data_2YP8 # _entry.id 2YP8 # _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 2YP8 PDBE EBI-54638 WWPDB D_1290054638 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 2YP2 unspecified 'HAEMAGGLUTININ OF 2004 HUMAN H3N2 VIRUS' PDB 2YP3 unspecified 'HAEMAGGLUTININ OF 2004 HUMAN H3N2 VIRUS IN COMPLEX WITH HUMAN RECEPTOR ANALOGUE 6SLN' PDB 2YP4 unspecified 'HAEMAGGLUTININ OF 2004 HUMAN H3N2 VIRUS IN COMPLEX WITH HUMAN RECEPTOR ANALOGUE LSTC' PDB 2YP5 unspecified 'HAEMAGGLUTININ OF 2004 HUMAN H3N2 VIRUS IN COMPLEX' PDB 2YP7 unspecified 'HAEMAGGLUTININ OF 2005 HUMAN H3N2 VIRUS' PDB 2YP9 unspecified 'HAEMAGGLUTININ OF 2005 HUMAN H3N2 VIRUS IN COMPLEX WITH AVIAN RECEPTOR ANALOGUE 3SLN' PDB 2YPG unspecified 'HAEMAGGLUTININ OF 1968 HUMAN H3N2 VIRUS IN COMPLEX WITH HUMAN RECEPTOR ANALOGUE LSTC' # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 2YP8 _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2012-10-29 _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Xiong, X.' 1 'Lin, Y.P.' 2 'Wharton, S.A.' 3 'Martin, S.R.' 4 'Coombs, P.J.' 5 'Vachieri, S.G.' 6 'Christodoulou, E.' 7 'Walker, P.A.' 8 'Liu, J.' 9 'Skehel, J.J.' 10 'Gamblin, S.J.' 11 'Hay, A.J.' 12 'Daniels, R.S.' 13 'McCauley, J.W.' 14 # _citation.id primary _citation.title 'Evolution of the Receptor Binding Properties of the Influenza A(H3N2) Hemagglutinin.' _citation.journal_abbrev Proc.Natl.Acad.Sci.USA _citation.journal_volume 109 _citation.page_first 21474 _citation.page_last ? _citation.year 2012 _citation.journal_id_ASTM PNASA6 _citation.country US _citation.journal_id_ISSN 0027-8424 _citation.journal_id_CSD 0040 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 23236176 _citation.pdbx_database_id_DOI 10.1073/PNAS.1218841110 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Lin, Y.P.' 1 primary 'Xiong, X.' 2 primary 'Wharton, S.A.' 3 primary 'Martin, S.R.' 4 primary 'Coombs, P.J.' 5 primary 'Vachieri, S.G.' 6 primary 'Christodoulou, E.' 7 primary 'Walker, P.A.' 8 primary 'Liu, J.' 9 primary 'Skehel, J.J.' 10 primary 'Gamblin, S.J.' 11 primary 'Hay, A.J.' 12 primary 'Daniels, R.S.' 13 primary 'Mccauley, J.W.' 14 # _cell.entry_id 2YP8 _cell.length_a 100.920 _cell.length_b 100.920 _cell.length_c 386.690 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 18 _cell.pdbx_unique_axis ? # _symmetry.entry_id 2YP8 _symmetry.space_group_name_H-M 'H 3 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 155 # 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 HEMAGGLUTININ 56488.215 1 ? YES 'TRYPSIN RELEASED ECTODOMAIN, RESIDUES 17-519' ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 10 ? ? ? ? 3 non-polymer man ALPHA-D-MANNOSE 180.156 1 ? ? ? ? 4 non-polymer syn '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' 238.305 3 ? ? ? ? 5 non-polymer syn 'TRIS(HYDROXYETHYL)AMINOMETHANE' 163.215 1 ? ? ? ? 6 non-polymer man 'O-SIALIC ACID' 309.270 1 ? ? ? ? 7 water nat water 18.015 510 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name HAEMAGGLUTININ # _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 ;QKLPGNDNSTATLCLGHHAVPNGTIVKTITNDQIEVTNATELVQSSSTGGICDSPHQILDGENCTLIDALLGDPQCDGFQ NKKWDLFVERSKAYSNCYPYDVPDYASLRSLVASSGTLEFNNESFNWTGVTQNGTSSACKRKSNNSFFSRLNWLTHLKFK YPALNVTMPNNEKFDKLYIWGVHHPGTDNDQIFLYAQASGRITVSTKRSQQTVIPNIGSRPRVRNIPSRISIYWTIVKPG DILLINSTGNLIAPRGYFKIRSGKSSIMRSDAPIGKCNSECITPNGSIPNDKPFQNVNRITYGACPRYVKQNTLKLATGM RNVPEKQTQGIFGAIAGFIENGWEGMVDGWYGFRHQNSEGIGQAADLKSTQAAINQINGKLNRLIGKTNEKFHQIEKEFS EVEGRIQDLEKYVEDTKIDLWSYNAELLVALENQHTIDLTDSEMNKLFERTKKQLRENAEDMGNGCFKIYHKCDNACIGS IRNGTYDHDVYRDEALNNRFQIK ; _entity_poly.pdbx_seq_one_letter_code_can ;QKLPGNDNSTATLCLGHHAVPNGTIVKTITNDQIEVTNATELVQSSSTGGICDSPHQILDGENCTLIDALLGDPQCDGFQ NKKWDLFVERSKAYSNCYPYDVPDYASLRSLVASSGTLEFNNESFNWTGVTQNGTSSACKRKSNNSFFSRLNWLTHLKFK YPALNVTMPNNEKFDKLYIWGVHHPGTDNDQIFLYAQASGRITVSTKRSQQTVIPNIGSRPRVRNIPSRISIYWTIVKPG DILLINSTGNLIAPRGYFKIRSGKSSIMRSDAPIGKCNSECITPNGSIPNDKPFQNVNRITYGACPRYVKQNTLKLATGM RNVPEKQTQGIFGAIAGFIENGWEGMVDGWYGFRHQNSEGIGQAADLKSTQAAINQINGKLNRLIGKTNEKFHQIEKEFS EVEGRIQDLEKYVEDTKIDLWSYNAELLVALENQHTIDLTDSEMNKLFERTKKQLRENAEDMGNGCFKIYHKCDNACIGS IRNGTYDHDVYRDEALNNRFQIK ; _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 LYS n 1 3 LEU n 1 4 PRO n 1 5 GLY n 1 6 ASN n 1 7 ASP n 1 8 ASN n 1 9 SER n 1 10 THR n 1 11 ALA n 1 12 THR n 1 13 LEU n 1 14 CYS n 1 15 LEU n 1 16 GLY n 1 17 HIS n 1 18 HIS n 1 19 ALA n 1 20 VAL n 1 21 PRO n 1 22 ASN n 1 23 GLY n 1 24 THR n 1 25 ILE n 1 26 VAL n 1 27 LYS n 1 28 THR n 1 29 ILE n 1 30 THR n 1 31 ASN n 1 32 ASP n 1 33 GLN n 1 34 ILE n 1 35 GLU n 1 36 VAL n 1 37 THR n 1 38 ASN n 1 39 ALA n 1 40 THR n 1 41 GLU n 1 42 LEU n 1 43 VAL n 1 44 GLN n 1 45 SER n 1 46 SER n 1 47 SER n 1 48 THR n 1 49 GLY n 1 50 GLY n 1 51 ILE n 1 52 CYS n 1 53 ASP n 1 54 SER n 1 55 PRO n 1 56 HIS n 1 57 GLN n 1 58 ILE n 1 59 LEU n 1 60 ASP n 1 61 GLY n 1 62 GLU n 1 63 ASN n 1 64 CYS n 1 65 THR n 1 66 LEU n 1 67 ILE n 1 68 ASP n 1 69 ALA n 1 70 LEU n 1 71 LEU n 1 72 GLY n 1 73 ASP n 1 74 PRO n 1 75 GLN n 1 76 CYS n 1 77 ASP n 1 78 GLY n 1 79 PHE n 1 80 GLN n 1 81 ASN n 1 82 LYS n 1 83 LYS n 1 84 TRP n 1 85 ASP n 1 86 LEU n 1 87 PHE n 1 88 VAL n 1 89 GLU n 1 90 ARG n 1 91 SER n 1 92 LYS n 1 93 ALA n 1 94 TYR n 1 95 SER n 1 96 ASN n 1 97 CYS n 1 98 TYR n 1 99 PRO n 1 100 TYR n 1 101 ASP n 1 102 VAL n 1 103 PRO n 1 104 ASP n 1 105 TYR n 1 106 ALA n 1 107 SER n 1 108 LEU n 1 109 ARG n 1 110 SER n 1 111 LEU n 1 112 VAL n 1 113 ALA n 1 114 SER n 1 115 SER n 1 116 GLY n 1 117 THR n 1 118 LEU n 1 119 GLU n 1 120 PHE n 1 121 ASN n 1 122 ASN n 1 123 GLU n 1 124 SER n 1 125 PHE n 1 126 ASN n 1 127 TRP n 1 128 THR n 1 129 GLY n 1 130 VAL n 1 131 THR n 1 132 GLN n 1 133 ASN n 1 134 GLY n 1 135 THR n 1 136 SER n 1 137 SER n 1 138 ALA n 1 139 CYS n 1 140 LYS n 1 141 ARG n 1 142 LYS n 1 143 SER n 1 144 ASN n 1 145 ASN n 1 146 SER n 1 147 PHE n 1 148 PHE n 1 149 SER n 1 150 ARG n 1 151 LEU n 1 152 ASN n 1 153 TRP n 1 154 LEU n 1 155 THR n 1 156 HIS n 1 157 LEU n 1 158 LYS n 1 159 PHE n 1 160 LYS n 1 161 TYR n 1 162 PRO n 1 163 ALA n 1 164 LEU n 1 165 ASN n 1 166 VAL n 1 167 THR n 1 168 MET n 1 169 PRO n 1 170 ASN n 1 171 ASN n 1 172 GLU n 1 173 LYS n 1 174 PHE n 1 175 ASP n 1 176 LYS n 1 177 LEU n 1 178 TYR n 1 179 ILE n 1 180 TRP n 1 181 GLY n 1 182 VAL n 1 183 HIS n 1 184 HIS n 1 185 PRO n 1 186 GLY n 1 187 THR n 1 188 ASP n 1 189 ASN n 1 190 ASP n 1 191 GLN n 1 192 ILE n 1 193 PHE n 1 194 LEU n 1 195 TYR n 1 196 ALA n 1 197 GLN n 1 198 ALA n 1 199 SER n 1 200 GLY n 1 201 ARG n 1 202 ILE n 1 203 THR n 1 204 VAL n 1 205 SER n 1 206 THR n 1 207 LYS n 1 208 ARG n 1 209 SER n 1 210 GLN n 1 211 GLN n 1 212 THR n 1 213 VAL n 1 214 ILE n 1 215 PRO n 1 216 ASN n 1 217 ILE n 1 218 GLY n 1 219 SER n 1 220 ARG n 1 221 PRO n 1 222 ARG n 1 223 VAL n 1 224 ARG n 1 225 ASN n 1 226 ILE n 1 227 PRO n 1 228 SER n 1 229 ARG n 1 230 ILE n 1 231 SER n 1 232 ILE n 1 233 TYR n 1 234 TRP n 1 235 THR n 1 236 ILE n 1 237 VAL n 1 238 LYS n 1 239 PRO n 1 240 GLY n 1 241 ASP n 1 242 ILE n 1 243 LEU n 1 244 LEU n 1 245 ILE n 1 246 ASN n 1 247 SER n 1 248 THR n 1 249 GLY n 1 250 ASN n 1 251 LEU n 1 252 ILE n 1 253 ALA n 1 254 PRO n 1 255 ARG n 1 256 GLY n 1 257 TYR n 1 258 PHE n 1 259 LYS n 1 260 ILE n 1 261 ARG n 1 262 SER n 1 263 GLY n 1 264 LYS n 1 265 SER n 1 266 SER n 1 267 ILE n 1 268 MET n 1 269 ARG n 1 270 SER n 1 271 ASP n 1 272 ALA n 1 273 PRO n 1 274 ILE n 1 275 GLY n 1 276 LYS n 1 277 CYS n 1 278 ASN n 1 279 SER n 1 280 GLU n 1 281 CYS n 1 282 ILE n 1 283 THR n 1 284 PRO n 1 285 ASN n 1 286 GLY n 1 287 SER n 1 288 ILE n 1 289 PRO n 1 290 ASN n 1 291 ASP n 1 292 LYS n 1 293 PRO n 1 294 PHE n 1 295 GLN n 1 296 ASN n 1 297 VAL n 1 298 ASN n 1 299 ARG n 1 300 ILE n 1 301 THR n 1 302 TYR n 1 303 GLY n 1 304 ALA n 1 305 CYS n 1 306 PRO n 1 307 ARG n 1 308 TYR n 1 309 VAL n 1 310 LYS n 1 311 GLN n 1 312 ASN n 1 313 THR n 1 314 LEU n 1 315 LYS n 1 316 LEU n 1 317 ALA n 1 318 THR n 1 319 GLY n 1 320 MET n 1 321 ARG n 1 322 ASN n 1 323 VAL n 1 324 PRO n 1 325 GLU n 1 326 LYS n 1 327 GLN n 1 328 THR n 1 329 GLN n 1 330 GLY n 1 331 ILE n 1 332 PHE n 1 333 GLY n 1 334 ALA n 1 335 ILE n 1 336 ALA n 1 337 GLY n 1 338 PHE n 1 339 ILE n 1 340 GLU n 1 341 ASN n 1 342 GLY n 1 343 TRP n 1 344 GLU n 1 345 GLY n 1 346 MET n 1 347 VAL n 1 348 ASP n 1 349 GLY n 1 350 TRP n 1 351 TYR n 1 352 GLY n 1 353 PHE n 1 354 ARG n 1 355 HIS n 1 356 GLN n 1 357 ASN n 1 358 SER n 1 359 GLU n 1 360 GLY n 1 361 ILE n 1 362 GLY n 1 363 GLN n 1 364 ALA n 1 365 ALA n 1 366 ASP n 1 367 LEU n 1 368 LYS n 1 369 SER n 1 370 THR n 1 371 GLN n 1 372 ALA n 1 373 ALA n 1 374 ILE n 1 375 ASN n 1 376 GLN n 1 377 ILE n 1 378 ASN n 1 379 GLY n 1 380 LYS n 1 381 LEU n 1 382 ASN n 1 383 ARG n 1 384 LEU n 1 385 ILE n 1 386 GLY n 1 387 LYS n 1 388 THR n 1 389 ASN n 1 390 GLU n 1 391 LYS n 1 392 PHE n 1 393 HIS n 1 394 GLN n 1 395 ILE n 1 396 GLU n 1 397 LYS n 1 398 GLU n 1 399 PHE n 1 400 SER n 1 401 GLU n 1 402 VAL n 1 403 GLU n 1 404 GLY n 1 405 ARG n 1 406 ILE n 1 407 GLN n 1 408 ASP n 1 409 LEU n 1 410 GLU n 1 411 LYS n 1 412 TYR n 1 413 VAL n 1 414 GLU n 1 415 ASP n 1 416 THR n 1 417 LYS n 1 418 ILE n 1 419 ASP n 1 420 LEU n 1 421 TRP n 1 422 SER n 1 423 TYR n 1 424 ASN n 1 425 ALA n 1 426 GLU n 1 427 LEU n 1 428 LEU n 1 429 VAL n 1 430 ALA n 1 431 LEU n 1 432 GLU n 1 433 ASN n 1 434 GLN n 1 435 HIS n 1 436 THR n 1 437 ILE n 1 438 ASP n 1 439 LEU n 1 440 THR n 1 441 ASP n 1 442 SER n 1 443 GLU n 1 444 MET n 1 445 ASN n 1 446 LYS n 1 447 LEU n 1 448 PHE n 1 449 GLU n 1 450 ARG n 1 451 THR n 1 452 LYS n 1 453 LYS n 1 454 GLN n 1 455 LEU n 1 456 ARG n 1 457 GLU n 1 458 ASN n 1 459 ALA n 1 460 GLU n 1 461 ASP n 1 462 MET n 1 463 GLY n 1 464 ASN n 1 465 GLY n 1 466 CYS n 1 467 PHE n 1 468 LYS n 1 469 ILE n 1 470 TYR n 1 471 HIS n 1 472 LYS n 1 473 CYS n 1 474 ASP n 1 475 ASN n 1 476 ALA n 1 477 CYS n 1 478 ILE n 1 479 GLY n 1 480 SER n 1 481 ILE n 1 482 ARG n 1 483 ASN n 1 484 GLY n 1 485 THR n 1 486 TYR n 1 487 ASP n 1 488 HIS n 1 489 ASP n 1 490 VAL n 1 491 TYR n 1 492 ARG n 1 493 ASP n 1 494 GLU n 1 495 ALA n 1 496 LEU n 1 497 ASN n 1 498 ASN n 1 499 ARG n 1 500 PHE n 1 501 GLN n 1 502 ILE n 1 503 LYS 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 ? _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene ? _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain H3N2 _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 'INFLUENZA A VIRUS' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 11320 _entity_src_gen.pdbx_gene_src_variant 'A/HONG KONG/4443/2005' _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 'FALL ARMYWORM' _entity_src_gen.pdbx_host_org_scientific_name 'SPODOPTERA FRUGIPERDA' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 7108 _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line SF9 _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 BACULOVIRUS _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name PACGP67A _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code I2D7A8_9INFA _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_align_begin ? _struct_ref.pdbx_db_accession I2D7A8 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 2YP8 _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 503 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession I2D7A8 _struct_ref_seq.db_align_beg 17 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 519 _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 503 # _struct_ref_seq_dif.align_id 1 _struct_ref_seq_dif.pdbx_pdb_id_code 2YP8 _struct_ref_seq_dif.mon_id GLN _struct_ref_seq_dif.pdbx_pdb_strand_id A _struct_ref_seq_dif.seq_num 329 _struct_ref_seq_dif.pdbx_pdb_ins_code ? _struct_ref_seq_dif.pdbx_seq_db_name UNP _struct_ref_seq_dif.pdbx_seq_db_accession_code I2D7A8 _struct_ref_seq_dif.db_mon_id ARG _struct_ref_seq_dif.pdbx_seq_db_seq_num 345 _struct_ref_seq_dif.details 'engineered mutation' _struct_ref_seq_dif.pdbx_auth_seq_num 329 _struct_ref_seq_dif.pdbx_ordinal 1 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 EPE non-polymer . '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' HEPES 'C8 H18 N2 O4 S' 238.305 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 SIA non-polymer . 'O-SIALIC ACID' ? 'C11 H19 N O9' 309.270 TAM non-polymer . 'TRIS(HYDROXYETHYL)AMINOMETHANE' ? 'C7 H17 N O3' 163.215 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 2YP8 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number ? # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.35 _exptl_crystal.density_percent_sol 63.33 _exptl_crystal.description NONE # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH ? _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details 'SITTING DROP, DEGLYCOSYLATED PROTEIN, 0.1 M HEPES PH 7.5, 0.2 M KCL, 30% PENTAERYTHRITOL PROPOXYLATE (5/4 PO/OH)' # _diffrn.id 1 _diffrn.ambient_temp 77 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'ADSC CCD' _diffrn_detector.pdbx_collection_date 2012-03-10 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.9763 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'DIAMOND BEAMLINE I03' _diffrn_source.pdbx_synchrotron_site Diamond _diffrn_source.pdbx_synchrotron_beamline I03 _diffrn_source.pdbx_wavelength 0.9763 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 2YP8 _reflns.observed_criterion_sigma_I 3.0 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 46.99 _reflns.d_resolution_high 1.80 _reflns.number_obs 70771 _reflns.number_all ? _reflns.percent_possible_obs 100.0 _reflns.pdbx_Rmerge_I_obs 0.10 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 12.40 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 7.1 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 2YP8 _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 67196 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F . _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 128.90 _refine.ls_d_res_high 1.80 _refine.ls_percent_reflns_obs 99.96 _refine.ls_R_factor_obs 0.17412 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.17286 _refine.ls_R_factor_R_free 0.19818 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.1 _refine.ls_number_reflns_R_free 3575 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.962 _refine.correlation_coeff_Fo_to_Fc_free 0.954 _refine.B_iso_mean 26.428 _refine.aniso_B[1][1] 0.64 _refine.aniso_B[2][2] 0.64 _refine.aniso_B[3][3] -0.96 _refine.aniso_B[1][2] 0.32 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.' _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.098 _refine.pdbx_overall_ESU_R_Free 0.096 _refine.overall_SU_ML 0.061 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 3.687 _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 3873 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 228 _refine_hist.number_atoms_solvent 510 _refine_hist.number_atoms_total 4611 _refine_hist.d_res_high 1.80 _refine_hist.d_res_low 128.90 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.009 0.020 ? 4246 'X-RAY DIFFRACTION' ? r_bond_other_d 0.001 0.020 ? 2893 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.309 1.998 ? 5772 'X-RAY DIFFRACTION' ? r_angle_other_deg 0.826 3.003 ? 7020 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.781 5.000 ? 502 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 35.085 24.950 ? 202 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 11.821 15.000 ? 697 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 13.236 15.000 ? 24 'X-RAY DIFFRACTION' ? r_chiral_restr 0.078 0.200 ? 651 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.005 0.020 ? 4623 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.001 0.020 ? 815 'X-RAY DIFFRACTION' ? r_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.800 _refine_ls_shell.d_res_low 1.847 _refine_ls_shell.number_reflns_R_work 4629 _refine_ls_shell.R_factor_R_work 0.292 _refine_ls_shell.percent_reflns_obs 100.00 _refine_ls_shell.R_factor_R_free 0.319 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 256 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 2YP8 _struct.title 'Haemagglutinin of 2005 Human H3N2 Virus in Complex with Human Receptor Analogue 6SLN' _struct.pdbx_descriptor HEMAGGLUTININ _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 2YP8 _struct_keywords.pdbx_keywords 'VIRAL PROTEIN' _struct_keywords.text 'VIRAL PROTEIN, RECEPTOR BINDING, MEMBRANE FUSION, INFLUENZA VIRUS EVOLUTION, GLYCOPROTEIN' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 2 ? D N N 2 ? E N N 2 ? F N N 2 ? G N N 2 ? H N N 3 ? I N N 2 ? J N N 2 ? K N N 2 ? L N N 2 ? M N N 4 ? N N N 4 ? O N N 4 ? P N N 5 ? Q N N 6 ? R N N 7 ? # _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 THR A 65 ? GLY A 72 ? THR A 65 GLY A 72 1 ? 8 HELX_P HELX_P2 2 ASP A 73 ? GLN A 80 ? ASP A 73 GLN A 80 5 ? 8 HELX_P HELX_P3 3 ASP A 104 ? GLY A 116 ? ASP A 104 GLY A 116 1 ? 13 HELX_P HELX_P4 4 THR A 187 ? ALA A 196 ? THR A 187 ALA A 196 1 ? 10 HELX_P HELX_P5 5 ASP A 366 ? ILE A 385 ? ASP A 366 ILE A 385 1 ? 20 HELX_P HELX_P6 6 GLY A 404 ? ARG A 456 ? GLY A 404 ARG A 456 1 ? 53 HELX_P HELX_P7 7 ASP A 474 ? ASN A 483 ? ASP A 474 ASN A 483 1 ? 10 HELX_P HELX_P8 8 ASP A 487 ? PHE A 500 ? ASP A 487 PHE A 500 1 ? 14 # _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 14 SG ? ? ? 1_555 A CYS 466 SG ? ? A CYS 14 A CYS 466 1_555 ? ? ? ? ? ? ? 2.061 ? disulf2 disulf ? ? A CYS 52 SG ? ? ? 1_555 A CYS 277 SG ? ? A CYS 52 A CYS 277 1_555 ? ? ? ? ? ? ? 2.094 ? disulf3 disulf ? ? A CYS 64 SG ? ? ? 1_555 A CYS 76 SG ? ? A CYS 64 A CYS 76 1_555 ? ? ? ? ? ? ? 2.109 ? disulf4 disulf ? ? A CYS 97 SG ? ? ? 1_555 A CYS 139 SG ? ? A CYS 97 A CYS 139 1_555 ? ? ? ? ? ? ? 2.064 ? disulf5 disulf ? ? A CYS 281 SG ? ? ? 1_555 A CYS 305 SG ? ? A CYS 281 A CYS 305 1_555 ? ? ? ? ? ? ? 2.044 ? disulf6 disulf ? ? A CYS 473 SG ? ? ? 1_555 A CYS 477 SG ? ? A CYS 473 A CYS 477 1_555 ? ? ? ? ? ? ? 2.118 ? covale1 covale ? ? A ASN 38 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 38 A NAG 1038 1_555 ? ? ? ? ? ? ? 1.446 ? covale2 covale ? ? A ASN 63 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 63 A NAG 1063 1_555 ? ? ? ? ? ? ? 1.436 ? covale3 covale ? ? A ASN 126 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 126 A NAG 1126 1_555 ? ? ? ? ? ? ? 1.440 ? covale4 covale ? ? A ASN 133 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 133 A NAG 1133 1_555 ? ? ? ? ? ? ? 1.442 ? covale5 covale ? ? A ASN 165 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 165 A NAG 1165 1_555 ? ? ? ? ? ? ? 1.439 ? covale6 covale ? ? A ASN 246 ND2 ? ? ? 1_555 I NAG . C1 ? ? A ASN 246 A NAG 1246 1_555 ? ? ? ? ? ? ? 1.458 ? covale7 covale ? ? A ASN 285 ND2 ? ? ? 1_555 K NAG . C1 ? ? A ASN 285 A NAG 1285 1_555 ? ? ? ? ? ? ? 1.439 ? covale8 covale ? ? A ASN 483 ND2 ? ? ? 1_555 L NAG . C1 ? ? A ASN 483 A NAG 1483 1_555 ? ? ? ? ? ? ? 1.456 ? covale9 covale ? ? F NAG . O4 ? ? ? 1_555 G NAG . C1 ? ? A NAG 1165 A NAG 1166 1_555 ? ? ? ? ? ? ? 1.435 ? covale10 covale ? ? H MAN . C1 ? ? ? 1_555 G NAG . O4 ? ? A MAN 1167 A NAG 1166 1_555 ? ? ? ? ? ? ? 1.454 ? covale11 covale ? ? I NAG . O4 ? ? ? 1_555 J NAG . C1 ? ? A NAG 1246 A NAG 1247 1_555 ? ? ? ? ? ? ? 1.444 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # _struct_mon_prot_cis.pdbx_id 1 _struct_mon_prot_cis.label_comp_id SER _struct_mon_prot_cis.label_seq_id 54 _struct_mon_prot_cis.label_asym_id A _struct_mon_prot_cis.label_alt_id . _struct_mon_prot_cis.pdbx_PDB_ins_code ? _struct_mon_prot_cis.auth_comp_id SER _struct_mon_prot_cis.auth_seq_id 54 _struct_mon_prot_cis.auth_asym_id A _struct_mon_prot_cis.pdbx_label_comp_id_2 PRO _struct_mon_prot_cis.pdbx_label_seq_id_2 55 _struct_mon_prot_cis.pdbx_label_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_ins_code_2 ? _struct_mon_prot_cis.pdbx_auth_comp_id_2 PRO _struct_mon_prot_cis.pdbx_auth_seq_id_2 55 _struct_mon_prot_cis.pdbx_auth_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_model_num 1 _struct_mon_prot_cis.pdbx_omega_angle 1.43 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA ? 5 ? AB ? 2 ? AC ? 2 ? AD ? 3 ? AE ? 2 ? AF ? 3 ? AG ? 5 ? AH ? 5 ? AI ? 2 ? AJ ? 2 ? AK ? 4 ? AL ? 4 ? # 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 AA 1 2 ? anti-parallel AA 2 3 ? anti-parallel AA 3 4 ? anti-parallel AA 4 5 ? anti-parallel AB 1 2 ? anti-parallel AC 1 2 ? anti-parallel AD 1 2 ? parallel AD 2 3 ? parallel AE 1 2 ? parallel AF 1 2 ? parallel AF 2 3 ? parallel AG 1 2 ? parallel AG 2 3 ? anti-parallel AG 3 4 ? anti-parallel AG 4 5 ? anti-parallel AH 1 2 ? parallel AH 2 3 ? anti-parallel AH 3 4 ? anti-parallel AH 4 5 ? anti-parallel AI 1 2 ? anti-parallel AJ 1 2 ? anti-parallel AK 1 2 ? anti-parallel AK 2 3 ? anti-parallel AK 3 4 ? anti-parallel AL 1 2 ? anti-parallel AL 2 3 ? anti-parallel AL 3 4 ? 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 AA 1 GLY A 360 ? ALA A 365 ? GLY A 360 ALA A 365 AA 2 TYR A 351 ? ASN A 357 ? TYR A 351 ASN A 357 AA 3 ALA A 11 ? HIS A 17 ? ALA A 11 HIS A 17 AA 4 CYS A 466 ? ILE A 469 ? CYS A 466 ILE A 469 AA 5 ALA A 459 ? ASP A 461 ? ALA A 459 ASP A 461 AB 1 THR A 24 ? VAL A 26 ? THR A 24 VAL A 26 AB 2 ILE A 34 ? VAL A 36 ? ILE A 34 VAL A 36 AC 1 ALA A 39 ? GLU A 41 ? ALA A 39 GLU A 41 AC 2 LYS A 315 ? ALA A 317 ? LYS A 315 ALA A 317 AD 1 VAL A 43 ? GLN A 44 ? VAL A 43 GLN A 44 AD 2 PHE A 294 ? GLN A 295 ? PHE A 294 GLN A 295 AD 3 ARG A 307 ? TYR A 308 ? ARG A 307 TYR A 308 AE 1 ILE A 51 ? SER A 54 ? ILE A 51 SER A 54 AE 2 ILE A 274 ? ASN A 278 ? ILE A 274 ASN A 278 AF 1 ILE A 58 ? ASP A 60 ? ILE A 58 ASP A 60 AF 2 LEU A 86 ? GLU A 89 ? LEU A 86 GLU A 89 AF 3 SER A 266 ? ARG A 269 ? SER A 266 ARG A 269 AG 1 TYR A 100 ? ASP A 101 ? TYR A 100 ASP A 101 AG 2 ARG A 229 ? VAL A 237 ? ARG A 229 VAL A 237 AG 3 LYS A 176 ? HIS A 184 ? LYS A 176 HIS A 184 AG 4 LEU A 251 ? PRO A 254 ? LEU A 251 PRO A 254 AG 5 LEU A 151 ? TRP A 153 ? LEU A 151 TRP A 153 AH 1 TYR A 100 ? ASP A 101 ? TYR A 100 ASP A 101 AH 2 ARG A 229 ? VAL A 237 ? ARG A 229 VAL A 237 AH 3 LYS A 176 ? HIS A 184 ? LYS A 176 HIS A 184 AH 4 GLY A 256 ? LYS A 259 ? GLY A 256 LYS A 259 AH 5 PHE A 120 ? ASN A 122 ? PHE A 120 ASN A 122 AI 1 VAL A 130 ? THR A 131 ? VAL A 130 THR A 131 AI 2 THR A 155 ? HIS A 156 ? THR A 155 HIS A 156 AJ 1 SER A 136 ? ARG A 141 ? SER A 136 ARG A 141 AJ 2 ASN A 144 ? SER A 146 ? ASN A 144 SER A 146 AK 1 LEU A 164 ? PRO A 169 ? LEU A 164 PRO A 169 AK 2 ILE A 242 ? SER A 247 ? ILE A 242 SER A 247 AK 3 ILE A 202 ? SER A 205 ? ILE A 202 SER A 205 AK 4 GLN A 210 ? VAL A 213 ? GLN A 210 VAL A 213 AL 1 GLY A 286 ? ILE A 288 ? GLY A 286 ILE A 288 AL 2 CYS A 281 ? THR A 283 ? CYS A 281 THR A 283 AL 3 TYR A 302 ? CYS A 305 ? TYR A 302 CYS A 305 AL 4 ASN A 389 ? LYS A 391 ? ASN A 389 LYS A 391 # 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 AA 1 2 N ALA A 364 ? N ALA A 364 O PHE A 353 ? O PHE A 353 AA 2 3 N GLN A 356 ? N GLN A 356 O THR A 12 ? O THR A 12 AA 3 4 N LEU A 13 ? N LEU A 13 O PHE A 467 ? O PHE A 467 AA 4 5 N LYS A 468 ? N LYS A 468 O GLU A 460 ? O GLU A 460 AB 1 2 N VAL A 26 ? N VAL A 26 O ILE A 34 ? O ILE A 34 AC 1 2 N THR A 40 ? N THR A 40 O LEU A 316 ? O LEU A 316 AD 1 2 N GLN A 44 ? N GLN A 44 O PHE A 294 ? O PHE A 294 AD 2 3 N GLN A 295 ? N GLN A 295 O ARG A 307 ? O ARG A 307 AE 1 2 N ASP A 53 ? N ASP A 53 O GLY A 275 ? O GLY A 275 AF 1 2 N LEU A 59 ? N LEU A 59 O LEU A 86 ? O LEU A 86 AF 2 3 N PHE A 87 ? N PHE A 87 O SER A 266 ? O SER A 266 AG 1 2 N ASP A 101 ? N ASP A 101 O ILE A 230 ? O ILE A 230 AG 2 3 N VAL A 237 ? N VAL A 237 O LYS A 176 ? O LYS A 176 AG 3 4 N GLY A 181 ? N GLY A 181 O ILE A 252 ? O ILE A 252 AG 4 5 N ALA A 253 ? N ALA A 253 O ASN A 152 ? O ASN A 152 AH 1 2 N ASP A 101 ? N ASP A 101 O ILE A 230 ? O ILE A 230 AH 2 3 N VAL A 237 ? N VAL A 237 O LYS A 176 ? O LYS A 176 AH 3 4 N LEU A 177 ? N LEU A 177 O PHE A 258 ? O PHE A 258 AH 4 5 N TYR A 257 ? N TYR A 257 O ASN A 121 ? O ASN A 121 AI 1 2 N THR A 131 ? N THR A 131 O THR A 155 ? O THR A 155 AJ 1 2 N ARG A 141 ? N ARG A 141 O ASN A 144 ? O ASN A 144 AK 1 2 N MET A 168 ? N MET A 168 O LEU A 243 ? O LEU A 243 AK 2 3 N ASN A 246 ? N ASN A 246 O THR A 203 ? O THR A 203 AK 3 4 N VAL A 204 ? N VAL A 204 O GLN A 211 ? O GLN A 211 AL 1 2 N ILE A 288 ? N ILE A 288 O CYS A 281 ? O CYS A 281 AL 2 3 N ILE A 282 ? N ILE A 282 O TYR A 302 ? O TYR A 302 AL 3 4 N CYS A 305 ? N CYS A 305 O ASN A 389 ? O ASN A 389 # 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 ? ? ? ? 10 'BINDING SITE FOR RESIDUE EPE A 1504' AC2 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE EPE A 1505' AC3 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE EPE A 1506' AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE TAM A 1507' AC5 Software ? ? ? ? 12 'BINDING SITE FOR RESIDUE SIA A 1508' AC6 Software ? ? ? ? 3 'BINDING SITE FOR MONO-SACCHARIDE NAG A1038 BOUND TO ASN A 38' AC7 Software ? ? ? ? 4 'BINDING SITE FOR MONO-SACCHARIDE NAG A1063 BOUND TO ASN A 63' AC8 Software ? ? ? ? 3 'BINDING SITE FOR MONO-SACCHARIDE NAG A1126 BOUND TO ASN A 126' AC9 Software ? ? ? ? 2 'BINDING SITE FOR MONO-SACCHARIDE NAG A1133 BOUND TO ASN A 133' BC1 Software ? ? ? ? 11 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 165 RESIDUES 1165 TO 1167' BC2 Software ? ? ? ? 11 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 246 RESIDUES 1246 TO 1247' BC3 Software ? ? ? ? 5 'BINDING SITE FOR MONO-SACCHARIDE NAG A1285 BOUND TO ASN A 285' BC4 Software ? ? ? ? 7 'BINDING SITE FOR MONO-SACCHARIDE NAG A1483 BOUND TO ASN A 483' # 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 10 ASP A 77 ? ASP A 77 . ? 1_555 ? 2 AC1 10 ARG A 141 ? ARG A 141 . ? 1_555 ? 3 AC1 10 SER A 146 ? SER A 146 . ? 1_555 ? 4 AC1 10 PHE A 147 ? PHE A 147 . ? 1_555 ? 5 AC1 10 PHE A 148 ? PHE A 148 . ? 1_555 ? 6 AC1 10 LEU A 151 ? LEU A 151 . ? 1_555 ? 7 AC1 10 ARG A 255 ? ARG A 255 . ? 1_555 ? 8 AC1 10 NAG E . ? NAG A 1133 . ? 1_555 ? 9 AC1 10 HOH R . ? HOH A 2102 . ? 1_555 ? 10 AC1 10 HOH R . ? HOH A 2173 . ? 1_555 ? 11 AC2 7 PRO A 99 ? PRO A 99 . ? 1_555 ? 12 AC2 7 TYR A 100 ? TYR A 100 . ? 1_555 ? 13 AC2 7 TYR A 105 ? TYR A 105 . ? 1_555 ? 14 AC2 7 ARG A 208 ? ARG A 208 . ? 3_455 ? 15 AC2 7 ARG A 224 ? ARG A 224 . ? 1_555 ? 16 AC2 7 HOH R . ? HOH A 2124 . ? 1_555 ? 17 AC2 7 HOH R . ? HOH A 2125 . ? 1_555 ? 18 AC3 7 ASN A 81 ? ASN A 81 . ? 1_555 ? 19 AC3 7 PHE A 120 ? PHE A 120 . ? 1_555 ? 20 AC3 7 ASN A 121 ? ASN A 121 . ? 1_555 ? 21 AC3 7 ASN A 122 ? ASN A 122 . ? 1_555 ? 22 AC3 7 GLU A 280 ? GLU A 280 . ? 10_455 ? 23 AC3 7 GLU A 390 ? GLU A 390 . ? 10_455 ? 24 AC3 7 HOH R . ? HOH A 2105 . ? 1_555 ? 25 AC4 4 ARG A 383 ? ARG A 383 . ? 1_555 ? 26 AC4 4 HOH R . ? HOH A 2394 . ? 1_555 ? 27 AC4 4 HOH R . ? HOH A 2508 . ? 1_555 ? 28 AC4 4 HOH R . ? HOH A 2509 . ? 1_555 ? 29 AC5 12 GLY A 134 ? GLY A 134 . ? 1_555 ? 30 AC5 12 THR A 135 ? THR A 135 . ? 1_555 ? 31 AC5 12 SER A 136 ? SER A 136 . ? 1_555 ? 32 AC5 12 SER A 137 ? SER A 137 . ? 1_555 ? 33 AC5 12 TRP A 153 ? TRP A 153 . ? 1_555 ? 34 AC5 12 ASP A 190 ? ASP A 190 . ? 1_555 ? 35 AC5 12 PHE A 193 ? PHE A 193 . ? 1_555 ? 36 AC5 12 LEU A 194 ? LEU A 194 . ? 1_555 ? 37 AC5 12 HOH R . ? HOH A 2128 . ? 1_555 ? 38 AC5 12 HOH R . ? HOH A 2175 . ? 1_555 ? 39 AC5 12 HOH R . ? HOH A 2177 . ? 1_555 ? 40 AC5 12 HOH R . ? HOH A 2229 . ? 1_555 ? 41 AC6 3 ASN A 38 ? ASN A 38 . ? 1_555 ? 42 AC6 3 THR A 318 ? THR A 318 . ? 1_555 ? 43 AC6 3 LEU A 381 ? LEU A 381 . ? 1_555 ? 44 AC7 4 GLU A 62 ? GLU A 62 . ? 1_555 ? 45 AC7 4 ASN A 63 ? ASN A 63 . ? 1_555 ? 46 AC7 4 TYR A 94 ? TYR A 94 . ? 1_555 ? 47 AC7 4 HOH R . ? HOH A 2086 . ? 1_555 ? 48 AC8 3 ASN A 126 ? ASN A 126 . ? 1_555 ? 49 AC8 3 THR A 128 ? THR A 128 . ? 1_555 ? 50 AC8 3 HOH R . ? HOH A 2168 . ? 1_555 ? 51 AC9 2 ASN A 133 ? ASN A 133 . ? 1_555 ? 52 AC9 2 EPE M . ? EPE A 1504 . ? 1_555 ? 53 BC1 11 ASN A 165 ? ASN A 165 . ? 1_555 ? 54 BC1 11 SER A 219 ? SER A 219 . ? 2_565 ? 55 BC1 11 PRO A 221 ? PRO A 221 . ? 2_565 ? 56 BC1 11 ARG A 222 ? ARG A 222 . ? 2_565 ? 57 BC1 11 NAG I . ? NAG A 1246 . ? 1_555 ? 58 BC1 11 HOH R . ? HOH A 2209 . ? 1_555 ? 59 BC1 11 HOH R . ? HOH A 2262 . ? 2_565 ? 60 BC1 11 HOH R . ? HOH A 2502 . ? 1_555 ? 61 BC1 11 HOH R . ? HOH A 2503 . ? 1_555 ? 62 BC1 11 HOH R . ? HOH A 2504 . ? 1_555 ? 63 BC1 11 HOH R . ? HOH A 2505 . ? 1_555 ? 64 BC2 11 ALA A 163 ? ALA A 163 . ? 1_555 ? 65 BC2 11 LEU A 164 ? LEU A 164 . ? 1_555 ? 66 BC2 11 ASN A 165 ? ASN A 165 . ? 1_555 ? 67 BC2 11 ARG A 201 ? ARG A 201 . ? 1_555 ? 68 BC2 11 ASN A 246 ? ASN A 246 . ? 1_555 ? 69 BC2 11 SER A 247 ? SER A 247 . ? 1_555 ? 70 BC2 11 THR A 248 ? THR A 248 . ? 1_555 ? 71 BC2 11 NAG F . ? NAG A 1165 . ? 1_555 ? 72 BC2 11 HOH R . ? HOH A 2239 . ? 1_555 ? 73 BC2 11 HOH R . ? HOH A 2258 . ? 2_565 ? 74 BC2 11 HOH R . ? HOH A 2506 . ? 1_555 ? 75 BC3 5 SER A 45 ? SER A 45 . ? 1_555 ? 76 BC3 5 ASN A 285 ? ASN A 285 . ? 1_555 ? 77 BC3 5 VAL A 297 ? VAL A 297 . ? 1_555 ? 78 BC3 5 HOH R . ? HOH A 2311 . ? 1_555 ? 79 BC3 5 HOH R . ? HOH A 2322 . ? 1_555 ? 80 BC4 7 ALA A 476 ? ALA A 476 . ? 1_555 ? 81 BC4 7 GLY A 479 ? GLY A 479 . ? 1_555 ? 82 BC4 7 ARG A 482 ? ARG A 482 . ? 1_555 ? 83 BC4 7 ASN A 483 ? ASN A 483 . ? 1_555 ? 84 BC4 7 THR A 485 ? THR A 485 . ? 1_555 ? 85 BC4 7 HOH R . ? HOH A 2485 . ? 1_555 ? 86 BC4 7 HOH R . ? HOH A 2486 . ? 1_555 ? # _database_PDB_matrix.entry_id 2YP8 _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 2YP8 _atom_sites.fract_transf_matrix[1][1] 0.009909 _atom_sites.fract_transf_matrix[1][2] 0.005721 _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] 0.011442 _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] 0.002586 _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 . ASN A 1 8 ? -55.361 9.134 -11.771 1.00 67.57 ? 8 ASN A N 1 ATOM 2 C CA . ASN A 1 8 ? -54.067 8.734 -12.396 1.00 66.40 ? 8 ASN A CA 1 ATOM 3 C C . ASN A 1 8 ? -53.242 9.960 -12.799 1.00 61.92 ? 8 ASN A C 1 ATOM 4 O O . ASN A 1 8 ? -53.806 11.022 -13.077 1.00 63.63 ? 8 ASN A O 1 ATOM 5 C CB . ASN A 1 8 ? -54.323 7.849 -13.615 1.00 69.98 ? 8 ASN A CB 1 ATOM 6 C CG . ASN A 1 8 ? -53.098 7.054 -14.022 1.00 72.63 ? 8 ASN A CG 1 ATOM 7 O OD1 . ASN A 1 8 ? -52.560 6.278 -13.230 1.00 73.28 ? 8 ASN A OD1 1 ATOM 8 N ND2 . ASN A 1 8 ? -52.649 7.245 -15.258 1.00 74.43 ? 8 ASN A ND2 1 ATOM 9 N N . SER A 1 9 ? -51.915 9.803 -12.828 1.00 55.37 ? 9 SER A N 1 ATOM 10 C CA . SER A 1 9 ? -50.968 10.917 -13.037 1.00 49.47 ? 9 SER A CA 1 ATOM 11 C C . SER A 1 9 ? -50.796 11.783 -11.775 1.00 43.31 ? 9 SER A C 1 ATOM 12 O O . SER A 1 9 ? -50.156 12.833 -11.812 1.00 39.38 ? 9 SER A O 1 ATOM 13 C CB . SER A 1 9 ? -51.391 11.778 -14.234 1.00 51.01 ? 9 SER A CB 1 ATOM 14 O OG . SER A 1 9 ? -52.453 12.660 -13.909 1.00 50.95 ? 9 SER A OG 1 ATOM 15 N N . THR A 1 10 ? -51.372 11.334 -10.661 1.00 39.14 ? 10 THR A N 1 ATOM 16 C CA . THR A 1 10 ? -51.289 12.046 -9.393 1.00 36.15 ? 10 THR A CA 1 ATOM 17 C C . THR A 1 10 ? -51.132 11.058 -8.244 1.00 33.30 ? 10 THR A C 1 ATOM 18 O O . THR A 1 10 ? -51.242 9.848 -8.418 1.00 33.14 ? 10 THR A O 1 ATOM 19 C CB . THR A 1 10 ? -52.543 12.901 -9.138 1.00 37.08 ? 10 THR A CB 1 ATOM 20 O OG1 . THR A 1 10 ? -53.683 12.054 -9.073 1.00 38.86 ? 10 THR A OG1 1 ATOM 21 C CG2 . THR A 1 10 ? -52.743 13.920 -10.242 1.00 39.08 ? 10 THR A CG2 1 ATOM 22 N N . ALA A 1 11 ? -50.856 11.589 -7.064 1.00 29.53 ? 11 ALA A N 1 ATOM 23 C CA . ALA A 1 11 ? -50.768 10.788 -5.865 1.00 28.25 ? 11 ALA A CA 1 ATOM 24 C C . ALA A 1 11 ? -51.399 11.603 -4.744 1.00 26.72 ? 11 ALA A C 1 ATOM 25 O O . ALA A 1 11 ? -51.606 12.810 -4.890 1.00 26.28 ? 11 ALA A O 1 ATOM 26 C CB . ALA A 1 11 ? -49.314 10.473 -5.545 1.00 27.90 ? 11 ALA A CB 1 ATOM 27 N N . THR A 1 12 ? -51.714 10.924 -3.647 1.00 25.66 ? 12 THR A N 1 ATOM 28 C CA . THR A 1 12 ? -52.200 11.556 -2.425 1.00 25.42 ? 12 THR A CA 1 ATOM 29 C C . THR A 1 12 ? -51.260 11.254 -1.276 1.00 24.16 ? 12 THR A C 1 ATOM 30 O O . THR A 1 12 ? -50.822 10.116 -1.105 1.00 24.59 ? 12 THR A O 1 ATOM 31 C CB . THR A 1 12 ? -53.596 11.039 -2.055 1.00 25.97 ? 12 THR A CB 1 ATOM 32 O OG1 . THR A 1 12 ? -54.463 11.189 -3.180 1.00 26.98 ? 12 THR A OG1 1 ATOM 33 C CG2 . THR A 1 12 ? -54.176 11.807 -0.866 1.00 26.39 ? 12 THR A CG2 1 ATOM 34 N N . LEU A 1 13 ? -50.954 12.275 -0.482 1.00 23.80 ? 13 LEU A N 1 ATOM 35 C CA . LEU A 1 13 ? -50.141 12.104 0.718 1.00 23.01 ? 13 LEU A CA 1 ATOM 36 C C . LEU A 1 13 ? -50.844 12.750 1.910 1.00 23.55 ? 13 LEU A C 1 ATOM 37 O O . LEU A 1 13 ? -51.029 13.958 1.932 1.00 23.02 ? 13 LEU A O 1 ATOM 38 C CB . LEU A 1 13 ? -48.766 12.725 0.527 1.00 22.60 ? 13 LEU A CB 1 ATOM 39 C CG . LEU A 1 13 ? -47.792 12.608 1.711 1.00 22.60 ? 13 LEU A CG 1 ATOM 40 C CD1 . LEU A 1 13 ? -47.429 11.154 2.002 1.00 22.84 ? 13 LEU A CD1 1 ATOM 41 C CD2 . LEU A 1 13 ? -46.553 13.467 1.460 1.00 23.12 ? 13 LEU A CD2 1 ATOM 42 N N . CYS A 1 14 ? -51.235 11.929 2.879 1.00 24.47 ? 14 CYS A N 1 ATOM 43 C CA . CYS A 1 14 ? -51.943 12.377 4.080 1.00 25.33 ? 14 CYS A CA 1 ATOM 44 C C . CYS A 1 14 ? -51.025 12.362 5.298 1.00 24.83 ? 14 CYS A C 1 ATOM 45 O O . CYS A 1 14 ? -50.171 11.481 5.450 1.00 23.80 ? 14 CYS A O 1 ATOM 46 C CB . CYS A 1 14 ? -53.146 11.464 4.340 1.00 27.57 ? 14 CYS A CB 1 ATOM 47 S SG . CYS A 1 14 ? -54.383 11.466 3.015 1.00 30.08 ? 14 CYS A SG 1 ATOM 48 N N . LEU A 1 15 ? -51.190 13.373 6.151 1.00 23.38 ? 15 LEU A N 1 ATOM 49 C CA . LEU A 1 15 ? -50.488 13.461 7.409 1.00 23.55 ? 15 LEU A CA 1 ATOM 50 C C . LEU A 1 15 ? -51.462 13.092 8.495 1.00 22.72 ? 15 LEU A C 1 ATOM 51 O O . LEU A 1 15 ? -52.617 13.503 8.450 1.00 23.45 ? 15 LEU A O 1 ATOM 52 C CB . LEU A 1 15 ? -49.990 14.881 7.637 1.00 23.99 ? 15 LEU A CB 1 ATOM 53 C CG . LEU A 1 15 ? -48.735 15.302 6.873 1.00 25.16 ? 15 LEU A CG 1 ATOM 54 C CD1 . LEU A 1 15 ? -47.577 14.487 7.394 1.00 26.80 ? 15 LEU A CD1 1 ATOM 55 C CD2 . LEU A 1 15 ? -48.894 15.147 5.363 1.00 27.30 ? 15 LEU A CD2 1 ATOM 56 N N . GLY A 1 16 ? -51.013 12.316 9.469 1.00 22.19 ? 16 GLY A N 1 ATOM 57 C CA . GLY A 1 16 ? -51.920 11.847 10.510 1.00 22.05 ? 16 GLY A CA 1 ATOM 58 C C . GLY A 1 16 ? -51.251 11.530 11.821 1.00 21.74 ? 16 GLY A C 1 ATOM 59 O O . GLY A 1 16 ? -50.034 11.602 11.954 1.00 20.55 ? 16 GLY A O 1 ATOM 60 N N . HIS A 1 17 ? -52.075 11.160 12.787 1.00 21.80 ? 17 HIS A N 1 ATOM 61 C CA . HIS A 1 17 ? -51.597 10.766 14.104 1.00 21.69 ? 17 HIS A CA 1 ATOM 62 C C . HIS A 1 17 ? -52.371 9.588 14.589 1.00 22.05 ? 17 HIS A C 1 ATOM 63 O O . HIS A 1 17 ? -53.465 9.330 14.096 1.00 23.21 ? 17 HIS A O 1 ATOM 64 C CB . HIS A 1 17 ? -51.700 11.944 15.086 1.00 21.48 ? 17 HIS A CB 1 ATOM 65 C CG . HIS A 1 17 ? -53.106 12.438 15.306 1.00 21.84 ? 17 HIS A CG 1 ATOM 66 N ND1 . HIS A 1 17 ? -54.025 11.738 16.012 1.00 22.02 ? 17 HIS A ND1 1 ATOM 67 C CD2 . HIS A 1 17 ? -53.736 13.593 14.885 1.00 22.25 ? 17 HIS A CD2 1 ATOM 68 C CE1 . HIS A 1 17 ? -55.194 12.412 16.005 1.00 22.56 ? 17 HIS A CE1 1 ATOM 69 N NE2 . HIS A 1 17 ? -55.018 13.544 15.327 1.00 23.23 ? 17 HIS A NE2 1 ATOM 70 N N . HIS A 1 18 ? -51.819 8.859 15.557 1.00 22.57 ? 18 HIS A N 1 ATOM 71 C CA . HIS A 1 18 ? -52.443 7.660 16.078 1.00 23.39 ? 18 HIS A CA 1 ATOM 72 C C . HIS A 1 18 ? -53.654 7.937 16.922 1.00 24.77 ? 18 HIS A C 1 ATOM 73 O O . HIS A 1 18 ? -53.942 9.077 17.293 1.00 23.55 ? 18 HIS A O 1 ATOM 74 C CB . HIS A 1 18 ? -51.434 6.782 16.830 1.00 24.27 ? 18 HIS A CB 1 ATOM 75 C CG . HIS A 1 18 ? -51.063 7.292 18.211 1.00 24.13 ? 18 HIS A CG 1 ATOM 76 N ND1 . HIS A 1 18 ? -50.538 6.488 19.164 1.00 25.67 ? 18 HIS A ND1 1 ATOM 77 C CD2 . HIS A 1 18 ? -51.170 8.565 18.784 1.00 24.34 ? 18 HIS A CD2 1 ATOM 78 C CE1 . HIS A 1 18 ? -50.302 7.219 20.283 1.00 24.95 ? 18 HIS A CE1 1 ATOM 79 N NE2 . HIS A 1 18 ? -50.692 8.486 20.048 1.00 24.22 ? 18 HIS A NE2 1 ATOM 80 N N . ALA A 1 19 ? -54.383 6.866 17.198 1.00 24.94 ? 19 ALA A N 1 ATOM 81 C CA . ALA A 1 19 ? -55.520 6.873 18.092 1.00 26.29 ? 19 ALA A CA 1 ATOM 82 C C . ALA A 1 19 ? -55.551 5.487 18.709 1.00 28.01 ? 19 ALA A C 1 ATOM 83 O O . ALA A 1 19 ? -54.983 4.549 18.142 1.00 29.59 ? 19 ALA A O 1 ATOM 84 C CB . ALA A 1 19 ? -56.818 7.165 17.354 1.00 26.57 ? 19 ALA A CB 1 ATOM 85 N N . VAL A 1 20 ? -56.189 5.365 19.867 1.00 28.92 ? 20 VAL A N 1 ATOM 86 C CA . VAL A 1 20 ? -56.240 4.097 20.580 1.00 29.49 ? 20 VAL A CA 1 ATOM 87 C C . VAL A 1 20 ? -57.684 3.767 20.877 1.00 32.07 ? 20 VAL A C 1 ATOM 88 O O . VAL A 1 20 ? -58.542 4.661 20.944 1.00 31.08 ? 20 VAL A O 1 ATOM 89 C CB . VAL A 1 20 ? -55.403 4.117 21.871 1.00 30.20 ? 20 VAL A CB 1 ATOM 90 C CG1 . VAL A 1 20 ? -53.942 4.370 21.536 1.00 29.37 ? 20 VAL A CG1 1 ATOM 91 C CG2 . VAL A 1 20 ? -55.943 5.159 22.849 1.00 28.58 ? 20 VAL A CG2 1 ATOM 92 N N . PRO A 1 21 ? -57.985 2.463 20.998 1.00 35.54 ? 21 PRO A N 1 ATOM 93 C CA . PRO A 1 21 ? -59.371 2.092 21.276 1.00 37.81 ? 21 PRO A CA 1 ATOM 94 C C . PRO A 1 21 ? -59.806 2.389 22.717 1.00 39.36 ? 21 PRO A C 1 ATOM 95 O O . PRO A 1 21 ? -60.999 2.547 22.960 1.00 44.09 ? 21 PRO A O 1 ATOM 96 C CB . PRO A 1 21 ? -59.395 0.585 20.988 1.00 37.53 ? 21 PRO A CB 1 ATOM 97 C CG . PRO A 1 21 ? -57.991 0.125 21.217 1.00 37.17 ? 21 PRO A CG 1 ATOM 98 C CD . PRO A 1 21 ? -57.113 1.290 20.814 1.00 36.37 ? 21 PRO A CD 1 ATOM 99 N N . ASN A 1 22 ? -58.851 2.481 23.645 1.00 38.95 ? 22 ASN A N 1 ATOM 100 C CA . ASN A 1 22 ? -59.142 2.616 25.077 1.00 40.18 ? 22 ASN A CA 1 ATOM 101 C C . ASN A 1 22 ? -58.545 3.903 25.691 1.00 36.64 ? 22 ASN A C 1 ATOM 102 O O . ASN A 1 22 ? -57.653 3.827 26.537 1.00 36.09 ? 22 ASN A O 1 ATOM 103 C CB . ASN A 1 22 ? -58.583 1.403 25.831 1.00 41.96 ? 22 ASN A CB 1 ATOM 104 C CG . ASN A 1 22 ? -57.074 1.247 25.645 1.00 46.12 ? 22 ASN A CG 1 ATOM 105 O OD1 . ASN A 1 22 ? -56.520 1.597 24.582 1.00 48.76 ? 22 ASN A OD1 1 ATOM 106 N ND2 . ASN A 1 22 ? -56.397 0.742 26.679 1.00 47.25 ? 22 ASN A ND2 1 ATOM 107 N N . GLY A 1 23 ? -59.049 5.064 25.282 1.00 34.65 ? 23 GLY A N 1 ATOM 108 C CA . GLY A 1 23 ? -58.498 6.355 25.754 1.00 33.87 ? 23 GLY A CA 1 ATOM 109 C C . GLY A 1 23 ? -58.936 6.693 27.173 1.00 32.41 ? 23 GLY A C 1 ATOM 110 O O . GLY A 1 23 ? -59.771 5.989 27.748 1.00 31.88 ? 23 GLY A O 1 ATOM 111 N N . THR A 1 24 ? -58.389 7.769 27.746 1.00 29.85 ? 24 THR A N 1 ATOM 112 C CA . THR A 1 24 ? -58.743 8.175 29.122 1.00 29.18 ? 24 THR A CA 1 ATOM 113 C C . THR A 1 24 ? -59.098 9.656 29.197 1.00 27.02 ? 24 THR A C 1 ATOM 114 O O . THR A 1 24 ? -58.495 10.477 28.503 1.00 26.15 ? 24 THR A O 1 ATOM 115 C CB . THR A 1 24 ? -57.598 7.977 30.128 1.00 31.59 ? 24 THR A CB 1 ATOM 116 O OG1 . THR A 1 24 ? -56.875 6.782 29.844 1.00 34.91 ? 24 THR A OG1 1 ATOM 117 C CG2 . THR A 1 24 ? -58.156 7.879 31.525 1.00 32.20 ? 24 THR A CG2 1 ATOM 118 N N . ILE A 1 25 ? -60.027 9.986 30.084 1.00 23.95 ? 25 ILE A N 1 ATOM 119 C CA . ILE A 1 25 ? -60.517 11.348 30.223 1.00 23.77 ? 25 ILE A CA 1 ATOM 120 C C . ILE A 1 25 ? -59.635 12.139 31.194 1.00 21.66 ? 25 ILE A C 1 ATOM 121 O O . ILE A 1 25 ? -59.338 11.668 32.296 1.00 20.07 ? 25 ILE A O 1 ATOM 122 C CB . ILE A 1 25 ? -61.980 11.378 30.705 1.00 25.46 ? 25 ILE A CB 1 ATOM 123 C CG1 . ILE A 1 25 ? -62.873 10.616 29.725 1.00 27.89 ? 25 ILE A CG1 1 ATOM 124 C CG2 . ILE A 1 25 ? -62.469 12.819 30.862 1.00 25.50 ? 25 ILE A CG2 1 ATOM 125 C CD1 . ILE A 1 25 ? -62.804 11.122 28.310 1.00 28.75 ? 25 ILE A CD1 1 ATOM 126 N N . VAL A 1 26 ? -59.199 13.316 30.750 1.00 20.29 ? 26 VAL A N 1 ATOM 127 C CA . VAL A 1 26 ? -58.483 14.261 31.599 1.00 19.59 ? 26 VAL A CA 1 ATOM 128 C C . VAL A 1 26 ? -59.121 15.639 31.543 1.00 19.89 ? 26 VAL A C 1 ATOM 129 O O . VAL A 1 26 ? -59.997 15.917 30.709 1.00 20.41 ? 26 VAL A O 1 ATOM 130 C CB . VAL A 1 26 ? -56.992 14.389 31.224 1.00 18.53 ? 26 VAL A CB 1 ATOM 131 C CG1 . VAL A 1 26 ? -56.288 13.040 31.336 1.00 18.69 ? 26 VAL A CG1 1 ATOM 132 C CG2 . VAL A 1 26 ? -56.843 15.042 29.844 1.00 17.83 ? 26 VAL A CG2 1 ATOM 133 N N . LYS A 1 27 ? -58.651 16.519 32.429 1.00 20.81 ? 27 LYS A N 1 ATOM 134 C CA . LYS A 1 27 ? -59.098 17.903 32.475 1.00 21.75 ? 27 LYS A CA 1 ATOM 135 C C . LYS A 1 27 ? -58.008 18.873 32.007 1.00 21.18 ? 27 LYS A C 1 ATOM 136 O O . LYS A 1 27 ? -56.857 18.750 32.376 1.00 19.47 ? 27 LYS A O 1 ATOM 137 C CB . LYS A 1 27 ? -59.505 18.250 33.907 1.00 23.76 ? 27 LYS A CB 1 ATOM 138 C CG . LYS A 1 27 ? -59.883 19.694 34.149 1.00 26.41 ? 27 LYS A CG 1 ATOM 139 C CD . LYS A 1 27 ? -60.341 19.901 35.600 1.00 28.58 ? 27 LYS A CD 1 ATOM 140 C CE . LYS A 1 27 ? -60.269 21.373 36.017 1.00 30.48 ? 27 LYS A CE 1 ATOM 141 N NZ . LYS A 1 27 ? -60.850 21.580 37.387 1.00 31.56 ? 27 LYS A NZ 1 ATOM 142 N N . THR A 1 28 ? -58.394 19.851 31.205 1.00 21.76 ? 28 THR A N 1 ATOM 143 C CA . THR A 1 28 ? -57.461 20.889 30.768 1.00 22.80 ? 28 THR A CA 1 ATOM 144 C C . THR A 1 28 ? -58.069 22.235 31.116 1.00 24.54 ? 28 THR A C 1 ATOM 145 O O . THR A 1 28 ? -59.141 22.317 31.717 1.00 25.43 ? 28 THR A O 1 ATOM 146 C CB . THR A 1 28 ? -57.183 20.812 29.253 1.00 22.82 ? 28 THR A CB 1 ATOM 147 O OG1 . THR A 1 28 ? -58.368 21.168 28.520 1.00 22.95 ? 28 THR A OG1 1 ATOM 148 C CG2 . THR A 1 28 ? -56.720 19.412 28.834 1.00 23.71 ? 28 THR A CG2 1 ATOM 149 N N . ILE A 1 29 ? -57.400 23.305 30.718 1.00 25.51 ? 29 ILE A N 1 ATOM 150 C CA . ILE A 1 29 ? -57.947 24.632 30.896 1.00 27.17 ? 29 ILE A CA 1 ATOM 151 C C . ILE A 1 29 ? -59.122 24.845 29.941 1.00 28.20 ? 29 ILE A C 1 ATOM 152 O O . ILE A 1 29 ? -60.108 25.456 30.312 1.00 31.27 ? 29 ILE A O 1 ATOM 153 C CB . ILE A 1 29 ? -56.875 25.705 30.651 1.00 27.64 ? 29 ILE A CB 1 ATOM 154 C CG1 . ILE A 1 29 ? -55.738 25.536 31.657 1.00 28.38 ? 29 ILE A CG1 1 ATOM 155 C CG2 . ILE A 1 29 ? -57.504 27.091 30.721 1.00 29.33 ? 29 ILE A CG2 1 ATOM 156 C CD1 . ILE A 1 29 ? -56.149 25.768 33.098 1.00 29.72 ? 29 ILE A CD1 1 ATOM 157 N N . THR A 1 30 ? -59.019 24.318 28.725 1.00 29.01 ? 30 THR A N 1 ATOM 158 C CA . THR A 1 30 ? -60.073 24.458 27.717 1.00 30.20 ? 30 THR A CA 1 ATOM 159 C C . THR A 1 30 ? -61.290 23.557 27.992 1.00 32.06 ? 30 THR A C 1 ATOM 160 O O . THR A 1 30 ? -62.427 23.954 27.748 1.00 32.22 ? 30 THR A O 1 ATOM 161 C CB . THR A 1 30 ? -59.520 24.137 26.308 1.00 30.08 ? 30 THR A CB 1 ATOM 162 O OG1 . THR A 1 30 ? -58.396 24.979 26.024 1.00 29.10 ? 30 THR A OG1 1 ATOM 163 C CG2 . THR A 1 30 ? -60.588 24.329 25.214 1.00 30.85 ? 30 THR A CG2 1 ATOM 164 N N . ASN A 1 31 ? -61.053 22.345 28.486 1.00 31.01 ? 31 ASN A N 1 ATOM 165 C CA . ASN A 1 31 ? -62.109 21.320 28.586 1.00 32.05 ? 31 ASN A CA 1 ATOM 166 C C . ASN A 1 31 ? -62.134 20.659 29.962 1.00 31.29 ? 31 ASN A C 1 ATOM 167 O O . ASN A 1 31 ? -61.104 20.186 30.425 1.00 28.83 ? 31 ASN A O 1 ATOM 168 C CB . ASN A 1 31 ? -61.829 20.205 27.577 1.00 34.58 ? 31 ASN A CB 1 ATOM 169 C CG . ASN A 1 31 ? -62.099 20.610 26.145 1.00 36.70 ? 31 ASN A CG 1 ATOM 170 O OD1 . ASN A 1 31 ? -63.249 20.825 25.764 1.00 41.67 ? 31 ASN A OD1 1 ATOM 171 N ND2 . ASN A 1 31 ? -61.045 20.673 25.329 1.00 35.53 ? 31 ASN A ND2 1 ATOM 172 N N . ASP A 1 32 ? -63.300 20.591 30.593 1.00 30.83 ? 32 ASP A N 1 ATOM 173 C CA A ASP A 1 32 ? -63.459 19.818 31.821 0.50 31.39 ? 32 ASP A CA 1 ATOM 174 C CA B ASP A 1 32 ? -63.475 19.818 31.820 0.50 31.14 ? 32 ASP A CA 1 ATOM 175 C C . ASP A 1 32 ? -63.176 18.330 31.575 1.00 30.29 ? 32 ASP A C 1 ATOM 176 O O . ASP A 1 32 ? -62.635 17.646 32.437 1.00 30.56 ? 32 ASP A O 1 ATOM 177 C CB A ASP A 1 32 ? -64.869 19.992 32.383 0.50 33.69 ? 32 ASP A CB 1 ATOM 178 C CB B ASP A 1 32 ? -64.905 19.975 32.343 0.50 33.07 ? 32 ASP A CB 1 ATOM 179 C CG A ASP A 1 32 ? -65.117 21.394 32.903 0.50 36.03 ? 32 ASP A CG 1 ATOM 180 C CG B ASP A 1 32 ? -65.154 19.196 33.625 0.50 34.71 ? 32 ASP A CG 1 ATOM 181 O OD1 A ASP A 1 32 ? -64.267 21.902 33.665 0.50 37.71 ? 32 ASP A OD1 1 ATOM 182 O OD1 B ASP A 1 32 ? -64.378 19.362 34.595 0.50 36.44 ? 32 ASP A OD1 1 ATOM 183 O OD2 A ASP A 1 32 ? -66.158 21.982 32.547 0.50 38.64 ? 32 ASP A OD2 1 ATOM 184 O OD2 B ASP A 1 32 ? -66.131 18.415 33.662 0.50 37.44 ? 32 ASP A OD2 1 ATOM 185 N N . GLN A 1 33 ? -63.530 17.850 30.389 1.00 29.11 ? 33 GLN A N 1 ATOM 186 C CA . GLN A 1 33 ? -63.330 16.450 29.995 1.00 29.12 ? 33 GLN A CA 1 ATOM 187 C C . GLN A 1 33 ? -62.824 16.395 28.562 1.00 27.70 ? 33 GLN A C 1 ATOM 188 O O . GLN A 1 33 ? -63.491 16.877 27.643 1.00 28.73 ? 33 GLN A O 1 ATOM 189 C CB . GLN A 1 33 ? -64.640 15.651 30.120 1.00 32.41 ? 33 GLN A CB 1 ATOM 190 C CG . GLN A 1 33 ? -65.150 15.521 31.553 1.00 34.78 ? 33 GLN A CG 1 ATOM 191 C CD . GLN A 1 33 ? -66.147 14.389 31.735 1.00 39.22 ? 33 GLN A CD 1 ATOM 192 O OE1 . GLN A 1 33 ? -67.055 14.207 30.927 1.00 43.24 ? 33 GLN A OE1 1 ATOM 193 N NE2 . GLN A 1 33 ? -65.983 13.625 32.804 1.00 40.90 ? 33 GLN A NE2 1 ATOM 194 N N . ILE A 1 34 ? -61.633 15.854 28.364 1.00 24.53 ? 34 ILE A N 1 ATOM 195 C CA . ILE A 1 34 ? -61.133 15.571 27.028 1.00 24.50 ? 34 ILE A CA 1 ATOM 196 C C . ILE A 1 34 ? -60.444 14.222 27.064 1.00 23.30 ? 34 ILE A C 1 ATOM 197 O O . ILE A 1 34 ? -59.691 13.932 27.991 1.00 22.29 ? 34 ILE A O 1 ATOM 198 C CB . ILE A 1 34 ? -60.203 16.673 26.460 1.00 24.73 ? 34 ILE A CB 1 ATOM 199 C CG1 . ILE A 1 34 ? -59.729 16.290 25.050 1.00 25.92 ? 34 ILE A CG1 1 ATOM 200 C CG2 . ILE A 1 34 ? -59.021 16.952 27.380 1.00 24.21 ? 34 ILE A CG2 1 ATOM 201 C CD1 . ILE A 1 34 ? -58.983 17.396 24.333 1.00 26.46 ? 34 ILE A CD1 1 ATOM 202 N N . GLU A 1 35 ? -60.739 13.383 26.071 1.00 23.40 ? 35 GLU A N 1 ATOM 203 C CA . GLU A 1 35 ? -60.129 12.077 25.998 1.00 23.74 ? 35 GLU A CA 1 ATOM 204 C C . GLU A 1 35 ? -58.759 12.182 25.319 1.00 22.11 ? 35 GLU A C 1 ATOM 205 O O . GLU A 1 35 ? -58.630 12.775 24.258 1.00 22.77 ? 35 GLU A O 1 ATOM 206 C CB . GLU A 1 35 ? -61.036 11.091 25.246 1.00 26.25 ? 35 GLU A CB 1 ATOM 207 C CG . GLU A 1 35 ? -60.688 9.640 25.467 1.00 28.85 ? 35 GLU A CG 1 ATOM 208 C CD . GLU A 1 35 ? -61.581 8.719 24.647 1.00 32.81 ? 35 GLU A CD 1 ATOM 209 O OE1 . GLU A 1 35 ? -62.815 8.721 24.873 1.00 37.18 ? 35 GLU A OE1 1 ATOM 210 O OE2 . GLU A 1 35 ? -61.047 8.009 23.773 1.00 34.48 ? 35 GLU A OE2 1 ATOM 211 N N . VAL A 1 36 ? -57.764 11.593 25.961 1.00 20.47 ? 36 VAL A N 1 ATOM 212 C CA . VAL A 1 36 ? -56.402 11.503 25.453 1.00 20.20 ? 36 VAL A CA 1 ATOM 213 C C . VAL A 1 36 ? -56.031 10.041 25.332 1.00 20.35 ? 36 VAL A C 1 ATOM 214 O O . VAL A 1 36 ? -56.747 9.178 25.836 1.00 21.24 ? 36 VAL A O 1 ATOM 215 C CB . VAL A 1 36 ? -55.413 12.242 26.379 1.00 19.27 ? 36 VAL A CB 1 ATOM 216 C CG1 . VAL A 1 36 ? -55.638 13.750 26.277 1.00 18.76 ? 36 VAL A CG1 1 ATOM 217 C CG2 . VAL A 1 36 ? -55.524 11.746 27.837 1.00 18.77 ? 36 VAL A CG2 1 ATOM 218 N N . THR A 1 37 ? -54.914 9.749 24.678 1.00 20.83 ? 37 THR A N 1 ATOM 219 C CA . THR A 1 37 ? -54.534 8.365 24.451 1.00 21.38 ? 37 THR A CA 1 ATOM 220 C C . THR A 1 37 ? -54.048 7.645 25.700 1.00 22.16 ? 37 THR A C 1 ATOM 221 O O . THR A 1 37 ? -54.137 6.425 25.799 1.00 22.41 ? 37 THR A O 1 ATOM 222 C CB . THR A 1 37 ? -53.452 8.245 23.373 1.00 21.64 ? 37 THR A CB 1 ATOM 223 O OG1 . THR A 1 37 ? -52.267 8.914 23.799 1.00 22.05 ? 37 THR A OG1 1 ATOM 224 C CG2 . THR A 1 37 ? -53.950 8.822 22.042 1.00 20.63 ? 37 THR A CG2 1 ATOM 225 N N . ASN A 1 38 ? -53.547 8.396 26.676 1.00 21.97 ? 38 ASN A N 1 ATOM 226 C CA . ASN A 1 38 ? -52.987 7.779 27.856 1.00 22.80 ? 38 ASN A CA 1 ATOM 227 C C . ASN A 1 38 ? -52.861 8.857 28.921 1.00 21.60 ? 38 ASN A C 1 ATOM 228 O O . ASN A 1 38 ? -52.728 10.038 28.592 1.00 19.33 ? 38 ASN A O 1 ATOM 229 C CB . ASN A 1 38 ? -51.619 7.194 27.524 1.00 25.33 ? 38 ASN A CB 1 ATOM 230 C CG . ASN A 1 38 ? -51.072 6.300 28.614 1.00 28.42 ? 38 ASN A CG 1 ATOM 231 O OD1 . ASN A 1 38 ? -51.810 5.705 29.391 1.00 29.04 ? 38 ASN A OD1 1 ATOM 232 N ND2 . ASN A 1 38 ? -49.750 6.206 28.662 1.00 36.04 ? 38 ASN A ND2 1 ATOM 233 N N . ALA A 1 39 ? -52.902 8.427 30.175 1.00 20.66 ? 39 ALA A N 1 ATOM 234 C CA . ALA A 1 39 ? -52.681 9.334 31.301 1.00 20.76 ? 39 ALA A CA 1 ATOM 235 C C . ALA A 1 39 ? -52.093 8.563 32.470 1.00 21.92 ? 39 ALA A C 1 ATOM 236 O O . ALA A 1 39 ? -52.059 7.320 32.471 1.00 22.44 ? 39 ALA A O 1 ATOM 237 C CB . ALA A 1 39 ? -53.997 10.011 31.688 1.00 20.70 ? 39 ALA A CB 1 ATOM 238 N N . THR A 1 40 ? -51.610 9.294 33.465 1.00 21.58 ? 40 THR A N 1 ATOM 239 C CA . THR A 1 40 ? -51.076 8.667 34.664 1.00 22.04 ? 40 THR A CA 1 ATOM 240 C C . THR A 1 40 ? -51.624 9.377 35.906 1.00 21.04 ? 40 THR A C 1 ATOM 241 O O . THR A 1 40 ? -51.925 10.564 35.868 1.00 19.82 ? 40 THR A O 1 ATOM 242 C CB . THR A 1 40 ? -49.537 8.635 34.630 1.00 22.90 ? 40 THR A CB 1 ATOM 243 O OG1 . THR A 1 40 ? -49.067 7.691 35.593 1.00 27.13 ? 40 THR A OG1 1 ATOM 244 C CG2 . THR A 1 40 ? -48.938 9.980 34.914 1.00 24.38 ? 40 THR A CG2 1 ATOM 245 N N . GLU A 1 41 ? -51.780 8.622 36.983 1.00 20.54 ? 41 GLU A N 1 ATOM 246 C CA . GLU A 1 41 ? -52.370 9.120 38.226 1.00 20.19 ? 41 GLU A CA 1 ATOM 247 C C . GLU A 1 41 ? -51.339 9.869 39.076 1.00 19.27 ? 41 GLU A C 1 ATOM 248 O O . GLU A 1 41 ? -50.234 9.356 39.335 1.00 19.34 ? 41 GLU A O 1 ATOM 249 C CB . GLU A 1 41 ? -52.932 7.940 39.015 1.00 21.01 ? 41 GLU A CB 1 ATOM 250 C CG . GLU A 1 41 ? -53.563 8.283 40.351 1.00 20.99 ? 41 GLU A CG 1 ATOM 251 C CD . GLU A 1 41 ? -54.689 9.291 40.232 1.00 21.30 ? 41 GLU A CD 1 ATOM 252 O OE1 . GLU A 1 41 ? -55.759 8.940 39.676 1.00 22.16 ? 41 GLU A OE1 1 ATOM 253 O OE2 . GLU A 1 41 ? -54.512 10.450 40.694 1.00 19.39 ? 41 GLU A OE2 1 ATOM 254 N N . LEU A 1 42 ? -51.691 11.069 39.529 1.00 17.65 ? 42 LEU A N 1 ATOM 255 C CA . LEU A 1 42 ? -50.767 11.859 40.342 1.00 16.97 ? 42 LEU A CA 1 ATOM 256 C C . LEU A 1 42 ? -51.113 11.897 41.838 1.00 16.31 ? 42 LEU A C 1 ATOM 257 O O . LEU A 1 42 ? -50.379 12.497 42.614 1.00 15.75 ? 42 LEU A O 1 ATOM 258 C CB . LEU A 1 42 ? -50.662 13.291 39.813 1.00 16.96 ? 42 LEU A CB 1 ATOM 259 C CG . LEU A 1 42 ? -50.072 13.470 38.406 1.00 17.48 ? 42 LEU A CG 1 ATOM 260 C CD1 . LEU A 1 42 ? -49.853 14.949 38.137 1.00 17.61 ? 42 LEU A CD1 1 ATOM 261 C CD2 . LEU A 1 42 ? -48.749 12.724 38.254 1.00 17.36 ? 42 LEU A CD2 1 ATOM 262 N N . VAL A 1 43 ? -52.244 11.323 42.221 1.00 16.14 ? 43 VAL A N 1 ATOM 263 C CA . VAL A 1 43 ? -52.638 11.229 43.623 1.00 16.43 ? 43 VAL A CA 1 ATOM 264 C C . VAL A 1 43 ? -52.526 9.794 44.115 1.00 17.07 ? 43 VAL A C 1 ATOM 265 O O . VAL A 1 43 ? -53.230 8.886 43.645 1.00 17.15 ? 43 VAL A O 1 ATOM 266 C CB . VAL A 1 43 ? -54.075 11.747 43.866 1.00 16.45 ? 43 VAL A CB 1 ATOM 267 C CG1 . VAL A 1 43 ? -54.456 11.633 45.339 1.00 16.45 ? 43 VAL A CG1 1 ATOM 268 C CG2 . VAL A 1 43 ? -54.212 13.197 43.389 1.00 16.62 ? 43 VAL A CG2 1 ATOM 269 N N . GLN A 1 44 ? -51.645 9.585 45.086 1.00 17.22 ? 44 GLN A N 1 ATOM 270 C CA . GLN A 1 44 ? -51.544 8.292 45.759 1.00 17.62 ? 44 GLN A CA 1 ATOM 271 C C . GLN A 1 44 ? -52.716 8.091 46.722 1.00 18.75 ? 44 GLN A C 1 ATOM 272 O O . GLN A 1 44 ? -52.909 8.865 47.662 1.00 17.35 ? 44 GLN A O 1 ATOM 273 C CB . GLN A 1 44 ? -50.217 8.194 46.514 1.00 17.54 ? 44 GLN A CB 1 ATOM 274 C CG . GLN A 1 44 ? -49.973 6.845 47.156 1.00 18.09 ? 44 GLN A CG 1 ATOM 275 C CD . GLN A 1 44 ? -49.796 5.749 46.139 1.00 18.80 ? 44 GLN A CD 1 ATOM 276 O OE1 . GLN A 1 44 ? -49.162 5.958 45.107 1.00 19.69 ? 44 GLN A OE1 1 ATOM 277 N NE2 . GLN A 1 44 ? -50.359 4.557 46.423 1.00 19.56 ? 44 GLN A NE2 1 ATOM 278 N N . SER A 1 45 ? -53.517 7.053 46.499 1.00 19.57 ? 45 SER A N 1 ATOM 279 C CA . SER A 1 45 ? -54.694 6.864 47.339 1.00 22.18 ? 45 SER A CA 1 ATOM 280 C C . SER A 1 45 ? -54.750 5.558 48.124 1.00 24.22 ? 45 SER A C 1 ATOM 281 O O . SER A 1 45 ? -55.685 5.330 48.882 1.00 25.03 ? 45 SER A O 1 ATOM 282 C CB . SER A 1 45 ? -55.968 7.063 46.510 1.00 23.84 ? 45 SER A CB 1 ATOM 283 O OG . SER A 1 45 ? -55.990 6.169 45.418 1.00 26.63 ? 45 SER A OG 1 ATOM 284 N N . SER A 1 46 ? -53.754 4.711 47.984 1.00 25.56 ? 46 SER A N 1 ATOM 285 C CA . SER A 1 46 ? -53.742 3.473 48.760 1.00 28.06 ? 46 SER A CA 1 ATOM 286 C C . SER A 1 46 ? -52.473 3.379 49.569 1.00 28.90 ? 46 SER A C 1 ATOM 287 O O . SER A 1 46 ? -51.453 4.012 49.224 1.00 26.44 ? 46 SER A O 1 ATOM 288 C CB . SER A 1 46 ? -53.821 2.283 47.825 1.00 28.33 ? 46 SER A CB 1 ATOM 289 O OG . SER A 1 46 ? -52.717 2.294 46.939 1.00 29.09 ? 46 SER A OG 1 ATOM 290 N N . SER A 1 47 ? -52.552 2.588 50.641 1.00 32.51 ? 47 SER A N 1 ATOM 291 C CA . SER A 1 47 ? -51.390 2.146 51.408 1.00 34.17 ? 47 SER A CA 1 ATOM 292 C C . SER A 1 47 ? -51.441 0.626 51.526 1.00 37.29 ? 47 SER A C 1 ATOM 293 O O . SER A 1 47 ? -52.511 0.050 51.474 1.00 37.33 ? 47 SER A O 1 ATOM 294 C CB . SER A 1 47 ? -51.402 2.719 52.829 1.00 35.46 ? 47 SER A CB 1 ATOM 295 O OG . SER A 1 47 ? -50.355 2.130 53.600 1.00 37.28 ? 47 SER A OG 1 ATOM 296 N N . THR A 1 48 ? -50.273 0.015 51.703 1.00 40.88 ? 48 THR A N 1 ATOM 297 C CA . THR A 1 48 ? -50.123 -1.402 52.067 1.00 44.09 ? 48 THR A CA 1 ATOM 298 C C . THR A 1 48 ? -50.844 -1.748 53.359 1.00 42.80 ? 48 THR A C 1 ATOM 299 O O . THR A 1 48 ? -51.310 -2.876 53.551 1.00 45.15 ? 48 THR A O 1 ATOM 300 C CB . THR A 1 48 ? -48.643 -1.719 52.349 1.00 46.81 ? 48 THR A CB 1 ATOM 301 O OG1 . THR A 1 48 ? -47.861 -1.443 51.180 1.00 51.85 ? 48 THR A OG1 1 ATOM 302 C CG2 . THR A 1 48 ? -48.464 -3.179 52.787 1.00 47.67 ? 48 THR A CG2 1 ATOM 303 N N . GLY A 1 49 ? -50.889 -0.782 54.272 1.00 39.21 ? 49 GLY A N 1 ATOM 304 C CA . GLY A 1 49 ? -51.509 -1.000 55.561 1.00 37.30 ? 49 GLY A CA 1 ATOM 305 C C . GLY A 1 49 ? -50.489 -1.334 56.632 1.00 34.72 ? 49 GLY A C 1 ATOM 306 O O . GLY A 1 49 ? -50.876 -1.457 57.796 1.00 35.99 ? 49 GLY A O 1 ATOM 307 N N . GLY A 1 50 ? -49.211 -1.494 56.249 1.00 29.09 ? 50 GLY A N 1 ATOM 308 C CA . GLY A 1 50 ? -48.128 -1.680 57.219 1.00 25.75 ? 50 GLY A CA 1 ATOM 309 C C . GLY A 1 50 ? -47.086 -0.570 57.203 1.00 22.67 ? 50 GLY A C 1 ATOM 310 O O . GLY A 1 50 ? -46.832 0.010 56.148 1.00 20.72 ? 50 GLY A O 1 ATOM 311 N N . ILE A 1 51 ? -46.483 -0.287 58.366 1.00 20.72 ? 51 ILE A N 1 ATOM 312 C CA . ILE A 1 51 ? -45.355 0.652 58.454 1.00 20.63 ? 51 ILE A CA 1 ATOM 313 C C . ILE A 1 51 ? -44.052 -0.132 58.218 1.00 21.38 ? 51 ILE A C 1 ATOM 314 O O . ILE A 1 51 ? -43.714 -1.010 59.016 1.00 22.18 ? 51 ILE A O 1 ATOM 315 C CB . ILE A 1 51 ? -45.310 1.378 59.817 1.00 20.62 ? 51 ILE A CB 1 ATOM 316 C CG1 . ILE A 1 51 ? -46.510 2.307 59.947 1.00 21.23 ? 51 ILE A CG1 1 ATOM 317 C CG2 . ILE A 1 51 ? -44.026 2.213 59.972 1.00 21.00 ? 51 ILE A CG2 1 ATOM 318 C CD1 . ILE A 1 51 ? -46.719 2.899 61.325 1.00 21.17 ? 51 ILE A CD1 1 ATOM 319 N N . CYS A 1 52 ? -43.336 0.189 57.136 1.00 20.90 ? 52 CYS A N 1 ATOM 320 C CA . CYS A 1 52 ? -42.062 -0.469 56.826 1.00 21.77 ? 52 CYS A CA 1 ATOM 321 C C . CYS A 1 52 ? -40.978 -0.046 57.821 1.00 21.12 ? 52 CYS A C 1 ATOM 322 O O . CYS A 1 52 ? -40.834 1.141 58.118 1.00 20.30 ? 52 CYS A O 1 ATOM 323 C CB . CYS A 1 52 ? -41.633 -0.137 55.409 1.00 23.29 ? 52 CYS A CB 1 ATOM 324 S SG . CYS A 1 52 ? -42.734 -0.880 54.160 1.00 26.68 ? 52 CYS A SG 1 ATOM 325 N N . ASP A 1 53 ? -40.213 -1.025 58.306 1.00 20.82 ? 53 ASP A N 1 ATOM 326 C CA . ASP A 1 53 ? -39.211 -0.777 59.340 1.00 21.53 ? 53 ASP A CA 1 ATOM 327 C C . ASP A 1 53 ? -37.918 -0.204 58.778 1.00 20.50 ? 53 ASP A C 1 ATOM 328 O O . ASP A 1 53 ? -36.993 0.085 59.533 1.00 21.20 ? 53 ASP A O 1 ATOM 329 C CB . ASP A 1 53 ? -38.933 -2.059 60.143 1.00 22.58 ? 53 ASP A CB 1 ATOM 330 C CG . ASP A 1 53 ? -38.198 -3.135 59.343 1.00 23.79 ? 53 ASP A CG 1 ATOM 331 O OD1 . ASP A 1 53 ? -37.844 -2.942 58.155 1.00 24.46 ? 53 ASP A OD1 1 ATOM 332 O OD2 . ASP A 1 53 ? -37.971 -4.229 59.931 1.00 26.24 ? 53 ASP A OD2 1 ATOM 333 N N . SER A 1 54 ? -37.854 -0.040 57.468 1.00 19.48 ? 54 SER A N 1 ATOM 334 C CA . SER A 1 54 ? -36.739 0.614 56.791 1.00 19.36 ? 54 SER A CA 1 ATOM 335 C C . SER A 1 54 ? -37.256 1.697 55.838 1.00 19.36 ? 54 SER A C 1 ATOM 336 O O . SER A 1 54 ? -38.388 1.560 55.321 1.00 18.55 ? 54 SER A O 1 ATOM 337 C CB . SER A 1 54 ? -35.949 -0.436 56.022 1.00 19.82 ? 54 SER A CB 1 ATOM 338 O OG . SER A 1 54 ? -35.672 -1.562 56.836 1.00 20.09 ? 54 SER A OG 1 ATOM 339 N N . PRO A 1 55 ? -36.454 2.754 55.572 1.00 18.86 ? 55 PRO A N 1 ATOM 340 C CA . PRO A 1 55 ? -35.114 3.014 56.051 1.00 19.49 ? 55 PRO A CA 1 ATOM 341 C C . PRO A 1 55 ? -35.017 3.888 57.310 1.00 19.02 ? 55 PRO A C 1 ATOM 342 O O . PRO A 1 55 ? -33.886 4.193 57.739 1.00 19.46 ? 55 PRO A O 1 ATOM 343 C CB . PRO A 1 55 ? -34.486 3.758 54.885 1.00 19.50 ? 55 PRO A CB 1 ATOM 344 C CG . PRO A 1 55 ? -35.617 4.641 54.396 1.00 19.30 ? 55 PRO A CG 1 ATOM 345 C CD . PRO A 1 55 ? -36.859 3.784 54.597 1.00 19.21 ? 55 PRO A CD 1 ATOM 346 N N . HIS A 1 56 ? -36.149 4.272 57.894 1.00 17.50 ? 56 HIS A N 1 ATOM 347 C CA . HIS A 1 56 ? -36.181 5.059 59.117 1.00 17.52 ? 56 HIS A CA 1 ATOM 348 C C . HIS A 1 56 ? -36.128 4.148 60.301 1.00 17.83 ? 56 HIS A C 1 ATOM 349 O O . HIS A 1 56 ? -36.647 3.014 60.270 1.00 17.88 ? 56 HIS A O 1 ATOM 350 C CB . HIS A 1 56 ? -37.447 5.917 59.183 1.00 17.36 ? 56 HIS A CB 1 ATOM 351 C CG . HIS A 1 56 ? -37.656 6.770 57.959 1.00 17.46 ? 56 HIS A CG 1 ATOM 352 N ND1 . HIS A 1 56 ? -36.838 7.813 57.642 1.00 17.49 ? 56 HIS A ND1 1 ATOM 353 C CD2 . HIS A 1 56 ? -38.608 6.694 56.951 1.00 17.68 ? 56 HIS A CD2 1 ATOM 354 C CE1 . HIS A 1 56 ? -37.268 8.378 56.501 1.00 18.06 ? 56 HIS A CE1 1 ATOM 355 N NE2 . HIS A 1 56 ? -38.352 7.695 56.078 1.00 17.64 ? 56 HIS A NE2 1 ATOM 356 N N . GLN A 1 57 ? -35.497 4.614 61.371 1.00 17.18 ? 57 GLN A N 1 ATOM 357 C CA . GLN A 1 57 ? -35.478 3.857 62.607 1.00 17.16 ? 57 GLN A CA 1 ATOM 358 C C . GLN A 1 57 ? -36.797 3.993 63.347 1.00 16.92 ? 57 GLN A C 1 ATOM 359 O O . GLN A 1 57 ? -37.147 5.072 63.847 1.00 17.03 ? 57 GLN A O 1 ATOM 360 C CB . GLN A 1 57 ? -34.342 4.304 63.529 1.00 17.05 ? 57 GLN A CB 1 ATOM 361 C CG . GLN A 1 57 ? -34.251 3.442 64.789 1.00 17.29 ? 57 GLN A CG 1 ATOM 362 C CD . GLN A 1 57 ? -33.073 3.787 65.665 1.00 17.79 ? 57 GLN A CD 1 ATOM 363 O OE1 . GLN A 1 57 ? -32.629 4.940 65.710 1.00 18.14 ? 57 GLN A OE1 1 ATOM 364 N NE2 . GLN A 1 57 ? -32.578 2.795 66.409 1.00 17.43 ? 57 GLN A NE2 1 ATOM 365 N N . ILE A 1 58 ? -37.514 2.886 63.426 1.00 17.33 ? 58 ILE A N 1 ATOM 366 C CA . ILE A 1 58 ? -38.842 2.847 64.013 1.00 18.15 ? 58 ILE A CA 1 ATOM 367 C C . ILE A 1 58 ? -38.760 2.310 65.418 1.00 18.86 ? 58 ILE A C 1 ATOM 368 O O . ILE A 1 58 ? -38.047 1.313 65.671 1.00 20.46 ? 58 ILE A O 1 ATOM 369 C CB . ILE A 1 58 ? -39.786 1.928 63.212 1.00 19.12 ? 58 ILE A CB 1 ATOM 370 C CG1 . ILE A 1 58 ? -39.828 2.348 61.743 1.00 19.45 ? 58 ILE A CG1 1 ATOM 371 C CG2 . ILE A 1 58 ? -41.196 1.955 63.824 1.00 19.83 ? 58 ILE A CG2 1 ATOM 372 C CD1 . ILE A 1 58 ? -40.327 3.761 61.476 1.00 19.45 ? 58 ILE A CD1 1 ATOM 373 N N . LEU A 1 59 ? -39.444 2.956 66.354 1.00 18.13 ? 59 LEU A N 1 ATOM 374 C CA . LEU A 1 59 ? -39.608 2.405 67.701 1.00 19.21 ? 59 LEU A CA 1 ATOM 375 C C . LEU A 1 59 ? -41.080 2.237 67.989 1.00 19.66 ? 59 LEU A C 1 ATOM 376 O O . LEU A 1 59 ? -41.801 3.213 68.124 1.00 19.44 ? 59 LEU A O 1 ATOM 377 C CB . LEU A 1 59 ? -38.960 3.287 68.759 1.00 19.44 ? 59 LEU A CB 1 ATOM 378 C CG . LEU A 1 59 ? -38.947 2.811 70.216 1.00 20.34 ? 59 LEU A CG 1 ATOM 379 C CD1 . LEU A 1 59 ? -38.533 1.346 70.300 1.00 21.19 ? 59 LEU A CD1 1 ATOM 380 C CD2 . LEU A 1 59 ? -38.027 3.687 71.064 1.00 19.83 ? 59 LEU A CD2 1 ATOM 381 N N . ASP A 1 60 ? -41.513 0.985 68.064 1.00 19.72 ? 60 ASP A N 1 ATOM 382 C CA . ASP A 1 60 ? -42.911 0.660 68.359 1.00 20.20 ? 60 ASP A CA 1 ATOM 383 C C . ASP A 1 60 ? -43.123 0.714 69.859 1.00 20.37 ? 60 ASP A C 1 ATOM 384 O O . ASP A 1 60 ? -42.525 -0.070 70.595 1.00 20.57 ? 60 ASP A O 1 ATOM 385 C CB . ASP A 1 60 ? -43.205 -0.750 67.861 1.00 20.73 ? 60 ASP A CB 1 ATOM 386 C CG . ASP A 1 60 ? -44.679 -1.130 67.957 1.00 21.26 ? 60 ASP A CG 1 ATOM 387 O OD1 . ASP A 1 60 ? -45.442 -0.480 68.699 1.00 21.80 ? 60 ASP A OD1 1 ATOM 388 O OD2 . ASP A 1 60 ? -45.067 -2.097 67.260 1.00 22.11 ? 60 ASP A OD2 1 ATOM 389 N N . GLY A 1 61 ? -43.949 1.642 70.322 1.00 20.12 ? 61 GLY A N 1 ATOM 390 C CA . GLY A 1 61 ? -44.198 1.808 71.742 1.00 20.69 ? 61 GLY A CA 1 ATOM 391 C C . GLY A 1 61 ? -44.961 0.658 72.388 1.00 21.70 ? 61 GLY A C 1 ATOM 392 O O . GLY A 1 61 ? -44.942 0.518 73.599 1.00 22.06 ? 61 GLY A O 1 ATOM 393 N N . GLU A 1 62 ? -45.620 -0.167 71.583 1.00 22.80 ? 62 GLU A N 1 ATOM 394 C CA . GLU A 1 62 ? -46.421 -1.289 72.088 1.00 24.61 ? 62 GLU A CA 1 ATOM 395 C C . GLU A 1 62 ? -47.392 -0.787 73.157 1.00 24.19 ? 62 GLU A C 1 ATOM 396 O O . GLU A 1 62 ? -48.232 0.060 72.855 1.00 23.08 ? 62 GLU A O 1 ATOM 397 C CB . GLU A 1 62 ? -45.497 -2.432 72.542 1.00 27.14 ? 62 GLU A CB 1 ATOM 398 C CG . GLU A 1 62 ? -44.611 -2.894 71.385 1.00 30.09 ? 62 GLU A CG 1 ATOM 399 C CD . GLU A 1 62 ? -43.803 -4.142 71.655 1.00 34.74 ? 62 GLU A CD 1 ATOM 400 O OE1 . GLU A 1 62 ? -42.726 -4.044 72.284 1.00 38.81 ? 62 GLU A OE1 1 ATOM 401 O OE2 . GLU A 1 62 ? -44.220 -5.218 71.176 1.00 39.44 ? 62 GLU A OE2 1 ATOM 402 N N . ASN A 1 63 ? -47.292 -1.256 74.399 1.00 24.63 ? 63 ASN A N 1 ATOM 403 C CA . ASN A 1 63 ? -48.222 -0.785 75.435 1.00 25.96 ? 63 ASN A CA 1 ATOM 404 C C . ASN A 1 63 ? -47.828 0.531 76.117 1.00 24.85 ? 63 ASN A C 1 ATOM 405 O O . ASN A 1 63 ? -48.511 0.978 77.038 1.00 24.13 ? 63 ASN A O 1 ATOM 406 C CB . ASN A 1 63 ? -48.373 -1.843 76.522 1.00 28.47 ? 63 ASN A CB 1 ATOM 407 C CG . ASN A 1 63 ? -49.186 -3.027 76.078 1.00 31.81 ? 63 ASN A CG 1 ATOM 408 O OD1 . ASN A 1 63 ? -50.096 -2.922 75.248 1.00 31.73 ? 63 ASN A OD1 1 ATOM 409 N ND2 . ASN A 1 63 ? -48.865 -4.176 76.653 1.00 35.98 ? 63 ASN A ND2 1 ATOM 410 N N . CYS A 1 64 ? -46.728 1.140 75.678 1.00 24.27 ? 64 CYS A N 1 ATOM 411 C CA . CYS A 1 64 ? -46.174 2.309 76.327 1.00 24.46 ? 64 CYS A CA 1 ATOM 412 C C . CYS A 1 64 ? -46.306 3.555 75.455 1.00 23.15 ? 64 CYS A C 1 ATOM 413 O O . CYS A 1 64 ? -45.968 3.521 74.265 1.00 22.24 ? 64 CYS A O 1 ATOM 414 C CB . CYS A 1 64 ? -44.686 2.094 76.598 1.00 26.92 ? 64 CYS A CB 1 ATOM 415 S SG . CYS A 1 64 ? -44.283 0.734 77.749 1.00 29.86 ? 64 CYS A SG 1 ATOM 416 N N . THR A 1 65 ? -46.741 4.653 76.062 1.00 21.60 ? 65 THR A N 1 ATOM 417 C CA . THR A 1 65 ? -46.567 5.966 75.456 1.00 20.77 ? 65 THR A CA 1 ATOM 418 C C . THR A 1 65 ? -45.105 6.374 75.608 1.00 19.76 ? 65 THR A C 1 ATOM 419 O O . THR A 1 65 ? -44.377 5.822 76.448 1.00 20.34 ? 65 THR A O 1 ATOM 420 C CB . THR A 1 65 ? -47.442 7.012 76.143 1.00 20.73 ? 65 THR A CB 1 ATOM 421 O OG1 . THR A 1 65 ? -47.031 7.111 77.515 1.00 21.13 ? 65 THR A OG1 1 ATOM 422 C CG2 . THR A 1 65 ? -48.962 6.630 76.051 1.00 21.89 ? 65 THR A CG2 1 ATOM 423 N N . LEU A 1 66 ? -44.683 7.360 74.828 1.00 19.41 ? 66 LEU A N 1 ATOM 424 C CA . LEU A 1 66 ? -43.337 7.922 74.979 1.00 18.74 ? 66 LEU A CA 1 ATOM 425 C C . LEU A 1 66 ? -43.113 8.407 76.411 1.00 18.93 ? 66 LEU A C 1 ATOM 426 O O . LEU A 1 66 ? -42.053 8.146 77.002 1.00 18.27 ? 66 LEU A O 1 ATOM 427 C CB . LEU A 1 66 ? -43.117 9.077 73.994 1.00 18.38 ? 66 LEU A CB 1 ATOM 428 C CG . LEU A 1 66 ? -41.756 9.781 74.050 1.00 18.51 ? 66 LEU A CG 1 ATOM 429 C CD1 . LEU A 1 66 ? -40.617 8.749 73.979 1.00 18.55 ? 66 LEU A CD1 1 ATOM 430 C CD2 . LEU A 1 66 ? -41.640 10.848 72.936 1.00 17.88 ? 66 LEU A CD2 1 ATOM 431 N N . ILE A 1 67 ? -44.096 9.112 76.973 1.00 19.62 ? 67 ILE A N 1 ATOM 432 C CA . ILE A 1 67 ? -43.925 9.662 78.331 1.00 20.39 ? 67 ILE A CA 1 ATOM 433 C C . ILE A 1 67 ? -43.817 8.521 79.347 1.00 20.49 ? 67 ILE A C 1 ATOM 434 O O . ILE A 1 67 ? -42.989 8.594 80.266 1.00 20.78 ? 67 ILE A O 1 ATOM 435 C CB . ILE A 1 67 ? -45.022 10.707 78.696 1.00 20.91 ? 67 ILE A CB 1 ATOM 436 C CG1 . ILE A 1 67 ? -44.899 11.993 77.851 1.00 21.60 ? 67 ILE A CG1 1 ATOM 437 C CG2 . ILE A 1 67 ? -44.994 11.079 80.175 1.00 20.84 ? 67 ILE A CG2 1 ATOM 438 C CD1 . ILE A 1 67 ? -43.523 12.603 77.761 1.00 23.02 ? 67 ILE A CD1 1 ATOM 439 N N . ASP A 1 68 ? -44.559 7.429 79.169 1.00 20.86 ? 68 ASP A N 1 ATOM 440 C CA . ASP A 1 68 ? -44.379 6.275 80.090 1.00 22.14 ? 68 ASP A CA 1 ATOM 441 C C . ASP A 1 68 ? -42.979 5.681 79.987 1.00 21.46 ? 68 ASP A C 1 ATOM 442 O O . ASP A 1 68 ? -42.363 5.310 81.012 1.00 21.45 ? 68 ASP A O 1 ATOM 443 C CB . ASP A 1 68 ? -45.450 5.199 79.890 1.00 23.27 ? 68 ASP A CB 1 ATOM 444 C CG . ASP A 1 68 ? -46.781 5.574 80.547 1.00 26.32 ? 68 ASP A CG 1 ATOM 445 O OD1 . ASP A 1 68 ? -46.813 6.467 81.400 1.00 28.98 ? 68 ASP A OD1 1 ATOM 446 O OD2 . ASP A 1 68 ? -47.817 5.010 80.188 1.00 31.75 ? 68 ASP A OD2 1 ATOM 447 N N . ALA A 1 69 ? -42.465 5.600 78.766 1.00 21.00 ? 69 ALA A N 1 ATOM 448 C CA . ALA A 1 69 ? -41.116 5.098 78.532 1.00 21.52 ? 69 ALA A CA 1 ATOM 449 C C . ALA A 1 69 ? -40.056 6.045 79.118 1.00 21.34 ? 69 ALA A C 1 ATOM 450 O O . ALA A 1 69 ? -39.020 5.580 79.606 1.00 22.66 ? 69 ALA A O 1 ATOM 451 C CB . ALA A 1 69 ? -40.878 4.884 77.043 1.00 21.53 ? 69 ALA A CB 1 ATOM 452 N N . LEU A 1 70 ? -40.325 7.357 79.073 1.00 20.50 ? 70 LEU A N 1 ATOM 453 C CA . LEU A 1 70 ? -39.442 8.369 79.649 1.00 20.51 ? 70 LEU A CA 1 ATOM 454 C C . LEU A 1 70 ? -39.337 8.232 81.180 1.00 21.50 ? 70 LEU A C 1 ATOM 455 O O . LEU A 1 70 ? -38.241 8.130 81.734 1.00 21.42 ? 70 LEU A O 1 ATOM 456 C CB . LEU A 1 70 ? -39.939 9.775 79.282 1.00 19.77 ? 70 LEU A CB 1 ATOM 457 C CG . LEU A 1 70 ? -39.193 11.015 79.789 1.00 19.36 ? 70 LEU A CG 1 ATOM 458 C CD1 . LEU A 1 70 ? -37.942 11.256 78.945 1.00 18.57 ? 70 LEU A CD1 1 ATOM 459 C CD2 . LEU A 1 70 ? -40.055 12.281 79.795 1.00 19.23 ? 70 LEU A CD2 1 ATOM 460 N N . LEU A 1 71 ? -40.482 8.217 81.843 1.00 21.45 ? 71 LEU A N 1 ATOM 461 C CA . LEU A 1 71 ? -40.525 8.132 83.297 1.00 22.44 ? 71 LEU A CA 1 ATOM 462 C C . LEU A 1 71 ? -39.993 6.786 83.783 1.00 22.75 ? 71 LEU A C 1 ATOM 463 O O . LEU A 1 71 ? -39.389 6.715 84.842 1.00 23.01 ? 71 LEU A O 1 ATOM 464 C CB . LEU A 1 71 ? -41.954 8.348 83.796 1.00 22.80 ? 71 LEU A CB 1 ATOM 465 C CG . LEU A 1 71 ? -42.636 9.671 83.427 1.00 23.74 ? 71 LEU A CG 1 ATOM 466 C CD1 . LEU A 1 71 ? -44.007 9.740 84.083 1.00 24.53 ? 71 LEU A CD1 1 ATOM 467 C CD2 . LEU A 1 71 ? -41.797 10.878 83.830 1.00 24.28 ? 71 LEU A CD2 1 ATOM 468 N N . GLY A 1 72 ? -40.218 5.731 83.006 1.00 22.74 ? 72 GLY A N 1 ATOM 469 C CA . GLY A 1 72 ? -39.709 4.400 83.328 1.00 23.42 ? 72 GLY A CA 1 ATOM 470 C C . GLY A 1 72 ? -40.708 3.492 84.027 1.00 25.13 ? 72 GLY A C 1 ATOM 471 O O . GLY A 1 72 ? -40.362 2.808 85.006 1.00 24.45 ? 72 GLY A O 1 ATOM 472 N N . ASP A 1 73 ? -41.943 3.490 83.516 1.00 25.31 ? 73 ASP A N 1 ATOM 473 C CA . ASP A 1 73 ? -42.973 2.518 83.890 1.00 27.29 ? 73 ASP A CA 1 ATOM 474 C C . ASP A 1 73 ? -42.368 1.115 83.673 1.00 27.79 ? 73 ASP A C 1 ATOM 475 O O . ASP A 1 73 ? -41.703 0.876 82.669 1.00 27.17 ? 73 ASP A O 1 ATOM 476 C CB . ASP A 1 73 ? -44.207 2.789 83.016 1.00 27.85 ? 73 ASP A CB 1 ATOM 477 C CG . ASP A 1 73 ? -45.416 1.932 83.364 1.00 30.78 ? 73 ASP A CG 1 ATOM 478 O OD1 . ASP A 1 73 ? -45.255 0.813 83.890 1.00 34.53 ? 73 ASP A OD1 1 ATOM 479 O OD2 . ASP A 1 73 ? -46.539 2.388 83.096 1.00 31.07 ? 73 ASP A OD2 1 ATOM 480 N N . PRO A 1 74 ? -42.514 0.199 84.652 1.00 30.39 ? 74 PRO A N 1 ATOM 481 C CA . PRO A 1 74 ? -41.864 -1.114 84.522 1.00 30.97 ? 74 PRO A CA 1 ATOM 482 C C . PRO A 1 74 ? -42.081 -1.851 83.199 1.00 31.09 ? 74 PRO A C 1 ATOM 483 O O . PRO A 1 74 ? -41.120 -2.412 82.648 1.00 31.78 ? 74 PRO A O 1 ATOM 484 C CB . PRO A 1 74 ? -42.452 -1.902 85.701 1.00 33.10 ? 74 PRO A CB 1 ATOM 485 C CG . PRO A 1 74 ? -42.618 -0.852 86.754 1.00 32.58 ? 74 PRO A CG 1 ATOM 486 C CD . PRO A 1 74 ? -43.022 0.414 86.022 1.00 31.50 ? 74 PRO A CD 1 ATOM 487 N N . GLN A 1 75 ? -43.294 -1.809 82.657 1.00 31.29 ? 75 GLN A N 1 ATOM 488 C CA . GLN A 1 75 ? -43.534 -2.459 81.363 1.00 31.96 ? 75 GLN A CA 1 ATOM 489 C C . GLN A 1 75 ? -42.747 -1.835 80.210 1.00 29.58 ? 75 GLN A C 1 ATOM 490 O O . GLN A 1 75 ? -42.669 -2.434 79.145 1.00 28.56 ? 75 GLN A O 1 ATOM 491 C CB . GLN A 1 75 ? -45.021 -2.551 81.022 1.00 33.31 ? 75 GLN A CB 1 ATOM 492 C CG . GLN A 1 75 ? -45.703 -1.253 80.674 1.00 34.58 ? 75 GLN A CG 1 ATOM 493 C CD . GLN A 1 75 ? -47.208 -1.412 80.555 1.00 37.20 ? 75 GLN A CD 1 ATOM 494 O OE1 . GLN A 1 75 ? -47.727 -2.520 80.634 1.00 40.48 ? 75 GLN A OE1 1 ATOM 495 N NE2 . GLN A 1 75 ? -47.915 -0.302 80.377 1.00 35.70 ? 75 GLN A NE2 1 ATOM 496 N N . CYS A 1 76 ? -42.144 -0.665 80.437 1.00 27.99 ? 76 CYS A N 1 ATOM 497 C CA . CYS A 1 76 ? -41.356 0.020 79.421 1.00 27.25 ? 76 CYS A CA 1 ATOM 498 C C . CYS A 1 76 ? -39.851 -0.086 79.649 1.00 26.49 ? 76 CYS A C 1 ATOM 499 O O . CYS A 1 76 ? -39.081 0.616 78.991 1.00 24.95 ? 76 CYS A O 1 ATOM 500 C CB . CYS A 1 76 ? -41.733 1.504 79.357 1.00 28.30 ? 76 CYS A CB 1 ATOM 501 S SG . CYS A 1 76 ? -43.503 1.810 79.386 1.00 29.93 ? 76 CYS A SG 1 ATOM 502 N N . ASP A 1 77 ? -39.412 -0.979 80.535 1.00 25.66 ? 77 ASP A N 1 ATOM 503 C CA . ASP A 1 77 ? -37.982 -1.082 80.843 1.00 26.09 ? 77 ASP A CA 1 ATOM 504 C C . ASP A 1 77 ? -37.119 -1.407 79.620 1.00 24.93 ? 77 ASP A C 1 ATOM 505 O O . ASP A 1 77 ? -35.965 -0.972 79.528 1.00 24.84 ? 77 ASP A O 1 ATOM 506 C CB . ASP A 1 77 ? -37.740 -2.131 81.935 1.00 27.12 ? 77 ASP A CB 1 ATOM 507 C CG . ASP A 1 77 ? -38.147 -1.652 83.321 1.00 28.65 ? 77 ASP A CG 1 ATOM 508 O OD1 . ASP A 1 77 ? -38.368 -0.437 83.533 1.00 28.65 ? 77 ASP A OD1 1 ATOM 509 O OD2 . ASP A 1 77 ? -38.197 -2.502 84.234 1.00 28.17 ? 77 ASP A OD2 1 ATOM 510 N N . GLY A 1 78 ? -37.680 -2.163 78.681 1.00 25.17 ? 78 GLY A N 1 ATOM 511 C CA . GLY A 1 78 ? -36.969 -2.532 77.460 1.00 25.18 ? 78 GLY A CA 1 ATOM 512 C C . GLY A 1 78 ? -36.618 -1.347 76.555 1.00 24.67 ? 78 GLY A C 1 ATOM 513 O O . GLY A 1 78 ? -35.752 -1.478 75.677 1.00 24.82 ? 78 GLY A O 1 ATOM 514 N N . PHE A 1 79 ? -37.263 -0.199 76.777 1.00 24.16 ? 79 PHE A N 1 ATOM 515 C CA . PHE A 1 79 ? -37.008 1.002 75.967 1.00 23.91 ? 79 PHE A CA 1 ATOM 516 C C . PHE A 1 79 ? -35.820 1.837 76.456 1.00 22.35 ? 79 PHE A C 1 ATOM 517 O O . PHE A 1 79 ? -35.462 2.840 75.824 1.00 20.88 ? 79 PHE A O 1 ATOM 518 C CB . PHE A 1 79 ? -38.245 1.917 75.934 1.00 26.24 ? 79 PHE A CB 1 ATOM 519 C CG . PHE A 1 79 ? -39.432 1.331 75.220 1.00 28.29 ? 79 PHE A CG 1 ATOM 520 C CD1 . PHE A 1 79 ? -40.344 0.543 75.895 1.00 30.30 ? 79 PHE A CD1 1 ATOM 521 C CD2 . PHE A 1 79 ? -39.674 1.620 73.894 1.00 31.61 ? 79 PHE A CD2 1 ATOM 522 C CE1 . PHE A 1 79 ? -41.453 0.015 75.250 1.00 30.12 ? 79 PHE A CE1 1 ATOM 523 C CE2 . PHE A 1 79 ? -40.786 1.087 73.241 1.00 31.81 ? 79 PHE A CE2 1 ATOM 524 C CZ . PHE A 1 79 ? -41.670 0.278 73.925 1.00 29.77 ? 79 PHE A CZ 1 ATOM 525 N N . GLN A 1 80 ? -35.210 1.474 77.585 1.00 21.54 ? 80 GLN A N 1 ATOM 526 C CA . GLN A 1 80 ? -34.185 2.337 78.162 1.00 21.19 ? 80 GLN A CA 1 ATOM 527 C C . GLN A 1 80 ? -33.099 2.690 77.157 1.00 20.73 ? 80 GLN A C 1 ATOM 528 O O . GLN A 1 80 ? -32.557 1.814 76.488 1.00 20.13 ? 80 GLN A O 1 ATOM 529 C CB . GLN A 1 80 ? -33.549 1.705 79.413 1.00 21.97 ? 80 GLN A CB 1 ATOM 530 C CG . GLN A 1 80 ? -34.442 1.750 80.641 1.00 22.92 ? 80 GLN A CG 1 ATOM 531 C CD . GLN A 1 80 ? -33.677 1.432 81.922 1.00 24.82 ? 80 GLN A CD 1 ATOM 532 O OE1 . GLN A 1 80 ? -32.531 0.965 81.876 1.00 25.15 ? 80 GLN A OE1 1 ATOM 533 N NE2 . GLN A 1 80 ? -34.296 1.717 83.069 1.00 25.56 ? 80 GLN A NE2 1 ATOM 534 N N . ASN A 1 81 ? -32.803 3.983 77.055 1.00 20.27 ? 81 ASN A N 1 ATOM 535 C CA . ASN A 1 81 ? -31.712 4.504 76.236 1.00 20.86 ? 81 ASN A CA 1 ATOM 536 C C . ASN A 1 81 ? -31.857 4.367 74.718 1.00 20.59 ? 81 ASN A C 1 ATOM 537 O O . ASN A 1 81 ? -30.930 4.680 73.977 1.00 21.16 ? 81 ASN A O 1 ATOM 538 C CB . ASN A 1 81 ? -30.371 3.925 76.690 1.00 21.83 ? 81 ASN A CB 1 ATOM 539 C CG . ASN A 1 81 ? -30.060 4.276 78.129 1.00 22.39 ? 81 ASN A CG 1 ATOM 540 O OD1 . ASN A 1 81 ? -29.992 5.451 78.486 1.00 22.93 ? 81 ASN A OD1 1 ATOM 541 N ND2 . ASN A 1 81 ? -29.900 3.261 78.967 1.00 23.13 ? 81 ASN A ND2 1 ATOM 542 N N . LYS A 1 82 ? -33.012 3.921 74.249 1.00 20.54 ? 82 LYS A N 1 ATOM 543 C CA . LYS A 1 82 ? -33.202 3.725 72.809 1.00 21.00 ? 82 LYS A CA 1 ATOM 544 C C . LYS A 1 82 ? -33.380 5.053 72.085 1.00 19.67 ? 82 LYS A C 1 ATOM 545 O O . LYS A 1 82 ? -33.792 6.047 72.693 1.00 19.25 ? 82 LYS A O 1 ATOM 546 C CB . LYS A 1 82 ? -34.416 2.828 72.544 1.00 22.53 ? 82 LYS A CB 1 ATOM 547 C CG . LYS A 1 82 ? -34.201 1.385 72.935 1.00 24.69 ? 82 LYS A CG 1 ATOM 548 C CD . LYS A 1 82 ? -35.416 0.509 72.653 1.00 26.15 ? 82 LYS A CD 1 ATOM 549 C CE . LYS A 1 82 ? -35.447 -0.049 71.237 1.00 27.12 ? 82 LYS A CE 1 ATOM 550 N NZ . LYS A 1 82 ? -36.171 -1.352 71.248 1.00 30.21 ? 82 LYS A NZ 1 ATOM 551 N N . LYS A 1 83 ? -33.077 5.041 70.788 1.00 19.09 ? 83 LYS A N 1 ATOM 552 C CA . LYS A 1 83 ? -33.281 6.170 69.888 1.00 18.86 ? 83 LYS A CA 1 ATOM 553 C C . LYS A 1 83 ? -34.270 5.784 68.782 1.00 18.32 ? 83 LYS A C 1 ATOM 554 O O . LYS A 1 83 ? -34.593 4.592 68.576 1.00 17.66 ? 83 LYS A O 1 ATOM 555 C CB . LYS A 1 83 ? -31.956 6.639 69.269 1.00 19.98 ? 83 LYS A CB 1 ATOM 556 C CG . LYS A 1 83 ? -30.848 6.966 70.268 1.00 20.63 ? 83 LYS A CG 1 ATOM 557 C CD . LYS A 1 83 ? -29.670 7.631 69.569 1.00 21.80 ? 83 LYS A CD 1 ATOM 558 C CE . LYS A 1 83 ? -28.384 7.595 70.395 1.00 23.40 ? 83 LYS A CE 1 ATOM 559 N NZ . LYS A 1 83 ? -27.702 6.268 70.450 1.00 23.48 ? 83 LYS A NZ 1 ATOM 560 N N . TRP A 1 84 ? -34.739 6.797 68.065 1.00 17.41 ? 84 TRP A N 1 ATOM 561 C CA . TRP A 1 84 ? -35.687 6.588 66.964 1.00 16.54 ? 84 TRP A CA 1 ATOM 562 C C . TRP A 1 84 ? -35.627 7.738 66.023 1.00 16.04 ? 84 TRP A C 1 ATOM 563 O O . TRP A 1 84 ? -35.235 8.851 66.396 1.00 15.78 ? 84 TRP A O 1 ATOM 564 C CB . TRP A 1 84 ? -37.125 6.429 67.462 1.00 16.46 ? 84 TRP A CB 1 ATOM 565 C CG . TRP A 1 84 ? -37.602 7.634 68.230 1.00 16.29 ? 84 TRP A CG 1 ATOM 566 C CD1 . TRP A 1 84 ? -38.284 8.752 67.749 1.00 15.80 ? 84 TRP A CD1 1 ATOM 567 C CD2 . TRP A 1 84 ? -37.390 7.900 69.645 1.00 16.41 ? 84 TRP A CD2 1 ATOM 568 N NE1 . TRP A 1 84 ? -38.508 9.644 68.748 1.00 16.06 ? 84 TRP A NE1 1 ATOM 569 C CE2 . TRP A 1 84 ? -38.014 9.189 69.919 1.00 16.51 ? 84 TRP A CE2 1 ATOM 570 C CE3 . TRP A 1 84 ? -36.814 7.203 70.684 1.00 16.72 ? 84 TRP A CE3 1 ATOM 571 C CZ2 . TRP A 1 84 ? -37.997 9.757 71.192 1.00 16.61 ? 84 TRP A CZ2 1 ATOM 572 C CZ3 . TRP A 1 84 ? -36.801 7.778 71.952 1.00 16.90 ? 84 TRP A CZ3 1 ATOM 573 C CH2 . TRP A 1 84 ? -37.361 9.036 72.195 1.00 17.32 ? 84 TRP A CH2 1 ATOM 574 N N . ASP A 1 85 ? -36.010 7.466 64.792 1.00 15.83 ? 85 ASP A N 1 ATOM 575 C CA . ASP A 1 85 ? -36.470 8.492 63.872 1.00 15.54 ? 85 ASP A CA 1 ATOM 576 C C . ASP A 1 85 ? -37.965 8.705 64.092 1.00 15.60 ? 85 ASP A C 1 ATOM 577 O O . ASP A 1 85 ? -38.435 9.851 64.110 1.00 15.36 ? 85 ASP A O 1 ATOM 578 C CB . ASP A 1 85 ? -36.198 8.082 62.422 1.00 15.78 ? 85 ASP A CB 1 ATOM 579 C CG . ASP A 1 85 ? -34.709 8.010 62.081 1.00 16.95 ? 85 ASP A CG 1 ATOM 580 O OD1 . ASP A 1 85 ? -33.931 8.802 62.667 1.00 17.27 ? 85 ASP A OD1 1 ATOM 581 O OD2 . ASP A 1 85 ? -34.338 7.175 61.204 1.00 16.89 ? 85 ASP A OD2 1 ATOM 582 N N . LEU A 1 86 ? -38.717 7.611 64.205 1.00 15.42 ? 86 LEU A N 1 ATOM 583 C CA . LEU A 1 86 ? -40.156 7.682 64.447 1.00 15.30 ? 86 LEU A CA 1 ATOM 584 C C . LEU A 1 86 ? -40.601 6.751 65.549 1.00 15.59 ? 86 LEU A C 1 ATOM 585 O O . LEU A 1 86 ? -40.416 5.534 65.476 1.00 16.06 ? 86 LEU A O 1 ATOM 586 C CB . LEU A 1 86 ? -40.953 7.386 63.153 1.00 14.78 ? 86 LEU A CB 1 ATOM 587 C CG . LEU A 1 86 ? -42.462 7.677 63.271 1.00 14.78 ? 86 LEU A CG 1 ATOM 588 C CD1 . LEU A 1 86 ? -42.734 9.177 63.477 1.00 14.51 ? 86 LEU A CD1 1 ATOM 589 C CD2 . LEU A 1 86 ? -43.174 7.180 62.019 1.00 14.66 ? 86 LEU A CD2 1 ATOM 590 N N . PHE A 1 87 ? -41.149 7.355 66.604 1.00 16.26 ? 87 PHE A N 1 ATOM 591 C CA . PHE A 1 87 ? -41.738 6.641 67.711 1.00 16.88 ? 87 PHE A CA 1 ATOM 592 C C . PHE A 1 87 ? -43.206 6.449 67.376 1.00 16.87 ? 87 PHE A C 1 ATOM 593 O O . PHE A 1 87 ? -43.902 7.420 67.056 1.00 16.20 ? 87 PHE A O 1 ATOM 594 C CB . PHE A 1 87 ? -41.597 7.423 69.012 1.00 17.58 ? 87 PHE A CB 1 ATOM 595 C CG . PHE A 1 87 ? -41.968 6.630 70.247 1.00 18.38 ? 87 PHE A CG 1 ATOM 596 C CD1 . PHE A 1 87 ? -43.288 6.348 70.550 1.00 18.45 ? 87 PHE A CD1 1 ATOM 597 C CD2 . PHE A 1 87 ? -40.975 6.130 71.104 1.00 19.34 ? 87 PHE A CD2 1 ATOM 598 C CE1 . PHE A 1 87 ? -43.621 5.605 71.682 1.00 19.46 ? 87 PHE A CE1 1 ATOM 599 C CE2 . PHE A 1 87 ? -41.313 5.387 72.221 1.00 19.89 ? 87 PHE A CE2 1 ATOM 600 C CZ . PHE A 1 87 ? -42.639 5.140 72.525 1.00 19.84 ? 87 PHE A CZ 1 ATOM 601 N N . VAL A 1 88 ? -43.670 5.208 67.446 1.00 17.30 ? 88 VAL A N 1 ATOM 602 C CA . VAL A 1 88 ? -45.061 4.887 67.081 1.00 17.81 ? 88 VAL A CA 1 ATOM 603 C C . VAL A 1 88 ? -45.856 4.546 68.331 1.00 18.62 ? 88 VAL A C 1 ATOM 604 O O . VAL A 1 88 ? -45.566 3.544 69.003 1.00 19.75 ? 88 VAL A O 1 ATOM 605 C CB . VAL A 1 88 ? -45.153 3.759 66.027 1.00 18.08 ? 88 VAL A CB 1 ATOM 606 C CG1 . VAL A 1 88 ? -46.610 3.428 65.699 1.00 18.52 ? 88 VAL A CG1 1 ATOM 607 C CG2 . VAL A 1 88 ? -44.392 4.134 64.762 1.00 17.56 ? 88 VAL A CG2 1 ATOM 608 N N . GLU A 1 89 ? -46.847 5.378 68.649 1.00 18.80 ? 89 GLU A N 1 ATOM 609 C CA . GLU A 1 89 ? -47.708 5.177 69.818 1.00 19.72 ? 89 GLU A CA 1 ATOM 610 C C . GLU A 1 89 ? -49.005 4.523 69.403 1.00 19.83 ? 89 GLU A C 1 ATOM 611 O O . GLU A 1 89 ? -49.688 4.999 68.481 1.00 18.83 ? 89 GLU A O 1 ATOM 612 C CB . GLU A 1 89 ? -48.085 6.498 70.519 1.00 20.05 ? 89 GLU A CB 1 ATOM 613 C CG . GLU A 1 89 ? -47.020 7.047 71.404 1.00 21.08 ? 89 GLU A CG 1 ATOM 614 C CD . GLU A 1 89 ? -47.427 8.296 72.199 1.00 20.68 ? 89 GLU A CD 1 ATOM 615 O OE1 . GLU A 1 89 ? -48.320 9.075 71.771 1.00 20.10 ? 89 GLU A OE1 1 ATOM 616 O OE2 . GLU A 1 89 ? -46.803 8.495 73.252 1.00 20.12 ? 89 GLU A OE2 1 ATOM 617 N N . ARG A 1 90 ? -49.362 3.478 70.150 1.00 20.37 ? 90 ARG A N 1 ATOM 618 C CA . ARG A 1 90 ? -50.501 2.622 69.872 1.00 21.62 ? 90 ARG A CA 1 ATOM 619 C C . ARG A 1 90 ? -51.696 3.050 70.697 1.00 22.76 ? 90 ARG A C 1 ATOM 620 O O . ARG A 1 90 ? -51.530 3.479 71.823 1.00 21.84 ? 90 ARG A O 1 ATOM 621 C CB . ARG A 1 90 ? -50.146 1.165 70.227 1.00 21.77 ? 90 ARG A CB 1 ATOM 622 C CG . ARG A 1 90 ? -48.826 0.668 69.648 1.00 21.99 ? 90 ARG A CG 1 ATOM 623 C CD . ARG A 1 90 ? -48.784 0.901 68.153 1.00 21.90 ? 90 ARG A CD 1 ATOM 624 N NE . ARG A 1 90 ? -47.843 0.060 67.418 1.00 21.72 ? 90 ARG A NE 1 ATOM 625 C CZ . ARG A 1 90 ? -47.892 -0.109 66.102 1.00 21.89 ? 90 ARG A CZ 1 ATOM 626 N NH1 . ARG A 1 90 ? -48.813 0.521 65.374 1.00 21.49 ? 90 ARG A NH1 1 ATOM 627 N NH2 . ARG A 1 90 ? -47.025 -0.904 65.493 1.00 22.00 ? 90 ARG A NH2 1 ATOM 628 N N . SER A 1 91 ? -52.900 2.911 70.147 1.00 24.22 ? 91 SER A N 1 ATOM 629 C CA . SER A 1 91 ? -54.106 3.310 70.878 1.00 25.74 ? 91 SER A CA 1 ATOM 630 C C . SER A 1 91 ? -54.353 2.430 72.106 1.00 27.13 ? 91 SER A C 1 ATOM 631 O O . SER A 1 91 ? -54.980 2.876 73.057 1.00 29.05 ? 91 SER A O 1 ATOM 632 C CB . SER A 1 91 ? -55.332 3.298 69.968 1.00 26.27 ? 91 SER A CB 1 ATOM 633 O OG . SER A 1 91 ? -55.625 1.988 69.561 1.00 26.83 ? 91 SER A OG 1 ATOM 634 N N . LYS A 1 92 ? -53.855 1.198 72.085 1.00 27.76 ? 92 LYS A N 1 ATOM 635 C CA . LYS A 1 92 ? -53.983 0.267 73.219 1.00 29.61 ? 92 LYS A CA 1 ATOM 636 C C . LYS A 1 92 ? -53.082 0.647 74.408 1.00 28.17 ? 92 LYS A C 1 ATOM 637 O O . LYS A 1 92 ? -53.210 0.062 75.479 1.00 28.15 ? 92 LYS A O 1 ATOM 638 C CB . LYS A 1 92 ? -53.613 -1.156 72.775 1.00 31.41 ? 92 LYS A CB 1 ATOM 639 C CG . LYS A 1 92 ? -52.105 -1.386 72.630 1.00 33.56 ? 92 LYS A CG 1 ATOM 640 C CD . LYS A 1 92 ? -51.756 -2.701 71.946 1.00 36.74 ? 92 LYS A CD 1 ATOM 641 C CE . LYS A 1 92 ? -50.240 -2.858 71.829 1.00 37.86 ? 92 LYS A CE 1 ATOM 642 N NZ . LYS A 1 92 ? -49.807 -4.271 71.654 1.00 37.81 ? 92 LYS A NZ 1 ATOM 643 N N . ALA A 1 93 ? -52.152 1.588 74.219 1.00 26.31 ? 93 ALA A N 1 ATOM 644 C CA . ALA A 1 93 ? -51.150 1.885 75.247 1.00 25.80 ? 93 ALA A CA 1 ATOM 645 C C . ALA A 1 93 ? -51.833 2.315 76.550 1.00 26.54 ? 93 ALA A C 1 ATOM 646 O O . ALA A 1 93 ? -52.875 2.986 76.533 1.00 26.92 ? 93 ALA A O 1 ATOM 647 C CB . ALA A 1 93 ? -50.149 2.944 74.768 1.00 24.49 ? 93 ALA A CB 1 ATOM 648 N N . TYR A 1 94 ? -51.271 1.890 77.676 1.00 26.73 ? 94 TYR A N 1 ATOM 649 C CA . TYR A 1 94 ? -51.831 2.240 78.991 1.00 28.07 ? 94 TYR A CA 1 ATOM 650 C C . TYR A 1 94 ? -50.740 2.363 80.033 1.00 27.92 ? 94 TYR A C 1 ATOM 651 O O . TYR A 1 94 ? -49.688 1.737 79.919 1.00 26.69 ? 94 TYR A O 1 ATOM 652 C CB . TYR A 1 94 ? -52.856 1.189 79.447 1.00 30.03 ? 94 TYR A CB 1 ATOM 653 C CG . TYR A 1 94 ? -52.270 -0.197 79.619 1.00 30.86 ? 94 TYR A CG 1 ATOM 654 C CD1 . TYR A 1 94 ? -52.078 -1.023 78.525 1.00 32.14 ? 94 TYR A CD1 1 ATOM 655 C CD2 . TYR A 1 94 ? -51.910 -0.678 80.877 1.00 32.89 ? 94 TYR A CD2 1 ATOM 656 C CE1 . TYR A 1 94 ? -51.546 -2.293 78.666 1.00 33.55 ? 94 TYR A CE1 1 ATOM 657 C CE2 . TYR A 1 94 ? -51.364 -1.942 81.035 1.00 33.62 ? 94 TYR A CE2 1 ATOM 658 C CZ . TYR A 1 94 ? -51.186 -2.752 79.922 1.00 34.73 ? 94 TYR A CZ 1 ATOM 659 O OH . TYR A 1 94 ? -50.646 -4.018 80.044 1.00 34.77 ? 94 TYR A OH 1 ATOM 660 N N . SER A 1 95 ? -50.993 3.186 81.045 1.00 28.19 ? 95 SER A N 1 ATOM 661 C CA . SER A 1 95 ? -50.046 3.360 82.139 1.00 28.55 ? 95 SER A CA 1 ATOM 662 C C . SER A 1 95 ? -50.297 2.327 83.210 1.00 28.82 ? 95 SER A C 1 ATOM 663 O O . SER A 1 95 ? -51.449 1.976 83.488 1.00 28.72 ? 95 SER A O 1 ATOM 664 C CB . SER A 1 95 ? -50.183 4.743 82.751 1.00 29.11 ? 95 SER A CB 1 ATOM 665 O OG . SER A 1 95 ? -49.911 5.734 81.787 1.00 28.61 ? 95 SER A OG 1 ATOM 666 N N . ASN A 1 96 ? -49.225 1.855 83.836 1.00 28.72 ? 96 ASN A N 1 ATOM 667 C CA . ASN A 1 96 ? -49.359 0.795 84.839 1.00 29.77 ? 96 ASN A CA 1 ATOM 668 C C . ASN A 1 96 ? -48.439 1.013 86.039 1.00 29.43 ? 96 ASN A C 1 ATOM 669 O O . ASN A 1 96 ? -47.906 0.067 86.606 1.00 29.98 ? 96 ASN A O 1 ATOM 670 C CB . ASN A 1 96 ? -49.120 -0.566 84.178 1.00 31.69 ? 96 ASN A CB 1 ATOM 671 C CG . ASN A 1 96 ? -49.776 -1.709 84.933 1.00 33.85 ? 96 ASN A CG 1 ATOM 672 O OD1 . ASN A 1 96 ? -50.753 -1.510 85.664 1.00 35.73 ? 96 ASN A OD1 1 ATOM 673 N ND2 . ASN A 1 96 ? -49.229 -2.911 84.776 1.00 34.41 ? 96 ASN A ND2 1 ATOM 674 N N . CYS A 1 97 ? -48.298 2.272 86.444 1.00 28.86 ? 97 CYS A N 1 ATOM 675 C CA . CYS A 1 97 ? -47.482 2.638 87.588 1.00 29.07 ? 97 CYS A CA 1 ATOM 676 C C . CYS A 1 97 ? -48.294 3.639 88.403 1.00 28.34 ? 97 CYS A C 1 ATOM 677 O O . CYS A 1 97 ? -49.532 3.634 88.345 1.00 26.84 ? 97 CYS A O 1 ATOM 678 C CB . CYS A 1 97 ? -46.142 3.175 87.066 1.00 29.99 ? 97 CYS A CB 1 ATOM 679 S SG . CYS A 1 97 ? -44.755 3.435 88.210 1.00 31.89 ? 97 CYS A SG 1 ATOM 680 N N . TYR A 1 98 ? -47.630 4.500 89.158 1.00 28.35 ? 98 TYR A N 1 ATOM 681 C CA . TYR A 1 98 ? -48.343 5.471 89.986 1.00 28.72 ? 98 TYR A CA 1 ATOM 682 C C . TYR A 1 98 ? -49.087 6.471 89.111 1.00 29.08 ? 98 TYR A C 1 ATOM 683 O O . TYR A 1 98 ? -48.526 6.946 88.117 1.00 28.44 ? 98 TYR A O 1 ATOM 684 C CB . TYR A 1 98 ? -47.363 6.202 90.890 1.00 28.84 ? 98 TYR A CB 1 ATOM 685 C CG . TYR A 1 98 ? -47.929 6.647 92.212 1.00 28.75 ? 98 TYR A CG 1 ATOM 686 C CD1 . TYR A 1 98 ? -48.530 7.895 92.358 1.00 28.83 ? 98 TYR A CD1 1 ATOM 687 C CD2 . TYR A 1 98 ? -47.834 5.824 93.334 1.00 29.75 ? 98 TYR A CD2 1 ATOM 688 C CE1 . TYR A 1 98 ? -49.025 8.307 93.591 1.00 29.50 ? 98 TYR A CE1 1 ATOM 689 C CE2 . TYR A 1 98 ? -48.329 6.223 94.560 1.00 29.52 ? 98 TYR A CE2 1 ATOM 690 C CZ . TYR A 1 98 ? -48.917 7.457 94.691 1.00 29.91 ? 98 TYR A CZ 1 ATOM 691 O OH . TYR A 1 98 ? -49.383 7.842 95.932 1.00 30.00 ? 98 TYR A OH 1 ATOM 692 N N . PRO A 1 99 ? -50.356 6.772 89.449 1.00 28.58 ? 99 PRO A N 1 ATOM 693 C CA . PRO A 1 99 ? -51.090 7.717 88.622 1.00 28.19 ? 99 PRO A CA 1 ATOM 694 C C . PRO A 1 99 ? -50.444 9.100 88.585 1.00 27.23 ? 99 PRO A C 1 ATOM 695 O O . PRO A 1 99 ? -50.018 9.628 89.605 1.00 25.90 ? 99 PRO A O 1 ATOM 696 C CB . PRO A 1 99 ? -52.489 7.774 89.257 1.00 29.25 ? 99 PRO A CB 1 ATOM 697 C CG . PRO A 1 99 ? -52.397 7.024 90.536 1.00 29.51 ? 99 PRO A CG 1 ATOM 698 C CD . PRO A 1 99 ? -51.224 6.113 90.440 1.00 29.38 ? 99 PRO A CD 1 ATOM 699 N N . TYR A 1 100 ? -50.353 9.666 87.393 1.00 25.84 ? 100 TYR A N 1 ATOM 700 C CA . TYR A 1 100 ? -49.678 10.945 87.227 1.00 25.10 ? 100 TYR A CA 1 ATOM 701 C C . TYR A 1 100 ? -50.369 11.810 86.189 1.00 25.17 ? 100 TYR A C 1 ATOM 702 O O . TYR A 1 100 ? -51.162 11.328 85.368 1.00 23.87 ? 100 TYR A O 1 ATOM 703 C CB . TYR A 1 100 ? -48.205 10.734 86.835 1.00 25.20 ? 100 TYR A CB 1 ATOM 704 C CG . TYR A 1 100 ? -48.006 10.219 85.417 1.00 25.01 ? 100 TYR A CG 1 ATOM 705 C CD1 . TYR A 1 100 ? -48.054 8.867 85.141 1.00 25.23 ? 100 TYR A CD1 1 ATOM 706 C CD2 . TYR A 1 100 ? -47.799 11.103 84.343 1.00 24.56 ? 100 TYR A CD2 1 ATOM 707 C CE1 . TYR A 1 100 ? -47.870 8.383 83.848 1.00 25.77 ? 100 TYR A CE1 1 ATOM 708 C CE2 . TYR A 1 100 ? -47.636 10.632 83.043 1.00 24.66 ? 100 TYR A CE2 1 ATOM 709 C CZ . TYR A 1 100 ? -47.678 9.272 82.795 1.00 25.23 ? 100 TYR A CZ 1 ATOM 710 O OH . TYR A 1 100 ? -47.494 8.779 81.512 1.00 24.76 ? 100 TYR A OH 1 ATOM 711 N N . ASP A 1 101 ? -50.083 13.103 86.253 1.00 25.70 ? 101 ASP A N 1 ATOM 712 C CA . ASP A 1 101 ? -50.363 13.987 85.136 1.00 26.24 ? 101 ASP A CA 1 ATOM 713 C C . ASP A 1 101 ? -49.134 14.854 84.828 1.00 24.91 ? 101 ASP A C 1 ATOM 714 O O . ASP A 1 101 ? -48.201 14.953 85.637 1.00 23.36 ? 101 ASP A O 1 ATOM 715 C CB . ASP A 1 101 ? -51.619 14.819 85.389 1.00 30.06 ? 101 ASP A CB 1 ATOM 716 C CG . ASP A 1 101 ? -51.372 16.020 86.268 1.00 33.90 ? 101 ASP A CG 1 ATOM 717 O OD1 . ASP A 1 101 ? -50.606 15.913 87.226 1.00 36.47 ? 101 ASP A OD1 1 ATOM 718 O OD2 . ASP A 1 101 ? -51.949 17.095 85.970 1.00 43.44 ? 101 ASP A OD2 1 ATOM 719 N N . VAL A 1 102 ? -49.139 15.449 83.644 1.00 22.55 ? 102 VAL A N 1 ATOM 720 C CA . VAL A 1 102 ? -48.079 16.356 83.217 1.00 22.13 ? 102 VAL A CA 1 ATOM 721 C C . VAL A 1 102 ? -48.766 17.633 82.774 1.00 22.83 ? 102 VAL A C 1 ATOM 722 O O . VAL A 1 102 ? -49.402 17.653 81.722 1.00 22.05 ? 102 VAL A O 1 ATOM 723 C CB . VAL A 1 102 ? -47.277 15.774 82.029 1.00 21.95 ? 102 VAL A CB 1 ATOM 724 C CG1 . VAL A 1 102 ? -46.032 16.622 81.736 1.00 21.65 ? 102 VAL A CG1 1 ATOM 725 C CG2 . VAL A 1 102 ? -46.894 14.306 82.288 1.00 21.64 ? 102 VAL A CG2 1 ATOM 726 N N . PRO A 1 103 ? -48.645 18.713 83.563 1.00 23.53 ? 103 PRO A N 1 ATOM 727 C CA . PRO A 1 103 ? -49.094 19.977 83.001 1.00 24.37 ? 103 PRO A CA 1 ATOM 728 C C . PRO A 1 103 ? -48.342 20.217 81.680 1.00 25.21 ? 103 PRO A C 1 ATOM 729 O O . PRO A 1 103 ? -47.138 20.027 81.639 1.00 27.94 ? 103 PRO A O 1 ATOM 730 C CB . PRO A 1 103 ? -48.675 21.005 84.062 1.00 24.41 ? 103 PRO A CB 1 ATOM 731 C CG . PRO A 1 103 ? -48.647 20.229 85.340 1.00 24.39 ? 103 PRO A CG 1 ATOM 732 C CD . PRO A 1 103 ? -48.189 18.844 84.963 1.00 23.91 ? 103 PRO A CD 1 ATOM 733 N N . ASP A 1 104 ? -49.026 20.603 80.620 1.00 26.52 ? 104 ASP A N 1 ATOM 734 C CA . ASP A 1 104 ? -48.374 20.701 79.268 1.00 26.70 ? 104 ASP A CA 1 ATOM 735 C C . ASP A 1 104 ? -47.663 19.403 78.811 1.00 23.40 ? 104 ASP A C 1 ATOM 736 O O . ASP A 1 104 ? -46.562 19.403 78.222 1.00 22.12 ? 104 ASP A O 1 ATOM 737 C CB . ASP A 1 104 ? -47.411 21.897 79.167 1.00 29.67 ? 104 ASP A CB 1 ATOM 738 C CG . ASP A 1 104 ? -47.301 22.469 77.719 1.00 33.24 ? 104 ASP A CG 1 ATOM 739 O OD1 . ASP A 1 104 ? -48.027 22.037 76.735 1.00 33.86 ? 104 ASP A OD1 1 ATOM 740 O OD2 . ASP A 1 104 ? -46.452 23.381 77.564 1.00 38.91 ? 104 ASP A OD2 1 ATOM 741 N N . TYR A 1 105 ? -48.351 18.303 79.057 1.00 20.97 ? 105 TYR A N 1 ATOM 742 C CA . TYR A 1 105 ? -48.045 17.008 78.495 1.00 20.01 ? 105 TYR A CA 1 ATOM 743 C C . TYR A 1 105 ? -47.687 17.067 77.008 1.00 18.63 ? 105 TYR A C 1 ATOM 744 O O . TYR A 1 105 ? -46.687 16.500 76.592 1.00 18.25 ? 105 TYR A O 1 ATOM 745 C CB . TYR A 1 105 ? -49.270 16.116 78.668 1.00 20.77 ? 105 TYR A CB 1 ATOM 746 C CG . TYR A 1 105 ? -49.092 14.679 78.228 1.00 21.64 ? 105 TYR A CG 1 ATOM 747 C CD1 . TYR A 1 105 ? -49.347 14.296 76.914 1.00 22.96 ? 105 TYR A CD1 1 ATOM 748 C CD2 . TYR A 1 105 ? -48.712 13.697 79.122 1.00 22.20 ? 105 TYR A CD2 1 ATOM 749 C CE1 . TYR A 1 105 ? -49.201 12.966 76.512 1.00 22.75 ? 105 TYR A CE1 1 ATOM 750 C CE2 . TYR A 1 105 ? -48.582 12.365 78.727 1.00 23.12 ? 105 TYR A CE2 1 ATOM 751 C CZ . TYR A 1 105 ? -48.810 12.016 77.413 1.00 22.79 ? 105 TYR A CZ 1 ATOM 752 O OH . TYR A 1 105 ? -48.684 10.689 77.000 1.00 24.19 ? 105 TYR A OH 1 ATOM 753 N N . ALA A 1 106 ? -48.505 17.747 76.213 1.00 17.62 ? 106 ALA A N 1 ATOM 754 C CA . ALA A 1 106 ? -48.253 17.799 74.760 1.00 17.36 ? 106 ALA A CA 1 ATOM 755 C C . ALA A 1 106 ? -46.886 18.362 74.449 1.00 17.39 ? 106 ALA A C 1 ATOM 756 O O . ALA A 1 106 ? -46.225 17.886 73.532 1.00 17.49 ? 106 ALA A O 1 ATOM 757 C CB . ALA A 1 106 ? -49.334 18.591 74.016 1.00 16.98 ? 106 ALA A CB 1 ATOM 758 N N . SER A 1 107 ? -46.447 19.373 75.203 1.00 17.90 ? 107 SER A N 1 ATOM 759 C CA . SER A 1 107 ? -45.124 19.939 74.935 1.00 17.99 ? 107 SER A CA 1 ATOM 760 C C . SER A 1 107 ? -43.984 19.015 75.326 1.00 17.50 ? 107 SER A C 1 ATOM 761 O O . SER A 1 107 ? -42.979 18.957 74.627 1.00 17.22 ? 107 SER A O 1 ATOM 762 C CB . SER A 1 107 ? -44.949 21.323 75.570 1.00 18.33 ? 107 SER A CB 1 ATOM 763 O OG . SER A 1 107 ? -45.732 22.285 74.858 1.00 18.76 ? 107 SER A OG 1 ATOM 764 N N . LEU A 1 108 ? -44.109 18.302 76.435 1.00 17.45 ? 108 LEU A N 1 ATOM 765 C CA . LEU A 1 108 ? -43.023 17.426 76.866 1.00 17.32 ? 108 LEU A CA 1 ATOM 766 C C . LEU A 1 108 ? -42.929 16.251 75.895 1.00 17.02 ? 108 LEU A C 1 ATOM 767 O O . LEU A 1 108 ? -41.828 15.851 75.471 1.00 17.19 ? 108 LEU A O 1 ATOM 768 C CB . LEU A 1 108 ? -43.249 16.934 78.293 1.00 17.51 ? 108 LEU A CB 1 ATOM 769 C CG . LEU A 1 108 ? -42.190 15.937 78.800 1.00 17.69 ? 108 LEU A CG 1 ATOM 770 C CD1 . LEU A 1 108 ? -40.788 16.539 78.777 1.00 18.03 ? 108 LEU A CD1 1 ATOM 771 C CD2 . LEU A 1 108 ? -42.554 15.494 80.197 1.00 17.67 ? 108 LEU A CD2 1 ATOM 772 N N . ARG A 1 109 ? -44.090 15.722 75.521 1.00 16.19 ? 109 ARG A N 1 ATOM 773 C CA . ARG A 1 109 ? -44.161 14.686 74.487 1.00 16.16 ? 109 ARG A CA 1 ATOM 774 C C . ARG A 1 109 ? -43.473 15.132 73.196 1.00 16.00 ? 109 ARG A C 1 ATOM 775 O O . ARG A 1 109 ? -42.658 14.394 72.635 1.00 15.38 ? 109 ARG A O 1 ATOM 776 C CB . ARG A 1 109 ? -45.612 14.273 74.249 1.00 16.07 ? 109 ARG A CB 1 ATOM 777 C CG . ARG A 1 109 ? -45.795 13.229 73.158 1.00 16.38 ? 109 ARG A CG 1 ATOM 778 C CD . ARG A 1 109 ? -47.261 12.816 73.099 1.00 16.48 ? 109 ARG A CD 1 ATOM 779 N NE . ARG A 1 109 ? -47.580 11.897 72.002 1.00 16.34 ? 109 ARG A NE 1 ATOM 780 C CZ . ARG A 1 109 ? -47.790 12.247 70.726 1.00 15.97 ? 109 ARG A CZ 1 ATOM 781 N NH1 . ARG A 1 109 ? -47.676 13.496 70.326 1.00 15.55 ? 109 ARG A NH1 1 ATOM 782 N NH2 . ARG A 1 109 ? -48.103 11.309 69.831 1.00 15.50 ? 109 ARG A NH2 1 ATOM 783 N N . SER A 1 110 ? -43.793 16.345 72.740 1.00 16.16 ? 110 SER A N 1 ATOM 784 C CA . SER A 1 110 ? -43.218 16.886 71.513 1.00 16.40 ? 110 SER A CA 1 ATOM 785 C C . SER A 1 110 ? -41.700 17.048 71.599 1.00 16.64 ? 110 SER A C 1 ATOM 786 O O . SER A 1 110 ? -40.969 16.660 70.686 1.00 17.17 ? 110 SER A O 1 ATOM 787 C CB . SER A 1 110 ? -43.868 18.234 71.155 1.00 16.65 ? 110 SER A CB 1 ATOM 788 O OG . SER A 1 110 ? -43.225 18.782 70.013 1.00 17.31 ? 110 SER A OG 1 ATOM 789 N N . LEU A 1 111 ? -41.220 17.661 72.668 1.00 16.60 ? 111 LEU A N 1 ATOM 790 C CA . LEU A 1 111 ? -39.787 17.943 72.745 1.00 17.52 ? 111 LEU A CA 1 ATOM 791 C C . LEU A 1 111 ? -38.959 16.669 72.870 1.00 16.94 ? 111 LEU A C 1 ATOM 792 O O . LEU A 1 111 ? -37.891 16.574 72.244 1.00 18.04 ? 111 LEU A O 1 ATOM 793 C CB . LEU A 1 111 ? -39.474 18.958 73.824 1.00 18.20 ? 111 LEU A CB 1 ATOM 794 C CG . LEU A 1 111 ? -39.514 18.565 75.276 1.00 18.50 ? 111 LEU A CG 1 ATOM 795 C CD1 . LEU A 1 111 ? -38.160 17.997 75.707 1.00 18.97 ? 111 LEU A CD1 1 ATOM 796 C CD2 . LEU A 1 111 ? -39.894 19.797 76.097 1.00 19.61 ? 111 LEU A CD2 1 ATOM 797 N N . VAL A 1 112 ? -39.464 15.680 73.598 1.00 17.09 ? 112 VAL A N 1 ATOM 798 C CA . VAL A 1 112 ? -38.767 14.372 73.682 1.00 16.99 ? 112 VAL A CA 1 ATOM 799 C C . VAL A 1 112 ? -38.831 13.655 72.323 1.00 16.71 ? 112 VAL A C 1 ATOM 800 O O . VAL A 1 112 ? -37.824 13.115 71.836 1.00 15.83 ? 112 VAL A O 1 ATOM 801 C CB . VAL A 1 112 ? -39.312 13.489 74.831 1.00 17.31 ? 112 VAL A CB 1 ATOM 802 C CG1 . VAL A 1 112 ? -38.582 12.140 74.838 1.00 17.76 ? 112 VAL A CG1 1 ATOM 803 C CG2 . VAL A 1 112 ? -39.122 14.197 76.195 1.00 17.62 ? 112 VAL A CG2 1 ATOM 804 N N . ALA A 1 113 ? -40.004 13.694 71.679 1.00 16.51 ? 113 ALA A N 1 ATOM 805 C CA . ALA A 1 113 ? -40.169 13.071 70.354 1.00 16.35 ? 113 ALA A CA 1 ATOM 806 C C . ALA A 1 113 ? -39.204 13.618 69.331 1.00 16.35 ? 113 ALA A C 1 ATOM 807 O O . ALA A 1 113 ? -38.650 12.846 68.571 1.00 15.73 ? 113 ALA A O 1 ATOM 808 C CB . ALA A 1 113 ? -41.591 13.252 69.826 1.00 15.70 ? 113 ALA A CB 1 ATOM 809 N N . SER A 1 114 ? -39.064 14.954 69.300 1.00 15.96 ? 114 SER A N 1 ATOM 810 C CA . SER A 1 114 ? -38.193 15.652 68.375 1.00 17.32 ? 114 SER A CA 1 ATOM 811 C C . SER A 1 114 ? -36.705 15.404 68.668 1.00 17.81 ? 114 SER A C 1 ATOM 812 O O . SER A 1 114 ? -35.886 15.329 67.731 1.00 18.70 ? 114 SER A O 1 ATOM 813 C CB . SER A 1 114 ? -38.483 17.167 68.404 1.00 17.82 ? 114 SER A CB 1 ATOM 814 O OG . SER A 1 114 ? -37.671 17.837 67.451 1.00 20.16 ? 114 SER A OG 1 ATOM 815 N N . SER A 1 115 ? -36.370 15.282 69.951 1.00 17.78 ? 115 SER A N 1 ATOM 816 C CA . SER A 1 115 ? -35.007 14.942 70.366 1.00 18.27 ? 115 SER A CA 1 ATOM 817 C C . SER A 1 115 ? -34.591 13.537 69.909 1.00 18.11 ? 115 SER A C 1 ATOM 818 O O . SER A 1 115 ? -33.437 13.326 69.501 1.00 19.43 ? 115 SER A O 1 ATOM 819 C CB . SER A 1 115 ? -34.865 15.100 71.888 1.00 18.68 ? 115 SER A CB 1 ATOM 820 O OG . SER A 1 115 ? -33.638 14.590 72.379 1.00 19.90 ? 115 SER A OG 1 ATOM 821 N N . GLY A 1 116 ? -35.509 12.585 69.973 1.00 17.35 ? 116 GLY A N 1 ATOM 822 C CA . GLY A 1 116 ? -35.316 11.266 69.352 1.00 17.09 ? 116 GLY A CA 1 ATOM 823 C C . GLY A 1 116 ? -34.455 10.295 70.156 1.00 17.31 ? 116 GLY A C 1 ATOM 824 O O . GLY A 1 116 ? -33.891 9.349 69.603 1.00 16.94 ? 116 GLY A O 1 ATOM 825 N N . THR A 1 117 ? -34.341 10.537 71.452 1.00 17.57 ? 117 THR A N 1 ATOM 826 C CA . THR A 1 117 ? -33.509 9.683 72.306 1.00 18.10 ? 117 THR A CA 1 ATOM 827 C C . THR A 1 117 ? -34.027 9.622 73.721 1.00 18.33 ? 117 THR A C 1 ATOM 828 O O . THR A 1 117 ? -34.531 10.606 74.268 1.00 18.54 ? 117 THR A O 1 ATOM 829 C CB . THR A 1 117 ? -32.015 10.119 72.317 1.00 18.29 ? 117 THR A CB 1 ATOM 830 O OG1 . THR A 1 117 ? -31.253 9.226 73.148 1.00 18.97 ? 117 THR A OG1 1 ATOM 831 C CG2 . THR A 1 117 ? -31.811 11.584 72.800 1.00 18.21 ? 117 THR A CG2 1 ATOM 832 N N . LEU A 1 118 ? -33.922 8.433 74.297 1.00 18.83 ? 118 LEU A N 1 ATOM 833 C CA . LEU A 1 118 ? -34.188 8.231 75.711 1.00 19.62 ? 118 LEU A CA 1 ATOM 834 C C . LEU A 1 118 ? -32.887 8.024 76.507 1.00 20.02 ? 118 LEU A C 1 ATOM 835 O O . LEU A 1 118 ? -32.933 7.581 77.642 1.00 20.22 ? 118 LEU A O 1 ATOM 836 C CB . LEU A 1 118 ? -35.110 7.030 75.893 1.00 19.94 ? 118 LEU A CB 1 ATOM 837 C CG . LEU A 1 118 ? -36.585 7.240 75.579 1.00 20.17 ? 118 LEU A CG 1 ATOM 838 C CD1 . LEU A 1 118 ? -37.334 5.911 75.474 1.00 21.07 ? 118 LEU A CD1 1 ATOM 839 C CD2 . LEU A 1 118 ? -37.202 8.106 76.645 1.00 20.14 ? 118 LEU A CD2 1 ATOM 840 N N . GLU A 1 119 ? -31.739 8.372 75.925 1.00 21.09 ? 119 GLU A N 1 ATOM 841 C CA . GLU A 1 119 ? -30.459 8.232 76.641 1.00 22.39 ? 119 GLU A CA 1 ATOM 842 C C . GLU A 1 119 ? -30.497 8.970 77.969 1.00 22.24 ? 119 GLU A C 1 ATOM 843 O O . GLU A 1 119 ? -30.803 10.167 78.007 1.00 22.13 ? 119 GLU A O 1 ATOM 844 C CB . GLU A 1 119 ? -29.323 8.817 75.831 1.00 23.97 ? 119 GLU A CB 1 ATOM 845 C CG . GLU A 1 119 ? -28.955 8.057 74.588 1.00 25.61 ? 119 GLU A CG 1 ATOM 846 C CD . GLU A 1 119 ? -28.111 8.933 73.684 1.00 27.15 ? 119 GLU A CD 1 ATOM 847 O OE1 . GLU A 1 119 ? -28.685 9.776 72.927 1.00 25.69 ? 119 GLU A OE1 1 ATOM 848 O OE2 . GLU A 1 119 ? -26.867 8.807 73.799 1.00 26.76 ? 119 GLU A OE2 1 ATOM 849 N N . PHE A 1 120 ? -30.131 8.262 79.046 1.00 22.85 ? 120 PHE A N 1 ATOM 850 C CA . PHE A 1 120 ? -30.238 8.763 80.402 1.00 22.73 ? 120 PHE A CA 1 ATOM 851 C C . PHE A 1 120 ? -28.902 8.525 81.107 1.00 24.00 ? 120 PHE A C 1 ATOM 852 O O . PHE A 1 120 ? -28.346 7.439 80.988 1.00 23.98 ? 120 PHE A O 1 ATOM 853 C CB . PHE A 1 120 ? -31.340 8.021 81.151 1.00 22.60 ? 120 PHE A CB 1 ATOM 854 C CG . PHE A 1 120 ? -31.621 8.572 82.526 1.00 23.33 ? 120 PHE A CG 1 ATOM 855 C CD1 . PHE A 1 120 ? -32.474 9.653 82.685 1.00 23.27 ? 120 PHE A CD1 1 ATOM 856 C CD2 . PHE A 1 120 ? -31.052 8.004 83.658 1.00 23.57 ? 120 PHE A CD2 1 ATOM 857 C CE1 . PHE A 1 120 ? -32.746 10.187 83.934 1.00 23.10 ? 120 PHE A CE1 1 ATOM 858 C CE2 . PHE A 1 120 ? -31.323 8.523 84.921 1.00 23.45 ? 120 PHE A CE2 1 ATOM 859 C CZ . PHE A 1 120 ? -32.173 9.618 85.060 1.00 24.06 ? 120 PHE A CZ 1 ATOM 860 N N . ASN A 1 121 ? -28.404 9.544 81.796 1.00 24.79 ? 121 ASN A N 1 ATOM 861 C CA . ASN A 1 121 ? -27.154 9.438 82.564 1.00 27.34 ? 121 ASN A CA 1 ATOM 862 C C . ASN A 1 121 ? -27.485 9.632 84.028 1.00 27.74 ? 121 ASN A C 1 ATOM 863 O O . ASN A 1 121 ? -28.034 10.668 84.419 1.00 25.93 ? 121 ASN A O 1 ATOM 864 C CB . ASN A 1 121 ? -26.163 10.495 82.123 1.00 29.90 ? 121 ASN A CB 1 ATOM 865 C CG . ASN A 1 121 ? -25.432 10.124 80.847 1.00 33.69 ? 121 ASN A CG 1 ATOM 866 O OD1 . ASN A 1 121 ? -25.383 8.960 80.456 1.00 36.48 ? 121 ASN A OD1 1 ATOM 867 N ND2 . ASN A 1 121 ? -24.844 11.127 80.190 1.00 38.63 ? 121 ASN A ND2 1 ATOM 868 N N . ASN A 1 122 ? -27.174 8.619 84.832 1.00 28.82 ? 122 ASN A N 1 ATOM 869 C CA . ASN A 1 122 ? -27.391 8.692 86.271 1.00 29.83 ? 122 ASN A CA 1 ATOM 870 C C . ASN A 1 122 ? -26.440 9.698 86.912 1.00 29.34 ? 122 ASN A C 1 ATOM 871 O O . ASN A 1 122 ? -25.306 9.879 86.453 1.00 28.53 ? 122 ASN A O 1 ATOM 872 C CB . ASN A 1 122 ? -27.239 7.303 86.903 1.00 32.37 ? 122 ASN A CB 1 ATOM 873 C CG . ASN A 1 122 ? -28.419 6.389 86.590 1.00 33.46 ? 122 ASN A CG 1 ATOM 874 O OD1 . ASN A 1 122 ? -28.330 5.511 85.735 1.00 37.83 ? 122 ASN A OD1 1 ATOM 875 N ND2 . ASN A 1 122 ? -29.529 6.606 87.268 1.00 33.69 ? 122 ASN A ND2 1 ATOM 876 N N . GLU A 1 123 ? -26.918 10.383 87.949 1.00 29.66 ? 123 GLU A N 1 ATOM 877 C CA . GLU A 1 123 ? -26.088 11.300 88.717 1.00 29.80 ? 123 GLU A CA 1 ATOM 878 C C . GLU A 1 123 ? -26.295 11.066 90.204 1.00 31.05 ? 123 GLU A C 1 ATOM 879 O O . GLU A 1 123 ? -27.365 10.632 90.627 1.00 29.60 ? 123 GLU A O 1 ATOM 880 C CB . GLU A 1 123 ? -26.417 12.759 88.398 1.00 29.07 ? 123 GLU A CB 1 ATOM 881 C CG . GLU A 1 123 ? -26.046 13.199 86.994 1.00 28.93 ? 123 GLU A CG 1 ATOM 882 C CD . GLU A 1 123 ? -26.445 14.629 86.710 1.00 28.36 ? 123 GLU A CD 1 ATOM 883 O OE1 . GLU A 1 123 ? -27.616 14.989 86.978 1.00 28.02 ? 123 GLU A OE1 1 ATOM 884 O OE2 . GLU A 1 123 ? -25.591 15.396 86.227 1.00 27.78 ? 123 GLU A OE2 1 ATOM 885 N N . SER A 1 124 ? -25.259 11.382 90.984 1.00 33.42 ? 124 SER A N 1 ATOM 886 C CA . SER A 1 124 ? -25.244 11.136 92.430 1.00 34.55 ? 124 SER A CA 1 ATOM 887 C C . SER A 1 124 ? -25.678 12.385 93.172 1.00 34.52 ? 124 SER A C 1 ATOM 888 O O . SER A 1 124 ? -24.851 13.223 93.548 1.00 33.32 ? 124 SER A O 1 ATOM 889 C CB . SER A 1 124 ? -23.840 10.731 92.903 1.00 37.16 ? 124 SER A CB 1 ATOM 890 O OG . SER A 1 124 ? -23.416 9.535 92.275 1.00 40.69 ? 124 SER A OG 1 ATOM 891 N N . PHE A 1 125 ? -26.982 12.522 93.363 1.00 35.33 ? 125 PHE A N 1 ATOM 892 C CA . PHE A 1 125 ? -27.505 13.644 94.119 1.00 35.57 ? 125 PHE A CA 1 ATOM 893 C C . PHE A 1 125 ? -27.216 13.391 95.589 1.00 37.88 ? 125 PHE A C 1 ATOM 894 O O . PHE A 1 125 ? -27.169 12.245 96.028 1.00 38.66 ? 125 PHE A O 1 ATOM 895 C CB . PHE A 1 125 ? -29.011 13.798 93.896 1.00 35.20 ? 125 PHE A CB 1 ATOM 896 C CG . PHE A 1 125 ? -29.365 14.429 92.584 1.00 33.15 ? 125 PHE A CG 1 ATOM 897 C CD1 . PHE A 1 125 ? -29.482 13.657 91.440 1.00 32.58 ? 125 PHE A CD1 1 ATOM 898 C CD2 . PHE A 1 125 ? -29.567 15.800 92.493 1.00 32.91 ? 125 PHE A CD2 1 ATOM 899 C CE1 . PHE A 1 125 ? -29.801 14.243 90.228 1.00 31.51 ? 125 PHE A CE1 1 ATOM 900 C CE2 . PHE A 1 125 ? -29.898 16.392 91.282 1.00 32.64 ? 125 PHE A CE2 1 ATOM 901 C CZ . PHE A 1 125 ? -30.002 15.606 90.147 1.00 31.17 ? 125 PHE A CZ 1 ATOM 902 N N . ASN A 1 126 ? -27.009 14.455 96.346 1.00 40.07 ? 126 ASN A N 1 ATOM 903 C CA . ASN A 1 126 ? -26.783 14.303 97.774 1.00 42.70 ? 126 ASN A CA 1 ATOM 904 C C . ASN A 1 126 ? -28.105 14.372 98.546 1.00 40.25 ? 126 ASN A C 1 ATOM 905 O O . ASN A 1 126 ? -28.546 15.460 98.937 1.00 38.67 ? 126 ASN A O 1 ATOM 906 C CB . ASN A 1 126 ? -25.796 15.365 98.253 1.00 48.40 ? 126 ASN A CB 1 ATOM 907 C CG . ASN A 1 126 ? -25.659 15.385 99.753 1.00 54.95 ? 126 ASN A CG 1 ATOM 908 O OD1 . ASN A 1 126 ? -25.951 14.393 100.423 1.00 54.23 ? 126 ASN A OD1 1 ATOM 909 N ND2 . ASN A 1 126 ? -25.228 16.520 100.292 1.00 65.50 ? 126 ASN A ND2 1 ATOM 910 N N . TRP A 1 127 ? -28.732 13.210 98.757 1.00 37.84 ? 127 TRP A N 1 ATOM 911 C CA . TRP A 1 127 ? -29.978 13.120 99.525 1.00 38.33 ? 127 TRP A CA 1 ATOM 912 C C . TRP A 1 127 ? -29.755 12.737 100.969 1.00 40.14 ? 127 TRP A C 1 ATOM 913 O O . TRP A 1 127 ? -30.383 11.804 101.492 1.00 40.17 ? 127 TRP A O 1 ATOM 914 C CB . TRP A 1 127 ? -30.933 12.120 98.896 1.00 37.50 ? 127 TRP A CB 1 ATOM 915 C CG . TRP A 1 127 ? -31.252 12.432 97.453 1.00 35.76 ? 127 TRP A CG 1 ATOM 916 C CD1 . TRP A 1 127 ? -31.104 11.590 96.361 1.00 35.50 ? 127 TRP A CD1 1 ATOM 917 C CD2 . TRP A 1 127 ? -31.781 13.690 96.901 1.00 35.97 ? 127 TRP A CD2 1 ATOM 918 N NE1 . TRP A 1 127 ? -31.499 12.211 95.204 1.00 34.16 ? 127 TRP A NE1 1 ATOM 919 C CE2 . TRP A 1 127 ? -31.910 13.474 95.452 1.00 34.77 ? 127 TRP A CE2 1 ATOM 920 C CE3 . TRP A 1 127 ? -32.145 14.928 97.436 1.00 35.72 ? 127 TRP A CE3 1 ATOM 921 C CZ2 . TRP A 1 127 ? -32.378 14.464 94.599 1.00 34.89 ? 127 TRP A CZ2 1 ATOM 922 C CZ3 . TRP A 1 127 ? -32.622 15.920 96.566 1.00 35.90 ? 127 TRP A CZ3 1 ATOM 923 C CH2 . TRP A 1 127 ? -32.733 15.694 95.177 1.00 35.89 ? 127 TRP A CH2 1 ATOM 924 N N . THR A 1 128 ? -28.883 13.475 101.633 1.00 41.85 ? 128 THR A N 1 ATOM 925 C CA . THR A 1 128 ? -28.609 13.241 103.050 1.00 43.46 ? 128 THR A CA 1 ATOM 926 C C . THR A 1 128 ? -29.831 13.559 103.911 1.00 42.07 ? 128 THR A C 1 ATOM 927 O O . THR A 1 128 ? -30.434 14.625 103.770 1.00 42.86 ? 128 THR A O 1 ATOM 928 C CB . THR A 1 128 ? -27.406 14.093 103.507 1.00 47.08 ? 128 THR A CB 1 ATOM 929 O OG1 . THR A 1 128 ? -26.220 13.608 102.862 1.00 49.83 ? 128 THR A OG1 1 ATOM 930 C CG2 . THR A 1 128 ? -27.218 14.029 105.030 1.00 46.90 ? 128 THR A CG2 1 ATOM 931 N N . GLY A 1 129 ? -30.196 12.621 104.789 1.00 42.03 ? 129 GLY A N 1 ATOM 932 C CA . GLY A 1 129 ? -31.237 12.849 105.791 1.00 41.68 ? 129 GLY A CA 1 ATOM 933 C C . GLY A 1 129 ? -32.627 12.362 105.428 1.00 41.39 ? 129 GLY A C 1 ATOM 934 O O . GLY A 1 129 ? -33.567 12.554 106.206 1.00 41.09 ? 129 GLY A O 1 ATOM 935 N N . VAL A 1 130 ? -32.769 11.751 104.246 1.00 39.47 ? 130 VAL A N 1 ATOM 936 C CA . VAL A 1 130 ? -34.047 11.186 103.808 1.00 37.55 ? 130 VAL A CA 1 ATOM 937 C C . VAL A 1 130 ? -33.876 9.733 103.402 1.00 36.66 ? 130 VAL A C 1 ATOM 938 O O . VAL A 1 130 ? -32.756 9.280 103.166 1.00 37.45 ? 130 VAL A O 1 ATOM 939 C CB . VAL A 1 130 ? -34.653 11.970 102.611 1.00 36.82 ? 130 VAL A CB 1 ATOM 940 C CG1 . VAL A 1 130 ? -35.027 13.383 103.036 1.00 36.72 ? 130 VAL A CG1 1 ATOM 941 C CG2 . VAL A 1 130 ? -33.685 11.977 101.426 1.00 35.84 ? 130 VAL A CG2 1 ATOM 942 N N . THR A 1 131 ? -34.992 9.008 103.354 1.00 35.57 ? 131 THR A N 1 ATOM 943 C CA . THR A 1 131 ? -35.029 7.664 102.808 1.00 36.41 ? 131 THR A CA 1 ATOM 944 C C . THR A 1 131 ? -35.284 7.774 101.298 1.00 36.30 ? 131 THR A C 1 ATOM 945 O O . THR A 1 131 ? -36.185 8.509 100.870 1.00 33.88 ? 131 THR A O 1 ATOM 946 C CB . THR A 1 131 ? -36.150 6.826 103.440 1.00 38.11 ? 131 THR A CB 1 ATOM 947 O OG1 . THR A 1 131 ? -36.004 6.816 104.870 1.00 38.91 ? 131 THR A OG1 1 ATOM 948 C CG2 . THR A 1 131 ? -36.121 5.388 102.920 1.00 38.21 ? 131 THR A CG2 1 ATOM 949 N N . GLN A 1 132 ? -34.481 7.057 100.514 1.00 35.45 ? 132 GLN A N 1 ATOM 950 C CA . GLN A 1 132 ? -34.601 7.043 99.049 1.00 34.78 ? 132 GLN A CA 1 ATOM 951 C C . GLN A 1 132 ? -35.366 5.808 98.604 1.00 35.10 ? 132 GLN A C 1 ATOM 952 O O . GLN A 1 132 ? -35.632 4.905 99.402 1.00 33.54 ? 132 GLN A O 1 ATOM 953 C CB . GLN A 1 132 ? -33.212 7.026 98.394 1.00 34.40 ? 132 GLN A CB 1 ATOM 954 C CG . GLN A 1 132 ? -32.358 8.246 98.678 1.00 34.53 ? 132 GLN A CG 1 ATOM 955 C CD . GLN A 1 132 ? -31.064 8.257 97.877 1.00 36.63 ? 132 GLN A CD 1 ATOM 956 O OE1 . GLN A 1 132 ? -31.060 8.029 96.655 1.00 36.13 ? 132 GLN A OE1 1 ATOM 957 N NE2 . GLN A 1 132 ? -29.954 8.532 98.555 1.00 35.23 ? 132 GLN A NE2 1 ATOM 958 N N . ASN A 1 133 ? -35.711 5.776 97.315 1.00 33.66 ? 133 ASN A N 1 ATOM 959 C CA . ASN A 1 133 ? -36.269 4.590 96.661 1.00 34.11 ? 133 ASN A CA 1 ATOM 960 C C . ASN A 1 133 ? -37.619 4.126 97.192 1.00 32.76 ? 133 ASN A C 1 ATOM 961 O O . ASN A 1 133 ? -37.867 2.922 97.302 1.00 31.75 ? 133 ASN A O 1 ATOM 962 C CB . ASN A 1 133 ? -35.278 3.418 96.686 1.00 36.64 ? 133 ASN A CB 1 ATOM 963 C CG . ASN A 1 133 ? -33.972 3.726 95.982 1.00 40.73 ? 133 ASN A CG 1 ATOM 964 O OD1 . ASN A 1 133 ? -33.813 4.783 95.346 1.00 37.95 ? 133 ASN A OD1 1 ATOM 965 N ND2 . ASN A 1 133 ? -33.017 2.791 96.085 1.00 47.37 ? 133 ASN A ND2 1 ATOM 966 N N . GLY A 1 134 ? -38.514 5.063 97.483 1.00 32.43 ? 134 GLY A N 1 ATOM 967 C CA . GLY A 1 134 ? -39.882 4.689 97.837 1.00 33.30 ? 134 GLY A CA 1 ATOM 968 C C . GLY A 1 134 ? -40.526 3.875 96.722 1.00 33.61 ? 134 GLY A C 1 ATOM 969 O O . GLY A 1 134 ? -40.268 4.126 95.525 1.00 32.59 ? 134 GLY A O 1 ATOM 970 N N . THR A 1 135 ? -41.345 2.897 97.107 1.00 33.31 ? 135 THR A N 1 ATOM 971 C CA . THR A 1 135 ? -42.049 2.047 96.152 1.00 34.75 ? 135 THR A CA 1 ATOM 972 C C . THR A 1 135 ? -43.552 1.992 96.433 1.00 35.34 ? 135 THR A C 1 ATOM 973 O O . THR A 1 135 ? -44.015 2.503 97.451 1.00 34.58 ? 135 THR A O 1 ATOM 974 C CB . THR A 1 135 ? -41.473 0.625 96.152 1.00 36.04 ? 135 THR A CB 1 ATOM 975 O OG1 . THR A 1 135 ? -41.664 0.028 97.445 1.00 35.88 ? 135 THR A OG1 1 ATOM 976 C CG2 . THR A 1 135 ? -39.967 0.652 95.812 1.00 36.21 ? 135 THR A CG2 1 ATOM 977 N N . SER A 1 136 ? -44.297 1.370 95.516 1.00 35.13 ? 136 SER A N 1 ATOM 978 C CA . SER A 1 136 ? -45.750 1.278 95.605 1.00 35.56 ? 136 SER A CA 1 ATOM 979 C C . SER A 1 136 ? -46.254 -0.025 94.986 1.00 36.80 ? 136 SER A C 1 ATOM 980 O O . SER A 1 136 ? -45.708 -0.513 93.979 1.00 35.25 ? 136 SER A O 1 ATOM 981 C CB . SER A 1 136 ? -46.402 2.475 94.899 1.00 36.02 ? 136 SER A CB 1 ATOM 982 O OG . SER A 1 136 ? -47.807 2.304 94.741 1.00 35.60 ? 136 SER A OG 1 ATOM 983 N N . SER A 1 137 ? -47.309 -0.582 95.584 1.00 36.83 ? 137 SER A N 1 ATOM 984 C CA . SER A 1 137 ? -47.984 -1.766 95.031 1.00 37.47 ? 137 SER A CA 1 ATOM 985 C C . SER A 1 137 ? -48.687 -1.443 93.710 1.00 37.55 ? 137 SER A C 1 ATOM 986 O O . SER A 1 137 ? -49.011 -2.354 92.945 1.00 37.35 ? 137 SER A O 1 ATOM 987 C CB . SER A 1 137 ? -49.000 -2.338 96.028 1.00 37.62 ? 137 SER A CB 1 ATOM 988 O OG . SER A 1 137 ? -50.084 -1.449 96.194 1.00 37.69 ? 137 SER A OG 1 ATOM 989 N N . ALA A 1 138 ? -48.917 -0.153 93.455 1.00 36.89 ? 138 ALA A N 1 ATOM 990 C CA . ALA A 1 138 ? -49.473 0.322 92.177 1.00 37.24 ? 138 ALA A CA 1 ATOM 991 C C . ALA A 1 138 ? -48.464 0.298 91.021 1.00 36.50 ? 138 ALA A C 1 ATOM 992 O O . ALA A 1 138 ? -48.833 0.572 89.877 1.00 37.00 ? 138 ALA A O 1 ATOM 993 C CB . ALA A 1 138 ? -50.031 1.737 92.337 1.00 35.57 ? 138 ALA A CB 1 ATOM 994 N N . CYS A 1 139 ? -47.204 -0.012 91.310 1.00 35.42 ? 139 CYS A N 1 ATOM 995 C CA . CYS A 1 139 ? -46.173 -0.004 90.290 1.00 35.94 ? 139 CYS A CA 1 ATOM 996 C C . CYS A 1 139 ? -45.246 -1.185 90.481 1.00 37.21 ? 139 CYS A C 1 ATOM 997 O O . CYS A 1 139 ? -44.104 -1.020 90.878 1.00 38.10 ? 139 CYS A O 1 ATOM 998 C CB . CYS A 1 139 ? -45.412 1.325 90.328 1.00 35.96 ? 139 CYS A CB 1 ATOM 999 S SG . CYS A 1 139 ? -44.241 1.583 88.961 1.00 35.30 ? 139 CYS A SG 1 ATOM 1000 N N . LYS A 1 140 ? -45.747 -2.377 90.170 1.00 38.09 ? 140 LYS A N 1 ATOM 1001 C CA . LYS A 1 140 ? -44.985 -3.617 90.354 1.00 40.37 ? 140 LYS A CA 1 ATOM 1002 C C . LYS A 1 140 ? -43.944 -3.799 89.257 1.00 40.37 ? 140 LYS A C 1 ATOM 1003 O O . LYS A 1 140 ? -44.252 -3.593 88.073 1.00 39.43 ? 140 LYS A O 1 ATOM 1004 C CB . LYS A 1 140 ? -45.907 -4.847 90.327 1.00 41.35 ? 140 LYS A CB 1 ATOM 1005 C CG . LYS A 1 140 ? -47.091 -4.808 91.277 1.00 43.07 ? 140 LYS A CG 1 ATOM 1006 C CD . LYS A 1 140 ? -46.789 -5.499 92.586 1.00 44.11 ? 140 LYS A CD 1 ATOM 1007 C CE . LYS A 1 140 ? -48.057 -5.746 93.384 1.00 45.77 ? 140 LYS A CE 1 ATOM 1008 N NZ . LYS A 1 140 ? -47.697 -6.049 94.797 1.00 47.95 ? 140 LYS A NZ 1 ATOM 1009 N N . ARG A 1 141 ? -42.731 -4.190 89.655 1.00 38.74 ? 141 ARG A N 1 ATOM 1010 C CA . ARG A 1 141 ? -41.658 -4.580 88.729 1.00 40.89 ? 141 ARG A CA 1 ATOM 1011 C C . ARG A 1 141 ? -41.191 -5.996 89.109 1.00 45.05 ? 141 ARG A C 1 ATOM 1012 O O . ARG A 1 141 ? -40.670 -6.208 90.212 1.00 44.39 ? 141 ARG A O 1 ATOM 1013 C CB . ARG A 1 141 ? -40.491 -3.579 88.788 1.00 38.98 ? 141 ARG A CB 1 ATOM 1014 C CG . ARG A 1 141 ? -39.298 -3.930 87.903 1.00 38.65 ? 141 ARG A CG 1 ATOM 1015 C CD . ARG A 1 141 ? -38.256 -2.817 87.861 1.00 37.26 ? 141 ARG A CD 1 ATOM 1016 N NE . ARG A 1 141 ? -38.566 -1.779 86.862 1.00 36.34 ? 141 ARG A NE 1 ATOM 1017 C CZ . ARG A 1 141 ? -39.057 -0.562 87.122 1.00 36.14 ? 141 ARG A CZ 1 ATOM 1018 N NH1 . ARG A 1 141 ? -39.338 -0.171 88.366 1.00 35.09 ? 141 ARG A NH1 1 ATOM 1019 N NH2 . ARG A 1 141 ? -39.280 0.291 86.114 1.00 35.17 ? 141 ARG A NH2 1 ATOM 1020 N N . LYS A 1 142 ? -41.397 -6.951 88.199 1.00 48.87 ? 142 LYS A N 1 ATOM 1021 C CA . LYS A 1 142 ? -41.143 -8.377 88.461 1.00 52.65 ? 142 LYS A CA 1 ATOM 1022 C C . LYS A 1 142 ? -41.780 -8.812 89.783 1.00 53.04 ? 142 LYS A C 1 ATOM 1023 O O . LYS A 1 142 ? -41.111 -9.347 90.665 1.00 53.81 ? 142 LYS A O 1 ATOM 1024 C CB . LYS A 1 142 ? -39.638 -8.692 88.431 1.00 54.58 ? 142 LYS A CB 1 ATOM 1025 C CG . LYS A 1 142 ? -39.006 -8.531 87.052 1.00 57.23 ? 142 LYS A CG 1 ATOM 1026 C CD . LYS A 1 142 ? -39.522 -9.578 86.062 1.00 59.31 ? 142 LYS A CD 1 ATOM 1027 C CE . LYS A 1 142 ? -39.312 -9.154 84.615 1.00 59.73 ? 142 LYS A CE 1 ATOM 1028 N NZ . LYS A 1 142 ? -37.870 -9.162 84.253 1.00 60.63 ? 142 LYS A NZ 1 ATOM 1029 N N . SER A 1 143 ? -43.076 -8.525 89.902 1.00 53.10 ? 143 SER A N 1 ATOM 1030 C CA . SER A 1 143 ? -43.910 -8.922 91.045 1.00 54.16 ? 143 SER A CA 1 ATOM 1031 C C . SER A 1 143 ? -43.589 -8.259 92.400 1.00 52.12 ? 143 SER A C 1 ATOM 1032 O O . SER A 1 143 ? -44.278 -8.526 93.391 1.00 54.93 ? 143 SER A O 1 ATOM 1033 C CB . SER A 1 143 ? -43.934 -10.451 91.181 1.00 55.79 ? 143 SER A CB 1 ATOM 1034 O OG . SER A 1 143 ? -44.455 -11.035 89.996 1.00 57.16 ? 143 SER A OG 1 ATOM 1035 N N . ASN A 1 144 ? -42.584 -7.383 92.444 1.00 47.85 ? 144 ASN A N 1 ATOM 1036 C CA . ASN A 1 144 ? -42.286 -6.611 93.648 1.00 45.64 ? 144 ASN A CA 1 ATOM 1037 C C . ASN A 1 144 ? -42.779 -5.182 93.523 1.00 43.77 ? 144 ASN A C 1 ATOM 1038 O O . ASN A 1 144 ? -42.816 -4.632 92.414 1.00 40.10 ? 144 ASN A O 1 ATOM 1039 C CB . ASN A 1 144 ? -40.787 -6.596 93.914 1.00 47.85 ? 144 ASN A CB 1 ATOM 1040 C CG . ASN A 1 144 ? -40.275 -7.933 94.399 1.00 50.83 ? 144 ASN A CG 1 ATOM 1041 O OD1 . ASN A 1 144 ? -41.057 -8.832 94.718 1.00 51.03 ? 144 ASN A OD1 1 ATOM 1042 N ND2 . ASN A 1 144 ? -38.959 -8.073 94.457 1.00 53.51 ? 144 ASN A ND2 1 ATOM 1043 N N . ASN A 1 145 ? -43.152 -4.588 94.656 1.00 39.24 ? 145 ASN A N 1 ATOM 1044 C CA . ASN A 1 145 ? -43.471 -3.167 94.701 1.00 37.53 ? 145 ASN A CA 1 ATOM 1045 C C . ASN A 1 145 ? -42.285 -2.389 94.169 1.00 35.39 ? 145 ASN A C 1 ATOM 1046 O O . ASN A 1 145 ? -41.147 -2.690 94.512 1.00 33.19 ? 145 ASN A O 1 ATOM 1047 C CB . ASN A 1 145 ? -43.766 -2.711 96.128 1.00 37.89 ? 145 ASN A CB 1 ATOM 1048 C CG . ASN A 1 145 ? -45.094 -3.219 96.651 1.00 38.09 ? 145 ASN A CG 1 ATOM 1049 O OD1 . ASN A 1 145 ? -45.776 -4.014 95.999 1.00 37.83 ? 145 ASN A OD1 1 ATOM 1050 N ND2 . ASN A 1 145 ? -45.473 -2.751 97.843 1.00 38.03 ? 145 ASN A ND2 1 ATOM 1051 N N . SER A 1 146 ? -42.551 -1.384 93.330 1.00 34.19 ? 146 SER A N 1 ATOM 1052 C CA . SER A 1 146 ? -41.476 -0.619 92.711 1.00 32.18 ? 146 SER A CA 1 ATOM 1053 C C . SER A 1 146 ? -41.951 0.808 92.404 1.00 30.70 ? 146 SER A C 1 ATOM 1054 O O . SER A 1 146 ? -42.859 1.331 93.063 1.00 28.61 ? 146 SER A O 1 ATOM 1055 C CB . SER A 1 146 ? -40.981 -1.340 91.442 1.00 32.86 ? 146 SER A CB 1 ATOM 1056 O OG . SER A 1 146 ? -39.674 -0.912 91.069 1.00 31.77 ? 146 SER A OG 1 ATOM 1057 N N . PHE A 1 147 ? -41.314 1.440 91.422 1.00 29.58 ? 147 PHE A N 1 ATOM 1058 C CA . PHE A 1 147 ? -41.613 2.829 91.072 1.00 28.26 ? 147 PHE A CA 1 ATOM 1059 C C . PHE A 1 147 ? -41.014 3.118 89.701 1.00 26.82 ? 147 PHE A C 1 ATOM 1060 O O . PHE A 1 147 ? -40.235 2.306 89.163 1.00 26.73 ? 147 PHE A O 1 ATOM 1061 C CB . PHE A 1 147 ? -40.972 3.760 92.109 1.00 27.89 ? 147 PHE A CB 1 ATOM 1062 C CG . PHE A 1 147 ? -41.559 5.143 92.146 1.00 27.59 ? 147 PHE A CG 1 ATOM 1063 C CD1 . PHE A 1 147 ? -42.893 5.334 92.480 1.00 27.44 ? 147 PHE A CD1 1 ATOM 1064 C CD2 . PHE A 1 147 ? -40.771 6.256 91.865 1.00 27.66 ? 147 PHE A CD2 1 ATOM 1065 C CE1 . PHE A 1 147 ? -43.433 6.602 92.544 1.00 27.23 ? 147 PHE A CE1 1 ATOM 1066 C CE2 . PHE A 1 147 ? -41.310 7.529 91.912 1.00 27.17 ? 147 PHE A CE2 1 ATOM 1067 C CZ . PHE A 1 147 ? -42.640 7.705 92.252 1.00 27.47 ? 147 PHE A CZ 1 ATOM 1068 N N . PHE A 1 148 ? -41.344 4.282 89.158 1.00 25.05 ? 148 PHE A N 1 ATOM 1069 C CA . PHE A 1 148 ? -40.720 4.751 87.924 1.00 24.72 ? 148 PHE A CA 1 ATOM 1070 C C . PHE A 1 148 ? -39.203 4.637 88.023 1.00 25.11 ? 148 PHE A C 1 ATOM 1071 O O . PHE A 1 148 ? -38.586 5.132 88.980 1.00 25.42 ? 148 PHE A O 1 ATOM 1072 C CB . PHE A 1 148 ? -41.066 6.212 87.679 1.00 24.19 ? 148 PHE A CB 1 ATOM 1073 C CG . PHE A 1 148 ? -42.529 6.458 87.478 1.00 24.29 ? 148 PHE A CG 1 ATOM 1074 C CD1 . PHE A 1 148 ? -43.157 6.083 86.305 1.00 24.74 ? 148 PHE A CD1 1 ATOM 1075 C CD2 . PHE A 1 148 ? -43.274 7.047 88.471 1.00 25.17 ? 148 PHE A CD2 1 ATOM 1076 C CE1 . PHE A 1 148 ? -44.518 6.327 86.113 1.00 25.35 ? 148 PHE A CE1 1 ATOM 1077 C CE2 . PHE A 1 148 ? -44.630 7.284 88.304 1.00 25.86 ? 148 PHE A CE2 1 ATOM 1078 C CZ . PHE A 1 148 ? -45.256 6.922 87.117 1.00 25.86 ? 148 PHE A CZ 1 ATOM 1079 N N . SER A 1 149 ? -38.600 3.997 87.028 1.00 24.74 ? 149 SER A N 1 ATOM 1080 C CA . SER A 1 149 ? -37.158 3.763 87.055 1.00 25.37 ? 149 SER A CA 1 ATOM 1081 C C . SER A 1 149 ? -36.312 5.032 87.162 1.00 24.75 ? 149 SER A C 1 ATOM 1082 O O . SER A 1 149 ? -35.240 5.019 87.790 1.00 23.74 ? 149 SER A O 1 ATOM 1083 C CB . SER A 1 149 ? -36.716 2.935 85.839 1.00 25.64 ? 149 SER A CB 1 ATOM 1084 O OG . SER A 1 149 ? -36.736 3.686 84.624 1.00 24.70 ? 149 SER A OG 1 ATOM 1085 N N . ARG A 1 150 ? -36.764 6.126 86.545 1.00 23.17 ? 150 ARG A N 1 ATOM 1086 C CA . ARG A 1 150 ? -35.939 7.326 86.465 1.00 23.26 ? 150 ARG A CA 1 ATOM 1087 C C . ARG A 1 150 ? -36.226 8.339 87.565 1.00 23.13 ? 150 ARG A C 1 ATOM 1088 O O . ARG A 1 150 ? -35.614 9.420 87.599 1.00 22.61 ? 150 ARG A O 1 ATOM 1089 C CB . ARG A 1 150 ? -36.085 7.985 85.082 1.00 22.79 ? 150 ARG A CB 1 ATOM 1090 C CG . ARG A 1 150 ? -35.885 7.015 83.928 1.00 22.79 ? 150 ARG A CG 1 ATOM 1091 C CD . ARG A 1 150 ? -34.534 6.331 84.023 1.00 23.76 ? 150 ARG A CD 1 ATOM 1092 N NE . ARG A 1 150 ? -34.097 5.736 82.769 1.00 23.32 ? 150 ARG A NE 1 ATOM 1093 C CZ . ARG A 1 150 ? -32.977 5.028 82.607 1.00 23.63 ? 150 ARG A CZ 1 ATOM 1094 N NH1 . ARG A 1 150 ? -32.151 4.797 83.638 1.00 23.73 ? 150 ARG A NH1 1 ATOM 1095 N NH2 . ARG A 1 150 ? -32.664 4.562 81.398 1.00 23.02 ? 150 ARG A NH2 1 ATOM 1096 N N . LEU A 1 151 ? -37.135 7.983 88.470 1.00 23.40 ? 151 LEU A N 1 ATOM 1097 C CA . LEU A 1 151 ? -37.528 8.867 89.544 1.00 23.39 ? 151 LEU A CA 1 ATOM 1098 C C . LEU A 1 151 ? -37.236 8.231 90.903 1.00 24.12 ? 151 LEU A C 1 ATOM 1099 O O . LEU A 1 151 ? -37.134 7.003 91.037 1.00 24.77 ? 151 LEU A O 1 ATOM 1100 C CB . LEU A 1 151 ? -38.998 9.247 89.412 1.00 23.19 ? 151 LEU A CB 1 ATOM 1101 C CG . LEU A 1 151 ? -39.322 10.076 88.153 1.00 22.90 ? 151 LEU A CG 1 ATOM 1102 C CD1 . LEU A 1 151 ? -40.820 10.130 87.952 1.00 21.93 ? 151 LEU A CD1 1 ATOM 1103 C CD2 . LEU A 1 151 ? -38.716 11.482 88.221 1.00 22.47 ? 151 LEU A CD2 1 ATOM 1104 N N . ASN A 1 152 ? -37.097 9.089 91.901 1.00 25.07 ? 152 ASN A N 1 ATOM 1105 C CA . ASN A 1 152 ? -36.647 8.665 93.246 1.00 25.67 ? 152 ASN A CA 1 ATOM 1106 C C . ASN A 1 152 ? -37.588 9.253 94.289 1.00 26.23 ? 152 ASN A C 1 ATOM 1107 O O . ASN A 1 152 ? -37.567 10.447 94.555 1.00 26.92 ? 152 ASN A O 1 ATOM 1108 C CB . ASN A 1 152 ? -35.205 9.120 93.475 1.00 26.12 ? 152 ASN A CB 1 ATOM 1109 C CG . ASN A 1 152 ? -34.600 8.526 94.737 1.00 26.96 ? 152 ASN A CG 1 ATOM 1110 O OD1 . ASN A 1 152 ? -35.301 7.879 95.518 1.00 26.37 ? 152 ASN A OD1 1 ATOM 1111 N ND2 . ASN A 1 152 ? -33.298 8.719 94.924 1.00 27.60 ? 152 ASN A ND2 1 ATOM 1112 N N . TRP A 1 153 ? -38.436 8.402 94.846 1.00 27.77 ? 153 TRP A N 1 ATOM 1113 C CA . TRP A 1 153 ? -39.414 8.816 95.835 1.00 28.91 ? 153 TRP A CA 1 ATOM 1114 C C . TRP A 1 153 ? -38.759 8.911 97.194 1.00 29.79 ? 153 TRP A C 1 ATOM 1115 O O . TRP A 1 153 ? -38.539 7.892 97.843 1.00 30.37 ? 153 TRP A O 1 ATOM 1116 C CB . TRP A 1 153 ? -40.543 7.805 95.878 1.00 29.12 ? 153 TRP A CB 1 ATOM 1117 C CG . TRP A 1 153 ? -41.767 8.248 96.633 1.00 29.58 ? 153 TRP A CG 1 ATOM 1118 C CD1 . TRP A 1 153 ? -41.944 9.405 97.386 1.00 30.18 ? 153 TRP A CD1 1 ATOM 1119 C CD2 . TRP A 1 153 ? -43.045 7.540 96.715 1.00 30.32 ? 153 TRP A CD2 1 ATOM 1120 N NE1 . TRP A 1 153 ? -43.213 9.463 97.897 1.00 29.83 ? 153 TRP A NE1 1 ATOM 1121 C CE2 . TRP A 1 153 ? -43.924 8.374 97.534 1.00 30.47 ? 153 TRP A CE2 1 ATOM 1122 C CE3 . TRP A 1 153 ? -43.536 6.350 96.195 1.00 31.49 ? 153 TRP A CE3 1 ATOM 1123 C CZ2 . TRP A 1 153 ? -45.235 8.010 97.813 1.00 31.87 ? 153 TRP A CZ2 1 ATOM 1124 C CZ3 . TRP A 1 153 ? -44.862 5.982 96.493 1.00 32.35 ? 153 TRP A CZ3 1 ATOM 1125 C CH2 . TRP A 1 153 ? -45.689 6.800 97.281 1.00 33.03 ? 153 TRP A CH2 1 ATOM 1126 N N . LEU A 1 154 ? -38.477 10.144 97.628 1.00 30.09 ? 154 LEU A N 1 ATOM 1127 C CA . LEU A 1 154 ? -37.842 10.417 98.927 1.00 30.81 ? 154 LEU A CA 1 ATOM 1128 C C . LEU A 1 154 ? -38.896 10.539 100.032 1.00 31.64 ? 154 LEU A C 1 ATOM 1129 O O . LEU A 1 154 ? -39.911 11.226 99.857 1.00 29.61 ? 154 LEU A O 1 ATOM 1130 C CB . LEU A 1 154 ? -37.051 11.722 98.858 1.00 31.56 ? 154 LEU A CB 1 ATOM 1131 C CG . LEU A 1 154 ? -36.037 11.875 97.717 1.00 31.43 ? 154 LEU A CG 1 ATOM 1132 C CD1 . LEU A 1 154 ? -35.399 13.255 97.763 1.00 32.60 ? 154 LEU A CD1 1 ATOM 1133 C CD2 . LEU A 1 154 ? -34.982 10.783 97.752 1.00 31.35 ? 154 LEU A CD2 1 ATOM 1134 N N . THR A 1 155 ? -38.648 9.868 101.163 1.00 32.22 ? 155 THR A N 1 ATOM 1135 C CA . THR A 1 155 ? -39.540 9.925 102.335 1.00 32.93 ? 155 THR A CA 1 ATOM 1136 C C . THR A 1 155 ? -38.695 10.209 103.582 1.00 33.45 ? 155 THR A C 1 ATOM 1137 O O . THR A 1 155 ? -37.470 10.241 103.501 1.00 31.78 ? 155 THR A O 1 ATOM 1138 C CB . THR A 1 155 ? -40.324 8.606 102.531 1.00 32.63 ? 155 THR A CB 1 ATOM 1139 O OG1 . THR A 1 155 ? -39.415 7.509 102.661 1.00 32.78 ? 155 THR A OG1 1 ATOM 1140 C CG2 . THR A 1 155 ? -41.252 8.356 101.341 1.00 32.46 ? 155 THR A CG2 1 ATOM 1141 N N . HIS A 1 156 ? -39.346 10.412 104.726 1.00 35.46 ? 156 HIS A N 1 ATOM 1142 C CA . HIS A 1 156 ? -38.615 10.773 105.946 1.00 36.82 ? 156 HIS A CA 1 ATOM 1143 C C . HIS A 1 156 ? -37.643 9.707 106.350 1.00 37.20 ? 156 HIS A C 1 ATOM 1144 O O . HIS A 1 156 ? -37.780 8.541 105.959 1.00 37.21 ? 156 HIS A O 1 ATOM 1145 C CB . HIS A 1 156 ? -39.577 11.079 107.097 1.00 37.15 ? 156 HIS A CB 1 ATOM 1146 C CG . HIS A 1 156 ? -40.240 9.860 107.690 1.00 37.22 ? 156 HIS A CG 1 ATOM 1147 N ND1 . HIS A 1 156 ? -39.562 8.941 108.411 1.00 38.44 ? 156 HIS A ND1 1 ATOM 1148 C CD2 . HIS A 1 156 ? -41.568 9.455 107.687 1.00 37.87 ? 156 HIS A CD2 1 ATOM 1149 C CE1 . HIS A 1 156 ? -40.409 7.981 108.819 1.00 38.48 ? 156 HIS A CE1 1 ATOM 1150 N NE2 . HIS A 1 156 ? -41.640 8.299 108.383 1.00 38.75 ? 156 HIS A NE2 1 ATOM 1151 N N . LEU A 1 157 ? -36.644 10.114 107.136 1.00 39.68 ? 157 LEU A N 1 ATOM 1152 C CA . LEU A 1 157 ? -35.696 9.203 107.773 1.00 39.42 ? 157 LEU A CA 1 ATOM 1153 C C . LEU A 1 157 ? -35.806 9.410 109.289 1.00 39.75 ? 157 LEU A C 1 ATOM 1154 O O . LEU A 1 157 ? -35.583 10.521 109.775 1.00 39.55 ? 157 LEU A O 1 ATOM 1155 C CB . LEU A 1 157 ? -34.271 9.521 107.308 1.00 39.57 ? 157 LEU A CB 1 ATOM 1156 C CG . LEU A 1 157 ? -33.140 8.656 107.871 1.00 39.39 ? 157 LEU A CG 1 ATOM 1157 C CD1 . LEU A 1 157 ? -33.332 7.190 107.495 1.00 40.43 ? 157 LEU A CD1 1 ATOM 1158 C CD2 . LEU A 1 157 ? -31.783 9.159 107.416 1.00 38.51 ? 157 LEU A CD2 1 ATOM 1159 N N . LYS A 1 158 ? -36.181 8.358 110.017 1.00 45.47 ? 158 LYS A N 1 ATOM 1160 C CA . LYS A 1 158 ? -36.356 8.430 111.480 1.00 47.98 ? 158 LYS A CA 1 ATOM 1161 C C . LYS A 1 158 ? -37.340 9.544 111.865 1.00 47.35 ? 158 LYS A C 1 ATOM 1162 O O . LYS A 1 158 ? -37.103 10.301 112.808 1.00 46.53 ? 158 LYS A O 1 ATOM 1163 C CB . LYS A 1 158 ? -35.007 8.665 112.188 1.00 50.24 ? 158 LYS A CB 1 ATOM 1164 C CG . LYS A 1 158 ? -33.858 7.761 111.758 1.00 52.99 ? 158 LYS A CG 1 ATOM 1165 C CD . LYS A 1 158 ? -34.088 6.298 112.110 1.00 56.12 ? 158 LYS A CD 1 ATOM 1166 C CE . LYS A 1 158 ? -32.777 5.515 112.110 1.00 58.03 ? 158 LYS A CE 1 ATOM 1167 N NZ . LYS A 1 158 ? -32.068 5.582 110.796 1.00 59.10 ? 158 LYS A NZ 1 ATOM 1168 N N . PHE A 1 159 ? -38.425 9.652 111.102 1.00 44.72 ? 159 PHE A N 1 ATOM 1169 C CA . PHE A 1 159 ? -39.451 10.685 111.285 1.00 44.54 ? 159 PHE A CA 1 ATOM 1170 C C . PHE A 1 159 ? -38.935 12.126 111.212 1.00 43.57 ? 159 PHE A C 1 ATOM 1171 O O . PHE A 1 159 ? -39.552 13.040 111.757 1.00 41.50 ? 159 PHE A O 1 ATOM 1172 C CB . PHE A 1 159 ? -40.236 10.438 112.575 1.00 47.00 ? 159 PHE A CB 1 ATOM 1173 C CG . PHE A 1 159 ? -40.726 9.028 112.705 1.00 48.93 ? 159 PHE A CG 1 ATOM 1174 C CD1 . PHE A 1 159 ? -41.873 8.617 112.038 1.00 48.86 ? 159 PHE A CD1 1 ATOM 1175 C CD2 . PHE A 1 159 ? -40.020 8.096 113.468 1.00 50.38 ? 159 PHE A CD2 1 ATOM 1176 C CE1 . PHE A 1 159 ? -42.318 7.308 112.137 1.00 51.00 ? 159 PHE A CE1 1 ATOM 1177 C CE2 . PHE A 1 159 ? -40.460 6.786 113.571 1.00 51.17 ? 159 PHE A CE2 1 ATOM 1178 C CZ . PHE A 1 159 ? -41.612 6.391 112.907 1.00 51.20 ? 159 PHE A CZ 1 ATOM 1179 N N . LYS A 1 160 ? -37.821 12.322 110.506 1.00 43.87 ? 160 LYS A N 1 ATOM 1180 C CA . LYS A 1 160 ? -37.373 13.656 110.123 1.00 43.66 ? 160 LYS A CA 1 ATOM 1181 C C . LYS A 1 160 ? -37.215 13.748 108.596 1.00 41.39 ? 160 LYS A C 1 ATOM 1182 O O . LYS A 1 160 ? -36.791 12.798 107.937 1.00 39.11 ? 160 LYS A O 1 ATOM 1183 C CB . LYS A 1 160 ? -36.055 14.010 110.801 1.00 46.73 ? 160 LYS A CB 1 ATOM 1184 C CG . LYS A 1 160 ? -36.182 14.217 112.307 1.00 50.10 ? 160 LYS A CG 1 ATOM 1185 C CD . LYS A 1 160 ? -34.998 14.991 112.877 1.00 52.64 ? 160 LYS A CD 1 ATOM 1186 C CE . LYS A 1 160 ? -35.220 15.365 114.341 1.00 55.25 ? 160 LYS A CE 1 ATOM 1187 N NZ . LYS A 1 160 ? -36.429 16.229 114.511 1.00 55.84 ? 160 LYS A NZ 1 ATOM 1188 N N . TYR A 1 161 ? -37.578 14.901 108.058 1.00 40.53 ? 161 TYR A N 1 ATOM 1189 C CA . TYR A 1 161 ? -37.326 15.235 106.660 1.00 39.63 ? 161 TYR A CA 1 ATOM 1190 C C . TYR A 1 161 ? -36.696 16.626 106.684 1.00 40.34 ? 161 TYR A C 1 ATOM 1191 O O . TYR A 1 161 ? -37.405 17.628 106.720 1.00 40.25 ? 161 TYR A O 1 ATOM 1192 C CB . TYR A 1 161 ? -38.636 15.214 105.874 1.00 38.77 ? 161 TYR A CB 1 ATOM 1193 C CG . TYR A 1 161 ? -38.496 15.218 104.362 1.00 37.22 ? 161 TYR A CG 1 ATOM 1194 C CD1 . TYR A 1 161 ? -37.926 16.297 103.690 1.00 37.08 ? 161 TYR A CD1 1 ATOM 1195 C CD2 . TYR A 1 161 ? -38.965 14.146 103.600 1.00 37.13 ? 161 TYR A CD2 1 ATOM 1196 C CE1 . TYR A 1 161 ? -37.816 16.302 102.300 1.00 35.15 ? 161 TYR A CE1 1 ATOM 1197 C CE2 . TYR A 1 161 ? -38.855 14.142 102.214 1.00 35.58 ? 161 TYR A CE2 1 ATOM 1198 C CZ . TYR A 1 161 ? -38.277 15.224 101.569 1.00 35.82 ? 161 TYR A CZ 1 ATOM 1199 O OH . TYR A 1 161 ? -38.176 15.221 100.178 1.00 33.11 ? 161 TYR A OH 1 ATOM 1200 N N . PRO A 1 162 ? -35.354 16.692 106.729 1.00 42.03 ? 162 PRO A N 1 ATOM 1201 C CA . PRO A 1 162 ? -34.701 17.993 106.791 1.00 43.26 ? 162 PRO A CA 1 ATOM 1202 C C . PRO A 1 162 ? -34.843 18.704 105.459 1.00 43.10 ? 162 PRO A C 1 ATOM 1203 O O . PRO A 1 162 ? -34.931 18.040 104.428 1.00 45.20 ? 162 PRO A O 1 ATOM 1204 C CB . PRO A 1 162 ? -33.237 17.641 107.055 1.00 44.43 ? 162 PRO A CB 1 ATOM 1205 C CG . PRO A 1 162 ? -33.061 16.299 106.435 1.00 45.34 ? 162 PRO A CG 1 ATOM 1206 C CD . PRO A 1 162 ? -34.380 15.592 106.616 1.00 44.71 ? 162 PRO A CD 1 ATOM 1207 N N . ALA A 1 163 ? -34.887 20.031 105.489 1.00 42.43 ? 163 ALA A N 1 ATOM 1208 C CA . ALA A 1 163 ? -35.034 20.827 104.282 1.00 41.68 ? 163 ALA A CA 1 ATOM 1209 C C . ALA A 1 163 ? -33.928 20.455 103.306 1.00 40.77 ? 163 ALA A C 1 ATOM 1210 O O . ALA A 1 163 ? -32.752 20.403 103.681 1.00 41.63 ? 163 ALA A O 1 ATOM 1211 C CB . ALA A 1 163 ? -34.982 22.310 104.604 1.00 42.18 ? 163 ALA A CB 1 ATOM 1212 N N . LEU A 1 164 ? -34.315 20.126 102.076 1.00 37.56 ? 164 LEU A N 1 ATOM 1213 C CA . LEU A 1 164 ? -33.345 19.801 101.040 1.00 37.46 ? 164 LEU A CA 1 ATOM 1214 C C . LEU A 1 164 ? -32.972 21.085 100.311 1.00 36.06 ? 164 LEU A C 1 ATOM 1215 O O . LEU A 1 164 ? -33.828 21.929 100.040 1.00 34.68 ? 164 LEU A O 1 ATOM 1216 C CB . LEU A 1 164 ? -33.909 18.767 100.057 1.00 37.17 ? 164 LEU A CB 1 ATOM 1217 C CG . LEU A 1 164 ? -34.292 17.404 100.655 1.00 38.06 ? 164 LEU A CG 1 ATOM 1218 C CD1 . LEU A 1 164 ? -35.018 16.550 99.623 1.00 37.12 ? 164 LEU A CD1 1 ATOM 1219 C CD2 . LEU A 1 164 ? -33.070 16.668 101.186 1.00 38.05 ? 164 LEU A CD2 1 ATOM 1220 N N . ASN A 1 165 ? -31.686 21.225 100.026 1.00 35.51 ? 165 ASN A N 1 ATOM 1221 C CA . ASN A 1 165 ? -31.166 22.329 99.258 1.00 36.60 ? 165 ASN A CA 1 ATOM 1222 C C . ASN A 1 165 ? -29.991 21.773 98.453 1.00 37.19 ? 165 ASN A C 1 ATOM 1223 O O . ASN A 1 165 ? -28.823 21.906 98.834 1.00 37.43 ? 165 ASN A O 1 ATOM 1224 C CB . ASN A 1 165 ? -30.757 23.481 100.172 1.00 38.38 ? 165 ASN A CB 1 ATOM 1225 C CG . ASN A 1 165 ? -30.250 24.674 99.398 1.00 40.18 ? 165 ASN A CG 1 ATOM 1226 O OD1 . ASN A 1 165 ? -30.914 25.149 98.470 1.00 40.49 ? 165 ASN A OD1 1 ATOM 1227 N ND2 . ASN A 1 165 ? -29.069 25.162 99.764 1.00 39.53 ? 165 ASN A ND2 1 ATOM 1228 N N . VAL A 1 166 ? -30.331 21.113 97.348 1.00 35.03 ? 166 VAL A N 1 ATOM 1229 C CA . VAL A 1 166 ? -29.416 20.211 96.669 1.00 34.71 ? 166 VAL A CA 1 ATOM 1230 C C . VAL A 1 166 ? -29.061 20.734 95.285 1.00 34.58 ? 166 VAL A C 1 ATOM 1231 O O . VAL A 1 166 ? -29.931 21.178 94.528 1.00 32.55 ? 166 VAL A O 1 ATOM 1232 C CB . VAL A 1 166 ? -30.034 18.801 96.588 1.00 35.17 ? 166 VAL A CB 1 ATOM 1233 C CG1 . VAL A 1 166 ? -29.130 17.857 95.823 1.00 34.94 ? 166 VAL A CG1 1 ATOM 1234 C CG2 . VAL A 1 166 ? -30.295 18.272 97.998 1.00 36.38 ? 166 VAL A CG2 1 ATOM 1235 N N . THR A 1 167 ? -27.778 20.654 94.955 1.00 35.11 ? 167 THR A N 1 ATOM 1236 C CA . THR A 1 167 ? -27.257 21.207 93.718 1.00 36.31 ? 167 THR A CA 1 ATOM 1237 C C . THR A 1 167 ? -26.714 20.138 92.733 1.00 35.28 ? 167 THR A C 1 ATOM 1238 O O . THR A 1 167 ? -26.208 19.071 93.138 1.00 34.43 ? 167 THR A O 1 ATOM 1239 C CB . THR A 1 167 ? -26.143 22.216 94.045 1.00 39.97 ? 167 THR A CB 1 ATOM 1240 O OG1 . THR A 1 167 ? -25.966 23.095 92.933 1.00 45.38 ? 167 THR A OG1 1 ATOM 1241 C CG2 . THR A 1 167 ? -24.844 21.499 94.346 1.00 40.05 ? 167 THR A CG2 1 ATOM 1242 N N . MET A 1 168 ? -26.818 20.430 91.436 1.00 32.90 ? 168 MET A N 1 ATOM 1243 C CA . MET A 1 168 ? -26.155 19.616 90.414 1.00 32.90 ? 168 MET A CA 1 ATOM 1244 C C . MET A 1 168 ? -25.680 20.505 89.262 1.00 33.34 ? 168 MET A C 1 ATOM 1245 O O . MET A 1 168 ? -26.492 20.951 88.447 1.00 32.92 ? 168 MET A O 1 ATOM 1246 C CB . MET A 1 168 ? -27.096 18.527 89.896 1.00 32.56 ? 168 MET A CB 1 ATOM 1247 C CG . MET A 1 168 ? -26.424 17.474 89.029 1.00 32.09 ? 168 MET A CG 1 ATOM 1248 S SD . MET A 1 168 ? -25.125 16.528 89.883 1.00 32.77 ? 168 MET A SD 1 ATOM 1249 C CE . MET A 1 168 ? -26.125 15.635 91.070 1.00 31.97 ? 168 MET A CE 1 ATOM 1250 N N . PRO A 1 169 ? -24.364 20.773 89.190 1.00 33.85 ? 169 PRO A N 1 ATOM 1251 C CA . PRO A 1 169 ? -23.866 21.627 88.119 1.00 33.88 ? 169 PRO A CA 1 ATOM 1252 C C . PRO A 1 169 ? -23.831 20.887 86.790 1.00 32.23 ? 169 PRO A C 1 ATOM 1253 O O . PRO A 1 169 ? -23.668 19.666 86.768 1.00 32.60 ? 169 PRO A O 1 ATOM 1254 C CB . PRO A 1 169 ? -22.445 21.967 88.575 1.00 35.51 ? 169 PRO A CB 1 ATOM 1255 C CG . PRO A 1 169 ? -22.028 20.793 89.388 1.00 35.91 ? 169 PRO A CG 1 ATOM 1256 C CD . PRO A 1 169 ? -23.270 20.267 90.047 1.00 35.40 ? 169 PRO A CD 1 ATOM 1257 N N . ASN A 1 170 ? -24.015 21.619 85.698 1.00 31.89 ? 170 ASN A N 1 ATOM 1258 C CA . ASN A 1 170 ? -23.794 21.082 84.363 1.00 32.22 ? 170 ASN A CA 1 ATOM 1259 C C . ASN A 1 170 ? -22.427 21.558 83.881 1.00 34.27 ? 170 ASN A C 1 ATOM 1260 O O . ASN A 1 170 ? -22.279 22.694 83.410 1.00 33.63 ? 170 ASN A O 1 ATOM 1261 C CB . ASN A 1 170 ? -24.903 21.515 83.375 1.00 31.59 ? 170 ASN A CB 1 ATOM 1262 C CG . ASN A 1 170 ? -24.708 20.933 81.977 1.00 31.80 ? 170 ASN A CG 1 ATOM 1263 O OD1 . ASN A 1 170 ? -23.689 20.296 81.687 1.00 32.33 ? 170 ASN A OD1 1 ATOM 1264 N ND2 . ASN A 1 170 ? -25.696 21.147 81.098 1.00 31.50 ? 170 ASN A ND2 1 ATOM 1265 N N . ASN A 1 171 ? -21.441 20.681 84.037 1.00 35.70 ? 171 ASN A N 1 ATOM 1266 C CA . ASN A 1 171 ? -20.082 20.915 83.548 1.00 38.41 ? 171 ASN A CA 1 ATOM 1267 C C . ASN A 1 171 ? -19.816 20.202 82.235 1.00 39.75 ? 171 ASN A C 1 ATOM 1268 O O . ASN A 1 171 ? -18.658 19.984 81.876 1.00 41.26 ? 171 ASN A O 1 ATOM 1269 C CB . ASN A 1 171 ? -19.068 20.470 84.606 1.00 39.24 ? 171 ASN A CB 1 ATOM 1270 C CG . ASN A 1 171 ? -19.245 21.207 85.912 1.00 39.98 ? 171 ASN A CG 1 ATOM 1271 O OD1 . ASN A 1 171 ? -19.273 20.598 86.980 1.00 44.13 ? 171 ASN A OD1 1 ATOM 1272 N ND2 . ASN A 1 171 ? -19.398 22.526 85.834 1.00 38.91 ? 171 ASN A ND2 1 ATOM 1273 N N . GLU A 1 172 ? -20.884 19.835 81.524 1.00 39.03 ? 172 GLU A N 1 ATOM 1274 C CA . GLU A 1 172 ? -20.774 19.186 80.216 1.00 39.64 ? 172 GLU A CA 1 ATOM 1275 C C . GLU A 1 172 ? -20.848 20.247 79.136 1.00 40.07 ? 172 GLU A C 1 ATOM 1276 O O . GLU A 1 172 ? -21.150 21.403 79.421 1.00 39.28 ? 172 GLU A O 1 ATOM 1277 C CB . GLU A 1 172 ? -21.911 18.182 79.981 1.00 40.20 ? 172 GLU A CB 1 ATOM 1278 C CG . GLU A 1 172 ? -22.123 17.172 81.090 1.00 41.17 ? 172 GLU A CG 1 ATOM 1279 C CD . GLU A 1 172 ? -20.921 16.283 81.312 1.00 43.95 ? 172 GLU A CD 1 ATOM 1280 O OE1 . GLU A 1 172 ? -20.257 15.907 80.325 1.00 45.15 ? 172 GLU A OE1 1 ATOM 1281 O OE2 . GLU A 1 172 ? -20.639 15.969 82.485 1.00 47.55 ? 172 GLU A OE2 1 ATOM 1282 N N . LYS A 1 173 ? -20.589 19.833 77.896 1.00 41.33 ? 173 LYS A N 1 ATOM 1283 C CA . LYS A 1 173 ? -20.684 20.710 76.726 1.00 43.82 ? 173 LYS A CA 1 ATOM 1284 C C . LYS A 1 173 ? -22.075 20.691 76.092 1.00 41.11 ? 173 LYS A C 1 ATOM 1285 O O . LYS A 1 173 ? -22.320 21.429 75.139 1.00 42.15 ? 173 LYS A O 1 ATOM 1286 C CB . LYS A 1 173 ? -19.628 20.327 75.669 1.00 47.45 ? 173 LYS A CB 1 ATOM 1287 C CG . LYS A 1 173 ? -18.216 20.819 75.978 1.00 52.63 ? 173 LYS A CG 1 ATOM 1288 C CD . LYS A 1 173 ? -17.989 22.260 75.520 1.00 56.46 ? 173 LYS A CD 1 ATOM 1289 C CE . LYS A 1 173 ? -16.648 22.818 75.985 1.00 58.82 ? 173 LYS A CE 1 ATOM 1290 N NZ . LYS A 1 173 ? -15.495 21.995 75.520 1.00 60.49 ? 173 LYS A NZ 1 ATOM 1291 N N . PHE A 1 174 ? -22.988 19.882 76.635 1.00 38.55 ? 174 PHE A N 1 ATOM 1292 C CA . PHE A 1 174 ? -24.365 19.756 76.107 1.00 35.91 ? 174 PHE A CA 1 ATOM 1293 C C . PHE A 1 174 ? -25.436 20.048 77.167 1.00 34.01 ? 174 PHE A C 1 ATOM 1294 O O . PHE A 1 174 ? -25.151 20.086 78.365 1.00 33.49 ? 174 PHE A O 1 ATOM 1295 C CB . PHE A 1 174 ? -24.599 18.345 75.557 1.00 35.94 ? 174 PHE A CB 1 ATOM 1296 C CG . PHE A 1 174 ? -24.186 17.251 76.500 1.00 36.97 ? 174 PHE A CG 1 ATOM 1297 C CD1 . PHE A 1 174 ? -25.014 16.865 77.556 1.00 36.62 ? 174 PHE A CD1 1 ATOM 1298 C CD2 . PHE A 1 174 ? -22.969 16.606 76.341 1.00 37.52 ? 174 PHE A CD2 1 ATOM 1299 C CE1 . PHE A 1 174 ? -24.626 15.867 78.428 1.00 37.21 ? 174 PHE A CE1 1 ATOM 1300 C CE2 . PHE A 1 174 ? -22.577 15.597 77.210 1.00 38.38 ? 174 PHE A CE2 1 ATOM 1301 C CZ . PHE A 1 174 ? -23.405 15.229 78.257 1.00 38.93 ? 174 PHE A CZ 1 ATOM 1302 N N . ASP A 1 175 ? -26.673 20.210 76.713 1.00 31.39 ? 175 ASP A N 1 ATOM 1303 C CA . ASP A 1 175 ? -27.805 20.491 77.603 1.00 30.96 ? 175 ASP A CA 1 ATOM 1304 C C . ASP A 1 175 ? -28.258 19.225 78.304 1.00 28.84 ? 175 ASP A C 1 ATOM 1305 O O . ASP A 1 175 ? -28.122 18.131 77.767 1.00 29.29 ? 175 ASP A O 1 ATOM 1306 C CB . ASP A 1 175 ? -28.989 21.059 76.825 1.00 31.26 ? 175 ASP A CB 1 ATOM 1307 C CG . ASP A 1 175 ? -28.750 22.466 76.317 1.00 34.53 ? 175 ASP A CG 1 ATOM 1308 O OD1 . ASP A 1 175 ? -27.690 23.059 76.631 1.00 35.26 ? 175 ASP A OD1 1 ATOM 1309 O OD2 . ASP A 1 175 ? -29.640 22.981 75.604 1.00 33.98 ? 175 ASP A OD2 1 ATOM 1310 N N . LYS A 1 176 ? -28.810 19.394 79.500 1.00 26.35 ? 176 LYS A N 1 ATOM 1311 C CA . LYS A 1 176 ? -29.383 18.300 80.261 1.00 25.04 ? 176 LYS A CA 1 ATOM 1312 C C . LYS A 1 176 ? -30.883 18.534 80.456 1.00 23.32 ? 176 LYS A C 1 ATOM 1313 O O . LYS A 1 176 ? -31.301 19.639 80.852 1.00 23.67 ? 176 LYS A O 1 ATOM 1314 C CB . LYS A 1 176 ? -28.735 18.230 81.652 1.00 25.60 ? 176 LYS A CB 1 ATOM 1315 C CG . LYS A 1 176 ? -27.249 17.914 81.692 1.00 26.23 ? 176 LYS A CG 1 ATOM 1316 C CD . LYS A 1 176 ? -26.781 17.950 83.143 1.00 27.34 ? 176 LYS A CD 1 ATOM 1317 C CE . LYS A 1 176 ? -25.330 17.525 83.313 1.00 27.82 ? 176 LYS A CE 1 ATOM 1318 N NZ . LYS A 1 176 ? -24.919 17.483 84.755 1.00 28.77 ? 176 LYS A NZ 1 ATOM 1319 N N . LEU A 1 177 ? -31.672 17.491 80.221 1.00 22.13 ? 177 LEU A N 1 ATOM 1320 C CA . LEU A 1 177 ? -33.115 17.515 80.470 1.00 21.35 ? 177 LEU A CA 1 ATOM 1321 C C . LEU A 1 177 ? -33.386 16.751 81.751 1.00 20.72 ? 177 LEU A C 1 ATOM 1322 O O . LEU A 1 177 ? -33.154 15.537 81.818 1.00 20.73 ? 177 LEU A O 1 ATOM 1323 C CB . LEU A 1 177 ? -33.897 16.869 79.309 1.00 21.03 ? 177 LEU A CB 1 ATOM 1324 C CG . LEU A 1 177 ? -35.404 16.640 79.500 1.00 20.82 ? 177 LEU A CG 1 ATOM 1325 C CD1 . LEU A 1 177 ? -36.148 17.951 79.705 1.00 20.49 ? 177 LEU A CD1 1 ATOM 1326 C CD2 . LEU A 1 177 ? -35.986 15.875 78.304 1.00 21.02 ? 177 LEU A CD2 1 ATOM 1327 N N . TYR A 1 178 ? -33.899 17.457 82.750 1.00 21.10 ? 178 TYR A N 1 ATOM 1328 C CA . TYR A 1 178 ? -34.308 16.838 84.012 1.00 21.85 ? 178 TYR A CA 1 ATOM 1329 C C . TYR A 1 178 ? -35.814 16.687 84.097 1.00 22.14 ? 178 TYR A C 1 ATOM 1330 O O . TYR A 1 178 ? -36.549 17.640 83.824 1.00 23.01 ? 178 TYR A O 1 ATOM 1331 C CB . TYR A 1 178 ? -33.832 17.670 85.191 1.00 21.80 ? 178 TYR A CB 1 ATOM 1332 C CG . TYR A 1 178 ? -32.356 17.560 85.446 1.00 22.19 ? 178 TYR A CG 1 ATOM 1333 C CD1 . TYR A 1 178 ? -31.836 16.500 86.185 1.00 22.61 ? 178 TYR A CD1 1 ATOM 1334 C CD2 . TYR A 1 178 ? -31.474 18.507 84.947 1.00 22.73 ? 178 TYR A CD2 1 ATOM 1335 C CE1 . TYR A 1 178 ? -30.470 16.388 86.422 1.00 23.45 ? 178 TYR A CE1 1 ATOM 1336 C CE2 . TYR A 1 178 ? -30.114 18.416 85.194 1.00 23.61 ? 178 TYR A CE2 1 ATOM 1337 C CZ . TYR A 1 178 ? -29.614 17.350 85.930 1.00 23.63 ? 178 TYR A CZ 1 ATOM 1338 O OH . TYR A 1 178 ? -28.258 17.278 86.154 1.00 25.25 ? 178 TYR A OH 1 ATOM 1339 N N . ILE A 1 179 ? -36.259 15.497 84.503 1.00 21.84 ? 179 ILE A N 1 ATOM 1340 C CA . ILE A 1 179 ? -37.675 15.198 84.730 1.00 21.60 ? 179 ILE A CA 1 ATOM 1341 C C . ILE A 1 179 ? -37.865 14.924 86.219 1.00 22.26 ? 179 ILE A C 1 ATOM 1342 O O . ILE A 1 179 ? -37.120 14.131 86.804 1.00 21.70 ? 179 ILE A O 1 ATOM 1343 C CB . ILE A 1 179 ? -38.108 13.939 83.950 1.00 21.79 ? 179 ILE A CB 1 ATOM 1344 C CG1 . ILE A 1 179 ? -37.751 14.057 82.456 1.00 21.68 ? 179 ILE A CG1 1 ATOM 1345 C CG2 . ILE A 1 179 ? -39.592 13.655 84.152 1.00 21.33 ? 179 ILE A CG2 1 ATOM 1346 C CD1 . ILE A 1 179 ? -38.399 15.231 81.718 1.00 21.91 ? 179 ILE A CD1 1 ATOM 1347 N N . TRP A 1 180 ? -38.839 15.590 86.828 1.00 21.94 ? 180 TRP A N 1 ATOM 1348 C CA . TRP A 1 180 ? -39.065 15.469 88.262 1.00 23.27 ? 180 TRP A CA 1 ATOM 1349 C C . TRP A 1 180 ? -40.521 15.635 88.550 1.00 23.42 ? 180 TRP A C 1 ATOM 1350 O O . TRP A 1 180 ? -41.308 15.892 87.637 1.00 23.14 ? 180 TRP A O 1 ATOM 1351 C CB . TRP A 1 180 ? -38.210 16.475 89.010 1.00 23.81 ? 180 TRP A CB 1 ATOM 1352 C CG . TRP A 1 180 ? -38.351 17.901 88.534 1.00 24.29 ? 180 TRP A CG 1 ATOM 1353 C CD1 . TRP A 1 180 ? -37.652 18.526 87.502 1.00 24.74 ? 180 TRP A CD1 1 ATOM 1354 C CD2 . TRP A 1 180 ? -39.233 18.927 89.080 1.00 24.37 ? 180 TRP A CD2 1 ATOM 1355 N NE1 . TRP A 1 180 ? -38.045 19.833 87.374 1.00 24.33 ? 180 TRP A NE1 1 ATOM 1356 C CE2 . TRP A 1 180 ? -38.991 20.135 88.299 1.00 24.71 ? 180 TRP A CE2 1 ATOM 1357 C CE3 . TRP A 1 180 ? -40.178 18.962 90.106 1.00 24.74 ? 180 TRP A CE3 1 ATOM 1358 C CZ2 . TRP A 1 180 ? -39.668 21.318 88.552 1.00 24.73 ? 180 TRP A CZ2 1 ATOM 1359 C CZ3 . TRP A 1 180 ? -40.843 20.164 90.364 1.00 24.65 ? 180 TRP A CZ3 1 ATOM 1360 C CH2 . TRP A 1 180 ? -40.615 21.307 89.584 1.00 24.53 ? 180 TRP A CH2 1 ATOM 1361 N N . GLY A 1 181 ? -40.907 15.471 89.810 1.00 23.60 ? 181 GLY A N 1 ATOM 1362 C CA . GLY A 1 181 ? -42.320 15.449 90.149 1.00 23.75 ? 181 GLY A CA 1 ATOM 1363 C C . GLY A 1 181 ? -42.657 15.924 91.540 1.00 24.60 ? 181 GLY A C 1 ATOM 1364 O O . GLY A 1 181 ? -41.781 16.056 92.401 1.00 24.26 ? 181 GLY A O 1 ATOM 1365 N N . VAL A 1 182 ? -43.947 16.172 91.742 1.00 24.35 ? 182 VAL A N 1 ATOM 1366 C CA . VAL A 1 182 ? -44.478 16.556 93.026 1.00 25.69 ? 182 VAL A CA 1 ATOM 1367 C C . VAL A 1 182 ? -45.563 15.551 93.368 1.00 25.47 ? 182 VAL A C 1 ATOM 1368 O O . VAL A 1 182 ? -46.429 15.266 92.551 1.00 24.92 ? 182 VAL A O 1 ATOM 1369 C CB . VAL A 1 182 ? -45.051 17.981 92.994 1.00 26.86 ? 182 VAL A CB 1 ATOM 1370 C CG1 . VAL A 1 182 ? -45.669 18.332 94.345 1.00 27.64 ? 182 VAL A CG1 1 ATOM 1371 C CG2 . VAL A 1 182 ? -43.939 18.960 92.644 1.00 27.76 ? 182 VAL A CG2 1 ATOM 1372 N N . HIS A 1 183 ? -45.490 14.993 94.566 1.00 25.68 ? 183 HIS A N 1 ATOM 1373 C CA . HIS A 1 183 ? -46.487 14.032 95.039 1.00 26.29 ? 183 HIS A CA 1 ATOM 1374 C C . HIS A 1 183 ? -47.583 14.753 95.779 1.00 26.72 ? 183 HIS A C 1 ATOM 1375 O O . HIS A 1 183 ? -47.307 15.524 96.703 1.00 26.59 ? 183 HIS A O 1 ATOM 1376 C CB . HIS A 1 183 ? -45.823 13.012 95.963 1.00 27.15 ? 183 HIS A CB 1 ATOM 1377 C CG . HIS A 1 183 ? -46.747 11.925 96.437 1.00 27.63 ? 183 HIS A CG 1 ATOM 1378 N ND1 . HIS A 1 183 ? -46.895 11.613 97.744 1.00 29.00 ? 183 HIS A ND1 1 ATOM 1379 C CD2 . HIS A 1 183 ? -47.582 11.065 95.731 1.00 28.08 ? 183 HIS A CD2 1 ATOM 1380 C CE1 . HIS A 1 183 ? -47.775 10.598 97.863 1.00 28.67 ? 183 HIS A CE1 1 ATOM 1381 N NE2 . HIS A 1 183 ? -48.196 10.264 96.630 1.00 28.52 ? 183 HIS A NE2 1 ATOM 1382 N N . HIS A 1 184 ? -48.824 14.509 95.357 1.00 27.05 ? 184 HIS A N 1 ATOM 1383 C CA . HIS A 1 184 ? -50.025 15.034 95.992 1.00 27.60 ? 184 HIS A CA 1 ATOM 1384 C C . HIS A 1 184 ? -50.675 13.893 96.749 1.00 27.82 ? 184 HIS A C 1 ATOM 1385 O O . HIS A 1 184 ? -51.344 13.065 96.140 1.00 27.30 ? 184 HIS A O 1 ATOM 1386 C CB . HIS A 1 184 ? -50.980 15.558 94.920 1.00 27.51 ? 184 HIS A CB 1 ATOM 1387 C CG . HIS A 1 184 ? -50.389 16.632 94.039 1.00 27.31 ? 184 HIS A CG 1 ATOM 1388 N ND1 . HIS A 1 184 ? -50.200 17.893 94.463 1.00 27.47 ? 184 HIS A ND1 1 ATOM 1389 C CD2 . HIS A 1 184 ? -49.951 16.591 92.706 1.00 26.77 ? 184 HIS A CD2 1 ATOM 1390 C CE1 . HIS A 1 184 ? -49.677 18.629 93.455 1.00 28.21 ? 184 HIS A CE1 1 ATOM 1391 N NE2 . HIS A 1 184 ? -49.527 17.828 92.381 1.00 26.92 ? 184 HIS A NE2 1 ATOM 1392 N N . PRO A 1 185 ? -50.450 13.794 98.080 1.00 28.42 ? 185 PRO A N 1 ATOM 1393 C CA . PRO A 1 185 ? -51.039 12.666 98.823 1.00 29.23 ? 185 PRO A CA 1 ATOM 1394 C C . PRO A 1 185 ? -52.554 12.750 98.973 1.00 29.95 ? 185 PRO A C 1 ATOM 1395 O O . PRO A 1 185 ? -53.114 13.841 99.016 1.00 30.02 ? 185 PRO A O 1 ATOM 1396 C CB . PRO A 1 185 ? -50.392 12.770 100.212 1.00 29.47 ? 185 PRO A CB 1 ATOM 1397 C CG . PRO A 1 185 ? -49.223 13.657 100.041 1.00 29.42 ? 185 PRO A CG 1 ATOM 1398 C CD . PRO A 1 185 ? -49.568 14.598 98.937 1.00 28.73 ? 185 PRO A CD 1 ATOM 1399 N N . GLY A 1 186 ? -53.201 11.593 99.071 1.00 31.56 ? 186 GLY A N 1 ATOM 1400 C CA . GLY A 1 186 ? -54.658 11.534 99.184 1.00 32.63 ? 186 GLY A CA 1 ATOM 1401 C C . GLY A 1 186 ? -55.206 12.173 100.455 1.00 34.26 ? 186 GLY A C 1 ATOM 1402 O O . GLY A 1 186 ? -56.261 12.810 100.422 1.00 34.56 ? 186 GLY A O 1 ATOM 1403 N N . THR A 1 187 ? -54.486 12.011 101.565 1.00 35.35 ? 187 THR A N 1 ATOM 1404 C CA . THR A 1 187 ? -54.930 12.486 102.889 1.00 36.85 ? 187 THR A CA 1 ATOM 1405 C C . THR A 1 187 ? -53.805 13.129 103.708 1.00 37.59 ? 187 THR A C 1 ATOM 1406 O O . THR A 1 187 ? -52.619 12.902 103.444 1.00 35.53 ? 187 THR A O 1 ATOM 1407 C CB . THR A 1 187 ? -55.501 11.315 103.714 1.00 38.06 ? 187 THR A CB 1 ATOM 1408 O OG1 . THR A 1 187 ? -54.432 10.458 104.154 1.00 38.27 ? 187 THR A OG1 1 ATOM 1409 C CG2 . THR A 1 187 ? -56.506 10.498 102.872 1.00 37.40 ? 187 THR A CG2 1 ATOM 1410 N N . ASP A 1 188 ? -54.186 13.909 104.720 1.00 40.39 ? 188 ASP A N 1 ATOM 1411 C CA . ASP A 1 188 ? -53.223 14.454 105.695 1.00 43.58 ? 188 ASP A CA 1 ATOM 1412 C C . ASP A 1 188 ? -52.459 13.340 106.434 1.00 43.74 ? 188 ASP A C 1 ATOM 1413 O O . ASP A 1 188 ? -51.302 13.527 106.805 1.00 42.68 ? 188 ASP A O 1 ATOM 1414 C CB . ASP A 1 188 ? -53.914 15.351 106.730 1.00 46.82 ? 188 ASP A CB 1 ATOM 1415 C CG . ASP A 1 188 ? -54.480 16.638 106.131 1.00 49.04 ? 188 ASP A CG 1 ATOM 1416 O OD1 . ASP A 1 188 ? -53.924 17.178 105.145 1.00 49.63 ? 188 ASP A OD1 1 ATOM 1417 O OD2 . ASP A 1 188 ? -55.497 17.124 106.669 1.00 50.80 ? 188 ASP A OD2 1 ATOM 1418 N N . ASN A 1 189 ? -53.110 12.198 106.653 1.00 44.38 ? 189 ASN A N 1 ATOM 1419 C CA . ASN A 1 189 ? -52.450 11.032 107.264 1.00 45.24 ? 189 ASN A CA 1 ATOM 1420 C C . ASN A 1 189 ? -51.263 10.546 106.435 1.00 42.95 ? 189 ASN A C 1 ATOM 1421 O O . ASN A 1 189 ? -50.203 10.235 106.977 1.00 40.75 ? 189 ASN A O 1 ATOM 1422 C CB . ASN A 1 189 ? -53.434 9.858 107.433 1.00 47.86 ? 189 ASN A CB 1 ATOM 1423 C CG . ASN A 1 189 ? -54.227 9.923 108.725 1.00 51.51 ? 189 ASN A CG 1 ATOM 1424 O OD1 . ASN A 1 189 ? -53.872 10.648 109.658 1.00 54.37 ? 189 ASN A OD1 1 ATOM 1425 N ND2 . ASN A 1 189 ? -55.312 9.149 108.788 1.00 52.56 ? 189 ASN A ND2 1 ATOM 1426 N N . ASP A 1 190 ? -51.459 10.461 105.119 1.00 41.76 ? 190 ASP A N 1 ATOM 1427 C CA . ASP A 1 190 ? -50.399 10.021 104.210 1.00 40.64 ? 190 ASP A CA 1 ATOM 1428 C C . ASP A 1 190 ? -49.249 11.022 104.183 1.00 37.58 ? 190 ASP A C 1 ATOM 1429 O O . ASP A 1 190 ? -48.090 10.632 104.099 1.00 36.08 ? 190 ASP A O 1 ATOM 1430 C CB . ASP A 1 190 ? -50.940 9.835 102.786 1.00 43.13 ? 190 ASP A CB 1 ATOM 1431 C CG . ASP A 1 190 ? -51.795 8.582 102.625 1.00 46.66 ? 190 ASP A CG 1 ATOM 1432 O OD1 . ASP A 1 190 ? -51.947 7.795 103.580 1.00 49.00 ? 190 ASP A OD1 1 ATOM 1433 O OD2 . ASP A 1 190 ? -52.314 8.376 101.511 1.00 50.80 ? 190 ASP A OD2 1 ATOM 1434 N N . GLN A 1 191 ? -49.581 12.310 104.236 1.00 36.00 ? 191 GLN A N 1 ATOM 1435 C CA . GLN A 1 191 ? -48.581 13.375 104.227 1.00 35.09 ? 191 GLN A CA 1 ATOM 1436 C C . GLN A 1 191 ? -47.611 13.211 105.391 1.00 35.66 ? 191 GLN A C 1 ATOM 1437 O O . GLN A 1 191 ? -46.397 13.270 105.216 1.00 35.45 ? 191 GLN A O 1 ATOM 1438 C CB . GLN A 1 191 ? -49.256 14.748 104.319 1.00 34.36 ? 191 GLN A CB 1 ATOM 1439 C CG . GLN A 1 191 ? -48.302 15.935 104.432 1.00 34.04 ? 191 GLN A CG 1 ATOM 1440 C CD . GLN A 1 191 ? -47.467 16.157 103.179 1.00 33.78 ? 191 GLN A CD 1 ATOM 1441 O OE1 . GLN A 1 191 ? -47.922 15.895 102.065 1.00 32.82 ? 191 GLN A OE1 1 ATOM 1442 N NE2 . GLN A 1 191 ? -46.243 16.665 103.357 1.00 33.67 ? 191 GLN A NE2 1 ATOM 1443 N N . ILE A 1 192 ? -48.158 13.010 106.583 1.00 37.08 ? 192 ILE A N 1 ATOM 1444 C CA . ILE A 1 192 ? -47.325 12.841 107.783 1.00 37.33 ? 192 ILE A CA 1 ATOM 1445 C C . ILE A 1 192 ? -46.584 11.503 107.758 1.00 37.38 ? 192 ILE A C 1 ATOM 1446 O O . ILE A 1 192 ? -45.391 11.431 108.070 1.00 36.73 ? 192 ILE A O 1 ATOM 1447 C CB . ILE A 1 192 ? -48.176 12.963 109.066 1.00 39.12 ? 192 ILE A CB 1 ATOM 1448 C CG1 . ILE A 1 192 ? -48.784 14.371 109.179 1.00 39.76 ? 192 ILE A CG1 1 ATOM 1449 C CG2 . ILE A 1 192 ? -47.343 12.639 110.304 1.00 40.38 ? 192 ILE A CG2 1 ATOM 1450 C CD1 . ILE A 1 192 ? -47.781 15.510 109.183 1.00 39.70 ? 192 ILE A CD1 1 ATOM 1451 N N . PHE A 1 193 ? -47.277 10.447 107.354 1.00 37.88 ? 193 PHE A N 1 ATOM 1452 C CA . PHE A 1 193 ? -46.661 9.127 107.271 1.00 38.82 ? 193 PHE A CA 1 ATOM 1453 C C . PHE A 1 193 ? -45.442 9.129 106.349 1.00 38.29 ? 193 PHE A C 1 ATOM 1454 O O . PHE A 1 193 ? -44.437 8.474 106.633 1.00 37.94 ? 193 PHE A O 1 ATOM 1455 C CB . PHE A 1 193 ? -47.680 8.094 106.798 1.00 40.42 ? 193 PHE A CB 1 ATOM 1456 C CG . PHE A 1 193 ? -47.129 6.704 106.698 1.00 42.99 ? 193 PHE A CG 1 ATOM 1457 C CD1 . PHE A 1 193 ? -47.165 5.849 107.797 1.00 45.24 ? 193 PHE A CD1 1 ATOM 1458 C CD2 . PHE A 1 193 ? -46.566 6.245 105.516 1.00 44.09 ? 193 PHE A CD2 1 ATOM 1459 C CE1 . PHE A 1 193 ? -46.650 4.562 107.712 1.00 46.52 ? 193 PHE A CE1 1 ATOM 1460 C CE2 . PHE A 1 193 ? -46.052 4.955 105.423 1.00 45.35 ? 193 PHE A CE2 1 ATOM 1461 C CZ . PHE A 1 193 ? -46.087 4.117 106.526 1.00 46.03 ? 193 PHE A CZ 1 ATOM 1462 N N . LEU A 1 194 ? -45.534 9.880 105.251 1.00 35.96 ? 194 LEU A N 1 ATOM 1463 C CA . LEU A 1 194 ? -44.471 9.907 104.255 1.00 34.84 ? 194 LEU A CA 1 ATOM 1464 C C . LEU A 1 194 ? -43.375 10.929 104.535 1.00 33.76 ? 194 LEU A C 1 ATOM 1465 O O . LEU A 1 194 ? -42.196 10.629 104.358 1.00 34.73 ? 194 LEU A O 1 ATOM 1466 C CB . LEU A 1 194 ? -45.069 10.194 102.873 1.00 33.84 ? 194 LEU A CB 1 ATOM 1467 C CG . LEU A 1 194 ? -45.937 9.108 102.244 1.00 34.09 ? 194 LEU A CG 1 ATOM 1468 C CD1 . LEU A 1 194 ? -46.674 9.669 101.026 1.00 32.15 ? 194 LEU A CD1 1 ATOM 1469 C CD2 . LEU A 1 194 ? -45.094 7.900 101.860 1.00 34.59 ? 194 LEU A CD2 1 ATOM 1470 N N . TYR A 1 195 ? -43.754 12.141 104.931 1.00 33.21 ? 195 TYR A N 1 ATOM 1471 C CA . TYR A 1 195 ? -42.796 13.251 105.013 1.00 34.02 ? 195 TYR A CA 1 ATOM 1472 C C . TYR A 1 195 ? -42.633 13.841 106.426 1.00 36.29 ? 195 TYR A C 1 ATOM 1473 O O . TYR A 1 195 ? -41.832 14.757 106.635 1.00 36.12 ? 195 TYR A O 1 ATOM 1474 C CB . TYR A 1 195 ? -43.176 14.336 103.992 1.00 33.56 ? 195 TYR A CB 1 ATOM 1475 C CG . TYR A 1 195 ? -43.512 13.743 102.636 1.00 31.34 ? 195 TYR A CG 1 ATOM 1476 C CD1 . TYR A 1 195 ? -42.536 13.112 101.874 1.00 31.26 ? 195 TYR A CD1 1 ATOM 1477 C CD2 . TYR A 1 195 ? -44.812 13.775 102.134 1.00 31.51 ? 195 TYR A CD2 1 ATOM 1478 C CE1 . TYR A 1 195 ? -42.833 12.547 100.654 1.00 30.57 ? 195 TYR A CE1 1 ATOM 1479 C CE2 . TYR A 1 195 ? -45.122 13.210 100.906 1.00 30.17 ? 195 TYR A CE2 1 ATOM 1480 C CZ . TYR A 1 195 ? -44.124 12.592 100.173 1.00 30.26 ? 195 TYR A CZ 1 ATOM 1481 O OH . TYR A 1 195 ? -44.412 12.007 98.954 1.00 30.74 ? 195 TYR A OH 1 ATOM 1482 N N . ALA A 1 196 ? -43.398 13.314 107.384 1.00 38.54 ? 196 ALA A N 1 ATOM 1483 C CA . ALA A 1 196 ? -43.261 13.673 108.810 1.00 40.47 ? 196 ALA A CA 1 ATOM 1484 C C . ALA A 1 196 ? -43.621 15.127 109.146 1.00 41.95 ? 196 ALA A C 1 ATOM 1485 O O . ALA A 1 196 ? -43.387 15.579 110.269 1.00 43.97 ? 196 ALA A O 1 ATOM 1486 C CB . ALA A 1 196 ? -41.858 13.341 109.296 1.00 39.68 ? 196 ALA A CB 1 ATOM 1487 N N . GLN A 1 197 ? -44.211 15.853 108.203 1.00 42.04 ? 197 GLN A N 1 ATOM 1488 C CA . GLN A 1 197 ? -44.582 17.252 108.435 1.00 43.48 ? 197 GLN A CA 1 ATOM 1489 C C . GLN A 1 197 ? -45.551 17.744 107.367 1.00 41.91 ? 197 GLN A C 1 ATOM 1490 O O . GLN A 1 197 ? -45.758 17.069 106.357 1.00 40.21 ? 197 GLN A O 1 ATOM 1491 C CB . GLN A 1 197 ? -43.331 18.143 108.486 1.00 45.24 ? 197 GLN A CB 1 ATOM 1492 C CG . GLN A 1 197 ? -42.468 18.096 107.231 1.00 46.09 ? 197 GLN A CG 1 ATOM 1493 C CD . GLN A 1 197 ? -40.994 18.366 107.494 1.00 47.81 ? 197 GLN A CD 1 ATOM 1494 O OE1 . GLN A 1 197 ? -40.579 18.641 108.624 1.00 50.29 ? 197 GLN A OE1 1 ATOM 1495 N NE2 . GLN A 1 197 ? -40.192 18.280 106.446 1.00 49.04 ? 197 GLN A NE2 1 ATOM 1496 N N . ALA A 1 198 ? -46.147 18.911 107.609 1.00 40.92 ? 198 ALA A N 1 ATOM 1497 C CA . ALA A 1 198 ? -47.125 19.505 106.692 1.00 41.16 ? 198 ALA A CA 1 ATOM 1498 C C . ALA A 1 198 ? -46.461 19.805 105.341 1.00 39.58 ? 198 ALA A C 1 ATOM 1499 O O . ALA A 1 198 ? -45.242 20.001 105.270 1.00 40.11 ? 198 ALA A O 1 ATOM 1500 C CB . ALA A 1 198 ? -47.700 20.783 107.290 1.00 41.52 ? 198 ALA A CB 1 ATOM 1501 N N . SER A 1 199 ? -47.261 19.822 104.283 1.00 38.63 ? 199 SER A N 1 ATOM 1502 C CA . SER A 1 199 ? -46.735 20.040 102.935 1.00 37.99 ? 199 SER A CA 1 ATOM 1503 C C . SER A 1 199 ? -46.313 21.493 102.776 1.00 38.63 ? 199 SER A C 1 ATOM 1504 O O . SER A 1 199 ? -46.888 22.394 103.393 1.00 37.79 ? 199 SER A O 1 ATOM 1505 C CB . SER A 1 199 ? -47.770 19.658 101.869 1.00 37.00 ? 199 SER A CB 1 ATOM 1506 O OG . SER A 1 199 ? -48.888 20.511 101.918 1.00 36.74 ? 199 SER A OG 1 ATOM 1507 N N . GLY A 1 200 ? -45.277 21.693 101.970 1.00 39.28 ? 200 GLY A N 1 ATOM 1508 C CA . GLY A 1 200 ? -44.796 23.019 101.604 1.00 38.91 ? 200 GLY A CA 1 ATOM 1509 C C . GLY A 1 200 ? -44.299 22.993 100.167 1.00 39.21 ? 200 GLY A C 1 ATOM 1510 O O . GLY A 1 200 ? -44.092 21.922 99.582 1.00 39.50 ? 200 GLY A O 1 ATOM 1511 N N . ARG A 1 201 ? -44.059 24.174 99.617 1.00 37.49 ? 201 ARG A N 1 ATOM 1512 C CA . ARG A 1 201 ? -43.735 24.302 98.202 1.00 36.43 ? 201 ARG A CA 1 ATOM 1513 C C . ARG A 1 201 ? -42.415 23.621 97.840 1.00 34.57 ? 201 ARG A C 1 ATOM 1514 O O . ARG A 1 201 ? -41.576 23.357 98.712 1.00 34.11 ? 201 ARG A O 1 ATOM 1515 C CB . ARG A 1 201 ? -43.706 25.780 97.816 1.00 37.48 ? 201 ARG A CB 1 ATOM 1516 C CG . ARG A 1 201 ? -42.554 26.556 98.420 1.00 38.15 ? 201 ARG A CG 1 ATOM 1517 C CD . ARG A 1 201 ? -42.883 28.034 98.569 1.00 38.90 ? 201 ARG A CD 1 ATOM 1518 N NE . ARG A 1 201 ? -41.747 28.728 99.175 1.00 39.56 ? 201 ARG A NE 1 ATOM 1519 C CZ . ARG A 1 201 ? -41.562 28.894 100.483 1.00 40.63 ? 201 ARG A CZ 1 ATOM 1520 N NH1 . ARG A 1 201 ? -42.454 28.441 101.365 1.00 41.16 ? 201 ARG A NH1 1 ATOM 1521 N NH2 . ARG A 1 201 ? -40.477 29.532 100.914 1.00 41.00 ? 201 ARG A NH2 1 ATOM 1522 N N . ILE A 1 202 ? -42.269 23.309 96.550 1.00 31.38 ? 202 ILE A N 1 ATOM 1523 C CA . ILE A 1 202 ? -41.016 22.820 95.979 1.00 30.91 ? 202 ILE A CA 1 ATOM 1524 C C . ILE A 1 202 ? -40.530 23.859 94.970 1.00 29.27 ? 202 ILE A C 1 ATOM 1525 O O . ILE A 1 202 ? -41.313 24.320 94.134 1.00 29.28 ? 202 ILE A O 1 ATOM 1526 C CB . ILE A 1 202 ? -41.216 21.466 95.263 1.00 30.61 ? 202 ILE A CB 1 ATOM 1527 C CG1 . ILE A 1 202 ? -41.537 20.371 96.284 1.00 32.20 ? 202 ILE A CG1 1 ATOM 1528 C CG2 . ILE A 1 202 ? -39.985 21.097 94.446 1.00 30.84 ? 202 ILE A CG2 1 ATOM 1529 C CD1 . ILE A 1 202 ? -42.061 19.087 95.673 1.00 32.02 ? 202 ILE A CD1 1 ATOM 1530 N N . THR A 1 203 ? -39.260 24.236 95.054 1.00 28.59 ? 203 THR A N 1 ATOM 1531 C CA . THR A 1 203 ? -38.678 25.165 94.087 1.00 28.66 ? 203 THR A CA 1 ATOM 1532 C C . THR A 1 203 ? -37.462 24.542 93.397 1.00 28.57 ? 203 THR A C 1 ATOM 1533 O O . THR A 1 203 ? -36.489 24.126 94.050 1.00 29.13 ? 203 THR A O 1 ATOM 1534 C CB . THR A 1 203 ? -38.331 26.531 94.725 1.00 29.65 ? 203 THR A CB 1 ATOM 1535 O OG1 . THR A 1 203 ? -39.529 27.133 95.227 1.00 28.82 ? 203 THR A OG1 1 ATOM 1536 C CG2 . THR A 1 203 ? -37.687 27.484 93.680 1.00 29.45 ? 203 THR A CG2 1 ATOM 1537 N N . VAL A 1 204 ? -37.539 24.460 92.066 1.00 26.93 ? 204 VAL A N 1 ATOM 1538 C CA . VAL A 1 204 ? -36.443 23.961 91.253 1.00 26.41 ? 204 VAL A CA 1 ATOM 1539 C C . VAL A 1 204 ? -35.990 25.107 90.365 1.00 26.43 ? 204 VAL A C 1 ATOM 1540 O O . VAL A 1 204 ? -36.794 25.692 89.638 1.00 25.90 ? 204 VAL A O 1 ATOM 1541 C CB . VAL A 1 204 ? -36.869 22.749 90.407 1.00 25.75 ? 204 VAL A CB 1 ATOM 1542 C CG1 . VAL A 1 204 ? -35.736 22.298 89.497 1.00 25.06 ? 204 VAL A CG1 1 ATOM 1543 C CG2 . VAL A 1 204 ? -37.341 21.621 91.317 1.00 25.27 ? 204 VAL A CG2 1 ATOM 1544 N N . SER A 1 205 ? -34.708 25.446 90.447 1.00 27.26 ? 205 SER A N 1 ATOM 1545 C CA . SER A 1 205 ? -34.220 26.656 89.799 1.00 27.70 ? 205 SER A CA 1 ATOM 1546 C C . SER A 1 205 ? -32.870 26.470 89.153 1.00 28.20 ? 205 SER A C 1 ATOM 1547 O O . SER A 1 205 ? -32.144 25.516 89.440 1.00 28.37 ? 205 SER A O 1 ATOM 1548 C CB . SER A 1 205 ? -34.157 27.801 90.811 1.00 28.23 ? 205 SER A CB 1 ATOM 1549 O OG . SER A 1 205 ? -33.276 27.477 91.882 1.00 29.07 ? 205 SER A OG 1 ATOM 1550 N N . THR A 1 206 ? -32.563 27.405 88.263 1.00 27.92 ? 206 THR A N 1 ATOM 1551 C CA . THR A 1 206 ? -31.257 27.546 87.651 1.00 28.61 ? 206 THR A CA 1 ATOM 1552 C C . THR A 1 206 ? -30.930 29.039 87.672 1.00 28.64 ? 206 THR A C 1 ATOM 1553 O O . THR A 1 206 ? -31.698 29.844 88.188 1.00 28.08 ? 206 THR A O 1 ATOM 1554 C CB . THR A 1 206 ? -31.269 27.044 86.193 1.00 28.43 ? 206 THR A CB 1 ATOM 1555 O OG1 . THR A 1 206 ? -32.078 27.916 85.388 1.00 29.47 ? 206 THR A OG1 1 ATOM 1556 C CG2 . THR A 1 206 ? -31.808 25.607 86.104 1.00 27.59 ? 206 THR A CG2 1 ATOM 1557 N N . LYS A 1 207 ? -29.809 29.417 87.086 1.00 29.71 ? 207 LYS A N 1 ATOM 1558 C CA . LYS A 1 207 ? -29.495 30.832 86.918 1.00 31.68 ? 207 LYS A CA 1 ATOM 1559 C C . LYS A 1 207 ? -30.499 31.559 86.032 1.00 32.86 ? 207 LYS A C 1 ATOM 1560 O O . LYS A 1 207 ? -30.712 32.759 86.195 1.00 33.90 ? 207 LYS A O 1 ATOM 1561 C CB . LYS A 1 207 ? -28.112 30.989 86.315 1.00 33.05 ? 207 LYS A CB 1 ATOM 1562 C CG . LYS A 1 207 ? -27.005 30.542 87.250 1.00 34.59 ? 207 LYS A CG 1 ATOM 1563 C CD . LYS A 1 207 ? -25.647 30.861 86.651 1.00 36.65 ? 207 LYS A CD 1 ATOM 1564 C CE . LYS A 1 207 ? -24.643 29.768 86.936 1.00 38.23 ? 207 LYS A CE 1 ATOM 1565 N NZ . LYS A 1 207 ? -23.406 29.986 86.143 1.00 40.05 ? 207 LYS A NZ 1 ATOM 1566 N N . ARG A 1 208 ? -31.120 30.839 85.100 1.00 33.99 ? 208 ARG A N 1 ATOM 1567 C CA . ARG A 1 208 ? -32.006 31.471 84.133 1.00 35.54 ? 208 ARG A CA 1 ATOM 1568 C C . ARG A 1 208 ? -33.491 31.168 84.316 1.00 34.88 ? 208 ARG A C 1 ATOM 1569 O O . ARG A 1 208 ? -34.311 31.735 83.593 1.00 35.86 ? 208 ARG A O 1 ATOM 1570 C CB . ARG A 1 208 ? -31.574 31.091 82.715 1.00 38.71 ? 208 ARG A CB 1 ATOM 1571 C CG . ARG A 1 208 ? -31.838 29.634 82.348 1.00 41.04 ? 208 ARG A CG 1 ATOM 1572 C CD . ARG A 1 208 ? -31.731 29.394 80.842 1.00 45.66 ? 208 ARG A CD 1 ATOM 1573 N NE . ARG A 1 208 ? -32.611 30.286 80.077 1.00 49.50 ? 208 ARG A NE 1 ATOM 1574 C CZ . ARG A 1 208 ? -33.933 30.143 79.943 1.00 50.75 ? 208 ARG A CZ 1 ATOM 1575 N NH1 . ARG A 1 208 ? -34.584 29.130 80.514 1.00 51.13 ? 208 ARG A NH1 1 ATOM 1576 N NH2 . ARG A 1 208 ? -34.617 31.032 79.229 1.00 52.69 ? 208 ARG A NH2 1 ATOM 1577 N N . SER A 1 209 ? -33.855 30.288 85.250 1.00 32.07 ? 209 SER A N 1 ATOM 1578 C CA . SER A 1 209 ? -35.256 29.871 85.376 1.00 31.60 ? 209 SER A CA 1 ATOM 1579 C C . SER A 1 209 ? -35.619 29.436 86.784 1.00 30.54 ? 209 SER A C 1 ATOM 1580 O O . SER A 1 209 ? -34.758 29.057 87.573 1.00 29.39 ? 209 SER A O 1 ATOM 1581 C CB . SER A 1 209 ? -35.549 28.712 84.400 1.00 31.56 ? 209 SER A CB 1 ATOM 1582 O OG . SER A 1 209 ? -34.799 27.559 84.763 1.00 32.93 ? 209 SER A OG 1 ATOM 1583 N N . GLN A 1 210 ? -36.907 29.471 87.092 1.00 29.56 ? 210 GLN A N 1 ATOM 1584 C CA . GLN A 1 210 ? -37.399 28.978 88.366 1.00 29.87 ? 210 GLN A CA 1 ATOM 1585 C C . GLN A 1 210 ? -38.802 28.448 88.206 1.00 29.67 ? 210 GLN A C 1 ATOM 1586 O O . GLN A 1 210 ? -39.605 29.033 87.479 1.00 29.67 ? 210 GLN A O 1 ATOM 1587 C CB . GLN A 1 210 ? -37.377 30.079 89.436 1.00 31.18 ? 210 GLN A CB 1 ATOM 1588 C CG . GLN A 1 210 ? -38.048 31.392 89.046 1.00 32.03 ? 210 GLN A CG 1 ATOM 1589 C CD . GLN A 1 210 ? -38.036 32.418 90.174 1.00 34.53 ? 210 GLN A CD 1 ATOM 1590 O OE1 . GLN A 1 210 ? -37.618 32.111 91.277 1.00 38.21 ? 210 GLN A OE1 1 ATOM 1591 N NE2 . GLN A 1 210 ? -38.513 33.633 89.902 1.00 33.85 ? 210 GLN A NE2 1 ATOM 1592 N N . GLN A 1 211 ? -39.083 27.334 88.876 1.00 28.92 ? 211 GLN A N 1 ATOM 1593 C CA . GLN A 1 211 ? -40.401 26.750 88.903 1.00 28.10 ? 211 GLN A CA 1 ATOM 1594 C C . GLN A 1 211 ? -40.728 26.412 90.348 1.00 27.77 ? 211 GLN A C 1 ATOM 1595 O O . GLN A 1 211 ? -40.010 25.645 90.991 1.00 27.22 ? 211 GLN A O 1 ATOM 1596 C CB . GLN A 1 211 ? -40.456 25.465 88.055 1.00 29.88 ? 211 GLN A CB 1 ATOM 1597 C CG . GLN A 1 211 ? -40.029 25.613 86.595 1.00 30.47 ? 211 GLN A CG 1 ATOM 1598 C CD . GLN A 1 211 ? -39.464 24.317 86.004 1.00 31.63 ? 211 GLN A CD 1 ATOM 1599 O OE1 . GLN A 1 211 ? -38.243 24.066 86.044 1.00 33.66 ? 211 GLN A OE1 1 ATOM 1600 N NE2 . GLN A 1 211 ? -40.334 23.496 85.478 1.00 31.16 ? 211 GLN A NE2 1 ATOM 1601 N N . THR A 1 212 ? -41.821 26.969 90.854 1.00 27.36 ? 212 THR A N 1 ATOM 1602 C CA . THR A 1 212 ? -42.297 26.631 92.197 1.00 26.50 ? 212 THR A CA 1 ATOM 1603 C C . THR A 1 212 ? -43.648 25.921 92.084 1.00 26.91 ? 212 THR A C 1 ATOM 1604 O O . THR A 1 212 ? -44.547 26.377 91.361 1.00 27.15 ? 212 THR A O 1 ATOM 1605 C CB . THR A 1 212 ? -42.393 27.884 93.094 1.00 26.15 ? 212 THR A CB 1 ATOM 1606 O OG1 . THR A 1 212 ? -41.086 28.427 93.296 1.00 25.70 ? 212 THR A OG1 1 ATOM 1607 C CG2 . THR A 1 212 ? -42.999 27.532 94.446 1.00 26.26 ? 212 THR A CG2 1 ATOM 1608 N N . VAL A 1 213 ? -43.775 24.783 92.765 1.00 26.89 ? 213 VAL A N 1 ATOM 1609 C CA . VAL A 1 213 ? -44.983 23.971 92.708 1.00 27.22 ? 213 VAL A CA 1 ATOM 1610 C C . VAL A 1 213 ? -45.464 23.640 94.121 1.00 27.95 ? 213 VAL A C 1 ATOM 1611 O O . VAL A 1 213 ? -44.663 23.302 94.988 1.00 27.52 ? 213 VAL A O 1 ATOM 1612 C CB . VAL A 1 213 ? -44.764 22.659 91.924 1.00 27.58 ? 213 VAL A CB 1 ATOM 1613 C CG1 . VAL A 1 213 ? -46.061 21.877 91.852 1.00 28.18 ? 213 VAL A CG1 1 ATOM 1614 C CG2 . VAL A 1 213 ? -44.251 22.938 90.511 1.00 27.93 ? 213 VAL A CG2 1 ATOM 1615 N N . ILE A 1 214 ? -46.778 23.739 94.332 1.00 29.34 ? 214 ILE A N 1 ATOM 1616 C CA . ILE A 1 214 ? -47.405 23.515 95.642 1.00 30.55 ? 214 ILE A CA 1 ATOM 1617 C C . ILE A 1 214 ? -48.046 22.131 95.660 1.00 30.34 ? 214 ILE A C 1 ATOM 1618 O O . ILE A 1 214 ? -48.977 21.885 94.904 1.00 30.00 ? 214 ILE A O 1 ATOM 1619 C CB . ILE A 1 214 ? -48.531 24.547 95.923 1.00 31.68 ? 214 ILE A CB 1 ATOM 1620 C CG1 . ILE A 1 214 ? -48.019 25.982 95.766 1.00 32.85 ? 214 ILE A CG1 1 ATOM 1621 C CG2 . ILE A 1 214 ? -49.124 24.366 97.323 1.00 31.88 ? 214 ILE A CG2 1 ATOM 1622 C CD1 . ILE A 1 214 ? -46.872 26.314 96.687 1.00 36.10 ? 214 ILE A CD1 1 ATOM 1623 N N . PRO A 1 215 ? -47.565 21.229 96.531 1.00 30.61 ? 215 PRO A N 1 ATOM 1624 C CA . PRO A 1 215 ? -48.288 19.968 96.708 1.00 30.44 ? 215 PRO A CA 1 ATOM 1625 C C . PRO A 1 215 ? -49.661 20.242 97.314 1.00 30.90 ? 215 PRO A C 1 ATOM 1626 O O . PRO A 1 215 ? -49.766 21.065 98.223 1.00 30.93 ? 215 PRO A O 1 ATOM 1627 C CB . PRO A 1 215 ? -47.408 19.172 97.679 1.00 32.10 ? 215 PRO A CB 1 ATOM 1628 C CG . PRO A 1 215 ? -46.096 19.888 97.719 1.00 31.95 ? 215 PRO A CG 1 ATOM 1629 C CD . PRO A 1 215 ? -46.383 21.321 97.399 1.00 31.31 ? 215 PRO A CD 1 ATOM 1630 N N . ASN A 1 216 ? -50.690 19.582 96.791 1.00 30.13 ? 216 ASN A N 1 ATOM 1631 C CA . ASN A 1 216 ? -52.064 19.764 97.238 1.00 30.10 ? 216 ASN A CA 1 ATOM 1632 C C . ASN A 1 216 ? -52.662 18.442 97.688 1.00 29.78 ? 216 ASN A C 1 ATOM 1633 O O . ASN A 1 216 ? -52.959 17.569 96.872 1.00 29.37 ? 216 ASN A O 1 ATOM 1634 C CB . ASN A 1 216 ? -52.913 20.364 96.122 1.00 30.38 ? 216 ASN A CB 1 ATOM 1635 C CG . ASN A 1 216 ? -52.444 21.739 95.708 1.00 31.17 ? 216 ASN A CG 1 ATOM 1636 O OD1 . ASN A 1 216 ? -52.294 22.619 96.550 1.00 32.30 ? 216 ASN A OD1 1 ATOM 1637 N ND2 . ASN A 1 216 ? -52.230 21.943 94.401 1.00 30.51 ? 216 ASN A ND2 1 ATOM 1638 N N . ILE A 1 217 ? -52.854 18.312 98.998 1.00 30.48 ? 217 ILE A N 1 ATOM 1639 C CA . ILE A 1 217 ? -53.389 17.094 99.601 1.00 30.64 ? 217 ILE A CA 1 ATOM 1640 C C . ILE A 1 217 ? -54.872 16.974 99.301 1.00 31.00 ? 217 ILE A C 1 ATOM 1641 O O . ILE A 1 217 ? -55.597 17.976 99.311 1.00 31.19 ? 217 ILE A O 1 ATOM 1642 C CB . ILE A 1 217 ? -53.148 17.094 101.134 1.00 31.95 ? 217 ILE A CB 1 ATOM 1643 C CG1 . ILE A 1 217 ? -51.637 17.004 101.411 1.00 31.78 ? 217 ILE A CG1 1 ATOM 1644 C CG2 . ILE A 1 217 ? -53.895 15.946 101.811 1.00 31.23 ? 217 ILE A CG2 1 ATOM 1645 C CD1 . ILE A 1 217 ? -51.212 17.593 102.738 1.00 34.25 ? 217 ILE A CD1 1 ATOM 1646 N N . GLY A 1 218 ? -55.322 15.754 99.019 1.00 31.25 ? 218 GLY A N 1 ATOM 1647 C CA . GLY A 1 218 ? -56.740 15.505 98.750 1.00 31.79 ? 218 GLY A CA 1 ATOM 1648 C C . GLY A 1 218 ? -56.947 14.236 97.950 1.00 32.07 ? 218 GLY A C 1 ATOM 1649 O O . GLY A 1 218 ? -56.070 13.809 97.193 1.00 30.87 ? 218 GLY A O 1 ATOM 1650 N N . SER A 1 219 ? -58.110 13.625 98.126 1.00 32.38 ? 219 SER A N 1 ATOM 1651 C CA . SER A 1 219 ? -58.473 12.461 97.351 1.00 33.63 ? 219 SER A CA 1 ATOM 1652 C C . SER A 1 219 ? -58.881 12.892 95.950 1.00 32.91 ? 219 SER A C 1 ATOM 1653 O O . SER A 1 219 ? -59.654 13.831 95.788 1.00 34.24 ? 219 SER A O 1 ATOM 1654 C CB . SER A 1 219 ? -59.638 11.723 97.998 1.00 35.15 ? 219 SER A CB 1 ATOM 1655 O OG . SER A 1 219 ? -59.340 11.401 99.334 1.00 38.74 ? 219 SER A OG 1 ATOM 1656 N N . ARG A 1 220 ? -58.319 12.217 94.955 1.00 30.75 ? 220 ARG A N 1 ATOM 1657 C CA . ARG A 1 220 ? -58.831 12.240 93.587 1.00 30.69 ? 220 ARG A CA 1 ATOM 1658 C C . ARG A 1 220 ? -59.511 10.896 93.370 1.00 30.52 ? 220 ARG A C 1 ATOM 1659 O O . ARG A 1 220 ? -59.314 9.963 94.180 1.00 30.63 ? 220 ARG A O 1 ATOM 1660 C CB . ARG A 1 220 ? -57.699 12.423 92.578 1.00 30.20 ? 220 ARG A CB 1 ATOM 1661 C CG . ARG A 1 220 ? -57.124 13.828 92.505 1.00 30.16 ? 220 ARG A CG 1 ATOM 1662 C CD . ARG A 1 220 ? -56.218 14.160 93.673 1.00 31.30 ? 220 ARG A CD 1 ATOM 1663 N NE . ARG A 1 220 ? -55.410 15.359 93.423 1.00 31.00 ? 220 ARG A NE 1 ATOM 1664 C CZ . ARG A 1 220 ? -54.715 16.017 94.355 1.00 31.74 ? 220 ARG A CZ 1 ATOM 1665 N NH1 . ARG A 1 220 ? -54.710 15.614 95.627 1.00 30.97 ? 220 ARG A NH1 1 ATOM 1666 N NH2 . ARG A 1 220 ? -54.009 17.089 94.010 1.00 31.96 ? 220 ARG A NH2 1 ATOM 1667 N N . PRO A 1 221 ? -60.326 10.778 92.313 1.00 30.26 ? 221 PRO A N 1 ATOM 1668 C CA . PRO A 1 221 ? -60.906 9.465 92.042 1.00 31.21 ? 221 PRO A CA 1 ATOM 1669 C C . PRO A 1 221 ? -59.821 8.398 91.867 1.00 31.73 ? 221 PRO A C 1 ATOM 1670 O O . PRO A 1 221 ? -58.796 8.629 91.219 1.00 31.89 ? 221 PRO A O 1 ATOM 1671 C CB . PRO A 1 221 ? -61.718 9.707 90.763 1.00 31.06 ? 221 PRO A CB 1 ATOM 1672 C CG . PRO A 1 221 ? -62.147 11.136 90.908 1.00 30.80 ? 221 PRO A CG 1 ATOM 1673 C CD . PRO A 1 221 ? -60.885 11.800 91.409 1.00 30.61 ? 221 PRO A CD 1 ATOM 1674 N N . ARG A 1 222 ? -60.014 7.245 92.490 1.00 31.45 ? 222 ARG A N 1 ATOM 1675 C CA . ARG A 1 222 ? -58.964 6.254 92.483 1.00 32.71 ? 222 ARG A CA 1 ATOM 1676 C C . ARG A 1 222 ? -58.677 5.773 91.082 1.00 31.90 ? 222 ARG A C 1 ATOM 1677 O O . ARG A 1 222 ? -59.588 5.572 90.290 1.00 31.26 ? 222 ARG A O 1 ATOM 1678 C CB . ARG A 1 222 ? -59.313 5.086 93.391 1.00 33.79 ? 222 ARG A CB 1 ATOM 1679 C CG . ARG A 1 222 ? -59.327 5.500 94.841 1.00 35.63 ? 222 ARG A CG 1 ATOM 1680 C CD . ARG A 1 222 ? -59.506 4.286 95.710 1.00 37.69 ? 222 ARG A CD 1 ATOM 1681 N NE . ARG A 1 222 ? -59.455 4.624 97.123 1.00 39.04 ? 222 ARG A NE 1 ATOM 1682 C CZ . ARG A 1 222 ? -59.250 3.736 98.089 1.00 41.23 ? 222 ARG A CZ 1 ATOM 1683 N NH1 . ARG A 1 222 ? -59.059 2.456 97.788 1.00 41.79 ? 222 ARG A NH1 1 ATOM 1684 N NH2 . ARG A 1 222 ? -59.223 4.133 99.356 1.00 42.46 ? 222 ARG A NH2 1 ATOM 1685 N N . VAL A 1 223 ? -57.385 5.656 90.783 1.00 32.34 ? 223 VAL A N 1 ATOM 1686 C CA . VAL A 1 223 ? -56.894 5.109 89.527 1.00 32.57 ? 223 VAL A CA 1 ATOM 1687 C C . VAL A 1 223 ? -55.993 3.959 89.948 1.00 33.98 ? 223 VAL A C 1 ATOM 1688 O O . VAL A 1 223 ? -55.043 4.151 90.715 1.00 32.26 ? 223 VAL A O 1 ATOM 1689 C CB . VAL A 1 223 ? -56.079 6.142 88.721 1.00 32.58 ? 223 VAL A CB 1 ATOM 1690 C CG1 . VAL A 1 223 ? -55.323 5.475 87.564 1.00 32.40 ? 223 VAL A CG1 1 ATOM 1691 C CG2 . VAL A 1 223 ? -56.972 7.265 88.200 1.00 32.48 ? 223 VAL A CG2 1 ATOM 1692 N N . ARG A 1 224 ? -56.296 2.764 89.454 1.00 36.30 ? 224 ARG A N 1 ATOM 1693 C CA . ARG A 1 224 ? -55.594 1.563 89.887 1.00 36.91 ? 224 ARG A CA 1 ATOM 1694 C C . ARG A 1 224 ? -55.486 1.586 91.421 1.00 36.12 ? 224 ARG A C 1 ATOM 1695 O O . ARG A 1 224 ? -54.431 1.336 91.997 1.00 38.90 ? 224 ARG A O 1 ATOM 1696 C CB . ARG A 1 224 ? -54.237 1.463 89.173 1.00 37.20 ? 224 ARG A CB 1 ATOM 1697 C CG . ARG A 1 224 ? -54.385 1.406 87.650 1.00 37.28 ? 224 ARG A CG 1 ATOM 1698 C CD . ARG A 1 224 ? -53.060 1.286 86.900 1.00 36.94 ? 224 ARG A CD 1 ATOM 1699 N NE . ARG A 1 224 ? -52.215 2.468 87.061 1.00 35.84 ? 224 ARG A NE 1 ATOM 1700 C CZ . ARG A 1 224 ? -52.336 3.600 86.364 1.00 35.39 ? 224 ARG A CZ 1 ATOM 1701 N NH1 . ARG A 1 224 ? -53.277 3.736 85.436 1.00 36.38 ? 224 ARG A NH1 1 ATOM 1702 N NH2 . ARG A 1 224 ? -51.513 4.609 86.598 1.00 35.40 ? 224 ARG A NH2 1 ATOM 1703 N N . ASN A 1 225 ? -56.608 1.936 92.053 1.00 36.58 ? 225 ASN A N 1 ATOM 1704 C CA . ASN A 1 225 ? -56.785 1.975 93.516 1.00 37.56 ? 225 ASN A CA 1 ATOM 1705 C C . ASN A 1 225 ? -55.999 3.054 94.285 1.00 36.16 ? 225 ASN A C 1 ATOM 1706 O O . ASN A 1 225 ? -55.889 2.992 95.518 1.00 36.52 ? 225 ASN A O 1 ATOM 1707 C CB . ASN A 1 225 ? -56.539 0.576 94.127 1.00 39.65 ? 225 ASN A CB 1 ATOM 1708 C CG . ASN A 1 225 ? -57.369 0.331 95.394 1.00 42.52 ? 225 ASN A CG 1 ATOM 1709 O OD1 . ASN A 1 225 ? -58.517 0.773 95.496 1.00 42.82 ? 225 ASN A OD1 1 ATOM 1710 N ND2 . ASN A 1 225 ? -56.785 -0.376 96.367 1.00 44.20 ? 225 ASN A ND2 1 ATOM 1711 N N . ILE A 1 226 ? -55.492 4.068 93.578 1.00 32.28 ? 226 ILE A N 1 ATOM 1712 C CA . ILE A 1 226 ? -54.710 5.130 94.195 1.00 30.34 ? 226 ILE A CA 1 ATOM 1713 C C . ILE A 1 226 ? -55.420 6.477 94.050 1.00 30.12 ? 226 ILE A C 1 ATOM 1714 O O . ILE A 1 226 ? -55.642 6.946 92.909 1.00 28.64 ? 226 ILE A O 1 ATOM 1715 C CB . ILE A 1 226 ? -53.307 5.252 93.555 1.00 30.51 ? 226 ILE A CB 1 ATOM 1716 C CG1 . ILE A 1 226 ? -52.518 3.947 93.703 1.00 31.35 ? 226 ILE A CG1 1 ATOM 1717 C CG2 . ILE A 1 226 ? -52.535 6.415 94.159 1.00 29.42 ? 226 ILE A CG2 1 ATOM 1718 C CD1 . ILE A 1 226 ? -52.236 3.552 95.143 1.00 31.90 ? 226 ILE A CD1 1 ATOM 1719 N N . PRO A 1 227 ? -55.769 7.105 95.185 1.00 30.10 ? 227 PRO A N 1 ATOM 1720 C CA . PRO A 1 227 ? -56.398 8.425 95.186 1.00 30.29 ? 227 PRO A CA 1 ATOM 1721 C C . PRO A 1 227 ? -55.405 9.593 95.172 1.00 29.74 ? 227 PRO A C 1 ATOM 1722 O O . PRO A 1 227 ? -55.816 10.742 95.002 1.00 30.10 ? 227 PRO A O 1 ATOM 1723 C CB . PRO A 1 227 ? -57.199 8.418 96.494 1.00 31.61 ? 227 PRO A CB 1 ATOM 1724 C CG . PRO A 1 227 ? -56.379 7.585 97.415 1.00 31.61 ? 227 PRO A CG 1 ATOM 1725 C CD . PRO A 1 227 ? -55.782 6.502 96.544 1.00 31.84 ? 227 PRO A CD 1 ATOM 1726 N N . SER A 1 228 ? -54.118 9.308 95.351 1.00 29.85 ? 228 SER A N 1 ATOM 1727 C CA . SER A 1 228 ? -53.069 10.329 95.259 1.00 29.39 ? 228 SER A CA 1 ATOM 1728 C C . SER A 1 228 ? -52.703 10.563 93.789 1.00 27.84 ? 228 SER A C 1 ATOM 1729 O O . SER A 1 228 ? -53.162 9.844 92.910 1.00 26.41 ? 228 SER A O 1 ATOM 1730 C CB . SER A 1 228 ? -51.810 9.877 96.002 1.00 31.21 ? 228 SER A CB 1 ATOM 1731 O OG . SER A 1 228 ? -52.081 9.526 97.343 1.00 33.36 ? 228 SER A OG 1 ATOM 1732 N N . ARG A 1 229 ? -51.849 11.557 93.544 1.00 27.05 ? 229 ARG A N 1 ATOM 1733 C CA . ARG A 1 229 ? -51.323 11.829 92.214 1.00 26.21 ? 229 ARG A CA 1 ATOM 1734 C C . ARG A 1 229 ? -49.873 12.308 92.292 1.00 25.73 ? 229 ARG A C 1 ATOM 1735 O O . ARG A 1 229 ? -49.442 12.860 93.304 1.00 26.90 ? 229 ARG A O 1 ATOM 1736 C CB . ARG A 1 229 ? -52.161 12.918 91.520 1.00 26.38 ? 229 ARG A CB 1 ATOM 1737 C CG . ARG A 1 229 ? -53.621 12.560 91.256 1.00 27.10 ? 229 ARG A CG 1 ATOM 1738 C CD . ARG A 1 229 ? -53.770 11.510 90.162 1.00 28.03 ? 229 ARG A CD 1 ATOM 1739 N NE . ARG A 1 229 ? -55.176 11.323 89.777 1.00 28.37 ? 229 ARG A NE 1 ATOM 1740 C CZ . ARG A 1 229 ? -55.994 10.384 90.252 1.00 29.09 ? 229 ARG A CZ 1 ATOM 1741 N NH1 . ARG A 1 229 ? -55.590 9.503 91.186 1.00 29.26 ? 229 ARG A NH1 1 ATOM 1742 N NH2 . ARG A 1 229 ? -57.242 10.343 89.820 1.00 28.09 ? 229 ARG A NH2 1 ATOM 1743 N N . ILE A 1 230 ? -49.131 12.090 91.213 1.00 25.28 ? 230 ILE A N 1 ATOM 1744 C CA . ILE A 1 230 ? -47.855 12.775 90.981 1.00 24.75 ? 230 ILE A CA 1 ATOM 1745 C C . ILE A 1 230 ? -48.018 13.708 89.763 1.00 24.46 ? 230 ILE A C 1 ATOM 1746 O O . ILE A 1 230 ? -48.544 13.294 88.736 1.00 23.46 ? 230 ILE A O 1 ATOM 1747 C CB . ILE A 1 230 ? -46.720 11.767 90.718 1.00 25.04 ? 230 ILE A CB 1 ATOM 1748 C CG1 . ILE A 1 230 ? -46.444 10.962 92.000 1.00 25.97 ? 230 ILE A CG1 1 ATOM 1749 C CG2 . ILE A 1 230 ? -45.461 12.491 90.253 1.00 25.33 ? 230 ILE A CG2 1 ATOM 1750 C CD1 . ILE A 1 230 ? -45.604 9.720 91.793 1.00 26.71 ? 230 ILE A CD1 1 ATOM 1751 N N . SER A 1 231 ? -47.582 14.954 89.906 1.00 24.33 ? 231 SER A N 1 ATOM 1752 C CA . SER A 1 231 ? -47.540 15.896 88.795 1.00 23.79 ? 231 SER A CA 1 ATOM 1753 C C . SER A 1 231 ? -46.088 16.041 88.325 1.00 22.89 ? 231 SER A C 1 ATOM 1754 O O . SER A 1 231 ? -45.171 16.236 89.137 1.00 22.50 ? 231 SER A O 1 ATOM 1755 C CB . SER A 1 231 ? -48.149 17.238 89.219 1.00 24.24 ? 231 SER A CB 1 ATOM 1756 O OG . SER A 1 231 ? -49.560 17.116 89.384 1.00 25.31 ? 231 SER A OG 1 ATOM 1757 N N . ILE A 1 232 ? -45.886 15.914 87.019 1.00 22.50 ? 232 ILE A N 1 ATOM 1758 C CA . ILE A 1 232 ? -44.547 15.855 86.427 1.00 22.18 ? 232 ILE A CA 1 ATOM 1759 C C . ILE A 1 232 ? -44.136 17.190 85.802 1.00 23.11 ? 232 ILE A C 1 ATOM 1760 O O . ILE A 1 232 ? -44.927 17.815 85.074 1.00 22.37 ? 232 ILE A O 1 ATOM 1761 C CB . ILE A 1 232 ? -44.493 14.776 85.335 1.00 21.86 ? 232 ILE A CB 1 ATOM 1762 C CG1 . ILE A 1 232 ? -44.761 13.393 85.928 1.00 22.09 ? 232 ILE A CG1 1 ATOM 1763 C CG2 . ILE A 1 232 ? -43.156 14.787 84.587 1.00 21.48 ? 232 ILE A CG2 1 ATOM 1764 C CD1 . ILE A 1 232 ? -43.735 12.945 86.965 1.00 23.56 ? 232 ILE A CD1 1 ATOM 1765 N N . TYR A 1 233 ? -42.890 17.588 86.064 1.00 22.08 ? 233 TYR A N 1 ATOM 1766 C CA . TYR A 1 233 ? -42.310 18.830 85.570 1.00 22.83 ? 233 TYR A CA 1 ATOM 1767 C C . TYR A 1 233 ? -40.967 18.547 84.928 1.00 22.48 ? 233 TYR A C 1 ATOM 1768 O O . TYR A 1 233 ? -40.388 17.470 85.135 1.00 22.34 ? 233 TYR A O 1 ATOM 1769 C CB . TYR A 1 233 ? -42.171 19.838 86.708 1.00 23.29 ? 233 TYR A CB 1 ATOM 1770 C CG . TYR A 1 233 ? -43.520 20.194 87.273 1.00 24.03 ? 233 TYR A CG 1 ATOM 1771 C CD1 . TYR A 1 233 ? -44.105 19.426 88.275 1.00 24.16 ? 233 TYR A CD1 1 ATOM 1772 C CD2 . TYR A 1 233 ? -44.246 21.267 86.762 1.00 24.74 ? 233 TYR A CD2 1 ATOM 1773 C CE1 . TYR A 1 233 ? -45.366 19.716 88.751 1.00 24.20 ? 233 TYR A CE1 1 ATOM 1774 C CE2 . TYR A 1 233 ? -45.509 21.554 87.229 1.00 24.69 ? 233 TYR A CE2 1 ATOM 1775 C CZ . TYR A 1 233 ? -46.055 20.791 88.233 1.00 25.42 ? 233 TYR A CZ 1 ATOM 1776 O OH . TYR A 1 233 ? -47.312 21.105 88.697 1.00 26.80 ? 233 TYR A OH 1 ATOM 1777 N N . TRP A 1 234 ? -40.465 19.502 84.145 1.00 22.20 ? 234 TRP A N 1 ATOM 1778 C CA . TRP A 1 234 ? -39.154 19.348 83.533 1.00 22.53 ? 234 TRP A CA 1 ATOM 1779 C C . TRP A 1 234 ? -38.386 20.634 83.520 1.00 22.54 ? 234 TRP A C 1 ATOM 1780 O O . TRP A 1 234 ? -38.958 21.730 83.543 1.00 23.24 ? 234 TRP A O 1 ATOM 1781 C CB . TRP A 1 234 ? -39.260 18.742 82.126 1.00 23.61 ? 234 TRP A CB 1 ATOM 1782 C CG . TRP A 1 234 ? -39.749 19.690 81.068 1.00 24.89 ? 234 TRP A CG 1 ATOM 1783 C CD1 . TRP A 1 234 ? -38.993 20.524 80.238 1.00 25.66 ? 234 TRP A CD1 1 ATOM 1784 C CD2 . TRP A 1 234 ? -41.124 19.927 80.690 1.00 26.19 ? 234 TRP A CD2 1 ATOM 1785 N NE1 . TRP A 1 234 ? -39.807 21.235 79.405 1.00 27.03 ? 234 TRP A NE1 1 ATOM 1786 C CE2 . TRP A 1 234 ? -41.092 20.926 79.625 1.00 26.22 ? 234 TRP A CE2 1 ATOM 1787 C CE3 . TRP A 1 234 ? -42.340 19.426 81.106 1.00 27.00 ? 234 TRP A CE3 1 ATOM 1788 C CZ2 . TRP A 1 234 ? -42.232 21.381 79.022 1.00 28.21 ? 234 TRP A CZ2 1 ATOM 1789 C CZ3 . TRP A 1 234 ? -43.501 19.895 80.484 1.00 28.56 ? 234 TRP A CZ3 1 ATOM 1790 C CH2 . TRP A 1 234 ? -43.443 20.852 79.465 1.00 28.58 ? 234 TRP A CH2 1 ATOM 1791 N N . THR A 1 235 ? -37.076 20.499 83.503 1.00 22.65 ? 235 THR A N 1 ATOM 1792 C CA . THR A 1 235 ? -36.156 21.630 83.521 1.00 23.14 ? 235 THR A CA 1 ATOM 1793 C C . THR A 1 235 ? -34.985 21.299 82.625 1.00 24.02 ? 235 THR A C 1 ATOM 1794 O O . THR A 1 235 ? -34.377 20.223 82.772 1.00 22.94 ? 235 THR A O 1 ATOM 1795 C CB . THR A 1 235 ? -35.616 21.887 84.945 1.00 23.66 ? 235 THR A CB 1 ATOM 1796 O OG1 . THR A 1 235 ? -36.704 21.986 85.883 1.00 22.85 ? 235 THR A OG1 1 ATOM 1797 C CG2 . THR A 1 235 ? -34.780 23.188 84.985 1.00 24.07 ? 235 THR A CG2 1 ATOM 1798 N N . ILE A 1 236 ? -34.636 22.212 81.718 1.00 24.12 ? 236 ILE A N 1 ATOM 1799 C CA . ILE A 1 236 ? -33.442 22.028 80.885 1.00 25.52 ? 236 ILE A CA 1 ATOM 1800 C C . ILE A 1 236 ? -32.309 22.887 81.450 1.00 25.91 ? 236 ILE A C 1 ATOM 1801 O O . ILE A 1 236 ? -32.505 24.074 81.686 1.00 27.96 ? 236 ILE A O 1 ATOM 1802 C CB . ILE A 1 236 ? -33.719 22.369 79.399 1.00 26.22 ? 236 ILE A CB 1 ATOM 1803 C CG1 . ILE A 1 236 ? -34.690 21.350 78.805 1.00 27.03 ? 236 ILE A CG1 1 ATOM 1804 C CG2 . ILE A 1 236 ? -32.424 22.361 78.598 1.00 26.29 ? 236 ILE A CG2 1 ATOM 1805 C CD1 . ILE A 1 236 ? -35.384 21.812 77.538 1.00 28.14 ? 236 ILE A CD1 1 ATOM 1806 N N . VAL A 1 237 ? -31.146 22.284 81.698 1.00 26.18 ? 237 VAL A N 1 ATOM 1807 C CA . VAL A 1 237 ? -30.005 22.982 82.287 1.00 26.76 ? 237 VAL A CA 1 ATOM 1808 C C . VAL A 1 237 ? -28.855 23.097 81.290 1.00 28.24 ? 237 VAL A C 1 ATOM 1809 O O . VAL A 1 237 ? -28.314 22.092 80.835 1.00 28.14 ? 237 VAL A O 1 ATOM 1810 C CB . VAL A 1 237 ? -29.516 22.268 83.564 1.00 26.61 ? 237 VAL A CB 1 ATOM 1811 C CG1 . VAL A 1 237 ? -28.327 23.004 84.194 1.00 26.73 ? 237 VAL A CG1 1 ATOM 1812 C CG2 . VAL A 1 237 ? -30.673 22.115 84.552 1.00 26.22 ? 237 VAL A CG2 1 ATOM 1813 N N . LYS A 1 238 ? -28.473 24.329 80.993 1.00 30.25 ? 238 LYS A N 1 ATOM 1814 C CA . LYS A 1 238 ? -27.419 24.635 80.017 1.00 31.80 ? 238 LYS A CA 1 ATOM 1815 C C . LYS A 1 238 ? -26.029 24.393 80.578 1.00 32.07 ? 238 LYS A C 1 ATOM 1816 O O . LYS A 1 238 ? -25.828 24.457 81.792 1.00 33.05 ? 238 LYS A O 1 ATOM 1817 C CB . LYS A 1 238 ? -27.489 26.109 79.611 1.00 33.93 ? 238 LYS A CB 1 ATOM 1818 C CG . LYS A 1 238 ? -28.843 26.604 79.133 1.00 35.66 ? 238 LYS A CG 1 ATOM 1819 C CD . LYS A 1 238 ? -29.312 25.904 77.880 1.00 35.89 ? 238 LYS A CD 1 ATOM 1820 C CE . LYS A 1 238 ? -28.557 26.373 76.650 1.00 37.89 ? 238 LYS A CE 1 ATOM 1821 N NZ . LYS A 1 238 ? -29.045 25.682 75.422 1.00 37.17 ? 238 LYS A NZ 1 ATOM 1822 N N . PRO A 1 239 ? -25.044 24.156 79.693 1.00 32.77 ? 239 PRO A N 1 ATOM 1823 C CA . PRO A 1 239 ? -23.650 24.138 80.128 1.00 33.59 ? 239 PRO A CA 1 ATOM 1824 C C . PRO A 1 239 ? -23.323 25.390 80.914 1.00 34.25 ? 239 PRO A C 1 ATOM 1825 O O . PRO A 1 239 ? -23.754 26.485 80.544 1.00 34.02 ? 239 PRO A O 1 ATOM 1826 C CB . PRO A 1 239 ? -22.873 24.115 78.800 1.00 34.60 ? 239 PRO A CB 1 ATOM 1827 C CG . PRO A 1 239 ? -23.793 23.429 77.856 1.00 33.81 ? 239 PRO A CG 1 ATOM 1828 C CD . PRO A 1 239 ? -25.161 23.918 78.243 1.00 33.30 ? 239 PRO A CD 1 ATOM 1829 N N . GLY A 1 240 ? -22.602 25.226 82.016 1.00 35.64 ? 240 GLY A N 1 ATOM 1830 C CA . GLY A 1 240 ? -22.235 26.351 82.859 1.00 36.66 ? 240 GLY A CA 1 ATOM 1831 C C . GLY A 1 240 ? -23.313 26.755 83.847 1.00 35.85 ? 240 GLY A C 1 ATOM 1832 O O . GLY A 1 240 ? -23.062 27.577 84.715 1.00 37.36 ? 240 GLY A O 1 ATOM 1833 N N . ASP A 1 241 ? -24.518 26.196 83.722 1.00 35.56 ? 241 ASP A N 1 ATOM 1834 C CA . ASP A 1 241 ? -25.587 26.459 84.684 1.00 33.93 ? 241 ASP A CA 1 ATOM 1835 C C . ASP A 1 241 ? -25.626 25.342 85.735 1.00 33.82 ? 241 ASP A C 1 ATOM 1836 O O . ASP A 1 241 ? -24.810 24.410 85.708 1.00 33.79 ? 241 ASP A O 1 ATOM 1837 C CB . ASP A 1 241 ? -26.942 26.630 83.970 1.00 33.34 ? 241 ASP A CB 1 ATOM 1838 C CG . ASP A 1 241 ? -27.899 27.597 84.702 1.00 34.71 ? 241 ASP A CG 1 ATOM 1839 O OD1 . ASP A 1 241 ? -27.816 27.743 85.959 1.00 34.73 ? 241 ASP A OD1 1 ATOM 1840 O OD2 . ASP A 1 241 ? -28.749 28.214 84.017 1.00 32.57 ? 241 ASP A OD2 1 ATOM 1841 N N . ILE A 1 242 ? -26.550 25.483 86.685 1.00 32.94 ? 242 ILE A N 1 ATOM 1842 C CA . ILE A 1 242 ? -26.629 24.646 87.866 1.00 33.39 ? 242 ILE A CA 1 ATOM 1843 C C . ILE A 1 242 ? -28.094 24.372 88.181 1.00 31.98 ? 242 ILE A C 1 ATOM 1844 O O . ILE A 1 242 ? -28.896 25.294 88.192 1.00 31.90 ? 242 ILE A O 1 ATOM 1845 C CB . ILE A 1 242 ? -26.008 25.373 89.082 1.00 35.03 ? 242 ILE A CB 1 ATOM 1846 C CG1 . ILE A 1 242 ? -24.511 25.634 88.872 1.00 36.38 ? 242 ILE A CG1 1 ATOM 1847 C CG2 . ILE A 1 242 ? -26.223 24.584 90.354 1.00 36.32 ? 242 ILE A CG2 1 ATOM 1848 C CD1 . ILE A 1 242 ? -23.932 26.657 89.843 1.00 37.90 ? 242 ILE A CD1 1 ATOM 1849 N N . LEU A 1 243 ? -28.446 23.116 88.424 1.00 30.65 ? 243 LEU A N 1 ATOM 1850 C CA . LEU A 1 243 ? -29.765 22.789 88.957 1.00 29.48 ? 243 LEU A CA 1 ATOM 1851 C C . LEU A 1 243 ? -29.714 22.922 90.481 1.00 30.81 ? 243 LEU A C 1 ATOM 1852 O O . LEU A 1 243 ? -28.765 22.450 91.106 1.00 31.98 ? 243 LEU A O 1 ATOM 1853 C CB . LEU A 1 243 ? -30.150 21.357 88.599 1.00 28.51 ? 243 LEU A CB 1 ATOM 1854 C CG . LEU A 1 243 ? -31.595 20.929 88.865 1.00 28.14 ? 243 LEU A CG 1 ATOM 1855 C CD1 . LEU A 1 243 ? -32.549 21.620 87.903 1.00 27.37 ? 243 LEU A CD1 1 ATOM 1856 C CD2 . LEU A 1 243 ? -31.754 19.420 88.745 1.00 27.62 ? 243 LEU A CD2 1 ATOM 1857 N N . LEU A 1 244 ? -30.731 23.562 91.056 1.00 29.86 ? 244 LEU A N 1 ATOM 1858 C CA . LEU A 1 244 ? -30.911 23.646 92.497 1.00 30.30 ? 244 LEU A CA 1 ATOM 1859 C C . LEU A 1 244 ? -32.334 23.205 92.850 1.00 29.80 ? 244 LEU A C 1 ATOM 1860 O O . LEU A 1 244 ? -33.315 23.735 92.307 1.00 28.42 ? 244 LEU A O 1 ATOM 1861 C CB . LEU A 1 244 ? -30.643 25.070 92.990 1.00 31.31 ? 244 LEU A CB 1 ATOM 1862 C CG . LEU A 1 244 ? -30.538 25.330 94.503 1.00 31.58 ? 244 LEU A CG 1 ATOM 1863 C CD1 . LEU A 1 244 ? -29.630 24.333 95.217 1.00 33.93 ? 244 LEU A CD1 1 ATOM 1864 C CD2 . LEU A 1 244 ? -30.034 26.753 94.733 1.00 31.77 ? 244 LEU A CD2 1 ATOM 1865 N N . ILE A 1 245 ? -32.426 22.213 93.734 1.00 29.16 ? 245 ILE A N 1 ATOM 1866 C CA . ILE A 1 245 ? -33.695 21.664 94.201 1.00 29.08 ? 245 ILE A CA 1 ATOM 1867 C C . ILE A 1 245 ? -33.872 21.984 95.697 1.00 30.84 ? 245 ILE A C 1 ATOM 1868 O O . ILE A 1 245 ? -33.008 21.640 96.507 1.00 31.04 ? 245 ILE A O 1 ATOM 1869 C CB . ILE A 1 245 ? -33.733 20.140 93.985 1.00 29.27 ? 245 ILE A CB 1 ATOM 1870 C CG1 . ILE A 1 245 ? -33.466 19.801 92.499 1.00 29.28 ? 245 ILE A CG1 1 ATOM 1871 C CG2 . ILE A 1 245 ? -35.050 19.573 94.485 1.00 29.71 ? 245 ILE A CG2 1 ATOM 1872 C CD1 . ILE A 1 245 ? -33.538 18.327 92.158 1.00 29.74 ? 245 ILE A CD1 1 ATOM 1873 N N . ASN A 1 246 ? -35.002 22.608 96.039 1.00 30.79 ? 246 ASN A N 1 ATOM 1874 C CA . ASN A 1 246 ? -35.284 23.131 97.387 1.00 32.31 ? 246 ASN A CA 1 ATOM 1875 C C . ASN A 1 246 ? -36.666 22.605 97.813 1.00 32.16 ? 246 ASN A C 1 ATOM 1876 O O . ASN A 1 246 ? -37.681 22.919 97.176 1.00 31.31 ? 246 ASN A O 1 ATOM 1877 C CB . ASN A 1 246 ? -35.259 24.660 97.302 1.00 34.60 ? 246 ASN A CB 1 ATOM 1878 C CG . ASN A 1 246 ? -35.202 25.370 98.655 1.00 37.95 ? 246 ASN A CG 1 ATOM 1879 O OD1 . ASN A 1 246 ? -35.504 26.563 98.715 1.00 39.54 ? 246 ASN A OD1 1 ATOM 1880 N ND2 . ASN A 1 246 ? -34.818 24.674 99.725 1.00 40.58 ? 246 ASN A ND2 1 ATOM 1881 N N . SER A 1 247 ? -36.715 21.787 98.862 1.00 31.84 ? 247 SER A N 1 ATOM 1882 C CA . SER A 1 247 ? -37.954 21.101 99.242 1.00 32.03 ? 247 SER A CA 1 ATOM 1883 C C . SER A 1 247 ? -37.943 20.666 100.706 1.00 33.49 ? 247 SER A C 1 ATOM 1884 O O . SER A 1 247 ? -36.876 20.412 101.266 1.00 33.34 ? 247 SER A O 1 ATOM 1885 C CB . SER A 1 247 ? -38.135 19.858 98.380 1.00 31.85 ? 247 SER A CB 1 ATOM 1886 O OG . SER A 1 247 ? -39.290 19.116 98.753 1.00 33.06 ? 247 SER A OG 1 ATOM 1887 N N . THR A 1 248 ? -39.141 20.538 101.283 1.00 33.69 ? 248 THR A N 1 ATOM 1888 C CA . THR A 1 248 ? -39.325 19.979 102.624 1.00 35.87 ? 248 THR A CA 1 ATOM 1889 C C . THR A 1 248 ? -40.219 18.732 102.611 1.00 35.30 ? 248 THR A C 1 ATOM 1890 O O . THR A 1 248 ? -40.734 18.311 103.658 1.00 35.57 ? 248 THR A O 1 ATOM 1891 C CB . THR A 1 248 ? -39.961 21.024 103.554 1.00 37.65 ? 248 THR A CB 1 ATOM 1892 O OG1 . THR A 1 248 ? -41.160 21.530 102.942 1.00 39.19 ? 248 THR A OG1 1 ATOM 1893 C CG2 . THR A 1 248 ? -38.968 22.171 103.815 1.00 38.08 ? 248 THR A CG2 1 ATOM 1894 N N . GLY A 1 249 ? -40.396 18.137 101.431 1.00 32.84 ? 249 GLY A N 1 ATOM 1895 C CA . GLY A 1 249 ? -41.273 16.987 101.275 1.00 32.26 ? 249 GLY A CA 1 ATOM 1896 C C . GLY A 1 249 ? -41.958 16.971 99.923 1.00 31.00 ? 249 GLY A C 1 ATOM 1897 O O . GLY A 1 249 ? -41.903 17.942 99.178 1.00 30.44 ? 249 GLY A O 1 ATOM 1898 N N . ASN A 1 250 ? -42.603 15.851 99.621 1.00 30.18 ? 250 ASN A N 1 ATOM 1899 C CA . ASN A 1 250 ? -43.435 15.695 98.420 1.00 29.28 ? 250 ASN A CA 1 ATOM 1900 C C . ASN A 1 250 ? -42.653 15.688 97.106 1.00 28.19 ? 250 ASN A C 1 ATOM 1901 O O . ASN A 1 250 ? -43.248 15.738 96.028 1.00 27.27 ? 250 ASN A O 1 ATOM 1902 C CB . ASN A 1 250 ? -44.541 16.765 98.381 1.00 28.75 ? 250 ASN A CB 1 ATOM 1903 C CG . ASN A 1 250 ? -45.414 16.749 99.624 1.00 30.08 ? 250 ASN A CG 1 ATOM 1904 O OD1 . ASN A 1 250 ? -45.041 17.303 100.660 1.00 31.23 ? 250 ASN A OD1 1 ATOM 1905 N ND2 . ASN A 1 250 ? -46.589 16.124 99.524 1.00 28.65 ? 250 ASN A ND2 1 ATOM 1906 N N . LEU A 1 251 ? -41.332 15.612 97.211 1.00 28.41 ? 251 LEU A N 1 ATOM 1907 C CA . LEU A 1 251 ? -40.447 15.647 96.055 1.00 27.81 ? 251 LEU A CA 1 ATOM 1908 C C . LEU A 1 251 ? -40.270 14.253 95.468 1.00 27.50 ? 251 LEU A C 1 ATOM 1909 O O . LEU A 1 251 ? -39.840 13.326 96.149 1.00 26.23 ? 251 LEU A O 1 ATOM 1910 C CB . LEU A 1 251 ? -39.082 16.234 96.442 1.00 27.48 ? 251 LEU A CB 1 ATOM 1911 C CG . LEU A 1 251 ? -38.018 16.246 95.331 1.00 27.56 ? 251 LEU A CG 1 ATOM 1912 C CD1 . LEU A 1 251 ? -38.449 17.132 94.172 1.00 26.33 ? 251 LEU A CD1 1 ATOM 1913 C CD2 . LEU A 1 251 ? -36.672 16.698 95.876 1.00 26.48 ? 251 LEU A CD2 1 ATOM 1914 N N . ILE A 1 252 ? -40.604 14.119 94.188 1.00 25.76 ? 252 ILE A N 1 ATOM 1915 C CA . ILE A 1 252 ? -40.246 12.954 93.411 1.00 25.47 ? 252 ILE A CA 1 ATOM 1916 C C . ILE A 1 252 ? -39.011 13.370 92.600 1.00 25.26 ? 252 ILE A C 1 ATOM 1917 O O . ILE A 1 252 ? -39.112 14.077 91.588 1.00 24.53 ? 252 ILE A O 1 ATOM 1918 C CB . ILE A 1 252 ? -41.416 12.516 92.515 1.00 25.90 ? 252 ILE A CB 1 ATOM 1919 C CG1 . ILE A 1 252 ? -42.665 12.229 93.362 1.00 26.86 ? 252 ILE A CG1 1 ATOM 1920 C CG2 . ILE A 1 252 ? -41.058 11.282 91.697 1.00 25.74 ? 252 ILE A CG2 1 ATOM 1921 C CD1 . ILE A 1 252 ? -42.501 11.111 94.383 1.00 27.03 ? 252 ILE A CD1 1 ATOM 1922 N N . ALA A 1 253 ? -37.845 12.945 93.061 1.00 25.10 ? 253 ALA A N 1 ATOM 1923 C CA . ALA A 1 253 ? -36.579 13.494 92.586 1.00 25.38 ? 253 ALA A CA 1 ATOM 1924 C C . ALA A 1 253 ? -36.072 12.813 91.325 1.00 24.73 ? 253 ALA A C 1 ATOM 1925 O O . ALA A 1 253 ? -36.362 11.629 91.089 1.00 24.51 ? 253 ALA A O 1 ATOM 1926 C CB . ALA A 1 253 ? -35.530 13.398 93.688 1.00 25.89 ? 253 ALA A CB 1 ATOM 1927 N N . PRO A 1 254 ? -35.285 13.548 90.514 1.00 24.82 ? 254 PRO A N 1 ATOM 1928 C CA . PRO A 1 254 ? -34.626 12.955 89.352 1.00 24.78 ? 254 PRO A CA 1 ATOM 1929 C C . PRO A 1 254 ? -33.449 12.088 89.783 1.00 25.30 ? 254 PRO A C 1 ATOM 1930 O O . PRO A 1 254 ? -32.839 12.377 90.816 1.00 24.71 ? 254 PRO A O 1 ATOM 1931 C CB . PRO A 1 254 ? -34.123 14.173 88.581 1.00 24.99 ? 254 PRO A CB 1 ATOM 1932 C CG . PRO A 1 254 ? -33.812 15.160 89.653 1.00 25.51 ? 254 PRO A CG 1 ATOM 1933 C CD . PRO A 1 254 ? -34.873 14.947 90.718 1.00 24.96 ? 254 PRO A CD 1 ATOM 1934 N N . ARG A 1 255 ? -33.163 11.032 89.023 1.00 25.86 ? 255 ARG A N 1 ATOM 1935 C CA . ARG A 1 255 ? -31.974 10.191 89.287 1.00 26.61 ? 255 ARG A CA 1 ATOM 1936 C C . ARG A 1 255 ? -30.799 10.571 88.378 1.00 26.75 ? 255 ARG A C 1 ATOM 1937 O O . ARG A 1 255 ? -29.732 9.934 88.410 1.00 28.24 ? 255 ARG A O 1 ATOM 1938 C CB . ARG A 1 255 ? -32.296 8.719 89.099 1.00 27.02 ? 255 ARG A CB 1 ATOM 1939 C CG . ARG A 1 255 ? -33.337 8.172 90.054 1.00 27.42 ? 255 ARG A CG 1 ATOM 1940 C CD . ARG A 1 255 ? -33.417 6.662 89.955 1.00 28.18 ? 255 ARG A CD 1 ATOM 1941 N NE . ARG A 1 255 ? -34.427 6.131 90.863 1.00 28.88 ? 255 ARG A NE 1 ATOM 1942 C CZ . ARG A 1 255 ? -34.210 5.800 92.139 1.00 30.46 ? 255 ARG A CZ 1 ATOM 1943 N NH1 . ARG A 1 255 ? -33.000 5.912 92.679 1.00 29.75 ? 255 ARG A NH1 1 ATOM 1944 N NH2 . ARG A 1 255 ? -35.222 5.340 92.873 1.00 31.03 ? 255 ARG A NH2 1 ATOM 1945 N N . GLY A 1 256 ? -30.994 11.613 87.578 1.00 25.57 ? 256 GLY A N 1 ATOM 1946 C CA . GLY A 1 256 ? -30.027 12.003 86.557 1.00 25.61 ? 256 GLY A CA 1 ATOM 1947 C C . GLY A 1 256 ? -30.755 12.753 85.465 1.00 24.68 ? 256 GLY A C 1 ATOM 1948 O O . GLY A 1 256 ? -31.831 13.293 85.719 1.00 24.38 ? 256 GLY A O 1 ATOM 1949 N N . TYR A 1 257 ? -30.168 12.789 84.270 1.00 24.47 ? 257 TYR A N 1 ATOM 1950 C CA . TYR A 1 257 ? -30.713 13.590 83.168 1.00 24.56 ? 257 TYR A CA 1 ATOM 1951 C C . TYR A 1 257 ? -30.793 12.813 81.876 1.00 23.77 ? 257 TYR A C 1 ATOM 1952 O O . TYR A 1 257 ? -30.046 11.846 81.641 1.00 23.68 ? 257 TYR A O 1 ATOM 1953 C CB . TYR A 1 257 ? -29.863 14.834 82.900 1.00 25.06 ? 257 TYR A CB 1 ATOM 1954 C CG . TYR A 1 257 ? -28.453 14.511 82.483 1.00 25.77 ? 257 TYR A CG 1 ATOM 1955 C CD1 . TYR A 1 257 ? -27.451 14.353 83.440 1.00 27.30 ? 257 TYR A CD1 1 ATOM 1956 C CD2 . TYR A 1 257 ? -28.114 14.350 81.145 1.00 26.36 ? 257 TYR A CD2 1 ATOM 1957 C CE1 . TYR A 1 257 ? -26.156 14.040 83.075 1.00 28.26 ? 257 TYR A CE1 1 ATOM 1958 C CE2 . TYR A 1 257 ? -26.823 14.033 80.770 1.00 27.15 ? 257 TYR A CE2 1 ATOM 1959 C CZ . TYR A 1 257 ? -25.848 13.883 81.745 1.00 28.21 ? 257 TYR A CZ 1 ATOM 1960 O OH . TYR A 1 257 ? -24.575 13.587 81.383 1.00 29.39 ? 257 TYR A OH 1 ATOM 1961 N N . PHE A 1 258 ? -31.693 13.282 81.022 1.00 22.68 ? 258 PHE A N 1 ATOM 1962 C CA . PHE A 1 258 ? -31.777 12.816 79.650 1.00 22.76 ? 258 PHE A CA 1 ATOM 1963 C C . PHE A 1 258 ? -30.932 13.701 78.765 1.00 24.77 ? 258 PHE A C 1 ATOM 1964 O O . PHE A 1 258 ? -30.867 14.915 78.964 1.00 24.78 ? 258 PHE A O 1 ATOM 1965 C CB . PHE A 1 258 ? -33.223 12.838 79.177 1.00 21.31 ? 258 PHE A CB 1 ATOM 1966 C CG . PHE A 1 258 ? -34.076 11.843 79.871 1.00 20.35 ? 258 PHE A CG 1 ATOM 1967 C CD1 . PHE A 1 258 ? -34.181 10.542 79.385 1.00 20.49 ? 258 PHE A CD1 1 ATOM 1968 C CD2 . PHE A 1 258 ? -34.737 12.178 81.032 1.00 20.79 ? 258 PHE A CD2 1 ATOM 1969 C CE1 . PHE A 1 258 ? -34.981 9.612 80.031 1.00 20.17 ? 258 PHE A CE1 1 ATOM 1970 C CE2 . PHE A 1 258 ? -35.547 11.257 81.676 1.00 20.43 ? 258 PHE A CE2 1 ATOM 1971 C CZ . PHE A 1 258 ? -35.650 9.964 81.171 1.00 20.41 ? 258 PHE A CZ 1 ATOM 1972 N N . LYS A 1 259 ? -30.248 13.073 77.820 1.00 27.56 ? 259 LYS A N 1 ATOM 1973 C CA . LYS A 1 259 ? -29.639 13.794 76.735 1.00 31.21 ? 259 LYS A CA 1 ATOM 1974 C C . LYS A 1 259 ? -30.778 14.435 75.951 1.00 31.67 ? 259 LYS A C 1 ATOM 1975 O O . LYS A 1 259 ? -31.889 13.882 75.845 1.00 31.85 ? 259 LYS A O 1 ATOM 1976 C CB . LYS A 1 259 ? -28.836 12.855 75.851 1.00 34.47 ? 259 LYS A CB 1 ATOM 1977 C CG . LYS A 1 259 ? -27.468 12.510 76.398 1.00 37.99 ? 259 LYS A CG 1 ATOM 1978 C CD . LYS A 1 259 ? -26.407 13.476 75.883 1.00 41.53 ? 259 LYS A CD 1 ATOM 1979 C CE . LYS A 1 259 ? -25.073 12.779 75.665 1.00 43.78 ? 259 LYS A CE 1 ATOM 1980 N NZ . LYS A 1 259 ? -24.628 12.037 76.879 1.00 47.41 ? 259 LYS A NZ 1 ATOM 1981 N N . ILE A 1 260 ? -30.536 15.630 75.458 1.00 31.77 ? 260 ILE A N 1 ATOM 1982 C CA . ILE A 1 260 ? -31.490 16.251 74.583 1.00 31.09 ? 260 ILE A CA 1 ATOM 1983 C C . ILE A 1 260 ? -30.737 16.591 73.303 1.00 31.23 ? 260 ILE A C 1 ATOM 1984 O O . ILE A 1 260 ? -29.700 17.257 73.334 1.00 32.38 ? 260 ILE A O 1 ATOM 1985 C CB . ILE A 1 260 ? -32.224 17.416 75.280 1.00 32.07 ? 260 ILE A CB 1 ATOM 1986 C CG1 . ILE A 1 260 ? -33.236 18.034 74.333 1.00 32.60 ? 260 ILE A CG1 1 ATOM 1987 C CG2 . ILE A 1 260 ? -31.255 18.451 75.828 1.00 33.02 ? 260 ILE A CG2 1 ATOM 1988 C CD1 . ILE A 1 260 ? -34.393 18.698 75.043 1.00 32.24 ? 260 ILE A CD1 1 ATOM 1989 N N . ARG A 1 261 ? -31.216 16.039 72.190 1.00 30.39 ? 261 ARG A N 1 ATOM 1990 C CA . ARG A 1 261 ? -30.537 16.153 70.899 1.00 31.59 ? 261 ARG A CA 1 ATOM 1991 C C . ARG A 1 261 ? -31.413 16.959 69.967 1.00 30.24 ? 261 ARG A C 1 ATOM 1992 O O . ARG A 1 261 ? -32.580 17.192 70.255 1.00 28.53 ? 261 ARG A O 1 ATOM 1993 C CB . ARG A 1 261 ? -30.263 14.760 70.320 1.00 33.92 ? 261 ARG A CB 1 ATOM 1994 C CG . ARG A 1 261 ? -29.324 13.919 71.197 1.00 37.08 ? 261 ARG A CG 1 ATOM 1995 C CD . ARG A 1 261 ? -28.810 12.675 70.472 1.00 40.43 ? 261 ARG A CD 1 ATOM 1996 N NE . ARG A 1 261 ? -27.928 11.833 71.295 1.00 42.17 ? 261 ARG A NE 1 ATOM 1997 C CZ . ARG A 1 261 ? -26.651 12.100 71.584 1.00 46.40 ? 261 ARG A CZ 1 ATOM 1998 N NH1 . ARG A 1 261 ? -26.062 13.211 71.140 1.00 46.89 ? 261 ARG A NH1 1 ATOM 1999 N NH2 . ARG A 1 261 ? -25.948 11.252 72.341 1.00 47.21 ? 261 ARG A NH2 1 ATOM 2000 N N . SER A 1 262 ? -30.855 17.404 68.855 1.00 31.18 ? 262 SER A N 1 ATOM 2001 C CA . SER A 1 262 ? -31.689 17.978 67.800 1.00 31.72 ? 262 SER A CA 1 ATOM 2002 C C . SER A 1 262 ? -31.498 17.177 66.532 1.00 30.47 ? 262 SER A C 1 ATOM 2003 O O . SER A 1 262 ? -30.394 16.712 66.219 1.00 29.42 ? 262 SER A O 1 ATOM 2004 C CB . SER A 1 262 ? -31.372 19.452 67.567 1.00 33.92 ? 262 SER A CB 1 ATOM 2005 O OG . SER A 1 262 ? -30.099 19.600 67.006 1.00 37.30 ? 262 SER A OG 1 ATOM 2006 N N . GLY A 1 263 ? -32.583 17.000 65.799 1.00 28.43 ? 263 GLY A N 1 ATOM 2007 C CA . GLY A 1 263 ? -32.526 16.282 64.544 1.00 27.81 ? 263 GLY A CA 1 ATOM 2008 C C . GLY A 1 263 ? -33.925 16.115 64.005 1.00 27.26 ? 263 GLY A C 1 ATOM 2009 O O . GLY A 1 263 ? -34.819 16.900 64.344 1.00 28.19 ? 263 GLY A O 1 ATOM 2010 N N . LYS A 1 264 ? -34.108 15.035 63.253 1.00 25.38 ? 264 LYS A N 1 ATOM 2011 C CA . LYS A 1 264 ? -35.268 14.856 62.407 1.00 24.79 ? 264 LYS A CA 1 ATOM 2012 C C . LYS A 1 264 ? -36.280 13.864 62.999 1.00 20.23 ? 264 LYS A C 1 ATOM 2013 O O . LYS A 1 264 ? -37.100 13.343 62.280 1.00 19.64 ? 264 LYS A O 1 ATOM 2014 C CB . LYS A 1 264 ? -34.805 14.385 61.023 1.00 27.69 ? 264 LYS A CB 1 ATOM 2015 C CG . LYS A 1 264 ? -33.699 15.235 60.368 1.00 32.68 ? 264 LYS A CG 1 ATOM 2016 C CD . LYS A 1 264 ? -33.929 16.747 60.440 1.00 35.75 ? 264 LYS A CD 1 ATOM 2017 C CE . LYS A 1 264 ? -32.714 17.576 59.986 1.00 39.10 ? 264 LYS A CE 1 ATOM 2018 N NZ . LYS A 1 264 ? -31.795 18.030 61.089 1.00 41.36 ? 264 LYS A NZ 1 ATOM 2019 N N . SER A 1 265 ? -36.213 13.598 64.304 1.00 18.28 ? 265 SER A N 1 ATOM 2020 C CA . SER A 1 265 ? -37.097 12.606 64.901 1.00 17.36 ? 265 SER A CA 1 ATOM 2021 C C . SER A 1 265 ? -38.503 13.154 65.140 1.00 16.85 ? 265 SER A C 1 ATOM 2022 O O . SER A 1 265 ? -38.692 14.356 65.256 1.00 16.13 ? 265 SER A O 1 ATOM 2023 C CB . SER A 1 265 ? -36.501 12.051 66.206 1.00 17.85 ? 265 SER A CB 1 ATOM 2024 O OG . SER A 1 265 ? -35.227 11.466 65.930 1.00 17.69 ? 265 SER A OG 1 ATOM 2025 N N . SER A 1 266 ? -39.474 12.245 65.199 1.00 15.97 ? 266 SER A N 1 ATOM 2026 C CA . SER A 1 266 ? -40.858 12.608 65.489 1.00 15.81 ? 266 SER A CA 1 ATOM 2027 C C . SER A 1 266 ? -41.578 11.440 66.144 1.00 15.64 ? 266 SER A C 1 ATOM 2028 O O . SER A 1 266 ? -40.956 10.432 66.508 1.00 15.40 ? 266 SER A O 1 ATOM 2029 C CB . SER A 1 266 ? -41.584 13.043 64.214 1.00 15.91 ? 266 SER A CB 1 ATOM 2030 O OG . SER A 1 266 ? -42.854 13.643 64.525 1.00 15.95 ? 266 SER A OG 1 ATOM 2031 N N . ILE A 1 267 ? -42.886 11.607 66.314 1.00 15.49 ? 267 ILE A N 1 ATOM 2032 C CA . ILE A 1 267 ? -43.757 10.631 66.938 1.00 15.70 ? 267 ILE A CA 1 ATOM 2033 C C . ILE A 1 267 ? -45.045 10.596 66.138 1.00 16.12 ? 267 ILE A C 1 ATOM 2034 O O . ILE A 1 267 ? -45.469 11.649 65.587 1.00 15.59 ? 267 ILE A O 1 ATOM 2035 C CB . ILE A 1 267 ? -44.009 10.993 68.420 1.00 15.58 ? 267 ILE A CB 1 ATOM 2036 C CG1 . ILE A 1 267 ? -44.823 9.901 69.144 1.00 16.29 ? 267 ILE A CG1 1 ATOM 2037 C CG2 . ILE A 1 267 ? -44.666 12.360 68.583 1.00 15.75 ? 267 ILE A CG2 1 ATOM 2038 C CD1 . ILE A 1 267 ? -44.732 9.998 70.664 1.00 16.45 ? 267 ILE A CD1 1 ATOM 2039 N N . MET A 1 268 ? -45.653 9.414 66.030 1.00 16.37 ? 268 MET A N 1 ATOM 2040 C CA . MET A 1 268 ? -46.882 9.248 65.261 1.00 17.04 ? 268 MET A CA 1 ATOM 2041 C C . MET A 1 268 ? -47.819 8.303 65.999 1.00 17.46 ? 268 MET A C 1 ATOM 2042 O O . MET A 1 268 ? -47.376 7.310 66.576 1.00 17.70 ? 268 MET A O 1 ATOM 2043 C CB . MET A 1 268 ? -46.602 8.675 63.870 1.00 17.37 ? 268 MET A CB 1 ATOM 2044 C CG . MET A 1 268 ? -47.789 8.693 62.898 1.00 17.99 ? 268 MET A CG 1 ATOM 2045 S SD . MET A 1 268 ? -47.329 8.053 61.274 1.00 18.73 ? 268 MET A SD 1 ATOM 2046 C CE . MET A 1 268 ? -46.305 9.405 60.628 1.00 18.15 ? 268 MET A CE 1 ATOM 2047 N N . ARG A 1 269 ? -49.108 8.626 65.986 1.00 17.35 ? 269 ARG A N 1 ATOM 2048 C CA . ARG A 1 269 ? -50.126 7.721 66.511 1.00 17.93 ? 269 ARG A CA 1 ATOM 2049 C C . ARG A 1 269 ? -50.600 6.835 65.374 1.00 17.94 ? 269 ARG A C 1 ATOM 2050 O O . ARG A 1 269 ? -51.078 7.335 64.331 1.00 17.53 ? 269 ARG A O 1 ATOM 2051 C CB . ARG A 1 269 ? -51.316 8.493 67.086 1.00 19.00 ? 269 ARG A CB 1 ATOM 2052 C CG . ARG A 1 269 ? -50.928 9.464 68.195 1.00 19.66 ? 269 ARG A CG 1 ATOM 2053 C CD . ARG A 1 269 ? -52.134 10.032 68.928 1.00 20.50 ? 269 ARG A CD 1 ATOM 2054 N NE . ARG A 1 269 ? -51.723 10.928 70.010 1.00 21.39 ? 269 ARG A NE 1 ATOM 2055 C CZ . ARG A 1 269 ? -51.501 12.236 69.866 1.00 21.86 ? 269 ARG A CZ 1 ATOM 2056 N NH1 . ARG A 1 269 ? -51.673 12.830 68.696 1.00 22.23 ? 269 ARG A NH1 1 ATOM 2057 N NH2 . ARG A 1 269 ? -51.121 12.958 70.907 1.00 22.04 ? 269 ARG A NH2 1 ATOM 2058 N N . SER A 1 270 ? -50.479 5.524 65.548 1.00 17.81 ? 270 SER A N 1 ATOM 2059 C CA . SER A 1 270 ? -50.894 4.583 64.534 1.00 18.78 ? 270 SER A CA 1 ATOM 2060 C C . SER A 1 270 ? -51.093 3.205 65.141 1.00 20.04 ? 270 SER A C 1 ATOM 2061 O O . SER A 1 270 ? -50.334 2.789 66.038 1.00 19.86 ? 270 SER A O 1 ATOM 2062 C CB . SER A 1 270 ? -49.832 4.451 63.436 1.00 18.66 ? 270 SER A CB 1 ATOM 2063 O OG . SER A 1 270 ? -50.190 3.444 62.489 1.00 18.65 ? 270 SER A OG 1 ATOM 2064 N N . ASP A 1 271 ? -52.073 2.491 64.612 1.00 20.88 ? 271 ASP A N 1 ATOM 2065 C CA . ASP A 1 271 ? -52.201 1.055 64.896 1.00 22.71 ? 271 ASP A CA 1 ATOM 2066 C C . ASP A 1 271 ? -51.742 0.122 63.786 1.00 23.31 ? 271 ASP A C 1 ATOM 2067 O O . ASP A 1 271 ? -51.984 -1.102 63.854 1.00 23.57 ? 271 ASP A O 1 ATOM 2068 C CB . ASP A 1 271 ? -53.637 0.745 65.318 1.00 24.10 ? 271 ASP A CB 1 ATOM 2069 C CG . ASP A 1 271 ? -53.971 1.333 66.662 1.00 25.71 ? 271 ASP A CG 1 ATOM 2070 O OD1 . ASP A 1 271 ? -53.071 1.420 67.532 1.00 26.16 ? 271 ASP A OD1 1 ATOM 2071 O OD2 . ASP A 1 271 ? -55.139 1.716 66.869 1.00 28.00 ? 271 ASP A OD2 1 ATOM 2072 N N . ALA A 1 272 ? -51.022 0.646 62.798 1.00 21.88 ? 272 ALA A N 1 ATOM 2073 C CA . ALA A 1 272 ? -50.598 -0.167 61.672 1.00 22.32 ? 272 ALA A CA 1 ATOM 2074 C C . ALA A 1 272 ? -49.483 -1.104 62.130 1.00 22.59 ? 272 ALA A C 1 ATOM 2075 O O . ALA A 1 272 ? -48.607 -0.693 62.888 1.00 21.26 ? 272 ALA A O 1 ATOM 2076 C CB . ALA A 1 272 ? -50.125 0.710 60.512 1.00 22.26 ? 272 ALA A CB 1 ATOM 2077 N N . PRO A 1 273 ? -49.510 -2.360 61.671 1.00 23.40 ? 273 PRO A N 1 ATOM 2078 C CA . PRO A 1 273 ? -48.411 -3.260 62.032 1.00 24.40 ? 273 PRO A CA 1 ATOM 2079 C C . PRO A 1 273 ? -47.094 -2.827 61.402 1.00 24.21 ? 273 PRO A C 1 ATOM 2080 O O . PRO A 1 273 ? -47.090 -2.220 60.333 1.00 23.09 ? 273 PRO A O 1 ATOM 2081 C CB . PRO A 1 273 ? -48.871 -4.613 61.461 1.00 25.33 ? 273 PRO A CB 1 ATOM 2082 C CG . PRO A 1 273 ? -49.785 -4.265 60.356 1.00 25.81 ? 273 PRO A CG 1 ATOM 2083 C CD . PRO A 1 273 ? -50.496 -3.015 60.798 1.00 24.81 ? 273 PRO A CD 1 ATOM 2084 N N . ILE A 1 274 ? -45.990 -3.135 62.068 1.00 25.21 ? 274 ILE A N 1 ATOM 2085 C CA . ILE A 1 274 ? -44.675 -2.852 61.523 1.00 25.91 ? 274 ILE A CA 1 ATOM 2086 C C . ILE A 1 274 ? -44.199 -4.038 60.698 1.00 27.22 ? 274 ILE A C 1 ATOM 2087 O O . ILE A 1 274 ? -44.226 -5.168 61.171 1.00 27.00 ? 274 ILE A O 1 ATOM 2088 C CB . ILE A 1 274 ? -43.688 -2.502 62.635 1.00 27.06 ? 274 ILE A CB 1 ATOM 2089 C CG1 . ILE A 1 274 ? -44.113 -1.166 63.273 1.00 28.18 ? 274 ILE A CG1 1 ATOM 2090 C CG2 . ILE A 1 274 ? -42.286 -2.333 62.065 1.00 27.04 ? 274 ILE A CG2 1 ATOM 2091 C CD1 . ILE A 1 274 ? -43.453 -0.895 64.587 1.00 30.20 ? 274 ILE A CD1 1 ATOM 2092 N N . GLY A 1 275 ? -43.789 -3.778 59.465 1.00 27.31 ? 275 GLY A N 1 ATOM 2093 C CA . GLY A 1 275 ? -43.328 -4.833 58.567 1.00 28.38 ? 275 GLY A CA 1 ATOM 2094 C C . GLY A 1 275 ? -41.856 -4.756 58.222 1.00 28.62 ? 275 GLY A C 1 ATOM 2095 O O . GLY A 1 275 ? -41.226 -3.694 58.337 1.00 26.66 ? 275 GLY A O 1 ATOM 2096 N N . LYS A 1 276 ? -41.311 -5.888 57.774 1.00 29.33 ? 276 LYS A N 1 ATOM 2097 C CA . LYS A 1 276 ? -39.953 -5.953 57.246 1.00 30.56 ? 276 LYS A CA 1 ATOM 2098 C C . LYS A 1 276 ? -39.967 -5.591 55.768 1.00 30.10 ? 276 LYS A C 1 ATOM 2099 O O . LYS A 1 276 ? -40.133 -6.438 54.901 1.00 31.20 ? 276 LYS A O 1 ATOM 2100 C CB . LYS A 1 276 ? -39.354 -7.340 57.486 1.00 34.04 ? 276 LYS A CB 1 ATOM 2101 C CG . LYS A 1 276 ? -39.268 -7.664 58.971 1.00 37.23 ? 276 LYS A CG 1 ATOM 2102 C CD . LYS A 1 276 ? -38.353 -8.842 59.270 1.00 41.18 ? 276 LYS A CD 1 ATOM 2103 C CE . LYS A 1 276 ? -38.437 -9.227 60.739 1.00 43.06 ? 276 LYS A CE 1 ATOM 2104 N NZ . LYS A 1 276 ? -38.008 -8.124 61.652 1.00 46.27 ? 276 LYS A NZ 1 ATOM 2105 N N . CYS A 1 277 ? -39.842 -4.306 55.490 1.00 27.67 ? 277 CYS A N 1 ATOM 2106 C CA . CYS A 1 277 ? -39.902 -3.778 54.135 1.00 27.38 ? 277 CYS A CA 1 ATOM 2107 C C . CYS A 1 277 ? -39.275 -2.384 54.176 1.00 24.68 ? 277 CYS A C 1 ATOM 2108 O O . CYS A 1 277 ? -38.873 -1.921 55.250 1.00 23.25 ? 277 CYS A O 1 ATOM 2109 C CB . CYS A 1 277 ? -41.345 -3.725 53.573 1.00 29.33 ? 277 CYS A CB 1 ATOM 2110 S SG . CYS A 1 277 ? -42.610 -2.920 54.617 1.00 33.78 ? 277 CYS A SG 1 ATOM 2111 N N . ASN A 1 278 ? -39.178 -1.751 53.011 1.00 23.21 ? 278 ASN A N 1 ATOM 2112 C CA . ASN A 1 278 ? -38.474 -0.488 52.856 1.00 22.76 ? 278 ASN A CA 1 ATOM 2113 C C . ASN A 1 278 ? -39.356 0.519 52.122 1.00 22.63 ? 278 ASN A C 1 ATOM 2114 O O . ASN A 1 278 ? -39.734 0.294 50.977 1.00 21.89 ? 278 ASN A O 1 ATOM 2115 C CB . ASN A 1 278 ? -37.187 -0.749 52.073 1.00 23.02 ? 278 ASN A CB 1 ATOM 2116 C CG . ASN A 1 278 ? -36.223 0.417 52.119 1.00 23.37 ? 278 ASN A CG 1 ATOM 2117 O OD1 . ASN A 1 278 ? -36.594 1.545 51.819 1.00 23.77 ? 278 ASN A OD1 1 ATOM 2118 N ND2 . ASN A 1 278 ? -34.974 0.141 52.445 1.00 23.04 ? 278 ASN A ND2 1 ATOM 2119 N N . SER A 1 279 ? -39.685 1.614 52.790 1.00 22.19 ? 279 SER A N 1 ATOM 2120 C CA . SER A 1 279 ? -40.484 2.686 52.182 1.00 22.60 ? 279 SER A CA 1 ATOM 2121 C C . SER A 1 279 ? -40.160 4.017 52.835 1.00 21.70 ? 279 SER A C 1 ATOM 2122 O O . SER A 1 279 ? -40.113 4.111 54.057 1.00 20.73 ? 279 SER A O 1 ATOM 2123 C CB . SER A 1 279 ? -41.979 2.361 52.310 1.00 23.83 ? 279 SER A CB 1 ATOM 2124 O OG . SER A 1 279 ? -42.770 3.393 51.748 1.00 25.94 ? 279 SER A OG 1 ATOM 2125 N N . GLU A 1 280 ? -39.947 5.051 52.021 1.00 21.44 ? 280 GLU A N 1 ATOM 2126 C CA . GLU A 1 280 ? -39.526 6.362 52.540 1.00 22.11 ? 280 GLU A CA 1 ATOM 2127 C C . GLU A 1 280 ? -40.623 7.131 53.305 1.00 20.57 ? 280 GLU A C 1 ATOM 2128 O O . GLU A 1 280 ? -40.321 7.899 54.222 1.00 19.51 ? 280 GLU A O 1 ATOM 2129 C CB . GLU A 1 280 ? -39.018 7.248 51.395 1.00 23.82 ? 280 GLU A CB 1 ATOM 2130 C CG . GLU A 1 280 ? -37.761 6.737 50.701 1.00 26.82 ? 280 GLU A CG 1 ATOM 2131 C CD . GLU A 1 280 ? -36.489 6.975 51.480 1.00 29.15 ? 280 GLU A CD 1 ATOM 2132 O OE1 . GLU A 1 280 ? -36.489 7.807 52.421 1.00 30.32 ? 280 GLU A OE1 1 ATOM 2133 O OE2 . GLU A 1 280 ? -35.476 6.320 51.139 1.00 30.51 ? 280 GLU A OE2 1 ATOM 2134 N N . CYS A 1 281 ? -41.878 6.951 52.889 1.00 19.74 ? 281 CYS A N 1 ATOM 2135 C CA . CYS A 1 281 ? -43.000 7.754 53.390 1.00 18.70 ? 281 CYS A CA 1 ATOM 2136 C C . CYS A 1 281 ? -43.871 6.955 54.325 1.00 18.25 ? 281 CYS A C 1 ATOM 2137 O O . CYS A 1 281 ? -44.384 5.895 53.936 1.00 18.09 ? 281 CYS A O 1 ATOM 2138 C CB . CYS A 1 281 ? -43.862 8.261 52.237 1.00 19.20 ? 281 CYS A CB 1 ATOM 2139 S SG . CYS A 1 281 ? -45.238 9.282 52.826 1.00 19.54 ? 281 CYS A SG 1 ATOM 2140 N N . ILE A 1 282 ? -44.012 7.457 55.554 1.00 17.19 ? 282 ILE A N 1 ATOM 2141 C CA . ILE A 1 282 ? -44.866 6.824 56.565 1.00 17.31 ? 282 ILE A CA 1 ATOM 2142 C C . ILE A 1 282 ? -46.100 7.693 56.854 1.00 16.71 ? 282 ILE A C 1 ATOM 2143 O O . ILE A 1 282 ? -46.008 8.919 57.000 1.00 16.21 ? 282 ILE A O 1 ATOM 2144 C CB . ILE A 1 282 ? -44.088 6.587 57.866 1.00 17.12 ? 282 ILE A CB 1 ATOM 2145 C CG1 . ILE A 1 282 ? -42.850 5.728 57.595 1.00 17.80 ? 282 ILE A CG1 1 ATOM 2146 C CG2 . ILE A 1 282 ? -44.979 5.945 58.944 1.00 17.04 ? 282 ILE A CG2 1 ATOM 2147 C CD1 . ILE A 1 282 ? -41.871 5.653 58.781 1.00 18.09 ? 282 ILE A CD1 1 ATOM 2148 N N . THR A 1 283 ? -47.261 7.047 56.899 1.00 16.58 ? 283 THR A N 1 ATOM 2149 C CA . THR A 1 283 ? -48.498 7.653 57.382 1.00 16.29 ? 283 THR A CA 1 ATOM 2150 C C . THR A 1 283 ? -49.093 6.733 58.463 1.00 16.51 ? 283 THR A C 1 ATOM 2151 O O . THR A 1 283 ? -48.704 5.568 58.557 1.00 16.45 ? 283 THR A O 1 ATOM 2152 C CB . THR A 1 283 ? -49.568 7.821 56.267 1.00 16.42 ? 283 THR A CB 1 ATOM 2153 O OG1 . THR A 1 283 ? -50.238 6.588 56.023 1.00 16.45 ? 283 THR A OG1 1 ATOM 2154 C CG2 . THR A 1 283 ? -48.963 8.370 54.943 1.00 16.80 ? 283 THR A CG2 1 ATOM 2155 N N . PRO A 1 284 ? -50.058 7.234 59.244 1.00 16.72 ? 284 PRO A N 1 ATOM 2156 C CA . PRO A 1 284 ? -50.737 6.393 60.234 1.00 17.27 ? 284 PRO A CA 1 ATOM 2157 C C . PRO A 1 284 ? -51.446 5.170 59.643 1.00 18.34 ? 284 PRO A C 1 ATOM 2158 O O . PRO A 1 284 ? -51.673 4.186 60.354 1.00 18.16 ? 284 PRO A O 1 ATOM 2159 C CB . PRO A 1 284 ? -51.750 7.348 60.868 1.00 17.46 ? 284 PRO A CB 1 ATOM 2160 C CG . PRO A 1 284 ? -51.161 8.717 60.687 1.00 17.06 ? 284 PRO A CG 1 ATOM 2161 C CD . PRO A 1 284 ? -50.464 8.653 59.367 1.00 16.77 ? 284 PRO A CD 1 ATOM 2162 N N . ASN A 1 285 ? -51.791 5.235 58.362 1.00 18.70 ? 285 ASN A N 1 ATOM 2163 C CA . ASN A 1 285 ? -52.444 4.119 57.673 1.00 20.33 ? 285 ASN A CA 1 ATOM 2164 C C . ASN A 1 285 ? -51.435 3.089 57.226 1.00 20.55 ? 285 ASN A C 1 ATOM 2165 O O . ASN A 1 285 ? -51.818 2.027 56.751 1.00 22.70 ? 285 ASN A O 1 ATOM 2166 C CB . ASN A 1 285 ? -53.143 4.578 56.407 1.00 21.62 ? 285 ASN A CB 1 ATOM 2167 C CG . ASN A 1 285 ? -54.090 5.733 56.624 1.00 23.45 ? 285 ASN A CG 1 ATOM 2168 O OD1 . ASN A 1 285 ? -53.689 6.856 56.900 1.00 22.32 ? 285 ASN A OD1 1 ATOM 2169 N ND2 . ASN A 1 285 ? -55.357 5.464 56.466 1.00 29.01 ? 285 ASN A ND2 1 ATOM 2170 N N . GLY A 1 286 ? -50.148 3.406 57.352 1.00 19.50 ? 286 GLY A N 1 ATOM 2171 C CA . GLY A 1 286 ? -49.094 2.595 56.789 1.00 19.30 ? 286 GLY A CA 1 ATOM 2172 C C . GLY A 1 286 ? -48.195 3.385 55.865 1.00 19.27 ? 286 GLY A C 1 ATOM 2173 O O . GLY A 1 286 ? -48.480 4.558 55.526 1.00 18.22 ? 286 GLY A O 1 ATOM 2174 N N . SER A 1 287 ? -47.113 2.743 55.435 1.00 19.29 ? 287 SER A N 1 ATOM 2175 C CA . SER A 1 287 ? -46.218 3.358 54.457 1.00 19.81 ? 287 SER A CA 1 ATOM 2176 C C . SER A 1 287 ? -46.914 3.473 53.112 1.00 19.72 ? 287 SER A C 1 ATOM 2177 O O . SER A 1 287 ? -47.763 2.661 52.781 1.00 20.17 ? 287 SER A O 1 ATOM 2178 C CB . SER A 1 287 ? -44.932 2.549 54.323 1.00 20.47 ? 287 SER A CB 1 ATOM 2179 O OG . SER A 1 287 ? -44.225 2.562 55.550 1.00 20.91 ? 287 SER A OG 1 ATOM 2180 N N . ILE A 1 288 ? -46.591 4.511 52.355 1.00 19.30 ? 288 ILE A N 1 ATOM 2181 C CA . ILE A 1 288 ? -47.144 4.665 51.025 1.00 19.78 ? 288 ILE A CA 1 ATOM 2182 C C . ILE A 1 288 ? -46.032 4.913 50.042 1.00 20.45 ? 288 ILE A C 1 ATOM 2183 O O . ILE A 1 288 ? -45.014 5.507 50.387 1.00 21.40 ? 288 ILE A O 1 ATOM 2184 C CB . ILE A 1 288 ? -48.213 5.792 50.940 1.00 19.36 ? 288 ILE A CB 1 ATOM 2185 C CG1 . ILE A 1 288 ? -47.591 7.161 51.273 1.00 19.34 ? 288 ILE A CG1 1 ATOM 2186 C CG2 . ILE A 1 288 ? -49.377 5.490 51.876 1.00 20.04 ? 288 ILE A CG2 1 ATOM 2187 C CD1 . ILE A 1 288 ? -48.506 8.371 50.997 1.00 19.34 ? 288 ILE A CD1 1 ATOM 2188 N N . PRO A 1 289 ? -46.207 4.456 48.801 1.00 21.78 ? 289 PRO A N 1 ATOM 2189 C CA . PRO A 1 289 ? -45.220 4.788 47.792 1.00 22.18 ? 289 PRO A CA 1 ATOM 2190 C C . PRO A 1 289 ? -45.144 6.299 47.587 1.00 21.70 ? 289 PRO A C 1 ATOM 2191 O O . PRO A 1 289 ? -46.153 6.991 47.780 1.00 21.42 ? 289 PRO A O 1 ATOM 2192 C CB . PRO A 1 289 ? -45.749 4.118 46.520 1.00 22.58 ? 289 PRO A CB 1 ATOM 2193 C CG . PRO A 1 289 ? -46.899 3.284 46.912 1.00 23.36 ? 289 PRO A CG 1 ATOM 2194 C CD . PRO A 1 289 ? -47.305 3.616 48.301 1.00 22.82 ? 289 PRO A CD 1 ATOM 2195 N N . ASN A 1 290 ? -43.979 6.788 47.191 1.00 21.36 ? 290 ASN A N 1 ATOM 2196 C CA . ASN A 1 290 ? -43.764 8.219 47.037 1.00 21.41 ? 290 ASN A CA 1 ATOM 2197 C C . ASN A 1 290 ? -43.368 8.623 45.619 1.00 21.24 ? 290 ASN A C 1 ATOM 2198 O O . ASN A 1 290 ? -42.738 9.658 45.416 1.00 22.34 ? 290 ASN A O 1 ATOM 2199 C CB . ASN A 1 290 ? -42.757 8.735 48.067 1.00 21.93 ? 290 ASN A CB 1 ATOM 2200 C CG . ASN A 1 290 ? -41.354 8.256 47.816 1.00 22.65 ? 290 ASN A CG 1 ATOM 2201 O OD1 . ASN A 1 290 ? -41.131 7.371 46.987 1.00 23.09 ? 290 ASN A OD1 1 ATOM 2202 N ND2 . ASN A 1 290 ? -40.398 8.813 48.565 1.00 21.76 ? 290 ASN A ND2 1 ATOM 2203 N N . ASP A 1 291 ? -43.788 7.830 44.642 1.00 21.39 ? 291 ASP A N 1 ATOM 2204 C CA . ASP A 1 291 ? -43.539 8.156 43.246 1.00 22.45 ? 291 ASP A CA 1 ATOM 2205 C C . ASP A 1 291 ? -44.386 9.388 42.839 1.00 21.16 ? 291 ASP A C 1 ATOM 2206 O O . ASP A 1 291 ? -43.899 10.269 42.133 1.00 21.96 ? 291 ASP A O 1 ATOM 2207 C CB . ASP A 1 291 ? -43.788 6.953 42.296 1.00 23.77 ? 291 ASP A CB 1 ATOM 2208 C CG . ASP A 1 291 ? -45.110 6.242 42.532 1.00 25.86 ? 291 ASP A CG 1 ATOM 2209 O OD1 . ASP A 1 291 ? -45.274 5.565 43.566 1.00 28.67 ? 291 ASP A OD1 1 ATOM 2210 O OD2 . ASP A 1 291 ? -46.005 6.316 41.665 1.00 28.88 ? 291 ASP A OD2 1 ATOM 2211 N N . LYS A 1 292 ? -45.608 9.459 43.344 1.00 19.41 ? 292 LYS A N 1 ATOM 2212 C CA . LYS A 1 292 ? -46.564 10.508 42.920 1.00 18.37 ? 292 LYS A CA 1 ATOM 2213 C C . LYS A 1 292 ? -46.350 11.795 43.707 1.00 17.14 ? 292 LYS A C 1 ATOM 2214 O O . LYS A 1 292 ? -45.850 11.764 44.839 1.00 17.48 ? 292 LYS A O 1 ATOM 2215 C CB . LYS A 1 292 ? -48.000 10.005 43.076 1.00 18.56 ? 292 LYS A CB 1 ATOM 2216 C CG . LYS A 1 292 ? -48.320 8.791 42.219 1.00 19.46 ? 292 LYS A CG 1 ATOM 2217 C CD . LYS A 1 292 ? -49.709 8.254 42.483 1.00 19.80 ? 292 LYS A CD 1 ATOM 2218 C CE . LYS A 1 292 ? -49.983 6.940 41.744 1.00 21.24 ? 292 LYS A CE 1 ATOM 2219 N NZ . LYS A 1 292 ? -49.131 5.810 42.251 1.00 22.49 ? 292 LYS A NZ 1 ATOM 2220 N N . PRO A 1 293 ? -46.714 12.943 43.123 1.00 16.42 ? 293 PRO A N 1 ATOM 2221 C CA . PRO A 1 293 ? -46.438 14.200 43.822 1.00 16.10 ? 293 PRO A CA 1 ATOM 2222 C C . PRO A 1 293 ? -47.447 14.539 44.923 1.00 15.47 ? 293 PRO A C 1 ATOM 2223 O O . PRO A 1 293 ? -47.140 15.354 45.820 1.00 15.15 ? 293 PRO A O 1 ATOM 2224 C CB . PRO A 1 293 ? -46.449 15.223 42.696 1.00 16.44 ? 293 PRO A CB 1 ATOM 2225 C CG . PRO A 1 293 ? -47.356 14.645 41.670 1.00 16.34 ? 293 PRO A CG 1 ATOM 2226 C CD . PRO A 1 293 ? -47.090 13.167 41.719 1.00 16.42 ? 293 PRO A CD 1 ATOM 2227 N N . PHE A 1 294 ? -48.626 13.936 44.839 1.00 14.96 ? 294 PHE A N 1 ATOM 2228 C CA . PHE A 1 294 ? -49.727 14.195 45.765 1.00 14.63 ? 294 PHE A CA 1 ATOM 2229 C C . PHE A 1 294 ? -50.248 12.879 46.342 1.00 14.43 ? 294 PHE A C 1 ATOM 2230 O O . PHE A 1 294 ? -49.992 11.798 45.794 1.00 14.26 ? 294 PHE A O 1 ATOM 2231 C CB . PHE A 1 294 ? -50.864 14.949 45.048 1.00 14.78 ? 294 PHE A CB 1 ATOM 2232 C CG . PHE A 1 294 ? -50.393 16.181 44.329 1.00 14.80 ? 294 PHE A CG 1 ATOM 2233 C CD1 . PHE A 1 294 ? -49.891 17.243 45.049 1.00 15.31 ? 294 PHE A CD1 1 ATOM 2234 C CD2 . PHE A 1 294 ? -50.438 16.269 42.938 1.00 15.49 ? 294 PHE A CD2 1 ATOM 2235 C CE1 . PHE A 1 294 ? -49.420 18.392 44.411 1.00 15.37 ? 294 PHE A CE1 1 ATOM 2236 C CE2 . PHE A 1 294 ? -49.969 17.422 42.303 1.00 15.50 ? 294 PHE A CE2 1 ATOM 2237 C CZ . PHE A 1 294 ? -49.464 18.464 43.040 1.00 15.37 ? 294 PHE A CZ 1 ATOM 2238 N N . GLN A 1 295 ? -50.985 12.984 47.429 1.00 14.18 ? 295 GLN A N 1 ATOM 2239 C CA . GLN A 1 295 ? -51.609 11.844 48.081 1.00 14.10 ? 295 GLN A CA 1 ATOM 2240 C C . GLN A 1 295 ? -52.831 12.293 48.856 1.00 14.48 ? 295 GLN A C 1 ATOM 2241 O O . GLN A 1 295 ? -52.909 13.432 49.306 1.00 13.87 ? 295 GLN A O 1 ATOM 2242 C CB . GLN A 1 295 ? -50.613 11.112 48.996 1.00 14.29 ? 295 GLN A CB 1 ATOM 2243 C CG . GLN A 1 295 ? -49.974 11.949 50.084 1.00 13.66 ? 295 GLN A CG 1 ATOM 2244 C CD . GLN A 1 295 ? -50.667 11.919 51.425 1.00 13.80 ? 295 GLN A CD 1 ATOM 2245 O OE1 . GLN A 1 295 ? -51.644 11.179 51.650 1.00 13.97 ? 295 GLN A OE1 1 ATOM 2246 N NE2 . GLN A 1 295 ? -50.137 12.732 52.366 1.00 13.33 ? 295 GLN A NE2 1 ATOM 2247 N N . ASN A 1 296 ? -53.803 11.387 48.984 1.00 14.76 ? 296 ASN A N 1 ATOM 2248 C CA A ASN A 1 296 ? -55.030 11.612 49.711 0.50 14.95 ? 296 ASN A CA 1 ATOM 2249 C CA B ASN A 1 296 ? -54.978 11.664 49.795 0.50 15.55 ? 296 ASN A CA 1 ATOM 2250 C C . ASN A 1 296 ? -55.200 10.575 50.847 1.00 15.63 ? 296 ASN A C 1 ATOM 2251 O O . ASN A 1 296 ? -56.319 10.359 51.343 1.00 16.59 ? 296 ASN A O 1 ATOM 2252 C CB A ASN A 1 296 ? -56.173 11.530 48.689 0.50 14.78 ? 296 ASN A CB 1 ATOM 2253 C CB B ASN A 1 296 ? -56.206 11.832 48.910 0.50 16.18 ? 296 ASN A CB 1 ATOM 2254 C CG A ASN A 1 296 ? -57.520 11.922 49.255 0.50 14.73 ? 296 ASN A CG 1 ATOM 2255 C CG B ASN A 1 296 ? -56.786 10.517 48.491 0.50 17.28 ? 296 ASN A CG 1 ATOM 2256 O OD1 A ASN A 1 296 ? -58.487 11.178 49.108 0.50 14.91 ? 296 ASN A OD1 1 ATOM 2257 O OD1 B ASN A 1 296 ? -56.056 9.519 48.360 0.50 18.06 ? 296 ASN A OD1 1 ATOM 2258 N ND2 A ASN A 1 296 ? -57.598 13.085 49.892 0.50 14.37 ? 296 ASN A ND2 1 ATOM 2259 N ND2 B ASN A 1 296 ? -58.114 10.474 48.351 0.50 17.92 ? 296 ASN A ND2 1 ATOM 2260 N N . VAL A 1 297 ? -54.110 9.923 51.249 1.00 15.56 ? 297 VAL A N 1 ATOM 2261 C CA . VAL A 1 297 ? -54.173 8.885 52.281 1.00 15.53 ? 297 VAL A CA 1 ATOM 2262 C C . VAL A 1 297 ? -54.299 9.516 53.686 1.00 15.61 ? 297 VAL A C 1 ATOM 2263 O O . VAL A 1 297 ? -55.201 9.162 54.444 1.00 15.83 ? 297 VAL A O 1 ATOM 2264 C CB . VAL A 1 297 ? -52.965 7.929 52.198 1.00 15.71 ? 297 VAL A CB 1 ATOM 2265 C CG1 . VAL A 1 297 ? -52.972 6.922 53.367 1.00 15.93 ? 297 VAL A CG1 1 ATOM 2266 C CG2 . VAL A 1 297 ? -52.914 7.209 50.841 1.00 16.12 ? 297 VAL A CG2 1 ATOM 2267 N N . ASN A 1 298 ? -53.430 10.469 54.036 1.00 15.04 ? 298 ASN A N 1 ATOM 2268 C CA . ASN A 1 298 ? -53.449 11.060 55.383 1.00 15.01 ? 298 ASN A CA 1 ATOM 2269 C C . ASN A 1 298 ? -52.670 12.364 55.390 1.00 14.81 ? 298 ASN A C 1 ATOM 2270 O O . ASN A 1 298 ? -51.553 12.464 54.826 1.00 14.27 ? 298 ASN A O 1 ATOM 2271 C CB . ASN A 1 298 ? -52.845 10.095 56.413 1.00 15.30 ? 298 ASN A CB 1 ATOM 2272 C CG . ASN A 1 298 ? -53.394 10.291 57.823 1.00 15.47 ? 298 ASN A CG 1 ATOM 2273 O OD1 . ASN A 1 298 ? -53.302 11.378 58.411 1.00 15.18 ? 298 ASN A OD1 1 ATOM 2274 N ND2 . ASN A 1 298 ? -53.969 9.219 58.383 1.00 16.47 ? 298 ASN A ND2 1 ATOM 2275 N N . ARG A 1 299 ? -53.229 13.350 56.072 1.00 15.07 ? 299 ARG A N 1 ATOM 2276 C CA . ARG A 1 299 ? -52.519 14.605 56.283 1.00 15.68 ? 299 ARG A CA 1 ATOM 2277 C C . ARG A 1 299 ? -51.308 14.454 57.225 1.00 15.04 ? 299 ARG A C 1 ATOM 2278 O O . ARG A 1 299 ? -50.406 15.299 57.219 1.00 13.76 ? 299 ARG A O 1 ATOM 2279 C CB . ARG A 1 299 ? -53.468 15.679 56.818 1.00 17.34 ? 299 ARG A CB 1 ATOM 2280 C CG . ARG A 1 299 ? -54.001 15.453 58.211 1.00 19.46 ? 299 ARG A CG 1 ATOM 2281 C CD . ARG A 1 299 ? -54.969 16.575 58.598 1.00 22.65 ? 299 ARG A CD 1 ATOM 2282 N NE . ARG A 1 299 ? -56.154 16.615 57.741 1.00 23.80 ? 299 ARG A NE 1 ATOM 2283 C CZ . ARG A 1 299 ? -57.024 17.642 57.693 1.00 26.15 ? 299 ARG A CZ 1 ATOM 2284 N NH1 . ARG A 1 299 ? -56.874 18.766 58.432 1.00 26.55 ? 299 ARG A NH1 1 ATOM 2285 N NH2 . ARG A 1 299 ? -58.057 17.563 56.887 1.00 27.05 ? 299 ARG A NH2 1 ATOM 2286 N N . ILE A 1 300 ? -51.296 13.390 58.023 1.00 14.68 ? 300 ILE A N 1 ATOM 2287 C CA . ILE A 1 300 ? -50.156 13.102 58.913 1.00 14.88 ? 300 ILE A CA 1 ATOM 2288 C C . ILE A 1 300 ? -49.157 12.270 58.131 1.00 15.26 ? 300 ILE A C 1 ATOM 2289 O O . ILE A 1 300 ? -49.489 11.177 57.665 1.00 14.68 ? 300 ILE A O 1 ATOM 2290 C CB . ILE A 1 300 ? -50.595 12.351 60.187 1.00 15.17 ? 300 ILE A CB 1 ATOM 2291 C CG1 . ILE A 1 300 ? -51.560 13.217 61.011 1.00 15.38 ? 300 ILE A CG1 1 ATOM 2292 C CG2 . ILE A 1 300 ? -49.365 11.929 61.037 1.00 14.99 ? 300 ILE A CG2 1 ATOM 2293 C CD1 . ILE A 1 300 ? -52.330 12.411 62.069 1.00 15.83 ? 300 ILE A CD1 1 ATOM 2294 N N . THR A 1 301 ? -47.931 12.782 57.994 1.00 15.77 ? 301 THR A N 1 ATOM 2295 C CA . THR A 1 301 ? -46.879 12.092 57.240 1.00 16.40 ? 301 THR A CA 1 ATOM 2296 C C . THR A 1 301 ? -45.512 12.255 57.925 1.00 16.57 ? 301 THR A C 1 ATOM 2297 O O . THR A 1 301 ? -45.278 13.225 58.690 1.00 16.83 ? 301 THR A O 1 ATOM 2298 C CB . THR A 1 301 ? -46.738 12.580 55.771 1.00 17.13 ? 301 THR A CB 1 ATOM 2299 O OG1 . THR A 1 301 ? -46.078 13.850 55.726 1.00 19.30 ? 301 THR A OG1 1 ATOM 2300 C CG2 . THR A 1 301 ? -48.079 12.700 55.058 1.00 17.94 ? 301 THR A CG2 1 ATOM 2301 N N . TYR A 1 302 ? -44.617 11.330 57.609 1.00 16.18 ? 302 TYR A N 1 ATOM 2302 C CA . TYR A 1 302 ? -43.212 11.407 58.036 1.00 16.32 ? 302 TYR A CA 1 ATOM 2303 C C . TYR A 1 302 ? -42.340 10.878 56.915 1.00 16.32 ? 302 TYR A C 1 ATOM 2304 O O . TYR A 1 302 ? -42.616 9.824 56.353 1.00 16.86 ? 302 TYR A O 1 ATOM 2305 C CB . TYR A 1 302 ? -42.952 10.630 59.344 1.00 16.55 ? 302 TYR A CB 1 ATOM 2306 C CG . TYR A 1 302 ? -41.504 10.721 59.802 1.00 16.73 ? 302 TYR A CG 1 ATOM 2307 C CD1 . TYR A 1 302 ? -40.532 9.846 59.323 1.00 17.39 ? 302 TYR A CD1 1 ATOM 2308 C CD2 . TYR A 1 302 ? -41.099 11.707 60.685 1.00 17.07 ? 302 TYR A CD2 1 ATOM 2309 C CE1 . TYR A 1 302 ? -39.204 9.954 59.719 1.00 17.37 ? 302 TYR A CE1 1 ATOM 2310 C CE2 . TYR A 1 302 ? -39.763 11.818 61.088 1.00 17.56 ? 302 TYR A CE2 1 ATOM 2311 C CZ . TYR A 1 302 ? -38.827 10.931 60.609 1.00 17.58 ? 302 TYR A CZ 1 ATOM 2312 O OH . TYR A 1 302 ? -37.506 11.047 60.992 1.00 18.67 ? 302 TYR A OH 1 ATOM 2313 N N . GLY A 1 303 ? -41.306 11.631 56.566 1.00 16.31 ? 303 GLY A N 1 ATOM 2314 C CA . GLY A 1 303 ? -40.351 11.220 55.542 1.00 16.77 ? 303 GLY A CA 1 ATOM 2315 C C . GLY A 1 303 ? -40.569 11.921 54.209 1.00 17.22 ? 303 GLY A C 1 ATOM 2316 O O . GLY A 1 303 ? -41.251 12.973 54.146 1.00 17.17 ? 303 GLY A O 1 ATOM 2317 N N . ALA A 1 304 ? -39.989 11.345 53.154 1.00 17.40 ? 304 ALA A N 1 ATOM 2318 C CA . ALA A 1 304 ? -40.121 11.885 51.788 1.00 17.69 ? 304 ALA A CA 1 ATOM 2319 C C . ALA A 1 304 ? -41.477 11.473 51.253 1.00 17.82 ? 304 ALA A C 1 ATOM 2320 O O . ALA A 1 304 ? -41.641 10.387 50.720 1.00 18.24 ? 304 ALA A O 1 ATOM 2321 C CB . ALA A 1 304 ? -38.989 11.381 50.888 1.00 18.38 ? 304 ALA A CB 1 ATOM 2322 N N . CYS A 1 305 ? -42.469 12.362 51.399 1.00 17.68 ? 305 CYS A N 1 ATOM 2323 C CA . CYS A 1 305 ? -43.849 12.005 51.112 1.00 17.83 ? 305 CYS A CA 1 ATOM 2324 C C . CYS A 1 305 ? -44.494 12.912 50.061 1.00 16.71 ? 305 CYS A C 1 ATOM 2325 O O . CYS A 1 305 ? -44.207 14.110 50.016 1.00 16.74 ? 305 CYS A O 1 ATOM 2326 C CB . CYS A 1 305 ? -44.679 12.168 52.379 1.00 18.91 ? 305 CYS A CB 1 ATOM 2327 S SG . CYS A 1 305 ? -44.311 10.924 53.615 1.00 21.54 ? 305 CYS A SG 1 ATOM 2328 N N . PRO A 1 306 ? -45.411 12.356 49.277 1.00 15.58 ? 306 PRO A N 1 ATOM 2329 C CA . PRO A 1 306 ? -46.271 13.220 48.449 1.00 15.35 ? 306 PRO A CA 1 ATOM 2330 C C . PRO A 1 306 ? -47.033 14.216 49.340 1.00 15.08 ? 306 PRO A C 1 ATOM 2331 O O . PRO A 1 306 ? -47.282 13.942 50.525 1.00 15.34 ? 306 PRO A O 1 ATOM 2332 C CB . PRO A 1 306 ? -47.224 12.221 47.771 1.00 15.47 ? 306 PRO A CB 1 ATOM 2333 C CG . PRO A 1 306 ? -46.546 10.876 47.907 1.00 15.63 ? 306 PRO A CG 1 ATOM 2334 C CD . PRO A 1 306 ? -45.816 10.949 49.199 1.00 15.60 ? 306 PRO A CD 1 ATOM 2335 N N . ARG A 1 307 ? -47.422 15.360 48.776 1.00 14.90 ? 307 ARG A N 1 ATOM 2336 C CA . ARG A 1 307 ? -48.181 16.340 49.522 1.00 14.67 ? 307 ARG A CA 1 ATOM 2337 C C . ARG A 1 307 ? -49.664 15.951 49.597 1.00 14.18 ? 307 ARG A C 1 ATOM 2338 O O . ARG A 1 307 ? -50.268 15.533 48.591 1.00 14.09 ? 307 ARG A O 1 ATOM 2339 C CB . ARG A 1 307 ? -48.053 17.718 48.867 1.00 14.93 ? 307 ARG A CB 1 ATOM 2340 C CG . ARG A 1 307 ? -46.648 18.298 48.985 1.00 15.53 ? 307 ARG A CG 1 ATOM 2341 C CD . ARG A 1 307 ? -46.648 19.787 48.689 1.00 15.77 ? 307 ARG A CD 1 ATOM 2342 N NE . ARG A 1 307 ? -45.351 20.414 48.973 1.00 16.45 ? 307 ARG A NE 1 ATOM 2343 C CZ . ARG A 1 307 ? -44.969 20.898 50.157 1.00 16.37 ? 307 ARG A CZ 1 ATOM 2344 N NH1 . ARG A 1 307 ? -45.725 20.828 51.232 1.00 16.33 ? 307 ARG A NH1 1 ATOM 2345 N NH2 . ARG A 1 307 ? -43.775 21.434 50.266 1.00 17.32 ? 307 ARG A NH2 1 ATOM 2346 N N . TYR A 1 308 ? -50.238 16.137 50.773 1.00 13.89 ? 308 TYR A N 1 ATOM 2347 C CA . TYR A 1 308 ? -51.645 15.839 51.005 1.00 14.04 ? 308 TYR A CA 1 ATOM 2348 C C . TYR A 1 308 ? -52.560 16.812 50.278 1.00 14.15 ? 308 TYR A C 1 ATOM 2349 O O . TYR A 1 308 ? -52.429 18.019 50.439 1.00 14.17 ? 308 TYR A O 1 ATOM 2350 C CB . TYR A 1 308 ? -51.987 15.859 52.484 1.00 14.44 ? 308 TYR A CB 1 ATOM 2351 C CG . TYR A 1 308 ? -53.408 15.398 52.734 1.00 14.95 ? 308 TYR A CG 1 ATOM 2352 C CD1 . TYR A 1 308 ? -53.739 14.042 52.694 1.00 15.54 ? 308 TYR A CD1 1 ATOM 2353 C CD2 . TYR A 1 308 ? -54.417 16.311 52.936 1.00 15.68 ? 308 TYR A CD2 1 ATOM 2354 C CE1 . TYR A 1 308 ? -55.043 13.614 52.908 1.00 16.42 ? 308 TYR A CE1 1 ATOM 2355 C CE2 . TYR A 1 308 ? -55.715 15.908 53.130 1.00 16.65 ? 308 TYR A CE2 1 ATOM 2356 C CZ . TYR A 1 308 ? -56.020 14.550 53.131 1.00 16.93 ? 308 TYR A CZ 1 ATOM 2357 O OH . TYR A 1 308 ? -57.335 14.191 53.328 1.00 18.71 ? 308 TYR A OH 1 ATOM 2358 N N . VAL A 1 309 ? -53.497 16.275 49.501 1.00 14.08 ? 309 VAL A N 1 ATOM 2359 C CA . VAL A 1 309 ? -54.523 17.078 48.863 1.00 14.07 ? 309 VAL A CA 1 ATOM 2360 C C . VAL A 1 309 ? -55.910 16.457 49.091 1.00 15.05 ? 309 VAL A C 1 ATOM 2361 O O . VAL A 1 309 ? -56.037 15.263 49.455 1.00 14.56 ? 309 VAL A O 1 ATOM 2362 C CB . VAL A 1 309 ? -54.257 17.209 47.350 1.00 13.67 ? 309 VAL A CB 1 ATOM 2363 C CG1 . VAL A 1 309 ? -52.891 17.910 47.099 1.00 13.69 ? 309 VAL A CG1 1 ATOM 2364 C CG2 . VAL A 1 309 ? -54.289 15.839 46.655 1.00 13.65 ? 309 VAL A CG2 1 ATOM 2365 N N . LYS A 1 310 ? -56.941 17.244 48.830 1.00 15.80 ? 310 LYS A N 1 ATOM 2366 C CA . LYS A 1 310 ? -58.321 16.753 49.010 1.00 17.57 ? 310 LYS A CA 1 ATOM 2367 C C . LYS A 1 310 ? -58.822 15.847 47.890 1.00 17.92 ? 310 LYS A C 1 ATOM 2368 O O . LYS A 1 310 ? -59.692 15.005 48.127 1.00 17.81 ? 310 LYS A O 1 ATOM 2369 C CB . LYS A 1 310 ? -59.274 17.924 49.199 1.00 20.29 ? 310 LYS A CB 1 ATOM 2370 C CG . LYS A 1 310 ? -59.083 18.665 50.516 1.00 23.24 ? 310 LYS A CG 1 ATOM 2371 C CD . LYS A 1 310 ? -59.982 19.901 50.600 1.00 26.40 ? 310 LYS A CD 1 ATOM 2372 C CE . LYS A 1 310 ? -59.835 20.766 49.351 1.00 29.22 ? 310 LYS A CE 1 ATOM 2373 N NZ . LYS A 1 310 ? -60.346 22.176 49.408 1.00 34.50 ? 310 LYS A NZ 1 ATOM 2374 N N . GLN A 1 311 ? -58.299 16.029 46.682 1.00 16.97 ? 311 GLN A N 1 ATOM 2375 C CA . GLN A 1 311 ? -58.709 15.257 45.507 1.00 17.56 ? 311 GLN A CA 1 ATOM 2376 C C . GLN A 1 311 ? -58.351 13.797 45.693 1.00 18.60 ? 311 GLN A C 1 ATOM 2377 O O . GLN A 1 311 ? -57.295 13.482 46.234 1.00 18.41 ? 311 GLN A O 1 ATOM 2378 C CB . GLN A 1 311 ? -58.000 15.783 44.263 1.00 16.63 ? 311 GLN A CB 1 ATOM 2379 C CG . GLN A 1 311 ? -58.395 17.211 43.897 1.00 16.27 ? 311 GLN A CG 1 ATOM 2380 C CD . GLN A 1 311 ? -57.423 18.252 44.402 1.00 16.10 ? 311 GLN A CD 1 ATOM 2381 O OE1 . GLN A 1 311 ? -56.844 18.119 45.484 1.00 15.61 ? 311 GLN A OE1 1 ATOM 2382 N NE2 . GLN A 1 311 ? -57.243 19.305 43.606 1.00 15.63 ? 311 GLN A NE2 1 ATOM 2383 N N . ASN A 1 312 ? -59.207 12.893 45.226 1.00 19.68 ? 312 ASN A N 1 ATOM 2384 C CA . ASN A 1 312 ? -58.831 11.475 45.290 1.00 21.71 ? 312 ASN A CA 1 ATOM 2385 C C . ASN A 1 312 ? -58.230 10.962 43.980 1.00 20.73 ? 312 ASN A C 1 ATOM 2386 O O . ASN A 1 312 ? -57.712 9.853 43.959 1.00 21.27 ? 312 ASN A O 1 ATOM 2387 C CB . ASN A 1 312 ? -59.986 10.584 45.792 1.00 24.92 ? 312 ASN A CB 1 ATOM 2388 C CG . ASN A 1 312 ? -61.253 10.792 45.034 1.00 28.77 ? 312 ASN A CG 1 ATOM 2389 O OD1 . ASN A 1 312 ? -61.239 11.149 43.869 1.00 33.19 ? 312 ASN A OD1 1 ATOM 2390 N ND2 . ASN A 1 312 ? -62.381 10.583 45.707 1.00 35.00 ? 312 ASN A ND2 1 ATOM 2391 N N . THR A 1 313 ? -58.267 11.787 42.924 1.00 18.94 ? 313 THR A N 1 ATOM 2392 C CA . THR A 1 313 ? -57.631 11.489 41.648 1.00 18.71 ? 313 THR A CA 1 ATOM 2393 C C . THR A 1 313 ? -57.305 12.797 40.917 1.00 18.37 ? 313 THR A C 1 ATOM 2394 O O . THR A 1 313 ? -58.072 13.764 40.976 1.00 18.11 ? 313 THR A O 1 ATOM 2395 C CB . THR A 1 313 ? -58.523 10.577 40.735 1.00 19.57 ? 313 THR A CB 1 ATOM 2396 O OG1 . THR A 1 313 ? -57.889 10.385 39.454 1.00 20.16 ? 313 THR A OG1 1 ATOM 2397 C CG2 . THR A 1 313 ? -59.869 11.217 40.503 1.00 19.77 ? 313 THR A CG2 1 ATOM 2398 N N . LEU A 1 314 ? -56.135 12.827 40.294 1.00 17.43 ? 314 LEU A N 1 ATOM 2399 C CA . LEU A 1 314 ? -55.758 13.860 39.347 1.00 17.38 ? 314 LEU A CA 1 ATOM 2400 C C . LEU A 1 314 ? -54.981 13.196 38.215 1.00 17.58 ? 314 LEU A C 1 ATOM 2401 O O . LEU A 1 314 ? -53.861 12.763 38.414 1.00 17.24 ? 314 LEU A O 1 ATOM 2402 C CB . LEU A 1 314 ? -54.859 14.893 40.030 1.00 17.42 ? 314 LEU A CB 1 ATOM 2403 C CG . LEU A 1 314 ? -55.520 15.900 40.967 1.00 17.82 ? 314 LEU A CG 1 ATOM 2404 C CD1 . LEU A 1 314 ? -54.443 16.673 41.747 1.00 18.07 ? 314 LEU A CD1 1 ATOM 2405 C CD2 . LEU A 1 314 ? -56.434 16.846 40.182 1.00 18.58 ? 314 LEU A CD2 1 ATOM 2406 N N . LYS A 1 315 ? -55.548 13.175 37.022 1.00 17.39 ? 315 LYS A N 1 ATOM 2407 C CA A LYS A 1 315 ? -54.930 12.463 35.914 0.50 18.21 ? 315 LYS A CA 1 ATOM 2408 C CA B LYS A 1 315 ? -54.934 12.457 35.917 0.50 18.15 ? 315 LYS A CA 1 ATOM 2409 C C . LYS A 1 315 ? -54.124 13.392 35.012 1.00 17.80 ? 315 LYS A C 1 ATOM 2410 O O . LYS A 1 315 ? -54.657 14.362 34.483 1.00 17.61 ? 315 LYS A O 1 ATOM 2411 C CB A LYS A 1 315 ? -56.011 11.747 35.101 0.50 19.06 ? 315 LYS A CB 1 ATOM 2412 C CB B LYS A 1 315 ? -56.024 11.724 35.120 0.50 18.90 ? 315 LYS A CB 1 ATOM 2413 C CG A LYS A 1 315 ? -56.665 10.615 35.878 0.50 20.27 ? 315 LYS A CG 1 ATOM 2414 C CG B LYS A 1 315 ? -56.625 10.542 35.881 0.50 19.99 ? 315 LYS A CG 1 ATOM 2415 C CD A LYS A 1 315 ? -55.698 9.469 36.113 0.50 20.92 ? 315 LYS A CD 1 ATOM 2416 C CD B LYS A 1 315 ? -58.018 10.173 35.372 0.50 20.53 ? 315 LYS A CD 1 ATOM 2417 C CE A LYS A 1 315 ? -55.820 8.421 35.010 0.50 21.95 ? 315 LYS A CE 1 ATOM 2418 C CE B LYS A 1 315 ? -58.646 9.050 36.201 0.50 21.63 ? 315 LYS A CE 1 ATOM 2419 N NZ A LYS A 1 315 ? -54.620 7.530 34.974 0.50 22.98 ? 315 LYS A NZ 1 ATOM 2420 N NZ B LYS A 1 315 ? -59.428 9.508 37.395 0.50 21.62 ? 315 LYS A NZ 1 ATOM 2421 N N . LEU A 1 316 ? -52.841 13.073 34.836 1.00 17.60 ? 316 LEU A N 1 ATOM 2422 C CA . LEU A 1 316 ? -51.934 13.824 33.985 1.00 17.30 ? 316 LEU A CA 1 ATOM 2423 C C . LEU A 1 316 ? -51.918 13.153 32.614 1.00 17.71 ? 316 LEU A C 1 ATOM 2424 O O . LEU A 1 316 ? -51.564 11.968 32.507 1.00 17.66 ? 316 LEU A O 1 ATOM 2425 C CB . LEU A 1 316 ? -50.515 13.772 34.568 1.00 17.65 ? 316 LEU A CB 1 ATOM 2426 C CG . LEU A 1 316 ? -49.414 14.529 33.844 1.00 17.84 ? 316 LEU A CG 1 ATOM 2427 C CD1 . LEU A 1 316 ? -49.559 16.037 34.046 1.00 17.60 ? 316 LEU A CD1 1 ATOM 2428 C CD2 . LEU A 1 316 ? -48.027 14.033 34.297 1.00 18.77 ? 316 LEU A CD2 1 ATOM 2429 N N . ALA A 1 317 ? -52.289 13.899 31.583 1.00 17.62 ? 317 ALA A N 1 ATOM 2430 C CA . ALA A 1 317 ? -52.195 13.383 30.210 1.00 18.11 ? 317 ALA A CA 1 ATOM 2431 C C . ALA A 1 317 ? -50.760 12.997 29.867 1.00 18.50 ? 317 ALA A C 1 ATOM 2432 O O . ALA A 1 317 ? -49.827 13.764 30.137 1.00 19.00 ? 317 ALA A O 1 ATOM 2433 C CB . ALA A 1 317 ? -52.710 14.417 29.215 1.00 17.80 ? 317 ALA A CB 1 ATOM 2434 N N . THR A 1 318 ? -50.587 11.809 29.271 1.00 18.98 ? 318 THR A N 1 ATOM 2435 C CA . THR A 1 318 ? -49.290 11.368 28.773 1.00 19.60 ? 318 THR A CA 1 ATOM 2436 C C . THR A 1 318 ? -49.358 10.991 27.291 1.00 20.32 ? 318 THR A C 1 ATOM 2437 O O . THR A 1 318 ? -48.506 10.272 26.792 1.00 21.94 ? 318 THR A O 1 ATOM 2438 C CB . THR A 1 318 ? -48.706 10.203 29.589 1.00 19.83 ? 318 THR A CB 1 ATOM 2439 O OG1 . THR A 1 318 ? -49.624 9.106 29.592 1.00 20.50 ? 318 THR A OG1 1 ATOM 2440 C CG2 . THR A 1 318 ? -48.381 10.659 31.052 1.00 19.63 ? 318 THR A CG2 1 ATOM 2441 N N . GLY A 1 319 ? -50.359 11.512 26.606 1.00 20.30 ? 319 GLY A N 1 ATOM 2442 C CA . GLY A 1 319 ? -50.483 11.344 25.169 1.00 21.11 ? 319 GLY A CA 1 ATOM 2443 C C . GLY A 1 319 ? -51.395 12.418 24.630 1.00 20.83 ? 319 GLY A C 1 ATOM 2444 O O . GLY A 1 319 ? -51.935 13.256 25.392 1.00 20.95 ? 319 GLY A O 1 ATOM 2445 N N . MET A 1 320 ? -51.559 12.412 23.311 1.00 20.24 ? 320 MET A N 1 ATOM 2446 C CA . MET A 1 320 ? -52.328 13.424 22.617 1.00 20.26 ? 320 MET A CA 1 ATOM 2447 C C . MET A 1 320 ? -53.834 13.184 22.717 1.00 20.45 ? 320 MET A C 1 ATOM 2448 O O . MET A 1 320 ? -54.283 12.157 23.234 1.00 21.68 ? 320 MET A O 1 ATOM 2449 C CB . MET A 1 320 ? -51.913 13.472 21.143 1.00 20.18 ? 320 MET A CB 1 ATOM 2450 C CG . MET A 1 320 ? -52.290 12.213 20.375 1.00 20.36 ? 320 MET A CG 1 ATOM 2451 S SD . MET A 1 320 ? -51.778 12.324 18.652 1.00 21.00 ? 320 MET A SD 1 ATOM 2452 C CE . MET A 1 320 ? -50.053 11.984 18.853 1.00 20.40 ? 320 MET A CE 1 ATOM 2453 N N . ARG A 1 321 ? -54.614 14.128 22.206 1.00 21.18 ? 321 ARG A N 1 ATOM 2454 C CA . ARG A 1 321 ? -56.053 13.938 22.091 1.00 22.47 ? 321 ARG A CA 1 ATOM 2455 C C . ARG A 1 321 ? -56.326 12.636 21.334 1.00 22.81 ? 321 ARG A C 1 ATOM 2456 O O . ARG A 1 321 ? -55.624 12.316 20.355 1.00 21.50 ? 321 ARG A O 1 ATOM 2457 C CB . ARG A 1 321 ? -56.742 15.107 21.388 1.00 24.34 ? 321 ARG A CB 1 ATOM 2458 C CG . ARG A 1 321 ? -56.278 15.321 19.953 1.00 26.99 ? 321 ARG A CG 1 ATOM 2459 C CD . ARG A 1 321 ? -57.017 16.434 19.238 1.00 29.66 ? 321 ARG A CD 1 ATOM 2460 N NE . ARG A 1 321 ? -56.608 17.765 19.681 1.00 30.01 ? 321 ARG A NE 1 ATOM 2461 C CZ . ARG A 1 321 ? -57.325 18.575 20.455 1.00 31.12 ? 321 ARG A CZ 1 ATOM 2462 N NH1 . ARG A 1 321 ? -58.512 18.210 20.929 1.00 32.95 ? 321 ARG A NH1 1 ATOM 2463 N NH2 . ARG A 1 321 ? -56.843 19.774 20.759 1.00 32.50 ? 321 ARG A NH2 1 ATOM 2464 N N . ASN A 1 322 ? -57.312 11.889 21.815 1.00 22.59 ? 322 ASN A N 1 ATOM 2465 C CA . ASN A 1 322 ? -57.697 10.619 21.193 1.00 24.09 ? 322 ASN A CA 1 ATOM 2466 C C . ASN A 1 322 ? -58.922 10.869 20.340 1.00 24.70 ? 322 ASN A C 1 ATOM 2467 O O . ASN A 1 322 ? -59.962 11.291 20.848 1.00 23.43 ? 322 ASN A O 1 ATOM 2468 C CB . ASN A 1 322 ? -58.016 9.568 22.230 1.00 24.41 ? 322 ASN A CB 1 ATOM 2469 C CG . ASN A 1 322 ? -57.993 8.163 21.654 1.00 24.76 ? 322 ASN A CG 1 ATOM 2470 O OD1 . ASN A 1 322 ? -57.088 7.795 20.891 1.00 24.25 ? 322 ASN A OD1 1 ATOM 2471 N ND2 . ASN A 1 322 ? -58.971 7.362 22.044 1.00 25.13 ? 322 ASN A ND2 1 ATOM 2472 N N . VAL A 1 323 ? -58.791 10.627 19.039 1.00 26.45 ? 323 VAL A N 1 ATOM 2473 C CA . VAL A 1 323 ? -59.829 11.013 18.094 1.00 28.09 ? 323 VAL A CA 1 ATOM 2474 C C . VAL A 1 323 ? -60.186 9.768 17.276 1.00 30.58 ? 323 VAL A C 1 ATOM 2475 O O . VAL A 1 323 ? -59.330 9.206 16.606 1.00 30.35 ? 323 VAL A O 1 ATOM 2476 C CB . VAL A 1 323 ? -59.369 12.162 17.153 1.00 28.41 ? 323 VAL A CB 1 ATOM 2477 C CG1 . VAL A 1 323 ? -60.520 12.620 16.277 1.00 29.14 ? 323 VAL A CG1 1 ATOM 2478 C CG2 . VAL A 1 323 ? -58.826 13.352 17.940 1.00 28.67 ? 323 VAL A CG2 1 ATOM 2479 N N . PRO A 1 324 ? -61.449 9.335 17.335 1.00 35.11 ? 324 PRO A N 1 ATOM 2480 C CA . PRO A 1 324 ? -61.857 8.152 16.542 1.00 36.64 ? 324 PRO A CA 1 ATOM 2481 C C . PRO A 1 324 ? -61.563 8.291 15.044 1.00 37.45 ? 324 PRO A C 1 ATOM 2482 O O . PRO A 1 324 ? -61.521 9.410 14.515 1.00 36.96 ? 324 PRO A O 1 ATOM 2483 C CB . PRO A 1 324 ? -63.366 8.098 16.764 1.00 37.68 ? 324 PRO A CB 1 ATOM 2484 C CG . PRO A 1 324 ? -63.751 9.514 16.997 1.00 38.07 ? 324 PRO A CG 1 ATOM 2485 C CD . PRO A 1 324 ? -62.621 10.097 17.810 1.00 36.77 ? 324 PRO A CD 1 ATOM 2486 N N . GLU A 1 325 ? -61.344 7.164 14.369 1.00 40.04 ? 325 GLU A N 1 ATOM 2487 C CA . GLU A 1 325 ? -61.185 7.178 12.915 1.00 42.06 ? 325 GLU A CA 1 ATOM 2488 C C . GLU A 1 325 ? -62.550 7.225 12.227 1.00 46.24 ? 325 GLU A C 1 ATOM 2489 O O . GLU A 1 325 ? -63.450 6.471 12.584 1.00 47.81 ? 325 GLU A O 1 ATOM 2490 C CB . GLU A 1 325 ? -60.409 5.953 12.443 1.00 41.57 ? 325 GLU A CB 1 ATOM 2491 C CG . GLU A 1 325 ? -59.936 6.072 10.995 1.00 40.38 ? 325 GLU A CG 1 ATOM 2492 C CD . GLU A 1 325 ? -58.713 5.231 10.715 1.00 39.95 ? 325 GLU A CD 1 ATOM 2493 O OE1 . GLU A 1 325 ? -58.361 4.390 11.574 1.00 39.91 ? 325 GLU A OE1 1 ATOM 2494 O OE2 . GLU A 1 325 ? -58.103 5.413 9.633 1.00 39.39 ? 325 GLU A OE2 1 ATOM 2495 N N . LYS A 1 326 ? -62.703 8.119 11.253 1.00 50.75 ? 326 LYS A N 1 ATOM 2496 C CA . LYS A 1 326 ? -63.933 8.180 10.455 1.00 56.07 ? 326 LYS A CA 1 ATOM 2497 C C . LYS A 1 326 ? -64.015 6.950 9.548 1.00 58.97 ? 326 LYS A C 1 ATOM 2498 O O . LYS A 1 326 ? -63.002 6.522 8.993 1.00 58.00 ? 326 LYS A O 1 ATOM 2499 C CB . LYS A 1 326 ? -63.970 9.463 9.624 1.00 57.02 ? 326 LYS A CB 1 ATOM 2500 C CG . LYS A 1 326 ? -64.037 10.730 10.459 1.00 58.00 ? 326 LYS A CG 1 ATOM 2501 C CD . LYS A 1 326 ? -64.598 11.894 9.653 1.00 60.27 ? 326 LYS A CD 1 ATOM 2502 C CE . LYS A 1 326 ? -64.647 13.182 10.465 1.00 60.63 ? 326 LYS A CE 1 ATOM 2503 N NZ . LYS A 1 326 ? -65.447 14.245 9.797 1.00 61.89 ? 326 LYS A NZ 1 ATOM 2504 N N . GLN A 1 327 ? -65.213 6.377 9.412 1.00 64.49 ? 327 GLN A N 1 ATOM 2505 C CA . GLN A 1 327 ? -65.408 5.135 8.642 1.00 67.59 ? 327 GLN A CA 1 ATOM 2506 C C . GLN A 1 327 ? -65.258 5.351 7.137 1.00 67.54 ? 327 GLN A C 1 ATOM 2507 O O . GLN A 1 327 ? -65.787 6.314 6.584 1.00 65.93 ? 327 GLN A O 1 ATOM 2508 C CB . GLN A 1 327 ? -66.785 4.528 8.929 1.00 71.00 ? 327 GLN A CB 1 ATOM 2509 C CG . GLN A 1 327 ? -67.022 4.154 10.388 1.00 72.60 ? 327 GLN A CG 1 ATOM 2510 C CD . GLN A 1 327 ? -68.264 3.296 10.586 1.00 74.26 ? 327 GLN A CD 1 ATOM 2511 O OE1 . GLN A 1 327 ? -69.111 3.175 9.693 1.00 74.22 ? 327 GLN A OE1 1 ATOM 2512 N NE2 . GLN A 1 327 ? -68.375 2.688 11.762 1.00 74.76 ? 327 GLN A NE2 1 ATOM 2513 N N . ALA A 1 334 ? -61.180 6.300 0.147 1.00 49.38 ? 334 ALA A N 1 ATOM 2514 C CA . ALA A 1 334 ? -60.133 7.315 0.023 1.00 45.72 ? 334 ALA A CA 1 ATOM 2515 C C . ALA A 1 334 ? -59.471 7.552 1.388 1.00 44.12 ? 334 ALA A C 1 ATOM 2516 O O . ALA A 1 334 ? -60.163 7.805 2.376 1.00 46.79 ? 334 ALA A O 1 ATOM 2517 C CB . ALA A 1 334 ? -60.711 8.615 -0.528 1.00 46.90 ? 334 ALA A CB 1 ATOM 2518 N N . ILE A 1 335 ? -58.140 7.465 1.438 1.00 38.51 ? 335 ILE A N 1 ATOM 2519 C CA . ILE A 1 335 ? -57.395 7.776 2.663 1.00 33.75 ? 335 ILE A CA 1 ATOM 2520 C C . ILE A 1 335 ? -57.675 9.210 3.104 1.00 31.77 ? 335 ILE A C 1 ATOM 2521 O O . ILE A 1 335 ? -58.124 10.036 2.319 1.00 31.81 ? 335 ILE A O 1 ATOM 2522 C CB . ILE A 1 335 ? -55.877 7.558 2.503 1.00 32.33 ? 335 ILE A CB 1 ATOM 2523 C CG1 . ILE A 1 335 ? -55.320 8.326 1.293 1.00 32.20 ? 335 ILE A CG1 1 ATOM 2524 C CG2 . ILE A 1 335 ? -55.561 6.071 2.383 1.00 33.21 ? 335 ILE A CG2 1 ATOM 2525 C CD1 . ILE A 1 335 ? -53.811 8.384 1.270 1.00 31.93 ? 335 ILE A CD1 1 ATOM 2526 N N . ALA A 1 336 ? -57.401 9.504 4.367 1.00 30.10 ? 336 ALA A N 1 ATOM 2527 C CA . ALA A 1 336 ? -57.662 10.833 4.906 1.00 28.79 ? 336 ALA A CA 1 ATOM 2528 C C . ALA A 1 336 ? -56.694 11.154 6.028 1.00 27.77 ? 336 ALA A C 1 ATOM 2529 O O . ALA A 1 336 ? -56.151 10.258 6.667 1.00 27.61 ? 336 ALA A O 1 ATOM 2530 C CB . ALA A 1 336 ? -59.105 10.953 5.378 1.00 29.10 ? 336 ALA A CB 1 ATOM 2531 N N . GLY A 1 337 ? -56.477 12.448 6.237 1.00 26.94 ? 337 GLY A N 1 ATOM 2532 C CA . GLY A 1 337 ? -55.466 12.951 7.154 1.00 26.90 ? 337 GLY A CA 1 ATOM 2533 C C . GLY A 1 337 ? -56.062 13.349 8.487 1.00 26.52 ? 337 GLY A C 1 ATOM 2534 O O . GLY A 1 337 ? -57.210 13.019 8.783 1.00 25.84 ? 337 GLY A O 1 ATOM 2535 N N . PHE A 1 338 ? -55.292 14.105 9.262 1.00 26.19 ? 338 PHE A N 1 ATOM 2536 C CA . PHE A 1 338 ? -55.623 14.354 10.663 1.00 26.95 ? 338 PHE A CA 1 ATOM 2537 C C . PHE A 1 338 ? -56.845 15.230 10.933 1.00 27.93 ? 338 PHE A C 1 ATOM 2538 O O . PHE A 1 338 ? -57.273 15.294 12.071 1.00 28.03 ? 338 PHE A O 1 ATOM 2539 C CB . PHE A 1 338 ? -54.417 14.946 11.414 1.00 26.11 ? 338 PHE A CB 1 ATOM 2540 C CG . PHE A 1 338 ? -54.043 16.337 10.984 1.00 26.29 ? 338 PHE A CG 1 ATOM 2541 C CD1 . PHE A 1 338 ? -53.183 16.545 9.923 1.00 26.49 ? 338 PHE A CD1 1 ATOM 2542 C CD2 . PHE A 1 338 ? -54.522 17.446 11.670 1.00 27.39 ? 338 PHE A CD2 1 ATOM 2543 C CE1 . PHE A 1 338 ? -52.836 17.820 9.528 1.00 27.23 ? 338 PHE A CE1 1 ATOM 2544 C CE2 . PHE A 1 338 ? -54.167 18.729 11.285 1.00 27.41 ? 338 PHE A CE2 1 ATOM 2545 C CZ . PHE A 1 338 ? -53.322 18.916 10.210 1.00 27.85 ? 338 PHE A CZ 1 ATOM 2546 N N . ILE A 1 339 ? -57.384 15.929 9.938 1.00 29.73 ? 339 ILE A N 1 ATOM 2547 C CA . ILE A 1 339 ? -58.499 16.850 10.203 1.00 32.63 ? 339 ILE A CA 1 ATOM 2548 C C . ILE A 1 339 ? -59.716 16.038 10.708 1.00 34.33 ? 339 ILE A C 1 ATOM 2549 O O . ILE A 1 339 ? -60.271 15.204 9.999 1.00 33.59 ? 339 ILE A O 1 ATOM 2550 C CB . ILE A 1 339 ? -58.846 17.734 8.979 1.00 32.66 ? 339 ILE A CB 1 ATOM 2551 C CG1 . ILE A 1 339 ? -57.650 18.605 8.589 1.00 32.30 ? 339 ILE A CG1 1 ATOM 2552 C CG2 . ILE A 1 339 ? -60.059 18.615 9.266 1.00 34.68 ? 339 ILE A CG2 1 ATOM 2553 C CD1 . ILE A 1 339 ? -57.279 19.664 9.602 1.00 31.79 ? 339 ILE A CD1 1 ATOM 2554 N N . GLU A 1 340 ? -60.053 16.243 11.981 1.00 38.41 ? 340 GLU A N 1 ATOM 2555 C CA . GLU A 1 340 ? -61.125 15.503 12.671 1.00 40.99 ? 340 GLU A CA 1 ATOM 2556 C C . GLU A 1 340 ? -61.020 13.978 12.536 1.00 38.55 ? 340 GLU A C 1 ATOM 2557 O O . GLU A 1 340 ? -62.021 13.312 12.369 1.00 37.39 ? 340 GLU A O 1 ATOM 2558 C CB . GLU A 1 340 ? -62.505 15.968 12.168 1.00 45.64 ? 340 GLU A CB 1 ATOM 2559 C CG . GLU A 1 340 ? -62.813 17.437 12.414 1.00 51.14 ? 340 GLU A CG 1 ATOM 2560 C CD . GLU A 1 340 ? -62.821 17.793 13.888 1.00 56.30 ? 340 GLU A CD 1 ATOM 2561 O OE1 . GLU A 1 340 ? -63.396 17.021 14.693 1.00 62.96 ? 340 GLU A OE1 1 ATOM 2562 O OE2 . GLU A 1 340 ? -62.252 18.848 14.246 1.00 61.59 ? 340 GLU A OE2 1 ATOM 2563 N N . ASN A 1 341 ? -59.816 13.418 12.644 1.00 37.36 ? 341 ASN A N 1 ATOM 2564 C CA . ASN A 1 341 ? -59.616 12.014 12.287 1.00 34.23 ? 341 ASN A CA 1 ATOM 2565 C C . ASN A 1 341 ? -58.299 11.437 12.803 1.00 33.12 ? 341 ASN A C 1 ATOM 2566 O O . ASN A 1 341 ? -57.240 11.920 12.433 1.00 34.98 ? 341 ASN A O 1 ATOM 2567 C CB . ASN A 1 341 ? -59.651 11.916 10.762 1.00 35.10 ? 341 ASN A CB 1 ATOM 2568 C CG . ASN A 1 341 ? -59.515 10.489 10.256 1.00 34.36 ? 341 ASN A CG 1 ATOM 2569 O OD1 . ASN A 1 341 ? -60.269 9.593 10.676 1.00 33.05 ? 341 ASN A OD1 1 ATOM 2570 N ND2 . ASN A 1 341 ? -58.546 10.268 9.350 1.00 31.99 ? 341 ASN A ND2 1 ATOM 2571 N N . GLY A 1 342 ? -58.362 10.435 13.676 1.00 30.19 ? 342 GLY A N 1 ATOM 2572 C CA . GLY A 1 342 ? -57.169 9.709 14.097 1.00 29.43 ? 342 GLY A CA 1 ATOM 2573 C C . GLY A 1 342 ? -57.017 8.368 13.403 1.00 28.97 ? 342 GLY A C 1 ATOM 2574 O O . GLY A 1 342 ? -57.974 7.858 12.829 1.00 29.53 ? 342 GLY A O 1 ATOM 2575 N N . TRP A 1 343 ? -55.822 7.787 13.487 1.00 27.69 ? 343 TRP A N 1 ATOM 2576 C CA . TRP A 1 343 ? -55.509 6.525 12.823 1.00 27.72 ? 343 TRP A CA 1 ATOM 2577 C C . TRP A 1 343 ? -55.260 5.426 13.816 1.00 29.54 ? 343 TRP A C 1 ATOM 2578 O O . TRP A 1 343 ? -54.164 5.307 14.369 1.00 27.92 ? 343 TRP A O 1 ATOM 2579 C CB . TRP A 1 343 ? -54.267 6.688 11.961 1.00 25.88 ? 343 TRP A CB 1 ATOM 2580 C CG . TRP A 1 343 ? -54.386 7.599 10.760 1.00 24.74 ? 343 TRP A CG 1 ATOM 2581 C CD1 . TRP A 1 343 ? -55.535 8.084 10.139 1.00 24.37 ? 343 TRP A CD1 1 ATOM 2582 C CD2 . TRP A 1 343 ? -53.278 8.121 9.972 1.00 24.34 ? 343 TRP A CD2 1 ATOM 2583 N NE1 . TRP A 1 343 ? -55.214 8.863 9.044 1.00 23.68 ? 343 TRP A NE1 1 ATOM 2584 C CE2 . TRP A 1 343 ? -53.870 8.923 8.897 1.00 23.94 ? 343 TRP A CE2 1 ATOM 2585 C CE3 . TRP A 1 343 ? -51.902 8.017 10.056 1.00 24.34 ? 343 TRP A CE3 1 ATOM 2586 C CZ2 . TRP A 1 343 ? -53.095 9.574 7.965 1.00 23.95 ? 343 TRP A CZ2 1 ATOM 2587 C CZ3 . TRP A 1 343 ? -51.127 8.684 9.111 1.00 24.57 ? 343 TRP A CZ3 1 ATOM 2588 C CH2 . TRP A 1 343 ? -51.711 9.434 8.086 1.00 24.33 ? 343 TRP A CH2 1 ATOM 2589 N N . GLU A 1 344 ? -56.266 4.595 14.063 1.00 33.75 ? 344 GLU A N 1 ATOM 2590 C CA . GLU A 1 344 ? -56.091 3.490 15.014 1.00 36.32 ? 344 GLU A CA 1 ATOM 2591 C C . GLU A 1 344 ? -55.079 2.450 14.537 1.00 37.48 ? 344 GLU A C 1 ATOM 2592 O O . GLU A 1 344 ? -54.355 1.860 15.343 1.00 37.60 ? 344 GLU A O 1 ATOM 2593 C CB . GLU A 1 344 ? -57.442 2.874 15.383 1.00 40.34 ? 344 GLU A CB 1 ATOM 2594 C CG . GLU A 1 344 ? -58.239 3.798 16.302 1.00 43.15 ? 344 GLU A CG 1 ATOM 2595 C CD . GLU A 1 344 ? -59.657 3.331 16.580 1.00 48.11 ? 344 GLU A CD 1 ATOM 2596 O OE1 . GLU A 1 344 ? -59.813 2.223 17.148 1.00 50.92 ? 344 GLU A OE1 1 ATOM 2597 O OE2 . GLU A 1 344 ? -60.608 4.088 16.247 1.00 49.24 ? 344 GLU A OE2 1 ATOM 2598 N N . GLY A 1 345 ? -54.972 2.278 13.223 1.00 37.38 ? 345 GLY A N 1 ATOM 2599 C CA . GLY A 1 345 ? -53.957 1.395 12.647 1.00 37.59 ? 345 GLY A CA 1 ATOM 2600 C C . GLY A 1 345 ? -52.515 1.853 12.720 1.00 37.98 ? 345 GLY A C 1 ATOM 2601 O O . GLY A 1 345 ? -51.626 1.112 12.320 1.00 37.33 ? 345 GLY A O 1 ATOM 2602 N N . MET A 1 346 ? -52.262 3.064 13.224 1.00 37.64 ? 346 MET A N 1 ATOM 2603 C CA . MET A 1 346 ? -50.897 3.602 13.321 1.00 38.30 ? 346 MET A CA 1 ATOM 2604 C C . MET A 1 346 ? -50.323 3.222 14.687 1.00 38.98 ? 346 MET A C 1 ATOM 2605 O O . MET A 1 346 ? -50.580 3.898 15.682 1.00 37.44 ? 346 MET A O 1 ATOM 2606 C CB . MET A 1 346 ? -50.935 5.132 13.096 1.00 39.54 ? 346 MET A CB 1 ATOM 2607 C CG . MET A 1 346 ? -49.705 5.960 13.448 1.00 41.18 ? 346 MET A CG 1 ATOM 2608 S SD . MET A 1 346 ? -48.641 6.400 12.061 1.00 46.06 ? 346 MET A SD 1 ATOM 2609 C CE . MET A 1 346 ? -47.367 5.177 12.319 1.00 45.78 ? 346 MET A CE 1 ATOM 2610 N N . VAL A 1 347 ? -49.548 2.141 14.730 1.00 38.81 ? 347 VAL A N 1 ATOM 2611 C CA . VAL A 1 347 ? -49.105 1.554 15.997 1.00 39.42 ? 347 VAL A CA 1 ATOM 2612 C C . VAL A 1 347 ? -47.591 1.594 16.253 1.00 39.46 ? 347 VAL A C 1 ATOM 2613 O O . VAL A 1 347 ? -47.151 1.248 17.350 1.00 42.08 ? 347 VAL A O 1 ATOM 2614 C CB . VAL A 1 347 ? -49.601 0.096 16.123 1.00 40.68 ? 347 VAL A CB 1 ATOM 2615 C CG1 . VAL A 1 347 ? -51.122 0.057 16.145 1.00 39.69 ? 347 VAL A CG1 1 ATOM 2616 C CG2 . VAL A 1 347 ? -49.050 -0.754 14.988 1.00 41.55 ? 347 VAL A CG2 1 ATOM 2617 N N . ASP A 1 348 ? -46.793 2.012 15.275 1.00 38.76 ? 348 ASP A N 1 ATOM 2618 C CA . ASP A 1 348 ? -45.339 2.113 15.464 1.00 38.76 ? 348 ASP A CA 1 ATOM 2619 C C . ASP A 1 348 ? -44.852 3.563 15.505 1.00 36.24 ? 348 ASP A C 1 ATOM 2620 O O . ASP A 1 348 ? -43.661 3.838 15.431 1.00 36.90 ? 348 ASP A O 1 ATOM 2621 C CB . ASP A 1 348 ? -44.598 1.326 14.380 1.00 42.26 ? 348 ASP A CB 1 ATOM 2622 C CG . ASP A 1 348 ? -44.800 1.896 12.989 1.00 45.22 ? 348 ASP A CG 1 ATOM 2623 O OD1 . ASP A 1 348 ? -45.857 2.531 12.733 1.00 46.61 ? 348 ASP A OD1 1 ATOM 2624 O OD2 . ASP A 1 348 ? -43.894 1.688 12.147 1.00 48.53 ? 348 ASP A OD2 1 ATOM 2625 N N . GLY A 1 349 ? -45.789 4.490 15.627 1.00 33.57 ? 349 GLY A N 1 ATOM 2626 C CA . GLY A 1 349 ? -45.454 5.901 15.741 1.00 31.12 ? 349 GLY A CA 1 ATOM 2627 C C . GLY A 1 349 ? -46.665 6.663 16.227 1.00 28.16 ? 349 GLY A C 1 ATOM 2628 O O . GLY A 1 349 ? -47.781 6.134 16.233 1.00 28.20 ? 349 GLY A O 1 ATOM 2629 N N . TRP A 1 350 ? -46.447 7.910 16.632 1.00 25.83 ? 350 TRP A N 1 ATOM 2630 C CA . TRP A 1 350 ? -47.538 8.783 17.032 1.00 24.33 ? 350 TRP A CA 1 ATOM 2631 C C . TRP A 1 350 ? -48.040 9.628 15.915 1.00 22.72 ? 350 TRP A C 1 ATOM 2632 O O . TRP A 1 350 ? -49.185 10.059 15.947 1.00 22.04 ? 350 TRP A O 1 ATOM 2633 C CB . TRP A 1 350 ? -47.072 9.706 18.145 1.00 24.74 ? 350 TRP A CB 1 ATOM 2634 C CG . TRP A 1 350 ? -47.033 9.044 19.495 1.00 25.28 ? 350 TRP A CG 1 ATOM 2635 C CD1 . TRP A 1 350 ? -46.965 7.690 19.790 1.00 26.57 ? 350 TRP A CD1 1 ATOM 2636 C CD2 . TRP A 1 350 ? -47.043 9.719 20.787 1.00 25.05 ? 350 TRP A CD2 1 ATOM 2637 N NE1 . TRP A 1 350 ? -46.953 7.484 21.145 1.00 26.81 ? 350 TRP A NE1 1 ATOM 2638 C CE2 . TRP A 1 350 ? -46.977 8.667 21.799 1.00 25.75 ? 350 TRP A CE2 1 ATOM 2639 C CE3 . TRP A 1 350 ? -47.099 11.038 21.187 1.00 25.49 ? 350 TRP A CE3 1 ATOM 2640 C CZ2 . TRP A 1 350 ? -46.985 8.952 23.152 1.00 25.63 ? 350 TRP A CZ2 1 ATOM 2641 C CZ3 . TRP A 1 350 ? -47.091 11.319 22.561 1.00 25.20 ? 350 TRP A CZ3 1 ATOM 2642 C CH2 . TRP A 1 350 ? -47.038 10.295 23.512 1.00 25.17 ? 350 TRP A CH2 1 ATOM 2643 N N . TYR A 1 351 ? -47.154 9.942 14.970 1.00 22.54 ? 351 TYR A N 1 ATOM 2644 C CA . TYR A 1 351 ? -47.474 10.735 13.791 1.00 22.13 ? 351 TYR A CA 1 ATOM 2645 C C . TYR A 1 351 ? -46.917 10.012 12.583 1.00 22.80 ? 351 TYR A C 1 ATOM 2646 O O . TYR A 1 351 ? -45.964 9.243 12.711 1.00 23.32 ? 351 TYR A O 1 ATOM 2647 C CB . TYR A 1 351 ? -46.803 12.091 13.844 1.00 22.28 ? 351 TYR A CB 1 ATOM 2648 C CG . TYR A 1 351 ? -47.087 12.853 15.126 1.00 22.11 ? 351 TYR A CG 1 ATOM 2649 C CD1 . TYR A 1 351 ? -48.199 13.657 15.225 1.00 22.02 ? 351 TYR A CD1 1 ATOM 2650 C CD2 . TYR A 1 351 ? -46.243 12.742 16.235 1.00 22.32 ? 351 TYR A CD2 1 ATOM 2651 C CE1 . TYR A 1 351 ? -48.472 14.358 16.402 1.00 22.08 ? 351 TYR A CE1 1 ATOM 2652 C CE2 . TYR A 1 351 ? -46.507 13.445 17.413 1.00 22.26 ? 351 TYR A CE2 1 ATOM 2653 C CZ . TYR A 1 351 ? -47.624 14.240 17.480 1.00 22.01 ? 351 TYR A CZ 1 ATOM 2654 O OH . TYR A 1 351 ? -47.900 14.943 18.630 1.00 22.65 ? 351 TYR A OH 1 ATOM 2655 N N . GLY A 1 352 ? -47.496 10.255 11.422 1.00 22.94 ? 352 GLY A N 1 ATOM 2656 C CA . GLY A 1 352 ? -46.939 9.658 10.203 1.00 23.61 ? 352 GLY A CA 1 ATOM 2657 C C . GLY A 1 352 ? -47.628 10.080 8.933 1.00 23.75 ? 352 GLY A C 1 ATOM 2658 O O . GLY A 1 352 ? -48.370 11.064 8.903 1.00 22.66 ? 352 GLY A O 1 ATOM 2659 N N . PHE A 1 353 ? -47.361 9.300 7.888 1.00 24.31 ? 353 PHE A N 1 ATOM 2660 C CA . PHE A 1 353 ? -47.794 9.576 6.528 1.00 24.81 ? 353 PHE A CA 1 ATOM 2661 C C . PHE A 1 353 ? -48.590 8.383 6.022 1.00 24.93 ? 353 PHE A C 1 ATOM 2662 O O . PHE A 1 353 ? -48.230 7.235 6.303 1.00 25.25 ? 353 PHE A O 1 ATOM 2663 C CB . PHE A 1 353 ? -46.580 9.714 5.616 1.00 25.54 ? 353 PHE A CB 1 ATOM 2664 C CG . PHE A 1 353 ? -45.632 10.823 5.980 1.00 26.26 ? 353 PHE A CG 1 ATOM 2665 C CD1 . PHE A 1 353 ? -44.570 10.602 6.842 1.00 27.01 ? 353 PHE A CD1 1 ATOM 2666 C CD2 . PHE A 1 353 ? -45.753 12.070 5.389 1.00 26.76 ? 353 PHE A CD2 1 ATOM 2667 C CE1 . PHE A 1 353 ? -43.674 11.619 7.151 1.00 27.22 ? 353 PHE A CE1 1 ATOM 2668 C CE2 . PHE A 1 353 ? -44.855 13.078 5.680 1.00 27.41 ? 353 PHE A CE2 1 ATOM 2669 C CZ . PHE A 1 353 ? -43.814 12.857 6.558 1.00 27.16 ? 353 PHE A CZ 1 ATOM 2670 N N . ARG A 1 354 ? -49.670 8.652 5.298 1.00 24.58 ? 354 ARG A N 1 ATOM 2671 C CA . ARG A 1 354 ? -50.317 7.643 4.451 1.00 25.36 ? 354 ARG A CA 1 ATOM 2672 C C . ARG A 1 354 ? -50.349 8.157 3.018 1.00 25.06 ? 354 ARG A C 1 ATOM 2673 O O . ARG A 1 354 ? -50.563 9.347 2.778 1.00 24.52 ? 354 ARG A O 1 ATOM 2674 C CB . ARG A 1 354 ? -51.733 7.351 4.901 1.00 25.71 ? 354 ARG A CB 1 ATOM 2675 C CG . ARG A 1 354 ? -51.807 6.396 6.069 1.00 26.97 ? 354 ARG A CG 1 ATOM 2676 C CD . ARG A 1 354 ? -53.241 6.095 6.452 1.00 27.24 ? 354 ARG A CD 1 ATOM 2677 N NE . ARG A 1 354 ? -53.271 5.258 7.641 1.00 28.07 ? 354 ARG A NE 1 ATOM 2678 C CZ . ARG A 1 354 ? -54.362 4.938 8.333 1.00 28.19 ? 354 ARG A CZ 1 ATOM 2679 N NH1 . ARG A 1 354 ? -55.554 5.378 7.975 1.00 28.51 ? 354 ARG A NH1 1 ATOM 2680 N NH2 . ARG A 1 354 ? -54.247 4.168 9.401 1.00 28.79 ? 354 ARG A NH2 1 ATOM 2681 N N . HIS A 1 355 ? -50.133 7.260 2.061 1.00 24.91 ? 355 HIS A N 1 ATOM 2682 C CA . HIS A 1 355 ? -50.063 7.668 0.677 1.00 25.12 ? 355 HIS A CA 1 ATOM 2683 C C . HIS A 1 355 ? -50.837 6.742 -0.185 1.00 26.00 ? 355 HIS A C 1 ATOM 2684 O O . HIS A 1 355 ? -51.098 5.596 0.201 1.00 25.15 ? 355 HIS A O 1 ATOM 2685 C CB . HIS A 1 355 ? -48.614 7.748 0.211 1.00 25.48 ? 355 HIS A CB 1 ATOM 2686 C CG . HIS A 1 355 ? -47.922 6.395 0.119 1.00 26.41 ? 355 HIS A CG 1 ATOM 2687 N ND1 . HIS A 1 355 ? -47.078 5.952 1.066 1.00 26.89 ? 355 HIS A ND1 1 ATOM 2688 C CD2 . HIS A 1 355 ? -47.994 5.388 -0.846 1.00 27.72 ? 355 HIS A CD2 1 ATOM 2689 C CE1 . HIS A 1 355 ? -46.624 4.723 0.720 1.00 27.78 ? 355 HIS A CE1 1 ATOM 2690 N NE2 . HIS A 1 355 ? -47.188 4.385 -0.445 1.00 27.75 ? 355 HIS A NE2 1 ATOM 2691 N N . GLN A 1 356 ? -51.258 7.268 -1.332 1.00 26.92 ? 356 GLN A N 1 ATOM 2692 C CA . GLN A 1 356 ? -51.832 6.492 -2.420 1.00 28.63 ? 356 GLN A CA 1 ATOM 2693 C C . GLN A 1 356 ? -51.121 6.899 -3.699 1.00 28.03 ? 356 GLN A C 1 ATOM 2694 O O . GLN A 1 356 ? -51.085 8.082 -4.048 1.00 27.04 ? 356 GLN A O 1 ATOM 2695 C CB . GLN A 1 356 ? -53.331 6.757 -2.575 1.00 31.47 ? 356 GLN A CB 1 ATOM 2696 C CG . GLN A 1 356 ? -53.967 5.931 -3.686 1.00 34.92 ? 356 GLN A CG 1 ATOM 2697 C CD . GLN A 1 356 ? -55.479 5.959 -3.667 1.00 38.07 ? 356 GLN A CD 1 ATOM 2698 O OE1 . GLN A 1 356 ? -56.130 4.969 -4.007 1.00 44.64 ? 356 GLN A OE1 1 ATOM 2699 N NE2 . GLN A 1 356 ? -56.048 7.093 -3.293 1.00 41.30 ? 356 GLN A NE2 1 ATOM 2700 N N . ASN A 1 357 ? -50.562 5.919 -4.400 1.00 27.62 ? 357 ASN A N 1 ATOM 2701 C CA . ASN A 1 357 ? -49.863 6.177 -5.638 1.00 27.73 ? 357 ASN A CA 1 ATOM 2702 C C . ASN A 1 357 ? -50.059 4.981 -6.559 1.00 29.47 ? 357 ASN A C 1 ATOM 2703 O O . ASN A 1 357 ? -50.904 4.128 -6.284 1.00 27.12 ? 357 ASN A O 1 ATOM 2704 C CB . ASN A 1 357 ? -48.381 6.476 -5.360 1.00 28.06 ? 357 ASN A CB 1 ATOM 2705 C CG . ASN A 1 357 ? -47.618 5.291 -4.768 1.00 27.74 ? 357 ASN A CG 1 ATOM 2706 O OD1 . ASN A 1 357 ? -48.128 4.157 -4.700 1.00 28.68 ? 357 ASN A OD1 1 ATOM 2707 N ND2 . ASN A 1 357 ? -46.378 5.542 -4.370 1.00 27.33 ? 357 ASN A ND2 1 ATOM 2708 N N . SER A 1 358 ? -49.291 4.950 -7.650 1.00 32.64 ? 358 SER A N 1 ATOM 2709 C CA . SER A 1 358 ? -49.293 3.852 -8.623 1.00 34.87 ? 358 SER A CA 1 ATOM 2710 C C . SER A 1 358 ? -49.055 2.465 -8.025 1.00 35.36 ? 358 SER A C 1 ATOM 2711 O O . SER A 1 358 ? -49.485 1.462 -8.607 1.00 38.07 ? 358 SER A O 1 ATOM 2712 C CB . SER A 1 358 ? -48.211 4.115 -9.700 1.00 36.82 ? 358 SER A CB 1 ATOM 2713 O OG . SER A 1 358 ? -46.994 4.609 -9.113 1.00 38.91 ? 358 SER A OG 1 ATOM 2714 N N . GLU A 1 359 ? -48.339 2.406 -6.907 1.00 34.42 ? 359 GLU A N 1 ATOM 2715 C CA . GLU A 1 359 ? -47.891 1.154 -6.315 1.00 34.67 ? 359 GLU A CA 1 ATOM 2716 C C . GLU A 1 359 ? -48.750 0.679 -5.132 1.00 33.89 ? 359 GLU A C 1 ATOM 2717 O O . GLU A 1 359 ? -48.473 -0.382 -4.567 1.00 33.86 ? 359 GLU A O 1 ATOM 2718 C CB . GLU A 1 359 ? -46.432 1.291 -5.876 1.00 36.05 ? 359 GLU A CB 1 ATOM 2719 C CG . GLU A 1 359 ? -45.510 1.793 -6.983 1.00 38.31 ? 359 GLU A CG 1 ATOM 2720 C CD . GLU A 1 359 ? -44.041 1.574 -6.687 1.00 40.55 ? 359 GLU A CD 1 ATOM 2721 O OE1 . GLU A 1 359 ? -43.566 0.429 -6.829 1.00 43.33 ? 359 GLU A OE1 1 ATOM 2722 O OE2 . GLU A 1 359 ? -43.341 2.537 -6.310 1.00 41.83 ? 359 GLU A OE2 1 ATOM 2723 N N . GLY A 1 360 ? -49.779 1.450 -4.761 1.00 31.20 ? 360 GLY A N 1 ATOM 2724 C CA . GLY A 1 360 ? -50.711 1.042 -3.709 1.00 29.98 ? 360 GLY A CA 1 ATOM 2725 C C . GLY A 1 360 ? -50.964 2.119 -2.665 1.00 28.91 ? 360 GLY A C 1 ATOM 2726 O O . GLY A 1 360 ? -50.803 3.301 -2.950 1.00 26.78 ? 360 GLY A O 1 ATOM 2727 N N . ILE A 1 361 ? -51.379 1.680 -1.478 1.00 28.54 ? 361 ILE A N 1 ATOM 2728 C CA . ILE A 1 361 ? -51.655 2.559 -0.332 1.00 29.68 ? 361 ILE A CA 1 ATOM 2729 C C . ILE A 1 361 ? -50.781 2.128 0.814 1.00 29.69 ? 361 ILE A C 1 ATOM 2730 O O . ILE A 1 361 ? -50.753 0.948 1.161 1.00 29.99 ? 361 ILE A O 1 ATOM 2731 C CB . ILE A 1 361 ? -53.130 2.495 0.078 1.00 30.79 ? 361 ILE A CB 1 ATOM 2732 C CG1 . ILE A 1 361 ? -53.973 3.133 -1.012 1.00 32.39 ? 361 ILE A CG1 1 ATOM 2733 C CG2 . ILE A 1 361 ? -53.365 3.233 1.403 1.00 32.33 ? 361 ILE A CG2 1 ATOM 2734 C CD1 . ILE A 1 361 ? -55.158 2.304 -1.422 1.00 33.85 ? 361 ILE A CD1 1 ATOM 2735 N N . GLY A 1 362 ? -50.044 3.072 1.389 1.00 28.54 ? 362 GLY A N 1 ATOM 2736 C CA . GLY A 1 362 ? -49.032 2.738 2.374 1.00 28.86 ? 362 GLY A CA 1 ATOM 2737 C C . GLY A 1 362 ? -49.066 3.678 3.559 1.00 29.10 ? 362 GLY A C 1 ATOM 2738 O O . GLY A 1 362 ? -49.697 4.739 3.499 1.00 27.28 ? 362 GLY A O 1 ATOM 2739 N N . GLN A 1 363 ? -48.385 3.258 4.621 1.00 29.59 ? 363 GLN A N 1 ATOM 2740 C CA . GLN A 1 363 ? -48.288 4.013 5.863 1.00 29.53 ? 363 GLN A CA 1 ATOM 2741 C C . GLN A 1 363 ? -46.866 3.928 6.371 1.00 29.53 ? 363 GLN A C 1 ATOM 2742 O O . GLN A 1 363 ? -46.219 2.881 6.257 1.00 28.96 ? 363 GLN A O 1 ATOM 2743 C CB . GLN A 1 363 ? -49.258 3.432 6.878 1.00 30.63 ? 363 GLN A CB 1 ATOM 2744 C CG . GLN A 1 363 ? -49.249 4.076 8.247 1.00 32.04 ? 363 GLN A CG 1 ATOM 2745 C CD . GLN A 1 363 ? -50.276 3.433 9.150 1.00 32.93 ? 363 GLN A CD 1 ATOM 2746 O OE1 . GLN A 1 363 ? -51.459 3.762 9.080 1.00 34.59 ? 363 GLN A OE1 1 ATOM 2747 N NE2 . GLN A 1 363 ? -49.834 2.480 9.980 1.00 33.97 ? 363 GLN A NE2 1 ATOM 2748 N N . ALA A 1 364 ? -46.368 5.034 6.923 1.00 27.95 ? 364 ALA A N 1 ATOM 2749 C CA . ALA A 1 364 ? -45.079 5.061 7.603 1.00 27.51 ? 364 ALA A CA 1 ATOM 2750 C C . ALA A 1 364 ? -45.135 6.068 8.754 1.00 27.94 ? 364 ALA A C 1 ATOM 2751 O O . ALA A 1 364 ? -45.704 7.170 8.611 1.00 25.43 ? 364 ALA A O 1 ATOM 2752 C CB . ALA A 1 364 ? -43.963 5.436 6.650 1.00 27.56 ? 364 ALA A CB 1 ATOM 2753 N N . ALA A 1 365 ? -44.535 5.678 9.872 1.00 28.95 ? 365 ALA A N 1 ATOM 2754 C CA . ALA A 1 365 ? -44.398 6.550 11.041 1.00 29.68 ? 365 ALA A CA 1 ATOM 2755 C C . ALA A 1 365 ? -43.316 7.583 10.809 1.00 30.59 ? 365 ALA A C 1 ATOM 2756 O O . ALA A 1 365 ? -42.341 7.298 10.128 1.00 30.93 ? 365 ALA A O 1 ATOM 2757 C CB . ALA A 1 365 ? -44.068 5.724 12.277 1.00 30.55 ? 365 ALA A CB 1 ATOM 2758 N N . ASP A 1 366 ? -43.488 8.784 11.373 1.00 29.74 ? 366 ASP A N 1 ATOM 2759 C CA . ASP A 1 366 ? -42.446 9.810 11.356 1.00 31.29 ? 366 ASP A CA 1 ATOM 2760 C C . ASP A 1 366 ? -41.770 9.820 12.722 1.00 33.03 ? 366 ASP A C 1 ATOM 2761 O O . ASP A 1 366 ? -42.395 10.165 13.730 1.00 30.69 ? 366 ASP A O 1 ATOM 2762 C CB . ASP A 1 366 ? -43.031 11.190 11.036 1.00 31.75 ? 366 ASP A CB 1 ATOM 2763 C CG . ASP A 1 366 ? -41.970 12.283 10.975 1.00 33.20 ? 366 ASP A CG 1 ATOM 2764 O OD1 . ASP A 1 366 ? -41.198 12.304 9.993 1.00 34.36 ? 366 ASP A OD1 1 ATOM 2765 O OD2 . ASP A 1 366 ? -41.906 13.132 11.901 1.00 32.66 ? 366 ASP A OD2 1 ATOM 2766 N N . LEU A 1 367 ? -40.495 9.436 12.750 1.00 34.13 ? 367 LEU A N 1 ATOM 2767 C CA . LEU A 1 367 ? -39.789 9.221 14.008 1.00 36.27 ? 367 LEU A CA 1 ATOM 2768 C C . LEU A 1 367 ? -39.552 10.527 14.746 1.00 36.00 ? 367 LEU A C 1 ATOM 2769 O O . LEU A 1 367 ? -39.756 10.588 15.956 1.00 35.79 ? 367 LEU A O 1 ATOM 2770 C CB . LEU A 1 367 ? -38.453 8.502 13.780 1.00 38.67 ? 367 LEU A CB 1 ATOM 2771 C CG . LEU A 1 367 ? -37.570 8.305 15.033 1.00 41.84 ? 367 LEU A CG 1 ATOM 2772 C CD1 . LEU A 1 367 ? -38.227 7.347 16.024 1.00 42.96 ? 367 LEU A CD1 1 ATOM 2773 C CD2 . LEU A 1 367 ? -36.179 7.813 14.638 1.00 44.45 ? 367 LEU A CD2 1 ATOM 2774 N N . LYS A 1 368 ? -39.128 11.561 14.025 1.00 35.99 ? 368 LYS A N 1 ATOM 2775 C CA . LYS A 1 368 ? -38.737 12.820 14.646 1.00 37.55 ? 368 LYS A CA 1 ATOM 2776 C C . LYS A 1 368 ? -39.874 13.442 15.447 1.00 36.10 ? 368 LYS A C 1 ATOM 2777 O O . LYS A 1 368 ? -39.676 13.855 16.603 1.00 34.08 ? 368 LYS A O 1 ATOM 2778 C CB . LYS A 1 368 ? -38.270 13.826 13.591 1.00 40.22 ? 368 LYS A CB 1 ATOM 2779 C CG . LYS A 1 368 ? -37.838 15.188 14.145 1.00 43.41 ? 368 LYS A CG 1 ATOM 2780 C CD . LYS A 1 368 ? -38.289 16.324 13.224 1.00 46.56 ? 368 LYS A CD 1 ATOM 2781 C CE . LYS A 1 368 ? -37.511 17.621 13.431 1.00 48.48 ? 368 LYS A CE 1 ATOM 2782 N NZ . LYS A 1 368 ? -37.587 18.475 12.204 1.00 49.91 ? 368 LYS A NZ 1 ATOM 2783 N N . SER A 1 369 ? -41.046 13.544 14.824 1.00 33.22 ? 369 SER A N 1 ATOM 2784 C CA . SER A 1 369 ? -42.209 14.171 15.472 1.00 31.91 ? 369 SER A CA 1 ATOM 2785 C C . SER A 1 369 ? -42.670 13.340 16.662 1.00 30.03 ? 369 SER A C 1 ATOM 2786 O O . SER A 1 369 ? -42.988 13.875 17.734 1.00 28.85 ? 369 SER A O 1 ATOM 2787 C CB . SER A 1 369 ? -43.346 14.369 14.467 1.00 31.57 ? 369 SER A CB 1 ATOM 2788 O OG . SER A 1 369 ? -43.758 13.127 13.930 1.00 32.77 ? 369 SER A OG 1 ATOM 2789 N N . THR A 1 370 ? -42.671 12.023 16.490 1.00 28.34 ? 370 THR A N 1 ATOM 2790 C CA . THR A 1 370 ? -43.039 11.110 17.558 1.00 28.35 ? 370 THR A CA 1 ATOM 2791 C C . THR A 1 370 ? -42.102 11.259 18.768 1.00 29.63 ? 370 THR A C 1 ATOM 2792 O O . THR A 1 370 ? -42.541 11.355 19.918 1.00 28.72 ? 370 THR A O 1 ATOM 2793 C CB . THR A 1 370 ? -43.002 9.656 17.068 1.00 28.21 ? 370 THR A CB 1 ATOM 2794 O OG1 . THR A 1 370 ? -43.966 9.495 16.019 1.00 25.86 ? 370 THR A OG1 1 ATOM 2795 C CG2 . THR A 1 370 ? -43.290 8.678 18.227 1.00 27.23 ? 370 THR A CG2 1 ATOM 2796 N N . GLN A 1 371 ? -40.806 11.299 18.496 1.00 30.63 ? 371 GLN A N 1 ATOM 2797 C CA . GLN A 1 371 ? -39.823 11.404 19.562 1.00 32.39 ? 371 GLN A CA 1 ATOM 2798 C C . GLN A 1 371 ? -39.868 12.773 20.255 1.00 31.28 ? 371 GLN A C 1 ATOM 2799 O O . GLN A 1 371 ? -39.654 12.866 21.465 1.00 30.61 ? 371 GLN A O 1 ATOM 2800 C CB . GLN A 1 371 ? -38.424 11.130 19.011 1.00 35.85 ? 371 GLN A CB 1 ATOM 2801 C CG . GLN A 1 371 ? -37.408 10.787 20.086 1.00 39.61 ? 371 GLN A CG 1 ATOM 2802 C CD . GLN A 1 371 ? -37.813 9.560 20.886 1.00 41.53 ? 371 GLN A CD 1 ATOM 2803 O OE1 . GLN A 1 371 ? -38.160 8.519 20.318 1.00 43.91 ? 371 GLN A OE1 1 ATOM 2804 N NE2 . GLN A 1 371 ? -37.783 9.681 22.212 1.00 42.11 ? 371 GLN A NE2 1 ATOM 2805 N N . ALA A 1 372 ? -40.131 13.825 19.488 1.00 29.81 ? 372 ALA A N 1 ATOM 2806 C CA . ALA A 1 372 ? -40.267 15.174 20.030 1.00 30.56 ? 372 ALA A CA 1 ATOM 2807 C C . ALA A 1 372 ? -41.384 15.260 21.088 1.00 29.50 ? 372 ALA A C 1 ATOM 2808 O O . ALA A 1 372 ? -41.186 15.831 22.176 1.00 28.88 ? 372 ALA A O 1 ATOM 2809 C CB . ALA A 1 372 ? -40.523 16.160 18.898 1.00 30.44 ? 372 ALA A CB 1 ATOM 2810 N N . ALA A 1 373 ? -42.543 14.681 20.782 1.00 28.11 ? 373 ALA A N 1 ATOM 2811 C CA . ALA A 1 373 ? -43.670 14.641 21.724 1.00 27.61 ? 373 ALA A CA 1 ATOM 2812 C C . ALA A 1 373 ? -43.347 13.776 22.940 1.00 27.81 ? 373 ALA A C 1 ATOM 2813 O O . ALA A 1 373 ? -43.569 14.187 24.092 1.00 27.67 ? 373 ALA A O 1 ATOM 2814 C CB . ALA A 1 373 ? -44.926 14.118 21.037 1.00 26.91 ? 373 ALA A CB 1 ATOM 2815 N N . ILE A 1 374 ? -42.809 12.589 22.692 1.00 28.36 ? 374 ILE A N 1 ATOM 2816 C CA . ILE A 1 374 ? -42.508 11.653 23.765 1.00 29.90 ? 374 ILE A CA 1 ATOM 2817 C C . ILE A 1 374 ? -41.468 12.242 24.724 1.00 30.19 ? 374 ILE A C 1 ATOM 2818 O O . ILE A 1 374 ? -41.624 12.129 25.948 1.00 29.48 ? 374 ILE A O 1 ATOM 2819 C CB . ILE A 1 374 ? -42.061 10.288 23.211 1.00 30.08 ? 374 ILE A CB 1 ATOM 2820 C CG1 . ILE A 1 374 ? -43.268 9.567 22.611 1.00 30.45 ? 374 ILE A CG1 1 ATOM 2821 C CG2 . ILE A 1 374 ? -41.426 9.432 24.292 1.00 31.24 ? 374 ILE A CG2 1 ATOM 2822 C CD1 . ILE A 1 374 ? -42.931 8.279 21.881 1.00 30.63 ? 374 ILE A CD1 1 ATOM 2823 N N . ASN A 1 375 ? -40.443 12.895 24.175 1.00 30.98 ? 375 ASN A N 1 ATOM 2824 C CA . ASN A 1 375 ? -39.392 13.515 25.004 1.00 32.74 ? 375 ASN A CA 1 ATOM 2825 C C . ASN A 1 375 ? -39.930 14.613 25.930 1.00 31.95 ? 375 ASN A C 1 ATOM 2826 O O . ASN A 1 375 ? -39.526 14.701 27.095 1.00 30.47 ? 375 ASN A O 1 ATOM 2827 C CB . ASN A 1 375 ? -38.272 14.101 24.130 1.00 34.65 ? 375 ASN A CB 1 ATOM 2828 C CG . ASN A 1 375 ? -37.364 13.038 23.535 1.00 35.60 ? 375 ASN A CG 1 ATOM 2829 O OD1 . ASN A 1 375 ? -37.396 11.865 23.923 1.00 38.56 ? 375 ASN A OD1 1 ATOM 2830 N ND2 . ASN A 1 375 ? -36.543 13.449 22.576 1.00 37.84 ? 375 ASN A ND2 1 ATOM 2831 N N . GLN A 1 376 ? -40.835 15.440 25.414 1.00 30.31 ? 376 GLN A N 1 ATOM 2832 C CA . GLN A 1 376 ? -41.422 16.510 26.204 1.00 30.72 ? 376 GLN A CA 1 ATOM 2833 C C . GLN A 1 376 ? -42.327 15.982 27.302 1.00 29.14 ? 376 GLN A C 1 ATOM 2834 O O . GLN A 1 376 ? -42.356 16.536 28.398 1.00 28.24 ? 376 GLN A O 1 ATOM 2835 C CB . GLN A 1 376 ? -42.190 17.480 25.320 1.00 30.68 ? 376 GLN A CB 1 ATOM 2836 C CG . GLN A 1 376 ? -41.278 18.281 24.406 1.00 32.33 ? 376 GLN A CG 1 ATOM 2837 C CD . GLN A 1 376 ? -42.069 19.134 23.469 1.00 31.75 ? 376 GLN A CD 1 ATOM 2838 O OE1 . GLN A 1 376 ? -42.715 20.080 23.887 1.00 33.50 ? 376 GLN A OE1 1 ATOM 2839 N NE2 . GLN A 1 376 ? -42.039 18.795 22.186 1.00 35.77 ? 376 GLN A NE2 1 ATOM 2840 N N . ILE A 1 377 ? -43.076 14.924 27.005 1.00 27.67 ? 377 ILE A N 1 ATOM 2841 C CA . ILE A 1 377 ? -43.937 14.310 28.001 1.00 27.53 ? 377 ILE A CA 1 ATOM 2842 C C . ILE A 1 377 ? -43.086 13.634 29.086 1.00 28.85 ? 377 ILE A C 1 ATOM 2843 O O . ILE A 1 377 ? -43.350 13.781 30.286 1.00 29.11 ? 377 ILE A O 1 ATOM 2844 C CB . ILE A 1 377 ? -44.932 13.339 27.361 1.00 26.38 ? 377 ILE A CB 1 ATOM 2845 C CG1 . ILE A 1 377 ? -45.984 14.141 26.573 1.00 25.82 ? 377 ILE A CG1 1 ATOM 2846 C CG2 . ILE A 1 377 ? -45.586 12.442 28.414 1.00 25.89 ? 377 ILE A CG2 1 ATOM 2847 C CD1 . ILE A 1 377 ? -46.791 13.306 25.591 1.00 25.51 ? 377 ILE A CD1 1 ATOM 2848 N N . ASN A 1 378 ? -42.041 12.937 28.671 1.00 29.55 ? 378 ASN A N 1 ATOM 2849 C CA . ASN A 1 378 ? -41.130 12.323 29.630 1.00 31.27 ? 378 ASN A CA 1 ATOM 2850 C C . ASN A 1 378 ? -40.456 13.361 30.510 1.00 31.64 ? 378 ASN A C 1 ATOM 2851 O O . ASN A 1 378 ? -40.209 13.102 31.691 1.00 32.41 ? 378 ASN A O 1 ATOM 2852 C CB . ASN A 1 378 ? -40.108 11.434 28.920 1.00 32.60 ? 378 ASN A CB 1 ATOM 2853 C CG . ASN A 1 378 ? -40.682 10.073 28.561 1.00 33.52 ? 378 ASN A CG 1 ATOM 2854 O OD1 . ASN A 1 378 ? -41.700 9.650 29.120 1.00 34.54 ? 378 ASN A OD1 1 ATOM 2855 N ND2 . ASN A 1 378 ? -40.032 9.375 27.638 1.00 33.88 ? 378 ASN A ND2 1 ATOM 2856 N N . GLY A 1 379 ? -40.186 14.536 29.943 1.00 30.73 ? 379 GLY A N 1 ATOM 2857 C CA . GLY A 1 379 ? -39.642 15.663 30.689 1.00 32.46 ? 379 GLY A CA 1 ATOM 2858 C C . GLY A 1 379 ? -40.541 16.097 31.828 1.00 33.09 ? 379 GLY A C 1 ATOM 2859 O O . GLY A 1 379 ? -40.072 16.296 32.954 1.00 30.99 ? 379 GLY A O 1 ATOM 2860 N N . LYS A 1 380 ? -41.836 16.255 31.559 1.00 31.67 ? 380 LYS A N 1 ATOM 2861 C CA . LYS A 1 380 ? -42.742 16.666 32.631 1.00 31.47 ? 380 LYS A CA 1 ATOM 2862 C C . LYS A 1 380 ? -42.961 15.555 33.639 1.00 30.05 ? 380 LYS A C 1 ATOM 2863 O O . LYS A 1 380 ? -43.077 15.835 34.821 1.00 31.05 ? 380 LYS A O 1 ATOM 2864 C CB . LYS A 1 380 ? -44.052 17.316 32.134 1.00 33.21 ? 380 LYS A CB 1 ATOM 2865 C CG . LYS A 1 380 ? -44.898 16.533 31.183 1.00 34.38 ? 380 LYS A CG 1 ATOM 2866 C CD . LYS A 1 380 ? -46.158 17.316 30.800 1.00 33.09 ? 380 LYS A CD 1 ATOM 2867 C CE . LYS A 1 380 ? -45.861 18.415 29.799 1.00 32.63 ? 380 LYS A CE 1 ATOM 2868 N NZ . LYS A 1 380 ? -47.015 19.320 29.639 1.00 30.60 ? 380 LYS A NZ 1 ATOM 2869 N N . LEU A 1 381 ? -42.949 14.295 33.211 1.00 29.52 ? 381 LEU A N 1 ATOM 2870 C CA . LEU A 1 381 ? -42.999 13.198 34.168 1.00 29.57 ? 381 LEU A CA 1 ATOM 2871 C C . LEU A 1 381 ? -41.778 13.234 35.087 1.00 31.28 ? 381 LEU A C 1 ATOM 2872 O O . LEU A 1 381 ? -41.886 12.974 36.270 1.00 30.74 ? 381 LEU A O 1 ATOM 2873 C CB . LEU A 1 381 ? -43.060 11.841 33.470 1.00 30.10 ? 381 LEU A CB 1 ATOM 2874 C CG . LEU A 1 381 ? -44.387 11.534 32.784 1.00 29.37 ? 381 LEU A CG 1 ATOM 2875 C CD1 . LEU A 1 381 ? -44.309 10.254 31.958 1.00 29.63 ? 381 LEU A CD1 1 ATOM 2876 C CD2 . LEU A 1 381 ? -45.489 11.451 33.830 1.00 28.79 ? 381 LEU A CD2 1 ATOM 2877 N N . ASN A 1 382 ? -40.619 13.551 34.521 1.00 32.88 ? 382 ASN A N 1 ATOM 2878 C CA . ASN A 1 382 ? -39.385 13.634 35.297 1.00 35.37 ? 382 ASN A CA 1 ATOM 2879 C C . ASN A 1 382 ? -39.424 14.736 36.382 1.00 34.21 ? 382 ASN A C 1 ATOM 2880 O O . ASN A 1 382 ? -38.824 14.569 37.439 1.00 34.77 ? 382 ASN A O 1 ATOM 2881 C CB . ASN A 1 382 ? -38.187 13.792 34.351 1.00 39.08 ? 382 ASN A CB 1 ATOM 2882 C CG . ASN A 1 382 ? -37.839 12.492 33.615 1.00 43.49 ? 382 ASN A CG 1 ATOM 2883 O OD1 . ASN A 1 382 ? -38.407 11.426 33.891 1.00 48.10 ? 382 ASN A OD1 1 ATOM 2884 N ND2 . ASN A 1 382 ? -36.904 12.577 32.666 1.00 46.55 ? 382 ASN A ND2 1 ATOM 2885 N N . ARG A 1 383 ? -40.143 15.832 36.140 1.00 31.83 ? 383 ARG A N 1 ATOM 2886 C CA . ARG A 1 383 ? -40.318 16.876 37.158 1.00 33.32 ? 383 ARG A CA 1 ATOM 2887 C C . ARG A 1 383 ? -41.294 16.475 38.255 1.00 31.23 ? 383 ARG A C 1 ATOM 2888 O O . ARG A 1 383 ? -41.209 16.977 39.368 1.00 30.83 ? 383 ARG A O 1 ATOM 2889 C CB . ARG A 1 383 ? -40.858 18.165 36.547 1.00 37.13 ? 383 ARG A CB 1 ATOM 2890 C CG . ARG A 1 383 ? -39.977 18.861 35.527 1.00 41.95 ? 383 ARG A CG 1 ATOM 2891 C CD . ARG A 1 383 ? -40.747 20.040 34.928 1.00 46.71 ? 383 ARG A CD 1 ATOM 2892 N NE . ARG A 1 383 ? -39.926 20.888 34.061 1.00 52.11 ? 383 ARG A NE 1 ATOM 2893 C CZ . ARG A 1 383 ? -40.290 22.092 33.595 1.00 54.33 ? 383 ARG A CZ 1 ATOM 2894 N NH1 . ARG A 1 383 ? -41.478 22.624 33.899 1.00 56.65 ? 383 ARG A NH1 1 ATOM 2895 N NH2 . ARG A 1 383 ? -39.456 22.778 32.818 1.00 51.78 ? 383 ARG A NH2 1 ATOM 2896 N N . LEU A 1 384 ? -42.251 15.614 37.926 1.00 28.84 ? 384 LEU A N 1 ATOM 2897 C CA . LEU A 1 384 ? -43.382 15.334 38.816 1.00 28.48 ? 384 LEU A CA 1 ATOM 2898 C C . LEU A 1 384 ? -43.304 14.006 39.542 1.00 28.38 ? 384 LEU A C 1 ATOM 2899 O O . LEU A 1 384 ? -43.945 13.836 40.579 1.00 27.89 ? 384 LEU A O 1 ATOM 2900 C CB . LEU A 1 384 ? -44.682 15.364 38.012 1.00 27.32 ? 384 LEU A CB 1 ATOM 2901 C CG . LEU A 1 384 ? -45.088 16.756 37.509 1.00 27.66 ? 384 LEU A CG 1 ATOM 2902 C CD1 . LEU A 1 384 ? -46.250 16.678 36.510 1.00 28.16 ? 384 LEU A CD1 1 ATOM 2903 C CD2 . LEU A 1 384 ? -45.416 17.676 38.682 1.00 28.80 ? 384 LEU A CD2 1 ATOM 2904 N N . ILE A 1 385 ? -42.572 13.048 38.975 1.00 26.65 ? 385 ILE A N 1 ATOM 2905 C CA . ILE A 1 385 ? -42.560 11.694 39.482 1.00 27.32 ? 385 ILE A CA 1 ATOM 2906 C C . ILE A 1 385 ? -41.238 11.471 40.208 1.00 27.79 ? 385 ILE A C 1 ATOM 2907 O O . ILE A 1 385 ? -40.164 11.839 39.707 1.00 27.91 ? 385 ILE A O 1 ATOM 2908 C CB . ILE A 1 385 ? -42.727 10.647 38.349 1.00 28.12 ? 385 ILE A CB 1 ATOM 2909 C CG1 . ILE A 1 385 ? -44.075 10.813 37.617 1.00 28.98 ? 385 ILE A CG1 1 ATOM 2910 C CG2 . ILE A 1 385 ? -42.623 9.224 38.894 1.00 28.31 ? 385 ILE A CG2 1 ATOM 2911 C CD1 . ILE A 1 385 ? -45.312 10.717 38.497 1.00 28.79 ? 385 ILE A CD1 1 ATOM 2912 N N . GLY A 1 386 ? -41.328 10.912 41.412 1.00 27.72 ? 386 GLY A N 1 ATOM 2913 C CA . GLY A 1 386 ? -40.149 10.580 42.201 1.00 28.78 ? 386 GLY A CA 1 ATOM 2914 C C . GLY A 1 386 ? -39.377 11.771 42.731 1.00 29.27 ? 386 GLY A C 1 ATOM 2915 O O . GLY A 1 386 ? -38.166 11.665 42.935 1.00 30.63 ? 386 GLY A O 1 ATOM 2916 N N . LYS A 1 387 ? -40.063 12.887 42.989 1.00 28.56 ? 387 LYS A N 1 ATOM 2917 C CA . LYS A 1 387 ? -39.411 14.122 43.404 1.00 29.53 ? 387 LYS A CA 1 ATOM 2918 C C . LYS A 1 387 ? -39.934 14.704 44.730 1.00 28.44 ? 387 LYS A C 1 ATOM 2919 O O . LYS A 1 387 ? -39.810 15.903 44.977 1.00 28.56 ? 387 LYS A O 1 ATOM 2920 C CB . LYS A 1 387 ? -39.533 15.157 42.288 1.00 30.70 ? 387 LYS A CB 1 ATOM 2921 C CG . LYS A 1 387 ? -38.918 14.702 40.975 1.00 31.83 ? 387 LYS A CG 1 ATOM 2922 C CD . LYS A 1 387 ? -37.402 14.603 41.079 1.00 33.00 ? 387 LYS A CD 1 ATOM 2923 C CE . LYS A 1 387 ? -36.746 14.317 39.732 1.00 34.56 ? 387 LYS A CE 1 ATOM 2924 N NZ . LYS A 1 387 ? -37.213 13.029 39.135 1.00 36.14 ? 387 LYS A NZ 1 ATOM 2925 N N . THR A 1 388 ? -40.474 13.854 45.603 1.00 27.60 ? 388 THR A N 1 ATOM 2926 C CA . THR A 1 388 ? -41.061 14.341 46.855 1.00 27.30 ? 388 THR A CA 1 ATOM 2927 C C . THR A 1 388 ? -39.980 14.883 47.789 1.00 29.84 ? 388 THR A C 1 ATOM 2928 O O . THR A 1 388 ? -38.790 14.501 47.698 1.00 29.28 ? 388 THR A O 1 ATOM 2929 C CB . THR A 1 388 ? -41.862 13.254 47.606 1.00 26.35 ? 388 THR A CB 1 ATOM 2930 O OG1 . THR A 1 388 ? -40.983 12.174 47.975 1.00 26.22 ? 388 THR A OG1 1 ATOM 2931 C CG2 . THR A 1 388 ? -43.055 12.743 46.734 1.00 25.89 ? 388 THR A CG2 1 ATOM 2932 N N . ASN A 1 389 ? -40.411 15.775 48.673 1.00 29.05 ? 389 ASN A N 1 ATOM 2933 C CA A ASN A 1 389 ? -39.507 16.355 49.658 0.50 30.55 ? 389 ASN A CA 1 ATOM 2934 C CA B ASN A 1 389 ? -39.529 16.389 49.653 0.50 30.19 ? 389 ASN A CA 1 ATOM 2935 C C . ASN A 1 389 ? -39.816 15.850 51.056 1.00 29.19 ? 389 ASN A C 1 ATOM 2936 O O . ASN A 1 389 ? -40.959 15.533 51.372 1.00 28.81 ? 389 ASN A O 1 ATOM 2937 C CB A ASN A 1 389 ? -39.503 17.892 49.614 0.50 32.27 ? 389 ASN A CB 1 ATOM 2938 C CB B ASN A 1 389 ? -39.709 17.903 49.616 0.50 31.16 ? 389 ASN A CB 1 ATOM 2939 C CG A ASN A 1 389 ? -40.886 18.517 49.738 0.50 33.38 ? 389 ASN A CG 1 ATOM 2940 C CG B ASN A 1 389 ? -39.126 18.530 48.357 0.50 32.31 ? 389 ASN A CG 1 ATOM 2941 O OD1 A ASN A 1 389 ? -41.866 17.884 50.161 0.50 35.62 ? 389 ASN A OD1 1 ATOM 2942 O OD1 B ASN A 1 389 ? -38.361 17.900 47.625 0.50 32.57 ? 389 ASN A OD1 1 ATOM 2943 N ND2 A ASN A 1 389 ? -40.966 19.795 49.372 0.50 33.63 ? 389 ASN A ND2 1 ATOM 2944 N ND2 B ASN A 1 389 ? -39.469 19.786 48.118 0.50 32.72 ? 389 ASN A ND2 1 ATOM 2945 N N . GLU A 1 390 ? -38.776 15.765 51.882 1.00 27.21 ? 390 GLU A N 1 ATOM 2946 C CA . GLU A 1 390 ? -38.905 15.261 53.240 1.00 25.48 ? 390 GLU A CA 1 ATOM 2947 C C . GLU A 1 390 ? -39.427 16.293 54.245 1.00 22.70 ? 390 GLU A C 1 ATOM 2948 O O . GLU A 1 390 ? -38.937 17.430 54.288 1.00 21.98 ? 390 GLU A O 1 ATOM 2949 C CB . GLU A 1 390 ? -37.536 14.768 53.728 1.00 27.62 ? 390 GLU A CB 1 ATOM 2950 C CG . GLU A 1 390 ? -37.093 13.448 53.116 1.00 30.09 ? 390 GLU A CG 1 ATOM 2951 C CD . GLU A 1 390 ? -35.861 12.895 53.794 1.00 31.76 ? 390 GLU A CD 1 ATOM 2952 O OE1 . GLU A 1 390 ? -34.827 13.577 53.685 1.00 31.80 ? 390 GLU A OE1 1 ATOM 2953 O OE2 . GLU A 1 390 ? -35.952 11.821 54.473 1.00 33.33 ? 390 GLU A OE2 1 ATOM 2954 N N . LYS A 1 391 ? -40.360 15.869 55.102 1.00 20.38 ? 391 LYS A N 1 ATOM 2955 C CA . LYS A 1 391 ? -40.738 16.603 56.316 1.00 19.69 ? 391 LYS A CA 1 ATOM 2956 C C . LYS A 1 391 ? -40.703 15.662 57.515 1.00 19.27 ? 391 LYS A C 1 ATOM 2957 O O . LYS A 1 391 ? -40.952 14.454 57.373 1.00 18.26 ? 391 LYS A O 1 ATOM 2958 C CB . LYS A 1 391 ? -42.138 17.214 56.218 1.00 20.44 ? 391 LYS A CB 1 ATOM 2959 C CG . LYS A 1 391 ? -42.323 18.170 55.040 1.00 20.99 ? 391 LYS A CG 1 ATOM 2960 C CD . LYS A 1 391 ? -41.534 19.454 55.215 1.00 21.02 ? 391 LYS A CD 1 ATOM 2961 C CE . LYS A 1 391 ? -41.808 20.430 54.084 1.00 21.59 ? 391 LYS A CE 1 ATOM 2962 N NZ . LYS A 1 391 ? -40.929 21.615 54.132 1.00 21.23 ? 391 LYS A NZ 1 ATOM 2963 N N . PHE A 1 392 ? -40.424 16.218 58.686 1.00 17.56 ? 392 PHE A N 1 ATOM 2964 C CA . PHE A 1 392 ? -40.156 15.410 59.861 1.00 18.05 ? 392 PHE A CA 1 ATOM 2965 C C . PHE A 1 392 ? -41.130 15.763 60.973 1.00 17.04 ? 392 PHE A C 1 ATOM 2966 O O . PHE A 1 392 ? -42.310 15.512 60.812 1.00 17.30 ? 392 PHE A O 1 ATOM 2967 C CB . PHE A 1 392 ? -38.669 15.541 60.222 1.00 19.18 ? 392 PHE A CB 1 ATOM 2968 C CG . PHE A 1 392 ? -37.755 15.135 59.081 1.00 20.26 ? 392 PHE A CG 1 ATOM 2969 C CD1 . PHE A 1 392 ? -37.733 13.836 58.645 1.00 21.37 ? 392 PHE A CD1 1 ATOM 2970 C CD2 . PHE A 1 392 ? -36.981 16.077 58.416 1.00 21.87 ? 392 PHE A CD2 1 ATOM 2971 C CE1 . PHE A 1 392 ? -36.929 13.442 57.576 1.00 22.23 ? 392 PHE A CE1 1 ATOM 2972 C CE2 . PHE A 1 392 ? -36.155 15.697 57.346 1.00 22.88 ? 392 PHE A CE2 1 ATOM 2973 C CZ . PHE A 1 392 ? -36.123 14.374 56.944 1.00 22.65 ? 392 PHE A CZ 1 ATOM 2974 N N . HIS A 1 393 ? -40.684 16.345 62.072 1.00 16.73 ? 393 HIS A N 1 ATOM 2975 C CA . HIS A 1 393 ? -41.612 16.712 63.156 1.00 16.60 ? 393 HIS A CA 1 ATOM 2976 C C . HIS A 1 393 ? -42.368 17.950 62.767 1.00 16.62 ? 393 HIS A C 1 ATOM 2977 O O . HIS A 1 393 ? -41.768 18.941 62.335 1.00 16.82 ? 393 HIS A O 1 ATOM 2978 C CB . HIS A 1 393 ? -40.856 16.950 64.440 1.00 17.37 ? 393 HIS A CB 1 ATOM 2979 C CG . HIS A 1 393 ? -41.725 16.970 65.662 1.00 17.71 ? 393 HIS A CG 1 ATOM 2980 N ND1 . HIS A 1 393 ? -42.569 15.969 65.964 1.00 18.40 ? 393 HIS A ND1 1 ATOM 2981 C CD2 . HIS A 1 393 ? -41.887 17.932 66.650 1.00 18.45 ? 393 HIS A CD2 1 ATOM 2982 C CE1 . HIS A 1 393 ? -43.206 16.257 67.109 1.00 18.31 ? 393 HIS A CE1 1 ATOM 2983 N NE2 . HIS A 1 393 ? -42.779 17.452 67.533 1.00 18.42 ? 393 HIS A NE2 1 ATOM 2984 N N A GLN A 1 394 ? -43.686 17.927 62.942 0.50 16.03 ? 394 GLN A N 1 ATOM 2985 N N B GLN A 1 394 ? -43.684 17.898 62.903 0.50 16.30 ? 394 GLN A N 1 ATOM 2986 C CA A GLN A 1 394 ? -44.553 18.995 62.429 0.50 16.03 ? 394 GLN A CA 1 ATOM 2987 C CA B GLN A 1 394 ? -44.540 19.012 62.528 0.50 16.51 ? 394 GLN A CA 1 ATOM 2988 C C A GLN A 1 394 ? -45.438 19.602 63.543 0.50 15.96 ? 394 GLN A C 1 ATOM 2989 C C B GLN A 1 394 ? -45.492 19.276 63.689 0.50 16.28 ? 394 GLN A C 1 ATOM 2990 O O A GLN A 1 394 ? -44.907 20.217 64.470 0.50 16.36 ? 394 GLN A O 1 ATOM 2991 O O B GLN A 1 394 ? -45.080 19.235 64.851 0.50 17.06 ? 394 GLN A O 1 ATOM 2992 C CB A GLN A 1 394 ? -45.331 18.442 61.223 0.50 15.87 ? 394 GLN A CB 1 ATOM 2993 C CB B GLN A 1 394 ? -45.265 18.668 61.226 0.50 16.67 ? 394 GLN A CB 1 ATOM 2994 C CG A GLN A 1 394 ? -44.395 18.031 60.087 0.50 15.90 ? 394 GLN A CG 1 ATOM 2995 C CG B GLN A 1 394 ? -44.323 18.365 60.072 0.50 16.99 ? 394 GLN A CG 1 ATOM 2996 C CD A GLN A 1 394 ? -45.043 17.175 59.020 0.50 15.91 ? 394 GLN A CD 1 ATOM 2997 C CD B GLN A 1 394 ? -45.043 18.171 58.752 0.50 17.34 ? 394 GLN A CD 1 ATOM 2998 O OE1 A GLN A 1 394 ? -46.008 17.604 58.383 0.50 16.24 ? 394 GLN A OE1 1 ATOM 2999 O OE1 B GLN A 1 394 ? -46.046 17.463 58.677 0.50 17.92 ? 394 GLN A OE1 1 ATOM 3000 N NE2 A GLN A 1 394 ? -44.499 15.967 58.795 0.50 15.82 ? 394 GLN A NE2 1 ATOM 3001 N NE2 B GLN A 1 394 ? -44.537 18.816 57.703 0.50 17.31 ? 394 GLN A NE2 1 ATOM 3002 N N . ILE A 1 395 ? -46.762 19.523 63.403 1.00 15.78 ? 395 ILE A N 1 ATOM 3003 C CA . ILE A 1 395 ? -47.712 19.821 64.463 1.00 15.48 ? 395 ILE A CA 1 ATOM 3004 C C . ILE A 1 395 ? -48.639 18.620 64.503 1.00 15.52 ? 395 ILE A C 1 ATOM 3005 O O . ILE A 1 395 ? -48.704 17.811 63.534 1.00 15.25 ? 395 ILE A O 1 ATOM 3006 C CB . ILE A 1 395 ? -48.530 21.115 64.203 1.00 15.04 ? 395 ILE A CB 1 ATOM 3007 C CG1 . ILE A 1 395 ? -49.280 21.051 62.859 1.00 15.18 ? 395 ILE A CG1 1 ATOM 3008 C CG2 . ILE A 1 395 ? -47.612 22.342 64.241 1.00 15.10 ? 395 ILE A CG2 1 ATOM 3009 C CD1 . ILE A 1 395 ? -50.339 22.145 62.692 1.00 15.04 ? 395 ILE A CD1 1 ATOM 3010 N N . GLU A 1 396 ? -49.376 18.504 65.600 1.00 15.86 ? 396 GLU A N 1 ATOM 3011 C CA . GLU A 1 396 ? -50.397 17.485 65.702 1.00 16.41 ? 396 GLU A CA 1 ATOM 3012 C C . GLU A 1 396 ? -51.599 17.907 64.865 1.00 16.14 ? 396 GLU A C 1 ATOM 3013 O O . GLU A 1 396 ? -51.881 19.101 64.674 1.00 15.76 ? 396 GLU A O 1 ATOM 3014 C CB . GLU A 1 396 ? -50.812 17.254 67.159 1.00 17.37 ? 396 GLU A CB 1 ATOM 3015 C CG . GLU A 1 396 ? -49.662 16.751 68.040 1.00 18.25 ? 396 GLU A CG 1 ATOM 3016 C CD . GLU A 1 396 ? -49.092 15.405 67.614 1.00 19.36 ? 396 GLU A CD 1 ATOM 3017 O OE1 . GLU A 1 396 ? -49.827 14.595 66.980 1.00 21.49 ? 396 GLU A OE1 1 ATOM 3018 O OE2 . GLU A 1 396 ? -47.892 15.126 67.930 1.00 20.23 ? 396 GLU A OE2 1 ATOM 3019 N N . LYS A 1 397 ? -52.309 16.913 64.360 1.00 15.65 ? 397 LYS A N 1 ATOM 3020 C CA . LYS A 1 397 ? -53.387 17.147 63.407 1.00 16.04 ? 397 LYS A CA 1 ATOM 3021 C C . LYS A 1 397 ? -54.689 16.411 63.761 1.00 16.81 ? 397 LYS A C 1 ATOM 3022 O O . LYS A 1 397 ? -55.707 16.591 63.077 1.00 17.54 ? 397 LYS A O 1 ATOM 3023 C CB . LYS A 1 397 ? -52.907 16.753 62.012 1.00 15.40 ? 397 LYS A CB 1 ATOM 3024 C CG . LYS A 1 397 ? -51.758 17.647 61.556 1.00 15.37 ? 397 LYS A CG 1 ATOM 3025 C CD . LYS A 1 397 ? -51.181 17.279 60.222 1.00 15.20 ? 397 LYS A CD 1 ATOM 3026 C CE . LYS A 1 397 ? -49.894 18.067 59.969 1.00 15.07 ? 397 LYS A CE 1 ATOM 3027 N NZ . LYS A 1 397 ? -49.386 17.821 58.583 1.00 15.03 ? 397 LYS A NZ 1 ATOM 3028 N N . GLU A 1 398 ? -54.648 15.599 64.805 1.00 17.83 ? 398 GLU A N 1 ATOM 3029 C CA . GLU A 1 398 ? -55.829 14.951 65.390 1.00 19.12 ? 398 GLU A CA 1 ATOM 3030 C C . GLU A 1 398 ? -55.742 15.152 66.897 1.00 18.94 ? 398 GLU A C 1 ATOM 3031 O O . GLU A 1 398 ? -54.631 15.169 67.454 1.00 17.92 ? 398 GLU A O 1 ATOM 3032 C CB . GLU A 1 398 ? -55.854 13.454 65.061 1.00 22.35 ? 398 GLU A CB 1 ATOM 3033 C CG . GLU A 1 398 ? -56.083 13.137 63.594 1.00 24.32 ? 398 GLU A CG 1 ATOM 3034 C CD . GLU A 1 398 ? -56.243 11.650 63.299 1.00 28.26 ? 398 GLU A CD 1 ATOM 3035 O OE1 . GLU A 1 398 ? -56.451 10.847 64.241 1.00 32.14 ? 398 GLU A OE1 1 ATOM 3036 O OE2 . GLU A 1 398 ? -56.178 11.270 62.109 1.00 31.22 ? 398 GLU A OE2 1 ATOM 3037 N N . PHE A 1 399 ? -56.896 15.292 67.558 1.00 19.10 ? 399 PHE A N 1 ATOM 3038 C CA . PHE A 1 399 ? -56.946 15.631 68.991 1.00 19.45 ? 399 PHE A CA 1 ATOM 3039 C C . PHE A 1 399 ? -58.009 14.804 69.699 1.00 21.30 ? 399 PHE A C 1 ATOM 3040 O O . PHE A 1 399 ? -59.124 14.680 69.182 1.00 22.45 ? 399 PHE A O 1 ATOM 3041 C CB . PHE A 1 399 ? -57.267 17.128 69.127 1.00 19.11 ? 399 PHE A CB 1 ATOM 3042 C CG . PHE A 1 399 ? -56.300 17.983 68.382 1.00 18.28 ? 399 PHE A CG 1 ATOM 3043 C CD1 . PHE A 1 399 ? -56.510 18.287 67.049 1.00 18.25 ? 399 PHE A CD1 1 ATOM 3044 C CD2 . PHE A 1 399 ? -55.147 18.430 69.004 1.00 18.42 ? 399 PHE A CD2 1 ATOM 3045 C CE1 . PHE A 1 399 ? -55.579 19.042 66.343 1.00 18.34 ? 399 PHE A CE1 1 ATOM 3046 C CE2 . PHE A 1 399 ? -54.212 19.177 68.306 1.00 18.40 ? 399 PHE A CE2 1 ATOM 3047 C CZ . PHE A 1 399 ? -54.428 19.478 66.974 1.00 18.14 ? 399 PHE A CZ 1 ATOM 3048 N N . SER A 1 400 ? -57.664 14.270 70.861 1.00 22.62 ? 400 SER A N 1 ATOM 3049 C CA . SER A 1 400 ? -58.599 13.448 71.655 1.00 24.61 ? 400 SER A CA 1 ATOM 3050 C C . SER A 1 400 ? -59.390 14.242 72.703 1.00 25.69 ? 400 SER A C 1 ATOM 3051 O O . SER A 1 400 ? -60.387 13.740 73.247 1.00 25.82 ? 400 SER A O 1 ATOM 3052 C CB . SER A 1 400 ? -57.829 12.312 72.310 1.00 24.92 ? 400 SER A CB 1 ATOM 3053 O OG . SER A 1 400 ? -56.809 12.814 73.161 1.00 27.16 ? 400 SER A OG 1 ATOM 3054 N N . GLU A 1 401 ? -58.964 15.470 72.989 1.00 25.04 ? 401 GLU A N 1 ATOM 3055 C CA . GLU A 1 401 ? -59.668 16.322 73.956 1.00 26.88 ? 401 GLU A CA 1 ATOM 3056 C C . GLU A 1 401 ? -60.011 17.651 73.326 1.00 25.68 ? 401 GLU A C 1 ATOM 3057 O O . GLU A 1 401 ? -59.316 18.111 72.419 1.00 23.64 ? 401 GLU A O 1 ATOM 3058 C CB . GLU A 1 401 ? -58.815 16.617 75.190 1.00 29.11 ? 401 GLU A CB 1 ATOM 3059 C CG . GLU A 1 401 ? -58.598 15.431 76.110 1.00 33.55 ? 401 GLU A CG 1 ATOM 3060 C CD . GLU A 1 401 ? -57.541 14.493 75.602 1.00 35.38 ? 401 GLU A CD 1 ATOM 3061 O OE1 . GLU A 1 401 ? -56.461 14.989 75.203 1.00 40.33 ? 401 GLU A OE1 1 ATOM 3062 O OE2 . GLU A 1 401 ? -57.789 13.263 75.606 1.00 38.47 ? 401 GLU A OE2 1 ATOM 3063 N N . VAL A 1 402 ? -61.058 18.270 73.860 1.00 24.59 ? 402 VAL A N 1 ATOM 3064 C CA . VAL A 1 402 ? -61.450 19.631 73.512 1.00 24.32 ? 402 VAL A CA 1 ATOM 3065 C C . VAL A 1 402 ? -60.549 20.625 74.253 1.00 23.06 ? 402 VAL A C 1 ATOM 3066 O O . VAL A 1 402 ? -60.336 20.496 75.463 1.00 21.92 ? 402 VAL A O 1 ATOM 3067 C CB . VAL A 1 402 ? -62.934 19.865 73.906 1.00 25.54 ? 402 VAL A CB 1 ATOM 3068 C CG1 . VAL A 1 402 ? -63.259 21.340 73.927 1.00 26.16 ? 402 VAL A CG1 1 ATOM 3069 C CG2 . VAL A 1 402 ? -63.852 19.126 72.941 1.00 26.41 ? 402 VAL A CG2 1 ATOM 3070 N N . GLU A 1 403 ? -60.005 21.617 73.549 1.00 21.88 ? 403 GLU A N 1 ATOM 3071 C CA . GLU A 1 403 ? -59.077 22.571 74.186 1.00 21.99 ? 403 GLU A CA 1 ATOM 3072 C C . GLU A 1 403 ? -59.302 24.058 73.896 1.00 21.55 ? 403 GLU A C 1 ATOM 3073 O O . GLU A 1 403 ? -58.820 24.912 74.658 1.00 22.41 ? 403 GLU A O 1 ATOM 3074 C CB . GLU A 1 403 ? -57.620 22.242 73.793 1.00 22.49 ? 403 GLU A CB 1 ATOM 3075 C CG . GLU A 1 403 ? -57.151 20.849 74.131 1.00 22.53 ? 403 GLU A CG 1 ATOM 3076 C CD . GLU A 1 403 ? -55.770 20.574 73.576 1.00 23.22 ? 403 GLU A CD 1 ATOM 3077 O OE1 . GLU A 1 403 ? -55.614 20.484 72.343 1.00 22.52 ? 403 GLU A OE1 1 ATOM 3078 O OE2 . GLU A 1 403 ? -54.824 20.470 74.365 1.00 24.17 ? 403 GLU A OE2 1 ATOM 3079 N N . GLY A 1 404 ? -59.971 24.379 72.795 1.00 20.14 ? 404 GLY A N 1 ATOM 3080 C CA . GLY A 1 404 ? -60.256 25.750 72.434 1.00 19.87 ? 404 GLY A CA 1 ATOM 3081 C C . GLY A 1 404 ? -59.147 26.397 71.604 1.00 18.74 ? 404 GLY A C 1 ATOM 3082 O O . GLY A 1 404 ? -58.706 25.832 70.620 1.00 17.88 ? 404 GLY A O 1 ATOM 3083 N N . ARG A 1 405 ? -58.697 27.573 72.036 1.00 18.13 ? 405 ARG A N 1 ATOM 3084 C CA . ARG A 1 405 ? -57.925 28.487 71.199 1.00 17.68 ? 405 ARG A CA 1 ATOM 3085 C C . ARG A 1 405 ? -56.702 27.901 70.454 1.00 17.05 ? 405 ARG A C 1 ATOM 3086 O O . ARG A 1 405 ? -56.570 28.082 69.242 1.00 16.79 ? 405 ARG A O 1 ATOM 3087 C CB . ARG A 1 405 ? -57.484 29.668 72.048 1.00 18.00 ? 405 ARG A CB 1 ATOM 3088 C CG . ARG A 1 405 ? -56.896 30.826 71.285 1.00 18.42 ? 405 ARG A CG 1 ATOM 3089 C CD . ARG A 1 405 ? -56.620 31.991 72.239 1.00 18.75 ? 405 ARG A CD 1 ATOM 3090 N NE . ARG A 1 405 ? -56.078 33.119 71.512 1.00 18.81 ? 405 ARG A NE 1 ATOM 3091 C CZ . ARG A 1 405 ? -55.934 34.332 72.011 1.00 19.25 ? 405 ARG A CZ 1 ATOM 3092 N NH1 . ARG A 1 405 ? -56.233 34.568 73.274 1.00 19.70 ? 405 ARG A NH1 1 ATOM 3093 N NH2 . ARG A 1 405 ? -55.478 35.314 71.244 1.00 19.71 ? 405 ARG A NH2 1 ATOM 3094 N N A ILE A 1 406 ? -55.813 27.227 71.176 0.50 16.86 ? 406 ILE A N 1 ATOM 3095 N N B ILE A 1 406 ? -55.814 27.229 71.161 0.50 17.08 ? 406 ILE A N 1 ATOM 3096 C CA A ILE A 1 406 ? -54.589 26.693 70.554 0.50 16.62 ? 406 ILE A CA 1 ATOM 3097 C CA B ILE A 1 406 ? -54.604 26.732 70.511 0.50 16.99 ? 406 ILE A CA 1 ATOM 3098 C C A ILE A 1 406 ? -54.925 25.635 69.504 0.50 16.20 ? 406 ILE A C 1 ATOM 3099 C C B ILE A 1 406 ? -54.930 25.639 69.490 0.50 16.38 ? 406 ILE A C 1 ATOM 3100 O O A ILE A 1 406 ? -54.388 25.646 68.383 0.50 15.56 ? 406 ILE A O 1 ATOM 3101 O O B ILE A 1 406 ? -54.389 25.630 68.371 0.50 15.69 ? 406 ILE A O 1 ATOM 3102 C CB A ILE A 1 406 ? -53.578 26.152 71.593 0.50 16.85 ? 406 ILE A CB 1 ATOM 3103 C CB B ILE A 1 406 ? -53.576 26.256 71.537 0.50 17.50 ? 406 ILE A CB 1 ATOM 3104 C CG1 A ILE A 1 406 ? -52.279 25.723 70.900 0.50 16.80 ? 406 ILE A CG1 1 ATOM 3105 C CG1 B ILE A 1 406 ? -53.331 27.350 72.581 0.50 17.99 ? 406 ILE A CG1 1 ATOM 3106 C CG2 A ILE A 1 406 ? -54.118 24.952 72.353 0.50 16.76 ? 406 ILE A CG2 1 ATOM 3107 C CG2 B ILE A 1 406 ? -52.277 25.873 70.839 0.50 17.53 ? 406 ILE A CG2 1 ATOM 3108 C CD1 A ILE A 1 406 ? -51.556 26.856 70.207 0.50 16.80 ? 406 ILE A CD1 1 ATOM 3109 C CD1 B ILE A 1 406 ? -53.063 28.720 72.002 0.50 18.33 ? 406 ILE A CD1 1 ATOM 3110 N N . GLN A 1 407 ? -55.838 24.736 69.853 1.00 16.15 ? 407 GLN A N 1 ATOM 3111 C CA . GLN A 1 407 ? -56.277 23.706 68.936 1.00 16.12 ? 407 GLN A CA 1 ATOM 3112 C C . GLN A 1 407 ? -57.000 24.282 67.702 1.00 15.64 ? 407 GLN A C 1 ATOM 3113 O O . GLN A 1 407 ? -56.832 23.771 66.592 1.00 15.67 ? 407 GLN A O 1 ATOM 3114 C CB . GLN A 1 407 ? -57.167 22.692 69.675 1.00 16.21 ? 407 GLN A CB 1 ATOM 3115 C CG . GLN A 1 407 ? -57.437 21.444 68.868 1.00 16.68 ? 407 GLN A CG 1 ATOM 3116 C CD . GLN A 1 407 ? -58.376 20.459 69.561 1.00 17.20 ? 407 GLN A CD 1 ATOM 3117 O OE1 . GLN A 1 407 ? -59.388 20.057 68.994 1.00 18.50 ? 407 GLN A OE1 1 ATOM 3118 N NE2 . GLN A 1 407 ? -58.032 20.060 70.774 1.00 17.11 ? 407 GLN A NE2 1 ATOM 3119 N N . ASP A 1 408 ? -57.829 25.306 67.905 1.00 15.71 ? 408 ASP A N 1 ATOM 3120 C CA . ASP A 1 408 ? -58.478 26.003 66.819 1.00 15.76 ? 408 ASP A CA 1 ATOM 3121 C C . ASP A 1 408 ? -57.418 26.491 65.803 1.00 15.19 ? 408 ASP A C 1 ATOM 3122 O O . ASP A 1 408 ? -57.598 26.361 64.596 1.00 14.61 ? 408 ASP A O 1 ATOM 3123 C CB . ASP A 1 408 ? -59.241 27.232 67.293 1.00 16.93 ? 408 ASP A CB 1 ATOM 3124 C CG . ASP A 1 408 ? -60.456 26.920 68.179 1.00 18.06 ? 408 ASP A CG 1 ATOM 3125 O OD1 . ASP A 1 408 ? -61.023 25.805 68.104 1.00 18.55 ? 408 ASP A OD1 1 ATOM 3126 O OD2 . ASP A 1 408 ? -60.833 27.847 68.931 1.00 18.87 ? 408 ASP A OD2 1 ATOM 3127 N N . LEU A 1 409 ? -56.333 27.068 66.319 1.00 14.73 ? 409 LEU A N 1 ATOM 3128 C CA . LEU A 1 409 ? -55.272 27.610 65.451 1.00 14.66 ? 409 LEU A CA 1 ATOM 3129 C C . LEU A 1 409 ? -54.544 26.466 64.737 1.00 14.29 ? 409 LEU A C 1 ATOM 3130 O O . LEU A 1 409 ? -54.318 26.543 63.531 1.00 13.94 ? 409 LEU A O 1 ATOM 3131 C CB . LEU A 1 409 ? -54.290 28.440 66.282 1.00 14.70 ? 409 LEU A CB 1 ATOM 3132 C CG . LEU A 1 409 ? -53.203 29.229 65.541 1.00 14.59 ? 409 LEU A CG 1 ATOM 3133 C CD1 . LEU A 1 409 ? -53.785 30.101 64.446 1.00 14.53 ? 409 LEU A CD1 1 ATOM 3134 C CD2 . LEU A 1 409 ? -52.407 30.005 66.592 1.00 14.98 ? 409 LEU A CD2 1 ATOM 3135 N N . GLU A 1 410 ? -54.204 25.401 65.464 1.00 14.52 ? 410 GLU A N 1 ATOM 3136 C CA . GLU A 1 410 ? -53.519 24.244 64.844 1.00 14.72 ? 410 GLU A CA 1 ATOM 3137 C C . GLU A 1 410 ? -54.359 23.671 63.697 1.00 14.61 ? 410 GLU A C 1 ATOM 3138 O O . GLU A 1 410 ? -53.859 23.382 62.585 1.00 13.70 ? 410 GLU A O 1 ATOM 3139 C CB . GLU A 1 410 ? -53.183 23.150 65.888 1.00 15.36 ? 410 GLU A CB 1 ATOM 3140 C CG . GLU A 1 410 ? -52.120 23.589 66.878 1.00 16.13 ? 410 GLU A CG 1 ATOM 3141 C CD . GLU A 1 410 ? -52.059 22.769 68.165 1.00 17.32 ? 410 GLU A CD 1 ATOM 3142 O OE1 . GLU A 1 410 ? -53.102 22.234 68.579 1.00 18.32 ? 410 GLU A OE1 1 ATOM 3143 O OE2 . GLU A 1 410 ? -50.967 22.715 68.802 1.00 18.44 ? 410 GLU A OE2 1 ATOM 3144 N N . LYS A 1 411 ? -55.658 23.536 63.934 1.00 14.35 ? 411 LYS A N 1 ATOM 3145 C CA . LYS A 1 411 ? -56.545 23.026 62.905 1.00 15.20 ? 411 LYS A CA 1 ATOM 3146 C C . LYS A 1 411 ? -56.683 23.973 61.709 1.00 14.18 ? 411 LYS A C 1 ATOM 3147 O O . LYS A 1 411 ? -56.754 23.531 60.557 1.00 13.92 ? 411 LYS A O 1 ATOM 3148 C CB . LYS A 1 411 ? -57.940 22.734 63.471 1.00 16.28 ? 411 LYS A CB 1 ATOM 3149 C CG . LYS A 1 411 ? -57.993 21.491 64.345 1.00 17.67 ? 411 LYS A CG 1 ATOM 3150 C CD . LYS A 1 411 ? -59.401 21.287 64.906 1.00 19.68 ? 411 LYS A CD 1 ATOM 3151 C CE . LYS A 1 411 ? -59.527 19.963 65.619 1.00 21.47 ? 411 LYS A CE 1 ATOM 3152 N NZ . LYS A 1 411 ? -60.917 19.682 66.108 1.00 24.16 ? 411 LYS A NZ 1 ATOM 3153 N N . TYR A 1 412 ? -56.745 25.267 61.974 1.00 13.84 ? 412 TYR A N 1 ATOM 3154 C CA . TYR A 1 412 ? -56.927 26.257 60.909 1.00 13.58 ? 412 TYR A CA 1 ATOM 3155 C C . TYR A 1 412 ? -55.672 26.358 60.039 1.00 13.15 ? 412 TYR A C 1 ATOM 3156 O O . TYR A 1 412 ? -55.758 26.477 58.837 1.00 13.23 ? 412 TYR A O 1 ATOM 3157 C CB . TYR A 1 412 ? -57.204 27.613 61.522 1.00 13.72 ? 412 TYR A CB 1 ATOM 3158 C CG . TYR A 1 412 ? -57.592 28.712 60.547 1.00 13.78 ? 412 TYR A CG 1 ATOM 3159 C CD1 . TYR A 1 412 ? -58.850 28.745 59.954 1.00 14.00 ? 412 TYR A CD1 1 ATOM 3160 C CD2 . TYR A 1 412 ? -56.709 29.758 60.253 1.00 14.04 ? 412 TYR A CD2 1 ATOM 3161 C CE1 . TYR A 1 412 ? -59.227 29.796 59.120 1.00 14.13 ? 412 TYR A CE1 1 ATOM 3162 C CE2 . TYR A 1 412 ? -57.074 30.803 59.407 1.00 13.97 ? 412 TYR A CE2 1 ATOM 3163 C CZ . TYR A 1 412 ? -58.331 30.811 58.836 1.00 14.15 ? 412 TYR A CZ 1 ATOM 3164 O OH . TYR A 1 412 ? -58.729 31.829 58.010 1.00 13.98 ? 412 TYR A OH 1 ATOM 3165 N N . VAL A 1 413 ? -54.516 26.277 60.673 1.00 13.26 ? 413 VAL A N 1 ATOM 3166 C CA . VAL A 1 413 ? -53.250 26.282 59.944 1.00 13.06 ? 413 VAL A CA 1 ATOM 3167 C C . VAL A 1 413 ? -53.214 25.116 58.935 1.00 13.17 ? 413 VAL A C 1 ATOM 3168 O O . VAL A 1 413 ? -52.884 25.295 57.748 1.00 13.20 ? 413 VAL A O 1 ATOM 3169 C CB . VAL A 1 413 ? -52.085 26.240 60.931 1.00 13.17 ? 413 VAL A CB 1 ATOM 3170 C CG1 . VAL A 1 413 ? -50.791 25.840 60.210 1.00 13.17 ? 413 VAL A CG1 1 ATOM 3171 C CG2 . VAL A 1 413 ? -51.915 27.608 61.611 1.00 13.22 ? 413 VAL A CG2 1 ATOM 3172 N N . GLU A 1 414 ? -53.587 23.934 59.410 1.00 13.47 ? 414 GLU A N 1 ATOM 3173 C CA . GLU A 1 414 ? -53.550 22.742 58.577 1.00 13.87 ? 414 GLU A CA 1 ATOM 3174 C C . GLU A 1 414 ? -54.605 22.774 57.479 1.00 13.80 ? 414 GLU A C 1 ATOM 3175 O O . GLU A 1 414 ? -54.297 22.453 56.334 1.00 13.29 ? 414 GLU A O 1 ATOM 3176 C CB . GLU A 1 414 ? -53.652 21.486 59.435 1.00 14.50 ? 414 GLU A CB 1 ATOM 3177 C CG . GLU A 1 414 ? -53.437 20.200 58.638 1.00 14.98 ? 414 GLU A CG 1 ATOM 3178 C CD . GLU A 1 414 ? -52.027 20.014 58.101 1.00 15.38 ? 414 GLU A CD 1 ATOM 3179 O OE1 . GLU A 1 414 ? -51.119 20.819 58.425 1.00 16.55 ? 414 GLU A OE1 1 ATOM 3180 O OE2 . GLU A 1 414 ? -51.792 19.006 57.371 1.00 16.14 ? 414 GLU A OE2 1 ATOM 3181 N N . ASP A 1 415 ? -55.830 23.194 57.813 1.00 14.27 ? 415 ASP A N 1 ATOM 3182 C CA . ASP A 1 415 ? -56.900 23.347 56.806 1.00 15.22 ? 415 ASP A CA 1 ATOM 3183 C C . ASP A 1 415 ? -56.475 24.324 55.706 1.00 14.31 ? 415 ASP A C 1 ATOM 3184 O O . ASP A 1 415 ? -56.694 24.063 54.520 1.00 13.63 ? 415 ASP A O 1 ATOM 3185 C CB . ASP A 1 415 ? -58.204 23.804 57.446 1.00 16.79 ? 415 ASP A CB 1 ATOM 3186 C CG . ASP A 1 415 ? -59.403 23.599 56.546 1.00 19.74 ? 415 ASP A CG 1 ATOM 3187 O OD1 . ASP A 1 415 ? -59.604 22.497 56.030 1.00 21.69 ? 415 ASP A OD1 1 ATOM 3188 O OD2 . ASP A 1 415 ? -60.144 24.562 56.359 1.00 22.30 ? 415 ASP A OD2 1 ATOM 3189 N N . THR A 1 416 ? -55.900 25.446 56.125 1.00 13.54 ? 416 THR A N 1 ATOM 3190 C CA . THR A 1 416 ? -55.421 26.482 55.222 1.00 13.36 ? 416 THR A CA 1 ATOM 3191 C C . THR A 1 416 ? -54.399 25.929 54.232 1.00 12.80 ? 416 THR A C 1 ATOM 3192 O O . THR A 1 416 ? -54.518 26.133 53.030 1.00 12.51 ? 416 THR A O 1 ATOM 3193 C CB . THR A 1 416 ? -54.843 27.657 56.036 1.00 13.47 ? 416 THR A CB 1 ATOM 3194 O OG1 . THR A 1 416 ? -55.902 28.249 56.809 1.00 14.00 ? 416 THR A OG1 1 ATOM 3195 C CG2 . THR A 1 416 ? -54.224 28.738 55.116 1.00 13.42 ? 416 THR A CG2 1 ATOM 3196 N N . LYS A 1 417 ? -53.408 25.238 54.773 1.00 12.31 ? 417 LYS A N 1 ATOM 3197 C CA . LYS A 1 417 ? -52.338 24.608 53.994 1.00 12.33 ? 417 LYS A CA 1 ATOM 3198 C C . LYS A 1 417 ? -52.901 23.622 52.980 1.00 12.02 ? 417 LYS A C 1 ATOM 3199 O O . LYS A 1 417 ? -52.566 23.666 51.817 1.00 11.81 ? 417 LYS A O 1 ATOM 3200 C CB . LYS A 1 417 ? -51.349 23.904 54.925 1.00 12.27 ? 417 LYS A CB 1 ATOM 3201 C CG . LYS A 1 417 ? -50.234 23.149 54.212 1.00 12.66 ? 417 LYS A CG 1 ATOM 3202 C CD . LYS A 1 417 ? -49.260 22.466 55.175 1.00 13.00 ? 417 LYS A CD 1 ATOM 3203 C CE . LYS A 1 417 ? -48.311 21.540 54.442 1.00 13.45 ? 417 LYS A CE 1 ATOM 3204 N NZ . LYS A 1 417 ? -47.406 20.722 55.363 1.00 14.07 ? 417 LYS A NZ 1 ATOM 3205 N N . ILE A 1 418 ? -53.810 22.759 53.421 1.00 11.89 ? 418 ILE A N 1 ATOM 3206 C CA . ILE A 1 418 ? -54.332 21.714 52.520 1.00 11.83 ? 418 ILE A CA 1 ATOM 3207 C C . ILE A 1 418 ? -55.152 22.316 51.386 1.00 11.74 ? 418 ILE A C 1 ATOM 3208 O O . ILE A 1 418 ? -55.028 21.894 50.243 1.00 11.40 ? 418 ILE A O 1 ATOM 3209 C CB . ILE A 1 418 ? -55.176 20.698 53.310 1.00 12.07 ? 418 ILE A CB 1 ATOM 3210 C CG1 . ILE A 1 418 ? -54.258 19.909 54.242 1.00 12.00 ? 418 ILE A CG1 1 ATOM 3211 C CG2 . ILE A 1 418 ? -55.952 19.795 52.354 1.00 12.00 ? 418 ILE A CG2 1 ATOM 3212 C CD1 . ILE A 1 418 ? -55.005 19.091 55.303 1.00 12.61 ? 418 ILE A CD1 1 ATOM 3213 N N . ASP A 1 419 ? -55.951 23.337 51.683 1.00 11.93 ? 419 ASP A N 1 ATOM 3214 C CA . ASP A 1 419 ? -56.720 23.967 50.631 1.00 12.18 ? 419 ASP A CA 1 ATOM 3215 C C . ASP A 1 419 ? -55.796 24.642 49.619 1.00 11.77 ? 419 ASP A C 1 ATOM 3216 O O . ASP A 1 419 ? -56.094 24.628 48.414 1.00 11.91 ? 419 ASP A O 1 ATOM 3217 C CB . ASP A 1 419 ? -57.695 25.000 51.199 1.00 12.77 ? 419 ASP A CB 1 ATOM 3218 C CG . ASP A 1 419 ? -58.944 24.376 51.790 1.00 13.79 ? 419 ASP A CG 1 ATOM 3219 O OD1 . ASP A 1 419 ? -59.133 23.138 51.686 1.00 14.85 ? 419 ASP A OD1 1 ATOM 3220 O OD2 . ASP A 1 419 ? -59.760 25.162 52.329 1.00 14.81 ? 419 ASP A OD2 1 ATOM 3221 N N . LEU A 1 420 ? -54.705 25.254 50.090 1.00 11.49 ? 420 LEU A N 1 ATOM 3222 C CA . LEU A 1 420 ? -53.787 25.927 49.150 1.00 11.45 ? 420 LEU A CA 1 ATOM 3223 C C . LEU A 1 420 ? -53.055 24.920 48.264 1.00 11.32 ? 420 LEU A C 1 ATOM 3224 O O . LEU A 1 420 ? -52.952 25.117 47.048 1.00 11.51 ? 420 LEU A O 1 ATOM 3225 C CB . LEU A 1 420 ? -52.837 26.885 49.855 1.00 11.32 ? 420 LEU A CB 1 ATOM 3226 C CG . LEU A 1 420 ? -53.511 28.188 50.322 1.00 11.37 ? 420 LEU A CG 1 ATOM 3227 C CD1 . LEU A 1 420 ? -52.746 28.800 51.488 1.00 11.44 ? 420 LEU A CD1 1 ATOM 3228 C CD2 . LEU A 1 420 ? -53.647 29.166 49.161 1.00 11.54 ? 420 LEU A CD2 1 ATOM 3229 N N . TRP A 1 421 ? -52.591 23.829 48.855 1.00 11.37 ? 421 TRP A N 1 ATOM 3230 C CA . TRP A 1 421 ? -52.011 22.759 48.042 1.00 11.39 ? 421 TRP A CA 1 ATOM 3231 C C . TRP A 1 421 ? -52.968 22.078 47.093 1.00 11.50 ? 421 TRP A C 1 ATOM 3232 O O . TRP A 1 421 ? -52.593 21.752 45.967 1.00 11.43 ? 421 TRP A O 1 ATOM 3233 C CB . TRP A 1 421 ? -51.281 21.750 48.909 1.00 11.43 ? 421 TRP A CB 1 ATOM 3234 C CG . TRP A 1 421 ? -49.931 22.280 49.231 1.00 11.45 ? 421 TRP A CG 1 ATOM 3235 C CD1 . TRP A 1 421 ? -49.466 22.725 50.455 1.00 11.68 ? 421 TRP A CD1 1 ATOM 3236 C CD2 . TRP A 1 421 ? -48.848 22.550 48.280 1.00 11.63 ? 421 TRP A CD2 1 ATOM 3237 N NE1 . TRP A 1 421 ? -48.179 23.187 50.332 1.00 11.89 ? 421 TRP A NE1 1 ATOM 3238 C CE2 . TRP A 1 421 ? -47.770 23.124 49.044 1.00 11.93 ? 421 TRP A CE2 1 ATOM 3239 C CE3 . TRP A 1 421 ? -48.681 22.352 46.903 1.00 11.66 ? 421 TRP A CE3 1 ATOM 3240 C CZ2 . TRP A 1 421 ? -46.556 23.489 48.451 1.00 12.04 ? 421 TRP A CZ2 1 ATOM 3241 C CZ3 . TRP A 1 421 ? -47.464 22.726 46.325 1.00 12.07 ? 421 TRP A CZ3 1 ATOM 3242 C CH2 . TRP A 1 421 ? -46.440 23.268 47.089 1.00 12.11 ? 421 TRP A CH2 1 ATOM 3243 N N . SER A 1 422 ? -54.211 21.861 47.525 1.00 11.57 ? 422 SER A N 1 ATOM 3244 C CA . SER A 1 422 ? -55.215 21.256 46.674 1.00 11.79 ? 422 SER A CA 1 ATOM 3245 C C . SER A 1 422 ? -55.507 22.133 45.455 1.00 11.84 ? 422 SER A C 1 ATOM 3246 O O . SER A 1 422 ? -55.631 21.641 44.353 1.00 11.48 ? 422 SER A O 1 ATOM 3247 C CB . SER A 1 422 ? -56.500 20.987 47.458 1.00 11.95 ? 422 SER A CB 1 ATOM 3248 O OG . SER A 1 422 ? -56.249 20.069 48.535 1.00 12.26 ? 422 SER A OG 1 ATOM 3249 N N . TYR A 1 423 ? -55.532 23.449 45.668 1.00 12.10 ? 423 TYR A N 1 ATOM 3250 C CA . TYR A 1 423 ? -55.666 24.420 44.588 1.00 12.43 ? 423 TYR A CA 1 ATOM 3251 C C . TYR A 1 423 ? -54.464 24.318 43.651 1.00 12.15 ? 423 TYR A C 1 ATOM 3252 O O . TYR A 1 423 ? -54.628 24.236 42.434 1.00 11.99 ? 423 TYR A O 1 ATOM 3253 C CB . TYR A 1 423 ? -55.786 25.857 45.138 1.00 12.81 ? 423 TYR A CB 1 ATOM 3254 C CG . TYR A 1 423 ? -55.851 26.866 44.023 1.00 13.41 ? 423 TYR A CG 1 ATOM 3255 C CD1 . TYR A 1 423 ? -57.042 27.103 43.374 1.00 13.93 ? 423 TYR A CD1 1 ATOM 3256 C CD2 . TYR A 1 423 ? -54.703 27.520 43.562 1.00 13.77 ? 423 TYR A CD2 1 ATOM 3257 C CE1 . TYR A 1 423 ? -57.119 27.981 42.301 1.00 14.46 ? 423 TYR A CE1 1 ATOM 3258 C CE2 . TYR A 1 423 ? -54.764 28.395 42.485 1.00 14.23 ? 423 TYR A CE2 1 ATOM 3259 C CZ . TYR A 1 423 ? -55.989 28.631 41.876 1.00 14.86 ? 423 TYR A CZ 1 ATOM 3260 O OH . TYR A 1 423 ? -56.106 29.484 40.801 1.00 16.25 ? 423 TYR A OH 1 ATOM 3261 N N . ASN A 1 424 ? -53.254 24.331 44.212 1.00 12.09 ? 424 ASN A N 1 ATOM 3262 C CA . ASN A 1 424 ? -52.058 24.271 43.366 1.00 12.23 ? 424 ASN A CA 1 ATOM 3263 C C . ASN A 1 424 ? -52.071 23.017 42.483 1.00 12.22 ? 424 ASN A C 1 ATOM 3264 O O . ASN A 1 424 ? -51.752 23.079 41.277 1.00 12.28 ? 424 ASN A O 1 ATOM 3265 C CB . ASN A 1 424 ? -50.778 24.263 44.196 1.00 12.29 ? 424 ASN A CB 1 ATOM 3266 C CG . ASN A 1 424 ? -50.477 25.597 44.836 1.00 12.47 ? 424 ASN A CG 1 ATOM 3267 O OD1 . ASN A 1 424 ? -50.967 26.640 44.385 1.00 12.68 ? 424 ASN A OD1 1 ATOM 3268 N ND2 . ASN A 1 424 ? -49.629 25.580 45.843 1.00 12.29 ? 424 ASN A ND2 1 ATOM 3269 N N . ALA A 1 425 ? -52.457 21.901 43.080 1.00 12.24 ? 425 ALA A N 1 ATOM 3270 C CA . ALA A 1 425 ? -52.504 20.618 42.370 1.00 12.70 ? 425 ALA A CA 1 ATOM 3271 C C . ALA A 1 425 ? -53.501 20.654 41.225 1.00 13.16 ? 425 ALA A C 1 ATOM 3272 O O . ALA A 1 425 ? -53.189 20.225 40.118 1.00 13.62 ? 425 ALA A O 1 ATOM 3273 C CB . ALA A 1 425 ? -52.830 19.461 43.331 1.00 12.39 ? 425 ALA A CB 1 ATOM 3274 N N . GLU A 1 426 ? -54.696 21.160 41.497 1.00 13.88 ? 426 GLU A N 1 ATOM 3275 C CA . GLU A 1 426 ? -55.731 21.305 40.487 1.00 14.82 ? 426 GLU A CA 1 ATOM 3276 C C . GLU A 1 426 ? -55.266 22.180 39.310 1.00 14.51 ? 426 GLU A C 1 ATOM 3277 O O . GLU A 1 426 ? -55.400 21.780 38.148 1.00 14.71 ? 426 GLU A O 1 ATOM 3278 C CB . GLU A 1 426 ? -57.019 21.851 41.109 1.00 15.99 ? 426 GLU A CB 1 ATOM 3279 C CG . GLU A 1 426 ? -58.246 21.723 40.203 1.00 17.59 ? 426 GLU A CG 1 ATOM 3280 C CD . GLU A 1 426 ? -58.828 20.312 40.146 1.00 19.09 ? 426 GLU A CD 1 ATOM 3281 O OE1 . GLU A 1 426 ? -58.810 19.595 41.163 1.00 19.71 ? 426 GLU A OE1 1 ATOM 3282 O OE2 . GLU A 1 426 ? -59.308 19.908 39.059 1.00 22.09 ? 426 GLU A OE2 1 ATOM 3283 N N . LEU A 1 427 ? -54.702 23.341 39.594 1.00 14.55 ? 427 LEU A N 1 ATOM 3284 C CA . LEU A 1 427 ? -54.224 24.232 38.534 1.00 14.78 ? 427 LEU A CA 1 ATOM 3285 C C . LEU A 1 427 ? -53.050 23.608 37.766 1.00 14.85 ? 427 LEU A C 1 ATOM 3286 O O . LEU A 1 427 ? -53.006 23.685 36.533 1.00 14.91 ? 427 LEU A O 1 ATOM 3287 C CB . LEU A 1 427 ? -53.813 25.575 39.110 1.00 15.03 ? 427 LEU A CB 1 ATOM 3288 C CG . LEU A 1 427 ? -53.322 26.634 38.137 1.00 15.40 ? 427 LEU A CG 1 ATOM 3289 C CD1 . LEU A 1 427 ? -54.440 26.963 37.128 1.00 15.74 ? 427 LEU A CD1 1 ATOM 3290 C CD2 . LEU A 1 427 ? -52.898 27.872 38.922 1.00 15.62 ? 427 LEU A CD2 1 ATOM 3291 N N . LEU A 1 428 ? -52.123 22.981 38.486 1.00 14.85 ? 428 LEU A N 1 ATOM 3292 C CA . LEU A 1 428 ? -50.915 22.413 37.869 1.00 15.73 ? 428 LEU A CA 1 ATOM 3293 C C . LEU A 1 428 ? -51.292 21.362 36.831 1.00 15.62 ? 428 LEU A C 1 ATOM 3294 O O . LEU A 1 428 ? -50.790 21.372 35.685 1.00 15.43 ? 428 LEU A O 1 ATOM 3295 C CB . LEU A 1 428 ? -49.980 21.808 38.920 1.00 16.31 ? 428 LEU A CB 1 ATOM 3296 C CG . LEU A 1 428 ? -48.662 21.221 38.379 1.00 17.24 ? 428 LEU A CG 1 ATOM 3297 C CD1 . LEU A 1 428 ? -47.891 22.274 37.590 1.00 18.78 ? 428 LEU A CD1 1 ATOM 3298 C CD2 . LEU A 1 428 ? -47.805 20.681 39.515 1.00 18.08 ? 428 LEU A CD2 1 ATOM 3299 N N . VAL A 1 429 ? -52.227 20.501 37.194 1.00 16.07 ? 429 VAL A N 1 ATOM 3300 C CA . VAL A 1 429 ? -52.583 19.404 36.303 1.00 16.82 ? 429 VAL A CA 1 ATOM 3301 C C . VAL A 1 429 ? -53.342 19.952 35.085 1.00 16.86 ? 429 VAL A C 1 ATOM 3302 O O . VAL A 1 429 ? -53.077 19.530 33.945 1.00 17.28 ? 429 VAL A O 1 ATOM 3303 C CB . VAL A 1 429 ? -53.323 18.283 37.056 1.00 17.32 ? 429 VAL A CB 1 ATOM 3304 C CG1 . VAL A 1 429 ? -53.784 17.180 36.100 1.00 18.30 ? 429 VAL A CG1 1 ATOM 3305 C CG2 . VAL A 1 429 ? -52.380 17.699 38.103 1.00 17.50 ? 429 VAL A CG2 1 ATOM 3306 N N . ALA A 1 430 ? -54.231 20.919 35.304 1.00 16.45 ? 430 ALA A N 1 ATOM 3307 C CA . ALA A 1 430 ? -54.954 21.545 34.210 1.00 17.02 ? 430 ALA A CA 1 ATOM 3308 C C . ALA A 1 430 ? -53.997 22.259 33.221 1.00 16.80 ? 430 ALA A C 1 ATOM 3309 O O . ALA A 1 430 ? -54.121 22.100 31.986 1.00 16.83 ? 430 ALA A O 1 ATOM 3310 C CB . ALA A 1 430 ? -56.006 22.517 34.726 1.00 16.58 ? 430 ALA A CB 1 ATOM 3311 N N . LEU A 1 431 ? -53.059 23.020 33.768 1.00 16.54 ? 431 LEU A N 1 ATOM 3312 C CA . LEU A 1 431 ? -52.033 23.702 32.967 1.00 17.09 ? 431 LEU A CA 1 ATOM 3313 C C . LEU A 1 431 ? -51.133 22.721 32.212 1.00 17.13 ? 431 LEU A C 1 ATOM 3314 O O . LEU A 1 431 ? -50.879 22.915 31.025 1.00 17.96 ? 431 LEU A O 1 ATOM 3315 C CB . LEU A 1 431 ? -51.169 24.595 33.840 1.00 17.22 ? 431 LEU A CB 1 ATOM 3316 C CG . LEU A 1 431 ? -51.834 25.879 34.336 1.00 17.86 ? 431 LEU A CG 1 ATOM 3317 C CD1 . LEU A 1 431 ? -50.873 26.586 35.274 1.00 17.99 ? 431 LEU A CD1 1 ATOM 3318 C CD2 . LEU A 1 431 ? -52.236 26.792 33.184 1.00 18.41 ? 431 LEU A CD2 1 ATOM 3319 N N . GLU A 1 432 ? -50.631 21.698 32.896 1.00 17.50 ? 432 GLU A N 1 ATOM 3320 C CA . GLU A 1 432 ? -49.789 20.712 32.251 1.00 18.42 ? 432 GLU A CA 1 ATOM 3321 C C . GLU A 1 432 ? -50.538 19.981 31.143 1.00 17.71 ? 432 GLU A C 1 ATOM 3322 O O . GLU A 1 432 ? -49.971 19.760 30.073 1.00 17.84 ? 432 GLU A O 1 ATOM 3323 C CB . GLU A 1 432 ? -49.224 19.721 33.250 1.00 19.93 ? 432 GLU A CB 1 ATOM 3324 C CG . GLU A 1 432 ? -48.182 20.347 34.166 1.00 22.03 ? 432 GLU A CG 1 ATOM 3325 C CD . GLU A 1 432 ? -46.791 20.448 33.569 1.00 25.71 ? 432 GLU A CD 1 ATOM 3326 O OE1 . GLU A 1 432 ? -46.607 20.240 32.345 1.00 26.44 ? 432 GLU A OE1 1 ATOM 3327 O OE2 . GLU A 1 432 ? -45.865 20.744 34.364 1.00 29.57 ? 432 GLU A OE2 1 ATOM 3328 N N . ASN A 1 433 ? -51.791 19.597 31.398 1.00 16.94 ? 433 ASN A N 1 ATOM 3329 C CA . ASN A 1 433 ? -52.588 18.882 30.413 1.00 16.87 ? 433 ASN A CA 1 ATOM 3330 C C . ASN A 1 433 ? -52.897 19.749 29.182 1.00 17.47 ? 433 ASN A C 1 ATOM 3331 O O . ASN A 1 433 ? -52.787 19.275 28.038 1.00 17.25 ? 433 ASN A O 1 ATOM 3332 C CB . ASN A 1 433 ? -53.867 18.331 31.030 1.00 16.42 ? 433 ASN A CB 1 ATOM 3333 C CG . ASN A 1 433 ? -53.614 17.169 31.981 1.00 15.98 ? 433 ASN A CG 1 ATOM 3334 O OD1 . ASN A 1 433 ? -52.521 16.617 32.042 1.00 16.05 ? 433 ASN A OD1 1 ATOM 3335 N ND2 . ASN A 1 433 ? -54.638 16.782 32.718 1.00 15.75 ? 433 ASN A ND2 1 ATOM 3336 N N . GLN A 1 434 ? -53.208 21.024 29.400 1.00 17.82 ? 434 GLN A N 1 ATOM 3337 C CA . GLN A 1 434 ? -53.358 21.959 28.295 1.00 19.13 ? 434 GLN A CA 1 ATOM 3338 C C . GLN A 1 434 ? -52.074 22.039 27.470 1.00 18.72 ? 434 GLN A C 1 ATOM 3339 O O . GLN A 1 434 ? -52.118 22.033 26.238 1.00 18.55 ? 434 GLN A O 1 ATOM 3340 C CB . GLN A 1 434 ? -53.736 23.362 28.779 1.00 20.83 ? 434 GLN A CB 1 ATOM 3341 C CG . GLN A 1 434 ? -54.085 24.305 27.630 1.00 22.62 ? 434 GLN A CG 1 ATOM 3342 C CD . GLN A 1 434 ? -55.315 23.826 26.902 1.00 25.08 ? 434 GLN A CD 1 ATOM 3343 O OE1 . GLN A 1 434 ? -56.388 23.703 27.514 1.00 26.67 ? 434 GLN A OE1 1 ATOM 3344 N NE2 . GLN A 1 434 ? -55.162 23.458 25.599 1.00 27.10 ? 434 GLN A NE2 1 ATOM 3345 N N . HIS A 1 435 ? -50.944 22.083 28.150 1.00 19.16 ? 435 HIS A N 1 ATOM 3346 C CA . HIS A 1 435 ? -49.646 22.167 27.467 1.00 20.04 ? 435 HIS A CA 1 ATOM 3347 C C . HIS A 1 435 ? -49.363 20.908 26.656 1.00 19.81 ? 435 HIS A C 1 ATOM 3348 O O . HIS A 1 435 ? -48.865 20.989 25.524 1.00 20.20 ? 435 HIS A O 1 ATOM 3349 C CB . HIS A 1 435 ? -48.546 22.437 28.487 1.00 21.29 ? 435 HIS A CB 1 ATOM 3350 C CG . HIS A 1 435 ? -47.169 22.542 27.884 1.00 22.72 ? 435 HIS A CG 1 ATOM 3351 N ND1 . HIS A 1 435 ? -46.294 21.511 27.904 1.00 23.97 ? 435 HIS A ND1 1 ATOM 3352 C CD2 . HIS A 1 435 ? -46.531 23.591 27.246 1.00 24.14 ? 435 HIS A CD2 1 ATOM 3353 C CE1 . HIS A 1 435 ? -45.152 21.887 27.293 1.00 24.96 ? 435 HIS A CE1 1 ATOM 3354 N NE2 . HIS A 1 435 ? -45.293 23.161 26.897 1.00 24.97 ? 435 HIS A NE2 1 ATOM 3355 N N . THR A 1 436 ? -49.721 19.754 27.201 1.00 18.97 ? 436 THR A N 1 ATOM 3356 C CA . THR A 1 436 ? -49.548 18.473 26.501 1.00 19.13 ? 436 THR A CA 1 ATOM 3357 C C . THR A 1 436 ? -50.409 18.394 25.245 1.00 19.64 ? 436 THR A C 1 ATOM 3358 O O . THR A 1 436 ? -49.907 17.989 24.170 1.00 19.88 ? 436 THR A O 1 ATOM 3359 C CB . THR A 1 436 ? -49.812 17.295 27.437 1.00 19.20 ? 436 THR A CB 1 ATOM 3360 O OG1 . THR A 1 436 ? -48.814 17.295 28.472 1.00 18.60 ? 436 THR A OG1 1 ATOM 3361 C CG2 . THR A 1 436 ? -49.782 15.932 26.652 1.00 18.92 ? 436 THR A CG2 1 ATOM 3362 N N . ILE A 1 437 ? -51.682 18.780 25.349 1.00 19.09 ? 437 ILE A N 1 ATOM 3363 C CA . ILE A 1 437 ? -52.550 18.845 24.182 1.00 20.39 ? 437 ILE A CA 1 ATOM 3364 C C . ILE A 1 437 ? -51.945 19.810 23.147 1.00 21.10 ? 437 ILE A C 1 ATOM 3365 O O . ILE A 1 437 ? -51.829 19.489 21.950 1.00 19.67 ? 437 ILE A O 1 ATOM 3366 C CB . ILE A 1 437 ? -53.974 19.297 24.562 1.00 20.77 ? 437 ILE A CB 1 ATOM 3367 C CG1 . ILE A 1 437 ? -54.653 18.275 25.467 1.00 21.46 ? 437 ILE A CG1 1 ATOM 3368 C CG2 . ILE A 1 437 ? -54.830 19.545 23.330 1.00 21.70 ? 437 ILE A CG2 1 ATOM 3369 C CD1 . ILE A 1 437 ? -54.588 16.851 24.974 1.00 22.56 ? 437 ILE A CD1 1 ATOM 3370 N N . ASP A 1 438 ? -51.540 20.990 23.612 1.00 20.50 ? 438 ASP A N 1 ATOM 3371 C CA . ASP A 1 438 ? -50.895 21.978 22.721 1.00 21.64 ? 438 ASP A CA 1 ATOM 3372 C C . ASP A 1 438 ? -49.616 21.475 22.040 1.00 21.14 ? 438 ASP A C 1 ATOM 3373 O O . ASP A 1 438 ? -49.476 21.633 20.833 1.00 23.04 ? 438 ASP A O 1 ATOM 3374 C CB . ASP A 1 438 ? -50.582 23.268 23.480 1.00 22.57 ? 438 ASP A CB 1 ATOM 3375 C CG . ASP A 1 438 ? -51.822 24.053 23.872 1.00 23.78 ? 438 ASP A CG 1 ATOM 3376 O OD1 . ASP A 1 438 ? -52.940 23.695 23.463 1.00 25.95 ? 438 ASP A OD1 1 ATOM 3377 O OD2 . ASP A 1 438 ? -51.656 25.049 24.635 1.00 25.70 ? 438 ASP A OD2 1 ATOM 3378 N N . LEU A 1 439 ? -48.710 20.855 22.778 1.00 20.70 ? 439 LEU A N 1 ATOM 3379 C CA . LEU A 1 439 ? -47.441 20.400 22.211 1.00 21.25 ? 439 LEU A CA 1 ATOM 3380 C C . LEU A 1 439 ? -47.638 19.220 21.228 1.00 21.57 ? 439 LEU A C 1 ATOM 3381 O O . LEU A 1 439 ? -46.936 19.123 20.229 1.00 21.35 ? 439 LEU A O 1 ATOM 3382 C CB . LEU A 1 439 ? -46.445 20.041 23.302 1.00 22.16 ? 439 LEU A CB 1 ATOM 3383 C CG . LEU A 1 439 ? -46.420 18.695 24.044 1.00 22.40 ? 439 LEU A CG 1 ATOM 3384 C CD1 . LEU A 1 439 ? -45.711 17.573 23.270 1.00 22.66 ? 439 LEU A CD1 1 ATOM 3385 C CD2 . LEU A 1 439 ? -45.717 18.874 25.397 1.00 22.75 ? 439 LEU A CD2 1 ATOM 3386 N N . THR A 1 440 ? -48.615 18.362 21.504 1.00 20.65 ? 440 THR A N 1 ATOM 3387 C CA . THR A 1 440 ? -48.889 17.231 20.608 1.00 21.55 ? 440 THR A CA 1 ATOM 3388 C C . THR A 1 440 ? -49.634 17.701 19.360 1.00 22.42 ? 440 THR A C 1 ATOM 3389 O O . THR A 1 440 ? -49.334 17.228 18.233 1.00 24.42 ? 440 THR A O 1 ATOM 3390 C CB . THR A 1 440 ? -49.619 16.081 21.327 1.00 20.78 ? 440 THR A CB 1 ATOM 3391 O OG1 . THR A 1 440 ? -50.752 16.586 22.025 1.00 20.05 ? 440 THR A OG1 1 ATOM 3392 C CG2 . THR A 1 440 ? -48.699 15.370 22.303 1.00 21.01 ? 440 THR A CG2 1 ATOM 3393 N N . ASP A 1 441 ? -50.577 18.633 19.520 1.00 22.39 ? 441 ASP A N 1 ATOM 3394 C CA . ASP A 1 441 ? -51.217 19.265 18.372 1.00 23.58 ? 441 ASP A CA 1 ATOM 3395 C C . ASP A 1 441 ? -50.149 19.963 17.518 1.00 25.11 ? 441 ASP A C 1 ATOM 3396 O O . ASP A 1 441 ? -50.185 19.898 16.274 1.00 24.73 ? 441 ASP A O 1 ATOM 3397 C CB . ASP A 1 441 ? -52.250 20.316 18.774 1.00 23.75 ? 441 ASP A CB 1 ATOM 3398 C CG . ASP A 1 441 ? -53.580 19.734 19.258 1.00 24.52 ? 441 ASP A CG 1 ATOM 3399 O OD1 . ASP A 1 441 ? -53.828 18.521 19.165 1.00 24.59 ? 441 ASP A OD1 1 ATOM 3400 O OD2 . ASP A 1 441 ? -54.418 20.539 19.721 1.00 25.67 ? 441 ASP A OD2 1 ATOM 3401 N N . SER A 1 442 ? -49.225 20.655 18.193 1.00 25.22 ? 442 SER A N 1 ATOM 3402 C CA . SER A 1 442 ? -48.177 21.396 17.493 1.00 26.23 ? 442 SER A CA 1 ATOM 3403 C C . SER A 1 442 ? -47.276 20.492 16.632 1.00 26.11 ? 442 SER A C 1 ATOM 3404 O O . SER A 1 442 ? -46.977 20.857 15.485 1.00 27.37 ? 442 SER A O 1 ATOM 3405 C CB . SER A 1 442 ? -47.337 22.241 18.463 1.00 26.80 ? 442 SER A CB 1 ATOM 3406 O OG . SER A 1 442 ? -46.251 22.846 17.756 1.00 28.22 ? 442 SER A OG 1 ATOM 3407 N N . GLU A 1 443 ? -46.844 19.345 17.152 1.00 25.56 ? 443 GLU A N 1 ATOM 3408 C CA . GLU A 1 443 ? -46.025 18.418 16.353 1.00 26.93 ? 443 GLU A CA 1 ATOM 3409 C C . GLU A 1 443 ? -46.752 17.975 15.074 1.00 26.53 ? 443 GLU A C 1 ATOM 3410 O O . GLU A 1 443 ? -46.119 17.845 14.035 1.00 28.53 ? 443 GLU A O 1 ATOM 3411 C CB . GLU A 1 443 ? -45.545 17.207 17.156 1.00 27.30 ? 443 GLU A CB 1 ATOM 3412 C CG . GLU A 1 443 ? -44.530 17.513 18.258 1.00 28.81 ? 443 GLU A CG 1 ATOM 3413 C CD . GLU A 1 443 ? -43.274 18.217 17.753 1.00 29.83 ? 443 GLU A CD 1 ATOM 3414 O OE1 . GLU A 1 443 ? -42.779 17.872 16.657 1.00 31.06 ? 443 GLU A OE1 1 ATOM 3415 O OE2 . GLU A 1 443 ? -42.778 19.123 18.450 1.00 31.09 ? 443 GLU A OE2 1 ATOM 3416 N N . MET A 1 444 ? -48.066 17.787 15.139 1.00 26.37 ? 444 MET A N 1 ATOM 3417 C CA . MET A 1 444 ? -48.851 17.405 13.958 1.00 25.63 ? 444 MET A CA 1 ATOM 3418 C C . MET A 1 444 ? -48.841 18.558 12.957 1.00 27.22 ? 444 MET A C 1 ATOM 3419 O O . MET A 1 444 ? -48.576 18.366 11.761 1.00 26.37 ? 444 MET A O 1 ATOM 3420 C CB . MET A 1 444 ? -50.299 17.070 14.334 1.00 24.89 ? 444 MET A CB 1 ATOM 3421 C CG . MET A 1 444 ? -51.180 16.635 13.161 1.00 24.66 ? 444 MET A CG 1 ATOM 3422 S SD . MET A 1 444 ? -50.860 14.917 12.675 1.00 24.15 ? 444 MET A SD 1 ATOM 3423 C CE . MET A 1 444 ? -49.515 15.070 11.514 1.00 25.80 ? 444 MET A CE 1 ATOM 3424 N N . ASN A 1 445 ? -49.132 19.760 13.443 1.00 27.58 ? 445 ASN A N 1 ATOM 3425 C CA . ASN A 1 445 ? -49.175 20.942 12.575 1.00 29.43 ? 445 ASN A CA 1 ATOM 3426 C C . ASN A 1 445 ? -47.818 21.243 11.948 1.00 28.27 ? 445 ASN A C 1 ATOM 3427 O O . ASN A 1 445 ? -47.753 21.579 10.768 1.00 28.43 ? 445 ASN A O 1 ATOM 3428 C CB . ASN A 1 445 ? -49.696 22.177 13.335 1.00 31.55 ? 445 ASN A CB 1 ATOM 3429 C CG . ASN A 1 445 ? -51.168 22.055 13.715 1.00 34.46 ? 445 ASN A CG 1 ATOM 3430 O OD1 . ASN A 1 445 ? -51.970 21.461 12.991 1.00 35.35 ? 445 ASN A OD1 1 ATOM 3431 N ND2 . ASN A 1 445 ? -51.528 22.632 14.860 1.00 37.16 ? 445 ASN A ND2 1 ATOM 3432 N N . LYS A 1 446 ? -46.745 21.081 12.717 1.00 28.67 ? 446 LYS A N 1 ATOM 3433 C CA . LYS A 1 446 ? -45.394 21.329 12.203 1.00 30.96 ? 446 LYS A CA 1 ATOM 3434 C C . LYS A 1 446 ? -45.059 20.348 11.060 1.00 31.10 ? 446 LYS A C 1 ATOM 3435 O O . LYS A 1 446 ? -44.531 20.754 10.018 1.00 30.68 ? 446 LYS A O 1 ATOM 3436 C CB . LYS A 1 446 ? -44.346 21.255 13.318 1.00 33.21 ? 446 LYS A CB 1 ATOM 3437 C CG . LYS A 1 446 ? -44.347 22.494 14.228 1.00 34.97 ? 446 LYS A CG 1 ATOM 3438 C CD . LYS A 1 446 ? -43.861 22.208 15.644 1.00 37.66 ? 446 LYS A CD 1 ATOM 3439 C CE . LYS A 1 446 ? -42.442 21.691 15.716 1.00 38.84 ? 446 LYS A CE 1 ATOM 3440 N NZ . LYS A 1 446 ? -42.003 21.512 17.130 1.00 41.13 ? 446 LYS A NZ 1 ATOM 3441 N N . LEU A 1 447 ? -45.412 19.078 11.244 1.00 29.30 ? 447 LEU A N 1 ATOM 3442 C CA . LEU A 1 447 ? -45.149 18.057 10.234 1.00 29.25 ? 447 LEU A CA 1 ATOM 3443 C C . LEU A 1 447 ? -45.912 18.369 8.944 1.00 28.14 ? 447 LEU A C 1 ATOM 3444 O O . LEU A 1 447 ? -45.378 18.225 7.835 1.00 28.73 ? 447 LEU A O 1 ATOM 3445 C CB . LEU A 1 447 ? -45.536 16.686 10.783 1.00 29.98 ? 447 LEU A CB 1 ATOM 3446 C CG . LEU A 1 447 ? -45.262 15.464 9.898 1.00 31.34 ? 447 LEU A CG 1 ATOM 3447 C CD1 . LEU A 1 447 ? -43.772 15.370 9.556 1.00 31.41 ? 447 LEU A CD1 1 ATOM 3448 C CD2 . LEU A 1 447 ? -45.755 14.212 10.596 1.00 31.26 ? 447 LEU A CD2 1 ATOM 3449 N N . PHE A 1 448 ? -47.161 18.802 9.074 1.00 26.85 ? 448 PHE A N 1 ATOM 3450 C CA . PHE A 1 448 ? -47.949 19.175 7.916 1.00 27.12 ? 448 PHE A CA 1 ATOM 3451 C C . PHE A 1 448 ? -47.329 20.363 7.193 1.00 28.27 ? 448 PHE A C 1 ATOM 3452 O O . PHE A 1 448 ? -47.227 20.368 5.959 1.00 26.55 ? 448 PHE A O 1 ATOM 3453 C CB . PHE A 1 448 ? -49.384 19.492 8.330 1.00 26.75 ? 448 PHE A CB 1 ATOM 3454 C CG . PHE A 1 448 ? -50.293 19.802 7.186 1.00 26.58 ? 448 PHE A CG 1 ATOM 3455 C CD1 . PHE A 1 448 ? -50.921 18.792 6.481 1.00 26.77 ? 448 PHE A CD1 1 ATOM 3456 C CD2 . PHE A 1 448 ? -50.518 21.119 6.800 1.00 27.20 ? 448 PHE A CD2 1 ATOM 3457 C CE1 . PHE A 1 448 ? -51.760 19.086 5.422 1.00 27.06 ? 448 PHE A CE1 1 ATOM 3458 C CE2 . PHE A 1 448 ? -51.357 21.417 5.743 1.00 26.95 ? 448 PHE A CE2 1 ATOM 3459 C CZ . PHE A 1 448 ? -51.988 20.399 5.058 1.00 27.45 ? 448 PHE A CZ 1 ATOM 3460 N N . GLU A 1 449 ? -46.924 21.377 7.957 1.00 29.39 ? 449 GLU A N 1 ATOM 3461 C CA . GLU A 1 449 ? -46.365 22.583 7.348 1.00 32.52 ? 449 GLU A CA 1 ATOM 3462 C C . GLU A 1 449 ? -45.059 22.317 6.639 1.00 30.91 ? 449 GLU A C 1 ATOM 3463 O O . GLU A 1 449 ? -44.843 22.834 5.543 1.00 30.89 ? 449 GLU A O 1 ATOM 3464 C CB . GLU A 1 449 ? -46.185 23.692 8.395 1.00 35.90 ? 449 GLU A CB 1 ATOM 3465 C CG . GLU A 1 449 ? -47.507 24.336 8.776 1.00 39.56 ? 449 GLU A CG 1 ATOM 3466 C CD . GLU A 1 449 ? -48.185 24.997 7.587 1.00 43.45 ? 449 GLU A CD 1 ATOM 3467 O OE1 . GLU A 1 449 ? -47.521 25.823 6.909 1.00 47.09 ? 449 GLU A OE1 1 ATOM 3468 O OE2 . GLU A 1 449 ? -49.369 24.672 7.322 1.00 44.05 ? 449 GLU A OE2 1 ATOM 3469 N N . ARG A 1 450 ? -44.179 21.522 7.233 1.00 31.75 ? 450 ARG A N 1 ATOM 3470 C CA . ARG A 1 450 ? -42.918 21.251 6.564 1.00 33.57 ? 450 ARG A CA 1 ATOM 3471 C C . ARG A 1 450 ? -43.089 20.413 5.290 1.00 31.50 ? 450 ARG A C 1 ATOM 3472 O O . ARG A 1 450 ? -42.360 20.608 4.309 1.00 29.92 ? 450 ARG A O 1 ATOM 3473 C CB . ARG A 1 450 ? -41.846 20.719 7.516 1.00 38.12 ? 450 ARG A CB 1 ATOM 3474 C CG . ARG A 1 450 ? -41.905 19.297 8.038 1.00 41.34 ? 450 ARG A CG 1 ATOM 3475 C CD . ARG A 1 450 ? -40.869 19.173 9.176 1.00 45.91 ? 450 ARG A CD 1 ATOM 3476 N NE . ARG A 1 450 ? -40.825 17.833 9.787 1.00 48.69 ? 450 ARG A NE 1 ATOM 3477 C CZ . ARG A 1 450 ? -41.230 17.516 11.027 1.00 49.67 ? 450 ARG A CZ 1 ATOM 3478 N NH1 . ARG A 1 450 ? -41.721 18.437 11.860 1.00 47.58 ? 450 ARG A NH1 1 ATOM 3479 N NH2 . ARG A 1 450 ? -41.132 16.247 11.445 1.00 48.99 ? 450 ARG A NH2 1 ATOM 3480 N N . THR A 1 451 ? -44.080 19.532 5.278 1.00 28.61 ? 451 THR A N 1 ATOM 3481 C CA . THR A 1 451 ? -44.406 18.762 4.067 1.00 27.17 ? 451 THR A CA 1 ATOM 3482 C C . THR A 1 451 ? -44.928 19.700 2.988 1.00 27.37 ? 451 THR A C 1 ATOM 3483 O O . THR A 1 451 ? -44.509 19.633 1.841 1.00 27.07 ? 451 THR A O 1 ATOM 3484 C CB . THR A 1 451 ? -45.430 17.654 4.397 1.00 26.13 ? 451 THR A CB 1 ATOM 3485 O OG1 . THR A 1 451 ? -44.891 16.830 5.441 1.00 25.13 ? 451 THR A OG1 1 ATOM 3486 C CG2 . THR A 1 451 ? -45.744 16.799 3.185 1.00 24.77 ? 451 THR A CG2 1 ATOM 3487 N N . LYS A 1 452 ? -45.819 20.602 3.368 1.00 28.23 ? 452 LYS A N 1 ATOM 3488 C CA . LYS A 1 452 ? -46.320 21.627 2.470 1.00 29.77 ? 452 LYS A CA 1 ATOM 3489 C C . LYS A 1 452 ? -45.177 22.412 1.830 1.00 30.67 ? 452 LYS A C 1 ATOM 3490 O O . LYS A 1 452 ? -45.203 22.692 0.619 1.00 28.81 ? 452 LYS A O 1 ATOM 3491 C CB . LYS A 1 452 ? -47.244 22.590 3.220 1.00 31.91 ? 452 LYS A CB 1 ATOM 3492 C CG . LYS A 1 452 ? -47.867 23.652 2.330 1.00 34.70 ? 452 LYS A CG 1 ATOM 3493 C CD . LYS A 1 452 ? -48.661 24.667 3.126 1.00 38.35 ? 452 LYS A CD 1 ATOM 3494 C CE . LYS A 1 452 ? -49.380 25.622 2.182 1.00 41.72 ? 452 LYS A CE 1 ATOM 3495 N NZ . LYS A 1 452 ? -50.187 24.859 1.171 1.00 43.35 ? 452 LYS A NZ 1 ATOM 3496 N N . LYS A 1 453 ? -44.176 22.755 2.634 1.00 31.34 ? 453 LYS A N 1 ATOM 3497 C CA . LYS A 1 453 ? -43.078 23.589 2.139 1.00 33.26 ? 453 LYS A CA 1 ATOM 3498 C C . LYS A 1 453 ? -42.218 22.810 1.137 1.00 31.74 ? 453 LYS A C 1 ATOM 3499 O O . LYS A 1 453 ? -41.799 23.374 0.126 1.00 32.57 ? 453 LYS A O 1 ATOM 3500 C CB . LYS A 1 453 ? -42.211 24.124 3.284 1.00 34.97 ? 453 LYS A CB 1 ATOM 3501 C CG . LYS A 1 453 ? -42.976 24.832 4.392 1.00 36.37 ? 453 LYS A CG 1 ATOM 3502 C CD . LYS A 1 453 ? -42.979 26.343 4.324 1.00 37.32 ? 453 LYS A CD 1 ATOM 3503 C CE . LYS A 1 453 ? -43.597 26.912 5.594 1.00 37.95 ? 453 LYS A CE 1 ATOM 3504 N NZ . LYS A 1 453 ? -43.731 28.388 5.632 1.00 37.93 ? 453 LYS A NZ 1 ATOM 3505 N N . GLN A 1 454 ? -41.973 21.523 1.404 1.00 30.87 ? 454 GLN A N 1 ATOM 3506 C CA . GLN A 1 454 ? -41.201 20.680 0.492 1.00 30.97 ? 454 GLN A CA 1 ATOM 3507 C C . GLN A 1 454 ? -41.836 20.627 -0.894 1.00 28.44 ? 454 GLN A C 1 ATOM 3508 O O . GLN A 1 454 ? -41.134 20.624 -1.921 1.00 28.28 ? 454 GLN A O 1 ATOM 3509 C CB . GLN A 1 454 ? -41.109 19.241 0.998 1.00 32.24 ? 454 GLN A CB 1 ATOM 3510 C CG . GLN A 1 454 ? -40.038 18.976 2.019 1.00 34.76 ? 454 GLN A CG 1 ATOM 3511 C CD . GLN A 1 454 ? -39.906 17.496 2.320 1.00 35.73 ? 454 GLN A CD 1 ATOM 3512 O OE1 . GLN A 1 454 ? -39.106 16.804 1.710 1.00 36.68 ? 454 GLN A OE1 1 ATOM 3513 N NE2 . GLN A 1 454 ? -40.694 17.012 3.260 1.00 34.92 ? 454 GLN A NE2 1 ATOM 3514 N N . LEU A 1 455 ? -43.160 20.531 -0.904 1.00 26.24 ? 455 LEU A N 1 ATOM 3515 C CA . LEU A 1 455 ? -43.918 20.253 -2.121 1.00 25.05 ? 455 LEU A CA 1 ATOM 3516 C C . LEU A 1 455 ? -44.015 21.455 -3.035 1.00 25.22 ? 455 LEU A C 1 ATOM 3517 O O . LEU A 1 455 ? -44.209 21.290 -4.227 1.00 23.81 ? 455 LEU A O 1 ATOM 3518 C CB . LEU A 1 455 ? -45.316 19.721 -1.764 1.00 24.39 ? 455 LEU A CB 1 ATOM 3519 C CG . LEU A 1 455 ? -45.245 18.338 -1.111 1.00 23.69 ? 455 LEU A CG 1 ATOM 3520 C CD1 . LEU A 1 455 ? -46.605 17.887 -0.588 1.00 22.58 ? 455 LEU A CD1 1 ATOM 3521 C CD2 . LEU A 1 455 ? -44.679 17.315 -2.101 1.00 23.70 ? 455 LEU A CD2 1 ATOM 3522 N N . ARG A 1 456 ? -43.864 22.663 -2.483 1.00 26.38 ? 456 ARG A N 1 ATOM 3523 C CA . ARG A 1 456 ? -43.868 23.899 -3.282 1.00 27.88 ? 456 ARG A CA 1 ATOM 3524 C C . ARG A 1 456 ? -45.096 23.949 -4.183 1.00 27.16 ? 456 ARG A C 1 ATOM 3525 O O . ARG A 1 456 ? -46.200 23.788 -3.704 1.00 26.58 ? 456 ARG A O 1 ATOM 3526 C CB . ARG A 1 456 ? -42.576 24.059 -4.093 1.00 29.64 ? 456 ARG A CB 1 ATOM 3527 C CG . ARG A 1 456 ? -41.341 24.378 -3.278 1.00 31.14 ? 456 ARG A CG 1 ATOM 3528 C CD . ARG A 1 456 ? -41.238 25.858 -2.966 1.00 32.50 ? 456 ARG A CD 1 ATOM 3529 N NE . ARG A 1 456 ? -40.928 26.717 -4.115 1.00 33.23 ? 456 ARG A NE 1 ATOM 3530 C CZ . ARG A 1 456 ? -39.709 27.138 -4.470 1.00 33.54 ? 456 ARG A CZ 1 ATOM 3531 N NH1 . ARG A 1 456 ? -38.610 26.750 -3.821 1.00 33.65 ? 456 ARG A NH1 1 ATOM 3532 N NH2 . ARG A 1 456 ? -39.579 27.950 -5.509 1.00 34.47 ? 456 ARG A NH2 1 ATOM 3533 N N . GLU A 1 457 ? -44.913 24.113 -5.488 1.00 28.01 ? 457 GLU A N 1 ATOM 3534 C CA . GLU A 1 457 ? -46.039 24.240 -6.405 1.00 28.48 ? 457 GLU A CA 1 ATOM 3535 C C . GLU A 1 457 ? -46.465 22.896 -7.016 1.00 27.95 ? 457 GLU A C 1 ATOM 3536 O O . GLU A 1 457 ? -47.245 22.865 -7.983 1.00 28.14 ? 457 GLU A O 1 ATOM 3537 C CB . GLU A 1 457 ? -45.666 25.217 -7.506 1.00 30.49 ? 457 GLU A CB 1 ATOM 3538 C CG . GLU A 1 457 ? -45.290 26.579 -6.963 1.00 32.84 ? 457 GLU A CG 1 ATOM 3539 C CD . GLU A 1 457 ? -46.430 27.244 -6.225 1.00 33.95 ? 457 GLU A CD 1 ATOM 3540 O OE1 . GLU A 1 457 ? -47.569 27.142 -6.714 1.00 37.78 ? 457 GLU A OE1 1 ATOM 3541 O OE2 . GLU A 1 457 ? -46.204 27.880 -5.184 1.00 35.84 ? 457 GLU A OE2 1 ATOM 3542 N N . ASN A 1 458 ? -45.969 21.790 -6.463 1.00 25.80 ? 458 ASN A N 1 ATOM 3543 C CA . ASN A 1 458 ? -46.255 20.468 -7.044 1.00 24.77 ? 458 ASN A CA 1 ATOM 3544 C C . ASN A 1 458 ? -47.465 19.779 -6.435 1.00 24.17 ? 458 ASN A C 1 ATOM 3545 O O . ASN A 1 458 ? -47.844 18.690 -6.870 1.00 23.44 ? 458 ASN A O 1 ATOM 3546 C CB . ASN A 1 458 ? -45.034 19.560 -6.917 1.00 24.72 ? 458 ASN A CB 1 ATOM 3547 C CG . ASN A 1 458 ? -43.828 20.118 -7.640 1.00 25.20 ? 458 ASN A CG 1 ATOM 3548 O OD1 . ASN A 1 458 ? -43.941 21.106 -8.372 1.00 25.72 ? 458 ASN A OD1 1 ATOM 3549 N ND2 . ASN A 1 458 ? -42.666 19.490 -7.441 1.00 25.83 ? 458 ASN A ND2 1 ATOM 3550 N N . ALA A 1 459 ? -48.079 20.423 -5.447 1.00 23.66 ? 459 ALA A N 1 ATOM 3551 C CA . ALA A 1 459 ? -49.202 19.839 -4.722 1.00 24.17 ? 459 ALA A CA 1 ATOM 3552 C C . ALA A 1 459 ? -50.189 20.891 -4.269 1.00 25.15 ? 459 ALA A C 1 ATOM 3553 O O . ALA A 1 459 ? -49.836 22.067 -4.140 1.00 26.28 ? 459 ALA A O 1 ATOM 3554 C CB . ALA A 1 459 ? -48.687 19.065 -3.509 1.00 22.82 ? 459 ALA A CB 1 ATOM 3555 N N . GLU A 1 460 ? -51.422 20.469 -4.010 1.00 25.26 ? 460 GLU A N 1 ATOM 3556 C CA . GLU A 1 460 ? -52.413 21.329 -3.356 1.00 26.47 ? 460 GLU A CA 1 ATOM 3557 C C . GLU A 1 460 ? -52.966 20.680 -2.086 1.00 26.50 ? 460 GLU A C 1 ATOM 3558 O O . GLU A 1 460 ? -53.098 19.452 -1.994 1.00 24.79 ? 460 GLU A O 1 ATOM 3559 C CB . GLU A 1 460 ? -53.551 21.689 -4.315 1.00 27.33 ? 460 GLU A CB 1 ATOM 3560 C CG . GLU A 1 460 ? -53.102 22.581 -5.461 1.00 27.22 ? 460 GLU A CG 1 ATOM 3561 C CD . GLU A 1 460 ? -54.139 22.772 -6.555 1.00 28.51 ? 460 GLU A CD 1 ATOM 3562 O OE1 . GLU A 1 460 ? -55.352 22.556 -6.310 1.00 28.85 ? 460 GLU A OE1 1 ATOM 3563 O OE2 . GLU A 1 460 ? -53.722 23.158 -7.668 1.00 28.07 ? 460 GLU A OE2 1 ATOM 3564 N N . ASP A 1 461 ? -53.293 21.533 -1.122 1.00 26.93 ? 461 ASP A N 1 ATOM 3565 C CA . ASP A 1 461 ? -53.918 21.135 0.126 1.00 27.97 ? 461 ASP A CA 1 ATOM 3566 C C . ASP A 1 461 ? -55.395 20.782 -0.109 1.00 29.16 ? 461 ASP A C 1 ATOM 3567 O O . ASP A 1 461 ? -56.177 21.644 -0.496 1.00 29.39 ? 461 ASP A O 1 ATOM 3568 C CB . ASP A 1 461 ? -53.812 22.314 1.103 1.00 29.00 ? 461 ASP A CB 1 ATOM 3569 C CG . ASP A 1 461 ? -54.240 21.967 2.515 1.00 29.52 ? 461 ASP A CG 1 ATOM 3570 O OD1 . ASP A 1 461 ? -54.955 20.961 2.738 1.00 28.94 ? 461 ASP A OD1 1 ATOM 3571 O OD2 . ASP A 1 461 ? -53.850 22.745 3.416 1.00 31.73 ? 461 ASP A OD2 1 ATOM 3572 N N . MET A 1 462 ? -55.766 19.523 0.122 1.00 28.25 ? 462 MET A N 1 ATOM 3573 C CA . MET A 1 462 ? -57.153 19.049 -0.078 1.00 30.29 ? 462 MET A CA 1 ATOM 3574 C C . MET A 1 462 ? -58.096 19.359 1.098 1.00 31.76 ? 462 MET A C 1 ATOM 3575 O O . MET A 1 462 ? -59.303 19.045 1.041 1.00 33.01 ? 462 MET A O 1 ATOM 3576 C CB . MET A 1 462 ? -57.166 17.530 -0.321 1.00 30.92 ? 462 MET A CB 1 ATOM 3577 C CG . MET A 1 462 ? -56.349 17.056 -1.517 1.00 31.59 ? 462 MET A CG 1 ATOM 3578 S SD . MET A 1 462 ? -56.057 15.269 -1.537 1.00 33.50 ? 462 MET A SD 1 ATOM 3579 C CE . MET A 1 462 ? -57.743 14.681 -1.457 1.00 36.14 ? 462 MET A CE 1 ATOM 3580 N N . GLY A 1 463 ? -57.559 19.929 2.176 1.00 30.13 ? 463 GLY A N 1 ATOM 3581 C CA . GLY A 1 463 ? -58.375 20.396 3.296 1.00 31.28 ? 463 GLY A CA 1 ATOM 3582 C C . GLY A 1 463 ? -58.688 19.366 4.369 1.00 31.21 ? 463 GLY A C 1 ATOM 3583 O O . GLY A 1 463 ? -59.348 19.690 5.349 1.00 31.91 ? 463 GLY A O 1 ATOM 3584 N N . ASN A 1 464 ? -58.206 18.135 4.197 1.00 29.60 ? 464 ASN A N 1 ATOM 3585 C CA . ASN A 1 464 ? -58.462 17.054 5.137 1.00 30.39 ? 464 ASN A CA 1 ATOM 3586 C C . ASN A 1 464 ? -57.166 16.531 5.769 1.00 28.67 ? 464 ASN A C 1 ATOM 3587 O O . ASN A 1 464 ? -57.133 15.409 6.262 1.00 30.93 ? 464 ASN A O 1 ATOM 3588 C CB . ASN A 1 464 ? -59.181 15.906 4.420 1.00 31.74 ? 464 ASN A CB 1 ATOM 3589 C CG . ASN A 1 464 ? -58.360 15.344 3.270 1.00 31.52 ? 464 ASN A CG 1 ATOM 3590 O OD1 . ASN A 1 464 ? -57.406 15.974 2.820 1.00 31.11 ? 464 ASN A OD1 1 ATOM 3591 N ND2 . ASN A 1 464 ? -58.724 14.162 2.791 1.00 33.40 ? 464 ASN A ND2 1 ATOM 3592 N N . GLY A 1 465 ? -56.116 17.346 5.767 1.00 27.09 ? 465 GLY A N 1 ATOM 3593 C CA . GLY A 1 465 ? -54.784 16.906 6.187 1.00 26.72 ? 465 GLY A CA 1 ATOM 3594 C C . GLY A 1 465 ? -53.992 16.144 5.133 1.00 25.04 ? 465 GLY A C 1 ATOM 3595 O O . GLY A 1 465 ? -52.955 15.547 5.453 1.00 25.37 ? 465 GLY A O 1 ATOM 3596 N N . CYS A 1 466 ? -54.448 16.192 3.882 1.00 24.97 ? 466 CYS A N 1 ATOM 3597 C CA . CYS A 1 466 ? -53.769 15.536 2.769 1.00 25.03 ? 466 CYS A CA 1 ATOM 3598 C C . CYS A 1 466 ? -53.428 16.509 1.656 1.00 24.14 ? 466 CYS A C 1 ATOM 3599 O O . CYS A 1 466 ? -54.113 17.520 1.448 1.00 23.94 ? 466 CYS A O 1 ATOM 3600 C CB . CYS A 1 466 ? -54.628 14.424 2.142 1.00 27.52 ? 466 CYS A CB 1 ATOM 3601 S SG . CYS A 1 466 ? -55.380 13.250 3.285 1.00 29.86 ? 466 CYS A SG 1 ATOM 3602 N N . PHE A 1 467 ? -52.376 16.161 0.928 1.00 22.98 ? 467 PHE A N 1 ATOM 3603 C CA . PHE A 1 467 ? -51.981 16.852 -0.297 1.00 23.18 ? 467 PHE A CA 1 ATOM 3604 C C . PHE A 1 467 ? -52.322 16.012 -1.529 1.00 23.75 ? 467 PHE A C 1 ATOM 3605 O O . PHE A 1 467 ? -52.115 14.802 -1.526 1.00 22.46 ? 467 PHE A O 1 ATOM 3606 C CB . PHE A 1 467 ? -50.483 17.091 -0.287 1.00 22.68 ? 467 PHE A CB 1 ATOM 3607 C CG . PHE A 1 467 ? -50.024 17.964 0.835 1.00 23.03 ? 467 PHE A CG 1 ATOM 3608 C CD1 . PHE A 1 467 ? -50.147 19.337 0.740 1.00 23.88 ? 467 PHE A CD1 1 ATOM 3609 C CD2 . PHE A 1 467 ? -49.493 17.417 1.984 1.00 22.84 ? 467 PHE A CD2 1 ATOM 3610 C CE1 . PHE A 1 467 ? -49.737 20.157 1.786 1.00 24.50 ? 467 PHE A CE1 1 ATOM 3611 C CE2 . PHE A 1 467 ? -49.080 18.221 3.022 1.00 23.49 ? 467 PHE A CE2 1 ATOM 3612 C CZ . PHE A 1 467 ? -49.210 19.589 2.933 1.00 24.06 ? 467 PHE A CZ 1 ATOM 3613 N N . LYS A 1 468 ? -52.841 16.669 -2.562 1.00 24.02 ? 468 LYS A N 1 ATOM 3614 C CA . LYS A 1 468 ? -52.906 16.100 -3.900 1.00 25.41 ? 468 LYS A CA 1 ATOM 3615 C C . LYS A 1 468 ? -51.625 16.506 -4.611 1.00 24.82 ? 468 LYS A C 1 ATOM 3616 O O . LYS A 1 468 ? -51.378 17.695 -4.841 1.00 24.33 ? 468 LYS A O 1 ATOM 3617 C CB . LYS A 1 468 ? -54.126 16.602 -4.658 1.00 28.22 ? 468 LYS A CB 1 ATOM 3618 C CG . LYS A 1 468 ? -54.210 16.055 -6.079 1.00 30.42 ? 468 LYS A CG 1 ATOM 3619 C CD . LYS A 1 468 ? -55.539 16.421 -6.720 1.00 33.71 ? 468 LYS A CD 1 ATOM 3620 C CE . LYS A 1 468 ? -55.646 15.869 -8.144 1.00 35.95 ? 468 LYS A CE 1 ATOM 3621 N NZ . LYS A 1 468 ? -56.922 16.298 -8.789 1.00 38.53 ? 468 LYS A NZ 1 ATOM 3622 N N . ILE A 1 469 ? -50.788 15.516 -4.894 1.00 23.96 ? 469 ILE A N 1 ATOM 3623 C CA . ILE A 1 469 ? -49.510 15.727 -5.564 1.00 23.98 ? 469 ILE A CA 1 ATOM 3624 C C . ILE A 1 469 ? -49.766 15.519 -7.058 1.00 25.28 ? 469 ILE A C 1 ATOM 3625 O O . ILE A 1 469 ? -50.227 14.459 -7.477 1.00 25.94 ? 469 ILE A O 1 ATOM 3626 C CB . ILE A 1 469 ? -48.443 14.738 -5.054 1.00 24.15 ? 469 ILE A CB 1 ATOM 3627 C CG1 . ILE A 1 469 ? -48.172 14.949 -3.554 1.00 23.35 ? 469 ILE A CG1 1 ATOM 3628 C CG2 . ILE A 1 469 ? -47.144 14.874 -5.837 1.00 23.87 ? 469 ILE A CG2 1 ATOM 3629 C CD1 . ILE A 1 469 ? -47.327 13.856 -2.946 1.00 23.98 ? 469 ILE A CD1 1 ATOM 3630 N N . TYR A 1 470 ? -49.462 16.528 -7.863 1.00 26.03 ? 470 TYR A N 1 ATOM 3631 C CA . TYR A 1 470 ? -49.895 16.547 -9.263 1.00 27.11 ? 470 TYR A CA 1 ATOM 3632 C C . TYR A 1 470 ? -48.874 15.932 -10.227 1.00 28.00 ? 470 TYR A C 1 ATOM 3633 O O . TYR A 1 470 ? -48.728 16.388 -11.364 1.00 28.98 ? 470 TYR A O 1 ATOM 3634 C CB . TYR A 1 470 ? -50.232 17.983 -9.677 1.00 27.62 ? 470 TYR A CB 1 ATOM 3635 C CG . TYR A 1 470 ? -51.584 18.442 -9.216 1.00 28.02 ? 470 TYR A CG 1 ATOM 3636 C CD1 . TYR A 1 470 ? -51.773 18.935 -7.928 1.00 27.81 ? 470 TYR A CD1 1 ATOM 3637 C CD2 . TYR A 1 470 ? -52.681 18.386 -10.067 1.00 28.57 ? 470 TYR A CD2 1 ATOM 3638 C CE1 . TYR A 1 470 ? -53.022 19.362 -7.505 1.00 28.08 ? 470 TYR A CE1 1 ATOM 3639 C CE2 . TYR A 1 470 ? -53.936 18.812 -9.654 1.00 29.36 ? 470 TYR A CE2 1 ATOM 3640 C CZ . TYR A 1 470 ? -54.098 19.302 -8.370 1.00 29.25 ? 470 TYR A CZ 1 ATOM 3641 O OH . TYR A 1 470 ? -55.337 19.725 -7.957 1.00 30.69 ? 470 TYR A OH 1 ATOM 3642 N N . HIS A 1 471 ? -48.158 14.906 -9.773 1.00 27.25 ? 471 HIS A N 1 ATOM 3643 C CA . HIS A 1 471 ? -47.246 14.178 -10.633 1.00 27.71 ? 471 HIS A CA 1 ATOM 3644 C C . HIS A 1 471 ? -47.175 12.761 -10.186 1.00 28.44 ? 471 HIS A C 1 ATOM 3645 O O . HIS A 1 471 ? -47.563 12.444 -9.075 1.00 27.04 ? 471 HIS A O 1 ATOM 3646 C CB . HIS A 1 471 ? -45.857 14.824 -10.647 1.00 27.37 ? 471 HIS A CB 1 ATOM 3647 C CG . HIS A 1 471 ? -45.181 14.878 -9.304 1.00 25.90 ? 471 HIS A CG 1 ATOM 3648 N ND1 . HIS A 1 471 ? -44.490 13.837 -8.800 1.00 26.88 ? 471 HIS A ND1 1 ATOM 3649 C CD2 . HIS A 1 471 ? -45.050 15.917 -8.390 1.00 25.15 ? 471 HIS A CD2 1 ATOM 3650 C CE1 . HIS A 1 471 ? -43.977 14.180 -7.609 1.00 26.08 ? 471 HIS A CE1 1 ATOM 3651 N NE2 . HIS A 1 471 ? -44.317 15.452 -7.359 1.00 25.67 ? 471 HIS A NE2 1 ATOM 3652 N N . LYS A 1 472 ? -46.691 11.885 -11.059 1.00 29.24 ? 472 LYS A N 1 ATOM 3653 C CA . LYS A 1 472 ? -46.480 10.504 -10.683 1.00 31.56 ? 472 LYS A CA 1 ATOM 3654 C C . LYS A 1 472 ? -45.479 10.492 -9.540 1.00 30.48 ? 472 LYS A C 1 ATOM 3655 O O . LYS A 1 472 ? -44.408 11.086 -9.648 1.00 29.91 ? 472 LYS A O 1 ATOM 3656 C CB . LYS A 1 472 ? -45.943 9.695 -11.867 1.00 33.97 ? 472 LYS A CB 1 ATOM 3657 C CG . LYS A 1 472 ? -45.615 8.260 -11.514 1.00 37.42 ? 472 LYS A CG 1 ATOM 3658 C CD . LYS A 1 472 ? -45.072 7.489 -12.709 1.00 40.62 ? 472 LYS A CD 1 ATOM 3659 C CE . LYS A 1 472 ? -44.890 6.015 -12.363 1.00 43.02 ? 472 LYS A CE 1 ATOM 3660 N NZ . LYS A 1 472 ? -44.191 5.280 -13.451 1.00 46.79 ? 472 LYS A NZ 1 ATOM 3661 N N . CYS A 1 473 ? -45.828 9.840 -8.437 1.00 30.40 ? 473 CYS A N 1 ATOM 3662 C CA . CYS A 1 473 ? -44.954 9.854 -7.254 1.00 31.14 ? 473 CYS A CA 1 ATOM 3663 C C . CYS A 1 473 ? -44.952 8.449 -6.672 1.00 31.22 ? 473 CYS A C 1 ATOM 3664 O O . CYS A 1 473 ? -45.788 8.104 -5.852 1.00 31.56 ? 473 CYS A O 1 ATOM 3665 C CB . CYS A 1 473 ? -45.384 10.947 -6.248 1.00 32.15 ? 473 CYS A CB 1 ATOM 3666 S SG . CYS A 1 473 ? -44.208 11.298 -4.899 1.00 33.40 ? 473 CYS A SG 1 ATOM 3667 N N . ASP A 1 474 ? -44.001 7.643 -7.137 1.00 31.09 ? 474 ASP A N 1 ATOM 3668 C CA . ASP A 1 474 ? -43.888 6.238 -6.778 1.00 31.18 ? 474 ASP A CA 1 ATOM 3669 C C . ASP A 1 474 ? -43.337 6.068 -5.353 1.00 30.86 ? 474 ASP A C 1 ATOM 3670 O O . ASP A 1 474 ? -43.149 7.036 -4.635 1.00 29.98 ? 474 ASP A O 1 ATOM 3671 C CB . ASP A 1 474 ? -43.036 5.488 -7.831 1.00 32.50 ? 474 ASP A CB 1 ATOM 3672 C CG . ASP A 1 474 ? -41.568 5.934 -7.868 1.00 32.80 ? 474 ASP A CG 1 ATOM 3673 O OD1 . ASP A 1 474 ? -41.079 6.646 -6.959 1.00 31.11 ? 474 ASP A OD1 1 ATOM 3674 O OD2 . ASP A 1 474 ? -40.868 5.537 -8.833 1.00 33.24 ? 474 ASP A OD2 1 ATOM 3675 N N . ASN A 1 475 ? -43.089 4.843 -4.926 1.00 30.66 ? 475 ASN A N 1 ATOM 3676 C CA . ASN A 1 475 ? -42.736 4.633 -3.530 1.00 30.94 ? 475 ASN A CA 1 ATOM 3677 C C . ASN A 1 475 ? -41.479 5.379 -3.106 1.00 30.33 ? 475 ASN A C 1 ATOM 3678 O O . ASN A 1 475 ? -41.418 5.913 -1.994 1.00 29.59 ? 475 ASN A O 1 ATOM 3679 C CB . ASN A 1 475 ? -42.603 3.148 -3.218 1.00 32.73 ? 475 ASN A CB 1 ATOM 3680 C CG . ASN A 1 475 ? -43.945 2.457 -3.100 1.00 33.20 ? 475 ASN A CG 1 ATOM 3681 O OD1 . ASN A 1 475 ? -44.997 3.102 -3.078 1.00 32.48 ? 475 ASN A OD1 1 ATOM 3682 N ND2 . ASN A 1 475 ? -43.913 1.127 -3.020 1.00 34.08 ? 475 ASN A ND2 1 ATOM 3683 N N . ALA A 1 476 ? -40.483 5.404 -3.985 1.00 30.33 ? 476 ALA A N 1 ATOM 3684 C CA . ALA A 1 476 ? -39.236 6.087 -3.687 1.00 30.90 ? 476 ALA A CA 1 ATOM 3685 C C . ALA A 1 476 ? -39.463 7.601 -3.634 1.00 29.66 ? 476 ALA A C 1 ATOM 3686 O O . ALA A 1 476 ? -38.891 8.284 -2.791 1.00 31.04 ? 476 ALA A O 1 ATOM 3687 C CB . ALA A 1 476 ? -38.152 5.705 -4.691 1.00 31.52 ? 476 ALA A CB 1 ATOM 3688 N N . CYS A 1 477 ? -40.334 8.114 -4.492 1.00 29.89 ? 477 CYS A N 1 ATOM 3689 C CA . CYS A 1 477 ? -40.675 9.527 -4.478 1.00 29.51 ? 477 CYS A CA 1 ATOM 3690 C C . CYS A 1 477 ? -41.327 9.895 -3.147 1.00 28.17 ? 477 CYS A C 1 ATOM 3691 O O . CYS A 1 477 ? -40.924 10.864 -2.507 1.00 27.70 ? 477 CYS A O 1 ATOM 3692 C CB . CYS A 1 477 ? -41.605 9.844 -5.654 1.00 31.58 ? 477 CYS A CB 1 ATOM 3693 S SG . CYS A 1 477 ? -42.279 11.519 -5.744 1.00 33.32 ? 477 CYS A SG 1 ATOM 3694 N N . ILE A 1 478 ? -42.309 9.105 -2.723 1.00 27.10 ? 478 ILE A N 1 ATOM 3695 C CA . ILE A 1 478 ? -42.950 9.325 -1.437 1.00 26.84 ? 478 ILE A CA 1 ATOM 3696 C C . ILE A 1 478 ? -41.915 9.287 -0.311 1.00 27.03 ? 478 ILE A C 1 ATOM 3697 O O . ILE A 1 478 ? -41.918 10.146 0.573 1.00 27.21 ? 478 ILE A O 1 ATOM 3698 C CB . ILE A 1 478 ? -44.087 8.320 -1.161 1.00 26.75 ? 478 ILE A CB 1 ATOM 3699 C CG1 . ILE A 1 478 ? -45.219 8.477 -2.188 1.00 26.58 ? 478 ILE A CG1 1 ATOM 3700 C CG2 . ILE A 1 478 ? -44.621 8.487 0.269 1.00 26.44 ? 478 ILE A CG2 1 ATOM 3701 C CD1 . ILE A 1 478 ? -45.944 9.806 -2.144 1.00 25.57 ? 478 ILE A CD1 1 ATOM 3702 N N . GLY A 1 479 ? -41.033 8.292 -0.341 1.00 28.27 ? 479 GLY A N 1 ATOM 3703 C CA . GLY A 1 479 ? -39.959 8.183 0.623 1.00 28.40 ? 479 GLY A CA 1 ATOM 3704 C C . GLY A 1 479 ? -39.079 9.413 0.684 1.00 29.40 ? 479 GLY A C 1 ATOM 3705 O O . GLY A 1 479 ? -38.687 9.833 1.774 1.00 30.05 ? 479 GLY A O 1 ATOM 3706 N N . SER A 1 480 ? -38.788 10.002 -0.473 1.00 29.05 ? 480 SER A N 1 ATOM 3707 C CA . SER A 1 480 ? -37.982 11.227 -0.537 1.00 29.92 ? 480 SER A CA 1 ATOM 3708 C C . SER A 1 480 ? -38.649 12.406 0.200 1.00 29.69 ? 480 SER A C 1 ATOM 3709 O O . SER A 1 480 ? -37.970 13.216 0.836 1.00 31.15 ? 480 SER A O 1 ATOM 3710 C CB . SER A 1 480 ? -37.640 11.594 -1.987 1.00 30.21 ? 480 SER A CB 1 ATOM 3711 O OG . SER A 1 480 ? -38.705 12.241 -2.682 1.00 30.49 ? 480 SER A OG 1 ATOM 3712 N N . ILE A 1 481 ? -39.974 12.475 0.137 1.00 28.73 ? 481 ILE A N 1 ATOM 3713 C CA . ILE A 1 481 ? -40.734 13.494 0.869 1.00 27.97 ? 481 ILE A CA 1 ATOM 3714 C C . ILE A 1 481 ? -40.636 13.206 2.358 1.00 29.32 ? 481 ILE A C 1 ATOM 3715 O O . ILE A 1 481 ? -40.322 14.092 3.153 1.00 30.04 ? 481 ILE A O 1 ATOM 3716 C CB . ILE A 1 481 ? -42.213 13.512 0.451 1.00 27.03 ? 481 ILE A CB 1 ATOM 3717 C CG1 . ILE A 1 481 ? -42.311 13.818 -1.053 1.00 26.25 ? 481 ILE A CG1 1 ATOM 3718 C CG2 . ILE A 1 481 ? -42.991 14.536 1.276 1.00 26.39 ? 481 ILE A CG2 1 ATOM 3719 C CD1 . ILE A 1 481 ? -43.672 13.581 -1.663 1.00 26.04 ? 481 ILE A CD1 1 ATOM 3720 N N . ARG A 1 482 ? -40.893 11.961 2.734 1.00 30.32 ? 482 ARG A N 1 ATOM 3721 C CA . ARG A 1 482 ? -40.826 11.553 4.136 1.00 31.84 ? 482 ARG A CA 1 ATOM 3722 C C . ARG A 1 482 ? -39.438 11.771 4.740 1.00 35.54 ? 482 ARG A C 1 ATOM 3723 O O . ARG A 1 482 ? -39.307 12.104 5.922 1.00 38.06 ? 482 ARG A O 1 ATOM 3724 C CB . ARG A 1 482 ? -41.213 10.081 4.270 1.00 31.69 ? 482 ARG A CB 1 ATOM 3725 C CG . ARG A 1 482 ? -42.668 9.799 3.984 1.00 30.94 ? 482 ARG A CG 1 ATOM 3726 C CD . ARG A 1 482 ? -43.093 8.430 4.473 1.00 31.25 ? 482 ARG A CD 1 ATOM 3727 N NE . ARG A 1 482 ? -42.136 7.405 4.066 1.00 33.10 ? 482 ARG A NE 1 ATOM 3728 C CZ . ARG A 1 482 ? -42.393 6.365 3.277 1.00 34.67 ? 482 ARG A CZ 1 ATOM 3729 N NH1 . ARG A 1 482 ? -43.608 6.124 2.790 1.00 34.19 ? 482 ARG A NH1 1 ATOM 3730 N NH2 . ARG A 1 482 ? -41.399 5.536 2.974 1.00 35.09 ? 482 ARG A NH2 1 ATOM 3731 N N . ASN A 1 483 ? -38.411 11.590 3.921 1.00 39.25 ? 483 ASN A N 1 ATOM 3732 C CA . ASN A 1 483 ? -37.019 11.656 4.356 1.00 44.63 ? 483 ASN A CA 1 ATOM 3733 C C . ASN A 1 483 ? -36.437 13.063 4.212 1.00 43.26 ? 483 ASN A C 1 ATOM 3734 O O . ASN A 1 483 ? -35.280 13.300 4.554 1.00 44.12 ? 483 ASN A O 1 ATOM 3735 C CB . ASN A 1 483 ? -36.201 10.662 3.528 1.00 51.70 ? 483 ASN A CB 1 ATOM 3736 C CG . ASN A 1 483 ? -34.971 10.144 4.251 1.00 60.98 ? 483 ASN A CG 1 ATOM 3737 O OD1 . ASN A 1 483 ? -34.574 10.681 5.288 1.00 63.03 ? 483 ASN A OD1 1 ATOM 3738 N ND2 . ASN A 1 483 ? -34.352 9.083 3.703 1.00 70.21 ? 483 ASN A ND2 1 ATOM 3739 N N . GLY A 1 484 ? -37.232 13.992 3.690 1.00 41.03 ? 484 GLY A N 1 ATOM 3740 C CA . GLY A 1 484 ? -36.807 15.376 3.550 1.00 40.84 ? 484 GLY A CA 1 ATOM 3741 C C . GLY A 1 484 ? -35.814 15.630 2.433 1.00 41.37 ? 484 GLY A C 1 ATOM 3742 O O . GLY A 1 484 ? -35.103 16.639 2.461 1.00 42.56 ? 484 GLY A O 1 ATOM 3743 N N . THR A 1 485 ? -35.767 14.743 1.438 1.00 40.08 ? 485 THR A N 1 ATOM 3744 C CA . THR A 1 485 ? -34.821 14.881 0.322 1.00 39.49 ? 485 THR A CA 1 ATOM 3745 C C . THR A 1 485 ? -35.498 15.102 -1.041 1.00 37.61 ? 485 THR A C 1 ATOM 3746 O O . THR A 1 485 ? -34.840 15.088 -2.070 1.00 37.96 ? 485 THR A O 1 ATOM 3747 C CB . THR A 1 485 ? -33.873 13.666 0.235 1.00 41.38 ? 485 THR A CB 1 ATOM 3748 O OG1 . THR A 1 485 ? -34.608 12.479 -0.096 1.00 40.82 ? 485 THR A OG1 1 ATOM 3749 C CG2 . THR A 1 485 ? -33.143 13.475 1.563 1.00 42.54 ? 485 THR A CG2 1 ATOM 3750 N N . TYR A 1 486 ? -36.808 15.329 -1.032 1.00 35.17 ? 486 TYR A N 1 ATOM 3751 C CA . TYR A 1 486 ? -37.584 15.543 -2.254 1.00 33.44 ? 486 TYR A CA 1 ATOM 3752 C C . TYR A 1 486 ? -37.132 16.823 -2.941 1.00 33.83 ? 486 TYR A C 1 ATOM 3753 O O . TYR A 1 486 ? -37.039 17.866 -2.304 1.00 33.52 ? 486 TYR A O 1 ATOM 3754 C CB . TYR A 1 486 ? -39.062 15.608 -1.881 1.00 31.48 ? 486 TYR A CB 1 ATOM 3755 C CG . TYR A 1 486 ? -40.052 16.004 -2.952 1.00 29.58 ? 486 TYR A CG 1 ATOM 3756 C CD1 . TYR A 1 486 ? -40.651 15.049 -3.771 1.00 29.04 ? 486 TYR A CD1 1 ATOM 3757 C CD2 . TYR A 1 486 ? -40.451 17.333 -3.094 1.00 28.66 ? 486 TYR A CD2 1 ATOM 3758 C CE1 . TYR A 1 486 ? -41.600 15.415 -4.724 1.00 27.81 ? 486 TYR A CE1 1 ATOM 3759 C CE2 . TYR A 1 486 ? -41.386 17.705 -4.033 1.00 27.34 ? 486 TYR A CE2 1 ATOM 3760 C CZ . TYR A 1 486 ? -41.962 16.752 -4.848 1.00 27.06 ? 486 TYR A CZ 1 ATOM 3761 O OH . TYR A 1 486 ? -42.902 17.154 -5.770 1.00 25.12 ? 486 TYR A OH 1 ATOM 3762 N N . ASP A 1 487 ? -36.814 16.716 -4.226 1.00 34.35 ? 487 ASP A N 1 ATOM 3763 C CA . ASP A 1 487 ? -36.382 17.851 -5.033 1.00 35.21 ? 487 ASP A CA 1 ATOM 3764 C C . ASP A 1 487 ? -37.549 18.300 -5.915 1.00 32.97 ? 487 ASP A C 1 ATOM 3765 O O . ASP A 1 487 ? -37.826 17.693 -6.953 1.00 31.74 ? 487 ASP A O 1 ATOM 3766 C CB . ASP A 1 487 ? -35.178 17.452 -5.889 1.00 38.23 ? 487 ASP A CB 1 ATOM 3767 C CG . ASP A 1 487 ? -34.560 18.628 -6.632 1.00 40.55 ? 487 ASP A CG 1 ATOM 3768 O OD1 . ASP A 1 487 ? -35.221 19.687 -6.757 1.00 40.08 ? 487 ASP A OD1 1 ATOM 3769 O OD2 . ASP A 1 487 ? -33.402 18.482 -7.090 1.00 43.71 ? 487 ASP A OD2 1 ATOM 3770 N N . HIS A 1 488 ? -38.219 19.379 -5.517 1.00 30.54 ? 488 HIS A N 1 ATOM 3771 C CA . HIS A 1 488 ? -39.435 19.823 -6.225 1.00 29.97 ? 488 HIS A CA 1 ATOM 3772 C C . HIS A 1 488 ? -39.175 20.211 -7.659 1.00 30.68 ? 488 HIS A C 1 ATOM 3773 O O . HIS A 1 488 ? -40.083 20.120 -8.506 1.00 29.10 ? 488 HIS A O 1 ATOM 3774 C CB . HIS A 1 488 ? -40.087 20.995 -5.490 1.00 29.94 ? 488 HIS A CB 1 ATOM 3775 C CG . HIS A 1 488 ? -39.409 22.305 -5.746 1.00 29.89 ? 488 HIS A CG 1 ATOM 3776 N ND1 . HIS A 1 488 ? -39.903 23.210 -6.599 1.00 30.46 ? 488 HIS A ND1 1 ATOM 3777 C CD2 . HIS A 1 488 ? -38.204 22.818 -5.276 1.00 30.65 ? 488 HIS A CD2 1 ATOM 3778 C CE1 . HIS A 1 488 ? -39.071 24.268 -6.661 1.00 30.82 ? 488 HIS A CE1 1 ATOM 3779 N NE2 . HIS A 1 488 ? -38.028 24.026 -5.853 1.00 31.32 ? 488 HIS A NE2 1 ATOM 3780 N N . ASP A 1 489 ? -37.954 20.660 -7.954 1.00 32.06 ? 489 ASP A N 1 ATOM 3781 C CA . ASP A 1 489 ? -37.618 21.101 -9.320 1.00 35.67 ? 489 ASP A CA 1 ATOM 3782 C C . ASP A 1 489 ? -37.700 19.960 -10.328 1.00 34.31 ? 489 ASP A C 1 ATOM 3783 O O . ASP A 1 489 ? -38.059 20.177 -11.476 1.00 35.46 ? 489 ASP A O 1 ATOM 3784 C CB . ASP A 1 489 ? -36.228 21.753 -9.391 1.00 38.90 ? 489 ASP A CB 1 ATOM 3785 C CG . ASP A 1 489 ? -36.227 23.186 -8.902 1.00 42.88 ? 489 ASP A CG 1 ATOM 3786 O OD1 . ASP A 1 489 ? -37.165 23.944 -9.242 1.00 47.11 ? 489 ASP A OD1 1 ATOM 3787 O OD2 . ASP A 1 489 ? -35.279 23.565 -8.179 1.00 46.39 ? 489 ASP A OD2 1 ATOM 3788 N N . VAL A 1 490 ? -37.402 18.746 -9.879 1.00 34.15 ? 490 VAL A N 1 ATOM 3789 C CA . VAL A 1 490 ? -37.454 17.560 -10.744 1.00 35.14 ? 490 VAL A CA 1 ATOM 3790 C C . VAL A 1 490 ? -38.840 17.364 -11.356 1.00 32.96 ? 490 VAL A C 1 ATOM 3791 O O . VAL A 1 490 ? -38.974 16.983 -12.522 1.00 33.28 ? 490 VAL A O 1 ATOM 3792 C CB . VAL A 1 490 ? -37.069 16.297 -9.948 1.00 35.96 ? 490 VAL A CB 1 ATOM 3793 C CG1 . VAL A 1 490 ? -37.287 15.042 -10.774 1.00 38.49 ? 490 VAL A CG1 1 ATOM 3794 C CG2 . VAL A 1 490 ? -35.622 16.390 -9.482 1.00 37.75 ? 490 VAL A CG2 1 ATOM 3795 N N . TYR A 1 491 ? -39.868 17.649 -10.569 1.00 30.63 ? 491 TYR A N 1 ATOM 3796 C CA . TYR A 1 491 ? -41.249 17.340 -10.942 1.00 29.77 ? 491 TYR A CA 1 ATOM 3797 C C . TYR A 1 491 ? -42.076 18.561 -11.339 1.00 28.73 ? 491 TYR A C 1 ATOM 3798 O O . TYR A 1 491 ? -43.209 18.410 -11.761 1.00 28.35 ? 491 TYR A O 1 ATOM 3799 C CB . TYR A 1 491 ? -41.948 16.633 -9.777 1.00 29.18 ? 491 TYR A CB 1 ATOM 3800 C CG . TYR A 1 491 ? -41.234 15.400 -9.280 1.00 30.35 ? 491 TYR A CG 1 ATOM 3801 C CD1 . TYR A 1 491 ? -41.402 14.174 -9.913 1.00 31.58 ? 491 TYR A CD1 1 ATOM 3802 C CD2 . TYR A 1 491 ? -40.391 15.455 -8.171 1.00 30.68 ? 491 TYR A CD2 1 ATOM 3803 C CE1 . TYR A 1 491 ? -40.760 13.033 -9.449 1.00 32.85 ? 491 TYR A CE1 1 ATOM 3804 C CE2 . TYR A 1 491 ? -39.737 14.322 -7.708 1.00 31.84 ? 491 TYR A CE2 1 ATOM 3805 C CZ . TYR A 1 491 ? -39.931 13.113 -8.342 1.00 32.31 ? 491 TYR A CZ 1 ATOM 3806 O OH . TYR A 1 491 ? -39.277 11.989 -7.888 1.00 33.69 ? 491 TYR A OH 1 ATOM 3807 N N . ARG A 1 492 ? -41.519 19.761 -11.208 1.00 29.30 ? 492 ARG A N 1 ATOM 3808 C CA . ARG A 1 492 ? -42.317 20.980 -11.316 1.00 29.68 ? 492 ARG A CA 1 ATOM 3809 C C . ARG A 1 492 ? -43.007 21.137 -12.664 1.00 30.88 ? 492 ARG A C 1 ATOM 3810 O O . ARG A 1 492 ? -44.190 21.488 -12.724 1.00 31.12 ? 492 ARG A O 1 ATOM 3811 C CB . ARG A 1 492 ? -41.448 22.204 -11.016 1.00 30.06 ? 492 ARG A CB 1 ATOM 3812 C CG . ARG A 1 492 ? -42.171 23.532 -11.064 1.00 29.82 ? 492 ARG A CG 1 ATOM 3813 C CD . ARG A 1 492 ? -41.209 24.607 -10.603 1.00 30.31 ? 492 ARG A CD 1 ATOM 3814 N NE . ARG A 1 492 ? -41.743 25.954 -10.716 1.00 30.64 ? 492 ARG A NE 1 ATOM 3815 C CZ . ARG A 1 492 ? -42.176 26.703 -9.706 1.00 30.41 ? 492 ARG A CZ 1 ATOM 3816 N NH1 . ARG A 1 492 ? -42.193 26.239 -8.459 1.00 29.28 ? 492 ARG A NH1 1 ATOM 3817 N NH2 . ARG A 1 492 ? -42.604 27.938 -9.953 1.00 31.24 ? 492 ARG A NH2 1 ATOM 3818 N N . ASP A 1 493 ? -42.278 20.893 -13.749 1.00 32.17 ? 493 ASP A N 1 ATOM 3819 C CA . ASP A 1 493 ? -42.871 20.978 -15.087 1.00 34.78 ? 493 ASP A CA 1 ATOM 3820 C C . ASP A 1 493 ? -44.096 20.064 -15.242 1.00 32.92 ? 493 ASP A C 1 ATOM 3821 O O . ASP A 1 493 ? -45.138 20.499 -15.741 1.00 31.83 ? 493 ASP A O 1 ATOM 3822 C CB . ASP A 1 493 ? -41.839 20.634 -16.172 1.00 38.20 ? 493 ASP A CB 1 ATOM 3823 C CG . ASP A 1 493 ? -40.820 21.754 -16.408 1.00 41.26 ? 493 ASP A CG 1 ATOM 3824 O OD1 . ASP A 1 493 ? -41.060 22.909 -15.995 1.00 43.24 ? 493 ASP A OD1 1 ATOM 3825 O OD2 . ASP A 1 493 ? -39.766 21.474 -17.024 1.00 45.28 ? 493 ASP A OD2 1 ATOM 3826 N N . GLU A 1 494 ? -43.956 18.805 -14.834 1.00 32.07 ? 494 GLU A N 1 ATOM 3827 C CA . GLU A 1 494 ? -45.067 17.844 -14.897 1.00 31.86 ? 494 GLU A CA 1 ATOM 3828 C C . GLU A 1 494 ? -46.224 18.335 -14.036 1.00 31.31 ? 494 GLU A C 1 ATOM 3829 O O . GLU A 1 494 ? -47.369 18.378 -14.484 1.00 30.50 ? 494 GLU A O 1 ATOM 3830 C CB . GLU A 1 494 ? -44.609 16.450 -14.453 1.00 32.26 ? 494 GLU A CB 1 ATOM 3831 C CG . GLU A 1 494 ? -45.710 15.394 -14.379 1.00 33.15 ? 494 GLU A CG 1 ATOM 3832 C CD . GLU A 1 494 ? -45.226 14.031 -13.879 1.00 33.14 ? 494 GLU A CD 1 ATOM 3833 O OE1 . GLU A 1 494 ? -44.019 13.858 -13.594 1.00 33.77 ? 494 GLU A OE1 1 ATOM 3834 O OE2 . GLU A 1 494 ? -46.058 13.112 -13.740 1.00 32.69 ? 494 GLU A OE2 1 ATOM 3835 N N . ALA A 1 495 ? -45.911 18.735 -12.805 1.00 30.87 ? 495 ALA A N 1 ATOM 3836 C CA . ALA A 1 495 ? -46.951 19.139 -11.859 1.00 30.62 ? 495 ALA A CA 1 ATOM 3837 C C . ALA A 1 495 ? -47.696 20.383 -12.326 1.00 30.80 ? 495 ALA A C 1 ATOM 3838 O O . ALA A 1 495 ? -48.913 20.427 -12.250 1.00 31.09 ? 495 ALA A O 1 ATOM 3839 C CB . ALA A 1 495 ? -46.369 19.338 -10.460 1.00 30.63 ? 495 ALA A CB 1 ATOM 3840 N N . LEU A 1 496 ? -46.980 21.385 -12.828 1.00 32.13 ? 496 LEU A N 1 ATOM 3841 C CA . LEU A 1 496 ? -47.638 22.630 -13.260 1.00 34.01 ? 496 LEU A CA 1 ATOM 3842 C C . LEU A 1 496 ? -48.597 22.401 -14.423 1.00 35.74 ? 496 LEU A C 1 ATOM 3843 O O . LEU A 1 496 ? -49.674 22.997 -14.473 1.00 36.68 ? 496 LEU A O 1 ATOM 3844 C CB . LEU A 1 496 ? -46.613 23.709 -13.618 1.00 34.73 ? 496 LEU A CB 1 ATOM 3845 C CG . LEU A 1 496 ? -45.887 24.309 -12.406 1.00 35.27 ? 496 LEU A CG 1 ATOM 3846 C CD1 . LEU A 1 496 ? -44.795 25.264 -12.878 1.00 36.56 ? 496 LEU A CD1 1 ATOM 3847 C CD2 . LEU A 1 496 ? -46.854 25.016 -11.465 1.00 36.92 ? 496 LEU A CD2 1 ATOM 3848 N N . ASN A 1 497 ? -48.199 21.541 -15.353 1.00 35.76 ? 497 ASN A N 1 ATOM 3849 C CA A ASN A 1 497 ? -49.050 21.153 -16.473 0.50 36.55 ? 497 ASN A CA 1 ATOM 3850 C CA B ASN A 1 497 ? -49.068 21.193 -16.462 0.50 36.96 ? 497 ASN A CA 1 ATOM 3851 C C . ASN A 1 497 ? -50.334 20.483 -15.996 1.00 36.57 ? 497 ASN A C 1 ATOM 3852 O O . ASN A 1 497 ? -51.424 20.776 -16.494 1.00 36.66 ? 497 ASN A O 1 ATOM 3853 C CB A ASN A 1 497 ? -48.298 20.200 -17.404 0.50 37.17 ? 497 ASN A CB 1 ATOM 3854 C CB B ASN A 1 497 ? -48.314 20.371 -17.504 0.50 38.25 ? 497 ASN A CB 1 ATOM 3855 C CG A ASN A 1 497 ? -49.156 19.710 -18.556 0.50 38.61 ? 497 ASN A CG 1 ATOM 3856 C CG B ASN A 1 497 ? -47.421 21.233 -18.371 0.50 39.25 ? 497 ASN A CG 1 ATOM 3857 O OD1 A ASN A 1 497 ? -49.444 18.517 -18.666 0.50 40.21 ? 497 ASN A OD1 1 ATOM 3858 O OD1 B ASN A 1 497 ? -47.789 21.587 -19.486 0.50 41.91 ? 497 ASN A OD1 1 ATOM 3859 N ND2 A ASN A 1 497 ? -49.587 20.634 -19.409 0.50 38.94 ? 497 ASN A ND2 1 ATOM 3860 N ND2 B ASN A 1 497 ? -46.258 21.608 -17.848 0.50 39.63 ? 497 ASN A ND2 1 ATOM 3861 N N . ASN A 1 498 ? -50.199 19.571 -15.035 1.00 35.40 ? 498 ASN A N 1 ATOM 3862 C CA . ASN A 1 498 ? -51.368 18.889 -14.478 1.00 35.81 ? 498 ASN A CA 1 ATOM 3863 C C . ASN A 1 498 ? -52.270 19.819 -13.662 1.00 36.22 ? 498 ASN A C 1 ATOM 3864 O O . ASN A 1 498 ? -53.488 19.723 -13.745 1.00 37.65 ? 498 ASN A O 1 ATOM 3865 C CB . ASN A 1 498 ? -50.949 17.681 -13.631 1.00 35.62 ? 498 ASN A CB 1 ATOM 3866 C CG . ASN A 1 498 ? -50.461 16.532 -14.472 1.00 37.51 ? 498 ASN A CG 1 ATOM 3867 O OD1 . ASN A 1 498 ? -50.785 16.444 -15.660 1.00 39.65 ? 498 ASN A OD1 1 ATOM 3868 N ND2 . ASN A 1 498 ? -49.674 15.645 -13.874 1.00 37.20 ? 498 ASN A ND2 1 ATOM 3869 N N . ARG A 1 499 ? -51.676 20.718 -12.888 1.00 35.95 ? 499 ARG A N 1 ATOM 3870 C CA . ARG A 1 499 ? -52.455 21.652 -12.066 1.00 37.63 ? 499 ARG A CA 1 ATOM 3871 C C . ARG A 1 499 ? -53.224 22.674 -12.877 1.00 42.35 ? 499 ARG A C 1 ATOM 3872 O O . ARG A 1 499 ? -54.404 22.917 -12.625 1.00 43.17 ? 499 ARG A O 1 ATOM 3873 C CB . ARG A 1 499 ? -51.550 22.413 -11.099 1.00 36.06 ? 499 ARG A CB 1 ATOM 3874 C CG . ARG A 1 499 ? -51.103 21.604 -9.904 1.00 33.71 ? 499 ARG A CG 1 ATOM 3875 C CD . ARG A 1 499 ? -50.224 22.448 -9.003 1.00 32.73 ? 499 ARG A CD 1 ATOM 3876 N NE . ARG A 1 499 ? -50.991 23.458 -8.279 1.00 31.92 ? 499 ARG A NE 1 ATOM 3877 C CZ . ARG A 1 499 ? -50.475 24.564 -7.747 1.00 32.82 ? 499 ARG A CZ 1 ATOM 3878 N NH1 . ARG A 1 499 ? -49.178 24.843 -7.858 1.00 32.89 ? 499 ARG A NH1 1 ATOM 3879 N NH2 . ARG A 1 499 ? -51.267 25.411 -7.112 1.00 34.02 ? 499 ARG A NH2 1 ATOM 3880 N N . PHE A 1 500 ? -52.542 23.291 -13.833 1.00 45.78 ? 500 PHE A N 1 ATOM 3881 C CA . PHE A 1 500 ? -53.120 24.391 -14.591 1.00 51.96 ? 500 PHE A CA 1 ATOM 3882 C C . PHE A 1 500 ? -53.422 23.924 -16.001 1.00 58.06 ? 500 PHE A C 1 ATOM 3883 O O . PHE A 1 500 ? -52.720 24.267 -16.943 1.00 63.67 ? 500 PHE A O 1 ATOM 3884 C CB . PHE A 1 500 ? -52.190 25.609 -14.543 1.00 51.20 ? 500 PHE A CB 1 ATOM 3885 C CG . PHE A 1 500 ? -51.825 26.024 -13.139 1.00 51.05 ? 500 PHE A CG 1 ATOM 3886 C CD1 . PHE A 1 500 ? -52.811 26.200 -12.173 1.00 50.87 ? 500 PHE A CD1 1 ATOM 3887 C CD2 . PHE A 1 500 ? -50.502 26.221 -12.775 1.00 51.36 ? 500 PHE A CD2 1 ATOM 3888 C CE1 . PHE A 1 500 ? -52.488 26.568 -10.876 1.00 51.51 ? 500 PHE A CE1 1 ATOM 3889 C CE2 . PHE A 1 500 ? -50.170 26.589 -11.478 1.00 51.21 ? 500 PHE A CE2 1 ATOM 3890 C CZ . PHE A 1 500 ? -51.163 26.769 -10.527 1.00 52.10 ? 500 PHE A CZ 1 ATOM 3891 N N . GLN A 1 501 ? -54.473 23.110 -16.107 1.00 64.31 ? 501 GLN A N 1 ATOM 3892 C CA . GLN A 1 501 ? -54.978 22.583 -17.375 1.00 70.05 ? 501 GLN A CA 1 ATOM 3893 C C . GLN A 1 501 ? -56.477 22.856 -17.478 1.00 76.31 ? 501 GLN A C 1 ATOM 3894 O O . GLN A 1 501 ? -57.230 22.558 -16.542 1.00 77.21 ? 501 GLN A O 1 ATOM 3895 C CB . GLN A 1 501 ? -54.748 21.065 -17.464 1.00 70.41 ? 501 GLN A CB 1 ATOM 3896 C CG . GLN A 1 501 ? -55.240 20.283 -16.247 1.00 70.74 ? 501 GLN A CG 1 ATOM 3897 C CD . GLN A 1 501 ? -55.342 18.783 -16.473 1.00 71.34 ? 501 GLN A CD 1 ATOM 3898 O OE1 . GLN A 1 501 ? -56.012 18.327 -17.399 1.00 75.29 ? 501 GLN A OE1 1 ATOM 3899 N NE2 . GLN A 1 501 ? -54.704 18.008 -15.602 1.00 69.32 ? 501 GLN A NE2 1 ATOM 3900 N N . ILE A 1 502 ? -56.915 23.420 -18.604 1.00 79.96 ? 502 ILE A N 1 ATOM 3901 C CA . ILE A 1 502 ? -58.351 23.554 -18.864 1.00 82.75 ? 502 ILE A CA 1 ATOM 3902 C C . ILE A 1 502 ? -58.913 22.154 -19.164 1.00 84.43 ? 502 ILE A C 1 ATOM 3903 O O . ILE A 1 502 ? -58.339 21.403 -19.958 1.00 86.33 ? 502 ILE A O 1 ATOM 3904 C CB . ILE A 1 502 ? -58.675 24.592 -19.978 1.00 83.84 ? 502 ILE A CB 1 ATOM 3905 C CG1 . ILE A 1 502 ? -58.174 24.140 -21.360 1.00 85.35 ? 502 ILE A CG1 1 ATOM 3906 C CG2 . ILE A 1 502 ? -58.096 25.952 -19.612 1.00 81.11 ? 502 ILE A CG2 1 ATOM 3907 C CD1 . ILE A 1 502 ? -58.412 25.155 -22.462 1.00 86.28 ? 502 ILE A CD1 1 ATOM 3908 N N . LYS A 1 503 ? -60.017 21.807 -18.501 1.00 85.08 ? 503 LYS A N 1 ATOM 3909 C CA . LYS A 1 503 ? -60.564 20.445 -18.523 1.00 85.33 ? 503 LYS A CA 1 ATOM 3910 C C . LYS A 1 503 ? -61.838 20.327 -19.359 1.00 87.13 ? 503 LYS A C 1 ATOM 3911 O O . LYS A 1 503 ? -62.149 21.194 -20.172 1.00 89.10 ? 503 LYS A O 1 ATOM 3912 C CB . LYS A 1 503 ? -60.857 19.988 -17.094 1.00 84.17 ? 503 LYS A CB 1 ATOM 3913 C CG . LYS A 1 503 ? -59.616 19.755 -16.247 1.00 81.45 ? 503 LYS A CG 1 ATOM 3914 C CD . LYS A 1 503 ? -59.998 19.509 -14.796 1.00 80.91 ? 503 LYS A CD 1 ATOM 3915 C CE . LYS A 1 503 ? -59.091 18.489 -14.127 1.00 78.88 ? 503 LYS A CE 1 ATOM 3916 N NZ . LYS A 1 503 ? -59.750 17.891 -12.935 1.00 78.35 ? 503 LYS A NZ 1 HETATM 3917 C C1 . NAG B 2 . ? -48.981 5.479 29.648 1.00 40.70 ? 1038 NAG A C1 1 HETATM 3918 C C2 . NAG B 2 . ? -48.256 4.207 29.212 1.00 46.80 ? 1038 NAG A C2 1 HETATM 3919 C C3 . NAG B 2 . ? -47.305 3.665 30.277 1.00 46.88 ? 1038 NAG A C3 1 HETATM 3920 C C4 . NAG B 2 . ? -46.414 4.778 30.821 1.00 47.18 ? 1038 NAG A C4 1 HETATM 3921 C C5 . NAG B 2 . ? -47.269 5.958 31.303 1.00 47.52 ? 1038 NAG A C5 1 HETATM 3922 C C6 . NAG B 2 . ? -46.393 7.103 31.809 1.00 46.34 ? 1038 NAG A C6 1 HETATM 3923 C C7 . NAG B 2 . ? -49.522 2.853 27.632 1.00 53.88 ? 1038 NAG A C7 1 HETATM 3924 C C8 . NAG B 2 . ? -50.590 1.814 27.442 1.00 52.92 ? 1038 NAG A C8 1 HETATM 3925 N N2 . NAG B 2 . ? -49.256 3.205 28.888 1.00 49.13 ? 1038 NAG A N2 1 HETATM 3926 O O3 . NAG B 2 . ? -46.494 2.678 29.684 1.00 46.21 ? 1038 NAG A O3 1 HETATM 3927 O O4 . NAG B 2 . ? -45.609 4.285 31.885 1.00 48.81 ? 1038 NAG A O4 1 HETATM 3928 O O5 . NAG B 2 . ? -48.113 6.439 30.267 1.00 42.93 ? 1038 NAG A O5 1 HETATM 3929 O O6 . NAG B 2 . ? -45.532 7.537 30.780 1.00 47.58 ? 1038 NAG A O6 1 HETATM 3930 O O7 . NAG B 2 . ? -48.938 3.340 26.659 1.00 55.30 ? 1038 NAG A O7 1 HETATM 3931 C C1 . NAG C 2 . ? -49.559 -5.403 76.380 1.00 38.07 ? 1063 NAG A C1 1 HETATM 3932 C C2 . NAG C 2 . ? -48.778 -6.701 76.263 1.00 44.26 ? 1063 NAG A C2 1 HETATM 3933 C C3 . NAG C 2 . ? -49.699 -7.889 76.016 1.00 46.50 ? 1063 NAG A C3 1 HETATM 3934 C C4 . NAG C 2 . ? -50.802 -7.892 77.069 1.00 47.32 ? 1063 NAG A C4 1 HETATM 3935 C C5 . NAG C 2 . ? -51.529 -6.545 76.977 1.00 45.86 ? 1063 NAG A C5 1 HETATM 3936 C C6 . NAG C 2 . ? -52.743 -6.426 77.889 1.00 44.88 ? 1063 NAG A C6 1 HETATM 3937 C C7 . NAG C 2 . ? -46.483 -6.429 75.455 1.00 46.95 ? 1063 NAG A C7 1 HETATM 3938 C C8 . NAG C 2 . ? -45.591 -6.321 74.251 1.00 50.18 ? 1063 NAG A C8 1 HETATM 3939 N N2 . NAG C 2 . ? -47.781 -6.587 75.210 1.00 46.61 ? 1063 NAG A N2 1 HETATM 3940 O O3 . NAG C 2 . ? -48.914 -9.054 76.089 1.00 50.21 ? 1063 NAG A O3 1 HETATM 3941 O O4 . NAG C 2 . ? -51.704 -8.967 76.869 1.00 50.28 ? 1063 NAG A O4 1 HETATM 3942 O O5 . NAG C 2 . ? -50.599 -5.538 77.328 1.00 41.16 ? 1063 NAG A O5 1 HETATM 3943 O O6 . NAG C 2 . ? -52.317 -6.651 79.215 1.00 44.92 ? 1063 NAG A O6 1 HETATM 3944 O O7 . NAG C 2 . ? -46.006 -6.360 76.587 1.00 50.83 ? 1063 NAG A O7 1 HETATM 3945 C C1 . NAG D 2 . ? -25.071 16.691 101.713 1.00 67.38 ? 1126 NAG A C1 1 HETATM 3946 C C2 . NAG D 2 . ? -23.553 16.608 101.904 1.00 74.59 ? 1126 NAG A C2 1 HETATM 3947 C C3 . NAG D 2 . ? -23.124 17.163 103.264 1.00 75.76 ? 1126 NAG A C3 1 HETATM 3948 C C4 . NAG D 2 . ? -23.820 18.489 103.556 1.00 77.11 ? 1126 NAG A C4 1 HETATM 3949 C C5 . NAG D 2 . ? -25.331 18.318 103.413 1.00 78.11 ? 1126 NAG A C5 1 HETATM 3950 C C6 . NAG D 2 . ? -26.107 19.597 103.732 1.00 77.51 ? 1126 NAG A C6 1 HETATM 3951 C C7 . NAG D 2 . ? -22.119 14.814 100.976 1.00 75.45 ? 1126 NAG A C7 1 HETATM 3952 C C8 . NAG D 2 . ? -21.856 13.333 100.944 1.00 73.07 ? 1126 NAG A C8 1 HETATM 3953 N N2 . NAG D 2 . ? -23.137 15.216 101.749 1.00 75.08 ? 1126 NAG A N2 1 HETATM 3954 O O3 . NAG D 2 . ? -21.728 17.358 103.275 1.00 78.59 ? 1126 NAG A O3 1 HETATM 3955 O O4 . NAG D 2 . ? -23.495 18.940 104.853 1.00 78.03 ? 1126 NAG A O4 1 HETATM 3956 O O5 . NAG D 2 . ? -25.606 17.946 102.079 1.00 73.12 ? 1126 NAG A O5 1 HETATM 3957 O O6 . NAG D 2 . ? -26.910 19.427 104.879 1.00 77.94 ? 1126 NAG A O6 1 HETATM 3958 O O7 . NAG D 2 . ? -21.409 15.574 100.315 1.00 74.53 ? 1126 NAG A O7 1 HETATM 3959 C C1 . NAG E 2 . ? -31.717 2.929 95.476 1.00 53.60 ? 1133 NAG A C1 1 HETATM 3960 C C2 . NAG E 2 . ? -30.739 2.170 94.581 1.00 65.06 ? 1133 NAG A C2 1 HETATM 3961 C C3 . NAG E 2 . ? -29.638 1.444 95.348 1.00 64.94 ? 1133 NAG A C3 1 HETATM 3962 C C4 . NAG E 2 . ? -29.003 2.400 96.350 1.00 65.08 ? 1133 NAG A C4 1 HETATM 3963 C C5 . NAG E 2 . ? -30.120 3.006 97.196 1.00 62.61 ? 1133 NAG A C5 1 HETATM 3964 C C6 . NAG E 2 . ? -29.620 3.944 98.287 1.00 63.48 ? 1133 NAG A C6 1 HETATM 3965 C C7 . NAG E 2 . ? -31.581 1.453 92.392 1.00 71.05 ? 1133 NAG A C7 1 HETATM 3966 C C8 . NAG E 2 . ? -31.013 2.703 91.774 1.00 71.08 ? 1133 NAG A C8 1 HETATM 3967 N N2 . NAG E 2 . ? -31.432 1.249 93.703 1.00 67.38 ? 1133 NAG A N2 1 HETATM 3968 O O3 . NAG E 2 . ? -28.688 0.974 94.416 1.00 67.48 ? 1133 NAG A O3 1 HETATM 3969 O O4 . NAG E 2 . ? -28.074 1.709 97.157 1.00 67.76 ? 1133 NAG A O4 1 HETATM 3970 O O5 . NAG E 2 . ? -30.951 3.749 96.330 1.00 62.51 ? 1133 NAG A O5 1 HETATM 3971 O O6 . NAG E 2 . ? -30.536 3.887 99.355 1.00 62.82 ? 1133 NAG A O6 1 HETATM 3972 O O7 . NAG E 2 . ? -32.176 0.640 91.690 1.00 73.02 ? 1133 NAG A O7 1 HETATM 3973 C C1 . NAG F 2 . ? -28.459 26.276 99.088 1.00 35.84 ? 1165 NAG A C1 1 HETATM 3974 C C2 . NAG F 2 . ? -28.000 27.434 99.967 1.00 38.64 ? 1165 NAG A C2 1 HETATM 3975 C C3 . NAG F 2 . ? -27.197 28.458 99.175 1.00 38.86 ? 1165 NAG A C3 1 HETATM 3976 C C4 . NAG F 2 . ? -26.110 27.811 98.337 1.00 37.21 ? 1165 NAG A C4 1 HETATM 3977 C C5 . NAG F 2 . ? -26.749 26.717 97.493 1.00 38.44 ? 1165 NAG A C5 1 HETATM 3978 C C6 . NAG F 2 . ? -25.737 26.007 96.607 1.00 39.02 ? 1165 NAG A C6 1 HETATM 3979 C C7 . NAG F 2 . ? -29.368 28.076 101.913 1.00 45.27 ? 1165 NAG A C7 1 HETATM 3980 C C8 . NAG F 2 . ? -30.579 28.823 102.403 1.00 45.27 ? 1165 NAG A C8 1 HETATM 3981 N N2 . NAG F 2 . ? -29.136 28.102 100.591 1.00 42.22 ? 1165 NAG A N2 1 HETATM 3982 O O3 . NAG F 2 . ? -26.610 29.387 100.054 1.00 40.26 ? 1165 NAG A O3 1 HETATM 3983 O O4 . NAG F 2 . ? -25.575 28.790 97.479 1.00 37.63 ? 1165 NAG A O4 1 HETATM 3984 O O5 . NAG F 2 . ? -27.384 25.763 98.322 1.00 34.24 ? 1165 NAG A O5 1 HETATM 3985 O O6 . NAG F 2 . ? -24.891 25.215 97.401 1.00 43.77 ? 1165 NAG A O6 1 HETATM 3986 O O7 . NAG F 2 . ? -28.649 27.475 102.721 1.00 45.88 ? 1165 NAG A O7 1 HETATM 3987 C C1 . NAG G 2 . ? -24.156 28.956 97.617 1.00 39.58 ? 1166 NAG A C1 1 HETATM 3988 C C2 . NAG G 2 . ? -23.634 29.691 96.381 1.00 39.39 ? 1166 NAG A C2 1 HETATM 3989 C C3 . NAG G 2 . ? -22.163 30.104 96.509 1.00 42.42 ? 1166 NAG A C3 1 HETATM 3990 C C4 . NAG G 2 . ? -21.803 30.646 97.900 1.00 47.58 ? 1166 NAG A C4 1 HETATM 3991 C C5 . NAG G 2 . ? -22.418 29.737 98.969 1.00 45.96 ? 1166 NAG A C5 1 HETATM 3992 C C6 . NAG G 2 . ? -22.127 30.180 100.400 1.00 47.05 ? 1166 NAG A C6 1 HETATM 3993 C C7 . NAG G 2 . ? -24.758 29.017 94.298 1.00 37.90 ? 1166 NAG A C7 1 HETATM 3994 C C8 . NAG G 2 . ? -24.822 27.988 93.204 1.00 36.18 ? 1166 NAG A C8 1 HETATM 3995 N N2 . NAG G 2 . ? -23.828 28.810 95.235 1.00 37.98 ? 1166 NAG A N2 1 HETATM 3996 O O3 . NAG G 2 . ? -21.832 31.062 95.520 1.00 40.10 ? 1166 NAG A O3 1 HETATM 3997 O O4 . NAG G 2 . ? -20.378 30.665 98.006 1.00 56.10 ? 1166 NAG A O4 1 HETATM 3998 O O5 . NAG G 2 . ? -23.826 29.681 98.791 1.00 41.96 ? 1166 NAG A O5 1 HETATM 3999 O O6 . NAG G 2 . ? -22.821 31.378 100.691 1.00 50.01 ? 1166 NAG A O6 1 HETATM 4000 O O7 . NAG G 2 . ? -25.519 29.986 94.296 1.00 34.29 ? 1166 NAG A O7 1 HETATM 4001 C C1 . MAN H 3 . ? -19.748 31.958 98.217 1.00 64.34 ? 1167 MAN A C1 1 HETATM 4002 C C2 . MAN H 3 . ? -18.838 32.348 97.049 1.00 68.83 ? 1167 MAN A C2 1 HETATM 4003 C C3 . MAN H 3 . ? -18.194 33.728 97.261 1.00 71.12 ? 1167 MAN A C3 1 HETATM 4004 C C4 . MAN H 3 . ? -18.471 34.266 98.660 1.00 72.21 ? 1167 MAN A C4 1 HETATM 4005 C C5 . MAN H 3 . ? -18.249 33.176 99.710 1.00 72.93 ? 1167 MAN A C5 1 HETATM 4006 C C6 . MAN H 3 . ? -18.736 33.639 101.081 1.00 75.53 ? 1167 MAN A C6 1 HETATM 4007 O O2 . MAN H 3 . ? -19.545 32.316 95.805 1.00 68.01 ? 1167 MAN A O2 1 HETATM 4008 O O3 . MAN H 3 . ? -18.646 34.692 96.300 1.00 69.37 ? 1167 MAN A O3 1 HETATM 4009 O O4 . MAN H 3 . ? -17.606 35.377 98.915 1.00 72.24 ? 1167 MAN A O4 1 HETATM 4010 O O5 . MAN H 3 . ? -18.911 31.944 99.379 1.00 68.63 ? 1167 MAN A O5 1 HETATM 4011 O O6 . MAN H 3 . ? -17.972 34.771 101.516 1.00 77.05 ? 1167 MAN A O6 1 HETATM 4012 C C1 . NAG I 2 . ? -34.763 25.370 101.005 1.00 39.03 ? 1246 NAG A C1 1 HETATM 4013 C C2 . NAG I 2 . ? -36.021 25.283 101.859 1.00 40.57 ? 1246 NAG A C2 1 HETATM 4014 C C3 . NAG I 2 . ? -35.863 26.103 103.138 1.00 44.46 ? 1246 NAG A C3 1 HETATM 4015 C C4 . NAG I 2 . ? -34.537 25.814 103.831 1.00 47.00 ? 1246 NAG A C4 1 HETATM 4016 C C5 . NAG I 2 . ? -33.396 25.951 102.829 1.00 45.61 ? 1246 NAG A C5 1 HETATM 4017 C C6 . NAG I 2 . ? -32.028 25.657 103.435 1.00 46.74 ? 1246 NAG A C6 1 HETATM 4018 C C7 . NAG I 2 . ? -38.196 25.133 100.719 1.00 41.35 ? 1246 NAG A C7 1 HETATM 4019 C C8 . NAG I 2 . ? -39.252 25.912 99.989 1.00 42.18 ? 1246 NAG A C8 1 HETATM 4020 N N2 . NAG I 2 . ? -37.147 25.838 101.138 1.00 40.39 ? 1246 NAG A N2 1 HETATM 4021 O O3 . NAG I 2 . ? -36.977 25.851 103.971 1.00 41.74 ? 1246 NAG A O3 1 HETATM 4022 O O4 . NAG I 2 . ? -34.373 26.729 104.898 1.00 56.51 ? 1246 NAG A O4 1 HETATM 4023 O O5 . NAG I 2 . ? -33.618 25.037 101.769 1.00 41.93 ? 1246 NAG A O5 1 HETATM 4024 O O6 . NAG I 2 . ? -31.986 24.304 103.835 1.00 48.34 ? 1246 NAG A O6 1 HETATM 4025 O O7 . NAG I 2 . ? -38.332 23.924 100.898 1.00 41.79 ? 1246 NAG A O7 1 HETATM 4026 C C1 . NAG J 2 . ? -34.563 26.107 106.187 1.00 60.34 ? 1247 NAG A C1 1 HETATM 4027 C C2 . NAG J 2 . ? -34.164 27.149 107.228 1.00 62.80 ? 1247 NAG A C2 1 HETATM 4028 C C3 . NAG J 2 . ? -34.545 26.747 108.655 1.00 66.91 ? 1247 NAG A C3 1 HETATM 4029 C C4 . NAG J 2 . ? -35.952 26.155 108.711 1.00 69.19 ? 1247 NAG A C4 1 HETATM 4030 C C5 . NAG J 2 . ? -36.055 25.037 107.673 1.00 68.46 ? 1247 NAG A C5 1 HETATM 4031 C C6 . NAG J 2 . ? -37.364 24.240 107.722 1.00 67.58 ? 1247 NAG A C6 1 HETATM 4032 C C7 . NAG J 2 . ? -32.182 28.475 106.635 1.00 58.81 ? 1247 NAG A C7 1 HETATM 4033 C C8 . NAG J 2 . ? -30.682 28.488 106.549 1.00 56.57 ? 1247 NAG A C8 1 HETATM 4034 N N2 . NAG J 2 . ? -32.730 27.348 107.089 1.00 60.03 ? 1247 NAG A N2 1 HETATM 4035 O O3 . NAG J 2 . ? -34.484 27.877 109.493 1.00 67.77 ? 1247 NAG A O3 1 HETATM 4036 O O4 . NAG J 2 . ? -36.222 25.698 110.019 1.00 72.46 ? 1247 NAG A O4 1 HETATM 4037 O O5 . NAG J 2 . ? -35.886 25.646 106.403 1.00 64.44 ? 1247 NAG A O5 1 HETATM 4038 O O6 . NAG J 2 . ? -38.464 25.006 107.282 1.00 66.87 ? 1247 NAG A O6 1 HETATM 4039 O O7 . NAG J 2 . ? -32.830 29.468 106.305 1.00 57.77 ? 1247 NAG A O7 1 HETATM 4040 C C1 . NAG K 2 . ? -56.303 6.541 56.587 1.00 30.63 ? 1285 NAG A C1 1 HETATM 4041 C C2 . NAG K 2 . ? -57.470 6.218 55.633 1.00 36.37 ? 1285 NAG A C2 1 HETATM 4042 C C3 . NAG K 2 . ? -58.623 7.222 55.784 1.00 40.26 ? 1285 NAG A C3 1 HETATM 4043 C C4 . NAG K 2 . ? -58.917 7.535 57.249 1.00 41.65 ? 1285 NAG A C4 1 HETATM 4044 C C5 . NAG K 2 . ? -57.608 7.878 57.974 1.00 42.18 ? 1285 NAG A C5 1 HETATM 4045 C C6 . NAG K 2 . ? -57.778 8.313 59.432 1.00 43.40 ? 1285 NAG A C6 1 HETATM 4046 C C7 . NAG K 2 . ? -56.772 4.915 53.649 1.00 37.33 ? 1285 NAG A C7 1 HETATM 4047 C C8 . NAG K 2 . ? -56.442 4.873 52.181 1.00 35.34 ? 1285 NAG A C8 1 HETATM 4048 N N2 . NAG K 2 . ? -57.101 6.102 54.212 1.00 35.89 ? 1285 NAG A N2 1 HETATM 4049 O O3 . NAG K 2 . ? -59.783 6.745 55.120 1.00 43.76 ? 1285 NAG A O3 1 HETATM 4050 O O4 . NAG K 2 . ? -59.806 8.635 57.281 1.00 45.53 ? 1285 NAG A O4 1 HETATM 4051 O O5 . NAG K 2 . ? -56.731 6.754 57.905 1.00 36.54 ? 1285 NAG A O5 1 HETATM 4052 O O6 . NAG K 2 . ? -58.265 7.240 60.198 1.00 46.11 ? 1285 NAG A O6 1 HETATM 4053 O O7 . NAG K 2 . ? -56.686 3.860 54.289 1.00 38.75 ? 1285 NAG A O7 1 HETATM 4054 C C1 . NAG L 2 . ? -34.783 8.409 2.486 1.00 71.56 ? 1483 NAG A C1 1 HETATM 4055 C C2 . NAG L 2 . ? -35.956 7.428 2.278 1.00 78.09 ? 1483 NAG A C2 1 HETATM 4056 C C3 . NAG L 2 . ? -35.860 6.695 0.940 1.00 76.90 ? 1483 NAG A C3 1 HETATM 4057 C C4 . NAG L 2 . ? -35.724 7.738 -0.158 1.00 75.35 ? 1483 NAG A C4 1 HETATM 4058 C C5 . NAG L 2 . ? -34.460 8.550 0.117 1.00 76.31 ? 1483 NAG A C5 1 HETATM 4059 C C6 . NAG L 2 . ? -34.174 9.554 -0.995 1.00 77.34 ? 1483 NAG A C6 1 HETATM 4060 C C7 . NAG L 2 . ? -37.220 6.276 4.042 1.00 82.32 ? 1483 NAG A C7 1 HETATM 4061 C C8 . NAG L 2 . ? -37.175 5.232 5.123 1.00 83.20 ? 1483 NAG A C8 1 HETATM 4062 N N2 . NAG L 2 . ? -36.083 6.459 3.361 1.00 79.72 ? 1483 NAG A N2 1 HETATM 4063 O O3 . NAG L 2 . ? -37.000 5.890 0.718 1.00 76.83 ? 1483 NAG A O3 1 HETATM 4064 O O4 . NAG L 2 . ? -35.717 7.122 -1.427 1.00 73.68 ? 1483 NAG A O4 1 HETATM 4065 O O5 . NAG L 2 . ? -34.617 9.244 1.345 1.00 72.42 ? 1483 NAG A O5 1 HETATM 4066 O O6 . NAG L 2 . ? -33.720 8.890 -2.153 1.00 82.52 ? 1483 NAG A O6 1 HETATM 4067 O O7 . NAG L 2 . ? -38.261 6.908 3.831 1.00 79.18 ? 1483 NAG A O7 1 HETATM 4068 N N1 . EPE M 4 . ? -35.069 0.038 88.914 1.00 70.71 ? 1504 EPE A N1 1 HETATM 4069 C C2 . EPE M 4 . ? -35.222 -0.773 90.131 1.00 68.04 ? 1504 EPE A C2 1 HETATM 4070 C C3 . EPE M 4 . ? -36.385 -0.162 90.903 1.00 65.68 ? 1504 EPE A C3 1 HETATM 4071 N N4 . EPE M 4 . ? -36.201 1.284 91.205 1.00 61.10 ? 1504 EPE A N4 1 HETATM 4072 C C5 . EPE M 4 . ? -35.597 2.097 90.125 1.00 59.50 ? 1504 EPE A C5 1 HETATM 4073 C C6 . EPE M 4 . ? -34.545 1.358 89.301 1.00 64.18 ? 1504 EPE A C6 1 HETATM 4074 C C7 . EPE M 4 . ? -37.523 1.847 91.560 1.00 54.33 ? 1504 EPE A C7 1 HETATM 4075 C C8 . EPE M 4 . ? -37.371 3.126 92.372 1.00 51.04 ? 1504 EPE A C8 1 HETATM 4076 O O8 . EPE M 4 . ? -37.509 4.312 91.562 1.00 37.05 ? 1504 EPE A O8 1 HETATM 4077 C C9 . EPE M 4 . ? -34.224 -0.622 87.904 1.00 77.78 ? 1504 EPE A C9 1 HETATM 4078 C C10 . EPE M 4 . ? -35.034 -0.736 86.618 1.00 83.11 ? 1504 EPE A C10 1 HETATM 4079 S S . EPE M 4 . ? -34.221 -1.650 85.489 1.00 94.88 ? 1504 EPE A S 1 HETATM 4080 O O1S . EPE M 4 . ? -35.010 -1.734 84.292 1.00 99.48 ? 1504 EPE A O1S 1 HETATM 4081 O O2S . EPE M 4 . ? -34.002 -2.981 85.993 1.00 95.61 ? 1504 EPE A O2S 1 HETATM 4082 O O3S . EPE M 4 . ? -32.780 -0.955 85.136 1.00 93.69 ? 1504 EPE A O3S 1 HETATM 4083 N N1 . EPE N 4 . ? -53.309 10.092 81.537 1.00 52.87 ? 1505 EPE A N1 1 HETATM 4084 C C2 . EPE N 4 . ? -52.904 11.509 81.630 1.00 56.00 ? 1505 EPE A C2 1 HETATM 4085 C C3 . EPE N 4 . ? -53.202 12.167 80.269 1.00 55.80 ? 1505 EPE A C3 1 HETATM 4086 N N4 . EPE N 4 . ? -52.400 11.498 79.219 1.00 55.62 ? 1505 EPE A N4 1 HETATM 4087 C C5 . EPE N 4 . ? -52.804 10.086 79.128 1.00 56.28 ? 1505 EPE A C5 1 HETATM 4088 C C6 . EPE N 4 . ? -52.523 9.424 80.483 1.00 53.45 ? 1505 EPE A C6 1 HETATM 4089 C C7 . EPE N 4 . ? -52.395 12.185 77.903 1.00 57.91 ? 1505 EPE A C7 1 HETATM 4090 C C8 . EPE N 4 . ? -53.768 12.653 77.434 1.00 59.49 ? 1505 EPE A C8 1 HETATM 4091 O O8 . EPE N 4 . ? -54.039 13.948 77.989 1.00 60.12 ? 1505 EPE A O8 1 HETATM 4092 C C9 . EPE N 4 . ? -53.359 9.356 82.843 1.00 48.43 ? 1505 EPE A C9 1 HETATM 4093 C C10 . EPE N 4 . ? -52.092 8.615 83.318 1.00 44.32 ? 1505 EPE A C10 1 HETATM 4094 S S . EPE N 4 . ? -52.479 7.639 84.651 1.00 42.28 ? 1505 EPE A S 1 HETATM 4095 O O1S . EPE N 4 . ? -51.281 7.227 85.322 1.00 36.02 ? 1505 EPE A O1S 1 HETATM 4096 O O2S . EPE N 4 . ? -53.210 6.487 84.163 1.00 41.89 ? 1505 EPE A O2S 1 HETATM 4097 O O3S . EPE N 4 . ? -53.434 8.492 85.664 1.00 42.33 ? 1505 EPE A O3S 1 HETATM 4098 N N1 . EPE O 4 . ? -25.274 4.595 79.521 1.00 62.02 ? 1506 EPE A N1 1 HETATM 4099 C C2 . EPE O 4 . ? -26.276 5.524 78.951 1.00 60.90 ? 1506 EPE A C2 1 HETATM 4100 C C3 . EPE O 4 . ? -26.662 5.121 77.526 1.00 60.39 ? 1506 EPE A C3 1 HETATM 4101 N N4 . EPE O 4 . ? -25.510 5.148 76.593 1.00 62.08 ? 1506 EPE A N4 1 HETATM 4102 C C5 . EPE O 4 . ? -24.210 5.117 77.315 1.00 61.42 ? 1506 EPE A C5 1 HETATM 4103 C C6 . EPE O 4 . ? -24.245 4.189 78.529 1.00 60.89 ? 1506 EPE A C6 1 HETATM 4104 C C7 . EPE O 4 . ? -25.622 4.077 75.573 1.00 57.81 ? 1506 EPE A C7 1 HETATM 4105 C C8 . EPE O 4 . ? -26.286 4.554 74.288 1.00 56.69 ? 1506 EPE A C8 1 HETATM 4106 O O8 . EPE O 4 . ? -27.706 4.456 74.417 1.00 52.87 ? 1506 EPE A O8 1 HETATM 4107 C C9 . EPE O 4 . ? -24.605 5.150 80.722 1.00 61.71 ? 1506 EPE A C9 1 HETATM 4108 C C10 . EPE O 4 . ? -25.617 5.639 81.753 1.00 59.21 ? 1506 EPE A C10 1 HETATM 4109 S S . EPE O 4 . ? -25.061 5.622 83.338 1.00 58.60 ? 1506 EPE A S 1 HETATM 4110 O O1S . EPE O 4 . ? -23.756 6.207 83.489 1.00 57.31 ? 1506 EPE A O1S 1 HETATM 4111 O O2S . EPE O 4 . ? -25.031 4.253 83.797 1.00 56.20 ? 1506 EPE A O2S 1 HETATM 4112 O O3S . EPE O 4 . ? -26.149 6.458 84.201 1.00 48.16 ? 1506 EPE A O3S 1 HETATM 4113 C C . TAM P 5 . ? -42.767 21.354 40.489 1.00 60.61 ? 1507 TAM A C 1 HETATM 4114 C C1 . TAM P 5 . ? -43.103 22.617 39.685 1.00 59.03 ? 1507 TAM A C1 1 HETATM 4115 C C2 . TAM P 5 . ? -44.028 20.765 41.154 1.00 59.79 ? 1507 TAM A C2 1 HETATM 4116 C C3 . TAM P 5 . ? -41.578 21.655 41.415 1.00 61.35 ? 1507 TAM A C3 1 HETATM 4117 C C4 . TAM P 5 . ? -43.945 22.332 38.443 1.00 60.04 ? 1507 TAM A C4 1 HETATM 4118 C C5 . TAM P 5 . ? -43.961 20.409 42.642 1.00 60.59 ? 1507 TAM A C5 1 HETATM 4119 C C6 . TAM P 5 . ? -41.733 22.927 42.241 1.00 59.38 ? 1507 TAM A C6 1 HETATM 4120 N N . TAM P 5 . ? -42.287 20.347 39.547 1.00 64.14 ? 1507 TAM A N 1 HETATM 4121 O O4 . TAM P 5 . ? -44.045 23.517 37.650 1.00 60.25 ? 1507 TAM A O4 1 HETATM 4122 O O5 . TAM P 5 . ? -45.095 19.595 42.974 1.00 59.66 ? 1507 TAM A O5 1 HETATM 4123 O O6 . TAM P 5 . ? -40.711 22.967 43.239 1.00 61.50 ? 1507 TAM A O6 1 HETATM 4124 C C1 . SIA Q 6 . ? -48.403 0.910 99.246 1.00 76.61 ? 1508 SIA A C1 1 HETATM 4125 C C2 . SIA Q 6 . ? -47.873 1.006 100.665 1.00 78.95 ? 1508 SIA A C2 1 HETATM 4126 C C3 . SIA Q 6 . ? -46.463 0.412 100.812 1.00 77.86 ? 1508 SIA A C3 1 HETATM 4127 C C4 . SIA Q 6 . ? -45.378 1.298 100.200 1.00 75.76 ? 1508 SIA A C4 1 HETATM 4128 C C5 . SIA Q 6 . ? -45.497 2.738 100.677 1.00 76.99 ? 1508 SIA A C5 1 HETATM 4129 C C6 . SIA Q 6 . ? -46.923 3.227 100.441 1.00 78.62 ? 1508 SIA A C6 1 HETATM 4130 C C7 . SIA Q 6 . ? -47.136 4.661 100.916 1.00 78.74 ? 1508 SIA A C7 1 HETATM 4131 C C8 . SIA Q 6 . ? -48.610 5.050 100.877 1.00 78.05 ? 1508 SIA A C8 1 HETATM 4132 C C9 . SIA Q 6 . ? -48.771 6.547 100.647 1.00 76.53 ? 1508 SIA A C9 1 HETATM 4133 C C10 . SIA Q 6 . ? -43.874 4.580 100.539 1.00 75.28 ? 1508 SIA A C10 1 HETATM 4134 C C11 . SIA Q 6 . ? -42.924 5.320 99.639 1.00 70.70 ? 1508 SIA A C11 1 HETATM 4135 N N5 . SIA Q 6 . ? -44.541 3.573 99.967 1.00 76.11 ? 1508 SIA A N5 1 HETATM 4136 O O1A . SIA Q 6 . ? -47.769 0.268 98.376 1.00 67.75 ? 1508 SIA A O1A 1 HETATM 4137 O O1B . SIA Q 6 . ? -49.488 1.481 98.994 1.00 76.11 ? 1508 SIA A O1B 1 HETATM 4138 O O2 . SIA Q 6 . ? -48.780 0.272 101.503 1.00 80.70 ? 1508 SIA A O2 1 HETATM 4139 O O4 . SIA Q 6 . ? -44.079 0.809 100.546 1.00 75.73 ? 1508 SIA A O4 1 HETATM 4140 O O6 . SIA Q 6 . ? -47.862 2.372 101.112 1.00 79.05 ? 1508 SIA A O6 1 HETATM 4141 O O7 . SIA Q 6 . ? -46.656 4.812 102.255 1.00 80.94 ? 1508 SIA A O7 1 HETATM 4142 O O8 . SIA Q 6 . ? -49.274 4.331 99.833 1.00 77.60 ? 1508 SIA A O8 1 HETATM 4143 O O9 . SIA Q 6 . ? -50.164 6.871 100.607 1.00 76.13 ? 1508 SIA A O9 1 HETATM 4144 O O10 . SIA Q 6 . ? -44.020 4.888 101.712 1.00 73.08 ? 1508 SIA A O10 1 HETATM 4145 O O . HOH R 7 . ? -48.404 13.175 -14.291 1.00 37.54 ? 2001 HOH A O 1 HETATM 4146 O O . HOH R 7 . ? -51.631 13.167 -16.848 1.00 60.59 ? 2002 HOH A O 1 HETATM 4147 O O . HOH R 7 . ? -48.232 8.002 -8.659 1.00 31.41 ? 2003 HOH A O 1 HETATM 4148 O O . HOH R 7 . ? -50.882 10.392 -17.088 1.00 63.47 ? 2004 HOH A O 1 HETATM 4149 O O . HOH R 7 . ? -54.389 9.283 -5.190 1.00 44.12 ? 2005 HOH A O 1 HETATM 4150 O O . HOH R 7 . ? -57.192 10.719 -2.279 1.00 46.63 ? 2006 HOH A O 1 HETATM 4151 O O . HOH R 7 . ? -58.878 16.522 15.932 1.00 33.61 ? 2007 HOH A O 1 HETATM 4152 O O . HOH R 7 . ? -54.012 17.059 15.524 1.00 44.66 ? 2008 HOH A O 1 HETATM 4153 O O . HOH R 7 . ? -54.805 11.039 11.588 1.00 24.99 ? 2009 HOH A O 1 HETATM 4154 O O . HOH R 7 . ? -56.110 10.579 18.293 1.00 23.27 ? 2010 HOH A O 1 HETATM 4155 O O . HOH R 7 . ? -56.900 15.135 14.716 1.00 39.93 ? 2011 HOH A O 1 HETATM 4156 O O . HOH R 7 . ? -50.630 3.794 18.658 1.00 45.54 ? 2012 HOH A O 1 HETATM 4157 O O . HOH R 7 . ? -50.284 10.028 22.210 1.00 22.45 ? 2013 HOH A O 1 HETATM 4158 O O . HOH R 7 . ? -53.109 2.613 17.970 1.00 45.61 ? 2014 HOH A O 1 HETATM 4159 O O . HOH R 7 . ? -61.331 5.234 23.693 1.00 39.20 ? 2015 HOH A O 1 HETATM 4160 O O . HOH R 7 . ? -55.638 5.269 28.112 1.00 42.22 ? 2016 HOH A O 1 HETATM 4161 O O . HOH R 7 . ? -61.386 7.834 31.477 1.00 32.04 ? 2017 HOH A O 1 HETATM 4162 O O . HOH R 7 . ? -57.147 15.642 34.673 1.00 16.90 ? 2018 HOH A O 1 HETATM 4163 O O . HOH R 7 . ? -58.027 20.711 25.677 1.00 28.33 ? 2019 HOH A O 1 HETATM 4164 O O . HOH R 7 . ? -30.240 8.515 65.954 1.00 26.00 ? 2020 HOH A O 1 HETATM 4165 O O . HOH R 7 . ? -65.651 24.275 27.850 1.00 46.85 ? 2021 HOH A O 1 HETATM 4166 O O . HOH R 7 . ? -48.554 -4.539 65.634 1.00 41.31 ? 2022 HOH A O 1 HETATM 4167 O O . HOH R 7 . ? -59.921 20.644 22.693 1.00 52.48 ? 2023 HOH A O 1 HETATM 4168 O O . HOH R 7 . ? -65.371 19.204 28.442 1.00 43.72 ? 2024 HOH A O 1 HETATM 4169 O O . HOH R 7 . ? -62.138 15.111 33.896 1.00 44.48 ? 2025 HOH A O 1 HETATM 4170 O O . HOH R 7 . ? -67.575 23.883 33.398 1.00 39.75 ? 2026 HOH A O 1 HETATM 4171 O O . HOH R 7 . ? -36.552 -5.999 76.680 1.00 43.99 ? 2027 HOH A O 1 HETATM 4172 O O . HOH R 7 . ? -62.565 14.073 23.962 1.00 30.04 ? 2028 HOH A O 1 HETATM 4173 O O . HOH R 7 . ? -60.355 13.720 22.183 1.00 31.00 ? 2029 HOH A O 1 HETATM 4174 O O . HOH R 7 . ? -49.990 7.230 24.053 1.00 46.26 ? 2030 HOH A O 1 HETATM 4175 O O . HOH R 7 . ? -29.080 9.782 62.232 1.00 41.60 ? 2031 HOH A O 1 HETATM 4176 O O . HOH R 7 . ? -51.008 4.778 32.094 1.00 46.96 ? 2032 HOH A O 1 HETATM 4177 O O . HOH R 7 . ? -48.155 7.469 26.466 1.00 34.35 ? 2033 HOH A O 1 HETATM 4178 O O . HOH R 7 . ? -54.094 5.301 66.445 1.00 41.56 ? 2034 HOH A O 1 HETATM 4179 O O . HOH R 7 . ? -52.547 7.441 71.574 1.00 50.60 ? 2035 HOH A O 1 HETATM 4180 O O . HOH R 7 . ? -50.871 -2.216 68.391 1.00 43.34 ? 2036 HOH A O 1 HETATM 4181 O O . HOH R 7 . ? -50.136 5.018 34.242 1.00 45.45 ? 2037 HOH A O 1 HETATM 4182 O O . HOH R 7 . ? -48.429 7.713 38.156 1.00 30.63 ? 2038 HOH A O 1 HETATM 4183 O O . HOH R 7 . ? -51.766 5.677 36.698 1.00 27.93 ? 2039 HOH A O 1 HETATM 4184 O O . HOH R 7 . ? -54.746 6.414 79.405 1.00 45.36 ? 2040 HOH A O 1 HETATM 4185 O O . HOH R 7 . ? -56.396 6.508 39.077 1.00 37.80 ? 2041 HOH A O 1 HETATM 4186 O O . HOH R 7 . ? -55.764 8.128 43.162 1.00 18.83 ? 2042 HOH A O 1 HETATM 4187 O O . HOH R 7 . ? -45.422 23.005 84.143 1.00 35.23 ? 2043 HOH A O 1 HETATM 4188 O O . HOH R 7 . ? -49.553 2.536 44.307 1.00 30.87 ? 2044 HOH A O 1 HETATM 4189 O O . HOH R 7 . ? -47.046 3.631 43.417 1.00 37.31 ? 2045 HOH A O 1 HETATM 4190 O O . HOH R 7 . ? -46.864 7.823 45.307 1.00 24.37 ? 2046 HOH A O 1 HETATM 4191 O O . HOH R 7 . ? -53.025 5.259 44.180 1.00 33.29 ? 2047 HOH A O 1 HETATM 4192 O O . HOH R 7 . ? -52.642 17.344 75.186 1.00 33.73 ? 2048 HOH A O 1 HETATM 4193 O O . HOH R 7 . ? -57.317 7.148 49.957 1.00 44.88 ? 2049 HOH A O 1 HETATM 4194 O O . HOH R 7 . ? -59.375 7.182 44.820 1.00 58.88 ? 2050 HOH A O 1 HETATM 4195 O O . HOH R 7 . ? -50.832 15.082 74.068 1.00 24.37 ? 2051 HOH A O 1 HETATM 4196 O O . HOH R 7 . ? -51.770 17.762 70.825 1.00 18.04 ? 2052 HOH A O 1 HETATM 4197 O O . HOH R 7 . ? -38.346 20.771 70.604 1.00 22.02 ? 2053 HOH A O 1 HETATM 4198 O O . HOH R 7 . ? -50.167 0.956 48.178 1.00 43.56 ? 2054 HOH A O 1 HETATM 4199 O O . HOH R 7 . ? -34.330 20.729 68.739 1.00 37.83 ? 2055 HOH A O 1 HETATM 4200 O O . HOH R 7 . ? -55.240 1.356 50.784 1.00 38.18 ? 2056 HOH A O 1 HETATM 4201 O O . HOH R 7 . ? -48.387 1.156 50.561 1.00 40.29 ? 2057 HOH A O 1 HETATM 4202 O O . HOH R 7 . ? -53.294 -0.705 59.252 1.00 46.45 ? 2058 HOH A O 1 HETATM 4203 O O . HOH R 7 . ? -41.683 3.145 56.108 1.00 20.17 ? 2059 HOH A O 1 HETATM 4204 O O . HOH R 7 . ? -38.692 2.956 58.292 1.00 19.70 ? 2060 HOH A O 1 HETATM 4205 O O . HOH R 7 . ? -36.485 0.395 62.193 1.00 15.69 ? 2061 HOH A O 1 HETATM 4206 O O . HOH R 7 . ? -34.198 1.280 59.303 1.00 23.13 ? 2062 HOH A O 1 HETATM 4207 O O . HOH R 7 . ? -36.422 -4.583 56.818 1.00 34.62 ? 2063 HOH A O 1 HETATM 4208 O O . HOH R 7 . ? -39.522 -5.166 62.063 1.00 31.53 ? 2064 HOH A O 1 HETATM 4209 O O . HOH R 7 . ? -35.553 -5.320 60.195 1.00 38.90 ? 2065 HOH A O 1 HETATM 4210 O O . HOH R 7 . ? -35.747 -3.384 61.771 1.00 58.85 ? 2066 HOH A O 1 HETATM 4211 O O . HOH R 7 . ? -32.999 -3.696 95.895 1.00 53.18 ? 2067 HOH A O 1 HETATM 4212 O O . HOH R 7 . ? -32.097 3.329 59.765 1.00 21.18 ? 2068 HOH A O 1 HETATM 4213 O O . HOH R 7 . ? -34.240 8.457 58.666 1.00 29.72 ? 2069 HOH A O 1 HETATM 4214 O O . HOH R 7 . ? -37.758 9.756 53.588 1.00 24.96 ? 2070 HOH A O 1 HETATM 4215 O O . HOH R 7 . ? -32.397 7.406 64.375 1.00 24.89 ? 2071 HOH A O 1 HETATM 4216 O O . HOH R 7 . ? -29.929 5.721 66.246 1.00 22.71 ? 2072 HOH A O 1 HETATM 4217 O O . HOH R 7 . ? -33.488 0.055 65.971 1.00 19.25 ? 2073 HOH A O 1 HETATM 4218 O O . HOH R 7 . ? -34.670 1.953 68.963 1.00 30.73 ? 2074 HOH A O 1 HETATM 4219 O O . HOH R 7 . ? -37.313 -1.499 63.877 1.00 31.10 ? 2075 HOH A O 1 HETATM 4220 O O . HOH R 7 . ? -35.987 0.481 67.232 1.00 34.15 ? 2076 HOH A O 1 HETATM 4221 O O . HOH R 7 . ? -39.786 -1.268 68.053 1.00 22.27 ? 2077 HOH A O 1 HETATM 4222 O O . HOH R 7 . ? -40.971 -2.200 70.708 1.00 29.62 ? 2078 HOH A O 1 HETATM 4223 O O . HOH R 7 . ? -47.136 -3.473 68.104 1.00 31.93 ? 2079 HOH A O 1 HETATM 4224 O O . HOH R 7 . ? -43.252 -3.938 66.445 1.00 26.77 ? 2080 HOH A O 1 HETATM 4225 O O . HOH R 7 . ? -47.532 2.650 72.161 1.00 19.49 ? 2081 HOH A O 1 HETATM 4226 O O . HOH R 7 . ? -45.805 -5.902 69.108 1.00 51.33 ? 2082 HOH A O 1 HETATM 4227 O O . HOH R 7 . ? -44.987 -2.533 75.934 1.00 34.90 ? 2083 HOH A O 1 HETATM 4228 O O . HOH R 7 . ? -48.389 3.846 78.374 1.00 37.80 ? 2084 HOH A O 1 HETATM 4229 O O . HOH R 7 . ? -52.924 -3.387 75.500 1.00 45.72 ? 2085 HOH A O 1 HETATM 4230 O O . HOH R 7 . ? -46.997 -4.387 78.413 1.00 43.64 ? 2086 HOH A O 1 HETATM 4231 O O . HOH R 7 . ? -46.668 1.998 80.102 1.00 35.36 ? 2087 HOH A O 1 HETATM 4232 O O . HOH R 7 . ? -48.648 8.760 78.983 1.00 27.41 ? 2088 HOH A O 1 HETATM 4233 O O . HOH R 7 . ? -46.350 10.303 75.279 1.00 18.17 ? 2089 HOH A O 1 HETATM 4234 O O . HOH R 7 . ? -46.767 5.034 83.712 1.00 29.57 ? 2090 HOH A O 1 HETATM 4235 O O . HOH R 7 . ? -50.287 5.723 79.121 1.00 38.32 ? 2091 HOH A O 1 HETATM 4236 O O . HOH R 7 . ? -31.969 20.917 72.466 1.00 31.48 ? 2092 HOH A O 1 HETATM 4237 O O . HOH R 7 . ? -38.181 2.967 80.221 1.00 21.79 ? 2093 HOH A O 1 HETATM 4238 O O . HOH R 7 . ? -36.387 6.121 80.611 1.00 23.37 ? 2094 HOH A O 1 HETATM 4239 O O . HOH R 7 . ? -45.745 -1.610 84.473 1.00 35.88 ? 2095 HOH A O 1 HETATM 4240 O O . HOH R 7 . ? -40.262 -2.930 77.905 1.00 38.73 ? 2096 HOH A O 1 HETATM 4241 O O . HOH R 7 . ? -33.579 -2.337 79.803 1.00 33.82 ? 2097 HOH A O 1 HETATM 4242 O O . HOH R 7 . ? -37.307 2.001 82.702 1.00 26.37 ? 2098 HOH A O 1 HETATM 4243 O O . HOH R 7 . ? -37.131 -5.080 84.170 1.00 44.13 ? 2099 HOH A O 1 HETATM 4244 O O . HOH R 7 . ? -47.437 26.463 100.247 1.00 49.05 ? 2100 HOH A O 1 HETATM 4245 O O . HOH R 7 . ? -35.687 -4.199 74.768 1.00 29.06 ? 2101 HOH A O 1 HETATM 4246 O O . HOH R 7 . ? -32.845 1.687 85.754 1.00 39.07 ? 2102 HOH A O 1 HETATM 4247 O O . HOH R 7 . ? -42.826 23.553 81.582 1.00 40.66 ? 2103 HOH A O 1 HETATM 4248 O O . HOH R 7 . ? -33.990 5.748 79.251 1.00 22.15 ? 2104 HOH A O 1 HETATM 4249 O O . HOH R 7 . ? -28.964 4.393 72.086 1.00 24.06 ? 2105 HOH A O 1 HETATM 4250 O O . HOH R 7 . ? -29.537 4.329 81.669 1.00 34.39 ? 2106 HOH A O 1 HETATM 4251 O O . HOH R 7 . ? -37.015 -1.612 68.500 1.00 30.28 ? 2107 HOH A O 1 HETATM 4252 O O . HOH R 7 . ? -38.801 -1.132 73.198 1.00 40.35 ? 2108 HOH A O 1 HETATM 4253 O O . HOH R 7 . ? -51.966 26.799 98.511 1.00 37.23 ? 2109 HOH A O 1 HETATM 4254 O O . HOH R 7 . ? -25.456 7.178 72.034 1.00 36.41 ? 2110 HOH A O 1 HETATM 4255 O O . HOH R 7 . ? -32.394 9.824 67.244 1.00 23.89 ? 2111 HOH A O 1 HETATM 4256 O O . HOH R 7 . ? -31.673 9.336 61.218 1.00 27.58 ? 2112 HOH A O 1 HETATM 4257 O O . HOH R 7 . ? -33.526 11.281 63.741 1.00 35.15 ? 2113 HOH A O 1 HETATM 4258 O O . HOH R 7 . ? -32.078 6.084 60.448 1.00 24.78 ? 2114 HOH A O 1 HETATM 4259 O O . HOH R 7 . ? -47.435 24.370 85.367 1.00 37.01 ? 2115 HOH A O 1 HETATM 4260 O O . HOH R 7 . ? -52.215 6.069 69.238 1.00 34.65 ? 2116 HOH A O 1 HETATM 4261 O O . HOH R 7 . ? -50.706 9.016 72.130 1.00 34.42 ? 2117 HOH A O 1 HETATM 4262 O O . HOH R 7 . ? -51.204 5.842 72.848 1.00 37.69 ? 2118 HOH A O 1 HETATM 4263 O O . HOH R 7 . ? -53.203 -0.451 69.510 1.00 27.19 ? 2119 HOH A O 1 HETATM 4264 O O . HOH R 7 . ? -54.438 4.705 74.940 1.00 46.35 ? 2120 HOH A O 1 HETATM 4265 O O . HOH R 7 . ? -55.630 -0.459 76.376 1.00 44.92 ? 2121 HOH A O 1 HETATM 4266 O O . HOH R 7 . ? -51.064 -6.265 73.068 1.00 55.69 ? 2122 HOH A O 1 HETATM 4267 O O . HOH R 7 . ? -52.271 6.040 75.381 1.00 51.72 ? 2123 HOH A O 1 HETATM 4268 O O . HOH R 7 . ? -53.160 5.150 81.467 1.00 41.76 ? 2124 HOH A O 1 HETATM 4269 O O . HOH R 7 . ? -51.020 7.591 79.202 1.00 52.89 ? 2125 HOH A O 1 HETATM 4270 O O . HOH R 7 . ? -48.071 -2.167 88.372 1.00 43.39 ? 2126 HOH A O 1 HETATM 4271 O O . HOH R 7 . ? -48.570 5.247 85.825 1.00 30.89 ? 2127 HOH A O 1 HETATM 4272 O O . HOH R 7 . ? -49.665 5.834 97.686 1.00 42.14 ? 2128 HOH A O 1 HETATM 4273 O O . HOH R 7 . ? -54.721 6.179 63.740 1.00 43.43 ? 2129 HOH A O 1 HETATM 4274 O O . HOH R 7 . ? -55.408 11.817 68.980 1.00 40.15 ? 2130 HOH A O 1 HETATM 4275 O O . HOH R 7 . ? -54.681 9.462 72.136 1.00 49.43 ? 2131 HOH A O 1 HETATM 4276 O O . HOH R 7 . ? -54.717 17.583 85.165 1.00 39.35 ? 2132 HOH A O 1 HETATM 4277 O O . HOH R 7 . ? -52.157 18.048 82.499 1.00 48.11 ? 2133 HOH A O 1 HETATM 4278 O O . HOH R 7 . ? -49.708 -5.489 56.788 1.00 52.22 ? 2134 HOH A O 1 HETATM 4279 O O . HOH R 7 . ? -47.918 -7.710 63.009 1.00 53.70 ? 2135 HOH A O 1 HETATM 4280 O O . HOH R 7 . ? -51.301 14.604 81.854 1.00 27.59 ? 2136 HOH A O 1 HETATM 4281 O O . HOH R 7 . ? -51.724 18.996 79.602 1.00 32.47 ? 2137 HOH A O 1 HETATM 4282 O O . HOH R 7 . ? -45.120 20.115 83.481 1.00 28.70 ? 2138 HOH A O 1 HETATM 4283 O O . HOH R 7 . ? -42.635 1.959 47.893 1.00 37.34 ? 2139 HOH A O 1 HETATM 4284 O O . HOH R 7 . ? -50.503 21.749 75.761 1.00 23.00 ? 2140 HOH A O 1 HETATM 4285 O O . HOH R 7 . ? -47.346 25.178 75.588 1.00 49.55 ? 2141 HOH A O 1 HETATM 4286 O O . HOH R 7 . ? -51.048 19.010 76.866 1.00 23.37 ? 2142 HOH A O 1 HETATM 4287 O O . HOH R 7 . ? -50.365 10.171 74.852 1.00 38.76 ? 2143 HOH A O 1 HETATM 4288 O O . HOH R 7 . ? -47.335 16.199 71.538 1.00 16.65 ? 2144 HOH A O 1 HETATM 4289 O O . HOH R 7 . ? -43.528 5.793 38.663 1.00 45.21 ? 2145 HOH A O 1 HETATM 4290 O O . HOH R 7 . ? -48.455 12.199 67.215 1.00 18.50 ? 2146 HOH A O 1 HETATM 4291 O O . HOH R 7 . ? -50.105 15.810 71.548 1.00 15.92 ? 2147 HOH A O 1 HETATM 4292 O O . HOH R 7 . ? -60.589 22.549 60.383 1.00 36.22 ? 2148 HOH A O 1 HETATM 4293 O O . HOH R 7 . ? -46.015 16.700 69.063 1.00 17.75 ? 2149 HOH A O 1 HETATM 4294 O O . HOH R 7 . ? -36.638 18.969 71.479 1.00 18.89 ? 2150 HOH A O 1 HETATM 4295 O O . HOH R 7 . ? -37.345 16.730 65.007 1.00 22.17 ? 2151 HOH A O 1 HETATM 4296 O O . HOH R 7 . ? -33.881 14.172 66.194 1.00 24.73 ? 2152 HOH A O 1 HETATM 4297 O O . HOH R 7 . ? -34.856 18.259 67.088 1.00 31.12 ? 2153 HOH A O 1 HETATM 4298 O O . HOH R 7 . ? -32.130 12.628 67.111 1.00 39.88 ? 2154 HOH A O 1 HETATM 4299 O O . HOH R 7 . ? -31.150 11.669 68.727 1.00 44.29 ? 2155 HOH A O 1 HETATM 4300 O O . HOH R 7 . ? -34.398 13.389 74.761 1.00 28.59 ? 2156 HOH A O 1 HETATM 4301 O O . HOH R 7 . ? -61.922 16.561 43.289 1.00 46.31 ? 2157 HOH A O 1 HETATM 4302 O O . HOH R 7 . ? -62.121 13.780 39.084 1.00 41.97 ? 2158 HOH A O 1 HETATM 4303 O O . HOH R 7 . ? -24.124 8.440 89.508 1.00 48.33 ? 2159 HOH A O 1 HETATM 4304 O O . HOH R 7 . ? -29.736 3.313 84.655 1.00 48.89 ? 2160 HOH A O 1 HETATM 4305 O O . HOH R 7 . ? -32.272 5.471 86.425 1.00 35.01 ? 2161 HOH A O 1 HETATM 4306 O O . HOH R 7 . ? -28.823 8.064 89.943 1.00 36.86 ? 2162 HOH A O 1 HETATM 4307 O O . HOH R 7 . ? -26.291 7.366 90.704 1.00 49.27 ? 2163 HOH A O 1 HETATM 4308 O O . HOH R 7 . ? -29.084 10.256 92.505 1.00 38.06 ? 2164 HOH A O 1 HETATM 4309 O O . HOH R 7 . ? -23.202 14.949 87.179 1.00 37.93 ? 2165 HOH A O 1 HETATM 4310 O O . HOH R 7 . ? -22.967 12.777 89.699 1.00 42.22 ? 2166 HOH A O 1 HETATM 4311 O O . HOH R 7 . ? -26.069 16.987 95.174 1.00 39.24 ? 2167 HOH A O 1 HETATM 4312 O O . HOH R 7 . ? -26.650 19.178 99.710 1.00 56.88 ? 2168 HOH A O 1 HETATM 4313 O O . HOH R 7 . ? -31.914 10.690 92.841 1.00 29.23 ? 2169 HOH A O 1 HETATM 4314 O O . HOH R 7 . ? -38.728 6.324 100.289 1.00 33.79 ? 2170 HOH A O 1 HETATM 4315 O O . HOH R 7 . ? -33.303 0.283 97.685 1.00 47.74 ? 2171 HOH A O 1 HETATM 4316 O O . HOH R 7 . ? -37.685 17.597 16.786 1.00 49.88 ? 2172 HOH A O 1 HETATM 4317 O O . HOH R 7 . ? -38.156 5.567 94.179 1.00 27.03 ? 2173 HOH A O 1 HETATM 4318 O O . HOH R 7 . ? -41.224 2.434 100.067 1.00 41.95 ? 2174 HOH A O 1 HETATM 4319 O O . HOH R 7 . ? -43.722 -0.832 98.729 1.00 51.54 ? 2175 HOH A O 1 HETATM 4320 O O . HOH R 7 . ? -39.817 -2.070 98.025 1.00 50.02 ? 2176 HOH A O 1 HETATM 4321 O O . HOH R 7 . ? -48.646 3.216 96.963 1.00 39.97 ? 2177 HOH A O 1 HETATM 4322 O O . HOH R 7 . ? -52.279 -0.747 94.652 1.00 45.73 ? 2178 HOH A O 1 HETATM 4323 O O . HOH R 7 . ? -44.268 6.850 25.821 1.00 49.78 ? 2179 HOH A O 1 HETATM 4324 O O . HOH R 7 . ? -38.135 18.719 42.467 1.00 42.99 ? 2180 HOH A O 1 HETATM 4325 O O . HOH R 7 . ? -44.424 -7.156 88.063 1.00 53.81 ? 2181 HOH A O 1 HETATM 4326 O O . HOH R 7 . ? -37.969 19.747 56.957 1.00 51.92 ? 2182 HOH A O 1 HETATM 4327 O O . HOH R 7 . ? -36.068 18.787 61.102 1.00 45.78 ? 2183 HOH A O 1 HETATM 4328 O O . HOH R 7 . ? -38.364 22.164 62.186 1.00 34.94 ? 2184 HOH A O 1 HETATM 4329 O O . HOH R 7 . ? -41.900 -5.983 85.528 1.00 49.17 ? 2185 HOH A O 1 HETATM 4330 O O . HOH R 7 . ? -42.184 22.618 60.786 1.00 23.15 ? 2186 HOH A O 1 HETATM 4331 O O . HOH R 7 . ? -55.370 8.757 67.399 1.00 51.74 ? 2187 HOH A O 1 HETATM 4332 O O . HOH R 7 . ? -63.277 20.243 69.097 1.00 36.99 ? 2188 HOH A O 1 HETATM 4333 O O . HOH R 7 . ? -57.356 22.137 78.209 1.00 57.64 ? 2189 HOH A O 1 HETATM 4334 O O . HOH R 7 . ? -43.061 -6.193 96.976 1.00 46.82 ? 2190 HOH A O 1 HETATM 4335 O O . HOH R 7 . ? -39.556 -4.069 96.489 1.00 48.56 ? 2191 HOH A O 1 HETATM 4336 O O . HOH R 7 . ? -35.746 11.823 86.043 1.00 29.23 ? 2192 HOH A O 1 HETATM 4337 O O . HOH R 7 . ? -53.113 27.113 29.432 1.00 42.64 ? 2193 HOH A O 1 HETATM 4338 O O . HOH R 7 . ? -50.463 29.134 30.361 0.33 56.07 ? 2194 HOH A O 1 HETATM 4339 O O . HOH R 7 . ? -39.994 13.627 98.862 1.00 31.00 ? 2195 HOH A O 1 HETATM 4340 O O . HOH R 7 . ? -39.814 6.906 105.309 1.00 34.73 ? 2196 HOH A O 1 HETATM 4341 O O . HOH R 7 . ? -48.102 27.203 27.073 1.00 37.71 ? 2197 HOH A O 1 HETATM 4342 O O . HOH R 7 . ? -50.459 29.133 27.511 0.33 49.02 ? 2198 HOH A O 1 HETATM 4343 O O . HOH R 7 . ? -42.620 6.860 105.422 1.00 39.01 ? 2199 HOH A O 1 HETATM 4344 O O . HOH R 7 . ? -44.017 6.792 108.807 1.00 43.79 ? 2200 HOH A O 1 HETATM 4345 O O . HOH R 7 . ? -50.459 29.132 24.704 0.33 53.48 ? 2201 HOH A O 1 HETATM 4346 O O . HOH R 7 . ? -36.643 5.936 109.160 1.00 48.94 ? 2202 HOH A O 1 HETATM 4347 O O . HOH R 7 . ? -38.725 19.886 5.415 1.00 53.14 ? 2203 HOH A O 1 HETATM 4348 O O . HOH R 7 . ? -38.739 16.769 109.789 1.00 45.65 ? 2204 HOH A O 1 HETATM 4349 O O . HOH R 7 . ? -37.266 21.396 0.782 1.00 36.78 ? 2205 HOH A O 1 HETATM 4350 O O . HOH R 7 . ? -50.459 29.132 -3.570 0.33 39.87 ? 2206 HOH A O 1 HETATM 4351 O O . HOH R 7 . ? -29.670 19.601 101.355 1.00 39.49 ? 2207 HOH A O 1 HETATM 4352 O O . HOH R 7 . ? -27.497 21.327 101.357 1.00 53.18 ? 2208 HOH A O 1 HETATM 4353 O O . HOH R 7 . ? -26.258 22.859 97.945 1.00 49.17 ? 2209 HOH A O 1 HETATM 4354 O O . HOH R 7 . ? -27.759 23.957 101.994 1.00 45.10 ? 2210 HOH A O 1 HETATM 4355 O O . HOH R 7 . ? -25.821 19.680 97.124 1.00 42.32 ? 2211 HOH A O 1 HETATM 4356 O O . HOH R 7 . ? -23.287 18.766 93.354 1.00 53.94 ? 2212 HOH A O 1 HETATM 4357 O O . HOH R 7 . ? -26.739 19.576 85.927 1.00 27.39 ? 2213 HOH A O 1 HETATM 4358 O O . HOH R 7 . ? -21.996 17.842 84.713 1.00 32.07 ? 2214 HOH A O 1 HETATM 4359 O O . HOH R 7 . ? -22.139 17.572 87.725 1.00 39.21 ? 2215 HOH A O 1 HETATM 4360 O O . HOH R 7 . ? -19.851 23.185 80.936 1.00 46.59 ? 2216 HOH A O 1 HETATM 4361 O O . HOH R 7 . ? -21.994 24.681 86.088 1.00 40.41 ? 2217 HOH A O 1 HETATM 4362 O O . HOH R 7 . ? -18.764 22.419 89.501 1.00 47.45 ? 2218 HOH A O 1 HETATM 4363 O O . HOH R 7 . ? -19.370 17.203 77.861 1.00 38.18 ? 2219 HOH A O 1 HETATM 4364 O O . HOH R 7 . ? -22.622 13.928 82.983 1.00 41.51 ? 2220 HOH A O 1 HETATM 4365 O O . HOH R 7 . ? -41.601 17.146 -17.348 1.00 46.19 ? 2221 HOH A O 1 HETATM 4366 O O . HOH R 7 . ? -27.049 20.202 73.947 1.00 38.82 ? 2222 HOH A O 1 HETATM 4367 O O . HOH R 7 . ? -27.789 16.599 75.460 1.00 31.30 ? 2223 HOH A O 1 HETATM 4368 O O . HOH R 7 . ? -32.190 22.250 74.839 1.00 31.39 ? 2224 HOH A O 1 HETATM 4369 O O . HOH R 7 . ? -48.976 25.491 -17.509 1.00 62.89 ? 2225 HOH A O 1 HETATM 4370 O O . HOH R 7 . ? -34.337 13.412 84.592 1.00 21.86 ? 2226 HOH A O 1 HETATM 4371 O O . HOH R 7 . ? -48.933 20.197 90.672 1.00 27.60 ? 2227 HOH A O 1 HETATM 4372 O O . HOH R 7 . ? -56.141 11.952 107.179 1.00 41.12 ? 2228 HOH A O 1 HETATM 4373 O O . HOH R 7 . ? -50.265 9.147 99.455 1.00 42.07 ? 2229 HOH A O 1 HETATM 4374 O O . HOH R 7 . ? -43.509 18.228 103.676 1.00 43.17 ? 2230 HOH A O 1 HETATM 4375 O O . HOH R 7 . ? -45.755 20.147 110.103 1.00 41.91 ? 2231 HOH A O 1 HETATM 4376 O O . HOH R 7 . ? -43.149 21.777 105.105 1.00 42.96 ? 2232 HOH A O 1 HETATM 4377 O O . HOH R 7 . ? -50.010 19.999 105.000 1.00 40.51 ? 2233 HOH A O 1 HETATM 4378 O O . HOH R 7 . ? -48.559 22.432 100.196 1.00 34.83 ? 2234 HOH A O 1 HETATM 4379 O O . HOH R 7 . ? -51.794 20.494 100.681 1.00 36.87 ? 2235 HOH A O 1 HETATM 4380 O O . HOH R 7 . ? -43.616 19.705 101.323 1.00 33.19 ? 2236 HOH A O 1 HETATM 4381 O O . HOH R 7 . ? -41.414 20.718 99.694 1.00 33.19 ? 2237 HOH A O 1 HETATM 4382 O O . HOH R 7 . ? -44.922 26.706 101.270 1.00 42.65 ? 2238 HOH A O 1 HETATM 4383 O O . HOH R 7 . ? -41.095 23.565 101.485 1.00 31.60 ? 2239 HOH A O 1 HETATM 4384 O O . HOH R 7 . ? -34.598 26.356 93.916 1.00 35.15 ? 2240 HOH A O 1 HETATM 4385 O O . HOH R 7 . ? -36.559 25.648 87.029 1.00 37.98 ? 2241 HOH A O 1 HETATM 4386 O O . HOH R 7 . ? -32.830 26.505 82.988 1.00 42.82 ? 2242 HOH A O 1 HETATM 4387 O O . HOH R 7 . ? -36.981 32.402 83.057 1.00 45.40 ? 2243 HOH A O 1 HETATM 4388 O O . HOH R 7 . ? -32.167 32.488 78.723 1.00 58.77 ? 2244 HOH A O 1 HETATM 4389 O O . HOH R 7 . ? -32.497 26.453 79.265 1.00 47.91 ? 2245 HOH A O 1 HETATM 4390 O O . HOH R 7 . ? -35.469 32.975 86.945 1.00 38.13 ? 2246 HOH A O 1 HETATM 4391 O O . HOH R 7 . ? -40.935 31.126 92.106 1.00 34.92 ? 2247 HOH A O 1 HETATM 4392 O O . HOH R 7 . ? -42.440 21.815 83.687 1.00 26.08 ? 2248 HOH A O 1 HETATM 4393 O O . HOH R 7 . ? -42.711 24.202 85.402 1.00 41.25 ? 2249 HOH A O 1 HETATM 4394 O O . HOH R 7 . ? -40.586 23.356 81.840 1.00 33.62 ? 2250 HOH A O 1 HETATM 4395 O O . HOH R 7 . ? -42.893 29.185 89.650 1.00 43.29 ? 2251 HOH A O 1 HETATM 4396 O O . HOH R 7 . ? -45.444 26.362 88.633 1.00 41.39 ? 2252 HOH A O 1 HETATM 4397 O O . HOH R 7 . ? -48.451 25.036 92.043 1.00 33.22 ? 2253 HOH A O 1 HETATM 4398 O O . HOH R 7 . ? -49.647 22.330 92.428 1.00 28.28 ? 2254 HOH A O 1 HETATM 4399 O O . HOH R 7 . ? -52.055 22.911 99.308 1.00 37.29 ? 2255 HOH A O 1 HETATM 4400 O O . HOH R 7 . ? -52.587 25.326 96.170 1.00 37.64 ? 2256 HOH A O 1 HETATM 4401 O O . HOH R 7 . ? -56.119 19.848 97.398 1.00 36.09 ? 2257 HOH A O 1 HETATM 4402 O O . HOH R 7 . ? -57.555 17.611 101.139 1.00 42.91 ? 2258 HOH A O 1 HETATM 4403 O O . HOH R 7 . ? -60.472 14.409 99.609 1.00 53.46 ? 2259 HOH A O 1 HETATM 4404 O O . HOH R 7 . ? -59.247 16.446 96.176 1.00 38.53 ? 2260 HOH A O 1 HETATM 4405 O O . HOH R 7 . ? -58.349 9.226 99.821 1.00 54.36 ? 2261 HOH A O 1 HETATM 4406 O O . HOH R 7 . ? -60.864 8.806 95.996 1.00 28.04 ? 2262 HOH A O 1 HETATM 4407 O O . HOH R 7 . ? -62.261 5.574 90.850 1.00 38.89 ? 2263 HOH A O 1 HETATM 4408 O O . HOH R 7 . ? -59.102 2.047 91.035 1.00 43.66 ? 2264 HOH A O 1 HETATM 4409 O O . HOH R 7 . ? -58.322 2.291 87.448 1.00 57.14 ? 2265 HOH A O 1 HETATM 4410 O O . HOH R 7 . ? -52.685 -1.049 92.034 1.00 47.99 ? 2266 HOH A O 1 HETATM 4411 O O . HOH R 7 . ? -52.649 6.950 97.680 1.00 38.00 ? 2267 HOH A O 1 HETATM 4412 O O . HOH R 7 . ? -56.500 13.534 88.723 1.00 31.43 ? 2268 HOH A O 1 HETATM 4413 O O . HOH R 7 . ? -48.498 23.202 87.684 1.00 37.83 ? 2269 HOH A O 1 HETATM 4414 O O . HOH R 7 . ? -38.672 24.090 81.885 1.00 43.48 ? 2270 HOH A O 1 HETATM 4415 O O . HOH R 7 . ? -39.355 23.215 77.804 1.00 33.30 ? 2271 HOH A O 1 HETATM 4416 O O . HOH R 7 . ? -36.423 24.918 81.417 1.00 39.47 ? 2272 HOH A O 1 HETATM 4417 O O . HOH R 7 . ? -30.004 26.546 82.380 1.00 36.53 ? 2273 HOH A O 1 HETATM 4418 O O . HOH R 7 . ? -24.332 27.403 78.083 1.00 43.56 ? 2274 HOH A O 1 HETATM 4419 O O . HOH R 7 . ? -24.547 29.040 82.014 1.00 43.41 ? 2275 HOH A O 1 HETATM 4420 O O . HOH R 7 . ? -27.661 30.023 82.180 1.00 42.74 ? 2276 HOH A O 1 HETATM 4421 O O . HOH R 7 . ? -30.441 6.756 91.832 1.00 34.78 ? 2277 HOH A O 1 HETATM 4422 O O . HOH R 7 . ? -34.102 19.319 70.900 1.00 27.57 ? 2278 HOH A O 1 HETATM 4423 O O . HOH R 7 . ? -26.766 14.880 68.423 1.00 58.63 ? 2279 HOH A O 1 HETATM 4424 O O . HOH R 7 . ? -24.605 9.291 70.273 1.00 43.12 ? 2280 HOH A O 1 HETATM 4425 O O . HOH R 7 . ? -27.797 17.343 68.930 1.00 44.90 ? 2281 HOH A O 1 HETATM 4426 O O . HOH R 7 . ? -28.301 19.946 69.577 1.00 55.07 ? 2282 HOH A O 1 HETATM 4427 O O . HOH R 7 . ? -35.354 20.126 64.676 1.00 49.34 ? 2283 HOH A O 1 HETATM 4428 O O . HOH R 7 . ? -31.875 13.297 62.857 1.00 30.78 ? 2284 HOH A O 1 HETATM 4429 O O . HOH R 7 . ? -45.291 15.609 63.531 1.00 22.37 ? 2285 HOH A O 1 HETATM 4430 O O . HOH R 7 . ? -44.406 13.790 61.305 1.00 30.45 ? 2286 HOH A O 1 HETATM 4431 O O . HOH R 7 . ? -46.265 14.306 65.802 1.00 24.22 ? 2287 HOH A O 1 HETATM 4432 O O . HOH R 7 . ? -46.020 12.092 62.924 1.00 29.21 ? 2288 HOH A O 1 HETATM 4433 O O . HOH R 7 . ? -49.916 11.102 64.791 1.00 17.19 ? 2289 HOH A O 1 HETATM 4434 O O . HOH R 7 . ? -53.315 8.651 63.606 1.00 30.09 ? 2290 HOH A O 1 HETATM 4435 O O . HOH R 7 . ? -52.452 11.720 65.804 1.00 20.09 ? 2291 HOH A O 1 HETATM 4436 O O . HOH R 7 . ? -52.890 15.528 69.507 1.00 17.07 ? 2292 HOH A O 1 HETATM 4437 O O . HOH R 7 . ? -54.570 14.120 71.119 1.00 25.58 ? 2293 HOH A O 1 HETATM 4438 O O . HOH R 7 . ? -51.462 12.252 73.681 1.00 33.12 ? 2294 HOH A O 1 HETATM 4439 O O . HOH R 7 . ? -53.997 12.205 72.975 1.00 38.81 ? 2295 HOH A O 1 HETATM 4440 O O . HOH R 7 . ? -53.662 3.345 62.450 1.00 27.86 ? 2296 HOH A O 1 HETATM 4441 O O . HOH R 7 . ? -50.778 -2.926 65.768 1.00 38.28 ? 2297 HOH A O 1 HETATM 4442 O O . HOH R 7 . ? -53.874 -2.847 63.365 1.00 36.81 ? 2298 HOH A O 1 HETATM 4443 O O . HOH R 7 . ? -46.875 -4.964 57.980 1.00 46.05 ? 2299 HOH A O 1 HETATM 4444 O O . HOH R 7 . ? -46.248 -4.660 64.405 1.00 32.77 ? 2300 HOH A O 1 HETATM 4445 O O . HOH R 7 . ? -43.554 -5.970 64.654 1.00 48.49 ? 2301 HOH A O 1 HETATM 4446 O O . HOH R 7 . ? -42.683 -8.383 57.688 1.00 37.78 ? 2302 HOH A O 1 HETATM 4447 O O . HOH R 7 . ? -35.583 -7.247 62.139 1.00 40.05 ? 2303 HOH A O 1 HETATM 4448 O O . HOH R 7 . ? -39.541 -3.433 50.597 1.00 34.58 ? 2304 HOH A O 1 HETATM 4449 O O . HOH R 7 . ? -42.221 -0.963 50.264 1.00 45.08 ? 2305 HOH A O 1 HETATM 4450 O O . HOH R 7 . ? -35.273 3.681 50.710 1.00 25.12 ? 2306 HOH A O 1 HETATM 4451 O O . HOH R 7 . ? -44.866 2.007 50.503 1.00 29.42 ? 2307 HOH A O 1 HETATM 4452 O O . HOH R 7 . ? -42.364 5.767 50.082 1.00 25.05 ? 2308 HOH A O 1 HETATM 4453 O O . HOH R 7 . ? -39.758 4.494 49.154 1.00 26.56 ? 2309 HOH A O 1 HETATM 4454 O O . HOH R 7 . ? -54.071 1.150 55.321 1.00 51.92 ? 2310 HOH A O 1 HETATM 4455 O O . HOH R 7 . ? -55.212 6.016 60.000 1.00 40.36 ? 2311 HOH A O 1 HETATM 4456 O O . HOH R 7 . ? -56.046 2.714 57.229 1.00 38.97 ? 2312 HOH A O 1 HETATM 4457 O O . HOH R 7 . ? -41.971 4.487 46.762 1.00 34.53 ? 2313 HOH A O 1 HETATM 4458 O O . HOH R 7 . ? -40.441 10.843 45.746 1.00 28.26 ? 2314 HOH A O 1 HETATM 4459 O O . HOH R 7 . ? -38.932 5.764 47.225 1.00 35.92 ? 2315 HOH A O 1 HETATM 4460 O O . HOH R 7 . ? -40.220 7.351 43.953 1.00 39.31 ? 2316 HOH A O 1 HETATM 4461 O O . HOH R 7 . ? -37.537 9.078 48.118 1.00 36.00 ? 2317 HOH A O 1 HETATM 4462 O O . HOH R 7 . ? -43.046 13.199 42.993 1.00 25.71 ? 2318 HOH A O 1 HETATM 4463 O O . HOH R 7 . ? -43.109 3.879 43.921 1.00 39.14 ? 2319 HOH A O 1 HETATM 4464 O O . HOH R 7 . ? -45.913 7.307 39.245 1.00 32.51 ? 2320 HOH A O 1 HETATM 4465 O O . HOH R 7 . ? -44.687 16.423 46.156 1.00 20.45 ? 2321 HOH A O 1 HETATM 4466 O O . HOH R 7 . ? -57.913 8.092 52.296 1.00 32.44 ? 2322 HOH A O 1 HETATM 4467 O O . HOH R 7 . ? -58.123 11.691 52.961 1.00 29.59 ? 2323 HOH A O 1 HETATM 4468 O O . HOH R 7 . ? -58.413 8.374 48.117 1.00 40.14 ? 2324 HOH A O 1 HETATM 4469 O O . HOH R 7 . ? -60.499 14.219 50.669 1.00 37.51 ? 2325 HOH A O 1 HETATM 4470 O O . HOH R 7 . ? -57.154 10.638 55.627 1.00 41.73 ? 2326 HOH A O 1 HETATM 4471 O O . HOH R 7 . ? -55.358 12.443 59.907 1.00 20.95 ? 2327 HOH A O 1 HETATM 4472 O O . HOH R 7 . ? -56.104 12.945 56.990 1.00 22.18 ? 2328 HOH A O 1 HETATM 4473 O O . HOH R 7 . ? -54.670 9.131 61.214 1.00 24.69 ? 2329 HOH A O 1 HETATM 4474 O O . HOH R 7 . ? -49.198 16.998 55.467 1.00 20.66 ? 2330 HOH A O 1 HETATM 4475 O O . HOH R 7 . ? -47.746 15.383 59.642 1.00 18.93 ? 2331 HOH A O 1 HETATM 4476 O O . HOH R 7 . ? -56.656 14.990 60.577 1.00 37.73 ? 2332 HOH A O 1 HETATM 4477 O O . HOH R 7 . ? -57.900 14.954 56.091 1.00 45.68 ? 2333 HOH A O 1 HETATM 4478 O O . HOH R 7 . ? -57.815 21.099 60.324 1.00 23.30 ? 2334 HOH A O 1 HETATM 4479 O O . HOH R 7 . ? -59.205 20.155 57.168 1.00 45.25 ? 2335 HOH A O 1 HETATM 4480 O O . HOH R 7 . ? -55.713 19.079 61.542 1.00 19.63 ? 2336 HOH A O 1 HETATM 4481 O O . HOH R 7 . ? -59.107 16.924 54.439 1.00 46.21 ? 2337 HOH A O 1 HETATM 4482 O O . HOH R 7 . ? -46.390 15.120 52.771 1.00 28.38 ? 2338 HOH A O 1 HETATM 4483 O O . HOH R 7 . ? -43.494 14.058 55.381 1.00 20.22 ? 2339 HOH A O 1 HETATM 4484 O O . HOH R 7 . ? -46.731 16.455 56.187 1.00 23.49 ? 2340 HOH A O 1 HETATM 4485 O O . HOH R 7 . ? -34.925 10.954 59.349 1.00 33.11 ? 2341 HOH A O 1 HETATM 4486 O O . HOH R 7 . ? -43.181 15.472 52.768 1.00 29.70 ? 2342 HOH A O 1 HETATM 4487 O O . HOH R 7 . ? -43.325 16.239 48.677 1.00 26.17 ? 2343 HOH A O 1 HETATM 4488 O O . HOH R 7 . ? -43.027 21.573 47.173 1.00 41.71 ? 2344 HOH A O 1 HETATM 4489 O O . HOH R 7 . ? -48.276 19.496 51.771 1.00 16.32 ? 2345 HOH A O 1 HETATM 4490 O O . HOH R 7 . ? -44.253 18.056 52.173 1.00 33.12 ? 2346 HOH A O 1 HETATM 4491 O O . HOH R 7 . ? -48.521 16.895 52.913 1.00 19.82 ? 2347 HOH A O 1 HETATM 4492 O O . HOH R 7 . ? -50.992 19.792 52.041 1.00 14.54 ? 2348 HOH A O 1 HETATM 4493 O O . HOH R 7 . ? -61.985 13.695 46.820 1.00 47.46 ? 2349 HOH A O 1 HETATM 4494 O O . HOH R 7 . ? -58.696 24.386 47.545 1.00 25.72 ? 2350 HOH A O 1 HETATM 4495 O O . HOH R 7 . ? -61.859 17.854 46.219 1.00 47.02 ? 2351 HOH A O 1 HETATM 4496 O O . HOH R 7 . ? -61.503 14.084 43.804 1.00 39.41 ? 2352 HOH A O 1 HETATM 4497 O O . HOH R 7 . ? -63.288 12.389 42.286 1.00 50.68 ? 2353 HOH A O 1 HETATM 4498 O O . HOH R 7 . ? -65.369 9.825 44.796 1.00 57.63 ? 2354 HOH A O 1 HETATM 4499 O O . HOH R 7 . ? -60.411 15.025 41.121 1.00 42.61 ? 2355 HOH A O 1 HETATM 4500 O O . HOH R 7 . ? -59.555 14.922 38.989 1.00 36.76 ? 2356 HOH A O 1 HETATM 4501 O O . HOH R 7 . ? -58.365 13.990 36.780 1.00 26.76 ? 2357 HOH A O 1 HETATM 4502 O O . HOH R 7 . ? -49.924 16.432 30.742 1.00 18.49 ? 2358 HOH A O 1 HETATM 4503 O O . HOH R 7 . ? -52.286 15.659 17.591 1.00 41.36 ? 2359 HOH A O 1 HETATM 4504 O O . HOH R 7 . ? -53.394 16.615 21.200 1.00 22.95 ? 2360 HOH A O 1 HETATM 4505 O O . HOH R 7 . ? -60.319 16.021 20.602 1.00 31.41 ? 2361 HOH A O 1 HETATM 4506 O O . HOH R 7 . ? -63.346 11.480 13.976 1.00 38.05 ? 2362 HOH A O 1 HETATM 4507 O O . HOH R 7 . ? -56.371 3.064 10.767 1.00 36.26 ? 2363 HOH A O 1 HETATM 4508 O O . HOH R 7 . ? -58.449 7.751 8.124 1.00 30.62 ? 2364 HOH A O 1 HETATM 4509 O O . HOH R 7 . ? -59.369 4.555 0.138 1.00 53.46 ? 2365 HOH A O 1 HETATM 4510 O O . HOH R 7 . ? -58.007 11.851 0.253 1.00 48.19 ? 2366 HOH A O 1 HETATM 4511 O O . HOH R 7 . ? -56.680 7.069 5.964 1.00 31.72 ? 2367 HOH A O 1 HETATM 4512 O O . HOH R 7 . ? -59.779 13.972 7.690 1.00 34.80 ? 2368 HOH A O 1 HETATM 4513 O O . HOH R 7 . ? -43.394 3.071 9.833 1.00 36.48 ? 2369 HOH A O 1 HETATM 4514 O O . HOH R 7 . ? -44.016 4.841 19.586 1.00 60.21 ? 2370 HOH A O 1 HETATM 4515 O O . HOH R 7 . ? -43.662 4.469 22.284 1.00 62.99 ? 2371 HOH A O 1 HETATM 4516 O O . HOH R 7 . ? -46.453 6.833 3.645 1.00 28.11 ? 2372 HOH A O 1 HETATM 4517 O O . HOH R 7 . ? -53.418 1.114 6.342 1.00 53.22 ? 2373 HOH A O 1 HETATM 4518 O O . HOH R 7 . ? -47.626 2.549 -2.513 1.00 27.07 ? 2374 HOH A O 1 HETATM 4519 O O . HOH R 7 . ? -46.206 -0.793 -2.952 1.00 39.81 ? 2375 HOH A O 1 HETATM 4520 O O . HOH R 7 . ? -40.218 3.269 -5.962 1.00 40.09 ? 2376 HOH A O 1 HETATM 4521 O O . HOH R 7 . ? -48.078 -0.562 1.081 1.00 53.41 ? 2377 HOH A O 1 HETATM 4522 O O . HOH R 7 . ? -41.710 8.293 7.531 1.00 37.23 ? 2378 HOH A O 1 HETATM 4523 O O . HOH R 7 . ? -39.210 8.880 10.212 1.00 37.02 ? 2379 HOH A O 1 HETATM 4524 O O . HOH R 7 . ? -40.395 10.651 8.091 1.00 43.42 ? 2380 HOH A O 1 HETATM 4525 O O . HOH R 7 . ? -38.314 11.974 11.138 1.00 35.25 ? 2381 HOH A O 1 HETATM 4526 O O . HOH R 7 . ? -35.716 10.832 16.495 1.00 53.12 ? 2382 HOH A O 1 HETATM 4527 O O . HOH R 7 . ? -37.334 14.767 17.538 1.00 39.60 ? 2383 HOH A O 1 HETATM 4528 O O . HOH R 7 . ? -42.212 3.629 34.516 1.00 53.60 ? 2384 HOH A O 1 HETATM 4529 O O . HOH R 7 . ? -37.978 10.302 26.122 1.00 48.05 ? 2385 HOH A O 1 HETATM 4530 O O . HOH R 7 . ? -44.510 20.347 20.197 1.00 29.49 ? 2386 HOH A O 1 HETATM 4531 O O . HOH R 7 . ? -44.558 9.148 27.068 1.00 50.98 ? 2387 HOH A O 1 HETATM 4532 O O . HOH R 7 . ? -40.747 6.860 26.742 1.00 50.96 ? 2388 HOH A O 1 HETATM 4533 O O . HOH R 7 . ? -41.298 19.795 31.736 1.00 57.87 ? 2389 HOH A O 1 HETATM 4534 O O . HOH R 7 . ? -36.410 12.806 36.316 1.00 55.36 ? 2390 HOH A O 1 HETATM 4535 O O . HOH R 7 . ? -42.530 17.475 41.967 1.00 36.66 ? 2391 HOH A O 1 HETATM 4536 O O . HOH R 7 . ? -38.970 18.126 40.084 1.00 44.79 ? 2392 HOH A O 1 HETATM 4537 O O . HOH R 7 . ? -43.461 21.187 32.961 1.00 51.84 ? 2393 HOH A O 1 HETATM 4538 O O . HOH R 7 . ? -42.019 24.190 36.963 1.00 55.23 ? 2394 HOH A O 1 HETATM 4539 O O . HOH R 7 . ? -36.242 12.354 44.762 1.00 45.43 ? 2395 HOH A O 1 HETATM 4540 O O . HOH R 7 . ? -43.037 15.643 44.086 1.00 28.02 ? 2396 HOH A O 1 HETATM 4541 O O . HOH R 7 . ? -36.151 16.792 50.856 1.00 40.56 ? 2397 HOH A O 1 HETATM 4542 O O . HOH R 7 . ? -39.111 19.633 52.682 1.00 37.72 ? 2398 HOH A O 1 HETATM 4543 O O . HOH R 7 . ? -34.353 10.943 56.464 1.00 35.82 ? 2399 HOH A O 1 HETATM 4544 O O . HOH R 7 . ? -39.907 19.087 58.868 1.00 27.36 ? 2400 HOH A O 1 HETATM 4545 O O . HOH R 7 . ? -38.133 17.874 62.628 1.00 23.78 ? 2401 HOH A O 1 HETATM 4546 O O . HOH R 7 . ? -42.306 20.664 65.106 1.00 33.38 ? 2402 HOH A O 1 HETATM 4547 O O . HOH R 7 . ? -39.447 19.798 61.745 1.00 28.88 ? 2403 HOH A O 1 HETATM 4548 O O . HOH R 7 . ? -45.868 18.736 54.484 1.00 25.94 ? 2404 HOH A O 1 HETATM 4549 O O . HOH R 7 . ? -42.197 20.701 58.770 1.00 33.25 ? 2405 HOH A O 1 HETATM 4550 O O . HOH R 7 . ? -48.548 15.452 62.381 1.00 25.79 ? 2406 HOH A O 1 HETATM 4551 O O . HOH R 7 . ? -48.526 20.231 67.818 1.00 17.61 ? 2407 HOH A O 1 HETATM 4552 O O . HOH R 7 . ? -53.611 20.475 62.929 1.00 15.94 ? 2408 HOH A O 1 HETATM 4553 O O . HOH R 7 . ? -48.443 13.341 63.970 1.00 26.87 ? 2409 HOH A O 1 HETATM 4554 O O . HOH R 7 . ? -51.436 14.345 64.917 1.00 20.06 ? 2410 HOH A O 1 HETATM 4555 O O . HOH R 7 . ? -58.187 17.557 63.593 1.00 32.37 ? 2411 HOH A O 1 HETATM 4556 O O . HOH R 7 . ? -54.365 10.548 65.172 1.00 36.68 ? 2412 HOH A O 1 HETATM 4557 O O . HOH R 7 . ? -59.287 15.682 65.799 1.00 25.52 ? 2413 HOH A O 1 HETATM 4558 O O . HOH R 7 . ? -58.145 11.526 68.236 1.00 52.64 ? 2414 HOH A O 1 HETATM 4559 O O . HOH R 7 . ? -61.479 11.423 72.008 1.00 50.29 ? 2415 HOH A O 1 HETATM 4560 O O . HOH R 7 . ? -61.688 16.096 70.810 1.00 45.35 ? 2416 HOH A O 1 HETATM 4561 O O . HOH R 7 . ? -63.101 14.721 73.032 1.00 48.22 ? 2417 HOH A O 1 HETATM 4562 O O . HOH R 7 . ? -61.734 13.879 75.761 1.00 52.21 ? 2418 HOH A O 1 HETATM 4563 O O . HOH R 7 . ? -56.006 16.376 72.674 1.00 32.00 ? 2419 HOH A O 1 HETATM 4564 O O . HOH R 7 . ? -61.364 18.355 69.780 1.00 29.70 ? 2420 HOH A O 1 HETATM 4565 O O . HOH R 7 . ? -62.706 16.586 75.794 1.00 32.95 ? 2421 HOH A O 1 HETATM 4566 O O . HOH R 7 . ? -60.955 18.591 77.871 1.00 42.49 ? 2422 HOH A O 1 HETATM 4567 O O . HOH R 7 . ? -58.172 19.413 77.672 1.00 53.02 ? 2423 HOH A O 1 HETATM 4568 O O . HOH R 7 . ? -61.031 22.411 70.988 1.00 20.88 ? 2424 HOH A O 1 HETATM 4569 O O . HOH R 7 . ? -56.259 26.615 74.016 1.00 25.01 ? 2425 HOH A O 1 HETATM 4570 O O . HOH R 7 . ? -58.258 24.779 77.111 1.00 41.94 ? 2426 HOH A O 1 HETATM 4571 O O . HOH R 7 . ? -53.727 18.169 72.687 1.00 23.31 ? 2427 HOH A O 1 HETATM 4572 O O . HOH R 7 . ? -60.373 23.143 68.283 1.00 23.58 ? 2428 HOH A O 1 HETATM 4573 O O . HOH R 7 . ? -60.175 26.092 63.470 1.00 18.45 ? 2429 HOH A O 1 HETATM 4574 O O . HOH R 7 . ? -63.364 25.292 69.485 1.00 22.03 ? 2430 HOH A O 1 HETATM 4575 O O . HOH R 7 . ? -61.369 30.195 67.737 1.00 23.56 ? 2431 HOH A O 1 HETATM 4576 O O . HOH R 7 . ? -50.603 19.904 69.526 1.00 21.92 ? 2432 HOH A O 1 HETATM 4577 O O . HOH R 7 . ? -48.511 22.843 67.731 1.00 16.62 ? 2433 HOH A O 1 HETATM 4578 O O . HOH R 7 . ? -61.081 17.214 67.223 1.00 32.33 ? 2434 HOH A O 1 HETATM 4579 O O . HOH R 7 . ? -62.200 21.791 66.798 1.00 36.57 ? 2435 HOH A O 1 HETATM 4580 O O . HOH R 7 . ? -51.395 27.767 56.980 1.00 27.87 ? 2436 HOH A O 1 HETATM 4581 O O . HOH R 7 . ? -50.786 19.124 54.799 1.00 18.32 ? 2437 HOH A O 1 HETATM 4582 O O . HOH R 7 . ? -59.051 21.588 53.971 1.00 33.90 ? 2438 HOH A O 1 HETATM 4583 O O . HOH R 7 . ? -62.108 22.342 57.618 1.00 52.34 ? 2439 HOH A O 1 HETATM 4584 O O . HOH R 7 . ? -60.149 26.452 57.476 1.00 32.40 ? 2440 HOH A O 1 HETATM 4585 O O . HOH R 7 . ? -58.569 27.897 56.106 1.00 16.58 ? 2441 HOH A O 1 HETATM 4586 O O . HOH R 7 . ? -56.387 28.186 52.408 1.00 11.14 ? 2442 HOH A O 1 HETATM 4587 O O . HOH R 7 . ? -58.884 27.513 53.448 1.00 15.01 ? 2443 HOH A O 1 HETATM 4588 O O . HOH R 7 . ? -52.110 27.966 46.476 1.00 13.91 ? 2444 HOH A O 1 HETATM 4589 O O . HOH R 7 . ? -53.947 30.945 40.314 1.00 13.28 ? 2445 HOH A O 1 HETATM 4590 O O . HOH R 7 . ? -50.825 27.551 41.777 1.00 15.05 ? 2446 HOH A O 1 HETATM 4591 O O . HOH R 7 . ? -57.196 19.872 37.173 1.00 24.49 ? 2447 HOH A O 1 HETATM 4592 O O . HOH R 7 . ? -60.707 17.729 41.174 1.00 38.04 ? 2448 HOH A O 1 HETATM 4593 O O . HOH R 7 . ? -59.907 17.379 38.369 1.00 37.24 ? 2449 HOH A O 1 HETATM 4594 O O . HOH R 7 . ? -50.922 25.389 29.648 1.00 24.49 ? 2450 HOH A O 1 HETATM 4595 O O . HOH R 7 . ? -57.291 22.369 23.595 1.00 39.89 ? 2451 HOH A O 1 HETATM 4596 O O . HOH R 7 . ? -50.181 25.395 27.084 1.00 30.66 ? 2452 HOH A O 1 HETATM 4597 O O . HOH R 7 . ? -50.495 23.728 19.481 1.00 37.07 ? 2453 HOH A O 1 HETATM 4598 O O . HOH R 7 . ? -49.347 26.759 23.357 1.00 46.93 ? 2454 HOH A O 1 HETATM 4599 O O . HOH R 7 . ? -43.314 17.738 14.058 1.00 30.58 ? 2455 HOH A O 1 HETATM 4600 O O . HOH R 7 . ? -40.267 18.187 15.905 1.00 37.63 ? 2456 HOH A O 1 HETATM 4601 O O . HOH R 7 . ? -50.183 24.356 16.560 1.00 43.55 ? 2457 HOH A O 1 HETATM 4602 O O . HOH R 7 . ? -43.075 23.057 10.364 1.00 38.33 ? 2458 HOH A O 1 HETATM 4603 O O . HOH R 7 . ? -51.348 25.273 5.943 1.00 39.70 ? 2459 HOH A O 1 HETATM 4604 O O . HOH R 7 . ? -40.094 22.131 4.552 1.00 37.30 ? 2460 HOH A O 1 HETATM 4605 O O . HOH R 7 . ? -42.278 16.277 5.439 1.00 41.61 ? 2461 HOH A O 1 HETATM 4606 O O . HOH R 7 . ? -46.917 23.080 -1.245 1.00 37.08 ? 2462 HOH A O 1 HETATM 4607 O O . HOH R 7 . ? -49.671 22.632 -0.986 1.00 44.29 ? 2463 HOH A O 1 HETATM 4608 O O . HOH R 7 . ? -52.095 24.674 2.936 1.00 45.45 ? 2464 HOH A O 1 HETATM 4609 O O . HOH R 7 . ? -40.076 25.340 0.191 1.00 41.78 ? 2465 HOH A O 1 HETATM 4610 O O . HOH R 7 . ? -38.802 22.031 -1.776 1.00 39.78 ? 2466 HOH A O 1 HETATM 4611 O O . HOH R 7 . ? -37.136 18.191 0.367 1.00 43.13 ? 2467 HOH A O 1 HETATM 4612 O O . HOH R 7 . ? -38.219 24.839 -1.751 1.00 31.42 ? 2468 HOH A O 1 HETATM 4613 O O . HOH R 7 . ? -35.908 28.420 -4.928 1.00 36.68 ? 2469 HOH A O 1 HETATM 4614 O O . HOH R 7 . ? -42.619 23.468 -7.388 1.00 27.31 ? 2470 HOH A O 1 HETATM 4615 O O . HOH R 7 . ? -49.795 27.629 -5.955 1.00 44.99 ? 2471 HOH A O 1 HETATM 4616 O O . HOH R 7 . ? -53.190 24.359 -1.673 1.00 38.85 ? 2472 HOH A O 1 HETATM 4617 O O . HOH R 7 . ? -56.372 24.500 -0.346 1.00 47.20 ? 2473 HOH A O 1 HETATM 4618 O O . HOH R 7 . ? -55.759 20.068 5.240 1.00 27.12 ? 2474 HOH A O 1 HETATM 4619 O O . HOH R 7 . ? -60.249 22.271 6.365 1.00 40.61 ? 2475 HOH A O 1 HETATM 4620 O O . HOH R 7 . ? -55.550 16.193 -11.731 1.00 53.50 ? 2476 HOH A O 1 HETATM 4621 O O . HOH R 7 . ? -57.467 19.664 -9.907 1.00 47.71 ? 2477 HOH A O 1 HETATM 4622 O O . HOH R 7 . ? -42.363 9.025 -9.203 1.00 28.04 ? 2478 HOH A O 1 HETATM 4623 O O . HOH R 7 . ? -43.074 11.677 -12.055 1.00 28.17 ? 2479 HOH A O 1 HETATM 4624 O O . HOH R 7 . ? -38.678 7.891 -7.596 1.00 32.12 ? 2480 HOH A O 1 HETATM 4625 O O . HOH R 7 . ? -43.451 2.266 0.213 1.00 44.85 ? 2481 HOH A O 1 HETATM 4626 O O . HOH R 7 . ? -37.374 9.392 -5.686 1.00 40.38 ? 2482 HOH A O 1 HETATM 4627 O O . HOH R 7 . ? -38.074 12.113 -5.390 1.00 40.39 ? 2483 HOH A O 1 HETATM 4628 O O . HOH R 7 . ? -40.412 14.814 6.241 1.00 47.92 ? 2484 HOH A O 1 HETATM 4629 O O . HOH R 7 . ? -40.195 6.525 6.179 1.00 49.79 ? 2485 HOH A O 1 HETATM 4630 O O . HOH R 7 . ? -31.974 9.320 2.169 1.00 64.17 ? 2486 HOH A O 1 HETATM 4631 O O . HOH R 7 . ? -37.176 20.441 -3.082 1.00 34.20 ? 2487 HOH A O 1 HETATM 4632 O O . HOH R 7 . ? -36.379 14.309 -5.409 1.00 38.26 ? 2488 HOH A O 1 HETATM 4633 O O . HOH R 7 . ? -39.415 19.898 -13.891 1.00 38.08 ? 2489 HOH A O 1 HETATM 4634 O O . HOH R 7 . ? -38.140 23.062 -12.671 1.00 60.19 ? 2490 HOH A O 1 HETATM 4635 O O . HOH R 7 . ? -41.591 14.926 -13.842 1.00 35.16 ? 2491 HOH A O 1 HETATM 4636 O O . HOH R 7 . ? -41.187 17.675 -14.551 1.00 32.25 ? 2492 HOH A O 1 HETATM 4637 O O . HOH R 7 . ? -36.805 16.189 -14.253 1.00 54.76 ? 2493 HOH A O 1 HETATM 4638 O O . HOH R 7 . ? -39.650 9.706 -9.330 1.00 37.68 ? 2494 HOH A O 1 HETATM 4639 O O . HOH R 7 . ? -47.907 16.789 -16.895 1.00 35.26 ? 2495 HOH A O 1 HETATM 4640 O O . HOH R 7 . ? -45.109 11.045 -15.289 1.00 48.49 ? 2496 HOH A O 1 HETATM 4641 O O . HOH R 7 . ? -56.224 20.052 -12.582 1.00 46.35 ? 2497 HOH A O 1 HETATM 4642 O O . HOH R 7 . ? -57.155 22.668 -13.555 1.00 41.68 ? 2498 HOH A O 1 HETATM 4643 O O . HOH R 7 . ? -51.363 24.862 -19.064 1.00 57.26 ? 2499 HOH A O 1 HETATM 4644 O O . HOH R 7 . ? -45.580 5.431 34.941 1.00 44.98 ? 2500 HOH A O 1 HETATM 4645 O O . HOH R 7 . ? -30.039 -3.216 95.179 1.00 53.73 ? 2501 HOH A O 1 HETATM 4646 O O . HOH R 7 . ? -26.826 31.754 98.266 1.00 36.06 ? 2502 HOH A O 1 HETATM 4647 O O . HOH R 7 . ? -24.851 28.257 101.745 1.00 50.66 ? 2503 HOH A O 1 HETATM 4648 O O . HOH R 7 . ? -21.850 26.787 95.101 1.00 49.23 ? 2504 HOH A O 1 HETATM 4649 O O . HOH R 7 . ? -22.199 30.746 92.672 1.00 41.00 ? 2505 HOH A O 1 HETATM 4650 O O . HOH R 7 . ? -34.607 30.587 104.488 1.00 53.78 ? 2506 HOH A O 1 HETATM 4651 O O . HOH R 7 . ? -58.828 3.241 56.925 1.00 51.27 ? 2507 HOH A O 1 HETATM 4652 O O . HOH R 7 . ? -45.512 19.401 45.090 1.00 60.63 ? 2508 HOH A O 1 HETATM 4653 O O . HOH R 7 . ? -40.118 24.620 45.124 1.00 54.92 ? 2509 HOH A O 1 HETATM 4654 O O . HOH R 7 . ? -50.498 29.118 101.610 0.33 44.70 ? 2510 HOH A O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . ASN A 8 ? 0.9739 0.7989 0.7945 -0.0566 -0.0692 -0.0388 8 ASN A N 2 C CA . ASN A 8 ? 0.9656 0.7777 0.7794 -0.0525 -0.0667 -0.0424 8 ASN A CA 3 C C . ASN A 8 ? 0.9065 0.7223 0.7239 -0.0460 -0.0623 -0.0432 8 ASN A C 4 O O . ASN A 8 ? 0.9235 0.7490 0.7450 -0.0452 -0.0619 -0.0415 8 ASN A O 5 C CB . ASN A 8 ? 1.0183 0.8200 0.8204 -0.0559 -0.0697 -0.0443 8 ASN A CB 6 C CG . ASN A 8 ? 1.0597 0.8464 0.8534 -0.0526 -0.0679 -0.0477 8 ASN A CG 7 O OD1 . ASN A 8 ? 1.0705 0.8505 0.8632 -0.0523 -0.0675 -0.0484 8 ASN A OD1 8 N ND2 . ASN A 8 ? 1.0863 0.8678 0.8738 -0.0499 -0.0668 -0.0499 8 ASN A ND2 9 N N . SER A 9 ? 0.8267 0.6348 0.6421 -0.0414 -0.0590 -0.0456 9 SER A N 10 C CA . SER A 9 ? 0.7497 0.5611 0.5689 -0.0355 -0.0545 -0.0463 9 SER A CA 11 C C . SER A 9 ? 0.6649 0.4859 0.4946 -0.0335 -0.0520 -0.0443 9 SER A C 12 O O . SER A 9 ? 0.6126 0.4376 0.4460 -0.0294 -0.0485 -0.0443 9 SER A O 13 C CB . SER A 9 ? 0.7687 0.5837 0.5857 -0.0348 -0.0544 -0.0462 9 SER A CB 14 O OG . SER A 9 ? 0.7620 0.5887 0.5852 -0.0364 -0.0555 -0.0432 9 SER A OG 15 N N . THR A 10 ? 0.6097 0.4338 0.4436 -0.0365 -0.0540 -0.0425 10 THR A N 16 C CA . THR A 10 ? 0.5658 0.3984 0.4091 -0.0350 -0.0521 -0.0406 10 THR A CA 17 C C . THR A 10 ? 0.5303 0.3596 0.3751 -0.0368 -0.0531 -0.0403 10 THR A C 18 O O . THR A 10 ? 0.5333 0.3541 0.3717 -0.0396 -0.0556 -0.0414 10 THR A O 19 C CB . THR A 10 ? 0.5720 0.4161 0.4205 -0.0369 -0.0535 -0.0374 10 THR A CB 20 O OG1 . THR A 10 ? 0.5950 0.4400 0.4416 -0.0425 -0.0579 -0.0361 10 THR A OG1 21 C CG2 . THR A 10 ? 0.5969 0.4443 0.4437 -0.0349 -0.0525 -0.0374 10 THR A CG2 22 N N . ALA A 11 ? 0.4779 0.3133 0.3305 -0.0350 -0.0511 -0.0390 11 ALA A N 23 C CA . ALA A 11 ? 0.4613 0.2952 0.3165 -0.0365 -0.0519 -0.0384 11 ALA A CA 24 C C . ALA A 11 ? 0.4352 0.2804 0.2994 -0.0369 -0.0516 -0.0354 11 ALA A C 25 O O . ALA A 11 ? 0.4259 0.2785 0.2938 -0.0350 -0.0500 -0.0343 11 ALA A O 26 C CB . ALA A 11 ? 0.4592 0.2869 0.3138 -0.0323 -0.0488 -0.0405 11 ALA A CB 27 N N . THR A 12 ? 0.4207 0.2665 0.2876 -0.0395 -0.0532 -0.0342 12 THR A N 28 C CA . THR A 12 ? 0.4115 0.2672 0.2868 -0.0396 -0.0528 -0.0314 12 THR A CA 29 C C . THR A 12 ? 0.3952 0.2486 0.2740 -0.0375 -0.0508 -0.0319 12 THR A C 30 O O . THR A 12 ? 0.4048 0.2499 0.2796 -0.0384 -0.0517 -0.0333 12 THR A O 31 C CB . THR A 12 ? 0.4167 0.2772 0.2928 -0.0451 -0.0567 -0.0288 12 THR A CB 32 O OG1 . THR A 12 ? 0.4300 0.2927 0.3023 -0.0474 -0.0589 -0.0284 12 THR A OG1 33 C CG2 . THR A 12 ? 0.4153 0.2872 0.3000 -0.0446 -0.0561 -0.0258 12 THR A CG2 34 N N . LEU A 13 ? 0.3861 0.2465 0.2717 -0.0346 -0.0481 -0.0309 13 LEU A N 35 C CA . LEU A 13 ? 0.3748 0.2348 0.2645 -0.0327 -0.0463 -0.0310 13 LEU A CA 36 C C . LEU A 13 ? 0.3760 0.2455 0.2730 -0.0334 -0.0463 -0.0281 13 LEU A C 37 O O . LEU A 13 ? 0.3660 0.2421 0.2664 -0.0314 -0.0446 -0.0270 13 LEU A O 38 C CB . LEU A 13 ? 0.3701 0.2284 0.2602 -0.0281 -0.0424 -0.0329 13 LEU A CB 39 C CG . LEU A 13 ? 0.3686 0.2271 0.2629 -0.0259 -0.0403 -0.0332 13 LEU A CG 40 C CD1 . LEU A 13 ? 0.3755 0.2261 0.2662 -0.0266 -0.0417 -0.0343 13 LEU A CD1 41 C CD2 . LEU A 13 ? 0.3746 0.2339 0.2699 -0.0218 -0.0364 -0.0347 13 LEU A CD2 42 N N . CYS A 14 ? 0.3871 0.2567 0.2860 -0.0360 -0.0482 -0.0268 14 CYS A N 43 C CA . CYS A 14 ? 0.3928 0.2712 0.2983 -0.0368 -0.0485 -0.0239 14 CYS A CA 44 C C . CYS A 14 ? 0.3851 0.2631 0.2949 -0.0345 -0.0463 -0.0242 14 CYS A C 45 O O . CYS A 14 ? 0.3754 0.2461 0.2827 -0.0339 -0.0460 -0.0259 14 CYS A O 46 C CB . CYS A 14 ? 0.4208 0.3008 0.3256 -0.0421 -0.0524 -0.0219 14 CYS A CB 47 S SG . CYS A 14 ? 0.4533 0.3359 0.3537 -0.0457 -0.0555 -0.0211 14 CYS A SG 48 N N . LEU A 15 ? 0.3623 0.2481 0.2779 -0.0328 -0.0447 -0.0224 15 LEU A N 49 C CA . LEU A 15 ? 0.3626 0.2494 0.2827 -0.0310 -0.0429 -0.0222 15 LEU A CA 50 C C . LEU A 15 ? 0.3491 0.2411 0.2730 -0.0337 -0.0449 -0.0194 15 LEU A C 51 O O . LEU A 15 ? 0.3557 0.2543 0.2810 -0.0352 -0.0463 -0.0172 15 LEU A O 52 C CB . LEU A 15 ? 0.3656 0.2568 0.2888 -0.0274 -0.0396 -0.0221 15 LEU A CB 53 C CG . LEU A 15 ? 0.3829 0.2697 0.3034 -0.0246 -0.0368 -0.0247 15 LEU A CG 54 C CD1 . LEU A 15 ? 0.4050 0.2873 0.3257 -0.0236 -0.0359 -0.0264 15 LEU A CD1 55 C CD2 . LEU A 15 ? 0.4132 0.2960 0.3280 -0.0251 -0.0377 -0.0261 15 LEU A CD2 56 N N . GLY A 16 ? 0.3427 0.2320 0.2681 -0.0341 -0.0451 -0.0195 16 GLY A N 57 C CA . GLY A 16 ? 0.3385 0.2322 0.2671 -0.0370 -0.0472 -0.0169 16 GLY A CA 58 C C . GLY A 16 ? 0.3337 0.2266 0.2657 -0.0358 -0.0460 -0.0168 16 GLY A C 59 O O . GLY A 16 ? 0.3199 0.2090 0.2518 -0.0327 -0.0438 -0.0187 16 GLY A O 60 N N . HIS A 17 ? 0.3321 0.2292 0.2670 -0.0383 -0.0478 -0.0143 17 HIS A N 61 C CA . HIS A 17 ? 0.3297 0.2264 0.2679 -0.0376 -0.0471 -0.0138 17 HIS A CA 62 C C . HIS A 17 ? 0.3352 0.2303 0.2721 -0.0421 -0.0502 -0.0121 17 HIS A C 63 O O . HIS A 17 ? 0.3496 0.2472 0.2849 -0.0459 -0.0527 -0.0107 17 HIS A O 64 C CB . HIS A 17 ? 0.3221 0.2274 0.2664 -0.0352 -0.0451 -0.0120 17 HIS A CB 65 C CG . HIS A 17 ? 0.3228 0.2371 0.2698 -0.0370 -0.0464 -0.0089 17 HIS A CG 66 N ND1 . HIS A 17 ? 0.3234 0.2411 0.2720 -0.0404 -0.0488 -0.0064 17 HIS A ND1 67 C CD2 . HIS A 17 ? 0.3255 0.2463 0.2735 -0.0355 -0.0457 -0.0077 17 HIS A CD2 68 C CE1 . HIS A 17 ? 0.3264 0.2534 0.2773 -0.0411 -0.0495 -0.0038 17 HIS A CE1 69 N NE2 . HIS A 17 ? 0.3345 0.2632 0.2849 -0.0377 -0.0476 -0.0045 17 HIS A NE2 70 N N . HIS A 18 ? 0.3429 0.2342 0.2804 -0.0418 -0.0500 -0.0123 18 HIS A N 71 C CA . HIS A 18 ? 0.3549 0.2432 0.2903 -0.0462 -0.0528 -0.0108 18 HIS A CA 72 C C . HIS A 18 ? 0.3675 0.2657 0.3079 -0.0489 -0.0541 -0.0073 18 HIS A C 73 O O . HIS A 18 ? 0.3472 0.2546 0.2930 -0.0467 -0.0525 -0.0059 18 HIS A O 74 C CB . HIS A 18 ? 0.3692 0.2496 0.3030 -0.0445 -0.0521 -0.0121 18 HIS A CB 75 C CG . HIS A 18 ? 0.3633 0.2496 0.3037 -0.0418 -0.0502 -0.0109 18 HIS A CG 76 N ND1 . HIS A 18 ? 0.3845 0.2663 0.3245 -0.0413 -0.0501 -0.0108 18 HIS A ND1 77 C CD2 . HIS A 18 ? 0.3606 0.2566 0.3075 -0.0395 -0.0482 -0.0097 18 HIS A CD2 78 C CE1 . HIS A 18 ? 0.3709 0.2598 0.3173 -0.0389 -0.0483 -0.0097 18 HIS A CE1 79 N NE2 . HIS A 18 ? 0.3576 0.2548 0.3079 -0.0379 -0.0471 -0.0090 18 HIS A NE2 80 N N . ALA A 19 ? 0.3711 0.2671 0.3091 -0.0540 -0.0569 -0.0058 19 ALA A N 81 C CA . ALA A 19 ? 0.3839 0.2890 0.3261 -0.0573 -0.0584 -0.0022 19 ALA A CA 82 C C . ALA A 19 ? 0.4093 0.3069 0.3478 -0.0612 -0.0605 -0.0017 19 ALA A C 83 O O . ALA A 19 ? 0.4357 0.3214 0.3672 -0.0621 -0.0613 -0.0039 19 ALA A O 84 C CB . ALA A 19 ? 0.3848 0.2978 0.3270 -0.0609 -0.0606 -0.0001 19 ALA A CB 85 N N . VAL A 20 ? 0.4173 0.3214 0.3600 -0.0632 -0.0612 0.0011 20 VAL A N 86 C CA . VAL A 20 ? 0.4280 0.3251 0.3672 -0.0669 -0.0630 0.0019 20 VAL A CA 87 C C . VAL A 20 ? 0.4576 0.3626 0.3980 -0.0734 -0.0658 0.0056 20 VAL A C 88 O O . VAL A 20 ? 0.4389 0.3570 0.3849 -0.0734 -0.0657 0.0079 20 VAL A O 89 C CB . VAL A 20 ? 0.4362 0.3323 0.3790 -0.0629 -0.0608 0.0018 20 VAL A CB 90 C CG1 . VAL A 20 ? 0.4285 0.3174 0.3699 -0.0569 -0.0581 -0.0016 20 VAL A CG1 91 C CG2 . VAL A 20 ? 0.4083 0.3179 0.3596 -0.0612 -0.0594 0.0045 20 VAL A CG2 92 N N . PRO A 21 ? 0.5063 0.4033 0.4405 -0.0791 -0.0685 0.0062 21 PRO A N 93 C CA . PRO A 21 ? 0.5322 0.4371 0.4672 -0.0862 -0.0714 0.0098 21 PRO A CA 94 C C . PRO A 21 ? 0.5459 0.4612 0.4882 -0.0857 -0.0706 0.0131 21 PRO A C 95 O O . PRO A 21 ? 0.6008 0.5279 0.5465 -0.0898 -0.0722 0.0165 21 PRO A O 96 C CB . PRO A 21 ? 0.5367 0.4275 0.4616 -0.0923 -0.0743 0.0091 21 PRO A CB 97 C CG . PRO A 21 ? 0.5382 0.4149 0.4590 -0.0873 -0.0723 0.0060 21 PRO A CG 98 C CD . PRO A 21 ? 0.5253 0.4055 0.4509 -0.0795 -0.0690 0.0036 21 PRO A CD 99 N N . ASN A 22 ? 0.5413 0.4528 0.4859 -0.0807 -0.0682 0.0120 22 ASN A N 100 C CA . ASN A 22 ? 0.5523 0.4713 0.5028 -0.0803 -0.0675 0.0148 22 ASN A CA 101 C C . ASN A 22 ? 0.5026 0.4288 0.4605 -0.0727 -0.0639 0.0143 22 ASN A C 102 O O . ASN A 22 ? 0.4968 0.4186 0.4558 -0.0691 -0.0621 0.0133 22 ASN A O 103 C CB . ASN A 22 ? 0.5804 0.4875 0.5260 -0.0819 -0.0681 0.0143 22 ASN A CB 104 C CG . ASN A 22 ? 0.6384 0.5331 0.5805 -0.0762 -0.0660 0.0104 22 ASN A CG 105 O OD1 . ASN A 22 ? 0.6739 0.5648 0.6138 -0.0734 -0.0652 0.0076 22 ASN A OD1 106 N ND2 . ASN A 22 ? 0.6547 0.5439 0.5965 -0.0741 -0.0650 0.0102 22 ASN A ND2 107 N N . GLY A 23 ? 0.4724 0.4094 0.4347 -0.0705 -0.0630 0.0152 23 GLY A N 108 C CA . GLY A 23 ? 0.4587 0.4013 0.4266 -0.0636 -0.0596 0.0146 23 GLY A CA 109 C C . GLY A 23 ? 0.4353 0.3870 0.4090 -0.0625 -0.0587 0.0176 23 GLY A C 110 O O . GLY A 23 ? 0.4273 0.3826 0.4013 -0.0673 -0.0607 0.0205 23 GLY A O 111 N N . THR A 24 ? 0.4004 0.3555 0.3781 -0.0566 -0.0558 0.0171 24 THR A N 112 C CA . THR A 24 ? 0.3875 0.3507 0.3703 -0.0549 -0.0547 0.0198 24 THR A CA 113 C C . THR A 24 ? 0.3556 0.3287 0.3423 -0.0502 -0.0525 0.0209 24 THR A C 114 O O . THR A 24 ? 0.3458 0.3162 0.3315 -0.0464 -0.0508 0.0185 24 THR A O 115 C CB . THR A 24 ? 0.4201 0.3766 0.4035 -0.0519 -0.0530 0.0182 24 THR A CB 116 O OG1 . THR A 24 ? 0.4677 0.4123 0.4463 -0.0541 -0.0542 0.0160 24 THR A OG1 117 C CG2 . THR A 24 ? 0.4243 0.3875 0.4115 -0.0525 -0.0530 0.0214 24 THR A CG2 118 N N . ILE A 25 ? 0.3119 0.2955 0.3024 -0.0501 -0.0525 0.0244 25 ILE A N 119 C CA . ILE A 25 ? 0.3056 0.2987 0.2988 -0.0454 -0.0505 0.0259 25 ILE A CA 120 C C . ILE A 25 ? 0.2792 0.2698 0.2740 -0.0399 -0.0475 0.0248 25 ILE A C 121 O O . ILE A 25 ? 0.2590 0.2482 0.2554 -0.0403 -0.0474 0.0253 25 ILE A O 122 C CB . ILE A 25 ? 0.3214 0.3281 0.3177 -0.0473 -0.0517 0.0306 25 ILE A CB 123 C CG1 . ILE A 25 ? 0.3517 0.3617 0.3463 -0.0534 -0.0548 0.0319 25 ILE A CG1 124 C CG2 . ILE A 25 ? 0.3182 0.3341 0.3165 -0.0414 -0.0494 0.0322 25 ILE A CG2 125 C CD1 . ILE A 25 ? 0.3640 0.3722 0.3559 -0.0523 -0.0549 0.0299 25 ILE A CD1 126 N N . VAL A 26 ? 0.2625 0.2522 0.2563 -0.0352 -0.0453 0.0231 26 VAL A N 127 C CA . VAL A 26 ? 0.2538 0.2419 0.2483 -0.0301 -0.0424 0.0223 26 VAL A CA 128 C C . VAL A 26 ? 0.2554 0.2505 0.2498 -0.0256 -0.0406 0.0238 26 VAL A C 129 O O . VAL A 26 ? 0.2602 0.2610 0.2539 -0.0259 -0.0414 0.0252 26 VAL A O 130 C CB . VAL A 26 ? 0.2448 0.2222 0.2370 -0.0285 -0.0410 0.0181 26 VAL A CB 131 C CG1 . VAL A 26 ? 0.2494 0.2195 0.2411 -0.0319 -0.0425 0.0165 26 VAL A CG1 132 C CG2 . VAL A 26 ? 0.2377 0.2128 0.2269 -0.0273 -0.0405 0.0162 26 VAL A CG2 133 N N . LYS A 27 ? 0.2674 0.2615 0.2618 -0.0214 -0.0382 0.0236 27 LYS A N 134 C CA . LYS A 27 ? 0.2784 0.2767 0.2711 -0.0163 -0.0361 0.0248 27 LYS A CA 135 C C . LYS A 27 ? 0.2753 0.2650 0.2641 -0.0132 -0.0338 0.0214 27 LYS A C 136 O O . LYS A 27 ? 0.2563 0.2387 0.2448 -0.0134 -0.0330 0.0189 27 LYS A O 137 C CB . LYS A 27 ? 0.3015 0.3051 0.2960 -0.0137 -0.0350 0.0274 27 LYS A CB 138 C CG . LYS A 27 ? 0.3352 0.3414 0.3268 -0.0078 -0.0325 0.0286 27 LYS A CG 139 C CD . LYS A 27 ? 0.3603 0.3720 0.3535 -0.0055 -0.0316 0.0313 27 LYS A CD 140 C CE . LYS A 27 ? 0.3865 0.3962 0.3751 0.0007 -0.0286 0.0314 27 LYS A CE 141 N NZ . LYS A 27 ? 0.3979 0.4135 0.3876 0.0034 -0.0277 0.0344 27 LYS A NZ 142 N N . THR A 28 ? 0.2834 0.2742 0.2690 -0.0103 -0.0328 0.0216 28 THR A N 143 C CA . THR A 28 ? 0.3007 0.2835 0.2818 -0.0074 -0.0305 0.0188 28 THR A CA 144 C C . THR A 28 ? 0.3230 0.3086 0.3006 -0.0020 -0.0283 0.0207 28 THR A C 145 O O . THR A 28 ? 0.3310 0.3250 0.3101 -0.0003 -0.0286 0.0240 28 THR A O 146 C CB . THR A 28 ? 0.3031 0.2819 0.2819 -0.0089 -0.0311 0.0166 28 THR A CB 147 O OG1 . THR A 28 ? 0.3027 0.2884 0.2806 -0.0076 -0.0317 0.0188 28 THR A OG1 148 C CG2 . THR A 28 ? 0.3145 0.2905 0.2958 -0.0139 -0.0334 0.0150 28 THR A CG2 149 N N . ILE A 29 ? 0.3394 0.3178 0.3118 0.0006 -0.0262 0.0186 29 ILE A N 150 C CA . ILE A 29 ? 0.3619 0.3410 0.3293 0.0059 -0.0241 0.0201 29 ILE A CA 151 C C . ILE A 29 ? 0.3731 0.3590 0.3394 0.0077 -0.0248 0.0223 29 ILE A C 152 O O . ILE A 29 ? 0.4103 0.4025 0.3751 0.0118 -0.0240 0.0254 29 ILE A O 153 C CB . ILE A 29 ? 0.3736 0.3419 0.3345 0.0077 -0.0217 0.0172 29 ILE A CB 154 C CG1 . ILE A 29 ? 0.3845 0.3473 0.3464 0.0060 -0.0210 0.0153 29 ILE A CG1 155 C CG2 . ILE A 29 ? 0.3976 0.3651 0.3516 0.0135 -0.0195 0.0189 29 ILE A CG2 156 C CD1 . ILE A 29 ? 0.4003 0.3662 0.3626 0.0084 -0.0203 0.0176 29 ILE A CD1 157 N N . THR A 30 ? 0.3833 0.3685 0.3504 0.0046 -0.0263 0.0209 30 THR A N 158 C CA . THR A 30 ? 0.3964 0.3882 0.3626 0.0057 -0.0272 0.0228 30 THR A CA 159 C C . THR A 30 ? 0.4140 0.4183 0.3857 0.0035 -0.0297 0.0263 30 THR A C 160 O O . THR A 30 ? 0.4132 0.4264 0.3843 0.0063 -0.0298 0.0294 30 THR A O 161 C CB . THR A 30 ? 0.3970 0.3836 0.3621 0.0027 -0.0282 0.0200 30 THR A CB 162 O OG1 . THR A 30 ? 0.3900 0.3657 0.3499 0.0043 -0.0259 0.0169 30 THR A OG1 163 C CG2 . THR A 30 ? 0.4050 0.3983 0.3688 0.0038 -0.0292 0.0218 30 THR A CG2 164 N N . ASN A 31 ? 0.3987 0.4039 0.3755 -0.0013 -0.0316 0.0261 31 ASN A N 165 C CA . ASN A 31 ? 0.4067 0.4226 0.3884 -0.0050 -0.0343 0.0291 31 ASN A CA 166 C C . ASN A 31 ? 0.3947 0.4134 0.3805 -0.0067 -0.0347 0.0305 31 ASN A C 167 O O . ASN A 31 ? 0.3660 0.3767 0.3526 -0.0088 -0.0346 0.0281 31 ASN A O 168 C CB . ASN A 31 ? 0.4394 0.4522 0.4222 -0.0110 -0.0369 0.0271 31 ASN A CB 169 C CG . ASN A 31 ? 0.4672 0.4801 0.4469 -0.0103 -0.0372 0.0264 31 ASN A CG 170 O OD1 . ASN A 31 ? 0.5269 0.5497 0.5068 -0.0093 -0.0380 0.0294 31 ASN A OD1 171 N ND2 . ASN A 31 ? 0.4570 0.4593 0.4337 -0.0110 -0.0366 0.0227 31 ASN A ND2 172 N N . ASP A 32 ? 0.3841 0.4145 0.3725 -0.0059 -0.0353 0.0346 32 ASP A N 173 C CA A ASP A 32 ? 0.3886 0.4228 0.3813 -0.0083 -0.0361 0.0363 32 ASP A CA 174 C CA B ASP A 32 ? 0.3854 0.4197 0.3780 -0.0083 -0.0361 0.0364 32 ASP A CA 175 C C . ASP A 32 ? 0.3746 0.4061 0.3701 -0.0157 -0.0390 0.0352 32 ASP A C 176 O O . ASP A 32 ? 0.3786 0.4062 0.3761 -0.0179 -0.0393 0.0346 32 ASP A O 177 C CB A ASP A 32 ? 0.4121 0.4608 0.4070 -0.0064 -0.0363 0.0412 32 ASP A CB 178 C CB B ASP A 32 ? 0.4041 0.4532 0.3991 -0.0065 -0.0364 0.0413 32 ASP A CB 179 C CG A ASP A 32 ? 0.4423 0.4928 0.4338 0.0014 -0.0332 0.0426 32 ASP A CG 180 C CG B ASP A 32 ? 0.4219 0.4758 0.4212 -0.0090 -0.0372 0.0435 32 ASP A CG 181 O OD1 A ASP A 32 ? 0.4672 0.5091 0.4564 0.0042 -0.0312 0.0407 32 ASP A OD1 182 O OD1 B ASP A 32 ? 0.4461 0.4934 0.4450 -0.0073 -0.0356 0.0421 32 ASP A OD1 183 O OD2 A ASP A 32 ? 0.4725 0.5326 0.4629 0.0050 -0.0329 0.0455 32 ASP A OD2 184 O OD2 B ASP A 32 ? 0.4517 0.5162 0.4545 -0.0130 -0.0394 0.0466 32 ASP A OD2 185 N N . GLN A 33 ? 0.3593 0.3922 0.3544 -0.0192 -0.0410 0.0349 33 GLN A N 186 C CA . GLN A 33 ? 0.3602 0.3895 0.3564 -0.0262 -0.0439 0.0338 33 GLN A CA 187 C C . GLN A 33 ? 0.3459 0.3678 0.3387 -0.0275 -0.0445 0.0307 33 GLN A C 188 O O . GLN A 33 ? 0.3576 0.3849 0.3491 -0.0265 -0.0449 0.0316 33 GLN A O 189 C CB . GLN A 33 ? 0.3969 0.4383 0.3961 -0.0308 -0.0466 0.0378 33 GLN A CB 190 C CG . GLN A 33 ? 0.4232 0.4722 0.4260 -0.0303 -0.0462 0.0411 33 GLN A CG 191 C CD . GLN A 33 ? 0.4755 0.5334 0.4810 -0.0370 -0.0492 0.0444 33 GLN A CD 192 O OE1 . GLN A 33 ? 0.5236 0.5898 0.5293 -0.0398 -0.0511 0.0463 33 GLN A OE1 193 N NE2 . GLN A 33 ? 0.4966 0.5531 0.5041 -0.0397 -0.0497 0.0452 33 GLN A NE2 194 N N . ILE A 34 ? 0.3101 0.3202 0.3015 -0.0294 -0.0446 0.0270 34 ILE A N 195 C CA . ILE A 34 ? 0.3132 0.3161 0.3014 -0.0313 -0.0455 0.0241 34 ILE A CA 196 C C . ILE A 34 ? 0.3010 0.2954 0.2887 -0.0362 -0.0472 0.0221 34 ILE A C 197 O O . ILE A 34 ? 0.2895 0.2790 0.2783 -0.0357 -0.0464 0.0212 34 ILE A O 198 C CB . ILE A 34 ? 0.3196 0.3154 0.3046 -0.0265 -0.0428 0.0211 34 ILE A CB 199 C CG1 . ILE A 34 ? 0.3381 0.3269 0.3199 -0.0288 -0.0438 0.0182 34 ILE A CG1 200 C CG2 . ILE A 34 ? 0.3153 0.3039 0.3005 -0.0240 -0.0405 0.0190 34 ILE A CG2 201 C CD1 . ILE A 34 ? 0.3479 0.3311 0.3263 -0.0246 -0.0414 0.0156 34 ILE A CD1 202 N N . GLU A 35 ? 0.3035 0.2962 0.2892 -0.0409 -0.0497 0.0217 35 GLU A N 203 C CA . GLU A 35 ? 0.3116 0.2950 0.2953 -0.0454 -0.0515 0.0198 35 GLU A CA 204 C C . GLU A 35 ? 0.2960 0.2676 0.2765 -0.0431 -0.0500 0.0154 35 GLU A C 205 O O . GLU A 35 ? 0.3054 0.2758 0.2837 -0.0415 -0.0494 0.0139 35 GLU A O 206 C CB . GLU A 35 ? 0.3434 0.3289 0.3251 -0.0518 -0.0549 0.0212 35 GLU A CB 207 C CG . GLU A 35 ? 0.3800 0.3569 0.3593 -0.0569 -0.0570 0.0203 35 GLU A CG 208 C CD . GLU A 35 ? 0.4308 0.4088 0.4070 -0.0637 -0.0605 0.0215 35 GLU A CD 209 O OE1 . GLU A 35 ? 0.4814 0.4711 0.4601 -0.0667 -0.0621 0.0252 35 GLU A OE1 210 O OE2 . GLU A 35 ? 0.4572 0.4245 0.4281 -0.0661 -0.0617 0.0188 35 GLU A OE2 211 N N . VAL A 36 ? 0.2779 0.2417 0.2581 -0.0430 -0.0495 0.0137 36 VAL A N 212 C CA . VAL A 36 ? 0.2789 0.2323 0.2563 -0.0411 -0.0482 0.0098 36 VAL A CA 213 C C . VAL A 36 ? 0.2847 0.2294 0.2589 -0.0449 -0.0502 0.0086 36 VAL A C 214 O O . VAL A 36 ? 0.2953 0.2417 0.2697 -0.0490 -0.0523 0.0108 36 VAL A O 215 C CB . VAL A 36 ? 0.2668 0.2189 0.2464 -0.0365 -0.0453 0.0087 36 VAL A CB 216 C CG1 . VAL A 36 ? 0.2581 0.2158 0.2387 -0.0324 -0.0431 0.0092 36 VAL A CG1 217 C CG2 . VAL A 36 ? 0.2588 0.2130 0.2414 -0.0372 -0.0455 0.0106 36 VAL A CG2 218 N N . THR A 37 ? 0.2952 0.2304 0.2659 -0.0436 -0.0495 0.0052 37 THR A N 219 C CA . THR A 37 ? 0.3068 0.2324 0.2730 -0.0466 -0.0513 0.0040 37 THR A CA 220 C C . THR A 37 ? 0.3175 0.2398 0.2846 -0.0465 -0.0512 0.0044 37 THR A C 221 O O . THR A 37 ? 0.3240 0.2399 0.2875 -0.0499 -0.0531 0.0046 37 THR A O 222 C CB . THR A 37 ? 0.3146 0.2311 0.2763 -0.0446 -0.0504 0.0003 37 THR A CB 223 O OG1 . THR A 37 ? 0.3194 0.2351 0.2833 -0.0397 -0.0475 -0.0014 37 THR A OG1 224 C CG2 . THR A 37 ? 0.3017 0.2204 0.2616 -0.0452 -0.0508 -0.0001 37 THR A CG2 225 N N . ASN A 38 ? 0.3122 0.2385 0.2837 -0.0427 -0.0489 0.0046 38 ASN A N 226 C CA . ASN A 38 ? 0.3235 0.2468 0.2959 -0.0420 -0.0486 0.0049 38 ASN A CA 227 C C . ASN A 38 ? 0.3040 0.2348 0.2819 -0.0386 -0.0464 0.0059 38 ASN A C 228 O O . ASN A 38 ? 0.2733 0.2081 0.2528 -0.0357 -0.0446 0.0053 38 ASN A O 229 C CB . ASN A 38 ? 0.3601 0.2734 0.3288 -0.0397 -0.0477 0.0016 38 ASN A CB 230 C CG . ASN A 38 ? 0.4009 0.3097 0.3692 -0.0393 -0.0479 0.0019 38 ASN A CG 231 O OD1 . ASN A 38 ? 0.4081 0.3182 0.3769 -0.0423 -0.0494 0.0043 38 ASN A OD1 232 N ND2 . ASN A 38 ? 0.4994 0.4033 0.4666 -0.0354 -0.0462 -0.0004 38 ASN A ND2 233 N N . ALA A 39 ? 0.2910 0.2230 0.2710 -0.0389 -0.0465 0.0076 39 ALA A N 234 C CA . ALA A 39 ? 0.2887 0.2266 0.2731 -0.0356 -0.0445 0.0085 39 ALA A CA 235 C C . ALA A 39 ? 0.3044 0.2390 0.2894 -0.0352 -0.0445 0.0087 39 ALA A C 236 O O . ALA A 39 ? 0.3140 0.2423 0.2960 -0.0378 -0.0462 0.0087 39 ALA A O 237 C CB . ALA A 39 ? 0.2836 0.2315 0.2711 -0.0365 -0.0448 0.0117 39 ALA A CB 238 N N . THR A 40 ? 0.2978 0.2359 0.2860 -0.0320 -0.0426 0.0089 40 THR A N 239 C CA . THR A 40 ? 0.3040 0.2400 0.2932 -0.0313 -0.0424 0.0093 40 THR A CA 240 C C . THR A 40 ? 0.2873 0.2312 0.2806 -0.0303 -0.0416 0.0118 40 THR A C 241 O O . THR A 40 ? 0.2695 0.2189 0.2645 -0.0285 -0.0402 0.0122 40 THR A O 242 C CB . THR A 40 ? 0.3170 0.2477 0.3051 -0.0280 -0.0409 0.0063 40 THR A CB 243 O OG1 . THR A 40 ? 0.3719 0.2991 0.3596 -0.0278 -0.0414 0.0067 40 THR A OG1 244 C CG2 . THR A 40 ? 0.3334 0.2685 0.3241 -0.0247 -0.0385 0.0053 40 THR A CG2 245 N N . GLU A 41 ? 0.2807 0.2245 0.2749 -0.0314 -0.0424 0.0135 41 GLU A N 246 C CA . GLU A 41 ? 0.2727 0.2237 0.2705 -0.0307 -0.0418 0.0162 41 GLU A CA 247 C C . GLU A 41 ? 0.2604 0.2118 0.2599 -0.0266 -0.0395 0.0149 41 GLU A C 248 O O . GLU A 41 ? 0.2633 0.2095 0.2618 -0.0254 -0.0392 0.0131 41 GLU A O 249 C CB . GLU A 41 ? 0.2834 0.2337 0.2810 -0.0339 -0.0436 0.0186 41 GLU A CB 250 C CG . GLU A 41 ? 0.2795 0.2371 0.2806 -0.0333 -0.0431 0.0216 41 GLU A CG 251 C CD . GLU A 41 ? 0.2796 0.2467 0.2830 -0.0330 -0.0426 0.0238 41 GLU A CD 252 O OE1 . GLU A 41 ? 0.2894 0.2600 0.2925 -0.0366 -0.0443 0.0257 41 GLU A OE1 253 O OE2 . GLU A 41 ? 0.2535 0.2245 0.2586 -0.0293 -0.0406 0.0237 41 GLU A OE2 254 N N . LEU A 42 ? 0.2372 0.1947 0.2387 -0.0245 -0.0380 0.0159 42 LEU A N 255 C CA . LEU A 42 ? 0.2282 0.1860 0.2306 -0.0212 -0.0360 0.0148 42 LEU A CA 256 C C . LEU A 42 ? 0.2176 0.1795 0.2223 -0.0205 -0.0358 0.0172 42 LEU A C 257 O O . LEU A 42 ? 0.2104 0.1724 0.2155 -0.0181 -0.0343 0.0164 42 LEU A O 258 C CB . LEU A 42 ? 0.2278 0.1873 0.2292 -0.0190 -0.0342 0.0136 42 LEU A CB 259 C CG . LEU A 42 ? 0.2366 0.1918 0.2357 -0.0191 -0.0339 0.0109 42 LEU A CG 260 C CD1 . LEU A 42 ? 0.2383 0.1947 0.2360 -0.0168 -0.0319 0.0099 42 LEU A CD1 261 C CD2 . LEU A 42 ? 0.2371 0.1867 0.2355 -0.0189 -0.0340 0.0083 42 LEU A CD2 262 N N . VAL A 43 ? 0.2139 0.1796 0.2197 -0.0227 -0.0371 0.0202 43 VAL A N 263 C CA . VAL A 43 ? 0.2156 0.1852 0.2234 -0.0223 -0.0370 0.0227 43 VAL A CA 264 C C . VAL A 43 ? 0.2249 0.1910 0.2326 -0.0248 -0.0387 0.0235 43 VAL A C 265 O O . VAL A 43 ? 0.2265 0.1918 0.2333 -0.0284 -0.0406 0.0247 43 VAL A O 266 C CB . VAL A 43 ? 0.2125 0.1906 0.2218 -0.0225 -0.0370 0.0261 43 VAL A CB 267 C CG1 . VAL A 43 ? 0.2105 0.1928 0.2217 -0.0219 -0.0368 0.0287 43 VAL A CG1 268 C CG2 . VAL A 43 ? 0.2141 0.1949 0.2224 -0.0194 -0.0352 0.0254 43 VAL A CG2 269 N N . GLN A 44 ? 0.2275 0.1911 0.2356 -0.0230 -0.0380 0.0228 44 GLN A N 270 C CA . GLN A 44 ? 0.2339 0.1940 0.2415 -0.0248 -0.0394 0.0238 44 GLN A CA 271 C C . GLN A 44 ? 0.2455 0.2117 0.2550 -0.0265 -0.0400 0.0276 44 GLN A C 272 O O . GLN A 44 ? 0.2253 0.1968 0.2369 -0.0243 -0.0388 0.0289 44 GLN A O 273 C CB . GLN A 44 ? 0.2340 0.1906 0.2416 -0.0219 -0.0384 0.0220 44 GLN A CB 274 C CG . GLN A 44 ? 0.2430 0.1948 0.2492 -0.0230 -0.0397 0.0228 44 GLN A CG 275 C CD . GLN A 44 ? 0.2559 0.1999 0.2582 -0.0251 -0.0412 0.0216 44 GLN A CD 276 O OE1 . GLN A 44 ? 0.2687 0.2096 0.2696 -0.0240 -0.0408 0.0190 44 GLN A OE1 277 N NE2 . GLN A 44 ? 0.2676 0.2079 0.2676 -0.0282 -0.0430 0.0235 44 GLN A NE2 278 N N . SER A 45 ? 0.2566 0.2218 0.2649 -0.0307 -0.0420 0.0295 45 SER A N 279 C CA . SER A 45 ? 0.2867 0.2588 0.2969 -0.0329 -0.0427 0.0334 45 SER A CA 280 C C . SER A 45 ? 0.3144 0.2824 0.3232 -0.0357 -0.0441 0.0351 45 SER A C 281 O O . SER A 45 ? 0.3223 0.2960 0.3325 -0.0378 -0.0446 0.0385 45 SER A O 282 C CB . SER A 45 ? 0.3056 0.2839 0.3164 -0.0359 -0.0437 0.0354 45 SER A CB 283 O OG . SER A 45 ? 0.3440 0.3162 0.3516 -0.0397 -0.0455 0.0343 45 SER A OG 284 N N . SER A 46 ? 0.3356 0.2940 0.3412 -0.0355 -0.0446 0.0329 46 SER A N 285 C CA . SER A 46 ? 0.3698 0.3231 0.3730 -0.0377 -0.0459 0.0344 46 SER A CA 286 C C . SER A 46 ? 0.3821 0.3309 0.3850 -0.0334 -0.0447 0.0327 46 SER A C 287 O O . SER A 46 ? 0.3512 0.2987 0.3546 -0.0296 -0.0434 0.0297 46 SER A O 288 C CB . SER A 46 ? 0.3780 0.3223 0.3759 -0.0417 -0.0479 0.0338 46 SER A CB 289 O OG . SER A 46 ? 0.3909 0.3280 0.3863 -0.0390 -0.0474 0.0301 46 SER A OG 290 N N . SER A 47 ? 0.4287 0.3757 0.4307 -0.0343 -0.0452 0.0346 47 SER A N 291 C CA . SER A 47 ? 0.4521 0.3935 0.4526 -0.0309 -0.0446 0.0333 47 SER A CA 292 C C . SER A 47 ? 0.4966 0.4285 0.4915 -0.0337 -0.0464 0.0343 47 SER A C 293 O O . SER A 47 ? 0.4976 0.4297 0.4911 -0.0387 -0.0479 0.0369 47 SER A O 294 C CB . SER A 47 ? 0.4650 0.4131 0.4692 -0.0284 -0.0434 0.0350 47 SER A CB 295 O OG . SER A 47 ? 0.4904 0.4331 0.4928 -0.0256 -0.0431 0.0341 47 SER A OG 296 N N . THR A 48 ? 0.5458 0.4699 0.5375 -0.0305 -0.0461 0.0324 48 THR A N 297 C CA . THR A 48 ? 0.5918 0.5058 0.5774 -0.0319 -0.0474 0.0333 48 THR A CA 298 C C . THR A 48 ? 0.5743 0.4912 0.5607 -0.0340 -0.0478 0.0369 48 THR A C 299 O O . THR A 48 ? 0.6080 0.5180 0.5893 -0.0377 -0.0494 0.0387 48 THR A O 300 C CB . THR A 48 ? 0.6290 0.5371 0.6123 -0.0262 -0.0465 0.0310 48 THR A CB 301 O OG1 . THR A 48 ? 0.6940 0.5995 0.6763 -0.0239 -0.0460 0.0277 48 THR A OG1 302 C CG2 . THR A 48 ? 0.6461 0.5429 0.6221 -0.0268 -0.0477 0.0320 48 THR A CG2 303 N N . GLY A 49 ? 0.5236 0.4503 0.5160 -0.0316 -0.0464 0.0377 49 GLY A N 304 C CA . GLY A 49 ? 0.4976 0.4281 0.4913 -0.0329 -0.0465 0.0410 49 GLY A CA 305 C C . GLY A 49 ? 0.4665 0.3936 0.4591 -0.0286 -0.0458 0.0406 49 GLY A C 306 O O . GLY A 49 ? 0.4810 0.4113 0.4748 -0.0290 -0.0456 0.0431 49 GLY A O 307 N N . GLY A 50 ? 0.3979 0.3191 0.3883 -0.0244 -0.0453 0.0375 50 GLY A N 308 C CA . GLY A 50 ? 0.3561 0.2758 0.3462 -0.0196 -0.0444 0.0368 50 GLY A CA 309 C C . GLY A 50 ? 0.3138 0.2394 0.3081 -0.0148 -0.0428 0.0341 50 GLY A C 310 O O . GLY A 50 ? 0.2883 0.2151 0.2837 -0.0144 -0.0424 0.0319 50 GLY A O 311 N N . ILE A 51 ? 0.2871 0.2165 0.2835 -0.0115 -0.0418 0.0345 51 ILE A N 312 C CA . ILE A 51 ? 0.2832 0.2178 0.2828 -0.0072 -0.0404 0.0319 51 ILE A CA 313 C C . ILE A 51 ? 0.2960 0.2243 0.2919 -0.0033 -0.0405 0.0300 51 ILE A C 314 O O . ILE A 51 ? 0.3086 0.2327 0.3015 -0.0016 -0.0409 0.0311 51 ILE A O 315 C CB . ILE A 51 ? 0.2793 0.2214 0.2826 -0.0055 -0.0395 0.0332 51 ILE A CB 316 C CG1 . ILE A 51 ? 0.2836 0.2325 0.2904 -0.0083 -0.0391 0.0349 51 ILE A CG1 317 C CG2 . ILE A 51 ? 0.2819 0.2284 0.2874 -0.0016 -0.0383 0.0306 51 ILE A CG2 318 C CD1 . ILE A 51 ? 0.2799 0.2351 0.2893 -0.0071 -0.0383 0.0366 51 ILE A CD1 319 N N . CYS A 52 ? 0.2901 0.2180 0.2859 -0.0018 -0.0400 0.0272 52 CYS A N 320 C CA . CYS A 52 ? 0.3038 0.2269 0.2962 0.0023 -0.0398 0.0253 52 CYS A CA 321 C C . CYS A 52 ? 0.2926 0.2221 0.2877 0.0065 -0.0388 0.0247 52 CYS A C 322 O O . CYS A 52 ? 0.2778 0.2158 0.2777 0.0065 -0.0379 0.0241 52 CYS A O 323 C CB . CYS A 52 ? 0.3234 0.2457 0.3155 0.0027 -0.0394 0.0226 52 CYS A CB 324 S SG . CYS A 52 ? 0.3710 0.2841 0.3583 -0.0018 -0.0409 0.0229 52 CYS A SG 325 N N . ASP A 53 ? 0.2915 0.2165 0.2829 0.0102 -0.0390 0.0250 53 ASP A N 326 C CA . ASP A 53 ? 0.2977 0.2289 0.2913 0.0142 -0.0383 0.0249 53 ASP A CA 327 C C . ASP A 53 ? 0.2822 0.2190 0.2777 0.0176 -0.0373 0.0222 53 ASP A C 328 O O . ASP A 53 ? 0.2882 0.2314 0.2857 0.0206 -0.0368 0.0219 53 ASP A O 329 C CB . ASP A 53 ? 0.3149 0.2393 0.3034 0.0171 -0.0389 0.0265 53 ASP A CB 330 C CG . ASP A 53 ? 0.3352 0.2511 0.3175 0.0207 -0.0391 0.0254 53 ASP A CG 331 O OD1 . ASP A 53 ? 0.3441 0.2593 0.3259 0.0212 -0.0388 0.0232 53 ASP A OD1 332 O OD2 . ASP A 53 ? 0.3703 0.2793 0.3472 0.0235 -0.0396 0.0267 53 ASP A OD2 333 N N . SER A 54 ? 0.2701 0.2049 0.2649 0.0168 -0.0371 0.0203 54 SER A N 334 C CA . SER A 54 ? 0.2659 0.2067 0.2628 0.0191 -0.0361 0.0178 54 SER A CA 335 C C . SER A 54 ? 0.2639 0.2076 0.2637 0.0154 -0.0357 0.0165 54 SER A C 336 O O . SER A 54 ? 0.2558 0.1944 0.2544 0.0118 -0.0364 0.0172 54 SER A O 337 C CB . SER A 54 ? 0.2756 0.2101 0.2673 0.0232 -0.0361 0.0167 54 SER A CB 338 O OG . SER A 54 ? 0.2821 0.2115 0.2696 0.0267 -0.0366 0.0183 54 SER A OG 339 N N . PRO A 55 ? 0.2539 0.2056 0.2571 0.0159 -0.0347 0.0146 55 PRO A N 340 C CA . PRO A 55 ? 0.2588 0.2179 0.2637 0.0193 -0.0339 0.0137 55 PRO A CA 341 C C . PRO A 55 ? 0.2490 0.2158 0.2575 0.0183 -0.0337 0.0146 55 PRO A C 342 O O . PRO A 55 ? 0.2517 0.2258 0.2618 0.0206 -0.0332 0.0138 55 PRO A O 343 C CB . PRO A 55 ? 0.2571 0.2202 0.2634 0.0189 -0.0330 0.0113 55 PRO A CB 344 C CG . PRO A 55 ? 0.2546 0.2164 0.2622 0.0142 -0.0330 0.0112 55 PRO A CG 345 C CD . PRO A 55 ? 0.2569 0.2107 0.2621 0.0127 -0.0341 0.0133 55 PRO A CD 346 N N . HIS A 56 ? 0.2298 0.1955 0.2393 0.0152 -0.0340 0.0161 56 HIS A N 347 C CA . HIS A 56 ? 0.2273 0.1989 0.2393 0.0143 -0.0338 0.0170 56 HIS A CA 348 C C . HIS A 56 ? 0.2321 0.2022 0.2428 0.0167 -0.0345 0.0190 56 HIS A C 349 O O . HIS A 56 ? 0.2362 0.1990 0.2440 0.0174 -0.0352 0.0203 56 HIS A O 350 C CB . HIS A 56 ? 0.2252 0.1962 0.2382 0.0105 -0.0337 0.0178 56 HIS A CB 351 C CG . HIS A 56 ? 0.2261 0.1973 0.2397 0.0082 -0.0331 0.0161 56 HIS A CG 352 N ND1 . HIS A 56 ? 0.2244 0.2009 0.2391 0.0078 -0.0322 0.0141 56 HIS A ND1 353 C CD2 . HIS A 56 ? 0.2307 0.1973 0.2434 0.0061 -0.0333 0.0161 56 HIS A CD2 354 C CE1 . HIS A 56 ? 0.2323 0.2069 0.2467 0.0057 -0.0318 0.0130 56 HIS A CE1 355 N NE2 . HIS A 56 ? 0.2293 0.1982 0.2426 0.0048 -0.0325 0.0142 56 HIS A NE2 356 N N . GLN A 57 ? 0.2212 0.1979 0.2337 0.0178 -0.0343 0.0192 57 GLN A N 357 C CA . GLN A 57 ? 0.2215 0.1974 0.2330 0.0199 -0.0348 0.0212 57 GLN A CA 358 C C . GLN A 57 ? 0.2193 0.1926 0.2309 0.0172 -0.0352 0.0234 57 GLN A C 359 O O . GLN A 57 ? 0.2186 0.1962 0.2322 0.0151 -0.0347 0.0235 57 GLN A O 360 C CB . GLN A 57 ? 0.2167 0.2011 0.2299 0.0220 -0.0346 0.0208 57 GLN A CB 361 C CG . GLN A 57 ? 0.2205 0.2041 0.2324 0.0248 -0.0352 0.0229 57 GLN A CG 362 C CD . GLN A 57 ? 0.2233 0.2157 0.2367 0.0270 -0.0352 0.0226 57 GLN A CD 363 O OE1 . GLN A 57 ? 0.2247 0.2241 0.2403 0.0250 -0.0348 0.0212 57 GLN A OE1 364 N NE2 . GLN A 57 ? 0.2195 0.2114 0.2311 0.0311 -0.0357 0.0239 57 GLN A NE2 365 N N . ILE A 58 ? 0.2277 0.1938 0.2367 0.0173 -0.0359 0.0252 58 ILE A N 366 C CA . ILE A 58 ? 0.2389 0.2026 0.2480 0.0145 -0.0362 0.0276 58 ILE A CA 367 C C . ILE A 58 ? 0.2480 0.2121 0.2562 0.0164 -0.0366 0.0297 58 ILE A C 368 O O . ILE A 58 ? 0.2702 0.2314 0.2758 0.0197 -0.0370 0.0299 58 ILE A O 369 C CB . ILE A 58 ? 0.2549 0.2103 0.2611 0.0125 -0.0369 0.0286 58 ILE A CB 370 C CG1 . ILE A 58 ? 0.2593 0.2138 0.2659 0.0109 -0.0367 0.0265 58 ILE A CG1 371 C CG2 . ILE A 58 ? 0.2640 0.2187 0.2706 0.0092 -0.0373 0.0313 58 ILE A CG2 372 C CD1 . ILE A 58 ? 0.2563 0.2163 0.2661 0.0083 -0.0359 0.0258 58 ILE A CD1 373 N N . LEU A 59 ? 0.2370 0.2046 0.2470 0.0148 -0.0363 0.0312 59 LEU A N 374 C CA . LEU A 59 ? 0.2512 0.2184 0.2601 0.0160 -0.0367 0.0336 59 LEU A CA 375 C C . LEU A 59 ? 0.2579 0.2225 0.2665 0.0128 -0.0369 0.0362 59 LEU A C 376 O O . LEU A 59 ? 0.2530 0.2216 0.2638 0.0108 -0.0363 0.0366 59 LEU A O 377 C CB . LEU A 59 ? 0.2510 0.2256 0.2619 0.0174 -0.0362 0.0332 59 LEU A CB 378 C CG . LEU A 59 ? 0.2625 0.2378 0.2725 0.0192 -0.0365 0.0354 59 LEU A CG 379 C CD1 . LEU A 59 ? 0.2762 0.2457 0.2829 0.0220 -0.0373 0.0363 59 LEU A CD1 380 C CD2 . LEU A 59 ? 0.2531 0.2358 0.2646 0.0207 -0.0362 0.0343 59 LEU A CD2 381 N N . ASP A 60 ? 0.2619 0.2198 0.2674 0.0125 -0.0377 0.0380 60 ASP A N 382 C CA . ASP A 60 ? 0.2690 0.2246 0.2739 0.0091 -0.0381 0.0409 60 ASP A CA 383 C C . ASP A 60 ? 0.2698 0.2287 0.2752 0.0100 -0.0379 0.0432 60 ASP A C 384 O O . ASP A 60 ? 0.2741 0.2303 0.2771 0.0126 -0.0382 0.0439 60 ASP A O 385 C CB . ASP A 60 ? 0.2804 0.2266 0.2806 0.0080 -0.0391 0.0420 60 ASP A CB 386 C CG . ASP A 60 ? 0.2880 0.2321 0.2874 0.0034 -0.0397 0.0450 60 ASP A CG 387 O OD1 . ASP A 60 ? 0.2919 0.2421 0.2942 0.0020 -0.0392 0.0468 60 ASP A OD1 388 O OD2 . ASP A 60 ? 0.3028 0.2390 0.2982 0.0011 -0.0406 0.0455 60 ASP A OD2 389 N N . GLY A 61 ? 0.2640 0.2284 0.2720 0.0083 -0.0372 0.0443 61 GLY A N 390 C CA . GLY A 61 ? 0.2699 0.2378 0.2783 0.0092 -0.0369 0.0465 61 GLY A CA 391 C C . GLY A 61 ? 0.2849 0.2485 0.2908 0.0078 -0.0375 0.0498 61 GLY A C 392 O O . GLY A 61 ? 0.2891 0.2543 0.2945 0.0092 -0.0374 0.0515 61 GLY A O 393 N N . GLU A 62 ? 0.3015 0.2595 0.3054 0.0048 -0.0383 0.0507 62 GLU A N 394 C CA . GLU A 62 ? 0.3270 0.2802 0.3278 0.0024 -0.0391 0.0540 62 GLU A CA 395 C C . GLU A 62 ? 0.3187 0.2785 0.3217 0.0012 -0.0384 0.0570 62 GLU A C 396 O O . GLU A 62 ? 0.3018 0.2673 0.3078 -0.0007 -0.0378 0.0574 62 GLU A O 397 C CB . GLU A 62 ? 0.3629 0.3088 0.3591 0.0054 -0.0397 0.0540 62 GLU A CB 398 C CG . GLU A 62 ? 0.4033 0.3430 0.3969 0.0070 -0.0402 0.0512 62 GLU A CG 399 C CD . GLU A 62 ? 0.4670 0.3981 0.4549 0.0101 -0.0408 0.0514 62 GLU A CD 400 O OE1 . GLU A 62 ? 0.5175 0.4511 0.5057 0.0148 -0.0405 0.0504 62 GLU A OE1 401 O OE2 . GLU A 62 ? 0.5314 0.4530 0.5139 0.0079 -0.0417 0.0525 62 GLU A OE2 402 N N . ASN A 63 ? 0.3250 0.2842 0.3264 0.0026 -0.0384 0.0589 63 ASN A N 403 C CA . ASN A 63 ? 0.3390 0.3047 0.3424 0.0017 -0.0377 0.0618 63 ASN A CA 404 C C . ASN A 63 ? 0.3214 0.2946 0.3278 0.0049 -0.0365 0.0606 63 ASN A C 405 O O . ASN A 63 ? 0.3104 0.2887 0.3178 0.0049 -0.0357 0.0628 63 ASN A O 406 C CB . ASN A 63 ? 0.3732 0.3351 0.3732 0.0016 -0.0381 0.0648 63 ASN A CB 407 C CG . ASN A 63 ? 0.4189 0.3742 0.4154 -0.0029 -0.0392 0.0671 63 ASN A CG 408 O OD1 . ASN A 63 ? 0.4170 0.3737 0.4147 -0.0069 -0.0394 0.0678 63 ASN A OD1 409 N ND2 . ASN A 63 ? 0.4759 0.4236 0.4675 -0.0024 -0.0399 0.0685 63 ASN A ND2 410 N N . CYS A 64 ? 0.3138 0.2874 0.3210 0.0075 -0.0363 0.0571 64 CYS A N 411 C CA . CYS A 64 ? 0.3136 0.2930 0.3225 0.0102 -0.0354 0.0556 64 CYS A CA 412 C C . CYS A 64 ? 0.2953 0.2782 0.3062 0.0096 -0.0346 0.0535 64 CYS A C 413 O O . CYS A 64 ? 0.2844 0.2649 0.2957 0.0087 -0.0349 0.0513 64 CYS A O 414 C CB . CYS A 64 ? 0.3457 0.3235 0.3534 0.0136 -0.0358 0.0534 64 CYS A CB 415 S SG . CYS A 64 ? 0.3854 0.3590 0.3900 0.0157 -0.0366 0.0556 64 CYS A SG 416 N N . THR A 65 ? 0.2737 0.2617 0.2853 0.0102 -0.0335 0.0540 65 THR A N 417 C CA . THR A 65 ? 0.2620 0.2526 0.2743 0.0106 -0.0326 0.0515 65 THR A CA 418 C C . THR A 65 ? 0.2495 0.2399 0.2612 0.0127 -0.0328 0.0484 65 THR A C 419 O O . THR A 65 ? 0.2572 0.2472 0.2681 0.0144 -0.0334 0.0486 65 THR A O 420 C CB . THR A 65 ? 0.2602 0.2552 0.2721 0.0112 -0.0313 0.0530 65 THR A CB 421 O OG1 . THR A 65 ? 0.2652 0.2616 0.2758 0.0134 -0.0311 0.0537 65 THR A OG1 422 C CG2 . THR A 65 ? 0.2738 0.2710 0.2868 0.0092 -0.0310 0.0566 65 THR A CG2 423 N N . LEU A 66 ? 0.2447 0.2360 0.2566 0.0125 -0.0323 0.0456 66 LEU A N 424 C CA . LEU A 66 ? 0.2361 0.2285 0.2473 0.0138 -0.0324 0.0428 66 LEU A CA 425 C C . LEU A 66 ? 0.2382 0.2331 0.2477 0.0155 -0.0321 0.0435 66 LEU A C 426 O O . LEU A 66 ? 0.2297 0.2257 0.2388 0.0169 -0.0328 0.0427 66 LEU A O 427 C CB . LEU A 66 ? 0.2315 0.2243 0.2424 0.0128 -0.0318 0.0401 66 LEU A CB 428 C CG . LEU A 66 ? 0.2329 0.2274 0.2428 0.0132 -0.0319 0.0371 66 LEU A CG 429 C CD1 . LEU A 66 ? 0.2329 0.2277 0.2441 0.0144 -0.0330 0.0363 66 LEU A CD1 430 C CD2 . LEU A 66 ? 0.2253 0.2193 0.2346 0.0116 -0.0312 0.0347 66 LEU A CD2 431 N N . ILE A 67 ? 0.2470 0.2432 0.2552 0.0155 -0.0311 0.0452 67 ILE A N 432 C CA . ILE A 67 ? 0.2569 0.2549 0.2627 0.0171 -0.0307 0.0458 67 ILE A CA 433 C C . ILE A 67 ? 0.2579 0.2562 0.2643 0.0184 -0.0315 0.0480 67 ILE A C 434 O O . ILE A 67 ? 0.2616 0.2612 0.2667 0.0198 -0.0319 0.0475 67 ILE A O 435 C CB . ILE A 67 ? 0.2640 0.2629 0.2675 0.0175 -0.0292 0.0471 67 ILE A CB 436 C CG1 . ILE A 67 ? 0.2738 0.2716 0.2752 0.0168 -0.0284 0.0445 67 ILE A CG1 437 C CG2 . ILE A 67 ? 0.2636 0.2639 0.2643 0.0194 -0.0288 0.0483 67 ILE A CG2 438 C CD1 . ILE A 67 ? 0.2925 0.2896 0.2922 0.0163 -0.0289 0.0412 67 ILE A CD1 439 N N . ASP A 68 ? 0.2626 0.2594 0.2705 0.0176 -0.0318 0.0504 68 ASP A N 440 C CA . ASP A 68 ? 0.2792 0.2750 0.2868 0.0188 -0.0326 0.0525 68 ASP A CA 441 C C . ASP A 68 ? 0.2710 0.2657 0.2786 0.0202 -0.0337 0.0505 68 ASP A C 442 O O . ASP A 68 ? 0.2709 0.2665 0.2774 0.0222 -0.0342 0.0511 68 ASP A O 443 C CB . ASP A 68 ? 0.2940 0.2876 0.3023 0.0171 -0.0328 0.0556 68 ASP A CB 444 C CG . ASP A 68 ? 0.3317 0.3284 0.3398 0.0165 -0.0318 0.0586 68 ASP A CG 445 O OD1 . ASP A 68 ? 0.3649 0.3645 0.3717 0.0182 -0.0309 0.0587 68 ASP A OD1 446 O OD2 . ASP A 68 ? 0.4002 0.3967 0.4093 0.0143 -0.0318 0.0610 68 ASP A OD2 447 N N . ALA A 69 ? 0.2654 0.2585 0.2740 0.0194 -0.0341 0.0483 69 ALA A N 448 C CA . ALA A 69 ? 0.2720 0.2649 0.2806 0.0211 -0.0349 0.0463 69 ALA A CA 449 C C . ALA A 69 ? 0.2682 0.2659 0.2764 0.0223 -0.0349 0.0442 69 ALA A C 450 O O . ALA A 69 ? 0.2844 0.2839 0.2923 0.0244 -0.0357 0.0438 69 ALA A O 451 C CB . ALA A 69 ? 0.2725 0.2630 0.2823 0.0201 -0.0352 0.0444 69 ALA A CB 452 N N . LEU A 70 ? 0.2571 0.2567 0.2648 0.0208 -0.0341 0.0431 70 LEU A N 453 C CA . LEU A 70 ? 0.2566 0.2599 0.2628 0.0210 -0.0341 0.0412 70 LEU A CA 454 C C . LEU A 70 ? 0.2691 0.2742 0.2736 0.0227 -0.0344 0.0429 70 LEU A C 455 O O . LEU A 70 ? 0.2671 0.2755 0.2712 0.0240 -0.0352 0.0421 70 LEU A O 456 C CB . LEU A 70 ? 0.2479 0.2508 0.2524 0.0190 -0.0331 0.0400 70 LEU A CB 457 C CG . LEU A 70 ? 0.2430 0.2481 0.2444 0.0182 -0.0330 0.0379 70 LEU A CG 458 C CD1 . LEU A 70 ? 0.2319 0.2394 0.2342 0.0170 -0.0336 0.0350 70 LEU A CD1 459 C CD2 . LEU A 70 ? 0.2433 0.2460 0.2413 0.0172 -0.0317 0.0378 70 LEU A CD2 460 N N . LEU A 71 ? 0.2692 0.2729 0.2727 0.0229 -0.0337 0.0455 71 LEU A N 461 C CA . LEU A 71 ? 0.2819 0.2870 0.2835 0.0245 -0.0337 0.0473 71 LEU A CA 462 C C . LEU A 71 ? 0.2856 0.2906 0.2881 0.0266 -0.0348 0.0487 71 LEU A C 463 O O . LEU A 71 ? 0.2885 0.2959 0.2896 0.0283 -0.0353 0.0490 71 LEU A O 464 C CB . LEU A 71 ? 0.2872 0.2911 0.2878 0.0244 -0.0326 0.0500 71 LEU A CB 465 C CG . LEU A 71 ? 0.2999 0.3034 0.2987 0.0233 -0.0313 0.0491 71 LEU A CG 466 C CD1 . LEU A 71 ? 0.3102 0.3138 0.3079 0.0240 -0.0302 0.0523 71 LEU A CD1 467 C CD2 . LEU A 71 ? 0.3076 0.3120 0.3029 0.0231 -0.0313 0.0466 71 LEU A CD2 468 N N . GLY A 72 ? 0.2859 0.2877 0.2900 0.0265 -0.0351 0.0494 72 GLY A N 469 C CA . GLY A 72 ? 0.2952 0.2954 0.2991 0.0288 -0.0360 0.0507 72 GLY A CA 470 C C . GLY A 72 ? 0.3184 0.3151 0.3211 0.0290 -0.0359 0.0542 72 GLY A C 471 O O . GLY A 72 ? 0.3104 0.3069 0.3115 0.0312 -0.0364 0.0557 72 GLY A O 472 N N . ASP A 73 ? 0.3213 0.3157 0.3246 0.0265 -0.0352 0.0556 73 ASP A N 473 C CA . ASP A 73 ? 0.3478 0.3388 0.3502 0.0257 -0.0352 0.0591 73 ASP A CA 474 C C . ASP A 73 ? 0.3564 0.3421 0.3571 0.0270 -0.0362 0.0595 73 ASP A C 475 O O . ASP A 73 ? 0.3491 0.3328 0.3502 0.0273 -0.0367 0.0574 73 ASP A O 476 C CB . ASP A 73 ? 0.3546 0.3450 0.3584 0.0224 -0.0345 0.0599 73 ASP A CB 477 C CG . ASP A 73 ? 0.3927 0.3809 0.3957 0.0206 -0.0344 0.0638 73 ASP A CG 478 O OD1 . ASP A 73 ? 0.4421 0.4265 0.4430 0.0213 -0.0351 0.0655 73 ASP A OD1 479 O OD2 . ASP A 73 ? 0.3952 0.3857 0.3994 0.0183 -0.0336 0.0651 73 ASP A OD2 480 N N . PRO A 74 ? 0.3910 0.3742 0.3893 0.0283 -0.0365 0.0622 74 PRO A N 481 C CA . PRO A 74 ? 0.4013 0.3786 0.3968 0.0303 -0.0375 0.0625 74 PRO A CA 482 C C . PRO A 74 ? 0.4053 0.3761 0.3998 0.0284 -0.0379 0.0620 74 PRO A C 483 O O . PRO A 74 ? 0.4155 0.3832 0.4085 0.0308 -0.0385 0.0604 74 PRO A O 484 C CB . PRO A 74 ? 0.4300 0.4047 0.4227 0.0305 -0.0375 0.0662 74 PRO A CB 485 C CG . PRO A 74 ? 0.4206 0.4022 0.4148 0.0311 -0.0367 0.0665 74 PRO A CG 486 C CD . PRO A 74 ? 0.4044 0.3904 0.4019 0.0288 -0.0360 0.0646 74 PRO A CD 487 N N . GLN A 75 ? 0.4081 0.3773 0.4034 0.0244 -0.0375 0.0634 75 GLN A N 488 C CA . GLN A 75 ? 0.4190 0.3820 0.4131 0.0221 -0.0380 0.0628 75 GLN A CA 489 C C . GLN A 75 ? 0.3875 0.3523 0.3838 0.0229 -0.0381 0.0591 75 GLN A C 490 O O . GLN A 75 ? 0.3770 0.3362 0.3718 0.0221 -0.0385 0.0582 75 GLN A O 491 C CB . GLN A 75 ? 0.4363 0.3982 0.4308 0.0172 -0.0378 0.0652 75 GLN A CB 492 C CG . GLN A 75 ? 0.4486 0.4178 0.4475 0.0152 -0.0369 0.0645 75 GLN A CG 493 C CD . GLN A 75 ? 0.4813 0.4512 0.4807 0.0108 -0.0367 0.0675 75 GLN A CD 494 O OE1 . GLN A 75 ? 0.5257 0.4901 0.5220 0.0085 -0.0374 0.0700 75 GLN A OE1 495 N NE2 . GLN A 75 ? 0.4590 0.4357 0.4617 0.0096 -0.0358 0.0675 75 GLN A NE2 496 N N . CYS A 76 ? 0.3640 0.3361 0.3633 0.0244 -0.0376 0.0570 76 CYS A N 497 C CA . CYS A 76 ? 0.3531 0.3277 0.3545 0.0249 -0.0375 0.0536 76 CYS A CA 498 C C . CYS A 76 ? 0.3429 0.3198 0.3438 0.0290 -0.0379 0.0516 76 CYS A C 499 O O . CYS A 76 ? 0.3214 0.3022 0.3243 0.0295 -0.0378 0.0489 76 CYS A O 500 C CB . CYS A 76 ? 0.3632 0.3442 0.3678 0.0231 -0.0366 0.0524 76 CYS A CB 501 S SG . CYS A 76 ? 0.3835 0.3647 0.3889 0.0193 -0.0359 0.0551 76 CYS A SG 502 N N . ASP A 77 ? 0.3339 0.3087 0.3321 0.0320 -0.0384 0.0532 77 ASP A N 503 C CA . ASP A 77 ? 0.3383 0.3167 0.3361 0.0363 -0.0388 0.0517 77 ASP A CA 504 C C . ASP A 77 ? 0.3242 0.3012 0.3217 0.0380 -0.0391 0.0494 77 ASP A C 505 O O . ASP A 77 ? 0.3204 0.3036 0.3195 0.0403 -0.0392 0.0473 77 ASP A O 506 C CB . ASP A 77 ? 0.3536 0.3289 0.3477 0.0396 -0.0393 0.0541 77 ASP A CB 507 C CG . ASP A 77 ? 0.3715 0.3509 0.3662 0.0392 -0.0391 0.0559 77 ASP A CG 508 O OD1 . ASP A 77 ? 0.3684 0.3539 0.3660 0.0372 -0.0386 0.0550 77 ASP A OD1 509 O OD2 . ASP A 77 ? 0.3675 0.3437 0.3590 0.0413 -0.0393 0.0582 77 ASP A OD2 510 N N . GLY A 78 ? 0.3307 0.2996 0.3260 0.0366 -0.0392 0.0497 78 GLY A N 511 C CA . GLY A 78 ? 0.3320 0.2983 0.3263 0.0383 -0.0393 0.0476 78 GLY A CA 512 C C . GLY A 78 ? 0.3219 0.2948 0.3206 0.0365 -0.0389 0.0447 78 GLY A C 513 O O . GLY A 78 ? 0.3236 0.2971 0.3221 0.0386 -0.0389 0.0427 78 GLY A O 514 N N . PHE A 79 ? 0.3127 0.2904 0.3147 0.0330 -0.0384 0.0445 79 PHE A N 515 C CA . PHE A 79 ? 0.3067 0.2897 0.3120 0.0310 -0.0379 0.0418 79 PHE A CA 516 C C . PHE A 79 ? 0.2833 0.2752 0.2905 0.0327 -0.0379 0.0401 79 PHE A C 517 O O . PHE A 79 ? 0.2625 0.2589 0.2718 0.0310 -0.0376 0.0378 79 PHE A O 518 C CB . PHE A 79 ? 0.3354 0.3188 0.3424 0.0268 -0.0373 0.0424 79 PHE A CB 519 C CG . PHE A 79 ? 0.3640 0.3407 0.3700 0.0242 -0.0374 0.0438 79 PHE A CG 520 C CD1 . PHE A 79 ? 0.3916 0.3640 0.3956 0.0234 -0.0376 0.0468 79 PHE A CD1 521 C CD2 . PHE A 79 ? 0.4063 0.3814 0.4133 0.0220 -0.0372 0.0422 79 PHE A CD2 522 C CE1 . PHE A 79 ? 0.3916 0.3584 0.3945 0.0202 -0.0378 0.0483 79 PHE A CE1 523 C CE2 . PHE A 79 ? 0.4111 0.3804 0.4170 0.0192 -0.0374 0.0435 79 PHE A CE2 524 C CZ . PHE A 79 ? 0.3872 0.3527 0.3911 0.0181 -0.0377 0.0466 79 PHE A CZ 525 N N . GLN A 80 ? 0.2724 0.2671 0.2785 0.0357 -0.0384 0.0412 80 GLN A N 526 C CA . GLN A 80 ? 0.2645 0.2683 0.2722 0.0364 -0.0385 0.0398 80 GLN A CA 527 C C . GLN A 80 ? 0.2565 0.2653 0.2659 0.0369 -0.0385 0.0371 80 GLN A C 528 O O . GLN A 80 ? 0.2498 0.2566 0.2582 0.0399 -0.0386 0.0368 80 GLN A O 529 C CB . GLN A 80 ? 0.2740 0.2804 0.2802 0.0402 -0.0391 0.0414 80 GLN A CB 530 C CG . GLN A 80 ? 0.2871 0.2916 0.2921 0.0393 -0.0391 0.0437 80 GLN A CG 531 C CD . GLN A 80 ? 0.3100 0.3189 0.3138 0.0427 -0.0397 0.0448 80 GLN A CD 532 O OE1 . GLN A 80 ? 0.3131 0.3258 0.3167 0.0463 -0.0402 0.0442 80 GLN A OE1 533 N NE2 . GLN A 80 ? 0.3196 0.3286 0.3226 0.0418 -0.0396 0.0465 80 GLN A NE2 534 N N . ASN A 81 ? 0.2480 0.2629 0.2593 0.0341 -0.0383 0.0352 81 ASN A N 535 C CA . ASN A 81 ? 0.2527 0.2739 0.2657 0.0338 -0.0383 0.0327 81 ASN A CA 536 C C . ASN A 81 ? 0.2504 0.2679 0.2640 0.0330 -0.0378 0.0313 81 ASN A C 537 O O . ASN A 81 ? 0.2554 0.2781 0.2703 0.0331 -0.0377 0.0294 81 ASN A O 538 C CB . ASN A 81 ? 0.2627 0.2908 0.2757 0.0380 -0.0389 0.0328 81 ASN A CB 539 C CG . ASN A 81 ? 0.2681 0.3018 0.2807 0.0383 -0.0395 0.0338 81 ASN A CG 540 O OD1 . ASN A 81 ? 0.2734 0.3113 0.2864 0.0347 -0.0396 0.0328 81 ASN A OD1 541 N ND2 . ASN A 81 ? 0.2783 0.3110 0.2893 0.0424 -0.0400 0.0358 81 ASN A ND2 542 N N . LYS A 82 ? 0.2529 0.2618 0.2655 0.0319 -0.0375 0.0323 82 LYS A N 543 C CA . LYS A 82 ? 0.2601 0.2648 0.2728 0.0311 -0.0371 0.0310 82 LYS A CA 544 C C . LYS A 82 ? 0.2419 0.2490 0.2564 0.0270 -0.0365 0.0290 82 LYS A C 545 O O . LYS A 82 ? 0.2358 0.2449 0.2505 0.0244 -0.0362 0.0290 82 LYS A O 546 C CB . LYS A 82 ? 0.2834 0.2783 0.2942 0.0306 -0.0371 0.0328 82 LYS A CB 547 C CG . LYS A 82 ? 0.3133 0.3034 0.3211 0.0346 -0.0377 0.0345 82 LYS A CG 548 C CD . LYS A 82 ? 0.3362 0.3161 0.3413 0.0332 -0.0378 0.0364 82 LYS A CD 549 C CE . LYS A 82 ? 0.3510 0.3248 0.3543 0.0332 -0.0378 0.0352 82 LYS A CE 550 N NZ . LYS A 82 ? 0.3951 0.3585 0.3939 0.0335 -0.0383 0.0373 82 LYS A NZ 551 N N . LYS A 83 ? 0.2345 0.2410 0.2496 0.0267 -0.0362 0.0272 83 LYS A N 552 C CA . LYS A 83 ? 0.2309 0.2383 0.2471 0.0230 -0.0355 0.0253 83 LYS A CA 553 C C . LYS A 83 ? 0.2268 0.2266 0.2425 0.0218 -0.0353 0.0254 83 LYS A C 554 O O . LYS A 83 ? 0.2209 0.2148 0.2351 0.0238 -0.0357 0.0266 83 LYS A O 555 C CB . LYS A 83 ? 0.2422 0.2569 0.2597 0.0233 -0.0354 0.0230 83 LYS A CB 556 C CG . LYS A 83 ? 0.2474 0.2710 0.2654 0.0242 -0.0359 0.0229 83 LYS A CG 557 C CD . LYS A 83 ? 0.2591 0.2907 0.2785 0.0231 -0.0357 0.0207 83 LYS A CD 558 C CE . LYS A 83 ? 0.2757 0.3174 0.2959 0.0250 -0.0363 0.0209 83 LYS A CE 559 N NZ . LYS A 83 ? 0.2760 0.3197 0.2964 0.0308 -0.0366 0.0219 83 LYS A NZ 560 N N . TRP A 84 ? 0.2153 0.2147 0.2315 0.0185 -0.0347 0.0241 84 TRP A N 561 C CA . TRP A 84 ? 0.2064 0.1995 0.2222 0.0169 -0.0344 0.0241 84 TRP A CA 562 C C . TRP A 84 ? 0.1993 0.1942 0.2158 0.0142 -0.0337 0.0220 84 TRP A C 563 O O . TRP A 84 ? 0.1945 0.1939 0.2111 0.0127 -0.0333 0.0210 84 TRP A O 564 C CB . TRP A 84 ? 0.2072 0.1957 0.2224 0.0154 -0.0345 0.0265 84 TRP A CB 565 C CG . TRP A 84 ? 0.2040 0.1955 0.2194 0.0136 -0.0339 0.0268 84 TRP A CG 566 C CD1 . TRP A 84 ? 0.1980 0.1891 0.2131 0.0110 -0.0332 0.0261 84 TRP A CD1 567 C CD2 . TRP A 84 ? 0.2045 0.1993 0.2194 0.0144 -0.0340 0.0279 84 TRP A CD2 568 N NE1 . TRP A 84 ? 0.2008 0.1942 0.2149 0.0104 -0.0327 0.0267 84 TRP A NE1 569 C CE2 . TRP A 84 ? 0.2058 0.2015 0.2198 0.0122 -0.0333 0.0277 84 TRP A CE2 570 C CE3 . TRP A 84 ? 0.2079 0.2046 0.2226 0.0169 -0.0347 0.0290 84 TRP A CE3 571 C CZ2 . TRP A 84 ? 0.2067 0.2048 0.2195 0.0125 -0.0331 0.0285 84 TRP A CZ2 572 C CZ3 . TRP A 84 ? 0.2094 0.2092 0.2234 0.0169 -0.0346 0.0298 84 TRP A CZ3 573 C CH2 . TRP A 84 ? 0.2149 0.2152 0.2278 0.0147 -0.0339 0.0295 84 TRP A CH2 574 N N . ASP A 85 ? 0.1981 0.1889 0.2145 0.0135 -0.0336 0.0213 85 ASP A N 575 C CA . ASP A 85 ? 0.1945 0.1846 0.2110 0.0106 -0.0329 0.0200 85 ASP A CA 576 C C . ASP A 85 ? 0.1967 0.1831 0.2127 0.0088 -0.0328 0.0218 85 ASP A C 577 O O . ASP A 85 ? 0.1936 0.1809 0.2091 0.0069 -0.0320 0.0215 85 ASP A O 578 C CB . ASP A 85 ? 0.1984 0.1861 0.2148 0.0108 -0.0328 0.0184 85 ASP A CB 579 C CG . ASP A 85 ? 0.2114 0.2041 0.2284 0.0126 -0.0327 0.0166 85 ASP A CG 580 O OD1 . ASP A 85 ? 0.2131 0.2121 0.2308 0.0121 -0.0325 0.0158 85 ASP A OD1 581 O OD2 . ASP A 85 ? 0.2115 0.2020 0.2280 0.0145 -0.0328 0.0159 85 ASP A OD2 582 N N . LEU A 86 ? 0.1960 0.1781 0.2116 0.0094 -0.0334 0.0238 86 LEU A N 583 C CA . LEU A 86 ? 0.1954 0.1751 0.2108 0.0076 -0.0334 0.0259 86 LEU A CA 584 C C . LEU A 86 ? 0.1997 0.1780 0.2147 0.0086 -0.0340 0.0286 86 LEU A C 585 O O . LEU A 86 ? 0.2071 0.1817 0.2211 0.0098 -0.0348 0.0293 86 LEU A O 586 C CB . LEU A 86 ? 0.1902 0.1658 0.2054 0.0058 -0.0336 0.0259 86 LEU A CB 587 C CG . LEU A 86 ? 0.1902 0.1654 0.2057 0.0037 -0.0334 0.0281 86 LEU A CG 588 C CD1 . LEU A 86 ? 0.1857 0.1645 0.2011 0.0032 -0.0322 0.0276 86 LEU A CD1 589 C CD2 . LEU A 86 ? 0.1901 0.1615 0.2051 0.0018 -0.0339 0.0281 86 LEU A CD2 590 N N . PHE A 87 ? 0.2072 0.1881 0.2223 0.0083 -0.0336 0.0301 87 PHE A N 591 C CA . PHE A 87 ? 0.2154 0.1955 0.2301 0.0089 -0.0340 0.0329 87 PHE A CA 592 C C . PHE A 87 ? 0.2159 0.1941 0.2308 0.0066 -0.0341 0.0351 87 PHE A C 593 O O . PHE A 87 ? 0.2066 0.1867 0.2219 0.0053 -0.0333 0.0351 87 PHE A O 594 C CB . PHE A 87 ? 0.2229 0.2072 0.2375 0.0098 -0.0335 0.0335 87 PHE A CB 595 C CG . PHE A 87 ? 0.2334 0.2173 0.2475 0.0109 -0.0339 0.0363 87 PHE A CG 596 C CD1 . PHE A 87 ? 0.2347 0.2175 0.2488 0.0095 -0.0339 0.0391 87 PHE A CD1 597 C CD2 . PHE A 87 ? 0.2454 0.2303 0.2589 0.0133 -0.0344 0.0362 87 PHE A CD2 598 C CE1 . PHE A 87 ? 0.2478 0.2302 0.2612 0.0103 -0.0343 0.0417 87 PHE A CE1 599 C CE2 . PHE A 87 ? 0.2529 0.2370 0.2656 0.0143 -0.0348 0.0388 87 PHE A CE2 600 C CZ . PHE A 87 ? 0.2528 0.2354 0.2654 0.0127 -0.0347 0.0415 87 PHE A CZ 601 N N . VAL A 88 ? 0.2230 0.1972 0.2369 0.0060 -0.0350 0.0370 88 VAL A N 602 C CA . VAL A 88 ? 0.2299 0.2027 0.2438 0.0031 -0.0353 0.0393 88 VAL A CA 603 C C . VAL A 88 ? 0.2398 0.2141 0.2536 0.0028 -0.0353 0.0426 88 VAL A C 604 O O . VAL A 88 ? 0.2555 0.2268 0.2678 0.0036 -0.0360 0.0438 88 VAL A O 605 C CB . VAL A 88 ? 0.2360 0.2026 0.2483 0.0015 -0.0363 0.0391 88 VAL A CB 606 C CG1 . VAL A 88 ? 0.2418 0.2078 0.2540 -0.0021 -0.0368 0.0417 88 VAL A CG1 607 C CG2 . VAL A 88 ? 0.2297 0.1951 0.2421 0.0020 -0.0362 0.0359 88 VAL A CG2 608 N N . GLU A 89 ? 0.2400 0.2190 0.2550 0.0019 -0.0345 0.0442 89 GLU A N 609 C CA . GLU A 89 ? 0.2508 0.2325 0.2659 0.0016 -0.0343 0.0476 89 GLU A CA 610 C C . GLU A 89 ? 0.2522 0.2337 0.2675 -0.0017 -0.0349 0.0503 89 GLU A C 611 O O . GLU A 89 ? 0.2385 0.2219 0.2548 -0.0034 -0.0347 0.0502 89 GLU A O 612 C CB . GLU A 89 ? 0.2529 0.2403 0.2686 0.0032 -0.0329 0.0480 89 GLU A CB 613 C CG . GLU A 89 ? 0.2660 0.2541 0.2808 0.0060 -0.0324 0.0464 89 GLU A CG 614 C CD . GLU A 89 ? 0.2597 0.2520 0.2738 0.0075 -0.0311 0.0470 89 GLU A CD 615 O OE1 . GLU A 89 ? 0.2517 0.2463 0.2657 0.0071 -0.0302 0.0476 89 GLU A OE1 616 O OE2 . GLU A 89 ? 0.2528 0.2458 0.2658 0.0094 -0.0309 0.0468 89 GLU A OE2 617 N N . ARG A 90 ? 0.2601 0.2396 0.2741 -0.0028 -0.0356 0.0530 90 ARG A N 618 C CA . ARG A 90 ? 0.2764 0.2551 0.2899 -0.0068 -0.0365 0.0559 90 ARG A CA 619 C C . ARG A 90 ? 0.2878 0.2739 0.3029 -0.0076 -0.0357 0.0594 90 ARG A C 620 O O . ARG A 90 ? 0.2751 0.2642 0.2905 -0.0050 -0.0348 0.0601 90 ARG A O 621 C CB . ARG A 90 ? 0.2819 0.2531 0.2920 -0.0078 -0.0378 0.0569 90 ARG A CB 622 C CG . ARG A 90 ? 0.2879 0.2518 0.2957 -0.0056 -0.0384 0.0537 90 ARG A CG 623 C CD . ARG A 90 ? 0.2872 0.2494 0.2954 -0.0070 -0.0386 0.0514 90 ARG A CD 624 N NE . ARG A 90 ? 0.2887 0.2427 0.2936 -0.0061 -0.0395 0.0492 90 ARG A NE 625 C CZ . ARG A 90 ? 0.2925 0.2428 0.2963 -0.0079 -0.0400 0.0476 90 ARG A CZ 626 N NH1 . ARG A 90 ? 0.2853 0.2398 0.2914 -0.0108 -0.0399 0.0480 90 ARG A NH1 627 N NH2 . ARG A 90 ? 0.2977 0.2401 0.2978 -0.0066 -0.0407 0.0457 90 ARG A NH2 628 N N . SER A 91 ? 0.3050 0.2943 0.3209 -0.0112 -0.0361 0.0617 91 SER A N 629 C CA . SER A 91 ? 0.3207 0.3185 0.3384 -0.0118 -0.0352 0.0653 91 SER A CA 630 C C . SER A 91 ? 0.3390 0.3363 0.3554 -0.0127 -0.0355 0.0684 91 SER A C 631 O O . SER A 91 ? 0.3607 0.3647 0.3783 -0.0115 -0.0345 0.0709 91 SER A O 632 C CB . SER A 91 ? 0.3254 0.3279 0.3445 -0.0157 -0.0356 0.0672 91 SER A CB 633 O OG . SER A 91 ? 0.3349 0.3323 0.3520 -0.0206 -0.0374 0.0686 91 SER A OG 634 N N . LYS A 92 ? 0.3507 0.3398 0.3643 -0.0146 -0.0369 0.0683 92 LYS A N 635 C CA . LYS A 92 ? 0.3755 0.3624 0.3869 -0.0154 -0.0373 0.0711 92 LYS A CA 636 C C . LYS A 92 ? 0.3573 0.3442 0.3685 -0.0105 -0.0364 0.0701 92 LYS A C 637 O O . LYS A 92 ? 0.3577 0.3441 0.3675 -0.0105 -0.0364 0.0725 92 LYS A O 638 C CB . LYS A 92 ? 0.4034 0.3796 0.4104 -0.0184 -0.0390 0.0708 92 LYS A CB 639 C CG . LYS A 92 ? 0.4340 0.4021 0.4387 -0.0144 -0.0393 0.0672 92 LYS A CG 640 C CD . LYS A 92 ? 0.4798 0.4367 0.4793 -0.0168 -0.0408 0.0666 92 LYS A CD 641 C CE . LYS A 92 ? 0.4969 0.4473 0.4944 -0.0120 -0.0408 0.0631 92 LYS A CE 642 N NZ . LYS A 92 ? 0.5024 0.4409 0.4934 -0.0127 -0.0421 0.0632 92 LYS A NZ 643 N N . ALA A 93 ? 0.3332 0.3206 0.3456 -0.0065 -0.0356 0.0666 93 ALA A N 644 C CA . ALA A 93 ? 0.3272 0.3139 0.3389 -0.0023 -0.0350 0.0654 93 ALA A CA 645 C C . ALA A 93 ? 0.3342 0.3274 0.3466 -0.0011 -0.0339 0.0683 93 ALA A C 646 O O . ALA A 93 ? 0.3362 0.3362 0.3504 -0.0019 -0.0330 0.0702 93 ALA A O 647 C CB . ALA A 93 ? 0.3102 0.2975 0.3229 0.0007 -0.0344 0.0613 93 ALA A CB 648 N N . TYR A 94 ? 0.3379 0.3291 0.3486 0.0009 -0.0340 0.0690 94 TYR A N 649 C CA . TYR A 94 ? 0.3529 0.3496 0.3638 0.0023 -0.0330 0.0717 94 TYR A CA 650 C C . TYR A 94 ? 0.3520 0.3471 0.3615 0.0062 -0.0328 0.0704 94 TYR A C 651 O O . TYR A 94 ? 0.3389 0.3281 0.3468 0.0072 -0.0338 0.0685 94 TYR A O 652 C CB . TYR A 94 ? 0.3779 0.3749 0.3879 -0.0012 -0.0334 0.0760 94 TYR A CB 653 C CG . TYR A 94 ? 0.3925 0.3808 0.3992 -0.0023 -0.0348 0.0763 94 TYR A CG 654 C CD1 . TYR A 94 ? 0.4116 0.3929 0.4166 -0.0050 -0.0361 0.0752 94 TYR A CD1 655 C CD2 . TYR A 94 ? 0.4194 0.4061 0.4240 -0.0003 -0.0348 0.0778 94 TYR A CD2 656 C CE1 . TYR A 94 ? 0.4339 0.4061 0.4346 -0.0056 -0.0373 0.0755 94 TYR A CE1 657 C CE2 . TYR A 94 ? 0.4328 0.4109 0.4335 -0.0009 -0.0360 0.0781 94 TYR A CE2 658 C CZ . TYR A 94 ? 0.4501 0.4206 0.4486 -0.0034 -0.0372 0.0770 94 TYR A CZ 659 O OH . TYR A 94 ? 0.4556 0.4163 0.4490 -0.0035 -0.0383 0.0773 94 TYR A OH 660 N N . SER A 95 ? 0.3536 0.3539 0.3632 0.0085 -0.0316 0.0714 95 SER A N 661 C CA . SER A 95 ? 0.3591 0.3585 0.3671 0.0120 -0.0315 0.0704 95 SER A CA 662 C C . SER A 95 ? 0.3635 0.3617 0.3699 0.0117 -0.0318 0.0736 95 SER A C 663 O O . SER A 95 ? 0.3611 0.3621 0.3678 0.0094 -0.0315 0.0772 95 SER A O 664 C CB . SER A 95 ? 0.3644 0.3690 0.3722 0.0147 -0.0300 0.0699 95 SER A CB 665 O OG . SER A 95 ? 0.3579 0.3628 0.3663 0.0150 -0.0296 0.0669 95 SER A OG 666 N N . ASN A 96 ? 0.3640 0.3585 0.3686 0.0140 -0.0325 0.0726 96 ASN A N 667 C CA . ASN A 96 ? 0.3789 0.3710 0.3812 0.0139 -0.0329 0.0755 96 ASN A CA 668 C C . ASN A 96 ? 0.3748 0.3675 0.3756 0.0179 -0.0328 0.0748 96 ASN A C 669 O O . ASN A 96 ? 0.3840 0.3725 0.3825 0.0189 -0.0336 0.0756 96 ASN A O 670 C CB . ASN A 96 ? 0.4065 0.3907 0.4068 0.0118 -0.0343 0.0757 96 ASN A CB 671 C CG . ASN A 96 ? 0.4357 0.4170 0.4332 0.0098 -0.0346 0.0797 96 ASN A CG 672 O OD1 . ASN A 96 ? 0.4576 0.4440 0.4558 0.0087 -0.0338 0.0828 96 ASN A OD1 673 N ND2 . ASN A 96 ? 0.4469 0.4197 0.4408 0.0096 -0.0358 0.0797 96 ASN A ND2 674 N N . CYS A 97 ? 0.3657 0.3633 0.3672 0.0200 -0.0318 0.0734 97 CYS A N 675 C CA . CYS A 97 ? 0.3686 0.3675 0.3685 0.0233 -0.0318 0.0727 97 CYS A CA 676 C C . CYS A 97 ? 0.3577 0.3618 0.3571 0.0243 -0.0303 0.0742 97 CYS A C 677 O O . CYS A 97 ? 0.3375 0.3443 0.3378 0.0226 -0.0294 0.0770 97 CYS A O 678 C CB . CYS A 97 ? 0.3803 0.3784 0.3804 0.0249 -0.0324 0.0685 97 CYS A CB 679 S SG . CYS A 97 ? 0.4047 0.4041 0.4028 0.0286 -0.0330 0.0668 97 CYS A SG 680 N N . TYR A 98 ? 0.3579 0.3637 0.3556 0.0270 -0.0300 0.0726 98 TYR A N 681 C CA . TYR A 98 ? 0.3617 0.3715 0.3578 0.0285 -0.0285 0.0739 98 TYR A CA 682 C C . TYR A 98 ? 0.3653 0.3772 0.3622 0.0277 -0.0273 0.0732 98 TYR A C 683 O O . TYR A 98 ? 0.3575 0.3678 0.3551 0.0270 -0.0277 0.0701 98 TYR A O 684 C CB . TYR A 98 ? 0.3642 0.3742 0.3574 0.0312 -0.0286 0.0718 98 TYR A CB 685 C CG . TYR A 98 ? 0.3631 0.3756 0.3534 0.0333 -0.0274 0.0741 98 TYR A CG 686 C CD1 . TYR A 98 ? 0.3643 0.3788 0.3523 0.0345 -0.0259 0.0739 98 TYR A CD1 687 C CD2 . TYR A 98 ? 0.3761 0.3886 0.3654 0.0344 -0.0278 0.0764 98 TYR A CD2 688 C CE1 . TYR A 98 ? 0.3732 0.3897 0.3579 0.0369 -0.0247 0.0760 98 TYR A CE1 689 C CE2 . TYR A 98 ? 0.3733 0.3882 0.3598 0.0365 -0.0267 0.0785 98 TYR A CE2 690 C CZ . TYR A 98 ? 0.3784 0.3953 0.3626 0.0378 -0.0252 0.0783 98 TYR A CZ 691 O OH . TYR A 98 ? 0.3800 0.3989 0.3608 0.0403 -0.0240 0.0803 98 TYR A OH 692 N N . PRO A 99 ? 0.3577 0.3736 0.3544 0.0279 -0.0259 0.0762 99 PRO A N 693 C CA . PRO A 99 ? 0.3519 0.3701 0.3490 0.0277 -0.0247 0.0758 99 PRO A CA 694 C C . PRO A 99 ? 0.3413 0.3579 0.3352 0.0299 -0.0241 0.0723 99 PRO A C 695 O O . PRO A 99 ? 0.3259 0.3419 0.3161 0.0322 -0.0238 0.0718 99 PRO A O 696 C CB . PRO A 99 ? 0.3635 0.3873 0.3604 0.0284 -0.0232 0.0800 99 PRO A CB 697 C CG . PRO A 99 ? 0.3671 0.3910 0.3629 0.0292 -0.0234 0.0824 99 PRO A CG 698 C CD . PRO A 99 ? 0.3670 0.3858 0.3635 0.0280 -0.0253 0.0805 99 PRO A CD 699 N N . TYR A 100 ? 0.3239 0.3393 0.3185 0.0288 -0.0241 0.0700 100 TYR A N 700 C CA . TYR A 100 ? 0.3166 0.3295 0.3076 0.0302 -0.0237 0.0665 100 TYR A CA 701 C C . TYR A 100 ? 0.3174 0.3307 0.3080 0.0301 -0.0226 0.0659 100 TYR A C 702 O O . TYR A 100 ? 0.2990 0.3147 0.2931 0.0285 -0.0225 0.0675 100 TYR A O 703 C CB . TYR A 100 ? 0.3187 0.3281 0.3103 0.0288 -0.0254 0.0629 100 TYR A CB 704 C CG . TYR A 100 ? 0.3155 0.3237 0.3110 0.0263 -0.0263 0.0615 100 TYR A CG 705 C CD1 . TYR A 100 ? 0.3171 0.3251 0.3161 0.0246 -0.0274 0.0630 100 TYR A CD1 706 C CD2 . TYR A 100 ? 0.3105 0.3172 0.3054 0.0255 -0.0260 0.0587 100 TYR A CD2 707 C CE1 . TYR A 100 ? 0.3237 0.3299 0.3255 0.0224 -0.0282 0.0616 100 TYR A CE1 708 C CE2 . TYR A 100 ? 0.3109 0.3165 0.3092 0.0232 -0.0267 0.0575 100 TYR A CE2 709 C CZ . TYR A 100 ? 0.3171 0.3225 0.3189 0.0217 -0.0279 0.0589 100 TYR A CZ 710 O OH . TYR A 100 ? 0.3109 0.3145 0.3153 0.0196 -0.0287 0.0576 100 TYR A OH 711 N N . ASP A 101 ? 0.3267 0.3374 0.3123 0.0319 -0.0217 0.0636 101 ASP A N 712 C CA . ASP A 101 ? 0.3343 0.3437 0.3187 0.0317 -0.0209 0.0620 101 ASP A CA 713 C C . ASP A 101 ? 0.3206 0.3245 0.3012 0.0311 -0.0214 0.0576 101 ASP A C 714 O O . ASP A 101 ? 0.3024 0.3044 0.2805 0.0312 -0.0222 0.0562 101 ASP A O 715 C CB . ASP A 101 ? 0.3831 0.3947 0.3640 0.0349 -0.0187 0.0643 101 ASP A CB 716 C CG . ASP A 101 ? 0.4357 0.4434 0.4087 0.0380 -0.0176 0.0631 101 ASP A CG 717 O OD1 . ASP A 101 ? 0.4695 0.4754 0.4405 0.0381 -0.0183 0.0624 101 ASP A OD1 718 O OD2 . ASP A 101 ? 0.5587 0.5648 0.5269 0.0404 -0.0160 0.0630 101 ASP A OD2 719 N N . VAL A 102 ? 0.2914 0.2934 0.2717 0.0301 -0.0212 0.0557 102 VAL A N 720 C CA . VAL A 102 ? 0.2891 0.2861 0.2655 0.0290 -0.0215 0.0517 102 VAL A CA 721 C C . VAL A 102 ? 0.3008 0.2949 0.2715 0.0308 -0.0197 0.0513 102 VAL A C 722 O O . VAL A 102 ? 0.2898 0.2851 0.2629 0.0305 -0.0192 0.0517 102 VAL A O 723 C CB . VAL A 102 ? 0.2852 0.2821 0.2665 0.0257 -0.0230 0.0495 102 VAL A CB 724 C CG1 . VAL A 102 ? 0.2841 0.2769 0.2616 0.0241 -0.0235 0.0455 102 VAL A CG1 725 C CG2 . VAL A 102 ? 0.2784 0.2782 0.2655 0.0246 -0.0245 0.0506 102 VAL A CG2 726 N N . PRO A 103 ? 0.3138 0.3036 0.2765 0.0328 -0.0187 0.0505 103 PRO A N 727 C CA . PRO A 103 ? 0.3282 0.3134 0.2844 0.0345 -0.0171 0.0495 103 PRO A CA 728 C C . PRO A 103 ? 0.3394 0.3217 0.2968 0.0312 -0.0180 0.0463 103 PRO A C 729 O O . PRO A 103 ? 0.3740 0.3551 0.3325 0.0281 -0.0195 0.0438 103 PRO A O 730 C CB . PRO A 103 ? 0.3339 0.3131 0.2804 0.0361 -0.0165 0.0483 103 PRO A CB 731 C CG . PRO A 103 ? 0.3316 0.3146 0.2803 0.0369 -0.0171 0.0504 103 PRO A CG 732 C CD . PRO A 103 ? 0.3204 0.3089 0.2789 0.0339 -0.0189 0.0507 103 PRO A CD 733 N N . ASP A 104 ? 0.3561 0.3380 0.3135 0.0318 -0.0170 0.0464 104 ASP A N 734 C CA . ASP A 104 ? 0.3583 0.3382 0.3178 0.0286 -0.0178 0.0436 104 ASP A CA 735 C C . ASP A 104 ? 0.3122 0.2964 0.2806 0.0252 -0.0198 0.0430 104 ASP A C 736 O O . ASP A 104 ? 0.2962 0.2786 0.2655 0.0222 -0.0210 0.0401 104 ASP A O 737 C CB . ASP A 104 ? 0.4012 0.3733 0.3525 0.0271 -0.0177 0.0400 104 ASP A CB 738 C CG . ASP A 104 ? 0.4478 0.4166 0.3982 0.0255 -0.0174 0.0379 104 ASP A CG 739 O OD1 . ASP A 104 ? 0.4528 0.4251 0.4084 0.0258 -0.0172 0.0391 104 ASP A OD1 740 O OD2 . ASP A 104 ? 0.5240 0.4864 0.4679 0.0235 -0.0175 0.0350 104 ASP A OD2 741 N N . TYR A 105 ? 0.2774 0.2672 0.2519 0.0258 -0.0201 0.0460 105 TYR A N 742 C CA . TYR A 105 ? 0.2616 0.2548 0.2437 0.0233 -0.0217 0.0462 105 TYR A CA 743 C C . TYR A 105 ? 0.2439 0.2356 0.2282 0.0209 -0.0222 0.0439 105 TYR A C 744 O O . TYR A 105 ? 0.2381 0.2296 0.2254 0.0186 -0.0236 0.0419 105 TYR A O 745 C CB . TYR A 105 ? 0.2680 0.2664 0.2545 0.0242 -0.0215 0.0501 105 TYR A CB 746 C CG . TYR A 105 ? 0.2760 0.2769 0.2693 0.0216 -0.0231 0.0508 105 TYR A CG 747 C CD1 . TYR A 105 ? 0.2913 0.2926 0.2882 0.0196 -0.0235 0.0504 105 TYR A CD1 748 C CD2 . TYR A 105 ? 0.2819 0.2840 0.2773 0.0214 -0.0241 0.0520 105 TYR A CD2 749 C CE1 . TYR A 105 ? 0.2867 0.2890 0.2885 0.0174 -0.0250 0.0510 105 TYR A CE1 750 C CE2 . TYR A 105 ? 0.2917 0.2948 0.2920 0.0193 -0.0255 0.0527 105 TYR A CE2 751 C CZ . TYR A 105 ? 0.2866 0.2893 0.2898 0.0173 -0.0259 0.0522 105 TYR A CZ 752 O OH . TYR A 105 ? 0.3032 0.3055 0.3102 0.0152 -0.0273 0.0528 105 TYR A OH 753 N N . ALA A 106 ? 0.2319 0.2228 0.2144 0.0218 -0.0210 0.0442 106 ALA A N 754 C CA . ALA A 106 ? 0.2285 0.2181 0.2130 0.0197 -0.0214 0.0421 106 ALA A CA 755 C C . ALA A 106 ? 0.2311 0.2164 0.2129 0.0177 -0.0220 0.0383 106 ALA A C 756 O O . ALA A 106 ? 0.2311 0.2166 0.2166 0.0153 -0.0230 0.0366 106 ALA A O 757 C CB . ALA A 106 ? 0.2246 0.2138 0.2066 0.0214 -0.0199 0.0430 106 ALA A CB 758 N N . SER A 107 ? 0.2412 0.2227 0.2162 0.0184 -0.0213 0.0371 107 SER A N 759 C CA . SER A 107 ? 0.2445 0.2225 0.2165 0.0158 -0.0220 0.0336 107 SER A CA 760 C C . SER A 107 ? 0.2356 0.2170 0.2122 0.0138 -0.0237 0.0328 107 SER A C 761 O O . SER A 107 ? 0.2315 0.2129 0.2096 0.0113 -0.0246 0.0304 107 SER A O 762 C CB . SER A 107 ? 0.2540 0.2259 0.2163 0.0164 -0.0209 0.0324 107 SER A CB 763 O OG . SER A 107 ? 0.2625 0.2301 0.2198 0.0179 -0.0194 0.0324 107 SER A OG 764 N N . LEU A 108 ? 0.2334 0.2177 0.2119 0.0152 -0.0242 0.0348 108 LEU A N 765 C CA . LEU A 108 ? 0.2294 0.2168 0.2116 0.0140 -0.0258 0.0341 108 LEU A CA 766 C C . LEU A 108 ? 0.2224 0.2126 0.2116 0.0132 -0.0267 0.0343 108 LEU A C 767 O O . LEU A 108 ? 0.2233 0.2149 0.2149 0.0116 -0.0278 0.0324 108 LEU A O 768 C CB . LEU A 108 ? 0.2312 0.2207 0.2134 0.0160 -0.0260 0.0364 108 LEU A CB 769 C CG . LEU A 108 ? 0.2310 0.2241 0.2170 0.0154 -0.0276 0.0361 108 LEU A CG 770 C CD1 . LEU A 108 ? 0.2360 0.2292 0.2195 0.0132 -0.0284 0.0331 108 LEU A CD1 771 C CD2 . LEU A 108 ? 0.2304 0.2251 0.2158 0.0175 -0.0277 0.0387 108 LEU A CD2 772 N N . ARG A 109 ? 0.2106 0.2015 0.2026 0.0141 -0.0263 0.0366 109 ARG A N 773 C CA . ARG A 109 ? 0.2081 0.2002 0.2055 0.0130 -0.0270 0.0368 109 ARG A CA 774 C C . ARG A 109 ? 0.2067 0.1971 0.2040 0.0111 -0.0272 0.0338 109 ARG A C 775 O O . ARG A 109 ? 0.1974 0.1887 0.1980 0.0101 -0.0282 0.0325 109 ARG A O 776 C CB . ARG A 109 ? 0.2060 0.1992 0.2053 0.0137 -0.0265 0.0397 109 ARG A CB 777 C CG . ARG A 109 ? 0.2083 0.2017 0.2121 0.0121 -0.0274 0.0400 109 ARG A CG 778 C CD . ARG A 109 ? 0.2083 0.2038 0.2138 0.0123 -0.0270 0.0433 109 ARG A CD 779 N NE . ARG A 109 ? 0.2056 0.2008 0.2145 0.0103 -0.0278 0.0436 109 ARG A NE 780 C CZ . ARG A 109 ? 0.2010 0.1953 0.2104 0.0091 -0.0277 0.0423 109 ARG A CZ 781 N NH1 . ARG A 109 ? 0.1970 0.1902 0.2034 0.0098 -0.0266 0.0405 109 ARG A NH1 782 N NH2 . ARG A 109 ? 0.1944 0.1882 0.2064 0.0072 -0.0286 0.0428 109 ARG A NH2 783 N N . SER A 110 ? 0.2110 0.1987 0.2042 0.0109 -0.0260 0.0327 110 SER A N 784 C CA . SER A 110 ? 0.2149 0.2007 0.2075 0.0090 -0.0259 0.0300 110 SER A CA 785 C C . SER A 110 ? 0.2179 0.2043 0.2098 0.0072 -0.0268 0.0273 110 SER A C 786 O O . SER A 110 ? 0.2233 0.2109 0.2181 0.0058 -0.0274 0.0257 110 SER A O 787 C CB . SER A 110 ? 0.2213 0.2031 0.2082 0.0094 -0.0244 0.0295 110 SER A CB 788 O OG . SER A 110 ? 0.2307 0.2103 0.2164 0.0073 -0.0244 0.0268 110 SER A OG 789 N N . LEU A 111 ? 0.2189 0.2050 0.2067 0.0072 -0.0267 0.0269 111 LEU A N 790 C CA . LEU A 111 ? 0.2304 0.2179 0.2171 0.0050 -0.0276 0.0245 111 LEU A CA 791 C C . LEU A 111 ? 0.2195 0.2122 0.2120 0.0054 -0.0290 0.0246 111 LEU A C 792 O O . LEU A 111 ? 0.2320 0.2272 0.2261 0.0038 -0.0296 0.0227 111 LEU A O 793 C CB . LEU A 111 ? 0.2419 0.2274 0.2221 0.0044 -0.0273 0.0239 111 LEU A CB 794 C CG . LEU A 111 ? 0.2452 0.2327 0.2251 0.0061 -0.0278 0.0257 111 LEU A CG 795 C CD1 . LEU A 111 ? 0.2484 0.2412 0.2310 0.0049 -0.0293 0.0247 111 LEU A CD1 796 C CD2 . LEU A 111 ? 0.2636 0.2460 0.2351 0.0064 -0.0268 0.0256 111 LEU A CD2 797 N N . VAL A 112 ? 0.2199 0.2141 0.2152 0.0076 -0.0294 0.0271 112 VAL A N 798 C CA . VAL A 112 ? 0.2157 0.2138 0.2158 0.0086 -0.0306 0.0275 112 VAL A CA 799 C C . VAL A 112 ? 0.2112 0.2087 0.2150 0.0083 -0.0308 0.0270 112 VAL A C 800 O O . VAL A 112 ? 0.1984 0.1984 0.2045 0.0083 -0.0315 0.0257 112 VAL A O 801 C CB . VAL A 112 ? 0.2192 0.2180 0.2205 0.0109 -0.0309 0.0303 112 VAL A CB 802 C CG1 . VAL A 112 ? 0.2227 0.2242 0.2278 0.0122 -0.0321 0.0307 112 VAL A CG1 803 C CG2 . VAL A 112 ? 0.2241 0.2236 0.2214 0.0112 -0.0308 0.0306 112 VAL A CG2 804 N N . ALA A 113 ? 0.2095 0.2039 0.2136 0.0083 -0.0301 0.0280 113 ALA A N 805 C CA . ALA A 113 ? 0.2069 0.2001 0.2139 0.0077 -0.0302 0.0275 113 ALA A CA 806 C C . ALA A 113 ? 0.2070 0.2007 0.2136 0.0061 -0.0302 0.0246 113 ALA A C 807 O O . ALA A 113 ? 0.1979 0.1924 0.2072 0.0063 -0.0308 0.0238 113 ALA A O 808 C CB . ALA A 113 ? 0.1997 0.1903 0.2065 0.0075 -0.0295 0.0290 113 ALA A CB 809 N N . SER A 114 ? 0.2036 0.1963 0.2064 0.0046 -0.0294 0.0231 114 SER A N 810 C CA . SER A 114 ? 0.2210 0.2141 0.2228 0.0024 -0.0292 0.0204 114 SER A CA 811 C C . SER A 114 ? 0.2252 0.2233 0.2281 0.0019 -0.0301 0.0190 114 SER A C 812 O O . SER A 114 ? 0.2353 0.2355 0.2397 0.0009 -0.0303 0.0172 114 SER A O 813 C CB . SER A 114 ? 0.2305 0.2200 0.2265 0.0008 -0.0281 0.0194 114 SER A CB 814 O OG . SER A 114 ? 0.2607 0.2500 0.2552 -0.0017 -0.0279 0.0169 114 SER A OG 815 N N . SER A 115 ? 0.2242 0.2248 0.2265 0.0027 -0.0307 0.0199 115 SER A N 816 C CA . SER A 115 ? 0.2279 0.2346 0.2315 0.0027 -0.0316 0.0190 115 SER A CA 817 C C . SER A 115 ? 0.2233 0.2327 0.2317 0.0052 -0.0323 0.0195 115 SER A C 818 O O . SER A 115 ? 0.2379 0.2523 0.2479 0.0051 -0.0328 0.0182 115 SER A O 819 C CB . SER A 115 ? 0.2332 0.2416 0.2348 0.0032 -0.0321 0.0201 115 SER A CB 820 O OG . SER A 115 ? 0.2458 0.2610 0.2493 0.0038 -0.0332 0.0198 115 SER A OG 821 N N . GLY A 116 ? 0.2143 0.2204 0.2244 0.0074 -0.0324 0.0215 116 GLY A N 822 C CA . GLY A 116 ? 0.2101 0.2161 0.2231 0.0096 -0.0329 0.0219 116 GLY A CA 823 C C . GLY A 116 ? 0.2111 0.2211 0.2254 0.0125 -0.0338 0.0228 116 GLY A C 824 O O . GLY A 116 ? 0.2057 0.2164 0.2215 0.0146 -0.0342 0.0225 116 GLY A O 825 N N . THR A 117 ? 0.2140 0.2263 0.2271 0.0128 -0.0341 0.0237 117 THR A N 826 C CA . THR A 117 ? 0.2190 0.2355 0.2330 0.0157 -0.0350 0.0246 117 THR A CA 827 C C . THR A 117 ? 0.2226 0.2384 0.2352 0.0165 -0.0352 0.0267 117 THR A C 828 O O . THR A 117 ? 0.2263 0.2412 0.2368 0.0145 -0.0348 0.0267 117 THR A O 829 C CB . THR A 117 ? 0.2186 0.2433 0.2331 0.0152 -0.0354 0.0228 117 THR A CB 830 O OG1 . THR A 117 ? 0.2253 0.2547 0.2407 0.0186 -0.0363 0.0239 117 THR A OG1 831 C CG2 . THR A 117 ? 0.2176 0.2447 0.2296 0.0114 -0.0353 0.0216 117 THR A CG2 832 N N . LEU A 118 ? 0.2287 0.2444 0.2421 0.0197 -0.0359 0.0284 118 LEU A N 833 C CA . LEU A 118 ? 0.2390 0.2551 0.2512 0.0210 -0.0362 0.0304 118 LEU A CA 834 C C . LEU A 118 ? 0.2417 0.2649 0.2540 0.0230 -0.0371 0.0302 118 LEU A C 835 O O . LEU A 118 ? 0.2443 0.2680 0.2558 0.0249 -0.0375 0.0319 118 LEU A O 836 C CB . LEU A 118 ? 0.2451 0.2553 0.2572 0.0230 -0.0363 0.0329 118 LEU A CB 837 C CG . LEU A 118 ? 0.2499 0.2545 0.2617 0.0209 -0.0355 0.0341 118 LEU A CG 838 C CD1 . LEU A 118 ? 0.2632 0.2623 0.2749 0.0222 -0.0358 0.0363 118 LEU A CD1 839 C CD2 . LEU A 118 ? 0.2499 0.2553 0.2600 0.0199 -0.0351 0.0351 118 LEU A CD2 840 N N . GLU A 119 ? 0.2528 0.2820 0.2662 0.0225 -0.0373 0.0281 119 GLU A N 841 C CA . GLU A 119 ? 0.2664 0.3041 0.2802 0.0242 -0.0382 0.0280 119 GLU A CA 842 C C . GLU A 119 ? 0.2644 0.3044 0.2762 0.0226 -0.0386 0.0285 119 GLU A C 843 O O . GLU A 119 ? 0.2640 0.3028 0.2738 0.0188 -0.0382 0.0274 119 GLU A O 844 C CB . GLU A 119 ? 0.2836 0.3284 0.2987 0.0225 -0.0383 0.0257 119 GLU A CB 845 C CG . GLU A 119 ? 0.3038 0.3485 0.3208 0.0247 -0.0380 0.0250 119 GLU A CG 846 C CD . GLU A 119 ? 0.3209 0.3717 0.3388 0.0217 -0.0378 0.0226 119 GLU A CD 847 O OE1 . GLU A 119 ? 0.3041 0.3506 0.3214 0.0180 -0.0371 0.0213 119 GLU A OE1 848 O OE2 . GLU A 119 ? 0.3124 0.3727 0.3316 0.0230 -0.0384 0.0222 119 GLU A OE2 849 N N . PHE A 120 ? 0.2712 0.3141 0.2828 0.0258 -0.0394 0.0301 120 PHE A N 850 C CA . PHE A 120 ? 0.2699 0.3143 0.2793 0.0249 -0.0398 0.0310 120 PHE A CA 851 C C . PHE A 120 ? 0.2826 0.3367 0.2925 0.0268 -0.0410 0.0310 120 PHE A C 852 O O . PHE A 120 ? 0.2809 0.3377 0.2925 0.0309 -0.0413 0.0319 120 PHE A O 853 C CB . PHE A 120 ? 0.2709 0.3085 0.2792 0.0273 -0.0395 0.0336 120 PHE A CB 854 C CG . PHE A 120 ? 0.2809 0.3189 0.2865 0.0265 -0.0397 0.0346 120 PHE A CG 855 C CD1 . PHE A 120 ? 0.2823 0.3162 0.2854 0.0234 -0.0390 0.0342 120 PHE A CD1 856 C CD2 . PHE A 120 ? 0.2827 0.3250 0.2879 0.0293 -0.0406 0.0360 120 PHE A CD2 857 C CE1 . PHE A 120 ? 0.2814 0.3150 0.2813 0.0229 -0.0391 0.0351 120 PHE A CE1 858 C CE2 . PHE A 120 ? 0.2820 0.3244 0.2844 0.0286 -0.0408 0.0369 120 PHE A CE2 859 C CZ . PHE A 120 ? 0.2922 0.3301 0.2918 0.0254 -0.0400 0.0364 120 PHE A CZ 860 N N . ASN A 121 ? 0.2916 0.3506 0.2996 0.0236 -0.0416 0.0301 121 ASN A N 861 C CA . ASN A 121 ? 0.3203 0.3897 0.3286 0.0247 -0.0429 0.0302 121 ASN A CA 862 C C . ASN A 121 ? 0.3266 0.3950 0.3320 0.0248 -0.0434 0.0316 121 ASN A C 863 O O . ASN A 121 ? 0.3062 0.3706 0.3083 0.0211 -0.0431 0.0309 121 ASN A O 864 C CB . ASN A 121 ? 0.3502 0.4274 0.3584 0.0201 -0.0434 0.0279 121 ASN A CB 865 C CG . ASN A 121 ? 0.3955 0.4775 0.4071 0.0211 -0.0431 0.0268 121 ASN A CG 866 O OD1 . ASN A 121 ? 0.4301 0.5117 0.4440 0.0260 -0.0429 0.0279 121 ASN A OD1 867 N ND2 . ASN A 121 ? 0.4566 0.5431 0.4679 0.0163 -0.0432 0.0247 121 ASN A ND2 868 N N . ASN A 122 ? 0.3391 0.4105 0.3452 0.0293 -0.0440 0.0335 122 ASN A N 869 C CA . ASN A 122 ? 0.3529 0.4241 0.3563 0.0299 -0.0446 0.0350 122 ASN A CA 870 C C . ASN A 122 ? 0.3444 0.4241 0.3459 0.0263 -0.0458 0.0336 122 ASN A C 871 O O . ASN A 122 ? 0.3306 0.4195 0.3338 0.0251 -0.0466 0.0324 122 ASN A O 872 C CB . ASN A 122 ? 0.3844 0.4566 0.3888 0.0358 -0.0450 0.0374 122 ASN A CB 873 C CG . ASN A 122 ? 0.4017 0.4634 0.4063 0.0384 -0.0439 0.0391 122 ASN A CG 874 O OD1 . ASN A 122 ? 0.4571 0.5169 0.4634 0.0412 -0.0436 0.0393 122 ASN A OD1 875 N ND2 . ASN A 122 ? 0.4076 0.4624 0.4100 0.0374 -0.0433 0.0403 122 ASN A ND2 876 N N . GLU A 123 ? 0.3510 0.4274 0.3485 0.0242 -0.0460 0.0340 123 GLU A N 877 C CA . GLU A 123 ? 0.3515 0.4347 0.3459 0.0205 -0.0473 0.0329 123 GLU A CA 878 C C . GLU A 123 ? 0.3683 0.4512 0.3601 0.0226 -0.0480 0.0347 123 GLU A C 879 O O . GLU A 123 ? 0.3530 0.4278 0.3438 0.0252 -0.0470 0.0364 123 GLU A O 880 C CB . GLU A 123 ? 0.3454 0.4235 0.3354 0.0144 -0.0469 0.0307 123 GLU A CB 881 C CG . GLU A 123 ? 0.3425 0.4221 0.3345 0.0114 -0.0465 0.0287 123 GLU A CG 882 C CD . GLU A 123 ? 0.3393 0.4123 0.3258 0.0056 -0.0459 0.0267 123 GLU A CD 883 O OE1 . GLU A 123 ? 0.3395 0.4023 0.3225 0.0058 -0.0448 0.0272 123 GLU A OE1 884 O OE2 . GLU A 123 ? 0.3307 0.4087 0.3160 0.0009 -0.0466 0.0248 123 GLU A OE2 885 N N . SER A 124 ? 0.3958 0.4878 0.3861 0.0212 -0.0496 0.0344 124 SER A N 886 C CA . SER A 124 ? 0.4104 0.5039 0.3982 0.0232 -0.0505 0.0361 124 SER A CA 887 C C . SER A 124 ? 0.4140 0.5021 0.3952 0.0185 -0.0506 0.0351 124 SER A C 888 O O . SER A 124 ? 0.3980 0.4919 0.3760 0.0142 -0.0520 0.0337 124 SER A O 889 C CB . SER A 124 ? 0.4383 0.5456 0.4280 0.0245 -0.0524 0.0365 124 SER A CB 890 O OG . SER A 124 ? 0.4797 0.5916 0.4746 0.0298 -0.0521 0.0376 124 SER A OG 891 N N . PHE A 125 ? 0.4288 0.5058 0.4075 0.0194 -0.0491 0.0359 125 PHE A N 892 C CA . PHE A 125 ? 0.4363 0.5069 0.4079 0.0160 -0.0489 0.0352 125 PHE A CA 893 C C . PHE A 125 ? 0.4653 0.5394 0.4344 0.0178 -0.0501 0.0367 125 PHE A C 894 O O . PHE A 125 ? 0.4729 0.5503 0.4456 0.0228 -0.0503 0.0389 125 PHE A O 895 C CB . PHE A 125 ? 0.4362 0.4949 0.4061 0.0172 -0.0468 0.0360 125 PHE A CB 896 C CG . PHE A 125 ? 0.4118 0.4657 0.3819 0.0144 -0.0457 0.0342 125 PHE A CG 897 C CD1 . PHE A 125 ? 0.4023 0.4570 0.3786 0.0163 -0.0450 0.0344 125 PHE A CD1 898 C CD2 . PHE A 125 ? 0.4129 0.4611 0.3764 0.0099 -0.0453 0.0322 125 PHE A CD2 899 C CE1 . PHE A 125 ? 0.3900 0.4405 0.3665 0.0137 -0.0440 0.0327 125 PHE A CE1 900 C CE2 . PHE A 125 ? 0.4111 0.4546 0.3744 0.0075 -0.0442 0.0306 125 PHE A CE2 901 C CZ . PHE A 125 ? 0.3897 0.4348 0.3598 0.0094 -0.0436 0.0309 125 PHE A CZ 902 N N . ASN A 126 ? 0.4956 0.5687 0.4580 0.0138 -0.0510 0.0355 126 ASN A N 903 C CA . ASN A 126 ? 0.5291 0.6049 0.4883 0.0153 -0.0521 0.0368 126 ASN A CA 904 C C . ASN A 126 ? 0.5030 0.5682 0.4580 0.0178 -0.0506 0.0384 126 ASN A C 905 O O . ASN A 126 ? 0.4878 0.5460 0.4354 0.0148 -0.0502 0.0373 126 ASN A O 906 C CB . ASN A 126 ? 0.6016 0.6822 0.5551 0.0094 -0.0540 0.0349 126 ASN A CB 907 C CG . ASN A 126 ? 0.6855 0.7676 0.6344 0.0103 -0.0552 0.0360 126 ASN A CG 908 O OD1 . ASN A 126 ? 0.6752 0.7584 0.6268 0.0157 -0.0550 0.0384 126 ASN A OD1 909 N ND2 . ASN A 126 ? 0.8221 0.9033 0.7632 0.0048 -0.0564 0.0342 126 ASN A ND2 910 N N . TRP A 127 ? 0.4714 0.5355 0.4307 0.0233 -0.0497 0.0410 127 TRP A N 911 C CA . TRP A 127 ? 0.4815 0.5373 0.4377 0.0260 -0.0482 0.0430 127 TRP A CA 912 C C . TRP A 127 ? 0.5042 0.5629 0.4579 0.0284 -0.0492 0.0448 127 TRP A C 913 O O . TRP A 127 ? 0.5045 0.5615 0.4602 0.0329 -0.0485 0.0474 127 TRP A O 914 C CB . TRP A 127 ? 0.4704 0.5222 0.4320 0.0299 -0.0465 0.0450 127 TRP A CB 915 C CG . TRP A 127 ? 0.4486 0.4972 0.4127 0.0278 -0.0455 0.0435 127 TRP A CG 916 C CD1 . TRP A 127 ? 0.4425 0.4932 0.4130 0.0292 -0.0453 0.0436 127 TRP A CD1 917 C CD2 . TRP A 127 ? 0.4550 0.4970 0.4147 0.0241 -0.0444 0.0415 127 TRP A CD2 918 N NE1 . TRP A 127 ? 0.4268 0.4733 0.3976 0.0265 -0.0442 0.0420 127 TRP A NE1 919 C CE2 . TRP A 127 ? 0.4383 0.4796 0.4029 0.0235 -0.0437 0.0407 127 TRP A CE2 920 C CE3 . TRP A 127 ? 0.4564 0.4925 0.4081 0.0216 -0.0440 0.0405 127 TRP A CE3 921 C CZ2 . TRP A 127 ? 0.4427 0.4783 0.4046 0.0205 -0.0426 0.0389 127 TRP A CZ2 922 C CZ3 . TRP A 127 ? 0.4619 0.4916 0.4105 0.0188 -0.0428 0.0387 127 TRP A CZ3 923 C CH2 . TRP A 127 ? 0.4600 0.4897 0.4138 0.0183 -0.0421 0.0379 127 TRP A CH2 924 N N . THR A 128 ? 0.5259 0.5889 0.4750 0.0252 -0.0509 0.0433 128 THR A N 925 C CA . THR A 128 ? 0.5463 0.6124 0.4923 0.0271 -0.0521 0.0447 128 THR A CA 926 C C . THR A 128 ? 0.5339 0.5903 0.4742 0.0287 -0.0505 0.0461 128 THR A C 927 O O . THR A 128 ? 0.5484 0.5969 0.4829 0.0261 -0.0495 0.0447 128 THR A O 928 C CB . THR A 128 ? 0.5916 0.6642 0.5330 0.0222 -0.0544 0.0426 128 THR A CB 929 O OG1 . THR A 128 ? 0.6205 0.7045 0.5680 0.0216 -0.0559 0.0420 128 THR A OG1 930 C CG2 . THR A 128 ? 0.5901 0.6646 0.5269 0.0236 -0.0556 0.0439 128 THR A CG2 931 N N . GLY A 129 ? 0.5327 0.5897 0.4744 0.0334 -0.0503 0.0489 129 GLY A N 932 C CA . GLY A 129 ? 0.5325 0.5822 0.4688 0.0354 -0.0489 0.0506 129 GLY A CA 933 C C . GLY A 129 ? 0.5303 0.5732 0.4691 0.0385 -0.0464 0.0527 129 GLY A C 934 O O . GLY A 129 ? 0.5297 0.5671 0.4643 0.0403 -0.0451 0.0543 129 GLY A O 935 N N . VAL A 130 ? 0.5035 0.5470 0.4489 0.0390 -0.0458 0.0528 130 VAL A N 936 C CA . VAL A 130 ? 0.4801 0.5181 0.4284 0.0414 -0.0437 0.0550 130 VAL A CA 937 C C . VAL A 130 ? 0.4654 0.5068 0.4207 0.0443 -0.0439 0.0569 130 VAL A C 938 O O . VAL A 130 ? 0.4723 0.5200 0.4305 0.0445 -0.0456 0.0560 130 VAL A O 939 C CB . VAL A 130 ? 0.4724 0.5055 0.4209 0.0388 -0.0423 0.0533 130 VAL A CB 940 C CG1 . VAL A 130 ? 0.4758 0.5033 0.4160 0.0366 -0.0416 0.0518 130 VAL A CG1 941 C CG2 . VAL A 130 ? 0.4573 0.4946 0.4099 0.0362 -0.0434 0.0508 130 VAL A CG2 942 N N . THR A 131 ? 0.4524 0.4894 0.4096 0.0467 -0.0423 0.0595 131 THR A N 943 C CA . THR A 131 ? 0.4610 0.4986 0.4238 0.0490 -0.0423 0.0613 131 THR A CA 944 C C . THR A 131 ? 0.4589 0.4945 0.4255 0.0469 -0.0416 0.0598 131 THR A C 945 O O . THR A 131 ? 0.4302 0.4614 0.3955 0.0451 -0.0402 0.0594 131 THR A O 946 C CB . THR A 131 ? 0.4839 0.5175 0.4465 0.0517 -0.0410 0.0650 131 THR A CB 947 O OG1 . THR A 131 ? 0.4949 0.5299 0.4535 0.0536 -0.0414 0.0664 131 THR A OG1 948 C CG2 . THR A 131 ? 0.4840 0.5169 0.4509 0.0538 -0.0411 0.0668 131 THR A CG2 949 N N . GLN A 132 ? 0.4458 0.4846 0.4164 0.0475 -0.0425 0.0591 132 GLN A N 950 C CA . GLN A 132 ? 0.4365 0.4737 0.4109 0.0458 -0.0420 0.0577 132 GLN A CA 951 C C . GLN A 132 ? 0.4411 0.4739 0.4183 0.0478 -0.0412 0.0602 132 GLN A C 952 O O . GLN A 132 ? 0.4221 0.4537 0.3986 0.0505 -0.0411 0.0629 132 GLN A O 953 C CB . GLN A 132 ? 0.4288 0.4723 0.4056 0.0452 -0.0436 0.0553 132 GLN A CB 954 C CG . GLN A 132 ? 0.4300 0.4782 0.4038 0.0421 -0.0447 0.0526 132 GLN A CG 955 C CD . GLN A 132 ? 0.4532 0.5086 0.4300 0.0410 -0.0460 0.0504 132 GLN A CD 956 O OE1 . GLN A 132 ? 0.4459 0.5005 0.4262 0.0405 -0.0455 0.0495 132 GLN A OE1 957 N NE2 . GLN A 132 ? 0.4334 0.4964 0.4087 0.0406 -0.0477 0.0495 132 GLN A NE2 958 N N . ASN A 133 ? 0.4228 0.4531 0.4029 0.0462 -0.0405 0.0592 133 ASN A N 959 C CA . ASN A 133 ? 0.4290 0.4551 0.4117 0.0474 -0.0400 0.0611 133 ASN A CA 960 C C . ASN A 133 ? 0.4140 0.4352 0.3955 0.0478 -0.0388 0.0644 133 ASN A C 961 O O . ASN A 133 ? 0.4020 0.4203 0.3839 0.0496 -0.0388 0.0668 133 ASN A O 962 C CB . ASN A 133 ? 0.4601 0.4882 0.4438 0.0507 -0.0412 0.0616 133 ASN A CB 963 C CG . ASN A 133 ? 0.5093 0.5432 0.4949 0.0504 -0.0424 0.0587 133 ASN A CG 964 O OD1 . ASN A 133 ? 0.4732 0.5090 0.4595 0.0473 -0.0423 0.0561 133 ASN A OD1 965 N ND2 . ASN A 133 ? 0.5923 0.6291 0.5783 0.0540 -0.0434 0.0591 133 ASN A ND2 966 N N . GLY A 134 ? 0.4106 0.4309 0.3906 0.0461 -0.0376 0.0647 134 GLY A N 967 C CA . GLY A 134 ? 0.4229 0.4397 0.4023 0.0462 -0.0362 0.0679 134 GLY A CA 968 C C . GLY A 134 ? 0.4272 0.4403 0.4096 0.0449 -0.0358 0.0689 134 GLY A C 969 O O . GLY A 134 ? 0.4136 0.4264 0.3983 0.0433 -0.0359 0.0666 134 GLY A O 970 N N . THR A 135 ? 0.4244 0.4346 0.4065 0.0454 -0.0353 0.0723 135 THR A N 971 C CA . THR A 135 ? 0.4433 0.4495 0.4274 0.0437 -0.0350 0.0737 135 THR A CA 972 C C . THR A 135 ? 0.4512 0.4565 0.4350 0.0421 -0.0335 0.0770 135 THR A C 973 O O . THR A 135 ? 0.4414 0.4490 0.4234 0.0430 -0.0327 0.0784 135 THR A O 974 C CB . THR A 135 ? 0.4611 0.4637 0.4445 0.0454 -0.0360 0.0748 135 THR A CB 975 O OG1 . THR A 135 ? 0.4603 0.4622 0.4408 0.0474 -0.0360 0.0778 135 THR A OG1 976 C CG2 . THR A 135 ? 0.4623 0.4671 0.4462 0.0475 -0.0373 0.0717 135 THR A CG2 977 N N . SER A 136 ? 0.4489 0.4512 0.4345 0.0397 -0.0333 0.0782 136 SER A N 978 C CA . SER A 136 ? 0.4542 0.4568 0.4401 0.0375 -0.0320 0.0814 136 SER A CA 979 C C . SER A 136 ? 0.4714 0.4691 0.4576 0.0352 -0.0324 0.0836 136 SER A C 980 O O . SER A 136 ? 0.4528 0.4468 0.4397 0.0345 -0.0334 0.0818 136 SER A O 981 C CB . SER A 136 ? 0.4583 0.4641 0.4461 0.0360 -0.0309 0.0801 136 SER A CB 982 O OG . SER A 136 ? 0.4522 0.4593 0.4410 0.0338 -0.0298 0.0833 136 SER A OG 983 N N . SER A 137 ? 0.4721 0.4697 0.4573 0.0337 -0.0317 0.0875 137 SER A N 984 C CA . SER A 137 ? 0.4821 0.4749 0.4667 0.0304 -0.0321 0.0900 137 SER A CA 985 C C . SER A 137 ? 0.4818 0.4755 0.4694 0.0269 -0.0318 0.0893 137 SER A C 986 O O . SER A 137 ? 0.4810 0.4700 0.4682 0.0239 -0.0324 0.0903 137 SER A O 987 C CB . SER A 137 ? 0.4843 0.4779 0.4671 0.0292 -0.0313 0.0946 137 SER A CB 988 O OG . SER A 137 ? 0.4821 0.4826 0.4670 0.0281 -0.0298 0.0961 137 SER A OG 989 N N . ALA A 138 ? 0.4707 0.4701 0.4608 0.0274 -0.0309 0.0876 138 ALA A N 990 C CA . ALA A 138 ? 0.4737 0.4745 0.4666 0.0248 -0.0306 0.0865 138 ALA A CA 991 C C . ALA A 138 ? 0.4653 0.4623 0.4591 0.0248 -0.0317 0.0826 138 ALA A C 992 O O . ALA A 138 ? 0.4708 0.4680 0.4668 0.0225 -0.0316 0.0815 138 ALA A O 993 C CB . ALA A 138 ? 0.4499 0.4574 0.4441 0.0259 -0.0291 0.0861 138 ALA A CB 994 N N . CYS A 139 ? 0.4532 0.4471 0.4454 0.0275 -0.0327 0.0806 139 CYS A N 995 C CA . CYS A 139 ? 0.4603 0.4516 0.4534 0.0281 -0.0336 0.0770 139 CYS A CA 996 C C . CYS A 139 ? 0.4792 0.4649 0.4697 0.0300 -0.0348 0.0770 139 CYS A C 997 O O . CYS A 139 ? 0.4903 0.4771 0.4801 0.0332 -0.0354 0.0751 139 CYS A O 998 C CB . CYS A 139 ? 0.4587 0.4546 0.4529 0.0301 -0.0334 0.0737 139 CYS A CB 999 S SG . CYS A 139 ? 0.4502 0.4447 0.4461 0.0303 -0.0343 0.0692 139 CYS A SG 1000 N N . LYS A 140 ? 0.4930 0.4726 0.4814 0.0279 -0.0353 0.0792 140 LYS A N 1001 C CA . LYS A 140 ? 0.5256 0.4982 0.5101 0.0300 -0.0363 0.0796 140 LYS A CA 1002 C C . LYS A 140 ? 0.5266 0.4960 0.5111 0.0315 -0.0371 0.0763 140 LYS A C 1003 O O . LYS A 140 ? 0.5144 0.4830 0.5008 0.0289 -0.0371 0.0749 140 LYS A O 1004 C CB . LYS A 140 ? 0.5415 0.5070 0.5224 0.0268 -0.0365 0.0832 140 LYS A CB 1005 C CG . LYS A 140 ? 0.5622 0.5310 0.5431 0.0245 -0.0356 0.0870 140 LYS A CG 1006 C CD . LYS A 140 ? 0.5776 0.5438 0.5545 0.0271 -0.0357 0.0892 140 LYS A CD 1007 C CE . LYS A 140 ? 0.5983 0.5663 0.5744 0.0240 -0.0349 0.0935 140 LYS A CE 1008 N NZ . LYS A 140 ? 0.6269 0.5948 0.6001 0.0273 -0.0348 0.0953 140 LYS A NZ 1009 N N . ARG A 141 ? 0.5070 0.4752 0.4894 0.0358 -0.0378 0.0752 141 ARG A N 1010 C CA . ARG A 141 ? 0.5356 0.5007 0.5172 0.0381 -0.0386 0.0725 141 ARG A CA 1011 C C . ARG A 141 ? 0.5930 0.5499 0.5687 0.0411 -0.0392 0.0742 141 ARG A C 1012 O O . ARG A 141 ? 0.5848 0.5431 0.5586 0.0446 -0.0394 0.0752 141 ARG A O 1013 C CB . ARG A 141 ? 0.5077 0.4808 0.4924 0.0411 -0.0387 0.0693 141 ARG A CB 1014 C CG . ARG A 141 ? 0.5041 0.4759 0.4883 0.0440 -0.0394 0.0667 141 ARG A CG 1015 C CD . ARG A 141 ? 0.4823 0.4632 0.4701 0.0456 -0.0395 0.0636 141 ARG A CD 1016 N NE . ARG A 141 ? 0.4684 0.4523 0.4599 0.0422 -0.0390 0.0613 141 ARG A NE 1017 C CZ . ARG A 141 ? 0.4633 0.4524 0.4574 0.0398 -0.0384 0.0608 141 ARG A CZ 1018 N NH1 . ARG A 141 ? 0.4492 0.4414 0.4427 0.0401 -0.0381 0.0623 141 ARG A NH1 1019 N NH2 . ARG A 141 ? 0.4494 0.4403 0.4462 0.0371 -0.0380 0.0587 141 ARG A NH2 1020 N N . LYS A 142 ? 0.6456 0.5934 0.6177 0.0398 -0.0396 0.0745 142 LYS A N 1021 C CA . LYS A 142 ? 0.6993 0.6367 0.6642 0.0421 -0.0401 0.0764 142 LYS A CA 1022 C C . LYS A 142 ? 0.7057 0.6416 0.6678 0.0415 -0.0399 0.0800 142 LYS A C 1023 O O . LYS A 142 ? 0.7173 0.6514 0.6757 0.0459 -0.0402 0.0810 142 LYS A O 1024 C CB . LYS A 142 ? 0.7245 0.6619 0.6874 0.0486 -0.0406 0.0744 142 LYS A CB 1025 C CG . LYS A 142 ? 0.7576 0.6947 0.7219 0.0494 -0.0408 0.0712 142 LYS A CG 1026 C CD . LYS A 142 ? 0.7900 0.7145 0.7487 0.0472 -0.0411 0.0718 142 LYS A CD 1027 C CE . LYS A 142 ? 0.7942 0.7196 0.7557 0.0459 -0.0411 0.0688 142 LYS A CE 1028 N NZ . LYS A 142 ? 0.8046 0.7328 0.7659 0.0520 -0.0413 0.0663 142 LYS A NZ 1029 N N . SER A 143 ? 0.7054 0.6428 0.6694 0.0362 -0.0394 0.0821 143 SER A N 1030 C CA . SER A 143 ? 0.7199 0.6562 0.6815 0.0345 -0.0391 0.0859 143 SER A CA 1031 C C . SER A 143 ? 0.6906 0.6351 0.6543 0.0377 -0.0386 0.0865 143 SER A C 1032 O O . SER A 143 ? 0.7269 0.6713 0.6889 0.0365 -0.0382 0.0897 143 SER A O 1033 C CB . SER A 143 ? 0.7478 0.6712 0.7008 0.0347 -0.0396 0.0883 143 SER A CB 1034 O OG . SER A 143 ? 0.7686 0.6839 0.7190 0.0305 -0.0401 0.0883 143 SER A OG 1035 N N . ASN A 144 ? 0.6328 0.5847 0.6002 0.0414 -0.0387 0.0834 144 ASN A N 1036 C CA . ASN A 144 ? 0.6015 0.5616 0.5709 0.0438 -0.0383 0.0836 144 ASN A CA 1037 C C . ASN A 144 ? 0.5729 0.5419 0.5480 0.0414 -0.0375 0.0822 144 ASN A C 1038 O O . ASN A 144 ? 0.5250 0.4954 0.5032 0.0395 -0.0375 0.0799 144 ASN A O 1039 C CB . ASN A 144 ? 0.6288 0.5914 0.5976 0.0494 -0.0390 0.0813 144 ASN A CB 1040 C CG . ASN A 144 ? 0.6714 0.6261 0.6338 0.0532 -0.0396 0.0832 144 ASN A CG 1041 O OD1 . ASN A 144 ? 0.6779 0.6249 0.6359 0.0513 -0.0395 0.0863 144 ASN A OD1 1042 N ND2 . ASN A 144 ? 0.7050 0.6616 0.6665 0.0584 -0.0403 0.0814 144 ASN A ND2 1043 N N . ASN A 145 ? 0.5135 0.4878 0.4893 0.0418 -0.0369 0.0836 145 ASN A N 1044 C CA . ASN A 145 ? 0.4878 0.4701 0.4677 0.0406 -0.0361 0.0822 145 ASN A CA 1045 C C . ASN A 145 ? 0.4588 0.4450 0.4408 0.0426 -0.0367 0.0781 145 ASN A C 1046 O O . ASN A 145 ? 0.4312 0.4178 0.4118 0.0462 -0.0376 0.0770 145 ASN A O 1047 C CB . ASN A 145 ? 0.4913 0.4780 0.4703 0.0419 -0.0354 0.0841 145 ASN A CB 1048 C CG . ASN A 145 ? 0.4948 0.4799 0.4724 0.0394 -0.0346 0.0882 145 ASN A CG 1049 O OD1 . ASN A 145 ? 0.4935 0.4736 0.4703 0.0363 -0.0346 0.0899 145 ASN A OD1 1050 N ND2 . ASN A 145 ? 0.4928 0.4821 0.4697 0.0404 -0.0337 0.0900 145 ASN A ND2 1051 N N . SER A 146 ? 0.4414 0.4309 0.4268 0.0404 -0.0362 0.0760 146 SER A N 1052 C CA . SER A 146 ? 0.4140 0.4071 0.4014 0.0415 -0.0367 0.0721 146 SER A CA 1053 C C . SER A 146 ? 0.3929 0.3906 0.3827 0.0393 -0.0358 0.0705 146 SER A C 1054 O O . SER A 146 ? 0.3660 0.3656 0.3553 0.0384 -0.0348 0.0723 146 SER A O 1055 C CB . SER A 146 ? 0.4240 0.4127 0.4117 0.0414 -0.0374 0.0706 146 SER A CB 1056 O OG . SER A 146 ? 0.4085 0.4009 0.3974 0.0435 -0.0381 0.0674 146 SER A OG 1057 N N . PHE A 147 ? 0.3776 0.3770 0.3693 0.0387 -0.0361 0.0672 147 PHE A N 1058 C CA . PHE A 147 ? 0.3592 0.3620 0.3522 0.0369 -0.0353 0.0654 147 PHE A CA 1059 C C . PHE A 147 ? 0.3404 0.3431 0.3355 0.0357 -0.0357 0.0622 147 PHE A C 1060 O O . PHE A 147 ? 0.3397 0.3406 0.3352 0.0369 -0.0366 0.0614 147 PHE A O 1061 C CB . PHE A 147 ? 0.3537 0.3609 0.3449 0.0384 -0.0354 0.0642 147 PHE A CB 1062 C CG . PHE A 147 ? 0.3495 0.3586 0.3400 0.0369 -0.0343 0.0633 147 PHE A CG 1063 C CD1 . PHE A 147 ? 0.3481 0.3565 0.3379 0.0363 -0.0330 0.0659 147 PHE A CD1 1064 C CD2 . PHE A 147 ? 0.3499 0.3613 0.3397 0.0363 -0.0346 0.0600 147 PHE A CD2 1065 C CE1 . PHE A 147 ? 0.3455 0.3552 0.3337 0.0357 -0.0318 0.0651 147 PHE A CE1 1066 C CE2 . PHE A 147 ? 0.3442 0.3559 0.3320 0.0352 -0.0335 0.0592 147 PHE A CE2 1067 C CZ . PHE A 147 ? 0.3487 0.3593 0.3355 0.0352 -0.0321 0.0617 147 PHE A CZ 1068 N N . PHE A 148 ? 0.3170 0.3215 0.3130 0.0338 -0.0350 0.0605 148 PHE A N 1069 C CA . PHE A 148 ? 0.3122 0.3171 0.3099 0.0326 -0.0353 0.0573 148 PHE A CA 1070 C C . PHE A 148 ? 0.3162 0.3240 0.3139 0.0344 -0.0365 0.0552 148 PHE A C 1071 O O . PHE A 148 ? 0.3194 0.3308 0.3155 0.0355 -0.0368 0.0547 148 PHE A O 1072 C CB . PHE A 148 ? 0.3050 0.3117 0.3022 0.0309 -0.0343 0.0557 148 PHE A CB 1073 C CG . PHE A 148 ? 0.3067 0.3119 0.3041 0.0295 -0.0331 0.0577 148 PHE A CG 1074 C CD1 . PHE A 148 ? 0.3125 0.3154 0.3121 0.0276 -0.0329 0.0579 148 PHE A CD1 1075 C CD2 . PHE A 148 ? 0.3182 0.3246 0.3133 0.0302 -0.0321 0.0594 148 PHE A CD2 1076 C CE1 . PHE A 148 ? 0.3201 0.3231 0.3200 0.0263 -0.0317 0.0599 148 PHE A CE1 1077 C CE2 . PHE A 148 ? 0.3269 0.3333 0.3223 0.0293 -0.0308 0.0615 148 PHE A CE2 1078 C CZ . PHE A 148 ? 0.3265 0.3316 0.3245 0.0273 -0.0306 0.0618 148 PHE A CZ 1079 N N . SER A 149 ? 0.3114 0.3179 0.3106 0.0348 -0.0371 0.0539 149 SER A N 1080 C CA . SER A 149 ? 0.3180 0.3282 0.3174 0.0370 -0.0381 0.0522 149 SER A CA 1081 C C . SER A 149 ? 0.3081 0.3244 0.3076 0.0359 -0.0384 0.0495 149 SER A C 1082 O O . SER A 149 ? 0.2939 0.3152 0.2929 0.0376 -0.0393 0.0489 149 SER A O 1083 C CB . SER A 149 ? 0.3218 0.3295 0.3225 0.0378 -0.0385 0.0513 149 SER A CB 1084 O OG . SER A 149 ? 0.3092 0.3173 0.3117 0.0352 -0.0381 0.0489 149 SER A OG 1085 N N . ARG A 150 ? 0.2882 0.3041 0.2879 0.0329 -0.0376 0.0479 150 ARG A N 1086 C CA . ARG A 150 ? 0.2881 0.3085 0.2871 0.0311 -0.0379 0.0452 150 ARG A CA 1087 C C . ARG A 150 ? 0.2873 0.3084 0.2828 0.0302 -0.0376 0.0454 150 ARG A C 1088 O O . ARG A 150 ? 0.2805 0.3042 0.2741 0.0282 -0.0378 0.0432 150 ARG A O 1089 C CB . ARG A 150 ? 0.2823 0.3012 0.2825 0.0284 -0.0373 0.0430 150 ARG A CB 1090 C CG . ARG A 150 ? 0.2817 0.2991 0.2848 0.0293 -0.0375 0.0427 150 ARG A CG 1091 C CD . ARG A 150 ? 0.2921 0.3142 0.2961 0.0318 -0.0386 0.0421 150 ARG A CD 1092 N NE . ARG A 150 ? 0.2862 0.3076 0.2922 0.0325 -0.0388 0.0409 150 ARG A NE 1093 C CZ . ARG A 150 ? 0.2885 0.3137 0.2954 0.0353 -0.0395 0.0404 150 ARG A CZ 1094 N NH1 . ARG A 150 ? 0.2883 0.3189 0.2944 0.0378 -0.0403 0.0411 150 ARG A NH1 1095 N NH2 . ARG A 150 ? 0.2808 0.3048 0.2890 0.0360 -0.0394 0.0394 150 ARG A NH2 1096 N N . LEU A 151 ? 0.2921 0.3107 0.2863 0.0316 -0.0370 0.0481 151 LEU A N 1097 C CA . LEU A 151 ? 0.2932 0.3117 0.2836 0.0313 -0.0365 0.0486 151 LEU A CA 1098 C C . LEU A 151 ? 0.3023 0.3228 0.2914 0.0338 -0.0372 0.0506 151 LEU A C 1099 O O . LEU A 151 ? 0.3099 0.3302 0.3008 0.0360 -0.0377 0.0523 151 LEU A O 1100 C CB . LEU A 151 ? 0.2924 0.3066 0.2818 0.0306 -0.0349 0.0501 151 LEU A CB 1101 C CG . LEU A 151 ? 0.2892 0.3015 0.2790 0.0282 -0.0342 0.0482 151 LEU A CG 1102 C CD1 . LEU A 151 ? 0.2780 0.2872 0.2678 0.0283 -0.0327 0.0503 151 LEU A CD1 1103 C CD2 . LEU A 151 ? 0.2850 0.2978 0.2708 0.0264 -0.0342 0.0454 151 LEU A CD2 1104 N N . ASN A 152 ? 0.3152 0.3369 0.3004 0.0335 -0.0373 0.0502 152 ASN A N 1105 C CA . ASN A 152 ? 0.3224 0.3468 0.3059 0.0357 -0.0381 0.0516 152 ASN A CA 1106 C C . ASN A 152 ? 0.3317 0.3535 0.3111 0.0361 -0.0371 0.0532 152 ASN A C 1107 O O . ASN A 152 ? 0.3421 0.3632 0.3174 0.0346 -0.0368 0.0517 152 ASN A O 1108 C CB . ASN A 152 ? 0.3266 0.3567 0.3091 0.0349 -0.0396 0.0492 152 ASN A CB 1109 C CG . ASN A 152 ? 0.3363 0.3702 0.3177 0.0375 -0.0408 0.0507 152 ASN A CG 1110 O OD1 . ASN A 152 ? 0.3298 0.3613 0.3105 0.0398 -0.0403 0.0534 152 ASN A OD1 1111 N ND2 . ASN A 152 ? 0.3423 0.3826 0.3235 0.0371 -0.0423 0.0490 152 ASN A ND2 1112 N N . TRP A 153 ? 0.3516 0.3716 0.3316 0.0382 -0.0364 0.0564 153 TRP A N 1113 C CA . TRP A 153 ? 0.3679 0.3860 0.3444 0.0391 -0.0352 0.0584 153 TRP A CA 1114 C C . TRP A 153 ? 0.3793 0.3999 0.3524 0.0406 -0.0361 0.0587 153 TRP A C 1115 O O . TRP A 153 ? 0.3859 0.4078 0.3600 0.0427 -0.0368 0.0607 153 TRP A O 1116 C CB . TRP A 153 ? 0.3704 0.3865 0.3492 0.0403 -0.0343 0.0619 153 TRP A CB 1117 C CG . TRP A 153 ? 0.3777 0.3924 0.3536 0.0411 -0.0327 0.0643 153 TRP A CG 1118 C CD1 . TRP A 153 ? 0.3872 0.4015 0.3580 0.0415 -0.0319 0.0637 153 TRP A CD1 1119 C CD2 . TRP A 153 ? 0.3869 0.4006 0.3643 0.0415 -0.0315 0.0679 153 TRP A CD2 1120 N NE1 . TRP A 153 ? 0.3835 0.3970 0.3529 0.0428 -0.0303 0.0666 153 TRP A NE1 1121 C CE2 . TRP A 153 ? 0.3902 0.4039 0.3637 0.0427 -0.0299 0.0693 153 TRP A CE2 1122 C CE3 . TRP A 153 ? 0.4009 0.4134 0.3819 0.0410 -0.0315 0.0700 153 TRP A CE3 1123 C CZ2 . TRP A 153 ? 0.4075 0.4217 0.3816 0.0433 -0.0285 0.0729 153 TRP A CZ2 1124 C CZ3 . TRP A 153 ? 0.4118 0.4242 0.3930 0.0409 -0.0302 0.0736 153 TRP A CZ3 1125 C CH2 . TRP A 153 ? 0.4209 0.4348 0.3992 0.0421 -0.0287 0.0751 153 TRP A CH2 1126 N N . LEU A 154 ? 0.3848 0.4052 0.3531 0.0394 -0.0362 0.0568 154 LEU A N 1127 C CA . LEU A 154 ? 0.3946 0.4171 0.3586 0.0402 -0.0371 0.0567 154 LEU A CA 1128 C C . LEU A 154 ? 0.4073 0.4271 0.3675 0.0423 -0.0358 0.0594 154 LEU A C 1129 O O . LEU A 154 ? 0.3836 0.3999 0.3415 0.0421 -0.0341 0.0598 154 LEU A O 1130 C CB . LEU A 154 ? 0.4055 0.4283 0.3650 0.0373 -0.0379 0.0534 154 LEU A CB 1131 C CG . LEU A 154 ? 0.4019 0.4277 0.3644 0.0346 -0.0390 0.0505 154 LEU A CG 1132 C CD1 . LEU A 154 ? 0.4189 0.4440 0.3756 0.0311 -0.0396 0.0475 154 LEU A CD1 1133 C CD2 . LEU A 154 ? 0.3973 0.4294 0.3643 0.0360 -0.0407 0.0508 154 LEU A CD2 1134 N N . THR A 155 ? 0.4143 0.4362 0.3737 0.0445 -0.0364 0.0613 155 THR A N 1135 C CA . THR A 155 ? 0.4251 0.4453 0.3808 0.0467 -0.0353 0.0640 155 THR A CA 1136 C C . THR A 155 ? 0.4325 0.4547 0.3835 0.0474 -0.0366 0.0634 155 THR A C 1137 O O . THR A 155 ? 0.4100 0.4358 0.3615 0.0462 -0.0384 0.0612 155 THR A O 1138 C CB . THR A 155 ? 0.4201 0.4401 0.3795 0.0488 -0.0345 0.0677 155 THR A CB 1139 O OG1 . THR A 155 ? 0.4201 0.4429 0.3824 0.0499 -0.0362 0.0681 155 THR A OG1 1140 C CG2 . THR A 155 ? 0.4172 0.4353 0.3807 0.0477 -0.0333 0.0685 155 THR A CG2 1141 N N . HIS A 156 ? 0.4601 0.4806 0.4066 0.0494 -0.0356 0.0654 156 HIS A N 1142 C CA . HIS A 156 ? 0.4785 0.5005 0.4198 0.0500 -0.0369 0.0648 156 HIS A CA 1143 C C . HIS A 156 ? 0.4806 0.5077 0.4252 0.0512 -0.0387 0.0655 156 HIS A C 1144 O O . HIS A 156 ? 0.4786 0.5067 0.4285 0.0526 -0.0387 0.0673 156 HIS A O 1145 C CB . HIS A 156 ? 0.4854 0.5045 0.4213 0.0524 -0.0353 0.0671 156 HIS A CB 1146 C CG . HIS A 156 ? 0.4848 0.5052 0.4238 0.0553 -0.0346 0.0711 156 HIS A CG 1147 N ND1 . HIS A 156 ? 0.4988 0.5224 0.4390 0.0568 -0.0360 0.0723 156 HIS A ND1 1148 C CD2 . HIS A 156 ? 0.4931 0.5119 0.4336 0.0568 -0.0325 0.0743 156 HIS A CD2 1149 C CE1 . HIS A 156 ? 0.4989 0.5220 0.4410 0.0590 -0.0349 0.0760 156 HIS A CE1 1150 N NE2 . HIS A 156 ? 0.5031 0.5236 0.4455 0.0588 -0.0328 0.0773 156 HIS A NE2 1151 N N . LEU A 157 ? 0.5122 0.5422 0.4530 0.0507 -0.0404 0.0640 157 LEU A N 1152 C CA . LEU A 157 ? 0.5066 0.5421 0.4491 0.0526 -0.0422 0.0649 157 LEU A CA 1153 C C . LEU A 157 ? 0.5128 0.5479 0.4494 0.0543 -0.0424 0.0662 157 LEU A C 1154 O O . LEU A 157 ? 0.5128 0.5467 0.4432 0.0525 -0.0428 0.0644 157 LEU A O 1155 C CB . LEU A 157 ? 0.5061 0.5474 0.4497 0.0501 -0.0444 0.0618 157 LEU A CB 1156 C CG . LEU A 157 ? 0.5008 0.5493 0.4463 0.0522 -0.0465 0.0624 157 LEU A CG 1157 C CD1 . LEU A 157 ? 0.5121 0.5608 0.4631 0.0557 -0.0460 0.0649 157 LEU A CD1 1158 C CD2 . LEU A 157 ? 0.4872 0.5425 0.4333 0.0492 -0.0485 0.0594 157 LEU A CD2 1159 N N . LYS A 158 ? 0.6334 0.6579 0.4364 0.0469 -0.1057 0.0307 158 LYS A N 1160 C CA . LYS A 158 ? 0.6698 0.6957 0.4574 0.0472 -0.1079 0.0332 158 LYS A CA 1161 C C . LYS A 158 ? 0.6601 0.6948 0.4439 0.0443 -0.1003 0.0312 158 LYS A C 1162 O O . LYS A 158 ? 0.6494 0.6903 0.4280 0.0459 -0.1013 0.0273 158 LYS A O 1163 C CB . LYS A 158 ? 0.6980 0.7253 0.4855 0.0525 -0.1158 0.0279 158 LYS A CB 1164 C CG . LYS A 158 ? 0.7330 0.7532 0.5271 0.0563 -0.1238 0.0275 158 LYS A CG 1165 C CD . LYS A 158 ? 0.7797 0.7891 0.5634 0.0555 -0.1287 0.0370 158 LYS A CD 1166 C CE . LYS A 158 ? 0.8046 0.8078 0.5924 0.0605 -0.1388 0.0355 158 LYS A CE 1167 N NZ . LYS A 158 ? 0.8116 0.8159 0.6178 0.0623 -0.1387 0.0291 158 LYS A NZ 1168 N N . PHE A 159 ? 0.6252 0.6609 0.4128 0.0402 -0.0929 0.0332 159 PHE A N 1169 C CA . PHE A 159 ? 0.6207 0.6646 0.4069 0.0373 -0.0853 0.0309 159 PHE A CA 1170 C C . PHE A 159 ? 0.6024 0.6552 0.3978 0.0397 -0.0841 0.0212 159 PHE A C 1171 O O . PHE A 159 ? 0.5747 0.6349 0.3669 0.0385 -0.0800 0.0182 159 PHE A O 1172 C CB . PHE A 159 ? 0.6571 0.7022 0.4263 0.0349 -0.0844 0.0361 159 PHE A CB 1173 C CG . PHE A 159 ? 0.6878 0.7238 0.4474 0.0321 -0.0858 0.0459 159 PHE A CG 1174 C CD1 . PHE A 159 ? 0.6872 0.7211 0.4480 0.0276 -0.0798 0.0506 159 PHE A CD1 1175 C CD2 . PHE A 159 ? 0.7118 0.7408 0.4616 0.0341 -0.0936 0.0505 159 PHE A CD2 1176 C CE1 . PHE A 159 ? 0.7199 0.7451 0.4724 0.0248 -0.0812 0.0598 159 PHE A CE1 1177 C CE2 . PHE A 159 ? 0.7278 0.7475 0.4690 0.0314 -0.0954 0.0599 159 PHE A CE2 1178 C CZ . PHE A 159 ? 0.7282 0.7460 0.4709 0.0267 -0.0890 0.0646 159 PHE A CZ 1179 N N . LYS A 160 ? 0.6025 0.6545 0.4099 0.0429 -0.0875 0.0160 160 LYS A N 1180 C CA . LYS A 160 ? 0.5935 0.6528 0.4123 0.0444 -0.0856 0.0071 160 LYS A CA 1181 C C . LYS A 160 ? 0.5605 0.6181 0.3940 0.0435 -0.0830 0.0050 160 LYS A C 1182 O O . LYS A 160 ? 0.5325 0.5838 0.3696 0.0439 -0.0857 0.0078 160 LYS A O 1183 C CB . LYS A 160 ? 0.6313 0.6931 0.4510 0.0490 -0.0922 0.0013 160 LYS A CB 1184 C CG . LYS A 160 ? 0.6773 0.7428 0.4833 0.0501 -0.0944 0.0016 160 LYS A CG 1185 C CD . LYS A 160 ? 0.7065 0.7771 0.5162 0.0545 -0.0993 -0.0063 160 LYS A CD 1186 C CE . LYS A 160 ? 0.7423 0.8180 0.5389 0.0554 -0.1006 -0.0069 160 LYS A CE 1187 N NZ . LYS A 160 ? 0.7482 0.8308 0.5427 0.0521 -0.0931 -0.0080 160 LYS A NZ 1188 N N . TYR A 161 ? 0.5450 0.6083 0.3866 0.0422 -0.0778 0.0000 161 TYR A N 1189 C CA . TYR A 161 ? 0.5290 0.5919 0.3846 0.0413 -0.0753 -0.0030 161 TYR A CA 1190 C C . TYR A 161 ? 0.5330 0.6028 0.3968 0.0430 -0.0751 -0.0116 161 TYR A C 1191 O O . TYR A 161 ? 0.5299 0.6044 0.3949 0.0414 -0.0705 -0.0141 161 TYR A O 1192 C CB . TYR A 161 ? 0.5182 0.5801 0.3749 0.0372 -0.0686 0.0007 161 TYR A CB 1193 C CG . TYR A 161 ? 0.4952 0.5549 0.3641 0.0359 -0.0663 -0.0003 161 TYR A CG 1194 C CD1 . TYR A 161 ? 0.4883 0.5519 0.3684 0.0363 -0.0652 -0.0070 161 TYR A CD1 1195 C CD2 . TYR A 161 ? 0.4960 0.5497 0.3650 0.0339 -0.0652 0.0054 161 TYR A CD2 1196 C CE1 . TYR A 161 ? 0.4610 0.5229 0.3515 0.0346 -0.0629 -0.0078 161 TYR A CE1 1197 C CE2 . TYR A 161 ? 0.4732 0.5254 0.3530 0.0326 -0.0631 0.0043 161 TYR A CE2 1198 C CZ . TYR A 161 ? 0.4714 0.5278 0.3615 0.0329 -0.0619 -0.0022 161 TYR A CZ 1199 O OH . TYR A 161 ? 0.4343 0.4893 0.3343 0.0312 -0.0596 -0.0031 161 TYR A OH 1200 N N . PRO A 162 ? 0.5525 0.6227 0.4218 0.0462 -0.0803 -0.0164 162 PRO A N 1201 C CA . PRO A 162 ? 0.5632 0.6398 0.4405 0.0477 -0.0803 -0.0247 162 PRO A CA 1202 C C . PRO A 162 ? 0.5568 0.6343 0.4464 0.0451 -0.0755 -0.0275 162 PRO A C 1203 O O . PRO A 162 ? 0.5834 0.6565 0.4772 0.0434 -0.0742 -0.0243 162 PRO A O 1204 C CB . PRO A 162 ? 0.5771 0.6532 0.4576 0.0516 -0.0873 -0.0284 162 PRO A CB 1205 C CG . PRO A 162 ? 0.5910 0.6601 0.4716 0.0514 -0.0895 -0.0232 162 PRO A CG 1206 C CD . PRO A 162 ? 0.5878 0.6529 0.4579 0.0486 -0.0863 -0.0149 162 PRO A CD 1207 N N . ALA A 163 ? 0.5447 0.6277 0.4396 0.0448 -0.0731 -0.0332 163 ALA A N 1208 C CA . ALA A 163 ? 0.5313 0.6149 0.4372 0.0421 -0.0688 -0.0358 163 ALA A CA 1209 C C . ALA A 163 ? 0.5173 0.5988 0.4329 0.0424 -0.0709 -0.0377 163 ALA A C 1210 O O . ALA A 163 ? 0.5267 0.6097 0.4450 0.0452 -0.0757 -0.0420 163 ALA A O 1211 C CB . ALA A 163 ? 0.5341 0.6236 0.4448 0.0424 -0.0676 -0.0424 163 ALA A CB 1212 N N . LEU A 164 ? 0.4761 0.5542 0.3965 0.0395 -0.0675 -0.0348 164 LEU A N 1213 C CA . LEU A 164 ? 0.4722 0.5489 0.4020 0.0392 -0.0686 -0.0369 164 LEU A CA 1214 C C . LEU A 164 ? 0.4498 0.5301 0.3902 0.0373 -0.0660 -0.0427 164 LEU A C 1215 O O . LEU A 164 ? 0.4318 0.5128 0.3729 0.0349 -0.0618 -0.0424 164 LEU A O 1216 C CB . LEU A 164 ? 0.4703 0.5419 0.4000 0.0369 -0.0665 -0.0310 164 LEU A CB 1217 C CG . LEU A 164 ? 0.4863 0.5533 0.4062 0.0383 -0.0691 -0.0247 164 LEU A CG 1218 C CD1 . LEU A 164 ? 0.4757 0.5380 0.3963 0.0356 -0.0662 -0.0192 164 LEU A CD1 1219 C CD2 . LEU A 164 ? 0.4865 0.5527 0.4063 0.0420 -0.0759 -0.0266 164 LEU A CD2 1220 N N . ASN A 165 ? 0.4394 0.5218 0.3880 0.0383 -0.0687 -0.0481 165 ASN A N 1221 C CA . ASN A 165 ? 0.4486 0.5340 0.4077 0.0361 -0.0664 -0.0535 165 ASN A CA 1222 C C . ASN A 165 ? 0.4533 0.5390 0.4208 0.0360 -0.0683 -0.0563 165 ASN A C 1223 O O . ASN A 165 ? 0.4535 0.5426 0.4258 0.0383 -0.0721 -0.0620 165 ASN A O 1224 C CB . ASN A 165 ? 0.4691 0.5592 0.4297 0.0378 -0.0681 -0.0594 165 ASN A CB 1225 C CG . ASN A 165 ? 0.4875 0.5802 0.4589 0.0351 -0.0658 -0.0647 165 ASN A CG 1226 O OD1 . ASN A 165 ? 0.4911 0.5819 0.4654 0.0314 -0.0613 -0.0627 165 ASN A OD1 1227 N ND2 . ASN A 165 ? 0.4758 0.5726 0.4534 0.0368 -0.0689 -0.0715 165 ASN A ND2 1228 N N . VAL A 166 ? 0.4264 0.5089 0.3957 0.0334 -0.0657 -0.0525 166 VAL A N 1229 C CA . VAL A 166 ? 0.4204 0.5027 0.3955 0.0338 -0.0677 -0.0540 166 VAL A CA 1230 C C . VAL A 166 ? 0.4150 0.4990 0.4000 0.0297 -0.0638 -0.0567 166 VAL A C 1231 O O . VAL A 166 ? 0.3899 0.4721 0.3747 0.0261 -0.0591 -0.0537 166 VAL A O 1232 C CB . VAL A 166 ? 0.4301 0.5073 0.3987 0.0346 -0.0687 -0.0474 166 VAL A CB 1233 C CG1 . VAL A 166 ? 0.4250 0.5020 0.4004 0.0351 -0.0709 -0.0493 166 VAL A CG1 1234 C CG2 . VAL A 166 ? 0.4496 0.5249 0.4077 0.0384 -0.0728 -0.0445 166 VAL A CG2 1235 N N . THR A 167 ? 0.4175 0.5052 0.4112 0.0302 -0.0660 -0.0626 167 THR A N 1236 C CA . THR A 167 ? 0.4286 0.5189 0.4318 0.0260 -0.0625 -0.0661 167 THR A CA 1237 C C . THR A 167 ? 0.4137 0.5044 0.4223 0.0253 -0.0627 -0.0666 167 THR A C 1238 O O . THR A 167 ? 0.4032 0.4935 0.4113 0.0289 -0.0673 -0.0672 167 THR A O 1239 C CB . THR A 167 ? 0.4707 0.5665 0.4815 0.0262 -0.0639 -0.0739 167 THR A CB 1240 O OG1 . THR A 167 ? 0.5361 0.6337 0.5542 0.0210 -0.0593 -0.0760 167 THR A OG1 1241 C CG2 . THR A 167 ? 0.4687 0.5680 0.4848 0.0295 -0.0689 -0.0793 167 THR A CG2 1242 N N . MET A 168 ? 0.3817 0.4730 0.3953 0.0205 -0.0580 -0.0665 168 MET A N 1243 C CA . MET A 168 ? 0.3787 0.4721 0.3991 0.0193 -0.0578 -0.0687 168 MET A CA 1244 C C . MET A 168 ? 0.3803 0.4776 0.4088 0.0139 -0.0532 -0.0725 168 MET A C 1245 O O . MET A 168 ? 0.3764 0.4714 0.4030 0.0098 -0.0486 -0.0686 168 MET A O 1246 C CB . MET A 168 ? 0.3777 0.4662 0.3930 0.0191 -0.0567 -0.0622 168 MET A CB 1247 C CG . MET A 168 ? 0.3688 0.4595 0.3907 0.0190 -0.0577 -0.0646 168 MET A CG 1248 S SD . MET A 168 ? 0.3752 0.4685 0.4013 0.0248 -0.0653 -0.0703 168 MET A SD 1249 C CE . MET A 168 ? 0.3718 0.4574 0.3855 0.0292 -0.0693 -0.0626 168 MET A CE 1250 N N . PRO A 169 ? 0.3817 0.4851 0.4192 0.0137 -0.0547 -0.0800 169 PRO A N 1251 C CA . PRO A 169 ? 0.3783 0.4857 0.4232 0.0080 -0.0502 -0.0836 169 PRO A CA 1252 C C . PRO A 169 ? 0.3559 0.4645 0.4042 0.0049 -0.0473 -0.0830 169 PRO A C 1253 O O . PRO A 169 ? 0.3604 0.4690 0.4091 0.0078 -0.0500 -0.0830 169 PRO A O 1254 C CB . PRO A 169 ? 0.3938 0.5078 0.4474 0.0094 -0.0531 -0.0923 169 PRO A CB 1255 C CG . PRO A 169 ? 0.3992 0.5133 0.4519 0.0155 -0.0591 -0.0937 169 PRO A CG 1256 C CD . PRO A 169 ? 0.3989 0.5058 0.4402 0.0185 -0.0605 -0.0857 169 PRO A CD 1257 N N . ASN A 170 ? 0.3507 0.4599 0.4010 -0.0010 -0.0420 -0.0823 170 ASN A N 1258 C CA . ASN A 170 ? 0.3525 0.4646 0.4071 -0.0048 -0.0389 -0.0831 170 ASN A CA 1259 C C . ASN A 170 ? 0.3722 0.4923 0.4372 -0.0080 -0.0377 -0.0913 170 ASN A C 1260 O O . ASN A 170 ? 0.3631 0.4844 0.4301 -0.0131 -0.0341 -0.0922 170 ASN A O 1261 C CB . ASN A 170 ? 0.3476 0.4553 0.3971 -0.0096 -0.0337 -0.0767 170 ASN A CB 1262 C CG . ASN A 170 ? 0.3481 0.4589 0.4012 -0.0136 -0.0305 -0.0775 170 ASN A CG 1263 O OD1 . ASN A 170 ? 0.3502 0.4673 0.4107 -0.0132 -0.0316 -0.0835 170 ASN A OD1 1264 N ND2 . ASN A 170 ? 0.3472 0.4541 0.3954 -0.0173 -0.0265 -0.0718 170 ASN A ND2 1265 N N . ASN A 171 ? 0.3865 0.5119 0.4580 -0.0049 -0.0411 -0.0972 171 ASN A N 1266 C CA . ASN A 171 ? 0.4142 0.5485 0.4967 -0.0076 -0.0402 -0.1059 171 ASN A CA 1267 C C . ASN A 171 ? 0.4281 0.5669 0.5153 -0.0111 -0.0372 -0.1078 171 ASN A C 1268 O O . ASN A 171 ? 0.4412 0.5882 0.5381 -0.0120 -0.0374 -0.1158 171 ASN A O 1269 C CB . ASN A 171 ? 0.4216 0.5597 0.5095 -0.0018 -0.0464 -0.1125 171 ASN A CB 1270 C CG . ASN A 171 ? 0.4335 0.5682 0.5171 0.0014 -0.0494 -0.1114 171 ASN A CG 1271 O OD1 . ASN A 171 ? 0.4880 0.6203 0.5682 0.0076 -0.0550 -0.1110 171 ASN A OD1 1272 N ND2 . ASN A 171 ? 0.4203 0.5545 0.5034 -0.0027 -0.0459 -0.1108 171 ASN A ND2 1273 N N . GLU A 172 ? 0.4227 0.5567 0.5035 -0.0128 -0.0344 -0.1010 172 GLU A N 1274 C CA . GLU A 172 ? 0.4280 0.5660 0.5122 -0.0164 -0.0312 -0.1023 172 GLU A CA 1275 C C . GLU A 172 ? 0.4328 0.5725 0.5170 -0.0244 -0.0248 -0.1014 172 GLU A C 1276 O O . GLU A 172 ? 0.4252 0.5613 0.5059 -0.0267 -0.0232 -0.0987 172 GLU A O 1277 C CB . GLU A 172 ? 0.4395 0.5713 0.5167 -0.0141 -0.0318 -0.0954 172 GLU A CB 1278 C CG . GLU A 172 ? 0.4540 0.5816 0.5285 -0.0066 -0.0380 -0.0939 172 GLU A CG 1279 C CD . GLU A 172 ? 0.4840 0.6180 0.5678 -0.0029 -0.0425 -0.1019 172 GLU A CD 1280 O OE1 . GLU A 172 ? 0.4942 0.6353 0.5857 -0.0055 -0.0405 -0.1073 172 GLU A OE1 1281 O OE2 . GLU A 172 ? 0.5303 0.6625 0.6136 0.0027 -0.0482 -0.1030 172 GLU A OE2 1282 N N . LYS A 173 ? 0.4459 0.5908 0.5337 -0.0286 -0.0212 -0.1036 173 LYS A N 1283 C CA . LYS A 173 ? 0.4771 0.6236 0.5641 -0.0367 -0.0150 -0.1022 173 LYS A CA 1284 C C . LYS A 173 ? 0.4486 0.5875 0.5258 -0.0386 -0.0124 -0.0933 173 LYS A C 1285 O O . LYS A 173 ? 0.4627 0.6012 0.5374 -0.0451 -0.0077 -0.0908 173 LYS A O 1286 C CB . LYS A 173 ? 0.5166 0.6738 0.6124 -0.0409 -0.0121 -0.1099 173 LYS A CB 1287 C CG . LYS A 173 ? 0.5760 0.7418 0.6819 -0.0422 -0.0125 -0.1190 173 LYS A CG 1288 C CD . LYS A 173 ? 0.6243 0.7909 0.7300 -0.0499 -0.0076 -0.1186 173 LYS A CD 1289 C CE . LYS A 173 ? 0.6483 0.8226 0.7638 -0.0508 -0.0083 -0.1274 173 LYS A CE 1290 N NZ . LYS A 173 ? 0.6620 0.8480 0.7883 -0.0510 -0.0082 -0.1370 173 LYS A NZ 1291 N N . PHE A 174 ? 0.4201 0.5527 0.4917 -0.0330 -0.0156 -0.0883 174 PHE A N 1292 C CA . PHE A 174 ? 0.3920 0.5174 0.4549 -0.0341 -0.0137 -0.0800 174 PHE A CA 1293 C C . PHE A 174 ? 0.3736 0.4899 0.4285 -0.0300 -0.0162 -0.0734 174 PHE A C 1294 O O . PHE A 174 ? 0.3671 0.4825 0.4227 -0.0254 -0.0201 -0.0750 174 PHE A O 1295 C CB . PHE A 174 ? 0.3916 0.5185 0.4553 -0.0319 -0.0145 -0.0800 174 PHE A CB 1296 C CG . PHE A 174 ? 0.4031 0.5309 0.4706 -0.0248 -0.0201 -0.0832 174 PHE A CG 1297 C CD1 . PHE A 174 ? 0.4033 0.5234 0.4645 -0.0193 -0.0239 -0.0779 174 PHE A CD1 1298 C CD2 . PHE A 174 ? 0.4040 0.5402 0.4811 -0.0238 -0.0217 -0.0916 174 PHE A CD2 1299 C CE1 . PHE A 174 ? 0.4099 0.5301 0.4737 -0.0131 -0.0295 -0.0803 174 PHE A CE1 1300 C CE2 . PHE A 174 ? 0.4137 0.5501 0.4943 -0.0172 -0.0276 -0.0944 174 PHE A CE2 1301 C CZ . PHE A 174 ? 0.4259 0.5538 0.4994 -0.0119 -0.0315 -0.0885 174 PHE A CZ 1302 N N . ASP A 175 ? 0.3451 0.4550 0.3924 -0.0316 -0.0141 -0.0663 175 ASP A N 1303 C CA . ASP A 175 ? 0.3449 0.4467 0.3846 -0.0283 -0.0159 -0.0600 175 ASP A CA 1304 C C . ASP A 175 ? 0.3197 0.4190 0.3571 -0.0221 -0.0197 -0.0581 175 ASP A C 1305 O O . ASP A 175 ? 0.3237 0.4254 0.3636 -0.0213 -0.0200 -0.0593 175 ASP A O 1306 C CB . ASP A 175 ? 0.3528 0.4489 0.3858 -0.0320 -0.0125 -0.0534 175 ASP A CB 1307 C CG . ASP A 175 ? 0.3941 0.4902 0.4276 -0.0379 -0.0095 -0.0537 175 ASP A CG 1308 O OD1 . ASP A 175 ? 0.4000 0.5004 0.4390 -0.0391 -0.0097 -0.0589 175 ASP A OD1 1309 O OD2 . ASP A 175 ? 0.3904 0.4818 0.4187 -0.0413 -0.0070 -0.0486 175 ASP A OD2 1310 N N . LYS A 176 ? 0.2913 0.3857 0.3239 -0.0180 -0.0225 -0.0551 176 LYS A N 1311 C CA . LYS A 176 ? 0.2772 0.3680 0.3060 -0.0126 -0.0259 -0.0521 176 LYS A CA 1312 C C . LYS A 176 ? 0.2607 0.3444 0.2810 -0.0124 -0.0248 -0.0446 176 LYS A C 1313 O O . LYS A 176 ? 0.2669 0.3481 0.2841 -0.0134 -0.0238 -0.0429 176 LYS A O 1314 C CB . LYS A 176 ? 0.2836 0.3753 0.3135 -0.0077 -0.0306 -0.0552 176 LYS A CB 1315 C CG . LYS A 176 ? 0.2863 0.3850 0.3250 -0.0068 -0.0329 -0.0630 176 LYS A CG 1316 C CD . LYS A 176 ? 0.3007 0.3990 0.3389 -0.0017 -0.0378 -0.0652 176 LYS A CD 1317 C CE . LYS A 176 ? 0.3016 0.4066 0.3486 0.0002 -0.0410 -0.0732 176 LYS A CE 1318 N NZ . LYS A 176 ? 0.3143 0.4186 0.3602 0.0055 -0.0464 -0.0749 176 LYS A NZ 1319 N N . LEU A 177 ? 0.2476 0.3283 0.2647 -0.0108 -0.0251 -0.0407 177 LEU A N 1320 C CA . LEU A 177 ? 0.2423 0.3167 0.2518 -0.0101 -0.0243 -0.0339 177 LEU A CA 1321 C C . LEU A 177 ? 0.2365 0.3082 0.2422 -0.0048 -0.0282 -0.0320 177 LEU A C 1322 O O . LEU A 177 ? 0.2362 0.3080 0.2433 -0.0023 -0.0307 -0.0324 177 LEU A O 1323 C CB . LEU A 177 ? 0.2393 0.3121 0.2476 -0.0123 -0.0217 -0.0306 177 LEU A CB 1324 C CG . LEU A 177 ? 0.2409 0.3078 0.2423 -0.0113 -0.0211 -0.0240 177 LEU A CG 1325 C CD1 . LEU A 177 ? 0.2391 0.3029 0.2363 -0.0130 -0.0192 -0.0214 177 LEU A CD1 1326 C CD2 . LEU A 177 ? 0.2435 0.3098 0.2451 -0.0132 -0.0191 -0.0217 177 LEU A CD2 1327 N N . TYR A 178 ? 0.2440 0.3129 0.2448 -0.0034 -0.0289 -0.0300 178 TYR A N 1328 C CA . TYR A 178 ? 0.2561 0.3221 0.2516 0.0010 -0.0322 -0.0274 178 TYR A CA 1329 C C . TYR A 178 ? 0.2638 0.3248 0.2524 0.0008 -0.0304 -0.0210 178 TYR A C 1330 O O . TYR A 178 ? 0.2759 0.3356 0.2625 -0.0014 -0.0276 -0.0192 178 TYR A O 1331 C CB . TYR A 178 ? 0.2554 0.3228 0.2500 0.0030 -0.0343 -0.0300 178 TYR A CB 1332 C CG . TYR A 178 ? 0.2567 0.3287 0.2575 0.0045 -0.0373 -0.0363 178 TYR A CG 1333 C CD1 . TYR A 178 ? 0.2620 0.3341 0.2627 0.0087 -0.0418 -0.0373 178 TYR A CD1 1334 C CD2 . TYR A 178 ? 0.2601 0.3364 0.2672 0.0017 -0.0357 -0.0414 178 TYR A CD2 1335 C CE1 . TYR A 178 ? 0.2690 0.3456 0.2761 0.0104 -0.0450 -0.0435 178 TYR A CE1 1336 C CE2 . TYR A 178 ? 0.2673 0.3485 0.2809 0.0030 -0.0384 -0.0477 178 TYR A CE2 1337 C CZ . TYR A 178 ? 0.2676 0.3490 0.2813 0.0076 -0.0432 -0.0490 178 TYR A CZ 1338 O OH . TYR A 178 ? 0.2839 0.3705 0.3046 0.0091 -0.0461 -0.0557 178 TYR A OH 1339 N N . ILE A 179 ? 0.2621 0.3204 0.2473 0.0034 -0.0324 -0.0178 179 ILE A N 1340 C CA . ILE A 179 ? 0.2626 0.3165 0.2413 0.0035 -0.0310 -0.0118 179 ILE A CA 1341 C C . ILE A 179 ? 0.2736 0.3258 0.2463 0.0070 -0.0340 -0.0100 179 ILE A C 1342 O O . ILE A 179 ? 0.2664 0.3187 0.2394 0.0098 -0.0379 -0.0112 179 ILE A O 1343 C CB . ILE A 179 ? 0.2655 0.3174 0.2449 0.0032 -0.0307 -0.0090 179 ILE A CB 1344 C CG1 . ILE A 179 ? 0.2612 0.3157 0.2468 0.0000 -0.0281 -0.0115 179 ILE A CG1 1345 C CG2 . ILE A 179 ? 0.2632 0.3108 0.2364 0.0030 -0.0290 -0.0032 179 ILE A CG2 1346 C CD1 . ILE A 179 ? 0.2644 0.3187 0.2492 -0.0037 -0.0241 -0.0105 179 ILE A CD1 1347 N N . TRP A 180 ? 0.2719 0.3226 0.2391 0.0068 -0.0324 -0.0074 180 TRP A N 1348 C CA . TRP A 180 ? 0.2911 0.3409 0.2518 0.0097 -0.0347 -0.0058 180 TRP A CA 1349 C C . TRP A 180 ? 0.2957 0.3433 0.2505 0.0088 -0.0321 -0.0013 180 TRP A C 1350 O O . TRP A 180 ? 0.2921 0.3388 0.2483 0.0062 -0.0288 0.0002 180 TRP A O 1351 C CB . TRP A 180 ? 0.2964 0.3497 0.2585 0.0109 -0.0364 -0.0105 180 TRP A CB 1352 C CG . TRP A 180 ? 0.3009 0.3560 0.2660 0.0084 -0.0334 -0.0129 180 TRP A CG 1353 C CD1 . TRP A 180 ? 0.3036 0.3607 0.2757 0.0059 -0.0320 -0.0164 180 TRP A CD1 1354 C CD2 . TRP A 180 ? 0.3031 0.3581 0.2647 0.0081 -0.0317 -0.0122 180 TRP A CD2 1355 N NE1 . TRP A 180 ? 0.2981 0.3554 0.2708 0.0039 -0.0298 -0.0174 180 TRP A NE1 1356 C CE2 . TRP A 180 ? 0.3052 0.3614 0.2721 0.0054 -0.0297 -0.0152 180 TRP A CE2 1357 C CE3 . TRP A 180 ? 0.3103 0.3645 0.2650 0.0095 -0.0316 -0.0096 180 TRP A CE3 1358 C CZ2 . TRP A 180 ? 0.3058 0.3620 0.2718 0.0046 -0.0282 -0.0156 180 TRP A CZ2 1359 C CZ3 . TRP A 180 ? 0.3091 0.3643 0.2632 0.0087 -0.0298 -0.0107 180 TRP A CZ3 1360 C CH2 . TRP A 180 ? 0.3055 0.3613 0.2653 0.0065 -0.0283 -0.0136 180 TRP A CH2 1361 N N . GLY A 181 ? 0.3006 0.3476 0.2486 0.0108 -0.0335 0.0005 181 GLY A N 1362 C CA . GLY A 181 ? 0.3048 0.3502 0.2471 0.0099 -0.0310 0.0047 181 GLY A CA 1363 C C . GLY A 181 ? 0.3173 0.3643 0.2530 0.0114 -0.0316 0.0048 181 GLY A C 1364 O O . GLY A 181 ? 0.3129 0.3616 0.2473 0.0137 -0.0348 0.0022 181 GLY A O 1365 N N . VAL A 182 ? 0.3155 0.3623 0.2473 0.0102 -0.0286 0.0074 182 VAL A N 1366 C CA . VAL A 182 ? 0.3339 0.3828 0.2592 0.0112 -0.0286 0.0076 182 VAL A CA 1367 C C . VAL A 182 ? 0.3340 0.3806 0.2528 0.0104 -0.0272 0.0131 182 VAL A C 1368 O O . VAL A 182 ? 0.3271 0.3720 0.2477 0.0083 -0.0244 0.0156 182 VAL A O 1369 C CB . VAL A 182 ? 0.3470 0.3990 0.2745 0.0104 -0.0260 0.0044 182 VAL A CB 1370 C CG1 . VAL A 182 ? 0.3581 0.4131 0.2789 0.0114 -0.0257 0.0042 182 VAL A CG1 1371 C CG2 . VAL A 182 ? 0.3555 0.4093 0.2896 0.0108 -0.0275 -0.0007 182 VAL A CG2 1372 N N . HIS A 183 ? 0.3392 0.3858 0.2506 0.0118 -0.0293 0.0151 183 HIS A N 1373 C CA . HIS A 183 ? 0.3499 0.3944 0.2543 0.0106 -0.0280 0.0206 183 HIS A CA 1374 C C . HIS A 183 ? 0.3556 0.4040 0.2554 0.0096 -0.0248 0.0203 183 HIS A C 1375 O O . HIS A 183 ? 0.3536 0.4058 0.2506 0.0110 -0.0257 0.0171 183 HIS A O 1376 C CB . HIS A 183 ? 0.3640 0.4058 0.2618 0.0123 -0.0322 0.0233 183 HIS A CB 1377 C CG . HIS A 183 ? 0.3735 0.4122 0.2638 0.0107 -0.0313 0.0295 183 HIS A CG 1378 N ND1 . HIS A 183 ? 0.3941 0.4331 0.2746 0.0110 -0.0326 0.0320 183 HIS A ND1 1379 C CD2 . HIS A 183 ? 0.3801 0.4153 0.2713 0.0084 -0.0291 0.0338 183 HIS A CD2 1380 C CE1 . HIS A 183 ? 0.3927 0.4283 0.2681 0.0088 -0.0313 0.0379 183 HIS A CE1 1381 N NE2 . HIS A 183 ? 0.3893 0.4226 0.2716 0.0073 -0.0291 0.0389 183 HIS A NE2 1382 N N . HIS A 184 ? 0.3601 0.4078 0.2596 0.0072 -0.0211 0.0231 184 HIS A N 1383 C CA . HIS A 184 ? 0.3670 0.4188 0.2627 0.0059 -0.0177 0.0229 184 HIS A CA 1384 C C . HIS A 184 ? 0.3733 0.4235 0.2604 0.0045 -0.0171 0.0284 184 HIS A C 1385 O O . HIS A 184 ? 0.3674 0.4144 0.2552 0.0025 -0.0153 0.0323 184 HIS A O 1386 C CB . HIS A 184 ? 0.3635 0.4158 0.2656 0.0042 -0.0141 0.0219 184 HIS A CB 1387 C CG . HIS A 184 ? 0.3581 0.4109 0.2685 0.0050 -0.0147 0.0173 184 HIS A CG 1388 N ND1 . HIS A 184 ? 0.3583 0.4150 0.2704 0.0061 -0.0150 0.0125 184 HIS A ND1 1389 C CD2 . HIS A 184 ? 0.3500 0.3996 0.2673 0.0044 -0.0151 0.0170 184 HIS A CD2 1390 C CE1 . HIS A 184 ? 0.3655 0.4210 0.2851 0.0061 -0.0155 0.0096 184 HIS A CE1 1391 N NE2 . HIS A 184 ? 0.3495 0.4010 0.2720 0.0050 -0.0154 0.0125 184 HIS A NE2 1392 N N . PRO A 185 ? 0.3830 0.4351 0.2616 0.0053 -0.0186 0.0290 185 PRO A N 1393 C CA . PRO A 185 ? 0.3970 0.4471 0.2666 0.0035 -0.0181 0.0349 185 PRO A CA 1394 C C . PRO A 185 ? 0.4057 0.4591 0.2730 0.0004 -0.0130 0.0361 185 PRO A C 1395 O O . PRO A 185 ? 0.4037 0.4629 0.2740 0.0004 -0.0103 0.0317 185 PRO A O 1396 C CB . PRO A 185 ? 0.4021 0.4543 0.2631 0.0052 -0.0211 0.0344 185 PRO A CB 1397 C CG . PRO A 185 ? 0.3990 0.4528 0.2658 0.0084 -0.0242 0.0287 185 PRO A CG 1398 C CD . PRO A 185 ? 0.3863 0.4421 0.2632 0.0079 -0.0213 0.0247 185 PRO A CD 1399 N N . GLY A 186 ? 0.4288 0.4788 0.2913 -0.0020 -0.0118 0.0420 186 GLY A N 1400 C CA . GLY A 186 ? 0.4419 0.4952 0.3026 -0.0053 -0.0067 0.0434 186 GLY A CA 1401 C C . GLY A 186 ? 0.4625 0.5231 0.3161 -0.0061 -0.0045 0.0413 186 GLY A C 1402 O O . GLY A 186 ? 0.4635 0.5298 0.3196 -0.0075 -0.0002 0.0385 186 GLY A O 1403 N N . THR A 187 ? 0.4791 0.5399 0.3241 -0.0050 -0.0074 0.0423 187 THR A N 1404 C CA . THR A 187 ? 0.4984 0.5663 0.3351 -0.0058 -0.0056 0.0407 187 THR A CA 1405 C C . THR A 187 ? 0.5082 0.5784 0.3415 -0.0024 -0.0096 0.0371 187 THR A C 1406 O O . THR A 187 ? 0.4832 0.5484 0.3184 0.0001 -0.0143 0.0375 187 THR A O 1407 C CB . THR A 187 ? 0.5183 0.5843 0.3435 -0.0094 -0.0044 0.0476 187 THR A CB 1408 O OG1 . THR A 187 ? 0.5254 0.5846 0.3439 -0.0081 -0.0097 0.0521 187 THR A OG1 1409 C CG2 . THR A 187 ? 0.5099 0.5725 0.3386 -0.0129 -0.0010 0.0518 187 THR A CG2 1410 N N . ASP A 188 ? 0.5426 0.6208 0.3712 -0.0026 -0.0077 0.0334 188 ASP A N 1411 C CA . ASP A 188 ? 0.5836 0.6648 0.4074 0.0003 -0.0114 0.0301 188 ASP A CA 1412 C C . ASP A 188 ? 0.5911 0.6665 0.4041 0.0004 -0.0157 0.0362 188 ASP A C 1413 O O . ASP A 188 ? 0.5785 0.6528 0.3903 0.0037 -0.0205 0.0344 188 ASP A O 1414 C CB . ASP A 188 ? 0.6226 0.7140 0.4421 -0.0003 -0.0082 0.0253 188 ASP A CB 1415 C CG . ASP A 188 ? 0.6451 0.7423 0.4757 0.0005 -0.0053 0.0180 188 ASP A CG 1416 O OD1 . ASP A 188 ? 0.6501 0.7443 0.4910 0.0028 -0.0071 0.0151 188 ASP A OD1 1417 O OD2 . ASP A 188 ? 0.6653 0.7704 0.4942 -0.0012 -0.0012 0.0151 188 ASP A OD2 1418 N N . ASN A 189 ? 0.6029 0.6747 0.4084 -0.0031 -0.0142 0.0432 189 ASN A N 1419 C CA . ASN A 189 ? 0.6195 0.6843 0.4149 -0.0032 -0.0187 0.0499 189 ASN A CA 1420 C C . ASN A 189 ? 0.5911 0.6475 0.3930 0.0000 -0.0242 0.0509 189 ASN A C 1421 O O . ASN A 189 ? 0.5659 0.6190 0.3631 0.0024 -0.0298 0.0519 189 ASN A O 1422 C CB . ASN A 189 ? 0.6564 0.7176 0.4443 -0.0081 -0.0159 0.0577 189 ASN A CB 1423 C CG . ASN A 189 ? 0.7046 0.7724 0.4802 -0.0114 -0.0125 0.0589 189 ASN A CG 1424 O OD1 . ASN A 189 ? 0.7405 0.8144 0.5108 -0.0097 -0.0135 0.0549 189 ASN A OD1 1425 N ND2 . ASN A 189 ? 0.7197 0.7866 0.4906 -0.0164 -0.0083 0.0642 189 ASN A ND2 1426 N N . ASP A 190 ? 0.5735 0.6269 0.3863 -0.0002 -0.0227 0.0505 190 ASP A N 1427 C CA . ASP A 190 ? 0.5591 0.6056 0.3793 0.0024 -0.0273 0.0507 190 ASP A CA 1428 C C . ASP A 190 ? 0.5175 0.5670 0.3434 0.0066 -0.0306 0.0440 190 ASP A C 1429 O O . ASP A 190 ? 0.4995 0.5445 0.3266 0.0094 -0.0359 0.0441 190 ASP A O 1430 C CB . ASP A 190 ? 0.5880 0.6320 0.4187 0.0010 -0.0244 0.0510 190 ASP A CB 1431 C CG . ASP A 190 ? 0.6358 0.6745 0.4625 -0.0026 -0.0226 0.0582 190 ASP A CG 1432 O OD1 . ASP A 190 ? 0.6698 0.7060 0.4856 -0.0044 -0.0238 0.0636 190 ASP A OD1 1433 O OD2 . ASP A 190 ? 0.6862 0.7231 0.5209 -0.0039 -0.0202 0.0585 190 ASP A OD2 1434 N N . GLN A 191 ? 0.4936 0.5507 0.3235 0.0070 -0.0275 0.0378 191 GLN A N 1435 C CA . GLN A 191 ? 0.4790 0.5394 0.3147 0.0106 -0.0301 0.0310 191 GLN A CA 1436 C C . GLN A 191 ? 0.4889 0.5494 0.3164 0.0131 -0.0352 0.0310 191 GLN A C 1437 O O . GLN A 191 ? 0.4857 0.5440 0.3172 0.0163 -0.0399 0.0286 191 GLN A O 1438 C CB . GLN A 191 ? 0.4656 0.5343 0.3054 0.0103 -0.0260 0.0249 191 GLN A CB 1439 C CG . GLN A 191 ? 0.4584 0.5310 0.3038 0.0137 -0.0285 0.0176 191 GLN A CG 1440 C CD . GLN A 191 ? 0.4526 0.5214 0.3095 0.0153 -0.0303 0.0153 191 GLN A CD 1441 O OE1 . GLN A 191 ? 0.4394 0.5050 0.3023 0.0136 -0.0280 0.0171 191 GLN A OE1 1442 N NE2 . GLN A 191 ? 0.4498 0.5195 0.3099 0.0183 -0.0343 0.0110 191 GLN A NE2 1443 N N . ILE A 192 ? 0.5099 0.5732 0.3256 0.0116 -0.0343 0.0335 192 ILE A N 1444 C CA . ILE A 192 ? 0.5162 0.5797 0.3223 0.0138 -0.0392 0.0338 192 ILE A CA 1445 C C . ILE A 192 ? 0.5213 0.5755 0.3233 0.0146 -0.0447 0.0400 192 ILE A C 1446 O O . ILE A 192 ? 0.5140 0.5660 0.3156 0.0181 -0.0505 0.0384 192 ILE A O 1447 C CB . ILE A 192 ? 0.5410 0.6103 0.3347 0.0114 -0.0364 0.0351 192 ILE A CB 1448 C CG1 . ILE A 192 ? 0.5442 0.6235 0.3429 0.0114 -0.0319 0.0277 192 ILE A CG1 1449 C CG2 . ILE A 192 ? 0.5610 0.6296 0.3434 0.0135 -0.0419 0.0366 192 ILE A CG2 1450 C CD1 . ILE A 192 ? 0.5397 0.6229 0.3458 0.0156 -0.0349 0.0198 192 ILE A CD1 1451 N N . PHE A 193 ? 0.5303 0.5787 0.3300 0.0114 -0.0430 0.0467 193 PHE A N 1452 C CA . PHE A 193 ? 0.5465 0.5854 0.3430 0.0120 -0.0483 0.0527 193 PHE A CA 1453 C C . PHE A 193 ? 0.5372 0.5725 0.3451 0.0158 -0.0528 0.0491 193 PHE A C 1454 O O . PHE A 193 ? 0.5352 0.5653 0.3408 0.0185 -0.0592 0.0505 193 PHE A O 1455 C CB . PHE A 193 ? 0.5691 0.6027 0.3639 0.0078 -0.0452 0.0597 193 PHE A CB 1456 C CG . PHE A 193 ? 0.6060 0.6293 0.3979 0.0083 -0.0507 0.0660 193 PHE A CG 1457 C CD1 . PHE A 193 ? 0.6407 0.6595 0.4186 0.0069 -0.0538 0.0725 193 PHE A CD1 1458 C CD2 . PHE A 193 ? 0.6180 0.6361 0.4209 0.0100 -0.0531 0.0653 193 PHE A CD2 1459 C CE1 . PHE A 193 ? 0.6611 0.6697 0.4367 0.0075 -0.0596 0.0784 193 PHE A CE1 1460 C CE2 . PHE A 193 ? 0.6377 0.6463 0.4388 0.0106 -0.0586 0.0706 193 PHE A CE2 1461 C CZ . PHE A 193 ? 0.6526 0.6561 0.4402 0.0095 -0.0621 0.0772 193 PHE A CZ 1462 N N . LEU A 194 ? 0.5025 0.5409 0.3227 0.0160 -0.0495 0.0441 194 LEU A N 1463 C CA . LEU A 194 ? 0.4854 0.5213 0.3170 0.0189 -0.0527 0.0405 194 LEU A CA 1464 C C . LEU A 194 ? 0.4687 0.5094 0.3045 0.0225 -0.0556 0.0332 194 LEU A C 1465 O O . LEU A 194 ? 0.4806 0.5185 0.3204 0.0256 -0.0609 0.0314 194 LEU A O 1466 C CB . LEU A 194 ? 0.4688 0.5054 0.3113 0.0169 -0.0478 0.0390 194 LEU A CB 1467 C CG . LEU A 194 ? 0.4739 0.5050 0.3160 0.0138 -0.0456 0.0453 194 LEU A CG 1468 C CD1 . LEU A 194 ? 0.4453 0.4789 0.2971 0.0119 -0.0402 0.0429 194 LEU A CD1 1469 C CD2 . LEU A 194 ? 0.4824 0.5055 0.3263 0.0154 -0.0511 0.0483 194 LEU A CD2 1470 N N . TYR A 195 ? 0.4592 0.5075 0.2951 0.0223 -0.0522 0.0286 195 TYR A N 1471 C CA . TYR A 195 ? 0.4657 0.5189 0.3078 0.0254 -0.0542 0.0210 195 TYR A CA 1472 C C . TYR A 195 ? 0.4956 0.5542 0.3290 0.0270 -0.0559 0.0185 195 TYR A C 1473 O O . TYR A 195 ? 0.4905 0.5533 0.3284 0.0297 -0.0579 0.0120 195 TYR A O 1474 C CB . TYR A 195 ? 0.4549 0.5121 0.3081 0.0243 -0.0495 0.0161 195 TYR A CB 1475 C CG . TYR A 195 ? 0.4259 0.4783 0.2863 0.0223 -0.0473 0.0190 195 TYR A CG 1476 C CD1 . TYR A 195 ? 0.4244 0.4723 0.2911 0.0238 -0.0509 0.0189 195 TYR A CD1 1477 C CD2 . TYR A 195 ? 0.4278 0.4806 0.2886 0.0190 -0.0418 0.0214 195 TYR A CD2 1478 C CE1 . TYR A 195 ? 0.4148 0.4588 0.2878 0.0220 -0.0490 0.0212 195 TYR A CE1 1479 C CE2 . TYR A 195 ? 0.4101 0.4588 0.2772 0.0173 -0.0400 0.0239 195 TYR A CE2 1480 C CZ . TYR A 195 ? 0.4109 0.4551 0.2838 0.0188 -0.0436 0.0239 195 TYR A CZ 1481 O OH . TYR A 195 ? 0.4161 0.4565 0.2952 0.0172 -0.0420 0.0260 195 TYR A OH 1482 N N . ALA A 196 ? 0.5283 0.5868 0.3492 0.0251 -0.0550 0.0235 196 ALA A N 1483 C CA . ALA A 196 ? 0.5547 0.6179 0.3652 0.0264 -0.0569 0.0221 196 ALA A CA 1484 C C . ALA A 196 ? 0.5693 0.6419 0.3827 0.0266 -0.0533 0.0150 196 ALA A C 1485 O O . ALA A 196 ? 0.5954 0.6731 0.4019 0.0282 -0.0551 0.0123 196 ALA A O 1486 C CB . ALA A 196 ? 0.5462 0.6065 0.3550 0.0304 -0.0645 0.0210 196 ALA A CB 1487 N N . GLN A 197 ? 0.5662 0.6413 0.3897 0.0252 -0.0485 0.0120 197 GLN A N 1488 C CA . GLN A 197 ? 0.5803 0.6638 0.4079 0.0255 -0.0454 0.0050 197 GLN A CA 1489 C C . GLN A 197 ? 0.5570 0.6415 0.3935 0.0230 -0.0398 0.0041 197 GLN A C 1490 O O . GLN A 197 ? 0.5362 0.6148 0.3768 0.0214 -0.0387 0.0081 197 GLN A O 1491 C CB . GLN A 197 ? 0.5993 0.6854 0.4341 0.0293 -0.0494 -0.0021 197 GLN A CB 1492 C CG . GLN A 197 ? 0.6077 0.6890 0.4544 0.0304 -0.0512 -0.0034 197 GLN A CG 1493 C CD . GLN A 197 ? 0.6282 0.7099 0.4784 0.0342 -0.0569 -0.0081 197 GLN A CD 1494 O OE1 . GLN A 197 ? 0.6604 0.7458 0.5043 0.0364 -0.0599 -0.0107 197 GLN A OE1 1495 N NE2 . GLN A 197 ? 0.6416 0.7197 0.5018 0.0349 -0.0584 -0.0095 197 GLN A NE2 1496 N N . ALA A 198 ? 0.5412 0.6328 0.3806 0.0228 -0.0367 -0.0014 198 ALA A N 1497 C CA . ALA A 198 ? 0.5409 0.6340 0.3886 0.0207 -0.0317 -0.0029 198 ALA A CA 1498 C C . ALA A 198 ? 0.5184 0.6070 0.3784 0.0215 -0.0328 -0.0047 198 ALA A C 1499 O O . ALA A 198 ? 0.5243 0.6116 0.3881 0.0240 -0.0368 -0.0074 198 ALA A O 1500 C CB . ALA A 198 ? 0.5421 0.6439 0.3914 0.0212 -0.0294 -0.0096 198 ALA A CB 1501 N N . SER A 199 ? 0.5050 0.5915 0.3710 0.0193 -0.0291 -0.0032 199 SER A N 1502 C CA . SER A 199 ? 0.4948 0.5770 0.3716 0.0194 -0.0297 -0.0043 199 SER A CA 1503 C C . SER A 199 ? 0.4988 0.5848 0.3841 0.0209 -0.0302 -0.0116 199 SER A C 1504 O O . SER A 199 ? 0.4864 0.5781 0.3713 0.0212 -0.0286 -0.0157 199 SER A O 1505 C CB . SER A 199 ? 0.4822 0.5612 0.3624 0.0165 -0.0257 -0.0006 199 SER A CB 1506 O OG . SER A 199 ? 0.4766 0.5604 0.3589 0.0153 -0.0220 -0.0034 199 SER A OG 1507 N N . GLY A 200 ? 0.5055 0.5883 0.3985 0.0218 -0.0325 -0.0134 200 GLY A N 1508 C CA . GLY A 200 ? 0.4971 0.5821 0.3992 0.0227 -0.0330 -0.0198 200 GLY A CA 1509 C C . GLY A 200 ? 0.4996 0.5797 0.4104 0.0215 -0.0330 -0.0191 200 GLY A C 1510 O O . GLY A 200 ? 0.5052 0.5806 0.4149 0.0207 -0.0333 -0.0145 200 GLY A O 1511 N N . ARG A 201 ? 0.4747 0.5556 0.3940 0.0213 -0.0327 -0.0238 201 ARG A N 1512 C CA . ARG A 201 ? 0.4600 0.5367 0.3873 0.0195 -0.0320 -0.0232 201 ARG A CA 1513 C C . ARG A 201 ? 0.4366 0.5108 0.3658 0.0201 -0.0348 -0.0227 201 ARG A C 1514 O O . ARG A 201 ? 0.4312 0.5072 0.3573 0.0225 -0.0381 -0.0243 201 ARG A O 1515 C CB . ARG A 201 ? 0.4703 0.5482 0.4056 0.0190 -0.0317 -0.0284 201 ARG A CB 1516 C CG . ARG A 201 ? 0.4766 0.5576 0.4152 0.0210 -0.0348 -0.0342 201 ARG A CG 1517 C CD . ARG A 201 ? 0.4835 0.5671 0.4275 0.0211 -0.0345 -0.0395 201 ARG A CD 1518 N NE . ARG A 201 ? 0.4897 0.5763 0.4370 0.0230 -0.0377 -0.0451 201 ARG A NE 1519 C CZ . ARG A 201 ? 0.5030 0.5947 0.4461 0.0258 -0.0396 -0.0485 201 ARG A CZ 1520 N NH1 . ARG A 201 ? 0.5115 0.6061 0.4463 0.0267 -0.0385 -0.0467 201 ARG A NH1 1521 N NH2 . ARG A 201 ? 0.5054 0.5996 0.4526 0.0274 -0.0426 -0.0538 201 ARG A NH2 1522 N N . ILE A 202 ? 0.3958 0.4661 0.3301 0.0180 -0.0337 -0.0207 202 ILE A N 1523 C CA . ILE A 202 ? 0.3891 0.4576 0.3274 0.0182 -0.0359 -0.0213 202 ILE A CA 1524 C C . ILE A 202 ? 0.3654 0.4337 0.3129 0.0163 -0.0351 -0.0249 202 ILE A C 1525 O O . ILE A 202 ? 0.3653 0.4317 0.3154 0.0139 -0.0323 -0.0236 202 ILE A O 1526 C CB . ILE A 202 ? 0.3873 0.4518 0.3239 0.0171 -0.0352 -0.0159 202 ILE A CB 1527 C CG1 . ILE A 202 ? 0.4107 0.4747 0.3381 0.0188 -0.0367 -0.0121 202 ILE A CG1 1528 C CG2 . ILE A 202 ? 0.3886 0.4519 0.3313 0.0169 -0.0370 -0.0174 202 ILE A CG2 1529 C CD1 . ILE A 202 ? 0.4106 0.4703 0.3356 0.0175 -0.0356 -0.0063 202 ILE A CD1 1530 N N . THR A 203 ? 0.3546 0.4247 0.3068 0.0172 -0.0375 -0.0293 203 THR A N 1531 C CA . THR A 203 ? 0.3527 0.4225 0.3135 0.0148 -0.0367 -0.0325 203 THR A CA 1532 C C . THR A 203 ? 0.3502 0.4197 0.3155 0.0143 -0.0380 -0.0335 203 THR A C 1533 O O . THR A 203 ? 0.3566 0.4282 0.3217 0.0167 -0.0412 -0.0360 203 THR A O 1534 C CB . THR A 203 ? 0.3630 0.4359 0.3273 0.0157 -0.0380 -0.0382 203 THR A CB 1535 O OG1 . THR A 203 ? 0.3535 0.4269 0.3146 0.0160 -0.0366 -0.0377 203 THR A OG1 1536 C CG2 . THR A 203 ? 0.3580 0.4298 0.3311 0.0127 -0.0372 -0.0411 203 THR A CG2 1537 N N . VAL A 204 ? 0.3289 0.3959 0.2982 0.0110 -0.0356 -0.0317 204 VAL A N 1538 C CA . VAL A 204 ? 0.3205 0.3879 0.2950 0.0098 -0.0362 -0.0332 204 VAL A CA 1539 C C . VAL A 204 ? 0.3183 0.3860 0.3000 0.0064 -0.0346 -0.0362 204 VAL A C 1540 O O . VAL A 204 ? 0.3123 0.3773 0.2944 0.0037 -0.0319 -0.0341 204 VAL A O 1541 C CB . VAL A 204 ? 0.3137 0.3782 0.2864 0.0087 -0.0348 -0.0284 204 VAL A CB 1542 C CG1 . VAL A 204 ? 0.3024 0.3682 0.2814 0.0073 -0.0352 -0.0307 204 VAL A CG1 1543 C CG2 . VAL A 204 ? 0.3104 0.3739 0.2758 0.0118 -0.0366 -0.0249 204 VAL A CG2 1544 N N . SER A 205 ? 0.3258 0.3967 0.3131 0.0064 -0.0363 -0.0413 205 SER A N 1545 C CA . SER A 205 ? 0.3289 0.4003 0.3229 0.0031 -0.0350 -0.0446 205 SER A CA 1546 C C . SER A 205 ? 0.3322 0.4064 0.3329 0.0013 -0.0353 -0.0484 205 SER A C 1547 O O . SER A 205 ? 0.3333 0.4100 0.3345 0.0036 -0.0374 -0.0499 205 SER A O 1548 C CB . SER A 205 ? 0.3349 0.4079 0.3298 0.0047 -0.0367 -0.0485 205 SER A CB 1549 O OG . SER A 205 ? 0.3442 0.4212 0.3390 0.0084 -0.0401 -0.0523 205 SER A OG 1550 N N . THR A 206 ? 0.3270 0.4009 0.3330 -0.0030 -0.0332 -0.0499 206 THR A N 1551 C CA . THR A 206 ? 0.3321 0.4095 0.3455 -0.0056 -0.0329 -0.0544 206 THR A CA 1552 C C . THR A 206 ? 0.3308 0.4083 0.3489 -0.0082 -0.0325 -0.0577 206 THR A C 1553 O O . THR A 206 ? 0.3253 0.4002 0.3411 -0.0074 -0.0329 -0.0567 206 THR A O 1554 C CB . THR A 206 ? 0.3297 0.4061 0.3444 -0.0098 -0.0297 -0.0518 206 THR A CB 1555 O OG1 . THR A 206 ? 0.3446 0.4167 0.3583 -0.0138 -0.0269 -0.0485 206 THR A OG1 1556 C CG2 . THR A 206 ? 0.3209 0.3962 0.3309 -0.0074 -0.0300 -0.0479 206 THR A CG2 1557 N N . LYS A 207 ? 0.3410 0.4215 0.3661 -0.0116 -0.0317 -0.0618 207 LYS A N 1558 C CA . LYS A 207 ? 0.3646 0.4444 0.3946 -0.0151 -0.0310 -0.0645 207 LYS A CA 1559 C C . LYS A 207 ? 0.3823 0.4561 0.4099 -0.0191 -0.0284 -0.0596 207 LYS A C 1560 O O . LYS A 207 ? 0.3958 0.4670 0.4252 -0.0206 -0.0287 -0.0604 207 LYS A O 1561 C CB . LYS A 207 ? 0.3778 0.4622 0.4156 -0.0187 -0.0301 -0.0694 207 LYS A CB 1562 C CG . LYS A 207 ? 0.3938 0.4844 0.4357 -0.0147 -0.0333 -0.0756 207 LYS A CG 1563 C CD . LYS A 207 ? 0.4153 0.5110 0.4661 -0.0188 -0.0321 -0.0812 207 LYS A CD 1564 C CE . LYS A 207 ? 0.4321 0.5340 0.4864 -0.0157 -0.0343 -0.0857 207 LYS A CE 1565 N NZ . LYS A 207 ? 0.4504 0.5578 0.5135 -0.0204 -0.0323 -0.0911 207 LYS A NZ 1566 N N . ARG A 208 ? 0.3987 0.4700 0.4225 -0.0209 -0.0261 -0.0547 208 ARG A N 1567 C CA . ARG A 208 ? 0.4210 0.4866 0.4426 -0.0249 -0.0238 -0.0500 208 ARG A CA 1568 C C . ARG A 208 ? 0.4165 0.4776 0.4312 -0.0223 -0.0238 -0.0448 208 ARG A C 1569 O O . ARG A 208 ? 0.4311 0.4872 0.4440 -0.0251 -0.0225 -0.0411 208 ARG A O 1570 C CB . ARG A 208 ? 0.4605 0.5267 0.4835 -0.0301 -0.0207 -0.0486 208 ARG A CB 1571 C CG . ARG A 208 ? 0.4907 0.5584 0.5103 -0.0284 -0.0198 -0.0461 208 ARG A CG 1572 C CD . ARG A 208 ? 0.5492 0.6166 0.5691 -0.0338 -0.0165 -0.0440 208 ARG A CD 1573 N NE . ARG A 208 ? 0.6008 0.6619 0.6177 -0.0377 -0.0150 -0.0395 208 ARG A NE 1574 C CZ . ARG A 208 ? 0.6203 0.6763 0.6316 -0.0363 -0.0149 -0.0343 208 ARG A CZ 1575 N NH1 . ARG A 208 ? 0.6262 0.6826 0.6338 -0.0315 -0.0159 -0.0326 208 ARG A NH1 1576 N NH2 . ARG A 208 ? 0.6474 0.6977 0.6566 -0.0399 -0.0140 -0.0308 208 ARG A NH2 1577 N N . SER A 209 ? 0.3816 0.4444 0.3925 -0.0172 -0.0255 -0.0444 209 SER A N 1578 C CA . SER A 209 ? 0.3789 0.4382 0.3835 -0.0151 -0.0251 -0.0394 209 SER A CA 1579 C C . SER A 209 ? 0.3661 0.4274 0.3669 -0.0096 -0.0274 -0.0402 209 SER A C 1580 O O . SER A 209 ? 0.3497 0.4150 0.3517 -0.0069 -0.0295 -0.0437 209 SER A O 1581 C CB . SER A 209 ? 0.3795 0.4381 0.3814 -0.0164 -0.0231 -0.0354 209 SER A CB 1582 O OG . SER A 209 ? 0.3953 0.4580 0.3976 -0.0139 -0.0242 -0.0372 209 SER A OG 1583 N N . GLN A 210 ? 0.3562 0.4147 0.3522 -0.0080 -0.0272 -0.0369 210 GLN A N 1584 C CA . GLN A 210 ? 0.3610 0.4214 0.3523 -0.0033 -0.0288 -0.0369 210 GLN A CA 1585 C C . GLN A 210 ? 0.3614 0.4189 0.3471 -0.0028 -0.0273 -0.0318 210 GLN A C 1586 O O . GLN A 210 ? 0.3624 0.4163 0.3485 -0.0051 -0.0258 -0.0296 210 GLN A O 1587 C CB . GLN A 210 ? 0.3766 0.4387 0.3693 -0.0013 -0.0308 -0.0410 210 GLN A CB 1588 C CG . GLN A 210 ? 0.3877 0.4462 0.3830 -0.0035 -0.0302 -0.0411 210 GLN A CG 1589 C CD . GLN A 210 ? 0.4179 0.4786 0.4151 -0.0011 -0.0325 -0.0458 210 GLN A CD 1590 O OE1 . GLN A 210 ? 0.4637 0.5287 0.4594 0.0022 -0.0343 -0.0486 210 GLN A OE1 1591 N NE2 . GLN A 210 ? 0.4093 0.4669 0.4099 -0.0027 -0.0326 -0.0467 210 GLN A NE2 1592 N N . GLN A 211 ? 0.3530 0.4119 0.3336 0.0001 -0.0279 -0.0299 211 GLN A N 1593 C CA . GLN A 211 ? 0.3451 0.4020 0.3203 0.0008 -0.0265 -0.0254 211 GLN A CA 1594 C C . GLN A 211 ? 0.3418 0.4014 0.3118 0.0047 -0.0280 -0.0259 211 GLN A C 1595 O O . GLN A 211 ? 0.3347 0.3965 0.3028 0.0068 -0.0298 -0.0267 211 GLN A O 1596 C CB . GLN A 211 ? 0.3687 0.4241 0.3424 -0.0002 -0.0252 -0.0215 211 GLN A CB 1597 C CG . GLN A 211 ? 0.3753 0.4288 0.3534 -0.0041 -0.0235 -0.0210 211 GLN A CG 1598 C CD . GLN A 211 ? 0.3897 0.4439 0.3681 -0.0044 -0.0233 -0.0197 211 GLN A CD 1599 O OE1 . GLN A 211 ? 0.4132 0.4703 0.3951 -0.0042 -0.0246 -0.0229 211 GLN A OE1 1600 N NE2 . GLN A 211 ? 0.3854 0.4374 0.3609 -0.0048 -0.0218 -0.0155 211 GLN A NE2 1601 N N . THR A 212 ? 0.3374 0.3970 0.3051 0.0055 -0.0273 -0.0256 212 THR A N 1602 C CA . THR A 212 ? 0.3274 0.3900 0.2892 0.0086 -0.0282 -0.0257 212 THR A CA 1603 C C . THR A 212 ? 0.3348 0.3958 0.2916 0.0083 -0.0259 -0.0210 212 THR A C 1604 O O . THR A 212 ? 0.3380 0.3967 0.2966 0.0065 -0.0241 -0.0197 212 THR A O 1605 C CB . THR A 212 ? 0.3215 0.3870 0.2849 0.0101 -0.0294 -0.0306 212 THR A CB 1606 O OG1 . THR A 212 ? 0.3137 0.3810 0.2816 0.0105 -0.0317 -0.0351 212 THR A OG1 1607 C CG2 . THR A 212 ? 0.3240 0.3931 0.2806 0.0129 -0.0298 -0.0306 212 THR A CG2 1608 N N . VAL A 213 ? 0.3362 0.3983 0.2869 0.0099 -0.0262 -0.0184 213 VAL A N 1609 C CA . VAL A 213 ? 0.3425 0.4032 0.2884 0.0094 -0.0241 -0.0137 213 VAL A CA 1610 C C . VAL A 213 ? 0.3530 0.4171 0.2917 0.0115 -0.0244 -0.0135 213 VAL A C 1611 O O . VAL A 213 ? 0.3479 0.4139 0.2835 0.0134 -0.0268 -0.0146 213 VAL A O 1612 C CB . VAL A 213 ? 0.3484 0.4060 0.2935 0.0083 -0.0237 -0.0094 213 VAL A CB 1613 C CG1 . VAL A 213 ? 0.3579 0.4141 0.2986 0.0075 -0.0214 -0.0048 213 VAL A CG1 1614 C CG2 . VAL A 213 ? 0.3515 0.4065 0.3031 0.0059 -0.0231 -0.0099 213 VAL A CG2 1615 N N . ILE A 214 ? 0.3711 0.4362 0.3072 0.0110 -0.0221 -0.0121 214 ILE A N 1616 C CA . ILE A 214 ? 0.3875 0.4565 0.3166 0.0123 -0.0217 -0.0120 214 ILE A CA 1617 C C . ILE A 214 ? 0.3876 0.4546 0.3106 0.0114 -0.0202 -0.0062 214 ILE A C 1618 O O . ILE A 214 ? 0.3834 0.4485 0.3078 0.0095 -0.0177 -0.0036 214 ILE A O 1619 C CB . ILE A 214 ? 0.4002 0.4724 0.3309 0.0122 -0.0198 -0.0150 214 ILE A CB 1620 C CG1 . ILE A 214 ? 0.4124 0.4855 0.3501 0.0129 -0.0214 -0.0206 214 ILE A CG1 1621 C CG2 . ILE A 214 ? 0.4035 0.4810 0.3268 0.0134 -0.0192 -0.0156 214 ILE A CG2 1622 C CD1 . ILE A 214 ? 0.4529 0.5290 0.3898 0.0151 -0.0243 -0.0244 214 ILE A CD1 1623 N N . PRO A 215 ? 0.3930 0.4604 0.3094 0.0126 -0.0219 -0.0041 215 PRO A N 1624 C CA . PRO A 215 ? 0.3937 0.4593 0.3036 0.0114 -0.0205 0.0014 215 PRO A CA 1625 C C . PRO A 215 ? 0.3995 0.4689 0.3057 0.0104 -0.0173 0.0015 215 PRO A C 1626 O O . PRO A 215 ? 0.3986 0.4731 0.3032 0.0116 -0.0175 -0.0024 215 PRO A O 1627 C CB . PRO A 215 ? 0.4169 0.4823 0.3202 0.0132 -0.0238 0.0029 215 PRO A CB 1628 C CG . PRO A 215 ? 0.4132 0.4796 0.3211 0.0152 -0.0270 -0.0018 215 PRO A CG 1629 C CD . PRO A 215 ? 0.4020 0.4713 0.3163 0.0149 -0.0255 -0.0067 215 PRO A CD 1630 N N . ASN A 216 ? 0.3906 0.4581 0.2960 0.0083 -0.0145 0.0054 216 ASN A N 1631 C CA . ASN A 216 ? 0.3897 0.4611 0.2926 0.0070 -0.0111 0.0054 216 ASN A CA 1632 C C . ASN A 216 ? 0.3886 0.4589 0.2838 0.0053 -0.0096 0.0111 216 ASN A C 1633 O O . ASN A 216 ? 0.3846 0.4504 0.2809 0.0037 -0.0087 0.0153 216 ASN A O 1634 C CB . ASN A 216 ? 0.3910 0.4616 0.3014 0.0058 -0.0088 0.0041 216 ASN A CB 1635 C CG . ASN A 216 ? 0.3983 0.4697 0.3161 0.0071 -0.0103 -0.0012 216 ASN A CG 1636 O OD1 . ASN A 216 ? 0.4113 0.4871 0.3288 0.0086 -0.0111 -0.0057 216 ASN A OD1 1637 N ND2 . ASN A 216 ? 0.3893 0.4563 0.3136 0.0063 -0.0106 -0.0008 216 ASN A ND2 1638 N N . ILE A 217 ? 0.3989 0.4733 0.2860 0.0054 -0.0094 0.0112 217 ILE A N 1639 C CA . ILE A 217 ? 0.4041 0.4775 0.2825 0.0034 -0.0081 0.0168 217 ILE A CA 1640 C C . ILE A 217 ? 0.4076 0.4831 0.2871 0.0007 -0.0035 0.0180 217 ILE A C 1641 O O . ILE A 217 ? 0.4070 0.4876 0.2905 0.0007 -0.0013 0.0133 217 ILE A O 1642 C CB . ILE A 217 ? 0.4224 0.5002 0.2911 0.0042 -0.0092 0.0164 217 ILE A CB 1643 C CG1 . ILE A 217 ? 0.4216 0.4966 0.2891 0.0070 -0.0142 0.0158 217 ILE A CG1 1644 C CG2 . ILE A 217 ? 0.4167 0.4940 0.2757 0.0013 -0.0072 0.0223 217 ILE A CG2 1645 C CD1 . ILE A 217 ? 0.4531 0.5335 0.3145 0.0088 -0.0159 0.0123 217 ILE A CD1 1646 N N . GLY A 218 ? 0.4131 0.4845 0.2896 -0.0015 -0.0023 0.0238 218 GLY A N 1647 C CA . GLY A 218 ? 0.4190 0.4924 0.2965 -0.0044 0.0020 0.0252 218 GLY A CA 1648 C C . GLY A 218 ? 0.4245 0.4913 0.3024 -0.0063 0.0024 0.0311 218 GLY A C 1649 O O . GLY A 218 ? 0.4103 0.4712 0.2914 -0.0051 -0.0005 0.0328 218 GLY A O 1650 N N . SER A 219 ? 0.4289 0.4972 0.3040 -0.0094 0.0060 0.0339 219 SER A N 1651 C CA . SER A 219 ? 0.4462 0.5087 0.3226 -0.0115 0.0067 0.0392 219 SER A CA 1652 C C . SER A 219 ? 0.4340 0.4955 0.3209 -0.0111 0.0077 0.0367 219 SER A C 1653 O O . SER A 219 ? 0.4477 0.5142 0.3391 -0.0111 0.0100 0.0323 219 SER A O 1654 C CB . SER A 219 ? 0.4668 0.5316 0.3372 -0.0152 0.0105 0.0427 219 SER A CB 1655 O OG . SER A 219 ? 0.5152 0.5815 0.3750 -0.0160 0.0098 0.0450 219 SER A OG 1656 N N . ARG A 220 ? 0.4075 0.4625 0.2982 -0.0107 0.0055 0.0393 220 ARG A N 1657 C CA . ARG A 220 ? 0.4046 0.4577 0.3037 -0.0111 0.0067 0.0387 220 ARG A CA 1658 C C . ARG A 220 ? 0.4041 0.4538 0.3016 -0.0139 0.0083 0.0440 220 ARG A C 1659 O O . ARG A 220 ? 0.4087 0.4562 0.2989 -0.0151 0.0075 0.0484 220 ARG A O 1660 C CB . ARG A 220 ? 0.3980 0.4468 0.3027 -0.0089 0.0033 0.0375 220 ARG A CB 1661 C CG . ARG A 220 ? 0.3952 0.4469 0.3035 -0.0066 0.0021 0.0321 220 ARG A CG 1662 C CD . ARG A 220 ? 0.4110 0.4645 0.3137 -0.0049 -0.0001 0.0308 220 ARG A CD 1663 N NE . ARG A 220 ? 0.4052 0.4600 0.3125 -0.0027 -0.0020 0.0259 220 ARG A NE 1664 C CZ . ARG A 220 ? 0.4145 0.4723 0.3189 -0.0009 -0.0038 0.0230 220 ARG A CZ 1665 N NH1 . ARG A 220 ? 0.4068 0.4667 0.3031 -0.0010 -0.0040 0.0245 220 ARG A NH1 1666 N NH2 . ARG A 220 ? 0.4154 0.4739 0.3249 0.0007 -0.0055 0.0186 220 ARG A NH2 1667 N N . PRO A 221 ? 0.3988 0.4479 0.3028 -0.0150 0.0102 0.0438 221 PRO A N 1668 C CA . PRO A 221 ? 0.4123 0.4577 0.3155 -0.0175 0.0114 0.0487 221 PRO A CA 1669 C C . PRO A 221 ? 0.4217 0.4603 0.3232 -0.0168 0.0076 0.0528 221 PRO A C 1670 O O . PRO A 221 ? 0.4234 0.4594 0.3286 -0.0144 0.0045 0.0511 221 PRO A O 1671 C CB . PRO A 221 ? 0.4075 0.4533 0.3193 -0.0179 0.0132 0.0466 221 PRO A CB 1672 C CG . PRO A 221 ? 0.4013 0.4531 0.3157 -0.0168 0.0146 0.0411 221 PRO A CG 1673 C CD . PRO A 221 ? 0.3999 0.4515 0.3116 -0.0142 0.0115 0.0392 221 PRO A CD 1674 N N . ARG A 222 ? 0.4211 0.4567 0.3168 -0.0190 0.0076 0.0579 222 ARG A N 1675 C CA . ARG A 222 ? 0.4401 0.4690 0.3337 -0.0180 0.0034 0.0616 222 ARG A CA 1676 C C . ARG A 222 ? 0.4284 0.4533 0.3304 -0.0171 0.0019 0.0614 222 ARG A C 1677 O O . ARG A 222 ? 0.4185 0.4437 0.3255 -0.0187 0.0044 0.0614 222 ARG A O 1678 C CB . ARG A 222 ? 0.4574 0.4832 0.3432 -0.0208 0.0036 0.0676 222 ARG A CB 1679 C CG . ARG A 222 ? 0.4826 0.5121 0.3588 -0.0214 0.0043 0.0680 222 ARG A CG 1680 C CD . ARG A 222 ? 0.5131 0.5383 0.3806 -0.0243 0.0037 0.0747 222 ARG A CD 1681 N NE . ARG A 222 ? 0.5324 0.5612 0.3897 -0.0250 0.0041 0.0754 222 ARG A NE 1682 C CZ . ARG A 222 ? 0.5648 0.5894 0.4123 -0.0268 0.0022 0.0811 222 ARG A CZ 1683 N NH1 . ARG A 222 ? 0.5747 0.5910 0.4220 -0.0279 -0.0003 0.0866 222 ARG A NH1 1684 N NH2 . ARG A 222 ? 0.5822 0.6108 0.4201 -0.0275 0.0028 0.0813 222 ARG A NH2 1685 N N . VAL A 223 ? 0.4344 0.4560 0.3381 -0.0145 -0.0022 0.0606 223 VAL A N 1686 C CA . VAL A 223 ? 0.4362 0.4540 0.3472 -0.0135 -0.0043 0.0602 223 VAL A CA 1687 C C . VAL A 223 ? 0.4570 0.4690 0.3649 -0.0127 -0.0087 0.0638 223 VAL A C 1688 O O . VAL A 223 ? 0.4368 0.4484 0.3404 -0.0108 -0.0117 0.0635 223 VAL A O 1689 C CB . VAL A 223 ? 0.4336 0.4537 0.3504 -0.0111 -0.0054 0.0550 223 VAL A CB 1690 C CG1 . VAL A 223 ? 0.4304 0.4469 0.3538 -0.0100 -0.0081 0.0545 223 VAL A CG1 1691 C CG2 . VAL A 223 ? 0.4295 0.4544 0.3499 -0.0118 -0.0017 0.0516 223 VAL A CG2 1692 N N . ARG A 224 ? 0.4872 0.4945 0.3975 -0.0140 -0.0094 0.0672 224 ARG A N 1693 C CA . ARG A 224 ? 0.4980 0.4989 0.4054 -0.0135 -0.0138 0.0711 224 ARG A CA 1694 C C . ARG A 224 ? 0.4917 0.4922 0.3885 -0.0140 -0.0147 0.0742 224 ARG A C 1695 O O . ARG A 224 ? 0.5290 0.5265 0.4223 -0.0119 -0.0192 0.0749 224 ARG A O 1696 C CB . ARG A 224 ? 0.5002 0.4993 0.4136 -0.0102 -0.0183 0.0679 224 ARG A CB 1697 C CG . ARG A 224 ? 0.4977 0.4977 0.4209 -0.0101 -0.0172 0.0650 224 ARG A CG 1698 C CD . ARG A 224 ? 0.4916 0.4908 0.4210 -0.0072 -0.0211 0.0613 224 ARG A CD 1699 N NE . ARG A 224 ? 0.4763 0.4797 0.4055 -0.0053 -0.0216 0.0570 224 ARG A NE 1700 C CZ . ARG A 224 ? 0.4678 0.4760 0.4006 -0.0054 -0.0187 0.0530 224 ARG A CZ 1701 N NH1 . ARG A 224 ? 0.4786 0.4882 0.4154 -0.0071 -0.0153 0.0525 224 ARG A NH1 1702 N NH2 . ARG A 224 ? 0.4670 0.4785 0.3995 -0.0037 -0.0195 0.0493 224 ARG A NH2 1703 N N . ASN A 225 ? 0.4980 0.5020 0.3897 -0.0168 -0.0103 0.0756 225 ASN A N 1704 C CA . ASN A 225 ? 0.5137 0.5186 0.3946 -0.0182 -0.0099 0.0786 225 ASN A CA 1705 C C . ASN A 225 ? 0.4960 0.5051 0.3727 -0.0157 -0.0112 0.0751 225 ASN A C 1706 O O . ASN A 225 ? 0.5036 0.5129 0.3710 -0.0163 -0.0120 0.0776 225 ASN A O 1707 C CB . ASN A 225 ? 0.5448 0.5419 0.4197 -0.0195 -0.0135 0.0852 225 ASN A CB 1708 C CG . ASN A 225 ? 0.5846 0.5823 0.4486 -0.0233 -0.0109 0.0900 225 ASN A CG 1709 O OD1 . ASN A 225 ? 0.5868 0.5900 0.4502 -0.0262 -0.0054 0.0893 225 ASN A OD1 1710 N ND2 . ASN A 225 ? 0.6106 0.6029 0.4658 -0.0234 -0.0150 0.0948 225 ASN A ND2 1711 N N . ILE A 226 ? 0.4432 0.4562 0.3268 -0.0130 -0.0112 0.0693 226 ILE A N 1712 C CA . ILE A 226 ? 0.4182 0.4351 0.2993 -0.0105 -0.0126 0.0654 226 ILE A CA 1713 C C . ILE A 226 ? 0.4120 0.4363 0.2959 -0.0109 -0.0082 0.0606 226 ILE A C 1714 O O . ILE A 226 ? 0.3901 0.4156 0.2822 -0.0105 -0.0066 0.0575 226 ILE A O 1715 C CB . ILE A 226 ? 0.4190 0.4339 0.3061 -0.0069 -0.0171 0.0621 226 ILE A CB 1716 C CG1 . ILE A 226 ? 0.4327 0.4405 0.3180 -0.0060 -0.0222 0.0660 226 ILE A CG1 1717 C CG2 . ILE A 226 ? 0.4043 0.4237 0.2896 -0.0045 -0.0183 0.0577 226 ILE A CG2 1718 C CD1 . ILE A 226 ? 0.4439 0.4495 0.3184 -0.0060 -0.0249 0.0698 226 ILE A CD1 1719 N N . PRO A 227 ? 0.4124 0.4414 0.2894 -0.0115 -0.0065 0.0599 227 PRO A N 1720 C CA . PRO A 227 ? 0.4116 0.4478 0.2912 -0.0114 -0.0029 0.0549 227 PRO A CA 1721 C C . PRO A 227 ? 0.4028 0.4417 0.2853 -0.0081 -0.0051 0.0494 227 PRO A C 1722 O O . PRO A 227 ? 0.4045 0.4485 0.2907 -0.0077 -0.0028 0.0448 227 PRO A O 1723 C CB . PRO A 227 ? 0.4300 0.4702 0.3005 -0.0138 -0.0002 0.0567 227 PRO A CB 1724 C CG . PRO A 227 ? 0.4344 0.4702 0.2962 -0.0134 -0.0041 0.0610 227 PRO A CG 1725 C CD . PRO A 227 ? 0.4386 0.4664 0.3045 -0.0128 -0.0074 0.0643 227 PRO A CD 1726 N N . SER A 228 ? 0.4056 0.4412 0.2870 -0.0058 -0.0097 0.0497 228 SER A N 1727 C CA . SER A 228 ? 0.3980 0.4358 0.2829 -0.0028 -0.0120 0.0445 228 SER A CA 1728 C C . SER A 228 ? 0.3756 0.4117 0.2705 -0.0021 -0.0123 0.0420 228 SER A C 1729 O O . SER A 228 ? 0.3573 0.3903 0.2558 -0.0035 -0.0113 0.0444 228 SER A O 1730 C CB . SER A 228 ? 0.4234 0.4585 0.3036 -0.0006 -0.0170 0.0455 228 SER A CB 1731 O OG . SER A 228 ? 0.4539 0.4897 0.3238 -0.0014 -0.0172 0.0486 228 SER A OG 1732 N N . ARG A 229 ? 0.3633 0.4016 0.2626 0.0000 -0.0138 0.0372 229 ARG A N 1733 C CA . ARG A 229 ? 0.3502 0.3871 0.2582 0.0004 -0.0144 0.0347 229 ARG A CA 1734 C C . ARG A 229 ? 0.3433 0.3807 0.2535 0.0028 -0.0180 0.0310 229 ARG A C 1735 O O . ARG A 229 ? 0.3585 0.3985 0.2648 0.0043 -0.0193 0.0291 229 ARG A O 1736 C CB . ARG A 229 ? 0.3498 0.3898 0.2627 -0.0006 -0.0110 0.0317 229 ARG A CB 1737 C CG . ARG A 229 ? 0.3589 0.3991 0.2715 -0.0029 -0.0073 0.0343 229 ARG A CG 1738 C CD . ARG A 229 ? 0.3709 0.4067 0.2871 -0.0041 -0.0073 0.0373 229 ARG A CD 1739 N NE . ARG A 229 ? 0.3746 0.4110 0.2920 -0.0063 -0.0037 0.0389 229 ARG A NE 1740 C CZ . ARG A 229 ? 0.3855 0.4209 0.2987 -0.0081 -0.0022 0.0429 229 ARG A CZ 1741 N NH1 . ARG A 229 ? 0.3905 0.4237 0.2972 -0.0081 -0.0040 0.0463 229 ARG A NH1 1742 N NH2 . ARG A 229 ? 0.3717 0.4084 0.2871 -0.0100 0.0010 0.0434 229 ARG A NH2 1743 N N . ILE A 230 ? 0.3362 0.3715 0.2529 0.0032 -0.0194 0.0298 230 ILE A N 1744 C CA . ILE A 230 ? 0.3275 0.3642 0.2486 0.0049 -0.0218 0.0253 230 ILE A CA 1745 C C . ILE A 230 ? 0.3209 0.3591 0.2492 0.0035 -0.0194 0.0223 230 ILE A C 1746 O O . ILE A 230 ? 0.3078 0.3441 0.2393 0.0019 -0.0177 0.0239 230 ILE A O 1747 C CB . ILE A 230 ? 0.3313 0.3652 0.2546 0.0062 -0.0256 0.0257 230 ILE A CB 1748 C CG1 . ILE A 230 ? 0.3463 0.3783 0.2621 0.0078 -0.0288 0.0285 230 ILE A CG1 1749 C CG2 . ILE A 230 ? 0.3323 0.3683 0.2617 0.0074 -0.0273 0.0205 230 ILE A CG2 1750 C CD1 . ILE A 230 ? 0.3565 0.3844 0.2738 0.0092 -0.0329 0.0300 230 ILE A CD1 1751 N N . SER A 231 ? 0.3176 0.3587 0.2479 0.0041 -0.0195 0.0181 231 SER A N 1752 C CA . SER A 231 ? 0.3084 0.3502 0.2450 0.0028 -0.0179 0.0153 231 SER A CA 1753 C C . SER A 231 ? 0.2954 0.3375 0.2368 0.0034 -0.0203 0.0121 231 SER A C 1754 O O . SER A 231 ? 0.2902 0.3340 0.2306 0.0053 -0.0228 0.0097 231 SER A O 1755 C CB . SER A 231 ? 0.3134 0.3578 0.2496 0.0027 -0.0164 0.0129 231 SER A CB 1756 O OG . SER A 231 ? 0.3278 0.3724 0.2613 0.0017 -0.0138 0.0153 231 SER A OG 1757 N N . ILE A 232 ? 0.2891 0.3301 0.2357 0.0017 -0.0194 0.0118 232 ILE A N 1758 C CA . ILE A 232 ? 0.2830 0.3248 0.2347 0.0018 -0.0212 0.0087 232 ILE A CA 1759 C C . ILE A 232 ? 0.2927 0.3363 0.2488 0.0002 -0.0202 0.0051 232 ILE A C 1760 O O . ILE A 232 ? 0.2833 0.3260 0.2405 -0.0017 -0.0177 0.0058 232 ILE A O 1761 C CB . ILE A 232 ? 0.2786 0.3186 0.2333 0.0007 -0.0210 0.0104 232 ILE A CB 1762 C CG1 . ILE A 232 ? 0.2835 0.3212 0.2345 0.0023 -0.0226 0.0139 232 ILE A CG1 1763 C CG2 . ILE A 232 ? 0.2711 0.3131 0.2319 0.0004 -0.0222 0.0065 232 ILE A CG2 1764 C CD1 . ILE A 232 ? 0.3026 0.3406 0.2518 0.0050 -0.0265 0.0127 232 ILE A CD1 1765 N N . TYR A 233 ? 0.2781 0.3239 0.2369 0.0010 -0.0222 0.0012 233 TYR A N 1766 C CA . TYR A 233 ? 0.2856 0.3330 0.2489 -0.0006 -0.0215 -0.0024 233 TYR A CA 1767 C C . TYR A 233 ? 0.2786 0.3280 0.2473 -0.0012 -0.0227 -0.0056 233 TYR A C 1768 O O . TYR A 233 ? 0.2767 0.3265 0.2456 0.0004 -0.0247 -0.0057 233 TYR A O 1769 C CB . TYR A 233 ? 0.2912 0.3405 0.2530 0.0009 -0.0227 -0.0050 233 TYR A CB 1770 C CG . TYR A 233 ? 0.3025 0.3508 0.2597 0.0013 -0.0212 -0.0026 233 TYR A CG 1771 C CD1 . TYR A 233 ? 0.3061 0.3543 0.2575 0.0033 -0.0218 -0.0001 233 TYR A CD1 1772 C CD2 . TYR A 233 ? 0.3112 0.3586 0.2701 -0.0004 -0.0193 -0.0029 233 TYR A CD2 1773 C CE1 . TYR A 233 ? 0.3078 0.3560 0.2555 0.0034 -0.0201 0.0016 233 TYR A CE1 1774 C CE2 . TYR A 233 ? 0.3118 0.3588 0.2674 0.0000 -0.0181 -0.0014 233 TYR A CE2 1775 C CZ . TYR A 233 ? 0.3226 0.3704 0.2727 0.0019 -0.0183 0.0006 233 TYR A CZ 1776 O OH . TYR A 233 ? 0.3408 0.3892 0.2881 0.0021 -0.0167 0.0016 233 TYR A OH 1777 N N . TRP A 234 ? 0.2733 0.3238 0.2463 -0.0039 -0.0214 -0.0083 234 TRP A N 1778 C CA . TRP A 234 ? 0.2747 0.3281 0.2533 -0.0050 -0.0221 -0.0120 234 TRP A CA 1779 C C . TRP A 234 ? 0.2729 0.3283 0.2551 -0.0066 -0.0219 -0.0161 234 TRP A C 1780 O O . TRP A 234 ? 0.2826 0.3364 0.2638 -0.0079 -0.0208 -0.0155 234 TRP A O 1781 C CB . TRP A 234 ? 0.2877 0.3407 0.2687 -0.0077 -0.0201 -0.0107 234 TRP A CB 1782 C CG . TRP A 234 ? 0.3041 0.3557 0.2857 -0.0116 -0.0172 -0.0098 234 TRP A CG 1783 C CD1 . TRP A 234 ? 0.3119 0.3653 0.2976 -0.0151 -0.0159 -0.0126 234 TRP A CD1 1784 C CD2 . TRP A 234 ? 0.3230 0.3709 0.3011 -0.0126 -0.0154 -0.0057 234 TRP A CD2 1785 N NE1 . TRP A 234 ? 0.3308 0.3812 0.3149 -0.0181 -0.0137 -0.0100 234 TRP A NE1 1786 C CE2 . TRP A 234 ? 0.3230 0.3702 0.3030 -0.0166 -0.0135 -0.0061 234 TRP A CE2 1787 C CE3 . TRP A 234 ? 0.3355 0.3809 0.3094 -0.0108 -0.0152 -0.0019 234 TRP A CE3 1788 C CZ2 . TRP A 234 ? 0.3501 0.3937 0.3277 -0.0182 -0.0119 -0.0029 234 TRP A CZ2 1789 C CZ3 . TRP A 234 ? 0.3568 0.3993 0.3289 -0.0125 -0.0133 0.0008 234 TRP A CZ3 1790 C CH2 . TRP A 234 ? 0.3567 0.3982 0.3308 -0.0160 -0.0119 0.0003 234 TRP A CH2 1791 N N . THR A 235 ? 0.2715 0.3306 0.2584 -0.0065 -0.0234 -0.0204 235 THR A N 1792 C CA . THR A 235 ? 0.2755 0.3371 0.2667 -0.0082 -0.0234 -0.0248 235 THR A CA 1793 C C . THR A 235 ? 0.2833 0.3487 0.2806 -0.0104 -0.0229 -0.0285 235 THR A C 1794 O O . THR A 235 ? 0.2682 0.3359 0.2674 -0.0082 -0.0249 -0.0301 235 THR A O 1795 C CB . THR A 235 ? 0.2815 0.3450 0.2723 -0.0045 -0.0266 -0.0279 235 THR A CB 1796 O OG1 . THR A 235 ? 0.2743 0.3351 0.2588 -0.0021 -0.0271 -0.0247 235 THR A OG1 1797 C CG2 . THR A 235 ? 0.2843 0.3502 0.2799 -0.0064 -0.0265 -0.0325 235 THR A CG2 1798 N N . ILE A 236 ? 0.2830 0.3494 0.2838 -0.0148 -0.0206 -0.0301 236 ILE A N 1799 C CA . ILE A 236 ? 0.2972 0.3682 0.3041 -0.0176 -0.0197 -0.0343 236 ILE A CA 1800 C C . ILE A 236 ? 0.2992 0.3739 0.3110 -0.0178 -0.0209 -0.0398 236 ILE A C 1801 O O . ILE A 236 ? 0.3261 0.3989 0.3373 -0.0193 -0.0204 -0.0397 236 ILE A O 1802 C CB . ILE A 236 ? 0.3062 0.3765 0.3135 -0.0230 -0.0159 -0.0325 236 ILE A CB 1803 C CG1 . ILE A 236 ? 0.3185 0.3863 0.3222 -0.0225 -0.0150 -0.0280 236 ILE A CG1 1804 C CG2 . ILE A 236 ? 0.3029 0.3791 0.3168 -0.0265 -0.0146 -0.0375 236 ILE A CG2 1805 C CD1 . ILE A 236 ? 0.3341 0.3993 0.3357 -0.0271 -0.0118 -0.0247 236 ILE A CD1 1806 N N . VAL A 237 ? 0.2994 0.3791 0.3162 -0.0162 -0.0228 -0.0448 237 VAL A N 1807 C CA . VAL A 237 ? 0.3035 0.3874 0.3256 -0.0160 -0.0244 -0.0506 237 VAL A CA 1808 C C . VAL A 237 ? 0.3179 0.4075 0.3474 -0.0203 -0.0223 -0.0556 237 VAL A C 1809 O O . VAL A 237 ? 0.3143 0.4077 0.3472 -0.0199 -0.0226 -0.0579 237 VAL A O 1810 C CB . VAL A 237 ? 0.3010 0.3867 0.3234 -0.0101 -0.0290 -0.0532 237 VAL A CB 1811 C CG1 . VAL A 237 ? 0.2991 0.3892 0.3272 -0.0096 -0.0308 -0.0597 237 VAL A CG1 1812 C CG2 . VAL A 237 ? 0.3005 0.3809 0.3148 -0.0063 -0.0306 -0.0482 237 VAL A CG2 1813 N N . LYS A 238 ? 0.3422 0.4325 0.3744 -0.0246 -0.0203 -0.0574 238 LYS A N 1814 C CA . LYS A 238 ? 0.3578 0.4536 0.3967 -0.0298 -0.0177 -0.0619 238 LYS A CA 1815 C C . LYS A 238 ? 0.3563 0.4591 0.4029 -0.0278 -0.0200 -0.0696 238 LYS A C 1816 O O . LYS A 238 ? 0.3688 0.4715 0.4155 -0.0232 -0.0237 -0.0715 238 LYS A O 1817 C CB . LYS A 238 ? 0.3855 0.4789 0.4245 -0.0352 -0.0151 -0.0611 238 LYS A CB 1818 C CG . LYS A 238 ? 0.4124 0.4983 0.4442 -0.0371 -0.0134 -0.0539 238 LYS A CG 1819 C CD . LYS A 238 ? 0.4162 0.5017 0.4454 -0.0400 -0.0106 -0.0505 238 LYS A CD 1820 C CE . LYS A 238 ? 0.4392 0.5282 0.4720 -0.0471 -0.0069 -0.0527 238 LYS A CE 1821 N NZ . LYS A 238 ? 0.4312 0.5201 0.4609 -0.0498 -0.0042 -0.0495 238 LYS A NZ 1822 N N . PRO A 239 ? 0.3607 0.4702 0.4139 -0.0315 -0.0180 -0.0744 239 PRO A N 1823 C CA . PRO A 239 ? 0.3658 0.4826 0.4276 -0.0305 -0.0198 -0.0825 239 PRO A CA 1824 C C . PRO A 239 ? 0.3739 0.4900 0.4374 -0.0309 -0.0208 -0.0846 239 PRO A C 1825 O O . PRO A 239 ? 0.3731 0.4854 0.4342 -0.0354 -0.0181 -0.0816 239 PRO A O 1826 C CB . PRO A 239 ? 0.3745 0.4978 0.4421 -0.0368 -0.0157 -0.0863 239 PRO A CB 1827 C CG . PRO A 239 ? 0.3673 0.4876 0.4295 -0.0382 -0.0134 -0.0808 239 PRO A CG 1828 C CD . PRO A 239 ? 0.3670 0.4780 0.4202 -0.0369 -0.0138 -0.0730 239 PRO A CD 1829 N N . GLY A 240 ? 0.3892 0.5084 0.4565 -0.0261 -0.0249 -0.0896 240 GLY A N 1830 C CA . GLY A 240 ? 0.4014 0.5206 0.4709 -0.0258 -0.0263 -0.0924 240 GLY A CA 1831 C C . GLY A 240 ? 0.3961 0.5082 0.4578 -0.0220 -0.0285 -0.0873 240 GLY A C 1832 O O . GLY A 240 ? 0.4146 0.5267 0.4779 -0.0206 -0.0305 -0.0899 240 GLY A O 1833 N N . ASP A 241 ? 0.3969 0.5033 0.4507 -0.0204 -0.0282 -0.0804 241 ASP A N 1834 C CA . ASP A 241 ? 0.3807 0.4812 0.4271 -0.0166 -0.0302 -0.0758 241 ASP A CA 1835 C C . ASP A 241 ? 0.3803 0.4810 0.4235 -0.0097 -0.0346 -0.0759 241 ASP A C 1836 O O . ASP A 241 ? 0.3770 0.4821 0.4244 -0.0078 -0.0365 -0.0796 241 ASP A O 1837 C CB . ASP A 241 ? 0.3777 0.4716 0.4172 -0.0192 -0.0271 -0.0684 241 ASP A CB 1838 C CG . ASP A 241 ? 0.3985 0.4872 0.4331 -0.0180 -0.0278 -0.0652 241 ASP A CG 1839 O OD1 . ASP A 241 ? 0.3988 0.4880 0.4325 -0.0135 -0.0311 -0.0673 241 ASP A OD1 1840 O OD2 . ASP A 241 ? 0.3739 0.4578 0.4055 -0.0215 -0.0251 -0.0608 241 ASP A OD2 1841 N N . ILE A 242 ? 0.3729 0.4693 0.4092 -0.0062 -0.0364 -0.0721 242 ILE A N 1842 C CA . ILE A 242 ? 0.3801 0.4762 0.4123 0.0000 -0.0408 -0.0719 242 ILE A CA 1843 C C . ILE A 242 ? 0.3675 0.4575 0.3901 0.0016 -0.0404 -0.0646 242 ILE A C 1844 O O . ILE A 242 ? 0.3683 0.4553 0.3881 -0.0001 -0.0384 -0.0621 242 ILE A O 1845 C CB . ILE A 242 ? 0.3994 0.4980 0.4335 0.0029 -0.0442 -0.0768 242 ILE A CB 1846 C CG1 . ILE A 242 ? 0.4110 0.5161 0.4551 0.0016 -0.0450 -0.0847 242 ILE A CG1 1847 C CG2 . ILE A 242 ? 0.4180 0.5157 0.4461 0.0091 -0.0488 -0.0757 242 ILE A CG2 1848 C CD1 . ILE A 242 ? 0.4282 0.5360 0.4756 0.0031 -0.0473 -0.0898 242 ILE A CD1 1849 N N . LEU A 243 ? 0.3526 0.4410 0.3708 0.0048 -0.0422 -0.0615 243 LEU A N 1850 C CA . LEU A 243 ? 0.3425 0.4258 0.3515 0.0069 -0.0423 -0.0552 243 LEU A CA 1851 C C . LEU A 243 ? 0.3605 0.4444 0.3655 0.0115 -0.0462 -0.0565 243 LEU A C 1852 O O . LEU A 243 ? 0.3737 0.4605 0.3808 0.0147 -0.0501 -0.0604 243 LEU A O 1853 C CB . LEU A 243 ? 0.3320 0.4132 0.3380 0.0081 -0.0427 -0.0512 243 LEU A CB 1854 C CG . LEU A 243 ? 0.3320 0.4079 0.3291 0.0091 -0.0418 -0.0442 243 LEU A CG 1855 C CD1 . LEU A 243 ? 0.3233 0.3967 0.3197 0.0048 -0.0371 -0.0409 243 LEU A CD1 1856 C CD2 . LEU A 243 ? 0.3269 0.4009 0.3217 0.0111 -0.0435 -0.0412 243 LEU A CD2 1857 N N . LEU A 244 ? 0.3512 0.4326 0.3504 0.0119 -0.0452 -0.0535 244 LEU A N 1858 C CA . LEU A 244 ? 0.3586 0.4404 0.3523 0.0161 -0.0484 -0.0539 244 LEU A CA 1859 C C . LEU A 244 ? 0.3566 0.4344 0.3411 0.0169 -0.0472 -0.0474 244 LEU A C 1860 O O . LEU A 244 ? 0.3404 0.4157 0.3236 0.0142 -0.0437 -0.0444 244 LEU A O 1861 C CB . LEU A 244 ? 0.3694 0.4537 0.3663 0.0157 -0.0485 -0.0585 244 LEU A CB 1862 C CG . LEU A 244 ? 0.3735 0.4600 0.3664 0.0200 -0.0521 -0.0610 244 LEU A CG 1863 C CD1 . LEU A 244 ? 0.4029 0.4913 0.3947 0.0240 -0.0569 -0.0630 244 LEU A CD1 1864 C CD2 . LEU A 244 ? 0.3728 0.4622 0.3717 0.0190 -0.0522 -0.0667 244 LEU A CD2 1865 N N . ILE A 245 ? 0.3509 0.4279 0.3291 0.0205 -0.0503 -0.0453 245 ILE A N 1866 C CA . ILE A 245 ? 0.3540 0.4276 0.3231 0.0214 -0.0495 -0.0392 245 ILE A CA 1867 C C . ILE A 245 ? 0.3778 0.4531 0.3405 0.0246 -0.0520 -0.0402 245 ILE A C 1868 O O . ILE A 245 ? 0.3801 0.4573 0.3419 0.0278 -0.0563 -0.0428 245 ILE A O 1869 C CB . ILE A 245 ? 0.3585 0.4291 0.3245 0.0224 -0.0510 -0.0351 245 ILE A CB 1870 C CG1 . ILE A 245 ? 0.3566 0.4265 0.3295 0.0194 -0.0486 -0.0351 245 ILE A CG1 1871 C CG2 . ILE A 245 ? 0.3683 0.4355 0.3249 0.0228 -0.0499 -0.0288 245 ILE A CG2 1872 C CD1 . ILE A 245 ? 0.3638 0.4308 0.3351 0.0202 -0.0500 -0.0315 245 ILE A CD1 1873 N N . ASN A 246 ? 0.3788 0.4537 0.3370 0.0238 -0.0495 -0.0381 246 ASN A N 1874 C CA . ASN A 246 ? 0.3992 0.4767 0.3518 0.0263 -0.0511 -0.0397 246 ASN A CA 1875 C C . ASN A 246 ? 0.4010 0.4765 0.3444 0.0262 -0.0491 -0.0339 246 ASN A C 1876 O O . ASN A 246 ? 0.3906 0.4644 0.3344 0.0237 -0.0453 -0.0314 246 ASN A O 1877 C CB . ASN A 246 ? 0.4252 0.5054 0.3837 0.0251 -0.0496 -0.0445 246 ASN A CB 1878 C CG . ASN A 246 ? 0.4674 0.5516 0.4227 0.0279 -0.0518 -0.0484 246 ASN A CG 1879 O OD1 . ASN A 246 ? 0.4859 0.5719 0.4446 0.0270 -0.0504 -0.0516 246 ASN A OD1 1880 N ND2 . ASN A 246 ? 0.5024 0.5880 0.4514 0.0312 -0.0554 -0.0483 246 ASN A ND2 1881 N N . SER A 247 ? 0.3997 0.4751 0.3347 0.0288 -0.0518 -0.0316 247 SER A N 1882 C CA . SER A 247 ? 0.4058 0.4790 0.3318 0.0282 -0.0500 -0.0256 247 SER A CA 1883 C C . SER A 247 ? 0.4271 0.5019 0.3433 0.0310 -0.0531 -0.0246 247 SER A C 1884 O O . SER A 247 ? 0.4251 0.5007 0.3409 0.0337 -0.0576 -0.0271 247 SER A O 1885 C CB . SER A 247 ? 0.4053 0.4736 0.3310 0.0268 -0.0493 -0.0203 247 SER A CB 1886 O OG . SER A 247 ? 0.4243 0.4903 0.3414 0.0261 -0.0477 -0.0144 247 SER A OG 1887 N N . THR A 248 ? 0.4322 0.5072 0.3403 0.0301 -0.0507 -0.0210 248 THR A N 1888 C CA . THR A 248 ? 0.4633 0.5393 0.3603 0.0319 -0.0530 -0.0187 248 THR A CA 1889 C C . THR A 248 ? 0.4601 0.5317 0.3492 0.0303 -0.0516 -0.0110 248 THR A C 1890 O O . THR A 248 ? 0.4668 0.5391 0.3455 0.0305 -0.0521 -0.0080 248 THR A O 1891 C CB . THR A 248 ? 0.4850 0.5668 0.3785 0.0322 -0.0513 -0.0220 248 THR A CB 1892 O OG1 . THR A 248 ? 0.5034 0.5857 0.3995 0.0295 -0.0462 -0.0211 248 THR A OG1 1893 C CG2 . THR A 248 ? 0.4868 0.5730 0.3870 0.0344 -0.0537 -0.0298 248 THR A CG2 1894 N N . GLY A 249 ? 0.4289 0.4960 0.3227 0.0284 -0.0499 -0.0079 249 GLY A N 1895 C CA . GLY A 249 ? 0.4250 0.4877 0.3129 0.0265 -0.0484 -0.0009 249 GLY A CA 1896 C C . GLY A 249 ? 0.4076 0.4681 0.3022 0.0236 -0.0442 0.0007 249 GLY A C 1897 O O . GLY A 249 ? 0.3971 0.4596 0.2998 0.0228 -0.0421 -0.0032 249 GLY A O 1898 N N . ASN A 250 ? 0.3999 0.4559 0.2908 0.0220 -0.0432 0.0067 250 ASN A N 1899 C CA . ASN A 250 ? 0.3876 0.4415 0.2834 0.0192 -0.0391 0.0090 250 ASN A CA 1900 C C . ASN A 250 ? 0.3710 0.4230 0.2769 0.0190 -0.0397 0.0068 250 ASN A C 1901 O O . ASN A 250 ? 0.3582 0.4089 0.2688 0.0168 -0.0364 0.0078 250 ASN A O 1902 C CB . ASN A 250 ? 0.3793 0.4371 0.2760 0.0174 -0.0345 0.0073 250 ASN A CB 1903 C CG . ASN A 250 ? 0.3983 0.4589 0.2853 0.0171 -0.0332 0.0091 250 ASN A CG 1904 O OD1 . ASN A 250 ? 0.4128 0.4774 0.2961 0.0190 -0.0349 0.0060 250 ASN A OD1 1905 N ND2 . ASN A 250 ? 0.3820 0.4412 0.2651 0.0147 -0.0300 0.0138 250 ASN A ND2 1906 N N . LEU A 251 ? 0.3728 0.4249 0.2817 0.0214 -0.0439 0.0037 251 LEU A N 1907 C CA . LEU A 251 ? 0.3621 0.4137 0.2807 0.0212 -0.0445 0.0007 251 LEU A CA 1908 C C . LEU A 251 ? 0.3596 0.4064 0.2788 0.0211 -0.0462 0.0044 251 LEU A C 1909 O O . LEU A 251 ? 0.3458 0.3901 0.2605 0.0231 -0.0503 0.0065 251 LEU A O 1910 C CB . LEU A 251 ? 0.3556 0.4102 0.2780 0.0236 -0.0482 -0.0051 251 LEU A CB 1911 C CG . LEU A 251 ? 0.3532 0.4082 0.2858 0.0234 -0.0491 -0.0089 251 LEU A CG 1912 C CD1 . LEU A 251 ? 0.3350 0.3911 0.2740 0.0202 -0.0445 -0.0103 251 LEU A CD1 1913 C CD2 . LEU A 251 ? 0.3372 0.3955 0.2731 0.0260 -0.0531 -0.0147 251 LEU A CD2 1914 N N . ILE A 252 ? 0.3360 0.3815 0.2612 0.0188 -0.0434 0.0051 252 ILE A N 1915 C CA . ILE A 252 ? 0.3323 0.3743 0.2609 0.0188 -0.0450 0.0069 252 ILE A CA 1916 C C . ILE A 252 ? 0.3257 0.3704 0.2638 0.0192 -0.0462 0.0011 252 ILE A C 1917 O O . ILE A 252 ? 0.3137 0.3603 0.2577 0.0169 -0.0428 -0.0009 252 ILE A O 1918 C CB . ILE A 252 ? 0.3385 0.3779 0.2674 0.0159 -0.0410 0.0111 252 ILE A CB 1919 C CG1 . ILE A 252 ? 0.3543 0.3920 0.2741 0.0152 -0.0393 0.0163 252 ILE A CG1 1920 C CG2 . ILE A 252 ? 0.3363 0.3723 0.2692 0.0160 -0.0428 0.0126 252 ILE A CG2 1921 C CD1 . ILE A 252 ? 0.3601 0.3943 0.2725 0.0169 -0.0433 0.0201 252 ILE A CD1 1922 N N . ALA A 253 ? 0.3230 0.3680 0.2625 0.0220 -0.0510 -0.0014 253 ALA A N 1923 C CA . ALA A 253 ? 0.3223 0.3712 0.2704 0.0226 -0.0524 -0.0079 253 ALA A CA 1924 C C . ALA A 253 ? 0.3116 0.3602 0.2676 0.0216 -0.0524 -0.0093 253 ALA A C 1925 O O . ALA A 253 ? 0.3105 0.3552 0.2653 0.0220 -0.0536 -0.0058 253 ALA A O 1926 C CB . ALA A 253 ? 0.3290 0.3792 0.2755 0.0263 -0.0578 -0.0109 253 ALA A CB 1927 N N . PRO A 254 ? 0.3087 0.3614 0.2730 0.0202 -0.0510 -0.0148 254 PRO A N 1928 C CA . PRO A 254 ? 0.3050 0.3589 0.2774 0.0193 -0.0511 -0.0174 254 PRO A CA 1929 C C . PRO A 254 ? 0.3104 0.3647 0.2859 0.0229 -0.0570 -0.0206 254 PRO A C 1930 O O . PRO A 254 ? 0.3032 0.3588 0.2769 0.0256 -0.0604 -0.0228 254 PRO A O 1931 C CB . PRO A 254 ? 0.3038 0.3625 0.2829 0.0166 -0.0479 -0.0223 254 PRO A CB 1932 C CG . PRO A 254 ? 0.3106 0.3714 0.2872 0.0180 -0.0492 -0.0247 254 PRO A CG 1933 C CD . PRO A 254 ? 0.3081 0.3651 0.2748 0.0195 -0.0497 -0.0193 254 PRO A CD 1934 N N . ARG A 255 ? 0.3162 0.3695 0.2965 0.0231 -0.0583 -0.0209 255 ARG A N 1935 C CA . ARG A 255 ? 0.3238 0.3780 0.3090 0.0266 -0.0643 -0.0249 255 ARG A CA 1936 C C . ARG A 255 ? 0.3197 0.3804 0.3160 0.0256 -0.0636 -0.0326 255 ARG A C 1937 O O . ARG A 255 ? 0.3359 0.3986 0.3383 0.0282 -0.0682 -0.0373 255 ARG A O 1938 C CB . ARG A 255 ? 0.3310 0.3801 0.3154 0.0280 -0.0670 -0.0211 255 ARG A CB 1939 C CG . ARG A 255 ? 0.3419 0.3843 0.3155 0.0290 -0.0683 -0.0134 255 ARG A CG 1940 C CD . ARG A 255 ? 0.3533 0.3902 0.3271 0.0307 -0.0723 -0.0104 255 ARG A CD 1941 N NE . ARG A 255 ? 0.3679 0.3983 0.3310 0.0310 -0.0732 -0.0027 255 ARG A NE 1942 C CZ . ARG A 255 ? 0.3914 0.4183 0.3475 0.0339 -0.0782 -0.0005 255 ARG A CZ 1943 N NH1 . ARG A 255 ? 0.3808 0.4099 0.3397 0.0372 -0.0833 -0.0055 255 ARG A NH1 1944 N NH2 . ARG A 255 ? 0.4038 0.4251 0.3497 0.0333 -0.0782 0.0067 255 ARG A NH2 1945 N N . GLY A 256 ? 0.3028 0.3670 0.3017 0.0216 -0.0581 -0.0341 256 GLY A N 1946 C CA . GLY A 256 ? 0.2978 0.3684 0.3066 0.0194 -0.0564 -0.0408 256 GLY A CA 1947 C C . GLY A 256 ? 0.2857 0.3572 0.2946 0.0143 -0.0499 -0.0390 256 GLY A C 1948 O O . GLY A 256 ? 0.2854 0.3534 0.2874 0.0131 -0.0473 -0.0340 256 GLY A O 1949 N N . TYR A 257 ? 0.2789 0.3550 0.2955 0.0115 -0.0476 -0.0433 257 TYR A N 1950 C CA . TYR A 257 ? 0.2795 0.3569 0.2964 0.0064 -0.0417 -0.0421 257 TYR A CA 1951 C C . TYR A 257 ? 0.2676 0.3465 0.2888 0.0043 -0.0397 -0.0425 257 TYR A C 1952 O O . TYR A 257 ? 0.2637 0.3451 0.2908 0.0061 -0.0426 -0.0464 257 TYR A O 1953 C CB . TYR A 257 ? 0.2825 0.3652 0.3043 0.0034 -0.0395 -0.0474 257 TYR A CB 1954 C CG . TYR A 257 ? 0.2860 0.3755 0.3174 0.0035 -0.0410 -0.0551 257 TYR A CG 1955 C CD1 . TYR A 257 ? 0.3036 0.3954 0.3383 0.0074 -0.0459 -0.0598 257 TYR A CD1 1956 C CD2 . TYR A 257 ? 0.2900 0.3841 0.3273 -0.0001 -0.0379 -0.0580 257 TYR A CD2 1957 C CE1 . TYR A 257 ? 0.3103 0.4089 0.3546 0.0077 -0.0475 -0.0675 257 TYR A CE1 1958 C CE2 . TYR A 257 ? 0.2946 0.3958 0.3412 -0.0001 -0.0392 -0.0657 257 TYR A CE2 1959 C CZ . TYR A 257 ? 0.3059 0.4094 0.3564 0.0038 -0.0440 -0.0705 257 TYR A CZ 1960 O OH . TYR A 257 ? 0.3150 0.4260 0.3754 0.0039 -0.0454 -0.0787 257 TYR A OH 1961 N N . PHE A 258 ? 0.2553 0.3327 0.2736 0.0004 -0.0350 -0.0390 258 PHE A N 1962 C CA . PHE A 258 ? 0.2542 0.3340 0.2763 -0.0025 -0.0323 -0.0397 258 PHE A CA 1963 C C . PHE A 258 ? 0.2757 0.3618 0.3034 -0.0069 -0.0290 -0.0449 258 PHE A C 1964 O O . PHE A 258 ? 0.2764 0.3627 0.3024 -0.0090 -0.0271 -0.0450 258 PHE A O 1965 C CB . PHE A 258 ? 0.2396 0.3143 0.2554 -0.0044 -0.0292 -0.0331 258 PHE A CB 1966 C CG . PHE A 258 ? 0.2311 0.3001 0.2420 -0.0009 -0.0318 -0.0281 258 PHE A CG 1967 C CD1 . PHE A 258 ? 0.2321 0.3005 0.2457 0.0003 -0.0333 -0.0278 258 PHE A CD1 1968 C CD2 . PHE A 258 ? 0.2405 0.3049 0.2445 0.0011 -0.0329 -0.0239 258 PHE A CD2 1969 C CE1 . PHE A 258 ? 0.2316 0.2942 0.2407 0.0031 -0.0357 -0.0228 258 PHE A CE1 1970 C CE2 . PHE A 258 ? 0.2392 0.2985 0.2383 0.0037 -0.0350 -0.0190 258 PHE A CE2 1971 C CZ . PHE A 258 ? 0.2385 0.2966 0.2402 0.0047 -0.0365 -0.0184 258 PHE A CZ 1972 N N . LYS A 259 ? 0.3071 0.3985 0.3415 -0.0082 -0.0285 -0.0495 259 LYS A N 1973 C CA . LYS A 259 ? 0.3497 0.4473 0.3886 -0.0134 -0.0244 -0.0536 259 LYS A CA 1974 C C . LYS A 259 ? 0.3589 0.4527 0.3915 -0.0176 -0.0200 -0.0478 259 LYS A C 1975 O O . LYS A 259 ? 0.3645 0.4533 0.3923 -0.0164 -0.0199 -0.0424 259 LYS A O 1976 C CB . LYS A 259 ? 0.3861 0.4904 0.4330 -0.0139 -0.0246 -0.0594 259 LYS A CB 1977 C CG . LYS A 259 ? 0.4261 0.5361 0.4811 -0.0110 -0.0284 -0.0670 259 LYS A CG 1978 C CD . LYS A 259 ? 0.4665 0.5842 0.5272 -0.0155 -0.0253 -0.0732 259 LYS A CD 1979 C CE . LYS A 259 ? 0.4885 0.6149 0.5599 -0.0143 -0.0275 -0.0823 259 LYS A CE 1980 N NZ . LYS A 259 ? 0.5342 0.6588 0.6081 -0.0075 -0.0341 -0.0843 259 LYS A NZ 1981 N N . ILE A 260 ? 0.3595 0.4553 0.3920 -0.0223 -0.0165 -0.0487 260 ILE A N 1982 C CA . ILE A 260 ? 0.3538 0.4464 0.3810 -0.0265 -0.0126 -0.0439 260 ILE A CA 1983 C C . ILE A 260 ? 0.3519 0.4511 0.3835 -0.0322 -0.0090 -0.0480 260 ILE A C 1984 O O . ILE A 260 ? 0.3634 0.4674 0.3993 -0.0345 -0.0082 -0.0528 260 ILE A O 1985 C CB . ILE A 260 ? 0.3703 0.4568 0.3914 -0.0267 -0.0123 -0.0393 260 ILE A CB 1986 C CG1 . ILE A 260 ? 0.3799 0.4627 0.3958 -0.0308 -0.0089 -0.0344 260 ILE A CG1 1987 C CG2 . ILE A 260 ? 0.3803 0.4696 0.4045 -0.0278 -0.0126 -0.0434 260 ILE A CG2 1988 C CD1 . ILE A 260 ? 0.3799 0.4555 0.3893 -0.0293 -0.0094 -0.0288 260 ILE A CD1 1989 N N . ARG A 261 ? 0.3413 0.4413 0.3719 -0.0344 -0.0068 -0.0466 261 ARG A N 1990 C CA . ARG A 261 ? 0.3529 0.4600 0.3872 -0.0398 -0.0032 -0.0507 261 ARG A CA 1991 C C . ARG A 261 ? 0.3392 0.4426 0.3668 -0.0448 0.0004 -0.0454 261 ARG A C 1992 O O . ARG A 261 ? 0.3223 0.4181 0.3435 -0.0434 -0.0001 -0.0391 261 ARG A O 1993 C CB . ARG A 261 ? 0.3790 0.4913 0.4185 -0.0381 -0.0040 -0.0544 261 ARG A CB 1994 C CG . ARG A 261 ? 0.4153 0.5312 0.4621 -0.0330 -0.0083 -0.0601 261 ARG A CG 1995 C CD . ARG A 261 ? 0.4532 0.5758 0.5070 -0.0321 -0.0089 -0.0656 261 ARG A CD 1996 N NE . ARG A 261 ? 0.4718 0.5973 0.5330 -0.0269 -0.0137 -0.0711 261 ARG A NE 1997 C CZ . ARG A 261 ? 0.5209 0.6530 0.5891 -0.0271 -0.0146 -0.0782 261 ARG A CZ 1998 N NH1 . ARG A 261 ? 0.5253 0.6621 0.5943 -0.0325 -0.0107 -0.0806 261 ARG A NH1 1999 N NH2 . ARG A 261 ? 0.5283 0.6622 0.6029 -0.0217 -0.0197 -0.0828 261 ARG A NH2 2000 N N . SER A 262 ? 0.3490 0.4576 0.3779 -0.0508 0.0040 -0.0479 262 SER A N 2001 C CA . SER A 262 ? 0.3591 0.4644 0.3814 -0.0556 0.0072 -0.0429 262 SER A CA 2002 C C . SER A 262 ? 0.3405 0.4523 0.3648 -0.0584 0.0095 -0.0457 262 SER A C 2003 O O . SER A 262 ? 0.3219 0.4425 0.3531 -0.0595 0.0103 -0.0526 262 SER A O 2004 C CB . SER A 262 ? 0.3883 0.4924 0.4081 -0.0613 0.0096 -0.0419 262 SER A CB 2005 O OG . SER A 262 ? 0.4264 0.5392 0.4517 -0.0657 0.0121 -0.0481 262 SER A OG 2006 N N . GLY A 263 ? 0.3179 0.4257 0.3364 -0.0593 0.0106 -0.0407 263 GLY A N 2007 C CA . GLY A 263 ? 0.3077 0.4214 0.3272 -0.0620 0.0128 -0.0430 263 GLY A CA 2008 C C . GLY A 263 ? 0.3052 0.4126 0.3178 -0.0617 0.0130 -0.0366 263 GLY A C 2009 O O . GLY A 263 ? 0.3218 0.4209 0.3282 -0.0616 0.0124 -0.0305 263 GLY A O 2010 N N . LYS A 264 ? 0.3081 0.3341 0.3219 -0.0012 -0.0451 -0.0237 264 LYS A N 2011 C CA . LYS A 264 ? 0.3022 0.3233 0.3161 -0.0007 -0.0444 -0.0223 264 LYS A CA 2012 C C . LYS A 264 ? 0.2469 0.2608 0.2609 0.0019 -0.0461 -0.0201 264 LYS A C 2013 O O . LYS A 264 ? 0.2401 0.2510 0.2549 0.0030 -0.0464 -0.0193 264 LYS A O 2014 C CB . LYS A 264 ? 0.3362 0.3630 0.3529 0.0005 -0.0448 -0.0249 264 LYS A CB 2015 C CG . LYS A 264 ? 0.3964 0.4318 0.4133 -0.0022 -0.0433 -0.0273 264 LYS A CG 2016 C CD . LYS A 264 ? 0.4374 0.4704 0.4503 -0.0070 -0.0404 -0.0258 264 LYS A CD 2017 C CE . LYS A 264 ? 0.4772 0.5187 0.4896 -0.0105 -0.0393 -0.0280 264 LYS A CE 2018 N NZ . LYS A 264 ? 0.5052 0.5501 0.5162 -0.0125 -0.0396 -0.0284 264 LYS A NZ 2019 N N . SER A 265 ? 0.2234 0.2347 0.2363 0.0026 -0.0474 -0.0191 265 SER A N 2020 C CA . SER A 265 ? 0.2140 0.2188 0.2266 0.0048 -0.0492 -0.0171 265 SER A CA 2021 C C . SER A 265 ? 0.2105 0.2088 0.2209 0.0030 -0.0472 -0.0136 265 SER A C 2022 O O . SER A 265 ? 0.2022 0.2000 0.2105 0.0004 -0.0446 -0.0127 265 SER A O 2023 C CB . SER A 265 ? 0.2206 0.2250 0.2326 0.0064 -0.0515 -0.0174 265 SER A CB 2024 O OG . SER A 265 ? 0.2155 0.2266 0.2298 0.0087 -0.0536 -0.0207 265 SER A OG 2025 N N . SER A 266 ? 0.2009 0.1944 0.2115 0.0045 -0.0487 -0.0118 266 SER A N 2026 C CA . SER A 266 ? 0.2011 0.1894 0.2099 0.0032 -0.0471 -0.0084 266 SER A CA 2027 C C . SER A 266 ? 0.2007 0.1843 0.2092 0.0046 -0.0495 -0.0065 266 SER A C 2028 O O . SER A 266 ? 0.1976 0.1809 0.2065 0.0066 -0.0524 -0.0078 266 SER A O 2029 C CB . SER A 266 ? 0.2020 0.1907 0.2116 0.0023 -0.0452 -0.0079 266 SER A CB 2030 O OG . SER A 266 ? 0.2044 0.1892 0.2121 0.0010 -0.0432 -0.0047 266 SER A OG 2031 N N . ILE A 267 ? 0.2003 0.1802 0.2077 0.0035 -0.0483 -0.0034 267 ILE A N 2032 C CA . ILE A 267 ? 0.2047 0.1802 0.2113 0.0039 -0.0502 -0.0010 267 ILE A CA 2033 C C . ILE A 267 ? 0.2103 0.1847 0.2173 0.0030 -0.0492 0.0011 267 ILE A C 2034 O O . ILE A 267 ? 0.2030 0.1791 0.2102 0.0019 -0.0463 0.0017 267 ILE A O 2035 C CB . ILE A 267 ? 0.2049 0.1779 0.2090 0.0031 -0.0494 0.0009 267 ILE A CB 2036 C CG1 . ILE A 267 ? 0.2158 0.1844 0.2187 0.0032 -0.0517 0.0033 267 ILE A CG1 2037 C CG2 . ILE A 267 ? 0.2074 0.1807 0.2102 0.0015 -0.0457 0.0027 267 ILE A CG2 2038 C CD1 . ILE A 267 ? 0.2194 0.1857 0.2199 0.0028 -0.0518 0.0046 267 ILE A CD1 2039 N N . MET A 268 ? 0.2144 0.1859 0.2214 0.0033 -0.0517 0.0023 268 MET A N 2040 C CA . MET A 268 ? 0.2231 0.1939 0.2305 0.0022 -0.0512 0.0045 268 MET A CA 2041 C C . MET A 268 ? 0.2302 0.1971 0.2360 0.0012 -0.0532 0.0074 268 MET A C 2042 O O . MET A 268 ? 0.2348 0.1985 0.2391 0.0020 -0.0562 0.0069 268 MET A O 2043 C CB . MET A 268 ? 0.2264 0.1981 0.2354 0.0030 -0.0526 0.0025 268 MET A CB 2044 C CG . MET A 268 ? 0.2340 0.2058 0.2437 0.0016 -0.0518 0.0045 268 MET A CG 2045 S SD . MET A 268 ? 0.2427 0.2151 0.2537 0.0027 -0.0535 0.0018 268 MET A SD 2046 C CE . MET A 268 ? 0.2329 0.2108 0.2456 0.0031 -0.0504 -0.0011 268 MET A CE 2047 N N . ARG A 269 ? 0.2285 0.1960 0.2343 -0.0003 -0.0515 0.0105 269 ARG A N 2048 C CA . ARG A 269 ? 0.2374 0.2022 0.2416 -0.0019 -0.0533 0.0136 269 ARG A CA 2049 C C . ARG A 269 ? 0.2377 0.2014 0.2424 -0.0026 -0.0553 0.0138 269 ARG A C 2050 O O . ARG A 269 ? 0.2309 0.1975 0.2375 -0.0030 -0.0537 0.0140 269 ARG A O 2051 C CB . ARG A 269 ? 0.2501 0.2173 0.2543 -0.0033 -0.0504 0.0169 269 ARG A CB 2052 C CG . ARG A 269 ? 0.2587 0.2264 0.2617 -0.0026 -0.0481 0.0168 269 ARG A CG 2053 C CD . ARG A 269 ? 0.2691 0.2386 0.2713 -0.0035 -0.0457 0.0202 269 ARG A CD 2054 N NE . ARG A 269 ? 0.2810 0.2502 0.2814 -0.0027 -0.0437 0.0200 269 ARG A NE 2055 C CZ . ARG A 269 ? 0.2866 0.2572 0.2866 -0.0017 -0.0407 0.0191 269 ARG A CZ 2056 N NH1 . ARG A 269 ? 0.2901 0.2628 0.2916 -0.0012 -0.0392 0.0184 269 ARG A NH1 2057 N NH2 . ARG A 269 ? 0.2901 0.2594 0.2877 -0.0012 -0.0392 0.0189 269 ARG A NH2 2058 N N . SER A 270 ? 0.2385 0.1973 0.2408 -0.0028 -0.0591 0.0138 270 SER A N 2059 C CA . SER A 270 ? 0.2517 0.2082 0.2534 -0.0036 -0.0615 0.0140 270 SER A CA 2060 C C . SER A 270 ? 0.2712 0.2212 0.2688 -0.0048 -0.0656 0.0152 270 SER A C 2061 O O . SER A 270 ? 0.2707 0.2174 0.2662 -0.0035 -0.0674 0.0141 270 SER A O 2062 C CB . SER A 270 ? 0.2499 0.2065 0.2526 -0.0012 -0.0624 0.0101 270 SER A CB 2063 O OG . SER A 270 ? 0.2514 0.2045 0.2525 -0.0018 -0.0651 0.0102 270 SER A OG 2064 N N . ASP A 271 ? 0.2830 0.2310 0.2791 -0.0073 -0.0672 0.0174 271 ASP A N 2065 C CA . ASP A 271 ? 0.3104 0.2509 0.3015 -0.0086 -0.0716 0.0183 271 ASP A CA 2066 C C . ASP A 271 ? 0.3204 0.2559 0.3093 -0.0073 -0.0749 0.0160 271 ASP A C 2067 O O . ASP A 271 ? 0.3278 0.2560 0.3116 -0.0087 -0.0788 0.0169 271 ASP A O 2068 C CB . ASP A 271 ? 0.3285 0.2691 0.3180 -0.0130 -0.0718 0.0228 271 ASP A CB 2069 C CG . ASP A 271 ? 0.3477 0.2912 0.3377 -0.0140 -0.0697 0.0249 271 ASP A CG 2070 O OD1 . ASP A 271 ? 0.3544 0.2959 0.3435 -0.0119 -0.0700 0.0232 271 ASP A OD1 2071 O OD2 . ASP A 271 ? 0.3749 0.3229 0.3660 -0.0167 -0.0677 0.0282 271 ASP A OD2 2072 N N . ALA A 272 ? 0.3001 0.2390 0.2921 -0.0046 -0.0734 0.0129 272 ALA A N 2073 C CA . ALA A 272 ? 0.3078 0.2425 0.2977 -0.0030 -0.0762 0.0106 272 ALA A CA 2074 C C . ALA A 272 ? 0.3146 0.2430 0.3006 0.0001 -0.0798 0.0079 272 ALA A C 2075 O O . ALA A 272 ? 0.2966 0.2271 0.2840 0.0024 -0.0790 0.0062 272 ALA A O 2076 C CB . ALA A 272 ? 0.3035 0.2443 0.2979 -0.0011 -0.0734 0.0080 272 ALA A CB 2077 N N . PRO A 273 ? 0.3293 0.2497 0.3100 0.0003 -0.0840 0.0074 273 PRO A N 2078 C CA . PRO A 273 ? 0.3454 0.2595 0.3219 0.0041 -0.0876 0.0046 273 PRO A CA 2079 C C . PRO A 273 ? 0.3403 0.2592 0.3201 0.0091 -0.0865 0.0000 273 PRO A C 2080 O O . PRO A 273 ? 0.3231 0.2474 0.3066 0.0093 -0.0841 -0.0010 273 PRO A O 2081 C CB . PRO A 273 ? 0.3629 0.2670 0.3324 0.0030 -0.0921 0.0052 273 PRO A CB 2082 C CG . PRO A 273 ? 0.3670 0.2745 0.3389 0.0001 -0.0903 0.0068 273 PRO A CG 2083 C CD . PRO A 273 ? 0.3494 0.2659 0.3273 -0.0027 -0.0857 0.0094 273 PRO A CD 2084 N N . ILE A 274 ? 0.3540 0.2714 0.3324 0.0129 -0.0882 -0.0024 274 ILE A N 2085 C CA . ILE A 274 ? 0.3603 0.2827 0.3414 0.0176 -0.0876 -0.0068 274 ILE A CA 2086 C C . ILE A 274 ? 0.3807 0.2965 0.3569 0.0212 -0.0916 -0.0094 274 ILE A C 2087 O O . ILE A 274 ? 0.3832 0.2895 0.3529 0.0221 -0.0958 -0.0090 274 ILE A O 2088 C CB . ILE A 274 ? 0.3733 0.2989 0.3559 0.0201 -0.0873 -0.0082 274 ILE A CB 2089 C CG1 . ILE A 274 ? 0.3834 0.3162 0.3710 0.0168 -0.0828 -0.0060 274 ILE A CG1 2090 C CG2 . ILE A 274 ? 0.3702 0.3017 0.3553 0.0251 -0.0871 -0.0128 274 ILE A CG2 2091 C CD1 . ILE A 274 ? 0.4084 0.3425 0.3962 0.0179 -0.0827 -0.0063 274 ILE A CD1 2092 N N . GLY A 275 ? 0.3795 0.2998 0.3583 0.0231 -0.0903 -0.0120 275 GLY A N 2093 C CA . GLY A 275 ? 0.3966 0.3110 0.3706 0.0268 -0.0938 -0.0147 275 GLY A CA 2094 C C . GLY A 275 ? 0.3971 0.3172 0.3731 0.0328 -0.0938 -0.0195 275 GLY A C 2095 O O . GLY A 275 ? 0.3667 0.2971 0.3489 0.0332 -0.0903 -0.0208 275 GLY A O 2096 N N . LYS A 276 ? 0.4102 0.3236 0.3805 0.0373 -0.0977 -0.0221 276 LYS A N 2097 C CA . LYS A 276 ? 0.4233 0.3424 0.3951 0.0435 -0.0980 -0.0269 276 LYS A CA 2098 C C . LYS A 276 ? 0.4149 0.3390 0.3894 0.0435 -0.0958 -0.0286 276 LYS A C 2099 O O . LYS A 276 ? 0.4328 0.3501 0.4023 0.0451 -0.0984 -0.0296 276 LYS A O 2100 C CB . LYS A 276 ? 0.4733 0.3826 0.4371 0.0490 -0.1034 -0.0291 276 LYS A CB 2101 C CG . LYS A 276 ? 0.5163 0.4208 0.4774 0.0491 -0.1055 -0.0276 276 LYS A CG 2102 C CD . LYS A 276 ? 0.5710 0.4684 0.5252 0.0559 -0.1105 -0.0305 276 LYS A CD 2103 C CE . LYS A 276 ? 0.5983 0.4891 0.5487 0.0552 -0.1129 -0.0285 276 LYS A CE 2104 N NZ . LYS A 276 ? 0.6328 0.5346 0.5907 0.0539 -0.1094 -0.0281 276 LYS A NZ 2105 N N . CYS A 277 ? 0.3780 0.3133 0.3598 0.0412 -0.0912 -0.0286 277 CYS A N 2106 C CA . CYS A 277 ? 0.3715 0.3124 0.3564 0.0404 -0.0886 -0.0299 277 CYS A CA 2107 C C . CYS A 277 ? 0.3304 0.2844 0.3228 0.0394 -0.0841 -0.0309 277 CYS A C 2108 O O . CYS A 277 ? 0.3104 0.2681 0.3050 0.0393 -0.0832 -0.0305 277 CYS A O 2109 C CB . CYS A 277 ? 0.3983 0.3340 0.3820 0.0351 -0.0880 -0.0263 277 CYS A CB 2110 S SG . CYS A 277 ? 0.4538 0.3896 0.4401 0.0284 -0.0856 -0.0209 277 CYS A SG 2111 N N . ASN A 278 ? 0.3085 0.2690 0.3041 0.0386 -0.0814 -0.0323 278 ASN A N 2112 C CA . ASN A 278 ? 0.2968 0.2694 0.2985 0.0377 -0.0773 -0.0337 278 ASN A CA 2113 C C . ASN A 278 ? 0.2933 0.2684 0.2979 0.0327 -0.0738 -0.0315 278 ASN A C 2114 O O . ASN A 278 ? 0.2848 0.2582 0.2883 0.0323 -0.0738 -0.0319 278 ASN A O 2115 C CB . ASN A 278 ? 0.2977 0.2769 0.3000 0.0428 -0.0778 -0.0385 278 ASN A CB 2116 C CG . ASN A 278 ? 0.2959 0.2880 0.3038 0.0422 -0.0743 -0.0403 278 ASN A CG 2117 O OD1 . ASN A 278 ? 0.2983 0.2950 0.3095 0.0377 -0.0707 -0.0388 278 ASN A OD1 2118 N ND2 . ASN A 278 ? 0.2896 0.2876 0.2981 0.0467 -0.0755 -0.0436 278 ASN A ND2 2119 N N . SER A 279 ? 0.2854 0.2643 0.2932 0.0289 -0.0708 -0.0292 279 SER A N 2120 C CA . SER A 279 ? 0.2889 0.2704 0.2992 0.0244 -0.0673 -0.0271 279 SER A CA 2121 C C . SER A 279 ? 0.2740 0.2624 0.2878 0.0221 -0.0639 -0.0265 279 SER A C 2122 O O . SER A 279 ? 0.2621 0.2496 0.2759 0.0218 -0.0642 -0.0253 279 SER A O 2123 C CB . SER A 279 ? 0.3080 0.2814 0.3160 0.0213 -0.0682 -0.0230 279 SER A CB 2124 O OG . SER A 279 ? 0.3330 0.3092 0.3434 0.0175 -0.0649 -0.0210 279 SER A OG 2125 N N . GLU A 280 ? 0.2677 0.2626 0.2841 0.0202 -0.0607 -0.0274 280 GLU A N 2126 C CA . GLU A 280 ? 0.2733 0.2745 0.2921 0.0178 -0.0576 -0.0272 280 GLU A CA 2127 C C . GLU A 280 ? 0.2551 0.2528 0.2737 0.0142 -0.0558 -0.0232 280 GLU A C 2128 O O . GLU A 280 ? 0.2406 0.2407 0.2599 0.0130 -0.0543 -0.0226 280 GLU A O 2129 C CB . GLU A 280 ? 0.2920 0.3003 0.3126 0.0164 -0.0549 -0.0292 280 GLU A CB 2130 C CG . GLU A 280 ? 0.3276 0.3421 0.3490 0.0198 -0.0559 -0.0335 280 GLU A CG 2131 C CD . GLU A 280 ? 0.3543 0.3760 0.3772 0.0213 -0.0558 -0.0357 280 GLU A CD 2132 O OE1 . GLU A 280 ? 0.3685 0.3913 0.3920 0.0188 -0.0543 -0.0341 280 GLU A OE1 2133 O OE2 . GLU A 280 ? 0.3697 0.3962 0.3930 0.0251 -0.0573 -0.0391 280 GLU A OE2 2134 N N . CYS A 281 ? 0.2466 0.2390 0.2642 0.0125 -0.0559 -0.0205 281 CYS A N 2135 C CA . CYS A 281 ? 0.2342 0.2245 0.2518 0.0093 -0.0539 -0.0168 281 CYS A CA 2136 C C . CYS A 281 ? 0.2312 0.2152 0.2471 0.0093 -0.0560 -0.0139 281 CYS A C 2137 O O . CYS A 281 ? 0.2313 0.2105 0.2454 0.0099 -0.0586 -0.0133 281 CYS A O 2138 C CB . CYS A 281 ? 0.2405 0.2307 0.2583 0.0072 -0.0522 -0.0155 281 CYS A CB 2139 S SG . CYS A 281 ? 0.2455 0.2338 0.2632 0.0041 -0.0496 -0.0111 281 CYS A SG 2140 N N . ILE A 282 ? 0.2179 0.2016 0.2337 0.0083 -0.0550 -0.0122 282 ILE A N 2141 C CA . ILE A 282 ? 0.2217 0.2001 0.2358 0.0078 -0.0567 -0.0092 282 ILE A CA 2142 C C . ILE A 282 ? 0.2141 0.1922 0.2285 0.0049 -0.0542 -0.0055 282 ILE A C 2143 O O . ILE A 282 ? 0.2064 0.1878 0.2217 0.0039 -0.0511 -0.0053 282 ILE A O 2144 C CB . ILE A 282 ? 0.2197 0.1976 0.2331 0.0093 -0.0579 -0.0099 282 ILE A CB 2145 C CG1 . ILE A 282 ? 0.2281 0.2069 0.2412 0.0127 -0.0605 -0.0137 282 ILE A CG1 2146 C CG2 . ILE A 282 ? 0.2213 0.1935 0.2325 0.0084 -0.0596 -0.0067 282 ILE A CG2 2147 C CD1 . ILE A 282 ? 0.2314 0.2115 0.2442 0.0145 -0.0615 -0.0150 282 ILE A CD1 2148 N N . THR A 283 ? 0.2142 0.1883 0.2274 0.0037 -0.0555 -0.0026 283 THR A N 2149 C CA . THR A 283 ? 0.2104 0.1846 0.2237 0.0014 -0.0536 0.0010 283 THR A CA 2150 C C . THR A 283 ? 0.2153 0.1852 0.2267 0.0008 -0.0559 0.0035 283 THR A C 2151 O O . THR A 283 ? 0.2164 0.1824 0.2259 0.0018 -0.0592 0.0024 283 THR A O 2152 C CB . THR A 283 ? 0.2116 0.1864 0.2256 -0.0001 -0.0528 0.0028 283 THR A CB 2153 O OG1 . THR A 283 ? 0.2138 0.1847 0.2263 -0.0009 -0.0558 0.0042 283 THR A OG1 2154 C CG2 . THR A 283 ? 0.2151 0.1928 0.2303 0.0004 -0.0515 0.0001 283 THR A CG2 2155 N N . PRO A 284 ? 0.2178 0.1883 0.2291 -0.0008 -0.0543 0.0068 284 PRO A N 2156 C CA . PRO A 284 ? 0.2266 0.1936 0.2359 -0.0020 -0.0563 0.0094 284 PRO A CA 2157 C C . PRO A 284 ? 0.2419 0.2052 0.2495 -0.0035 -0.0594 0.0108 284 PRO A C 2158 O O . PRO A 284 ? 0.2421 0.2010 0.2469 -0.0044 -0.0622 0.0121 284 PRO A O 2159 C CB . PRO A 284 ? 0.2276 0.1977 0.2377 -0.0035 -0.0533 0.0126 284 PRO A CB 2160 C CG . PRO A 284 ? 0.2209 0.1946 0.2324 -0.0023 -0.0500 0.0109 284 PRO A CG 2161 C CD . PRO A 284 ? 0.2167 0.1911 0.2293 -0.0014 -0.0505 0.0079 284 PRO A CD 2162 N N . ASN A 285 ? 0.2458 0.2104 0.2544 -0.0040 -0.0591 0.0105 285 ASN A N 2163 C CA . ASN A 285 ? 0.2683 0.2291 0.2748 -0.0056 -0.0621 0.0116 285 ASN A CA 2164 C C . ASN A 285 ? 0.2736 0.2294 0.2777 -0.0035 -0.0654 0.0084 285 ASN A C 2165 O O . ASN A 285 ? 0.3034 0.2543 0.3045 -0.0046 -0.0684 0.0090 285 ASN A O 2166 C CB . ASN A 285 ? 0.2829 0.2469 0.2913 -0.0068 -0.0606 0.0124 285 ASN A CB 2167 C CG . ASN A 285 ? 0.3035 0.2730 0.3143 -0.0080 -0.0571 0.0151 285 ASN A CG 2168 O OD1 . ASN A 285 ? 0.2875 0.2603 0.3000 -0.0066 -0.0541 0.0142 285 ASN A OD1 2169 N ND2 . ASN A 285 ? 0.3737 0.3442 0.3843 -0.0106 -0.0575 0.0184 285 ASN A ND2 2170 N N . GLY A 286 ? 0.2595 0.2167 0.2646 -0.0005 -0.0648 0.0050 286 GLY A N 2171 C CA . GLY A 286 ? 0.2585 0.2127 0.2618 0.0022 -0.0674 0.0014 286 GLY A CA 2172 C C . GLY A 286 ? 0.2555 0.2149 0.2617 0.0042 -0.0652 -0.0018 286 GLY A C 2173 O O . GLY A 286 ? 0.2395 0.2041 0.2487 0.0030 -0.0617 -0.0011 286 GLY A O 2174 N N . SER A 287 ? 0.2565 0.2147 0.2616 0.0073 -0.0672 -0.0053 287 SER A N 2175 C CA . SER A 287 ? 0.2605 0.2241 0.2680 0.0091 -0.0654 -0.0087 287 SER A CA 2176 C C . SER A 287 ? 0.2591 0.2231 0.2671 0.0075 -0.0647 -0.0081 287 SER A C 2177 O O . SER A 287 ? 0.2673 0.2261 0.2727 0.0061 -0.0669 -0.0063 287 SER A O 2178 C CB . SER A 287 ? 0.2696 0.2324 0.2757 0.0132 -0.0680 -0.0126 287 SER A CB 2179 O OG . SER A 287 ? 0.2750 0.2384 0.2810 0.0147 -0.0684 -0.0132 287 SER A OG 2180 N N . ILE A 288 ? 0.2509 0.2207 0.2617 0.0072 -0.0616 -0.0095 288 ILE A N 2181 C CA . ILE A 288 ? 0.2566 0.2270 0.2678 0.0059 -0.0609 -0.0092 288 ILE A CA 2182 C C . ILE A 288 ? 0.2634 0.2379 0.2756 0.0080 -0.0601 -0.0132 288 ILE A C 2183 O O . ILE A 288 ? 0.2732 0.2526 0.2871 0.0092 -0.0586 -0.0154 288 ILE A O 2184 C CB . ILE A 288 ? 0.2498 0.2229 0.2629 0.0028 -0.0578 -0.0061 288 ILE A CB 2185 C CG1 . ILE A 288 ? 0.2469 0.2256 0.2623 0.0028 -0.0543 -0.0071 288 ILE A CG1 2186 C CG2 . ILE A 288 ? 0.2597 0.2297 0.2719 0.0008 -0.0586 -0.0021 288 ILE A CG2 2187 C CD1 . ILE A 288 ? 0.2457 0.2268 0.2623 0.0005 -0.0512 -0.0046 288 ILE A CD1 2188 N N . PRO A 289 ? 0.2811 0.2541 0.2922 0.0081 -0.0610 -0.0141 289 PRO A N 2189 C CA . PRO A 289 ? 0.2841 0.2620 0.2964 0.0097 -0.0599 -0.0178 289 PRO A CA 2190 C C . PRO A 289 ? 0.2750 0.2592 0.2902 0.0076 -0.0558 -0.0175 289 PRO A C 2191 O O . PRO A 289 ? 0.2715 0.2551 0.2872 0.0049 -0.0542 -0.0144 289 PRO A O 2192 C CB . PRO A 289 ? 0.2911 0.2653 0.3013 0.0094 -0.0614 -0.0179 289 PRO A CB 2193 C CG . PRO A 289 ? 0.3042 0.2714 0.3118 0.0078 -0.0639 -0.0146 289 PRO A CG 2194 C CD . PRO A 289 ? 0.2971 0.2642 0.3057 0.0065 -0.0633 -0.0119 289 PRO A CD 2195 N N . ASN A 290 ? 0.2683 0.2583 0.2848 0.0088 -0.0544 -0.0208 290 ASN A N 2196 C CA . ASN A 290 ? 0.2666 0.2620 0.2848 0.0065 -0.0509 -0.0209 290 ASN A CA 2197 C C . ASN A 290 ? 0.2631 0.2622 0.2815 0.0060 -0.0495 -0.0231 290 ASN A C 2198 O O . ASN A 290 ? 0.2751 0.2794 0.2944 0.0046 -0.0470 -0.0244 290 ASN A O 2199 C CB . ASN A 290 ? 0.2714 0.2709 0.2906 0.0072 -0.0499 -0.0222 290 ASN A CB 2200 C CG . ASN A 290 ? 0.2787 0.2832 0.2985 0.0100 -0.0509 -0.0263 290 ASN A CG 2201 O OD1 . ASN A 290 ? 0.2849 0.2885 0.3039 0.0122 -0.0527 -0.0283 290 ASN A OD1 2202 N ND2 . ASN A 290 ? 0.2654 0.2750 0.2863 0.0102 -0.0498 -0.0277 290 ASN A ND2 2203 N N . ASP A 291 ? 0.2664 0.2624 0.2836 0.0066 -0.0511 -0.0234 291 ASP A N 2204 C CA . ASP A 291 ? 0.2789 0.2778 0.2961 0.0059 -0.0499 -0.0252 291 ASP A CA 2205 C C . ASP A 291 ? 0.2624 0.2617 0.2799 0.0023 -0.0472 -0.0227 291 ASP A C 2206 O O . ASP A 291 ? 0.2710 0.2745 0.2886 0.0009 -0.0450 -0.0241 291 ASP A O 2207 C CB . ASP A 291 ? 0.2976 0.2924 0.3128 0.0077 -0.0526 -0.0262 291 ASP A CB 2208 C CG . ASP A 291 ? 0.3272 0.3144 0.3407 0.0067 -0.0548 -0.0227 291 ASP A CG 2209 O OD1 . ASP A 291 ? 0.3643 0.3478 0.3769 0.0077 -0.0568 -0.0216 291 ASP A OD1 2210 O OD2 . ASP A 291 ? 0.3664 0.3514 0.3791 0.0047 -0.0546 -0.0210 291 ASP A OD2 2211 N N . LYS A 292 ? 0.2418 0.2367 0.2590 0.0009 -0.0474 -0.0190 292 LYS A N 2212 C CA . LYS A 292 ? 0.2288 0.2234 0.2458 -0.0017 -0.0452 -0.0164 292 LYS A CA 2213 C C . LYS A 292 ? 0.2122 0.2092 0.2295 -0.0030 -0.0425 -0.0156 292 LYS A C 2214 O O . LYS A 292 ? 0.2162 0.2140 0.2340 -0.0021 -0.0427 -0.0159 292 LYS A O 2215 C CB . LYS A 292 ? 0.2329 0.2228 0.2495 -0.0025 -0.0466 -0.0127 292 LYS A CB 2216 C CG . LYS A 292 ? 0.2458 0.2324 0.2612 -0.0020 -0.0494 -0.0131 292 LYS A CG 2217 C CD . LYS A 292 ? 0.2516 0.2340 0.2665 -0.0033 -0.0510 -0.0092 292 LYS A CD 2218 C CE . LYS A 292 ? 0.2720 0.2500 0.2847 -0.0030 -0.0542 -0.0096 292 LYS A CE 2219 N NZ . LYS A 292 ? 0.2893 0.2645 0.3004 -0.0003 -0.0568 -0.0119 292 LYS A NZ 2220 N N . PRO A 293 ? 0.2033 0.2009 0.2196 -0.0051 -0.0402 -0.0147 293 PRO A N 2221 C CA . PRO A 293 ? 0.1990 0.1980 0.2144 -0.0063 -0.0378 -0.0142 293 PRO A CA 2222 C C . PRO A 293 ? 0.1922 0.1882 0.2073 -0.0064 -0.0373 -0.0107 293 PRO A C 2223 O O . PRO A 293 ? 0.1883 0.1846 0.2024 -0.0068 -0.0359 -0.0104 293 PRO A O 2224 C CB . PRO A 293 ? 0.2037 0.2035 0.2172 -0.0084 -0.0358 -0.0147 293 PRO A CB 2225 C CG . PRO A 293 ? 0.2030 0.2007 0.2168 -0.0084 -0.0369 -0.0136 293 PRO A CG 2226 C CD . PRO A 293 ? 0.2036 0.2011 0.2191 -0.0063 -0.0397 -0.0149 293 PRO A CD 2227 N N . PHE A 294 ? 0.1864 0.1798 0.2022 -0.0061 -0.0386 -0.0081 294 PHE A N 2228 C CA . PHE A 294 ? 0.1830 0.1743 0.1986 -0.0060 -0.0382 -0.0045 294 PHE A CA 2229 C C . PHE A 294 ? 0.1806 0.1702 0.1975 -0.0052 -0.0409 -0.0031 294 PHE A C 2230 O O . PHE A 294 ? 0.1785 0.1673 0.1959 -0.0047 -0.0431 -0.0045 294 PHE A O 2231 C CB . PHE A 294 ? 0.1854 0.1760 0.2001 -0.0070 -0.0369 -0.0021 294 PHE A CB 2232 C CG . PHE A 294 ? 0.1863 0.1774 0.1986 -0.0081 -0.0347 -0.0035 294 PHE A CG 2233 C CD1 . PHE A 294 ? 0.1935 0.1844 0.2037 -0.0084 -0.0328 -0.0039 294 PHE A CD1 2234 C CD2 . PHE A 294 ? 0.1950 0.1865 0.2068 -0.0091 -0.0347 -0.0044 294 PHE A CD2 2235 C CE1 . PHE A 294 ? 0.1954 0.1860 0.2025 -0.0099 -0.0309 -0.0051 294 PHE A CE1 2236 C CE2 . PHE A 294 ? 0.1960 0.1876 0.2051 -0.0104 -0.0327 -0.0057 294 PHE A CE2 2237 C CZ . PHE A 294 ? 0.1955 0.1865 0.2021 -0.0109 -0.0308 -0.0060 294 PHE A CZ 2238 N N . GLN A 295 ? 0.1776 0.1663 0.1946 -0.0051 -0.0407 -0.0004 295 GLN A N 2239 C CA . GLN A 295 ? 0.1770 0.1639 0.1947 -0.0049 -0.0430 0.0014 295 GLN A CA 2240 C C . GLN A 295 ? 0.1817 0.1689 0.1995 -0.0053 -0.0420 0.0053 295 GLN A C 2241 O O . GLN A 295 ? 0.1739 0.1620 0.1909 -0.0051 -0.0395 0.0059 295 GLN A O 2242 C CB . GLN A 295 ? 0.1797 0.1656 0.1974 -0.0036 -0.0446 -0.0004 295 GLN A CB 2243 C CG . GLN A 295 ? 0.1715 0.1586 0.1889 -0.0031 -0.0428 -0.0009 295 GLN A CG 2244 C CD . GLN A 295 ? 0.1736 0.1596 0.1909 -0.0031 -0.0428 0.0019 295 GLN A CD 2245 O OE1 . GLN A 295 ? 0.1762 0.1608 0.1937 -0.0036 -0.0443 0.0044 295 GLN A OE1 2246 N NE2 . GLN A 295 ? 0.1677 0.1543 0.1842 -0.0027 -0.0410 0.0014 295 GLN A NE2 2247 N N . ASN A 296 ? 0.1853 0.1716 0.2036 -0.0061 -0.0439 0.0078 296 ASN A N 2248 C CA A ASN A 296 ? 0.1872 0.1748 0.2058 -0.0067 -0.0433 0.0115 296 ASN A CA 2249 C CA B ASN A 296 ? 0.1948 0.1824 0.2134 -0.0066 -0.0431 0.0115 296 ASN A CA 2250 C C . ASN A 296 ? 0.1964 0.1824 0.2149 -0.0071 -0.0454 0.0129 296 ASN A C 2251 O O . ASN A 296 ? 0.2080 0.1953 0.2268 -0.0082 -0.0457 0.0162 296 ASN A O 2252 C CB A ASN A 296 ? 0.1844 0.1735 0.2036 -0.0080 -0.0436 0.0137 296 ASN A CB 2253 C CB B ASN A 296 ? 0.2020 0.1916 0.2211 -0.0077 -0.0429 0.0140 296 ASN A CB 2254 C CG A ASN A 296 ? 0.1825 0.1747 0.2023 -0.0083 -0.0426 0.0176 296 ASN A CG 2255 C CG B ASN A 296 ? 0.2163 0.2047 0.2356 -0.0094 -0.0460 0.0152 296 ASN A CG 2256 O OD1 A ASN A 296 ? 0.1843 0.1776 0.2047 -0.0100 -0.0443 0.0201 296 ASN A OD1 2257 O OD1 B ASN A 296 ? 0.2275 0.2126 0.2460 -0.0095 -0.0483 0.0132 296 ASN A OD1 2258 N ND2 A ASN A 296 ? 0.1776 0.1713 0.1969 -0.0068 -0.0399 0.0182 296 ASN A ND2 2259 N ND2 B ASN A 296 ? 0.2232 0.2142 0.2433 -0.0108 -0.0461 0.0186 296 ASN A ND2 2260 N N . VAL A 297 ? 0.1967 0.1801 0.2145 -0.0063 -0.0470 0.0104 297 VAL A N 2261 C CA . VAL A 297 ? 0.1974 0.1783 0.2144 -0.0066 -0.0493 0.0114 297 VAL A CA 2262 C C . VAL A 297 ? 0.1980 0.1801 0.2150 -0.0062 -0.0476 0.0129 297 VAL A C 2263 O O . VAL A 297 ? 0.2007 0.1830 0.2174 -0.0073 -0.0481 0.0159 297 VAL A O 2264 C CB . VAL A 297 ? 0.2013 0.1786 0.2170 -0.0054 -0.0519 0.0081 297 VAL A CB 2265 C CG1 . VAL A 297 ? 0.2057 0.1796 0.2199 -0.0055 -0.0544 0.0091 297 VAL A CG1 2266 C CG2 . VAL A 297 ? 0.2072 0.1828 0.2223 -0.0057 -0.0538 0.0067 297 VAL A CG2 2267 N N . ASN A 298 ? 0.1904 0.1735 0.2074 -0.0047 -0.0454 0.0109 298 ASN A N 2268 C CA . ASN A 298 ? 0.1901 0.1736 0.2065 -0.0042 -0.0439 0.0121 298 ASN A CA 2269 C C . ASN A 298 ? 0.1874 0.1720 0.2032 -0.0031 -0.0411 0.0101 298 ASN A C 2270 O O . ASN A 298 ? 0.1806 0.1652 0.1964 -0.0027 -0.0412 0.0069 298 ASN A O 2271 C CB . ASN A 298 ? 0.1950 0.1757 0.2106 -0.0039 -0.0462 0.0114 298 ASN A CB 2272 C CG . ASN A 298 ? 0.1974 0.1782 0.2122 -0.0042 -0.0454 0.0140 298 ASN A CG 2273 O OD1 . ASN A 298 ? 0.1933 0.1755 0.2077 -0.0034 -0.0428 0.0141 298 ASN A OD1 2274 N ND2 . ASN A 298 ? 0.2108 0.1899 0.2249 -0.0054 -0.0478 0.0160 298 ASN A ND2 2275 N N . ARG A 299 ? 0.1906 0.1762 0.2055 -0.0028 -0.0387 0.0120 299 ARG A N 2276 C CA . ARG A 299 ? 0.1991 0.1844 0.2122 -0.0021 -0.0363 0.0104 299 ARG A CA 2277 C C . ARG A 299 ? 0.1915 0.1757 0.2040 -0.0018 -0.0369 0.0083 299 ARG A C 2278 O O . ARG A 299 ? 0.1759 0.1600 0.1869 -0.0017 -0.0355 0.0062 299 ARG A O 2279 C CB . ARG A 299 ? 0.2205 0.2063 0.2319 -0.0014 -0.0337 0.0130 299 ARG A CB 2280 C CG . ARG A 299 ? 0.2475 0.2333 0.2585 -0.0010 -0.0337 0.0153 299 ARG A CG 2281 C CD . ARG A 299 ? 0.2884 0.2749 0.2973 0.0001 -0.0310 0.0177 299 ARG A CD 2282 N NE . ARG A 299 ? 0.3015 0.2909 0.3117 0.0002 -0.0307 0.0198 299 ARG A NE 2283 C CZ . ARG A 299 ? 0.3315 0.3221 0.3399 0.0019 -0.0284 0.0215 299 ARG A CZ 2284 N NH1 . ARG A 299 ? 0.3385 0.3269 0.3433 0.0035 -0.0262 0.0214 299 ARG A NH1 2285 N NH2 . ARG A 299 ? 0.3412 0.3350 0.3513 0.0020 -0.0285 0.0234 299 ARG A NH2 2286 N N . ILE A 300 ? 0.1871 0.1702 0.2002 -0.0017 -0.0390 0.0089 300 ILE A N 2287 C CA . ILE A 300 ? 0.1902 0.1723 0.2028 -0.0012 -0.0401 0.0069 300 ILE A CA 2288 C C . ILE A 300 ? 0.1945 0.1768 0.2083 -0.0007 -0.0423 0.0038 300 ILE A C 2289 O O . ILE A 300 ? 0.1873 0.1684 0.2019 -0.0007 -0.0447 0.0042 300 ILE A O 2290 C CB . ILE A 300 ? 0.1947 0.1749 0.2067 -0.0012 -0.0415 0.0090 300 ILE A CB 2291 C CG1 . ILE A 300 ? 0.1976 0.1782 0.2083 -0.0013 -0.0391 0.0119 300 ILE A CG1 2292 C CG2 . ILE A 300 ? 0.1929 0.1719 0.2045 -0.0004 -0.0430 0.0068 300 ILE A CG2 2293 C CD1 . ILE A 300 ? 0.2038 0.1835 0.2142 -0.0018 -0.0404 0.0147 300 ILE A CD1 2294 N N . THR A 301 ? 0.2006 0.1845 0.2142 -0.0004 -0.0416 0.0009 301 THR A N 2295 C CA . THR A 301 ? 0.2076 0.1929 0.2224 0.0004 -0.0434 -0.0023 301 THR A CA 2296 C C . THR A 301 ? 0.2092 0.1964 0.2238 0.0011 -0.0437 -0.0049 301 THR A C 2297 O O . THR A 301 ? 0.2128 0.2004 0.2260 0.0003 -0.0418 -0.0045 301 THR A O 2298 C CB . THR A 301 ? 0.2159 0.2036 0.2314 -0.0001 -0.0423 -0.0038 301 THR A CB 2299 O OG1 . THR A 301 ? 0.2430 0.2328 0.2573 -0.0010 -0.0398 -0.0051 301 THR A OG1 2300 C CG2 . THR A 301 ? 0.2265 0.2130 0.2420 -0.0010 -0.0416 -0.0012 301 THR A CG2 2301 N N . TYR A 302 ? 0.2035 0.1919 0.2191 0.0027 -0.0460 -0.0075 302 TYR A N 2302 C CA . TYR A 302 ? 0.2041 0.1958 0.2201 0.0036 -0.0464 -0.0104 302 TYR A CA 2303 C C . TYR A 302 ? 0.2025 0.1977 0.2198 0.0050 -0.0476 -0.0137 302 TYR A C 2304 O O . TYR A 302 ? 0.2099 0.2030 0.2275 0.0065 -0.0498 -0.0140 302 TYR A O 2305 C CB . TYR A 302 ? 0.2079 0.1974 0.2233 0.0051 -0.0486 -0.0100 302 TYR A CB 2306 C CG . TYR A 302 ? 0.2088 0.2023 0.2245 0.0061 -0.0492 -0.0130 302 TYR A CG 2307 C CD1 . TYR A 302 ? 0.2158 0.2121 0.2328 0.0087 -0.0515 -0.0161 302 TYR A CD1 2308 C CD2 . TYR A 302 ? 0.2129 0.2079 0.2277 0.0047 -0.0474 -0.0127 302 TYR A CD2 2309 C CE1 . TYR A 302 ? 0.2136 0.2150 0.2313 0.0098 -0.0519 -0.0188 302 TYR A CE1 2310 C CE2 . TYR A 302 ? 0.2174 0.2170 0.2327 0.0053 -0.0479 -0.0153 302 TYR A CE2 2311 C CZ . TYR A 302 ? 0.2158 0.2191 0.2328 0.0079 -0.0502 -0.0183 302 TYR A CZ 2312 O OH . TYR A 302 ? 0.2275 0.2365 0.2453 0.0086 -0.0507 -0.0209 302 TYR A OH 2313 N N . GLY A 303 ? 0.2003 0.2009 0.2183 0.0044 -0.0461 -0.0162 303 GLY A N 2314 C CA . GLY A 303 ? 0.2041 0.2095 0.2234 0.0058 -0.0470 -0.0196 303 GLY A CA 2315 C C . GLY A 303 ? 0.2091 0.2165 0.2286 0.0040 -0.0449 -0.0200 303 GLY A C 2316 O O . GLY A 303 ? 0.2094 0.2152 0.2276 0.0014 -0.0425 -0.0180 303 GLY A O 2317 N N . ALA A 304 ? 0.2098 0.2205 0.2305 0.0054 -0.0459 -0.0227 304 ALA A N 2318 C CA . ALA A 304 ? 0.2128 0.2255 0.2335 0.0038 -0.0442 -0.0234 304 ALA A CA 2319 C C . ALA A 304 ? 0.2166 0.2235 0.2367 0.0037 -0.0447 -0.0209 304 ALA A C 2320 O O . ALA A 304 ? 0.2226 0.2275 0.2429 0.0057 -0.0469 -0.0216 304 ALA A O 2321 C CB . ALA A 304 ? 0.2190 0.2379 0.2411 0.0056 -0.0451 -0.0273 304 ALA A CB 2322 N N . CYS A 305 ? 0.2163 0.2202 0.2353 0.0013 -0.0428 -0.0180 305 CYS A N 2323 C CA . CYS A 305 ? 0.2200 0.2189 0.2386 0.0010 -0.0433 -0.0151 305 CYS A CA 2324 C C . CYS A 305 ? 0.2060 0.2050 0.2239 -0.0010 -0.0411 -0.0141 305 CYS A C 2325 O O . CYS A 305 ? 0.2062 0.2069 0.2228 -0.0028 -0.0387 -0.0143 305 CYS A O 2326 C CB . CYS A 305 ? 0.2351 0.2305 0.2529 0.0006 -0.0431 -0.0119 305 CYS A CB 2327 S SG . CYS A 305 ? 0.2690 0.2623 0.2870 0.0029 -0.0462 -0.0121 305 CYS A SG 2328 N N . PRO A 306 ? 0.1925 0.1889 0.2105 -0.0009 -0.0421 -0.0128 306 PRO A N 2329 C CA . PRO A 306 ? 0.1900 0.1857 0.2072 -0.0028 -0.0402 -0.0111 306 PRO A CA 2330 C C . PRO A 306 ? 0.1877 0.1816 0.2035 -0.0038 -0.0382 -0.0081 306 PRO A C 2331 O O . PRO A 306 ? 0.1914 0.1838 0.2074 -0.0031 -0.0389 -0.0066 306 PRO A O 2332 C CB . PRO A 306 ? 0.1924 0.1853 0.2100 -0.0024 -0.0422 -0.0097 306 PRO A CB 2333 C CG . PRO A 306 ? 0.1943 0.1867 0.2125 -0.0003 -0.0451 -0.0117 306 PRO A CG 2334 C CD . PRO A 306 ? 0.1935 0.1870 0.2120 0.0005 -0.0451 -0.0124 306 PRO A CD 2335 N N . ARG A 307 ? 0.1860 0.1797 0.2002 -0.0052 -0.0360 -0.0073 307 ARG A N 2336 C CA . ARG A 307 ? 0.1845 0.1761 0.1967 -0.0056 -0.0342 -0.0047 307 ARG A CA 2337 C C . ARG A 307 ? 0.1787 0.1684 0.1917 -0.0051 -0.0348 -0.0012 307 ARG A C 2338 O O . ARG A 307 ? 0.1772 0.1670 0.1911 -0.0053 -0.0356 -0.0007 307 ARG A O 2339 C CB . ARG A 307 ? 0.1890 0.1801 0.1981 -0.0072 -0.0318 -0.0051 307 ARG A CB 2340 C CG . ARG A 307 ? 0.1964 0.1897 0.2040 -0.0085 -0.0309 -0.0080 307 ARG A CG 2341 C CD . ARG A 307 ? 0.2016 0.1928 0.2047 -0.0104 -0.0285 -0.0077 307 ARG A CD 2342 N NE . ARG A 307 ? 0.2104 0.2034 0.2113 -0.0123 -0.0277 -0.0100 307 ARG A NE 2343 C CZ . ARG A 307 ? 0.2103 0.2021 0.2092 -0.0126 -0.0271 -0.0097 307 ARG A CZ 2344 N NH1 . ARG A 307 ? 0.2109 0.1998 0.2097 -0.0109 -0.0272 -0.0074 307 ARG A NH1 2345 N NH2 . ARG A 307 ? 0.2222 0.2163 0.2193 -0.0148 -0.0265 -0.0119 307 ARG A NH2 2346 N N . TYR A 308 ? 0.1755 0.1640 0.1880 -0.0045 -0.0343 0.0010 308 TYR A N 2347 C CA . TYR A 308 ? 0.1774 0.1653 0.1906 -0.0040 -0.0347 0.0044 308 TYR A CA 2348 C C . TYR A 308 ? 0.1793 0.1671 0.1910 -0.0042 -0.0329 0.0061 308 TYR A C 2349 O O . TYR A 308 ? 0.1810 0.1676 0.1898 -0.0040 -0.0308 0.0060 308 TYR A O 2350 C CB . TYR A 308 ? 0.1828 0.1700 0.1956 -0.0033 -0.0344 0.0063 308 TYR A CB 2351 C CG . TYR A 308 ? 0.1888 0.1766 0.2027 -0.0031 -0.0350 0.0099 308 TYR A CG 2352 C CD1 . TYR A 308 ? 0.1955 0.1834 0.2115 -0.0037 -0.0377 0.0106 308 TYR A CD1 2353 C CD2 . TYR A 308 ? 0.1982 0.1866 0.2109 -0.0025 -0.0330 0.0124 308 TYR A CD2 2354 C CE1 . TYR A 308 ? 0.2060 0.1951 0.2228 -0.0042 -0.0383 0.0140 308 TYR A CE1 2355 C CE2 . TYR A 308 ? 0.2093 0.1997 0.2233 -0.0024 -0.0335 0.0156 308 TYR A CE2 2356 C CZ . TYR A 308 ? 0.2120 0.2030 0.2282 -0.0036 -0.0361 0.0165 308 TYR A CZ 2357 O OH . TYR A 308 ? 0.2333 0.2270 0.2506 -0.0041 -0.0365 0.0199 308 TYR A OH 2358 N N . VAL A 309 ? 0.1776 0.1663 0.1909 -0.0044 -0.0339 0.0077 309 VAL A N 2359 C CA . VAL A 309 ? 0.1777 0.1668 0.1899 -0.0042 -0.0326 0.0098 309 VAL A CA 2360 C C . VAL A 309 ? 0.1888 0.1799 0.2030 -0.0040 -0.0335 0.0132 309 VAL A C 2361 O O . VAL A 309 ? 0.1817 0.1733 0.1979 -0.0047 -0.0357 0.0138 309 VAL A O 2362 C CB . VAL A 309 ? 0.1728 0.1619 0.1847 -0.0052 -0.0327 0.0081 309 VAL A CB 2363 C CG1 . VAL A 309 ? 0.1742 0.1621 0.1838 -0.0058 -0.0315 0.0047 309 VAL A CG1 2364 C CG2 . VAL A 309 ? 0.1713 0.1612 0.1858 -0.0060 -0.0353 0.0075 309 VAL A CG2 2365 N N . LYS A 310 ? 0.1983 0.1906 0.2115 -0.0031 -0.0321 0.0155 310 LYS A N 2366 C CA . LYS A 310 ? 0.2189 0.2145 0.2341 -0.0031 -0.0329 0.0190 310 LYS A CA 2367 C C . LYS A 310 ? 0.2221 0.2192 0.2394 -0.0048 -0.0350 0.0196 310 LYS A C 2368 O O . LYS A 310 ? 0.2193 0.2189 0.2385 -0.0057 -0.0365 0.0220 310 LYS A O 2369 C CB . LYS A 310 ? 0.2534 0.2506 0.2668 -0.0010 -0.0307 0.0213 310 LYS A CB 2370 C CG . LYS A 310 ? 0.2920 0.2878 0.3031 0.0007 -0.0288 0.0215 310 LYS A CG 2371 C CD . LYS A 310 ? 0.3326 0.3292 0.3410 0.0034 -0.0266 0.0234 310 LYS A CD 2372 C CE . LYS A 310 ? 0.3701 0.3642 0.3758 0.0037 -0.0259 0.0222 310 LYS A CE 2373 N NZ . LYS A 310 ? 0.4392 0.4313 0.4402 0.0066 -0.0238 0.0231 310 LYS A NZ 2374 N N . GLN A 311 ? 0.2109 0.2064 0.2274 -0.0053 -0.0351 0.0174 311 GLN A N 2375 C CA . GLN A 311 ? 0.2177 0.2139 0.2355 -0.0069 -0.0370 0.0177 311 GLN A CA 2376 C C . GLN A 311 ? 0.2307 0.2258 0.2499 -0.0084 -0.0398 0.0170 311 GLN A C 2377 O O . GLN A 311 ? 0.2292 0.2221 0.2481 -0.0081 -0.0402 0.0147 311 GLN A O 2378 C CB . GLN A 311 ? 0.2071 0.2014 0.2234 -0.0072 -0.0364 0.0151 311 GLN A CB 2379 C CG . GLN A 311 ? 0.2032 0.1975 0.2171 -0.0060 -0.0340 0.0158 311 GLN A CG 2380 C CD . GLN A 311 ? 0.2030 0.1946 0.2139 -0.0051 -0.0320 0.0137 311 GLN A CD 2381 O OE1 . GLN A 311 ? 0.1969 0.1879 0.2080 -0.0047 -0.0318 0.0130 311 GLN A OE1 2382 N NE2 . GLN A 311 ? 0.1987 0.1884 0.2065 -0.0050 -0.0306 0.0128 311 GLN A NE2 2383 N N . ASN A 312 ? 0.2438 0.2400 0.2641 -0.0101 -0.0419 0.0190 312 ASN A N 2384 C CA . ASN A 312 ? 0.2703 0.2638 0.2906 -0.0115 -0.0449 0.0182 312 ASN A CA 2385 C C . ASN A 312 ? 0.2590 0.2499 0.2785 -0.0122 -0.0463 0.0156 312 ASN A C 2386 O O . ASN A 312 ? 0.2672 0.2548 0.2859 -0.0128 -0.0488 0.0142 312 ASN A O 2387 C CB . ASN A 312 ? 0.3101 0.3053 0.3312 -0.0134 -0.0468 0.0218 312 ASN A CB 2388 C CG . ASN A 312 ? 0.3574 0.3565 0.3793 -0.0147 -0.0468 0.0246 312 ASN A CG 2389 O OD1 . ASN A 312 ? 0.4135 0.4124 0.4352 -0.0146 -0.0465 0.0237 312 ASN A OD1 2390 N ND2 . ASN A 312 ? 0.4345 0.4376 0.4575 -0.0158 -0.0471 0.0283 312 ASN A ND2 2391 N N . THR A 313 ? 0.2361 0.2280 0.2554 -0.0120 -0.0449 0.0149 313 THR A N 2392 C CA . THR A 313 ? 0.2342 0.2239 0.2525 -0.0125 -0.0458 0.0122 313 THR A CA 2393 C C . THR A 313 ? 0.2300 0.2206 0.2474 -0.0117 -0.0432 0.0108 313 THR A C 2394 O O . THR A 313 ? 0.2259 0.2186 0.2433 -0.0113 -0.0414 0.0130 313 THR A O 2395 C CB . THR A 313 ? 0.2454 0.2346 0.2634 -0.0146 -0.0483 0.0139 313 THR A CB 2396 O OG1 . THR A 313 ? 0.2541 0.2411 0.2708 -0.0148 -0.0489 0.0112 313 THR A OG1 2397 C CG2 . THR A 313 ? 0.2464 0.2394 0.2654 -0.0153 -0.0474 0.0175 313 THR A CG2 2398 N N . LEU A 314 ? 0.2189 0.2080 0.2353 -0.0115 -0.0429 0.0072 314 LEU A N 2399 C CA . LEU A 314 ? 0.2186 0.2080 0.2336 -0.0116 -0.0410 0.0057 314 LEU A CA 2400 C C . LEU A 314 ? 0.2218 0.2098 0.2360 -0.0122 -0.0423 0.0027 314 LEU A C 2401 O O . LEU A 314 ? 0.2176 0.2053 0.2319 -0.0115 -0.0427 -0.0002 314 LEU A O 2402 C CB . LEU A 314 ? 0.2194 0.2090 0.2333 -0.0107 -0.0386 0.0040 314 LEU A CB 2403 C CG . LEU A 314 ? 0.2245 0.2147 0.2378 -0.0097 -0.0367 0.0065 314 LEU A CG 2404 C CD1 . LEU A 314 ? 0.2284 0.2179 0.2402 -0.0091 -0.0349 0.0045 314 LEU A CD1 2405 C CD2 . LEU A 314 ? 0.2346 0.2249 0.2463 -0.0098 -0.0356 0.0084 314 LEU A CD2 2406 N N . LYS A 315 ? 0.2197 0.2075 0.2333 -0.0133 -0.0428 0.0033 315 LYS A N 2407 C CA A LYS A 315 ? 0.2309 0.2173 0.2436 -0.0139 -0.0442 0.0006 315 LYS A CA 2408 C CA B LYS A 315 ? 0.2301 0.2164 0.2428 -0.0139 -0.0442 0.0006 315 LYS A CA 2409 C C . LYS A 315 ? 0.2260 0.2131 0.2370 -0.0142 -0.0422 -0.0019 315 LYS A C 2410 O O . LYS A 315 ? 0.2238 0.2113 0.2338 -0.0150 -0.0407 -0.0006 315 LYS A O 2411 C CB A LYS A 315 ? 0.2421 0.2273 0.2545 -0.0153 -0.0463 0.0028 315 LYS A CB 2412 C CB B LYS A 315 ? 0.2401 0.2253 0.2526 -0.0153 -0.0464 0.0028 315 LYS A CB 2413 C CG A LYS A 315 ? 0.2575 0.2415 0.2708 -0.0157 -0.0488 0.0050 315 LYS A CG 2414 C CG B LYS A 315 ? 0.2541 0.2379 0.2673 -0.0157 -0.0490 0.0048 315 LYS A CG 2415 C CD A LYS A 315 ? 0.2671 0.2481 0.2794 -0.0148 -0.0508 0.0022 315 LYS A CD 2416 C CD B LYS A 315 ? 0.2608 0.2449 0.2741 -0.0177 -0.0506 0.0083 315 LYS A CD 2417 C CE A LYS A 315 ? 0.2820 0.2596 0.2922 -0.0158 -0.0535 0.0014 315 LYS A CE 2418 C CE B LYS A 315 ? 0.2752 0.2580 0.2887 -0.0187 -0.0532 0.0107 315 LYS A CE 2419 N NZ A LYS A 315 ? 0.2966 0.2714 0.3052 -0.0140 -0.0549 -0.0022 315 LYS A NZ 2420 N NZ B LYS A 315 ? 0.2732 0.2595 0.2887 -0.0185 -0.0521 0.0139 315 LYS A NZ 2421 N N . LEU A 316 ? 0.2235 0.2110 0.2341 -0.0136 -0.0422 -0.0056 316 LEU A N 2422 C CA . LEU A 316 ? 0.2198 0.2087 0.2288 -0.0143 -0.0404 -0.0084 316 LEU A CA 2423 C C . LEU A 316 ? 0.2255 0.2135 0.2335 -0.0150 -0.0418 -0.0098 316 LEU A C 2424 O O . LEU A 316 ? 0.2253 0.2122 0.2335 -0.0139 -0.0438 -0.0114 316 LEU A O 2425 C CB . LEU A 316 ? 0.2233 0.2146 0.2328 -0.0133 -0.0397 -0.0117 316 LEU A CB 2426 C CG . LEU A 316 ? 0.2253 0.2193 0.2332 -0.0143 -0.0378 -0.0148 316 LEU A CG 2427 C CD1 . LEU A 316 ? 0.2230 0.2168 0.2289 -0.0159 -0.0353 -0.0136 316 LEU A CD1 2428 C CD2 . LEU A 316 ? 0.2356 0.2330 0.2446 -0.0129 -0.0379 -0.0183 316 LEU A CD2 2429 N N . ALA A 317 ? 0.2250 0.2128 0.2313 -0.0165 -0.0407 -0.0093 317 ALA A N 2430 C CA . ALA A 317 ? 0.2321 0.2189 0.2370 -0.0173 -0.0418 -0.0109 317 ALA A CA 2431 C C . ALA A 317 ? 0.2364 0.2253 0.2408 -0.0165 -0.0415 -0.0152 317 ALA A C 2432 O O . ALA A 317 ? 0.2420 0.2338 0.2461 -0.0167 -0.0395 -0.0171 317 ALA A O 2433 C CB . ALA A 317 ? 0.2290 0.2154 0.2318 -0.0192 -0.0404 -0.0098 317 ALA A CB 2434 N N . THR A 318 ? 0.2432 0.2307 0.2471 -0.0156 -0.0437 -0.0168 318 THR A N 2435 C CA . THR A 318 ? 0.2506 0.2404 0.2538 -0.0144 -0.0436 -0.0211 318 THR A CA 2436 C C . THR A 318 ? 0.2609 0.2492 0.2617 -0.0151 -0.0443 -0.0224 318 THR A C 2437 O O . THR A 318 ? 0.2814 0.2707 0.2813 -0.0135 -0.0450 -0.0257 318 THR A O 2438 C CB . THR A 318 ? 0.2533 0.2426 0.2574 -0.0114 -0.0455 -0.0227 318 THR A CB 2439 O OG1 . THR A 318 ? 0.2638 0.2479 0.2671 -0.0110 -0.0485 -0.0207 318 THR A OG1 2440 C CG2 . THR A 318 ? 0.2493 0.2409 0.2556 -0.0107 -0.0445 -0.0220 318 THR A CG2 2441 N N . GLY A 319 ? 0.2617 0.2480 0.2615 -0.0173 -0.0441 -0.0199 319 GLY A N 2442 C CA . GLY A 319 ? 0.2732 0.2581 0.2705 -0.0185 -0.0446 -0.0208 319 GLY A CA 2443 C C . GLY A 319 ? 0.2703 0.2544 0.2667 -0.0211 -0.0434 -0.0181 319 GLY A C 2444 O O . GLY A 319 ? 0.2713 0.2558 0.2688 -0.0216 -0.0423 -0.0155 319 GLY A O 2445 N N . MET A 320 ? 0.2640 0.2469 0.2580 -0.0225 -0.0436 -0.0187 320 MET A N 2446 C CA . MET A 320 ? 0.2651 0.2470 0.2575 -0.0248 -0.0426 -0.0165 320 MET A CA 2447 C C . MET A 320 ? 0.2682 0.2473 0.2614 -0.0253 -0.0445 -0.0123 320 MET A C 2448 O O . MET A 320 ? 0.2838 0.2614 0.2784 -0.0244 -0.0467 -0.0111 320 MET A O 2449 C CB . MET A 320 ? 0.2652 0.2469 0.2546 -0.0262 -0.0423 -0.0188 320 MET A CB 2450 C CG . MET A 320 ? 0.2688 0.2474 0.2571 -0.0259 -0.0450 -0.0191 320 MET A CG 2451 S SD . MET A 320 ? 0.2783 0.2568 0.2628 -0.0275 -0.0444 -0.0219 320 MET A SD 2452 C CE . MET A 320 ? 0.2690 0.2521 0.2538 -0.0254 -0.0431 -0.0270 320 MET A CE 2453 N N . ARG A 321 ? 0.2780 0.2565 0.2700 -0.0268 -0.0437 -0.0100 321 ARG A N 2454 C CA . ARG A 321 ? 0.2947 0.2717 0.2872 -0.0275 -0.0455 -0.0061 321 ARG A CA 2455 C C . ARG A 321 ? 0.3002 0.2747 0.2918 -0.0281 -0.0482 -0.0065 321 ARG A C 2456 O O . ARG A 321 ? 0.2846 0.2581 0.2740 -0.0285 -0.0483 -0.0094 321 ARG A O 2457 C CB . ARG A 321 ? 0.3192 0.2957 0.3097 -0.0288 -0.0444 -0.0042 321 ARG A CB 2458 C CG . ARG A 321 ? 0.3544 0.3296 0.3415 -0.0305 -0.0440 -0.0064 321 ARG A CG 2459 C CD . ARG A 321 ? 0.3894 0.3634 0.3740 -0.0317 -0.0433 -0.0044 321 ARG A CD 2460 N NE . ARG A 321 ? 0.3943 0.3685 0.3772 -0.0315 -0.0408 -0.0046 321 ARG A NE 2461 C CZ . ARG A 321 ? 0.4083 0.3825 0.3916 -0.0304 -0.0402 -0.0018 321 ARG A CZ 2462 N NH1 . ARG A 321 ? 0.4302 0.4053 0.4161 -0.0292 -0.0417 0.0015 321 ARG A NH1 2463 N NH2 . ARG A 321 ? 0.4271 0.4002 0.4075 -0.0304 -0.0380 -0.0024 321 ARG A NH2 2464 N N . ASN A 322 ? 0.2971 0.2707 0.2903 -0.0282 -0.0505 -0.0036 322 ASN A N 2465 C CA . ASN A 322 ? 0.3177 0.2881 0.3093 -0.0292 -0.0535 -0.0034 322 ASN A CA 2466 C C . ASN A 322 ? 0.3259 0.2959 0.3167 -0.0313 -0.0545 -0.0003 322 ASN A C 2467 O O . ASN A 322 ? 0.3084 0.2807 0.3012 -0.0317 -0.0546 0.0033 322 ASN A O 2468 C CB . ASN A 322 ? 0.3216 0.2909 0.3147 -0.0286 -0.0556 -0.0020 322 ASN A CB 2469 C CG . ASN A 322 ? 0.3287 0.2932 0.3188 -0.0292 -0.0588 -0.0030 322 ASN A CG 2470 O OD1 . ASN A 322 ? 0.3238 0.2861 0.3112 -0.0284 -0.0588 -0.0066 322 ASN A OD1 2471 N ND2 . ASN A 322 ? 0.3339 0.2966 0.3240 -0.0306 -0.0614 0.0000 322 ASN A ND2 2472 N N . VAL A 323 ? 0.3498 0.3174 0.3375 -0.0326 -0.0553 -0.0017 323 VAL A N 2473 C CA . VAL A 323 ? 0.3710 0.3384 0.3575 -0.0347 -0.0560 0.0008 323 VAL A CA 2474 C C . VAL A 323 ? 0.4049 0.3683 0.3887 -0.0364 -0.0592 0.0008 323 VAL A C 2475 O O . VAL A 323 ? 0.4038 0.3642 0.3848 -0.0361 -0.0596 -0.0025 323 VAL A O 2476 C CB . VAL A 323 ? 0.3757 0.3435 0.3601 -0.0351 -0.0537 -0.0008 323 VAL A CB 2477 C CG1 . VAL A 323 ? 0.3854 0.3531 0.3686 -0.0369 -0.0546 0.0021 323 VAL A CG1 2478 C CG2 . VAL A 323 ? 0.3776 0.3481 0.3634 -0.0336 -0.0507 -0.0014 323 VAL A CG2 2479 N N . PRO A 324 ? 0.4620 0.4256 0.4464 -0.0382 -0.0616 0.0046 324 PRO A N 2480 C CA . PRO A 324 ? 0.4839 0.4430 0.4650 -0.0404 -0.0649 0.0050 324 PRO A CA 2481 C C . PRO A 324 ? 0.4963 0.4527 0.4737 -0.0415 -0.0648 0.0029 324 PRO A C 2482 O O . PRO A 324 ? 0.4893 0.4480 0.4669 -0.0414 -0.0627 0.0028 324 PRO A O 2483 C CB . PRO A 324 ? 0.4956 0.4574 0.4785 -0.0427 -0.0667 0.0100 324 PRO A CB 2484 C CG . PRO A 324 ? 0.4977 0.4649 0.4836 -0.0416 -0.0641 0.0117 324 PRO A CG 2485 C CD . PRO A 324 ? 0.4804 0.4485 0.4679 -0.0387 -0.0612 0.0089 324 PRO A CD 2486 N N . GLU A 325 ? 0.5323 0.4834 0.5057 -0.0424 -0.0672 0.0013 325 GLU A N 2487 C CA . GLU A 325 ? 0.5601 0.5083 0.5295 -0.0437 -0.0675 -0.0003 325 GLU A CA 2488 C C . GLU A 325 ? 0.6132 0.5615 0.5819 -0.0469 -0.0696 0.0036 325 GLU A C 2489 O O . GLU A 325 ? 0.6334 0.5809 0.6022 -0.0488 -0.0723 0.0066 325 GLU A O 2490 C CB . GLU A 325 ? 0.5575 0.4996 0.5223 -0.0430 -0.0693 -0.0037 325 GLU A CB 2491 C CG . GLU A 325 ? 0.5447 0.4843 0.5053 -0.0436 -0.0689 -0.0064 325 GLU A CG 2492 C CD . GLU A 325 ? 0.5418 0.4774 0.4987 -0.0412 -0.0690 -0.0111 325 GLU A CD 2493 O OE1 . GLU A 325 ? 0.5420 0.4755 0.4987 -0.0393 -0.0703 -0.0120 325 GLU A OE1 2494 O OE2 . GLU A 325 ? 0.5359 0.4707 0.4898 -0.0411 -0.0680 -0.0140 325 GLU A OE2 2495 N N . LYS A 326 ? 0.6702 0.6198 0.6380 -0.0478 -0.0683 0.0037 326 LYS A N 2496 C CA . LYS A 326 ? 0.7379 0.6877 0.7047 -0.0507 -0.0703 0.0071 326 LYS A CA 2497 C C . LYS A 326 ? 0.7784 0.7219 0.7401 -0.0530 -0.0735 0.0063 326 LYS A C 2498 O O . LYS A 326 ? 0.7688 0.7079 0.7269 -0.0520 -0.0731 0.0023 326 LYS A O 2499 C CB . LYS A 326 ? 0.7493 0.7012 0.7157 -0.0508 -0.0682 0.0071 326 LYS A CB 2500 C CG . LYS A 326 ? 0.7587 0.7158 0.7290 -0.0487 -0.0654 0.0083 326 LYS A CG 2501 C CD . LYS A 326 ? 0.7873 0.7459 0.7567 -0.0493 -0.0646 0.0099 326 LYS A CD 2502 C CE . LYS A 326 ? 0.7897 0.7522 0.7617 -0.0470 -0.0619 0.0110 326 LYS A CE 2503 N NZ . LYS A 326 ? 0.8056 0.7694 0.7765 -0.0473 -0.0617 0.0133 326 LYS A NZ 2504 N N . GLN A 327 ? 0.8487 0.7919 0.8098 -0.0560 -0.0766 0.0101 327 GLN A N 2505 C CA . GLN A 327 ? 0.8920 0.8284 0.8475 -0.0587 -0.0801 0.0098 327 GLN A CA 2506 C C . GLN A 327 ? 0.8939 0.8271 0.8452 -0.0599 -0.0801 0.0082 327 GLN A C 2507 O O . GLN A 327 ? 0.8718 0.8088 0.8245 -0.0607 -0.0791 0.0099 327 GLN A O 2508 C CB . GLN A 327 ? 0.9346 0.8722 0.8906 -0.0623 -0.0835 0.0147 327 GLN A CB 2509 C CG . GLN A 327 ? 0.9529 0.8931 0.9123 -0.0618 -0.0839 0.0165 327 GLN A CG 2510 C CD . GLN A 327 ? 0.9743 0.9146 0.9327 -0.0661 -0.0877 0.0209 327 GLN A CD 2511 O OE1 . GLN A 327 ? 0.9744 0.9147 0.9307 -0.0695 -0.0898 0.0232 327 GLN A OE1 2512 N NE2 . GLN A 327 ? 0.9802 0.9206 0.9398 -0.0662 -0.0887 0.0221 327 GLN A NE2 2513 N N . ALA A 334 ? 0.6778 0.5942 0.6041 -0.0596 -0.0741 -0.0109 334 ALA A N 2514 C CA . ALA A 334 ? 0.6296 0.5502 0.5571 -0.0580 -0.0701 -0.0140 334 ALA A CA 2515 C C . ALA A 334 ? 0.6062 0.5314 0.5387 -0.0549 -0.0680 -0.0149 334 ALA A C 2516 O O . ALA A 334 ? 0.6376 0.5654 0.5746 -0.0549 -0.0684 -0.0117 334 ALA A O 2517 C CB . ALA A 334 ? 0.6433 0.5668 0.5717 -0.0602 -0.0689 -0.0116 334 ALA A CB 2518 N N . ILE A 335 ? 0.5350 0.4614 0.4668 -0.0524 -0.0658 -0.0194 335 ILE A N 2519 C CA . ILE A 335 ? 0.4715 0.4027 0.4078 -0.0496 -0.0635 -0.0207 335 ILE A CA 2520 C C . ILE A 335 ? 0.4434 0.3799 0.3838 -0.0505 -0.0611 -0.0184 335 ILE A C 2521 O O . ILE A 335 ? 0.4443 0.3808 0.3832 -0.0528 -0.0606 -0.0170 335 ILE A O 2522 C CB . ILE A 335 ? 0.4535 0.3865 0.3882 -0.0469 -0.0613 -0.0261 335 ILE A CB 2523 C CG1 . ILE A 335 ? 0.4523 0.3870 0.3840 -0.0484 -0.0590 -0.0283 335 ILE A CG1 2524 C CG2 . ILE A 335 ? 0.4677 0.3953 0.3986 -0.0447 -0.0638 -0.0284 335 ILE A CG2 2525 C CD1 . ILE A 335 ? 0.4475 0.3866 0.3788 -0.0460 -0.0562 -0.0332 335 ILE A CD1 2526 N N . ALA A 336 ? 0.4194 0.3597 0.3643 -0.0486 -0.0598 -0.0181 336 ALA A N 2527 C CA . ALA A 336 ? 0.4004 0.3447 0.3486 -0.0491 -0.0577 -0.0160 336 ALA A CA 2528 C C . ALA A 336 ? 0.3849 0.3335 0.3364 -0.0466 -0.0552 -0.0179 336 ALA A C 2529 O O . ALA A 336 ? 0.3826 0.3312 0.3352 -0.0444 -0.0558 -0.0198 336 ALA A O 2530 C CB . ALA A 336 ? 0.4036 0.3477 0.3542 -0.0501 -0.0597 -0.0109 336 ALA A CB 2531 N N . GLY A 337 ? 0.3731 0.3248 0.3256 -0.0472 -0.0526 -0.0176 337 GLY A N 2532 C CA . GLY A 337 ? 0.3704 0.3263 0.3252 -0.0456 -0.0500 -0.0196 337 GLY A CA 2533 C C . GLY A 337 ? 0.3636 0.3212 0.3227 -0.0444 -0.0500 -0.0165 337 GLY A C 2534 O O . GLY A 337 ? 0.3549 0.3110 0.3156 -0.0445 -0.0521 -0.0130 337 GLY A O 2535 N N . PHE A 338 ? 0.3577 0.3188 0.3184 -0.0436 -0.0474 -0.0178 338 PHE A N 2536 C CA . PHE A 338 ? 0.3654 0.3282 0.3301 -0.0420 -0.0472 -0.0156 338 PHE A CA 2537 C C . PHE A 338 ? 0.3778 0.3399 0.3433 -0.0426 -0.0475 -0.0112 338 PHE A C 2538 O O . PHE A 338 ? 0.3775 0.3410 0.3463 -0.0411 -0.0476 -0.0092 338 PHE A O 2539 C CB . PHE A 338 ? 0.3532 0.3198 0.3190 -0.0411 -0.0444 -0.0182 338 PHE A CB 2540 C CG . PHE A 338 ? 0.3562 0.3234 0.3191 -0.0432 -0.0420 -0.0186 338 PHE A CG 2541 C CD1 . PHE A 338 ? 0.3598 0.3277 0.3190 -0.0450 -0.0407 -0.0216 338 PHE A CD1 2542 C CD2 . PHE A 338 ? 0.3702 0.3371 0.3333 -0.0433 -0.0410 -0.0160 338 PHE A CD2 2543 C CE1 . PHE A 338 ? 0.3702 0.3382 0.3259 -0.0474 -0.0387 -0.0219 338 PHE A CE1 2544 C CE2 . PHE A 338 ? 0.3720 0.3381 0.3311 -0.0454 -0.0390 -0.0164 338 PHE A CE2 2545 C CZ . PHE A 338 ? 0.3787 0.3453 0.3341 -0.0477 -0.0379 -0.0193 338 PHE A CZ 2546 N N . ILE A 339 ? 0.4024 0.3625 0.3647 -0.0445 -0.0476 -0.0099 339 ILE A N 2547 C CA . ILE A 339 ? 0.4392 0.3988 0.4017 -0.0445 -0.0478 -0.0060 339 ILE A CA 2548 C C . ILE A 339 ? 0.4593 0.4195 0.4254 -0.0435 -0.0504 -0.0025 339 ILE A C 2549 O O . ILE A 339 ? 0.4507 0.4094 0.4161 -0.0447 -0.0527 -0.0018 339 ILE A O 2550 C CB . ILE A 339 ? 0.4419 0.3989 0.3998 -0.0465 -0.0476 -0.0053 339 ILE A CB 2551 C CG1 . ILE A 339 ? 0.4388 0.3954 0.3929 -0.0479 -0.0449 -0.0085 339 ILE A CG1 2552 C CG2 . ILE A 339 ? 0.4676 0.4242 0.4256 -0.0457 -0.0481 -0.0012 339 ILE A CG2 2553 C CD1 . ILE A 339 ? 0.4320 0.3895 0.3862 -0.0470 -0.0428 -0.0083 339 ILE A CD1 2554 N N . GLU A 340 ? 0.5090 0.4716 0.4786 -0.0417 -0.0500 -0.0006 340 GLU A N 2555 C CA . GLU A 340 ? 0.5400 0.5042 0.5132 -0.0409 -0.0522 0.0025 340 GLU A CA 2556 C C . GLU A 340 ? 0.5092 0.4722 0.4831 -0.0416 -0.0545 0.0015 340 GLU A C 2557 O O . GLU A 340 ? 0.4944 0.4572 0.4690 -0.0426 -0.0571 0.0042 340 GLU A O 2558 C CB . GLU A 340 ? 0.5989 0.5636 0.5717 -0.0416 -0.0536 0.0065 340 GLU A CB 2559 C CG . GLU A 340 ? 0.6686 0.6340 0.6404 -0.0402 -0.0518 0.0080 340 GLU A CG 2560 C CD . GLU A 340 ? 0.7320 0.7000 0.7070 -0.0377 -0.0505 0.0090 340 GLU A CD 2561 O OE1 . GLU A 340 ? 0.8141 0.7850 0.7930 -0.0370 -0.0519 0.0109 340 GLU A OE1 2562 O OE2 . GLU A 340 ? 0.8000 0.7670 0.7731 -0.0367 -0.0482 0.0079 340 GLU A OE2 2563 N N . ASN A 341 ? 0.4946 0.4567 0.4680 -0.0409 -0.0538 -0.0022 341 ASN A N 2564 C CA . ASN A 341 ? 0.4563 0.4157 0.4285 -0.0413 -0.0561 -0.0037 341 ASN A CA 2565 C C . ASN A 341 ? 0.4421 0.4015 0.4146 -0.0394 -0.0552 -0.0076 341 ASN A C 2566 O O . ASN A 341 ? 0.4658 0.4263 0.4369 -0.0391 -0.0530 -0.0109 341 ASN A O 2567 C CB . ASN A 341 ? 0.4697 0.4262 0.4377 -0.0434 -0.0569 -0.0047 341 ASN A CB 2568 C CG . ASN A 341 ? 0.4624 0.4149 0.4280 -0.0438 -0.0595 -0.0062 341 ASN A CG 2569 O OD1 . ASN A 341 ? 0.4460 0.3971 0.4125 -0.0443 -0.0621 -0.0039 341 ASN A OD1 2570 N ND2 . ASN A 341 ? 0.4342 0.3848 0.3963 -0.0438 -0.0587 -0.0101 341 ASN A ND2 2571 N N . GLY A 342 ? 0.4047 0.3634 0.3789 -0.0382 -0.0568 -0.0072 342 GLY A N 2572 C CA . GLY A 342 ? 0.3952 0.3535 0.3692 -0.0361 -0.0566 -0.0110 342 GLY A CA 2573 C C . GLY A 342 ? 0.3922 0.3456 0.3626 -0.0361 -0.0592 -0.0127 342 GLY A C 2574 O O . GLY A 342 ? 0.4011 0.3511 0.3695 -0.0381 -0.0617 -0.0104 342 GLY A O 2575 N N . TRP A 343 ? 0.3766 0.3295 0.3457 -0.0337 -0.0588 -0.0168 343 TRP A N 2576 C CA . TRP A 343 ? 0.3802 0.3280 0.3450 -0.0329 -0.0612 -0.0191 343 TRP A CA 2577 C C . TRP A 343 ? 0.4041 0.3492 0.3689 -0.0305 -0.0632 -0.0197 343 TRP A C 2578 O O . TRP A 343 ? 0.3826 0.3299 0.3483 -0.0275 -0.0619 -0.0229 343 TRP A O 2579 C CB . TRP A 343 ? 0.3571 0.3065 0.3195 -0.0315 -0.0592 -0.0238 343 TRP A CB 2580 C CG . TRP A 343 ? 0.3427 0.2935 0.3035 -0.0340 -0.0576 -0.0238 343 TRP A CG 2581 C CD1 . TRP A 343 ? 0.3388 0.2880 0.2989 -0.0372 -0.0584 -0.0203 343 TRP A CD1 2582 C CD2 . TRP A 343 ? 0.3371 0.2912 0.2962 -0.0337 -0.0550 -0.0277 343 TRP A CD2 2583 N NE1 . TRP A 343 ? 0.3303 0.2808 0.2883 -0.0387 -0.0565 -0.0218 343 TRP A NE1 2584 C CE2 . TRP A 343 ? 0.3329 0.2864 0.2901 -0.0369 -0.0544 -0.0261 343 TRP A CE2 2585 C CE3 . TRP A 343 ? 0.3359 0.2938 0.2950 -0.0311 -0.0532 -0.0320 343 TRP A CE3 2586 C CZ2 . TRP A 343 ? 0.3329 0.2889 0.2879 -0.0379 -0.0521 -0.0288 343 TRP A CZ2 2587 C CZ3 . TRP A 343 ? 0.3383 0.2997 0.2955 -0.0321 -0.0507 -0.0348 343 TRP A CZ3 2588 C CH2 . TRP A 343 ? 0.3364 0.2966 0.2914 -0.0356 -0.0502 -0.0332 343 TRP A CH2 2589 N N . GLU A 344 ? 0.4594 0.3998 0.4229 -0.0320 -0.0664 -0.0167 344 GLU A N 2590 C CA . GLU A 344 ? 0.4936 0.4302 0.4561 -0.0301 -0.0687 -0.0170 344 GLU A CA 2591 C C . GLU A 344 ? 0.5116 0.4433 0.4689 -0.0270 -0.0700 -0.0215 344 GLU A C 2592 O O . GLU A 344 ? 0.5135 0.4442 0.4706 -0.0238 -0.0705 -0.0235 344 GLU A O 2593 C CB . GLU A 344 ? 0.5460 0.4788 0.5078 -0.0330 -0.0719 -0.0125 344 GLU A CB 2594 C CG . GLU A 344 ? 0.5777 0.5164 0.5452 -0.0345 -0.0705 -0.0086 344 GLU A CG 2595 C CD . GLU A 344 ? 0.6411 0.5782 0.6085 -0.0379 -0.0733 -0.0038 344 GLU A CD 2596 O OE1 . GLU A 344 ? 0.6793 0.6113 0.6441 -0.0381 -0.0762 -0.0031 344 GLU A OE1 2597 O OE2 . GLU A 344 ? 0.6534 0.5942 0.6230 -0.0403 -0.0727 -0.0006 344 GLU A OE2 2598 N N . GLY A 345 ? 0.5127 0.4416 0.4658 -0.0277 -0.0704 -0.0232 345 GLY A N 2599 C CA . GLY A 345 ? 0.5184 0.4433 0.4664 -0.0244 -0.0713 -0.0277 345 GLY A CA 2600 C C . GLY A 345 ? 0.5206 0.4519 0.4705 -0.0206 -0.0681 -0.0323 345 GLY A C 2601 O O . GLY A 345 ? 0.5144 0.4434 0.4604 -0.0172 -0.0687 -0.0362 345 GLY A O 2602 N N . MET A 346 ? 0.5116 0.4510 0.4673 -0.0212 -0.0647 -0.0317 346 MET A N 2603 C CA . MET A 346 ? 0.5169 0.4635 0.4748 -0.0184 -0.0615 -0.0357 346 MET A CA 2604 C C . MET A 346 ? 0.5242 0.4723 0.4846 -0.0151 -0.0618 -0.0366 346 MET A C 2605 O O . MET A 346 ? 0.5018 0.4536 0.4669 -0.0160 -0.0605 -0.0342 346 MET A O 2606 C CB . MET A 346 ? 0.5289 0.4825 0.4906 -0.0213 -0.0580 -0.0346 346 MET A CB 2607 C CG . MET A 346 ? 0.5460 0.5079 0.5107 -0.0198 -0.0545 -0.0376 346 MET A CG 2608 S SD . MET A 346 ? 0.6071 0.5738 0.5692 -0.0199 -0.0519 -0.0419 346 MET A SD 2609 C CE . MET A 346 ? 0.6038 0.5714 0.5642 -0.0141 -0.0529 -0.0468 346 MET A CE 2610 N N . VAL A 347 ? 0.5242 0.4693 0.4811 -0.0109 -0.0634 -0.0399 347 VAL A N 2611 C CA . VAL A 347 ? 0.5316 0.4762 0.4898 -0.0076 -0.0645 -0.0406 347 VAL A CA 2612 C C . VAL A 347 ? 0.5294 0.4809 0.4889 -0.0030 -0.0625 -0.0453 347 VAL A C 2613 O O . VAL A 347 ? 0.5618 0.5140 0.5229 -0.0001 -0.0631 -0.0459 347 VAL A O 2614 C CB . VAL A 347 ? 0.5531 0.4869 0.5054 -0.0062 -0.0690 -0.0400 347 VAL A CB 2615 C CG1 . VAL A 347 ? 0.5425 0.4710 0.4943 -0.0111 -0.0711 -0.0348 347 VAL A CG1 2616 C CG2 . VAL A 347 ? 0.5679 0.4971 0.5136 -0.0035 -0.0704 -0.0437 347 VAL A CG2 2617 N N . ASP A 348 ? 0.5190 0.4758 0.4779 -0.0024 -0.0602 -0.0486 348 ASP A N 2618 C CA . ASP A 348 ? 0.5157 0.4807 0.4762 0.0016 -0.0581 -0.0530 348 ASP A CA 2619 C C . ASP A 348 ? 0.4785 0.4540 0.4441 -0.0010 -0.0540 -0.0531 348 ASP A C 2620 O O . ASP A 348 ? 0.4836 0.4675 0.4506 0.0010 -0.0517 -0.0567 348 ASP A O 2621 C CB . ASP A 348 ? 0.5622 0.5261 0.5174 0.0051 -0.0588 -0.0574 348 ASP A CB 2622 C CG . ASP A 348 ? 0.5998 0.5649 0.5532 0.0018 -0.0572 -0.0576 348 ASP A CG 2623 O OD1 . ASP A 348 ? 0.6180 0.5805 0.5723 -0.0031 -0.0570 -0.0538 348 ASP A OD1 2624 O OD2 . ASP A 348 ? 0.6414 0.6102 0.5922 0.0044 -0.0562 -0.0618 348 ASP A OD2 2625 N N . GLY A 349 ? 0.4441 0.4192 0.4122 -0.0057 -0.0530 -0.0491 349 GLY A N 2626 C CA . GLY A 349 ? 0.4091 0.3923 0.3810 -0.0086 -0.0494 -0.0487 349 GLY A CA 2627 C C . GLY A 349 ? 0.3718 0.3522 0.3460 -0.0126 -0.0494 -0.0438 349 GLY A C 2628 O O . GLY A 349 ? 0.3751 0.3482 0.3479 -0.0135 -0.0519 -0.0408 349 GLY A O 2629 N N . TRP A 350 ? 0.3393 0.3254 0.3166 -0.0148 -0.0465 -0.0429 350 TRP A N 2630 C CA . TRP A 350 ? 0.3203 0.3044 0.2994 -0.0182 -0.0461 -0.0385 350 TRP A CA 2631 C C . TRP A 350 ? 0.3008 0.2843 0.2779 -0.0219 -0.0450 -0.0373 350 TRP A C 2632 O O . TRP A 350 ? 0.2934 0.2733 0.2707 -0.0242 -0.0456 -0.0335 350 TRP A O 2633 C CB . TRP A 350 ? 0.3226 0.3120 0.3052 -0.0185 -0.0439 -0.0381 350 TRP A CB 2634 C CG . TRP A 350 ? 0.3289 0.3175 0.3141 -0.0157 -0.0453 -0.0375 350 TRP A CG 2635 C CD1 . TRP A 350 ? 0.3468 0.3316 0.3310 -0.0123 -0.0481 -0.0386 350 TRP A CD1 2636 C CD2 . TRP A 350 ? 0.3240 0.3151 0.3126 -0.0160 -0.0442 -0.0357 350 TRP A CD2 2637 N NE1 . TRP A 350 ? 0.3489 0.3338 0.3357 -0.0107 -0.0488 -0.0375 350 TRP A NE1 2638 C CE2 . TRP A 350 ? 0.3332 0.3221 0.3229 -0.0127 -0.0464 -0.0358 350 TRP A CE2 2639 C CE3 . TRP A 350 ? 0.3281 0.3221 0.3181 -0.0185 -0.0417 -0.0341 350 TRP A CE3 2640 C CZ2 . TRP A 350 ? 0.3302 0.3205 0.3229 -0.0122 -0.0460 -0.0343 350 TRP A CZ2 2641 C CZ3 . TRP A 350 ? 0.3232 0.3183 0.3159 -0.0178 -0.0414 -0.0327 350 TRP A CZ3 2642 C CH2 . TRP A 350 ? 0.3228 0.3164 0.3171 -0.0147 -0.0434 -0.0328 350 TRP A CH2 2643 N N . TYR A 351 ? 0.2978 0.2854 0.2730 -0.0225 -0.0431 -0.0405 351 TYR A N 2644 C CA . TYR A 351 ? 0.2937 0.2807 0.2662 -0.0260 -0.0420 -0.0399 351 TYR A CA 2645 C C . TYR A 351 ? 0.3034 0.2904 0.2723 -0.0250 -0.0424 -0.0433 351 TYR A C 2646 O O . TYR A 351 ? 0.3089 0.2990 0.2779 -0.0216 -0.0426 -0.0468 351 TYR A O 2647 C CB . TYR A 351 ? 0.2935 0.2865 0.2665 -0.0286 -0.0387 -0.0406 351 TYR A CB 2648 C CG . TYR A 351 ? 0.2901 0.2837 0.2661 -0.0292 -0.0379 -0.0379 351 TYR A CG 2649 C CD1 . TYR A 351 ? 0.2904 0.2800 0.2661 -0.0315 -0.0380 -0.0340 351 TYR A CD1 2650 C CD2 . TYR A 351 ? 0.2902 0.2885 0.2691 -0.0270 -0.0372 -0.0395 351 TYR A CD2 2651 C CE1 . TYR A 351 ? 0.2902 0.2802 0.2682 -0.0317 -0.0372 -0.0317 351 TYR A CE1 2652 C CE2 . TYR A 351 ? 0.2886 0.2871 0.2699 -0.0275 -0.0365 -0.0371 351 TYR A CE2 2653 C CZ . TYR A 351 ? 0.2871 0.2813 0.2679 -0.0298 -0.0365 -0.0332 351 TYR A CZ 2654 O OH . TYR A 351 ? 0.2946 0.2887 0.2771 -0.0300 -0.0357 -0.0309 351 TYR A OH 2655 N N . GLY A 352 ? 0.3073 0.2911 0.2731 -0.0277 -0.0426 -0.0424 352 GLY A N 2656 C CA . GLY A 352 ? 0.3170 0.3010 0.2790 -0.0269 -0.0428 -0.0458 352 GLY A CA 2657 C C . GLY A 352 ? 0.3211 0.3014 0.2795 -0.0304 -0.0429 -0.0444 352 GLY A C 2658 O O . GLY A 352 ? 0.3077 0.2867 0.2665 -0.0337 -0.0422 -0.0413 352 GLY A O 2659 N N . PHE A 353 ? 0.3301 0.3086 0.2847 -0.0293 -0.0438 -0.0470 353 PHE A N 2660 C CA . PHE A 353 ? 0.3388 0.3143 0.2893 -0.0324 -0.0438 -0.0466 353 PHE A CA 2661 C C . PHE A 353 ? 0.3442 0.3115 0.2915 -0.0312 -0.0473 -0.0458 353 PHE A C 2662 O O . PHE A 353 ? 0.3492 0.3146 0.2956 -0.0274 -0.0490 -0.0478 353 PHE A O 2663 C CB . PHE A 353 ? 0.3469 0.3284 0.2950 -0.0322 -0.0415 -0.0511 353 PHE A CB 2664 C CG . PHE A 353 ? 0.3523 0.3426 0.3026 -0.0338 -0.0381 -0.0524 353 PHE A CG 2665 C CD1 . PHE A 353 ? 0.3586 0.3557 0.3118 -0.0308 -0.0369 -0.0551 353 PHE A CD1 2666 C CD2 . PHE A 353 ? 0.3588 0.3503 0.3074 -0.0385 -0.0361 -0.0512 353 PHE A CD2 2667 C CE1 . PHE A 353 ? 0.3579 0.3634 0.3128 -0.0328 -0.0339 -0.0563 353 PHE A CE1 2668 C CE2 . PHE A 353 ? 0.3642 0.3631 0.3138 -0.0406 -0.0331 -0.0524 353 PHE A CE2 2669 C CZ . PHE A 353 ? 0.3576 0.3638 0.3105 -0.0379 -0.0320 -0.0549 353 PHE A CZ 2670 N N . ARG A 354 ? 0.3422 0.3044 0.2874 -0.0345 -0.0485 -0.0428 354 ARG A N 2671 C CA . ARG A 354 ? 0.3560 0.3107 0.2967 -0.0344 -0.0514 -0.0425 354 ARG A CA 2672 C C . ARG A 354 ? 0.3536 0.3079 0.2903 -0.0374 -0.0505 -0.0432 354 ARG A C 2673 O O . ARG A 354 ? 0.3458 0.3025 0.2833 -0.0407 -0.0486 -0.0415 354 ARG A O 2674 C CB . ARG A 354 ? 0.3621 0.3109 0.3039 -0.0358 -0.0544 -0.0377 354 ARG A CB 2675 C CG . ARG A 354 ? 0.3782 0.3247 0.3218 -0.0328 -0.0565 -0.0373 354 ARG A CG 2676 C CD . ARG A 354 ? 0.3831 0.3243 0.3274 -0.0349 -0.0594 -0.0325 354 ARG A CD 2677 N NE . ARG A 354 ? 0.3936 0.3330 0.3396 -0.0323 -0.0612 -0.0320 354 ARG A NE 2678 C CZ . ARG A 354 ? 0.3958 0.3319 0.3431 -0.0337 -0.0636 -0.0279 354 ARG A CZ 2679 N NH1 . ARG A 354 ? 0.4001 0.3351 0.3479 -0.0372 -0.0645 -0.0240 354 ARG A NH1 2680 N NH2 . ARG A 354 ? 0.4036 0.3380 0.3519 -0.0314 -0.0651 -0.0279 354 ARG A NH2 2681 N N . HIS A 355 ? 0.3547 0.3053 0.2865 -0.0363 -0.0518 -0.0456 355 HIS A N 2682 C CA . HIS A 355 ? 0.3588 0.3090 0.2864 -0.0389 -0.0508 -0.0467 355 HIS A CA 2683 C C . HIS A 355 ? 0.3744 0.3163 0.2970 -0.0395 -0.0540 -0.0459 355 HIS A C 2684 O O . HIS A 355 ? 0.3659 0.3023 0.2871 -0.0370 -0.0569 -0.0458 355 HIS A O 2685 C CB . HIS A 355 ? 0.3615 0.3186 0.2877 -0.0372 -0.0480 -0.0518 355 HIS A CB 2686 C CG . HIS A 355 ? 0.3748 0.3303 0.2982 -0.0323 -0.0493 -0.0556 355 HIS A CG 2687 N ND1 . HIS A 355 ? 0.3786 0.3384 0.3047 -0.0280 -0.0488 -0.0580 355 HIS A ND1 2688 C CD2 . HIS A 355 ? 0.3955 0.3448 0.3128 -0.0308 -0.0514 -0.0575 355 HIS A CD2 2689 C CE1 . HIS A 355 ? 0.3923 0.3488 0.3142 -0.0237 -0.0505 -0.0613 355 HIS A CE1 2690 N NE2 . HIS A 355 ? 0.3961 0.3459 0.3124 -0.0255 -0.0520 -0.0609 355 HIS A NE2 2691 N N . GLN A 356 ? 0.3878 0.3278 0.3071 -0.0430 -0.0538 -0.0450 356 GLN A N 2692 C CA . GLN A 356 ? 0.4139 0.3464 0.3273 -0.0440 -0.0564 -0.0449 356 GLN A CA 2693 C C . GLN A 356 ? 0.4069 0.3418 0.3162 -0.0452 -0.0542 -0.0480 356 GLN A C 2694 O O . GLN A 356 ? 0.3927 0.3316 0.3029 -0.0484 -0.0519 -0.0472 356 GLN A O 2695 C CB . GLN A 356 ? 0.4516 0.3790 0.3652 -0.0478 -0.0588 -0.0397 356 GLN A CB 2696 C CG . GLN A 356 ? 0.5000 0.4194 0.4073 -0.0492 -0.0618 -0.0393 356 GLN A CG 2697 C CD . GLN A 356 ? 0.5412 0.4560 0.4490 -0.0525 -0.0648 -0.0341 356 GLN A CD 2698 O OE1 . GLN A 356 ? 0.6281 0.5358 0.5320 -0.0531 -0.0682 -0.0330 356 GLN A OE1 2699 N NE2 . GLN A 356 ? 0.5793 0.4981 0.4915 -0.0547 -0.0636 -0.0308 356 GLN A NE2 2700 N N . ASN A 357 ? 0.4043 0.3365 0.3086 -0.0427 -0.0550 -0.0516 357 ASN A N 2701 C CA . ASN A 357 ? 0.4063 0.3409 0.3062 -0.0436 -0.0530 -0.0549 357 ASN A CA 2702 C C . ASN A 357 ? 0.4335 0.3599 0.3263 -0.0422 -0.0557 -0.0564 357 ASN A C 2703 O O . ASN A 357 ? 0.4068 0.3252 0.2982 -0.0418 -0.0593 -0.0542 357 ASN A O 2704 C CB . ASN A 357 ? 0.4065 0.3511 0.3085 -0.0409 -0.0494 -0.0593 357 ASN A CB 2705 C CG . ASN A 357 ? 0.4024 0.3473 0.3041 -0.0349 -0.0502 -0.0627 357 ASN A CG 2706 O OD1 . ASN A 357 ? 0.4181 0.3546 0.3167 -0.0326 -0.0536 -0.0623 357 ASN A OD1 2707 N ND2 . ASN A 357 ? 0.3931 0.3477 0.2975 -0.0323 -0.0473 -0.0662 357 ASN A ND2 2708 N N . SER A 358 ? 0.4745 0.4028 0.3627 -0.0419 -0.0541 -0.0602 358 SER A N 2709 C CA . SER A 358 ? 0.5077 0.4287 0.3883 -0.0401 -0.0562 -0.0625 358 SER A CA 2710 C C . SER A 358 ? 0.5164 0.4322 0.3948 -0.0346 -0.0588 -0.0644 358 SER A C 2711 O O . SER A 358 ? 0.5561 0.4623 0.4278 -0.0338 -0.0619 -0.0647 358 SER A O 2712 C CB . SER A 358 ? 0.5318 0.4585 0.4087 -0.0396 -0.0531 -0.0670 358 SER A CB 2713 O OG . SER A 358 ? 0.5528 0.4910 0.4343 -0.0373 -0.0495 -0.0700 358 SER A OG 2714 N N . GLU A 359 ? 0.5009 0.4226 0.3841 -0.0309 -0.0575 -0.0659 359 GLU A N 2715 C CA . GLU A 359 ? 0.5061 0.4240 0.3870 -0.0250 -0.0595 -0.0684 359 GLU A CA 2716 C C . GLU A 359 ? 0.4974 0.4093 0.3809 -0.0249 -0.0627 -0.0647 359 GLU A C 2717 O O . GLU A 359 ? 0.4993 0.4067 0.3804 -0.0202 -0.0648 -0.0663 359 GLU A O 2718 C CB . GLU A 359 ? 0.5189 0.4478 0.4029 -0.0203 -0.0562 -0.0730 359 GLU A CB 2719 C CG . GLU A 359 ? 0.5457 0.4823 0.4275 -0.0206 -0.0528 -0.0768 359 GLU A CG 2720 C CD . GLU A 359 ? 0.5703 0.5169 0.4534 -0.0149 -0.0503 -0.0819 359 GLU A CD 2721 O OE1 . GLU A 359 ? 0.6085 0.5513 0.4865 -0.0090 -0.0518 -0.0854 359 GLU A OE1 2722 O OE2 . GLU A 359 ? 0.5806 0.5390 0.4695 -0.0161 -0.0467 -0.0826 359 GLU A OE2 2723 N N . GLY A 360 ? 0.4618 0.3736 0.3498 -0.0298 -0.0631 -0.0597 360 GLY A N 2724 C CA . GLY A 360 ? 0.4473 0.3539 0.3377 -0.0304 -0.0660 -0.0557 360 GLY A CA 2725 C C . GLY A 360 ? 0.4284 0.3424 0.3274 -0.0325 -0.0641 -0.0526 360 GLY A C 2726 O O . GLY A 360 ? 0.3981 0.3190 0.3003 -0.0351 -0.0611 -0.0522 360 GLY A O 2727 N N . ILE A 361 ? 0.4236 0.3353 0.3255 -0.0313 -0.0660 -0.0504 361 ILE A N 2728 C CA . ILE A 361 ? 0.4334 0.3511 0.3430 -0.0326 -0.0646 -0.0474 361 ILE A CA 2729 C C . ILE A 361 ? 0.4315 0.3525 0.3439 -0.0279 -0.0640 -0.0498 361 ILE A C 2730 O O . ILE A 361 ? 0.4387 0.3532 0.3476 -0.0248 -0.0668 -0.0507 361 ILE A O 2731 C CB . ILE A 361 ? 0.4488 0.3613 0.3597 -0.0362 -0.0675 -0.0419 361 ILE A CB 2732 C CG1 . ILE A 361 ? 0.4700 0.3811 0.3792 -0.0410 -0.0677 -0.0394 361 ILE A CG1 2733 C CG2 . ILE A 361 ? 0.4638 0.3821 0.3823 -0.0366 -0.0662 -0.0392 361 ILE A CG2 2734 C CD1 . ILE A 361 ? 0.4931 0.3951 0.3978 -0.0436 -0.0719 -0.0364 361 ILE A CD1 2735 N N . GLY A 362 ? 0.4119 0.3425 0.3300 -0.0273 -0.0605 -0.0508 362 GLY A N 2736 C CA . GLY A 362 ? 0.4134 0.3486 0.3342 -0.0225 -0.0596 -0.0536 362 GLY A CA 2737 C C . GLY A 362 ? 0.4119 0.3537 0.3400 -0.0236 -0.0576 -0.0514 362 GLY A C 2738 O O . GLY A 362 ? 0.3872 0.3312 0.3181 -0.0278 -0.0564 -0.0482 362 GLY A O 2739 N N . GLN A 363 ? 0.4164 0.3608 0.3469 -0.0196 -0.0575 -0.0530 363 GLN A N 2740 C CA . GLN A 363 ? 0.4114 0.3619 0.3486 -0.0200 -0.0559 -0.0513 363 GLN A CA 2741 C C . GLN A 363 ? 0.4083 0.3664 0.3473 -0.0156 -0.0538 -0.0556 363 GLN A C 2742 O O . GLN A 363 ? 0.4028 0.3591 0.3385 -0.0110 -0.0551 -0.0590 363 GLN A O 2743 C CB . GLN A 363 ? 0.4271 0.3713 0.3654 -0.0200 -0.0589 -0.0477 363 GLN A CB 2744 C CG . GLN A 363 ? 0.4410 0.3903 0.3858 -0.0200 -0.0576 -0.0457 363 GLN A CG 2745 C CD . GLN A 363 ? 0.4543 0.3971 0.3996 -0.0204 -0.0607 -0.0420 363 GLN A CD 2746 O OE1 . GLN A 363 ? 0.4761 0.4161 0.4221 -0.0241 -0.0618 -0.0378 363 GLN A OE1 2747 N NE2 . GLN A 363 ? 0.4684 0.4089 0.4131 -0.0165 -0.0624 -0.0435 363 GLN A NE2 2748 N N . ALA A 364 ? 0.3836 0.3506 0.3278 -0.0169 -0.0507 -0.0555 364 ALA A N 2749 C CA . ALA A 364 ? 0.3742 0.3496 0.3212 -0.0133 -0.0487 -0.0590 364 ALA A CA 2750 C C . ALA A 364 ? 0.3759 0.3564 0.3289 -0.0153 -0.0469 -0.0565 364 ALA A C 2751 O O . ALA A 364 ? 0.3434 0.3248 0.2978 -0.0199 -0.0455 -0.0537 364 ALA A O 2752 C CB . ALA A 364 ? 0.3727 0.3561 0.3182 -0.0130 -0.0459 -0.0631 364 ALA A CB 2753 N N . ALA A 365 ? 0.3869 0.3704 0.3426 -0.0117 -0.0471 -0.0577 365 ALA A N 2754 C CA . ALA A 365 ? 0.3925 0.3813 0.3536 -0.0129 -0.0454 -0.0560 365 ALA A CA 2755 C C . ALA A 365 ? 0.4000 0.3994 0.3628 -0.0144 -0.0417 -0.0585 365 ALA A C 2756 O O . ALA A 365 ? 0.4032 0.4078 0.3642 -0.0124 -0.0406 -0.0625 365 ALA A O 2757 C CB . ALA A 365 ? 0.4031 0.3914 0.3661 -0.0084 -0.0470 -0.0567 365 ALA A CB 2758 N N . ASP A 366 ? 0.3872 0.3897 0.3531 -0.0180 -0.0397 -0.0561 366 ASP A N 2759 C CA . ASP A 366 ? 0.4030 0.4155 0.3704 -0.0200 -0.0363 -0.0580 366 ASP A CA 2760 C C . ASP A 366 ? 0.4218 0.4397 0.3934 -0.0177 -0.0358 -0.0587 366 ASP A C 2761 O O . ASP A 366 ? 0.3923 0.4071 0.3664 -0.0185 -0.0363 -0.0555 366 ASP A O 2762 C CB . ASP A 366 ? 0.4094 0.4209 0.3761 -0.0258 -0.0346 -0.0550 366 ASP A CB 2763 C CG . ASP A 366 ? 0.4244 0.4453 0.3915 -0.0287 -0.0313 -0.0569 366 ASP A CG 2764 O OD1 . ASP A 366 ? 0.4381 0.4643 0.4029 -0.0294 -0.0298 -0.0600 366 ASP A OD1 2765 O OD2 . ASP A 366 ? 0.4161 0.4391 0.3855 -0.0305 -0.0301 -0.0552 366 ASP A OD2 2766 N N . LEU A 367 ? 0.4327 0.4590 0.4050 -0.0145 -0.0348 -0.0629 367 LEU A N 2767 C CA . LEU A 367 ? 0.4568 0.4882 0.4328 -0.0114 -0.0347 -0.0639 367 LEU A CA 2768 C C . LEU A 367 ? 0.4507 0.4874 0.4295 -0.0154 -0.0323 -0.0623 367 LEU A C 2769 O O . LEU A 367 ? 0.4475 0.4829 0.4292 -0.0146 -0.0330 -0.0604 367 LEU A O 2770 C CB . LEU A 367 ? 0.4844 0.5244 0.4604 -0.0067 -0.0343 -0.0690 367 LEU A CB 2771 C CG . LEU A 367 ? 0.5210 0.5679 0.5008 -0.0032 -0.0341 -0.0705 367 LEU A CG 2772 C CD1 . LEU A 367 ? 0.5378 0.5760 0.5183 0.0005 -0.0374 -0.0687 367 LEU A CD1 2773 C CD2 . LEU A 367 ? 0.5505 0.6082 0.5302 0.0008 -0.0331 -0.0756 367 LEU A CD2 2774 N N . LYS A 368 ? 0.4493 0.4914 0.4267 -0.0199 -0.0297 -0.0629 368 LYS A N 2775 C CA . LYS A 368 ? 0.4667 0.5141 0.4457 -0.0239 -0.0273 -0.0619 368 LYS A CA 2776 C C . LYS A 368 ? 0.4508 0.4901 0.4305 -0.0262 -0.0281 -0.0572 368 LYS A C 2777 O O . LYS A 368 ? 0.4237 0.4650 0.4060 -0.0263 -0.0276 -0.0562 368 LYS A O 2778 C CB . LYS A 368 ? 0.4998 0.5523 0.4757 -0.0291 -0.0247 -0.0629 368 LYS A CB 2779 C CG . LYS A 368 ? 0.5386 0.5957 0.5147 -0.0341 -0.0224 -0.0618 368 LYS A CG 2780 C CD . LYS A 368 ? 0.5813 0.6348 0.5528 -0.0401 -0.0211 -0.0600 368 LYS A CD 2781 C CE . LYS A 368 ? 0.6040 0.6638 0.5740 -0.0456 -0.0185 -0.0601 368 LYS A CE 2782 N NZ . LYS A 368 ? 0.6244 0.6829 0.5889 -0.0510 -0.0172 -0.0599 368 LYS A NZ 2783 N N . SER A 369 ? 0.4181 0.4486 0.3954 -0.0279 -0.0292 -0.0545 369 SER A N 2784 C CA . SER A 369 ? 0.4038 0.4270 0.3815 -0.0299 -0.0298 -0.0500 369 SER A CA 2785 C C . SER A 369 ? 0.3801 0.3998 0.3611 -0.0260 -0.0320 -0.0485 369 SER A C 2786 O O . SER A 369 ? 0.3648 0.3833 0.3478 -0.0266 -0.0318 -0.0461 369 SER A O 2787 C CB . SER A 369 ? 0.4031 0.4187 0.3775 -0.0322 -0.0307 -0.0475 369 SER A CB 2788 O OG . SER A 369 ? 0.4198 0.4313 0.3937 -0.0292 -0.0331 -0.0482 369 SER A OG 2789 N N . THR A 370 ? 0.3592 0.3770 0.3404 -0.0219 -0.0341 -0.0501 370 THR A N 2790 C CA . THR A 370 ? 0.3598 0.3738 0.3433 -0.0183 -0.0365 -0.0490 370 THR A CA 2791 C C . THR A 370 ? 0.3727 0.3933 0.3595 -0.0166 -0.0355 -0.0503 370 THR A C 2792 O O . THR A 370 ? 0.3613 0.3795 0.3504 -0.0161 -0.0361 -0.0479 370 THR A O 2793 C CB . THR A 370 ? 0.3597 0.3705 0.3415 -0.0142 -0.0390 -0.0510 370 THR A CB 2794 O OG1 . THR A 370 ? 0.3333 0.3373 0.3119 -0.0160 -0.0402 -0.0494 370 THR A OG1 2795 C CG2 . THR A 370 ? 0.3480 0.3547 0.3316 -0.0105 -0.0416 -0.0501 370 THR A CG2 2796 N N . GLN A 371 ? 0.3824 0.4118 0.3695 -0.0157 -0.0339 -0.0542 371 GLN A N 2797 C CA . GLN A 371 ? 0.4012 0.4379 0.3913 -0.0141 -0.0330 -0.0558 371 GLN A CA 2798 C C . GLN A 371 ? 0.3862 0.4248 0.3774 -0.0184 -0.0309 -0.0535 371 GLN A C 2799 O O . GLN A 371 ? 0.3763 0.4163 0.3701 -0.0174 -0.0310 -0.0528 371 GLN A O 2800 C CB . GLN A 371 ? 0.4417 0.4886 0.4317 -0.0122 -0.0317 -0.0605 371 GLN A CB 2801 C CG . GLN A 371 ? 0.4858 0.5400 0.4791 -0.0087 -0.0317 -0.0626 371 GLN A CG 2802 C CD . GLN A 371 ? 0.5119 0.5597 0.5061 -0.0035 -0.0348 -0.0622 371 GLN A CD 2803 O OE1 . GLN A 371 ? 0.5447 0.5869 0.5366 -0.0003 -0.0370 -0.0630 371 GLN A OE1 2804 N NE2 . GLN A 371 ? 0.5183 0.5663 0.5154 -0.0028 -0.0352 -0.0607 371 GLN A NE2 2805 N N . ALA A 372 ? 0.3688 0.4066 0.3573 -0.0232 -0.0292 -0.0523 372 ALA A N 2806 C CA . ALA A 372 ? 0.3784 0.4161 0.3664 -0.0275 -0.0274 -0.0500 372 ALA A CA 2807 C C . ALA A 372 ? 0.3671 0.3971 0.3565 -0.0268 -0.0288 -0.0460 372 ALA A C 2808 O O . ALA A 372 ? 0.3584 0.3897 0.3491 -0.0274 -0.0280 -0.0450 372 ALA A O 2809 C CB . ALA A 372 ? 0.3788 0.4149 0.3626 -0.0323 -0.0259 -0.0492 372 ALA A CB 2810 N N . ALA A 373 ? 0.3522 0.3745 0.3411 -0.0255 -0.0307 -0.0438 373 ALA A N 2811 C CA . ALA A 373 ? 0.3476 0.3634 0.3380 -0.0247 -0.0321 -0.0400 373 ALA A CA 2812 C C . ALA A 373 ? 0.3486 0.3657 0.3424 -0.0208 -0.0335 -0.0406 373 ALA A C 2813 O O . ALA A 373 ? 0.3465 0.3627 0.3419 -0.0209 -0.0333 -0.0386 373 ALA A O 2814 C CB . ALA A 373 ? 0.3416 0.3501 0.3307 -0.0244 -0.0341 -0.0377 373 ALA A CB 2815 N N . ILE A 374 ? 0.3547 0.3736 0.3491 -0.0174 -0.0349 -0.0434 374 ILE A N 2816 C CA . ILE A 374 ? 0.3733 0.3925 0.3702 -0.0133 -0.0366 -0.0441 374 ILE A CA 2817 C C . ILE A 374 ? 0.3739 0.4002 0.3729 -0.0134 -0.0349 -0.0455 374 ILE A C 2818 O O . ILE A 374 ? 0.3646 0.3897 0.3657 -0.0121 -0.0356 -0.0440 374 ILE A O 2819 C CB . ILE A 374 ? 0.3759 0.3951 0.3718 -0.0093 -0.0386 -0.0472 374 ILE A CB 2820 C CG1 . ILE A 374 ? 0.3843 0.3944 0.3779 -0.0091 -0.0410 -0.0450 374 ILE A CG1 2821 C CG2 . ILE A 374 ? 0.3893 0.4102 0.3872 -0.0049 -0.0400 -0.0487 374 ILE A CG2 2822 C CD1 . ILE A 374 ? 0.3880 0.3964 0.3792 -0.0055 -0.0431 -0.0479 374 ILE A CD1 2823 N N . ASN A 375 ? 0.3815 0.4156 0.3799 -0.0154 -0.0326 -0.0481 375 ASN A N 2824 C CA . ASN A 375 ? 0.4006 0.4424 0.4007 -0.0162 -0.0309 -0.0494 375 ASN A CA 2825 C C . ASN A 375 ? 0.3917 0.4302 0.3918 -0.0193 -0.0299 -0.0461 375 ASN A C 2826 O O . ASN A 375 ? 0.3715 0.4123 0.3736 -0.0184 -0.0299 -0.0459 375 ASN A O 2827 C CB . ASN A 375 ? 0.4223 0.4731 0.4211 -0.0187 -0.0286 -0.0526 375 ASN A CB 2828 C CG . ASN A 375 ? 0.4319 0.4890 0.4314 -0.0147 -0.0293 -0.0567 375 ASN A CG 2829 O OD1 . ASN A 375 ? 0.4697 0.5248 0.4706 -0.0096 -0.0316 -0.0576 375 ASN A OD1 2830 N ND2 . ASN A 375 ? 0.4582 0.5230 0.4564 -0.0168 -0.0274 -0.0593 375 ASN A ND2 2831 N N . GLN A 376 ? 0.3737 0.4066 0.3711 -0.0227 -0.0292 -0.0434 376 GLN A N 2832 C CA . GLN A 376 ? 0.3805 0.4095 0.3770 -0.0253 -0.0283 -0.0402 376 GLN A CA 2833 C C . GLN A 376 ? 0.3617 0.3851 0.3604 -0.0225 -0.0301 -0.0374 376 GLN A C 2834 O O . GLN A 376 ? 0.3502 0.3731 0.3496 -0.0230 -0.0295 -0.0359 376 GLN A O 2835 C CB . GLN A 376 ? 0.3830 0.4071 0.3756 -0.0290 -0.0273 -0.0381 376 GLN A CB 2836 C CG . GLN A 376 ? 0.4032 0.4325 0.3926 -0.0329 -0.0253 -0.0404 376 GLN A CG 2837 C CD . GLN A 376 ? 0.3992 0.4227 0.3843 -0.0362 -0.0247 -0.0384 376 GLN A CD 2838 O OE1 . GLN A 376 ? 0.4240 0.4422 0.4067 -0.0380 -0.0242 -0.0356 376 GLN A OE1 2839 N NE2 . GLN A 376 ? 0.4503 0.4746 0.4340 -0.0367 -0.0248 -0.0398 376 GLN A NE2 2840 N N . ILE A 377 ? 0.3441 0.3633 0.3438 -0.0199 -0.0323 -0.0367 377 ILE A N 2841 C CA . ILE A 377 ? 0.3434 0.3576 0.3450 -0.0176 -0.0341 -0.0341 377 ILE A CA 2842 C C . ILE A 377 ? 0.3579 0.3758 0.3622 -0.0146 -0.0349 -0.0359 377 ILE A C 2843 O O . ILE A 377 ? 0.3613 0.3777 0.3670 -0.0140 -0.0351 -0.0340 377 ILE A O 2844 C CB . ILE A 377 ? 0.3308 0.3394 0.3319 -0.0162 -0.0365 -0.0328 377 ILE A CB 2845 C CG1 . ILE A 377 ? 0.3259 0.3304 0.3248 -0.0192 -0.0358 -0.0301 377 ILE A CG1 2846 C CG2 . ILE A 377 ? 0.3253 0.3299 0.3284 -0.0137 -0.0387 -0.0308 377 ILE A CG2 2847 C CD1 . ILE A 377 ? 0.3236 0.3239 0.3214 -0.0187 -0.0378 -0.0294 377 ILE A CD1 2848 N N . ASN A 378 ? 0.3650 0.3880 0.3697 -0.0125 -0.0353 -0.0396 378 ASN A N 2849 C CA . ASN A 378 ? 0.3846 0.4119 0.3916 -0.0093 -0.0360 -0.0417 378 ASN A CA 2850 C C . ASN A 378 ? 0.3873 0.4196 0.3952 -0.0114 -0.0340 -0.0417 378 ASN A C 2851 O O . ASN A 378 ? 0.3962 0.4292 0.4061 -0.0095 -0.0347 -0.0414 378 ASN A O 2852 C CB . ASN A 378 ? 0.3997 0.4322 0.4067 -0.0063 -0.0367 -0.0459 378 ASN A CB 2853 C CG . ASN A 378 ? 0.4138 0.4401 0.4197 -0.0028 -0.0396 -0.0460 378 ASN A CG 2854 O OD1 . ASN A 378 ? 0.4291 0.4480 0.4350 -0.0023 -0.0415 -0.0430 378 ASN A OD1 2855 N ND2 . ASN A 378 ? 0.4178 0.4469 0.4225 -0.0004 -0.0402 -0.0493 378 ASN A ND2 2856 N N . GLY A 379 ? 0.3754 0.4105 0.3815 -0.0155 -0.0316 -0.0418 379 GLY A N 2857 C CA . GLY A 379 ? 0.3963 0.4348 0.4020 -0.0184 -0.0296 -0.0414 379 GLY A CA 2858 C C . GLY A 379 ? 0.4064 0.4386 0.4121 -0.0187 -0.0299 -0.0378 379 GLY A C 2859 O O . GLY A 379 ? 0.3787 0.4130 0.3856 -0.0184 -0.0296 -0.0378 379 GLY A O 2860 N N . LYS A 380 ? 0.3914 0.4160 0.3957 -0.0193 -0.0303 -0.0347 380 LYS A N 2861 C CA . LYS A 380 ? 0.3907 0.4099 0.3950 -0.0193 -0.0305 -0.0313 380 LYS A CA 2862 C C . LYS A 380 ? 0.3721 0.3900 0.3796 -0.0156 -0.0326 -0.0307 380 LYS A C 2863 O O . LYS A 380 ? 0.3848 0.4016 0.3930 -0.0153 -0.0324 -0.0292 380 LYS A O 2864 C CB . LYS A 380 ? 0.4158 0.4284 0.4176 -0.0210 -0.0301 -0.0280 380 LYS A CB 2865 C CG . LYS A 380 ? 0.4315 0.4409 0.4336 -0.0199 -0.0317 -0.0273 380 LYS A CG 2866 C CD . LYS A 380 ? 0.4178 0.4217 0.4176 -0.0216 -0.0313 -0.0239 380 LYS A CD 2867 C CE . LYS A 380 ? 0.4132 0.4175 0.4091 -0.0250 -0.0294 -0.0247 380 LYS A CE 2868 N NZ . LYS A 380 ? 0.3903 0.3889 0.3833 -0.0262 -0.0289 -0.0214 380 LYS A NZ 2869 N N . LEU A 381 ? 0.3649 0.3827 0.3738 -0.0128 -0.0346 -0.0321 381 LEU A N 2870 C CA . LEU A 381 ? 0.3654 0.3816 0.3763 -0.0094 -0.0368 -0.0319 381 LEU A CA 2871 C C . LEU A 381 ? 0.3846 0.4067 0.3971 -0.0082 -0.0364 -0.0342 381 LEU A C 2872 O O . LEU A 381 ? 0.3778 0.3984 0.3916 -0.0068 -0.0372 -0.0330 381 LEU A O 2873 C CB . LEU A 381 ? 0.3727 0.3872 0.3837 -0.0065 -0.0392 -0.0334 381 LEU A CB 2874 C CG . LEU A 381 ? 0.3661 0.3741 0.3757 -0.0074 -0.0405 -0.0308 381 LEU A CG 2875 C CD1 . LEU A 381 ? 0.3703 0.3764 0.3789 -0.0050 -0.0428 -0.0327 381 LEU A CD1 2876 C CD2 . LEU A 381 ? 0.3601 0.3631 0.3705 -0.0074 -0.0414 -0.0269 381 LEU A CD2 2877 N N . ASN A 382 ? 0.4026 0.4318 0.4149 -0.0090 -0.0350 -0.0374 382 ASN A N 2878 C CA . ASN A 382 ? 0.4313 0.4675 0.4452 -0.0082 -0.0346 -0.0397 382 ASN A CA 2879 C C . ASN A 382 ? 0.4168 0.4526 0.4303 -0.0109 -0.0330 -0.0376 382 ASN A C 2880 O O . ASN A 382 ? 0.4225 0.4610 0.4375 -0.0095 -0.0335 -0.0382 382 ASN A O 2881 C CB . ASN A 382 ? 0.4753 0.5203 0.4890 -0.0089 -0.0333 -0.0434 382 ASN A CB 2882 C CG . ASN A 382 ? 0.5304 0.5771 0.5448 -0.0047 -0.0352 -0.0462 382 ASN A CG 2883 O OD1 . ASN A 382 ? 0.5905 0.6315 0.6053 -0.0013 -0.0376 -0.0455 382 ASN A OD1 2884 N ND2 . ASN A 382 ? 0.5667 0.6211 0.5809 -0.0051 -0.0340 -0.0494 382 ASN A ND2 2885 N N . ARG A 383 ? 0.3889 0.4206 0.3998 -0.0144 -0.0314 -0.0352 383 ARG A N 2886 C CA . ARG A 383 ? 0.4089 0.4385 0.4184 -0.0166 -0.0301 -0.0330 383 ARG A CA 2887 C C . ARG A 383 ? 0.3841 0.4076 0.3947 -0.0145 -0.0314 -0.0301 383 ARG A C 2888 O O . ARG A 383 ? 0.3794 0.4022 0.3897 -0.0150 -0.0309 -0.0289 383 ARG A O 2889 C CB . ARG A 383 ? 0.4597 0.4857 0.4651 -0.0206 -0.0282 -0.0313 383 ARG A CB 2890 C CG . ARG A 383 ? 0.5199 0.5509 0.5229 -0.0240 -0.0266 -0.0336 383 ARG A CG 2891 C CD . ARG A 383 ? 0.5837 0.6088 0.5820 -0.0274 -0.0252 -0.0314 383 ARG A CD 2892 N NE . ARG A 383 ? 0.6520 0.6810 0.6469 -0.0316 -0.0235 -0.0332 383 ARG A NE 2893 C CZ . ARG A 383 ? 0.6834 0.7077 0.6729 -0.0354 -0.0222 -0.0317 383 ARG A CZ 2894 N NH1 . ARG A 383 ? 0.7165 0.7322 0.7035 -0.0350 -0.0222 -0.0285 383 ARG A NH1 2895 N NH2 . ARG A 383 ? 0.6510 0.6792 0.6371 -0.0395 -0.0208 -0.0335 383 ARG A NH2 2896 N N . LEU A 384 ? 0.3550 0.3740 0.3666 -0.0124 -0.0331 -0.0287 384 LEU A N 2897 C CA . LEU A 384 ? 0.3522 0.3654 0.3644 -0.0111 -0.0342 -0.0254 384 LEU A CA 2898 C C . LEU A 384 ? 0.3503 0.3629 0.3649 -0.0077 -0.0367 -0.0258 384 LEU A C 2899 O O . LEU A 384 ? 0.3451 0.3542 0.3602 -0.0069 -0.0374 -0.0234 384 LEU A O 2900 C CB . LEU A 384 ? 0.3395 0.3477 0.3506 -0.0118 -0.0345 -0.0229 384 LEU A CB 2901 C CG . LEU A 384 ? 0.3454 0.3520 0.3534 -0.0148 -0.0322 -0.0214 384 LEU A CG 2902 C CD1 . LEU A 384 ? 0.3533 0.3561 0.3604 -0.0152 -0.0327 -0.0195 384 LEU A CD1 2903 C CD2 . LEU A 384 ? 0.3611 0.3653 0.3678 -0.0155 -0.0310 -0.0192 384 LEU A CD2 2904 N N . ILE A 385 ? 0.3271 0.3427 0.3426 -0.0056 -0.0381 -0.0287 385 ILE A N 2905 C CA . ILE A 385 ? 0.3358 0.3494 0.3525 -0.0021 -0.0409 -0.0292 385 ILE A CA 2906 C C . ILE A 385 ? 0.3395 0.3587 0.3575 -0.0002 -0.0411 -0.0320 385 ILE A C 2907 O O . ILE A 385 ? 0.3387 0.3646 0.3570 -0.0006 -0.0399 -0.0350 385 ILE A O 2908 C CB . ILE A 385 ? 0.3469 0.3585 0.3628 -0.0004 -0.0428 -0.0306 385 ILE A CB 2909 C CG1 . ILE A 385 ? 0.3600 0.3664 0.3747 -0.0025 -0.0428 -0.0276 385 ILE A CG1 2910 C CG2 . ILE A 385 ? 0.3504 0.3590 0.3663 0.0032 -0.0460 -0.0313 385 ILE A CG2 2911 C CD1 . ILE A 385 ? 0.3593 0.3603 0.3742 -0.0030 -0.0437 -0.0236 385 ILE A CD1 2912 N N . GLY A 386 ? 0.3392 0.3560 0.3580 0.0017 -0.0427 -0.0310 386 GLY A N 2913 C CA . GLY A 386 ? 0.3505 0.3722 0.3705 0.0040 -0.0434 -0.0335 386 GLY A CA 2914 C C . GLY A 386 ? 0.3546 0.3820 0.3752 0.0015 -0.0410 -0.0341 386 GLY A C 2915 O O . GLY A 386 ? 0.3692 0.4035 0.3909 0.0028 -0.0410 -0.0369 386 GLY A O 2916 N N . LYS A 387 ? 0.3470 0.3717 0.3664 -0.0018 -0.0390 -0.0313 387 LYS A N 2917 C CA . LYS A 387 ? 0.3582 0.3870 0.3768 -0.0047 -0.0367 -0.0316 387 LYS A CA 2918 C C . LYS A 387 ? 0.3460 0.3707 0.3638 -0.0057 -0.0361 -0.0287 387 LYS A C 2919 O O . LYS A 387 ? 0.3480 0.3731 0.3638 -0.0088 -0.0341 -0.0280 387 LYS A O 2920 C CB . LYS A 387 ? 0.3734 0.4030 0.3899 -0.0083 -0.0344 -0.0316 387 LYS A CB 2921 C CG . LYS A 387 ? 0.3859 0.4204 0.4029 -0.0077 -0.0346 -0.0346 387 LYS A CG 2922 C CD . LYS A 387 ? 0.3970 0.4410 0.4155 -0.0071 -0.0344 -0.0382 387 LYS A CD 2923 C CE . LYS A 387 ? 0.4148 0.4647 0.4336 -0.0067 -0.0341 -0.0413 387 LYS A CE 2924 N NZ . LYS A 387 ? 0.4357 0.4821 0.4552 -0.0028 -0.0364 -0.0419 387 LYS A NZ 2925 N N . THR A 388 ? 0.3364 0.3570 0.3552 -0.0032 -0.0381 -0.0272 388 THR A N 2926 C CA . THR A 388 ? 0.3342 0.3507 0.3521 -0.0040 -0.0376 -0.0244 388 THR A CA 2927 C C . THR A 388 ? 0.3650 0.3858 0.3828 -0.0047 -0.0368 -0.0257 388 THR A C 2928 O O . THR A 388 ? 0.3552 0.3824 0.3745 -0.0036 -0.0375 -0.0288 388 THR A O 2929 C CB . THR A 388 ? 0.3236 0.3350 0.3425 -0.0014 -0.0399 -0.0224 388 THR A CB 2930 O OG1 . THR A 388 ? 0.3206 0.3345 0.3409 0.0015 -0.0422 -0.0248 388 THR A OG1 2931 C CG2 . THR A 388 ? 0.3193 0.3263 0.3379 -0.0013 -0.0408 -0.0206 388 THR A CG2 2932 N N . ASN A 389 ? 0.3567 0.3742 0.3725 -0.0065 -0.0355 -0.0234 389 ASN A N 2933 C CA A ASN A 389 ? 0.3750 0.3956 0.3901 -0.0077 -0.0348 -0.0242 389 ASN A CA 2934 C CA B ASN A 389 ? 0.3704 0.3909 0.3855 -0.0077 -0.0348 -0.0241 389 ASN A CA 2935 C C . ASN A 389 ? 0.3587 0.3760 0.3744 -0.0057 -0.0362 -0.0226 389 ASN A C 2936 O O . ASN A 389 ? 0.3557 0.3673 0.3713 -0.0047 -0.0367 -0.0199 389 ASN A O 2937 C CB A ASN A 389 ? 0.3984 0.4178 0.4096 -0.0116 -0.0322 -0.0233 389 ASN A CB 2938 C CB B ASN A 389 ? 0.3848 0.4032 0.3958 -0.0115 -0.0322 -0.0228 389 ASN A CB 2939 C CG A ASN A 389 ? 0.4159 0.4277 0.4245 -0.0122 -0.0311 -0.0198 389 ASN A CG 2940 C CG B ASN A 389 ? 0.3985 0.4208 0.4082 -0.0142 -0.0308 -0.0248 389 ASN A CG 2941 O OD1 A ASN A 389 ? 0.4452 0.4530 0.4550 -0.0100 -0.0321 -0.0177 389 ASN A OD1 2942 O OD1 B ASN A 389 ? 0.3989 0.4273 0.4110 -0.0133 -0.0316 -0.0275 389 ASN A OD1 2943 N ND2 A ASN A 389 ? 0.4212 0.4310 0.4256 -0.0152 -0.0290 -0.0193 389 ASN A ND2 2944 N ND2 B ASN A 389 ? 0.4063 0.4252 0.4117 -0.0174 -0.0288 -0.0234 389 ASN A ND2 2945 N N . GLU A 390 ? 0.3320 0.3533 0.3484 -0.0053 -0.0367 -0.0242 390 GLU A N 2946 C CA . GLU A 390 ? 0.3108 0.3294 0.3276 -0.0035 -0.0382 -0.0229 390 GLU A CA 2947 C C . GLU A 390 ? 0.2781 0.2923 0.2919 -0.0057 -0.0365 -0.0203 390 GLU A C 2948 O O . GLU A 390 ? 0.2694 0.2851 0.2807 -0.0086 -0.0346 -0.0207 390 GLU A O 2949 C CB . GLU A 390 ? 0.3352 0.3604 0.3538 -0.0021 -0.0396 -0.0258 390 GLU A CB 2950 C CG . GLU A 390 ? 0.3645 0.3927 0.3858 0.0015 -0.0420 -0.0282 390 GLU A CG 2951 C CD . GLU A 390 ? 0.3832 0.4172 0.4061 0.0038 -0.0437 -0.0307 390 GLU A CD 2952 O OE1 . GLU A 390 ? 0.3812 0.4225 0.4043 0.0020 -0.0425 -0.0326 390 GLU A OE1 2953 O OE2 . GLU A 390 ? 0.4039 0.4349 0.4273 0.0072 -0.0463 -0.0305 390 GLU A OE2 2954 N N . LYS A 391 ? 0.2506 0.2593 0.2642 -0.0042 -0.0373 -0.0177 391 LYS A N 2955 C CA . LYS A 391 ? 0.2440 0.2489 0.2551 -0.0053 -0.0362 -0.0155 391 LYS A CA 2956 C C . LYS A 391 ? 0.2387 0.2423 0.2511 -0.0030 -0.0383 -0.0149 391 LYS A C 2957 O O . LYS A 391 ? 0.2254 0.2283 0.2399 -0.0007 -0.0405 -0.0150 391 LYS A O 2958 C CB . LYS A 391 ? 0.2561 0.2554 0.2650 -0.0059 -0.0346 -0.0123 391 LYS A CB 2959 C CG . LYS A 391 ? 0.2638 0.2631 0.2707 -0.0080 -0.0326 -0.0125 391 LYS A CG 2960 C CD . LYS A 391 ? 0.2652 0.2652 0.2682 -0.0109 -0.0308 -0.0135 391 LYS A CD 2961 C CE . LYS A 391 ? 0.2739 0.2725 0.2739 -0.0130 -0.0290 -0.0134 391 LYS A CE 2962 N NZ . LYS A 391 ? 0.2705 0.2697 0.2662 -0.0165 -0.0275 -0.0146 391 LYS A NZ 2963 N N . PHE A 392 ? 0.2181 0.2206 0.2284 -0.0039 -0.0377 -0.0143 392 PHE A N 2964 C CA . PHE A 392 ? 0.2241 0.2260 0.2354 -0.0021 -0.0397 -0.0141 392 PHE A CA 2965 C C . PHE A 392 ? 0.2141 0.2103 0.2230 -0.0024 -0.0389 -0.0109 392 PHE A C 2966 O O . PHE A 392 ? 0.2186 0.2112 0.2275 -0.0019 -0.0388 -0.0086 392 PHE A O 2967 C CB . PHE A 392 ? 0.2364 0.2441 0.2481 -0.0025 -0.0403 -0.0169 392 PHE A CB 2968 C CG . PHE A 392 ? 0.2470 0.2614 0.2613 -0.0018 -0.0410 -0.0201 392 PHE A CG 2969 C CD1 . PHE A 392 ? 0.2599 0.2750 0.2768 0.0013 -0.0435 -0.0212 392 PHE A CD1 2970 C CD2 . PHE A 392 ? 0.2660 0.2854 0.2795 -0.0045 -0.0393 -0.0218 392 PHE A CD2 2971 C CE1 . PHE A 392 ? 0.2681 0.2892 0.2871 0.0024 -0.0441 -0.0242 392 PHE A CE1 2972 C CE2 . PHE A 392 ? 0.2756 0.3019 0.2915 -0.0038 -0.0398 -0.0248 392 PHE A CE2 2973 C CZ . PHE A 392 ? 0.2714 0.2987 0.2902 0.0000 -0.0422 -0.0260 392 PHE A CZ 2974 N N . HIS A 393 ? 0.2110 0.2066 0.2177 -0.0034 -0.0383 -0.0107 393 HIS A N 2975 C CA . HIS A 393 ? 0.2121 0.2024 0.2162 -0.0035 -0.0374 -0.0077 393 HIS A CA 2976 C C . HIS A 393 ? 0.2144 0.2018 0.2152 -0.0051 -0.0346 -0.0061 393 HIS A C 2977 O O . HIS A 393 ? 0.2174 0.2058 0.2158 -0.0072 -0.0331 -0.0074 393 HIS A O 2978 C CB . HIS A 393 ? 0.2225 0.2126 0.2247 -0.0040 -0.0378 -0.0080 393 HIS A CB 2979 C CG . HIS A 393 ? 0.2292 0.2142 0.2293 -0.0035 -0.0375 -0.0052 393 HIS A CG 2980 N ND1 . HIS A 393 ? 0.2381 0.2210 0.2399 -0.0018 -0.0389 -0.0035 393 HIS A ND1 2981 C CD2 . HIS A 393 ? 0.2411 0.2227 0.2370 -0.0047 -0.0358 -0.0038 393 HIS A CD2 2982 C CE1 . HIS A 393 ? 0.2391 0.2182 0.2383 -0.0019 -0.0381 -0.0011 393 HIS A CE1 2983 N NE2 . HIS A 393 ? 0.2419 0.2201 0.2376 -0.0034 -0.0362 -0.0014 393 HIS A NE2 2984 N N A GLN A 394 ? 0.2083 0.1919 0.2085 -0.0042 -0.0339 -0.0033 394 GLN A N 2985 N N B GLN A 394 ? 0.2117 0.1954 0.2120 -0.0042 -0.0339 -0.0033 394 GLN A N 2986 C CA A GLN A 394 ? 0.2103 0.1912 0.2075 -0.0049 -0.0314 -0.0017 394 GLN A CA 2987 C CA B GLN A 394 ? 0.2165 0.1972 0.2136 -0.0049 -0.0314 -0.0017 394 GLN A CA 2988 C C A GLN A 394 ? 0.2121 0.1885 0.2058 -0.0043 -0.0300 0.0009 394 GLN A C 2989 C C B GLN A 394 ? 0.2157 0.1925 0.2103 -0.0039 -0.0305 0.0011 394 GLN A C 2990 O O A GLN A 394 ? 0.2188 0.1934 0.2092 -0.0051 -0.0293 0.0007 394 GLN A O 2991 O O B GLN A 394 ? 0.2263 0.2020 0.2197 -0.0040 -0.0309 0.0012 394 GLN A O 2992 C CB A GLN A 394 ? 0.2069 0.1889 0.2070 -0.0041 -0.0319 -0.0012 394 GLN A CB 2993 C CB B GLN A 394 ? 0.2173 0.1991 0.2167 -0.0043 -0.0315 -0.0013 394 GLN A CB 2994 C CG A GLN A 394 ? 0.2050 0.1911 0.2077 -0.0046 -0.0329 -0.0041 394 GLN A CG 2995 C CG B GLN A 394 ? 0.2192 0.2051 0.2210 -0.0051 -0.0324 -0.0042 394 GLN A CG 2996 C CD A GLN A 394 ? 0.2037 0.1909 0.2096 -0.0036 -0.0340 -0.0038 394 GLN A CD 2997 C CD B GLN A 394 ? 0.2230 0.2094 0.2263 -0.0048 -0.0322 -0.0038 394 GLN A CD 2998 O OE1 A GLN A 394 ? 0.2087 0.1944 0.2138 -0.0038 -0.0328 -0.0022 394 GLN A OE1 2999 O OE1 B GLN A 394 ? 0.2300 0.2154 0.2352 -0.0035 -0.0331 -0.0019 394 GLN A OE1 3000 N NE2 A GLN A 394 ? 0.2008 0.1903 0.2098 -0.0025 -0.0365 -0.0055 394 GLN A NE2 3001 N NE2 B GLN A 394 ? 0.2224 0.2104 0.2248 -0.0063 -0.0312 -0.0055 394 GLN A NE2 3002 N N . ILE A 395 ? 0.2102 0.1852 0.2042 -0.0030 -0.0293 0.0035 395 ILE A N 3003 C CA . ILE A 395 ? 0.2081 0.1802 0.1997 -0.0019 -0.0282 0.0062 395 ILE A CA 3004 C C . ILE A 395 ? 0.2067 0.1805 0.2023 -0.0008 -0.0297 0.0081 395 ILE A C 3005 O O . ILE A 395 ? 0.2013 0.1775 0.2005 -0.0008 -0.0311 0.0075 395 ILE A O 3006 C CB . ILE A 395 ? 0.2051 0.1741 0.1922 -0.0013 -0.0255 0.0076 395 ILE A CB 3007 C CG1 . ILE A 395 ? 0.2055 0.1763 0.1947 -0.0008 -0.0252 0.0082 395 ILE A CG1 3008 C CG2 . ILE A 395 ? 0.2086 0.1746 0.1904 -0.0029 -0.0242 0.0059 395 ILE A CG2 3009 C CD1 . ILE A 395 ? 0.2061 0.1741 0.1913 0.0005 -0.0229 0.0101 395 ILE A CD1 3010 N N . GLU A 396 ? 0.2118 0.1844 0.2064 0.0000 -0.0293 0.0104 396 GLU A N 3011 C CA . GLU A 396 ? 0.2173 0.1914 0.2147 0.0005 -0.0305 0.0127 396 GLU A CA 3012 C C . GLU A 396 ? 0.2133 0.1888 0.2110 0.0012 -0.0290 0.0145 396 GLU A C 3013 O O . GLU A 396 ? 0.2100 0.1841 0.2045 0.0020 -0.0267 0.0148 396 GLU A O 3014 C CB . GLU A 396 ? 0.2303 0.2032 0.2263 0.0009 -0.0305 0.0146 396 GLU A CB 3015 C CG . GLU A 396 ? 0.2420 0.2135 0.2377 0.0003 -0.0323 0.0129 396 GLU A CG 3016 C CD . GLU A 396 ? 0.2546 0.2272 0.2538 0.0000 -0.0356 0.0115 396 GLU A CD 3017 O OE1 . GLU A 396 ? 0.2804 0.2542 0.2820 -0.0001 -0.0368 0.0127 396 GLU A OE1 3018 O OE2 . GLU A 396 ? 0.2656 0.2380 0.2649 -0.0002 -0.0371 0.0092 396 GLU A OE2 3019 N N . LYS A 397 ? 0.2052 0.1831 0.2063 0.0009 -0.0305 0.0158 397 LYS A N 3020 C CA . LYS A 397 ? 0.2091 0.1891 0.2112 0.0014 -0.0296 0.0174 397 LYS A CA 3021 C C . LYS A 397 ? 0.2174 0.2001 0.2212 0.0013 -0.0302 0.0207 397 LYS A C 3022 O O . LYS A 397 ? 0.2253 0.2108 0.2301 0.0017 -0.0294 0.0225 397 LYS A O 3023 C CB . LYS A 397 ? 0.1999 0.1807 0.2043 0.0005 -0.0309 0.0154 397 LYS A CB 3024 C CG . LYS A 397 ? 0.2008 0.1800 0.2032 0.0003 -0.0299 0.0125 397 LYS A CG 3025 C CD . LYS A 397 ? 0.1974 0.1779 0.2019 -0.0004 -0.0310 0.0103 397 LYS A CD 3026 C CE . LYS A 397 ? 0.1968 0.1764 0.1992 -0.0012 -0.0302 0.0073 397 LYS A CE 3027 N NZ . LYS A 397 ? 0.1951 0.1766 0.1994 -0.0019 -0.0310 0.0052 397 LYS A NZ 3028 N N . GLU A 398 ? 0.2304 0.2126 0.2345 0.0006 -0.0316 0.0216 398 GLU A N 3029 C CA . GLU A 398 ? 0.2454 0.2303 0.2504 0.0000 -0.0321 0.0248 398 GLU A CA 3030 C C . GLU A 398 ? 0.2445 0.2280 0.2471 0.0005 -0.0313 0.0257 398 GLU A C 3031 O O . GLU A 398 ? 0.2332 0.2133 0.2344 0.0004 -0.0320 0.0236 398 GLU A O 3032 C CB . GLU A 398 ? 0.2856 0.2705 0.2930 -0.0019 -0.0355 0.0251 398 GLU A CB 3033 C CG . GLU A 398 ? 0.3093 0.2956 0.3189 -0.0026 -0.0364 0.0246 398 GLU A CG 3034 C CD . GLU A 398 ? 0.3591 0.3445 0.3699 -0.0047 -0.0399 0.0252 398 GLU A CD 3035 O OE1 . GLU A 398 ? 0.4090 0.3933 0.4189 -0.0059 -0.0415 0.0267 398 GLU A OE1 3036 O OE2 . GLU A 398 ? 0.3962 0.3816 0.4083 -0.0052 -0.0411 0.0242 398 GLU A OE2 3037 N N . PHE A 399 ? 0.2457 0.2322 0.2478 0.0009 -0.0300 0.0287 399 PHE A N 3038 C CA . PHE A 399 ? 0.2514 0.2368 0.2507 0.0016 -0.0288 0.0297 399 PHE A CA 3039 C C . PHE A 399 ? 0.2733 0.2623 0.2735 0.0002 -0.0295 0.0329 399 PHE A C 3040 O O . PHE A 399 ? 0.2857 0.2797 0.2877 0.0000 -0.0290 0.0351 399 PHE A O 3041 C CB . PHE A 399 ? 0.2481 0.2335 0.2443 0.0044 -0.0253 0.0298 399 PHE A CB 3042 C CG . PHE A 399 ? 0.2394 0.2210 0.2339 0.0051 -0.0247 0.0269 399 PHE A CG 3043 C CD1 . PHE A 399 ? 0.2381 0.2211 0.2340 0.0055 -0.0243 0.0264 399 PHE A CD1 3044 C CD2 . PHE A 399 ? 0.2436 0.2207 0.2352 0.0050 -0.0245 0.0248 399 PHE A CD2 3045 C CE1 . PHE A 399 ? 0.2410 0.2206 0.2351 0.0056 -0.0238 0.0237 399 PHE A CE1 3046 C CE2 . PHE A 399 ? 0.2449 0.2191 0.2349 0.0051 -0.0241 0.0221 399 PHE A CE2 3047 C CZ . PHE A 399 ? 0.2409 0.2163 0.2321 0.0053 -0.0237 0.0216 399 PHE A CZ 3048 N N . SER A 400 ? 0.2913 0.2781 0.2901 -0.0007 -0.0306 0.0332 400 SER A N 3049 C CA . SER A 400 ? 0.3154 0.3051 0.3143 -0.0026 -0.0314 0.0363 400 SER A CA 3050 C C . SER A 400 ? 0.3289 0.3216 0.3256 -0.0009 -0.0284 0.0384 400 SER A C 3051 O O . SER A 400 ? 0.3288 0.3260 0.3259 -0.0023 -0.0284 0.0413 400 SER A O 3052 C CB . SER A 400 ? 0.3211 0.3063 0.3192 -0.0048 -0.0346 0.0355 400 SER A CB 3053 O OG . SER A 400 ? 0.3518 0.3327 0.3474 -0.0035 -0.0341 0.0336 400 SER A OG 3054 N N . GLU A 401 ? 0.3223 0.3126 0.3162 0.0018 -0.0259 0.0369 401 GLU A N 3055 C CA . GLU A 401 ? 0.3458 0.3383 0.3369 0.0040 -0.0230 0.0386 401 GLU A CA 3056 C C . GLU A 401 ? 0.3309 0.3242 0.3204 0.0075 -0.0201 0.0382 401 GLU A C 3057 O O . GLU A 401 ? 0.3062 0.2962 0.2956 0.0081 -0.0203 0.0359 401 GLU A O 3058 C CB . GLU A 401 ? 0.3772 0.3642 0.3644 0.0044 -0.0227 0.0374 401 GLU A CB 3059 C CG . GLU A 401 ? 0.4337 0.4196 0.4212 0.0015 -0.0252 0.0383 401 GLU A CG 3060 C CD . GLU A 401 ? 0.4576 0.4395 0.4469 -0.0006 -0.0286 0.0361 401 GLU A CD 3061 O OE1 . GLU A 401 ? 0.5218 0.4998 0.5105 0.0003 -0.0287 0.0333 401 GLU A OE1 3062 O OE2 . GLU A 401 ? 0.4959 0.4787 0.4869 -0.0033 -0.0313 0.0374 401 GLU A OE2 3063 N N . VAL A 402 ? 0.3163 0.3139 0.3041 0.0099 -0.0176 0.0403 402 VAL A N 3064 C CA . VAL A 402 ? 0.3139 0.3114 0.2987 0.0140 -0.0147 0.0401 402 VAL A CA 3065 C C . VAL A 402 ? 0.3024 0.2922 0.2815 0.0158 -0.0133 0.0380 402 VAL A C 3066 O O . VAL A 402 ? 0.2893 0.2772 0.2660 0.0154 -0.0132 0.0384 402 VAL A O 3067 C CB . VAL A 402 ? 0.3265 0.3321 0.3115 0.0163 -0.0125 0.0432 402 VAL A CB 3068 C CG1 . VAL A 402 ? 0.3366 0.3406 0.3167 0.0214 -0.0095 0.0428 402 VAL A CG1 3069 C CG2 . VAL A 402 ? 0.3332 0.3467 0.3235 0.0148 -0.0136 0.0451 402 VAL A CG2 3070 N N . GLU A 403 ? 0.2900 0.2749 0.2661 0.0175 -0.0125 0.0359 403 GLU A N 3071 C CA . GLU A 403 ? 0.2962 0.2730 0.2661 0.0186 -0.0115 0.0339 403 GLU A CA 3072 C C . GLU A 403 ? 0.2940 0.2669 0.2578 0.0224 -0.0090 0.0333 403 GLU A C 3073 O O . GLU A 403 ? 0.3092 0.2756 0.2666 0.0237 -0.0078 0.0324 403 GLU A O 3074 C CB . GLU A 403 ? 0.3039 0.2757 0.2747 0.0154 -0.0137 0.0311 403 GLU A CB 3075 C CG . GLU A 403 ? 0.3023 0.2759 0.2777 0.0120 -0.0165 0.0311 403 GLU A CG 3076 C CD . GLU A 403 ? 0.3119 0.2817 0.2885 0.0097 -0.0186 0.0282 403 GLU A CD 3077 O OE1 . GLU A 403 ? 0.3018 0.2727 0.2810 0.0091 -0.0193 0.0271 403 GLU A OE1 3078 O OE2 . GLU A 403 ? 0.3257 0.2919 0.3005 0.0085 -0.0195 0.0269 403 GLU A OE2 3079 N N . GLY A 404 ? 0.2747 0.2505 0.2398 0.0242 -0.0084 0.0338 404 GLY A N 3080 C CA . GLY A 404 ? 0.2747 0.2464 0.2337 0.0281 -0.0063 0.0334 404 GLY A CA 3081 C C . GLY A 404 ? 0.2641 0.2281 0.2198 0.0267 -0.0069 0.0306 404 GLY A C 3082 O O . GLY A 404 ? 0.2511 0.2166 0.2114 0.0240 -0.0086 0.0296 404 GLY A O 3083 N N . ARG A 405 ? 0.2619 0.2175 0.2092 0.0284 -0.0056 0.0294 405 ARG A N 3084 C CA . ARG A 405 ? 0.2604 0.2086 0.2027 0.0278 -0.0057 0.0272 405 ARG A CA 3085 C C . ARG A 405 ? 0.2512 0.1988 0.1976 0.0229 -0.0079 0.0250 405 ARG A C 3086 O O . ARG A 405 ? 0.2478 0.1952 0.1951 0.0222 -0.0084 0.0241 405 ARG A O 3087 C CB . ARG A 405 ? 0.2709 0.2096 0.2031 0.0293 -0.0044 0.0263 405 ARG A CB 3088 C CG . ARG A 405 ? 0.2817 0.2116 0.2064 0.0292 -0.0042 0.0245 405 ARG A CG 3089 C CD . ARG A 405 ? 0.2930 0.2129 0.2066 0.0309 -0.0029 0.0239 405 ARG A CD 3090 N NE . ARG A 405 ? 0.2994 0.2101 0.2048 0.0304 -0.0028 0.0223 405 ARG A NE 3091 C CZ . ARG A 405 ? 0.3125 0.2127 0.2063 0.0322 -0.0018 0.0218 405 ARG A CZ 3092 N NH1 . ARG A 405 ? 0.3205 0.2182 0.2099 0.0347 -0.0007 0.0226 405 ARG A NH1 3093 N NH2 . ARG A 405 ? 0.3237 0.2153 0.2098 0.0313 -0.0020 0.0205 405 ARG A NH2 3094 N N A ILE A 406 ? 0.2482 0.1956 0.1967 0.0198 -0.0093 0.0241 406 ILE A N 3095 N N B ILE A 406 ? 0.2509 0.1984 0.1994 0.0198 -0.0093 0.0241 406 ILE A N 3096 C CA A ILE A 406 ? 0.2440 0.1913 0.1960 0.0157 -0.0113 0.0219 406 ILE A CA 3097 C CA B ILE A 406 ? 0.2488 0.1959 0.2006 0.0158 -0.0113 0.0219 406 ILE A CA 3098 C C A ILE A 406 ? 0.2336 0.1879 0.1938 0.0146 -0.0128 0.0223 406 ILE A C 3099 C C B ILE A 406 ? 0.2360 0.1903 0.1961 0.0146 -0.0128 0.0223 406 ILE A C 3100 O O A ILE A 406 ? 0.2251 0.1792 0.1867 0.0129 -0.0136 0.0207 406 ILE A O 3101 O O B ILE A 406 ? 0.2267 0.1809 0.1885 0.0129 -0.0137 0.0207 406 ILE A O 3102 C CB A ILE A 406 ? 0.2472 0.1932 0.1996 0.0131 -0.0126 0.0209 406 ILE A CB 3103 C CB B ILE A 406 ? 0.2558 0.2014 0.2077 0.0132 -0.0125 0.0208 406 ILE A CB 3104 C CG1 A ILE A 406 ? 0.2455 0.1918 0.2010 0.0094 -0.0146 0.0183 406 ILE A CG1 3105 C CG1 B ILE A 406 ? 0.2673 0.2056 0.2105 0.0142 -0.0110 0.0206 406 ILE A CG1 3106 C CG2 A ILE A 406 ? 0.2423 0.1940 0.2003 0.0131 -0.0135 0.0226 406 ILE A CG2 3107 C CG2 B ILE A 406 ? 0.2552 0.2009 0.2099 0.0095 -0.0145 0.0183 406 ILE A CG2 3108 C CD1 A ILE A 406 ? 0.2493 0.1901 0.1990 0.0082 -0.0140 0.0164 406 ILE A CD1 3109 C CD1 B ILE A 406 ? 0.2768 0.2077 0.2119 0.0148 -0.0099 0.0194 406 ILE A CD1 3110 N N . GLN A 407 ? 0.2293 0.1897 0.1944 0.0154 -0.0131 0.0244 407 GLN A N 3111 C CA . GLN A 407 ? 0.2244 0.1911 0.1966 0.0143 -0.0146 0.0251 407 GLN A CA 3112 C C . GLN A 407 ? 0.2181 0.1861 0.1900 0.0161 -0.0136 0.0256 407 GLN A C 3113 O O . GLN A 407 ? 0.2163 0.1866 0.1923 0.0144 -0.0150 0.0248 407 GLN A O 3114 C CB . GLN A 407 ? 0.2223 0.1948 0.1986 0.0144 -0.0151 0.0276 407 GLN A CB 3115 C CG . GLN A 407 ? 0.2242 0.2022 0.2073 0.0123 -0.0173 0.0282 407 GLN A CG 3116 C CD . GLN A 407 ? 0.2278 0.2114 0.2142 0.0118 -0.0179 0.0310 407 GLN A CD 3117 O OE1 . GLN A 407 ? 0.2413 0.2305 0.2309 0.0119 -0.0180 0.0329 407 GLN A OE1 3118 N NE2 . GLN A 407 ? 0.2275 0.2097 0.2129 0.0109 -0.0184 0.0312 407 GLN A NE2 3119 N N . ASP A 408 ? 0.2210 0.1876 0.1881 0.0197 -0.0114 0.0268 408 ASP A N 3120 C CA . ASP A 408 ? 0.2221 0.1889 0.1877 0.0219 -0.0105 0.0272 408 ASP A CA 3121 C C . ASP A 408 ? 0.2174 0.1787 0.1807 0.0198 -0.0112 0.0245 408 ASP A C 3122 O O . ASP A 408 ? 0.2084 0.1719 0.1745 0.0193 -0.0118 0.0243 408 ASP A O 3123 C CB . ASP A 408 ? 0.2403 0.2040 0.1989 0.0265 -0.0081 0.0283 408 ASP A CB 3124 C CG . ASP A 408 ? 0.2519 0.2220 0.2122 0.0294 -0.0070 0.0311 408 ASP A CG 3125 O OD1 . ASP A 408 ? 0.2530 0.2313 0.2204 0.0280 -0.0080 0.0327 408 ASP A OD1 3126 O OD2 . ASP A 408 ? 0.2654 0.2322 0.2193 0.0331 -0.0051 0.0316 408 ASP A OD2 3127 N N . LEU A 409 ? 0.2156 0.1703 0.1738 0.0184 -0.0111 0.0226 409 LEU A N 3128 C CA . LEU A 409 ? 0.2172 0.1670 0.1726 0.0159 -0.0116 0.0201 409 LEU A CA 3129 C C . LEU A 409 ? 0.2085 0.1629 0.1712 0.0123 -0.0137 0.0187 409 LEU A C 3130 O O . LEU A 409 ? 0.2036 0.1583 0.1674 0.0111 -0.0142 0.0177 409 LEU A O 3131 C CB . LEU A 409 ? 0.2227 0.1649 0.1708 0.0147 -0.0111 0.0186 409 LEU A CB 3132 C CG . LEU A 409 ? 0.2249 0.1612 0.1679 0.0119 -0.0113 0.0162 409 LEU A CG 3133 C CD1 . LEU A 409 ? 0.2266 0.1599 0.1655 0.0136 -0.0104 0.0165 409 LEU A CD1 3134 C CD2 . LEU A 409 ? 0.2347 0.1639 0.1702 0.0108 -0.0108 0.0153 409 LEU A CD2 3135 N N . GLU A 410 ? 0.2087 0.1665 0.1762 0.0108 -0.0151 0.0188 410 GLU A N 3136 C CA . GLU A 410 ? 0.2078 0.1697 0.1818 0.0080 -0.0173 0.0174 410 GLU A CA 3137 C C . GLU A 410 ? 0.2032 0.1698 0.1820 0.0084 -0.0179 0.0184 410 GLU A C 3138 O O . GLU A 410 ? 0.1904 0.1582 0.1717 0.0067 -0.0190 0.0168 410 GLU A O 3139 C CB . GLU A 410 ? 0.2139 0.1781 0.1915 0.0069 -0.0189 0.0176 410 GLU A CB 3140 C CG . GLU A 410 ? 0.2265 0.1864 0.2000 0.0058 -0.0188 0.0161 410 GLU A CG 3141 C CD . GLU A 410 ? 0.2406 0.2016 0.2158 0.0056 -0.0198 0.0169 410 GLU A CD 3142 O OE1 . GLU A 410 ? 0.2514 0.2154 0.2289 0.0070 -0.0196 0.0193 410 GLU A OE1 3143 O OE2 . GLU A 410 ? 0.2557 0.2148 0.2298 0.0040 -0.0206 0.0153 410 GLU A OE2 3144 N N . LYS A 411 ? 0.1984 0.1683 0.1785 0.0107 -0.0172 0.0211 411 LYS A N 3145 C CA . LYS A 411 ? 0.2060 0.1808 0.1904 0.0110 -0.0177 0.0224 411 LYS A CA 3146 C C . LYS A 411 ? 0.1949 0.1674 0.1763 0.0120 -0.0168 0.0217 411 LYS A C 3147 O O . LYS A 411 ? 0.1896 0.1646 0.1745 0.0108 -0.0178 0.0214 411 LYS A O 3148 C CB . LYS A 411 ? 0.2175 0.1972 0.2036 0.0132 -0.0171 0.0256 411 LYS A CB 3149 C CG . LYS A 411 ? 0.2326 0.2157 0.2227 0.0115 -0.0186 0.0267 411 LYS A CG 3150 C CD . LYS A 411 ? 0.2558 0.2445 0.2473 0.0132 -0.0178 0.0300 411 LYS A CD 3151 C CE . LYS A 411 ? 0.2761 0.2681 0.2714 0.0109 -0.0196 0.0312 411 LYS A CE 3152 N NZ . LYS A 411 ? 0.3074 0.3061 0.3042 0.0118 -0.0189 0.0346 411 LYS A NZ 3153 N N . TYR A 412 ? 0.1945 0.1620 0.1692 0.0141 -0.0149 0.0217 412 TYR A N 3154 C CA . TYR A 412 ? 0.1937 0.1579 0.1643 0.0152 -0.0140 0.0212 412 TYR A CA 3155 C C . TYR A 412 ? 0.1894 0.1506 0.1594 0.0118 -0.0149 0.0183 412 TYR A C 3156 O O . TYR A 412 ? 0.1901 0.1516 0.1607 0.0113 -0.0152 0.0178 412 TYR A O 3157 C CB . TYR A 412 ? 0.2003 0.1583 0.1625 0.0182 -0.0120 0.0216 412 TYR A CB 3158 C CG . TYR A 412 ? 0.2043 0.1582 0.1610 0.0202 -0.0110 0.0216 412 TYR A CG 3159 C CD1 . TYR A 412 ? 0.2051 0.1632 0.1636 0.0233 -0.0106 0.0236 412 TYR A CD1 3160 C CD2 . TYR A 412 ? 0.2129 0.1583 0.1621 0.0189 -0.0107 0.0196 412 TYR A CD2 3161 C CE1 . TYR A 412 ? 0.2101 0.1638 0.1628 0.0256 -0.0099 0.0236 412 TYR A CE1 3162 C CE2 . TYR A 412 ? 0.2157 0.1562 0.1587 0.0207 -0.0100 0.0196 412 TYR A CE2 3163 C CZ . TYR A 412 ? 0.2160 0.1605 0.1609 0.0242 -0.0096 0.0215 412 TYR A CZ 3164 O OH . TYR A 412 ? 0.2177 0.1570 0.1562 0.0264 -0.0091 0.0216 412 TYR A OH 3165 N N . VAL A 413 ? 0.1920 0.1507 0.1609 0.0095 -0.0154 0.0165 413 VAL A N 3166 C CA . VAL A 413 ? 0.1899 0.1473 0.1588 0.0061 -0.0163 0.0137 413 VAL A CA 3167 C C . VAL A 413 ? 0.1870 0.1502 0.1632 0.0046 -0.0180 0.0132 413 VAL A C 3168 O O . VAL A 413 ? 0.1873 0.1504 0.1635 0.0032 -0.0183 0.0119 413 VAL A O 3169 C CB . VAL A 413 ? 0.1925 0.1480 0.1599 0.0040 -0.0167 0.0122 413 VAL A CB 3170 C CG1 . VAL A 413 ? 0.1911 0.1483 0.1609 0.0005 -0.0181 0.0094 413 VAL A CG1 3171 C CG2 . VAL A 413 ? 0.1987 0.1466 0.1569 0.0046 -0.0151 0.0121 413 VAL A CG2 3172 N N . GLU A 414 ? 0.1872 0.1552 0.1692 0.0049 -0.0193 0.0143 414 GLU A N 3173 C CA . GLU A 414 ? 0.1887 0.1613 0.1770 0.0035 -0.0212 0.0139 414 GLU A CA 3174 C C . GLU A 414 ? 0.1866 0.1613 0.1762 0.0046 -0.0210 0.0153 414 GLU A C 3175 O O . GLU A 414 ? 0.1791 0.1550 0.1708 0.0031 -0.0219 0.0140 414 GLU A O 3176 C CB . GLU A 414 ? 0.1940 0.1698 0.1868 0.0033 -0.0228 0.0147 414 GLU A CB 3177 C CG . GLU A 414 ? 0.1972 0.1763 0.1953 0.0018 -0.0251 0.0139 414 GLU A CG 3178 C CD . GLU A 414 ? 0.2023 0.1809 0.2009 0.0000 -0.0262 0.0106 414 GLU A CD 3179 O OE1 . GLU A 414 ? 0.2191 0.1953 0.2143 -0.0006 -0.0252 0.0089 414 GLU A OE1 3180 O OE2 . GLU A 414 ? 0.2099 0.1908 0.2123 -0.0007 -0.0281 0.0096 414 GLU A OE2 3181 N N . ASP A 415 ? 0.1927 0.1681 0.1810 0.0072 -0.0198 0.0180 415 ASP A N 3182 C CA . ASP A 415 ? 0.2037 0.1816 0.1930 0.0085 -0.0195 0.0196 415 ASP A CA 3183 C C . ASP A 415 ? 0.1948 0.1686 0.1800 0.0081 -0.0188 0.0179 415 ASP A C 3184 O O . ASP A 415 ? 0.1849 0.1605 0.1723 0.0073 -0.0196 0.0177 415 ASP A O 3185 C CB . ASP A 415 ? 0.2234 0.2031 0.2113 0.0118 -0.0181 0.0225 415 ASP A CB 3186 C CG . ASP A 415 ? 0.2583 0.2428 0.2489 0.0130 -0.0183 0.0246 415 ASP A CG 3187 O OD1 . ASP A 415 ? 0.2798 0.2686 0.2758 0.0110 -0.0201 0.0250 415 ASP A OD1 3188 O OD2 . ASP A 415 ? 0.2922 0.2758 0.2792 0.0159 -0.0169 0.0257 415 ASP A OD2 3189 N N . THR A 416 ? 0.1892 0.1571 0.1679 0.0085 -0.0174 0.0168 416 THR A N 3190 C CA . THR A 416 ? 0.1904 0.1533 0.1637 0.0077 -0.0168 0.0153 416 THR A CA 3191 C C . THR A 416 ? 0.1818 0.1461 0.1581 0.0041 -0.0181 0.0128 416 THR A C 3192 O O . THR A 416 ? 0.1784 0.1425 0.1543 0.0035 -0.0182 0.0124 416 THR A O 3193 C CB . THR A 416 ? 0.1968 0.1525 0.1621 0.0079 -0.0154 0.0145 416 THR A CB 3194 O OG1 . THR A 416 ? 0.2053 0.1594 0.1671 0.0119 -0.0141 0.0168 416 THR A OG1 3195 C CG2 . THR A 416 ? 0.2005 0.1501 0.1592 0.0062 -0.0149 0.0128 416 THR A CG2 3196 N N . LYS A 417 ? 0.1743 0.1401 0.1533 0.0021 -0.0190 0.0112 417 LYS A N 3197 C CA . LYS A 417 ? 0.1727 0.1409 0.1549 -0.0008 -0.0203 0.0086 417 LYS A CA 3198 C C . LYS A 417 ? 0.1654 0.1380 0.1532 -0.0007 -0.0217 0.0091 417 LYS A C 3199 O O . LYS A 417 ? 0.1625 0.1355 0.1505 -0.0022 -0.0220 0.0077 417 LYS A O 3200 C CB . LYS A 417 ? 0.1705 0.1404 0.1552 -0.0020 -0.0213 0.0072 417 LYS A CB 3201 C CG . LYS A 417 ? 0.1731 0.1463 0.1614 -0.0044 -0.0228 0.0044 417 LYS A CG 3202 C CD . LYS A 417 ? 0.1761 0.1511 0.1665 -0.0051 -0.0239 0.0030 417 LYS A CD 3203 C CE . LYS A 417 ? 0.1790 0.1583 0.1737 -0.0064 -0.0256 0.0004 417 LYS A CE 3204 N NZ . LYS A 417 ? 0.1852 0.1668 0.1824 -0.0065 -0.0270 -0.0009 417 LYS A NZ 3205 N N . ILE A 418 ? 0.1613 0.1372 0.1533 0.0006 -0.0225 0.0112 418 ILE A N 3206 C CA . ILE A 418 ? 0.1575 0.1374 0.1545 0.0002 -0.0241 0.0118 418 ILE A CA 3207 C C . ILE A 418 ? 0.1569 0.1365 0.1524 0.0009 -0.0234 0.0128 418 ILE A C 3208 O O . ILE A 418 ? 0.1515 0.1325 0.1491 -0.0003 -0.0244 0.0119 418 ILE A O 3209 C CB . ILE A 418 ? 0.1581 0.1413 0.1591 0.0011 -0.0252 0.0142 418 ILE A CB 3210 C CG1 . ILE A 418 ? 0.1567 0.1399 0.1593 0.0002 -0.0264 0.0128 418 ILE A CG1 3211 C CG2 . ILE A 418 ? 0.1547 0.1414 0.1596 0.0006 -0.0268 0.0153 418 ILE A CG2 3212 C CD1 . ILE A 418 ? 0.1629 0.1482 0.1679 0.0009 -0.0273 0.0152 418 ILE A CD1 3213 N N . ASP A 419 ? 0.1613 0.1388 0.1529 0.0032 -0.0218 0.0147 419 ASP A N 3214 C CA . ASP A 419 ? 0.1654 0.1424 0.1550 0.0042 -0.0213 0.0156 419 ASP A CA 3215 C C . ASP A 419 ? 0.1627 0.1358 0.1487 0.0022 -0.0210 0.0131 419 ASP A C 3216 O O . ASP A 419 ? 0.1640 0.1378 0.1505 0.0017 -0.0214 0.0131 419 ASP A O 3217 C CB . ASP A 419 ? 0.1749 0.1500 0.1602 0.0076 -0.0196 0.0179 419 ASP A CB 3218 C CG . ASP A 419 ? 0.1846 0.1654 0.1739 0.0097 -0.0198 0.0209 419 ASP A CG 3219 O OD1 . ASP A 419 ? 0.1944 0.1800 0.1896 0.0081 -0.0215 0.0215 419 ASP A OD1 3220 O OD2 . ASP A 419 ? 0.1987 0.1789 0.1848 0.0130 -0.0184 0.0227 419 ASP A OD2 3221 N N . LEU A 420 ? 0.1617 0.1309 0.1437 0.0008 -0.0202 0.0111 420 LEU A N 3222 C CA . LEU A 420 ? 0.1636 0.1295 0.1417 -0.0016 -0.0199 0.0088 420 LEU A CA 3223 C C . LEU A 420 ? 0.1589 0.1290 0.1420 -0.0041 -0.0213 0.0067 420 LEU A C 3224 O O . LEU A 420 ? 0.1618 0.1315 0.1439 -0.0054 -0.0215 0.0058 420 LEU A O 3225 C CB . LEU A 420 ? 0.1657 0.1266 0.1376 -0.0028 -0.0188 0.0073 420 LEU A CB 3226 C CG . LEU A 420 ? 0.1711 0.1255 0.1353 -0.0004 -0.0173 0.0090 420 LEU A CG 3227 C CD1 . LEU A 420 ? 0.1750 0.1252 0.1344 -0.0012 -0.0165 0.0082 420 LEU A CD1 3228 C CD2 . LEU A 420 ? 0.1768 0.1265 0.1351 -0.0009 -0.0168 0.0087 420 LEU A CD2 3229 N N . TRP A 421 ? 0.1567 0.1305 0.1448 -0.0045 -0.0225 0.0059 421 TRP A N 3230 C CA . TRP A 421 ? 0.1541 0.1317 0.1469 -0.0062 -0.0241 0.0041 421 TRP A CA 3231 C C . TRP A 421 ? 0.1536 0.1335 0.1496 -0.0055 -0.0252 0.0054 421 TRP A C 3232 O O . TRP A 421 ? 0.1520 0.1331 0.1491 -0.0070 -0.0259 0.0039 421 TRP A O 3233 C CB . TRP A 421 ? 0.1525 0.1328 0.1490 -0.0064 -0.0254 0.0029 421 TRP A CB 3234 C CG . TRP A 421 ? 0.1538 0.1334 0.1477 -0.0081 -0.0247 0.0004 421 TRP A CG 3235 C CD1 . TRP A 421 ? 0.1581 0.1360 0.1496 -0.0081 -0.0240 0.0003 421 TRP A CD1 3236 C CD2 . TRP A 421 ? 0.1561 0.1369 0.1488 -0.0106 -0.0245 -0.0024 421 TRP A CD2 3237 N NE1 . TRP A 421 ? 0.1614 0.1396 0.1507 -0.0105 -0.0236 -0.0022 421 TRP A NE1 3238 C CE2 . TRP A 421 ? 0.1610 0.1411 0.1508 -0.0122 -0.0238 -0.0039 421 TRP A CE2 3239 C CE3 . TRP A 421 ? 0.1557 0.1381 0.1492 -0.0118 -0.0249 -0.0037 421 TRP A CE3 3240 C CZ2 . TRP A 421 ? 0.1623 0.1443 0.1505 -0.0150 -0.0235 -0.0067 421 TRP A CZ2 3241 C CZ3 . TRP A 421 ? 0.1608 0.1448 0.1526 -0.0144 -0.0245 -0.0066 421 TRP A CZ3 3242 C CH2 . TRP A 421 ? 0.1622 0.1464 0.1515 -0.0160 -0.0238 -0.0080 421 TRP A CH2 3243 N N . SER A 422 ? 0.1537 0.1346 0.1513 -0.0035 -0.0254 0.0084 422 SER A N 3244 C CA . SER A 422 ? 0.1546 0.1380 0.1551 -0.0032 -0.0265 0.0101 422 SER A CA 3245 C C . SER A 422 ? 0.1570 0.1385 0.1543 -0.0034 -0.0256 0.0100 422 SER A C 3246 O O . SER A 422 ? 0.1514 0.1343 0.1505 -0.0045 -0.0267 0.0096 422 SER A O 3247 C CB . SER A 422 ? 0.1553 0.1410 0.1576 -0.0012 -0.0266 0.0135 422 SER A CB 3248 O OG . SER A 422 ? 0.1578 0.1450 0.1630 -0.0014 -0.0276 0.0136 422 SER A OG 3249 N N . TYR A 423 ? 0.1634 0.1409 0.1552 -0.0025 -0.0239 0.0103 423 TYR A N 3250 C CA . TYR A 423 ? 0.1702 0.1445 0.1575 -0.0028 -0.0231 0.0100 423 TYR A CA 3251 C C . TYR A 423 ? 0.1670 0.1407 0.1537 -0.0060 -0.0234 0.0069 423 TYR A C 3252 O O . TYR A 423 ? 0.1648 0.1389 0.1517 -0.0069 -0.0240 0.0065 423 TYR A O 3253 C CB . TYR A 423 ? 0.1793 0.1480 0.1594 -0.0013 -0.0213 0.0107 423 TYR A CB 3254 C CG . TYR A 423 ? 0.1903 0.1545 0.1648 -0.0018 -0.0208 0.0103 423 TYR A CG 3255 C CD1 . TYR A 423 ? 0.1969 0.1615 0.1709 0.0004 -0.0209 0.0124 423 TYR A CD1 3256 C CD2 . TYR A 423 ? 0.1976 0.1579 0.1674 -0.0048 -0.0202 0.0077 423 TYR A CD2 3257 C CE1 . TYR A 423 ? 0.2068 0.1671 0.1755 0.0000 -0.0206 0.0121 423 TYR A CE1 3258 C CE2 . TYR A 423 ? 0.2068 0.1626 0.1710 -0.0056 -0.0199 0.0074 423 TYR A CE2 3259 C CZ . TYR A 423 ? 0.2152 0.1707 0.1787 -0.0030 -0.0201 0.0096 423 TYR A CZ 3260 O OH . TYR A 423 ? 0.2362 0.1870 0.1940 -0.0037 -0.0200 0.0094 423 TYR A OH 3261 N N . ASN A 424 ? 0.1666 0.1400 0.1527 -0.0076 -0.0232 0.0046 424 ASN A N 3262 C CA . ASN A 424 ? 0.1683 0.1423 0.1538 -0.0106 -0.0233 0.0016 424 ASN A CA 3263 C C . ASN A 424 ? 0.1648 0.1433 0.1559 -0.0111 -0.0250 0.0007 424 ASN A C 3264 O O . ASN A 424 ? 0.1658 0.1445 0.1561 -0.0128 -0.0251 -0.0006 424 ASN A O 3265 C CB . ASN A 424 ? 0.1689 0.1437 0.1541 -0.0121 -0.0230 -0.0005 424 ASN A CB 3266 C CG . ASN A 424 ? 0.1752 0.1449 0.1536 -0.0127 -0.0214 -0.0004 424 ASN A CG 3267 O OD1 . ASN A 424 ? 0.1813 0.1462 0.1541 -0.0126 -0.0205 0.0005 424 ASN A OD1 3268 N ND2 . ASN A 424 ? 0.1728 0.1431 0.1511 -0.0135 -0.0213 -0.0015 424 ASN A ND2 3269 N N . ALA A 425 ? 0.1624 0.1438 0.1585 -0.0097 -0.0263 0.0017 425 ALA A N 3270 C CA . ALA A 425 ? 0.1658 0.1503 0.1664 -0.0100 -0.0282 0.0011 425 ALA A CA 3271 C C . ALA A 425 ? 0.1717 0.1559 0.1722 -0.0100 -0.0286 0.0026 425 ALA A C 3272 O O . ALA A 425 ? 0.1770 0.1621 0.1782 -0.0113 -0.0294 0.0011 425 ALA A O 3273 C CB . ALA A 425 ? 0.1598 0.1462 0.1645 -0.0087 -0.0298 0.0022 425 ALA A CB 3274 N N . GLU A 426 ? 0.1815 0.1647 0.1809 -0.0084 -0.0281 0.0057 426 GLU A N 3275 C CA . GLU A 426 ? 0.1935 0.1768 0.1926 -0.0081 -0.0285 0.0074 426 GLU A CA 3276 C C . GLU A 426 ? 0.1919 0.1724 0.1868 -0.0096 -0.0276 0.0058 426 GLU A C 3277 O O . GLU A 426 ? 0.1939 0.1753 0.1897 -0.0107 -0.0285 0.0053 426 GLU A O 3278 C CB . GLU A 426 ? 0.2085 0.1919 0.2068 -0.0056 -0.0278 0.0108 426 GLU A CB 3279 C CG . GLU A 426 ? 0.2279 0.2131 0.2273 -0.0051 -0.0286 0.0132 426 GLU A CG 3280 C CD . GLU A 426 ? 0.2437 0.2331 0.2484 -0.0057 -0.0308 0.0145 426 GLU A CD 3281 O OE1 . GLU A 426 ? 0.2500 0.2412 0.2574 -0.0055 -0.0314 0.0150 426 GLU A OE1 3282 O OE2 . GLU A 426 ? 0.2809 0.2715 0.2867 -0.0067 -0.0320 0.0150 426 GLU A OE2 3283 N N . LEU A 427 ? 0.1953 0.1723 0.1852 -0.0100 -0.0259 0.0049 427 LEU A N 3284 C CA . LEU A 427 ? 0.2009 0.1747 0.1859 -0.0119 -0.0251 0.0034 427 LEU A CA 3285 C C . LEU A 427 ? 0.2003 0.1765 0.1870 -0.0146 -0.0257 0.0002 427 LEU A C 3286 O O . LEU A 427 ? 0.2017 0.1776 0.1872 -0.0161 -0.0259 -0.0006 427 LEU A O 3287 C CB . LEU A 427 ? 0.2079 0.1767 0.1863 -0.0121 -0.0234 0.0031 427 LEU A CB 3288 C CG . LEU A 427 ? 0.2163 0.1806 0.1881 -0.0144 -0.0226 0.0018 427 LEU A CG 3289 C CD1 . LEU A 427 ? 0.2218 0.1843 0.1919 -0.0132 -0.0230 0.0037 427 LEU A CD1 3290 C CD2 . LEU A 427 ? 0.2232 0.1819 0.1880 -0.0148 -0.0212 0.0017 427 LEU A CD2 3291 N N . LEU A 428 ? 0.1986 0.1775 0.1880 -0.0151 -0.0259 -0.0016 428 LEU A N 3292 C CA . LEU A 428 ? 0.2082 0.1901 0.1991 -0.0171 -0.0263 -0.0049 428 LEU A CA 3293 C C . LEU A 428 ? 0.2049 0.1891 0.1993 -0.0170 -0.0280 -0.0051 428 LEU A C 3294 O O . LEU A 428 ? 0.2027 0.1875 0.1960 -0.0188 -0.0279 -0.0070 428 LEU A O 3295 C CB . LEU A 428 ? 0.2136 0.1985 0.2073 -0.0168 -0.0266 -0.0065 428 LEU A CB 3296 C CG . LEU A 428 ? 0.2234 0.2125 0.2188 -0.0184 -0.0270 -0.0101 428 LEU A CG 3297 C CD1 . LEU A 428 ? 0.2448 0.2334 0.2354 -0.0214 -0.0255 -0.0119 428 LEU A CD1 3298 C CD2 . LEU A 428 ? 0.2322 0.2242 0.2302 -0.0176 -0.0274 -0.0115 428 LEU A CD2 3299 N N . VAL A 429 ? 0.2092 0.1941 0.2072 -0.0151 -0.0294 -0.0030 429 VAL A N 3300 C CA . VAL A 429 ? 0.2172 0.2037 0.2181 -0.0152 -0.0312 -0.0031 429 VAL A CA 3301 C C . VAL A 429 ? 0.2191 0.2038 0.2176 -0.0160 -0.0310 -0.0019 429 VAL A C 3302 O O . VAL A 429 ? 0.2241 0.2094 0.2228 -0.0172 -0.0317 -0.0034 429 VAL A O 3303 C CB . VAL A 429 ? 0.2219 0.2094 0.2267 -0.0136 -0.0330 -0.0011 429 VAL A CB 3304 C CG1 . VAL A 429 ? 0.2334 0.2215 0.2402 -0.0140 -0.0351 -0.0009 429 VAL A CG1 3305 C CG2 . VAL A 429 ? 0.2230 0.2120 0.2297 -0.0129 -0.0334 -0.0028 429 VAL A CG2 3306 N N . ALA A 430 ? 0.2154 0.1979 0.2115 -0.0151 -0.0301 0.0006 430 ALA A N 3307 C CA . ALA A 430 ? 0.2243 0.2048 0.2176 -0.0156 -0.0299 0.0018 430 ALA A CA 3308 C C . ALA A 430 ? 0.2235 0.2022 0.2126 -0.0180 -0.0289 -0.0008 430 ALA A C 3309 O O . ALA A 430 ? 0.2241 0.2026 0.2125 -0.0193 -0.0295 -0.0013 430 ALA A O 3310 C CB . ALA A 430 ? 0.2203 0.1987 0.2110 -0.0135 -0.0290 0.0048 430 ALA A CB 3311 N N . LEU A 431 ? 0.2216 0.1990 0.2076 -0.0190 -0.0274 -0.0024 431 LEU A N 3312 C CA . LEU A 431 ? 0.2304 0.2065 0.2121 -0.0219 -0.0263 -0.0049 431 LEU A CA 3313 C C . LEU A 431 ? 0.2285 0.2089 0.2133 -0.0234 -0.0271 -0.0079 431 LEU A C 3314 O O . LEU A 431 ? 0.2398 0.2199 0.2224 -0.0254 -0.0269 -0.0092 431 LEU A O 3315 C CB . LEU A 431 ? 0.2339 0.2084 0.2120 -0.0230 -0.0248 -0.0060 431 LEU A CB 3316 C CG . LEU A 431 ? 0.2458 0.2144 0.2181 -0.0220 -0.0238 -0.0037 431 LEU A CG 3317 C CD1 . LEU A 431 ? 0.2492 0.2162 0.2180 -0.0234 -0.0226 -0.0049 431 LEU A CD1 3318 C CD2 . LEU A 431 ? 0.2563 0.2203 0.2228 -0.0233 -0.0235 -0.0031 431 LEU A CD2 3319 N N . GLU A 432 ? 0.2304 0.2146 0.2198 -0.0223 -0.0279 -0.0091 432 GLU A N 3320 C CA . GLU A 432 ? 0.2399 0.2279 0.2319 -0.0230 -0.0287 -0.0120 432 GLU A CA 3321 C C . GLU A 432 ? 0.2306 0.2182 0.2240 -0.0227 -0.0302 -0.0113 432 GLU A C 3322 O O . GLU A 432 ? 0.2321 0.2211 0.2246 -0.0241 -0.0303 -0.0136 432 GLU A O 3323 C CB . GLU A 432 ? 0.2566 0.2479 0.2528 -0.0212 -0.0296 -0.0131 432 GLU A CB 3324 C CG . GLU A 432 ? 0.2830 0.2759 0.2780 -0.0220 -0.0282 -0.0146 432 GLU A CG 3325 C CD . GLU A 432 ? 0.3285 0.3257 0.3226 -0.0241 -0.0274 -0.0183 432 GLU A CD 3326 O OE1 . GLU A 432 ? 0.3375 0.3359 0.3310 -0.0252 -0.0275 -0.0197 432 GLU A OE1 3327 O OE2 . GLU A 432 ? 0.3766 0.3763 0.3705 -0.0248 -0.0266 -0.0196 432 GLU A OE2 3328 N N . ASN A 433 ? 0.2208 0.2068 0.2160 -0.0210 -0.0314 -0.0083 433 ASN A N 3329 C CA . ASN A 433 ? 0.2197 0.2052 0.2159 -0.0210 -0.0331 -0.0073 433 ASN A CA 3330 C C . ASN A 433 ? 0.2294 0.2127 0.2217 -0.0227 -0.0324 -0.0070 433 ASN A C 3331 O O . ASN A 433 ? 0.2265 0.2101 0.2186 -0.0238 -0.0331 -0.0083 433 ASN A O 3332 C CB . ASN A 433 ? 0.2132 0.1983 0.2121 -0.0193 -0.0345 -0.0039 433 ASN A CB 3333 C CG . ASN A 433 ? 0.2060 0.1927 0.2085 -0.0180 -0.0359 -0.0043 433 ASN A CG 3334 O OD1 . ASN A 433 ? 0.2061 0.1941 0.2094 -0.0179 -0.0362 -0.0073 433 ASN A OD1 3335 N ND2 . ASN A 433 ? 0.2024 0.1890 0.2070 -0.0169 -0.0370 -0.0013 433 ASN A ND2 3336 N N . GLN A 434 ? 0.2359 0.2165 0.2246 -0.0230 -0.0309 -0.0056 434 GLN A N 3337 C CA . GLN A 434 ? 0.2550 0.2328 0.2390 -0.0247 -0.0302 -0.0055 434 GLN A CA 3338 C C . GLN A 434 ? 0.2500 0.2291 0.2319 -0.0275 -0.0293 -0.0091 434 GLN A C 3339 O O . GLN A 434 ? 0.2488 0.2272 0.2288 -0.0290 -0.0296 -0.0098 434 GLN A O 3340 C CB . GLN A 434 ? 0.2795 0.2532 0.2586 -0.0244 -0.0288 -0.0037 434 GLN A CB 3341 C CG . GLN A 434 ? 0.3053 0.2750 0.2789 -0.0258 -0.0284 -0.0032 434 GLN A CG 3342 C CD . GLN A 434 ? 0.3358 0.3057 0.3113 -0.0246 -0.0300 -0.0009 434 GLN A CD 3343 O OE1 . GLN A 434 ? 0.3550 0.3254 0.3327 -0.0220 -0.0307 0.0019 434 GLN A OE1 3344 N NE2 . GLN A 434 ? 0.3614 0.3316 0.3365 -0.0266 -0.0307 -0.0022 434 GLN A NE2 3345 N N . HIS A 435 ? 0.2547 0.2361 0.2369 -0.0281 -0.0284 -0.0113 435 HIS A N 3346 C CA . HIS A 435 ? 0.2655 0.2498 0.2461 -0.0307 -0.0274 -0.0148 435 HIS A CA 3347 C C . HIS A 435 ? 0.2603 0.2480 0.2442 -0.0302 -0.0287 -0.0168 435 HIS A C 3348 O O . HIS A 435 ? 0.2656 0.2543 0.2473 -0.0323 -0.0284 -0.0188 435 HIS A O 3349 C CB . HIS A 435 ? 0.2804 0.2674 0.2611 -0.0312 -0.0263 -0.0165 435 HIS A CB 3350 C CG . HIS A 435 ? 0.2975 0.2889 0.2768 -0.0340 -0.0252 -0.0201 435 HIS A CG 3351 N ND1 . HIS A 435 ? 0.3099 0.3073 0.2933 -0.0331 -0.0257 -0.0229 435 HIS A ND1 3352 C CD2 . HIS A 435 ? 0.3175 0.3083 0.2914 -0.0378 -0.0237 -0.0213 435 HIS A CD2 3353 C CE1 . HIS A 435 ? 0.3219 0.3233 0.3030 -0.0360 -0.0245 -0.0257 435 HIS A CE1 3354 N NE2 . HIS A 435 ? 0.3253 0.3227 0.3005 -0.0392 -0.0232 -0.0247 435 HIS A NE2 3355 N N . THR A 436 ? 0.2477 0.2366 0.2362 -0.0276 -0.0304 -0.0162 436 THR A N 3356 C CA . THR A 436 ? 0.2483 0.2392 0.2392 -0.0267 -0.0320 -0.0180 436 THR A CA 3357 C C . THR A 436 ? 0.2563 0.2444 0.2455 -0.0277 -0.0329 -0.0167 436 THR A C 3358 O O . THR A 436 ? 0.2592 0.2485 0.2475 -0.0286 -0.0331 -0.0191 436 THR A O 3359 C CB . THR A 436 ? 0.2476 0.2390 0.2427 -0.0239 -0.0338 -0.0173 436 THR A CB 3360 O OG1 . THR A 436 ? 0.2385 0.2331 0.2351 -0.0231 -0.0330 -0.0191 436 THR A OG1 3361 C CG2 . THR A 436 ? 0.2436 0.2352 0.2400 -0.0229 -0.0359 -0.0188 436 THR A CG2 3362 N N . ILE A 437 ? 0.2506 0.2353 0.2394 -0.0273 -0.0334 -0.0132 437 ILE A N 3363 C CA . ILE A 437 ? 0.2685 0.2507 0.2554 -0.0283 -0.0343 -0.0118 437 ILE A CA 3364 C C . ILE A 437 ? 0.2793 0.2607 0.2615 -0.0310 -0.0327 -0.0135 437 ILE A C 3365 O O . ILE A 437 ? 0.2617 0.2431 0.2426 -0.0323 -0.0332 -0.0148 437 ILE A O 3366 C CB . ILE A 437 ? 0.2741 0.2538 0.2611 -0.0272 -0.0348 -0.0076 437 ILE A CB 3367 C CG1 . ILE A 437 ? 0.2809 0.2618 0.2724 -0.0252 -0.0366 -0.0057 437 ILE A CG1 3368 C CG2 . ILE A 437 ? 0.2874 0.2648 0.2721 -0.0284 -0.0356 -0.0061 437 ILE A CG2 3369 C CD1 . ILE A 437 ? 0.2940 0.2755 0.2875 -0.0251 -0.0387 -0.0068 437 ILE A CD1 3370 N N . ASP A 438 ? 0.2731 0.2536 0.2523 -0.0321 -0.0308 -0.0135 438 ASP A N 3371 C CA . ASP A 438 ? 0.2896 0.2690 0.2635 -0.0352 -0.0293 -0.0151 438 ASP A CA 3372 C C . ASP A 438 ? 0.2817 0.2656 0.2558 -0.0369 -0.0288 -0.0190 438 ASP A C 3373 O O . ASP A 438 ? 0.3069 0.2903 0.2781 -0.0390 -0.0286 -0.0201 438 ASP A O 3374 C CB . ASP A 438 ? 0.3034 0.2806 0.2734 -0.0363 -0.0276 -0.0145 438 ASP A CB 3375 C CG . ASP A 438 ? 0.3213 0.2932 0.2890 -0.0347 -0.0279 -0.0109 438 ASP A CG 3376 O OD1 . ASP A 438 ? 0.3487 0.3193 0.3179 -0.0332 -0.0293 -0.0087 438 ASP A OD1 3377 O OD2 . ASP A 438 ? 0.3476 0.3168 0.3118 -0.0350 -0.0267 -0.0102 438 ASP A OD2 3378 N N . LEU A 439 ? 0.2734 0.2620 0.2509 -0.0358 -0.0286 -0.0212 439 LEU A N 3379 C CA . LEU A 439 ? 0.2785 0.2726 0.2564 -0.0369 -0.0279 -0.0250 439 LEU A CA 3380 C C . LEU A 439 ? 0.2817 0.2764 0.2612 -0.0356 -0.0295 -0.0262 439 LEU A C 3381 O O . LEU A 439 ? 0.2787 0.2761 0.2565 -0.0372 -0.0290 -0.0288 439 LEU A O 3382 C CB . LEU A 439 ? 0.2872 0.2864 0.2682 -0.0356 -0.0275 -0.0270 439 LEU A CB 3383 C CG . LEU A 439 ? 0.2878 0.2891 0.2740 -0.0317 -0.0291 -0.0275 439 LEU A CG 3384 C CD1 . LEU A 439 ? 0.2893 0.2946 0.2770 -0.0304 -0.0300 -0.0308 439 LEU A CD1 3385 C CD2 . LEU A 439 ? 0.2906 0.2949 0.2787 -0.0309 -0.0284 -0.0281 439 LEU A CD2 3386 N N . THR A 440 ? 0.2701 0.2621 0.2524 -0.0331 -0.0316 -0.0241 440 THR A N 3387 C CA . THR A 440 ? 0.2814 0.2728 0.2645 -0.0320 -0.0334 -0.0249 440 THR A CA 3388 C C . THR A 440 ? 0.2948 0.2826 0.2744 -0.0342 -0.0336 -0.0236 440 THR A C 3389 O O . THR A 440 ? 0.3204 0.3087 0.2985 -0.0350 -0.0340 -0.0256 440 THR A O 3390 C CB . THR A 440 ? 0.2710 0.2606 0.2577 -0.0291 -0.0358 -0.0233 440 THR A CB 3391 O OG1 . THR A 440 ? 0.2625 0.2491 0.2499 -0.0290 -0.0361 -0.0194 440 THR A OG1 3392 C CG2 . THR A 440 ? 0.2718 0.2650 0.2614 -0.0267 -0.0360 -0.0255 440 THR A CG2 3393 N N . ASP A 441 ? 0.2962 0.2802 0.2741 -0.0351 -0.0334 -0.0203 441 ASP A N 3394 C CA . ASP A 441 ? 0.3138 0.2943 0.2878 -0.0372 -0.0334 -0.0190 441 ASP A CA 3395 C C . ASP A 441 ? 0.3339 0.3161 0.3038 -0.0403 -0.0315 -0.0219 441 ASP A C 3396 O O . ASP A 441 ? 0.3303 0.3115 0.2976 -0.0419 -0.0318 -0.0227 441 ASP A O 3397 C CB . ASP A 441 ? 0.3178 0.2944 0.2900 -0.0373 -0.0332 -0.0154 441 ASP A CB 3398 C CG . ASP A 441 ? 0.3269 0.3021 0.3024 -0.0349 -0.0352 -0.0119 441 ASP A CG 3399 O OD1 . ASP A 441 ? 0.3264 0.3026 0.3050 -0.0338 -0.0370 -0.0120 441 ASP A OD1 3400 O OD2 . ASP A 441 ? 0.3425 0.3155 0.3171 -0.0342 -0.0350 -0.0090 441 ASP A OD2 3401 N N . SER A 442 ? 0.3347 0.3195 0.3038 -0.0413 -0.0296 -0.0233 442 SER A N 3402 C CA . SER A 442 ? 0.3482 0.3352 0.3131 -0.0448 -0.0278 -0.0258 442 SER A CA 3403 C C . SER A 442 ? 0.3446 0.3367 0.3105 -0.0450 -0.0277 -0.0295 442 SER A C 3404 O O . SER A 442 ? 0.3619 0.3541 0.3239 -0.0478 -0.0270 -0.0307 442 SER A O 3405 C CB . SER A 442 ? 0.3551 0.3442 0.3189 -0.0462 -0.0260 -0.0265 442 SER A CB 3406 O OG . SER A 442 ? 0.3733 0.3656 0.3331 -0.0500 -0.0242 -0.0291 442 SER A OG 3407 N N . GLU A 443 ? 0.3348 0.3309 0.3053 -0.0419 -0.0285 -0.0312 443 GLU A N 3408 C CA . GLU A 443 ? 0.3503 0.3511 0.3215 -0.0412 -0.0287 -0.0347 443 GLU A CA 3409 C C . GLU A 443 ? 0.3473 0.3441 0.3165 -0.0416 -0.0300 -0.0342 443 GLU A C 3410 O O . GLU A 443 ? 0.3725 0.3720 0.3394 -0.0429 -0.0293 -0.0369 443 GLU A O 3411 C CB . GLU A 443 ? 0.3522 0.3567 0.3281 -0.0372 -0.0297 -0.0365 443 GLU A CB 3412 C CG . GLU A 443 ? 0.3688 0.3790 0.3467 -0.0368 -0.0283 -0.0380 443 GLU A CG 3413 C CD . GLU A 443 ? 0.3802 0.3971 0.3558 -0.0400 -0.0259 -0.0409 443 GLU A CD 3414 O OE1 . GLU A 443 ? 0.3954 0.4153 0.3695 -0.0405 -0.0256 -0.0435 443 GLU A OE1 3415 O OE2 . GLU A 443 ? 0.3956 0.4148 0.3705 -0.0421 -0.0244 -0.0407 443 GLU A OE2 3416 N N . MET A 444 ? 0.3471 0.3380 0.3168 -0.0406 -0.0319 -0.0309 444 MET A N 3417 C CA . MET A 444 ? 0.3397 0.3266 0.3073 -0.0412 -0.0333 -0.0300 444 MET A CA 3418 C C . MET A 444 ? 0.3621 0.3474 0.3246 -0.0451 -0.0319 -0.0298 444 MET A C 3419 O O . MET A 444 ? 0.3521 0.3377 0.3119 -0.0466 -0.0319 -0.0315 444 MET A O 3420 C CB . MET A 444 ? 0.3315 0.3133 0.3008 -0.0397 -0.0356 -0.0260 444 MET A CB 3421 C CG . MET A 444 ? 0.3306 0.3084 0.2979 -0.0405 -0.0374 -0.0248 444 MET A CG 3422 S SD . MET A 444 ? 0.3238 0.3017 0.2920 -0.0383 -0.0395 -0.0274 444 MET A SD 3423 C CE . MET A 444 ? 0.3444 0.3263 0.3092 -0.0398 -0.0375 -0.0321 444 MET A CE 3424 N N . ASN A 445 ? 0.3680 0.3511 0.3286 -0.0467 -0.0309 -0.0276 445 ASN A N 3425 C CA . ASN A 445 ? 0.3943 0.3745 0.3491 -0.0504 -0.0298 -0.0271 445 ASN A CA 3426 C C . ASN A 445 ? 0.3790 0.3641 0.3309 -0.0534 -0.0277 -0.0308 445 ASN A C 3427 O O . ASN A 445 ? 0.3828 0.3666 0.3304 -0.0562 -0.0274 -0.0314 445 ASN A O 3428 C CB . ASN A 445 ? 0.4233 0.3995 0.3758 -0.0511 -0.0292 -0.0242 445 ASN A CB 3429 C CG . ASN A 445 ? 0.4611 0.4327 0.4154 -0.0485 -0.0311 -0.0203 445 ASN A CG 3430 O OD1 . ASN A 445 ? 0.4728 0.4425 0.4277 -0.0479 -0.0328 -0.0191 445 ASN A OD1 3431 N ND2 . ASN A 445 ? 0.4956 0.4657 0.4506 -0.0471 -0.0307 -0.0182 445 ASN A ND2 3432 N N . LYS A 446 ? 0.3812 0.3725 0.3357 -0.0528 -0.0265 -0.0331 446 LYS A N 3433 C CA . LYS A 446 ? 0.4088 0.4065 0.3611 -0.0556 -0.0245 -0.0367 446 LYS A CA 3434 C C . LYS A 446 ? 0.4093 0.4101 0.3619 -0.0549 -0.0249 -0.0394 446 LYS A C 3435 O O . LYS A 446 ? 0.4048 0.4075 0.3533 -0.0583 -0.0237 -0.0411 446 LYS A O 3436 C CB . LYS A 446 ? 0.4338 0.4384 0.3894 -0.0547 -0.0233 -0.0386 446 LYS A CB 3437 C CG . LYS A 446 ? 0.4577 0.4598 0.4109 -0.0570 -0.0222 -0.0366 446 LYS A CG 3438 C CD . LYS A 446 ? 0.4889 0.4951 0.4467 -0.0546 -0.0220 -0.0371 446 LYS A CD 3439 C CE . LYS A 446 ? 0.4996 0.5160 0.4600 -0.0545 -0.0208 -0.0410 446 LYS A CE 3440 N NZ . LYS A 446 ? 0.5261 0.5460 0.4905 -0.0523 -0.0207 -0.0412 446 LYS A NZ 3441 N N . LEU A 447 ? 0.3853 0.3859 0.3420 -0.0507 -0.0267 -0.0397 447 LEU A N 3442 C CA . LEU A 447 ? 0.3840 0.3864 0.3406 -0.0494 -0.0275 -0.0422 447 LEU A CA 3443 C C . LEU A 447 ? 0.3735 0.3702 0.3255 -0.0519 -0.0281 -0.0409 447 LEU A C 3444 O O . LEU A 447 ? 0.3811 0.3802 0.3302 -0.0535 -0.0274 -0.0433 447 LEU A O 3445 C CB . LEU A 447 ? 0.3924 0.3935 0.3531 -0.0445 -0.0298 -0.0422 447 LEU A CB 3446 C CG . LEU A 447 ? 0.4095 0.4114 0.3697 -0.0422 -0.0309 -0.0450 447 LEU A CG 3447 C CD1 . LEU A 447 ? 0.4075 0.4184 0.3673 -0.0421 -0.0289 -0.0495 447 LEU A CD1 3448 C CD2 . LEU A 447 ? 0.4084 0.4072 0.3718 -0.0377 -0.0335 -0.0443 447 LEU A CD2 3449 N N . PHE A 448 ? 0.3598 0.3494 0.3110 -0.0524 -0.0294 -0.0370 448 PHE A N 3450 C CA . PHE A 448 ? 0.3664 0.3506 0.3133 -0.0548 -0.0301 -0.0353 448 PHE A CA 3451 C C . PHE A 448 ? 0.3826 0.3677 0.3239 -0.0594 -0.0280 -0.0363 448 PHE A C 3452 O O . PHE A 448 ? 0.3622 0.3466 0.2998 -0.0616 -0.0278 -0.0375 448 PHE A O 3453 C CB . PHE A 448 ? 0.3638 0.3413 0.3112 -0.0540 -0.0319 -0.0309 448 PHE A CB 3454 C CG . PHE A 448 ? 0.3649 0.3368 0.3082 -0.0559 -0.0330 -0.0289 448 PHE A CG 3455 C CD1 . PHE A 448 ? 0.3677 0.3375 0.3117 -0.0547 -0.0352 -0.0286 448 PHE A CD1 3456 C CD2 . PHE A 448 ? 0.3755 0.3440 0.3137 -0.0591 -0.0321 -0.0274 448 PHE A CD2 3457 C CE1 . PHE A 448 ? 0.3743 0.3392 0.3145 -0.0566 -0.0363 -0.0268 448 PHE A CE1 3458 C CE2 . PHE A 448 ? 0.3754 0.3387 0.3097 -0.0607 -0.0333 -0.0256 448 PHE A CE2 3459 C CZ . PHE A 448 ? 0.3818 0.3436 0.3173 -0.0595 -0.0354 -0.0252 448 PHE A CZ 3460 N N . GLU A 449 ? 0.4523 0.3432 0.3211 -0.0446 0.0601 -0.0745 449 GLU A N 3461 C CA . GLU A 449 ? 0.4994 0.3761 0.3598 -0.0508 0.0668 -0.0780 449 GLU A CA 3462 C C . GLU A 449 ? 0.4693 0.3657 0.3392 -0.0574 0.0564 -0.0784 449 GLU A C 3463 O O . GLU A 449 ? 0.4676 0.3625 0.3436 -0.0548 0.0590 -0.0768 449 GLU A O 3464 C CB . GLU A 449 ? 0.5613 0.4098 0.3930 -0.0632 0.0770 -0.0856 449 GLU A CB 3465 C CG . GLU A 449 ? 0.6206 0.4417 0.4408 -0.0533 0.0937 -0.0836 449 GLU A CG 3466 C CD . GLU A 449 ? 0.6688 0.4822 0.4996 -0.0409 0.1038 -0.0770 449 GLU A CD 3467 O OE1 . GLU A 449 ? 0.7193 0.5242 0.5457 -0.0468 0.1069 -0.0799 449 GLU A OE1 3468 O OE2 . GLU A 449 ? 0.6702 0.4886 0.5147 -0.0258 0.1080 -0.0677 449 GLU A OE2 3469 N N . ARG A 450 ? 0.4727 0.3889 0.3447 -0.0649 0.0455 -0.0788 450 ARG A N 3470 C CA . ARG A 450 ? 0.4851 0.4225 0.3679 -0.0693 0.0373 -0.0763 450 ARG A CA 3471 C C . ARG A 450 ? 0.4480 0.3985 0.3501 -0.0547 0.0335 -0.0701 450 ARG A C 3472 O O . ARG A 450 ? 0.4233 0.3809 0.3325 -0.0542 0.0326 -0.0678 450 ARG A O 3473 C CB . ARG A 450 ? 0.5365 0.4943 0.4172 -0.0813 0.0277 -0.0755 450 ARG A CB 3474 C CG . ARG A 450 ? 0.5672 0.5454 0.4580 -0.0744 0.0198 -0.0707 450 ARG A CG 3475 C CD . ARG A 450 ? 0.6216 0.6171 0.5055 -0.0897 0.0125 -0.0698 450 ARG A CD 3476 N NE . ARG A 450 ? 0.6467 0.6632 0.5400 -0.0834 0.0058 -0.0639 450 ARG A NE 3477 C CZ . ARG A 450 ? 0.6630 0.6779 0.5462 -0.0868 0.0045 -0.0657 450 ARG A CZ 3478 N NH1 . ARG A 450 ? 0.6518 0.6433 0.5125 -0.0967 0.0099 -0.0736 450 ARG A NH1 3479 N NH2 . ARG A 450 ? 0.6440 0.6793 0.5381 -0.0795 -0.0009 -0.0590 450 ARG A NH2 3480 N N . THR A 451 ? 0.4089 0.3605 0.3175 -0.0436 0.0320 -0.0674 451 THR A N 3481 C CA . THR A 451 ? 0.3842 0.3424 0.3056 -0.0317 0.0287 -0.0625 451 THR A CA 3482 C C . THR A 451 ? 0.3909 0.3363 0.3128 -0.0273 0.0357 -0.0618 451 THR A C 3483 O O . THR A 451 ? 0.3836 0.3336 0.3112 -0.0233 0.0341 -0.0594 451 THR A O 3484 C CB . THR A 451 ? 0.3687 0.3291 0.2947 -0.0241 0.0250 -0.0596 451 THR A CB 3485 O OG1 . THR A 451 ? 0.3524 0.3247 0.2777 -0.0278 0.0196 -0.0597 451 THR A OG1 3486 C CG2 . THR A 451 ? 0.3478 0.3117 0.2817 -0.0151 0.0205 -0.0553 451 THR A CG2 3487 N N . LYS A 452 ? 0.4096 0.3383 0.3246 -0.0272 0.0447 -0.0628 452 LYS A N 3488 C CA . LYS A 452 ? 0.4332 0.3495 0.3483 -0.0226 0.0535 -0.0605 452 LYS A CA 3489 C C . LYS A 452 ? 0.4459 0.3608 0.3585 -0.0288 0.0555 -0.0631 452 LYS A C 3490 O O . LYS A 452 ? 0.4201 0.3356 0.3389 -0.0228 0.0572 -0.0595 452 LYS A O 3491 C CB . LYS A 452 ? 0.4706 0.3663 0.3753 -0.0220 0.0663 -0.0608 452 LYS A CB 3492 C CG . LYS A 452 ? 0.5098 0.3928 0.4156 -0.0149 0.0777 -0.0559 452 LYS A CG 3493 C CD . LYS A 452 ? 0.5685 0.4272 0.4611 -0.0132 0.0937 -0.0553 452 LYS A CD 3494 C CE . LYS A 452 ? 0.6130 0.4621 0.5098 -0.0030 0.1061 -0.0471 452 LYS A CE 3495 N NZ . LYS A 452 ? 0.6193 0.4909 0.5366 0.0075 0.0982 -0.0363 452 LYS A NZ 3496 N N . LYS A 453 ? 0.4575 0.3719 0.3611 -0.0416 0.0547 -0.0683 453 LYS A N 3497 C CA . LYS A 453 ? 0.4829 0.3964 0.3841 -0.0500 0.0566 -0.0697 453 LYS A CA 3498 C C . LYS A 453 ? 0.4515 0.3872 0.3672 -0.0453 0.0484 -0.0648 453 LYS A C 3499 O O . LYS A 453 ? 0.4611 0.3960 0.3805 -0.0436 0.0517 -0.0627 453 LYS A O 3500 C CB . LYS A 453 ? 0.5107 0.4202 0.3976 -0.0681 0.0561 -0.0753 453 LYS A CB 3501 C CG . LYS A 453 ? 0.5442 0.4271 0.4106 -0.0736 0.0652 -0.0812 453 LYS A CG 3502 C CD . LYS A 453 ? 0.5722 0.4250 0.4209 -0.0812 0.0786 -0.0854 453 LYS A CD 3503 C CE . LYS A 453 ? 0.5984 0.4221 0.4215 -0.0875 0.0882 -0.0916 453 LYS A CE 3504 N NZ . LYS A 453 ? 0.6184 0.4043 0.4185 -0.0939 0.1046 -0.0962 453 LYS A NZ 3505 N N . GLN A 454 ? 0.4323 0.3858 0.3548 -0.0420 0.0394 -0.0624 454 GLN A N 3506 C CA . GLN A 454 ? 0.4242 0.3948 0.3574 -0.0351 0.0340 -0.0569 454 GLN A CA 3507 C C . GLN A 454 ? 0.3935 0.3568 0.3299 -0.0230 0.0366 -0.0544 454 GLN A C 3508 O O . GLN A 454 ? 0.3883 0.3571 0.3288 -0.0189 0.0371 -0.0508 454 GLN A O 3509 C CB . GLN A 454 ? 0.4343 0.4188 0.3716 -0.0307 0.0266 -0.0542 454 GLN A CB 3510 C CG . GLN A 454 ? 0.4598 0.4623 0.3985 -0.0402 0.0220 -0.0522 454 GLN A CG 3511 C CD . GLN A 454 ? 0.4657 0.4819 0.4099 -0.0325 0.0166 -0.0475 454 GLN A CD 3512 O OE1 . GLN A 454 ? 0.4712 0.5000 0.4224 -0.0255 0.0158 -0.0406 454 GLN A OE1 3513 N NE2 . GLN A 454 ? 0.4580 0.4702 0.3984 -0.0328 0.0145 -0.0503 454 GLN A NE2 3514 N N . LEU A 455 ? 0.3699 0.3226 0.3043 -0.0174 0.0378 -0.0549 455 LEU A N 3515 C CA . LEU A 455 ? 0.3553 0.3044 0.2921 -0.0074 0.0374 -0.0512 455 LEU A CA 3516 C C . LEU A 455 ? 0.3603 0.3010 0.2970 -0.0057 0.0451 -0.0496 455 LEU A C 3517 O O . LEU A 455 ? 0.3418 0.2829 0.2798 0.0013 0.0442 -0.0458 455 LEU A O 3518 C CB . LEU A 455 ? 0.3480 0.2934 0.2850 -0.0037 0.0350 -0.0497 455 LEU A CB 3519 C CG . LEU A 455 ? 0.3366 0.2896 0.2738 -0.0037 0.0270 -0.0503 455 LEU A CG 3520 C CD1 . LEU A 455 ? 0.3229 0.2734 0.2615 -0.0020 0.0249 -0.0481 455 LEU A CD1 3521 C CD2 . LEU A 455 ? 0.3361 0.2926 0.2717 0.0016 0.0219 -0.0483 455 LEU A CD2 3522 N N . ARG A 456 ? 0.3793 0.3107 0.3123 -0.0126 0.0532 -0.0523 456 ARG A N 3523 C CA . ARG A 456 ? 0.4019 0.3231 0.3342 -0.0112 0.0625 -0.0504 456 ARG A CA 3524 C C . ARG A 456 ? 0.3926 0.3109 0.3285 -0.0003 0.0648 -0.0441 456 ARG A C 3525 O O . ARG A 456 ? 0.3858 0.3016 0.3223 0.0026 0.0655 -0.0418 456 ARG A O 3526 C CB . ARG A 456 ? 0.4205 0.3496 0.3559 -0.0130 0.0617 -0.0494 456 ARG A CB 3527 C CG . ARG A 456 ? 0.4385 0.3724 0.3719 -0.0262 0.0609 -0.0526 456 ARG A CG 3528 C CD . ARG A 456 ? 0.4644 0.3807 0.3896 -0.0358 0.0710 -0.0557 456 ARG A CD 3529 N NE . ARG A 456 ? 0.4742 0.3857 0.4024 -0.0326 0.0780 -0.0521 456 ARG A NE 3530 C CZ . ARG A 456 ? 0.4745 0.3935 0.4061 -0.0399 0.0782 -0.0503 456 ARG A CZ 3531 N NH1 . ARG A 456 ? 0.4697 0.4049 0.4038 -0.0511 0.0708 -0.0503 456 ARG A NH1 3532 N NH2 . ARG A 456 ? 0.4876 0.4003 0.4217 -0.0358 0.0858 -0.0467 456 ARG A NH2 3533 N N . GLU A 457 ? 0.4014 0.3226 0.3402 0.0054 0.0652 -0.0399 457 GLU A N 3534 C CA . GLU A 457 ? 0.4062 0.3276 0.3481 0.0142 0.0666 -0.0323 457 GLU A CA 3535 C C . GLU A 457 ? 0.3962 0.3275 0.3380 0.0181 0.0545 -0.0297 457 GLU A C 3536 O O . GLU A 457 ? 0.3972 0.3318 0.3400 0.0233 0.0526 -0.0227 457 GLU A O 3537 C CB . GLU A 457 ? 0.4326 0.3503 0.3754 0.0179 0.0742 -0.0286 457 GLU A CB 3538 C CG . GLU A 457 ? 0.4681 0.3714 0.4081 0.0129 0.0872 -0.0311 457 GLU A CG 3539 C CD . GLU A 457 ? 0.4868 0.3779 0.4250 0.0152 0.0970 -0.0282 457 GLU A CD 3540 O OE1 . GLU A 457 ? 0.5314 0.4283 0.4756 0.0242 0.0975 -0.0191 457 GLU A OE1 3541 O OE2 . GLU A 457 ? 0.5187 0.3944 0.4485 0.0079 0.1048 -0.0339 457 GLU A OE2 3542 N N . ASN A 458 ? 0.3685 0.3040 0.3076 0.0147 0.0465 -0.0346 458 ASN A N 3543 C CA . ASN A 458 ? 0.3559 0.2949 0.2902 0.0172 0.0362 -0.0333 458 ASN A CA 3544 C C . ASN A 458 ? 0.3469 0.2884 0.2829 0.0158 0.0302 -0.0310 458 ASN A C 3545 O O . ASN A 458 ? 0.3395 0.2814 0.2697 0.0156 0.0214 -0.0298 458 ASN A O 3546 C CB . ASN A 458 ? 0.3563 0.2970 0.2859 0.0165 0.0326 -0.0379 458 ASN A CB 3547 C CG . ASN A 458 ? 0.3622 0.3036 0.2915 0.0187 0.0380 -0.0376 458 ASN A CG 3548 O OD1 . ASN A 458 ? 0.3690 0.3079 0.3001 0.0207 0.0436 -0.0348 458 ASN A OD1 3549 N ND2 . ASN A 458 ? 0.3689 0.3152 0.2974 0.0190 0.0371 -0.0388 458 ASN A ND2 3550 N N . ALA A 459 ? 0.3384 0.2796 0.2808 0.0144 0.0358 -0.0298 459 ALA A N 3551 C CA . ALA A 459 ? 0.3422 0.2874 0.2885 0.0135 0.0316 -0.0262 459 ALA A CA 3552 C C . ALA A 459 ? 0.3527 0.2968 0.3061 0.0166 0.0415 -0.0193 459 ALA A C 3553 O O . ALA A 459 ? 0.3701 0.3057 0.3225 0.0178 0.0528 -0.0207 459 ALA A O 3554 C CB . ALA A 459 ? 0.3260 0.2710 0.2700 0.0092 0.0284 -0.0331 459 ALA A CB 3555 N N . GLU A 460 ? 0.3493 0.3012 0.3093 0.0179 0.0382 -0.0111 460 GLU A N 3556 C CA . GLU A 460 ? 0.3623 0.3135 0.3296 0.0228 0.0493 -0.0026 460 GLU A CA 3557 C C . GLU A 460 ? 0.3612 0.3144 0.3309 0.0211 0.0476 -0.0024 460 GLU A C 3558 O O . GLU A 460 ? 0.3368 0.2977 0.3072 0.0169 0.0354 -0.0034 460 GLU A O 3559 C CB . GLU A 460 ? 0.3658 0.3293 0.3433 0.0284 0.0500 0.0130 460 GLU A CB 3560 C CG . GLU A 460 ? 0.3660 0.3265 0.3416 0.0319 0.0554 0.0146 460 GLU A CG 3561 C CD . GLU A 460 ? 0.3737 0.3506 0.3588 0.0363 0.0530 0.0311 460 GLU A CD 3562 O OE1 . GLU A 460 ? 0.3695 0.3608 0.3657 0.0382 0.0514 0.0446 460 GLU A OE1 3563 O OE2 . GLU A 460 ? 0.3692 0.3461 0.3509 0.0378 0.0528 0.0317 460 GLU A OE2 3564 N N . ASP A 461 ? 0.3703 0.3137 0.3391 0.0247 0.0613 -0.0010 461 ASP A N 3565 C CA . ASP A 461 ? 0.3829 0.3265 0.3533 0.0252 0.0632 0.0008 461 ASP A CA 3566 C C . ASP A 461 ? 0.3870 0.3481 0.3729 0.0305 0.0608 0.0181 461 ASP A C 3567 O O . ASP A 461 ? 0.3863 0.3506 0.3799 0.0384 0.0710 0.0311 461 ASP A O 3568 C CB . ASP A 461 ? 0.4063 0.3291 0.3662 0.0280 0.0811 -0.0024 461 ASP A CB 3569 C CG . ASP A 461 ? 0.4156 0.3340 0.3718 0.0280 0.0845 -0.0030 461 ASP A CG 3570 O OD1 . ASP A 461 ? 0.3995 0.3335 0.3664 0.0288 0.0758 0.0035 461 ASP A OD1 3571 O OD2 . ASP A 461 ? 0.4561 0.3530 0.3965 0.0265 0.0967 -0.0103 461 ASP A OD2 3572 N N . MET A 462 ? 0.3697 0.3429 0.3606 0.0258 0.0477 0.0197 462 MET A N 3573 C CA . MET A 462 ? 0.3836 0.3768 0.3902 0.0276 0.0426 0.0372 462 MET A CA 3574 C C . MET A 462 ? 0.3992 0.3938 0.4136 0.0349 0.0546 0.0475 462 MET A C 3575 O O . MET A 462 ? 0.4031 0.4173 0.4335 0.0372 0.0520 0.0651 462 MET A O 3576 C CB . MET A 462 ? 0.3886 0.3910 0.3950 0.0178 0.0238 0.0346 462 MET A CB 3577 C CG . MET A 462 ? 0.4019 0.4007 0.3977 0.0114 0.0126 0.0260 462 MET A CG 3578 S SD . MET A 462 ? 0.4298 0.4264 0.4164 0.0008 -0.0045 0.0183 462 MET A SD 3579 C CE . MET A 462 ? 0.4513 0.4685 0.4533 -0.0035 -0.0125 0.0372 462 MET A CE 3580 N N . GLY A 463 ? 0.3894 0.3639 0.3915 0.0377 0.0672 0.0375 463 GLY A N 3581 C CA . GLY A 463 ? 0.4050 0.3743 0.4091 0.0463 0.0824 0.0464 463 GLY A CA 3582 C C . GLY A 463 ? 0.4015 0.3763 0.4078 0.0436 0.0765 0.0460 463 GLY A C 3583 O O . GLY A 463 ? 0.4120 0.3817 0.4186 0.0513 0.0895 0.0533 463 GLY A O 3584 N N . ASN A 464 ? 0.3782 0.3614 0.3847 0.0337 0.0585 0.0378 464 ASN A N 3585 C CA . ASN A 464 ? 0.3856 0.3744 0.3947 0.0306 0.0519 0.0376 464 ASN A CA 3586 C C . ASN A 464 ? 0.3733 0.3496 0.3664 0.0236 0.0467 0.0186 464 ASN A C 3587 O O . ASN A 464 ? 0.3994 0.3815 0.3941 0.0194 0.0375 0.0166 464 ASN A O 3588 C CB . ASN A 464 ? 0.3905 0.4009 0.4144 0.0246 0.0354 0.0479 464 ASN A CB 3589 C CG . ASN A 464 ? 0.3906 0.3998 0.4072 0.0156 0.0213 0.0380 464 ASN A CG 3590 O OD1 . ASN A 464 ? 0.3928 0.3902 0.3988 0.0160 0.0247 0.0274 464 ASN A OD1 3591 N ND2 . ASN A 464 ? 0.4096 0.4290 0.4302 0.0073 0.0062 0.0417 464 ASN A ND2 3592 N N . GLY A 465 ? 0.3635 0.3238 0.3419 0.0223 0.0528 0.0063 465 GLY A N 3593 C CA . GLY A 465 ? 0.3653 0.3190 0.3308 0.0148 0.0467 -0.0091 465 GLY A CA 3594 C C . GLY A 465 ? 0.3413 0.3018 0.3080 0.0093 0.0332 -0.0145 465 GLY A C 3595 O O . GLY A 465 ? 0.3481 0.3078 0.3078 0.0045 0.0274 -0.0239 465 GLY A O 3596 N N . CYS A 466 ? 0.3358 0.3026 0.3101 0.0105 0.0291 -0.0077 466 CYS A N 3597 C CA . CYS A 466 ? 0.3368 0.3058 0.3084 0.0062 0.0182 -0.0123 466 CYS A CA 3598 C C . CYS A 466 ? 0.3273 0.2927 0.2969 0.0078 0.0220 -0.0127 466 CYS A C 3599 O O . CYS A 466 ? 0.3231 0.2885 0.2979 0.0127 0.0309 -0.0049 466 CYS A O 3600 C CB . CYS A 466 ? 0.3628 0.3416 0.3411 0.0032 0.0064 -0.0041 466 CYS A CB 3601 S SG . CYS A 466 ? 0.3882 0.3734 0.3726 0.0012 0.0016 0.0006 466 CYS A SG 3602 N N . PHE A 467 ? 0.3161 0.2785 0.2784 0.0049 0.0163 -0.0204 467 PHE A N 3603 C CA . PHE A 467 ? 0.3202 0.2801 0.2802 0.0062 0.0179 -0.0206 467 PHE A CA 3604 C C . PHE A 467 ? 0.3266 0.2905 0.2851 0.0043 0.0070 -0.0165 467 PHE A C 3605 O O . PHE A 467 ? 0.3128 0.2750 0.2655 0.0007 -0.0015 -0.0196 467 PHE A O 3606 C CB . PHE A 467 ? 0.3188 0.2722 0.2704 0.0044 0.0200 -0.0310 467 PHE A CB 3607 C CG . PHE A 467 ? 0.3264 0.2738 0.2748 0.0027 0.0293 -0.0361 467 PHE A CG 3608 C CD1 . PHE A 467 ? 0.3405 0.2793 0.2873 0.0043 0.0405 -0.0350 467 PHE A CD1 3609 C CD2 . PHE A 467 ? 0.3248 0.2734 0.2695 -0.0011 0.0273 -0.0414 467 PHE A CD2 3610 C CE1 . PHE A 467 ? 0.3549 0.2826 0.2931 0.0005 0.0496 -0.0407 467 PHE A CE1 3611 C CE2 . PHE A 467 ? 0.3377 0.2792 0.2753 -0.0052 0.0348 -0.0463 467 PHE A CE2 3612 C CZ . PHE A 467 ? 0.3507 0.2799 0.2835 -0.0051 0.0459 -0.0466 467 PHE A CZ 3613 N N . LYS A 468 ? 0.3277 0.2954 0.2894 0.0062 0.0080 -0.0092 468 LYS A N 3614 C CA . LYS A 468 ? 0.3475 0.3156 0.3023 0.0032 -0.0014 -0.0071 468 LYS A CA 3615 C C . LYS A 468 ? 0.3462 0.3051 0.2915 0.0055 0.0022 -0.0154 468 LYS A C 3616 O O . LYS A 468 ? 0.3388 0.2975 0.2880 0.0097 0.0112 -0.0144 468 LYS A O 3617 C CB . LYS A 468 ? 0.3760 0.3566 0.3396 0.0036 -0.0030 0.0070 468 LYS A CB 3618 C CG . LYS A 468 ? 0.4076 0.3879 0.3602 -0.0016 -0.0138 0.0091 468 LYS A CG 3619 C CD . LYS A 468 ? 0.4397 0.4382 0.4029 -0.0033 -0.0178 0.0260 468 LYS A CD 3620 C CE . LYS A 468 ? 0.4734 0.4708 0.4217 -0.0111 -0.0300 0.0280 468 LYS A CE 3621 N NZ . LYS A 468 ? 0.4945 0.5148 0.4547 -0.0138 -0.0348 0.0470 468 LYS A NZ 3622 N N . ILE A 469 ? 0.3422 0.2927 0.2751 0.0036 -0.0031 -0.0227 469 ILE A N 3623 C CA . ILE A 469 ? 0.3478 0.2910 0.2722 0.0067 0.0005 -0.0288 469 ILE A CA 3624 C C . ILE A 469 ? 0.3696 0.3081 0.2828 0.0062 -0.0047 -0.0255 469 ILE A C 3625 O O . ILE A 469 ? 0.3839 0.3163 0.2854 0.0015 -0.0136 -0.0247 469 ILE A O 3626 C CB . ILE A 469 ? 0.3544 0.2916 0.2713 0.0071 -0.0003 -0.0359 469 ILE A CB 3627 C CG1 . ILE A 469 ? 0.3389 0.2826 0.2655 0.0062 0.0036 -0.0385 469 ILE A CG1 3628 C CG2 . ILE A 469 ? 0.3553 0.2871 0.2645 0.0115 0.0039 -0.0391 469 ILE A CG2 3629 C CD1 . ILE A 469 ? 0.3490 0.2912 0.2708 0.0066 0.0018 -0.0423 469 ILE A CD1 3630 N N . TYR A 470 ? 0.3782 0.3178 0.2926 0.0101 0.0008 -0.0237 470 TYR A N 3631 C CA . TYR A 470 ? 0.3957 0.3337 0.3006 0.0094 -0.0038 -0.0185 470 TYR A CA 3632 C C . TYR A 470 ? 0.4186 0.3417 0.3035 0.0115 -0.0044 -0.0244 470 TYR A C 3633 O O . TYR A 470 ? 0.4342 0.3549 0.3119 0.0140 -0.0031 -0.0219 470 TYR A O 3634 C CB . TYR A 470 ? 0.3949 0.3425 0.3119 0.0138 0.0035 -0.0113 470 TYR A CB 3635 C CG . TYR A 470 ? 0.3904 0.3518 0.3224 0.0128 0.0034 -0.0006 470 TYR A CG 3636 C CD1 . TYR A 470 ? 0.3825 0.3468 0.3274 0.0148 0.0111 -0.0007 470 TYR A CD1 3637 C CD2 . TYR A 470 ? 0.3934 0.3658 0.3261 0.0098 -0.0039 0.0110 470 TYR A CD2 3638 C CE1 . TYR A 470 ? 0.3772 0.3535 0.3359 0.0162 0.0134 0.0110 470 TYR A CE1 3639 C CE2 . TYR A 470 ? 0.3922 0.3814 0.3417 0.0103 -0.0030 0.0244 470 TYR A CE2 3640 C CZ . TYR A 470 ? 0.3860 0.3764 0.3488 0.0146 0.0066 0.0245 470 TYR A CZ 3641 O OH . TYR A 470 ? 0.3935 0.3996 0.3727 0.0173 0.0099 0.0395 470 TYR A OH 3642 N N . HIS A 471 ? 0.4156 0.3283 0.2912 0.0117 -0.0050 -0.0310 471 HIS A N 3643 C CA . HIS A 471 ? 0.4343 0.3298 0.2887 0.0154 -0.0036 -0.0350 471 HIS A CA 3644 C C . HIS A 471 ? 0.4526 0.3344 0.2933 0.0130 -0.0073 -0.0389 471 HIS A C 3645 O O . HIS A 471 ? 0.4289 0.3177 0.2806 0.0097 -0.0098 -0.0392 471 HIS A O 3646 C CB . HIS A 471 ? 0.4269 0.3253 0.2876 0.0238 0.0069 -0.0368 471 HIS A CB 3647 C CG . HIS A 471 ? 0.3997 0.3082 0.2759 0.0247 0.0111 -0.0390 471 HIS A CG 3648 N ND1 . HIS A 471 ? 0.4160 0.3192 0.2862 0.0272 0.0121 -0.0412 471 HIS A ND1 3649 C CD2 . HIS A 471 ? 0.3790 0.3019 0.2744 0.0230 0.0152 -0.0388 471 HIS A CD2 3650 C CE1 . HIS A 471 ? 0.3954 0.3130 0.2822 0.0263 0.0150 -0.0416 471 HIS A CE1 3651 N NE2 . HIS A 471 ? 0.3823 0.3101 0.2826 0.0229 0.0166 -0.0410 471 HIS A NE2 3652 N N . LYS A 472 ? 0.4788 0.3384 0.2935 0.0151 -0.0065 -0.0417 472 LYS A N 3653 C CA . LYS A 472 ? 0.5198 0.3610 0.3181 0.0147 -0.0069 -0.0452 472 LYS A CA 3654 C C . LYS A 472 ? 0.4965 0.3492 0.3122 0.0224 0.0010 -0.0457 472 LYS A C 3655 O O . LYS A 472 ? 0.4840 0.3446 0.3077 0.0306 0.0093 -0.0444 472 LYS A O 3656 C CB . LYS A 472 ? 0.5720 0.3828 0.3359 0.0183 -0.0032 -0.0479 472 LYS A CB 3657 C CG . LYS A 472 ? 0.6304 0.4168 0.3742 0.0200 0.0000 -0.0511 472 LYS A CG 3658 C CD . LYS A 472 ? 0.6961 0.4463 0.4008 0.0248 0.0065 -0.0537 472 LYS A CD 3659 C CE . LYS A 472 ? 0.7444 0.4649 0.4253 0.0260 0.0110 -0.0565 472 LYS A CE 3660 N NZ . LYS A 472 ? 0.8187 0.4995 0.4592 0.0338 0.0219 -0.0586 472 LYS A NZ 3661 N N . CYS A 473 ? 0.4922 0.3481 0.3147 0.0189 -0.0020 -0.0464 473 CYS A N 3662 C CA . CYS A 473 ? 0.4908 0.3615 0.3307 0.0245 0.0039 -0.0457 473 CYS A CA 3663 C C . CYS A 473 ? 0.5001 0.3571 0.3290 0.0252 0.0038 -0.0464 473 CYS A C 3664 O O . CYS A 473 ? 0.5008 0.3620 0.3362 0.0186 -0.0022 -0.0467 473 CYS A O 3665 C CB . CYS A 473 ? 0.4866 0.3820 0.3527 0.0199 0.0016 -0.0448 473 CYS A CB 3666 S SG . CYS A 473 ? 0.4892 0.4052 0.3746 0.0235 0.0079 -0.0438 473 CYS A SG 3667 N N . ASP A 474 ? 0.5101 0.3495 0.3215 0.0343 0.0122 -0.0457 474 ASP A N 3668 C CA . ASP A 474 ? 0.5229 0.3428 0.3187 0.0372 0.0154 -0.0456 474 ASP A CA 3669 C C . ASP A 474 ? 0.5042 0.3460 0.3220 0.0415 0.0185 -0.0417 474 ASP A C 3670 O O . ASP A 474 ? 0.4754 0.3455 0.3178 0.0397 0.0167 -0.0403 474 ASP A O 3671 C CB . ASP A 474 ? 0.5593 0.3495 0.3260 0.0477 0.0263 -0.0448 474 ASP A CB 3672 C CG . ASP A 474 ? 0.5536 0.3597 0.3328 0.0618 0.0384 -0.0382 474 ASP A CG 3673 O OD1 . ASP A 474 ? 0.5113 0.3505 0.3200 0.0627 0.0380 -0.0341 474 ASP A OD1 3674 O OD2 . ASP A 474 ? 0.5738 0.3578 0.3311 0.0720 0.0488 -0.0361 474 ASP A OD2 3675 N N . ASN A 475 ? 0.5100 0.3376 0.3171 0.0465 0.0236 -0.0397 475 ASN A N 3676 C CA . ASN A 475 ? 0.4994 0.3492 0.3270 0.0491 0.0249 -0.0353 475 ASN A CA 3677 C C . ASN A 475 ? 0.4745 0.3542 0.3234 0.0565 0.0307 -0.0287 475 ASN A C 3678 O O . ASN A 475 ? 0.4488 0.3558 0.3195 0.0522 0.0268 -0.0271 475 ASN A O 3679 C CB . ASN A 475 ? 0.5345 0.3627 0.3462 0.0552 0.0313 -0.0326 475 ASN A CB 3680 C CG . ASN A 475 ? 0.5514 0.3595 0.3502 0.0437 0.0227 -0.0380 475 ASN A CG 3681 O OD1 . ASN A 475 ? 0.5367 0.3536 0.3437 0.0316 0.0113 -0.0419 475 ASN A OD1 3682 N ND2 . ASN A 475 ? 0.5783 0.3592 0.3571 0.0475 0.0289 -0.0368 475 ASN A ND2 3683 N N . ALA A 476 ? 0.4790 0.3530 0.3201 0.0667 0.0401 -0.0243 476 ALA A N 3684 C CA . ALA A 476 ? 0.4694 0.3735 0.3310 0.0727 0.0455 -0.0158 476 ALA A CA 3685 C C . ALA A 476 ? 0.4410 0.3660 0.3197 0.0620 0.0377 -0.0200 476 ALA A C 3686 O O . ALA A 476 ? 0.4419 0.3960 0.3413 0.0584 0.0361 -0.0161 476 ALA A O 3687 C CB . ALA A 476 ? 0.4853 0.3777 0.3345 0.0875 0.0588 -0.0081 476 ALA A CB 3688 N N . CYS A 477 ? 0.4524 0.3619 0.3211 0.0561 0.0328 -0.0276 477 CYS A N 3689 C CA . CYS A 477 ? 0.4378 0.3626 0.3205 0.0473 0.0274 -0.0312 477 CYS A CA 3690 C C . CYS A 477 ? 0.4107 0.3511 0.3084 0.0376 0.0204 -0.0339 477 CYS A C 3691 O O . CYS A 477 ? 0.3929 0.3537 0.3059 0.0325 0.0199 -0.0331 477 CYS A O 3692 C CB . CYS A 477 ? 0.4755 0.3806 0.3437 0.0439 0.0238 -0.0366 477 CYS A CB 3693 S SG . CYS A 477 ? 0.4882 0.4068 0.3710 0.0348 0.0189 -0.0398 477 CYS A SG 3694 N N . ILE A 478 ? 0.4030 0.3324 0.2943 0.0345 0.0156 -0.0368 478 ILE A N 3695 C CA . ILE A 478 ? 0.3912 0.3336 0.2950 0.0271 0.0104 -0.0384 478 ILE A CA 3696 C C . ILE A 478 ? 0.3821 0.3465 0.2984 0.0285 0.0131 -0.0336 478 ILE A C 3697 O O . ILE A 478 ? 0.3753 0.3557 0.3029 0.0213 0.0108 -0.0348 478 ILE A O 3698 C CB . ILE A 478 ? 0.3975 0.3256 0.2931 0.0244 0.0055 -0.0401 478 ILE A CB 3699 C CG1 . ILE A 478 ? 0.4042 0.3162 0.2894 0.0194 0.0003 -0.0432 478 ILE A CG1 3700 C CG2 . ILE A 478 ? 0.3842 0.3270 0.2932 0.0189 0.0019 -0.0403 478 ILE A CG2 3701 C CD1 . ILE A 478 ? 0.3835 0.3071 0.2810 0.0135 -0.0026 -0.0441 478 ILE A CD1 3702 N N . GLY A 479 ? 0.3991 0.3633 0.3117 0.0377 0.0186 -0.0272 479 GLY A N 3703 C CA . GLY A 479 ? 0.3880 0.3773 0.3136 0.0397 0.0211 -0.0193 479 GLY A CA 3704 C C . GLY A 479 ? 0.3890 0.4008 0.3272 0.0345 0.0211 -0.0167 479 GLY A C 3705 O O . GLY A 479 ? 0.3860 0.4203 0.3354 0.0271 0.0179 -0.0143 479 GLY A O 3706 N N . SER A 480 ? 0.3879 0.3930 0.3228 0.0369 0.0243 -0.0173 480 SER A N 3707 C CA . SER A 480 ? 0.3888 0.4127 0.3349 0.0308 0.0247 -0.0148 480 SER A CA 3708 C C . SER A 480 ? 0.3835 0.4109 0.3337 0.0163 0.0187 -0.0230 480 SER A C 3709 O O . SER A 480 ? 0.3929 0.4390 0.3516 0.0070 0.0172 -0.0209 480 SER A O 3710 C CB . SER A 480 ? 0.3979 0.4111 0.3385 0.0373 0.0301 -0.0138 480 SER A CB 3711 O OG . SER A 480 ? 0.4107 0.4046 0.3430 0.0333 0.0275 -0.0232 480 SER A OG 3712 N N . ILE A 481 ? 0.3800 0.3887 0.3228 0.0142 0.0159 -0.0313 481 ILE A N 3713 C CA . ILE A 481 ? 0.3701 0.3779 0.3145 0.0034 0.0130 -0.0379 481 ILE A CA 3714 C C . ILE A 481 ? 0.3817 0.4025 0.3296 -0.0024 0.0098 -0.0371 481 ILE A C 3715 O O . ILE A 481 ? 0.3873 0.4171 0.3369 -0.0130 0.0089 -0.0388 481 ILE A O 3716 C CB . ILE A 481 ? 0.3667 0.3552 0.3048 0.0045 0.0116 -0.0431 481 ILE A CB 3717 C CG1 . ILE A 481 ? 0.3624 0.3394 0.2956 0.0094 0.0139 -0.0432 481 ILE A CG1 3718 C CG2 . ILE A 481 ? 0.3589 0.3455 0.2984 -0.0038 0.0117 -0.0477 481 ILE A CG2 3719 C CD1 . ILE A 481 ? 0.3670 0.3286 0.2936 0.0107 0.0110 -0.0452 481 ILE A CD1 3720 N N . ARG A 482 ? 0.3951 0.4151 0.3418 0.0036 0.0084 -0.0345 482 ARG A N 3721 C CA . ARG A 482 ? 0.4089 0.4419 0.3588 -0.0004 0.0055 -0.0326 482 ARG A CA 3722 C C . ARG A 482 ? 0.4446 0.5038 0.4020 -0.0053 0.0049 -0.0254 482 ARG A C 3723 O O . ARG A 482 ? 0.4722 0.5436 0.4301 -0.0151 0.0015 -0.0258 482 ARG A O 3724 C CB . ARG A 482 ? 0.4098 0.4367 0.3574 0.0086 0.0055 -0.0294 482 ARG A CB 3725 C CG . ARG A 482 ? 0.4095 0.4152 0.3506 0.0094 0.0037 -0.0351 482 ARG A CG 3726 C CD . ARG A 482 ? 0.4159 0.4166 0.3546 0.0145 0.0028 -0.0322 482 ARG A CD 3727 N NE . ARG A 482 ? 0.4401 0.4413 0.3763 0.0241 0.0073 -0.0253 482 ARG A NE 3728 C CZ . ARG A 482 ? 0.4707 0.4509 0.3956 0.0313 0.0100 -0.0246 482 ARG A CZ 3729 N NH1 . ARG A 482 ? 0.4745 0.4339 0.3904 0.0280 0.0063 -0.0300 482 ARG A NH1 3730 N NH2 . ARG A 482 ? 0.4774 0.4571 0.3988 0.0417 0.0170 -0.0172 482 ARG A NH2 3731 N N . ASN A 483 ? 0.4868 0.5551 0.4492 0.0010 0.0083 -0.0177 483 ASN A N 3732 C CA . ASN A 483 ? 0.5414 0.6398 0.5143 -0.0021 0.0079 -0.0065 483 ASN A CA 3733 C C . ASN A 483 ? 0.5203 0.6274 0.4958 -0.0153 0.0062 -0.0080 483 ASN A C 3734 O O . ASN A 483 ? 0.5190 0.6534 0.5039 -0.0218 0.0043 0.0018 483 ASN A O 3735 C CB . ASN A 483 ? 0.6277 0.7314 0.6053 0.0138 0.0146 0.0052 483 ASN A CB 3736 C CG . ASN A 483 ? 0.7294 0.8674 0.7201 0.0155 0.0150 0.0214 483 ASN A CG 3737 O OD1 . ASN A 483 ? 0.7454 0.9070 0.7423 0.0017 0.0084 0.0240 483 ASN A OD1 3738 N ND2 . ASN A 483 ? 0.8444 0.9851 0.8381 0.0326 0.0236 0.0336 483 ASN A ND2 3739 N N . GLY A 484 ? 0.5021 0.5868 0.4697 -0.0195 0.0073 -0.0189 484 GLY A N 3740 C CA . GLY A 484 ? 0.4992 0.5859 0.4664 -0.0324 0.0072 -0.0217 484 GLY A CA 3741 C C . GLY A 484 ? 0.4999 0.5963 0.4754 -0.0279 0.0109 -0.0137 484 GLY A C 3742 O O . GLY A 484 ? 0.5105 0.6172 0.4891 -0.0401 0.0100 -0.0120 484 GLY A O 3743 N N . THR A 485 ? 0.4848 0.5758 0.4620 -0.0110 0.0158 -0.0089 485 THR A N 3744 C CA . THR A 485 ? 0.4725 0.5713 0.4564 -0.0038 0.0212 -0.0001 485 THR A CA 3745 C C . THR A 485 ? 0.4608 0.5326 0.4356 0.0051 0.0262 -0.0068 485 THR A C 3746 O O . THR A 485 ? 0.4639 0.5373 0.4410 0.0138 0.0319 -0.0001 485 THR A O 3747 C CB . THR A 485 ? 0.4876 0.6050 0.4797 0.0097 0.0254 0.0149 485 THR A CB 3748 O OG1 . THR A 485 ? 0.4916 0.5867 0.4727 0.0241 0.0289 0.0119 485 THR A OG1 3749 C CG2 . THR A 485 ? 0.4877 0.6374 0.4910 0.0006 0.0198 0.0244 485 THR A CG2 3750 N N . TYR A 486 ? 0.4409 0.4897 0.4055 0.0029 0.0242 -0.0185 486 TYR A N 3751 C CA . TYR A 486 ? 0.4297 0.4554 0.3854 0.0097 0.0273 -0.0239 486 TYR A CA 3752 C C . TYR A 486 ? 0.4329 0.4601 0.3923 0.0050 0.0307 -0.0235 486 TYR A C 3753 O O . TYR A 486 ? 0.4262 0.4583 0.3889 -0.0078 0.0295 -0.0264 486 TYR A O 3754 C CB . TYR A 486 ? 0.4131 0.4215 0.3613 0.0062 0.0237 -0.0333 486 TYR A CB 3755 C CG . TYR A 486 ? 0.3981 0.3868 0.3388 0.0099 0.0251 -0.0377 486 TYR A CG 3756 C CD1 . TYR A 486 ? 0.3994 0.3737 0.3301 0.0185 0.0241 -0.0379 486 TYR A CD1 3757 C CD2 . TYR A 486 ? 0.3877 0.3714 0.3297 0.0036 0.0274 -0.0413 486 TYR A CD2 3758 C CE1 . TYR A 486 ? 0.3909 0.3508 0.3147 0.0199 0.0237 -0.0405 486 TYR A CE1 3759 C CE2 . TYR A 486 ? 0.3773 0.3470 0.3144 0.0074 0.0288 -0.0430 486 TYR A CE2 3760 C CZ . TYR A 486 ? 0.3797 0.3398 0.3086 0.0150 0.0260 -0.0421 486 TYR A CZ 3761 O OH . TYR A 486 ? 0.3601 0.3099 0.2844 0.0170 0.0259 -0.0422 486 TYR A OH 3762 N N . ASP A 487 ? 0.4424 0.4635 0.3992 0.0154 0.0358 -0.0196 487 ASP A N 3763 C CA . ASP A 487 ? 0.4518 0.4735 0.4122 0.0131 0.0401 -0.0181 487 ASP A CA 3764 C C . ASP A 487 ? 0.4345 0.4333 0.3849 0.0163 0.0413 -0.0253 487 ASP A C 3765 O O . ASP A 487 ? 0.4261 0.4126 0.3670 0.0271 0.0432 -0.0245 487 ASP A O 3766 C CB . ASP A 487 ? 0.4849 0.5176 0.4499 0.0237 0.0461 -0.0068 487 ASP A CB 3767 C CG . ASP A 487 ? 0.5104 0.5481 0.4820 0.0206 0.0507 -0.0032 487 ASP A CG 3768 O OD1 . ASP A 487 ? 0.5092 0.5352 0.4781 0.0130 0.0505 -0.0106 487 ASP A OD1 3769 O OD2 . ASP A 487 ? 0.5425 0.5959 0.5224 0.0267 0.0557 0.0084 487 ASP A OD2 3770 N N . HIS A 488 ? 0.4055 0.3981 0.3565 0.0068 0.0410 -0.0312 488 HIS A N 3771 C CA . HIS A 488 ? 0.4066 0.3815 0.3506 0.0100 0.0424 -0.0354 488 HIS A CA 3772 C C . HIS A 488 ? 0.4179 0.3879 0.3597 0.0176 0.0473 -0.0318 488 HIS A C 3773 O O . HIS A 488 ? 0.4046 0.3625 0.3385 0.0234 0.0469 -0.0327 488 HIS A O 3774 C CB . HIS A 488 ? 0.4079 0.3764 0.3531 0.0003 0.0445 -0.0402 488 HIS A CB 3775 C CG . HIS A 488 ? 0.4061 0.3747 0.3548 -0.0058 0.0509 -0.0391 488 HIS A CG 3776 N ND1 . HIS A 488 ? 0.4176 0.3749 0.3647 -0.0025 0.0571 -0.0387 488 HIS A ND1 3777 C CD2 . HIS A 488 ? 0.4101 0.3903 0.3641 -0.0160 0.0518 -0.0371 488 HIS A CD2 3778 C CE1 . HIS A 488 ? 0.4208 0.3790 0.3711 -0.0099 0.0626 -0.0374 488 HIS A CE1 3779 N NE2 . HIS A 488 ? 0.4209 0.3936 0.3753 -0.0192 0.0587 -0.0365 488 HIS A NE2 3780 N N . ASP A 489 ? 0.4294 0.4102 0.3782 0.0170 0.0517 -0.0265 489 ASP A N 3781 C CA . ASP A 489 ? 0.4771 0.4539 0.4242 0.0247 0.0576 -0.0221 489 ASP A CA 3782 C C . ASP A 489 ? 0.4669 0.4350 0.4016 0.0380 0.0576 -0.0198 489 ASP A C 3783 O O . ASP A 489 ? 0.4879 0.4452 0.4142 0.0444 0.0602 -0.0191 489 ASP A O 3784 C CB . ASP A 489 ? 0.5088 0.5013 0.4676 0.0211 0.0624 -0.0150 489 ASP A CB 3785 C CG . ASP A 489 ? 0.5576 0.5494 0.5222 0.0076 0.0648 -0.0178 489 ASP A CG 3786 O OD1 . ASP A 489 ? 0.6181 0.5942 0.5776 0.0077 0.0679 -0.0222 489 ASP A OD1 3787 O OD2 . ASP A 489 ? 0.5942 0.6008 0.5675 -0.0036 0.0640 -0.0147 489 ASP A OD2 3788 N N . VAL A 490 ? 0.4651 0.4359 0.3964 0.0418 0.0551 -0.0185 490 VAL A N 3789 C CA . VAL A 490 ? 0.4882 0.4444 0.4023 0.0537 0.0566 -0.0171 490 VAL A CA 3790 C C . VAL A 490 ? 0.4725 0.4089 0.3706 0.0535 0.0516 -0.0234 490 VAL A C 3791 O O . VAL A 490 ? 0.4875 0.4086 0.3684 0.0608 0.0536 -0.0227 490 VAL A O 3792 C CB . VAL A 490 ? 0.4980 0.4578 0.4106 0.0568 0.0554 -0.0151 490 VAL A CB 3793 C CG1 . VAL A 490 ? 0.5454 0.4822 0.4346 0.0677 0.0578 -0.0153 490 VAL A CG1 3794 C CG2 . VAL A 490 ? 0.5071 0.4909 0.4362 0.0582 0.0604 -0.0050 490 VAL A CG2 3795 N N . TYR A 491 ? 0.4409 0.3786 0.3442 0.0446 0.0452 -0.0285 491 TYR A N 3796 C CA . TYR A 491 ? 0.4383 0.3629 0.3300 0.0428 0.0389 -0.0319 491 TYR A CA 3797 C C . TYR A 491 ? 0.4226 0.3488 0.3202 0.0395 0.0392 -0.0312 491 TYR A C 3798 O O . TYR A 491 ? 0.4222 0.3423 0.3125 0.0381 0.0339 -0.0310 491 TYR A O 3799 C CB . TYR A 491 ? 0.4298 0.3554 0.3235 0.0370 0.0322 -0.0354 491 TYR A CB 3800 C CG . TYR A 491 ? 0.4468 0.3710 0.3354 0.0407 0.0326 -0.0351 491 TYR A CG 3801 C CD1 . TYR A 491 ? 0.4755 0.3811 0.3433 0.0457 0.0314 -0.0357 491 TYR A CD1 3802 C CD2 . TYR A 491 ? 0.4408 0.3812 0.3436 0.0388 0.0345 -0.0334 491 TYR A CD2 3803 C CE1 . TYR A 491 ? 0.4947 0.3963 0.3568 0.0508 0.0341 -0.0343 491 TYR A CE1 3804 C CE2 . TYR A 491 ? 0.4560 0.3978 0.3560 0.0437 0.0358 -0.0307 491 TYR A CE2 3805 C CZ . TYR A 491 ? 0.4752 0.3969 0.3553 0.0507 0.0366 -0.0309 491 TYR A CZ 3806 O OH . TYR A 491 ? 0.4944 0.4150 0.3707 0.0573 0.0403 -0.0271 491 TYR A OH 3807 N N . ARG A 492 ? 0.4227 0.3573 0.3333 0.0380 0.0457 -0.0295 492 ARG A N 3808 C CA . ARG A 492 ? 0.4251 0.3600 0.3425 0.0352 0.0484 -0.0283 492 ARG A CA 3809 C C . ARG A 492 ? 0.4452 0.3741 0.3537 0.0405 0.0478 -0.0242 492 ARG A C 3810 O O . ARG A 492 ? 0.4475 0.3769 0.3579 0.0389 0.0456 -0.0216 492 ARG A O 3811 C CB . ARG A 492 ? 0.4242 0.3646 0.3532 0.0318 0.0567 -0.0276 492 ARG A CB 3812 C CG . ARG A 492 ? 0.4208 0.3571 0.3552 0.0299 0.0629 -0.0260 492 ARG A CG 3813 C CD . ARG A 492 ? 0.4240 0.3616 0.3659 0.0235 0.0707 -0.0268 492 ARG A CD 3814 N NE . ARG A 492 ? 0.4304 0.3591 0.3747 0.0224 0.0798 -0.0250 492 ARG A NE 3815 C CZ . ARG A 492 ? 0.4302 0.3503 0.3750 0.0156 0.0849 -0.0280 492 ARG A CZ 3816 N NH1 . ARG A 492 ? 0.4161 0.3370 0.3593 0.0082 0.0804 -0.0335 492 ARG A NH1 3817 N NH2 . ARG A 492 ? 0.4443 0.3531 0.3894 0.0168 0.0960 -0.0251 492 ARG A NH2 3818 N N . ASP A 493 ? 0.4663 0.3907 0.3650 0.0470 0.0503 -0.0222 493 ASP A N 3819 C CA . ASP A 493 ? 0.5056 0.4238 0.3921 0.0513 0.0491 -0.0182 493 ASP A CA 3820 C C . ASP A 493 ? 0.4883 0.4008 0.3615 0.0474 0.0383 -0.0188 493 ASP A C 3821 O O . ASP A 493 ? 0.4731 0.3894 0.3466 0.0458 0.0350 -0.0137 493 ASP A O 3822 C CB . ASP A 493 ? 0.5559 0.4665 0.4289 0.0595 0.0538 -0.0166 493 ASP A CB 3823 C CG . ASP A 493 ? 0.5876 0.5059 0.4741 0.0632 0.0642 -0.0127 493 ASP A CG 3824 O OD1 . ASP A 493 ? 0.6050 0.5306 0.5072 0.0591 0.0680 -0.0114 493 ASP A OD1 3825 O OD2 . ASP A 493 ? 0.6413 0.5571 0.5217 0.0703 0.0698 -0.0101 493 ASP A OD2 3826 N N . GLU A 494 ? 0.4839 0.3884 0.3460 0.0457 0.0331 -0.0234 494 GLU A N 3827 C CA . GLU A 494 ? 0.4882 0.3856 0.3365 0.0395 0.0222 -0.0243 494 GLU A CA 3828 C C . GLU A 494 ? 0.4706 0.3819 0.3368 0.0332 0.0180 -0.0213 494 GLU A C 3829 O O . GLU A 494 ? 0.4598 0.3752 0.3235 0.0289 0.0111 -0.0158 494 GLU A O 3830 C CB . GLU A 494 ? 0.5025 0.3866 0.3366 0.0392 0.0199 -0.0299 494 GLU A CB 3831 C CG . GLU A 494 ? 0.5217 0.3965 0.3411 0.0307 0.0086 -0.0313 494 GLU A CG 3832 C CD . GLU A 494 ? 0.5318 0.3906 0.3368 0.0312 0.0085 -0.0366 494 GLU A CD 3833 O OE1 . GLU A 494 ? 0.5395 0.3966 0.3468 0.0395 0.0174 -0.0378 494 GLU A OE1 3834 O OE2 . GLU A 494 ? 0.5337 0.3825 0.3258 0.0232 -0.0001 -0.0382 494 GLU A OE2 3835 N N . ALA A 495 ? 0.4567 0.3758 0.3403 0.0325 0.0225 -0.0238 495 ALA A N 3836 C CA . ALA A 495 ? 0.4453 0.3742 0.3438 0.0280 0.0208 -0.0211 495 ALA A CA 3837 C C . ALA A 495 ? 0.4415 0.3786 0.3502 0.0302 0.0255 -0.0128 495 ALA A C 3838 O O . ALA A 495 ? 0.4407 0.3857 0.3547 0.0278 0.0212 -0.0057 495 ALA A O 3839 C CB . ALA A 495 ? 0.4405 0.3725 0.3507 0.0264 0.0257 -0.0261 495 ALA A CB 3840 N N . LEU A 496 ? 0.4574 0.3936 0.3695 0.0351 0.0348 -0.0119 496 LEU A N 3841 C CA . LEU A 496 ? 0.4759 0.4182 0.3978 0.0387 0.0418 -0.0030 496 LEU A CA 3842 C C . LEU A 496 ? 0.4980 0.4466 0.4131 0.0393 0.0343 0.0061 496 LEU A C 3843 O O . LEU A 496 ? 0.5028 0.4624 0.4282 0.0405 0.0356 0.0167 496 LEU A O 3844 C CB . LEU A 496 ? 0.4852 0.4234 0.4108 0.0431 0.0534 -0.0040 496 LEU A CB 3845 C CG . LEU A 496 ? 0.4906 0.4247 0.4246 0.0396 0.0616 -0.0103 496 LEU A CG 3846 C CD1 . LEU A 496 ? 0.5076 0.4378 0.4436 0.0415 0.0714 -0.0106 496 LEU A CD1 3847 C CD2 . LEU A 496 ? 0.5087 0.4422 0.4516 0.0384 0.0675 -0.0072 496 LEU A CD2 3848 N N . ASN A 497 ? 0.5069 0.4483 0.4034 0.0383 0.0271 0.0031 497 ASN A N 3849 C CA A ASN A 497 ? 0.5199 0.4649 0.4037 0.0355 0.0175 0.0105 497 ASN A CA 3850 C CA B ASN A 497 ? 0.5248 0.4702 0.4092 0.0356 0.0178 0.0108 497 ASN A CA 3851 C C . ASN A 497 ? 0.5163 0.4706 0.4026 0.0271 0.0062 0.0156 497 ASN A C 3852 O O . ASN A 497 ? 0.5107 0.4801 0.4019 0.0248 0.0012 0.0281 497 ASN A O 3853 C CB A ASN A 497 ? 0.5426 0.4705 0.3992 0.0350 0.0129 0.0038 497 ASN A CB 3854 C CB B ASN A 497 ? 0.5553 0.4847 0.4133 0.0358 0.0138 0.0050 497 ASN A CB 3855 C CG A ASN A 497 ? 0.5674 0.4951 0.4044 0.0289 0.0014 0.0101 497 ASN A CG 3856 C CG B ASN A 497 ? 0.5692 0.4958 0.4262 0.0447 0.0242 0.0063 497 ASN A CG 3857 O OD1 A ASN A 497 ? 0.5984 0.5146 0.4147 0.0204 -0.0091 0.0060 497 ASN A OD1 3858 O OD1 B ASN A 497 ? 0.6043 0.5342 0.4536 0.0463 0.0227 0.0136 497 ASN A OD1 3859 N ND2 A ASN A 497 ? 0.5656 0.5057 0.4078 0.0321 0.0034 0.0206 497 ASN A ND2 3860 N ND2 B ASN A 497 ? 0.5724 0.4950 0.4383 0.0499 0.0344 0.0006 497 ASN A ND2 3861 N N . ASN A 498 ? 0.5045 0.4519 0.3885 0.0224 0.0021 0.0076 498 ASN A N 3862 C CA . ASN A 498 ? 0.5055 0.4616 0.3933 0.0140 -0.0082 0.0125 498 ASN A CA 3863 C C . ASN A 498 ? 0.4957 0.4705 0.4097 0.0170 -0.0022 0.0229 498 ASN A C 3864 O O . ASN A 498 ? 0.5061 0.4970 0.4274 0.0125 -0.0093 0.0352 498 ASN A O 3865 C CB . ASN A 498 ? 0.5106 0.4534 0.3893 0.0094 -0.0125 0.0015 498 ASN A CB 3866 C CG . ASN A 498 ? 0.5512 0.4736 0.4002 0.0052 -0.0194 -0.0054 498 ASN A CG 3867 O OD1 . ASN A 498 ? 0.5850 0.5042 0.4174 0.0016 -0.0253 -0.0013 498 ASN A OD1 3868 N ND2 . ASN A 498 ? 0.5554 0.4625 0.3954 0.0059 -0.0179 -0.0153 498 ASN A ND2 3869 N N . ARG A 499 ? 0.4891 0.4609 0.4157 0.0242 0.0112 0.0190 499 ARG A N 3870 C CA . ARG A 499 ? 0.5001 0.4826 0.4469 0.0286 0.0205 0.0280 499 ARG A CA 3871 C C . ARG A 499 ? 0.5520 0.5484 0.5087 0.0345 0.0259 0.0440 499 ARG A C 3872 O O . ARG A 499 ? 0.5523 0.5650 0.5229 0.0359 0.0264 0.0584 499 ARG A O 3873 C CB . ARG A 499 ? 0.4826 0.4530 0.4343 0.0329 0.0342 0.0188 499 ARG A CB 3874 C CG . ARG A 499 ? 0.4563 0.4194 0.4051 0.0279 0.0310 0.0076 499 ARG A CG 3875 C CD . ARG A 499 ? 0.4463 0.3990 0.3980 0.0296 0.0435 -0.0002 499 ARG A CD 3876 N NE . ARG A 499 ? 0.4330 0.3852 0.3945 0.0335 0.0553 0.0066 499 ARG A NE 3877 C CZ . ARG A 499 ? 0.4487 0.3883 0.4099 0.0351 0.0692 0.0028 499 ARG A CZ 3878 N NH1 . ARG A 499 ? 0.4549 0.3854 0.4094 0.0318 0.0716 -0.0068 499 ARG A NH1 3879 N NH2 . ARG A 499 ? 0.4638 0.3987 0.4301 0.0398 0.0816 0.0097 499 ARG A NH2 3880 N N . PHE A 500 ? 0.5991 0.5904 0.5499 0.0391 0.0311 0.0430 500 PHE A N 3881 C CA . PHE A 500 ? 0.6700 0.6733 0.6307 0.0466 0.0390 0.0582 500 PHE A CA 3882 C C . PHE A 500 ? 0.7478 0.7610 0.6970 0.0427 0.0265 0.0652 500 PHE A C 3883 O O . PHE A 500 ? 0.8242 0.8309 0.7640 0.0462 0.0293 0.0627 500 PHE A O 3884 C CB . PHE A 500 ? 0.6641 0.6536 0.6277 0.0548 0.0564 0.0534 500 PHE A CB 3885 C CG . PHE A 500 ? 0.6648 0.6409 0.6338 0.0554 0.0675 0.0449 500 PHE A CG 3886 C CD1 . PHE A 500 ? 0.6572 0.6384 0.6372 0.0572 0.0723 0.0525 500 PHE A CD1 3887 C CD2 . PHE A 500 ? 0.6769 0.6358 0.6388 0.0533 0.0729 0.0304 500 PHE A CD2 3888 C CE1 . PHE A 500 ? 0.6704 0.6360 0.6506 0.0569 0.0827 0.0440 500 PHE A CE1 3889 C CE2 . PHE A 500 ? 0.6785 0.6249 0.6422 0.0511 0.0815 0.0226 500 PHE A CE2 3890 C CZ . PHE A 500 ? 0.6869 0.6348 0.6579 0.0528 0.0866 0.0285 500 PHE A CZ 3891 N N . GLN A 501 ? 0.8220 0.8505 0.7707 0.0343 0.0121 0.0740 501 GLN A N 3892 C CA . GLN A 501 ? 0.8957 0.9350 0.8308 0.0265 -0.0025 0.0823 501 GLN A CA 3893 C C . GLN A 501 ? 0.9583 1.0293 0.9118 0.0248 -0.0072 0.1058 501 GLN A C 3894 O O . GLN A 501 ? 0.9615 1.0431 0.9289 0.0220 -0.0093 0.1115 501 GLN A O 3895 C CB . GLN A 501 ? 0.9133 0.9380 0.8238 0.0130 -0.0187 0.0697 501 GLN A CB 3896 C CG . GLN A 501 ? 0.9145 0.9405 0.8324 0.0064 -0.0241 0.0670 501 GLN A CG 3897 C CD . GLN A 501 ? 0.9343 0.9485 0.8276 -0.0086 -0.0412 0.0594 501 GLN A CD 3898 O OE1 . GLN A 501 ? 0.9864 1.0081 0.8660 -0.0197 -0.0549 0.0676 501 GLN A OE1 3899 N NE2 . GLN A 501 ? 0.9174 0.9125 0.8039 -0.0099 -0.0403 0.0445 501 GLN A NE2 3900 N N . ILE A 502 ? 0.9982 1.0866 0.9530 0.0269 -0.0086 0.1212 502 ILE A N 3901 C CA . ILE A 502 ? 1.0160 1.1402 0.9878 0.0236 -0.0160 0.1469 502 ILE A CA 3902 C C . ILE A 502 ? 1.0413 1.1711 0.9956 0.0030 -0.0402 0.1465 502 ILE A C 3903 O O . ILE A 502 ? 1.0817 1.1929 1.0056 -0.0069 -0.0514 0.1337 502 ILE A O 3904 C CB . ILE A 502 ? 1.0204 1.1650 0.9998 0.0321 -0.0103 0.1660 502 ILE A CB 3905 C CG1 . ILE A 502 ? 1.0521 1.1886 1.0022 0.0234 -0.0229 0.1597 502 ILE A CG1 3906 C CG2 . ILE A 502 ? 0.9847 1.1181 0.9789 0.0514 0.0150 0.1651 502 ILE A CG2 3907 C CD1 . ILE A 502 ? 1.0552 1.2112 1.0118 0.0321 -0.0171 0.1779 502 ILE A CD1 3908 N N . LYS A 503 ? 1.0358 1.1888 1.0077 -0.0031 -0.0470 0.1607 503 LYS A N 3909 C CA . LYS A 503 ? 1.0431 1.1987 1.0001 -0.0241 -0.0690 0.1594 503 LYS A CA 3910 C C . LYS A 503 ? 1.0512 1.2452 1.0139 -0.0372 -0.0857 0.1857 503 LYS A C 3911 O O . LYS A 503 ? 1.0656 1.2819 1.0376 -0.0306 -0.0821 0.2029 503 LYS A O 3912 C CB . LYS A 503 ? 1.0240 1.1779 0.9961 -0.0243 -0.0664 0.1560 503 LYS A CB 3913 C CG . LYS A 503 ? 1.0056 1.1222 0.9668 -0.0176 -0.0558 0.1292 503 LYS A CG 3914 C CD . LYS A 503 ? 0.9918 1.1110 0.9712 -0.0154 -0.0511 0.1292 503 LYS A CD 3915 C CE . LYS A 503 ? 0.9831 1.0706 0.9432 -0.0208 -0.0540 0.1048 503 LYS A CE 3916 N NZ . LYS A 503 ? 0.9694 1.0643 0.9430 -0.0250 -0.0567 0.1081 503 LYS A NZ # _database_PDB_caveat.id 1 _database_PDB_caveat.text 'NAG A 1133 WRONG CHIRALITY AT ATOM C1' # 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 LYS 2 2 ? ? ? A . n A 1 3 LEU 3 3 ? ? ? A . n A 1 4 PRO 4 4 ? ? ? A . n A 1 5 GLY 5 5 ? ? ? A . n A 1 6 ASN 6 6 ? ? ? A . n A 1 7 ASP 7 7 ? ? ? A . n A 1 8 ASN 8 8 8 ASN ASN A . n A 1 9 SER 9 9 9 SER SER A . n A 1 10 THR 10 10 10 THR THR A . n A 1 11 ALA 11 11 11 ALA ALA A . n A 1 12 THR 12 12 12 THR THR A . n A 1 13 LEU 13 13 13 LEU LEU A . n A 1 14 CYS 14 14 14 CYS CYS A . n A 1 15 LEU 15 15 15 LEU LEU A . n A 1 16 GLY 16 16 16 GLY GLY A . n A 1 17 HIS 17 17 17 HIS HIS A . n A 1 18 HIS 18 18 18 HIS HIS A . n A 1 19 ALA 19 19 19 ALA ALA A . n A 1 20 VAL 20 20 20 VAL VAL A . n A 1 21 PRO 21 21 21 PRO PRO A . n A 1 22 ASN 22 22 22 ASN ASN A . n A 1 23 GLY 23 23 23 GLY GLY A . n A 1 24 THR 24 24 24 THR THR A . n A 1 25 ILE 25 25 25 ILE ILE A . n A 1 26 VAL 26 26 26 VAL VAL A . n A 1 27 LYS 27 27 27 LYS LYS A . n A 1 28 THR 28 28 28 THR THR A . n A 1 29 ILE 29 29 29 ILE ILE A . n A 1 30 THR 30 30 30 THR THR A . n A 1 31 ASN 31 31 31 ASN ASN A . n A 1 32 ASP 32 32 32 ASP ASP A . n A 1 33 GLN 33 33 33 GLN GLN A . n A 1 34 ILE 34 34 34 ILE ILE A . n A 1 35 GLU 35 35 35 GLU GLU A . n A 1 36 VAL 36 36 36 VAL VAL A . n A 1 37 THR 37 37 37 THR THR A . n A 1 38 ASN 38 38 38 ASN ASN A . n A 1 39 ALA 39 39 39 ALA ALA A . n A 1 40 THR 40 40 40 THR THR A . n A 1 41 GLU 41 41 41 GLU GLU A . n A 1 42 LEU 42 42 42 LEU LEU A . n A 1 43 VAL 43 43 43 VAL VAL A . n A 1 44 GLN 44 44 44 GLN GLN A . n A 1 45 SER 45 45 45 SER SER A . n A 1 46 SER 46 46 46 SER SER A . n A 1 47 SER 47 47 47 SER SER A . n A 1 48 THR 48 48 48 THR THR A . n A 1 49 GLY 49 49 49 GLY GLY A . n A 1 50 GLY 50 50 50 GLY GLY A . n A 1 51 ILE 51 51 51 ILE ILE A . n A 1 52 CYS 52 52 52 CYS CYS A . n A 1 53 ASP 53 53 53 ASP ASP A . n A 1 54 SER 54 54 54 SER SER A . n A 1 55 PRO 55 55 55 PRO PRO A . n A 1 56 HIS 56 56 56 HIS HIS A . n A 1 57 GLN 57 57 57 GLN GLN A . n A 1 58 ILE 58 58 58 ILE ILE A . n A 1 59 LEU 59 59 59 LEU LEU A . n A 1 60 ASP 60 60 60 ASP ASP A . n A 1 61 GLY 61 61 61 GLY GLY A . n A 1 62 GLU 62 62 62 GLU GLU A . n A 1 63 ASN 63 63 63 ASN ASN A . n A 1 64 CYS 64 64 64 CYS CYS A . n A 1 65 THR 65 65 65 THR THR A . n A 1 66 LEU 66 66 66 LEU LEU A . n A 1 67 ILE 67 67 67 ILE ILE A . n A 1 68 ASP 68 68 68 ASP ASP A . n A 1 69 ALA 69 69 69 ALA ALA A . n A 1 70 LEU 70 70 70 LEU LEU A . n A 1 71 LEU 71 71 71 LEU LEU A . n A 1 72 GLY 72 72 72 GLY GLY A . n A 1 73 ASP 73 73 73 ASP ASP A . n A 1 74 PRO 74 74 74 PRO PRO A . n A 1 75 GLN 75 75 75 GLN GLN A . n A 1 76 CYS 76 76 76 CYS CYS A . n A 1 77 ASP 77 77 77 ASP ASP A . n A 1 78 GLY 78 78 78 GLY GLY A . n A 1 79 PHE 79 79 79 PHE PHE A . n A 1 80 GLN 80 80 80 GLN GLN A . n A 1 81 ASN 81 81 81 ASN ASN A . n A 1 82 LYS 82 82 82 LYS LYS A . n A 1 83 LYS 83 83 83 LYS LYS A . n A 1 84 TRP 84 84 84 TRP TRP A . n A 1 85 ASP 85 85 85 ASP ASP A . n A 1 86 LEU 86 86 86 LEU LEU A . n A 1 87 PHE 87 87 87 PHE PHE A . n A 1 88 VAL 88 88 88 VAL VAL A . n A 1 89 GLU 89 89 89 GLU GLU A . n A 1 90 ARG 90 90 90 ARG ARG A . n A 1 91 SER 91 91 91 SER SER A . n A 1 92 LYS 92 92 92 LYS LYS A . n A 1 93 ALA 93 93 93 ALA ALA A . n A 1 94 TYR 94 94 94 TYR TYR A . n A 1 95 SER 95 95 95 SER SER A . n A 1 96 ASN 96 96 96 ASN ASN A . n A 1 97 CYS 97 97 97 CYS CYS A . n A 1 98 TYR 98 98 98 TYR TYR A . n A 1 99 PRO 99 99 99 PRO PRO A . n A 1 100 TYR 100 100 100 TYR TYR A . n A 1 101 ASP 101 101 101 ASP ASP A . n A 1 102 VAL 102 102 102 VAL VAL A . n A 1 103 PRO 103 103 103 PRO PRO A . n A 1 104 ASP 104 104 104 ASP ASP A . n A 1 105 TYR 105 105 105 TYR TYR A . n A 1 106 ALA 106 106 106 ALA ALA A . n A 1 107 SER 107 107 107 SER SER A . n A 1 108 LEU 108 108 108 LEU LEU A . n A 1 109 ARG 109 109 109 ARG ARG A . n A 1 110 SER 110 110 110 SER SER A . n A 1 111 LEU 111 111 111 LEU LEU A . n A 1 112 VAL 112 112 112 VAL VAL A . n A 1 113 ALA 113 113 113 ALA ALA A . n A 1 114 SER 114 114 114 SER SER A . n A 1 115 SER 115 115 115 SER SER A . n A 1 116 GLY 116 116 116 GLY GLY A . n A 1 117 THR 117 117 117 THR THR A . n A 1 118 LEU 118 118 118 LEU LEU A . n A 1 119 GLU 119 119 119 GLU GLU A . n A 1 120 PHE 120 120 120 PHE PHE A . n A 1 121 ASN 121 121 121 ASN ASN A . n A 1 122 ASN 122 122 122 ASN ASN A . n A 1 123 GLU 123 123 123 GLU GLU A . n A 1 124 SER 124 124 124 SER SER A . n A 1 125 PHE 125 125 125 PHE PHE A . n A 1 126 ASN 126 126 126 ASN ASN A . n A 1 127 TRP 127 127 127 TRP TRP A . n A 1 128 THR 128 128 128 THR THR A . n A 1 129 GLY 129 129 129 GLY GLY A . n A 1 130 VAL 130 130 130 VAL VAL A . n A 1 131 THR 131 131 131 THR THR A . n A 1 132 GLN 132 132 132 GLN GLN A . n A 1 133 ASN 133 133 133 ASN ASN A . n A 1 134 GLY 134 134 134 GLY GLY A . n A 1 135 THR 135 135 135 THR THR A . n A 1 136 SER 136 136 136 SER SER A . n A 1 137 SER 137 137 137 SER SER A . n A 1 138 ALA 138 138 138 ALA ALA A . n A 1 139 CYS 139 139 139 CYS CYS A . n A 1 140 LYS 140 140 140 LYS LYS A . n A 1 141 ARG 141 141 141 ARG ARG A . n A 1 142 LYS 142 142 142 LYS LYS A . n A 1 143 SER 143 143 143 SER SER A . n A 1 144 ASN 144 144 144 ASN ASN A . n A 1 145 ASN 145 145 145 ASN ASN A . n A 1 146 SER 146 146 146 SER SER A . n A 1 147 PHE 147 147 147 PHE PHE A . n A 1 148 PHE 148 148 148 PHE PHE A . n A 1 149 SER 149 149 149 SER SER A . n A 1 150 ARG 150 150 150 ARG ARG A . n A 1 151 LEU 151 151 151 LEU LEU A . n A 1 152 ASN 152 152 152 ASN ASN A . n A 1 153 TRP 153 153 153 TRP TRP A . n A 1 154 LEU 154 154 154 LEU LEU A . n A 1 155 THR 155 155 155 THR THR A . n A 1 156 HIS 156 156 156 HIS HIS A . n A 1 157 LEU 157 157 157 LEU LEU A . n A 1 158 LYS 158 158 158 LYS LYS A . n A 1 159 PHE 159 159 159 PHE PHE A . n A 1 160 LYS 160 160 160 LYS LYS A . n A 1 161 TYR 161 161 161 TYR TYR A . n A 1 162 PRO 162 162 162 PRO PRO A . n A 1 163 ALA 163 163 163 ALA ALA A . n A 1 164 LEU 164 164 164 LEU LEU A . n A 1 165 ASN 165 165 165 ASN ASN A . n A 1 166 VAL 166 166 166 VAL VAL A . n A 1 167 THR 167 167 167 THR THR A . n A 1 168 MET 168 168 168 MET MET A . n A 1 169 PRO 169 169 169 PRO PRO A . n A 1 170 ASN 170 170 170 ASN ASN A . n A 1 171 ASN 171 171 171 ASN ASN A . n A 1 172 GLU 172 172 172 GLU GLU A . n A 1 173 LYS 173 173 173 LYS LYS A . n A 1 174 PHE 174 174 174 PHE PHE A . n A 1 175 ASP 175 175 175 ASP ASP A . n A 1 176 LYS 176 176 176 LYS LYS A . n A 1 177 LEU 177 177 177 LEU LEU A . n A 1 178 TYR 178 178 178 TYR TYR A . n A 1 179 ILE 179 179 179 ILE ILE A . n A 1 180 TRP 180 180 180 TRP TRP A . n A 1 181 GLY 181 181 181 GLY GLY A . n A 1 182 VAL 182 182 182 VAL VAL A . n A 1 183 HIS 183 183 183 HIS HIS A . n A 1 184 HIS 184 184 184 HIS HIS A . n A 1 185 PRO 185 185 185 PRO PRO A . n A 1 186 GLY 186 186 186 GLY GLY A . n A 1 187 THR 187 187 187 THR THR A . n A 1 188 ASP 188 188 188 ASP ASP A . n A 1 189 ASN 189 189 189 ASN ASN A . n A 1 190 ASP 190 190 190 ASP ASP A . n A 1 191 GLN 191 191 191 GLN GLN A . n A 1 192 ILE 192 192 192 ILE ILE A . n A 1 193 PHE 193 193 193 PHE PHE A . n A 1 194 LEU 194 194 194 LEU LEU A . n A 1 195 TYR 195 195 195 TYR TYR A . n A 1 196 ALA 196 196 196 ALA ALA A . n A 1 197 GLN 197 197 197 GLN GLN A . n A 1 198 ALA 198 198 198 ALA ALA A . n A 1 199 SER 199 199 199 SER SER A . n A 1 200 GLY 200 200 200 GLY GLY A . n A 1 201 ARG 201 201 201 ARG ARG A . n A 1 202 ILE 202 202 202 ILE ILE A . n A 1 203 THR 203 203 203 THR THR A . n A 1 204 VAL 204 204 204 VAL VAL A . n A 1 205 SER 205 205 205 SER SER A . n A 1 206 THR 206 206 206 THR THR A . n A 1 207 LYS 207 207 207 LYS LYS A . n A 1 208 ARG 208 208 208 ARG ARG A . n A 1 209 SER 209 209 209 SER SER A . n A 1 210 GLN 210 210 210 GLN GLN A . n A 1 211 GLN 211 211 211 GLN GLN A . n A 1 212 THR 212 212 212 THR THR A . n A 1 213 VAL 213 213 213 VAL VAL A . n A 1 214 ILE 214 214 214 ILE ILE A . n A 1 215 PRO 215 215 215 PRO PRO A . n A 1 216 ASN 216 216 216 ASN ASN A . n A 1 217 ILE 217 217 217 ILE ILE A . n A 1 218 GLY 218 218 218 GLY GLY A . n A 1 219 SER 219 219 219 SER SER A . n A 1 220 ARG 220 220 220 ARG ARG A . n A 1 221 PRO 221 221 221 PRO PRO A . n A 1 222 ARG 222 222 222 ARG ARG A . n A 1 223 VAL 223 223 223 VAL VAL A . n A 1 224 ARG 224 224 224 ARG ARG A . n A 1 225 ASN 225 225 225 ASN ASN A . n A 1 226 ILE 226 226 226 ILE ILE A . n A 1 227 PRO 227 227 227 PRO PRO A . n A 1 228 SER 228 228 228 SER SER A . n A 1 229 ARG 229 229 229 ARG ARG A . n A 1 230 ILE 230 230 230 ILE ILE A . n A 1 231 SER 231 231 231 SER SER A . n A 1 232 ILE 232 232 232 ILE ILE A . n A 1 233 TYR 233 233 233 TYR TYR A . n A 1 234 TRP 234 234 234 TRP TRP A . n A 1 235 THR 235 235 235 THR THR A . n A 1 236 ILE 236 236 236 ILE ILE A . n A 1 237 VAL 237 237 237 VAL VAL A . n A 1 238 LYS 238 238 238 LYS LYS A . n A 1 239 PRO 239 239 239 PRO PRO A . n A 1 240 GLY 240 240 240 GLY GLY A . n A 1 241 ASP 241 241 241 ASP ASP A . n A 1 242 ILE 242 242 242 ILE ILE A . n A 1 243 LEU 243 243 243 LEU LEU A . n A 1 244 LEU 244 244 244 LEU LEU A . n A 1 245 ILE 245 245 245 ILE ILE A . n A 1 246 ASN 246 246 246 ASN ASN A . n A 1 247 SER 247 247 247 SER SER A . n A 1 248 THR 248 248 248 THR THR A . n A 1 249 GLY 249 249 249 GLY GLY A . n A 1 250 ASN 250 250 250 ASN ASN A . n A 1 251 LEU 251 251 251 LEU LEU A . n A 1 252 ILE 252 252 252 ILE ILE A . n A 1 253 ALA 253 253 253 ALA ALA A . n A 1 254 PRO 254 254 254 PRO PRO A . n A 1 255 ARG 255 255 255 ARG ARG A . n A 1 256 GLY 256 256 256 GLY GLY A . n A 1 257 TYR 257 257 257 TYR TYR A . n A 1 258 PHE 258 258 258 PHE PHE A . n A 1 259 LYS 259 259 259 LYS LYS A . n A 1 260 ILE 260 260 260 ILE ILE A . n A 1 261 ARG 261 261 261 ARG ARG A . n A 1 262 SER 262 262 262 SER SER A . n A 1 263 GLY 263 263 263 GLY GLY A . n A 1 264 LYS 264 264 264 LYS LYS A . n A 1 265 SER 265 265 265 SER SER A . n A 1 266 SER 266 266 266 SER SER A . n A 1 267 ILE 267 267 267 ILE ILE A . n A 1 268 MET 268 268 268 MET MET A . n A 1 269 ARG 269 269 269 ARG ARG A . n A 1 270 SER 270 270 270 SER SER A . n A 1 271 ASP 271 271 271 ASP ASP A . n A 1 272 ALA 272 272 272 ALA ALA A . n A 1 273 PRO 273 273 273 PRO PRO A . n A 1 274 ILE 274 274 274 ILE ILE A . n A 1 275 GLY 275 275 275 GLY GLY A . n A 1 276 LYS 276 276 276 LYS LYS A . n A 1 277 CYS 277 277 277 CYS CYS A . n A 1 278 ASN 278 278 278 ASN ASN A . n A 1 279 SER 279 279 279 SER SER A . n A 1 280 GLU 280 280 280 GLU GLU A . n A 1 281 CYS 281 281 281 CYS CYS A . n A 1 282 ILE 282 282 282 ILE ILE A . n A 1 283 THR 283 283 283 THR THR A . n A 1 284 PRO 284 284 284 PRO PRO A . n A 1 285 ASN 285 285 285 ASN ASN A . n A 1 286 GLY 286 286 286 GLY GLY A . n A 1 287 SER 287 287 287 SER SER A . n A 1 288 ILE 288 288 288 ILE ILE A . n A 1 289 PRO 289 289 289 PRO PRO A . n A 1 290 ASN 290 290 290 ASN ASN A . n A 1 291 ASP 291 291 291 ASP ASP A . n A 1 292 LYS 292 292 292 LYS LYS A . n A 1 293 PRO 293 293 293 PRO PRO A . n A 1 294 PHE 294 294 294 PHE PHE A . n A 1 295 GLN 295 295 295 GLN GLN A . n A 1 296 ASN 296 296 296 ASN ASN A . n A 1 297 VAL 297 297 297 VAL VAL A . n A 1 298 ASN 298 298 298 ASN ASN A . n A 1 299 ARG 299 299 299 ARG ARG A . n A 1 300 ILE 300 300 300 ILE ILE A . n A 1 301 THR 301 301 301 THR THR A . n A 1 302 TYR 302 302 302 TYR TYR A . n A 1 303 GLY 303 303 303 GLY GLY A . n A 1 304 ALA 304 304 304 ALA ALA A . n A 1 305 CYS 305 305 305 CYS CYS A . n A 1 306 PRO 306 306 306 PRO PRO A . n A 1 307 ARG 307 307 307 ARG ARG A . n A 1 308 TYR 308 308 308 TYR TYR A . n A 1 309 VAL 309 309 309 VAL VAL A . n A 1 310 LYS 310 310 310 LYS LYS A . n A 1 311 GLN 311 311 311 GLN GLN A . n A 1 312 ASN 312 312 312 ASN ASN A . n A 1 313 THR 313 313 313 THR THR A . n A 1 314 LEU 314 314 314 LEU LEU A . n A 1 315 LYS 315 315 315 LYS LYS A . n A 1 316 LEU 316 316 316 LEU LEU A . n A 1 317 ALA 317 317 317 ALA ALA A . n A 1 318 THR 318 318 318 THR THR A . n A 1 319 GLY 319 319 319 GLY GLY A . n A 1 320 MET 320 320 320 MET MET 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 VAL 323 323 323 VAL VAL A . n A 1 324 PRO 324 324 324 PRO PRO A . n A 1 325 GLU 325 325 325 GLU GLU A . n A 1 326 LYS 326 326 326 LYS LYS A . n A 1 327 GLN 327 327 327 GLN GLN A . n A 1 328 THR 328 328 ? ? ? A . n A 1 329 GLN 329 329 ? ? ? A . n A 1 330 GLY 330 330 ? ? ? A . n A 1 331 ILE 331 331 ? ? ? A . n A 1 332 PHE 332 332 ? ? ? A . n A 1 333 GLY 333 333 ? ? ? A . n A 1 334 ALA 334 334 334 ALA ALA A . n A 1 335 ILE 335 335 335 ILE ILE A . n A 1 336 ALA 336 336 336 ALA ALA A . n A 1 337 GLY 337 337 337 GLY GLY A . n A 1 338 PHE 338 338 338 PHE PHE A . n A 1 339 ILE 339 339 339 ILE ILE A . n A 1 340 GLU 340 340 340 GLU GLU A . n A 1 341 ASN 341 341 341 ASN ASN A . n A 1 342 GLY 342 342 342 GLY GLY A . n A 1 343 TRP 343 343 343 TRP TRP A . n A 1 344 GLU 344 344 344 GLU GLU A . n A 1 345 GLY 345 345 345 GLY GLY A . n A 1 346 MET 346 346 346 MET MET A . n A 1 347 VAL 347 347 347 VAL VAL A . n A 1 348 ASP 348 348 348 ASP ASP A . n A 1 349 GLY 349 349 349 GLY GLY A . n A 1 350 TRP 350 350 350 TRP TRP A . n A 1 351 TYR 351 351 351 TYR TYR A . n A 1 352 GLY 352 352 352 GLY GLY A . n A 1 353 PHE 353 353 353 PHE PHE A . n A 1 354 ARG 354 354 354 ARG ARG A . n A 1 355 HIS 355 355 355 HIS HIS A . n A 1 356 GLN 356 356 356 GLN GLN A . n A 1 357 ASN 357 357 357 ASN ASN A . n A 1 358 SER 358 358 358 SER SER A . n A 1 359 GLU 359 359 359 GLU GLU A . n A 1 360 GLY 360 360 360 GLY GLY A . n A 1 361 ILE 361 361 361 ILE ILE A . n A 1 362 GLY 362 362 362 GLY GLY A . n A 1 363 GLN 363 363 363 GLN GLN A . n A 1 364 ALA 364 364 364 ALA ALA 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 LEU 367 367 367 LEU LEU A . n A 1 368 LYS 368 368 368 LYS LYS A . n A 1 369 SER 369 369 369 SER SER A . n A 1 370 THR 370 370 370 THR THR A . n A 1 371 GLN 371 371 371 GLN GLN A . n A 1 372 ALA 372 372 372 ALA ALA A . n A 1 373 ALA 373 373 373 ALA ALA A . n A 1 374 ILE 374 374 374 ILE ILE A . n A 1 375 ASN 375 375 375 ASN ASN A . n A 1 376 GLN 376 376 376 GLN GLN A . n A 1 377 ILE 377 377 377 ILE ILE A . n A 1 378 ASN 378 378 378 ASN ASN A . n A 1 379 GLY 379 379 379 GLY GLY A . n A 1 380 LYS 380 380 380 LYS LYS A . n A 1 381 LEU 381 381 381 LEU LEU A . n A 1 382 ASN 382 382 382 ASN ASN A . n A 1 383 ARG 383 383 383 ARG ARG A . n A 1 384 LEU 384 384 384 LEU LEU A . n A 1 385 ILE 385 385 385 ILE ILE A . n A 1 386 GLY 386 386 386 GLY GLY A . n A 1 387 LYS 387 387 387 LYS LYS A . n A 1 388 THR 388 388 388 THR THR A . n A 1 389 ASN 389 389 389 ASN ASN A . n A 1 390 GLU 390 390 390 GLU GLU A . n A 1 391 LYS 391 391 391 LYS LYS A . n A 1 392 PHE 392 392 392 PHE PHE A . n A 1 393 HIS 393 393 393 HIS HIS A . n A 1 394 GLN 394 394 394 GLN GLN A . n A 1 395 ILE 395 395 395 ILE ILE A . n A 1 396 GLU 396 396 396 GLU GLU A . n A 1 397 LYS 397 397 397 LYS LYS A . n A 1 398 GLU 398 398 398 GLU GLU A . n A 1 399 PHE 399 399 399 PHE PHE A . n A 1 400 SER 400 400 400 SER SER A . n A 1 401 GLU 401 401 401 GLU GLU A . n A 1 402 VAL 402 402 402 VAL VAL A . n A 1 403 GLU 403 403 403 GLU GLU A . n A 1 404 GLY 404 404 404 GLY GLY A . n A 1 405 ARG 405 405 405 ARG ARG A . n A 1 406 ILE 406 406 406 ILE ILE A . n A 1 407 GLN 407 407 407 GLN GLN A . n A 1 408 ASP 408 408 408 ASP ASP A . n A 1 409 LEU 409 409 409 LEU LEU A . n A 1 410 GLU 410 410 410 GLU GLU A . n A 1 411 LYS 411 411 411 LYS LYS A . n A 1 412 TYR 412 412 412 TYR TYR A . n A 1 413 VAL 413 413 413 VAL VAL A . n A 1 414 GLU 414 414 414 GLU GLU A . n A 1 415 ASP 415 415 415 ASP ASP A . n A 1 416 THR 416 416 416 THR THR A . n A 1 417 LYS 417 417 417 LYS LYS A . n A 1 418 ILE 418 418 418 ILE ILE A . n A 1 419 ASP 419 419 419 ASP ASP A . n A 1 420 LEU 420 420 420 LEU LEU A . n A 1 421 TRP 421 421 421 TRP TRP A . n A 1 422 SER 422 422 422 SER SER A . n A 1 423 TYR 423 423 423 TYR TYR A . n A 1 424 ASN 424 424 424 ASN ASN A . n A 1 425 ALA 425 425 425 ALA ALA A . n A 1 426 GLU 426 426 426 GLU GLU A . n A 1 427 LEU 427 427 427 LEU LEU A . n A 1 428 LEU 428 428 428 LEU LEU A . n A 1 429 VAL 429 429 429 VAL VAL A . n A 1 430 ALA 430 430 430 ALA ALA A . n A 1 431 LEU 431 431 431 LEU LEU A . n A 1 432 GLU 432 432 432 GLU GLU A . n A 1 433 ASN 433 433 433 ASN ASN A . n A 1 434 GLN 434 434 434 GLN GLN A . n A 1 435 HIS 435 435 435 HIS HIS A . n A 1 436 THR 436 436 436 THR THR A . n A 1 437 ILE 437 437 437 ILE ILE A . n A 1 438 ASP 438 438 438 ASP ASP A . n A 1 439 LEU 439 439 439 LEU LEU A . n A 1 440 THR 440 440 440 THR THR A . n A 1 441 ASP 441 441 441 ASP ASP A . n A 1 442 SER 442 442 442 SER SER A . n A 1 443 GLU 443 443 443 GLU GLU A . n A 1 444 MET 444 444 444 MET MET A . n A 1 445 ASN 445 445 445 ASN ASN A . n A 1 446 LYS 446 446 446 LYS LYS A . n A 1 447 LEU 447 447 447 LEU LEU A . n A 1 448 PHE 448 448 448 PHE PHE A . n A 1 449 GLU 449 449 449 GLU GLU A . n A 1 450 ARG 450 450 450 ARG ARG A . n A 1 451 THR 451 451 451 THR THR A . n A 1 452 LYS 452 452 452 LYS LYS A . n A 1 453 LYS 453 453 453 LYS LYS A . n A 1 454 GLN 454 454 454 GLN GLN A . n A 1 455 LEU 455 455 455 LEU LEU A . n A 1 456 ARG 456 456 456 ARG ARG A . n A 1 457 GLU 457 457 457 GLU GLU A . n A 1 458 ASN 458 458 458 ASN ASN A . n A 1 459 ALA 459 459 459 ALA ALA A . n A 1 460 GLU 460 460 460 GLU GLU A . n A 1 461 ASP 461 461 461 ASP ASP A . n A 1 462 MET 462 462 462 MET MET A . n A 1 463 GLY 463 463 463 GLY GLY A . n A 1 464 ASN 464 464 464 ASN ASN A . n A 1 465 GLY 465 465 465 GLY GLY A . n A 1 466 CYS 466 466 466 CYS CYS A . n A 1 467 PHE 467 467 467 PHE PHE A . n A 1 468 LYS 468 468 468 LYS LYS A . n A 1 469 ILE 469 469 469 ILE ILE A . n A 1 470 TYR 470 470 470 TYR TYR A . n A 1 471 HIS 471 471 471 HIS HIS A . n A 1 472 LYS 472 472 472 LYS LYS A . n A 1 473 CYS 473 473 473 CYS CYS A . n A 1 474 ASP 474 474 474 ASP ASP A . n A 1 475 ASN 475 475 475 ASN ASN A . n A 1 476 ALA 476 476 476 ALA ALA A . n A 1 477 CYS 477 477 477 CYS CYS A . n A 1 478 ILE 478 478 478 ILE ILE A . n A 1 479 GLY 479 479 479 GLY GLY A . n A 1 480 SER 480 480 480 SER SER A . n A 1 481 ILE 481 481 481 ILE ILE A . n A 1 482 ARG 482 482 482 ARG ARG A . n A 1 483 ASN 483 483 483 ASN ASN A . n A 1 484 GLY 484 484 484 GLY GLY A . n A 1 485 THR 485 485 485 THR THR A . n A 1 486 TYR 486 486 486 TYR TYR A . n A 1 487 ASP 487 487 487 ASP ASP A . n A 1 488 HIS 488 488 488 HIS HIS A . n A 1 489 ASP 489 489 489 ASP ASP A . n A 1 490 VAL 490 490 490 VAL VAL A . n A 1 491 TYR 491 491 491 TYR TYR A . n A 1 492 ARG 492 492 492 ARG ARG A . n A 1 493 ASP 493 493 493 ASP ASP A . n A 1 494 GLU 494 494 494 GLU GLU A . n A 1 495 ALA 495 495 495 ALA ALA A . n A 1 496 LEU 496 496 496 LEU LEU A . n A 1 497 ASN 497 497 497 ASN ASN A . n A 1 498 ASN 498 498 498 ASN ASN A . n A 1 499 ARG 499 499 499 ARG ARG A . n A 1 500 PHE 500 500 500 PHE PHE A . n A 1 501 GLN 501 501 501 GLN GLN A . n A 1 502 ILE 502 502 502 ILE ILE A . n A 1 503 LYS 503 503 503 LYS LYS 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 1038 1038 NAG NAG A . C 2 NAG 1 1063 1063 NAG NAG A . D 2 NAG 1 1126 1126 NAG NAG A . E 2 NAG 1 1133 1133 NAG NAG A . F 2 NAG 1 1165 1165 NAG NAG A . G 2 NAG 2 1166 1166 NAG NAG A . H 3 MAN 3 1167 1167 MAN MAN A . I 2 NAG 1 1246 1246 NAG NAG A . J 2 NAG 2 1247 1247 NAG NAG A . K 2 NAG 1 1285 1285 NAG NAG A . L 2 NAG 1 1483 1483 NAG NAG A . M 4 EPE 1 1504 1504 EPE EPE A . N 4 EPE 1 1505 1505 EPE EPE A . O 4 EPE 1 1506 1506 EPE EPE A . P 5 TAM 1 1507 1507 TAM TAM A . Q 6 SIA 1 1508 1508 SIA SIA A . R 7 HOH 1 2001 2001 HOH HOH A . R 7 HOH 2 2002 2002 HOH HOH A . R 7 HOH 3 2003 2003 HOH HOH A . R 7 HOH 4 2004 2004 HOH HOH A . R 7 HOH 5 2005 2005 HOH HOH A . R 7 HOH 6 2006 2006 HOH HOH A . R 7 HOH 7 2007 2007 HOH HOH A . R 7 HOH 8 2008 2008 HOH HOH A . R 7 HOH 9 2009 2009 HOH HOH A . R 7 HOH 10 2010 2010 HOH HOH A . R 7 HOH 11 2011 2011 HOH HOH A . R 7 HOH 12 2012 2012 HOH HOH A . R 7 HOH 13 2013 2013 HOH HOH A . R 7 HOH 14 2014 2014 HOH HOH A . R 7 HOH 15 2015 2015 HOH HOH A . R 7 HOH 16 2016 2016 HOH HOH A . R 7 HOH 17 2017 2017 HOH HOH A . R 7 HOH 18 2018 2018 HOH HOH A . R 7 HOH 19 2019 2019 HOH HOH A . R 7 HOH 20 2020 2020 HOH HOH A . R 7 HOH 21 2021 2021 HOH HOH A . R 7 HOH 22 2022 2022 HOH HOH A . R 7 HOH 23 2023 2023 HOH HOH A . R 7 HOH 24 2024 2024 HOH HOH A . R 7 HOH 25 2025 2025 HOH HOH A . R 7 HOH 26 2026 2026 HOH HOH A . R 7 HOH 27 2027 2027 HOH HOH A . R 7 HOH 28 2028 2028 HOH HOH A . R 7 HOH 29 2029 2029 HOH HOH A . R 7 HOH 30 2030 2030 HOH HOH A . R 7 HOH 31 2031 2031 HOH HOH A . R 7 HOH 32 2032 2032 HOH HOH A . R 7 HOH 33 2033 2033 HOH HOH A . R 7 HOH 34 2034 2034 HOH HOH A . R 7 HOH 35 2035 2035 HOH HOH A . R 7 HOH 36 2036 2036 HOH HOH A . R 7 HOH 37 2037 2037 HOH HOH A . R 7 HOH 38 2038 2038 HOH HOH A . R 7 HOH 39 2039 2039 HOH HOH A . R 7 HOH 40 2040 2040 HOH HOH A . R 7 HOH 41 2041 2041 HOH HOH A . R 7 HOH 42 2042 2042 HOH HOH A . R 7 HOH 43 2043 2043 HOH HOH A . R 7 HOH 44 2044 2044 HOH HOH A . R 7 HOH 45 2045 2045 HOH HOH A . R 7 HOH 46 2046 2046 HOH HOH A . R 7 HOH 47 2047 2047 HOH HOH A . R 7 HOH 48 2048 2048 HOH HOH A . R 7 HOH 49 2049 2049 HOH HOH A . R 7 HOH 50 2050 2050 HOH HOH A . R 7 HOH 51 2051 2051 HOH HOH A . R 7 HOH 52 2052 2052 HOH HOH A . R 7 HOH 53 2053 2053 HOH HOH A . R 7 HOH 54 2054 2054 HOH HOH A . R 7 HOH 55 2055 2055 HOH HOH A . R 7 HOH 56 2056 2056 HOH HOH A . R 7 HOH 57 2057 2057 HOH HOH A . R 7 HOH 58 2058 2058 HOH HOH A . R 7 HOH 59 2059 2059 HOH HOH A . R 7 HOH 60 2060 2060 HOH HOH A . R 7 HOH 61 2061 2061 HOH HOH A . R 7 HOH 62 2062 2062 HOH HOH A . R 7 HOH 63 2063 2063 HOH HOH A . R 7 HOH 64 2064 2064 HOH HOH A . R 7 HOH 65 2065 2065 HOH HOH A . R 7 HOH 66 2066 2066 HOH HOH A . R 7 HOH 67 2067 2067 HOH HOH A . R 7 HOH 68 2068 2068 HOH HOH A . R 7 HOH 69 2069 2069 HOH HOH A . R 7 HOH 70 2070 2070 HOH HOH A . R 7 HOH 71 2071 2071 HOH HOH A . R 7 HOH 72 2072 2072 HOH HOH A . R 7 HOH 73 2073 2073 HOH HOH A . R 7 HOH 74 2074 2074 HOH HOH A . R 7 HOH 75 2075 2075 HOH HOH A . R 7 HOH 76 2076 2076 HOH HOH A . R 7 HOH 77 2077 2077 HOH HOH A . R 7 HOH 78 2078 2078 HOH HOH A . R 7 HOH 79 2079 2079 HOH HOH A . R 7 HOH 80 2080 2080 HOH HOH A . R 7 HOH 81 2081 2081 HOH HOH A . R 7 HOH 82 2082 2082 HOH HOH A . R 7 HOH 83 2083 2083 HOH HOH A . R 7 HOH 84 2084 2084 HOH HOH A . R 7 HOH 85 2085 2085 HOH HOH A . R 7 HOH 86 2086 2086 HOH HOH A . R 7 HOH 87 2087 2087 HOH HOH A . R 7 HOH 88 2088 2088 HOH HOH A . R 7 HOH 89 2089 2089 HOH HOH A . R 7 HOH 90 2090 2090 HOH HOH A . R 7 HOH 91 2091 2091 HOH HOH A . R 7 HOH 92 2092 2092 HOH HOH A . R 7 HOH 93 2093 2093 HOH HOH A . R 7 HOH 94 2094 2094 HOH HOH A . R 7 HOH 95 2095 2095 HOH HOH A . R 7 HOH 96 2096 2096 HOH HOH A . R 7 HOH 97 2097 2097 HOH HOH A . R 7 HOH 98 2098 2098 HOH HOH A . R 7 HOH 99 2099 2099 HOH HOH A . R 7 HOH 100 2100 2100 HOH HOH A . R 7 HOH 101 2101 2101 HOH HOH A . R 7 HOH 102 2102 2102 HOH HOH A . R 7 HOH 103 2103 2103 HOH HOH A . R 7 HOH 104 2104 2104 HOH HOH A . R 7 HOH 105 2105 2105 HOH HOH A . R 7 HOH 106 2106 2106 HOH HOH A . R 7 HOH 107 2107 2107 HOH HOH A . R 7 HOH 108 2108 2108 HOH HOH A . R 7 HOH 109 2109 2109 HOH HOH A . R 7 HOH 110 2110 2110 HOH HOH A . R 7 HOH 111 2111 2111 HOH HOH A . R 7 HOH 112 2112 2112 HOH HOH A . R 7 HOH 113 2113 2113 HOH HOH A . R 7 HOH 114 2114 2114 HOH HOH A . R 7 HOH 115 2115 2115 HOH HOH A . R 7 HOH 116 2116 2116 HOH HOH A . R 7 HOH 117 2117 2117 HOH HOH A . R 7 HOH 118 2118 2118 HOH HOH A . R 7 HOH 119 2119 2119 HOH HOH A . R 7 HOH 120 2120 2120 HOH HOH A . R 7 HOH 121 2121 2121 HOH HOH A . R 7 HOH 122 2122 2122 HOH HOH A . R 7 HOH 123 2123 2123 HOH HOH A . R 7 HOH 124 2124 2124 HOH HOH A . R 7 HOH 125 2125 2125 HOH HOH A . R 7 HOH 126 2126 2126 HOH HOH A . R 7 HOH 127 2127 2127 HOH HOH A . R 7 HOH 128 2128 2128 HOH HOH A . R 7 HOH 129 2129 2129 HOH HOH A . R 7 HOH 130 2130 2130 HOH HOH A . R 7 HOH 131 2131 2131 HOH HOH A . R 7 HOH 132 2132 2132 HOH HOH A . R 7 HOH 133 2133 2133 HOH HOH A . R 7 HOH 134 2134 2134 HOH HOH A . R 7 HOH 135 2135 2135 HOH HOH A . R 7 HOH 136 2136 2136 HOH HOH A . R 7 HOH 137 2137 2137 HOH HOH A . R 7 HOH 138 2138 2138 HOH HOH A . R 7 HOH 139 2139 2139 HOH HOH A . R 7 HOH 140 2140 2140 HOH HOH A . R 7 HOH 141 2141 2141 HOH HOH A . R 7 HOH 142 2142 2142 HOH HOH A . R 7 HOH 143 2143 2143 HOH HOH A . R 7 HOH 144 2144 2144 HOH HOH A . R 7 HOH 145 2145 2145 HOH HOH A . R 7 HOH 146 2146 2146 HOH HOH A . R 7 HOH 147 2147 2147 HOH HOH A . R 7 HOH 148 2148 2148 HOH HOH A . R 7 HOH 149 2149 2149 HOH HOH A . R 7 HOH 150 2150 2150 HOH HOH A . R 7 HOH 151 2151 2151 HOH HOH A . R 7 HOH 152 2152 2152 HOH HOH A . R 7 HOH 153 2153 2153 HOH HOH A . R 7 HOH 154 2154 2154 HOH HOH A . R 7 HOH 155 2155 2155 HOH HOH A . R 7 HOH 156 2156 2156 HOH HOH A . R 7 HOH 157 2157 2157 HOH HOH A . R 7 HOH 158 2158 2158 HOH HOH A . R 7 HOH 159 2159 2159 HOH HOH A . R 7 HOH 160 2160 2160 HOH HOH A . R 7 HOH 161 2161 2161 HOH HOH A . R 7 HOH 162 2162 2162 HOH HOH A . R 7 HOH 163 2163 2163 HOH HOH A . R 7 HOH 164 2164 2164 HOH HOH A . R 7 HOH 165 2165 2165 HOH HOH A . R 7 HOH 166 2166 2166 HOH HOH A . R 7 HOH 167 2167 2167 HOH HOH A . R 7 HOH 168 2168 2168 HOH HOH A . R 7 HOH 169 2169 2169 HOH HOH A . R 7 HOH 170 2170 2170 HOH HOH A . R 7 HOH 171 2171 2171 HOH HOH A . R 7 HOH 172 2172 2172 HOH HOH A . R 7 HOH 173 2173 2173 HOH HOH A . R 7 HOH 174 2174 2174 HOH HOH A . R 7 HOH 175 2175 2175 HOH HOH A . R 7 HOH 176 2176 2176 HOH HOH A . R 7 HOH 177 2177 2177 HOH HOH A . R 7 HOH 178 2178 2178 HOH HOH A . R 7 HOH 179 2179 2179 HOH HOH A . R 7 HOH 180 2180 2180 HOH HOH A . R 7 HOH 181 2181 2181 HOH HOH A . R 7 HOH 182 2182 2182 HOH HOH A . R 7 HOH 183 2183 2183 HOH HOH A . R 7 HOH 184 2184 2184 HOH HOH A . R 7 HOH 185 2185 2185 HOH HOH A . R 7 HOH 186 2186 2186 HOH HOH A . R 7 HOH 187 2187 2187 HOH HOH A . R 7 HOH 188 2188 2188 HOH HOH A . R 7 HOH 189 2189 2189 HOH HOH A . R 7 HOH 190 2190 2190 HOH HOH A . R 7 HOH 191 2191 2191 HOH HOH A . R 7 HOH 192 2192 2192 HOH HOH A . R 7 HOH 193 2193 2193 HOH HOH A . R 7 HOH 194 2194 2194 HOH HOH A . R 7 HOH 195 2195 2195 HOH HOH A . R 7 HOH 196 2196 2196 HOH HOH A . R 7 HOH 197 2197 2197 HOH HOH A . R 7 HOH 198 2198 2198 HOH HOH A . R 7 HOH 199 2199 2199 HOH HOH A . R 7 HOH 200 2200 2200 HOH HOH A . R 7 HOH 201 2201 2201 HOH HOH A . R 7 HOH 202 2202 2202 HOH HOH A . R 7 HOH 203 2203 2203 HOH HOH A . R 7 HOH 204 2204 2204 HOH HOH A . R 7 HOH 205 2205 2205 HOH HOH A . R 7 HOH 206 2206 2206 HOH HOH A . R 7 HOH 207 2207 2207 HOH HOH A . R 7 HOH 208 2208 2208 HOH HOH A . R 7 HOH 209 2209 2209 HOH HOH A . R 7 HOH 210 2210 2210 HOH HOH A . R 7 HOH 211 2211 2211 HOH HOH A . R 7 HOH 212 2212 2212 HOH HOH A . R 7 HOH 213 2213 2213 HOH HOH A . R 7 HOH 214 2214 2214 HOH HOH A . R 7 HOH 215 2215 2215 HOH HOH A . R 7 HOH 216 2216 2216 HOH HOH A . R 7 HOH 217 2217 2217 HOH HOH A . R 7 HOH 218 2218 2218 HOH HOH A . R 7 HOH 219 2219 2219 HOH HOH A . R 7 HOH 220 2220 2220 HOH HOH A . R 7 HOH 221 2221 2221 HOH HOH A . R 7 HOH 222 2222 2222 HOH HOH A . R 7 HOH 223 2223 2223 HOH HOH A . R 7 HOH 224 2224 2224 HOH HOH A . R 7 HOH 225 2225 2225 HOH HOH A . R 7 HOH 226 2226 2226 HOH HOH A . R 7 HOH 227 2227 2227 HOH HOH A . R 7 HOH 228 2228 2228 HOH HOH A . R 7 HOH 229 2229 2229 HOH HOH A . R 7 HOH 230 2230 2230 HOH HOH A . R 7 HOH 231 2231 2231 HOH HOH A . R 7 HOH 232 2232 2232 HOH HOH A . R 7 HOH 233 2233 2233 HOH HOH A . R 7 HOH 234 2234 2234 HOH HOH A . R 7 HOH 235 2235 2235 HOH HOH A . R 7 HOH 236 2236 2236 HOH HOH A . R 7 HOH 237 2237 2237 HOH HOH A . R 7 HOH 238 2238 2238 HOH HOH A . R 7 HOH 239 2239 2239 HOH HOH A . R 7 HOH 240 2240 2240 HOH HOH A . R 7 HOH 241 2241 2241 HOH HOH A . R 7 HOH 242 2242 2242 HOH HOH A . R 7 HOH 243 2243 2243 HOH HOH A . R 7 HOH 244 2244 2244 HOH HOH A . R 7 HOH 245 2245 2245 HOH HOH A . R 7 HOH 246 2246 2246 HOH HOH A . R 7 HOH 247 2247 2247 HOH HOH A . R 7 HOH 248 2248 2248 HOH HOH A . R 7 HOH 249 2249 2249 HOH HOH A . R 7 HOH 250 2250 2250 HOH HOH A . R 7 HOH 251 2251 2251 HOH HOH A . R 7 HOH 252 2252 2252 HOH HOH A . R 7 HOH 253 2253 2253 HOH HOH A . R 7 HOH 254 2254 2254 HOH HOH A . R 7 HOH 255 2255 2255 HOH HOH A . R 7 HOH 256 2256 2256 HOH HOH A . R 7 HOH 257 2257 2257 HOH HOH A . R 7 HOH 258 2258 2258 HOH HOH A . R 7 HOH 259 2259 2259 HOH HOH A . R 7 HOH 260 2260 2260 HOH HOH A . R 7 HOH 261 2261 2261 HOH HOH A . R 7 HOH 262 2262 2262 HOH HOH A . R 7 HOH 263 2263 2263 HOH HOH A . R 7 HOH 264 2264 2264 HOH HOH A . R 7 HOH 265 2265 2265 HOH HOH A . R 7 HOH 266 2266 2266 HOH HOH A . R 7 HOH 267 2267 2267 HOH HOH A . R 7 HOH 268 2268 2268 HOH HOH A . R 7 HOH 269 2269 2269 HOH HOH A . R 7 HOH 270 2270 2270 HOH HOH A . R 7 HOH 271 2271 2271 HOH HOH A . R 7 HOH 272 2272 2272 HOH HOH A . R 7 HOH 273 2273 2273 HOH HOH A . R 7 HOH 274 2274 2274 HOH HOH A . R 7 HOH 275 2275 2275 HOH HOH A . R 7 HOH 276 2276 2276 HOH HOH A . R 7 HOH 277 2277 2277 HOH HOH A . R 7 HOH 278 2278 2278 HOH HOH A . R 7 HOH 279 2279 2279 HOH HOH A . R 7 HOH 280 2280 2280 HOH HOH A . R 7 HOH 281 2281 2281 HOH HOH A . R 7 HOH 282 2282 2282 HOH HOH A . R 7 HOH 283 2283 2283 HOH HOH A . R 7 HOH 284 2284 2284 HOH HOH A . R 7 HOH 285 2285 2285 HOH HOH A . R 7 HOH 286 2286 2286 HOH HOH A . R 7 HOH 287 2287 2287 HOH HOH A . R 7 HOH 288 2288 2288 HOH HOH A . R 7 HOH 289 2289 2289 HOH HOH A . R 7 HOH 290 2290 2290 HOH HOH A . R 7 HOH 291 2291 2291 HOH HOH A . R 7 HOH 292 2292 2292 HOH HOH A . R 7 HOH 293 2293 2293 HOH HOH A . R 7 HOH 294 2294 2294 HOH HOH A . R 7 HOH 295 2295 2295 HOH HOH A . R 7 HOH 296 2296 2296 HOH HOH A . R 7 HOH 297 2297 2297 HOH HOH A . R 7 HOH 298 2298 2298 HOH HOH A . R 7 HOH 299 2299 2299 HOH HOH A . R 7 HOH 300 2300 2300 HOH HOH A . R 7 HOH 301 2301 2301 HOH HOH A . R 7 HOH 302 2302 2302 HOH HOH A . R 7 HOH 303 2303 2303 HOH HOH A . R 7 HOH 304 2304 2304 HOH HOH A . R 7 HOH 305 2305 2305 HOH HOH A . R 7 HOH 306 2306 2306 HOH HOH A . R 7 HOH 307 2307 2307 HOH HOH A . R 7 HOH 308 2308 2308 HOH HOH A . R 7 HOH 309 2309 2309 HOH HOH A . R 7 HOH 310 2310 2310 HOH HOH A . R 7 HOH 311 2311 2311 HOH HOH A . R 7 HOH 312 2312 2312 HOH HOH A . R 7 HOH 313 2313 2313 HOH HOH A . R 7 HOH 314 2314 2314 HOH HOH A . R 7 HOH 315 2315 2315 HOH HOH A . R 7 HOH 316 2316 2316 HOH HOH A . R 7 HOH 317 2317 2317 HOH HOH A . R 7 HOH 318 2318 2318 HOH HOH A . R 7 HOH 319 2319 2319 HOH HOH A . R 7 HOH 320 2320 2320 HOH HOH A . R 7 HOH 321 2321 2321 HOH HOH A . R 7 HOH 322 2322 2322 HOH HOH A . R 7 HOH 323 2323 2323 HOH HOH A . R 7 HOH 324 2324 2324 HOH HOH A . R 7 HOH 325 2325 2325 HOH HOH A . R 7 HOH 326 2326 2326 HOH HOH A . R 7 HOH 327 2327 2327 HOH HOH A . R 7 HOH 328 2328 2328 HOH HOH A . R 7 HOH 329 2329 2329 HOH HOH A . R 7 HOH 330 2330 2330 HOH HOH A . R 7 HOH 331 2331 2331 HOH HOH A . R 7 HOH 332 2332 2332 HOH HOH A . R 7 HOH 333 2333 2333 HOH HOH A . R 7 HOH 334 2334 2334 HOH HOH A . R 7 HOH 335 2335 2335 HOH HOH A . R 7 HOH 336 2336 2336 HOH HOH A . R 7 HOH 337 2337 2337 HOH HOH A . R 7 HOH 338 2338 2338 HOH HOH A . R 7 HOH 339 2339 2339 HOH HOH A . R 7 HOH 340 2340 2340 HOH HOH A . R 7 HOH 341 2341 2341 HOH HOH A . R 7 HOH 342 2342 2342 HOH HOH A . R 7 HOH 343 2343 2343 HOH HOH A . R 7 HOH 344 2344 2344 HOH HOH A . R 7 HOH 345 2345 2345 HOH HOH A . R 7 HOH 346 2346 2346 HOH HOH A . R 7 HOH 347 2347 2347 HOH HOH A . R 7 HOH 348 2348 2348 HOH HOH A . R 7 HOH 349 2349 2349 HOH HOH A . R 7 HOH 350 2350 2350 HOH HOH A . R 7 HOH 351 2351 2351 HOH HOH A . R 7 HOH 352 2352 2352 HOH HOH A . R 7 HOH 353 2353 2353 HOH HOH A . R 7 HOH 354 2354 2354 HOH HOH A . R 7 HOH 355 2355 2355 HOH HOH A . R 7 HOH 356 2356 2356 HOH HOH A . R 7 HOH 357 2357 2357 HOH HOH A . R 7 HOH 358 2358 2358 HOH HOH A . R 7 HOH 359 2359 2359 HOH HOH A . R 7 HOH 360 2360 2360 HOH HOH A . R 7 HOH 361 2361 2361 HOH HOH A . R 7 HOH 362 2362 2362 HOH HOH A . R 7 HOH 363 2363 2363 HOH HOH A . R 7 HOH 364 2364 2364 HOH HOH A . R 7 HOH 365 2365 2365 HOH HOH A . R 7 HOH 366 2366 2366 HOH HOH A . R 7 HOH 367 2367 2367 HOH HOH A . R 7 HOH 368 2368 2368 HOH HOH A . R 7 HOH 369 2369 2369 HOH HOH A . R 7 HOH 370 2370 2370 HOH HOH A . R 7 HOH 371 2371 2371 HOH HOH A . R 7 HOH 372 2372 2372 HOH HOH A . R 7 HOH 373 2373 2373 HOH HOH A . R 7 HOH 374 2374 2374 HOH HOH A . R 7 HOH 375 2375 2375 HOH HOH A . R 7 HOH 376 2376 2376 HOH HOH A . R 7 HOH 377 2377 2377 HOH HOH A . R 7 HOH 378 2378 2378 HOH HOH A . R 7 HOH 379 2379 2379 HOH HOH A . R 7 HOH 380 2380 2380 HOH HOH A . R 7 HOH 381 2381 2381 HOH HOH A . R 7 HOH 382 2382 2382 HOH HOH A . R 7 HOH 383 2383 2383 HOH HOH A . R 7 HOH 384 2384 2384 HOH HOH A . R 7 HOH 385 2385 2385 HOH HOH A . R 7 HOH 386 2386 2386 HOH HOH A . R 7 HOH 387 2387 2387 HOH HOH A . R 7 HOH 388 2388 2388 HOH HOH A . R 7 HOH 389 2389 2389 HOH HOH A . R 7 HOH 390 2390 2390 HOH HOH A . R 7 HOH 391 2391 2391 HOH HOH A . R 7 HOH 392 2392 2392 HOH HOH A . R 7 HOH 393 2393 2393 HOH HOH A . R 7 HOH 394 2394 2394 HOH HOH A . R 7 HOH 395 2395 2395 HOH HOH A . R 7 HOH 396 2396 2396 HOH HOH A . R 7 HOH 397 2397 2397 HOH HOH A . R 7 HOH 398 2398 2398 HOH HOH A . R 7 HOH 399 2399 2399 HOH HOH A . R 7 HOH 400 2400 2400 HOH HOH A . R 7 HOH 401 2401 2401 HOH HOH A . R 7 HOH 402 2402 2402 HOH HOH A . R 7 HOH 403 2403 2403 HOH HOH A . R 7 HOH 404 2404 2404 HOH HOH A . R 7 HOH 405 2405 2405 HOH HOH A . R 7 HOH 406 2406 2406 HOH HOH A . R 7 HOH 407 2407 2407 HOH HOH A . R 7 HOH 408 2408 2408 HOH HOH A . R 7 HOH 409 2409 2409 HOH HOH A . R 7 HOH 410 2410 2410 HOH HOH A . R 7 HOH 411 2411 2411 HOH HOH A . R 7 HOH 412 2412 2412 HOH HOH A . R 7 HOH 413 2413 2413 HOH HOH A . R 7 HOH 414 2414 2414 HOH HOH A . R 7 HOH 415 2415 2415 HOH HOH A . R 7 HOH 416 2416 2416 HOH HOH A . R 7 HOH 417 2417 2417 HOH HOH A . R 7 HOH 418 2418 2418 HOH HOH A . R 7 HOH 419 2419 2419 HOH HOH A . R 7 HOH 420 2420 2420 HOH HOH A . R 7 HOH 421 2421 2421 HOH HOH A . R 7 HOH 422 2422 2422 HOH HOH A . R 7 HOH 423 2423 2423 HOH HOH A . R 7 HOH 424 2424 2424 HOH HOH A . R 7 HOH 425 2425 2425 HOH HOH A . R 7 HOH 426 2426 2426 HOH HOH A . R 7 HOH 427 2427 2427 HOH HOH A . R 7 HOH 428 2428 2428 HOH HOH A . R 7 HOH 429 2429 2429 HOH HOH A . R 7 HOH 430 2430 2430 HOH HOH A . R 7 HOH 431 2431 2431 HOH HOH A . R 7 HOH 432 2432 2432 HOH HOH A . R 7 HOH 433 2433 2433 HOH HOH A . R 7 HOH 434 2434 2434 HOH HOH A . R 7 HOH 435 2435 2435 HOH HOH A . R 7 HOH 436 2436 2436 HOH HOH A . R 7 HOH 437 2437 2437 HOH HOH A . R 7 HOH 438 2438 2438 HOH HOH A . R 7 HOH 439 2439 2439 HOH HOH A . R 7 HOH 440 2440 2440 HOH HOH A . R 7 HOH 441 2441 2441 HOH HOH A . R 7 HOH 442 2442 2442 HOH HOH A . R 7 HOH 443 2443 2443 HOH HOH A . R 7 HOH 444 2444 2444 HOH HOH A . R 7 HOH 445 2445 2445 HOH HOH A . R 7 HOH 446 2446 2446 HOH HOH A . R 7 HOH 447 2447 2447 HOH HOH A . R 7 HOH 448 2448 2448 HOH HOH A . R 7 HOH 449 2449 2449 HOH HOH A . R 7 HOH 450 2450 2450 HOH HOH A . R 7 HOH 451 2451 2451 HOH HOH A . R 7 HOH 452 2452 2452 HOH HOH A . R 7 HOH 453 2453 2453 HOH HOH A . R 7 HOH 454 2454 2454 HOH HOH A . R 7 HOH 455 2455 2455 HOH HOH A . R 7 HOH 456 2456 2456 HOH HOH A . R 7 HOH 457 2457 2457 HOH HOH A . R 7 HOH 458 2458 2458 HOH HOH A . R 7 HOH 459 2459 2459 HOH HOH A . R 7 HOH 460 2460 2460 HOH HOH A . R 7 HOH 461 2461 2461 HOH HOH A . R 7 HOH 462 2462 2462 HOH HOH A . R 7 HOH 463 2463 2463 HOH HOH A . R 7 HOH 464 2464 2464 HOH HOH A . R 7 HOH 465 2465 2465 HOH HOH A . R 7 HOH 466 2466 2466 HOH HOH A . R 7 HOH 467 2467 2467 HOH HOH A . R 7 HOH 468 2468 2468 HOH HOH A . R 7 HOH 469 2469 2469 HOH HOH A . R 7 HOH 470 2470 2470 HOH HOH A . R 7 HOH 471 2471 2471 HOH HOH A . R 7 HOH 472 2472 2472 HOH HOH A . R 7 HOH 473 2473 2473 HOH HOH A . R 7 HOH 474 2474 2474 HOH HOH A . R 7 HOH 475 2475 2475 HOH HOH A . R 7 HOH 476 2476 2476 HOH HOH A . R 7 HOH 477 2477 2477 HOH HOH A . R 7 HOH 478 2478 2478 HOH HOH A . R 7 HOH 479 2479 2479 HOH HOH A . R 7 HOH 480 2480 2480 HOH HOH A . R 7 HOH 481 2481 2481 HOH HOH A . R 7 HOH 482 2482 2482 HOH HOH A . R 7 HOH 483 2483 2483 HOH HOH A . R 7 HOH 484 2484 2484 HOH HOH A . R 7 HOH 485 2485 2485 HOH HOH A . R 7 HOH 486 2486 2486 HOH HOH A . R 7 HOH 487 2487 2487 HOH HOH A . R 7 HOH 488 2488 2488 HOH HOH A . R 7 HOH 489 2489 2489 HOH HOH A . R 7 HOH 490 2490 2490 HOH HOH A . R 7 HOH 491 2491 2491 HOH HOH A . R 7 HOH 492 2492 2492 HOH HOH A . R 7 HOH 493 2493 2493 HOH HOH A . R 7 HOH 494 2494 2494 HOH HOH A . R 7 HOH 495 2495 2495 HOH HOH A . R 7 HOH 496 2496 2496 HOH HOH A . R 7 HOH 497 2497 2497 HOH HOH A . R 7 HOH 498 2498 2498 HOH HOH A . R 7 HOH 499 2499 2499 HOH HOH A . R 7 HOH 500 2500 2500 HOH HOH A . R 7 HOH 501 2501 2501 HOH HOH A . R 7 HOH 502 2502 2502 HOH HOH A . R 7 HOH 503 2503 2503 HOH HOH A . R 7 HOH 504 2504 2504 HOH HOH A . R 7 HOH 505 2505 2505 HOH HOH A . R 7 HOH 506 2506 2506 HOH HOH A . R 7 HOH 507 2507 2507 HOH HOH A . R 7 HOH 508 2508 2508 HOH HOH A . R 7 HOH 509 2509 2509 HOH HOH A . R 7 HOH 510 2510 2510 HOH HOH A . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 38 A ASN 38 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 63 A ASN 63 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 126 A ASN 126 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 133 A ASN 133 ? ASN 'GLYCOSYLATION SITE' 5 A ASN 165 A ASN 165 ? ASN 'GLYCOSYLATION SITE' 6 A ASN 246 A ASN 246 ? ASN 'GLYCOSYLATION SITE' 7 A ASN 285 A ASN 285 ? ASN 'GLYCOSYLATION SITE' 8 A ASN 483 A ASN 483 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details trimeric _pdbx_struct_assembly.oligomeric_count 3 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1,2,3 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 28400 ? 1 MORE 162.5 ? 1 'SSA (A^2)' 61610 ? # loop_ _pdbx_struct_oper_list.id _pdbx_struct_oper_list.type _pdbx_struct_oper_list.name _pdbx_struct_oper_list.symmetry_operation _pdbx_struct_oper_list.matrix[1][1] _pdbx_struct_oper_list.matrix[1][2] _pdbx_struct_oper_list.matrix[1][3] _pdbx_struct_oper_list.vector[1] _pdbx_struct_oper_list.matrix[2][1] _pdbx_struct_oper_list.matrix[2][2] _pdbx_struct_oper_list.matrix[2][3] _pdbx_struct_oper_list.vector[2] _pdbx_struct_oper_list.matrix[3][1] _pdbx_struct_oper_list.matrix[3][2] _pdbx_struct_oper_list.matrix[3][3] _pdbx_struct_oper_list.vector[3] 1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 2 'crystal symmetry operation' 2_565 -y,x-y+1,z -0.5000000000 -0.8660254038 0.0000000000 -50.4600000000 0.8660254038 -0.5000000000 0.0000000000 87.3992837499 0.0000000000 0.0000000000 1.0000000000 0.0000000000 3 'crystal symmetry operation' 3_455 -x+y-1,-x,z -0.5000000000 0.8660254038 0.0000000000 -100.9200000000 -0.8660254038 -0.5000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 # loop_ _pdbx_struct_special_symmetry.id _pdbx_struct_special_symmetry.PDB_model_num _pdbx_struct_special_symmetry.auth_asym_id _pdbx_struct_special_symmetry.auth_comp_id _pdbx_struct_special_symmetry.auth_seq_id _pdbx_struct_special_symmetry.PDB_ins_code _pdbx_struct_special_symmetry.label_asym_id _pdbx_struct_special_symmetry.label_comp_id _pdbx_struct_special_symmetry.label_seq_id 1 1 A HOH 2194 ? R HOH . 2 1 A HOH 2198 ? R HOH . 3 1 A HOH 2201 ? R HOH . 4 1 A HOH 2206 ? R HOH . 5 1 A HOH 2510 ? R HOH . # 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 2012-11-07 2 'Structure model' 1 1 2012-12-26 3 'Structure model' 1 2 2013-01-16 # _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' 'Database references' 2 2 'Structure model' 'Structure summary' 3 3 'Structure model' 'Database references' # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] 'X-RAY DIFFRACTION' 1 ? refined -44.2513 7.2681 67.2875 0.0732 0.0534 0.0886 0.0051 -0.0334 0.0361 0.0732 0.1194 0.7730 -0.0301 -0.0141 -0.1279 -0.0034 -0.0495 -0.0674 0.0055 0.0521 0.0062 0.0721 -0.0064 -0.0487 'X-RAY DIFFRACTION' 2 ? refined -39.3532 17.0872 91.8617 0.0947 0.1481 0.0414 0.0150 -0.0383 -0.0077 0.5202 0.3598 0.3027 0.0858 0.2094 0.2900 -0.0111 -0.1458 -0.0068 0.1293 0.0952 -0.0989 0.0601 0.0395 -0.0841 'X-RAY DIFFRACTION' 3 ? refined -49.7144 13.8917 38.2731 0.0768 0.0698 0.0894 -0.0104 -0.0390 -0.0108 0.0559 0.1239 0.6628 0.0392 0.1293 -0.0196 0.0225 0.0233 -0.0466 -0.0211 0.0623 0.0012 0.0187 0.0539 -0.0848 'X-RAY DIFFRACTION' 4 ? refined -46.1786 17.9148 -4.8689 0.1164 0.0606 0.0475 0.0108 0.0222 -0.0408 0.9344 1.4766 2.3781 0.2023 -0.9222 -1.6302 0.1616 0.0302 0.1126 -0.1018 -0.0067 0.0379 0.0036 0.0277 -0.1549 # loop_ _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection _pdbx_refine_tls_group.selection_details 'X-RAY DIFFRACTION' 1 1 A 8 ? ? A 157 ? ? ? ? 'X-RAY DIFFRACTION' 2 2 A 158 ? ? A 263 ? ? ? ? 'X-RAY DIFFRACTION' 3 3 A 264 ? ? A 448 ? ? ? ? 'X-RAY DIFFRACTION' 4 4 A 449 ? ? A 503 ? ? ? ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.6.0117 ? 1 MOSFLM 'data reduction' . ? 2 SCALA 'data scaling' . ? 3 PHASER phasing . ? 4 # _pdbx_entry_details.entry_id 2YP8 _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details ;THE GLOBAL INITIATIVE ON SHARING ALL INFLUENZA DATA ( GISAID) ACCESSION NUMBER PROVIDED EPI347408 ; # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 O A HOH 2091 ? ? O A HOH 2125 ? ? 2.01 2 1 O A HOH 2250 ? ? O A HOH 2270 ? ? 2.05 3 1 O A HOH 2154 ? ? O A HOH 2155 ? ? 2.12 4 1 ND2 A ASN 296 ? B O A HOH 2324 ? ? 2.13 5 1 O5 A TAM 1507 ? ? O A HOH 2508 ? ? 2.17 # _pdbx_validate_symm_contact.id 1 _pdbx_validate_symm_contact.PDB_model_num 1 _pdbx_validate_symm_contact.auth_atom_id_1 O _pdbx_validate_symm_contact.auth_asym_id_1 A _pdbx_validate_symm_contact.auth_comp_id_1 HOH _pdbx_validate_symm_contact.auth_seq_id_1 2405 _pdbx_validate_symm_contact.PDB_ins_code_1 ? _pdbx_validate_symm_contact.label_alt_id_1 ? _pdbx_validate_symm_contact.site_symmetry_1 1_555 _pdbx_validate_symm_contact.auth_atom_id_2 O _pdbx_validate_symm_contact.auth_asym_id_2 A _pdbx_validate_symm_contact.auth_comp_id_2 HOH _pdbx_validate_symm_contact.auth_seq_id_2 2440 _pdbx_validate_symm_contact.PDB_ins_code_2 ? _pdbx_validate_symm_contact.label_alt_id_2 ? _pdbx_validate_symm_contact.site_symmetry_2 2_565 _pdbx_validate_symm_contact.dist 2.19 # 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 GLU A 62 ? ? 51.63 -117.93 2 1 ASN A 96 ? ? -140.26 38.36 3 1 CYS A 97 ? ? -135.22 -153.90 4 1 TRP A 127 ? ? -96.88 52.67 5 1 SER A 143 ? ? 67.35 -0.23 6 1 SER A 146 ? ? -151.78 -155.09 7 1 ASN A 341 ? ? -164.92 117.20 8 1 PHE A 392 ? ? -122.38 -113.10 9 1 GLN A 394 ? A -125.59 -119.64 10 1 GLN A 394 ? B -131.09 -137.46 11 1 ARG A 456 ? ? 51.48 -124.80 12 1 TYR A 470 ? ? -91.54 34.29 13 1 PHE A 500 ? ? -108.24 73.35 # _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 1133 _pdbx_validate_chiral.PDB_ins_code ? _pdbx_validate_chiral.details 'WRONG HAND' _pdbx_validate_chiral.omega . # loop_ _pdbx_distant_solvent_atoms.id _pdbx_distant_solvent_atoms.PDB_model_num _pdbx_distant_solvent_atoms.auth_atom_id _pdbx_distant_solvent_atoms.label_alt_id _pdbx_distant_solvent_atoms.auth_asym_id _pdbx_distant_solvent_atoms.auth_comp_id _pdbx_distant_solvent_atoms.auth_seq_id _pdbx_distant_solvent_atoms.PDB_ins_code _pdbx_distant_solvent_atoms.neighbor_macromolecule_distance _pdbx_distant_solvent_atoms.neighbor_ligand_distance 1 1 O ? A HOH 2194 ? 6.27 . 2 1 O ? A HOH 2510 ? 7.84 . # 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 LYS 2 ? A LYS 2 3 1 Y 1 A LEU 3 ? A LEU 3 4 1 Y 1 A PRO 4 ? A PRO 4 5 1 Y 1 A GLY 5 ? A GLY 5 6 1 Y 1 A ASN 6 ? A ASN 6 7 1 Y 1 A ASP 7 ? A ASP 7 8 1 Y 1 A THR 328 ? A THR 328 9 1 Y 1 A GLN 329 ? A GLN 329 10 1 Y 1 A GLY 330 ? A GLY 330 11 1 Y 1 A ILE 331 ? A ILE 331 12 1 Y 1 A PHE 332 ? A PHE 332 13 1 Y 1 A GLY 333 ? A GLY 333 # 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 '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' EPE 5 'TRIS(HYDROXYETHYL)AMINOMETHANE' TAM 6 'O-SIALIC ACID' SIA 7 water HOH #