.00 34.33 ? 194 ALA A C 1 ATOM 1562 O O . ALA A 1 194 ? -1.843 67.165 11.737 1.00 34.59 ? 194 ALA A O 1 ATOM 1563 C CB . ALA A 1 194 ? -0.520 64.327 12.185 1.00 33.31 ? 194 ALA A CB 1 ATOM 1564 N N . ASP A 1 195 ? -1.939 66.705 13.931 1.00 35.46 ? 195 ASP A N 1 ATOM 1565 C CA . ASP A 1 195 ? -1.926 68.104 14.329 1.00 36.51 ? 195 ASP A CA 1 ATOM 1566 C C . ASP A 1 195 ? -0.598 68.814 14.140 1.00 35.77 ? 195 ASP A C 1 ATOM 1567 O O . ASP A 1 195 ? 0.466 68.215 14.257 1.00 36.29 ? 195 ASP A O 1 ATOM 1568 C CB . ASP A 1 195 ? -2.333 68.234 15.798 1.00 40.12 ? 195 ASP A CB 1 ATOM 1569 C CG . ASP A 1 195 ? -3.826 68.070 16.012 1.00 44.42 ? 195 ASP A CG 1 ATOM 1570 O OD1 . ASP A 1 195 ? -4.245 68.010 17.190 1.00 47.33 ? 195 ASP A OD1 1 ATOM 1571 O OD2 . ASP A 1 195 ? -4.582 68.011 15.013 1.00 45.54 ? 195 ASP A OD2 1 ATOM 1572 N N . ALA A 1 196 ? -0.690 70.106 13.842 1.00 35.08 ? 196 ALA A N 1 ATOM 1573 C CA . ALA A 1 196 ? 0.466 70.984 13.681 1.00 34.79 ? 196 ALA A CA 1 ATOM 1574 C C . ALA A 1 196 ? 1.688 70.425 12.966 1.00 34.47 ? 196 ALA A C 1 ATOM 1575 O O . ALA A 1 196 ? 2.819 70.778 13.310 1.00 34.59 ? 196 ALA A O 1 ATOM 1576 C CB . ALA A 1 196 ? 0.884 71.508 15.050 1.00 33.05 ? 196 ALA A CB 1 ATOM 1577 N N . THR A 1 197 ? 1.477 69.572 11.972 1.00 34.01 ? 197 THR A N 1 ATOM 1578 C CA . THR A 1 197 ? 2.601 68.998 11.241 1.00 33.26 ? 197 THR A CA 1 ATOM 1579 C C . THR A 1 197 ? 2.893 69.770 9.960 1.00 32.00 ? 197 THR A C 1 ATOM 1580 O O . THR A 1 197 ? 3.945 69.598 9.355 1.00 31.08 ? 197 THR A O 1 ATOM 1581 C CB . THR A 1 197 ? 2.338 67.524 10.862 1.00 33.06 ? 197 THR A CB 1 ATOM 1582 O OG1 . THR A 1 197 ? 1.163 67.446 10.051 1.00 33.26 ? 197 THR A OG1 1 ATOM 1583 C CG2 . THR A 1 197 ? 2.147 66.670 12.110 1.00 34.55 ? 197 THR A CG2 1 ATOM 1584 N N . GLY A 1 198 ? 1.972 70.639 9.560 1.00 32.08 ? 198 GLY A N 1 ATOM 1585 C CA . GLY A 1 198 ? 2.167 71.375 8.327 1.00 31.55 ? 198 GLY A CA 1 ATOM 1586 C C . GLY A 1 198 ? 1.632 70.509 7.199 1.00 33.09 ? 198 GLY A C 1 ATOM 1587 O O . GLY A 1 198 ? 1.040 69.452 7.456 1.00 31.96 ? 198 GLY A O 1 ATOM 1588 N N . THR A 1 199 ? 1.847 70.925 5.955 1.00 32.85 ? 199 THR A N 1 ATOM 1589 C CA . THR A 1 199 ? 1.340 70.169 4.808 1.00 32.93 ? 199 THR A CA 1 ATOM 1590 C C . THR A 1 199 ? 1.888 68.752 4.648 1.00 31.48 ? 199 THR A C 1 ATOM 1591 O O . THR A 1 199 ? 3.093 68.528 4.707 1.00 31.68 ? 199 THR A O 1 ATOM 1592 C CB . THR A 1 199 ? 1.608 70.917 3.485 1.00 34.54 ? 199 THR A CB 1 ATOM 1593 O OG1 . THR A 1 199 ? 1.036 72.229 3.545 1.00 38.18 ? 199 THR A OG1 1 ATOM 1594 C CG2 . THR A 1 199 ? 0.988 70.165 2.318 1.00 34.31 ? 199 THR A CG2 1 ATOM 1595 N N . TRP A 1 200 ? 0.988 67.797 4.445 1.00 28.83 ? 200 TRP A N 1 ATOM 1596 C CA . TRP A 1 200 ? 1.386 66.414 4.224 1.00 27.14 ? 200 TRP A CA 1 ATOM 1597 C C . TRP A 1 200 ? 1.694 66.301 2.740 1.00 27.61 ? 200 TRP A C 1 ATOM 1598 O O . TRP A 1 200 ? 0.807 66.469 1.904 1.00 27.70 ? 200 TRP A O 1 ATOM 1599 C CB . TRP A 1 200 ? 0.247 65.462 4.587 1.00 25.15 ? 200 TRP A CB 1 ATOM 1600 C CG . TRP A 1 200 ? 0.286 64.990 6.003 1.00 24.23 ? 200 TRP A CG 1 ATOM 1601 C CD1 . TRP A 1 200 ? 0.944 65.576 7.042 1.00 23.78 ? 200 TRP A CD1 1 ATOM 1602 C CD2 . TRP A 1 200 ? -0.381 63.841 6.546 1.00 23.56 ? 200 TRP A CD2 1 ATOM 1603 N NE1 . TRP A 1 200 ? 0.734 64.866 8.202 1.00 24.14 ? 200 TRP A NE1 1 ATOM 1604 C CE2 . TRP A 1 200 ? -0.076 63.796 7.927 1.00 24.46 ? 200 TRP A CE2 1 ATOM 1605 C CE3 . TRP A 1 200 ? -1.207 62.847 6.001 1.00 22.20 ? 200 TRP A CE3 1 ATOM 1606 C CZ2 . TRP A 1 200 ? -0.568 62.791 8.775 1.00 24.42 ? 200 TRP A CZ2 1 ATOM 1607 C CZ3 . TRP A 1 200 ? -1.699 61.848 6.842 1.00 22.76 ? 200 TRP A CZ3 1 ATOM 1608 C CH2 . TRP A 1 200 ? -1.375 61.829 8.214 1.00 24.48 ? 200 TRP A CH2 1 ATOM 1609 N N . GLU A 1 201 ? 2.948 66.024 2.407 1.00 26.72 ? 201 GLU A N 1 ATOM 1610 C CA . GLU A 1 201 ? 3.337 65.912 1.011 1.00 25.95 ? 201 GLU A CA 1 ATOM 1611 C C . GLU A 1 201 ? 3.501 64.473 0.545 1.00 26.68 ? 201 GLU A C 1 ATOM 1612 O O . GLU A 1 201 ? 3.943 63.610 1.305 1.00 27.77 ? 201 GLU A O 1 ATOM 1613 C CB . GLU A 1 201 ? 4.632 66.677 0.777 1.00 25.97 ? 201 GLU A CB 1 ATOM 1614 C CG . GLU A 1 201 ? 4.488 68.168 0.984 1.00 26.59 ? 201 GLU A CG 1 ATOM 1615 C CD . GLU A 1 201 ? 5.757 68.923 0.651 1.00 27.48 ? 201 GLU A CD 1 ATOM 1616 O OE1 . GLU A 1 201 ? 5.655 70.030 0.084 1.00 28.80 ? 201 GLU A OE1 1 ATOM 1617 O OE2 . GLU A 1 201 ? 6.856 68.417 0.961 1.00 27.18 ? 201 GLU A OE2 1 ATOM 1618 N N . CYS A 1 202 ? 3.130 64.227 -0.710 1.00 25.71 ? 202 CYS A N 1 ATOM 1619 C CA . CYS A 1 202 ? 3.236 62.911 -1.335 1.00 25.54 ? 202 CYS A CA 1 ATOM 1620 C C . CYS A 1 202 ? 2.757 61.739 -0.483 1.00 25.62 ? 202 CYS A C 1 ATOM 1621 O O . CYS A 1 202 ? 3.514 60.806 -0.208 1.00 25.28 ? 202 CYS A O 1 ATOM 1622 C CB . CYS A 1 202 ? 4.678 62.663 -1.766 1.00 24.96 ? 202 CYS A CB 1 ATOM 1623 S SG . CYS A 1 202 ? 5.316 63.938 -2.866 1.00 28.20 ? 202 CYS A SG 1 ATOM 1624 N N . PRO A 1 203 ? 1.482 61.766 -0.068 1.00 24.75 ? 203 PRO A N 1 ATOM 1625 C CA . PRO A 1 203 ? 0.903 60.698 0.752 1.00 23.48 ? 203 PRO A CA 1 ATOM 1626 C C . PRO A 1 203 ? 0.911 59.410 -0.057 1.00 24.12 ? 203 PRO A C 1 ATOM 1627 O O . PRO A 1 203 ? 0.731 59.436 -1.273 1.00 23.52 ? 203 PRO A O 1 ATOM 1628 C CB . PRO A 1 203 ? -0.531 61.169 0.991 1.00 23.34 ? 203 PRO A CB 1 ATOM 1629 C CG . PRO A 1 203 ? -0.497 62.633 0.688 1.00 26.31 ? 203 PRO A CG 1 ATOM 1630 C CD . PRO A 1 203 ? 0.458 62.750 -0.446 1.00 23.97 ? 203 PRO A CD 1 ATOM 1631 N N . ASP A 1 204 ? 1.121 58.289 0.609 1.00 23.79 ? 204 ASP A N 1 ATOM 1632 C CA . ASP A 1 204 ? 1.108 57.010 -0.075 1.00 24.02 ? 204 ASP A CA 1 ATOM 1633 C C . ASP A 1 204 ? 0.336 56.097 0.870 1.00 24.22 ? 204 ASP A C 1 ATOM 1634 O O . ASP A 1 204 ? 0.577 56.101 2.075 1.00 24.25 ? 204 ASP A O 1 ATOM 1635 C CB . ASP A 1 204 ? 2.541 56.512 -0.300 1.00 26.22 ? 204 ASP A CB 1 ATOM 1636 C CG . ASP A 1 204 ? 2.642 55.497 -1.435 1.00 28.63 ? 204 ASP A CG 1 ATOM 1637 O OD1 . ASP A 1 204 ? 1.597 55.181 -2.047 1.00 29.50 ? 204 ASP A OD1 1 ATOM 1638 O OD2 . ASP A 1 204 ? 3.766 55.020 -1.717 1.00 27.67 ? 204 ASP A OD2 1 ATOM 1639 N N . PHE A 1 205 ? -0.617 55.348 0.331 1.00 23.36 ? 205 PHE A N 1 ATOM 1640 C CA . PHE A 1 205 ? -1.435 54.454 1.137 1.00 22.69 ? 205 PHE A CA 1 ATOM 1641 C C . PHE A 1 205 ? -1.503 53.124 0.412 1.00 23.43 ? 205 PHE A C 1 ATOM 1642 O O . PHE A 1 205 ? -2.055 53.041 -0.683 1.00 23.50 ? 205 PHE A O 1 ATOM 1643 C CB . PHE A 1 205 ? -2.840 55.031 1.292 1.00 22.14 ? 205 PHE A CB 1 ATOM 1644 C CG . PHE A 1 205 ? -3.690 54.293 2.277 1.00 23.16 ? 205 PHE A CG 1 ATOM 1645 C CD1 . PHE A 1 205 ? -3.426 54.380 3.640 1.00 23.49 ? 205 PHE A CD1 1 ATOM 1646 C CD2 . PHE A 1 205 ? -4.741 53.488 1.843 1.00 23.04 ? 205 PHE A CD2 1 ATOM 1647 C CE1 . PHE A 1 205 ? -4.193 53.677 4.560 1.00 23.30 ? 205 PHE A CE1 1 ATOM 1648 C CE2 . PHE A 1 205 ? -5.516 52.779 2.754 1.00 23.98 ? 205 PHE A CE2 1 ATOM 1649 C CZ . PHE A 1 205 ? -5.243 52.872 4.117 1.00 23.16 ? 205 PHE A CZ 1 ATOM 1650 N N . TYR A 1 206 ? -0.951 52.081 1.022 1.00 23.20 ? 206 TYR A N 1 ATOM 1651 C CA . TYR A 1 206 ? -0.930 50.775 0.374 1.00 22.58 ? 206 TYR A CA 1 ATOM 1652 C C . TYR A 1 206 ? -0.919 49.601 1.347 1.00 23.14 ? 206 TYR A C 1 ATOM 1653 O O . TYR A 1 206 ? -0.646 49.762 2.536 1.00 23.44 ? 206 TYR A O 1 ATOM 1654 C CB . TYR A 1 206 ? 0.302 50.695 -0.536 1.00 21.30 ? 206 TYR A CB 1 ATOM 1655 C CG . TYR A 1 206 ? 1.598 50.951 0.201 1.00 21.00 ? 206 TYR A CG 1 ATOM 1656 C CD1 . TYR A 1 206 ? 2.252 49.920 0.875 1.00 20.46 ? 206 TYR A CD1 1 ATOM 1657 C CD2 . TYR A 1 206 ? 2.142 52.239 0.275 1.00 20.46 ? 206 TYR A CD2 1 ATOM 1658 C CE1 . TYR A 1 206 ? 3.409 50.159 1.606 1.00 19.58 ? 206 TYR A CE1 1 ATOM 1659 C CE2 . TYR A 1 206 ? 3.301 52.488 1.007 1.00 20.22 ? 206 TYR A CE2 1 ATOM 1660 C CZ . TYR A 1 206 ? 3.928 51.443 1.671 1.00 20.18 ? 206 TYR A CZ 1 ATOM 1661 O OH . TYR A 1 206 ? 5.069 51.676 2.408 1.00 19.20 ? 206 TYR A OH 1 ATOM 1662 N N . PRO A 1 207 ? -1.227 48.398 0.844 1.00 23.22 ? 207 PRO A N 1 ATOM 1663 C CA . PRO A 1 207 ? -1.246 47.198 1.674 1.00 22.42 ? 207 PRO A CA 1 ATOM 1664 C C . PRO A 1 207 ? 0.071 46.427 1.616 1.00 23.39 ? 207 PRO A C 1 ATOM 1665 O O . PRO A 1 207 ? 0.820 46.516 0.641 1.00 22.31 ? 207 PRO A O 1 ATOM 1666 C CB . PRO A 1 207 ? -2.381 46.400 1.064 1.00 22.74 ? 207 PRO A CB 1 ATOM 1667 C CG . PRO A 1 207 ? -2.164 46.651 -0.391 1.00 22.90 ? 207 PRO A CG 1 ATOM 1668 C CD . PRO A 1 207 ? -1.921 48.148 -0.435 1.00 22.50 ? 207 PRO A CD 1 ATOM 1669 N N . VAL A 1 208 ? 0.343 45.678 2.678 1.00 23.73 ? 208 VAL A N 1 ATOM 1670 C CA . VAL A 1 208 ? 1.528 44.839 2.766 1.00 23.17 ? 208 VAL A CA 1 ATOM 1671 C C . VAL A 1 208 ? 1.043 43.513 3.347 1.00 25.02 ? 208 VAL A C 1 ATOM 1672 O O . VAL A 1 208 ? 0.203 43.488 4.248 1.00 22.45 ? 208 VAL A O 1 ATOM 1673 C CB . VAL A 1 208 ? 2.621 45.450 3.685 1.00 22.10 ? 208 VAL A CB 1 ATOM 1674 C CG1 . VAL A 1 208 ? 3.078 46.780 3.127 1.00 20.28 ? 208 VAL A CG1 1 ATOM 1675 C CG2 . VAL A 1 208 ? 2.095 45.610 5.096 1.00 19.62 ? 208 VAL A CG2 1 ATOM 1676 N N . PRO A 1 209 ? 1.547 42.393 2.818 1.00 27.07 ? 209 PRO A N 1 ATOM 1677 C CA . PRO A 1 209 ? 1.154 41.062 3.290 1.00 28.45 ? 209 PRO A CA 1 ATOM 1678 C C . PRO A 1 209 ? 1.864 40.610 4.566 1.00 31.23 ? 209 PRO A C 1 ATOM 1679 O O . PRO A 1 209 ? 3.094 40.615 4.637 1.00 31.97 ? 209 PRO A O 1 ATOM 1680 C CB . PRO A 1 209 ? 1.490 40.174 2.098 1.00 27.99 ? 209 PRO A CB 1 ATOM 1681 C CG . PRO A 1 209 ? 2.733 40.821 1.561 1.00 28.00 ? 209 PRO A CG 1 ATOM 1682 C CD . PRO A 1 209 ? 2.400 42.300 1.617 1.00 26.26 ? 209 PRO A CD 1 ATOM 1683 N N . LEU A 1 210 ? 1.092 40.217 5.575 1.00 33.64 ? 210 LEU A N 1 ATOM 1684 C CA . LEU A 1 210 ? 1.690 39.749 6.817 1.00 35.41 ? 210 LEU A CA 1 ATOM 1685 C C . LEU A 1 210 ? 2.372 38.414 6.557 1.00 37.87 ? 210 LEU A C 1 ATOM 1686 O O . LEU A 1 210 ? 1.931 37.628 5.712 1.00 38.45 ? 210 LEU A O 1 ATOM 1687 C CB . LEU A 1 210 ? 0.628 39.599 7.906 1.00 34.45 ? 210 LEU A CB 1 ATOM 1688 C CG . LEU A 1 210 ? -0.016 40.910 8.359 1.00 35.42 ? 210 LEU A CG 1 ATOM 1689 C CD1 . LEU A 1 210 ? -0.976 40.638 9.500 1.00 33.53 ? 210 LEU A CD1 1 ATOM 1690 C CD2 . LEU A 1 210 ? 1.060 41.893 8.800 1.00 34.40 ? 210 LEU A CD2 1 ATOM 1691 N N . ASN A 1 211 ? 3.456 38.170 7.282 1.00 40.94 ? 211 ASN A N 1 ATOM 1692 C CA . ASN A 1 211 ? 4.232 36.942 7.132 1.00 45.73 ? 211 ASN A CA 1 ATOM 1693 C C . ASN A 1 211 ? 4.515 36.630 5.653 1.00 43.99 ? 211 ASN A C 1 ATOM 1694 O O . ASN A 1 211 ? 4.124 35.587 5.125 1.00 44.51 ? 211 ASN A O 1 ATOM 1695 C CB . ASN A 1 211 ? 3.508 35.756 7.786 1.00 51.69 ? 211 ASN A CB 1 ATOM 1696 C CG . ASN A 1 211 ? 4.453 34.602 8.103 1.00 57.32 ? 211 ASN A CG 1 ATOM 1697 O OD1 . ASN A 1 211 ? 4.025 33.453 8.259 1.00 60.63 ? 211 ASN A OD1 1 ATOM 1698 N ND2 . ASN A 1 211 ? 5.747 34.907 8.215 1.00 58.72 ? 211 ASN A ND2 1 ATOM 1699 N N . SER A 1 212 ? 5.196 37.563 4.997 1.00 41.40 ? 212 SER A N 1 ATOM 1700 C CA . SER A 1 212 ? 5.576 37.441 3.598 1.00 37.77 ? 212 SER A CA 1 ATOM 1701 C C . SER A 1 212 ? 6.574 38.547 3.311 1.00 37.09 ? 212 SER A C 1 ATOM 1702 O O . SER A 1 212 ? 6.477 39.635 3.875 1.00 37.57 ? 212 SER A O 1 ATOM 1703 C CB . SER A 1 212 ? 4.361 37.613 2.691 1.00 37.56 ? 212 SER A CB 1 ATOM 1704 O OG . SER A 1 212 ? 4.762 37.697 1.331 1.00 36.38 ? 212 SER A OG 1 ATOM 1705 N N . THR A 1 213 ? 7.538 38.276 2.443 1.00 34.97 ? 213 THR A N 1 ATOM 1706 C CA . THR A 1 213 ? 8.522 39.287 2.102 1.00 34.24 ? 213 THR A CA 1 ATOM 1707 C C . THR A 1 213 ? 8.229 39.808 0.701 1.00 34.90 ? 213 THR A C 1 ATOM 1708 O O . THR A 1 213 ? 9.111 40.337 0.025 1.00 35.17 ? 213 THR A O 1 ATOM 1709 C CB . THR A 1 213 ? 9.942 38.711 2.137 1.00 33.49 ? 213 THR A CB 1 ATOM 1710 O OG1 . THR A 1 213 ? 10.071 37.694 1.137 1.00 33.18 ? 213 THR A OG1 1 ATOM 1711 C CG2 . THR A 1 213 ? 10.230 38.117 3.501 1.00 31.86 ? 213 THR A CG2 1 ATOM 1712 N N . ASN A 1 214 ? 6.976 39.663 0.280 1.00 34.01 ? 214 ASN A N 1 ATOM 1713 C CA . ASN A 1 214 ? 6.561 40.099 -1.046 1.00 34.41 ? 214 ASN A CA 1 ATOM 1714 C C . ASN A 1 214 ? 5.672 41.328 -1.021 1.00 33.12 ? 214 ASN A C 1 ATOM 1715 O O . ASN A 1 214 ? 5.342 41.847 0.043 1.00 32.88 ? 214 ASN A O 1 ATOM 1716 C CB . ASN A 1 214 ? 5.835 38.960 -1.754 1.00 36.94 ? 214 ASN A CB 1 ATOM 1717 C CG . ASN A 1 214 ? 6.728 37.752 -1.975 1.00 40.03 ? 214 ASN A CG 1 ATOM 1718 O OD1 . ASN A 1 214 ? 6.246 36.625 -2.041 1.00 42.88 ? 214 ASN A OD1 1 ATOM 1719 N ND2 . ASN A 1 214 ? 8.033 37.984 -2.101 1.00 39.52 ? 214 ASN A ND2 1 ATOM 1720 N N . GLY A 1 215 ? 5.291 41.788 -2.209 1.00 31.78 ? 215 GLY A N 1 ATOM 1721 C CA . GLY A 1 215 ? 4.443 42.959 -2.319 1.00 29.65 ? 215 GLY A CA 1 ATOM 1722 C C . GLY A 1 215 ? 3.034 42.606 -2.745 1.00 29.34 ? 215 GLY A C 1 ATOM 1723 O O . GLY A 1 215 ? 2.753 41.473 -3.139 1.00 27.83 ? 215 GLY A O 1 ATOM 1724 N N . LEU A 1 216 ? 2.137 43.581 -2.666 1.00 29.66 ? 216 LEU A N 1 ATOM 1725 C CA . LEU A 1 216 ? 0.747 43.366 -3.045 1.00 29.73 ? 216 LEU A CA 1 ATOM 1726 C C . LEU A 1 216 ? 0.220 44.481 -3.916 1.00 30.59 ? 216 LEU A C 1 ATOM 1727 O O . LEU A 1 216 ? 0.682 45.619 -3.847 1.00 30.37 ? 216 LEU A O 1 ATOM 1728 C CB . LEU A 1 216 ? -0.142 43.283 -1.808 1.00 28.89 ? 216 LEU A CB 1 ATOM 1729 C CG . LEU A 1 216 ? -0.046 42.041 -0.936 1.00 28.81 ? 216 LEU A CG 1 ATOM 1730 C CD1 . LEU A 1 216 ? -0.856 42.257 0.324 1.00 27.13 ? 216 LEU A CD1 1 ATOM 1731 C CD2 . LEU A 1 216 ? -0.550 40.839 -1.712 1.00 27.18 ? 216 LEU A CD2 1 ATOM 1732 N N . ASP A 1 217 ? -0.762 44.144 -4.738 1.00 31.54 ? 217 ASP A N 1 ATOM 1733 C CA . ASP A 1 217 ? -1.385 45.136 -5.583 1.00 31.92 ? 217 ASP A CA 1 ATOM 1734 C C . ASP A 1 217 ? -2.063 46.109 -4.613 1.00 31.10 ? 217 ASP A C 1 ATOM 1735 O O . ASP A 1 217 ? -2.563 45.696 -3.566 1.00 31.03 ? 217 ASP A O 1 ATOM 1736 C CB . ASP A 1 217 ? -2.420 44.477 -6.486 1.00 33.51 ? 217 ASP A CB 1 ATOM 1737 C CG . ASP A 1 217 ? -3.176 45.484 -7.320 1.00 35.81 ? 217 ASP A CG 1 ATOM 1738 O OD1 . ASP A 1 217 ? -2.530 46.188 -8.128 1.00 36.66 ? 217 ASP A OD1 1 ATOM 1739 O OD2 . ASP A 1 217 ? -4.412 45.574 -7.157 1.00 35.73 ? 217 ASP A OD2 1 ATOM 1740 N N . THR A 1 218 ? -2.081 47.392 -4.954 1.00 30.19 ? 218 THR A N 1 ATOM 1741 C CA . THR A 1 218 ? -2.679 48.396 -4.084 1.00 30.01 ? 218 THR A CA 1 ATOM 1742 C C . THR A 1 218 ? -4.126 48.105 -3.676 1.00 29.58 ? 218 THR A C 1 ATOM 1743 O O . THR A 1 218 ? -4.560 48.533 -2.611 1.00 30.40 ? 218 THR A O 1 ATOM 1744 C CB . THR A 1 218 ? -2.619 49.797 -4.733 1.00 29.22 ? 218 THR A CB 1 ATOM 1745 O OG1 . THR A 1 218 ? -1.330 49.995 -5.322 1.00 30.48 ? 218 THR A OG1 1 ATOM 1746 C CG2 . THR A 1 218 ? -2.832 50.877 -3.689 1.00 27.62 ? 218 THR A CG2 1 ATOM 1747 N N . SER A 1 219 ? -4.866 47.367 -4.496 1.00 30.26 ? 219 SER A N 1 ATOM 1748 C CA . SER A 1 219 ? -6.264 47.070 -4.178 1.00 31.53 ? 219 SER A CA 1 ATOM 1749 C C . SER A 1 219 ? -6.545 45.808 -3.359 1.00 33.28 ? 219 SER A C 1 ATOM 1750 O O . SER A 1 219 ? -7.699 45.407 -3.215 1.00 34.92 ? 219 SER A O 1 ATOM 1751 C CB . SER A 1 219 ? -7.096 47.023 -5.458 1.00 29.15 ? 219 SER A CB 1 ATOM 1752 O OG . SER A 1 219 ? -7.257 48.315 -6.006 1.00 27.01 ? 219 SER A OG 1 ATOM 1753 N N . VAL A 1 220 ? -5.510 45.182 -2.817 1.00 34.15 ? 220 VAL A N 1 ATOM 1754 C CA . VAL A 1 220 ? -5.711 43.980 -2.020 1.00 35.88 ? 220 VAL A CA 1 ATOM 1755 C C . VAL A 1 220 ? -6.118 44.337 -0.593 1.00 38.23 ? 220 VAL A C 1 ATOM 1756 O O . VAL A 1 220 ? -5.752 45.392 -0.076 1.00 39.59 ? 220 VAL A O 1 ATOM 1757 C CB . VAL A 1 220 ? -4.426 43.134 -1.980 1.00 35.37 ? 220 VAL A CB 1 ATOM 1758 C CG1 . VAL A 1 220 ? -4.607 41.944 -1.056 1.00 32.95 ? 220 VAL A CG1 1 ATOM 1759 C CG2 . VAL A 1 220 ? -4.075 42.675 -3.384 1.00 34.96 ? 220 VAL A CG2 1 ATOM 1760 N N . TYR A 1 221 ? -6.891 43.461 0.038 1.00 40.86 ? 221 TYR A N 1 ATOM 1761 C CA . TYR A 1 221 ? -7.330 43.681 1.411 1.00 44.32 ? 221 TYR A CA 1 ATOM 1762 C C . TYR A 1 221 ? -7.616 42.333 2.060 1.00 42.68 ? 221 TYR A C 1 ATOM 1763 O O . TYR A 1 221 ? -7.744 41.323 1.372 1.00 43.33 ? 221 TYR A O 1 ATOM 1764 C CB . TYR A 1 221 ? -8.575 44.577 1.440 1.00 50.21 ? 221 TYR A CB 1 ATOM 1765 C CG . TYR A 1 221 ? -9.735 44.035 0.645 1.00 58.52 ? 221 TYR A CG 1 ATOM 1766 C CD1 . TYR A 1 221 ? -10.485 42.951 1.116 1.00 61.89 ? 221 TYR A CD1 1 ATOM 1767 C CD2 . TYR A 1 221 ? -10.063 44.575 -0.601 1.00 61.90 ? 221 TYR A CD2 1 ATOM 1768 C CE1 . TYR A 1 221 ? -11.532 42.411 0.365 1.00 63.79 ? 221 TYR A CE1 1 ATOM 1769 C CE2 . TYR A 1 221 ? -11.111 44.041 -1.363 1.00 65.12 ? 221 TYR A CE2 1 ATOM 1770 C CZ . TYR A 1 221 ? -11.837 42.958 -0.871 1.00 65.41 ? 221 TYR A CZ 1 ATOM 1771 O OH . TYR A 1 221 ? -12.858 42.416 -1.618 1.00 66.77 ? 221 TYR A OH 1 ATOM 1772 N N . GLY A 1 222 ? -7.703 42.311 3.381 1.00 41.35 ? 222 GLY A N 1 ATOM 1773 C CA . GLY A 1 222 ? -7.953 41.057 4.060 1.00 40.41 ? 222 GLY A CA 1 ATOM 1774 C C . GLY A 1 222 ? -7.376 41.045 5.457 1.00 40.54 ? 222 GLY A C 1 ATOM 1775 O O . GLY A 1 222 ? -6.698 41.987 5.870 1.00 41.24 ? 222 GLY A O 1 ATOM 1776 N N . GLY A 1 223 ? -7.639 39.970 6.188 1.00 40.10 ? 223 GLY A N 1 ATOM 1777 C CA . GLY A 1 223 ? -7.152 39.874 7.550 1.00 39.73 ? 223 GLY A CA 1 ATOM 1778 C C . GLY A 1 223 ? -5.659 39.671 7.635 1.00 40.02 ? 223 GLY A C 1 ATOM 1779 O O . GLY A 1 223 ? -5.023 40.070 8.611 1.00 40.62 ? 223 GLY A O 1 ATOM 1780 N N . SER A 1 224 ? -5.100 39.045 6.609 1.00 40.26 ? 224 SER A N 1 ATOM 1781 C CA . SER A 1 224 ? -3.670 38.774 6.557 1.00 41.33 ? 224 SER A CA 1 ATOM 1782 C C . SER A 1 224 ? -2.948 39.926 5.864 1.00 39.62 ? 224 SER A C 1 ATOM 1783 O O . SER A 1 224 ? -1.846 39.772 5.333 1.00 38.87 ? 224 SER A O 1 ATOM 1784 C CB . SER A 1 224 ? -3.438 37.476 5.794 1.00 43.49 ? 224 SER A CB 1 ATOM 1785 O OG . SER A 1 224 ? -4.174 37.506 4.580 1.00 48.64 ? 224 SER A OG 1 ATOM 1786 N N . VAL A 1 225 ? -3.589 41.085 5.881 1.00 37.95 ? 225 VAL A N 1 ATOM 1787 C CA . VAL A 1 225 ? -3.039 42.277 5.264 1.00 35.96 ? 225 VAL A CA 1 ATOM 1788 C C . VAL A 1 225 ? -3.172 43.479 6.194 1.00 35.15 ? 225 VAL A C 1 ATOM 1789 O O . VAL A 1 225 ? -4.155 43.617 6.925 1.00 35.60 ? 225 VAL A O 1 ATOM 1790 C CB . VAL A 1 225 ? -3.774 42.603 3.943 1.00 35.80 ? 225 VAL A CB 1 ATOM 1791 C CG1 . VAL A 1 225 ? -3.302 43.937 3.393 1.00 35.10 ? 225 VAL A CG1 1 ATOM 1792 C CG2 . VAL A 1 225 ? -3.539 41.501 2.931 1.00 35.63 ? 225 VAL A CG2 1 ATOM 1793 N N . ARG A 1 226 ? -2.165 44.340 6.162 1.00 33.28 ? 226 ARG A N 1 ATOM 1794 C CA . ARG A 1 226 ? -2.165 45.558 6.951 1.00 30.83 ? 226 ARG A CA 1 ATOM 1795 C C . ARG A 1 226 ? -1.850 46.682 5.978 1.00 29.45 ? 226 ARG A C 1 ATOM 1796 O O . ARG A 1 226 ? -1.284 46.443 4.907 1.00 27.51 ? 226 ARG A O 1 ATOM 1797 C CB . ARG A 1 226 ? -1.102 45.497 8.050 1.00 32.00 ? 226 ARG A CB 1 ATOM 1798 C CG . ARG A 1 226 ? -1.453 44.566 9.190 1.00 33.04 ? 226 ARG A CG 1 ATOM 1799 C CD . ARG A 1 226 ? -2.682 45.057 9.943 1.00 35.63 ? 226 ARG A CD 1 ATOM 1800 N NE . ARG A 1 226 ? -3.087 44.110 10.982 1.00 37.58 ? 226 ARG A NE 1 ATOM 1801 C CZ . ARG A 1 226 ? -3.700 42.954 10.748 1.00 38.15 ? 226 ARG A CZ 1 ATOM 1802 N NH1 . ARG A 1 226 ? -3.997 42.589 9.507 1.00 37.51 ? 226 ARG A NH1 1 ATOM 1803 N NH2 . ARG A 1 226 ? -4.007 42.152 11.759 1.00 39.14 ? 226 ARG A NH2 1 ATOM 1804 N N . HIS A 1 227 ? -2.225 47.903 6.335 1.00 27.89 ? 227 HIS A N 1 ATOM 1805 C CA . HIS A 1 227 ? -1.963 49.034 5.465 1.00 27.71 ? 227 HIS A CA 1 ATOM 1806 C C . HIS A 1 227 ? -0.945 50.008 6.030 1.00 27.85 ? 227 HIS A C 1 ATOM 1807 O O . HIS A 1 227 ? -0.794 50.150 7.248 1.00 27.56 ? 227 HIS A O 1 ATOM 1808 C CB . HIS A 1 227 ? -3.262 49.774 5.147 1.00 29.01 ? 227 HIS A CB 1 ATOM 1809 C CG . HIS A 1 227 ? -4.035 49.171 4.014 1.00 30.19 ? 227 HIS A CG 1 ATOM 1810 N ND1 . HIS A 1 227 ? -4.591 47.911 4.077 1.00 30.44 ? 227 HIS A ND1 1 ATOM 1811 C CD2 . HIS A 1 227 ? -4.320 49.648 2.780 1.00 29.43 ? 227 HIS A CD2 1 ATOM 1812 C CE1 . HIS A 1 227 ? -5.182 47.637 2.928 1.00 30.37 ? 227 HIS A CE1 1 ATOM 1813 N NE2 . HIS A 1 227 ? -5.032 48.674 2.123 1.00 30.70 ? 227 HIS A NE2 1 ATOM 1814 N N . VAL A 1 228 ? -0.231 50.661 5.122 1.00 26.60 ? 228 VAL A N 1 ATOM 1815 C CA . VAL A 1 228 ? 0.774 51.642 5.487 1.00 25.53 ? 228 VAL A CA 1 ATOM 1816 C C . VAL A 1 228 ? 0.281 53.012 5.040 1.00 25.99 ? 228 VAL A C 1 ATOM 1817 O O . VAL A 1 228 ? -0.160 53.186 3.903 1.00 26.23 ? 228 VAL A O 1 ATOM 1818 C CB . VAL A 1 228 ? 2.123 51.353 4.793 1.00 24.49 ? 228 VAL A CB 1 ATOM 1819 C CG1 . VAL A 1 228 ? 3.158 52.373 5.228 1.00 23.91 ? 228 VAL A CG1 1 ATOM 1820 C CG2 . VAL A 1 228 ? 2.587 49.948 5.120 1.00 24.70 ? 228 VAL A CG2 1 ATOM 1821 N N . MET A 1 229 ? 0.325 53.973 5.953 1.00 25.86 ? 229 MET A N 1 ATOM 1822 C CA . MET A 1 229 ? -0.077 55.340 5.657 1.00 25.21 ? 229 MET A CA 1 ATOM 1823 C C . MET A 1 229 ? 1.225 56.126 5.735 1.00 25.25 ? 229 MET A C 1 ATOM 1824 O O . MET A 1 229 ? 1.794 56.299 6.814 1.00 25.74 ? 229 MET A O 1 ATOM 1825 C CB . MET A 1 229 ? -1.071 55.845 6.705 1.00 27.16 ? 229 MET A CB 1 ATOM 1826 C CG . MET A 1 229 ? -1.401 57.330 6.621 1.00 28.93 ? 229 MET A CG 1 ATOM 1827 S SD . MET A 1 229 ? -2.387 57.817 5.187 1.00 34.36 ? 229 MET A SD 1 ATOM 1828 C CE . MET A 1 229 ? -1.133 58.557 4.140 1.00 32.94 ? 229 MET A CE 1 ATOM 1829 N N . LYS A 1 230 ? 1.706 56.572 4.580 1.00 24.07 ? 230 LYS A N 1 ATOM 1830 C CA . LYS A 1 230 ? 2.952 57.320 4.501 1.00 22.87 ? 230 LYS A CA 1 ATOM 1831 C C . LYS A 1 230 ? 2.697 58.765 4.103 1.00 23.79 ? 230 LYS A C 1 ATOM 1832 O O . LYS A 1 230 ? 1.852 59.044 3.252 1.00 24.58 ? 230 LYS A O 1 ATOM 1833 C CB . LYS A 1 230 ? 3.890 56.649 3.486 1.00 21.00 ? 230 LYS A CB 1 ATOM 1834 C CG . LYS A 1 230 ? 5.177 57.405 3.192 1.00 19.10 ? 230 LYS A CG 1 ATOM 1835 C CD . LYS A 1 230 ? 4.982 58.501 2.151 1.00 20.82 ? 230 LYS A CD 1 ATOM 1836 C CE . LYS A 1 230 ? 6.242 59.352 1.998 1.00 19.46 ? 230 LYS A CE 1 ATOM 1837 N NZ . LYS A 1 230 ? 6.120 60.364 0.913 1.00 14.40 ? 230 LYS A NZ 1 ATOM 1838 N N . ALA A 1 231 ? 3.430 59.681 4.725 1.00 23.82 ? 231 ALA A N 1 ATOM 1839 C CA . ALA A 1 231 ? 3.297 61.098 4.409 1.00 24.43 ? 231 ALA A CA 1 ATOM 1840 C C . ALA A 1 231 ? 4.588 61.835 4.730 1.00 25.25 ? 231 ALA A C 1 ATOM 1841 O O . ALA A 1 231 ? 5.277 61.523 5.707 1.00 25.05 ? 231 ALA A O 1 ATOM 1842 C CB . ALA A 1 231 ? 2.141 61.714 5.182 1.00 23.03 ? 231 ALA A CB 1 ATOM 1843 N N . GLY A 1 232 ? 4.916 62.810 3.892 1.00 25.48 ? 232 GLY A N 1 ATOM 1844 C CA . GLY A 1 232 ? 6.116 63.583 4.110 1.00 25.88 ? 232 GLY A CA 1 ATOM 1845 C C . GLY A 1 232 ? 5.773 64.926 4.720 1.00 26.64 ? 232 GLY A C 1 ATOM 1846 O O . GLY A 1 232 ? 4.904 65.637 4.220 1.00 27.24 ? 232 GLY A O 1 ATOM 1847 N N . PHE A 1 233 ? 6.432 65.260 5.822 1.00 26.61 ? 233 PHE A N 1 ATOM 1848 C CA . PHE A 1 233 ? 6.220 66.543 6.476 1.00 25.92 ? 233 PHE A CA 1 ATOM 1849 C C . PHE A 1 233 ? 7.374 66.840 7.421 1.00 26.05 ? 233 PHE A C 1 ATOM 1850 O O . PHE A 1 233 ? 8.083 65.934 7.870 1.00 24.20 ? 233 PHE A O 1 ATOM 1851 C CB . PHE A 1 233 ? 4.866 66.594 7.207 1.00 24.69 ? 233 PHE A CB 1 ATOM 1852 C CG . PHE A 1 233 ? 4.728 65.608 8.323 1.00 24.61 ? 233 PHE A CG 1 ATOM 1853 C CD1 . PHE A 1 233 ? 5.312 65.851 9.562 1.00 24.45 ? 233 PHE A CD1 1 ATOM 1854 C CD2 . PHE A 1 233 ? 4.002 64.434 8.138 1.00 24.37 ? 233 PHE A CD2 1 ATOM 1855 C CE1 . PHE A 1 233 ? 5.177 64.937 10.607 1.00 24.81 ? 233 PHE A CE1 1 ATOM 1856 C CE2 . PHE A 1 233 ? 3.859 63.513 9.171 1.00 24.91 ? 233 PHE A CE2 1 ATOM 1857 C CZ . PHE A 1 233 ? 4.448 63.764 10.411 1.00 25.82 ? 233 PHE A CZ 1 ATOM 1858 N N . GLU A 1 234 ? 7.554 68.125 7.699 1.00 25.72 ? 234 GLU A N 1 ATOM 1859 C CA . GLU A 1 234 ? 8.631 68.606 8.545 1.00 26.76 ? 234 GLU A CA 1 ATOM 1860 C C . GLU A 1 234 ? 9.977 68.109 8.029 1.00 25.70 ? 234 GLU A C 1 ATOM 1861 O O . GLU A 1 234 ? 10.897 67.847 8.802 1.00 26.21 ? 234 GLU A O 1 ATOM 1862 C CB . GLU A 1 234 ? 8.409 68.196 10.002 1.00 29.54 ? 234 GLU A CB 1 ATOM 1863 C CG . GLU A 1 234 ? 7.081 68.702 10.536 1.00 35.51 ? 234 GLU A CG 1 ATOM 1864 C CD . GLU A 1 234 ? 6.939 68.577 12.040 1.00 37.61 ? 234 GLU A CD 1 ATOM 1865 O OE1 . GLU A 1 234 ? 7.235 67.495 12.590 1.00 39.92 ? 234 GLU A OE1 1 ATOM 1866 O OE2 . GLU A 1 234 ? 6.511 69.567 12.670 1.00 39.29 ? 234 GLU A OE2 1 ATOM 1867 N N . GLY A 1 235 ? 10.071 67.971 6.709 1.00 23.51 ? 235 GLY A N 1 ATOM 1868 C CA . GLY A 1 235 ? 11.315 67.560 6.081 1.00 22.88 ? 235 GLY A CA 1 ATOM 1869 C C . GLY A 1 235 ? 11.641 66.090 5.937 1.00 23.67 ? 235 GLY A C 1 ATOM 1870 O O . GLY A 1 235 ? 12.694 65.753 5.393 1.00 23.91 ? 235 GLY A O 1 ATOM 1871 N N . HIS A 1 236 ? 10.759 65.211 6.401 1.00 23.59 ? 236 HIS A N 1 ATOM 1872 C CA . HIS A 1 236 ? 11.021 63.779 6.306 1.00 23.01 ? 236 HIS A CA 1 ATOM 1873 C C . HIS A 1 236 ? 9.810 62.969 5.924 1.00 22.32 ? 236 HIS A C 1 ATOM 1874 O O . HIS A 1 236 ? 8.679 63.447 5.999 1.00 24.90 ? 236 HIS A O 1 ATOM 1875 C CB . HIS A 1 236 ? 11.559 63.261 7.631 1.00 23.15 ? 236 HIS A CB 1 ATOM 1876 C CG . HIS A 1 236 ? 12.823 63.929 8.053 1.00 25.08 ? 236 HIS A CG 1 ATOM 1877 N ND1 . HIS A 1 236 ? 12.953 64.586 9.255 1.00 26.00 ? 236 HIS A ND1 1 ATOM 1878 C CD2 . HIS A 1 236 ? 14.009 64.070 7.415 1.00 25.19 ? 236 HIS A CD2 1 ATOM 1879 C CE1 . HIS A 1 236 ? 14.163 65.108 9.341 1.00 24.45 ? 236 HIS A CE1 1 ATOM 1880 N NE2 . HIS A 1 236 ? 14.823 64.809 8.237 1.00 24.45 ? 236 HIS A NE2 1 ATOM 1881 N N . ASP A 1 237 ? 10.060 61.738 5.502 1.00 21.02 ? 237 ASP A N 1 ATOM 1882 C CA . ASP A 1 237 ? 8.986 60.840 5.134 1.00 21.10 ? 237 ASP A CA 1 ATOM 1883 C C . ASP A 1 237 ? 8.693 59.922 6.308 1.00 20.43 ? 237 ASP A C 1 ATOM 1884 O O . ASP A 1 237 ? 9.563 59.175 6.754 1.00 19.79 ? 237 ASP A O 1 ATOM 1885 C CB . ASP A 1 237 ? 9.365 60.022 3.903 1.00 21.81 ? 237 ASP A CB 1 ATOM 1886 C CG . ASP A 1 237 ? 9.279 60.831 2.623 1.00 25.62 ? 237 ASP A CG 1 ATOM 1887 O OD1 . ASP A 1 237 ? 8.640 61.908 2.637 1.00 27.03 ? 237 ASP A OD1 1 ATOM 1888 O OD2 . ASP A 1 237 ? 9.840 60.388 1.599 1.00 25.52 ? 237 ASP A OD2 1 ATOM 1889 N N . TRP A 1 238 ? 7.469 59.999 6.818 1.00 19.99 ? 238 TRP A N 1 ATOM 1890 C CA . TRP A 1 238 ? 7.066 59.173 7.945 1.00 21.36 ? 238 TRP A CA 1 ATOM 1891 C C . TRP A 1 238 ? 6.006 58.189 7.490 1.00 21.68 ? 238 TRP A C 1 ATOM 1892 O O . TRP A 1 238 ? 5.359 58.388 6.460 1.00 22.50 ? 238 TRP A O 1 ATOM 1893 C CB . TRP A 1 238 ? 6.486 60.030 9.078 1.00 21.09 ? 238 TRP A CB 1 ATOM 1894 C CG . TRP A 1 238 ? 7.256 61.285 9.355 1.00 22.81 ? 238 TRP A CG 1 ATOM 1895 C CD1 . TRP A 1 238 ? 7.162 62.479 8.680 1.00 21.63 ? 238 TRP A CD1 1 ATOM 1896 C CD2 . TRP A 1 238 ? 8.266 61.467 10.353 1.00 22.00 ? 238 TRP A CD2 1 ATOM 1897 N NE1 . TRP A 1 238 ? 8.055 63.385 9.199 1.00 22.49 ? 238 TRP A NE1 1 ATOM 1898 C CE2 . TRP A 1 238 ? 8.747 62.792 10.227 1.00 22.46 ? 238 TRP A CE2 1 ATOM 1899 C CE3 . TRP A 1 238 ? 8.815 60.638 11.345 1.00 21.84 ? 238 TRP A CE3 1 ATOM 1900 C CZ2 . TRP A 1 238 ? 9.751 63.307 11.053 1.00 19.82 ? 238 TRP A CZ2 1 ATOM 1901 C CZ3 . TRP A 1 238 ? 9.816 61.153 12.168 1.00 20.65 ? 238 TRP A CZ3 1 ATOM 1902 C CH2 . TRP A 1 238 ? 10.272 62.476 12.013 1.00 19.80 ? 238 TRP A CH2 1 ATOM 1903 N N . TYR A 1 239 ? 5.832 57.122 8.258 1.00 21.35 ? 239 TYR A N 1 ATOM 1904 C CA . TYR A 1 239 ? 4.822 56.135 7.930 1.00 21.89 ? 239 TYR A CA 1 ATOM 1905 C C . TYR A 1 239 ? 4.360 55.422 9.187 1.00 22.87 ? 239 TYR A C 1 ATOM 1906 O O . TYR A 1 239 ? 5.057 55.392 10.199 1.00 22.31 ? 239 TYR A O 1 ATOM 1907 C CB . TYR A 1 239 ? 5.356 55.125 6.906 1.00 19.47 ? 239 TYR A CB 1 ATOM 1908 C CG . TYR A 1 239 ? 6.280 54.060 7.457 1.00 19.29 ? 239 TYR A CG 1 ATOM 1909 C CD1 . TYR A 1 239 ? 5.776 52.951 8.137 1.00 19.42 ? 239 TYR A CD1 1 ATOM 1910 C CD2 . TYR A 1 239 ? 7.660 54.151 7.273 1.00 19.95 ? 239 TYR A CD2 1 ATOM 1911 C CE1 . TYR A 1 239 ? 6.627 51.953 8.616 1.00 21.46 ? 239 TYR A CE1 1 ATOM 1912 C CE2 . TYR A 1 239 ? 8.519 53.166 7.745 1.00 20.67 ? 239 TYR A CE2 1 ATOM 1913 C CZ . TYR A 1 239 ? 8.000 52.070 8.414 1.00 22.02 ? 239 TYR A CZ 1 ATOM 1914 O OH . TYR A 1 239 ? 8.855 51.096 8.871 1.00 20.87 ? 239 TYR A OH 1 ATOM 1915 N N . THR A 1 240 ? 3.167 54.856 9.112 1.00 24.17 ? 240 THR A N 1 ATOM 1916 C CA . THR A 1 240 ? 2.600 54.136 10.233 1.00 25.07 ? 240 THR A CA 1 ATOM 1917 C C . THR A 1 240 ? 1.824 52.945 9.680 1.00 25.17 ? 240 THR A C 1 ATOM 1918 O O . THR A 1 240 ? 1.146 53.053 8.658 1.00 24.86 ? 240 THR A O 1 ATOM 1919 C CB . THR A 1 240 ? 1.679 55.067 11.078 1.00 25.08 ? 240 THR A CB 1 ATOM 1920 O OG1 . THR A 1 240 ? 1.045 54.306 12.111 1.00 27.94 ? 240 THR A OG1 1 ATOM 1921 C CG2 . THR A 1 240 ? 0.625 55.732 10.208 1.00 23.83 ? 240 THR A CG2 1 ATOM 1922 N N . ILE A 1 241 ? 1.965 51.803 10.343 1.00 25.31 ? 241 ILE A N 1 ATOM 1923 C CA . ILE A 1 241 ? 1.298 50.573 9.939 1.00 25.75 ? 241 ILE A CA 1 ATOM 1924 C C . ILE A 1 241 ? -0.029 50.462 10.670 1.00 27.72 ? 241 ILE A C 1 ATOM 1925 O O . ILE A 1 241 ? -0.118 50.780 11.855 1.00 28.25 ? 241 ILE A O 1 ATOM 1926 C CB . ILE A 1 241 ? 2.177 49.352 10.278 1.00 24.53 ? 241 ILE A CB 1 ATOM 1927 C CG1 . ILE A 1 241 ? 3.435 49.380 9.401 1.00 24.36 ? 241 ILE A CG1 1 ATOM 1928 C CG2 . ILE A 1 241 ? 1.379 48.057 10.111 1.00 23.25 ? 241 ILE A CG2 1 ATOM 1929 C CD1 . ILE A 1 241 ? 4.510 48.380 9.800 1.00 22.08 ? 241 ILE A CD1 1 ATOM 1930 N N . GLY A 1 242 ? -1.064 50.013 9.967 1.00 28.51 ? 242 GLY A N 1 ATOM 1931 C CA . GLY A 1 242 ? -2.359 49.890 10.603 1.00 29.07 ? 242 GLY A CA 1 ATOM 1932 C C . GLY A 1 242 ? -3.375 49.061 9.847 1.00 30.62 ? 242 GLY A C 1 ATOM 1933 O O . GLY A 1 242 ? -3.042 48.339 8.906 1.00 29.60 ? 242 GLY A O 1 ATOM 1934 N N . THR A 1 243 ? -4.628 49.182 10.276 1.00 31.63 ? 243 THR A N 1 ATOM 1935 C CA . THR A 1 243 ? -5.744 48.461 9.683 1.00 31.67 ? 243 THR A CA 1 ATOM 1936 C C . THR A 1 243 ? -6.682 49.414 8.955 1.00 32.07 ? 243 THR A C 1 ATOM 1937 O O . THR A 1 243 ? -7.018 50.486 9.463 1.00 28.76 ? 243 THR A O 1 ATOM 1938 C CB . THR A 1 243 ? -6.538 47.709 10.766 1.00 32.50 ? 243 THR A CB 1 ATOM 1939 O OG1 . THR A 1 243 ? -5.701 46.703 11.351 1.00 33.94 ? 243 THR A OG1 1 ATOM 1940 C CG2 . THR A 1 243 ? -7.781 47.057 10.171 1.00 31.67 ? 243 THR A CG2 1 ATOM 1941 N N . TYR A 1 244 ? -7.108 49.005 7.763 1.00 33.40 ? 244 TYR A N 1 ATOM 1942 C CA . TYR A 1 244 ? -7.996 49.815 6.943 1.00 35.47 ? 244 TYR A CA 1 ATOM 1943 C C . TYR A 1 244 ? -9.378 49.189 6.785 1.00 37.66 ? 244 TYR A C 1 ATOM 1944 O O . TYR A 1 244 ? -9.506 47.994 6.523 1.00 37.71 ? 244 TYR A O 1 ATOM 1945 C CB . TYR A 1 244 ? -7.349 50.034 5.573 1.00 33.14 ? 244 TYR A CB 1 ATOM 1946 C CG . TYR A 1 244 ? -8.214 50.733 4.549 1.00 32.43 ? 244 TYR A CG 1 ATOM 1947 C CD1 . TYR A 1 244 ? -8.861 51.936 4.844 1.00 31.48 ? 244 TYR A CD1 1 ATOM 1948 C CD2 . TYR A 1 244 ? -8.347 50.211 3.263 1.00 32.48 ? 244 TYR A CD2 1 ATOM 1949 C CE1 . TYR A 1 244 ? -9.620 52.603 3.874 1.00 32.37 ? 244 TYR A CE1 1 ATOM 1950 C CE2 . TYR A 1 244 ? -9.098 50.864 2.287 1.00 32.93 ? 244 TYR A CE2 1 ATOM 1951 C CZ . TYR A 1 244 ? -9.731 52.058 2.594 1.00 33.80 ? 244 TYR A CZ 1 ATOM 1952 O OH . TYR A 1 244 ? -10.454 52.700 1.612 1.00 31.97 ? 244 TYR A OH 1 ATOM 1953 N N . SER A 1 245 ? -10.408 50.009 6.963 1.00 40.90 ? 245 SER A N 1 ATOM 1954 C CA . SER A 1 245 ? -11.794 49.569 6.824 1.00 43.85 ? 245 SER A CA 1 ATOM 1955 C C . SER A 1 245 ? -12.484 50.412 5.745 1.00 45.66 ? 245 SER A C 1 ATOM 1956 O O . SER A 1 245 ? -13.006 51.493 6.029 1.00 44.88 ? 245 SER A O 1 ATOM 1957 C CB . SER A 1 245 ? -12.541 49.726 8.153 1.00 43.97 ? 245 SER A CB 1 ATOM 1958 O OG . SER A 1 245 ? -11.960 48.930 9.171 1.00 45.30 ? 245 SER A OG 1 ATOM 1959 N N . PRO A 1 246 ? -12.491 49.925 4.492 1.00 47.71 ? 246 PRO A N 1 ATOM 1960 C CA . PRO A 1 246 ? -13.108 50.616 3.353 1.00 50.53 ? 246 PRO A CA 1 ATOM 1961 C C . PRO A 1 246 ? -14.540 51.047 3.658 1.00 53.94 ? 246 PRO A C 1 ATOM 1962 O O . PRO A 1 246 ? -14.944 52.181 3.377 1.00 53.40 ? 246 PRO A O 1 ATOM 1963 C CB . PRO A 1 246 ? -13.065 49.567 2.245 1.00 49.99 ? 246 PRO A CB 1 ATOM 1964 C CG . PRO A 1 246 ? -11.878 48.735 2.604 1.00 49.99 ? 246 PRO A CG 1 ATOM 1965 C CD . PRO A 1 246 ? -12.011 48.590 4.093 1.00 48.00 ? 246 PRO A CD 1 ATOM 1966 N N . ASP A 1 247 ? -15.296 50.111 4.227 1.00 57.33 ? 247 ASP A N 1 ATOM 1967 C CA . ASP A 1 247 ? -16.689 50.309 4.600 1.00 59.97 ? 247 ASP A CA 1 ATOM 1968 C C . ASP A 1 247 ? -16.944 51.672 5.229 1.00 59.95 ? 247 ASP A C 1 ATOM 1969 O O . ASP A 1 247 ? -17.864 52.387 4.828 1.00 60.91 ? 247 ASP A O 1 ATOM 1970 C CB . ASP A 1 247 ? -17.111 49.212 5.572 1.00 63.80 ? 247 ASP A CB 1 ATOM 1971 C CG . ASP A 1 247 ? -16.002 48.852 6.552 1.00 69.01 ? 247 ASP A CG 1 ATOM 1972 O OD1 . ASP A 1 247 ? -15.055 48.134 6.145 1.00 69.39 ? 247 ASP A OD1 1 ATOM 1973 O OD2 . ASP A 1 247 ? -16.069 49.299 7.722 1.00 71.34 ? 247 ASP A OD2 1 ATOM 1974 N N . ARG A 1 248 ? -16.135 52.033 6.217 1.00 59.14 ? 248 ARG A N 1 ATOM 1975 C CA . ARG A 1 248 ? -16.306 53.319 6.877 1.00 58.99 ? 248 ARG A CA 1 ATOM 1976 C C . ARG A 1 248 ? -15.104 54.239 6.693 1.00 56.32 ? 248 ARG A C 1 ATOM 1977 O O . ARG A 1 248 ? -14.957 55.233 7.409 1.00 55.74 ? 248 ARG A O 1 ATOM 1978 C CB . ARG A 1 248 ? -16.608 53.099 8.362 1.00 62.67 ? 248 ARG A CB 1 ATOM 1979 C CG . ARG A 1 248 ? -15.723 52.065 9.028 1.00 67.35 ? 248 ARG A CG 1 ATOM 1980 C CD . ARG A 1 248 ? -16.344 51.565 10.327 1.00 71.77 ? 248 ARG A CD 1 ATOM 1981 N NE . ARG A 1 248 ? -15.518 50.537 10.959 1.00 75.99 ? 248 ARG A NE 1 ATOM 1982 C CZ . ARG A 1 248 ? -14.375 50.779 11.597 1.00 77.58 ? 248 ARG A CZ 1 ATOM 1983 N NH1 . ARG A 1 248 ? -13.918 52.022 11.696 1.00 78.30 ? 248 ARG A NH1 1 ATOM 1984 N NH2 . ARG A 1 248 ? -13.680 49.776 12.125 1.00 77.37 ? 248 ARG A NH2 1 ATOM 1985 N N . GLU A 1 249 ? -14.265 53.912 5.712 1.00 52.91 ? 249 GLU A N 1 ATOM 1986 C CA . GLU A 1 249 ? -13.067 54.687 5.398 1.00 49.79 ? 249 GLU A CA 1 ATOM 1987 C C . GLU A 1 249 ? -12.289 55.036 6.656 1.00 48.28 ? 249 GLU A C 1 ATOM 1988 O O . GLU A 1 249 ? -12.005 56.205 6.934 1.00 48.45 ? 249 GLU A O 1 ATOM 1989 C CB . GLU A 1 249 ? -13.445 55.957 4.636 1.00 48.41 ? 249 GLU A CB 1 ATOM 1990 C CG . GLU A 1 249 ? -14.093 55.668 3.297 1.00 49.21 ? 249 GLU A CG 1 ATOM 1991 C CD . GLU A 1 249 ? -13.146 54.994 2.312 1.00 48.73 ? 249 GLU A CD 1 ATOM 1992 O OE1 . GLU A 1 249 ? -12.195 54.311 2.748 1.00 45.95 ? 249 GLU A OE1 1 ATOM 1993 O OE2 . GLU A 1 249 ? -13.367 55.133 1.094 1.00 50.53 ? 249 GLU A OE2 1 ATOM 1994 N N . ASN A 1 250 ? -11.937 54.002 7.407 1.00 46.09 ? 250 ASN A N 1 ATOM 1995 C CA . ASN A 1 250 ? -11.213 54.179 8.649 1.00 43.82 ? 250 ASN A CA 1 ATOM 1996 C C . ASN A 1 250 ? -9.852 53.496 8.663 1.00 41.88 ? 250 ASN A C 1 ATOM 1997 O O . ASN A 1 250 ? -9.718 52.319 8.315 1.00 39.80 ? 250 ASN A O 1 ATOM 1998 C CB . ASN A 1 250 ? -12.056 53.650 9.809 1.00 46.46 ? 250 ASN A CB 1 ATOM 1999 C CG . ASN A 1 250 ? -11.325 53.710 11.133 1.00 49.82 ? 250 ASN A CG 1 ATOM 2000 O OD1 . ASN A 1 250 ? -11.067 54.793 11.660 1.00 53.05 ? 250 ASN A OD1 1 ATOM 2001 N ND2 . ASN A 1 250 ? -10.976 52.543 11.675 1.00 50.02 ? 250 ASN A ND2 1 ATOM 2002 N N . PHE A 1 251 ? -8.841 54.256 9.066 1.00 39.82 ? 251 PHE A N 1 ATOM 2003 C CA . PHE A 1 251 ? -7.486 53.743 9.182 1.00 37.87 ? 251 PHE A CA 1 ATOM 2004 C C . PHE A 1 251 ? -7.114 53.819 10.653 1.00 37.12 ? 251 PHE A C 1 ATOM 2005 O O . PHE A 1 251 ? -7.081 54.900 11.237 1.00 36.94 ? 251 PHE A O 1 ATOM 2006 C CB . PHE A 1 251 ? -6.500 54.581 8.373 1.00 36.43 ? 251 PHE A CB 1 ATOM 2007 C CG . PHE A 1 251 ? -5.075 54.166 8.565 1.00 34.68 ? 251 PHE A CG 1 ATOM 2008 C CD1 . PHE A 1 251 ? -4.650 52.899 8.173 1.00 33.37 ? 251 PHE A CD1 1 ATOM 2009 C CD2 . PHE A 1 251 ? -4.164 55.020 9.179 1.00 33.99 ? 251 PHE A CD2 1 ATOM 2010 C CE1 . PHE A 1 251 ? -3.340 52.485 8.390 1.00 32.25 ? 251 PHE A CE1 1 ATOM 2011 C CE2 . PHE A 1 251 ? -2.852 54.617 9.401 1.00 33.97 ? 251 PHE A CE2 1 ATOM 2012 C CZ . PHE A 1 251 ? -2.439 53.345 9.005 1.00 33.36 ? 251 PHE A CZ 1 ATOM 2013 N N . LEU A 1 252 ? -6.838 52.671 11.252 1.00 37.18 ? 252 LEU A N 1 ATOM 2014 C CA . LEU A 1 252 ? -6.491 52.632 12.660 1.00 37.22 ? 252 LEU A CA 1 ATOM 2015 C C . LEU A 1 252 ? -5.016 52.274 12.846 1.00 36.82 ? 252 LEU A C 1 ATOM 2016 O O . LEU A 1 252 ? -4.593 51.167 12.518 1.00 36.53 ? 252 LEU A O 1 ATOM 2017 C CB . LEU A 1 252 ? -7.368 51.603 13.369 1.00 38.99 ? 252 LEU A CB 1 ATOM 2018 C CG . LEU A 1 252 ? -7.772 51.850 14.824 1.00 42.04 ? 252 LEU A CG 1 ATOM 2019 C CD1 . LEU A 1 252 ? -8.219 50.517 15.416 1.00 41.95 ? 252 LEU A CD1 1 ATOM 2020 C CD2 . LEU A 1 252 ? -6.611 52.425 15.640 1.00 42.80 ? 252 LEU A CD2 1 ATOM 2021 N N . PRO A 1 253 ? -4.211 53.215 13.366 1.00 36.60 ? 253 PRO A N 1 ATOM 2022 C CA . PRO A 1 253 ? -2.783 52.970 13.588 1.00 36.21 ? 253 PRO A CA 1 ATOM 2023 C C . PRO A 1 253 ? -2.580 51.805 14.548 1.00 36.78 ? 253 PRO A C 1 ATOM 2024 O O . PRO A 1 253 ? -3.205 51.741 15.608 1.00 37.17 ? 253 PRO A O 1 ATOM 2025 C CB . PRO A 1 253 ? -2.296 54.284 14.185 1.00 36.39 ? 253 PRO A CB 1 ATOM 2026 C CG . PRO A 1 253 ? -3.215 55.290 13.583 1.00 38.59 ? 253 PRO A CG 1 ATOM 2027 C CD . PRO A 1 253 ? -4.555 54.610 13.686 1.00 37.17 ? 253 PRO A CD 1 ATOM 2028 N N . GLN A 1 254 ? -1.699 50.889 14.175 1.00 36.61 ? 254 GLN A N 1 ATOM 2029 C CA . GLN A 1 254 ? -1.408 49.725 14.993 1.00 37.00 ? 254 GLN A CA 1 ATOM 2030 C C . GLN A 1 254 ? -0.992 50.101 16.416 1.00 37.03 ? 254 GLN A C 1 ATOM 2031 O O . GLN A 1 254 ? -1.344 49.410 17.374 1.00 37.04 ? 254 GLN A O 1 ATOM 2032 C CB . GLN A 1 254 ? -0.299 48.915 14.341 1.00 39.89 ? 254 GLN A CB 1 ATOM 2033 C CG . GLN A 1 254 ? -0.330 47.456 14.687 1.00 43.46 ? 254 GLN A CG 1 ATOM 2034 C CD . GLN A 1 254 ? 0.828 46.711 14.075 1.00 46.33 ? 254 GLN A CD 1 ATOM 2035 O OE1 . GLN A 1 254 ? 0.756 45.500 13.863 1.00 48.73 ? 254 GLN A OE1 1 ATOM 2036 N NE2 . GLN A 1 254 ? 1.912 47.429 13.791 1.00 47.83 ? 254 GLN A NE2 1 ATOM 2037 N N . ASN A 1 255 ? -0.235 51.189 16.551 1.00 36.62 ? 255 ASN A N 1 ATOM 2038 C CA . ASN A 1 255 ? 0.225 51.646 17.861 1.00 36.46 ? 255 ASN A CA 1 ATOM 2039 C C . ASN A 1 255 ? -0.661 52.760 18.412 1.00 36.96 ? 255 ASN A C 1 ATOM 2040 O O . ASN A 1 255 ? -0.289 53.449 19.364 1.00 37.16 ? 255 ASN A O 1 ATOM 2041 C CB . ASN A 1 255 ? 1.680 52.139 17.789 1.00 35.20 ? 255 ASN A CB 1 ATOM 2042 C CG . ASN A 1 255 ? 1.858 53.331 16.860 1.00 34.52 ? 255 ASN A CG 1 ATOM 2043 O OD1 . ASN A 1 255 ? 0.905 54.049 16.546 1.00 35.08 ? 255 ASN A OD1 1 ATOM 2044 N ND2 . ASN A 1 255 ? 3.093 53.559 16.435 1.00 33.93 ? 255 ASN A ND2 1 ATOM 2045 N N . GLY A 1 256 ? -1.828 52.930 17.795 1.00 37.06 ? 256 GLY A N 1 ATOM 2046 C CA . GLY A 1 256 ? -2.776 53.947 18.219 1.00 36.48 ? 256 GLY A CA 1 ATOM 2047 C C . GLY A 1 256 ? -2.257 55.374 18.285 1.00 35.69 ? 256 GLY A C 1 ATOM 2048 O O . GLY A 1 256 ? -2.862 56.228 18.928 1.00 35.24 ? 256 GLY A O 1 ATOM 2049 N N . LEU A 1 257 ? -1.144 55.646 17.617 1.00 35.19 ? 257 LEU A N 1 ATOM 2050 C CA . LEU A 1 257 ? -0.583 56.986 17.647 1.00 35.34 ? 257 LEU A CA 1 ATOM 2051 C C . LEU A 1 257 ? -0.838 57.766 16.373 1.00 36.25 ? 257 LEU A C 1 ATOM 2052 O O . LEU A 1 257 ? -1.046 57.192 15.305 1.00 37.45 ? 257 LEU A O 1 ATOM 2053 C CB . LEU A 1 257 ? 0.930 56.930 17.870 1.00 35.33 ? 257 LEU A CB 1 ATOM 2054 C CG . LEU A 1 257 ? 1.491 56.238 19.107 1.00 34.56 ? 257 LEU A CG 1 ATOM 2055 C CD1 . LEU A 1 257 ? 3.003 56.439 19.132 1.00 33.27 ? 257 LEU A CD1 1 ATOM 2056 C CD2 . LEU A 1 257 ? 0.852 56.819 20.360 1.00 35.01 ? 257 LEU A CD2 1 ATOM 2057 N N . SER A 1 258 ? -0.823 59.085 16.495 1.00 36.64 ? 258 SER A N 1 ATOM 2058 C CA . SER A 1 258 ? -0.985 59.955 15.341 1.00 37.04 ? 258 SER A CA 1 ATOM 2059 C C . SER A 1 258 ? 0.436 60.400 15.047 1.00 36.16 ? 258 SER A C 1 ATOM 2060 O O . SER A 1 258 ? 1.221 60.602 15.972 1.00 36.56 ? 258 SER A O 1 ATOM 2061 C CB . SER A 1 258 ? -1.837 61.174 15.685 1.00 37.36 ? 258 SER A CB 1 ATOM 2062 O OG . SER A 1 258 ? -3.120 60.784 16.130 1.00 41.22 ? 258 SER A OG 1 ATOM 2063 N N . LEU A 1 259 ? 0.786 60.535 13.777 1.00 34.45 ? 259 LEU A N 1 ATOM 2064 C CA . LEU A 1 259 ? 2.132 60.967 13.452 1.00 32.91 ? 259 LEU A CA 1 ATOM 2065 C C . LEU A 1 259 ? 2.396 62.306 14.134 1.00 32.70 ? 259 LEU A C 1 ATOM 2066 O O . LEU A 1 259 ? 1.506 63.156 14.231 1.00 33.76 ? 259 LEU A O 1 ATOM 2067 C CB . LEU A 1 259 ? 2.299 61.073 11.934 1.00 31.08 ? 259 LEU A CB 1 ATOM 2068 C CG . LEU A 1 259 ? 2.120 59.736 11.206 1.00 29.83 ? 259 LEU A CG 1 ATOM 2069 C CD1 . LEU A 1 259 ? 2.156 59.958 9.708 1.00 29.80 ? 259 LEU A CD1 1 ATOM 2070 C CD2 . LEU A 1 259 ? 3.207 58.760 11.633 1.00 28.29 ? 259 LEU A CD2 1 ATOM 2071 N N . THR A 1 260 ? 3.614 62.473 14.637 1.00 32.57 ? 260 THR A N 1 ATOM 2072 C CA . THR A 1 260 ? 4.012 63.705 15.310 1.00 32.85 ? 260 THR A CA 1 ATOM 2073 C C . THR A 1 260 ? 5.364 64.181 14.787 1.00 32.98 ? 260 THR A C 1 ATOM 2074 O O . THR A 1 260 ? 5.805 65.291 15.097 1.00 33.39 ? 260 THR A O 1 ATOM 2075 C CB . THR A 1 260 ? 4.133 63.507 16.844 1.00 32.69 ? 260 THR A CB 1 ATOM 2076 O OG1 . THR A 1 260 ? 5.069 62.460 17.121 1.00 34.84 ? 260 THR A OG1 1 ATOM 2077 C CG2 . THR A 1 260 ? 2.792 63.147 17.449 1.00 33.36 ? 260 THR A CG2 1 ATOM 2078 N N . GLY A 1 261 ? 6.016 63.339 13.990 1.00 31.57 ? 261 GLY A N 1 ATOM 2079 C CA . GLY A 1 261 ? 7.315 63.697 13.463 1.00 30.42 ? 261 GLY A CA 1 ATOM 2080 C C . GLY A 1 261 ? 8.336 63.679 14.583 1.00 29.72 ? 261 GLY A C 1 ATOM 2081 O O . GLY A 1 261 ? 9.271 64.480 14.609 1.00 29.81 ? 261 GLY A O 1 ATOM 2082 N N . SER A 1 262 ? 8.146 62.760 15.522 1.00 28.61 ? 262 SER A N 1 ATOM 2083 C CA . SER A 1 262 ? 9.049 62.627 16.657 1.00 29.15 ? 262 SER A CA 1 ATOM 2084 C C . SER A 1 262 ? 9.748 61.277 16.606 1.00 29.39 ? 262 SER A C 1 ATOM 2085 O O . SER A 1 262 ? 9.457 60.442 15.751 1.00 28.40 ? 262 SER A O 1 ATOM 2086 C CB . SER A 1 262 ? 8.274 62.730 17.971 1.00 28.69 ? 262 SER A CB 1 ATOM 2087 O OG . SER A 1 262 ? 7.458 61.586 18.167 1.00 26.75 ? 262 SER A OG 1 ATOM 2088 N N . THR A 1 263 ? 10.661 61.066 17.546 1.00 30.09 ? 263 THR A N 1 ATOM 2089 C CA . THR A 1 263 ? 11.405 59.821 17.623 1.00 30.73 ? 263 THR A CA 1 ATOM 2090 C C . THR A 1 263 ? 10.462 58.653 17.918 1.00 31.68 ? 263 THR A C 1 ATOM 2091 O O . THR A 1 263 ? 10.888 57.502 17.996 1.00 31.51 ? 263 THR A O 1 ATOM 2092 C CB . THR A 1 263 ? 12.487 59.908 18.708 1.00 30.42 ? 263 THR A CB 1 ATOM 2093 O OG1 . THR A 1 263 ? 11.875 60.169 19.976 1.00 30.88 ? 263 THR A OG1 1 ATOM 2094 C CG2 . THR A 1 263 ? 13.465 61.032 18.381 1.00 28.49 ? 263 THR A CG2 1 ATOM 2095 N N . LEU A 1 264 ? 9.179 58.964 18.078 1.00 32.66 ? 264 LEU A N 1 ATOM 2096 C CA . LEU A 1 264 ? 8.150 57.955 18.334 1.00 33.39 ? 264 LEU A CA 1 ATOM 2097 C C . LEU A 1 264 ? 7.671 57.335 17.014 1.00 33.80 ? 264 LEU A C 1 ATOM 2098 O O . LEU A 1 264 ? 7.132 56.226 17.002 1.00 34.25 ? 264 LEU A O 1 ATOM 2099 C CB . LEU A 1 264 ? 6.943 58.591 19.034 1.00 33.67 ? 264 LEU A CB 1 ATOM 2100 C CG . LEU A 1 264 ? 6.841 58.640 20.556 1.00 34.81 ? 264 LEU A CG 1 ATOM 2101 C CD1 . LEU A 1 264 ? 8.199 58.881 21.163 1.00 37.63 ? 264 LEU A CD1 1 ATOM 2102 C CD2 . LEU A 1 264 ? 5.859 59.740 20.950 1.00 34.40 ? 264 LEU A CD2 1 ATOM 2103 N N . ASP A 1 265 ? 7.867 58.056 15.911 1.00 32.04 ? 265 ASP A N 1 ATOM 2104 C CA . ASP A 1 265 ? 7.426 57.587 14.599 1.00 30.29 ? 265 ASP A CA 1 ATOM 2105 C C . ASP A 1 265 ? 8.502 56.906 13.763 1.00 27.66 ? 265 ASP A C 1 ATOM 2106 O O . ASP A 1 265 ? 9.697 57.085 13.989 1.00 26.64 ? 265 ASP A O 1 ATOM 2107 C CB . ASP A 1 265 ? 6.849 58.753 13.793 1.00 32.80 ? 265 ASP A CB 1 ATOM 2108 C CG . ASP A 1 265 ? 5.748 59.489 14.533 1.00 34.43 ? 265 ASP A CG 1 ATOM 2109 O OD1 . ASP A 1 265 ? 4.853 58.817 15.093 1.00 35.17 ? 265 ASP A OD1 1 ATOM 2110 O OD2 . ASP A 1 265 ? 5.774 60.740 14.544 1.00 34.42 ? 265 ASP A OD2 1 ATOM 2111 N N . LEU A 1 266 ? 8.058 56.134 12.779 1.00 24.75 ? 266 LEU A N 1 ATOM 2112 C CA . LEU A 1 266 ? 8.958 55.429 11.881 1.00 23.06 ? 266 LEU A CA 1 ATOM 2113 C C . LEU A 1 266 ? 9.196 56.202 10.588 1.00 23.02 ? 266 LEU A C 1 ATOM 2114 O O . LEU A 1 266 ? 8.372 57.018 10.165 1.00 21.57 ? 266 LEU A O 1 ATOM 2115 C CB . LEU A 1 266 ? 8.383 54.060 11.527 1.00 21.96 ? 266 LEU A CB 1 ATOM 2116 C CG . LEU A 1 266 ? 8.361 53.032 12.656 1.00 22.42 ? 266 LEU A CG 1 ATOM 2117 C CD1 . LEU A 1 266 ? 7.494 51.841 12.265 1.00 18.68 ? 266 LEU A CD1 1 ATOM 2118 C CD2 . LEU A 1 266 ? 9.784 52.600 12.960 1.00 19.13 ? 266 LEU A CD2 1 ATOM 2119 N N . ARG A 1 267 ? 10.339 55.930 9.971 1.00 22.88 ? 267 ARG A N 1 ATOM 2120 C CA . ARG A 1 267 ? 10.707 56.542 8.704 1.00 22.70 ? 267 ARG A CA 1 ATOM 2121 C C . ARG A 1 267 ? 11.214 55.423 7.814 1.00 21.88 ? 267 ARG A C 1 ATOM 2122 O O . ARG A 1 267 ? 11.600 54.365 8.304 1.00 22.04 ? 267 ARG A O 1 ATOM 2123 C CB . ARG A 1 267 ? 11.845 57.544 8.871 1.00 22.52 ? 267 ARG A CB 1 ATOM 2124 C CG . ARG A 1 267 ? 11.550 58.750 9.713 1.00 23.38 ? 267 ARG A CG 1 ATOM 2125 C CD . ARG A 1 267 ? 12.686 59.738 9.535 1.00 23.47 ? 267 ARG A CD 1 ATOM 2126 N NE . ARG A 1 267 ? 12.838 60.621 10.683 1.00 23.36 ? 267 ARG A NE 1 ATOM 2127 C CZ . ARG A 1 267 ? 13.822 61.502 10.812 1.00 21.95 ? 267 ARG A CZ 1 ATOM 2128 N NH1 . ARG A 1 267 ? 14.737 61.621 9.860 1.00 19.31 ? 267 ARG A NH1 1 ATOM 2129 N NH2 . ARG A 1 267 ? 13.897 62.257 11.899 1.00 21.95 ? 267 ARG A NH2 1 ATOM 2130 N N . TYR A 1 268 ? 11.210 55.650 6.509 1.00 21.15 ? 268 TYR A N 1 ATOM 2131 C CA . TYR A 1 268 ? 11.737 54.654 5.596 1.00 20.74 ? 268 TYR A CA 1 ATOM 2132 C C . TYR A 1 268 ? 13.244 54.727 5.780 1.00 21.77 ? 268 TYR A C 1 ATOM 2133 O O . TYR A 1 268 ? 13.913 53.737 6.072 1.00 21.12 ? 268 TYR A O 1 ATOM 2134 C CB . TYR A 1 268 ? 11.438 55.015 4.145 1.00 18.68 ? 268 TYR A CB 1 ATOM 2135 C CG . TYR A 1 268 ? 10.029 54.783 3.681 1.00 20.51 ? 268 TYR A CG 1 ATOM 2136 C CD1 . TYR A 1 268 ? 9.395 53.557 3.891 1.00 20.64 ? 268 TYR A CD1 1 ATOM 2137 C CD2 . TYR A 1 268 ? 9.359 55.754 2.935 1.00 19.64 ? 268 TYR A CD2 1 ATOM 2138 C CE1 . TYR A 1 268 ? 8.133 53.300 3.363 1.00 20.32 ? 268 TYR A CE1 1 ATOM 2139 C CE2 . TYR A 1 268 ? 8.098 55.508 2.401 1.00 20.51 ? 268 TYR A CE2 1 ATOM 2140 C CZ . TYR A 1 268 ? 7.492 54.278 2.616 1.00 20.00 ? 268 TYR A CZ 1 ATOM 2141 O OH . TYR A 1 268 ? 6.260 54.018 2.061 1.00 19.12 ? 268 TYR A OH 1 ATOM 2142 N N . ASP A 1 269 ? 13.755 55.941 5.614 1.00 22.98 ? 269 ASP A N 1 ATOM 2143 C CA . ASP A 1 269 ? 15.177 56.225 5.695 1.00 23.12 ? 269 ASP A CA 1 ATOM 2144 C C . ASP A 1 269 ? 15.381 57.369 6.690 1.00 23.49 ? 269 ASP A C 1 ATOM 2145 O O . ASP A 1 269 ? 14.562 58.281 6.763 1.00 23.29 ? 269 ASP A O 1 ATOM 2146 C CB . ASP A 1 269 ? 15.657 56.629 4.302 1.00 22.35 ? 269 ASP A CB 1 ATOM 2147 C CG . ASP A 1 269 ? 17.154 56.628 4.170 1.00 23.97 ? 269 ASP A CG 1 ATOM 2148 O OD1 . ASP A 1 269 ? 17.673 55.714 3.500 1.00 24.37 ? 269 ASP A OD1 1 ATOM 2149 O OD2 . ASP A 1 269 ? 17.813 57.538 4.726 1.00 26.80 ? 269 ASP A OD2 1 ATOM 2150 N N . TYR A 1 270 ? 16.479 57.324 7.441 1.00 23.32 ? 270 TYR A N 1 ATOM 2151 C CA . TYR A 1 270 ? 16.760 58.348 8.439 1.00 22.53 ? 270 TYR A CA 1 ATOM 2152 C C . TYR A 1 270 ? 17.793 59.394 8.022 1.00 22.29 ? 270 TYR A C 1 ATOM 2153 O O . TYR A 1 270 ? 18.305 60.130 8.858 1.00 23.01 ? 270 TYR A O 1 ATOM 2154 C CB . TYR A 1 270 ? 17.169 57.668 9.748 1.00 23.07 ? 270 TYR A CB 1 ATOM 2155 C CG . TYR A 1 270 ? 16.035 56.868 10.351 1.00 25.55 ? 270 TYR A CG 1 ATOM 2156 C CD1 . TYR A 1 270 ? 15.094 57.477 11.185 1.00 26.09 ? 270 TYR A CD1 1 ATOM 2157 C CD2 . TYR A 1 270 ? 15.849 55.520 10.020 1.00 25.68 ? 270 TYR A CD2 1 ATOM 2158 C CE1 . TYR A 1 270 ? 13.989 56.764 11.674 1.00 26.03 ? 270 TYR A CE1 1 ATOM 2159 C CE2 . TYR A 1 270 ? 14.746 54.799 10.501 1.00 24.70 ? 270 TYR A CE2 1 ATOM 2160 C CZ . TYR A 1 270 ? 13.821 55.428 11.327 1.00 26.57 ? 270 TYR A CZ 1 ATOM 2161 O OH . TYR A 1 270 ? 12.727 54.728 11.802 1.00 26.96 ? 270 TYR A OH 1 ATOM 2162 N N . GLY A 1 271 ? 18.092 59.457 6.726 1.00 21.37 ? 271 GLY A N 1 ATOM 2163 C CA . GLY A 1 271 ? 19.034 60.446 6.224 1.00 20.24 ? 271 GLY A CA 1 ATOM 2164 C C . GLY A 1 271 ? 18.321 61.337 5.216 1.00 21.98 ? 271 GLY A C 1 ATOM 2165 O O . GLY A 1 271 ? 17.191 61.778 5.460 1.00 21.11 ? 271 GLY A O 1 ATOM 2166 N N . GLN A 1 272 ? 18.974 61.609 4.087 1.00 22.13 ? 272 GLN A N 1 ATOM 2167 C CA . GLN A 1 272 ? 18.388 62.425 3.023 1.00 22.45 ? 272 GLN A CA 1 ATOM 2168 C C . GLN A 1 272 ? 17.492 61.511 2.195 1.00 22.89 ? 272 GLN A C 1 ATOM 2169 O O . GLN A 1 272 ? 17.969 60.717 1.390 1.00 22.97 ? 272 GLN A O 1 ATOM 2170 C CB . GLN A 1 272 ? 19.487 63.006 2.142 1.00 25.04 ? 272 GLN A CB 1 ATOM 2171 C CG . GLN A 1 272 ? 20.306 64.084 2.814 1.00 26.83 ? 272 GLN A CG 1 ATOM 2172 C CD . GLN A 1 272 ? 19.467 65.292 3.165 1.00 29.13 ? 272 GLN A CD 1 ATOM 2173 O OE1 . GLN A 1 272 ? 18.654 65.755 2.361 1.00 29.94 ? 272 GLN A OE1 1 ATOM 2174 N NE2 . GLN A 1 272 ? 19.666 65.820 4.365 1.00 30.85 ? 272 GLN A NE2 1 ATOM 2175 N N . PHE A 1 273 ? 16.188 61.644 2.383 1.00 23.41 ? 273 PHE A N 1 ATOM 2176 C CA . PHE A 1 273 ? 15.228 60.779 1.708 1.00 24.17 ? 273 PHE A CA 1 ATOM 2177 C C . PHE A 1 273 ? 13.901 61.518 1.775 1.00 24.26 ? 273 PHE A C 1 ATOM 2178 O O . PHE A 1 273 ? 13.409 61.788 2.867 1.00 25.25 ? 273 PHE A O 1 ATOM 2179 C CB . PHE A 1 273 ? 15.121 59.488 2.513 1.00 24.22 ? 273 PHE A CB 1 ATOM 2180 C CG . PHE A 1 273 ? 14.651 58.304 1.736 1.00 25.15 ? 273 PHE A CG 1 ATOM 2181 C CD1 . PHE A 1 273 ? 15.538 57.597 0.933 1.00 24.29 ? 273 PHE A CD1 1 ATOM 2182 C CD2 . PHE A 1 273 ? 13.348 57.831 1.881 1.00 24.87 ? 273 PHE A CD2 1 ATOM 2183 C CE1 . PHE A 1 273 ? 15.141 56.426 0.294 1.00 24.44 ? 273 PHE A CE1 1 ATOM 2184 C CE2 . PHE A 1 273 ? 12.940 56.660 1.246 1.00 25.58 ? 273 PHE A CE2 1 ATOM 2185 C CZ . PHE A 1 273 ? 13.842 55.954 0.452 1.00 24.03 ? 273 PHE A CZ 1 ATOM 2186 N N . TYR A 1 274 ? 13.310 61.845 0.633 1.00 23.73 ? 274 TYR A N 1 ATOM 2187 C CA . TYR A 1 274 ? 12.049 62.575 0.671 1.00 23.71 ? 274 TYR A CA 1 ATOM 2188 C C . TYR A 1 274 ? 11.144 62.329 -0.539 1.00 23.44 ? 274 TYR A C 1 ATOM 2189 O O . TYR A 1 274 ? 11.600 61.860 -1.588 1.00 22.53 ? 274 TYR A O 1 ATOM 2190 C CB . TYR A 1 274 ? 12.328 64.084 0.813 1.00 22.64 ? 274 TYR A CB 1 ATOM 2191 C CG . TYR A 1 274 ? 11.137 64.862 1.327 1.00 23.63 ? 274 TYR A CG 1 ATOM 2192 C CD1 . TYR A 1 274 ? 10.663 64.663 2.630 1.00 23.02 ? 274 TYR A CD1 1 ATOM 2193 C CD2 . TYR A 1 274 ? 10.443 65.747 0.498 1.00 21.12 ? 274 TYR A CD2 1 ATOM 2194 C CE1 . TYR A 1 274 ? 9.521 65.321 3.094 1.00 22.73 ? 274 TYR A CE1 1 ATOM 2195 C CE2 . TYR A 1 274 ? 9.299 66.409 0.950 1.00 21.14 ? 274 TYR A CE2 1 ATOM 2196 C CZ . TYR A 1 274 ? 8.842 66.187 2.249 1.00 23.22 ? 274 TYR A CZ 1 ATOM 2197 O OH . TYR A 1 274 ? 7.693 66.803 2.695 1.00 24.10 ? 274 TYR A OH 1 ATOM 2198 N N . ALA A 1 275 ? 9.860 62.651 -0.377 1.00 22.15 ? 275 ALA A N 1 ATOM 2199 C CA . ALA A 1 275 ? 8.871 62.491 -1.439 1.00 21.90 ? 275 ALA A CA 1 ATOM 2200 C C . ALA A 1 275 ? 8.845 61.064 -1.968 1.00 21.57 ? 275 ALA A C 1 ATOM 2201 O O . ALA A 1 275 ? 8.592 60.835 -3.149 1.00 23.47 ? 275 ALA A O 1 ATOM 2202 C CB . ALA A 1 275 ? 9.166 63.459 -2.575 1.00 19.07 ? 275 ALA A CB 1 ATOM 2203 N N . SER A 1 276 ? 9.111 60.105 -1.091 1.00 20.88 ? 276 SER A N 1 ATOM 2204 C CA . SER A 1 276 ? 9.126 58.710 -1.501 1.00 21.90 ? 276 SER A CA 1 ATOM 2205 C C . SER A 1 276 ? 7.753 58.266 -2.007 1.00 22.58 ? 276 SER A C 1 ATOM 2206 O O . SER A 1 276 ? 6.714 58.668 -1.473 1.00 23.01 ? 276 SER A O 1 ATOM 2207 C CB . SER A 1 276 ? 9.578 57.824 -0.336 1.00 20.36 ? 276 SER A CB 1 ATOM 2208 O OG . SER A 1 276 ? 8.774 58.036 0.813 1.00 22.09 ? 276 SER A OG 1 ATOM 2209 N N . LYS A 1 277 ? 7.766 57.447 -3.053 1.00 21.80 ? 277 LYS A N 1 ATOM 2210 C CA . LYS A 1 277 ? 6.545 56.926 -3.655 1.00 21.31 ? 277 LYS A CA 1 ATOM 2211 C C . LYS A 1 277 ? 6.792 55.475 -4.083 1.00 21.80 ? 277 LYS A C 1 ATOM 2212 O O . LYS A 1 277 ? 7.883 55.127 -4.552 1.00 20.07 ? 277 LYS A O 1 ATOM 2213 C CB . LYS A 1 277 ? 6.150 57.795 -4.852 1.00 20.00 ? 277 LYS A CB 1 ATOM 2214 C CG . LYS A 1 277 ? 4.883 57.353 -5.559 1.00 21.65 ? 277 LYS A CG 1 ATOM 2215 C CD . LYS A 1 277 ? 4.364 58.448 -6.484 1.00 21.16 ? 277 LYS A CD 1 ATOM 2216 C CE . LYS A 1 277 ? 3.849 59.652 -5.691 1.00 20.25 ? 277 LYS A CE 1 ATOM 2217 N NZ . LYS A 1 277 ? 2.714 59.288 -4.790 1.00 16.99 ? 277 LYS A NZ 1 ATOM 2218 N N . SER A 1 278 ? 5.785 54.624 -3.915 1.00 21.24 ? 278 SER A N 1 ATOM 2219 C CA . SER A 1 278 ? 5.938 53.217 -4.264 1.00 20.51 ? 278 SER A CA 1 ATOM 2220 C C . SER A 1 278 ? 4.938 52.765 -5.310 1.00 21.54 ? 278 SER A C 1 ATOM 2221 O O . SER A 1 278 ? 3.921 53.422 -5.543 1.00 21.92 ? 278 SER A O 1 ATOM 2222 C CB . SER A 1 278 ? 5.754 52.351 -3.018 1.00 20.32 ? 278 SER A CB 1 ATOM 2223 O OG . SER A 1 278 ? 4.411 52.407 -2.550 1.00 16.75 ? 278 SER A OG 1 ATOM 2224 N N . PHE A 1 279 ? 5.235 51.638 -5.946 1.00 20.97 ? 279 PHE A N 1 ATOM 2225 C CA . PHE A 1 279 ? 4.330 51.082 -6.936 1.00 21.90 ? 279 PHE A CA 1 ATOM 2226 C C . PHE A 1 279 ? 4.449 49.569 -6.870 1.00 21.97 ? 279 PHE A C 1 ATOM 2227 O O . PHE A 1 279 ? 5.450 49.043 -6.387 1.00 22.45 ? 279 PHE A O 1 ATOM 2228 C CB . PHE A 1 279 ? 4.662 51.615 -8.340 1.00 22.08 ? 279 PHE A CB 1 ATOM 2229 C CG . PHE A 1 279 ? 5.928 51.062 -8.927 1.00 22.62 ? 279 PHE A CG 1 ATOM 2230 C CD1 . PHE A 1 279 ? 5.886 49.974 -9.798 1.00 19.83 ? 279 PHE A CD1 1 ATOM 2231 C CD2 . PHE A 1 279 ? 7.161 51.629 -8.618 1.00 21.44 ? 279 PHE A CD2 1 ATOM 2232 C CE1 . PHE A 1 279 ? 7.051 49.462 -10.354 1.00 19.12 ? 279 PHE A CE1 1 ATOM 2233 C CE2 . PHE A 1 279 ? 8.338 51.122 -9.170 1.00 21.12 ? 279 PHE A CE2 1 ATOM 2234 C CZ . PHE A 1 279 ? 8.283 50.038 -10.040 1.00 20.80 ? 279 PHE A CZ 1 ATOM 2235 N N . PHE A 1 280 ? 3.413 48.870 -7.319 1.00 22.86 ? 280 PHE A N 1 ATOM 2236 C CA . PHE A 1 280 ? 3.438 47.416 -7.302 1.00 24.47 ? 280 PHE A CA 1 ATOM 2237 C C . PHE A 1 280 ? 3.952 46.873 -8.627 1.00 25.72 ? 280 PHE A C 1 ATOM 2238 O O . PHE A 1 280 ? 3.530 47.314 -9.698 1.00 26.64 ? 280 PHE A O 1 ATOM 2239 C CB . PHE A 1 280 ? 2.045 46.852 -7.028 1.00 23.99 ? 280 PHE A CB 1 ATOM 2240 C CG . PHE A 1 280 ? 1.982 45.349 -7.069 1.00 24.59 ? 280 PHE A CG 1 ATOM 2241 C CD1 . PHE A 1 280 ? 2.704 44.582 -6.151 1.00 24.57 ? 280 PHE A CD1 1 ATOM 2242 C CD2 . PHE A 1 280 ? 1.211 44.694 -8.032 1.00 23.26 ? 280 PHE A CD2 1 ATOM 2243 C CE1 . PHE A 1 280 ? 2.661 43.181 -6.188 1.00 22.90 ? 280 PHE A CE1 1 ATOM 2244 C CE2 . PHE A 1 280 ? 1.160 43.298 -8.079 1.00 23.07 ? 280 PHE A CE2 1 ATOM 2245 C CZ . PHE A 1 280 ? 1.888 42.541 -7.153 1.00 23.39 ? 280 PHE A CZ 1 ATOM 2246 N N . ASP A 1 281 ? 4.870 45.916 -8.535 1.00 26.53 ? 281 ASP A N 1 ATOM 2247 C CA . ASP A 1 281 ? 5.474 45.261 -9.695 1.00 27.48 ? 281 ASP A CA 1 ATOM 2248 C C . ASP A 1 281 ? 4.816 43.888 -9.753 1.00 28.85 ? 281 ASP A C 1 ATOM 2249 O O . ASP A 1 281 ? 5.205 42.993 -9.011 1.00 28.02 ? 281 ASP A O 1 ATOM 2250 C CB . ASP A 1 281 ? 6.975 45.106 -9.446 1.00 27.96 ? 281 ASP A CB 1 ATOM 2251 C CG . ASP A 1 281 ? 7.699 44.421 -10.583 1.00 27.88 ? 281 ASP A CG 1 ATOM 2252 O OD1 . ASP A 1 281 ? 7.106 43.555 -11.263 1.00 24.63 ? 281 ASP A OD1 1 ATOM 2253 O OD2 . ASP A 1 281 ? 8.887 44.743 -10.778 1.00 28.23 ? 281 ASP A OD2 1 ATOM 2254 N N . ASP A 1 282 ? 3.825 43.705 -10.618 1.00 31.64 ? 282 ASP A N 1 ATOM 2255 C CA . ASP A 1 282 ? 3.150 42.410 -10.670 1.00 35.11 ? 282 ASP A CA 1 ATOM 2256 C C . ASP A 1 282 ? 3.954 41.311 -11.354 1.00 33.59 ? 282 ASP A C 1 ATOM 2257 O O . ASP A 1 282 ? 3.564 40.145 -11.320 1.00 34.61 ? 282 ASP A O 1 ATOM 2258 C CB . ASP A 1 282 ? 1.773 42.542 -11.327 1.00 39.88 ? 282 ASP A CB 1 ATOM 2259 C CG . ASP A 1 282 ? 1.853 42.644 -12.828 1.00 47.73 ? 282 ASP A CG 1 ATOM 2260 O OD1 . ASP A 1 282 ? 2.650 43.467 -13.333 1.00 52.98 ? 282 ASP A OD1 1 ATOM 2261 O OD2 . ASP A 1 282 ? 1.111 41.900 -13.505 1.00 52.56 ? 282 ASP A OD2 1 ATOM 2262 N N . ALA A 1 283 ? 5.080 41.675 -11.962 1.00 32.08 ? 283 ALA A N 1 ATOM 2263 C CA . ALA A 1 283 ? 5.932 40.692 -12.626 1.00 31.33 ? 283 ALA A CA 1 ATOM 2264 C C . ALA A 1 283 ? 6.783 39.959 -11.590 1.00 32.86 ? 283 ALA A C 1 ATOM 2265 O O . ALA A 1 283 ? 6.992 38.753 -11.688 1.00 34.16 ? 283 ALA A O 1 ATOM 2266 C CB . ALA A 1 283 ? 6.826 41.372 -13.647 1.00 28.45 ? 283 ALA A CB 1 ATOM 2267 N N . LYS A 1 284 ? 7.272 40.695 -10.597 1.00 33.84 ? 284 LYS A N 1 ATOM 2268 C CA . LYS A 1 284 ? 8.095 40.110 -9.539 1.00 34.12 ? 284 LYS A CA 1 ATOM 2269 C C . LYS A 1 284 ? 7.324 40.020 -8.218 1.00 34.50 ? 284 LYS A C 1 ATOM 2270 O O . LYS A 1 284 ? 7.866 39.564 -7.211 1.00 34.98 ? 284 LYS A O 1 ATOM 2271 C CB . LYS A 1 284 ? 9.355 40.951 -9.312 1.00 34.49 ? 284 LYS A CB 1 ATOM 2272 C CG . LYS A 1 284 ? 10.300 41.074 -10.495 1.00 33.87 ? 284 LYS A CG 1 ATOM 2273 C CD . LYS A 1 284 ? 10.978 39.758 -10.807 1.00 35.51 ? 284 LYS A CD 1 ATOM 2274 C CE . LYS A 1 284 ? 12.153 39.936 -11.770 1.00 37.15 ? 284 LYS A CE 1 ATOM 2275 N NZ . LYS A 1 284 ? 13.322 40.620 -11.138 1.00 35.20 ? 284 LYS A NZ 1 ATOM 2276 N N . ASN A 1 285 ? 6.068 40.461 -8.225 1.00 34.52 ? 285 ASN A N 1 ATOM 2277 C CA . ASN A 1 285 ? 5.235 40.449 -7.021 1.00 34.59 ? 285 ASN A CA 1 ATOM 2278 C C . ASN A 1 285 ? 5.950 41.123 -5.861 1.00 32.42 ? 285 ASN A C 1 ATOM 2279 O O . ASN A 1 285 ? 6.136 40.540 -4.791 1.00 32.79 ? 285 ASN A O 1 ATOM 2280 C CB . ASN A 1 285 ? 4.850 39.016 -6.657 1.00 37.08 ? 285 ASN A CB 1 ATOM 2281 C CG . ASN A 1 285 ? 3.821 38.445 -7.611 1.00 43.63 ? 285 ASN A CG 1 ATOM 2282 O OD1 . ASN A 1 285 ? 2.655 38.847 -7.595 1.00 45.53 ? 285 ASN A OD1 1 ATOM 2283 N ND2 . ASN A 1 285 ? 4.251 37.521 -8.469 1.00 47.29 ? 285 ASN A ND2 1 ATOM 2284 N N . ARG A 1 286 ? 6.340 42.369 -6.091 1.00 28.77 ? 286 ARG A N 1 ATOM 2285 C CA . ARG A 1 286 ? 7.053 43.152 -5.096 1.00 26.65 ? 286 ARG A CA 1 ATOM 2286 C C . ARG A 1 286 ? 6.626 44.609 -5.172 1.00 24.35 ? 286 ARG A C 1 ATOM 2287 O O . ARG A 1 286 ? 6.207 45.092 -6.225 1.00 23.30 ? 286 ARG A O 1 ATOM 2288 C CB . ARG A 1 286 ? 8.561 43.077 -5.362 1.00 24.45 ? 286 ARG A CB 1 ATOM 2289 C CG . ARG A 1 286 ? 8.927 43.652 -6.722 1.00 23.99 ? 286 ARG A CG 1 ATOM 2290 C CD . ARG A 1 286 ? 10.417 43.603 -7.016 1.00 24.33 ? 286 ARG A CD 1 ATOM 2291 N NE . ARG A 1 286 ? 10.667 43.962 -8.410 1.00 24.38 ? 286 ARG A NE 1 ATOM 2292 C CZ . ARG A 1 286 ? 11.858 43.940 -8.998 1.00 23.84 ? 286 ARG A CZ 1 ATOM 2293 N NH1 . ARG A 1 286 ? 12.940 43.573 -8.318 1.00 23.22 ? 286 ARG A NH1 1 ATOM 2294 N NH2 . ARG A 1 286 ? 11.964 44.287 -10.275 1.00 21.24 ? 286 ARG A NH2 1 ATOM 2295 N N . ARG A 1 287 ? 6.722 45.304 -4.048 1.00 22.02 ? 287 ARG A N 1 ATOM 2296 C CA . ARG A 1 287 ? 6.406 46.719 -4.035 1.00 21.35 ? 287 ARG A CA 1 ATOM 2297 C C . ARG A 1 287 ? 7.766 47.417 -4.103 1.00 21.57 ? 287 ARG A C 1 ATOM 2298 O O . ARG A 1 287 ? 8.670 47.114 -3.320 1.00 19.02 ? 287 ARG A O 1 ATOM 2299 C CB . ARG A 1 287 ? 5.660 47.098 -2.760 1.00 20.66 ? 287 ARG A CB 1 ATOM 2300 C CG . ARG A 1 287 ? 5.421 48.590 -2.609 1.00 21.13 ? 287 ARG A CG 1 ATOM 2301 C CD . ARG A 1 287 ? 4.295 48.840 -1.619 1.00 22.18 ? 287 ARG A CD 1 ATOM 2302 N NE . ARG A 1 287 ? 3.015 48.418 -2.177 1.00 21.12 ? 287 ARG A NE 1 ATOM 2303 C CZ . ARG A 1 287 ? 2.309 49.129 -3.053 1.00 20.80 ? 287 ARG A CZ 1 ATOM 2304 N NH1 . ARG A 1 287 ? 2.756 50.313 -3.463 1.00 18.00 ? 287 ARG A NH1 1 ATOM 2305 N NH2 . ARG A 1 287 ? 1.173 48.640 -3.544 1.00 19.30 ? 287 ARG A NH2 1 ATOM 2306 N N . VAL A 1 288 ? 7.917 48.323 -5.061 1.00 20.56 ? 288 VAL A N 1 ATOM 2307 C CA . VAL A 1 288 ? 9.172 49.038 -5.231 1.00 20.74 ? 288 VAL A CA 1 ATOM 2308 C C . VAL A 1 288 ? 9.034 50.483 -4.761 1.00 22.21 ? 288 VAL A C 1 ATOM 2309 O O . VAL A 1 288 ? 8.029 51.148 -5.032 1.00 22.67 ? 288 VAL A O 1 ATOM 2310 C CB . VAL A 1 288 ? 9.618 48.984 -6.704 1.00 21.54 ? 288 VAL A CB 1 ATOM 2311 C CG1 . VAL A 1 288 ? 10.954 49.692 -6.885 1.00 20.88 ? 288 VAL A CG1 1 ATOM 2312 C CG2 . VAL A 1 288 ? 9.724 47.531 -7.141 1.00 19.97 ? 288 VAL A CG2 1 ATOM 2313 N N . LEU A 1 289 ? 10.051 50.958 -4.048 1.00 22.26 ? 289 LEU A N 1 ATOM 2314 C CA . LEU A 1 289 ? 10.043 52.311 -3.511 1.00 22.23 ? 289 LEU A CA 1 ATOM 2315 C C . LEU A 1 289 ? 11.105 53.208 -4.133 1.00 22.60 ? 289 LEU A C 1 ATOM 2316 O O . LEU A 1 289 ? 12.271 52.823 -4.225 1.00 23.41 ? 289 LEU A O 1 ATOM 2317 C CB . LEU A 1 289 ? 10.251 52.263 -1.992 1.00 21.86 ? 289 LEU A CB 1 ATOM 2318 C CG . LEU A 1 289 ? 10.172 53.573 -1.201 1.00 22.63 ? 289 LEU A CG 1 ATOM 2319 C CD1 . LEU A 1 289 ? 8.767 54.145 -1.299 1.00 20.35 ? 289 LEU A CD1 1 ATOM 2320 C CD2 . LEU A 1 289 ? 10.537 53.317 0.253 1.00 20.57 ? 289 LEU A CD2 1 ATOM 2321 N N . TRP A 1 290 ? 10.681 54.397 -4.563 1.00 22.49 ? 290 TRP A N 1 ATOM 2322 C CA . TRP A 1 290 ? 11.560 55.411 -5.153 1.00 21.10 ? 290 TRP A CA 1 ATOM 2323 C C . TRP A 1 290 ? 11.576 56.603 -4.203 1.00 22.21 ? 290 TRP A C 1 ATOM 2324 O O . TRP A 1 290 ? 10.578 56.882 -3.533 1.00 22.41 ? 290 TRP A O 1 ATOM 2325 C CB . TRP A 1 290 ? 11.022 55.938 -6.484 1.00 21.29 ? 290 TRP A CB 1 ATOM 2326 C CG . TRP A 1 290 ? 11.225 55.085 -7.684 1.00 21.93 ? 290 TRP A CG 1 ATOM 2327 C CD1 . TRP A 1 290 ? 10.311 54.252 -8.258 1.00 21.57 ? 290 TRP A CD1 1 ATOM 2328 C CD2 . TRP A 1 290 ? 12.396 55.027 -8.505 1.00 21.51 ? 290 TRP A CD2 1 ATOM 2329 N NE1 . TRP A 1 290 ? 10.837 53.683 -9.392 1.00 22.72 ? 290 TRP A NE1 1 ATOM 2330 C CE2 . TRP A 1 290 ? 12.115 54.141 -9.569 1.00 22.09 ? 290 TRP A CE2 1 ATOM 2331 C CE3 . TRP A 1 290 ? 13.653 55.641 -8.450 1.00 20.94 ? 290 TRP A CE3 1 ATOM 2332 C CZ2 . TRP A 1 290 ? 13.045 53.852 -10.571 1.00 22.04 ? 290 TRP A CZ2 1 ATOM 2333 C CZ3 . TRP A 1 290 ? 14.581 55.352 -9.450 1.00 22.25 ? 290 TRP A CZ3 1 ATOM 2334 C CH2 . TRP A 1 290 ? 14.270 54.467 -10.496 1.00 22.47 ? 290 TRP A CH2 1 ATOM 2335 N N . ALA A 1 291 ? 12.691 57.319 -4.155 1.00 20.69 ? 291 ALA A N 1 ATOM 2336 C CA . ALA A 1 291 ? 12.765 58.496 -3.306 1.00 21.39 ? 291 ALA A CA 1 ATOM 2337 C C . ALA A 1 291 ? 13.788 59.491 -3.816 1.00 21.65 ? 291 ALA A C 1 ATOM 2338 O O . ALA A 1 291 ? 14.847 59.118 -4.330 1.00 21.29 ? 291 ALA A O 1 ATOM 2339 C CB . ALA A 1 291 ? 13.089 58.108 -1.872 1.00 21.12 ? 291 ALA A CB 1 ATOM 2340 N N . TRP A 1 292 ? 13.447 60.765 -3.673 1.00 20.89 ? 292 TRP A N 1 ATOM 2341 C CA . TRP A 1 292 ? 14.315 61.850 -4.085 1.00 20.47 ? 292 TRP A CA 1 ATOM 2342 C C . TRP A 1 292 ? 15.365 62.062 -2.998 1.00 20.94 ? 292 TRP A C 1 ATOM 2343 O O . TRP A 1 292 ? 15.051 62.075 -1.809 1.00 19.73 ? 292 TRP A O 1 ATOM 2344 C CB . TRP A 1 292 ? 13.477 63.121 -4.290 1.00 20.33 ? 292 TRP A CB 1 ATOM 2345 C CG . TRP A 1 292 ? 14.267 64.399 -4.404 1.00 21.40 ? 292 TRP A CG 1 ATOM 2346 C CD1 . TRP A 1 292 ? 15.426 64.591 -5.104 1.00 22.15 ? 292 TRP A CD1 1 ATOM 2347 C CD2 . TRP A 1 292 ? 13.942 65.666 -3.813 1.00 19.68 ? 292 TRP A CD2 1 ATOM 2348 N NE1 . TRP A 1 292 ? 15.848 65.896 -4.980 1.00 20.70 ? 292 TRP A NE1 1 ATOM 2349 C CE2 . TRP A 1 292 ? 14.959 66.579 -4.195 1.00 20.63 ? 292 TRP A CE2 1 ATOM 2350 C CE3 . TRP A 1 292 ? 12.895 66.120 -2.998 1.00 18.63 ? 292 TRP A CE3 1 ATOM 2351 C CZ2 . TRP A 1 292 ? 14.960 67.923 -3.788 1.00 19.11 ? 292 TRP A CZ2 1 ATOM 2352 C CZ3 . TRP A 1 292 ? 12.893 67.459 -2.591 1.00 19.00 ? 292 TRP A CZ3 1 ATOM 2353 C CH2 . TRP A 1 292 ? 13.924 68.343 -2.989 1.00 19.11 ? 292 TRP A CH2 1 ATOM 2354 N N . VAL A 1 293 ? 16.621 62.185 -3.403 1.00 20.70 ? 293 VAL A N 1 ATOM 2355 C CA . VAL A 1 293 ? 17.687 62.430 -2.444 1.00 21.30 ? 293 VAL A CA 1 ATOM 2356 C C . VAL A 1 293 ? 18.251 63.801 -2.800 1.00 21.79 ? 293 VAL A C 1 ATOM 2357 O O . VAL A 1 293 ? 18.995 63.946 -3.769 1.00 21.87 ? 293 VAL A O 1 ATOM 2358 C CB . VAL A 1 293 ? 18.798 61.356 -2.532 1.00 21.45 ? 293 VAL A CB 1 ATOM 2359 C CG1 . VAL A 1 293 ? 19.839 61.603 -1.452 1.00 21.42 ? 293 VAL A CG1 1 ATOM 2360 C CG2 . VAL A 1 293 ? 18.196 59.969 -2.368 1.00 19.54 ? 293 VAL A CG2 1 ATOM 2361 N N . PRO A 1 294 ? 17.880 64.831 -2.029 1.00 22.57 ? 294 PRO A N 1 ATOM 2362 C CA . PRO A 1 294 ? 18.337 66.205 -2.256 1.00 23.19 ? 294 PRO A CA 1 ATOM 2363 C C . PRO A 1 294 ? 19.850 66.377 -2.180 1.00 25.89 ? 294 PRO A C 1 ATOM 2364 O O . PRO A 1 294 ? 20.576 65.489 -1.719 1.00 26.49 ? 294 PRO A O 1 ATOM 2365 C CB . PRO A 1 294 ? 17.634 66.993 -1.152 1.00 21.88 ? 294 PRO A CB 1 ATOM 2366 C CG . PRO A 1 294 ? 16.426 66.168 -0.839 1.00 21.09 ? 294 PRO A CG 1 ATOM 2367 C CD . PRO A 1 294 ? 16.974 64.770 -0.870 1.00 20.74 ? 294 PRO A CD 1 ATOM 2368 N N . GLU A 1 295 ? 20.317 67.530 -2.644 1.00 27.26 ? 295 GLU A N 1 ATOM 2369 C CA . GLU A 1 295 ? 21.733 67.865 -2.604 1.00 26.52 ? 295 GLU A CA 1 ATOM 2370 C C . GLU A 1 295 ? 21.979 68.422 -1.216 1.00 25.75 ? 295 GLU A C 1 ATOM 2371 O O . GLU A 1 295 ? 21.059 68.953 -0.593 1.00 26.10 ? 295 GLU A O 1 ATOM 2372 C CB . GLU A 1 295 ? 22.053 68.953 -3.628 1.00 26.54 ? 295 GLU A CB 1 ATOM 2373 C CG . GLU A 1 295 ? 21.848 68.534 -5.057 1.00 28.93 ? 295 GLU A CG 1 ATOM 2374 C CD . GLU A 1 295 ? 22.820 67.460 -5.466 1.00 30.59 ? 295 GLU A CD 1 ATOM 2375 O OE1 . GLU A 1 295 ? 24.040 67.734 -5.452 1.00 31.07 ? 295 GLU A OE1 1 ATOM 2376 O OE2 . GLU A 1 295 ? 22.368 66.343 -5.794 1.00 32.61 ? 295 GLU A OE2 1 ATOM 2377 N N . THR A 1 296 ? 23.200 68.288 -0.713 1.00 25.26 ? 296 THR A N 1 ATOM 2378 C CA . THR A 1 296 ? 23.509 68.845 0.594 1.00 24.29 ? 296 THR A CA 1 ATOM 2379 C C . THR A 1 296 ? 24.661 69.830 0.448 1.00 25.73 ? 296 THR A C 1 ATOM 2380 O O . THR A 1 296 ? 25.262 70.261 1.431 1.00 26.61 ? 296 THR A O 1 ATOM 2381 C CB . THR A 1 296 ? 23.842 67.763 1.641 1.00 23.52 ? 296 THR A CB 1 ATOM 2382 O OG1 . THR A 1 296 ? 24.835 66.874 1.124 1.00 26.06 ? 296 THR A OG1 1 ATOM 2383 C CG2 . THR A 1 296 ? 22.588 66.980 2.003 1.00 21.38 ? 296 THR A CG2 1 ATOM 2384 N N . ASP A 1 297 ? 24.967 70.175 -0.802 1.00 25.68 ? 297 ASP A N 1 ATOM 2385 C CA . ASP A 1 297 ? 25.994 71.168 -1.079 1.00 26.66 ? 297 ASP A CA 1 ATOM 2386 C C . ASP A 1 297 ? 25.198 72.475 -1.231 1.00 27.46 ? 297 ASP A C 1 ATOM 2387 O O . ASP A 1 297 ? 23.988 72.484 -0.991 1.00 28.14 ? 297 ASP A O 1 ATOM 2388 C CB . ASP A 1 297 ? 26.770 70.815 -2.357 1.00 26.35 ? 297 ASP A CB 1 ATOM 2389 C CG . ASP A 1 297 ? 25.878 70.685 -3.573 1.00 28.04 ? 297 ASP A CG 1 ATOM 2390 O OD1 . ASP A 1 297 ? 24.647 70.876 -3.440 1.00 28.09 ? 297 ASP A OD1 1 ATOM 2391 O OD2 . ASP A 1 297 ? 26.416 70.391 -4.665 1.00 25.16 ? 297 ASP A OD2 1 ATOM 2392 N N . SER A 1 298 ? 25.840 73.574 -1.615 1.00 27.27 ? 298 SER A N 1 ATOM 2393 C CA . SER A 1 298 ? 25.108 74.836 -1.737 1.00 27.67 ? 298 SER A CA 1 ATOM 2394 C C . SER A 1 298 ? 24.456 75.034 -3.100 1.00 29.15 ? 298 SER A C 1 ATOM 2395 O O . SER A 1 298 ? 24.793 74.351 -4.074 1.00 27.86 ? 298 SER A O 1 ATOM 2396 C CB . SER A 1 298 ? 26.031 76.023 -1.462 1.00 26.36 ? 298 SER A CB 1 ATOM 2397 O OG . SER A 1 298 ? 26.909 76.239 -2.552 1.00 28.14 ? 298 SER A OG 1 ATOM 2398 N N . GLN A 1 299 ? 23.525 75.980 -3.163 1.00 29.81 ? 299 GLN A N 1 ATOM 2399 C CA . GLN A 1 299 ? 22.840 76.280 -4.411 1.00 31.38 ? 299 GLN A CA 1 ATOM 2400 C C . GLN A 1 299 ? 23.849 76.732 -5.460 1.00 31.76 ? 299 GLN A C 1 ATOM 2401 O O . GLN A 1 299 ? 23.728 76.406 -6.645 1.00 31.74 ? 299 GLN A O 1 ATOM 2402 C CB . GLN A 1 299 ? 21.797 77.372 -4.204 1.00 32.18 ? 299 GLN A CB 1 ATOM 2403 C CG . GLN A 1 299 ? 21.173 77.842 -5.504 1.00 36.63 ? 299 GLN A CG 1 ATOM 2404 C CD . GLN A 1 299 ? 19.957 78.704 -5.275 1.00 39.83 ? 299 GLN A CD 1 ATOM 2405 O OE1 . GLN A 1 299 ? 18.924 78.228 -4.795 1.00 40.30 ? 299 GLN A OE1 1 ATOM 2406 N NE2 . GLN A 1 299 ? 20.069 79.985 -5.609 1.00 40.50 ? 299 GLN A NE2 1 ATOM 2407 N N . ALA A 1 300 ? 24.844 77.492 -5.015 1.00 32.04 ? 300 ALA A N 1 ATOM 2408 C CA . ALA A 1 300 ? 25.883 77.975 -5.911 1.00 33.40 ? 300 ALA A CA 1 ATOM 2409 C C . ALA A 1 300 ? 26.625 76.771 -6.477 1.00 34.40 ? 300 ALA A C 1 ATOM 2410 O O . ALA A 1 300 ? 26.975 76.746 -7.660 1.00 34.22 ? 300 ALA A O 1 ATOM 2411 C CB . ALA A 1 300 ? 26.842 78.883 -5.159 1.00 31.82 ? 300 ALA A CB 1 ATOM 2412 N N . ASP A 1 301 ? 26.859 75.775 -5.622 1.00 34.90 ? 301 ASP A N 1 ATOM 2413 C CA . ASP A 1 301 ? 27.547 74.558 -6.039 1.00 35.26 ? 301 ASP A CA 1 ATOM 2414 C C . ASP A 1 301 ? 26.733 73.839 -7.106 1.00 34.02 ? 301 ASP A C 1 ATOM 2415 O O . ASP A 1 301 ? 27.287 73.341 -8.089 1.00 33.64 ? 301 ASP A O 1 ATOM 2416 C CB . ASP A 1 301 ? 27.769 73.618 -4.847 1.00 37.40 ? 301 ASP A CB 1 ATOM 2417 C CG . ASP A 1 301 ? 28.786 74.157 -3.856 1.00 38.85 ? 301 ASP A CG 1 ATOM 2418 O OD1 . ASP A 1 301 ? 29.852 74.637 -4.300 1.00 41.09 ? 301 ASP A OD1 1 ATOM 2419 O OD2 . ASP A 1 301 ? 28.527 74.089 -2.636 1.00 39.65 ? 301 ASP A OD2 1 ATOM 2420 N N . ASP A 1 302 ? 25.417 73.796 -6.908 1.00 32.42 ? 302 ASP A N 1 ATOM 2421 C CA . ASP A 1 302 ? 24.523 73.137 -7.852 1.00 30.25 ? 302 ASP A CA 1 ATOM 2422 C C . ASP A 1 302 ? 24.578 73.826 -9.204 1.00 30.00 ? 302 ASP A C 1 ATOM 2423 O O . ASP A 1 302 ? 24.805 73.182 -10.232 1.00 28.28 ? 302 ASP A O 1 ATOM 2424 C CB . ASP A 1 302 ? 23.084 73.144 -7.325 1.00 29.47 ? 302 ASP A CB 1 ATOM 2425 C CG . ASP A 1 302 ? 22.933 72.361 -6.035 1.00 29.63 ? 302 ASP A CG 1 ATOM 2426 O OD1 . ASP A 1 302 ? 23.767 71.462 -5.789 1.00 28.36 ? 302 ASP A OD1 1 ATOM 2427 O OD2 . ASP A 1 302 ? 21.979 72.633 -5.273 1.00 28.44 ? 302 ASP A OD2 1 ATOM 2428 N N . ILE A 1 303 ? 24.364 75.138 -9.195 1.00 29.95 ? 303 ILE A N 1 ATOM 2429 C CA . ILE A 1 303 ? 24.398 75.931 -10.418 1.00 30.62 ? 303 ILE A CA 1 ATOM 2430 C C . ILE A 1 303 ? 25.745 75.776 -11.113 1.00 31.58 ? 303 ILE A C 1 ATOM 2431 O O . ILE A 1 303 ? 25.818 75.704 -12.340 1.00 31.99 ? 303 ILE A O 1 ATOM 2432 C CB . ILE A 1 303 ? 24.173 77.420 -10.111 1.00 29.74 ? 303 ILE A CB 1 ATOM 2433 C CG1 . ILE A 1 303 ? 22.764 77.617 -9.559 1.00 29.05 ? 303 ILE A CG1 1 ATOM 2434 C CG2 . ILE A 1 303 ? 24.379 78.252 -11.364 1.00 25.89 ? 303 ILE A CG2 1 ATOM 2435 C CD1 . ILE A 1 303 ? 22.536 78.985 -8.988 1.00 28.60 ? 303 ILE A CD1 1 ATOM 2436 N N . GLU A 1 304 ? 26.807 75.718 -10.320 1.00 31.94 ? 304 GLU A N 1 ATOM 2437 C CA . GLU A 1 304 ? 28.141 75.580 -10.870 1.00 33.92 ? 304 GLU A CA 1 ATOM 2438 C C . GLU A 1 304 ? 28.360 74.207 -11.501 1.00 33.21 ? 304 GLU A C 1 ATOM 2439 O O . GLU A 1 304 ? 28.881 74.121 -12.614 1.00 33.51 ? 304 GLU A O 1 ATOM 2440 C CB . GLU A 1 304 ? 29.189 75.846 -9.784 1.00 38.04 ? 304 GLU A CB 1 ATOM 2441 C CG . GLU A 1 304 ? 30.580 76.193 -10.319 1.00 43.77 ? 304 GLU A CG 1 ATOM 2442 C CD . GLU A 1 304 ? 31.334 74.990 -10.884 1.00 50.87 ? 304 GLU A CD 1 ATOM 2443 O OE1 . GLU A 1 304 ? 32.313 75.208 -11.636 1.00 53.78 ? 304 GLU A OE1 1 ATOM 2444 O OE2 . GLU A 1 304 ? 30.964 73.832 -10.571 1.00 52.60 ? 304 GLU A OE2 1 ATOM 2445 N N . LYS A 1 305 ? 27.968 73.132 -10.814 1.00 32.10 ? 305 LYS A N 1 ATOM 2446 C CA . LYS A 1 305 ? 28.167 71.801 -11.387 1.00 30.83 ? 305 LYS A CA 1 ATOM 2447 C C . LYS A 1 305 ? 27.086 71.455 -12.412 1.00 30.60 ? 305 LYS A C 1 ATOM 2448 O O . LYS A 1 305 ? 27.173 70.443 -13.107 1.00 29.75 ? 305 LYS A O 1 ATOM 2449 C CB . LYS A 1 305 ? 28.279 70.721 -10.289 1.00 30.54 ? 305 LYS A CB 1 ATOM 2450 C CG . LYS A 1 305 ? 27.025 70.389 -9.494 1.00 30.13 ? 305 LYS A CG 1 ATOM 2451 C CD . LYS A 1 305 ? 27.375 69.364 -8.406 1.00 29.08 ? 305 LYS A CD 1 ATOM 2452 C CE . LYS A 1 305 ? 26.144 68.699 -7.778 1.00 27.85 ? 305 LYS A CE 1 ATOM 2453 N NZ . LYS A 1 305 ? 25.269 69.623 -7.017 1.00 26.99 ? 305 LYS A NZ 1 ATOM 2454 N N . GLY A 1 306 ? 26.073 72.314 -12.505 1.00 30.13 ? 306 GLY A N 1 ATOM 2455 C CA . GLY A 1 306 ? 25.020 72.132 -13.490 1.00 29.78 ? 306 GLY A CA 1 ATOM 2456 C C . GLY A 1 306 ? 23.860 71.192 -13.234 1.00 31.05 ? 306 GLY A C 1 ATOM 2457 O O . GLY A 1 306 ? 22.989 71.054 -14.092 1.00 32.50 ? 306 GLY A O 1 ATOM 2458 N N . TRP A 1 307 ? 23.830 70.536 -12.082 1.00 30.39 ? 307 TRP A N 1 ATOM 2459 C CA . TRP A 1 307 ? 22.732 69.628 -11.788 1.00 28.58 ? 307 TRP A CA 1 ATOM 2460 C C . TRP A 1 307 ? 22.473 69.541 -10.296 1.00 28.64 ? 307 TRP A C 1 ATOM 2461 O O . TRP A 1 307 ? 23.304 69.940 -9.478 1.00 28.50 ? 307 TRP A O 1 ATOM 2462 C CB . TRP A 1 307 ? 23.028 68.226 -12.331 1.00 28.29 ? 307 TRP A CB 1 ATOM 2463 C CG . TRP A 1 307 ? 24.228 67.577 -11.703 1.00 28.33 ? 307 TRP A CG 1 ATOM 2464 C CD1 . TRP A 1 307 ? 25.536 67.745 -12.061 1.00 28.90 ? 307 TRP A CD1 1 ATOM 2465 C CD2 . TRP A 1 307 ? 24.231 66.679 -10.586 1.00 27.88 ? 307 TRP A CD2 1 ATOM 2466 N NE1 . TRP A 1 307 ? 26.353 67.005 -11.236 1.00 28.90 ? 307 TRP A NE1 1 ATOM 2467 C CE2 . TRP A 1 307 ? 25.578 66.341 -10.322 1.00 28.68 ? 307 TRP A CE2 1 ATOM 2468 C CE3 . TRP A 1 307 ? 23.225 66.127 -9.778 1.00 27.75 ? 307 TRP A CE3 1 ATOM 2469 C CZ2 . TRP A 1 307 ? 25.946 65.474 -9.285 1.00 27.40 ? 307 TRP A CZ2 1 ATOM 2470 C CZ3 . TRP A 1 307 ? 23.590 65.266 -8.744 1.00 26.46 ? 307 TRP A CZ3 1 ATOM 2471 C CH2 . TRP A 1 307 ? 24.940 64.949 -8.510 1.00 27.22 ? 307 TRP A CH2 1 ATOM 2472 N N . ALA A 1 308 ? 21.310 69.016 -9.944 1.00 27.47 ? 308 ALA A N 1 ATOM 2473 C CA . ALA A 1 308 ? 20.959 68.861 -8.546 1.00 26.29 ? 308 ALA A CA 1 ATOM 2474 C C . ALA A 1 308 ? 19.828 67.852 -8.403 1.00 25.72 ? 308 ALA A C 1 ATOM 2475 O O . ALA A 1 308 ? 18.829 67.901 -9.127 1.00 25.00 ? 308 ALA A O 1 ATOM 2476 C CB . ALA A 1 308 ? 20.559 70.203 -7.944 1.00 23.50 ? 308 ALA A CB 1 ATOM 2477 N N . GLY A 1 309 ? 20.009 66.927 -7.469 1.00 24.85 ? 309 GLY A N 1 ATOM 2478 C CA . GLY A 1 309 ? 19.001 65.920 -7.226 1.00 23.36 ? 309 GLY A CA 1 ATOM 2479 C C . GLY A 1 309 ? 19.335 64.532 -7.737 1.00 22.90 ? 309 GLY A C 1 ATOM 2480 O O . GLY A 1 309 ? 19.828 64.352 -8.852 1.00 21.24 ? 309 GLY A O 1 ATOM 2481 N N . LEU A 1 310 ? 19.067 63.542 -6.896 1.00 22.28 ? 310 LEU A N 1 ATOM 2482 C CA . LEU A 1 310 ? 19.289 62.149 -7.243 1.00 22.47 ? 310 LEU A CA 1 ATOM 2483 C C . LEU A 1 310 ? 18.060 61.389 -6.790 1.00 22.31 ? 310 LEU A C 1 ATOM 2484 O O . LEU A 1 310 ? 17.219 61.914 -6.059 1.00 21.80 ? 310 LEU A O 1 ATOM 2485 C CB . LEU A 1 310 ? 20.492 61.566 -6.494 1.00 20.99 ? 310 LEU A CB 1 ATOM 2486 C CG . LEU A 1 310 ? 21.907 62.082 -6.738 1.00 22.10 ? 310 LEU A CG 1 ATOM 2487 C CD1 . LEU A 1 310 ? 22.874 61.285 -5.866 1.00 20.28 ? 310 LEU A CD1 1 ATOM 2488 C CD2 . LEU A 1 310 ? 22.267 61.942 -8.208 1.00 20.94 ? 310 LEU A CD2 1 ATOM 2489 N N . GLN A 1 311 ? 17.954 60.150 -7.242 1.00 22.36 ? 311 GLN A N 1 ATOM 2490 C CA . GLN A 1 311 ? 16.875 59.281 -6.820 1.00 22.10 ? 311 GLN A CA 1 ATOM 2491 C C . GLN A 1 311 ? 17.619 58.180 -6.083 1.00 22.94 ? 311 GLN A C 1 ATOM 2492 O O . GLN A 1 311 ? 18.747 57.830 -6.453 1.00 22.40 ? 311 GLN A O 1 ATOM 2493 C CB . GLN A 1 311 ? 16.140 58.675 -8.017 1.00 21.96 ? 311 GLN A CB 1 ATOM 2494 C CG . GLN A 1 311 ? 15.193 59.613 -8.744 1.00 25.54 ? 311 GLN A CG 1 ATOM 2495 C CD . GLN A 1 311 ? 14.080 60.146 -7.851 1.00 26.54 ? 311 GLN A CD 1 ATOM 2496 O OE1 . GLN A 1 311 ? 13.409 59.386 -7.140 1.00 26.49 ? 311 GLN A OE1 1 ATOM 2497 N NE2 . GLN A 1 311 ? 13.867 61.456 -7.897 1.00 24.93 ? 311 GLN A NE2 1 ATOM 2498 N N . SER A 1 312 ? 17.022 57.657 -5.021 1.00 22.81 ? 312 SER A N 1 ATOM 2499 C CA . SER A 1 312 ? 17.646 56.563 -4.292 1.00 22.24 ? 312 SER A CA 1 ATOM 2500 C C . SER A 1 312 ? 17.560 55.365 -5.233 1.00 22.92 ? 312 SER A C 1 ATOM 2501 O O . SER A 1 312 ? 16.795 55.383 -6.203 1.00 21.22 ? 312 SER A O 1 ATOM 2502 C CB . SER A 1 312 ? 16.857 56.268 -3.022 1.00 22.30 ? 312 SER A CB 1 ATOM 2503 O OG . SER A 1 312 ? 15.483 56.095 -3.329 1.00 22.70 ? 312 SER A OG 1 ATOM 2504 N N . PHE A 1 313 ? 18.346 54.327 -4.985 1.00 22.92 ? 313 PHE A N 1 ATOM 2505 C CA . PHE A 1 313 ? 18.242 53.171 -5.854 1.00 22.43 ? 313 PHE A CA 1 ATOM 2506 C C . PHE A 1 313 ? 16.913 52.524 -5.504 1.00 22.77 ? 313 PHE A C 1 ATOM 2507 O O . PHE A 1 313 ? 16.587 52.362 -4.326 1.00 21.52 ? 313 PHE A O 1 ATOM 2508 C CB . PHE A 1 313 ? 19.365 52.178 -5.613 1.00 23.90 ? 313 PHE A CB 1 ATOM 2509 C CG . PHE A 1 313 ? 19.412 51.100 -6.637 1.00 26.07 ? 313 PHE A CG 1 ATOM 2510 C CD1 . PHE A 1 313 ? 19.863 51.374 -7.921 1.00 27.35 ? 313 PHE A CD1 1 ATOM 2511 C CD2 . PHE A 1 313 ? 18.933 49.830 -6.351 1.00 26.75 ? 313 PHE A CD2 1 ATOM 2512 C CE1 . PHE A 1 313 ? 19.832 50.402 -8.906 1.00 28.45 ? 313 PHE A CE1 1 ATOM 2513 C CE2 . PHE A 1 313 ? 18.898 48.850 -7.330 1.00 27.09 ? 313 PHE A CE2 1 ATOM 2514 C CZ . PHE A 1 313 ? 19.346 49.137 -8.611 1.00 27.90 ? 313 PHE A CZ 1 ATOM 2515 N N . PRO A 1 314 ? 16.123 52.145 -6.514 1.00 22.33 ? 314 PRO A N 1 ATOM 2516 C CA . PRO A 1 314 ? 14.831 51.526 -6.194 1.00 21.93 ? 314 PRO A CA 1 ATOM 2517 C C . PRO A 1 314 ? 14.945 50.323 -5.261 1.00 23.12 ? 314 PRO A C 1 ATOM 2518 O O . PRO A 1 314 ? 15.760 49.430 -5.489 1.00 23.29 ? 314 PRO A O 1 ATOM 2519 C CB . PRO A 1 314 ? 14.263 51.166 -7.570 1.00 22.47 ? 314 PRO A CB 1 ATOM 2520 C CG . PRO A 1 314 ? 15.476 51.023 -8.434 1.00 23.46 ? 314 PRO A CG 1 ATOM 2521 C CD . PRO A 1 314 ? 16.381 52.132 -7.964 1.00 22.04 ? 314 PRO A CD 1 ATOM 2522 N N . ARG A 1 315 ? 14.149 50.302 -4.197 1.00 21.93 ? 315 ARG A N 1 ATOM 2523 C CA . ARG A 1 315 ? 14.209 49.170 -3.289 1.00 22.07 ? 315 ARG A CA 1 ATOM 2524 C C . ARG A 1 315 ? 12.893 48.445 -3.024 1.00 22.08 ? 315 ARG A C 1 ATOM 2525 O O . ARG A 1 315 ? 11.809 49.031 -3.088 1.00 20.95 ? 315 ARG A O 1 ATOM 2526 C CB . ARG A 1 315 ? 14.893 49.563 -1.965 1.00 23.19 ? 315 ARG A CB 1 ATOM 2527 C CG . ARG A 1 315 ? 14.558 50.917 -1.376 1.00 21.58 ? 315 ARG A CG 1 ATOM 2528 C CD . ARG A 1 315 ? 15.833 51.629 -0.892 1.00 20.23 ? 315 ARG A CD 1 ATOM 2529 N NE . ARG A 1 315 ? 15.600 52.364 0.347 1.00 21.56 ? 315 ARG A NE 1 ATOM 2530 C CZ . ARG A 1 315 ? 16.452 53.221 0.910 1.00 20.15 ? 315 ARG A CZ 1 ATOM 2531 N NH1 . ARG A 1 315 ? 17.626 53.490 0.361 1.00 15.55 ? 315 ARG A NH1 1 ATOM 2532 N NH2 . ARG A 1 315 ? 16.123 53.801 2.052 1.00 22.47 ? 315 ARG A NH2 1 ATOM 2533 N N . ALA A 1 316 ? 13.004 47.144 -2.771 1.00 22.07 ? 316 ALA A N 1 ATOM 2534 C CA . ALA A 1 316 ? 11.847 46.311 -2.482 1.00 21.92 ? 316 ALA A CA 1 ATOM 2535 C C . ALA A 1 316 ? 11.403 46.657 -1.074 1.00 21.99 ? 316 ALA A C 1 ATOM 2536 O O . ALA A 1 316 ? 12.225 46.888 -0.182 1.00 20.95 ? 316 ALA A O 1 ATOM 2537 C CB . ALA A 1 316 ? 12.209 44.843 -2.579 1.00 21.45 ? 316 ALA A CB 1 ATOM 2538 N N . LEU A 1 317 ? 10.095 46.681 -0.880 1.00 22.17 ? 317 LEU A N 1 ATOM 2539 C CA . LEU A 1 317 ? 9.525 47.054 0.393 1.00 23.51 ? 317 LEU A CA 1 ATOM 2540 C C . LEU A 1 317 ? 8.574 45.983 0.890 1.00 24.15 ? 317 LEU A C 1 ATOM 2541 O O . LEU A 1 317 ? 7.713 45.529 0.143 1.00 26.11 ? 317 LEU A O 1 ATOM 2542 C CB . LEU A 1 317 ? 8.780 48.377 0.203 1.00 24.36 ? 317 LEU A CB 1 ATOM 2543 C CG . LEU A 1 317 ? 8.091 49.092 1.358 1.00 25.54 ? 317 LEU A CG 1 ATOM 2544 C CD1 . LEU A 1 317 ? 9.117 49.476 2.413 1.00 27.28 ? 317 LEU A CD1 1 ATOM 2545 C CD2 . LEU A 1 317 ? 7.391 50.332 0.816 1.00 26.20 ? 317 LEU A CD2 1 ATOM 2546 N N . TRP A 1 318 ? 8.733 45.568 2.141 1.00 23.72 ? 318 TRP A N 1 ATOM 2547 C CA . TRP A 1 318 ? 7.834 44.570 2.711 1.00 24.63 ? 318 TRP A CA 1 ATOM 2548 C C . TRP A 1 318 ? 7.790 44.728 4.231 1.00 25.93 ? 318 TRP A C 1 ATOM 2549 O O . TRP A 1 318 ? 8.603 45.454 4.811 1.00 25.39 ? 318 TRP A O 1 ATOM 2550 C CB . TRP A 1 318 ? 8.264 43.154 2.296 1.00 23.43 ? 318 TRP A CB 1 ATOM 2551 C CG . TRP A 1 318 ? 9.549 42.676 2.888 1.00 24.53 ? 318 TRP A CG 1 ATOM 2552 C CD1 . TRP A 1 318 ? 9.714 42.056 4.094 1.00 25.06 ? 318 TRP A CD1 1 ATOM 2553 C CD2 . TRP A 1 318 ? 10.859 42.797 2.318 1.00 23.95 ? 318 TRP A CD2 1 ATOM 2554 N NE1 . TRP A 1 318 ? 11.045 41.783 4.312 1.00 24.23 ? 318 TRP A NE1 1 ATOM 2555 C CE2 . TRP A 1 318 ? 11.770 42.227 3.237 1.00 24.88 ? 318 TRP A CE2 1 ATOM 2556 C CE3 . TRP A 1 318 ? 11.352 43.331 1.120 1.00 24.76 ? 318 TRP A CE3 1 ATOM 2557 C CZ2 . TRP A 1 318 ? 13.151 42.177 2.997 1.00 24.45 ? 318 TRP A CZ2 1 ATOM 2558 C CZ3 . TRP A 1 318 ? 12.729 43.282 0.879 1.00 24.73 ? 318 TRP A CZ3 1 ATOM 2559 C CH2 . TRP A 1 318 ? 13.609 42.708 1.816 1.00 25.45 ? 318 TRP A CH2 1 ATOM 2560 N N . ILE A 1 319 ? 6.829 44.078 4.880 1.00 26.92 ? 319 ILE A N 1 ATOM 2561 C CA . ILE A 1 319 ? 6.712 44.192 6.327 1.00 28.10 ? 319 ILE A CA 1 ATOM 2562 C C . ILE A 1 319 ? 7.510 43.107 7.031 1.00 29.68 ? 319 ILE A C 1 ATOM 2563 O O . ILE A 1 319 ? 7.565 41.971 6.572 1.00 29.02 ? 319 ILE A O 1 ATOM 2564 C CB . ILE A 1 319 ? 5.242 44.119 6.780 1.00 28.34 ? 319 ILE A CB 1 ATOM 2565 C CG1 . ILE A 1 319 ? 5.131 44.600 8.228 1.00 27.83 ? 319 ILE A CG1 1 ATOM 2566 C CG2 . ILE A 1 319 ? 4.722 42.693 6.653 1.00 28.28 ? 319 ILE A CG2 1 ATOM 2567 C CD1 . ILE A 1 319 ? 3.717 44.846 8.677 1.00 27.19 ? 319 ILE A CD1 1 ATOM 2568 N N . ASP A 1 320 ? 8.132 43.471 8.148 1.00 33.01 ? 320 ASP A N 1 ATOM 2569 C CA . ASP A 1 320 ? 8.943 42.540 8.921 1.00 35.96 ? 320 ASP A CA 1 ATOM 2570 C C . ASP A 1 320 ? 8.115 41.405 9.506 1.00 37.47 ? 320 ASP A C 1 ATOM 2571 O O . ASP A 1 320 ? 6.913 41.550 9.719 1.00 35.75 ? 320 ASP A O 1 ATOM 2572 C CB . ASP A 1 320 ? 9.648 43.274 10.058 1.00 37.53 ? 320 ASP A CB 1 ATOM 2573 C CG . ASP A 1 320 ? 10.631 42.389 10.790 1.00 39.23 ? 320 ASP A CG 1 ATOM 2574 O OD1 . ASP A 1 320 ? 11.654 41.999 10.187 1.00 44.00 ? 320 ASP A OD1 1 ATOM 2575 O OD2 . ASP A 1 320 ? 10.382 42.071 11.964 1.00 40.94 ? 320 ASP A OD2 1 ATOM 2576 N N . ARG A 1 321 ? 8.765 40.277 9.772 1.00 40.49 ? 321 ARG A N 1 ATOM 2577 C CA . ARG A 1 321 ? 8.072 39.128 10.337 1.00 44.57 ? 321 ARG A CA 1 ATOM 2578 C C . ARG A 1 321 ? 7.308 39.505 11.614 1.00 44.44 ? 321 ARG A C 1 ATOM 2579 O O . ARG A 1 321 ? 6.270 38.914 11.908 1.00 44.29 ? 321 ARG A O 1 ATOM 2580 C CB . ARG A 1 321 ? 9.060 37.988 10.632 1.00 49.43 ? 321 ARG A CB 1 ATOM 2581 C CG . ARG A 1 321 ? 10.131 38.311 11.675 1.00 60.09 ? 321 ARG A CG 1 ATOM 2582 C CD . ARG A 1 321 ? 11.426 38.871 11.053 1.00 69.19 ? 321 ARG A CD 1 ATOM 2583 N NE . ARG A 1 321 ? 12.370 39.354 12.069 1.00 75.45 ? 321 ARG A NE 1 ATOM 2584 C CZ . ARG A 1 321 ? 13.664 39.588 11.849 1.00 77.84 ? 321 ARG A CZ 1 ATOM 2585 N NH1 . ARG A 1 321 ? 14.186 39.379 10.645 1.00 79.45 ? 321 ARG A NH1 1 ATOM 2586 N NH2 . ARG A 1 321 ? 14.437 40.035 12.834 1.00 79.51 ? 321 ARG A NH2 1 ATOM 2587 N N . ASN A 1 322 ? 7.806 40.494 12.359 1.00 43.93 ? 322 ASN A N 1 ATOM 2588 C CA . ASN A 1 322 ? 7.149 40.918 13.597 1.00 43.22 ? 322 ASN A CA 1 ATOM 2589 C C . ASN A 1 322 ? 5.984 41.882 13.386 1.00 40.82 ? 322 ASN A C 1 ATOM 2590 O O . ASN A 1 322 ? 5.300 42.246 14.341 1.00 40.70 ? 322 ASN A O 1 ATOM 2591 C CB . ASN A 1 322 ? 8.156 41.554 14.568 1.00 48.69 ? 322 ASN A CB 1 ATOM 2592 C CG . ASN A 1 322 ? 8.737 42.878 14.051 1.00 54.63 ? 322 ASN A CG 1 ATOM 2593 O OD1 . ASN A 1 322 ? 8.038 43.696 13.445 1.00 54.44 ? 322 ASN A OD1 1 ATOM 2594 N ND2 . ASN A 1 322 ? 10.027 43.095 14.315 1.00 58.93 ? 322 ASN A ND2 1 ATOM 2595 N N . GLY A 1 323 ? 5.776 42.307 12.143 1.00 38.50 ? 323 GLY A N 1 ATOM 2596 C CA . GLY A 1 323 ? 4.681 43.211 11.822 1.00 34.74 ? 323 GLY A CA 1 ATOM 2597 C C . GLY A 1 323 ? 4.714 44.609 12.417 1.00 33.62 ? 323 GLY A C 1 ATOM 2598 O O . GLY A 1 323 ? 3.731 45.337 12.313 1.00 32.91 ? 323 GLY A O 1 ATOM 2599 N N . LYS A 1 324 ? 5.834 45.004 13.018 1.00 32.84 ? 324 LYS A N 1 ATOM 2600 C CA . LYS A 1 324 ? 5.932 46.322 13.640 1.00 32.74 ? 324 LYS A CA 1 ATOM 2601 C C . LYS A 1 324 ? 6.638 47.396 12.820 1.00 30.21 ? 324 LYS A C 1 ATOM 2602 O O . LYS A 1 324 ? 6.601 48.574 13.181 1.00 28.53 ? 324 LYS A O 1 ATOM 2603 C CB . LYS A 1 324 ? 6.612 46.213 15.000 1.00 36.15 ? 324 LYS A CB 1 ATOM 2604 C CG . LYS A 1 324 ? 5.876 45.340 16.003 1.00 42.45 ? 324 LYS A CG 1 ATOM 2605 C CD . LYS A 1 324 ? 6.618 45.336 17.335 1.00 50.73 ? 324 LYS A CD 1 ATOM 2606 C CE . LYS A 1 324 ? 8.076 44.872 17.158 1.00 54.50 ? 324 LYS A CE 1 ATOM 2607 N NZ . LYS A 1 324 ? 8.943 45.153 18.351 1.00 56.80 ? 324 LYS A NZ 1 ATOM 2608 N N . GLN A 1 325 ? 7.293 46.994 11.734 1.00 28.88 ? 325 GLN A N 1 ATOM 2609 C CA . GLN A 1 325 ? 7.984 47.941 10.860 1.00 27.79 ? 325 GLN A CA 1 ATOM 2610 C C . GLN A 1 325 ? 8.173 47.390 9.453 1.00 27.08 ? 325 GLN A C 1 ATOM 2611 O O . GLN A 1 325 ? 7.958 46.202 9.192 1.00 27.40 ? 325 GLN A O 1 ATOM 2612 C CB . GLN A 1 325 ? 9.357 48.314 11.415 1.00 27.24 ? 325 GLN A CB 1 ATOM 2613 C CG . GLN A 1 325 ? 10.340 47.165 11.428 1.00 29.79 ? 325 GLN A CG 1 ATOM 2614 C CD . GLN A 1 325 ? 11.783 47.626 11.519 1.00 31.09 ? 325 GLN A CD 1 ATOM 2615 O OE1 . GLN A 1 325 ? 12.331 48.179 10.562 1.00 31.89 ? 325 GLN A OE1 1 ATOM 2616 N NE2 . GLN A 1 325 ? 12.406 47.403 12.670 1.00 31.69 ? 325 GLN A NE2 1 ATOM 2617 N N . LEU A 1 326 ? 8.587 48.275 8.554 1.00 24.82 ? 326 LEU A N 1 ATOM 2618 C CA . LEU A 1 326 ? 8.830 47.929 7.163 1.00 23.49 ? 326 LEU A CA 1 ATOM 2619 C C . LEU A 1 326 ? 10.308 47.604 6.928 1.00 23.32 ? 326 LEU A C 1 ATOM 2620 O O . LEU A 1 326 ? 11.184 48.063 7.661 1.00 22.67 ? 326 LEU A O 1 ATOM 2621 C CB . LEU A 1 326 ? 8.402 49.097 6.271 1.00 22.53 ? 326 LEU A CB 1 ATOM 2622 C CG . LEU A 1 326 ? 6.994 49.099 5.670 1.00 22.98 ? 326 LEU A CG 1 ATOM 2623 C CD1 . LEU A 1 326 ? 6.031 48.339 6.547 1.00 23.52 ? 326 LEU A CD1 1 ATOM 2624 C CD2 . LEU A 1 326 ? 6.545 50.543 5.456 1.00 20.89 ? 326 LEU A CD2 1 ATOM 2625 N N . ILE A 1 327 ? 10.575 46.795 5.909 1.00 23.05 ? 327 ILE A N 1 ATOM 2626 C CA . ILE A 1 327 ? 11.942 46.426 5.566 1.00 23.48 ? 327 ILE A CA 1 ATOM 2627 C C . ILE A 1 327 ? 12.220 46.869 4.131 1.00 24.78 ? 327 ILE A C 1 ATOM 2628 O O . ILE A 1 327 ? 11.341 46.769 3.261 1.00 25.11 ? 327 ILE A O 1 ATOM 2629 C CB . ILE A 1 327 ? 12.161 44.890 5.647 1.00 23.45 ? 327 ILE A CB 1 ATOM 2630 C CG1 . ILE A 1 327 ? 11.748 44.361 7.023 1.00 23.36 ? 327 ILE A CG1 1 ATOM 2631 C CG2 . ILE A 1 327 ? 13.622 44.558 5.361 1.00 19.86 ? 327 ILE A CG2 1 ATOM 2632 C CD1 . ILE A 1 327 ? 12.576 44.898 8.173 1.00 24.07 ? 327 ILE A CD1 1 ATOM 2633 N N . GLN A 1 328 ? 13.433 47.356 3.884 1.00 22.35 ? 328 GLN A N 1 ATOM 2634 C CA . GLN A 1 328 ? 13.821 47.795 2.547 1.00 21.56 ? 328 GLN A CA 1 ATOM 2635 C C . GLN A 1 328 ? 15.110 47.128 2.106 1.00 22.04 ? 328 GLN A C 1 ATOM 2636 O O . GLN A 1 328 ? 16.000 46.875 2.919 1.00 20.92 ? 328 GLN A O 1 ATOM 2637 C CB . GLN A 1 328 ? 14.020 49.305 2.506 1.00 21.42 ? 328 GLN A CB 1 ATOM 2638 C CG . GLN A 1 328 ? 12.755 50.108 2.551 1.00 21.96 ? 328 GLN A CG 1 ATOM 2639 C CD . GLN A 1 328 ? 13.025 51.510 3.028 1.00 23.64 ? 328 GLN A CD 1 ATOM 2640 O OE1 . GLN A 1 328 ? 13.076 51.764 4.231 1.00 24.36 ? 328 GLN A OE1 1 ATOM 2641 N NE2 . GLN A 1 328 ? 13.231 52.427 2.091 1.00 23.27 ? 328 GLN A NE2 1 ATOM 2642 N N . TRP A 1 329 ? 15.215 46.867 0.811 1.00 19.65 ? 329 TRP A N 1 ATOM 2643 C CA . TRP A 1 329 ? 16.400 46.230 0.271 1.00 19.80 ? 329 TRP A CA 1 ATOM 2644 C C . TRP A 1 329 ? 16.467 46.559 -1.208 1.00 21.54 ? 329 TRP A C 1 ATOM 2645 O O . TRP A 1 329 ? 15.453 46.497 -1.910 1.00 21.50 ? 329 TRP A O 1 ATOM 2646 C CB . TRP A 1 329 ? 16.309 44.715 0.472 1.00 19.39 ? 329 TRP A CB 1 ATOM 2647 C CG . TRP A 1 329 ? 17.617 44.014 0.387 1.00 20.93 ? 329 TRP A CG 1 ATOM 2648 C CD1 . TRP A 1 329 ? 18.025 43.152 -0.591 1.00 21.28 ? 329 TRP A CD1 1 ATOM 2649 C CD2 . TRP A 1 329 ? 18.697 44.097 1.326 1.00 20.89 ? 329 TRP A CD2 1 ATOM 2650 N NE1 . TRP A 1 329 ? 19.293 42.688 -0.318 1.00 19.11 ? 329 TRP A NE1 1 ATOM 2651 C CE2 . TRP A 1 329 ? 19.728 43.252 0.854 1.00 21.13 ? 329 TRP A CE2 1 ATOM 2652 C CE3 . TRP A 1 329 ? 18.894 44.805 2.520 1.00 20.02 ? 329 TRP A CE3 1 ATOM 2653 C CZ2 . TRP A 1 329 ? 20.939 43.092 1.537 1.00 19.47 ? 329 TRP A CZ2 1 ATOM 2654 C CZ3 . TRP A 1 329 ? 20.100 44.648 3.200 1.00 20.40 ? 329 TRP A CZ3 1 ATOM 2655 C CH2 . TRP A 1 329 ? 21.106 43.796 2.704 1.00 20.93 ? 329 TRP A CH2 1 ATOM 2656 N N . PRO A 1 330 ? 17.655 46.931 -1.704 1.00 20.83 ? 330 PRO A N 1 ATOM 2657 C CA . PRO A 1 330 ? 17.742 47.251 -3.126 1.00 20.04 ? 330 PRO A CA 1 ATOM 2658 C C . PRO A 1 330 ? 17.318 46.082 -4.011 1.00 21.15 ? 330 PRO A C 1 ATOM 2659 O O . PRO A 1 330 ? 17.695 44.937 -3.751 1.00 20.35 ? 330 PRO A O 1 ATOM 2660 C CB . PRO A 1 330 ? 19.210 47.666 -3.308 1.00 21.12 ? 330 PRO A CB 1 ATOM 2661 C CG . PRO A 1 330 ? 19.916 47.100 -2.126 1.00 22.20 ? 330 PRO A CG 1 ATOM 2662 C CD . PRO A 1 330 ? 18.922 47.214 -1.012 1.00 22.34 ? 330 PRO A CD 1 ATOM 2663 N N . VAL A 1 331 ? 16.520 46.378 -5.040 1.00 20.40 ? 331 VAL A N 1 ATOM 2664 C CA . VAL A 1 331 ? 16.028 45.355 -5.960 1.00 20.50 ? 331 VAL A CA 1 ATOM 2665 C C . VAL A 1 331 ? 17.167 44.496 -6.500 1.00 22.55 ? 331 VAL A C 1 ATOM 2666 O O . VAL A 1 331 ? 18.238 44.998 -6.847 1.00 22.73 ? 331 VAL A O 1 ATOM 2667 C CB . VAL A 1 331 ? 15.233 45.983 -7.130 1.00 20.69 ? 331 VAL A CB 1 ATOM 2668 C CG1 . VAL A 1 331 ? 14.003 46.681 -6.587 1.00 18.89 ? 331 VAL A CG1 1 ATOM 2669 C CG2 . VAL A 1 331 ? 16.099 46.961 -7.901 1.00 19.13 ? 331 VAL A CG2 1 ATOM 2670 N N . GLU A 1 332 ? 16.920 43.194 -6.570 1.00 24.11 ? 332 GLU A N 1 ATOM 2671 C CA . GLU A 1 332 ? 17.925 42.232 -7.007 1.00 24.81 ? 332 GLU A CA 1 ATOM 2672 C C . GLU A 1 332 ? 18.655 42.559 -8.304 1.00 24.42 ? 332 GLU A C 1 ATOM 2673 O O . GLU A 1 332 ? 19.819 42.180 -8.472 1.00 23.64 ? 332 GLU A O 1 ATOM 2674 C CB . GLU A 1 332 ? 17.292 40.850 -7.109 1.00 25.95 ? 332 GLU A CB 1 ATOM 2675 C CG . GLU A 1 332 ? 16.259 40.733 -8.198 1.00 33.63 ? 332 GLU A CG 1 ATOM 2676 C CD . GLU A 1 332 ? 15.471 39.443 -8.103 1.00 38.79 ? 332 GLU A CD 1 ATOM 2677 O OE1 . GLU A 1 332 ? 16.032 38.442 -7.597 1.00 40.85 ? 332 GLU A OE1 1 ATOM 2678 O OE2 . GLU A 1 332 ? 14.299 39.427 -8.545 1.00 40.90 ? 332 GLU A OE2 1 ATOM 2679 N N . GLU A 1 333 ? 17.989 43.263 -9.213 1.00 23.06 ? 333 GLU A N 1 ATOM 2680 C CA . GLU A 1 333 ? 18.609 43.624 -10.485 1.00 22.33 ? 333 GLU A CA 1 ATOM 2681 C C . GLU A 1 333 ? 19.939 44.352 -10.329 1.00 22.91 ? 333 GLU A C 1 ATOM 2682 O O . GLU A 1 333 ? 20.774 44.313 -11.230 1.00 23.71 ? 333 GLU A O 1 ATOM 2683 C CB . GLU A 1 333 ? 17.670 44.490 -11.329 1.00 22.41 ? 333 GLU A CB 1 ATOM 2684 C CG . GLU A 1 333 ? 16.499 43.743 -11.933 1.00 23.34 ? 333 GLU A CG 1 ATOM 2685 C CD . GLU A 1 333 ? 15.356 43.534 -10.954 1.00 27.02 ? 333 GLU A CD 1 ATOM 2686 O OE1 . GLU A 1 333 ? 15.535 43.802 -9.742 1.00 28.13 ? 333 GLU A OE1 1 ATOM 2687 O OE2 . GLU A 1 333 ? 14.274 43.097 -11.406 1.00 27.62 ? 333 GLU A OE2 1 ATOM 2688 N N . ILE A 1 334 ? 20.142 45.017 -9.195 1.00 22.42 ? 334 ILE A N 1 ATOM 2689 C CA . ILE A 1 334 ? 21.383 45.747 -8.984 1.00 23.40 ? 334 ILE A CA 1 ATOM 2690 C C . ILE A 1 334 ? 22.566 44.792 -8.918 1.00 24.36 ? 334 ILE A C 1 ATOM 2691 O O . ILE A 1 334 ? 23.693 45.160 -9.243 1.00 22.51 ? 334 ILE A O 1 ATOM 2692 C CB . ILE A 1 334 ? 21.342 46.581 -7.677 1.00 24.08 ? 334 ILE A CB 1 ATOM 2693 C CG1 . ILE A 1 334 ? 22.466 47.628 -7.687 1.00 23.35 ? 334 ILE A CG1 1 ATOM 2694 C CG2 . ILE A 1 334 ? 21.503 45.667 -6.463 1.00 23.41 ? 334 ILE A CG2 1 ATOM 2695 C CD1 . ILE A 1 334 ? 22.403 48.628 -6.540 1.00 22.75 ? 334 ILE A CD1 1 ATOM 2696 N N . GLU A 1 335 ? 22.306 43.558 -8.508 1.00 25.95 ? 335 GLU A N 1 ATOM 2697 C CA . GLU A 1 335 ? 23.375 42.583 -8.391 1.00 28.90 ? 335 GLU A CA 1 ATOM 2698 C C . GLU A 1 335 ? 24.089 42.293 -9.708 1.00 29.93 ? 335 GLU A C 1 ATOM 2699 O O . GLU A 1 335 ? 25.242 41.868 -9.709 1.00 29.10 ? 335 GLU A O 1 ATOM 2700 C CB . GLU A 1 335 ? 22.827 41.308 -7.759 1.00 30.48 ? 335 GLU A CB 1 ATOM 2701 C CG . GLU A 1 335 ? 22.575 41.488 -6.266 1.00 35.11 ? 335 GLU A CG 1 ATOM 2702 C CD . GLU A 1 335 ? 21.609 40.471 -5.694 1.00 37.85 ? 335 GLU A CD 1 ATOM 2703 O OE1 . GLU A 1 335 ? 21.742 39.272 -6.032 1.00 37.69 ? 335 GLU A OE1 1 ATOM 2704 O OE2 . GLU A 1 335 ? 20.725 40.875 -4.899 1.00 37.61 ? 335 GLU A OE2 1 ATOM 2705 N N . GLU A 1 336 ? 23.420 42.552 -10.826 1.00 30.60 ? 336 GLU A N 1 ATOM 2706 C CA . GLU A 1 336 ? 24.016 42.319 -12.136 1.00 32.31 ? 336 GLU A CA 1 ATOM 2707 C C . GLU A 1 336 ? 25.119 43.316 -12.457 1.00 31.56 ? 336 GLU A C 1 ATOM 2708 O O . GLU A 1 336 ? 25.831 43.152 -13.445 1.00 34.22 ? 336 GLU A O 1 ATOM 2709 C CB . GLU A 1 336 ? 22.951 42.387 -13.230 1.00 36.72 ? 336 GLU A CB 1 ATOM 2710 C CG . GLU A 1 336 ? 21.890 41.318 -13.091 1.00 46.51 ? 336 GLU A CG 1 ATOM 2711 C CD . GLU A 1 336 ? 22.483 39.915 -13.120 1.00 52.36 ? 336 GLU A CD 1 ATOM 2712 O OE1 . GLU A 1 336 ? 22.990 39.509 -14.193 1.00 55.44 ? 336 GLU A OE1 1 ATOM 2713 O OE2 . GLU A 1 336 ? 22.450 39.226 -12.068 1.00 54.38 ? 336 GLU A OE2 1 ATOM 2714 N N . LEU A 1 337 ? 25.255 44.348 -11.631 1.00 28.55 ? 337 LEU A N 1 ATOM 2715 C CA . LEU A 1 337 ? 26.283 45.359 -11.852 1.00 26.53 ? 337 LEU A CA 1 ATOM 2716 C C . LEU A 1 337 ? 27.580 44.961 -11.161 1.00 26.42 ? 337 LEU A C 1 ATOM 2717 O O . LEU A 1 337 ? 28.638 45.529 -11.427 1.00 26.33 ? 337 LEU A O 1 ATOM 2718 C CB . LEU A 1 337 ? 25.821 46.725 -11.330 1.00 24.90 ? 337 LEU A CB 1 ATOM 2719 C CG . LEU A 1 337 ? 24.641 47.421 -12.021 1.00 23.86 ? 337 LEU A CG 1 ATOM 2720 C CD1 . LEU A 1 337 ? 24.334 48.734 -11.309 1.00 20.05 ? 337 LEU A CD1 1 ATOM 2721 C CD2 . LEU A 1 337 ? 24.967 47.675 -13.485 1.00 20.06 ? 337 LEU A CD2 1 ATOM 2722 N N . ARG A 1 338 ? 27.490 43.976 -10.273 1.00 26.02 ? 338 ARG A N 1 ATOM 2723 C CA . ARG A 1 338 ? 28.655 43.510 -9.534 1.00 26.47 ? 338 ARG A CA 1 ATOM 2724 C C . ARG A 1 338 ? 29.717 42.938 -10.462 1.00 27.73 ? 338 ARG A C 1 ATOM 2725 O O . ARG A 1 338 ? 29.417 42.131 -11.338 1.00 28.21 ? 338 ARG A O 1 ATOM 2726 C CB . ARG A 1 338 ? 28.225 42.467 -8.496 1.00 23.88 ? 338 ARG A CB 1 ATOM 2727 C CG . ARG A 1 338 ? 27.412 43.065 -7.357 1.00 22.41 ? 338 ARG A CG 1 ATOM 2728 C CD . ARG A 1 338 ? 26.840 42.008 -6.432 1.00 21.70 ? 338 ARG A CD 1 ATOM 2729 N NE . ARG A 1 338 ? 26.212 42.611 -5.259 1.00 21.60 ? 338 ARG A NE 1 ATOM 2730 C CZ . ARG A 1 338 ? 25.621 41.923 -4.284 1.00 22.41 ? 338 ARG A CZ 1 ATOM 2731 N NH1 . ARG A 1 338 ? 25.572 40.598 -4.343 1.00 19.86 ? 338 ARG A NH1 1 ATOM 2732 N NH2 . ARG A 1 338 ? 25.089 42.558 -3.242 1.00 20.10 ? 338 ARG A NH2 1 ATOM 2733 N N . GLN A 1 339 ? 30.957 43.380 -10.270 1.00 29.54 ? 339 GLN A N 1 ATOM 2734 C CA . GLN A 1 339 ? 32.088 42.923 -11.074 1.00 30.60 ? 339 GLN A CA 1 ATOM 2735 C C . GLN A 1 339 ? 32.963 41.995 -10.238 1.00 30.25 ? 339 GLN A C 1 ATOM 2736 O O . GLN A 1 339 ? 32.513 40.930 -9.816 1.00 30.04 ? 339 GLN A O 1 ATOM 2737 C CB . GLN A 1 339 ? 32.902 44.127 -11.561 1.00 34.30 ? 339 GLN A CB 1 ATOM 2738 C CG . GLN A 1 339 ? 32.130 45.053 -12.481 1.00 40.85 ? 339 GLN A CG 1 ATOM 2739 C CD . GLN A 1 339 ? 31.640 44.341 -13.739 1.00 47.40 ? 339 GLN A CD 1 ATOM 2740 O OE1 . GLN A 1 339 ? 32.405 44.112 -14.684 1.00 50.08 ? 339 GLN A OE1 1 ATOM 2741 N NE2 . GLN A 1 339 ? 30.359 43.975 -13.750 1.00 48.51 ? 339 GLN A NE2 1 ATOM 2742 N N . ASN A 1 340 ? 34.209 42.392 -9.995 1.00 30.33 ? 340 ASN A N 1 ATOM 2743 C CA . ASN A 1 340 ? 35.112 41.575 -9.191 1.00 29.70 ? 340 ASN A CA 1 ATOM 2744 C C . ASN A 1 340 ? 34.715 41.694 -7.724 1.00 30.52 ? 340 ASN A C 1 ATOM 2745 O O . ASN A 1 340 ? 34.111 42.687 -7.306 1.00 29.52 ? 340 ASN A O 1 ATOM 2746 C CB . ASN A 1 340 ? 36.566 42.021 -9.371 1.00 29.29 ? 340 ASN A CB 1 ATOM 2747 C CG . ASN A 1 340 ? 36.832 43.397 -8.789 1.00 30.14 ? 340 ASN A CG 1 ATOM 2748 O OD1 . ASN A 1 340 ? 36.293 44.401 -9.258 1.00 29.36 ? 340 ASN A OD1 1 ATOM 2749 N ND2 . ASN A 1 340 ? 37.665 43.448 -7.758 1.00 28.57 ? 340 ASN A ND2 1 ATOM 2750 N N . GLN A 1 341 ? 35.060 40.680 -6.940 1.00 30.45 ? 341 GLN A N 1 ATOM 2751 C CA . GLN A 1 341 ? 34.712 40.670 -5.534 1.00 30.49 ? 341 GLN A CA 1 ATOM 2752 C C . GLN A 1 341 ? 35.922 40.485 -4.627 1.00 30.36 ? 341 GLN A C 1 ATOM 2753 O O . GLN A 1 341 ? 36.857 39.757 -4.960 1.00 30.33 ? 341 GLN A O 1 ATOM 2754 C CB . GLN A 1 341 ? 33.711 39.545 -5.264 1.00 30.73 ? 341 GLN A CB 1 ATOM 2755 C CG . GLN A 1 341 ? 33.131 39.569 -3.858 1.00 36.91 ? 341 GLN A CG 1 ATOM 2756 C CD . GLN A 1 341 ? 32.455 38.262 -3.463 1.00 40.31 ? 341 GLN A CD 1 ATOM 2757 O OE1 . GLN A 1 341 ? 31.686 37.686 -4.236 1.00 41.85 ? 341 GLN A OE1 1 ATOM 2758 N NE2 . GLN A 1 341 ? 32.734 37.796 -2.246 1.00 42.16 ? 341 GLN A NE2 1 ATOM 2759 N N . VAL A 1 342 ? 35.903 41.163 -3.485 1.00 29.75 ? 342 VAL A N 1 ATOM 2760 C CA . VAL A 1 342 ? 36.962 41.035 -2.491 1.00 29.69 ? 342 VAL A CA 1 ATOM 2761 C C . VAL A 1 342 ? 36.228 40.609 -1.225 1.00 31.43 ? 342 VAL A C 1 ATOM 2762 O O . VAL A 1 342 ? 35.256 41.241 -0.819 1.00 31.83 ? 342 VAL A O 1 ATOM 2763 C CB . VAL A 1 342 ? 37.709 42.359 -2.267 1.00 28.36 ? 342 VAL A CB 1 ATOM 2764 C CG1 . VAL A 1 342 ? 38.652 42.229 -1.089 1.00 27.24 ? 342 VAL A CG1 1 ATOM 2765 C CG2 . VAL A 1 342 ? 38.506 42.710 -3.513 1.00 27.33 ? 342 VAL A CG2 1 ATOM 2766 N N . ASN A 1 343 ? 36.688 39.526 -0.612 1.00 33.11 ? 343 ASN A N 1 ATOM 2767 C CA . ASN A 1 343 ? 36.028 38.986 0.568 1.00 34.38 ? 343 ASN A CA 1 ATOM 2768 C C . ASN A 1 343 ? 36.952 38.879 1.789 1.00 32.95 ? 343 ASN A C 1 ATOM 2769 O O . ASN A 1 343 ? 38.168 38.812 1.654 1.00 32.71 ? 343 ASN A O 1 ATOM 2770 C CB . ASN A 1 343 ? 35.473 37.608 0.203 1.00 38.51 ? 343 ASN A CB 1 ATOM 2771 C CG . ASN A 1 343 ? 34.344 37.173 1.102 1.00 45.81 ? 343 ASN A CG 1 ATOM 2772 O OD1 . ASN A 1 343 ? 33.244 37.723 1.042 1.00 50.23 ? 343 ASN A OD1 1 ATOM 2773 N ND2 . ASN A 1 343 ? 34.605 36.178 1.950 1.00 49.54 ? 343 ASN A ND2 1 ATOM 2774 N N . LEU A 1 344 ? 36.362 38.882 2.980 1.00 32.17 ? 344 LEU A N 1 ATOM 2775 C CA . LEU A 1 344 ? 37.119 38.744 4.226 1.00 31.97 ? 344 LEU A CA 1 ATOM 2776 C C . LEU A 1 344 ? 36.309 37.893 5.189 1.00 31.49 ? 344 LEU A C 1 ATOM 2777 O O . LEU A 1 344 ? 35.091 38.007 5.239 1.00 32.37 ? 344 LEU A O 1 ATOM 2778 C CB . LEU A 1 344 ? 37.372 40.099 4.886 1.00 32.34 ? 344 LEU A CB 1 ATOM 2779 C CG . LEU A 1 344 ? 38.230 41.151 4.192 1.00 35.85 ? 344 LEU A CG 1 ATOM 2780 C CD1 . LEU A 1 344 ? 38.405 42.320 5.148 1.00 35.69 ? 344 LEU A CD1 1 ATOM 2781 C CD2 . LEU A 1 344 ? 39.587 40.580 3.799 1.00 35.78 ? 344 LEU A CD2 1 ATOM 2782 N N . GLN A 1 345 ? 36.974 37.036 5.952 1.00 31.83 ? 345 GLN A N 1 ATOM 2783 C CA . GLN A 1 345 ? 36.260 36.212 6.919 1.00 33.41 ? 345 GLN A CA 1 ATOM 2784 C C . GLN A 1 345 ? 37.059 35.966 8.176 1.00 32.44 ? 345 GLN A C 1 ATOM 2785 O O . GLN A 1 345 ? 38.287 35.924 8.145 1.00 32.51 ? 345 GLN A O 1 ATOM 2786 C CB . GLN A 1 345 ? 35.879 34.865 6.316 1.00 34.17 ? 345 GLN A CB 1 ATOM 2787 C CG . GLN A 1 345 ? 34.912 34.969 5.176 1.00 40.82 ? 345 GLN A CG 1 ATOM 2788 C CD . GLN A 1 345 ? 34.516 33.618 4.643 1.00 44.02 ? 345 GLN A CD 1 ATOM 2789 O OE1 . GLN A 1 345 ? 33.996 33.508 3.533 1.00 47.87 ? 345 GLN A OE1 1 ATOM 2790 N NE2 . GLN A 1 345 ? 34.750 32.574 5.434 1.00 43.83 ? 345 GLN A NE2 1 ATOM 2791 N N . ASN A 1 346 ? 36.348 35.809 9.285 1.00 32.03 ? 346 ASN A N 1 ATOM 2792 C CA . ASN A 1 346 ? 36.975 35.531 10.566 1.00 33.40 ? 346 ASN A CA 1 ATOM 2793 C C . ASN A 1 346 ? 38.172 36.445 10.834 1.00 32.45 ? 346 ASN A C 1 ATOM 2794 O O . ASN A 1 346 ? 39.268 35.981 11.146 1.00 32.01 ? 346 ASN A O 1 ATOM 2795 C CB . ASN A 1 346 ? 37.412 34.069 10.587 1.00 35.54 ? 346 ASN A CB 1 ATOM 2796 C CG . ASN A 1 346 ? 37.741 33.585 11.972 1.00 40.20 ? 346 ASN A CG 1 ATOM 2797 O OD1 . ASN A 1 346 ? 36.910 33.664 12.880 1.00 43.23 ? 346 ASN A OD1 1 ATOM 2798 N ND2 . ASN A 1 346 ? 38.955 33.072 12.149 1.00 42.58 ? 346 ASN A ND2 1 ATOM 2799 N N . LYS A 1 347 ? 37.947 37.749 10.714 1.00 32.00 ? 347 LYS A N 1 ATOM 2800 C CA . LYS A 1 347 ? 38.995 38.743 10.923 1.00 32.76 ? 347 LYS A CA 1 ATOM 2801 C C . LYS A 1 347 ? 38.726 39.612 12.148 1.00 34.23 ? 347 LYS A C 1 ATOM 2802 O O . LYS A 1 347 ? 37.681 40.259 12.246 1.00 34.30 ? 347 LYS A O 1 ATOM 2803 C CB . LYS A 1 347 ? 39.108 39.640 9.688 1.00 32.23 ? 347 LYS A CB 1 ATOM 2804 C CG . LYS A 1 347 ? 40.022 40.835 9.866 1.00 30.94 ? 347 LYS A CG 1 ATOM 2805 C CD . LYS A 1 347 ? 41.463 40.404 10.037 1.00 31.84 ? 347 LYS A CD 1 ATOM 2806 C CE . LYS A 1 347 ? 42.348 41.600 10.307 1.00 30.51 ? 347 LYS A CE 1 ATOM 2807 N NZ . LYS A 1 347 ? 43.778 41.240 10.207 1.00 32.04 ? 347 LYS A NZ 1 ATOM 2808 N N . ASN A 1 348 ? 39.673 39.636 13.076 1.00 35.29 ? 348 ASN A N 1 ATOM 2809 C CA . ASN A 1 348 ? 39.512 40.441 14.275 1.00 37.28 ? 348 ASN A CA 1 ATOM 2810 C C . ASN A 1 348 ? 39.920 41.882 14.060 1.00 36.99 ? 348 ASN A C 1 ATOM 2811 O O . ASN A 1 348 ? 40.927 42.164 13.413 1.00 35.95 ? 348 ASN A O 1 ATOM 2812 C CB . ASN A 1 348 ? 40.330 39.858 15.421 1.00 41.29 ? 348 ASN A CB 1 ATOM 2813 C CG . ASN A 1 348 ? 39.617 38.725 16.114 1.00 48.16 ? 348 ASN A CG 1 ATOM 2814 O OD1 . ASN A 1 348 ? 38.590 38.934 16.771 1.00 51.35 ? 348 ASN A OD1 1 ATOM 2815 N ND2 . ASN A 1 348 ? 40.145 37.509 15.964 1.00 50.18 ? 348 ASN A ND2 1 ATOM 2816 N N . LEU A 1 349 ? 39.117 42.792 14.599 1.00 36.53 ? 349 LEU A N 1 ATOM 2817 C CA . LEU A 1 349 ? 39.399 44.214 14.509 1.00 36.63 ? 349 LEU A CA 1 ATOM 2818 C C . LEU A 1 349 ? 39.733 44.671 15.915 1.00 37.36 ? 349 LEU A C 1 ATOM 2819 O O . LEU A 1 349 ? 38.843 44.905 16.732 1.00 38.14 ? 349 LEU A O 1 ATOM 2820 C CB . LEU A 1 349 ? 38.184 44.982 13.994 1.00 36.80 ? 349 LEU A CB 1 ATOM 2821 C CG . LEU A 1 349 ? 37.746 44.713 12.555 1.00 37.62 ? 349 LEU A CG 1 ATOM 2822 C CD1 . LEU A 1 349 ? 36.551 45.594 12.221 1.00 36.79 ? 349 LEU A CD1 1 ATOM 2823 C CD2 . LEU A 1 349 ? 38.897 44.994 11.605 1.00 36.90 ? 349 LEU A CD2 1 ATOM 2824 N N . LYS A 1 350 ? 41.021 44.776 16.208 1.00 38.12 ? 350 LYS A N 1 ATOM 2825 C CA . LYS A 1 350 ? 41.438 45.201 17.531 1.00 39.35 ? 350 LYS A CA 1 ATOM 2826 C C . LYS A 1 350 ? 41.070 46.659 17.760 1.00 36.39 ? 350 LYS A C 1 ATOM 2827 O O . LYS A 1 350 ? 40.905 47.428 16.815 1.00 35.95 ? 350 LYS A O 1 ATOM 2828 C CB . LYS A 1 350 ? 42.946 44.987 17.705 1.00 43.70 ? 350 LYS A CB 1 ATOM 2829 C CG . LYS A 1 350 ? 43.786 45.478 16.540 1.00 52.10 ? 350 LYS A CG 1 ATOM 2830 C CD . LYS A 1 350 ? 45.272 45.176 16.751 1.00 57.30 ? 350 LYS A CD 1 ATOM 2831 C CE . LYS A 1 350 ? 46.108 45.620 15.544 1.00 61.28 ? 350 LYS A CE 1 ATOM 2832 N NZ . LYS A 1 350 ? 45.976 47.083 15.238 1.00 62.20 ? 350 LYS A NZ 1 ATOM 2833 N N . PRO A 1 351 ? 40.921 47.055 19.029 1.00 33.88 ? 351 PRO A N 1 ATOM 2834 C CA . PRO A 1 351 ? 40.566 48.425 19.395 1.00 32.81 ? 351 PRO A CA 1 ATOM 2835 C C . PRO A 1 351 ? 41.380 49.493 18.666 1.00 33.20 ? 351 PRO A C 1 ATOM 2836 O O . PRO A 1 351 ? 42.599 49.392 18.557 1.00 33.74 ? 351 PRO A O 1 ATOM 2837 C CB . PRO A 1 351 ? 40.803 48.441 20.897 1.00 32.08 ? 351 PRO A CB 1 ATOM 2838 C CG . PRO A 1 351 ? 40.406 47.068 21.292 1.00 31.82 ? 351 PRO A CG 1 ATOM 2839 C CD . PRO A 1 351 ? 41.064 46.219 20.233 1.00 32.81 ? 351 PRO A CD 1 ATOM 2840 N N . GLY A 1 352 ? 40.687 50.511 18.168 1.00 32.86 ? 352 GLY A N 1 ATOM 2841 C CA . GLY A 1 352 ? 41.342 51.603 17.472 1.00 31.62 ? 352 GLY A CA 1 ATOM 2842 C C . GLY A 1 352 ? 42.057 51.232 16.188 1.00 31.61 ? 352 GLY A C 1 ATOM 2843 O O . GLY A 1 352 ? 42.976 51.936 15.770 1.00 33.14 ? 352 GLY A O 1 ATOM 2844 N N . SER A 1 353 ? 41.642 50.146 15.548 1.00 29.95 ? 353 SER A N 1 ATOM 2845 C CA . SER A 1 353 ? 42.287 49.728 14.311 1.00 27.76 ? 353 SER A CA 1 ATOM 2846 C C . SER A 1 353 ? 41.513 50.167 13.077 1.00 27.37 ? 353 SER A C 1 ATOM 2847 O O . SER A 1 353 ? 40.320 50.484 13.151 1.00 26.26 ? 353 SER A O 1 ATOM 2848 C CB . SER A 1 353 ? 42.453 48.209 14.287 1.00 28.02 ? 353 SER A CB 1 ATOM 2849 O OG . SER A 1 353 ? 41.196 47.560 14.237 1.00 28.90 ? 353 SER A OG 1 ATOM 2850 N N . VAL A 1 354 ? 42.214 50.176 11.945 1.00 26.47 ? 354 VAL A N 1 ATOM 2851 C CA . VAL A 1 354 ? 41.653 50.552 10.651 1.00 24.55 ? 354 VAL A CA 1 ATOM 2852 C C . VAL A 1 354 ? 42.210 49.613 9.578 1.00 25.11 ? 354 VAL A C 1 ATOM 2853 O O . VAL A 1 354 ? 43.416 49.570 9.332 1.00 26.04 ? 354 VAL A O 1 ATOM 2854 C CB . VAL A 1 354 ? 42.006 52.011 10.294 1.00 23.01 ? 354 VAL A CB 1 ATOM 2855 C CG1 . VAL A 1 354 ? 41.523 52.341 8.889 1.00 22.77 ? 354 VAL A CG1 1 ATOM 2856 C CG2 . VAL A 1 354 ? 41.370 52.951 11.303 1.00 20.46 ? 354 VAL A CG2 1 ATOM 2857 N N . LEU A 1 355 ? 41.321 48.857 8.947 1.00 25.09 ? 355 LEU A N 1 ATOM 2858 C CA . LEU A 1 355 ? 41.711 47.896 7.918 1.00 25.21 ? 355 LEU A CA 1 ATOM 2859 C C . LEU A 1 355 ? 41.281 48.339 6.525 1.00 25.39 ? 355 LEU A C 1 ATOM 2860 O O . LEU A 1 355 ? 40.094 48.547 6.269 1.00 26.44 ? 355 LEU A O 1 ATOM 2861 C CB . LEU A 1 355 ? 41.077 46.545 8.232 1.00 25.03 ? 355 LEU A CB 1 ATOM 2862 C CG . LEU A 1 355 ? 41.390 45.401 7.282 1.00 24.60 ? 355 LEU A CG 1 ATOM 2863 C CD1 . LEU A 1 355 ? 42.872 45.057 7.371 1.00 22.85 ? 355 LEU A CD1 1 ATOM 2864 C CD2 . LEU A 1 355 ? 40.534 44.203 7.652 1.00 24.18 ? 355 LEU A CD2 1 ATOM 2865 N N . GLU A 1 356 ? 42.234 48.470 5.614 1.00 25.00 ? 356 GLU A N 1 ATOM 2866 C CA . GLU A 1 356 ? 41.893 48.891 4.265 1.00 26.42 ? 356 GLU A CA 1 ATOM 2867 C C . GLU A 1 356 ? 41.503 47.731 3.347 1.00 27.74 ? 356 GLU A C 1 ATOM 2868 O O . GLU A 1 356 ? 42.124 46.666 3.372 1.00 28.82 ? 356 GLU A O 1 ATOM 2869 C CB . GLU A 1 356 ? 43.051 49.682 3.651 1.00 24.86 ? 356 GLU A CB 1 ATOM 2870 C CG . GLU A 1 356 ? 42.895 49.933 2.163 1.00 28.64 ? 356 GLU A CG 1 ATOM 2871 C CD . GLU A 1 356 ? 43.724 51.100 1.660 1.00 31.34 ? 356 GLU A CD 1 ATOM 2872 O OE1 . GLU A 1 356 ? 44.848 51.313 2.162 1.00 33.14 ? 356 GLU A OE1 1 ATOM 2873 O OE2 . GLU A 1 356 ? 43.251 51.802 0.745 1.00 34.20 ? 356 GLU A OE2 1 ATOM 2874 N N . ILE A 1 357 ? 40.452 47.947 2.555 1.00 27.66 ? 357 ILE A N 1 ATOM 2875 C CA . ILE A 1 357 ? 39.972 46.954 1.603 1.00 28.06 ? 357 ILE A CA 1 ATOM 2876 C C . ILE A 1 357 ? 40.621 47.292 0.274 1.00 28.72 ? 357 ILE A C 1 ATOM 2877 O O . ILE A 1 357 ? 40.407 48.377 -0.263 1.00 30.28 ? 357 ILE A O 1 ATOM 2878 C CB . ILE A 1 357 ? 38.441 47.024 1.404 1.00 28.69 ? 357 ILE A CB 1 ATOM 2879 C CG1 . ILE A 1 357 ? 37.722 46.956 2.753 1.00 28.08 ? 357 ILE A CG1 1 ATOM 2880 C CG2 . ILE A 1 357 ? 37.987 45.884 0.500 1.00 25.39 ? 357 ILE A CG2 1 ATOM 2881 C CD1 . ILE A 1 357 ? 38.051 45.730 3.556 1.00 28.27 ? 357 ILE A CD1 1 ATOM 2882 N N . HIS A 1 358 ? 41.404 46.363 -0.262 1.00 29.38 ? 358 HIS A N 1 ATOM 2883 C CA . HIS A 1 358 ? 42.095 46.591 -1.525 1.00 28.43 ? 358 HIS A CA 1 ATOM 2884 C C . HIS A 1 358 ? 41.458 45.907 -2.730 1.00 28.56 ? 358 HIS A C 1 ATOM 2885 O O . HIS A 1 358 ? 40.776 44.889 -2.597 1.00 27.04 ? 358 HIS A O 1 ATOM 2886 C CB . HIS A 1 358 ? 43.539 46.123 -1.399 1.00 27.98 ? 358 HIS A CB 1 ATOM 2887 C CG . HIS A 1 358 ? 44.343 46.903 -0.410 1.00 29.21 ? 358 HIS A CG 1 ATOM 2888 N ND1 . HIS A 1 358 ? 45.091 48.004 -0.763 1.00 29.39 ? 358 HIS A ND1 1 ATOM 2889 C CD2 . HIS A 1 358 ? 44.503 46.748 0.927 1.00 28.66 ? 358 HIS A CD2 1 ATOM 2890 C CE1 . HIS A 1 358 ? 45.681 48.495 0.316 1.00 28.05 ? 358 HIS A CE1 1 ATOM 2891 N NE2 . HIS A 1 358 ? 45.341 47.752 1.352 1.00 28.44 ? 358 HIS A NE2 1 ATOM 2892 N N . GLY A 1 359 ? 41.694 46.487 -3.908 1.00 28.82 ? 359 GLY A N 1 ATOM 2893 C CA . GLY A 1 359 ? 41.187 45.921 -5.148 1.00 28.29 ? 359 GLY A CA 1 ATOM 2894 C C . GLY A 1 359 ? 39.745 46.195 -5.520 1.00 27.57 ? 359 GLY A C 1 ATOM 2895 O O . GLY A 1 359 ? 39.185 45.491 -6.352 1.00 28.77 ? 359 GLY A O 1 ATOM 2896 N N . ILE A 1 360 ? 39.152 47.224 -4.929 1.00 27.84 ? 360 ILE A N 1 ATOM 2897 C CA . ILE A 1 360 ? 37.763 47.579 -5.201 1.00 26.67 ? 360 ILE A CA 1 ATOM 2898 C C . ILE A 1 360 ? 37.644 49.023 -5.687 1.00 25.38 ? 360 ILE A C 1 ATOM 2899 O O . ILE A 1 360 ? 38.400 49.885 -5.253 1.00 26.72 ? 360 ILE A O 1 ATOM 2900 C CB . ILE A 1 360 ? 36.912 47.409 -3.909 1.00 27.92 ? 360 ILE A CB 1 ATOM 2901 C CG1 . ILE A 1 360 ? 36.697 45.925 -3.626 1.00 28.35 ? 360 ILE A CG1 1 ATOM 2902 C CG2 . ILE A 1 360 ? 35.587 48.136 -4.033 1.00 26.78 ? 360 ILE A CG2 1 ATOM 2903 C CD1 . ILE A 1 360 ? 35.962 45.196 -4.742 1.00 29.76 ? 360 ILE A CD1 1 ATOM 2904 N N . ALA A 1 361 ? 36.713 49.290 -6.597 1.00 23.59 ? 361 ALA A N 1 ATOM 2905 C CA . ALA A 1 361 ? 36.514 50.662 -7.062 1.00 23.14 ? 361 ALA A CA 1 ATOM 2906 C C . ALA A 1 361 ? 35.790 51.344 -5.900 1.00 23.16 ? 361 ALA A C 1 ATOM 2907 O O . ALA A 1 361 ? 34.564 51.335 -5.831 1.00 23.41 ? 361 ALA A O 1 ATOM 2908 C CB . ALA A 1 361 ? 35.646 50.675 -8.307 1.00 21.80 ? 361 ALA A CB 1 ATOM 2909 N N . ALA A 1 362 ? 36.559 51.923 -4.987 1.00 22.91 ? 362 ALA A N 1 ATOM 2910 C CA . ALA A 1 362 ? 36.011 52.553 -3.786 1.00 24.22 ? 362 ALA A CA 1 ATOM 2911 C C . ALA A 1 362 ? 34.925 53.624 -3.941 1.00 24.35 ? 362 ALA A C 1 ATOM 2912 O O . ALA A 1 362 ? 34.207 53.904 -2.982 1.00 22.83 ? 362 ALA A O 1 ATOM 2913 C CB . ALA A 1 362 ? 37.157 53.101 -2.932 1.00 23.17 ? 362 ALA A CB 1 ATOM 2914 N N . SER A 1 363 ? 34.799 54.226 -5.120 1.00 25.42 ? 363 SER A N 1 ATOM 2915 C CA . SER A 1 363 ? 33.783 55.259 -5.330 1.00 27.60 ? 363 SER A CA 1 ATOM 2916 C C . SER A 1 363 ? 32.479 54.695 -5.878 1.00 28.29 ? 363 SER A C 1 ATOM 2917 O O . SER A 1 363 ? 31.456 55.384 -5.906 1.00 29.38 ? 363 SER A O 1 ATOM 2918 C CB . SER A 1 363 ? 34.288 56.327 -6.307 1.00 27.06 ? 363 SER A CB 1 ATOM 2919 O OG . SER A 1 363 ? 35.282 57.146 -5.722 1.00 32.95 ? 363 SER A OG 1 ATOM 2920 N N . GLN A 1 364 ? 32.513 53.443 -6.312 1.00 27.15 ? 364 GLN A N 1 ATOM 2921 C CA . GLN A 1 364 ? 31.335 52.825 -6.898 1.00 26.90 ? 364 GLN A CA 1 ATOM 2922 C C . GLN A 1 364 ? 31.331 51.336 -6.562 1.00 26.64 ? 364 GLN A C 1 ATOM 2923 O O . GLN A 1 364 ? 31.749 50.498 -7.367 1.00 27.43 ? 364 GLN A O 1 ATOM 2924 C CB . GLN A 1 364 ? 31.383 53.047 -8.412 1.00 26.32 ? 364 GLN A CB 1 ATOM 2925 C CG . GLN A 1 364 ? 30.058 52.970 -9.122 1.00 27.52 ? 364 GLN A CG 1 ATOM 2926 C CD . GLN A 1 364 ? 30.168 53.397 -10.576 1.00 27.29 ? 364 GLN A CD 1 ATOM 2927 O OE1 . GLN A 1 364 ? 30.616 54.506 -10.874 1.00 27.73 ? 364 GLN A OE1 1 ATOM 2928 N NE2 . GLN A 1 364 ? 29.757 52.519 -11.488 1.00 25.70 ? 364 GLN A NE2 1 ATOM 2929 N N . ALA A 1 365 ? 30.847 51.013 -5.369 1.00 25.02 ? 365 ALA A N 1 ATOM 2930 C CA . ALA A 1 365 ? 30.826 49.633 -4.913 1.00 23.82 ? 365 ALA A CA 1 ATOM 2931 C C . ALA A 1 365 ? 29.628 49.271 -4.044 1.00 24.57 ? 365 ALA A C 1 ATOM 2932 O O . ALA A 1 365 ? 28.890 50.137 -3.561 1.00 24.03 ? 365 ALA A O 1 ATOM 2933 C CB . ALA A 1 365 ? 32.102 49.342 -4.149 1.00 22.28 ? 365 ALA A CB 1 ATOM 2934 N N . ASP A 1 366 ? 29.456 47.969 -3.859 1.00 24.21 ? 366 ASP A N 1 ATOM 2935 C CA . ASP A 1 366 ? 28.391 47.412 -3.039 1.00 24.59 ? 366 ASP A CA 1 ATOM 2936 C C . ASP A 1 366 ? 29.157 46.644 -1.958 1.00 24.73 ? 366 ASP A C 1 ATOM 2937 O O . ASP A 1 366 ? 29.814 45.639 -2.242 1.00 23.92 ? 366 ASP A O 1 ATOM 2938 C CB . ASP A 1 366 ? 27.526 46.474 -3.887 1.00 24.65 ? 366 ASP A CB 1 ATOM 2939 C CG . ASP A 1 366 ? 26.306 45.953 -3.144 1.00 26.91 ? 366 ASP A CG 1 ATOM 2940 O OD1 . ASP A 1 366 ? 26.082 46.344 -1.978 1.00 28.53 ? 366 ASP A OD1 1 ATOM 2941 O OD2 . ASP A 1 366 ? 25.564 45.143 -3.737 1.00 27.65 ? 366 ASP A OD2 1 ATOM 2942 N N . VAL A 1 367 ? 29.100 47.138 -0.726 1.00 24.54 ? 367 VAL A N 1 ATOM 2943 C CA . VAL A 1 367 ? 29.828 46.509 0.366 1.00 24.71 ? 367 VAL A CA 1 ATOM 2944 C C . VAL A 1 367 ? 28.927 45.960 1.459 1.00 25.97 ? 367 VAL A C 1 ATOM 2945 O O . VAL A 1 367 ? 28.057 46.656 1.980 1.00 26.07 ? 367 VAL A O 1 ATOM 2946 C CB . VAL A 1 367 ? 30.820 47.500 1.000 1.00 23.47 ? 367 VAL A CB 1 ATOM 2947 C CG1 . VAL A 1 367 ? 31.705 46.777 1.999 1.00 22.98 ? 367 VAL A CG1 1 ATOM 2948 C CG2 . VAL A 1 367 ? 31.659 48.158 -0.086 1.00 21.51 ? 367 VAL A CG2 1 ATOM 2949 N N . THR A 1 368 ? 29.152 44.698 1.801 1.00 27.72 ? 368 THR A N 1 ATOM 2950 C CA . THR A 1 368 ? 28.378 44.022 2.829 1.00 29.24 ? 368 THR A CA 1 ATOM 2951 C C . THR A 1 368 ? 29.318 43.501 3.896 1.00 28.80 ? 368 THR A C 1 ATOM 2952 O O . THR A 1 368 ? 30.359 42.925 3.586 1.00 28.68 ? 368 THR A O 1 ATOM 2953 C CB . THR A 1 368 ? 27.602 42.829 2.250 1.00 31.09 ? 368 THR A CB 1 ATOM 2954 O OG1 . THR A 1 368 ? 26.712 43.293 1.230 1.00 35.45 ? 368 THR A OG1 1 ATOM 2955 C CG2 . THR A 1 368 ? 26.793 42.149 3.335 1.00 35.05 ? 368 THR A CG2 1 ATOM 2956 N N . ILE A 1 369 ? 28.950 43.696 5.155 1.00 28.16 ? 369 ILE A N 1 ATOM 2957 C CA . ILE A 1 369 ? 29.784 43.237 6.250 1.00 28.22 ? 369 ILE A CA 1 ATOM 2958 C C . ILE A 1 369 ? 28.931 42.780 7.419 1.00 28.36 ? 369 ILE A C 1 ATOM 2959 O O . ILE A 1 369 ? 27.817 43.262 7.617 1.00 28.86 ? 369 ILE A O 1 ATOM 2960 C CB . ILE A 1 369 ? 30.756 44.350 6.699 1.00 28.40 ? 369 ILE A CB 1 ATOM 2961 C CG1 . ILE A 1 369 ? 31.662 43.836 7.812 1.00 28.86 ? 369 ILE A CG1 1 ATOM 2962 C CG2 . ILE A 1 369 ? 29.984 45.561 7.161 1.00 27.96 ? 369 ILE A CG2 1 ATOM 2963 C CD1 . ILE A 1 369 ? 32.847 44.742 8.077 1.00 33.12 ? 369 ILE A CD1 1 ATOM 2964 N N . SER A 1 370 ? 29.453 41.834 8.187 1.00 28.81 ? 370 SER A N 1 ATOM 2965 C CA . SER A 1 370 ? 28.730 41.302 9.330 1.00 28.67 ? 370 SER A CA 1 ATOM 2966 C C . SER A 1 370 ? 29.674 41.199 10.532 1.00 28.89 ? 370 SER A C 1 ATOM 2967 O O . SER A 1 370 ? 30.759 40.626 10.442 1.00 28.13 ? 370 SER A O 1 ATOM 2968 C CB . SER A 1 370 ? 28.154 39.934 8.965 1.00 27.55 ? 370 SER A CB 1 ATOM 2969 O OG . SER A 1 370 ? 27.209 39.509 9.926 1.00 31.76 ? 370 SER A OG 1 ATOM 2970 N N . PHE A 1 371 ? 29.252 41.764 11.657 1.00 30.00 ? 371 PHE A N 1 ATOM 2971 C CA . PHE A 1 371 ? 30.061 41.771 12.871 1.00 31.51 ? 371 PHE A CA 1 ATOM 2972 C C . PHE A 1 371 ? 29.619 40.772 13.941 1.00 33.78 ? 371 PHE A C 1 ATOM 2973 O O . PHE A 1 371 ? 28.432 40.680 14.271 1.00 33.55 ? 371 PHE A O 1 ATOM 2974 C CB . PHE A 1 371 ? 30.038 43.171 13.485 1.00 30.13 ? 371 PHE A CB 1 ATOM 2975 C CG . PHE A 1 371 ? 30.638 44.232 12.613 1.00 29.47 ? 371 PHE A CG 1 ATOM 2976 C CD1 . PHE A 1 371 ? 32.019 44.335 12.468 1.00 28.52 ? 371 PHE A CD1 1 ATOM 2977 C CD2 . PHE A 1 371 ? 29.824 45.147 11.952 1.00 28.65 ? 371 PHE A CD2 1 ATOM 2978 C CE1 . PHE A 1 371 ? 32.582 45.335 11.683 1.00 28.11 ? 371 PHE A CE1 1 ATOM 2979 C CE2 . PHE A 1 371 ? 30.376 46.152 11.161 1.00 28.60 ? 371 PHE A CE2 1 ATOM 2980 C CZ . PHE A 1 371 ? 31.759 46.248 11.027 1.00 28.19 ? 371 PHE A CZ 1 ATOM 2981 N N . LYS A 1 372 ? 30.580 40.030 14.487 1.00 36.61 ? 372 LYS A N 1 ATOM 2982 C CA . LYS A 1 372 ? 30.296 39.076 15.556 1.00 39.39 ? 372 LYS A CA 1 ATOM 2983 C C . LYS A 1 372 ? 30.840 39.715 16.829 1.00 40.28 ? 372 LYS A C 1 ATOM 2984 O O . LYS A 1 372 ? 32.044 39.960 16.943 1.00 39.18 ? 372 LYS A O 1 ATOM 2985 C CB . LYS A 1 372 ? 30.997 37.736 15.313 1.00 41.32 ? 372 LYS A CB 1 ATOM 2986 C CG . LYS A 1 372 ? 30.472 36.612 16.203 1.00 44.69 ? 372 LYS A CG 1 ATOM 2987 C CD . LYS A 1 372 ? 31.302 35.339 16.096 1.00 48.54 ? 372 LYS A CD 1 ATOM 2988 C CE . LYS A 1 372 ? 32.691 35.529 16.706 1.00 53.28 ? 372 LYS A CE 1 ATOM 2989 N NZ . LYS A 1 372 ? 33.523 34.282 16.696 1.00 54.33 ? 372 LYS A NZ 1 ATOM 2990 N N . LEU A 1 373 ? 29.955 39.988 17.781 1.00 41.91 ? 373 LEU A N 1 ATOM 2991 C CA . LEU A 1 373 ? 30.364 40.630 19.022 1.00 44.49 ? 373 LEU A CA 1 ATOM 2992 C C . LEU A 1 373 ? 30.711 39.683 20.162 1.00 47.51 ? 373 LEU A C 1 ATOM 2993 O O . LEU A 1 373 ? 30.115 38.615 20.317 1.00 47.35 ? 373 LEU A O 1 ATOM 2994 C CB . LEU A 1 373 ? 29.279 41.597 19.492 1.00 42.51 ? 373 LEU A CB 1 ATOM 2995 C CG . LEU A 1 373 ? 28.926 42.747 18.554 1.00 42.26 ? 373 LEU A CG 1 ATOM 2996 C CD1 . LEU A 1 373 ? 27.960 43.670 19.263 1.00 42.78 ? 373 LEU A CD1 1 ATOM 2997 C CD2 . LEU A 1 373 ? 30.179 43.505 18.156 1.00 43.01 ? 373 LEU A CD2 1 ATOM 2998 N N . GLU A 1 374 ? 31.683 40.104 20.963 1.00 51.19 ? 374 GLU A N 1 ATOM 2999 C CA . GLU A 1 374 ? 32.144 39.337 22.114 1.00 53.73 ? 374 GLU A CA 1 ATOM 3000 C C . GLU A 1 374 ? 32.108 40.216 23.363 1.00 52.45 ? 374 GLU A C 1 ATOM 3001 O O . GLU A 1 374 ? 32.554 41.370 23.343 1.00 52.05 ? 374 GLU A O 1 ATOM 3002 C CB . GLU A 1 374 ? 33.580 38.847 21.888 1.00 58.61 ? 374 GLU A CB 1 ATOM 3003 C CG . GLU A 1 374 ? 34.575 39.973 21.555 1.00 65.31 ? 374 GLU A CG 1 ATOM 3004 C CD . GLU A 1 374 ? 36.043 39.567 21.729 1.00 68.62 ? 374 GLU A CD 1 ATOM 3005 O OE1 . GLU A 1 374 ? 36.475 38.562 21.117 1.00 69.90 ? 374 GLU A OE1 1 ATOM 3006 O OE2 . GLU A 1 374 ? 36.765 40.263 22.480 1.00 70.01 ? 374 GLU A OE2 1 ATOM 3007 N N . GLY A 1 375 ? 31.576 39.662 24.445 1.00 50.46 ? 375 GLY A N 1 ATOM 3008 C CA . GLY A 1 375 ? 31.510 40.401 25.691 1.00 48.07 ? 375 GLY A CA 1 ATOM 3009 C C . GLY A 1 375 ? 30.559 41.578 25.662 1.00 45.89 ? 375 GLY A C 1 ATOM 3010 O O . GLY A 1 375 ? 30.965 42.717 25.885 1.00 45.17 ? 375 GLY A O 1 ATOM 3011 N N . LEU A 1 376 ? 29.289 41.301 25.383 1.00 43.98 ? 376 LEU A N 1 ATOM 3012 C CA . LEU A 1 376 ? 28.275 42.339 25.343 1.00 42.53 ? 376 LEU A CA 1 ATOM 3013 C C . LEU A 1 376 ? 28.158 42.993 26.711 1.00 43.07 ? 376 LEU A C 1 ATOM 3014 O O . LEU A 1 376 ? 27.926 44.195 26.817 1.00 43.87 ? 376 LEU A O 1 ATOM 3015 C CB . LEU A 1 376 ? 26.921 41.748 24.952 1.00 40.76 ? 376 LEU A CB 1 ATOM 3016 C CG . LEU A 1 376 ? 26.761 41.263 23.515 1.00 39.40 ? 376 LEU A CG 1 ATOM 3017 C CD1 . LEU A 1 376 ? 25.427 40.553 23.358 1.00 39.83 ? 376 LEU A CD1 1 ATOM 3018 C CD2 . LEU A 1 376 ? 26.854 42.447 22.572 1.00 40.32 ? 376 LEU A CD2 1 ATOM 3019 N N . LYS A 1 377 ? 28.320 42.196 27.757 1.00 42.69 ? 377 LYS A N 1 ATOM 3020 C CA . LYS A 1 377 ? 28.225 42.703 29.115 1.00 42.68 ? 377 LYS A CA 1 ATOM 3021 C C . LYS A 1 377 ? 29.066 43.957 29.321 1.00 40.80 ? 377 LYS A C 1 ATOM 3022 O O . LYS A 1 377 ? 28.813 44.723 30.245 1.00 41.17 ? 377 LYS A O 1 ATOM 3023 C CB . LYS A 1 377 ? 28.656 41.621 30.104 1.00 46.61 ? 377 LYS A CB 1 ATOM 3024 C CG . LYS A 1 377 ? 29.966 40.944 29.725 1.00 54.29 ? 377 LYS A CG 1 ATOM 3025 C CD . LYS A 1 377 ? 30.423 39.952 30.791 1.00 58.02 ? 377 LYS A CD 1 ATOM 3026 C CE . LYS A 1 377 ? 30.815 40.657 32.083 1.00 59.19 ? 377 LYS A CE 1 ATOM 3027 N NZ . LYS A 1 377 ? 31.281 39.693 33.117 1.00 61.06 ? 377 LYS A NZ 1 ATOM 3028 N N . GLU A 1 378 ? 30.057 44.175 28.460 1.00 38.37 ? 378 GLU A N 1 ATOM 3029 C CA . GLU A 1 378 ? 30.918 45.352 28.584 1.00 37.14 ? 378 GLU A CA 1 ATOM 3030 C C . GLU A 1 378 ? 30.300 46.612 27.986 1.00 35.08 ? 378 GLU A C 1 ATOM 3031 O O . GLU A 1 378 ? 30.856 47.707 28.109 1.00 33.36 ? 378 GLU A O 1 ATOM 3032 C CB . GLU A 1 378 ? 32.273 45.099 27.919 1.00 39.59 ? 378 GLU A CB 1 ATOM 3033 C CG . GLU A 1 378 ? 33.028 43.912 28.476 1.00 43.17 ? 378 GLU A CG 1 ATOM 3034 C CD . GLU A 1 378 ? 33.043 43.890 29.993 1.00 46.09 ? 378 GLU A CD 1 ATOM 3035 O OE1 . GLU A 1 378 ? 33.409 44.921 30.602 1.00 47.45 ? 378 GLU A OE1 1 ATOM 3036 O OE2 . GLU A 1 378 ? 32.691 42.837 30.574 1.00 47.79 ? 378 GLU A OE2 1 ATOM 3037 N N . ALA A 1 379 ? 29.155 46.451 27.333 1.00 32.91 ? 379 ALA A N 1 ATOM 3038 C CA . ALA A 1 379 ? 28.464 47.569 26.712 1.00 31.26 ? 379 ALA A CA 1 ATOM 3039 C C . ALA A 1 379 ? 28.226 48.696 27.704 1.00 31.74 ? 379 ALA A C 1 ATOM 3040 O O . ALA A 1 379 ? 27.846 48.466 28.856 1.00 31.67 ? 379 ALA A O 1 ATOM 3041 C CB . ALA A 1 379 ? 27.137 47.104 26.126 1.00 29.69 ? 379 ALA A CB 1 ATOM 3042 N N . GLU A 1 380 ? 28.465 49.918 27.242 1.00 31.23 ? 380 GLU A N 1 ATOM 3043 C CA . GLU A 1 380 ? 28.262 51.112 28.043 1.00 30.34 ? 380 GLU A CA 1 ATOM 3044 C C . GLU A 1 380 ? 26.828 51.139 28.518 1.00 30.63 ? 380 GLU A C 1 ATOM 3045 O O . GLU A 1 380 ? 25.913 50.793 27.771 1.00 31.17 ? 380 GLU A O 1 ATOM 3046 C CB . GLU A 1 380 ? 28.518 52.353 27.199 1.00 30.23 ? 380 GLU A CB 1 ATOM 3047 C CG . GLU A 1 380 ? 29.954 52.529 26.781 1.00 33.61 ? 380 GLU A CG 1 ATOM 3048 C CD . GLU A 1 380 ? 30.081 53.401 25.555 1.00 35.89 ? 380 GLU A CD 1 ATOM 3049 O OE1 . GLU A 1 380 ? 30.313 52.842 24.463 1.00 37.02 ? 380 GLU A OE1 1 ATOM 3050 O OE2 . GLU A 1 380 ? 29.935 54.638 25.679 1.00 36.23 ? 380 GLU A OE2 1 ATOM 3051 N N . VAL A 1 381 ? 26.624 51.553 29.763 1.00 31.11 ? 381 VAL A N 1 ATOM 3052 C CA . VAL A 1 381 ? 25.274 51.627 30.288 1.00 30.94 ? 381 VAL A CA 1 ATOM 3053 C C . VAL A 1 381 ? 24.643 52.943 29.866 1.00 31.15 ? 381 VAL A C 1 ATOM 3054 O O . VAL A 1 381 ? 25.159 54.022 30.158 1.00 32.03 ? 381 VAL A O 1 ATOM 3055 C CB . VAL A 1 381 ? 25.258 51.523 31.816 1.00 30.54 ? 381 VAL A CB 1 ATOM 3056 C CG1 . VAL A 1 381 ? 23.835 51.672 32.330 1.00 28.96 ? 381 VAL A CG1 1 ATOM 3057 C CG2 . VAL A 1 381 ? 25.834 50.187 32.241 1.00 29.60 ? 381 VAL A CG2 1 ATOM 3058 N N . LEU A 1 382 ? 23.531 52.848 29.153 1.00 29.72 ? 382 LEU A N 1 ATOM 3059 C CA . LEU A 1 382 ? 22.837 54.032 28.692 1.00 29.61 ? 382 LEU A CA 1 ATOM 3060 C C . LEU A 1 382 ? 21.420 53.678 28.287 1.00 30.49 ? 382 LEU A C 1 ATOM 3061 O O . LEU A 1 382 ? 21.210 52.961 27.311 1.00 32.03 ? 382 LEU A O 1 ATOM 3062 C CB . LEU A 1 382 ? 23.573 54.647 27.497 1.00 28.32 ? 382 LEU A CB 1 ATOM 3063 C CG . LEU A 1 382 ? 22.783 55.686 26.690 1.00 28.24 ? 382 LEU A CG 1 ATOM 3064 C CD1 . LEU A 1 382 ? 22.425 56.860 27.579 1.00 28.43 ? 382 LEU A CD1 1 ATOM 3065 C CD2 . LEU A 1 382 ? 23.595 56.148 25.497 1.00 27.26 ? 382 LEU A CD2 1 ATOM 3066 N N . ASP A 1 383 ? 20.445 54.164 29.046 1.00 30.70 ? 383 ASP A N 1 ATOM 3067 C CA . ASP A 1 383 ? 19.056 53.905 28.708 1.00 30.68 ? 383 ASP A CA 1 ATOM 3068 C C . ASP A 1 383 ? 18.779 54.786 27.495 1.00 31.56 ? 383 ASP A C 1 ATOM 3069 O O . ASP A 1 383 ? 19.092 55.979 27.510 1.00 31.30 ? 383 ASP A O 1 ATOM 3070 C CB . ASP A 1 383 ? 18.133 54.308 29.851 1.00 29.74 ? 383 ASP A CB 1 ATOM 3071 C CG . ASP A 1 383 ? 16.707 53.874 29.615 1.00 30.69 ? 383 ASP A CG 1 ATOM 3072 O OD1 . ASP A 1 383 ? 16.291 52.859 30.210 1.00 31.07 ? 383 ASP A OD1 1 ATOM 3073 O OD2 . ASP A 1 383 ? 16.008 54.536 28.820 1.00 30.20 ? 383 ASP A OD2 1 ATOM 3074 N N . THR A 1 384 ? 18.201 54.211 26.446 1.00 31.07 ? 384 THR A N 1 ATOM 3075 C CA . THR A 1 384 ? 17.929 54.980 25.238 1.00 30.80 ? 384 THR A CA 1 ATOM 3076 C C . THR A 1 384 ? 16.440 55.147 24.930 1.00 31.64 ? 384 THR A C 1 ATOM 3077 O O . THR A 1 384 ? 16.057 55.436 23.791 1.00 31.91 ? 384 THR A O 1 ATOM 3078 C CB . THR A 1 384 ? 18.656 54.351 24.013 1.00 31.20 ? 384 THR A CB 1 ATOM 3079 O OG1 . THR A 1 384 ? 18.429 52.937 23.984 1.00 29.43 ? 384 THR A OG1 1 ATOM 3080 C CG2 . THR A 1 384 ? 20.161 54.614 24.088 1.00 29.81 ? 384 THR A CG2 1 ATOM 3081 N N . THR A 1 385 ? 15.608 54.988 25.956 1.00 30.48 ? 385 THR A N 1 ATOM 3082 C CA . THR A 1 385 ? 14.159 55.120 25.815 1.00 30.29 ? 385 THR A CA 1 ATOM 3083 C C . THR A 1 385 ? 13.699 56.414 25.126 1.00 30.75 ? 385 THR A C 1 ATOM 3084 O O . THR A 1 385 ? 12.843 56.377 24.237 1.00 30.19 ? 385 THR A O 1 ATOM 3085 C CB . THR A 1 385 ? 13.469 55.032 27.191 1.00 30.65 ? 385 THR A CB 1 ATOM 3086 O OG1 . THR A 1 385 ? 13.760 53.764 27.788 1.00 32.50 ? 385 THR A OG1 1 ATOM 3087 C CG2 . THR A 1 385 ? 11.970 55.184 27.047 1.00 28.95 ? 385 THR A CG2 1 ATOM 3088 N N . LEU A 1 386 ? 14.259 57.551 25.537 1.00 29.13 ? 386 LEU A N 1 ATOM 3089 C CA . LEU A 1 386 ? 13.880 58.838 24.957 1.00 27.99 ? 386 LEU A CA 1 ATOM 3090 C C . LEU A 1 386 ? 15.008 59.481 24.173 1.00 28.74 ? 386 LEU A C 1 ATOM 3091 O O . LEU A 1 386 ? 14.851 60.578 23.635 1.00 29.04 ? 386 LEU A O 1 ATOM 3092 C CB . LEU A 1 386 ? 13.435 59.810 26.054 1.00 26.31 ? 386 LEU A CB 1 ATOM 3093 C CG . LEU A 1 386 ? 12.320 59.341 26.986 1.00 25.23 ? 386 LEU A CG 1 ATOM 3094 C CD1 . LEU A 1 386 ? 11.998 60.441 27.976 1.00 24.41 ? 386 LEU A CD1 1 ATOM 3095 C CD2 . LEU A 1 386 ? 11.094 58.974 26.180 1.00 23.39 ? 386 LEU A CD2 1 ATOM 3096 N N . VAL A 1 387 ? 16.148 58.807 24.106 1.00 29.17 ? 387 VAL A N 1 ATOM 3097 C CA . VAL A 1 387 ? 17.289 59.358 23.389 1.00 29.02 ? 387 VAL A CA 1 ATOM 3098 C C . VAL A 1 387 ? 17.025 59.530 21.899 1.00 30.13 ? 387 VAL A C 1 ATOM 3099 O O . VAL A 1 387 ? 16.387 58.689 21.263 1.00 30.42 ? 387 VAL A O 1 ATOM 3100 C CB . VAL A 1 387 ? 18.539 58.474 23.581 1.00 29.17 ? 387 VAL A CB 1 ATOM 3101 C CG1 . VAL A 1 387 ? 19.686 58.983 22.716 1.00 27.09 ? 387 VAL A CG1 1 ATOM 3102 C CG2 . VAL A 1 387 ? 18.947 58.484 25.044 1.00 30.06 ? 387 VAL A CG2 1 ATOM 3103 N N . ASP A 1 388 ? 17.504 60.642 21.351 1.00 29.34 ? 388 ASP A N 1 ATOM 3104 C CA . ASP A 1 388 ? 17.355 60.916 19.933 1.00 28.91 ? 388 ASP A CA 1 ATOM 3105 C C . ASP A 1 388 ? 18.615 60.404 19.243 1.00 29.43 ? 388 ASP A C 1 ATOM 3106 O O . ASP A 1 388 ? 19.690 60.999 19.359 1.00 27.90 ? 388 ASP A O 1 ATOM 3107 C CB . ASP A 1 388 ? 17.193 62.416 19.695 1.00 30.10 ? 388 ASP A CB 1 ATOM 3108 C CG . ASP A 1 388 ? 17.354 62.792 18.238 1.00 31.61 ? 388 ASP A CG 1 ATOM 3109 O OD1 . ASP A 1 388 ? 17.349 61.887 17.375 1.00 33.56 ? 388 ASP A OD1 1 ATOM 3110 O OD2 . ASP A 1 388 ? 17.482 63.998 17.952 1.00 32.73 ? 388 ASP A OD2 1 ATOM 3111 N N . PRO A 1 389 ? 18.492 59.290 18.504 1.00 29.70 ? 389 PRO A N 1 ATOM 3112 C CA . PRO A 1 389 ? 19.624 58.688 17.798 1.00 28.99 ? 389 PRO A CA 1 ATOM 3113 C C . PRO A 1 389 ? 20.424 59.647 16.929 1.00 28.60 ? 389 PRO A C 1 ATOM 3114 O O . PRO A 1 389 ? 21.647 59.553 16.881 1.00 28.80 ? 389 PRO A O 1 ATOM 3115 C CB . PRO A 1 389 ? 18.979 57.551 17.003 1.00 29.46 ? 389 PRO A CB 1 ATOM 3116 C CG . PRO A 1 389 ? 17.589 58.035 16.780 1.00 29.30 ? 389 PRO A CG 1 ATOM 3117 C CD . PRO A 1 389 ? 17.229 58.641 18.111 1.00 28.58 ? 389 PRO A CD 1 ATOM 3118 N N . GLN A 1 390 ? 19.764 60.574 16.248 1.00 27.81 ? 390 GLN A N 1 ATOM 3119 C CA . GLN A 1 390 ? 20.527 61.498 15.421 1.00 28.45 ? 390 GLN A CA 1 ATOM 3120 C C . GLN A 1 390 ? 21.380 62.426 16.283 1.00 28.68 ? 390 GLN A C 1 ATOM 3121 O O . GLN A 1 390 ? 22.540 62.690 15.961 1.00 29.13 ? 390 GLN A O 1 ATOM 3122 C CB . GLN A 1 390 ? 19.620 62.337 14.521 1.00 27.96 ? 390 GLN A CB 1 ATOM 3123 C CG . GLN A 1 390 ? 20.395 63.427 13.799 1.00 28.64 ? 390 GLN A CG 1 ATOM 3124 C CD . GLN A 1 390 ? 19.557 64.208 12.824 1.00 29.18 ? 390 GLN A CD 1 ATOM 3125 O OE1 . GLN A 1 390 ? 18.436 64.603 13.130 1.00 32.96 ? 390 GLN A OE1 1 ATOM 3126 N NE2 . GLN A 1 390 ? 20.105 64.454 11.640 1.00 30.09 ? 390 GLN A NE2 1 ATOM 3127 N N . ALA A 1 391 ? 20.805 62.919 17.376 1.00 28.29 ? 391 ALA A N 1 ATOM 3128 C CA . ALA A 1 391 ? 21.534 63.810 18.273 1.00 27.61 ? 391 ALA A CA 1 ATOM 3129 C C . ALA A 1 391 ? 22.751 63.068 18.812 1.00 27.40 ? 391 ALA A C 1 ATOM 3130 O O . ALA A 1 391 ? 23.859 63.608 18.862 1.00 27.02 ? 391 ALA A O 1 ATOM 3131 C CB . ALA A 1 391 ? 20.639 64.245 19.422 1.00 27.23 ? 391 ALA A CB 1 ATOM 3132 N N . LEU A 1 392 ? 22.528 61.820 19.203 1.00 25.87 ? 392 LEU A N 1 ATOM 3133 C CA . LEU A 1 392 ? 23.586 60.992 19.741 1.00 25.31 ? 392 LEU A CA 1 ATOM 3134 C C . LEU A 1 392 ? 24.724 60.783 18.739 1.00 26.73 ? 392 LEU A C 1 ATOM 3135 O O . LEU A 1 392 ? 25.891 60.861 19.114 1.00 25.84 ? 392 LEU A O 1 ATOM 3136 C CB . LEU A 1 392 ? 23.009 59.651 20.183 1.00 23.86 ? 392 LEU A CB 1 ATOM 3137 C CG . LEU A 1 392 ? 23.911 58.775 21.052 1.00 23.67 ? 392 LEU A CG 1 ATOM 3138 C CD1 . LEU A 1 392 ? 24.415 59.563 22.247 1.00 21.82 ? 392 LEU A CD1 1 ATOM 3139 C CD2 . LEU A 1 392 ? 23.124 57.558 21.511 1.00 23.12 ? 392 LEU A CD2 1 ATOM 3140 N N . CYS A 1 393 ? 24.397 60.531 17.471 1.00 28.34 ? 393 CYS A N 1 ATOM 3141 C CA . CYS A 1 393 ? 25.437 60.325 16.461 1.00 30.85 ? 393 CYS A CA 1 ATOM 3142 C C . CYS A 1 393 ? 26.198 61.607 16.198 1.00 30.14 ? 393 CYS A C 1 ATOM 3143 O O . CYS A 1 393 ? 27.394 61.579 15.916 1.00 29.53 ? 393 CYS A O 1 ATOM 3144 C CB . CYS A 1 393 ? 24.856 59.838 15.134 1.00 33.50 ? 393 CYS A CB 1 ATOM 3145 S SG . CYS A 1 393 ? 24.111 58.170 15.152 1.00 46.66 ? 393 CYS A SG 1 ATOM 3146 N N . ASN A 1 394 ? 25.502 62.734 16.263 1.00 29.20 ? 394 ASN A N 1 ATOM 3147 C CA . ASN A 1 394 ? 26.161 64.004 16.035 1.00 30.62 ? 394 ASN A CA 1 ATOM 3148 C C . ASN A 1 394 ? 27.042 64.344 17.229 1.00 31.98 ? 394 ASN A C 1 ATOM 3149 O O . ASN A 1 394 ? 28.090 64.970 17.076 1.00 31.19 ? 394 ASN A O 1 ATOM 3150 C CB . ASN A 1 394 ? 25.127 65.099 15.781 1.00 30.04 ? 394 ASN A CB 1 ATOM 3151 C CG . ASN A 1 394 ? 24.703 65.165 14.321 1.00 32.39 ? 394 ASN A CG 1 ATOM 3152 O OD1 . ASN A 1 394 ? 25.495 65.537 13.452 1.00 33.63 ? 394 ASN A OD1 1 ATOM 3153 N ND2 . ASN A 1 394 ? 23.455 64.796 14.043 1.00 30.04 ? 394 ASN A ND2 1 ATOM 3154 N N . GLU A 1 395 ? 26.623 63.914 18.416 1.00 32.90 ? 395 GLU A N 1 ATOM 3155 C CA . GLU A 1 395 ? 27.398 64.165 19.620 1.00 33.97 ? 395 GLU A CA 1 ATOM 3156 C C . GLU A 1 395 ? 28.623 63.250 19.660 1.00 34.00 ? 395 GLU A C 1 ATOM 3157 O O . GLU A 1 395 ? 29.710 63.683 20.038 1.00 34.01 ? 395 GLU A O 1 ATOM 3158 C CB . GLU A 1 395 ? 26.541 63.936 20.875 1.00 37.46 ? 395 GLU A CB 1 ATOM 3159 C CG . GLU A 1 395 ? 27.319 64.046 22.188 1.00 42.57 ? 395 GLU A CG 1 ATOM 3160 C CD . GLU A 1 395 ? 26.498 63.659 23.420 1.00 48.62 ? 395 GLU A CD 1 ATOM 3161 O OE1 . GLU A 1 395 ? 25.869 62.574 23.419 1.00 50.27 ? 395 GLU A OE1 1 ATOM 3162 O OE2 . GLU A 1 395 ? 26.494 64.433 24.403 1.00 52.39 ? 395 GLU A OE2 1 ATOM 3163 N N . ARG A 1 396 ? 28.449 61.991 19.259 1.00 32.32 ? 396 ARG A N 1 ATOM 3164 C CA . ARG A 1 396 ? 29.539 61.020 19.276 1.00 30.83 ? 396 ARG A CA 1 ATOM 3165 C C . ARG A 1 396 ? 29.844 60.416 17.912 1.00 29.85 ? 396 ARG A C 1 ATOM 3166 O O . ARG A 1 396 ? 29.278 59.388 17.534 1.00 31.07 ? 396 ARG A O 1 ATOM 3167 C CB . ARG A 1 396 ? 29.220 59.889 20.255 1.00 32.49 ? 396 ARG A CB 1 ATOM 3168 C CG . ARG A 1 396 ? 28.827 60.369 21.632 1.00 33.36 ? 396 ARG A CG 1 ATOM 3169 C CD . ARG A 1 396 ? 28.571 59.216 22.576 1.00 35.99 ? 396 ARG A CD 1 ATOM 3170 N NE . ARG A 1 396 ? 27.836 59.671 23.751 1.00 40.48 ? 396 ARG A NE 1 ATOM 3171 C CZ . ARG A 1 396 ? 27.417 58.883 24.737 1.00 41.56 ? 396 ARG A CZ 1 ATOM 3172 N NH1 . ARG A 1 396 ? 27.663 57.576 24.704 1.00 41.98 ? 396 ARG A NH1 1 ATOM 3173 N NH2 . ARG A 1 396 ? 26.739 59.407 25.753 1.00 40.86 ? 396 ARG A NH2 1 ATOM 3174 N N . GLY A 1 397 ? 30.751 61.056 17.185 1.00 28.17 ? 397 GLY A N 1 ATOM 3175 C CA . GLY A 1 397 ? 31.129 60.568 15.874 1.00 25.94 ? 397 GLY A CA 1 ATOM 3176 C C . GLY A 1 397 ? 32.128 59.434 15.968 1.00 26.09 ? 397 GLY A C 1 ATOM 3177 O O . GLY A 1 397 ? 32.304 58.832 17.028 1.00 25.65 ? 397 GLY A O 1 ATOM 3178 N N . ALA A 1 398 ? 32.791 59.147 14.854 1.00 27.03 ? 398 ALA A N 1 ATOM 3179 C CA . ALA A 1 398 ? 33.767 58.069 14.795 1.00 27.19 ? 398 ALA A CA 1 ATOM 3180 C C . ALA A 1 398 ? 34.960 58.293 15.724 1.00 28.46 ? 398 ALA A C 1 ATOM 3181 O O . ALA A 1 398 ? 35.653 57.341 16.088 1.00 28.41 ? 398 ALA A O 1 ATOM 3182 C CB . ALA A 1 398 ? 34.247 57.890 13.367 1.00 24.84 ? 398 ALA A CB 1 ATOM 3183 N N . SER A 1 399 ? 35.201 59.543 16.108 1.00 28.19 ? 399 SER A N 1 ATOM 3184 C CA . SER A 1 399 ? 36.321 59.847 16.986 1.00 27.31 ? 399 SER A CA 1 ATOM 3185 C C . SER A 1 399 ? 35.964 59.672 18.455 1.00 27.12 ? 399 SER A C 1 ATOM 3186 O O . SER A 1 399 ? 36.843 59.690 19.310 1.00 26.42 ? 399 SER A O 1 ATOM 3187 C CB . SER A 1 399 ? 36.814 61.267 16.741 1.00 28.22 ? 399 SER A CB 1 ATOM 3188 O OG . SER A 1 399 ? 35.779 62.200 16.971 1.00 31.95 ? 399 SER A OG 1 ATOM 3189 N N . SER A 1 400 ? 34.677 59.518 18.754 1.00 26.97 ? 400 SER A N 1 ATOM 3190 C CA . SER A 1 400 ? 34.239 59.316 20.132 1.00 26.60 ? 400 SER A CA 1 ATOM 3191 C C . SER A 1 400 ? 34.330 57.817 20.396 1.00 27.35 ? 400 SER A C 1 ATOM 3192 O O . SER A 1 400 ? 33.510 57.046 19.903 1.00 28.55 ? 400 SER A O 1 ATOM 3193 C CB . SER A 1 400 ? 32.796 59.798 20.320 1.00 26.48 ? 400 SER A CB 1 ATOM 3194 O OG . SER A 1 400 ? 32.307 59.462 21.614 1.00 28.15 ? 400 SER A OG 1 ATOM 3195 N N . ARG A 1 401 ? 35.330 57.408 21.170 1.00 27.23 ? 401 ARG A N 1 ATOM 3196 C CA . ARG A 1 401 ? 35.543 55.994 21.455 1.00 26.94 ? 401 ARG A CA 1 ATOM 3197 C C . ARG A 1 401 ? 34.693 55.426 22.588 1.00 26.53 ? 401 ARG A C 1 ATOM 3198 O O . ARG A 1 401 ? 34.659 55.971 23.685 1.00 29.05 ? 401 ARG A O 1 ATOM 3199 C CB . ARG A 1 401 ? 37.029 55.753 21.748 1.00 26.31 ? 401 ARG A CB 1 ATOM 3200 C CG . ARG A 1 401 ? 37.967 56.278 20.658 1.00 26.45 ? 401 ARG A CG 1 ATOM 3201 C CD . ARG A 1 401 ? 39.377 55.767 20.870 1.00 26.78 ? 401 ARG A CD 1 ATOM 3202 N NE . ARG A 1 401 ? 39.396 54.307 20.889 1.00 30.72 ? 401 ARG A NE 1 ATOM 3203 C CZ . ARG A 1 401 ? 40.435 53.567 21.271 1.00 32.37 ? 401 ARG A CZ 1 ATOM 3204 N NH1 . ARG A 1 401 ? 41.560 54.143 21.673 1.00 31.98 ? 401 ARG A NH1 1 ATOM 3205 N NH2 . ARG A 1 401 ? 40.342 52.243 21.263 1.00 31.56 ? 401 ARG A NH2 1 ATOM 3206 N N . GLY A 1 402 ? 34.004 54.325 22.312 1.00 26.00 ? 402 GLY A N 1 ATOM 3207 C CA . GLY A 1 402 ? 33.182 53.689 23.327 1.00 24.92 ? 402 GLY A CA 1 ATOM 3208 C C . GLY A 1 402 ? 33.714 52.302 23.648 1.00 26.20 ? 402 GLY A C 1 ATOM 3209 O O . GLY A 1 402 ? 34.881 51.998 23.372 1.00 25.89 ? 402 GLY A O 1 ATOM 3210 N N . ALA A 1 403 ? 32.876 51.462 24.249 1.00 26.39 ? 403 ALA A N 1 ATOM 3211 C CA . ALA A 1 403 ? 33.269 50.092 24.576 1.00 26.12 ? 403 ALA A CA 1 ATOM 3212 C C . ALA A 1 403 ? 32.987 49.302 23.305 1.00 26.10 ? 403 ALA A C 1 ATOM 3213 O O . ALA A 1 403 ? 33.902 48.891 22.595 1.00 25.65 ? 403 ALA A O 1 ATOM 3214 C CB . ALA A 1 403 ? 32.430 49.562 25.724 1.00 24.32 ? 403 ALA A CB 1 ATOM 3215 N N . LEU A 1 404 ? 31.702 49.104 23.035 1.00 26.19 ? 404 LEU A N 1 ATOM 3216 C CA . LEU A 1 404 ? 31.244 48.420 21.836 1.00 25.85 ? 404 LEU A CA 1 ATOM 3217 C C . LEU A 1 404 ? 30.863 49.523 20.846 1.00 25.53 ? 404 LEU A C 1 ATOM 3218 O O . LEU A 1 404 ? 29.743 50.046 20.866 1.00 24.67 ? 404 LEU A O 1 ATOM 3219 C CB . LEU A 1 404 ? 30.029 47.552 22.158 1.00 27.13 ? 404 LEU A CB 1 ATOM 3220 C CG . LEU A 1 404 ? 30.244 46.048 22.352 1.00 28.15 ? 404 LEU A CG 1 ATOM 3221 C CD1 . LEU A 1 404 ? 31.706 45.732 22.541 1.00 28.44 ? 404 LEU A CD1 1 ATOM 3222 C CD2 . LEU A 1 404 ? 29.426 45.581 23.539 1.00 26.27 ? 404 LEU A CD2 1 ATOM 3223 N N . GLY A 1 405 ? 31.815 49.881 19.995 1.00 24.01 ? 405 GLY A N 1 ATOM 3224 C CA . GLY A 1 405 ? 31.590 50.926 19.022 1.00 23.25 ? 405 GLY A CA 1 ATOM 3225 C C . GLY A 1 405 ? 32.513 52.097 19.308 1.00 24.04 ? 405 GLY A C 1 ATOM 3226 O O . GLY A 1 405 ? 33.005 52.247 20.428 1.00 23.52 ? 405 GLY A O 1 ATOM 3227 N N . PRO A 1 406 ? 32.764 52.955 18.311 1.00 23.64 ? 406 PRO A N 1 ATOM 3228 C CA . PRO A 1 406 ? 32.182 52.797 16.979 1.00 23.49 ? 406 PRO A CA 1 ATOM 3229 C C . PRO A 1 406 ? 32.945 51.797 16.118 1.00 23.50 ? 406 PRO A C 1 ATOM 3230 O O . PRO A 1 406 ? 34.174 51.823 16.052 1.00 22.79 ? 406 PRO A O 1 ATOM 3231 C CB . PRO A 1 406 ? 32.251 54.211 16.408 1.00 22.53 ? 406 PRO A CB 1 ATOM 3232 C CG . PRO A 1 406 ? 33.553 54.713 16.971 1.00 22.63 ? 406 PRO A CG 1 ATOM 3233 C CD . PRO A 1 406 ? 33.518 54.220 18.415 1.00 23.45 ? 406 PRO A CD 1 ATOM 3234 N N . PHE A 1 407 ? 32.213 50.897 15.480 1.00 23.22 ? 407 PHE A N 1 ATOM 3235 C CA . PHE A 1 407 ? 32.841 49.943 14.583 1.00 23.13 ? 407 PHE A CA 1 ATOM 3236 C C . PHE A 1 407 ? 31.978 49.869 13.335 1.00 23.29 ? 407 PHE A C 1 ATOM 3237 O O . PHE A 1 407 ? 30.748 49.820 13.411 1.00 22.17 ? 407 PHE A O 1 ATOM 3238 C CB . PHE A 1 407 ? 33.018 48.564 15.246 1.00 21.00 ? 407 PHE A CB 1 ATOM 3239 C CG . PHE A 1 407 ? 31.740 47.914 15.676 1.00 19.48 ? 407 PHE A CG 1 ATOM 3240 C CD1 . PHE A 1 407 ? 30.922 47.276 14.753 1.00 18.57 ? 407 PHE A CD1 1 ATOM 3241 C CD2 . PHE A 1 407 ? 31.364 47.923 17.017 1.00 19.66 ? 407 PHE A CD2 1 ATOM 3242 C CE1 . PHE A 1 407 ? 29.744 46.650 15.158 1.00 18.64 ? 407 PHE A CE1 1 ATOM 3243 C CE2 . PHE A 1 407 ? 30.190 47.302 17.435 1.00 18.41 ? 407 PHE A CE2 1 ATOM 3244 C CZ . PHE A 1 407 ? 29.378 46.663 16.503 1.00 18.69 ? 407 PHE A CZ 1 ATOM 3245 N N . GLY A 1 408 ? 32.636 49.910 12.183 1.00 23.56 ? 408 GLY A N 1 ATOM 3246 C CA . GLY A 1 408 ? 31.911 49.862 10.932 1.00 23.02 ? 408 GLY A CA 1 ATOM 3247 C C . GLY A 1 408 ? 32.749 50.119 9.696 1.00 23.65 ? 408 GLY A C 1 ATOM 3248 O O . GLY A 1 408 ? 33.850 49.588 9.537 1.00 24.34 ? 408 GLY A O 1 ATOM 3249 N N . LEU A 1 409 ? 32.227 50.968 8.824 1.00 24.34 ? 409 LEU A N 1 ATOM 3250 C CA . LEU A 1 409 ? 32.891 51.267 7.571 1.00 24.85 ? 409 LEU A CA 1 ATOM 3251 C C . LEU A 1 409 ? 33.290 52.732 7.397 1.00 24.63 ? 409 LEU A C 1 ATOM 3252 O O . LEU A 1 409 ? 32.659 53.638 7.944 1.00 23.90 ? 409 LEU A O 1 ATOM 3253 C CB . LEU A 1 409 ? 31.961 50.868 6.429 1.00 26.95 ? 409 LEU A CB 1 ATOM 3254 C CG . LEU A 1 409 ? 32.584 50.293 5.166 1.00 30.39 ? 409 LEU A CG 1 ATOM 3255 C CD1 . LEU A 1 409 ? 33.113 48.899 5.468 1.00 31.67 ? 409 LEU A CD1 1 ATOM 3256 C CD2 . LEU A 1 409 ? 31.538 50.233 4.062 1.00 31.84 ? 409 LEU A CD2 1 ATOM 3257 N N . LEU A 1 410 ? 34.358 52.944 6.637 1.00 24.90 ? 410 LEU A N 1 ATOM 3258 C CA . LEU A 1 410 ? 34.836 54.283 6.307 1.00 24.81 ? 410 LEU A CA 1 ATOM 3259 C C . LEU A 1 410 ? 34.745 54.323 4.781 1.00 26.19 ? 410 LEU A C 1 ATOM 3260 O O . LEU A 1 410 ? 35.571 53.712 4.093 1.00 26.34 ? 410 LEU A O 1 ATOM 3261 C CB . LEU A 1 410 ? 36.289 54.482 6.748 1.00 23.11 ? 410 LEU A CB 1 ATOM 3262 C CG . LEU A 1 410 ? 36.605 54.461 8.246 1.00 23.67 ? 410 LEU A CG 1 ATOM 3263 C CD1 . LEU A 1 410 ? 38.097 54.673 8.431 1.00 23.00 ? 410 LEU A CD1 1 ATOM 3264 C CD2 . LEU A 1 410 ? 35.818 55.538 8.987 1.00 19.75 ? 410 LEU A CD2 1 ATOM 3265 N N . ALA A 1 411 ? 33.729 55.010 4.256 1.00 24.96 ? 411 ALA A N 1 ATOM 3266 C CA . ALA A 1 411 ? 33.531 55.098 2.810 1.00 24.55 ? 411 ALA A CA 1 ATOM 3267 C C . ALA A 1 411 ? 33.907 56.473 2.269 1.00 24.53 ? 411 ALA A C 1 ATOM 3268 O O . ALA A 1 411 ? 34.020 57.432 3.032 1.00 25.64 ? 411 ALA A O 1 ATOM 3269 C CB . ALA A 1 411 ? 32.081 54.766 2.461 1.00 21.68 ? 411 ALA A CB 1 ATOM 3270 N N . MET A 1 412 ? 34.090 56.560 0.953 1.00 24.66 ? 412 MET A N 1 ATOM 3271 C CA . MET A 1 412 ? 34.475 57.805 0.292 1.00 25.04 ? 412 MET A CA 1 ATOM 3272 C C . MET A 1 412 ? 35.555 58.503 1.103 1.00 25.59 ? 412 MET A C 1 ATOM 3273 O O . MET A 1 412 ? 35.478 59.700 1.374 1.00 25.31 ? 412 MET A O 1 ATOM 3274 C CB . MET A 1 412 ? 33.268 58.729 0.121 1.00 25.30 ? 412 MET A CB 1 ATOM 3275 C CG . MET A 1 412 ? 32.290 58.272 -0.946 1.00 24.55 ? 412 MET A CG 1 ATOM 3276 S SD . MET A 1 412 ? 33.110 57.813 -2.493 1.00 27.54 ? 412 MET A SD 1 ATOM 3277 C CE . MET A 1 412 ? 33.762 59.392 -3.048 1.00 23.32 ? 412 MET A CE 1 ATOM 3278 N N . ALA A 1 413 ? 36.568 57.737 1.484 1.00 26.26 ? 413 ALA A N 1 ATOM 3279 C CA . ALA A 1 413 ? 37.664 58.252 2.286 1.00 27.48 ? 413 ALA A CA 1 ATOM 3280 C C . ALA A 1 413 ? 38.923 58.489 1.467 1.00 29.27 ? 413 ALA A C 1 ATOM 3281 O O . ALA A 1 413 ? 39.164 57.809 0.467 1.00 29.24 ? 413 ALA A O 1 ATOM 3282 C CB . ALA A 1 413 ? 37.960 57.283 3.412 1.00 26.06 ? 413 ALA A CB 1 ATOM 3283 N N . SER A 1 414 ? 39.724 59.462 1.893 1.00 29.69 ? 414 SER A N 1 ATOM 3284 C CA . SER A 1 414 ? 40.975 59.759 1.209 1.00 31.79 ? 414 SER A CA 1 ATOM 3285 C C . SER A 1 414 ? 42.054 58.879 1.833 1.00 34.00 ? 414 SER A C 1 ATOM 3286 O O . SER A 1 414 ? 41.894 58.398 2.953 1.00 33.47 ? 414 SER A O 1 ATOM 3287 C CB . SER A 1 414 ? 41.336 61.240 1.356 1.00 29.87 ? 414 SER A CB 1 ATOM 3288 O OG . SER A 1 414 ? 41.503 61.607 2.712 1.00 30.20 ? 414 SER A OG 1 ATOM 3289 N N . LYS A 1 415 ? 43.143 58.661 1.104 1.00 37.42 ? 415 LYS A N 1 ATOM 3290 C CA . LYS A 1 415 ? 44.230 57.817 1.589 1.00 40.40 ? 415 LYS A CA 1 ATOM 3291 C C . LYS A 1 415 ? 44.692 58.191 2.997 1.00 40.36 ? 415 LYS A C 1 ATOM 3292 O O . LYS A 1 415 ? 44.895 57.325 3.847 1.00 39.65 ? 415 LYS A O 1 ATOM 3293 C CB . LYS A 1 415 ? 45.415 57.884 0.623 1.00 43.26 ? 415 LYS A CB 1 ATOM 3294 C CG . LYS A 1 415 ? 46.485 56.836 0.892 1.00 49.20 ? 415 LYS A CG 1 ATOM 3295 C CD . LYS A 1 415 ? 47.618 56.910 -0.128 1.00 53.42 ? 415 LYS A CD 1 ATOM 3296 C CE . LYS A 1 415 ? 48.662 55.820 0.115 1.00 55.60 ? 415 LYS A CE 1 ATOM 3297 N NZ . LYS A 1 415 ? 48.085 54.441 0.014 1.00 58.24 ? 415 LYS A NZ 1 ATOM 3298 N N . ASP A 1 416 ? 44.845 59.486 3.237 1.00 40.52 ? 416 ASP A N 1 ATOM 3299 C CA . ASP A 1 416 ? 45.293 59.996 4.531 1.00 41.38 ? 416 ASP A CA 1 ATOM 3300 C C . ASP A 1 416 ? 44.182 60.057 5.582 1.00 40.20 ? 416 ASP A C 1 ATOM 3301 O O . ASP A 1 416 ? 44.433 60.390 6.742 1.00 39.60 ? 416 ASP A O 1 ATOM 3302 C CB . ASP A 1 416 ? 45.873 61.399 4.341 1.00 45.11 ? 416 ASP A CB 1 ATOM 3303 C CG . ASP A 1 416 ? 44.958 62.297 3.520 1.00 47.55 ? 416 ASP A CG 1 ATOM 3304 O OD1 . ASP A 1 416 ? 43.760 62.394 3.855 1.00 48.12 ? 416 ASP A OD1 1 ATOM 3305 O OD2 . ASP A 1 416 ? 45.433 62.906 2.539 1.00 50.29 ? 416 ASP A OD2 1 ATOM 3306 N N . LEU A 1 417 ? 42.958 59.743 5.166 1.00 37.87 ? 417 LEU A N 1 ATOM 3307 C CA . LEU A 1 417 ? 41.791 59.783 6.044 1.00 35.73 ? 417 LEU A CA 1 ATOM 3308 C C . LEU A 1 417 ? 41.458 61.201 6.501 1.00 35.67 ? 417 LEU A C 1 ATOM 3309 O O . LEU A 1 417 ? 40.774 61.392 7.504 1.00 35.84 ? 417 LEU A O 1 ATOM 3310 C CB . LEU A 1 417 ? 41.983 58.884 7.270 1.00 31.80 ? 417 LEU A CB 1 ATOM 3311 C CG . LEU A 1 417 ? 41.957 57.375 7.030 1.00 29.79 ? 417 LEU A CG 1 ATOM 3312 C CD1 . LEU A 1 417 ? 41.947 56.677 8.365 1.00 27.54 ? 417 LEU A CD1 1 ATOM 3313 C CD2 . LEU A 1 417 ? 40.722 56.977 6.235 1.00 29.32 ? 417 LEU A CD2 1 ATOM 3314 N N . LYS A 1 418 ? 41.940 62.193 5.758 1.00 36.47 ? 418 LYS A N 1 ATOM 3315 C CA . LYS A 1 418 ? 41.670 63.591 6.076 1.00 36.82 ? 418 LYS A CA 1 ATOM 3316 C C . LYS A 1 418 ? 40.171 63.806 5.873 1.00 34.98 ? 418 LYS A C 1 ATOM 3317 O O . LYS A 1 418 ? 39.558 64.651 6.521 1.00 35.96 ? 418 LYS A O 1 ATOM 3318 C CB . LYS A 1 418 ? 42.458 64.511 5.139 1.00 41.49 ? 418 LYS A CB 1 ATOM 3319 C CG . LYS A 1 418 ? 43.061 65.748 5.801 1.00 47.85 ? 418 LYS A CG 1 ATOM 3320 C CD . LYS A 1 418 ? 44.229 65.383 6.723 1.00 52.35 ? 418 LYS A CD 1 ATOM 3321 C CE . LYS A 1 418 ? 45.350 64.650 5.975 1.00 54.38 ? 418 LYS A CE 1 ATOM 3322 N NZ . LYS A 1 418 ? 45.981 65.470 4.897 1.00 55.55 ? 418 LYS A NZ 1 ATOM 3323 N N . GLU A 1 419 ? 39.596 63.036 4.954 1.00 32.71 ? 419 GLU A N 1 ATOM 3324 C CA . GLU A 1 419 ? 38.167 63.090 4.656 1.00 30.93 ? 419 GLU A CA 1 ATOM 3325 C C . GLU A 1 419 ? 37.645 61.662 4.673 1.00 29.73 ? 419 GLU A C 1 ATOM 3326 O O . GLU A 1 419 ? 38.285 60.756 4.140 1.00 29.74 ? 419 GLU A O 1 ATOM 3327 C CB . GLU A 1 419 ? 37.916 63.725 3.285 1.00 30.46 ? 419 GLU A CB 1 ATOM 3328 C CG . GLU A 1 419 ? 38.147 65.227 3.263 1.00 31.53 ? 419 GLU A CG 1 ATOM 3329 C CD . GLU A 1 419 ? 38.025 65.824 1.879 1.00 32.20 ? 419 GLU A CD 1 ATOM 3330 O OE1 . GLU A 1 419 ? 38.786 65.408 0.975 1.00 32.95 ? 419 GLU A OE1 1 ATOM 3331 O OE2 . GLU A 1 419 ? 37.168 66.714 1.698 1.00 34.25 ? 419 GLU A OE2 1 ATOM 3332 N N . GLN A 1 420 ? 36.486 61.460 5.288 1.00 28.35 ? 420 GLN A N 1 ATOM 3333 C CA . GLN A 1 420 ? 35.910 60.126 5.389 1.00 26.59 ? 420 GLN A CA 1 ATOM 3334 C C . GLN A 1 420 ? 34.451 60.191 5.799 1.00 26.35 ? 420 GLN A C 1 ATOM 3335 O O . GLN A 1 420 ? 34.009 61.164 6.412 1.00 26.29 ? 420 GLN A O 1 ATOM 3336 C CB . GLN A 1 420 ? 36.659 59.313 6.449 1.00 26.73 ? 420 GLN A CB 1 ATOM 3337 C CG . GLN A 1 420 ? 36.622 59.974 7.831 1.00 26.95 ? 420 GLN A CG 1 ATOM 3338 C CD . GLN A 1 420 ? 37.142 59.089 8.954 1.00 27.61 ? 420 GLN A CD 1 ATOM 3339 O OE1 . GLN A 1 420 ? 38.217 58.498 8.850 1.00 29.03 ? 420 GLN A OE1 1 ATOM 3340 N NE2 . GLN A 1 420 ? 36.385 59.012 10.045 1.00 23.33 ? 420 GLN A NE2 1 ATOM 3341 N N . SER A 1 421 ? 33.709 59.145 5.458 1.00 24.41 ? 421 SER A N 1 ATOM 3342 C CA . SER A 1 421 ? 32.313 59.044 5.842 1.00 23.87 ? 421 SER A CA 1 ATOM 3343 C C . SER A 1 421 ? 32.234 57.747 6.626 1.00 23.96 ? 421 SER A C 1 ATOM 3344 O O . SER A 1 421 ? 32.464 56.665 6.088 1.00 24.63 ? 421 SER A O 1 ATOM 3345 C CB . SER A 1 421 ? 31.417 58.999 4.612 1.00 23.77 ? 421 SER A CB 1 ATOM 3346 O OG . SER A 1 421 ? 31.407 60.263 3.970 1.00 25.68 ? 421 SER A OG 1 ATOM 3347 N N . ALA A 1 422 ? 31.928 57.862 7.911 1.00 23.81 ? 422 ALA A N 1 ATOM 3348 C CA . ALA A 1 422 ? 31.873 56.697 8.779 1.00 23.01 ? 422 ALA A CA 1 ATOM 3349 C C . ALA A 1 422 ? 30.479 56.168 9.076 1.00 23.25 ? 422 ALA A C 1 ATOM 3350 O O . ALA A 1 422 ? 29.667 56.846 9.704 1.00 23.24 ? 422 ALA A O 1 ATOM 3351 C CB . ALA A 1 422 ? 32.589 57.009 10.086 1.00 20.57 ? 422 ALA A CB 1 ATOM 3352 N N . ILE A 1 423 ? 30.201 54.956 8.609 1.00 22.02 ? 423 ILE A N 1 ATOM 3353 C CA . ILE A 1 423 ? 28.921 54.326 8.885 1.00 21.77 ? 423 ILE A CA 1 ATOM 3354 C C . ILE A 1 423 ? 29.290 53.252 9.911 1.00 21.54 ? 423 ILE A C 1 ATOM 3355 O O . ILE A 1 423 ? 30.039 52.325 9.607 1.00 21.44 ? 423 ILE A O 1 ATOM 3356 C CB . ILE A 1 423 ? 28.292 53.707 7.605 1.00 22.68 ? 423 ILE A CB 1 ATOM 3357 C CG1 . ILE A 1 423 ? 27.804 54.816 6.663 1.00 23.42 ? 423 ILE A CG1 1 ATOM 3358 C CG2 . ILE A 1 423 ? 27.063 52.880 7.972 1.00 19.71 ? 423 ILE A CG2 1 ATOM 3359 C CD1 . ILE A 1 423 ? 28.861 55.751 6.183 1.00 23.71 ? 423 ILE A CD1 1 ATOM 3360 N N . PHE A 1 424 ? 28.782 53.393 11.130 1.00 20.99 ? 424 PHE A N 1 ATOM 3361 C CA . PHE A 1 424 ? 29.125 52.458 12.196 1.00 21.40 ? 424 PHE A CA 1 ATOM 3362 C C . PHE A 1 424 ? 28.010 52.149 13.187 1.00 21.79 ? 424 PHE A C 1 ATOM 3363 O O . PHE A 1 424 ? 26.916 52.702 13.118 1.00 21.38 ? 424 PHE A O 1 ATOM 3364 C CB . PHE A 1 424 ? 30.323 53.008 12.965 1.00 21.28 ? 424 PHE A CB 1 ATOM 3365 C CG . PHE A 1 424 ? 30.053 54.325 13.647 1.00 20.45 ? 424 PHE A CG 1 ATOM 3366 C CD1 . PHE A 1 424 ? 29.320 54.381 14.832 1.00 20.02 ? 424 PHE A CD1 1 ATOM 3367 C CD2 . PHE A 1 424 ? 30.551 55.512 13.111 1.00 20.46 ? 424 PHE A CD2 1 ATOM 3368 C CE1 . PHE A 1 424 ? 29.088 55.599 15.476 1.00 18.54 ? 424 PHE A CE1 1 ATOM 3369 C CE2 . PHE A 1 424 ? 30.324 56.737 13.748 1.00 20.81 ? 424 PHE A CE2 1 ATOM 3370 C CZ . PHE A 1 424 ? 29.594 56.779 14.932 1.00 18.44 ? 424 PHE A CZ 1 ATOM 3371 N N . PHE A 1 425 ? 28.318 51.267 14.129 1.00 22.44 ? 425 PHE A N 1 ATOM 3372 C CA . PHE A 1 425 ? 27.362 50.867 15.152 1.00 23.55 ? 425 PHE A CA 1 ATOM 3373 C C . PHE A 1 425 ? 27.943 51.091 16.548 1.00 25.08 ? 425 PHE A C 1 ATOM 3374 O O . PHE A 1 425 ? 29.160 51.241 16.714 1.00 25.00 ? 425 PHE A O 1 ATOM 3375 C CB . PHE A 1 425 ? 27.024 49.379 14.999 1.00 22.66 ? 425 PHE A CB 1 ATOM 3376 C CG . PHE A 1 425 ? 26.365 49.024 13.690 1.00 23.16 ? 425 PHE A CG 1 ATOM 3377 C CD1 . PHE A 1 425 ? 25.035 49.351 13.451 1.00 22.69 ? 425 PHE A CD1 1 ATOM 3378 C CD2 . PHE A 1 425 ? 27.068 48.323 12.712 1.00 22.94 ? 425 PHE A CD2 1 ATOM 3379 C CE1 . PHE A 1 425 ? 24.411 48.984 12.260 1.00 23.54 ? 425 PHE A CE1 1 ATOM 3380 C CE2 . PHE A 1 425 ? 26.453 47.949 11.513 1.00 25.20 ? 425 PHE A CE2 1 ATOM 3381 C CZ . PHE A 1 425 ? 25.120 48.280 11.287 1.00 24.61 ? 425 PHE A CZ 1 ATOM 3382 N N . ARG A 1 426 ? 27.058 51.132 17.544 1.00 25.29 ? 426 ARG A N 1 ATOM 3383 C CA . ARG A 1 426 ? 27.439 51.264 18.951 1.00 24.34 ? 426 ARG A CA 1 ATOM 3384 C C . ARG A 1 426 ? 26.448 50.354 19.649 1.00 24.42 ? 426 ARG A C 1 ATOM 3385 O O . ARG A 1 426 ? 25.320 50.200 19.182 1.00 23.33 ? 426 ARG A O 1 ATOM 3386 C CB . ARG A 1 426 ? 27.264 52.696 19.479 1.00 22.66 ? 426 ARG A CB 1 ATOM 3387 C CG . ARG A 1 426 ? 27.880 53.775 18.598 1.00 27.10 ? 426 ARG A CG 1 ATOM 3388 C CD . ARG A 1 426 ? 27.994 55.125 19.307 1.00 23.20 ? 426 ARG A CD 1 ATOM 3389 N NE . ARG A 1 426 ? 29.257 55.203 20.017 1.00 24.50 ? 426 ARG A NE 1 ATOM 3390 C CZ . ARG A 1 426 ? 30.256 56.017 19.700 1.00 25.58 ? 426 ARG A CZ 1 ATOM 3391 N NH1 . ARG A 1 426 ? 30.157 56.858 18.679 1.00 25.93 ? 426 ARG A NH1 1 ATOM 3392 N NH2 . ARG A 1 426 ? 31.382 55.958 20.391 1.00 27.82 ? 426 ARG A NH2 1 ATOM 3393 N N . VAL A 1 427 ? 26.863 49.714 20.736 1.00 25.27 ? 427 VAL A N 1 ATOM 3394 C CA . VAL A 1 427 ? 25.943 48.856 21.468 1.00 25.60 ? 427 VAL A CA 1 ATOM 3395 C C . VAL A 1 427 ? 25.872 49.361 22.895 1.00 26.68 ? 427 VAL A C 1 ATOM 3396 O O . VAL A 1 427 ? 26.897 49.652 23.508 1.00 27.90 ? 427 VAL A O 1 ATOM 3397 C CB . VAL A 1 427 ? 26.388 47.377 21.459 1.00 25.43 ? 427 VAL A CB 1 ATOM 3398 C CG1 . VAL A 1 427 ? 25.386 46.532 22.231 1.00 23.52 ? 427 VAL A CG1 1 ATOM 3399 C CG2 . VAL A 1 427 ? 26.480 46.871 20.027 1.00 25.07 ? 427 VAL A CG2 1 ATOM 3400 N N . PHE A 1 428 ? 24.655 49.491 23.410 1.00 27.51 ? 428 PHE A N 1 ATOM 3401 C CA . PHE A 1 428 ? 24.443 49.977 24.768 1.00 27.70 ? 428 PHE A CA 1 ATOM 3402 C C . PHE A 1 428 ? 23.533 49.011 25.505 1.00 29.67 ? 428 PHE A C 1 ATOM 3403 O O . PHE A 1 428 ? 22.929 48.118 24.901 1.00 29.94 ? 428 PHE A O 1 ATOM 3404 C CB . PHE A 1 428 ? 23.754 51.348 24.758 1.00 25.56 ? 428 PHE A CB 1 ATOM 3405 C CG . PHE A 1 428 ? 24.530 52.427 24.060 1.00 25.76 ? 428 PHE A CG 1 ATOM 3406 C CD1 . PHE A 1 428 ? 25.666 52.980 24.643 1.00 25.73 ? 428 PHE A CD1 1 ATOM 3407 C CD2 . PHE A 1 428 ? 24.105 52.914 22.827 1.00 25.02 ? 428 PHE A CD2 1 ATOM 3408 C CE1 . PHE A 1 428 ? 26.370 54.009 24.008 1.00 25.62 ? 428 PHE A CE1 1 ATOM 3409 C CE2 . PHE A 1 428 ? 24.798 53.940 22.181 1.00 25.77 ? 428 PHE A CE2 1 ATOM 3410 C CZ . PHE A 1 428 ? 25.932 54.489 22.772 1.00 25.62 ? 428 PHE A CZ 1 ATOM 3411 N N . GLN A 1 429 ? 23.436 49.203 26.814 1.00 30.11 ? 429 GLN A N 1 ATOM 3412 C CA . GLN A 1 429 ? 22.556 48.395 27.638 1.00 31.00 ? 429 GLN A CA 1 ATOM 3413 C C . GLN A 1 429 ? 21.953 49.298 28.703 1.00 32.50 ? 429 GLN A C 1 ATOM 3414 O O . GLN A 1 429 ? 22.586 50.267 29.135 1.00 30.92 ? 429 GLN A O 1 ATOM 3415 C CB . GLN A 1 429 ? 23.316 47.248 28.298 1.00 30.50 ? 429 GLN A CB 1 ATOM 3416 C CG . GLN A 1 429 ? 24.438 47.685 29.214 1.00 32.04 ? 429 GLN A CG 1 ATOM 3417 C CD . GLN A 1 429 ? 25.049 46.518 29.966 1.00 33.02 ? 429 GLN A CD 1 ATOM 3418 O OE1 . GLN A 1 429 ? 26.271 46.373 30.024 1.00 33.75 ? 429 GLN A OE1 1 ATOM 3419 N NE2 . GLN A 1 429 ? 24.196 45.678 30.551 1.00 31.50 ? 429 GLN A NE2 1 ATOM 3420 N N . ASN A 1 430 ? 20.720 48.998 29.104 1.00 33.79 ? 430 ASN A N 1 ATOM 3421 C CA . ASN A 1 430 ? 20.068 49.779 30.143 1.00 35.64 ? 430 ASN A CA 1 ATOM 3422 C C . ASN A 1 430 ? 20.438 49.143 31.480 1.00 37.58 ? 430 ASN A C 1 ATOM 3423 O O . ASN A 1 430 ? 21.175 48.153 31.520 1.00 36.95 ? 430 ASN A O 1 ATOM 3424 C CB . ASN A 1 430 ? 18.545 49.801 29.954 1.00 33.12 ? 430 ASN A CB 1 ATOM 3425 C CG . ASN A 1 430 ? 17.919 48.424 30.035 1.00 33.97 ? 430 ASN A CG 1 ATOM 3426 O OD1 . ASN A 1 430 ? 18.586 47.436 30.340 1.00 35.83 ? 430 ASN A OD1 1 ATOM 3427 N ND2 . ASN A 1 430 ? 16.623 48.353 29.767 1.00 32.38 ? 430 ASN A ND2 1 ATOM 3428 N N . GLN A 1 431 ? 19.930 49.705 32.568 1.00 40.09 ? 431 GLN A N 1 ATOM 3429 C CA . GLN A 1 431 ? 20.245 49.190 33.890 1.00 43.15 ? 431 GLN A CA 1 ATOM 3430 C C . GLN A 1 431 ? 19.840 47.721 34.045 1.00 43.32 ? 431 GLN A C 1 ATOM 3431 O O . GLN A 1 431 ? 20.553 46.948 34.678 1.00 44.50 ? 431 GLN A O 1 ATOM 3432 C CB . GLN A 1 431 ? 19.565 50.051 34.961 1.00 46.14 ? 431 GLN A CB 1 ATOM 3433 C CG . GLN A 1 431 ? 20.346 50.160 36.269 1.00 50.90 ? 431 GLN A CG 1 ATOM 3434 C CD . GLN A 1 431 ? 21.742 50.748 36.073 1.00 53.87 ? 431 GLN A CD 1 ATOM 3435 O OE1 . GLN A 1 431 ? 21.902 51.831 35.502 1.00 54.88 ? 431 GLN A OE1 1 ATOM 3436 N NE2 . GLN A 1 431 ? 22.758 50.035 36.555 1.00 54.45 ? 431 GLN A NE2 1 ATOM 3437 N N . LEU A 1 432 ? 18.712 47.333 33.458 1.00 43.18 ? 432 LEU A N 1 ATOM 3438 C CA . LEU A 1 432 ? 18.243 45.953 33.563 1.00 43.26 ? 432 LEU A CA 1 ATOM 3439 C C . LEU A 1 432 ? 19.019 44.975 32.691 1.00 43.12 ? 432 LEU A C 1 ATOM 3440 O O . LEU A 1 432 ? 18.684 43.794 32.630 1.00 42.91 ? 432 LEU A O 1 ATOM 3441 C CB . LEU A 1 432 ? 16.751 45.859 33.221 1.00 45.26 ? 432 LEU A CB 1 ATOM 3442 C CG . LEU A 1 432 ? 15.780 46.669 34.091 1.00 47.31 ? 432 LEU A CG 1 ATOM 3443 C CD1 . LEU A 1 432 ? 16.091 46.435 35.566 1.00 46.49 ? 432 LEU A CD1 1 ATOM 3444 C CD2 . LEU A 1 432 ? 15.903 48.152 33.762 1.00 49.22 ? 432 LEU A CD2 1 ATOM 3445 N N . GLY A 1 433 ? 20.049 45.464 32.011 1.00 42.94 ? 433 GLY A N 1 ATOM 3446 C CA . GLY A 1 433 ? 20.847 44.590 31.171 1.00 43.02 ? 433 GLY A CA 1 ATOM 3447 C C . GLY A 1 433 ? 20.354 44.385 29.749 1.00 43.43 ? 433 GLY A C 1 ATOM 3448 O O . GLY A 1 433 ? 20.927 43.588 29.006 1.00 44.00 ? 433 GLY A O 1 ATOM 3449 N N . ARG A 1 434 ? 19.292 45.085 29.367 1.00 43.88 ? 434 ARG A N 1 ATOM 3450 C CA . ARG A 1 434 ? 18.750 44.976 28.013 1.00 44.12 ? 434 ARG A CA 1 ATOM 3451 C C . ARG A 1 434 ? 19.631 45.760 27.042 1.00 41.30 ? 434 ARG A C 1 ATOM 3452 O O . ARG A 1 434 ? 20.047 46.882 27.336 1.00 40.38 ? 434 ARG A O 1 ATOM 3453 C CB . ARG A 1 434 ? 17.317 45.509 27.980 1.00 48.99 ? 434 ARG A CB 1 ATOM 3454 C CG . ARG A 1 434 ? 16.299 44.517 28.504 1.00 56.50 ? 434 ARG A CG 1 ATOM 3455 C CD . ARG A 1 434 ? 16.012 43.475 27.438 1.00 63.96 ? 434 ARG A CD 1 ATOM 3456 N NE . ARG A 1 434 ? 15.637 42.174 27.987 1.00 68.18 ? 434 ARG A NE 1 ATOM 3457 C CZ . ARG A 1 434 ? 15.414 41.098 27.238 1.00 70.86 ? 434 ARG A CZ 1 ATOM 3458 N NH1 . ARG A 1 434 ? 15.527 41.182 25.915 1.00 70.76 ? 434 ARG A NH1 1 ATOM 3459 N NH2 . ARG A 1 434 ? 15.097 39.938 27.805 1.00 71.50 ? 434 ARG A NH2 1 ATOM 3460 N N . TYR A 1 435 ? 19.914 45.170 25.885 1.00 37.31 ? 435 TYR A N 1 ATOM 3461 C CA . TYR A 1 435 ? 20.770 45.819 24.898 1.00 34.32 ? 435 TYR A CA 1 ATOM 3462 C C . TYR A 1 435 ? 20.017 46.558 23.808 1.00 33.09 ? 435 TYR A C 1 ATOM 3463 O O . TYR A 1 435 ? 18.881 46.220 23.474 1.00 32.59 ? 435 TYR A O 1 ATOM 3464 C CB . TYR A 1 435 ? 21.680 44.791 24.229 1.00 32.06 ? 435 TYR A CB 1 ATOM 3465 C CG . TYR A 1 435 ? 22.574 44.042 25.179 1.00 31.40 ? 435 TYR A CG 1 ATOM 3466 C CD1 . TYR A 1 435 ? 23.648 44.672 25.804 1.00 30.65 ? 435 TYR A CD1 1 ATOM 3467 C CD2 . TYR A 1 435 ? 22.347 42.695 25.451 1.00 30.58 ? 435 TYR A CD2 1 ATOM 3468 C CE1 . TYR A 1 435 ? 24.477 43.977 26.676 1.00 30.40 ? 435 TYR A CE1 1 ATOM 3469 C CE2 . TYR A 1 435 ? 23.165 41.993 26.318 1.00 29.98 ? 435 TYR A CE2 1 ATOM 3470 C CZ . TYR A 1 435 ? 24.226 42.634 26.928 1.00 30.85 ? 435 TYR A CZ 1 ATOM 3471 O OH . TYR A 1 435 ? 25.031 41.929 27.790 1.00 31.64 ? 435 TYR A OH 1 ATOM 3472 N N . SER A 1 436 ? 20.665 47.574 23.257 1.00 31.34 ? 436 SER A N 1 ATOM 3473 C CA . SER A 1 436 ? 20.091 48.345 22.167 1.00 30.46 ? 436 SER A CA 1 ATOM 3474 C C . SER A 1 436 ? 21.233 48.653 21.197 1.00 29.06 ? 436 SER A C 1 ATOM 3475 O O . SER A 1 436 ? 22.397 48.758 21.603 1.00 28.28 ? 436 SER A O 1 ATOM 3476 C CB . SER A 1 436 ? 19.430 49.632 22.685 1.00 29.60 ? 436 SER A CB 1 ATOM 3477 O OG . SER A 1 436 ? 20.384 50.577 23.130 1.00 33.61 ? 436 SER A OG 1 ATOM 3478 N N . VAL A 1 437 ? 20.901 48.779 19.917 1.00 26.85 ? 437 VAL A N 1 ATOM 3479 C CA . VAL A 1 437 ? 21.895 49.040 18.888 1.00 25.13 ? 437 VAL A CA 1 ATOM 3480 C C . VAL A 1 437 ? 21.665 50.356 18.173 1.00 25.19 ? 437 VAL A C 1 ATOM 3481 O O . VAL A 1 437 ? 20.549 50.667 17.748 1.00 24.49 ? 437 VAL A O 1 ATOM 3482 C CB . VAL A 1 437 ? 21.897 47.909 17.841 1.00 25.82 ? 437 VAL A CB 1 ATOM 3483 C CG1 . VAL A 1 437 ? 22.960 48.173 16.779 1.00 23.14 ? 437 VAL A CG1 1 ATOM 3484 C CG2 . VAL A 1 437 ? 22.134 46.572 18.537 1.00 24.78 ? 437 VAL A CG2 1 ATOM 3485 N N . LEU A 1 438 ? 22.737 51.124 18.034 1.00 23.99 ? 438 LEU A N 1 ATOM 3486 C CA . LEU A 1 438 ? 22.671 52.406 17.361 1.00 24.12 ? 438 LEU A CA 1 ATOM 3487 C C . LEU A 1 438 ? 23.453 52.345 16.054 1.00 25.85 ? 438 LEU A C 1 ATOM 3488 O O . LEU A 1 438 ? 24.568 51.813 16.004 1.00 25.20 ? 438 LEU A O 1 ATOM 3489 C CB . LEU A 1 438 ? 23.249 53.499 18.259 1.00 23.91 ? 438 LEU A CB 1 ATOM 3490 C CG . LEU A 1 438 ? 23.343 54.887 17.623 1.00 25.22 ? 438 LEU A CG 1 ATOM 3491 C CD1 . LEU A 1 438 ? 21.948 55.455 17.427 1.00 25.15 ? 438 LEU A CD1 1 ATOM 3492 C CD2 . LEU A 1 438 ? 24.176 55.801 18.504 1.00 23.30 ? 438 LEU A CD2 1 ATOM 3493 N N . MET A 1 439 ? 22.855 52.879 14.995 1.00 26.73 ? 439 MET A N 1 ATOM 3494 C CA . MET A 1 439 ? 23.491 52.912 13.685 1.00 26.53 ? 439 MET A CA 1 ATOM 3495 C C . MET A 1 439 ? 23.719 54.374 13.333 1.00 26.99 ? 439 MET A C 1 ATOM 3496 O O . MET A 1 439 ? 22.797 55.185 13.398 1.00 28.40 ? 439 MET A O 1 ATOM 3497 C CB . MET A 1 439 ? 22.597 52.257 12.634 1.00 25.80 ? 439 MET A CB 1 ATOM 3498 C CG . MET A 1 439 ? 23.208 52.237 11.245 1.00 25.19 ? 439 MET A CG 1 ATOM 3499 S SD . MET A 1 439 ? 22.097 51.526 10.025 1.00 28.96 ? 439 MET A SD 1 ATOM 3500 C CE . MET A 1 439 ? 22.802 52.180 8.493 1.00 28.47 ? 439 MET A CE 1 ATOM 3501 N N . CYS A 1 440 ? 24.944 54.707 12.953 1.00 27.12 ? 440 CYS A N 1 ATOM 3502 C CA . CYS A 1 440 ? 25.280 56.081 12.630 1.00 27.95 ? 440 CYS A CA 1 ATOM 3503 C C . CYS A 1 440 ? 25.909 56.292 11.267 1.00 27.91 ? 440 CYS A C 1 ATOM 3504 O O . CYS A 1 440 ? 26.583 55.419 10.733 1.00 29.52 ? 440 CYS A O 1 ATOM 3505 C CB . CYS A 1 440 ? 26.266 56.638 13.658 1.00 31.25 ? 440 CYS A CB 1 ATOM 3506 S SG . CYS A 1 440 ? 25.667 56.870 15.358 1.00 36.67 ? 440 CYS A SG 1 ATOM 3507 N N . SER A 1 441 ? 25.691 57.482 10.723 1.00 26.75 ? 441 SER A N 1 ATOM 3508 C CA . SER A 1 441 ? 26.292 57.890 9.466 1.00 26.49 ? 441 SER A CA 1 ATOM 3509 C C . SER A 1 441 ? 26.951 59.210 9.829 1.00 26.43 ? 441 SER A C 1 ATOM 3510 O O . SER A 1 441 ? 26.328 60.272 9.776 1.00 26.16 ? 441 SER A O 1 ATOM 3511 C CB . SER A 1 441 ? 25.239 58.098 8.386 1.00 27.35 ? 441 SER A CB 1 ATOM 3512 O OG . SER A 1 441 ? 24.677 56.857 8.009 1.00 31.66 ? 441 SER A OG 1 ATOM 3513 N N . ASP A 1 442 ? 28.207 59.116 10.255 1.00 26.20 ? 442 ASP A N 1 ATOM 3514 C CA . ASP A 1 442 ? 28.992 60.273 10.656 1.00 25.24 ? 442 ASP A CA 1 ATOM 3515 C C . ASP A 1 442 ? 29.553 60.934 9.407 1.00 24.83 ? 442 ASP A C 1 ATOM 3516 O O . ASP A 1 442 ? 30.429 60.388 8.734 1.00 23.87 ? 442 ASP A O 1 ATOM 3517 C CB . ASP A 1 442 ? 30.127 59.829 11.587 1.00 26.81 ? 442 ASP A CB 1 ATOM 3518 C CG . ASP A 1 442 ? 31.008 60.979 12.037 1.00 28.70 ? 442 ASP A CG 1 ATOM 3519 O OD1 . ASP A 1 442 ? 30.732 62.140 11.656 1.00 28.65 ? 442 ASP A OD1 1 ATOM 3520 O OD2 . ASP A 1 442 ? 31.982 60.716 12.776 1.00 28.96 ? 442 ASP A OD2 1 ATOM 3521 N N . LEU A 1 443 ? 29.028 62.111 9.098 1.00 24.26 ? 443 LEU A N 1 ATOM 3522 C CA . LEU A 1 443 ? 29.449 62.863 7.929 1.00 24.31 ? 443 LEU A CA 1 ATOM 3523 C C . LEU A 1 443 ? 30.269 64.095 8.304 1.00 24.35 ? 443 LEU A C 1 ATOM 3524 O O . LEU A 1 443 ? 30.696 64.849 7.433 1.00 23.98 ? 443 LEU A O 1 ATOM 3525 C CB . LEU A 1 443 ? 28.211 63.275 7.132 1.00 23.04 ? 443 LEU A CB 1 ATOM 3526 C CG . LEU A 1 443 ? 27.586 62.255 6.170 1.00 23.50 ? 443 LEU A CG 1 ATOM 3527 C CD1 . LEU A 1 443 ? 27.801 60.837 6.653 1.00 21.66 ? 443 LEU A CD1 1 ATOM 3528 C CD2 . LEU A 1 443 ? 26.108 62.571 6.018 1.00 20.16 ? 443 LEU A CD2 1 ATOM 3529 N N . SER A 1 444 ? 30.492 64.278 9.604 1.00 25.10 ? 444 SER A N 1 ATOM 3530 C CA . SER A 1 444 ? 31.237 65.423 10.128 1.00 26.66 ? 444 SER A CA 1 ATOM 3531 C C . SER A 1 444 ? 32.562 65.696 9.419 1.00 27.60 ? 444 SER A C 1 ATOM 3532 O O . SER A 1 444 ? 32.952 66.855 9.240 1.00 27.63 ? 444 SER A O 1 ATOM 3533 C CB . SER A 1 444 ? 31.496 65.237 11.622 1.00 25.91 ? 444 SER A CB 1 ATOM 3534 O OG . SER A 1 444 ? 32.368 64.149 11.867 1.00 29.92 ? 444 SER A OG 1 ATOM 3535 N N . ARG A 1 445 ? 33.248 64.632 9.012 1.00 27.51 ? 445 ARG A N 1 ATOM 3536 C CA . ARG A 1 445 ? 34.528 64.766 8.326 1.00 27.71 ? 445 ARG A CA 1 ATOM 3537 C C . ARG A 1 445 ? 34.478 64.256 6.890 1.00 27.52 ? 445 ARG A C 1 ATOM 3538 O O . ARG A 1 445 ? 35.506 63.929 6.301 1.00 27.07 ? 445 ARG A O 1 ATOM 3539 C CB . ARG A 1 445 ? 35.603 64.006 9.099 1.00 28.38 ? 445 ARG A CB 1 ATOM 3540 C CG . ARG A 1 445 ? 35.841 64.532 10.506 1.00 29.24 ? 445 ARG A CG 1 ATOM 3541 C CD . ARG A 1 445 ? 37.010 63.813 11.136 1.00 31.65 ? 445 ARG A CD 1 ATOM 3542 N NE . ARG A 1 445 ? 36.601 62.722 12.013 1.00 34.54 ? 445 ARG A NE 1 ATOM 3543 C CZ . ARG A 1 445 ? 37.359 61.659 12.272 1.00 36.57 ? 445 ARG A CZ 1 ATOM 3544 N NH1 . ARG A 1 445 ? 38.557 61.549 11.707 1.00 35.84 ? 445 ARG A NH1 1 ATOM 3545 N NH2 . ARG A 1 445 ? 36.935 60.719 13.113 1.00 36.39 ? 445 ARG A NH2 1 ATOM 3546 N N . SER A 1 446 ? 33.277 64.196 6.328 1.00 27.22 ? 446 SER A N 1 ATOM 3547 C CA . SER A 1 446 ? 33.102 63.706 4.970 1.00 28.03 ? 446 SER A CA 1 ATOM 3548 C C . SER A 1 446 ? 33.747 64.622 3.936 1.00 28.52 ? 446 SER A C 1 ATOM 3549 O O . SER A 1 446 ? 34.022 64.203 2.813 1.00 29.53 ? 446 SER A O 1 ATOM 3550 C CB . SER A 1 446 ? 31.615 63.552 4.657 1.00 28.14 ? 446 SER A CB 1 ATOM 3551 O OG . SER A 1 446 ? 30.948 64.796 4.771 1.00 26.60 ? 446 SER A OG 1 ATOM 3552 N N . THR A 1 447 ? 33.993 65.872 4.307 1.00 27.14 ? 447 THR A N 1 ATOM 3553 C CA . THR A 1 447 ? 34.596 66.809 3.374 1.00 25.27 ? 447 THR A CA 1 ATOM 3554 C C . THR A 1 447 ? 35.256 67.954 4.114 1.00 26.11 ? 447 THR A C 1 ATOM 3555 O O . THR A 1 447 ? 34.866 68.282 5.231 1.00 26.76 ? 447 THR A O 1 ATOM 3556 C CB . THR A 1 447 ? 33.537 67.395 2.415 1.00 24.16 ? 447 THR A CB 1 ATOM 3557 O OG1 . THR A 1 447 ? 34.167 68.274 1.478 1.00 22.93 ? 447 THR A OG1 1 ATOM 3558 C CG2 . THR A 1 447 ? 32.487 68.168 3.192 1.00 21.44 ? 447 THR A CG2 1 ATOM 3559 N N . VAL A 1 448 ? 36.265 68.554 3.497 1.00 26.02 ? 448 VAL A N 1 ATOM 3560 C CA . VAL A 1 448 ? 36.942 69.684 4.111 1.00 27.00 ? 448 VAL A CA 1 ATOM 3561 C C . VAL A 1 448 ? 36.415 70.950 3.460 1.00 29.06 ? 448 VAL A C 1 ATOM 3562 O O . VAL A 1 448 ? 36.851 72.054 3.784 1.00 30.49 ? 448 VAL A O 1 ATOM 3563 C CB . VAL A 1 448 ? 38.472 69.625 3.917 1.00 25.55 ? 448 VAL A CB 1 ATOM 3564 C CG1 . VAL A 1 448 ? 39.029 68.385 4.593 1.00 24.66 ? 448 VAL A CG1 1 ATOM 3565 C CG2 . VAL A 1 448 ? 38.815 69.634 2.434 1.00 24.25 ? 448 VAL A CG2 1 ATOM 3566 N N . ARG A 1 449 ? 35.473 70.780 2.536 1.00 30.07 ? 449 ARG A N 1 ATOM 3567 C CA . ARG A 1 449 ? 34.871 71.903 1.827 1.00 31.18 ? 449 ARG A CA 1 ATOM 3568 C C . ARG A 1 449 ? 33.948 72.712 2.731 1.00 32.65 ? 449 ARG A C 1 ATOM 3569 O O . ARG A 1 449 ? 33.443 72.209 3.734 1.00 31.94 ? 449 ARG A O 1 ATOM 3570 C CB . ARG A 1 449 ? 34.065 71.407 0.626 1.00 31.69 ? 449 ARG A CB 1 ATOM 3571 C CG . ARG A 1 449 ? 34.887 70.821 -0.492 1.00 30.97 ? 449 ARG A CG 1 ATOM 3572 C CD . ARG A 1 449 ? 34.315 71.277 -1.814 1.00 33.10 ? 449 ARG A CD 1 ATOM 3573 N NE . ARG A 1 449 ? 33.238 70.428 -2.309 1.00 35.70 ? 449 ARG A NE 1 ATOM 3574 C CZ . ARG A 1 449 ? 32.223 70.864 -3.053 1.00 36.57 ? 449 ARG A CZ 1 ATOM 3575 N NH1 . ARG A 1 449 ? 32.131 72.145 -3.378 1.00 34.92 ? 449 ARG A NH1 1 ATOM 3576 N NH2 . ARG A 1 449 ? 31.313 70.009 -3.500 1.00 36.78 ? 449 ARG A NH2 1 ATOM 3577 N N . SER A 1 450 ? 33.724 73.968 2.364 1.00 34.04 ? 450 SER A N 1 ATOM 3578 C CA . SER A 1 450 ? 32.843 74.836 3.135 1.00 36.90 ? 450 SER A CA 1 ATOM 3579 C C . SER A 1 450 ? 31.475 74.902 2.469 1.00 37.03 ? 450 SER A C 1 ATOM 3580 O O . SER A 1 450 ? 31.331 74.578 1.287 1.00 38.33 ? 450 SER A O 1 ATOM 3581 C CB . SER A 1 450 ? 33.427 76.245 3.220 1.00 38.18 ? 450 SER A CB 1 ATOM 3582 O OG . SER A 1 450 ? 34.726 76.218 3.780 1.00 44.33 ? 450 SER A OG 1 ATOM 3583 N N . ASN A 1 451 ? 30.476 75.328 3.230 1.00 36.94 ? 451 ASN A N 1 ATOM 3584 C CA . ASN A 1 451 ? 29.116 75.456 2.718 1.00 37.13 ? 451 ASN A CA 1 ATOM 3585 C C . ASN A 1 451 ? 28.523 74.120 2.298 1.00 35.49 ? 451 ASN A C 1 ATOM 3586 O O . ASN A 1 451 ? 27.747 74.050 1.342 1.00 36.16 ? 451 ASN A O 1 ATOM 3587 C CB . ASN A 1 451 ? 29.080 76.422 1.533 1.00 40.38 ? 451 ASN A CB 1 ATOM 3588 C CG . ASN A 1 451 ? 29.746 77.740 1.847 1.00 44.00 ? 451 ASN A CG 1 ATOM 3589 O OD1 . ASN A 1 451 ? 29.383 78.415 2.811 1.00 46.58 ? 451 ASN A OD1 1 ATOM 3590 N ND2 . ASN A 1 451 ? 30.734 78.115 1.038 1.00 46.54 ? 451 ASN A ND2 1 ATOM 3591 N N . ILE A 1 452 ? 28.904 73.062 3.010 1.00 31.73 ? 452 ILE A N 1 ATOM 3592 C CA . ILE A 1 452 ? 28.388 71.727 2.751 1.00 28.31 ? 452 ILE A CA 1 ATOM 3593 C C . ILE A 1 452 ? 27.693 71.257 4.026 1.00 28.40 ? 452 ILE A C 1 ATOM 3594 O O . ILE A 1 452 ? 28.288 71.272 5.104 1.00 28.45 ? 452 ILE A O 1 ATOM 3595 C CB . ILE A 1 452 ? 29.518 70.735 2.412 1.00 27.09 ? 452 ILE A CB 1 ATOM 3596 C CG1 . ILE A 1 452 ? 30.270 71.204 1.168 1.00 25.62 ? 452 ILE A CG1 1 ATOM 3597 C CG2 . ILE A 1 452 ? 28.937 69.350 2.172 1.00 24.41 ? 452 ILE A CG2 1 ATOM 3598 C CD1 . ILE A 1 452 ? 29.409 71.267 -0.077 1.00 23.32 ? 452 ILE A CD1 1 ATOM 3599 N N . ASP A 1 453 ? 26.430 70.865 3.913 1.00 27.86 ? 453 ASP A N 1 ATOM 3600 C CA . ASP A 1 453 ? 25.700 70.383 5.077 1.00 26.51 ? 453 ASP A CA 1 ATOM 3601 C C . ASP A 1 453 ? 26.280 69.025 5.445 1.00 26.43 ? 453 ASP A C 1 ATOM 3602 O O . ASP A 1 453 ? 26.033 68.029 4.763 1.00 26.24 ? 453 ASP A O 1 ATOM 3603 C CB . ASP A 1 453 ? 24.219 70.233 4.761 1.00 27.15 ? 453 ASP A CB 1 ATOM 3604 C CG . ASP A 1 453 ? 23.417 69.743 5.956 1.00 31.40 ? 453 ASP A CG 1 ATOM 3605 O OD1 . ASP A 1 453 ? 24.033 69.304 6.956 1.00 30.04 ? 453 ASP A OD1 1 ATOM 3606 O OD2 . ASP A 1 453 ? 22.165 69.787 5.889 1.00 33.55 ? 453 ASP A OD2 1 ATOM 3607 N N . THR A 1 454 ? 27.051 68.985 6.522 1.00 25.00 ? 454 THR A N 1 ATOM 3608 C CA . THR A 1 454 ? 27.668 67.741 6.941 1.00 25.05 ? 454 THR A CA 1 ATOM 3609 C C . THR A 1 454 ? 27.040 67.142 8.197 1.00 26.52 ? 454 THR A C 1 ATOM 3610 O O . THR A 1 454 ? 27.695 66.427 8.955 1.00 27.15 ? 454 THR A O 1 ATOM 3611 C CB . THR A 1 454 ? 29.179 67.933 7.150 1.00 25.09 ? 454 THR A CB 1 ATOM 3612 O OG1 . THR A 1 454 ? 29.409 69.008 8.070 1.00 24.11 ? 454 THR A OG1 1 ATOM 3613 C CG2 . THR A 1 454 ? 29.851 68.257 5.819 1.00 23.74 ? 454 THR A CG2 1 ATOM 3614 N N . THR A 1 455 ? 25.761 67.433 8.403 1.00 25.89 ? 455 THR A N 1 ATOM 3615 C CA . THR A 1 455 ? 25.022 66.906 9.543 1.00 24.52 ? 455 THR A CA 1 ATOM 3616 C C . THR A 1 455 ? 25.041 65.381 9.485 1.00 24.93 ? 455 THR A C 1 ATOM 3617 O O . THR A 1 455 ? 24.908 64.796 8.409 1.00 24.64 ? 455 THR A O 1 ATOM 3618 C CB . THR A 1 455 ? 23.556 67.354 9.491 1.00 25.54 ? 455 THR A CB 1 ATOM 3619 O OG1 . THR A 1 455 ? 23.501 68.782 9.499 1.00 27.21 ? 455 THR A OG1 1 ATOM 3620 C CG2 . THR A 1 455 ? 22.776 66.798 10.672 1.00 22.15 ? 455 THR A CG2 1 ATOM 3621 N N . SER A 1 456 ? 25.192 64.736 10.635 1.00 23.72 ? 456 SER A N 1 ATOM 3622 C CA . SER A 1 456 ? 25.205 63.281 10.674 1.00 22.62 ? 456 SER A CA 1 ATOM 3623 C C . SER A 1 456 ? 23.800 62.744 10.913 1.00 22.18 ? 456 SER A C 1 ATOM 3624 O O . SER A 1 456 ? 22.934 63.456 11.420 1.00 20.94 ? 456 SER A O 1 ATOM 3625 C CB . SER A 1 456 ? 26.145 62.788 11.772 1.00 23.03 ? 456 SER A CB 1 ATOM 3626 O OG . SER A 1 456 ? 27.490 63.089 11.451 1.00 23.88 ? 456 SER A OG 1 ATOM 3627 N N . TYR A 1 457 ? 23.584 61.484 10.546 1.00 21.67 ? 457 TYR A N 1 ATOM 3628 C CA . TYR A 1 457 ? 22.281 60.844 10.709 1.00 21.34 ? 457 TYR A CA 1 ATOM 3629 C C . TYR A 1 457 ? 22.435 59.567 11.520 1.00 21.31 ? 457 TYR A C 1 ATOM 3630 O O . TYR A 1 457 ? 23.469 58.907 11.458 1.00 22.65 ? 457 TYR A O 1 ATOM 3631 C CB . TYR A 1 457 ? 21.685 60.522 9.332 1.00 21.75 ? 457 TYR A CB 1 ATOM 3632 C CG . TYR A 1 457 ? 21.629 61.726 8.429 1.00 21.86 ? 457 TYR A CG 1 ATOM 3633 C CD1 . TYR A 1 457 ? 20.744 62.772 8.690 1.00 22.00 ? 457 TYR A CD1 1 ATOM 3634 C CD2 . TYR A 1 457 ? 22.522 61.868 7.365 1.00 21.51 ? 457 TYR A CD2 1 ATOM 3635 C CE1 . TYR A 1 457 ? 20.759 63.936 7.920 1.00 24.79 ? 457 TYR A CE1 1 ATOM 3636 C CE2 . TYR A 1 457 ? 22.547 63.028 6.587 1.00 22.92 ? 457 TYR A CE2 1 ATOM 3637 C CZ . TYR A 1 457 ? 21.666 64.059 6.874 1.00 25.53 ? 457 TYR A CZ 1 ATOM 3638 O OH . TYR A 1 457 ? 21.712 65.230 6.150 1.00 27.96 ? 457 TYR A OH 1 ATOM 3639 N N . GLY A 1 458 ? 21.405 59.221 12.282 1.00 20.68 ? 458 GLY A N 1 ATOM 3640 C CA . GLY A 1 458 ? 21.469 58.017 13.084 1.00 21.75 ? 458 GLY A CA 1 ATOM 3641 C C . GLY A 1 458 ? 20.096 57.467 13.406 1.00 23.71 ? 458 GLY A C 1 ATOM 3642 O O . GLY A 1 458 ? 19.088 58.155 13.236 1.00 24.03 ? 458 GLY A O 1 ATOM 3643 N N . ALA A 1 459 ? 20.056 56.222 13.871 1.00 24.32 ? 459 ALA A N 1 ATOM 3644 C CA . ALA A 1 459 ? 18.797 55.576 14.228 1.00 24.92 ? 459 ALA A CA 1 ATOM 3645 C C . ALA A 1 459 ? 19.086 54.295 14.989 1.00 25.55 ? 459 ALA A C 1 ATOM 3646 O O . ALA A 1 459 ? 20.174 53.731 14.869 1.00 25.67 ? 459 ALA A O 1 ATOM 3647 C CB . ALA A 1 459 ? 17.996 55.266 12.977 1.00 22.73 ? 459 ALA A CB 1 ATOM 3648 N N . PHE A 1 460 ? 18.121 53.846 15.785 1.00 26.50 ? 460 PHE A N 1 ATOM 3649 C CA . PHE A 1 460 ? 18.283 52.614 16.544 1.00 28.99 ? 460 PHE A CA 1 ATOM 3650 C C . PHE A 1 460 ? 17.844 51.428 15.700 1.00 29.92 ? 460 PHE A C 1 ATOM 3651 O O . PHE A 1 460 ? 16.865 51.513 14.958 1.00 31.89 ? 460 PHE A O 1 ATOM 3652 C CB . PHE A 1 460 ? 17.473 52.662 17.841 1.00 28.47 ? 460 PHE A CB 1 ATOM 3653 C CG . PHE A 1 460 ? 18.041 53.597 18.864 1.00 29.88 ? 460 PHE A CG 1 ATOM 3654 C CD1 . PHE A 1 460 ? 17.422 54.811 19.139 1.00 30.39 ? 460 PHE A CD1 1 ATOM 3655 C CD2 . PHE A 1 460 ? 19.229 53.284 19.519 1.00 30.08 ? 460 PHE A CD2 1 ATOM 3656 C CE1 . PHE A 1 460 ? 17.982 55.710 20.051 1.00 31.54 ? 460 PHE A CE1 1 ATOM 3657 C CE2 . PHE A 1 460 ? 19.799 54.172 20.431 1.00 31.63 ? 460 PHE A CE2 1 ATOM 3658 C CZ . PHE A 1 460 ? 19.173 55.390 20.697 1.00 31.43 ? 460 PHE A CZ 1 ATOM 3659 N N . VAL A 1 461 ? 18.584 50.329 15.808 1.00 30.13 ? 461 VAL A N 1 ATOM 3660 C CA . VAL A 1 461 ? 18.279 49.125 15.049 1.00 29.19 ? 461 VAL A CA 1 ATOM 3661 C C . VAL A 1 461 ? 17.580 48.130 15.949 1.00 30.47 ? 461 VAL A C 1 ATOM 3662 O O . VAL A 1 461 ? 18.067 47.801 17.029 1.00 30.85 ? 461 VAL A O 1 ATOM 3663 C CB . VAL A 1 461 ? 19.552 48.469 14.505 1.00 27.88 ? 461 VAL A CB 1 ATOM 3664 C CG1 . VAL A 1 461 ? 19.185 47.333 13.568 1.00 27.63 ? 461 VAL A CG1 1 ATOM 3665 C CG2 . VAL A 1 461 ? 20.400 49.506 13.804 1.00 27.34 ? 461 VAL A CG2 1 ATOM 3666 N N . ASP A 1 462 ? 16.436 47.643 15.499 1.00 31.67 ? 462 ASP A N 1 ATOM 3667 C CA . ASP A 1 462 ? 15.678 46.700 16.291 1.00 33.51 ? 462 ASP A CA 1 ATOM 3668 C C . ASP A 1 462 ? 16.132 45.250 16.116 1.00 33.49 ? 462 ASP A C 1 ATOM 3669 O O . ASP A 1 462 ? 15.506 44.472 15.392 1.00 32.57 ? 462 ASP A O 1 ATOM 3670 C CB . ASP A 1 462 ? 14.196 46.846 15.958 1.00 36.67 ? 462 ASP A CB 1 ATOM 3671 C CG . ASP A 1 462 ? 13.325 45.945 16.795 1.00 40.66 ? 462 ASP A CG 1 ATOM 3672 O OD1 . ASP A 1 462 ? 13.662 45.735 17.983 1.00 42.11 ? 462 ASP A OD1 1 ATOM 3673 O OD2 . ASP A 1 462 ? 12.298 45.460 16.269 1.00 44.98 ? 462 ASP A OD2 1 ATOM 3674 N N . ILE A 1 463 ? 17.232 44.901 16.784 1.00 33.05 ? 463 ILE A N 1 ATOM 3675 C CA . ILE A 1 463 ? 17.780 43.547 16.744 1.00 32.36 ? 463 ILE A CA 1 ATOM 3676 C C . ILE A 1 463 ? 18.352 43.184 18.110 1.00 33.22 ? 463 ILE A C 1 ATOM 3677 O O . ILE A 1 463 ? 18.699 44.066 18.898 1.00 33.64 ? 463 ILE A O 1 ATOM 3678 C CB . ILE A 1 463 ? 18.916 43.407 15.709 1.00 32.19 ? 463 ILE A CB 1 ATOM 3679 C CG1 . ILE A 1 463 ? 20.082 44.317 16.092 1.00 30.29 ? 463 ILE A CG1 1 ATOM 3680 C CG2 . ILE A 1 463 ? 18.401 43.732 14.318 1.00 31.29 ? 463 ILE A CG2 1 ATOM 3681 C CD1 . ILE A 1 463 ? 21.298 44.131 15.219 1.00 31.19 ? 463 ILE A CD1 1 ATOM 3682 N N . ASP A 1 464 ? 18.449 41.885 18.388 1.00 33.54 ? 464 ASP A N 1 ATOM 3683 C CA . ASP A 1 464 ? 18.992 41.408 19.659 1.00 33.41 ? 464 ASP A CA 1 ATOM 3684 C C . ASP A 1 464 ? 20.437 40.946 19.450 1.00 32.86 ? 464 ASP A C 1 ATOM 3685 O O . ASP A 1 464 ? 20.680 39.845 18.951 1.00 32.80 ? 464 ASP A O 1 ATOM 3686 C CB . ASP A 1 464 ? 18.126 40.265 20.200 1.00 34.98 ? 464 ASP A CB 1 ATOM 3687 C CG . ASP A 1 464 ? 18.695 39.636 21.461 1.00 38.06 ? 464 ASP A CG 1 ATOM 3688 O OD1 . ASP A 1 464 ? 19.464 40.316 22.181 1.00 37.51 ? 464 ASP A OD1 1 ATOM 3689 O OD2 . ASP A 1 464 ? 18.360 38.459 21.735 1.00 39.88 ? 464 ASP A OD2 1 ATOM 3690 N N . PRO A 1 465 ? 21.411 41.792 19.838 1.00 31.81 ? 465 PRO A N 1 ATOM 3691 C CA . PRO A 1 465 ? 22.852 41.538 19.714 1.00 31.51 ? 465 PRO A CA 1 ATOM 3692 C C . PRO A 1 465 ? 23.286 40.203 20.300 1.00 32.31 ? 465 PRO A C 1 ATOM 3693 O O . PRO A 1 465 ? 24.339 39.675 19.950 1.00 32.48 ? 465 PRO A O 1 ATOM 3694 C CB . PRO A 1 465 ? 23.480 42.709 20.467 1.00 30.53 ? 465 PRO A CB 1 ATOM 3695 C CG . PRO A 1 465 ? 22.463 43.772 20.370 1.00 31.22 ? 465 PRO A CG 1 ATOM 3696 C CD . PRO A 1 465 ? 21.177 43.032 20.593 1.00 30.33 ? 465 PRO A CD 1 ATOM 3697 N N . ARG A 1 466 ? 22.480 39.665 21.203 1.00 33.44 ? 466 ARG A N 1 ATOM 3698 C CA . ARG A 1 466 ? 22.814 38.399 21.832 1.00 35.30 ? 466 ARG A CA 1 ATOM 3699 C C . ARG A 1 466 ? 22.677 37.211 20.887 1.00 36.67 ? 466 ARG A C 1 ATOM 3700 O O . ARG A 1 466 ? 23.526 36.320 20.880 1.00 38.71 ? 466 ARG A O 1 ATOM 3701 C CB . ARG A 1 466 ? 21.928 38.169 23.053 1.00 33.01 ? 466 ARG A CB 1 ATOM 3702 C CG . ARG A 1 466 ? 22.167 39.138 24.184 1.00 34.73 ? 466 ARG A CG 1 ATOM 3703 C CD . ARG A 1 466 ? 21.163 38.903 25.292 1.00 33.57 ? 466 ARG A CD 1 ATOM 3704 N NE . ARG A 1 466 ? 19.798 39.032 24.793 1.00 35.03 ? 466 ARG A NE 1 ATOM 3705 C CZ . ARG A 1 466 ? 18.708 38.741 25.495 1.00 35.87 ? 466 ARG A CZ 1 ATOM 3706 N NH1 . ARG A 1 466 ? 18.820 38.298 26.741 1.00 37.77 ? 466 ARG A NH1 1 ATOM 3707 N NH2 . ARG A 1 466 ? 17.505 38.890 24.953 1.00 34.68 ? 466 ARG A NH2 1 ATOM 3708 N N . SER A 1 467 ? 21.620 37.207 20.082 1.00 36.84 ? 467 SER A N 1 ATOM 3709 C CA . SER A 1 467 ? 21.366 36.095 19.185 1.00 37.57 ? 467 SER A CA 1 ATOM 3710 C C . SER A 1 467 ? 21.626 36.320 17.697 1.00 38.35 ? 467 SER A C 1 ATOM 3711 O O . SER A 1 467 ? 21.592 35.366 16.918 1.00 39.49 ? 467 SER A O 1 ATOM 3712 C CB . SER A 1 467 ? 19.929 35.615 19.380 1.00 38.38 ? 467 SER A CB 1 ATOM 3713 O OG . SER A 1 467 ? 19.009 36.656 19.104 1.00 43.14 ? 467 SER A OG 1 ATOM 3714 N N . GLU A 1 468 ? 21.867 37.561 17.286 1.00 38.60 ? 468 GLU A N 1 ATOM 3715 C CA . GLU A 1 468 ? 22.139 37.824 15.875 1.00 38.67 ? 468 GLU A CA 1 ATOM 3716 C C . GLU A 1 468 ? 23.243 38.843 15.645 1.00 36.96 ? 468 GLU A C 1 ATOM 3717 O O . GLU A 1 468 ? 23.319 39.859 16.335 1.00 37.12 ? 468 GLU A O 1 ATOM 3718 C CB . GLU A 1 468 ? 20.867 38.263 15.141 1.00 40.48 ? 468 GLU A CB 1 ATOM 3719 C CG . GLU A 1 468 ? 20.027 39.291 15.865 1.00 47.48 ? 468 GLU A CG 1 ATOM 3720 C CD . GLU A 1 468 ? 18.757 39.649 15.094 1.00 51.86 ? 468 GLU A CD 1 ATOM 3721 O OE1 . GLU A 1 468 ? 17.795 40.150 15.727 1.00 51.68 ? 468 GLU A OE1 1 ATOM 3722 O OE2 . GLU A 1 468 ? 18.730 39.435 13.856 1.00 52.26 ? 468 GLU A OE2 1 ATOM 3723 N N . GLU A 1 469 ? 24.108 38.550 14.676 1.00 34.93 ? 469 GLU A N 1 ATOM 3724 C CA . GLU A 1 469 ? 25.215 39.434 14.340 1.00 33.00 ? 469 GLU A CA 1 ATOM 3725 C C . GLU A 1 469 ? 24.689 40.706 13.706 1.00 30.84 ? 469 GLU A C 1 ATOM 3726 O O . GLU A 1 469 ? 23.640 40.706 13.063 1.00 30.96 ? 469 GLU A O 1 ATOM 3727 C CB . GLU A 1 469 ? 26.170 38.748 13.366 1.00 34.64 ? 469 GLU A CB 1 ATOM 3728 C CG . GLU A 1 469 ? 26.800 37.481 13.905 1.00 37.59 ? 469 GLU A CG 1 ATOM 3729 C CD . GLU A 1 469 ? 27.848 36.907 12.965 1.00 40.15 ? 469 GLU A CD 1 ATOM 3730 O OE1 . GLU A 1 469 ? 28.466 35.880 13.322 1.00 40.82 ? 469 GLU A OE1 1 ATOM 3731 O OE2 . GLU A 1 469 ? 28.053 37.484 11.871 1.00 39.50 ? 469 GLU A OE2 1 ATOM 3732 N N . ILE A 1 470 ? 25.418 41.795 13.889 1.00 29.42 ? 470 ILE A N 1 ATOM 3733 C CA . ILE A 1 470 ? 25.014 43.071 13.326 1.00 27.83 ? 470 ILE A CA 1 ATOM 3734 C C . ILE A 1 470 ? 25.538 43.160 11.903 1.00 27.32 ? 470 ILE A C 1 ATOM 3735 O O . ILE A 1 470 ? 26.745 43.140 11.679 1.00 27.92 ? 470 ILE A O 1 ATOM 3736 C CB . ILE A 1 470 ? 25.582 44.212 14.152 1.00 27.73 ? 470 ILE A CB 1 ATOM 3737 C CG1 . ILE A 1 470 ? 25.155 44.028 15.608 1.00 27.18 ? 470 ILE A CG1 1 ATOM 3738 C CG2 . ILE A 1 470 ? 25.100 45.540 13.606 1.00 27.30 ? 470 ILE A CG2 1 ATOM 3739 C CD1 . ILE A 1 470 ? 25.754 45.037 16.542 1.00 30.39 ? 470 ILE A CD1 1 ATOM 3740 N N . SER A 1 471 ? 24.630 43.243 10.935 1.00 26.46 ? 471 SER A N 1 ATOM 3741 C CA . SER A 1 471 ? 25.046 43.322 9.540 1.00 25.84 ? 471 SER A CA 1 ATOM 3742 C C . SER A 1 471 ? 24.790 44.703 8.944 1.00 24.91 ? 471 SER A C 1 ATOM 3743 O O . SER A 1 471 ? 23.866 45.416 9.355 1.00 22.01 ? 471 SER A O 1 ATOM 3744 C CB . SER A 1 471 ? 24.329 42.257 8.710 1.00 26.10 ? 471 SER A CB 1 ATOM 3745 O OG . SER A 1 471 ? 22.948 42.545 8.605 1.00 31.98 ? 471 SER A OG 1 ATOM 3746 N N . LEU A 1 472 ? 25.611 45.068 7.962 1.00 23.71 ? 472 LEU A N 1 ATOM 3747 C CA . LEU A 1 472 ? 25.509 46.367 7.314 1.00 23.77 ? 472 LEU A CA 1 ATOM 3748 C C . LEU A 1 472 ? 25.871 46.323 5.832 1.00 24.66 ? 472 LEU A C 1 ATOM 3749 O O . LEU A 1 472 ? 26.952 45.865 5.463 1.00 26.20 ? 472 LEU A O 1 ATOM 3750 C CB . LEU A 1 472 ? 26.436 47.360 8.020 1.00 20.80 ? 472 LEU A CB 1 ATOM 3751 C CG . LEU A 1 472 ? 26.647 48.711 7.332 1.00 20.77 ? 472 LEU A CG 1 ATOM 3752 C CD1 . LEU A 1 472 ? 25.378 49.541 7.433 1.00 18.38 ? 472 LEU A CD1 1 ATOM 3753 C CD2 . LEU A 1 472 ? 27.818 49.434 7.983 1.00 19.82 ? 472 LEU A CD2 1 ATOM 3754 N N . ARG A 1 473 ? 24.967 46.799 4.982 1.00 24.07 ? 473 ARG A N 1 ATOM 3755 C CA . ARG A 1 473 ? 25.238 46.848 3.552 1.00 24.48 ? 473 ARG A CA 1 ATOM 3756 C C . ARG A 1 473 ? 25.343 48.316 3.142 1.00 25.80 ? 473 ARG A C 1 ATOM 3757 O O . ARG A 1 473 ? 24.587 49.163 3.625 1.00 26.30 ? 473 ARG A O 1 ATOM 3758 C CB . ARG A 1 473 ? 24.130 46.164 2.750 1.00 22.67 ? 473 ARG A CB 1 ATOM 3759 C CG . ARG A 1 473 ? 24.396 46.157 1.247 1.00 22.30 ? 473 ARG A CG 1 ATOM 3760 C CD . ARG A 1 473 ? 23.278 45.467 0.478 1.00 21.83 ? 473 ARG A CD 1 ATOM 3761 N NE . ARG A 1 473 ? 23.483 45.527 -0.969 1.00 20.58 ? 473 ARG A NE 1 ATOM 3762 C CZ . ARG A 1 473 ? 22.602 45.090 -1.867 1.00 20.30 ? 473 ARG A CZ 1 ATOM 3763 N NH1 . ARG A 1 473 ? 21.450 44.554 -1.476 1.00 18.56 ? 473 ARG A NH1 1 ATOM 3764 N NH2 . ARG A 1 473 ? 22.866 45.198 -3.160 1.00 18.45 ? 473 ARG A NH2 1 ATOM 3765 N N . ASN A 1 474 ? 26.289 48.615 2.261 1.00 26.08 ? 474 ASN A N 1 ATOM 3766 C CA . ASN A 1 474 ? 26.496 49.981 1.798 1.00 24.59 ? 474 ASN A CA 1 ATOM 3767 C C . ASN A 1 474 ? 26.607 50.105 0.290 1.00 24.43 ? 474 ASN A C 1 ATOM 3768 O O . ASN A 1 474 ? 27.441 49.455 -0.349 1.00 24.00 ? 474 ASN A O 1 ATOM 3769 C CB . ASN A 1 474 ? 27.763 50.572 2.418 1.00 26.07 ? 474 ASN A CB 1 ATOM 3770 C CG . ASN A 1 474 ? 27.529 51.110 3.804 1.00 28.50 ? 474 ASN A CG 1 ATOM 3771 O OD1 . ASN A 1 474 ? 26.903 52.155 3.973 1.00 30.33 ? 474 ASN A OD1 1 ATOM 3772 N ND2 . ASN A 1 474 ? 28.025 50.398 4.811 1.00 30.15 ? 474 ASN A ND2 1 ATOM 3773 N N . LEU A 1 475 ? 25.752 50.951 -0.268 1.00 22.25 ? 475 LEU A N 1 ATOM 3774 C CA . LEU A 1 475 ? 25.764 51.228 -1.691 1.00 20.31 ? 475 LEU A CA 1 ATOM 3775 C C . LEU A 1 475 ? 26.582 52.515 -1.813 1.00 21.14 ? 475 LEU A C 1 ATOM 3776 O O . LEU A 1 475 ? 26.126 53.590 -1.416 1.00 22.14 ? 475 LEU A O 1 ATOM 3777 C CB . LEU A 1 475 ? 24.335 51.439 -2.184 1.00 18.54 ? 475 LEU A CB 1 ATOM 3778 C CG . LEU A 1 475 ? 23.733 50.372 -3.102 1.00 19.42 ? 475 LEU A CG 1 ATOM 3779 C CD1 . LEU A 1 475 ? 24.109 48.973 -2.656 1.00 15.86 ? 475 LEU A CD1 1 ATOM 3780 C CD2 . LEU A 1 475 ? 22.231 50.556 -3.125 1.00 16.27 ? 475 LEU A CD2 1 ATOM 3781 N N . ILE A 1 476 ? 27.806 52.399 -2.314 1.00 20.24 ? 476 ILE A N 1 ATOM 3782 C CA . ILE A 1 476 ? 28.666 53.565 -2.467 1.00 20.38 ? 476 ILE A CA 1 ATOM 3783 C C . ILE A 1 476 ? 28.662 54.011 -3.923 1.00 22.61 ? 476 ILE A C 1 ATOM 3784 O O . ILE A 1 476 ? 29.076 53.259 -4.812 1.00 23.83 ? 476 ILE A O 1 ATOM 3785 C CB . ILE A 1 476 ? 30.118 53.250 -2.059 1.00 20.04 ? 476 ILE A CB 1 ATOM 3786 C CG1 . ILE A 1 476 ? 30.153 52.666 -0.644 1.00 20.84 ? 476 ILE A CG1 1 ATOM 3787 C CG2 . ILE A 1 476 ? 30.958 54.519 -2.129 1.00 19.02 ? 476 ILE A CG2 1 ATOM 3788 C CD1 . ILE A 1 476 ? 31.556 52.263 -0.176 1.00 19.32 ? 476 ILE A CD1 1 ATOM 3789 N N . ASP A 1 477 ? 28.197 55.235 -4.170 1.00 22.63 ? 477 ASP A N 1 ATOM 3790 C CA . ASP A 1 477 ? 28.146 55.757 -5.532 1.00 23.04 ? 477 ASP A CA 1 ATOM 3791 C C . ASP A 1 477 ? 28.496 57.248 -5.613 1.00 23.64 ? 477 ASP A C 1 ATOM 3792 O O . ASP A 1 477 ? 27.628 58.091 -5.833 1.00 23.11 ? 477 ASP A O 1 ATOM 3793 C CB . ASP A 1 477 ? 26.755 55.500 -6.137 1.00 21.60 ? 477 ASP A CB 1 ATOM 3794 C CG . ASP A 1 477 ? 26.766 55.528 -7.649 1.00 22.53 ? 477 ASP A CG 1 ATOM 3795 O OD1 . ASP A 1 477 ? 25.707 55.278 -8.272 1.00 22.67 ? 477 ASP A OD1 1 ATOM 3796 O OD2 . ASP A 1 477 ? 27.844 55.804 -8.216 1.00 21.32 ? 477 ASP A OD2 1 ATOM 3797 N N . HIS A 1 478 ? 29.778 57.552 -5.427 1.00 24.35 ? 478 HIS A N 1 ATOM 3798 C CA . HIS A 1 478 ? 30.310 58.915 -5.488 1.00 24.83 ? 478 HIS A CA 1 ATOM 3799 C C . HIS A 1 478 ? 29.786 59.928 -4.475 1.00 25.74 ? 478 HIS A C 1 ATOM 3800 O O . HIS A 1 478 ? 30.355 60.058 -3.396 1.00 28.35 ? 478 HIS A O 1 ATOM 3801 C CB . HIS A 1 478 ? 30.159 59.473 -6.903 1.00 25.29 ? 478 HIS A CB 1 ATOM 3802 C CG . HIS A 1 478 ? 30.857 58.652 -7.940 1.00 28.19 ? 478 HIS A CG 1 ATOM 3803 N ND1 . HIS A 1 478 ? 30.324 57.487 -8.451 1.00 28.96 ? 478 HIS A ND1 1 ATOM 3804 C CD2 . HIS A 1 478 ? 32.071 58.797 -8.523 1.00 28.47 ? 478 HIS A CD2 1 ATOM 3805 C CE1 . HIS A 1 478 ? 31.179 56.950 -9.302 1.00 27.87 ? 478 HIS A CE1 1 ATOM 3806 N NE2 . HIS A 1 478 ? 32.247 57.725 -9.364 1.00 28.81 ? 478 HIS A NE2 1 ATOM 3807 N N . SER A 1 479 ? 28.729 60.665 -4.804 1.00 25.10 ? 479 SER A N 1 ATOM 3808 C CA . SER A 1 479 ? 28.222 61.656 -3.856 1.00 24.81 ? 479 SER A CA 1 ATOM 3809 C C . SER A 1 479 ? 27.063 61.139 -3.019 1.00 24.77 ? 479 SER A C 1 ATOM 3810 O O . SER A 1 479 ? 26.442 61.895 -2.272 1.00 25.63 ? 479 SER A O 1 ATOM 3811 C CB . SER A 1 479 ? 27.798 62.945 -4.573 1.00 24.65 ? 479 SER A CB 1 ATOM 3812 O OG . SER A 1 479 ? 26.552 62.797 -5.229 1.00 24.53 ? 479 SER A OG 1 ATOM 3813 N N . ILE A 1 480 ? 26.767 59.852 -3.143 1.00 24.46 ? 480 ILE A N 1 ATOM 3814 C CA . ILE A 1 480 ? 25.688 59.267 -2.361 1.00 23.05 ? 480 ILE A CA 1 ATOM 3815 C C . ILE A 1 480 ? 26.100 57.931 -1.760 1.00 24.43 ? 480 ILE A C 1 ATOM 3816 O O . ILE A 1 480 ? 26.841 57.162 -2.374 1.00 24.22 ? 480 ILE A O 1 ATOM 3817 C CB . ILE A 1 480 ? 24.411 59.039 -3.210 1.00 22.61 ? 480 ILE A CB 1 ATOM 3818 C CG1 . ILE A 1 480 ? 23.253 58.628 -2.288 1.00 19.63 ? 480 ILE A CG1 1 ATOM 3819 C CG2 . ILE A 1 480 ? 24.661 57.960 -4.265 1.00 18.16 ? 480 ILE A CG2 1 ATOM 3820 C CD1 . ILE A 1 480 ? 21.916 58.461 -2.978 1.00 16.84 ? 480 ILE A CD1 1 ATOM 3821 N N . ILE A 1 481 ? 25.623 57.672 -0.548 1.00 24.16 ? 481 ILE A N 1 ATOM 3822 C CA . ILE A 1 481 ? 25.889 56.416 0.133 1.00 24.19 ? 481 ILE A CA 1 ATOM 3823 C C . ILE A 1 481 ? 24.584 55.966 0.770 1.00 25.26 ? 481 ILE A C 1 ATOM 3824 O O . ILE A 1 481 ? 23.971 56.711 1.536 1.00 25.31 ? 481 ILE A O 1 ATOM 3825 C CB . ILE A 1 481 ? 26.935 56.558 1.261 1.00 25.29 ? 481 ILE A CB 1 ATOM 3826 C CG1 . ILE A 1 481 ? 28.294 56.951 0.688 1.00 25.15 ? 481 ILE A CG1 1 ATOM 3827 C CG2 . ILE A 1 481 ? 27.055 55.242 2.015 1.00 24.24 ? 481 ILE A CG2 1 ATOM 3828 C CD1 . ILE A 1 481 ? 29.350 57.166 1.749 1.00 22.59 ? 481 ILE A CD1 1 ATOM 3829 N N . GLU A 1 482 ? 24.145 54.758 0.442 1.00 25.50 ? 482 GLU A N 1 ATOM 3830 C CA . GLU A 1 482 ? 22.923 54.230 1.032 1.00 24.15 ? 482 GLU A CA 1 ATOM 3831 C C . GLU A 1 482 ? 23.304 53.088 1.968 1.00 23.95 ? 482 GLU A C 1 ATOM 3832 O O . GLU A 1 482 ? 23.850 52.069 1.544 1.00 23.09 ? 482 GLU A O 1 ATOM 3833 C CB . GLU A 1 482 ? 21.961 53.749 -0.052 1.00 23.13 ? 482 GLU A CB 1 ATOM 3834 C CG . GLU A 1 482 ? 21.504 54.859 -0.966 1.00 25.35 ? 482 GLU A CG 1 ATOM 3835 C CD . GLU A 1 482 ? 20.421 54.416 -1.917 1.00 27.42 ? 482 GLU A CD 1 ATOM 3836 O OE1 . GLU A 1 482 ? 19.331 54.042 -1.439 1.00 30.69 ? 482 GLU A OE1 1 ATOM 3837 O OE2 . GLU A 1 482 ? 20.656 54.439 -3.143 1.00 26.75 ? 482 GLU A OE2 1 ATOM 3838 N N . SER A 1 483 ? 23.021 53.281 3.250 1.00 23.67 ? 483 SER A N 1 ATOM 3839 C CA . SER A 1 483 ? 23.345 52.298 4.266 1.00 23.99 ? 483 SER A CA 1 ATOM 3840 C C . SER A 1 483 ? 22.119 51.524 4.737 1.00 24.47 ? 483 SER A C 1 ATOM 3841 O O . SER A 1 483 ? 21.096 52.108 5.109 1.00 23.45 ? 483 SER A O 1 ATOM 3842 C CB . SER A 1 483 ? 24.005 53.000 5.447 1.00 24.30 ? 483 SER A CB 1 ATOM 3843 O OG . SER A 1 483 ? 25.095 53.789 5.001 1.00 25.14 ? 483 SER A OG 1 ATOM 3844 N N . PHE A 1 484 ? 22.239 50.200 4.716 1.00 23.69 ? 484 PHE A N 1 ATOM 3845 C CA . PHE A 1 484 ? 21.165 49.312 5.134 1.00 22.16 ? 484 PHE A CA 1 ATOM 3846 C C . PHE A 1 484 ? 21.654 48.485 6.308 1.00 21.85 ? 484 PHE A C 1 ATOM 3847 O O . PHE A 1 484 ? 22.505 47.612 6.148 1.00 21.87 ? 484 PHE A O 1 ATOM 3848 C CB . PHE A 1 484 ? 20.770 48.381 3.985 1.00 22.25 ? 484 PHE A CB 1 ATOM 3849 C CG . PHE A 1 484 ? 20.264 49.102 2.769 1.00 22.70 ? 484 PHE A CG 1 ATOM 3850 C CD1 . PHE A 1 484 ? 18.900 49.323 2.589 1.00 21.97 ? 484 PHE A CD1 1 ATOM 3851 C CD2 . PHE A 1 484 ? 21.154 49.586 1.815 1.00 22.12 ? 484 PHE A CD2 1 ATOM 3852 C CE1 . PHE A 1 484 ? 18.429 50.018 1.478 1.00 21.71 ? 484 PHE A CE1 1 ATOM 3853 C CE2 . PHE A 1 484 ? 20.693 50.285 0.696 1.00 22.91 ? 484 PHE A CE2 1 ATOM 3854 C CZ . PHE A 1 484 ? 19.328 50.502 0.529 1.00 23.02 ? 484 PHE A CZ 1 ATOM 3855 N N . GLY A 1 485 ? 21.124 48.773 7.491 1.00 21.32 ? 485 GLY A N 1 ATOM 3856 C CA . GLY A 1 485 ? 21.524 48.027 8.664 1.00 19.91 ? 485 GLY A CA 1 ATOM 3857 C C . GLY A 1 485 ? 20.568 46.882 8.944 1.00 19.57 ? 485 GLY A C 1 ATOM 3858 O O . GLY A 1 485 ? 19.362 46.998 8.710 1.00 18.30 ? 485 GLY A O 1 ATOM 3859 N N . ALA A 1 486 ? 21.113 45.771 9.433 1.00 18.90 ? 486 ALA A N 1 ATOM 3860 C CA . ALA A 1 486 ? 20.321 44.597 9.774 1.00 20.14 ? 486 ALA A CA 1 ATOM 3861 C C . ALA A 1 486 ? 19.370 44.168 8.661 1.00 21.88 ? 486 ALA A C 1 ATOM 3862 O O . ALA A 1 486 ? 18.159 44.067 8.870 1.00 23.29 ? 486 ALA A O 1 ATOM 3863 C CB . ALA A 1 486 ? 19.533 44.855 11.057 1.00 16.88 ? 486 ALA A CB 1 ATOM 3864 N N . GLY A 1 487 ? 19.922 43.923 7.477 1.00 22.31 ? 487 GLY A N 1 ATOM 3865 C CA . GLY A 1 487 ? 19.113 43.483 6.352 1.00 21.19 ? 487 GLY A CA 1 ATOM 3866 C C . GLY A 1 487 ? 18.031 44.428 5.859 1.00 22.24 ? 487 GLY A C 1 ATOM 3867 O O . GLY A 1 487 ? 17.151 44.015 5.102 1.00 23.21 ? 487 GLY A O 1 ATOM 3868 N N . GLY A 1 488 ? 18.075 45.687 6.276 1.00 21.19 ? 488 GLY A N 1 ATOM 3869 C CA . GLY A 1 488 ? 17.071 46.626 5.816 1.00 22.16 ? 488 GLY A CA 1 ATOM 3870 C C . GLY A 1 488 ? 16.119 47.126 6.881 1.00 24.06 ? 488 GLY A C 1 ATOM 3871 O O . GLY A 1 488 ? 15.134 47.798 6.560 1.00 23.23 ? 488 GLY A O 1 ATOM 3872 N N . LYS A 1 489 ? 16.396 46.802 8.144 1.00 23.39 ? 489 LYS A N 1 ATOM 3873 C CA . LYS A 1 489 ? 15.545 47.259 9.238 1.00 22.79 ? 489 LYS A CA 1 ATOM 3874 C C . LYS A 1 489 ? 15.790 48.740 9.500 1.00 22.97 ? 489 LYS A C 1 ATOM 3875 O O . LYS A 1 489 ? 14.895 49.461 9.951 1.00 21.43 ? 489 LYS A O 1 ATOM 3876 C CB . LYS A 1 489 ? 15.828 46.470 10.519 1.00 23.16 ? 489 LYS A CB 1 ATOM 3877 C CG . LYS A 1 489 ? 15.080 45.159 10.636 1.00 23.40 ? 489 LYS A CG 1 ATOM 3878 C CD . LYS A 1 489 ? 15.316 44.525 11.997 1.00 25.49 ? 489 LYS A CD 1 ATOM 3879 C CE . LYS A 1 489 ? 14.429 43.307 12.211 1.00 29.32 ? 489 LYS A CE 1 ATOM 3880 N NZ . LYS A 1 489 ? 14.560 42.744 13.585 1.00 31.87 ? 489 LYS A NZ 1 ATOM 3881 N N . THR A 1 490 ? 17.010 49.184 9.215 1.00 21.53 ? 490 THR A N 1 ATOM 3882 C CA . THR A 1 490 ? 17.384 50.575 9.424 1.00 21.92 ? 490 THR A CA 1 ATOM 3883 C C . THR A 1 490 ? 18.161 51.090 8.223 1.00 23.40 ? 490 THR A C 1 ATOM 3884 O O . THR A 1 490 ? 19.273 50.636 7.937 1.00 23.22 ? 490 THR A O 1 ATOM 3885 C CB . THR A 1 490 ? 18.241 50.732 10.693 1.00 22.02 ? 490 THR A CB 1 ATOM 3886 O OG1 . THR A 1 490 ? 17.511 50.237 11.823 1.00 23.78 ? 490 THR A OG1 1 ATOM 3887 C CG2 . THR A 1 490 ? 18.587 52.191 10.924 1.00 21.17 ? 490 THR A CG2 1 ATOM 3888 N N . CYS A 1 491 ? 17.563 52.048 7.525 1.00 22.77 ? 491 CYS A N 1 ATOM 3889 C CA . CYS A 1 491 ? 18.174 52.620 6.340 1.00 22.35 ? 491 CYS A CA 1 ATOM 3890 C C . CYS A 1 491 ? 18.524 54.090 6.525 1.00 23.26 ? 491 CYS A C 1 ATOM 3891 O O . CYS A 1 491 ? 17.749 54.861 7.102 1.00 23.31 ? 491 CYS A O 1 ATOM 3892 C CB . CYS A 1 491 ? 17.222 52.456 5.157 1.00 22.66 ? 491 CYS A CB 1 ATOM 3893 S SG . CYS A 1 491 ? 16.632 50.767 4.960 1.00 23.15 ? 491 CYS A SG 1 ATOM 3894 N N . ILE A 1 492 ? 19.698 54.472 6.031 1.00 22.15 ? 492 ILE A N 1 ATOM 3895 C CA . ILE A 1 492 ? 20.163 55.851 6.122 1.00 20.84 ? 492 ILE A CA 1 ATOM 3896 C C . ILE A 1 492 ? 20.866 56.228 4.828 1.00 20.90 ? 492 ILE A C 1 ATOM 3897 O O . ILE A 1 492 ? 21.851 55.594 4.452 1.00 21.49 ? 492 ILE A O 1 ATOM 3898 C CB . ILE A 1 492 ? 21.183 56.049 7.256 1.00 21.14 ? 492 ILE A CB 1 ATOM 3899 C CG1 . ILE A 1 492 ? 20.614 55.553 8.583 1.00 20.83 ? 492 ILE A CG1 1 ATOM 3900 C CG2 . ILE A 1 492 ? 21.554 57.526 7.352 1.00 21.28 ? 492 ILE A CG2 1 ATOM 3901 C CD1 . ILE A 1 492 ? 21.593 55.692 9.745 1.00 19.53 ? 492 ILE A CD1 1 ATOM 3902 N N . THR A 1 493 ? 20.364 57.256 4.157 1.00 18.34 ? 493 THR A N 1 ATOM 3903 C CA . THR A 1 493 ? 20.968 57.708 2.919 1.00 18.65 ? 493 THR A CA 1 ATOM 3904 C C . THR A 1 493 ? 21.793 58.966 3.190 1.00 20.15 ? 493 THR A C 1 ATOM 3905 O O . THR A 1 493 ? 21.321 59.905 3.833 1.00 18.58 ? 493 THR A O 1 ATOM 3906 C CB . THR A 1 493 ? 19.891 58.016 1.858 1.00 19.31 ? 493 THR A CB 1 ATOM 3907 O OG1 . THR A 1 493 ? 19.185 56.810 1.530 1.00 21.62 ? 493 THR A OG1 1 ATOM 3908 C CG2 . THR A 1 493 ? 20.529 58.582 0.592 1.00 15.61 ? 493 THR A CG2 1 ATOM 3909 N N . SER A 1 494 ? 23.026 58.980 2.694 1.00 20.10 ? 494 SER A N 1 ATOM 3910 C CA . SER A 1 494 ? 23.912 60.120 2.898 1.00 20.12 ? 494 SER A CA 1 ATOM 3911 C C . SER A 1 494 ? 24.398 60.740 1.594 1.00 21.26 ? 494 SER A C 1 ATOM 3912 O O . SER A 1 494 ? 24.619 60.046 0.596 1.00 20.48 ? 494 SER A O 1 ATOM 3913 C CB . SER A 1 494 ? 25.153 59.700 3.697 1.00 20.31 ? 494 SER A CB 1 ATOM 3914 O OG . SER A 1 494 ? 24.821 59.134 4.947 1.00 21.73 ? 494 SER A OG 1 ATOM 3915 N N . ARG A 1 495 ? 24.558 62.059 1.611 1.00 21.10 ? 495 ARG A N 1 ATOM 3916 C CA . ARG A 1 495 ? 25.092 62.773 0.459 1.00 20.16 ? 495 ARG A CA 1 ATOM 3917 C C . ARG A 1 495 ? 26.397 63.371 0.970 1.00 19.98 ? 495 ARG A C 1 ATOM 3918 O O . ARG A 1 495 ? 26.413 64.024 2.021 1.00 17.54 ? 495 ARG A O 1 ATOM 3919 C CB . ARG A 1 495 ? 24.145 63.885 -0.013 1.00 19.94 ? 495 ARG A CB 1 ATOM 3920 C CG . ARG A 1 495 ? 22.891 63.402 -0.740 1.00 19.77 ? 495 ARG A CG 1 ATOM 3921 C CD . ARG A 1 495 ? 23.205 62.456 -1.902 1.00 19.08 ? 495 ARG A CD 1 ATOM 3922 N NE . ARG A 1 495 ? 23.966 63.071 -2.988 1.00 18.10 ? 495 ARG A NE 1 ATOM 3923 C CZ . ARG A 1 495 ? 23.475 63.949 -3.860 1.00 19.71 ? 495 ARG A CZ 1 ATOM 3924 N NH1 . ARG A 1 495 ? 22.208 64.337 -3.787 1.00 19.03 ? 495 ARG A NH1 1 ATOM 3925 N NH2 . ARG A 1 495 ? 24.250 64.426 -4.827 1.00 18.60 ? 495 ARG A NH2 1 ATOM 3926 N N . ILE A 1 496 ? 27.489 63.115 0.252 1.00 19.52 ? 496 ILE A N 1 ATOM 3927 C CA . ILE A 1 496 ? 28.797 63.632 0.646 1.00 20.22 ? 496 ILE A CA 1 ATOM 3928 C C . ILE A 1 496 ? 29.553 64.215 -0.536 1.00 21.46 ? 496 ILE A C 1 ATOM 3929 O O . ILE A 1 496 ? 29.443 63.733 -1.665 1.00 20.09 ? 496 ILE A O 1 ATOM 3930 C CB . ILE A 1 496 ? 29.678 62.545 1.322 1.00 19.39 ? 496 ILE A CB 1 ATOM 3931 C CG1 . ILE A 1 496 ? 29.970 61.393 0.348 1.00 20.95 ? 496 ILE A CG1 1 ATOM 3932 C CG2 . ILE A 1 496 ? 29.001 62.066 2.596 1.00 17.29 ? 496 ILE A CG2 1 ATOM 3933 C CD1 . ILE A 1 496 ? 28.771 60.529 -0.015 1.00 19.87 ? 496 ILE A CD1 1 ATOM 3934 N N . TYR A 1 497 ? 30.327 65.256 -0.260 1.00 22.61 ? 497 TYR A N 1 ATOM 3935 C CA . TYR A 1 497 ? 31.081 65.932 -1.299 1.00 24.74 ? 497 TYR A CA 1 ATOM 3936 C C . TYR A 1 497 ? 32.534 66.143 -0.905 1.00 26.60 ? 497 TYR A C 1 ATOM 3937 O O . TYR A 1 497 ? 32.995 67.276 -0.761 1.00 26.64 ? 497 TYR A O 1 ATOM 3938 C CB . TYR A 1 497 ? 30.430 67.278 -1.594 1.00 24.73 ? 497 TYR A CB 1 ATOM 3939 C CG . TYR A 1 497 ? 28.967 67.182 -1.947 1.00 24.97 ? 497 TYR A CG 1 ATOM 3940 C CD1 . TYR A 1 497 ? 28.552 67.077 -3.276 1.00 24.53 ? 497 TYR A CD1 1 ATOM 3941 C CD2 . TYR A 1 497 ? 27.990 67.203 -0.948 1.00 24.74 ? 497 TYR A CD2 1 ATOM 3942 C CE1 . TYR A 1 497 ? 27.196 67.005 -3.600 1.00 25.60 ? 497 TYR A CE1 1 ATOM 3943 C CE2 . TYR A 1 497 ? 26.636 67.128 -1.261 1.00 25.00 ? 497 TYR A CE2 1 ATOM 3944 C CZ . TYR A 1 497 ? 26.245 67.033 -2.586 1.00 26.17 ? 497 TYR A CZ 1 ATOM 3945 O OH . TYR A 1 497 ? 24.903 66.993 -2.892 1.00 26.63 ? 497 TYR A OH 1 ATOM 3946 N N . PRO A 1 498 ? 33.279 65.049 -0.715 1.00 28.12 ? 498 PRO A N 1 ATOM 3947 C CA . PRO A 1 498 ? 34.683 65.213 -0.341 1.00 28.94 ? 498 PRO A CA 1 ATOM 3948 C C . PRO A 1 498 ? 35.437 65.954 -1.445 1.00 31.31 ? 498 PRO A C 1 ATOM 3949 O O . PRO A 1 498 ? 35.118 65.831 -2.628 1.00 30.98 ? 498 PRO A O 1 ATOM 3950 C CB . PRO A 1 498 ? 35.158 63.774 -0.154 1.00 27.82 ? 498 PRO A CB 1 ATOM 3951 C CG . PRO A 1 498 ? 34.294 63.007 -1.115 1.00 27.94 ? 498 PRO A CG 1 ATOM 3952 C CD . PRO A 1 498 ? 32.939 63.628 -0.905 1.00 28.41 ? 498 PRO A CD 1 ATOM 3953 N N . LYS A 1 499 ? 36.435 66.730 -1.053 1.00 33.79 ? 499 LYS A N 1 ATOM 3954 C CA . LYS A 1 499 ? 37.210 67.498 -2.012 1.00 35.42 ? 499 LYS A CA 1 ATOM 3955 C C . LYS A 1 499 ? 38.213 66.661 -2.804 1.00 35.08 ? 499 LYS A C 1 ATOM 3956 O O . LYS A 1 499 ? 38.425 66.898 -3.992 1.00 34.69 ? 499 LYS A O 1 ATOM 3957 C CB . LYS A 1 499 ? 37.942 68.619 -1.283 1.00 37.50 ? 499 LYS A CB 1 ATOM 3958 C CG . LYS A 1 499 ? 38.724 69.535 -2.185 1.00 40.65 ? 499 LYS A CG 1 ATOM 3959 C CD . LYS A 1 499 ? 39.536 70.497 -1.352 1.00 45.20 ? 499 LYS A CD 1 ATOM 3960 C CE . LYS A 1 499 ? 40.343 71.436 -2.223 1.00 47.64 ? 499 LYS A CE 1 ATOM 3961 N NZ . LYS A 1 499 ? 41.211 72.307 -1.384 1.00 51.63 ? 499 LYS A NZ 1 ATOM 3962 N N . PHE A 1 500 ? 38.817 65.675 -2.149 1.00 34.67 ? 500 PHE A N 1 ATOM 3963 C CA . PHE A 1 500 ? 39.826 64.840 -2.788 1.00 35.57 ? 500 PHE A CA 1 ATOM 3964 C C . PHE A 1 500 ? 39.418 64.167 -4.094 1.00 36.43 ? 500 PHE A C 1 ATOM 3965 O O . PHE A 1 500 ? 40.274 63.856 -4.924 1.00 36.22 ? 500 PHE A O 1 ATOM 3966 C CB . PHE A 1 500 ? 40.324 63.773 -1.805 1.00 34.72 ? 500 PHE A CB 1 ATOM 3967 C CG . PHE A 1 500 ? 39.414 62.579 -1.675 1.00 34.71 ? 500 PHE A CG 1 ATOM 3968 C CD1 . PHE A 1 500 ? 39.398 61.585 -2.651 1.00 33.95 ? 500 PHE A CD1 1 ATOM 3969 C CD2 . PHE A 1 500 ? 38.579 62.445 -0.571 1.00 35.27 ? 500 PHE A CD2 1 ATOM 3970 C CE1 . PHE A 1 500 ? 38.565 60.473 -2.529 1.00 34.49 ? 500 PHE A CE1 1 ATOM 3971 C CE2 . PHE A 1 500 ? 37.741 61.335 -0.437 1.00 34.52 ? 500 PHE A CE2 1 ATOM 3972 C CZ . PHE A 1 500 ? 37.734 60.348 -1.418 1.00 34.59 ? 500 PHE A CZ 1 ATOM 3973 N N . VAL A 1 501 ? 38.123 63.941 -4.283 1.00 37.40 ? 501 VAL A N 1 ATOM 3974 C CA . VAL A 1 501 ? 37.659 63.263 -5.491 1.00 39.49 ? 501 VAL A CA 1 ATOM 3975 C C . VAL A 1 501 ? 38.082 63.926 -6.790 1.00 40.75 ? 501 VAL A C 1 ATOM 3976 O O . VAL A 1 501 ? 37.979 63.326 -7.856 1.00 41.42 ? 501 VAL A O 1 ATOM 3977 C CB . VAL A 1 501 ? 36.123 63.099 -5.505 1.00 37.88 ? 501 VAL A CB 1 ATOM 3978 C CG1 . VAL A 1 501 ? 35.684 62.292 -4.303 1.00 36.70 ? 501 VAL A CG1 1 ATOM 3979 C CG2 . VAL A 1 501 ? 35.449 64.460 -5.534 1.00 39.32 ? 501 VAL A CG2 1 ATOM 3980 N N . ASN A 1 502 ? 38.562 65.158 -6.715 1.00 42.59 ? 502 ASN A N 1 ATOM 3981 C CA . ASN A 1 502 ? 38.980 65.835 -7.931 1.00 45.64 ? 502 ASN A CA 1 ATOM 3982 C C . ASN A 1 502 ? 40.378 65.478 -8.392 1.00 47.20 ? 502 ASN A C 1 ATOM 3983 O O . ASN A 1 502 ? 40.750 65.786 -9.521 1.00 48.96 ? 502 ASN A O 1 ATOM 3984 C CB . ASN A 1 502 ? 38.879 67.347 -7.769 1.00 45.71 ? 502 ASN A CB 1 ATOM 3985 C CG . ASN A 1 502 ? 37.467 67.840 -7.921 1.00 47.18 ? 502 ASN A CG 1 ATOM 3986 O OD1 . ASN A 1 502 ? 36.793 68.147 -6.932 1.00 48.05 ? 502 ASN A OD1 1 ATOM 3987 N ND2 . ASN A 1 502 ? 36.996 67.907 -9.168 1.00 45.14 ? 502 ASN A ND2 1 ATOM 3988 N N . ASN A 1 503 ? 41.152 64.825 -7.532 1.00 48.52 ? 503 ASN A N 1 ATOM 3989 C CA . ASN A 1 503 ? 42.516 64.461 -7.897 1.00 50.24 ? 503 ASN A CA 1 ATOM 3990 C C . ASN A 1 503 ? 42.834 62.984 -7.682 1.00 50.31 ? 503 ASN A C 1 ATOM 3991 O O . ASN A 1 503 ? 43.072 62.245 -8.642 1.00 52.37 ? 503 ASN A O 1 ATOM 3992 C CB . ASN A 1 503 ? 43.501 65.318 -7.107 1.00 52.13 ? 503 ASN A CB 1 ATOM 3993 C CG . ASN A 1 503 ? 42.986 66.725 -6.883 1.00 55.63 ? 503 ASN A CG 1 ATOM 3994 O OD1 . ASN A 1 503 ? 42.147 66.958 -6.006 1.00 56.69 ? 503 ASN A OD1 1 ATOM 3995 N ND2 . ASN A 1 503 ? 43.469 67.670 -7.685 1.00 56.54 ? 503 ASN A ND2 1 ATOM 3996 N N . GLU A 1 504 ? 42.827 62.554 -6.427 1.00 48.49 ? 504 GLU A N 1 ATOM 3997 C CA . GLU A 1 504 ? 43.137 61.172 -6.098 1.00 46.71 ? 504 GLU A CA 1 ATOM 3998 C C . GLU A 1 504 ? 41.901 60.286 -6.022 1.00 44.22 ? 504 GLU A C 1 ATOM 3999 O O . GLU A 1 504 ? 40.773 60.778 -5.982 1.00 43.11 ? 504 GLU A O 1 ATOM 4000 C CB . GLU A 1 504 ? 43.878 61.129 -4.772 1.00 48.77 ? 504 GLU A CB 1 ATOM 4001 C CG . GLU A 1 504 ? 43.049 61.625 -3.618 1.00 52.33 ? 504 GLU A CG 1 ATOM 4002 C CD . GLU A 1 504 ? 43.898 62.076 -2.455 1.00 55.29 ? 504 GLU A CD 1 ATOM 4003 O OE1 . GLU A 1 504 ? 44.523 63.154 -2.570 1.00 55.71 ? 504 GLU A OE1 1 ATOM 4004 O OE2 . GLU A 1 504 ? 43.945 61.348 -1.435 1.00 57.77 ? 504 GLU A OE2 1 ATOM 4005 N N . GLU A 1 505 ? 42.126 58.974 -6.007 1.00 42.18 ? 505 GLU A N 1 ATOM 4006 C CA . GLU A 1 505 ? 41.036 58.009 -5.928 1.00 40.68 ? 505 GLU A CA 1 ATOM 4007 C C . GLU A 1 505 ? 40.562 57.843 -4.496 1.00 38.45 ? 505 GLU A C 1 ATOM 4008 O O . GLU A 1 505 ? 41.262 58.201 -3.550 1.00 37.65 ? 505 GLU A O 1 ATOM 4009 C CB . GLU A 1 505 ? 41.480 56.652 -6.457 1.00 43.25 ? 505 GLU A CB 1 ATOM 4010 C CG . GLU A 1 505 ? 41.949 56.676 -7.890 1.00 50.24 ? 505 GLU A CG 1 ATOM 4011 C CD . GLU A 1 505 ? 42.248 55.287 -8.420 1.00 54.68 ? 505 GLU A CD 1 ATOM 4012 O OE1 . GLU A 1 505 ? 43.000 54.543 -7.747 1.00 56.42 ? 505 GLU A OE1 1 ATOM 4013 O OE2 . GLU A 1 505 ? 41.732 54.938 -9.507 1.00 57.20 ? 505 GLU A OE2 1 ATOM 4014 N N . ALA A 1 506 ? 39.367 57.287 -4.347 1.00 36.28 ? 506 ALA A N 1 ATOM 4015 C CA . ALA A 1 506 ? 38.783 57.072 -3.032 1.00 34.06 ? 506 ALA A CA 1 ATOM 4016 C C . ALA A 1 506 ? 39.263 55.758 -2.442 1.00 32.87 ? 506 ALA A C 1 ATOM 4017 O O . ALA A 1 506 ? 39.783 54.902 -3.152 1.00 32.47 ? 506 ALA A O 1 ATOM 4018 C CB . ALA A 1 506 ? 37.268 57.071 -3.133 1.00 33.10 ? 506 ALA A CB 1 ATOM 4019 N N . HIS A 1 507 ? 39.094 55.612 -1.134 1.00 32.55 ? 507 HIS A N 1 ATOM 4020 C CA . HIS A 1 507 ? 39.498 54.398 -0.448 1.00 31.24 ? 507 HIS A CA 1 ATOM 4021 C C . HIS A 1 507 ? 38.361 53.847 0.392 1.00 29.78 ? 507 HIS A C 1 ATOM 4022 O O . HIS A 1 507 ? 37.398 54.553 0.701 1.00 28.94 ? 507 HIS A O 1 ATOM 4023 C CB . HIS A 1 507 ? 40.720 54.654 0.428 1.00 33.34 ? 507 HIS A CB 1 ATOM 4024 C CG . HIS A 1 507 ? 41.964 54.952 -0.348 1.00 36.05 ? 507 HIS A CG 1 ATOM 4025 N ND1 . HIS A 1 507 ? 42.167 56.149 -0.997 1.00 38.62 ? 507 HIS A ND1 1 ATOM 4026 C CD2 . HIS A 1 507 ? 43.058 54.196 -0.597 1.00 35.75 ? 507 HIS A CD2 1 ATOM 4027 C CE1 . HIS A 1 507 ? 43.335 56.120 -1.614 1.00 38.63 ? 507 HIS A CE1 1 ATOM 4028 N NE2 . HIS A 1 507 ? 43.896 54.946 -1.387 1.00 37.70 ? 507 HIS A NE2 1 ATOM 4029 N N . LEU A 1 508 ? 38.484 52.575 0.748 1.00 27.78 ? 508 LEU A N 1 ATOM 4030 C CA . LEU A 1 508 ? 37.480 51.880 1.532 1.00 26.90 ? 508 LEU A CA 1 ATOM 4031 C C . LEU A 1 508 ? 38.159 51.238 2.734 1.00 27.00 ? 508 LEU A C 1 ATOM 4032 O O . LEU A 1 508 ? 39.199 50.597 2.597 1.00 28.24 ? 508 LEU A O 1 ATOM 4033 C CB . LEU A 1 508 ? 36.813 50.818 0.655 1.00 25.94 ? 508 LEU A CB 1 ATOM 4034 C CG . LEU A 1 508 ? 35.741 49.912 1.251 1.00 24.91 ? 508 LEU A CG 1 ATOM 4035 C CD1 . LEU A 1 508 ? 34.644 50.748 1.878 1.00 23.90 ? 508 LEU A CD1 1 ATOM 4036 C CD2 . LEU A 1 508 ? 35.185 49.022 0.149 1.00 23.09 ? 508 LEU A CD2 1 ATOM 4037 N N . PHE A 1 509 ? 37.569 51.416 3.912 1.00 27.32 ? 509 PHE A N 1 ATOM 4038 C CA . PHE A 1 509 ? 38.133 50.868 5.147 1.00 27.20 ? 509 PHE A CA 1 ATOM 4039 C C . PHE A 1 509 ? 37.085 50.264 6.071 1.00 26.98 ? 509 PHE A C 1 ATOM 4040 O O . PHE A 1 509 ? 35.901 50.604 6.013 1.00 27.07 ? 509 PHE A O 1 ATOM 4041 C CB . PHE A 1 509 ? 38.823 51.963 5.962 1.00 27.87 ? 509 PHE A CB 1 ATOM 4042 C CG . PHE A 1 509 ? 39.954 52.634 5.266 1.00 26.83 ? 509 PHE A CG 1 ATOM 4043 C CD1 . PHE A 1 509 ? 41.244 52.147 5.394 1.00 26.26 ? 509 PHE A CD1 1 ATOM 4044 C CD2 . PHE A 1 509 ? 39.734 53.783 4.511 1.00 26.10 ? 509 PHE A CD2 1 ATOM 4045 C CE1 . PHE A 1 509 ? 42.306 52.796 4.786 1.00 26.19 ? 509 PHE A CE1 1 ATOM 4046 C CE2 . PHE A 1 509 ? 40.789 54.441 3.896 1.00 26.40 ? 509 PHE A CE2 1 ATOM 4047 C CZ . PHE A 1 509 ? 42.079 53.947 4.035 1.00 27.88 ? 509 PHE A CZ 1 ATOM 4048 N N . VAL A 1 510 ? 37.553 49.379 6.939 1.00 27.08 ? 510 VAL A N 1 ATOM 4049 C CA . VAL A 1 510 ? 36.722 48.756 7.957 1.00 27.55 ? 510 VAL A CA 1 ATOM 4050 C C . VAL A 1 510 ? 37.418 49.258 9.222 1.00 27.91 ? 510 VAL A C 1 ATOM 4051 O O . VAL A 1 510 ? 38.650 49.300 9.270 1.00 27.98 ? 510 VAL A O 1 ATOM 4052 C CB . VAL A 1 510 ? 36.791 47.217 7.887 1.00 26.53 ? 510 VAL A CB 1 ATOM 4053 C CG1 . VAL A 1 510 ? 35.983 46.615 9.008 1.00 28.13 ? 510 VAL A CG1 1 ATOM 4054 C CG2 . VAL A 1 510 ? 36.259 46.736 6.556 1.00 27.41 ? 510 VAL A CG2 1 ATOM 4055 N N . PHE A 1 511 ? 36.667 49.669 10.236 1.00 28.00 ? 511 PHE A N 1 ATOM 4056 C CA . PHE A 1 511 ? 37.333 50.176 11.432 1.00 28.08 ? 511 PHE A CA 1 ATOM 4057 C C . PHE A 1 511 ? 36.609 49.859 12.728 1.00 28.32 ? 511 PHE A C 1 ATOM 4058 O O . PHE A 1 511 ? 35.419 49.540 12.743 1.00 27.33 ? 511 PHE A O 1 ATOM 4059 C CB . PHE A 1 511 ? 37.526 51.698 11.324 1.00 27.98 ? 511 PHE A CB 1 ATOM 4060 C CG . PHE A 1 511 ? 36.296 52.490 11.679 1.00 28.03 ? 511 PHE A CG 1 ATOM 4061 C CD1 . PHE A 1 511 ? 36.201 53.141 12.907 1.00 28.44 ? 511 PHE A CD1 1 ATOM 4062 C CD2 . PHE A 1 511 ? 35.211 52.538 10.811 1.00 28.72 ? 511 PHE A CD2 1 ATOM 4063 C CE1 . PHE A 1 511 ? 35.036 53.830 13.268 1.00 29.29 ? 511 PHE A CE1 1 ATOM 4064 C CE2 . PHE A 1 511 ? 34.041 53.223 11.160 1.00 30.08 ? 511 PHE A CE2 1 ATOM 4065 C CZ . PHE A 1 511 ? 33.955 53.869 12.392 1.00 29.44 ? 511 PHE A CZ 1 ATOM 4066 N N . ASN A 1 512 ? 37.355 49.956 13.821 1.00 29.47 ? 512 ASN A N 1 ATOM 4067 C CA . ASN A 1 512 ? 36.815 49.724 15.147 1.00 29.97 ? 512 ASN A CA 1 ATOM 4068 C C . ASN A 1 512 ? 37.523 50.667 16.105 1.00 30.78 ? 512 ASN A C 1 ATOM 4069 O O . ASN A 1 512 ? 38.672 50.425 16.475 1.00 30.98 ? 512 ASN A O 1 ATOM 4070 C CB . ASN A 1 512 ? 37.038 48.279 15.576 1.00 29.00 ? 512 ASN A CB 1 ATOM 4071 C CG . ASN A 1 512 ? 36.674 48.049 17.019 1.00 29.73 ? 512 ASN A CG 1 ATOM 4072 O OD1 . ASN A 1 512 ? 35.812 48.736 17.565 1.00 30.83 ? 512 ASN A OD1 1 ATOM 4073 N ND2 . ASN A 1 512 ? 37.316 47.072 17.647 1.00 31.12 ? 512 ASN A ND2 1 ATOM 4074 N N . ASN A 1 513 ? 36.846 51.749 16.488 1.00 31.69 ? 513 ASN A N 1 ATOM 4075 C CA . ASN A 1 513 ? 37.435 52.728 17.396 1.00 32.05 ? 513 ASN A CA 1 ATOM 4076 C C . ASN A 1 513 ? 36.955 52.545 18.831 1.00 31.94 ? 513 ASN A C 1 ATOM 4077 O O . ASN A 1 513 ? 37.085 53.446 19.657 1.00 31.29 ? 513 ASN A O 1 ATOM 4078 C CB . ASN A 1 513 ? 37.129 54.155 16.933 1.00 32.93 ? 513 ASN A CB 1 ATOM 4079 C CG . ASN A 1 513 ? 38.367 55.034 16.910 1.00 33.91 ? 513 ASN A CG 1 ATOM 4080 O OD1 . ASN A 1 513 ? 39.299 54.810 17.677 1.00 36.23 ? 513 ASN A OD1 1 ATOM 4081 N ND2 . ASN A 1 513 ? 38.376 56.026 16.022 1.00 37.83 ? 513 ASN A ND2 1 ATOM 4082 N N . GLY A 1 514 ? 36.392 51.378 19.124 1.00 32.19 ? 514 GLY A N 1 ATOM 4083 C CA . GLY A 1 514 ? 35.937 51.107 20.473 1.00 33.05 ? 514 GLY A CA 1 ATOM 4084 C C . GLY A 1 514 ? 37.091 50.540 21.285 1.00 33.63 ? 514 GLY A C 1 ATOM 4085 O O . GLY A 1 514 ? 38.175 50.301 20.748 1.00 32.90 ? 514 GLY A O 1 ATOM 4086 N N . THR A 1 515 ? 36.873 50.325 22.578 1.00 33.82 ? 515 THR A N 1 ATOM 4087 C CA . THR A 1 515 ? 37.923 49.773 23.426 1.00 33.66 ? 515 THR A CA 1 ATOM 4088 C C . THR A 1 515 ? 37.806 48.253 23.455 1.00 34.44 ? 515 THR A C 1 ATOM 4089 O O . THR A 1 515 ? 38.729 47.556 23.861 1.00 34.86 ? 515 THR A O 1 ATOM 4090 C CB . THR A 1 515 ? 37.839 50.338 24.861 1.00 31.45 ? 515 THR A CB 1 ATOM 4091 O OG1 . THR A 1 515 ? 36.560 50.032 25.434 1.00 31.69 ? 515 THR A OG1 1 ATOM 4092 C CG2 . THR A 1 515 ? 38.040 51.846 24.835 1.00 29.64 ? 515 THR A CG2 1 ATOM 4093 N N . GLN A 1 516 ? 36.659 47.754 23.012 1.00 35.70 ? 516 GLN A N 1 ATOM 4094 C CA . GLN A 1 516 ? 36.407 46.324 22.950 1.00 37.38 ? 516 GLN A CA 1 ATOM 4095 C C . GLN A 1 516 ? 36.701 45.811 21.550 1.00 38.67 ? 516 GLN A C 1 ATOM 4096 O O . GLN A 1 516 ? 36.591 46.540 20.564 1.00 39.83 ? 516 GLN A O 1 ATOM 4097 C CB . GLN A 1 516 ? 34.953 46.024 23.296 1.00 38.71 ? 516 GLN A CB 1 ATOM 4098 C CG . GLN A 1 516 ? 34.631 46.235 24.747 1.00 42.22 ? 516 GLN A CG 1 ATOM 4099 C CD . GLN A 1 516 ? 35.237 45.165 25.619 1.00 43.17 ? 516 GLN A CD 1 ATOM 4100 O OE1 . GLN A 1 516 ? 34.822 44.004 25.570 1.00 44.95 ? 516 GLN A OE1 1 ATOM 4101 N NE2 . GLN A 1 516 ? 36.228 45.542 26.419 1.00 41.87 ? 516 GLN A NE2 1 ATOM 4102 N N . ASN A 1 517 ? 37.057 44.540 21.471 1.00 39.36 ? 517 ASN A N 1 ATOM 4103 C CA . ASN A 1 517 ? 37.384 43.911 20.208 1.00 38.98 ? 517 ASN A CA 1 ATOM 4104 C C . ASN A 1 517 ? 36.122 43.411 19.502 1.00 37.35 ? 517 ASN A C 1 ATOM 4105 O O . ASN A 1 517 ? 35.175 42.963 20.154 1.00 37.22 ? 517 ASN A O 1 ATOM 4106 C CB . ASN A 1 517 ? 38.338 42.747 20.494 1.00 42.32 ? 517 ASN A CB 1 ATOM 4107 C CG . ASN A 1 517 ? 39.058 42.259 19.261 1.00 48.55 ? 517 ASN A CG 1 ATOM 4108 O OD1 . ASN A 1 517 ? 38.469 41.605 18.393 1.00 50.25 ? 517 ASN A OD1 1 ATOM 4109 N ND2 . ASN A 1 517 ? 40.348 42.579 19.169 1.00 51.23 ? 517 ASN A ND2 1 ATOM 4110 N N . VAL A 1 518 ? 36.094 43.526 18.177 1.00 36.19 ? 518 VAL A N 1 ATOM 4111 C CA . VAL A 1 518 ? 34.963 43.023 17.382 1.00 35.67 ? 518 VAL A CA 1 ATOM 4112 C C . VAL A 1 518 ? 35.528 42.217 16.217 1.00 34.85 ? 518 VAL A C 1 ATOM 4113 O O . VAL A 1 518 ? 36.649 42.459 15.768 1.00 34.39 ? 518 VAL A O 1 ATOM 4114 C CB . VAL A 1 518 ? 34.048 44.147 16.795 1.00 35.03 ? 518 VAL A CB 1 ATOM 4115 C CG1 . VAL A 1 518 ? 33.342 44.886 17.914 1.00 36.38 ? 518 VAL A CG1 1 ATOM 4116 C CG2 . VAL A 1 518 ? 34.860 45.101 15.938 1.00 35.29 ? 518 VAL A CG2 1 ATOM 4117 N N . LYS A 1 519 ? 34.753 41.256 15.734 1.00 34.10 ? 519 LYS A N 1 ATOM 4118 C CA . LYS A 1 519 ? 35.205 40.429 14.633 1.00 33.84 ? 519 LYS A CA 1 ATOM 4119 C C . LYS A 1 519 ? 34.302 40.512 13.418 1.00 33.44 ? 519 LYS A C 1 ATOM 4120 O O . LYS A 1 519 ? 33.079 40.629 13.527 1.00 34.01 ? 519 LYS A O 1 ATOM 4121 C CB . LYS A 1 519 ? 35.319 38.964 15.082 1.00 35.37 ? 519 LYS A CB 1 ATOM 4122 C CG . LYS A 1 519 ? 35.541 37.976 13.933 1.00 39.14 ? 519 LYS A CG 1 ATOM 4123 C CD . LYS A 1 519 ? 35.675 36.524 14.397 1.00 41.88 ? 519 LYS A CD 1 ATOM 4124 C CE . LYS A 1 519 ? 37.045 36.247 15.012 1.00 44.00 ? 519 LYS A CE 1 ATOM 4125 N NZ . LYS A 1 519 ? 37.219 34.807 15.368 1.00 44.50 ? 519 LYS A NZ 1 ATOM 4126 N N . ILE A 1 520 ? 34.923 40.466 12.250 1.00 32.52 ? 520 ILE A N 1 ATOM 4127 C CA . ILE A 1 520 ? 34.188 40.482 11.001 1.00 30.94 ? 520 ILE A CA 1 ATOM 4128 C C . ILE A 1 520 ? 33.992 39.013 10.667 1.00 30.09 ? 520 ILE A C 1 ATOM 4129 O O . ILE A 1 520 ? 34.951 38.329 10.317 1.00 29.63 ? 520 ILE A O 1 ATOM 4130 C CB . ILE A 1 520 ? 35.010 41.132 9.879 1.00 30.90 ? 520 ILE A CB 1 ATOM 4131 C CG1 . ILE A 1 520 ? 35.280 42.599 10.213 1.00 32.24 ? 520 ILE A CG1 1 ATOM 4132 C CG2 . ILE A 1 520 ? 34.276 41.003 8.553 1.00 30.30 ? 520 ILE A CG2 1 ATOM 4133 C CD1 . ILE A 1 520 ? 36.158 43.297 9.198 1.00 33.27 ? 520 ILE A CD1 1 ATOM 4134 N N . SER A 1 521 ? 32.774 38.506 10.806 1.00 29.75 ? 521 SER A N 1 ATOM 4135 C CA . SER A 1 521 ? 32.557 37.108 10.479 1.00 30.96 ? 521 SER A CA 1 ATOM 4136 C C . SER A 1 521 ? 32.730 37.000 8.967 1.00 32.31 ? 521 SER A C 1 ATOM 4137 O O . SER A 1 521 ? 33.432 36.123 8.469 1.00 33.26 ? 521 SER A O 1 ATOM 4138 C CB . SER A 1 521 ? 31.162 36.645 10.909 1.00 28.53 ? 521 SER A CB 1 ATOM 4139 O OG . SER A 1 521 ? 30.145 37.355 10.232 1.00 33.08 ? 521 SER A OG 1 ATOM 4140 N N . GLU A 1 522 ? 32.107 37.911 8.233 1.00 32.72 ? 522 GLU A N 1 ATOM 4141 C CA . GLU A 1 522 ? 32.236 37.902 6.791 1.00 34.27 ? 522 GLU A CA 1 ATOM 4142 C C . GLU A 1 522 ? 32.034 39.287 6.211 1.00 32.95 ? 522 GLU A C 1 ATOM 4143 O O . GLU A 1 522 ? 31.298 40.103 6.761 1.00 31.47 ? 522 GLU A O 1 ATOM 4144 C CB . GLU A 1 522 ? 31.243 36.921 6.164 1.00 37.74 ? 522 GLU A CB 1 ATOM 4145 C CG . GLU A 1 522 ? 31.208 36.999 4.642 1.00 46.77 ? 522 GLU A CG 1 ATOM 4146 C CD . GLU A 1 522 ? 30.719 35.718 3.985 1.00 51.95 ? 522 GLU A CD 1 ATOM 4147 O OE1 . GLU A 1 522 ? 29.747 35.112 4.496 1.00 54.66 ? 522 GLU A OE1 1 ATOM 4148 O OE2 . GLU A 1 522 ? 31.303 35.329 2.946 1.00 53.36 ? 522 GLU A OE2 1 ATOM 4149 N N . MET A 1 523 ? 32.707 39.546 5.096 1.00 32.31 ? 523 MET A N 1 ATOM 4150 C CA . MET A 1 523 ? 32.610 40.829 4.425 1.00 32.61 ? 523 MET A CA 1 ATOM 4151 C C . MET A 1 523 ? 32.763 40.642 2.917 1.00 32.23 ? 523 MET A C 1 ATOM 4152 O O . MET A 1 523 ? 33.720 40.020 2.461 1.00 32.15 ? 523 MET A O 1 ATOM 4153 C CB . MET A 1 523 ? 33.696 41.765 4.949 1.00 34.51 ? 523 MET A CB 1 ATOM 4154 C CG . MET A 1 523 ? 33.452 43.222 4.629 1.00 38.90 ? 523 MET A CG 1 ATOM 4155 S SD . MET A 1 523 ? 34.695 43.914 3.545 1.00 45.96 ? 523 MET A SD 1 ATOM 4156 C CE . MET A 1 523 ? 34.108 43.358 1.965 1.00 40.66 ? 523 MET A CE 1 ATOM 4157 N N . SER A 1 524 ? 31.811 41.170 2.150 1.00 31.87 ? 524 SER A N 1 ATOM 4158 C CA . SER A 1 524 ? 31.847 41.074 0.689 1.00 30.76 ? 524 SER A CA 1 ATOM 4159 C C . SER A 1 524 ? 31.777 42.455 0.068 1.00 30.69 ? 524 SER A C 1 ATOM 4160 O O . SER A 1 524 ? 30.907 43.256 0.411 1.00 30.45 ? 524 SER A O 1 ATOM 4161 C CB . SER A 1 524 ? 30.676 40.251 0.160 1.00 30.25 ? 524 SER A CB 1 ATOM 4162 O OG . SER A 1 524 ? 30.779 38.896 0.546 1.00 33.56 ? 524 SER A OG 1 ATOM 4163 N N . ALA A 1 525 ? 32.696 42.725 -0.854 1.00 29.26 ? 525 ALA A N 1 ATOM 4164 C CA . ALA A 1 525 ? 32.743 44.008 -1.544 1.00 28.21 ? 525 ALA A CA 1 ATOM 4165 C C . ALA A 1 525 ? 32.840 43.769 -3.045 1.00 28.30 ? 525 ALA A C 1 ATOM 4166 O O . ALA A 1 525 ? 33.669 42.985 -3.508 1.00 28.10 ? 525 ALA A O 1 ATOM 4167 C CB . ALA A 1 525 ? 33.935 44.821 -1.062 1.00 25.71 ? 525 ALA A CB 1 ATOM 4168 N N . TRP A 1 526 ? 31.985 44.447 -3.801 1.00 27.87 ? 526 TRP A N 1 ATOM 4169 C CA . TRP A 1 526 ? 31.970 44.319 -5.252 1.00 27.99 ? 526 TRP A CA 1 ATOM 4170 C C . TRP A 1 526 ? 32.126 45.673 -5.913 1.00 28.11 ? 526 TRP A C 1 ATOM 4171 O O . TRP A 1 526 ? 31.547 46.658 -5.461 1.00 28.44 ? 526 TRP A O 1 ATOM 4172 C CB . TRP A 1 526 ? 30.637 43.750 -5.737 1.00 27.83 ? 526 TRP A CB 1 ATOM 4173 C CG . TRP A 1 526 ? 30.409 42.315 -5.477 1.00 29.23 ? 526 TRP A CG 1 ATOM 4174 C CD1 . TRP A 1 526 ? 30.798 41.267 -6.258 1.00 29.42 ? 526 TRP A CD1 1 ATOM 4175 C CD2 . TRP A 1 526 ? 29.676 41.756 -4.385 1.00 30.71 ? 526 TRP A CD2 1 ATOM 4176 N NE1 . TRP A 1 526 ? 30.343 40.084 -5.724 1.00 30.65 ? 526 TRP A NE1 1 ATOM 4177 C CE2 . TRP A 1 526 ? 29.651 40.357 -4.572 1.00 30.67 ? 526 TRP A CE2 1 ATOM 4178 C CE3 . TRP A 1 526 ? 29.034 42.303 -3.264 1.00 32.23 ? 526 TRP A CE3 1 ATOM 4179 C CZ2 . TRP A 1 526 ? 29.007 39.494 -3.679 1.00 32.49 ? 526 TRP A CZ2 1 ATOM 4180 C CZ3 . TRP A 1 526 ? 28.391 41.443 -2.373 1.00 34.17 ? 526 TRP A CZ3 1 ATOM 4181 C CH2 . TRP A 1 526 ? 28.384 40.054 -2.589 1.00 32.99 ? 526 TRP A CH2 1 ATOM 4182 N N . SER A 1 527 ? 32.910 45.720 -6.983 1.00 27.49 ? 527 SER A N 1 ATOM 4183 C CA . SER A 1 527 ? 33.051 46.948 -7.742 1.00 26.43 ? 527 SER A CA 1 ATOM 4184 C C . SER A 1 527 ? 31.767 46.938 -8.563 1.00 26.40 ? 527 SER A C 1 ATOM 4185 O O . SER A 1 527 ? 31.352 45.882 -9.052 1.00 25.34 ? 527 SER A O 1 ATOM 4186 C CB . SER A 1 527 ? 34.260 46.883 -8.672 1.00 26.00 ? 527 SER A CB 1 ATOM 4187 O OG . SER A 1 527 ? 35.469 46.875 -7.938 1.00 29.47 ? 527 SER A OG 1 ATOM 4188 N N . MET A 1 528 ? 31.126 48.090 -8.699 1.00 26.33 ? 528 MET A N 1 ATOM 4189 C CA . MET A 1 528 ? 29.883 48.166 -9.458 1.00 26.97 ? 528 MET A CA 1 ATOM 4190 C C . MET A 1 528 ? 30.110 48.850 -10.794 1.00 27.56 ? 528 MET A C 1 ATOM 4191 O O . MET A 1 528 ? 30.584 49.984 -10.839 1.00 28.42 ? 528 MET A O 1 ATOM 4192 C CB . MET A 1 528 ? 28.838 48.950 -8.666 1.00 27.36 ? 528 MET A CB 1 ATOM 4193 C CG . MET A 1 528 ? 28.520 48.354 -7.314 1.00 26.78 ? 528 MET A CG 1 ATOM 4194 S SD . MET A 1 528 ? 27.768 46.740 -7.480 1.00 30.06 ? 528 MET A SD 1 ATOM 4195 C CE . MET A 1 528 ? 26.052 47.189 -7.688 1.00 29.74 ? 528 MET A CE 1 ATOM 4196 N N . LYS A 1 529 ? 29.781 48.174 -11.887 1.00 27.85 ? 529 LYS A N 1 ATOM 4197 C CA . LYS A 1 529 ? 29.967 48.795 -13.189 1.00 29.38 ? 529 LYS A CA 1 ATOM 4198 C C . LYS A 1 529 ? 28.863 49.822 -13.392 1.00 29.19 ? 529 LYS A C 1 ATOM 4199 O O . LYS A 1 529 ? 27.805 49.738 -12.768 1.00 29.83 ? 529 LYS A O 1 ATOM 4200 C CB . LYS A 1 529 ? 29.921 47.755 -14.308 1.00 30.43 ? 529 LYS A CB 1 ATOM 4201 C CG . LYS A 1 529 ? 28.560 47.147 -14.535 1.00 35.22 ? 529 LYS A CG 1 ATOM 4202 C CD . LYS A 1 529 ? 28.541 46.279 -15.784 1.00 39.08 ? 529 LYS A CD 1 ATOM 4203 C CE . LYS A 1 529 ? 27.168 45.629 -15.972 1.00 44.44 ? 529 LYS A CE 1 ATOM 4204 N NZ . LYS A 1 529 ? 27.041 44.848 -17.241 1.00 46.52 ? 529 LYS A NZ 1 ATOM 4205 N N . ASN A 1 530 ? 29.115 50.800 -14.253 1.00 27.91 ? 530 ASN A N 1 ATOM 4206 C CA . ASN A 1 530 ? 28.138 51.838 -14.534 1.00 27.83 ? 530 ASN A CA 1 ATOM 4207 C C . ASN A 1 530 ? 26.848 51.270 -15.087 1.00 29.12 ? 530 ASN A C 1 ATOM 4208 O O . ASN A 1 530 ? 26.849 50.253 -15.782 1.00 30.83 ? 530 ASN A O 1 ATOM 4209 C CB . ASN A 1 530 ? 28.676 52.806 -15.579 1.00 27.86 ? 530 ASN A CB 1 ATOM 4210 C CG . ASN A 1 530 ? 29.818 53.637 -15.080 1.00 27.86 ? 530 ASN A CG 1 ATOM 4211 O OD1 . ASN A 1 530 ? 30.546 54.219 -15.871 1.00 29.61 ? 530 ASN A OD1 1 ATOM 4212 N ND2 . ASN A 1 530 ? 29.979 53.717 -13.767 1.00 31.88 ? 530 ASN A ND2 1 ATOM 4213 N N . ALA A 1 531 ? 25.745 51.939 -14.780 1.00 29.47 ? 531 ALA A N 1 ATOM 4214 C CA . ALA A 1 531 ? 24.447 51.547 -15.311 1.00 29.67 ? 531 ALA A CA 1 ATOM 4215 C C . ALA A 1 531 ? 24.384 52.302 -16.646 1.00 30.30 ? 531 ALA A C 1 ATOM 4216 O O . ALA A 1 531 ? 24.994 53.364 -16.782 1.00 30.46 ? 531 ALA A O 1 ATOM 4217 C CB . ALA A 1 531 ? 23.334 52.011 -14.384 1.00 26.79 ? 531 ALA A CB 1 ATOM 4218 N N . LYS A 1 532 ? 23.680 51.767 -17.636 1.00 30.63 ? 532 LYS A N 1 ATOM 4219 C CA . LYS A 1 532 ? 23.594 52.458 -18.917 1.00 31.82 ? 532 LYS A CA 1 ATOM 4220 C C . LYS A 1 532 ? 22.470 53.485 -18.920 1.00 30.88 ? 532 LYS A C 1 ATOM 4221 O O . LYS A 1 532 ? 21.380 53.232 -18.414 1.00 31.05 ? 532 LYS A O 1 ATOM 4222 C CB . LYS A 1 532 ? 23.385 51.458 -20.051 1.00 33.78 ? 532 LYS A CB 1 ATOM 4223 C CG . LYS A 1 532 ? 24.585 50.580 -20.313 1.00 41.40 ? 532 LYS A CG 1 ATOM 4224 C CD . LYS A 1 532 ? 24.170 49.262 -20.961 1.00 48.25 ? 532 LYS A CD 1 ATOM 4225 C CE . LYS A 1 532 ? 25.384 48.386 -21.268 1.00 51.87 ? 532 LYS A CE 1 ATOM 4226 N NZ . LYS A 1 532 ? 26.239 48.139 -20.064 1.00 55.49 ? 532 LYS A NZ 1 ATOM 4227 N N . PHE A 1 533 ? 22.755 54.654 -19.481 1.00 30.43 ? 533 PHE A N 1 ATOM 4228 C CA . PHE A 1 533 ? 21.783 55.734 -19.579 1.00 30.11 ? 533 PHE A CA 1 ATOM 4229 C C . PHE A 1 533 ? 21.814 56.267 -20.998 1.00 31.93 ? 533 PHE A C 1 ATOM 4230 O O . PHE A 1 533 ? 22.678 57.068 -21.357 1.00 33.58 ? 533 PHE A O 1 ATOM 4231 C CB . PHE A 1 533 ? 22.129 56.855 -18.604 1.00 28.39 ? 533 PHE A CB 1 ATOM 4232 C CG . PHE A 1 533 ? 21.771 56.551 -17.185 1.00 28.72 ? 533 PHE A CG 1 ATOM 4233 C CD1 . PHE A 1 533 ? 20.478 56.768 -16.721 1.00 27.78 ? 533 PHE A CD1 1 ATOM 4234 C CD2 . PHE A 1 533 ? 22.721 56.031 -16.312 1.00 28.81 ? 533 PHE A CD2 1 ATOM 4235 C CE1 . PHE A 1 533 ? 20.134 56.472 -15.406 1.00 28.52 ? 533 PHE A CE1 1 ATOM 4236 C CE2 . PHE A 1 533 ? 22.390 55.728 -14.992 1.00 28.95 ? 533 PHE A CE2 1 ATOM 4237 C CZ . PHE A 1 533 ? 21.093 55.950 -14.537 1.00 29.48 ? 533 PHE A CZ 1 ATOM 4238 N N . VAL A 1 534 ? 20.869 55.809 -21.808 1.00 33.07 ? 534 VAL A N 1 ATOM 4239 C CA . VAL A 1 534 ? 20.783 56.233 -23.191 1.00 33.66 ? 534 VAL A CA 1 ATOM 4240 C C . VAL A 1 534 ? 19.769 57.349 -23.356 1.00 35.44 ? 534 VAL A C 1 ATOM 4241 O O . VAL A 1 534 ? 18.703 57.335 -22.741 1.00 36.42 ? 534 VAL A O 1 ATOM 4242 C CB . VAL A 1 534 ? 20.370 55.069 -24.088 1.00 33.58 ? 534 VAL A CB 1 ATOM 4243 C CG1 . VAL A 1 534 ? 20.282 55.533 -25.529 1.00 33.75 ? 534 VAL A CG1 1 ATOM 4244 C CG2 . VAL A 1 534 ? 21.365 53.939 -23.942 1.00 32.39 ? 534 VAL A CG2 1 ATOM 4245 N N . VAL A 1 535 ? 20.105 58.321 -24.190 1.00 36.97 ? 535 VAL A N 1 ATOM 4246 C CA . VAL A 1 535 ? 19.205 59.431 -24.441 1.00 39.30 ? 535 VAL A CA 1 ATOM 4247 C C . VAL A 1 535 ? 18.510 59.255 -25.783 1.00 41.61 ? 535 VAL A C 1 ATOM 4248 O O . VAL A 1 535 ? 19.156 59.015 -26.803 1.00 41.86 ? 535 VAL A O 1 ATOM 4249 C CB . VAL A 1 535 ? 19.960 60.767 -24.452 1.00 38.31 ? 535 VAL A CB 1 ATOM 4250 C CG1 . VAL A 1 535 ? 19.009 61.899 -24.806 1.00 37.24 ? 535 VAL A CG1 1 ATOM 4251 C CG2 . VAL A 1 535 ? 20.593 61.010 -23.096 1.00 38.68 ? 535 VAL A CG2 1 ATOM 4252 N N . ASP A 1 536 ? 17.187 59.365 -25.768 1.00 44.24 ? 536 ASP A N 1 ATOM 4253 C CA . ASP A 1 536 ? 16.378 59.244 -26.973 1.00 47.80 ? 536 ASP A CA 1 ATOM 4254 C C . ASP A 1 536 ? 15.328 60.354 -26.930 1.00 50.39 ? 536 ASP A C 1 ATOM 4255 O O . ASP A 1 536 ? 14.124 60.096 -26.852 1.00 50.75 ? 536 ASP A O 1 ATOM 4256 C CB . ASP A 1 536 ? 15.694 57.883 -27.015 1.00 49.10 ? 536 ASP A CB 1 ATOM 4257 C CG . ASP A 1 536 ? 14.863 57.691 -28.266 1.00 52.21 ? 536 ASP A CG 1 ATOM 4258 O OD1 . ASP A 1 536 ? 14.207 56.634 -28.376 1.00 52.59 ? 536 ASP A OD1 1 ATOM 4259 O OD2 . ASP A 1 536 ? 14.870 58.592 -29.137 1.00 55.12 ? 536 ASP A OD2 1 ATOM 4260 N N . GLN A 1 537 ? 15.806 61.593 -26.982 1.00 52.70 ? 537 GLN A N 1 ATOM 4261 C CA . GLN A 1 537 ? 14.944 62.762 -26.912 1.00 55.10 ? 537 GLN A CA 1 ATOM 4262 C C . GLN A 1 537 ? 14.824 63.554 -28.210 1.00 58.11 ? 537 GLN A C 1 ATOM 4263 O O . GLN A 1 537 ? 14.911 62.997 -29.309 1.00 58.40 ? 537 GLN A O 1 ATOM 4264 C CB . GLN A 1 537 ? 15.449 63.679 -25.803 1.00 53.31 ? 537 GLN A CB 1 ATOM 4265 C CG . GLN A 1 537 ? 15.270 63.106 -24.417 1.00 53.44 ? 537 GLN A CG 1 ATOM 4266 C CD . GLN A 1 537 ? 16.045 63.876 -23.374 1.00 53.70 ? 537 GLN A CD 1 ATOM 4267 O OE1 . GLN A 1 537 ? 15.771 63.772 -22.178 1.00 54.23 ? 537 GLN A OE1 1 ATOM 4268 N NE2 . GLN A 1 537 ? 17.031 64.648 -23.820 1.00 53.71 ? 537 GLN A NE2 1 ATOM 4269 N N . SER A 1 538 ? 14.608 64.861 -28.056 1.00 61.40 ? 538 SER A N 1 ATOM 4270 C CA . SER A 1 538 ? 14.467 65.801 -29.167 1.00 62.27 ? 538 SER A CA 1 ATOM 4271 C C . SER A 1 538 ? 13.450 65.315 -30.199 1.00 62.27 ? 538 SER A C 1 ATOM 4272 O O . SER A 1 538 ? 12.348 64.882 -29.853 1.00 61.41 ? 538 SER A O 1 ATOM 4273 C CB . SER A 1 538 ? 15.831 66.030 -29.832 1.00 63.55 ? 538 SER A CB 1 ATOM 4274 O OG . SER A 1 538 ? 15.769 67.068 -30.795 1.00 66.63 ? 538 SER A OG 1 HETATM 4275 C C1 . NAG B 2 . ? 38.801 57.378 16.365 1.00 38.02 ? 650 NAG A C1 1 HETATM 4276 C C2 . NAG B 2 . ? 39.128 58.112 15.055 1.00 39.89 ? 650 NAG A C2 1 HETATM 4277 C C3 . NAG B 2 . ? 40.365 59.000 15.174 1.00 40.79 ? 650 NAG A C3 1 HETATM 4278 C C4 . NAG B 2 . ? 40.333 59.721 16.517 1.00 43.08 ? 650 NAG A C4 1 HETATM 4279 C C5 . NAG B 2 . ? 40.408 58.690 17.651 1.00 40.00 ? 650 NAG A C5 1 HETATM 4280 C C6 . NAG B 2 . ? 39.608 59.095 18.858 1.00 38.47 ? 650 NAG A C6 1 HETATM 4281 C C7 . NAG B 2 . ? 38.485 57.146 12.962 1.00 37.78 ? 650 NAG A C7 1 HETATM 4282 C C8 . NAG B 2 . ? 38.625 56.019 11.952 1.00 37.68 ? 650 NAG A C8 1 HETATM 4283 N N2 . NAG B 2 . ? 39.325 57.151 13.991 1.00 38.20 ? 650 NAG A N2 1 HETATM 4284 O O3 . NAG B 2 . ? 40.376 59.940 14.111 1.00 39.00 ? 650 NAG A O3 1 HETATM 4285 O O4 . NAG B 2 . ? 41.442 60.641 16.621 1.00 49.74 ? 650 NAG A O4 1 HETATM 4286 O O5 . NAG B 2 . ? 39.944 57.368 17.235 1.00 39.53 ? 650 NAG A O5 1 HETATM 4287 O O6 . NAG B 2 . ? 39.766 60.480 19.119 1.00 35.36 ? 650 NAG A O6 1 HETATM 4288 O O7 . NAG B 2 . ? 37.617 58.007 12.809 1.00 37.20 ? 650 NAG A O7 1 HETATM 4289 C C1 . NAG C 2 . ? 41.361 61.823 15.887 1.00 58.95 ? 660 NAG A C1 1 HETATM 4290 C C2 . NAG C 2 . ? 40.740 62.959 16.713 1.00 63.32 ? 660 NAG A C2 1 HETATM 4291 C C3 . NAG C 2 . ? 41.669 63.353 17.863 1.00 67.71 ? 660 NAG A C3 1 HETATM 4292 C C4 . NAG C 2 . ? 43.041 63.746 17.317 1.00 68.89 ? 660 NAG A C4 1 HETATM 4293 C C5 . NAG C 2 . ? 43.615 62.590 16.469 1.00 65.50 ? 660 NAG A C5 1 HETATM 4294 C C6 . NAG C 2 . ? 44.027 61.334 17.243 1.00 61.16 ? 660 NAG A C6 1 HETATM 4295 C C7 . NAG C 2 . ? 39.871 63.989 14.716 1.00 62.87 ? 660 NAG A C7 1 HETATM 4296 C C8 . NAG C 2 . ? 38.370 64.234 14.722 1.00 62.70 ? 660 NAG A C8 1 HETATM 4297 N N2 . NAG C 2 . ? 40.511 64.118 15.870 1.00 62.10 ? 660 NAG A N2 1 HETATM 4298 O O3 . NAG C 2 . ? 41.809 62.268 18.771 1.00 70.32 ? 660 NAG A O3 1 HETATM 4299 O O4 . NAG C 2 . ? 42.938 64.963 16.529 1.00 74.86 ? 660 NAG A O4 1 HETATM 4300 O O5 . NAG C 2 . ? 42.680 62.185 15.420 1.00 64.34 ? 660 NAG A O5 1 HETATM 4301 O O6 . NAG C 2 . ? 44.132 61.576 18.637 1.00 53.05 ? 660 NAG A O6 1 HETATM 4302 O O7 . NAG C 2 . ? 40.441 63.683 13.669 1.00 63.11 ? 660 NAG A O7 1 HETATM 4303 C C1 . MAN D 3 . ? 42.830 66.156 17.254 1.00 81.53 ? 670 MAN A C1 1 HETATM 4304 C C2 . MAN D 3 . ? 41.480 66.857 16.994 1.00 82.72 ? 670 MAN A C2 1 HETATM 4305 C C3 . MAN D 3 . ? 41.413 67.427 15.576 1.00 83.54 ? 670 MAN A C3 1 HETATM 4306 C C4 . MAN D 3 . ? 42.625 68.313 15.313 1.00 84.72 ? 670 MAN A C4 1 HETATM 4307 C C5 . MAN D 3 . ? 43.912 67.523 15.573 1.00 85.43 ? 670 MAN A C5 1 HETATM 4308 C C6 . MAN D 3 . ? 45.152 68.381 15.392 1.00 85.92 ? 670 MAN A C6 1 HETATM 4309 O O2 . MAN D 3 . ? 41.305 67.915 17.929 1.00 82.17 ? 670 MAN A O2 1 HETATM 4310 O O3 . MAN D 3 . ? 40.229 68.199 15.435 1.00 83.33 ? 670 MAN A O3 1 HETATM 4311 O O4 . MAN D 3 . ? 42.600 68.768 13.969 1.00 85.35 ? 670 MAN A O4 1 HETATM 4312 O O5 . MAN D 3 . ? 43.937 67.026 16.935 1.00 84.22 ? 670 MAN A O5 1 HETATM 4313 O O6 . MAN D 3 . ? 45.244 68.876 14.063 1.00 86.31 ? 670 MAN A O6 1 HETATM 4314 C C1 . NAG E 2 . ? 2.455 55.071 -31.651 1.00 39.74 ? 680 NAG A C1 1 HETATM 4315 C C2 . NAG E 2 . ? 2.964 56.021 -32.742 1.00 41.78 ? 680 NAG A C2 1 HETATM 4316 C C3 . NAG E 2 . ? 3.522 55.205 -33.913 1.00 42.30 ? 680 NAG A C3 1 HETATM 4317 C C4 . NAG E 2 . ? 4.600 54.243 -33.414 1.00 44.91 ? 680 NAG A C4 1 HETATM 4318 C C5 . NAG E 2 . ? 4.026 53.369 -32.291 1.00 44.10 ? 680 NAG A C5 1 HETATM 4319 C C6 . NAG E 2 . ? 5.081 52.469 -31.671 1.00 44.17 ? 680 NAG A C6 1 HETATM 4320 C C7 . NAG E 2 . ? 2.065 58.186 -33.343 1.00 41.58 ? 680 NAG A C7 1 HETATM 4321 C C8 . NAG E 2 . ? 0.866 58.995 -33.815 1.00 40.77 ? 680 NAG A C8 1 HETATM 4322 N N2 . NAG E 2 . ? 1.883 56.875 -33.202 1.00 42.35 ? 680 NAG A N2 1 HETATM 4323 O O3 . NAG E 2 . ? 4.070 56.077 -34.888 1.00 41.19 ? 680 NAG A O3 1 HETATM 4324 O O4 . NAG E 2 . ? 5.062 53.411 -34.500 1.00 49.30 ? 680 NAG A O4 1 HETATM 4325 O O5 . NAG E 2 . ? 3.510 54.198 -31.227 1.00 41.65 ? 680 NAG A O5 1 HETATM 4326 O O6 . NAG E 2 . ? 6.188 53.227 -31.196 1.00 43.26 ? 680 NAG A O6 1 HETATM 4327 O O7 . NAG E 2 . ? 3.138 58.749 -33.107 1.00 40.94 ? 680 NAG A O7 1 HETATM 4328 C C1 . NAG F 2 . ? 6.413 53.494 -34.806 1.00 54.64 ? 690 NAG A C1 1 HETATM 4329 C C2 . NAG F 2 . ? 6.803 52.363 -35.763 1.00 57.25 ? 690 NAG A C2 1 HETATM 4330 C C3 . NAG F 2 . ? 8.269 52.512 -36.157 1.00 60.04 ? 690 NAG A C3 1 HETATM 4331 C C4 . NAG F 2 . ? 8.506 53.892 -36.769 1.00 61.57 ? 690 NAG A C4 1 HETATM 4332 C C5 . NAG F 2 . ? 8.029 54.981 -35.793 1.00 61.25 ? 690 NAG A C5 1 HETATM 4333 C C6 . NAG F 2 . ? 8.106 56.368 -36.407 1.00 62.34 ? 690 NAG A C6 1 HETATM 4334 C C7 . NAG F 2 . ? 5.386 50.539 -35.101 1.00 58.10 ? 690 NAG A C7 1 HETATM 4335 C C8 . NAG F 2 . ? 4.958 49.867 -33.803 1.00 58.22 ? 690 NAG A C8 1 HETATM 4336 N N2 . NAG F 2 . ? 6.600 51.071 -35.139 1.00 57.00 ? 690 NAG A N2 1 HETATM 4337 O O3 . NAG F 2 . ? 8.618 51.504 -37.093 1.00 61.70 ? 690 NAG A O3 1 HETATM 4338 O O4 . NAG F 2 . ? 9.891 54.058 -37.050 1.00 63.68 ? 690 NAG A O4 1 HETATM 4339 O O5 . NAG F 2 . ? 6.643 54.764 -35.434 1.00 58.48 ? 690 NAG A O5 1 HETATM 4340 O O6 . NAG F 2 . ? 6.951 56.643 -37.193 1.00 63.11 ? 690 NAG A O6 1 HETATM 4341 O O7 . NAG F 2 . ? 4.610 50.582 -36.058 1.00 58.17 ? 690 NAG A O7 1 HETATM 4342 C C1 . FRU G 4 . ? 7.661 67.802 -2.290 1.00 34.74 ? 800 FRU A C1 1 HETATM 4343 C C2 . FRU G 4 . ? 6.875 68.753 -3.217 1.00 34.45 ? 800 FRU A C2 1 HETATM 4344 C C3 . FRU G 4 . ? 5.444 68.267 -3.523 1.00 31.78 ? 800 FRU A C3 1 HETATM 4345 C C4 . FRU G 4 . ? 5.064 69.052 -4.776 1.00 31.90 ? 800 FRU A C4 1 HETATM 4346 C C5 . FRU G 4 . ? 6.381 69.053 -5.536 1.00 32.75 ? 800 FRU A C5 1 HETATM 4347 C C6 . FRU G 4 . ? 6.685 70.316 -6.331 1.00 33.20 ? 800 FRU A C6 1 HETATM 4348 O O1 . FRU G 4 . ? 9.070 67.914 -2.506 1.00 30.31 ? 800 FRU A O1 1 HETATM 4349 O O2 . FRU G 4 . ? 6.918 70.086 -2.605 1.00 36.29 ? 800 FRU A O2 1 HETATM 4350 O O3 . FRU G 4 . ? 4.559 68.386 -2.415 1.00 27.87 ? 800 FRU A O3 1 HETATM 4351 O O4 . FRU G 4 . ? 4.090 68.402 -5.602 1.00 29.33 ? 800 FRU A O4 1 HETATM 4352 O O5 . FRU G 4 . ? 7.414 68.856 -4.557 1.00 35.23 ? 800 FRU A O5 1 HETATM 4353 O O6 . FRU G 4 . ? 7.811 69.976 -7.154 1.00 29.97 ? 800 FRU A O6 1 HETATM 4354 O O . HOH H 5 . ? 13.892 42.468 -5.614 1.00 2.23 ? 1001 HOH A O 1 HETATM 4355 O O . HOH H 5 . ? 24.410 56.333 4.956 1.00 14.31 ? 1002 HOH A O 1 HETATM 4356 O O . HOH H 5 . ? 7.502 61.040 -22.686 1.00 31.88 ? 1003 HOH A O 1 HETATM 4357 O O . HOH H 5 . ? -15.951 70.965 0.277 1.00 25.04 ? 1004 HOH A O 1 HETATM 4358 O O . HOH H 5 . ? 2.909 45.702 -0.861 1.00 9.92 ? 1005 HOH A O 1 HETATM 4359 O O . HOH H 5 . ? 8.668 39.230 -4.478 1.00 23.07 ? 1006 HOH A O 1 HETATM 4360 O O . HOH H 5 . ? 2.774 55.948 -9.299 1.00 17.64 ? 1007 HOH A O 1 HETATM 4361 O O . HOH H 5 . ? 3.978 58.859 -2.369 1.00 14.33 ? 1008 HOH A O 1 HETATM 4362 O O . HOH H 5 . ? 23.903 64.349 3.630 1.00 17.33 ? 1009 HOH A O 1 HETATM 4363 O O . HOH H 5 . ? 11.558 51.723 8.877 1.00 22.36 ? 1010 HOH A O 1 HETATM 4364 O O . HOH H 5 . ? 30.050 52.953 21.773 1.00 24.44 ? 1011 HOH A O 1 HETATM 4365 O O . HOH H 5 . ? 11.890 58.309 5.575 1.00 11.53 ? 1012 HOH A O 1 HETATM 4366 O O . HOH H 5 . ? 2.474 55.404 -6.492 1.00 21.32 ? 1013 HOH A O 1 HETATM 4367 O O . HOH H 5 . ? -1.843 54.751 -2.813 1.00 14.32 ? 1014 HOH A O 1 HETATM 4368 O O . HOH H 5 . ? 14.812 52.101 8.185 1.00 14.98 ? 1015 HOH A O 1 HETATM 4369 O O . HOH H 5 . ? 1.234 61.190 -3.296 1.00 14.67 ? 1016 HOH A O 1 HETATM 4370 O O . HOH H 5 . ? 24.343 65.952 5.934 1.00 15.31 ? 1017 HOH A O 1 HETATM 4371 O O . HOH H 5 . ? 32.693 61.939 8.720 1.00 20.82 ? 1018 HOH A O 1 HETATM 4372 O O . HOH H 5 . ? 5.138 41.973 3.373 1.00 26.23 ? 1019 HOH A O 1 HETATM 4373 O O . HOH H 5 . ? 9.620 66.654 12.915 1.00 26.50 ? 1020 HOH A O 1 HETATM 4374 O O . HOH H 5 . ? 12.871 60.867 5.317 1.00 13.97 ? 1021 HOH A O 1 HETATM 4375 O O . HOH H 5 . ? 17.626 53.060 -11.021 1.00 18.08 ? 1022 HOH A O 1 HETATM 4376 O O . HOH H 5 . ? 14.992 61.068 7.093 1.00 11.72 ? 1023 HOH A O 1 HETATM 4377 O O . HOH H 5 . ? 28.149 65.591 11.451 1.00 32.72 ? 1024 HOH A O 1 HETATM 4378 O O . HOH H 5 . ? 18.406 51.915 -2.426 1.00 26.40 ? 1025 HOH A O 1 HETATM 4379 O O . HOH H 5 . ? 1.108 56.715 -4.531 1.00 21.97 ? 1026 HOH A O 1 HETATM 4380 O O . HOH H 5 . ? 7.134 63.068 0.875 1.00 26.95 ? 1027 HOH A O 1 HETATM 4381 O O . HOH H 5 . ? 38.700 40.978 -6.895 1.00 18.70 ? 1028 HOH A O 1 HETATM 4382 O O . HOH H 5 . ? -5.267 48.125 -7.581 1.00 26.68 ? 1029 HOH A O 1 HETATM 4383 O O . HOH H 5 . ? 18.223 54.938 -8.905 1.00 17.83 ? 1030 HOH A O 1 HETATM 4384 O O . HOH H 5 . ? 19.880 65.831 -11.134 1.00 15.92 ? 1031 HOH A O 1 HETATM 4385 O O . HOH H 5 . ? 34.079 60.663 10.833 1.00 23.93 ? 1032 HOH A O 1 HETATM 4386 O O . HOH H 5 . ? 20.229 43.635 -3.700 1.00 17.31 ? 1033 HOH A O 1 HETATM 4387 O O . HOH H 5 . ? -3.602 50.445 -7.974 1.00 29.23 ? 1034 HOH A O 1 HETATM 4388 O O . HOH H 5 . ? 23.886 57.605 -12.922 1.00 34.45 ? 1035 HOH A O 1 HETATM 4389 O O . HOH H 5 . ? 5.159 44.627 0.336 1.00 22.40 ? 1036 HOH A O 1 HETATM 4390 O O . HOH H 5 . ? 27.369 66.464 2.884 1.00 21.57 ? 1037 HOH A O 1 HETATM 4391 O O . HOH H 5 . ? 13.194 49.873 6.825 1.00 16.53 ? 1038 HOH A O 1 HETATM 4392 O O . HOH H 5 . ? 6.993 75.231 -10.239 1.00 33.31 ? 1039 HOH A O 1 HETATM 4393 O O . HOH H 5 . ? 29.720 71.957 7.355 1.00 17.50 ? 1040 HOH A O 1 HETATM 4394 O O . HOH H 5 . ? 19.942 74.065 -6.526 1.00 20.70 ? 1041 HOH A O 1 HETATM 4395 O O . HOH H 5 . ? 34.760 54.230 -0.233 1.00 22.04 ? 1042 HOH A O 1 HETATM 4396 O O . HOH H 5 . ? 12.341 63.716 -19.621 1.00 26.70 ? 1043 HOH A O 1 HETATM 4397 O O . HOH H 5 . ? 29.495 50.261 24.522 1.00 18.29 ? 1044 HOH A O 1 HETATM 4398 O O . HOH H 5 . ? 2.736 49.653 -11.827 1.00 30.88 ? 1045 HOH A O 1 HETATM 4399 O O . HOH H 5 . ? 5.949 55.589 -0.130 1.00 36.79 ? 1046 HOH A O 1 HETATM 4400 O O . HOH H 5 . ? 25.666 62.772 26.748 1.00 9.49 ? 1047 HOH A O 1 HETATM 4401 O O . HOH H 5 . ? 30.112 66.065 2.460 1.00 17.74 ? 1048 HOH A O 1 HETATM 4402 O O . HOH H 5 . ? 21.522 64.945 -13.082 1.00 21.98 ? 1049 HOH A O 1 HETATM 4403 O O . HOH H 5 . ? 9.374 52.763 -11.848 1.00 13.90 ? 1050 HOH A O 1 HETATM 4404 O O . HOH H 5 . ? 17.554 51.606 32.467 1.00 38.02 ? 1051 HOH A O 1 HETATM 4405 O O . HOH H 5 . ? 1.401 51.908 14.140 1.00 26.10 ? 1052 HOH A O 1 HETATM 4406 O O . HOH H 5 . ? 2.314 73.900 1.888 1.00 22.35 ? 1053 HOH A O 1 HETATM 4407 O O . HOH H 5 . ? 29.659 66.789 -10.399 1.00 2.23 ? 1054 HOH A O 1 HETATM 4408 O O . HOH H 5 . ? 20.179 53.021 -11.874 1.00 23.83 ? 1055 HOH A O 1 HETATM 4409 O O . HOH H 5 . ? 14.414 61.147 -18.076 1.00 25.30 ? 1056 HOH A O 1 HETATM 4410 O O . HOH H 5 . ? 18.187 48.604 19.511 1.00 21.00 ? 1057 HOH A O 1 HETATM 4411 O O . HOH H 5 . ? 1.979 67.484 -21.219 1.00 27.43 ? 1058 HOH A O 1 HETATM 4412 O O . HOH H 5 . ? 8.024 43.733 -2.082 1.00 23.77 ? 1059 HOH A O 1 HETATM 4413 O O . HOH H 5 . ? 39.582 52.826 14.454 1.00 21.41 ? 1060 HOH A O 1 HETATM 4414 O O . HOH H 5 . ? 4.389 43.807 -17.424 1.00 17.18 ? 1061 HOH A O 1 HETATM 4415 O O . HOH H 5 . ? 11.592 76.964 -14.414 1.00 26.81 ? 1062 HOH A O 1 HETATM 4416 O O . HOH H 5 . ? 13.853 61.925 21.252 1.00 21.63 ? 1063 HOH A O 1 HETATM 4417 O O . HOH H 5 . ? 5.282 54.967 12.959 1.00 20.26 ? 1064 HOH A O 1 HETATM 4418 O O . HOH H 5 . ? 23.414 63.324 22.438 1.00 21.55 ? 1065 HOH A O 1 HETATM 4419 O O . HOH H 5 . ? 3.591 56.318 14.810 1.00 33.35 ? 1066 HOH A O 1 HETATM 4420 O O . HOH H 5 . ? 14.647 53.707 -2.958 1.00 22.65 ? 1067 HOH A O 1 HETATM 4421 O O . HOH H 5 . ? 1.148 50.665 -7.891 1.00 24.12 ? 1068 HOH A O 1 HETATM 4422 O O . HOH H 5 . ? 24.953 48.286 -16.923 1.00 29.75 ? 1069 HOH A O 1 HETATM 4423 O O . HOH H 5 . ? 3.771 60.123 17.182 1.00 36.93 ? 1070 HOH A O 1 HETATM 4424 O O . HOH H 5 . ? 4.898 50.384 -21.439 1.00 22.52 ? 1071 HOH A O 1 HETATM 4425 O O . HOH H 5 . ? 29.091 62.650 14.098 1.00 28.78 ? 1072 HOH A O 1 HETATM 4426 O O . HOH H 5 . ? 7.930 68.605 4.735 1.00 25.82 ? 1073 HOH A O 1 HETATM 4427 O O . HOH H 5 . ? 6.723 61.789 -5.037 1.00 26.16 ? 1074 HOH A O 1 HETATM 4428 O O . HOH H 5 . ? 17.572 46.113 20.553 1.00 34.48 ? 1075 HOH A O 1 HETATM 4429 O O . HOH H 5 . ? 30.354 56.894 23.385 1.00 32.36 ? 1076 HOH A O 1 HETATM 4430 O O . HOH H 5 . ? 18.806 60.958 11.683 1.00 24.80 ? 1077 HOH A O 1 HETATM 4431 O O . HOH H 5 . ? 29.342 70.584 -5.053 1.00 30.26 ? 1078 HOH A O 1 HETATM 4432 O O . HOH H 5 . ? 31.303 68.987 -9.545 1.00 32.40 ? 1079 HOH A O 1 HETATM 4433 O O . HOH H 5 . ? 17.117 68.644 -6.287 1.00 22.90 ? 1080 HOH A O 1 HETATM 4434 O O . HOH H 5 . ? 20.376 50.875 25.889 1.00 20.74 ? 1081 HOH A O 1 HETATM 4435 O O . HOH H 5 . ? 23.759 59.250 -15.138 1.00 51.33 ? 1082 HOH A O 1 HETATM 4436 O O . HOH H 5 . ? 0.819 51.515 -5.231 1.00 28.64 ? 1083 HOH A O 1 HETATM 4437 O O . HOH H 5 . ? 33.645 61.324 2.788 1.00 23.76 ? 1084 HOH A O 1 HETATM 4438 O O . HOH H 5 . ? 0.399 53.505 -3.591 1.00 19.22 ? 1085 HOH A O 1 HETATM 4439 O O . HOH H 5 . ? 21.692 60.415 -16.700 1.00 36.31 ? 1086 HOH A O 1 HETATM 4440 O O . HOH H 5 . ? 34.135 48.201 19.661 1.00 28.96 ? 1087 HOH A O 1 HETATM 4441 O O . HOH H 5 . ? 31.013 70.697 -7.343 1.00 26.56 ? 1088 HOH A O 1 HETATM 4442 O O . HOH H 5 . ? -1.173 60.514 11.710 1.00 29.64 ? 1089 HOH A O 1 HETATM 4443 O O . HOH H 5 . ? 18.454 69.349 -3.909 1.00 31.88 ? 1090 HOH A O 1 HETATM 4444 O O . HOH H 5 . ? 27.502 38.699 17.520 1.00 40.46 ? 1091 HOH A O 1 HETATM 4445 O O . HOH H 5 . ? 15.101 37.513 26.975 1.00 47.92 ? 1092 HOH A O 1 HETATM 4446 O O . HOH H 5 . ? 1.362 39.755 -5.133 1.00 23.16 ? 1093 HOH A O 1 HETATM 4447 O O . HOH H 5 . ? 16.868 59.763 13.450 1.00 24.99 ? 1094 HOH A O 1 HETATM 4448 O O . HOH H 5 . ? 18.827 66.712 -18.601 1.00 24.50 ? 1095 HOH A O 1 HETATM 4449 O O . HOH H 5 . ? 18.407 49.250 26.176 1.00 26.98 ? 1096 HOH A O 1 HETATM 4450 O O . HOH H 5 . ? 3.743 52.368 12.822 1.00 25.45 ? 1097 HOH A O 1 HETATM 4451 O O . HOH H 5 . ? 15.031 65.690 18.036 1.00 29.67 ? 1098 HOH A O 1 HETATM 4452 O O . HOH H 5 . ? 15.314 55.059 15.576 1.00 28.69 ? 1099 HOH A O 1 HETATM 4453 O O . HOH H 5 . ? 1.402 57.341 -25.489 1.00 27.52 ? 1100 HOH A O 1 HETATM 4454 O O . HOH H 5 . ? 21.244 55.993 31.351 1.00 22.79 ? 1101 HOH A O 1 HETATM 4455 O O . HOH H 5 . ? 3.425 57.814 -27.367 1.00 17.84 ? 1102 HOH A O 1 HETATM 4456 O O . HOH H 5 . ? -1.047 41.424 -5.358 1.00 32.03 ? 1103 HOH A O 1 HETATM 4457 O O . HOH H 5 . ? 21.375 41.019 -1.758 1.00 23.10 ? 1104 HOH A O 1 HETATM 4458 O O . HOH H 5 . ? 1.695 52.786 -10.130 1.00 29.08 ? 1105 HOH A O 1 HETATM 4459 O O . HOH H 5 . ? 34.133 61.962 14.188 1.00 24.16 ? 1106 HOH A O 1 HETATM 4460 O O . HOH H 5 . ? 23.362 65.962 21.839 1.00 29.52 ? 1107 HOH A O 1 HETATM 4461 O O . HOH H 5 . ? -13.182 53.024 -13.439 1.00 22.89 ? 1108 HOH A O 1 HETATM 4462 O O . HOH H 5 . ? 17.051 51.691 26.810 1.00 31.35 ? 1109 HOH A O 1 HETATM 4463 O O . HOH H 5 . ? 13.713 64.435 20.249 1.00 26.96 ? 1110 HOH A O 1 HETATM 4464 O O . HOH H 5 . ? 2.838 78.396 -9.751 1.00 26.89 ? 1111 HOH A O 1 HETATM 4465 O O . HOH H 5 . ? -1.819 50.533 -10.653 1.00 39.77 ? 1112 HOH A O 1 HETATM 4466 O O . HOH H 5 . ? 5.703 70.118 7.318 1.00 33.11 ? 1113 HOH A O 1 HETATM 4467 O O . HOH H 5 . ? -4.746 74.913 3.860 1.00 35.93 ? 1114 HOH A O 1 HETATM 4468 O O . HOH H 5 . ? 16.042 42.879 -3.477 1.00 27.14 ? 1115 HOH A O 1 HETATM 4469 O O . HOH H 5 . ? 23.826 41.430 -0.688 1.00 18.61 ? 1116 HOH A O 1 HETATM 4470 O O . HOH H 5 . ? 21.934 72.611 -2.652 1.00 31.31 ? 1117 HOH A O 1 HETATM 4471 O O . HOH H 5 . ? -12.080 50.858 -14.192 1.00 22.52 ? 1118 HOH A O 1 HETATM 4472 O O . HOH H 5 . ? -12.883 54.727 -15.381 1.00 28.33 ? 1119 HOH A O 1 HETATM 4473 O O . HOH H 5 . ? 2.920 58.513 -30.080 1.00 30.83 ? 1120 HOH A O 1 HETATM 4474 O O . HOH H 5 . ? 24.569 39.085 -2.218 1.00 29.46 ? 1121 HOH A O 1 HETATM 4475 O O . HOH H 5 . ? -11.389 51.007 -16.803 1.00 36.10 ? 1122 HOH A O 1 HETATM 4476 O O . HOH H 5 . ? 36.009 53.973 -7.599 1.00 30.00 ? 1123 HOH A O 1 HETATM 4477 O O . HOH H 5 . ? 16.365 48.659 -19.451 1.00 28.02 ? 1124 HOH A O 1 HETATM 4478 O O . HOH H 5 . ? 3.175 64.413 -23.791 1.00 27.71 ? 1125 HOH A O 1 HETATM 4479 O O . HOH H 5 . ? 2.560 60.137 19.946 1.00 43.52 ? 1126 HOH A O 1 HETATM 4480 O O . HOH H 5 . ? -15.891 67.008 -3.602 1.00 28.63 ? 1127 HOH A O 1 HETATM 4481 O O . HOH H 5 . ? -7.557 74.800 -21.088 1.00 20.62 ? 1128 HOH A O 1 HETATM 4482 O O . HOH H 5 . ? -5.552 46.635 6.659 1.00 2.23 ? 1129 HOH A O 1 HETATM 4483 O O . HOH H 5 . ? 16.114 58.001 27.567 1.00 32.53 ? 1130 HOH A O 1 HETATM 4484 O O . HOH H 5 . ? -2.410 76.121 5.599 1.00 37.66 ? 1131 HOH A O 1 HETATM 4485 O O . HOH H 5 . ? 5.170 65.218 -25.639 1.00 39.96 ? 1132 HOH A O 1 HETATM 4486 O O . HOH H 5 . ? -7.157 67.105 -24.087 1.00 25.59 ? 1133 HOH A O 1 HETATM 4487 O O . HOH H 5 . ? 12.011 59.046 13.929 1.00 29.80 ? 1134 HOH A O 1 HETATM 4488 O O . HOH H 5 . ? 5.022 78.624 -11.140 1.00 34.07 ? 1135 HOH A O 1 HETATM 4489 O O . HOH H 5 . ? -0.154 60.224 19.341 1.00 37.34 ? 1136 HOH A O 1 HETATM 4490 O O . HOH H 5 . ? 40.303 59.050 10.873 1.00 33.32 ? 1137 HOH A O 1 HETATM 4491 O O . HOH H 5 . ? 5.507 58.178 -30.819 1.00 35.24 ? 1138 HOH A O 1 HETATM 4492 O O . HOH H 5 . ? 37.929 56.145 -6.743 1.00 17.99 ? 1139 HOH A O 1 HETATM 4493 O O . HOH H 5 . ? -2.125 52.998 -30.312 1.00 33.50 ? 1140 HOH A O 1 HETATM 4494 O O . HOH H 5 . ? -14.466 64.958 -10.319 1.00 37.69 ? 1141 HOH A O 1 HETATM 4495 O O . HOH H 5 . ? 1.556 77.301 -19.900 1.00 36.98 ? 1142 HOH A O 1 HETATM 4496 O O . HOH H 5 . ? 23.900 66.256 19.030 1.00 34.95 ? 1143 HOH A O 1 HETATM 4497 O O . HOH H 5 . ? 26.379 39.034 -6.456 1.00 27.00 ? 1144 HOH A O 1 HETATM 4498 O O . HOH H 5 . ? -3.011 57.821 -9.842 1.00 33.03 ? 1145 HOH A O 1 HETATM 4499 O O . HOH H 5 . ? 10.357 60.902 -26.257 1.00 37.22 ? 1146 HOH A O 1 HETATM 4500 O O . HOH H 5 . ? 31.582 50.915 -15.719 1.00 29.34 ? 1147 HOH A O 1 HETATM 4501 O O . HOH H 5 . ? 18.693 42.355 25.452 1.00 29.39 ? 1148 HOH A O 1 HETATM 4502 O O . HOH H 5 . ? -4.228 66.648 -24.330 1.00 29.11 ? 1149 HOH A O 1 HETATM 4503 O O . HOH H 5 . ? 16.140 75.485 -5.691 1.00 29.70 ? 1150 HOH A O 1 HETATM 4504 O O . HOH H 5 . ? 22.342 44.800 6.416 1.00 21.18 ? 1151 HOH A O 1 HETATM 4505 O O . HOH H 5 . ? 14.167 56.853 21.146 1.00 34.49 ? 1152 HOH A O 1 HETATM 4506 O O . HOH H 5 . ? 41.340 35.883 13.228 1.00 35.52 ? 1153 HOH A O 1 HETATM 4507 O O . HOH H 5 . ? 27.108 71.384 8.069 1.00 37.52 ? 1154 HOH A O 1 HETATM 4508 O O . HOH H 5 . ? 18.376 65.577 16.035 1.00 24.59 ? 1155 HOH A O 1 HETATM 4509 O O . HOH H 5 . ? 18.444 79.435 -10.854 1.00 32.12 ? 1156 HOH A O 1 HETATM 4510 O O . HOH H 5 . ? 12.722 61.407 14.545 1.00 29.11 ? 1157 HOH A O 1 HETATM 4511 O O . HOH H 5 . ? 31.215 75.729 6.344 1.00 35.88 ? 1158 HOH A O 1 HETATM 4512 O O . HOH H 5 . ? -7.829 73.786 -18.289 1.00 39.23 ? 1159 HOH A O 1 HETATM 4513 O O . HOH H 5 . ? 11.559 63.586 18.554 1.00 30.04 ? 1160 HOH A O 1 HETATM 4514 O O . HOH H 5 . ? 18.704 75.489 -4.793 1.00 37.64 ? 1161 HOH A O 1 HETATM 4515 O O . HOH H 5 . ? 24.728 78.894 -2.513 1.00 33.53 ? 1162 HOH A O 1 HETATM 4516 O O . HOH H 5 . ? 42.402 38.116 12.823 1.00 18.38 ? 1163 HOH A O 1 HETATM 4517 O O . HOH H 5 . ? -8.129 75.435 -12.703 1.00 31.69 ? 1164 HOH A O 1 HETATM 4518 O O . HOH H 5 . ? -9.781 50.121 10.872 1.00 31.37 ? 1165 HOH A O 1 HETATM 4519 O O . HOH H 5 . ? -9.138 47.705 -1.731 1.00 40.93 ? 1166 HOH A O 1 HETATM 4520 O O . HOH H 5 . ? -17.436 58.554 -9.847 1.00 32.29 ? 1167 HOH A O 1 HETATM 4521 O O . HOH H 5 . ? -10.208 75.038 -16.460 1.00 40.83 ? 1168 HOH A O 1 HETATM 4522 O O . HOH H 5 . ? 4.469 73.730 -21.208 1.00 41.47 ? 1169 HOH A O 1 HETATM 4523 O O . HOH H 5 . ? -7.796 69.649 -22.970 1.00 48.04 ? 1170 HOH A O 1 HETATM 4524 O O . HOH H 5 . ? 10.868 68.319 14.824 1.00 35.65 ? 1171 HOH A O 1 HETATM 4525 O O . HOH H 5 . ? 14.872 65.376 -18.355 1.00 37.43 ? 1172 HOH A O 1 HETATM 4526 O O . HOH H 5 . ? 15.659 64.913 3.294 1.00 40.17 ? 1173 HOH A O 1 HETATM 4527 O O . HOH H 5 . ? 2.599 50.401 -24.193 1.00 36.67 ? 1174 HOH A O 1 HETATM 4528 O O . HOH H 5 . ? -10.517 76.532 -1.035 1.00 33.44 ? 1175 HOH A O 1 HETATM 4529 O O . HOH H 5 . ? -11.486 63.780 3.218 1.00 38.34 ? 1176 HOH A O 1 HETATM 4530 O O . HOH H 5 . ? 31.218 74.927 -1.250 1.00 29.65 ? 1177 HOH A O 1 HETATM 4531 O O . HOH H 5 . ? 41.047 42.127 -6.286 1.00 32.30 ? 1178 HOH A O 1 HETATM 4532 O O . HOH H 5 . ? -7.101 50.458 -22.691 1.00 34.26 ? 1179 HOH A O 1 HETATM 4533 O O . HOH H 5 . ? 11.897 63.938 15.377 1.00 27.42 ? 1180 HOH A O 1 HETATM 4534 O O . HOH H 5 . ? 22.440 72.356 -16.593 1.00 35.26 ? 1181 HOH A O 1 HETATM 4535 O O . HOH H 5 . ? 22.740 76.717 -0.654 1.00 33.62 ? 1182 HOH A O 1 HETATM 4536 O O . HOH H 5 . ? 3.482 48.213 -25.869 1.00 47.32 ? 1183 HOH A O 1 HETATM 4537 O O . HOH H 5 . ? -13.247 71.222 -14.006 1.00 37.71 ? 1184 HOH A O 1 HETATM 4538 O O . HOH H 5 . ? 9.737 41.510 -2.537 1.00 37.15 ? 1185 HOH A O 1 HETATM 4539 O O . HOH H 5 . ? 14.089 78.384 -13.530 1.00 15.71 ? 1186 HOH A O 1 HETATM 4540 O O . HOH H 5 . ? -5.616 80.418 -0.490 1.00 27.44 ? 1187 HOH A O 1 HETATM 4541 O O . HOH H 5 . ? 14.255 54.360 21.833 1.00 20.50 ? 1188 HOH A O 1 HETATM 4542 O O . HOH H 5 . ? 23.349 36.374 13.213 1.00 34.25 ? 1189 HOH A O 1 HETATM 4543 O O . HOH H 5 . ? 4.302 40.080 9.239 1.00 41.60 ? 1190 HOH A O 1 HETATM 4544 O O . HOH H 5 . ? 2.442 44.623 -16.084 1.00 33.51 ? 1191 HOH A O 1 HETATM 4545 O O . HOH H 5 . ? 5.847 47.183 -24.242 1.00 35.58 ? 1192 HOH A O 1 HETATM 4546 O O . HOH H 5 . ? 14.121 58.086 15.130 1.00 43.68 ? 1193 HOH A O 1 HETATM 4547 O O . HOH H 5 . ? 6.257 60.672 -29.667 1.00 38.86 ? 1194 HOH A O 1 HETATM 4548 O O . HOH H 5 . ? -0.983 62.863 19.124 1.00 35.04 ? 1195 HOH A O 1 HETATM 4549 O O . HOH H 5 . ? 12.013 80.023 -12.537 1.00 33.17 ? 1196 HOH A O 1 HETATM 4550 O O . HOH H 5 . ? 23.281 45.573 -15.809 1.00 43.23 ? 1197 HOH A O 1 HETATM 4551 O O . HOH H 5 . ? 27.479 79.037 -9.146 1.00 45.80 ? 1198 HOH A O 1 HETATM 4552 O O . HOH H 5 . ? 18.511 68.724 1.672 1.00 35.29 ? 1199 HOH A O 1 HETATM 4553 O O . HOH H 5 . ? 12.284 40.224 6.509 1.00 35.80 ? 1200 HOH A O 1 HETATM 4554 O O . HOH H 5 . ? 14.108 65.916 15.348 1.00 36.73 ? 1201 HOH A O 1 HETATM 4555 O O . HOH H 5 . ? 6.988 77.257 -8.373 1.00 34.63 ? 1202 HOH A O 1 HETATM 4556 O O . HOH H 5 . ? 20.958 66.351 16.178 1.00 29.88 ? 1203 HOH A O 1 HETATM 4557 O O . HOH H 5 . ? 8.562 46.640 -24.987 1.00 32.21 ? 1204 HOH A O 1 HETATM 4558 O O . HOH H 5 . ? 33.846 74.268 -1.899 1.00 41.81 ? 1205 HOH A O 1 HETATM 4559 O O . HOH H 5 . ? 21.420 76.568 -12.880 1.00 27.53 ? 1206 HOH A O 1 HETATM 4560 O O . HOH H 5 . ? 20.586 79.239 -12.539 1.00 32.99 ? 1207 HOH A O 1 HETATM 4561 O O . HOH H 5 . ? -4.640 61.680 13.752 1.00 40.30 ? 1208 HOH A O 1 HETATM 4562 O O . HOH H 5 . ? 5.236 78.922 -14.838 1.00 41.91 ? 1209 HOH A O 1 HETATM 4563 O O . HOH H 5 . ? 33.714 71.076 -6.320 1.00 30.98 ? 1210 HOH A O 1 HETATM 4564 O O . HOH H 5 . ? 22.693 58.623 -25.307 1.00 30.68 ? 1211 HOH A O 1 HETATM 4565 O O . HOH H 5 . ? -17.019 65.669 -9.199 1.00 31.71 ? 1212 HOH A O 1 HETATM 4566 O O . HOH H 5 . ? 8.902 55.268 -28.565 1.00 28.23 ? 1213 HOH A O 1 HETATM 4567 O O . HOH H 5 . ? -10.385 76.991 -4.648 1.00 30.86 ? 1214 HOH A O 1 HETATM 4568 O O . HOH H 5 . ? 24.236 42.954 4.814 1.00 5.75 ? 1215 HOH A O 1 HETATM 4569 O O . HOH H 5 . ? 10.946 44.277 -17.839 1.00 42.36 ? 1216 HOH A O 1 HETATM 4570 O O . HOH H 5 . ? 21.579 68.264 21.271 1.00 25.00 ? 1217 HOH A O 1 HETATM 4571 O O . HOH H 5 . ? -5.486 66.231 12.965 1.00 44.42 ? 1218 HOH A O 1 HETATM 4572 O O . HOH H 5 . ? -2.148 71.058 -26.164 1.00 35.97 ? 1219 HOH A O 1 HETATM 4573 O O . HOH H 5 . ? 1.020 74.545 5.692 1.00 38.77 ? 1220 HOH A O 1 HETATM 4574 O O . HOH H 5 . ? 11.061 79.229 -16.264 1.00 40.09 ? 1221 HOH A O 1 HETATM 4575 O O . HOH H 5 . ? 7.680 35.591 1.366 1.00 41.87 ? 1222 HOH A O 1 HETATM 4576 O O . HOH H 5 . ? 6.310 54.938 19.381 1.00 42.49 ? 1223 HOH A O 1 HETATM 4577 O O . HOH H 5 . ? 46.092 43.688 7.632 1.00 42.84 ? 1224 HOH A O 1 HETATM 4578 O O . HOH H 5 . ? 21.253 67.549 13.655 1.00 34.50 ? 1225 HOH A O 1 HETATM 4579 O O . HOH H 5 . ? 43.532 49.006 -4.133 1.00 21.60 ? 1226 HOH A O 1 HETATM 4580 O O . HOH H 5 . ? 22.611 60.812 -19.556 1.00 49.01 ? 1227 HOH A O 1 HETATM 4581 O O . HOH H 5 . ? 5.311 76.560 -19.401 1.00 41.07 ? 1228 HOH A O 1 HETATM 4582 O O . HOH H 5 . ? -13.003 69.602 -6.479 1.00 42.60 ? 1229 HOH A O 1 HETATM 4583 O O . HOH H 5 . ? 47.358 47.910 3.757 1.00 22.28 ? 1230 HOH A O 1 HETATM 4584 O O . HOH H 5 . ? 48.737 45.993 3.631 1.00 26.51 ? 1231 HOH A O 1 HETATM 4585 O O . HOH H 5 . ? 18.192 62.049 -28.603 1.00 37.39 ? 1232 HOH A O 1 HETATM 4586 O O . HOH H 5 . ? 29.865 73.017 -8.242 1.00 33.94 ? 1233 HOH A O 1 HETATM 4587 O O . HOH H 5 . ? 10.774 38.182 -1.744 1.00 33.96 ? 1234 HOH A O 1 HETATM 4588 O O . HOH H 5 . ? -11.604 66.712 4.556 1.00 34.37 ? 1235 HOH A O 1 HETATM 4589 O O . HOH H 5 . ? -15.969 48.969 0.162 1.00 28.61 ? 1236 HOH A O 1 HETATM 4590 O O . HOH H 5 . ? 15.748 69.606 0.918 1.00 39.57 ? 1237 HOH A O 1 HETATM 4591 O O . HOH H 5 . ? 15.005 48.877 13.120 1.00 30.25 ? 1238 HOH A O 1 HETATM 4592 O O . HOH H 5 . ? 41.900 62.221 -13.852 1.00 38.31 ? 1239 HOH A O 1 HETATM 4593 O O . HOH H 5 . ? 28.748 47.693 4.508 1.00 34.79 ? 1240 HOH A O 1 HETATM 4594 O O . HOH H 5 . ? 40.913 50.824 -5.879 1.00 41.90 ? 1241 HOH A O 1 HETATM 4595 O O . HOH H 5 . ? -5.965 57.719 10.937 1.00 33.02 ? 1242 HOH A O 1 HETATM 4596 O O . HOH H 5 . ? 14.237 46.267 29.682 1.00 30.24 ? 1243 HOH A O 1 HETATM 4597 O O . HOH H 5 . ? 1.044 46.398 -14.400 1.00 43.01 ? 1244 HOH A O 1 HETATM 4598 O O . HOH H 5 . ? 1.206 44.488 11.524 1.00 32.75 ? 1245 HOH A O 1 HETATM 4599 O O . HOH H 5 . ? 13.676 67.341 2.674 1.00 35.44 ? 1246 HOH A O 1 HETATM 4600 O O . HOH H 5 . ? 5.286 69.840 4.591 1.00 33.85 ? 1247 HOH A O 1 HETATM 4601 O O . HOH H 5 . ? 16.029 50.188 20.430 1.00 35.24 ? 1248 HOH A O 1 HETATM 4602 O O . HOH H 5 . ? 19.800 71.375 -1.099 1.00 38.11 ? 1249 HOH A O 1 HETATM 4603 O O . HOH H 5 . ? 45.104 48.018 6.219 1.00 35.63 ? 1250 HOH A O 1 HETATM 4604 O O . HOH H 5 . ? 6.777 39.394 6.806 1.00 34.95 ? 1251 HOH A O 1 HETATM 4605 O O . HOH H 5 . ? 8.072 66.687 -24.475 1.00 40.12 ? 1252 HOH A O 1 HETATM 4606 O O . HOH H 5 . ? 19.431 79.167 -15.197 1.00 38.69 ? 1253 HOH A O 1 HETATM 4607 O O . HOH H 5 . ? 12.105 40.358 -0.314 1.00 32.68 ? 1254 HOH A O 1 HETATM 4608 O O . HOH H 5 . ? 14.442 74.610 -3.751 1.00 34.11 ? 1255 HOH A O 1 HETATM 4609 O O . HOH H 5 . ? 21.987 68.052 18.364 1.00 31.29 ? 1256 HOH A O 1 HETATM 4610 O O . HOH H 5 . ? -4.062 58.847 17.826 1.00 41.62 ? 1257 HOH A O 1 HETATM 4611 O O . HOH H 5 . ? 35.671 75.131 0.380 1.00 47.88 ? 1258 HOH A O 1 HETATM 4612 O O . HOH H 5 . ? -9.966 75.855 7.721 1.00 37.61 ? 1259 HOH A O 1 HETATM 4613 O O . HOH H 5 . ? 21.758 72.122 -19.130 1.00 36.24 ? 1260 HOH A O 1 HETATM 4614 O O . HOH H 5 . ? 6.076 57.647 -33.936 1.00 47.13 ? 1261 HOH A O 1 HETATM 4615 O O . HOH H 5 . ? 17.107 41.793 3.276 1.00 34.05 ? 1262 HOH A O 1 HETATM 4616 O O . HOH H 5 . ? 6.839 42.310 -17.125 1.00 42.61 ? 1263 HOH A O 1 HETATM 4617 O O . HOH H 5 . ? -4.645 79.368 -19.386 1.00 41.77 ? 1264 HOH A O 1 HETATM 4618 O O . HOH H 5 . ? 28.240 79.165 -11.771 1.00 40.00 ? 1265 HOH A O 1 HETATM 4619 O O . HOH H 5 . ? 15.604 78.353 -5.427 1.00 50.60 ? 1266 HOH A O 1 HETATM 4620 O O . HOH H 5 . ? 11.685 55.496 14.959 1.00 36.37 ? 1267 HOH A O 1 HETATM 4621 O O . HOH H 5 . ? 9.999 79.009 -8.072 1.00 39.28 ? 1268 HOH A O 1 HETATM 4622 O O . HOH H 5 . ? 18.237 65.951 -26.467 1.00 50.76 ? 1269 HOH A O 1 HETATM 4623 O O . HOH H 5 . ? 10.087 52.710 -29.041 1.00 49.20 ? 1270 HOH A O 1 HETATM 4624 O O . HOH H 5 . ? 25.191 73.808 1.995 1.00 42.04 ? 1271 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 GLN 1 1 ? ? ? A . n A 1 2 GLN 2 2 2 GLN GLN A . n A 1 3 ILE 3 3 3 ILE ILE A . n A 1 4 GLU 4 4 4 GLU GLU A . n A 1 5 GLN 5 5 5 GLN GLN A . n A 1 6 PRO 6 6 6 PRO PRO A . n A 1 7 TYR 7 7 7 TYR TYR A . n A 1 8 ARG 8 8 8 ARG ARG A . n A 1 9 THR 9 9 9 THR THR A . n A 1 10 GLY 10 10 10 GLY GLY A . n A 1 11 TYR 11 11 11 TYR TYR A . n A 1 12 HIS 12 12 12 HIS HIS A . n A 1 13 PHE 13 13 13 PHE PHE A . n A 1 14 GLN 14 14 14 GLN GLN A . n A 1 15 PRO 15 15 15 PRO PRO A . n A 1 16 PRO 16 16 16 PRO PRO A . n A 1 17 SER 17 17 17 SER SER A . n A 1 18 ASN 18 18 18 ASN ASN A . n A 1 19 TRP 19 19 19 TRP TRP A . n A 1 20 MET 20 20 20 MET MET A . n A 1 21 ASN 21 21 21 ASN ASN A . n A 1 22 ASP 22 22 22 ASP ASP A . n A 1 23 PRO 23 23 23 PRO PRO A . n A 1 24 ASN 24 24 24 ASN ASN A . n A 1 25 GLY 25 25 25 GLY GLY A . n A 1 26 PRO 26 26 26 PRO PRO A . n A 1 27 MET 27 27 27 MET MET A . n A 1 28 LEU 28 28 28 LEU LEU A . n A 1 29 TYR 29 29 29 TYR TYR A . n A 1 30 GLN 30 30 30 GLN GLN A . n A 1 31 GLY 31 31 31 GLY GLY A . n A 1 32 VAL 32 32 32 VAL VAL A . n A 1 33 TYR 33 33 33 TYR TYR A . n A 1 34 HIS 34 34 34 HIS HIS A . n A 1 35 PHE 35 35 35 PHE PHE A . n A 1 36 PHE 36 36 36 PHE PHE A . n A 1 37 TYR 37 37 37 TYR TYR A . n A 1 38 GLN 38 38 38 GLN GLN A . n A 1 39 TYR 39 39 39 TYR TYR A . n A 1 40 ASN 40 40 40 ASN ASN A . n A 1 41 PRO 41 41 41 PRO PRO A . n A 1 42 TYR 42 42 42 TYR TYR A . n A 1 43 ALA 43 43 43 ALA ALA A . n A 1 44 ALA 44 44 44 ALA ALA A . n A 1 45 THR 45 45 45 THR THR A . n A 1 46 PHE 46 46 46 PHE PHE A . n A 1 47 GLY 47 47 47 GLY GLY A . n A 1 48 ASP 48 48 48 ASP ASP A . n A 1 49 VAL 49 49 49 VAL VAL A . n A 1 50 ILE 50 50 50 ILE ILE A . n A 1 51 ILE 51 51 51 ILE ILE A . n A 1 52 TRP 52 52 52 TRP TRP A . n A 1 53 GLY 53 53 53 GLY GLY A . n A 1 54 HIS 54 54 54 HIS HIS A . n A 1 55 ALA 55 55 55 ALA ALA A . n A 1 56 VAL 56 56 56 VAL VAL A . n A 1 57 SER 57 57 57 SER SER A . n A 1 58 TYR 58 58 58 TYR TYR A . n A 1 59 ASP 59 59 59 ASP ASP A . n A 1 60 LEU 60 60 60 LEU LEU A . n A 1 61 VAL 61 61 61 VAL VAL A . n A 1 62 ASN 62 62 62 ASN ASN A . n A 1 63 TRP 63 63 63 TRP TRP A . n A 1 64 ILE 64 64 64 ILE ILE A . n A 1 65 HIS 65 65 65 HIS HIS A . n A 1 66 LEU 66 66 66 LEU LEU A . n A 1 67 ASP 67 67 67 ASP ASP A . n A 1 68 PRO 68 68 68 PRO PRO A . n A 1 69 ALA 69 69 69 ALA ALA A . n A 1 70 ILE 70 70 70 ILE ILE A . n A 1 71 TYR 71 71 71 TYR TYR A . n A 1 72 PRO 72 72 72 PRO PRO A . n A 1 73 THR 73 73 73 THR THR A . n A 1 74 GLN 74 74 74 GLN GLN A . n A 1 75 GLU 75 75 75 GLU GLU A . n A 1 76 ALA 76 76 76 ALA ALA A . n A 1 77 ASP 77 77 77 ASP ASP A . n A 1 78 SER 78 78 78 SER SER A . n A 1 79 LYS 79 79 79 LYS LYS A . n A 1 80 SER 80 80 80 SER SER A . n A 1 81 CYS 81 81 81 CYS CYS A . n A 1 82 TRP 82 82 82 TRP TRP A . n A 1 83 SER 83 83 83 SER SER A . n A 1 84 GLY 84 84 84 GLY GLY A . n A 1 85 SER 85 85 85 SER SER A . n A 1 86 ALA 86 86 86 ALA ALA A . n A 1 87 THR 87 87 87 THR THR A . n A 1 88 ILE 88 88 88 ILE ILE A . n A 1 89 LEU 89 89 89 LEU LEU A . n A 1 90 PRO 90 90 90 PRO PRO A . n A 1 91 GLY 91 91 91 GLY GLY A . n A 1 92 ASN 92 92 92 ASN ASN A . n A 1 93 ILE 93 93 93 ILE ILE A . n A 1 94 PRO 94 94 94 PRO PRO A . n A 1 95 ALA 95 95 95 ALA ALA A . n A 1 96 MET 96 96 96 MET MET A . n A 1 97 LEU 97 97 97 LEU LEU A . n A 1 98 TYR 98 98 98 TYR TYR A . n A 1 99 THR 99 99 99 THR THR A . n A 1 100 GLY 100 100 100 GLY GLY A . n A 1 101 SER 101 101 101 SER SER A . n A 1 102 ASP 102 102 102 ASP ASP A . n A 1 103 SER 103 103 103 SER SER A . n A 1 104 LYS 104 104 104 LYS LYS A . n A 1 105 SER 105 105 105 SER SER A . n A 1 106 ARG 106 106 106 ARG ARG A . n A 1 107 GLN 107 107 107 GLN GLN A . n A 1 108 VAL 108 108 108 VAL VAL A . n A 1 109 GLN 109 109 109 GLN GLN 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 ALA 112 112 112 ALA ALA A . n A 1 113 TRP 113 113 113 TRP TRP A . n A 1 114 PRO 114 114 114 PRO PRO A . n A 1 115 LYS 115 115 115 LYS LYS A . n A 1 116 ASN 116 116 116 ASN ASN A . n A 1 117 LEU 117 117 117 LEU LEU A . n A 1 118 SER 118 118 118 SER SER A . n A 1 119 ASP 119 119 119 ASP ASP A . n A 1 120 PRO 120 120 120 PRO PRO A . n A 1 121 PHE 121 121 121 PHE PHE A . n A 1 122 LEU 122 122 122 LEU LEU A . n A 1 123 ARG 123 123 123 ARG ARG A . n A 1 124 GLU 124 124 124 GLU GLU A . n A 1 125 TRP 125 125 125 TRP TRP A . n A 1 126 VAL 126 126 126 VAL VAL A . n A 1 127 LYS 127 127 127 LYS LYS A . n A 1 128 HIS 128 128 128 HIS HIS A . n A 1 129 PRO 129 129 129 PRO PRO A . n A 1 130 LYS 130 130 130 LYS LYS A . n A 1 131 ASN 131 131 131 ASN ASN A . n A 1 132 PRO 132 132 132 PRO PRO A . n A 1 133 LEU 133 133 133 LEU LEU A . n A 1 134 ILE 134 134 134 ILE ILE A . n A 1 135 THR 135 135 135 THR THR A . n A 1 136 PRO 136 136 136 PRO PRO A . n A 1 137 PRO 137 137 137 PRO PRO A . n A 1 138 GLU 138 138 138 GLU GLU A . n A 1 139 GLY 139 139 139 GLY GLY A . n A 1 140 VAL 140 140 140 VAL VAL A . n A 1 141 LYS 141 141 141 LYS LYS A . n A 1 142 ASP 142 142 142 ASP ASP A . n A 1 143 ASP 143 143 143 ASP ASP A . n A 1 144 CYS 144 144 144 CYS CYS A . n A 1 145 PHE 145 145 145 PHE PHE A . n A 1 146 ARG 146 146 146 ARG ARG A . n A 1 147 ASP 147 147 147 ASP ASP A . n A 1 148 PRO 148 148 148 PRO PRO A . n A 1 149 SER 149 149 149 SER SER A . n A 1 150 THR 150 150 150 THR THR A . n A 1 151 ALA 151 151 151 ALA ALA A . n A 1 152 TRP 152 152 152 TRP TRP A . n A 1 153 LEU 153 153 153 LEU LEU A . n A 1 154 GLY 154 154 154 GLY GLY A . n A 1 155 PRO 155 155 155 PRO PRO A . n A 1 156 ASP 156 156 156 ASP ASP A . n A 1 157 GLY 157 157 157 GLY GLY A . n A 1 158 VAL 158 158 158 VAL VAL A . n A 1 159 TRP 159 159 159 TRP TRP A . n A 1 160 ARG 160 160 160 ARG ARG A . n A 1 161 ILE 161 161 161 ILE ILE A . n A 1 162 VAL 162 162 162 VAL VAL A . n A 1 163 VAL 163 163 163 VAL VAL A . n A 1 164 GLY 164 164 164 GLY GLY A . n A 1 165 GLY 165 165 165 GLY GLY A . n A 1 166 ASP 166 166 166 ASP ASP A . n A 1 167 ARG 167 167 167 ARG ARG A . n A 1 168 ASP 168 168 168 ASP ASP A . n A 1 169 ASN 169 169 169 ASN ASN A . n A 1 170 ASN 170 170 170 ASN ASN A . n A 1 171 GLY 171 171 171 GLY GLY A . n A 1 172 MET 172 172 172 MET MET A . n A 1 173 ALA 173 173 173 ALA ALA A . n A 1 174 PHE 174 174 174 PHE PHE A . n A 1 175 LEU 175 175 175 LEU LEU A . n A 1 176 TYR 176 176 176 TYR TYR A . n A 1 177 GLN 177 177 177 GLN GLN A . n A 1 178 SER 178 178 178 SER SER A . n A 1 179 THR 179 179 179 THR THR A . n A 1 180 ASP 180 180 180 ASP ASP A . n A 1 181 PHE 181 181 181 PHE PHE A . n A 1 182 VAL 182 182 182 VAL VAL A . n A 1 183 ASN 183 183 183 ASN ASN A . n A 1 184 TRP 184 184 184 TRP TRP A . n A 1 185 LYS 185 185 185 LYS LYS A . n A 1 186 ARG 186 186 186 ARG ARG A . n A 1 187 TYR 187 187 187 TYR TYR A . n A 1 188 ASP 188 188 188 ASP ASP A . n A 1 189 GLN 189 189 189 GLN GLN A . n A 1 190 PRO 190 190 190 PRO PRO A . n A 1 191 LEU 191 191 191 LEU LEU A . n A 1 192 SER 192 192 192 SER SER A . n A 1 193 SER 193 193 193 SER SER A . n A 1 194 ALA 194 194 194 ALA ALA A . n A 1 195 ASP 195 195 195 ASP ASP A . n A 1 196 ALA 196 196 196 ALA ALA A . n A 1 197 THR 197 197 197 THR THR A . n A 1 198 GLY 198 198 198 GLY GLY A . n A 1 199 THR 199 199 199 THR THR A . n A 1 200 TRP 200 200 200 TRP TRP A . n A 1 201 GLU 201 201 201 GLU GLU A . n A 1 202 CYS 202 202 202 CYS CYS A . n A 1 203 PRO 203 203 203 PRO PRO A . n A 1 204 ASP 204 204 204 ASP ASP A . n A 1 205 PHE 205 205 205 PHE PHE A . n A 1 206 TYR 206 206 206 TYR TYR A . n A 1 207 PRO 207 207 207 PRO PRO A . n A 1 208 VAL 208 208 208 VAL VAL 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 ASN 211 211 211 ASN ASN A . n A 1 212 SER 212 212 212 SER SER A . n A 1 213 THR 213 213 213 THR THR A . n A 1 214 ASN 214 214 214 ASN ASN A . n A 1 215 GLY 215 215 215 GLY GLY A . n A 1 216 LEU 216 216 216 LEU LEU A . n A 1 217 ASP 217 217 217 ASP ASP A . n A 1 218 THR 218 218 218 THR THR A . n A 1 219 SER 219 219 219 SER SER A . n A 1 220 VAL 220 220 220 VAL VAL A . n A 1 221 TYR 221 221 221 TYR TYR A . n A 1 222 GLY 222 222 222 GLY GLY A . n A 1 223 GLY 223 223 223 GLY GLY A . n A 1 224 SER 224 224 224 SER SER A . n A 1 225 VAL 225 225 225 VAL VAL A . n A 1 226 ARG 226 226 226 ARG ARG A . n A 1 227 HIS 227 227 227 HIS HIS A . n A 1 228 VAL 228 228 228 VAL VAL A . n A 1 229 MET 229 229 229 MET MET A . n A 1 230 LYS 230 230 230 LYS LYS A . n A 1 231 ALA 231 231 231 ALA ALA A . n A 1 232 GLY 232 232 232 GLY GLY A . n A 1 233 PHE 233 233 233 PHE PHE A . n A 1 234 GLU 234 234 234 GLU GLU A . n A 1 235 GLY 235 235 235 GLY GLY A . n A 1 236 HIS 236 236 236 HIS HIS A . n A 1 237 ASP 237 237 237 ASP ASP A . n A 1 238 TRP 238 238 238 TRP TRP A . n A 1 239 TYR 239 239 239 TYR TYR A . n A 1 240 THR 240 240 240 THR THR A . n A 1 241 ILE 241 241 241 ILE ILE A . n A 1 242 GLY 242 242 242 GLY GLY A . n A 1 243 THR 243 243 243 THR THR A . n A 1 244 TYR 244 244 244 TYR TYR A . n A 1 245 SER 245 245 245 SER SER A . n A 1 246 PRO 246 246 246 PRO PRO A . n A 1 247 ASP 247 247 247 ASP ASP A . n A 1 248 ARG 248 248 248 ARG ARG A . n A 1 249 GLU 249 249 249 GLU GLU A . n A 1 250 ASN 250 250 250 ASN ASN A . n A 1 251 PHE 251 251 251 PHE PHE A . n A 1 252 LEU 252 252 252 LEU LEU A . n A 1 253 PRO 253 253 253 PRO PRO A . n A 1 254 GLN 254 254 254 GLN GLN A . n A 1 255 ASN 255 255 255 ASN ASN A . n A 1 256 GLY 256 256 256 GLY GLY A . n A 1 257 LEU 257 257 257 LEU LEU A . n A 1 258 SER 258 258 258 SER SER A . n A 1 259 LEU 259 259 259 LEU LEU A . n A 1 260 THR 260 260 260 THR THR A . n A 1 261 GLY 261 261 261 GLY GLY A . n A 1 262 SER 262 262 262 SER SER A . n A 1 263 THR 263 263 263 THR THR A . n A 1 264 LEU 264 264 264 LEU LEU A . n A 1 265 ASP 265 265 265 ASP ASP A . n A 1 266 LEU 266 266 266 LEU LEU A . n A 1 267 ARG 267 267 267 ARG ARG A . n A 1 268 TYR 268 268 268 TYR TYR A . n A 1 269 ASP 269 269 269 ASP ASP A . n A 1 270 TYR 270 270 270 TYR TYR A . n A 1 271 GLY 271 271 271 GLY GLY A . n A 1 272 GLN 272 272 272 GLN GLN A . n A 1 273 PHE 273 273 273 PHE PHE A . n A 1 274 TYR 274 274 274 TYR TYR A . n A 1 275 ALA 275 275 275 ALA ALA A . n A 1 276 SER 276 276 276 SER SER A . n A 1 277 LYS 277 277 277 LYS LYS A . n A 1 278 SER 278 278 278 SER SER A . n A 1 279 PHE 279 279 279 PHE PHE A . n A 1 280 PHE 280 280 280 PHE PHE A . n A 1 281 ASP 281 281 281 ASP ASP A . n A 1 282 ASP 282 282 282 ASP ASP A . n A 1 283 ALA 283 283 283 ALA ALA A . n A 1 284 LYS 284 284 284 LYS LYS A . n A 1 285 ASN 285 285 285 ASN ASN A . n A 1 286 ARG 286 286 286 ARG ARG A . n A 1 287 ARG 287 287 287 ARG ARG A . n A 1 288 VAL 288 288 288 VAL VAL A . n A 1 289 LEU 289 289 289 LEU LEU A . n A 1 290 TRP 290 290 290 TRP TRP A . n A 1 291 ALA 291 291 291 ALA ALA A . n A 1 292 TRP 292 292 292 TRP TRP A . n A 1 293 VAL 293 293 293 VAL VAL A . n A 1 294 PRO 294 294 294 PRO PRO A . n A 1 295 GLU 295 295 295 GLU GLU A . n A 1 296 THR 296 296 296 THR THR A . n A 1 297 ASP 297 297 297 ASP ASP A . n A 1 298 SER 298 298 298 SER SER A . n A 1 299 GLN 299 299 299 GLN GLN A . n A 1 300 ALA 300 300 300 ALA ALA A . n A 1 301 ASP 301 301 301 ASP ASP A . n A 1 302 ASP 302 302 302 ASP ASP A . n A 1 303 ILE 303 303 303 ILE ILE A . n A 1 304 GLU 304 304 304 GLU GLU A . n A 1 305 LYS 305 305 305 LYS LYS A . n A 1 306 GLY 306 306 306 GLY GLY A . n A 1 307 TRP 307 307 307 TRP TRP A . n A 1 308 ALA 308 308 308 ALA ALA A . n A 1 309 GLY 309 309 309 GLY GLY A . n A 1 310 LEU 310 310 310 LEU LEU A . n A 1 311 GLN 311 311 311 GLN GLN A . n A 1 312 SER 312 312 312 SER SER A . n A 1 313 PHE 313 313 313 PHE PHE A . n A 1 314 PRO 314 314 314 PRO PRO A . n A 1 315 ARG 315 315 315 ARG ARG A . n A 1 316 ALA 316 316 316 ALA ALA A . n A 1 317 LEU 317 317 317 LEU LEU A . n A 1 318 TRP 318 318 318 TRP TRP A . n A 1 319 ILE 319 319 319 ILE ILE A . n A 1 320 ASP 320 320 320 ASP ASP A . n A 1 321 ARG 321 321 321 ARG ARG A . n A 1 322 ASN 322 322 322 ASN ASN A . n A 1 323 GLY 323 323 323 GLY GLY A . n A 1 324 LYS 324 324 324 LYS LYS A . n A 1 325 GLN 325 325 325 GLN GLN A . n A 1 326 LEU 326 326 326 LEU LEU A . n A 1 327 ILE 327 327 327 ILE ILE A . n A 1 328 GLN 328 328 328 GLN GLN A . n A 1 329 TRP 329 329 329 TRP TRP A . n A 1 330 PRO 330 330 330 PRO PRO A . n A 1 331 VAL 331 331 331 VAL VAL A . n A 1 332 GLU 332 332 332 GLU GLU A . n A 1 333 GLU 333 333 333 GLU GLU A . n A 1 334 ILE 334 334 334 ILE ILE A . n A 1 335 GLU 335 335 335 GLU GLU A . n A 1 336 GLU 336 336 336 GLU GLU A . n A 1 337 LEU 337 337 337 LEU LEU A . n A 1 338 ARG 338 338 338 ARG ARG A . n A 1 339 GLN 339 339 339 GLN GLN A . n A 1 340 ASN 340 340 340 ASN ASN A . n A 1 341 GLN 341 341 341 GLN GLN A . n A 1 342 VAL 342 342 342 VAL VAL A . n A 1 343 ASN 343 343 343 ASN ASN A . n A 1 344 LEU 344 344 344 LEU LEU A . n A 1 345 GLN 345 345 345 GLN GLN A . n A 1 346 ASN 346 346 346 ASN ASN A . n A 1 347 LYS 347 347 347 LYS LYS A . n A 1 348 ASN 348 348 348 ASN ASN A . n A 1 349 LEU 349 349 349 LEU LEU A . n A 1 350 LYS 350 350 350 LYS LYS A . n A 1 351 PRO 351 351 351 PRO PRO A . n A 1 352 GLY 352 352 352 GLY GLY A . n A 1 353 SER 353 353 353 SER SER A . n A 1 354 VAL 354 354 354 VAL VAL A . n A 1 355 LEU 355 355 355 LEU LEU A . n A 1 356 GLU 356 356 356 GLU GLU A . n A 1 357 ILE 357 357 357 ILE ILE A . n A 1 358 HIS 358 358 358 HIS HIS A . n A 1 359 GLY 359 359 359 GLY GLY A . n A 1 360 ILE 360 360 360 ILE ILE A . n A 1 361 ALA 361 361 361 ALA ALA A . n A 1 362 ALA 362 362 362 ALA ALA A . n A 1 363 SER 363 363 363 SER SER A . n A 1 364 GLN 364 364 364 GLN GLN A . n A 1 365 ALA 365 365 365 ALA ALA A . n A 1 366 ASP 366 366 366 ASP ASP A . n A 1 367 VAL 367 367 367 VAL VAL A . n A 1 368 THR 368 368 368 THR THR A . n A 1 369 ILE 369 369 369 ILE ILE A . n A 1 370 SER 370 370 370 SER SER A . n A 1 371 PHE 371 371 371 PHE PHE A . n A 1 372 LYS 372 372 372 LYS LYS A . n A 1 373 LEU 373 373 373 LEU LEU A . n A 1 374 GLU 374 374 374 GLU GLU A . n A 1 375 GLY 375 375 375 GLY GLY A . n A 1 376 LEU 376 376 376 LEU LEU A . n A 1 377 LYS 377 377 377 LYS LYS A . n A 1 378 GLU 378 378 378 GLU GLU A . n A 1 379 ALA 379 379 379 ALA ALA A . n A 1 380 GLU 380 380 380 GLU GLU A . n A 1 381 VAL 381 381 381 VAL VAL A . n A 1 382 LEU 382 382 382 LEU LEU A . n A 1 383 ASP 383 383 383 ASP ASP A . n A 1 384 THR 384 384 384 THR THR A . n A 1 385 THR 385 385 385 THR THR A . n A 1 386 LEU 386 386 386 LEU LEU A . n A 1 387 VAL 387 387 387 VAL VAL A . n A 1 388 ASP 388 388 388 ASP ASP A . n A 1 389 PRO 389 389 389 PRO PRO A . n A 1 390 GLN 390 390 390 GLN GLN A . n A 1 391 ALA 391 391 391 ALA ALA A . n A 1 392 LEU 392 392 392 LEU LEU A . n A 1 393 CYS 393 393 393 CYS CYS A . n A 1 394 ASN 394 394 394 ASN ASN A . n A 1 395 GLU 395 395 395 GLU GLU A . n A 1 396 ARG 396 396 396 ARG ARG A . n A 1 397 GLY 397 397 397 GLY GLY A . n A 1 398 ALA 398 398 398 ALA ALA A . n A 1 399 SER 399 399 399 SER SER A . n A 1 400 SER 400 400 400 SER SER A . n A 1 401 ARG 401 401 401 ARG ARG A . n A 1 402 GLY 402 402 402 GLY GLY A . n A 1 403 ALA 403 403 403 ALA ALA A . n A 1 404 LEU 404 404 404 LEU LEU A . n A 1 405 GLY 405 405 405 GLY GLY A . n A 1 406 PRO 406 406 406 PRO PRO A . n A 1 407 PHE 407 407 407 PHE PHE A . n A 1 408 GLY 408 408 408 GLY GLY A . n A 1 409 LEU 409 409 409 LEU LEU A . n A 1 410 LEU 410 410 410 LEU LEU A . n A 1 411 ALA 411 411 411 ALA ALA A . n A 1 412 MET 412 412 412 MET MET A . n A 1 413 ALA 413 413 413 ALA ALA A . n A 1 414 SER 414 414 414 SER SER A . n A 1 415 LYS 415 415 415 LYS LYS A . n A 1 416 ASP 416 416 416 ASP ASP A . n A 1 417 LEU 417 417 417 LEU LEU A . n A 1 418 LYS 418 418 418 LYS LYS A . n A 1 419 GLU 419 419 419 GLU GLU A . n A 1 420 GLN 420 420 420 GLN GLN A . n A 1 421 SER 421 421 421 SER SER A . n A 1 422 ALA 422 422 422 ALA ALA A . n A 1 423 ILE 423 423 423 ILE ILE A . n A 1 424 PHE 424 424 424 PHE PHE A . n A 1 425 PHE 425 425 425 PHE PHE A . n A 1 426 ARG 426 426 426 ARG ARG A . n A 1 427 VAL 427 427 427 VAL VAL A . n A 1 428 PHE 428 428 428 PHE PHE A . n A 1 429 GLN 429 429 429 GLN GLN A . n A 1 430 ASN 430 430 430 ASN ASN A . n A 1 431 GLN 431 431 431 GLN GLN A . n A 1 432 LEU 432 432 432 LEU LEU A . n A 1 433 GLY 433 433 433 GLY GLY A . n A 1 434 ARG 434 434 434 ARG ARG A . n A 1 435 TYR 435 435 435 TYR TYR A . n A 1 436 SER 436 436 436 SER SER A . n A 1 437 VAL 437 437 437 VAL VAL A . n A 1 438 LEU 438 438 438 LEU LEU A . n A 1 439 MET 439 439 439 MET MET A . n A 1 440 CYS 440 440 440 CYS CYS A . n A 1 441 SER 441 441 441 SER SER A . n A 1 442 ASP 442 442 442 ASP ASP A . n A 1 443 LEU 443 443 443 LEU LEU A . n A 1 444 SER 444 444 444 SER SER A . n A 1 445 ARG 445 445 445 ARG ARG A . n A 1 446 SER 446 446 446 SER SER A . n A 1 447 THR 447 447 447 THR THR A . n A 1 448 VAL 448 448 448 VAL VAL A . n A 1 449 ARG 449 449 449 ARG ARG A . n A 1 450 SER 450 450 450 SER SER A . n A 1 451 ASN 451 451 451 ASN ASN A . n A 1 452 ILE 452 452 452 ILE ILE A . n A 1 453 ASP 453 453 453 ASP ASP A . n A 1 454 THR 454 454 454 THR THR A . n A 1 455 THR 455 455 455 THR THR A . n A 1 456 SER 456 456 456 SER SER A . n A 1 457 TYR 457 457 457 TYR TYR A . n A 1 458 GLY 458 458 458 GLY GLY A . n A 1 459 ALA 459 459 459 ALA ALA A . n A 1 460 PHE 460 460 460 PHE PHE A . n A 1 461 VAL 461 461 461 VAL VAL A . n A 1 462 ASP 462 462 462 ASP ASP A . n A 1 463 ILE 463 463 463 ILE ILE A . n A 1 464 ASP 464 464 464 ASP ASP A . n A 1 465 PRO 465 465 465 PRO PRO A . n A 1 466 ARG 466 466 466 ARG ARG A . n A 1 467 SER 467 467 467 SER SER A . n A 1 468 GLU 468 468 468 GLU GLU A . n A 1 469 GLU 469 469 469 GLU GLU A . n A 1 470 ILE 470 470 470 ILE ILE A . n A 1 471 SER 471 471 471 SER SER A . n A 1 472 LEU 472 472 472 LEU LEU A . n A 1 473 ARG 473 473 473 ARG ARG A . n A 1 474 ASN 474 474 474 ASN ASN A . n A 1 475 LEU 475 475 475 LEU LEU A . n A 1 476 ILE 476 476 476 ILE ILE A . n A 1 477 ASP 477 477 477 ASP ASP A . n A 1 478 HIS 478 478 478 HIS HIS A . n A 1 479 SER 479 479 479 SER SER A . n A 1 480 ILE 480 480 480 ILE ILE A . n A 1 481 ILE 481 481 481 ILE ILE A . n A 1 482 GLU 482 482 482 GLU GLU A . n A 1 483 SER 483 483 483 SER SER A . n A 1 484 PHE 484 484 484 PHE PHE A . n A 1 485 GLY 485 485 485 GLY GLY A . n A 1 486 ALA 486 486 486 ALA ALA A . n A 1 487 GLY 487 487 487 GLY GLY A . n A 1 488 GLY 488 488 488 GLY GLY A . n A 1 489 LYS 489 489 489 LYS LYS A . n A 1 490 THR 490 490 490 THR THR A . n A 1 491 CYS 491 491 491 CYS CYS A . n A 1 492 ILE 492 492 492 ILE ILE A . n A 1 493 THR 493 493 493 THR THR A . n A 1 494 SER 494 494 494 SER SER A . n A 1 495 ARG 495 495 495 ARG ARG A . n A 1 496 ILE 496 496 496 ILE ILE A . n A 1 497 TYR 497 497 497 TYR TYR A . n A 1 498 PRO 498 498 498 PRO PRO A . n A 1 499 LYS 499 499 499 LYS LYS A . n A 1 500 PHE 500 500 500 PHE PHE A . n A 1 501 VAL 501 501 501 VAL VAL A . n A 1 502 ASN 502 502 502 ASN ASN A . n A 1 503 ASN 503 503 503 ASN ASN A . n A 1 504 GLU 504 504 504 GLU GLU A . n A 1 505 GLU 505 505 505 GLU GLU A . n A 1 506 ALA 506 506 506 ALA ALA A . n A 1 507 HIS 507 507 507 HIS HIS A . n A 1 508 LEU 508 508 508 LEU LEU A . n A 1 509 PHE 509 509 509 PHE PHE A . n A 1 510 VAL 510 510 510 VAL VAL A . n A 1 511 PHE 511 511 511 PHE PHE A . n A 1 512 ASN 512 512 512 ASN ASN A . n A 1 513 ASN 513 513 513 ASN ASN A . n A 1 514 GLY 514 514 514 GLY GLY A . n A 1 515 THR 515 515 515 THR THR A . n A 1 516 GLN 516 516 516 GLN GLN A . n A 1 517 ASN 517 517 517 ASN ASN A . n A 1 518 VAL 518 518 518 VAL VAL A . n A 1 519 LYS 519 519 519 LYS LYS A . n A 1 520 ILE 520 520 520 ILE ILE A . n A 1 521 SER 521 521 521 SER SER A . n A 1 522 GLU 522 522 522 GLU GLU A . n A 1 523 MET 523 523 523 MET MET A . n A 1 524 SER 524 524 524 SER SER A . n A 1 525 ALA 525 525 525 ALA ALA A . n A 1 526 TRP 526 526 526 TRP TRP A . n A 1 527 SER 527 527 527 SER SER A . n A 1 528 MET 528 528 528 MET MET A . n A 1 529 LYS 529 529 529 LYS LYS A . n A 1 530 ASN 530 530 530 ASN ASN A . n A 1 531 ALA 531 531 531 ALA ALA A . n A 1 532 LYS 532 532 532 LYS LYS A . n A 1 533 PHE 533 533 533 PHE PHE A . n A 1 534 VAL 534 534 534 VAL VAL A . n A 1 535 VAL 535 535 535 VAL VAL A . n A 1 536 ASP 536 536 536 ASP ASP A . n A 1 537 GLN 537 537 537 GLN GLN A . n A 1 538 SER 538 538 538 SER SER A . n A 1 539 VAL 539 539 ? ? ? A . n A 1 540 LYS 540 540 ? ? ? A . n A 1 541 SER 541 541 ? ? ? A . n A 1 542 ALA 542 542 ? ? ? A . n A 1 543 ALA 543 543 ? ? ? A . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 NAG 1 650 650 NAG NAG A . C 2 NAG 2 660 660 NAG NAG A . D 3 MAN 3 670 670 MAN MAN A . E 2 NAG 1 680 680 NAG NAG A . F 2 NAG 2 690 690 NAG NAG A . G 4 FRU 1 800 800 FRU FRU A . H 5 HOH 1 1001 1001 HOH TIP A . H 5 HOH 2 1002 1002 HOH TIP A . H 5 HOH 3 1003 1003 HOH TIP A . H 5 HOH 4 1004 1004 HOH TIP A . H 5 HOH 5 1005 1005 HOH TIP A . H 5 HOH 6 1006 1006 HOH TIP A . H 5 HOH 7 1007 1007 HOH TIP A . H 5 HOH 8 1008 1008 HOH TIP A . H 5 HOH 9 1009 1009 HOH TIP A . H 5 HOH 10 1010 1010 HOH TIP A . H 5 HOH 11 1011 1011 HOH TIP A . H 5 HOH 12 1012 1012 HOH TIP A . H 5 HOH 13 1013 1013 HOH TIP A . H 5 HOH 14 1014 1014 HOH TIP A . H 5 HOH 15 1015 1015 HOH TIP A . H 5 HOH 16 1016 1016 HOH TIP A . H 5 HOH 17 1017 1017 HOH TIP A . H 5 HOH 18 1018 1018 HOH TIP A . H 5 HOH 19 1019 1019 HOH TIP A . H 5 HOH 20 1020 1020 HOH TIP A . H 5 HOH 21 1021 1021 HOH TIP A . H 5 HOH 22 1022 1022 HOH TIP A . H 5 HOH 23 1023 1023 HOH TIP A . H 5 HOH 24 1024 1024 HOH TIP A . H 5 HOH 25 1025 1025 HOH TIP A . H 5 HOH 26 1026 1026 HOH TIP A . H 5 HOH 27 1027 1027 HOH TIP A . H 5 HOH 28 1028 1028 HOH TIP A . H 5 HOH 29 1029 1029 HOH TIP A . H 5 HOH 30 1030 1030 HOH TIP A . H 5 HOH 31 1031 1031 HOH TIP A . H 5 HOH 32 1032 1032 HOH TIP A . H 5 HOH 33 1033 1033 HOH TIP A . H 5 HOH 34 1034 1034 HOH TIP A . H 5 HOH 35 1035 1035 HOH TIP A . H 5 HOH 36 1036 1036 HOH TIP A . H 5 HOH 37 1037 1037 HOH TIP A . H 5 HOH 38 1038 1038 HOH TIP A . H 5 HOH 39 1039 1039 HOH TIP A . H 5 HOH 40 1040 1040 HOH TIP A . H 5 HOH 41 1041 1041 HOH TIP A . H 5 HOH 42 1042 1042 HOH TIP A . H 5 HOH 43 1043 1043 HOH TIP A . H 5 HOH 44 1044 1044 HOH TIP A . H 5 HOH 45 1045 1045 HOH TIP A . H 5 HOH 46 1046 1046 HOH TIP A . H 5 HOH 47 1047 1047 HOH TIP A . H 5 HOH 48 1048 1048 HOH TIP A . H 5 HOH 49 1049 1049 HOH TIP A . H 5 HOH 50 1050 1050 HOH TIP A . H 5 HOH 51 1051 1051 HOH TIP A . H 5 HOH 52 1052 1052 HOH TIP A . H 5 HOH 53 1053 1053 HOH TIP A . H 5 HOH 54 1054 1054 HOH TIP A . H 5 HOH 55 1055 1055 HOH TIP A . H 5 HOH 56 1056 1056 HOH TIP A . H 5 HOH 57 1057 1057 HOH TIP A . H 5 HOH 58 1058 1058 HOH TIP A . H 5 HOH 59 1059 1059 HOH TIP A . H 5 HOH 60 1060 1060 HOH TIP A . H 5 HOH 61 1061 1061 HOH TIP A . H 5 HOH 62 1062 1062 HOH TIP A . H 5 HOH 63 1063 1063 HOH TIP A . H 5 HOH 64 1064 1064 HOH TIP A . H 5 HOH 65 1065 1065 HOH TIP A . H 5 HOH 66 1066 1066 HOH TIP A . H 5 HOH 67 1067 1067 HOH TIP A . H 5 HOH 68 1068 1068 HOH TIP A . H 5 HOH 69 1069 1069 HOH TIP A . H 5 HOH 70 1070 1070 HOH TIP A . H 5 HOH 71 1071 1071 HOH TIP A . H 5 HOH 72 1072 1072 HOH TIP A . H 5 HOH 73 1073 1073 HOH TIP A . H 5 HOH 74 1074 1074 HOH TIP A . H 5 HOH 75 1075 1075 HOH TIP A . H 5 HOH 76 1076 1076 HOH TIP A . H 5 HOH 77 1077 1077 HOH TIP A . H 5 HOH 78 1078 1078 HOH TIP A . H 5 HOH 79 1079 1079 HOH TIP A . H 5 HOH 80 1080 1080 HOH TIP A . H 5 HOH 81 1081 1081 HOH TIP A . H 5 HOH 82 1082 1082 HOH TIP A . H 5 HOH 83 1083 1083 HOH TIP A . H 5 HOH 84 1084 1084 HOH TIP A . H 5 HOH 85 1085 1085 HOH TIP A . H 5 HOH 86 1086 1086 HOH TIP A . H 5 HOH 87 1087 1087 HOH TIP A . H 5 HOH 88 1088 1088 HOH TIP A . H 5 HOH 89 1089 1089 HOH TIP A . H 5 HOH 90 1090 1090 HOH TIP A . H 5 HOH 91 1091 1091 HOH TIP A . H 5 HOH 92 1092 1092 HOH TIP A . H 5 HOH 93 1093 1093 HOH TIP A . H 5 HOH 94 1094 1094 HOH TIP A . H 5 HOH 95 1095 1095 HOH TIP A . H 5 HOH 96 1096 1096 HOH TIP A . H 5 HOH 97 1097 1097 HOH TIP A . H 5 HOH 98 1098 1098 HOH TIP A . H 5 HOH 99 1099 1099 HOH TIP A . H 5 HOH 100 1100 1100 HOH TIP A . H 5 HOH 101 1101 1101 HOH TIP A . H 5 HOH 102 1102 1102 HOH TIP A . H 5 HOH 103 1103 1103 HOH TIP A . H 5 HOH 104 1104 1104 HOH TIP A . H 5 HOH 105 1105 1105 HOH TIP A . H 5 HOH 106 1106 1106 HOH TIP A . H 5 HOH 107 1107 1107 HOH TIP A . H 5 HOH 108 1108 1108 HOH TIP A . H 5 HOH 109 1109 1109 HOH TIP A . H 5 HOH 110 1110 1110 HOH TIP A . H 5 HOH 111 1111 1111 HOH TIP A . H 5 HOH 112 1112 1112 HOH TIP A . H 5 HOH 113 1113 1113 HOH TIP A . H 5 HOH 114 1114 1114 HOH TIP A . H 5 HOH 115 1115 1115 HOH TIP A . H 5 HOH 116 1116 1116 HOH TIP A . H 5 HOH 117 1117 1117 HOH TIP A . H 5 HOH 118 1118 1118 HOH TIP A . H 5 HOH 119 1119 1119 HOH TIP A . H 5 HOH 120 1120 1120 HOH TIP A . H 5 HOH 121 1121 1121 HOH TIP A . H 5 HOH 122 1122 1122 HOH TIP A . H 5 HOH 123 1123 1123 HOH TIP A . H 5 HOH 124 1124 1124 HOH TIP A . H 5 HOH 125 1125 1125 HOH TIP A . H 5 HOH 126 1126 1126 HOH TIP A . H 5 HOH 127 1127 1127 HOH TIP A . H 5 HOH 128 1128 1128 HOH TIP A . H 5 HOH 129 1129 1129 HOH TIP A . H 5 HOH 130 1130 1130 HOH TIP A . H 5 HOH 131 1131 1131 HOH TIP A . H 5 HOH 132 1132 1132 HOH TIP A . H 5 HOH 133 1133 1133 HOH TIP A . H 5 HOH 134 1134 1134 HOH TIP A . H 5 HOH 135 1135 1135 HOH TIP A . H 5 HOH 136 1136 1136 HOH TIP A . H 5 HOH 137 1137 1137 HOH TIP A . H 5 HOH 138 1138 1138 HOH TIP A . H 5 HOH 139 1139 1139 HOH TIP A . H 5 HOH 140 1140 1140 HOH TIP A . H 5 HOH 141 1141 1141 HOH TIP A . H 5 HOH 142 1142 1142 HOH TIP A . H 5 HOH 143 1143 1143 HOH TIP A . H 5 HOH 144 1144 1144 HOH TIP A . H 5 HOH 145 1145 1145 HOH TIP A . H 5 HOH 146 1146 1146 HOH TIP A . H 5 HOH 147 1147 1147 HOH TIP A . H 5 HOH 148 1148 1148 HOH TIP A . H 5 HOH 149 1149 1149 HOH TIP A . H 5 HOH 150 1150 1150 HOH TIP A . H 5 HOH 151 1151 1151 HOH TIP A . H 5 HOH 152 1152 1152 HOH TIP A . H 5 HOH 153 1153 1153 HOH TIP A . H 5 HOH 154 1154 1154 HOH TIP A . H 5 HOH 155 1155 1155 HOH TIP A . H 5 HOH 156 1156 1156 HOH TIP A . H 5 HOH 157 1157 1157 HOH TIP A . H 5 HOH 158 1158 1158 HOH TIP A . H 5 HOH 159 1159 1159 HOH TIP A . H 5 HOH 160 1160 1160 HOH TIP A . H 5 HOH 161 1161 1161 HOH TIP A . H 5 HOH 162 1162 1162 HOH TIP A . H 5 HOH 163 1163 1163 HOH TIP A . H 5 HOH 164 1164 1164 HOH TIP A . H 5 HOH 165 1165 1165 HOH TIP A . H 5 HOH 166 1166 1166 HOH TIP A . H 5 HOH 167 1167 1167 HOH TIP A . H 5 HOH 168 1168 1168 HOH TIP A . H 5 HOH 169 1169 1169 HOH TIP A . H 5 HOH 170 1170 1170 HOH TIP A . H 5 HOH 171 1171 1171 HOH TIP A . H 5 HOH 172 1172 1172 HOH TIP A . H 5 HOH 173 1173 1173 HOH TIP A . H 5 HOH 174 1174 1174 HOH TIP A . H 5 HOH 175 1175 1175 HOH TIP A . H 5 HOH 176 1176 1176 HOH TIP A . H 5 HOH 177 1177 1177 HOH TIP A . H 5 HOH 178 1178 1178 HOH TIP A . H 5 HOH 179 1179 1179 HOH TIP A . H 5 HOH 180 1180 1180 HOH TIP A . H 5 HOH 181 1181 1181 HOH TIP A . H 5 HOH 182 1182 1182 HOH TIP A . H 5 HOH 183 1183 1183 HOH TIP A . H 5 HOH 184 1184 1184 HOH TIP A . H 5 HOH 185 1185 1185 HOH TIP A . H 5 HOH 186 1186 1186 HOH TIP A . H 5 HOH 187 1187 1187 HOH TIP A . H 5 HOH 188 1188 1188 HOH TIP A . H 5 HOH 189 1189 1189 HOH TIP A . H 5 HOH 190 1190 1190 HOH TIP A . H 5 HOH 191 1191 1191 HOH TIP A . H 5 HOH 192 1192 1192 HOH TIP A . H 5 HOH 193 1193 1193 HOH TIP A . H 5 HOH 194 1194 1194 HOH TIP A . H 5 HOH 195 1195 1195 HOH TIP A . H 5 HOH 196 1196 1196 HOH TIP A . H 5 HOH 197 1197 1197 HOH TIP A . H 5 HOH 198 1198 1198 HOH TIP A . H 5 HOH 199 1199 1199 HOH TIP A . H 5 HOH 200 1200 1200 HOH TIP A . H 5 HOH 201 1201 1201 HOH TIP A . H 5 HOH 202 1202 1202 HOH TIP A . H 5 HOH 203 1203 1203 HOH TIP A . H 5 HOH 204 1204 1204 HOH TIP A . H 5 HOH 205 1205 1205 HOH TIP A . H 5 HOH 206 1206 1206 HOH TIP A . H 5 HOH 207 1207 1207 HOH TIP A . H 5 HOH 208 1208 1208 HOH TIP A . H 5 HOH 209 1209 1209 HOH TIP A . H 5 HOH 210 1210 1210 HOH TIP A . H 5 HOH 211 1211 1211 HOH TIP A . H 5 HOH 212 1212 1212 HOH TIP A . H 5 HOH 213 1213 1213 HOH TIP A . H 5 HOH 214 1214 1214 HOH TIP A . H 5 HOH 215 1215 1215 HOH TIP A . H 5 HOH 216 1216 1216 HOH TIP A . H 5 HOH 217 1217 1217 HOH TIP A . H 5 HOH 218 1218 1218 HOH TIP A . H 5 HOH 219 1219 1219 HOH TIP A . H 5 HOH 220 1220 1220 HOH TIP A . H 5 HOH 221 1221 1221 HOH TIP A . H 5 HOH 222 1222 1222 HOH TIP A . H 5 HOH 223 1223 1223 HOH TIP A . H 5 HOH 224 1224 1224 HOH TIP A . H 5 HOH 225 1225 1225 HOH TIP A . H 5 HOH 226 1226 1226 HOH TIP A . H 5 HOH 227 1227 1227 HOH TIP A . H 5 HOH 228 1228 1228 HOH TIP A . H 5 HOH 229 1229 1229 HOH TIP A . H 5 HOH 230 1230 1230 HOH TIP A . H 5 HOH 231 1231 1231 HOH TIP A . H 5 HOH 232 1232 1232 HOH TIP A . H 5 HOH 233 1233 1233 HOH TIP A . H 5 HOH 234 1234 1234 HOH TIP A . H 5 HOH 235 1235 1235 HOH TIP A . H 5 HOH 236 1236 1236 HOH TIP A . H 5 HOH 237 1237 1237 HOH TIP A . H 5 HOH 238 1238 1238 HOH TIP A . H 5 HOH 239 1239 1239 HOH TIP A . H 5 HOH 240 1240 1240 HOH TIP A . H 5 HOH 241 1241 1241 HOH TIP A . H 5 HOH 242 1242 1242 HOH TIP A . H 5 HOH 243 1243 1243 HOH TIP A . H 5 HOH 244 1244 1244 HOH TIP A . H 5 HOH 245 1245 1245 HOH TIP A . H 5 HOH 246 1246 1246 HOH TIP A . H 5 HOH 247 1247 1247 HOH TIP A . H 5 HOH 248 1248 1248 HOH TIP A . H 5 HOH 249 1249 1249 HOH TIP A . H 5 HOH 250 1250 1250 HOH TIP A . H 5 HOH 251 1251 1251 HOH TIP A . H 5 HOH 252 1252 1252 HOH TIP A . H 5 HOH 253 1253 1253 HOH TIP A . H 5 HOH 254 1254 1254 HOH TIP A . H 5 HOH 255 1255 1255 HOH TIP A . H 5 HOH 256 1256 1256 HOH TIP A . H 5 HOH 257 1257 1257 HOH TIP A . H 5 HOH 258 1258 1258 HOH TIP A . H 5 HOH 259 1259 1259 HOH TIP A . H 5 HOH 260 1260 1260 HOH TIP A . H 5 HOH 261 1261 1261 HOH TIP A . H 5 HOH 262 1262 1262 HOH TIP A . H 5 HOH 263 1263 1263 HOH TIP A . H 5 HOH 264 1264 1264 HOH TIP A . H 5 HOH 265 1265 1265 HOH TIP A . H 5 HOH 266 1266 1266 HOH TIP A . H 5 HOH 267 1267 1267 HOH TIP A . H 5 HOH 268 1268 1268 HOH TIP A . H 5 HOH 269 1269 1269 HOH TIP A . H 5 HOH 270 1270 1270 HOH TIP A . H 5 HOH 271 1271 1271 HOH TIP A . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 116 A ASN 116 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 513 A ASN 513 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_defined_assembly _pdbx_struct_assembly.method_details ? _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2006-08-29 2 'Structure model' 1 1 2008-04-30 3 'Structure model' 1 2 2011-07-13 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Version format compliance' 2 3 'Structure model' 'Non-polymer description' 3 3 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal CNS refinement 1.1 ? 1 DENZO 'data reduction' . ? 2 SCALEPACK 'data scaling' . ? 3 CNS phasing . ? 4 # 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 TYR A 11 ? ? -143.22 23.26 2 1 SER A 17 ? ? -170.98 -178.73 3 1 ASN A 18 ? ? 74.65 -166.53 4 1 ASN A 21 ? ? -125.51 -121.77 5 1 ASP A 22 ? ? -39.43 130.84 6 1 ALA A 44 ? ? -96.80 30.14 7 1 ASP A 77 ? ? -156.44 29.68 8 1 SER A 80 ? ? 169.06 157.80 9 1 GLU A 138 ? ? -50.18 -77.91 10 1 ASP A 147 ? ? 65.72 66.63 11 1 ALA A 196 ? ? 39.78 34.84 12 1 PHE A 273 ? ? -160.72 119.62 13 1 GLN A 339 ? ? -107.02 -116.89 14 1 LEU A 382 ? ? -162.80 112.09 15 1 ALA A 403 ? ? -85.59 -71.89 16 1 HIS A 478 ? ? 61.95 -91.13 17 1 ASN A 503 ? ? -127.90 -65.52 18 1 GLN A 537 ? ? -110.08 -149.92 # _pdbx_validate_chiral.id 1 _pdbx_validate_chiral.PDB_model_num 1 _pdbx_validate_chiral.auth_atom_id C1 _pdbx_validate_chiral.label_alt_id ? _pdbx_validate_chiral.auth_asym_id A _pdbx_validate_chiral.auth_comp_id NAG _pdbx_validate_chiral.auth_seq_id 650 _pdbx_validate_chiral.PDB_ins_code ? _pdbx_validate_chiral.details 'WRONG HAND' _pdbx_validate_chiral.omega . # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A GLN 1 ? A GLN 1 2 1 Y 1 A VAL 539 ? A VAL 539 3 1 Y 1 A LYS 540 ? A LYS 540 4 1 Y 1 A SER 541 ? A SER 541 5 1 Y 1 A ALA 542 ? A ALA 542 6 1 Y 1 A ALA 543 ? A ALA 543 # 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 FRUCTOSE FRU 5 water HOH #