data_4MWT # _entry.id 4MWT # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.284 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 4MWT RCSB RCSB082464 WWPDB D_1000082464 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 1IVY 'zymogen form' unspecified PDB 4MWS . unspecified # _pdbx_database_status.entry_id 4MWT _pdbx_database_status.status_code REL _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.recvd_initial_deposition_date 2013-09-25 _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Kolli, N.' 1 'Garman, S.C.' 2 # _citation.id primary _citation.title 'Proteolytic activation of human cathepsin A.' _citation.journal_abbrev J.Biol.Chem. _citation.journal_volume 289 _citation.page_first 11592 _citation.page_last 11600 _citation.year 2014 _citation.journal_id_ASTM JBCHA3 _citation.country US _citation.journal_id_ISSN 0021-9258 _citation.journal_id_CSD 0071 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 24599961 _citation.pdbx_database_id_DOI 10.1074/jbc.M113.524280 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Kolli, N.' 1 primary 'Garman, S.C.' 2 # _cell.entry_id 4MWT _cell.length_a 134.575 _cell.length_b 134.575 _cell.length_c 99.776 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 12 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 4MWT _symmetry.space_group_name_H-M 'P 31 2 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 152 _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man 'Lysosomal protective protein' 48655.582 2 3.4.16.5 ? ? ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 5 ? ? ? ? 3 non-polymer man BETA-D-MANNOSE 180.156 1 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name ;Carboxypeptidase C, Carboxypeptidase L, Cathepsin A, Protective protein cathepsin A, PPCA, Protective protein for beta-galactosidase ; # _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 ;APDQDEIQRLPGLAKQPSFRQYSGYLKGSGSKHLHYWFVESQKDPENSPVVLWLNGGPGCSSLDGLLTEHGPFLVQPDGV TLEYNPYSWNLIANVLYLESPAGVGFSYSDDKFYATNDTEVAQSNFEALQDFFRLFPEYKNNKLFLTGESYAGIYIPTLA VLVMQDPSMNLQGLAVGNGLSSYEQNDNSLVYFAYYHGLLGNRLWSSLQTHCCSQNKCNFYDNKDLECVTNLQEVARIVG NSGLNIYNLYAPCAGGVPSHFRSGDKVRMDPPCTNTTAASTYLNNPYVRKALNIPEQLPQWDMCNFLVNLQYRRLYRSMN SQYLKLLSSQKYQILLYNGDVDMACNFMGDEWFVDSLNQKMEVQRRPWLVKYGDSGEQIAGFVKEFSHIAFLTIKGAGHM VPTDKPLAAFTMFSRFLNKQPYHHHHHH ; _entity_poly.pdbx_seq_one_letter_code_can ;APDQDEIQRLPGLAKQPSFRQYSGYLKGSGSKHLHYWFVESQKDPENSPVVLWLNGGPGCSSLDGLLTEHGPFLVQPDGV TLEYNPYSWNLIANVLYLESPAGVGFSYSDDKFYATNDTEVAQSNFEALQDFFRLFPEYKNNKLFLTGESYAGIYIPTLA VLVMQDPSMNLQGLAVGNGLSSYEQNDNSLVYFAYYHGLLGNRLWSSLQTHCCSQNKCNFYDNKDLECVTNLQEVARIVG NSGLNIYNLYAPCAGGVPSHFRSGDKVRMDPPCTNTTAASTYLNNPYVRKALNIPEQLPQWDMCNFLVNLQYRRLYRSMN SQYLKLLSSQKYQILLYNGDVDMACNFMGDEWFVDSLNQKMEVQRRPWLVKYGDSGEQIAGFVKEFSHIAFLTIKGAGHM VPTDKPLAAFTMFSRFLNKQPYHHHHHH ; _entity_poly.pdbx_strand_id A,B _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ALA n 1 2 PRO n 1 3 ASP n 1 4 GLN n 1 5 ASP n 1 6 GLU n 1 7 ILE n 1 8 GLN n 1 9 ARG n 1 10 LEU n 1 11 PRO n 1 12 GLY n 1 13 LEU n 1 14 ALA n 1 15 LYS n 1 16 GLN n 1 17 PRO n 1 18 SER n 1 19 PHE n 1 20 ARG n 1 21 GLN n 1 22 TYR n 1 23 SER n 1 24 GLY n 1 25 TYR n 1 26 LEU n 1 27 LYS n 1 28 GLY n 1 29 SER n 1 30 GLY n 1 31 SER n 1 32 LYS n 1 33 HIS n 1 34 LEU n 1 35 HIS n 1 36 TYR n 1 37 TRP n 1 38 PHE n 1 39 VAL n 1 40 GLU n 1 41 SER n 1 42 GLN n 1 43 LYS n 1 44 ASP n 1 45 PRO n 1 46 GLU n 1 47 ASN n 1 48 SER n 1 49 PRO n 1 50 VAL n 1 51 VAL n 1 52 LEU n 1 53 TRP n 1 54 LEU n 1 55 ASN n 1 56 GLY n 1 57 GLY n 1 58 PRO n 1 59 GLY n 1 60 CYS n 1 61 SER n 1 62 SER n 1 63 LEU n 1 64 ASP n 1 65 GLY n 1 66 LEU n 1 67 LEU n 1 68 THR n 1 69 GLU n 1 70 HIS n 1 71 GLY n 1 72 PRO n 1 73 PHE n 1 74 LEU n 1 75 VAL n 1 76 GLN n 1 77 PRO n 1 78 ASP n 1 79 GLY n 1 80 VAL n 1 81 THR n 1 82 LEU n 1 83 GLU n 1 84 TYR n 1 85 ASN n 1 86 PRO n 1 87 TYR n 1 88 SER n 1 89 TRP n 1 90 ASN n 1 91 LEU n 1 92 ILE n 1 93 ALA n 1 94 ASN n 1 95 VAL n 1 96 LEU n 1 97 TYR n 1 98 LEU n 1 99 GLU n 1 100 SER n 1 101 PRO n 1 102 ALA n 1 103 GLY n 1 104 VAL n 1 105 GLY n 1 106 PHE n 1 107 SER n 1 108 TYR n 1 109 SER n 1 110 ASP n 1 111 ASP n 1 112 LYS n 1 113 PHE n 1 114 TYR n 1 115 ALA n 1 116 THR n 1 117 ASN n 1 118 ASP n 1 119 THR n 1 120 GLU n 1 121 VAL n 1 122 ALA n 1 123 GLN n 1 124 SER n 1 125 ASN n 1 126 PHE n 1 127 GLU n 1 128 ALA n 1 129 LEU n 1 130 GLN n 1 131 ASP n 1 132 PHE n 1 133 PHE n 1 134 ARG n 1 135 LEU n 1 136 PHE n 1 137 PRO n 1 138 GLU n 1 139 TYR n 1 140 LYS n 1 141 ASN n 1 142 ASN n 1 143 LYS n 1 144 LEU n 1 145 PHE n 1 146 LEU n 1 147 THR n 1 148 GLY n 1 149 GLU n 1 150 SER n 1 151 TYR n 1 152 ALA n 1 153 GLY n 1 154 ILE n 1 155 TYR n 1 156 ILE n 1 157 PRO n 1 158 THR n 1 159 LEU n 1 160 ALA n 1 161 VAL n 1 162 LEU n 1 163 VAL n 1 164 MET n 1 165 GLN n 1 166 ASP n 1 167 PRO n 1 168 SER n 1 169 MET n 1 170 ASN n 1 171 LEU n 1 172 GLN n 1 173 GLY n 1 174 LEU n 1 175 ALA n 1 176 VAL n 1 177 GLY n 1 178 ASN n 1 179 GLY n 1 180 LEU n 1 181 SER n 1 182 SER n 1 183 TYR n 1 184 GLU n 1 185 GLN n 1 186 ASN n 1 187 ASP n 1 188 ASN n 1 189 SER n 1 190 LEU n 1 191 VAL n 1 192 TYR n 1 193 PHE n 1 194 ALA n 1 195 TYR n 1 196 TYR n 1 197 HIS n 1 198 GLY n 1 199 LEU n 1 200 LEU n 1 201 GLY n 1 202 ASN n 1 203 ARG n 1 204 LEU n 1 205 TRP n 1 206 SER n 1 207 SER n 1 208 LEU n 1 209 GLN n 1 210 THR n 1 211 HIS n 1 212 CYS n 1 213 CYS n 1 214 SER n 1 215 GLN n 1 216 ASN n 1 217 LYS n 1 218 CYS n 1 219 ASN n 1 220 PHE n 1 221 TYR n 1 222 ASP n 1 223 ASN n 1 224 LYS n 1 225 ASP n 1 226 LEU n 1 227 GLU n 1 228 CYS n 1 229 VAL n 1 230 THR n 1 231 ASN n 1 232 LEU n 1 233 GLN n 1 234 GLU n 1 235 VAL n 1 236 ALA n 1 237 ARG n 1 238 ILE n 1 239 VAL n 1 240 GLY n 1 241 ASN n 1 242 SER n 1 243 GLY n 1 244 LEU n 1 245 ASN n 1 246 ILE n 1 247 TYR n 1 248 ASN n 1 249 LEU n 1 250 TYR n 1 251 ALA n 1 252 PRO n 1 253 CYS n 1 254 ALA n 1 255 GLY n 1 256 GLY n 1 257 VAL n 1 258 PRO n 1 259 SER n 1 260 HIS n 1 261 PHE n 1 262 ARG n 1 263 SER n 1 264 GLY n 1 265 ASP n 1 266 LYS n 1 267 VAL n 1 268 ARG n 1 269 MET n 1 270 ASP n 1 271 PRO n 1 272 PRO n 1 273 CYS n 1 274 THR n 1 275 ASN n 1 276 THR n 1 277 THR n 1 278 ALA n 1 279 ALA n 1 280 SER n 1 281 THR n 1 282 TYR n 1 283 LEU n 1 284 ASN n 1 285 ASN n 1 286 PRO n 1 287 TYR n 1 288 VAL n 1 289 ARG n 1 290 LYS n 1 291 ALA n 1 292 LEU n 1 293 ASN n 1 294 ILE n 1 295 PRO n 1 296 GLU n 1 297 GLN n 1 298 LEU n 1 299 PRO n 1 300 GLN n 1 301 TRP n 1 302 ASP n 1 303 MET n 1 304 CYS n 1 305 ASN n 1 306 PHE n 1 307 LEU n 1 308 VAL n 1 309 ASN n 1 310 LEU n 1 311 GLN n 1 312 TYR n 1 313 ARG n 1 314 ARG n 1 315 LEU n 1 316 TYR n 1 317 ARG n 1 318 SER n 1 319 MET n 1 320 ASN n 1 321 SER n 1 322 GLN n 1 323 TYR n 1 324 LEU n 1 325 LYS n 1 326 LEU n 1 327 LEU n 1 328 SER n 1 329 SER n 1 330 GLN n 1 331 LYS n 1 332 TYR n 1 333 GLN n 1 334 ILE n 1 335 LEU n 1 336 LEU n 1 337 TYR n 1 338 ASN n 1 339 GLY n 1 340 ASP n 1 341 VAL n 1 342 ASP n 1 343 MET n 1 344 ALA n 1 345 CYS n 1 346 ASN n 1 347 PHE n 1 348 MET n 1 349 GLY n 1 350 ASP n 1 351 GLU n 1 352 TRP n 1 353 PHE n 1 354 VAL n 1 355 ASP n 1 356 SER n 1 357 LEU n 1 358 ASN n 1 359 GLN n 1 360 LYS n 1 361 MET n 1 362 GLU n 1 363 VAL n 1 364 GLN n 1 365 ARG n 1 366 ARG n 1 367 PRO n 1 368 TRP n 1 369 LEU n 1 370 VAL n 1 371 LYS n 1 372 TYR n 1 373 GLY n 1 374 ASP n 1 375 SER n 1 376 GLY n 1 377 GLU n 1 378 GLN n 1 379 ILE n 1 380 ALA n 1 381 GLY n 1 382 PHE n 1 383 VAL n 1 384 LYS n 1 385 GLU n 1 386 PHE n 1 387 SER n 1 388 HIS n 1 389 ILE n 1 390 ALA n 1 391 PHE n 1 392 LEU n 1 393 THR n 1 394 ILE n 1 395 LYS n 1 396 GLY n 1 397 ALA n 1 398 GLY n 1 399 HIS n 1 400 MET n 1 401 VAL n 1 402 PRO n 1 403 THR n 1 404 ASP n 1 405 LYS n 1 406 PRO n 1 407 LEU n 1 408 ALA n 1 409 ALA n 1 410 PHE n 1 411 THR n 1 412 MET n 1 413 PHE n 1 414 SER n 1 415 ARG n 1 416 PHE n 1 417 LEU n 1 418 ASN n 1 419 LYS n 1 420 GLN n 1 421 PRO n 1 422 TYR n 1 423 HIS n 1 424 HIS n 1 425 HIS n 1 426 HIS n 1 427 HIS n 1 428 HIS 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 human _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene 'CTSA, PPGB' _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details 'Selected with blasticidin' _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'Homo sapiens' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 9606 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name ? _entity_src_gen.pdbx_host_org_scientific_name 'Trichoplusia ni' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 7111 _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 HI-FIVE _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type 'Stable cell line' _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name 'pIB/V5-His-TOPO TA' _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code PPGB_HUMAN _struct_ref.pdbx_db_accession P10619 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;APDQDEIQRLPGLAKQPSFRQYSGYLKGSGSKHLHYWFVESQKDPENSPVVLWLNGGPGCSSLDGLLTEHGPFLVQPDGV TLEYNPYSWNLIANVLYLESPAGVGFSYSDDKFYATNDTEVAQSNFEALQDFFRLFPEYKNNKLFLTGESYAGIYIPTLA VLVMQDPSMNLQGLAVGNGLSSYEQNDNSLVYFAYYHGLLGNRLWSSLQTHCCSQNKCNFYDNKDLECVTNLQEVARIVG NSGLNIYNLYAPCAGGVPSHFRYEKDTVVVQDLGNIFTRLPLKRMWHQALLRSGDKVRMDPPCTNTTAASTYLNNPYVRK ALNIPEQLPQWDMCNFLVNLQYRRLYRSMNSQYLKLLSSQKYQILLYNGDVDMACNFMGDEWFVDSLNQKMEVQRRPWLV KYGDSGEQIAGFVKEFSHIAFLTIKGAGHMVPTDKPLAAFTMFSRFLNKQPY ; _struct_ref.pdbx_align_begin 29 _struct_ref.pdbx_db_isoform ? # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.pdbx_db_align_beg_ins_code _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_db_align_end_ins_code _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 4MWT A 1 ? 422 ? P10619 29 ? 480 ? 1 452 2 1 4MWT B 1 ? 422 ? P10619 29 ? 480 ? 1 452 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 4MWT ? A ? ? UNP P10619 TYR 291 DELETION ? 1 1 4MWT ? A ? ? UNP P10619 GLU 292 DELETION ? 2 1 4MWT ? A ? ? UNP P10619 LYS 293 DELETION ? 3 1 4MWT ? A ? ? UNP P10619 ASP 294 DELETION ? 4 1 4MWT ? A ? ? UNP P10619 THR 295 DELETION ? 5 1 4MWT ? A ? ? UNP P10619 VAL 296 DELETION ? 6 1 4MWT ? A ? ? UNP P10619 VAL 297 DELETION ? 7 1 4MWT ? A ? ? UNP P10619 VAL 298 DELETION ? 8 1 4MWT ? A ? ? UNP P10619 GLN 299 DELETION ? 9 1 4MWT ? A ? ? UNP P10619 ASP 300 DELETION ? 10 1 4MWT ? A ? ? UNP P10619 LEU 301 DELETION ? 11 1 4MWT ? A ? ? UNP P10619 GLY 302 DELETION ? 12 1 4MWT ? A ? ? UNP P10619 ASN 303 DELETION ? 13 1 4MWT ? A ? ? UNP P10619 ILE 304 DELETION ? 14 1 4MWT ? A ? ? UNP P10619 PHE 305 DELETION ? 15 1 4MWT ? A ? ? UNP P10619 THR 306 DELETION ? 16 1 4MWT ? A ? ? UNP P10619 ARG 307 DELETION ? 17 1 4MWT ? A ? ? UNP P10619 LEU 308 DELETION ? 18 1 4MWT ? A ? ? UNP P10619 PRO 309 DELETION ? 19 1 4MWT ? A ? ? UNP P10619 LEU 310 DELETION ? 20 1 4MWT ? A ? ? UNP P10619 LYS 311 DELETION ? 21 1 4MWT ? A ? ? UNP P10619 ARG 312 DELETION ? 22 1 4MWT ? A ? ? UNP P10619 MET 313 DELETION ? 23 1 4MWT ? A ? ? UNP P10619 TRP 314 DELETION ? 24 1 4MWT ? A ? ? UNP P10619 HIS 315 DELETION ? 25 1 4MWT ? A ? ? UNP P10619 GLN 316 DELETION ? 26 1 4MWT ? A ? ? UNP P10619 ALA 317 DELETION ? 27 1 4MWT ? A ? ? UNP P10619 LEU 318 DELETION ? 28 1 4MWT ? A ? ? UNP P10619 LEU 319 DELETION ? 29 1 4MWT ? A ? ? UNP P10619 ARG 320 DELETION ? 30 1 4MWT HIS A 423 ? UNP P10619 ? ? 'EXPRESSION TAG' 453 31 1 4MWT HIS A 424 ? UNP P10619 ? ? 'EXPRESSION TAG' 454 32 1 4MWT HIS A 425 ? UNP P10619 ? ? 'EXPRESSION TAG' 455 33 1 4MWT HIS A 426 ? UNP P10619 ? ? 'EXPRESSION TAG' 456 34 1 4MWT HIS A 427 ? UNP P10619 ? ? 'EXPRESSION TAG' 457 35 1 4MWT HIS A 428 ? UNP P10619 ? ? 'EXPRESSION TAG' 458 36 2 4MWT ? B ? ? UNP P10619 TYR 291 DELETION ? 37 2 4MWT ? B ? ? UNP P10619 GLU 292 DELETION ? 38 2 4MWT ? B ? ? UNP P10619 LYS 293 DELETION ? 39 2 4MWT ? B ? ? UNP P10619 ASP 294 DELETION ? 40 2 4MWT ? B ? ? UNP P10619 THR 295 DELETION ? 41 2 4MWT ? B ? ? UNP P10619 VAL 296 DELETION ? 42 2 4MWT ? B ? ? UNP P10619 VAL 297 DELETION ? 43 2 4MWT ? B ? ? UNP P10619 VAL 298 DELETION ? 44 2 4MWT ? B ? ? UNP P10619 GLN 299 DELETION ? 45 2 4MWT ? B ? ? UNP P10619 ASP 300 DELETION ? 46 2 4MWT ? B ? ? UNP P10619 LEU 301 DELETION ? 47 2 4MWT ? B ? ? UNP P10619 GLY 302 DELETION ? 48 2 4MWT ? B ? ? UNP P10619 ASN 303 DELETION ? 49 2 4MWT ? B ? ? UNP P10619 ILE 304 DELETION ? 50 2 4MWT ? B ? ? UNP P10619 PHE 305 DELETION ? 51 2 4MWT ? B ? ? UNP P10619 THR 306 DELETION ? 52 2 4MWT ? B ? ? UNP P10619 ARG 307 DELETION ? 53 2 4MWT ? B ? ? UNP P10619 LEU 308 DELETION ? 54 2 4MWT ? B ? ? UNP P10619 PRO 309 DELETION ? 55 2 4MWT ? B ? ? UNP P10619 LEU 310 DELETION ? 56 2 4MWT ? B ? ? UNP P10619 LYS 311 DELETION ? 57 2 4MWT ? B ? ? UNP P10619 ARG 312 DELETION ? 58 2 4MWT ? B ? ? UNP P10619 MET 313 DELETION ? 59 2 4MWT ? B ? ? UNP P10619 TRP 314 DELETION ? 60 2 4MWT ? B ? ? UNP P10619 HIS 315 DELETION ? 61 2 4MWT ? B ? ? UNP P10619 GLN 316 DELETION ? 62 2 4MWT ? B ? ? UNP P10619 ALA 317 DELETION ? 63 2 4MWT ? B ? ? UNP P10619 LEU 318 DELETION ? 64 2 4MWT ? B ? ? UNP P10619 LEU 319 DELETION ? 65 2 4MWT ? B ? ? UNP P10619 ARG 320 DELETION ? 66 2 4MWT HIS B 423 ? UNP P10619 ? ? 'EXPRESSION TAG' 453 67 2 4MWT HIS B 424 ? UNP P10619 ? ? 'EXPRESSION TAG' 454 68 2 4MWT HIS B 425 ? UNP P10619 ? ? 'EXPRESSION TAG' 455 69 2 4MWT HIS B 426 ? UNP P10619 ? ? 'EXPRESSION TAG' 456 70 2 4MWT HIS B 427 ? UNP P10619 ? ? 'EXPRESSION TAG' 457 71 2 4MWT HIS B 428 ? UNP P10619 ? ? 'EXPRESSION TAG' 458 72 # 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 BMA D-saccharide . BETA-D-MANNOSE ? 'C6 H12 O6' 180.156 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 4MWT _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.68 _exptl_crystal.density_percent_sol 54.08 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, SITTING DROP' _exptl_crystal_grow.temp 293 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 7.0 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '10% PEG 3350, 0.1M ammonium tartrate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K' # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector PIXEL _diffrn_detector.type 'PILATUS CBF' _diffrn_detector.pdbx_collection_date 2012-08-12 _diffrn_detector.details 'FOCUSING MIRRORS' # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'SI(111) DOUBLE CRYSTAL' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.9792 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'APS BEAMLINE 24-ID-C' _diffrn_source.pdbx_synchrotron_site APS _diffrn_source.pdbx_synchrotron_beamline 24-ID-C _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 0.9792 # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4MWT _reflns.observed_criterion_sigma_I 0.0 _reflns.observed_criterion_sigma_F 0.0 _reflns.d_resolution_low 50.000 _reflns.d_resolution_high 3.850 _reflns.number_obs 9724 _reflns.number_all 10218 _reflns.percent_possible_obs 95.200 _reflns.pdbx_Rmerge_I_obs 0.175 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 3.100 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 3.400 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? # loop_ _reflns_shell.pdbx_diffrn_id _reflns_shell.pdbx_ordinal _reflns_shell.d_res_high _reflns_shell.d_res_low _reflns_shell.percent_possible_all _reflns_shell.Rmerge_I_obs _reflns_shell.pdbx_Rsym_value _reflns_shell.meanI_over_sigI_obs _reflns_shell.pdbx_redundancy _reflns_shell.percent_possible_obs _reflns_shell.number_unique_all _reflns_shell.number_measured_all _reflns_shell.number_measured_obs _reflns_shell.number_unique_obs _reflns_shell.pdbx_chi_squared 1 1 3.850 3.920 98.000 0.527 ? ? 3.500 ? ? ? ? ? ? 1 2 3.920 3.990 98.600 0.504 ? ? 3.500 ? ? ? ? ? ? 1 3 3.990 4.060 96.500 0.447 ? ? 3.400 ? ? ? ? ? ? 1 4 4.060 4.150 96.000 0.374 ? ? 3.600 ? ? ? ? ? ? 1 5 4.150 4.240 94.700 0.349 ? ? 3.400 ? ? ? ? ? ? 1 6 4.240 4.340 94.200 0.270 ? ? 3.500 ? ? ? ? ? ? 1 7 4.340 4.440 92.000 0.253 ? ? 3.300 ? ? ? ? ? ? 1 8 4.440 4.560 84.000 0.249 ? ? 3.300 ? ? ? ? ? ? 1 9 4.560 4.700 95.600 0.214 ? ? 3.400 ? ? ? ? ? ? 1 10 4.700 4.850 99.000 0.201 ? ? 3.500 ? ? ? ? ? ? 1 11 4.850 5.020 98.800 0.199 ? ? 3.500 ? ? ? ? ? ? 1 12 5.020 5.220 99.000 0.199 ? ? 3.500 ? ? ? ? ? ? 1 13 5.220 5.460 98.600 0.199 ? ? 3.400 ? ? ? ? ? ? 1 14 5.460 5.750 97.500 0.196 ? ? 3.400 ? ? ? ? ? ? 1 15 5.750 6.110 94.200 0.174 ? ? 3.400 ? ? ? ? ? ? 1 16 6.110 6.580 91.100 0.169 ? ? 3.400 ? ? ? ? ? ? 1 17 6.580 7.240 88.500 0.135 ? ? 3.400 ? ? ? ? ? ? 1 18 7.240 8.280 98.700 0.090 ? ? 3.500 ? ? ? ? ? ? 1 19 8.280 10.420 97.700 0.057 ? ? 3.300 ? ? ? ? ? ? 1 20 10.420 50.000 91.200 0.051 ? ? 3.200 ? ? ? ? ? ? # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4MWT _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 9241 _refine.ls_number_reflns_all 10208 _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 45.86 _refine.ls_d_res_high 3.85 _refine.ls_percent_reflns_obs 95.09 _refine.ls_R_factor_obs 0.32275 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.32264 _refine.ls_R_factor_R_free 0.32501 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 4.8 _refine.ls_number_reflns_R_free 466 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min 1.000 _refine.occupancy_max 1.000 _refine.correlation_coeff_Fo_to_Fc 0.751 _refine.correlation_coeff_Fo_to_Fc_free 0.701 _refine.B_iso_mean 81.429 _refine.aniso_B[1][1] 0.66 _refine.aniso_B[2][2] 0.66 _refine.aniso_B[3][3] -2.14 _refine.aniso_B[1][2] 0.66 _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 ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model isotropic _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free 1.099 _refine.overall_SU_ML 0.966 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 153.587 _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.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 6596 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 81 _refine_hist.number_atoms_solvent 0 _refine_hist.number_atoms_total 6677 _refine_hist.d_res_high 3.85 _refine_hist.d_res_low 45.86 # 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 0.008 0.020 ? 6873 'X-RAY DIFFRACTION' ? r_bond_other_d ? ? ? ? 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.146 1.966 ? 9354 'X-RAY DIFFRACTION' ? r_angle_other_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 6.185 5.000 ? 822 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 38.431 24.824 ? 340 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 14.115 15.000 ? 1074 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 15.940 15.000 ? 26 'X-RAY DIFFRACTION' ? r_chiral_restr 0.063 0.200 ? 988 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.006 0.021 ? 5365 'X-RAY DIFFRACTION' ? r_gen_planes_other ? ? ? ? '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' ? # loop_ _refine_ls_restr_ncs.dom_id _refine_ls_restr_ncs.pdbx_auth_asym_id _refine_ls_restr_ncs.pdbx_number _refine_ls_restr_ncs.rms_dev_position _refine_ls_restr_ncs.weight_position _refine_ls_restr_ncs.pdbx_type _refine_ls_restr_ncs.pdbx_ens_id _refine_ls_restr_ncs.pdbx_ordinal _refine_ls_restr_ncs.pdbx_refine_id _refine_ls_restr_ncs.ncs_model_details _refine_ls_restr_ncs.rms_dev_B_iso _refine_ls_restr_ncs.weight_B_iso 1 A 605 0.05 0.05 'interatomic distance' 1 1 'X-RAY DIFFRACTION' ? ? ? 2 B 605 0.05 0.05 'interatomic distance' 1 2 '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 3.847 _refine_ls_shell.d_res_low 3.946 _refine_ls_shell.number_reflns_R_work 691 _refine_ls_shell.R_factor_R_work 0.355 _refine_ls_shell.percent_reflns_obs 98.10 _refine_ls_shell.R_factor_R_free 0.321 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 32 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.number_reflns_obs ? # loop_ _struct_ncs_dom.id _struct_ncs_dom.details _struct_ncs_dom.pdbx_ens_id 1 A 1 2 B 1 # loop_ _struct_ncs_dom_lim.dom_id _struct_ncs_dom_lim.beg_auth_asym_id _struct_ncs_dom_lim.beg_auth_seq_id _struct_ncs_dom_lim.end_auth_asym_id _struct_ncs_dom_lim.end_auth_seq_id _struct_ncs_dom_lim.pdbx_component_id _struct_ncs_dom_lim.pdbx_refine_code _struct_ncs_dom_lim.beg_label_asym_id _struct_ncs_dom_lim.beg_label_comp_id _struct_ncs_dom_lim.beg_label_seq_id _struct_ncs_dom_lim.beg_label_alt_id _struct_ncs_dom_lim.end_label_asym_id _struct_ncs_dom_lim.end_label_comp_id _struct_ncs_dom_lim.end_label_seq_id _struct_ncs_dom_lim.end_label_alt_id _struct_ncs_dom_lim.pdbx_ens_id _struct_ncs_dom_lim.selection_details 1 A 1 A 452 0 0 ? ? ? ? ? ? ? ? 1 ? 2 B 1 B 452 0 0 ? ? ? ? ? ? ? ? 1 ? # _struct_ncs_ens.id 1 _struct_ncs_ens.details ? # _struct.entry_id 4MWT _struct.title 'Crystal structure of human PPCA (trigonal crystal form 2)' _struct.pdbx_descriptor 'Lysosomal protective protein (E.C.3.4.16.5)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4MWT _struct_keywords.text ;cathepsin A, glycoprotein, serine protease, carboxypeptidase, protective protein, N-linked glycosylation, proteolytically activated form, lysosomal enzyme, HYDROLASE ; _struct_keywords.pdbx_keywords HYDROLASE # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 1 ? C N N 2 ? D N N 2 ? E N N 3 ? F N N 2 ? G N N 2 ? H N N 2 ? # 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 PRO A 2 ? GLU A 6 ? PRO A 2 GLU A 6 5 ? 5 HELX_P HELX_P2 2 ASP A 44 ? SER A 48 ? ASP A 44 SER A 48 5 ? 5 HELX_P HELX_P3 3 SER A 62 ? GLU A 69 ? SER A 62 GLU A 69 1 ? 8 HELX_P HELX_P4 4 SER A 88 ? ILE A 92 ? SER A 88 ILE A 92 5 ? 5 HELX_P HELX_P5 5 ASN A 117 ? PHE A 136 ? ASN A 117 PHE A 136 1 ? 20 HELX_P HELX_P6 6 PRO A 137 ? LYS A 140 ? PRO A 137 LYS A 140 5 ? 4 HELX_P HELX_P7 7 TYR A 151 ? GLN A 165 ? TYR A 151 GLN A 165 1 ? 15 HELX_P HELX_P8 8 SER A 182 ? HIS A 197 ? SER A 182 HIS A 197 1 ? 16 HELX_P HELX_P9 9 LEU A 200 ? CYS A 213 ? LEU A 200 CYS A 213 1 ? 14 HELX_P HELX_P10 10 ASP A 225 ? ASN A 241 ? ASP A 225 ASN A 241 1 ? 17 HELX_P HELX_P11 11 THR A 276 ? ASN A 285 ? THR A 306 ASN A 315 1 ? 10 HELX_P HELX_P12 12 ASN A 285 ? LEU A 292 ? ASN A 315 LEU A 322 1 ? 8 HELX_P HELX_P13 13 ASN A 305 ? GLN A 311 ? ASN A 335 GLN A 341 1 ? 7 HELX_P HELX_P14 14 MET A 319 ? GLN A 330 ? MET A 349 GLN A 360 1 ? 12 HELX_P HELX_P15 15 ASN A 346 ? SER A 356 ? ASN A 376 SER A 386 1 ? 11 HELX_P HELX_P16 16 MET A 400 ? LYS A 405 ? MET A 430 LYS A 435 1 ? 6 HELX_P HELX_P17 17 LYS A 405 ? ASN A 418 ? LYS A 435 ASN A 448 1 ? 14 HELX_P HELX_P18 18 PRO B 2 ? GLU B 6 ? PRO B 2 GLU B 6 5 ? 5 HELX_P HELX_P19 19 ASP B 44 ? SER B 48 ? ASP B 44 SER B 48 5 ? 5 HELX_P HELX_P20 20 SER B 62 ? GLU B 69 ? SER B 62 GLU B 69 1 ? 8 HELX_P HELX_P21 21 SER B 88 ? ILE B 92 ? SER B 88 ILE B 92 5 ? 5 HELX_P HELX_P22 22 ASN B 117 ? PHE B 136 ? ASN B 117 PHE B 136 1 ? 20 HELX_P HELX_P23 23 PRO B 137 ? LYS B 140 ? PRO B 137 LYS B 140 5 ? 4 HELX_P HELX_P24 24 TYR B 151 ? GLN B 165 ? TYR B 151 GLN B 165 1 ? 15 HELX_P HELX_P25 25 SER B 182 ? HIS B 197 ? SER B 182 HIS B 197 1 ? 16 HELX_P HELX_P26 26 LEU B 200 ? CYS B 212 ? LEU B 200 CYS B 212 1 ? 13 HELX_P HELX_P27 27 ASP B 225 ? ASN B 241 ? ASP B 225 ASN B 241 1 ? 17 HELX_P HELX_P28 28 THR B 276 ? ASN B 285 ? THR B 306 ASN B 315 1 ? 10 HELX_P HELX_P29 29 ASN B 285 ? LEU B 292 ? ASN B 315 LEU B 322 1 ? 8 HELX_P HELX_P30 30 ASN B 305 ? GLN B 311 ? ASN B 335 GLN B 341 1 ? 7 HELX_P HELX_P31 31 MET B 319 ? GLN B 330 ? MET B 349 GLN B 360 1 ? 12 HELX_P HELX_P32 32 ASN B 346 ? SER B 356 ? ASN B 376 SER B 386 1 ? 11 HELX_P HELX_P33 33 MET B 400 ? LYS B 405 ? MET B 430 LYS B 435 1 ? 6 HELX_P HELX_P34 34 LYS B 405 ? ASN B 418 ? LYS B 435 ASN B 448 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 60 SG ? ? ? 1_555 A CYS 304 SG ? ? A CYS 60 A CYS 334 1_555 ? ? ? ? ? ? ? 2.059 ? disulf2 disulf ? ? A CYS 212 SG ? ? ? 1_555 A CYS 228 SG ? ? A CYS 212 A CYS 228 1_555 ? ? ? ? ? ? ? 2.019 ? disulf3 disulf ? ? A CYS 213 SG ? ? ? 1_555 A CYS 218 SG ? ? A CYS 213 A CYS 218 1_555 ? ? ? ? ? ? ? 2.044 ? disulf4 disulf ? ? A CYS 253 SG ? ? ? 1_555 A CYS 273 SG ? ? A CYS 253 A CYS 303 1_555 ? ? ? ? ? ? ? 2.052 ? disulf5 disulf ? ? B CYS 60 SG ? ? ? 1_555 B CYS 304 SG ? ? B CYS 60 B CYS 334 1_555 ? ? ? ? ? ? ? 2.047 ? disulf6 disulf ? ? B CYS 212 SG ? ? ? 1_555 B CYS 228 SG ? ? B CYS 212 B CYS 228 1_555 ? ? ? ? ? ? ? 2.046 ? disulf7 disulf ? ? B CYS 213 SG ? ? ? 1_555 B CYS 218 SG ? ? B CYS 213 B CYS 218 1_555 ? ? ? ? ? ? ? 2.046 ? disulf8 disulf ? ? B CYS 253 SG ? ? ? 1_555 B CYS 273 SG ? ? B CYS 253 B CYS 303 1_555 ? ? ? ? ? ? ? 2.042 ? covale1 covale ? ? C NAG . O4 ? ? ? 1_555 D NAG . C1 ? ? A NAG 501 A NAG 502 1_555 ? ? ? ? ? ? ? 1.433 ? covale2 covale ? ? D NAG . O4 ? ? ? 1_555 E BMA . C1 ? ? A NAG 502 A BMA 503 1_555 ? ? ? ? ? ? ? 1.435 ? covale3 covale ? ? B ASN 275 ND2 ? ? ? 1_555 H NAG . C1 ? ? B ASN 305 B NAG 502 1_555 ? ? ? ? ? ? ? 1.435 ? covale4 covale ? ? A ASN 117 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 117 A NAG 501 1_555 ? ? ? ? ? ? ? 1.436 ? covale5 covale ? ? B ASN 117 ND2 ? ? ? 1_555 G NAG . C1 ? ? B ASN 117 B NAG 501 1_555 ? ? ? ? ? ? ? 1.440 ? covale6 covale ? ? A ASN 275 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 305 A NAG 504 1_555 ? ? ? ? ? ? ? 1.471 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 GLY 57 A . ? GLY 57 A PRO 58 A ? PRO 58 A 1 -8.05 2 SER 100 A . ? SER 100 A PRO 101 A ? PRO 101 A 1 -0.41 3 GLY 57 B . ? GLY 57 B PRO 58 B ? PRO 58 B 1 -7.92 4 SER 100 B . ? SER 100 B PRO 101 B ? PRO 101 B 1 -2.81 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 3 ? B ? 10 ? C ? 2 ? D ? 3 ? E ? 10 ? F ? 2 ? G ? 2 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel A 2 3 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? parallel B 4 5 ? parallel B 5 6 ? parallel B 6 7 ? parallel B 7 8 ? parallel B 8 9 ? anti-parallel B 9 10 ? anti-parallel C 1 2 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? anti-parallel E 1 2 ? anti-parallel E 2 3 ? anti-parallel E 3 4 ? parallel E 4 5 ? parallel E 5 6 ? parallel E 6 7 ? parallel E 7 8 ? parallel E 8 9 ? anti-parallel E 9 10 ? anti-parallel F 1 2 ? anti-parallel G 1 2 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 GLN A 21 ? LYS A 27 ? GLN A 21 LYS A 27 A 2 LYS A 32 ? VAL A 39 ? LYS A 32 VAL A 39 A 3 TYR A 108 ? SER A 109 ? TYR A 108 SER A 109 B 1 GLN A 21 ? LYS A 27 ? GLN A 21 LYS A 27 B 2 LYS A 32 ? VAL A 39 ? LYS A 32 VAL A 39 B 3 ASN A 94 ? LEU A 98 ? ASN A 94 LEU A 98 B 4 VAL A 50 ? LEU A 54 ? VAL A 50 LEU A 54 B 5 LEU A 144 ? GLU A 149 ? LEU A 144 GLU A 149 B 6 LEU A 171 ? GLY A 177 ? LEU A 171 GLY A 177 B 7 GLN A 333 ? GLY A 339 ? GLN A 363 GLY A 369 B 8 ILE A 389 ? ILE A 394 ? ILE A 419 ILE A 424 B 9 GLY A 376 ? PHE A 386 ? GLY A 406 PHE A 416 B 10 ARG A 366 ? TYR A 372 ? ARG A 396 TYR A 402 C 1 PHE A 73 ? VAL A 75 ? PHE A 73 VAL A 75 C 2 LEU A 82 ? TYR A 84 ? LEU A 82 TYR A 84 D 1 GLN B 21 ? LYS B 27 ? GLN B 21 LYS B 27 D 2 LYS B 32 ? VAL B 39 ? LYS B 32 VAL B 39 D 3 TYR B 108 ? SER B 109 ? TYR B 108 SER B 109 E 1 GLN B 21 ? LYS B 27 ? GLN B 21 LYS B 27 E 2 LYS B 32 ? VAL B 39 ? LYS B 32 VAL B 39 E 3 ASN B 94 ? LEU B 98 ? ASN B 94 LEU B 98 E 4 VAL B 50 ? LEU B 54 ? VAL B 50 LEU B 54 E 5 LEU B 144 ? GLU B 149 ? LEU B 144 GLU B 149 E 6 LEU B 171 ? GLY B 177 ? LEU B 171 GLY B 177 E 7 GLN B 333 ? GLY B 339 ? GLN B 363 GLY B 369 E 8 ILE B 389 ? ILE B 394 ? ILE B 419 ILE B 424 E 9 GLY B 376 ? PHE B 386 ? GLY B 406 PHE B 416 E 10 ARG B 366 ? TYR B 372 ? ARG B 396 TYR B 402 F 1 PHE B 73 ? VAL B 75 ? PHE B 73 VAL B 75 F 2 LEU B 82 ? TYR B 84 ? LEU B 82 TYR B 84 G 1 CYS B 213 ? SER B 214 ? CYS B 213 SER B 214 G 2 LYS B 217 ? CYS B 218 ? LYS B 217 CYS B 218 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 N GLY A 24 ? N GLY A 24 O TYR A 36 ? O TYR A 36 A 2 3 N HIS A 33 ? N HIS A 33 O TYR A 108 ? O TYR A 108 B 1 2 N GLY A 24 ? N GLY A 24 O TYR A 36 ? O TYR A 36 B 2 3 N TRP A 37 ? N TRP A 37 O TYR A 97 ? O TYR A 97 B 3 4 O LEU A 96 ? O LEU A 96 N VAL A 51 ? N VAL A 51 B 4 5 N VAL A 50 ? N VAL A 50 O PHE A 145 ? O PHE A 145 B 5 6 N LEU A 144 ? N LEU A 144 O GLN A 172 ? O GLN A 172 B 6 7 N VAL A 176 ? N VAL A 176 O LEU A 335 ? O LEU A 365 B 7 8 N ASN A 338 ? N ASN A 368 O ILE A 394 ? O ILE A 424 B 8 9 O THR A 393 ? O THR A 423 N PHE A 382 ? N PHE A 412 B 9 10 O VAL A 383 ? O VAL A 413 N ARG A 366 ? N ARG A 396 C 1 2 N LEU A 74 ? N LEU A 74 O GLU A 83 ? O GLU A 83 D 1 2 N GLY B 24 ? N GLY B 24 O TYR B 36 ? O TYR B 36 D 2 3 N HIS B 33 ? N HIS B 33 O TYR B 108 ? O TYR B 108 E 1 2 N GLY B 24 ? N GLY B 24 O TYR B 36 ? O TYR B 36 E 2 3 N TRP B 37 ? N TRP B 37 O TYR B 97 ? O TYR B 97 E 3 4 O LEU B 96 ? O LEU B 96 N VAL B 51 ? N VAL B 51 E 4 5 N VAL B 50 ? N VAL B 50 O PHE B 145 ? O PHE B 145 E 5 6 N LEU B 144 ? N LEU B 144 O GLN B 172 ? O GLN B 172 E 6 7 N VAL B 176 ? N VAL B 176 O LEU B 335 ? O LEU B 365 E 7 8 N ASN B 338 ? N ASN B 368 O ILE B 394 ? O ILE B 424 E 8 9 O PHE B 391 ? O PHE B 421 N LYS B 384 ? N LYS B 414 E 9 10 O VAL B 383 ? O VAL B 413 N ARG B 366 ? N ARG B 396 F 1 2 N LEU B 74 ? N LEU B 74 O GLU B 83 ? O GLU B 83 G 1 2 N SER B 214 ? N SER B 214 O LYS B 217 ? O LYS B 217 # 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 ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 501' AC2 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 502' AC3 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE BMA A 503' AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 504' AC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG B 501' AC6 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG B 502' # 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 5 ASN A 117 ? ASN A 117 . ? 1_555 ? 2 AC1 5 GLU A 120 ? GLU A 120 . ? 1_555 ? 3 AC1 5 ARG A 313 ? ARG A 343 . ? 1_555 ? 4 AC1 5 LEU A 315 ? LEU A 345 . ? 1_555 ? 5 AC1 5 NAG D . ? NAG A 502 . ? 1_555 ? 6 AC2 2 NAG C . ? NAG A 501 . ? 1_555 ? 7 AC2 2 BMA E . ? BMA A 503 . ? 1_555 ? 8 AC3 2 GLN A 165 ? GLN A 165 . ? 4_555 ? 9 AC3 2 NAG D . ? NAG A 502 . ? 1_555 ? 10 AC4 4 PRO A 77 ? PRO A 77 . ? 1_555 ? 11 AC4 4 GLY A 255 ? GLY A 255 . ? 1_555 ? 12 AC4 4 ASN A 275 ? ASN A 305 . ? 1_555 ? 13 AC4 4 THR A 277 ? THR A 307 . ? 1_555 ? 14 AC5 4 ASN B 117 ? ASN B 117 . ? 1_555 ? 15 AC5 4 GLU B 120 ? GLU B 120 . ? 1_555 ? 16 AC5 4 ARG B 313 ? ARG B 343 . ? 1_555 ? 17 AC5 4 LEU B 315 ? LEU B 345 . ? 1_555 ? 18 AC6 3 PRO B 77 ? PRO B 77 . ? 1_555 ? 19 AC6 3 ASN B 275 ? ASN B 305 . ? 1_555 ? 20 AC6 3 THR B 277 ? THR B 307 . ? 1_555 ? # _atom_sites.entry_id 4MWT _atom_sites.fract_transf_matrix[1][1] 0.007431 _atom_sites.fract_transf_matrix[1][2] 0.004290 _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] 0.008580 _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] 0.010022 _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 . ALA A 1 1 ? 18.440 -0.806 -12.928 1.00 92.17 ? 1 ALA A N 1 ATOM 2 C CA . ALA A 1 1 ? 19.415 -1.373 -11.950 1.00 87.32 ? 1 ALA A CA 1 ATOM 3 C C . ALA A 1 1 ? 19.669 -0.414 -10.781 1.00 89.70 ? 1 ALA A C 1 ATOM 4 O O . ALA A 1 1 ? 20.006 0.761 -11.000 1.00 87.51 ? 1 ALA A O 1 ATOM 5 C CB . ALA A 1 1 ? 20.717 -1.716 -12.644 1.00 84.37 ? 1 ALA A CB 1 ATOM 6 N N . PRO A 1 2 ? 19.497 -0.909 -9.531 1.00 88.26 ? 2 PRO A N 1 ATOM 7 C CA . PRO A 1 2 ? 19.800 -0.115 -8.340 1.00 87.68 ? 2 PRO A CA 1 ATOM 8 C C . PRO A 1 2 ? 21.298 -0.049 -8.125 1.00 88.32 ? 2 PRO A C 1 ATOM 9 O O . PRO A 1 2 ? 21.922 -1.044 -7.776 1.00 88.87 ? 2 PRO A O 1 ATOM 10 C CB . PRO A 1 2 ? 19.111 -0.879 -7.213 1.00 86.29 ? 2 PRO A CB 1 ATOM 11 C CG . PRO A 1 2 ? 19.045 -2.283 -7.688 1.00 83.52 ? 2 PRO A CG 1 ATOM 12 C CD . PRO A 1 2 ? 19.007 -2.252 -9.186 1.00 83.33 ? 2 PRO A CD 1 ATOM 13 N N . ASP A 1 3 ? 21.860 1.120 -8.375 1.00 92.59 ? 3 ASP A N 1 ATOM 14 C CA . ASP A 1 3 ? 23.302 1.299 -8.439 1.00 94.45 ? 3 ASP A CA 1 ATOM 15 C C . ASP A 1 3 ? 23.960 0.959 -7.105 1.00 92.19 ? 3 ASP A C 1 ATOM 16 O O . ASP A 1 3 ? 25.023 0.334 -7.068 1.00 87.37 ? 3 ASP A O 1 ATOM 17 C CB . ASP A 1 3 ? 23.639 2.732 -8.877 1.00 96.56 ? 3 ASP A CB 1 ATOM 18 C CG . ASP A 1 3 ? 23.218 3.018 -10.317 1.00 99.89 ? 3 ASP A CG 1 ATOM 19 O OD1 . ASP A 1 3 ? 22.000 2.976 -10.619 1.00 106.53 ? 3 ASP A OD1 1 ATOM 20 O OD2 . ASP A 1 3 ? 24.107 3.279 -11.148 1.00 99.83 ? 3 ASP A OD2 1 ATOM 21 N N . GLN A 1 4 ? 23.303 1.358 -6.023 1.00 93.52 ? 4 GLN A N 1 ATOM 22 C CA . GLN A 1 4 ? 23.817 1.171 -4.663 1.00 92.92 ? 4 GLN A CA 1 ATOM 23 C C . GLN A 1 4 ? 23.975 -0.307 -4.302 1.00 84.83 ? 4 GLN A C 1 ATOM 24 O O . GLN A 1 4 ? 24.804 -0.666 -3.474 1.00 83.42 ? 4 GLN A O 1 ATOM 25 C CB . GLN A 1 4 ? 22.928 1.920 -3.639 1.00 96.78 ? 4 GLN A CB 1 ATOM 26 C CG . GLN A 1 4 ? 21.572 1.281 -3.311 1.00 100.87 ? 4 GLN A CG 1 ATOM 27 C CD . GLN A 1 4 ? 20.413 1.740 -4.200 1.00 103.75 ? 4 GLN A CD 1 ATOM 28 O OE1 . GLN A 1 4 ? 20.609 2.249 -5.307 1.00 99.57 ? 4 GLN A OE1 1 ATOM 29 N NE2 . GLN A 1 4 ? 19.193 1.534 -3.717 1.00 101.04 ? 4 GLN A NE2 1 ATOM 30 N N . ASP A 1 5 ? 23.166 -1.153 -4.923 1.00 80.12 ? 5 ASP A N 1 ATOM 31 C CA . ASP A 1 5 ? 23.280 -2.591 -4.753 1.00 75.34 ? 5 ASP A CA 1 ATOM 32 C C . ASP A 1 5 ? 24.420 -3.210 -5.558 1.00 77.45 ? 5 ASP A C 1 ATOM 33 O O . ASP A 1 5 ? 24.724 -4.377 -5.365 1.00 73.10 ? 5 ASP A O 1 ATOM 34 C CB . ASP A 1 5 ? 21.976 -3.273 -5.153 1.00 74.36 ? 5 ASP A CB 1 ATOM 35 C CG . ASP A 1 5 ? 20.860 -3.048 -4.150 1.00 75.47 ? 5 ASP A CG 1 ATOM 36 O OD1 . ASP A 1 5 ? 21.060 -2.327 -3.148 1.00 76.50 ? 5 ASP A OD1 1 ATOM 37 O OD2 . ASP A 1 5 ? 19.761 -3.594 -4.375 1.00 75.05 ? 5 ASP A OD2 1 ATOM 38 N N . GLU A 1 6 ? 25.036 -2.460 -6.474 1.00 83.62 ? 6 GLU A N 1 ATOM 39 C CA . GLU A 1 6 ? 26.112 -3.016 -7.295 1.00 82.98 ? 6 GLU A CA 1 ATOM 40 C C . GLU A 1 6 ? 27.209 -3.503 -6.383 1.00 79.66 ? 6 GLU A C 1 ATOM 41 O O . GLU A 1 6 ? 27.485 -2.884 -5.363 1.00 77.36 ? 6 GLU A O 1 ATOM 42 C CB . GLU A 1 6 ? 26.668 -2.005 -8.312 1.00 89.05 ? 6 GLU A CB 1 ATOM 43 C CG . GLU A 1 6 ? 27.859 -2.539 -9.123 1.00 92.89 ? 6 GLU A CG 1 ATOM 44 C CD . GLU A 1 6 ? 27.995 -1.961 -10.534 1.00 96.00 ? 6 GLU A CD 1 ATOM 45 O OE1 . GLU A 1 6 ? 27.660 -0.770 -10.762 1.00 92.13 ? 6 GLU A OE1 1 ATOM 46 O OE2 . GLU A 1 6 ? 28.450 -2.722 -11.423 1.00 92.91 ? 6 GLU A OE2 1 ATOM 47 N N . ILE A 1 7 ? 27.799 -4.636 -6.747 1.00 80.66 ? 7 ILE A N 1 ATOM 48 C CA . ILE A 1 7 ? 28.900 -5.230 -6.002 1.00 80.30 ? 7 ILE A CA 1 ATOM 49 C C . ILE A 1 7 ? 30.203 -4.769 -6.629 1.00 82.72 ? 7 ILE A C 1 ATOM 50 O O . ILE A 1 7 ? 30.469 -5.057 -7.792 1.00 86.73 ? 7 ILE A O 1 ATOM 51 C CB . ILE A 1 7 ? 28.842 -6.758 -6.060 1.00 78.30 ? 7 ILE A CB 1 ATOM 52 C CG1 . ILE A 1 7 ? 27.507 -7.254 -5.536 1.00 78.60 ? 7 ILE A CG1 1 ATOM 53 C CG2 . ILE A 1 7 ? 29.978 -7.365 -5.256 1.00 79.04 ? 7 ILE A CG2 1 ATOM 54 C CD1 . ILE A 1 7 ? 27.273 -8.719 -5.813 1.00 80.37 ? 7 ILE A CD1 1 ATOM 55 N N . GLN A 1 8 ? 31.015 -4.069 -5.857 1.00 88.23 ? 8 GLN A N 1 ATOM 56 C CA . GLN A 1 8 ? 32.187 -3.417 -6.405 1.00 94.46 ? 8 GLN A CA 1 ATOM 57 C C . GLN A 1 8 ? 33.370 -4.365 -6.443 1.00 95.46 ? 8 GLN A C 1 ATOM 58 O O . GLN A 1 8 ? 33.688 -4.896 -7.504 1.00 105.32 ? 8 GLN A O 1 ATOM 59 C CB . GLN A 1 8 ? 32.511 -2.142 -5.627 1.00 98.08 ? 8 GLN A CB 1 ATOM 60 C CG . GLN A 1 8 ? 31.497 -1.028 -5.834 1.00 102.95 ? 8 GLN A CG 1 ATOM 61 C CD . GLN A 1 8 ? 31.419 -0.573 -7.288 1.00 107.69 ? 8 GLN A CD 1 ATOM 62 O OE1 . GLN A 1 8 ? 32.409 -0.614 -8.015 1.00 110.38 ? 8 GLN A OE1 1 ATOM 63 N NE2 . GLN A 1 8 ? 30.237 -0.151 -7.721 1.00 109.56 ? 8 GLN A NE2 1 ATOM 64 N N . ARG A 1 9 ? 34.033 -4.563 -5.309 1.00 93.17 ? 9 ARG A N 1 ATOM 65 C CA . ARG A 1 9 ? 35.177 -5.457 -5.247 1.00 95.33 ? 9 ARG A CA 1 ATOM 66 C C . ARG A 1 9 ? 34.867 -6.575 -4.301 1.00 93.64 ? 9 ARG A C 1 ATOM 67 O O . ARG A 1 9 ? 34.678 -6.347 -3.108 1.00 93.42 ? 9 ARG A O 1 ATOM 68 C CB . ARG A 1 9 ? 36.439 -4.730 -4.788 1.00 98.21 ? 9 ARG A CB 1 ATOM 69 C CG . ARG A 1 9 ? 36.877 -3.617 -5.716 1.00 102.03 ? 9 ARG A CG 1 ATOM 70 C CD . ARG A 1 9 ? 37.405 -4.135 -7.051 1.00 109.23 ? 9 ARG A CD 1 ATOM 71 N NE . ARG A 1 9 ? 38.819 -4.508 -7.070 1.00 110.10 ? 9 ARG A NE 1 ATOM 72 C CZ . ARG A 1 9 ? 39.784 -3.841 -7.699 1.00 108.97 ? 9 ARG A CZ 1 ATOM 73 N NH1 . ARG A 1 9 ? 39.527 -2.718 -8.361 1.00 107.92 ? 9 ARG A NH1 1 ATOM 74 N NH2 . ARG A 1 9 ? 41.027 -4.302 -7.654 1.00 106.57 ? 9 ARG A NH2 1 ATOM 75 N N . LEU A 1 10 ? 34.819 -7.785 -4.834 1.00 87.34 ? 10 LEU A N 1 ATOM 76 C CA . LEU A 1 10 ? 34.447 -8.932 -4.040 1.00 83.59 ? 10 LEU A CA 1 ATOM 77 C C . LEU A 1 10 ? 35.706 -9.669 -3.528 1.00 79.85 ? 10 LEU A C 1 ATOM 78 O O . LEU A 1 10 ? 36.473 -10.210 -4.320 1.00 83.54 ? 10 LEU A O 1 ATOM 79 C CB . LEU A 1 10 ? 33.557 -9.845 -4.878 1.00 80.21 ? 10 LEU A CB 1 ATOM 80 C CG . LEU A 1 10 ? 32.691 -10.845 -4.129 1.00 75.44 ? 10 LEU A CG 1 ATOM 81 C CD1 . LEU A 1 10 ? 31.663 -10.134 -3.275 1.00 75.14 ? 10 LEU A CD1 1 ATOM 82 C CD2 . LEU A 1 10 ? 32.022 -11.776 -5.123 1.00 73.49 ? 10 LEU A CD2 1 ATOM 83 N N . PRO A 1 11 ? 35.924 -9.689 -2.200 1.00 75.50 ? 11 PRO A N 1 ATOM 84 C CA . PRO A 1 11 ? 37.090 -10.362 -1.624 1.00 75.45 ? 11 PRO A CA 1 ATOM 85 C C . PRO A 1 11 ? 37.254 -11.813 -2.067 1.00 77.34 ? 11 PRO A C 1 ATOM 86 O O . PRO A 1 11 ? 36.301 -12.572 -2.031 1.00 80.33 ? 11 PRO A O 1 ATOM 87 C CB . PRO A 1 11 ? 36.815 -10.315 -0.119 1.00 72.38 ? 11 PRO A CB 1 ATOM 88 C CG . PRO A 1 11 ? 35.953 -9.140 0.067 1.00 73.87 ? 11 PRO A CG 1 ATOM 89 C CD . PRO A 1 11 ? 35.113 -9.026 -1.166 1.00 74.10 ? 11 PRO A CD 1 ATOM 90 N N . GLY A 1 12 ? 38.461 -12.195 -2.460 1.00 82.05 ? 12 GLY A N 1 ATOM 91 C CA . GLY A 1 12 ? 38.754 -13.578 -2.831 1.00 82.52 ? 12 GLY A CA 1 ATOM 92 C C . GLY A 1 12 ? 38.876 -13.789 -4.327 1.00 84.86 ? 12 GLY A C 1 ATOM 93 O O . GLY A 1 12 ? 39.187 -14.886 -4.775 1.00 85.67 ? 12 GLY A O 1 ATOM 94 N N . LEU A 1 13 ? 38.626 -12.736 -5.098 1.00 87.14 ? 13 LEU A N 1 ATOM 95 C CA . LEU A 1 13 ? 38.889 -12.749 -6.523 1.00 87.59 ? 13 LEU A CA 1 ATOM 96 C C . LEU A 1 13 ? 40.261 -12.149 -6.830 1.00 90.28 ? 13 LEU A C 1 ATOM 97 O O . LEU A 1 13 ? 40.584 -11.060 -6.382 1.00 93.38 ? 13 LEU A O 1 ATOM 98 C CB . LEU A 1 13 ? 37.810 -11.969 -7.266 1.00 87.71 ? 13 LEU A CB 1 ATOM 99 C CG . LEU A 1 13 ? 36.443 -12.639 -7.375 1.00 87.10 ? 13 LEU A CG 1 ATOM 100 C CD1 . LEU A 1 13 ? 35.483 -11.733 -8.128 1.00 87.15 ? 13 LEU A CD1 1 ATOM 101 C CD2 . LEU A 1 13 ? 36.541 -13.991 -8.061 1.00 87.96 ? 13 LEU A CD2 1 ATOM 102 N N . ALA A 1 14 ? 41.063 -12.867 -7.597 1.00 93.00 ? 14 ALA A N 1 ATOM 103 C CA . ALA A 1 14 ? 42.300 -12.318 -8.122 1.00 95.81 ? 14 ALA A CA 1 ATOM 104 C C . ALA A 1 14 ? 41.994 -11.183 -9.085 1.00 96.88 ? 14 ALA A C 1 ATOM 105 O O . ALA A 1 14 ? 42.502 -10.085 -8.920 1.00 98.85 ? 14 ALA A O 1 ATOM 106 C CB . ALA A 1 14 ? 43.106 -13.392 -8.824 1.00 96.83 ? 14 ALA A CB 1 ATOM 107 N N . LYS A 1 15 ? 41.160 -11.448 -10.088 1.00 99.29 ? 15 LYS A N 1 ATOM 108 C CA . LYS A 1 15 ? 40.792 -10.432 -11.076 1.00 101.12 ? 15 LYS A CA 1 ATOM 109 C C . LYS A 1 15 ? 39.299 -10.219 -11.058 1.00 95.05 ? 15 LYS A C 1 ATOM 110 O O . LYS A 1 15 ? 38.528 -11.158 -10.955 1.00 92.26 ? 15 LYS A O 1 ATOM 111 C CB . LYS A 1 15 ? 41.250 -10.817 -12.488 1.00 107.45 ? 15 LYS A CB 1 ATOM 112 C CG . LYS A 1 15 ? 40.325 -11.785 -13.208 1.00 110.84 ? 15 LYS A CG 1 ATOM 113 C CD . LYS A 1 15 ? 41.017 -12.544 -14.325 1.00 114.69 ? 15 LYS A CD 1 ATOM 114 C CE . LYS A 1 15 ? 40.129 -13.672 -14.818 1.00 115.35 ? 15 LYS A CE 1 ATOM 115 N NZ . LYS A 1 15 ? 40.895 -14.651 -15.625 1.00 120.98 ? 15 LYS A NZ 1 ATOM 116 N N . GLN A 1 16 ? 38.896 -8.967 -11.185 1.00 96.41 ? 16 GLN A N 1 ATOM 117 C CA . GLN A 1 16 ? 37.495 -8.605 -11.089 1.00 89.93 ? 16 GLN A CA 1 ATOM 118 C C . GLN A 1 16 ? 36.688 -9.149 -12.262 1.00 81.60 ? 16 GLN A C 1 ATOM 119 O O . GLN A 1 16 ? 37.241 -9.362 -13.331 1.00 80.02 ? 16 GLN A O 1 ATOM 120 C CB . GLN A 1 16 ? 37.344 -7.086 -10.961 1.00 93.19 ? 16 GLN A CB 1 ATOM 121 C CG . GLN A 1 16 ? 37.790 -6.556 -9.599 1.00 96.47 ? 16 GLN A CG 1 ATOM 122 C CD . GLN A 1 16 ? 36.988 -7.143 -8.437 1.00 99.65 ? 16 GLN A CD 1 ATOM 123 O OE1 . GLN A 1 16 ? 35.754 -7.106 -8.429 1.00 94.67 ? 16 GLN A OE1 1 ATOM 124 N NE2 . GLN A 1 16 ? 37.690 -7.704 -7.458 1.00 101.32 ? 16 GLN A NE2 1 ATOM 125 N N . PRO A 1 17 ? 35.385 -9.406 -12.047 1.00 78.70 ? 17 PRO A N 1 ATOM 126 C CA . PRO A 1 17 ? 34.473 -9.935 -13.071 1.00 76.12 ? 17 PRO A CA 1 ATOM 127 C C . PRO A 1 17 ? 34.297 -9.024 -14.259 1.00 73.90 ? 17 PRO A C 1 ATOM 128 O O . PRO A 1 17 ? 34.311 -7.818 -14.103 1.00 75.63 ? 17 PRO A O 1 ATOM 129 C CB . PRO A 1 17 ? 33.128 -10.027 -12.344 1.00 75.02 ? 17 PRO A CB 1 ATOM 130 C CG . PRO A 1 17 ? 33.462 -10.050 -10.901 1.00 76.13 ? 17 PRO A CG 1 ATOM 131 C CD . PRO A 1 17 ? 34.697 -9.224 -10.756 1.00 78.95 ? 17 PRO A CD 1 ATOM 132 N N . SER A 1 18 ? 34.101 -9.609 -15.431 1.00 72.87 ? 18 SER A N 1 ATOM 133 C CA . SER A 1 18 ? 33.800 -8.850 -16.636 1.00 74.46 ? 18 SER A CA 1 ATOM 134 C C . SER A 1 18 ? 32.325 -8.449 -16.712 1.00 75.51 ? 18 SER A C 1 ATOM 135 O O . SER A 1 18 ? 31.934 -7.693 -17.594 1.00 78.09 ? 18 SER A O 1 ATOM 136 C CB . SER A 1 18 ? 34.170 -9.667 -17.882 1.00 74.64 ? 18 SER A CB 1 ATOM 137 O OG . SER A 1 18 ? 33.277 -10.750 -18.086 1.00 72.36 ? 18 SER A OG 1 ATOM 138 N N . PHE A 1 19 ? 31.516 -8.957 -15.788 1.00 73.46 ? 19 PHE A N 1 ATOM 139 C CA . PHE A 1 19 ? 30.066 -8.765 -15.822 1.00 72.09 ? 19 PHE A CA 1 ATOM 140 C C . PHE A 1 19 ? 29.635 -8.016 -14.579 1.00 75.29 ? 19 PHE A C 1 ATOM 141 O O . PHE A 1 19 ? 30.289 -8.092 -13.533 1.00 78.21 ? 19 PHE A O 1 ATOM 142 C CB . PHE A 1 19 ? 29.346 -10.108 -15.904 1.00 69.88 ? 19 PHE A CB 1 ATOM 143 C CG . PHE A 1 19 ? 29.741 -11.079 -14.823 1.00 70.45 ? 19 PHE A CG 1 ATOM 144 C CD1 . PHE A 1 19 ? 29.111 -11.057 -13.593 1.00 70.43 ? 19 PHE A CD1 1 ATOM 145 C CD2 . PHE A 1 19 ? 30.750 -12.006 -15.028 1.00 72.17 ? 19 PHE A CD2 1 ATOM 146 C CE1 . PHE A 1 19 ? 29.453 -11.943 -12.590 1.00 67.19 ? 19 PHE A CE1 1 ATOM 147 C CE2 . PHE A 1 19 ? 31.109 -12.884 -14.021 1.00 72.22 ? 19 PHE A CE2 1 ATOM 148 C CZ . PHE A 1 19 ? 30.462 -12.845 -12.800 1.00 69.67 ? 19 PHE A CZ 1 ATOM 149 N N . ARG A 1 20 ? 28.550 -7.269 -14.692 1.00 77.26 ? 20 ARG A N 1 ATOM 150 C CA . ARG A 1 20 ? 27.989 -6.620 -13.527 1.00 78.79 ? 20 ARG A CA 1 ATOM 151 C C . ARG A 1 20 ? 27.248 -7.639 -12.647 1.00 74.84 ? 20 ARG A C 1 ATOM 152 O O . ARG A 1 20 ? 26.724 -8.650 -13.118 1.00 72.62 ? 20 ARG A O 1 ATOM 153 C CB . ARG A 1 20 ? 27.060 -5.479 -13.928 1.00 84.77 ? 20 ARG A CB 1 ATOM 154 C CG . ARG A 1 20 ? 27.721 -4.364 -14.731 1.00 92.72 ? 20 ARG A CG 1 ATOM 155 C CD . ARG A 1 20 ? 26.869 -3.097 -14.736 1.00 98.43 ? 20 ARG A CD 1 ATOM 156 N NE . ARG A 1 20 ? 27.012 -2.338 -15.980 1.00 106.88 ? 20 ARG A NE 1 ATOM 157 C CZ . ARG A 1 20 ? 26.418 -2.643 -17.140 1.00 112.96 ? 20 ARG A CZ 1 ATOM 158 N NH1 . ARG A 1 20 ? 25.624 -3.705 -17.253 1.00 109.82 ? 20 ARG A NH1 1 ATOM 159 N NH2 . ARG A 1 20 ? 26.620 -1.879 -18.206 1.00 114.34 ? 20 ARG A NH2 1 ATOM 160 N N . GLN A 1 21 ? 27.247 -7.360 -11.355 1.00 72.20 ? 21 GLN A N 1 ATOM 161 C CA . GLN A 1 21 ? 26.523 -8.138 -10.386 1.00 68.74 ? 21 GLN A CA 1 ATOM 162 C C . GLN A 1 21 ? 26.082 -7.242 -9.250 1.00 70.19 ? 21 GLN A C 1 ATOM 163 O O . GLN A 1 21 ? 26.811 -6.343 -8.811 1.00 71.33 ? 21 GLN A O 1 ATOM 164 C CB . GLN A 1 21 ? 27.378 -9.278 -9.851 1.00 68.43 ? 21 GLN A CB 1 ATOM 165 C CG . GLN A 1 21 ? 28.782 -8.895 -9.434 1.00 68.42 ? 21 GLN A CG 1 ATOM 166 C CD . GLN A 1 21 ? 29.524 -10.054 -8.795 1.00 69.82 ? 21 GLN A CD 1 ATOM 167 O OE1 . GLN A 1 21 ? 29.017 -11.165 -8.729 1.00 71.16 ? 21 GLN A OE1 1 ATOM 168 N NE2 . GLN A 1 21 ? 30.735 -9.797 -8.320 1.00 73.17 ? 21 GLN A NE2 1 ATOM 169 N N . TYR A 1 22 ? 24.882 -7.507 -8.762 1.00 72.33 ? 22 TYR A N 1 ATOM 170 C CA . TYR A 1 22 ? 24.256 -6.692 -7.734 1.00 73.40 ? 22 TYR A CA 1 ATOM 171 C C . TYR A 1 22 ? 23.888 -7.569 -6.554 1.00 70.50 ? 22 TYR A C 1 ATOM 172 O O . TYR A 1 22 ? 23.564 -8.740 -6.733 1.00 69.72 ? 22 TYR A O 1 ATOM 173 C CB . TYR A 1 22 ? 23.003 -6.032 -8.314 1.00 73.28 ? 22 TYR A CB 1 ATOM 174 C CG . TYR A 1 22 ? 23.288 -5.095 -9.480 1.00 74.05 ? 22 TYR A CG 1 ATOM 175 C CD1 . TYR A 1 22 ? 23.539 -5.593 -10.765 1.00 72.58 ? 22 TYR A CD1 1 ATOM 176 C CD2 . TYR A 1 22 ? 23.299 -3.708 -9.299 1.00 75.09 ? 22 TYR A CD2 1 ATOM 177 C CE1 . TYR A 1 22 ? 23.798 -4.748 -11.826 1.00 73.13 ? 22 TYR A CE1 1 ATOM 178 C CE2 . TYR A 1 22 ? 23.551 -2.858 -10.356 1.00 77.55 ? 22 TYR A CE2 1 ATOM 179 C CZ . TYR A 1 22 ? 23.802 -3.384 -11.615 1.00 75.98 ? 22 TYR A CZ 1 ATOM 180 O OH . TYR A 1 22 ? 24.061 -2.538 -12.656 1.00 78.59 ? 22 TYR A OH 1 ATOM 181 N N . SER A 1 23 ? 23.918 -6.996 -5.353 1.00 70.17 ? 23 SER A N 1 ATOM 182 C CA . SER A 1 23 ? 23.435 -7.695 -4.156 1.00 68.24 ? 23 SER A CA 1 ATOM 183 C C . SER A 1 23 ? 22.694 -6.757 -3.227 1.00 66.57 ? 23 SER A C 1 ATOM 184 O O . SER A 1 23 ? 23.257 -5.759 -2.799 1.00 68.09 ? 23 SER A O 1 ATOM 185 C CB . SER A 1 23 ? 24.593 -8.326 -3.404 1.00 67.32 ? 23 SER A CB 1 ATOM 186 O OG . SER A 1 23 ? 24.168 -8.756 -2.130 1.00 65.84 ? 23 SER A OG 1 ATOM 187 N N . GLY A 1 24 ? 21.447 -7.100 -2.902 1.00 65.98 ? 24 GLY A N 1 ATOM 188 C CA . GLY A 1 24 ? 20.596 -6.269 -2.033 1.00 65.30 ? 24 GLY A CA 1 ATOM 189 C C . GLY A 1 24 ? 19.308 -6.970 -1.632 1.00 63.55 ? 24 GLY A C 1 ATOM 190 O O . GLY A 1 24 ? 19.283 -8.182 -1.528 1.00 62.46 ? 24 GLY A O 1 ATOM 191 N N . TYR A 1 25 ? 18.227 -6.207 -1.463 1.00 63.85 ? 25 TYR A N 1 ATOM 192 C CA . TYR A 1 25 ? 16.985 -6.716 -0.872 1.00 60.81 ? 25 TYR A CA 1 ATOM 193 C C . TYR A 1 25 ? 15.725 -6.452 -1.687 1.00 60.78 ? 25 TYR A C 1 ATOM 194 O O . TYR A 1 25 ? 15.474 -5.340 -2.140 1.00 60.17 ? 25 TYR A O 1 ATOM 195 C CB . TYR A 1 25 ? 16.822 -6.155 0.545 1.00 61.15 ? 25 TYR A CB 1 ATOM 196 C CG . TYR A 1 25 ? 17.735 -6.855 1.496 1.00 61.91 ? 25 TYR A CG 1 ATOM 197 C CD1 . TYR A 1 25 ? 19.062 -6.488 1.611 1.00 62.03 ? 25 TYR A CD1 1 ATOM 198 C CD2 . TYR A 1 25 ? 17.292 -7.949 2.230 1.00 65.12 ? 25 TYR A CD2 1 ATOM 199 C CE1 . TYR A 1 25 ? 19.925 -7.172 2.462 1.00 63.74 ? 25 TYR A CE1 1 ATOM 200 C CE2 . TYR A 1 25 ? 18.143 -8.638 3.087 1.00 64.78 ? 25 TYR A CE2 1 ATOM 201 C CZ . TYR A 1 25 ? 19.459 -8.246 3.197 1.00 62.62 ? 25 TYR A CZ 1 ATOM 202 O OH . TYR A 1 25 ? 20.294 -8.919 4.039 1.00 62.94 ? 25 TYR A OH 1 ATOM 203 N N . LEU A 1 26 ? 14.922 -7.495 -1.845 1.00 63.42 ? 26 LEU A N 1 ATOM 204 C CA . LEU A 1 26 ? 13.637 -7.407 -2.512 1.00 64.53 ? 26 LEU A CA 1 ATOM 205 C C . LEU A 1 26 ? 12.527 -7.466 -1.486 1.00 66.25 ? 26 LEU A C 1 ATOM 206 O O . LEU A 1 26 ? 12.602 -8.225 -0.531 1.00 65.93 ? 26 LEU A O 1 ATOM 207 C CB . LEU A 1 26 ? 13.469 -8.564 -3.480 1.00 66.72 ? 26 LEU A CB 1 ATOM 208 C CG . LEU A 1 26 ? 14.617 -8.812 -4.462 1.00 67.95 ? 26 LEU A CG 1 ATOM 209 C CD1 . LEU A 1 26 ? 14.261 -9.985 -5.353 1.00 66.55 ? 26 LEU A CD1 1 ATOM 210 C CD2 . LEU A 1 26 ? 14.911 -7.580 -5.289 1.00 68.36 ? 26 LEU A CD2 1 ATOM 211 N N . LYS A 1 27 ? 11.505 -6.651 -1.680 1.00 71.42 ? 27 LYS A N 1 ATOM 212 C CA . LYS A 1 27 ? 10.365 -6.634 -0.776 1.00 78.61 ? 27 LYS A CA 1 ATOM 213 C C . LYS A 1 27 ? 9.494 -7.838 -1.044 1.00 79.20 ? 27 LYS A C 1 ATOM 214 O O . LYS A 1 27 ? 9.134 -8.087 -2.182 1.00 93.00 ? 27 LYS A O 1 ATOM 215 C CB . LYS A 1 27 ? 9.539 -5.350 -0.950 1.00 78.40 ? 27 LYS A CB 1 ATOM 216 C CG . LYS A 1 27 ? 10.187 -4.116 -0.355 1.00 80.39 ? 27 LYS A CG 1 ATOM 217 C CD . LYS A 1 27 ? 9.154 -3.095 0.111 1.00 83.47 ? 27 LYS A CD 1 ATOM 218 C CE . LYS A 1 27 ? 8.513 -2.348 -1.051 1.00 84.26 ? 27 LYS A CE 1 ATOM 219 N NZ . LYS A 1 27 ? 9.472 -1.458 -1.767 1.00 81.95 ? 27 LYS A NZ 1 ATOM 220 N N . GLY A 1 28 ? 9.147 -8.575 -0.003 1.00 77.87 ? 28 GLY A N 1 ATOM 221 C CA . GLY A 1 28 ? 8.167 -9.636 -0.136 1.00 79.82 ? 28 GLY A CA 1 ATOM 222 C C . GLY A 1 28 ? 6.831 -9.183 0.446 1.00 80.99 ? 28 GLY A C 1 ATOM 223 O O . GLY A 1 28 ? 6.488 -8.005 0.369 1.00 92.21 ? 28 GLY A O 1 ATOM 224 N N . SER A 1 29 ? 6.060 -10.114 1.000 1.00 74.11 ? 29 SER A N 1 ATOM 225 C CA . SER A 1 29 ? 4.836 -9.753 1.678 1.00 75.83 ? 29 SER A CA 1 ATOM 226 C C . SER A 1 29 ? 5.192 -9.108 3.017 1.00 77.51 ? 29 SER A C 1 ATOM 227 O O . SER A 1 29 ? 6.329 -9.192 3.472 1.00 74.58 ? 29 SER A O 1 ATOM 228 C CB . SER A 1 29 ? 3.924 -10.972 1.877 1.00 74.82 ? 29 SER A CB 1 ATOM 229 O OG . SER A 1 29 ? 4.060 -11.535 3.166 1.00 75.64 ? 29 SER A OG 1 ATOM 230 N N . GLY A 1 30 ? 4.212 -8.454 3.629 1.00 82.42 ? 30 GLY A N 1 ATOM 231 C CA . GLY A 1 30 ? 4.370 -7.869 4.956 1.00 83.16 ? 30 GLY A CA 1 ATOM 232 C C . GLY A 1 30 ? 5.667 -7.110 5.073 1.00 79.28 ? 30 GLY A C 1 ATOM 233 O O . GLY A 1 30 ? 6.018 -6.354 4.176 1.00 78.52 ? 30 GLY A O 1 ATOM 234 N N . SER A 1 31 ? 6.387 -7.342 6.164 1.00 77.66 ? 31 SER A N 1 ATOM 235 C CA . SER A 1 31 ? 7.640 -6.646 6.419 1.00 75.99 ? 31 SER A CA 1 ATOM 236 C C . SER A 1 31 ? 8.846 -7.541 6.158 1.00 74.71 ? 31 SER A C 1 ATOM 237 O O . SER A 1 31 ? 9.870 -7.419 6.833 1.00 78.48 ? 31 SER A O 1 ATOM 238 C CB . SER A 1 31 ? 7.660 -6.113 7.857 1.00 74.21 ? 31 SER A CB 1 ATOM 239 O OG . SER A 1 31 ? 7.701 -7.163 8.809 1.00 73.25 ? 31 SER A OG 1 ATOM 240 N N . LYS A 1 32 ? 8.728 -8.429 5.175 1.00 70.54 ? 32 LYS A N 1 ATOM 241 C CA . LYS A 1 32 ? 9.808 -9.359 4.842 1.00 69.90 ? 32 LYS A CA 1 ATOM 242 C C . LYS A 1 32 ? 10.759 -8.815 3.741 1.00 71.16 ? 32 LYS A C 1 ATOM 243 O O . LYS A 1 32 ? 10.319 -8.212 2.771 1.00 80.56 ? 32 LYS A O 1 ATOM 244 C CB . LYS A 1 32 ? 9.228 -10.697 4.411 1.00 66.87 ? 32 LYS A CB 1 ATOM 245 C CG . LYS A 1 32 ? 8.198 -11.304 5.348 1.00 66.28 ? 32 LYS A CG 1 ATOM 246 C CD . LYS A 1 32 ? 7.504 -12.477 4.673 1.00 67.05 ? 32 LYS A CD 1 ATOM 247 C CE . LYS A 1 32 ? 6.428 -13.117 5.530 1.00 69.65 ? 32 LYS A CE 1 ATOM 248 N NZ . LYS A 1 32 ? 5.201 -12.277 5.617 1.00 73.81 ? 32 LYS A NZ 1 ATOM 249 N N . HIS A 1 33 ? 12.056 -9.045 3.898 1.00 68.39 ? 33 HIS A N 1 ATOM 250 C CA . HIS A 1 33 ? 13.060 -8.525 2.978 1.00 65.62 ? 33 HIS A CA 1 ATOM 251 C C . HIS A 1 33 ? 14.049 -9.607 2.598 1.00 65.10 ? 33 HIS A C 1 ATOM 252 O O . HIS A 1 33 ? 14.835 -10.054 3.421 1.00 62.68 ? 33 HIS A O 1 ATOM 253 C CB . HIS A 1 33 ? 13.813 -7.377 3.630 1.00 69.19 ? 33 HIS A CB 1 ATOM 254 C CG . HIS A 1 33 ? 12.993 -6.142 3.803 1.00 72.43 ? 33 HIS A CG 1 ATOM 255 N ND1 . HIS A 1 33 ? 12.413 -5.799 5.003 1.00 77.98 ? 33 HIS A ND1 1 ATOM 256 C CD2 . HIS A 1 33 ? 12.656 -5.171 2.925 1.00 73.12 ? 33 HIS A CD2 1 ATOM 257 C CE1 . HIS A 1 33 ? 11.751 -4.667 4.857 1.00 77.59 ? 33 HIS A CE1 1 ATOM 258 N NE2 . HIS A 1 33 ? 11.882 -4.267 3.605 1.00 74.89 ? 33 HIS A NE2 1 ATOM 259 N N . LEU A 1 34 ? 14.004 -10.026 1.340 1.00 68.62 ? 34 LEU A N 1 ATOM 260 C CA . LEU A 1 34 ? 14.775 -11.168 0.866 1.00 68.50 ? 34 LEU A CA 1 ATOM 261 C C . LEU A 1 34 ? 16.066 -10.715 0.216 1.00 69.08 ? 34 LEU A C 1 ATOM 262 O O . LEU A 1 34 ? 16.049 -9.890 -0.687 1.00 71.78 ? 34 LEU A O 1 ATOM 263 C CB . LEU A 1 34 ? 13.965 -11.972 -0.155 1.00 69.45 ? 34 LEU A CB 1 ATOM 264 C CG . LEU A 1 34 ? 12.546 -12.373 0.209 1.00 69.48 ? 34 LEU A CG 1 ATOM 265 C CD1 . LEU A 1 34 ? 11.978 -13.265 -0.867 1.00 68.41 ? 34 LEU A CD1 1 ATOM 266 C CD2 . LEU A 1 34 ? 12.495 -13.082 1.548 1.00 73.28 ? 34 LEU A CD2 1 ATOM 267 N N . HIS A 1 35 ? 17.179 -11.284 0.649 1.00 67.52 ? 35 HIS A N 1 ATOM 268 C CA . HIS A 1 35 ? 18.461 -10.956 0.058 1.00 65.87 ? 35 HIS A CA 1 ATOM 269 C C . HIS A 1 35 ? 18.611 -11.627 -1.286 1.00 64.13 ? 35 HIS A C 1 ATOM 270 O O . HIS A 1 35 ? 18.329 -12.807 -1.418 1.00 67.64 ? 35 HIS A O 1 ATOM 271 C CB . HIS A 1 35 ? 19.606 -11.389 0.967 1.00 65.39 ? 35 HIS A CB 1 ATOM 272 C CG . HIS A 1 35 ? 20.956 -11.160 0.367 1.00 63.62 ? 35 HIS A CG 1 ATOM 273 N ND1 . HIS A 1 35 ? 21.968 -12.083 0.441 1.00 61.22 ? 35 HIS A ND1 1 ATOM 274 C CD2 . HIS A 1 35 ? 21.451 -10.117 -0.334 1.00 61.31 ? 35 HIS A CD2 1 ATOM 275 C CE1 . HIS A 1 35 ? 23.035 -11.609 -0.173 1.00 60.54 ? 35 HIS A CE1 1 ATOM 276 N NE2 . HIS A 1 35 ? 22.741 -10.425 -0.665 1.00 60.26 ? 35 HIS A NE2 1 ATOM 277 N N . TYR A 1 36 ? 19.055 -10.870 -2.279 1.00 63.09 ? 36 TYR A N 1 ATOM 278 C CA . TYR A 1 36 ? 19.288 -11.401 -3.614 1.00 61.44 ? 36 TYR A CA 1 ATOM 279 C C . TYR A 1 36 ? 20.727 -11.162 -4.028 1.00 61.74 ? 36 TYR A C 1 ATOM 280 O O . TYR A 1 36 ? 21.392 -10.269 -3.514 1.00 63.62 ? 36 TYR A O 1 ATOM 281 C CB . TYR A 1 36 ? 18.346 -10.743 -4.625 1.00 62.89 ? 36 TYR A CB 1 ATOM 282 C CG . TYR A 1 36 ? 18.736 -9.324 -5.026 1.00 63.37 ? 36 TYR A CG 1 ATOM 283 C CD1 . TYR A 1 36 ? 18.214 -8.223 -4.364 1.00 64.71 ? 36 TYR A CD1 1 ATOM 284 C CD2 . TYR A 1 36 ? 19.601 -9.096 -6.076 1.00 63.57 ? 36 TYR A CD2 1 ATOM 285 C CE1 . TYR A 1 36 ? 18.559 -6.939 -4.719 1.00 63.78 ? 36 TYR A CE1 1 ATOM 286 C CE2 . TYR A 1 36 ? 19.949 -7.819 -6.451 1.00 65.57 ? 36 TYR A CE2 1 ATOM 287 C CZ . TYR A 1 36 ? 19.433 -6.742 -5.761 1.00 67.83 ? 36 TYR A CZ 1 ATOM 288 O OH . TYR A 1 36 ? 19.795 -5.460 -6.143 1.00 71.37 ? 36 TYR A OH 1 ATOM 289 N N . TRP A 1 37 ? 21.188 -11.977 -4.966 1.00 61.08 ? 37 TRP A N 1 ATOM 290 C CA . TRP A 1 37 ? 22.493 -11.831 -5.597 1.00 60.25 ? 37 TRP A CA 1 ATOM 291 C C . TRP A 1 37 ? 22.316 -12.132 -7.088 1.00 63.12 ? 37 TRP A C 1 ATOM 292 O O . TRP A 1 37 ? 22.027 -13.262 -7.481 1.00 64.53 ? 37 TRP A O 1 ATOM 293 C CB . TRP A 1 37 ? 23.469 -12.797 -4.966 1.00 58.25 ? 37 TRP A CB 1 ATOM 294 C CG . TRP A 1 37 ? 24.873 -12.613 -5.361 1.00 58.14 ? 37 TRP A CG 1 ATOM 295 C CD1 . TRP A 1 37 ? 25.346 -12.027 -6.503 1.00 60.99 ? 37 TRP A CD1 1 ATOM 296 C CD2 . TRP A 1 37 ? 26.023 -13.053 -4.629 1.00 56.58 ? 37 TRP A CD2 1 ATOM 297 N NE1 . TRP A 1 37 ? 26.723 -12.069 -6.521 1.00 61.20 ? 37 TRP A NE1 1 ATOM 298 C CE2 . TRP A 1 37 ? 27.160 -12.696 -5.384 1.00 58.68 ? 37 TRP A CE2 1 ATOM 299 C CE3 . TRP A 1 37 ? 26.201 -13.719 -3.419 1.00 55.91 ? 37 TRP A CE3 1 ATOM 300 C CZ2 . TRP A 1 37 ? 28.453 -12.968 -4.955 1.00 58.16 ? 37 TRP A CZ2 1 ATOM 301 C CZ3 . TRP A 1 37 ? 27.490 -13.994 -2.997 1.00 57.04 ? 37 TRP A CZ3 1 ATOM 302 C CH2 . TRP A 1 37 ? 28.598 -13.619 -3.766 1.00 57.47 ? 37 TRP A CH2 1 ATOM 303 N N . PHE A 1 38 ? 22.463 -11.098 -7.906 1.00 65.19 ? 38 PHE A N 1 ATOM 304 C CA . PHE A 1 38 ? 22.132 -11.148 -9.325 1.00 64.13 ? 38 PHE A CA 1 ATOM 305 C C . PHE A 1 38 ? 23.415 -11.087 -10.115 1.00 65.38 ? 38 PHE A C 1 ATOM 306 O O . PHE A 1 38 ? 24.162 -10.130 -9.976 1.00 64.42 ? 38 PHE A O 1 ATOM 307 C CB . PHE A 1 38 ? 21.277 -9.939 -9.640 1.00 65.71 ? 38 PHE A CB 1 ATOM 308 C CG . PHE A 1 38 ? 20.746 -9.902 -11.038 1.00 65.33 ? 38 PHE A CG 1 ATOM 309 C CD1 . PHE A 1 38 ? 19.819 -10.834 -11.468 1.00 65.85 ? 38 PHE A CD1 1 ATOM 310 C CD2 . PHE A 1 38 ? 21.129 -8.902 -11.906 1.00 65.51 ? 38 PHE A CD2 1 ATOM 311 C CE1 . PHE A 1 38 ? 19.314 -10.790 -12.757 1.00 65.37 ? 38 PHE A CE1 1 ATOM 312 C CE2 . PHE A 1 38 ? 20.635 -8.858 -13.190 1.00 65.37 ? 38 PHE A CE2 1 ATOM 313 C CZ . PHE A 1 38 ? 19.730 -9.802 -13.616 1.00 65.71 ? 38 PHE A CZ 1 ATOM 314 N N . VAL A 1 39 ? 23.697 -12.118 -10.908 1.00 67.68 ? 39 VAL A N 1 ATOM 315 C CA . VAL A 1 39 ? 24.897 -12.120 -11.758 1.00 72.41 ? 39 VAL A CA 1 ATOM 316 C C . VAL A 1 39 ? 24.550 -12.029 -13.254 1.00 75.18 ? 39 VAL A C 1 ATOM 317 O O . VAL A 1 39 ? 23.925 -12.936 -13.817 1.00 72.82 ? 39 VAL A O 1 ATOM 318 C CB . VAL A 1 39 ? 25.808 -13.328 -11.490 1.00 71.82 ? 39 VAL A CB 1 ATOM 319 C CG1 . VAL A 1 39 ? 26.601 -13.112 -10.215 1.00 71.88 ? 39 VAL A CG1 1 ATOM 320 C CG2 . VAL A 1 39 ? 25.018 -14.619 -11.427 1.00 70.20 ? 39 VAL A CG2 1 ATOM 321 N N . GLU A 1 40 ? 24.940 -10.921 -13.879 1.00 76.38 ? 40 GLU A N 1 ATOM 322 C CA . GLU A 1 40 ? 24.586 -10.672 -15.271 1.00 81.76 ? 40 GLU A CA 1 ATOM 323 C C . GLU A 1 40 ? 25.206 -11.707 -16.183 1.00 76.77 ? 40 GLU A C 1 ATOM 324 O O . GLU A 1 40 ? 26.287 -12.201 -15.909 1.00 79.12 ? 40 GLU A O 1 ATOM 325 C CB . GLU A 1 40 ? 25.004 -9.264 -15.706 1.00 89.15 ? 40 GLU A CB 1 ATOM 326 C CG . GLU A 1 40 ? 24.213 -8.138 -15.041 1.00 93.85 ? 40 GLU A CG 1 ATOM 327 C CD . GLU A 1 40 ? 24.295 -6.813 -15.788 1.00 97.39 ? 40 GLU A CD 1 ATOM 328 O OE1 . GLU A 1 40 ? 25.235 -6.624 -16.597 1.00 97.21 ? 40 GLU A OE1 1 ATOM 329 O OE2 . GLU A 1 40 ? 23.412 -5.957 -15.561 1.00 96.86 ? 40 GLU A OE2 1 ATOM 330 N N . SER A 1 41 ? 24.516 -12.051 -17.262 1.00 76.96 ? 41 SER A N 1 ATOM 331 C CA . SER A 1 41 ? 25.069 -12.979 -18.244 1.00 78.35 ? 41 SER A CA 1 ATOM 332 C C . SER A 1 41 ? 26.433 -12.502 -18.680 1.00 79.27 ? 41 SER A C 1 ATOM 333 O O . SER A 1 41 ? 26.607 -11.320 -18.980 1.00 81.47 ? 41 SER A O 1 ATOM 334 C CB . SER A 1 41 ? 24.179 -13.095 -19.479 1.00 77.32 ? 41 SER A CB 1 ATOM 335 O OG . SER A 1 41 ? 24.872 -13.727 -20.541 1.00 75.21 ? 41 SER A OG 1 ATOM 336 N N . GLN A 1 42 ? 27.393 -13.420 -18.728 1.00 76.37 ? 42 GLN A N 1 ATOM 337 C CA . GLN A 1 42 ? 28.727 -13.081 -19.211 1.00 78.80 ? 42 GLN A CA 1 ATOM 338 C C . GLN A 1 42 ? 28.720 -12.752 -20.708 1.00 80.83 ? 42 GLN A C 1 ATOM 339 O O . GLN A 1 42 ? 29.675 -12.184 -21.223 1.00 75.40 ? 42 GLN A O 1 ATOM 340 C CB . GLN A 1 42 ? 29.696 -14.224 -18.962 1.00 75.45 ? 42 GLN A CB 1 ATOM 341 C CG . GLN A 1 42 ? 29.872 -14.601 -17.505 1.00 74.93 ? 42 GLN A CG 1 ATOM 342 C CD . GLN A 1 42 ? 31.137 -15.411 -17.280 1.00 76.18 ? 42 GLN A CD 1 ATOM 343 O OE1 . GLN A 1 42 ? 32.207 -15.077 -17.800 1.00 73.92 ? 42 GLN A OE1 1 ATOM 344 N NE2 . GLN A 1 42 ? 31.025 -16.480 -16.503 1.00 77.03 ? 42 GLN A NE2 1 ATOM 345 N N . LYS A 1 43 ? 27.637 -13.118 -21.387 1.00 82.53 ? 43 LYS A N 1 ATOM 346 C CA . LYS A 1 43 ? 27.508 -12.948 -22.816 1.00 89.04 ? 43 LYS A CA 1 ATOM 347 C C . LYS A 1 43 ? 26.167 -12.282 -23.119 1.00 89.90 ? 43 LYS A C 1 ATOM 348 O O . LYS A 1 43 ? 25.124 -12.941 -23.165 1.00 94.60 ? 43 LYS A O 1 ATOM 349 C CB . LYS A 1 43 ? 27.644 -14.321 -23.493 1.00 92.65 ? 43 LYS A CB 1 ATOM 350 C CG . LYS A 1 43 ? 27.176 -14.430 -24.941 1.00 97.95 ? 43 LYS A CG 1 ATOM 351 C CD . LYS A 1 43 ? 27.963 -13.531 -25.879 1.00 101.91 ? 43 LYS A CD 1 ATOM 352 C CE . LYS A 1 43 ? 27.617 -13.849 -27.321 1.00 105.47 ? 43 LYS A CE 1 ATOM 353 N NZ . LYS A 1 43 ? 28.280 -12.932 -28.275 1.00 109.61 ? 43 LYS A NZ 1 ATOM 354 N N . ASP A 1 44 ? 26.209 -10.971 -23.302 1.00 87.95 ? 44 ASP A N 1 ATOM 355 C CA . ASP A 1 44 ? 25.050 -10.187 -23.729 1.00 92.16 ? 44 ASP A CA 1 ATOM 356 C C . ASP A 1 44 ? 23.858 -10.264 -22.780 1.00 92.21 ? 44 ASP A C 1 ATOM 357 O O . ASP A 1 44 ? 22.872 -10.941 -23.068 1.00 87.47 ? 44 ASP A O 1 ATOM 358 C CB . ASP A 1 44 ? 24.618 -10.573 -25.144 1.00 93.49 ? 44 ASP A CB 1 ATOM 359 C CG . ASP A 1 44 ? 23.704 -9.545 -25.771 1.00 96.49 ? 44 ASP A CG 1 ATOM 360 O OD1 . ASP A 1 44 ? 23.654 -8.398 -25.264 1.00 101.05 ? 44 ASP A OD1 1 ATOM 361 O OD2 . ASP A 1 44 ? 23.049 -9.879 -26.780 1.00 96.25 ? 44 ASP A OD2 1 ATOM 362 N N . PRO A 1 45 ? 23.960 -9.561 -21.643 1.00 95.49 ? 45 PRO A N 1 ATOM 363 C CA . PRO A 1 45 ? 22.884 -9.441 -20.668 1.00 93.90 ? 45 PRO A CA 1 ATOM 364 C C . PRO A 1 45 ? 21.543 -9.066 -21.292 1.00 93.36 ? 45 PRO A C 1 ATOM 365 O O . PRO A 1 45 ? 20.543 -9.690 -20.999 1.00 95.04 ? 45 PRO A O 1 ATOM 366 C CB . PRO A 1 45 ? 23.380 -8.326 -19.747 1.00 94.83 ? 45 PRO A CB 1 ATOM 367 C CG . PRO A 1 45 ? 24.859 -8.459 -19.784 1.00 95.73 ? 45 PRO A CG 1 ATOM 368 C CD . PRO A 1 45 ? 25.194 -8.898 -21.180 1.00 94.11 ? 45 PRO A CD 1 ATOM 369 N N . GLU A 1 46 ? 21.542 -8.078 -22.172 1.00 94.71 ? 46 GLU A N 1 ATOM 370 C CA . GLU A 1 46 ? 20.314 -7.568 -22.779 1.00 92.19 ? 46 GLU A CA 1 ATOM 371 C C . GLU A 1 46 ? 19.518 -8.598 -23.609 1.00 90.54 ? 46 GLU A C 1 ATOM 372 O O . GLU A 1 46 ? 18.339 -8.395 -23.871 1.00 90.39 ? 46 GLU A O 1 ATOM 373 C CB . GLU A 1 46 ? 20.659 -6.377 -23.665 1.00 97.53 ? 46 GLU A CB 1 ATOM 374 C CG . GLU A 1 46 ? 19.505 -5.434 -23.910 1.00 102.00 ? 46 GLU A CG 1 ATOM 375 C CD . GLU A 1 46 ? 19.722 -4.549 -25.113 1.00 102.97 ? 46 GLU A CD 1 ATOM 376 O OE1 . GLU A 1 46 ? 20.160 -5.069 -26.164 1.00 103.35 ? 46 GLU A OE1 1 ATOM 377 O OE2 . GLU A 1 46 ? 19.434 -3.342 -25.002 1.00 103.04 ? 46 GLU A OE2 1 ATOM 378 N N . ASN A 1 47 ? 20.165 -9.681 -24.038 1.00 88.45 ? 47 ASN A N 1 ATOM 379 C CA . ASN A 1 47 ? 19.494 -10.754 -24.775 1.00 87.99 ? 47 ASN A CA 1 ATOM 380 C C . ASN A 1 47 ? 19.672 -12.131 -24.153 1.00 88.00 ? 47 ASN A C 1 ATOM 381 O O . ASN A 1 47 ? 19.221 -13.125 -24.728 1.00 90.64 ? 47 ASN A O 1 ATOM 382 C CB . ASN A 1 47 ? 19.971 -10.821 -26.225 1.00 90.48 ? 47 ASN A CB 1 ATOM 383 C CG . ASN A 1 47 ? 19.580 -9.609 -27.031 1.00 92.54 ? 47 ASN A CG 1 ATOM 384 O OD1 . ASN A 1 47 ? 18.397 -9.305 -27.192 1.00 93.44 ? 47 ASN A OD1 1 ATOM 385 N ND2 . ASN A 1 47 ? 20.572 -8.911 -27.550 1.00 93.57 ? 47 ASN A ND2 1 ATOM 386 N N . SER A 1 48 ? 20.324 -12.214 -22.999 1.00 85.43 ? 48 SER A N 1 ATOM 387 C CA . SER A 1 48 ? 20.346 -13.463 -22.250 1.00 81.68 ? 48 SER A CA 1 ATOM 388 C C . SER A 1 48 ? 19.113 -13.516 -21.328 1.00 79.08 ? 48 SER A C 1 ATOM 389 O O . SER A 1 48 ? 18.683 -12.485 -20.806 1.00 79.86 ? 48 SER A O 1 ATOM 390 C CB . SER A 1 48 ? 21.640 -13.599 -21.458 1.00 82.46 ? 48 SER A CB 1 ATOM 391 O OG . SER A 1 48 ? 22.719 -13.980 -22.292 1.00 83.63 ? 48 SER A OG 1 ATOM 392 N N . PRO A 1 49 ? 18.535 -14.713 -21.119 1.00 75.15 ? 49 PRO A N 1 ATOM 393 C CA . PRO A 1 49 ? 17.368 -14.822 -20.239 1.00 74.90 ? 49 PRO A CA 1 ATOM 394 C C . PRO A 1 49 ? 17.607 -14.493 -18.763 1.00 71.09 ? 49 PRO A C 1 ATOM 395 O O . PRO A 1 49 ? 18.736 -14.253 -18.332 1.00 67.63 ? 49 PRO A O 1 ATOM 396 C CB . PRO A 1 49 ? 16.969 -16.294 -20.353 1.00 74.47 ? 49 PRO A CB 1 ATOM 397 C CG . PRO A 1 49 ? 17.644 -16.789 -21.582 1.00 75.25 ? 49 PRO A CG 1 ATOM 398 C CD . PRO A 1 49 ? 18.914 -16.018 -21.673 1.00 74.62 ? 49 PRO A CD 1 ATOM 399 N N . VAL A 1 50 ? 16.513 -14.465 -18.021 1.00 69.79 ? 50 VAL A N 1 ATOM 400 C CA . VAL A 1 50 ? 16.521 -14.204 -16.598 1.00 68.42 ? 50 VAL A CA 1 ATOM 401 C C . VAL A 1 50 ? 16.137 -15.489 -15.880 1.00 65.87 ? 50 VAL A C 1 ATOM 402 O O . VAL A 1 50 ? 15.028 -15.987 -16.040 1.00 68.52 ? 50 VAL A O 1 ATOM 403 C CB . VAL A 1 50 ? 15.546 -13.082 -16.226 1.00 69.74 ? 50 VAL A CB 1 ATOM 404 C CG1 . VAL A 1 50 ? 15.396 -12.960 -14.711 1.00 68.65 ? 50 VAL A CG1 1 ATOM 405 C CG2 . VAL A 1 50 ? 16.032 -11.766 -16.789 1.00 70.46 ? 50 VAL A CG2 1 ATOM 406 N N . VAL A 1 51 ? 17.068 -16.008 -15.092 1.00 60.34 ? 51 VAL A N 1 ATOM 407 C CA . VAL A 1 51 ? 16.887 -17.243 -14.362 1.00 60.17 ? 51 VAL A CA 1 ATOM 408 C C . VAL A 1 51 ? 16.812 -16.977 -12.854 1.00 59.53 ? 51 VAL A C 1 ATOM 409 O O . VAL A 1 51 ? 17.708 -16.366 -12.273 1.00 59.36 ? 51 VAL A O 1 ATOM 410 C CB . VAL A 1 51 ? 18.057 -18.192 -14.653 1.00 59.83 ? 51 VAL A CB 1 ATOM 411 C CG1 . VAL A 1 51 ? 18.080 -19.359 -13.672 1.00 58.02 ? 51 VAL A CG1 1 ATOM 412 C CG2 . VAL A 1 51 ? 17.980 -18.683 -16.089 1.00 60.21 ? 51 VAL A CG2 1 ATOM 413 N N . LEU A 1 52 ? 15.743 -17.438 -12.226 1.00 58.64 ? 52 LEU A N 1 ATOM 414 C CA . LEU A 1 52 ? 15.640 -17.432 -10.759 1.00 59.68 ? 52 LEU A CA 1 ATOM 415 C C . LEU A 1 52 ? 16.124 -18.790 -10.271 1.00 58.31 ? 52 LEU A C 1 ATOM 416 O O . LEU A 1 52 ? 15.679 -19.823 -10.783 1.00 57.38 ? 52 LEU A O 1 ATOM 417 C CB . LEU A 1 52 ? 14.188 -17.231 -10.323 1.00 59.06 ? 52 LEU A CB 1 ATOM 418 C CG . LEU A 1 52 ? 13.901 -17.357 -8.829 1.00 60.66 ? 52 LEU A CG 1 ATOM 419 C CD1 . LEU A 1 52 ? 14.434 -16.149 -8.065 1.00 62.80 ? 52 LEU A CD1 1 ATOM 420 C CD2 . LEU A 1 52 ? 12.414 -17.515 -8.577 1.00 61.12 ? 52 LEU A CD2 1 ATOM 421 N N . TRP A 1 53 ? 17.037 -18.805 -9.310 1.00 54.93 ? 53 TRP A N 1 ATOM 422 C CA . TRP A 1 53 ? 17.471 -20.068 -8.724 1.00 54.57 ? 53 TRP A CA 1 ATOM 423 C C . TRP A 1 53 ? 17.106 -20.099 -7.253 1.00 55.92 ? 53 TRP A C 1 ATOM 424 O O . TRP A 1 53 ? 17.473 -19.184 -6.525 1.00 62.42 ? 53 TRP A O 1 ATOM 425 C CB . TRP A 1 53 ? 18.969 -20.247 -8.852 1.00 55.05 ? 53 TRP A CB 1 ATOM 426 C CG . TRP A 1 53 ? 19.429 -21.452 -8.108 1.00 52.60 ? 53 TRP A CG 1 ATOM 427 C CD1 . TRP A 1 53 ? 19.967 -21.481 -6.859 1.00 52.12 ? 53 TRP A CD1 1 ATOM 428 C CD2 . TRP A 1 53 ? 19.344 -22.800 -8.546 1.00 51.11 ? 53 TRP A CD2 1 ATOM 429 N NE1 . TRP A 1 53 ? 20.227 -22.771 -6.489 1.00 51.14 ? 53 TRP A NE1 1 ATOM 430 C CE2 . TRP A 1 53 ? 19.866 -23.605 -7.511 1.00 51.94 ? 53 TRP A CE2 1 ATOM 431 C CE3 . TRP A 1 53 ? 18.876 -23.413 -9.716 1.00 50.74 ? 53 TRP A CE3 1 ATOM 432 C CZ2 . TRP A 1 53 ? 19.957 -24.999 -7.616 1.00 51.34 ? 53 TRP A CZ2 1 ATOM 433 C CZ3 . TRP A 1 53 ? 18.956 -24.791 -9.827 1.00 50.18 ? 53 TRP A CZ3 1 ATOM 434 C CH2 . TRP A 1 53 ? 19.496 -25.574 -8.780 1.00 51.94 ? 53 TRP A CH2 1 ATOM 435 N N . LEU A 1 54 ? 16.368 -21.121 -6.823 1.00 53.94 ? 54 LEU A N 1 ATOM 436 C CA . LEU A 1 54 ? 16.015 -21.289 -5.419 1.00 51.21 ? 54 LEU A CA 1 ATOM 437 C C . LEU A 1 54 ? 16.521 -22.628 -4.961 1.00 53.29 ? 54 LEU A C 1 ATOM 438 O O . LEU A 1 54 ? 16.160 -23.670 -5.525 1.00 54.03 ? 54 LEU A O 1 ATOM 439 C CB . LEU A 1 54 ? 14.509 -21.273 -5.217 1.00 50.99 ? 54 LEU A CB 1 ATOM 440 C CG . LEU A 1 54 ? 13.707 -20.003 -5.455 1.00 51.84 ? 54 LEU A CG 1 ATOM 441 C CD1 . LEU A 1 54 ? 12.223 -20.288 -5.235 1.00 52.38 ? 54 LEU A CD1 1 ATOM 442 C CD2 . LEU A 1 54 ? 14.157 -18.894 -4.540 1.00 52.51 ? 54 LEU A CD2 1 ATOM 443 N N . ASN A 1 55 ? 17.335 -22.617 -3.917 1.00 53.59 ? 55 ASN A N 1 ATOM 444 C CA . ASN A 1 55 ? 17.613 -23.832 -3.190 1.00 52.15 ? 55 ASN A CA 1 ATOM 445 C C . ASN A 1 55 ? 16.443 -24.131 -2.266 1.00 50.82 ? 55 ASN A C 1 ATOM 446 O O . ASN A 1 55 ? 15.620 -23.266 -2.008 1.00 49.11 ? 55 ASN A O 1 ATOM 447 C CB . ASN A 1 55 ? 18.915 -23.711 -2.415 1.00 53.45 ? 55 ASN A CB 1 ATOM 448 C CG . ASN A 1 55 ? 20.102 -24.066 -3.262 1.00 55.77 ? 55 ASN A CG 1 ATOM 449 O OD1 . ASN A 1 55 ? 20.830 -23.202 -3.711 1.00 55.40 ? 55 ASN A OD1 1 ATOM 450 N ND2 . ASN A 1 55 ? 20.303 -25.362 -3.495 1.00 59.71 ? 55 ASN A ND2 1 ATOM 451 N N . GLY A 1 56 ? 16.375 -25.360 -1.774 1.00 52.22 ? 56 GLY A N 1 ATOM 452 C CA . GLY A 1 56 ? 15.241 -25.810 -0.992 1.00 54.77 ? 56 GLY A CA 1 ATOM 453 C C . GLY A 1 56 ? 15.450 -25.681 0.499 1.00 55.30 ? 56 GLY A C 1 ATOM 454 O O . GLY A 1 56 ? 15.729 -24.586 1.006 1.00 56.77 ? 56 GLY A O 1 ATOM 455 N N . GLY A 1 57 ? 15.333 -26.815 1.187 1.00 55.31 ? 57 GLY A N 1 ATOM 456 C CA . GLY A 1 57 ? 15.530 -26.895 2.637 1.00 56.76 ? 57 GLY A CA 1 ATOM 457 C C . GLY A 1 57 ? 14.407 -27.696 3.258 1.00 56.33 ? 57 GLY A C 1 ATOM 458 O O . GLY A 1 57 ? 14.506 -28.914 3.374 1.00 55.29 ? 57 GLY A O 1 ATOM 459 N N . PRO A 1 58 ? 13.317 -27.026 3.637 1.00 54.04 ? 58 PRO A N 1 ATOM 460 C CA . PRO A 1 58 ? 13.138 -25.573 3.672 1.00 55.17 ? 58 PRO A CA 1 ATOM 461 C C . PRO A 1 58 ? 14.006 -24.956 4.743 1.00 56.55 ? 58 PRO A C 1 ATOM 462 O O . PRO A 1 58 ? 14.185 -25.552 5.809 1.00 58.65 ? 58 PRO A O 1 ATOM 463 C CB . PRO A 1 58 ? 11.674 -25.392 4.061 1.00 54.95 ? 58 PRO A CB 1 ATOM 464 C CG . PRO A 1 58 ? 11.035 -26.709 3.833 1.00 55.42 ? 58 PRO A CG 1 ATOM 465 C CD . PRO A 1 58 ? 12.090 -27.755 3.955 1.00 53.19 ? 58 PRO A CD 1 ATOM 466 N N . GLY A 1 59 ? 14.508 -23.758 4.487 1.00 56.88 ? 59 GLY A N 1 ATOM 467 C CA . GLY A 1 59 ? 15.362 -23.089 5.439 1.00 55.32 ? 59 GLY A CA 1 ATOM 468 C C . GLY A 1 59 ? 16.761 -22.906 4.944 1.00 56.28 ? 59 GLY A C 1 ATOM 469 O O . GLY A 1 59 ? 17.529 -22.200 5.587 1.00 60.50 ? 59 GLY A O 1 ATOM 470 N N . CYS A 1 60 ? 17.096 -23.503 3.801 1.00 58.86 ? 60 CYS A N 1 ATOM 471 C CA . CYS A 1 60 ? 18.458 -23.415 3.235 1.00 62.73 ? 60 CYS A CA 1 ATOM 472 C C . CYS A 1 60 ? 18.654 -22.318 2.174 1.00 60.62 ? 60 CYS A C 1 ATOM 473 O O . CYS A 1 60 ? 17.719 -21.913 1.481 1.00 60.88 ? 60 CYS A O 1 ATOM 474 C CB . CYS A 1 60 ? 18.898 -24.767 2.679 1.00 65.58 ? 60 CYS A CB 1 ATOM 475 S SG . CYS A 1 60 ? 18.857 -26.075 3.929 1.00 74.55 ? 60 CYS A SG 1 ATOM 476 N N . SER A 1 61 ? 19.893 -21.878 2.037 1.00 56.72 ? 61 SER A N 1 ATOM 477 C CA . SER A 1 61 ? 20.219 -20.693 1.274 1.00 56.11 ? 61 SER A CA 1 ATOM 478 C C . SER A 1 61 ? 20.510 -20.970 -0.177 1.00 57.27 ? 61 SER A C 1 ATOM 479 O O . SER A 1 61 ? 21.201 -21.938 -0.490 1.00 55.59 ? 61 SER A O 1 ATOM 480 C CB . SER A 1 61 ? 21.473 -20.053 1.844 1.00 56.57 ? 61 SER A CB 1 ATOM 481 O OG . SER A 1 61 ? 21.830 -18.910 1.090 1.00 58.12 ? 61 SER A OG 1 ATOM 482 N N . SER A 1 62 ? 20.027 -20.079 -1.045 1.00 56.79 ? 62 SER A N 1 ATOM 483 C CA . SER A 1 62 ? 20.335 -20.111 -2.472 1.00 56.79 ? 62 SER A CA 1 ATOM 484 C C . SER A 1 62 ? 21.757 -19.616 -2.786 1.00 61.54 ? 62 SER A C 1 ATOM 485 O O . SER A 1 62 ? 22.193 -19.669 -3.939 1.00 65.47 ? 62 SER A O 1 ATOM 486 C CB . SER A 1 62 ? 19.314 -19.288 -3.261 1.00 55.12 ? 62 SER A CB 1 ATOM 487 O OG . SER A 1 62 ? 17.995 -19.781 -3.085 1.00 52.66 ? 62 SER A OG 1 ATOM 488 N N . LEU A 1 63 ? 22.481 -19.124 -1.787 1.00 62.79 ? 63 LEU A N 1 ATOM 489 C CA . LEU A 1 63 ? 23.871 -18.754 -2.009 1.00 64.48 ? 63 LEU A CA 1 ATOM 490 C C . LEU A 1 63 ? 24.769 -19.978 -1.988 1.00 66.68 ? 63 LEU A C 1 ATOM 491 O O . LEU A 1 63 ? 25.888 -19.926 -2.484 1.00 65.63 ? 63 LEU A O 1 ATOM 492 C CB . LEU A 1 63 ? 24.336 -17.725 -0.990 1.00 65.21 ? 63 LEU A CB 1 ATOM 493 C CG . LEU A 1 63 ? 23.559 -16.403 -1.004 1.00 66.29 ? 63 LEU A CG 1 ATOM 494 C CD1 . LEU A 1 63 ? 24.277 -15.386 -0.133 1.00 65.56 ? 63 LEU A CD1 1 ATOM 495 C CD2 . LEU A 1 63 ? 23.354 -15.855 -2.414 1.00 64.95 ? 63 LEU A CD2 1 ATOM 496 N N . ASP A 1 64 ? 24.284 -21.081 -1.425 1.00 70.90 ? 64 ASP A N 1 ATOM 497 C CA . ASP A 1 64 ? 24.930 -22.381 -1.632 1.00 75.55 ? 64 ASP A CA 1 ATOM 498 C C . ASP A 1 64 ? 24.972 -22.682 -3.132 1.00 75.84 ? 64 ASP A C 1 ATOM 499 O O . ASP A 1 64 ? 26.017 -23.068 -3.662 1.00 79.38 ? 64 ASP A O 1 ATOM 500 C CB . ASP A 1 64 ? 24.187 -23.504 -0.902 1.00 79.60 ? 64 ASP A CB 1 ATOM 501 C CG . ASP A 1 64 ? 24.956 -24.824 -0.923 1.00 89.26 ? 64 ASP A CG 1 ATOM 502 O OD1 . ASP A 1 64 ? 26.143 -24.834 -0.530 1.00 92.04 ? 64 ASP A OD1 1 ATOM 503 O OD2 . ASP A 1 64 ? 24.380 -25.858 -1.326 1.00 94.15 ? 64 ASP A OD2 1 ATOM 504 N N . GLY A 1 65 ? 23.844 -22.472 -3.814 1.00 70.26 ? 65 GLY A N 1 ATOM 505 C CA . GLY A 1 65 ? 23.767 -22.638 -5.260 1.00 65.29 ? 65 GLY A CA 1 ATOM 506 C C . GLY A 1 65 ? 24.860 -21.864 -5.964 1.00 64.67 ? 65 GLY A C 1 ATOM 507 O O . GLY A 1 65 ? 25.629 -22.411 -6.769 1.00 63.88 ? 65 GLY A O 1 ATOM 508 N N . LEU A 1 66 ? 24.931 -20.581 -5.660 1.00 62.45 ? 66 LEU A N 1 ATOM 509 C CA . LEU A 1 66 ? 25.940 -19.726 -6.255 1.00 60.72 ? 66 LEU A CA 1 ATOM 510 C C . LEU A 1 66 ? 27.345 -20.237 -5.950 1.00 60.21 ? 66 LEU A C 1 ATOM 511 O O . LEU A 1 66 ? 28.114 -20.513 -6.870 1.00 57.64 ? 66 LEU A O 1 ATOM 512 C CB . LEU A 1 66 ? 25.778 -18.287 -5.765 1.00 58.15 ? 66 LEU A CB 1 ATOM 513 C CG . LEU A 1 66 ? 26.496 -17.276 -6.652 1.00 58.38 ? 66 LEU A CG 1 ATOM 514 C CD1 . LEU A 1 66 ? 25.937 -15.900 -6.413 1.00 58.21 ? 66 LEU A CD1 1 ATOM 515 C CD2 . LEU A 1 66 ? 27.995 -17.272 -6.451 1.00 58.13 ? 66 LEU A CD2 1 ATOM 516 N N . LEU A 1 67 ? 27.653 -20.389 -4.662 1.00 60.10 ? 67 LEU A N 1 ATOM 517 C CA . LEU A 1 67 ? 29.029 -20.570 -4.214 1.00 61.81 ? 67 LEU A CA 1 ATOM 518 C C . LEU A 1 67 ? 29.558 -21.991 -4.297 1.00 64.03 ? 67 LEU A C 1 ATOM 519 O O . LEU A 1 67 ? 30.777 -22.189 -4.230 1.00 63.07 ? 67 LEU A O 1 ATOM 520 C CB . LEU A 1 67 ? 29.192 -20.061 -2.787 1.00 63.37 ? 67 LEU A CB 1 ATOM 521 C CG . LEU A 1 67 ? 29.202 -18.543 -2.674 1.00 65.83 ? 67 LEU A CG 1 ATOM 522 C CD1 . LEU A 1 67 ? 28.971 -18.101 -1.233 1.00 67.76 ? 67 LEU A CD1 1 ATOM 523 C CD2 . LEU A 1 67 ? 30.501 -17.971 -3.209 1.00 67.29 ? 67 LEU A CD2 1 ATOM 524 N N . THR A 1 68 ? 28.670 -22.978 -4.423 1.00 62.77 ? 68 THR A N 1 ATOM 525 C CA . THR A 1 68 ? 29.111 -24.375 -4.485 1.00 62.44 ? 68 THR A CA 1 ATOM 526 C C . THR A 1 68 ? 28.556 -25.190 -5.657 1.00 61.84 ? 68 THR A C 1 ATOM 527 O O . THR A 1 68 ? 28.968 -26.326 -5.832 1.00 64.19 ? 68 THR A O 1 ATOM 528 C CB . THR A 1 68 ? 28.788 -25.123 -3.178 1.00 60.24 ? 68 THR A CB 1 ATOM 529 O OG1 . THR A 1 68 ? 27.400 -25.446 -3.155 1.00 67.85 ? 68 THR A OG1 1 ATOM 530 C CG2 . THR A 1 68 ? 29.124 -24.277 -1.959 1.00 60.27 ? 68 THR A CG2 1 ATOM 531 N N . GLU A 1 69 ? 27.639 -24.634 -6.447 1.00 62.64 ? 69 GLU A N 1 ATOM 532 C CA . GLU A 1 69 ? 27.010 -25.384 -7.540 1.00 61.99 ? 69 GLU A CA 1 ATOM 533 C C . GLU A 1 69 ? 27.255 -24.818 -8.945 1.00 66.74 ? 69 GLU A C 1 ATOM 534 O O . GLU A 1 69 ? 27.958 -25.441 -9.749 1.00 72.97 ? 69 GLU A O 1 ATOM 535 C CB . GLU A 1 69 ? 25.527 -25.489 -7.316 1.00 63.13 ? 69 GLU A CB 1 ATOM 536 C CG . GLU A 1 69 ? 25.121 -26.098 -5.997 1.00 64.95 ? 69 GLU A CG 1 ATOM 537 C CD . GLU A 1 69 ? 23.657 -26.457 -6.002 1.00 68.15 ? 69 GLU A CD 1 ATOM 538 O OE1 . GLU A 1 69 ? 23.302 -27.386 -6.758 1.00 66.97 ? 69 GLU A OE1 1 ATOM 539 O OE2 . GLU A 1 69 ? 22.873 -25.809 -5.266 1.00 72.71 ? 69 GLU A OE2 1 ATOM 540 N N . HIS A 1 70 ? 26.694 -23.654 -9.262 1.00 64.30 ? 70 HIS A N 1 ATOM 541 C CA . HIS A 1 70 ? 26.835 -23.129 -10.626 1.00 62.52 ? 70 HIS A CA 1 ATOM 542 C C . HIS A 1 70 ? 26.968 -21.606 -10.752 1.00 61.92 ? 70 HIS A C 1 ATOM 543 O O . HIS A 1 70 ? 26.649 -21.042 -11.793 1.00 63.85 ? 70 HIS A O 1 ATOM 544 C CB . HIS A 1 70 ? 25.657 -23.610 -11.454 1.00 63.13 ? 70 HIS A CB 1 ATOM 545 C CG . HIS A 1 70 ? 24.320 -23.239 -10.890 1.00 66.49 ? 70 HIS A CG 1 ATOM 546 N ND1 . HIS A 1 70 ? 23.224 -24.066 -10.983 1.00 66.90 ? 70 HIS A ND1 1 ATOM 547 C CD2 . HIS A 1 70 ? 23.898 -22.134 -10.234 1.00 65.09 ? 70 HIS A CD2 1 ATOM 548 C CE1 . HIS A 1 70 ? 22.187 -23.488 -10.409 1.00 64.85 ? 70 HIS A CE1 1 ATOM 549 N NE2 . HIS A 1 70 ? 22.569 -22.315 -9.947 1.00 66.21 ? 70 HIS A NE2 1 ATOM 550 N N . GLY A 1 71 ? 27.415 -20.938 -9.694 1.00 59.51 ? 71 GLY A N 1 ATOM 551 C CA . GLY A 1 71 ? 27.669 -19.507 -9.759 1.00 57.04 ? 71 GLY A CA 1 ATOM 552 C C . GLY A 1 71 ? 28.903 -19.287 -10.605 1.00 56.15 ? 71 GLY A C 1 ATOM 553 O O . GLY A 1 71 ? 29.591 -20.247 -10.942 1.00 54.79 ? 71 GLY A O 1 ATOM 554 N N . PRO A 1 72 ? 29.166 -18.038 -10.991 1.00 55.59 ? 72 PRO A N 1 ATOM 555 C CA . PRO A 1 72 ? 30.336 -17.676 -11.770 1.00 58.18 ? 72 PRO A CA 1 ATOM 556 C C . PRO A 1 72 ? 31.645 -17.998 -11.052 1.00 61.50 ? 72 PRO A C 1 ATOM 557 O O . PRO A 1 72 ? 32.693 -18.174 -11.688 1.00 64.00 ? 72 PRO A O 1 ATOM 558 C CB . PRO A 1 72 ? 30.194 -16.165 -11.953 1.00 58.80 ? 72 PRO A CB 1 ATOM 559 C CG . PRO A 1 72 ? 29.210 -15.726 -10.921 1.00 59.45 ? 72 PRO A CG 1 ATOM 560 C CD . PRO A 1 72 ? 28.292 -16.884 -10.745 1.00 58.50 ? 72 PRO A CD 1 ATOM 561 N N . PHE A 1 73 ? 31.590 -18.078 -9.736 1.00 61.08 ? 73 PHE A N 1 ATOM 562 C CA . PHE A 1 73 ? 32.752 -18.442 -8.988 1.00 60.60 ? 73 PHE A CA 1 ATOM 563 C C . PHE A 1 73 ? 32.341 -19.270 -7.794 1.00 58.54 ? 73 PHE A C 1 ATOM 564 O O . PHE A 1 73 ? 31.278 -19.059 -7.237 1.00 56.59 ? 73 PHE A O 1 ATOM 565 C CB . PHE A 1 73 ? 33.503 -17.192 -8.561 1.00 62.72 ? 73 PHE A CB 1 ATOM 566 C CG . PHE A 1 73 ? 32.624 -16.000 -8.349 1.00 62.65 ? 73 PHE A CG 1 ATOM 567 C CD1 . PHE A 1 73 ? 31.784 -15.930 -7.255 1.00 63.13 ? 73 PHE A CD1 1 ATOM 568 C CD2 . PHE A 1 73 ? 32.646 -14.931 -9.244 1.00 63.25 ? 73 PHE A CD2 1 ATOM 569 C CE1 . PHE A 1 73 ? 30.979 -14.820 -7.049 1.00 62.27 ? 73 PHE A CE1 1 ATOM 570 C CE2 . PHE A 1 73 ? 31.842 -13.825 -9.048 1.00 62.34 ? 73 PHE A CE2 1 ATOM 571 C CZ . PHE A 1 73 ? 31.008 -13.771 -7.946 1.00 61.98 ? 73 PHE A CZ 1 ATOM 572 N N . LEU A 1 74 ? 33.206 -20.198 -7.402 1.00 58.69 ? 74 LEU A N 1 ATOM 573 C CA . LEU A 1 74 ? 32.935 -21.089 -6.290 1.00 58.90 ? 74 LEU A CA 1 ATOM 574 C C . LEU A 1 74 ? 33.949 -20.876 -5.180 1.00 58.95 ? 74 LEU A C 1 ATOM 575 O O . LEU A 1 74 ? 35.150 -20.829 -5.438 1.00 60.46 ? 74 LEU A O 1 ATOM 576 C CB . LEU A 1 74 ? 33.008 -22.542 -6.745 1.00 58.06 ? 74 LEU A CB 1 ATOM 577 C CG . LEU A 1 74 ? 32.317 -22.926 -8.046 1.00 58.55 ? 74 LEU A CG 1 ATOM 578 C CD1 . LEU A 1 74 ? 32.656 -24.374 -8.368 1.00 57.37 ? 74 LEU A CD1 1 ATOM 579 C CD2 . LEU A 1 74 ? 30.815 -22.725 -7.970 1.00 59.05 ? 74 LEU A CD2 1 ATOM 580 N N . VAL A 1 75 ? 33.461 -20.767 -3.944 1.00 58.09 ? 75 VAL A N 1 ATOM 581 C CA . VAL A 1 75 ? 34.317 -20.719 -2.763 1.00 58.42 ? 75 VAL A CA 1 ATOM 582 C C . VAL A 1 75 ? 35.147 -21.990 -2.659 1.00 59.61 ? 75 VAL A C 1 ATOM 583 O O . VAL A 1 75 ? 34.649 -23.079 -2.928 1.00 59.15 ? 75 VAL A O 1 ATOM 584 C CB . VAL A 1 75 ? 33.491 -20.525 -1.479 1.00 57.52 ? 75 VAL A CB 1 ATOM 585 C CG1 . VAL A 1 75 ? 32.766 -21.793 -1.102 1.00 58.15 ? 75 VAL A CG1 1 ATOM 586 C CG2 . VAL A 1 75 ? 34.367 -20.058 -0.329 1.00 61.19 ? 75 VAL A CG2 1 ATOM 587 N N . GLN A 1 76 ? 36.421 -21.819 -2.313 1.00 64.86 ? 76 GLN A N 1 ATOM 588 C CA . GLN A 1 76 ? 37.395 -22.911 -2.177 1.00 67.95 ? 76 GLN A CA 1 ATOM 589 C C . GLN A 1 76 ? 37.539 -23.306 -0.712 1.00 68.07 ? 76 GLN A C 1 ATOM 590 O O . GLN A 1 76 ? 37.120 -22.559 0.158 1.00 69.63 ? 76 GLN A O 1 ATOM 591 C CB . GLN A 1 76 ? 38.754 -22.447 -2.704 1.00 72.35 ? 76 GLN A CB 1 ATOM 592 C CG . GLN A 1 76 ? 38.714 -21.893 -4.115 1.00 73.90 ? 76 GLN A CG 1 ATOM 593 C CD . GLN A 1 76 ? 38.443 -22.996 -5.104 1.00 71.28 ? 76 GLN A CD 1 ATOM 594 O OE1 . GLN A 1 76 ? 39.314 -23.829 -5.362 1.00 67.97 ? 76 GLN A OE1 1 ATOM 595 N NE2 . GLN A 1 76 ? 37.223 -23.047 -5.614 1.00 68.20 ? 76 GLN A NE2 1 ATOM 596 N N . PRO A 1 77 ? 38.176 -24.451 -0.425 1.00 69.51 ? 77 PRO A N 1 ATOM 597 C CA . PRO A 1 77 ? 38.139 -25.047 0.923 1.00 71.67 ? 77 PRO A CA 1 ATOM 598 C C . PRO A 1 77 ? 38.716 -24.215 2.049 1.00 75.43 ? 77 PRO A C 1 ATOM 599 O O . PRO A 1 77 ? 38.379 -24.446 3.203 1.00 76.42 ? 77 PRO A O 1 ATOM 600 C CB . PRO A 1 77 ? 38.954 -26.327 0.763 1.00 69.78 ? 77 PRO A CB 1 ATOM 601 C CG . PRO A 1 77 ? 38.872 -26.650 -0.681 1.00 69.90 ? 77 PRO A CG 1 ATOM 602 C CD . PRO A 1 77 ? 38.918 -25.312 -1.355 1.00 72.13 ? 77 PRO A CD 1 ATOM 603 N N . ASP A 1 78 ? 39.566 -23.248 1.717 1.00 80.21 ? 78 ASP A N 1 ATOM 604 C CA . ASP A 1 78 ? 40.115 -22.321 2.718 1.00 81.17 ? 78 ASP A CA 1 ATOM 605 C C . ASP A 1 78 ? 39.111 -21.294 3.229 1.00 78.67 ? 78 ASP A C 1 ATOM 606 O O . ASP A 1 78 ? 39.419 -20.522 4.107 1.00 81.27 ? 78 ASP A O 1 ATOM 607 C CB . ASP A 1 78 ? 41.353 -21.598 2.157 1.00 85.56 ? 78 ASP A CB 1 ATOM 608 C CG . ASP A 1 78 ? 41.053 -20.776 0.905 1.00 83.96 ? 78 ASP A CG 1 ATOM 609 O OD1 . ASP A 1 78 ? 39.901 -20.354 0.723 1.00 84.81 ? 78 ASP A OD1 1 ATOM 610 O OD2 . ASP A 1 78 ? 41.975 -20.549 0.107 1.00 80.66 ? 78 ASP A OD2 1 ATOM 611 N N . GLY A 1 79 ? 37.927 -21.243 2.638 1.00 83.10 ? 79 GLY A N 1 ATOM 612 C CA . GLY A 1 79 ? 36.895 -20.299 3.057 1.00 80.74 ? 79 GLY A CA 1 ATOM 613 C C . GLY A 1 79 ? 37.143 -18.865 2.642 1.00 80.32 ? 79 GLY A C 1 ATOM 614 O O . GLY A 1 79 ? 36.357 -17.988 2.970 1.00 81.06 ? 79 GLY A O 1 ATOM 615 N N . VAL A 1 80 ? 38.225 -18.629 1.906 1.00 80.20 ? 80 VAL A N 1 ATOM 616 C CA . VAL A 1 80 ? 38.726 -17.280 1.623 1.00 78.58 ? 80 VAL A CA 1 ATOM 617 C C . VAL A 1 80 ? 38.801 -16.981 0.125 1.00 79.68 ? 80 VAL A C 1 ATOM 618 O O . VAL A 1 80 ? 38.446 -15.894 -0.323 1.00 80.39 ? 80 VAL A O 1 ATOM 619 C CB . VAL A 1 80 ? 40.114 -17.108 2.264 1.00 78.01 ? 80 VAL A CB 1 ATOM 620 C CG1 . VAL A 1 80 ? 40.873 -15.950 1.655 1.00 79.89 ? 80 VAL A CG1 1 ATOM 621 C CG2 . VAL A 1 80 ? 39.966 -16.914 3.774 1.00 77.79 ? 80 VAL A CG2 1 ATOM 622 N N . THR A 1 81 ? 39.284 -17.952 -0.638 1.00 80.37 ? 81 THR A N 1 ATOM 623 C CA . THR A 1 81 ? 39.512 -17.791 -2.056 1.00 76.14 ? 81 THR A CA 1 ATOM 624 C C . THR A 1 81 ? 38.294 -18.208 -2.846 1.00 74.73 ? 81 THR A C 1 ATOM 625 O O . THR A 1 81 ? 37.693 -19.236 -2.562 1.00 74.87 ? 81 THR A O 1 ATOM 626 C CB . THR A 1 81 ? 40.694 -18.661 -2.509 1.00 78.73 ? 81 THR A CB 1 ATOM 627 O OG1 . THR A 1 81 ? 41.766 -18.583 -1.556 1.00 74.69 ? 81 THR A OG1 1 ATOM 628 C CG2 . THR A 1 81 ? 41.191 -18.229 -3.896 1.00 80.32 ? 81 THR A CG2 1 ATOM 629 N N . LEU A 1 82 ? 37.956 -17.404 -3.848 1.00 76.21 ? 82 LEU A N 1 ATOM 630 C CA . LEU A 1 82 ? 36.954 -17.740 -4.848 1.00 74.54 ? 82 LEU A CA 1 ATOM 631 C C . LEU A 1 82 ? 37.656 -18.016 -6.176 1.00 75.76 ? 82 LEU A C 1 ATOM 632 O O . LEU A 1 82 ? 38.538 -17.259 -6.576 1.00 78.44 ? 82 LEU A O 1 ATOM 633 C CB . LEU A 1 82 ? 36.010 -16.568 -5.053 1.00 74.89 ? 82 LEU A CB 1 ATOM 634 C CG . LEU A 1 82 ? 35.091 -16.123 -3.918 1.00 73.25 ? 82 LEU A CG 1 ATOM 635 C CD1 . LEU A 1 82 ? 34.037 -15.193 -4.482 1.00 73.86 ? 82 LEU A CD1 1 ATOM 636 C CD2 . LEU A 1 82 ? 34.406 -17.276 -3.233 1.00 70.82 ? 82 LEU A CD2 1 ATOM 637 N N . GLU A 1 83 ? 37.285 -19.103 -6.844 1.00 73.50 ? 83 GLU A N 1 ATOM 638 C CA . GLU A 1 83 ? 37.811 -19.412 -8.170 1.00 75.25 ? 83 GLU A CA 1 ATOM 639 C C . GLU A 1 83 ? 36.676 -19.349 -9.175 1.00 74.18 ? 83 GLU A C 1 ATOM 640 O O . GLU A 1 83 ? 35.559 -19.758 -8.873 1.00 72.01 ? 83 GLU A O 1 ATOM 641 C CB . GLU A 1 83 ? 38.455 -20.802 -8.221 1.00 78.55 ? 83 GLU A CB 1 ATOM 642 C CG . GLU A 1 83 ? 39.828 -20.937 -7.570 1.00 83.29 ? 83 GLU A CG 1 ATOM 643 C CD . GLU A 1 83 ? 40.860 -19.908 -8.043 1.00 87.42 ? 83 GLU A CD 1 ATOM 644 O OE1 . GLU A 1 83 ? 40.781 -19.398 -9.190 1.00 86.74 ? 83 GLU A OE1 1 ATOM 645 O OE2 . GLU A 1 83 ? 41.779 -19.618 -7.254 1.00 87.30 ? 83 GLU A OE2 1 ATOM 646 N N . TYR A 1 84 ? 36.962 -18.820 -10.364 1.00 71.85 ? 84 TYR A N 1 ATOM 647 C CA . TYR A 1 84 ? 35.951 -18.708 -11.387 1.00 70.38 ? 84 TYR A CA 1 ATOM 648 C C . TYR A 1 84 ? 35.499 -20.114 -11.765 1.00 72.43 ? 84 TYR A C 1 ATOM 649 O O . TYR A 1 84 ? 36.244 -21.082 -11.600 1.00 72.49 ? 84 TYR A O 1 ATOM 650 C CB . TYR A 1 84 ? 36.442 -17.917 -12.624 1.00 69.40 ? 84 TYR A CB 1 ATOM 651 C CG . TYR A 1 84 ? 36.388 -16.408 -12.450 1.00 67.70 ? 84 TYR A CG 1 ATOM 652 C CD1 . TYR A 1 84 ? 35.224 -15.700 -12.719 1.00 67.40 ? 84 TYR A CD1 1 ATOM 653 C CD2 . TYR A 1 84 ? 37.487 -15.699 -11.977 1.00 67.67 ? 84 TYR A CD2 1 ATOM 654 C CE1 . TYR A 1 84 ? 35.157 -14.328 -12.532 1.00 68.25 ? 84 TYR A CE1 1 ATOM 655 C CE2 . TYR A 1 84 ? 37.426 -14.323 -11.782 1.00 68.59 ? 84 TYR A CE2 1 ATOM 656 C CZ . TYR A 1 84 ? 36.251 -13.641 -12.071 1.00 68.69 ? 84 TYR A CZ 1 ATOM 657 O OH . TYR A 1 84 ? 36.116 -12.273 -11.921 1.00 67.35 ? 84 TYR A OH 1 ATOM 658 N N . ASN A 1 85 ? 34.268 -20.207 -12.255 1.00 69.73 ? 85 ASN A N 1 ATOM 659 C CA . ASN A 1 85 ? 33.660 -21.458 -12.606 1.00 64.39 ? 85 ASN A CA 1 ATOM 660 C C . ASN A 1 85 ? 33.443 -21.475 -14.114 1.00 63.05 ? 85 ASN A C 1 ATOM 661 O O . ASN A 1 85 ? 32.597 -20.759 -14.614 1.00 59.48 ? 85 ASN A O 1 ATOM 662 C CB . ASN A 1 85 ? 32.342 -21.585 -11.855 1.00 63.97 ? 85 ASN A CB 1 ATOM 663 C CG . ASN A 1 85 ? 31.590 -22.846 -12.189 1.00 62.35 ? 85 ASN A CG 1 ATOM 664 O OD1 . ASN A 1 85 ? 32.028 -23.660 -12.992 1.00 66.22 ? 85 ASN A OD1 1 ATOM 665 N ND2 . ASN A 1 85 ? 30.435 -22.994 -11.600 1.00 62.79 ? 85 ASN A ND2 1 ATOM 666 N N . PRO A 1 86 ? 34.179 -22.332 -14.837 1.00 66.03 ? 86 PRO A N 1 ATOM 667 C CA . PRO A 1 86 ? 34.075 -22.387 -16.309 1.00 65.19 ? 86 PRO A CA 1 ATOM 668 C C . PRO A 1 86 ? 32.750 -22.946 -16.801 1.00 67.28 ? 86 PRO A C 1 ATOM 669 O O . PRO A 1 86 ? 32.412 -22.773 -17.973 1.00 65.26 ? 86 PRO A O 1 ATOM 670 C CB . PRO A 1 86 ? 35.196 -23.342 -16.721 1.00 65.47 ? 86 PRO A CB 1 ATOM 671 C CG . PRO A 1 86 ? 35.838 -23.835 -15.460 1.00 66.17 ? 86 PRO A CG 1 ATOM 672 C CD . PRO A 1 86 ? 34.968 -23.456 -14.302 1.00 64.73 ? 86 PRO A CD 1 ATOM 673 N N . TYR A 1 87 ? 32.018 -23.624 -15.907 1.00 68.53 ? 87 TYR A N 1 ATOM 674 C CA . TYR A 1 87 ? 30.712 -24.196 -16.219 1.00 62.00 ? 87 TYR A CA 1 ATOM 675 C C . TYR A 1 87 ? 29.586 -23.394 -15.581 1.00 61.62 ? 87 TYR A C 1 ATOM 676 O O . TYR A 1 87 ? 28.491 -23.894 -15.460 1.00 62.08 ? 87 TYR A O 1 ATOM 677 C CB . TYR A 1 87 ? 30.664 -25.644 -15.768 1.00 59.12 ? 87 TYR A CB 1 ATOM 678 C CG . TYR A 1 87 ? 31.865 -26.447 -16.223 1.00 62.13 ? 87 TYR A CG 1 ATOM 679 C CD1 . TYR A 1 87 ? 32.133 -26.614 -17.573 1.00 65.21 ? 87 TYR A CD1 1 ATOM 680 C CD2 . TYR A 1 87 ? 32.755 -27.010 -15.305 1.00 61.74 ? 87 TYR A CD2 1 ATOM 681 C CE1 . TYR A 1 87 ? 33.237 -27.332 -17.995 1.00 67.36 ? 87 TYR A CE1 1 ATOM 682 C CE2 . TYR A 1 87 ? 33.865 -27.730 -15.719 1.00 62.89 ? 87 TYR A CE2 1 ATOM 683 C CZ . TYR A 1 87 ? 34.094 -27.890 -17.064 1.00 66.46 ? 87 TYR A CZ 1 ATOM 684 O OH . TYR A 1 87 ? 35.181 -28.588 -17.499 1.00 69.84 ? 87 TYR A OH 1 ATOM 685 N N . SER A 1 88 ? 29.822 -22.130 -15.239 1.00 63.94 ? 88 SER A N 1 ATOM 686 C CA . SER A 1 88 ? 28.790 -21.324 -14.577 1.00 64.63 ? 88 SER A CA 1 ATOM 687 C C . SER A 1 88 ? 27.590 -21.049 -15.444 1.00 64.03 ? 88 SER A C 1 ATOM 688 O O . SER A 1 88 ? 27.704 -20.815 -16.642 1.00 66.54 ? 88 SER A O 1 ATOM 689 C CB . SER A 1 88 ? 29.317 -19.971 -14.133 1.00 67.62 ? 88 SER A CB 1 ATOM 690 O OG . SER A 1 88 ? 28.234 -19.172 -13.662 1.00 65.91 ? 88 SER A OG 1 ATOM 691 N N . TRP A 1 89 ? 26.431 -21.039 -14.814 1.00 62.97 ? 89 TRP A N 1 ATOM 692 C CA . TRP A 1 89 ? 25.183 -20.850 -15.541 1.00 63.04 ? 89 TRP A CA 1 ATOM 693 C C . TRP A 1 89 ? 25.036 -19.427 -16.038 1.00 63.00 ? 89 TRP A C 1 ATOM 694 O O . TRP A 1 89 ? 24.348 -19.193 -17.036 1.00 62.15 ? 89 TRP A O 1 ATOM 695 C CB . TRP A 1 89 ? 23.981 -21.266 -14.678 1.00 59.87 ? 89 TRP A CB 1 ATOM 696 C CG . TRP A 1 89 ? 23.850 -22.745 -14.543 1.00 57.88 ? 89 TRP A CG 1 ATOM 697 C CD1 . TRP A 1 89 ? 24.827 -23.685 -14.755 1.00 56.99 ? 89 TRP A CD1 1 ATOM 698 C CD2 . TRP A 1 89 ? 22.689 -23.466 -14.141 1.00 55.86 ? 89 TRP A CD2 1 ATOM 699 N NE1 . TRP A 1 89 ? 24.334 -24.933 -14.518 1.00 55.11 ? 89 TRP A NE1 1 ATOM 700 C CE2 . TRP A 1 89 ? 23.025 -24.828 -14.136 1.00 53.59 ? 89 TRP A CE2 1 ATOM 701 C CE3 . TRP A 1 89 ? 21.398 -23.093 -13.788 1.00 57.58 ? 89 TRP A CE3 1 ATOM 702 C CZ2 . TRP A 1 89 ? 22.112 -25.819 -13.806 1.00 52.65 ? 89 TRP A CZ2 1 ATOM 703 C CZ3 . TRP A 1 89 ? 20.494 -24.078 -13.445 1.00 56.56 ? 89 TRP A CZ3 1 ATOM 704 C CH2 . TRP A 1 89 ? 20.861 -25.428 -13.456 1.00 54.72 ? 89 TRP A CH2 1 ATOM 705 N N . ASN A 1 90 ? 25.697 -18.482 -15.378 1.00 62.83 ? 90 ASN A N 1 ATOM 706 C CA . ASN A 1 90 ? 25.647 -17.104 -15.850 1.00 65.65 ? 90 ASN A CA 1 ATOM 707 C C . ASN A 1 90 ? 26.563 -16.866 -17.056 1.00 68.00 ? 90 ASN A C 1 ATOM 708 O O . ASN A 1 90 ? 26.792 -15.716 -17.437 1.00 74.85 ? 90 ASN A O 1 ATOM 709 C CB . ASN A 1 90 ? 25.990 -16.116 -14.744 1.00 65.14 ? 90 ASN A CB 1 ATOM 710 C CG . ASN A 1 90 ? 27.472 -15.840 -14.661 1.00 70.87 ? 90 ASN A CG 1 ATOM 711 O OD1 . ASN A 1 90 ? 28.287 -16.766 -14.679 1.00 69.76 ? 90 ASN A OD1 1 ATOM 712 N ND2 . ASN A 1 90 ? 27.839 -14.559 -14.600 1.00 74.15 ? 90 ASN A ND2 1 ATOM 713 N N . LEU A 1 91 ? 27.100 -17.931 -17.650 1.00 65.85 ? 91 LEU A N 1 ATOM 714 C CA . LEU A 1 91 ? 27.772 -17.801 -18.937 1.00 66.14 ? 91 LEU A CA 1 ATOM 715 C C . LEU A 1 91 ? 26.778 -17.384 -20.011 1.00 69.29 ? 91 LEU A C 1 ATOM 716 O O . LEU A 1 91 ? 27.121 -16.612 -20.904 1.00 70.52 ? 91 LEU A O 1 ATOM 717 C CB . LEU A 1 91 ? 28.477 -19.097 -19.350 1.00 64.18 ? 91 LEU A CB 1 ATOM 718 C CG . LEU A 1 91 ? 29.805 -19.385 -18.632 1.00 63.23 ? 91 LEU A CG 1 ATOM 719 C CD1 . LEU A 1 91 ? 30.255 -20.809 -18.916 1.00 62.12 ? 91 LEU A CD1 1 ATOM 720 C CD2 . LEU A 1 91 ? 30.901 -18.395 -18.994 1.00 61.60 ? 91 LEU A CD2 1 ATOM 721 N N . ILE A 1 92 ? 25.549 -17.885 -19.898 1.00 68.92 ? 92 ILE A N 1 ATOM 722 C CA . ILE A 1 92 ? 24.507 -17.688 -20.905 1.00 68.45 ? 92 ILE A CA 1 ATOM 723 C C . ILE A 1 92 ? 23.183 -17.235 -20.304 1.00 71.12 ? 92 ILE A C 1 ATOM 724 O O . ILE A 1 92 ? 22.150 -17.360 -20.940 1.00 75.34 ? 92 ILE A O 1 ATOM 725 C CB . ILE A 1 92 ? 24.238 -18.991 -21.663 1.00 67.94 ? 92 ILE A CB 1 ATOM 726 C CG1 . ILE A 1 92 ? 23.815 -20.105 -20.677 1.00 67.54 ? 92 ILE A CG1 1 ATOM 727 C CG2 . ILE A 1 92 ? 25.472 -19.378 -22.455 1.00 69.66 ? 92 ILE A CG2 1 ATOM 728 C CD1 . ILE A 1 92 ? 23.363 -21.399 -21.324 1.00 66.81 ? 92 ILE A CD1 1 ATOM 729 N N . ALA A 1 93 ? 23.194 -16.739 -19.075 1.00 71.26 ? 93 ALA A N 1 ATOM 730 C CA . ALA A 1 93 ? 21.960 -16.318 -18.438 1.00 71.24 ? 93 ALA A CA 1 ATOM 731 C C . ALA A 1 93 ? 22.190 -15.284 -17.339 1.00 69.22 ? 93 ALA A C 1 ATOM 732 O O . ALA A 1 93 ? 23.275 -15.201 -16.769 1.00 70.64 ? 93 ALA A O 1 ATOM 733 C CB . ALA A 1 93 ? 21.238 -17.525 -17.873 1.00 71.44 ? 93 ALA A CB 1 ATOM 734 N N . ASN A 1 94 ? 21.165 -14.494 -17.068 1.00 65.29 ? 94 ASN A N 1 ATOM 735 C CA . ASN A 1 94 ? 21.174 -13.609 -15.921 1.00 67.45 ? 94 ASN A CA 1 ATOM 736 C C . ASN A 1 94 ? 20.529 -14.386 -14.796 1.00 68.91 ? 94 ASN A C 1 ATOM 737 O O . ASN A 1 94 ? 19.320 -14.622 -14.814 1.00 67.79 ? 94 ASN A O 1 ATOM 738 C CB . ASN A 1 94 ? 20.413 -12.320 -16.216 1.00 67.56 ? 94 ASN A CB 1 ATOM 739 C CG . ASN A 1 94 ? 20.878 -11.651 -17.506 1.00 66.78 ? 94 ASN A CG 1 ATOM 740 O OD1 . ASN A 1 94 ? 22.020 -11.232 -17.607 1.00 63.57 ? 94 ASN A OD1 1 ATOM 741 N ND2 . ASN A 1 94 ? 19.991 -11.568 -18.502 1.00 67.12 ? 94 ASN A ND2 1 ATOM 742 N N . VAL A 1 95 ? 21.341 -14.803 -13.826 1.00 70.41 ? 95 VAL A N 1 ATOM 743 C CA . VAL A 1 95 ? 20.897 -15.720 -12.782 1.00 67.32 ? 95 VAL A CA 1 ATOM 744 C C . VAL A 1 95 ? 20.619 -14.903 -11.530 1.00 66.28 ? 95 VAL A C 1 ATOM 745 O O . VAL A 1 95 ? 21.501 -14.203 -11.038 1.00 69.53 ? 95 VAL A O 1 ATOM 746 C CB . VAL A 1 95 ? 21.960 -16.801 -12.478 1.00 67.57 ? 95 VAL A CB 1 ATOM 747 C CG1 . VAL A 1 95 ? 21.322 -18.011 -11.829 1.00 66.48 ? 95 VAL A CG1 1 ATOM 748 C CG2 . VAL A 1 95 ? 22.688 -17.228 -13.747 1.00 70.63 ? 95 VAL A CG2 1 ATOM 749 N N . LEU A 1 96 ? 19.403 -15.002 -11.016 1.00 65.82 ? 96 LEU A N 1 ATOM 750 C CA . LEU A 1 96 ? 19.015 -14.331 -9.766 1.00 65.18 ? 96 LEU A CA 1 ATOM 751 C C . LEU A 1 96 ? 18.950 -15.321 -8.605 1.00 60.88 ? 96 LEU A C 1 ATOM 752 O O . LEU A 1 96 ? 17.963 -16.042 -8.469 1.00 63.28 ? 96 LEU A O 1 ATOM 753 C CB . LEU A 1 96 ? 17.656 -13.634 -9.949 1.00 65.24 ? 96 LEU A CB 1 ATOM 754 C CG . LEU A 1 96 ? 17.104 -12.818 -8.766 1.00 65.90 ? 96 LEU A CG 1 ATOM 755 C CD1 . LEU A 1 96 ? 18.050 -11.706 -8.326 1.00 64.65 ? 96 LEU A CD1 1 ATOM 756 C CD2 . LEU A 1 96 ? 15.742 -12.233 -9.116 1.00 66.59 ? 96 LEU A CD2 1 ATOM 757 N N . TYR A 1 97 ? 19.994 -15.360 -7.778 1.00 61.32 ? 97 TYR A N 1 ATOM 758 C CA . TYR A 1 97 ? 20.049 -16.253 -6.592 1.00 60.45 ? 97 TYR A CA 1 ATOM 759 C C . TYR A 1 97 ? 19.329 -15.588 -5.442 1.00 56.19 ? 97 TYR A C 1 ATOM 760 O O . TYR A 1 97 ? 19.778 -14.556 -4.978 1.00 55.79 ? 97 TYR A O 1 ATOM 761 C CB . TYR A 1 97 ? 21.495 -16.557 -6.178 1.00 59.06 ? 97 TYR A CB 1 ATOM 762 C CG . TYR A 1 97 ? 22.255 -17.309 -7.225 1.00 60.00 ? 97 TYR A CG 1 ATOM 763 C CD1 . TYR A 1 97 ? 22.846 -16.645 -8.291 1.00 62.00 ? 97 TYR A CD1 1 ATOM 764 C CD2 . TYR A 1 97 ? 22.349 -18.694 -7.183 1.00 61.00 ? 97 TYR A CD2 1 ATOM 765 C CE1 . TYR A 1 97 ? 23.523 -17.341 -9.277 1.00 63.23 ? 97 TYR A CE1 1 ATOM 766 C CE2 . TYR A 1 97 ? 23.020 -19.398 -8.171 1.00 59.88 ? 97 TYR A CE2 1 ATOM 767 C CZ . TYR A 1 97 ? 23.602 -18.713 -9.215 1.00 61.94 ? 97 TYR A CZ 1 ATOM 768 O OH . TYR A 1 97 ? 24.274 -19.373 -10.208 1.00 63.97 ? 97 TYR A OH 1 ATOM 769 N N . LEU A 1 98 ? 18.213 -16.166 -4.997 1.00 55.90 ? 98 LEU A N 1 ATOM 770 C CA . LEU A 1 98 ? 17.344 -15.514 -3.996 1.00 60.11 ? 98 LEU A CA 1 ATOM 771 C C . LEU A 1 98 ? 17.282 -16.259 -2.678 1.00 59.83 ? 98 LEU A C 1 ATOM 772 O O . LEU A 1 98 ? 16.833 -17.411 -2.639 1.00 68.78 ? 98 LEU A O 1 ATOM 773 C CB . LEU A 1 98 ? 15.925 -15.374 -4.533 1.00 60.86 ? 98 LEU A CB 1 ATOM 774 C CG . LEU A 1 98 ? 14.990 -14.508 -3.690 1.00 61.57 ? 98 LEU A CG 1 ATOM 775 C CD1 . LEU A 1 98 ? 15.478 -13.072 -3.604 1.00 61.35 ? 98 LEU A CD1 1 ATOM 776 C CD2 . LEU A 1 98 ? 13.588 -14.553 -4.263 1.00 60.18 ? 98 LEU A CD2 1 ATOM 777 N N . GLU A 1 99 ? 17.734 -15.625 -1.602 1.00 54.89 ? 99 GLU A N 1 ATOM 778 C CA . GLU A 1 99 ? 17.669 -16.259 -0.286 1.00 54.26 ? 99 GLU A CA 1 ATOM 779 C C . GLU A 1 99 ? 16.261 -16.144 0.276 1.00 52.45 ? 99 GLU A C 1 ATOM 780 O O . GLU A 1 99 ? 15.780 -15.051 0.550 1.00 51.84 ? 99 GLU A O 1 ATOM 781 C CB . GLU A 1 99 ? 18.671 -15.644 0.674 1.00 53.39 ? 99 GLU A CB 1 ATOM 782 C CG . GLU A 1 99 ? 20.094 -15.974 0.323 1.00 53.13 ? 99 GLU A CG 1 ATOM 783 C CD . GLU A 1 99 ? 21.061 -15.554 1.400 1.00 54.83 ? 99 GLU A CD 1 ATOM 784 O OE1 . GLU A 1 99 ? 21.093 -14.346 1.726 1.00 55.52 ? 99 GLU A OE1 1 ATOM 785 O OE2 . GLU A 1 99 ? 21.792 -16.435 1.916 1.00 53.72 ? 99 GLU A OE2 1 ATOM 786 N N . SER A 1 100 ? 15.614 -17.280 0.453 1.00 51.69 ? 100 SER A N 1 ATOM 787 C CA . SER A 1 100 ? 14.202 -17.303 0.803 1.00 52.25 ? 100 SER A CA 1 ATOM 788 C C . SER A 1 100 ? 13.859 -18.616 1.490 1.00 52.13 ? 100 SER A C 1 ATOM 789 O O . SER A 1 100 ? 14.543 -19.620 1.282 1.00 53.66 ? 100 SER A O 1 ATOM 790 C CB . SER A 1 100 ? 13.374 -17.089 -0.471 1.00 53.41 ? 100 SER A CB 1 ATOM 791 O OG . SER A 1 100 ? 12.272 -17.988 -0.594 1.00 54.73 ? 100 SER A OG 1 ATOM 792 N N . PRO A 1 101 ? 12.819 -18.621 2.329 1.00 54.42 ? 101 PRO A N 1 ATOM 793 C CA . PRO A 1 101 ? 11.947 -17.509 2.694 1.00 56.61 ? 101 PRO A CA 1 ATOM 794 C C . PRO A 1 101 ? 12.594 -16.615 3.739 1.00 58.08 ? 101 PRO A C 1 ATOM 795 O O . PRO A 1 101 ? 13.730 -16.859 4.134 1.00 59.00 ? 101 PRO A O 1 ATOM 796 C CB . PRO A 1 101 ? 10.717 -18.218 3.269 1.00 54.73 ? 101 PRO A CB 1 ATOM 797 C CG . PRO A 1 101 ? 11.294 -19.436 3.907 1.00 55.69 ? 101 PRO A CG 1 ATOM 798 C CD . PRO A 1 101 ? 12.389 -19.877 2.971 1.00 56.52 ? 101 PRO A CD 1 ATOM 799 N N . ALA A 1 102 ? 11.863 -15.602 4.186 1.00 60.45 ? 102 ALA A N 1 ATOM 800 C CA . ALA A 1 102 ? 12.315 -14.713 5.264 1.00 60.59 ? 102 ALA A CA 1 ATOM 801 C C . ALA A 1 102 ? 13.014 -15.446 6.401 1.00 60.65 ? 102 ALA A C 1 ATOM 802 O O . ALA A 1 102 ? 12.421 -16.329 7.032 1.00 62.78 ? 102 ALA A O 1 ATOM 803 C CB . ALA A 1 102 ? 11.133 -13.943 5.828 1.00 61.37 ? 102 ALA A CB 1 ATOM 804 N N . GLY A 1 103 ? 14.261 -15.064 6.664 1.00 61.04 ? 103 GLY A N 1 ATOM 805 C CA . GLY A 1 103 ? 15.033 -15.594 7.786 1.00 65.02 ? 103 GLY A CA 1 ATOM 806 C C . GLY A 1 103 ? 16.218 -16.450 7.349 1.00 68.80 ? 103 GLY A C 1 ATOM 807 O O . GLY A 1 103 ? 17.185 -16.619 8.094 1.00 68.09 ? 103 GLY A O 1 ATOM 808 N N . VAL A 1 104 ? 16.125 -17.010 6.147 1.00 66.97 ? 104 VAL A N 1 ATOM 809 C CA . VAL A 1 104 ? 17.198 -17.800 5.568 1.00 62.83 ? 104 VAL A CA 1 ATOM 810 C C . VAL A 1 104 ? 18.345 -16.888 5.145 1.00 62.86 ? 104 VAL A C 1 ATOM 811 O O . VAL A 1 104 ? 18.112 -15.809 4.580 1.00 60.97 ? 104 VAL A O 1 ATOM 812 C CB . VAL A 1 104 ? 16.701 -18.562 4.333 1.00 61.27 ? 104 VAL A CB 1 ATOM 813 C CG1 . VAL A 1 104 ? 17.840 -19.309 3.668 1.00 61.87 ? 104 VAL A CG1 1 ATOM 814 C CG2 . VAL A 1 104 ? 15.598 -19.518 4.724 1.00 61.28 ? 104 VAL A CG2 1 ATOM 815 N N . GLY A 1 105 ? 19.572 -17.325 5.428 1.00 60.66 ? 105 GLY A N 1 ATOM 816 C CA . GLY A 1 105 ? 20.776 -16.592 5.060 1.00 59.84 ? 105 GLY A CA 1 ATOM 817 C C . GLY A 1 105 ? 20.816 -15.176 5.596 1.00 61.92 ? 105 GLY A C 1 ATOM 818 O O . GLY A 1 105 ? 20.787 -14.974 6.801 1.00 60.38 ? 105 GLY A O 1 ATOM 819 N N . PHE A 1 106 ? 20.887 -14.199 4.693 1.00 63.80 ? 106 PHE A N 1 ATOM 820 C CA . PHE A 1 106 ? 20.858 -12.780 5.052 1.00 63.71 ? 106 PHE A CA 1 ATOM 821 C C . PHE A 1 106 ? 19.455 -12.170 4.932 1.00 62.40 ? 106 PHE A C 1 ATOM 822 O O . PHE A 1 106 ? 19.273 -10.973 5.148 1.00 61.97 ? 106 PHE A O 1 ATOM 823 C CB . PHE A 1 106 ? 21.824 -12.001 4.159 1.00 64.46 ? 106 PHE A CB 1 ATOM 824 C CG . PHE A 1 106 ? 23.270 -12.311 4.401 1.00 66.83 ? 106 PHE A CG 1 ATOM 825 C CD1 . PHE A 1 106 ? 23.803 -12.286 5.685 1.00 70.23 ? 106 PHE A CD1 1 ATOM 826 C CD2 . PHE A 1 106 ? 24.122 -12.578 3.339 1.00 69.17 ? 106 PHE A CD2 1 ATOM 827 C CE1 . PHE A 1 106 ? 25.148 -12.549 5.917 1.00 71.36 ? 106 PHE A CE1 1 ATOM 828 C CE2 . PHE A 1 106 ? 25.467 -12.849 3.563 1.00 73.43 ? 106 PHE A CE2 1 ATOM 829 C CZ . PHE A 1 106 ? 25.982 -12.834 4.857 1.00 71.40 ? 106 PHE A CZ 1 ATOM 830 N N . SER A 1 107 ? 18.467 -12.975 4.571 1.00 58.93 ? 107 SER A N 1 ATOM 831 C CA . SER A 1 107 ? 17.112 -12.476 4.462 1.00 58.03 ? 107 SER A CA 1 ATOM 832 C C . SER A 1 107 ? 16.514 -12.376 5.851 1.00 59.89 ? 107 SER A C 1 ATOM 833 O O . SER A 1 107 ? 16.768 -13.221 6.712 1.00 55.46 ? 107 SER A O 1 ATOM 834 C CB . SER A 1 107 ? 16.266 -13.390 3.576 1.00 58.28 ? 107 SER A CB 1 ATOM 835 O OG . SER A 1 107 ? 16.762 -13.408 2.245 1.00 58.82 ? 107 SER A OG 1 ATOM 836 N N . TYR A 1 108 ? 15.694 -11.356 6.055 1.00 65.41 ? 108 TYR A N 1 ATOM 837 C CA . TYR A 1 108 ? 15.040 -11.128 7.339 1.00 70.14 ? 108 TYR A CA 1 ATOM 838 C C . TYR A 1 108 ? 13.653 -10.517 7.169 1.00 75.17 ? 108 TYR A C 1 ATOM 839 O O . TYR A 1 108 ? 13.206 -10.254 6.051 1.00 77.06 ? 108 TYR A O 1 ATOM 840 C CB . TYR A 1 108 ? 15.887 -10.187 8.177 1.00 70.78 ? 108 TYR A CB 1 ATOM 841 C CG . TYR A 1 108 ? 15.981 -8.800 7.599 1.00 71.47 ? 108 TYR A CG 1 ATOM 842 C CD1 . TYR A 1 108 ? 16.818 -8.532 6.524 1.00 71.14 ? 108 TYR A CD1 1 ATOM 843 C CD2 . TYR A 1 108 ? 15.246 -7.754 8.132 1.00 76.13 ? 108 TYR A CD2 1 ATOM 844 C CE1 . TYR A 1 108 ? 16.927 -7.267 5.999 1.00 70.72 ? 108 TYR A CE1 1 ATOM 845 C CE2 . TYR A 1 108 ? 15.340 -6.481 7.597 1.00 78.02 ? 108 TYR A CE2 1 ATOM 846 C CZ . TYR A 1 108 ? 16.191 -6.251 6.537 1.00 73.98 ? 108 TYR A CZ 1 ATOM 847 O OH . TYR A 1 108 ? 16.295 -5.006 5.994 1.00 79.82 ? 108 TYR A OH 1 ATOM 848 N N . SER A 1 109 ? 12.982 -10.308 8.296 1.00 78.68 ? 109 SER A N 1 ATOM 849 C CA . SER A 1 109 ? 11.789 -9.473 8.356 1.00 81.91 ? 109 SER A CA 1 ATOM 850 C C . SER A 1 109 ? 11.898 -8.564 9.566 1.00 80.66 ? 109 SER A C 1 ATOM 851 O O . SER A 1 109 ? 12.594 -8.885 10.520 1.00 79.84 ? 109 SER A O 1 ATOM 852 C CB . SER A 1 109 ? 10.542 -10.331 8.481 1.00 85.25 ? 109 SER A CB 1 ATOM 853 O OG . SER A 1 109 ? 10.483 -10.933 9.762 1.00 93.37 ? 109 SER A OG 1 ATOM 854 N N . ASP A 1 110 ? 11.207 -7.436 9.528 1.00 85.08 ? 110 ASP A N 1 ATOM 855 C CA . ASP A 1 110 ? 11.231 -6.481 10.636 1.00 86.79 ? 110 ASP A CA 1 ATOM 856 C C . ASP A 1 110 ? 10.752 -7.105 11.938 1.00 87.06 ? 110 ASP A C 1 ATOM 857 O O . ASP A 1 110 ? 11.357 -6.897 12.987 1.00 89.42 ? 110 ASP A O 1 ATOM 858 C CB . ASP A 1 110 ? 10.379 -5.260 10.318 1.00 87.92 ? 110 ASP A CB 1 ATOM 859 C CG . ASP A 1 110 ? 10.970 -4.406 9.223 1.00 92.49 ? 110 ASP A CG 1 ATOM 860 O OD1 . ASP A 1 110 ? 12.161 -4.598 8.881 1.00 97.22 ? 110 ASP A OD1 1 ATOM 861 O OD2 . ASP A 1 110 ? 10.241 -3.531 8.707 1.00 93.48 ? 110 ASP A OD2 1 ATOM 862 N N . ASP A 1 111 ? 9.677 -7.873 11.867 1.00 84.70 ? 111 ASP A N 1 ATOM 863 C CA . ASP A 1 111 ? 9.127 -8.510 13.057 1.00 84.55 ? 111 ASP A CA 1 ATOM 864 C C . ASP A 1 111 ? 9.848 -9.802 13.449 1.00 84.58 ? 111 ASP A C 1 ATOM 865 O O . ASP A 1 111 ? 9.592 -10.345 14.505 1.00 88.13 ? 111 ASP A O 1 ATOM 866 C CB . ASP A 1 111 ? 7.621 -8.758 12.890 1.00 88.64 ? 111 ASP A CB 1 ATOM 867 C CG . ASP A 1 111 ? 7.288 -9.711 11.748 1.00 90.04 ? 111 ASP A CG 1 ATOM 868 O OD1 . ASP A 1 111 ? 8.030 -9.754 10.749 1.00 94.26 ? 111 ASP A OD1 1 ATOM 869 O OD2 . ASP A 1 111 ? 6.267 -10.411 11.851 1.00 89.01 ? 111 ASP A OD2 1 ATOM 870 N N . LYS A 1 112 ? 10.735 -10.302 12.600 1.00 85.83 ? 112 LYS A N 1 ATOM 871 C CA . LYS A 1 112 ? 11.503 -11.520 12.878 1.00 87.16 ? 112 LYS A CA 1 ATOM 872 C C . LYS A 1 112 ? 10.681 -12.792 13.116 1.00 86.35 ? 112 LYS A C 1 ATOM 873 O O . LYS A 1 112 ? 11.211 -13.765 13.651 1.00 86.68 ? 112 LYS A O 1 ATOM 874 C CB . LYS A 1 112 ? 12.451 -11.332 14.073 1.00 91.35 ? 112 LYS A CB 1 ATOM 875 C CG . LYS A 1 112 ? 13.430 -10.173 13.966 1.00 95.98 ? 112 LYS A CG 1 ATOM 876 C CD . LYS A 1 112 ? 14.853 -10.598 14.328 1.00 99.16 ? 112 LYS A CD 1 ATOM 877 C CE . LYS A 1 112 ? 14.994 -11.141 15.744 1.00 100.38 ? 112 LYS A CE 1 ATOM 878 N NZ . LYS A 1 112 ? 15.260 -10.070 16.733 1.00 101.25 ? 112 LYS A NZ 1 ATOM 879 N N . PHE A 1 113 ? 9.406 -12.806 12.745 1.00 81.43 ? 113 PHE A N 1 ATOM 880 C CA . PHE A 1 113 ? 8.606 -14.024 12.887 1.00 80.66 ? 113 PHE A CA 1 ATOM 881 C C . PHE A 1 113 ? 8.822 -14.816 11.616 1.00 74.09 ? 113 PHE A C 1 ATOM 882 O O . PHE A 1 113 ? 8.404 -14.397 10.540 1.00 73.74 ? 113 PHE A O 1 ATOM 883 C CB . PHE A 1 113 ? 7.119 -13.697 13.096 1.00 87.59 ? 113 PHE A CB 1 ATOM 884 C CG . PHE A 1 113 ? 6.250 -14.896 13.404 1.00 89.47 ? 113 PHE A CG 1 ATOM 885 C CD1 . PHE A 1 113 ? 6.488 -15.687 14.522 1.00 91.53 ? 113 PHE A CD1 1 ATOM 886 C CD2 . PHE A 1 113 ? 5.165 -15.209 12.591 1.00 91.36 ? 113 PHE A CD2 1 ATOM 887 C CE1 . PHE A 1 113 ? 5.679 -16.778 14.807 1.00 93.80 ? 113 PHE A CE1 1 ATOM 888 C CE2 . PHE A 1 113 ? 4.353 -16.297 12.874 1.00 93.18 ? 113 PHE A CE2 1 ATOM 889 C CZ . PHE A 1 113 ? 4.610 -17.081 13.986 1.00 93.62 ? 113 PHE A CZ 1 ATOM 890 N N . TYR A 1 114 ? 9.483 -15.955 11.728 1.00 72.02 ? 114 TYR A N 1 ATOM 891 C CA . TYR A 1 114 ? 9.910 -16.699 10.542 1.00 67.57 ? 114 TYR A CA 1 ATOM 892 C C . TYR A 1 114 ? 9.156 -17.993 10.307 1.00 65.95 ? 114 TYR A C 1 ATOM 893 O O . TYR A 1 114 ? 9.467 -18.712 9.363 1.00 71.93 ? 114 TYR A O 1 ATOM 894 C CB . TYR A 1 114 ? 11.417 -16.950 10.610 1.00 65.25 ? 114 TYR A CB 1 ATOM 895 C CG . TYR A 1 114 ? 12.260 -15.693 10.555 1.00 64.52 ? 114 TYR A CG 1 ATOM 896 C CD1 . TYR A 1 114 ? 12.017 -14.702 9.614 1.00 62.81 ? 114 TYR A CD1 1 ATOM 897 C CD2 . TYR A 1 114 ? 13.313 -15.499 11.439 1.00 68.15 ? 114 TYR A CD2 1 ATOM 898 C CE1 . TYR A 1 114 ? 12.789 -13.562 9.555 1.00 63.84 ? 114 TYR A CE1 1 ATOM 899 C CE2 . TYR A 1 114 ? 14.099 -14.352 11.381 1.00 67.40 ? 114 TYR A CE2 1 ATOM 900 C CZ . TYR A 1 114 ? 13.827 -13.392 10.431 1.00 64.08 ? 114 TYR A CZ 1 ATOM 901 O OH . TYR A 1 114 ? 14.587 -12.259 10.366 1.00 63.89 ? 114 TYR A OH 1 ATOM 902 N N . ALA A 1 115 ? 8.179 -18.309 11.158 1.00 66.92 ? 115 ALA A N 1 ATOM 903 C CA . ALA A 1 115 ? 7.255 -19.412 10.872 1.00 61.62 ? 115 ALA A CA 1 ATOM 904 C C . ALA A 1 115 ? 6.502 -19.037 9.622 1.00 59.83 ? 115 ALA A C 1 ATOM 905 O O . ALA A 1 115 ? 6.057 -17.890 9.490 1.00 58.30 ? 115 ALA A O 1 ATOM 906 C CB . ALA A 1 115 ? 6.286 -19.644 12.009 1.00 60.99 ? 115 ALA A CB 1 ATOM 907 N N . THR A 1 116 ? 6.395 -19.984 8.696 1.00 57.23 ? 116 THR A N 1 ATOM 908 C CA . THR A 1 116 ? 5.773 -19.726 7.418 1.00 57.54 ? 116 THR A CA 1 ATOM 909 C C . THR A 1 116 ? 5.286 -21.040 6.818 1.00 60.82 ? 116 THR A C 1 ATOM 910 O O . THR A 1 116 ? 5.319 -22.074 7.484 1.00 61.06 ? 116 THR A O 1 ATOM 911 C CB . THR A 1 116 ? 6.734 -18.953 6.477 1.00 57.58 ? 116 THR A CB 1 ATOM 912 O OG1 . THR A 1 116 ? 6.019 -18.447 5.345 1.00 63.99 ? 116 THR A OG1 1 ATOM 913 C CG2 . THR A 1 116 ? 7.885 -19.803 5.992 1.00 55.88 ? 116 THR A CG2 1 ATOM 914 N N . ASN A 1 117 ? 4.784 -20.986 5.586 1.00 64.35 ? 117 ASN A N 1 ATOM 915 C CA . ASN A 1 117 ? 4.241 -22.164 4.914 1.00 66.75 ? 117 ASN A CA 1 ATOM 916 C C . ASN A 1 117 ? 4.222 -21.995 3.390 1.00 64.12 ? 117 ASN A C 1 ATOM 917 O O . ASN A 1 117 ? 4.412 -20.889 2.890 1.00 65.09 ? 117 ASN A O 1 ATOM 918 C CB . ASN A 1 117 ? 2.843 -22.481 5.451 1.00 69.38 ? 117 ASN A CB 1 ATOM 919 C CG . ASN A 1 117 ? 1.814 -21.436 5.066 1.00 73.86 ? 117 ASN A CG 1 ATOM 920 O OD1 . ASN A 1 117 ? 1.786 -20.963 3.917 1.00 74.61 ? 117 ASN A OD1 1 ATOM 921 N ND2 . ASN A 1 117 ? 0.948 -21.075 6.028 1.00 73.23 ? 117 ASN A ND2 1 ATOM 922 N N . ASP A 1 118 ? 3.975 -23.085 2.672 1.00 60.13 ? 118 ASP A N 1 ATOM 923 C CA . ASP A 1 118 ? 4.119 -23.112 1.216 1.00 60.24 ? 118 ASP A CA 1 ATOM 924 C C . ASP A 1 118 ? 3.380 -21.963 0.488 1.00 61.57 ? 118 ASP A C 1 ATOM 925 O O . ASP A 1 118 ? 3.943 -21.324 -0.405 1.00 59.31 ? 118 ASP A O 1 ATOM 926 C CB . ASP A 1 118 ? 3.626 -24.441 0.670 1.00 60.37 ? 118 ASP A CB 1 ATOM 927 C CG . ASP A 1 118 ? 4.432 -25.617 1.158 1.00 60.15 ? 118 ASP A CG 1 ATOM 928 O OD1 . ASP A 1 118 ? 5.658 -25.517 1.308 1.00 56.78 ? 118 ASP A OD1 1 ATOM 929 O OD2 . ASP A 1 118 ? 3.820 -26.678 1.378 1.00 64.71 ? 118 ASP A OD2 1 ATOM 930 N N . THR A 1 119 ? 2.135 -21.700 0.879 1.00 63.97 ? 119 THR A N 1 ATOM 931 C CA . THR A 1 119 ? 1.333 -20.654 0.234 1.00 65.26 ? 119 THR A CA 1 ATOM 932 C C . THR A 1 119 ? 1.910 -19.283 0.520 1.00 63.83 ? 119 THR A C 1 ATOM 933 O O . THR A 1 119 ? 1.916 -18.418 -0.359 1.00 63.12 ? 119 THR A O 1 ATOM 934 C CB . THR A 1 119 ? -0.163 -20.681 0.660 1.00 68.42 ? 119 THR A CB 1 ATOM 935 O OG1 . THR A 1 119 ? -0.287 -20.776 2.090 1.00 68.61 ? 119 THR A OG1 1 ATOM 936 C CG2 . THR A 1 119 ? -0.878 -21.865 0.018 1.00 69.05 ? 119 THR A CG2 1 ATOM 937 N N . GLU A 1 120 ? 2.387 -19.076 1.744 1.00 61.60 ? 120 GLU A N 1 ATOM 938 C CA . GLU A 1 120 ? 2.942 -17.782 2.105 1.00 61.43 ? 120 GLU A CA 1 ATOM 939 C C . GLU A 1 120 ? 4.274 -17.555 1.425 1.00 62.51 ? 120 GLU A C 1 ATOM 940 O O . GLU A 1 120 ? 4.563 -16.443 0.974 1.00 62.54 ? 120 GLU A O 1 ATOM 941 C CB . GLU A 1 120 ? 3.101 -17.621 3.614 1.00 60.85 ? 120 GLU A CB 1 ATOM 942 C CG . GLU A 1 120 ? 3.407 -16.181 3.983 1.00 61.35 ? 120 GLU A CG 1 ATOM 943 C CD . GLU A 1 120 ? 3.504 -15.935 5.469 1.00 63.88 ? 120 GLU A CD 1 ATOM 944 O OE1 . GLU A 1 120 ? 3.951 -16.854 6.200 1.00 62.79 ? 120 GLU A OE1 1 ATOM 945 O OE2 . GLU A 1 120 ? 3.148 -14.807 5.897 1.00 67.63 ? 120 GLU A OE2 1 ATOM 946 N N . VAL A 1 121 ? 5.087 -18.601 1.348 1.00 63.49 ? 121 VAL A N 1 ATOM 947 C CA . VAL A 1 121 ? 6.392 -18.479 0.710 1.00 62.75 ? 121 VAL A CA 1 ATOM 948 C C . VAL A 1 121 ? 6.229 -18.221 -0.770 1.00 63.89 ? 121 VAL A C 1 ATOM 949 O O . VAL A 1 121 ? 6.951 -17.401 -1.338 1.00 66.06 ? 121 VAL A O 1 ATOM 950 C CB . VAL A 1 121 ? 7.257 -19.716 0.927 1.00 60.64 ? 121 VAL A CB 1 ATOM 951 C CG1 . VAL A 1 121 ? 8.523 -19.612 0.117 1.00 59.67 ? 121 VAL A CG1 1 ATOM 952 C CG2 . VAL A 1 121 ? 7.594 -19.867 2.410 1.00 60.98 ? 121 VAL A CG2 1 ATOM 953 N N . ALA A 1 122 ? 5.264 -18.897 -1.385 1.00 65.46 ? 122 ALA A N 1 ATOM 954 C CA . ALA A 1 122 ? 4.968 -18.692 -2.806 1.00 65.90 ? 122 ALA A CA 1 ATOM 955 C C . ALA A 1 122 ? 4.666 -17.226 -3.066 1.00 66.45 ? 122 ALA A C 1 ATOM 956 O O . ALA A 1 122 ? 5.296 -16.576 -3.900 1.00 64.39 ? 122 ALA A O 1 ATOM 957 C CB . ALA A 1 122 ? 3.800 -19.556 -3.238 1.00 64.97 ? 122 ALA A CB 1 ATOM 958 N N . GLN A 1 123 ? 3.720 -16.703 -2.302 1.00 68.02 ? 123 GLN A N 1 ATOM 959 C CA . GLN A 1 123 ? 3.321 -15.302 -2.401 1.00 67.56 ? 123 GLN A CA 1 ATOM 960 C C . GLN A 1 123 ? 4.484 -14.349 -2.147 1.00 66.03 ? 123 GLN A C 1 ATOM 961 O O . GLN A 1 123 ? 4.605 -13.319 -2.793 1.00 67.56 ? 123 GLN A O 1 ATOM 962 C CB . GLN A 1 123 ? 2.213 -15.031 -1.388 1.00 69.01 ? 123 GLN A CB 1 ATOM 963 C CG . GLN A 1 123 ? 1.637 -13.632 -1.460 1.00 71.96 ? 123 GLN A CG 1 ATOM 964 C CD . GLN A 1 123 ? 0.989 -13.347 -2.795 1.00 70.98 ? 123 GLN A CD 1 ATOM 965 O OE1 . GLN A 1 123 ? 0.348 -14.216 -3.378 1.00 67.46 ? 123 GLN A OE1 1 ATOM 966 N NE2 . GLN A 1 123 ? 1.170 -12.129 -3.293 1.00 72.30 ? 123 GLN A NE2 1 ATOM 967 N N . SER A 1 124 ? 5.325 -14.694 -1.182 1.00 65.90 ? 124 SER A N 1 ATOM 968 C CA . SER A 1 124 ? 6.464 -13.870 -0.809 1.00 65.92 ? 124 SER A CA 1 ATOM 969 C C . SER A 1 124 ? 7.458 -13.762 -1.962 1.00 67.15 ? 124 SER A C 1 ATOM 970 O O . SER A 1 124 ? 7.914 -12.669 -2.300 1.00 65.85 ? 124 SER A O 1 ATOM 971 C CB . SER A 1 124 ? 7.149 -14.474 0.413 1.00 65.35 ? 124 SER A CB 1 ATOM 972 O OG . SER A 1 124 ? 8.137 -13.611 0.913 1.00 63.92 ? 124 SER A OG 1 ATOM 973 N N . ASN A 1 125 ? 7.788 -14.909 -2.562 1.00 66.78 ? 125 ASN A N 1 ATOM 974 C CA . ASN A 1 125 ? 8.665 -14.951 -3.738 1.00 65.58 ? 125 ASN A CA 1 ATOM 975 C C . ASN A 1 125 ? 8.075 -14.196 -4.936 1.00 64.04 ? 125 ASN A C 1 ATOM 976 O O . ASN A 1 125 ? 8.778 -13.468 -5.635 1.00 57.02 ? 125 ASN A O 1 ATOM 977 C CB . ASN A 1 125 ? 8.891 -16.384 -4.184 1.00 66.42 ? 125 ASN A CB 1 ATOM 978 C CG . ASN A 1 125 ? 9.751 -17.171 -3.237 1.00 66.38 ? 125 ASN A CG 1 ATOM 979 O OD1 . ASN A 1 125 ? 9.463 -18.337 -2.955 1.00 70.33 ? 125 ASN A OD1 1 ATOM 980 N ND2 . ASN A 1 125 ? 10.831 -16.565 -2.771 1.00 64.57 ? 125 ASN A ND2 1 ATOM 981 N N . PHE A 1 126 ? 6.779 -14.389 -5.154 1.00 63.79 ? 126 PHE A N 1 ATOM 982 C CA . PHE A 1 126 ? 6.082 -13.703 -6.209 1.00 66.71 ? 126 PHE A CA 1 ATOM 983 C C . PHE A 1 126 ? 6.196 -12.202 -6.073 1.00 66.38 ? 126 PHE A C 1 ATOM 984 O O . PHE A 1 126 ? 6.533 -11.517 -7.035 1.00 67.75 ? 126 PHE A O 1 ATOM 985 C CB . PHE A 1 126 ? 4.622 -14.091 -6.247 1.00 69.19 ? 126 PHE A CB 1 ATOM 986 C CG . PHE A 1 126 ? 3.846 -13.301 -7.240 1.00 75.47 ? 126 PHE A CG 1 ATOM 987 C CD1 . PHE A 1 126 ? 4.174 -13.365 -8.587 1.00 75.32 ? 126 PHE A CD1 1 ATOM 988 C CD2 . PHE A 1 126 ? 2.832 -12.447 -6.831 1.00 78.94 ? 126 PHE A CD2 1 ATOM 989 C CE1 . PHE A 1 126 ? 3.480 -12.624 -9.517 1.00 75.67 ? 126 PHE A CE1 1 ATOM 990 C CE2 . PHE A 1 126 ? 2.141 -11.696 -7.756 1.00 80.50 ? 126 PHE A CE2 1 ATOM 991 C CZ . PHE A 1 126 ? 2.467 -11.790 -9.105 1.00 78.26 ? 126 PHE A CZ 1 ATOM 992 N N . GLU A 1 127 ? 5.959 -11.699 -4.867 1.00 68.36 ? 127 GLU A N 1 ATOM 993 C CA . GLU A 1 127 ? 6.045 -10.256 -4.595 1.00 68.66 ? 127 GLU A CA 1 ATOM 994 C C . GLU A 1 127 ? 7.481 -9.745 -4.681 1.00 70.82 ? 127 GLU A C 1 ATOM 995 O O . GLU A 1 127 ? 7.717 -8.641 -5.151 1.00 73.16 ? 127 GLU A O 1 ATOM 996 C CB . GLU A 1 127 ? 5.445 -9.915 -3.229 1.00 66.82 ? 127 GLU A CB 1 ATOM 997 C CG . GLU A 1 127 ? 3.921 -10.063 -3.156 1.00 67.14 ? 127 GLU A CG 1 ATOM 998 C CD . GLU A 1 127 ? 3.307 -9.353 -1.961 1.00 65.98 ? 127 GLU A CD 1 ATOM 999 O OE1 . GLU A 1 127 ? 3.792 -8.254 -1.639 1.00 63.43 ? 127 GLU A OE1 1 ATOM 1000 O OE2 . GLU A 1 127 ? 2.336 -9.880 -1.348 1.00 65.20 ? 127 GLU A OE2 1 ATOM 1001 N N . ALA A 1 128 ? 8.443 -10.561 -4.253 1.00 71.51 ? 128 ALA A N 1 ATOM 1002 C CA . ALA A 1 128 ? 9.865 -10.243 -4.419 1.00 70.13 ? 128 ALA A CA 1 ATOM 1003 C C . ALA A 1 128 ? 10.289 -10.178 -5.890 1.00 73.06 ? 128 ALA A C 1 ATOM 1004 O O . ALA A 1 128 ? 11.101 -9.343 -6.286 1.00 73.16 ? 128 ALA A O 1 ATOM 1005 C CB . ALA A 1 128 ? 10.696 -11.273 -3.700 1.00 68.51 ? 128 ALA A CB 1 ATOM 1006 N N . LEU A 1 129 ? 9.751 -11.086 -6.692 1.00 73.02 ? 129 LEU A N 1 ATOM 1007 C CA . LEU A 1 129 ? 10.005 -11.087 -8.117 1.00 72.29 ? 129 LEU A CA 1 ATOM 1008 C C . LEU A 1 129 ? 9.400 -9.811 -8.713 1.00 75.32 ? 129 LEU A C 1 ATOM 1009 O O . LEU A 1 129 ? 10.033 -9.155 -9.537 1.00 73.81 ? 129 LEU A O 1 ATOM 1010 C CB . LEU A 1 129 ? 9.410 -12.348 -8.739 1.00 72.28 ? 129 LEU A CB 1 ATOM 1011 C CG . LEU A 1 129 ? 10.084 -13.008 -9.940 1.00 72.43 ? 129 LEU A CG 1 ATOM 1012 C CD1 . LEU A 1 129 ? 11.526 -13.388 -9.680 1.00 73.43 ? 129 LEU A CD1 1 ATOM 1013 C CD2 . LEU A 1 129 ? 9.301 -14.250 -10.303 1.00 71.60 ? 129 LEU A CD2 1 ATOM 1014 N N . GLN A 1 130 ? 8.192 -9.445 -8.278 1.00 76.67 ? 130 GLN A N 1 ATOM 1015 C CA . GLN A 1 130 ? 7.606 -8.146 -8.636 1.00 79.22 ? 130 GLN A CA 1 ATOM 1016 C C . GLN A 1 130 ? 8.542 -6.992 -8.275 1.00 79.38 ? 130 GLN A C 1 ATOM 1017 O O . GLN A 1 130 ? 8.901 -6.190 -9.121 1.00 86.10 ? 130 GLN A O 1 ATOM 1018 C CB . GLN A 1 130 ? 6.243 -7.942 -7.960 1.00 81.59 ? 130 GLN A CB 1 ATOM 1019 C CG . GLN A 1 130 ? 5.130 -8.772 -8.574 1.00 83.94 ? 130 GLN A CG 1 ATOM 1020 C CD . GLN A 1 130 ? 3.741 -8.289 -8.205 1.00 85.41 ? 130 GLN A CD 1 ATOM 1021 O OE1 . GLN A 1 130 ? 3.462 -7.979 -7.054 1.00 84.74 ? 130 GLN A OE1 1 ATOM 1022 N NE2 . GLN A 1 130 ? 2.855 -8.248 -9.190 1.00 91.04 ? 130 GLN A NE2 1 ATOM 1023 N N . ASP A 1 131 ? 8.967 -6.937 -7.023 1.00 79.89 ? 131 ASP A N 1 ATOM 1024 C CA . ASP A 1 131 ? 9.887 -5.892 -6.572 1.00 79.71 ? 131 ASP A CA 1 ATOM 1025 C C . ASP A 1 131 ? 11.186 -5.888 -7.365 1.00 76.27 ? 131 ASP A C 1 ATOM 1026 O O . ASP A 1 131 ? 11.823 -4.855 -7.502 1.00 78.50 ? 131 ASP A O 1 ATOM 1027 C CB . ASP A 1 131 ? 10.214 -6.044 -5.069 1.00 79.59 ? 131 ASP A CB 1 ATOM 1028 C CG . ASP A 1 131 ? 10.834 -4.780 -4.467 1.00 80.75 ? 131 ASP A CG 1 ATOM 1029 O OD1 . ASP A 1 131 ? 10.295 -3.680 -4.710 1.00 82.62 ? 131 ASP A OD1 1 ATOM 1030 O OD2 . ASP A 1 131 ? 11.847 -4.885 -3.737 1.00 80.82 ? 131 ASP A OD2 1 ATOM 1031 N N . PHE A 1 132 ? 11.587 -7.045 -7.871 1.00 74.63 ? 132 PHE A N 1 ATOM 1032 C CA . PHE A 1 132 ? 12.805 -7.133 -8.670 1.00 73.19 ? 132 PHE A CA 1 ATOM 1033 C C . PHE A 1 132 ? 12.710 -6.297 -9.920 1.00 70.61 ? 132 PHE A C 1 ATOM 1034 O O . PHE A 1 132 ? 13.607 -5.523 -10.229 1.00 69.46 ? 132 PHE A O 1 ATOM 1035 C CB . PHE A 1 132 ? 13.076 -8.558 -9.086 1.00 71.50 ? 132 PHE A CB 1 ATOM 1036 C CG . PHE A 1 132 ? 14.243 -8.695 -10.002 1.00 72.44 ? 132 PHE A CG 1 ATOM 1037 C CD1 . PHE A 1 132 ? 15.542 -8.550 -9.523 1.00 71.80 ? 132 PHE A CD1 1 ATOM 1038 C CD2 . PHE A 1 132 ? 14.057 -8.994 -11.342 1.00 74.87 ? 132 PHE A CD2 1 ATOM 1039 C CE1 . PHE A 1 132 ? 16.626 -8.702 -10.370 1.00 73.11 ? 132 PHE A CE1 1 ATOM 1040 C CE2 . PHE A 1 132 ? 15.135 -9.152 -12.194 1.00 73.00 ? 132 PHE A CE2 1 ATOM 1041 C CZ . PHE A 1 132 ? 16.421 -9.001 -11.712 1.00 73.95 ? 132 PHE A CZ 1 ATOM 1042 N N . PHE A 1 133 ? 11.602 -6.456 -10.625 1.00 71.39 ? 133 PHE A N 1 ATOM 1043 C CA . PHE A 1 133 ? 11.414 -5.777 -11.897 1.00 71.55 ? 133 PHE A CA 1 ATOM 1044 C C . PHE A 1 133 ? 11.176 -4.286 -11.756 1.00 71.03 ? 133 PHE A C 1 ATOM 1045 O O . PHE A 1 133 ? 11.395 -3.547 -12.728 1.00 69.11 ? 133 PHE A O 1 ATOM 1046 C CB . PHE A 1 133 ? 10.309 -6.443 -12.705 1.00 69.78 ? 133 PHE A CB 1 ATOM 1047 C CG . PHE A 1 133 ? 10.659 -7.816 -13.152 1.00 67.59 ? 133 PHE A CG 1 ATOM 1048 C CD1 . PHE A 1 133 ? 11.795 -8.034 -13.902 1.00 69.40 ? 133 PHE A CD1 1 ATOM 1049 C CD2 . PHE A 1 133 ? 9.861 -8.903 -12.820 1.00 67.90 ? 133 PHE A CD2 1 ATOM 1050 C CE1 . PHE A 1 133 ? 12.134 -9.319 -14.310 1.00 69.33 ? 133 PHE A CE1 1 ATOM 1051 C CE2 . PHE A 1 133 ? 10.183 -10.190 -13.236 1.00 65.36 ? 133 PHE A CE2 1 ATOM 1052 C CZ . PHE A 1 133 ? 11.318 -10.396 -13.982 1.00 66.23 ? 133 PHE A CZ 1 ATOM 1053 N N . ARG A 1 134 ? 10.741 -3.844 -10.574 1.00 70.10 ? 134 ARG A N 1 ATOM 1054 C CA . ARG A 1 134 ? 10.664 -2.404 -10.290 1.00 75.54 ? 134 ARG A CA 1 ATOM 1055 C C . ARG A 1 134 ? 12.057 -1.833 -10.228 1.00 73.37 ? 134 ARG A C 1 ATOM 1056 O O . ARG A 1 134 ? 12.295 -0.721 -10.704 1.00 74.16 ? 134 ARG A O 1 ATOM 1057 C CB . ARG A 1 134 ? 9.965 -2.110 -8.964 1.00 80.56 ? 134 ARG A CB 1 ATOM 1058 C CG . ARG A 1 134 ? 8.505 -2.520 -8.893 1.00 86.10 ? 134 ARG A CG 1 ATOM 1059 C CD . ARG A 1 134 ? 7.866 -1.984 -7.618 1.00 90.94 ? 134 ARG A CD 1 ATOM 1060 N NE . ARG A 1 134 ? 6.765 -2.826 -7.126 1.00 93.58 ? 134 ARG A NE 1 ATOM 1061 C CZ . ARG A 1 134 ? 6.695 -3.386 -5.916 1.00 95.00 ? 134 ARG A CZ 1 ATOM 1062 N NH1 . ARG A 1 134 ? 7.655 -3.223 -4.996 1.00 94.98 ? 134 ARG A NH1 1 ATOM 1063 N NH2 . ARG A 1 134 ? 5.638 -4.119 -5.612 1.00 97.57 ? 134 ARG A NH2 1 ATOM 1064 N N . LEU A 1 135 ? 12.965 -2.610 -9.642 1.00 70.70 ? 135 LEU A N 1 ATOM 1065 C CA . LEU A 1 135 ? 14.359 -2.217 -9.469 1.00 70.25 ? 135 LEU A CA 1 ATOM 1066 C C . LEU A 1 135 ? 15.161 -2.480 -10.721 1.00 73.75 ? 135 LEU A C 1 ATOM 1067 O O . LEU A 1 135 ? 16.078 -1.722 -11.043 1.00 81.17 ? 135 LEU A O 1 ATOM 1068 C CB . LEU A 1 135 ? 14.987 -2.965 -8.298 1.00 67.94 ? 135 LEU A CB 1 ATOM 1069 C CG . LEU A 1 135 ? 14.350 -2.677 -6.928 1.00 67.74 ? 135 LEU A CG 1 ATOM 1070 C CD1 . LEU A 1 135 ? 14.619 -3.787 -5.930 1.00 66.72 ? 135 LEU A CD1 1 ATOM 1071 C CD2 . LEU A 1 135 ? 14.819 -1.348 -6.376 1.00 67.81 ? 135 LEU A CD2 1 ATOM 1072 N N . PHE A 1 136 ? 14.804 -3.532 -11.447 1.00 72.12 ? 136 PHE A N 1 ATOM 1073 C CA . PHE A 1 136 ? 15.474 -3.877 -12.699 1.00 71.42 ? 136 PHE A CA 1 ATOM 1074 C C . PHE A 1 136 ? 14.502 -3.866 -13.869 1.00 69.45 ? 136 PHE A C 1 ATOM 1075 O O . PHE A 1 136 ? 14.250 -4.895 -14.464 1.00 68.69 ? 136 PHE A O 1 ATOM 1076 C CB . PHE A 1 136 ? 16.084 -5.271 -12.569 1.00 69.95 ? 136 PHE A CB 1 ATOM 1077 C CG . PHE A 1 136 ? 17.333 -5.319 -11.738 1.00 68.27 ? 136 PHE A CG 1 ATOM 1078 C CD1 . PHE A 1 136 ? 17.270 -5.472 -10.374 1.00 67.57 ? 136 PHE A CD1 1 ATOM 1079 C CD2 . PHE A 1 136 ? 18.583 -5.228 -12.338 1.00 70.11 ? 136 PHE A CD2 1 ATOM 1080 C CE1 . PHE A 1 136 ? 18.427 -5.528 -9.605 1.00 68.90 ? 136 PHE A CE1 1 ATOM 1081 C CE2 . PHE A 1 136 ? 19.742 -5.285 -11.584 1.00 69.08 ? 136 PHE A CE2 1 ATOM 1082 C CZ . PHE A 1 136 ? 19.665 -5.436 -10.212 1.00 67.20 ? 136 PHE A CZ 1 ATOM 1083 N N . PRO A 1 137 ? 13.945 -2.698 -14.205 1.00 72.66 ? 137 PRO A N 1 ATOM 1084 C CA . PRO A 1 137 ? 12.933 -2.642 -15.287 1.00 75.88 ? 137 PRO A CA 1 ATOM 1085 C C . PRO A 1 137 ? 13.431 -3.066 -16.675 1.00 77.28 ? 137 PRO A C 1 ATOM 1086 O O . PRO A 1 137 ? 12.656 -3.609 -17.469 1.00 74.96 ? 137 PRO A O 1 ATOM 1087 C CB . PRO A 1 137 ? 12.487 -1.173 -15.292 1.00 74.33 ? 137 PRO A CB 1 ATOM 1088 C CG . PRO A 1 137 ? 13.549 -0.427 -14.572 1.00 73.38 ? 137 PRO A CG 1 ATOM 1089 C CD . PRO A 1 137 ? 14.169 -1.380 -13.593 1.00 72.03 ? 137 PRO A CD 1 ATOM 1090 N N . GLU A 1 138 ? 14.716 -2.833 -16.934 1.00 80.37 ? 138 GLU A N 1 ATOM 1091 C CA . GLU A 1 138 ? 15.359 -3.179 -18.211 1.00 83.12 ? 138 GLU A CA 1 ATOM 1092 C C . GLU A 1 138 ? 15.434 -4.683 -18.467 1.00 82.54 ? 138 GLU A C 1 ATOM 1093 O O . GLU A 1 138 ? 15.792 -5.102 -19.568 1.00 86.87 ? 138 GLU A O 1 ATOM 1094 C CB . GLU A 1 138 ? 16.764 -2.551 -18.305 1.00 85.49 ? 138 GLU A CB 1 ATOM 1095 C CG . GLU A 1 138 ? 17.801 -3.057 -17.295 1.00 86.59 ? 138 GLU A CG 1 ATOM 1096 C CD . GLU A 1 138 ? 17.736 -2.369 -15.929 1.00 86.82 ? 138 GLU A CD 1 ATOM 1097 O OE1 . GLU A 1 138 ? 16.629 -2.194 -15.382 1.00 87.43 ? 138 GLU A OE1 1 ATOM 1098 O OE2 . GLU A 1 138 ? 18.799 -2.003 -15.393 1.00 82.71 ? 138 GLU A OE2 1 ATOM 1099 N N . TYR A 1 139 ? 15.086 -5.483 -17.459 1.00 83.60 ? 139 TYR A N 1 ATOM 1100 C CA . TYR A 1 139 ? 15.030 -6.944 -17.584 1.00 84.85 ? 139 TYR A CA 1 ATOM 1101 C C . TYR A 1 139 ? 13.607 -7.511 -17.641 1.00 87.92 ? 139 TYR A C 1 ATOM 1102 O O . TYR A 1 139 ? 13.422 -8.731 -17.672 1.00 88.68 ? 139 TYR A O 1 ATOM 1103 C CB . TYR A 1 139 ? 15.814 -7.606 -16.448 1.00 81.52 ? 139 TYR A CB 1 ATOM 1104 C CG . TYR A 1 139 ? 17.299 -7.434 -16.591 1.00 83.81 ? 139 TYR A CG 1 ATOM 1105 C CD1 . TYR A 1 139 ? 17.961 -7.905 -17.720 1.00 88.95 ? 139 TYR A CD1 1 ATOM 1106 C CD2 . TYR A 1 139 ? 18.043 -6.788 -15.627 1.00 80.26 ? 139 TYR A CD2 1 ATOM 1107 C CE1 . TYR A 1 139 ? 19.320 -7.739 -17.879 1.00 88.76 ? 139 TYR A CE1 1 ATOM 1108 C CE2 . TYR A 1 139 ? 19.400 -6.618 -15.776 1.00 81.77 ? 139 TYR A CE2 1 ATOM 1109 C CZ . TYR A 1 139 ? 20.034 -7.095 -16.902 1.00 84.58 ? 139 TYR A CZ 1 ATOM 1110 O OH . TYR A 1 139 ? 21.381 -6.925 -17.061 1.00 83.85 ? 139 TYR A OH 1 ATOM 1111 N N . LYS A 1 140 ? 12.609 -6.635 -17.686 1.00 91.92 ? 140 LYS A N 1 ATOM 1112 C CA . LYS A 1 140 ? 11.217 -7.068 -17.830 1.00 91.55 ? 140 LYS A CA 1 ATOM 1113 C C . LYS A 1 140 ? 10.939 -7.779 -19.151 1.00 88.32 ? 140 LYS A C 1 ATOM 1114 O O . LYS A 1 140 ? 10.021 -8.577 -19.231 1.00 89.77 ? 140 LYS A O 1 ATOM 1115 C CB . LYS A 1 140 ? 10.264 -5.880 -17.714 1.00 95.45 ? 140 LYS A CB 1 ATOM 1116 C CG . LYS A 1 140 ? 10.065 -5.357 -16.310 1.00 100.14 ? 140 LYS A CG 1 ATOM 1117 C CD . LYS A 1 140 ? 9.001 -4.269 -16.292 1.00 103.17 ? 140 LYS A CD 1 ATOM 1118 C CE . LYS A 1 140 ? 8.629 -3.868 -14.873 1.00 104.99 ? 140 LYS A CE 1 ATOM 1119 N NZ . LYS A 1 140 ? 7.493 -2.913 -14.856 1.00 108.11 ? 140 LYS A NZ 1 ATOM 1120 N N . ASN A 1 141 ? 11.703 -7.475 -20.192 1.00 90.55 ? 141 ASN A N 1 ATOM 1121 C CA . ASN A 1 141 ? 11.469 -8.076 -21.513 1.00 95.96 ? 141 ASN A CA 1 ATOM 1122 C C . ASN A 1 141 ? 12.068 -9.454 -21.645 1.00 92.40 ? 141 ASN A C 1 ATOM 1123 O O . ASN A 1 141 ? 11.572 -10.278 -22.420 1.00 94.64 ? 141 ASN A O 1 ATOM 1124 C CB . ASN A 1 141 ? 12.037 -7.186 -22.623 1.00 100.57 ? 141 ASN A CB 1 ATOM 1125 C CG . ASN A 1 141 ? 11.328 -5.858 -22.713 1.00 107.64 ? 141 ASN A CG 1 ATOM 1126 O OD1 . ASN A 1 141 ? 11.961 -4.812 -22.897 1.00 112.36 ? 141 ASN A OD1 1 ATOM 1127 N ND2 . ASN A 1 141 ? 10.000 -5.882 -22.564 1.00 108.86 ? 141 ASN A ND2 1 ATOM 1128 N N . ASN A 1 142 ? 13.140 -9.688 -20.892 1.00 82.97 ? 142 ASN A N 1 ATOM 1129 C CA . ASN A 1 142 ? 13.945 -10.880 -21.052 1.00 79.25 ? 142 ASN A CA 1 ATOM 1130 C C . ASN A 1 142 ? 13.137 -12.130 -20.809 1.00 79.24 ? 142 ASN A C 1 ATOM 1131 O O . ASN A 1 142 ? 12.176 -12.110 -20.056 1.00 83.44 ? 142 ASN A O 1 ATOM 1132 C CB . ASN A 1 142 ? 15.136 -10.840 -20.112 1.00 75.06 ? 142 ASN A CB 1 ATOM 1133 C CG . ASN A 1 142 ? 16.035 -9.640 -20.355 1.00 76.67 ? 142 ASN A CG 1 ATOM 1134 O OD1 . ASN A 1 142 ? 15.566 -8.508 -20.459 1.00 76.07 ? 142 ASN A OD1 1 ATOM 1135 N ND2 . ASN A 1 142 ? 17.338 -9.880 -20.433 1.00 76.50 ? 142 ASN A ND2 1 ATOM 1136 N N . LYS A 1 143 ? 13.510 -13.213 -21.473 1.00 80.44 ? 143 LYS A N 1 ATOM 1137 C CA . LYS A 1 143 ? 12.874 -14.480 -21.220 1.00 80.50 ? 143 LYS A CA 1 ATOM 1138 C C . LYS A 1 143 ? 13.122 -14.803 -19.751 1.00 76.20 ? 143 LYS A C 1 ATOM 1139 O O . LYS A 1 143 ? 14.225 -14.624 -19.265 1.00 74.50 ? 143 LYS A O 1 ATOM 1140 C CB . LYS A 1 143 ? 13.445 -15.575 -22.120 1.00 82.88 ? 143 LYS A CB 1 ATOM 1141 C CG . LYS A 1 143 ? 13.259 -15.354 -23.610 1.00 84.92 ? 143 LYS A CG 1 ATOM 1142 C CD . LYS A 1 143 ? 13.619 -16.610 -24.380 1.00 89.39 ? 143 LYS A CD 1 ATOM 1143 C CE . LYS A 1 143 ? 14.110 -16.296 -25.783 1.00 95.79 ? 143 LYS A CE 1 ATOM 1144 N NZ . LYS A 1 143 ? 14.303 -17.525 -26.608 1.00 99.90 ? 143 LYS A NZ 1 ATOM 1145 N N . LEU A 1 144 ? 12.091 -15.273 -19.051 1.00 76.79 ? 144 LEU A N 1 ATOM 1146 C CA . LEU A 1 144 ? 12.170 -15.524 -17.604 1.00 71.67 ? 144 LEU A CA 1 ATOM 1147 C C . LEU A 1 144 ? 11.956 -16.989 -17.275 1.00 67.30 ? 144 LEU A C 1 ATOM 1148 O O . LEU A 1 144 ? 10.889 -17.540 -17.516 1.00 64.14 ? 144 LEU A O 1 ATOM 1149 C CB . LEU A 1 144 ? 11.135 -14.690 -16.861 1.00 69.80 ? 144 LEU A CB 1 ATOM 1150 C CG . LEU A 1 144 ? 10.948 -15.008 -15.381 1.00 68.66 ? 144 LEU A CG 1 ATOM 1151 C CD1 . LEU A 1 144 ? 12.204 -14.701 -14.603 1.00 68.94 ? 144 LEU A CD1 1 ATOM 1152 C CD2 . LEU A 1 144 ? 9.789 -14.231 -14.800 1.00 69.97 ? 144 LEU A CD2 1 ATOM 1153 N N . PHE A 1 145 ? 12.975 -17.601 -16.691 1.00 66.72 ? 145 PHE A N 1 ATOM 1154 C CA . PHE A 1 145 ? 12.891 -18.970 -16.217 1.00 67.09 ? 145 PHE A CA 1 ATOM 1155 C C . PHE A 1 145 ? 12.971 -19.060 -14.689 1.00 64.27 ? 145 PHE A C 1 ATOM 1156 O O . PHE A 1 145 ? 13.728 -18.347 -14.035 1.00 59.73 ? 145 PHE A O 1 ATOM 1157 C CB . PHE A 1 145 ? 13.998 -19.817 -16.846 1.00 67.99 ? 145 PHE A CB 1 ATOM 1158 C CG . PHE A 1 145 ? 13.914 -19.894 -18.331 1.00 67.94 ? 145 PHE A CG 1 ATOM 1159 C CD1 . PHE A 1 145 ? 14.377 -18.864 -19.131 1.00 68.66 ? 145 PHE A CD1 1 ATOM 1160 C CD2 . PHE A 1 145 ? 13.317 -20.987 -18.933 1.00 70.03 ? 145 PHE A CD2 1 ATOM 1161 C CE1 . PHE A 1 145 ? 14.253 -18.943 -20.518 1.00 70.66 ? 145 PHE A CE1 1 ATOM 1162 C CE2 . PHE A 1 145 ? 13.192 -21.068 -20.313 1.00 69.54 ? 145 PHE A CE2 1 ATOM 1163 C CZ . PHE A 1 145 ? 13.659 -20.050 -21.104 1.00 67.90 ? 145 PHE A CZ 1 ATOM 1164 N N . LEU A 1 146 ? 12.186 -19.979 -14.146 1.00 64.49 ? 146 LEU A N 1 ATOM 1165 C CA . LEU A 1 146 ? 12.147 -20.254 -12.728 1.00 61.18 ? 146 LEU A CA 1 ATOM 1166 C C . LEU A 1 146 ? 12.827 -21.594 -12.523 1.00 63.16 ? 146 LEU A C 1 ATOM 1167 O O . LEU A 1 146 ? 12.366 -22.597 -13.060 1.00 62.95 ? 146 LEU A O 1 ATOM 1168 C CB . LEU A 1 146 ? 10.690 -20.338 -12.254 1.00 60.01 ? 146 LEU A CB 1 ATOM 1169 C CG . LEU A 1 146 ? 9.746 -19.196 -12.634 1.00 59.22 ? 146 LEU A CG 1 ATOM 1170 C CD1 . LEU A 1 146 ? 8.342 -19.477 -12.150 1.00 59.43 ? 146 LEU A CD1 1 ATOM 1171 C CD2 . LEU A 1 146 ? 10.233 -17.876 -12.059 1.00 57.65 ? 146 LEU A CD2 1 ATOM 1172 N N . THR A 1 147 ? 13.910 -21.619 -11.749 1.00 64.19 ? 147 THR A N 1 ATOM 1173 C CA . THR A 1 147 ? 14.645 -22.859 -11.508 1.00 64.41 ? 147 THR A CA 1 ATOM 1174 C C . THR A 1 147 ? 14.914 -23.015 -10.052 1.00 63.96 ? 147 THR A C 1 ATOM 1175 O O . THR A 1 147 ? 15.068 -22.036 -9.350 1.00 63.60 ? 147 THR A O 1 ATOM 1176 C CB . THR A 1 147 ? 16.008 -22.892 -12.219 1.00 67.82 ? 147 THR A CB 1 ATOM 1177 O OG1 . THR A 1 147 ? 16.885 -21.931 -11.618 1.00 70.41 ? 147 THR A OG1 1 ATOM 1178 C CG2 . THR A 1 147 ? 15.869 -22.614 -13.744 1.00 67.02 ? 147 THR A CG2 1 ATOM 1179 N N . GLY A 1 148 ? 15.008 -24.257 -9.605 1.00 69.12 ? 148 GLY A N 1 ATOM 1180 C CA . GLY A 1 148 ? 15.281 -24.547 -8.199 1.00 66.48 ? 148 GLY A CA 1 ATOM 1181 C C . GLY A 1 148 ? 15.791 -25.949 -7.987 1.00 63.43 ? 148 GLY A C 1 ATOM 1182 O O . GLY A 1 148 ? 15.968 -26.711 -8.934 1.00 62.19 ? 148 GLY A O 1 ATOM 1183 N N . GLU A 1 149 ? 16.003 -26.292 -6.727 1.00 63.39 ? 149 GLU A N 1 ATOM 1184 C CA . GLU A 1 149 ? 16.475 -27.618 -6.351 1.00 61.45 ? 149 GLU A CA 1 ATOM 1185 C C . GLU A 1 149 ? 15.785 -28.088 -5.078 1.00 60.67 ? 149 GLU A C 1 ATOM 1186 O O . GLU A 1 149 ? 15.248 -27.272 -4.332 1.00 60.47 ? 149 GLU A O 1 ATOM 1187 C CB . GLU A 1 149 ? 17.959 -27.540 -6.122 1.00 60.35 ? 149 GLU A CB 1 ATOM 1188 C CG . GLU A 1 149 ? 18.647 -28.856 -5.878 1.00 63.93 ? 149 GLU A CG 1 ATOM 1189 C CD . GLU A 1 149 ? 20.063 -28.645 -5.406 1.00 69.02 ? 149 GLU A CD 1 ATOM 1190 O OE1 . GLU A 1 149 ? 20.883 -28.175 -6.226 1.00 66.23 ? 149 GLU A OE1 1 ATOM 1191 O OE2 . GLU A 1 149 ? 20.335 -28.931 -4.214 1.00 71.96 ? 149 GLU A OE2 1 ATOM 1192 N N . SER A 1 150 ? 15.770 -29.398 -4.838 1.00 58.94 ? 150 SER A N 1 ATOM 1193 C CA . SER A 1 150 ? 15.396 -29.933 -3.517 1.00 58.89 ? 150 SER A CA 1 ATOM 1194 C C . SER A 1 150 ? 13.943 -29.548 -3.162 1.00 56.72 ? 150 SER A C 1 ATOM 1195 O O . SER A 1 150 ? 13.055 -29.696 -3.987 1.00 58.48 ? 150 SER A O 1 ATOM 1196 C CB . SER A 1 150 ? 16.415 -29.444 -2.459 1.00 58.63 ? 150 SER A CB 1 ATOM 1197 O OG . SER A 1 150 ? 16.238 -30.079 -1.202 1.00 57.69 ? 150 SER A OG 1 ATOM 1198 N N . TYR A 1 151 ? 13.693 -29.039 -1.963 1.00 53.10 ? 151 TYR A N 1 ATOM 1199 C CA . TYR A 1 151 ? 12.341 -28.611 -1.610 1.00 53.66 ? 151 TYR A CA 1 ATOM 1200 C C . TYR A 1 151 ? 11.751 -27.582 -2.584 1.00 52.90 ? 151 TYR A C 1 ATOM 1201 O O . TYR A 1 151 ? 10.550 -27.336 -2.555 1.00 53.05 ? 151 TYR A O 1 ATOM 1202 C CB . TYR A 1 151 ? 12.265 -28.066 -0.168 1.00 53.82 ? 151 TYR A CB 1 ATOM 1203 C CG . TYR A 1 151 ? 10.847 -27.977 0.306 1.00 53.04 ? 151 TYR A CG 1 ATOM 1204 C CD1 . TYR A 1 151 ? 10.189 -29.091 0.750 1.00 53.44 ? 151 TYR A CD1 1 ATOM 1205 C CD2 . TYR A 1 151 ? 10.152 -26.797 0.249 1.00 55.08 ? 151 TYR A CD2 1 ATOM 1206 C CE1 . TYR A 1 151 ? 8.877 -29.023 1.161 1.00 55.02 ? 151 TYR A CE1 1 ATOM 1207 C CE2 . TYR A 1 151 ? 8.840 -26.718 0.664 1.00 56.66 ? 151 TYR A CE2 1 ATOM 1208 C CZ . TYR A 1 151 ? 8.204 -27.839 1.119 1.00 56.15 ? 151 TYR A CZ 1 ATOM 1209 O OH . TYR A 1 151 ? 6.875 -27.785 1.512 1.00 60.86 ? 151 TYR A OH 1 ATOM 1210 N N . ALA A 1 152 ? 12.575 -26.974 -3.429 1.00 52.57 ? 152 ALA A N 1 ATOM 1211 C CA . ALA A 1 152 ? 12.068 -26.021 -4.423 1.00 54.01 ? 152 ALA A CA 1 ATOM 1212 C C . ALA A 1 152 ? 11.267 -26.730 -5.505 1.00 55.36 ? 152 ALA A C 1 ATOM 1213 O O . ALA A 1 152 ? 10.730 -26.096 -6.389 1.00 57.09 ? 152 ALA A O 1 ATOM 1214 C CB . ALA A 1 152 ? 13.204 -25.229 -5.049 1.00 55.52 ? 152 ALA A CB 1 ATOM 1215 N N . GLY A 1 153 ? 11.214 -28.054 -5.452 1.00 56.00 ? 153 GLY A N 1 ATOM 1216 C CA . GLY A 1 153 ? 10.222 -28.790 -6.212 1.00 58.21 ? 153 GLY A CA 1 ATOM 1217 C C . GLY A 1 153 ? 8.814 -28.398 -5.805 1.00 59.08 ? 153 GLY A C 1 ATOM 1218 O O . GLY A 1 153 ? 7.879 -28.638 -6.557 1.00 59.57 ? 153 GLY A O 1 ATOM 1219 N N . ILE A 1 154 ? 8.682 -27.834 -4.599 1.00 59.36 ? 154 ILE A N 1 ATOM 1220 C CA . ILE A 1 154 ? 7.450 -27.205 -4.123 1.00 59.10 ? 154 ILE A CA 1 ATOM 1221 C C . ILE A 1 154 ? 7.448 -25.695 -4.343 1.00 59.38 ? 154 ILE A C 1 ATOM 1222 O O . ILE A 1 154 ? 6.461 -25.124 -4.817 1.00 62.11 ? 154 ILE A O 1 ATOM 1223 C CB . ILE A 1 154 ? 7.232 -27.448 -2.626 1.00 57.36 ? 154 ILE A CB 1 ATOM 1224 C CG1 . ILE A 1 154 ? 7.264 -28.939 -2.306 1.00 58.15 ? 154 ILE A CG1 1 ATOM 1225 C CG2 . ILE A 1 154 ? 5.909 -26.849 -2.183 1.00 58.72 ? 154 ILE A CG2 1 ATOM 1226 C CD1 . ILE A 1 154 ? 6.217 -29.767 -3.019 1.00 58.46 ? 154 ILE A CD1 1 ATOM 1227 N N . TYR A 1 155 ? 8.540 -25.037 -3.993 1.00 57.52 ? 155 TYR A N 1 ATOM 1228 C CA . TYR A 1 155 ? 8.614 -23.591 -4.185 1.00 57.58 ? 155 TYR A CA 1 ATOM 1229 C C . TYR A 1 155 ? 8.268 -23.210 -5.620 1.00 56.75 ? 155 TYR A C 1 ATOM 1230 O O . TYR A 1 155 ? 7.478 -22.299 -5.851 1.00 56.58 ? 155 TYR A O 1 ATOM 1231 C CB . TYR A 1 155 ? 10.010 -23.031 -3.875 1.00 57.87 ? 155 TYR A CB 1 ATOM 1232 C CG . TYR A 1 155 ? 10.512 -23.127 -2.448 1.00 58.50 ? 155 TYR A CG 1 ATOM 1233 C CD1 . TYR A 1 155 ? 9.645 -23.130 -1.359 1.00 59.48 ? 155 TYR A CD1 1 ATOM 1234 C CD2 . TYR A 1 155 ? 11.877 -23.169 -2.192 1.00 60.46 ? 155 TYR A CD2 1 ATOM 1235 C CE1 . TYR A 1 155 ? 10.120 -23.203 -0.065 1.00 59.14 ? 155 TYR A CE1 1 ATOM 1236 C CE2 . TYR A 1 155 ? 12.358 -23.238 -0.901 1.00 60.20 ? 155 TYR A CE2 1 ATOM 1237 C CZ . TYR A 1 155 ? 11.474 -23.257 0.161 1.00 60.40 ? 155 TYR A CZ 1 ATOM 1238 O OH . TYR A 1 155 ? 11.968 -23.301 1.455 1.00 64.40 ? 155 TYR A OH 1 ATOM 1239 N N . ILE A 1 156 ? 8.872 -23.907 -6.579 1.00 58.90 ? 156 ILE A N 1 ATOM 1240 C CA . ILE A 1 156 ? 8.889 -23.457 -7.982 1.00 61.54 ? 156 ILE A CA 1 ATOM 1241 C C . ILE A 1 156 ? 7.542 -23.595 -8.715 1.00 61.74 ? 156 ILE A C 1 ATOM 1242 O O . ILE A 1 156 ? 7.087 -22.636 -9.327 1.00 60.92 ? 156 ILE A O 1 ATOM 1243 C CB . ILE A 1 156 ? 10.030 -24.129 -8.781 1.00 61.30 ? 156 ILE A CB 1 ATOM 1244 C CG1 . ILE A 1 156 ? 11.394 -23.592 -8.337 1.00 60.85 ? 156 ILE A CG1 1 ATOM 1245 C CG2 . ILE A 1 156 ? 9.849 -23.945 -10.282 1.00 64.51 ? 156 ILE A CG2 1 ATOM 1246 C CD1 . ILE A 1 156 ? 11.622 -22.119 -8.586 1.00 63.48 ? 156 ILE A CD1 1 ATOM 1247 N N . PRO A 1 157 ? 6.916 -24.779 -8.675 1.00 60.66 ? 157 PRO A N 1 ATOM 1248 C CA . PRO A 1 157 ? 5.636 -24.874 -9.347 1.00 63.00 ? 157 PRO A CA 1 ATOM 1249 C C . PRO A 1 157 ? 4.604 -23.970 -8.721 1.00 69.07 ? 157 PRO A C 1 ATOM 1250 O O . PRO A 1 157 ? 3.835 -23.357 -9.445 1.00 71.06 ? 157 PRO A O 1 ATOM 1251 C CB . PRO A 1 157 ? 5.244 -26.332 -9.159 1.00 62.64 ? 157 PRO A CB 1 ATOM 1252 C CG . PRO A 1 157 ? 6.532 -27.046 -8.992 1.00 62.05 ? 157 PRO A CG 1 ATOM 1253 C CD . PRO A 1 157 ? 7.360 -26.089 -8.180 1.00 62.86 ? 157 PRO A CD 1 ATOM 1254 N N . THR A 1 158 ? 4.599 -23.869 -7.388 1.00 70.51 ? 158 THR A N 1 ATOM 1255 C CA . THR A 1 158 ? 3.611 -23.039 -6.699 1.00 68.19 ? 158 THR A CA 1 ATOM 1256 C C . THR A 1 158 ? 3.825 -21.579 -7.069 1.00 69.90 ? 158 THR A C 1 ATOM 1257 O O . THR A 1 158 ? 2.857 -20.839 -7.321 1.00 70.43 ? 158 THR A O 1 ATOM 1258 C CB . THR A 1 158 ? 3.655 -23.215 -5.165 1.00 66.46 ? 158 THR A CB 1 ATOM 1259 O OG1 . THR A 1 158 ? 4.940 -22.871 -4.654 1.00 64.87 ? 158 THR A OG1 1 ATOM 1260 C CG2 . THR A 1 158 ? 3.340 -24.638 -4.777 1.00 67.10 ? 158 THR A CG2 1 ATOM 1261 N N . LEU A 1 159 ? 5.094 -21.174 -7.110 1.00 68.45 ? 159 LEU A N 1 ATOM 1262 C CA . LEU A 1 159 ? 5.473 -19.830 -7.560 1.00 67.18 ? 159 LEU A CA 1 ATOM 1263 C C . LEU A 1 159 ? 5.022 -19.611 -8.993 1.00 68.76 ? 159 LEU A C 1 ATOM 1264 O O . LEU A 1 159 ? 4.344 -18.638 -9.285 1.00 70.95 ? 159 LEU A O 1 ATOM 1265 C CB . LEU A 1 159 ? 6.983 -19.635 -7.491 1.00 64.06 ? 159 LEU A CB 1 ATOM 1266 C CG . LEU A 1 159 ? 7.497 -18.305 -8.053 1.00 63.89 ? 159 LEU A CG 1 ATOM 1267 C CD1 . LEU A 1 159 ? 6.762 -17.141 -7.419 1.00 64.67 ? 159 LEU A CD1 1 ATOM 1268 C CD2 . LEU A 1 159 ? 9.009 -18.149 -7.852 1.00 60.99 ? 159 LEU A CD2 1 ATOM 1269 N N . ALA A 1 160 ? 5.379 -20.549 -9.862 1.00 68.05 ? 160 ALA A N 1 ATOM 1270 C CA . ALA A 1 160 ? 5.101 -20.449 -11.288 1.00 70.65 ? 160 ALA A CA 1 ATOM 1271 C C . ALA A 1 160 ? 3.632 -20.172 -11.563 1.00 73.77 ? 160 ALA A C 1 ATOM 1272 O O . ALA A 1 160 ? 3.298 -19.338 -12.403 1.00 77.73 ? 160 ALA A O 1 ATOM 1273 C CB . ALA A 1 160 ? 5.530 -21.718 -12.003 1.00 71.53 ? 160 ALA A CB 1 ATOM 1274 N N . VAL A 1 161 ? 2.760 -20.866 -10.848 1.00 72.09 ? 161 VAL A N 1 ATOM 1275 C CA . VAL A 1 161 ? 1.340 -20.620 -10.955 1.00 70.18 ? 161 VAL A CA 1 ATOM 1276 C C . VAL A 1 161 ? 1.001 -19.146 -10.693 1.00 72.56 ? 161 VAL A C 1 ATOM 1277 O O . VAL A 1 161 ? 0.241 -18.547 -11.431 1.00 84.11 ? 161 VAL A O 1 ATOM 1278 C CB . VAL A 1 161 ? 0.562 -21.524 -10.007 1.00 67.62 ? 161 VAL A CB 1 ATOM 1279 C CG1 . VAL A 1 161 ? -0.861 -21.020 -9.851 1.00 72.05 ? 161 VAL A CG1 1 ATOM 1280 C CG2 . VAL A 1 161 ? 0.577 -22.951 -10.526 1.00 67.70 ? 161 VAL A CG2 1 ATOM 1281 N N . LEU A 1 162 ? 1.566 -18.553 -9.658 1.00 71.45 ? 162 LEU A N 1 ATOM 1282 C CA . LEU A 1 162 ? 1.334 -17.137 -9.401 1.00 69.02 ? 162 LEU A CA 1 ATOM 1283 C C . LEU A 1 162 ? 1.881 -16.291 -10.546 1.00 72.01 ? 162 LEU A C 1 ATOM 1284 O O . LEU A 1 162 ? 1.262 -15.292 -10.928 1.00 73.03 ? 162 LEU A O 1 ATOM 1285 C CB . LEU A 1 162 ? 1.975 -16.699 -8.071 1.00 65.87 ? 162 LEU A CB 1 ATOM 1286 C CG . LEU A 1 162 ? 1.440 -17.339 -6.792 1.00 63.93 ? 162 LEU A CG 1 ATOM 1287 C CD1 . LEU A 1 162 ? 2.217 -16.864 -5.575 1.00 61.07 ? 162 LEU A CD1 1 ATOM 1288 C CD2 . LEU A 1 162 ? -0.034 -17.052 -6.609 1.00 64.56 ? 162 LEU A CD2 1 ATOM 1289 N N . VAL A 1 163 ? 3.051 -16.671 -11.067 1.00 70.76 ? 163 VAL A N 1 ATOM 1290 C CA . VAL A 1 163 ? 3.706 -15.940 -12.155 1.00 69.37 ? 163 VAL A CA 1 ATOM 1291 C C . VAL A 1 163 ? 2.866 -16.066 -13.429 1.00 73.96 ? 163 VAL A C 1 ATOM 1292 O O . VAL A 1 163 ? 2.727 -15.116 -14.206 1.00 75.25 ? 163 VAL A O 1 ATOM 1293 C CB . VAL A 1 163 ? 5.122 -16.481 -12.417 1.00 65.33 ? 163 VAL A CB 1 ATOM 1294 C CG1 . VAL A 1 163 ? 5.741 -15.813 -13.631 1.00 66.17 ? 163 VAL A CG1 1 ATOM 1295 C CG2 . VAL A 1 163 ? 6.003 -16.276 -11.203 1.00 64.16 ? 163 VAL A CG2 1 ATOM 1296 N N . MET A 1 164 ? 2.300 -17.247 -13.619 1.00 78.54 ? 164 MET A N 1 ATOM 1297 C CA . MET A 1 164 ? 1.421 -17.533 -14.740 1.00 85.93 ? 164 MET A CA 1 ATOM 1298 C C . MET A 1 164 ? 0.253 -16.555 -14.800 1.00 91.94 ? 164 MET A C 1 ATOM 1299 O O . MET A 1 164 ? -0.212 -16.205 -15.875 1.00 94.07 ? 164 MET A O 1 ATOM 1300 C CB . MET A 1 164 ? 0.906 -18.965 -14.604 1.00 87.03 ? 164 MET A CB 1 ATOM 1301 C CG . MET A 1 164 ? 0.001 -19.426 -15.721 1.00 92.25 ? 164 MET A CG 1 ATOM 1302 S SD . MET A 1 164 ? -0.505 -21.126 -15.454 1.00 96.56 ? 164 MET A SD 1 ATOM 1303 C CE . MET A 1 164 ? -1.316 -20.957 -13.867 1.00 96.13 ? 164 MET A CE 1 ATOM 1304 N N . GLN A 1 165 ? -0.216 -16.123 -13.631 1.00 97.45 ? 165 GLN A N 1 ATOM 1305 C CA . GLN A 1 165 ? -1.294 -15.142 -13.531 1.00 96.46 ? 165 GLN A CA 1 ATOM 1306 C C . GLN A 1 165 ? -0.892 -13.717 -13.916 1.00 91.54 ? 165 GLN A C 1 ATOM 1307 O O . GLN A 1 165 ? -1.761 -12.914 -14.205 1.00 101.18 ? 165 GLN A O 1 ATOM 1308 C CB . GLN A 1 165 ? -1.874 -15.132 -12.113 1.00 97.87 ? 165 GLN A CB 1 ATOM 1309 C CG . GLN A 1 165 ? -2.557 -16.426 -11.704 1.00 104.14 ? 165 GLN A CG 1 ATOM 1310 C CD . GLN A 1 165 ? -2.826 -16.516 -10.208 1.00 110.86 ? 165 GLN A CD 1 ATOM 1311 O OE1 . GLN A 1 165 ? -2.698 -15.532 -9.479 1.00 111.62 ? 165 GLN A OE1 1 ATOM 1312 N NE2 . GLN A 1 165 ? -3.183 -17.706 -9.738 1.00 114.84 ? 165 GLN A NE2 1 ATOM 1313 N N . ASP A 1 166 ? 0.398 -13.393 -13.917 1.00 88.11 ? 166 ASP A N 1 ATOM 1314 C CA . ASP A 1 166 ? 0.857 -12.026 -14.232 1.00 87.27 ? 166 ASP A CA 1 ATOM 1315 C C . ASP A 1 166 ? 1.561 -11.937 -15.596 1.00 86.92 ? 166 ASP A C 1 ATOM 1316 O O . ASP A 1 166 ? 2.739 -12.275 -15.706 1.00 83.84 ? 166 ASP A O 1 ATOM 1317 C CB . ASP A 1 166 ? 1.786 -11.502 -13.138 1.00 84.80 ? 166 ASP A CB 1 ATOM 1318 C CG . ASP A 1 166 ? 2.253 -10.074 -13.397 1.00 90.10 ? 166 ASP A CG 1 ATOM 1319 O OD1 . ASP A 1 166 ? 1.826 -9.452 -14.394 1.00 97.26 ? 166 ASP A OD1 1 ATOM 1320 O OD2 . ASP A 1 166 ? 3.061 -9.563 -12.605 1.00 90.39 ? 166 ASP A OD2 1 ATOM 1321 N N . PRO A 1 167 ? 0.854 -11.448 -16.633 1.00 88.08 ? 167 PRO A N 1 ATOM 1322 C CA . PRO A 1 167 ? 1.412 -11.476 -17.987 1.00 88.96 ? 167 PRO A CA 1 ATOM 1323 C C . PRO A 1 167 ? 2.445 -10.383 -18.249 1.00 87.21 ? 167 PRO A C 1 ATOM 1324 O O . PRO A 1 167 ? 3.062 -10.379 -19.309 1.00 86.98 ? 167 PRO A O 1 ATOM 1325 C CB . PRO A 1 167 ? 0.181 -11.301 -18.878 1.00 91.50 ? 167 PRO A CB 1 ATOM 1326 C CG . PRO A 1 167 ? -0.839 -10.626 -18.026 1.00 90.60 ? 167 PRO A CG 1 ATOM 1327 C CD . PRO A 1 167 ? -0.418 -10.713 -16.587 1.00 88.82 ? 167 PRO A CD 1 ATOM 1328 N N . SER A 1 168 ? 2.595 -9.454 -17.303 1.00 84.23 ? 168 SER A N 1 ATOM 1329 C CA . SER A 1 168 ? 3.714 -8.509 -17.297 1.00 81.25 ? 168 SER A CA 1 ATOM 1330 C C . SER A 1 168 ? 5.039 -9.251 -17.160 1.00 82.40 ? 168 SER A C 1 ATOM 1331 O O . SER A 1 168 ? 6.034 -8.826 -17.709 1.00 81.50 ? 168 SER A O 1 ATOM 1332 C CB . SER A 1 168 ? 3.568 -7.494 -16.158 1.00 81.33 ? 168 SER A CB 1 ATOM 1333 O OG . SER A 1 168 ? 4.808 -7.216 -15.531 1.00 80.58 ? 168 SER A OG 1 ATOM 1334 N N . MET A 1 169 ? 5.037 -10.363 -16.428 1.00 83.02 ? 169 MET A N 1 ATOM 1335 C CA . MET A 1 169 ? 6.205 -11.242 -16.337 1.00 80.19 ? 169 MET A CA 1 ATOM 1336 C C . MET A 1 169 ? 6.262 -12.202 -17.528 1.00 81.55 ? 169 MET A C 1 ATOM 1337 O O . MET A 1 169 ? 5.291 -12.909 -17.812 1.00 81.56 ? 169 MET A O 1 ATOM 1338 C CB . MET A 1 169 ? 6.171 -12.049 -15.041 1.00 76.05 ? 169 MET A CB 1 ATOM 1339 C CG . MET A 1 169 ? 6.507 -11.237 -13.806 1.00 75.70 ? 169 MET A CG 1 ATOM 1340 S SD . MET A 1 169 ? 6.245 -12.170 -12.282 1.00 78.33 ? 169 MET A SD 1 ATOM 1341 C CE . MET A 1 169 ? 6.022 -10.831 -11.125 1.00 78.27 ? 169 MET A CE 1 ATOM 1342 N N . ASN A 1 170 ? 7.418 -12.254 -18.183 1.00 80.64 ? 170 ASN A N 1 ATOM 1343 C CA . ASN A 1 170 ? 7.609 -13.030 -19.421 1.00 81.11 ? 170 ASN A CA 1 ATOM 1344 C C . ASN A 1 170 ? 8.094 -14.461 -19.156 1.00 77.02 ? 170 ASN A C 1 ATOM 1345 O O . ASN A 1 170 ? 9.147 -14.882 -19.646 1.00 74.52 ? 170 ASN A O 1 ATOM 1346 C CB . ASN A 1 170 ? 8.593 -12.287 -20.355 1.00 82.04 ? 170 ASN A CB 1 ATOM 1347 C CG . ASN A 1 170 ? 8.664 -12.887 -21.757 1.00 79.69 ? 170 ASN A CG 1 ATOM 1348 O OD1 . ASN A 1 170 ? 7.771 -13.609 -22.178 1.00 79.31 ? 170 ASN A OD1 1 ATOM 1349 N ND2 . ASN A 1 170 ? 9.739 -12.601 -22.471 1.00 78.09 ? 170 ASN A ND2 1 ATOM 1350 N N . LEU A 1 171 ? 7.290 -15.211 -18.408 1.00 74.45 ? 171 LEU A N 1 ATOM 1351 C CA . LEU A 1 171 ? 7.606 -16.589 -18.040 1.00 70.42 ? 171 LEU A CA 1 ATOM 1352 C C . LEU A 1 171 ? 7.699 -17.494 -19.277 1.00 74.95 ? 171 LEU A C 1 ATOM 1353 O O . LEU A 1 171 ? 6.732 -17.645 -20.028 1.00 71.74 ? 171 LEU A O 1 ATOM 1354 C CB . LEU A 1 171 ? 6.542 -17.128 -17.091 1.00 68.51 ? 171 LEU A CB 1 ATOM 1355 C CG . LEU A 1 171 ? 6.689 -18.577 -16.627 1.00 68.06 ? 171 LEU A CG 1 ATOM 1356 C CD1 . LEU A 1 171 ? 7.983 -18.766 -15.858 1.00 64.81 ? 171 LEU A CD1 1 ATOM 1357 C CD2 . LEU A 1 171 ? 5.491 -18.994 -15.789 1.00 69.14 ? 171 LEU A CD2 1 ATOM 1358 N N . GLN A 1 172 ? 8.853 -18.110 -19.484 1.00 78.21 ? 172 GLN A N 1 ATOM 1359 C CA . GLN A 1 172 ? 8.993 -19.033 -20.595 1.00 80.83 ? 172 GLN A CA 1 ATOM 1360 C C . GLN A 1 172 ? 9.123 -20.483 -20.146 1.00 78.63 ? 172 GLN A C 1 ATOM 1361 O O . GLN A 1 172 ? 8.608 -21.370 -20.812 1.00 84.83 ? 172 GLN A O 1 ATOM 1362 C CB . GLN A 1 172 ? 10.139 -18.588 -21.512 1.00 86.25 ? 172 GLN A CB 1 ATOM 1363 C CG . GLN A 1 172 ? 9.805 -17.349 -22.351 1.00 87.12 ? 172 GLN A CG 1 ATOM 1364 C CD . GLN A 1 172 ? 8.575 -17.498 -23.256 1.00 89.58 ? 172 GLN A CD 1 ATOM 1365 O OE1 . GLN A 1 172 ? 8.327 -18.550 -23.855 1.00 89.70 ? 172 GLN A OE1 1 ATOM 1366 N NE2 . GLN A 1 172 ? 7.803 -16.430 -23.364 1.00 90.18 ? 172 GLN A NE2 1 ATOM 1367 N N . GLY A 1 173 ? 9.790 -20.733 -19.025 1.00 77.57 ? 173 GLY A N 1 ATOM 1368 C CA . GLY A 1 173 ? 9.854 -22.094 -18.462 1.00 74.33 ? 173 GLY A CA 1 ATOM 1369 C C . GLY A 1 173 ? 10.287 -22.227 -17.006 1.00 70.13 ? 173 GLY A C 1 ATOM 1370 O O . GLY A 1 173 ? 10.568 -21.235 -16.321 1.00 63.18 ? 173 GLY A O 1 ATOM 1371 N N . LEU A 1 174 ? 10.346 -23.473 -16.545 1.00 68.61 ? 174 LEU A N 1 ATOM 1372 C CA . LEU A 1 174 ? 10.863 -23.789 -15.218 1.00 66.51 ? 174 LEU A CA 1 ATOM 1373 C C . LEU A 1 174 ? 11.623 -25.116 -15.175 1.00 66.45 ? 174 LEU A C 1 ATOM 1374 O O . LEU A 1 174 ? 11.280 -26.050 -15.887 1.00 71.16 ? 174 LEU A O 1 ATOM 1375 C CB . LEU A 1 174 ? 9.727 -23.790 -14.209 1.00 66.25 ? 174 LEU A CB 1 ATOM 1376 C CG . LEU A 1 174 ? 8.542 -24.715 -14.485 1.00 68.34 ? 174 LEU A CG 1 ATOM 1377 C CD1 . LEU A 1 174 ? 8.656 -26.003 -13.697 1.00 69.12 ? 174 LEU A CD1 1 ATOM 1378 C CD2 . LEU A 1 174 ? 7.221 -24.067 -14.147 1.00 67.40 ? 174 LEU A CD2 1 ATOM 1379 N N . ALA A 1 175 ? 12.662 -25.193 -14.348 1.00 63.29 ? 175 ALA A N 1 ATOM 1380 C CA . ALA A 1 175 ? 13.419 -26.429 -14.180 1.00 61.33 ? 175 ALA A CA 1 ATOM 1381 C C . ALA A 1 175 ? 13.660 -26.749 -12.701 1.00 59.82 ? 175 ALA A C 1 ATOM 1382 O O . ALA A 1 175 ? 14.007 -25.868 -11.920 1.00 56.73 ? 175 ALA A O 1 ATOM 1383 C CB . ALA A 1 175 ? 14.735 -26.347 -14.924 1.00 59.58 ? 175 ALA A CB 1 ATOM 1384 N N . VAL A 1 176 ? 13.515 -28.023 -12.336 1.00 57.80 ? 176 VAL A N 1 ATOM 1385 C CA . VAL A 1 176 ? 13.668 -28.461 -10.952 1.00 55.65 ? 176 VAL A CA 1 ATOM 1386 C C . VAL A 1 176 ? 14.674 -29.607 -10.824 1.00 56.07 ? 176 VAL A C 1 ATOM 1387 O O . VAL A 1 176 ? 14.487 -30.665 -11.404 1.00 63.36 ? 176 VAL A O 1 ATOM 1388 C CB . VAL A 1 176 ? 12.300 -28.892 -10.404 1.00 55.50 ? 176 VAL A CB 1 ATOM 1389 C CG1 . VAL A 1 176 ? 12.432 -29.642 -9.091 1.00 55.54 ? 176 VAL A CG1 1 ATOM 1390 C CG2 . VAL A 1 176 ? 11.404 -27.679 -10.252 1.00 56.08 ? 176 VAL A CG2 1 ATOM 1391 N N . GLY A 1 177 ? 15.711 -29.407 -10.018 1.00 55.80 ? 177 GLY A N 1 ATOM 1392 C CA . GLY A 1 177 ? 16.755 -30.413 -9.802 1.00 54.80 ? 177 GLY A CA 1 ATOM 1393 C C . GLY A 1 177 ? 16.514 -31.240 -8.551 1.00 55.03 ? 177 GLY A C 1 ATOM 1394 O O . GLY A 1 177 ? 16.335 -30.705 -7.462 1.00 50.66 ? 177 GLY A O 1 ATOM 1395 N N . ASN A 1 178 ? 16.522 -32.558 -8.697 1.00 58.11 ? 178 ASN A N 1 ATOM 1396 C CA . ASN A 1 178 ? 16.173 -33.451 -7.593 1.00 59.03 ? 178 ASN A CA 1 ATOM 1397 C C . ASN A 1 178 ? 15.106 -32.843 -6.708 1.00 59.14 ? 178 ASN A C 1 ATOM 1398 O O . ASN A 1 178 ? 15.318 -32.588 -5.528 1.00 59.13 ? 178 ASN A O 1 ATOM 1399 C CB . ASN A 1 178 ? 17.413 -33.802 -6.800 1.00 56.45 ? 178 ASN A CB 1 ATOM 1400 C CG . ASN A 1 178 ? 18.318 -34.708 -7.574 1.00 56.74 ? 178 ASN A CG 1 ATOM 1401 O OD1 . ASN A 1 178 ? 19.051 -34.254 -8.465 1.00 57.56 ? 178 ASN A OD1 1 ATOM 1402 N ND2 . ASN A 1 178 ? 18.263 -36.005 -7.268 1.00 54.48 ? 178 ASN A ND2 1 ATOM 1403 N N . GLY A 1 179 ? 13.968 -32.569 -7.324 1.00 60.61 ? 179 GLY A N 1 ATOM 1404 C CA . GLY A 1 179 ? 12.888 -31.882 -6.661 1.00 62.29 ? 179 GLY A CA 1 ATOM 1405 C C . GLY A 1 179 ? 12.027 -32.836 -5.880 1.00 67.08 ? 179 GLY A C 1 ATOM 1406 O O . GLY A 1 179 ? 12.038 -34.050 -6.133 1.00 68.86 ? 179 GLY A O 1 ATOM 1407 N N . LEU A 1 180 ? 11.290 -32.270 -4.924 1.00 65.02 ? 180 LEU A N 1 ATOM 1408 C CA . LEU A 1 180 ? 10.253 -32.976 -4.220 1.00 63.66 ? 180 LEU A CA 1 ATOM 1409 C C . LEU A 1 180 ? 8.933 -32.619 -4.873 1.00 66.48 ? 180 LEU A C 1 ATOM 1410 O O . LEU A 1 180 ? 8.319 -31.585 -4.568 1.00 72.08 ? 180 LEU A O 1 ATOM 1411 C CB . LEU A 1 180 ? 10.262 -32.574 -2.758 1.00 65.71 ? 180 LEU A CB 1 ATOM 1412 C CG . LEU A 1 180 ? 9.278 -33.257 -1.813 1.00 66.91 ? 180 LEU A CG 1 ATOM 1413 C CD1 . LEU A 1 180 ? 9.348 -34.769 -1.940 1.00 68.25 ? 180 LEU A CD1 1 ATOM 1414 C CD2 . LEU A 1 180 ? 9.597 -32.825 -0.388 1.00 69.12 ? 180 LEU A CD2 1 ATOM 1415 N N . SER A 1 181 ? 8.519 -33.466 -5.803 1.00 65.94 ? 181 SER A N 1 ATOM 1416 C CA . SER A 1 181 ? 7.273 -33.275 -6.536 1.00 66.79 ? 181 SER A CA 1 ATOM 1417 C C . SER A 1 181 ? 6.098 -34.001 -5.881 1.00 65.62 ? 181 SER A C 1 ATOM 1418 O O . SER A 1 181 ? 4.972 -33.510 -5.940 1.00 64.33 ? 181 SER A O 1 ATOM 1419 C CB . SER A 1 181 ? 7.448 -33.757 -7.977 1.00 69.27 ? 181 SER A CB 1 ATOM 1420 O OG . SER A 1 181 ? 8.427 -32.983 -8.649 1.00 74.54 ? 181 SER A OG 1 ATOM 1421 N N . SER A 1 182 ? 6.367 -35.167 -5.283 1.00 62.48 ? 182 SER A N 1 ATOM 1422 C CA . SER A 1 182 ? 5.361 -35.962 -4.595 1.00 60.93 ? 182 SER A CA 1 ATOM 1423 C C . SER A 1 182 ? 5.930 -36.799 -3.473 1.00 57.94 ? 182 SER A C 1 ATOM 1424 O O . SER A 1 182 ? 6.697 -37.708 -3.737 1.00 59.59 ? 182 SER A O 1 ATOM 1425 C CB . SER A 1 182 ? 4.664 -36.896 -5.577 1.00 63.79 ? 182 SER A CB 1 ATOM 1426 O OG . SER A 1 182 ? 4.043 -37.984 -4.882 1.00 67.55 ? 182 SER A OG 1 ATOM 1427 N N . TYR A 1 183 ? 5.508 -36.541 -2.232 1.00 58.17 ? 183 TYR A N 1 ATOM 1428 C CA . TYR A 1 183 ? 5.974 -37.327 -1.072 1.00 57.52 ? 183 TYR A CA 1 ATOM 1429 C C . TYR A 1 183 ? 5.707 -38.819 -1.249 1.00 57.57 ? 183 TYR A C 1 ATOM 1430 O O . TYR A 1 183 ? 6.567 -39.640 -0.948 1.00 61.18 ? 183 TYR A O 1 ATOM 1431 C CB . TYR A 1 183 ? 5.332 -36.865 0.244 1.00 57.42 ? 183 TYR A CB 1 ATOM 1432 C CG . TYR A 1 183 ? 5.714 -35.481 0.714 1.00 59.15 ? 183 TYR A CG 1 ATOM 1433 C CD1 . TYR A 1 183 ? 6.805 -35.275 1.538 1.00 59.21 ? 183 TYR A CD1 1 ATOM 1434 C CD2 . TYR A 1 183 ? 4.965 -34.375 0.344 1.00 63.20 ? 183 TYR A CD2 1 ATOM 1435 C CE1 . TYR A 1 183 ? 7.138 -34.003 1.965 1.00 62.34 ? 183 TYR A CE1 1 ATOM 1436 C CE2 . TYR A 1 183 ? 5.286 -33.105 0.769 1.00 63.49 ? 183 TYR A CE2 1 ATOM 1437 C CZ . TYR A 1 183 ? 6.367 -32.914 1.574 1.00 64.60 ? 183 TYR A CZ 1 ATOM 1438 O OH . TYR A 1 183 ? 6.664 -31.619 1.976 1.00 68.60 ? 183 TYR A OH 1 ATOM 1439 N N . GLU A 1 184 ? 4.535 -39.169 -1.763 1.00 59.54 ? 184 GLU A N 1 ATOM 1440 C CA . GLU A 1 184 ? 4.160 -40.574 -1.900 1.00 64.29 ? 184 GLU A CA 1 ATOM 1441 C C . GLU A 1 184 ? 5.086 -41.325 -2.863 1.00 64.16 ? 184 GLU A C 1 ATOM 1442 O O . GLU A 1 184 ? 5.590 -42.400 -2.532 1.00 59.93 ? 184 GLU A O 1 ATOM 1443 C CB . GLU A 1 184 ? 2.709 -40.717 -2.357 1.00 67.96 ? 184 GLU A CB 1 ATOM 1444 C CG . GLU A 1 184 ? 2.212 -42.156 -2.378 1.00 72.33 ? 184 GLU A CG 1 ATOM 1445 C CD . GLU A 1 184 ? 0.747 -42.273 -2.725 1.00 78.63 ? 184 GLU A CD 1 ATOM 1446 O OE1 . GLU A 1 184 ? -0.046 -41.405 -2.299 1.00 80.01 ? 184 GLU A OE1 1 ATOM 1447 O OE2 . GLU A 1 184 ? 0.388 -43.246 -3.416 1.00 81.73 ? 184 GLU A OE2 1 ATOM 1448 N N . GLN A 1 185 ? 5.304 -40.766 -4.049 1.00 66.06 ? 185 GLN A N 1 ATOM 1449 C CA . GLN A 1 185 ? 6.171 -41.423 -5.036 1.00 68.44 ? 185 GLN A CA 1 ATOM 1450 C C . GLN A 1 185 ? 7.619 -41.440 -4.577 1.00 63.89 ? 185 GLN A C 1 ATOM 1451 O O . GLN A 1 185 ? 8.350 -42.407 -4.826 1.00 60.01 ? 185 GLN A O 1 ATOM 1452 C CB . GLN A 1 185 ? 6.037 -40.771 -6.423 1.00 68.70 ? 185 GLN A CB 1 ATOM 1453 C CG . GLN A 1 185 ? 4.887 -41.351 -7.214 1.00 71.82 ? 185 GLN A CG 1 ATOM 1454 C CD . GLN A 1 185 ? 4.346 -40.403 -8.249 1.00 74.96 ? 185 GLN A CD 1 ATOM 1455 O OE1 . GLN A 1 185 ? 4.201 -40.761 -9.421 1.00 75.84 ? 185 GLN A OE1 1 ATOM 1456 N NE2 . GLN A 1 185 ? 4.039 -39.184 -7.826 1.00 73.64 ? 185 GLN A NE2 1 ATOM 1457 N N . ASN A 1 186 ? 8.020 -40.356 -3.930 1.00 60.68 ? 186 ASN A N 1 ATOM 1458 C CA . ASN A 1 186 ? 9.361 -40.250 -3.386 1.00 62.07 ? 186 ASN A CA 1 ATOM 1459 C C . ASN A 1 186 ? 9.584 -41.376 -2.394 1.00 63.59 ? 186 ASN A C 1 ATOM 1460 O O . ASN A 1 186 ? 10.615 -42.059 -2.433 1.00 64.53 ? 186 ASN A O 1 ATOM 1461 C CB . ASN A 1 186 ? 9.547 -38.889 -2.703 1.00 60.87 ? 186 ASN A CB 1 ATOM 1462 C CG . ASN A 1 186 ? 10.974 -38.623 -2.287 1.00 60.21 ? 186 ASN A CG 1 ATOM 1463 O OD1 . ASN A 1 186 ? 11.897 -39.332 -2.667 1.00 61.45 ? 186 ASN A OD1 1 ATOM 1464 N ND2 . ASN A 1 186 ? 11.161 -37.585 -1.496 1.00 62.06 ? 186 ASN A ND2 1 ATOM 1465 N N . ASP A 1 187 ? 8.600 -41.573 -1.523 1.00 61.98 ? 187 ASP A N 1 ATOM 1466 C CA . ASP A 1 187 ? 8.743 -42.512 -0.437 1.00 63.50 ? 187 ASP A CA 1 ATOM 1467 C C . ASP A 1 187 ? 8.679 -43.954 -0.905 1.00 61.11 ? 187 ASP A C 1 ATOM 1468 O O . ASP A 1 187 ? 9.496 -44.767 -0.501 1.00 64.26 ? 187 ASP A O 1 ATOM 1469 C CB . ASP A 1 187 ? 7.726 -42.216 0.661 1.00 67.21 ? 187 ASP A CB 1 ATOM 1470 C CG . ASP A 1 187 ? 8.027 -40.908 1.404 1.00 72.17 ? 187 ASP A CG 1 ATOM 1471 O OD1 . ASP A 1 187 ? 8.770 -40.056 0.866 1.00 77.45 ? 187 ASP A OD1 1 ATOM 1472 O OD2 . ASP A 1 187 ? 7.510 -40.724 2.528 1.00 79.29 ? 187 ASP A OD2 1 ATOM 1473 N N . ASN A 1 188 ? 7.713 -44.285 -1.742 1.00 61.11 ? 188 ASN A N 1 ATOM 1474 C CA . ASN A 1 188 ? 7.618 -45.632 -2.309 1.00 61.52 ? 188 ASN A CA 1 ATOM 1475 C C . ASN A 1 188 ? 8.854 -45.975 -3.160 1.00 62.21 ? 188 ASN A C 1 ATOM 1476 O O . ASN A 1 188 ? 9.419 -47.055 -3.016 1.00 58.92 ? 188 ASN A O 1 ATOM 1477 C CB . ASN A 1 188 ? 6.363 -45.766 -3.178 1.00 63.78 ? 188 ASN A CB 1 ATOM 1478 C CG . ASN A 1 188 ? 5.064 -45.712 -2.375 1.00 62.96 ? 188 ASN A CG 1 ATOM 1479 O OD1 . ASN A 1 188 ? 4.932 -46.331 -1.320 1.00 64.57 ? 188 ASN A OD1 1 ATOM 1480 N ND2 . ASN A 1 188 ? 4.085 -45.005 -2.904 1.00 62.16 ? 188 ASN A ND2 1 ATOM 1481 N N . SER A 1 189 ? 9.276 -45.047 -4.024 1.00 61.06 ? 189 SER A N 1 ATOM 1482 C CA . SER A 1 189 ? 10.427 -45.276 -4.907 1.00 58.99 ? 189 SER A CA 1 ATOM 1483 C C . SER A 1 189 ? 11.755 -45.397 -4.145 1.00 58.93 ? 189 SER A C 1 ATOM 1484 O O . SER A 1 189 ? 12.621 -46.185 -4.513 1.00 57.02 ? 189 SER A O 1 ATOM 1485 C CB . SER A 1 189 ? 10.534 -44.189 -5.986 1.00 57.99 ? 189 SER A CB 1 ATOM 1486 O OG . SER A 1 189 ? 10.736 -42.886 -5.460 1.00 54.50 ? 189 SER A OG 1 ATOM 1487 N N . LEU A 1 190 ? 11.905 -44.632 -3.075 1.00 61.13 ? 190 LEU A N 1 ATOM 1488 C CA . LEU A 1 190 ? 13.111 -44.711 -2.228 1.00 61.49 ? 190 LEU A CA 1 ATOM 1489 C C . LEU A 1 190 ? 13.327 -46.101 -1.673 1.00 61.13 ? 190 LEU A C 1 ATOM 1490 O O . LEU A 1 190 ? 14.449 -46.573 -1.593 1.00 63.70 ? 190 LEU A O 1 ATOM 1491 C CB . LEU A 1 190 ? 13.010 -43.723 -1.061 1.00 60.94 ? 190 LEU A CB 1 ATOM 1492 C CG . LEU A 1 190 ? 14.191 -43.616 -0.106 1.00 60.97 ? 190 LEU A CG 1 ATOM 1493 C CD1 . LEU A 1 190 ? 15.512 -43.593 -0.875 1.00 64.06 ? 190 LEU A CD1 1 ATOM 1494 C CD2 . LEU A 1 190 ? 14.046 -42.364 0.752 1.00 58.93 ? 190 LEU A CD2 1 ATOM 1495 N N . VAL A 1 191 ? 12.245 -46.770 -1.298 1.00 61.42 ? 191 VAL A N 1 ATOM 1496 C CA . VAL A 1 191 ? 12.372 -48.082 -0.678 1.00 60.37 ? 191 VAL A CA 1 ATOM 1497 C C . VAL A 1 191 ? 12.872 -49.105 -1.691 1.00 60.65 ? 191 VAL A C 1 ATOM 1498 O O . VAL A 1 191 ? 13.780 -49.879 -1.374 1.00 60.54 ? 191 VAL A O 1 ATOM 1499 C CB . VAL A 1 191 ? 11.066 -48.520 -0.029 1.00 61.14 ? 191 VAL A CB 1 ATOM 1500 C CG1 . VAL A 1 191 ? 11.200 -49.901 0.591 1.00 60.23 ? 191 VAL A CG1 1 ATOM 1501 C CG2 . VAL A 1 191 ? 10.681 -47.503 1.018 1.00 62.46 ? 191 VAL A CG2 1 ATOM 1502 N N . TYR A 1 192 ? 12.301 -49.111 -2.902 1.00 60.26 ? 192 TYR A N 1 ATOM 1503 C CA . TYR A 1 192 ? 12.848 -49.929 -4.000 1.00 60.09 ? 192 TYR A CA 1 ATOM 1504 C C . TYR A 1 192 ? 14.290 -49.522 -4.220 1.00 59.78 ? 192 TYR A C 1 ATOM 1505 O O . TYR A 1 192 ? 15.169 -50.366 -4.349 1.00 58.10 ? 192 TYR A O 1 ATOM 1506 C CB . TYR A 1 192 ? 12.086 -49.724 -5.305 1.00 62.49 ? 192 TYR A CB 1 ATOM 1507 C CG . TYR A 1 192 ? 10.752 -50.419 -5.370 1.00 64.72 ? 192 TYR A CG 1 ATOM 1508 C CD1 . TYR A 1 192 ? 10.668 -51.742 -5.752 1.00 61.64 ? 192 TYR A CD1 1 ATOM 1509 C CD2 . TYR A 1 192 ? 9.574 -49.743 -5.053 1.00 64.72 ? 192 TYR A CD2 1 ATOM 1510 C CE1 . TYR A 1 192 ? 9.460 -52.380 -5.807 1.00 64.81 ? 192 TYR A CE1 1 ATOM 1511 C CE2 . TYR A 1 192 ? 8.354 -50.382 -5.100 1.00 65.79 ? 192 TYR A CE2 1 ATOM 1512 C CZ . TYR A 1 192 ? 8.302 -51.701 -5.483 1.00 67.53 ? 192 TYR A CZ 1 ATOM 1513 O OH . TYR A 1 192 ? 7.088 -52.359 -5.554 1.00 70.52 ? 192 TYR A OH 1 ATOM 1514 N N . PHE A 1 193 ? 14.536 -48.215 -4.241 1.00 57.61 ? 193 PHE A N 1 ATOM 1515 C CA . PHE A 1 193 ? 15.872 -47.722 -4.472 1.00 54.75 ? 193 PHE A CA 1 ATOM 1516 C C . PHE A 1 193 ? 16.805 -48.399 -3.506 1.00 54.87 ? 193 PHE A C 1 ATOM 1517 O O . PHE A 1 193 ? 17.832 -48.933 -3.902 1.00 56.32 ? 193 PHE A O 1 ATOM 1518 C CB . PHE A 1 193 ? 15.923 -46.212 -4.296 1.00 53.25 ? 193 PHE A CB 1 ATOM 1519 C CG . PHE A 1 193 ? 17.211 -45.590 -4.719 1.00 51.93 ? 193 PHE A CG 1 ATOM 1520 C CD1 . PHE A 1 193 ? 18.305 -45.621 -3.888 1.00 50.99 ? 193 PHE A CD1 1 ATOM 1521 C CD2 . PHE A 1 193 ? 17.313 -44.929 -5.939 1.00 52.88 ? 193 PHE A CD2 1 ATOM 1522 C CE1 . PHE A 1 193 ? 19.488 -45.028 -4.264 1.00 51.47 ? 193 PHE A CE1 1 ATOM 1523 C CE2 . PHE A 1 193 ? 18.495 -44.337 -6.323 1.00 52.21 ? 193 PHE A CE2 1 ATOM 1524 C CZ . PHE A 1 193 ? 19.589 -44.391 -5.481 1.00 50.75 ? 193 PHE A CZ 1 ATOM 1525 N N . ALA A 1 194 ? 16.430 -48.389 -2.237 1.00 57.66 ? 194 ALA A N 1 ATOM 1526 C CA . ALA A 1 194 ? 17.294 -48.889 -1.173 1.00 58.38 ? 194 ALA A CA 1 ATOM 1527 C C . ALA A 1 194 ? 17.611 -50.351 -1.363 1.00 59.82 ? 194 ALA A C 1 ATOM 1528 O O . ALA A 1 194 ? 18.755 -50.750 -1.235 1.00 61.34 ? 194 ALA A O 1 ATOM 1529 C CB . ALA A 1 194 ? 16.655 -48.655 0.184 1.00 58.07 ? 194 ALA A CB 1 ATOM 1530 N N . TYR A 1 195 ? 16.612 -51.157 -1.696 1.00 62.31 ? 195 TYR A N 1 ATOM 1531 C CA . TYR A 1 195 ? 16.857 -52.595 -1.867 1.00 64.81 ? 195 TYR A CA 1 ATOM 1532 C C . TYR A 1 195 ? 17.790 -52.862 -3.034 1.00 65.22 ? 195 TYR A C 1 ATOM 1533 O O . TYR A 1 195 ? 18.788 -53.594 -2.889 1.00 65.78 ? 195 TYR A O 1 ATOM 1534 C CB . TYR A 1 195 ? 15.563 -53.390 -2.061 1.00 65.66 ? 195 TYR A CB 1 ATOM 1535 C CG . TYR A 1 195 ? 15.767 -54.866 -2.347 1.00 67.84 ? 195 TYR A CG 1 ATOM 1536 C CD1 . TYR A 1 195 ? 16.494 -55.683 -1.479 1.00 69.61 ? 195 TYR A CD1 1 ATOM 1537 C CD2 . TYR A 1 195 ? 15.212 -55.458 -3.473 1.00 69.67 ? 195 TYR A CD2 1 ATOM 1538 C CE1 . TYR A 1 195 ? 16.669 -57.040 -1.742 1.00 67.70 ? 195 TYR A CE1 1 ATOM 1539 C CE2 . TYR A 1 195 ? 15.376 -56.813 -3.736 1.00 67.70 ? 195 TYR A CE2 1 ATOM 1540 C CZ . TYR A 1 195 ? 16.108 -57.592 -2.873 1.00 66.44 ? 195 TYR A CZ 1 ATOM 1541 O OH . TYR A 1 195 ? 16.280 -58.913 -3.164 1.00 64.34 ? 195 TYR A OH 1 ATOM 1542 N N . TYR A 1 196 ? 17.470 -52.257 -4.177 1.00 62.66 ? 196 TYR A N 1 ATOM 1543 C CA . TYR A 1 196 ? 18.155 -52.571 -5.426 1.00 61.76 ? 196 TYR A CA 1 ATOM 1544 C C . TYR A 1 196 ? 19.512 -51.906 -5.574 1.00 62.25 ? 196 TYR A C 1 ATOM 1545 O O . TYR A 1 196 ? 20.267 -52.237 -6.489 1.00 63.63 ? 196 TYR A O 1 ATOM 1546 C CB . TYR A 1 196 ? 17.248 -52.305 -6.612 1.00 58.41 ? 196 TYR A CB 1 ATOM 1547 C CG . TYR A 1 196 ? 16.128 -53.306 -6.681 1.00 58.19 ? 196 TYR A CG 1 ATOM 1548 C CD1 . TYR A 1 196 ? 16.345 -54.612 -7.113 1.00 59.56 ? 196 TYR A CD1 1 ATOM 1549 C CD2 . TYR A 1 196 ? 14.858 -52.968 -6.273 1.00 61.11 ? 196 TYR A CD2 1 ATOM 1550 C CE1 . TYR A 1 196 ? 15.306 -55.535 -7.163 1.00 61.11 ? 196 TYR A CE1 1 ATOM 1551 C CE2 . TYR A 1 196 ? 13.811 -53.876 -6.323 1.00 61.43 ? 196 TYR A CE2 1 ATOM 1552 C CZ . TYR A 1 196 ? 14.033 -55.151 -6.766 1.00 61.82 ? 196 TYR A CZ 1 ATOM 1553 O OH . TYR A 1 196 ? 12.965 -56.017 -6.812 1.00 66.03 ? 196 TYR A OH 1 ATOM 1554 N N . HIS A 1 197 ? 19.823 -51.010 -4.649 1.00 62.39 ? 197 HIS A N 1 ATOM 1555 C CA . HIS A 1 197 ? 21.170 -50.476 -4.513 1.00 64.67 ? 197 HIS A CA 1 ATOM 1556 C C . HIS A 1 197 ? 21.936 -51.117 -3.366 1.00 64.32 ? 197 HIS A C 1 ATOM 1557 O O . HIS A 1 197 ? 22.959 -50.592 -2.940 1.00 68.56 ? 197 HIS A O 1 ATOM 1558 C CB . HIS A 1 197 ? 21.132 -48.964 -4.310 1.00 64.26 ? 197 HIS A CB 1 ATOM 1559 C CG . HIS A 1 197 ? 20.740 -48.210 -5.537 1.00 62.76 ? 197 HIS A CG 1 ATOM 1560 N ND1 . HIS A 1 197 ? 19.456 -48.210 -6.026 1.00 61.35 ? 197 HIS A ND1 1 ATOM 1561 C CD2 . HIS A 1 197 ? 21.459 -47.422 -6.366 1.00 61.76 ? 197 HIS A CD2 1 ATOM 1562 C CE1 . HIS A 1 197 ? 19.399 -47.458 -7.109 1.00 62.48 ? 197 HIS A CE1 1 ATOM 1563 N NE2 . HIS A 1 197 ? 20.599 -46.963 -7.336 1.00 63.96 ? 197 HIS A NE2 1 ATOM 1564 N N . GLY A 1 198 ? 21.417 -52.214 -2.837 1.00 64.35 ? 198 GLY A N 1 ATOM 1565 C CA . GLY A 1 198 ? 22.187 -53.080 -1.948 1.00 65.79 ? 198 GLY A CA 1 ATOM 1566 C C . GLY A 1 198 ? 22.212 -52.749 -0.461 1.00 63.96 ? 198 GLY A C 1 ATOM 1567 O O . GLY A 1 198 ? 23.108 -53.209 0.260 1.00 64.08 ? 198 GLY A O 1 ATOM 1568 N N . LEU A 1 199 ? 21.223 -51.997 0.009 1.00 59.71 ? 199 LEU A N 1 ATOM 1569 C CA . LEU A 1 199 ? 21.221 -51.508 1.376 1.00 61.26 ? 199 LEU A CA 1 ATOM 1570 C C . LEU A 1 199 ? 20.326 -52.329 2.317 1.00 63.17 ? 199 LEU A C 1 ATOM 1571 O O . LEU A 1 199 ? 20.390 -52.150 3.533 1.00 59.36 ? 199 LEU A O 1 ATOM 1572 C CB . LEU A 1 199 ? 20.763 -50.048 1.402 1.00 62.63 ? 199 LEU A CB 1 ATOM 1573 C CG . LEU A 1 199 ? 21.212 -49.116 0.275 1.00 62.40 ? 199 LEU A CG 1 ATOM 1574 C CD1 . LEU A 1 199 ? 20.734 -47.699 0.533 1.00 62.16 ? 199 LEU A CD1 1 ATOM 1575 C CD2 . LEU A 1 199 ? 22.716 -49.125 0.121 1.00 65.33 ? 199 LEU A CD2 1 ATOM 1576 N N . LEU A 1 200 ? 19.501 -53.225 1.765 1.00 65.15 ? 200 LEU A N 1 ATOM 1577 C CA . LEU A 1 200 ? 18.423 -53.856 2.537 1.00 67.41 ? 200 LEU A CA 1 ATOM 1578 C C . LEU A 1 200 ? 18.517 -55.355 2.742 1.00 72.58 ? 200 LEU A C 1 ATOM 1579 O O . LEU A 1 200 ? 18.210 -55.852 3.839 1.00 84.02 ? 200 LEU A O 1 ATOM 1580 C CB . LEU A 1 200 ? 17.067 -53.580 1.896 1.00 65.03 ? 200 LEU A CB 1 ATOM 1581 C CG . LEU A 1 200 ? 16.585 -52.139 1.815 1.00 62.46 ? 200 LEU A CG 1 ATOM 1582 C CD1 . LEU A 1 200 ? 15.083 -52.148 1.673 1.00 61.01 ? 200 LEU A CD1 1 ATOM 1583 C CD2 . LEU A 1 200 ? 16.996 -51.300 3.013 1.00 63.29 ? 200 LEU A CD2 1 ATOM 1584 N N . GLY A 1 201 ? 18.875 -56.090 1.705 1.00 70.50 ? 201 GLY A N 1 ATOM 1585 C CA . GLY A 1 201 ? 18.929 -57.532 1.818 1.00 70.33 ? 201 GLY A CA 1 ATOM 1586 C C . GLY A 1 201 ? 17.548 -58.153 1.821 1.00 72.12 ? 201 GLY A C 1 ATOM 1587 O O . GLY A 1 201 ? 16.543 -57.460 1.942 1.00 67.97 ? 201 GLY A O 1 ATOM 1588 N N . ASN A 1 202 ? 17.525 -59.479 1.751 1.00 78.26 ? 202 ASN A N 1 ATOM 1589 C CA . ASN A 1 202 ? 16.333 -60.229 1.434 1.00 80.08 ? 202 ASN A CA 1 ATOM 1590 C C . ASN A 1 202 ? 15.362 -60.482 2.593 1.00 82.61 ? 202 ASN A C 1 ATOM 1591 O O . ASN A 1 202 ? 14.155 -60.522 2.374 1.00 83.09 ? 202 ASN A O 1 ATOM 1592 C CB . ASN A 1 202 ? 16.737 -61.548 0.822 1.00 88.70 ? 202 ASN A CB 1 ATOM 1593 C CG . ASN A 1 202 ? 15.580 -62.249 0.155 1.00 101.41 ? 202 ASN A CG 1 ATOM 1594 O OD1 . ASN A 1 202 ? 15.224 -63.374 0.529 1.00 114.45 ? 202 ASN A OD1 1 ATOM 1595 N ND2 . ASN A 1 202 ? 14.970 -61.586 -0.834 1.00 98.49 ? 202 ASN A ND2 1 ATOM 1596 N N . ARG A 1 203 ? 15.863 -60.667 3.813 1.00 82.79 ? 203 ARG A N 1 ATOM 1597 C CA . ARG A 1 203 ? 14.967 -60.849 4.952 1.00 83.22 ? 203 ARG A CA 1 ATOM 1598 C C . ARG A 1 203 ? 14.120 -59.608 5.095 1.00 80.86 ? 203 ARG A C 1 ATOM 1599 O O . ARG A 1 203 ? 12.895 -59.686 5.162 1.00 82.71 ? 203 ARG A O 1 ATOM 1600 C CB . ARG A 1 203 ? 15.721 -61.114 6.256 1.00 89.59 ? 203 ARG A CB 1 ATOM 1601 C CG . ARG A 1 203 ? 16.398 -62.468 6.330 1.00 98.96 ? 203 ARG A CG 1 ATOM 1602 C CD . ARG A 1 203 ? 16.655 -62.899 7.770 1.00 109.19 ? 203 ARG A CD 1 ATOM 1603 N NE . ARG A 1 203 ? 17.727 -63.897 7.870 1.00 126.58 ? 203 ARG A NE 1 ATOM 1604 C CZ . ARG A 1 203 ? 17.622 -65.190 7.541 1.00 133.75 ? 203 ARG A CZ 1 ATOM 1605 N NH1 . ARG A 1 203 ? 16.485 -65.696 7.071 1.00 137.37 ? 203 ARG A NH1 1 ATOM 1606 N NH2 . ARG A 1 203 ? 18.670 -65.991 7.684 1.00 128.92 ? 203 ARG A NH2 1 ATOM 1607 N N . LEU A 1 204 ? 14.770 -58.453 5.119 1.00 76.62 ? 204 LEU A N 1 ATOM 1608 C CA . LEU A 1 204 ? 14.052 -57.196 5.245 1.00 74.39 ? 204 LEU A CA 1 ATOM 1609 C C . LEU A 1 204 ? 13.170 -56.932 4.020 1.00 73.66 ? 204 LEU A C 1 ATOM 1610 O O . LEU A 1 204 ? 12.017 -56.531 4.175 1.00 68.77 ? 204 LEU A O 1 ATOM 1611 C CB . LEU A 1 204 ? 15.019 -56.040 5.495 1.00 73.74 ? 204 LEU A CB 1 ATOM 1612 C CG . LEU A 1 204 ? 14.440 -54.621 5.566 1.00 72.51 ? 204 LEU A CG 1 ATOM 1613 C CD1 . LEU A 1 204 ? 13.360 -54.520 6.608 1.00 70.75 ? 204 LEU A CD1 1 ATOM 1614 C CD2 . LEU A 1 204 ? 15.542 -53.602 5.848 1.00 74.64 ? 204 LEU A CD2 1 ATOM 1615 N N . TRP A 1 205 ? 13.698 -57.145 2.812 1.00 72.18 ? 205 TRP A N 1 ATOM 1616 C CA . TRP A 1 205 ? 12.868 -57.015 1.606 1.00 72.27 ? 205 TRP A CA 1 ATOM 1617 C C . TRP A 1 205 ? 11.628 -57.915 1.687 1.00 76.22 ? 205 TRP A C 1 ATOM 1618 O O . TRP A 1 205 ? 10.524 -57.451 1.467 1.00 75.01 ? 205 TRP A O 1 ATOM 1619 C CB . TRP A 1 205 ? 13.670 -57.304 0.347 1.00 71.78 ? 205 TRP A CB 1 ATOM 1620 C CG . TRP A 1 205 ? 12.940 -57.044 -0.934 1.00 72.85 ? 205 TRP A CG 1 ATOM 1621 C CD1 . TRP A 1 205 ? 12.680 -57.943 -1.919 1.00 72.38 ? 205 TRP A CD1 1 ATOM 1622 C CD2 . TRP A 1 205 ? 12.378 -55.799 -1.375 1.00 76.10 ? 205 TRP A CD2 1 ATOM 1623 N NE1 . TRP A 1 205 ? 11.995 -57.343 -2.946 1.00 72.81 ? 205 TRP A NE1 1 ATOM 1624 C CE2 . TRP A 1 205 ? 11.795 -56.029 -2.641 1.00 74.12 ? 205 TRP A CE2 1 ATOM 1625 C CE3 . TRP A 1 205 ? 12.299 -54.515 -0.820 1.00 75.96 ? 205 TRP A CE3 1 ATOM 1626 C CZ2 . TRP A 1 205 ? 11.144 -55.027 -3.360 1.00 74.91 ? 205 TRP A CZ2 1 ATOM 1627 C CZ3 . TRP A 1 205 ? 11.655 -53.508 -1.547 1.00 75.27 ? 205 TRP A CZ3 1 ATOM 1628 C CH2 . TRP A 1 205 ? 11.084 -53.776 -2.799 1.00 75.60 ? 205 TRP A CH2 1 ATOM 1629 N N . SER A 1 206 ? 11.794 -59.180 2.049 1.00 80.21 ? 206 SER A N 1 ATOM 1630 C CA . SER A 1 206 ? 10.641 -60.075 2.214 1.00 86.12 ? 206 SER A CA 1 ATOM 1631 C C . SER A 1 206 ? 9.614 -59.519 3.190 1.00 87.41 ? 206 SER A C 1 ATOM 1632 O O . SER A 1 206 ? 8.417 -59.533 2.911 1.00 91.43 ? 206 SER A O 1 ATOM 1633 C CB . SER A 1 206 ? 11.070 -61.450 2.715 1.00 88.70 ? 206 SER A CB 1 ATOM 1634 O OG . SER A 1 206 ? 11.747 -62.162 1.703 1.00 92.80 ? 206 SER A OG 1 ATOM 1635 N N . SER A 1 207 ? 10.082 -59.055 4.343 1.00 83.67 ? 207 SER A N 1 ATOM 1636 C CA . SER A 1 207 ? 9.181 -58.564 5.363 1.00 84.60 ? 207 SER A CA 1 ATOM 1637 C C . SER A 1 207 ? 8.385 -57.423 4.792 1.00 80.72 ? 207 SER A C 1 ATOM 1638 O O . SER A 1 207 ? 7.160 -57.430 4.827 1.00 86.39 ? 207 SER A O 1 ATOM 1639 C CB . SER A 1 207 ? 9.942 -58.100 6.612 1.00 88.46 ? 207 SER A CB 1 ATOM 1640 O OG . SER A 1 207 ? 10.613 -59.179 7.241 1.00 94.74 ? 207 SER A OG 1 ATOM 1641 N N . LEU A 1 208 ? 9.094 -56.455 4.240 1.00 79.52 ? 208 LEU A N 1 ATOM 1642 C CA . LEU A 1 208 ? 8.475 -55.303 3.615 1.00 75.78 ? 208 LEU A CA 1 ATOM 1643 C C . LEU A 1 208 ? 7.372 -55.720 2.622 1.00 77.81 ? 208 LEU A C 1 ATOM 1644 O O . LEU A 1 208 ? 6.255 -55.241 2.717 1.00 79.81 ? 208 LEU A O 1 ATOM 1645 C CB . LEU A 1 208 ? 9.549 -54.444 2.941 1.00 74.19 ? 208 LEU A CB 1 ATOM 1646 C CG . LEU A 1 208 ? 10.415 -53.635 3.919 1.00 75.28 ? 208 LEU A CG 1 ATOM 1647 C CD1 . LEU A 1 208 ? 11.776 -53.272 3.337 1.00 74.53 ? 208 LEU A CD1 1 ATOM 1648 C CD2 . LEU A 1 208 ? 9.691 -52.371 4.363 1.00 77.37 ? 208 LEU A CD2 1 ATOM 1649 N N . GLN A 1 209 ? 7.692 -56.607 1.681 1.00 79.17 ? 209 GLN A N 1 ATOM 1650 C CA . GLN A 1 209 ? 6.719 -57.143 0.713 1.00 80.27 ? 209 GLN A CA 1 ATOM 1651 C C . GLN A 1 209 ? 5.493 -57.730 1.394 1.00 82.46 ? 209 GLN A C 1 ATOM 1652 O O . GLN A 1 209 ? 4.346 -57.418 1.051 1.00 83.48 ? 209 GLN A O 1 ATOM 1653 C CB . GLN A 1 209 ? 7.363 -58.246 -0.146 1.00 80.65 ? 209 GLN A CB 1 ATOM 1654 C CG . GLN A 1 209 ? 8.340 -57.766 -1.203 1.00 81.26 ? 209 GLN A CG 1 ATOM 1655 C CD . GLN A 1 209 ? 7.627 -57.125 -2.370 1.00 83.64 ? 209 GLN A CD 1 ATOM 1656 O OE1 . GLN A 1 209 ? 7.339 -57.761 -3.383 1.00 83.50 ? 209 GLN A OE1 1 ATOM 1657 N NE2 . GLN A 1 209 ? 7.287 -55.870 -2.207 1.00 87.03 ? 209 GLN A NE2 1 ATOM 1658 N N . THR A 1 210 ? 5.757 -58.593 2.362 1.00 83.76 ? 210 THR A N 1 ATOM 1659 C CA . THR A 1 210 ? 4.709 -59.264 3.107 1.00 84.35 ? 210 THR A CA 1 ATOM 1660 C C . THR A 1 210 ? 3.728 -58.282 3.760 1.00 84.84 ? 210 THR A C 1 ATOM 1661 O O . THR A 1 210 ? 2.525 -58.411 3.583 1.00 79.45 ? 210 THR A O 1 ATOM 1662 C CB . THR A 1 210 ? 5.316 -60.139 4.214 1.00 84.40 ? 210 THR A CB 1 ATOM 1663 O OG1 . THR A 1 210 ? 6.094 -61.182 3.625 1.00 84.07 ? 210 THR A OG1 1 ATOM 1664 C CG2 . THR A 1 210 ? 4.228 -60.734 5.075 1.00 84.34 ? 210 THR A CG2 1 ATOM 1665 N N . HIS A 1 211 ? 4.264 -57.317 4.509 1.00 83.14 ? 211 HIS A N 1 ATOM 1666 C CA . HIS A 1 211 ? 3.467 -56.450 5.371 1.00 84.74 ? 211 HIS A CA 1 ATOM 1667 C C . HIS A 1 211 ? 3.016 -55.147 4.715 1.00 85.48 ? 211 HIS A C 1 ATOM 1668 O O . HIS A 1 211 ? 2.003 -54.576 5.097 1.00 89.01 ? 211 HIS A O 1 ATOM 1669 C CB . HIS A 1 211 ? 4.255 -56.119 6.640 1.00 89.62 ? 211 HIS A CB 1 ATOM 1670 C CG . HIS A 1 211 ? 4.735 -57.320 7.383 1.00 93.06 ? 211 HIS A CG 1 ATOM 1671 N ND1 . HIS A 1 211 ? 5.971 -57.374 7.981 1.00 94.49 ? 211 HIS A ND1 1 ATOM 1672 C CD2 . HIS A 1 211 ? 4.155 -58.519 7.607 1.00 94.53 ? 211 HIS A CD2 1 ATOM 1673 C CE1 . HIS A 1 211 ? 6.129 -58.553 8.551 1.00 97.76 ? 211 HIS A CE1 1 ATOM 1674 N NE2 . HIS A 1 211 ? 5.042 -59.265 8.340 1.00 96.32 ? 211 HIS A NE2 1 ATOM 1675 N N . CYS A 1 212 ? 3.762 -54.675 3.728 1.00 83.90 ? 212 CYS A N 1 ATOM 1676 C CA . CYS A 1 212 ? 3.451 -53.411 3.083 1.00 80.68 ? 212 CYS A CA 1 ATOM 1677 C C . CYS A 1 212 ? 2.877 -53.544 1.692 1.00 79.93 ? 212 CYS A C 1 ATOM 1678 O O . CYS A 1 212 ? 2.562 -52.541 1.074 1.00 76.98 ? 212 CYS A O 1 ATOM 1679 C CB . CYS A 1 212 ? 4.713 -52.582 2.969 1.00 77.38 ? 212 CYS A CB 1 ATOM 1680 S SG . CYS A 1 212 ? 5.616 -52.428 4.512 1.00 74.66 ? 212 CYS A SG 1 ATOM 1681 N N . CYS A 1 213 ? 2.792 -54.761 1.175 1.00 82.85 ? 213 CYS A N 1 ATOM 1682 C CA . CYS A 1 213 ? 2.438 -54.946 -0.227 1.00 88.30 ? 213 CYS A CA 1 ATOM 1683 C C . CYS A 1 213 ? 1.523 -56.121 -0.421 1.00 90.94 ? 213 CYS A C 1 ATOM 1684 O O . CYS A 1 213 ? 1.726 -57.169 0.173 1.00 92.17 ? 213 CYS A O 1 ATOM 1685 C CB . CYS A 1 213 ? 3.686 -55.167 -1.098 1.00 88.63 ? 213 CYS A CB 1 ATOM 1686 S SG . CYS A 1 213 ? 5.121 -54.127 -0.750 1.00 89.17 ? 213 CYS A SG 1 ATOM 1687 N N . SER A 1 214 ? 0.522 -55.936 -1.266 1.00 98.35 ? 214 SER A N 1 ATOM 1688 C CA . SER A 1 214 ? -0.229 -57.047 -1.805 1.00 110.43 ? 214 SER A CA 1 ATOM 1689 C C . SER A 1 214 ? -0.126 -57.047 -3.331 1.00 108.81 ? 214 SER A C 1 ATOM 1690 O O . SER A 1 214 ? -0.593 -56.116 -3.987 1.00 108.74 ? 214 SER A O 1 ATOM 1691 C CB . SER A 1 214 ? -1.697 -56.979 -1.369 1.00 119.30 ? 214 SER A CB 1 ATOM 1692 O OG . SER A 1 214 ? -2.390 -55.942 -2.048 1.00 122.29 ? 214 SER A OG 1 ATOM 1693 N N . GLN A 1 215 ? 0.509 -58.090 -3.869 1.00 107.80 ? 215 GLN A N 1 ATOM 1694 C CA . GLN A 1 215 ? 0.409 -58.483 -5.276 1.00 110.50 ? 215 GLN A CA 1 ATOM 1695 C C . GLN A 1 215 ? 0.280 -57.335 -6.291 1.00 112.38 ? 215 GLN A C 1 ATOM 1696 O O . GLN A 1 215 ? -0.819 -56.956 -6.673 1.00 106.13 ? 215 GLN A O 1 ATOM 1697 C CB . GLN A 1 215 ? -0.732 -59.516 -5.421 1.00 111.25 ? 215 GLN A CB 1 ATOM 1698 C CG . GLN A 1 215 ? -2.065 -59.148 -4.759 1.00 111.49 ? 215 GLN A CG 1 ATOM 1699 C CD . GLN A 1 215 ? -2.839 -60.349 -4.220 1.00 118.31 ? 215 GLN A CD 1 ATOM 1700 O OE1 . GLN A 1 215 ? -2.427 -61.494 -4.373 1.00 112.23 ? 215 GLN A OE1 1 ATOM 1701 N NE2 . GLN A 1 215 ? -3.971 -60.083 -3.571 1.00 125.38 ? 215 GLN A NE2 1 ATOM 1702 N N . ASN A 1 216 ? 1.422 -56.782 -6.702 1.00 117.11 ? 216 ASN A N 1 ATOM 1703 C CA . ASN A 1 216 ? 1.509 -55.747 -7.758 1.00 117.26 ? 216 ASN A CA 1 ATOM 1704 C C . ASN A 1 216 ? 1.257 -54.276 -7.320 1.00 112.38 ? 216 ASN A C 1 ATOM 1705 O O . ASN A 1 216 ? 1.081 -53.369 -8.150 1.00 109.17 ? 216 ASN A O 1 ATOM 1706 C CB . ASN A 1 216 ? 0.676 -56.136 -8.991 1.00 119.79 ? 216 ASN A CB 1 ATOM 1707 C CG . ASN A 1 216 ? 1.477 -56.920 -9.997 1.00 117.54 ? 216 ASN A CG 1 ATOM 1708 O OD1 . ASN A 1 216 ? 2.256 -56.357 -10.765 1.00 113.50 ? 216 ASN A OD1 1 ATOM 1709 N ND2 . ASN A 1 216 ? 1.289 -58.224 -10.004 1.00 115.58 ? 216 ASN A ND2 1 ATOM 1710 N N . LYS A 1 217 ? 1.258 -54.029 -6.015 1.00 104.84 ? 217 LYS A N 1 ATOM 1711 C CA . LYS A 1 217 ? 1.483 -52.683 -5.541 1.00 95.04 ? 217 LYS A CA 1 ATOM 1712 C C . LYS A 1 217 ? 1.853 -52.647 -4.065 1.00 92.58 ? 217 LYS A C 1 ATOM 1713 O O . LYS A 1 217 ? 1.276 -53.352 -3.244 1.00 87.47 ? 217 LYS A O 1 ATOM 1714 C CB . LYS A 1 217 ? 0.248 -51.846 -5.752 1.00 94.96 ? 217 LYS A CB 1 ATOM 1715 C CG . LYS A 1 217 ? 0.563 -50.374 -5.896 1.00 91.77 ? 217 LYS A CG 1 ATOM 1716 C CD . LYS A 1 217 ? -0.676 -49.599 -6.273 1.00 94.49 ? 217 LYS A CD 1 ATOM 1717 C CE . LYS A 1 217 ? -1.760 -49.729 -5.195 1.00 98.32 ? 217 LYS A CE 1 ATOM 1718 N NZ . LYS A 1 217 ? -2.302 -48.419 -4.745 1.00 102.79 ? 217 LYS A NZ 1 ATOM 1719 N N . CYS A 1 218 ? 2.811 -51.794 -3.745 1.00 88.56 ? 218 CYS A N 1 ATOM 1720 C CA . CYS A 1 218 ? 3.224 -51.577 -2.370 1.00 86.51 ? 218 CYS A CA 1 ATOM 1721 C C . CYS A 1 218 ? 2.698 -50.246 -1.846 1.00 83.33 ? 218 CYS A C 1 ATOM 1722 O O . CYS A 1 218 ? 2.492 -49.304 -2.606 1.00 83.71 ? 218 CYS A O 1 ATOM 1723 C CB . CYS A 1 218 ? 4.744 -51.576 -2.305 1.00 87.10 ? 218 CYS A CB 1 ATOM 1724 S SG . CYS A 1 218 ? 5.513 -53.202 -2.530 1.00 85.84 ? 218 CYS A SG 1 ATOM 1725 N N . ASN A 1 219 ? 2.453 -50.179 -0.544 1.00 80.14 ? 219 ASN A N 1 ATOM 1726 C CA . ASN A 1 219 ? 2.271 -48.899 0.124 1.00 77.07 ? 219 ASN A CA 1 ATOM 1727 C C . ASN A 1 219 ? 3.357 -48.771 1.160 1.00 72.97 ? 219 ASN A C 1 ATOM 1728 O O . ASN A 1 219 ? 3.279 -49.372 2.234 1.00 70.04 ? 219 ASN A O 1 ATOM 1729 C CB . ASN A 1 219 ? 0.902 -48.772 0.795 1.00 79.35 ? 219 ASN A CB 1 ATOM 1730 C CG . ASN A 1 219 ? 0.699 -47.417 1.470 1.00 78.20 ? 219 ASN A CG 1 ATOM 1731 O OD1 . ASN A 1 219 ? 1.507 -46.503 1.327 1.00 72.03 ? 219 ASN A OD1 1 ATOM 1732 N ND2 . ASN A 1 219 ? -0.400 -47.283 2.192 1.00 79.85 ? 219 ASN A ND2 1 ATOM 1733 N N . PHE A 1 220 ? 4.388 -48.013 0.805 1.00 69.81 ? 220 PHE A N 1 ATOM 1734 C CA . PHE A 1 220 ? 5.429 -47.637 1.748 1.00 68.49 ? 220 PHE A CA 1 ATOM 1735 C C . PHE A 1 220 ? 5.259 -46.186 2.196 1.00 70.49 ? 220 PHE A C 1 ATOM 1736 O O . PHE A 1 220 ? 6.079 -45.680 2.948 1.00 74.47 ? 220 PHE A O 1 ATOM 1737 C CB . PHE A 1 220 ? 6.795 -47.791 1.118 1.00 64.54 ? 220 PHE A CB 1 ATOM 1738 C CG . PHE A 1 220 ? 7.105 -49.183 0.655 1.00 61.38 ? 220 PHE A CG 1 ATOM 1739 C CD1 . PHE A 1 220 ? 6.972 -50.269 1.509 1.00 61.52 ? 220 PHE A CD1 1 ATOM 1740 C CD2 . PHE A 1 220 ? 7.600 -49.393 -0.606 1.00 58.62 ? 220 PHE A CD2 1 ATOM 1741 C CE1 . PHE A 1 220 ? 7.293 -51.548 1.091 1.00 61.81 ? 220 PHE A CE1 1 ATOM 1742 C CE2 . PHE A 1 220 ? 7.913 -50.668 -1.032 1.00 60.69 ? 220 PHE A CE2 1 ATOM 1743 C CZ . PHE A 1 220 ? 7.757 -51.752 -0.190 1.00 60.72 ? 220 PHE A CZ 1 ATOM 1744 N N . TYR A 1 221 ? 4.193 -45.528 1.748 1.00 71.42 ? 221 TYR A N 1 ATOM 1745 C CA . TYR A 1 221 ? 3.932 -44.129 2.103 1.00 71.41 ? 221 TYR A CA 1 ATOM 1746 C C . TYR A 1 221 ? 3.213 -43.983 3.451 1.00 70.78 ? 221 TYR A C 1 ATOM 1747 O O . TYR A 1 221 ? 3.770 -43.454 4.394 1.00 67.79 ? 221 TYR A O 1 ATOM 1748 C CB . TYR A 1 221 ? 3.119 -43.446 0.998 1.00 72.56 ? 221 TYR A CB 1 ATOM 1749 C CG . TYR A 1 221 ? 2.710 -42.009 1.298 1.00 72.88 ? 221 TYR A CG 1 ATOM 1750 C CD1 . TYR A 1 221 ? 3.632 -41.076 1.771 1.00 72.25 ? 221 TYR A CD1 1 ATOM 1751 C CD2 . TYR A 1 221 ? 1.409 -41.581 1.072 1.00 72.47 ? 221 TYR A CD2 1 ATOM 1752 C CE1 . TYR A 1 221 ? 3.264 -39.763 2.026 1.00 73.32 ? 221 TYR A CE1 1 ATOM 1753 C CE2 . TYR A 1 221 ? 1.028 -40.279 1.323 1.00 73.64 ? 221 TYR A CE2 1 ATOM 1754 C CZ . TYR A 1 221 ? 1.953 -39.370 1.801 1.00 76.62 ? 221 TYR A CZ 1 ATOM 1755 O OH . TYR A 1 221 ? 1.573 -38.065 2.046 1.00 79.63 ? 221 TYR A OH 1 ATOM 1756 N N . ASP A 1 222 ? 1.976 -44.446 3.528 1.00 74.99 ? 222 ASP A N 1 ATOM 1757 C CA . ASP A 1 222 ? 1.130 -44.192 4.695 1.00 79.08 ? 222 ASP A CA 1 ATOM 1758 C C . ASP A 1 222 ? 0.463 -45.471 5.171 1.00 78.51 ? 222 ASP A C 1 ATOM 1759 O O . ASP A 1 222 ? -0.647 -45.452 5.674 1.00 82.69 ? 222 ASP A O 1 ATOM 1760 C CB . ASP A 1 222 ? 0.072 -43.111 4.367 1.00 79.72 ? 222 ASP A CB 1 ATOM 1761 C CG . ASP A 1 222 ? -0.767 -43.460 3.148 1.00 78.26 ? 222 ASP A CG 1 ATOM 1762 O OD1 . ASP A 1 222 ? -0.791 -44.640 2.758 1.00 77.83 ? 222 ASP A OD1 1 ATOM 1763 O OD2 . ASP A 1 222 ? -1.395 -42.550 2.575 1.00 80.13 ? 222 ASP A OD2 1 ATOM 1764 N N . ASN A 1 223 ? 1.164 -46.577 5.024 1.00 80.38 ? 223 ASN A N 1 ATOM 1765 C CA . ASN A 1 223 ? 0.631 -47.883 5.368 1.00 84.48 ? 223 ASN A CA 1 ATOM 1766 C C . ASN A 1 223 ? 0.378 -47.997 6.861 1.00 86.40 ? 223 ASN A C 1 ATOM 1767 O O . ASN A 1 223 ? 1.214 -47.602 7.670 1.00 82.91 ? 223 ASN A O 1 ATOM 1768 C CB . ASN A 1 223 ? 1.612 -48.962 4.938 1.00 88.92 ? 223 ASN A CB 1 ATOM 1769 C CG . ASN A 1 223 ? 0.963 -50.311 4.781 1.00 90.75 ? 223 ASN A CG 1 ATOM 1770 O OD1 . ASN A 1 223 ? 0.233 -50.764 5.656 1.00 96.65 ? 223 ASN A OD1 1 ATOM 1771 N ND2 . ASN A 1 223 ? 1.244 -50.969 3.670 1.00 92.57 ? 223 ASN A ND2 1 ATOM 1772 N N . LYS A 1 224 ? -0.778 -48.541 7.222 1.00 91.59 ? 224 LYS A N 1 ATOM 1773 C CA . LYS A 1 224 ? -1.195 -48.611 8.626 1.00 94.09 ? 224 LYS A CA 1 ATOM 1774 C C . LYS A 1 224 ? -0.878 -49.947 9.273 1.00 93.28 ? 224 LYS A C 1 ATOM 1775 O O . LYS A 1 224 ? -1.049 -50.101 10.471 1.00 97.68 ? 224 LYS A O 1 ATOM 1776 C CB . LYS A 1 224 ? -2.688 -48.300 8.754 1.00 95.25 ? 224 LYS A CB 1 ATOM 1777 C CG . LYS A 1 224 ? -3.066 -46.874 8.380 1.00 94.08 ? 224 LYS A CG 1 ATOM 1778 C CD . LYS A 1 224 ? -2.513 -45.859 9.373 1.00 95.72 ? 224 LYS A CD 1 ATOM 1779 C CE . LYS A 1 224 ? -2.830 -44.434 8.967 1.00 95.81 ? 224 LYS A CE 1 ATOM 1780 N NZ . LYS A 1 224 ? -2.117 -44.031 7.720 1.00 97.24 ? 224 LYS A NZ 1 ATOM 1781 N N . ASP A 1 225 ? -0.409 -50.907 8.491 1.00 90.96 ? 225 ASP A N 1 ATOM 1782 C CA . ASP A 1 225 ? 0.009 -52.180 9.049 1.00 92.79 ? 225 ASP A CA 1 ATOM 1783 C C . ASP A 1 225 ? 1.181 -51.933 9.998 1.00 93.08 ? 225 ASP A C 1 ATOM 1784 O O . ASP A 1 225 ? 2.207 -51.382 9.603 1.00 91.26 ? 225 ASP A O 1 ATOM 1785 C CB . ASP A 1 225 ? 0.395 -53.146 7.933 1.00 95.25 ? 225 ASP A CB 1 ATOM 1786 C CG . ASP A 1 225 ? 0.578 -54.568 8.427 1.00 98.94 ? 225 ASP A CG 1 ATOM 1787 O OD1 . ASP A 1 225 ? 1.143 -54.753 9.528 1.00 99.56 ? 225 ASP A OD1 1 ATOM 1788 O OD2 . ASP A 1 225 ? 0.149 -55.498 7.712 1.00 96.00 ? 225 ASP A OD2 1 ATOM 1789 N N . LEU A 1 226 ? 1.010 -52.327 11.254 1.00 94.80 ? 226 LEU A N 1 ATOM 1790 C CA . LEU A 1 226 ? 1.988 -52.032 12.306 1.00 95.35 ? 226 LEU A CA 1 ATOM 1791 C C . LEU A 1 226 ? 3.317 -52.764 12.103 1.00 94.96 ? 226 LEU A C 1 ATOM 1792 O O . LEU A 1 226 ? 4.378 -52.272 12.498 1.00 93.76 ? 226 LEU A O 1 ATOM 1793 C CB . LEU A 1 226 ? 1.394 -52.359 13.681 1.00 97.49 ? 226 LEU A CB 1 ATOM 1794 C CG . LEU A 1 226 ? 0.228 -51.447 14.074 1.00 98.44 ? 226 LEU A CG 1 ATOM 1795 C CD1 . LEU A 1 226 ? -0.859 -52.215 14.807 1.00 102.34 ? 226 LEU A CD1 1 ATOM 1796 C CD2 . LEU A 1 226 ? 0.712 -50.261 14.891 1.00 95.45 ? 226 LEU A CD2 1 ATOM 1797 N N . GLU A 1 227 ? 3.257 -53.938 11.490 1.00 95.26 ? 227 GLU A N 1 ATOM 1798 C CA . GLU A 1 227 ? 4.468 -54.653 11.112 1.00 91.69 ? 227 GLU A CA 1 ATOM 1799 C C . GLU A 1 227 ? 5.151 -54.009 9.919 1.00 89.56 ? 227 GLU A C 1 ATOM 1800 O O . GLU A 1 227 ? 6.378 -54.064 9.819 1.00 85.52 ? 227 GLU A O 1 ATOM 1801 C CB . GLU A 1 227 ? 4.175 -56.114 10.816 1.00 94.99 ? 227 GLU A CB 1 ATOM 1802 C CG . GLU A 1 227 ? 4.302 -56.971 12.059 1.00 96.97 ? 227 GLU A CG 1 ATOM 1803 C CD . GLU A 1 227 ? 4.465 -58.423 11.706 1.00 97.57 ? 227 GLU A CD 1 ATOM 1804 O OE1 . GLU A 1 227 ? 5.628 -58.898 11.727 1.00 95.18 ? 227 GLU A OE1 1 ATOM 1805 O OE2 . GLU A 1 227 ? 3.432 -59.063 11.383 1.00 94.94 ? 227 GLU A OE2 1 ATOM 1806 N N . CYS A 1 228 ? 4.370 -53.400 9.026 1.00 87.97 ? 228 CYS A N 1 ATOM 1807 C CA . CYS A 1 228 ? 4.948 -52.604 7.937 1.00 84.94 ? 228 CYS A CA 1 ATOM 1808 C C . CYS A 1 228 ? 5.696 -51.399 8.506 1.00 81.33 ? 228 CYS A C 1 ATOM 1809 O O . CYS A 1 228 ? 6.816 -51.113 8.105 1.00 81.21 ? 228 CYS A O 1 ATOM 1810 C CB . CYS A 1 228 ? 3.876 -52.146 6.939 1.00 83.92 ? 228 CYS A CB 1 ATOM 1811 S SG . CYS A 1 228 ? 4.491 -51.125 5.567 1.00 78.31 ? 228 CYS A SG 1 ATOM 1812 N N . VAL A 1 229 ? 5.083 -50.712 9.462 1.00 79.92 ? 229 VAL A N 1 ATOM 1813 C CA . VAL A 1 229 ? 5.707 -49.536 10.057 1.00 78.48 ? 229 VAL A CA 1 ATOM 1814 C C . VAL A 1 229 ? 7.054 -49.843 10.700 1.00 79.63 ? 229 VAL A C 1 ATOM 1815 O O . VAL A 1 229 ? 8.014 -49.091 10.530 1.00 82.61 ? 229 VAL A O 1 ATOM 1816 C CB . VAL A 1 229 ? 4.780 -48.859 11.076 1.00 75.34 ? 229 VAL A CB 1 ATOM 1817 C CG1 . VAL A 1 229 ? 5.527 -47.808 11.887 1.00 74.34 ? 229 VAL A CG1 1 ATOM 1818 C CG2 . VAL A 1 229 ? 3.632 -48.210 10.333 1.00 76.71 ? 229 VAL A CG2 1 ATOM 1819 N N . THR A 1 230 ? 7.132 -50.946 11.428 1.00 78.37 ? 230 THR A N 1 ATOM 1820 C CA . THR A 1 230 ? 8.375 -51.323 12.091 1.00 76.00 ? 230 THR A CA 1 ATOM 1821 C C . THR A 1 230 ? 9.495 -51.501 11.069 1.00 76.45 ? 230 THR A C 1 ATOM 1822 O O . THR A 1 230 ? 10.637 -51.171 11.346 1.00 80.04 ? 230 THR A O 1 ATOM 1823 C CB . THR A 1 230 ? 8.185 -52.613 12.892 1.00 77.21 ? 230 THR A CB 1 ATOM 1824 O OG1 . THR A 1 230 ? 7.096 -52.428 13.800 1.00 77.22 ? 230 THR A OG1 1 ATOM 1825 C CG2 . THR A 1 230 ? 9.449 -52.995 13.670 1.00 76.72 ? 230 THR A CG2 1 ATOM 1826 N N . ASN A 1 231 ? 9.159 -52.020 9.891 1.00 76.32 ? 231 ASN A N 1 ATOM 1827 C CA . ASN A 1 231 ? 10.125 -52.222 8.825 1.00 74.89 ? 231 ASN A CA 1 ATOM 1828 C C . ASN A 1 231 ? 10.451 -50.959 8.066 1.00 76.11 ? 231 ASN A C 1 ATOM 1829 O O . ASN A 1 231 ? 11.618 -50.716 7.737 1.00 76.62 ? 231 ASN A O 1 ATOM 1830 C CB . ASN A 1 231 ? 9.621 -53.268 7.850 1.00 77.66 ? 231 ASN A CB 1 ATOM 1831 C CG . ASN A 1 231 ? 9.720 -54.662 8.411 1.00 79.82 ? 231 ASN A CG 1 ATOM 1832 O OD1 . ASN A 1 231 ? 10.610 -54.948 9.209 1.00 78.07 ? 231 ASN A OD1 1 ATOM 1833 N ND2 . ASN A 1 231 ? 8.804 -55.533 8.014 1.00 81.66 ? 231 ASN A ND2 1 ATOM 1834 N N . LEU A 1 232 ? 9.441 -50.145 7.785 1.00 73.93 ? 232 LEU A N 1 ATOM 1835 C CA . LEU A 1 232 ? 9.715 -48.854 7.169 1.00 73.88 ? 232 LEU A CA 1 ATOM 1836 C C . LEU A 1 232 ? 10.660 -48.049 8.061 1.00 73.40 ? 232 LEU A C 1 ATOM 1837 O O . LEU A 1 232 ? 11.563 -47.378 7.562 1.00 76.03 ? 232 LEU A O 1 ATOM 1838 C CB . LEU A 1 232 ? 8.434 -48.083 6.872 1.00 73.23 ? 232 LEU A CB 1 ATOM 1839 C CG . LEU A 1 232 ? 7.643 -48.594 5.661 1.00 74.38 ? 232 LEU A CG 1 ATOM 1840 C CD1 . LEU A 1 232 ? 6.290 -47.896 5.532 1.00 74.27 ? 232 LEU A CD1 1 ATOM 1841 C CD2 . LEU A 1 232 ? 8.439 -48.419 4.380 1.00 74.52 ? 232 LEU A CD2 1 ATOM 1842 N N . GLN A 1 233 ? 10.468 -48.137 9.373 1.00 73.75 ? 233 GLN A N 1 ATOM 1843 C CA . GLN A 1 233 ? 11.358 -47.473 10.318 1.00 75.36 ? 233 GLN A CA 1 ATOM 1844 C C . GLN A 1 233 ? 12.790 -47.966 10.204 1.00 75.09 ? 233 GLN A C 1 ATOM 1845 O O . GLN A 1 233 ? 13.732 -47.168 10.260 1.00 69.75 ? 233 GLN A O 1 ATOM 1846 C CB . GLN A 1 233 ? 10.870 -47.687 11.737 1.00 79.17 ? 233 GLN A CB 1 ATOM 1847 C CG . GLN A 1 233 ? 9.641 -46.871 12.080 1.00 79.74 ? 233 GLN A CG 1 ATOM 1848 C CD . GLN A 1 233 ? 9.103 -47.169 13.458 1.00 78.07 ? 233 GLN A CD 1 ATOM 1849 O OE1 . GLN A 1 233 ? 8.337 -46.386 13.998 1.00 79.85 ? 233 GLN A OE1 1 ATOM 1850 N NE2 . GLN A 1 233 ? 9.494 -48.302 14.033 1.00 75.78 ? 233 GLN A NE2 1 ATOM 1851 N N . GLU A 1 234 ? 12.949 -49.276 10.045 1.00 74.08 ? 234 GLU A N 1 ATOM 1852 C CA . GLU A 1 234 ? 14.264 -49.848 9.823 1.00 74.57 ? 234 GLU A CA 1 ATOM 1853 C C . GLU A 1 234 ? 14.876 -49.272 8.544 1.00 72.65 ? 234 GLU A C 1 ATOM 1854 O O . GLU A 1 234 ? 16.005 -48.800 8.572 1.00 67.95 ? 234 GLU A O 1 ATOM 1855 C CB . GLU A 1 234 ? 14.185 -51.370 9.774 1.00 80.48 ? 234 GLU A CB 1 ATOM 1856 C CG . GLU A 1 234 ? 15.416 -52.100 9.245 1.00 88.31 ? 234 GLU A CG 1 ATOM 1857 C CD . GLU A 1 234 ? 16.651 -51.935 10.114 1.00 99.53 ? 234 GLU A CD 1 ATOM 1858 O OE1 . GLU A 1 234 ? 16.840 -50.856 10.717 1.00 105.31 ? 234 GLU A OE1 1 ATOM 1859 O OE2 . GLU A 1 234 ? 17.453 -52.893 10.186 1.00 106.32 ? 234 GLU A OE2 1 ATOM 1860 N N . VAL A 1 235 ? 14.125 -49.285 7.439 1.00 71.67 ? 235 VAL A N 1 ATOM 1861 C CA . VAL A 1 235 ? 14.579 -48.664 6.182 1.00 69.30 ? 235 VAL A CA 1 ATOM 1862 C C . VAL A 1 235 ? 14.959 -47.206 6.405 1.00 68.23 ? 235 VAL A C 1 ATOM 1863 O O . VAL A 1 235 ? 16.037 -46.779 6.020 1.00 67.26 ? 235 VAL A O 1 ATOM 1864 C CB . VAL A 1 235 ? 13.505 -48.681 5.074 1.00 68.92 ? 235 VAL A CB 1 ATOM 1865 C CG1 . VAL A 1 235 ? 13.947 -47.858 3.878 1.00 63.74 ? 235 VAL A CG1 1 ATOM 1866 C CG2 . VAL A 1 235 ? 13.178 -50.095 4.647 1.00 70.02 ? 235 VAL A CG2 1 ATOM 1867 N N . ALA A 1 236 ? 14.073 -46.439 7.022 1.00 67.76 ? 236 ALA A N 1 ATOM 1868 C CA . ALA A 1 236 ? 14.398 -45.054 7.356 1.00 68.33 ? 236 ALA A CA 1 ATOM 1869 C C . ALA A 1 236 ? 15.742 -44.947 8.106 1.00 68.17 ? 236 ALA A C 1 ATOM 1870 O O . ALA A 1 236 ? 16.533 -44.051 7.833 1.00 68.17 ? 236 ALA A O 1 ATOM 1871 C CB . ALA A 1 236 ? 13.284 -44.431 8.171 1.00 68.00 ? 236 ALA A CB 1 ATOM 1872 N N . ARG A 1 237 ? 16.001 -45.864 9.036 1.00 68.70 ? 237 ARG A N 1 ATOM 1873 C CA . ARG A 1 237 ? 17.249 -45.853 9.794 1.00 69.05 ? 237 ARG A CA 1 ATOM 1874 C C . ARG A 1 237 ? 18.456 -46.170 8.920 1.00 66.66 ? 237 ARG A C 1 ATOM 1875 O O . ARG A 1 237 ? 19.521 -45.579 9.093 1.00 71.60 ? 237 ARG A O 1 ATOM 1876 C CB . ARG A 1 237 ? 17.190 -46.836 10.968 1.00 73.99 ? 237 ARG A CB 1 ATOM 1877 C CG . ARG A 1 237 ? 18.417 -46.802 11.876 1.00 79.34 ? 237 ARG A CG 1 ATOM 1878 C CD . ARG A 1 237 ? 18.502 -48.030 12.769 1.00 85.62 ? 237 ARG A CD 1 ATOM 1879 N NE . ARG A 1 237 ? 18.738 -49.268 12.016 1.00 89.34 ? 237 ARG A NE 1 ATOM 1880 C CZ . ARG A 1 237 ? 19.910 -49.662 11.508 1.00 87.32 ? 237 ARG A CZ 1 ATOM 1881 N NH1 . ARG A 1 237 ? 21.002 -48.919 11.640 1.00 84.56 ? 237 ARG A NH1 1 ATOM 1882 N NH2 . ARG A 1 237 ? 19.985 -50.816 10.857 1.00 86.00 ? 237 ARG A NH2 1 ATOM 1883 N N . ILE A 1 238 ? 18.309 -47.110 7.998 1.00 63.26 ? 238 ILE A N 1 ATOM 1884 C CA . ILE A 1 238 ? 19.439 -47.515 7.171 1.00 61.51 ? 238 ILE A CA 1 ATOM 1885 C C . ILE A 1 238 ? 19.805 -46.393 6.213 1.00 60.15 ? 238 ILE A C 1 ATOM 1886 O O . ILE A 1 238 ? 20.967 -45.992 6.103 1.00 62.65 ? 238 ILE A O 1 ATOM 1887 C CB . ILE A 1 238 ? 19.148 -48.797 6.375 1.00 60.53 ? 238 ILE A CB 1 ATOM 1888 C CG1 . ILE A 1 238 ? 18.930 -49.975 7.322 1.00 61.54 ? 238 ILE A CG1 1 ATOM 1889 C CG2 . ILE A 1 238 ? 20.321 -49.113 5.466 1.00 61.02 ? 238 ILE A CG2 1 ATOM 1890 C CD1 . ILE A 1 238 ? 18.443 -51.229 6.651 1.00 62.58 ? 238 ILE A CD1 1 ATOM 1891 N N . VAL A 1 239 ? 18.795 -45.862 5.556 1.00 58.34 ? 239 VAL A N 1 ATOM 1892 C CA . VAL A 1 239 ? 18.992 -44.852 4.542 1.00 61.62 ? 239 VAL A CA 1 ATOM 1893 C C . VAL A 1 239 ? 19.495 -43.541 5.121 1.00 62.91 ? 239 VAL A C 1 ATOM 1894 O O . VAL A 1 239 ? 20.495 -42.996 4.654 1.00 62.90 ? 239 VAL A O 1 ATOM 1895 C CB . VAL A 1 239 ? 17.683 -44.605 3.764 1.00 63.62 ? 239 VAL A CB 1 ATOM 1896 C CG1 . VAL A 1 239 ? 17.814 -43.396 2.846 1.00 65.06 ? 239 VAL A CG1 1 ATOM 1897 C CG2 . VAL A 1 239 ? 17.334 -45.842 2.958 1.00 64.14 ? 239 VAL A CG2 1 ATOM 1898 N N . GLY A 1 240 ? 18.803 -43.051 6.142 1.00 63.44 ? 240 GLY A N 1 ATOM 1899 C CA . GLY A 1 240 ? 18.987 -41.687 6.611 1.00 65.28 ? 240 GLY A CA 1 ATOM 1900 C C . GLY A 1 240 ? 19.837 -41.530 7.849 1.00 64.70 ? 240 GLY A C 1 ATOM 1901 O O . GLY A 1 240 ? 20.321 -40.438 8.119 1.00 62.89 ? 240 GLY A O 1 ATOM 1902 N N . ASN A 1 241 ? 20.018 -42.594 8.613 1.00 65.70 ? 241 ASN A N 1 ATOM 1903 C CA . ASN A 1 241 ? 20.521 -42.423 9.964 1.00 69.48 ? 241 ASN A CA 1 ATOM 1904 C C . ASN A 1 241 ? 21.556 -43.436 10.394 1.00 67.81 ? 241 ASN A C 1 ATOM 1905 O O . ASN A 1 241 ? 21.583 -43.832 11.552 1.00 78.87 ? 241 ASN A O 1 ATOM 1906 C CB . ASN A 1 241 ? 19.348 -42.420 10.957 1.00 72.39 ? 241 ASN A CB 1 ATOM 1907 C CG . ASN A 1 241 ? 19.609 -41.520 12.161 1.00 78.39 ? 241 ASN A CG 1 ATOM 1908 O OD1 . ASN A 1 241 ? 19.923 -41.997 13.260 1.00 74.08 ? 241 ASN A OD1 1 ATOM 1909 N ND2 . ASN A 1 241 ? 19.510 -40.205 11.949 1.00 79.76 ? 241 ASN A ND2 1 ATOM 1910 N N . SER A 1 242 ? 22.416 -43.852 9.482 1.00 64.88 ? 242 SER A N 1 ATOM 1911 C CA . SER A 1 242 ? 23.369 -44.905 9.787 1.00 66.10 ? 242 SER A CA 1 ATOM 1912 C C . SER A 1 242 ? 24.734 -44.760 9.127 1.00 67.47 ? 242 SER A C 1 ATOM 1913 O O . SER A 1 242 ? 25.487 -45.733 9.115 1.00 68.36 ? 242 SER A O 1 ATOM 1914 C CB . SER A 1 242 ? 22.780 -46.249 9.370 1.00 68.36 ? 242 SER A CB 1 ATOM 1915 O OG . SER A 1 242 ? 23.005 -46.497 7.993 1.00 70.99 ? 242 SER A OG 1 ATOM 1916 N N . GLY A 1 243 ? 25.048 -43.586 8.573 1.00 65.50 ? 243 GLY A N 1 ATOM 1917 C CA . GLY A 1 243 ? 26.372 -43.316 8.020 1.00 66.23 ? 243 GLY A CA 1 ATOM 1918 C C . GLY A 1 243 ? 26.487 -43.093 6.515 1.00 69.25 ? 243 GLY A C 1 ATOM 1919 O O . GLY A 1 243 ? 27.517 -42.598 6.033 1.00 72.61 ? 243 GLY A O 1 ATOM 1920 N N . LEU A 1 244 ? 25.452 -43.450 5.761 1.00 68.22 ? 244 LEU A N 1 ATOM 1921 C CA . LEU A 1 244 ? 25.459 -43.234 4.314 1.00 63.69 ? 244 LEU A CA 1 ATOM 1922 C C . LEU A 1 244 ? 25.235 -41.772 3.983 1.00 64.41 ? 244 LEU A C 1 ATOM 1923 O O . LEU A 1 244 ? 24.687 -41.017 4.785 1.00 63.97 ? 244 LEU A O 1 ATOM 1924 C CB . LEU A 1 244 ? 24.359 -44.039 3.644 1.00 62.07 ? 244 LEU A CB 1 ATOM 1925 C CG . LEU A 1 244 ? 24.466 -45.543 3.761 1.00 57.47 ? 244 LEU A CG 1 ATOM 1926 C CD1 . LEU A 1 244 ? 23.226 -46.176 3.183 1.00 57.26 ? 244 LEU A CD1 1 ATOM 1927 C CD2 . LEU A 1 244 ? 25.696 -46.028 3.045 1.00 56.19 ? 244 LEU A CD2 1 ATOM 1928 N N . ASN A 1 245 ? 25.660 -41.380 2.793 1.00 64.58 ? 245 ASN A N 1 ATOM 1929 C CA . ASN A 1 245 ? 25.425 -40.037 2.338 1.00 63.11 ? 245 ASN A CA 1 ATOM 1930 C C . ASN A 1 245 ? 24.134 -39.982 1.541 1.00 64.39 ? 245 ASN A C 1 ATOM 1931 O O . ASN A 1 245 ? 24.100 -40.343 0.359 1.00 63.35 ? 245 ASN A O 1 ATOM 1932 C CB . ASN A 1 245 ? 26.584 -39.535 1.515 1.00 61.17 ? 245 ASN A CB 1 ATOM 1933 C CG . ASN A 1 245 ? 26.481 -38.062 1.238 1.00 59.65 ? 245 ASN A CG 1 ATOM 1934 O OD1 . ASN A 1 245 ? 25.393 -37.487 1.265 1.00 55.15 ? 245 ASN A OD1 1 ATOM 1935 N ND2 . ASN A 1 245 ? 27.613 -37.433 0.999 1.00 60.42 ? 245 ASN A ND2 1 ATOM 1936 N N . ILE A 1 246 ? 23.074 -39.519 2.207 1.00 62.75 ? 246 ILE A N 1 ATOM 1937 C CA . ILE A 1 246 ? 21.733 -39.504 1.635 1.00 60.47 ? 246 ILE A CA 1 ATOM 1938 C C . ILE A 1 246 ? 21.652 -38.657 0.355 1.00 62.05 ? 246 ILE A C 1 ATOM 1939 O O . ILE A 1 246 ? 20.837 -38.930 -0.528 1.00 62.05 ? 246 ILE A O 1 ATOM 1940 C CB . ILE A 1 246 ? 20.697 -39.053 2.685 1.00 58.62 ? 246 ILE A CB 1 ATOM 1941 C CG1 . ILE A 1 246 ? 19.288 -39.392 2.227 1.00 60.70 ? 246 ILE A CG1 1 ATOM 1942 C CG2 . ILE A 1 246 ? 20.803 -37.574 2.980 1.00 58.17 ? 246 ILE A CG2 1 ATOM 1943 C CD1 . ILE A 1 246 ? 18.263 -39.271 3.329 1.00 62.71 ? 246 ILE A CD1 1 ATOM 1944 N N . TYR A 1 247 ? 22.511 -37.651 0.262 1.00 62.81 ? 247 TYR A N 1 ATOM 1945 C CA . TYR A 1 247 ? 22.578 -36.784 -0.904 1.00 66.24 ? 247 TYR A CA 1 ATOM 1946 C C . TYR A 1 247 ? 23.288 -37.489 -2.070 1.00 65.61 ? 247 TYR A C 1 ATOM 1947 O O . TYR A 1 247 ? 23.056 -37.177 -3.242 1.00 66.74 ? 247 TYR A O 1 ATOM 1948 C CB . TYR A 1 247 ? 23.326 -35.491 -0.548 1.00 71.44 ? 247 TYR A CB 1 ATOM 1949 C CG . TYR A 1 247 ? 22.500 -34.353 0.039 1.00 78.40 ? 247 TYR A CG 1 ATOM 1950 C CD1 . TYR A 1 247 ? 21.369 -34.585 0.843 1.00 76.70 ? 247 TYR A CD1 1 ATOM 1951 C CD2 . TYR A 1 247 ? 22.881 -33.029 -0.196 1.00 83.30 ? 247 TYR A CD2 1 ATOM 1952 C CE1 . TYR A 1 247 ? 20.639 -33.530 1.371 1.00 79.14 ? 247 TYR A CE1 1 ATOM 1953 C CE2 . TYR A 1 247 ? 22.154 -31.969 0.320 1.00 90.56 ? 247 TYR A CE2 1 ATOM 1954 C CZ . TYR A 1 247 ? 21.039 -32.216 1.100 1.00 88.72 ? 247 TYR A CZ 1 ATOM 1955 O OH . TYR A 1 247 ? 20.351 -31.120 1.579 1.00 90.72 ? 247 TYR A OH 1 ATOM 1956 N N . ASN A 1 248 ? 24.175 -38.415 -1.747 1.00 62.55 ? 248 ASN A N 1 ATOM 1957 C CA . ASN A 1 248 ? 24.959 -39.105 -2.762 1.00 59.56 ? 248 ASN A CA 1 ATOM 1958 C C . ASN A 1 248 ? 25.529 -40.381 -2.167 1.00 59.21 ? 248 ASN A C 1 ATOM 1959 O O . ASN A 1 248 ? 26.547 -40.363 -1.482 1.00 59.92 ? 248 ASN A O 1 ATOM 1960 C CB . ASN A 1 248 ? 26.080 -38.204 -3.284 1.00 58.22 ? 248 ASN A CB 1 ATOM 1961 C CG . ASN A 1 248 ? 27.029 -38.923 -4.234 1.00 57.68 ? 248 ASN A CG 1 ATOM 1962 O OD1 . ASN A 1 248 ? 26.936 -40.124 -4.460 1.00 57.33 ? 248 ASN A OD1 1 ATOM 1963 N ND2 . ASN A 1 248 ? 27.952 -38.175 -4.796 1.00 59.43 ? 248 ASN A ND2 1 ATOM 1964 N N . LEU A 1 249 ? 24.869 -41.486 -2.476 1.00 55.38 ? 249 LEU A N 1 ATOM 1965 C CA . LEU A 1 249 ? 25.166 -42.787 -1.895 1.00 53.70 ? 249 LEU A CA 1 ATOM 1966 C C . LEU A 1 249 ? 26.577 -43.296 -2.052 1.00 52.69 ? 249 LEU A C 1 ATOM 1967 O O . LEU A 1 249 ? 27.013 -44.087 -1.235 1.00 56.79 ? 249 LEU A O 1 ATOM 1968 C CB . LEU A 1 249 ? 24.231 -43.834 -2.504 1.00 53.29 ? 249 LEU A CB 1 ATOM 1969 C CG . LEU A 1 249 ? 24.425 -45.296 -2.125 1.00 52.07 ? 249 LEU A CG 1 ATOM 1970 C CD1 . LEU A 1 249 ? 24.209 -45.501 -0.636 1.00 53.48 ? 249 LEU A CD1 1 ATOM 1971 C CD2 . LEU A 1 249 ? 23.449 -46.135 -2.919 1.00 54.52 ? 249 LEU A CD2 1 ATOM 1972 N N . TYR A 1 250 ? 27.277 -42.883 -3.098 1.00 52.44 ? 250 TYR A N 1 ATOM 1973 C CA . TYR A 1 250 ? 28.629 -43.388 -3.352 1.00 54.94 ? 250 TYR A CA 1 ATOM 1974 C C . TYR A 1 250 ? 29.725 -42.441 -2.884 1.00 53.34 ? 250 TYR A C 1 ATOM 1975 O O . TYR A 1 250 ? 30.912 -42.703 -3.112 1.00 52.55 ? 250 TYR A O 1 ATOM 1976 C CB . TYR A 1 250 ? 28.782 -43.752 -4.831 1.00 56.05 ? 250 TYR A CB 1 ATOM 1977 C CG . TYR A 1 250 ? 27.814 -44.813 -5.183 1.00 54.65 ? 250 TYR A CG 1 ATOM 1978 C CD1 . TYR A 1 250 ? 27.965 -46.083 -4.675 1.00 57.19 ? 250 TYR A CD1 1 ATOM 1979 C CD2 . TYR A 1 250 ? 26.706 -44.537 -5.971 1.00 55.93 ? 250 TYR A CD2 1 ATOM 1980 C CE1 . TYR A 1 250 ? 27.044 -47.077 -4.958 1.00 61.85 ? 250 TYR A CE1 1 ATOM 1981 C CE2 . TYR A 1 250 ? 25.778 -45.515 -6.261 1.00 58.64 ? 250 TYR A CE2 1 ATOM 1982 C CZ . TYR A 1 250 ? 25.953 -46.780 -5.748 1.00 59.48 ? 250 TYR A CZ 1 ATOM 1983 O OH . TYR A 1 250 ? 25.048 -47.753 -6.021 1.00 64.83 ? 250 TYR A OH 1 ATOM 1984 N N . ALA A 1 251 ? 29.306 -41.365 -2.221 1.00 51.58 ? 251 ALA A N 1 ATOM 1985 C CA . ALA A 1 251 ? 30.206 -40.387 -1.634 1.00 54.57 ? 251 ALA A CA 1 ATOM 1986 C C . ALA A 1 251 ? 30.361 -40.598 -0.130 1.00 59.48 ? 251 ALA A C 1 ATOM 1987 O O . ALA A 1 251 ? 29.413 -40.993 0.551 1.00 61.22 ? 251 ALA A O 1 ATOM 1988 C CB . ALA A 1 251 ? 29.686 -38.993 -1.887 1.00 52.96 ? 251 ALA A CB 1 ATOM 1989 N N . PRO A 1 252 ? 31.555 -40.296 0.409 1.00 63.91 ? 252 PRO A N 1 ATOM 1990 C CA . PRO A 1 252 ? 31.741 -40.367 1.861 1.00 64.69 ? 252 PRO A CA 1 ATOM 1991 C C . PRO A 1 252 ? 30.905 -39.317 2.568 1.00 66.07 ? 252 PRO A C 1 ATOM 1992 O O . PRO A 1 252 ? 30.605 -38.282 1.989 1.00 62.24 ? 252 PRO A O 1 ATOM 1993 C CB . PRO A 1 252 ? 33.216 -40.038 2.033 1.00 65.87 ? 252 PRO A CB 1 ATOM 1994 C CG . PRO A 1 252 ? 33.526 -39.135 0.884 1.00 64.02 ? 252 PRO A CG 1 ATOM 1995 C CD . PRO A 1 252 ? 32.705 -39.661 -0.261 1.00 62.95 ? 252 PRO A CD 1 ATOM 1996 N N . CYS A 1 253 ? 30.528 -39.595 3.808 1.00 71.71 ? 253 CYS A N 1 ATOM 1997 C CA . CYS A 1 253 ? 29.737 -38.666 4.603 1.00 74.49 ? 253 CYS A CA 1 ATOM 1998 C C . CYS A 1 253 ? 30.680 -37.719 5.302 1.00 73.82 ? 253 CYS A C 1 ATOM 1999 O O . CYS A 1 253 ? 31.503 -38.150 6.087 1.00 72.95 ? 253 CYS A O 1 ATOM 2000 C CB . CYS A 1 253 ? 28.886 -39.428 5.629 1.00 77.71 ? 253 CYS A CB 1 ATOM 2001 S SG . CYS A 1 253 ? 27.876 -38.378 6.696 1.00 81.89 ? 253 CYS A SG 1 ATOM 2002 N N . ALA A 1 254 ? 30.556 -36.433 5.014 1.00 74.90 ? 254 ALA A N 1 ATOM 2003 C CA . ALA A 1 254 ? 31.391 -35.423 5.646 1.00 79.36 ? 254 ALA A CA 1 ATOM 2004 C C . ALA A 1 254 ? 31.460 -35.562 7.188 1.00 84.93 ? 254 ALA A C 1 ATOM 2005 O O . ALA A 1 254 ? 30.453 -35.431 7.888 1.00 80.02 ? 254 ALA A O 1 ATOM 2006 C CB . ALA A 1 254 ? 30.891 -34.042 5.276 1.00 79.08 ? 254 ALA A CB 1 ATOM 2007 N N . GLY A 1 255 ? 32.654 -35.828 7.706 1.00 89.02 ? 255 GLY A N 1 ATOM 2008 C CA . GLY A 1 255 ? 32.884 -35.816 9.151 1.00 93.92 ? 255 GLY A CA 1 ATOM 2009 C C . GLY A 1 255 ? 32.468 -37.080 9.872 1.00 95.61 ? 255 GLY A C 1 ATOM 2010 O O . GLY A 1 255 ? 31.815 -37.022 10.921 1.00 98.95 ? 255 GLY A O 1 ATOM 2011 N N . GLY A 1 256 ? 32.862 -38.222 9.312 1.00 91.18 ? 256 GLY A N 1 ATOM 2012 C CA . GLY A 1 256 ? 32.742 -39.511 9.987 1.00 91.01 ? 256 GLY A CA 1 ATOM 2013 C C . GLY A 1 256 ? 31.327 -40.009 10.189 1.00 91.11 ? 256 GLY A C 1 ATOM 2014 O O . GLY A 1 256 ? 30.364 -39.333 9.837 1.00 94.44 ? 256 GLY A O 1 ATOM 2015 N N . VAL A 1 257 ? 31.206 -41.199 10.761 1.00 91.41 ? 257 VAL A N 1 ATOM 2016 C CA . VAL A 1 257 ? 29.905 -41.824 10.951 1.00 97.00 ? 257 VAL A CA 1 ATOM 2017 C C . VAL A 1 257 ? 29.454 -41.710 12.429 1.00 108.61 ? 257 VAL A C 1 ATOM 2018 O O . VAL A 1 257 ? 30.081 -42.274 13.327 1.00 104.26 ? 257 VAL A O 1 ATOM 2019 C CB . VAL A 1 257 ? 29.874 -43.273 10.398 1.00 90.02 ? 257 VAL A CB 1 ATOM 2020 C CG1 . VAL A 1 257 ? 30.060 -43.249 8.894 1.00 83.45 ? 257 VAL A CG1 1 ATOM 2021 C CG2 . VAL A 1 257 ? 30.926 -44.166 11.033 1.00 92.87 ? 257 VAL A CG2 1 ATOM 2022 N N . PRO A 1 258 ? 28.371 -40.950 12.682 1.00 125.58 ? 258 PRO A N 1 ATOM 2023 C CA . PRO A 1 258 ? 27.952 -40.595 14.047 1.00 135.01 ? 258 PRO A CA 1 ATOM 2024 C C . PRO A 1 258 ? 28.001 -41.734 15.067 1.00 135.36 ? 258 PRO A C 1 ATOM 2025 O O . PRO A 1 258 ? 27.736 -42.880 14.722 1.00 137.90 ? 258 PRO A O 1 ATOM 2026 C CB . PRO A 1 258 ? 26.513 -40.110 13.851 1.00 134.74 ? 258 PRO A CB 1 ATOM 2027 C CG . PRO A 1 258 ? 26.503 -39.538 12.475 1.00 131.39 ? 258 PRO A CG 1 ATOM 2028 C CD . PRO A 1 258 ? 27.487 -40.340 11.668 1.00 128.75 ? 258 PRO A CD 1 ATOM 2029 N N . ARG A 1 268 ? 23.158 -25.418 15.478 1.00 103.34 ? 298 ARG A N 1 ATOM 2030 C CA . ARG A 1 268 ? 23.054 -25.065 14.066 1.00 98.94 ? 298 ARG A CA 1 ATOM 2031 C C . ARG A 1 268 ? 22.696 -26.278 13.222 1.00 93.92 ? 298 ARG A C 1 ATOM 2032 O O . ARG A 1 268 ? 23.222 -27.356 13.435 1.00 96.78 ? 298 ARG A O 1 ATOM 2033 C CB . ARG A 1 268 ? 24.369 -24.464 13.570 1.00 98.13 ? 298 ARG A CB 1 ATOM 2034 C CG . ARG A 1 268 ? 24.284 -23.900 12.161 1.00 95.51 ? 298 ARG A CG 1 ATOM 2035 C CD . ARG A 1 268 ? 25.519 -23.109 11.769 1.00 93.77 ? 298 ARG A CD 1 ATOM 2036 N NE . ARG A 1 268 ? 26.473 -23.890 10.991 1.00 93.93 ? 298 ARG A NE 1 ATOM 2037 C CZ . ARG A 1 268 ? 27.548 -24.515 11.467 1.00 100.58 ? 298 ARG A CZ 1 ATOM 2038 N NH1 . ARG A 1 268 ? 27.853 -24.472 12.760 1.00 108.95 ? 298 ARG A NH1 1 ATOM 2039 N NH2 . ARG A 1 268 ? 28.335 -25.193 10.635 1.00 100.55 ? 298 ARG A NH2 1 ATOM 2040 N N . MET A 1 269 ? 21.796 -26.088 12.261 1.00 98.81 ? 299 MET A N 1 ATOM 2041 C CA . MET A 1 269 ? 21.403 -27.151 11.337 1.00 95.45 ? 299 MET A CA 1 ATOM 2042 C C . MET A 1 269 ? 22.161 -27.002 10.035 1.00 90.21 ? 299 MET A C 1 ATOM 2043 O O . MET A 1 269 ? 21.898 -26.094 9.252 1.00 82.39 ? 299 MET A O 1 ATOM 2044 C CB . MET A 1 269 ? 19.891 -27.130 11.051 1.00 96.52 ? 299 MET A CB 1 ATOM 2045 C CG . MET A 1 269 ? 19.455 -28.057 9.910 1.00 98.06 ? 299 MET A CG 1 ATOM 2046 S SD . MET A 1 269 ? 17.692 -28.013 9.499 1.00 96.67 ? 299 MET A SD 1 ATOM 2047 C CE . MET A 1 269 ? 17.145 -29.472 10.381 1.00 97.56 ? 299 MET A CE 1 ATOM 2048 N N . ASP A 1 270 ? 23.111 -27.899 9.817 1.00 89.20 ? 300 ASP A N 1 ATOM 2049 C CA . ASP A 1 270 ? 23.660 -28.102 8.498 1.00 85.75 ? 300 ASP A CA 1 ATOM 2050 C C . ASP A 1 270 ? 22.772 -29.142 7.851 1.00 81.95 ? 300 ASP A C 1 ATOM 2051 O O . ASP A 1 270 ? 22.044 -29.838 8.548 1.00 79.51 ? 300 ASP A O 1 ATOM 2052 C CB . ASP A 1 270 ? 25.101 -28.611 8.563 1.00 85.63 ? 300 ASP A CB 1 ATOM 2053 C CG . ASP A 1 270 ? 26.057 -27.581 9.133 1.00 89.24 ? 300 ASP A CG 1 ATOM 2054 O OD1 . ASP A 1 270 ? 25.675 -26.868 10.079 1.00 93.50 ? 300 ASP A OD1 1 ATOM 2055 O OD2 . ASP A 1 270 ? 27.195 -27.484 8.636 1.00 93.86 ? 300 ASP A OD2 1 ATOM 2056 N N . PRO A 1 271 ? 22.807 -29.236 6.514 1.00 79.72 ? 301 PRO A N 1 ATOM 2057 C CA . PRO A 1 271 ? 22.287 -30.425 5.871 1.00 78.18 ? 301 PRO A CA 1 ATOM 2058 C C . PRO A 1 271 ? 23.137 -31.618 6.291 1.00 77.81 ? 301 PRO A C 1 ATOM 2059 O O . PRO A 1 271 ? 24.315 -31.437 6.581 1.00 80.98 ? 301 PRO A O 1 ATOM 2060 C CB . PRO A 1 271 ? 22.484 -30.139 4.375 1.00 79.98 ? 301 PRO A CB 1 ATOM 2061 C CG . PRO A 1 271 ? 22.764 -28.685 4.261 1.00 77.37 ? 301 PRO A CG 1 ATOM 2062 C CD . PRO A 1 271 ? 23.374 -28.277 5.552 1.00 77.38 ? 301 PRO A CD 1 ATOM 2063 N N . PRO A 1 272 ? 22.569 -32.828 6.303 1.00 79.39 ? 302 PRO A N 1 ATOM 2064 C CA . PRO A 1 272 ? 23.356 -33.960 6.785 1.00 84.09 ? 302 PRO A CA 1 ATOM 2065 C C . PRO A 1 272 ? 24.439 -34.394 5.798 1.00 82.77 ? 302 PRO A C 1 ATOM 2066 O O . PRO A 1 272 ? 24.284 -34.231 4.582 1.00 77.73 ? 302 PRO A O 1 ATOM 2067 C CB . PRO A 1 272 ? 22.313 -35.076 6.980 1.00 82.79 ? 302 PRO A CB 1 ATOM 2068 C CG . PRO A 1 272 ? 21.068 -34.614 6.294 1.00 83.21 ? 302 PRO A CG 1 ATOM 2069 C CD . PRO A 1 272 ? 21.330 -33.275 5.653 1.00 82.92 ? 302 PRO A CD 1 ATOM 2070 N N . CYS A 1 273 ? 25.519 -34.941 6.346 1.00 80.60 ? 303 CYS A N 1 ATOM 2071 C CA . CYS A 1 273 ? 26.698 -35.356 5.582 1.00 80.92 ? 303 CYS A CA 1 ATOM 2072 C C . CYS A 1 273 ? 27.321 -34.239 4.744 1.00 79.23 ? 303 CYS A C 1 ATOM 2073 O O . CYS A 1 273 ? 28.078 -34.517 3.816 1.00 83.51 ? 303 CYS A O 1 ATOM 2074 C CB . CYS A 1 273 ? 26.386 -36.583 4.711 1.00 79.94 ? 303 CYS A CB 1 ATOM 2075 S SG . CYS A 1 273 ? 26.119 -38.087 5.676 1.00 83.74 ? 303 CYS A SG 1 ATOM 2076 N N . THR A 1 274 ? 27.033 -32.990 5.095 1.00 75.85 ? 304 THR A N 1 ATOM 2077 C CA . THR A 1 274 ? 27.479 -31.836 4.326 1.00 75.66 ? 304 THR A CA 1 ATOM 2078 C C . THR A 1 274 ? 28.380 -30.930 5.165 1.00 72.22 ? 304 THR A C 1 ATOM 2079 O O . THR A 1 274 ? 28.004 -30.524 6.257 1.00 71.89 ? 304 THR A O 1 ATOM 2080 C CB . THR A 1 274 ? 26.267 -31.016 3.818 1.00 78.66 ? 304 THR A CB 1 ATOM 2081 O OG1 . THR A 1 274 ? 25.229 -31.899 3.399 1.00 77.06 ? 304 THR A OG1 1 ATOM 2082 C CG2 . THR A 1 274 ? 26.652 -30.113 2.639 1.00 80.96 ? 304 THR A CG2 1 ATOM 2083 N N . ASN A 1 275 ? 29.571 -30.621 4.657 1.00 73.92 ? 305 ASN A N 1 ATOM 2084 C CA . ASN A 1 275 ? 30.452 -29.615 5.271 1.00 74.20 ? 305 ASN A CA 1 ATOM 2085 C C . ASN A 1 275 ? 30.110 -28.236 4.710 1.00 71.56 ? 305 ASN A C 1 ATOM 2086 O O . ASN A 1 275 ? 30.196 -28.022 3.505 1.00 68.02 ? 305 ASN A O 1 ATOM 2087 C CB . ASN A 1 275 ? 31.913 -29.955 4.982 1.00 74.25 ? 305 ASN A CB 1 ATOM 2088 C CG . ASN A 1 275 ? 32.890 -29.104 5.754 1.00 77.65 ? 305 ASN A CG 1 ATOM 2089 O OD1 . ASN A 1 275 ? 32.523 -28.112 6.379 1.00 84.14 ? 305 ASN A OD1 1 ATOM 2090 N ND2 . ASN A 1 275 ? 34.165 -29.498 5.709 1.00 81.49 ? 305 ASN A ND2 1 ATOM 2091 N N . THR A 1 276 ? 29.702 -27.316 5.579 1.00 71.37 ? 306 THR A N 1 ATOM 2092 C CA . THR A 1 276 ? 29.316 -25.967 5.154 1.00 72.54 ? 306 THR A CA 1 ATOM 2093 C C . THR A 1 276 ? 30.326 -24.926 5.624 1.00 75.65 ? 306 THR A C 1 ATOM 2094 O O . THR A 1 276 ? 30.032 -23.731 5.648 1.00 73.47 ? 306 THR A O 1 ATOM 2095 C CB . THR A 1 276 ? 27.911 -25.575 5.679 1.00 70.25 ? 306 THR A CB 1 ATOM 2096 O OG1 . THR A 1 276 ? 27.965 -25.314 7.085 1.00 70.64 ? 306 THR A OG1 1 ATOM 2097 C CG2 . THR A 1 276 ? 26.910 -26.682 5.429 1.00 70.63 ? 306 THR A CG2 1 ATOM 2098 N N . THR A 1 277 ? 31.522 -25.374 5.986 1.00 76.11 ? 307 THR A N 1 ATOM 2099 C CA . THR A 1 277 ? 32.516 -24.472 6.531 1.00 76.77 ? 307 THR A CA 1 ATOM 2100 C C . THR A 1 277 ? 32.985 -23.486 5.477 1.00 75.01 ? 307 THR A C 1 ATOM 2101 O O . THR A 1 277 ? 32.951 -22.280 5.699 1.00 80.05 ? 307 THR A O 1 ATOM 2102 C CB . THR A 1 277 ? 33.715 -25.244 7.091 1.00 80.14 ? 307 THR A CB 1 ATOM 2103 O OG1 . THR A 1 277 ? 33.236 -26.259 7.971 1.00 80.77 ? 307 THR A OG1 1 ATOM 2104 C CG2 . THR A 1 277 ? 34.655 -24.314 7.859 1.00 82.06 ? 307 THR A CG2 1 ATOM 2105 N N . ALA A 1 278 ? 33.405 -23.995 4.327 1.00 72.08 ? 308 ALA A N 1 ATOM 2106 C CA . ALA A 1 278 ? 33.958 -23.150 3.272 1.00 71.32 ? 308 ALA A CA 1 ATOM 2107 C C . ALA A 1 278 ? 33.103 -21.914 3.002 1.00 70.83 ? 308 ALA A C 1 ATOM 2108 O O . ALA A 1 278 ? 33.593 -20.803 3.026 1.00 69.30 ? 308 ALA A O 1 ATOM 2109 C CB . ALA A 1 278 ? 34.134 -23.953 1.996 1.00 70.89 ? 308 ALA A CB 1 ATOM 2110 N N . ALA A 1 279 ? 31.818 -22.118 2.761 1.00 74.51 ? 309 ALA A N 1 ATOM 2111 C CA . ALA A 1 279 ? 30.917 -21.030 2.381 1.00 73.56 ? 309 ALA A CA 1 ATOM 2112 C C . ALA A 1 279 ? 30.629 -20.100 3.539 1.00 73.99 ? 309 ALA A C 1 ATOM 2113 O O . ALA A 1 279 ? 30.616 -18.880 3.365 1.00 74.37 ? 309 ALA A O 1 ATOM 2114 C CB . ALA A 1 279 ? 29.616 -21.586 1.827 1.00 73.83 ? 309 ALA A CB 1 ATOM 2115 N N . SER A 1 280 ? 30.390 -20.676 4.714 1.00 75.30 ? 310 SER A N 1 ATOM 2116 C CA . SER A 1 280 ? 30.102 -19.895 5.920 1.00 74.89 ? 310 SER A CA 1 ATOM 2117 C C . SER A 1 280 ? 31.271 -18.999 6.291 1.00 73.12 ? 310 SER A C 1 ATOM 2118 O O . SER A 1 280 ? 31.103 -17.790 6.480 1.00 73.10 ? 310 SER A O 1 ATOM 2119 C CB . SER A 1 280 ? 29.774 -20.804 7.094 1.00 75.47 ? 310 SER A CB 1 ATOM 2120 O OG . SER A 1 280 ? 29.222 -20.045 8.155 1.00 80.70 ? 310 SER A OG 1 ATOM 2121 N N . THR A 1 281 ? 32.453 -19.594 6.374 1.00 70.65 ? 311 THR A N 1 ATOM 2122 C CA . THR A 1 281 ? 33.663 -18.838 6.606 1.00 71.14 ? 311 THR A CA 1 ATOM 2123 C C . THR A 1 281 ? 33.720 -17.647 5.676 1.00 74.03 ? 311 THR A C 1 ATOM 2124 O O . THR A 1 281 ? 34.018 -16.533 6.104 1.00 77.27 ? 311 THR A O 1 ATOM 2125 C CB . THR A 1 281 ? 34.903 -19.702 6.395 1.00 72.53 ? 311 THR A CB 1 ATOM 2126 O OG1 . THR A 1 281 ? 34.905 -20.753 7.365 1.00 75.25 ? 311 THR A OG1 1 ATOM 2127 C CG2 . THR A 1 281 ? 36.185 -18.878 6.538 1.00 73.12 ? 311 THR A CG2 1 ATOM 2128 N N . TYR A 1 282 ? 33.400 -17.868 4.408 1.00 76.40 ? 312 TYR A N 1 ATOM 2129 C CA . TYR A 1 282 ? 33.520 -16.812 3.425 1.00 77.90 ? 312 TYR A CA 1 ATOM 2130 C C . TYR A 1 282 ? 32.502 -15.719 3.666 1.00 78.94 ? 312 TYR A C 1 ATOM 2131 O O . TYR A 1 282 ? 32.872 -14.563 3.824 1.00 80.05 ? 312 TYR A O 1 ATOM 2132 C CB . TYR A 1 282 ? 33.370 -17.345 2.006 1.00 78.21 ? 312 TYR A CB 1 ATOM 2133 C CG . TYR A 1 282 ? 33.450 -16.238 0.996 1.00 77.15 ? 312 TYR A CG 1 ATOM 2134 C CD1 . TYR A 1 282 ? 34.667 -15.741 0.585 1.00 77.86 ? 312 TYR A CD1 1 ATOM 2135 C CD2 . TYR A 1 282 ? 32.306 -15.667 0.488 1.00 77.51 ? 312 TYR A CD2 1 ATOM 2136 C CE1 . TYR A 1 282 ? 34.742 -14.712 -0.323 1.00 79.25 ? 312 TYR A CE1 1 ATOM 2137 C CE2 . TYR A 1 282 ? 32.368 -14.636 -0.421 1.00 77.87 ? 312 TYR A CE2 1 ATOM 2138 C CZ . TYR A 1 282 ? 33.584 -14.158 -0.822 1.00 77.99 ? 312 TYR A CZ 1 ATOM 2139 O OH . TYR A 1 282 ? 33.622 -13.115 -1.718 1.00 78.97 ? 312 TYR A OH 1 ATOM 2140 N N . LEU A 1 283 ? 31.225 -16.085 3.692 1.00 77.70 ? 313 LEU A N 1 ATOM 2141 C CA . LEU A 1 283 ? 30.139 -15.096 3.784 1.00 74.28 ? 313 LEU A CA 1 ATOM 2142 C C . LEU A 1 283 ? 30.039 -14.335 5.120 1.00 75.22 ? 313 LEU A C 1 ATOM 2143 O O . LEU A 1 283 ? 29.412 -13.279 5.176 1.00 74.30 ? 313 LEU A O 1 ATOM 2144 C CB . LEU A 1 283 ? 28.799 -15.758 3.481 1.00 72.02 ? 313 LEU A CB 1 ATOM 2145 C CG . LEU A 1 283 ? 28.612 -16.234 2.041 1.00 70.38 ? 313 LEU A CG 1 ATOM 2146 C CD1 . LEU A 1 283 ? 27.425 -17.179 1.941 1.00 67.07 ? 313 LEU A CD1 1 ATOM 2147 C CD2 . LEU A 1 283 ? 28.452 -15.044 1.109 1.00 70.54 ? 313 LEU A CD2 1 ATOM 2148 N N . ASN A 1 284 ? 30.623 -14.869 6.189 1.00 76.10 ? 314 ASN A N 1 ATOM 2149 C CA . ASN A 1 284 ? 30.645 -14.170 7.479 1.00 74.80 ? 314 ASN A CA 1 ATOM 2150 C C . ASN A 1 284 ? 31.785 -13.175 7.615 1.00 75.78 ? 314 ASN A C 1 ATOM 2151 O O . ASN A 1 284 ? 31.790 -12.366 8.537 1.00 77.56 ? 314 ASN A O 1 ATOM 2152 C CB . ASN A 1 284 ? 30.689 -15.174 8.621 1.00 75.19 ? 314 ASN A CB 1 ATOM 2153 C CG . ASN A 1 284 ? 29.371 -15.887 8.803 1.00 73.57 ? 314 ASN A CG 1 ATOM 2154 O OD1 . ASN A 1 284 ? 28.366 -15.258 9.117 1.00 71.93 ? 314 ASN A OD1 1 ATOM 2155 N ND2 . ASN A 1 284 ? 29.362 -17.199 8.599 1.00 72.38 ? 314 ASN A ND2 1 ATOM 2156 N N . ASN A 1 285 ? 32.749 -13.240 6.703 1.00 80.48 ? 315 ASN A N 1 ATOM 2157 C CA . ASN A 1 285 ? 33.776 -12.208 6.594 1.00 81.38 ? 315 ASN A CA 1 ATOM 2158 C C . ASN A 1 285 ? 33.115 -10.839 6.527 1.00 81.27 ? 315 ASN A C 1 ATOM 2159 O O . ASN A 1 285 ? 32.394 -10.555 5.578 1.00 80.25 ? 315 ASN A O 1 ATOM 2160 C CB . ASN A 1 285 ? 34.625 -12.431 5.340 1.00 82.78 ? 315 ASN A CB 1 ATOM 2161 C CG . ASN A 1 285 ? 35.682 -11.363 5.143 1.00 85.21 ? 315 ASN A CG 1 ATOM 2162 O OD1 . ASN A 1 285 ? 35.715 -10.368 5.857 1.00 85.27 ? 315 ASN A OD1 1 ATOM 2163 N ND2 . ASN A 1 285 ? 36.558 -11.572 4.167 1.00 85.83 ? 315 ASN A ND2 1 ATOM 2164 N N . PRO A 1 286 ? 33.362 -9.980 7.527 1.00 84.75 ? 316 PRO A N 1 ATOM 2165 C CA . PRO A 1 286 ? 32.707 -8.664 7.557 1.00 85.96 ? 316 PRO A CA 1 ATOM 2166 C C . PRO A 1 286 ? 32.870 -7.862 6.263 1.00 85.40 ? 316 PRO A C 1 ATOM 2167 O O . PRO A 1 286 ? 31.967 -7.115 5.876 1.00 81.01 ? 316 PRO A O 1 ATOM 2168 C CB . PRO A 1 286 ? 33.405 -7.945 8.715 1.00 86.14 ? 316 PRO A CB 1 ATOM 2169 C CG . PRO A 1 286 ? 33.943 -9.032 9.577 1.00 86.62 ? 316 PRO A CG 1 ATOM 2170 C CD . PRO A 1 286 ? 34.272 -10.170 8.671 1.00 83.99 ? 316 PRO A CD 1 ATOM 2171 N N . TYR A 1 287 ? 34.012 -8.024 5.602 1.00 85.51 ? 317 TYR A N 1 ATOM 2172 C CA . TYR A 1 287 ? 34.265 -7.330 4.344 1.00 86.88 ? 317 TYR A CA 1 ATOM 2173 C C . TYR A 1 287 ? 33.385 -7.873 3.205 1.00 82.61 ? 317 TYR A C 1 ATOM 2174 O O . TYR A 1 287 ? 32.949 -7.117 2.342 1.00 81.26 ? 317 TYR A O 1 ATOM 2175 C CB . TYR A 1 287 ? 35.759 -7.377 3.986 1.00 88.20 ? 317 TYR A CB 1 ATOM 2176 C CG . TYR A 1 287 ? 36.641 -6.746 5.037 1.00 93.37 ? 317 TYR A CG 1 ATOM 2177 C CD1 . TYR A 1 287 ? 36.702 -5.365 5.187 1.00 98.04 ? 317 TYR A CD1 1 ATOM 2178 C CD2 . TYR A 1 287 ? 37.407 -7.531 5.899 1.00 95.41 ? 317 TYR A CD2 1 ATOM 2179 C CE1 . TYR A 1 287 ? 37.506 -4.789 6.163 1.00 101.64 ? 317 TYR A CE1 1 ATOM 2180 C CE2 . TYR A 1 287 ? 38.204 -6.967 6.877 1.00 98.52 ? 317 TYR A CE2 1 ATOM 2181 C CZ . TYR A 1 287 ? 38.250 -5.599 7.004 1.00 102.03 ? 317 TYR A CZ 1 ATOM 2182 O OH . TYR A 1 287 ? 39.040 -5.048 7.976 1.00 109.88 ? 317 TYR A OH 1 ATOM 2183 N N . VAL A 1 288 ? 33.110 -9.171 3.216 1.00 79.47 ? 318 VAL A N 1 ATOM 2184 C CA . VAL A 1 288 ? 32.188 -9.756 2.244 1.00 75.63 ? 318 VAL A CA 1 ATOM 2185 C C . VAL A 1 288 ? 30.764 -9.236 2.446 1.00 76.81 ? 318 VAL A C 1 ATOM 2186 O O . VAL A 1 288 ? 30.094 -8.872 1.483 1.00 77.07 ? 318 VAL A O 1 ATOM 2187 C CB . VAL A 1 288 ? 32.194 -11.290 2.308 1.00 73.30 ? 318 VAL A CB 1 ATOM 2188 C CG1 . VAL A 1 288 ? 31.065 -11.869 1.470 1.00 70.75 ? 318 VAL A CG1 1 ATOM 2189 C CG2 . VAL A 1 288 ? 33.530 -11.835 1.838 1.00 72.14 ? 318 VAL A CG2 1 ATOM 2190 N N . ARG A 1 289 ? 30.306 -9.197 3.696 1.00 78.72 ? 319 ARG A N 1 ATOM 2191 C CA . ARG A 1 289 ? 28.990 -8.642 4.022 1.00 76.72 ? 319 ARG A CA 1 ATOM 2192 C C . ARG A 1 289 ? 28.867 -7.202 3.515 1.00 77.64 ? 319 ARG A C 1 ATOM 2193 O O . ARG A 1 289 ? 27.837 -6.808 2.955 1.00 74.86 ? 319 ARG A O 1 ATOM 2194 C CB . ARG A 1 289 ? 28.732 -8.712 5.537 1.00 75.50 ? 319 ARG A CB 1 ATOM 2195 C CG . ARG A 1 289 ? 28.427 -10.107 6.058 1.00 73.19 ? 319 ARG A CG 1 ATOM 2196 C CD . ARG A 1 289 ? 28.288 -10.146 7.582 1.00 74.17 ? 319 ARG A CD 1 ATOM 2197 N NE . ARG A 1 289 ? 27.116 -9.410 8.073 1.00 74.31 ? 319 ARG A NE 1 ATOM 2198 C CZ . ARG A 1 289 ? 26.117 -9.917 8.795 1.00 70.91 ? 319 ARG A CZ 1 ATOM 2199 N NH1 . ARG A 1 289 ? 26.110 -11.187 9.151 1.00 71.70 ? 319 ARG A NH1 1 ATOM 2200 N NH2 . ARG A 1 289 ? 25.112 -9.135 9.176 1.00 69.00 ? 319 ARG A NH2 1 ATOM 2201 N N . LYS A 1 290 ? 29.922 -6.424 3.733 1.00 81.51 ? 320 LYS A N 1 ATOM 2202 C CA . LYS A 1 290 ? 29.978 -5.020 3.290 1.00 81.09 ? 320 LYS A CA 1 ATOM 2203 C C . LYS A 1 290 ? 29.899 -4.921 1.761 1.00 76.76 ? 320 LYS A C 1 ATOM 2204 O O . LYS A 1 290 ? 29.147 -4.110 1.231 1.00 81.00 ? 320 LYS A O 1 ATOM 2205 C CB . LYS A 1 290 ? 31.260 -4.350 3.809 1.00 82.64 ? 320 LYS A CB 1 ATOM 2206 C CG . LYS A 1 290 ? 31.086 -2.907 4.247 1.00 84.95 ? 320 LYS A CG 1 ATOM 2207 C CD . LYS A 1 290 ? 32.259 -2.401 5.093 1.00 88.82 ? 320 LYS A CD 1 ATOM 2208 C CE . LYS A 1 290 ? 32.460 -3.175 6.410 1.00 87.16 ? 320 LYS A CE 1 ATOM 2209 N NZ . LYS A 1 290 ? 33.823 -3.035 6.991 1.00 86.90 ? 320 LYS A NZ 1 ATOM 2210 N N . ALA A 1 291 ? 30.661 -5.772 1.074 1.00 70.37 ? 321 ALA A N 1 ATOM 2211 C CA . ALA A 1 291 ? 30.708 -5.812 -0.385 1.00 68.52 ? 321 ALA A CA 1 ATOM 2212 C C . ALA A 1 291 ? 29.373 -6.162 -0.982 1.00 68.28 ? 321 ALA A C 1 ATOM 2213 O O . ALA A 1 291 ? 29.065 -5.754 -2.095 1.00 70.80 ? 321 ALA A O 1 ATOM 2214 C CB . ALA A 1 291 ? 31.745 -6.826 -0.853 1.00 68.55 ? 321 ALA A CB 1 ATOM 2215 N N . LEU A 1 292 ? 28.603 -6.942 -0.225 1.00 70.21 ? 322 LEU A N 1 ATOM 2216 C CA . LEU A 1 292 ? 27.275 -7.424 -0.602 1.00 67.09 ? 322 LEU A CA 1 ATOM 2217 C C . LEU A 1 292 ? 26.171 -6.608 0.050 1.00 67.11 ? 322 LEU A C 1 ATOM 2218 O O . LEU A 1 292 ? 25.029 -7.066 0.141 1.00 60.88 ? 322 LEU A O 1 ATOM 2219 C CB . LEU A 1 292 ? 27.113 -8.887 -0.186 1.00 64.73 ? 322 LEU A CB 1 ATOM 2220 C CG . LEU A 1 292 ? 28.049 -9.901 -0.830 1.00 65.56 ? 322 LEU A CG 1 ATOM 2221 C CD1 . LEU A 1 292 ? 27.938 -11.238 -0.115 1.00 65.63 ? 322 LEU A CD1 1 ATOM 2222 C CD2 . LEU A 1 292 ? 27.728 -10.059 -2.304 1.00 65.91 ? 322 LEU A CD2 1 ATOM 2223 N N . ASN A 1 293 ? 26.518 -5.414 0.526 1.00 70.95 ? 323 ASN A N 1 ATOM 2224 C CA . ASN A 1 293 ? 25.524 -4.456 1.030 1.00 71.22 ? 323 ASN A CA 1 ATOM 2225 C C . ASN A 1 293 ? 24.603 -5.087 2.073 1.00 71.57 ? 323 ASN A C 1 ATOM 2226 O O . ASN A 1 293 ? 23.399 -4.876 2.058 1.00 71.37 ? 323 ASN A O 1 ATOM 2227 C CB . ASN A 1 293 ? 24.729 -3.891 -0.149 1.00 70.76 ? 323 ASN A CB 1 ATOM 2228 C CG . ASN A 1 293 ? 25.632 -3.428 -1.284 1.00 73.75 ? 323 ASN A CG 1 ATOM 2229 O OD1 . ASN A 1 293 ? 26.586 -2.686 -1.064 1.00 78.07 ? 323 ASN A OD1 1 ATOM 2230 N ND2 . ASN A 1 293 ? 25.373 -3.900 -2.488 1.00 73.69 ? 323 ASN A ND2 1 ATOM 2231 N N . ILE A 1 294 ? 25.179 -5.889 2.962 1.00 73.65 ? 324 ILE A N 1 ATOM 2232 C CA . ILE A 1 294 ? 24.413 -6.512 4.018 1.00 74.85 ? 324 ILE A CA 1 ATOM 2233 C C . ILE A 1 294 ? 24.449 -5.588 5.214 1.00 75.66 ? 324 ILE A C 1 ATOM 2234 O O . ILE A 1 294 ? 25.526 -5.150 5.621 1.00 79.71 ? 324 ILE A O 1 ATOM 2235 C CB . ILE A 1 294 ? 24.981 -7.878 4.434 1.00 76.34 ? 324 ILE A CB 1 ATOM 2236 C CG1 . ILE A 1 294 ? 25.131 -8.801 3.227 1.00 75.32 ? 324 ILE A CG1 1 ATOM 2237 C CG2 . ILE A 1 294 ? 24.071 -8.536 5.465 1.00 76.95 ? 324 ILE A CG2 1 ATOM 2238 C CD1 . ILE A 1 294 ? 23.834 -9.153 2.530 1.00 74.27 ? 324 ILE A CD1 1 ATOM 2239 N N . PRO A 1 295 ? 23.278 -5.275 5.783 1.00 72.77 ? 325 PRO A N 1 ATOM 2240 C CA . PRO A 1 295 ? 23.289 -4.489 6.995 1.00 74.26 ? 325 PRO A CA 1 ATOM 2241 C C . PRO A 1 295 ? 23.977 -5.228 8.143 1.00 76.02 ? 325 PRO A C 1 ATOM 2242 O O . PRO A 1 295 ? 23.809 -6.434 8.291 1.00 72.84 ? 325 PRO A O 1 ATOM 2243 C CB . PRO A 1 295 ? 21.799 -4.270 7.286 1.00 73.66 ? 325 PRO A CB 1 ATOM 2244 C CG . PRO A 1 295 ? 21.126 -4.419 5.973 1.00 71.50 ? 325 PRO A CG 1 ATOM 2245 C CD . PRO A 1 295 ? 21.913 -5.491 5.283 1.00 73.31 ? 325 PRO A CD 1 ATOM 2246 N N . GLU A 1 296 ? 24.722 -4.484 8.951 1.00 80.69 ? 326 GLU A N 1 ATOM 2247 C CA . GLU A 1 296 ? 25.572 -5.045 9.999 1.00 83.11 ? 326 GLU A CA 1 ATOM 2248 C C . GLU A 1 296 ? 24.819 -5.811 11.079 1.00 78.16 ? 326 GLU A C 1 ATOM 2249 O O . GLU A 1 296 ? 25.238 -6.893 11.467 1.00 74.59 ? 326 GLU A O 1 ATOM 2250 C CB . GLU A 1 296 ? 26.382 -3.924 10.648 1.00 90.80 ? 326 GLU A CB 1 ATOM 2251 C CG . GLU A 1 296 ? 27.570 -4.384 11.475 1.00 97.93 ? 326 GLU A CG 1 ATOM 2252 C CD . GLU A 1 296 ? 28.374 -3.212 12.032 1.00 101.43 ? 326 GLU A CD 1 ATOM 2253 O OE1 . GLU A 1 296 ? 27.773 -2.182 12.415 1.00 97.60 ? 326 GLU A OE1 1 ATOM 2254 O OE2 . GLU A 1 296 ? 29.616 -3.323 12.087 1.00 103.29 ? 326 GLU A OE2 1 ATOM 2255 N N . GLN A 1 297 ? 23.698 -5.270 11.538 1.00 76.89 ? 327 GLN A N 1 ATOM 2256 C CA . GLN A 1 297 ? 22.992 -5.837 12.703 1.00 75.03 ? 327 GLN A CA 1 ATOM 2257 C C . GLN A 1 297 ? 22.468 -7.253 12.510 1.00 72.06 ? 327 GLN A C 1 ATOM 2258 O O . GLN A 1 297 ? 22.124 -7.910 13.479 1.00 71.36 ? 327 GLN A O 1 ATOM 2259 C CB . GLN A 1 297 ? 21.844 -4.926 13.169 1.00 75.59 ? 327 GLN A CB 1 ATOM 2260 C CG . GLN A 1 297 ? 20.585 -4.960 12.308 1.00 79.11 ? 327 GLN A CG 1 ATOM 2261 C CD . GLN A 1 297 ? 20.648 -4.072 11.065 1.00 81.75 ? 327 GLN A CD 1 ATOM 2262 O OE1 . GLN A 1 297 ? 21.710 -3.547 10.694 1.00 75.85 ? 327 GLN A OE1 1 ATOM 2263 N NE2 . GLN A 1 297 ? 19.491 -3.888 10.419 1.00 81.95 ? 327 GLN A NE2 1 ATOM 2264 N N . LEU A 1 298 ? 22.406 -7.727 11.272 1.00 73.33 ? 328 LEU A N 1 ATOM 2265 C CA . LEU A 1 298 ? 21.854 -9.048 10.991 1.00 71.58 ? 328 LEU A CA 1 ATOM 2266 C C . LEU A 1 298 ? 22.733 -10.174 11.527 1.00 69.82 ? 328 LEU A C 1 ATOM 2267 O O . LEU A 1 298 ? 23.962 -10.059 11.523 1.00 72.18 ? 328 LEU A O 1 ATOM 2268 C CB . LEU A 1 298 ? 21.639 -9.220 9.477 1.00 71.69 ? 328 LEU A CB 1 ATOM 2269 C CG . LEU A 1 298 ? 20.567 -8.343 8.813 1.00 70.87 ? 328 LEU A CG 1 ATOM 2270 C CD1 . LEU A 1 298 ? 20.615 -8.520 7.304 1.00 69.49 ? 328 LEU A CD1 1 ATOM 2271 C CD2 . LEU A 1 298 ? 19.177 -8.660 9.345 1.00 68.94 ? 328 LEU A CD2 1 ATOM 2272 N N . PRO A 1 299 ? 22.108 -11.282 11.960 1.00 67.23 ? 329 PRO A N 1 ATOM 2273 C CA . PRO A 1 299 ? 22.849 -12.410 12.520 1.00 66.00 ? 329 PRO A CA 1 ATOM 2274 C C . PRO A 1 299 ? 23.794 -13.045 11.525 1.00 68.91 ? 329 PRO A C 1 ATOM 2275 O O . PRO A 1 299 ? 23.737 -12.742 10.334 1.00 72.41 ? 329 PRO A O 1 ATOM 2276 C CB . PRO A 1 299 ? 21.751 -13.404 12.910 1.00 63.33 ? 329 PRO A CB 1 ATOM 2277 C CG . PRO A 1 299 ? 20.561 -13.037 12.108 1.00 60.68 ? 329 PRO A CG 1 ATOM 2278 C CD . PRO A 1 299 ? 20.665 -11.568 11.847 1.00 64.66 ? 329 PRO A CD 1 ATOM 2279 N N . GLN A 1 300 ? 24.645 -13.939 12.007 1.00 72.43 ? 330 GLN A N 1 ATOM 2280 C CA . GLN A 1 300 ? 25.611 -14.594 11.152 1.00 74.21 ? 330 GLN A CA 1 ATOM 2281 C C . GLN A 1 300 ? 24.886 -15.351 10.042 1.00 73.81 ? 330 GLN A C 1 ATOM 2282 O O . GLN A 1 300 ? 23.721 -15.723 10.192 1.00 69.33 ? 330 GLN A O 1 ATOM 2283 C CB . GLN A 1 300 ? 26.516 -15.543 11.960 1.00 81.48 ? 330 GLN A CB 1 ATOM 2284 C CG . GLN A 1 300 ? 25.847 -16.801 12.513 1.00 90.17 ? 330 GLN A CG 1 ATOM 2285 C CD . GLN A 1 300 ? 26.837 -17.906 12.896 1.00 101.98 ? 330 GLN A CD 1 ATOM 2286 O OE1 . GLN A 1 300 ? 27.979 -17.635 13.274 1.00 108.30 ? 330 GLN A OE1 1 ATOM 2287 N NE2 . GLN A 1 300 ? 26.393 -19.160 12.809 1.00 103.39 ? 330 GLN A NE2 1 ATOM 2288 N N . TRP A 1 301 ? 25.579 -15.594 8.936 1.00 70.50 ? 331 TRP A N 1 ATOM 2289 C CA . TRP A 1 301 ? 25.036 -16.416 7.866 1.00 68.81 ? 331 TRP A CA 1 ATOM 2290 C C . TRP A 1 301 ? 25.236 -17.898 8.166 1.00 69.95 ? 331 TRP A C 1 ATOM 2291 O O . TRP A 1 301 ? 26.315 -18.303 8.598 1.00 76.61 ? 331 TRP A O 1 ATOM 2292 C CB . TRP A 1 301 ? 25.711 -16.069 6.547 1.00 68.84 ? 331 TRP A CB 1 ATOM 2293 C CG . TRP A 1 301 ? 25.146 -16.768 5.348 1.00 64.27 ? 331 TRP A CG 1 ATOM 2294 C CD1 . TRP A 1 301 ? 24.171 -16.310 4.522 1.00 64.08 ? 331 TRP A CD1 1 ATOM 2295 C CD2 . TRP A 1 301 ? 25.548 -18.033 4.830 1.00 60.61 ? 331 TRP A CD2 1 ATOM 2296 N NE1 . TRP A 1 301 ? 23.932 -17.221 3.518 1.00 61.77 ? 331 TRP A NE1 1 ATOM 2297 C CE2 . TRP A 1 301 ? 24.768 -18.286 3.683 1.00 58.41 ? 331 TRP A CE2 1 ATOM 2298 C CE3 . TRP A 1 301 ? 26.492 -18.978 5.226 1.00 61.21 ? 331 TRP A CE3 1 ATOM 2299 C CZ2 . TRP A 1 301 ? 24.894 -19.445 2.926 1.00 57.01 ? 331 TRP A CZ2 1 ATOM 2300 C CZ3 . TRP A 1 301 ? 26.622 -20.141 4.466 1.00 63.14 ? 331 TRP A CZ3 1 ATOM 2301 C CH2 . TRP A 1 301 ? 25.815 -20.363 3.330 1.00 59.28 ? 331 TRP A CH2 1 ATOM 2302 N N . ASP A 1 302 ? 24.176 -18.675 7.937 1.00 67.86 ? 332 ASP A N 1 ATOM 2303 C CA . ASP A 1 302 ? 24.176 -20.130 7.967 1.00 62.87 ? 332 ASP A CA 1 ATOM 2304 C C . ASP A 1 302 ? 23.554 -20.625 6.673 1.00 63.14 ? 332 ASP A C 1 ATOM 2305 O O . ASP A 1 302 ? 22.577 -20.059 6.182 1.00 57.06 ? 332 ASP A O 1 ATOM 2306 C CB . ASP A 1 302 ? 23.310 -20.654 9.112 1.00 63.95 ? 332 ASP A CB 1 ATOM 2307 C CG . ASP A 1 302 ? 23.823 -20.274 10.469 1.00 69.01 ? 332 ASP A CG 1 ATOM 2308 O OD1 . ASP A 1 302 ? 25.052 -20.145 10.647 1.00 71.48 ? 332 ASP A OD1 1 ATOM 2309 O OD2 . ASP A 1 302 ? 22.980 -20.120 11.378 1.00 75.72 ? 332 ASP A OD2 1 ATOM 2310 N N . MET A 1 303 ? 24.072 -21.722 6.142 1.00 67.85 ? 333 MET A N 1 ATOM 2311 C CA . MET A 1 303 ? 23.502 -22.297 4.932 1.00 69.80 ? 333 MET A CA 1 ATOM 2312 C C . MET A 1 303 ? 22.033 -22.642 5.137 1.00 69.33 ? 333 MET A C 1 ATOM 2313 O O . MET A 1 303 ? 21.246 -22.458 4.216 1.00 74.73 ? 333 MET A O 1 ATOM 2314 C CB . MET A 1 303 ? 24.271 -23.525 4.466 1.00 72.84 ? 333 MET A CB 1 ATOM 2315 C CG . MET A 1 303 ? 23.916 -23.956 3.058 1.00 76.96 ? 333 MET A CG 1 ATOM 2316 S SD . MET A 1 303 ? 24.235 -25.700 2.793 1.00 89.35 ? 333 MET A SD 1 ATOM 2317 C CE . MET A 1 303 ? 26.000 -25.639 2.480 1.00 92.76 ? 333 MET A CE 1 ATOM 2318 N N . CYS A 1 304 ? 21.661 -23.149 6.311 1.00 68.28 ? 334 CYS A N 1 ATOM 2319 C CA . CYS A 1 304 ? 20.231 -23.312 6.649 1.00 69.39 ? 334 CYS A CA 1 ATOM 2320 C C . CYS A 1 304 ? 19.889 -22.719 7.999 1.00 66.11 ? 334 CYS A C 1 ATOM 2321 O O . CYS A 1 304 ? 20.748 -22.547 8.853 1.00 67.16 ? 334 CYS A O 1 ATOM 2322 C CB . CYS A 1 304 ? 19.771 -24.771 6.608 1.00 68.44 ? 334 CYS A CB 1 ATOM 2323 S SG . CYS A 1 304 ? 20.429 -25.686 5.200 1.00 77.01 ? 334 CYS A SG 1 ATOM 2324 N N . ASN A 1 305 ? 18.619 -22.387 8.157 1.00 66.10 ? 335 ASN A N 1 ATOM 2325 C CA . ASN A 1 305 ? 18.082 -21.883 9.401 1.00 65.03 ? 335 ASN A CA 1 ATOM 2326 C C . ASN A 1 305 ? 17.205 -22.952 10.027 1.00 66.40 ? 335 ASN A C 1 ATOM 2327 O O . ASN A 1 305 ? 16.164 -23.305 9.476 1.00 59.95 ? 335 ASN A O 1 ATOM 2328 C CB . ASN A 1 305 ? 17.266 -20.648 9.113 1.00 66.46 ? 335 ASN A CB 1 ATOM 2329 C CG . ASN A 1 305 ? 16.977 -19.848 10.346 1.00 69.92 ? 335 ASN A CG 1 ATOM 2330 O OD1 . ASN A 1 305 ? 16.755 -20.400 11.429 1.00 73.11 ? 335 ASN A OD1 1 ATOM 2331 N ND2 . ASN A 1 305 ? 16.960 -18.525 10.194 1.00 71.06 ? 335 ASN A ND2 1 ATOM 2332 N N . PHE A 1 306 ? 17.651 -23.472 11.169 1.00 73.86 ? 336 PHE A N 1 ATOM 2333 C CA . PHE A 1 306 ? 16.887 -24.445 11.961 1.00 81.89 ? 336 PHE A CA 1 ATOM 2334 C C . PHE A 1 306 ? 15.499 -23.928 12.348 1.00 80.81 ? 336 PHE A C 1 ATOM 2335 O O . PHE A 1 306 ? 14.517 -24.659 12.248 1.00 77.34 ? 336 PHE A O 1 ATOM 2336 C CB . PHE A 1 306 ? 17.668 -24.895 13.211 1.00 91.91 ? 336 PHE A CB 1 ATOM 2337 C CG . PHE A 1 306 ? 18.290 -23.763 14.011 1.00 106.34 ? 336 PHE A CG 1 ATOM 2338 C CD1 . PHE A 1 306 ? 19.562 -23.266 13.687 1.00 117.79 ? 336 PHE A CD1 1 ATOM 2339 C CD2 . PHE A 1 306 ? 17.628 -23.212 15.107 1.00 110.98 ? 336 PHE A CD2 1 ATOM 2340 C CE1 . PHE A 1 306 ? 20.141 -22.237 14.426 1.00 121.12 ? 336 PHE A CE1 1 ATOM 2341 C CE2 . PHE A 1 306 ? 18.204 -22.186 15.847 1.00 113.97 ? 336 PHE A CE2 1 ATOM 2342 C CZ . PHE A 1 306 ? 19.460 -21.699 15.508 1.00 118.75 ? 336 PHE A CZ 1 ATOM 2343 N N . LEU A 1 307 ? 15.410 -22.660 12.738 1.00 81.04 ? 337 LEU A N 1 ATOM 2344 C CA . LEU A 1 307 ? 14.121 -22.063 13.085 1.00 83.39 ? 337 LEU A CA 1 ATOM 2345 C C . LEU A 1 307 ? 13.154 -22.226 11.929 1.00 80.80 ? 337 LEU A C 1 ATOM 2346 O O . LEU A 1 307 ? 12.108 -22.854 12.071 1.00 82.19 ? 337 LEU A O 1 ATOM 2347 C CB . LEU A 1 307 ? 14.249 -20.574 13.425 1.00 89.69 ? 337 LEU A CB 1 ATOM 2348 C CG . LEU A 1 307 ? 15.141 -20.179 14.606 1.00 94.47 ? 337 LEU A CG 1 ATOM 2349 C CD1 . LEU A 1 307 ? 15.274 -18.663 14.660 1.00 94.42 ? 337 LEU A CD1 1 ATOM 2350 C CD2 . LEU A 1 307 ? 14.604 -20.747 15.914 1.00 94.54 ? 337 LEU A CD2 1 ATOM 2351 N N . VAL A 1 308 ? 13.523 -21.666 10.781 1.00 76.55 ? 338 VAL A N 1 ATOM 2352 C CA . VAL A 1 308 ? 12.701 -21.749 9.586 1.00 71.73 ? 338 VAL A CA 1 ATOM 2353 C C . VAL A 1 308 ? 12.254 -23.179 9.384 1.00 67.84 ? 338 VAL A C 1 ATOM 2354 O O . VAL A 1 308 ? 11.057 -23.461 9.332 1.00 68.72 ? 338 VAL A O 1 ATOM 2355 C CB . VAL A 1 308 ? 13.455 -21.266 8.326 1.00 69.66 ? 338 VAL A CB 1 ATOM 2356 C CG1 . VAL A 1 308 ? 12.664 -21.582 7.067 1.00 68.02 ? 338 VAL A CG1 1 ATOM 2357 C CG2 . VAL A 1 308 ? 13.715 -19.767 8.402 1.00 70.23 ? 338 VAL A CG2 1 ATOM 2358 N N . ASN A 1 309 ? 13.215 -24.080 9.290 1.00 65.04 ? 339 ASN A N 1 ATOM 2359 C CA . ASN A 1 309 ? 12.907 -25.473 8.990 1.00 65.46 ? 339 ASN A CA 1 ATOM 2360 C C . ASN A 1 309 ? 11.980 -26.066 10.030 1.00 64.51 ? 339 ASN A C 1 ATOM 2361 O O . ASN A 1 309 ? 10.956 -26.633 9.683 1.00 66.25 ? 339 ASN A O 1 ATOM 2362 C CB . ASN A 1 309 ? 14.187 -26.298 8.883 1.00 67.86 ? 339 ASN A CB 1 ATOM 2363 C CG . ASN A 1 309 ? 13.936 -27.695 8.365 1.00 68.87 ? 339 ASN A CG 1 ATOM 2364 O OD1 . ASN A 1 309 ? 13.617 -28.603 9.134 1.00 70.21 ? 339 ASN A OD1 1 ATOM 2365 N ND2 . ASN A 1 309 ? 14.090 -27.883 7.061 1.00 71.19 ? 339 ASN A ND2 1 ATOM 2366 N N . LEU A 1 310 ? 12.329 -25.932 11.305 1.00 64.24 ? 340 LEU A N 1 ATOM 2367 C CA . LEU A 1 310 ? 11.503 -26.482 12.379 1.00 65.66 ? 340 LEU A CA 1 ATOM 2368 C C . LEU A 1 310 ? 10.112 -25.877 12.466 1.00 67.79 ? 340 LEU A C 1 ATOM 2369 O O . LEU A 1 310 ? 9.159 -26.574 12.791 1.00 68.90 ? 340 LEU A O 1 ATOM 2370 C CB . LEU A 1 310 ? 12.202 -26.347 13.728 1.00 67.28 ? 340 LEU A CB 1 ATOM 2371 C CG . LEU A 1 310 ? 13.438 -27.241 13.882 1.00 69.95 ? 340 LEU A CG 1 ATOM 2372 C CD1 . LEU A 1 310 ? 14.158 -26.897 15.183 1.00 73.05 ? 340 LEU A CD1 1 ATOM 2373 C CD2 . LEU A 1 310 ? 13.085 -28.723 13.832 1.00 67.33 ? 340 LEU A CD2 1 ATOM 2374 N N . GLN A 1 311 ? 9.993 -24.585 12.183 1.00 70.36 ? 341 GLN A N 1 ATOM 2375 C CA . GLN A 1 311 ? 8.702 -23.909 12.242 1.00 67.24 ? 341 GLN A CA 1 ATOM 2376 C C . GLN A 1 311 ? 7.915 -23.966 10.947 1.00 66.97 ? 341 GLN A C 1 ATOM 2377 O O . GLN A 1 311 ? 6.868 -23.332 10.850 1.00 72.97 ? 341 GLN A O 1 ATOM 2378 C CB . GLN A 1 311 ? 8.888 -22.454 12.620 1.00 67.14 ? 341 GLN A CB 1 ATOM 2379 C CG . GLN A 1 311 ? 9.363 -22.244 14.034 1.00 68.47 ? 341 GLN A CG 1 ATOM 2380 C CD . GLN A 1 311 ? 9.417 -20.779 14.364 1.00 70.97 ? 341 GLN A CD 1 ATOM 2381 O OE1 . GLN A 1 311 ? 10.270 -20.059 13.856 1.00 76.92 ? 341 GLN A OE1 1 ATOM 2382 N NE2 . GLN A 1 311 ? 8.515 -20.325 15.220 1.00 76.45 ? 341 GLN A NE2 1 ATOM 2383 N N . TYR A 1 312 ? 8.392 -24.727 9.962 1.00 65.15 ? 342 TYR A N 1 ATOM 2384 C CA . TYR A 1 312 ? 7.814 -24.700 8.616 1.00 61.82 ? 342 TYR A CA 1 ATOM 2385 C C . TYR A 1 312 ? 6.656 -25.661 8.477 1.00 65.04 ? 342 TYR A C 1 ATOM 2386 O O . TYR A 1 312 ? 6.769 -26.837 8.823 1.00 67.67 ? 342 TYR A O 1 ATOM 2387 C CB . TYR A 1 312 ? 8.868 -25.029 7.558 1.00 56.13 ? 342 TYR A CB 1 ATOM 2388 C CG . TYR A 1 312 ? 8.469 -24.665 6.146 1.00 53.81 ? 342 TYR A CG 1 ATOM 2389 C CD1 . TYR A 1 312 ? 7.671 -25.525 5.375 1.00 54.80 ? 342 TYR A CD1 1 ATOM 2390 C CD2 . TYR A 1 312 ? 8.895 -23.478 5.570 1.00 51.06 ? 342 TYR A CD2 1 ATOM 2391 C CE1 . TYR A 1 312 ? 7.313 -25.208 4.070 1.00 53.42 ? 342 TYR A CE1 1 ATOM 2392 C CE2 . TYR A 1 312 ? 8.540 -23.150 4.275 1.00 52.56 ? 342 TYR A CE2 1 ATOM 2393 C CZ . TYR A 1 312 ? 7.757 -24.018 3.524 1.00 52.74 ? 342 TYR A CZ 1 ATOM 2394 O OH . TYR A 1 312 ? 7.402 -23.673 2.246 1.00 50.39 ? 342 TYR A OH 1 ATOM 2395 N N . ARG A 1 313 ? 5.564 -25.166 7.906 1.00 70.61 ? 343 ARG A N 1 ATOM 2396 C CA . ARG A 1 313 ? 4.348 -25.943 7.724 1.00 76.21 ? 343 ARG A CA 1 ATOM 2397 C C . ARG A 1 313 ? 4.162 -26.347 6.253 1.00 75.11 ? 343 ARG A C 1 ATOM 2398 O O . ARG A 1 313 ? 3.953 -25.498 5.395 1.00 73.83 ? 343 ARG A O 1 ATOM 2399 C CB . ARG A 1 313 ? 3.167 -25.118 8.213 1.00 81.22 ? 343 ARG A CB 1 ATOM 2400 C CG . ARG A 1 313 ? 1.918 -25.919 8.491 1.00 88.87 ? 343 ARG A CG 1 ATOM 2401 C CD . ARG A 1 313 ? 1.839 -26.441 9.914 1.00 91.75 ? 343 ARG A CD 1 ATOM 2402 N NE . ARG A 1 313 ? 0.469 -26.866 10.173 1.00 95.88 ? 343 ARG A NE 1 ATOM 2403 C CZ . ARG A 1 313 ? -0.542 -26.040 10.421 1.00 101.33 ? 343 ARG A CZ 1 ATOM 2404 N NH1 . ARG A 1 313 ? -0.350 -24.723 10.482 1.00 101.14 ? 343 ARG A NH1 1 ATOM 2405 N NH2 . ARG A 1 313 ? -1.755 -26.534 10.618 1.00 107.53 ? 343 ARG A NH2 1 ATOM 2406 N N . ARG A 1 314 ? 4.251 -27.645 5.982 1.00 75.51 ? 344 ARG A N 1 ATOM 2407 C CA . ARG A 1 314 ? 4.146 -28.193 4.625 1.00 71.19 ? 344 ARG A CA 1 ATOM 2408 C C . ARG A 1 314 ? 2.701 -28.480 4.268 1.00 70.65 ? 344 ARG A C 1 ATOM 2409 O O . ARG A 1 314 ? 2.056 -29.266 4.947 1.00 80.68 ? 344 ARG A O 1 ATOM 2410 C CB . ARG A 1 314 ? 4.917 -29.506 4.536 1.00 71.19 ? 344 ARG A CB 1 ATOM 2411 C CG . ARG A 1 314 ? 6.425 -29.368 4.651 1.00 74.60 ? 344 ARG A CG 1 ATOM 2412 C CD . ARG A 1 314 ? 7.024 -30.695 5.071 1.00 76.01 ? 344 ARG A CD 1 ATOM 2413 N NE . ARG A 1 314 ? 8.461 -30.809 4.847 1.00 73.70 ? 344 ARG A NE 1 ATOM 2414 C CZ . ARG A 1 314 ? 9.392 -30.484 5.733 1.00 70.18 ? 344 ARG A CZ 1 ATOM 2415 N NH1 . ARG A 1 314 ? 9.072 -29.980 6.927 1.00 71.74 ? 344 ARG A NH1 1 ATOM 2416 N NH2 . ARG A 1 314 ? 10.658 -30.657 5.420 1.00 67.12 ? 344 ARG A NH2 1 ATOM 2417 N N . LEU A 1 315 ? 2.199 -27.873 3.198 1.00 66.78 ? 345 LEU A N 1 ATOM 2418 C CA . LEU A 1 315 ? 0.778 -27.957 2.849 1.00 63.62 ? 345 LEU A CA 1 ATOM 2419 C C . LEU A 1 315 ? 0.527 -28.799 1.628 1.00 63.88 ? 345 LEU A C 1 ATOM 2420 O O . LEU A 1 315 ? -0.329 -29.666 1.646 1.00 67.06 ? 345 LEU A O 1 ATOM 2421 C CB . LEU A 1 315 ? 0.213 -26.573 2.596 1.00 63.23 ? 345 LEU A CB 1 ATOM 2422 C CG . LEU A 1 315 ? 0.484 -25.561 3.700 1.00 62.00 ? 345 LEU A CG 1 ATOM 2423 C CD1 . LEU A 1 315 ? 0.045 -24.180 3.247 1.00 63.28 ? 345 LEU A CD1 1 ATOM 2424 C CD2 . LEU A 1 315 ? -0.212 -25.994 4.972 1.00 62.97 ? 345 LEU A CD2 1 ATOM 2425 N N . TYR A 1 316 ? 1.267 -28.544 0.558 1.00 64.68 ? 346 TYR A N 1 ATOM 2426 C CA . TYR A 1 316 ? 1.105 -29.336 -0.651 1.00 65.36 ? 346 TYR A CA 1 ATOM 2427 C C . TYR A 1 316 ? 1.810 -30.679 -0.508 1.00 66.78 ? 346 TYR A C 1 ATOM 2428 O O . TYR A 1 316 ? 2.964 -30.752 -0.104 1.00 69.03 ? 346 TYR A O 1 ATOM 2429 C CB . TYR A 1 316 ? 1.629 -28.603 -1.870 1.00 63.42 ? 346 TYR A CB 1 ATOM 2430 C CG . TYR A 1 316 ? 0.979 -27.274 -2.113 1.00 64.01 ? 346 TYR A CG 1 ATOM 2431 C CD1 . TYR A 1 316 ? -0.354 -27.186 -2.487 1.00 64.83 ? 346 TYR A CD1 1 ATOM 2432 C CD2 . TYR A 1 316 ? 1.707 -26.095 -1.979 1.00 64.45 ? 346 TYR A CD2 1 ATOM 2433 C CE1 . TYR A 1 316 ? -0.945 -25.949 -2.705 1.00 67.76 ? 346 TYR A CE1 1 ATOM 2434 C CE2 . TYR A 1 316 ? 1.134 -24.859 -2.207 1.00 63.32 ? 346 TYR A CE2 1 ATOM 2435 C CZ . TYR A 1 316 ? -0.184 -24.781 -2.565 1.00 66.04 ? 346 TYR A CZ 1 ATOM 2436 O OH . TYR A 1 316 ? -0.735 -23.532 -2.774 1.00 65.25 ? 346 TYR A OH 1 ATOM 2437 N N . ARG A 1 317 ? 1.081 -31.724 -0.857 1.00 69.70 ? 347 ARG A N 1 ATOM 2438 C CA . ARG A 1 317 ? 1.502 -33.097 -0.730 1.00 73.38 ? 347 ARG A CA 1 ATOM 2439 C C . ARG A 1 317 ? 1.927 -33.653 -2.112 1.00 74.14 ? 347 ARG A C 1 ATOM 2440 O O . ARG A 1 317 ? 2.509 -34.741 -2.214 1.00 70.43 ? 347 ARG A O 1 ATOM 2441 C CB . ARG A 1 317 ? 0.315 -33.886 -0.150 1.00 79.28 ? 347 ARG A CB 1 ATOM 2442 C CG . ARG A 1 317 ? 0.629 -35.126 0.678 1.00 82.78 ? 347 ARG A CG 1 ATOM 2443 C CD . ARG A 1 317 ? 1.703 -34.912 1.733 1.00 82.92 ? 347 ARG A CD 1 ATOM 2444 N NE . ARG A 1 317 ? 1.561 -33.668 2.477 1.00 87.30 ? 347 ARG A NE 1 ATOM 2445 C CZ . ARG A 1 317 ? 2.369 -33.291 3.469 1.00 91.31 ? 347 ARG A CZ 1 ATOM 2446 N NH1 . ARG A 1 317 ? 3.377 -34.064 3.859 1.00 92.61 ? 347 ARG A NH1 1 ATOM 2447 N NH2 . ARG A 1 317 ? 2.165 -32.132 4.079 1.00 89.82 ? 347 ARG A NH2 1 ATOM 2448 N N . SER A 1 318 ? 1.615 -32.911 -3.172 1.00 73.07 ? 348 SER A N 1 ATOM 2449 C CA . SER A 1 318 ? 1.917 -33.326 -4.539 1.00 71.97 ? 348 SER A CA 1 ATOM 2450 C C . SER A 1 318 ? 1.772 -32.144 -5.495 1.00 71.42 ? 348 SER A C 1 ATOM 2451 O O . SER A 1 318 ? 0.845 -31.348 -5.369 1.00 71.79 ? 348 SER A O 1 ATOM 2452 C CB . SER A 1 318 ? 0.972 -34.434 -4.967 1.00 73.38 ? 348 SER A CB 1 ATOM 2453 O OG . SER A 1 318 ? 1.119 -34.735 -6.348 1.00 81.99 ? 348 SER A OG 1 ATOM 2454 N N . MET A 1 319 ? 2.668 -32.047 -6.469 1.00 71.26 ? 349 MET A N 1 ATOM 2455 C CA . MET A 1 319 ? 2.654 -30.929 -7.421 1.00 71.71 ? 349 MET A CA 1 ATOM 2456 C C . MET A 1 319 ? 1.950 -31.275 -8.719 1.00 71.41 ? 349 MET A C 1 ATOM 2457 O O . MET A 1 319 ? 2.026 -30.535 -9.699 1.00 73.94 ? 349 MET A O 1 ATOM 2458 C CB . MET A 1 319 ? 4.076 -30.467 -7.717 1.00 70.89 ? 349 MET A CB 1 ATOM 2459 C CG . MET A 1 319 ? 4.766 -29.857 -6.511 1.00 70.53 ? 349 MET A CG 1 ATOM 2460 S SD . MET A 1 319 ? 4.231 -28.180 -6.138 1.00 72.99 ? 349 MET A SD 1 ATOM 2461 C CE . MET A 1 319 ? 3.027 -28.452 -4.860 1.00 71.38 ? 349 MET A CE 1 ATOM 2462 N N . ASN A 1 320 ? 1.249 -32.393 -8.722 1.00 69.85 ? 350 ASN A N 1 ATOM 2463 C CA . ASN A 1 320 ? 0.455 -32.779 -9.866 1.00 71.33 ? 350 ASN A CA 1 ATOM 2464 C C . ASN A 1 320 ? -0.479 -31.671 -10.424 1.00 74.41 ? 350 ASN A C 1 ATOM 2465 O O . ASN A 1 320 ? -0.526 -31.437 -11.631 1.00 80.51 ? 350 ASN A O 1 ATOM 2466 C CB . ASN A 1 320 ? -0.370 -33.989 -9.484 1.00 72.96 ? 350 ASN A CB 1 ATOM 2467 C CG . ASN A 1 320 ? -1.089 -34.573 -10.657 1.00 72.74 ? 350 ASN A CG 1 ATOM 2468 O OD1 . ASN A 1 320 ? -2.279 -34.350 -10.846 1.00 77.25 ? 350 ASN A OD1 1 ATOM 2469 N ND2 . ASN A 1 320 ? -0.366 -35.300 -11.472 1.00 73.24 ? 350 ASN A ND2 1 ATOM 2470 N N . SER A 1 321 ? -1.236 -31.006 -9.565 1.00 72.08 ? 351 SER A N 1 ATOM 2471 C CA . SER A 1 321 ? -2.120 -29.949 -10.033 1.00 73.75 ? 351 SER A CA 1 ATOM 2472 C C . SER A 1 321 ? -1.337 -28.853 -10.713 1.00 73.84 ? 351 SER A C 1 ATOM 2473 O O . SER A 1 321 ? -1.605 -28.485 -11.848 1.00 80.19 ? 351 SER A O 1 ATOM 2474 C CB . SER A 1 321 ? -2.886 -29.344 -8.874 1.00 72.38 ? 351 SER A CB 1 ATOM 2475 O OG . SER A 1 321 ? -3.593 -30.365 -8.223 1.00 75.98 ? 351 SER A OG 1 ATOM 2476 N N . GLN A 1 322 ? -0.345 -28.354 -10.009 1.00 72.21 ? 352 GLN A N 1 ATOM 2477 C CA . GLN A 1 322 ? 0.366 -27.180 -10.443 1.00 71.66 ? 352 GLN A CA 1 ATOM 2478 C C . GLN A 1 322 ? 0.977 -27.408 -11.814 1.00 72.47 ? 352 GLN A C 1 ATOM 2479 O O . GLN A 1 322 ? 1.003 -26.495 -12.644 1.00 72.34 ? 352 GLN A O 1 ATOM 2480 C CB . GLN A 1 322 ? 1.443 -26.809 -9.415 1.00 72.69 ? 352 GLN A CB 1 ATOM 2481 C CG . GLN A 1 322 ? 0.908 -26.224 -8.100 1.00 71.89 ? 352 GLN A CG 1 ATOM 2482 C CD . GLN A 1 322 ? 0.374 -27.263 -7.125 1.00 71.70 ? 352 GLN A CD 1 ATOM 2483 O OE1 . GLN A 1 322 ? 0.435 -28.478 -7.380 1.00 73.84 ? 352 GLN A OE1 1 ATOM 2484 N NE2 . GLN A 1 322 ? -0.150 -26.796 -5.998 1.00 70.60 ? 352 GLN A NE2 1 ATOM 2485 N N . TYR A 1 323 ? 1.473 -28.617 -12.050 1.00 72.19 ? 353 TYR A N 1 ATOM 2486 C CA . TYR A 1 323 ? 2.189 -28.906 -13.285 1.00 75.00 ? 353 TYR A CA 1 ATOM 2487 C C . TYR A 1 323 ? 1.215 -29.018 -14.447 1.00 78.29 ? 353 TYR A C 1 ATOM 2488 O O . TYR A 1 323 ? 1.476 -28.482 -15.531 1.00 82.03 ? 353 TYR A O 1 ATOM 2489 C CB . TYR A 1 323 ? 3.070 -30.153 -13.148 1.00 74.98 ? 353 TYR A CB 1 ATOM 2490 C CG . TYR A 1 323 ? 4.436 -29.876 -12.532 1.00 75.87 ? 353 TYR A CG 1 ATOM 2491 C CD1 . TYR A 1 323 ? 5.444 -29.300 -13.276 1.00 76.15 ? 353 TYR A CD1 1 ATOM 2492 C CD2 . TYR A 1 323 ? 4.721 -30.213 -11.211 1.00 77.07 ? 353 TYR A CD2 1 ATOM 2493 C CE1 . TYR A 1 323 ? 6.697 -29.073 -12.734 1.00 77.97 ? 353 TYR A CE1 1 ATOM 2494 C CE2 . TYR A 1 323 ? 5.966 -29.978 -10.658 1.00 77.33 ? 353 TYR A CE2 1 ATOM 2495 C CZ . TYR A 1 323 ? 6.955 -29.405 -11.423 1.00 78.47 ? 353 TYR A CZ 1 ATOM 2496 O OH . TYR A 1 323 ? 8.203 -29.157 -10.872 1.00 79.74 ? 353 TYR A OH 1 ATOM 2497 N N . LEU A 1 324 ? 0.098 -29.704 -14.231 1.00 75.34 ? 354 LEU A N 1 ATOM 2498 C CA . LEU A 1 324 ? -0.939 -29.781 -15.254 1.00 75.91 ? 354 LEU A CA 1 ATOM 2499 C C . LEU A 1 324 ? -1.476 -28.392 -15.552 1.00 79.60 ? 354 LEU A C 1 ATOM 2500 O O . LEU A 1 324 ? -1.670 -28.013 -16.708 1.00 85.62 ? 354 LEU A O 1 ATOM 2501 C CB . LEU A 1 324 ? -2.073 -30.699 -14.813 1.00 75.05 ? 354 LEU A CB 1 ATOM 2502 C CG . LEU A 1 324 ? -1.721 -32.181 -14.633 1.00 72.33 ? 354 LEU A CG 1 ATOM 2503 C CD1 . LEU A 1 324 ? -2.853 -32.914 -13.915 1.00 71.32 ? 354 LEU A CD1 1 ATOM 2504 C CD2 . LEU A 1 324 ? -1.386 -32.839 -15.962 1.00 68.89 ? 354 LEU A CD2 1 ATOM 2505 N N . LYS A 1 325 ? -1.694 -27.623 -14.499 1.00 80.61 ? 355 LYS A N 1 ATOM 2506 C CA . LYS A 1 325 ? -2.125 -26.247 -14.635 1.00 83.78 ? 355 LYS A CA 1 ATOM 2507 C C . LYS A 1 325 ? -1.116 -25.404 -15.420 1.00 84.92 ? 355 LYS A C 1 ATOM 2508 O O . LYS A 1 325 ? -1.496 -24.478 -16.118 1.00 92.00 ? 355 LYS A O 1 ATOM 2509 C CB . LYS A 1 325 ? -2.359 -25.647 -13.254 1.00 85.25 ? 355 LYS A CB 1 ATOM 2510 C CG . LYS A 1 325 ? -3.180 -24.383 -13.273 1.00 92.71 ? 355 LYS A CG 1 ATOM 2511 C CD . LYS A 1 325 ? -3.467 -23.893 -11.864 1.00 96.08 ? 355 LYS A CD 1 ATOM 2512 C CE . LYS A 1 325 ? -4.503 -24.750 -11.156 1.00 95.98 ? 355 LYS A CE 1 ATOM 2513 N NZ . LYS A 1 325 ? -5.083 -23.999 -10.009 1.00 97.45 ? 355 LYS A NZ 1 ATOM 2514 N N . LEU A 1 326 ? 0.166 -25.718 -15.299 1.00 82.59 ? 356 LEU A N 1 ATOM 2515 C CA . LEU A 1 326 ? 1.195 -25.022 -16.062 1.00 82.37 ? 356 LEU A CA 1 ATOM 2516 C C . LEU A 1 326 ? 1.320 -25.601 -17.467 1.00 79.25 ? 356 LEU A C 1 ATOM 2517 O O . LEU A 1 326 ? 1.729 -24.910 -18.398 1.00 78.70 ? 356 LEU A O 1 ATOM 2518 C CB . LEU A 1 326 ? 2.542 -25.100 -15.345 1.00 83.97 ? 356 LEU A CB 1 ATOM 2519 C CG . LEU A 1 326 ? 2.682 -24.258 -14.068 1.00 84.25 ? 356 LEU A CG 1 ATOM 2520 C CD1 . LEU A 1 326 ? 3.677 -24.889 -13.107 1.00 81.53 ? 356 LEU A CD1 1 ATOM 2521 C CD2 . LEU A 1 326 ? 3.073 -22.818 -14.376 1.00 82.01 ? 356 LEU A CD2 1 ATOM 2522 N N . LEU A 1 327 ? 0.966 -26.866 -17.617 1.00 74.77 ? 357 LEU A N 1 ATOM 2523 C CA . LEU A 1 327 ? 1.061 -27.522 -18.910 1.00 76.91 ? 357 LEU A CA 1 ATOM 2524 C C . LEU A 1 327 ? -0.112 -27.237 -19.818 1.00 80.89 ? 357 LEU A C 1 ATOM 2525 O O . LEU A 1 327 ? 0.036 -27.261 -21.032 1.00 80.60 ? 357 LEU A O 1 ATOM 2526 C CB . LEU A 1 327 ? 1.169 -29.025 -18.722 1.00 77.25 ? 357 LEU A CB 1 ATOM 2527 C CG . LEU A 1 327 ? 2.548 -29.494 -18.297 1.00 74.21 ? 357 LEU A CG 1 ATOM 2528 C CD1 . LEU A 1 327 ? 2.416 -30.860 -17.654 1.00 73.70 ? 357 LEU A CD1 1 ATOM 2529 C CD2 . LEU A 1 327 ? 3.500 -29.497 -19.487 1.00 74.08 ? 357 LEU A CD2 1 ATOM 2530 N N . SER A 1 328 ? -1.279 -26.992 -19.230 1.00 88.68 ? 358 SER A N 1 ATOM 2531 C CA . SER A 1 328 ? -2.502 -26.739 -19.996 1.00 93.83 ? 358 SER A CA 1 ATOM 2532 C C . SER A 1 328 ? -2.333 -25.566 -20.956 1.00 95.76 ? 358 SER A C 1 ATOM 2533 O O . SER A 1 328 ? -2.719 -25.654 -22.112 1.00 94.43 ? 358 SER A O 1 ATOM 2534 C CB . SER A 1 328 ? -3.668 -26.442 -19.061 1.00 93.27 ? 358 SER A CB 1 ATOM 2535 O OG . SER A 1 328 ? -3.458 -25.206 -18.410 1.00 93.46 ? 358 SER A OG 1 ATOM 2536 N N . SER A 1 329 ? -1.750 -24.478 -20.464 1.00 99.05 ? 359 SER A N 1 ATOM 2537 C CA . SER A 1 329 ? -1.510 -23.292 -21.286 1.00 100.35 ? 359 SER A CA 1 ATOM 2538 C C . SER A 1 329 ? -0.630 -23.615 -22.480 1.00 97.78 ? 359 SER A C 1 ATOM 2539 O O . SER A 1 329 ? -0.853 -23.105 -23.573 1.00 100.82 ? 359 SER A O 1 ATOM 2540 C CB . SER A 1 329 ? -0.844 -22.192 -20.465 1.00 102.08 ? 359 SER A CB 1 ATOM 2541 O OG . SER A 1 329 ? 0.542 -22.440 -20.332 1.00 108.02 ? 359 SER A OG 1 ATOM 2542 N N . GLN A 1 330 ? 0.380 -24.450 -22.253 1.00 96.37 ? 360 GLN A N 1 ATOM 2543 C CA . GLN A 1 330 ? 1.368 -24.821 -23.273 1.00 98.23 ? 360 GLN A CA 1 ATOM 2544 C C . GLN A 1 330 ? 2.254 -23.674 -23.768 1.00 92.79 ? 360 GLN A C 1 ATOM 2545 O O . GLN A 1 330 ? 2.812 -23.740 -24.841 1.00 85.48 ? 360 GLN A O 1 ATOM 2546 C CB . GLN A 1 330 ? 0.712 -25.525 -24.455 1.00 102.02 ? 360 GLN A CB 1 ATOM 2547 C CG . GLN A 1 330 ? 0.212 -26.909 -24.125 1.00 106.66 ? 360 GLN A CG 1 ATOM 2548 C CD . GLN A 1 330 ? -0.720 -27.412 -25.210 1.00 115.52 ? 360 GLN A CD 1 ATOM 2549 O OE1 . GLN A 1 330 ? -1.938 -27.228 -25.126 1.00 116.60 ? 360 GLN A OE1 1 ATOM 2550 N NE2 . GLN A 1 330 ? -0.154 -27.987 -26.269 1.00 122.58 ? 360 GLN A NE2 1 ATOM 2551 N N . LYS A 1 331 ? 2.414 -22.648 -22.954 1.00 93.94 ? 361 LYS A N 1 ATOM 2552 C CA . LYS A 1 331 ? 3.396 -21.619 -23.229 1.00 95.15 ? 361 LYS A CA 1 ATOM 2553 C C . LYS A 1 331 ? 4.739 -21.958 -22.584 1.00 90.62 ? 361 LYS A C 1 ATOM 2554 O O . LYS A 1 331 ? 5.734 -21.316 -22.892 1.00 88.83 ? 361 LYS A O 1 ATOM 2555 C CB . LYS A 1 331 ? 2.923 -20.282 -22.678 1.00 98.87 ? 361 LYS A CB 1 ATOM 2556 C CG . LYS A 1 331 ? 1.527 -19.877 -23.108 1.00 101.19 ? 361 LYS A CG 1 ATOM 2557 C CD . LYS A 1 331 ? 1.146 -18.547 -22.484 1.00 102.39 ? 361 LYS A CD 1 ATOM 2558 C CE . LYS A 1 331 ? -0.217 -18.086 -22.966 1.00 106.54 ? 361 LYS A CE 1 ATOM 2559 N NZ . LYS A 1 331 ? -0.594 -16.783 -22.365 1.00 107.44 ? 361 LYS A NZ 1 ATOM 2560 N N . TYR A 1 332 ? 4.765 -22.962 -21.700 1.00 86.35 ? 362 TYR A N 1 ATOM 2561 C CA . TYR A 1 332 ? 5.885 -23.135 -20.777 1.00 79.70 ? 362 TYR A CA 1 ATOM 2562 C C . TYR A 1 332 ? 6.679 -24.427 -20.977 1.00 78.62 ? 362 TYR A C 1 ATOM 2563 O O . TYR A 1 332 ? 6.116 -25.522 -21.030 1.00 79.71 ? 362 TYR A O 1 ATOM 2564 C CB . TYR A 1 332 ? 5.396 -23.011 -19.319 1.00 78.19 ? 362 TYR A CB 1 ATOM 2565 C CG . TYR A 1 332 ? 4.585 -21.756 -19.061 1.00 78.29 ? 362 TYR A CG 1 ATOM 2566 C CD1 . TYR A 1 332 ? 5.058 -20.498 -19.447 1.00 79.01 ? 362 TYR A CD1 1 ATOM 2567 C CD2 . TYR A 1 332 ? 3.337 -21.820 -18.461 1.00 76.91 ? 362 TYR A CD2 1 ATOM 2568 C CE1 . TYR A 1 332 ? 4.306 -19.361 -19.237 1.00 78.03 ? 362 TYR A CE1 1 ATOM 2569 C CE2 . TYR A 1 332 ? 2.584 -20.678 -18.250 1.00 75.32 ? 362 TYR A CE2 1 ATOM 2570 C CZ . TYR A 1 332 ? 3.076 -19.460 -18.643 1.00 76.33 ? 362 TYR A CZ 1 ATOM 2571 O OH . TYR A 1 332 ? 2.363 -18.316 -18.442 1.00 77.98 ? 362 TYR A OH 1 ATOM 2572 N N . GLN A 1 333 ? 7.999 -24.274 -21.061 1.00 73.75 ? 363 GLN A N 1 ATOM 2573 C CA . GLN A 1 333 ? 8.920 -25.377 -21.250 1.00 74.81 ? 363 GLN A CA 1 ATOM 2574 C C . GLN A 1 333 ? 9.467 -25.872 -19.902 1.00 71.58 ? 363 GLN A C 1 ATOM 2575 O O . GLN A 1 333 ? 10.207 -25.156 -19.236 1.00 71.84 ? 363 GLN A O 1 ATOM 2576 C CB . GLN A 1 333 ? 10.058 -24.891 -22.142 1.00 80.68 ? 363 GLN A CB 1 ATOM 2577 C CG . GLN A 1 333 ? 11.001 -25.970 -22.655 1.00 90.01 ? 363 GLN A CG 1 ATOM 2578 C CD . GLN A 1 333 ? 12.374 -25.418 -23.023 1.00 98.34 ? 363 GLN A CD 1 ATOM 2579 O OE1 . GLN A 1 333 ? 12.630 -24.208 -22.913 1.00 98.37 ? 363 GLN A OE1 1 ATOM 2580 N NE2 . GLN A 1 333 ? 13.273 -26.305 -23.462 1.00 101.65 ? 363 GLN A NE2 1 ATOM 2581 N N . ILE A 1 334 ? 9.131 -27.104 -19.521 1.00 68.85 ? 364 ILE A N 1 ATOM 2582 C CA . ILE A 1 334 ? 9.429 -27.627 -18.180 1.00 65.72 ? 364 ILE A CA 1 ATOM 2583 C C . ILE A 1 334 ? 10.453 -28.764 -18.186 1.00 62.22 ? 364 ILE A C 1 ATOM 2584 O O . ILE A 1 334 ? 10.348 -29.678 -19.001 1.00 63.37 ? 364 ILE A O 1 ATOM 2585 C CB . ILE A 1 334 ? 8.142 -28.144 -17.507 1.00 69.52 ? 364 ILE A CB 1 ATOM 2586 C CG1 . ILE A 1 334 ? 7.114 -27.022 -17.405 1.00 71.04 ? 364 ILE A CG1 1 ATOM 2587 C CG2 . ILE A 1 334 ? 8.445 -28.750 -16.125 1.00 70.17 ? 364 ILE A CG2 1 ATOM 2588 C CD1 . ILE A 1 334 ? 5.734 -27.492 -17.005 1.00 72.69 ? 364 ILE A CD1 1 ATOM 2589 N N . LEU A 1 335 ? 11.409 -28.725 -17.254 1.00 58.97 ? 365 LEU A N 1 ATOM 2590 C CA . LEU A 1 335 ? 12.398 -29.806 -17.084 1.00 60.26 ? 365 LEU A CA 1 ATOM 2591 C C . LEU A 1 335 ? 12.507 -30.259 -15.648 1.00 62.63 ? 365 LEU A C 1 ATOM 2592 O O . LEU A 1 335 ? 12.677 -29.448 -14.725 1.00 65.08 ? 365 LEU A O 1 ATOM 2593 C CB . LEU A 1 335 ? 13.786 -29.362 -17.531 1.00 60.18 ? 365 LEU A CB 1 ATOM 2594 C CG . LEU A 1 335 ? 14.952 -30.332 -17.338 1.00 58.07 ? 365 LEU A CG 1 ATOM 2595 C CD1 . LEU A 1 335 ? 14.906 -31.436 -18.373 1.00 58.60 ? 365 LEU A CD1 1 ATOM 2596 C CD2 . LEU A 1 335 ? 16.296 -29.611 -17.423 1.00 59.84 ? 365 LEU A CD2 1 ATOM 2597 N N . LEU A 1 336 ? 12.449 -31.564 -15.460 1.00 62.43 ? 366 LEU A N 1 ATOM 2598 C CA . LEU A 1 336 ? 12.792 -32.151 -14.190 1.00 61.59 ? 366 LEU A CA 1 ATOM 2599 C C . LEU A 1 336 ? 14.021 -32.980 -14.448 1.00 62.25 ? 366 LEU A C 1 ATOM 2600 O O . LEU A 1 336 ? 14.028 -33.847 -15.333 1.00 67.21 ? 366 LEU A O 1 ATOM 2601 C CB . LEU A 1 336 ? 11.660 -33.019 -13.652 1.00 63.15 ? 366 LEU A CB 1 ATOM 2602 C CG . LEU A 1 336 ? 10.652 -32.298 -12.754 1.00 60.41 ? 366 LEU A CG 1 ATOM 2603 C CD1 . LEU A 1 336 ? 9.707 -31.443 -13.557 1.00 60.69 ? 366 LEU A CD1 1 ATOM 2604 C CD2 . LEU A 1 336 ? 9.869 -33.319 -11.966 1.00 62.37 ? 366 LEU A CD2 1 ATOM 2605 N N . TYR A 1 337 ? 15.073 -32.702 -13.699 1.00 60.20 ? 367 TYR A N 1 ATOM 2606 C CA . TYR A 1 337 ? 16.294 -33.482 -13.802 1.00 60.63 ? 367 TYR A CA 1 ATOM 2607 C C . TYR A 1 337 ? 16.687 -34.003 -12.434 1.00 58.21 ? 367 TYR A C 1 ATOM 2608 O O . TYR A 1 337 ? 16.390 -33.378 -11.416 1.00 53.82 ? 367 TYR A O 1 ATOM 2609 C CB . TYR A 1 337 ? 17.416 -32.657 -14.443 1.00 59.56 ? 367 TYR A CB 1 ATOM 2610 C CG . TYR A 1 337 ? 17.868 -31.467 -13.627 1.00 61.70 ? 367 TYR A CG 1 ATOM 2611 C CD1 . TYR A 1 337 ? 17.157 -30.274 -13.650 1.00 61.16 ? 367 TYR A CD1 1 ATOM 2612 C CD2 . TYR A 1 337 ? 19.017 -31.538 -12.823 1.00 60.32 ? 367 TYR A CD2 1 ATOM 2613 C CE1 . TYR A 1 337 ? 17.574 -29.185 -12.908 1.00 60.91 ? 367 TYR A CE1 1 ATOM 2614 C CE2 . TYR A 1 337 ? 19.441 -30.454 -12.085 1.00 58.01 ? 367 TYR A CE2 1 ATOM 2615 C CZ . TYR A 1 337 ? 18.716 -29.278 -12.137 1.00 59.91 ? 367 TYR A CZ 1 ATOM 2616 O OH . TYR A 1 337 ? 19.118 -28.187 -11.401 1.00 61.70 ? 367 TYR A OH 1 ATOM 2617 N N . ASN A 1 338 ? 17.360 -35.146 -12.415 1.00 60.49 ? 368 ASN A N 1 ATOM 2618 C CA . ASN A 1 338 ? 17.711 -35.811 -11.157 1.00 64.80 ? 368 ASN A CA 1 ATOM 2619 C C . ASN A 1 338 ? 19.084 -36.503 -11.224 1.00 63.51 ? 368 ASN A C 1 ATOM 2620 O O . ASN A 1 338 ? 19.403 -37.187 -12.197 1.00 59.66 ? 368 ASN A O 1 ATOM 2621 C CB . ASN A 1 338 ? 16.636 -36.854 -10.773 1.00 67.89 ? 368 ASN A CB 1 ATOM 2622 C CG . ASN A 1 338 ? 15.400 -36.248 -10.103 1.00 68.70 ? 368 ASN A CG 1 ATOM 2623 O OD1 . ASN A 1 338 ? 14.654 -35.467 -10.696 1.00 68.39 ? 368 ASN A OD1 1 ATOM 2624 N ND2 . ASN A 1 338 ? 15.158 -36.653 -8.866 1.00 74.08 ? 368 ASN A ND2 1 ATOM 2625 N N . GLY A 1 339 ? 19.888 -36.326 -10.180 1.00 61.67 ? 369 GLY A N 1 ATOM 2626 C CA . GLY A 1 339 ? 21.047 -37.172 -9.975 1.00 60.20 ? 369 GLY A CA 1 ATOM 2627 C C . GLY A 1 339 ? 20.612 -38.575 -9.609 1.00 57.72 ? 369 GLY A C 1 ATOM 2628 O O . GLY A 1 339 ? 19.818 -38.766 -8.681 1.00 60.19 ? 369 GLY A O 1 ATOM 2629 N N . ASP A 1 340 ? 21.147 -39.569 -10.297 1.00 56.91 ? 370 ASP A N 1 ATOM 2630 C CA . ASP A 1 340 ? 20.663 -40.951 -10.109 1.00 60.31 ? 370 ASP A CA 1 ATOM 2631 C C . ASP A 1 340 ? 21.322 -41.750 -8.969 1.00 59.39 ? 370 ASP A C 1 ATOM 2632 O O . ASP A 1 340 ? 21.093 -42.952 -8.838 1.00 56.08 ? 370 ASP A O 1 ATOM 2633 C CB . ASP A 1 340 ? 20.707 -41.727 -11.436 1.00 59.92 ? 370 ASP A CB 1 ATOM 2634 C CG . ASP A 1 340 ? 22.092 -42.091 -11.865 1.00 63.55 ? 370 ASP A CG 1 ATOM 2635 O OD1 . ASP A 1 340 ? 23.085 -41.503 -11.353 1.00 74.19 ? 370 ASP A OD1 1 ATOM 2636 O OD2 . ASP A 1 340 ? 22.205 -42.974 -12.736 1.00 68.40 ? 370 ASP A OD2 1 ATOM 2637 N N . VAL A 1 341 ? 22.145 -41.086 -8.164 1.00 61.44 ? 371 VAL A N 1 ATOM 2638 C CA . VAL A 1 341 ? 22.657 -41.685 -6.940 1.00 62.50 ? 371 VAL A CA 1 ATOM 2639 C C . VAL A 1 341 ? 22.271 -40.875 -5.685 1.00 61.44 ? 371 VAL A C 1 ATOM 2640 O O . VAL A 1 341 ? 22.864 -41.052 -4.616 1.00 62.20 ? 371 VAL A O 1 ATOM 2641 C CB . VAL A 1 341 ? 24.173 -41.917 -7.044 1.00 63.89 ? 371 VAL A CB 1 ATOM 2642 C CG1 . VAL A 1 341 ? 24.466 -42.879 -8.195 1.00 63.34 ? 371 VAL A CG1 1 ATOM 2643 C CG2 . VAL A 1 341 ? 24.906 -40.610 -7.256 1.00 64.84 ? 371 VAL A CG2 1 ATOM 2644 N N . ASP A 1 342 ? 21.260 -40.019 -5.820 1.00 58.48 ? 372 ASP A N 1 ATOM 2645 C CA . ASP A 1 342 ? 20.689 -39.292 -4.690 1.00 60.41 ? 372 ASP A CA 1 ATOM 2646 C C . ASP A 1 342 ? 19.545 -40.089 -4.030 1.00 60.64 ? 372 ASP A C 1 ATOM 2647 O O . ASP A 1 342 ? 18.716 -40.686 -4.723 1.00 63.30 ? 372 ASP A O 1 ATOM 2648 C CB . ASP A 1 342 ? 20.156 -37.930 -5.150 1.00 60.42 ? 372 ASP A CB 1 ATOM 2649 C CG . ASP A 1 342 ? 19.419 -37.181 -4.039 1.00 59.76 ? 372 ASP A CG 1 ATOM 2650 O OD1 . ASP A 1 342 ? 19.788 -37.355 -2.868 1.00 57.98 ? 372 ASP A OD1 1 ATOM 2651 O OD2 . ASP A 1 342 ? 18.438 -36.463 -4.332 1.00 57.20 ? 372 ASP A OD2 1 ATOM 2652 N N . MET A 1 343 ? 19.483 -40.054 -2.702 1.00 58.00 ? 373 MET A N 1 ATOM 2653 C CA . MET A 1 343 ? 18.412 -40.726 -1.963 1.00 58.31 ? 373 MET A CA 1 ATOM 2654 C C . MET A 1 343 ? 17.483 -39.772 -1.254 1.00 58.76 ? 373 MET A C 1 ATOM 2655 O O . MET A 1 343 ? 16.422 -40.194 -0.785 1.00 61.46 ? 373 MET A O 1 ATOM 2656 C CB . MET A 1 343 ? 18.997 -41.705 -0.961 1.00 57.67 ? 373 MET A CB 1 ATOM 2657 C CG . MET A 1 343 ? 19.778 -42.811 -1.637 1.00 58.67 ? 373 MET A CG 1 ATOM 2658 S SD . MET A 1 343 ? 20.303 -44.119 -0.527 1.00 58.68 ? 373 MET A SD 1 ATOM 2659 C CE . MET A 1 343 ? 21.117 -43.197 0.763 1.00 57.59 ? 373 MET A CE 1 ATOM 2660 N N . ALA A 1 344 ? 17.870 -38.501 -1.164 1.00 58.00 ? 374 ALA A N 1 ATOM 2661 C CA . ALA A 1 344 ? 16.965 -37.454 -0.699 1.00 60.84 ? 374 ALA A CA 1 ATOM 2662 C C . ALA A 1 344 ? 15.749 -37.301 -1.618 1.00 59.15 ? 374 ALA A C 1 ATOM 2663 O O . ALA A 1 344 ? 14.631 -37.305 -1.150 1.00 59.18 ? 374 ALA A O 1 ATOM 2664 C CB . ALA A 1 344 ? 17.694 -36.122 -0.567 1.00 61.78 ? 374 ALA A CB 1 ATOM 2665 N N . CYS A 1 345 ? 15.975 -37.157 -2.920 1.00 62.29 ? 375 CYS A N 1 ATOM 2666 C CA . CYS A 1 345 ? 14.875 -37.067 -3.907 1.00 65.02 ? 375 CYS A CA 1 ATOM 2667 C C . CYS A 1 345 ? 15.164 -37.941 -5.119 1.00 63.38 ? 375 CYS A C 1 ATOM 2668 O O . CYS A 1 345 ? 15.511 -37.438 -6.179 1.00 65.31 ? 375 CYS A O 1 ATOM 2669 C CB . CYS A 1 345 ? 14.660 -35.613 -4.346 1.00 65.30 ? 375 CYS A CB 1 ATOM 2670 S SG . CYS A 1 345 ? 13.983 -34.566 -3.044 1.00 66.71 ? 375 CYS A SG 1 ATOM 2671 N N . ASN A 1 346 ? 15.022 -39.249 -4.958 1.00 60.18 ? 376 ASN A N 1 ATOM 2672 C CA . ASN A 1 346 ? 15.629 -40.163 -5.898 1.00 61.31 ? 376 ASN A CA 1 ATOM 2673 C C . ASN A 1 346 ? 15.026 -39.998 -7.283 1.00 61.85 ? 376 ASN A C 1 ATOM 2674 O O . ASN A 1 346 ? 13.893 -39.568 -7.413 1.00 60.54 ? 376 ASN A O 1 ATOM 2675 C CB . ASN A 1 346 ? 15.545 -41.603 -5.383 1.00 63.68 ? 376 ASN A CB 1 ATOM 2676 C CG . ASN A 1 346 ? 14.179 -42.208 -5.566 1.00 64.90 ? 376 ASN A CG 1 ATOM 2677 O OD1 . ASN A 1 346 ? 13.837 -42.620 -6.671 1.00 64.78 ? 376 ASN A OD1 1 ATOM 2678 N ND2 . ASN A 1 346 ? 13.391 -42.272 -4.490 1.00 63.44 ? 376 ASN A ND2 1 ATOM 2679 N N . PHE A 1 347 ? 15.806 -40.328 -8.314 1.00 63.23 ? 377 PHE A N 1 ATOM 2680 C CA . PHE A 1 347 ? 15.417 -40.086 -9.715 1.00 61.04 ? 377 PHE A CA 1 ATOM 2681 C C . PHE A 1 347 ? 14.114 -40.787 -10.104 1.00 60.66 ? 377 PHE A C 1 ATOM 2682 O O . PHE A 1 347 ? 13.317 -40.257 -10.895 1.00 59.66 ? 377 PHE A O 1 ATOM 2683 C CB . PHE A 1 347 ? 16.532 -40.503 -10.684 1.00 57.90 ? 377 PHE A CB 1 ATOM 2684 C CG . PHE A 1 347 ? 16.650 -41.984 -10.851 1.00 59.81 ? 377 PHE A CG 1 ATOM 2685 C CD1 . PHE A 1 347 ? 17.442 -42.727 -10.001 1.00 60.83 ? 377 PHE A CD1 1 ATOM 2686 C CD2 . PHE A 1 347 ? 15.942 -42.645 -11.843 1.00 61.79 ? 377 PHE A CD2 1 ATOM 2687 C CE1 . PHE A 1 347 ? 17.535 -44.103 -10.141 1.00 61.92 ? 377 PHE A CE1 1 ATOM 2688 C CE2 . PHE A 1 347 ? 16.033 -44.011 -11.995 1.00 61.76 ? 377 PHE A CE2 1 ATOM 2689 C CZ . PHE A 1 347 ? 16.830 -44.747 -11.142 1.00 62.14 ? 377 PHE A CZ 1 ATOM 2690 N N . MET A 1 348 ? 13.896 -41.975 -9.570 1.00 60.99 ? 378 MET A N 1 ATOM 2691 C CA . MET A 1 348 ? 12.727 -42.745 -9.990 1.00 65.51 ? 378 MET A CA 1 ATOM 2692 C C . MET A 1 348 ? 11.439 -42.103 -9.551 1.00 63.67 ? 378 MET A C 1 ATOM 2693 O O . MET A 1 348 ? 10.483 -42.073 -10.313 1.00 68.37 ? 378 MET A O 1 ATOM 2694 C CB . MET A 1 348 ? 12.775 -44.183 -9.490 1.00 65.63 ? 378 MET A CB 1 ATOM 2695 C CG . MET A 1 348 ? 11.632 -45.021 -10.034 1.00 66.90 ? 378 MET A CG 1 ATOM 2696 S SD . MET A 1 348 ? 11.974 -46.782 -9.921 1.00 69.45 ? 378 MET A SD 1 ATOM 2697 C CE . MET A 1 348 ? 13.160 -46.981 -11.258 1.00 69.22 ? 378 MET A CE 1 ATOM 2698 N N . GLY A 1 349 ? 11.419 -41.590 -8.324 1.00 64.93 ? 379 GLY A N 1 ATOM 2699 C CA . GLY A 1 349 ? 10.247 -40.902 -7.792 1.00 62.20 ? 379 GLY A CA 1 ATOM 2700 C C . GLY A 1 349 ? 9.789 -39.861 -8.784 1.00 60.73 ? 379 GLY A C 1 ATOM 2701 O O . GLY A 1 349 ? 8.620 -39.806 -9.135 1.00 57.84 ? 379 GLY A O 1 ATOM 2702 N N . ASP A 1 350 ? 10.720 -39.040 -9.252 1.00 61.85 ? 380 ASP A N 1 ATOM 2703 C CA . ASP A 1 350 ? 10.385 -38.000 -10.220 1.00 64.81 ? 380 ASP A CA 1 ATOM 2704 C C . ASP A 1 350 ? 10.093 -38.525 -11.625 1.00 67.29 ? 380 ASP A C 1 ATOM 2705 O O . ASP A 1 350 ? 9.244 -37.973 -12.323 1.00 70.79 ? 380 ASP A O 1 ATOM 2706 C CB . ASP A 1 350 ? 11.477 -36.952 -10.262 1.00 64.19 ? 380 ASP A CB 1 ATOM 2707 C CG . ASP A 1 350 ? 11.443 -36.071 -9.048 1.00 63.55 ? 380 ASP A CG 1 ATOM 2708 O OD1 . ASP A 1 350 ? 10.342 -35.568 -8.723 1.00 62.93 ? 380 ASP A OD1 1 ATOM 2709 O OD2 . ASP A 1 350 ? 12.507 -35.872 -8.434 1.00 66.89 ? 380 ASP A OD2 1 ATOM 2710 N N . GLU A 1 351 ? 10.753 -39.598 -12.035 1.00 67.43 ? 381 GLU A N 1 ATOM 2711 C CA . GLU A 1 351 ? 10.384 -40.231 -13.294 1.00 70.80 ? 381 GLU A CA 1 ATOM 2712 C C . GLU A 1 351 ? 8.944 -40.741 -13.244 1.00 73.53 ? 381 GLU A C 1 ATOM 2713 O O . GLU A 1 351 ? 8.191 -40.558 -14.204 1.00 73.24 ? 381 GLU A O 1 ATOM 2714 C CB . GLU A 1 351 ? 11.323 -41.369 -13.647 1.00 73.76 ? 381 GLU A CB 1 ATOM 2715 C CG . GLU A 1 351 ? 11.120 -41.881 -15.062 1.00 79.25 ? 381 GLU A CG 1 ATOM 2716 C CD . GLU A 1 351 ? 12.319 -42.630 -15.618 1.00 82.95 ? 381 GLU A CD 1 ATOM 2717 O OE1 . GLU A 1 351 ? 13.131 -43.171 -14.830 1.00 76.76 ? 381 GLU A OE1 1 ATOM 2718 O OE2 . GLU A 1 351 ? 12.433 -42.678 -16.864 1.00 88.69 ? 381 GLU A OE2 1 ATOM 2719 N N . TRP A 1 352 ? 8.565 -41.376 -12.127 1.00 71.78 ? 382 TRP A N 1 ATOM 2720 C CA . TRP A 1 352 ? 7.174 -41.793 -11.906 1.00 67.49 ? 382 TRP A CA 1 ATOM 2721 C C . TRP A 1 352 ? 6.241 -40.602 -11.896 1.00 66.17 ? 382 TRP A C 1 ATOM 2722 O O . TRP A 1 352 ? 5.155 -40.657 -12.440 1.00 68.53 ? 382 TRP A O 1 ATOM 2723 C CB . TRP A 1 352 ? 7.004 -42.482 -10.565 1.00 67.97 ? 382 TRP A CB 1 ATOM 2724 C CG . TRP A 1 352 ? 7.560 -43.857 -10.448 1.00 67.11 ? 382 TRP A CG 1 ATOM 2725 C CD1 . TRP A 1 352 ? 8.092 -44.614 -11.436 1.00 67.52 ? 382 TRP A CD1 1 ATOM 2726 C CD2 . TRP A 1 352 ? 7.585 -44.658 -9.258 1.00 66.93 ? 382 TRP A CD2 1 ATOM 2727 N NE1 . TRP A 1 352 ? 8.474 -45.835 -10.936 1.00 69.23 ? 382 TRP A NE1 1 ATOM 2728 C CE2 . TRP A 1 352 ? 8.167 -45.892 -9.602 1.00 68.69 ? 382 TRP A CE2 1 ATOM 2729 C CE3 . TRP A 1 352 ? 7.162 -44.451 -7.938 1.00 66.54 ? 382 TRP A CE3 1 ATOM 2730 C CZ2 . TRP A 1 352 ? 8.339 -46.930 -8.672 1.00 66.74 ? 382 TRP A CZ2 1 ATOM 2731 C CZ3 . TRP A 1 352 ? 7.345 -45.475 -7.009 1.00 68.89 ? 382 TRP A CZ3 1 ATOM 2732 C CH2 . TRP A 1 352 ? 7.928 -46.700 -7.386 1.00 68.01 ? 382 TRP A CH2 1 ATOM 2733 N N . PHE A 1 353 ? 6.657 -39.533 -11.242 1.00 64.80 ? 383 PHE A N 1 ATOM 2734 C CA . PHE A 1 353 ? 5.836 -38.353 -11.150 1.00 66.74 ? 383 PHE A CA 1 ATOM 2735 C C . PHE A 1 353 ? 5.561 -37.748 -12.515 1.00 71.04 ? 383 PHE A C 1 ATOM 2736 O O . PHE A 1 353 ? 4.416 -37.417 -12.829 1.00 74.08 ? 383 PHE A O 1 ATOM 2737 C CB . PHE A 1 353 ? 6.492 -37.305 -10.289 1.00 63.90 ? 383 PHE A CB 1 ATOM 2738 C CG . PHE A 1 353 ? 5.767 -36.002 -10.303 1.00 63.30 ? 383 PHE A CG 1 ATOM 2739 C CD1 . PHE A 1 353 ? 4.688 -35.793 -9.462 1.00 64.25 ? 383 PHE A CD1 1 ATOM 2740 C CD2 . PHE A 1 353 ? 6.163 -34.982 -11.145 1.00 63.40 ? 383 PHE A CD2 1 ATOM 2741 C CE1 . PHE A 1 353 ? 4.013 -34.585 -9.460 1.00 65.06 ? 383 PHE A CE1 1 ATOM 2742 C CE2 . PHE A 1 353 ? 5.489 -33.769 -11.147 1.00 65.04 ? 383 PHE A CE2 1 ATOM 2743 C CZ . PHE A 1 353 ? 4.409 -33.576 -10.305 1.00 64.25 ? 383 PHE A CZ 1 ATOM 2744 N N . VAL A 1 354 ? 6.600 -37.618 -13.330 1.00 71.70 ? 384 VAL A N 1 ATOM 2745 C CA . VAL A 1 354 ? 6.429 -37.083 -14.675 1.00 72.70 ? 384 VAL A CA 1 ATOM 2746 C C . VAL A 1 354 ? 5.566 -38.024 -15.516 1.00 73.19 ? 384 VAL A C 1 ATOM 2747 O O . VAL A 1 354 ? 4.570 -37.588 -16.076 1.00 76.51 ? 384 VAL A O 1 ATOM 2748 C CB . VAL A 1 354 ? 7.775 -36.843 -15.375 1.00 74.80 ? 384 VAL A CB 1 ATOM 2749 C CG1 . VAL A 1 354 ? 7.558 -36.461 -16.834 1.00 76.75 ? 384 VAL A CG1 1 ATOM 2750 C CG2 . VAL A 1 354 ? 8.560 -35.761 -14.645 1.00 75.38 ? 384 VAL A CG2 1 ATOM 2751 N N . ASP A 1 355 ? 5.938 -39.302 -15.579 1.00 72.23 ? 385 ASP A N 1 ATOM 2752 C CA . ASP A 1 355 ? 5.179 -40.310 -16.335 1.00 74.00 ? 385 ASP A CA 1 ATOM 2753 C C . ASP A 1 355 ? 3.706 -40.277 -15.987 1.00 74.33 ? 385 ASP A C 1 ATOM 2754 O O . ASP A 1 355 ? 2.859 -40.374 -16.878 1.00 75.69 ? 385 ASP A O 1 ATOM 2755 C CB . ASP A 1 355 ? 5.731 -41.727 -16.135 1.00 74.87 ? 385 ASP A CB 1 ATOM 2756 C CG . ASP A 1 355 ? 7.047 -41.957 -16.860 1.00 79.07 ? 385 ASP A CG 1 ATOM 2757 O OD1 . ASP A 1 355 ? 7.502 -41.076 -17.618 1.00 85.14 ? 385 ASP A OD1 1 ATOM 2758 O OD2 . ASP A 1 355 ? 7.659 -43.017 -16.651 1.00 89.04 ? 385 ASP A OD2 1 ATOM 2759 N N . SER A 1 356 ? 3.396 -40.092 -14.707 1.00 74.59 ? 386 SER A N 1 ATOM 2760 C CA . SER A 1 356 ? 1.998 -40.049 -14.254 1.00 73.97 ? 386 SER A CA 1 ATOM 2761 C C . SER A 1 356 ? 1.308 -38.692 -14.496 1.00 74.35 ? 386 SER A C 1 ATOM 2762 O O . SER A 1 356 ? 0.160 -38.519 -14.129 1.00 73.45 ? 386 SER A O 1 ATOM 2763 C CB . SER A 1 356 ? 1.900 -40.461 -12.782 1.00 71.77 ? 386 SER A CB 1 ATOM 2764 O OG . SER A 1 356 ? 2.427 -39.470 -11.936 1.00 68.90 ? 386 SER A OG 1 ATOM 2765 N N . LEU A 1 357 ? 1.992 -37.734 -15.120 1.00 74.98 ? 387 LEU A N 1 ATOM 2766 C CA . LEU A 1 357 ? 1.307 -36.546 -15.633 1.00 76.49 ? 387 LEU A CA 1 ATOM 2767 C C . LEU A 1 357 ? 0.489 -36.809 -16.910 1.00 78.87 ? 387 LEU A C 1 ATOM 2768 O O . LEU A 1 357 ? -0.340 -35.977 -17.265 1.00 80.77 ? 387 LEU A O 1 ATOM 2769 C CB . LEU A 1 357 ? 2.289 -35.410 -15.914 1.00 73.36 ? 387 LEU A CB 1 ATOM 2770 C CG . LEU A 1 357 ? 2.868 -34.711 -14.706 1.00 69.15 ? 387 LEU A CG 1 ATOM 2771 C CD1 . LEU A 1 357 ? 3.834 -33.639 -15.156 1.00 70.92 ? 387 LEU A CD1 1 ATOM 2772 C CD2 . LEU A 1 357 ? 1.777 -34.085 -13.873 1.00 71.22 ? 387 LEU A CD2 1 ATOM 2773 N N . ASN A 1 358 ? 0.720 -37.941 -17.576 1.00 80.20 ? 388 ASN A N 1 ATOM 2774 C CA . ASN A 1 358 ? 0.061 -38.278 -18.852 1.00 84.73 ? 388 ASN A CA 1 ATOM 2775 C C . ASN A 1 358 ? 0.086 -37.134 -19.849 1.00 86.97 ? 388 ASN A C 1 ATOM 2776 O O . ASN A 1 358 ? -0.926 -36.468 -20.057 1.00 94.79 ? 388 ASN A O 1 ATOM 2777 C CB . ASN A 1 358 ? -1.396 -38.696 -18.649 1.00 85.83 ? 388 ASN A CB 1 ATOM 2778 C CG . ASN A 1 358 ? -1.545 -40.035 -17.964 1.00 87.14 ? 388 ASN A CG 1 ATOM 2779 O OD1 . ASN A 1 358 ? -0.590 -40.790 -17.800 1.00 83.69 ? 388 ASN A OD1 1 ATOM 2780 N ND2 . ASN A 1 358 ? -2.770 -40.334 -17.555 1.00 88.57 ? 388 ASN A ND2 1 ATOM 2781 N N . GLN A 1 359 ? 1.241 -36.888 -20.444 1.00 84.71 ? 389 GLN A N 1 ATOM 2782 C CA . GLN A 1 359 ? 1.357 -35.905 -21.492 1.00 84.65 ? 389 GLN A CA 1 ATOM 2783 C C . GLN A 1 359 ? 1.622 -36.662 -22.759 1.00 88.91 ? 389 GLN A C 1 ATOM 2784 O O . GLN A 1 359 ? 1.916 -37.851 -22.706 1.00 85.59 ? 389 GLN A O 1 ATOM 2785 C CB . GLN A 1 359 ? 2.492 -34.937 -21.183 1.00 83.47 ? 389 GLN A CB 1 ATOM 2786 C CG . GLN A 1 359 ? 2.277 -34.153 -19.898 1.00 82.22 ? 389 GLN A CG 1 ATOM 2787 C CD . GLN A 1 359 ? 1.036 -33.287 -19.950 1.00 80.62 ? 389 GLN A CD 1 ATOM 2788 O OE1 . GLN A 1 359 ? 0.942 -32.385 -20.780 1.00 86.15 ? 389 GLN A OE1 1 ATOM 2789 N NE2 . GLN A 1 359 ? 0.078 -33.560 -19.084 1.00 77.38 ? 389 GLN A NE2 1 ATOM 2790 N N . LYS A 1 360 ? 1.501 -35.982 -23.895 1.00 95.16 ? 390 LYS A N 1 ATOM 2791 C CA . LYS A 1 360 ? 1.760 -36.613 -25.178 1.00 103.35 ? 390 LYS A CA 1 ATOM 2792 C C . LYS A 1 360 ? 3.253 -36.849 -25.340 1.00 103.39 ? 390 LYS A C 1 ATOM 2793 O O . LYS A 1 360 ? 4.037 -35.908 -25.444 1.00 104.99 ? 390 LYS A O 1 ATOM 2794 C CB . LYS A 1 360 ? 1.230 -35.774 -26.340 1.00 110.46 ? 390 LYS A CB 1 ATOM 2795 C CG . LYS A 1 360 ? 1.259 -36.494 -27.689 1.00 118.23 ? 390 LYS A CG 1 ATOM 2796 C CD . LYS A 1 360 ? 0.323 -35.837 -28.702 1.00 124.84 ? 390 LYS A CD 1 ATOM 2797 C CE . LYS A 1 360 ? -0.045 -36.766 -29.849 1.00 123.89 ? 390 LYS A CE 1 ATOM 2798 N NZ . LYS A 1 360 ? -1.174 -36.224 -30.654 1.00 124.75 ? 390 LYS A NZ 1 ATOM 2799 N N . MET A 1 361 ? 3.632 -38.117 -25.362 1.00 102.59 ? 391 MET A N 1 ATOM 2800 C CA . MET A 1 361 ? 5.007 -38.497 -25.571 1.00 104.37 ? 391 MET A CA 1 ATOM 2801 C C . MET A 1 361 ? 5.492 -37.956 -26.897 1.00 102.33 ? 391 MET A C 1 ATOM 2802 O O . MET A 1 361 ? 4.805 -38.067 -27.899 1.00 105.82 ? 391 MET A O 1 ATOM 2803 C CB . MET A 1 361 ? 5.145 -40.009 -25.550 1.00 111.80 ? 391 MET A CB 1 ATOM 2804 C CG . MET A 1 361 ? 6.473 -40.514 -26.077 1.00 122.58 ? 391 MET A CG 1 ATOM 2805 S SD . MET A 1 361 ? 6.893 -42.128 -25.398 1.00 140.10 ? 391 MET A SD 1 ATOM 2806 C CE . MET A 1 361 ? 7.714 -41.656 -23.878 1.00 130.65 ? 391 MET A CE 1 ATOM 2807 N N . GLU A 1 362 ? 6.668 -37.352 -26.880 1.00 98.20 ? 392 GLU A N 1 ATOM 2808 C CA . GLU A 1 362 ? 7.318 -36.913 -28.091 1.00 99.27 ? 392 GLU A CA 1 ATOM 2809 C C . GLU A 1 362 ? 8.511 -37.812 -28.372 1.00 102.05 ? 392 GLU A C 1 ATOM 2810 O O . GLU A 1 362 ? 8.386 -38.763 -29.144 1.00 110.79 ? 392 GLU A O 1 ATOM 2811 C CB . GLU A 1 362 ? 7.718 -35.451 -27.992 1.00 96.71 ? 392 GLU A CB 1 ATOM 2812 C CG . GLU A 1 362 ? 6.526 -34.517 -28.082 1.00 98.70 ? 392 GLU A CG 1 ATOM 2813 C CD . GLU A 1 362 ? 6.912 -33.118 -28.502 1.00 100.83 ? 392 GLU A CD 1 ATOM 2814 O OE1 . GLU A 1 362 ? 8.124 -32.814 -28.503 1.00 101.97 ? 392 GLU A OE1 1 ATOM 2815 O OE2 . GLU A 1 362 ? 6.006 -32.321 -28.825 1.00 101.18 ? 392 GLU A OE2 1 ATOM 2816 N N . VAL A 1 363 ? 9.652 -37.537 -27.745 1.00 99.36 ? 393 VAL A N 1 ATOM 2817 C CA . VAL A 1 363 ? 10.825 -38.387 -27.911 1.00 98.45 ? 393 VAL A CA 1 ATOM 2818 C C . VAL A 1 363 ? 10.779 -39.532 -26.901 1.00 94.97 ? 393 VAL A C 1 ATOM 2819 O O . VAL A 1 363 ? 10.590 -39.314 -25.706 1.00 92.05 ? 393 VAL A O 1 ATOM 2820 C CB . VAL A 1 363 ? 12.151 -37.608 -27.739 1.00 100.26 ? 393 VAL A CB 1 ATOM 2821 C CG1 . VAL A 1 363 ? 13.348 -38.516 -28.013 1.00 102.29 ? 393 VAL A CG1 1 ATOM 2822 C CG2 . VAL A 1 363 ? 12.195 -36.386 -28.647 1.00 100.37 ? 393 VAL A CG2 1 ATOM 2823 N N . GLN A 1 364 ? 10.978 -40.748 -27.397 1.00 96.29 ? 394 GLN A N 1 ATOM 2824 C CA . GLN A 1 364 ? 11.068 -41.942 -26.555 1.00 93.15 ? 394 GLN A CA 1 ATOM 2825 C C . GLN A 1 364 ? 12.313 -41.859 -25.667 1.00 89.36 ? 394 GLN A C 1 ATOM 2826 O O . GLN A 1 364 ? 13.228 -41.090 -25.939 1.00 91.34 ? 394 GLN A O 1 ATOM 2827 C CB . GLN A 1 364 ? 11.107 -43.202 -27.429 1.00 97.27 ? 394 GLN A CB 1 ATOM 2828 C CG . GLN A 1 364 ? 9.841 -43.456 -28.259 1.00 107.39 ? 394 GLN A CG 1 ATOM 2829 C CD . GLN A 1 364 ? 9.844 -42.794 -29.650 1.00 113.75 ? 394 GLN A CD 1 ATOM 2830 O OE1 . GLN A 1 364 ? 9.840 -41.564 -29.778 1.00 116.28 ? 394 GLN A OE1 1 ATOM 2831 N NE2 . GLN A 1 364 ? 9.837 -43.612 -30.694 1.00 113.87 ? 394 GLN A NE2 1 ATOM 2832 N N . ARG A 1 365 ? 12.355 -42.658 -24.608 1.00 85.86 ? 395 ARG A N 1 ATOM 2833 C CA . ARG A 1 365 ? 13.462 -42.600 -23.650 1.00 79.92 ? 395 ARG A CA 1 ATOM 2834 C C . ARG A 1 365 ? 14.778 -43.072 -24.251 1.00 77.70 ? 395 ARG A C 1 ATOM 2835 O O . ARG A 1 365 ? 14.854 -44.180 -24.757 1.00 78.77 ? 395 ARG A O 1 ATOM 2836 C CB . ARG A 1 365 ? 13.144 -43.438 -22.419 1.00 78.08 ? 395 ARG A CB 1 ATOM 2837 C CG . ARG A 1 365 ? 14.019 -43.153 -21.210 1.00 76.14 ? 395 ARG A CG 1 ATOM 2838 C CD . ARG A 1 365 ? 13.696 -44.137 -20.087 1.00 77.27 ? 395 ARG A CD 1 ATOM 2839 N NE . ARG A 1 365 ? 14.125 -43.671 -18.768 1.00 71.95 ? 395 ARG A NE 1 ATOM 2840 C CZ . ARG A 1 365 ? 15.300 -43.917 -18.209 1.00 69.18 ? 395 ARG A CZ 1 ATOM 2841 N NH1 . ARG A 1 365 ? 16.222 -44.637 -18.835 1.00 71.64 ? 395 ARG A NH1 1 ATOM 2842 N NH2 . ARG A 1 365 ? 15.558 -43.425 -17.006 1.00 65.80 ? 395 ARG A NH2 1 ATOM 2843 N N . ARG A 1 366 ? 15.813 -42.245 -24.171 1.00 77.49 ? 396 ARG A N 1 ATOM 2844 C CA . ARG A 1 366 ? 17.125 -42.596 -24.723 1.00 80.55 ? 396 ARG A CA 1 ATOM 2845 C C . ARG A 1 366 ? 18.264 -42.006 -23.893 1.00 75.62 ? 396 ARG A C 1 ATOM 2846 O O . ARG A 1 366 ? 18.017 -41.236 -22.970 1.00 77.81 ? 396 ARG A O 1 ATOM 2847 C CB . ARG A 1 366 ? 17.240 -42.098 -26.178 1.00 88.00 ? 396 ARG A CB 1 ATOM 2848 C CG . ARG A 1 366 ? 16.878 -40.635 -26.343 1.00 93.62 ? 396 ARG A CG 1 ATOM 2849 C CD . ARG A 1 366 ? 17.583 -39.942 -27.490 1.00 98.71 ? 396 ARG A CD 1 ATOM 2850 N NE . ARG A 1 366 ? 17.300 -38.504 -27.434 1.00 105.60 ? 396 ARG A NE 1 ATOM 2851 C CZ . ARG A 1 366 ? 18.097 -37.569 -26.909 1.00 109.31 ? 396 ARG A CZ 1 ATOM 2852 N NH1 . ARG A 1 366 ? 19.279 -37.873 -26.386 1.00 107.87 ? 396 ARG A NH1 1 ATOM 2853 N NH2 . ARG A 1 366 ? 17.709 -36.302 -26.918 1.00 112.41 ? 396 ARG A NH2 1 ATOM 2854 N N . PRO A 1 367 ? 19.516 -42.372 -24.220 1.00 72.23 ? 397 PRO A N 1 ATOM 2855 C CA . PRO A 1 367 ? 20.726 -41.724 -23.717 1.00 68.19 ? 397 PRO A CA 1 ATOM 2856 C C . PRO A 1 367 ? 20.818 -40.268 -24.097 1.00 67.58 ? 397 PRO A C 1 ATOM 2857 O O . PRO A 1 367 ? 20.130 -39.842 -24.998 1.00 71.10 ? 397 PRO A O 1 ATOM 2858 C CB . PRO A 1 367 ? 21.838 -42.478 -24.437 1.00 68.98 ? 397 PRO A CB 1 ATOM 2859 C CG . PRO A 1 367 ? 21.293 -43.843 -24.653 1.00 70.97 ? 397 PRO A CG 1 ATOM 2860 C CD . PRO A 1 367 ? 19.810 -43.699 -24.794 1.00 73.50 ? 397 PRO A CD 1 ATOM 2861 N N . TRP A 1 368 ? 21.666 -39.515 -23.413 1.00 68.31 ? 398 TRP A N 1 ATOM 2862 C CA . TRP A 1 368 ? 22.128 -38.220 -23.911 1.00 70.37 ? 398 TRP A CA 1 ATOM 2863 C C . TRP A 1 368 ? 23.598 -38.032 -23.563 1.00 70.75 ? 398 TRP A C 1 ATOM 2864 O O . TRP A 1 368 ? 24.052 -38.461 -22.500 1.00 72.20 ? 398 TRP A O 1 ATOM 2865 C CB . TRP A 1 368 ? 21.268 -37.065 -23.406 1.00 68.26 ? 398 TRP A CB 1 ATOM 2866 C CG . TRP A 1 368 ? 21.312 -36.810 -21.953 1.00 69.02 ? 398 TRP A CG 1 ATOM 2867 C CD1 . TRP A 1 368 ? 20.593 -37.448 -20.977 1.00 71.87 ? 398 TRP A CD1 1 ATOM 2868 C CD2 . TRP A 1 368 ? 22.071 -35.802 -21.287 1.00 69.25 ? 398 TRP A CD2 1 ATOM 2869 N NE1 . TRP A 1 368 ? 20.881 -36.910 -19.741 1.00 69.38 ? 398 TRP A NE1 1 ATOM 2870 C CE2 . TRP A 1 368 ? 21.778 -35.892 -19.910 1.00 67.80 ? 398 TRP A CE2 1 ATOM 2871 C CE3 . TRP A 1 368 ? 22.982 -34.836 -21.720 1.00 71.73 ? 398 TRP A CE3 1 ATOM 2872 C CZ2 . TRP A 1 368 ? 22.362 -35.058 -18.969 1.00 68.81 ? 398 TRP A CZ2 1 ATOM 2873 C CZ3 . TRP A 1 368 ? 23.564 -34.004 -20.780 1.00 72.80 ? 398 TRP A CZ3 1 ATOM 2874 C CH2 . TRP A 1 368 ? 23.253 -34.123 -19.418 1.00 70.40 ? 398 TRP A CH2 1 ATOM 2875 N N . LEU A 1 369 ? 24.340 -37.399 -24.465 1.00 70.67 ? 399 LEU A N 1 ATOM 2876 C CA . LEU A 1 369 ? 25.797 -37.426 -24.399 1.00 72.27 ? 399 LEU A CA 1 ATOM 2877 C C . LEU A 1 369 ? 26.445 -36.101 -24.009 1.00 74.12 ? 399 LEU A C 1 ATOM 2878 O O . LEU A 1 369 ? 25.830 -35.033 -24.078 1.00 75.54 ? 399 LEU A O 1 ATOM 2879 C CB . LEU A 1 369 ? 26.360 -37.889 -25.748 1.00 74.52 ? 399 LEU A CB 1 ATOM 2880 C CG . LEU A 1 369 ? 25.736 -39.145 -26.362 1.00 74.70 ? 399 LEU A CG 1 ATOM 2881 C CD1 . LEU A 1 369 ? 26.349 -39.447 -27.721 1.00 74.65 ? 399 LEU A CD1 1 ATOM 2882 C CD2 . LEU A 1 369 ? 25.899 -40.318 -25.420 1.00 73.82 ? 399 LEU A CD2 1 ATOM 2883 N N . VAL A 1 370 ? 27.700 -36.187 -23.595 1.00 74.01 ? 400 VAL A N 1 ATOM 2884 C CA . VAL A 1 370 ? 28.522 -35.024 -23.302 1.00 73.80 ? 400 VAL A CA 1 ATOM 2885 C C . VAL A 1 370 ? 29.931 -35.316 -23.810 1.00 73.45 ? 400 VAL A C 1 ATOM 2886 O O . VAL A 1 370 ? 30.398 -36.442 -23.715 1.00 75.90 ? 400 VAL A O 1 ATOM 2887 C CB . VAL A 1 370 ? 28.536 -34.722 -21.784 1.00 72.77 ? 400 VAL A CB 1 ATOM 2888 C CG1 . VAL A 1 370 ? 29.594 -33.682 -21.442 1.00 72.86 ? 400 VAL A CG1 1 ATOM 2889 C CG2 . VAL A 1 370 ? 27.169 -34.239 -21.338 1.00 70.87 ? 400 VAL A CG2 1 ATOM 2890 N N . LYS A 1 371 ? 30.583 -34.311 -24.370 1.00 74.98 ? 401 LYS A N 1 ATOM 2891 C CA . LYS A 1 371 ? 31.943 -34.451 -24.857 1.00 83.43 ? 401 LYS A CA 1 ATOM 2892 C C . LYS A 1 371 ? 32.909 -34.075 -23.752 1.00 84.31 ? 401 LYS A C 1 ATOM 2893 O O . LYS A 1 371 ? 32.770 -33.014 -23.150 1.00 91.26 ? 401 LYS A O 1 ATOM 2894 C CB . LYS A 1 371 ? 32.175 -33.554 -26.073 1.00 90.89 ? 401 LYS A CB 1 ATOM 2895 C CG . LYS A 1 371 ? 33.434 -33.883 -26.861 1.00 98.53 ? 401 LYS A CG 1 ATOM 2896 C CD . LYS A 1 371 ? 33.480 -33.122 -28.182 1.00 104.68 ? 401 LYS A CD 1 ATOM 2897 C CE . LYS A 1 371 ? 34.644 -33.566 -29.055 1.00 105.43 ? 401 LYS A CE 1 ATOM 2898 N NZ . LYS A 1 371 ? 34.408 -33.261 -30.489 1.00 106.37 ? 401 LYS A NZ 1 ATOM 2899 N N . TYR A 1 372 ? 33.869 -34.946 -23.466 1.00 84.14 ? 402 TYR A N 1 ATOM 2900 C CA . TYR A 1 372 ? 34.898 -34.669 -22.475 1.00 84.33 ? 402 TYR A CA 1 ATOM 2901 C C . TYR A 1 372 ? 36.278 -34.596 -23.111 1.00 92.59 ? 402 TYR A C 1 ATOM 2902 O O . TYR A 1 372 ? 36.508 -35.137 -24.194 1.00 101.12 ? 402 TYR A O 1 ATOM 2903 C CB . TYR A 1 372 ? 34.874 -35.748 -21.398 1.00 82.46 ? 402 TYR A CB 1 ATOM 2904 C CG . TYR A 1 372 ? 33.625 -35.717 -20.541 1.00 78.81 ? 402 TYR A CG 1 ATOM 2905 C CD1 . TYR A 1 372 ? 33.484 -34.781 -19.514 1.00 76.46 ? 402 TYR A CD1 1 ATOM 2906 C CD2 . TYR A 1 372 ? 32.592 -36.621 -20.753 1.00 76.43 ? 402 TYR A CD2 1 ATOM 2907 C CE1 . TYR A 1 372 ? 32.351 -34.744 -18.728 1.00 73.33 ? 402 TYR A CE1 1 ATOM 2908 C CE2 . TYR A 1 372 ? 31.457 -36.592 -19.973 1.00 76.04 ? 402 TYR A CE2 1 ATOM 2909 C CZ . TYR A 1 372 ? 31.339 -35.657 -18.963 1.00 76.67 ? 402 TYR A CZ 1 ATOM 2910 O OH . TYR A 1 372 ? 30.194 -35.632 -18.193 1.00 77.31 ? 402 TYR A OH 1 ATOM 2911 N N . GLY A 1 373 ? 37.196 -33.920 -22.433 1.00 103.39 ? 403 GLY A N 1 ATOM 2912 C CA . GLY A 1 373 ? 38.597 -33.845 -22.863 1.00 111.35 ? 403 GLY A CA 1 ATOM 2913 C C . GLY A 1 373 ? 39.279 -35.200 -22.788 1.00 116.44 ? 403 GLY A C 1 ATOM 2914 O O . GLY A 1 373 ? 39.394 -35.780 -21.706 1.00 118.31 ? 403 GLY A O 1 ATOM 2915 N N . ASP A 1 374 ? 39.698 -35.711 -23.947 1.00 121.88 ? 404 ASP A N 1 ATOM 2916 C CA . ASP A 1 374 ? 40.342 -37.029 -24.085 1.00 127.10 ? 404 ASP A CA 1 ATOM 2917 C C . ASP A 1 374 ? 39.338 -38.188 -24.079 1.00 121.39 ? 404 ASP A C 1 ATOM 2918 O O . ASP A 1 374 ? 39.396 -39.056 -24.960 1.00 120.93 ? 404 ASP A O 1 ATOM 2919 C CB . ASP A 1 374 ? 41.435 -37.249 -23.022 1.00 131.35 ? 404 ASP A CB 1 ATOM 2920 C CG . ASP A 1 374 ? 42.407 -38.360 -23.399 1.00 135.90 ? 404 ASP A CG 1 ATOM 2921 O OD1 . ASP A 1 374 ? 42.323 -39.454 -22.800 1.00 134.54 ? 404 ASP A OD1 1 ATOM 2922 O OD2 . ASP A 1 374 ? 43.248 -38.139 -24.296 1.00 135.92 ? 404 ASP A OD2 1 ATOM 2923 N N . SER A 1 375 ? 38.422 -38.196 -23.107 1.00 110.23 ? 405 SER A N 1 ATOM 2924 C CA . SER A 1 375 ? 37.426 -39.264 -22.978 1.00 103.39 ? 405 SER A CA 1 ATOM 2925 C C . SER A 1 375 ? 36.469 -39.396 -24.170 1.00 101.26 ? 405 SER A C 1 ATOM 2926 O O . SER A 1 375 ? 35.853 -40.435 -24.341 1.00 101.83 ? 405 SER A O 1 ATOM 2927 C CB . SER A 1 375 ? 36.598 -39.078 -21.707 1.00 101.23 ? 405 SER A CB 1 ATOM 2928 O OG . SER A 1 375 ? 37.354 -39.376 -20.555 1.00 100.96 ? 405 SER A OG 1 ATOM 2929 N N . GLY A 1 376 ? 36.346 -38.361 -24.994 1.00 98.38 ? 406 GLY A N 1 ATOM 2930 C CA . GLY A 1 376 ? 35.392 -38.379 -26.101 1.00 94.58 ? 406 GLY A CA 1 ATOM 2931 C C . GLY A 1 376 ? 33.974 -38.215 -25.582 1.00 93.63 ? 406 GLY A C 1 ATOM 2932 O O . GLY A 1 376 ? 33.765 -37.725 -24.464 1.00 92.26 ? 406 GLY A O 1 ATOM 2933 N N . GLU A 1 377 ? 32.996 -38.625 -26.383 1.00 87.64 ? 407 GLU A N 1 ATOM 2934 C CA . GLU A 1 377 ? 31.616 -38.547 -25.954 1.00 84.43 ? 407 GLU A CA 1 ATOM 2935 C C . GLU A 1 377 ? 31.287 -39.647 -24.932 1.00 81.75 ? 407 GLU A C 1 ATOM 2936 O O . GLU A 1 377 ? 31.731 -40.795 -25.053 1.00 81.38 ? 407 GLU A O 1 ATOM 2937 C CB . GLU A 1 377 ? 30.662 -38.592 -27.146 1.00 87.42 ? 407 GLU A CB 1 ATOM 2938 C CG . GLU A 1 377 ? 30.630 -37.295 -27.935 1.00 91.65 ? 407 GLU A CG 1 ATOM 2939 C CD . GLU A 1 377 ? 29.283 -37.010 -28.586 1.00 93.94 ? 407 GLU A CD 1 ATOM 2940 O OE1 . GLU A 1 377 ? 28.810 -37.835 -29.399 1.00 96.71 ? 407 GLU A OE1 1 ATOM 2941 O OE2 . GLU A 1 377 ? 28.706 -35.945 -28.303 1.00 94.93 ? 407 GLU A OE2 1 ATOM 2942 N N . GLN A 1 378 ? 30.524 -39.274 -23.912 1.00 74.65 ? 408 GLN A N 1 ATOM 2943 C CA . GLN A 1 378 ? 30.057 -40.219 -22.918 1.00 72.92 ? 408 GLN A CA 1 ATOM 2944 C C . GLN A 1 378 ? 28.584 -40.054 -22.684 1.00 71.57 ? 408 GLN A C 1 ATOM 2945 O O . GLN A 1 378 ? 27.983 -39.045 -23.051 1.00 74.38 ? 408 GLN A O 1 ATOM 2946 C CB . GLN A 1 378 ? 30.775 -39.997 -21.594 1.00 72.70 ? 408 GLN A CB 1 ATOM 2947 C CG . GLN A 1 378 ? 32.257 -40.312 -21.623 1.00 73.29 ? 408 GLN A CG 1 ATOM 2948 C CD . GLN A 1 378 ? 32.556 -41.794 -21.821 1.00 73.24 ? 408 GLN A CD 1 ATOM 2949 O OE1 . GLN A 1 378 ? 31.719 -42.670 -21.557 1.00 71.33 ? 408 GLN A OE1 1 ATOM 2950 N NE2 . GLN A 1 378 ? 33.761 -42.081 -22.271 1.00 72.91 ? 408 GLN A NE2 1 ATOM 2951 N N . ILE A 1 379 ? 28.007 -41.042 -22.032 1.00 68.45 ? 409 ILE A N 1 ATOM 2952 C CA . ILE A 1 379 ? 26.625 -40.970 -21.624 1.00 67.04 ? 409 ILE A CA 1 ATOM 2953 C C . ILE A 1 379 ? 26.539 -40.207 -20.301 1.00 65.22 ? 409 ILE A C 1 ATOM 2954 O O . ILE A 1 379 ? 27.091 -40.630 -19.290 1.00 59.87 ? 409 ILE A O 1 ATOM 2955 C CB . ILE A 1 379 ? 26.050 -42.377 -21.504 1.00 68.43 ? 409 ILE A CB 1 ATOM 2956 C CG1 . ILE A 1 379 ? 25.900 -42.961 -22.914 1.00 72.26 ? 409 ILE A CG1 1 ATOM 2957 C CG2 . ILE A 1 379 ? 24.717 -42.358 -20.785 1.00 69.47 ? 409 ILE A CG2 1 ATOM 2958 C CD1 . ILE A 1 379 ? 25.670 -44.448 -22.926 1.00 74.69 ? 409 ILE A CD1 1 ATOM 2959 N N . ALA A 1 380 ? 25.858 -39.071 -20.319 1.00 64.71 ? 410 ALA A N 1 ATOM 2960 C CA . ALA A 1 380 ? 25.699 -38.252 -19.116 1.00 64.12 ? 410 ALA A CA 1 ATOM 2961 C C . ALA A 1 380 ? 24.461 -38.663 -18.332 1.00 64.28 ? 410 ALA A C 1 ATOM 2962 O O . ALA A 1 380 ? 24.391 -38.457 -17.130 1.00 66.39 ? 410 ALA A O 1 ATOM 2963 C CB . ALA A 1 380 ? 25.636 -36.776 -19.479 1.00 62.90 ? 410 ALA A CB 1 ATOM 2964 N N . GLY A 1 381 ? 23.500 -39.251 -19.021 1.00 65.91 ? 411 GLY A N 1 ATOM 2965 C CA . GLY A 1 381 ? 22.299 -39.782 -18.394 1.00 68.12 ? 411 GLY A CA 1 ATOM 2966 C C . GLY A 1 381 ? 21.259 -40.193 -19.434 1.00 68.10 ? 411 GLY A C 1 ATOM 2967 O O . GLY A 1 381 ? 21.585 -40.383 -20.611 1.00 68.62 ? 411 GLY A O 1 ATOM 2968 N N . PHE A 1 382 ? 20.007 -40.313 -18.998 1.00 65.02 ? 412 PHE A N 1 ATOM 2969 C CA . PHE A 1 382 ? 18.913 -40.660 -19.883 1.00 64.30 ? 412 PHE A CA 1 ATOM 2970 C C . PHE A 1 382 ? 17.859 -39.577 -19.887 1.00 68.14 ? 412 PHE A C 1 ATOM 2971 O O . PHE A 1 382 ? 17.696 -38.889 -18.885 1.00 71.02 ? 412 PHE A O 1 ATOM 2972 C CB . PHE A 1 382 ? 18.336 -41.993 -19.465 1.00 61.04 ? 412 PHE A CB 1 ATOM 2973 C CG . PHE A 1 382 ? 19.249 -43.126 -19.758 1.00 61.48 ? 412 PHE A CG 1 ATOM 2974 C CD1 . PHE A 1 382 ? 20.276 -43.441 -18.887 1.00 61.28 ? 412 PHE A CD1 1 ATOM 2975 C CD2 . PHE A 1 382 ? 19.145 -43.824 -20.947 1.00 63.37 ? 412 PHE A CD2 1 ATOM 2976 C CE1 . PHE A 1 382 ? 21.142 -44.469 -19.176 1.00 62.23 ? 412 PHE A CE1 1 ATOM 2977 C CE2 . PHE A 1 382 ? 20.016 -44.851 -21.245 1.00 63.98 ? 412 PHE A CE2 1 ATOM 2978 C CZ . PHE A 1 382 ? 21.015 -45.178 -20.359 1.00 62.68 ? 412 PHE A CZ 1 ATOM 2979 N N . VAL A 1 383 ? 17.161 -39.427 -21.015 1.00 69.95 ? 413 VAL A N 1 ATOM 2980 C CA . VAL A 1 383 ? 16.116 -38.411 -21.167 1.00 71.25 ? 413 VAL A CA 1 ATOM 2981 C C . VAL A 1 383 ? 14.855 -38.944 -21.853 1.00 75.02 ? 413 VAL A C 1 ATOM 2982 O O . VAL A 1 383 ? 14.935 -39.698 -22.820 1.00 81.29 ? 413 VAL A O 1 ATOM 2983 C CB . VAL A 1 383 ? 16.638 -37.190 -21.939 1.00 69.92 ? 413 VAL A CB 1 ATOM 2984 C CG1 . VAL A 1 383 ? 16.970 -37.556 -23.372 1.00 70.56 ? 413 VAL A CG1 1 ATOM 2985 C CG2 . VAL A 1 383 ? 15.637 -36.044 -21.889 1.00 70.12 ? 413 VAL A CG2 1 ATOM 2986 N N . LYS A 1 384 ? 13.702 -38.522 -21.340 1.00 75.56 ? 414 LYS A N 1 ATOM 2987 C CA . LYS A 1 384 ? 12.393 -38.946 -21.805 1.00 76.08 ? 414 LYS A CA 1 ATOM 2988 C C . LYS A 1 384 ? 11.604 -37.676 -22.015 1.00 77.77 ? 414 LYS A C 1 ATOM 2989 O O . LYS A 1 384 ? 11.304 -36.998 -21.048 1.00 81.49 ? 414 LYS A O 1 ATOM 2990 C CB . LYS A 1 384 ? 11.739 -39.811 -20.724 1.00 79.63 ? 414 LYS A CB 1 ATOM 2991 C CG . LYS A 1 384 ? 10.479 -40.572 -21.117 1.00 85.34 ? 414 LYS A CG 1 ATOM 2992 C CD . LYS A 1 384 ? 9.883 -41.306 -19.918 1.00 86.29 ? 414 LYS A CD 1 ATOM 2993 C CE . LYS A 1 384 ? 8.867 -42.375 -20.319 1.00 92.64 ? 414 LYS A CE 1 ATOM 2994 N NZ . LYS A 1 384 ? 9.431 -43.759 -20.447 1.00 94.17 ? 414 LYS A NZ 1 ATOM 2995 N N . GLU A 1 385 ? 11.285 -37.326 -23.260 1.00 80.59 ? 415 GLU A N 1 ATOM 2996 C CA . GLU A 1 385 ? 10.571 -36.073 -23.539 1.00 82.28 ? 415 GLU A CA 1 ATOM 2997 C C . GLU A 1 385 ? 9.070 -36.253 -23.789 1.00 82.32 ? 415 GLU A C 1 ATOM 2998 O O . GLU A 1 385 ? 8.639 -37.219 -24.404 1.00 91.61 ? 415 GLU A O 1 ATOM 2999 C CB . GLU A 1 385 ? 11.201 -35.325 -24.725 1.00 85.68 ? 415 GLU A CB 1 ATOM 3000 C CG . GLU A 1 385 ? 12.612 -34.806 -24.457 1.00 85.57 ? 415 GLU A CG 1 ATOM 3001 C CD . GLU A 1 385 ? 13.005 -33.613 -25.323 1.00 85.46 ? 415 GLU A CD 1 ATOM 3002 O OE1 . GLU A 1 385 ? 12.420 -32.522 -25.180 1.00 81.16 ? 415 GLU A OE1 1 ATOM 3003 O OE2 . GLU A 1 385 ? 13.927 -33.762 -26.142 1.00 91.03 ? 415 GLU A OE2 1 ATOM 3004 N N . PHE A 1 386 ? 8.291 -35.311 -23.281 1.00 77.26 ? 416 PHE A N 1 ATOM 3005 C CA . PHE A 1 386 ? 6.889 -35.145 -23.625 1.00 78.10 ? 416 PHE A CA 1 ATOM 3006 C C . PHE A 1 386 ? 6.742 -33.740 -24.225 1.00 77.39 ? 416 PHE A C 1 ATOM 3007 O O . PHE A 1 386 ? 7.689 -32.963 -24.198 1.00 73.53 ? 416 PHE A O 1 ATOM 3008 C CB . PHE A 1 386 ? 6.010 -35.289 -22.371 1.00 80.06 ? 416 PHE A CB 1 ATOM 3009 C CG . PHE A 1 386 ? 6.129 -36.620 -21.681 1.00 79.29 ? 416 PHE A CG 1 ATOM 3010 C CD1 . PHE A 1 386 ? 7.106 -36.841 -20.708 1.00 74.14 ? 416 PHE A CD1 1 ATOM 3011 C CD2 . PHE A 1 386 ? 5.245 -37.647 -21.984 1.00 78.61 ? 416 PHE A CD2 1 ATOM 3012 C CE1 . PHE A 1 386 ? 7.207 -38.071 -20.080 1.00 72.73 ? 416 PHE A CE1 1 ATOM 3013 C CE2 . PHE A 1 386 ? 5.351 -38.879 -21.362 1.00 76.84 ? 416 PHE A CE2 1 ATOM 3014 C CZ . PHE A 1 386 ? 6.325 -39.093 -20.408 1.00 74.29 ? 416 PHE A CZ 1 ATOM 3015 N N . SER A 1 387 ? 5.561 -33.382 -24.722 1.00 80.91 ? 417 SER A N 1 ATOM 3016 C CA . SER A 1 387 ? 5.379 -32.015 -25.232 1.00 81.73 ? 417 SER A CA 1 ATOM 3017 C C . SER A 1 387 ? 5.444 -31.045 -24.039 1.00 80.84 ? 417 SER A C 1 ATOM 3018 O O . SER A 1 387 ? 4.634 -31.118 -23.086 1.00 79.85 ? 417 SER A O 1 ATOM 3019 C CB . SER A 1 387 ? 4.098 -31.828 -26.048 1.00 81.11 ? 417 SER A CB 1 ATOM 3020 O OG . SER A 1 387 ? 2.989 -31.642 -25.204 1.00 79.31 ? 417 SER A OG 1 ATOM 3021 N N . HIS A 1 388 ? 6.456 -30.196 -24.076 1.00 80.70 ? 418 HIS A N 1 ATOM 3022 C CA . HIS A 1 388 ? 6.673 -29.146 -23.076 1.00 85.54 ? 418 HIS A CA 1 ATOM 3023 C C . HIS A 1 388 ? 7.243 -29.615 -21.752 1.00 87.35 ? 418 HIS A C 1 ATOM 3024 O O . HIS A 1 388 ? 7.560 -28.790 -20.901 1.00 98.32 ? 418 HIS A O 1 ATOM 3025 C CB . HIS A 1 388 ? 5.404 -28.327 -22.793 1.00 85.03 ? 418 HIS A CB 1 ATOM 3026 C CG . HIS A 1 388 ? 4.892 -27.595 -23.986 1.00 87.73 ? 418 HIS A CG 1 ATOM 3027 N ND1 . HIS A 1 388 ? 4.007 -28.156 -24.876 1.00 91.11 ? 418 HIS A ND1 1 ATOM 3028 C CD2 . HIS A 1 388 ? 5.169 -26.360 -24.460 1.00 87.36 ? 418 HIS A CD2 1 ATOM 3029 C CE1 . HIS A 1 388 ? 3.745 -27.293 -25.839 1.00 92.66 ? 418 HIS A CE1 1 ATOM 3030 N NE2 . HIS A 1 388 ? 4.438 -26.196 -25.610 1.00 90.73 ? 418 HIS A NE2 1 ATOM 3031 N N . ILE A 1 389 ? 7.379 -30.917 -21.552 1.00 86.55 ? 419 ILE A N 1 ATOM 3032 C CA . ILE A 1 389 ? 7.954 -31.403 -20.303 1.00 82.59 ? 419 ILE A CA 1 ATOM 3033 C C . ILE A 1 389 ? 8.864 -32.596 -20.532 1.00 81.00 ? 419 ILE A C 1 ATOM 3034 O O . ILE A 1 389 ? 8.468 -33.590 -21.140 1.00 84.16 ? 419 ILE A O 1 ATOM 3035 C CB . ILE A 1 389 ? 6.875 -31.742 -19.261 1.00 84.05 ? 419 ILE A CB 1 ATOM 3036 C CG1 . ILE A 1 389 ? 7.513 -32.060 -17.907 1.00 80.01 ? 419 ILE A CG1 1 ATOM 3037 C CG2 . ILE A 1 389 ? 5.995 -32.895 -19.726 1.00 86.98 ? 419 ILE A CG2 1 ATOM 3038 C CD1 . ILE A 1 389 ? 6.559 -31.883 -16.755 1.00 79.64 ? 419 ILE A CD1 1 ATOM 3039 N N . ALA A 1 390 ? 10.084 -32.480 -20.028 1.00 75.19 ? 420 ALA A N 1 ATOM 3040 C CA . ALA A 1 390 ? 11.091 -33.503 -20.175 1.00 72.33 ? 420 ALA A CA 1 ATOM 3041 C C . ALA A 1 390 ? 11.495 -34.000 -18.817 1.00 69.29 ? 420 ALA A C 1 ATOM 3042 O O . ALA A 1 390 ? 11.582 -33.202 -17.882 1.00 69.15 ? 420 ALA A O 1 ATOM 3043 C CB . ALA A 1 390 ? 12.305 -32.912 -20.866 1.00 72.80 ? 420 ALA A CB 1 ATOM 3044 N N . PHE A 1 391 ? 11.772 -35.298 -18.705 1.00 66.05 ? 421 PHE A N 1 ATOM 3045 C CA . PHE A 1 391 ? 12.503 -35.826 -17.555 1.00 61.41 ? 421 PHE A CA 1 ATOM 3046 C C . PHE A 1 391 ? 13.885 -36.279 -17.960 1.00 63.28 ? 421 PHE A C 1 ATOM 3047 O O . PHE A 1 391 ? 14.064 -36.874 -19.003 1.00 68.25 ? 421 PHE A O 1 ATOM 3048 C CB . PHE A 1 391 ? 11.794 -36.991 -16.908 1.00 58.44 ? 421 PHE A CB 1 ATOM 3049 C CG . PHE A 1 391 ? 12.550 -37.564 -15.751 1.00 55.30 ? 421 PHE A CG 1 ATOM 3050 C CD1 . PHE A 1 391 ? 12.623 -36.883 -14.552 1.00 52.81 ? 421 PHE A CD1 1 ATOM 3051 C CD2 . PHE A 1 391 ? 13.240 -38.750 -15.881 1.00 54.28 ? 421 PHE A CD2 1 ATOM 3052 C CE1 . PHE A 1 391 ? 13.336 -37.399 -13.485 1.00 51.16 ? 421 PHE A CE1 1 ATOM 3053 C CE2 . PHE A 1 391 ? 13.960 -39.257 -14.829 1.00 53.96 ? 421 PHE A CE2 1 ATOM 3054 C CZ . PHE A 1 391 ? 14.000 -38.588 -13.618 1.00 51.41 ? 421 PHE A CZ 1 ATOM 3055 N N . LEU A 1 392 ? 14.859 -36.059 -17.099 1.00 63.57 ? 422 LEU A N 1 ATOM 3056 C CA . LEU A 1 392 ? 16.221 -36.340 -17.471 1.00 64.56 ? 422 LEU A CA 1 ATOM 3057 C C . LEU A 1 392 ? 17.049 -36.675 -16.238 1.00 62.53 ? 422 LEU A C 1 ATOM 3058 O O . LEU A 1 392 ? 16.891 -36.021 -15.219 1.00 63.23 ? 422 LEU A O 1 ATOM 3059 C CB . LEU A 1 392 ? 16.745 -35.103 -18.186 1.00 68.34 ? 422 LEU A CB 1 ATOM 3060 C CG . LEU A 1 392 ? 18.192 -35.005 -18.601 1.00 68.25 ? 422 LEU A CG 1 ATOM 3061 C CD1 . LEU A 1 392 ? 18.266 -34.276 -19.924 1.00 74.23 ? 422 LEU A CD1 1 ATOM 3062 C CD2 . LEU A 1 392 ? 19.006 -34.285 -17.559 1.00 66.19 ? 422 LEU A CD2 1 ATOM 3063 N N . THR A 1 393 ? 17.921 -37.678 -16.336 1.00 59.47 ? 423 THR A N 1 ATOM 3064 C CA . THR A 1 393 ? 18.832 -38.027 -15.250 1.00 57.88 ? 423 THR A CA 1 ATOM 3065 C C . THR A 1 393 ? 20.255 -37.586 -15.529 1.00 59.15 ? 423 THR A C 1 ATOM 3066 O O . THR A 1 393 ? 20.627 -37.354 -16.676 1.00 61.49 ? 423 THR A O 1 ATOM 3067 C CB . THR A 1 393 ? 18.927 -39.534 -15.010 1.00 58.12 ? 423 THR A CB 1 ATOM 3068 O OG1 . THR A 1 393 ? 19.510 -40.162 -16.156 1.00 56.62 ? 423 THR A OG1 1 ATOM 3069 C CG2 . THR A 1 393 ? 17.559 -40.131 -14.699 1.00 59.28 ? 423 THR A CG2 1 ATOM 3070 N N . ILE A 1 394 ? 21.043 -37.489 -14.459 1.00 57.21 ? 424 ILE A N 1 ATOM 3071 C CA . ILE A 1 394 ? 22.469 -37.265 -14.563 1.00 56.83 ? 424 ILE A CA 1 ATOM 3072 C C . ILE A 1 394 ? 23.215 -38.420 -13.895 1.00 55.12 ? 424 ILE A C 1 ATOM 3073 O O . ILE A 1 394 ? 23.316 -38.507 -12.682 1.00 56.38 ? 424 ILE A O 1 ATOM 3074 C CB . ILE A 1 394 ? 22.878 -35.919 -13.960 1.00 58.24 ? 424 ILE A CB 1 ATOM 3075 C CG1 . ILE A 1 394 ? 22.276 -34.768 -14.767 1.00 61.72 ? 424 ILE A CG1 1 ATOM 3076 C CG2 . ILE A 1 394 ? 24.385 -35.765 -13.996 1.00 57.63 ? 424 ILE A CG2 1 ATOM 3077 C CD1 . ILE A 1 394 ? 20.807 -34.520 -14.538 1.00 60.77 ? 424 ILE A CD1 1 ATOM 3078 N N . LYS A 1 395 ? 23.742 -39.305 -14.712 1.00 57.17 ? 425 LYS A N 1 ATOM 3079 C CA . LYS A 1 395 ? 24.305 -40.536 -14.234 1.00 58.89 ? 425 LYS A CA 1 ATOM 3080 C C . LYS A 1 395 ? 25.478 -40.271 -13.312 1.00 59.70 ? 425 LYS A C 1 ATOM 3081 O O . LYS A 1 395 ? 26.355 -39.487 -13.644 1.00 62.58 ? 425 LYS A O 1 ATOM 3082 C CB . LYS A 1 395 ? 24.765 -41.369 -15.416 1.00 62.31 ? 425 LYS A CB 1 ATOM 3083 C CG . LYS A 1 395 ? 25.319 -42.718 -15.033 1.00 63.49 ? 425 LYS A CG 1 ATOM 3084 C CD . LYS A 1 395 ? 25.385 -43.617 -16.249 1.00 68.10 ? 425 LYS A CD 1 ATOM 3085 C CE . LYS A 1 395 ? 26.387 -43.126 -17.286 1.00 71.42 ? 425 LYS A CE 1 ATOM 3086 N NZ . LYS A 1 395 ? 27.770 -43.110 -16.753 1.00 74.46 ? 425 LYS A NZ 1 ATOM 3087 N N . GLY A 1 396 ? 25.484 -40.922 -12.157 1.00 58.11 ? 426 GLY A N 1 ATOM 3088 C CA . GLY A 1 396 ? 26.531 -40.735 -11.174 1.00 57.46 ? 426 GLY A CA 1 ATOM 3089 C C . GLY A 1 396 ? 26.554 -39.391 -10.464 1.00 56.21 ? 426 GLY A C 1 ATOM 3090 O O . GLY A 1 396 ? 27.578 -39.035 -9.893 1.00 60.09 ? 426 GLY A O 1 ATOM 3091 N N . ALA A 1 397 ? 25.454 -38.639 -10.496 1.00 51.74 ? 427 ALA A N 1 ATOM 3092 C CA . ALA A 1 397 ? 25.368 -37.377 -9.768 1.00 48.96 ? 427 ALA A CA 1 ATOM 3093 C C . ALA A 1 397 ? 24.418 -37.506 -8.587 1.00 50.07 ? 427 ALA A C 1 ATOM 3094 O O . ALA A 1 397 ? 23.445 -38.256 -8.626 1.00 51.39 ? 427 ALA A O 1 ATOM 3095 C CB . ALA A 1 397 ? 24.913 -36.258 -10.678 1.00 48.45 ? 427 ALA A CB 1 ATOM 3096 N N . GLY A 1 398 ? 24.693 -36.742 -7.542 1.00 50.15 ? 428 GLY A N 1 ATOM 3097 C CA . GLY A 1 398 ? 23.900 -36.778 -6.348 1.00 50.67 ? 428 GLY A CA 1 ATOM 3098 C C . GLY A 1 398 ? 22.860 -35.693 -6.345 1.00 53.76 ? 428 GLY A C 1 ATOM 3099 O O . GLY A 1 398 ? 22.450 -35.198 -7.400 1.00 50.21 ? 428 GLY A O 1 ATOM 3100 N N . HIS A 1 399 ? 22.440 -35.335 -5.128 1.00 56.79 ? 429 HIS A N 1 ATOM 3101 C CA . HIS A 1 399 ? 21.407 -34.336 -4.871 1.00 59.64 ? 429 HIS A CA 1 ATOM 3102 C C . HIS A 1 399 ? 21.757 -32.986 -5.480 1.00 62.02 ? 429 HIS A C 1 ATOM 3103 O O . HIS A 1 399 ? 20.863 -32.231 -5.856 1.00 71.21 ? 429 HIS A O 1 ATOM 3104 C CB . HIS A 1 399 ? 21.214 -34.181 -3.348 1.00 62.15 ? 429 HIS A CB 1 ATOM 3105 C CG . HIS A 1 399 ? 19.947 -33.493 -2.949 1.00 59.75 ? 429 HIS A CG 1 ATOM 3106 N ND1 . HIS A 1 399 ? 18.706 -33.982 -3.272 1.00 60.04 ? 429 HIS A ND1 1 ATOM 3107 C CD2 . HIS A 1 399 ? 19.733 -32.373 -2.228 1.00 58.98 ? 429 HIS A CD2 1 ATOM 3108 C CE1 . HIS A 1 399 ? 17.778 -33.173 -2.797 1.00 59.90 ? 429 HIS A CE1 1 ATOM 3109 N NE2 . HIS A 1 399 ? 18.374 -32.186 -2.163 1.00 60.03 ? 429 HIS A NE2 1 ATOM 3110 N N . MET A 1 400 ? 23.046 -32.681 -5.583 1.00 62.92 ? 430 MET A N 1 ATOM 3111 C CA . MET A 1 400 ? 23.478 -31.389 -6.106 1.00 62.84 ? 430 MET A CA 1 ATOM 3112 C C . MET A 1 400 ? 24.241 -31.590 -7.392 1.00 58.60 ? 430 MET A C 1 ATOM 3113 O O . MET A 1 400 ? 25.465 -31.685 -7.413 1.00 56.99 ? 430 MET A O 1 ATOM 3114 C CB . MET A 1 400 ? 24.291 -30.648 -5.059 1.00 67.19 ? 430 MET A CB 1 ATOM 3115 C CG . MET A 1 400 ? 23.391 -30.097 -3.966 1.00 71.27 ? 430 MET A CG 1 ATOM 3116 S SD . MET A 1 400 ? 24.234 -29.821 -2.401 1.00 81.34 ? 430 MET A SD 1 ATOM 3117 C CE . MET A 1 400 ? 25.461 -28.623 -2.909 1.00 80.40 ? 430 MET A CE 1 ATOM 3118 N N . VAL A 1 401 ? 23.472 -31.662 -8.464 1.00 56.55 ? 431 VAL A N 1 ATOM 3119 C CA . VAL A 1 401 ? 23.960 -32.029 -9.790 1.00 55.71 ? 431 VAL A CA 1 ATOM 3120 C C . VAL A 1 401 ? 25.149 -31.194 -10.245 1.00 53.58 ? 431 VAL A C 1 ATOM 3121 O O . VAL A 1 401 ? 26.198 -31.758 -10.540 1.00 54.75 ? 431 VAL A O 1 ATOM 3122 C CB . VAL A 1 401 ? 22.807 -31.982 -10.809 1.00 57.25 ? 431 VAL A CB 1 ATOM 3123 C CG1 . VAL A 1 401 ? 23.313 -31.889 -12.237 1.00 59.72 ? 431 VAL A CG1 1 ATOM 3124 C CG2 . VAL A 1 401 ? 21.904 -33.188 -10.613 1.00 57.91 ? 431 VAL A CG2 1 ATOM 3125 N N . PRO A 1 402 ? 25.015 -29.862 -10.260 1.00 52.54 ? 432 PRO A N 1 ATOM 3126 C CA . PRO A 1 402 ? 26.122 -29.012 -10.739 1.00 54.10 ? 432 PRO A CA 1 ATOM 3127 C C . PRO A 1 402 ? 27.440 -29.173 -9.996 1.00 57.16 ? 432 PRO A C 1 ATOM 3128 O O . PRO A 1 402 ? 28.482 -28.839 -10.555 1.00 63.29 ? 432 PRO A O 1 ATOM 3129 C CB . PRO A 1 402 ? 25.589 -27.588 -10.558 1.00 53.28 ? 432 PRO A CB 1 ATOM 3130 C CG . PRO A 1 402 ? 24.102 -27.725 -10.543 1.00 53.36 ? 432 PRO A CG 1 ATOM 3131 C CD . PRO A 1 402 ? 23.850 -29.052 -9.870 1.00 53.92 ? 432 PRO A CD 1 ATOM 3132 N N . THR A 1 403 ? 27.394 -29.659 -8.753 1.00 56.50 ? 433 THR A N 1 ATOM 3133 C CA . THR A 1 403 ? 28.604 -29.936 -7.968 1.00 56.66 ? 433 THR A CA 1 ATOM 3134 C C . THR A 1 403 ? 29.239 -31.258 -8.394 1.00 58.48 ? 433 THR A C 1 ATOM 3135 O O . THR A 1 403 ? 30.434 -31.329 -8.685 1.00 56.73 ? 433 THR A O 1 ATOM 3136 C CB . THR A 1 403 ? 28.295 -30.021 -6.450 1.00 55.24 ? 433 THR A CB 1 ATOM 3137 O OG1 . THR A 1 403 ? 27.499 -28.897 -6.049 1.00 55.12 ? 433 THR A OG1 1 ATOM 3138 C CG2 . THR A 1 403 ? 29.574 -30.070 -5.630 1.00 54.01 ? 433 THR A CG2 1 ATOM 3139 N N . ASP A 1 404 ? 28.430 -32.307 -8.410 1.00 59.07 ? 434 ASP A N 1 ATOM 3140 C CA . ASP A 1 404 ? 28.917 -33.624 -8.779 1.00 59.38 ? 434 ASP A CA 1 ATOM 3141 C C . ASP A 1 404 ? 29.300 -33.676 -10.286 1.00 58.67 ? 434 ASP A C 1 ATOM 3142 O O . ASP A 1 404 ? 30.335 -34.232 -10.623 1.00 58.18 ? 434 ASP A O 1 ATOM 3143 C CB . ASP A 1 404 ? 27.876 -34.685 -8.394 1.00 61.00 ? 434 ASP A CB 1 ATOM 3144 C CG . ASP A 1 404 ? 27.563 -34.694 -6.880 1.00 64.13 ? 434 ASP A CG 1 ATOM 3145 O OD1 . ASP A 1 404 ? 28.473 -34.428 -6.060 1.00 63.23 ? 434 ASP A OD1 1 ATOM 3146 O OD2 . ASP A 1 404 ? 26.400 -34.979 -6.494 1.00 67.09 ? 434 ASP A OD2 1 ATOM 3147 N N . LYS A 1 405 ? 28.500 -33.062 -11.168 1.00 56.95 ? 435 LYS A N 1 ATOM 3148 C CA . LYS A 1 405 ? 28.729 -33.099 -12.629 1.00 55.49 ? 435 LYS A CA 1 ATOM 3149 C C . LYS A 1 405 ? 28.459 -31.727 -13.241 1.00 59.96 ? 435 LYS A C 1 ATOM 3150 O O . LYS A 1 405 ? 27.398 -31.502 -13.831 1.00 61.33 ? 435 LYS A O 1 ATOM 3151 C CB . LYS A 1 405 ? 27.819 -34.113 -13.310 1.00 52.59 ? 435 LYS A CB 1 ATOM 3152 C CG . LYS A 1 405 ? 27.876 -35.529 -12.769 1.00 52.22 ? 435 LYS A CG 1 ATOM 3153 C CD . LYS A 1 405 ? 29.167 -36.250 -13.046 1.00 52.45 ? 435 LYS A CD 1 ATOM 3154 C CE . LYS A 1 405 ? 29.164 -37.620 -12.382 1.00 53.35 ? 435 LYS A CE 1 ATOM 3155 N NZ . LYS A 1 405 ? 30.277 -38.467 -12.893 1.00 55.27 ? 435 LYS A NZ 1 ATOM 3156 N N . PRO A 1 406 ? 29.406 -30.788 -13.091 1.00 60.86 ? 436 PRO A N 1 ATOM 3157 C CA . PRO A 1 406 ? 29.178 -29.441 -13.632 1.00 59.66 ? 436 PRO A CA 1 ATOM 3158 C C . PRO A 1 406 ? 28.970 -29.407 -15.156 1.00 60.83 ? 436 PRO A C 1 ATOM 3159 O O . PRO A 1 406 ? 28.015 -28.799 -15.641 1.00 62.90 ? 436 PRO A O 1 ATOM 3160 C CB . PRO A 1 406 ? 30.443 -28.671 -13.245 1.00 59.32 ? 436 PRO A CB 1 ATOM 3161 C CG . PRO A 1 406 ? 31.398 -29.663 -12.655 1.00 59.11 ? 436 PRO A CG 1 ATOM 3162 C CD . PRO A 1 406 ? 30.617 -30.873 -12.262 1.00 59.62 ? 436 PRO A CD 1 ATOM 3163 N N . LEU A 1 407 ? 29.843 -30.064 -15.902 1.00 61.23 ? 437 LEU A N 1 ATOM 3164 C CA . LEU A 1 407 ? 29.783 -29.970 -17.350 1.00 62.45 ? 437 LEU A CA 1 ATOM 3165 C C . LEU A 1 407 ? 28.456 -30.496 -17.870 1.00 64.81 ? 437 LEU A C 1 ATOM 3166 O O . LEU A 1 407 ? 27.815 -29.867 -18.723 1.00 63.76 ? 437 LEU A O 1 ATOM 3167 C CB . LEU A 1 407 ? 30.932 -30.725 -17.995 1.00 61.70 ? 437 LEU A CB 1 ATOM 3168 C CG . LEU A 1 407 ? 30.936 -30.677 -19.526 1.00 63.35 ? 437 LEU A CG 1 ATOM 3169 C CD1 . LEU A 1 407 ? 30.886 -29.263 -20.054 1.00 62.12 ? 437 LEU A CD1 1 ATOM 3170 C CD2 . LEU A 1 407 ? 32.167 -31.383 -20.061 1.00 66.78 ? 437 LEU A CD2 1 ATOM 3171 N N . ALA A 1 408 ? 28.052 -31.653 -17.356 1.00 64.00 ? 438 ALA A N 1 ATOM 3172 C CA . ALA A 1 408 ? 26.773 -32.232 -17.721 1.00 61.69 ? 438 ALA A CA 1 ATOM 3173 C C . ALA A 1 408 ? 25.646 -31.296 -17.339 1.00 62.72 ? 438 ALA A C 1 ATOM 3174 O O . ALA A 1 408 ? 24.700 -31.118 -18.100 1.00 68.54 ? 438 ALA A O 1 ATOM 3175 C CB . ALA A 1 408 ? 26.597 -33.583 -17.062 1.00 60.08 ? 438 ALA A CB 1 ATOM 3176 N N . ALA A 1 409 ? 25.756 -30.688 -16.164 1.00 62.78 ? 439 ALA A N 1 ATOM 3177 C CA . ALA A 1 409 ? 24.739 -29.763 -15.679 1.00 62.61 ? 439 ALA A CA 1 ATOM 3178 C C . ALA A 1 409 ? 24.639 -28.531 -16.556 1.00 64.54 ? 439 ALA A C 1 ATOM 3179 O O . ALA A 1 409 ? 23.554 -28.021 -16.803 1.00 65.35 ? 439 ALA A O 1 ATOM 3180 C CB . ALA A 1 409 ? 25.031 -29.360 -14.253 1.00 58.51 ? 439 ALA A CB 1 ATOM 3181 N N . PHE A 1 410 ? 25.780 -28.047 -17.019 1.00 68.72 ? 440 PHE A N 1 ATOM 3182 C CA . PHE A 1 410 ? 25.807 -26.870 -17.889 1.00 70.71 ? 440 PHE A CA 1 ATOM 3183 C C . PHE A 1 410 ? 25.195 -27.210 -19.236 1.00 70.33 ? 440 PHE A C 1 ATOM 3184 O O . PHE A 1 410 ? 24.333 -26.482 -19.726 1.00 74.70 ? 440 PHE A O 1 ATOM 3185 C CB . PHE A 1 410 ? 27.237 -26.346 -18.084 1.00 71.44 ? 440 PHE A CB 1 ATOM 3186 C CG . PHE A 1 410 ? 27.299 -25.108 -18.915 1.00 72.33 ? 440 PHE A CG 1 ATOM 3187 C CD1 . PHE A 1 410 ? 26.967 -23.872 -18.362 1.00 73.76 ? 440 PHE A CD1 1 ATOM 3188 C CD2 . PHE A 1 410 ? 27.640 -25.174 -20.250 1.00 71.82 ? 440 PHE A CD2 1 ATOM 3189 C CE1 . PHE A 1 410 ? 26.990 -22.725 -19.131 1.00 73.58 ? 440 PHE A CE1 1 ATOM 3190 C CE2 . PHE A 1 410 ? 27.675 -24.032 -21.025 1.00 72.95 ? 440 PHE A CE2 1 ATOM 3191 C CZ . PHE A 1 410 ? 27.343 -22.808 -20.469 1.00 75.71 ? 440 PHE A CZ 1 ATOM 3192 N N . THR A 1 411 ? 25.633 -28.324 -19.817 1.00 66.54 ? 441 THR A N 1 ATOM 3193 C CA . THR A 1 411 ? 25.119 -28.780 -21.108 1.00 64.78 ? 441 THR A CA 1 ATOM 3194 C C . THR A 1 411 ? 23.610 -28.869 -21.079 1.00 65.06 ? 441 THR A C 1 ATOM 3195 O O . THR A 1 411 ? 22.925 -28.339 -21.953 1.00 67.27 ? 441 THR A O 1 ATOM 3196 C CB . THR A 1 411 ? 25.665 -30.160 -21.466 1.00 61.95 ? 441 THR A CB 1 ATOM 3197 O OG1 . THR A 1 411 ? 27.077 -30.085 -21.649 1.00 62.09 ? 441 THR A OG1 1 ATOM 3198 C CG2 . THR A 1 411 ? 25.040 -30.647 -22.717 1.00 62.92 ? 441 THR A CG2 1 ATOM 3199 N N . MET A 1 412 ? 23.105 -29.547 -20.060 1.00 66.65 ? 442 MET A N 1 ATOM 3200 C CA . MET A 1 412 ? 21.672 -29.746 -19.874 1.00 66.46 ? 442 MET A CA 1 ATOM 3201 C C . MET A 1 412 ? 20.984 -28.404 -19.884 1.00 63.58 ? 442 MET A C 1 ATOM 3202 O O . MET A 1 412 ? 20.026 -28.190 -20.615 1.00 68.27 ? 442 MET A O 1 ATOM 3203 C CB . MET A 1 412 ? 21.425 -30.449 -18.532 1.00 67.16 ? 442 MET A CB 1 ATOM 3204 C CG . MET A 1 412 ? 19.979 -30.491 -18.070 1.00 68.70 ? 442 MET A CG 1 ATOM 3205 S SD . MET A 1 412 ? 19.857 -30.710 -16.279 1.00 69.80 ? 442 MET A SD 1 ATOM 3206 C CE . MET A 1 412 ? 20.340 -29.090 -15.697 1.00 72.08 ? 442 MET A CE 1 ATOM 3207 N N . PHE A 1 413 ? 21.484 -27.516 -19.042 1.00 60.11 ? 443 PHE A N 1 ATOM 3208 C CA . PHE A 1 413 ? 20.923 -26.191 -18.855 1.00 61.68 ? 443 PHE A CA 1 ATOM 3209 C C . PHE A 1 413 ? 20.960 -25.360 -20.139 1.00 64.31 ? 443 PHE A C 1 ATOM 3210 O O . PHE A 1 413 ? 19.948 -24.784 -20.549 1.00 60.93 ? 443 PHE A O 1 ATOM 3211 C CB . PHE A 1 413 ? 21.687 -25.499 -17.738 1.00 59.49 ? 443 PHE A CB 1 ATOM 3212 C CG . PHE A 1 413 ? 21.272 -24.099 -17.504 1.00 59.40 ? 443 PHE A CG 1 ATOM 3213 C CD1 . PHE A 1 413 ? 20.040 -23.814 -16.984 1.00 60.03 ? 443 PHE A CD1 1 ATOM 3214 C CD2 . PHE A 1 413 ? 22.141 -23.055 -17.787 1.00 64.69 ? 443 PHE A CD2 1 ATOM 3215 C CE1 . PHE A 1 413 ? 19.665 -22.503 -16.760 1.00 63.10 ? 443 PHE A CE1 1 ATOM 3216 C CE2 . PHE A 1 413 ? 21.777 -21.740 -17.567 1.00 63.75 ? 443 PHE A CE2 1 ATOM 3217 C CZ . PHE A 1 413 ? 20.536 -21.464 -17.052 1.00 63.59 ? 443 PHE A CZ 1 ATOM 3218 N N . SER A 1 414 ? 22.122 -25.336 -20.784 1.00 67.71 ? 444 SER A N 1 ATOM 3219 C CA . SER A 1 414 ? 22.284 -24.668 -22.081 1.00 71.38 ? 444 SER A CA 1 ATOM 3220 C C . SER A 1 414 ? 21.290 -25.150 -23.132 1.00 72.35 ? 444 SER A C 1 ATOM 3221 O O . SER A 1 414 ? 20.687 -24.348 -23.851 1.00 72.57 ? 444 SER A O 1 ATOM 3222 C CB . SER A 1 414 ? 23.683 -24.893 -22.607 1.00 71.93 ? 444 SER A CB 1 ATOM 3223 O OG . SER A 1 414 ? 23.872 -24.127 -23.772 1.00 78.32 ? 444 SER A OG 1 ATOM 3224 N N . ARG A 1 415 ? 21.128 -26.463 -23.203 1.00 70.56 ? 445 ARG A N 1 ATOM 3225 C CA . ARG A 1 415 ? 20.185 -27.070 -24.129 1.00 72.67 ? 445 ARG A CA 1 ATOM 3226 C C . ARG A 1 415 ? 18.728 -26.818 -23.738 1.00 71.89 ? 445 ARG A C 1 ATOM 3227 O O . ARG A 1 415 ? 17.836 -26.900 -24.589 1.00 70.42 ? 445 ARG A O 1 ATOM 3228 C CB . ARG A 1 415 ? 20.464 -28.566 -24.242 1.00 72.24 ? 445 ARG A CB 1 ATOM 3229 C CG . ARG A 1 415 ? 21.780 -28.836 -24.919 1.00 75.51 ? 445 ARG A CG 1 ATOM 3230 C CD . ARG A 1 415 ? 22.232 -30.276 -24.816 1.00 78.43 ? 445 ARG A CD 1 ATOM 3231 N NE . ARG A 1 415 ? 23.447 -30.477 -25.616 1.00 82.95 ? 445 ARG A NE 1 ATOM 3232 C CZ . ARG A 1 415 ? 24.097 -31.630 -25.746 1.00 83.47 ? 445 ARG A CZ 1 ATOM 3233 N NH1 . ARG A 1 415 ? 23.677 -32.722 -25.121 1.00 80.02 ? 445 ARG A NH1 1 ATOM 3234 N NH2 . ARG A 1 415 ? 25.183 -31.686 -26.509 1.00 89.22 ? 445 ARG A NH2 1 ATOM 3235 N N . PHE A 1 416 ? 18.498 -26.528 -22.460 1.00 69.54 ? 446 PHE A N 1 ATOM 3236 C CA . PHE A 1 416 ? 17.163 -26.238 -21.940 1.00 70.57 ? 446 PHE A CA 1 ATOM 3237 C C . PHE A 1 416 ? 16.826 -24.816 -22.330 1.00 74.13 ? 446 PHE A C 1 ATOM 3238 O O . PHE A 1 416 ? 15.826 -24.568 -23.010 1.00 75.78 ? 446 PHE A O 1 ATOM 3239 C CB . PHE A 1 416 ? 17.143 -26.436 -20.412 1.00 70.28 ? 446 PHE A CB 1 ATOM 3240 C CG . PHE A 1 416 ? 15.952 -25.839 -19.707 1.00 66.37 ? 446 PHE A CG 1 ATOM 3241 C CD1 . PHE A 1 416 ? 14.719 -26.441 -19.769 1.00 66.27 ? 446 PHE A CD1 1 ATOM 3242 C CD2 . PHE A 1 416 ? 16.095 -24.702 -18.924 1.00 65.95 ? 446 PHE A CD2 1 ATOM 3243 C CE1 . PHE A 1 416 ? 13.634 -25.894 -19.106 1.00 66.75 ? 446 PHE A CE1 1 ATOM 3244 C CE2 . PHE A 1 416 ? 15.017 -24.147 -18.255 1.00 64.41 ? 446 PHE A CE2 1 ATOM 3245 C CZ . PHE A 1 416 ? 13.783 -24.745 -18.348 1.00 65.40 ? 446 PHE A CZ 1 ATOM 3246 N N . LEU A 1 417 ? 17.690 -23.888 -21.942 1.00 74.72 ? 447 LEU A N 1 ATOM 3247 C CA . LEU A 1 417 ? 17.512 -22.480 -22.296 1.00 76.56 ? 447 LEU A CA 1 ATOM 3248 C C . LEU A 1 417 ? 17.280 -22.259 -23.791 1.00 77.00 ? 447 LEU A C 1 ATOM 3249 O O . LEU A 1 417 ? 16.476 -21.423 -24.188 1.00 74.30 ? 447 LEU A O 1 ATOM 3250 C CB . LEU A 1 417 ? 18.730 -21.665 -21.878 1.00 75.41 ? 447 LEU A CB 1 ATOM 3251 C CG . LEU A 1 417 ? 18.806 -21.174 -20.438 1.00 75.66 ? 447 LEU A CG 1 ATOM 3252 C CD1 . LEU A 1 417 ? 19.832 -20.056 -20.367 1.00 78.22 ? 447 LEU A CD1 1 ATOM 3253 C CD2 . LEU A 1 417 ? 17.483 -20.673 -19.904 1.00 77.34 ? 447 LEU A CD2 1 ATOM 3254 N N . ASN A 1 418 ? 18.009 -23.004 -24.606 1.00 81.48 ? 448 ASN A N 1 ATOM 3255 C CA . ASN A 1 418 ? 17.963 -22.850 -26.054 1.00 85.09 ? 448 ASN A CA 1 ATOM 3256 C C . ASN A 1 418 ? 16.957 -23.771 -26.764 1.00 90.72 ? 448 ASN A C 1 ATOM 3257 O O . ASN A 1 418 ? 17.151 -24.099 -27.920 1.00 94.43 ? 448 ASN A O 1 ATOM 3258 C CB . ASN A 1 418 ? 19.372 -23.052 -26.622 1.00 81.85 ? 448 ASN A CB 1 ATOM 3259 C CG . ASN A 1 418 ? 20.339 -21.993 -26.138 1.00 80.37 ? 448 ASN A CG 1 ATOM 3260 O OD1 . ASN A 1 418 ? 20.187 -20.827 -26.460 1.00 80.91 ? 448 ASN A OD1 1 ATOM 3261 N ND2 . ASN A 1 418 ? 21.332 -22.392 -25.367 1.00 79.20 ? 448 ASN A ND2 1 ATOM 3262 N N . LYS A 1 419 ? 15.888 -24.178 -26.087 1.00 98.34 ? 449 LYS A N 1 ATOM 3263 C CA . LYS A 1 419 ? 14.839 -24.999 -26.709 1.00 110.02 ? 449 LYS A CA 1 ATOM 3264 C C . LYS A 1 419 ? 15.390 -26.121 -27.585 1.00 113.65 ? 449 LYS A C 1 ATOM 3265 O O . LYS A 1 419 ? 14.776 -26.472 -28.599 1.00 109.80 ? 449 LYS A O 1 ATOM 3266 C CB . LYS A 1 419 ? 13.906 -24.150 -27.593 1.00 115.86 ? 449 LYS A CB 1 ATOM 3267 C CG . LYS A 1 419 ? 13.525 -22.778 -27.065 1.00 120.54 ? 449 LYS A CG 1 ATOM 3268 C CD . LYS A 1 419 ? 12.527 -22.123 -28.013 1.00 127.43 ? 449 LYS A CD 1 ATOM 3269 C CE . LYS A 1 419 ? 12.564 -20.607 -27.928 1.00 130.22 ? 449 LYS A CE 1 ATOM 3270 N NZ . LYS A 1 419 ? 12.299 -20.110 -26.551 1.00 130.66 ? 449 LYS A NZ 1 ATOM 3271 N N . GLN A 1 420 ? 16.534 -26.677 -27.201 1.00 121.05 ? 450 GLN A N 1 ATOM 3272 C CA . GLN A 1 420 ? 17.241 -27.656 -28.031 1.00 126.32 ? 450 GLN A CA 1 ATOM 3273 C C . GLN A 1 420 ? 17.045 -29.084 -27.516 1.00 126.43 ? 450 GLN A C 1 ATOM 3274 O O . GLN A 1 420 ? 16.778 -29.286 -26.328 1.00 123.55 ? 450 GLN A O 1 ATOM 3275 C CB . GLN A 1 420 ? 18.737 -27.323 -28.080 1.00 125.96 ? 450 GLN A CB 1 ATOM 3276 C CG . GLN A 1 420 ? 19.122 -26.293 -29.134 1.00 126.41 ? 450 GLN A CG 1 ATOM 3277 C CD . GLN A 1 420 ? 20.375 -25.516 -28.780 1.00 130.45 ? 450 GLN A CD 1 ATOM 3278 O OE1 . GLN A 1 420 ? 21.110 -25.875 -27.857 1.00 134.65 ? 450 GLN A OE1 1 ATOM 3279 N NE2 . GLN A 1 420 ? 20.627 -24.439 -29.515 1.00 133.13 ? 450 GLN A NE2 1 ATOM 3280 N N . PRO A 1 421 ? 17.177 -30.083 -28.415 1.00 129.98 ? 451 PRO A N 1 ATOM 3281 C CA . PRO A 1 421 ? 17.137 -31.477 -27.974 1.00 125.87 ? 451 PRO A CA 1 ATOM 3282 C C . PRO A 1 421 ? 18.373 -31.807 -27.137 1.00 118.54 ? 451 PRO A C 1 ATOM 3283 O O . PRO A 1 421 ? 19.464 -31.317 -27.438 1.00 110.31 ? 451 PRO A O 1 ATOM 3284 C CB . PRO A 1 421 ? 17.121 -32.263 -29.294 1.00 128.26 ? 451 PRO A CB 1 ATOM 3285 C CG . PRO A 1 421 ? 17.778 -31.367 -30.285 1.00 128.06 ? 451 PRO A CG 1 ATOM 3286 C CD . PRO A 1 421 ? 17.429 -29.968 -29.867 1.00 128.95 ? 451 PRO A CD 1 ATOM 3287 N N . TYR A 1 422 ? 18.205 -32.633 -26.108 1.00 113.25 ? 452 TYR A N 1 ATOM 3288 C CA . TYR A 1 422 ? 19.271 -32.863 -25.126 1.00 110.51 ? 452 TYR A CA 1 ATOM 3289 C C . TYR A 1 422 ? 20.276 -33.891 -25.627 1.00 117.23 ? 452 TYR A C 1 ATOM 3290 O O . TYR A 1 422 ? 21.470 -33.759 -25.359 1.00 121.93 ? 452 TYR A O 1 ATOM 3291 C CB . TYR A 1 422 ? 18.699 -33.272 -23.760 1.00 102.49 ? 452 TYR A CB 1 ATOM 3292 C CG . TYR A 1 422 ? 17.728 -32.255 -23.178 1.00 99.29 ? 452 TYR A CG 1 ATOM 3293 C CD1 . TYR A 1 422 ? 16.404 -32.203 -23.611 1.00 96.65 ? 452 TYR A CD1 1 ATOM 3294 C CD2 . TYR A 1 422 ? 18.130 -31.349 -22.202 1.00 94.18 ? 452 TYR A CD2 1 ATOM 3295 C CE1 . TYR A 1 422 ? 15.512 -31.288 -23.096 1.00 93.11 ? 452 TYR A CE1 1 ATOM 3296 C CE2 . TYR A 1 422 ? 17.244 -30.428 -21.676 1.00 92.97 ? 452 TYR A CE2 1 ATOM 3297 C CZ . TYR A 1 422 ? 15.929 -30.403 -22.129 1.00 96.33 ? 452 TYR A CZ 1 ATOM 3298 O OH . TYR A 1 422 ? 15.015 -29.496 -21.625 1.00 94.42 ? 452 TYR A OH 1 ATOM 3299 N N . ALA B 1 1 ? 61.852 -73.964 -4.198 1.00 127.02 ? 1 ALA B N 1 ATOM 3300 C CA . ALA B 1 1 ? 61.805 -72.847 -5.183 1.00 123.46 ? 1 ALA B CA 1 ATOM 3301 C C . ALA B 1 1 ? 62.739 -73.107 -6.381 1.00 120.33 ? 1 ALA B C 1 ATOM 3302 O O . ALA B 1 1 ? 63.931 -73.356 -6.192 1.00 117.87 ? 1 ALA B O 1 ATOM 3303 C CB . ALA B 1 1 ? 62.156 -71.528 -4.506 1.00 120.20 ? 1 ALA B CB 1 ATOM 3304 N N . PRO B 1 2 ? 62.193 -73.052 -7.615 1.00 114.76 ? 2 PRO B N 1 ATOM 3305 C CA . PRO B 1 2 ? 63.007 -73.140 -8.819 1.00 110.84 ? 2 PRO B CA 1 ATOM 3306 C C . PRO B 1 2 ? 63.779 -71.849 -9.041 1.00 108.97 ? 2 PRO B C 1 ATOM 3307 O O . PRO B 1 2 ? 63.200 -70.825 -9.406 1.00 107.54 ? 2 PRO B O 1 ATOM 3308 C CB . PRO B 1 2 ? 61.984 -73.373 -9.928 1.00 109.32 ? 2 PRO B CB 1 ATOM 3309 C CG . PRO B 1 2 ? 60.733 -72.757 -9.428 1.00 108.42 ? 2 PRO B CG 1 ATOM 3310 C CD . PRO B 1 2 ? 60.777 -72.809 -7.930 1.00 111.40 ? 2 PRO B CD 1 ATOM 3311 N N . ASP B 1 3 ? 65.084 -71.917 -8.818 1.00 108.56 ? 3 ASP B N 1 ATOM 3312 C CA . ASP B 1 3 ? 65.936 -70.743 -8.794 1.00 112.03 ? 3 ASP B CA 1 ATOM 3313 C C . ASP B 1 3 ? 65.932 -70.007 -10.144 1.00 111.17 ? 3 ASP B C 1 ATOM 3314 O O . ASP B 1 3 ? 65.884 -68.773 -10.187 1.00 109.24 ? 3 ASP B O 1 ATOM 3315 C CB . ASP B 1 3 ? 67.370 -71.148 -8.410 1.00 120.52 ? 3 ASP B CB 1 ATOM 3316 C CG . ASP B 1 3 ? 67.483 -71.679 -6.973 1.00 122.76 ? 3 ASP B CG 1 ATOM 3317 O OD1 . ASP B 1 3 ? 66.811 -72.671 -6.634 1.00 121.74 ? 3 ASP B OD1 1 ATOM 3318 O OD2 . ASP B 1 3 ? 68.273 -71.111 -6.192 1.00 121.98 ? 3 ASP B OD2 1 ATOM 3319 N N . GLN B 1 4 ? 65.953 -70.776 -11.233 1.00 106.82 ? 4 GLN B N 1 ATOM 3320 C CA . GLN B 1 4 ? 65.998 -70.239 -12.591 1.00 104.12 ? 4 GLN B CA 1 ATOM 3321 C C . GLN B 1 4 ? 64.762 -69.400 -12.947 1.00 102.15 ? 4 GLN B C 1 ATOM 3322 O O . GLN B 1 4 ? 64.827 -68.503 -13.788 1.00 100.92 ? 4 GLN B O 1 ATOM 3323 C CB . GLN B 1 4 ? 66.195 -71.373 -13.609 1.00 105.43 ? 4 GLN B CB 1 ATOM 3324 C CG . GLN B 1 4 ? 64.968 -72.233 -13.918 1.00 103.03 ? 4 GLN B CG 1 ATOM 3325 C CD . GLN B 1 4 ? 64.793 -73.440 -13.016 1.00 104.96 ? 4 GLN B CD 1 ATOM 3326 O OE1 . GLN B 1 4 ? 65.389 -73.550 -11.942 1.00 107.59 ? 4 GLN B OE1 1 ATOM 3327 N NE2 . GLN B 1 4 ? 63.955 -74.365 -13.456 1.00 108.24 ? 4 GLN B NE2 1 ATOM 3328 N N . ASP B 1 5 ? 63.646 -69.701 -12.299 1.00 101.20 ? 5 ASP B N 1 ATOM 3329 C CA . ASP B 1 5 ? 62.436 -68.915 -12.442 1.00 101.98 ? 5 ASP B CA 1 ATOM 3330 C C . ASP B 1 5 ? 62.459 -67.609 -11.643 1.00 103.01 ? 5 ASP B C 1 ATOM 3331 O O . ASP B 1 5 ? 61.580 -66.774 -11.838 1.00 104.61 ? 5 ASP B O 1 ATOM 3332 C CB . ASP B 1 5 ? 61.219 -69.728 -11.996 1.00 101.91 ? 5 ASP B CB 1 ATOM 3333 C CG . ASP B 1 5 ? 60.863 -70.835 -12.969 1.00 101.05 ? 5 ASP B CG 1 ATOM 3334 O OD1 . ASP B 1 5 ? 61.568 -71.001 -13.983 1.00 106.22 ? 5 ASP B OD1 1 ATOM 3335 O OD2 . ASP B 1 5 ? 59.855 -71.523 -12.732 1.00 95.58 ? 5 ASP B OD2 1 ATOM 3336 N N . GLU B 1 6 ? 63.426 -67.428 -10.747 1.00 102.78 ? 6 GLU B N 1 ATOM 3337 C CA . GLU B 1 6 ? 63.474 -66.210 -9.944 1.00 106.80 ? 6 GLU B CA 1 ATOM 3338 C C . GLU B 1 6 ? 63.555 -65.013 -10.876 1.00 105.78 ? 6 GLU B C 1 ATOM 3339 O O . GLU B 1 6 ? 64.205 -65.081 -11.915 1.00 108.61 ? 6 GLU B O 1 ATOM 3340 C CB . GLU B 1 6 ? 64.653 -66.199 -8.959 1.00 114.08 ? 6 GLU B CB 1 ATOM 3341 C CG . GLU B 1 6 ? 64.780 -64.897 -8.166 1.00 118.40 ? 6 GLU B CG 1 ATOM 3342 C CD . GLU B 1 6 ? 65.394 -65.046 -6.772 1.00 123.55 ? 6 GLU B CD 1 ATOM 3343 O OE1 . GLU B 1 6 ? 66.283 -65.903 -6.566 1.00 122.71 ? 6 GLU B OE1 1 ATOM 3344 O OE2 . GLU B 1 6 ? 64.987 -64.276 -5.875 1.00 121.56 ? 6 GLU B OE2 1 ATOM 3345 N N . ILE B 1 7 ? 62.861 -63.940 -10.504 1.00 99.06 ? 7 ILE B N 1 ATOM 3346 C CA . ILE B 1 7 ? 62.852 -62.707 -11.264 1.00 97.93 ? 7 ILE B CA 1 ATOM 3347 C C . ILE B 1 7 ? 63.889 -61.786 -10.660 1.00 102.79 ? 7 ILE B C 1 ATOM 3348 O O . ILE B 1 7 ? 63.785 -61.399 -9.497 1.00 97.85 ? 7 ILE B O 1 ATOM 3349 C CB . ILE B 1 7 ? 61.490 -62.013 -11.198 1.00 95.85 ? 7 ILE B CB 1 ATOM 3350 C CG1 . ILE B 1 7 ? 60.395 -62.949 -11.691 1.00 95.73 ? 7 ILE B CG1 1 ATOM 3351 C CG2 . ILE B 1 7 ? 61.496 -60.732 -12.024 1.00 95.37 ? 7 ILE B CG2 1 ATOM 3352 C CD1 . ILE B 1 7 ? 59.006 -62.444 -11.396 1.00 92.50 ? 7 ILE B CD1 1 ATOM 3353 N N . GLN B 1 8 ? 64.875 -61.420 -11.462 1.00 105.92 ? 8 GLN B N 1 ATOM 3354 C CA . GLN B 1 8 ? 66.017 -60.704 -10.948 1.00 112.87 ? 8 GLN B CA 1 ATOM 3355 C C . GLN B 1 8 ? 65.758 -59.201 -10.898 1.00 111.51 ? 8 GLN B C 1 ATOM 3356 O O . GLN B 1 8 ? 65.458 -58.660 -9.832 1.00 111.48 ? 8 GLN B O 1 ATOM 3357 C CB . GLN B 1 8 ? 67.261 -61.049 -11.769 1.00 120.78 ? 8 GLN B CB 1 ATOM 3358 C CG . GLN B 1 8 ? 67.771 -62.470 -11.586 1.00 122.21 ? 8 GLN B CG 1 ATOM 3359 C CD . GLN B 1 8 ? 68.256 -62.746 -10.173 1.00 124.30 ? 8 GLN B CD 1 ATOM 3360 O OE1 . GLN B 1 8 ? 68.864 -61.886 -9.534 1.00 122.69 ? 8 GLN B OE1 1 ATOM 3361 N NE2 . GLN B 1 8 ? 67.995 -63.955 -9.680 1.00 125.60 ? 8 GLN B NE2 1 ATOM 3362 N N . ARG B 1 9 ? 65.864 -58.529 -12.037 1.00 110.35 ? 9 ARG B N 1 ATOM 3363 C CA . ARG B 1 9 ? 65.635 -57.090 -12.096 1.00 107.45 ? 9 ARG B CA 1 ATOM 3364 C C . ARG B 1 9 ? 64.513 -56.819 -13.058 1.00 99.37 ? 9 ARG B C 1 ATOM 3365 O O . ARG B 1 9 ? 64.616 -57.106 -14.253 1.00 99.63 ? 9 ARG B O 1 ATOM 3366 C CB . ARG B 1 9 ? 66.891 -56.360 -12.543 1.00 111.51 ? 9 ARG B CB 1 ATOM 3367 C CG . ARG B 1 9 ? 68.057 -56.558 -11.596 1.00 115.30 ? 9 ARG B CG 1 ATOM 3368 C CD . ARG B 1 9 ? 67.898 -55.835 -10.280 1.00 111.99 ? 9 ARG B CD 1 ATOM 3369 N NE . ARG B 1 9 ? 68.465 -54.511 -10.435 1.00 109.78 ? 9 ARG B NE 1 ATOM 3370 C CZ . ARG B 1 9 ? 69.600 -54.090 -9.887 1.00 113.59 ? 9 ARG B CZ 1 ATOM 3371 N NH1 . ARG B 1 9 ? 70.305 -54.857 -9.063 1.00 115.27 ? 9 ARG B NH1 1 ATOM 3372 N NH2 . ARG B 1 9 ? 70.014 -52.856 -10.137 1.00 118.18 ? 9 ARG B NH2 1 ATOM 3373 N N . LEU B 1 10 ? 63.440 -56.257 -12.530 1.00 93.98 ? 10 LEU B N 1 ATOM 3374 C CA . LEU B 1 10 ? 62.236 -56.051 -13.312 1.00 93.55 ? 10 LEU B CA 1 ATOM 3375 C C . LEU B 1 10 ? 62.170 -54.614 -13.845 1.00 92.60 ? 10 LEU B C 1 ATOM 3376 O O . LEU B 1 10 ? 62.099 -53.671 -13.055 1.00 94.92 ? 10 LEU B O 1 ATOM 3377 C CB . LEU B 1 10 ? 61.030 -56.382 -12.439 1.00 93.56 ? 10 LEU B CB 1 ATOM 3378 C CG . LEU B 1 10 ? 59.726 -56.678 -13.158 1.00 92.07 ? 10 LEU B CG 1 ATOM 3379 C CD1 . LEU B 1 10 ? 59.833 -57.938 -14.000 1.00 91.12 ? 10 LEU B CD1 1 ATOM 3380 C CD2 . LEU B 1 10 ? 58.613 -56.806 -12.135 1.00 91.82 ? 10 LEU B CD2 1 ATOM 3381 N N . PRO B 1 11 ? 62.227 -54.440 -15.183 1.00 93.34 ? 11 PRO B N 1 ATOM 3382 C CA . PRO B 1 11 ? 62.223 -53.096 -15.777 1.00 96.99 ? 11 PRO B CA 1 ATOM 3383 C C . PRO B 1 11 ? 61.045 -52.234 -15.326 1.00 99.23 ? 11 PRO B C 1 ATOM 3384 O O . PRO B 1 11 ? 59.919 -52.708 -15.327 1.00 99.17 ? 11 PRO B O 1 ATOM 3385 C CB . PRO B 1 11 ? 62.105 -53.379 -17.280 1.00 95.57 ? 11 PRO B CB 1 ATOM 3386 C CG . PRO B 1 11 ? 62.700 -54.717 -17.471 1.00 94.29 ? 11 PRO B CG 1 ATOM 3387 C CD . PRO B 1 11 ? 62.418 -55.484 -16.208 1.00 92.55 ? 11 PRO B CD 1 ATOM 3388 N N . GLY B 1 12 ? 61.307 -50.987 -14.956 1.00 99.59 ? 12 GLY B N 1 ATOM 3389 C CA . GLY B 1 12 ? 60.255 -50.056 -14.571 1.00 97.81 ? 12 GLY B CA 1 ATOM 3390 C C . GLY B 1 12 ? 60.173 -49.826 -13.075 1.00 103.86 ? 12 GLY B C 1 ATOM 3391 O O . GLY B 1 12 ? 59.363 -49.020 -12.615 1.00 104.58 ? 12 GLY B O 1 ATOM 3392 N N . LEU B 1 13 ? 60.982 -50.552 -12.304 1.00 107.93 ? 13 LEU B N 1 ATOM 3393 C CA . LEU B 1 13 ? 61.107 -50.307 -10.866 1.00 107.41 ? 13 LEU B CA 1 ATOM 3394 C C . LEU B 1 13 ? 62.282 -49.387 -10.575 1.00 106.32 ? 13 LEU B C 1 ATOM 3395 O O . LEU B 1 13 ? 63.390 -49.629 -11.034 1.00 104.08 ? 13 LEU B O 1 ATOM 3396 C CB . LEU B 1 13 ? 61.282 -51.613 -10.098 1.00 107.79 ? 13 LEU B CB 1 ATOM 3397 C CG . LEU B 1 13 ? 60.041 -52.484 -9.957 1.00 108.65 ? 13 LEU B CG 1 ATOM 3398 C CD1 . LEU B 1 13 ? 60.378 -53.750 -9.191 1.00 112.12 ? 13 LEU B CD1 1 ATOM 3399 C CD2 . LEU B 1 13 ? 58.917 -51.735 -9.264 1.00 110.20 ? 13 LEU B CD2 1 ATOM 3400 N N . ALA B 1 14 ? 62.028 -48.327 -9.825 1.00 104.83 ? 14 ALA B N 1 ATOM 3401 C CA . ALA B 1 14 ? 63.091 -47.470 -9.349 1.00 106.96 ? 14 ALA B CA 1 ATOM 3402 C C . ALA B 1 14 ? 63.973 -48.244 -8.379 1.00 106.95 ? 14 ALA B C 1 ATOM 3403 O O . ALA B 1 14 ? 65.185 -48.286 -8.556 1.00 105.24 ? 14 ALA B O 1 ATOM 3404 C CB . ALA B 1 14 ? 62.520 -46.231 -8.683 1.00 109.89 ? 14 ALA B CB 1 ATOM 3405 N N . LYS B 1 15 ? 63.364 -48.852 -7.363 1.00 109.57 ? 15 LYS B N 1 ATOM 3406 C CA . LYS B 1 15 ? 64.108 -49.645 -6.375 1.00 118.35 ? 15 LYS B CA 1 ATOM 3407 C C . LYS B 1 15 ? 63.559 -51.065 -6.280 1.00 115.92 ? 15 LYS B C 1 ATOM 3408 O O . LYS B 1 15 ? 62.351 -51.277 -6.323 1.00 109.57 ? 15 LYS B O 1 ATOM 3409 C CB . LYS B 1 15 ? 64.101 -48.968 -5.001 1.00 120.96 ? 15 LYS B CB 1 ATOM 3410 C CG . LYS B 1 15 ? 62.846 -49.204 -4.185 1.00 121.41 ? 15 LYS B CG 1 ATOM 3411 C CD . LYS B 1 15 ? 62.634 -48.124 -3.138 1.00 126.29 ? 15 LYS B CD 1 ATOM 3412 C CE . LYS B 1 15 ? 61.242 -48.225 -2.542 1.00 127.49 ? 15 LYS B CE 1 ATOM 3413 N NZ . LYS B 1 15 ? 60.864 -46.987 -1.818 1.00 130.81 ? 15 LYS B NZ 1 ATOM 3414 N N . GLN B 1 16 ? 64.464 -52.028 -6.149 1.00 118.74 ? 16 GLN B N 1 ATOM 3415 C CA . GLN B 1 16 ? 64.109 -53.438 -6.243 1.00 112.46 ? 16 GLN B CA 1 ATOM 3416 C C . GLN B 1 16 ? 63.277 -53.892 -5.059 1.00 107.28 ? 16 GLN B C 1 ATOM 3417 O O . GLN B 1 16 ? 63.345 -53.279 -3.996 1.00 107.37 ? 16 GLN B O 1 ATOM 3418 C CB . GLN B 1 16 ? 65.359 -54.301 -6.383 1.00 113.36 ? 16 GLN B CB 1 ATOM 3419 C CG . GLN B 1 16 ? 66.004 -54.188 -7.753 1.00 115.64 ? 16 GLN B CG 1 ATOM 3420 C CD . GLN B 1 16 ? 65.075 -54.605 -8.891 1.00 115.57 ? 16 GLN B CD 1 ATOM 3421 O OE1 . GLN B 1 16 ? 64.544 -55.718 -8.901 1.00 118.07 ? 16 GLN B OE1 1 ATOM 3422 N NE2 . GLN B 1 16 ? 64.911 -53.731 -9.877 1.00 115.16 ? 16 GLN B NE2 1 ATOM 3423 N N . PRO B 1 17 ? 62.461 -54.945 -5.259 1.00 101.93 ? 17 PRO B N 1 ATOM 3424 C CA . PRO B 1 17 ? 61.566 -55.475 -4.232 1.00 98.65 ? 17 PRO B CA 1 ATOM 3425 C C . PRO B 1 17 ? 62.298 -56.028 -3.044 1.00 99.35 ? 17 PRO B C 1 ATOM 3426 O O . PRO B 1 17 ? 63.368 -56.581 -3.198 1.00 102.54 ? 17 PRO B O 1 ATOM 3427 C CB . PRO B 1 17 ? 60.842 -56.614 -4.943 1.00 98.79 ? 17 PRO B CB 1 ATOM 3428 C CG . PRO B 1 17 ? 60.951 -56.312 -6.398 1.00 98.25 ? 17 PRO B CG 1 ATOM 3429 C CD . PRO B 1 17 ? 62.255 -55.607 -6.560 1.00 99.72 ? 17 PRO B CD 1 ATOM 3430 N N . SER B 1 18 ? 61.696 -55.888 -1.872 1.00 100.24 ? 18 SER B N 1 ATOM 3431 C CA . SER B 1 18 ? 62.216 -56.463 -0.646 1.00 103.33 ? 18 SER B CA 1 ATOM 3432 C C . SER B 1 18 ? 61.878 -57.956 -0.518 1.00 107.18 ? 18 SER B C 1 ATOM 3433 O O . SER B 1 18 ? 62.340 -58.619 0.416 1.00 116.97 ? 18 SER B O 1 ATOM 3434 C CB . SER B 1 18 ? 61.649 -55.708 0.558 1.00 103.46 ? 18 SER B CB 1 ATOM 3435 O OG . SER B 1 18 ? 60.264 -55.970 0.724 1.00 97.98 ? 18 SER B OG 1 ATOM 3436 N N . PHE B 1 19 ? 61.093 -58.478 -1.460 1.00 103.62 ? 19 PHE B N 1 ATOM 3437 C CA . PHE B 1 19 ? 60.587 -59.844 -1.413 1.00 100.34 ? 19 PHE B CA 1 ATOM 3438 C C . PHE B 1 19 ? 61.014 -60.592 -2.664 1.00 99.44 ? 19 PHE B C 1 ATOM 3439 O O . PHE B 1 19 ? 61.226 -60.003 -3.722 1.00 98.42 ? 19 PHE B O 1 ATOM 3440 C CB . PHE B 1 19 ? 59.053 -59.835 -1.304 1.00 100.21 ? 19 PHE B CB 1 ATOM 3441 C CG . PHE B 1 19 ? 58.365 -59.033 -2.385 1.00 103.10 ? 19 PHE B CG 1 ATOM 3442 C CD1 . PHE B 1 19 ? 58.303 -57.641 -2.327 1.00 105.34 ? 19 PHE B CD1 1 ATOM 3443 C CD2 . PHE B 1 19 ? 57.782 -59.666 -3.468 1.00 105.66 ? 19 PHE B CD2 1 ATOM 3444 C CE1 . PHE B 1 19 ? 57.679 -56.916 -3.330 1.00 103.97 ? 19 PHE B CE1 1 ATOM 3445 C CE2 . PHE B 1 19 ? 57.154 -58.945 -4.472 1.00 102.22 ? 19 PHE B CE2 1 ATOM 3446 C CZ . PHE B 1 19 ? 57.108 -57.571 -4.404 1.00 102.29 ? 19 PHE B CZ 1 ATOM 3447 N N . ARG B 1 20 ? 61.139 -61.902 -2.547 1.00 100.92 ? 20 ARG B N 1 ATOM 3448 C CA . ARG B 1 20 ? 61.400 -62.720 -3.715 1.00 100.76 ? 20 ARG B CA 1 ATOM 3449 C C . ARG B 1 20 ? 60.131 -62.879 -4.564 1.00 95.90 ? 20 ARG B C 1 ATOM 3450 O O . ARG B 1 20 ? 59.003 -62.864 -4.063 1.00 89.38 ? 20 ARG B O 1 ATOM 3451 C CB . ARG B 1 20 ? 61.957 -64.095 -3.318 1.00 107.91 ? 20 ARG B CB 1 ATOM 3452 C CG . ARG B 1 20 ? 63.271 -64.054 -2.549 1.00 111.80 ? 20 ARG B CG 1 ATOM 3453 C CD . ARG B 1 20 ? 63.958 -65.411 -2.543 1.00 114.38 ? 20 ARG B CD 1 ATOM 3454 N NE . ARG B 1 20 ? 64.724 -65.631 -1.317 1.00 118.25 ? 20 ARG B NE 1 ATOM 3455 C CZ . ARG B 1 20 ? 64.204 -65.982 -0.140 1.00 116.55 ? 20 ARG B CZ 1 ATOM 3456 N NH1 . ARG B 1 20 ? 62.897 -66.161 0.007 1.00 117.71 ? 20 ARG B NH1 1 ATOM 3457 N NH2 . ARG B 1 20 ? 64.998 -66.155 0.907 1.00 116.61 ? 20 ARG B NH2 1 ATOM 3458 N N . GLN B 1 21 ? 60.345 -63.029 -5.865 1.00 95.16 ? 21 GLN B N 1 ATOM 3459 C CA . GLN B 1 21 ? 59.287 -63.316 -6.810 1.00 91.30 ? 21 GLN B CA 1 ATOM 3460 C C . GLN B 1 21 ? 59.813 -64.159 -7.970 1.00 94.05 ? 21 GLN B C 1 ATOM 3461 O O . GLN B 1 21 ? 60.927 -63.956 -8.437 1.00 101.36 ? 21 GLN B O 1 ATOM 3462 C CB . GLN B 1 21 ? 58.684 -62.024 -7.336 1.00 87.26 ? 21 GLN B CB 1 ATOM 3463 C CG . GLN B 1 21 ? 59.687 -60.984 -7.781 1.00 84.46 ? 21 GLN B CG 1 ATOM 3464 C CD . GLN B 1 21 ? 59.015 -59.790 -8.429 1.00 85.66 ? 21 GLN B CD 1 ATOM 3465 O OE1 . GLN B 1 21 ? 57.783 -59.697 -8.466 1.00 79.38 ? 21 GLN B OE1 1 ATOM 3466 N NE2 . GLN B 1 21 ? 59.819 -58.870 -8.955 1.00 87.42 ? 21 GLN B NE2 1 ATOM 3467 N N . TYR B 1 22 ? 58.995 -65.097 -8.421 1.00 91.20 ? 22 TYR B N 1 ATOM 3468 C CA . TYR B 1 22 ? 59.376 -66.055 -9.434 1.00 93.06 ? 22 TYR B CA 1 ATOM 3469 C C . TYR B 1 22 ? 58.399 -66.001 -10.598 1.00 90.55 ? 22 TYR B C 1 ATOM 3470 O O . TYR B 1 22 ? 57.228 -65.706 -10.401 1.00 87.41 ? 22 TYR B O 1 ATOM 3471 C CB . TYR B 1 22 ? 59.375 -67.453 -8.825 1.00 98.00 ? 22 TYR B CB 1 ATOM 3472 C CG . TYR B 1 22 ? 60.362 -67.637 -7.675 1.00 106.23 ? 22 TYR B CG 1 ATOM 3473 C CD1 . TYR B 1 22 ? 60.084 -67.156 -6.395 1.00 106.16 ? 22 TYR B CD1 1 ATOM 3474 C CD2 . TYR B 1 22 ? 61.569 -68.304 -7.868 1.00 110.27 ? 22 TYR B CD2 1 ATOM 3475 C CE1 . TYR B 1 22 ? 60.978 -67.332 -5.349 1.00 105.51 ? 22 TYR B CE1 1 ATOM 3476 C CE2 . TYR B 1 22 ? 62.461 -68.478 -6.825 1.00 111.35 ? 22 TYR B CE2 1 ATOM 3477 C CZ . TYR B 1 22 ? 62.161 -67.989 -5.570 1.00 108.18 ? 22 TYR B CZ 1 ATOM 3478 O OH . TYR B 1 22 ? 63.049 -68.177 -4.535 1.00 113.64 ? 22 TYR B OH 1 ATOM 3479 N N . SER B 1 23 ? 58.888 -66.255 -11.811 1.00 89.42 ? 23 SER B N 1 ATOM 3480 C CA . SER B 1 23 ? 58.027 -66.332 -12.990 1.00 83.80 ? 23 SER B CA 1 ATOM 3481 C C . SER B 1 23 ? 58.482 -67.435 -13.923 1.00 83.06 ? 23 SER B C 1 ATOM 3482 O O . SER B 1 23 ? 59.618 -67.416 -14.374 1.00 84.22 ? 23 SER B O 1 ATOM 3483 C CB . SER B 1 23 ? 58.023 -65.010 -13.754 1.00 84.64 ? 23 SER B CB 1 ATOM 3484 O OG . SER B 1 23 ? 57.422 -65.176 -15.030 1.00 81.83 ? 23 SER B OG 1 ATOM 3485 N N . GLY B 1 24 ? 57.585 -68.369 -14.228 1.00 81.99 ? 24 GLY B N 1 ATOM 3486 C CA . GLY B 1 24 ? 57.897 -69.513 -15.082 1.00 82.66 ? 24 GLY B CA 1 ATOM 3487 C C . GLY B 1 24 ? 56.666 -70.303 -15.462 1.00 83.35 ? 24 GLY B C 1 ATOM 3488 O O . GLY B 1 24 ? 55.581 -69.739 -15.552 1.00 85.07 ? 24 GLY B O 1 ATOM 3489 N N . TYR B 1 25 ? 56.819 -71.617 -15.640 1.00 84.32 ? 25 TYR B N 1 ATOM 3490 C CA . TYR B 1 25 ? 55.749 -72.465 -16.192 1.00 83.44 ? 25 TYR B CA 1 ATOM 3491 C C . TYR B 1 25 ? 55.380 -73.690 -15.356 1.00 83.43 ? 25 TYR B C 1 ATOM 3492 O O . TYR B 1 25 ? 56.249 -74.443 -14.903 1.00 87.80 ? 25 TYR B O 1 ATOM 3493 C CB . TYR B 1 25 ? 56.116 -72.888 -17.623 1.00 84.33 ? 25 TYR B CB 1 ATOM 3494 C CG . TYR B 1 25 ? 55.914 -71.756 -18.584 1.00 82.45 ? 25 TYR B CG 1 ATOM 3495 C CD1 . TYR B 1 25 ? 56.882 -70.775 -18.733 1.00 80.92 ? 25 TYR B CD1 1 ATOM 3496 C CD2 . TYR B 1 25 ? 54.717 -71.624 -19.287 1.00 81.84 ? 25 TYR B CD2 1 ATOM 3497 C CE1 . TYR B 1 25 ? 56.681 -69.709 -19.590 1.00 81.18 ? 25 TYR B CE1 1 ATOM 3498 C CE2 . TYR B 1 25 ? 54.505 -70.564 -20.145 1.00 80.64 ? 25 TYR B CE2 1 ATOM 3499 C CZ . TYR B 1 25 ? 55.490 -69.610 -20.293 1.00 82.04 ? 25 TYR B CZ 1 ATOM 3500 O OH . TYR B 1 25 ? 55.277 -68.549 -21.137 1.00 86.87 ? 25 TYR B OH 1 ATOM 3501 N N . LEU B 1 26 ? 54.082 -73.887 -15.175 1.00 81.20 ? 26 LEU B N 1 ATOM 3502 C CA . LEU B 1 26 ? 53.561 -75.046 -14.486 1.00 87.30 ? 26 LEU B CA 1 ATOM 3503 C C . LEU B 1 26 ? 52.969 -76.004 -15.507 1.00 87.94 ? 26 LEU B C 1 ATOM 3504 O O . LEU B 1 26 ? 52.301 -75.583 -16.446 1.00 85.10 ? 26 LEU B O 1 ATOM 3505 C CB . LEU B 1 26 ? 52.484 -74.635 -13.486 1.00 90.26 ? 26 LEU B CB 1 ATOM 3506 C CG . LEU B 1 26 ? 52.836 -73.513 -12.520 1.00 95.90 ? 26 LEU B CG 1 ATOM 3507 C CD1 . LEU B 1 26 ? 51.656 -73.250 -11.600 1.00 100.93 ? 26 LEU B CD1 1 ATOM 3508 C CD2 . LEU B 1 26 ? 54.076 -73.842 -11.705 1.00 98.97 ? 26 LEU B CD2 1 ATOM 3509 N N . LYS B 1 27 ? 53.200 -77.291 -15.312 1.00 92.02 ? 27 LYS B N 1 ATOM 3510 C CA . LYS B 1 27 ? 52.629 -78.302 -16.192 1.00 100.88 ? 27 LYS B CA 1 ATOM 3511 C C . LYS B 1 27 ? 51.161 -78.507 -15.878 1.00 102.39 ? 27 LYS B C 1 ATOM 3512 O O . LYS B 1 27 ? 50.791 -78.672 -14.717 1.00 107.83 ? 27 LYS B O 1 ATOM 3513 C CB . LYS B 1 27 ? 53.364 -79.630 -16.033 1.00 106.70 ? 27 LYS B CB 1 ATOM 3514 C CG . LYS B 1 27 ? 54.741 -79.640 -16.666 1.00 111.34 ? 27 LYS B CG 1 ATOM 3515 C CD . LYS B 1 27 ? 55.142 -81.031 -17.131 1.00 114.52 ? 27 LYS B CD 1 ATOM 3516 C CE . LYS B 1 27 ? 55.540 -81.939 -15.975 1.00 114.61 ? 27 LYS B CE 1 ATOM 3517 N NZ . LYS B 1 27 ? 56.797 -81.504 -15.301 1.00 113.98 ? 27 LYS B NZ 1 ATOM 3518 N N . GLY B 1 28 ? 50.321 -78.482 -16.903 1.00 103.73 ? 28 GLY B N 1 ATOM 3519 C CA . GLY B 1 28 ? 48.911 -78.816 -16.723 1.00 108.53 ? 28 GLY B CA 1 ATOM 3520 C C . GLY B 1 28 ? 48.644 -80.216 -17.267 1.00 106.86 ? 28 GLY B C 1 ATOM 3521 O O . GLY B 1 28 ? 49.510 -81.075 -17.196 1.00 116.42 ? 28 GLY B O 1 ATOM 3522 N N . SER B 1 29 ? 47.451 -80.442 -17.805 1.00 99.67 ? 29 SER B N 1 ATOM 3523 C CA . SER B 1 29 ? 47.159 -81.692 -18.478 1.00 101.41 ? 29 SER B CA 1 ATOM 3524 C C . SER B 1 29 ? 47.851 -81.694 -19.843 1.00 103.16 ? 29 SER B C 1 ATOM 3525 O O . SER B 1 29 ? 48.329 -80.656 -20.307 1.00 110.76 ? 29 SER B O 1 ATOM 3526 C CB . SER B 1 29 ? 45.649 -81.893 -18.638 1.00 102.31 ? 29 SER B CB 1 ATOM 3527 O OG . SER B 1 29 ? 45.187 -81.488 -19.921 1.00 98.34 ? 29 SER B OG 1 ATOM 3528 N N . GLY B 1 30 ? 47.916 -82.866 -20.472 1.00 97.76 ? 30 GLY B N 1 ATOM 3529 C CA . GLY B 1 30 ? 48.470 -83.010 -21.815 1.00 93.83 ? 30 GLY B CA 1 ATOM 3530 C C . GLY B 1 30 ? 49.768 -82.266 -21.984 1.00 90.36 ? 30 GLY B C 1 ATOM 3531 O O . GLY B 1 30 ? 50.623 -82.320 -21.105 1.00 89.63 ? 30 GLY B O 1 ATOM 3532 N N . SER B 1 31 ? 49.893 -81.534 -23.087 1.00 87.54 ? 31 SER B N 1 ATOM 3533 C CA . SER B 1 31 ? 51.095 -80.758 -23.371 1.00 89.80 ? 31 SER B CA 1 ATOM 3534 C C . SER B 1 31 ? 50.875 -79.263 -23.126 1.00 89.08 ? 31 SER B C 1 ATOM 3535 O O . SER B 1 31 ? 51.426 -78.421 -23.847 1.00 84.85 ? 31 SER B O 1 ATOM 3536 C CB . SER B 1 31 ? 51.545 -80.996 -24.819 1.00 93.02 ? 31 SER B CB 1 ATOM 3537 O OG . SER B 1 31 ? 50.626 -80.456 -25.759 1.00 91.56 ? 31 SER B OG 1 ATOM 3538 N N . LYS B 1 32 ? 50.096 -78.931 -22.097 1.00 87.91 ? 32 LYS B N 1 ATOM 3539 C CA . LYS B 1 32 ? 49.811 -77.525 -21.758 1.00 87.32 ? 32 LYS B CA 1 ATOM 3540 C C . LYS B 1 32 ? 50.770 -76.944 -20.692 1.00 83.51 ? 32 LYS B C 1 ATOM 3541 O O . LYS B 1 32 ? 51.109 -77.608 -19.712 1.00 80.54 ? 32 LYS B O 1 ATOM 3542 C CB . LYS B 1 32 ? 48.367 -77.386 -21.282 1.00 85.87 ? 32 LYS B CB 1 ATOM 3543 C CG . LYS B 1 32 ? 47.315 -77.999 -22.195 1.00 85.31 ? 32 LYS B CG 1 ATOM 3544 C CD . LYS B 1 32 ? 45.973 -78.032 -21.481 1.00 86.41 ? 32 LYS B CD 1 ATOM 3545 C CE . LYS B 1 32 ? 44.879 -78.679 -22.308 1.00 89.28 ? 32 LYS B CE 1 ATOM 3546 N NZ . LYS B 1 32 ? 45.025 -80.159 -22.383 1.00 92.70 ? 32 LYS B NZ 1 ATOM 3547 N N . HIS B 1 33 ? 51.190 -75.700 -20.884 1.00 81.64 ? 33 HIS B N 1 ATOM 3548 C CA . HIS B 1 33 ? 52.137 -75.061 -19.978 1.00 85.61 ? 33 HIS B CA 1 ATOM 3549 C C . HIS B 1 33 ? 51.655 -73.681 -19.579 1.00 83.49 ? 33 HIS B C 1 ATOM 3550 O O . HIS B 1 33 ? 51.642 -72.776 -20.402 1.00 85.22 ? 33 HIS B O 1 ATOM 3551 C CB . HIS B 1 33 ? 53.495 -74.947 -20.651 1.00 89.90 ? 33 HIS B CB 1 ATOM 3552 C CG . HIS B 1 33 ? 54.182 -76.254 -20.837 1.00 94.06 ? 33 HIS B CG 1 ATOM 3553 N ND1 . HIS B 1 33 ? 54.175 -76.935 -22.036 1.00 94.48 ? 33 HIS B ND1 1 ATOM 3554 C CD2 . HIS B 1 33 ? 54.895 -77.010 -19.973 1.00 97.72 ? 33 HIS B CD2 1 ATOM 3555 C CE1 . HIS B 1 33 ? 54.855 -78.054 -21.904 1.00 98.19 ? 33 HIS B CE1 1 ATOM 3556 N NE2 . HIS B 1 33 ? 55.305 -78.122 -20.663 1.00 103.70 ? 33 HIS B NE2 1 ATOM 3557 N N . LEU B 1 34 ? 51.310 -73.519 -18.303 1.00 84.92 ? 34 LEU B N 1 ATOM 3558 C CA . LEU B 1 34 ? 50.718 -72.284 -17.804 1.00 82.71 ? 34 LEU B CA 1 ATOM 3559 C C . LEU B 1 34 ? 51.755 -71.368 -17.184 1.00 81.99 ? 34 LEU B C 1 ATOM 3560 O O . LEU B 1 34 ? 52.494 -71.767 -16.299 1.00 80.51 ? 34 LEU B O 1 ATOM 3561 C CB . LEU B 1 34 ? 49.657 -72.596 -16.756 1.00 81.05 ? 34 LEU B CB 1 ATOM 3562 C CG . LEU B 1 34 ? 48.612 -73.659 -17.106 1.00 82.99 ? 34 LEU B CG 1 ATOM 3563 C CD1 . LEU B 1 34 ? 47.581 -73.720 -15.997 1.00 84.29 ? 34 LEU B CD1 1 ATOM 3564 C CD2 . LEU B 1 34 ? 47.930 -73.376 -18.433 1.00 81.60 ? 34 LEU B CD2 1 ATOM 3565 N N . HIS B 1 35 ? 51.796 -70.124 -17.640 1.00 83.76 ? 35 HIS B N 1 ATOM 3566 C CA . HIS B 1 35 ? 52.710 -69.144 -17.072 1.00 81.92 ? 35 HIS B CA 1 ATOM 3567 C C . HIS B 1 35 ? 52.209 -68.690 -15.715 1.00 77.97 ? 35 HIS B C 1 ATOM 3568 O O . HIS B 1 35 ? 51.041 -68.374 -15.559 1.00 75.41 ? 35 HIS B O 1 ATOM 3569 C CB . HIS B 1 35 ? 52.859 -67.942 -17.993 1.00 82.71 ? 35 HIS B CB 1 ATOM 3570 C CG . HIS B 1 35 ? 53.725 -66.865 -17.431 1.00 81.82 ? 35 HIS B CG 1 ATOM 3571 N ND1 . HIS B 1 35 ? 53.403 -65.531 -17.517 1.00 83.10 ? 35 HIS B ND1 1 ATOM 3572 C CD2 . HIS B 1 35 ? 54.889 -66.926 -16.754 1.00 83.17 ? 35 HIS B CD2 1 ATOM 3573 C CE1 . HIS B 1 35 ? 54.337 -64.816 -16.925 1.00 80.51 ? 35 HIS B CE1 1 ATOM 3574 N NE2 . HIS B 1 35 ? 55.256 -65.637 -16.462 1.00 82.21 ? 35 HIS B NE2 1 ATOM 3575 N N . TYR B 1 36 ? 53.105 -68.661 -14.741 1.00 80.28 ? 36 TYR B N 1 ATOM 3576 C CA . TYR B 1 36 ? 52.782 -68.197 -13.398 1.00 80.32 ? 36 TYR B CA 1 ATOM 3577 C C . TYR B 1 36 ? 53.693 -67.049 -13.012 1.00 78.13 ? 36 TYR B C 1 ATOM 3578 O O . TYR B 1 36 ? 54.782 -66.883 -13.574 1.00 77.71 ? 36 TYR B O 1 ATOM 3579 C CB . TYR B 1 36 ? 52.925 -69.324 -12.374 1.00 85.55 ? 36 TYR B CB 1 ATOM 3580 C CG . TYR B 1 36 ? 54.358 -69.648 -11.984 1.00 88.27 ? 36 TYR B CG 1 ATOM 3581 C CD1 . TYR B 1 36 ? 54.981 -69.000 -10.908 1.00 89.15 ? 36 TYR B CD1 1 ATOM 3582 C CD2 . TYR B 1 36 ? 55.084 -70.605 -12.677 1.00 88.03 ? 36 TYR B CD2 1 ATOM 3583 C CE1 . TYR B 1 36 ? 56.287 -69.296 -10.548 1.00 89.35 ? 36 TYR B CE1 1 ATOM 3584 C CE2 . TYR B 1 36 ? 56.389 -70.907 -12.325 1.00 90.25 ? 36 TYR B CE2 1 ATOM 3585 C CZ . TYR B 1 36 ? 56.986 -70.254 -11.263 1.00 89.23 ? 36 TYR B CZ 1 ATOM 3586 O OH . TYR B 1 36 ? 58.281 -70.559 -10.931 1.00 87.12 ? 36 TYR B OH 1 ATOM 3587 N N . TRP B 1 37 ? 53.222 -66.258 -12.055 1.00 73.23 ? 37 TRP B N 1 ATOM 3588 C CA . TRP B 1 37 ? 53.983 -65.174 -11.454 1.00 73.84 ? 37 TRP B CA 1 ATOM 3589 C C . TRP B 1 37 ? 53.663 -65.181 -9.957 1.00 77.71 ? 37 TRP B C 1 ATOM 3590 O O . TRP B 1 37 ? 52.544 -64.873 -9.540 1.00 77.64 ? 37 TRP B O 1 ATOM 3591 C CB . TRP B 1 37 ? 53.592 -63.848 -12.090 1.00 71.62 ? 37 TRP B CB 1 ATOM 3592 C CG . TRP B 1 37 ? 54.447 -62.680 -11.719 1.00 69.75 ? 37 TRP B CG 1 ATOM 3593 C CD1 . TRP B 1 37 ? 55.201 -62.533 -10.598 1.00 70.02 ? 37 TRP B CD1 1 ATOM 3594 C CD2 . TRP B 1 37 ? 54.592 -61.467 -12.462 1.00 68.19 ? 37 TRP B CD2 1 ATOM 3595 N NE1 . TRP B 1 37 ? 55.822 -61.313 -10.604 1.00 72.14 ? 37 TRP B NE1 1 ATOM 3596 C CE2 . TRP B 1 37 ? 55.462 -60.639 -11.738 1.00 71.00 ? 37 TRP B CE2 1 ATOM 3597 C CE3 . TRP B 1 37 ? 54.067 -61.004 -13.669 1.00 69.48 ? 37 TRP B CE3 1 ATOM 3598 C CZ2 . TRP B 1 37 ? 55.832 -59.365 -12.187 1.00 73.47 ? 37 TRP B CZ2 1 ATOM 3599 C CZ3 . TRP B 1 37 ? 54.428 -59.735 -14.117 1.00 69.95 ? 37 TRP B CZ3 1 ATOM 3600 C CH2 . TRP B 1 37 ? 55.305 -58.934 -13.376 1.00 72.67 ? 37 TRP B CH2 1 ATOM 3601 N N . PHE B 1 38 ? 54.662 -65.524 -9.156 1.00 81.97 ? 38 PHE B N 1 ATOM 3602 C CA . PHE B 1 38 ? 54.501 -65.753 -7.733 1.00 82.34 ? 38 PHE B CA 1 ATOM 3603 C C . PHE B 1 38 ? 55.191 -64.630 -6.978 1.00 83.58 ? 38 PHE B C 1 ATOM 3604 O O . PHE B 1 38 ? 56.385 -64.440 -7.144 1.00 78.82 ? 38 PHE B O 1 ATOM 3605 C CB . PHE B 1 38 ? 55.158 -67.078 -7.409 1.00 86.93 ? 38 PHE B CB 1 ATOM 3606 C CG . PHE B 1 38 ? 54.970 -67.534 -5.997 1.00 93.04 ? 38 PHE B CG 1 ATOM 3607 C CD1 . PHE B 1 38 ? 53.715 -67.900 -5.534 1.00 94.34 ? 38 PHE B CD1 1 ATOM 3608 C CD2 . PHE B 1 38 ? 56.055 -67.647 -5.142 1.00 94.78 ? 38 PHE B CD2 1 ATOM 3609 C CE1 . PHE B 1 38 ? 53.546 -68.347 -4.234 1.00 96.35 ? 38 PHE B CE1 1 ATOM 3610 C CE2 . PHE B 1 38 ? 55.888 -68.094 -3.843 1.00 98.18 ? 38 PHE B CE2 1 ATOM 3611 C CZ . PHE B 1 38 ? 54.635 -68.444 -3.390 1.00 96.64 ? 38 PHE B CZ 1 ATOM 3612 N N . VAL B 1 39 ? 54.446 -63.882 -6.165 1.00 88.85 ? 39 VAL B N 1 ATOM 3613 C CA . VAL B 1 39 ? 55.042 -62.824 -5.330 1.00 90.70 ? 39 VAL B CA 1 ATOM 3614 C C . VAL B 1 39 ? 54.980 -63.172 -3.843 1.00 95.74 ? 39 VAL B C 1 ATOM 3615 O O . VAL B 1 39 ? 53.900 -63.268 -3.249 1.00 95.96 ? 39 VAL B O 1 ATOM 3616 C CB . VAL B 1 39 ? 54.410 -61.447 -5.582 1.00 91.58 ? 39 VAL B CB 1 ATOM 3617 C CG1 . VAL B 1 39 ? 54.949 -60.870 -6.882 1.00 94.85 ? 39 VAL B CG1 1 ATOM 3618 C CG2 . VAL B 1 39 ? 52.889 -61.519 -5.617 1.00 89.24 ? 39 VAL B CG2 1 ATOM 3619 N N . GLU B 1 40 ? 56.154 -63.365 -3.244 1.00 98.83 ? 40 GLU B N 1 ATOM 3620 C CA . GLU B 1 40 ? 56.236 -63.769 -1.843 1.00 97.76 ? 40 GLU B CA 1 ATOM 3621 C C . GLU B 1 40 ? 55.639 -62.700 -0.926 1.00 92.53 ? 40 GLU B C 1 ATOM 3622 O O . GLU B 1 40 ? 55.738 -61.515 -1.207 1.00 86.13 ? 40 GLU B O 1 ATOM 3623 C CB . GLU B 1 40 ? 57.691 -64.060 -1.443 1.00 102.67 ? 40 GLU B CB 1 ATOM 3624 C CG . GLU B 1 40 ? 58.284 -65.306 -2.096 1.00 104.49 ? 40 GLU B CG 1 ATOM 3625 C CD . GLU B 1 40 ? 59.501 -65.855 -1.372 1.00 107.37 ? 40 GLU B CD 1 ATOM 3626 O OE1 . GLU B 1 40 ? 60.146 -65.107 -0.598 1.00 105.99 ? 40 GLU B OE1 1 ATOM 3627 O OE2 . GLU B 1 40 ? 59.819 -67.044 -1.591 1.00 104.74 ? 40 GLU B OE2 1 ATOM 3628 N N . SER B 1 41 ? 55.024 -63.125 0.170 1.00 92.16 ? 41 SER B N 1 ATOM 3629 C CA . SER B 1 41 ? 54.516 -62.182 1.162 1.00 91.98 ? 41 SER B CA 1 ATOM 3630 C C . SER B 1 41 ? 55.613 -61.209 1.567 1.00 95.11 ? 41 SER B C 1 ATOM 3631 O O . SER B 1 41 ? 56.742 -61.613 1.831 1.00 101.00 ? 41 SER B O 1 ATOM 3632 C CB . SER B 1 41 ? 54.022 -62.903 2.406 1.00 91.40 ? 41 SER B CB 1 ATOM 3633 O OG . SER B 1 41 ? 53.848 -61.985 3.467 1.00 92.87 ? 41 SER B OG 1 ATOM 3634 N N . GLN B 1 42 ? 55.283 -59.931 1.618 1.00 96.11 ? 42 GLN B N 1 ATOM 3635 C CA . GLN B 1 42 ? 56.241 -58.925 2.062 1.00 99.30 ? 42 GLN B CA 1 ATOM 3636 C C . GLN B 1 42 ? 56.555 -59.074 3.552 1.00 102.56 ? 42 GLN B C 1 ATOM 3637 O O . GLN B 1 42 ? 57.507 -58.491 4.043 1.00 100.80 ? 42 GLN B O 1 ATOM 3638 C CB . GLN B 1 42 ? 55.701 -57.523 1.796 1.00 100.17 ? 42 GLN B CB 1 ATOM 3639 C CG . GLN B 1 42 ? 55.418 -57.204 0.331 1.00 97.43 ? 42 GLN B CG 1 ATOM 3640 C CD . GLN B 1 42 ? 55.311 -55.711 0.070 1.00 96.54 ? 42 GLN B CD 1 ATOM 3641 O OE1 . GLN B 1 42 ? 56.125 -54.931 0.552 1.00 96.70 ? 42 GLN B OE1 1 ATOM 3642 N NE2 . GLN B 1 42 ? 54.291 -55.307 -0.673 1.00 94.85 ? 42 GLN B NE2 1 ATOM 3643 N N . LYS B 1 43 ? 55.735 -59.844 4.261 1.00 105.82 ? 43 LYS B N 1 ATOM 3644 C CA . LYS B 1 43 ? 55.856 -60.024 5.705 1.00 108.19 ? 43 LYS B CA 1 ATOM 3645 C C . LYS B 1 43 ? 55.817 -61.518 6.018 1.00 107.89 ? 43 LYS B C 1 ATOM 3646 O O . LYS B 1 43 ? 54.751 -62.132 6.077 1.00 104.94 ? 43 LYS B O 1 ATOM 3647 C CB . LYS B 1 43 ? 54.721 -59.266 6.397 1.00 110.37 ? 43 LYS B CB 1 ATOM 3648 C CG . LYS B 1 43 ? 54.421 -59.641 7.838 1.00 120.37 ? 43 LYS B CG 1 ATOM 3649 C CD . LYS B 1 43 ? 55.583 -59.375 8.776 1.00 126.25 ? 43 LYS B CD 1 ATOM 3650 C CE . LYS B 1 43 ? 55.133 -59.552 10.218 1.00 128.22 ? 43 LYS B CE 1 ATOM 3651 N NZ . LYS B 1 43 ? 56.252 -59.401 11.176 1.00 135.17 ? 43 LYS B NZ 1 ATOM 3652 N N . ASP B 1 44 ? 56.999 -62.096 6.171 1.00 108.18 ? 44 ASP B N 1 ATOM 3653 C CA . ASP B 1 44 ? 57.158 -63.480 6.581 1.00 110.96 ? 44 ASP B CA 1 ATOM 3654 C C . ASP B 1 44 ? 56.481 -64.486 5.651 1.00 109.41 ? 44 ASP B C 1 ATOM 3655 O O . ASP B 1 44 ? 55.428 -65.044 5.975 1.00 108.28 ? 44 ASP B O 1 ATOM 3656 C CB . ASP B 1 44 ? 56.680 -63.692 8.013 1.00 115.35 ? 44 ASP B CB 1 ATOM 3657 C CG . ASP B 1 44 ? 57.241 -64.968 8.625 1.00 121.19 ? 44 ASP B CG 1 ATOM 3658 O OD1 . ASP B 1 44 ? 58.261 -65.496 8.116 1.00 120.57 ? 44 ASP B OD1 1 ATOM 3659 O OD2 . ASP B 1 44 ? 56.661 -65.448 9.617 1.00 124.06 ? 44 ASP B OD2 1 ATOM 3660 N N . PRO B 1 45 ? 57.100 -64.730 4.489 1.00 110.04 ? 45 PRO B N 1 ATOM 3661 C CA . PRO B 1 45 ? 56.666 -65.753 3.546 1.00 107.47 ? 45 PRO B CA 1 ATOM 3662 C C . PRO B 1 45 ? 56.385 -67.111 4.191 1.00 113.92 ? 45 PRO B C 1 ATOM 3663 O O . PRO B 1 45 ? 55.345 -67.709 3.931 1.00 123.63 ? 45 PRO B O 1 ATOM 3664 C CB . PRO B 1 45 ? 57.849 -65.855 2.596 1.00 107.04 ? 45 PRO B CB 1 ATOM 3665 C CG . PRO B 1 45 ? 58.439 -64.491 2.592 1.00 105.48 ? 45 PRO B CG 1 ATOM 3666 C CD . PRO B 1 45 ? 58.259 -63.975 3.982 1.00 108.09 ? 45 PRO B CD 1 ATOM 3667 N N . GLU B 1 46 ? 57.295 -67.579 5.039 1.00 119.32 ? 46 GLU B N 1 ATOM 3668 C CA . GLU B 1 46 ? 57.194 -68.910 5.640 1.00 122.91 ? 46 GLU B CA 1 ATOM 3669 C C . GLU B 1 46 ? 55.922 -69.131 6.469 1.00 120.42 ? 46 GLU B C 1 ATOM 3670 O O . GLU B 1 46 ? 55.549 -70.272 6.744 1.00 113.23 ? 46 GLU B O 1 ATOM 3671 C CB . GLU B 1 46 ? 58.417 -69.162 6.517 1.00 130.84 ? 46 GLU B CB 1 ATOM 3672 C CG . GLU B 1 46 ? 58.703 -70.630 6.770 1.00 136.33 ? 46 GLU B CG 1 ATOM 3673 C CD . GLU B 1 46 ? 59.584 -70.850 7.978 1.00 142.61 ? 46 GLU B CD 1 ATOM 3674 O OE1 . GLU B 1 46 ? 59.350 -70.204 9.021 1.00 148.74 ? 46 GLU B OE1 1 ATOM 3675 O OE2 . GLU B 1 46 ? 60.505 -71.680 7.882 1.00 143.70 ? 46 GLU B OE2 1 ATOM 3676 N N . ASN B 1 47 ? 55.282 -68.046 6.898 1.00 124.73 ? 47 ASN B N 1 ATOM 3677 C CA . ASN B 1 47 ? 54.047 -68.122 7.690 1.00 125.20 ? 47 ASN B CA 1 ATOM 3678 C C . ASN B 1 47 ? 52.899 -67.279 7.147 1.00 116.88 ? 47 ASN B C 1 ATOM 3679 O O . ASN B 1 47 ? 51.861 -67.167 7.795 1.00 117.79 ? 47 ASN B O 1 ATOM 3680 C CB . ASN B 1 47 ? 54.344 -67.736 9.140 1.00 130.99 ? 47 ASN B CB 1 ATOM 3681 C CG . ASN B 1 47 ? 55.286 -68.718 9.810 1.00 138.23 ? 47 ASN B CG 1 ATOM 3682 O OD1 . ASN B 1 47 ? 54.919 -69.860 10.080 1.00 141.08 ? 47 ASN B OD1 1 ATOM 3683 N ND2 . ASN B 1 47 ? 56.513 -68.284 10.059 1.00 139.41 ? 47 ASN B ND2 1 ATOM 3684 N N . SER B 1 48 ? 53.083 -66.679 5.975 1.00 109.58 ? 48 SER B N 1 ATOM 3685 C CA . SER B 1 48 ? 51.972 -66.060 5.259 1.00 101.99 ? 48 SER B CA 1 ATOM 3686 C C . SER B 1 48 ? 51.309 -67.114 4.362 1.00 98.63 ? 48 SER B C 1 ATOM 3687 O O . SER B 1 48 ? 51.984 -68.007 3.861 1.00 97.47 ? 48 SER B O 1 ATOM 3688 C CB . SER B 1 48 ? 52.449 -64.866 4.438 1.00 98.31 ? 48 SER B CB 1 ATOM 3689 O OG . SER B 1 48 ? 52.652 -63.733 5.256 1.00 99.74 ? 48 SER B OG 1 ATOM 3690 N N . PRO B 1 49 ? 49.983 -67.033 4.172 1.00 98.58 ? 49 PRO B N 1 ATOM 3691 C CA . PRO B 1 49 ? 49.296 -68.042 3.354 1.00 99.27 ? 49 PRO B CA 1 ATOM 3692 C C . PRO B 1 49 ? 49.656 -68.023 1.871 1.00 96.63 ? 49 PRO B C 1 ATOM 3693 O O . PRO B 1 49 ? 50.388 -67.143 1.407 1.00 88.92 ? 49 PRO B O 1 ATOM 3694 C CB . PRO B 1 49 ? 47.811 -67.686 3.511 1.00 99.91 ? 49 PRO B CB 1 ATOM 3695 C CG . PRO B 1 49 ? 47.734 -66.836 4.735 1.00 102.90 ? 49 PRO B CG 1 ATOM 3696 C CD . PRO B 1 49 ? 49.031 -66.086 4.777 1.00 101.05 ? 49 PRO B CD 1 ATOM 3697 N N . VAL B 1 50 ? 49.111 -69.000 1.152 1.00 95.88 ? 50 VAL B N 1 ATOM 3698 C CA . VAL B 1 50 ? 49.293 -69.132 -0.276 1.00 97.01 ? 50 VAL B CA 1 ATOM 3699 C C . VAL B 1 50 ? 47.959 -68.856 -0.971 1.00 96.79 ? 50 VAL B C 1 ATOM 3700 O O . VAL B 1 50 ? 46.991 -69.588 -0.793 1.00 91.05 ? 50 VAL B O 1 ATOM 3701 C CB . VAL B 1 50 ? 49.809 -70.535 -0.646 1.00 98.59 ? 50 VAL B CB 1 ATOM 3702 C CG1 . VAL B 1 50 ? 49.812 -70.745 -2.155 1.00 98.82 ? 50 VAL B CG1 1 ATOM 3703 C CG2 . VAL B 1 50 ? 51.211 -70.730 -0.110 1.00 102.96 ? 50 VAL B CG2 1 ATOM 3704 N N . VAL B 1 51 ? 47.940 -67.796 -1.775 1.00 97.15 ? 51 VAL B N 1 ATOM 3705 C CA . VAL B 1 51 ? 46.751 -67.361 -2.489 1.00 94.90 ? 51 VAL B CA 1 ATOM 3706 C C . VAL B 1 51 ? 46.908 -67.565 -4.003 1.00 89.17 ? 51 VAL B C 1 ATOM 3707 O O . VAL B 1 51 ? 47.867 -67.086 -4.603 1.00 93.93 ? 51 VAL B O 1 ATOM 3708 C CB . VAL B 1 51 ? 46.496 -65.875 -2.195 1.00 96.29 ? 51 VAL B CB 1 ATOM 3709 C CG1 . VAL B 1 51 ? 45.458 -65.303 -3.146 1.00 98.25 ? 51 VAL B CG1 1 ATOM 3710 C CG2 . VAL B 1 51 ? 46.066 -65.699 -0.748 1.00 98.29 ? 51 VAL B CG2 1 ATOM 3711 N N . LEU B 1 52 ? 45.979 -68.291 -4.607 1.00 81.31 ? 52 LEU B N 1 ATOM 3712 C CA . LEU B 1 52 ? 45.908 -68.403 -6.055 1.00 75.47 ? 52 LEU B CA 1 ATOM 3713 C C . LEU B 1 52 ? 44.941 -67.334 -6.520 1.00 75.70 ? 52 LEU B C 1 ATOM 3714 O O . LEU B 1 52 ? 43.837 -67.219 -5.986 1.00 74.47 ? 52 LEU B O 1 ATOM 3715 C CB . LEU B 1 52 ? 45.378 -69.772 -6.467 1.00 76.87 ? 52 LEU B CB 1 ATOM 3716 C CG . LEU B 1 52 ? 45.095 -69.990 -7.964 1.00 78.83 ? 52 LEU B CG 1 ATOM 3717 C CD1 . LEU B 1 52 ? 46.381 -70.103 -8.767 1.00 79.63 ? 52 LEU B CD1 1 ATOM 3718 C CD2 . LEU B 1 52 ? 44.236 -71.226 -8.181 1.00 79.50 ? 52 LEU B CD2 1 ATOM 3719 N N . TRP B 1 53 ? 45.340 -66.541 -7.507 1.00 73.33 ? 53 TRP B N 1 ATOM 3720 C CA . TRP B 1 53 ? 44.439 -65.568 -8.087 1.00 69.05 ? 53 TRP B CA 1 ATOM 3721 C C . TRP B 1 53 ? 44.204 -65.917 -9.546 1.00 66.23 ? 53 TRP B C 1 ATOM 3722 O O . TRP B 1 53 ? 45.152 -66.011 -10.303 1.00 67.33 ? 53 TRP B O 1 ATOM 3723 C CB . TRP B 1 53 ? 45.014 -64.158 -7.984 1.00 67.35 ? 53 TRP B CB 1 ATOM 3724 C CG . TRP B 1 53 ? 44.169 -63.184 -8.716 1.00 65.59 ? 53 TRP B CG 1 ATOM 3725 C CD1 . TRP B 1 53 ? 44.373 -62.701 -9.968 1.00 64.56 ? 53 TRP B CD1 1 ATOM 3726 C CD2 . TRP B 1 53 ? 42.950 -62.615 -8.258 1.00 67.73 ? 53 TRP B CD2 1 ATOM 3727 N NE1 . TRP B 1 53 ? 43.366 -61.849 -10.317 1.00 63.46 ? 53 TRP B NE1 1 ATOM 3728 C CE2 . TRP B 1 53 ? 42.476 -61.775 -9.280 1.00 67.99 ? 53 TRP B CE2 1 ATOM 3729 C CE3 . TRP B 1 53 ? 42.213 -62.723 -7.075 1.00 68.80 ? 53 TRP B CE3 1 ATOM 3730 C CZ2 . TRP B 1 53 ? 41.297 -61.049 -9.157 1.00 68.72 ? 53 TRP B CZ2 1 ATOM 3731 C CZ3 . TRP B 1 53 ? 41.042 -62.004 -6.951 1.00 68.39 ? 53 TRP B CZ3 1 ATOM 3732 C CH2 . TRP B 1 53 ? 40.593 -61.182 -7.985 1.00 69.07 ? 53 TRP B CH2 1 ATOM 3733 N N . LEU B 1 54 ? 42.946 -66.078 -9.936 1.00 65.52 ? 54 LEU B N 1 ATOM 3734 C CA . LEU B 1 54 ? 42.580 -66.297 -11.337 1.00 64.05 ? 54 LEU B CA 1 ATOM 3735 C C . LEU B 1 54 ? 41.630 -65.213 -11.804 1.00 62.77 ? 54 LEU B C 1 ATOM 3736 O O . LEU B 1 54 ? 40.570 -65.017 -11.214 1.00 60.40 ? 54 LEU B O 1 ATOM 3737 C CB . LEU B 1 54 ? 41.865 -67.626 -11.521 1.00 64.28 ? 54 LEU B CB 1 ATOM 3738 C CG . LEU B 1 54 ? 42.601 -68.941 -11.301 1.00 67.19 ? 54 LEU B CG 1 ATOM 3739 C CD1 . LEU B 1 54 ? 41.633 -70.099 -11.475 1.00 66.18 ? 54 LEU B CD1 1 ATOM 3740 C CD2 . LEU B 1 54 ? 43.775 -69.085 -12.249 1.00 68.05 ? 54 LEU B CD2 1 ATOM 3741 N N . ASN B 1 55 ? 42.010 -64.506 -12.862 1.00 63.65 ? 55 ASN B N 1 ATOM 3742 C CA . ASN B 1 55 ? 41.065 -63.668 -13.572 1.00 59.04 ? 55 ASN B CA 1 ATOM 3743 C C . ASN B 1 55 ? 40.237 -64.557 -14.472 1.00 59.80 ? 55 ASN B C 1 ATOM 3744 O O . ASN B 1 55 ? 40.596 -65.706 -14.730 1.00 59.33 ? 55 ASN B O 1 ATOM 3745 C CB . ASN B 1 55 ? 41.771 -62.593 -14.371 1.00 58.37 ? 55 ASN B CB 1 ATOM 3746 C CG . ASN B 1 55 ? 42.057 -61.358 -13.551 1.00 59.34 ? 55 ASN B CG 1 ATOM 3747 O OD1 . ASN B 1 55 ? 43.189 -61.135 -13.127 1.00 62.92 ? 55 ASN B OD1 1 ATOM 3748 N ND2 . ASN B 1 55 ? 41.031 -60.563 -13.296 1.00 59.65 ? 55 ASN B ND2 1 ATOM 3749 N N . GLY B 1 56 ? 39.113 -64.032 -14.926 1.00 61.87 ? 56 GLY B N 1 ATOM 3750 C CA . GLY B 1 56 ? 38.153 -64.824 -15.669 1.00 64.48 ? 56 GLY B CA 1 ATOM 3751 C C . GLY B 1 56 ? 38.338 -64.688 -17.160 1.00 65.34 ? 56 GLY B C 1 ATOM 3752 O O . GLY B 1 56 ? 39.411 -64.992 -17.696 1.00 65.23 ? 56 GLY B O 1 ATOM 3753 N N . GLY B 1 57 ? 37.270 -64.245 -17.818 1.00 65.00 ? 57 GLY B N 1 ATOM 3754 C CA . GLY B 1 57 ? 37.246 -64.057 -19.266 1.00 63.06 ? 57 GLY B CA 1 ATOM 3755 C C . GLY B 1 57 ? 35.982 -64.684 -19.817 1.00 62.76 ? 57 GLY B C 1 ATOM 3756 O O . GLY B 1 57 ? 34.957 -64.014 -19.918 1.00 59.37 ? 57 GLY B O 1 ATOM 3757 N N . PRO B 1 58 ? 36.042 -65.975 -20.185 1.00 63.49 ? 58 PRO B N 1 ATOM 3758 C CA . PRO B 1 58 ? 37.238 -66.834 -20.271 1.00 65.44 ? 58 PRO B CA 1 ATOM 3759 C C . PRO B 1 58 ? 38.154 -66.393 -21.388 1.00 66.10 ? 58 PRO B C 1 ATOM 3760 O O . PRO B 1 58 ? 37.676 -65.933 -22.431 1.00 68.03 ? 58 PRO B O 1 ATOM 3761 C CB . PRO B 1 58 ? 36.683 -68.206 -20.635 1.00 66.26 ? 58 PRO B CB 1 ATOM 3762 C CG . PRO B 1 58 ? 35.232 -68.129 -20.364 1.00 66.52 ? 58 PRO B CG 1 ATOM 3763 C CD . PRO B 1 58 ? 34.814 -66.707 -20.496 1.00 62.83 ? 58 PRO B CD 1 ATOM 3764 N N . GLY B 1 59 ? 39.450 -66.523 -21.174 1.00 62.01 ? 59 GLY B N 1 ATOM 3765 C CA . GLY B 1 59 ? 40.416 -66.073 -22.148 1.00 60.09 ? 59 GLY B CA 1 ATOM 3766 C C . GLY B 1 59 ? 41.278 -64.932 -21.672 1.00 62.22 ? 59 GLY B C 1 ATOM 3767 O O . GLY B 1 59 ? 42.251 -64.602 -22.343 1.00 65.07 ? 59 GLY B O 1 ATOM 3768 N N . CYS B 1 60 ? 40.951 -64.348 -20.514 1.00 64.33 ? 60 CYS B N 1 ATOM 3769 C CA . CYS B 1 60 ? 41.687 -63.198 -19.976 1.00 64.61 ? 60 CYS B CA 1 ATOM 3770 C C . CYS B 1 60 ? 42.753 -63.546 -18.932 1.00 63.89 ? 60 CYS B C 1 ATOM 3771 O O . CYS B 1 60 ? 42.685 -64.551 -18.250 1.00 64.01 ? 60 CYS B O 1 ATOM 3772 C CB . CYS B 1 60 ? 40.726 -62.157 -19.414 1.00 65.69 ? 60 CYS B CB 1 ATOM 3773 S SG . CYS B 1 60 ? 39.540 -61.568 -20.646 1.00 72.84 ? 60 CYS B SG 1 ATOM 3774 N N . SER B 1 61 ? 43.740 -62.676 -18.827 1.00 64.83 ? 61 SER B N 1 ATOM 3775 C CA . SER B 1 61 ? 44.963 -62.953 -18.100 1.00 62.93 ? 61 SER B CA 1 ATOM 3776 C C . SER B 1 61 ? 44.891 -62.558 -16.658 1.00 60.52 ? 61 SER B C 1 ATOM 3777 O O . SER B 1 61 ? 44.400 -61.483 -16.345 1.00 55.35 ? 61 SER B O 1 ATOM 3778 C CB . SER B 1 61 ? 46.115 -62.163 -18.716 1.00 64.36 ? 61 SER B CB 1 ATOM 3779 O OG . SER B 1 61 ? 47.312 -62.391 -17.995 1.00 65.46 ? 61 SER B OG 1 ATOM 3780 N N . SER B 1 62 ? 45.468 -63.396 -15.801 1.00 63.52 ? 62 SER B N 1 ATOM 3781 C CA . SER B 1 62 ? 45.628 -63.088 -14.380 1.00 65.24 ? 62 SER B CA 1 ATOM 3782 C C . SER B 1 62 ? 46.762 -62.085 -14.101 1.00 67.78 ? 62 SER B C 1 ATOM 3783 O O . SER B 1 62 ? 46.955 -61.664 -12.960 1.00 66.73 ? 62 SER B O 1 ATOM 3784 C CB . SER B 1 62 ? 45.873 -64.366 -13.589 1.00 66.73 ? 62 SER B CB 1 ATOM 3785 O OG . SER B 1 62 ? 44.795 -65.270 -13.727 1.00 69.57 ? 62 SER B OG 1 ATOM 3786 N N . LEU B 1 63 ? 47.513 -61.696 -15.126 1.00 69.35 ? 63 LEU B N 1 ATOM 3787 C CA . LEU B 1 63 ? 48.510 -60.650 -14.940 1.00 71.02 ? 63 LEU B CA 1 ATOM 3788 C C . LEU B 1 63 ? 47.871 -59.279 -14.941 1.00 72.28 ? 63 LEU B C 1 ATOM 3789 O O . LEU B 1 63 ? 48.477 -58.315 -14.479 1.00 73.06 ? 63 LEU B O 1 ATOM 3790 C CB . LEU B 1 63 ? 49.610 -60.737 -15.996 1.00 71.51 ? 63 LEU B CB 1 ATOM 3791 C CG . LEU B 1 63 ? 50.395 -62.048 -15.990 1.00 72.06 ? 63 LEU B CG 1 ATOM 3792 C CD1 . LEU B 1 63 ? 51.608 -61.921 -16.900 1.00 74.14 ? 63 LEU B CD1 1 ATOM 3793 C CD2 . LEU B 1 63 ? 50.809 -62.470 -14.582 1.00 68.64 ? 63 LEU B CD2 1 ATOM 3794 N N . ASP B 1 64 ? 46.660 -59.182 -15.475 1.00 75.82 ? 64 ASP B N 1 ATOM 3795 C CA . ASP B 1 64 ? 45.852 -57.989 -15.270 1.00 80.86 ? 64 ASP B CA 1 ATOM 3796 C C . ASP B 1 64 ? 45.657 -57.788 -13.768 1.00 79.29 ? 64 ASP B C 1 ATOM 3797 O O . ASP B 1 64 ? 45.822 -56.680 -13.259 1.00 80.95 ? 64 ASP B O 1 ATOM 3798 C CB . ASP B 1 64 ? 44.496 -58.103 -15.973 1.00 85.23 ? 64 ASP B CB 1 ATOM 3799 C CG . ASP B 1 64 ? 43.713 -56.801 -15.949 1.00 90.67 ? 64 ASP B CG 1 ATOM 3800 O OD1 . ASP B 1 64 ? 44.265 -55.759 -16.362 1.00 90.85 ? 64 ASP B OD1 1 ATOM 3801 O OD2 . ASP B 1 64 ? 42.540 -56.818 -15.517 1.00 99.99 ? 64 ASP B OD2 1 ATOM 3802 N N . GLY B 1 65 ? 45.307 -58.866 -13.071 1.00 78.67 ? 65 GLY B N 1 ATOM 3803 C CA . GLY B 1 65 ? 45.142 -58.841 -11.618 1.00 77.85 ? 65 GLY B CA 1 ATOM 3804 C C . GLY B 1 65 ? 46.353 -58.255 -10.943 1.00 78.08 ? 65 GLY B C 1 ATOM 3805 O O . GLY B 1 65 ? 46.264 -57.300 -10.170 1.00 77.66 ? 65 GLY B O 1 ATOM 3806 N N . LEU B 1 66 ? 47.505 -58.810 -11.279 1.00 78.45 ? 66 LEU B N 1 ATOM 3807 C CA . LEU B 1 66 ? 48.750 -58.314 -10.732 1.00 75.71 ? 66 LEU B CA 1 ATOM 3808 C C . LEU B 1 66 ? 48.970 -56.844 -11.067 1.00 71.75 ? 66 LEU B C 1 ATOM 3809 O O . LEU B 1 66 ? 49.118 -56.017 -10.164 1.00 70.48 ? 66 LEU B O 1 ATOM 3810 C CB . LEU B 1 66 ? 49.920 -59.154 -11.236 1.00 75.26 ? 66 LEU B CB 1 ATOM 3811 C CG . LEU B 1 66 ? 51.162 -59.006 -10.366 1.00 77.91 ? 66 LEU B CG 1 ATOM 3812 C CD1 . LEU B 1 66 ? 52.090 -60.167 -10.624 1.00 82.68 ? 66 LEU B CD1 1 ATOM 3813 C CD2 . LEU B 1 66 ? 51.888 -57.695 -10.613 1.00 82.82 ? 66 LEU B CD2 1 ATOM 3814 N N . LEU B 1 67 ? 48.972 -56.527 -12.361 1.00 70.57 ? 67 LEU B N 1 ATOM 3815 C CA . LEU B 1 67 ? 49.458 -55.236 -12.843 1.00 70.50 ? 67 LEU B CA 1 ATOM 3816 C C . LEU B 1 67 ? 48.467 -54.082 -12.760 1.00 72.71 ? 67 LEU B C 1 ATOM 3817 O O . LEU B 1 67 ? 48.885 -52.913 -12.835 1.00 71.54 ? 67 LEU B O 1 ATOM 3818 C CB . LEU B 1 67 ? 49.949 -55.353 -14.280 1.00 70.29 ? 67 LEU B CB 1 ATOM 3819 C CG . LEU B 1 67 ? 51.292 -56.064 -14.423 1.00 71.95 ? 67 LEU B CG 1 ATOM 3820 C CD1 . LEU B 1 67 ? 51.523 -56.482 -15.862 1.00 71.47 ? 67 LEU B CD1 1 ATOM 3821 C CD2 . LEU B 1 67 ? 52.437 -55.188 -13.933 1.00 73.61 ? 67 LEU B CD2 1 ATOM 3822 N N . THR B 1 68 ? 47.176 -54.386 -12.592 1.00 70.37 ? 68 THR B N 1 ATOM 3823 C CA . THR B 1 68 ? 46.167 -53.334 -12.503 1.00 66.63 ? 68 THR B CA 1 ATOM 3824 C C . THR B 1 68 ? 45.220 -53.426 -11.320 1.00 64.40 ? 68 THR B C 1 ATOM 3825 O O . THR B 1 68 ? 44.427 -52.521 -11.138 1.00 64.66 ? 68 THR B O 1 ATOM 3826 C CB . THR B 1 68 ? 45.320 -53.280 -13.776 1.00 69.39 ? 68 THR B CB 1 ATOM 3827 O OG1 . THR B 1 68 ? 44.373 -54.352 -13.760 1.00 71.99 ? 68 THR B OG1 1 ATOM 3828 C CG2 . THR B 1 68 ? 46.202 -53.389 -15.029 1.00 68.73 ? 68 THR B CG2 1 ATOM 3829 N N . GLU B 1 69 ? 45.299 -54.480 -10.512 1.00 65.93 ? 69 GLU B N 1 ATOM 3830 C CA . GLU B 1 69 ? 44.365 -54.656 -9.395 1.00 68.87 ? 69 GLU B CA 1 ATOM 3831 C C . GLU B 1 69 ? 45.015 -54.693 -8.004 1.00 73.82 ? 69 GLU B C 1 ATOM 3832 O O . GLU B 1 69 ? 44.795 -53.779 -7.197 1.00 82.83 ? 69 GLU B O 1 ATOM 3833 C CB . GLU B 1 69 ? 43.540 -55.916 -9.575 1.00 68.11 ? 69 GLU B CB 1 ATOM 3834 C CG . GLU B 1 69 ? 42.775 -55.998 -10.874 1.00 64.98 ? 69 GLU B CG 1 ATOM 3835 C CD . GLU B 1 69 ? 41.760 -57.108 -10.823 1.00 64.29 ? 69 GLU B CD 1 ATOM 3836 O OE1 . GLU B 1 69 ? 40.792 -56.979 -10.037 1.00 59.95 ? 69 GLU B OE1 1 ATOM 3837 O OE2 . GLU B 1 69 ? 41.937 -58.111 -11.541 1.00 65.78 ? 69 GLU B OE2 1 ATOM 3838 N N . HIS B 1 70 ? 45.774 -55.741 -7.694 1.00 69.39 ? 70 HIS B N 1 ATOM 3839 C CA . HIS B 1 70 ? 46.317 -55.869 -6.339 1.00 70.84 ? 70 HIS B CA 1 ATOM 3840 C C . HIS B 1 70 ? 47.707 -56.481 -6.237 1.00 72.93 ? 70 HIS B C 1 ATOM 3841 O O . HIS B 1 70 ? 48.072 -57.014 -5.196 1.00 74.79 ? 70 HIS B O 1 ATOM 3842 C CB . HIS B 1 70 ? 45.342 -56.659 -5.468 1.00 71.17 ? 70 HIS B CB 1 ATOM 3843 C CG . HIS B 1 70 ? 45.008 -58.013 -6.002 1.00 66.66 ? 70 HIS B CG 1 ATOM 3844 N ND1 . HIS B 1 70 ? 43.756 -58.567 -5.882 1.00 66.08 ? 70 HIS B ND1 1 ATOM 3845 C CD2 . HIS B 1 70 ? 45.754 -58.919 -6.664 1.00 63.95 ? 70 HIS B CD2 1 ATOM 3846 C CE1 . HIS B 1 70 ? 43.753 -59.765 -6.432 1.00 65.44 ? 70 HIS B CE1 1 ATOM 3847 N NE2 . HIS B 1 70 ? 44.954 -60.004 -6.910 1.00 62.83 ? 70 HIS B NE2 1 ATOM 3848 N N . GLY B 1 71 ? 48.483 -56.398 -7.308 1.00 75.89 ? 71 GLY B N 1 ATOM 3849 C CA . GLY B 1 71 ? 49.845 -56.862 -7.268 1.00 77.60 ? 71 GLY B CA 1 ATOM 3850 C C . GLY B 1 71 ? 50.630 -55.885 -6.433 1.00 82.50 ? 71 GLY B C 1 ATOM 3851 O O . GLY B 1 71 ? 50.141 -54.810 -6.124 1.00 79.52 ? 71 GLY B O 1 ATOM 3852 N N . PRO B 1 72 ? 51.863 -56.254 -6.063 1.00 88.66 ? 72 PRO B N 1 ATOM 3853 C CA . PRO B 1 72 ? 52.779 -55.376 -5.331 1.00 87.72 ? 72 PRO B CA 1 ATOM 3854 C C . PRO B 1 72 ? 53.105 -54.089 -6.072 1.00 87.26 ? 72 PRO B C 1 ATOM 3855 O O . PRO B 1 72 ? 53.481 -53.094 -5.459 1.00 92.24 ? 72 PRO B O 1 ATOM 3856 C CB . PRO B 1 72 ? 54.040 -56.227 -5.178 1.00 92.02 ? 72 PRO B CB 1 ATOM 3857 C CG . PRO B 1 72 ? 53.928 -57.309 -6.196 1.00 92.06 ? 72 PRO B CG 1 ATOM 3858 C CD . PRO B 1 72 ? 52.465 -57.568 -6.332 1.00 90.89 ? 72 PRO B CD 1 ATOM 3859 N N . PHE B 1 73 ? 52.987 -54.111 -7.391 1.00 86.07 ? 73 PHE B N 1 ATOM 3860 C CA . PHE B 1 73 ? 53.227 -52.919 -8.185 1.00 85.76 ? 73 PHE B CA 1 ATOM 3861 C C . PHE B 1 73 ? 52.292 -52.892 -9.374 1.00 81.46 ? 73 PHE B C 1 ATOM 3862 O O . PHE B 1 73 ? 51.929 -53.940 -9.904 1.00 80.79 ? 73 PHE B O 1 ATOM 3863 C CB . PHE B 1 73 ? 54.680 -52.861 -8.653 1.00 84.25 ? 73 PHE B CB 1 ATOM 3864 C CG . PHE B 1 73 ? 55.297 -54.207 -8.867 1.00 83.06 ? 73 PHE B CG 1 ATOM 3865 C CD1 . PHE B 1 73 ? 54.923 -54.988 -9.947 1.00 80.16 ? 73 PHE B CD1 1 ATOM 3866 C CD2 . PHE B 1 73 ? 56.242 -54.698 -7.979 1.00 82.77 ? 73 PHE B CD2 1 ATOM 3867 C CE1 . PHE B 1 73 ? 55.488 -56.231 -10.146 1.00 79.36 ? 73 PHE B CE1 1 ATOM 3868 C CE2 . PHE B 1 73 ? 56.807 -55.939 -8.170 1.00 81.67 ? 73 PHE B CE2 1 ATOM 3869 C CZ . PHE B 1 73 ? 56.431 -56.708 -9.256 1.00 80.16 ? 73 PHE B CZ 1 ATOM 3870 N N . LEU B 1 74 ? 51.894 -51.692 -9.766 1.00 76.05 ? 74 LEU B N 1 ATOM 3871 C CA . LEU B 1 74 ? 50.955 -51.516 -10.847 1.00 74.91 ? 74 LEU B CA 1 ATOM 3872 C C . LEU B 1 74 ? 51.621 -50.743 -11.984 1.00 74.92 ? 74 LEU B C 1 ATOM 3873 O O . LEU B 1 74 ? 52.238 -49.705 -11.754 1.00 74.76 ? 74 LEU B O 1 ATOM 3874 C CB . LEU B 1 74 ? 49.718 -50.750 -10.361 1.00 71.33 ? 74 LEU B CB 1 ATOM 3875 C CG . LEU B 1 74 ? 49.076 -51.149 -9.035 1.00 71.79 ? 74 LEU B CG 1 ATOM 3876 C CD1 . LEU B 1 74 ? 47.989 -50.147 -8.695 1.00 73.71 ? 74 LEU B CD1 1 ATOM 3877 C CD2 . LEU B 1 74 ? 48.513 -52.562 -9.084 1.00 71.04 ? 74 LEU B CD2 1 ATOM 3878 N N . VAL B 1 75 ? 51.459 -51.237 -13.204 1.00 68.45 ? 75 VAL B N 1 ATOM 3879 C CA . VAL B 1 75 ? 51.877 -50.511 -14.386 1.00 70.70 ? 75 VAL B CA 1 ATOM 3880 C C . VAL B 1 75 ? 51.169 -49.164 -14.461 1.00 73.58 ? 75 VAL B C 1 ATOM 3881 O O . VAL B 1 75 ? 49.957 -49.081 -14.205 1.00 75.11 ? 75 VAL B O 1 ATOM 3882 C CB . VAL B 1 75 ? 51.594 -51.333 -15.670 1.00 71.15 ? 75 VAL B CB 1 ATOM 3883 C CG1 . VAL B 1 75 ? 50.106 -51.368 -15.996 1.00 68.10 ? 75 VAL B CG1 1 ATOM 3884 C CG2 . VAL B 1 75 ? 52.391 -50.802 -16.852 1.00 71.46 ? 75 VAL B CG2 1 ATOM 3885 N N . GLN B 1 76 ? 51.926 -48.132 -14.842 1.00 75.94 ? 76 GLN B N 1 ATOM 3886 C CA . GLN B 1 76 ? 51.427 -46.754 -14.987 1.00 75.51 ? 76 GLN B CA 1 ATOM 3887 C C . GLN B 1 76 ? 51.103 -46.452 -16.457 1.00 74.55 ? 76 GLN B C 1 ATOM 3888 O O . GLN B 1 76 ? 51.529 -47.190 -17.339 1.00 76.39 ? 76 GLN B O 1 ATOM 3889 C CB . GLN B 1 76 ? 52.476 -45.775 -14.488 1.00 78.08 ? 76 GLN B CB 1 ATOM 3890 C CG . GLN B 1 76 ? 52.994 -46.080 -13.092 1.00 79.39 ? 76 GLN B CG 1 ATOM 3891 C CD . GLN B 1 76 ? 52.003 -45.806 -11.982 1.00 80.47 ? 76 GLN B CD 1 ATOM 3892 O OE1 . GLN B 1 76 ? 51.927 -44.688 -11.452 1.00 85.01 ? 76 GLN B OE1 1 ATOM 3893 N NE2 . GLN B 1 76 ? 51.276 -46.835 -11.577 1.00 79.48 ? 76 GLN B NE2 1 ATOM 3894 N N . PRO B 1 77 ? 50.370 -45.360 -16.729 1.00 72.79 ? 77 PRO B N 1 ATOM 3895 C CA . PRO B 1 77 ? 49.806 -45.118 -18.065 1.00 73.40 ? 77 PRO B CA 1 ATOM 3896 C C . PRO B 1 77 ? 50.794 -45.028 -19.231 1.00 82.88 ? 77 PRO B C 1 ATOM 3897 O O . PRO B 1 77 ? 50.395 -45.227 -20.379 1.00 82.65 ? 77 PRO B O 1 ATOM 3898 C CB . PRO B 1 77 ? 49.089 -43.792 -17.899 1.00 72.47 ? 77 PRO B CB 1 ATOM 3899 C CG . PRO B 1 77 ? 48.813 -43.690 -16.439 1.00 71.04 ? 77 PRO B CG 1 ATOM 3900 C CD . PRO B 1 77 ? 50.011 -44.283 -15.796 1.00 72.33 ? 77 PRO B CD 1 ATOM 3901 N N . ASP B 1 78 ? 52.062 -44.734 -18.945 1.00 91.64 ? 78 ASP B N 1 ATOM 3902 C CA . ASP B 1 78 ? 53.105 -44.708 -19.983 1.00 93.54 ? 78 ASP B CA 1 ATOM 3903 C C . ASP B 1 78 ? 53.508 -46.098 -20.486 1.00 90.44 ? 78 ASP B C 1 ATOM 3904 O O . ASP B 1 78 ? 54.310 -46.209 -21.399 1.00 102.27 ? 78 ASP B O 1 ATOM 3905 C CB . ASP B 1 78 ? 54.351 -43.970 -19.484 1.00 95.39 ? 78 ASP B CB 1 ATOM 3906 C CG . ASP B 1 78 ? 54.971 -44.617 -18.260 1.00 98.74 ? 78 ASP B CG 1 ATOM 3907 O OD1 . ASP B 1 78 ? 54.783 -45.831 -18.048 1.00 102.39 ? 78 ASP B OD1 1 ATOM 3908 O OD2 . ASP B 1 78 ? 55.647 -43.907 -17.496 1.00 100.33 ? 78 ASP B OD2 1 ATOM 3909 N N . GLY B 1 79 ? 52.989 -47.150 -19.878 1.00 82.51 ? 79 GLY B N 1 ATOM 3910 C CA . GLY B 1 79 ? 53.306 -48.507 -20.297 1.00 81.11 ? 79 GLY B CA 1 ATOM 3911 C C . GLY B 1 79 ? 54.700 -48.974 -19.921 1.00 82.57 ? 79 GLY B C 1 ATOM 3912 O O . GLY B 1 79 ? 55.076 -50.093 -20.238 1.00 82.38 ? 79 GLY B O 1 ATOM 3913 N N . VAL B 1 80 ? 55.446 -48.137 -19.215 1.00 84.24 ? 80 VAL B N 1 ATOM 3914 C CA . VAL B 1 80 ? 56.862 -48.357 -18.972 1.00 89.02 ? 80 VAL B CA 1 ATOM 3915 C C . VAL B 1 80 ? 57.195 -48.406 -17.476 1.00 88.93 ? 80 VAL B C 1 ATOM 3916 O O . VAL B 1 80 ? 57.976 -49.245 -17.028 1.00 90.76 ? 80 VAL B O 1 ATOM 3917 C CB . VAL B 1 80 ? 57.688 -47.243 -19.660 1.00 93.53 ? 80 VAL B CB 1 ATOM 3918 C CG1 . VAL B 1 80 ? 59.096 -47.157 -19.089 1.00 94.01 ? 80 VAL B CG1 1 ATOM 3919 C CG2 . VAL B 1 80 ? 57.741 -47.470 -21.164 1.00 93.54 ? 80 VAL B CG2 1 ATOM 3920 N N . THR B 1 81 ? 56.620 -47.488 -16.717 1.00 86.71 ? 81 THR B N 1 ATOM 3921 C CA . THR B 1 81 ? 56.909 -47.356 -15.302 1.00 88.54 ? 81 THR B CA 1 ATOM 3922 C C . THR B 1 81 ? 55.973 -48.212 -14.459 1.00 86.67 ? 81 THR B C 1 ATOM 3923 O O . THR B 1 81 ? 54.770 -48.257 -14.715 1.00 83.42 ? 81 THR B O 1 ATOM 3924 C CB . THR B 1 81 ? 56.721 -45.899 -14.856 1.00 92.66 ? 81 THR B CB 1 ATOM 3925 O OG1 . THR B 1 81 ? 57.283 -45.028 -15.841 1.00 96.13 ? 81 THR B OG1 1 ATOM 3926 C CG2 . THR B 1 81 ? 57.372 -45.650 -13.483 1.00 93.30 ? 81 THR B CG2 1 ATOM 3927 N N . LEU B 1 82 ? 56.543 -48.877 -13.453 1.00 86.27 ? 82 LEU B N 1 ATOM 3928 C CA . LEU B 1 82 ? 55.796 -49.597 -12.424 1.00 79.96 ? 82 LEU B CA 1 ATOM 3929 C C . LEU B 1 82 ? 55.910 -48.827 -11.119 1.00 84.67 ? 82 LEU B C 1 ATOM 3930 O O . LEU B 1 82 ? 57.002 -48.404 -10.748 1.00 88.98 ? 82 LEU B O 1 ATOM 3931 C CB . LEU B 1 82 ? 56.384 -50.996 -12.226 1.00 76.85 ? 82 LEU B CB 1 ATOM 3932 C CG . LEU B 1 82 ? 56.314 -52.034 -13.356 1.00 74.93 ? 82 LEU B CG 1 ATOM 3933 C CD1 . LEU B 1 82 ? 56.616 -53.397 -12.789 1.00 74.15 ? 82 LEU B CD1 1 ATOM 3934 C CD2 . LEU B 1 82 ? 54.948 -52.092 -14.020 1.00 75.59 ? 82 LEU B CD2 1 ATOM 3935 N N . GLU B 1 83 ? 54.791 -48.646 -10.420 1.00 88.67 ? 83 GLU B N 1 ATOM 3936 C CA . GLU B 1 83 ? 54.792 -48.024 -9.085 1.00 87.95 ? 83 GLU B CA 1 ATOM 3937 C C . GLU B 1 83 ? 54.332 -49.059 -8.066 1.00 88.10 ? 83 GLU B C 1 ATOM 3938 O O . GLU B 1 83 ? 53.432 -49.840 -8.340 1.00 85.52 ? 83 GLU B O 1 ATOM 3939 C CB . GLU B 1 83 ? 53.873 -46.796 -9.021 1.00 84.92 ? 83 GLU B CB 1 ATOM 3940 C CG . GLU B 1 83 ? 54.393 -45.528 -9.690 1.00 91.20 ? 83 GLU B CG 1 ATOM 3941 C CD . GLU B 1 83 ? 55.791 -45.083 -9.243 1.00 97.01 ? 83 GLU B CD 1 ATOM 3942 O OE1 . GLU B 1 83 ? 56.233 -45.403 -8.109 1.00 98.76 ? 83 GLU B OE1 1 ATOM 3943 O OE2 . GLU B 1 83 ? 56.458 -44.402 -10.053 1.00 96.14 ? 83 GLU B OE2 1 ATOM 3944 N N . TYR B 1 84 ? 54.943 -49.052 -6.883 1.00 91.49 ? 84 TYR B N 1 ATOM 3945 C CA . TYR B 1 84 ? 54.553 -49.986 -5.835 1.00 91.87 ? 84 TYR B CA 1 ATOM 3946 C C . TYR B 1 84 ? 53.123 -49.701 -5.436 1.00 86.84 ? 84 TYR B C 1 ATOM 3947 O O . TYR B 1 84 ? 52.629 -48.586 -5.605 1.00 86.85 ? 84 TYR B O 1 ATOM 3948 C CB . TYR B 1 84 ? 55.482 -49.934 -4.600 1.00 95.91 ? 84 TYR B CB 1 ATOM 3949 C CG . TYR B 1 84 ? 56.727 -50.765 -4.763 1.00 101.05 ? 84 TYR B CG 1 ATOM 3950 C CD1 . TYR B 1 84 ? 57.631 -50.454 -5.762 1.00 102.97 ? 84 TYR B CD1 1 ATOM 3951 C CD2 . TYR B 1 84 ? 57.008 -51.869 -3.935 1.00 100.75 ? 84 TYR B CD2 1 ATOM 3952 C CE1 . TYR B 1 84 ? 58.780 -51.193 -5.948 1.00 103.64 ? 84 TYR B CE1 1 ATOM 3953 C CE2 . TYR B 1 84 ? 58.162 -52.625 -4.126 1.00 101.51 ? 84 TYR B CE2 1 ATOM 3954 C CZ . TYR B 1 84 ? 59.045 -52.272 -5.142 1.00 102.80 ? 84 TYR B CZ 1 ATOM 3955 O OH . TYR B 1 84 ? 60.213 -52.945 -5.391 1.00 100.48 ? 84 TYR B OH 1 ATOM 3956 N N . ASN B 1 85 ? 52.472 -50.723 -4.912 1.00 83.95 ? 85 ASN B N 1 ATOM 3957 C CA . ASN B 1 85 ? 51.085 -50.652 -4.521 1.00 80.51 ? 85 ASN B CA 1 ATOM 3958 C C . ASN B 1 85 ? 50.991 -50.816 -3.007 1.00 80.67 ? 85 ASN B C 1 ATOM 3959 O O . ASN B 1 85 ? 51.216 -51.907 -2.500 1.00 77.84 ? 85 ASN B O 1 ATOM 3960 C CB . ASN B 1 85 ? 50.321 -51.756 -5.240 1.00 78.03 ? 85 ASN B CB 1 ATOM 3961 C CG . ASN B 1 85 ? 48.858 -51.806 -4.861 1.00 78.66 ? 85 ASN B CG 1 ATOM 3962 O OD1 . ASN B 1 85 ? 48.371 -51.009 -4.064 1.00 79.69 ? 85 ASN B OD1 1 ATOM 3963 N ND2 . ASN B 1 85 ? 48.150 -52.755 -5.433 1.00 78.16 ? 85 ASN B ND2 1 ATOM 3964 N N . PRO B 1 86 ? 50.639 -49.737 -2.283 1.00 80.58 ? 86 PRO B N 1 ATOM 3965 C CA . PRO B 1 86 ? 50.560 -49.794 -0.819 1.00 79.73 ? 86 PRO B CA 1 ATOM 3966 C C . PRO B 1 86 ? 49.444 -50.688 -0.288 1.00 78.93 ? 86 PRO B C 1 ATOM 3967 O O . PRO B 1 86 ? 49.448 -51.046 0.891 1.00 80.37 ? 86 PRO B O 1 ATOM 3968 C CB . PRO B 1 86 ? 50.269 -48.339 -0.410 1.00 81.84 ? 86 PRO B CB 1 ATOM 3969 C CG . PRO B 1 86 ? 50.129 -47.554 -1.671 1.00 81.25 ? 86 PRO B CG 1 ATOM 3970 C CD . PRO B 1 86 ? 50.016 -48.514 -2.813 1.00 79.44 ? 86 PRO B CD 1 ATOM 3971 N N . TYR B 1 87 ? 48.481 -51.014 -1.145 1.00 77.46 ? 87 TYR B N 1 ATOM 3972 C CA . TYR B 1 87 ? 47.368 -51.877 -0.776 1.00 74.26 ? 87 TYR B CA 1 ATOM 3973 C C . TYR B 1 87 ? 47.507 -53.262 -1.388 1.00 73.17 ? 87 TYR B C 1 ATOM 3974 O O . TYR B 1 87 ? 46.522 -53.972 -1.491 1.00 74.28 ? 87 TYR B O 1 ATOM 3975 C CB . TYR B 1 87 ? 46.051 -51.227 -1.210 1.00 72.70 ? 87 TYR B CB 1 ATOM 3976 C CG . TYR B 1 87 ? 45.942 -49.793 -0.751 1.00 74.55 ? 87 TYR B CG 1 ATOM 3977 C CD1 . TYR B 1 87 ? 45.943 -49.477 0.615 1.00 76.39 ? 87 TYR B CD1 1 ATOM 3978 C CD2 . TYR B 1 87 ? 45.868 -48.749 -1.662 1.00 73.66 ? 87 TYR B CD2 1 ATOM 3979 C CE1 . TYR B 1 87 ? 45.868 -48.172 1.054 1.00 74.55 ? 87 TYR B CE1 1 ATOM 3980 C CE2 . TYR B 1 87 ? 45.790 -47.435 -1.224 1.00 73.28 ? 87 TYR B CE2 1 ATOM 3981 C CZ . TYR B 1 87 ? 45.788 -47.160 0.137 1.00 72.81 ? 87 TYR B CZ 1 ATOM 3982 O OH . TYR B 1 87 ? 45.728 -45.880 0.603 1.00 70.88 ? 87 TYR B OH 1 ATOM 3983 N N . SER B 1 88 ? 48.715 -53.659 -1.778 1.00 74.47 ? 88 SER B N 1 ATOM 3984 C CA . SER B 1 88 ? 48.905 -54.954 -2.445 1.00 76.80 ? 88 SER B CA 1 ATOM 3985 C C . SER B 1 88 ? 48.575 -56.126 -1.555 1.00 76.10 ? 88 SER B C 1 ATOM 3986 O O . SER B 1 88 ? 48.881 -56.123 -0.368 1.00 83.76 ? 88 SER B O 1 ATOM 3987 C CB . SER B 1 88 ? 50.332 -55.148 -2.929 1.00 78.57 ? 88 SER B CB 1 ATOM 3988 O OG . SER B 1 88 ? 50.489 -56.480 -3.403 1.00 78.32 ? 88 SER B OG 1 ATOM 3989 N N . TRP B 1 89 ? 47.998 -57.152 -2.156 1.00 72.32 ? 89 TRP B N 1 ATOM 3990 C CA . TRP B 1 89 ? 47.599 -58.330 -1.414 1.00 74.22 ? 89 TRP B CA 1 ATOM 3991 C C . TRP B 1 89 ? 48.789 -59.137 -0.938 1.00 76.67 ? 89 TRP B C 1 ATOM 3992 O O . TRP B 1 89 ? 48.692 -59.845 0.065 1.00 77.52 ? 89 TRP B O 1 ATOM 3993 C CB . TRP B 1 89 ? 46.655 -59.199 -2.241 1.00 71.91 ? 89 TRP B CB 1 ATOM 3994 C CG . TRP B 1 89 ? 45.291 -58.605 -2.346 1.00 72.61 ? 89 TRP B CG 1 ATOM 3995 C CD1 . TRP B 1 89 ? 44.945 -57.296 -2.147 1.00 73.25 ? 89 TRP B CD1 1 ATOM 3996 C CD2 . TRP B 1 89 ? 44.087 -59.287 -2.703 1.00 69.40 ? 89 TRP B CD2 1 ATOM 3997 N NE1 . TRP B 1 89 ? 43.600 -57.134 -2.352 1.00 73.20 ? 89 TRP B NE1 1 ATOM 3998 C CE2 . TRP B 1 89 ? 43.052 -58.339 -2.692 1.00 69.96 ? 89 TRP B CE2 1 ATOM 3999 C CE3 . TRP B 1 89 ? 43.787 -60.604 -3.033 1.00 69.27 ? 89 TRP B CE3 1 ATOM 4000 C CZ2 . TRP B 1 89 ? 41.734 -58.672 -2.992 1.00 69.60 ? 89 TRP B CZ2 1 ATOM 4001 C CZ3 . TRP B 1 89 ? 42.477 -60.930 -3.340 1.00 69.11 ? 89 TRP B CZ3 1 ATOM 4002 C CH2 . TRP B 1 89 ? 41.472 -59.970 -3.318 1.00 68.88 ? 89 TRP B CH2 1 ATOM 4003 N N . ASN B 1 90 ? 49.919 -59.022 -1.629 1.00 80.27 ? 90 ASN B N 1 ATOM 4004 C CA . ASN B 1 90 ? 51.118 -59.728 -1.176 1.00 85.92 ? 90 ASN B CA 1 ATOM 4005 C C . ASN B 1 90 ? 51.798 -59.033 0.018 1.00 92.85 ? 90 ASN B C 1 ATOM 4006 O O . ASN B 1 90 ? 52.932 -59.373 0.366 1.00 98.70 ? 90 ASN B O 1 ATOM 4007 C CB . ASN B 1 90 ? 52.127 -59.917 -2.305 1.00 79.60 ? 90 ASN B CB 1 ATOM 4008 C CG . ASN B 1 90 ? 53.084 -58.754 -2.414 1.00 81.76 ? 90 ASN B CG 1 ATOM 4009 O OD1 . ASN B 1 90 ? 52.667 -57.598 -2.408 1.00 81.79 ? 90 ASN B OD1 1 ATOM 4010 N ND2 . ASN B 1 90 ? 54.374 -59.049 -2.501 1.00 85.14 ? 90 ASN B ND2 1 ATOM 4011 N N . LEU B 1 91 ? 51.140 -58.041 0.613 1.00 91.05 ? 91 LEU B N 1 ATOM 4012 C CA . LEU B 1 91 ? 51.618 -57.495 1.874 1.00 92.53 ? 91 LEU B CA 1 ATOM 4013 C C . LEU B 1 91 ? 51.526 -58.557 2.957 1.00 94.18 ? 91 LEU B C 1 ATOM 4014 O O . LEU B 1 91 ? 52.394 -58.627 3.835 1.00 101.85 ? 91 LEU B O 1 ATOM 4015 C CB . LEU B 1 91 ? 50.833 -56.256 2.290 1.00 92.31 ? 91 LEU B CB 1 ATOM 4016 C CG . LEU B 1 91 ? 51.193 -54.967 1.549 1.00 95.87 ? 91 LEU B CG 1 ATOM 4017 C CD1 . LEU B 1 91 ? 50.174 -53.881 1.847 1.00 94.99 ? 91 LEU B CD1 1 ATOM 4018 C CD2 . LEU B 1 91 ? 52.599 -54.474 1.876 1.00 97.68 ? 91 LEU B CD2 1 ATOM 4019 N N . ILE B 1 92 ? 50.496 -59.389 2.871 1.00 87.05 ? 92 ILE B N 1 ATOM 4020 C CA . ILE B 1 92 ? 50.198 -60.382 3.896 1.00 86.54 ? 92 ILE B CA 1 ATOM 4021 C C . ILE B 1 92 ? 49.941 -61.764 3.321 1.00 85.51 ? 92 ILE B C 1 ATOM 4022 O O . ILE B 1 92 ? 49.362 -62.610 3.998 1.00 89.03 ? 92 ILE B O 1 ATOM 4023 C CB . ILE B 1 92 ? 48.945 -59.979 4.690 1.00 88.07 ? 92 ILE B CB 1 ATOM 4024 C CG1 . ILE B 1 92 ? 47.738 -59.832 3.740 1.00 85.97 ? 92 ILE B CG1 1 ATOM 4025 C CG2 . ILE B 1 92 ? 49.219 -58.707 5.473 1.00 87.74 ? 92 ILE B CG2 1 ATOM 4026 C CD1 . ILE B 1 92 ? 46.409 -59.608 4.428 1.00 87.05 ? 92 ILE B CD1 1 ATOM 4027 N N . ALA B 1 93 ? 50.356 -62.007 2.082 1.00 83.24 ? 93 ALA B N 1 ATOM 4028 C CA . ALA B 1 93 ? 50.119 -63.302 1.476 1.00 80.81 ? 93 ALA B CA 1 ATOM 4029 C C . ALA B 1 93 ? 51.102 -63.603 0.366 1.00 82.28 ? 93 ALA B C 1 ATOM 4030 O O . ALA B 1 93 ? 51.674 -62.700 -0.231 1.00 79.42 ? 93 ALA B O 1 ATOM 4031 C CB . ALA B 1 93 ? 48.701 -63.366 0.948 1.00 79.09 ? 93 ALA B CB 1 ATOM 4032 N N . ASN B 1 94 ? 51.293 -64.889 0.100 1.00 83.61 ? 94 ASN B N 1 ATOM 4033 C CA . ASN B 1 94 ? 52.038 -65.325 -1.066 1.00 86.60 ? 94 ASN B CA 1 ATOM 4034 C C . ASN B 1 94 ? 51.028 -65.538 -2.176 1.00 86.93 ? 94 ASN B C 1 ATOM 4035 O O . ASN B 1 94 ? 50.234 -66.482 -2.126 1.00 87.22 ? 94 ASN B O 1 ATOM 4036 C CB . ASN B 1 94 ? 52.806 -66.614 -0.768 1.00 89.65 ? 94 ASN B CB 1 ATOM 4037 C CG . ASN B 1 94 ? 53.655 -66.512 0.494 1.00 92.10 ? 94 ASN B CG 1 ATOM 4038 O OD1 . ASN B 1 94 ? 54.578 -65.706 0.559 1.00 92.48 ? 94 ASN B OD1 1 ATOM 4039 N ND2 . ASN B 1 94 ? 53.346 -67.327 1.498 1.00 92.27 ? 94 ASN B ND2 1 ATOM 4040 N N . VAL B 1 95 ? 51.038 -64.639 -3.155 1.00 85.13 ? 95 VAL B N 1 ATOM 4041 C CA . VAL B 1 95 ? 49.991 -64.592 -4.168 1.00 83.89 ? 95 VAL B CA 1 ATOM 4042 C C . VAL B 1 95 ? 50.523 -65.227 -5.448 1.00 81.85 ? 95 VAL B C 1 ATOM 4043 O O . VAL B 1 95 ? 51.559 -64.804 -5.957 1.00 83.48 ? 95 VAL B O 1 ATOM 4044 C CB . VAL B 1 95 ? 49.541 -63.142 -4.467 1.00 84.07 ? 95 VAL B CB 1 ATOM 4045 C CG1 . VAL B 1 95 ? 48.155 -63.133 -5.090 1.00 84.62 ? 95 VAL B CG1 1 ATOM 4046 C CG2 . VAL B 1 95 ? 49.541 -62.285 -3.211 1.00 83.31 ? 95 VAL B CG2 1 ATOM 4047 N N . LEU B 1 96 ? 49.830 -66.249 -5.942 1.00 77.18 ? 96 LEU B N 1 ATOM 4048 C CA . LEU B 1 96 ? 50.214 -66.946 -7.175 1.00 79.62 ? 96 LEU B CA 1 ATOM 4049 C C . LEU B 1 96 ? 49.286 -66.557 -8.326 1.00 80.48 ? 96 LEU B C 1 ATOM 4050 O O . LEU B 1 96 ? 48.178 -67.073 -8.423 1.00 84.24 ? 96 LEU B O 1 ATOM 4051 C CB . LEU B 1 96 ? 50.183 -68.473 -6.969 1.00 78.02 ? 96 LEU B CB 1 ATOM 4052 C CG . LEU B 1 96 ? 50.603 -69.371 -8.148 1.00 76.61 ? 96 LEU B CG 1 ATOM 4053 C CD1 . LEU B 1 96 ? 52.024 -69.083 -8.629 1.00 78.62 ? 96 LEU B CD1 1 ATOM 4054 C CD2 . LEU B 1 96 ? 50.472 -70.838 -7.788 1.00 75.91 ? 96 LEU B CD2 1 ATOM 4055 N N . TYR B 1 97 ? 49.739 -65.643 -9.185 1.00 79.28 ? 97 TYR B N 1 ATOM 4056 C CA . TYR B 1 97 ? 48.954 -65.179 -10.339 1.00 73.82 ? 97 TYR B CA 1 ATOM 4057 C C . TYR B 1 97 ? 49.164 -66.143 -11.488 1.00 75.05 ? 97 TYR B C 1 ATOM 4058 O O . TYR B 1 97 ? 50.273 -66.244 -11.996 1.00 81.28 ? 97 TYR B O 1 ATOM 4059 C CB . TYR B 1 97 ? 49.380 -63.765 -10.761 1.00 72.45 ? 97 TYR B CB 1 ATOM 4060 C CG . TYR B 1 97 ? 49.098 -62.717 -9.706 1.00 71.28 ? 97 TYR B CG 1 ATOM 4061 C CD1 . TYR B 1 97 ? 49.989 -62.493 -8.678 1.00 72.79 ? 97 TYR B CD1 1 ATOM 4062 C CD2 . TYR B 1 97 ? 47.938 -61.959 -9.734 1.00 69.08 ? 97 TYR B CD2 1 ATOM 4063 C CE1 . TYR B 1 97 ? 49.735 -61.551 -7.704 1.00 73.52 ? 97 TYR B CE1 1 ATOM 4064 C CE2 . TYR B 1 97 ? 47.679 -61.012 -8.763 1.00 67.45 ? 97 TYR B CE2 1 ATOM 4065 C CZ . TYR B 1 97 ? 48.581 -60.822 -7.744 1.00 69.01 ? 97 TYR B CZ 1 ATOM 4066 O OH . TYR B 1 97 ? 48.370 -59.903 -6.751 1.00 71.09 ? 97 TYR B OH 1 ATOM 4067 N N . LEU B 1 98 ? 48.115 -66.843 -11.902 1.00 73.88 ? 98 LEU B N 1 ATOM 4068 C CA . LEU B 1 98 ? 48.249 -67.907 -12.899 1.00 76.51 ? 98 LEU B CA 1 ATOM 4069 C C . LEU B 1 98 ? 47.525 -67.591 -14.208 1.00 79.53 ? 98 LEU B C 1 ATOM 4070 O O . LEU B 1 98 ? 46.297 -67.450 -14.216 1.00 79.10 ? 98 LEU B O 1 ATOM 4071 C CB . LEU B 1 98 ? 47.704 -69.217 -12.343 1.00 74.30 ? 98 LEU B CB 1 ATOM 4072 C CG . LEU B 1 98 ? 47.998 -70.445 -13.205 1.00 73.07 ? 98 LEU B CG 1 ATOM 4073 C CD1 . LEU B 1 98 ? 49.481 -70.705 -13.322 1.00 75.26 ? 98 LEU B CD1 1 ATOM 4074 C CD2 . LEU B 1 98 ? 47.309 -71.649 -12.605 1.00 75.42 ? 98 LEU B CD2 1 ATOM 4075 N N . GLU B 1 99 ? 48.275 -67.516 -15.313 1.00 75.72 ? 99 GLU B N 1 ATOM 4076 C CA . GLU B 1 99 ? 47.665 -67.287 -16.623 1.00 70.85 ? 99 GLU B CA 1 ATOM 4077 C C . GLU B 1 99 ? 47.081 -68.581 -17.166 1.00 69.43 ? 99 GLU B C 1 ATOM 4078 O O . GLU B 1 99 ? 47.797 -69.537 -17.437 1.00 70.04 ? 99 GLU B O 1 ATOM 4079 C CB . GLU B 1 99 ? 48.669 -66.725 -17.598 1.00 71.39 ? 99 GLU B CB 1 ATOM 4080 C CG . GLU B 1 99 ? 49.076 -65.314 -17.263 1.00 76.01 ? 99 GLU B CG 1 ATOM 4081 C CD . GLU B 1 99 ? 49.886 -64.669 -18.367 1.00 77.01 ? 99 GLU B CD 1 ATOM 4082 O OE1 . GLU B 1 99 ? 50.954 -65.222 -18.715 1.00 75.71 ? 99 GLU B OE1 1 ATOM 4083 O OE2 . GLU B 1 99 ? 49.446 -63.615 -18.876 1.00 74.06 ? 99 GLU B OE2 1 ATOM 4084 N N . SER B 1 100 ? 45.770 -68.608 -17.315 1.00 67.71 ? 100 SER B N 1 ATOM 4085 C CA . SER B 1 100 ? 45.075 -69.831 -17.640 1.00 66.40 ? 100 SER B CA 1 ATOM 4086 C C . SER B 1 100 ? 43.729 -69.510 -18.265 1.00 64.67 ? 100 SER B C 1 ATOM 4087 O O . SER B 1 100 ? 43.192 -68.429 -18.047 1.00 58.78 ? 100 SER B O 1 ATOM 4088 C CB . SER B 1 100 ? 44.908 -70.668 -16.365 1.00 68.57 ? 100 SER B CB 1 ATOM 4089 O OG . SER B 1 100 ? 43.657 -71.325 -16.316 1.00 68.91 ? 100 SER B OG 1 ATOM 4090 N N . PRO B 1 101 ? 43.179 -70.438 -19.064 1.00 70.20 ? 101 PRO B N 1 ATOM 4091 C CA . PRO B 1 101 ? 43.741 -71.726 -19.467 1.00 72.24 ? 101 PRO B CA 1 ATOM 4092 C C . PRO B 1 101 ? 44.803 -71.594 -20.554 1.00 74.47 ? 101 PRO B C 1 ATOM 4093 O O . PRO B 1 101 ? 45.146 -70.483 -20.948 1.00 79.34 ? 101 PRO B O 1 ATOM 4094 C CB . PRO B 1 101 ? 42.527 -72.459 -20.010 1.00 73.27 ? 101 PRO B CB 1 ATOM 4095 C CG . PRO B 1 101 ? 41.707 -71.371 -20.618 1.00 72.40 ? 101 PRO B CG 1 ATOM 4096 C CD . PRO B 1 101 ? 41.866 -70.205 -19.691 1.00 71.04 ? 101 PRO B CD 1 ATOM 4097 N N . ALA B 1 102 ? 45.327 -72.721 -21.015 1.00 78.41 ? 102 ALA B N 1 ATOM 4098 C CA . ALA B 1 102 ? 46.309 -72.753 -22.113 1.00 79.47 ? 102 ALA B CA 1 ATOM 4099 C C . ALA B 1 102 ? 45.971 -71.794 -23.247 1.00 78.47 ? 102 ALA B C 1 ATOM 4100 O O . ALA B 1 102 ? 44.899 -71.896 -23.843 1.00 77.04 ? 102 ALA B O 1 ATOM 4101 C CB . ALA B 1 102 ? 46.415 -74.154 -22.673 1.00 81.59 ? 102 ALA B CB 1 ATOM 4102 N N . GLY B 1 103 ? 46.894 -70.877 -23.530 1.00 78.09 ? 103 GLY B N 1 ATOM 4103 C CA . GLY B 1 103 ? 46.771 -69.956 -24.657 1.00 79.81 ? 103 GLY B CA 1 ATOM 4104 C C . GLY B 1 103 ? 46.605 -68.513 -24.222 1.00 80.23 ? 103 GLY B C 1 ATOM 4105 O O . GLY B 1 103 ? 46.908 -67.590 -24.977 1.00 78.00 ? 103 GLY B O 1 ATOM 4106 N N . VAL B 1 104 ? 46.108 -68.325 -23.004 1.00 78.61 ? 104 VAL B N 1 ATOM 4107 C CA . VAL B 1 104 ? 45.945 -67.009 -22.417 1.00 71.31 ? 104 VAL B CA 1 ATOM 4108 C C . VAL B 1 104 ? 47.305 -66.444 -22.040 1.00 70.03 ? 104 VAL B C 1 ATOM 4109 O O . VAL B 1 104 ? 48.146 -67.152 -21.484 1.00 75.78 ? 104 VAL B O 1 ATOM 4110 C CB . VAL B 1 104 ? 45.073 -67.081 -21.155 1.00 68.42 ? 104 VAL B CB 1 ATOM 4111 C CG1 . VAL B 1 104 ? 44.979 -65.723 -20.484 1.00 68.68 ? 104 VAL B CG1 1 ATOM 4112 C CG2 . VAL B 1 104 ? 43.684 -67.586 -21.509 1.00 68.64 ? 104 VAL B CG2 1 ATOM 4113 N N . GLY B 1 105 ? 47.507 -65.168 -22.336 1.00 66.79 ? 105 GLY B N 1 ATOM 4114 C CA . GLY B 1 105 ? 48.741 -64.474 -21.986 1.00 68.71 ? 105 GLY B CA 1 ATOM 4115 C C . GLY B 1 105 ? 49.995 -65.111 -22.551 1.00 68.61 ? 105 GLY B C 1 ATOM 4116 O O . GLY B 1 105 ? 50.127 -65.243 -23.754 1.00 67.34 ? 105 GLY B O 1 ATOM 4117 N N . PHE B 1 106 ? 50.912 -65.497 -21.669 1.00 71.70 ? 106 PHE B N 1 ATOM 4118 C CA . PHE B 1 106 ? 52.133 -66.200 -22.048 1.00 73.54 ? 106 PHE B CA 1 ATOM 4119 C C . PHE B 1 106 ? 51.997 -67.718 -21.921 1.00 77.06 ? 106 PHE B C 1 ATOM 4120 O O . PHE B 1 106 ? 52.947 -68.458 -22.182 1.00 81.48 ? 106 PHE B O 1 ATOM 4121 C CB . PHE B 1 106 ? 53.309 -65.724 -21.187 1.00 71.38 ? 106 PHE B CB 1 ATOM 4122 C CG . PHE B 1 106 ? 53.725 -64.306 -21.454 1.00 71.53 ? 106 PHE B CG 1 ATOM 4123 C CD1 . PHE B 1 106 ? 53.962 -63.861 -22.766 1.00 73.88 ? 106 PHE B CD1 1 ATOM 4124 C CD2 . PHE B 1 106 ? 53.917 -63.421 -20.415 1.00 69.21 ? 106 PHE B CD2 1 ATOM 4125 C CE1 . PHE B 1 106 ? 54.360 -62.560 -23.027 1.00 69.57 ? 106 PHE B CE1 1 ATOM 4126 C CE2 . PHE B 1 106 ? 54.318 -62.118 -20.669 1.00 69.68 ? 106 PHE B CE2 1 ATOM 4127 C CZ . PHE B 1 106 ? 54.539 -61.687 -21.977 1.00 69.65 ? 106 PHE B CZ 1 ATOM 4128 N N . SER B 1 107 ? 50.825 -68.192 -21.522 1.00 78.90 ? 107 SER B N 1 ATOM 4129 C CA . SER B 1 107 ? 50.600 -69.626 -21.419 1.00 82.23 ? 107 SER B CA 1 ATOM 4130 C C . SER B 1 107 ? 50.354 -70.209 -22.807 1.00 81.07 ? 107 SER B C 1 ATOM 4131 O O . SER B 1 107 ? 49.721 -69.577 -23.652 1.00 82.62 ? 107 SER B O 1 ATOM 4132 C CB . SER B 1 107 ? 49.415 -69.926 -20.497 1.00 81.29 ? 107 SER B CB 1 ATOM 4133 O OG . SER B 1 107 ? 49.671 -69.470 -19.182 1.00 77.55 ? 107 SER B OG 1 ATOM 4134 N N . TYR B 1 108 ? 50.843 -71.419 -23.024 1.00 82.76 ? 108 TYR B N 1 ATOM 4135 C CA . TYR B 1 108 ? 50.701 -72.099 -24.308 1.00 85.37 ? 108 TYR B CA 1 ATOM 4136 C C . TYR B 1 108 ? 50.573 -73.601 -24.130 1.00 87.22 ? 108 TYR B C 1 ATOM 4137 O O . TYR B 1 108 ? 50.626 -74.121 -23.010 1.00 86.22 ? 108 TYR B O 1 ATOM 4138 C CB . TYR B 1 108 ? 51.916 -71.815 -25.175 1.00 87.10 ? 108 TYR B CB 1 ATOM 4139 C CG . TYR B 1 108 ? 53.195 -72.404 -24.619 1.00 91.70 ? 108 TYR B CG 1 ATOM 4140 C CD1 . TYR B 1 108 ? 53.863 -71.792 -23.567 1.00 96.76 ? 108 TYR B CD1 1 ATOM 4141 C CD2 . TYR B 1 108 ? 53.739 -73.570 -25.144 1.00 94.73 ? 108 TYR B CD2 1 ATOM 4142 C CE1 . TYR B 1 108 ? 55.032 -72.322 -23.051 1.00 99.68 ? 108 TYR B CE1 1 ATOM 4143 C CE2 . TYR B 1 108 ? 54.913 -74.106 -24.634 1.00 96.15 ? 108 TYR B CE2 1 ATOM 4144 C CZ . TYR B 1 108 ? 55.553 -73.478 -23.585 1.00 98.40 ? 108 TYR B CZ 1 ATOM 4145 O OH . TYR B 1 108 ? 56.724 -73.976 -23.062 1.00 100.10 ? 108 TYR B OH 1 ATOM 4146 N N . SER B 1 109 ? 50.402 -74.288 -25.252 1.00 90.21 ? 109 SER B N 1 ATOM 4147 C CA . SER B 1 109 ? 50.561 -75.736 -25.314 1.00 97.26 ? 109 SER B CA 1 ATOM 4148 C C . SER B 1 109 ? 51.394 -76.080 -26.537 1.00 96.68 ? 109 SER B C 1 ATOM 4149 O O . SER B 1 109 ? 51.416 -75.326 -27.500 1.00 97.40 ? 109 SER B O 1 ATOM 4150 C CB . SER B 1 109 ? 49.205 -76.424 -25.407 1.00 97.55 ? 109 SER B CB 1 ATOM 4151 O OG . SER B 1 109 ? 48.622 -76.189 -26.673 1.00 95.70 ? 109 SER B OG 1 ATOM 4152 N N . ASP B 1 110 ? 52.060 -77.224 -26.504 1.00 99.98 ? 110 ASP B N 1 ATOM 4153 C CA . ASP B 1 110 ? 52.878 -77.667 -27.634 1.00 101.50 ? 110 ASP B CA 1 ATOM 4154 C C . ASP B 1 110 ? 52.072 -77.796 -28.919 1.00 98.45 ? 110 ASP B C 1 ATOM 4155 O O . ASP B 1 110 ? 52.519 -77.368 -29.979 1.00 95.86 ? 110 ASP B O 1 ATOM 4156 C CB . ASP B 1 110 ? 53.550 -79.007 -27.326 1.00 105.34 ? 110 ASP B CB 1 ATOM 4157 C CG . ASP B 1 110 ? 54.619 -78.898 -26.256 1.00 105.10 ? 110 ASP B CG 1 ATOM 4158 O OD1 . ASP B 1 110 ? 55.039 -77.767 -25.931 1.00 96.99 ? 110 ASP B OD1 1 ATOM 4159 O OD2 . ASP B 1 110 ? 55.033 -79.959 -25.747 1.00 109.00 ? 110 ASP B OD2 1 ATOM 4160 N N . ASP B 1 111 ? 50.885 -78.377 -28.819 1.00 97.01 ? 111 ASP B N 1 ATOM 4161 C CA . ASP B 1 111 ? 50.032 -78.563 -29.989 1.00 99.81 ? 111 ASP B CA 1 ATOM 4162 C C . ASP B 1 111 ? 49.222 -77.318 -30.358 1.00 100.09 ? 111 ASP B C 1 ATOM 4163 O O . ASP B 1 111 ? 48.593 -77.289 -31.403 1.00 102.49 ? 111 ASP B O 1 ATOM 4164 C CB . ASP B 1 111 ? 49.102 -79.769 -29.800 1.00 99.84 ? 111 ASP B CB 1 ATOM 4165 C CG . ASP B 1 111 ? 48.136 -79.604 -28.641 1.00 97.94 ? 111 ASP B CG 1 ATOM 4166 O OD1 . ASP B 1 111 ? 48.475 -78.919 -27.649 1.00 98.87 ? 111 ASP B OD1 1 ATOM 4167 O OD2 . ASP B 1 111 ? 47.038 -80.180 -28.722 1.00 97.70 ? 111 ASP B OD2 1 ATOM 4168 N N . LYS B 1 112 ? 49.226 -76.299 -29.511 1.00 103.31 ? 112 LYS B N 1 ATOM 4169 C CA . LYS B 1 112 ? 48.511 -75.044 -29.781 1.00 106.83 ? 112 LYS B CA 1 ATOM 4170 C C . LYS B 1 112 ? 46.997 -75.169 -29.989 1.00 105.47 ? 112 LYS B C 1 ATOM 4171 O O . LYS B 1 112 ? 46.380 -74.244 -30.515 1.00 110.47 ? 112 LYS B O 1 ATOM 4172 C CB . LYS B 1 112 ? 49.103 -74.304 -30.993 1.00 112.57 ? 112 LYS B CB 1 ATOM 4173 C CG . LYS B 1 112 ? 50.594 -73.994 -30.926 1.00 117.36 ? 112 LYS B CG 1 ATOM 4174 C CD . LYS B 1 112 ? 50.894 -72.547 -31.310 1.00 118.79 ? 112 LYS B CD 1 ATOM 4175 C CE . LYS B 1 112 ? 50.447 -72.175 -32.721 1.00 119.86 ? 112 LYS B CE 1 ATOM 4176 N NZ . LYS B 1 112 ? 51.489 -72.456 -33.738 1.00 121.67 ? 112 LYS B NZ 1 ATOM 4177 N N . PHE B 1 113 ? 46.389 -76.276 -29.576 1.00 104.85 ? 113 PHE B N 1 ATOM 4178 C CA . PHE B 1 113 ? 44.935 -76.397 -29.645 1.00 105.77 ? 113 PHE B CA 1 ATOM 4179 C C . PHE B 1 113 ? 44.363 -75.810 -28.365 1.00 101.07 ? 113 PHE B C 1 ATOM 4180 O O . PHE B 1 113 ? 44.547 -76.368 -27.288 1.00 103.84 ? 113 PHE B O 1 ATOM 4181 C CB . PHE B 1 113 ? 44.503 -77.853 -29.817 1.00 111.49 ? 113 PHE B CB 1 ATOM 4182 C CG . PHE B 1 113 ? 43.025 -78.027 -30.082 1.00 123.60 ? 113 PHE B CG 1 ATOM 4183 C CD1 . PHE B 1 113 ? 42.419 -77.428 -31.194 1.00 130.37 ? 113 PHE B CD1 1 ATOM 4184 C CD2 . PHE B 1 113 ? 42.238 -78.810 -29.241 1.00 126.56 ? 113 PHE B CD2 1 ATOM 4185 C CE1 . PHE B 1 113 ? 41.063 -77.593 -31.448 1.00 132.96 ? 113 PHE B CE1 1 ATOM 4186 C CE2 . PHE B 1 113 ? 40.882 -78.982 -29.496 1.00 131.34 ? 113 PHE B CE2 1 ATOM 4187 C CZ . PHE B 1 113 ? 40.296 -78.374 -30.600 1.00 134.70 ? 113 PHE B CZ 1 ATOM 4188 N N . TYR B 1 114 ? 43.682 -74.677 -28.477 1.00 94.82 ? 114 TYR B N 1 ATOM 4189 C CA . TYR B 1 114 ? 43.267 -73.930 -27.291 1.00 82.78 ? 114 TYR B CA 1 ATOM 4190 C C . TYR B 1 114 ? 41.782 -73.946 -27.022 1.00 78.34 ? 114 TYR B C 1 ATOM 4191 O O . TYR B 1 114 ? 41.332 -73.338 -26.060 1.00 77.04 ? 114 TYR B O 1 ATOM 4192 C CB . TYR B 1 114 ? 43.763 -72.493 -27.393 1.00 79.46 ? 114 TYR B CB 1 ATOM 4193 C CG . TYR B 1 114 ? 45.278 -72.361 -27.389 1.00 78.80 ? 114 TYR B CG 1 ATOM 4194 C CD1 . TYR B 1 114 ? 46.057 -73.030 -26.449 1.00 73.97 ? 114 TYR B CD1 1 ATOM 4195 C CD2 . TYR B 1 114 ? 45.931 -71.541 -28.313 1.00 77.47 ? 114 TYR B CD2 1 ATOM 4196 C CE1 . TYR B 1 114 ? 47.431 -72.894 -26.430 1.00 73.30 ? 114 TYR B CE1 1 ATOM 4197 C CE2 . TYR B 1 114 ? 47.311 -71.400 -28.289 1.00 75.27 ? 114 TYR B CE2 1 ATOM 4198 C CZ . TYR B 1 114 ? 48.054 -72.080 -27.344 1.00 71.62 ? 114 TYR B CZ 1 ATOM 4199 O OH . TYR B 1 114 ? 49.418 -71.949 -27.309 1.00 68.71 ? 114 TYR B OH 1 ATOM 4200 N N . ALA B 1 115 ? 41.015 -74.645 -27.851 1.00 81.42 ? 115 ALA B N 1 ATOM 4201 C CA . ALA B 1 115 ? 39.613 -74.907 -27.523 1.00 81.91 ? 115 ALA B CA 1 ATOM 4202 C C . ALA B 1 115 ? 39.611 -75.754 -26.270 1.00 79.24 ? 115 ALA B C 1 ATOM 4203 O O . ALA B 1 115 ? 40.379 -76.707 -26.161 1.00 76.62 ? 115 ALA B O 1 ATOM 4204 C CB . ALA B 1 115 ? 38.901 -75.633 -28.645 1.00 82.53 ? 115 ALA B CB 1 ATOM 4205 N N . THR B 1 116 ? 38.767 -75.393 -25.316 1.00 78.27 ? 116 THR B N 1 ATOM 4206 C CA . THR B 1 116 ? 38.736 -76.084 -24.032 1.00 76.67 ? 116 THR B CA 1 ATOM 4207 C C . THR B 1 116 ? 37.364 -75.889 -23.393 1.00 73.70 ? 116 THR B C 1 ATOM 4208 O O . THR B 1 116 ? 36.459 -75.331 -24.019 1.00 67.18 ? 116 THR B O 1 ATOM 4209 C CB . THR B 1 116 ? 39.906 -75.622 -23.119 1.00 75.26 ? 116 THR B CB 1 ATOM 4210 O OG1 . THR B 1 116 ? 40.044 -76.496 -21.995 1.00 76.18 ? 116 THR B OG1 1 ATOM 4211 C CG2 . THR B 1 116 ? 39.715 -74.201 -22.633 1.00 71.14 ? 116 THR B CG2 1 ATOM 4212 N N . ASN B 1 117 ? 37.207 -76.378 -22.169 1.00 75.27 ? 117 ASN B N 1 ATOM 4213 C CA . ASN B 1 117 ? 35.939 -76.285 -21.464 1.00 79.06 ? 117 ASN B CA 1 ATOM 4214 C C . ASN B 1 117 ? 36.118 -76.376 -19.949 1.00 79.86 ? 117 ASN B C 1 ATOM 4215 O O . ASN B 1 117 ? 37.189 -76.729 -19.471 1.00 82.32 ? 117 ASN B O 1 ATOM 4216 C CB . ASN B 1 117 ? 34.981 -77.358 -21.972 1.00 84.25 ? 117 ASN B CB 1 ATOM 4217 C CG . ASN B 1 117 ? 35.406 -78.762 -21.594 1.00 89.75 ? 117 ASN B CG 1 ATOM 4218 O OD1 . ASN B 1 117 ? 35.837 -79.007 -20.462 1.00 95.81 ? 117 ASN B OD1 1 ATOM 4219 N ND2 . ASN B 1 117 ? 35.262 -79.703 -22.542 1.00 92.20 ? 117 ASN B ND2 1 ATOM 4220 N N . ASP B 1 118 ? 35.057 -76.068 -19.206 1.00 80.58 ? 118 ASP B N 1 ATOM 4221 C CA . ASP B 1 118 ? 35.124 -75.916 -17.746 1.00 75.71 ? 118 ASP B CA 1 ATOM 4222 C C . ASP B 1 118 ? 35.792 -77.097 -17.031 1.00 77.81 ? 118 ASP B C 1 ATOM 4223 O O . ASP B 1 118 ? 36.642 -76.892 -16.161 1.00 75.64 ? 118 ASP B O 1 ATOM 4224 C CB . ASP B 1 118 ? 33.724 -75.706 -17.172 1.00 72.43 ? 118 ASP B CB 1 ATOM 4225 C CG . ASP B 1 118 ? 33.066 -74.424 -17.651 1.00 68.11 ? 118 ASP B CG 1 ATOM 4226 O OD1 . ASP B 1 118 ? 33.747 -73.392 -17.805 1.00 61.47 ? 118 ASP B OD1 1 ATOM 4227 O OD2 . ASP B 1 118 ? 31.843 -74.453 -17.830 1.00 68.55 ? 118 ASP B OD2 1 ATOM 4228 N N . THR B 1 119 ? 35.417 -78.322 -17.409 1.00 79.79 ? 119 THR B N 1 ATOM 4229 C CA . THR B 1 119 ? 35.963 -79.524 -16.771 1.00 82.51 ? 119 THR B CA 1 ATOM 4230 C C . THR B 1 119 ? 37.437 -79.690 -17.095 1.00 80.19 ? 119 THR B C 1 ATOM 4231 O O . THR B 1 119 ? 38.218 -80.076 -16.223 1.00 83.31 ? 119 THR B O 1 ATOM 4232 C CB . THR B 1 119 ? 35.208 -80.817 -17.154 1.00 86.62 ? 119 THR B CB 1 ATOM 4233 O OG1 . THR B 1 119 ? 35.042 -80.897 -18.573 1.00 94.04 ? 119 THR B OG1 1 ATOM 4234 C CG2 . THR B 1 119 ? 33.840 -80.869 -16.488 1.00 86.97 ? 119 THR B CG2 1 ATOM 4235 N N . GLU B 1 120 ? 37.822 -79.378 -18.333 1.00 77.02 ? 120 GLU B N 1 ATOM 4236 C CA . GLU B 1 120 ? 39.216 -79.509 -18.733 1.00 75.62 ? 120 GLU B CA 1 ATOM 4237 C C . GLU B 1 120 ? 40.075 -78.445 -18.080 1.00 75.09 ? 120 GLU B C 1 ATOM 4238 O O . GLU B 1 120 ? 41.190 -78.734 -17.638 1.00 72.73 ? 120 GLU B O 1 ATOM 4239 C CB . GLU B 1 120 ? 39.394 -79.448 -20.240 1.00 75.02 ? 120 GLU B CB 1 ATOM 4240 C CG . GLU B 1 120 ? 40.800 -79.854 -20.649 1.00 79.95 ? 120 GLU B CG 1 ATOM 4241 C CD . GLU B 1 120 ? 41.027 -79.894 -22.149 1.00 84.06 ? 120 GLU B CD 1 ATOM 4242 O OE1 . GLU B 1 120 ? 40.412 -79.075 -22.879 1.00 83.23 ? 120 GLU B OE1 1 ATOM 4243 O OE2 . GLU B 1 120 ? 41.827 -80.755 -22.593 1.00 85.07 ? 120 GLU B OE2 1 ATOM 4244 N N . VAL B 1 121 ? 39.565 -77.219 -18.013 1.00 73.61 ? 121 VAL B N 1 ATOM 4245 C CA . VAL B 1 121 ? 40.315 -76.137 -17.401 1.00 71.15 ? 121 VAL B CA 1 ATOM 4246 C C . VAL B 1 121 ? 40.502 -76.398 -15.914 1.00 73.41 ? 121 VAL B C 1 ATOM 4247 O O . VAL B 1 121 ? 41.570 -76.141 -15.364 1.00 72.90 ? 121 VAL B O 1 ATOM 4248 C CB . VAL B 1 121 ? 39.629 -74.795 -17.593 1.00 71.96 ? 121 VAL B CB 1 ATOM 4249 C CG1 . VAL B 1 121 ? 40.347 -73.720 -16.795 1.00 73.67 ? 121 VAL B CG1 1 ATOM 4250 C CG2 . VAL B 1 121 ? 39.613 -74.430 -19.064 1.00 73.74 ? 121 VAL B CG2 1 ATOM 4251 N N . ALA B 1 122 ? 39.460 -76.909 -15.268 1.00 73.88 ? 122 ALA B N 1 ATOM 4252 C CA . ALA B 1 122 ? 39.528 -77.223 -13.852 1.00 77.57 ? 122 ALA B CA 1 ATOM 4253 C C . ALA B 1 122 ? 40.673 -78.187 -13.616 1.00 80.85 ? 122 ALA B C 1 ATOM 4254 O O . ALA B 1 122 ? 41.552 -77.942 -12.784 1.00 80.95 ? 122 ALA B O 1 ATOM 4255 C CB . ALA B 1 122 ? 38.211 -77.826 -13.374 1.00 78.73 ? 122 ALA B CB 1 ATOM 4256 N N . GLN B 1 123 ? 40.649 -79.283 -14.363 1.00 88.61 ? 123 GLN B N 1 ATOM 4257 C CA . GLN B 1 123 ? 41.675 -80.310 -14.275 1.00 93.77 ? 123 GLN B CA 1 ATOM 4258 C C . GLN B 1 123 ? 43.071 -79.748 -14.564 1.00 96.49 ? 123 GLN B C 1 ATOM 4259 O O . GLN B 1 123 ? 44.047 -80.116 -13.924 1.00 100.12 ? 123 GLN B O 1 ATOM 4260 C CB . GLN B 1 123 ? 41.364 -81.426 -15.265 1.00 93.19 ? 123 GLN B CB 1 ATOM 4261 C CG . GLN B 1 123 ? 42.328 -82.592 -15.202 1.00 95.22 ? 123 GLN B CG 1 ATOM 4262 C CD . GLN B 1 123 ? 42.312 -83.265 -13.851 1.00 97.53 ? 123 GLN B CD 1 ATOM 4263 O OE1 . GLN B 1 123 ? 41.252 -83.410 -13.239 1.00 101.72 ? 123 GLN B OE1 1 ATOM 4264 N NE2 . GLN B 1 123 ? 43.484 -83.681 -13.376 1.00 94.38 ? 123 GLN B NE2 1 ATOM 4265 N N . SER B 1 124 ? 43.151 -78.862 -15.543 1.00 95.48 ? 124 SER B N 1 ATOM 4266 C CA . SER B 1 124 ? 44.406 -78.259 -15.945 1.00 90.62 ? 124 SER B CA 1 ATOM 4267 C C . SER B 1 124 ? 44.991 -77.434 -14.805 1.00 87.78 ? 124 SER B C 1 ATOM 4268 O O . SER B 1 124 ? 46.181 -77.538 -14.512 1.00 87.84 ? 124 SER B O 1 ATOM 4269 C CB . SER B 1 124 ? 44.172 -77.383 -17.181 1.00 90.99 ? 124 SER B CB 1 ATOM 4270 O OG . SER B 1 124 ? 45.380 -76.917 -17.715 1.00 91.61 ? 124 SER B OG 1 ATOM 4271 N N . ASN B 1 125 ? 44.156 -76.602 -14.179 1.00 86.44 ? 125 ASN B N 1 ATOM 4272 C CA . ASN B 1 125 ? 44.574 -75.781 -13.034 1.00 84.58 ? 125 ASN B CA 1 ATOM 4273 C C . ASN B 1 125 ? 44.989 -76.633 -11.858 1.00 85.50 ? 125 ASN B C 1 ATOM 4274 O O . ASN B 1 125 ? 45.983 -76.349 -11.175 1.00 81.69 ? 125 ASN B O 1 ATOM 4275 C CB . ASN B 1 125 ? 43.440 -74.887 -12.565 1.00 85.11 ? 125 ASN B CB 1 ATOM 4276 C CG . ASN B 1 125 ? 43.149 -73.763 -13.518 1.00 84.87 ? 125 ASN B CG 1 ATOM 4277 O OD1 . ASN B 1 125 ? 41.987 -73.451 -13.780 1.00 91.23 ? 125 ASN B OD1 1 ATOM 4278 N ND2 . ASN B 1 125 ? 44.190 -73.122 -14.015 1.00 82.95 ? 125 ASN B ND2 1 ATOM 4279 N N . PHE B 1 126 ? 44.193 -77.663 -11.603 1.00 84.18 ? 126 PHE B N 1 ATOM 4280 C CA . PHE B 1 126 ? 44.486 -78.581 -10.532 1.00 85.32 ? 126 PHE B CA 1 ATOM 4281 C C . PHE B 1 126 ? 45.868 -79.179 -10.709 1.00 88.67 ? 126 PHE B C 1 ATOM 4282 O O . PHE B 1 126 ? 46.646 -79.227 -9.747 1.00 94.86 ? 126 PHE B O 1 ATOM 4283 C CB . PHE B 1 126 ? 43.459 -79.697 -10.463 1.00 84.97 ? 126 PHE B CB 1 ATOM 4284 C CG . PHE B 1 126 ? 43.813 -80.745 -9.472 1.00 87.11 ? 126 PHE B CG 1 ATOM 4285 C CD1 . PHE B 1 126 ? 43.937 -80.418 -8.124 1.00 91.55 ? 126 PHE B CD1 1 ATOM 4286 C CD2 . PHE B 1 126 ? 44.060 -82.039 -9.872 1.00 88.03 ? 126 PHE B CD2 1 ATOM 4287 C CE1 . PHE B 1 126 ? 44.277 -81.374 -7.187 1.00 94.84 ? 126 PHE B CE1 1 ATOM 4288 C CE2 . PHE B 1 126 ? 44.409 -83.001 -8.946 1.00 94.37 ? 126 PHE B CE2 1 ATOM 4289 C CZ . PHE B 1 126 ? 44.520 -82.671 -7.599 1.00 96.25 ? 126 PHE B CZ 1 ATOM 4290 N N . GLU B 1 127 ? 46.164 -79.644 -11.922 1.00 84.62 ? 127 GLU B N 1 ATOM 4291 C CA . GLU B 1 127 ? 47.448 -80.279 -12.198 1.00 87.38 ? 127 GLU B CA 1 ATOM 4292 C C . GLU B 1 127 ? 48.586 -79.274 -12.127 1.00 86.41 ? 127 GLU B C 1 ATOM 4293 O O . GLU B 1 127 ? 49.685 -79.604 -11.690 1.00 88.42 ? 127 GLU B O 1 ATOM 4294 C CB . GLU B 1 127 ? 47.434 -81.004 -13.554 1.00 88.41 ? 127 GLU B CB 1 ATOM 4295 C CG . GLU B 1 127 ? 46.581 -82.274 -13.578 1.00 88.79 ? 127 GLU B CG 1 ATOM 4296 C CD . GLU B 1 127 ? 46.910 -83.196 -14.745 1.00 91.56 ? 127 GLU B CD 1 ATOM 4297 O OE1 . GLU B 1 127 ? 48.112 -83.315 -15.066 1.00 90.55 ? 127 GLU B OE1 1 ATOM 4298 O OE2 . GLU B 1 127 ? 45.976 -83.784 -15.353 1.00 92.67 ? 127 GLU B OE2 1 ATOM 4299 N N . ALA B 1 128 ? 48.323 -78.053 -12.557 1.00 84.10 ? 128 ALA B N 1 ATOM 4300 C CA . ALA B 1 128 ? 49.296 -76.966 -12.435 1.00 86.14 ? 128 ALA B CA 1 ATOM 4301 C C . ALA B 1 128 ? 49.585 -76.605 -10.982 1.00 83.92 ? 128 ALA B C 1 ATOM 4302 O O . ALA B 1 128 ? 50.712 -76.302 -10.617 1.00 79.20 ? 128 ALA B O 1 ATOM 4303 C CB . ALA B 1 128 ? 48.788 -75.751 -13.175 1.00 88.33 ? 128 ALA B CB 1 ATOM 4304 N N . LEU B 1 129 ? 48.547 -76.631 -10.157 1.00 88.67 ? 129 LEU B N 1 ATOM 4305 C CA . LEU B 1 129 ? 48.692 -76.410 -8.726 1.00 89.15 ? 129 LEU B CA 1 ATOM 4306 C C . LEU B 1 129 ? 49.527 -77.553 -8.135 1.00 96.50 ? 129 LEU B C 1 ATOM 4307 O O . LEU B 1 129 ? 50.427 -77.310 -7.334 1.00 103.80 ? 129 LEU B O 1 ATOM 4308 C CB . LEU B 1 129 ? 47.323 -76.322 -8.068 1.00 87.16 ? 129 LEU B CB 1 ATOM 4309 C CG . LEU B 1 129 ? 47.104 -75.411 -6.857 1.00 89.43 ? 129 LEU B CG 1 ATOM 4310 C CD1 . LEU B 1 129 ? 47.455 -73.956 -7.123 1.00 89.16 ? 129 LEU B CD1 1 ATOM 4311 C CD2 . LEU B 1 129 ? 45.648 -75.503 -6.456 1.00 90.02 ? 129 LEU B CD2 1 ATOM 4312 N N . GLN B 1 130 ? 49.258 -78.788 -8.557 1.00 96.44 ? 130 GLN B N 1 ATOM 4313 C CA . GLN B 1 130 ? 50.127 -79.919 -8.213 1.00 95.65 ? 130 GLN B CA 1 ATOM 4314 C C . GLN B 1 130 ? 51.577 -79.653 -8.616 1.00 96.08 ? 130 GLN B C 1 ATOM 4315 O O . GLN B 1 130 ? 52.476 -79.724 -7.782 1.00 103.07 ? 130 GLN B O 1 ATOM 4316 C CB . GLN B 1 130 ? 49.641 -81.216 -8.865 1.00 94.87 ? 130 GLN B CB 1 ATOM 4317 C CG . GLN B 1 130 ? 48.396 -81.786 -8.212 1.00 95.50 ? 130 GLN B CG 1 ATOM 4318 C CD . GLN B 1 130 ? 48.132 -83.237 -8.570 1.00 97.92 ? 130 GLN B CD 1 ATOM 4319 O OE1 . GLN B 1 130 ? 48.254 -83.636 -9.724 1.00 101.71 ? 130 GLN B OE1 1 ATOM 4320 N NE2 . GLN B 1 130 ? 47.764 -84.032 -7.577 1.00 100.03 ? 130 GLN B NE2 1 ATOM 4321 N N . ASP B 1 131 ? 51.803 -79.324 -9.884 1.00 95.24 ? 131 ASP B N 1 ATOM 4322 C CA . ASP B 1 131 ? 53.157 -79.039 -10.370 1.00 96.32 ? 131 ASP B CA 1 ATOM 4323 C C . ASP B 1 131 ? 53.805 -77.915 -9.576 1.00 94.08 ? 131 ASP B C 1 ATOM 4324 O O . ASP B 1 131 ? 55.018 -77.856 -9.475 1.00 96.78 ? 131 ASP B O 1 ATOM 4325 C CB . ASP B 1 131 ? 53.152 -78.691 -11.874 1.00 97.72 ? 131 ASP B CB 1 ATOM 4326 C CG . ASP B 1 131 ? 54.553 -78.751 -12.512 1.00 105.08 ? 131 ASP B CG 1 ATOM 4327 O OD1 . ASP B 1 131 ? 55.282 -79.741 -12.293 1.00 107.98 ? 131 ASP B OD1 1 ATOM 4328 O OD2 . ASP B 1 131 ? 54.924 -77.817 -13.258 1.00 107.25 ? 131 ASP B OD2 1 ATOM 4329 N N . PHE B 1 132 ? 52.996 -77.005 -9.043 1.00 95.86 ? 132 PHE B N 1 ATOM 4330 C CA . PHE B 1 132 ? 53.514 -75.880 -8.272 1.00 92.60 ? 132 PHE B CA 1 ATOM 4331 C C . PHE B 1 132 ? 54.230 -76.369 -7.042 1.00 96.73 ? 132 PHE B C 1 ATOM 4332 O O . PHE B 1 132 ? 55.339 -75.939 -6.748 1.00 95.49 ? 132 PHE B O 1 ATOM 4333 C CB . PHE B 1 132 ? 52.392 -74.940 -7.846 1.00 87.08 ? 132 PHE B CB 1 ATOM 4334 C CG . PHE B 1 132 ? 52.845 -73.834 -6.933 1.00 86.38 ? 132 PHE B CG 1 ATOM 4335 C CD1 . PHE B 1 132 ? 53.598 -72.779 -7.425 1.00 83.87 ? 132 PHE B CD1 1 ATOM 4336 C CD2 . PHE B 1 132 ? 52.516 -73.842 -5.584 1.00 86.45 ? 132 PHE B CD2 1 ATOM 4337 C CE1 . PHE B 1 132 ? 54.015 -71.753 -6.589 1.00 81.69 ? 132 PHE B CE1 1 ATOM 4338 C CE2 . PHE B 1 132 ? 52.928 -72.816 -4.744 1.00 85.37 ? 132 PHE B CE2 1 ATOM 4339 C CZ . PHE B 1 132 ? 53.684 -71.775 -5.248 1.00 83.16 ? 132 PHE B CZ 1 ATOM 4340 N N . PHE B 1 133 ? 53.575 -77.266 -6.321 1.00 104.51 ? 133 PHE B N 1 ATOM 4341 C CA . PHE B 1 133 ? 54.101 -77.745 -5.051 1.00 109.56 ? 133 PHE B CA 1 ATOM 4342 C C . PHE B 1 133 ? 55.283 -78.688 -5.201 1.00 109.07 ? 133 PHE B C 1 ATOM 4343 O O . PHE B 1 133 ? 56.050 -78.840 -4.249 1.00 109.08 ? 133 PHE B O 1 ATOM 4344 C CB . PHE B 1 133 ? 52.996 -78.378 -4.218 1.00 109.97 ? 133 PHE B CB 1 ATOM 4345 C CG . PHE B 1 133 ? 51.974 -77.396 -3.747 1.00 108.89 ? 133 PHE B CG 1 ATOM 4346 C CD1 . PHE B 1 133 ? 52.353 -76.287 -2.996 1.00 107.48 ? 133 PHE B CD1 1 ATOM 4347 C CD2 . PHE B 1 133 ? 50.639 -77.578 -4.043 1.00 107.07 ? 133 PHE B CD2 1 ATOM 4348 C CE1 . PHE B 1 133 ? 51.413 -75.377 -2.554 1.00 106.50 ? 133 PHE B CE1 1 ATOM 4349 C CE2 . PHE B 1 133 ? 49.695 -76.671 -3.607 1.00 106.68 ? 133 PHE B CE2 1 ATOM 4350 C CZ . PHE B 1 133 ? 50.081 -75.569 -2.861 1.00 106.66 ? 133 PHE B CZ 1 ATOM 4351 N N . ARG B 1 134 ? 55.435 -79.299 -6.378 1.00 106.92 ? 134 ARG B N 1 ATOM 4352 C CA . ARG B 1 134 ? 56.650 -80.054 -6.688 1.00 109.97 ? 134 ARG B CA 1 ATOM 4353 C C . ARG B 1 134 ? 57.827 -79.093 -6.776 1.00 111.46 ? 134 ARG B C 1 ATOM 4354 O O . ARG B 1 134 ? 58.931 -79.409 -6.329 1.00 116.92 ? 134 ARG B O 1 ATOM 4355 C CB . ARG B 1 134 ? 56.551 -80.801 -8.017 1.00 106.62 ? 134 ARG B CB 1 ATOM 4356 C CG . ARG B 1 134 ? 55.486 -81.870 -8.086 1.00 107.78 ? 134 ARG B CG 1 ATOM 4357 C CD . ARG B 1 134 ? 55.642 -82.668 -9.371 1.00 110.80 ? 134 ARG B CD 1 ATOM 4358 N NE . ARG B 1 134 ? 54.360 -83.173 -9.876 1.00 110.84 ? 134 ARG B NE 1 ATOM 4359 C CZ . ARG B 1 134 ? 53.854 -82.953 -11.100 1.00 108.80 ? 134 ARG B CZ 1 ATOM 4360 N NH1 . ARG B 1 134 ? 54.501 -82.240 -12.018 1.00 100.91 ? 134 ARG B NH1 1 ATOM 4361 N NH2 . ARG B 1 134 ? 52.677 -83.481 -11.419 1.00 109.49 ? 134 ARG B NH2 1 ATOM 4362 N N . LEU B 1 135 ? 57.571 -77.925 -7.357 1.00 104.53 ? 135 LEU B N 1 ATOM 4363 C CA . LEU B 1 135 ? 58.582 -76.903 -7.549 1.00 107.74 ? 135 LEU B CA 1 ATOM 4364 C C . LEU B 1 135 ? 58.776 -76.071 -6.293 1.00 106.49 ? 135 LEU B C 1 ATOM 4365 O O . LEU B 1 135 ? 59.879 -75.613 -6.016 1.00 111.26 ? 135 LEU B O 1 ATOM 4366 C CB . LEU B 1 135 ? 58.202 -75.997 -8.731 1.00 109.96 ? 135 LEU B CB 1 ATOM 4367 C CG . LEU B 1 135 ? 58.117 -76.698 -10.096 1.00 108.73 ? 135 LEU B CG 1 ATOM 4368 C CD1 . LEU B 1 135 ? 57.255 -75.931 -11.087 1.00 107.31 ? 135 LEU B CD1 1 ATOM 4369 C CD2 . LEU B 1 135 ? 59.503 -76.936 -10.671 1.00 109.68 ? 135 LEU B CD2 1 ATOM 4370 N N . PHE B 1 136 ? 57.701 -75.867 -5.544 1.00 106.37 ? 136 PHE B N 1 ATOM 4371 C CA . PHE B 1 136 ? 57.745 -75.092 -4.304 1.00 107.23 ? 136 PHE B CA 1 ATOM 4372 C C . PHE B 1 136 ? 57.298 -75.954 -3.127 1.00 110.05 ? 136 PHE B C 1 ATOM 4373 O O . PHE B 1 136 ? 56.285 -75.657 -2.513 1.00 113.85 ? 136 PHE B O 1 ATOM 4374 C CB . PHE B 1 136 ? 56.822 -73.872 -4.416 1.00 103.14 ? 136 PHE B CB 1 ATOM 4375 C CG . PHE B 1 136 ? 57.370 -72.757 -5.268 1.00 99.91 ? 136 PHE B CG 1 ATOM 4376 C CD1 . PHE B 1 136 ? 57.172 -72.752 -6.650 1.00 94.68 ? 136 PHE B CD1 1 ATOM 4377 C CD2 . PHE B 1 136 ? 58.062 -71.703 -4.693 1.00 96.05 ? 136 PHE B CD2 1 ATOM 4378 C CE1 . PHE B 1 136 ? 57.652 -71.723 -7.437 1.00 89.36 ? 136 PHE B CE1 1 ATOM 4379 C CE2 . PHE B 1 136 ? 58.551 -70.673 -5.480 1.00 96.25 ? 136 PHE B CE2 1 ATOM 4380 C CZ . PHE B 1 136 ? 58.340 -70.680 -6.855 1.00 92.91 ? 136 PHE B CZ 1 ATOM 4381 N N . PRO B 1 137 ? 58.052 -77.012 -2.800 1.00 112.83 ? 137 PRO B N 1 ATOM 4382 C CA . PRO B 1 137 ? 57.630 -77.914 -1.715 1.00 113.67 ? 137 PRO B CA 1 ATOM 4383 C C . PRO B 1 137 ? 57.541 -77.263 -0.327 1.00 112.20 ? 137 PRO B C 1 ATOM 4384 O O . PRO B 1 137 ? 56.695 -77.655 0.483 1.00 105.19 ? 137 PRO B O 1 ATOM 4385 C CB . PRO B 1 137 ? 58.694 -79.016 -1.733 1.00 118.13 ? 137 PRO B CB 1 ATOM 4386 C CG . PRO B 1 137 ? 59.860 -78.445 -2.472 1.00 117.60 ? 137 PRO B CG 1 ATOM 4387 C CD . PRO B 1 137 ? 59.309 -77.444 -3.433 1.00 115.41 ? 137 PRO B CD 1 ATOM 4388 N N . GLU B 1 138 ? 58.385 -76.262 -0.083 1.00 110.62 ? 138 GLU B N 1 ATOM 4389 C CA . GLU B 1 138 ? 58.414 -75.521 1.192 1.00 110.64 ? 138 GLU B CA 1 ATOM 4390 C C . GLU B 1 138 ? 57.134 -74.730 1.496 1.00 108.69 ? 138 GLU B C 1 ATOM 4391 O O . GLU B 1 138 ? 56.981 -74.192 2.597 1.00 106.19 ? 138 GLU B O 1 ATOM 4392 C CB . GLU B 1 138 ? 59.643 -74.587 1.245 1.00 108.80 ? 138 GLU B CB 1 ATOM 4393 C CG . GLU B 1 138 ? 59.678 -73.440 0.228 1.00 104.98 ? 138 GLU B CG 1 ATOM 4394 C CD . GLU B 1 138 ? 60.229 -73.832 -1.147 1.00 102.08 ? 138 GLU B CD 1 ATOM 4395 O OE1 . GLU B 1 138 ? 59.836 -74.891 -1.680 1.00 96.87 ? 138 GLU B OE1 1 ATOM 4396 O OE2 . GLU B 1 138 ? 61.043 -73.063 -1.710 1.00 95.94 ? 138 GLU B OE2 1 ATOM 4397 N N . TYR B 1 139 ? 56.245 -74.635 0.505 1.00 108.37 ? 139 TYR B N 1 ATOM 4398 C CA . TYR B 1 139 ? 54.956 -73.954 0.660 1.00 107.82 ? 139 TYR B CA 1 ATOM 4399 C C . TYR B 1 139 ? 53.770 -74.918 0.745 1.00 108.20 ? 139 TYR B C 1 ATOM 4400 O O . TYR B 1 139 ? 52.619 -74.480 0.782 1.00 101.97 ? 139 TYR B O 1 ATOM 4401 C CB . TYR B 1 139 ? 54.745 -72.949 -0.480 1.00 102.44 ? 139 TYR B CB 1 ATOM 4402 C CG . TYR B 1 139 ? 55.628 -71.727 -0.360 1.00 100.40 ? 139 TYR B CG 1 ATOM 4403 C CD1 . TYR B 1 139 ? 55.565 -70.910 0.758 1.00 102.96 ? 139 TYR B CD1 1 ATOM 4404 C CD2 . TYR B 1 139 ? 56.520 -71.386 -1.367 1.00 97.88 ? 139 TYR B CD2 1 ATOM 4405 C CE1 . TYR B 1 139 ? 56.371 -69.789 0.877 1.00 101.92 ? 139 TYR B CE1 1 ATOM 4406 C CE2 . TYR B 1 139 ? 57.318 -70.268 -1.263 1.00 97.69 ? 139 TYR B CE2 1 ATOM 4407 C CZ . TYR B 1 139 ? 57.245 -69.473 -0.135 1.00 101.09 ? 139 TYR B CZ 1 ATOM 4408 O OH . TYR B 1 139 ? 58.044 -68.353 -0.025 1.00 101.68 ? 139 TYR B OH 1 ATOM 4409 N N . LYS B 1 140 ? 54.050 -76.218 0.776 1.00 110.00 ? 140 LYS B N 1 ATOM 4410 C CA . LYS B 1 140 ? 52.999 -77.221 0.927 1.00 113.74 ? 140 LYS B CA 1 ATOM 4411 C C . LYS B 1 140 ? 52.281 -77.118 2.267 1.00 113.91 ? 140 LYS B C 1 ATOM 4412 O O . LYS B 1 140 ? 51.135 -77.524 2.374 1.00 108.64 ? 140 LYS B O 1 ATOM 4413 C CB . LYS B 1 140 ? 53.561 -78.635 0.800 1.00 119.35 ? 140 LYS B CB 1 ATOM 4414 C CG . LYS B 1 140 ? 53.880 -79.073 -0.614 1.00 121.47 ? 140 LYS B CG 1 ATOM 4415 C CD . LYS B 1 140 ? 54.307 -80.533 -0.626 1.00 125.52 ? 140 LYS B CD 1 ATOM 4416 C CE . LYS B 1 140 ? 54.452 -81.071 -2.038 1.00 123.26 ? 140 LYS B CE 1 ATOM 4417 N NZ . LYS B 1 140 ? 54.723 -82.529 -2.030 1.00 122.98 ? 140 LYS B NZ 1 ATOM 4418 N N . ASN B 1 141 ? 52.952 -76.598 3.292 1.00 117.24 ? 141 ASN B N 1 ATOM 4419 C CA . ASN B 1 141 ? 52.349 -76.497 4.625 1.00 122.46 ? 141 ASN B CA 1 ATOM 4420 C C . ASN B 1 141 ? 51.440 -75.289 4.786 1.00 114.30 ? 141 ASN B C 1 ATOM 4421 O O . ASN B 1 141 ? 50.484 -75.322 5.568 1.00 104.84 ? 141 ASN B O 1 ATOM 4422 C CB . ASN B 1 141 ? 53.434 -76.441 5.702 1.00 131.73 ? 141 ASN B CB 1 ATOM 4423 C CG . ASN B 1 141 ? 54.252 -77.715 5.772 1.00 138.72 ? 141 ASN B CG 1 ATOM 4424 O OD1 . ASN B 1 141 ? 55.473 -77.675 5.919 1.00 141.52 ? 141 ASN B OD1 1 ATOM 4425 N ND2 . ASN B 1 141 ? 53.580 -78.856 5.661 1.00 138.49 ? 141 ASN B ND2 1 ATOM 4426 N N . ASN B 1 142 ? 51.745 -74.235 4.037 1.00 107.16 ? 142 ASN B N 1 ATOM 4427 C CA . ASN B 1 142 ? 51.085 -72.958 4.198 1.00 104.97 ? 142 ASN B CA 1 ATOM 4428 C C . ASN B 1 142 ? 49.591 -73.070 3.968 1.00 101.41 ? 142 ASN B C 1 ATOM 4429 O O . ASN B 1 142 ? 49.132 -73.927 3.215 1.00 97.03 ? 142 ASN B O 1 ATOM 4430 C CB . ASN B 1 142 ? 51.676 -71.925 3.237 1.00 107.12 ? 142 ASN B CB 1 ATOM 4431 C CG . ASN B 1 142 ? 53.172 -71.719 3.448 1.00 108.15 ? 142 ASN B CG 1 ATOM 4432 O OD1 . ASN B 1 142 ? 53.929 -72.687 3.530 1.00 113.27 ? 142 ASN B OD1 1 ATOM 4433 N ND2 . ASN B 1 142 ? 53.604 -70.458 3.511 1.00 102.88 ? 142 ASN B ND2 1 ATOM 4434 N N . LYS B 1 143 ? 48.831 -72.209 4.631 1.00 101.04 ? 143 LYS B N 1 ATOM 4435 C CA . LYS B 1 143 ? 47.397 -72.146 4.402 1.00 100.67 ? 143 LYS B CA 1 ATOM 4436 C C . LYS B 1 143 ? 47.184 -71.779 2.934 1.00 94.04 ? 143 LYS B C 1 ATOM 4437 O O . LYS B 1 143 ? 47.872 -70.900 2.423 1.00 91.66 ? 143 LYS B O 1 ATOM 4438 C CB . LYS B 1 143 ? 46.744 -71.099 5.305 1.00 102.63 ? 143 LYS B CB 1 ATOM 4439 C CG . LYS B 1 143 ? 46.895 -71.348 6.793 1.00 106.17 ? 143 LYS B CG 1 ATOM 4440 C CD . LYS B 1 143 ? 45.998 -70.411 7.579 1.00 110.77 ? 143 LYS B CD 1 ATOM 4441 C CE . LYS B 1 143 ? 46.546 -70.126 8.970 1.00 114.25 ? 143 LYS B CE 1 ATOM 4442 N NZ . LYS B 1 143 ? 45.582 -69.366 9.820 1.00 114.01 ? 143 LYS B NZ 1 ATOM 4443 N N . LEU B 1 144 ? 46.276 -72.481 2.261 1.00 88.94 ? 144 LEU B N 1 ATOM 4444 C CA . LEU B 1 144 ? 46.070 -72.312 0.820 1.00 87.11 ? 144 LEU B CA 1 ATOM 4445 C C . LEU B 1 144 ? 44.673 -71.800 0.503 1.00 88.24 ? 144 LEU B C 1 ATOM 4446 O O . LEU B 1 144 ? 43.680 -72.475 0.778 1.00 93.01 ? 144 LEU B O 1 ATOM 4447 C CB . LEU B 1 144 ? 46.286 -73.632 0.090 1.00 87.53 ? 144 LEU B CB 1 ATOM 4448 C CG . LEU B 1 144 ? 45.888 -73.664 -1.392 1.00 86.84 ? 144 LEU B CG 1 ATOM 4449 C CD1 . LEU B 1 144 ? 46.747 -72.706 -2.195 1.00 84.25 ? 144 LEU B CD1 1 ATOM 4450 C CD2 . LEU B 1 144 ? 45.986 -75.065 -1.963 1.00 84.96 ? 144 LEU B CD2 1 ATOM 4451 N N . PHE B 1 145 ? 44.606 -70.612 -0.084 1.00 84.83 ? 145 PHE B N 1 ATOM 4452 C CA . PHE B 1 145 ? 43.345 -70.039 -0.524 1.00 84.41 ? 145 PHE B CA 1 ATOM 4453 C C . PHE B 1 145 ? 43.270 -69.929 -2.045 1.00 84.48 ? 145 PHE B C 1 ATOM 4454 O O . PHE B 1 145 ? 44.254 -69.602 -2.726 1.00 81.42 ? 145 PHE B O 1 ATOM 4455 C CB . PHE B 1 145 ? 43.143 -68.664 0.098 1.00 82.94 ? 145 PHE B CB 1 ATOM 4456 C CG . PHE B 1 145 ? 43.023 -68.700 1.585 1.00 81.94 ? 145 PHE B CG 1 ATOM 4457 C CD1 . PHE B 1 145 ? 41.800 -68.927 2.193 1.00 81.20 ? 145 PHE B CD1 1 ATOM 4458 C CD2 . PHE B 1 145 ? 44.138 -68.528 2.375 1.00 79.19 ? 145 PHE B CD2 1 ATOM 4459 C CE1 . PHE B 1 145 ? 41.699 -68.973 3.575 1.00 81.19 ? 145 PHE B CE1 1 ATOM 4460 C CE2 . PHE B 1 145 ? 44.043 -68.563 3.747 1.00 82.26 ? 145 PHE B CE2 1 ATOM 4461 C CZ . PHE B 1 145 ? 42.827 -68.785 4.353 1.00 81.87 ? 145 PHE B CZ 1 ATOM 4462 N N . LEU B 1 146 ? 42.082 -70.206 -2.558 1.00 82.92 ? 146 LEU B N 1 ATOM 4463 C CA . LEU B 1 146 ? 41.790 -70.111 -3.976 1.00 80.34 ? 146 LEU B CA 1 ATOM 4464 C C . LEU B 1 146 ? 40.933 -68.873 -4.177 1.00 79.51 ? 146 LEU B C 1 ATOM 4465 O O . LEU B 1 146 ? 39.847 -68.789 -3.618 1.00 75.39 ? 146 LEU B O 1 ATOM 4466 C CB . LEU B 1 146 ? 41.019 -71.353 -4.426 1.00 79.62 ? 146 LEU B CB 1 ATOM 4467 C CG . LEU B 1 146 ? 41.588 -72.720 -4.046 1.00 79.71 ? 146 LEU B CG 1 ATOM 4468 C CD1 . LEU B 1 146 ? 40.655 -73.822 -4.509 1.00 79.64 ? 146 LEU B CD1 1 ATOM 4469 C CD2 . LEU B 1 146 ? 42.960 -72.924 -4.642 1.00 81.88 ? 146 LEU B CD2 1 ATOM 4470 N N . THR B 1 147 ? 41.429 -67.905 -4.944 1.00 79.13 ? 147 THR B N 1 ATOM 4471 C CA . THR B 1 147 ? 40.698 -66.664 -5.178 1.00 76.50 ? 147 THR B CA 1 ATOM 4472 C C . THR B 1 147 ? 40.663 -66.358 -6.650 1.00 74.48 ? 147 THR B C 1 ATOM 4473 O O . THR B 1 147 ? 41.578 -66.704 -7.380 1.00 73.14 ? 147 THR B O 1 ATOM 4474 C CB . THR B 1 147 ? 41.339 -65.448 -4.494 1.00 78.35 ? 147 THR B CB 1 ATOM 4475 O OG1 . THR B 1 147 ? 42.588 -65.154 -5.129 1.00 79.02 ? 147 THR B OG1 1 ATOM 4476 C CG2 . THR B 1 147 ? 41.541 -65.693 -2.989 1.00 79.87 ? 147 THR B CG2 1 ATOM 4477 N N . GLY B 1 148 ? 39.599 -65.701 -7.080 1.00 75.00 ? 148 GLY B N 1 ATOM 4478 C CA . GLY B 1 148 ? 39.440 -65.350 -8.479 1.00 72.05 ? 148 GLY B CA 1 ATOM 4479 C C . GLY B 1 148 ? 38.425 -64.259 -8.680 1.00 70.11 ? 148 GLY B C 1 ATOM 4480 O O . GLY B 1 148 ? 37.886 -63.713 -7.714 1.00 66.02 ? 148 GLY B O 1 ATOM 4481 N N . GLU B 1 149 ? 38.192 -63.923 -9.944 1.00 69.56 ? 149 GLU B N 1 ATOM 4482 C CA . GLU B 1 149 ? 37.263 -62.865 -10.302 1.00 69.46 ? 149 GLU B CA 1 ATOM 4483 C C . GLU B 1 149 ? 36.505 -63.247 -11.549 1.00 66.61 ? 149 GLU B C 1 ATOM 4484 O O . GLU B 1 149 ? 36.949 -64.099 -12.293 1.00 63.76 ? 149 GLU B O 1 ATOM 4485 C CB . GLU B 1 149 ? 38.056 -61.595 -10.552 1.00 73.09 ? 149 GLU B CB 1 ATOM 4486 C CG . GLU B 1 149 ? 37.232 -60.357 -10.782 1.00 75.16 ? 149 GLU B CG 1 ATOM 4487 C CD . GLU B 1 149 ? 38.089 -59.229 -11.280 1.00 76.10 ? 149 GLU B CD 1 ATOM 4488 O OE1 . GLU B 1 149 ? 38.915 -58.731 -10.487 1.00 71.09 ? 149 GLU B OE1 1 ATOM 4489 O OE2 . GLU B 1 149 ? 37.944 -58.870 -12.471 1.00 81.77 ? 149 GLU B OE2 1 ATOM 4490 N N . SER B 1 150 ? 35.352 -62.630 -11.767 1.00 72.77 ? 150 SER B N 1 ATOM 4491 C CA . SER B 1 150 ? 34.673 -62.701 -13.071 1.00 76.54 ? 150 SER B CA 1 ATOM 4492 C C . SER B 1 150 ? 34.299 -64.157 -13.405 1.00 71.25 ? 150 SER B C 1 ATOM 4493 O O . SER B 1 150 ? 33.772 -64.861 -12.558 1.00 69.36 ? 150 SER B O 1 ATOM 4494 C CB . SER B 1 150 ? 35.571 -62.052 -14.148 1.00 80.61 ? 150 SER B CB 1 ATOM 4495 O OG . SER B 1 150 ? 34.911 -61.905 -15.391 1.00 86.72 ? 150 SER B OG 1 ATOM 4496 N N . TYR B 1 151 ? 34.597 -64.631 -14.612 1.00 71.61 ? 151 TYR B N 1 ATOM 4497 C CA . TYR B 1 151 ? 34.331 -66.034 -14.958 1.00 67.11 ? 151 TYR B CA 1 ATOM 4498 C C . TYR B 1 151 ? 34.985 -67.036 -13.998 1.00 66.79 ? 151 TYR B C 1 ATOM 4499 O O . TYR B 1 151 ? 34.610 -68.201 -13.994 1.00 71.70 ? 151 TYR B O 1 ATOM 4500 C CB . TYR B 1 151 ? 34.744 -66.365 -16.405 1.00 63.45 ? 151 TYR B CB 1 ATOM 4501 C CG . TYR B 1 151 ? 34.133 -67.659 -16.864 1.00 59.44 ? 151 TYR B CG 1 ATOM 4502 C CD1 . TYR B 1 151 ? 32.826 -67.703 -17.284 1.00 58.02 ? 151 TYR B CD1 1 ATOM 4503 C CD2 . TYR B 1 151 ? 34.834 -68.836 -16.817 1.00 57.92 ? 151 TYR B CD2 1 ATOM 4504 C CE1 . TYR B 1 151 ? 32.237 -68.889 -17.665 1.00 57.04 ? 151 TYR B CE1 1 ATOM 4505 C CE2 . TYR B 1 151 ? 34.248 -70.030 -17.184 1.00 58.26 ? 151 TYR B CE2 1 ATOM 4506 C CZ . TYR B 1 151 ? 32.944 -70.053 -17.609 1.00 56.45 ? 151 TYR B CZ 1 ATOM 4507 O OH . TYR B 1 151 ? 32.338 -71.236 -17.986 1.00 56.51 ? 151 TYR B OH 1 ATOM 4508 N N . ALA B 1 152 ? 35.933 -66.594 -13.173 1.00 65.39 ? 152 ALA B N 1 ATOM 4509 C CA . ALA B 1 152 ? 36.533 -67.469 -12.172 1.00 64.89 ? 152 ALA B CA 1 ATOM 4510 C C . ALA B 1 152 ? 35.543 -67.821 -11.056 1.00 69.57 ? 152 ALA B C 1 ATOM 4511 O O . ALA B 1 152 ? 35.858 -68.605 -10.176 1.00 75.39 ? 152 ALA B O 1 ATOM 4512 C CB . ALA B 1 152 ? 37.782 -66.854 -11.588 1.00 60.28 ? 152 ALA B CB 1 ATOM 4513 N N . GLY B 1 153 ? 34.349 -67.238 -11.083 1.00 70.04 ? 153 GLY B N 1 ATOM 4514 C CA . GLY B 1 153 ? 33.232 -67.751 -10.297 1.00 69.31 ? 153 GLY B CA 1 ATOM 4515 C C . GLY B 1 153 ? 32.881 -69.171 -10.701 1.00 67.89 ? 153 GLY B C 1 ATOM 4516 O O . GLY B 1 153 ? 32.252 -69.880 -9.924 1.00 66.71 ? 153 GLY B O 1 ATOM 4517 N N . ILE B 1 154 ? 33.300 -69.571 -11.907 1.00 65.50 ? 154 ILE B N 1 ATOM 4518 C CA . ILE B 1 154 ? 33.260 -70.961 -12.369 1.00 67.60 ? 154 ILE B CA 1 ATOM 4519 C C . ILE B 1 154 ? 34.589 -71.685 -12.170 1.00 68.00 ? 154 ILE B C 1 ATOM 4520 O O . ILE B 1 154 ? 34.621 -72.821 -11.693 1.00 67.64 ? 154 ILE B O 1 ATOM 4521 C CB . ILE B 1 154 ? 32.908 -71.055 -13.865 1.00 67.70 ? 154 ILE B CB 1 ATOM 4522 C CG1 . ILE B 1 154 ? 31.606 -70.314 -14.168 1.00 67.83 ? 154 ILE B CG1 1 ATOM 4523 C CG2 . ILE B 1 154 ? 32.796 -72.513 -14.295 1.00 72.90 ? 154 ILE B CG2 1 ATOM 4524 C CD1 . ILE B 1 154 ? 30.395 -70.834 -13.430 1.00 67.88 ? 154 ILE B CD1 1 ATOM 4525 N N . TYR B 1 155 ? 35.684 -71.052 -12.562 1.00 67.88 ? 155 TYR B N 1 ATOM 4526 C CA . TYR B 1 155 ? 36.989 -71.679 -12.398 1.00 71.51 ? 155 TYR B CA 1 ATOM 4527 C C . TYR B 1 155 ? 37.190 -72.153 -10.961 1.00 71.01 ? 155 TYR B C 1 ATOM 4528 O O . TYR B 1 155 ? 37.596 -73.279 -10.737 1.00 73.74 ? 155 TYR B O 1 ATOM 4529 C CB . TYR B 1 155 ? 38.147 -70.725 -12.740 1.00 70.95 ? 155 TYR B CB 1 ATOM 4530 C CG . TYR B 1 155 ? 38.276 -70.259 -14.174 1.00 70.76 ? 155 TYR B CG 1 ATOM 4531 C CD1 . TYR B 1 155 ? 37.848 -71.035 -15.249 1.00 71.81 ? 155 TYR B CD1 1 ATOM 4532 C CD2 . TYR B 1 155 ? 38.898 -69.057 -14.458 1.00 74.71 ? 155 TYR B CD2 1 ATOM 4533 C CE1 . TYR B 1 155 ? 37.996 -70.598 -16.555 1.00 67.88 ? 155 TYR B CE1 1 ATOM 4534 C CE2 . TYR B 1 155 ? 39.056 -68.617 -15.766 1.00 72.89 ? 155 TYR B CE2 1 ATOM 4535 C CZ . TYR B 1 155 ? 38.601 -69.392 -16.805 1.00 68.36 ? 155 TYR B CZ 1 ATOM 4536 O OH . TYR B 1 155 ? 38.754 -68.930 -18.088 1.00 71.46 ? 155 TYR B OH 1 ATOM 4537 N N . ILE B 1 156 ? 36.906 -71.280 -9.999 1.00 71.25 ? 156 ILE B N 1 ATOM 4538 C CA . ILE B 1 156 ? 37.337 -71.474 -8.603 1.00 76.48 ? 156 ILE B CA 1 ATOM 4539 C C . ILE B 1 156 ? 36.581 -72.569 -7.837 1.00 78.59 ? 156 ILE B C 1 ATOM 4540 O O . ILE B 1 156 ? 37.208 -73.432 -7.243 1.00 80.36 ? 156 ILE B O 1 ATOM 4541 C CB . ILE B 1 156 ? 37.305 -70.144 -7.807 1.00 76.48 ? 156 ILE B CB 1 ATOM 4542 C CG1 . ILE B 1 156 ? 38.420 -69.210 -8.282 1.00 75.19 ? 156 ILE B CG1 1 ATOM 4543 C CG2 . ILE B 1 156 ? 37.405 -70.377 -6.308 1.00 81.21 ? 156 ILE B CG2 1 ATOM 4544 C CD1 . ILE B 1 156 ? 39.827 -69.713 -8.070 1.00 76.01 ? 156 ILE B CD1 1 ATOM 4545 N N . PRO B 1 157 ? 35.245 -72.537 -7.832 1.00 78.19 ? 157 PRO B N 1 ATOM 4546 C CA . PRO B 1 157 ? 34.568 -73.627 -7.153 1.00 78.21 ? 157 PRO B CA 1 ATOM 4547 C C . PRO B 1 157 ? 34.847 -74.973 -7.783 1.00 79.24 ? 157 PRO B C 1 ATOM 4548 O O . PRO B 1 157 ? 35.028 -75.939 -7.060 1.00 88.45 ? 157 PRO B O 1 ATOM 4549 C CB . PRO B 1 157 ? 33.093 -73.274 -7.310 1.00 78.70 ? 157 PRO B CB 1 ATOM 4550 C CG . PRO B 1 157 ? 33.080 -71.809 -7.486 1.00 76.61 ? 157 PRO B CG 1 ATOM 4551 C CD . PRO B 1 157 ? 34.290 -71.540 -8.327 1.00 76.40 ? 157 PRO B CD 1 ATOM 4552 N N . THR B 1 158 ? 34.887 -75.039 -9.114 1.00 79.27 ? 158 THR B N 1 ATOM 4553 C CA . THR B 1 158 ? 35.128 -76.308 -9.809 1.00 78.19 ? 158 THR B CA 1 ATOM 4554 C C . THR B 1 158 ? 36.524 -76.815 -9.473 1.00 78.98 ? 158 THR B C 1 ATOM 4555 O O . THR B 1 158 ? 36.718 -78.008 -9.228 1.00 82.12 ? 158 THR B O 1 ATOM 4556 C CB . THR B 1 158 ? 34.962 -76.200 -11.340 1.00 75.88 ? 158 THR B CB 1 ATOM 4557 O OG1 . THR B 1 158 ? 35.875 -75.238 -11.876 1.00 80.89 ? 158 THR B OG1 1 ATOM 4558 C CG2 . THR B 1 158 ? 33.556 -75.800 -11.702 1.00 76.49 ? 158 THR B CG2 1 ATOM 4559 N N . LEU B 1 159 ? 37.483 -75.897 -9.454 1.00 75.29 ? 159 LEU B N 1 ATOM 4560 C CA . LEU B 1 159 ? 38.841 -76.206 -9.051 1.00 77.64 ? 159 LEU B CA 1 ATOM 4561 C C . LEU B 1 159 ? 38.842 -76.709 -7.623 1.00 79.96 ? 159 LEU B C 1 ATOM 4562 O O . LEU B 1 159 ? 39.403 -77.754 -7.336 1.00 85.39 ? 159 LEU B O 1 ATOM 4563 C CB . LEU B 1 159 ? 39.746 -74.966 -9.149 1.00 75.23 ? 159 LEU B CB 1 ATOM 4564 C CG . LEU B 1 159 ? 41.176 -75.149 -8.630 1.00 75.89 ? 159 LEU B CG 1 ATOM 4565 C CD1 . LEU B 1 159 ? 41.834 -76.356 -9.275 1.00 75.28 ? 159 LEU B CD1 1 ATOM 4566 C CD2 . LEU B 1 159 ? 42.030 -73.909 -8.853 1.00 75.55 ? 159 LEU B CD2 1 ATOM 4567 N N . ALA B 1 160 ? 38.218 -75.942 -6.735 1.00 80.88 ? 160 ALA B N 1 ATOM 4568 C CA . ALA B 1 160 ? 38.220 -76.216 -5.295 1.00 80.81 ? 160 ALA B CA 1 ATOM 4569 C C . ALA B 1 160 ? 37.772 -77.627 -5.007 1.00 82.17 ? 160 ALA B C 1 ATOM 4570 O O . ALA B 1 160 ? 38.369 -78.316 -4.184 1.00 87.80 ? 160 ALA B O 1 ATOM 4571 C CB . ALA B 1 160 ? 37.334 -75.223 -4.560 1.00 80.50 ? 160 ALA B CB 1 ATOM 4572 N N . VAL B 1 161 ? 36.736 -78.065 -5.702 1.00 81.27 ? 161 VAL B N 1 ATOM 4573 C CA . VAL B 1 161 ? 36.281 -79.442 -5.586 1.00 88.03 ? 161 VAL B CA 1 ATOM 4574 C C . VAL B 1 161 ? 37.396 -80.448 -5.873 1.00 87.33 ? 161 VAL B C 1 ATOM 4575 O O . VAL B 1 161 ? 37.581 -81.390 -5.127 1.00 90.38 ? 161 VAL B O 1 ATOM 4576 C CB . VAL B 1 161 ? 35.081 -79.709 -6.502 1.00 89.57 ? 161 VAL B CB 1 ATOM 4577 C CG1 . VAL B 1 161 ? 34.840 -81.195 -6.650 1.00 90.22 ? 161 VAL B CG1 1 ATOM 4578 C CG2 . VAL B 1 161 ? 33.849 -79.009 -5.942 1.00 91.74 ? 161 VAL B CG2 1 ATOM 4579 N N . LEU B 1 162 ? 38.156 -80.236 -6.932 1.00 89.12 ? 162 LEU B N 1 ATOM 4580 C CA . LEU B 1 162 ? 39.294 -81.108 -7.216 1.00 92.67 ? 162 LEU B CA 1 ATOM 4581 C C . LEU B 1 162 ? 40.341 -81.029 -6.099 1.00 96.38 ? 162 LEU B C 1 ATOM 4582 O O . LEU B 1 162 ? 40.917 -82.044 -5.717 1.00 102.37 ? 162 LEU B O 1 ATOM 4583 C CB . LEU B 1 162 ? 39.939 -80.763 -8.565 1.00 88.08 ? 162 LEU B CB 1 ATOM 4584 C CG . LEU B 1 162 ? 39.080 -80.927 -9.816 1.00 86.28 ? 162 LEU B CG 1 ATOM 4585 C CD1 . LEU B 1 162 ? 39.846 -80.473 -11.044 1.00 90.41 ? 162 LEU B CD1 1 ATOM 4586 C CD2 . LEU B 1 162 ? 38.631 -82.357 -9.995 1.00 88.55 ? 162 LEU B CD2 1 ATOM 4587 N N . VAL B 1 163 ? 40.572 -79.823 -5.583 1.00 94.77 ? 163 VAL B N 1 ATOM 4588 C CA . VAL B 1 163 ? 41.542 -79.600 -4.512 1.00 94.13 ? 163 VAL B CA 1 ATOM 4589 C C . VAL B 1 163 ? 41.061 -80.271 -3.231 1.00 96.31 ? 163 VAL B C 1 ATOM 4590 O O . VAL B 1 163 ? 41.847 -80.838 -2.471 1.00 94.23 ? 163 VAL B O 1 ATOM 4591 C CB . VAL B 1 163 ? 41.745 -78.100 -4.252 1.00 91.52 ? 163 VAL B CB 1 ATOM 4592 C CG1 . VAL B 1 163 ? 42.650 -77.870 -3.050 1.00 92.76 ? 163 VAL B CG1 1 ATOM 4593 C CG2 . VAL B 1 163 ? 42.316 -77.425 -5.486 1.00 87.97 ? 163 VAL B CG2 1 ATOM 4594 N N . MET B 1 164 ? 39.756 -80.192 -3.006 1.00 98.12 ? 164 MET B N 1 ATOM 4595 C CA . MET B 1 164 ? 39.106 -80.819 -1.862 1.00 103.59 ? 164 MET B CA 1 ATOM 4596 C C . MET B 1 164 ? 39.396 -82.319 -1.817 1.00 106.64 ? 164 MET B C 1 ATOM 4597 O O . MET B 1 164 ? 39.507 -82.895 -0.739 1.00 103.15 ? 164 MET B O 1 ATOM 4598 C CB . MET B 1 164 ? 37.605 -80.581 -1.950 1.00 102.60 ? 164 MET B CB 1 ATOM 4599 C CG . MET B 1 164 ? 36.805 -81.144 -0.796 1.00 103.97 ? 164 MET B CG 1 ATOM 4600 S SD . MET B 1 164 ? 35.071 -80.791 -1.031 1.00 104.59 ? 164 MET B SD 1 ATOM 4601 C CE . MET B 1 164 ? 34.787 -81.597 -2.606 1.00 103.91 ? 164 MET B CE 1 ATOM 4602 N N . GLN B 1 165 ? 39.526 -82.935 -2.991 1.00 110.32 ? 165 GLN B N 1 ATOM 4603 C CA . GLN B 1 165 ? 39.860 -84.351 -3.091 1.00 113.99 ? 165 GLN B CA 1 ATOM 4604 C C . GLN B 1 165 ? 41.308 -84.682 -2.707 1.00 117.80 ? 165 GLN B C 1 ATOM 4605 O O . GLN B 1 165 ? 41.598 -85.835 -2.415 1.00 127.63 ? 165 GLN B O 1 ATOM 4606 C CB . GLN B 1 165 ? 39.594 -84.869 -4.508 1.00 111.66 ? 165 GLN B CB 1 ATOM 4607 C CG . GLN B 1 165 ? 38.141 -84.851 -4.934 1.00 112.49 ? 165 GLN B CG 1 ATOM 4608 C CD . GLN B 1 165 ? 37.971 -85.025 -6.443 1.00 115.89 ? 165 GLN B CD 1 ATOM 4609 O OE1 . GLN B 1 165 ? 38.898 -85.410 -7.149 1.00 117.37 ? 165 GLN B OE1 1 ATOM 4610 N NE2 . GLN B 1 165 ? 36.769 -84.750 -6.937 1.00 117.82 ? 165 GLN B NE2 1 ATOM 4611 N N . ASP B 1 166 ? 42.214 -83.705 -2.722 1.00 115.85 ? 166 ASP B N 1 ATOM 4612 C CA . ASP B 1 166 ? 43.631 -83.972 -2.429 1.00 115.57 ? 166 ASP B CA 1 ATOM 4613 C C . ASP B 1 166 ? 44.059 -83.410 -1.071 1.00 120.02 ? 166 ASP B C 1 ATOM 4614 O O . ASP B 1 166 ? 44.336 -82.212 -0.963 1.00 123.74 ? 166 ASP B O 1 ATOM 4615 C CB . ASP B 1 166 ? 44.515 -83.407 -3.540 1.00 109.47 ? 166 ASP B CB 1 ATOM 4616 C CG . ASP B 1 166 ? 45.997 -83.673 -3.307 1.00 107.12 ? 166 ASP B CG 1 ATOM 4617 O OD1 . ASP B 1 166 ? 46.354 -84.338 -2.321 1.00 102.61 ? 166 ASP B OD1 1 ATOM 4618 O OD2 . ASP B 1 166 ? 46.814 -83.205 -4.128 1.00 106.18 ? 166 ASP B OD2 1 ATOM 4619 N N . PRO B 1 167 ? 44.164 -84.279 -0.040 1.00 127.89 ? 167 PRO B N 1 ATOM 4620 C CA . PRO B 1 167 ? 44.450 -83.799 1.318 1.00 124.10 ? 167 PRO B CA 1 ATOM 4621 C C . PRO B 1 167 ? 45.912 -83.420 1.554 1.00 120.41 ? 167 PRO B C 1 ATOM 4622 O O . PRO B 1 167 ? 46.230 -82.869 2.604 1.00 118.36 ? 167 PRO B O 1 ATOM 4623 C CB . PRO B 1 167 ? 44.050 -84.980 2.200 1.00 126.54 ? 167 PRO B CB 1 ATOM 4624 C CG . PRO B 1 167 ? 44.146 -86.186 1.325 1.00 126.55 ? 167 PRO B CG 1 ATOM 4625 C CD . PRO B 1 167 ? 44.230 -85.750 -0.111 1.00 126.68 ? 167 PRO B CD 1 ATOM 4626 N N . SER B 1 168 ? 46.777 -83.715 0.587 1.00 114.72 ? 168 SER B N 1 ATOM 4627 C CA . SER B 1 168 ? 48.119 -83.157 0.552 1.00 114.06 ? 168 SER B CA 1 ATOM 4628 C C . SER B 1 168 ? 48.074 -81.638 0.437 1.00 110.79 ? 168 SER B C 1 ATOM 4629 O O . SER B 1 168 ? 48.941 -80.964 0.973 1.00 114.94 ? 168 SER B O 1 ATOM 4630 C CB . SER B 1 168 ? 48.930 -83.739 -0.615 1.00 114.98 ? 168 SER B CB 1 ATOM 4631 O OG . SER B 1 168 ? 49.753 -82.761 -1.235 1.00 110.39 ? 168 SER B OG 1 ATOM 4632 N N . MET B 1 169 ? 47.086 -81.109 -0.281 1.00 108.83 ? 169 MET B N 1 ATOM 4633 C CA . MET B 1 169 ? 46.886 -79.659 -0.389 1.00 105.09 ? 169 MET B CA 1 ATOM 4634 C C . MET B 1 169 ? 46.097 -79.131 0.811 1.00 102.62 ? 169 MET B C 1 ATOM 4635 O O . MET B 1 169 ? 45.024 -79.651 1.122 1.00 94.69 ? 169 MET B O 1 ATOM 4636 C CB . MET B 1 169 ? 46.150 -79.304 -1.684 1.00 101.62 ? 169 MET B CB 1 ATOM 4637 C CG . MET B 1 169 ? 46.996 -79.389 -2.942 1.00 103.60 ? 169 MET B CG 1 ATOM 4638 S SD . MET B 1 169 ? 46.050 -79.159 -4.466 1.00 102.03 ? 169 MET B SD 1 ATOM 4639 C CE . MET B 1 169 ? 47.087 -80.009 -5.638 1.00 102.94 ? 169 MET B CE 1 ATOM 4640 N N . ASN B 1 170 ? 46.632 -78.082 1.450 1.00 101.77 ? 170 ASN B N 1 ATOM 4641 C CA . ASN B 1 170 ? 46.082 -77.521 2.701 1.00 101.98 ? 170 ASN B CA 1 ATOM 4642 C C . ASN B 1 170 ? 45.048 -76.415 2.460 1.00 99.47 ? 170 ASN B C 1 ATOM 4643 O O . ASN B 1 170 ? 45.216 -75.265 2.905 1.00 103.42 ? 170 ASN B O 1 ATOM 4644 C CB . ASN B 1 170 ? 47.224 -76.993 3.586 1.00 102.90 ? 170 ASN B CB 1 ATOM 4645 C CG . ASN B 1 170 ? 46.764 -76.617 4.992 1.00 104.55 ? 170 ASN B CG 1 ATOM 4646 O OD1 . ASN B 1 170 ? 45.719 -77.059 5.451 1.00 103.82 ? 170 ASN B OD1 1 ATOM 4647 N ND2 . ASN B 1 170 ? 47.552 -75.792 5.678 1.00 105.63 ? 170 ASN B ND2 1 ATOM 4648 N N . LEU B 1 171 ? 43.986 -76.770 1.747 1.00 93.97 ? 171 LEU B N 1 ATOM 4649 C CA . LEU B 1 171 ? 42.942 -75.822 1.376 1.00 93.24 ? 171 LEU B CA 1 ATOM 4650 C C . LEU B 1 171 ? 42.227 -75.271 2.610 1.00 93.76 ? 171 LEU B C 1 ATOM 4651 O O . LEU B 1 171 ? 41.652 -76.027 3.371 1.00 95.91 ? 171 LEU B O 1 ATOM 4652 C CB . LEU B 1 171 ? 41.940 -76.506 0.438 1.00 89.37 ? 171 LEU B CB 1 ATOM 4653 C CG . LEU B 1 171 ? 40.736 -75.686 -0.017 1.00 85.44 ? 171 LEU B CG 1 ATOM 4654 C CD1 . LEU B 1 171 ? 41.185 -74.468 -0.797 1.00 81.35 ? 171 LEU B CD1 1 ATOM 4655 C CD2 . LEU B 1 171 ? 39.792 -76.540 -0.838 1.00 84.04 ? 171 LEU B CD2 1 ATOM 4656 N N . GLN B 1 172 ? 42.259 -73.961 2.808 1.00 93.67 ? 172 GLN B N 1 ATOM 4657 C CA . GLN B 1 172 ? 41.548 -73.373 3.931 1.00 100.59 ? 172 GLN B CA 1 ATOM 4658 C C . GLN B 1 172 ? 40.323 -72.559 3.524 1.00 103.48 ? 172 GLN B C 1 ATOM 4659 O O . GLN B 1 172 ? 39.318 -72.572 4.233 1.00 106.69 ? 172 GLN B O 1 ATOM 4660 C CB . GLN B 1 172 ? 42.504 -72.565 4.806 1.00 105.37 ? 172 GLN B CB 1 ATOM 4661 C CG . GLN B 1 172 ? 43.441 -73.435 5.639 1.00 108.11 ? 172 GLN B CG 1 ATOM 4662 C CD . GLN B 1 172 ? 42.695 -74.349 6.613 1.00 109.08 ? 172 GLN B CD 1 ATOM 4663 O OE1 . GLN B 1 172 ? 41.970 -73.884 7.496 1.00 103.77 ? 172 GLN B OE1 1 ATOM 4664 N NE2 . GLN B 1 172 ? 42.871 -75.654 6.450 1.00 108.47 ? 172 GLN B NE2 1 ATOM 4665 N N . GLY B 1 173 ? 40.385 -71.882 2.378 1.00 105.74 ? 173 GLY B N 1 ATOM 4666 C CA . GLY B 1 173 ? 39.219 -71.172 1.853 1.00 99.84 ? 173 GLY B CA 1 ATOM 4667 C C . GLY B 1 173 ? 39.282 -70.743 0.393 1.00 96.17 ? 173 GLY B C 1 ATOM 4668 O O . GLY B 1 173 ? 40.255 -71.002 -0.325 1.00 90.86 ? 173 GLY B O 1 ATOM 4669 N N . LEU B 1 174 ? 38.218 -70.085 -0.043 1.00 95.94 ? 174 LEU B N 1 ATOM 4670 C CA . LEU B 1 174 ? 38.149 -69.507 -1.377 1.00 95.81 ? 174 LEU B CA 1 ATOM 4671 C C . LEU B 1 174 ? 37.337 -68.211 -1.407 1.00 93.96 ? 174 LEU B C 1 ATOM 4672 O O . LEU B 1 174 ? 36.375 -68.060 -0.669 1.00 92.44 ? 174 LEU B O 1 ATOM 4673 C CB . LEU B 1 174 ? 37.581 -70.519 -2.367 1.00 99.24 ? 174 LEU B CB 1 ATOM 4674 C CG . LEU B 1 174 ? 36.208 -71.113 -2.045 1.00 105.03 ? 174 LEU B CG 1 ATOM 4675 C CD1 . LEU B 1 174 ? 35.115 -70.402 -2.808 1.00 108.80 ? 174 LEU B CD1 1 ATOM 4676 C CD2 . LEU B 1 174 ? 36.139 -72.592 -2.382 1.00 111.47 ? 174 LEU B CD2 1 ATOM 4677 N N . ALA B 1 175 ? 37.740 -67.272 -2.257 1.00 92.07 ? 175 ALA B N 1 ATOM 4678 C CA . ALA B 1 175 ? 37.020 -66.016 -2.412 1.00 86.55 ? 175 ALA B CA 1 ATOM 4679 C C . ALA B 1 175 ? 36.827 -65.658 -3.892 1.00 82.03 ? 175 ALA B C 1 ATOM 4680 O O . ALA B 1 175 ? 37.744 -65.788 -4.697 1.00 83.70 ? 175 ALA B O 1 ATOM 4681 C CB . ALA B 1 175 ? 37.755 -64.904 -1.691 1.00 89.20 ? 175 ALA B CB 1 ATOM 4682 N N . VAL B 1 176 ? 35.640 -65.176 -4.235 1.00 76.57 ? 176 VAL B N 1 ATOM 4683 C CA . VAL B 1 176 ? 35.292 -64.856 -5.616 1.00 69.85 ? 176 VAL B CA 1 ATOM 4684 C C . VAL B 1 176 ? 34.749 -63.423 -5.752 1.00 69.31 ? 176 VAL B C 1 ATOM 4685 O O . VAL B 1 176 ? 33.745 -63.074 -5.140 1.00 68.85 ? 176 VAL B O 1 ATOM 4686 C CB . VAL B 1 176 ? 34.254 -65.858 -6.126 1.00 67.37 ? 176 VAL B CB 1 ATOM 4687 C CG1 . VAL B 1 176 ? 33.631 -65.398 -7.431 1.00 66.03 ? 176 VAL B CG1 1 ATOM 4688 C CG2 . VAL B 1 176 ? 34.888 -67.231 -6.276 1.00 68.14 ? 176 VAL B CG2 1 ATOM 4689 N N . GLY B 1 177 ? 35.422 -62.614 -6.569 1.00 67.33 ? 177 GLY B N 1 ATOM 4690 C CA . GLY B 1 177 ? 35.051 -61.220 -6.795 1.00 64.41 ? 177 GLY B CA 1 ATOM 4691 C C . GLY B 1 177 ? 34.181 -61.058 -8.030 1.00 62.35 ? 177 GLY B C 1 ATOM 4692 O O . GLY B 1 177 ? 34.542 -61.489 -9.116 1.00 60.66 ? 177 GLY B O 1 ATOM 4693 N N . ASN B 1 178 ? 33.036 -60.417 -7.863 1.00 63.34 ? 178 ASN B N 1 ATOM 4694 C CA . ASN B 1 178 ? 32.071 -60.305 -8.932 1.00 61.96 ? 178 ASN B CA 1 ATOM 4695 C C . ASN B 1 178 ? 32.091 -61.541 -9.806 1.00 66.51 ? 178 ASN B C 1 ATOM 4696 O O . ASN B 1 178 ? 32.370 -61.487 -11.004 1.00 69.31 ? 178 ASN B O 1 ATOM 4697 C CB . ASN B 1 178 ? 32.333 -59.058 -9.735 1.00 59.10 ? 178 ASN B CB 1 ATOM 4698 C CG . ASN B 1 178 ? 31.994 -57.827 -8.960 1.00 57.76 ? 178 ASN B CG 1 ATOM 4699 O OD1 . ASN B 1 178 ? 32.759 -57.404 -8.094 1.00 58.82 ? 178 ASN B OD1 1 ATOM 4700 N ND2 . ASN B 1 178 ? 30.829 -57.253 -9.238 1.00 57.12 ? 178 ASN B ND2 1 ATOM 4701 N N . GLY B 1 179 ? 31.790 -62.666 -9.177 1.00 69.35 ? 179 GLY B N 1 ATOM 4702 C CA . GLY B 1 179 ? 31.846 -63.945 -9.837 1.00 66.62 ? 179 GLY B CA 1 ATOM 4703 C C . GLY B 1 179 ? 30.573 -64.249 -10.575 1.00 66.58 ? 179 GLY B C 1 ATOM 4704 O O . GLY B 1 179 ? 29.525 -63.664 -10.296 1.00 64.14 ? 179 GLY B O 1 ATOM 4705 N N . LEU B 1 180 ? 30.694 -65.163 -11.532 1.00 67.68 ? 180 LEU B N 1 ATOM 4706 C CA . LEU B 1 180 ? 29.570 -65.747 -12.213 1.00 70.18 ? 180 LEU B CA 1 ATOM 4707 C C . LEU B 1 180 ? 29.274 -67.080 -11.541 1.00 68.83 ? 180 LEU B C 1 ATOM 4708 O O . LEU B 1 180 ? 29.861 -68.106 -11.877 1.00 76.55 ? 180 LEU B O 1 ATOM 4709 C CB . LEU B 1 180 ? 29.894 -65.928 -13.694 1.00 73.54 ? 180 LEU B CB 1 ATOM 4710 C CG . LEU B 1 180 ? 28.803 -66.467 -14.619 1.00 77.48 ? 180 LEU B CG 1 ATOM 4711 C CD1 . LEU B 1 180 ? 27.509 -65.698 -14.456 1.00 75.21 ? 180 LEU B CD1 1 ATOM 4712 C CD2 . LEU B 1 180 ? 29.300 -66.393 -16.062 1.00 79.83 ? 180 LEU B CD2 1 ATOM 4713 N N . SER B 1 181 ? 28.361 -67.045 -10.579 1.00 66.39 ? 181 SER B N 1 ATOM 4714 C CA . SER B 1 181 ? 27.942 -68.224 -9.833 1.00 65.76 ? 181 SER B CA 1 ATOM 4715 C C . SER B 1 181 ? 26.726 -68.912 -10.439 1.00 62.21 ? 181 SER B C 1 ATOM 4716 O O . SER B 1 181 ? 26.613 -70.139 -10.379 1.00 59.22 ? 181 SER B O 1 ATOM 4717 C CB . SER B 1 181 ? 27.654 -67.835 -8.376 1.00 70.34 ? 181 SER B CB 1 ATOM 4718 O OG . SER B 1 181 ? 28.836 -67.334 -7.740 1.00 69.39 ? 181 SER B OG 1 ATOM 4719 N N . SER B 1 182 ? 25.812 -68.125 -11.004 1.00 59.98 ? 182 SER B N 1 ATOM 4720 C CA . SER B 1 182 ? 24.625 -68.664 -11.664 1.00 63.78 ? 182 SER B CA 1 ATOM 4721 C C . SER B 1 182 ? 24.146 -67.765 -12.778 1.00 65.28 ? 182 SER B C 1 ATOM 4722 O O . SER B 1 182 ? 23.725 -66.646 -12.520 1.00 63.73 ? 182 SER B O 1 ATOM 4723 C CB . SER B 1 182 ? 23.491 -68.832 -10.660 1.00 65.96 ? 182 SER B CB 1 ATOM 4724 O OG . SER B 1 182 ? 22.236 -68.874 -11.316 1.00 68.97 ? 182 SER B OG 1 ATOM 4725 N N . TYR B 1 183 ? 24.164 -68.263 -14.009 1.00 71.50 ? 183 TYR B N 1 ATOM 4726 C CA . TYR B 1 183 ? 23.665 -67.479 -15.157 1.00 76.58 ? 183 TYR B CA 1 ATOM 4727 C C . TYR B 1 183 ? 22.234 -66.989 -14.945 1.00 76.55 ? 183 TYR B C 1 ATOM 4728 O O . TYR B 1 183 ? 21.918 -65.856 -15.285 1.00 75.17 ? 183 TYR B O 1 ATOM 4729 C CB . TYR B 1 183 ? 23.727 -68.280 -16.475 1.00 79.67 ? 183 TYR B CB 1 ATOM 4730 C CG . TYR B 1 183 ? 25.119 -68.599 -16.990 1.00 78.76 ? 183 TYR B CG 1 ATOM 4731 C CD1 . TYR B 1 183 ? 25.786 -67.736 -17.848 1.00 73.01 ? 183 TYR B CD1 1 ATOM 4732 C CD2 . TYR B 1 183 ? 25.746 -69.783 -16.633 1.00 81.40 ? 183 TYR B CD2 1 ATOM 4733 C CE1 . TYR B 1 183 ? 27.043 -68.036 -18.321 1.00 73.27 ? 183 TYR B CE1 1 ATOM 4734 C CE2 . TYR B 1 183 ? 27.005 -70.087 -17.104 1.00 78.60 ? 183 TYR B CE2 1 ATOM 4735 C CZ . TYR B 1 183 ? 27.647 -69.213 -17.946 1.00 74.50 ? 183 TYR B CZ 1 ATOM 4736 O OH . TYR B 1 183 ? 28.893 -69.538 -18.422 1.00 75.21 ? 183 TYR B OH 1 ATOM 4737 N N . GLU B 1 184 ? 21.377 -67.850 -14.396 1.00 78.44 ? 184 GLU B N 1 ATOM 4738 C CA . GLU B 1 184 ? 19.969 -67.527 -14.240 1.00 80.22 ? 184 GLU B CA 1 ATOM 4739 C C . GLU B 1 184 ? 19.775 -66.351 -13.296 1.00 79.30 ? 184 GLU B C 1 ATOM 4740 O O . GLU B 1 184 ? 19.080 -65.396 -13.637 1.00 81.27 ? 184 GLU B O 1 ATOM 4741 C CB . GLU B 1 184 ? 19.170 -68.739 -13.752 1.00 82.18 ? 184 GLU B CB 1 ATOM 4742 C CG . GLU B 1 184 ? 17.668 -68.499 -13.699 1.00 83.64 ? 184 GLU B CG 1 ATOM 4743 C CD . GLU B 1 184 ? 16.875 -69.726 -13.311 1.00 86.70 ? 184 GLU B CD 1 ATOM 4744 O OE1 . GLU B 1 184 ? 17.244 -70.840 -13.734 1.00 84.59 ? 184 GLU B OE1 1 ATOM 4745 O OE2 . GLU B 1 184 ? 15.872 -69.568 -12.588 1.00 88.81 ? 184 GLU B OE2 1 ATOM 4746 N N . GLN B 1 185 ? 20.390 -66.411 -12.122 1.00 76.01 ? 185 GLN B N 1 ATOM 4747 C CA . GLN B 1 185 ? 20.250 -65.330 -11.143 1.00 76.85 ? 185 GLN B CA 1 ATOM 4748 C C . GLN B 1 185 ? 20.943 -64.054 -11.610 1.00 74.02 ? 185 GLN B C 1 ATOM 4749 O O . GLN B 1 185 ? 20.445 -62.947 -11.390 1.00 72.64 ? 185 GLN B O 1 ATOM 4750 C CB . GLN B 1 185 ? 20.767 -65.758 -9.777 1.00 79.87 ? 185 GLN B CB 1 ATOM 4751 C CG . GLN B 1 185 ? 19.716 -66.488 -8.961 1.00 85.75 ? 185 GLN B CG 1 ATOM 4752 C CD . GLN B 1 185 ? 20.310 -67.410 -7.929 1.00 92.50 ? 185 GLN B CD 1 ATOM 4753 O OE1 . GLN B 1 185 ? 19.962 -67.349 -6.747 1.00 97.42 ? 185 GLN B OE1 1 ATOM 4754 N NE2 . GLN B 1 185 ? 21.219 -68.270 -8.367 1.00 94.69 ? 185 GLN B NE2 1 ATOM 4755 N N . ASN B 1 186 ? 22.078 -64.219 -12.275 1.00 70.22 ? 186 ASN B N 1 ATOM 4756 C CA . ASN B 1 186 ? 22.789 -63.099 -12.855 1.00 67.29 ? 186 ASN B CA 1 ATOM 4757 C C . ASN B 1 186 ? 21.904 -62.372 -13.851 1.00 68.22 ? 186 ASN B C 1 ATOM 4758 O O . ASN B 1 186 ? 21.811 -61.135 -13.826 1.00 59.78 ? 186 ASN B O 1 ATOM 4759 C CB . ASN B 1 186 ? 24.033 -63.587 -13.576 1.00 68.05 ? 186 ASN B CB 1 ATOM 4760 C CG . ASN B 1 186 ? 24.912 -62.455 -14.068 1.00 69.21 ? 186 ASN B CG 1 ATOM 4761 O OD1 . ASN B 1 186 ? 24.794 -61.323 -13.622 1.00 70.34 ? 186 ASN B OD1 1 ATOM 4762 N ND2 . ASN B 1 186 ? 25.838 -62.773 -14.962 1.00 73.47 ? 186 ASN B ND2 1 ATOM 4763 N N . ASP B 1 187 ? 21.244 -63.148 -14.716 1.00 70.82 ? 187 ASP B N 1 ATOM 4764 C CA . ASP B 1 187 ? 20.462 -62.582 -15.816 1.00 72.03 ? 187 ASP B CA 1 ATOM 4765 C C . ASP B 1 187 ? 19.172 -61.966 -15.325 1.00 69.68 ? 187 ASP B C 1 ATOM 4766 O O . ASP B 1 187 ? 18.871 -60.854 -15.697 1.00 70.07 ? 187 ASP B O 1 ATOM 4767 C CB . ASP B 1 187 ? 20.195 -63.628 -16.894 1.00 79.53 ? 187 ASP B CB 1 ATOM 4768 C CG . ASP B 1 187 ? 21.458 -64.001 -17.667 1.00 87.56 ? 187 ASP B CG 1 ATOM 4769 O OD1 . ASP B 1 187 ? 22.579 -63.758 -17.152 1.00 94.22 ? 187 ASP B OD1 1 ATOM 4770 O OD2 . ASP B 1 187 ? 21.340 -64.548 -18.781 1.00 90.77 ? 187 ASP B OD2 1 ATOM 4771 N N . ASN B 1 188 ? 18.437 -62.659 -14.459 1.00 68.10 ? 188 ASN B N 1 ATOM 4772 C CA . ASN B 1 188 ? 17.235 -62.094 -13.872 1.00 67.82 ? 188 ASN B CA 1 ATOM 4773 C C . ASN B 1 188 ? 17.551 -60.840 -13.052 1.00 67.53 ? 188 ASN B C 1 ATOM 4774 O O . ASN B 1 188 ? 16.869 -59.827 -13.192 1.00 72.60 ? 188 ASN B O 1 ATOM 4775 C CB . ASN B 1 188 ? 16.522 -63.109 -12.974 1.00 71.16 ? 188 ASN B CB 1 ATOM 4776 C CG . ASN B 1 188 ? 15.928 -64.285 -13.743 1.00 70.09 ? 188 ASN B CG 1 ATOM 4777 O OD1 . ASN B 1 188 ? 15.321 -64.125 -14.809 1.00 73.90 ? 188 ASN B OD1 1 ATOM 4778 N ND2 . ASN B 1 188 ? 16.075 -65.474 -13.182 1.00 67.00 ? 188 ASN B ND2 1 ATOM 4779 N N . SER B 1 189 ? 18.572 -60.900 -12.194 1.00 60.72 ? 189 SER B N 1 ATOM 4780 C CA . SER B 1 189 ? 18.919 -59.759 -11.330 1.00 57.76 ? 189 SER B CA 1 ATOM 4781 C C . SER B 1 189 ? 19.424 -58.544 -12.113 1.00 56.07 ? 189 SER B C 1 ATOM 4782 O O . SER B 1 189 ? 19.160 -57.411 -11.741 1.00 60.80 ? 189 SER B O 1 ATOM 4783 C CB . SER B 1 189 ? 19.935 -60.164 -10.250 1.00 56.90 ? 189 SER B CB 1 ATOM 4784 O OG . SER B 1 189 ? 21.173 -60.606 -10.789 1.00 54.32 ? 189 SER B OG 1 ATOM 4785 N N . LEU B 1 190 ? 20.165 -58.771 -13.186 1.00 57.12 ? 190 LEU B N 1 ATOM 4786 C CA . LEU B 1 190 ? 20.665 -57.689 -14.039 1.00 56.65 ? 190 LEU B CA 1 ATOM 4787 C C . LEU B 1 190 ? 19.532 -56.847 -14.575 1.00 60.10 ? 190 LEU B C 1 ATOM 4788 O O . LEU B 1 190 ? 19.646 -55.631 -14.672 1.00 62.80 ? 190 LEU B O 1 ATOM 4789 C CB . LEU B 1 190 ? 21.463 -58.251 -15.216 1.00 57.43 ? 190 LEU B CB 1 ATOM 4790 C CG . LEU B 1 190 ? 22.100 -57.276 -16.206 1.00 59.47 ? 190 LEU B CG 1 ATOM 4791 C CD1 . LEU B 1 190 ? 22.758 -56.114 -15.477 1.00 59.83 ? 190 LEU B CD1 1 ATOM 4792 C CD2 . LEU B 1 190 ? 23.114 -58.004 -17.088 1.00 58.71 ? 190 LEU B CD2 1 ATOM 4793 N N . VAL B 1 191 ? 18.429 -57.485 -14.932 1.00 63.28 ? 191 VAL B N 1 ATOM 4794 C CA . VAL B 1 191 ? 17.334 -56.765 -15.545 1.00 62.20 ? 191 VAL B CA 1 ATOM 4795 C C . VAL B 1 191 ? 16.684 -55.842 -14.534 1.00 61.79 ? 191 VAL B C 1 ATOM 4796 O O . VAL B 1 191 ? 16.438 -54.677 -14.845 1.00 67.15 ? 191 VAL B O 1 ATOM 4797 C CB . VAL B 1 191 ? 16.330 -57.717 -16.167 1.00 64.58 ? 191 VAL B CB 1 ATOM 4798 C CG1 . VAL B 1 191 ? 15.175 -56.943 -16.767 1.00 65.56 ? 191 VAL B CG1 1 ATOM 4799 C CG2 . VAL B 1 191 ? 17.032 -58.547 -17.236 1.00 65.94 ? 191 VAL B CG2 1 ATOM 4800 N N . TYR B 1 192 ? 16.444 -56.330 -13.318 1.00 61.17 ? 192 TYR B N 1 ATOM 4801 C CA . TYR B 1 192 ? 16.015 -55.455 -12.218 1.00 61.79 ? 192 TYR B CA 1 ATOM 4802 C C . TYR B 1 192 ? 17.067 -54.365 -12.006 1.00 58.59 ? 192 TYR B C 1 ATOM 4803 O O . TYR B 1 192 ? 16.754 -53.190 -11.884 1.00 53.37 ? 192 TYR B O 1 ATOM 4804 C CB . TYR B 1 192 ? 15.812 -56.227 -10.914 1.00 64.39 ? 192 TYR B CB 1 ATOM 4805 C CG . TYR B 1 192 ? 14.555 -57.086 -10.833 1.00 68.75 ? 192 TYR B CG 1 ATOM 4806 C CD1 . TYR B 1 192 ? 14.529 -58.368 -11.352 1.00 70.97 ? 192 TYR B CD1 1 ATOM 4807 C CD2 . TYR B 1 192 ? 13.414 -56.625 -10.199 1.00 72.75 ? 192 TYR B CD2 1 ATOM 4808 C CE1 . TYR B 1 192 ? 13.399 -59.153 -11.267 1.00 74.47 ? 192 TYR B CE1 1 ATOM 4809 C CE2 . TYR B 1 192 ? 12.277 -57.405 -10.099 1.00 75.72 ? 192 TYR B CE2 1 ATOM 4810 C CZ . TYR B 1 192 ? 12.280 -58.672 -10.634 1.00 78.14 ? 192 TYR B CZ 1 ATOM 4811 O OH . TYR B 1 192 ? 11.158 -59.460 -10.545 1.00 82.97 ? 192 TYR B OH 1 ATOM 4812 N N . PHE B 1 193 ? 18.326 -54.764 -11.989 1.00 57.54 ? 193 PHE B N 1 ATOM 4813 C CA . PHE B 1 193 ? 19.399 -53.813 -11.792 1.00 57.32 ? 193 PHE B CA 1 ATOM 4814 C C . PHE B 1 193 ? 19.244 -52.672 -12.779 1.00 58.85 ? 193 PHE B C 1 ATOM 4815 O O . PHE B 1 193 ? 19.265 -51.513 -12.395 1.00 60.10 ? 193 PHE B O 1 ATOM 4816 C CB . PHE B 1 193 ? 20.734 -54.479 -11.991 1.00 56.24 ? 193 PHE B CB 1 ATOM 4817 C CG . PHE B 1 193 ? 21.896 -53.632 -11.605 1.00 57.70 ? 193 PHE B CG 1 ATOM 4818 C CD1 . PHE B 1 193 ? 22.376 -52.664 -12.466 1.00 59.59 ? 193 PHE B CD1 1 ATOM 4819 C CD2 . PHE B 1 193 ? 22.543 -53.837 -10.401 1.00 58.30 ? 193 PHE B CD2 1 ATOM 4820 C CE1 . PHE B 1 193 ? 23.471 -51.907 -12.135 1.00 59.20 ? 193 PHE B CE1 1 ATOM 4821 C CE2 . PHE B 1 193 ? 23.623 -53.076 -10.054 1.00 58.05 ? 193 PHE B CE2 1 ATOM 4822 C CZ . PHE B 1 193 ? 24.094 -52.110 -10.928 1.00 60.94 ? 193 PHE B CZ 1 ATOM 4823 N N . ALA B 1 194 ? 19.061 -53.015 -14.050 1.00 59.45 ? 194 ALA B N 1 ATOM 4824 C CA . ALA B 1 194 ? 19.012 -52.031 -15.115 1.00 56.63 ? 194 ALA B CA 1 ATOM 4825 C C . ALA B 1 194 ? 17.877 -51.063 -14.884 1.00 55.55 ? 194 ALA B C 1 ATOM 4826 O O . ALA B 1 194 ? 18.054 -49.867 -15.047 1.00 59.34 ? 194 ALA B O 1 ATOM 4827 C CB . ALA B 1 194 ? 18.874 -52.718 -16.476 1.00 59.22 ? 194 ALA B CB 1 ATOM 4828 N N . TYR B 1 195 ? 16.705 -51.559 -14.515 1.00 55.98 ? 195 TYR B N 1 ATOM 4829 C CA . TYR B 1 195 ? 15.549 -50.661 -14.347 1.00 60.25 ? 195 TYR B CA 1 ATOM 4830 C C . TYR B 1 195 ? 15.760 -49.698 -13.210 1.00 59.48 ? 195 TYR B C 1 ATOM 4831 O O . TYR B 1 195 ? 15.590 -48.487 -13.371 1.00 64.37 ? 195 TYR B O 1 ATOM 4832 C CB . TYR B 1 195 ? 14.240 -51.429 -14.123 1.00 62.51 ? 195 TYR B CB 1 ATOM 4833 C CG . TYR B 1 195 ? 13.047 -50.537 -13.810 1.00 65.87 ? 195 TYR B CG 1 ATOM 4834 C CD1 . TYR B 1 195 ? 12.662 -49.510 -14.671 1.00 68.36 ? 195 TYR B CD1 1 ATOM 4835 C CD2 . TYR B 1 195 ? 12.303 -50.722 -12.641 1.00 69.28 ? 195 TYR B CD2 1 ATOM 4836 C CE1 . TYR B 1 195 ? 11.572 -48.698 -14.379 1.00 69.77 ? 195 TYR B CE1 1 ATOM 4837 C CE2 . TYR B 1 195 ? 11.214 -49.923 -12.343 1.00 69.34 ? 195 TYR B CE2 1 ATOM 4838 C CZ . TYR B 1 195 ? 10.850 -48.915 -13.212 1.00 71.59 ? 195 TYR B CZ 1 ATOM 4839 O OH . TYR B 1 195 ? 9.756 -48.142 -12.913 1.00 74.71 ? 195 TYR B OH 1 ATOM 4840 N N . TYR B 1 196 ? 16.150 -50.247 -12.064 1.00 59.76 ? 196 TYR B N 1 ATOM 4841 C CA . TYR B 1 196 ? 16.227 -49.487 -10.829 1.00 58.48 ? 196 TYR B CA 1 ATOM 4842 C C . TYR B 1 196 ? 17.468 -48.618 -10.734 1.00 59.25 ? 196 TYR B C 1 ATOM 4843 O O . TYR B 1 196 ? 17.553 -47.782 -9.825 1.00 63.50 ? 196 TYR B O 1 ATOM 4844 C CB . TYR B 1 196 ? 16.082 -50.410 -9.624 1.00 59.80 ? 196 TYR B CB 1 ATOM 4845 C CG . TYR B 1 196 ? 14.680 -50.965 -9.505 1.00 60.49 ? 196 TYR B CG 1 ATOM 4846 C CD1 . TYR B 1 196 ? 13.645 -50.181 -9.030 1.00 61.53 ? 196 TYR B CD1 1 ATOM 4847 C CD2 . TYR B 1 196 ? 14.391 -52.264 -9.876 1.00 58.56 ? 196 TYR B CD2 1 ATOM 4848 C CE1 . TYR B 1 196 ? 12.358 -50.681 -8.930 1.00 61.31 ? 196 TYR B CE1 1 ATOM 4849 C CE2 . TYR B 1 196 ? 13.117 -52.765 -9.775 1.00 60.20 ? 196 TYR B CE2 1 ATOM 4850 C CZ . TYR B 1 196 ? 12.103 -51.974 -9.305 1.00 61.12 ? 196 TYR B CZ 1 ATOM 4851 O OH . TYR B 1 196 ? 10.835 -52.502 -9.235 1.00 61.97 ? 196 TYR B OH 1 ATOM 4852 N N . HIS B 1 197 ? 18.394 -48.781 -11.678 1.00 56.08 ? 197 HIS B N 1 ATOM 4853 C CA . HIS B 1 197 ? 19.512 -47.855 -11.846 1.00 54.18 ? 197 HIS B CA 1 ATOM 4854 C C . HIS B 1 197 ? 19.290 -46.927 -13.011 1.00 55.48 ? 197 HIS B C 1 ATOM 4855 O O . HIS B 1 197 ? 20.218 -46.253 -13.439 1.00 57.49 ? 197 HIS B O 1 ATOM 4856 C CB . HIS B 1 197 ? 20.816 -48.600 -12.069 1.00 54.34 ? 197 HIS B CB 1 ATOM 4857 C CG . HIS B 1 197 ? 21.325 -49.283 -10.853 1.00 54.73 ? 197 HIS B CG 1 ATOM 4858 N ND1 . HIS B 1 197 ? 20.708 -50.384 -10.318 1.00 57.83 ? 197 HIS B ND1 1 ATOM 4859 C CD2 . HIS B 1 197 ? 22.394 -49.033 -10.070 1.00 56.18 ? 197 HIS B CD2 1 ATOM 4860 C CE1 . HIS B 1 197 ? 21.363 -50.776 -9.244 1.00 59.55 ? 197 HIS B CE1 1 ATOM 4861 N NE2 . HIS B 1 197 ? 22.394 -49.975 -9.073 1.00 59.82 ? 197 HIS B NE2 1 ATOM 4862 N N . GLY B 1 198 ? 18.064 -46.874 -13.529 1.00 58.05 ? 198 GLY B N 1 ATOM 4863 C CA . GLY B 1 198 ? 17.630 -45.754 -14.387 1.00 57.14 ? 198 GLY B CA 1 ATOM 4864 C C . GLY B 1 198 ? 17.932 -45.883 -15.868 1.00 58.35 ? 198 GLY B C 1 ATOM 4865 O O . GLY B 1 198 ? 17.950 -44.887 -16.593 1.00 56.03 ? 198 GLY B O 1 ATOM 4866 N N . LEU B 1 199 ? 18.102 -47.110 -16.332 1.00 59.00 ? 199 LEU B N 1 ATOM 4867 C CA . LEU B 1 199 ? 18.497 -47.348 -17.708 1.00 60.37 ? 199 LEU B CA 1 ATOM 4868 C C . LEU B 1 199 ? 17.323 -47.730 -18.613 1.00 64.96 ? 199 LEU B C 1 ATOM 4869 O O . LEU B 1 199 ? 17.480 -47.762 -19.841 1.00 71.40 ? 199 LEU B O 1 ATOM 4870 C CB . LEU B 1 199 ? 19.562 -48.454 -17.752 1.00 58.39 ? 199 LEU B CB 1 ATOM 4871 C CG . LEU B 1 199 ? 20.628 -48.491 -16.650 1.00 58.24 ? 199 LEU B CG 1 ATOM 4872 C CD1 . LEU B 1 199 ? 21.636 -49.582 -16.926 1.00 57.39 ? 199 LEU B CD1 1 ATOM 4873 C CD2 . LEU B 1 199 ? 21.338 -47.158 -16.509 1.00 60.50 ? 199 LEU B CD2 1 ATOM 4874 N N . LEU B 1 200 ? 16.165 -48.039 -18.034 1.00 67.13 ? 200 LEU B N 1 ATOM 4875 C CA . LEU B 1 200 ? 15.089 -48.714 -18.789 1.00 68.65 ? 200 LEU B CA 1 ATOM 4876 C C . LEU B 1 200 ? 13.815 -47.916 -18.981 1.00 68.83 ? 200 LEU B C 1 ATOM 4877 O O . LEU B 1 200 ? 13.212 -47.961 -20.045 1.00 75.63 ? 200 LEU B O 1 ATOM 4878 C CB . LEU B 1 200 ? 14.717 -50.035 -18.118 1.00 66.91 ? 200 LEU B CB 1 ATOM 4879 C CG . LEU B 1 200 ? 15.762 -51.140 -18.037 1.00 67.56 ? 200 LEU B CG 1 ATOM 4880 C CD1 . LEU B 1 200 ? 15.045 -52.470 -17.876 1.00 70.58 ? 200 LEU B CD1 1 ATOM 4881 C CD2 . LEU B 1 200 ? 16.662 -51.193 -19.262 1.00 70.50 ? 200 LEU B CD2 1 ATOM 4882 N N . GLY B 1 201 ? 13.366 -47.240 -17.941 1.00 68.22 ? 201 GLY B N 1 ATOM 4883 C CA . GLY B 1 201 ? 12.120 -46.510 -18.024 1.00 67.16 ? 201 GLY B CA 1 ATOM 4884 C C . GLY B 1 201 ? 10.925 -47.431 -17.992 1.00 68.37 ? 201 GLY B C 1 ATOM 4885 O O . GLY B 1 201 ? 11.056 -48.652 -18.093 1.00 68.54 ? 201 GLY B O 1 ATOM 4886 N N . ASN B 1 202 ? 9.748 -46.825 -17.888 1.00 72.72 ? 202 ASN B N 1 ATOM 4887 C CA . ASN B 1 202 ? 8.535 -47.534 -17.527 1.00 76.80 ? 202 ASN B CA 1 ATOM 4888 C C . ASN B 1 202 ? 7.836 -48.296 -18.657 1.00 80.34 ? 202 ASN B C 1 ATOM 4889 O O . ASN B 1 202 ? 7.238 -49.346 -18.416 1.00 79.39 ? 202 ASN B O 1 ATOM 4890 C CB . ASN B 1 202 ? 7.561 -46.557 -16.896 1.00 79.20 ? 202 ASN B CB 1 ATOM 4891 C CG . ASN B 1 202 ? 6.408 -47.256 -16.208 1.00 87.47 ? 202 ASN B CG 1 ATOM 4892 O OD1 . ASN B 1 202 ? 5.239 -47.063 -16.580 1.00 88.72 ? 202 ASN B OD1 1 ATOM 4893 N ND2 . ASN B 1 202 ? 6.728 -48.096 -15.211 1.00 83.90 ? 202 ASN B ND2 1 ATOM 4894 N N . ARG B 1 203 ? 7.870 -47.772 -19.878 1.00 83.35 ? 203 ARG B N 1 ATOM 4895 C CA . ARG B 1 203 ? 7.257 -48.480 -20.997 1.00 86.98 ? 203 ARG B CA 1 ATOM 4896 C C . ARG B 1 203 ? 7.953 -49.820 -21.168 1.00 80.67 ? 203 ARG B C 1 ATOM 4897 O O . ARG B 1 203 ? 7.314 -50.857 -21.214 1.00 75.88 ? 203 ARG B O 1 ATOM 4898 C CB . ARG B 1 203 ? 7.319 -47.669 -22.292 1.00 95.16 ? 203 ARG B CB 1 ATOM 4899 C CG . ARG B 1 203 ? 6.423 -46.438 -22.300 1.00 106.25 ? 203 ARG B CG 1 ATOM 4900 C CD . ARG B 1 203 ? 6.093 -45.983 -23.717 1.00 118.07 ? 203 ARG B CD 1 ATOM 4901 N NE . ARG B 1 203 ? 5.684 -44.576 -23.776 1.00 132.84 ? 203 ARG B NE 1 ATOM 4902 C CZ . ARG B 1 203 ? 4.498 -44.096 -23.389 1.00 139.48 ? 203 ARG B CZ 1 ATOM 4903 N NH1 . ARG B 1 203 ? 3.556 -44.887 -22.891 1.00 139.89 ? 203 ARG B NH1 1 ATOM 4904 N NH2 . ARG B 1 203 ? 4.250 -42.798 -23.501 1.00 140.44 ? 203 ARG B NH2 1 ATOM 4905 N N . LEU B 1 204 ? 9.271 -49.790 -21.221 1.00 80.70 ? 204 LEU B N 1 ATOM 4906 C CA . LEU B 1 204 ? 10.049 -51.018 -21.352 1.00 83.45 ? 204 LEU B CA 1 ATOM 4907 C C . LEU B 1 204 ? 9.916 -51.912 -20.116 1.00 85.65 ? 204 LEU B C 1 ATOM 4908 O O . LEU B 1 204 ? 9.709 -53.119 -20.262 1.00 92.79 ? 204 LEU B O 1 ATOM 4909 C CB . LEU B 1 204 ? 11.520 -50.711 -21.638 1.00 81.17 ? 204 LEU B CB 1 ATOM 4910 C CG . LEU B 1 204 ? 12.487 -51.893 -21.724 1.00 79.66 ? 204 LEU B CG 1 ATOM 4911 C CD1 . LEU B 1 204 ? 12.039 -52.902 -22.755 1.00 82.06 ? 204 LEU B CD1 1 ATOM 4912 C CD2 . LEU B 1 204 ? 13.888 -51.411 -22.042 1.00 78.99 ? 204 LEU B CD2 1 ATOM 4913 N N . TRP B 1 205 ? 10.005 -51.335 -18.912 1.00 78.23 ? 205 TRP B N 1 ATOM 4914 C CA . TRP B 1 205 ? 9.747 -52.112 -17.701 1.00 75.31 ? 205 TRP B CA 1 ATOM 4915 C C . TRP B 1 205 ? 8.368 -52.793 -17.760 1.00 75.08 ? 205 TRP B C 1 ATOM 4916 O O . TRP B 1 205 ? 8.266 -53.976 -17.528 1.00 73.39 ? 205 TRP B O 1 ATOM 4917 C CB . TRP B 1 205 ? 9.890 -51.249 -16.442 1.00 74.87 ? 205 TRP B CB 1 ATOM 4918 C CG . TRP B 1 205 ? 9.809 -52.020 -15.130 1.00 74.32 ? 205 TRP B CG 1 ATOM 4919 C CD1 . TRP B 1 205 ? 8.927 -51.804 -14.117 1.00 77.25 ? 205 TRP B CD1 1 ATOM 4920 C CD2 . TRP B 1 205 ? 10.625 -53.118 -14.713 1.00 70.86 ? 205 TRP B CD2 1 ATOM 4921 N NE1 . TRP B 1 205 ? 9.149 -52.688 -13.090 1.00 76.04 ? 205 TRP B NE1 1 ATOM 4922 C CE2 . TRP B 1 205 ? 10.183 -53.509 -13.436 1.00 73.28 ? 205 TRP B CE2 1 ATOM 4923 C CE3 . TRP B 1 205 ? 11.691 -53.798 -15.287 1.00 72.74 ? 205 TRP B CE3 1 ATOM 4924 C CZ2 . TRP B 1 205 ? 10.766 -54.553 -12.728 1.00 74.33 ? 205 TRP B CZ2 1 ATOM 4925 C CZ3 . TRP B 1 205 ? 12.271 -54.848 -14.581 1.00 72.45 ? 205 TRP B CZ3 1 ATOM 4926 C CH2 . TRP B 1 205 ? 11.810 -55.207 -13.315 1.00 71.99 ? 205 TRP B CH2 1 ATOM 4927 N N . SER B 1 206 ? 7.319 -52.058 -18.099 1.00 78.42 ? 206 SER B N 1 ATOM 4928 C CA . SER B 1 206 ? 5.991 -52.654 -18.224 1.00 85.03 ? 206 SER B CA 1 ATOM 4929 C C . SER B 1 206 ? 5.979 -53.815 -19.194 1.00 86.76 ? 206 SER B C 1 ATOM 4930 O O . SER B 1 206 ? 5.426 -54.872 -18.890 1.00 91.30 ? 206 SER B O 1 ATOM 4931 C CB . SER B 1 206 ? 4.964 -51.639 -18.711 1.00 90.67 ? 206 SER B CB 1 ATOM 4932 O OG . SER B 1 206 ? 4.656 -50.709 -17.701 1.00 99.00 ? 206 SER B OG 1 ATOM 4933 N N . SER B 1 207 ? 6.568 -53.619 -20.368 1.00 83.51 ? 207 SER B N 1 ATOM 4934 C CA . SER B 1 207 ? 6.551 -54.651 -21.387 1.00 83.71 ? 207 SER B CA 1 ATOM 4935 C C . SER B 1 207 ? 7.205 -55.894 -20.809 1.00 82.36 ? 207 SER B C 1 ATOM 4936 O O . SER B 1 207 ? 6.630 -56.970 -20.832 1.00 88.48 ? 207 SER B O 1 ATOM 4937 C CB . SER B 1 207 ? 7.274 -54.206 -22.653 1.00 83.93 ? 207 SER B CB 1 ATOM 4938 O OG . SER B 1 207 ? 6.634 -53.108 -23.267 1.00 82.31 ? 207 SER B OG 1 ATOM 4939 N N . LEU B 1 208 ? 8.400 -55.722 -20.275 1.00 78.64 ? 208 LEU B N 1 ATOM 4940 C CA . LEU B 1 208 ? 9.142 -56.812 -19.663 1.00 78.11 ? 208 LEU B CA 1 ATOM 4941 C C . LEU B 1 208 ? 8.307 -57.584 -18.640 1.00 80.88 ? 208 LEU B C 1 ATOM 4942 O O . LEU B 1 208 ? 8.172 -58.795 -18.758 1.00 85.87 ? 208 LEU B O 1 ATOM 4943 C CB . LEU B 1 208 ? 10.419 -56.275 -19.027 1.00 74.67 ? 208 LEU B CB 1 ATOM 4944 C CG . LEU B 1 208 ? 11.506 -55.903 -20.037 1.00 75.40 ? 208 LEU B CG 1 ATOM 4945 C CD1 . LEU B 1 208 ? 12.470 -54.866 -19.475 1.00 75.41 ? 208 LEU B CD1 1 ATOM 4946 C CD2 . LEU B 1 208 ? 12.269 -57.140 -20.498 1.00 74.90 ? 208 LEU B CD2 1 ATOM 4947 N N . GLN B 1 209 ? 7.724 -56.882 -17.671 1.00 81.93 ? 209 GLN B N 1 ATOM 4948 C CA . GLN B 1 209 ? 6.801 -57.482 -16.698 1.00 83.83 ? 209 GLN B CA 1 ATOM 4949 C C . GLN B 1 209 ? 5.684 -58.266 -17.391 1.00 88.13 ? 209 GLN B C 1 ATOM 4950 O O . GLN B 1 209 ? 5.390 -59.412 -17.041 1.00 86.68 ? 209 GLN B O 1 ATOM 4951 C CB . GLN B 1 209 ? 6.161 -56.395 -15.820 1.00 84.51 ? 209 GLN B CB 1 ATOM 4952 C CG . GLN B 1 209 ? 7.079 -55.767 -14.777 1.00 82.97 ? 209 GLN B CG 1 ATOM 4953 C CD . GLN B 1 209 ? 7.350 -56.682 -13.583 1.00 84.02 ? 209 GLN B CD 1 ATOM 4954 O OE1 . GLN B 1 209 ? 6.450 -56.944 -12.793 1.00 82.27 ? 209 GLN B OE1 1 ATOM 4955 N NE2 . GLN B 1 209 ? 8.585 -57.177 -13.453 1.00 83.30 ? 209 GLN B NE2 1 ATOM 4956 N N . THR B 1 210 ? 5.047 -57.620 -18.361 1.00 89.28 ? 210 THR B N 1 ATOM 4957 C CA . THR B 1 210 ? 3.929 -58.209 -19.077 1.00 94.75 ? 210 THR B CA 1 ATOM 4958 C C . THR B 1 210 ? 4.290 -59.535 -19.736 1.00 94.73 ? 210 THR B C 1 ATOM 4959 O O . THR B 1 210 ? 3.585 -60.527 -19.544 1.00 102.92 ? 210 THR B O 1 ATOM 4960 C CB . THR B 1 210 ? 3.423 -57.254 -20.168 1.00 97.45 ? 210 THR B CB 1 ATOM 4961 O OG1 . THR B 1 210 ? 2.865 -56.092 -19.558 1.00 102.04 ? 210 THR B OG1 1 ATOM 4962 C CG2 . THR B 1 210 ? 2.374 -57.903 -21.001 1.00 100.17 ? 210 THR B CG2 1 ATOM 4963 N N . HIS B 1 211 ? 5.375 -59.538 -20.505 1.00 88.53 ? 211 HIS B N 1 ATOM 4964 C CA . HIS B 1 211 ? 5.723 -60.660 -21.368 1.00 91.85 ? 211 HIS B CA 1 ATOM 4965 C C . HIS B 1 211 ? 6.654 -61.679 -20.732 1.00 90.20 ? 211 HIS B C 1 ATOM 4966 O O . HIS B 1 211 ? 6.669 -62.848 -21.126 1.00 96.38 ? 211 HIS B O 1 ATOM 4967 C CB . HIS B 1 211 ? 6.360 -60.142 -22.654 1.00 95.96 ? 211 HIS B CB 1 ATOM 4968 C CG . HIS B 1 211 ? 5.515 -59.151 -23.391 1.00 101.01 ? 211 HIS B CG 1 ATOM 4969 N ND1 . HIS B 1 211 ? 6.040 -58.048 -24.018 1.00 101.54 ? 211 HIS B ND1 1 ATOM 4970 C CD2 . HIS B 1 211 ? 4.179 -59.091 -23.589 1.00 105.83 ? 211 HIS B CD2 1 ATOM 4971 C CE1 . HIS B 1 211 ? 5.067 -57.353 -24.578 1.00 103.64 ? 211 HIS B CE1 1 ATOM 4972 N NE2 . HIS B 1 211 ? 3.926 -57.965 -24.332 1.00 105.69 ? 211 HIS B NE2 1 ATOM 4973 N N . CYS B 1 212 ? 7.436 -61.251 -19.756 1.00 86.27 ? 212 CYS B N 1 ATOM 4974 C CA . CYS B 1 212 ? 8.409 -62.125 -19.145 1.00 84.84 ? 212 CYS B CA 1 ATOM 4975 C C . CYS B 1 212 ? 8.028 -62.564 -17.758 1.00 87.30 ? 212 CYS B C 1 ATOM 4976 O O . CYS B 1 212 ? 8.760 -63.337 -17.149 1.00 89.95 ? 212 CYS B O 1 ATOM 4977 C CB . CYS B 1 212 ? 9.750 -61.415 -19.050 1.00 83.24 ? 212 CYS B CB 1 ATOM 4978 S SG . CYS B 1 212 ? 10.315 -60.682 -20.590 1.00 79.85 ? 212 CYS B SG 1 ATOM 4979 N N . CYS B 1 213 ? 6.921 -62.058 -17.231 1.00 91.89 ? 213 CYS B N 1 ATOM 4980 C CA . CYS B 1 213 ? 6.599 -62.290 -15.828 1.00 95.86 ? 213 CYS B CA 1 ATOM 4981 C C . CYS B 1 213 ? 5.124 -62.516 -15.629 1.00 99.00 ? 213 CYS B C 1 ATOM 4982 O O . CYS B 1 213 ? 4.299 -61.758 -16.120 1.00 104.51 ? 213 CYS B O 1 ATOM 4983 C CB . CYS B 1 213 ? 7.039 -61.114 -14.953 1.00 96.96 ? 213 CYS B CB 1 ATOM 4984 S SG . CYS B 1 213 ? 8.653 -60.391 -15.344 1.00 97.30 ? 213 CYS B SG 1 ATOM 4985 N N . SER B 1 214 ? 4.796 -63.562 -14.891 1.00 102.27 ? 214 SER B N 1 ATOM 4986 C CA . SER B 1 214 ? 3.429 -63.798 -14.472 1.00 108.84 ? 214 SER B CA 1 ATOM 4987 C C . SER B 1 214 ? 3.394 -63.865 -12.953 1.00 108.80 ? 214 SER B C 1 ATOM 4988 O O . SER B 1 214 ? 4.135 -64.635 -12.349 1.00 103.77 ? 214 SER B O 1 ATOM 4989 C CB . SER B 1 214 ? 2.893 -65.095 -15.069 1.00 113.39 ? 214 SER B CB 1 ATOM 4990 O OG . SER B 1 214 ? 3.496 -66.231 -14.482 1.00 114.51 ? 214 SER B OG 1 ATOM 4991 N N . GLN B 1 215 ? 2.553 -63.033 -12.349 1.00 110.92 ? 215 GLN B N 1 ATOM 4992 C CA . GLN B 1 215 ? 2.250 -63.119 -10.916 1.00 111.29 ? 215 GLN B CA 1 ATOM 4993 C C . GLN B 1 215 ? 3.502 -62.963 -10.056 1.00 107.31 ? 215 GLN B C 1 ATOM 4994 O O . GLN B 1 215 ? 3.706 -63.667 -9.060 1.00 102.06 ? 215 GLN B O 1 ATOM 4995 C CB . GLN B 1 215 ? 1.524 -64.423 -10.573 1.00 114.60 ? 215 GLN B CB 1 ATOM 4996 C CG . GLN B 1 215 ? 0.304 -64.721 -11.429 1.00 115.13 ? 215 GLN B CG 1 ATOM 4997 C CD . GLN B 1 215 ? -0.614 -65.747 -10.784 1.00 117.67 ? 215 GLN B CD 1 ATOM 4998 O OE1 . GLN B 1 215 ? -1.829 -65.565 -10.703 1.00 122.97 ? 215 GLN B OE1 1 ATOM 4999 N NE2 . GLN B 1 215 ? -0.029 -66.834 -10.315 1.00 116.30 ? 215 GLN B NE2 1 ATOM 5000 N N . ASN B 1 216 ? 4.344 -62.036 -10.479 1.00 110.35 ? 216 ASN B N 1 ATOM 5001 C CA . ASN B 1 216 ? 5.489 -61.571 -9.689 1.00 112.33 ? 216 ASN B CA 1 ATOM 5002 C C . ASN B 1 216 ? 6.605 -62.569 -9.472 1.00 109.49 ? 216 ASN B C 1 ATOM 5003 O O . ASN B 1 216 ? 7.245 -62.543 -8.428 1.00 109.24 ? 216 ASN B O 1 ATOM 5004 C CB . ASN B 1 216 ? 5.020 -61.020 -8.337 1.00 112.14 ? 216 ASN B CB 1 ATOM 5005 C CG . ASN B 1 216 ? 3.887 -60.035 -8.492 1.00 108.32 ? 216 ASN B CG 1 ATOM 5006 O OD1 . ASN B 1 216 ? 3.954 -59.163 -9.346 1.00 99.65 ? 216 ASN B OD1 1 ATOM 5007 N ND2 . ASN B 1 216 ? 2.816 -60.198 -7.709 1.00 110.21 ? 216 ASN B ND2 1 ATOM 5008 N N . LYS B 1 217 ? 6.822 -63.439 -10.454 1.00 107.42 ? 217 LYS B N 1 ATOM 5009 C CA . LYS B 1 217 ? 8.069 -64.175 -10.569 1.00 106.40 ? 217 LYS B CA 1 ATOM 5010 C C . LYS B 1 217 ? 8.417 -64.182 -12.046 1.00 105.04 ? 217 LYS B C 1 ATOM 5011 O O . LYS B 1 217 ? 7.649 -64.672 -12.877 1.00 106.84 ? 217 LYS B O 1 ATOM 5012 C CB . LYS B 1 217 ? 7.999 -65.579 -9.962 1.00 112.48 ? 217 LYS B CB 1 ATOM 5013 C CG . LYS B 1 217 ? 9.365 -66.145 -9.580 1.00 116.52 ? 217 LYS B CG 1 ATOM 5014 C CD . LYS B 1 217 ? 9.275 -67.284 -8.579 1.00 120.02 ? 217 LYS B CD 1 ATOM 5015 C CE . LYS B 1 217 ? 8.587 -68.489 -9.161 1.00 122.82 ? 217 LYS B CE 1 ATOM 5016 N NZ . LYS B 1 217 ? 9.481 -69.324 -9.998 1.00 121.40 ? 217 LYS B NZ 1 ATOM 5017 N N . CYS B 1 218 ? 9.565 -63.584 -12.358 1.00 101.12 ? 218 CYS B N 1 ATOM 5018 C CA . CYS B 1 218 ? 9.951 -63.268 -13.723 1.00 93.28 ? 218 CYS B CA 1 ATOM 5019 C C . CYS B 1 218 ? 10.851 -64.350 -14.262 1.00 89.45 ? 218 CYS B C 1 ATOM 5020 O O . CYS B 1 218 ? 11.593 -64.981 -13.511 1.00 85.74 ? 218 CYS B O 1 ATOM 5021 C CB . CYS B 1 218 ? 10.701 -61.931 -13.776 1.00 93.44 ? 218 CYS B CB 1 ATOM 5022 S SG . CYS B 1 218 ? 9.676 -60.466 -13.574 1.00 96.78 ? 218 CYS B SG 1 ATOM 5023 N N . ASN B 1 219 ? 10.779 -64.571 -15.567 1.00 86.63 ? 219 ASN B N 1 ATOM 5024 C CA . ASN B 1 219 ? 11.804 -65.333 -16.242 1.00 83.43 ? 219 ASN B CA 1 ATOM 5025 C C . ASN B 1 219 ? 12.442 -64.432 -17.280 1.00 84.03 ? 219 ASN B C 1 ATOM 5026 O O . ASN B 1 219 ? 11.878 -64.218 -18.346 1.00 87.76 ? 219 ASN B O 1 ATOM 5027 C CB . ASN B 1 219 ? 11.240 -66.597 -16.887 1.00 81.72 ? 219 ASN B CB 1 ATOM 5028 C CG . ASN B 1 219 ? 12.317 -67.442 -17.525 1.00 78.22 ? 219 ASN B CG 1 ATOM 5029 O OD1 . ASN B 1 219 ? 13.502 -67.164 -17.381 1.00 75.07 ? 219 ASN B OD1 1 ATOM 5030 N ND2 . ASN B 1 219 ? 11.911 -68.466 -18.251 1.00 79.14 ? 219 ASN B ND2 1 ATOM 5031 N N . PHE B 1 220 ? 13.593 -63.867 -16.938 1.00 81.20 ? 220 PHE B N 1 ATOM 5032 C CA . PHE B 1 220 ? 14.399 -63.131 -17.896 1.00 80.63 ? 220 PHE B CA 1 ATOM 5033 C C . PHE B 1 220 ? 15.549 -63.999 -18.359 1.00 82.83 ? 220 PHE B C 1 ATOM 5034 O O . PHE B 1 220 ? 16.383 -63.544 -19.138 1.00 83.05 ? 220 PHE B O 1 ATOM 5035 C CB . PHE B 1 220 ? 14.954 -61.840 -17.290 1.00 77.99 ? 220 PHE B CB 1 ATOM 5036 C CG . PHE B 1 220 ? 13.902 -60.885 -16.818 1.00 77.13 ? 220 PHE B CG 1 ATOM 5037 C CD1 . PHE B 1 220 ? 12.874 -60.498 -17.653 1.00 76.10 ? 220 PHE B CD1 1 ATOM 5038 C CD2 . PHE B 1 220 ? 13.950 -60.359 -15.534 1.00 74.46 ? 220 PHE B CD2 1 ATOM 5039 C CE1 . PHE B 1 220 ? 11.917 -59.617 -17.210 1.00 73.48 ? 220 PHE B CE1 1 ATOM 5040 C CE2 . PHE B 1 220 ? 12.989 -59.485 -15.087 1.00 72.38 ? 220 PHE B CE2 1 ATOM 5041 C CZ . PHE B 1 220 ? 11.970 -59.115 -15.929 1.00 72.54 ? 220 PHE B CZ 1 ATOM 5042 N N . TYR B 1 221 ? 15.600 -65.233 -17.874 1.00 84.08 ? 221 TYR B N 1 ATOM 5043 C CA . TYR B 1 221 ? 16.691 -66.127 -18.209 1.00 86.83 ? 221 TYR B CA 1 ATOM 5044 C C . TYR B 1 221 ? 16.496 -66.857 -19.540 1.00 84.86 ? 221 TYR B C 1 ATOM 5045 O O . TYR B 1 221 ? 17.223 -66.614 -20.502 1.00 84.04 ? 221 TYR B O 1 ATOM 5046 C CB . TYR B 1 221 ? 16.909 -67.136 -17.078 1.00 86.32 ? 221 TYR B CB 1 ATOM 5047 C CG . TYR B 1 221 ? 17.968 -68.166 -17.381 1.00 88.83 ? 221 TYR B CG 1 ATOM 5048 C CD1 . TYR B 1 221 ? 19.208 -67.794 -17.910 1.00 86.25 ? 221 TYR B CD1 1 ATOM 5049 C CD2 . TYR B 1 221 ? 17.746 -69.511 -17.122 1.00 90.93 ? 221 TYR B CD2 1 ATOM 5050 C CE1 . TYR B 1 221 ? 20.174 -68.732 -18.180 1.00 83.79 ? 221 TYR B CE1 1 ATOM 5051 C CE2 . TYR B 1 221 ? 18.712 -70.454 -17.388 1.00 90.55 ? 221 TYR B CE2 1 ATOM 5052 C CZ . TYR B 1 221 ? 19.919 -70.054 -17.912 1.00 87.91 ? 221 TYR B CZ 1 ATOM 5053 O OH . TYR B 1 221 ? 20.861 -70.994 -18.180 1.00 92.27 ? 221 TYR B OH 1 ATOM 5054 N N . ASP B 1 222 ? 15.530 -67.762 -19.586 1.00 86.04 ? 222 ASP B N 1 ATOM 5055 C CA . ASP B 1 222 ? 15.355 -68.644 -20.741 1.00 87.42 ? 222 ASP B CA 1 ATOM 5056 C C . ASP B 1 222 ? 13.922 -68.614 -21.225 1.00 87.21 ? 222 ASP B C 1 ATOM 5057 O O . ASP B 1 222 ? 13.396 -69.606 -21.707 1.00 91.55 ? 222 ASP B O 1 ATOM 5058 C CB . ASP B 1 222 ? 15.795 -70.074 -20.395 1.00 86.96 ? 222 ASP B CB 1 ATOM 5059 C CG . ASP B 1 222 ? 15.096 -70.622 -19.167 1.00 88.80 ? 222 ASP B CG 1 ATOM 5060 O OD1 . ASP B 1 222 ? 14.035 -70.079 -18.783 1.00 89.70 ? 222 ASP B OD1 1 ATOM 5061 O OD2 . ASP B 1 222 ? 15.611 -71.596 -18.586 1.00 85.35 ? 222 ASP B OD2 1 ATOM 5062 N N . ASN B 1 223 ? 13.305 -67.452 -21.103 1.00 90.58 ? 223 ASN B N 1 ATOM 5063 C CA . ASN B 1 223 ? 11.911 -67.277 -21.450 1.00 95.79 ? 223 ASN B CA 1 ATOM 5064 C C . ASN B 1 223 ? 11.697 -67.477 -22.945 1.00 99.24 ? 223 ASN B C 1 ATOM 5065 O O . ASN B 1 223 ? 12.453 -66.960 -23.763 1.00 96.68 ? 223 ASN B O 1 ATOM 5066 C CB . ASN B 1 223 ? 11.445 -65.887 -21.029 1.00 95.92 ? 223 ASN B CB 1 ATOM 5067 C CG . ASN B 1 223 ? 9.949 -65.799 -20.872 1.00 100.70 ? 223 ASN B CG 1 ATOM 5068 O OD1 . ASN B 1 223 ? 9.205 -66.246 -21.730 1.00 105.77 ? 223 ASN B OD1 1 ATOM 5069 N ND2 . ASN B 1 223 ? 9.499 -65.229 -19.764 1.00 102.62 ? 223 ASN B ND2 1 ATOM 5070 N N . LYS B 1 224 ? 10.656 -68.223 -23.288 1.00 106.12 ? 224 LYS B N 1 ATOM 5071 C CA . LYS B 1 224 ? 10.388 -68.571 -24.677 1.00 108.44 ? 224 LYS B CA 1 ATOM 5072 C C . LYS B 1 224 ? 9.370 -67.641 -25.314 1.00 105.76 ? 224 LYS B C 1 ATOM 5073 O O . LYS B 1 224 ? 9.143 -67.712 -26.514 1.00 109.69 ? 224 LYS B O 1 ATOM 5074 C CB . LYS B 1 224 ? 9.916 -70.024 -24.785 1.00 113.41 ? 224 LYS B CB 1 ATOM 5075 C CG . LYS B 1 224 ? 10.963 -71.058 -24.387 1.00 114.21 ? 224 LYS B CG 1 ATOM 5076 C CD . LYS B 1 224 ? 12.126 -71.113 -25.368 1.00 113.14 ? 224 LYS B CD 1 ATOM 5077 C CE . LYS B 1 224 ? 13.199 -72.092 -24.924 1.00 111.45 ? 224 LYS B CE 1 ATOM 5078 N NZ . LYS B 1 224 ? 13.895 -71.646 -23.682 1.00 109.28 ? 224 LYS B NZ 1 ATOM 5079 N N . ASP B 1 225 ? 8.759 -66.769 -24.522 1.00 103.53 ? 225 ASP B N 1 ATOM 5080 C CA . ASP B 1 225 ? 7.816 -65.808 -25.058 1.00 104.27 ? 225 ASP B CA 1 ATOM 5081 C C . ASP B 1 225 ? 8.553 -64.892 -26.029 1.00 105.53 ? 225 ASP B C 1 ATOM 5082 O O . ASP B 1 225 ? 9.513 -64.234 -25.654 1.00 106.08 ? 225 ASP B O 1 ATOM 5083 C CB . ASP B 1 225 ? 7.160 -65.011 -23.932 1.00 102.19 ? 225 ASP B CB 1 ATOM 5084 C CG . ASP B 1 225 ? 5.979 -64.207 -24.404 1.00 105.87 ? 225 ASP B CG 1 ATOM 5085 O OD1 . ASP B 1 225 ? 6.040 -63.621 -25.497 1.00 113.75 ? 225 ASP B OD1 1 ATOM 5086 O OD2 . ASP B 1 225 ? 4.979 -64.133 -23.672 1.00 111.41 ? 225 ASP B OD2 1 ATOM 5087 N N . LEU B 1 226 ? 8.096 -64.864 -27.277 1.00 109.52 ? 226 LEU B N 1 ATOM 5088 C CA . LEU B 1 226 ? 8.770 -64.122 -28.350 1.00 109.52 ? 226 LEU B CA 1 ATOM 5089 C C . LEU B 1 226 ? 8.734 -62.607 -28.145 1.00 103.72 ? 226 LEU B C 1 ATOM 5090 O O . LEU B 1 226 ? 9.648 -61.905 -28.559 1.00 103.36 ? 226 LEU B O 1 ATOM 5091 C CB . LEU B 1 226 ? 8.157 -64.488 -29.706 1.00 113.62 ? 226 LEU B CB 1 ATOM 5092 C CG . LEU B 1 226 ? 8.423 -65.939 -30.116 1.00 115.73 ? 226 LEU B CG 1 ATOM 5093 C CD1 . LEU B 1 226 ? 7.222 -66.557 -30.816 1.00 119.99 ? 226 LEU B CD1 1 ATOM 5094 C CD2 . LEU B 1 226 ? 9.673 -66.035 -30.975 1.00 114.72 ? 226 LEU B CD2 1 ATOM 5095 N N . GLU B 1 227 ? 7.679 -62.118 -27.510 1.00 100.74 ? 227 GLU B N 1 ATOM 5096 C CA . GLU B 1 227 ? 7.582 -60.713 -27.147 1.00 101.21 ? 227 GLU B CA 1 ATOM 5097 C C . GLU B 1 227 ? 8.528 -60.397 -25.981 1.00 98.19 ? 227 GLU B C 1 ATOM 5098 O O . GLU B 1 227 ? 9.049 -59.289 -25.894 1.00 100.71 ? 227 GLU B O 1 ATOM 5099 C CB . GLU B 1 227 ? 6.130 -60.329 -26.785 1.00 103.22 ? 227 GLU B CB 1 ATOM 5100 C CG . GLU B 1 227 ? 5.185 -60.025 -27.953 1.00 103.29 ? 227 GLU B CG 1 ATOM 5101 C CD . GLU B 1 227 ? 3.799 -59.561 -27.501 1.00 107.69 ? 227 GLU B CD 1 ATOM 5102 O OE1 . GLU B 1 227 ? 3.387 -58.440 -27.868 1.00 111.37 ? 227 GLU B OE1 1 ATOM 5103 O OE2 . GLU B 1 227 ? 3.111 -60.300 -26.769 1.00 105.47 ? 227 GLU B OE2 1 ATOM 5104 N N . CYS B 1 228 ? 8.745 -61.362 -25.087 1.00 94.78 ? 228 CYS B N 1 ATOM 5105 C CA . CYS B 1 228 ? 9.743 -61.216 -24.021 1.00 89.61 ? 228 CYS B CA 1 ATOM 5106 C C . CYS B 1 228 ? 11.137 -61.131 -24.612 1.00 85.76 ? 228 CYS B C 1 ATOM 5107 O O . CYS B 1 228 ? 11.927 -60.279 -24.230 1.00 86.53 ? 228 CYS B O 1 ATOM 5108 C CB . CYS B 1 228 ? 9.671 -62.378 -23.016 1.00 91.80 ? 228 CYS B CB 1 ATOM 5109 S SG . CYS B 1 228 ? 10.878 -62.331 -21.663 1.00 89.54 ? 228 CYS B SG 1 ATOM 5110 N N . VAL B 1 229 ? 11.438 -62.007 -25.561 1.00 86.87 ? 229 VAL B N 1 ATOM 5111 C CA . VAL B 1 229 ? 12.753 -62.018 -26.186 1.00 83.34 ? 229 VAL B CA 1 ATOM 5112 C C . VAL B 1 229 ? 13.071 -60.685 -26.849 1.00 82.80 ? 229 VAL B C 1 ATOM 5113 O O . VAL B 1 229 ? 14.183 -60.182 -26.710 1.00 81.13 ? 229 VAL B O 1 ATOM 5114 C CB . VAL B 1 229 ? 12.895 -63.167 -27.187 1.00 81.78 ? 229 VAL B CB 1 ATOM 5115 C CG1 . VAL B 1 229 ? 14.142 -62.997 -28.041 1.00 80.55 ? 229 VAL B CG1 1 ATOM 5116 C CG2 . VAL B 1 229 ? 12.953 -64.486 -26.435 1.00 81.29 ? 229 VAL B CG2 1 ATOM 5117 N N . THR B 1 230 ? 12.105 -60.106 -27.547 1.00 85.33 ? 230 THR B N 1 ATOM 5118 C CA . THR B 1 230 ? 12.327 -58.829 -28.218 1.00 89.86 ? 230 THR B CA 1 ATOM 5119 C C . THR B 1 230 ? 12.729 -57.743 -27.226 1.00 88.69 ? 230 THR B C 1 ATOM 5120 O O . THR B 1 230 ? 13.561 -56.894 -27.530 1.00 91.91 ? 230 THR B O 1 ATOM 5121 C CB . THR B 1 230 ? 11.083 -58.392 -28.988 1.00 93.46 ? 230 THR B CB 1 ATOM 5122 O OG1 . THR B 1 230 ? 10.707 -59.437 -29.882 1.00 101.57 ? 230 THR B OG1 1 ATOM 5123 C CG2 . THR B 1 230 ? 11.332 -57.108 -29.788 1.00 95.01 ? 230 THR B CG2 1 ATOM 5124 N N . ASN B 1 231 ? 12.156 -57.792 -26.033 1.00 88.29 ? 231 ASN B N 1 ATOM 5125 C CA . ASN B 1 231 ? 12.484 -56.849 -24.976 1.00 85.83 ? 231 ASN B CA 1 ATOM 5126 C C . ASN B 1 231 ? 13.786 -57.159 -24.256 1.00 84.82 ? 231 ASN B C 1 ATOM 5127 O O . ASN B 1 231 ? 14.545 -56.247 -23.941 1.00 83.33 ? 231 ASN B O 1 ATOM 5128 C CB . ASN B 1 231 ? 11.347 -56.795 -23.974 1.00 87.37 ? 231 ASN B CB 1 ATOM 5129 C CG . ASN B 1 231 ? 10.154 -56.066 -24.524 1.00 91.06 ? 231 ASN B CG 1 ATOM 5130 O OD1 . ASN B 1 231 ? 10.300 -55.144 -25.331 1.00 89.79 ? 231 ASN B OD1 1 ATOM 5131 N ND2 . ASN B 1 231 ? 8.970 -56.460 -24.097 1.00 91.09 ? 231 ASN B ND2 1 ATOM 5132 N N . LEU B 1 232 ? 14.043 -58.434 -23.979 1.00 83.98 ? 232 LEU B N 1 ATOM 5133 C CA . LEU B 1 232 ? 15.317 -58.808 -23.390 1.00 83.84 ? 232 LEU B CA 1 ATOM 5134 C C . LEU B 1 232 ? 16.451 -58.377 -24.306 1.00 87.25 ? 232 LEU B C 1 ATOM 5135 O O . LEU B 1 232 ? 17.473 -57.881 -23.834 1.00 90.82 ? 232 LEU B O 1 ATOM 5136 C CB . LEU B 1 232 ? 15.386 -60.297 -23.082 1.00 85.07 ? 232 LEU B CB 1 ATOM 5137 C CG . LEU B 1 232 ? 14.596 -60.756 -21.840 1.00 86.29 ? 232 LEU B CG 1 ATOM 5138 C CD1 . LEU B 1 232 ? 14.570 -62.271 -21.703 1.00 87.15 ? 232 LEU B CD1 1 ATOM 5139 C CD2 . LEU B 1 232 ? 15.159 -60.137 -20.568 1.00 84.24 ? 232 LEU B CD2 1 ATOM 5140 N N . GLN B 1 233 ? 16.243 -58.502 -25.614 1.00 88.90 ? 233 GLN B N 1 ATOM 5141 C CA . GLN B 1 233 ? 17.207 -58.015 -26.596 1.00 84.87 ? 233 GLN B CA 1 ATOM 5142 C C . GLN B 1 233 ? 17.445 -56.516 -26.483 1.00 80.30 ? 233 GLN B C 1 ATOM 5143 O O . GLN B 1 233 ? 18.583 -56.054 -26.584 1.00 79.13 ? 233 GLN B O 1 ATOM 5144 C CB . GLN B 1 233 ? 16.732 -58.338 -28.001 1.00 89.59 ? 233 GLN B CB 1 ATOM 5145 C CG . GLN B 1 233 ? 16.864 -59.803 -28.350 1.00 94.43 ? 233 GLN B CG 1 ATOM 5146 C CD . GLN B 1 233 ? 16.291 -60.146 -29.714 1.00 98.20 ? 233 GLN B CD 1 ATOM 5147 O OE1 . GLN B 1 233 ? 16.607 -61.191 -30.266 1.00 98.25 ? 233 GLN B OE1 1 ATOM 5148 N NE2 . GLN B 1 233 ? 15.456 -59.269 -30.264 1.00 96.99 ? 233 GLN B NE2 1 ATOM 5149 N N . GLU B 1 234 ? 16.373 -55.762 -26.286 1.00 76.39 ? 234 GLU B N 1 ATOM 5150 C CA . GLU B 1 234 ? 16.488 -54.332 -26.069 1.00 78.19 ? 234 GLU B CA 1 ATOM 5151 C C . GLU B 1 234 ? 17.314 -54.060 -24.813 1.00 75.99 ? 234 GLU B C 1 ATOM 5152 O O . GLU B 1 234 ? 18.259 -53.281 -24.867 1.00 76.75 ? 234 GLU B O 1 ATOM 5153 C CB . GLU B 1 234 ? 15.101 -53.676 -25.995 1.00 83.69 ? 234 GLU B CB 1 ATOM 5154 C CG . GLU B 1 234 ? 15.043 -52.247 -25.474 1.00 87.31 ? 234 GLU B CG 1 ATOM 5155 C CD . GLU B 1 234 ? 15.751 -51.240 -26.356 1.00 93.85 ? 234 GLU B CD 1 ATOM 5156 O OE1 . GLU B 1 234 ? 16.779 -51.581 -26.977 1.00 98.30 ? 234 GLU B OE1 1 ATOM 5157 O OE2 . GLU B 1 234 ? 15.282 -50.082 -26.413 1.00 102.60 ? 234 GLU B OE2 1 ATOM 5158 N N . VAL B 1 235 ? 16.973 -54.710 -23.698 1.00 72.95 ? 235 VAL B N 1 ATOM 5159 C CA . VAL B 1 235 ? 17.760 -54.596 -22.465 1.00 69.73 ? 235 VAL B CA 1 ATOM 5160 C C . VAL B 1 235 ? 19.219 -54.916 -22.743 1.00 66.94 ? 235 VAL B C 1 ATOM 5161 O O . VAL B 1 235 ? 20.101 -54.175 -22.356 1.00 66.50 ? 235 VAL B O 1 ATOM 5162 C CB . VAL B 1 235 ? 17.271 -55.545 -21.347 1.00 67.22 ? 235 VAL B CB 1 ATOM 5163 C CG1 . VAL B 1 235 ? 18.234 -55.535 -20.164 1.00 65.20 ? 235 VAL B CG1 1 ATOM 5164 C CG2 . VAL B 1 235 ? 15.885 -55.160 -20.888 1.00 67.49 ? 235 VAL B CG2 1 ATOM 5165 N N . ALA B 1 236 ? 19.470 -56.045 -23.380 1.00 69.57 ? 236 ALA B N 1 ATOM 5166 C CA . ALA B 1 236 ? 20.837 -56.416 -23.737 1.00 73.59 ? 236 ALA B CA 1 ATOM 5167 C C . ALA B 1 236 ? 21.545 -55.285 -24.502 1.00 77.46 ? 236 ALA B C 1 ATOM 5168 O O . ALA B 1 236 ? 22.709 -55.000 -24.253 1.00 79.66 ? 236 ALA B O 1 ATOM 5169 C CB . ALA B 1 236 ? 20.849 -57.705 -24.554 1.00 72.82 ? 236 ALA B CB 1 ATOM 5170 N N . ARG B 1 237 ? 20.837 -54.642 -25.422 1.00 82.52 ? 237 ARG B N 1 ATOM 5171 C CA . ARG B 1 237 ? 21.412 -53.550 -26.203 1.00 84.11 ? 237 ARG B CA 1 ATOM 5172 C C . ARG B 1 237 ? 21.712 -52.321 -25.338 1.00 77.45 ? 237 ARG B C 1 ATOM 5173 O O . ARG B 1 237 ? 22.721 -51.660 -25.529 1.00 75.19 ? 237 ARG B O 1 ATOM 5174 C CB . ARG B 1 237 ? 20.481 -53.159 -27.354 1.00 90.27 ? 237 ARG B CB 1 ATOM 5175 C CG . ARG B 1 237 ? 21.048 -52.095 -28.279 1.00 97.60 ? 237 ARG B CG 1 ATOM 5176 C CD . ARG B 1 237 ? 19.975 -51.451 -29.146 1.00 111.20 ? 237 ARG B CD 1 ATOM 5177 N NE . ARG B 1 237 ? 19.015 -50.659 -28.374 1.00 117.83 ? 237 ARG B NE 1 ATOM 5178 C CZ . ARG B 1 237 ? 19.239 -49.445 -27.869 1.00 120.74 ? 237 ARG B CZ 1 ATOM 5179 N NH1 . ARG B 1 237 ? 20.409 -48.829 -28.033 1.00 122.20 ? 237 ARG B NH1 1 ATOM 5180 N NH2 . ARG B 1 237 ? 18.280 -48.835 -27.180 1.00 119.20 ? 237 ARG B NH2 1 ATOM 5181 N N . ILE B 1 238 ? 20.835 -52.007 -24.399 1.00 74.49 ? 238 ILE B N 1 ATOM 5182 C CA . ILE B 1 238 ? 21.035 -50.824 -23.563 1.00 74.50 ? 238 ILE B CA 1 ATOM 5183 C C . ILE B 1 238 ? 22.222 -51.034 -22.627 1.00 69.41 ? 238 ILE B C 1 ATOM 5184 O O . ILE B 1 238 ? 23.115 -50.194 -22.531 1.00 64.26 ? 238 ILE B O 1 ATOM 5185 C CB . ILE B 1 238 ? 19.793 -50.485 -22.724 1.00 75.28 ? 238 ILE B CB 1 ATOM 5186 C CG1 . ILE B 1 238 ? 18.628 -50.128 -23.644 1.00 76.95 ? 238 ILE B CG1 1 ATOM 5187 C CG2 . ILE B 1 238 ? 20.085 -49.303 -21.819 1.00 76.39 ? 238 ILE B CG2 1 ATOM 5188 C CD1 . ILE B 1 238 ? 17.310 -49.972 -22.937 1.00 76.69 ? 238 ILE B CD1 1 ATOM 5189 N N . VAL B 1 239 ? 22.229 -52.177 -21.965 1.00 65.91 ? 239 VAL B N 1 ATOM 5190 C CA . VAL B 1 239 ? 23.233 -52.475 -20.960 1.00 67.06 ? 239 VAL B CA 1 ATOM 5191 C C . VAL B 1 239 ? 24.609 -52.642 -21.580 1.00 68.54 ? 239 VAL B C 1 ATOM 5192 O O . VAL B 1 239 ? 25.566 -52.026 -21.135 1.00 68.98 ? 239 VAL B O 1 ATOM 5193 C CB . VAL B 1 239 ? 22.844 -53.734 -20.160 1.00 64.60 ? 239 VAL B CB 1 ATOM 5194 C CG1 . VAL B 1 239 ? 23.971 -54.190 -19.259 1.00 64.64 ? 239 VAL B CG1 1 ATOM 5195 C CG2 . VAL B 1 239 ? 21.607 -53.452 -19.326 1.00 66.42 ? 239 VAL B CG2 1 ATOM 5196 N N . GLY B 1 240 ? 24.692 -53.477 -22.606 1.00 74.25 ? 240 GLY B N 1 ATOM 5197 C CA . GLY B 1 240 ? 25.966 -53.955 -23.106 1.00 74.60 ? 240 GLY B CA 1 ATOM 5198 C C . GLY B 1 240 ? 26.465 -53.271 -24.363 1.00 76.37 ? 240 GLY B C 1 ATOM 5199 O O . GLY B 1 240 ? 27.653 -53.317 -24.653 1.00 79.32 ? 240 GLY B O 1 ATOM 5200 N N . ASN B 1 241 ? 25.582 -52.628 -25.113 1.00 75.43 ? 241 ASN B N 1 ATOM 5201 C CA . ASN B 1 241 ? 25.914 -52.258 -26.488 1.00 77.55 ? 241 ASN B CA 1 ATOM 5202 C C . ASN B 1 241 ? 25.481 -50.870 -26.900 1.00 72.97 ? 241 ASN B C 1 ATOM 5203 O O . ASN B 1 241 ? 25.122 -50.661 -28.051 1.00 71.00 ? 241 ASN B O 1 ATOM 5204 C CB . ASN B 1 241 ? 25.298 -53.279 -27.452 1.00 79.55 ? 241 ASN B CB 1 ATOM 5205 C CG . ASN B 1 241 ? 25.994 -53.308 -28.792 1.00 83.66 ? 241 ASN B CG 1 ATOM 5206 O OD1 . ASN B 1 241 ? 25.402 -53.022 -29.841 1.00 81.72 ? 241 ASN B OD1 1 ATOM 5207 N ND2 . ASN B 1 241 ? 27.271 -53.659 -28.766 1.00 89.32 ? 241 ASN B ND2 1 ATOM 5208 N N . SER B 1 242 ? 25.557 -49.916 -25.982 1.00 67.76 ? 242 SER B N 1 ATOM 5209 C CA . SER B 1 242 ? 25.080 -48.588 -26.278 1.00 67.44 ? 242 SER B CA 1 ATOM 5210 C C . SER B 1 242 ? 25.881 -47.454 -25.655 1.00 64.89 ? 242 SER B C 1 ATOM 5211 O O . SER B 1 242 ? 25.393 -46.332 -25.651 1.00 63.90 ? 242 SER B O 1 ATOM 5212 C CB . SER B 1 242 ? 23.632 -48.468 -25.826 1.00 68.95 ? 242 SER B CB 1 ATOM 5213 O OG . SER B 1 242 ? 23.573 -48.139 -24.452 1.00 72.41 ? 242 SER B OG 1 ATOM 5214 N N . GLY B 1 243 ? 27.079 -47.727 -25.140 1.00 63.76 ? 243 GLY B N 1 ATOM 5215 C CA . GLY B 1 243 ? 27.961 -46.685 -24.590 1.00 64.50 ? 243 GLY B CA 1 ATOM 5216 C C . GLY B 1 243 ? 28.263 -46.734 -23.088 1.00 64.84 ? 243 GLY B C 1 ATOM 5217 O O . GLY B 1 243 ? 29.189 -46.073 -22.619 1.00 67.65 ? 243 GLY B O 1 ATOM 5218 N N . LEU B 1 244 ? 27.486 -47.488 -22.322 1.00 61.93 ? 244 LEU B N 1 ATOM 5219 C CA . LEU B 1 244 ? 27.716 -47.581 -20.881 1.00 58.98 ? 244 LEU B CA 1 ATOM 5220 C C . LEU B 1 244 ? 28.882 -48.478 -20.580 1.00 59.75 ? 244 LEU B C 1 ATOM 5221 O O . LEU B 1 244 ? 29.240 -49.337 -21.382 1.00 63.04 ? 244 LEU B O 1 ATOM 5222 C CB . LEU B 1 244 ? 26.494 -48.144 -20.161 1.00 56.44 ? 244 LEU B CB 1 ATOM 5223 C CG . LEU B 1 244 ? 25.230 -47.329 -20.242 1.00 53.03 ? 244 LEU B CG 1 ATOM 5224 C CD1 . LEU B 1 244 ? 24.086 -48.103 -19.639 1.00 52.44 ? 244 LEU B CD1 1 ATOM 5225 C CD2 . LEU B 1 244 ? 25.428 -46.016 -19.529 1.00 54.71 ? 244 LEU B CD2 1 ATOM 5226 N N . ASN B 1 245 ? 29.455 -48.299 -19.396 1.00 59.56 ? 245 ASN B N 1 ATOM 5227 C CA . ASN B 1 245 ? 30.522 -49.153 -18.953 1.00 57.21 ? 245 ASN B CA 1 ATOM 5228 C C . ASN B 1 245 ? 29.949 -50.293 -18.122 1.00 60.51 ? 245 ASN B C 1 ATOM 5229 O O . ASN B 1 245 ? 29.643 -50.144 -16.932 1.00 54.31 ? 245 ASN B O 1 ATOM 5230 C CB . ASN B 1 245 ? 31.536 -48.369 -18.163 1.00 56.25 ? 245 ASN B CB 1 ATOM 5231 C CG . ASN B 1 245 ? 32.787 -49.157 -17.904 1.00 58.49 ? 245 ASN B CG 1 ATOM 5232 O OD1 . ASN B 1 245 ? 32.777 -50.383 -17.919 1.00 55.12 ? 245 ASN B OD1 1 ATOM 5233 N ND2 . ASN B 1 245 ? 33.886 -48.457 -17.686 1.00 62.36 ? 245 ASN B ND2 1 ATOM 5234 N N . ILE B 1 246 ? 29.851 -51.448 -18.768 1.00 62.62 ? 246 ILE B N 1 ATOM 5235 C CA . ILE B 1 246 ? 29.247 -52.624 -18.169 1.00 61.08 ? 246 ILE B CA 1 ATOM 5236 C C . ILE B 1 246 ? 29.974 -53.093 -16.910 1.00 58.21 ? 246 ILE B C 1 ATOM 5237 O O . ILE B 1 246 ? 29.365 -53.674 -16.008 1.00 59.59 ? 246 ILE B O 1 ATOM 5238 C CB . ILE B 1 246 ? 29.136 -53.767 -19.213 1.00 62.14 ? 246 ILE B CB 1 ATOM 5239 C CG1 . ILE B 1 246 ? 28.167 -54.838 -18.739 1.00 65.25 ? 246 ILE B CG1 1 ATOM 5240 C CG2 . ILE B 1 246 ? 30.479 -54.392 -19.530 1.00 59.73 ? 246 ILE B CG2 1 ATOM 5241 C CD1 . ILE B 1 246 ? 27.769 -55.798 -19.840 1.00 66.96 ? 246 ILE B CD1 1 ATOM 5242 N N . TYR B 1 247 ? 31.270 -52.842 -16.859 1.00 55.98 ? 247 TYR B N 1 ATOM 5243 C CA . TYR B 1 247 ? 32.096 -53.192 -15.701 1.00 58.41 ? 247 TYR B CA 1 ATOM 5244 C C . TYR B 1 247 ? 31.861 -52.208 -14.532 1.00 55.54 ? 247 TYR B C 1 ATOM 5245 O O . TYR B 1 247 ? 32.046 -52.549 -13.370 1.00 51.59 ? 247 TYR B O 1 ATOM 5246 C CB . TYR B 1 247 ? 33.577 -53.165 -16.106 1.00 63.89 ? 247 TYR B CB 1 ATOM 5247 C CG . TYR B 1 247 ? 34.159 -54.443 -16.697 1.00 69.75 ? 247 TYR B CG 1 ATOM 5248 C CD1 . TYR B 1 247 ? 33.398 -55.323 -17.465 1.00 71.54 ? 247 TYR B CD1 1 ATOM 5249 C CD2 . TYR B 1 247 ? 35.497 -54.749 -16.490 1.00 81.28 ? 247 TYR B CD2 1 ATOM 5250 C CE1 . TYR B 1 247 ? 33.949 -56.484 -17.996 1.00 76.85 ? 247 TYR B CE1 1 ATOM 5251 C CE2 . TYR B 1 247 ? 36.062 -55.904 -17.006 1.00 89.83 ? 247 TYR B CE2 1 ATOM 5252 C CZ . TYR B 1 247 ? 35.292 -56.773 -17.758 1.00 87.92 ? 247 TYR B CZ 1 ATOM 5253 O OH . TYR B 1 247 ? 35.901 -57.911 -18.253 1.00 85.05 ? 247 TYR B OH 1 ATOM 5254 N N . ASN B 1 248 ? 31.468 -50.980 -14.855 1.00 52.92 ? 248 ASN B N 1 ATOM 5255 C CA . ASN B 1 248 ? 31.258 -49.956 -13.847 1.00 52.10 ? 248 ASN B CA 1 ATOM 5256 C C . ASN B 1 248 ? 30.397 -48.835 -14.417 1.00 52.21 ? 248 ASN B C 1 ATOM 5257 O O . ASN B 1 248 ? 30.874 -47.965 -15.122 1.00 51.67 ? 248 ASN B O 1 ATOM 5258 C CB . ASN B 1 248 ? 32.592 -49.413 -13.366 1.00 52.16 ? 248 ASN B CB 1 ATOM 5259 C CG . ASN B 1 248 ? 32.449 -48.228 -12.429 1.00 51.47 ? 248 ASN B CG 1 ATOM 5260 O OD1 . ASN B 1 248 ? 31.357 -47.730 -12.170 1.00 48.22 ? 248 ASN B OD1 1 ATOM 5261 N ND2 . ASN B 1 248 ? 33.567 -47.773 -11.916 1.00 53.22 ? 248 ASN B ND2 1 ATOM 5262 N N . LEU B 1 249 ? 29.121 -48.880 -14.079 1.00 51.16 ? 249 LEU B N 1 ATOM 5263 C CA . LEU B 1 249 ? 28.110 -48.007 -14.647 1.00 51.06 ? 249 LEU B CA 1 ATOM 5264 C C . LEU B 1 249 ? 28.358 -46.527 -14.503 1.00 50.59 ? 249 LEU B C 1 ATOM 5265 O O . LEU B 1 249 ? 27.828 -45.757 -15.292 1.00 53.94 ? 249 LEU B O 1 ATOM 5266 C CB . LEU B 1 249 ? 26.758 -48.327 -13.990 1.00 52.66 ? 249 LEU B CB 1 ATOM 5267 C CG . LEU B 1 249 ? 25.555 -47.455 -14.345 1.00 52.11 ? 249 LEU B CG 1 ATOM 5268 C CD1 . LEU B 1 249 ? 25.248 -47.539 -15.843 1.00 53.68 ? 249 LEU B CD1 1 ATOM 5269 C CD2 . LEU B 1 249 ? 24.366 -47.910 -13.526 1.00 49.74 ? 249 LEU B CD2 1 ATOM 5270 N N . TYR B 1 250 ? 29.098 -46.115 -13.479 1.00 50.25 ? 250 TYR B N 1 ATOM 5271 C CA . TYR B 1 250 ? 29.287 -44.690 -13.205 1.00 50.74 ? 250 TYR B CA 1 ATOM 5272 C C . TYR B 1 250 ? 30.604 -44.183 -13.719 1.00 52.55 ? 250 TYR B C 1 ATOM 5273 O O . TYR B 1 250 ? 30.924 -43.006 -13.556 1.00 56.78 ? 250 TYR B O 1 ATOM 5274 C CB . TYR B 1 250 ? 29.080 -44.398 -11.709 1.00 49.96 ? 250 TYR B CB 1 ATOM 5275 C CG . TYR B 1 250 ? 27.674 -44.743 -11.316 1.00 50.75 ? 250 TYR B CG 1 ATOM 5276 C CD1 . TYR B 1 250 ? 26.606 -44.000 -11.802 1.00 52.51 ? 250 TYR B CD1 1 ATOM 5277 C CD2 . TYR B 1 250 ? 27.397 -45.855 -10.550 1.00 53.77 ? 250 TYR B CD2 1 ATOM 5278 C CE1 . TYR B 1 250 ? 25.310 -44.337 -11.495 1.00 54.36 ? 250 TYR B CE1 1 ATOM 5279 C CE2 . TYR B 1 250 ? 26.098 -46.203 -10.220 1.00 52.01 ? 250 TYR B CE2 1 ATOM 5280 C CZ . TYR B 1 250 ? 25.066 -45.443 -10.694 1.00 55.20 ? 250 TYR B CZ 1 ATOM 5281 O OH . TYR B 1 250 ? 23.776 -45.770 -10.384 1.00 60.57 ? 250 TYR B OH 1 ATOM 5282 N N . ALA B 1 251 ? 31.327 -45.066 -14.394 1.00 55.69 ? 251 ALA B N 1 ATOM 5283 C CA . ALA B 1 251 ? 32.591 -44.743 -15.049 1.00 60.81 ? 251 ALA B CA 1 ATOM 5284 C C . ALA B 1 251 ? 32.421 -44.521 -16.558 1.00 62.89 ? 251 ALA B C 1 ATOM 5285 O O . ALA B 1 251 ? 31.607 -45.177 -17.204 1.00 59.42 ? 251 ALA B O 1 ATOM 5286 C CB . ALA B 1 251 ? 33.590 -45.869 -14.820 1.00 60.78 ? 251 ALA B CB 1 ATOM 5287 N N . PRO B 1 252 ? 33.228 -43.618 -17.131 1.00 67.88 ? 252 PRO B N 1 ATOM 5288 C CA . PRO B 1 252 ? 33.201 -43.430 -18.576 1.00 67.79 ? 252 PRO B CA 1 ATOM 5289 C C . PRO B 1 252 ? 33.715 -44.666 -19.302 1.00 67.47 ? 252 PRO B C 1 ATOM 5290 O O . PRO B 1 252 ? 34.515 -45.405 -18.741 1.00 64.01 ? 252 PRO B O 1 ATOM 5291 C CB . PRO B 1 252 ? 34.161 -42.268 -18.783 1.00 69.86 ? 252 PRO B CB 1 ATOM 5292 C CG . PRO B 1 252 ? 35.142 -42.403 -17.665 1.00 68.44 ? 252 PRO B CG 1 ATOM 5293 C CD . PRO B 1 252 ? 34.347 -42.890 -16.501 1.00 66.61 ? 252 PRO B CD 1 ATOM 5294 N N . CYS B 1 253 ? 33.242 -44.885 -20.528 1.00 70.99 ? 253 CYS B N 1 ATOM 5295 C CA . CYS B 1 253 ? 33.661 -46.025 -21.334 1.00 72.48 ? 253 CYS B CA 1 ATOM 5296 C C . CYS B 1 253 ? 34.920 -45.637 -22.078 1.00 75.11 ? 253 CYS B C 1 ATOM 5297 O O . CYS B 1 253 ? 34.910 -44.696 -22.851 1.00 78.48 ? 253 CYS B O 1 ATOM 5298 C CB . CYS B 1 253 ? 32.573 -46.424 -22.327 1.00 73.12 ? 253 CYS B CB 1 ATOM 5299 S SG . CYS B 1 253 ? 32.979 -47.819 -23.411 1.00 72.45 ? 253 CYS B SG 1 ATOM 5300 N N . ALA B 1 254 ? 36.007 -46.349 -21.821 1.00 79.84 ? 254 ALA B N 1 ATOM 5301 C CA . ALA B 1 254 ? 37.292 -46.056 -22.447 1.00 83.37 ? 254 ALA B CA 1 ATOM 5302 C C . ALA B 1 254 ? 37.174 -45.823 -23.952 1.00 88.46 ? 254 ALA B C 1 ATOM 5303 O O . ALA B 1 254 ? 36.740 -46.705 -24.693 1.00 85.55 ? 254 ALA B O 1 ATOM 5304 C CB . ALA B 1 254 ? 38.279 -47.179 -22.166 1.00 81.71 ? 254 ALA B CB 1 ATOM 5305 N N . GLY B 1 255 ? 37.538 -44.620 -24.389 1.00 95.03 ? 255 GLY B N 1 ATOM 5306 C CA . GLY B 1 255 ? 37.620 -44.307 -25.812 1.00 101.78 ? 255 GLY B CA 1 ATOM 5307 C C . GLY B 1 255 ? 36.292 -43.945 -26.449 1.00 104.90 ? 255 GLY B C 1 ATOM 5308 O O . GLY B 1 255 ? 35.953 -44.451 -27.528 1.00 106.39 ? 255 GLY B O 1 ATOM 5309 N N . GLY B 1 256 ? 35.541 -43.075 -25.777 1.00 99.73 ? 256 GLY B N 1 ATOM 5310 C CA . GLY B 1 256 ? 34.291 -42.556 -26.305 1.00 100.93 ? 256 GLY B CA 1 ATOM 5311 C C . GLY B 1 256 ? 33.222 -43.608 -26.478 1.00 100.14 ? 256 GLY B C 1 ATOM 5312 O O . GLY B 1 256 ? 33.397 -44.761 -26.102 1.00 98.18 ? 256 GLY B O 1 ATOM 5313 N N . VAL B 1 257 ? 32.115 -43.203 -27.076 1.00 101.80 ? 257 VAL B N 1 ATOM 5314 C CA . VAL B 1 257 ? 31.011 -44.115 -27.326 1.00 105.10 ? 257 VAL B CA 1 ATOM 5315 C C . VAL B 1 257 ? 31.026 -44.561 -28.805 1.00 117.15 ? 257 VAL B C 1 ATOM 5316 O O . VAL B 1 257 ? 30.838 -43.745 -29.712 1.00 118.48 ? 257 VAL B O 1 ATOM 5317 C CB . VAL B 1 257 ? 29.663 -43.520 -26.859 1.00 97.84 ? 257 VAL B CB 1 ATOM 5318 C CG1 . VAL B 1 257 ? 29.682 -43.375 -25.351 1.00 97.09 ? 257 VAL B CG1 1 ATOM 5319 C CG2 . VAL B 1 257 ? 29.352 -42.180 -27.499 1.00 97.48 ? 257 VAL B CG2 1 ATOM 5320 N N . PRO B 1 258 ? 31.284 -45.861 -29.051 1.00 125.22 ? 258 PRO B N 1 ATOM 5321 C CA . PRO B 1 258 ? 31.514 -46.377 -30.412 1.00 132.68 ? 258 PRO B CA 1 ATOM 5322 C C . PRO B 1 258 ? 30.577 -45.826 -31.496 1.00 130.25 ? 258 PRO B C 1 ATOM 5323 O O . PRO B 1 258 ? 29.400 -45.596 -31.240 1.00 127.03 ? 258 PRO B O 1 ATOM 5324 C CB . PRO B 1 258 ? 31.328 -47.888 -30.245 1.00 131.07 ? 258 PRO B CB 1 ATOM 5325 C CG . PRO B 1 258 ? 31.742 -48.155 -28.838 1.00 127.06 ? 258 PRO B CG 1 ATOM 5326 C CD . PRO B 1 258 ? 31.378 -46.935 -28.041 1.00 124.08 ? 258 PRO B CD 1 ATOM 5327 N N . ARG B 1 268 ? 41.849 -58.200 -32.274 1.00 99.37 ? 298 ARG B N 1 ATOM 5328 C CA . ARG B 1 268 ? 42.136 -58.434 -30.864 1.00 99.75 ? 298 ARG B CA 1 ATOM 5329 C C . ARG B 1 268 ? 40.920 -58.144 -29.986 1.00 96.12 ? 298 ARG B C 1 ATOM 5330 O O . ARG B 1 268 ? 40.234 -57.147 -30.186 1.00 82.47 ? 298 ARG B O 1 ATOM 5331 C CB . ARG B 1 268 ? 43.316 -57.579 -30.400 1.00 98.76 ? 298 ARG B CB 1 ATOM 5332 C CG . ARG B 1 268 ? 43.802 -57.929 -29.000 1.00 95.74 ? 298 ARG B CG 1 ATOM 5333 C CD . ARG B 1 268 ? 45.109 -57.238 -28.641 1.00 99.30 ? 298 ARG B CD 1 ATOM 5334 N NE . ARG B 1 268 ? 44.920 -56.015 -27.864 1.00 100.17 ? 298 ARG B NE 1 ATOM 5335 C CZ . ARG B 1 268 ? 44.904 -54.776 -28.353 1.00 103.92 ? 298 ARG B CZ 1 ATOM 5336 N NH1 . ARG B 1 268 ? 45.067 -54.541 -29.656 1.00 104.40 ? 298 ARG B NH1 1 ATOM 5337 N NH2 . ARG B 1 268 ? 44.721 -53.753 -27.525 1.00 102.69 ? 298 ARG B NH2 1 ATOM 5338 N N . MET B 1 269 ? 40.674 -59.023 -29.016 1.00 97.55 ? 299 MET B N 1 ATOM 5339 C CA . MET B 1 269 ? 39.585 -58.849 -28.061 1.00 95.20 ? 299 MET B CA 1 ATOM 5340 C C . MET B 1 269 ? 40.123 -58.256 -26.777 1.00 93.14 ? 299 MET B C 1 ATOM 5341 O O . MET B 1 269 ? 40.824 -58.921 -26.012 1.00 95.43 ? 299 MET B O 1 ATOM 5342 C CB . MET B 1 269 ? 38.886 -60.176 -27.743 1.00 98.05 ? 299 MET B CB 1 ATOM 5343 C CG . MET B 1 269 ? 37.906 -60.099 -26.570 1.00 99.64 ? 299 MET B CG 1 ATOM 5344 S SD . MET B 1 269 ? 37.113 -61.648 -26.111 1.00 100.09 ? 299 MET B SD 1 ATOM 5345 C CE . MET B 1 269 ? 35.545 -61.436 -26.952 1.00 110.57 ? 299 MET B CE 1 ATOM 5346 N N . ASP B 1 270 ? 39.807 -56.993 -26.554 1.00 94.20 ? 300 ASP B N 1 ATOM 5347 C CA . ASP B 1 270 ? 39.954 -56.411 -25.244 1.00 91.77 ? 300 ASP B CA 1 ATOM 5348 C C . ASP B 1 270 ? 38.643 -56.698 -24.556 1.00 90.69 ? 300 ASP B C 1 ATOM 5349 O O . ASP B 1 270 ? 37.656 -57.000 -25.219 1.00 91.80 ? 300 ASP B O 1 ATOM 5350 C CB . ASP B 1 270 ? 40.196 -54.908 -25.333 1.00 95.51 ? 300 ASP B CB 1 ATOM 5351 C CG . ASP B 1 270 ? 41.540 -54.569 -25.943 1.00 103.75 ? 300 ASP B CG 1 ATOM 5352 O OD1 . ASP B 1 270 ? 41.956 -55.250 -26.901 1.00 116.21 ? 300 ASP B OD1 1 ATOM 5353 O OD2 . ASP B 1 270 ? 42.189 -53.615 -25.479 1.00 103.04 ? 300 ASP B OD2 1 ATOM 5354 N N . PRO B 1 271 ? 38.623 -56.620 -23.222 1.00 90.03 ? 301 PRO B N 1 ATOM 5355 C CA . PRO B 1 271 ? 37.346 -56.492 -22.547 1.00 87.82 ? 301 PRO B CA 1 ATOM 5356 C C . PRO B 1 271 ? 36.697 -55.179 -22.975 1.00 92.89 ? 301 PRO B C 1 ATOM 5357 O O . PRO B 1 271 ? 37.412 -54.228 -23.302 1.00 93.11 ? 301 PRO B O 1 ATOM 5358 C CB . PRO B 1 271 ? 37.723 -56.433 -21.061 1.00 86.91 ? 301 PRO B CB 1 ATOM 5359 C CG . PRO B 1 271 ? 39.138 -56.883 -20.971 1.00 85.20 ? 301 PRO B CG 1 ATOM 5360 C CD . PRO B 1 271 ? 39.758 -56.564 -22.289 1.00 89.10 ? 301 PRO B CD 1 ATOM 5361 N N . PRO B 1 272 ? 35.358 -55.105 -22.960 1.00 92.61 ? 302 PRO B N 1 ATOM 5362 C CA . PRO B 1 272 ? 34.731 -53.879 -23.455 1.00 90.98 ? 302 PRO B CA 1 ATOM 5363 C C . PRO B 1 272 ? 34.884 -52.704 -22.483 1.00 85.17 ? 302 PRO B C 1 ATOM 5364 O O . PRO B 1 272 ? 34.988 -52.898 -21.274 1.00 79.13 ? 302 PRO B O 1 ATOM 5365 C CB . PRO B 1 272 ? 33.265 -54.271 -23.622 1.00 93.07 ? 302 PRO B CB 1 ATOM 5366 C CG . PRO B 1 272 ? 33.094 -55.585 -22.918 1.00 93.04 ? 302 PRO B CG 1 ATOM 5367 C CD . PRO B 1 272 ? 34.394 -55.980 -22.287 1.00 89.16 ? 302 PRO B CD 1 ATOM 5368 N N . CYS B 1 273 ? 34.916 -51.502 -23.047 1.00 86.30 ? 303 CYS B N 1 ATOM 5369 C CA . CYS B 1 273 ? 35.130 -50.254 -22.308 1.00 79.52 ? 303 CYS B CA 1 ATOM 5370 C C . CYS B 1 273 ? 36.424 -50.229 -21.504 1.00 77.48 ? 303 CYS B C 1 ATOM 5371 O O . CYS B 1 273 ? 36.575 -49.408 -20.605 1.00 79.32 ? 303 CYS B O 1 ATOM 5372 C CB . CYS B 1 273 ? 33.925 -49.939 -21.417 1.00 75.94 ? 303 CYS B CB 1 ATOM 5373 S SG . CYS B 1 273 ? 32.444 -49.483 -22.356 1.00 81.05 ? 303 CYS B SG 1 ATOM 5374 N N . THR B 1 274 ? 37.371 -51.088 -21.866 1.00 74.38 ? 304 THR B N 1 ATOM 5375 C CA . THR B 1 274 ? 38.627 -51.222 -21.138 1.00 74.42 ? 304 THR B CA 1 ATOM 5376 C C . THR B 1 274 ? 39.824 -50.866 -22.032 1.00 72.71 ? 304 THR B C 1 ATOM 5377 O O . THR B 1 274 ? 39.965 -51.403 -23.115 1.00 71.24 ? 304 THR B O 1 ATOM 5378 C CB . THR B 1 274 ? 38.786 -52.660 -20.607 1.00 74.49 ? 304 THR B CB 1 ATOM 5379 O OG1 . THR B 1 274 ? 37.523 -53.143 -20.149 1.00 74.97 ? 304 THR B OG1 1 ATOM 5380 C CG2 . THR B 1 274 ? 39.792 -52.728 -19.459 1.00 75.89 ? 304 THR B CG2 1 ATOM 5381 N N . ASN B 1 275 ? 40.680 -49.961 -21.571 1.00 75.16 ? 305 ASN B N 1 ATOM 5382 C CA . ASN B 1 275 ? 41.964 -49.695 -22.219 1.00 76.20 ? 305 ASN B CA 1 ATOM 5383 C C . ASN B 1 275 ? 43.024 -50.643 -21.653 1.00 74.22 ? 305 ASN B C 1 ATOM 5384 O O . ASN B 1 275 ? 43.296 -50.632 -20.460 1.00 70.35 ? 305 ASN B O 1 ATOM 5385 C CB . ASN B 1 275 ? 42.368 -48.242 -21.985 1.00 80.12 ? 305 ASN B CB 1 ATOM 5386 C CG . ASN B 1 275 ? 43.560 -47.807 -22.828 1.00 85.23 ? 305 ASN B CG 1 ATOM 5387 O OD1 . ASN B 1 275 ? 44.265 -48.621 -23.412 1.00 81.17 ? 305 ASN B OD1 1 ATOM 5388 N ND2 . ASN B 1 275 ? 43.782 -46.495 -22.884 1.00 91.47 ? 305 ASN B ND2 1 ATOM 5389 N N . THR B 1 276 ? 43.603 -51.474 -22.507 1.00 76.19 ? 306 THR B N 1 ATOM 5390 C CA . THR B 1 276 ? 44.612 -52.447 -22.079 1.00 81.14 ? 306 THR B CA 1 ATOM 5391 C C . THR B 1 276 ? 46.006 -52.063 -22.584 1.00 85.78 ? 306 THR B C 1 ATOM 5392 O O . THR B 1 276 ? 46.909 -52.907 -22.625 1.00 89.08 ? 306 THR B O 1 ATOM 5393 C CB . THR B 1 276 ? 44.277 -53.875 -22.575 1.00 82.49 ? 306 THR B CB 1 ATOM 5394 O OG1 . THR B 1 276 ? 44.503 -53.981 -23.987 1.00 80.87 ? 306 THR B OG1 1 ATOM 5395 C CG2 . THR B 1 276 ? 42.837 -54.220 -22.282 1.00 81.69 ? 306 THR B CG2 1 ATOM 5396 N N . THR B 1 277 ? 46.186 -50.803 -22.967 1.00 82.97 ? 307 THR B N 1 ATOM 5397 C CA . THR B 1 277 ? 47.438 -50.377 -23.557 1.00 82.59 ? 307 THR B CA 1 ATOM 5398 C C . THR B 1 277 ? 48.553 -50.436 -22.526 1.00 81.92 ? 307 THR B C 1 ATOM 5399 O O . THR B 1 277 ? 49.594 -51.051 -22.772 1.00 83.44 ? 307 THR B O 1 ATOM 5400 C CB . THR B 1 277 ? 47.338 -48.962 -24.135 1.00 82.88 ? 307 THR B CB 1 ATOM 5401 O OG1 . THR B 1 277 ? 46.193 -48.892 -24.981 1.00 85.74 ? 307 THR B OG1 1 ATOM 5402 C CG2 . THR B 1 277 ? 48.582 -48.608 -24.949 1.00 83.99 ? 307 THR B CG2 1 ATOM 5403 N N . ALA B 1 278 ? 48.336 -49.811 -21.377 1.00 77.05 ? 308 ALA B N 1 ATOM 5404 C CA . ALA B 1 278 ? 49.380 -49.713 -20.358 1.00 78.87 ? 308 ALA B CA 1 ATOM 5405 C C . ALA B 1 278 ? 50.060 -51.056 -20.089 1.00 80.49 ? 308 ALA B C 1 ATOM 5406 O O . ALA B 1 278 ? 51.275 -51.164 -20.155 1.00 84.29 ? 308 ALA B O 1 ATOM 5407 C CB . ALA B 1 278 ? 48.809 -49.150 -19.075 1.00 77.39 ? 308 ALA B CB 1 ATOM 5408 N N . ALA B 1 279 ? 49.266 -52.084 -19.821 1.00 82.70 ? 309 ALA B N 1 ATOM 5409 C CA . ALA B 1 279 ? 49.797 -53.403 -19.451 1.00 81.48 ? 309 ALA B CA 1 ATOM 5410 C C . ALA B 1 279 ? 50.444 -54.121 -20.627 1.00 80.55 ? 309 ALA B C 1 ATOM 5411 O O . ALA B 1 279 ? 51.503 -54.712 -20.477 1.00 84.23 ? 309 ALA B O 1 ATOM 5412 C CB . ALA B 1 279 ? 48.701 -54.271 -18.854 1.00 77.74 ? 309 ALA B CB 1 ATOM 5413 N N . SER B 1 280 ? 49.798 -54.069 -21.785 1.00 80.17 ? 310 SER B N 1 ATOM 5414 C CA . SER B 1 280 ? 50.303 -54.716 -22.990 1.00 78.88 ? 310 SER B CA 1 ATOM 5415 C C . SER B 1 280 ? 51.639 -54.115 -23.401 1.00 85.03 ? 310 SER B C 1 ATOM 5416 O O . SER B 1 280 ? 52.611 -54.835 -23.635 1.00 87.31 ? 310 SER B O 1 ATOM 5417 C CB . SER B 1 280 ? 49.315 -54.567 -24.137 1.00 77.81 ? 310 SER B CB 1 ATOM 5418 O OG . SER B 1 280 ? 49.669 -55.415 -25.212 1.00 80.19 ? 310 SER B OG 1 ATOM 5419 N N . THR B 1 281 ? 51.682 -52.791 -23.486 1.00 85.22 ? 311 THR B N 1 ATOM 5420 C CA . THR B 1 281 ? 52.921 -52.097 -23.780 1.00 85.98 ? 311 THR B CA 1 ATOM 5421 C C . THR B 1 281 ? 54.020 -52.617 -22.882 1.00 83.52 ? 311 THR B C 1 ATOM 5422 O O . THR B 1 281 ? 55.120 -52.891 -23.346 1.00 83.31 ? 311 THR B O 1 ATOM 5423 C CB . THR B 1 281 ? 52.770 -50.585 -23.583 1.00 85.88 ? 311 THR B CB 1 ATOM 5424 O OG1 . THR B 1 281 ? 51.813 -50.086 -24.524 1.00 88.02 ? 311 THR B OG1 1 ATOM 5425 C CG2 . THR B 1 281 ? 54.106 -49.870 -23.785 1.00 85.88 ? 311 THR B CG2 1 ATOM 5426 N N . TYR B 1 282 ? 53.711 -52.772 -21.602 1.00 81.85 ? 312 TYR B N 1 ATOM 5427 C CA . TYR B 1 282 ? 54.718 -53.167 -20.642 1.00 83.65 ? 312 TYR B CA 1 ATOM 5428 C C . TYR B 1 282 ? 55.181 -54.590 -20.877 1.00 85.23 ? 312 TYR B C 1 ATOM 5429 O O . TYR B 1 282 ? 56.364 -54.823 -21.066 1.00 93.70 ? 312 TYR B O 1 ATOM 5430 C CB . TYR B 1 282 ? 54.221 -53.021 -19.215 1.00 83.62 ? 312 TYR B CB 1 ATOM 5431 C CG . TYR B 1 282 ? 55.256 -53.476 -18.235 1.00 86.78 ? 312 TYR B CG 1 ATOM 5432 C CD1 . TYR B 1 282 ? 56.297 -52.645 -17.868 1.00 89.47 ? 312 TYR B CD1 1 ATOM 5433 C CD2 . TYR B 1 282 ? 55.219 -54.759 -17.708 1.00 88.49 ? 312 TYR B CD2 1 ATOM 5434 C CE1 . TYR B 1 282 ? 57.264 -53.070 -16.981 1.00 94.79 ? 312 TYR B CE1 1 ATOM 5435 C CE2 . TYR B 1 282 ? 56.178 -55.197 -16.823 1.00 90.52 ? 312 TYR B CE2 1 ATOM 5436 C CZ . TYR B 1 282 ? 57.204 -54.358 -16.462 1.00 95.54 ? 312 TYR B CZ 1 ATOM 5437 O OH . TYR B 1 282 ? 58.152 -54.809 -15.571 1.00 97.13 ? 312 TYR B OH 1 ATOM 5438 N N . LEU B 1 283 ? 54.249 -55.533 -20.877 1.00 84.32 ? 313 LEU B N 1 ATOM 5439 C CA . LEU B 1 283 ? 54.580 -56.968 -20.969 1.00 81.32 ? 313 LEU B CA 1 ATOM 5440 C C . LEU B 1 283 ? 55.144 -57.443 -22.323 1.00 82.16 ? 313 LEU B C 1 ATOM 5441 O O . LEU B 1 283 ? 55.778 -58.486 -22.386 1.00 79.78 ? 313 LEU B O 1 ATOM 5442 C CB . LEU B 1 283 ? 53.359 -57.813 -20.618 1.00 78.35 ? 313 LEU B CB 1 ATOM 5443 C CG . LEU B 1 283 ? 52.897 -57.731 -19.166 1.00 77.12 ? 313 LEU B CG 1 ATOM 5444 C CD1 . LEU B 1 283 ? 51.500 -58.317 -19.017 1.00 74.75 ? 313 LEU B CD1 1 ATOM 5445 C CD2 . LEU B 1 283 ? 53.888 -58.432 -18.253 1.00 76.77 ? 313 LEU B CD2 1 ATOM 5446 N N . ASN B 1 284 ? 54.923 -56.688 -23.393 1.00 85.22 ? 314 ASN B N 1 ATOM 5447 C CA . ASN B 1 284 ? 55.512 -57.006 -24.696 1.00 86.67 ? 314 ASN B CA 1 ATOM 5448 C C . ASN B 1 284 ? 56.935 -56.474 -24.869 1.00 91.14 ? 314 ASN B C 1 ATOM 5449 O O . ASN B 1 284 ? 57.621 -56.856 -25.819 1.00 91.24 ? 314 ASN B O 1 ATOM 5450 C CB . ASN B 1 284 ? 54.620 -56.493 -25.819 1.00 86.34 ? 314 ASN B CB 1 ATOM 5451 C CG . ASN B 1 284 ? 53.359 -57.302 -25.954 1.00 85.55 ? 314 ASN B CG 1 ATOM 5452 O OD1 . ASN B 1 284 ? 53.414 -58.488 -26.263 1.00 87.21 ? 314 ASN B OD1 1 ATOM 5453 N ND2 . ASN B 1 284 ? 52.218 -56.679 -25.712 1.00 82.46 ? 314 ASN B ND2 1 ATOM 5454 N N . ASN B 1 285 ? 57.367 -55.591 -23.964 1.00 92.47 ? 315 ASN B N 1 ATOM 5455 C CA . ASN B 1 285 ? 58.768 -55.178 -23.893 1.00 96.39 ? 315 ASN B CA 1 ATOM 5456 C C . ASN B 1 285 ? 59.662 -56.414 -23.845 1.00 95.26 ? 315 ASN B C 1 ATOM 5457 O O . ASN B 1 285 ? 59.597 -57.169 -22.889 1.00 96.43 ? 315 ASN B O 1 ATOM 5458 C CB . ASN B 1 285 ? 59.023 -54.309 -22.652 1.00 95.12 ? 315 ASN B CB 1 ATOM 5459 C CG . ASN B 1 285 ? 60.481 -53.885 -22.513 1.00 97.60 ? 315 ASN B CG 1 ATOM 5460 O OD1 . ASN B 1 285 ? 61.351 -54.340 -23.259 1.00 100.67 ? 315 ASN B OD1 1 ATOM 5461 N ND2 . ASN B 1 285 ? 60.756 -53.027 -21.545 1.00 93.03 ? 315 ASN B ND2 1 ATOM 5462 N N . PRO B 1 286 ? 60.492 -56.627 -24.880 1.00 96.87 ? 316 PRO B N 1 ATOM 5463 C CA . PRO B 1 286 ? 61.327 -57.834 -24.929 1.00 94.79 ? 316 PRO B CA 1 ATOM 5464 C C . PRO B 1 286 ? 62.151 -58.068 -23.662 1.00 92.94 ? 316 PRO B C 1 ATOM 5465 O O . PRO B 1 286 ? 62.394 -59.210 -23.279 1.00 91.67 ? 316 PRO B O 1 ATOM 5466 C CB . PRO B 1 286 ? 62.250 -57.575 -26.124 1.00 99.57 ? 316 PRO B CB 1 ATOM 5467 C CG . PRO B 1 286 ? 61.535 -56.578 -26.974 1.00 99.30 ? 316 PRO B CG 1 ATOM 5468 C CD . PRO B 1 286 ? 60.723 -55.738 -26.038 1.00 98.05 ? 316 PRO B CD 1 ATOM 5469 N N . TYR B 1 287 ? 62.571 -56.991 -23.015 1.00 96.35 ? 317 TYR B N 1 ATOM 5470 C CA . TYR B 1 287 ? 63.345 -57.096 -21.779 1.00 99.81 ? 317 TYR B CA 1 ATOM 5471 C C . TYR B 1 287 ? 62.482 -57.587 -20.604 1.00 99.01 ? 317 TYR B C 1 ATOM 5472 O O . TYR B 1 287 ? 62.965 -58.315 -19.732 1.00 110.36 ? 317 TYR B O 1 ATOM 5473 C CB . TYR B 1 287 ? 64.049 -55.766 -21.464 1.00 101.88 ? 317 TYR B CB 1 ATOM 5474 C CG . TYR B 1 287 ? 65.008 -55.333 -22.565 1.00 103.30 ? 317 TYR B CG 1 ATOM 5475 C CD1 . TYR B 1 287 ? 66.230 -55.973 -22.744 1.00 103.04 ? 317 TYR B CD1 1 ATOM 5476 C CD2 . TYR B 1 287 ? 64.677 -54.304 -23.444 1.00 104.23 ? 317 TYR B CD2 1 ATOM 5477 C CE1 . TYR B 1 287 ? 67.099 -55.595 -23.757 1.00 103.93 ? 317 TYR B CE1 1 ATOM 5478 C CE2 . TYR B 1 287 ? 65.542 -53.922 -24.457 1.00 105.87 ? 317 TYR B CE2 1 ATOM 5479 C CZ . TYR B 1 287 ? 66.751 -54.568 -24.606 1.00 107.01 ? 317 TYR B CZ 1 ATOM 5480 O OH . TYR B 1 287 ? 67.605 -54.186 -25.611 1.00 113.43 ? 317 TYR B OH 1 ATOM 5481 N N . VAL B 1 288 ? 61.210 -57.215 -20.587 1.00 92.81 ? 318 VAL B N 1 ATOM 5482 C CA . VAL B 1 288 ? 60.286 -57.725 -19.574 1.00 90.17 ? 318 VAL B CA 1 ATOM 5483 C C . VAL B 1 288 ? 60.059 -59.220 -19.752 1.00 89.50 ? 318 VAL B C 1 ATOM 5484 O O . VAL B 1 288 ? 60.085 -59.970 -18.773 1.00 89.93 ? 318 VAL B O 1 ATOM 5485 C CB . VAL B 1 288 ? 58.938 -56.984 -19.605 1.00 87.42 ? 318 VAL B CB 1 ATOM 5486 C CG1 . VAL B 1 288 ? 57.918 -57.682 -18.731 1.00 85.50 ? 318 VAL B CG1 1 ATOM 5487 C CG2 . VAL B 1 288 ? 59.121 -55.546 -19.141 1.00 89.73 ? 318 VAL B CG2 1 ATOM 5488 N N . ARG B 1 289 ? 59.833 -59.647 -20.995 1.00 87.01 ? 319 ARG B N 1 ATOM 5489 C CA . ARG B 1 289 ? 59.675 -61.070 -21.310 1.00 82.99 ? 319 ARG B CA 1 ATOM 5490 C C . ARG B 1 289 ? 60.897 -61.872 -20.843 1.00 84.24 ? 319 ARG B C 1 ATOM 5491 O O . ARG B 1 289 ? 60.766 -62.940 -20.245 1.00 82.01 ? 319 ARG B O 1 ATOM 5492 C CB . ARG B 1 289 ? 59.446 -61.260 -22.815 1.00 82.00 ? 319 ARG B CB 1 ATOM 5493 C CG . ARG B 1 289 ? 58.059 -60.859 -23.300 1.00 78.57 ? 319 ARG B CG 1 ATOM 5494 C CD . ARG B 1 289 ? 57.913 -60.981 -24.817 1.00 77.35 ? 319 ARG B CD 1 ATOM 5495 N NE . ARG B 1 289 ? 57.987 -62.363 -25.294 1.00 76.58 ? 319 ARG B NE 1 ATOM 5496 C CZ . ARG B 1 289 ? 57.042 -63.002 -25.985 1.00 76.02 ? 319 ARG B CZ 1 ATOM 5497 N NH1 . ARG B 1 289 ? 55.907 -62.406 -26.335 1.00 75.08 ? 319 ARG B NH1 1 ATOM 5498 N NH2 . ARG B 1 289 ? 57.239 -64.252 -26.359 1.00 73.86 ? 319 ARG B NH2 1 ATOM 5499 N N . LYS B 1 290 ? 62.079 -61.322 -21.092 1.00 88.76 ? 320 LYS B N 1 ATOM 5500 C CA . LYS B 1 290 ? 63.343 -61.900 -20.636 1.00 94.69 ? 320 LYS B CA 1 ATOM 5501 C C . LYS B 1 290 ? 63.410 -62.006 -19.102 1.00 95.53 ? 320 LYS B C 1 ATOM 5502 O O . LYS B 1 290 ? 63.791 -63.048 -18.562 1.00 95.92 ? 320 LYS B O 1 ATOM 5503 C CB . LYS B 1 290 ? 64.491 -61.012 -21.091 1.00 98.12 ? 320 LYS B CB 1 ATOM 5504 C CG . LYS B 1 290 ? 65.891 -61.633 -21.067 1.00 102.71 ? 320 LYS B CG 1 ATOM 5505 C CD . LYS B 1 290 ? 66.906 -60.753 -20.331 1.00 105.15 ? 320 LYS B CD 1 ATOM 5506 C CE . LYS B 1 290 ? 66.784 -59.262 -20.664 1.00 106.32 ? 320 LYS B CE 1 ATOM 5507 N NZ . LYS B 1 290 ? 67.590 -58.363 -19.787 1.00 103.13 ? 320 LYS B NZ 1 ATOM 5508 N N . ALA B 1 291 ? 63.054 -60.920 -18.417 1.00 89.67 ? 321 ALA B N 1 ATOM 5509 C CA . ALA B 1 291 ? 63.089 -60.857 -16.953 1.00 91.02 ? 321 ALA B CA 1 ATOM 5510 C C . ALA B 1 291 ? 62.151 -61.865 -16.322 1.00 89.73 ? 321 ALA B C 1 ATOM 5511 O O . ALA B 1 291 ? 62.388 -62.326 -15.199 1.00 90.54 ? 321 ALA B O 1 ATOM 5512 C CB . ALA B 1 291 ? 62.721 -59.464 -16.481 1.00 89.74 ? 321 ALA B CB 1 ATOM 5513 N N . LEU B 1 292 ? 61.085 -62.172 -17.057 1.00 87.81 ? 322 LEU B N 1 ATOM 5514 C CA . LEU B 1 292 ? 60.048 -63.092 -16.639 1.00 84.13 ? 322 LEU B CA 1 ATOM 5515 C C . LEU B 1 292 ? 60.221 -64.448 -17.288 1.00 84.16 ? 322 LEU B C 1 ATOM 5516 O O . LEU B 1 292 ? 59.275 -65.242 -17.338 1.00 90.38 ? 322 LEU B O 1 ATOM 5517 C CB . LEU B 1 292 ? 58.683 -62.541 -17.041 1.00 83.72 ? 322 LEU B CB 1 ATOM 5518 C CG . LEU B 1 292 ? 58.253 -61.234 -16.394 1.00 83.98 ? 322 LEU B CG 1 ATOM 5519 C CD1 . LEU B 1 292 ? 57.010 -60.702 -17.083 1.00 83.41 ? 322 LEU B CD1 1 ATOM 5520 C CD2 . LEU B 1 292 ? 57.994 -61.429 -14.905 1.00 86.56 ? 322 LEU B CD2 1 ATOM 5521 N N . ASN B 1 293 ? 61.416 -64.716 -17.805 1.00 85.10 ? 323 ASN B N 1 ATOM 5522 C CA . ASN B 1 293 ? 61.768 -66.051 -18.288 1.00 82.76 ? 323 ASN B CA 1 ATOM 5523 C C . ASN B 1 293 ? 60.753 -66.583 -19.304 1.00 81.17 ? 323 ASN B C 1 ATOM 5524 O O . ASN B 1 293 ? 60.368 -67.748 -19.265 1.00 82.52 ? 323 ASN B O 1 ATOM 5525 C CB . ASN B 1 293 ? 61.906 -67.002 -17.088 1.00 79.54 ? 323 ASN B CB 1 ATOM 5526 C CG . ASN B 1 293 ? 62.758 -66.411 -15.975 1.00 80.75 ? 323 ASN B CG 1 ATOM 5527 O OD1 . ASN B 1 293 ? 63.866 -65.951 -16.218 1.00 82.73 ? 323 ASN B OD1 1 ATOM 5528 N ND2 . ASN B 1 293 ? 62.249 -66.423 -14.746 1.00 81.96 ? 323 ASN B ND2 1 ATOM 5529 N N . ILE B 1 294 ? 60.308 -65.711 -20.199 1.00 80.22 ? 324 ILE B N 1 ATOM 5530 C CA . ILE B 1 294 ? 59.366 -66.103 -21.229 1.00 81.91 ? 324 ILE B CA 1 ATOM 5531 C C . ILE B 1 294 ? 60.171 -66.522 -22.446 1.00 87.64 ? 324 ILE B C 1 ATOM 5532 O O . ILE B 1 294 ? 61.060 -65.794 -22.881 1.00 92.38 ? 324 ILE B O 1 ATOM 5533 C CB . ILE B 1 294 ? 58.425 -64.956 -21.631 1.00 80.91 ? 324 ILE B CB 1 ATOM 5534 C CG1 . ILE B 1 294 ? 57.713 -64.359 -20.408 1.00 79.14 ? 324 ILE B CG1 1 ATOM 5535 C CG2 . ILE B 1 294 ? 57.395 -65.445 -22.631 1.00 81.74 ? 324 ILE B CG2 1 ATOM 5536 C CD1 . ILE B 1 294 ? 56.808 -65.318 -19.682 1.00 79.93 ? 324 ILE B CD1 1 ATOM 5537 N N . PRO B 1 295 ? 59.872 -67.698 -23.006 1.00 92.06 ? 325 PRO B N 1 ATOM 5538 C CA . PRO B 1 295 ? 60.531 -68.068 -24.257 1.00 95.91 ? 325 PRO B CA 1 ATOM 5539 C C . PRO B 1 295 ? 60.171 -67.120 -25.401 1.00 94.92 ? 325 PRO B C 1 ATOM 5540 O O . PRO B 1 295 ? 59.025 -66.696 -25.514 1.00 96.76 ? 325 PRO B O 1 ATOM 5541 C CB . PRO B 1 295 ? 60.004 -69.480 -24.531 1.00 96.53 ? 325 PRO B CB 1 ATOM 5542 C CG . PRO B 1 295 ? 59.579 -69.998 -23.198 1.00 95.63 ? 325 PRO B CG 1 ATOM 5543 C CD . PRO B 1 295 ? 59.038 -68.791 -22.484 1.00 94.05 ? 325 PRO B CD 1 ATOM 5544 N N . GLU B 1 296 ? 61.152 -66.804 -26.235 1.00 97.24 ? 326 GLU B N 1 ATOM 5545 C CA . GLU B 1 296 ? 61.012 -65.794 -27.277 1.00 97.84 ? 326 GLU B CA 1 ATOM 5546 C C . GLU B 1 296 ? 59.937 -66.108 -28.311 1.00 100.06 ? 326 GLU B C 1 ATOM 5547 O O . GLU B 1 296 ? 59.178 -65.230 -28.696 1.00 105.42 ? 326 GLU B O 1 ATOM 5548 C CB . GLU B 1 296 ? 62.350 -65.590 -28.001 1.00 100.81 ? 326 GLU B CB 1 ATOM 5549 C CG . GLU B 1 296 ? 62.443 -64.313 -28.840 1.00 98.83 ? 326 GLU B CG 1 ATOM 5550 C CD . GLU B 1 296 ? 63.766 -64.170 -29.563 1.00 99.68 ? 326 GLU B CD 1 ATOM 5551 O OE1 . GLU B 1 296 ? 64.224 -65.168 -30.154 1.00 100.95 ? 326 GLU B OE1 1 ATOM 5552 O OE2 . GLU B 1 296 ? 64.343 -63.063 -29.557 1.00 100.89 ? 326 GLU B OE2 1 ATOM 5553 N N . GLN B 1 297 ? 59.883 -67.349 -28.772 1.00 103.36 ? 327 GLN B N 1 ATOM 5554 C CA . GLN B 1 297 ? 59.031 -67.702 -29.919 1.00 106.17 ? 327 GLN B CA 1 ATOM 5555 C C . GLN B 1 297 ? 57.541 -67.494 -29.684 1.00 99.54 ? 327 GLN B C 1 ATOM 5556 O O . GLN B 1 297 ? 56.774 -67.507 -30.644 1.00 100.68 ? 327 GLN B O 1 ATOM 5557 C CB . GLN B 1 297 ? 59.285 -69.145 -30.391 1.00 111.40 ? 327 GLN B CB 1 ATOM 5558 C CG . GLN B 1 297 ? 58.700 -70.244 -29.506 1.00 114.12 ? 327 GLN B CG 1 ATOM 5559 C CD . GLN B 1 297 ? 59.570 -70.610 -28.305 1.00 118.15 ? 327 GLN B CD 1 ATOM 5560 O OE1 . GLN B 1 297 ? 60.532 -69.911 -27.964 1.00 117.19 ? 327 GLN B OE1 1 ATOM 5561 N NE2 . GLN B 1 297 ? 59.212 -71.711 -27.637 1.00 117.70 ? 327 GLN B NE2 1 ATOM 5562 N N . LEU B 1 298 ? 57.133 -67.318 -28.429 1.00 90.88 ? 328 LEU B N 1 ATOM 5563 C CA . LEU B 1 298 ? 55.717 -67.182 -28.107 1.00 88.80 ? 328 LEU B CA 1 ATOM 5564 C C . LEU B 1 298 ? 55.121 -65.864 -28.631 1.00 85.75 ? 328 LEU B C 1 ATOM 5565 O O . LEU B 1 298 ? 55.806 -64.843 -28.664 1.00 83.73 ? 328 LEU B O 1 ATOM 5566 C CB . LEU B 1 298 ? 55.506 -67.282 -26.595 1.00 90.72 ? 328 LEU B CB 1 ATOM 5567 C CG . LEU B 1 298 ? 55.791 -68.622 -25.927 1.00 90.58 ? 328 LEU B CG 1 ATOM 5568 C CD1 . LEU B 1 298 ? 55.699 -68.476 -24.410 1.00 89.11 ? 328 LEU B CD1 1 ATOM 5569 C CD2 . LEU B 1 298 ? 54.832 -69.694 -26.430 1.00 88.90 ? 328 LEU B CD2 1 ATOM 5570 N N . PRO B 1 299 ? 53.838 -65.885 -29.026 1.00 81.18 ? 329 PRO B N 1 ATOM 5571 C CA . PRO B 1 299 ? 53.194 -64.712 -29.607 1.00 81.99 ? 329 PRO B CA 1 ATOM 5572 C C . PRO B 1 299 ? 53.087 -63.576 -28.613 1.00 84.68 ? 329 PRO B C 1 ATOM 5573 O O . PRO B 1 299 ? 53.371 -63.761 -27.422 1.00 91.28 ? 329 PRO B O 1 ATOM 5574 C CB . PRO B 1 299 ? 51.797 -65.211 -29.992 1.00 80.55 ? 329 PRO B CB 1 ATOM 5575 C CG . PRO B 1 299 ? 51.573 -66.428 -29.170 1.00 80.37 ? 329 PRO B CG 1 ATOM 5576 C CD . PRO B 1 299 ? 52.918 -67.029 -28.912 1.00 81.68 ? 329 PRO B CD 1 ATOM 5577 N N . GLN B 1 300 ? 52.684 -62.408 -29.098 1.00 82.77 ? 330 GLN B N 1 ATOM 5578 C CA . GLN B 1 300 ? 52.595 -61.241 -28.242 1.00 81.45 ? 330 GLN B CA 1 ATOM 5579 C C . GLN B 1 300 ? 51.615 -61.497 -27.108 1.00 78.38 ? 330 GLN B C 1 ATOM 5580 O O . GLN B 1 300 ? 50.738 -62.350 -27.224 1.00 73.12 ? 330 GLN B O 1 ATOM 5581 C CB . GLN B 1 300 ? 52.183 -60.006 -29.051 1.00 83.42 ? 330 GLN B CB 1 ATOM 5582 C CG . GLN B 1 300 ? 50.754 -60.001 -29.572 1.00 82.09 ? 330 GLN B CG 1 ATOM 5583 C CD . GLN B 1 300 ? 50.255 -58.605 -29.926 1.00 82.39 ? 330 GLN B CD 1 ATOM 5584 O OE1 . GLN B 1 300 ? 51.030 -57.722 -30.281 1.00 80.82 ? 330 GLN B OE1 1 ATOM 5585 N NE2 . GLN B 1 300 ? 48.943 -58.403 -29.821 1.00 84.41 ? 330 GLN B NE2 1 ATOM 5586 N N . TRP B 1 301 ? 51.785 -60.773 -26.011 1.00 80.14 ? 331 TRP B N 1 ATOM 5587 C CA . TRP B 1 301 ? 50.854 -60.846 -24.899 1.00 81.33 ? 331 TRP B CA 1 ATOM 5588 C C . TRP B 1 301 ? 49.639 -59.965 -25.175 1.00 85.74 ? 331 TRP B C 1 ATOM 5589 O O . TRP B 1 301 ? 49.784 -58.817 -25.619 1.00 89.92 ? 331 TRP B O 1 ATOM 5590 C CB . TRP B 1 301 ? 51.530 -60.402 -23.608 1.00 81.46 ? 331 TRP B CB 1 ATOM 5591 C CG . TRP B 1 301 ? 50.681 -60.549 -22.376 1.00 81.88 ? 331 TRP B CG 1 ATOM 5592 C CD1 . TRP B 1 301 ? 50.631 -61.619 -21.532 1.00 81.00 ? 331 TRP B CD1 1 ATOM 5593 C CD2 . TRP B 1 301 ? 49.777 -59.585 -21.843 1.00 82.91 ? 331 TRP B CD2 1 ATOM 5594 N NE1 . TRP B 1 301 ? 49.745 -61.387 -20.513 1.00 76.30 ? 331 TRP B NE1 1 ATOM 5595 C CE2 . TRP B 1 301 ? 49.205 -60.146 -20.678 1.00 80.43 ? 331 TRP B CE2 1 ATOM 5596 C CE3 . TRP B 1 301 ? 49.385 -58.299 -22.239 1.00 84.69 ? 331 TRP B CE3 1 ATOM 5597 C CZ2 . TRP B 1 301 ? 48.266 -59.461 -19.895 1.00 79.82 ? 331 TRP B CZ2 1 ATOM 5598 C CZ3 . TRP B 1 301 ? 48.441 -57.618 -21.462 1.00 83.09 ? 331 TRP B CZ3 1 ATOM 5599 C CH2 . TRP B 1 301 ? 47.894 -58.203 -20.305 1.00 79.63 ? 331 TRP B CH2 1 ATOM 5600 N N . ASP B 1 302 ? 48.459 -60.526 -24.913 1.00 81.01 ? 332 ASP B N 1 ATOM 5601 C CA . ASP B 1 302 ? 47.186 -59.821 -24.910 1.00 76.58 ? 332 ASP B CA 1 ATOM 5602 C C . ASP B 1 302 ? 46.480 -60.103 -23.583 1.00 77.87 ? 332 ASP B C 1 ATOM 5603 O O . ASP B 1 302 ? 46.537 -61.224 -23.072 1.00 76.49 ? 332 ASP B O 1 ATOM 5604 C CB . ASP B 1 302 ? 46.280 -60.347 -26.017 1.00 75.94 ? 332 ASP B CB 1 ATOM 5605 C CG . ASP B 1 302 ? 46.822 -60.104 -27.391 1.00 79.79 ? 332 ASP B CG 1 ATOM 5606 O OD1 . ASP B 1 302 ? 47.507 -59.090 -27.609 1.00 79.74 ? 332 ASP B OD1 1 ATOM 5607 O OD2 . ASP B 1 302 ? 46.518 -60.919 -28.277 1.00 85.37 ? 332 ASP B OD2 1 ATOM 5608 N N . MET B 1 303 ? 45.777 -59.114 -23.042 1.00 79.58 ? 333 MET B N 1 ATOM 5609 C CA . MET B 1 303 ? 45.033 -59.325 -21.801 1.00 78.99 ? 333 MET B CA 1 ATOM 5610 C C . MET B 1 303 ? 44.021 -60.440 -21.955 1.00 76.20 ? 333 MET B C 1 ATOM 5611 O O . MET B 1 303 ? 43.839 -61.212 -21.027 1.00 71.77 ? 333 MET B O 1 ATOM 5612 C CB . MET B 1 303 ? 44.345 -58.057 -21.324 1.00 84.84 ? 333 MET B CB 1 ATOM 5613 C CG . MET B 1 303 ? 43.837 -58.151 -19.900 1.00 86.49 ? 333 MET B CG 1 ATOM 5614 S SD . MET B 1 303 ? 42.487 -57.013 -19.608 1.00 101.77 ? 333 MET B SD 1 ATOM 5615 C CE . MET B 1 303 ? 43.390 -55.494 -19.333 1.00 106.83 ? 333 MET B CE 1 ATOM 5616 N N . CYS B 1 304 ? 43.378 -60.538 -23.117 1.00 77.14 ? 334 CYS B N 1 ATOM 5617 C CA . CYS B 1 304 ? 42.551 -61.711 -23.417 1.00 77.50 ? 334 CYS B CA 1 ATOM 5618 C C . CYS B 1 304 ? 42.870 -62.295 -24.770 1.00 77.46 ? 334 CYS B C 1 ATOM 5619 O O . CYS B 1 304 ? 43.391 -61.617 -25.647 1.00 80.65 ? 334 CYS B O 1 ATOM 5620 C CB . CYS B 1 304 ? 41.051 -61.411 -23.347 1.00 76.99 ? 334 CYS B CB 1 ATOM 5621 S SG . CYS B 1 304 ? 40.596 -60.388 -21.943 1.00 81.33 ? 334 CYS B SG 1 ATOM 5622 N N . ASN B 1 305 ? 42.544 -63.571 -24.916 1.00 75.08 ? 335 ASN B N 1 ATOM 5623 C CA . ASN B 1 305 ? 42.667 -64.279 -26.159 1.00 74.35 ? 335 ASN B CA 1 ATOM 5624 C C . ASN B 1 305 ? 41.288 -64.534 -26.746 1.00 79.53 ? 335 ASN B C 1 ATOM 5625 O O . ASN B 1 305 ? 40.491 -65.287 -26.186 1.00 75.90 ? 335 ASN B O 1 ATOM 5626 C CB . ASN B 1 305 ? 43.361 -65.589 -25.897 1.00 77.54 ? 335 ASN B CB 1 ATOM 5627 C CG . ASN B 1 305 ? 43.884 -66.233 -27.159 1.00 79.51 ? 335 ASN B CG 1 ATOM 5628 O OD1 . ASN B 1 305 ? 43.252 -66.177 -28.212 1.00 82.89 ? 335 ASN B OD1 1 ATOM 5629 N ND2 . ASN B 1 305 ? 45.040 -66.871 -27.049 1.00 79.23 ? 335 ASN B ND2 1 ATOM 5630 N N . PHE B 1 306 ? 41.010 -63.886 -27.871 1.00 88.46 ? 336 PHE B N 1 ATOM 5631 C CA . PHE B 1 306 ? 39.768 -64.097 -28.620 1.00 91.78 ? 336 PHE B CA 1 ATOM 5632 C C . PHE B 1 306 ? 39.548 -65.567 -28.978 1.00 85.68 ? 336 PHE B C 1 ATOM 5633 O O . PHE B 1 306 ? 38.424 -66.062 -28.874 1.00 80.38 ? 336 PHE B O 1 ATOM 5634 C CB . PHE B 1 306 ? 39.713 -63.209 -29.887 1.00 103.21 ? 336 PHE B CB 1 ATOM 5635 C CG . PHE B 1 306 ? 40.982 -63.219 -30.726 1.00 116.56 ? 336 PHE B CG 1 ATOM 5636 C CD1 . PHE B 1 306 ? 42.042 -62.353 -30.438 1.00 126.21 ? 336 PHE B CD1 1 ATOM 5637 C CD2 . PHE B 1 306 ? 41.105 -64.067 -31.823 1.00 123.57 ? 336 PHE B CD2 1 ATOM 5638 C CE1 . PHE B 1 306 ? 43.196 -62.350 -31.210 1.00 131.14 ? 336 PHE B CE1 1 ATOM 5639 C CE2 . PHE B 1 306 ? 42.257 -64.065 -32.598 1.00 131.49 ? 336 PHE B CE2 1 ATOM 5640 C CZ . PHE B 1 306 ? 43.303 -63.207 -32.293 1.00 133.14 ? 336 PHE B CZ 1 ATOM 5641 N N . LEU B 1 307 ? 40.603 -66.259 -29.401 1.00 80.86 ? 337 LEU B N 1 ATOM 5642 C CA . LEU B 1 307 ? 40.480 -67.668 -29.762 1.00 86.32 ? 337 LEU B CA 1 ATOM 5643 C C . LEU B 1 307 ? 39.900 -68.440 -28.592 1.00 85.07 ? 337 LEU B C 1 ATOM 5644 O O . LEU B 1 307 ? 38.819 -69.016 -28.699 1.00 84.64 ? 337 LEU B O 1 ATOM 5645 C CB . LEU B 1 307 ? 41.826 -68.291 -30.151 1.00 88.95 ? 337 LEU B CB 1 ATOM 5646 C CG . LEU B 1 307 ? 42.561 -67.708 -31.360 1.00 92.31 ? 337 LEU B CG 1 ATOM 5647 C CD1 . LEU B 1 307 ? 43.952 -68.321 -31.454 1.00 93.43 ? 337 LEU B CD1 1 ATOM 5648 C CD2 . LEU B 1 307 ? 41.762 -67.909 -32.647 1.00 90.06 ? 337 LEU B CD2 1 ATOM 5649 N N . VAL B 1 308 ? 40.615 -68.415 -27.473 1.00 79.90 ? 338 VAL B N 1 ATOM 5650 C CA . VAL B 1 308 ? 40.182 -69.085 -26.262 1.00 75.43 ? 338 VAL B CA 1 ATOM 5651 C C . VAL B 1 308 ? 38.715 -68.770 -26.009 1.00 70.37 ? 338 VAL B C 1 ATOM 5652 O O . VAL B 1 308 ? 37.890 -69.666 -25.947 1.00 69.66 ? 338 VAL B O 1 ATOM 5653 C CB . VAL B 1 308 ? 41.010 -68.652 -25.037 1.00 76.01 ? 338 VAL B CB 1 ATOM 5654 C CG1 . VAL B 1 308 ? 40.389 -69.188 -23.758 1.00 78.29 ? 338 VAL B CG1 1 ATOM 5655 C CG2 . VAL B 1 308 ? 42.446 -69.134 -25.149 1.00 77.48 ? 338 VAL B CG2 1 ATOM 5656 N N . ASN B 1 309 ? 38.395 -67.493 -25.899 1.00 69.10 ? 339 ASN B N 1 ATOM 5657 C CA . ASN B 1 309 ? 37.031 -67.078 -25.580 1.00 71.25 ? 339 ASN B CA 1 ATOM 5658 C C . ASN B 1 309 ? 36.007 -67.592 -26.587 1.00 73.27 ? 339 ASN B C 1 ATOM 5659 O O . ASN B 1 309 ? 35.034 -68.221 -26.203 1.00 73.98 ? 339 ASN B O 1 ATOM 5660 C CB . ASN B 1 309 ? 36.928 -65.557 -25.477 1.00 70.35 ? 339 ASN B CB 1 ATOM 5661 C CG . ASN B 1 309 ? 35.594 -65.096 -24.918 1.00 69.24 ? 339 ASN B CG 1 ATOM 5662 O OD1 . ASN B 1 309 ? 34.629 -64.925 -25.655 1.00 67.11 ? 339 ASN B OD1 1 ATOM 5663 N ND2 . ASN B 1 309 ? 35.542 -64.878 -23.607 1.00 66.41 ? 339 ASN B ND2 1 ATOM 5664 N N . LEU B 1 310 ? 36.240 -67.335 -27.867 1.00 75.73 ? 340 LEU B N 1 ATOM 5665 C CA . LEU B 1 310 ? 35.331 -67.790 -28.914 1.00 79.55 ? 340 LEU B CA 1 ATOM 5666 C C . LEU B 1 310 ? 35.212 -69.309 -29.012 1.00 80.85 ? 340 LEU B C 1 ATOM 5667 O O . LEU B 1 310 ? 34.140 -69.817 -29.307 1.00 79.93 ? 340 LEU B O 1 ATOM 5668 C CB . LEU B 1 310 ? 35.753 -67.231 -30.270 1.00 84.91 ? 340 LEU B CB 1 ATOM 5669 C CG . LEU B 1 310 ? 35.577 -65.717 -30.410 1.00 85.40 ? 340 LEU B CG 1 ATOM 5670 C CD1 . LEU B 1 310 ? 36.185 -65.254 -31.728 1.00 88.72 ? 340 LEU B CD1 1 ATOM 5671 C CD2 . LEU B 1 310 ? 34.116 -65.307 -30.309 1.00 84.04 ? 340 LEU B CD2 1 ATOM 5672 N N . GLN B 1 311 ? 36.297 -70.029 -28.758 1.00 80.12 ? 341 GLN B N 1 ATOM 5673 C CA . GLN B 1 311 ? 36.272 -71.492 -28.813 1.00 83.27 ? 341 GLN B CA 1 ATOM 5674 C C . GLN B 1 311 ? 35.899 -72.163 -27.495 1.00 85.09 ? 341 GLN B C 1 ATOM 5675 O O . GLN B 1 311 ? 35.983 -73.383 -27.391 1.00 91.88 ? 341 GLN B O 1 ATOM 5676 C CB . GLN B 1 311 ? 37.637 -72.018 -29.236 1.00 84.02 ? 341 GLN B CB 1 ATOM 5677 C CG . GLN B 1 311 ? 38.015 -71.682 -30.659 1.00 83.85 ? 341 GLN B CG 1 ATOM 5678 C CD . GLN B 1 311 ? 39.358 -72.249 -31.006 1.00 81.30 ? 341 GLN B CD 1 ATOM 5679 O OE1 . GLN B 1 311 ? 40.371 -71.809 -30.474 1.00 78.04 ? 341 GLN B OE1 1 ATOM 5680 N NE2 . GLN B 1 311 ? 39.374 -73.265 -31.856 1.00 83.15 ? 341 GLN B NE2 1 ATOM 5681 N N . TYR B 1 312 ? 35.497 -71.387 -26.495 1.00 84.29 ? 342 TYR B N 1 ATOM 5682 C CA . TYR B 1 312 ? 35.294 -71.917 -25.144 1.00 81.81 ? 342 TYR B CA 1 ATOM 5683 C C . TYR B 1 312 ? 33.900 -72.478 -24.962 1.00 81.36 ? 342 TYR B C 1 ATOM 5684 O O . TYR B 1 312 ? 32.916 -71.833 -25.303 1.00 80.73 ? 342 TYR B O 1 ATOM 5685 C CB . TYR B 1 312 ? 35.532 -70.831 -24.093 1.00 75.72 ? 342 TYR B CB 1 ATOM 5686 C CG . TYR B 1 312 ? 35.693 -71.352 -22.687 1.00 70.21 ? 342 TYR B CG 1 ATOM 5687 C CD1 . TYR B 1 312 ? 34.588 -71.630 -21.889 1.00 68.67 ? 342 TYR B CD1 1 ATOM 5688 C CD2 . TYR B 1 312 ? 36.954 -71.564 -22.152 1.00 69.75 ? 342 TYR B CD2 1 ATOM 5689 C CE1 . TYR B 1 312 ? 34.731 -72.104 -20.598 1.00 68.37 ? 342 TYR B CE1 1 ATOM 5690 C CE2 . TYR B 1 312 ? 37.115 -72.031 -20.855 1.00 70.18 ? 342 TYR B CE2 1 ATOM 5691 C CZ . TYR B 1 312 ? 36.000 -72.303 -20.083 1.00 69.44 ? 342 TYR B CZ 1 ATOM 5692 O OH . TYR B 1 312 ? 36.172 -72.770 -18.805 1.00 68.42 ? 342 TYR B OH 1 ATOM 5693 N N . ARG B 1 313 ? 33.833 -73.670 -24.385 1.00 86.08 ? 343 ARG B N 1 ATOM 5694 C CA . ARG B 1 313 ? 32.583 -74.385 -24.193 1.00 90.97 ? 343 ARG B CA 1 ATOM 5695 C C . ARG B 1 313 ? 32.186 -74.347 -22.720 1.00 90.16 ? 343 ARG B C 1 ATOM 5696 O O . ARG B 1 313 ? 32.852 -74.928 -21.868 1.00 90.64 ? 343 ARG B O 1 ATOM 5697 C CB . ARG B 1 313 ? 32.755 -75.818 -24.674 1.00 100.11 ? 343 ARG B CB 1 ATOM 5698 C CG . ARG B 1 313 ? 31.464 -76.566 -24.947 1.00 111.04 ? 343 ARG B CG 1 ATOM 5699 C CD . ARG B 1 313 ? 30.984 -76.389 -26.383 1.00 117.98 ? 343 ARG B CD 1 ATOM 5700 N NE . ARG B 1 313 ? 30.044 -77.428 -26.795 1.00 123.74 ? 343 ARG B NE 1 ATOM 5701 C CZ . ARG B 1 313 ? 30.376 -78.677 -27.117 1.00 128.50 ? 343 ARG B CZ 1 ATOM 5702 N NH1 . ARG B 1 313 ? 31.639 -79.084 -27.063 1.00 125.85 ? 343 ARG B NH1 1 ATOM 5703 N NH2 . ARG B 1 313 ? 29.430 -79.532 -27.483 1.00 131.82 ? 343 ARG B NH2 1 ATOM 5704 N N . ARG B 1 314 ? 31.098 -73.646 -22.430 1.00 91.48 ? 344 ARG B N 1 ATOM 5705 C CA . ARG B 1 314 ? 30.619 -73.456 -21.064 1.00 88.82 ? 344 ARG B CA 1 ATOM 5706 C C . ARG B 1 314 ? 29.683 -74.596 -20.690 1.00 85.87 ? 344 ARG B C 1 ATOM 5707 O O . ARG B 1 314 ? 28.674 -74.785 -21.347 1.00 82.52 ? 344 ARG B O 1 ATOM 5708 C CB . ARG B 1 314 ? 29.859 -72.138 -20.958 1.00 90.61 ? 344 ARG B CB 1 ATOM 5709 C CG . ARG B 1 314 ? 30.702 -70.887 -21.122 1.00 89.96 ? 344 ARG B CG 1 ATOM 5710 C CD . ARG B 1 314 ? 29.834 -69.716 -21.560 1.00 97.31 ? 344 ARG B CD 1 ATOM 5711 N NE . ARG B 1 314 ? 30.497 -68.412 -21.490 1.00 97.97 ? 344 ARG B NE 1 ATOM 5712 C CZ . ARG B 1 314 ? 31.205 -67.852 -22.475 1.00 100.68 ? 344 ARG B CZ 1 ATOM 5713 N NH1 . ARG B 1 314 ? 31.374 -68.466 -23.641 1.00 98.15 ? 344 ARG B NH1 1 ATOM 5714 N NH2 . ARG B 1 314 ? 31.756 -66.656 -22.288 1.00 104.61 ? 344 ARG B NH2 1 ATOM 5715 N N . LEU B 1 315 ? 29.995 -75.318 -19.614 1.00 86.23 ? 345 LEU B N 1 ATOM 5716 C CA . LEU B 1 315 ? 29.250 -76.524 -19.238 1.00 85.79 ? 345 LEU B CA 1 ATOM 5717 C C . LEU B 1 315 ? 28.407 -76.339 -17.993 1.00 84.02 ? 345 LEU B C 1 ATOM 5718 O O . LEU B 1 315 ? 27.236 -76.692 -17.986 1.00 82.75 ? 345 LEU B O 1 ATOM 5719 C CB . LEU B 1 315 ? 30.201 -77.685 -19.008 1.00 86.89 ? 345 LEU B CB 1 ATOM 5720 C CG . LEU B 1 315 ? 31.187 -77.936 -20.137 1.00 87.53 ? 345 LEU B CG 1 ATOM 5721 C CD1 . LEU B 1 315 ? 32.201 -78.978 -19.696 1.00 88.74 ? 345 LEU B CD1 1 ATOM 5722 C CD2 . LEU B 1 315 ? 30.443 -78.349 -21.396 1.00 86.57 ? 345 LEU B CD2 1 ATOM 5723 N N . TYR B 1 316 ? 29.008 -75.813 -16.932 1.00 82.67 ? 346 TYR B N 1 ATOM 5724 C CA . TYR B 1 316 ? 28.269 -75.576 -15.696 1.00 81.02 ? 346 TYR B CA 1 ATOM 5725 C C . TYR B 1 316 ? 27.429 -74.323 -15.822 1.00 78.93 ? 346 TYR B C 1 ATOM 5726 O O . TYR B 1 316 ? 27.914 -73.275 -16.251 1.00 78.87 ? 346 TYR B O 1 ATOM 5727 C CB . TYR B 1 316 ? 29.193 -75.446 -14.497 1.00 79.79 ? 346 TYR B CB 1 ATOM 5728 C CG . TYR B 1 316 ? 30.058 -76.649 -14.266 1.00 80.40 ? 346 TYR B CG 1 ATOM 5729 C CD1 . TYR B 1 316 ? 29.510 -77.864 -13.875 1.00 80.81 ? 346 TYR B CD1 1 ATOM 5730 C CD2 . TYR B 1 316 ? 31.435 -76.572 -14.443 1.00 78.61 ? 346 TYR B CD2 1 ATOM 5731 C CE1 . TYR B 1 316 ? 30.317 -78.971 -13.663 1.00 81.72 ? 346 TYR B CE1 1 ATOM 5732 C CE2 . TYR B 1 316 ? 32.247 -77.665 -14.234 1.00 78.60 ? 346 TYR B CE2 1 ATOM 5733 C CZ . TYR B 1 316 ? 31.693 -78.862 -13.837 1.00 81.09 ? 346 TYR B CZ 1 ATOM 5734 O OH . TYR B 1 316 ? 32.534 -79.937 -13.637 1.00 80.75 ? 346 TYR B OH 1 ATOM 5735 N N . ARG B 1 317 ? 26.170 -74.471 -15.431 1.00 79.89 ? 347 ARG B N 1 ATOM 5736 C CA . ARG B 1 317 ? 25.147 -73.453 -15.524 1.00 80.07 ? 347 ARG B CA 1 ATOM 5737 C C . ARG B 1 317 ? 24.868 -72.823 -14.137 1.00 79.12 ? 347 ARG B C 1 ATOM 5738 O O . ARG B 1 317 ? 24.200 -71.792 -14.024 1.00 83.13 ? 347 ARG B O 1 ATOM 5739 C CB . ARG B 1 317 ? 23.891 -74.126 -16.079 1.00 82.53 ? 347 ARG B CB 1 ATOM 5740 C CG . ARG B 1 317 ? 22.958 -73.256 -16.891 1.00 86.93 ? 347 ARG B CG 1 ATOM 5741 C CD . ARG B 1 317 ? 23.671 -72.409 -17.942 1.00 88.15 ? 347 ARG B CD 1 ATOM 5742 N NE . ARG B 1 317 ? 24.682 -73.119 -18.713 1.00 84.85 ? 347 ARG B NE 1 ATOM 5743 C CZ . ARG B 1 317 ? 25.355 -72.585 -19.729 1.00 83.11 ? 347 ARG B CZ 1 ATOM 5744 N NH1 . ARG B 1 317 ? 25.155 -71.326 -20.105 1.00 80.48 ? 347 ARG B NH1 1 ATOM 5745 N NH2 . ARG B 1 317 ? 26.239 -73.320 -20.384 1.00 87.61 ? 347 ARG B NH2 1 ATOM 5746 N N . SER B 1 318 ? 25.416 -73.427 -13.088 1.00 78.03 ? 348 SER B N 1 ATOM 5747 C CA . SER B 1 318 ? 25.239 -72.942 -11.723 1.00 76.04 ? 348 SER B CA 1 ATOM 5748 C C . SER B 1 318 ? 26.233 -73.618 -10.789 1.00 74.77 ? 348 SER B C 1 ATOM 5749 O O . SER B 1 318 ? 26.494 -74.806 -10.917 1.00 74.03 ? 348 SER B O 1 ATOM 5750 C CB . SER B 1 318 ? 23.827 -73.237 -11.250 1.00 79.17 ? 348 SER B CB 1 ATOM 5751 O OG . SER B 1 318 ? 23.668 -72.937 -9.876 1.00 84.29 ? 348 SER B OG 1 ATOM 5752 N N . MET B 1 319 ? 26.780 -72.862 -9.843 1.00 75.46 ? 349 MET B N 1 ATOM 5753 C CA . MET B 1 319 ? 27.785 -73.390 -8.914 1.00 76.59 ? 349 MET B CA 1 ATOM 5754 C C . MET B 1 319 ? 27.177 -73.840 -7.588 1.00 79.85 ? 349 MET B C 1 ATOM 5755 O O . MET B 1 319 ? 27.891 -74.098 -6.622 1.00 76.79 ? 349 MET B O 1 ATOM 5756 C CB . MET B 1 319 ? 28.876 -72.352 -8.662 1.00 74.04 ? 349 MET B CB 1 ATOM 5757 C CG . MET B 1 319 ? 29.711 -72.039 -9.898 1.00 70.10 ? 349 MET B CG 1 ATOM 5758 S SD . MET B 1 319 ? 30.924 -73.311 -10.292 1.00 67.41 ? 349 MET B SD 1 ATOM 5759 C CE . MET B 1 319 ? 30.076 -74.245 -11.545 1.00 69.40 ? 349 MET B CE 1 ATOM 5760 N N . ASN B 1 320 ? 25.856 -73.940 -7.554 1.00 83.78 ? 350 ASN B N 1 ATOM 5761 C CA . ASN B 1 320 ? 25.147 -74.432 -6.384 1.00 87.87 ? 350 ASN B CA 1 ATOM 5762 C C . ASN B 1 320 ? 25.680 -75.769 -5.831 1.00 90.70 ? 350 ASN B C 1 ATOM 5763 O O . ASN B 1 320 ? 25.911 -75.902 -4.629 1.00 91.05 ? 350 ASN B O 1 ATOM 5764 C CB . ASN B 1 320 ? 23.676 -74.570 -6.726 1.00 89.99 ? 350 ASN B CB 1 ATOM 5765 C CG . ASN B 1 320 ? 22.848 -74.917 -5.524 1.00 90.32 ? 350 ASN B CG 1 ATOM 5766 O OD1 . ASN B 1 320 ? 22.487 -76.071 -5.320 1.00 94.79 ? 350 ASN B OD1 1 ATOM 5767 N ND2 . ASN B 1 320 ? 22.573 -73.925 -4.701 1.00 86.20 ? 350 ASN B ND2 1 ATOM 5768 N N . SER B 1 321 ? 25.882 -76.751 -6.700 1.00 91.16 ? 351 SER B N 1 ATOM 5769 C CA . SER B 1 321 ? 26.405 -78.036 -6.254 1.00 94.59 ? 351 SER B CA 1 ATOM 5770 C C . SER B 1 321 ? 27.758 -77.859 -5.598 1.00 92.84 ? 351 SER B C 1 ATOM 5771 O O . SER B 1 321 ? 27.978 -78.262 -4.457 1.00 93.81 ? 351 SER B O 1 ATOM 5772 C CB . SER B 1 321 ? 26.549 -79.000 -7.429 1.00 94.71 ? 351 SER B CB 1 ATOM 5773 O OG . SER B 1 321 ? 25.326 -79.123 -8.118 1.00 95.11 ? 351 SER B OG 1 ATOM 5774 N N . GLN B 1 322 ? 28.656 -77.226 -6.332 1.00 89.88 ? 352 GLN B N 1 ATOM 5775 C CA . GLN B 1 322 ? 30.044 -77.138 -5.933 1.00 91.52 ? 352 GLN B CA 1 ATOM 5776 C C . GLN B 1 322 ? 30.186 -76.479 -4.570 1.00 92.73 ? 352 GLN B C 1 ATOM 5777 O O . GLN B 1 322 ? 31.000 -76.908 -3.752 1.00 97.51 ? 352 GLN B O 1 ATOM 5778 C CB . GLN B 1 322 ? 30.858 -76.375 -6.984 1.00 88.39 ? 352 GLN B CB 1 ATOM 5779 C CG . GLN B 1 322 ? 31.071 -77.124 -8.295 1.00 87.67 ? 352 GLN B CG 1 ATOM 5780 C CD . GLN B 1 322 ? 29.879 -77.094 -9.245 1.00 87.99 ? 352 GLN B CD 1 ATOM 5781 O OE1 . GLN B 1 322 ? 28.857 -76.478 -8.964 1.00 82.26 ? 352 GLN B OE1 1 ATOM 5782 N NE2 . GLN B 1 322 ? 30.009 -77.787 -10.381 1.00 91.68 ? 352 GLN B NE2 1 ATOM 5783 N N . TYR B 1 323 ? 29.377 -75.459 -4.319 1.00 92.24 ? 353 TYR B N 1 ATOM 5784 C CA . TYR B 1 323 ? 29.482 -74.694 -3.081 1.00 91.65 ? 353 TYR B CA 1 ATOM 5785 C C . TYR B 1 323 ? 28.928 -75.480 -1.891 1.00 92.17 ? 353 TYR B C 1 ATOM 5786 O O . TYR B 1 323 ? 29.552 -75.515 -0.830 1.00 92.88 ? 353 TYR B O 1 ATOM 5787 C CB . TYR B 1 323 ? 28.802 -73.326 -3.207 1.00 90.88 ? 353 TYR B CB 1 ATOM 5788 C CG . TYR B 1 323 ? 29.675 -72.257 -3.839 1.00 88.35 ? 353 TYR B CG 1 ATOM 5789 C CD1 . TYR B 1 323 ? 30.681 -71.642 -3.114 1.00 85.54 ? 353 TYR B CD1 1 ATOM 5790 C CD2 . TYR B 1 323 ? 29.489 -71.866 -5.159 1.00 89.58 ? 353 TYR B CD2 1 ATOM 5791 C CE1 . TYR B 1 323 ? 31.476 -70.672 -3.682 1.00 84.17 ? 353 TYR B CE1 1 ATOM 5792 C CE2 . TYR B 1 323 ? 30.282 -70.898 -5.740 1.00 87.04 ? 353 TYR B CE2 1 ATOM 5793 C CZ . TYR B 1 323 ? 31.279 -70.301 -5.000 1.00 86.46 ? 353 TYR B CZ 1 ATOM 5794 O OH . TYR B 1 323 ? 32.074 -69.326 -5.583 1.00 84.36 ? 353 TYR B OH 1 ATOM 5795 N N . LEU B 1 324 ? 27.790 -76.139 -2.074 1.00 93.93 ? 354 LEU B N 1 ATOM 5796 C CA . LEU B 1 324 ? 27.259 -77.027 -1.032 1.00 97.70 ? 354 LEU B CA 1 ATOM 5797 C C . LEU B 1 324 ? 28.238 -78.166 -0.753 1.00 100.37 ? 354 LEU B C 1 ATOM 5798 O O . LEU B 1 324 ? 28.515 -78.501 0.398 1.00 105.20 ? 354 LEU B O 1 ATOM 5799 C CB . LEU B 1 324 ? 25.908 -77.603 -1.438 1.00 96.12 ? 354 LEU B CB 1 ATOM 5800 C CG . LEU B 1 324 ? 24.772 -76.599 -1.602 1.00 95.52 ? 354 LEU B CG 1 ATOM 5801 C CD1 . LEU B 1 324 ? 23.576 -77.253 -2.279 1.00 95.24 ? 354 LEU B CD1 1 ATOM 5802 C CD2 . LEU B 1 324 ? 24.386 -75.986 -0.264 1.00 98.22 ? 354 LEU B CD2 1 ATOM 5803 N N . LYS B 1 325 ? 28.781 -78.734 -1.821 1.00 101.19 ? 355 LYS B N 1 ATOM 5804 C CA . LYS B 1 325 ? 29.792 -79.766 -1.708 1.00 102.10 ? 355 LYS B CA 1 ATOM 5805 C C . LYS B 1 325 ? 31.035 -79.284 -0.967 1.00 96.53 ? 355 LYS B C 1 ATOM 5806 O O . LYS B 1 325 ? 31.677 -80.051 -0.280 1.00 98.24 ? 355 LYS B O 1 ATOM 5807 C CB . LYS B 1 325 ? 30.165 -80.264 -3.098 1.00 105.62 ? 355 LYS B CB 1 ATOM 5808 C CG . LYS B 1 325 ? 30.871 -81.601 -3.095 1.00 112.43 ? 355 LYS B CG 1 ATOM 5809 C CD . LYS B 1 325 ? 31.123 -82.092 -4.513 1.00 114.52 ? 355 LYS B CD 1 ATOM 5810 C CE . LYS B 1 325 ? 29.856 -82.588 -5.186 1.00 114.29 ? 355 LYS B CE 1 ATOM 5811 N NZ . LYS B 1 325 ? 30.192 -83.455 -6.343 1.00 116.30 ? 355 LYS B NZ 1 ATOM 5812 N N . LEU B 1 326 ? 31.370 -78.013 -1.109 1.00 96.67 ? 356 LEU B N 1 ATOM 5813 C CA . LEU B 1 326 ? 32.484 -77.429 -0.366 1.00 100.55 ? 356 LEU B CA 1 ATOM 5814 C C . LEU B 1 326 ? 32.074 -77.033 1.053 1.00 103.77 ? 356 LEU B C 1 ATOM 5815 O O . LEU B 1 326 ? 32.900 -76.991 1.961 1.00 108.45 ? 356 LEU B O 1 ATOM 5816 C CB . LEU B 1 326 ? 33.032 -76.208 -1.099 1.00 100.22 ? 356 LEU B CB 1 ATOM 5817 C CG . LEU B 1 326 ? 33.800 -76.494 -2.398 1.00 103.63 ? 356 LEU B CG 1 ATOM 5818 C CD1 . LEU B 1 326 ? 33.703 -75.320 -3.360 1.00 102.50 ? 356 LEU B CD1 1 ATOM 5819 C CD2 . LEU B 1 326 ? 35.256 -76.837 -2.128 1.00 103.67 ? 356 LEU B CD2 1 ATOM 5820 N N . LEU B 1 327 ? 30.797 -76.738 1.241 1.00 104.66 ? 357 LEU B N 1 ATOM 5821 C CA . LEU B 1 327 ? 30.296 -76.326 2.549 1.00 104.58 ? 357 LEU B CA 1 ATOM 5822 C C . LEU B 1 327 ? 30.019 -77.493 3.461 1.00 107.69 ? 357 LEU B C 1 ATOM 5823 O O . LEU B 1 327 ? 30.106 -77.348 4.667 1.00 108.94 ? 357 LEU B O 1 ATOM 5824 C CB . LEU B 1 327 ? 29.025 -75.518 2.399 1.00 102.01 ? 357 LEU B CB 1 ATOM 5825 C CG . LEU B 1 327 ? 29.261 -74.085 1.957 1.00 100.89 ? 357 LEU B CG 1 ATOM 5826 C CD1 . LEU B 1 327 ? 27.982 -73.550 1.339 1.00 102.45 ? 357 LEU B CD1 1 ATOM 5827 C CD2 . LEU B 1 327 ? 29.735 -73.229 3.123 1.00 98.17 ? 357 LEU B CD2 1 ATOM 5828 N N . SER B 1 328 ? 29.671 -78.636 2.884 1.00 107.70 ? 358 SER B N 1 ATOM 5829 C CA . SER B 1 328 ? 29.329 -79.817 3.665 1.00 114.60 ? 358 SER B CA 1 ATOM 5830 C C . SER B 1 328 ? 30.458 -80.211 4.608 1.00 117.74 ? 358 SER B C 1 ATOM 5831 O O . SER B 1 328 ? 30.214 -80.506 5.778 1.00 120.18 ? 358 SER B O 1 ATOM 5832 C CB . SER B 1 328 ? 29.015 -80.991 2.743 1.00 114.37 ? 358 SER B CB 1 ATOM 5833 O OG . SER B 1 328 ? 30.185 -81.403 2.065 1.00 111.60 ? 358 SER B OG 1 ATOM 5834 N N . SER B 1 329 ? 31.685 -80.217 4.094 1.00 114.83 ? 359 SER B N 1 ATOM 5835 C CA . SER B 1 329 ? 32.857 -80.561 4.900 1.00 115.02 ? 359 SER B CA 1 ATOM 5836 C C . SER B 1 329 ? 33.026 -79.616 6.083 1.00 115.85 ? 359 SER B C 1 ATOM 5837 O O . SER B 1 329 ? 33.386 -80.043 7.175 1.00 121.53 ? 359 SER B O 1 ATOM 5838 C CB . SER B 1 329 ? 34.127 -80.519 4.055 1.00 113.25 ? 359 SER B CB 1 ATOM 5839 O OG . SER B 1 329 ? 34.567 -79.185 3.889 1.00 107.84 ? 359 SER B OG 1 ATOM 5840 N N . GLN B 1 330 ? 32.770 -78.334 5.846 1.00 109.33 ? 360 GLN B N 1 ATOM 5841 C CA . GLN B 1 330 ? 32.931 -77.277 6.854 1.00 109.96 ? 360 GLN B CA 1 ATOM 5842 C C . GLN B 1 330 ? 34.361 -77.034 7.323 1.00 110.10 ? 360 GLN B C 1 ATOM 5843 O O . GLN B 1 330 ? 34.584 -76.503 8.402 1.00 104.11 ? 360 GLN B O 1 ATOM 5844 C CB . GLN B 1 330 ? 31.999 -77.489 8.045 1.00 116.51 ? 360 GLN B CB 1 ATOM 5845 C CG . GLN B 1 330 ? 30.555 -77.184 7.701 1.00 120.93 ? 360 GLN B CG 1 ATOM 5846 C CD . GLN B 1 330 ? 29.566 -77.431 8.806 1.00 125.43 ? 360 GLN B CD 1 ATOM 5847 O OE1 . GLN B 1 330 ? 28.408 -77.710 8.525 1.00 125.94 ? 360 GLN B OE1 1 ATOM 5848 N NE2 . GLN B 1 330 ? 29.995 -77.294 10.062 1.00 126.80 ? 360 GLN B NE2 1 ATOM 5849 N N . LYS B 1 331 ? 35.327 -77.390 6.486 1.00 115.77 ? 361 LYS B N 1 ATOM 5850 C CA . LYS B 1 331 ? 36.710 -77.030 6.730 1.00 113.78 ? 361 LYS B CA 1 ATOM 5851 C C . LYS B 1 331 ? 37.024 -75.703 6.072 1.00 110.55 ? 361 LYS B C 1 ATOM 5852 O O . LYS B 1 331 ? 38.064 -75.120 6.350 1.00 113.03 ? 361 LYS B O 1 ATOM 5853 C CB . LYS B 1 331 ? 37.649 -78.086 6.159 1.00 117.74 ? 361 LYS B CB 1 ATOM 5854 C CG . LYS B 1 331 ? 37.356 -79.501 6.608 1.00 122.68 ? 361 LYS B CG 1 ATOM 5855 C CD . LYS B 1 331 ? 38.338 -80.463 5.971 1.00 126.94 ? 361 LYS B CD 1 ATOM 5856 C CE . LYS B 1 331 ? 38.132 -81.882 6.478 1.00 131.04 ? 361 LYS B CE 1 ATOM 5857 N NZ . LYS B 1 331 ? 39.126 -82.817 5.888 1.00 127.77 ? 361 LYS B NZ 1 ATOM 5858 N N . TYR B 1 332 ? 36.126 -75.220 5.210 1.00 107.57 ? 362 TYR B N 1 ATOM 5859 C CA . TYR B 1 332 ? 36.470 -74.152 4.268 1.00 103.66 ? 362 TYR B CA 1 ATOM 5860 C C . TYR B 1 332 ? 35.707 -72.834 4.488 1.00 106.34 ? 362 TYR B C 1 ATOM 5861 O O . TYR B 1 332 ? 34.481 -72.809 4.575 1.00 102.28 ? 362 TYR B O 1 ATOM 5862 C CB . TYR B 1 332 ? 36.311 -74.653 2.815 1.00 96.75 ? 362 TYR B CB 1 ATOM 5863 C CG . TYR B 1 332 ? 37.019 -75.977 2.543 1.00 93.80 ? 362 TYR B CG 1 ATOM 5864 C CD1 . TYR B 1 332 ? 38.352 -76.165 2.906 1.00 92.91 ? 362 TYR B CD1 1 ATOM 5865 C CD2 . TYR B 1 332 ? 36.352 -77.045 1.946 1.00 90.58 ? 362 TYR B CD2 1 ATOM 5866 C CE1 . TYR B 1 332 ? 38.990 -77.369 2.674 1.00 90.42 ? 362 TYR B CE1 1 ATOM 5867 C CE2 . TYR B 1 332 ? 36.988 -78.253 1.725 1.00 90.63 ? 362 TYR B CE2 1 ATOM 5868 C CZ . TYR B 1 332 ? 38.308 -78.403 2.090 1.00 90.43 ? 362 TYR B CZ 1 ATOM 5869 O OH . TYR B 1 332 ? 38.958 -79.589 1.869 1.00 92.78 ? 362 TYR B OH 1 ATOM 5870 N N . GLN B 1 333 ? 36.465 -71.744 4.557 1.00 110.02 ? 363 GLN B N 1 ATOM 5871 C CA . GLN B 1 333 ? 35.936 -70.398 4.760 1.00 112.22 ? 363 GLN B CA 1 ATOM 5872 C C . GLN B 1 333 ? 35.746 -69.691 3.401 1.00 106.49 ? 363 GLN B C 1 ATOM 5873 O O . GLN B 1 333 ? 36.720 -69.402 2.699 1.00 104.50 ? 363 GLN B O 1 ATOM 5874 C CB . GLN B 1 333 ? 36.927 -69.624 5.622 1.00 120.99 ? 363 GLN B CB 1 ATOM 5875 C CG . GLN B 1 333 ? 36.455 -68.269 6.123 1.00 130.77 ? 363 GLN B CG 1 ATOM 5876 C CD . GLN B 1 333 ? 37.614 -67.331 6.459 1.00 142.07 ? 363 GLN B CD 1 ATOM 5877 O OE1 . GLN B 1 333 ? 38.785 -67.694 6.327 1.00 148.13 ? 363 GLN B OE1 1 ATOM 5878 N NE2 . GLN B 1 333 ? 37.289 -66.112 6.881 1.00 148.26 ? 363 GLN B NE2 1 ATOM 5879 N N . ILE B 1 334 ? 34.499 -69.402 3.042 1.00 99.45 ? 364 ILE B N 1 ATOM 5880 C CA . ILE B 1 334 ? 34.158 -68.908 1.691 1.00 93.53 ? 364 ILE B CA 1 ATOM 5881 C C . ILE B 1 334 ? 33.637 -67.462 1.694 1.00 86.63 ? 364 ILE B C 1 ATOM 5882 O O . ILE B 1 334 ? 32.795 -67.113 2.520 1.00 84.02 ? 364 ILE B O 1 ATOM 5883 C CB . ILE B 1 334 ? 33.081 -69.806 1.041 1.00 92.94 ? 364 ILE B CB 1 ATOM 5884 C CG1 . ILE B 1 334 ? 33.582 -71.249 0.932 1.00 90.54 ? 364 ILE B CG1 1 ATOM 5885 C CG2 . ILE B 1 334 ? 32.667 -69.260 -0.323 1.00 92.91 ? 364 ILE B CG2 1 ATOM 5886 C CD1 . ILE B 1 334 ? 32.509 -72.247 0.569 1.00 89.28 ? 364 ILE B CD1 1 ATOM 5887 N N . LEU B 1 335 ? 34.129 -66.643 0.766 1.00 76.58 ? 365 LEU B N 1 ATOM 5888 C CA . LEU B 1 335 ? 33.663 -65.258 0.602 1.00 73.21 ? 365 LEU B CA 1 ATOM 5889 C C . LEU B 1 335 ? 33.291 -64.938 -0.844 1.00 72.23 ? 365 LEU B C 1 ATOM 5890 O O . LEU B 1 335 ? 34.056 -65.198 -1.788 1.00 71.52 ? 365 LEU B O 1 ATOM 5891 C CB . LEU B 1 335 ? 34.735 -64.261 1.020 1.00 70.66 ? 365 LEU B CB 1 ATOM 5892 C CG . LEU B 1 335 ? 34.442 -62.769 0.814 1.00 69.08 ? 365 LEU B CG 1 ATOM 5893 C CD1 . LEU B 1 335 ? 33.465 -62.271 1.864 1.00 69.18 ? 365 LEU B CD1 1 ATOM 5894 C CD2 . LEU B 1 335 ? 35.719 -61.934 0.844 1.00 66.52 ? 365 LEU B CD2 1 ATOM 5895 N N . LEU B 1 336 ? 32.112 -64.369 -1.010 1.00 67.71 ? 366 LEU B N 1 ATOM 5896 C CA . LEU B 1 336 ? 31.723 -63.815 -2.275 1.00 65.17 ? 366 LEU B CA 1 ATOM 5897 C C . LEU B 1 336 ? 31.594 -62.341 -2.021 1.00 66.10 ? 366 LEU B C 1 ATOM 5898 O O . LEU B 1 336 ? 30.860 -61.917 -1.126 1.00 66.10 ? 366 LEU B O 1 ATOM 5899 C CB . LEU B 1 336 ? 30.414 -64.415 -2.772 1.00 63.95 ? 366 LEU B CB 1 ATOM 5900 C CG . LEU B 1 336 ? 30.540 -65.643 -3.668 1.00 63.67 ? 366 LEU B CG 1 ATOM 5901 C CD1 . LEU B 1 336 ? 30.864 -66.887 -2.870 1.00 67.01 ? 366 LEU B CD1 1 ATOM 5902 C CD2 . LEU B 1 336 ? 29.254 -65.864 -4.423 1.00 63.66 ? 366 LEU B CD2 1 ATOM 5903 N N . TYR B 1 337 ? 32.334 -61.561 -2.797 1.00 69.49 ? 367 TYR B N 1 ATOM 5904 C CA . TYR B 1 337 ? 32.246 -60.114 -2.718 1.00 68.26 ? 367 TYR B CA 1 ATOM 5905 C C . TYR B 1 337 ? 31.952 -59.526 -4.089 1.00 64.41 ? 367 TYR B C 1 ATOM 5906 O O . TYR B 1 337 ? 32.338 -60.092 -5.105 1.00 61.25 ? 367 TYR B O 1 ATOM 5907 C CB . TYR B 1 337 ? 33.522 -59.527 -2.119 1.00 67.97 ? 367 TYR B CB 1 ATOM 5908 C CG . TYR B 1 337 ? 34.757 -59.710 -2.968 1.00 65.84 ? 367 TYR B CG 1 ATOM 5909 C CD1 . TYR B 1 337 ? 35.469 -60.896 -2.938 1.00 64.35 ? 367 TYR B CD1 1 ATOM 5910 C CD2 . TYR B 1 337 ? 35.232 -58.674 -3.779 1.00 64.43 ? 367 TYR B CD2 1 ATOM 5911 C CE1 . TYR B 1 337 ? 36.608 -61.055 -3.704 1.00 65.58 ? 367 TYR B CE1 1 ATOM 5912 C CE2 . TYR B 1 337 ? 36.372 -58.826 -4.553 1.00 62.94 ? 367 TYR B CE2 1 ATOM 5913 C CZ . TYR B 1 337 ? 37.059 -60.013 -4.513 1.00 63.20 ? 367 TYR B CZ 1 ATOM 5914 O OH . TYR B 1 337 ? 38.184 -60.164 -5.288 1.00 60.59 ? 367 TYR B OH 1 ATOM 5915 N N . ASN B 1 338 ? 31.255 -58.402 -4.107 1.00 64.86 ? 368 ASN B N 1 ATOM 5916 C CA . ASN B 1 338 ? 30.814 -57.796 -5.351 1.00 68.47 ? 368 ASN B CA 1 ATOM 5917 C C . ASN B 1 338 ? 30.866 -56.265 -5.314 1.00 66.47 ? 368 ASN B C 1 ATOM 5918 O O . ASN B 1 338 ? 30.459 -55.654 -4.332 1.00 71.70 ? 368 ASN B O 1 ATOM 5919 C CB . ASN B 1 338 ? 29.381 -58.249 -5.687 1.00 70.89 ? 368 ASN B CB 1 ATOM 5920 C CG . ASN B 1 338 ? 29.315 -59.635 -6.347 1.00 73.78 ? 368 ASN B CG 1 ATOM 5921 O OD1 . ASN B 1 338 ? 29.656 -60.662 -5.742 1.00 75.54 ? 368 ASN B OD1 1 ATOM 5922 N ND2 . ASN B 1 338 ? 28.826 -59.669 -7.585 1.00 71.62 ? 368 ASN B ND2 1 ATOM 5923 N N . GLY B 1 339 ? 31.381 -55.657 -6.381 1.00 59.83 ? 369 GLY B N 1 ATOM 5924 C CA . GLY B 1 339 ? 31.208 -54.241 -6.604 1.00 57.78 ? 369 GLY B CA 1 ATOM 5925 C C . GLY B 1 339 ? 29.766 -53.943 -6.946 1.00 56.34 ? 369 GLY B C 1 ATOM 5926 O O . GLY B 1 339 ? 29.197 -54.559 -7.841 1.00 55.58 ? 369 GLY B O 1 ATOM 5927 N N . ASP B 1 340 ? 29.162 -52.998 -6.235 1.00 55.72 ? 370 ASP B N 1 ATOM 5928 C CA . ASP B 1 340 ? 27.724 -52.776 -6.384 1.00 57.30 ? 370 ASP B CA 1 ATOM 5929 C C . ASP B 1 340 ? 27.323 -51.809 -7.515 1.00 56.68 ? 370 ASP B C 1 ATOM 5930 O O . ASP B 1 340 ? 26.150 -51.442 -7.638 1.00 56.45 ? 370 ASP B O 1 ATOM 5931 C CB . ASP B 1 340 ? 27.101 -52.350 -5.055 1.00 59.08 ? 370 ASP B CB 1 ATOM 5932 C CG . ASP B 1 340 ? 27.476 -50.922 -4.645 1.00 62.26 ? 370 ASP B CG 1 ATOM 5933 O OD1 . ASP B 1 340 ? 28.449 -50.351 -5.179 1.00 55.01 ? 370 ASP B OD1 1 ATOM 5934 O OD2 . ASP B 1 340 ? 26.764 -50.379 -3.777 1.00 66.46 ? 370 ASP B OD2 1 ATOM 5935 N N . VAL B 1 341 ? 28.281 -51.410 -8.340 1.00 55.79 ? 371 VAL B N 1 ATOM 5936 C CA . VAL B 1 341 ? 27.967 -50.693 -9.574 1.00 56.61 ? 371 VAL B CA 1 ATOM 5937 C C . VAL B 1 341 ? 28.451 -51.438 -10.845 1.00 59.33 ? 371 VAL B C 1 ATOM 5938 O O . VAL B 1 341 ? 28.578 -50.842 -11.918 1.00 60.67 ? 371 VAL B O 1 ATOM 5939 C CB . VAL B 1 341 ? 28.498 -49.263 -9.494 1.00 56.03 ? 371 VAL B CB 1 ATOM 5940 C CG1 . VAL B 1 341 ? 27.825 -48.547 -8.333 1.00 58.81 ? 371 VAL B CG1 1 ATOM 5941 C CG2 . VAL B 1 341 ? 30.006 -49.245 -9.315 1.00 56.17 ? 371 VAL B CG2 1 ATOM 5942 N N . ASP B 1 342 ? 28.708 -52.739 -10.710 1.00 58.18 ? 372 ASP B N 1 ATOM 5943 C CA . ASP B 1 342 ? 29.054 -53.595 -11.834 1.00 57.79 ? 372 ASP B CA 1 ATOM 5944 C C . ASP B 1 342 ? 27.819 -54.221 -12.446 1.00 60.03 ? 372 ASP B C 1 ATOM 5945 O O . ASP B 1 342 ? 26.907 -54.643 -11.719 1.00 66.10 ? 372 ASP B O 1 ATOM 5946 C CB . ASP B 1 342 ? 29.984 -54.722 -11.379 1.00 57.19 ? 372 ASP B CB 1 ATOM 5947 C CG . ASP B 1 342 ? 30.240 -55.734 -12.481 1.00 58.42 ? 372 ASP B CG 1 ATOM 5948 O OD1 . ASP B 1 342 ? 30.280 -55.325 -13.669 1.00 58.49 ? 372 ASP B OD1 1 ATOM 5949 O OD2 . ASP B 1 342 ? 30.411 -56.932 -12.176 1.00 57.21 ? 372 ASP B OD2 1 ATOM 5950 N N . MET B 1 343 ? 27.795 -54.306 -13.777 1.00 58.28 ? 373 MET B N 1 ATOM 5951 C CA . MET B 1 343 ? 26.674 -54.916 -14.484 1.00 60.22 ? 373 MET B CA 1 ATOM 5952 C C . MET B 1 343 ? 27.037 -56.197 -15.201 1.00 60.51 ? 373 MET B C 1 ATOM 5953 O O . MET B 1 343 ? 26.151 -56.913 -15.649 1.00 65.97 ? 373 MET B O 1 ATOM 5954 C CB . MET B 1 343 ? 26.074 -53.933 -15.483 1.00 62.36 ? 373 MET B CB 1 ATOM 5955 C CG . MET B 1 343 ? 25.501 -52.709 -14.815 1.00 62.12 ? 373 MET B CG 1 ATOM 5956 S SD . MET B 1 343 ? 24.585 -51.611 -15.899 1.00 63.23 ? 373 MET B SD 1 ATOM 5957 C CE . MET B 1 343 ? 25.748 -51.366 -17.232 1.00 65.06 ? 373 MET B CE 1 ATOM 5958 N N . ALA B 1 344 ? 28.325 -56.480 -15.325 1.00 57.13 ? 374 ALA B N 1 ATOM 5959 C CA . ALA B 1 344 ? 28.781 -57.783 -15.793 1.00 56.89 ? 374 ALA B CA 1 ATOM 5960 C C . ALA B 1 344 ? 28.350 -58.907 -14.846 1.00 58.55 ? 374 ALA B C 1 ATOM 5961 O O . ALA B 1 344 ? 27.796 -59.893 -15.289 1.00 58.06 ? 374 ALA B O 1 ATOM 5962 C CB . ALA B 1 344 ? 30.294 -57.788 -15.948 1.00 57.32 ? 374 ALA B CB 1 ATOM 5963 N N . CYS B 1 345 ? 28.615 -58.759 -13.547 1.00 64.83 ? 375 CYS B N 1 ATOM 5964 C CA . CYS B 1 345 ? 28.195 -59.754 -12.532 1.00 64.93 ? 375 CYS B CA 1 ATOM 5965 C C . CYS B 1 345 ? 27.611 -59.061 -11.316 1.00 62.31 ? 375 CYS B C 1 ATOM 5966 O O . CYS B 1 345 ? 28.224 -59.004 -10.257 1.00 65.20 ? 375 CYS B O 1 ATOM 5967 C CB . CYS B 1 345 ? 29.372 -60.632 -12.115 1.00 65.56 ? 375 CYS B CB 1 ATOM 5968 S SG . CYS B 1 345 ? 29.930 -61.712 -13.447 1.00 65.08 ? 375 CYS B SG 1 ATOM 5969 N N . ASN B 1 346 ? 26.405 -58.546 -11.458 1.00 63.19 ? 376 ASN B N 1 ATOM 5970 C CA . ASN B 1 346 ? 25.910 -57.584 -10.493 1.00 63.87 ? 376 ASN B CA 1 ATOM 5971 C C . ASN B 1 346 ? 25.789 -58.193 -9.096 1.00 61.58 ? 376 ASN B C 1 ATOM 5972 O O . ASN B 1 346 ? 25.614 -59.401 -8.962 1.00 66.14 ? 376 ASN B O 1 ATOM 5973 C CB . ASN B 1 346 ? 24.593 -56.983 -10.982 1.00 66.46 ? 376 ASN B CB 1 ATOM 5974 C CG . ASN B 1 346 ? 23.418 -57.902 -10.755 1.00 68.10 ? 376 ASN B CG 1 ATOM 5975 O OD1 . ASN B 1 346 ? 22.919 -58.003 -9.643 1.00 67.74 ? 376 ASN B OD1 1 ATOM 5976 N ND2 . ASN B 1 346 ? 22.968 -58.575 -11.811 1.00 71.77 ? 376 ASN B ND2 1 ATOM 5977 N N . PHE B 1 347 ? 25.898 -57.353 -8.071 1.00 59.85 ? 377 PHE B N 1 ATOM 5978 C CA . PHE B 1 347 ? 25.954 -57.812 -6.666 1.00 58.78 ? 377 PHE B CA 1 ATOM 5979 C C . PHE B 1 347 ? 24.730 -58.625 -6.239 1.00 62.00 ? 377 PHE B C 1 ATOM 5980 O O . PHE B 1 347 ? 24.843 -59.576 -5.462 1.00 59.13 ? 377 PHE B O 1 ATOM 5981 C CB . PHE B 1 347 ? 26.136 -56.625 -5.718 1.00 56.85 ? 377 PHE B CB 1 ATOM 5982 C CG . PHE B 1 347 ? 24.897 -55.805 -5.537 1.00 57.41 ? 377 PHE B CG 1 ATOM 5983 C CD1 . PHE B 1 347 ? 24.618 -54.754 -6.381 1.00 56.26 ? 377 PHE B CD1 1 ATOM 5984 C CD2 . PHE B 1 347 ? 23.993 -56.107 -4.524 1.00 59.55 ? 377 PHE B CD2 1 ATOM 5985 C CE1 . PHE B 1 347 ? 23.449 -54.029 -6.229 1.00 58.32 ? 377 PHE B CE1 1 ATOM 5986 C CE2 . PHE B 1 347 ? 22.837 -55.379 -4.362 1.00 57.92 ? 377 PHE B CE2 1 ATOM 5987 C CZ . PHE B 1 347 ? 22.563 -54.334 -5.212 1.00 58.03 ? 377 PHE B CZ 1 ATOM 5988 N N . MET B 1 348 ? 23.560 -58.255 -6.745 1.00 61.42 ? 378 MET B N 1 ATOM 5989 C CA . MET B 1 348 ? 22.344 -58.897 -6.297 1.00 64.34 ? 378 MET B CA 1 ATOM 5990 C C . MET B 1 348 ? 22.283 -60.339 -6.736 1.00 67.13 ? 378 MET B C 1 ATOM 5991 O O . MET B 1 348 ? 21.854 -61.194 -5.963 1.00 74.98 ? 378 MET B O 1 ATOM 5992 C CB . MET B 1 348 ? 21.098 -58.164 -6.775 1.00 69.03 ? 378 MET B CB 1 ATOM 5993 C CG . MET B 1 348 ? 19.821 -58.755 -6.208 1.00 72.60 ? 378 MET B CG 1 ATOM 5994 S SD . MET B 1 348 ? 18.447 -57.598 -6.293 1.00 81.20 ? 378 MET B SD 1 ATOM 5995 C CE . MET B 1 348 ? 18.861 -56.472 -4.968 1.00 77.47 ? 378 MET B CE 1 ATOM 5996 N N . GLY B 1 349 ? 22.687 -60.610 -7.973 1.00 66.59 ? 379 GLY B N 1 ATOM 5997 C CA . GLY B 1 349 ? 22.711 -61.970 -8.492 1.00 66.15 ? 379 GLY B CA 1 ATOM 5998 C C . GLY B 1 349 ? 23.444 -62.882 -7.538 1.00 66.48 ? 379 GLY B C 1 ATOM 5999 O O . GLY B 1 349 ? 22.940 -63.932 -7.169 1.00 65.06 ? 379 GLY B O 1 ATOM 6000 N N . ASP B 1 350 ? 24.624 -62.459 -7.101 1.00 67.37 ? 380 ASP B N 1 ATOM 6001 C CA . ASP B 1 350 ? 25.387 -63.243 -6.139 1.00 70.03 ? 380 ASP B CA 1 ATOM 6002 C C . ASP B 1 350 ? 24.781 -63.227 -4.729 1.00 71.26 ? 380 ASP B C 1 ATOM 6003 O O . ASP B 1 350 ? 24.879 -64.219 -4.010 1.00 76.87 ? 380 ASP B O 1 ATOM 6004 C CB . ASP B 1 350 ? 26.835 -62.772 -6.083 1.00 72.47 ? 380 ASP B CB 1 ATOM 6005 C CG . ASP B 1 350 ? 27.652 -63.274 -7.229 1.00 74.06 ? 380 ASP B CG 1 ATOM 6006 O OD1 . ASP B 1 350 ? 27.472 -64.441 -7.635 1.00 74.34 ? 380 ASP B OD1 1 ATOM 6007 O OD2 . ASP B 1 350 ? 28.484 -62.491 -7.727 1.00 77.88 ? 380 ASP B OD2 1 ATOM 6008 N N . GLU B 1 351 ? 24.167 -62.124 -4.318 1.00 66.45 ? 381 GLU B N 1 ATOM 6009 C CA . GLU B 1 351 ? 23.464 -62.131 -3.035 1.00 71.63 ? 381 GLU B CA 1 ATOM 6010 C C . GLU B 1 351 ? 22.331 -63.152 -3.044 1.00 72.70 ? 381 GLU B C 1 ATOM 6011 O O . GLU B 1 351 ? 22.141 -63.879 -2.067 1.00 77.34 ? 381 GLU B O 1 ATOM 6012 C CB . GLU B 1 351 ? 22.928 -60.752 -2.665 1.00 73.43 ? 381 GLU B CB 1 ATOM 6013 C CG . GLU B 1 351 ? 22.419 -60.675 -1.233 1.00 77.43 ? 381 GLU B CG 1 ATOM 6014 C CD . GLU B 1 351 ? 22.345 -59.263 -0.682 1.00 79.65 ? 381 GLU B CD 1 ATOM 6015 O OE1 . GLU B 1 351 ? 22.248 -58.294 -1.471 1.00 77.75 ? 381 GLU B OE1 1 ATOM 6016 O OE2 . GLU B 1 351 ? 22.371 -59.127 0.562 1.00 82.48 ? 381 GLU B OE2 1 ATOM 6017 N N . TRP B 1 352 ? 21.583 -63.202 -4.142 1.00 70.19 ? 382 TRP B N 1 ATOM 6018 C CA . TRP B 1 352 ? 20.547 -64.217 -4.313 1.00 71.31 ? 382 TRP B CA 1 ATOM 6019 C C . TRP B 1 352 ? 21.135 -65.602 -4.306 1.00 75.28 ? 382 TRP B C 1 ATOM 6020 O O . TRP B 1 352 ? 20.564 -66.527 -3.745 1.00 82.87 ? 382 TRP B O 1 ATOM 6021 C CB . TRP B 1 352 ? 19.827 -64.064 -5.647 1.00 68.09 ? 382 TRP B CB 1 ATOM 6022 C CG . TRP B 1 352 ? 18.877 -62.926 -5.751 1.00 68.50 ? 382 TRP B CG 1 ATOM 6023 C CD1 . TRP B 1 352 ? 18.490 -62.075 -4.758 1.00 67.88 ? 382 TRP B CD1 1 ATOM 6024 C CD2 . TRP B 1 352 ? 18.160 -62.529 -6.930 1.00 66.49 ? 382 TRP B CD2 1 ATOM 6025 N NE1 . TRP B 1 352 ? 17.591 -61.165 -5.249 1.00 69.08 ? 382 TRP B NE1 1 ATOM 6026 C CE2 . TRP B 1 352 ? 17.368 -61.424 -6.578 1.00 69.42 ? 382 TRP B CE2 1 ATOM 6027 C CE3 . TRP B 1 352 ? 18.125 -62.994 -8.246 1.00 63.53 ? 382 TRP B CE3 1 ATOM 6028 C CZ2 . TRP B 1 352 ? 16.543 -60.771 -7.505 1.00 69.39 ? 382 TRP B CZ2 1 ATOM 6029 C CZ3 . TRP B 1 352 ? 17.304 -62.355 -9.161 1.00 66.23 ? 382 TRP B CZ3 1 ATOM 6030 C CH2 . TRP B 1 352 ? 16.522 -61.255 -8.787 1.00 68.02 ? 382 TRP B CH2 1 ATOM 6031 N N . PHE B 1 353 ? 22.255 -65.757 -4.989 1.00 77.45 ? 383 PHE B N 1 ATOM 6032 C CA . PHE B 1 353 ? 22.885 -67.050 -5.090 1.00 75.94 ? 383 PHE B CA 1 ATOM 6033 C C . PHE B 1 353 ? 23.284 -67.558 -3.715 1.00 73.13 ? 383 PHE B C 1 ATOM 6034 O O . PHE B 1 353 ? 23.060 -68.717 -3.397 1.00 72.15 ? 383 PHE B O 1 ATOM 6035 C CB . PHE B 1 353 ? 24.108 -66.975 -5.995 1.00 75.47 ? 383 PHE B CB 1 ATOM 6036 C CG . PHE B 1 353 ? 24.911 -68.232 -6.006 1.00 76.40 ? 383 PHE B CG 1 ATOM 6037 C CD1 . PHE B 1 353 ? 24.549 -69.287 -6.822 1.00 75.10 ? 383 PHE B CD1 1 ATOM 6038 C CD2 . PHE B 1 353 ? 26.013 -68.365 -5.175 1.00 74.15 ? 383 PHE B CD2 1 ATOM 6039 C CE1 . PHE B 1 353 ? 25.273 -70.447 -6.825 1.00 75.53 ? 383 PHE B CE1 1 ATOM 6040 C CE2 . PHE B 1 353 ? 26.746 -69.524 -5.177 1.00 74.48 ? 383 PHE B CE2 1 ATOM 6041 C CZ . PHE B 1 353 ? 26.371 -70.566 -6.001 1.00 76.50 ? 383 PHE B CZ 1 ATOM 6042 N N . VAL B 1 354 ? 23.904 -66.694 -2.920 1.00 71.08 ? 384 VAL B N 1 ATOM 6043 C CA . VAL B 1 354 ? 24.354 -67.089 -1.592 1.00 72.74 ? 384 VAL B CA 1 ATOM 6044 C C . VAL B 1 354 ? 23.164 -67.391 -0.710 1.00 76.99 ? 384 VAL B C 1 ATOM 6045 O O . VAL B 1 354 ? 23.076 -68.471 -0.142 1.00 81.18 ? 384 VAL B O 1 ATOM 6046 C CB . VAL B 1 354 ? 25.228 -66.016 -0.931 1.00 71.68 ? 384 VAL B CB 1 ATOM 6047 C CG1 . VAL B 1 354 ? 25.502 -66.373 0.525 1.00 71.80 ? 384 VAL B CG1 1 ATOM 6048 C CG2 . VAL B 1 354 ? 26.538 -65.846 -1.699 1.00 69.87 ? 384 VAL B CG2 1 ATOM 6049 N N . ASP B 1 355 ? 22.230 -66.450 -0.630 1.00 81.52 ? 385 ASP B N 1 ATOM 6050 C CA . ASP B 1 355 ? 20.998 -66.637 0.163 1.00 81.78 ? 385 ASP B CA 1 ATOM 6051 C C . ASP B 1 355 ? 20.308 -67.964 -0.161 1.00 81.69 ? 385 ASP B C 1 ATOM 6052 O O . ASP B 1 355 ? 19.828 -68.653 0.744 1.00 91.26 ? 385 ASP B O 1 ATOM 6053 C CB . ASP B 1 355 ? 20.022 -65.470 -0.035 1.00 81.74 ? 385 ASP B CB 1 ATOM 6054 C CG . ASP B 1 355 ? 20.487 -64.173 0.651 1.00 83.89 ? 385 ASP B CG 1 ATOM 6055 O OD1 . ASP B 1 355 ? 21.499 -64.185 1.394 1.00 79.72 ? 385 ASP B OD1 1 ATOM 6056 O OD2 . ASP B 1 355 ? 19.811 -63.137 0.453 1.00 83.45 ? 385 ASP B OD2 1 ATOM 6057 N N . SER B 1 356 ? 20.297 -68.339 -1.435 1.00 76.53 ? 386 SER B N 1 ATOM 6058 C CA . SER B 1 356 ? 19.654 -69.577 -1.851 1.00 79.22 ? 386 SER B CA 1 ATOM 6059 C C . SER B 1 356 ? 20.497 -70.832 -1.600 1.00 77.83 ? 386 SER B C 1 ATOM 6060 O O . SER B 1 356 ? 20.050 -71.930 -1.893 1.00 77.46 ? 386 SER B O 1 ATOM 6061 C CB . SER B 1 356 ? 19.201 -69.496 -3.327 1.00 77.98 ? 386 SER B CB 1 ATOM 6062 O OG . SER B 1 356 ? 20.297 -69.524 -4.217 1.00 80.29 ? 386 SER B OG 1 ATOM 6063 N N . LEU B 1 357 ? 21.694 -70.689 -1.050 1.00 76.91 ? 387 LEU B N 1 ATOM 6064 C CA . LEU B 1 357 ? 22.417 -71.856 -0.547 1.00 80.90 ? 387 LEU B CA 1 ATOM 6065 C C . LEU B 1 357 ? 21.826 -72.449 0.741 1.00 88.75 ? 387 LEU B C 1 ATOM 6066 O O . LEU B 1 357 ? 22.182 -73.571 1.103 1.00 93.75 ? 387 LEU B O 1 ATOM 6067 C CB . LEU B 1 357 ? 23.886 -71.535 -0.301 1.00 80.56 ? 387 LEU B CB 1 ATOM 6068 C CG . LEU B 1 357 ? 24.753 -71.361 -1.546 1.00 82.79 ? 387 LEU B CG 1 ATOM 6069 C CD1 . LEU B 1 357 ? 26.171 -71.004 -1.143 1.00 83.55 ? 387 LEU B CD1 1 ATOM 6070 C CD2 . LEU B 1 357 ? 24.758 -72.619 -2.385 1.00 82.47 ? 387 LEU B CD2 1 ATOM 6071 N N . ASN B 1 358 ? 20.963 -71.705 1.441 1.00 90.14 ? 388 ASN B N 1 ATOM 6072 C CA . ASN B 1 358 ? 20.398 -72.135 2.728 1.00 95.18 ? 388 ASN B CA 1 ATOM 6073 C C . ASN B 1 358 ? 21.450 -72.658 3.710 1.00 96.39 ? 388 ASN B C 1 ATOM 6074 O O . ASN B 1 358 ? 21.555 -73.854 3.934 1.00 99.72 ? 388 ASN B O 1 ATOM 6075 C CB . ASN B 1 358 ? 19.340 -73.225 2.540 1.00 101.92 ? 388 ASN B CB 1 ATOM 6076 C CG . ASN B 1 358 ? 18.092 -72.737 1.845 1.00 103.87 ? 388 ASN B CG 1 ATOM 6077 O OD1 . ASN B 1 358 ? 17.865 -71.542 1.701 1.00 106.19 ? 388 ASN B OD1 1 ATOM 6078 N ND2 . ASN B 1 358 ? 17.265 -73.681 1.411 1.00 107.82 ? 388 ASN B ND2 1 ATOM 6079 N N . GLN B 1 359 ? 22.221 -71.756 4.288 1.00 94.49 ? 389 GLN B N 1 ATOM 6080 C CA . GLN B 1 359 ? 23.168 -72.094 5.321 1.00 95.85 ? 389 GLN B CA 1 ATOM 6081 C C . GLN B 1 359 ? 22.671 -71.475 6.610 1.00 104.12 ? 389 GLN B C 1 ATOM 6082 O O . GLN B 1 359 ? 21.742 -70.673 6.590 1.00 105.45 ? 389 GLN B O 1 ATOM 6083 C CB . GLN B 1 359 ? 24.533 -71.542 4.955 1.00 92.94 ? 389 GLN B CB 1 ATOM 6084 C CG . GLN B 1 359 ? 25.080 -72.115 3.662 1.00 90.24 ? 389 GLN B CG 1 ATOM 6085 C CD . GLN B 1 359 ? 25.245 -73.629 3.727 1.00 89.48 ? 389 GLN B CD 1 ATOM 6086 O OE1 . GLN B 1 359 ? 26.014 -74.136 4.539 1.00 91.18 ? 389 GLN B OE1 1 ATOM 6087 N NE2 . GLN B 1 359 ? 24.538 -74.350 2.865 1.00 85.68 ? 389 GLN B NE2 1 ATOM 6088 N N . LYS B 1 360 ? 23.275 -71.855 7.729 1.00 117.19 ? 390 LYS B N 1 ATOM 6089 C CA . LYS B 1 360 ? 22.900 -71.302 9.032 1.00 127.00 ? 390 LYS B CA 1 ATOM 6090 C C . LYS B 1 360 ? 23.358 -69.859 9.156 1.00 126.87 ? 390 LYS B C 1 ATOM 6091 O O . LYS B 1 360 ? 24.555 -69.587 9.182 1.00 132.90 ? 390 LYS B O 1 ATOM 6092 C CB . LYS B 1 360 ? 23.494 -72.129 10.173 1.00 132.81 ? 390 LYS B CB 1 ATOM 6093 C CG . LYS B 1 360 ? 22.941 -71.763 11.545 1.00 138.58 ? 390 LYS B CG 1 ATOM 6094 C CD . LYS B 1 360 ? 23.204 -72.864 12.568 1.00 145.86 ? 390 LYS B CD 1 ATOM 6095 C CE . LYS B 1 360 ? 22.291 -72.763 13.782 1.00 148.77 ? 390 LYS B CE 1 ATOM 6096 N NZ . LYS B 1 360 ? 22.349 -73.990 14.621 1.00 150.29 ? 390 LYS B NZ 1 ATOM 6097 N N . MET B 1 361 ? 22.404 -68.938 9.208 1.00 127.04 ? 391 MET B N 1 ATOM 6098 C CA . MET B 1 361 ? 22.720 -67.529 9.381 1.00 129.71 ? 391 MET B CA 1 ATOM 6099 C C . MET B 1 361 ? 23.474 -67.338 10.674 1.00 128.63 ? 391 MET B C 1 ATOM 6100 O O . MET B 1 361 ? 23.090 -67.883 11.697 1.00 141.42 ? 391 MET B O 1 ATOM 6101 C CB . MET B 1 361 ? 21.455 -66.681 9.396 1.00 136.93 ? 391 MET B CB 1 ATOM 6102 C CG . MET B 1 361 ? 21.659 -65.265 9.909 1.00 147.17 ? 391 MET B CG 1 ATOM 6103 S SD . MET B 1 361 ? 20.436 -64.110 9.284 1.00 165.45 ? 391 MET B SD 1 ATOM 6104 C CE . MET B 1 361 ? 21.185 -63.637 7.717 1.00 159.97 ? 391 MET B CE 1 ATOM 6105 N N . GLU B 1 362 ? 24.551 -66.573 10.618 1.00 125.51 ? 392 GLU B N 1 ATOM 6106 C CA . GLU B 1 362 ? 25.282 -66.190 11.815 1.00 126.63 ? 392 GLU B CA 1 ATOM 6107 C C . GLU B 1 362 ? 25.063 -64.707 12.105 1.00 119.94 ? 392 GLU B C 1 ATOM 6108 O O . GLU B 1 362 ? 24.189 -64.365 12.895 1.00 117.76 ? 392 GLU B O 1 ATOM 6109 C CB . GLU B 1 362 ? 26.756 -66.532 11.662 1.00 128.04 ? 392 GLU B CB 1 ATOM 6110 C CG . GLU B 1 362 ? 27.029 -68.022 11.741 1.00 133.00 ? 392 GLU B CG 1 ATOM 6111 C CD . GLU B 1 362 ? 28.474 -68.337 12.055 1.00 137.73 ? 392 GLU B CD 1 ATOM 6112 O OE1 . GLU B 1 362 ? 29.304 -67.406 12.034 1.00 136.21 ? 392 GLU B OE1 1 ATOM 6113 O OE2 . GLU B 1 362 ? 28.779 -69.519 12.327 1.00 140.71 ? 392 GLU B OE2 1 ATOM 6114 N N . VAL B 1 363 ? 25.829 -63.834 11.456 1.00 112.42 ? 393 VAL B N 1 ATOM 6115 C CA . VAL B 1 363 ? 25.650 -62.396 11.623 1.00 108.73 ? 393 VAL B CA 1 ATOM 6116 C C . VAL B 1 363 ? 24.601 -61.898 10.636 1.00 108.09 ? 393 VAL B C 1 ATOM 6117 O O . VAL B 1 363 ? 24.664 -62.192 9.432 1.00 110.92 ? 393 VAL B O 1 ATOM 6118 C CB . VAL B 1 363 ? 26.957 -61.608 11.405 1.00 107.20 ? 393 VAL B CB 1 ATOM 6119 C CG1 . VAL B 1 363 ? 26.738 -60.124 11.667 1.00 104.94 ? 393 VAL B CG1 1 ATOM 6120 C CG2 . VAL B 1 363 ? 28.073 -62.151 12.284 1.00 108.19 ? 393 VAL B CG2 1 ATOM 6121 N N . GLN B 1 364 ? 23.639 -61.141 11.154 1.00 105.16 ? 394 GLN B N 1 ATOM 6122 C CA . GLN B 1 364 ? 22.599 -60.521 10.334 1.00 101.91 ? 394 GLN B CA 1 ATOM 6123 C C . GLN B 1 364 ? 23.233 -59.463 9.413 1.00 95.48 ? 394 GLN B C 1 ATOM 6124 O O . GLN B 1 364 ? 24.361 -59.027 9.644 1.00 92.78 ? 394 GLN B O 1 ATOM 6125 C CB . GLN B 1 364 ? 21.531 -59.886 11.227 1.00 104.74 ? 394 GLN B CB 1 ATOM 6126 C CG . GLN B 1 364 ? 20.778 -60.858 12.133 1.00 110.55 ? 394 GLN B CG 1 ATOM 6127 C CD . GLN B 1 364 ? 21.439 -61.089 13.505 1.00 114.13 ? 394 GLN B CD 1 ATOM 6128 O OE1 . GLN B 1 364 ? 22.528 -61.658 13.600 1.00 117.46 ? 394 GLN B OE1 1 ATOM 6129 N NE2 . GLN B 1 364 ? 20.761 -60.674 14.570 1.00 111.70 ? 394 GLN B NE2 1 ATOM 6130 N N . ARG B 1 365 ? 22.525 -59.068 8.362 1.00 88.28 ? 395 ARG B N 1 ATOM 6131 C CA . ARG B 1 365 ? 23.095 -58.150 7.362 1.00 85.38 ? 395 ARG B CA 1 ATOM 6132 C C . ARG B 1 365 ? 23.326 -56.755 7.933 1.00 82.72 ? 395 ARG B C 1 ATOM 6133 O O . ARG B 1 365 ? 22.404 -56.143 8.456 1.00 77.53 ? 395 ARG B O 1 ATOM 6134 C CB . ARG B 1 365 ? 22.181 -58.049 6.139 1.00 83.41 ? 395 ARG B CB 1 ATOM 6135 C CG . ARG B 1 365 ? 22.820 -57.442 4.909 1.00 80.38 ? 395 ARG B CG 1 ATOM 6136 C CD . ARG B 1 365 ? 21.797 -57.281 3.807 1.00 78.04 ? 395 ARG B CD 1 ATOM 6137 N NE . ARG B 1 365 ? 22.406 -57.141 2.484 1.00 75.29 ? 395 ARG B NE 1 ATOM 6138 C CZ . ARG B 1 365 ? 22.739 -55.995 1.900 1.00 77.15 ? 395 ARG B CZ 1 ATOM 6139 N NH1 . ARG B 1 365 ? 22.557 -54.823 2.509 1.00 77.30 ? 395 ARG B NH1 1 ATOM 6140 N NH2 . ARG B 1 365 ? 23.267 -56.020 0.679 1.00 78.31 ? 395 ARG B NH2 1 ATOM 6141 N N . ARG B 1 366 ? 24.551 -56.251 7.813 1.00 82.27 ? 396 ARG B N 1 ATOM 6142 C CA . ARG B 1 366 ? 24.890 -54.926 8.339 1.00 84.87 ? 396 ARG B CA 1 ATOM 6143 C C . ARG B 1 366 ? 25.931 -54.218 7.469 1.00 78.47 ? 396 ARG B C 1 ATOM 6144 O O . ARG B 1 366 ? 26.477 -54.814 6.544 1.00 74.64 ? 396 ARG B O 1 ATOM 6145 C CB . ARG B 1 366 ? 25.407 -55.040 9.789 1.00 90.80 ? 396 ARG B CB 1 ATOM 6146 C CG . ARG B 1 366 ? 26.523 -56.050 9.951 1.00 96.13 ? 396 ARG B CG 1 ATOM 6147 C CD . ARG B 1 366 ? 27.493 -55.734 11.085 1.00 102.49 ? 396 ARG B CD 1 ATOM 6148 N NE . ARG B 1 366 ? 28.629 -56.661 11.024 1.00 110.18 ? 396 ARG B NE 1 ATOM 6149 C CZ . ARG B 1 366 ? 29.816 -56.417 10.460 1.00 110.82 ? 396 ARG B CZ 1 ATOM 6150 N NH1 . ARG B 1 366 ? 30.103 -55.240 9.919 1.00 110.58 ? 396 ARG B NH1 1 ATOM 6151 N NH2 . ARG B 1 366 ? 30.747 -57.363 10.453 1.00 115.01 ? 396 ARG B NH2 1 ATOM 6152 N N . PRO B 1 367 ? 26.187 -52.930 7.754 1.00 76.54 ? 397 PRO B N 1 ATOM 6153 C CA . PRO B 1 367 ? 27.335 -52.180 7.235 1.00 72.13 ? 397 PRO B CA 1 ATOM 6154 C C . PRO B 1 367 ? 28.672 -52.776 7.618 1.00 73.22 ? 397 PRO B C 1 ATOM 6155 O O . PRO B 1 367 ? 28.737 -53.583 8.523 1.00 73.54 ? 397 PRO B O 1 ATOM 6156 C CB . PRO B 1 367 ? 27.207 -50.838 7.934 1.00 70.43 ? 397 PRO B CB 1 ATOM 6157 C CG . PRO B 1 367 ? 25.746 -50.666 8.164 1.00 72.40 ? 397 PRO B CG 1 ATOM 6158 C CD . PRO B 1 367 ? 25.164 -52.037 8.331 1.00 75.40 ? 397 PRO B CD 1 ATOM 6159 N N . TRP B 1 368 ? 29.724 -52.397 6.905 1.00 74.57 ? 398 TRP B N 1 ATOM 6160 C CA . TRP B 1 368 ? 31.091 -52.610 7.371 1.00 75.31 ? 398 TRP B CA 1 ATOM 6161 C C . TRP B 1 368 ? 31.953 -51.417 6.976 1.00 75.81 ? 398 TRP B C 1 ATOM 6162 O O . TRP B 1 368 ? 31.769 -50.833 5.908 1.00 74.11 ? 398 TRP B O 1 ATOM 6163 C CB . TRP B 1 368 ? 31.675 -53.932 6.865 1.00 75.42 ? 398 TRP B CB 1 ATOM 6164 C CG . TRP B 1 368 ? 31.898 -54.037 5.385 1.00 76.32 ? 398 TRP B CG 1 ATOM 6165 C CD1 . TRP B 1 368 ? 30.978 -54.379 4.435 1.00 77.08 ? 398 TRP B CD1 1 ATOM 6166 C CD2 . TRP B 1 368 ? 33.135 -53.858 4.691 1.00 74.43 ? 398 TRP B CD2 1 ATOM 6167 N NE1 . TRP B 1 368 ? 31.564 -54.402 3.191 1.00 75.05 ? 398 TRP B NE1 1 ATOM 6168 C CE2 . TRP B 1 368 ? 32.887 -54.090 3.321 1.00 71.18 ? 398 TRP B CE2 1 ATOM 6169 C CE3 . TRP B 1 368 ? 34.426 -53.501 5.092 1.00 76.39 ? 398 TRP B CE3 1 ATOM 6170 C CZ2 . TRP B 1 368 ? 33.879 -53.976 2.350 1.00 68.67 ? 398 TRP B CZ2 1 ATOM 6171 C CZ3 . TRP B 1 368 ? 35.423 -53.396 4.116 1.00 74.38 ? 398 TRP B CZ3 1 ATOM 6172 C CH2 . TRP B 1 368 ? 35.139 -53.631 2.764 1.00 68.98 ? 398 TRP B CH2 1 ATOM 6173 N N . LEU B 1 369 ? 32.882 -51.054 7.852 1.00 78.08 ? 399 LEU B N 1 ATOM 6174 C CA . LEU B 1 369 ? 33.549 -49.768 7.766 1.00 76.70 ? 399 LEU B CA 1 ATOM 6175 C C . LEU B 1 369 ? 35.021 -49.847 7.363 1.00 76.51 ? 399 LEU B C 1 ATOM 6176 O O . LEU B 1 369 ? 35.653 -50.901 7.408 1.00 75.32 ? 399 LEU B O 1 ATOM 6177 C CB . LEU B 1 369 ? 33.419 -49.032 9.099 1.00 78.53 ? 399 LEU B CB 1 ATOM 6178 C CG . LEU B 1 369 ? 32.023 -48.973 9.718 1.00 79.32 ? 399 LEU B CG 1 ATOM 6179 C CD1 . LEU B 1 369 ? 32.055 -48.260 11.067 1.00 82.95 ? 399 LEU B CD1 1 ATOM 6180 C CD2 . LEU B 1 369 ? 31.055 -48.283 8.777 1.00 78.80 ? 399 LEU B CD2 1 ATOM 6181 N N . VAL B 1 370 ? 35.537 -48.709 6.920 1.00 75.95 ? 400 VAL B N 1 ATOM 6182 C CA . VAL B 1 370 ? 36.936 -48.557 6.583 1.00 76.20 ? 400 VAL B CA 1 ATOM 6183 C C . VAL B 1 370 ? 37.346 -47.180 7.062 1.00 78.24 ? 400 VAL B C 1 ATOM 6184 O O . VAL B 1 370 ? 36.578 -46.229 6.968 1.00 81.05 ? 400 VAL B O 1 ATOM 6185 C CB . VAL B 1 370 ? 37.183 -48.714 5.058 1.00 76.28 ? 400 VAL B CB 1 ATOM 6186 C CG1 . VAL B 1 370 ? 38.604 -48.299 4.675 1.00 78.13 ? 400 VAL B CG1 1 ATOM 6187 C CG2 . VAL B 1 370 ? 36.942 -50.150 4.627 1.00 74.67 ? 400 VAL B CG2 1 ATOM 6188 N N . LYS B 1 371 ? 38.552 -47.080 7.588 1.00 81.39 ? 401 LYS B N 1 ATOM 6189 C CA . LYS B 1 371 ? 39.073 -45.806 8.050 1.00 88.40 ? 401 LYS B CA 1 ATOM 6190 C C . LYS B 1 371 ? 39.852 -45.161 6.905 1.00 85.90 ? 401 LYS B C 1 ATOM 6191 O O . LYS B 1 371 ? 40.718 -45.789 6.304 1.00 83.27 ? 401 LYS B O 1 ATOM 6192 C CB . LYS B 1 371 ? 39.968 -46.031 9.267 1.00 95.33 ? 401 LYS B CB 1 ATOM 6193 C CG . LYS B 1 371 ? 40.257 -44.790 10.083 1.00 100.83 ? 401 LYS B CG 1 ATOM 6194 C CD . LYS B 1 371 ? 40.904 -45.156 11.418 1.00 107.37 ? 401 LYS B CD 1 ATOM 6195 C CE . LYS B 1 371 ? 41.015 -43.955 12.352 1.00 111.71 ? 401 LYS B CE 1 ATOM 6196 N NZ . LYS B 1 371 ? 41.104 -44.360 13.782 1.00 110.94 ? 401 LYS B NZ 1 ATOM 6197 N N . TYR B 1 372 ? 39.532 -43.916 6.599 1.00 88.16 ? 402 TYR B N 1 ATOM 6198 C CA . TYR B 1 372 ? 40.252 -43.159 5.584 1.00 89.24 ? 402 TYR B CA 1 ATOM 6199 C C . TYR B 1 372 ? 41.015 -42.002 6.217 1.00 99.39 ? 402 TYR B C 1 ATOM 6200 O O . TYR B 1 372 ? 40.679 -41.553 7.316 1.00 104.31 ? 402 TYR B O 1 ATOM 6201 C CB . TYR B 1 372 ? 39.279 -42.641 4.534 1.00 84.83 ? 402 TYR B CB 1 ATOM 6202 C CG . TYR B 1 372 ? 38.676 -43.741 3.718 1.00 83.00 ? 402 TYR B CG 1 ATOM 6203 C CD1 . TYR B 1 372 ? 37.493 -44.358 4.107 1.00 79.44 ? 402 TYR B CD1 1 ATOM 6204 C CD2 . TYR B 1 372 ? 39.309 -44.201 2.561 1.00 83.38 ? 402 TYR B CD2 1 ATOM 6205 C CE1 . TYR B 1 372 ? 36.951 -45.393 3.359 1.00 77.53 ? 402 TYR B CE1 1 ATOM 6206 C CE2 . TYR B 1 372 ? 38.768 -45.231 1.804 1.00 78.77 ? 402 TYR B CE2 1 ATOM 6207 C CZ . TYR B 1 372 ? 37.594 -45.824 2.209 1.00 74.64 ? 402 TYR B CZ 1 ATOM 6208 O OH . TYR B 1 372 ? 37.085 -46.854 1.473 1.00 72.43 ? 402 TYR B OH 1 ATOM 6209 N N . GLY B 1 373 ? 42.044 -41.532 5.517 1.00 110.01 ? 403 GLY B N 1 ATOM 6210 C CA . GLY B 1 373 ? 42.812 -40.368 5.943 1.00 117.08 ? 403 GLY B CA 1 ATOM 6211 C C . GLY B 1 373 ? 41.956 -39.116 5.920 1.00 130.58 ? 403 GLY B C 1 ATOM 6212 O O . GLY B 1 373 ? 41.484 -38.691 4.857 1.00 130.05 ? 403 GLY B O 1 ATOM 6213 N N . ASP B 1 374 ? 41.739 -38.542 7.105 1.00 144.72 ? 404 ASP B N 1 ATOM 6214 C CA . ASP B 1 374 ? 40.916 -37.337 7.304 1.00 153.92 ? 404 ASP B CA 1 ATOM 6215 C C . ASP B 1 374 ? 39.404 -37.620 7.295 1.00 148.63 ? 404 ASP B C 1 ATOM 6216 O O . ASP B 1 374 ? 38.688 -37.147 8.188 1.00 144.47 ? 404 ASP B O 1 ATOM 6217 C CB . ASP B 1 374 ? 41.265 -36.230 6.291 1.00 158.72 ? 404 ASP B CB 1 ATOM 6218 C CG . ASP B 1 374 ? 40.848 -34.844 6.774 1.00 158.74 ? 404 ASP B CG 1 ATOM 6219 O OD1 . ASP B 1 374 ? 39.860 -34.294 6.236 1.00 149.70 ? 404 ASP B OD1 1 ATOM 6220 O OD2 . ASP B 1 374 ? 41.506 -34.313 7.697 1.00 154.65 ? 404 ASP B OD2 1 ATOM 6221 N N . SER B 1 375 ? 38.929 -38.385 6.304 1.00 136.05 ? 405 SER B N 1 ATOM 6222 C CA . SER B 1 375 ? 37.500 -38.713 6.177 1.00 128.25 ? 405 SER B CA 1 ATOM 6223 C C . SER B 1 375 ? 36.928 -39.472 7.368 1.00 124.70 ? 405 SER B C 1 ATOM 6224 O O . SER B 1 375 ? 35.710 -39.505 7.547 1.00 125.03 ? 405 SER B O 1 ATOM 6225 C CB . SER B 1 375 ? 37.231 -39.518 4.900 1.00 122.60 ? 405 SER B CB 1 ATOM 6226 O OG . SER B 1 375 ? 37.325 -38.703 3.756 1.00 125.47 ? 405 SER B OG 1 ATOM 6227 N N . GLY B 1 376 ? 37.787 -40.093 8.170 1.00 117.54 ? 406 GLY B N 1 ATOM 6228 C CA . GLY B 1 376 ? 37.325 -40.899 9.280 1.00 115.13 ? 406 GLY B CA 1 ATOM 6229 C C . GLY B 1 376 ? 36.744 -42.198 8.758 1.00 109.51 ? 406 GLY B C 1 ATOM 6230 O O . GLY B 1 376 ? 37.068 -42.645 7.649 1.00 101.28 ? 406 GLY B O 1 ATOM 6231 N N . GLU B 1 377 ? 35.881 -42.812 9.556 1.00 104.85 ? 407 GLU B N 1 ATOM 6232 C CA . GLU B 1 377 ? 35.291 -44.074 9.158 1.00 104.63 ? 407 GLU B CA 1 ATOM 6233 C C . GLU B 1 377 ? 34.176 -43.860 8.138 1.00 96.26 ? 407 GLU B C 1 ATOM 6234 O O . GLU B 1 377 ? 33.383 -42.923 8.244 1.00 93.57 ? 407 GLU B O 1 ATOM 6235 C CB . GLU B 1 377 ? 34.796 -44.853 10.379 1.00 111.01 ? 407 GLU B CB 1 ATOM 6236 C CG . GLU B 1 377 ? 35.932 -45.464 11.190 1.00 118.65 ? 407 GLU B CG 1 ATOM 6237 C CD . GLU B 1 377 ? 35.555 -46.752 11.906 1.00 122.59 ? 407 GLU B CD 1 ATOM 6238 O OE1 . GLU B 1 377 ? 34.601 -46.748 12.710 1.00 127.59 ? 407 GLU B OE1 1 ATOM 6239 O OE2 . GLU B 1 377 ? 36.227 -47.776 11.667 1.00 123.84 ? 407 GLU B OE2 1 ATOM 6240 N N . GLN B 1 378 ? 34.142 -44.731 7.138 1.00 86.14 ? 408 GLN B N 1 ATOM 6241 C CA . GLN B 1 378 ? 33.086 -44.715 6.141 1.00 78.38 ? 408 GLN B CA 1 ATOM 6242 C C . GLN B 1 378 ? 32.534 -46.101 5.947 1.00 76.78 ? 408 GLN B C 1 ATOM 6243 O O . GLN B 1 378 ? 33.132 -47.098 6.347 1.00 77.66 ? 408 GLN B O 1 ATOM 6244 C CB . GLN B 1 378 ? 33.616 -44.216 4.806 1.00 74.37 ? 408 GLN B CB 1 ATOM 6245 C CG . GLN B 1 378 ? 34.058 -42.768 4.809 1.00 72.93 ? 408 GLN B CG 1 ATOM 6246 C CD . GLN B 1 378 ? 32.915 -41.797 5.001 1.00 72.96 ? 408 GLN B CD 1 ATOM 6247 O OE1 . GLN B 1 378 ? 31.745 -42.100 4.715 1.00 71.07 ? 408 GLN B OE1 1 ATOM 6248 N NE2 . GLN B 1 378 ? 33.247 -40.613 5.487 1.00 72.54 ? 408 GLN B NE2 1 ATOM 6249 N N . ILE B 1 379 ? 31.374 -46.149 5.331 1.00 74.79 ? 409 ILE B N 1 ATOM 6250 C CA . ILE B 1 379 ? 30.757 -47.405 4.982 1.00 72.67 ? 409 ILE B CA 1 ATOM 6251 C C . ILE B 1 379 ? 31.347 -47.860 3.663 1.00 71.74 ? 409 ILE B C 1 ATOM 6252 O O . ILE B 1 379 ? 31.210 -47.191 2.646 1.00 70.40 ? 409 ILE B O 1 ATOM 6253 C CB . ILE B 1 379 ? 29.242 -47.245 4.899 1.00 71.42 ? 409 ILE B CB 1 ATOM 6254 C CG1 . ILE B 1 379 ? 28.691 -47.080 6.316 1.00 72.28 ? 409 ILE B CG1 1 ATOM 6255 C CG2 . ILE B 1 379 ? 28.609 -48.436 4.212 1.00 71.04 ? 409 ILE B CG2 1 ATOM 6256 C CD1 . ILE B 1 379 ? 27.271 -46.583 6.351 1.00 73.53 ? 409 ILE B CD1 1 ATOM 6257 N N . ALA B 1 380 ? 32.037 -48.985 3.692 1.00 75.00 ? 410 ALA B N 1 ATOM 6258 C CA . ALA B 1 380 ? 32.656 -49.528 2.486 1.00 74.75 ? 410 ALA B CA 1 ATOM 6259 C C . ALA B 1 380 ? 31.694 -50.428 1.725 1.00 70.86 ? 410 ALA B C 1 ATOM 6260 O O . ALA B 1 380 ? 31.830 -50.607 0.518 1.00 71.27 ? 410 ALA B O 1 ATOM 6261 C CB . ALA B 1 380 ? 33.935 -50.279 2.830 1.00 76.15 ? 410 ALA B CB 1 ATOM 6262 N N . GLY B 1 381 ? 30.731 -50.989 2.441 1.00 69.97 ? 411 GLY B N 1 ATOM 6263 C CA . GLY B 1 381 ? 29.678 -51.799 1.842 1.00 66.67 ? 411 GLY B CA 1 ATOM 6264 C C . GLY B 1 381 ? 28.865 -52.510 2.915 1.00 65.16 ? 411 GLY B C 1 ATOM 6265 O O . GLY B 1 381 ? 28.883 -52.123 4.086 1.00 61.49 ? 411 GLY B O 1 ATOM 6266 N N . PHE B 1 382 ? 28.164 -53.561 2.513 1.00 65.27 ? 412 PHE B N 1 ATOM 6267 C CA . PHE B 1 382 ? 27.351 -54.343 3.430 1.00 67.11 ? 412 PHE B CA 1 ATOM 6268 C C . PHE B 1 382 ? 27.774 -55.786 3.432 1.00 67.14 ? 412 PHE B C 1 ATOM 6269 O O . PHE B 1 382 ? 28.278 -56.266 2.431 1.00 70.79 ? 412 PHE B O 1 ATOM 6270 C CB . PHE B 1 382 ? 25.888 -54.211 3.045 1.00 68.22 ? 412 PHE B CB 1 ATOM 6271 C CG . PHE B 1 382 ? 25.335 -52.854 3.332 1.00 65.24 ? 412 PHE B CG 1 ATOM 6272 C CD1 . PHE B 1 382 ? 25.513 -51.817 2.423 1.00 60.72 ? 412 PHE B CD1 1 ATOM 6273 C CD2 . PHE B 1 382 ? 24.677 -52.607 4.522 1.00 63.90 ? 412 PHE B CD2 1 ATOM 6274 C CE1 . PHE B 1 382 ? 25.018 -50.561 2.695 1.00 60.53 ? 412 PHE B CE1 1 ATOM 6275 C CE2 . PHE B 1 382 ? 24.188 -51.350 4.807 1.00 63.27 ? 412 PHE B CE2 1 ATOM 6276 C CZ . PHE B 1 382 ? 24.361 -50.323 3.897 1.00 62.18 ? 412 PHE B CZ 1 ATOM 6277 N N . VAL B 1 383 ? 27.584 -56.460 4.567 1.00 69.84 ? 413 VAL B N 1 ATOM 6278 C CA . VAL B 1 383 ? 27.989 -57.860 4.733 1.00 70.43 ? 413 VAL B CA 1 ATOM 6279 C C . VAL B 1 383 ? 26.933 -58.706 5.464 1.00 71.97 ? 413 VAL B C 1 ATOM 6280 O O . VAL B 1 383 ? 26.333 -58.263 6.447 1.00 72.58 ? 413 VAL B O 1 ATOM 6281 C CB . VAL B 1 383 ? 29.335 -57.969 5.470 1.00 69.56 ? 413 VAL B CB 1 ATOM 6282 C CG1 . VAL B 1 383 ? 29.210 -57.480 6.907 1.00 73.59 ? 413 VAL B CG1 1 ATOM 6283 C CG2 . VAL B 1 383 ? 29.857 -59.396 5.426 1.00 69.77 ? 413 VAL B CG2 1 ATOM 6284 N N . LYS B 1 384 ? 26.732 -59.920 4.965 1.00 72.61 ? 414 LYS B N 1 ATOM 6285 C CA . LYS B 1 384 ? 25.741 -60.852 5.464 1.00 79.47 ? 414 LYS B CA 1 ATOM 6286 C C . LYS B 1 384 ? 26.483 -62.152 5.673 1.00 84.38 ? 414 LYS B C 1 ATOM 6287 O O . LYS B 1 384 ? 26.905 -62.756 4.694 1.00 87.02 ? 414 LYS B O 1 ATOM 6288 C CB . LYS B 1 384 ? 24.646 -61.035 4.410 1.00 81.71 ? 414 LYS B CB 1 ATOM 6289 C CG . LYS B 1 384 ? 23.387 -61.768 4.855 1.00 87.71 ? 414 LYS B CG 1 ATOM 6290 C CD . LYS B 1 384 ? 22.426 -61.955 3.680 1.00 91.54 ? 414 LYS B CD 1 ATOM 6291 C CE . LYS B 1 384 ? 21.009 -62.330 4.127 1.00 98.21 ? 414 LYS B CE 1 ATOM 6292 N NZ . LYS B 1 384 ? 20.070 -61.169 4.274 1.00 99.65 ? 414 LYS B NZ 1 ATOM 6293 N N . GLU B 1 385 ? 26.675 -62.576 6.924 1.00 87.42 ? 415 GLU B N 1 ATOM 6294 C CA . GLU B 1 385 ? 27.442 -63.795 7.193 1.00 92.85 ? 415 GLU B CA 1 ATOM 6295 C C . GLU B 1 385 ? 26.569 -65.028 7.467 1.00 93.67 ? 415 GLU B C 1 ATOM 6296 O O . GLU B 1 385 ? 25.535 -64.934 8.116 1.00 102.50 ? 415 GLU B O 1 ATOM 6297 C CB . GLU B 1 385 ? 28.422 -63.583 8.353 1.00 101.03 ? 415 GLU B CB 1 ATOM 6298 C CG . GLU B 1 385 ? 29.538 -62.592 8.050 1.00 103.88 ? 415 GLU B CG 1 ATOM 6299 C CD . GLU B 1 385 ? 30.794 -62.808 8.894 1.00 106.94 ? 415 GLU B CD 1 ATOM 6300 O OE1 . GLU B 1 385 ? 31.468 -63.845 8.731 1.00 104.58 ? 415 GLU B OE1 1 ATOM 6301 O OE2 . GLU B 1 385 ? 31.135 -61.919 9.698 1.00 109.58 ? 415 GLU B OE2 1 ATOM 6302 N N . PHE B 1 386 ? 26.989 -66.168 6.923 1.00 92.06 ? 416 PHE B N 1 ATOM 6303 C CA . PHE B 1 386 ? 26.446 -67.471 7.247 1.00 91.52 ? 416 PHE B CA 1 ATOM 6304 C C . PHE B 1 386 ? 27.602 -68.319 7.741 1.00 94.96 ? 416 PHE B C 1 ATOM 6305 O O . PHE B 1 386 ? 28.753 -67.884 7.796 1.00 91.74 ? 416 PHE B O 1 ATOM 6306 C CB . PHE B 1 386 ? 25.856 -68.175 6.021 1.00 90.92 ? 416 PHE B CB 1 ATOM 6307 C CG . PHE B 1 386 ? 24.712 -67.460 5.395 1.00 89.65 ? 416 PHE B CG 1 ATOM 6308 C CD1 . PHE B 1 386 ? 23.421 -67.656 5.857 1.00 92.55 ? 416 PHE B CD1 1 ATOM 6309 C CD2 . PHE B 1 386 ? 24.919 -66.603 4.329 1.00 87.77 ? 416 PHE B CD2 1 ATOM 6310 C CE1 . PHE B 1 386 ? 22.355 -66.986 5.276 1.00 92.95 ? 416 PHE B CE1 1 ATOM 6311 C CE2 . PHE B 1 386 ? 23.863 -65.936 3.742 1.00 86.17 ? 416 PHE B CE2 1 ATOM 6312 C CZ . PHE B 1 386 ? 22.580 -66.128 4.212 1.00 89.55 ? 416 PHE B CZ 1 ATOM 6313 N N . SER B 1 387 ? 27.288 -69.551 8.081 1.00 100.93 ? 417 SER B N 1 ATOM 6314 C CA . SER B 1 387 ? 28.263 -70.448 8.633 1.00 105.27 ? 417 SER B CA 1 ATOM 6315 C C . SER B 1 387 ? 29.250 -70.811 7.522 1.00 103.94 ? 417 SER B C 1 ATOM 6316 O O . SER B 1 387 ? 28.868 -71.473 6.561 1.00 99.35 ? 417 SER B O 1 ATOM 6317 C CB . SER B 1 387 ? 27.507 -71.666 9.174 1.00 106.22 ? 417 SER B CB 1 ATOM 6318 O OG . SER B 1 387 ? 28.283 -72.422 10.072 1.00 109.13 ? 417 SER B OG 1 ATOM 6319 N N . HIS B 1 388 ? 30.490 -70.322 7.636 1.00 102.23 ? 418 HIS B N 1 ATOM 6320 C CA . HIS B 1 388 ? 31.566 -70.588 6.659 1.00 103.28 ? 418 HIS B CA 1 ATOM 6321 C C . HIS B 1 388 ? 31.430 -69.863 5.325 1.00 98.10 ? 418 HIS B C 1 ATOM 6322 O O . HIS B 1 388 ? 32.304 -69.977 4.470 1.00 98.74 ? 418 HIS B O 1 ATOM 6323 C CB . HIS B 1 388 ? 31.712 -72.088 6.382 1.00 109.96 ? 418 HIS B CB 1 ATOM 6324 C CG . HIS B 1 388 ? 32.087 -72.875 7.589 1.00 115.40 ? 418 HIS B CG 1 ATOM 6325 N ND1 . HIS B 1 388 ? 31.152 -73.415 8.445 1.00 123.57 ? 418 HIS B ND1 1 ATOM 6326 C CD2 . HIS B 1 388 ? 33.295 -73.192 8.098 1.00 117.12 ? 418 HIS B CD2 1 ATOM 6327 C CE1 . HIS B 1 388 ? 31.771 -74.038 9.429 1.00 128.34 ? 418 HIS B CE1 1 ATOM 6328 N NE2 . HIS B 1 388 ? 33.072 -73.918 9.241 1.00 126.21 ? 418 HIS B NE2 1 ATOM 6329 N N . ILE B 1 389 ? 30.352 -69.122 5.131 1.00 94.24 ? 419 ILE B N 1 ATOM 6330 C CA . ILE B 1 389 ? 30.179 -68.389 3.889 1.00 87.07 ? 419 ILE B CA 1 ATOM 6331 C C . ILE B 1 389 ? 29.578 -67.011 4.130 1.00 83.23 ? 419 ILE B C 1 ATOM 6332 O O . ILE B 1 389 ? 28.533 -66.874 4.751 1.00 80.64 ? 419 ILE B O 1 ATOM 6333 C CB . ILE B 1 389 ? 29.355 -69.189 2.874 1.00 84.70 ? 419 ILE B CB 1 ATOM 6334 C CG1 . ILE B 1 389 ? 29.356 -68.490 1.521 1.00 82.33 ? 419 ILE B CG1 1 ATOM 6335 C CG2 . ILE B 1 389 ? 27.939 -69.408 3.367 1.00 87.85 ? 419 ILE B CG2 1 ATOM 6336 C CD1 . ILE B 1 389 ? 29.043 -69.427 0.386 1.00 84.04 ? 419 ILE B CD1 1 ATOM 6337 N N . ALA B 1 390 ? 30.269 -65.996 3.623 1.00 82.38 ? 420 ALA B N 1 ATOM 6338 C CA . ALA B 1 390 ? 29.869 -64.601 3.774 1.00 78.48 ? 420 ALA B CA 1 ATOM 6339 C C . ALA B 1 390 ? 29.609 -64.013 2.412 1.00 75.14 ? 420 ALA B C 1 ATOM 6340 O O . ALA B 1 390 ? 30.312 -64.337 1.463 1.00 71.00 ? 420 ALA B O 1 ATOM 6341 C CB . ALA B 1 390 ? 30.979 -63.824 4.435 1.00 76.78 ? 420 ALA B CB 1 ATOM 6342 N N . PHE B 1 391 ? 28.592 -63.168 2.311 1.00 78.07 ? 421 PHE B N 1 ATOM 6343 C CA . PHE B 1 391 ? 28.444 -62.302 1.145 1.00 77.66 ? 421 PHE B CA 1 ATOM 6344 C C . PHE B 1 391 ? 28.703 -60.862 1.524 1.00 75.83 ? 421 PHE B C 1 ATOM 6345 O O . PHE B 1 391 ? 28.293 -60.412 2.584 1.00 77.99 ? 421 PHE B O 1 ATOM 6346 C CB . PHE B 1 391 ? 27.065 -62.388 0.529 1.00 77.70 ? 421 PHE B CB 1 ATOM 6347 C CG . PHE B 1 391 ? 26.896 -61.463 -0.632 1.00 75.87 ? 421 PHE B CG 1 ATOM 6348 C CD1 . PHE B 1 391 ? 27.509 -61.743 -1.848 1.00 72.66 ? 421 PHE B CD1 1 ATOM 6349 C CD2 . PHE B 1 391 ? 26.186 -60.285 -0.497 1.00 72.93 ? 421 PHE B CD2 1 ATOM 6350 C CE1 . PHE B 1 391 ? 27.381 -60.882 -2.920 1.00 69.71 ? 421 PHE B CE1 1 ATOM 6351 C CE2 . PHE B 1 391 ? 26.057 -59.422 -1.564 1.00 69.79 ? 421 PHE B CE2 1 ATOM 6352 C CZ . PHE B 1 391 ? 26.653 -59.718 -2.776 1.00 69.07 ? 421 PHE B CZ 1 ATOM 6353 N N . LEU B 1 392 ? 29.349 -60.125 0.641 1.00 73.36 ? 422 LEU B N 1 ATOM 6354 C CA . LEU B 1 392 ? 29.783 -58.788 0.995 1.00 72.55 ? 422 LEU B CA 1 ATOM 6355 C C . LEU B 1 392 ? 29.886 -57.911 -0.243 1.00 67.57 ? 422 LEU B C 1 ATOM 6356 O O . LEU B 1 392 ? 30.339 -58.375 -1.266 1.00 65.71 ? 422 LEU B O 1 ATOM 6357 C CB . LEU B 1 392 ? 31.124 -58.914 1.695 1.00 74.22 ? 422 LEU B CB 1 ATOM 6358 C CG . LEU B 1 392 ? 31.909 -57.682 2.082 1.00 73.53 ? 422 LEU B CG 1 ATOM 6359 C CD1 . LEU B 1 392 ? 32.617 -57.947 3.389 1.00 76.25 ? 422 LEU B CD1 1 ATOM 6360 C CD2 . LEU B 1 392 ? 32.911 -57.320 1.002 1.00 73.79 ? 422 LEU B CD2 1 ATOM 6361 N N . THR B 1 393 ? 29.430 -56.661 -0.148 1.00 65.62 ? 423 THR B N 1 ATOM 6362 C CA . THR B 1 393 ? 29.519 -55.712 -1.253 1.00 61.13 ? 423 THR B CA 1 ATOM 6363 C C . THR B 1 393 ? 30.574 -54.672 -1.009 1.00 61.79 ? 423 THR B C 1 ATOM 6364 O O . THR B 1 393 ? 30.973 -54.443 0.127 1.00 67.57 ? 423 THR B O 1 ATOM 6365 C CB . THR B 1 393 ? 28.220 -54.922 -1.467 1.00 61.76 ? 423 THR B CB 1 ATOM 6366 O OG1 . THR B 1 393 ? 27.967 -54.102 -0.329 1.00 59.94 ? 423 THR B OG1 1 ATOM 6367 C CG2 . THR B 1 393 ? 27.036 -55.849 -1.741 1.00 63.57 ? 423 THR B CG2 1 ATOM 6368 N N . ILE B 1 394 ? 31.014 -54.035 -2.088 1.00 59.07 ? 424 ILE B N 1 ATOM 6369 C CA . ILE B 1 394 ? 31.914 -52.896 -2.011 1.00 56.84 ? 424 ILE B CA 1 ATOM 6370 C C . ILE B 1 394 ? 31.249 -51.700 -2.685 1.00 55.62 ? 424 ILE B C 1 ATOM 6371 O O . ILE B 1 394 ? 31.186 -51.599 -3.906 1.00 55.36 ? 424 ILE B O 1 ATOM 6372 C CB . ILE B 1 394 ? 33.273 -53.187 -2.646 1.00 56.80 ? 424 ILE B CB 1 ATOM 6373 C CG1 . ILE B 1 394 ? 34.018 -54.246 -1.844 1.00 58.79 ? 424 ILE B CG1 1 ATOM 6374 C CG2 . ILE B 1 394 ? 34.120 -51.934 -2.653 1.00 59.07 ? 424 ILE B CG2 1 ATOM 6375 C CD1 . ILE B 1 394 ? 33.530 -55.653 -2.042 1.00 61.68 ? 424 ILE B CD1 1 ATOM 6376 N N . LYS B 1 395 ? 30.769 -50.780 -1.863 1.00 54.00 ? 425 LYS B N 1 ATOM 6377 C CA . LYS B 1 395 ? 29.958 -49.698 -2.340 1.00 53.74 ? 425 LYS B CA 1 ATOM 6378 C C . LYS B 1 395 ? 30.731 -48.828 -3.289 1.00 54.38 ? 425 LYS B C 1 ATOM 6379 O O . LYS B 1 395 ? 31.825 -48.429 -2.991 1.00 56.17 ? 425 LYS B O 1 ATOM 6380 C CB . LYS B 1 395 ? 29.452 -48.886 -1.167 1.00 54.59 ? 425 LYS B CB 1 ATOM 6381 C CG . LYS B 1 395 ? 28.512 -47.764 -1.544 1.00 54.65 ? 425 LYS B CG 1 ATOM 6382 C CD . LYS B 1 395 ? 27.737 -47.274 -0.326 1.00 55.25 ? 425 LYS B CD 1 ATOM 6383 C CE . LYS B 1 395 ? 28.629 -46.603 0.697 1.00 55.80 ? 425 LYS B CE 1 ATOM 6384 N NZ . LYS B 1 395 ? 29.274 -45.388 0.141 1.00 56.85 ? 425 LYS B NZ 1 ATOM 6385 N N . GLY B 1 396 ? 30.146 -48.545 -4.444 1.00 56.34 ? 426 GLY B N 1 ATOM 6386 C CA . GLY B 1 396 ? 30.783 -47.712 -5.449 1.00 55.76 ? 426 GLY B CA 1 ATOM 6387 C C . GLY B 1 396 ? 31.951 -48.337 -6.175 1.00 56.24 ? 426 GLY B C 1 ATOM 6388 O O . GLY B 1 396 ? 32.736 -47.618 -6.780 1.00 56.42 ? 426 GLY B O 1 ATOM 6389 N N . ALA B 1 397 ? 32.068 -49.661 -6.139 1.00 57.48 ? 427 ALA B N 1 ATOM 6390 C CA . ALA B 1 397 ? 33.117 -50.364 -6.890 1.00 57.58 ? 427 ALA B CA 1 ATOM 6391 C C . ALA B 1 397 ? 32.526 -51.155 -8.037 1.00 57.28 ? 427 ALA B C 1 ATOM 6392 O O . ALA B 1 397 ? 31.399 -51.647 -7.964 1.00 60.02 ? 427 ALA B O 1 ATOM 6393 C CB . ALA B 1 397 ? 33.901 -51.287 -5.988 1.00 56.32 ? 427 ALA B CB 1 ATOM 6394 N N . GLY B 1 398 ? 33.299 -51.279 -9.102 1.00 56.72 ? 428 GLY B N 1 ATOM 6395 C CA . GLY B 1 398 ? 32.849 -51.973 -10.286 1.00 57.66 ? 428 GLY B CA 1 ATOM 6396 C C . GLY B 1 398 ? 33.290 -53.409 -10.289 1.00 58.06 ? 428 GLY B C 1 ATOM 6397 O O . GLY B 1 398 ? 33.537 -53.998 -9.237 1.00 58.29 ? 428 GLY B O 1 ATOM 6398 N N . HIS B 1 399 ? 33.394 -53.953 -11.498 1.00 59.63 ? 429 HIS B N 1 ATOM 6399 C CA . HIS B 1 399 ? 33.747 -55.343 -11.741 1.00 59.64 ? 429 HIS B CA 1 ATOM 6400 C C . HIS B 1 399 ? 35.101 -55.678 -11.147 1.00 59.17 ? 429 HIS B C 1 ATOM 6401 O O . HIS B 1 399 ? 35.344 -56.815 -10.774 1.00 59.63 ? 429 HIS B O 1 ATOM 6402 C CB . HIS B 1 399 ? 33.755 -55.597 -13.257 1.00 61.15 ? 429 HIS B CB 1 ATOM 6403 C CG . HIS B 1 399 ? 33.731 -57.039 -13.642 1.00 63.26 ? 429 HIS B CG 1 ATOM 6404 N ND1 . HIS B 1 399 ? 32.708 -57.885 -13.289 1.00 65.30 ? 429 HIS B ND1 1 ATOM 6405 C CD2 . HIS B 1 399 ? 34.587 -57.771 -14.392 1.00 66.19 ? 429 HIS B CD2 1 ATOM 6406 C CE1 . HIS B 1 399 ? 32.947 -59.085 -13.785 1.00 69.95 ? 429 HIS B CE1 1 ATOM 6407 N NE2 . HIS B 1 399 ? 34.084 -59.044 -14.452 1.00 67.80 ? 429 HIS B NE2 1 ATOM 6408 N N . MET B 1 400 ? 35.989 -54.693 -11.082 1.00 61.68 ? 430 MET B N 1 ATOM 6409 C CA . MET B 1 400 ? 37.345 -54.918 -10.605 1.00 62.55 ? 430 MET B CA 1 ATOM 6410 C C . MET B 1 400 ? 37.559 -54.130 -9.345 1.00 61.80 ? 430 MET B C 1 ATOM 6411 O O . MET B 1 400 ? 38.074 -53.017 -9.362 1.00 69.54 ? 430 MET B O 1 ATOM 6412 C CB . MET B 1 400 ? 38.357 -54.572 -11.687 1.00 66.46 ? 430 MET B CB 1 ATOM 6413 C CG . MET B 1 400 ? 38.385 -55.641 -12.768 1.00 71.24 ? 430 MET B CG 1 ATOM 6414 S SD . MET B 1 400 ? 39.008 -55.121 -14.362 1.00 77.78 ? 430 MET B SD 1 ATOM 6415 C CE . MET B 1 400 ? 40.648 -54.552 -13.905 1.00 76.81 ? 430 MET B CE 1 ATOM 6416 N N . VAL B 1 401 ? 37.146 -54.748 -8.251 1.00 59.89 ? 431 VAL B N 1 ATOM 6417 C CA . VAL B 1 401 ? 37.102 -54.137 -6.941 1.00 59.24 ? 431 VAL B CA 1 ATOM 6418 C C . VAL B 1 401 ? 38.416 -53.491 -6.535 1.00 60.07 ? 431 VAL B C 1 ATOM 6419 O O . VAL B 1 401 ? 38.440 -52.293 -6.247 1.00 60.87 ? 431 VAL B O 1 ATOM 6420 C CB . VAL B 1 401 ? 36.617 -55.164 -5.893 1.00 62.69 ? 431 VAL B CB 1 ATOM 6421 C CG1 . VAL B 1 401 ? 36.973 -54.752 -4.471 1.00 64.34 ? 431 VAL B CG1 1 ATOM 6422 C CG2 . VAL B 1 401 ? 35.119 -55.380 -6.044 1.00 62.04 ? 431 VAL B CG2 1 ATOM 6423 N N . PRO B 1 402 ? 39.522 -54.258 -6.520 1.00 60.18 ? 432 PRO B N 1 ATOM 6424 C CA . PRO B 1 402 ? 40.813 -53.684 -6.078 1.00 59.13 ? 432 PRO B CA 1 ATOM 6425 C C . PRO B 1 402 ? 41.293 -52.459 -6.857 1.00 62.08 ? 432 PRO B C 1 ATOM 6426 O O . PRO B 1 402 ? 42.099 -51.698 -6.334 1.00 70.22 ? 432 PRO B O 1 ATOM 6427 C CB . PRO B 1 402 ? 41.800 -54.827 -6.291 1.00 60.18 ? 432 PRO B CB 1 ATOM 6428 C CG . PRO B 1 402 ? 40.967 -56.063 -6.280 1.00 62.49 ? 432 PRO B CG 1 ATOM 6429 C CD . PRO B 1 402 ? 39.663 -55.667 -6.912 1.00 60.62 ? 432 PRO B CD 1 ATOM 6430 N N . THR B 1 403 ? 40.829 -52.285 -8.095 1.00 59.22 ? 433 THR B N 1 ATOM 6431 C CA . THR B 1 403 ? 41.157 -51.101 -8.898 1.00 58.86 ? 433 THR B CA 1 ATOM 6432 C C . THR B 1 403 ? 40.302 -49.900 -8.465 1.00 57.89 ? 433 THR B C 1 ATOM 6433 O O . THR B 1 403 ? 40.804 -48.815 -8.208 1.00 57.86 ? 433 THR B O 1 ATOM 6434 C CB . THR B 1 403 ? 40.893 -51.355 -10.404 1.00 57.26 ? 433 THR B CB 1 ATOM 6435 O OG1 . THR B 1 403 ? 41.457 -52.604 -10.804 1.00 55.31 ? 433 THR B OG1 1 ATOM 6436 C CG2 . THR B 1 403 ? 41.461 -50.229 -11.255 1.00 55.28 ? 433 THR B CG2 1 ATOM 6437 N N . ASP B 1 404 ? 39.000 -50.105 -8.403 1.00 57.55 ? 434 ASP B N 1 ATOM 6438 C CA . ASP B 1 404 ? 38.090 -49.048 -8.023 1.00 58.38 ? 434 ASP B CA 1 ATOM 6439 C C . ASP B 1 404 ? 38.265 -48.664 -6.520 1.00 58.49 ? 434 ASP B C 1 ATOM 6440 O O . ASP B 1 404 ? 38.274 -47.492 -6.198 1.00 54.67 ? 434 ASP B O 1 ATOM 6441 C CB . ASP B 1 404 ? 36.644 -49.458 -8.371 1.00 59.99 ? 434 ASP B CB 1 ATOM 6442 C CG . ASP B 1 404 ? 36.449 -49.760 -9.882 1.00 63.75 ? 434 ASP B CG 1 ATOM 6443 O OD1 . ASP B 1 404 ? 37.109 -49.120 -10.731 1.00 62.81 ? 434 ASP B OD1 1 ATOM 6444 O OD2 . ASP B 1 404 ? 35.628 -50.640 -10.224 1.00 64.66 ? 434 ASP B OD2 1 ATOM 6445 N N . LYS B 1 405 ? 38.434 -49.649 -5.634 1.00 58.23 ? 435 LYS B N 1 ATOM 6446 C CA . LYS B 1 405 ? 38.537 -49.417 -4.187 1.00 62.76 ? 435 LYS B CA 1 ATOM 6447 C C . LYS B 1 405 ? 39.617 -50.299 -3.584 1.00 65.95 ? 435 LYS B C 1 ATOM 6448 O O . LYS B 1 405 ? 39.308 -51.322 -2.961 1.00 68.15 ? 435 LYS B O 1 ATOM 6449 C CB . LYS B 1 405 ? 37.211 -49.724 -3.455 1.00 63.63 ? 435 LYS B CB 1 ATOM 6450 C CG . LYS B 1 405 ? 35.984 -48.998 -3.982 1.00 62.60 ? 435 LYS B CG 1 ATOM 6451 C CD . LYS B 1 405 ? 36.000 -47.504 -3.715 1.00 62.73 ? 435 LYS B CD 1 ATOM 6452 C CE . LYS B 1 405 ? 34.791 -46.848 -4.351 1.00 64.11 ? 435 LYS B CE 1 ATOM 6453 N NZ . LYS B 1 405 ? 34.573 -45.470 -3.845 1.00 64.25 ? 435 LYS B NZ 1 ATOM 6454 N N . PRO B 1 406 ? 40.889 -49.923 -3.772 1.00 65.63 ? 436 PRO B N 1 ATOM 6455 C CA . PRO B 1 406 ? 41.963 -50.756 -3.244 1.00 62.74 ? 436 PRO B CA 1 ATOM 6456 C C . PRO B 1 406 ? 41.913 -50.933 -1.722 1.00 64.22 ? 436 PRO B C 1 ATOM 6457 O O . PRO B 1 406 ? 42.011 -52.063 -1.223 1.00 58.50 ? 436 PRO B O 1 ATOM 6458 C CB . PRO B 1 406 ? 43.245 -50.025 -3.675 1.00 63.82 ? 436 PRO B CB 1 ATOM 6459 C CG . PRO B 1 406 ? 42.836 -48.745 -4.302 1.00 63.80 ? 436 PRO B CG 1 ATOM 6460 C CD . PRO B 1 406 ? 41.381 -48.849 -4.650 1.00 64.79 ? 436 PRO B CD 1 ATOM 6461 N N . LEU B 1 407 ? 41.763 -49.838 -0.987 1.00 66.36 ? 437 LEU B N 1 ATOM 6462 C CA . LEU B 1 407 ? 41.853 -49.920 0.472 1.00 69.80 ? 437 LEU B CA 1 ATOM 6463 C C . LEU B 1 407 ? 40.769 -50.820 1.043 1.00 68.92 ? 437 LEU B C 1 ATOM 6464 O O . LEU B 1 407 ? 41.034 -51.683 1.886 1.00 68.68 ? 437 LEU B O 1 ATOM 6465 C CB . LEU B 1 407 ? 41.762 -48.542 1.110 1.00 70.36 ? 437 LEU B CB 1 ATOM 6466 C CG . LEU B 1 407 ? 41.827 -48.545 2.636 1.00 71.60 ? 437 LEU B CG 1 ATOM 6467 C CD1 . LEU B 1 407 ? 43.057 -49.270 3.141 1.00 75.80 ? 437 LEU B CD1 1 ATOM 6468 C CD2 . LEU B 1 407 ? 41.807 -47.129 3.158 1.00 73.43 ? 437 LEU B CD2 1 ATOM 6469 N N . ALA B 1 408 ? 39.549 -50.619 0.572 1.00 66.88 ? 438 ALA B N 1 ATOM 6470 C CA . ALA B 1 408 ? 38.444 -51.469 0.973 1.00 69.37 ? 438 ALA B CA 1 ATOM 6471 C C . ALA B 1 408 ? 38.707 -52.923 0.587 1.00 69.88 ? 438 ALA B C 1 ATOM 6472 O O . ALA B 1 408 ? 38.425 -53.831 1.360 1.00 72.72 ? 438 ALA B O 1 ATOM 6473 C CB . ALA B 1 408 ? 37.156 -50.982 0.337 1.00 71.14 ? 438 ALA B CB 1 ATOM 6474 N N . ALA B 1 409 ? 39.263 -53.132 -0.604 1.00 69.42 ? 439 ALA B N 1 ATOM 6475 C CA . ALA B 1 409 ? 39.579 -54.478 -1.086 1.00 67.99 ? 439 ALA B CA 1 ATOM 6476 C C . ALA B 1 409 ? 40.641 -55.142 -0.234 1.00 69.21 ? 439 ALA B C 1 ATOM 6477 O O . ALA B 1 409 ? 40.575 -56.336 0.023 1.00 69.22 ? 439 ALA B O 1 ATOM 6478 C CB . ALA B 1 409 ? 40.044 -54.430 -2.527 1.00 67.11 ? 439 ALA B CB 1 ATOM 6479 N N . PHE B 1 410 ? 41.630 -54.367 0.190 1.00 71.34 ? 440 PHE B N 1 ATOM 6480 C CA . PHE B 1 410 ? 42.694 -54.898 1.038 1.00 72.15 ? 440 PHE B CA 1 ATOM 6481 C C . PHE B 1 410 ? 42.130 -55.268 2.403 1.00 70.80 ? 440 PHE B C 1 ATOM 6482 O O . PHE B 1 410 ? 42.362 -56.362 2.901 1.00 67.42 ? 440 PHE B O 1 ATOM 6483 C CB . PHE B 1 410 ? 43.839 -53.888 1.192 1.00 73.10 ? 440 PHE B CB 1 ATOM 6484 C CG . PHE B 1 410 ? 44.975 -54.407 1.994 1.00 76.72 ? 440 PHE B CG 1 ATOM 6485 C CD1 . PHE B 1 410 ? 45.891 -55.285 1.423 1.00 81.36 ? 440 PHE B CD1 1 ATOM 6486 C CD2 . PHE B 1 410 ? 45.115 -54.062 3.330 1.00 79.77 ? 440 PHE B CD2 1 ATOM 6487 C CE1 . PHE B 1 410 ? 46.938 -55.798 2.170 1.00 83.87 ? 440 PHE B CE1 1 ATOM 6488 C CE2 . PHE B 1 410 ? 46.161 -54.560 4.085 1.00 82.80 ? 440 PHE B CE2 1 ATOM 6489 C CZ . PHE B 1 410 ? 47.072 -55.430 3.508 1.00 86.91 ? 440 PHE B CZ 1 ATOM 6490 N N . THR B 1 411 ? 41.376 -54.347 2.990 1.00 72.06 ? 441 THR B N 1 ATOM 6491 C CA . THR B 1 411 ? 40.758 -54.568 4.293 1.00 75.73 ? 441 THR B CA 1 ATOM 6492 C C . THR B 1 411 ? 39.957 -55.858 4.301 1.00 76.39 ? 441 THR B C 1 ATOM 6493 O O . THR B 1 411 ? 40.106 -56.689 5.191 1.00 83.05 ? 441 THR B O 1 ATOM 6494 C CB . THR B 1 411 ? 39.814 -53.415 4.671 1.00 73.38 ? 441 THR B CB 1 ATOM 6495 O OG1 . THR B 1 411 ? 40.568 -52.212 4.825 1.00 76.15 ? 441 THR B OG1 1 ATOM 6496 C CG2 . THR B 1 411 ? 39.106 -53.714 5.962 1.00 72.94 ? 441 THR B CG2 1 ATOM 6497 N N . MET B 1 412 ? 39.083 -55.981 3.318 1.00 75.44 ? 442 MET B N 1 ATOM 6498 C CA . MET B 1 412 ? 38.225 -57.132 3.175 1.00 76.47 ? 442 MET B CA 1 ATOM 6499 C C . MET B 1 412 ? 39.064 -58.391 3.172 1.00 77.57 ? 442 MET B C 1 ATOM 6500 O O . MET B 1 412 ? 38.815 -59.320 3.924 1.00 79.61 ? 442 MET B O 1 ATOM 6501 C CB . MET B 1 412 ? 37.465 -57.019 1.852 1.00 75.62 ? 442 MET B CB 1 ATOM 6502 C CG . MET B 1 412 ? 36.728 -58.275 1.427 1.00 77.51 ? 442 MET B CG 1 ATOM 6503 S SD . MET B 1 412 ? 36.430 -58.296 -0.345 1.00 77.38 ? 442 MET B SD 1 ATOM 6504 C CE . MET B 1 412 ? 38.070 -58.652 -0.978 1.00 77.80 ? 442 MET B CE 1 ATOM 6505 N N . PHE B 1 413 ? 40.065 -58.387 2.305 1.00 77.83 ? 443 PHE B N 1 ATOM 6506 C CA . PHE B 1 413 ? 40.960 -59.508 2.102 1.00 76.57 ? 443 PHE B CA 1 ATOM 6507 C C . PHE B 1 413 ? 41.741 -59.860 3.369 1.00 77.14 ? 443 PHE B C 1 ATOM 6508 O O . PHE B 1 413 ? 41.779 -61.014 3.780 1.00 75.59 ? 443 PHE B O 1 ATOM 6509 C CB . PHE B 1 413 ? 41.908 -59.159 0.951 1.00 77.07 ? 443 PHE B CB 1 ATOM 6510 C CG . PHE B 1 413 ? 42.941 -60.188 0.690 1.00 76.84 ? 443 PHE B CG 1 ATOM 6511 C CD1 . PHE B 1 413 ? 42.580 -61.428 0.193 1.00 76.12 ? 443 PHE B CD1 1 ATOM 6512 C CD2 . PHE B 1 413 ? 44.272 -59.921 0.943 1.00 78.31 ? 443 PHE B CD2 1 ATOM 6513 C CE1 . PHE B 1 413 ? 43.536 -62.393 -0.034 1.00 78.95 ? 443 PHE B CE1 1 ATOM 6514 C CE2 . PHE B 1 413 ? 45.239 -60.877 0.712 1.00 80.40 ? 443 PHE B CE2 1 ATOM 6515 C CZ . PHE B 1 413 ? 44.871 -62.114 0.221 1.00 81.21 ? 443 PHE B CZ 1 ATOM 6516 N N . SER B 1 414 ? 42.346 -58.854 3.985 1.00 80.48 ? 444 SER B N 1 ATOM 6517 C CA . SER B 1 414 ? 43.042 -59.014 5.267 1.00 84.83 ? 444 SER B CA 1 ATOM 6518 C C . SER B 1 414 ? 42.175 -59.640 6.349 1.00 86.26 ? 444 SER B C 1 ATOM 6519 O O . SER B 1 414 ? 42.604 -60.544 7.061 1.00 85.68 ? 444 SER B O 1 ATOM 6520 C CB . SER B 1 414 ? 43.528 -57.667 5.772 1.00 88.03 ? 444 SER B CB 1 ATOM 6521 O OG . SER B 1 414 ? 44.314 -57.850 6.929 1.00 94.13 ? 444 SER B OG 1 ATOM 6522 N N . ARG B 1 415 ? 40.951 -59.144 6.464 1.00 85.98 ? 445 ARG B N 1 ATOM 6523 C CA . ARG B 1 415 ? 39.980 -59.677 7.421 1.00 88.20 ? 445 ARG B CA 1 ATOM 6524 C C . ARG B 1 415 ? 39.486 -61.075 7.055 1.00 89.07 ? 445 ARG B C 1 ATOM 6525 O O . ARG B 1 415 ? 39.007 -61.803 7.917 1.00 96.86 ? 445 ARG B O 1 ATOM 6526 C CB . ARG B 1 415 ? 38.802 -58.716 7.553 1.00 86.47 ? 445 ARG B CB 1 ATOM 6527 C CG . ARG B 1 415 ? 39.211 -57.413 8.202 1.00 89.82 ? 445 ARG B CG 1 ATOM 6528 C CD . ARG B 1 415 ? 38.152 -56.329 8.126 1.00 88.93 ? 445 ARG B CD 1 ATOM 6529 N NE . ARG B 1 415 ? 38.561 -55.167 8.909 1.00 90.31 ? 445 ARG B NE 1 ATOM 6530 C CZ . ARG B 1 415 ? 37.865 -54.041 9.034 1.00 94.38 ? 445 ARG B CZ 1 ATOM 6531 N NH1 . ARG B 1 415 ? 36.692 -53.890 8.426 1.00 89.26 ? 445 ARG B NH1 1 ATOM 6532 N NH2 . ARG B 1 415 ? 38.350 -53.052 9.778 1.00 100.38 ? 445 ARG B NH2 1 ATOM 6533 N N . PHE B 1 416 ? 39.585 -61.424 5.775 1.00 86.65 ? 446 PHE B N 1 ATOM 6534 C CA . PHE B 1 416 ? 39.197 -62.734 5.279 1.00 85.96 ? 446 PHE B CA 1 ATOM 6535 C C . PHE B 1 416 ? 40.291 -63.709 5.657 1.00 90.26 ? 446 PHE B C 1 ATOM 6536 O O . PHE B 1 416 ? 40.034 -64.703 6.345 1.00 90.05 ? 446 PHE B O 1 ATOM 6537 C CB . PHE B 1 416 ? 38.983 -62.676 3.752 1.00 81.31 ? 446 PHE B CB 1 ATOM 6538 C CG . PHE B 1 416 ? 38.924 -64.021 3.064 1.00 78.97 ? 446 PHE B CG 1 ATOM 6539 C CD1 . PHE B 1 416 ? 37.807 -64.830 3.174 1.00 81.46 ? 446 PHE B CD1 1 ATOM 6540 C CD2 . PHE B 1 416 ? 39.961 -64.450 2.260 1.00 76.91 ? 446 PHE B CD2 1 ATOM 6541 C CE1 . PHE B 1 416 ? 37.747 -66.053 2.521 1.00 80.33 ? 446 PHE B CE1 1 ATOM 6542 C CE2 . PHE B 1 416 ? 39.900 -65.660 1.593 1.00 75.98 ? 446 PHE B CE2 1 ATOM 6543 C CZ . PHE B 1 416 ? 38.797 -66.468 1.728 1.00 78.13 ? 446 PHE B CZ 1 ATOM 6544 N N . LEU B 1 417 ? 41.512 -63.405 5.222 1.00 93.16 ? 447 LEU B N 1 ATOM 6545 C CA . LEU B 1 417 ? 42.681 -64.227 5.547 1.00 98.22 ? 447 LEU B CA 1 ATOM 6546 C C . LEU B 1 417 ? 42.796 -64.518 7.035 1.00 101.53 ? 447 LEU B C 1 ATOM 6547 O O . LEU B 1 417 ? 43.141 -65.624 7.430 1.00 104.81 ? 447 LEU B O 1 ATOM 6548 C CB . LEU B 1 417 ? 43.976 -63.550 5.097 1.00 95.64 ? 447 LEU B CB 1 ATOM 6549 C CG . LEU B 1 417 ? 44.413 -63.730 3.647 1.00 95.50 ? 447 LEU B CG 1 ATOM 6550 C CD1 . LEU B 1 417 ? 45.875 -63.358 3.527 1.00 93.75 ? 447 LEU B CD1 1 ATOM 6551 C CD2 . LEU B 1 417 ? 44.202 -65.145 3.133 1.00 95.69 ? 447 LEU B CD2 1 ATOM 6552 N N . ASN B 1 418 ? 42.501 -63.516 7.850 1.00 104.16 ? 448 ASN B N 1 ATOM 6553 C CA . ASN B 1 418 ? 42.654 -63.620 9.298 1.00 105.64 ? 448 ASN B CA 1 ATOM 6554 C C . ASN B 1 418 ? 41.387 -64.060 10.042 1.00 104.58 ? 448 ASN B C 1 ATOM 6555 O O . ASN B 1 418 ? 41.218 -63.717 11.198 1.00 107.50 ? 448 ASN B O 1 ATOM 6556 C CB . ASN B 1 418 ? 43.171 -62.280 9.850 1.00 103.82 ? 448 ASN B CB 1 ATOM 6557 C CG . ASN B 1 418 ? 44.553 -61.936 9.333 1.00 101.38 ? 448 ASN B CG 1 ATOM 6558 O OD1 . ASN B 1 418 ? 45.506 -62.632 9.623 1.00 102.55 ? 448 ASN B OD1 1 ATOM 6559 N ND2 . ASN B 1 418 ? 44.661 -60.877 8.549 1.00 102.89 ? 448 ASN B ND2 1 ATOM 6560 N N . LYS B 1 419 ? 40.502 -64.815 9.395 1.00 108.16 ? 449 LYS B N 1 ATOM 6561 C CA . LYS B 1 419 ? 39.286 -65.329 10.055 1.00 117.79 ? 449 LYS B CA 1 ATOM 6562 C C . LYS B 1 419 ? 38.589 -64.293 10.949 1.00 122.68 ? 449 LYS B C 1 ATOM 6563 O O . LYS B 1 419 ? 38.015 -64.653 11.978 1.00 118.50 ? 449 LYS B O 1 ATOM 6564 C CB . LYS B 1 419 ? 39.599 -66.550 10.936 1.00 124.35 ? 449 LYS B CB 1 ATOM 6565 C CG . LYS B 1 419 ? 40.607 -67.549 10.391 1.00 127.25 ? 449 LYS B CG 1 ATOM 6566 C CD . LYS B 1 419 ? 40.724 -68.738 11.337 1.00 129.76 ? 449 LYS B CD 1 ATOM 6567 C CE . LYS B 1 419 ? 42.065 -69.434 11.222 1.00 131.32 ? 449 LYS B CE 1 ATOM 6568 N NZ . LYS B 1 419 ? 42.334 -69.905 9.836 1.00 131.32 ? 449 LYS B NZ 1 ATOM 6569 N N . GLN B 1 420 ? 38.644 -63.024 10.560 1.00 129.28 ? 450 GLN B N 1 ATOM 6570 C CA . GLN B 1 420 ? 38.146 -61.927 11.396 1.00 134.83 ? 450 GLN B CA 1 ATOM 6571 C C . GLN B 1 420 ? 36.782 -61.419 10.912 1.00 140.28 ? 450 GLN B C 1 ATOM 6572 O O . GLN B 1 420 ? 36.443 -61.570 9.727 1.00 134.70 ? 450 GLN B O 1 ATOM 6573 C CB . GLN B 1 420 ? 39.155 -60.775 11.404 1.00 134.18 ? 450 GLN B CB 1 ATOM 6574 C CG . GLN B 1 420 ? 40.274 -60.920 12.426 1.00 135.34 ? 450 GLN B CG 1 ATOM 6575 C CD . GLN B 1 420 ? 41.552 -60.200 12.024 1.00 132.97 ? 450 GLN B CD 1 ATOM 6576 O OE1 . GLN B 1 420 ? 41.565 -59.391 11.095 1.00 123.36 ? 450 GLN B OE1 1 ATOM 6577 N NE2 . GLN B 1 420 ? 42.637 -60.496 12.729 1.00 136.35 ? 450 GLN B NE2 1 ATOM 6578 N N . PRO B 1 421 ? 35.994 -60.815 11.824 1.00 143.27 ? 451 PRO B N 1 ATOM 6579 C CA . PRO B 1 421 ? 34.735 -60.186 11.413 1.00 135.92 ? 451 PRO B CA 1 ATOM 6580 C C . PRO B 1 421 ? 35.012 -58.951 10.556 1.00 125.27 ? 451 PRO B C 1 ATOM 6581 O O . PRO B 1 421 ? 35.980 -58.233 10.815 1.00 119.73 ? 451 PRO B O 1 ATOM 6582 C CB . PRO B 1 421 ? 34.078 -59.807 12.746 1.00 139.19 ? 451 PRO B CB 1 ATOM 6583 C CG . PRO B 1 421 ? 35.210 -59.655 13.703 1.00 141.60 ? 451 PRO B CG 1 ATOM 6584 C CD . PRO B 1 421 ? 36.260 -60.635 13.266 1.00 142.44 ? 451 PRO B CD 1 ATOM 6585 N N . TYR B 1 422 ? 34.177 -58.709 9.546 1.00 118.54 ? 452 TYR B N 1 ATOM 6586 C CA . TYR B 1 422 ? 34.465 -57.676 8.535 1.00 112.17 ? 452 TYR B CA 1 ATOM 6587 C C . TYR B 1 422 ? 34.059 -56.289 9.032 1.00 112.22 ? 452 TYR B C 1 ATOM 6588 O O . TYR B 1 422 ? 34.740 -55.312 8.736 1.00 100.61 ? 452 TYR B O 1 ATOM 6589 C CB . TYR B 1 422 ? 33.798 -57.995 7.188 1.00 103.61 ? 452 TYR B CB 1 ATOM 6590 C CG . TYR B 1 422 ? 34.203 -59.336 6.606 1.00 102.51 ? 452 TYR B CG 1 ATOM 6591 C CD1 . TYR B 1 422 ? 33.619 -60.519 7.064 1.00 102.77 ? 452 TYR B CD1 1 ATOM 6592 C CD2 . TYR B 1 422 ? 35.167 -59.429 5.601 1.00 98.89 ? 452 TYR B CD2 1 ATOM 6593 C CE1 . TYR B 1 422 ? 33.981 -61.746 6.548 1.00 100.71 ? 452 TYR B CE1 1 ATOM 6594 C CE2 . TYR B 1 422 ? 35.538 -60.660 5.077 1.00 97.41 ? 452 TYR B CE2 1 ATOM 6595 C CZ . TYR B 1 422 ? 34.939 -61.815 5.555 1.00 99.99 ? 452 TYR B CZ 1 ATOM 6596 O OH . TYR B 1 422 ? 35.295 -63.054 5.063 1.00 102.14 ? 452 TYR B OH 1 HETATM 6597 C C1 . NAG C 2 . ? -0.090 -20.101 5.840 1.00 131.99 ? 501 NAG A C1 1 HETATM 6598 C C2 . NAG C 2 . ? -1.468 -20.377 6.414 1.00 137.78 ? 501 NAG A C2 1 HETATM 6599 C C3 . NAG C 2 . ? -2.422 -19.268 6.008 1.00 143.08 ? 501 NAG A C3 1 HETATM 6600 C C4 . NAG C 2 . ? -1.872 -17.964 6.516 1.00 143.40 ? 501 NAG A C4 1 HETATM 6601 C C5 . NAG C 2 . ? -0.521 -17.800 5.860 1.00 138.20 ? 501 NAG A C5 1 HETATM 6602 C C6 . NAG C 2 . ? 0.069 -16.446 6.188 1.00 137.30 ? 501 NAG A C6 1 HETATM 6603 C C7 . NAG C 2 . ? -2.093 -22.711 6.779 1.00 137.02 ? 501 NAG A C7 1 HETATM 6604 C C8 . NAG C 2 . ? -2.675 -23.952 6.150 1.00 131.55 ? 501 NAG A C8 1 HETATM 6605 N N2 . NAG C 2 . ? -1.989 -21.649 5.975 1.00 136.65 ? 501 NAG A N2 1 HETATM 6606 O O3 . NAG C 2 . ? -3.650 -19.405 6.643 1.00 152.46 ? 501 NAG A O3 1 HETATM 6607 O O4 . NAG C 2 . ? -2.766 -16.945 6.138 1.00 152.10 ? 501 NAG A O4 1 HETATM 6608 O O5 . NAG C 2 . ? 0.312 -18.843 6.324 1.00 130.39 ? 501 NAG A O5 1 HETATM 6609 O O6 . NAG C 2 . ? 0.318 -16.397 7.569 1.00 134.66 ? 501 NAG A O6 1 HETATM 6610 O O7 . NAG C 2 . ? -1.742 -22.715 7.972 1.00 140.89 ? 501 NAG A O7 1 HETATM 6611 C C1 . NAG D 2 . ? -3.056 -16.053 7.221 1.00 152.66 ? 502 NAG A C1 1 HETATM 6612 C C2 . NAG D 2 . ? -3.816 -14.853 6.696 1.00 155.07 ? 502 NAG A C2 1 HETATM 6613 C C3 . NAG D 2 . ? -4.055 -13.855 7.827 1.00 158.02 ? 502 NAG A C3 1 HETATM 6614 C C4 . NAG D 2 . ? -4.548 -14.543 9.122 1.00 159.26 ? 502 NAG A C4 1 HETATM 6615 C C5 . NAG D 2 . ? -3.788 -15.841 9.395 1.00 154.17 ? 502 NAG A C5 1 HETATM 6616 C C6 . NAG D 2 . ? -4.347 -16.629 10.567 1.00 152.36 ? 502 NAG A C6 1 HETATM 6617 C C7 . NAG D 2 . ? -3.422 -14.535 4.286 1.00 152.56 ? 502 NAG A C7 1 HETATM 6618 C C8 . NAG D 2 . ? -2.602 -13.876 3.224 1.00 150.77 ? 502 NAG A C8 1 HETATM 6619 N N2 . NAG D 2 . ? -3.109 -14.270 5.567 1.00 155.18 ? 502 NAG A N2 1 HETATM 6620 O O3 . NAG D 2 . ? -4.979 -12.907 7.352 1.00 155.21 ? 502 NAG A O3 1 HETATM 6621 O O4 . NAG D 2 . ? -4.433 -13.708 10.269 1.00 161.17 ? 502 NAG A O4 1 HETATM 6622 O O5 . NAG D 2 . ? -3.845 -16.634 8.230 1.00 155.04 ? 502 NAG A O5 1 HETATM 6623 O O6 . NAG D 2 . ? -4.214 -18.008 10.310 1.00 155.49 ? 502 NAG A O6 1 HETATM 6624 O O7 . NAG D 2 . ? -4.326 -15.277 3.929 1.00 148.89 ? 502 NAG A O7 1 HETATM 6625 C C1 . BMA E 3 . ? -5.475 -12.725 10.347 1.00 164.30 ? 503 BMA A C1 1 HETATM 6626 C C2 . BMA E 3 . ? -5.997 -12.542 11.757 1.00 165.27 ? 503 BMA A C2 1 HETATM 6627 C C3 . BMA E 3 . ? -7.241 -11.670 11.731 1.00 168.48 ? 503 BMA A C3 1 HETATM 6628 C C4 . BMA E 3 . ? -7.211 -10.544 10.687 1.00 171.39 ? 503 BMA A C4 1 HETATM 6629 C C5 . BMA E 3 . ? -6.124 -10.602 9.596 1.00 174.65 ? 503 BMA A C5 1 HETATM 6630 C C6 . BMA E 3 . ? -5.583 -9.209 9.262 1.00 174.88 ? 503 BMA A C6 1 HETATM 6631 O O2 . BMA E 3 . ? -5.019 -11.900 12.581 1.00 159.22 ? 503 BMA A O2 1 HETATM 6632 O O3 . BMA E 3 . ? -7.370 -11.064 13.025 1.00 170.24 ? 503 BMA A O3 1 HETATM 6633 O O4 . BMA E 3 . ? -8.476 -10.515 10.019 1.00 164.51 ? 503 BMA A O4 1 HETATM 6634 O O5 . BMA E 3 . ? -5.026 -11.446 9.949 1.00 170.41 ? 503 BMA A O5 1 HETATM 6635 O O6 . BMA E 3 . ? -6.540 -8.487 8.478 1.00 171.16 ? 503 BMA A O6 1 HETATM 6636 C C1 . NAG F 2 . ? 35.266 -28.812 6.403 1.00 144.26 ? 504 NAG A C1 1 HETATM 6637 C C2 . NAG F 2 . ? 36.330 -29.811 6.844 1.00 151.84 ? 504 NAG A C2 1 HETATM 6638 C C3 . NAG F 2 . ? 37.424 -29.120 7.651 1.00 152.09 ? 504 NAG A C3 1 HETATM 6639 C C4 . NAG F 2 . ? 38.017 -27.995 6.817 1.00 152.07 ? 504 NAG A C4 1 HETATM 6640 C C5 . NAG F 2 . ? 36.901 -27.089 6.313 1.00 147.67 ? 504 NAG A C5 1 HETATM 6641 C C6 . NAG F 2 . ? 37.483 -26.004 5.421 1.00 144.39 ? 504 NAG A C6 1 HETATM 6642 C C7 . NAG F 2 . ? 35.645 -32.141 7.057 1.00 157.51 ? 504 NAG A C7 1 HETATM 6643 C C8 . NAG F 2 . ? 35.016 -33.195 7.920 1.00 155.53 ? 504 NAG A C8 1 HETATM 6644 N N2 . NAG F 2 . ? 35.739 -30.920 7.578 1.00 156.85 ? 504 NAG A N2 1 HETATM 6645 O O3 . NAG F 2 . ? 38.435 -30.036 7.992 1.00 150.11 ? 504 NAG A O3 1 HETATM 6646 O O4 . NAG F 2 . ? 38.931 -27.239 7.589 1.00 160.63 ? 504 NAG A O4 1 HETATM 6647 O O5 . NAG F 2 . ? 35.909 -27.823 5.623 1.00 143.42 ? 504 NAG A O5 1 HETATM 6648 O O6 . NAG F 2 . ? 36.916 -26.058 4.134 1.00 146.22 ? 504 NAG A O6 1 HETATM 6649 O O7 . NAG F 2 . ? 36.039 -32.417 5.920 1.00 160.80 ? 504 NAG A O7 1 HETATM 6650 C C1 . NAG G 2 . ? 35.612 -81.090 -22.374 1.00 150.97 ? 501 NAG B C1 1 HETATM 6651 C C2 . NAG G 2 . ? 34.720 -82.022 -23.193 1.00 158.58 ? 501 NAG B C2 1 HETATM 6652 C C3 . NAG G 2 . ? 35.200 -83.480 -23.119 1.00 162.15 ? 501 NAG B C3 1 HETATM 6653 C C4 . NAG G 2 . ? 36.699 -83.582 -23.380 1.00 158.05 ? 501 NAG B C4 1 HETATM 6654 C C5 . NAG G 2 . ? 37.439 -82.573 -22.517 1.00 158.75 ? 501 NAG B C5 1 HETATM 6655 C C6 . NAG G 2 . ? 38.938 -82.593 -22.780 1.00 159.51 ? 501 NAG B C6 1 HETATM 6656 C C7 . NAG G 2 . ? 32.333 -81.581 -23.620 1.00 157.87 ? 501 NAG B C7 1 HETATM 6657 C C8 . NAG G 2 . ? 30.962 -81.461 -23.001 1.00 154.28 ? 501 NAG B C8 1 HETATM 6658 N N2 . NAG G 2 . ? 33.335 -81.868 -22.771 1.00 155.44 ? 501 NAG B N2 1 HETATM 6659 O O3 . NAG G 2 . ? 34.530 -84.333 -24.033 1.00 162.21 ? 501 NAG B O3 1 HETATM 6660 O O4 . NAG G 2 . ? 37.112 -84.868 -22.999 1.00 162.48 ? 501 NAG B O4 1 HETATM 6661 O O5 . NAG G 2 . ? 36.956 -81.271 -22.754 1.00 155.01 ? 501 NAG B O5 1 HETATM 6662 O O6 . NAG G 2 . ? 39.186 -82.179 -24.105 1.00 159.28 ? 501 NAG B O6 1 HETATM 6663 O O7 . NAG G 2 . ? 32.470 -81.418 -24.843 1.00 148.88 ? 501 NAG B O7 1 HETATM 6664 C C1 . NAG H 2 . ? 44.864 -45.907 -23.620 1.00 153.68 ? 502 NAG B C1 1 HETATM 6665 C C2 . NAG H 2 . ? 44.426 -44.555 -24.199 1.00 160.18 ? 502 NAG B C2 1 HETATM 6666 C C3 . NAG H 2 . ? 45.569 -43.641 -24.609 1.00 158.66 ? 502 NAG B C3 1 HETATM 6667 C C4 . NAG H 2 . ? 46.723 -43.696 -23.617 1.00 158.48 ? 502 NAG B C4 1 HETATM 6668 C C5 . NAG H 2 . ? 47.078 -45.159 -23.366 1.00 157.32 ? 502 NAG B C5 1 HETATM 6669 C C6 . NAG H 2 . ? 48.240 -45.349 -22.409 1.00 157.60 ? 502 NAG B C6 1 HETATM 6670 C C7 . NAG H 2 . ? 42.298 -44.448 -25.404 1.00 161.40 ? 502 NAG B C7 1 HETATM 6671 C C8 . NAG H 2 . ? 41.561 -44.785 -26.673 1.00 163.52 ? 502 NAG B C8 1 HETATM 6672 N N2 . NAG H 2 . ? 43.579 -44.796 -25.354 1.00 162.57 ? 502 NAG B N2 1 HETATM 6673 O O3 . NAG H 2 . ? 45.069 -42.338 -24.678 1.00 157.99 ? 502 NAG B O3 1 HETATM 6674 O O4 . NAG H 2 . ? 47.827 -42.985 -24.137 1.00 156.17 ? 502 NAG B O4 1 HETATM 6675 O O5 . NAG H 2 . ? 45.974 -45.779 -22.768 1.00 151.86 ? 502 NAG B O5 1 HETATM 6676 O O6 . NAG H 2 . ? 47.784 -45.095 -21.104 1.00 155.88 ? 502 NAG B O6 1 HETATM 6677 O O7 . NAG H 2 . ? 41.722 -43.885 -24.479 1.00 153.39 ? 502 NAG B O7 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 . ALA A 1 ? 1.3172 1.0720 1.1126 0.0425 0.0662 0.0583 1 ALA A N 2 C CA . ALA A 1 ? 1.2460 1.0102 1.0613 0.0295 0.0638 0.0489 1 ALA A CA 3 C C . ALA A 1 ? 1.2747 1.0321 1.1010 0.0240 0.0691 0.0445 1 ALA A C 4 O O . ALA A 1 ? 1.2547 0.9932 1.0770 0.0250 0.0820 0.0470 1 ALA A O 5 C CB . ALA A 1 ? 1.2094 0.9685 1.0275 0.0236 0.0707 0.0470 1 ALA A CB 6 N N . PRO A 2 ? 1.2473 1.0193 1.0868 0.0186 0.0597 0.0379 2 PRO A N 7 C CA . PRO A 2 ? 1.2379 1.0050 1.0883 0.0127 0.0634 0.0323 2 PRO A CA 8 C C . PRO A 2 ? 1.2427 1.0063 1.1066 0.0020 0.0700 0.0249 2 PRO A C 9 O O . PRO A 2 ? 1.2416 1.0188 1.1163 -0.0044 0.0631 0.0188 2 PRO A O 10 C CB . PRO A 2 ? 1.2119 0.9969 1.0697 0.0116 0.0502 0.0281 2 PRO A CB 11 C CG . PRO A 2 ? 1.1716 0.9722 1.0294 0.0117 0.0407 0.0281 2 PRO A CG 12 C CD . PRO A 2 ? 1.1764 0.9692 1.0204 0.0179 0.0455 0.0353 2 PRO A CD 13 N N . ASP A 3 ? 1.3033 1.0482 1.1665 0.0005 0.0837 0.0255 3 ASP A N 14 C CA . ASP A 3 ? 1.3246 1.0638 1.2002 -0.0089 0.0925 0.0193 3 ASP A CA 15 C C . ASP A 3 ? 1.2853 1.0373 1.1802 -0.0188 0.0858 0.0079 3 ASP A C 16 O O . ASP A 3 ? 1.2175 0.9772 1.1247 -0.0263 0.0848 0.0015 3 ASP A O 17 C CB . ASP A 3 ? 1.3607 1.0760 1.2320 -0.0082 0.1096 0.0221 3 ASP A CB 18 C CG . ASP A 3 ? 1.4142 1.1154 1.2655 0.0018 0.1176 0.0333 3 ASP A CG 19 O OD1 . ASP A 3 ? 1.5029 1.2056 1.3390 0.0122 0.1120 0.0408 3 ASP A OD1 20 O OD2 . ASP A 3 ? 1.4179 1.1067 1.2685 -0.0003 0.1294 0.0344 3 ASP A OD2 21 N N . GLN A 4 ? 1.3007 1.0549 1.1975 -0.0180 0.0812 0.0054 4 GLN A N 22 C CA . GLN A 4 ? 1.2843 1.0490 1.1970 -0.0260 0.0748 -0.0053 4 GLN A CA 23 C C . GLN A 4 ? 1.1728 0.9586 1.0917 -0.0282 0.0614 -0.0091 4 GLN A C 24 O O . GLN A 4 ? 1.1471 0.9422 1.0801 -0.0354 0.0571 -0.0184 4 GLN A O 25 C CB . GLN A 4 ? 1.3354 1.0964 1.2453 -0.0230 0.0730 -0.0059 4 GLN A CB 26 C CG . GLN A 4 ? 1.3866 1.1586 1.2873 -0.0153 0.0616 -0.0008 4 GLN A CG 27 C CD . GLN A 4 ? 1.4317 1.1946 1.3156 -0.0046 0.0652 0.0104 4 GLN A CD 28 O OE1 . GLN A 4 ? 1.3857 1.1357 1.2617 -0.0017 0.0749 0.0161 4 GLN A OE1 29 N NE2 . GLN A 4 ? 1.3969 1.1668 1.2751 0.0016 0.0574 0.0136 4 GLN A NE2 30 N N . ASP A 5 ? 1.1142 0.9074 1.0224 -0.0216 0.0548 -0.0021 5 ASP A N 31 C CA . ASP A 5 ? 1.0462 0.8575 0.9588 -0.0232 0.0435 -0.0046 5 ASP A CA 32 C C . ASP A 5 ? 1.0702 0.8838 0.9884 -0.0280 0.0465 -0.0064 5 ASP A C 33 O O . ASP A 5 ? 1.0086 0.8365 0.9322 -0.0303 0.0383 -0.0096 5 ASP A O 34 C CB . ASP A 5 ? 1.0355 0.8539 0.9358 -0.0149 0.0358 0.0027 5 ASP A CB 35 C CG . ASP A 5 ? 1.0491 0.8709 0.9472 -0.0109 0.0299 0.0030 5 ASP A CG 36 O OD1 . ASP A 5 ? 1.0616 0.8791 0.9659 -0.0141 0.0319 -0.0019 5 ASP A OD1 37 O OD2 . ASP A 5 ? 1.0440 0.8729 0.9345 -0.0045 0.0235 0.0082 5 ASP A OD2 38 N N . GLU A 6 ? 1.1539 0.9529 1.0702 -0.0290 0.0588 -0.0040 6 GLU A N 39 C CA . GLU A 6 ? 1.1439 0.9439 1.0650 -0.0332 0.0628 -0.0052 6 GLU A CA 40 C C . GLU A 6 ? 1.0914 0.9035 1.0317 -0.0421 0.0586 -0.0159 6 GLU A C 41 O O . GLU A 6 ? 1.0591 0.8708 1.0094 -0.0464 0.0588 -0.0229 6 GLU A O 42 C CB . GLU A 6 ? 1.2287 1.0090 1.1458 -0.0332 0.0787 -0.0015 6 GLU A CB 43 C CG . GLU A 6 ? 1.2750 1.0557 1.1986 -0.0381 0.0842 -0.0032 6 GLU A CG 44 C CD . GLU A 6 ? 1.3249 1.0868 1.2357 -0.0338 0.0978 0.0047 6 GLU A CD 45 O OE1 . GLU A 6 ? 1.2843 1.0288 1.1873 -0.0303 0.1080 0.0089 6 GLU A OE1 46 O OE2 . GLU A 6 ? 1.2860 1.0501 1.1938 -0.0335 0.0988 0.0069 6 GLU A OE2 47 N N . ILE A 7 ? 1.0990 0.9219 1.0435 -0.0443 0.0543 -0.0174 7 ILE A N 48 C CA . ILE A 7 ? 1.0844 0.9200 1.0466 -0.0519 0.0499 -0.0271 7 ILE A CA 49 C C . ILE A 7 ? 1.1141 0.9418 1.0870 -0.0581 0.0616 -0.0305 7 ILE A C 50 O O . ILE A 7 ? 1.1685 0.9909 1.1356 -0.0567 0.0676 -0.0253 7 ILE A O 51 C CB . ILE A 7 ? 1.0541 0.9055 1.0152 -0.0505 0.0393 -0.0267 7 ILE A CB 52 C CG1 . ILE A 7 ? 1.0590 0.9174 1.0098 -0.0444 0.0289 -0.0230 7 ILE A CG1 53 C CG2 . ILE A 7 ? 1.0532 0.9177 1.0320 -0.0572 0.0346 -0.0366 7 ILE A CG2 54 C CD1 . ILE A 7 ? 1.0785 0.9496 1.0256 -0.0423 0.0204 -0.0210 7 ILE A CD1 55 N N . GLN A 8 ? 1.1787 1.0057 1.1676 -0.0649 0.0651 -0.0395 8 GLN A N 56 C CA . GLN A 8 ? 1.2569 1.0746 1.2576 -0.0712 0.0782 -0.0432 8 GLN A CA 57 C C . GLN A 8 ? 1.2599 1.0912 1.2759 -0.0768 0.0753 -0.0496 8 GLN A C 58 O O . GLN A 8 ? 1.3869 1.2160 1.3987 -0.0758 0.0798 -0.0447 8 GLN A O 59 C CB . GLN A 8 ? 1.3016 1.1114 1.3135 -0.0764 0.0845 -0.0507 8 GLN A CB 60 C CG . GLN A 8 ? 1.3742 1.1661 1.3711 -0.0711 0.0916 -0.0434 8 GLN A CG 61 C CD . GLN A 8 ? 1.4446 1.2182 1.4287 -0.0672 0.1054 -0.0336 8 GLN A CD 62 O OE1 . GLN A 8 ? 1.4775 1.2470 1.4694 -0.0715 0.1145 -0.0348 8 GLN A OE1 63 N NE2 . GLN A 8 ? 1.4785 1.2412 1.4428 -0.0585 0.1070 -0.0236 8 GLN A NE2 64 N N . ARG A 9 ? 1.2205 1.0656 1.2537 -0.0822 0.0681 -0.0606 9 ARG A N 65 C CA . ARG A 9 ? 1.2378 1.0973 1.2867 -0.0869 0.0646 -0.0673 9 ARG A CA 66 C C . ARG A 9 ? 1.2107 1.0884 1.2588 -0.0841 0.0486 -0.0701 9 ARG A C 67 O O . ARG A 9 ? 1.2043 1.0882 1.2567 -0.0845 0.0411 -0.0764 9 ARG A O 68 C CB . ARG A 9 ? 1.2661 1.1268 1.3386 -0.0958 0.0707 -0.0792 9 ARG A CB 69 C CG . ARG A 9 ? 1.3198 1.1614 1.3954 -0.0994 0.0886 -0.0773 9 ARG A CG 70 C CD . ARG A 9 ? 1.4133 1.2503 1.4866 -0.0992 0.0972 -0.0712 9 ARG A CD 71 N NE . ARG A 9 ? 1.4132 1.2605 1.5093 -0.1064 0.0997 -0.0801 9 ARG A NE 72 C CZ . ARG A 9 ? 1.3978 1.2353 1.5073 -0.1125 0.1148 -0.0831 9 ARG A CZ 73 N NH1 . ARG A 9 ? 1.3942 1.2098 1.4962 -0.1123 0.1297 -0.0779 9 ARG A NH1 74 N NH2 . ARG A 9 ? 1.3560 1.2057 1.4874 -0.1187 0.1155 -0.0916 9 ARG A NH2 75 N N . LEU A 10 ? 1.1303 1.0157 1.1724 -0.0811 0.0438 -0.0654 10 LEU A N 76 C CA . LEU A 10 ? 1.0786 0.9795 1.1178 -0.0776 0.0299 -0.0666 10 LEU A CA 77 C C . LEU A 10 ? 1.0199 0.9366 1.0774 -0.0819 0.0250 -0.0760 10 LEU A C 78 O O . LEU A 10 ? 1.0641 0.9830 1.1271 -0.0840 0.0292 -0.0753 10 LEU A O 79 C CB . LEU A 10 ? 1.0420 0.9420 1.0634 -0.0714 0.0273 -0.0562 10 LEU A CB 80 C CG . LEU A 10 ? 0.9808 0.8918 0.9938 -0.0664 0.0145 -0.0547 10 LEU A CG 81 C CD1 . LEU A 10 ? 0.9805 0.8876 0.9866 -0.0634 0.0110 -0.0542 10 LEU A CD1 82 C CD2 . LEU A 10 ? 0.9610 0.8715 0.9597 -0.0618 0.0135 -0.0459 10 LEU A CD2 83 N N . PRO A 11 ? 0.9581 0.8858 1.0245 -0.0828 0.0160 -0.0848 11 PRO A N 84 C CA . PRO A 11 ? 0.9465 0.8903 1.0299 -0.0857 0.0102 -0.0942 11 PRO A CA 85 C C . PRO A 11 ? 0.9686 0.9217 1.0482 -0.0826 0.0056 -0.0901 11 PRO A C 86 O O . PRO A 11 ? 1.0113 0.9654 1.0753 -0.0769 -0.0002 -0.0833 11 PRO A O 87 C CB . PRO A 11 ? 0.9044 0.8569 0.9888 -0.0836 -0.0008 -0.1011 11 PRO A CB 88 C CG . PRO A 11 ? 0.9304 0.8695 1.0068 -0.0833 0.0032 -0.0989 11 PRO A CG 89 C CD . PRO A 11 ? 0.9431 0.8683 1.0040 -0.0807 0.0111 -0.0867 11 PRO A CD 90 N N . GLY A 12 ? 1.0209 0.9810 1.1154 -0.0865 0.0087 -0.0946 12 GLY A N 91 C CA . GLY A 12 ? 1.0245 0.9939 1.1170 -0.0838 0.0047 -0.0917 12 GLY A CA 92 C C . GLY A 12 ? 1.0591 1.0190 1.1463 -0.0847 0.0149 -0.0839 12 GLY A C 93 O O . GLY A 12 ? 1.0676 1.0336 1.1536 -0.0831 0.0133 -0.0815 12 GLY A O 94 N N . LEU A 13 ? 1.0945 1.0388 1.1777 -0.0868 0.0257 -0.0799 13 LEU A N 95 C CA . LEU A 13 ? 1.1052 1.0387 1.1841 -0.0878 0.0370 -0.0735 13 LEU A CA 96 C C . LEU A 13 ? 1.1325 1.0651 1.2326 -0.0949 0.0473 -0.0804 13 LEU A C 97 O O . LEU A 13 ? 1.1689 1.0982 1.2807 -0.0994 0.0516 -0.0867 13 LEU A O 98 C CB . LEU A 13 ? 1.1189 1.0345 1.1792 -0.0847 0.0438 -0.0643 13 LEU A CB 99 C CG . LEU A 13 ? 1.1185 1.0335 1.1572 -0.0775 0.0360 -0.0559 13 LEU A CG 100 C CD1 . LEU A 13 ? 1.1303 1.0281 1.1527 -0.0742 0.0432 -0.0476 13 LEU A CD1 101 C CD2 . LEU A 13 ? 1.1295 1.0502 1.1621 -0.0750 0.0334 -0.0518 13 LEU A CD2 102 N N . ALA A 14 ? 1.1640 1.0997 1.2697 -0.0961 0.0517 -0.0796 14 ALA A N 103 C CA . ALA A 14 ? 1.1943 1.1269 1.3189 -0.1027 0.0638 -0.0846 14 ALA A CA 104 C C . ALA A 14 ? 1.2179 1.1287 1.3340 -0.1038 0.0785 -0.0785 14 ALA A C 105 O O . ALA A 14 ? 1.2403 1.1452 1.3702 -0.1093 0.0868 -0.0842 14 ALA A O 106 C CB . ALA A 14 ? 1.2035 1.1425 1.3329 -0.1028 0.0659 -0.0835 14 ALA A CB 107 N N . LYS A 15 ? 1.2603 1.1589 1.3533 -0.0982 0.0818 -0.0671 15 LYS A N 108 C CA . LYS A 15 ? 1.2947 1.1714 1.3757 -0.0974 0.0956 -0.0599 15 LYS A CA 109 C C . LYS A 15 ? 1.2284 1.0973 1.2857 -0.0904 0.0902 -0.0519 15 LYS A C 110 O O . LYS A 15 ? 1.1949 1.0713 1.2392 -0.0852 0.0793 -0.0478 15 LYS A O 111 C CB . LYS A 15 ? 1.3804 1.2471 1.4548 -0.0963 0.1068 -0.0534 15 LYS A CB 112 C CG . LYS A 15 ? 1.4322 1.2970 1.4819 -0.0886 0.1011 -0.0436 15 LYS A CG 113 C CD . LYS A 15 ? 1.4828 1.3446 1.5303 -0.0884 0.1083 -0.0401 15 LYS A CD 114 C CE . LYS A 15 ? 1.4976 1.3617 1.5234 -0.0814 0.0997 -0.0328 15 LYS A CE 115 N NZ . LYS A 15 ? 1.5678 1.4339 1.5947 -0.0817 0.1036 -0.0316 15 LYS A NZ 116 N N . GLN A 16 ? 1.2524 1.1059 1.3047 -0.0904 0.0986 -0.0497 16 GLN A N 117 C CA . GLN A 16 ? 1.1796 1.0258 1.2115 -0.0838 0.0940 -0.0428 16 GLN A CA 118 C C . GLN A 16 ? 1.0849 0.9228 1.0925 -0.0762 0.0948 -0.0314 16 GLN A C 119 O O . GLN A 16 ? 1.0685 0.8988 1.0730 -0.0761 0.1040 -0.0279 16 GLN A O 120 C CB . GLN A 16 ? 1.2256 1.0563 1.2588 -0.0855 0.1041 -0.0433 16 GLN A CB 121 C CG . GLN A 16 ? 1.2572 1.0974 1.3108 -0.0919 0.0997 -0.0548 16 GLN A CG 122 C CD . GLN A 16 ? 1.2936 1.1489 1.3435 -0.0887 0.0825 -0.0570 16 GLN A CD 123 O OE1 . GLN A 16 ? 1.2382 1.0891 1.2696 -0.0822 0.0777 -0.0499 16 GLN A OE1 124 N NE2 . GLN A 16 ? 1.3031 1.1762 1.3703 -0.0928 0.0735 -0.0668 16 GLN A NE2 125 N N . PRO A 17 ? 1.0530 0.8931 1.0439 -0.0696 0.0849 -0.0263 17 PRO A N 126 C CA . PRO A 17 ? 1.0300 0.8643 0.9978 -0.0618 0.0834 -0.0165 17 PRO A CA 127 C C . PRO A 17 ? 1.0139 0.8268 0.9670 -0.0578 0.0971 -0.0087 17 PRO A C 128 O O . PRO A 17 ? 1.0390 0.8401 0.9942 -0.0589 0.1055 -0.0089 17 PRO A O 129 C CB . PRO A 17 ? 1.0173 0.8578 0.9751 -0.0569 0.0713 -0.0146 17 PRO A CB 130 C CG . PRO A 17 ? 1.0209 0.8749 0.9966 -0.0620 0.0637 -0.0236 17 PRO A CG 131 C CD . PRO A 17 ? 1.0523 0.9013 1.0461 -0.0693 0.0741 -0.0302 17 PRO A CD 132 N N . SER A 18 ? 1.0081 0.8155 0.9450 -0.0527 0.0993 -0.0019 18 SER A N 133 C CA . SER A 18 ? 1.0414 0.8280 0.9596 -0.0466 0.1113 0.0066 18 SER A CA 134 C C . SER A 18 ? 1.0629 0.8448 0.9612 -0.0378 0.1056 0.0133 18 SER A C 135 O O . SER A 18 ? 1.1070 0.8714 0.9884 -0.0314 0.1146 0.0206 18 SER A O 136 C CB . SER A 18 ? 1.0487 0.8313 0.9560 -0.0438 0.1154 0.0111 18 SER A CB 137 O OG . SER A 18 ? 1.0208 0.8137 0.9146 -0.0384 0.1025 0.0140 18 SER A OG 138 N N . PHE A 19 ? 1.0311 0.8284 0.9315 -0.0371 0.0911 0.0108 19 PHE A N 139 C CA . PHE A 19 ? 1.0198 0.8161 0.9030 -0.0287 0.0840 0.0165 19 PHE A CA 140 C C . PHE A 19 ? 1.0562 0.8557 0.9486 -0.0307 0.0803 0.0128 19 PHE A C 141 O O . PHE A 19 ? 1.0836 0.8926 0.9951 -0.0383 0.0776 0.0048 19 PHE A O 142 C CB . PHE A 19 ? 0.9892 0.8006 0.8654 -0.0255 0.0703 0.0172 19 PHE A CB 143 C CG . PHE A 19 ? 0.9843 0.8145 0.8781 -0.0321 0.0603 0.0094 19 PHE A CG 144 C CD1 . PHE A 19 ? 0.9782 0.8189 0.8789 -0.0330 0.0509 0.0059 19 PHE A CD1 145 C CD2 . PHE A 19 ? 1.0008 0.8376 0.9035 -0.0370 0.0609 0.0058 19 PHE A CD2 146 C CE1 . PHE A 19 ? 0.9270 0.7838 0.8419 -0.0380 0.0422 -0.0007 19 PHE A CE1 147 C CE2 . PHE A 19 ? 0.9909 0.8444 0.9086 -0.0420 0.0520 -0.0009 19 PHE A CE2 148 C CZ . PHE A 19 ? 0.9535 0.8167 0.8768 -0.0423 0.0427 -0.0041 19 PHE A CZ 149 N N . ARG A 20 ? 1.0885 0.8799 0.9670 -0.0236 0.0803 0.0185 20 ARG A N 150 C CA . ARG A 20 ? 1.1046 0.8992 0.9896 -0.0245 0.0760 0.0156 20 ARG A CA 151 C C . ARG A 20 ? 1.0469 0.8611 0.9355 -0.0243 0.0600 0.0125 20 ARG A C 152 O O . ARG A 20 ? 1.0187 0.8413 0.8989 -0.0205 0.0523 0.0151 20 ARG A O 153 C CB . ARG A 20 ? 1.1908 0.9700 1.0599 -0.0164 0.0818 0.0229 20 ARG A CB 154 C CG . ARG A 20 ? 1.3003 1.0575 1.1648 -0.0159 0.0991 0.0265 20 ARG A CG 155 C CD . ARG A 20 ? 1.3815 1.1240 1.2343 -0.0090 0.1049 0.0321 20 ARG A CD 156 N NE . ARG A 20 ? 1.5012 1.2218 1.3378 -0.0028 0.1194 0.0399 20 ARG A NE 157 C CZ . ARG A 20 ? 1.5870 1.3026 1.4022 0.0070 0.1187 0.0481 20 ARG A CZ 158 N NH1 . ARG A 20 ? 1.5441 1.2757 1.3527 0.0113 0.1042 0.0490 20 ARG A NH1 159 N NH2 . ARG A 20 ? 1.6166 1.3108 1.4168 0.0130 0.1331 0.0551 20 ARG A NH2 160 N N . GLN A 21 ? 1.0071 0.8279 0.9083 -0.0285 0.0557 0.0066 21 GLN A N 161 C CA . GLN A 21 ? 0.9567 0.7935 0.8612 -0.0280 0.0424 0.0038 21 GLN A CA 162 C C . GLN A 21 ? 0.9741 0.8093 0.8835 -0.0285 0.0413 0.0011 21 GLN A C 163 O O . GLN A 21 ? 0.9877 0.8156 0.9068 -0.0334 0.0486 -0.0031 21 GLN A O 164 C CB . GLN A 21 ? 0.9434 0.7949 0.8617 -0.0343 0.0362 -0.0030 21 GLN A CB 165 C CG . GLN A 21 ? 0.9380 0.7882 0.8733 -0.0424 0.0426 -0.0103 21 GLN A CG 166 C CD . GLN A 21 ? 0.9460 0.8123 0.8943 -0.0473 0.0350 -0.0171 21 GLN A CD 167 O OE1 . GLN A 21 ? 0.9609 0.8379 0.9048 -0.0448 0.0261 -0.0159 21 GLN A OE1 168 N NE2 . GLN A 21 ? 0.9821 0.8505 0.9472 -0.0541 0.0387 -0.0245 21 GLN A NE2 169 N N . TYR A 22 ? 1.0007 0.8430 0.9042 -0.0236 0.0324 0.0032 22 TYR A N 170 C CA . TYR A 22 ? 1.0143 0.8546 0.9196 -0.0226 0.0310 0.0018 22 TYR A CA 171 C C . TYR A 22 ? 0.9700 0.8262 0.8823 -0.0240 0.0193 -0.0028 22 TYR A C 172 O O . TYR A 22 ? 0.9572 0.8244 0.8674 -0.0226 0.0119 -0.0020 22 TYR A O 173 C CB . TYR A 22 ? 1.0209 0.8526 0.9106 -0.0137 0.0327 0.0101 22 TYR A CB 174 C CG . TYR A 22 ? 1.0400 0.8538 0.9199 -0.0107 0.0451 0.0158 22 TYR A CG 175 C CD1 . TYR A 22 ? 1.0252 0.8363 0.8962 -0.0081 0.0478 0.0201 22 TYR A CD1 176 C CD2 . TYR A 22 ? 1.0587 0.8571 0.9373 -0.0100 0.0547 0.0169 22 TYR A CD2 177 C CE1 . TYR A 22 ? 1.0415 0.8349 0.9019 -0.0045 0.0598 0.0257 22 TYR A CE1 178 C CE2 . TYR A 22 ? 1.0990 0.8796 0.9678 -0.0067 0.0671 0.0225 22 TYR A CE2 179 C CZ . TYR A 22 ? 1.0831 0.8611 0.9425 -0.0037 0.0697 0.0271 22 TYR A CZ 180 O OH . TYR A 22 ? 1.1262 0.8851 0.9745 0.0002 0.0828 0.0330 22 TYR A OH 181 N N . SER A 23 ? 0.9633 0.8196 0.8831 -0.0265 0.0183 -0.0079 23 SER A N 182 C CA . SER A 23 ? 0.9332 0.8022 0.8573 -0.0265 0.0081 -0.0116 23 SER A CA 183 C C . SER A 23 ? 0.9143 0.7781 0.8368 -0.0241 0.0081 -0.0120 23 SER A C 184 O O . SER A 23 ? 0.9346 0.7900 0.8625 -0.0276 0.0139 -0.0159 23 SER A O 185 C CB . SER A 23 ? 0.9140 0.7922 0.8514 -0.0330 0.0047 -0.0201 23 SER A CB 186 O OG . SER A 23 ? 0.8914 0.7786 0.8316 -0.0323 -0.0035 -0.0239 23 SER A OG 187 N N . GLY A 24 ? 0.9073 0.7764 0.8233 -0.0186 0.0019 -0.0084 24 GLY A N 188 C CA . GLY A 24 ? 0.9009 0.7654 0.8145 -0.0154 0.0018 -0.0079 24 GLY A CA 189 C C . GLY A 24 ? 0.8772 0.7509 0.7864 -0.0101 -0.0059 -0.0049 24 GLY A C 190 O O . GLY A 24 ? 0.8588 0.7441 0.7703 -0.0108 -0.0124 -0.0062 24 GLY A O 191 N N . TYR A 25 ? 0.8850 0.7531 0.7879 -0.0046 -0.0045 -0.0007 25 TYR A N 192 C CA . TYR A 25 ? 0.8443 0.7206 0.7453 0.0000 -0.0110 0.0012 25 TYR A CA 193 C C . TYR A 25 ? 0.8473 0.7224 0.7396 0.0077 -0.0107 0.0089 25 TYR A C 194 O O . TYR A 25 ? 0.8453 0.7092 0.7316 0.0113 -0.0046 0.0129 25 TYR A O 195 C CB . TYR A 25 ? 0.8486 0.7220 0.7525 -0.0005 -0.0113 -0.0028 25 TYR A CB 196 C CG . TYR A 25 ? 0.8534 0.7335 0.7651 -0.0060 -0.0155 -0.0104 25 TYR A CG 197 C CD1 . TYR A 25 ? 0.8542 0.7304 0.7720 -0.0120 -0.0123 -0.0163 25 TYR A CD1 198 C CD2 . TYR A 25 ? 0.8900 0.7810 0.8033 -0.0049 -0.0225 -0.0119 25 TYR A CD2 199 C CE1 . TYR A 25 ? 0.8709 0.7548 0.7960 -0.0163 -0.0171 -0.0237 25 TYR A CE1 200 C CE2 . TYR A 25 ? 0.8818 0.7788 0.8007 -0.0087 -0.0264 -0.0186 25 TYR A CE2 201 C CZ . TYR A 25 ? 0.8535 0.7475 0.7782 -0.0142 -0.0242 -0.0245 25 TYR A CZ 202 O OH . TYR A 25 ? 0.8533 0.7543 0.7836 -0.0171 -0.0288 -0.0313 25 TYR A OH 203 N N . LEU A 26 ? 0.8767 0.7638 0.7690 0.0104 -0.0174 0.0105 26 LEU A N 204 C CA . LEU A 26 ? 0.8919 0.7816 0.7781 0.0179 -0.0191 0.0165 26 LEU A CA 205 C C . LEU A 26 ? 0.9110 0.8059 0.8001 0.0211 -0.0226 0.0164 26 LEU A C 206 O O . LEU A 26 ? 0.9026 0.8045 0.7980 0.0178 -0.0264 0.0121 26 LEU A O 207 C CB . LEU A 26 ? 0.9165 0.8167 0.8017 0.0186 -0.0242 0.0176 26 LEU A CB 208 C CG . LEU A 26 ? 0.9339 0.8307 0.8168 0.0149 -0.0215 0.0172 26 LEU A CG 209 C CD1 . LEU A 26 ? 0.9132 0.8208 0.7944 0.0163 -0.0271 0.0181 26 LEU A CD1 210 C CD2 . LEU A 26 ? 0.9469 0.8292 0.8213 0.0179 -0.0135 0.0215 26 LEU A CD2 211 N N . LYS A 27 ? 0.9793 0.8704 0.8636 0.0279 -0.0209 0.0213 27 LYS A N 212 C CA . LYS A 27 ? 1.0679 0.9636 0.9552 0.0316 -0.0233 0.0218 27 LYS A CA 213 C C . LYS A 27 ? 1.0689 0.9800 0.9603 0.0335 -0.0302 0.0220 27 LYS A C 214 O O . LYS A 27 ? 1.2431 1.1589 1.1313 0.0369 -0.0324 0.0249 27 LYS A O 215 C CB . LYS A 27 ? 1.0702 0.9570 0.9513 0.0389 -0.0188 0.0271 27 LYS A CB 216 C CG . LYS A 27 ? 1.1015 0.9727 0.9800 0.0370 -0.0114 0.0261 27 LYS A CG 217 C CD . LYS A 27 ? 1.1437 1.0085 1.0191 0.0436 -0.0081 0.0298 27 LYS A CD 218 C CE . LYS A 27 ? 1.1582 1.0181 1.0250 0.0520 -0.0051 0.0371 27 LYS A CE 219 N NZ . LYS A 27 ? 1.1364 0.9811 0.9960 0.0508 0.0027 0.0387 27 LYS A NZ 220 N N . GLY A 28 ? 1.0473 0.9655 0.9456 0.0316 -0.0333 0.0187 28 GLY A N 221 C CA . GLY A 28 ? 1.0656 0.9977 0.9694 0.0334 -0.0386 0.0187 28 GLY A CA 222 C C . GLY A 28 ? 1.0790 1.0130 0.9853 0.0393 -0.0383 0.0211 28 GLY A C 223 O O . GLY A 28 ? 1.2253 1.1512 1.1268 0.0440 -0.0348 0.0247 28 GLY A O 224 N N . SER A 29 ? 0.9857 0.9301 0.8999 0.0392 -0.0414 0.0192 29 SER A N 225 C CA . SER A 29 ? 1.0055 0.9519 0.9237 0.0441 -0.0404 0.0209 29 SER A CA 226 C C . SER A 29 ? 1.0313 0.9664 0.9472 0.0429 -0.0358 0.0197 29 SER A C 227 O O . SER A 29 ? 0.9972 0.9261 0.9104 0.0378 -0.0348 0.0164 29 SER A O 228 C CB . SER A 29 ? 0.9846 0.9451 0.9131 0.0439 -0.0439 0.0188 29 SER A CB 229 O OG . SER A 29 ? 0.9943 0.9532 0.9263 0.0406 -0.0420 0.0158 29 SER A OG 230 N N . GLY A 30 ? 1.0938 1.0267 1.0108 0.0480 -0.0333 0.0219 30 GLY A N 231 C CA . GLY A 30 ? 1.1075 1.0300 1.0220 0.0476 -0.0291 0.0206 30 GLY A CA 232 C C . GLY A 30 ? 1.0650 0.9749 0.9721 0.0439 -0.0264 0.0187 30 GLY A C 233 O O . GLY A 30 ? 1.0589 0.9633 0.9612 0.0448 -0.0248 0.0212 30 GLY A O 234 N N . SER A 31 ? 1.0464 0.9516 0.9526 0.0399 -0.0258 0.0142 31 SER A N 235 C CA . SER A 31 ? 1.0305 0.9248 0.9317 0.0358 -0.0235 0.0109 31 SER A CA 236 C C . SER A 31 ? 1.0122 0.9111 0.9152 0.0296 -0.0268 0.0066 31 SER A C 237 O O . SER A 31 ? 1.0622 0.9558 0.9638 0.0256 -0.0265 0.0017 31 SER A O 238 C CB . SER A 31 ? 1.0119 0.8973 0.9102 0.0364 -0.0208 0.0079 31 SER A CB 239 O OG . SER A 31 ? 0.9974 0.8879 0.8976 0.0351 -0.0234 0.0044 31 SER A OG 240 N N . LYS A 32 ? 0.9550 0.8638 0.8611 0.0289 -0.0302 0.0082 32 LYS A N 241 C CA . LYS A 32 ? 0.9447 0.8584 0.8527 0.0234 -0.0331 0.0047 32 LYS A CA 242 C C . LYS A 32 ? 0.9630 0.8720 0.8684 0.0207 -0.0315 0.0052 32 LYS A C 243 O O . LYS A 32 ? 1.0838 0.9908 0.9862 0.0240 -0.0297 0.0097 32 LYS A O 244 C CB . LYS A 32 ? 0.9004 0.8268 0.8133 0.0236 -0.0371 0.0054 32 LYS A CB 245 C CG . LYS A 32 ? 0.8901 0.8213 0.8067 0.0263 -0.0375 0.0054 32 LYS A CG 246 C CD . LYS A 32 ? 0.8937 0.8373 0.8165 0.0264 -0.0406 0.0062 32 LYS A CD 247 C CE . LYS A 32 ? 0.9231 0.8716 0.8514 0.0287 -0.0399 0.0061 32 LYS A CE 248 N NZ . LYS A 32 ? 0.9754 0.9234 0.9054 0.0343 -0.0379 0.0096 32 LYS A NZ 249 N N . HIS A 33 ? 0.9283 0.8356 0.8346 0.0152 -0.0318 0.0006 33 HIS A N 250 C CA . HIS A 33 ? 0.8954 0.7973 0.8003 0.0121 -0.0290 0.0004 33 HIS A CA 251 C C . HIS A 33 ? 0.8853 0.7942 0.7937 0.0072 -0.0320 -0.0026 33 HIS A C 252 O O . HIS A 33 ? 0.8531 0.7637 0.7647 0.0037 -0.0338 -0.0079 33 HIS A O 253 C CB . HIS A 33 ? 0.9448 0.8352 0.8489 0.0097 -0.0247 -0.0029 33 HIS A CB 254 C CG . HIS A 33 ? 0.9904 0.8714 0.8901 0.0143 -0.0201 0.0005 33 HIS A CG 255 N ND1 . HIS A 33 ? 1.0619 0.9399 0.9608 0.0167 -0.0200 -0.0008 33 HIS A ND1 256 C CD2 . HIS A 33 ? 1.0032 0.8764 0.8983 0.0176 -0.0152 0.0056 33 HIS A CD2 257 C CE1 . HIS A 33 ? 1.0613 0.9304 0.9561 0.0209 -0.0152 0.0031 33 HIS A CE1 258 N NE2 . HIS A 33 ? 1.0291 0.8950 0.9213 0.0217 -0.0122 0.0072 33 HIS A NE2 259 N N . LEU A 34 ? 0.9290 0.8419 0.8363 0.0075 -0.0326 0.0004 34 LEU A N 260 C CA . LEU A 34 ? 0.9241 0.8442 0.8343 0.0035 -0.0354 -0.0018 34 LEU A CA 261 C C . LEU A 34 ? 0.9335 0.8474 0.8437 -0.0006 -0.0317 -0.0033 34 LEU A C 262 O O . LEU A 34 ? 0.9716 0.8783 0.8774 0.0009 -0.0275 0.0002 34 LEU A O 263 C CB . LEU A 34 ? 0.9338 0.8621 0.8427 0.0061 -0.0384 0.0019 34 LEU A CB 264 C CG . LEU A 34 ? 0.9314 0.8666 0.8417 0.0105 -0.0414 0.0038 34 LEU A CG 265 C CD1 . LEU A 34 ? 0.9147 0.8591 0.8253 0.0118 -0.0448 0.0056 34 LEU A CD1 266 C CD2 . LEU A 34 ? 0.9768 0.9157 0.8916 0.0091 -0.0432 0.0001 34 LEU A CD2 267 N N . HIS A 35 ? 0.9111 0.8280 0.8264 -0.0055 -0.0330 -0.0086 35 HIS A N 268 C CA . HIS A 35 ? 0.8908 0.8032 0.8084 -0.0100 -0.0293 -0.0108 35 HIS A CA 269 C C . HIS A 35 ? 0.8685 0.7841 0.7837 -0.0103 -0.0292 -0.0076 35 HIS A C 270 O O . HIS A 35 ? 0.9098 0.8345 0.8256 -0.0099 -0.0337 -0.0074 35 HIS A O 271 C CB . HIS A 35 ? 0.8812 0.7973 0.8059 -0.0147 -0.0314 -0.0179 35 HIS A CB 272 C CG . HIS A 35 ? 0.8581 0.7714 0.7876 -0.0198 -0.0277 -0.0209 35 HIS A CG 273 N ND1 . HIS A 35 ? 0.8233 0.7439 0.7589 -0.0235 -0.0303 -0.0252 35 HIS A ND1 274 C CD2 . HIS A 35 ? 0.8321 0.7358 0.7616 -0.0216 -0.0208 -0.0200 35 HIS A CD2 275 C CE1 . HIS A 35 ? 0.8145 0.7309 0.7546 -0.0276 -0.0254 -0.0272 35 HIS A CE1 276 N NE2 . HIS A 35 ? 0.8158 0.7214 0.7522 -0.0267 -0.0192 -0.0240 35 HIS A NE2 277 N N . TYR A 36 ? 0.8593 0.7665 0.7714 -0.0107 -0.0235 -0.0052 36 TYR A N 278 C CA . TYR A 36 ? 0.8392 0.7475 0.7475 -0.0106 -0.0225 -0.0022 36 TYR A CA 279 C C . TYR A 36 ? 0.8435 0.7465 0.7558 -0.0158 -0.0171 -0.0050 36 TYR A C 280 O O . TYR A 36 ? 0.8679 0.7642 0.7850 -0.0188 -0.0127 -0.0082 36 TYR A O 281 C CB . TYR A 36 ? 0.8630 0.7653 0.7612 -0.0044 -0.0200 0.0045 36 TYR A CB 282 C CG . TYR A 36 ? 0.8752 0.7629 0.7695 -0.0037 -0.0114 0.0068 36 TYR A CG 283 C CD1 . TYR A 36 ? 0.8950 0.7754 0.7881 -0.0013 -0.0087 0.0077 36 TYR A CD1 284 C CD2 . TYR A 36 ? 0.8813 0.7614 0.7725 -0.0053 -0.0052 0.0082 36 TYR A CD2 285 C CE1 . TYR A 36 ? 0.8893 0.7552 0.7788 -0.0007 0.0000 0.0097 36 TYR A CE1 286 C CE2 . TYR A 36 ? 0.9127 0.7782 0.8003 -0.0046 0.0039 0.0104 36 TYR A CE2 287 C CZ . TYR A 36 ? 0.9440 0.8023 0.8309 -0.0024 0.0066 0.0111 36 TYR A CZ 288 O OH . TYR A 36 ? 0.9953 0.8376 0.8785 -0.0018 0.0168 0.0132 36 TYR A OH 289 N N . TRP A 37 ? 0.8344 0.7407 0.7455 -0.0170 -0.0172 -0.0041 37 TRP A N 290 C CA . TRP A 37 ? 0.8244 0.7257 0.7389 -0.0215 -0.0112 -0.0058 37 TRP A CA 291 C C . TRP A 37 ? 0.8650 0.7633 0.7698 -0.0185 -0.0089 -0.0004 37 TRP A C 292 O O . TRP A 37 ? 0.8809 0.7875 0.7833 -0.0176 -0.0140 0.0002 37 TRP A O 293 C CB . TRP A 37 ? 0.7926 0.7032 0.7173 -0.0267 -0.0148 -0.0120 37 TRP A CB 294 C CG . TRP A 37 ? 0.7901 0.6972 0.7218 -0.0318 -0.0089 -0.0152 37 TRP A CG 295 C CD1 . TRP A 37 ? 0.8307 0.7277 0.7588 -0.0322 -0.0007 -0.0121 37 TRP A CD1 296 C CD2 . TRP A 37 ? 0.7639 0.6778 0.7079 -0.0370 -0.0106 -0.0223 37 TRP A CD2 297 N NE1 . TRP A 37 ? 0.8298 0.7270 0.7685 -0.0380 0.0033 -0.0170 37 TRP A NE1 298 C CE2 . TRP A 37 ? 0.7907 0.6990 0.7397 -0.0409 -0.0030 -0.0235 37 TRP A CE2 299 C CE3 . TRP A 37 ? 0.7497 0.6738 0.7005 -0.0380 -0.0175 -0.0277 37 TRP A CE3 300 C CZ2 . TRP A 37 ? 0.7777 0.6917 0.7401 -0.0463 -0.0027 -0.0304 37 TRP A CZ2 301 C CZ3 . TRP A 37 ? 0.7585 0.6879 0.7209 -0.0426 -0.0177 -0.0343 37 TRP A CZ3 302 C CH2 . TRP A 37 ? 0.7632 0.6883 0.7321 -0.0468 -0.0106 -0.0359 37 TRP A CH2 303 N N . PHE A 38 ? 0.8977 0.7832 0.7960 -0.0166 -0.0009 0.0034 38 PHE A N 304 C CA . PHE A 38 ? 0.8902 0.7704 0.7760 -0.0117 0.0016 0.0094 38 PHE A CA 305 C C . PHE A 38 ? 0.9080 0.7808 0.7951 -0.0156 0.0096 0.0088 38 PHE A C 306 O O . PHE A 38 ? 0.8977 0.7606 0.7894 -0.0186 0.0178 0.0075 38 PHE A O 307 C CB . PHE A 38 ? 0.9171 0.7865 0.7927 -0.0053 0.0057 0.0150 38 PHE A CB 308 C CG . PHE A 38 ? 0.9192 0.7832 0.7796 0.0017 0.0073 0.0215 38 PHE A CG 309 C CD1 . PHE A 38 ? 0.9242 0.7988 0.7788 0.0060 -0.0010 0.0231 38 PHE A CD1 310 C CD2 . PHE A 38 ? 0.9298 0.7778 0.7813 0.0045 0.0176 0.0260 38 PHE A CD2 311 C CE1 . PHE A 38 ? 0.9245 0.7947 0.7643 0.0132 -0.0004 0.0285 38 PHE A CE1 312 C CE2 . PHE A 38 ? 0.9353 0.7776 0.7708 0.0122 0.0190 0.0322 38 PHE A CE2 313 C CZ . PHE A 38 ? 0.9377 0.7916 0.7671 0.0167 0.0094 0.0332 38 PHE A CZ 314 N N . VAL A 39 ? 0.9367 0.8142 0.8207 -0.0159 0.0078 0.0094 39 VAL A N 315 C CA . VAL A 39 ? 0.9989 0.8690 0.8833 -0.0190 0.0161 0.0093 39 VAL A CA 316 C C . VAL A 39 ? 1.0427 0.9036 0.9101 -0.0127 0.0202 0.0161 39 VAL A C 317 O O . VAL A 39 ? 1.0131 0.8809 0.8726 -0.0091 0.0137 0.0178 39 VAL A O 318 C CB . VAL A 39 ? 0.9842 0.8651 0.8794 -0.0250 0.0127 0.0040 39 VAL A CB 319 C CG1 . VAL A 39 ? 0.9779 0.8635 0.8897 -0.0313 0.0124 -0.0028 39 VAL A CG1 320 C CG2 . VAL A 39 ? 0.9604 0.8542 0.8525 -0.0229 0.0025 0.0039 39 VAL A CG2 321 N N . GLU A 40 ? 1.0651 0.9100 0.9266 -0.0110 0.0311 0.0197 40 GLU A N 322 C CA . GLU A 40 ? 1.1432 0.9771 0.9862 -0.0035 0.0358 0.0267 40 GLU A CA 323 C C . GLU A 40 ? 1.0805 0.9165 0.9198 -0.0047 0.0362 0.0265 40 GLU A C 324 O O . GLU A 40 ? 1.1049 0.9446 0.9567 -0.0119 0.0384 0.0219 40 GLU A O 325 C CB . GLU A 40 ? 1.2451 1.0594 1.0827 -0.0016 0.0494 0.0306 40 GLU A CB 326 C CG . GLU A 40 ? 1.3067 1.1158 1.1432 0.0016 0.0500 0.0324 40 GLU A CG 327 C CD . GLU A 40 ? 1.3627 1.1505 1.1872 0.0068 0.0633 0.0385 40 GLU A CD 328 O OE1 . GLU A 40 ? 1.3652 1.1411 1.1869 0.0054 0.0741 0.0400 40 GLU A OE1 329 O OE2 . GLU A 40 ? 1.3599 1.1424 1.1778 0.0126 0.0635 0.0421 40 GLU A OE2 330 N N . SER A 41 ? 1.0892 0.9233 0.9113 0.0027 0.0337 0.0313 41 SER A N 331 C CA . SER A 41 ? 1.1089 0.9430 0.9250 0.0024 0.0348 0.0315 41 SER A CA 332 C C . SER A 41 ? 1.1239 0.9447 0.9433 -0.0016 0.0483 0.0319 41 SER A C 333 O O . SER A 41 ? 1.1588 0.9639 0.9727 0.0009 0.0586 0.0357 41 SER A O 334 C CB . SER A 41 ? 1.1046 0.9343 0.8988 0.0124 0.0324 0.0371 41 SER A CB 335 O OG . SER A 41 ? 1.0823 0.9070 0.8683 0.0126 0.0367 0.0380 41 SER A OG 336 N N . GLN A 42 ? 1.0822 0.9086 0.9107 -0.0078 0.0489 0.0279 42 GLN A N 337 C CA . GLN A 42 ? 1.1153 0.9301 0.9483 -0.0119 0.0620 0.0279 42 GLN A CA 338 C C . GLN A 42 ? 1.1538 0.9516 0.9655 -0.0044 0.0710 0.0349 42 GLN A C 339 O O . GLN A 42 ? 1.0896 0.8734 0.9017 -0.0061 0.0843 0.0365 42 GLN A O 340 C CB . GLN A 42 ? 1.0646 0.8904 0.9116 -0.0192 0.0599 0.0222 42 GLN A CB 341 C CG . GLN A 42 ? 1.0459 0.8876 0.9134 -0.0260 0.0519 0.0151 42 GLN A CG 342 C CD . GLN A 42 ? 1.0542 0.9031 0.9372 -0.0332 0.0536 0.0097 42 GLN A CD 343 O OE1 . GLN A 42 ? 1.0270 0.8669 0.9144 -0.0361 0.0647 0.0097 42 GLN A OE1 344 N NE2 . GLN A 42 ? 1.0567 0.9217 0.9483 -0.0358 0.0432 0.0052 42 GLN A NE2 345 N N . LYS A 43 ? 1.1811 0.9804 0.9742 0.0039 0.0636 0.0388 43 LYS A N 346 C CA . LYS A 43 ? 1.2760 1.0608 1.0462 0.0124 0.0698 0.0453 43 LYS A CA 347 C C . LYS A 43 ? 1.2940 1.0750 1.0466 0.0230 0.0653 0.0506 43 LYS A C 348 O O . LYS A 43 ? 1.3516 1.1448 1.0979 0.0273 0.0527 0.0498 43 LYS A O 349 C CB . LYS A 43 ? 1.3211 1.1134 1.0855 0.0123 0.0643 0.0436 43 LYS A CB 350 C CG . LYS A 43 ? 1.4006 1.1826 1.1384 0.0226 0.0656 0.0492 43 LYS A CG 351 C CD . LYS A 43 ? 1.4624 1.2213 1.1882 0.0263 0.0823 0.0551 43 LYS A CD 352 C CE . LYS A 43 ? 1.5198 1.2690 1.2184 0.0365 0.0830 0.0600 43 LYS A CE 353 N NZ . LYS A 43 ? 1.5854 1.3101 1.2691 0.0417 0.1001 0.0667 43 LYS A NZ 354 N N . ASP A 44 ? 1.2772 1.0414 1.0230 0.0271 0.0760 0.0555 44 ASP A N 355 C CA . ASP A 44 ? 1.3392 1.0962 1.0661 0.0386 0.0743 0.0617 44 ASP A CA 356 C C . ASP A 44 ? 1.3321 1.1055 1.0659 0.0396 0.0606 0.0592 44 ASP A C 357 O O . ASP A 44 ? 1.2711 1.0557 0.9964 0.0451 0.0487 0.0591 44 ASP A O 358 C CB . ASP A 44 ? 1.3667 1.1175 1.0680 0.0493 0.0730 0.0666 44 ASP A CB 359 C CG . ASP A 44 ? 1.4162 1.1543 1.0957 0.0625 0.0754 0.0742 44 ASP A CG 360 O OD1 . ASP A 44 ? 1.4758 1.2045 1.1588 0.0631 0.0826 0.0768 44 ASP A OD1 361 O OD2 . ASP A 44 ? 1.4206 1.1577 1.0789 0.0728 0.0703 0.0774 44 ASP A OD2 362 N N . PRO A 45 ? 1.3681 1.1424 1.1177 0.0341 0.0626 0.0569 45 PRO A N 363 C CA . PRO A 45 ? 1.3415 1.1284 1.0978 0.0351 0.0520 0.0551 45 PRO A CA 364 C C . PRO A 45 ? 1.3416 1.1270 1.0786 0.0478 0.0467 0.0608 45 PRO A C 365 O O . PRO A 45 ? 1.3570 1.1584 1.0956 0.0500 0.0338 0.0587 45 PRO A O 366 C CB . PRO A 45 ? 1.3518 1.1303 1.1210 0.0298 0.0608 0.0541 45 PRO A CB 367 C CG . PRO A 45 ? 1.3614 1.1342 1.1418 0.0208 0.0706 0.0507 45 PRO A CG 368 C CD . PRO A 45 ? 1.3492 1.1134 1.1130 0.0257 0.0753 0.0549 45 PRO A CD 369 N N . GLU A 46 ? 1.3711 1.1372 1.0901 0.0565 0.0570 0.0680 46 GLU A N 370 C CA . GLU A 46 ? 1.3467 1.1097 1.0462 0.0701 0.0529 0.0740 46 GLU A CA 371 C C . GLU A 46 ? 1.3260 1.1012 1.0128 0.0771 0.0405 0.0736 46 GLU A C 372 O O . GLU A 46 ? 1.3261 1.1061 1.0020 0.0872 0.0328 0.0763 46 GLU A O 373 C CB . GLU A 46 ? 1.4292 1.1666 1.1100 0.0783 0.0683 0.0821 46 GLU A CB 374 C CG . GLU A 46 ? 1.4932 1.2243 1.1579 0.0915 0.0673 0.0886 46 GLU A CG 375 C CD . GLU A 46 ? 1.5221 1.2284 1.1618 0.1028 0.0807 0.0974 46 GLU A CD 376 O OE1 . GLU A 46 ? 1.5334 1.2339 1.1594 0.1060 0.0832 0.0991 46 GLU A OE1 377 O OE2 . GLU A 46 ? 1.5299 1.2220 1.1630 0.1089 0.0890 0.1028 46 GLU A OE2 378 N N . ASN A 47 ? 1.2973 1.0776 0.9858 0.0719 0.0386 0.0700 47 ASN A N 379 C CA . ASN A 47 ? 1.2907 1.0833 0.9691 0.0769 0.0268 0.0681 47 ASN A CA 380 C C . ASN A 47 ? 1.2782 1.0902 0.9749 0.0662 0.0173 0.0600 47 ASN A C 381 O O . ASN A 47 ? 1.3103 1.1327 1.0009 0.0686 0.0081 0.0573 47 ASN A O 382 C CB . ASN A 47 ? 1.3347 1.1124 0.9905 0.0841 0.0337 0.0726 47 ASN A CB 383 C CG . ASN A 47 ? 1.3748 1.1338 1.0074 0.0977 0.0414 0.0812 47 ASN A CG 384 O OD1 . ASN A 47 ? 1.3877 1.1520 1.0104 0.1079 0.0332 0.0834 47 ASN A OD1 385 N ND2 . ASN A 47 ? 1.3980 1.1349 1.0221 0.0983 0.0576 0.0862 47 ASN A ND2 386 N N . SER A 48 ? 1.2369 1.0536 0.9553 0.0549 0.0195 0.0557 48 SER A N 387 C CA . SER A 48 ? 1.1773 1.0128 0.9131 0.0459 0.0100 0.0483 48 SER A CA 388 C C . SER A 48 ? 1.1362 0.9871 0.8811 0.0468 -0.0010 0.0458 48 SER A C 389 O O . SER A 48 ? 1.1472 0.9937 0.8933 0.0498 0.0011 0.0486 48 SER A O 390 C CB . SER A 48 ? 1.1817 1.0157 0.9355 0.0342 0.0170 0.0447 48 SER A CB 391 O OG . SER A 48 ? 1.2012 1.0264 0.9497 0.0321 0.0248 0.0453 48 SER A OG 392 N N . PRO A 49 ? 1.0783 0.9468 0.8301 0.0442 -0.0123 0.0405 49 PRO A N 393 C CA . PRO A 49 ? 1.0669 0.9501 0.8287 0.0448 -0.0221 0.0379 49 PRO A CA 394 C C . PRO A 49 ? 1.0115 0.8976 0.7918 0.0372 -0.0204 0.0356 49 PRO A C 395 O O . PRO A 49 ? 0.9677 0.8464 0.7555 0.0305 -0.0125 0.0350 49 PRO A O 396 C CB . PRO A 49 ? 1.0544 0.9538 0.8211 0.0417 -0.0321 0.0319 49 PRO A CB 397 C CG . PRO A 49 ? 1.0711 0.9633 0.8244 0.0432 -0.0289 0.0327 49 PRO A CG 398 C CD . PRO A 49 ? 1.0697 0.9446 0.8207 0.0407 -0.0159 0.0366 49 PRO A CD 399 N N . VAL A 50 ? 0.9889 0.8862 0.7763 0.0389 -0.0279 0.0341 50 VAL A N 400 C CA . VAL A 50 ? 0.9650 0.8661 0.7683 0.0331 -0.0278 0.0317 50 VAL A CA 401 C C . VAL A 50 ? 0.9226 0.8408 0.7393 0.0274 -0.0364 0.0256 50 VAL A C 402 O O . VAL A 50 ? 0.9525 0.8820 0.7689 0.0311 -0.0446 0.0242 50 VAL A O 403 C CB . VAL A 50 ? 0.9833 0.8820 0.7842 0.0398 -0.0281 0.0354 50 VAL A CB 404 C CG1 . VAL A 50 ? 0.9621 0.8667 0.7793 0.0341 -0.0295 0.0323 50 VAL A CG1 405 C CG2 . VAL A 50 ? 1.0028 0.8826 0.7915 0.0447 -0.0177 0.0415 50 VAL A CG2 406 N N . VAL A 51 ? 0.8480 0.7678 0.6767 0.0186 -0.0342 0.0218 51 VAL A N 407 C CA . VAL A 51 ? 0.8373 0.7707 0.6781 0.0130 -0.0405 0.0163 51 VAL A CA 408 C C . VAL A 51 ? 0.8237 0.7604 0.6777 0.0092 -0.0407 0.0143 51 VAL A C 409 O O . VAL A 51 ? 0.8226 0.7517 0.6809 0.0056 -0.0349 0.0142 51 VAL A O 410 C CB . VAL A 51 ? 0.8323 0.7653 0.6754 0.0069 -0.0380 0.0135 51 VAL A CB 411 C CG1 . VAL A 51 ? 0.8011 0.7457 0.6576 0.0006 -0.0424 0.0082 51 VAL A CG1 412 C CG2 . VAL A 51 ? 0.8420 0.7736 0.6720 0.0107 -0.0391 0.0147 51 VAL A CG2 413 N N . LEU A 52 ? 0.8066 0.7544 0.6670 0.0100 -0.0473 0.0121 52 LEU A N 414 C CA . LEU A 52 ? 0.8145 0.7661 0.6869 0.0063 -0.0480 0.0096 52 LEU A CA 415 C C . LEU A 52 ? 0.7918 0.7511 0.6727 0.0001 -0.0501 0.0048 52 LEU A C 416 O O . LEU A 52 ? 0.7774 0.7447 0.6581 0.0000 -0.0543 0.0029 52 LEU A O 417 C CB . LEU A 52 ? 0.8033 0.7622 0.6782 0.0109 -0.0529 0.0102 52 LEU A CB 418 C CG . LEU A 52 ? 0.8184 0.7817 0.7046 0.0080 -0.0539 0.0076 52 LEU A CG 419 C CD1 . LEU A 52 ? 0.8488 0.8018 0.7354 0.0076 -0.0486 0.0092 52 LEU A CD1 420 C CD2 . LEU A 52 ? 0.8197 0.7927 0.7098 0.0120 -0.0590 0.0074 52 LEU A CD2 421 N N . TRP A 53 ? 0.7472 0.7042 0.6354 -0.0047 -0.0472 0.0027 53 TRP A N 422 C CA . TRP A 53 ? 0.7378 0.7017 0.6336 -0.0096 -0.0490 -0.0014 53 TRP A CA 423 C C . TRP A 53 ? 0.7510 0.7185 0.6551 -0.0106 -0.0506 -0.0035 53 TRP A C 424 O O . TRP A 53 ? 0.8346 0.7966 0.7405 -0.0108 -0.0480 -0.0032 53 TRP A O 425 C CB . TRP A 53 ? 0.7451 0.7042 0.6422 -0.0141 -0.0447 -0.0028 53 TRP A CB 426 C CG . TRP A 53 ? 0.7093 0.6750 0.6141 -0.0181 -0.0464 -0.0068 53 TRP A CG 427 C CD1 . TRP A 53 ? 0.7005 0.6671 0.6127 -0.0205 -0.0461 -0.0094 53 TRP A CD1 428 C CD2 . TRP A 53 ? 0.6884 0.6602 0.5932 -0.0196 -0.0486 -0.0086 53 TRP A CD2 429 N NE1 . TRP A 53 ? 0.6847 0.6572 0.6010 -0.0227 -0.0477 -0.0123 53 TRP A NE1 430 C CE2 . TRP A 53 ? 0.6952 0.6707 0.6075 -0.0226 -0.0489 -0.0118 53 TRP A CE2 431 C CE3 . TRP A 53 ? 0.6848 0.6590 0.5837 -0.0185 -0.0504 -0.0082 53 TRP A CE3 432 C CZ2 . TRP A 53 ? 0.6853 0.6659 0.5993 -0.0247 -0.0499 -0.0141 53 TRP A CZ2 433 C CZ3 . TRP A 53 ? 0.6751 0.6549 0.5764 -0.0211 -0.0518 -0.0111 53 TRP A CZ3 434 C CH2 . TRP A 53 ? 0.6940 0.6766 0.6029 -0.0243 -0.0511 -0.0138 53 TRP A CH2 435 N N . LEU A 54 ? 0.7215 0.6976 0.6303 -0.0109 -0.0543 -0.0057 54 LEU A N 436 C CA . LEU A 54 ? 0.6838 0.6626 0.5993 -0.0114 -0.0551 -0.0075 54 LEU A CA 437 C C . LEU A 54 ? 0.7071 0.6902 0.6272 -0.0149 -0.0554 -0.0108 54 LEU A C 438 O O . LEU A 54 ? 0.7146 0.7031 0.6352 -0.0159 -0.0569 -0.0120 54 LEU A O 439 C CB . LEU A 54 ? 0.6783 0.6628 0.5960 -0.0079 -0.0580 -0.0067 54 LEU A CB 440 C CG . LEU A 54 ? 0.6914 0.6729 0.6054 -0.0030 -0.0582 -0.0033 54 LEU A CG 441 C CD1 . LEU A 54 ? 0.6938 0.6836 0.6125 -0.0001 -0.0614 -0.0036 54 LEU A CD1 442 C CD2 . LEU A 54 ? 0.7026 0.6760 0.6165 -0.0027 -0.0550 -0.0023 54 LEU A CD2 443 N N . ASN A 55 ? 0.7107 0.6914 0.6340 -0.0166 -0.0539 -0.0125 55 ASN A N 444 C CA . ASN A 55 ? 0.6899 0.6744 0.6171 -0.0183 -0.0541 -0.0153 55 ASN A CA 445 C C . ASN A 55 ? 0.6710 0.6585 0.6011 -0.0161 -0.0551 -0.0155 55 ASN A C 446 O O . ASN A 55 ? 0.6498 0.6363 0.5798 -0.0134 -0.0556 -0.0138 55 ASN A O 447 C CB . ASN A 55 ? 0.7068 0.6882 0.6357 -0.0198 -0.0528 -0.0173 55 ASN A CB 448 C CG . ASN A 55 ? 0.7365 0.7173 0.6650 -0.0227 -0.0513 -0.0181 55 ASN A CG 449 O OD1 . ASN A 55 ? 0.7335 0.7100 0.6612 -0.0238 -0.0494 -0.0177 55 ASN A OD1 450 N ND2 . ASN A 55 ? 0.7850 0.7694 0.7141 -0.0241 -0.0513 -0.0194 55 ASN A ND2 451 N N . GLY A 56 ? 0.6868 0.6775 0.6197 -0.0170 -0.0546 -0.0174 56 GLY A N 452 C CA . GLY A 56 ? 0.7171 0.7103 0.6534 -0.0152 -0.0542 -0.0177 56 GLY A CA 453 C C . GLY A 56 ? 0.7251 0.7145 0.6613 -0.0131 -0.0528 -0.0182 56 GLY A C 454 O O . GLY A 56 ? 0.7458 0.7311 0.6800 -0.0116 -0.0532 -0.0176 56 GLY A O 455 N N . GLY A 57 ? 0.7245 0.7146 0.6622 -0.0128 -0.0508 -0.0195 57 GLY A N 456 C CA . GLY A 57 ? 0.7450 0.7309 0.6807 -0.0098 -0.0491 -0.0200 57 GLY A CA 457 C C . GLY A 57 ? 0.7385 0.7248 0.6769 -0.0082 -0.0459 -0.0198 57 GLY A C 458 O O . GLY A 57 ? 0.7250 0.7116 0.6641 -0.0088 -0.0432 -0.0207 57 GLY A O 459 N N . PRO A 58 ? 0.7089 0.6950 0.6493 -0.0061 -0.0454 -0.0185 58 PRO A N 460 C CA . PRO A 58 ? 0.7243 0.7086 0.6632 -0.0046 -0.0477 -0.0171 58 PRO A CA 461 C C . PRO A 58 ? 0.7457 0.7237 0.6790 -0.0022 -0.0479 -0.0177 58 PRO A C 462 O O . PRO A 58 ? 0.7744 0.7490 0.7048 0.0002 -0.0459 -0.0185 58 PRO A O 463 C CB . PRO A 58 ? 0.7196 0.7052 0.6629 -0.0023 -0.0458 -0.0158 58 PRO A CB 464 C CG . PRO A 58 ? 0.7222 0.7123 0.6712 -0.0040 -0.0432 -0.0171 58 PRO A CG 465 C CD . PRO A 58 ? 0.6958 0.6837 0.6414 -0.0055 -0.0419 -0.0185 58 PRO A CD 466 N N . GLY A 59 ? 0.7511 0.7271 0.6826 -0.0026 -0.0502 -0.0175 59 GLY A N 467 C CA . GLY A 59 ? 0.7346 0.7053 0.6619 -0.0009 -0.0509 -0.0192 59 GLY A CA 468 C C . GLY A 59 ? 0.7466 0.7178 0.6738 -0.0038 -0.0529 -0.0214 59 GLY A C 469 O O . GLY A 59 ? 0.8018 0.7698 0.7271 -0.0032 -0.0541 -0.0237 59 GLY A O 470 N N . CYS A 60 ? 0.7772 0.7525 0.7066 -0.0071 -0.0532 -0.0210 60 CYS A N 471 C CA . CYS A 60 ? 0.8257 0.8016 0.7560 -0.0101 -0.0542 -0.0230 60 CYS A CA 472 C C . CYS A 60 ? 0.7994 0.7736 0.7303 -0.0125 -0.0541 -0.0217 60 CYS A C 473 O O . CYS A 60 ? 0.8028 0.7770 0.7331 -0.0120 -0.0537 -0.0189 60 CYS A O 474 C CB . CYS A 60 ? 0.8601 0.8401 0.7915 -0.0119 -0.0537 -0.0234 60 CYS A CB 475 S SG . CYS A 60 ? 0.9744 0.9543 0.9036 -0.0084 -0.0525 -0.0246 60 CYS A SG 476 N N . SER A 61 ? 0.7499 0.7228 0.6823 -0.0147 -0.0542 -0.0241 61 SER A N 477 C CA . SER A 61 ? 0.7433 0.7123 0.6761 -0.0167 -0.0527 -0.0233 61 SER A CA 478 C C . SER A 61 ? 0.7577 0.7278 0.6903 -0.0192 -0.0513 -0.0214 61 SER A C 479 O O . SER A 61 ? 0.7348 0.7084 0.6689 -0.0210 -0.0514 -0.0227 61 SER A O 480 C CB . SER A 61 ? 0.7487 0.7157 0.6849 -0.0184 -0.0527 -0.0276 61 SER A CB 481 O OG . SER A 61 ? 0.7697 0.7316 0.7068 -0.0207 -0.0499 -0.0270 61 SER A OG 482 N N . SER A 62 ? 0.7539 0.7200 0.6836 -0.0188 -0.0496 -0.0183 62 SER A N 483 C CA . SER A 62 ? 0.7550 0.7200 0.6824 -0.0204 -0.0477 -0.0162 62 SER A CA 484 C C . SER A 62 ? 0.8156 0.7768 0.7459 -0.0238 -0.0445 -0.0183 62 SER A C 485 O O . SER A 62 ? 0.8667 0.8259 0.7949 -0.0252 -0.0419 -0.0167 62 SER A O 486 C CB . SER A 62 ? 0.7368 0.6984 0.6590 -0.0175 -0.0469 -0.0120 62 SER A CB 487 O OG . SER A 62 ? 0.7042 0.6708 0.6255 -0.0147 -0.0499 -0.0106 62 SER A OG 488 N N . LEU A 63 ? 0.8301 0.7901 0.7653 -0.0250 -0.0444 -0.0220 63 LEU A N 489 C CA . LEU A 63 ? 0.8503 0.8084 0.7910 -0.0287 -0.0415 -0.0252 63 LEU A CA 490 C C . LEU A 63 ? 0.8746 0.8394 0.8194 -0.0305 -0.0430 -0.0279 63 LEU A C 491 O O . LEU A 63 ? 0.8599 0.8243 0.8094 -0.0336 -0.0402 -0.0298 63 LEU A O 492 C CB . LEU A 63 ? 0.8590 0.8142 0.8045 -0.0296 -0.0412 -0.0293 63 LEU A CB 493 C CG . LEU A 63 ? 0.8766 0.8237 0.8182 -0.0279 -0.0386 -0.0267 63 LEU A CG 494 C CD1 . LEU A 63 ? 0.8665 0.8101 0.8142 -0.0300 -0.0373 -0.0319 63 LEU A CD1 495 C CD2 . LEU A 63 ? 0.8636 0.8039 0.8002 -0.0278 -0.0336 -0.0217 63 LEU A CD2 496 N N . ASP A 64 ? 0.9267 0.8971 0.8700 -0.0284 -0.0466 -0.0280 64 ASP A N 497 C CA . ASP A 64 ? 0.9833 0.9590 0.9283 -0.0294 -0.0473 -0.0292 64 ASP A CA 498 C C . ASP A 64 ? 0.9884 0.9625 0.9303 -0.0311 -0.0444 -0.0262 64 ASP A C 499 O O . ASP A 64 ? 1.0319 1.0069 0.9770 -0.0335 -0.0423 -0.0275 64 ASP A O 500 C CB . ASP A 64 ? 1.0340 1.0139 0.9763 -0.0264 -0.0503 -0.0289 64 ASP A CB 501 C CG . ASP A 64 ? 1.1541 1.1387 1.0983 -0.0269 -0.0505 -0.0305 64 ASP A CG 502 O OD1 . ASP A 64 ? 1.1869 1.1737 1.1362 -0.0276 -0.0509 -0.0341 64 ASP A OD1 503 O OD2 . ASP A 64 ? 1.2166 1.2028 1.1576 -0.0264 -0.0503 -0.0286 64 ASP A OD2 504 N N . GLY A 65 ? 0.9208 0.8924 0.8564 -0.0295 -0.0442 -0.0222 65 GLY A N 505 C CA . GLY A 65 ? 0.8602 0.8295 0.7907 -0.0302 -0.0419 -0.0193 65 GLY A CA 506 C C . GLY A 65 ? 0.8538 0.8174 0.7858 -0.0326 -0.0370 -0.0193 65 GLY A C 507 O O . GLY A 65 ? 0.8439 0.8073 0.7758 -0.0345 -0.0344 -0.0194 65 GLY A O 508 N N . LEU A 66 ? 0.8271 0.7853 0.7605 -0.0326 -0.0349 -0.0194 66 LEU A N 509 C CA . LEU A 66 ? 0.8064 0.7580 0.7424 -0.0351 -0.0290 -0.0197 66 LEU A CA 510 C C . LEU A 66 ? 0.7953 0.7512 0.7410 -0.0388 -0.0280 -0.0244 66 LEU A C 511 O O . LEU A 66 ? 0.7631 0.7172 0.7094 -0.0408 -0.0238 -0.0238 66 LEU A O 512 C CB . LEU A 66 ? 0.7756 0.7208 0.7129 -0.0348 -0.0268 -0.0198 66 LEU A CB 513 C CG . LEU A 66 ? 0.7818 0.7172 0.7191 -0.0367 -0.0189 -0.0186 66 LEU A CG 514 C CD1 . LEU A 66 ? 0.7833 0.7105 0.7179 -0.0350 -0.0162 -0.0169 66 LEU A CD1 515 C CD2 . LEU A 66 ? 0.7742 0.7111 0.7232 -0.0416 -0.0156 -0.0238 66 LEU A CD2 516 N N . LEU A 67 ? 0.7895 0.7514 0.7425 -0.0392 -0.0319 -0.0289 67 LEU A N 517 C CA . LEU A 67 ? 0.8060 0.7724 0.7699 -0.0421 -0.0313 -0.0343 67 LEU A CA 518 C C . LEU A 67 ? 0.8312 0.8048 0.7968 -0.0421 -0.0332 -0.0353 67 LEU A C 519 O O . LEU A 67 ? 0.8147 0.7921 0.7894 -0.0444 -0.0319 -0.0392 67 LEU A O 520 C CB . LEU A 67 ? 0.8225 0.7922 0.7927 -0.0417 -0.0351 -0.0394 67 LEU A CB 521 C CG . LEU A 67 ? 0.8553 0.8177 0.8280 -0.0434 -0.0317 -0.0405 67 LEU A CG 522 C CD1 . LEU A 67 ? 0.8781 0.8430 0.8533 -0.0418 -0.0364 -0.0448 67 LEU A CD1 523 C CD2 . LEU A 67 ? 0.8712 0.8315 0.8540 -0.0481 -0.0257 -0.0439 67 LEU A CD2 524 N N . THR A 68 ? 0.8171 0.7927 0.7749 -0.0395 -0.0361 -0.0323 68 THR A N 525 C CA . THR A 68 ? 0.8108 0.7921 0.7695 -0.0392 -0.0372 -0.0331 68 THR A CA 526 C C . THR A 68 ? 0.8066 0.7859 0.7571 -0.0391 -0.0356 -0.0290 68 THR A C 527 O O . THR A 68 ? 0.8351 0.8178 0.7860 -0.0392 -0.0355 -0.0296 68 THR A O 528 C CB . THR A 68 ? 0.7809 0.7680 0.7399 -0.0361 -0.0424 -0.0351 68 THR A CB 529 O OG1 . THR A 68 ? 0.8804 0.8660 0.8314 -0.0338 -0.0441 -0.0317 68 THR A OG1 530 C CG2 . THR A 68 ? 0.7788 0.7675 0.7435 -0.0353 -0.0450 -0.0393 68 THR A CG2 531 N N . GLU A 69 ? 0.8210 0.7949 0.7639 -0.0384 -0.0344 -0.0253 69 GLU A N 532 C CA . GLU A 69 ? 0.8160 0.7887 0.7505 -0.0377 -0.0340 -0.0222 69 GLU A CA 533 C C . GLU A 69 ? 0.8805 0.8459 0.8093 -0.0384 -0.0291 -0.0194 69 GLU A C 534 O O . GLU A 69 ? 0.9601 0.9245 0.8878 -0.0399 -0.0260 -0.0193 69 GLU A O 535 C CB . GLU A 69 ? 0.8317 0.8058 0.7608 -0.0350 -0.0379 -0.0205 69 GLU A CB 536 C CG . GLU A 69 ? 0.8518 0.8314 0.7846 -0.0337 -0.0417 -0.0226 69 GLU A CG 537 C CD . GLU A 69 ? 0.8932 0.8746 0.8215 -0.0317 -0.0445 -0.0210 69 GLU A CD 538 O OE1 . GLU A 69 ? 0.8788 0.8619 0.8037 -0.0321 -0.0445 -0.0206 69 GLU A OE1 539 O OE2 . GLU A 69 ? 0.9509 0.9322 0.8795 -0.0297 -0.0464 -0.0205 69 GLU A OE2 540 N N . HIS A 70 ? 0.8531 0.8127 0.7773 -0.0369 -0.0278 -0.0168 70 HIS A N 541 C CA . HIS A 70 ? 0.8360 0.7872 0.7522 -0.0363 -0.0228 -0.0134 70 HIS A CA 542 C C . HIS A 70 ? 0.8315 0.7740 0.7471 -0.0358 -0.0181 -0.0115 70 HIS A C 543 O O . HIS A 70 ? 0.8618 0.7964 0.7675 -0.0333 -0.0147 -0.0076 70 HIS A O 544 C CB . HIS A 70 ? 0.8473 0.7989 0.7523 -0.0330 -0.0259 -0.0106 70 HIS A CB 545 C CG . HIS A 70 ? 0.8895 0.8440 0.7925 -0.0300 -0.0310 -0.0097 70 HIS A CG 546 N ND1 . HIS A 70 ? 0.8938 0.8543 0.7934 -0.0282 -0.0361 -0.0099 70 HIS A ND1 547 C CD2 . HIS A 70 ? 0.8721 0.8242 0.7768 -0.0285 -0.0313 -0.0088 70 HIS A CD2 548 C CE1 . HIS A 70 ? 0.8672 0.8295 0.7670 -0.0256 -0.0394 -0.0091 70 HIS A CE1 549 N NE2 . HIS A 70 ? 0.8854 0.8424 0.7876 -0.0255 -0.0365 -0.0082 70 HIS A NE2 550 N N . GLY A 71 ? 0.7973 0.7409 0.7226 -0.0377 -0.0179 -0.0145 71 GLY A N 551 C CA . GLY A 71 ? 0.7687 0.7034 0.6950 -0.0381 -0.0124 -0.0136 71 GLY A CA 552 C C . GLY A 71 ? 0.7586 0.6870 0.6877 -0.0410 -0.0043 -0.0137 71 GLY A C 553 O O . GLY A 71 ? 0.7391 0.6715 0.6709 -0.0429 -0.0038 -0.0151 71 GLY A O 554 N N . PRO A 72 ? 0.7554 0.6732 0.6836 -0.0413 0.0029 -0.0121 72 PRO A N 555 C CA . PRO A 72 ? 0.7895 0.6997 0.7213 -0.0442 0.0124 -0.0122 72 PRO A CA 556 C C . PRO A 72 ? 0.8231 0.7409 0.7725 -0.0498 0.0130 -0.0188 72 PRO A C 557 O O . PRO A 72 ? 0.8540 0.7693 0.8083 -0.0526 0.0195 -0.0197 72 PRO A O 558 C CB . PRO A 72 ? 0.8025 0.7001 0.7315 -0.0433 0.0195 -0.0098 72 PRO A CB 559 C CG . PRO A 72 ? 0.8095 0.7108 0.7384 -0.0414 0.0129 -0.0105 72 PRO A CG 560 C CD . PRO A 72 ? 0.7961 0.7075 0.7191 -0.0384 0.0033 -0.0096 72 PRO A CD 561 N N . PHE A 73 ? 0.8116 0.7387 0.7702 -0.0510 0.0063 -0.0236 73 PHE A N 562 C CA . PHE A 73 ? 0.7973 0.7333 0.7719 -0.0550 0.0052 -0.0304 73 PHE A CA 563 C C . PHE A 73 ? 0.7665 0.7143 0.7433 -0.0534 -0.0049 -0.0334 73 PHE A C 564 O O . PHE A 73 ? 0.7439 0.6918 0.7144 -0.0505 -0.0097 -0.0319 73 PHE A O 565 C CB . PHE A 73 ? 0.8214 0.7534 0.8083 -0.0590 0.0106 -0.0349 73 PHE A CB 566 C CG . PHE A 73 ? 0.8255 0.7488 0.8060 -0.0572 0.0119 -0.0326 73 PHE A CG 567 C CD1 . PHE A 73 ? 0.8305 0.7588 0.8093 -0.0550 0.0039 -0.0339 73 PHE A CD1 568 C CD2 . PHE A 73 ? 0.8395 0.7486 0.8152 -0.0574 0.0219 -0.0288 73 PHE A CD2 569 C CE1 . PHE A 73 ? 0.8242 0.7443 0.7973 -0.0532 0.0055 -0.0317 73 PHE A CE1 570 C CE2 . PHE A 73 ? 0.8328 0.7332 0.8023 -0.0553 0.0236 -0.0264 73 PHE A CE2 571 C CZ . PHE A 73 ? 0.8266 0.7330 0.7952 -0.0533 0.0152 -0.0280 73 PHE A CZ 572 N N . LEU A 74 ? 0.7621 0.7195 0.7480 -0.0548 -0.0075 -0.0376 74 LEU A N 573 C CA . LEU A 74 ? 0.7609 0.7287 0.7481 -0.0525 -0.0162 -0.0402 74 LEU A CA 574 C C . LEU A 74 ? 0.7538 0.7298 0.7560 -0.0545 -0.0188 -0.0479 74 LEU A C 575 O O . LEU A 74 ? 0.7683 0.7467 0.7820 -0.0578 -0.0149 -0.0516 74 LEU A O 576 C CB . LEU A 74 ? 0.7502 0.7226 0.7332 -0.0511 -0.0177 -0.0383 74 LEU A CB 577 C CG . LEU A 74 ? 0.7630 0.7285 0.7328 -0.0498 -0.0147 -0.0321 74 LEU A CG 578 C CD1 . LEU A 74 ? 0.7468 0.7174 0.7154 -0.0493 -0.0157 -0.0319 74 LEU A CD1 579 C CD2 . LEU A 74 ? 0.7742 0.7367 0.7324 -0.0465 -0.0185 -0.0282 74 LEU A CD2 580 N N . VAL A 75 ? 0.7415 0.7218 0.7436 -0.0522 -0.0255 -0.0506 75 VAL A N 581 C CA . VAL A 75 ? 0.7386 0.7281 0.7529 -0.0526 -0.0300 -0.0583 75 VAL A CA 582 C C . VAL A 75 ? 0.7487 0.7478 0.7681 -0.0514 -0.0326 -0.0605 75 VAL A C 583 O O . VAL A 75 ? 0.7457 0.7454 0.7560 -0.0485 -0.0341 -0.0561 75 VAL A O 584 C CB . VAL A 75 ? 0.7282 0.7195 0.7377 -0.0489 -0.0369 -0.0598 75 VAL A CB 585 C CG1 . VAL A 75 ? 0.7382 0.7333 0.7379 -0.0440 -0.0420 -0.0565 75 VAL A CG1 586 C CG2 . VAL A 75 ? 0.7682 0.7667 0.7898 -0.0497 -0.0409 -0.0686 75 VAL A CG2 587 N N . GLN A 76 ? 0.8078 0.8142 0.8423 -0.0537 -0.0326 -0.0675 76 GLN A N 588 C CA . GLN A 76 ? 0.8411 0.8577 0.8828 -0.0523 -0.0348 -0.0704 76 GLN A CA 589 C C . GLN A 76 ? 0.8386 0.8652 0.8825 -0.0477 -0.0439 -0.0757 76 GLN A C 590 O O . GLN A 76 ? 0.8589 0.8847 0.9018 -0.0468 -0.0476 -0.0786 76 GLN A O 591 C CB . GLN A 76 ? 0.8902 0.9097 0.9488 -0.0574 -0.0292 -0.0754 76 GLN A CB 592 C CG . GLN A 76 ? 0.9144 0.9225 0.9709 -0.0617 -0.0191 -0.0705 76 GLN A CG 593 C CD . GLN A 76 ? 0.8859 0.8908 0.9316 -0.0600 -0.0164 -0.0636 76 GLN A CD 594 O OE1 . GLN A 76 ? 0.8398 0.8507 0.8919 -0.0599 -0.0153 -0.0650 76 GLN A OE1 595 N NE2 . GLN A 76 ? 0.8553 0.8512 0.8846 -0.0581 -0.0158 -0.0567 76 GLN A NE2 596 N N . PRO A 77 ? 0.8530 0.8883 0.8994 -0.0442 -0.0471 -0.0773 77 PRO A N 597 C CA . PRO A 77 ? 0.8788 0.9219 0.9224 -0.0377 -0.0555 -0.0805 77 PRO A CA 598 C C . PRO A 77 ? 0.9206 0.9710 0.9744 -0.0372 -0.0612 -0.0895 77 PRO A C 599 O O . PRO A 77 ? 0.9342 0.9877 0.9816 -0.0315 -0.0681 -0.0914 77 PRO A O 600 C CB . PRO A 77 ? 0.8513 0.9019 0.8980 -0.0347 -0.0560 -0.0805 77 PRO A CB 601 C CG . PRO A 77 ? 0.8559 0.8997 0.9001 -0.0387 -0.0480 -0.0745 77 PRO A CG 602 C CD . PRO A 77 ? 0.8841 0.9217 0.9346 -0.0453 -0.0426 -0.0754 77 PRO A CD 603 N N . ASP A 78 ? 0.9752 1.0278 1.0445 -0.0432 -0.0581 -0.0952 78 ASP A N 604 C CA . ASP A 78 ? 0.9813 1.0406 1.0620 -0.0439 -0.0631 -0.1049 78 ASP A CA 605 C C . ASP A 78 ? 0.9553 1.0059 1.0278 -0.0445 -0.0640 -0.1044 78 ASP A C 606 O O . ASP A 78 ? 0.9845 1.0392 1.0640 -0.0448 -0.0683 -0.1123 78 ASP A O 607 C CB . ASP A 78 ? 1.0283 1.0923 1.1301 -0.0509 -0.0581 -0.1117 78 ASP A CB 608 C CG . ASP A 78 ? 1.0123 1.0635 1.1143 -0.0580 -0.0473 -0.1068 78 ASP A CG 609 O OD1 . ASP A 78 ? 1.0316 1.0712 1.1196 -0.0578 -0.0453 -0.1006 78 ASP A OD1 610 O OD2 . ASP A 78 ? 0.9655 1.0179 1.0813 -0.0631 -0.0406 -0.1090 78 ASP A OD2 611 N N . GLY A 79 ? 1.0201 1.0588 1.0784 -0.0448 -0.0597 -0.0956 79 GLY A N 612 C CA . GLY A 79 ? 0.9959 1.0258 1.0459 -0.0449 -0.0600 -0.0942 79 GLY A CA 613 C C . GLY A 79 ? 0.9895 1.0134 1.0490 -0.0516 -0.0541 -0.0974 79 GLY A C 614 O O . GLY A 79 ? 1.0034 1.0195 1.0569 -0.0519 -0.0536 -0.0966 79 GLY A O 615 N N . VAL A 80 ? 0.9821 1.0087 1.0564 -0.0570 -0.0488 -0.1009 80 VAL A N 616 C CA . VAL A 80 ? 0.9588 0.9809 1.0458 -0.0638 -0.0425 -0.1060 80 VAL A CA 617 C C . VAL A 80 ? 0.9759 0.9878 1.0636 -0.0687 -0.0311 -0.0999 80 VAL A C 618 O O . VAL A 80 ? 0.9891 0.9896 1.0756 -0.0722 -0.0241 -0.0981 80 VAL A O 619 C CB . VAL A 80 ? 0.9402 0.9757 1.0479 -0.0663 -0.0461 -0.1182 80 VAL A CB 620 C CG1 . VAL A 80 ? 0.9597 0.9913 1.0843 -0.0746 -0.0371 -0.1233 80 VAL A CG1 621 C CG2 . VAL A 80 ? 0.9356 0.9780 1.0420 -0.0621 -0.0565 -0.1254 80 VAL A CG2 622 N N . THR A 81 ? 0.9830 0.9985 1.0719 -0.0683 -0.0289 -0.0967 81 THR A N 623 C CA . THR A 81 ? 0.9322 0.9388 1.0218 -0.0723 -0.0182 -0.0915 81 THR A CA 624 C C . THR A 81 ? 0.9247 0.9208 0.9938 -0.0689 -0.0161 -0.0804 81 THR A C 625 O O . THR A 81 ? 0.9287 0.9287 0.9870 -0.0640 -0.0223 -0.0768 81 THR A O 626 C CB . THR A 81 ? 0.9580 0.9739 1.0595 -0.0734 -0.0165 -0.0940 81 THR A CB 627 O OG1 . THR A 81 ? 0.8958 0.9259 1.0159 -0.0745 -0.0220 -0.1050 81 THR A OG1 628 C CG2 . THR A 81 ? 0.9797 0.9860 1.0858 -0.0785 -0.0039 -0.0908 81 THR A CG2 629 N N . LEU A 82 ? 0.9496 0.9324 1.0136 -0.0715 -0.0069 -0.0754 82 LEU A N 630 C CA . LEU A 82 ? 0.9377 0.9106 0.9837 -0.0686 -0.0039 -0.0653 82 LEU A CA 631 C C . LEU A 82 ? 0.9541 0.9224 1.0020 -0.0710 0.0050 -0.0623 82 LEU A C 632 O O . LEU A 82 ? 0.9853 0.9497 1.0451 -0.0757 0.0132 -0.0655 82 LEU A O 633 C CB . LEU A 82 ? 0.9496 0.9096 0.9862 -0.0684 0.0000 -0.0613 82 LEU A CB 634 C CG . LEU A 82 ? 0.9302 0.8910 0.9618 -0.0657 -0.0069 -0.0626 82 LEU A CG 635 C CD1 . LEU A 82 ? 0.9467 0.8936 0.9657 -0.0642 -0.0018 -0.0560 82 LEU A CD1 636 C CD2 . LEU A 82 ? 0.8994 0.8687 0.9226 -0.0606 -0.0166 -0.0610 82 LEU A CD2 637 N N . GLU A 83 ? 0.9293 0.8975 0.9658 -0.0680 0.0040 -0.0564 83 GLU A N 638 C CA . GLU A 83 ? 0.9540 0.9162 0.9889 -0.0694 0.0126 -0.0526 83 GLU A CA 639 C C . GLU A 83 ? 0.9511 0.9012 0.9659 -0.0662 0.0155 -0.0437 83 GLU A C 640 O O . GLU A 83 ? 0.9272 0.8786 0.9301 -0.0622 0.0085 -0.0405 83 GLU A O 641 C CB . GLU A 83 ? 0.9911 0.9634 1.0298 -0.0684 0.0095 -0.0538 83 GLU A CB 642 C CG . GLU A 83 ? 1.0401 1.0244 1.0998 -0.0713 0.0086 -0.0622 83 GLU A CG 643 C CD . GLU A 83 ? 1.0888 1.0687 1.1638 -0.0771 0.0187 -0.0661 83 GLU A CD 644 O OE1 . GLU A 83 ? 1.0868 1.0534 1.1554 -0.0786 0.0288 -0.0610 83 GLU A OE1 645 O OE2 . GLU A 83 ? 1.0777 1.0677 1.1716 -0.0799 0.0167 -0.0748 83 GLU A OE2 646 N N . TYR A 84 ? 0.9267 0.8649 0.9380 -0.0675 0.0259 -0.0400 84 TYR A N 647 C CA . TYR A 84 ? 0.9187 0.8452 0.9102 -0.0636 0.0287 -0.0319 84 TYR A CA 648 C C . TYR A 84 ? 0.9464 0.8780 0.9274 -0.0604 0.0231 -0.0287 84 TYR A C 649 O O . TYR A 84 ? 0.9416 0.8820 0.9305 -0.0617 0.0213 -0.0318 84 TYR A O 650 C CB . TYR A 84 ? 0.9122 0.8239 0.9006 -0.0649 0.0418 -0.0283 84 TYR A CB 651 C CG . TYR A 84 ? 0.8929 0.7946 0.8845 -0.0665 0.0482 -0.0289 84 TYR A CG 652 C CD1 . TYR A 84 ? 0.8977 0.7894 0.8735 -0.0621 0.0484 -0.0231 84 TYR A CD1 653 C CD2 . TYR A 84 ? 0.8855 0.7886 0.8969 -0.0723 0.0538 -0.0357 84 TYR A CD2 654 C CE1 . TYR A 84 ? 0.9110 0.7928 0.8892 -0.0632 0.0547 -0.0235 84 TYR A CE1 655 C CE2 . TYR A 84 ? 0.8993 0.7927 0.9141 -0.0742 0.0601 -0.0367 84 TYR A CE2 656 C CZ . TYR A 84 ? 0.9101 0.7922 0.9076 -0.0695 0.0609 -0.0302 84 TYR A CZ 657 O OH . TYR A 84 ? 0.8964 0.7672 0.8952 -0.0706 0.0679 -0.0304 84 TYR A OH 658 N N . ASN A 85 ? 0.9197 0.8461 0.8834 -0.0560 0.0204 -0.0230 85 ASN A N 659 C CA . ASN A 85 ? 0.8542 0.7849 0.8075 -0.0530 0.0149 -0.0205 85 ASN A CA 660 C C . ASN A 85 ? 0.8459 0.7653 0.7841 -0.0506 0.0212 -0.0148 85 ASN A C 661 O O . ASN A 85 ? 0.8076 0.7186 0.7337 -0.0473 0.0224 -0.0105 85 ASN A O 662 C CB . ASN A 85 ? 0.8494 0.7849 0.7962 -0.0499 0.0058 -0.0197 85 ASN A CB 663 C CG . ASN A 85 ? 0.8307 0.7706 0.7676 -0.0472 0.0003 -0.0177 85 ASN A CG 664 O OD1 . ASN A 85 ? 0.8811 0.8201 0.8147 -0.0475 0.0029 -0.0168 85 ASN A OD1 665 N ND2 . ASN A 85 ? 0.8364 0.7804 0.7687 -0.0446 -0.0066 -0.0171 85 ASN A ND2 666 N N . PRO A 86 ? 0.8838 0.8032 0.8218 -0.0516 0.0249 -0.0146 86 PRO A N 667 C CA . PRO A 86 ? 0.8821 0.7900 0.8047 -0.0490 0.0313 -0.0094 86 PRO A CA 668 C C . PRO A 86 ? 0.9144 0.8221 0.8195 -0.0441 0.0247 -0.0060 86 PRO A C 669 O O . PRO A 86 ? 0.8974 0.7949 0.7870 -0.0406 0.0286 -0.0015 86 PRO A O 670 C CB . PRO A 86 ? 0.8828 0.7931 0.8115 -0.0515 0.0354 -0.0112 86 PRO A CB 671 C CG . PRO A 86 ? 0.8809 0.8050 0.8280 -0.0550 0.0304 -0.0173 86 PRO A CG 672 C CD . PRO A 86 ? 0.8599 0.7904 0.8092 -0.0541 0.0219 -0.0190 86 PRO A CD 673 N N . TYR A 87 ? 0.9257 0.8445 0.8334 -0.0438 0.0149 -0.0083 87 TYR A N 674 C CA . TYR A 87 ? 0.8467 0.7676 0.7412 -0.0399 0.0079 -0.0063 87 TYR A CA 675 C C . TYR A 87 ? 0.8422 0.7643 0.7348 -0.0374 0.0027 -0.0054 87 TYR A C 676 O O . TYR A 87 ? 0.8480 0.7755 0.7349 -0.0350 -0.0043 -0.0052 87 TYR A O 677 C CB . TYR A 87 ? 0.8054 0.7367 0.7039 -0.0413 0.0021 -0.0095 87 TYR A CB 678 C CG . TYR A 87 ? 0.8423 0.7733 0.7450 -0.0439 0.0074 -0.0108 87 TYR A CG 679 C CD1 . TYR A 87 ? 0.8880 0.8100 0.7794 -0.0426 0.0133 -0.0080 87 TYR A CD1 680 C CD2 . TYR A 87 ? 0.8296 0.7689 0.7470 -0.0470 0.0067 -0.0148 87 TYR A CD2 681 C CE1 . TYR A 87 ? 0.9142 0.8354 0.8095 -0.0448 0.0187 -0.0090 87 TYR A CE1 682 C CE2 . TYR A 87 ? 0.8427 0.7821 0.7647 -0.0489 0.0117 -0.0159 87 TYR A CE2 683 C CZ . TYR A 87 ? 0.8945 0.8247 0.8056 -0.0481 0.0179 -0.0129 87 TYR A CZ 684 O OH . TYR A 87 ? 0.9362 0.8659 0.8516 -0.0498 0.0234 -0.0138 87 TYR A OH 685 N N . SER A 88 ? 0.8719 0.7886 0.7690 -0.0379 0.0067 -0.0048 88 SER A N 686 C CA . SER A 88 ? 0.8808 0.7983 0.7765 -0.0355 0.0023 -0.0038 88 SER A CA 687 C C . SER A 88 ? 0.8804 0.7928 0.7596 -0.0296 0.0004 0.0007 88 SER A C 688 O O . SER A 88 ? 0.9193 0.8221 0.7867 -0.0268 0.0056 0.0043 88 SER A O 689 C CB . SER A 88 ? 0.9184 0.8293 0.8214 -0.0372 0.0081 -0.0042 88 SER A CB 690 O OG . SER A 88 ? 0.8985 0.8083 0.7974 -0.0339 0.0045 -0.0025 88 SER A OG 691 N N . TRP A 89 ? 0.8651 0.7838 0.7435 -0.0272 -0.0070 0.0005 89 TRP A N 692 C CA . TRP A 89 ? 0.8713 0.7881 0.7357 -0.0212 -0.0105 0.0041 89 TRP A CA 693 C C . TRP A 89 ? 0.8777 0.7823 0.7337 -0.0171 -0.0047 0.0087 89 TRP A C 694 O O . TRP A 89 ? 0.8736 0.7730 0.7149 -0.0111 -0.0049 0.0125 89 TRP A O 695 C CB . TRP A 89 ? 0.8263 0.7541 0.6943 -0.0201 -0.0197 0.0022 89 TRP A CB 696 C CG . TRP A 89 ? 0.7965 0.7343 0.6680 -0.0224 -0.0248 -0.0012 89 TRP A CG 697 C CD1 . TRP A 89 ? 0.7839 0.7228 0.6587 -0.0262 -0.0224 -0.0034 89 TRP A CD1 698 C CD2 . TRP A 89 ? 0.7674 0.7150 0.6400 -0.0213 -0.0324 -0.0031 89 TRP A CD2 699 N NE1 . TRP A 89 ? 0.7563 0.7042 0.6332 -0.0273 -0.0278 -0.0063 89 TRP A NE1 700 C CE2 . TRP A 89 ? 0.7355 0.6888 0.6116 -0.0246 -0.0338 -0.0063 89 TRP A CE2 701 C CE3 . TRP A 89 ? 0.7881 0.7399 0.6597 -0.0178 -0.0376 -0.0024 89 TRP A CE3 702 C CZ2 . TRP A 89 ? 0.7198 0.6822 0.5984 -0.0248 -0.0397 -0.0090 89 TRP A CZ2 703 C CZ3 . TRP A 89 ? 0.7707 0.7325 0.6458 -0.0181 -0.0437 -0.0053 89 TRP A CZ3 704 C CH2 . TRP A 89 ? 0.7446 0.7112 0.6232 -0.0218 -0.0445 -0.0087 89 TRP A CH2 705 N N . ASN A 90 ? 0.8742 0.7738 0.7391 -0.0199 0.0006 0.0081 90 ASN A N 706 C CA . ASN A 90 ? 0.9170 0.8031 0.7742 -0.0163 0.0079 0.0125 90 ASN A CA 707 C C . ASN A 90 ? 0.9536 0.8269 0.8030 -0.0158 0.0181 0.0155 90 ASN A C 708 O O . ASN A 90 ? 1.0465 0.9064 0.8909 -0.0137 0.0267 0.0189 90 ASN A O 709 C CB . ASN A 90 ? 0.9071 0.7912 0.7765 -0.0197 0.0109 0.0104 90 ASN A CB 710 C CG . ASN A 90 ? 0.9777 0.8568 0.8581 -0.0258 0.0195 0.0076 90 ASN A CG 711 O OD1 . ASN A 90 ? 0.9593 0.8443 0.8468 -0.0299 0.0192 0.0043 90 ASN A OD1 712 N ND2 . ASN A 90 ? 1.0224 0.8902 0.9048 -0.0264 0.0279 0.0086 90 ASN A ND2 713 N N . LEU A 91 ? 0.9259 0.8021 0.7739 -0.0176 0.0180 0.0142 91 LEU A N 714 C CA . LEU A 91 ? 0.9374 0.8009 0.7745 -0.0156 0.0272 0.0177 91 LEU A CA 715 C C . LEU A 91 ? 0.9873 0.8424 0.8029 -0.0065 0.0268 0.0235 91 LEU A C 716 O O . LEU A 91 ? 1.0117 0.8515 0.8159 -0.0027 0.0364 0.0282 91 LEU A O 717 C CB . LEU A 91 ? 0.9103 0.7788 0.7494 -0.0189 0.0268 0.0151 91 LEU A CB 718 C CG . LEU A 91 ? 0.8903 0.7633 0.7488 -0.0269 0.0308 0.0103 91 LEU A CG 719 C CD1 . LEU A 91 ? 0.8733 0.7535 0.7333 -0.0292 0.0281 0.0078 91 LEU A CD1 720 C CD2 . LEU A 91 ? 0.8727 0.7326 0.7351 -0.0290 0.0438 0.0117 91 LEU A CD2 721 N N . ILE A 92 ? 0.9810 0.8461 0.7913 -0.0027 0.0159 0.0230 92 ILE A N 722 C CA . ILE A 92 ? 0.9831 0.8440 0.7736 0.0064 0.0128 0.0273 92 ILE A CA 723 C C . ILE A 92 ? 1.0145 0.8825 0.8050 0.0107 0.0047 0.0278 92 ILE A C 724 O O . ILE A 92 ? 1.0714 0.9419 0.8491 0.0178 -0.0014 0.0295 92 ILE A O 725 C CB . ILE A 92 ? 0.9770 0.8448 0.7596 0.0076 0.0065 0.0253 92 ILE A CB 726 C CG1 . ILE A 92 ? 0.9610 0.8468 0.7583 0.0022 -0.0035 0.0193 92 ILE A CG1 727 C CG2 . ILE A 92 ? 1.0029 0.8617 0.7821 0.0051 0.0154 0.0258 92 ILE A CG2 728 C CD1 . ILE A 92 ? 0.9513 0.8450 0.7421 0.0031 -0.0105 0.0164 92 ILE A CD1 729 N N . ALA A 93 ? 1.0103 0.8820 0.8152 0.0065 0.0043 0.0259 93 ALA A N 730 C CA . ALA A 93 ? 1.0075 0.8858 0.8134 0.0103 -0.0027 0.0263 93 ALA A CA 731 C C . ALA A 93 ? 0.9794 0.8541 0.7964 0.0072 0.0013 0.0261 93 ALA A C 732 O O . ALA A 93 ? 0.9941 0.8667 0.8230 0.0003 0.0067 0.0234 93 ALA A O 733 C CB . ALA A 93 ? 1.0015 0.8972 0.8154 0.0078 -0.0139 0.0215 93 ALA A CB 734 N N . ASN A 94 ? 0.9311 0.8052 0.7441 0.0127 -0.0012 0.0287 94 ASN A N 735 C CA . ASN A 94 ? 0.9556 0.8280 0.7791 0.0101 0.0009 0.0279 94 ASN A CA 736 C C . ASN A 94 ? 0.9646 0.8532 0.8002 0.0069 -0.0089 0.0232 94 ASN A C 737 O O . ASN A 94 ? 0.9491 0.8455 0.7809 0.0118 -0.0164 0.0239 94 ASN A O 738 C CB . ASN A 94 ? 0.9642 0.8262 0.7764 0.0182 0.0043 0.0336 94 ASN A CB 739 C CG . ASN A 94 ? 0.9653 0.8103 0.7616 0.0235 0.0142 0.0393 94 ASN A CG 740 O OD1 . ASN A 94 ? 0.9271 0.7613 0.7267 0.0190 0.0243 0.0392 94 ASN A OD1 741 N ND2 . ASN A 94 ? 0.9761 0.8189 0.7551 0.0333 0.0113 0.0439 94 ASN A ND2 742 N N . VAL A 95 ? 0.9771 0.8707 0.8273 -0.0008 -0.0088 0.0182 95 VAL A N 743 C CA . VAL A 95 ? 0.9297 0.8376 0.7906 -0.0041 -0.0172 0.0136 95 VAL A CA 744 C C . VAL A 95 ? 0.9139 0.8216 0.7827 -0.0049 -0.0173 0.0125 95 VAL A C 745 O O . VAL A 95 ? 0.9551 0.8562 0.8302 -0.0087 -0.0115 0.0110 95 VAL A O 746 C CB . VAL A 95 ? 0.9276 0.8415 0.7981 -0.0110 -0.0175 0.0089 95 VAL A CB 747 C CG1 . VAL A 95 ? 0.9072 0.8349 0.7836 -0.0123 -0.0260 0.0054 95 VAL A CG1 748 C CG2 . VAL A 95 ? 0.9705 0.8792 0.8335 -0.0111 -0.0132 0.0103 95 VAL A CG2 749 N N . LEU A 96 ? 0.9054 0.8206 0.7746 -0.0016 -0.0238 0.0127 96 LEU A N 750 C CA . LEU A 96 ? 0.8949 0.8105 0.7710 -0.0019 -0.0246 0.0115 96 LEU A CA 751 C C . LEU A 96 ? 0.8330 0.7601 0.7199 -0.0060 -0.0304 0.0066 96 LEU A C 752 O O . LEU A 96 ? 0.8602 0.7965 0.7475 -0.0039 -0.0365 0.0063 96 LEU A O 753 C CB . LEU A 96 ? 0.8984 0.8130 0.7671 0.0055 -0.0267 0.0158 96 LEU A CB 754 C CG . LEU A 96 ? 0.9055 0.8190 0.7793 0.0063 -0.0267 0.0155 96 LEU A CG 755 C CD1 . LEU A 96 ? 0.8929 0.7943 0.7692 0.0032 -0.0189 0.0149 96 LEU A CD1 756 C CD2 . LEU A 96 ? 0.9167 0.8302 0.7829 0.0145 -0.0289 0.0201 96 LEU A CD2 757 N N . TYR A 97 ? 0.8358 0.7625 0.7316 -0.0116 -0.0284 0.0025 97 TYR A N 758 C CA . TYR A 97 ? 0.8186 0.7547 0.7233 -0.0146 -0.0333 -0.0020 97 TYR A CA 759 C C . TYR A 97 ? 0.7639 0.6998 0.6713 -0.0128 -0.0348 -0.0025 97 TYR A C 760 O O . TYR A 97 ? 0.7606 0.6892 0.6698 -0.0138 -0.0310 -0.0033 97 TYR A O 761 C CB . TYR A 97 ? 0.7983 0.7347 0.7110 -0.0203 -0.0311 -0.0066 97 TYR A CB 762 C CG . TYR A 97 ? 0.8105 0.7474 0.7215 -0.0224 -0.0293 -0.0064 97 TYR A CG 763 C CD1 . TYR A 97 ? 0.8405 0.7682 0.7468 -0.0225 -0.0228 -0.0039 97 TYR A CD1 764 C CD2 . TYR A 97 ? 0.8195 0.7651 0.7329 -0.0239 -0.0332 -0.0085 97 TYR A CD2 765 C CE1 . TYR A 97 ? 0.8570 0.7844 0.7609 -0.0240 -0.0207 -0.0035 97 TYR A CE1 766 C CE2 . TYR A 97 ? 0.8060 0.7516 0.7172 -0.0256 -0.0313 -0.0082 97 TYR A CE2 767 C CZ . TYR A 97 ? 0.8367 0.7734 0.7431 -0.0256 -0.0251 -0.0057 97 TYR A CZ 768 O OH . TYR A 97 ? 0.8638 0.7994 0.7673 -0.0270 -0.0226 -0.0053 97 TYR A OH 769 N N . LEU A 98 ? 0.7576 0.7009 0.6654 -0.0102 -0.0398 -0.0022 98 LEU A N 770 C CA . LEU A 98 ? 0.8107 0.7533 0.7198 -0.0074 -0.0409 -0.0018 98 LEU A CA 771 C C . LEU A 98 ? 0.8030 0.7518 0.7184 -0.0090 -0.0441 -0.0056 98 LEU A C 772 O O . LEU A 98 ? 0.9131 0.8698 0.8303 -0.0090 -0.0475 -0.0063 98 LEU A O 773 C CB . LEU A 98 ? 0.8208 0.7661 0.7252 -0.0018 -0.0432 0.0022 98 LEU A CB 774 C CG . LEU A 98 ? 0.8305 0.7735 0.7353 0.0018 -0.0430 0.0036 98 LEU A CG 775 C CD1 . LEU A 98 ? 0.8327 0.7636 0.7344 0.0023 -0.0375 0.0050 98 LEU A CD1 776 C CD2 . LEU A 98 ? 0.8121 0.7604 0.7140 0.0075 -0.0461 0.0069 98 LEU A CD2 777 N N . GLU A 99 ? 0.7407 0.6854 0.6591 -0.0101 -0.0428 -0.0082 99 GLU A N 778 C CA . GLU A 99 ? 0.7300 0.6791 0.6523 -0.0104 -0.0457 -0.0116 99 GLU A CA 779 C C . GLU A 99 ? 0.7070 0.6576 0.6281 -0.0061 -0.0471 -0.0094 99 GLU A C 780 O O . GLU A 99 ? 0.7018 0.6467 0.6209 -0.0036 -0.0453 -0.0078 99 GLU A O 781 C CB . GLU A 99 ? 0.7195 0.6642 0.6449 -0.0127 -0.0445 -0.0161 99 GLU A CB 782 C CG . GLU A 99 ? 0.7145 0.6603 0.6439 -0.0171 -0.0437 -0.0194 99 GLU A CG 783 C CD . GLU A 99 ? 0.7349 0.6793 0.6690 -0.0192 -0.0440 -0.0252 99 GLU A CD 784 O OE1 . GLU A 99 ? 0.7459 0.6833 0.6801 -0.0193 -0.0415 -0.0262 99 GLU A OE1 785 O OE2 . GLU A 99 ? 0.7178 0.6680 0.6554 -0.0205 -0.0468 -0.0291 99 GLU A OE2 786 N N . SER A 100 ? 0.6944 0.6524 0.6173 -0.0053 -0.0497 -0.0095 100 SER A N 787 C CA . SER A 100 ? 0.7003 0.6611 0.6237 -0.0014 -0.0506 -0.0074 100 SER A CA 788 C C . SER A 100 ? 0.6955 0.6625 0.6224 -0.0017 -0.0521 -0.0093 100 SER A C 789 O O . SER A 100 ? 0.7135 0.6838 0.6415 -0.0045 -0.0529 -0.0113 100 SER A O 790 C CB . SER A 100 ? 0.7148 0.6782 0.6363 0.0008 -0.0513 -0.0037 100 SER A CB 791 O OG . SER A 100 ? 0.7274 0.6994 0.6525 0.0023 -0.0537 -0.0035 100 SER A OG 792 N N . PRO A 101 ? 0.7238 0.6915 0.6523 0.0012 -0.0517 -0.0086 101 PRO A N 793 C CA . PRO A 101 ? 0.7532 0.7170 0.6806 0.0049 -0.0504 -0.0063 101 PRO A CA 794 C C . PRO A 101 ? 0.7757 0.7311 0.6999 0.0053 -0.0488 -0.0079 101 PRO A C 795 O O . PRO A 101 ? 0.7882 0.7417 0.7116 0.0026 -0.0492 -0.0112 101 PRO A O 796 C CB . PRO A 101 ? 0.7262 0.6952 0.6580 0.0073 -0.0502 -0.0059 101 PRO A CB 797 C CG . PRO A 101 ? 0.7375 0.7080 0.6702 0.0051 -0.0500 -0.0088 101 PRO A CG 798 C CD . PRO A 101 ? 0.7477 0.7201 0.6794 0.0013 -0.0517 -0.0101 101 PRO A CD 799 N N . ALA A 102 ? 0.8078 0.7583 0.7304 0.0086 -0.0471 -0.0060 102 ALA A N 800 C CA . ALA A 102 ? 0.8135 0.7555 0.7328 0.0093 -0.0454 -0.0081 102 ALA A CA 801 C C . ALA A 102 ? 0.8146 0.7565 0.7332 0.0084 -0.0465 -0.0123 102 ALA A C 802 O O . ALA A 102 ? 0.8403 0.7852 0.7596 0.0103 -0.0464 -0.0122 102 ALA A O 803 C CB . ALA A 102 ? 0.8250 0.7634 0.7433 0.0139 -0.0433 -0.0054 102 ALA A CB 804 N N . GLY A 103 ? 0.8213 0.7594 0.7385 0.0058 -0.0471 -0.0161 103 GLY A N 805 C CA . GLY A 103 ? 0.8723 0.8102 0.7879 0.0058 -0.0488 -0.0207 103 GLY A CA 806 C C . GLY A 103 ? 0.9175 0.8606 0.8357 0.0023 -0.0511 -0.0236 103 GLY A C 807 O O . GLY A 103 ? 0.9090 0.8518 0.8263 0.0019 -0.0531 -0.0282 103 GLY A O 808 N N . VAL A 104 ? 0.8917 0.8399 0.8128 0.0001 -0.0511 -0.0209 104 VAL A N 809 C CA . VAL A 104 ? 0.8369 0.7897 0.7606 -0.0033 -0.0525 -0.0230 104 VAL A CA 810 C C . VAL A 104 ? 0.8376 0.7873 0.7634 -0.0068 -0.0520 -0.0257 104 VAL A C 811 O O . VAL A 104 ? 0.8153 0.7602 0.7408 -0.0074 -0.0496 -0.0237 104 VAL A O 812 C CB . VAL A 104 ? 0.8147 0.7728 0.7402 -0.0045 -0.0523 -0.0195 104 VAL A CB 813 C CG1 . VAL A 104 ? 0.8204 0.7822 0.7480 -0.0081 -0.0531 -0.0214 104 VAL A CG1 814 C CG2 . VAL A 104 ? 0.8137 0.7754 0.7393 -0.0018 -0.0522 -0.0178 104 VAL A CG2 815 N N . GLY A 105 ? 0.8080 0.7604 0.7363 -0.0089 -0.0538 -0.0302 105 GLY A N 816 C CA . GLY A 105 ? 0.7967 0.7474 0.7294 -0.0129 -0.0530 -0.0338 105 GLY A CA 817 C C . GLY A 105 ? 0.8254 0.7689 0.7580 -0.0130 -0.0515 -0.0361 105 GLY A C 818 O O . GLY A 105 ? 0.8072 0.7492 0.7378 -0.0107 -0.0534 -0.0395 105 GLY A O 819 N N . PHE A 106 ? 0.8506 0.7888 0.7846 -0.0155 -0.0475 -0.0342 106 PHE A N 820 C CA . PHE A 106 ? 0.8524 0.7821 0.7862 -0.0159 -0.0445 -0.0359 106 PHE A CA 821 C C . PHE A 106 ? 0.8397 0.7638 0.7674 -0.0119 -0.0422 -0.0299 106 PHE A C 822 O O . PHE A 106 ? 0.8373 0.7532 0.7637 -0.0116 -0.0390 -0.0302 106 PHE A O 823 C CB . PHE A 106 ? 0.8615 0.7870 0.8004 -0.0207 -0.0401 -0.0374 106 PHE A CB 824 C CG . PHE A 106 ? 0.8872 0.8177 0.8343 -0.0249 -0.0418 -0.0445 106 PHE A CG 825 C CD1 . PHE A 106 ? 0.9284 0.8617 0.8782 -0.0247 -0.0459 -0.0516 106 PHE A CD1 826 C CD2 . PHE A 106 ? 0.9145 0.8470 0.8667 -0.0287 -0.0393 -0.0443 106 PHE A CD2 827 C CE1 . PHE A 106 ? 0.9378 0.8771 0.8962 -0.0281 -0.0482 -0.0588 106 PHE A CE1 828 C CE2 . PHE A 106 ? 0.9635 0.9015 0.9248 -0.0325 -0.0407 -0.0512 106 PHE A CE2 829 C CZ . PHE A 106 ? 0.9352 0.8773 0.9001 -0.0322 -0.0455 -0.0586 106 PHE A CZ 830 N N . SER A 107 ? 0.7951 0.7238 0.7198 -0.0089 -0.0436 -0.0249 107 SER A N 831 C CA . SER A 107 ? 0.7862 0.7116 0.7067 -0.0047 -0.0419 -0.0197 107 SER A CA 832 C C . SER A 107 ? 0.8113 0.7349 0.7294 -0.0013 -0.0431 -0.0213 107 SER A C 833 O O . SER A 107 ? 0.7537 0.6815 0.6720 -0.0009 -0.0462 -0.0244 107 SER A O 834 C CB . SER A 107 ? 0.7875 0.7196 0.7072 -0.0029 -0.0433 -0.0149 107 SER A CB 835 O OG . SER A 107 ? 0.7940 0.7266 0.7141 -0.0052 -0.0419 -0.0131 107 SER A OG 836 N N . TYR A 108 ? 0.8844 0.8013 0.7995 0.0015 -0.0403 -0.0188 108 TYR A N 837 C CA . TYR A 108 ? 0.9465 0.8601 0.8585 0.0051 -0.0405 -0.0198 108 TYR A CA 838 C C . TYR A 108 ? 1.0121 0.9224 0.9216 0.0096 -0.0377 -0.0141 108 TYR A C 839 O O . TYR A 108 ? 1.0356 0.9466 0.9454 0.0104 -0.0363 -0.0096 108 TYR A O 840 C CB . TYR A 108 ? 0.9573 0.8635 0.8685 0.0033 -0.0396 -0.0256 108 TYR A CB 841 C CG . TYR A 108 ? 0.9690 0.8662 0.8801 0.0020 -0.0348 -0.0245 108 TYR A CG 842 C CD1 . TYR A 108 ? 0.9639 0.8603 0.8785 -0.0021 -0.0326 -0.0247 108 TYR A CD1 843 C CD2 . TYR A 108 ? 1.0322 0.9207 0.9394 0.0051 -0.0315 -0.0231 108 TYR A CD2 844 C CE1 . TYR A 108 ? 0.9621 0.8487 0.8761 -0.0031 -0.0269 -0.0234 108 TYR A CE1 845 C CE2 . TYR A 108 ? 1.0596 0.9386 0.9662 0.0042 -0.0261 -0.0219 108 TYR A CE2 846 C CZ . TYR A 108 ? 1.0078 0.8856 0.9176 0.0000 -0.0237 -0.0220 108 TYR A CZ 847 O OH . TYR A 108 ? 1.0856 0.9526 0.9943 -0.0005 -0.0172 -0.0205 108 TYR A OH 848 N N . SER A 109 ? 1.0586 0.9655 0.9652 0.0132 -0.0371 -0.0145 109 SER A N 849 C CA . SER A 109 ? 1.1019 1.0039 1.0064 0.0177 -0.0338 -0.0101 109 SER A CA 850 C C . SER A 109 ? 1.0908 0.9830 0.9908 0.0190 -0.0318 -0.0134 109 SER A C 851 O O . SER A 109 ? 1.0812 0.9727 0.9796 0.0178 -0.0339 -0.0188 109 SER A O 852 C CB . SER A 109 ? 1.1412 1.0502 1.0474 0.0215 -0.0346 -0.0064 109 SER A CB 853 O OG . SER A 109 ? 1.2449 1.1534 1.1491 0.0230 -0.0353 -0.0092 109 SER A OG 854 N N . ASP A 110 ? 1.1502 1.0347 1.0478 0.0219 -0.0277 -0.0103 110 ASP A N 855 C CA . ASP A 110 ? 1.1769 1.0509 1.0698 0.0233 -0.0251 -0.0134 110 ASP A CA 856 C C . ASP A 110 ? 1.1812 1.0559 1.0708 0.0267 -0.0265 -0.0150 110 ASP A C 857 O O . ASP A 110 ? 1.2142 1.0837 1.0996 0.0263 -0.0274 -0.0207 110 ASP A O 858 C CB . ASP A 110 ? 1.1947 1.0605 1.0853 0.0269 -0.0198 -0.0086 110 ASP A CB 859 C CG . ASP A 110 ? 1.2540 1.1147 1.1453 0.0241 -0.0168 -0.0075 110 ASP A CG 860 O OD1 . ASP A 110 ? 1.3126 1.1747 1.2066 0.0187 -0.0182 -0.0117 110 ASP A OD1 861 O OD2 . ASP A 110 ? 1.2692 1.1242 1.1583 0.0278 -0.0124 -0.0023 110 ASP A OD2 862 N N . ASP A 111 ? 1.1484 1.0295 1.0400 0.0302 -0.0265 -0.0104 111 ASP A N 863 C CA . ASP A 111 ? 1.1477 1.0285 1.0361 0.0339 -0.0264 -0.0111 111 ASP A CA 864 C C . ASP A 111 ? 1.1461 1.0330 1.0342 0.0322 -0.0303 -0.0147 111 ASP A C 865 O O . ASP A 111 ? 1.1933 1.0782 1.0769 0.0355 -0.0298 -0.0158 111 ASP A O 866 C CB . ASP A 111 ? 1.1970 1.0816 1.0889 0.0384 -0.0236 -0.0051 111 ASP A CB 867 C CG . ASP A 111 ? 1.2082 1.1050 1.1079 0.0369 -0.0259 -0.0020 111 ASP A CG 868 O OD1 . ASP A 111 ? 1.2596 1.1601 1.1615 0.0330 -0.0284 -0.0026 111 ASP A OD1 869 O OD2 . ASP A 111 ? 1.1917 1.0942 1.0958 0.0396 -0.0247 0.0006 111 ASP A OD2 870 N N . LYS A 112 ? 1.1585 1.0519 1.0507 0.0276 -0.0336 -0.0162 112 LYS A N 871 C CA . LYS A 112 ? 1.1734 1.0726 1.0655 0.0261 -0.0372 -0.0195 112 LYS A CA 872 C C . LYS A 112 ? 1.1610 1.0657 1.0542 0.0289 -0.0364 -0.0166 112 LYS A C 873 O O . LYS A 112 ? 1.1653 1.0721 1.0561 0.0293 -0.0383 -0.0191 112 LYS A O 874 C CB . LYS A 112 ? 1.2305 1.1243 1.1161 0.0267 -0.0393 -0.0261 112 LYS A CB 875 C CG . LYS A 112 ? 1.2906 1.1794 1.1766 0.0230 -0.0401 -0.0310 112 LYS A CG 876 C CD . LYS A 112 ? 1.3297 1.2219 1.2158 0.0204 -0.0450 -0.0381 112 LYS A CD 877 C CE . LYS A 112 ? 1.3486 1.2389 1.2264 0.0252 -0.0475 -0.0420 112 LYS A CE 878 N NZ . LYS A 112 ? 1.3644 1.2460 1.2363 0.0266 -0.0477 -0.0476 112 LYS A NZ 879 N N . PHE A 113 ? 1.0966 1.0035 0.9938 0.0311 -0.0335 -0.0115 113 PHE A N 880 C CA . PHE A 113 ? 1.0838 0.9964 0.9844 0.0330 -0.0320 -0.0093 113 PHE A CA 881 C C . PHE A 113 ? 0.9949 0.9176 0.9027 0.0289 -0.0346 -0.0084 113 PHE A C 882 O O . PHE A 113 ? 0.9873 0.9142 0.9001 0.0277 -0.0351 -0.0057 113 PHE A O 883 C CB . PHE A 113 ? 1.1709 1.0824 1.0744 0.0371 -0.0275 -0.0051 113 PHE A CB 884 C CG . PHE A 113 ? 1.1917 1.1078 1.0997 0.0389 -0.0246 -0.0035 113 PHE A CG 885 C CD1 . PHE A 113 ? 1.2215 1.1328 1.1232 0.0412 -0.0226 -0.0052 113 PHE A CD1 886 C CD2 . PHE A 113 ? 1.2093 1.1342 1.1277 0.0387 -0.0235 -0.0004 113 PHE A CD2 887 C CE1 . PHE A 113 ? 1.2480 1.1620 1.1540 0.0427 -0.0184 -0.0036 113 PHE A CE1 888 C CE2 . PHE A 113 ? 1.2290 1.1580 1.1533 0.0397 -0.0200 0.0003 113 PHE A CE2 889 C CZ . PHE A 113 ? 1.2386 1.1616 1.1567 0.0415 -0.0168 -0.0010 113 PHE A CZ 890 N N . TYR A 114 ? 0.9676 0.8938 0.8750 0.0272 -0.0362 -0.0106 114 TYR A N 891 C CA . TYR A 114 ? 0.9064 0.8412 0.8195 0.0229 -0.0389 -0.0105 114 TYR A CA 892 C C . TYR A 114 ? 0.8818 0.8235 0.8005 0.0229 -0.0373 -0.0090 114 TYR A C 893 O O . TYR A 114 ? 0.9537 0.9023 0.8767 0.0194 -0.0393 -0.0093 114 TYR A O 894 C CB . TYR A 114 ? 0.8784 0.8127 0.7880 0.0201 -0.0422 -0.0146 114 TYR A CB 895 C CG . TYR A 114 ? 0.8717 0.8009 0.7787 0.0185 -0.0437 -0.0170 114 TYR A CG 896 C CD1 . TYR A 114 ? 0.8493 0.7779 0.7590 0.0170 -0.0431 -0.0147 114 TYR A CD1 897 C CD2 . TYR A 114 ? 0.9208 0.8458 0.8228 0.0186 -0.0456 -0.0219 114 TYR A CD2 898 C CE1 . TYR A 114 ? 0.8650 0.7877 0.7728 0.0151 -0.0431 -0.0170 114 TYR A CE1 899 C CE2 . TYR A 114 ? 0.9129 0.8336 0.8144 0.0164 -0.0466 -0.0250 114 TYR A CE2 900 C CZ . TYR A 114 ? 0.8704 0.7894 0.7750 0.0143 -0.0448 -0.0224 114 TYR A CZ 901 O OH . TYR A 114 ? 0.8697 0.7833 0.7743 0.0119 -0.0444 -0.0255 114 TYR A OH 902 N N . ALA A 115 ? 0.8947 0.8340 0.8137 0.0265 -0.0332 -0.0076 115 ALA A N 903 C CA . ALA A 115 ? 0.8227 0.7687 0.7497 0.0261 -0.0305 -0.0064 115 ALA A CA 904 C C . ALA A 115 ? 0.7943 0.7487 0.7301 0.0245 -0.0324 -0.0045 115 ALA A C 905 O O . ALA A 115 ? 0.7756 0.7282 0.7112 0.0265 -0.0326 -0.0026 115 ALA A O 906 C CB . ALA A 115 ? 0.8165 0.7576 0.7431 0.0305 -0.0246 -0.0051 115 ALA A CB 907 N N . THR A 116 ? 0.7561 0.7194 0.6989 0.0212 -0.0338 -0.0052 116 THR A N 908 C CA . THR A 116 ? 0.7546 0.7268 0.7047 0.0200 -0.0366 -0.0041 116 THR A CA 909 C C . THR A 116 ? 0.7899 0.7716 0.7491 0.0172 -0.0364 -0.0057 116 THR A C 910 O O . THR A 116 ? 0.7932 0.7732 0.7533 0.0165 -0.0328 -0.0071 116 THR A O 911 C CB . THR A 116 ? 0.7571 0.7285 0.7020 0.0181 -0.0411 -0.0038 116 THR A CB 912 O OG1 . THR A 116 ? 0.8346 0.8126 0.7840 0.0190 -0.0435 -0.0019 116 THR A OG1 913 C CG2 . THR A 116 ? 0.7357 0.7087 0.6785 0.0139 -0.0432 -0.0061 116 THR A CG2 914 N N . ASN A 117 ? 0.8294 0.8205 0.7950 0.0160 -0.0400 -0.0056 117 ASN A N 915 C CA . ASN A 117 ? 0.8532 0.8542 0.8285 0.0131 -0.0404 -0.0081 117 ASN A CA 916 C C . ASN A 117 ? 0.8164 0.8261 0.7936 0.0118 -0.0463 -0.0085 117 ASN A C 917 O O . ASN A 117 ? 0.8311 0.8389 0.8028 0.0141 -0.0492 -0.0062 117 ASN A O 918 C CB . ASN A 117 ? 0.8813 0.8869 0.8677 0.0149 -0.0362 -0.0085 117 ASN A CB 919 C CG . ASN A 117 ? 0.9346 0.9456 0.9262 0.0187 -0.0383 -0.0067 117 ASN A CG 920 O OD1 . ASN A 117 ? 0.9419 0.9592 0.9335 0.0191 -0.0438 -0.0063 117 ASN A OD1 921 N ND2 . ASN A 117 ? 0.9262 0.9344 0.9216 0.0222 -0.0335 -0.0053 117 ASN A ND2 922 N N . ASP A 118 ? 0.7606 0.7789 0.7449 0.0085 -0.0475 -0.0116 118 ASP A N 923 C CA . ASP A 118 ? 0.7597 0.7854 0.7437 0.0071 -0.0532 -0.0127 118 ASP A CA 924 C C . ASP A 118 ? 0.7747 0.8052 0.7591 0.0117 -0.0573 -0.0105 118 ASP A C 925 O O . ASP A 118 ? 0.7494 0.7782 0.7256 0.0128 -0.0609 -0.0087 118 ASP A O 926 C CB . ASP A 118 ? 0.7547 0.7902 0.7487 0.0034 -0.0537 -0.0172 118 ASP A CB 927 C CG . ASP A 118 ? 0.7542 0.7846 0.7464 -0.0007 -0.0497 -0.0191 118 ASP A CG 928 O OD1 . ASP A 118 ? 0.7176 0.7400 0.6996 -0.0015 -0.0496 -0.0176 118 ASP A OD1 929 O OD2 . ASP A 118 ? 0.8073 0.8421 0.8092 -0.0032 -0.0464 -0.0223 118 ASP A OD2 930 N N . THR A 119 ? 0.8003 0.8361 0.7938 0.0149 -0.0562 -0.0103 119 THR A N 931 C CA . THR A 119 ? 0.8146 0.8558 0.8092 0.0202 -0.0600 -0.0082 119 THR A CA 932 C C . THR A 119 ? 0.8043 0.8338 0.7869 0.0239 -0.0589 -0.0033 119 THR A C 933 O O . THR A 119 ? 0.7972 0.8271 0.7740 0.0275 -0.0623 -0.0009 119 THR A O 934 C CB . THR A 119 ? 0.8468 0.8971 0.8556 0.0230 -0.0586 -0.0094 119 THR A CB 935 O OG1 . THR A 119 ? 0.8511 0.8936 0.8619 0.0227 -0.0516 -0.0085 119 THR A OG1 936 C CG2 . THR A 119 ? 0.8454 0.9100 0.8679 0.0198 -0.0610 -0.0151 119 THR A CG2 937 N N . GLU A 120 ? 0.7810 0.7999 0.7596 0.0232 -0.0540 -0.0021 120 GLU A N 938 C CA . GLU A 120 ? 0.7861 0.7936 0.7543 0.0260 -0.0525 0.0015 120 GLU A CA 939 C C . GLU A 120 ? 0.8052 0.8067 0.7631 0.0235 -0.0544 0.0019 120 GLU A C 940 O O . GLU A 120 ? 0.8099 0.8056 0.7604 0.0263 -0.0548 0.0048 120 GLU A O 941 C CB . GLU A 120 ? 0.7827 0.7805 0.7488 0.0262 -0.0472 0.0018 120 GLU A CB 942 C CG . GLU A 120 ? 0.7955 0.7826 0.7528 0.0296 -0.0457 0.0050 120 GLU A CG 943 C CD . GLU A 120 ? 0.8317 0.8092 0.7859 0.0305 -0.0409 0.0050 120 GLU A CD 944 O OE1 . GLU A 120 ? 0.8187 0.7942 0.7727 0.0278 -0.0392 0.0025 120 GLU A OE1 945 O OE2 . GLU A 120 ? 0.8825 0.8535 0.8335 0.0345 -0.0388 0.0074 120 GLU A OE2 946 N N . VAL A 121 ? 0.8175 0.8197 0.7751 0.0185 -0.0547 -0.0008 121 VAL A N 947 C CA . VAL A 121 ? 0.8126 0.8097 0.7618 0.0158 -0.0560 -0.0008 121 VAL A CA 948 C C . VAL A 121 ? 0.8262 0.8282 0.7730 0.0175 -0.0598 0.0003 121 VAL A C 949 O O . VAL A 121 ? 0.8587 0.8540 0.7972 0.0183 -0.0597 0.0026 121 VAL A O 950 C CB . VAL A 121 ? 0.7856 0.7829 0.7354 0.0107 -0.0555 -0.0040 121 VAL A CB 951 C CG1 . VAL A 121 ? 0.7768 0.7705 0.7196 0.0080 -0.0568 -0.0040 121 VAL A CG1 952 C CG2 . VAL A 121 ? 0.7925 0.7830 0.7414 0.0103 -0.0517 -0.0049 121 VAL A CG2 953 N N . ALA A 122 ? 0.8398 0.8533 0.7940 0.0182 -0.0630 -0.0013 122 ALA A N 954 C CA . ALA A 122 ? 0.8443 0.8638 0.7957 0.0210 -0.0675 -0.0006 122 ALA A CA 955 C C . ALA A 122 ? 0.8552 0.8694 0.7999 0.0273 -0.0673 0.0040 122 ALA A C 956 O O . ALA A 122 ? 0.8344 0.8426 0.7691 0.0290 -0.0676 0.0066 122 ALA A O 957 C CB . ALA A 122 ? 0.8241 0.8580 0.7863 0.0214 -0.0712 -0.0041 122 ALA A CB 958 N N . GLN A 123 ? 0.8729 0.8883 0.8231 0.0309 -0.0659 0.0053 123 GLN A N 959 C CA . GLN A 123 ? 0.8708 0.8806 0.8153 0.0375 -0.0649 0.0099 123 GLN A CA 960 C C . GLN A 123 ? 0.8603 0.8547 0.7939 0.0366 -0.0605 0.0127 123 GLN A C 961 O O . GLN A 123 ? 0.8847 0.8726 0.8097 0.0409 -0.0597 0.0165 123 GLN A O 962 C CB . GLN A 123 ? 0.8853 0.8980 0.8385 0.0405 -0.0628 0.0103 123 GLN A CB 963 C CG . GLN A 123 ? 0.9258 0.9338 0.8745 0.0479 -0.0616 0.0151 123 GLN A CG 964 C CD . GLN A 123 ? 0.9113 0.9276 0.8580 0.0541 -0.0668 0.0167 123 GLN A CD 965 O OE1 . GLN A 123 ? 0.8593 0.8896 0.8141 0.0540 -0.0718 0.0133 123 GLN A OE1 966 N NE2 . GLN A 123 ? 0.9348 0.9420 0.8703 0.0598 -0.0653 0.0216 123 GLN A NE2 967 N N . SER A 124 ? 0.8606 0.8487 0.7945 0.0312 -0.0575 0.0106 124 SER A N 968 C CA . SER A 124 ? 0.8680 0.8427 0.7939 0.0294 -0.0535 0.0117 124 SER A CA 969 C C . SER A 124 ? 0.8874 0.8583 0.8057 0.0278 -0.0540 0.0125 124 SER A C 970 O O . SER A 124 ? 0.8768 0.8377 0.7875 0.0298 -0.0509 0.0154 124 SER A O 971 C CB . SER A 124 ? 0.8608 0.8324 0.7895 0.0244 -0.0516 0.0082 124 SER A CB 972 O OG . SER A 124 ? 0.8487 0.8085 0.7714 0.0229 -0.0482 0.0083 124 SER A OG 973 N N . ASN A 125 ? 0.8796 0.8577 0.8000 0.0242 -0.0570 0.0098 125 ASN A N 974 C CA . ASN A 125 ? 0.8677 0.8429 0.7810 0.0229 -0.0573 0.0105 125 ASN A CA 975 C C . ASN A 125 ? 0.8506 0.8257 0.7568 0.0296 -0.0586 0.0145 125 ASN A C 976 O O . ASN A 125 ? 0.7679 0.7336 0.6649 0.0308 -0.0557 0.0172 125 ASN A O 977 C CB . ASN A 125 ? 0.8740 0.8582 0.7911 0.0187 -0.0606 0.0068 125 ASN A CB 978 C CG . ASN A 125 ? 0.8727 0.8554 0.7940 0.0126 -0.0590 0.0034 125 ASN A CG 979 O OD1 . ASN A 125 ? 0.9180 0.9085 0.8458 0.0101 -0.0607 0.0003 125 ASN A OD1 980 N ND2 . ASN A 125 ? 0.8541 0.8272 0.7719 0.0104 -0.0555 0.0035 125 ASN A ND2 981 N N . PHE A 126 ? 0.8426 0.8280 0.7532 0.0342 -0.0628 0.0147 126 PHE A N 982 C CA . PHE A 126 ? 0.8812 0.8680 0.7852 0.0419 -0.0650 0.0183 126 PHE A CA 983 C C . PHE A 126 ? 0.8841 0.8578 0.7800 0.0467 -0.0598 0.0234 126 PHE A C 984 O O . PHE A 126 ? 0.9077 0.8739 0.7925 0.0508 -0.0581 0.0270 126 PHE A O 985 C CB . PHE A 126 ? 0.9049 0.9062 0.8177 0.0461 -0.0703 0.0168 126 PHE A CB 986 C CG . PHE A 126 ? 0.9860 0.9894 0.8920 0.0555 -0.0731 0.0205 126 PHE A CG 987 C CD1 . PHE A 126 ? 0.9877 0.9906 0.8832 0.0584 -0.0757 0.0215 126 PHE A CD1 988 C CD2 . PHE A 126 ? 1.0287 1.0332 0.9373 0.0621 -0.0726 0.0234 126 PHE A CD2 989 C CE1 . PHE A 126 ? 0.9945 0.9987 0.8817 0.0682 -0.0784 0.0252 126 PHE A CE1 990 C CE2 . PHE A 126 ? 1.0504 1.0566 0.9517 0.0717 -0.0753 0.0271 126 PHE A CE2 991 C CZ . PHE A 126 ? 1.0258 1.0319 0.9159 0.0751 -0.0783 0.0280 126 PHE A CZ 992 N N . GLU A 127 ? 0.9089 0.8786 0.8096 0.0462 -0.0566 0.0236 127 GLU A N 993 C CA . GLU A 127 ? 0.9195 0.8759 0.8133 0.0502 -0.0510 0.0279 127 GLU A CA 994 C C . GLU A 127 ? 0.9539 0.8961 0.8405 0.0458 -0.0453 0.0283 127 GLU A C 995 O O . GLU A 127 ? 0.9904 0.9210 0.8680 0.0497 -0.0405 0.0324 127 GLU A O 996 C CB . GLU A 127 ? 0.8941 0.8498 0.7949 0.0504 -0.0489 0.0274 127 GLU A CB 997 C CG . GLU A 127 ? 0.8917 0.8595 0.7998 0.0563 -0.0528 0.0281 127 GLU A CG 998 C CD . GLU A 127 ? 0.8772 0.8405 0.7890 0.0586 -0.0491 0.0293 127 GLU A CD 999 O OE1 . GLU A 127 ? 0.8520 0.8012 0.7565 0.0596 -0.0436 0.0318 127 GLU A OE1 1000 O OE2 . GLU A 127 ? 0.8606 0.8338 0.7827 0.0594 -0.0511 0.0275 127 GLU A OE2 1001 N N . ALA A 128 ? 0.9610 0.9040 0.8520 0.0379 -0.0453 0.0239 128 ALA A N 1002 C CA . ALA A 128 ? 0.9487 0.8807 0.8351 0.0330 -0.0405 0.0232 128 ALA A CA 1003 C C . ALA A 128 ? 0.9899 0.9187 0.8672 0.0351 -0.0397 0.0259 128 ALA A C 1004 O O . ALA A 128 ? 0.9976 0.9137 0.8681 0.0349 -0.0336 0.0280 128 ALA A O 1005 C CB . ALA A 128 ? 0.9243 0.8606 0.8180 0.0251 -0.0420 0.0177 128 ALA A CB 1006 N N . LEU A 129 ? 0.9858 0.9257 0.8630 0.0371 -0.0456 0.0255 129 LEU A N 1007 C CA . LEU A 129 ? 0.9806 0.9182 0.8477 0.0403 -0.0456 0.0281 129 LEU A CA 1008 C C . LEU A 129 ? 1.0253 0.9545 0.8820 0.0496 -0.0427 0.0342 129 LEU A C 1009 O O . LEU A 129 ? 1.0137 0.9310 0.8595 0.0519 -0.0374 0.0377 129 LEU A O 1010 C CB . LEU A 129 ? 0.9746 0.9270 0.8445 0.0407 -0.0533 0.0255 129 LEU A CB 1011 C CG . LEU A 129 ? 0.9788 0.9313 0.8417 0.0395 -0.0543 0.0249 129 LEU A CG 1012 C CD1 . LEU A 129 ? 0.9929 0.9391 0.8578 0.0312 -0.0499 0.0224 129 LEU A CD1 1013 C CD2 . LEU A 129 ? 0.9612 0.9297 0.8294 0.0395 -0.0624 0.0211 129 LEU A CD2 1014 N N . GLN A 130 ? 1.0394 0.9741 0.8992 0.0552 -0.0454 0.0356 130 GLN A N 1015 C CA . GLN A 130 ? 1.0778 1.0037 0.9283 0.0644 -0.0418 0.0416 130 GLN A CA 1016 C C . GLN A 130 ? 1.0879 0.9950 0.9332 0.0623 -0.0319 0.0439 130 GLN A C 1017 O O . GLN A 130 ? 1.1810 1.0758 1.0145 0.0669 -0.0263 0.0485 130 GLN A O 1018 C CB . GLN A 130 ? 1.1025 1.0373 0.9601 0.0695 -0.0455 0.0421 130 GLN A CB 1019 C CG . GLN A 130 ? 1.1251 1.0776 0.9865 0.0741 -0.0546 0.0406 130 GLN A CG 1020 C CD . GLN A 130 ? 1.1397 1.0993 1.0059 0.0818 -0.0572 0.0425 130 GLN A CD 1021 O OE1 . GLN A 130 ? 1.1292 1.0873 1.0031 0.0798 -0.0545 0.0420 130 GLN A OE1 1022 N NE2 . GLN A 130 ? 1.2096 1.1778 1.0714 0.0908 -0.0627 0.0443 130 GLN A NE2 1023 N N . ASP A 131 ? 1.0921 0.9968 0.9465 0.0554 -0.0295 0.0404 131 ASP A N 1024 C CA . ASP A 131 ? 1.0961 0.9843 0.9480 0.0523 -0.0205 0.0409 131 ASP A CA 1025 C C . ASP A 131 ? 1.0574 0.9364 0.9039 0.0481 -0.0154 0.0408 131 ASP A C 1026 O O . ASP A 131 ? 1.0926 0.9562 0.9338 0.0481 -0.0067 0.0429 131 ASP A O 1027 C CB . ASP A 131 ? 1.0905 0.9798 0.9534 0.0449 -0.0203 0.0356 131 ASP A CB 1028 C CG . ASP A 131 ? 1.1112 0.9843 0.9723 0.0431 -0.0116 0.0357 131 ASP A CG 1029 O OD1 . ASP A 131 ? 1.1406 1.0040 0.9944 0.0499 -0.0069 0.0407 131 ASP A OD1 1030 O OD2 . ASP A 131 ? 1.1112 0.9812 0.9784 0.0352 -0.0096 0.0305 131 ASP A OD2 1031 N N . PHE A 132 ? 1.0329 0.9211 0.8815 0.0444 -0.0201 0.0380 132 PHE A N 1032 C CA . PHE A 132 ? 1.0188 0.8991 0.8627 0.0407 -0.0153 0.0379 132 PHE A CA 1033 C C . PHE A 132 ? 0.9951 0.8636 0.8240 0.0487 -0.0098 0.0445 132 PHE A C 1034 O O . PHE A 132 ? 0.9872 0.8406 0.8113 0.0472 -0.0005 0.0461 132 PHE A O 1035 C CB . PHE A 132 ? 0.9921 0.8848 0.8396 0.0367 -0.0217 0.0344 132 PHE A CB 1036 C CG . PHE A 132 ? 1.0084 0.8935 0.8505 0.0338 -0.0167 0.0347 132 PHE A CG 1037 C CD1 . PHE A 132 ? 1.0004 0.8786 0.8490 0.0257 -0.0109 0.0312 132 PHE A CD1 1038 C CD2 . PHE A 132 ? 1.0429 0.9281 0.8737 0.0391 -0.0181 0.0380 132 PHE A CD2 1039 C CE1 . PHE A 132 ? 1.0205 0.8920 0.8654 0.0228 -0.0057 0.0314 132 PHE A CE1 1040 C CE2 . PHE A 132 ? 1.0235 0.9011 0.8490 0.0366 -0.0129 0.0384 132 PHE A CE2 1041 C CZ . PHE A 132 ? 1.0353 0.9059 0.8683 0.0283 -0.0063 0.0353 132 PHE A CZ 1042 N N . PHE A 133 ? 1.0050 0.8806 0.8268 0.0575 -0.0155 0.0479 133 PHE A N 1043 C CA . PHE A 133 ? 1.0159 0.8814 0.8212 0.0669 -0.0116 0.0545 133 PHE A CA 1044 C C . PHE A 133 ? 1.0170 0.8668 0.8150 0.0731 -0.0031 0.0599 133 PHE A C 1045 O O . PHE A 133 ? 1.0022 0.8379 0.7857 0.0796 0.0039 0.0655 133 PHE A O 1046 C CB . PHE A 133 ? 0.9906 0.8699 0.7906 0.0750 -0.0213 0.0556 133 PHE A CB 1047 C CG . PHE A 133 ? 0.9578 0.8487 0.7613 0.0698 -0.0277 0.0511 133 PHE A CG 1048 C CD1 . PHE A 133 ? 0.9859 0.8681 0.7828 0.0664 -0.0227 0.0512 133 PHE A CD1 1049 C CD2 . PHE A 133 ? 0.9521 0.8621 0.7658 0.0682 -0.0380 0.0464 133 PHE A CD2 1050 C CE1 . PHE A 133 ? 0.9806 0.8730 0.7804 0.0617 -0.0282 0.0470 133 PHE A CE1 1051 C CE2 . PHE A 133 ? 0.9156 0.8355 0.7323 0.0633 -0.0433 0.0420 133 PHE A CE2 1052 C CZ . PHE A 133 ? 0.9319 0.8430 0.7413 0.0602 -0.0386 0.0424 133 PHE A CZ 1053 N N . ARG A 134 ? 1.0018 0.8528 0.8088 0.0713 -0.0030 0.0583 134 ARG A N 1054 C CA . ARG A 134 ? 1.0781 0.9125 0.8796 0.0755 0.0063 0.0626 134 ARG A CA 1055 C C . ARG A 134 ? 1.0561 0.8739 0.8577 0.0681 0.0173 0.0613 134 ARG A C 1056 O O . ARG A 134 ? 1.0755 0.8754 0.8668 0.0727 0.0276 0.0663 134 ARG A O 1057 C CB . ARG A 134 ? 1.1367 0.9758 0.9483 0.0743 0.0041 0.0605 134 ARG A CB 1058 C CG . ARG A 134 ? 1.2010 1.0558 1.0147 0.0817 -0.0053 0.0617 134 ARG A CG 1059 C CD . ARG A 134 ? 1.2595 1.1144 1.0811 0.0816 -0.0046 0.0608 134 ARG A CD 1060 N NE . ARG A 134 ? 1.2833 1.1574 1.1147 0.0829 -0.0145 0.0583 134 ARG A NE 1061 C CZ . ARG A 134 ? 1.2944 1.1764 1.1386 0.0760 -0.0176 0.0530 134 ARG A CZ 1062 N NH1 . ARG A 134 ? 1.2953 1.1692 1.1442 0.0674 -0.0129 0.0490 134 ARG A NH1 1063 N NH2 . ARG A 134 ? 1.3188 1.2170 1.1712 0.0782 -0.0253 0.0514 134 ARG A NH2 1064 N N . LEU A 135 ? 1.0161 0.8402 0.8299 0.0571 0.0153 0.0544 135 LEU A N 1065 C CA . LEU A 135 ? 1.0131 0.8249 0.8311 0.0486 0.0246 0.0513 135 LEU A CA 1066 C C . LEU A 135 ? 1.0621 0.8678 0.8721 0.0487 0.0290 0.0534 135 LEU A C 1067 O O . LEU A 135 ? 1.1624 0.9519 0.9696 0.0463 0.0403 0.0544 135 LEU A O 1068 C CB . LEU A 135 ? 0.9749 0.7972 0.8092 0.0377 0.0199 0.0428 135 LEU A CB 1069 C CG . LEU A 135 ? 0.9683 0.7947 0.8106 0.0368 0.0167 0.0400 135 LEU A CG 1070 C CD1 . LEU A 135 ? 0.9461 0.7874 0.8014 0.0291 0.0086 0.0327 135 LEU A CD1 1071 C CD2 . LEU A 135 ? 0.9746 0.7844 0.8175 0.0347 0.0269 0.0394 135 LEU A CD2 1072 N N . PHE A 136 ? 1.0387 0.8566 0.8448 0.0515 0.0207 0.0540 136 PHE A N 1073 C CA . PHE A 136 ? 1.0347 0.8473 0.8314 0.0526 0.0242 0.0563 136 PHE A CA 1074 C C . PHE A 136 ? 1.0153 0.8283 0.7951 0.0650 0.0208 0.0628 136 PHE A C 1075 O O . PHE A 136 ? 1.0025 0.8275 0.7799 0.0664 0.0126 0.0618 136 PHE A O 1076 C CB . PHE A 136 ? 1.0079 0.8347 0.8149 0.0441 0.0172 0.0500 136 PHE A CB 1077 C CG . PHE A 136 ? 0.9826 0.8073 0.8038 0.0327 0.0217 0.0438 136 PHE A CG 1078 C CD1 . PHE A 136 ? 0.9664 0.7995 0.8014 0.0268 0.0173 0.0382 136 PHE A CD1 1079 C CD2 . PHE A 136 ? 1.0095 0.8241 0.8302 0.0282 0.0304 0.0432 136 PHE A CD2 1080 C CE1 . PHE A 136 ? 0.9791 0.8115 0.8271 0.0170 0.0204 0.0319 136 PHE A CE1 1081 C CE2 . PHE A 136 ? 0.9917 0.8061 0.8270 0.0178 0.0339 0.0367 136 PHE A CE2 1082 C CZ . PHE A 136 ? 0.9602 0.7839 0.8090 0.0124 0.0284 0.0308 136 PHE A CZ 1083 N N . PRO A 137 ? 1.0643 0.8643 0.8319 0.0745 0.0269 0.0694 137 PRO A N 1084 C CA . PRO A 137 ? 1.1102 0.9116 0.8610 0.0880 0.0227 0.0756 137 PRO A CA 1085 C C . PRO A 137 ? 1.1344 0.9307 0.8708 0.0917 0.0245 0.0783 137 PRO A C 1086 O O . PRO A 137 ? 1.1051 0.9108 0.8319 0.1000 0.0159 0.0800 137 PRO A O 1087 C CB . PRO A 137 ? 1.0996 0.8842 0.8401 0.0967 0.0317 0.0823 137 PRO A CB 1088 C CG . PRO A 137 ? 1.0898 0.8596 0.8386 0.0875 0.0436 0.0802 137 PRO A CG 1089 C CD . PRO A 137 ? 1.0615 0.8452 0.8301 0.0739 0.0377 0.0712 137 PRO A CD 1090 N N . GLU A 138 ? 1.1786 0.9604 0.9144 0.0856 0.0356 0.0782 138 GLU A N 1091 C CA . GLU A 138 ? 1.2206 0.9946 0.9428 0.0883 0.0397 0.0808 138 GLU A CA 1092 C C . GLU A 138 ? 1.2055 0.9976 0.9330 0.0837 0.0285 0.0755 138 GLU A C 1093 O O . GLU A 138 ? 1.2658 1.0538 0.9809 0.0870 0.0298 0.0774 138 GLU A O 1094 C CB . GLU A 138 ? 1.2568 1.0111 0.9804 0.0815 0.0554 0.0811 138 GLU A CB 1095 C CG . GLU A 138 ? 1.2609 1.0220 1.0069 0.0660 0.0559 0.0728 138 GLU A CG 1096 C CD . GLU A 138 ? 1.2588 1.0200 1.0197 0.0602 0.0575 0.0693 138 GLU A CD 1097 O OE1 . GLU A 138 ? 1.2638 1.0328 1.0251 0.0650 0.0503 0.0702 138 GLU A OE1 1098 O OE2 . GLU A 138 ? 1.2055 0.9591 0.9780 0.0508 0.0660 0.0653 138 GLU A OE2 1099 N N . TYR A 139 ? 1.2068 1.0178 0.9516 0.0765 0.0182 0.0690 139 TYR A N 1100 C CA . TYR A 139 ? 1.2146 1.0435 0.9657 0.0721 0.0074 0.0636 139 TYR A CA 1101 C C . TYR A 139 ? 1.2479 1.0945 0.9981 0.0789 -0.0059 0.0627 139 TYR A C 1102 O O . TYR A 139 ? 1.2500 1.1124 1.0067 0.0752 -0.0152 0.0577 139 TYR A O 1103 C CB . TYR A 139 ? 1.1628 1.0000 0.9345 0.0585 0.0062 0.0563 139 TYR A CB 1104 C CG . TYR A 139 ? 1.1952 1.0197 0.9694 0.0511 0.0171 0.0553 139 TYR A CG 1105 C CD1 . TYR A 139 ? 1.2654 1.0845 1.0298 0.0519 0.0204 0.0567 139 TYR A CD1 1106 C CD2 . TYR A 139 ? 1.1483 0.9661 0.9349 0.0434 0.0243 0.0527 139 TYR A CD2 1107 C CE1 . TYR A 139 ? 1.2655 1.0732 1.0334 0.0452 0.0311 0.0558 139 TYR A CE1 1108 C CE2 . TYR A 139 ? 1.1696 0.9768 0.9604 0.0366 0.0343 0.0512 139 TYR A CE2 1109 C CZ . TYR A 139 ? 1.2098 1.0121 0.9917 0.0374 0.0379 0.0529 139 TYR A CZ 1110 O OH . TYR A 139 ? 1.2022 0.9943 0.9895 0.0306 0.0485 0.0512 139 TYR A OH 1111 N N . LYS A 140 ? 1.3018 1.1459 1.0445 0.0889 -0.0066 0.0674 140 LYS A N 1112 C CA . LYS A 140 ? 1.2917 1.1528 1.0339 0.0964 -0.0189 0.0667 140 LYS A CA 1113 C C . LYS A 140 ? 1.2535 1.1201 0.9820 0.1033 -0.0254 0.0670 140 LYS A C 1114 O O . LYS A 140 ? 1.2643 1.1491 0.9973 0.1055 -0.0371 0.0631 140 LYS A O 1115 C CB . LYS A 140 ? 1.3452 1.2008 1.0805 0.1071 -0.0172 0.0724 140 LYS A CB 1116 C CG . LYS A 140 ? 1.3993 1.2557 1.1497 0.1017 -0.0151 0.0708 140 LYS A CG 1117 C CD . LYS A 140 ? 1.4415 1.2939 1.1844 0.1134 -0.0143 0.0766 140 LYS A CD 1118 C CE . LYS A 140 ? 1.4584 1.3139 1.2166 0.1086 -0.0138 0.0745 140 LYS A CE 1119 N NZ . LYS A 140 ? 1.5006 1.3543 1.2525 0.1205 -0.0140 0.0798 140 LYS A NZ 1120 N N . ASN A 141 ? 1.2926 1.1433 1.0043 0.1071 -0.0175 0.0712 141 ASN A N 1121 C CA . ASN A 141 ? 1.3655 1.2193 1.0611 0.1149 -0.0231 0.0718 141 ASN A CA 1122 C C . ASN A 141 ? 1.3144 1.1783 1.0178 0.1053 -0.0278 0.0652 141 ASN A C 1123 O O . ASN A 141 ? 1.3412 1.2161 1.0383 0.1095 -0.0370 0.0625 141 ASN A O 1124 C CB . ASN A 141 ? 1.4394 1.2702 1.1115 0.1240 -0.0118 0.0797 141 ASN A CB 1125 C CG . ASN A 141 ? 1.5364 1.3565 1.1967 0.1362 -0.0074 0.0870 141 ASN A CG 1126 O OD1 . ASN A 141 ? 1.6069 1.4050 1.2571 0.1388 0.0062 0.0932 141 ASN A OD1 1127 N ND2 . ASN A 141 ? 1.5462 1.3817 1.2083 0.1438 -0.0186 0.0863 141 ASN A ND2 1128 N N . ASN A 142 ? 1.1916 1.0519 0.9087 0.0927 -0.0215 0.0623 142 ASN A N 1129 C CA . ASN A 142 ? 1.1407 1.0065 0.8638 0.0837 -0.0231 0.0570 142 ASN A CA 1130 C C . ASN A 142 ? 1.1296 1.0178 0.8634 0.0809 -0.0366 0.0502 142 ASN A C 1131 O O . ASN A 142 ? 1.1752 1.0755 0.9195 0.0815 -0.0433 0.0482 142 ASN A O 1132 C CB . ASN A 142 ? 1.0845 0.9445 0.8227 0.0713 -0.0149 0.0547 142 ASN A CB 1133 C CG . ASN A 142 ? 1.1151 0.9528 0.8451 0.0726 -0.0003 0.0604 142 ASN A CG 1134 O OD1 . ASN A 142 ? 1.1140 0.9414 0.8347 0.0806 0.0040 0.0659 142 ASN A OD1 1135 N ND2 . ASN A 142 ? 1.1142 0.9441 0.8482 0.0646 0.0076 0.0588 142 ASN A ND2 1136 N N . LYS A 143 ? 1.1441 1.0371 0.8751 0.0780 -0.0400 0.0466 143 LYS A N 1137 C CA . LYS A 143 ? 1.1342 1.0473 0.8768 0.0738 -0.0513 0.0394 143 LYS A CA 1138 C C . LYS A 143 ? 1.0701 0.9903 0.8349 0.0626 -0.0509 0.0353 143 LYS A C 1139 O O . LYS A 143 ? 1.0498 0.9607 0.8199 0.0555 -0.0427 0.0358 143 LYS A O 1140 C CB . LYS A 143 ? 1.1661 1.0805 0.9023 0.0712 -0.0529 0.0361 143 LYS A CB 1141 C CG . LYS A 143 ? 1.2024 1.1093 0.9148 0.0825 -0.0535 0.0396 143 LYS A CG 1142 C CD . LYS A 143 ? 1.2587 1.1705 0.9670 0.0794 -0.0573 0.0347 143 LYS A CD 1143 C CE . LYS A 143 ? 1.3533 1.2494 1.0366 0.0879 -0.0520 0.0395 143 LYS A CE 1144 N NZ . LYS A 143 ? 1.4056 1.3071 1.0831 0.0862 -0.0569 0.0344 143 LYS A NZ 1145 N N . LEU A 144 ? 1.0679 1.0044 0.8454 0.0615 -0.0596 0.0311 144 LEU A N 1146 C CA . LEU A 144 ? 0.9943 0.9372 0.7913 0.0526 -0.0594 0.0277 144 LEU A CA 1147 C C . LEU A 144 ? 0.9297 0.8880 0.7393 0.0456 -0.0664 0.0206 144 LEU A C 1148 O O . LEU A 144 ? 0.8843 0.8561 0.6965 0.0487 -0.0748 0.0172 144 LEU A O 1149 C CB . LEU A 144 ? 0.9677 0.9142 0.7700 0.0572 -0.0615 0.0296 144 LEU A CB 1150 C CG . LEU A 144 ? 0.9443 0.8989 0.7654 0.0497 -0.0627 0.0258 144 LEU A CG 1151 C CD1 . LEU A 144 ? 0.9498 0.8934 0.7759 0.0420 -0.0543 0.0263 144 LEU A CD1 1152 C CD2 . LEU A 144 ? 0.9581 0.9170 0.7832 0.0555 -0.0652 0.0278 144 LEU A CD2 1153 N N . PHE A 145 ? 0.9202 0.8766 0.7383 0.0363 -0.0624 0.0179 145 PHE A N 1154 C CA . PHE A 145 ? 0.9165 0.8853 0.7471 0.0291 -0.0671 0.0116 145 PHE A CA 1155 C C . PHE A 145 ? 0.8744 0.8466 0.7209 0.0227 -0.0657 0.0096 145 PHE A C 1156 O O . PHE A 145 ? 0.8193 0.7822 0.6677 0.0203 -0.0595 0.0118 145 PHE A O 1157 C CB . PHE A 145 ? 0.9306 0.8954 0.7571 0.0243 -0.0642 0.0098 145 PHE A CB 1158 C CG . PHE A 145 ? 0.9365 0.8981 0.7467 0.0304 -0.0659 0.0111 145 PHE A CG 1159 C CD1 . PHE A 145 ? 0.9555 0.9028 0.7503 0.0365 -0.0600 0.0170 145 PHE A CD1 1160 C CD2 . PHE A 145 ? 0.9593 0.9321 0.7692 0.0306 -0.0732 0.0060 145 PHE A CD2 1161 C CE1 . PHE A 145 ? 0.9878 0.9315 0.7653 0.0434 -0.0616 0.0184 145 PHE A CE1 1162 C CE2 . PHE A 145 ? 0.9594 0.9297 0.7530 0.0370 -0.0756 0.0066 145 PHE A CE2 1163 C CZ . PHE A 145 ? 0.9491 0.9048 0.7258 0.0438 -0.0699 0.0130 145 PHE A CZ 1164 N N . LEU A 146 ? 0.8689 0.8544 0.7267 0.0201 -0.0714 0.0048 146 LEU A N 1165 C CA . LEU A 146 ? 0.8211 0.8104 0.6929 0.0147 -0.0706 0.0026 146 LEU A CA 1166 C C . LEU A 146 ? 0.8429 0.8358 0.7209 0.0074 -0.0702 -0.0018 146 LEU A C 1167 O O . LEU A 146 ? 0.8370 0.8383 0.7163 0.0065 -0.0745 -0.0056 146 LEU A O 1168 C CB . LEU A 146 ? 0.7996 0.8006 0.6798 0.0176 -0.0761 0.0007 146 LEU A CB 1169 C CG . LEU A 146 ? 0.7917 0.7925 0.6660 0.0263 -0.0782 0.0045 146 LEU A CG 1170 C CD1 . LEU A 146 ? 0.7860 0.8004 0.6715 0.0282 -0.0838 0.0016 146 LEU A CD1 1171 C CD2 . LEU A 146 ? 0.7772 0.7653 0.6478 0.0280 -0.0720 0.0097 146 LEU A CD2 1172 N N . THR A 147 ? 0.8567 0.8435 0.7387 0.0022 -0.0652 -0.0018 147 THR A N 1173 C CA . THR A 147 ? 0.8568 0.8461 0.7441 -0.0039 -0.0643 -0.0055 147 THR A CA 1174 C C . THR A 147 ? 0.8476 0.8374 0.7449 -0.0077 -0.0624 -0.0070 147 THR A C 1175 O O . THR A 147 ? 0.8445 0.8292 0.7428 -0.0066 -0.0601 -0.0048 147 THR A O 1176 C CB . THR A 147 ? 0.9053 0.8860 0.7856 -0.0061 -0.0597 -0.0044 147 THR A CB 1177 O OG1 . THR A 147 ? 0.9406 0.9125 0.8219 -0.0072 -0.0544 -0.0020 147 THR A OG1 1178 C CG2 . THR A 147 ? 0.9008 0.8779 0.7678 -0.0014 -0.0604 -0.0022 147 THR A CG2 1179 N N . GLY A 148 ? 0.9089 0.9042 0.8130 -0.0118 -0.0630 -0.0107 148 GLY A N 1180 C CA . GLY A 148 ? 0.8726 0.8682 0.7849 -0.0146 -0.0612 -0.0121 148 GLY A CA 1181 C C . GLY A 148 ? 0.8317 0.8302 0.7480 -0.0188 -0.0603 -0.0155 148 GLY A C 1182 O O . GLY A 148 ? 0.8164 0.8166 0.7297 -0.0203 -0.0608 -0.0169 148 GLY A O 1183 N N . GLU A 149 ? 0.8291 0.8277 0.7514 -0.0203 -0.0587 -0.0167 149 GLU A N 1184 C CA . GLU A 149 ? 0.8029 0.8032 0.7287 -0.0234 -0.0571 -0.0194 149 GLU A CA 1185 C C . GLU A 149 ? 0.7899 0.7928 0.7222 -0.0230 -0.0565 -0.0207 149 GLU A C 1186 O O . GLU A 149 ? 0.7872 0.7892 0.7209 -0.0205 -0.0569 -0.0193 149 GLU A O 1187 C CB . GLU A 149 ? 0.7911 0.7862 0.7154 -0.0251 -0.0544 -0.0191 149 GLU A CB 1188 C CG . GLU A 149 ? 0.8354 0.8315 0.7618 -0.0276 -0.0524 -0.0214 149 GLU A CG 1189 C CD . GLU A 149 ? 0.9011 0.8934 0.8279 -0.0283 -0.0503 -0.0215 149 GLU A CD 1190 O OE1 . GLU A 149 ? 0.8676 0.8570 0.7917 -0.0294 -0.0492 -0.0206 149 GLU A OE1 1191 O OE2 . GLU A 149 ? 0.9372 0.9297 0.8673 -0.0275 -0.0498 -0.0225 149 GLU A OE2 1192 N N . SER A 150 ? 0.7663 0.7713 0.7017 -0.0251 -0.0548 -0.0232 150 SER A N 1193 C CA . SER A 150 ? 0.7641 0.7689 0.7042 -0.0244 -0.0524 -0.0240 150 SER A CA 1194 C C . SER A 150 ? 0.7338 0.7423 0.6787 -0.0224 -0.0535 -0.0239 150 SER A C 1195 O O . SER A 150 ? 0.7533 0.7675 0.7009 -0.0230 -0.0557 -0.0252 150 SER A O 1196 C CB . SER A 150 ? 0.7635 0.7628 0.7014 -0.0228 -0.0511 -0.0228 150 SER A CB 1197 O OG . SER A 150 ? 0.7514 0.7492 0.6912 -0.0213 -0.0485 -0.0234 150 SER A OG 1198 N N . TYR A 151 ? 0.6885 0.6943 0.6347 -0.0199 -0.0522 -0.0226 151 TYR A N 1199 C CA . TYR A 151 ? 0.6929 0.7019 0.6440 -0.0177 -0.0527 -0.0222 151 TYR A CA 1200 C C . TYR A 151 ? 0.6824 0.6950 0.6326 -0.0162 -0.0569 -0.0209 151 TYR A C 1201 O O . TYR A 151 ? 0.6809 0.6984 0.6363 -0.0145 -0.0580 -0.0211 151 TYR A O 1202 C CB . TYR A 151 ? 0.6968 0.7007 0.6474 -0.0147 -0.0505 -0.0206 151 TYR A CB 1203 C CG . TYR A 151 ? 0.6837 0.6908 0.6408 -0.0128 -0.0494 -0.0207 151 TYR A CG 1204 C CD1 . TYR A 151 ? 0.6861 0.6950 0.6494 -0.0139 -0.0455 -0.0227 151 TYR A CD1 1205 C CD2 . TYR A 151 ? 0.7089 0.7172 0.6666 -0.0101 -0.0515 -0.0188 151 TYR A CD2 1206 C CE1 . TYR A 151 ? 0.7023 0.7147 0.6733 -0.0125 -0.0438 -0.0230 151 TYR A CE1 1207 C CE2 . TYR A 151 ? 0.7253 0.7373 0.6901 -0.0082 -0.0503 -0.0189 151 TYR A CE2 1208 C CZ . TYR A 151 ? 0.7156 0.7300 0.6876 -0.0096 -0.0465 -0.0212 151 TYR A CZ 1209 O OH . TYR A 151 ? 0.7710 0.7896 0.7519 -0.0081 -0.0446 -0.0217 151 TYR A OH 1210 N N . ALA A 152 ? 0.6812 0.6913 0.6249 -0.0164 -0.0587 -0.0195 152 ALA A N 1211 C CA . ALA A 152 ? 0.6998 0.7119 0.6404 -0.0139 -0.0620 -0.0178 152 ALA A CA 1212 C C . ALA A 152 ? 0.7133 0.7336 0.6564 -0.0146 -0.0651 -0.0203 152 ALA A C 1213 O O . ALA A 152 ? 0.7351 0.7584 0.6754 -0.0118 -0.0685 -0.0194 152 ALA A O 1214 C CB . ALA A 152 ? 0.7239 0.7294 0.6563 -0.0138 -0.0618 -0.0154 152 ALA A CB 1215 N N . GLY A 153 ? 0.7186 0.7424 0.6666 -0.0181 -0.0637 -0.0239 153 GLY A N 1216 C CA . GLY A 153 ? 0.7417 0.7745 0.6953 -0.0191 -0.0664 -0.0277 153 GLY A CA 1217 C C . GLY A 153 ? 0.7477 0.7872 0.7097 -0.0165 -0.0679 -0.0284 153 GLY A C 1218 O O . GLY A 153 ? 0.7493 0.7979 0.7162 -0.0161 -0.0717 -0.0315 153 GLY A O 1219 N N . ILE A 154 ? 0.7520 0.7873 0.7160 -0.0147 -0.0650 -0.0258 154 ILE A N 1220 C CA . ILE A 154 ? 0.7449 0.7848 0.7158 -0.0113 -0.0658 -0.0252 154 ILE A CA 1221 C C . ILE A 154 ? 0.7518 0.7886 0.7158 -0.0064 -0.0683 -0.0208 154 ILE A C 1222 O O . ILE A 154 ? 0.7833 0.8266 0.7500 -0.0028 -0.0718 -0.0206 154 ILE A O 1223 C CB . ILE A 154 ? 0.7223 0.7582 0.6985 -0.0115 -0.0603 -0.0248 154 ILE A CB 1224 C CG1 . ILE A 154 ? 0.7301 0.7669 0.7122 -0.0158 -0.0563 -0.0285 154 ILE A CG1 1225 C CG2 . ILE A 154 ? 0.7352 0.7762 0.7194 -0.0082 -0.0606 -0.0243 154 ILE A CG2 1226 C CD1 . ILE A 154 ? 0.7269 0.7745 0.7198 -0.0182 -0.0578 -0.0336 154 ILE A CD1 1227 N N . TYR A 155 ? 0.7343 0.7613 0.6898 -0.0061 -0.0663 -0.0175 155 TYR A N 1228 C CA . TYR A 155 ? 0.7389 0.7610 0.6876 -0.0019 -0.0674 -0.0134 155 TYR A CA 1229 C C . TYR A 155 ? 0.7285 0.7551 0.6726 0.0009 -0.0719 -0.0128 155 TYR A C 1230 O O . TYR A 155 ? 0.7258 0.7544 0.6693 0.0059 -0.0739 -0.0107 155 TYR A O 1231 C CB . TYR A 155 ? 0.7488 0.7602 0.6895 -0.0030 -0.0647 -0.0112 155 TYR A CB 1232 C CG . TYR A 155 ? 0.7581 0.7639 0.7006 -0.0044 -0.0610 -0.0115 155 TYR A CG 1233 C CD1 . TYR A 155 ? 0.7683 0.7751 0.7164 -0.0027 -0.0594 -0.0117 155 TYR A CD1 1234 C CD2 . TYR A 155 ? 0.7866 0.7858 0.7246 -0.0068 -0.0592 -0.0117 155 TYR A CD2 1235 C CE1 . TYR A 155 ? 0.7662 0.7670 0.7137 -0.0030 -0.0562 -0.0119 155 TYR A CE1 1236 C CE2 . TYR A 155 ? 0.7847 0.7793 0.7232 -0.0072 -0.0568 -0.0124 155 TYR A CE2 1237 C CZ . TYR A 155 ? 0.7858 0.7808 0.7282 -0.0050 -0.0553 -0.0124 155 TYR A CZ 1238 O OH . TYR A 155 ? 0.8387 0.8283 0.7797 -0.0044 -0.0531 -0.0131 155 TYR A OH 1239 N N . ILE A 156 ? 0.7567 0.7842 0.6968 -0.0016 -0.0733 -0.0147 156 ILE A N 1240 C CA . ILE A 156 ? 0.7928 0.8210 0.7241 0.0016 -0.0768 -0.0134 156 ILE A CA 1241 C C . ILE A 156 ? 0.7901 0.8301 0.7256 0.0052 -0.0825 -0.0158 156 ILE A C 1242 O O . ILE A 156 ? 0.7815 0.8218 0.7112 0.0112 -0.0852 -0.0130 156 ILE A O 1243 C CB . ILE A 156 ? 0.7933 0.8177 0.7178 -0.0019 -0.0759 -0.0145 156 ILE A CB 1244 C CG1 . ILE A 156 ? 0.7934 0.8061 0.7123 -0.0037 -0.0710 -0.0114 156 ILE A CG1 1245 C CG2 . ILE A 156 ? 0.8363 0.8627 0.7518 0.0016 -0.0799 -0.0142 156 ILE A CG2 1246 C CD1 . ILE A 156 ? 0.8321 0.8367 0.7429 0.0006 -0.0696 -0.0066 156 ILE A CD1 1247 N N . PRO A 157 ? 0.7697 0.8195 0.7154 0.0018 -0.0842 -0.0212 157 PRO A N 1248 C CA . PRO A 157 ? 0.7932 0.8557 0.7447 0.0051 -0.0900 -0.0245 157 PRO A CA 1249 C C . PRO A 157 ? 0.8668 0.9328 0.8244 0.0101 -0.0907 -0.0224 157 PRO A C 1250 O O . PRO A 157 ? 0.8905 0.9629 0.8464 0.0161 -0.0957 -0.0219 157 PRO A O 1251 C CB . PRO A 157 ? 0.7818 0.8526 0.7455 -0.0007 -0.0898 -0.0312 157 PRO A CB 1252 C CG . PRO A 157 ? 0.7790 0.8408 0.7375 -0.0061 -0.0852 -0.0310 157 PRO A CG 1253 C CD . PRO A 157 ? 0.7954 0.8454 0.7473 -0.0047 -0.0809 -0.0250 157 PRO A CD 1254 N N . THR A 158 ? 0.8844 0.9461 0.8484 0.0081 -0.0855 -0.0209 158 THR A N 1255 C CA . THR A 158 ? 0.8520 0.9164 0.8222 0.0127 -0.0853 -0.0189 158 THR A CA 1256 C C . THR A 158 ? 0.8801 0.9371 0.8383 0.0191 -0.0860 -0.0129 158 THR A C 1257 O O . THR A 158 ? 0.8844 0.9470 0.8443 0.0254 -0.0891 -0.0115 158 THR A O 1258 C CB . THR A 158 ? 0.8296 0.8887 0.8067 0.0097 -0.0789 -0.0183 158 THR A CB 1259 O OG1 . THR A 158 ? 0.8174 0.8630 0.7844 0.0079 -0.0748 -0.0149 158 THR A OG1 1260 C CG2 . THR A 158 ? 0.8317 0.8969 0.8206 0.0040 -0.0769 -0.0238 158 THR A CG2 1261 N N . LEU A 159 ? 0.8698 0.9142 0.8164 0.0177 -0.0828 -0.0095 159 LEU A N 1262 C CA . LEU A 159 ? 0.8611 0.8962 0.7952 0.0231 -0.0821 -0.0039 159 LEU A CA 1263 C C . LEU A 159 ? 0.8815 0.9222 0.8087 0.0288 -0.0877 -0.0036 159 LEU A C 1264 O O . LEU A 159 ? 0.9102 0.9515 0.8338 0.0361 -0.0894 -0.0004 159 LEU A O 1265 C CB . LEU A 159 ? 0.8290 0.8510 0.7539 0.0195 -0.0775 -0.0018 159 LEU A CB 1266 C CG . LEU A 159 ? 0.8348 0.8457 0.7469 0.0242 -0.0754 0.0035 159 LEU A CG 1267 C CD1 . LEU A 159 ? 0.8453 0.8534 0.7584 0.0295 -0.0739 0.0070 159 LEU A CD1 1268 C CD2 . LEU A 159 ? 0.8041 0.8028 0.7104 0.0195 -0.0701 0.0046 159 LEU A CD2 1269 N N . ALA A 160 ? 0.8719 0.9166 0.7968 0.0260 -0.0904 -0.0071 160 ALA A N 1270 C CA . ALA A 160 ? 0.9065 0.9554 0.8224 0.0314 -0.0959 -0.0073 160 ALA A CA 1271 C C . ALA A 160 ? 0.9396 1.0016 0.8617 0.0381 -0.1021 -0.0088 160 ALA A C 1272 O O . ALA A 160 ? 0.9933 1.0547 0.9052 0.0464 -0.1052 -0.0056 160 ALA A O 1273 C CB . ALA A 160 ? 0.9163 0.9695 0.8318 0.0263 -0.0982 -0.0125 160 ALA A CB 1274 N N . VAL A 161 ? 0.9089 0.9824 0.8478 0.0349 -0.1035 -0.0136 161 VAL A N 1275 C CA . VAL A 161 ? 0.8769 0.9642 0.8252 0.0407 -0.1089 -0.0157 161 VAL A CA 1276 C C . VAL A 161 ? 0.9111 0.9922 0.8533 0.0488 -0.1073 -0.0088 161 VAL A C 1277 O O . VAL A 161 ? 1.0565 1.1440 0.9951 0.0573 -0.1125 -0.0078 161 VAL A O 1278 C CB . VAL A 161 ? 0.8343 0.9322 0.8028 0.0350 -0.1080 -0.0213 161 VAL A CB 1279 C CG1 . VAL A 161 ? 0.8825 0.9928 0.8622 0.0413 -0.1117 -0.0222 161 VAL A CG1 1280 C CG2 . VAL A 161 ? 0.8300 0.9368 0.8052 0.0288 -0.1109 -0.0290 161 VAL A CG2 1281 N N . LEU A 162 ? 0.9018 0.9703 0.8425 0.0466 -0.1001 -0.0044 162 LEU A N 1282 C CA . LEU A 162 ? 0.8758 0.9366 0.8100 0.0538 -0.0976 0.0019 162 LEU A CA 1283 C C . LEU A 162 ? 0.9230 0.9745 0.8384 0.0604 -0.0982 0.0069 162 LEU A C 1284 O O . LEU A 162 ? 0.9381 0.9892 0.8475 0.0696 -0.0997 0.0109 162 LEU A O 1285 C CB . LEU A 162 ? 0.8399 0.8877 0.7750 0.0495 -0.0896 0.0049 162 LEU A CB 1286 C CG . LEU A 162 ? 0.8081 0.8617 0.7592 0.0445 -0.0874 0.0015 162 LEU A CG 1287 C CD1 . LEU A 162 ? 0.7774 0.8169 0.7258 0.0411 -0.0801 0.0044 162 LEU A CD1 1288 C CD2 . LEU A 162 ? 0.8084 0.8738 0.7706 0.0502 -0.0903 0.0008 162 LEU A CD2 1289 N N . VAL A 163 ? 0.9132 0.9564 0.8190 0.0560 -0.0962 0.0069 163 VAL A N 1290 C CA . VAL A 163 ? 0.9054 0.9376 0.7927 0.0616 -0.0951 0.0116 163 VAL A CA 1291 C C . VAL A 163 ? 0.9616 1.0048 0.8434 0.0697 -0.1034 0.0101 163 VAL A C 1292 O O . VAL A 163 ? 0.9846 1.0220 0.8524 0.0792 -0.1038 0.0151 163 VAL A O 1293 C CB . VAL A 163 ? 0.8597 0.8821 0.7402 0.0544 -0.0911 0.0111 163 VAL A CB 1294 C CG1 . VAL A 163 ? 0.8805 0.8918 0.7419 0.0603 -0.0894 0.0157 163 VAL A CG1 1295 C CG2 . VAL A 163 ? 0.8470 0.8589 0.7319 0.0473 -0.0836 0.0123 163 VAL A CG2 1296 N N . MET A 164 ? 1.0107 1.0697 0.9037 0.0663 -0.1098 0.0029 164 MET A N 1297 C CA . MET A 164 ? 1.1004 1.1730 0.9913 0.0732 -0.1190 -0.0006 164 MET A CA 1298 C C . MET A 164 ? 1.1741 1.2532 1.0658 0.0840 -0.1227 0.0021 164 MET A C 1299 O O . MET A 164 ? 1.2032 1.2866 1.0844 0.0937 -0.1287 0.0028 164 MET A O 1300 C CB . MET A 164 ? 1.1031 1.1923 1.0112 0.0659 -0.1241 -0.0100 164 MET A CB 1301 C CG . MET A 164 ? 1.1635 1.2691 1.0723 0.0715 -0.1345 -0.0158 164 MET A CG 1302 S SD . MET A 164 ? 1.2050 1.3281 1.1357 0.0611 -0.1384 -0.0274 164 MET A SD 1303 C CE . MET A 164 ? 1.1905 1.3189 1.1429 0.0578 -0.1340 -0.0274 164 MET A CE 1304 N N . GLN A 165 ? 1.2398 1.3194 1.1434 0.0828 -0.1191 0.0036 165 GLN A N 1305 C CA . GLN A 165 ? 1.2249 1.3095 1.1304 0.0928 -0.1213 0.0069 165 GLN A CA 1306 C C . GLN A 165 ? 1.1748 1.2426 1.0606 0.1020 -0.1166 0.0161 165 GLN A C 1307 O O . GLN A 165 ? 1.2965 1.3684 1.1794 0.1127 -0.1196 0.0190 165 GLN A O 1308 C CB . GLN A 165 ? 1.2353 1.3239 1.1591 0.0884 -0.1176 0.0059 165 GLN A CB 1309 C CG . GLN A 165 ? 1.3018 1.4080 1.2469 0.0812 -0.1215 -0.0028 165 GLN A CG 1310 C CD . GLN A 165 ? 1.3820 1.4874 1.3426 0.0753 -0.1153 -0.0032 165 GLN A CD 1311 O OE1 . GLN A 165 ? 1.3969 1.4908 1.3533 0.0778 -0.1094 0.0027 165 GLN A OE1 1312 N NE2 . GLN A 165 ? 1.4230 1.5394 1.4008 0.0675 -0.1160 -0.0103 165 GLN A NE2 1313 N N . ASP A 166 ? 1.1419 1.1909 1.0149 0.0981 -0.1089 0.0204 166 ASP A N 1314 C CA . ASP A 166 ? 1.1433 1.1742 0.9982 0.1058 -0.1026 0.0290 166 ASP A CA 1315 C C . ASP A 166 ? 1.1486 1.1706 0.9831 0.1106 -0.1028 0.0316 166 ASP A C 1316 O O . ASP A 166 ? 1.1151 1.1264 0.9440 0.1034 -0.0978 0.0316 166 ASP A O 1317 C CB . ASP A 166 ? 1.1171 1.1315 0.9731 0.0985 -0.0922 0.0324 166 ASP A CB 1318 C CG . ASP A 166 ? 1.1965 1.1913 1.0356 0.1055 -0.0844 0.0407 166 ASP A CG 1319 O OD1 . ASP A 166 ? 1.2922 1.2854 1.1178 0.1169 -0.0865 0.0448 166 ASP A OD1 1320 O OD2 . ASP A 166 ? 1.2047 1.1855 1.0439 0.0999 -0.0759 0.0429 166 ASP A OD2 1321 N N . PRO A 167 ? 1.1661 1.1918 0.9886 0.1235 -0.1082 0.0340 167 PRO A N 1322 C CA . PRO A 167 ? 1.1864 1.2048 0.9887 0.1290 -0.1092 0.0359 167 PRO A CA 1323 C C . PRO A 167 ? 1.1791 1.1723 0.9622 0.1321 -0.0978 0.0446 167 PRO A C 1324 O O . PRO A 167 ? 1.1851 1.1691 0.9506 0.1359 -0.0964 0.0469 167 PRO A O 1325 C CB . PRO A 167 ? 1.2157 1.2480 1.0127 0.1427 -0.1194 0.0352 167 PRO A CB 1326 C CG . PRO A 167 ? 1.1979 1.2371 1.0071 0.1470 -0.1199 0.0368 167 PRO A CG 1327 C CD . PRO A 167 ? 1.1717 1.2061 0.9969 0.1346 -0.1125 0.0362 167 PRO A CD 1328 N N . SER A 168 ? 1.1439 1.1260 0.9305 0.1308 -0.0896 0.0492 168 SER A N 1329 C CA . SER A 168 ? 1.1185 1.0764 0.8919 0.1300 -0.0772 0.0560 168 SER A CA 1330 C C . SER A 168 ? 1.1343 1.0857 0.9105 0.1173 -0.0725 0.0528 168 SER A C 1331 O O . SER A 168 ? 1.1332 1.0676 0.8957 0.1175 -0.0645 0.0568 168 SER A O 1332 C CB . SER A 168 ? 1.1201 1.0697 0.9002 0.1293 -0.0700 0.0596 168 SER A CB 1333 O OG . SER A 168 ? 1.1156 1.0491 0.8968 0.1196 -0.0596 0.0606 168 SER A OG 1334 N N . MET A 169 ? 1.1317 1.0966 0.9258 0.1066 -0.0770 0.0456 169 MET A N 1335 C CA . MET A 169 ? 1.0957 1.0575 0.8933 0.0952 -0.0742 0.0419 169 MET A CA 1336 C C . MET A 169 ? 1.1131 1.0820 0.9031 0.0967 -0.0806 0.0386 169 MET A C 1337 O O . MET A 169 ? 1.1055 1.0919 0.9013 0.0993 -0.0905 0.0338 169 MET A O 1338 C CB . MET A 169 ? 1.0329 1.0051 0.8515 0.0840 -0.0759 0.0360 169 MET A CB 1339 C CG . MET A 169 ? 1.0296 0.9918 0.8547 0.0800 -0.0682 0.0383 169 MET A CG 1340 S SD . MET A 169 ? 1.0512 1.0261 0.8988 0.0696 -0.0709 0.0317 169 MET A SD 1341 C CE . MET A 169 ? 1.0529 1.0176 0.9032 0.0716 -0.0643 0.0360 169 MET A CE 1342 N N . ASN A 170 ? 1.1100 1.0657 0.8882 0.0944 -0.0746 0.0405 170 ASN A N 1343 C CA . ASN A 170 ? 1.1188 1.0773 0.8858 0.0967 -0.0790 0.0383 170 ASN A CA 1344 C C . ASN A 170 ? 1.0595 1.0276 0.8390 0.0850 -0.0821 0.0309 170 ASN A C 1345 O O . ASN A 170 ? 1.0329 0.9926 0.8057 0.0806 -0.0777 0.0307 170 ASN A O 1346 C CB . ASN A 170 ? 1.1446 1.0819 0.8905 0.1016 -0.0697 0.0450 170 ASN A CB 1347 C CG . ASN A 170 ? 1.1199 1.0581 0.8498 0.1071 -0.0741 0.0439 170 ASN A CG 1348 O OD1 . ASN A 170 ? 1.1090 1.0636 0.8407 0.1105 -0.0851 0.0390 170 ASN A OD1 1349 N ND2 . ASN A 170 ? 1.1106 1.0310 0.8253 0.1078 -0.0652 0.0482 170 ASN A ND2 1350 N N . LEU A 171 ? 1.0153 1.0007 0.8126 0.0805 -0.0891 0.0249 171 LEU A N 1351 C CA . LEU A 171 ? 0.9567 0.9516 0.7671 0.0698 -0.0918 0.0178 171 LEU A CA 1352 C C . LEU A 171 ? 1.0157 1.0152 0.8168 0.0712 -0.0970 0.0141 171 LEU A C 1353 O O . LEU A 171 ? 0.9728 0.9830 0.7697 0.0786 -0.1055 0.0117 171 LEU A O 1354 C CB . LEU A 171 ? 0.9203 0.9323 0.7504 0.0665 -0.0978 0.0125 171 LEU A CB 1355 C CG . LEU A 171 ? 0.9063 0.9286 0.7510 0.0560 -0.1002 0.0051 171 LEU A CG 1356 C CD1 . LEU A 171 ? 0.8677 0.8790 0.7158 0.0467 -0.0919 0.0061 171 LEU A CD1 1357 C CD2 . LEU A 171 ? 0.9084 0.9468 0.7716 0.0545 -0.1054 0.0003 171 LEU A CD2 1358 N N . GLN A 172 ? 1.0604 1.0523 0.8586 0.0642 -0.0922 0.0131 172 GLN A N 1359 C CA . GLN A 172 ? 1.0953 1.0909 0.8849 0.0647 -0.0966 0.0092 172 GLN A CA 1360 C C . GLN A 172 ? 1.0587 1.0651 0.8635 0.0541 -0.0994 0.0014 172 GLN A C 1361 O O . GLN A 172 ? 1.1338 1.1510 0.9384 0.0546 -0.1066 -0.0043 172 GLN A O 1362 C CB . GLN A 172 ? 1.1766 1.1538 0.9468 0.0674 -0.0889 0.0146 172 GLN A CB 1363 C CG . GLN A 172 ? 1.1973 1.1647 0.9481 0.0805 -0.0877 0.0215 172 GLN A CG 1364 C CD . GLN A 172 ? 1.2270 1.2068 0.9697 0.0910 -0.0989 0.0188 172 GLN A CD 1365 O OE1 . GLN A 172 ? 1.2251 1.2154 0.9677 0.0897 -0.1062 0.0123 172 GLN A OE1 1366 N NE2 . GLN A 172 ? 1.2373 1.2159 0.9730 0.1016 -0.1004 0.0235 172 GLN A NE2 1367 N N . GLY A 173 ? 1.0420 1.0456 0.8596 0.0448 -0.0937 0.0011 173 GLY A N 1368 C CA . GLY A 173 ? 0.9927 1.0060 0.8251 0.0353 -0.0955 -0.0056 173 GLY A CA 1369 C C . GLY A 173 ? 0.9349 0.9470 0.7824 0.0272 -0.0904 -0.0057 173 GLY A C 1370 O O . GLY A 173 ? 0.8495 0.8536 0.6974 0.0281 -0.0855 -0.0009 173 GLY A O 1371 N N . LEU A 174 ? 0.9094 0.9289 0.7684 0.0196 -0.0914 -0.0115 174 LEU A N 1372 C CA . LEU A 174 ? 0.8791 0.8971 0.7506 0.0123 -0.0866 -0.0120 174 LEU A CA 1373 C C . LEU A 174 ? 0.8768 0.8954 0.7524 0.0047 -0.0846 -0.0162 174 LEU A C 1374 O O . LEU A 174 ? 0.9344 0.9597 0.8096 0.0037 -0.0886 -0.0209 174 LEU A O 1375 C CB . LEU A 174 ? 0.8678 0.8958 0.7534 0.0122 -0.0895 -0.0140 174 LEU A CB 1376 C CG . LEU A 174 ? 0.8862 0.9295 0.7807 0.0120 -0.0963 -0.0206 174 LEU A CG 1377 C CD1 . LEU A 174 ? 0.8902 0.9380 0.7979 0.0037 -0.0942 -0.0257 174 LEU A CD1 1378 C CD2 . LEU A 174 ? 0.8691 0.9212 0.7706 0.0173 -0.1005 -0.0205 174 LEU A CD2 1379 N N . ALA A 175 ? 0.8379 0.8493 0.7173 -0.0003 -0.0786 -0.0147 175 ALA A N 1380 C CA . ALA A 175 ? 0.8116 0.8231 0.6953 -0.0069 -0.0761 -0.0182 175 ALA A CA 1381 C C . ALA A 175 ? 0.7883 0.8004 0.6841 -0.0116 -0.0729 -0.0189 175 ALA A C 1382 O O . ALA A 175 ? 0.7505 0.7572 0.6475 -0.0108 -0.0701 -0.0155 175 ALA A O 1383 C CB . ALA A 175 ? 0.7964 0.7976 0.6697 -0.0077 -0.0716 -0.0157 175 ALA A CB 1384 N N . VAL A 176 ? 0.7581 0.7758 0.6619 -0.0161 -0.0730 -0.0235 176 VAL A N 1385 C CA . VAL A 176 ? 0.7274 0.7455 0.6413 -0.0196 -0.0699 -0.0243 176 VAL A CA 1386 C C . VAL A 176 ? 0.7333 0.7485 0.6482 -0.0244 -0.0661 -0.0263 176 VAL A C 1387 O O . VAL A 176 ? 0.8242 0.8431 0.7398 -0.0268 -0.0669 -0.0301 176 VAL A O 1388 C CB . VAL A 176 ? 0.7190 0.7464 0.6433 -0.0196 -0.0725 -0.0276 176 VAL A CB 1389 C CG1 . VAL A 176 ? 0.7166 0.7436 0.6500 -0.0231 -0.0684 -0.0290 176 VAL A CG1 1390 C CG2 . VAL A 176 ? 0.7254 0.7551 0.6501 -0.0145 -0.0754 -0.0250 176 VAL A CG2 1391 N N . GLY A 177 ? 0.7319 0.7409 0.6474 -0.0257 -0.0621 -0.0242 177 GLY A N 1392 C CA . GLY A 177 ? 0.7198 0.7260 0.6364 -0.0294 -0.0583 -0.0256 177 GLY A CA 1393 C C . GLY A 177 ? 0.7191 0.7275 0.6440 -0.0311 -0.0563 -0.0275 177 GLY A C 1394 O O . GLY A 177 ? 0.6628 0.6705 0.5914 -0.0295 -0.0559 -0.0261 177 GLY A O 1395 N N . ASN A 178 ? 0.7568 0.7669 0.6840 -0.0339 -0.0546 -0.0307 178 ASN A N 1396 C CA . ASN A 178 ? 0.7657 0.7770 0.7001 -0.0351 -0.0517 -0.0325 178 ASN A CA 1397 C C . ASN A 178 ? 0.7643 0.7784 0.7042 -0.0329 -0.0529 -0.0318 178 ASN A C 1398 O O . ASN A 178 ? 0.7646 0.7756 0.7061 -0.0313 -0.0509 -0.0301 178 ASN A O 1399 C CB . ASN A 178 ? 0.7352 0.7410 0.6685 -0.0353 -0.0477 -0.0311 178 ASN A CB 1400 C CG . ASN A 178 ? 0.7408 0.7444 0.6706 -0.0377 -0.0455 -0.0323 178 ASN A CG 1401 O OD1 . ASN A 178 ? 0.7536 0.7552 0.6781 -0.0379 -0.0463 -0.0311 178 ASN A OD1 1402 N ND2 . ASN A 178 ? 0.7114 0.7145 0.6440 -0.0394 -0.0418 -0.0346 178 ASN A ND2 1403 N N . GLY A 179 ? 0.7801 0.8003 0.7224 -0.0323 -0.0566 -0.0334 179 GLY A N 1404 C CA . GLY A 179 ? 0.7983 0.8220 0.7461 -0.0298 -0.0581 -0.0327 179 GLY A CA 1405 C C . GLY A 179 ? 0.8548 0.8817 0.8121 -0.0314 -0.0550 -0.0357 179 GLY A C 1406 O O . GLY A 179 ? 0.8761 0.9038 0.8361 -0.0348 -0.0525 -0.0392 179 GLY A O 1407 N N . LEU A 180 ? 0.8269 0.8545 0.7890 -0.0290 -0.0544 -0.0343 180 LEU A N 1408 C CA . LEU A 180 ? 0.8052 0.8360 0.7774 -0.0300 -0.0511 -0.0370 180 LEU A CA 1409 C C . LEU A 180 ? 0.8352 0.8759 0.8146 -0.0295 -0.0555 -0.0396 180 LEU A C 1410 O O . LEU A 180 ? 0.9049 0.9477 0.8858 -0.0259 -0.0577 -0.0373 180 LEU A O 1411 C CB . LEU A 180 ? 0.8330 0.8580 0.8054 -0.0272 -0.0473 -0.0339 180 LEU A CB 1412 C CG . LEU A 180 ? 0.8450 0.8705 0.8267 -0.0275 -0.0419 -0.0356 180 LEU A CG 1413 C CD1 . LEU A 180 ? 0.8609 0.8857 0.8465 -0.0315 -0.0369 -0.0393 180 LEU A CD1 1414 C CD2 . LEU A 180 ? 0.8770 0.8943 0.8546 -0.0238 -0.0381 -0.0319 180 LEU A CD2 1415 N N . SER A 181 ? 0.8247 0.8720 0.8085 -0.0327 -0.0571 -0.0447 181 SER A N 1416 C CA . SER A 181 ? 0.8291 0.8878 0.8207 -0.0321 -0.0623 -0.0485 181 SER A CA 1417 C C . SER A 181 ? 0.8072 0.8718 0.8143 -0.0345 -0.0585 -0.0530 181 SER A C 1418 O O . SER A 181 ? 0.7850 0.8584 0.8007 -0.0325 -0.0617 -0.0547 181 SER A O 1419 C CB . SER A 181 ? 0.8602 0.9236 0.8479 -0.0341 -0.0669 -0.0526 181 SER A CB 1420 O OG . SER A 181 ? 0.9335 0.9914 0.9072 -0.0314 -0.0699 -0.0483 181 SER A OG 1421 N N . SER A 182 ? 0.7680 0.8273 0.7786 -0.0383 -0.0512 -0.0548 182 SER A N 1422 C CA . SER A 182 ? 0.7425 0.8049 0.7676 -0.0409 -0.0453 -0.0589 182 SER A CA 1423 C C . SER A 182 ? 0.7090 0.7598 0.7324 -0.0421 -0.0356 -0.0569 182 SER A C 1424 O O . SER A 182 ? 0.7331 0.7789 0.7520 -0.0450 -0.0327 -0.0581 182 SER A O 1425 C CB . SER A 182 ? 0.7720 0.8442 0.8074 -0.0458 -0.0472 -0.0672 182 SER A CB 1426 O OG . SER A 182 ? 0.8155 0.8870 0.8639 -0.0498 -0.0386 -0.0713 182 SER A OG 1427 N N . TYR A 183 ? 0.7122 0.7587 0.7391 -0.0396 -0.0303 -0.0540 183 TYR A N 1428 C CA . TYR A 183 ? 0.7089 0.7435 0.7329 -0.0394 -0.0206 -0.0518 183 TYR A CA 1429 C C . TYR A 183 ? 0.7070 0.7410 0.7392 -0.0446 -0.0137 -0.0572 183 TYR A C 1430 O O . TYR A 183 ? 0.7583 0.7828 0.7835 -0.0452 -0.0081 -0.0559 183 TYR A O 1431 C CB . TYR A 183 ? 0.7079 0.7384 0.7353 -0.0356 -0.0155 -0.0487 183 TYR A CB 1432 C CG . TYR A 183 ? 0.7339 0.7616 0.7518 -0.0301 -0.0201 -0.0430 183 TYR A CG 1433 C CD1 . TYR A 183 ? 0.7427 0.7594 0.7476 -0.0266 -0.0181 -0.0382 183 TYR A CD1 1434 C CD2 . TYR A 183 ? 0.7809 0.8170 0.8032 -0.0283 -0.0264 -0.0427 183 TYR A CD2 1435 C CE1 . TYR A 183 ? 0.7857 0.7999 0.7829 -0.0221 -0.0222 -0.0339 183 TYR A CE1 1436 C CE2 . TYR A 183 ? 0.7886 0.8212 0.8025 -0.0235 -0.0298 -0.0378 183 TYR A CE2 1437 C CZ . TYR A 183 ? 0.8104 0.8320 0.8120 -0.0208 -0.0277 -0.0336 183 TYR A CZ 1438 O OH . TYR A 183 ? 0.8646 0.8829 0.8588 -0.0166 -0.0311 -0.0296 183 TYR A OH 1439 N N . GLU A 184 ? 0.7234 0.7677 0.7709 -0.0485 -0.0140 -0.0636 184 GLU A N 1440 C CA . GLU A 184 ? 0.7804 0.8242 0.8380 -0.0542 -0.0065 -0.0698 184 GLU A CA 1441 C C . GLU A 184 ? 0.7819 0.8238 0.8319 -0.0575 -0.0084 -0.0721 184 GLU A C 1442 O O . GLU A 184 ? 0.7323 0.7647 0.7798 -0.0595 0.0000 -0.0724 184 GLU A O 1443 C CB . GLU A 184 ? 0.8157 0.8732 0.8930 -0.0580 -0.0079 -0.0775 184 GLU A CB 1444 C CG . GLU A 184 ? 0.8670 0.9237 0.9574 -0.0645 0.0013 -0.0846 184 GLU A CG 1445 C CD . GLU A 184 ? 0.9346 1.0057 1.0470 -0.0684 0.0003 -0.0930 184 GLU A CD 1446 O OE1 . GLU A 184 ? 0.9477 1.0250 1.0672 -0.0652 -0.0017 -0.0915 184 GLU A OE1 1447 O OE2 . GLU A 184 ? 0.9685 1.0450 1.0916 -0.0747 0.0018 -0.1014 184 GLU A OE2 1448 N N . GLN A 185 ? 0.8046 0.8548 0.8503 -0.0577 -0.0187 -0.0736 185 GLN A N 1449 C CA . GLN A 185 ? 0.8379 0.8863 0.8758 -0.0606 -0.0206 -0.0758 185 GLN A CA 1450 C C . GLN A 185 ? 0.7898 0.8255 0.8119 -0.0576 -0.0177 -0.0689 185 GLN A C 1451 O O . GLN A 185 ? 0.7443 0.7737 0.7618 -0.0600 -0.0134 -0.0700 185 GLN A O 1452 C CB . GLN A 185 ? 0.8384 0.8978 0.8739 -0.0605 -0.0322 -0.0787 185 GLN A CB 1453 C CG . GLN A 185 ? 0.8689 0.9407 0.9191 -0.0652 -0.0347 -0.0883 185 GLN A CG 1454 C CD . GLN A 185 ? 0.9044 0.9891 0.9546 -0.0627 -0.0466 -0.0905 185 GLN A CD 1455 O OE1 . GLN A 185 ? 0.9130 1.0049 0.9634 -0.0650 -0.0522 -0.0968 185 GLN A OE1 1456 N NE2 . GLN A 185 ? 0.8873 0.9745 0.9363 -0.0573 -0.0504 -0.0854 185 GLN A NE2 1457 N N . ASN A 186 ? 0.7528 0.7853 0.7673 -0.0522 -0.0203 -0.0623 186 ASN A N 1458 C CA . ASN A 186 ? 0.7784 0.8004 0.7794 -0.0489 -0.0183 -0.0563 186 ASN A CA 1459 C C . ASN A 186 ? 0.8009 0.8127 0.8022 -0.0490 -0.0075 -0.0557 186 ASN A C 1460 O O . ASN A 186 ? 0.8179 0.8225 0.8112 -0.0490 -0.0042 -0.0544 186 ASN A O 1461 C CB . ASN A 186 ? 0.7655 0.7863 0.7609 -0.0435 -0.0221 -0.0505 186 ASN A CB 1462 C CG . ASN A 186 ? 0.7641 0.7766 0.7467 -0.0401 -0.0220 -0.0454 186 ASN A CG 1463 O OD1 . ASN A 186 ? 0.7830 0.7915 0.7601 -0.0415 -0.0203 -0.0457 186 ASN A OD1 1464 N ND2 . ASN A 186 ? 0.7898 0.7998 0.7681 -0.0357 -0.0239 -0.0411 186 ASN A ND2 1465 N N . ASP A 187 ? 0.7779 0.7888 0.7882 -0.0487 -0.0014 -0.0565 187 ASP A N 1466 C CA . ASP A 187 ? 0.8014 0.8007 0.8104 -0.0474 0.0097 -0.0548 187 ASP A CA 1467 C C . ASP A 187 ? 0.7704 0.7669 0.7845 -0.0526 0.0168 -0.0598 187 ASP A C 1468 O O . ASP A 187 ? 0.8164 0.8024 0.8227 -0.0511 0.0235 -0.0576 187 ASP A O 1469 C CB . ASP A 187 ? 0.8464 0.8442 0.8627 -0.0450 0.0149 -0.0536 187 ASP A CB 1470 C CG . ASP A 187 ? 0.9127 0.9090 0.9205 -0.0386 0.0100 -0.0476 187 ASP A CG 1471 O OD1 . ASP A 187 ? 0.9809 0.9806 0.9809 -0.0373 0.0011 -0.0456 187 ASP A OD1 1472 O OD2 . ASP A 187 ? 1.0042 0.9952 1.0131 -0.0351 0.0156 -0.0451 187 ASP A OD2 1473 N N . ASN A 188 ? 0.7628 0.7688 0.7902 -0.0585 0.0154 -0.0669 188 ASN A N 1474 C CA . ASN A 188 ? 0.7667 0.7708 0.7999 -0.0644 0.0217 -0.0730 188 ASN A CA 1475 C C . ASN A 188 ? 0.7804 0.7816 0.8016 -0.0650 0.0183 -0.0723 188 ASN A C 1476 O O . ASN A 188 ? 0.7432 0.7347 0.7605 -0.0660 0.0265 -0.0724 188 ASN A O 1477 C CB . ASN A 188 ? 0.7852 0.8026 0.8353 -0.0706 0.0183 -0.0819 188 ASN A CB 1478 C CG . ASN A 188 ? 0.7688 0.7890 0.8342 -0.0713 0.0240 -0.0840 188 ASN A CG 1479 O OD1 . ASN A 188 ? 0.7923 0.8017 0.8594 -0.0703 0.0359 -0.0819 188 ASN A OD1 1480 N ND2 . ASN A 188 ? 0.7500 0.7848 0.8268 -0.0727 0.0161 -0.0883 188 ASN A ND2 1481 N N . SER A 189 ? 0.7654 0.7741 0.7805 -0.0640 0.0070 -0.0714 189 SER A N 1482 C CA . SER A 189 ? 0.7435 0.7499 0.7476 -0.0646 0.0037 -0.0708 189 SER A CA 1483 C C . SER A 189 ? 0.7510 0.7458 0.7422 -0.0597 0.0079 -0.0638 189 SER A C 1484 O O . SER A 189 ? 0.7308 0.7198 0.7157 -0.0606 0.0111 -0.0638 189 SER A O 1485 C CB . SER A 189 ? 0.7290 0.7450 0.7290 -0.0640 -0.0083 -0.0710 189 SER A CB 1486 O OG . SER A 189 ? 0.6862 0.7032 0.6812 -0.0588 -0.0134 -0.0650 189 SER A OG 1487 N N . LEU A 190 ? 0.7811 0.7730 0.7686 -0.0542 0.0078 -0.0581 190 LEU A N 1488 C CA . LEU A 190 ? 0.7928 0.7748 0.7687 -0.0487 0.0111 -0.0520 190 LEU A CA 1489 C C . LEU A 190 ? 0.7922 0.7634 0.7668 -0.0485 0.0226 -0.0522 190 LEU A C 1490 O O . LEU A 190 ? 0.8300 0.7947 0.7955 -0.0459 0.0249 -0.0495 190 LEU A O 1491 C CB . LEU A 190 ? 0.7872 0.7678 0.7605 -0.0429 0.0097 -0.0472 190 LEU A CB 1492 C CG . LEU A 190 ? 0.7942 0.7665 0.7559 -0.0363 0.0113 -0.0415 190 LEU A CG 1493 C CD1 . LEU A 190 ? 0.8355 0.8085 0.7898 -0.0364 0.0069 -0.0406 190 LEU A CD1 1494 C CD2 . LEU A 190 ? 0.7687 0.7422 0.7281 -0.0315 0.0069 -0.0380 190 LEU A CD2 1495 N N . VAL A 191 ? 0.7933 0.7626 0.7776 -0.0511 0.0303 -0.0555 191 VAL A N 1496 C CA . VAL A 191 ? 0.7846 0.7417 0.7674 -0.0505 0.0429 -0.0552 191 VAL A CA 1497 C C . VAL A 191 ? 0.7890 0.7443 0.7710 -0.0552 0.0453 -0.0590 191 VAL A C 1498 O O . VAL A 191 ? 0.7940 0.7392 0.7671 -0.0521 0.0516 -0.0561 191 VAL A O 1499 C CB . VAL A 191 ? 0.7913 0.7459 0.7857 -0.0525 0.0518 -0.0579 191 VAL A CB 1500 C CG1 . VAL A 191 ? 0.7853 0.7255 0.7775 -0.0516 0.0663 -0.0574 191 VAL A CG1 1501 C CG2 . VAL A 191 ? 0.8083 0.7633 0.8016 -0.0470 0.0499 -0.0534 191 VAL A CG2 1502 N N . TYR A 192 ? 0.7780 0.7430 0.7684 -0.0621 0.0400 -0.0657 192 TYR A N 1503 C CA . TYR A 192 ? 0.7769 0.7411 0.7649 -0.0664 0.0405 -0.0695 192 TYR A CA 1504 C C . TYR A 192 ? 0.7782 0.7403 0.7525 -0.0620 0.0353 -0.0641 192 TYR A C 1505 O O . TYR A 192 ? 0.7619 0.7161 0.7293 -0.0612 0.0406 -0.0630 192 TYR A O 1506 C CB . TYR A 192 ? 0.8003 0.7769 0.7971 -0.0731 0.0327 -0.0772 192 TYR A CB 1507 C CG . TYR A 192 ? 0.8223 0.8019 0.8348 -0.0793 0.0383 -0.0851 192 TYR A CG 1508 C CD1 . TYR A 192 ? 0.7838 0.7576 0.8004 -0.0846 0.0469 -0.0908 192 TYR A CD1 1509 C CD2 . TYR A 192 ? 0.8153 0.8038 0.8396 -0.0800 0.0352 -0.0872 192 TYR A CD2 1510 C CE1 . TYR A 192 ? 0.8175 0.7945 0.8502 -0.0908 0.0524 -0.0988 192 TYR A CE1 1511 C CE2 . TYR A 192 ? 0.8222 0.8145 0.8630 -0.0859 0.0406 -0.0951 192 TYR A CE2 1512 C CZ . TYR A 192 ? 0.8446 0.8312 0.8899 -0.0916 0.0492 -0.1012 192 TYR A CZ 1513 O OH . TYR A 192 ? 0.8750 0.8658 0.9386 -0.0982 0.0550 -0.1100 192 TYR A OH 1514 N N . PHE A 193 ? 0.7497 0.7187 0.7205 -0.0588 0.0255 -0.0607 193 PHE A N 1515 C CA . PHE A 193 ? 0.7174 0.6855 0.6772 -0.0551 0.0205 -0.0561 193 PHE A CA 1516 C C . PHE A 193 ? 0.7251 0.6823 0.6773 -0.0497 0.0282 -0.0514 193 PHE A C 1517 O O . PHE A 193 ? 0.7470 0.7001 0.6927 -0.0490 0.0299 -0.0503 193 PHE A O 1518 C CB . PHE A 193 ? 0.6966 0.6717 0.6548 -0.0519 0.0111 -0.0527 193 PHE A CB 1519 C CG . PHE A 193 ? 0.6827 0.6584 0.6320 -0.0493 0.0055 -0.0493 193 PHE A CG 1520 C CD1 . PHE A 193 ? 0.6750 0.6448 0.6174 -0.0438 0.0078 -0.0445 193 PHE A CD1 1521 C CD2 . PHE A 193 ? 0.6928 0.6752 0.6410 -0.0520 -0.0020 -0.0509 193 PHE A CD2 1522 C CE1 . PHE A 193 ? 0.6825 0.6539 0.6190 -0.0419 0.0029 -0.0419 193 PHE A CE1 1523 C CE2 . PHE A 193 ? 0.6867 0.6691 0.6277 -0.0499 -0.0059 -0.0477 193 PHE A CE2 1524 C CZ . PHE A 193 ? 0.6715 0.6488 0.6077 -0.0452 -0.0033 -0.0435 193 PHE A CZ 1525 N N . ALA A 194 ? 0.7620 0.7142 0.7146 -0.0454 0.0331 -0.0485 194 ALA A N 1526 C CA . ALA A 194 ? 0.7775 0.7194 0.7211 -0.0383 0.0395 -0.0434 194 ALA A CA 1527 C C . ALA A 194 ? 0.7995 0.7321 0.7410 -0.0394 0.0496 -0.0447 194 ALA A C 1528 O O . ALA A 194 ? 0.8234 0.7508 0.7562 -0.0350 0.0515 -0.0415 194 ALA A O 1529 C CB . ALA A 194 ? 0.7750 0.7124 0.7188 -0.0334 0.0437 -0.0406 194 ALA A CB 1530 N N . TYR A 195 ? 0.8289 0.7595 0.7788 -0.0454 0.0564 -0.0497 195 TYR A N 1531 C CA . TYR A 195 ? 0.8646 0.7848 0.8128 -0.0469 0.0673 -0.0513 195 TYR A CA 1532 C C . TYR A 195 ? 0.8706 0.7930 0.8145 -0.0496 0.0636 -0.0529 195 TYR A C 1533 O O . TYR A 195 ? 0.8831 0.7972 0.8187 -0.0457 0.0690 -0.0498 195 TYR A O 1534 C CB . TYR A 195 ? 0.8721 0.7904 0.8323 -0.0540 0.0754 -0.0578 195 TYR A CB 1535 C CG . TYR A 195 ? 0.9037 0.8109 0.8629 -0.0566 0.0872 -0.0603 195 TYR A CG 1536 C CD1 . TYR A 195 ? 0.9342 0.8271 0.8833 -0.0497 0.0976 -0.0549 195 TYR A CD1 1537 C CD2 . TYR A 195 ? 0.9227 0.8336 0.8908 -0.0657 0.0880 -0.0685 195 TYR A CD2 1538 C CE1 . TYR A 195 ? 0.9141 0.7958 0.8621 -0.0519 0.1093 -0.0570 195 TYR A CE1 1539 C CE2 . TYR A 195 ? 0.9015 0.8015 0.8690 -0.0686 0.0993 -0.0713 195 TYR A CE2 1540 C CZ . TYR A 195 ? 0.8939 0.7790 0.8514 -0.0617 0.1103 -0.0653 195 TYR A CZ 1541 O OH . TYR A 195 ? 0.8714 0.7451 0.8279 -0.0643 0.1219 -0.0680 195 TYR A OH 1542 N N . TYR A 196 ? 0.8328 0.7662 0.7818 -0.0555 0.0544 -0.0573 196 TYR A N 1543 C CA . TYR A 196 ? 0.8221 0.7570 0.7675 -0.0590 0.0517 -0.0598 196 TYR A CA 1544 C C . TYR A 196 ? 0.8307 0.7675 0.7668 -0.0541 0.0453 -0.0546 196 TYR A C 1545 O O . TYR A 196 ? 0.8498 0.7859 0.7816 -0.0558 0.0446 -0.0556 196 TYR A O 1546 C CB . TYR A 196 ? 0.7737 0.7184 0.7271 -0.0667 0.0453 -0.0671 196 TYR A CB 1547 C CG . TYR A 196 ? 0.7685 0.7105 0.7319 -0.0727 0.0533 -0.0739 196 TYR A CG 1548 C CD1 . TYR A 196 ? 0.7890 0.7225 0.7515 -0.0762 0.0622 -0.0775 196 TYR A CD1 1549 C CD2 . TYR A 196 ? 0.7998 0.7474 0.7744 -0.0750 0.0527 -0.0770 196 TYR A CD2 1550 C CE1 . TYR A 196 ? 0.8059 0.7367 0.7791 -0.0824 0.0702 -0.0846 196 TYR A CE1 1551 C CE2 . TYR A 196 ? 0.8007 0.7466 0.7868 -0.0810 0.0605 -0.0840 196 TYR A CE2 1552 C CZ . TYR A 196 ? 0.8086 0.7460 0.7942 -0.0849 0.0693 -0.0880 196 TYR A CZ 1553 O OH . TYR A 196 ? 0.8580 0.7941 0.8566 -0.0915 0.0773 -0.0958 196 TYR A OH 1554 N N . HIS A 197 ? 0.8327 0.7715 0.7662 -0.0481 0.0413 -0.0495 197 HIS A N 1555 C CA . HIS A 197 ? 0.8638 0.8035 0.7898 -0.0426 0.0369 -0.0446 197 HIS A CA 1556 C C . HIS A 197 ? 0.8645 0.7952 0.7840 -0.0349 0.0439 -0.0399 197 HIS A C 1557 O O . HIS A 197 ? 0.9193 0.8517 0.8339 -0.0292 0.0399 -0.0360 197 HIS A O 1558 C CB . HIS A 197 ? 0.8553 0.8038 0.7824 -0.0409 0.0268 -0.0426 197 HIS A CB 1559 C CG . HIS A 197 ? 0.8324 0.7894 0.7627 -0.0465 0.0190 -0.0459 197 HIS A CG 1560 N ND1 . HIS A 197 ? 0.8109 0.7720 0.7480 -0.0518 0.0178 -0.0507 197 HIS A ND1 1561 C CD2 . HIS A 197 ? 0.8191 0.7811 0.7464 -0.0470 0.0122 -0.0452 197 HIS A CD2 1562 C CE1 . HIS A 197 ? 0.8228 0.7911 0.7598 -0.0547 0.0101 -0.0525 197 HIS A CE1 1563 N NE2 . HIS A 197 ? 0.8438 0.8119 0.7745 -0.0519 0.0071 -0.0490 197 HIS A NE2 1564 N N . GLY A 198 ? 0.8680 0.7892 0.7877 -0.0345 0.0543 -0.0405 198 GLY A N 1565 C CA . GLY A 198 ? 0.8923 0.8030 0.8041 -0.0268 0.0627 -0.0362 198 GLY A CA 1566 C C . GLY A 198 ? 0.8721 0.7791 0.7789 -0.0181 0.0638 -0.0314 198 GLY A C 1567 O O . GLY A 198 ? 0.8785 0.7792 0.7769 -0.0098 0.0676 -0.0272 198 GLY A O 1568 N N . LEU A 199 ? 0.8154 0.7260 0.7270 -0.0192 0.0608 -0.0321 199 LEU A N 1569 C CA . LEU A 199 ? 0.8377 0.7456 0.7440 -0.0110 0.0606 -0.0278 199 LEU A CA 1570 C C . LEU A 199 ? 0.8663 0.7622 0.7715 -0.0084 0.0727 -0.0268 199 LEU A C 1571 O O . LEU A 199 ? 0.8223 0.7127 0.7203 0.0000 0.0746 -0.0228 199 LEU A O 1572 C CB . LEU A 199 ? 0.8499 0.7686 0.7612 -0.0128 0.0499 -0.0285 199 LEU A CB 1573 C CG . LEU A 199 ? 0.8417 0.7721 0.7568 -0.0179 0.0389 -0.0306 199 LEU A CG 1574 C CD1 . LEU A 199 ? 0.8348 0.7733 0.7533 -0.0181 0.0302 -0.0304 199 LEU A CD1 1575 C CD2 . LEU A 199 ? 0.8804 0.8121 0.7895 -0.0137 0.0358 -0.0283 199 LEU A CD2 1576 N N . LEU A 200 ? 0.8906 0.7820 0.8027 -0.0154 0.0810 -0.0308 200 LEU A N 1577 C CA . LEU A 200 ? 0.9218 0.8030 0.8365 -0.0151 0.0927 -0.0310 200 LEU A CA 1578 C C . LEU A 200 ? 0.9937 0.8597 0.9042 -0.0134 0.1077 -0.0303 200 LEU A C 1579 O O . LEU A 200 ? 1.1446 0.9981 1.0496 -0.0070 0.1182 -0.0269 200 LEU A O 1580 C CB . LEU A 200 ? 0.8841 0.7728 0.8138 -0.0251 0.0914 -0.0372 200 LEU A CB 1581 C CG . LEU A 200 ? 0.8453 0.7472 0.7806 -0.0269 0.0792 -0.0380 200 LEU A CG 1582 C CD1 . LEU A 200 ? 0.8212 0.7262 0.7704 -0.0339 0.0825 -0.0430 200 LEU A CD1 1583 C CD2 . LEU A 200 ? 0.8594 0.7598 0.7855 -0.0175 0.0754 -0.0321 200 LEU A CD2 1584 N N . GLY A 201 ? 0.9666 0.8324 0.8794 -0.0189 0.1097 -0.0336 201 GLY A N 1585 C CA . GLY A 201 ? 0.9707 0.8214 0.8801 -0.0180 0.1246 -0.0335 201 GLY A CA 1586 C C . GLY A 201 ? 0.9915 0.8364 0.9121 -0.0253 0.1354 -0.0385 201 GLY A C 1587 O O . GLY A 201 ? 0.9333 0.7854 0.8636 -0.0293 0.1317 -0.0412 201 GLY A O 1588 N N . ASN A 202 ? 1.0743 0.9055 0.9938 -0.0264 0.1495 -0.0397 202 ASN A N 1589 C CA . ASN A 202 ? 1.0943 0.9211 1.0271 -0.0357 0.1601 -0.0465 202 ASN A CA 1590 C C . ASN A 202 ? 1.1293 0.9449 1.0646 -0.0329 0.1725 -0.0448 202 ASN A C 1591 O O . ASN A 202 ? 1.1289 0.9480 1.0798 -0.0415 0.1759 -0.0512 202 ASN A O 1592 C CB . ASN A 202 ? 1.2077 1.0237 1.1385 -0.0387 0.1707 -0.0489 202 ASN A CB 1593 C CG . ASN A 202 ? 1.3636 1.1787 1.3107 -0.0508 0.1787 -0.0585 202 ASN A CG 1594 O OD1 . ASN A 202 ? 1.5338 1.3330 1.4818 -0.0514 0.1955 -0.0594 202 ASN A OD1 1595 N ND2 . ASN A 202 ? 1.3167 1.1487 1.2767 -0.0604 0.1668 -0.0660 202 ASN A ND2 1596 N N . ARG A 203 ? 1.1408 0.9433 1.0613 -0.0208 0.1796 -0.0365 203 ARG A N 1597 C CA . ARG A 203 ? 1.1499 0.9407 1.0711 -0.0172 0.1919 -0.0341 203 ARG A CA 1598 C C . ARG A 203 ? 1.1120 0.9169 1.0433 -0.0204 0.1814 -0.0362 203 ARG A C 1599 O O . ARG A 203 ? 1.1306 0.9356 1.0761 -0.0270 0.1878 -0.0408 203 ARG A O 1600 C CB . ARG A 203 ? 1.2428 1.0178 1.1434 -0.0018 0.1992 -0.0244 203 ARG A CB 1601 C CG . ARG A 203 ? 1.3709 1.1283 1.2608 0.0030 0.2133 -0.0214 203 ARG A CG 1602 C CD . ARG A 203 ? 1.5130 1.2509 1.3847 0.0178 0.2256 -0.0126 203 ARG A CD 1603 N NE . ARG A 203 ? 1.7429 1.4673 1.5993 0.0263 0.2335 -0.0078 203 ARG A NE 1604 C CZ . ARG A 203 ? 1.8382 1.5479 1.6958 0.0231 0.2495 -0.0094 203 ARG A CZ 1605 N NH1 . ARG A 203 ? 1.8795 1.5860 1.7540 0.0108 0.2597 -0.0166 203 ARG A NH1 1606 N NH2 . ARG A 203 ? 1.7859 1.4840 1.6281 0.0325 0.2556 -0.0042 203 ARG A NH2 1607 N N . LEU A 204 ? 1.0564 0.8735 0.9813 -0.0160 0.1655 -0.0330 204 LEU A N 1608 C CA . LEU A 204 ? 1.0209 0.8513 0.9541 -0.0183 0.1549 -0.0344 204 LEU A CA 1609 C C . LEU A 204 ? 1.0002 0.8456 0.9529 -0.0317 0.1484 -0.0435 204 LEU A C 1610 O O . LEU A 204 ? 0.9323 0.7827 0.8977 -0.0362 0.1491 -0.0469 204 LEU A O 1611 C CB . LEU A 204 ? 1.0134 0.8528 0.9354 -0.0109 0.1397 -0.0295 204 LEU A CB 1612 C CG . LEU A 204 ? 0.9909 0.8443 0.9197 -0.0127 0.1274 -0.0305 204 LEU A CG 1613 C CD1 . LEU A 204 ? 0.9700 0.8161 0.9019 -0.0103 0.1362 -0.0291 204 LEU A CD1 1614 C CD2 . LEU A 204 ? 1.0196 0.8797 0.9365 -0.0051 0.1142 -0.0258 204 LEU A CD2 1615 N N . TRP A 205 ? 0.9782 0.8309 0.9331 -0.0376 0.1420 -0.0476 205 TRP A N 1616 C CA . TRP A 205 ? 0.9692 0.8354 0.9413 -0.0497 0.1362 -0.0568 205 TRP A CA 1617 C C . TRP A 205 ? 1.0163 0.8762 1.0032 -0.0567 0.1502 -0.0631 205 TRP A C 1618 O O . TRP A 205 ? 0.9924 0.8627 0.9947 -0.0630 0.1470 -0.0687 205 TRP A O 1619 C CB . TRP A 205 ? 0.9619 0.8334 0.9317 -0.0541 0.1298 -0.0601 205 TRP A CB 1620 C CG . TRP A 205 ? 0.9658 0.8520 0.9501 -0.0649 0.1214 -0.0693 205 TRP A CG 1621 C CD1 . TRP A 205 ? 0.9573 0.8434 0.9493 -0.0734 0.1255 -0.0771 205 TRP A CD1 1622 C CD2 . TRP A 205 ? 0.9987 0.9019 0.9908 -0.0678 0.1074 -0.0718 205 TRP A CD2 1623 N NE1 . TRP A 205 ? 0.9534 0.8559 0.9570 -0.0810 0.1142 -0.0846 205 TRP A NE1 1624 C CE2 . TRP A 205 ? 0.9664 0.8795 0.9702 -0.0775 0.1032 -0.0812 205 TRP A CE2 1625 C CE3 . TRP A 205 ? 0.9952 0.9058 0.9850 -0.0628 0.0982 -0.0672 205 TRP A CE3 1626 C CZ2 . TRP A 205 ? 0.9678 0.8978 0.9804 -0.0816 0.0900 -0.0857 205 TRP A CZ2 1627 C CZ3 . TRP A 205 ? 0.9779 0.9049 0.9770 -0.0674 0.0857 -0.0715 205 TRP A CZ3 1628 C CH2 . TRP A 205 ? 0.9752 0.9117 0.9853 -0.0763 0.0817 -0.0804 205 TRP A CH2 1629 N N . SER A 206 ? 1.0741 0.9167 1.0568 -0.0553 0.1662 -0.0622 206 SER A N 1630 C CA . SER A 206 ? 1.1466 0.9814 1.1439 -0.0620 0.1816 -0.0681 206 SER A CA 1631 C C . SER A 206 ? 1.1606 0.9953 1.1653 -0.0601 0.1854 -0.0667 206 SER A C 1632 O O . SER A 206 ? 1.2026 1.0444 1.2269 -0.0687 0.1878 -0.0744 206 SER A O 1633 C CB . SER A 206 ? 1.1898 1.0024 1.1779 -0.0581 0.2002 -0.0650 206 SER A CB 1634 O OG . SER A 206 ? 1.2427 1.0547 1.2286 -0.0624 0.1996 -0.0685 206 SER A OG 1635 N N . SER A 207 ? 1.1210 0.9476 1.1103 -0.0485 0.1863 -0.0571 207 SER A N 1636 C CA . SER A 207 ? 1.1322 0.9561 1.1259 -0.0454 0.1913 -0.0548 207 SER A CA 1637 C C . SER A 207 ? 1.0709 0.9159 1.0801 -0.0521 0.1769 -0.0602 207 SER A C 1638 O O . SER A 207 ? 1.1355 0.9844 1.1626 -0.0584 0.1821 -0.0658 207 SER A O 1639 C CB . SER A 207 ? 1.1917 1.0054 1.1639 -0.0311 0.1912 -0.0439 207 SER A CB 1640 O OG . SER A 207 ? 1.2831 1.0763 1.2401 -0.0234 0.2055 -0.0385 207 SER A OG 1641 N N . LEU A 208 ? 1.0534 0.9118 1.0561 -0.0505 0.1594 -0.0587 208 LEU A N 1642 C CA . LEU A 208 ? 0.9953 0.8737 1.0101 -0.0557 0.1446 -0.0630 208 LEU A CA 1643 C C . LEU A 208 ? 1.0100 0.8988 1.0474 -0.0680 0.1456 -0.0743 208 LEU A C 1644 O O . LEU A 208 ? 1.0273 0.9248 1.0799 -0.0717 0.1446 -0.0782 208 LEU A O 1645 C CB . LEU A 208 ? 0.9753 0.8644 0.9792 -0.0533 0.1275 -0.0605 208 LEU A CB 1646 C CG . LEU A 208 ? 0.9964 0.8812 0.9826 -0.0420 0.1226 -0.0511 208 LEU A CG 1647 C CD1 . LEU A 208 ? 0.9894 0.8789 0.9631 -0.0390 0.1111 -0.0483 208 LEU A CD1 1648 C CD2 . LEU A 208 ? 1.0181 0.9120 1.0095 -0.0405 0.1150 -0.0501 208 LEU A CD2 1649 N N . GLN A 209 ? 1.0268 0.9149 1.0664 -0.0741 0.1475 -0.0797 209 GLN A N 1650 C CA . GLN A 209 ? 1.0307 0.9280 1.0912 -0.0859 0.1489 -0.0915 209 GLN A CA 1651 C C . GLN A 209 ? 1.0550 0.9459 1.1321 -0.0897 0.1643 -0.0955 209 GLN A C 1652 O O . GLN A 209 ? 1.0567 0.9611 1.1540 -0.0966 0.1612 -0.1033 209 GLN A O 1653 C CB . GLN A 209 ? 1.0385 0.9299 1.0956 -0.0905 0.1530 -0.0956 209 GLN A CB 1654 C CG . GLN A 209 ? 1.0464 0.9476 1.0932 -0.0902 0.1374 -0.0952 209 GLN A CG 1655 C CD . GLN A 209 ? 1.0650 0.9869 1.1257 -0.0980 0.1234 -0.1042 209 GLN A CD 1656 O OE1 . GLN A 209 ? 1.0586 0.9853 1.1284 -0.1062 0.1231 -0.1135 209 GLN A OE1 1657 N NE2 . GLN A 209 ? 1.1034 1.0373 1.1658 -0.0951 0.1121 -0.1018 209 GLN A NE2 1658 N N . THR A 210 ? 1.0813 0.9513 1.1497 -0.0847 0.1814 -0.0901 210 THR A N 1659 C CA . THR A 210 ? 1.0877 0.9474 1.1697 -0.0874 0.1993 -0.0928 210 THR A CA 1660 C C . THR A 210 ? 1.0877 0.9556 1.1799 -0.0859 0.1965 -0.0919 210 THR A C 1661 O O . THR A 210 ? 1.0092 0.8848 1.1244 -0.0939 0.2009 -0.1003 210 THR A O 1662 C CB . THR A 210 ? 1.1027 0.9364 1.1674 -0.0787 0.2173 -0.0840 210 THR A CB 1663 O OG1 . THR A 210 ? 1.1039 0.9286 1.1615 -0.0806 0.2225 -0.0856 210 THR A OG1 1664 C CG2 . THR A 210 ? 1.1018 0.9232 1.1792 -0.0804 0.2368 -0.0857 210 THR A CG2 1665 N N . HIS A 211 ? 1.0722 0.9388 1.1478 -0.0756 0.1893 -0.0821 211 HIS A N 1666 C CA . HIS A 211 ? 1.0898 0.9592 1.1706 -0.0719 0.1895 -0.0792 211 HIS A CA 1667 C C . HIS A 211 ? 1.0881 0.9809 1.1789 -0.0750 0.1706 -0.0827 211 HIS A C 1668 O O . HIS A 211 ? 1.1262 1.0255 1.2302 -0.0760 0.1712 -0.0843 211 HIS A O 1669 C CB . HIS A 211 ? 1.1649 1.0186 1.2214 -0.0585 0.1930 -0.0669 211 HIS A CB 1670 C CG . HIS A 211 ? 1.2208 1.0505 1.2644 -0.0531 0.2113 -0.0620 211 HIS A CG 1671 N ND1 . HIS A 211 ? 1.2516 1.0688 1.2696 -0.0419 0.2110 -0.0527 211 HIS A ND1 1672 C CD2 . HIS A 211 ? 1.2410 1.0567 1.2937 -0.0571 0.2309 -0.0654 211 HIS A CD2 1673 C CE1 . HIS A 211 ? 1.3025 1.0987 1.3132 -0.0384 0.2294 -0.0499 211 HIS A CE1 1674 N NE2 . HIS A 211 ? 1.2782 1.0722 1.3093 -0.0477 0.2422 -0.0574 211 HIS A NE2 1675 N N . CYS A 212 ? 1.0662 0.9709 1.1505 -0.0761 0.1545 -0.0836 212 CYS A N 1676 C CA . CYS A 212 ? 1.0166 0.9418 1.1071 -0.0776 0.1366 -0.0859 212 CYS A CA 1677 C C . CYS A 212 ? 0.9953 0.9381 1.1036 -0.0880 0.1282 -0.0972 212 CYS A C 1678 O O . CYS A 212 ? 0.9504 0.9103 1.0640 -0.0891 0.1136 -0.0996 212 CYS A O 1679 C CB . CYS A 212 ? 0.9813 0.9080 1.0506 -0.0705 0.1233 -0.0784 212 CYS A CB 1680 S SG . CYS A 212 ? 0.9612 0.8685 1.0068 -0.0574 0.1304 -0.0658 212 CYS A SG 1681 N N . CYS A 213 ? 1.0312 0.9694 1.1471 -0.0950 0.1370 -0.1041 213 CYS A N 1682 C CA . CYS A 213 ? 1.0904 1.0446 1.2198 -0.1042 0.1279 -0.1151 213 CYS A CA 1683 C C . CYS A 213 ? 1.1176 1.0699 1.2679 -0.1136 0.1410 -0.1257 213 CYS A C 1684 O O . CYS A 213 ? 1.1402 1.0743 1.2874 -0.1135 0.1577 -0.1240 213 CYS A O 1685 C CB . CYS A 213 ? 1.1007 1.0533 1.2134 -0.1035 0.1202 -0.1137 213 CYS A CB 1686 S SG . CYS A 213 ? 1.1180 1.0667 1.2034 -0.0922 0.1094 -0.1006 213 CYS A SG 1687 N N . SER A 214 ? 1.1980 1.1693 1.3696 -0.1214 0.1334 -0.1368 214 SER A N 1688 C CA . SER A 214 ? 1.3433 1.3168 1.5357 -0.1320 0.1421 -0.1495 214 SER A CA 1689 C C . SER A 214 ? 1.3162 1.3060 1.5119 -0.1380 0.1272 -0.1591 214 SER A C 1690 O O . SER A 214 ? 1.3064 1.3161 1.5088 -0.1383 0.1114 -0.1629 214 SER A O 1691 C CB . SER A 214 ? 1.4438 1.4258 1.6631 -0.1366 0.1486 -0.1564 214 SER A CB 1692 O OG . SER A 214 ? 1.4696 1.4757 1.7008 -0.1379 0.1314 -0.1618 214 SER A OG 1693 N N . GLN A 215 ? 1.3086 1.2889 1.4981 -0.1419 0.1328 -0.1624 215 GLN A N 1694 C CA . GLN A 215 ? 1.3364 1.3291 1.5330 -0.1498 0.1238 -0.1744 215 GLN A CA 1695 C C . GLN A 215 ? 1.3530 1.3680 1.5488 -0.1485 0.1015 -0.1773 215 GLN A C 1696 O O . GLN A 215 ? 1.2611 1.2944 1.4768 -0.1526 0.0945 -0.1864 215 GLN A O 1697 C CB . GLN A 215 ? 1.3357 1.3311 1.5599 -0.1608 0.1354 -0.1886 215 GLN A CB 1698 C CG . GLN A 215 ? 1.3276 1.3325 1.5760 -0.1629 0.1395 -0.1925 215 GLN A CG 1699 C CD . GLN A 215 ? 1.4105 1.4048 1.6797 -0.1708 0.1607 -0.2001 215 GLN A CD 1700 O OE1 . GLN A 215 ? 1.3393 1.3192 1.6057 -0.1752 0.1725 -0.2032 215 GLN A OE1 1701 N NE2 . GLN A 215 ? 1.4907 1.4916 1.7815 -0.1726 0.1664 -0.2031 215 GLN A NE2 1702 N N . ASN A 216 ? 1.4214 1.4343 1.5938 -0.1423 0.0912 -0.1692 216 ASN A N 1703 C CA . ASN A 216 ? 1.4193 1.4499 1.5861 -0.1401 0.0710 -0.1708 216 ASN A CA 1704 C C . ASN A 216 ? 1.3550 1.3954 1.5193 -0.1327 0.0605 -0.1633 216 ASN A C 1705 O O . ASN A 216 ? 1.3096 1.3657 1.4725 -0.1310 0.0446 -0.1654 216 ASN A O 1706 C CB . ASN A 216 ? 1.4401 1.4874 1.6239 -0.1487 0.0636 -0.1866 216 ASN A CB 1707 C CG . ASN A 216 ? 1.4172 1.4590 1.5895 -0.1520 0.0624 -0.1909 216 ASN A CG 1708 O OD1 . ASN A 216 ? 1.3709 1.4156 1.5256 -0.1478 0.0504 -0.1871 216 ASN A OD1 1709 N ND2 . ASN A 216 ? 1.3920 1.4250 1.5743 -0.1597 0.0756 -0.1987 216 ASN A ND2 1710 N N . LYS A 217 ? 1.2637 1.2937 1.4259 -0.1278 0.0697 -0.1543 217 LYS A N 1711 C CA . LYS A 217 ? 1.1419 1.1753 1.2937 -0.1194 0.0608 -0.1443 217 LYS A CA 1712 C C . LYS A 217 ? 1.1192 1.1357 1.2624 -0.1132 0.0728 -0.1333 217 LYS A C 1713 O O . LYS A 217 ? 1.0537 1.0617 1.2079 -0.1155 0.0873 -0.1348 217 LYS A O 1714 C CB . LYS A 217 ? 1.1285 1.1813 1.2981 -0.1204 0.0518 -0.1500 217 LYS A CB 1715 C CG . LYS A 217 ? 1.0897 1.1504 1.2467 -0.1127 0.0373 -0.1424 217 LYS A CG 1716 C CD . LYS A 217 ? 1.1115 1.1926 1.2861 -0.1134 0.0275 -0.1489 217 LYS A CD 1717 C CE . LYS A 217 ? 1.1534 1.2344 1.3477 -0.1149 0.0386 -0.1503 217 LYS A CE 1718 N NZ . LYS A 217 ? 1.2063 1.2961 1.4029 -0.1088 0.0316 -0.1452 217 LYS A NZ 1719 N N . CYS A 218 ? 1.0765 1.0883 1.1998 -0.1051 0.0666 -0.1226 218 CYS A N 1720 C CA . CYS A 218 ? 1.0590 1.0563 1.1717 -0.0978 0.0751 -0.1120 218 CYS A CA 1721 C C . CYS A 218 ? 1.0152 1.0209 1.1300 -0.0928 0.0678 -0.1076 218 CYS A C 1722 O O . CYS A 218 ? 1.0145 1.0350 1.1308 -0.0925 0.0537 -0.1094 218 CYS A O 1723 C CB . CYS A 218 ? 1.0782 1.0640 1.1672 -0.0921 0.0735 -0.1034 218 CYS A CB 1724 S SG . CYS A 218 ? 1.0693 1.0396 1.1523 -0.0956 0.0860 -0.1055 218 CYS A SG 1725 N N . ASN A 219 ? 0.9783 0.9737 1.0926 -0.0884 0.0779 -0.1018 219 ASN A N 1726 C CA . ASN A 219 ? 0.9397 0.9385 1.0499 -0.0818 0.0719 -0.0952 219 ASN A CA 1727 C C . ASN A 219 ? 0.9004 0.8825 0.9894 -0.0734 0.0766 -0.0844 219 ASN A C 1728 O O . ASN A 219 ? 0.8688 0.8364 0.9558 -0.0707 0.0904 -0.0811 219 ASN A O 1729 C CB . ASN A 219 ? 0.9609 0.9637 1.0901 -0.0832 0.0788 -0.0982 219 ASN A CB 1730 C CG . ASN A 219 ? 0.9468 0.9528 1.0713 -0.0762 0.0727 -0.0914 219 ASN A CG 1731 O OD1 . ASN A 219 ? 0.8735 0.8807 0.9824 -0.0710 0.0620 -0.0855 219 ASN A OD1 1732 N ND2 . ASN A 219 ? 0.9626 0.9698 1.1016 -0.0763 0.0799 -0.0926 219 ASN A ND2 1733 N N . PHE A 220 ? 0.8651 0.8491 0.9381 -0.0691 0.0652 -0.0795 220 PHE A N 1734 C CA . PHE A 220 ? 0.8589 0.8307 0.9124 -0.0606 0.0664 -0.0698 220 PHE A CA 1735 C C . PHE A 220 ? 0.8834 0.8610 0.9336 -0.0553 0.0577 -0.0651 220 PHE A C 1736 O O . PHE A 220 ? 0.9416 0.9113 0.9765 -0.0482 0.0566 -0.0579 220 PHE A O 1737 C CB . PHE A 220 ? 0.8147 0.7840 0.8534 -0.0595 0.0607 -0.0675 220 PHE A CB 1738 C CG . PHE A 220 ? 0.7766 0.7391 0.8162 -0.0640 0.0689 -0.0715 220 PHE A CG 1739 C CD1 . PHE A 220 ? 0.7833 0.7311 0.8231 -0.0632 0.0845 -0.0705 220 PHE A CD1 1740 C CD2 . PHE A 220 ? 0.7399 0.7090 0.7783 -0.0685 0.0616 -0.0756 220 PHE A CD2 1741 C CE1 . PHE A 220 ? 0.7894 0.7297 0.8294 -0.0672 0.0928 -0.0739 220 PHE A CE1 1742 C CE2 . PHE A 220 ? 0.7684 0.7304 0.8069 -0.0726 0.0694 -0.0793 220 PHE A CE2 1743 C CZ . PHE A 220 ? 0.7731 0.7209 0.8129 -0.0722 0.0851 -0.0786 220 PHE A CZ 1744 N N . TYR A 221 ? 0.8858 0.8773 0.9504 -0.0584 0.0517 -0.0695 221 TYR A N 1745 C CA . TYR A 221 ? 0.8845 0.8818 0.9470 -0.0536 0.0438 -0.0655 221 TYR A CA 1746 C C . TYR A 221 ? 0.8779 0.8675 0.9438 -0.0496 0.0534 -0.0621 221 TYR A C 1747 O O . TYR A 221 ? 0.8478 0.8281 0.8998 -0.0426 0.0544 -0.0551 221 TYR A O 1748 C CB . TYR A 221 ? 0.8886 0.9043 0.9640 -0.0576 0.0326 -0.0713 221 TYR A CB 1749 C CG . TYR A 221 ? 0.8906 0.9128 0.9655 -0.0528 0.0251 -0.0675 221 TYR A CG 1750 C CD1 . TYR A 221 ? 0.8904 0.9064 0.9482 -0.0464 0.0203 -0.0599 221 TYR A CD1 1751 C CD2 . TYR A 221 ? 0.8754 0.9104 0.9676 -0.0547 0.0226 -0.0721 221 TYR A CD2 1752 C CE1 . TYR A 221 ? 0.9025 0.9235 0.9597 -0.0422 0.0140 -0.0567 221 TYR A CE1 1753 C CE2 . TYR A 221 ? 0.8887 0.9290 0.9801 -0.0500 0.0161 -0.0685 221 TYR A CE2 1754 C CZ . TYR A 221 ? 0.9349 0.9676 1.0085 -0.0439 0.0122 -0.0607 221 TYR A CZ 1755 O OH . TYR A 221 ? 0.9719 1.0090 1.0446 -0.0393 0.0064 -0.0573 221 TYR A OH 1756 N N . ASP A 222 ? 0.9236 0.9173 1.0083 -0.0540 0.0607 -0.0676 222 ASP A N 1757 C CA . ASP A 222 ? 0.9753 0.9635 1.0656 -0.0506 0.0695 -0.0650 222 ASP A CA 1758 C C . ASP A 222 ? 0.9669 0.9466 1.0692 -0.0544 0.0859 -0.0687 222 ASP A C 1759 O O . ASP A 222 ? 1.0145 0.9957 1.1316 -0.0555 0.0933 -0.0708 222 ASP A O 1760 C CB . ASP A 222 ? 0.9734 0.9777 1.0778 -0.0514 0.0611 -0.0677 222 ASP A CB 1761 C CG . ASP A 222 ? 0.9423 0.9637 1.0672 -0.0595 0.0564 -0.0777 222 ASP A CG 1762 O OD1 . ASP A 222 ? 0.9351 0.9547 1.0671 -0.0653 0.0628 -0.0833 222 ASP A OD1 1763 O OD2 . ASP A 222 ? 0.9580 0.9948 1.0916 -0.0596 0.0460 -0.0801 222 ASP A OD2 1764 N N . ASN A 223 ? 0.9960 0.9660 1.0918 -0.0563 0.0924 -0.0693 223 ASN A N 1765 C CA . ASN A 223 ? 1.0477 1.0080 1.1540 -0.0604 0.1089 -0.0731 223 ASN A CA 1766 C C . ASN A 223 ? 1.0796 1.0230 1.1800 -0.0538 0.1232 -0.0667 223 ASN A C 1767 O O . ASN A 223 ? 1.0462 0.9783 1.1257 -0.0451 0.1227 -0.0583 223 ASN A O 1768 C CB . ASN A 223 ? 1.1101 1.0616 1.2066 -0.0622 0.1125 -0.0737 223 ASN A CB 1769 C CG . ASN A 223 ? 1.1296 1.0765 1.2419 -0.0697 0.1266 -0.0809 223 ASN A CG 1770 O OD1 . ASN A 223 ? 1.2050 1.1422 1.3250 -0.0693 0.1412 -0.0806 223 ASN A OD1 1771 N ND2 . ASN A 223 ? 1.1493 1.1019 1.2658 -0.0764 0.1230 -0.0874 223 ASN A ND2 1772 N N . LYS A 224 ? 1.1398 1.0815 1.2587 -0.0578 0.1360 -0.0711 224 LYS A N 1773 C CA . LYS A 224 ? 1.1781 1.1038 1.2931 -0.0516 0.1507 -0.0654 224 LYS A CA 1774 C C . LYS A 224 ? 1.1773 1.0817 1.2850 -0.0502 0.1690 -0.0633 224 LYS A C 1775 O O . LYS A 224 ? 1.2412 1.1289 1.3410 -0.0436 0.1822 -0.0575 224 LYS A O 1776 C CB . LYS A 224 ? 1.1811 1.1168 1.3210 -0.0558 0.1550 -0.0706 224 LYS A CB 1777 C CG . LYS A 224 ? 1.1587 1.1125 1.3034 -0.0547 0.1388 -0.0708 224 LYS A CG 1778 C CD . LYS A 224 ? 1.1898 1.1342 1.3127 -0.0440 0.1355 -0.0606 224 LYS A CD 1779 C CE . LYS A 224 ? 1.1841 1.1454 1.3108 -0.0428 0.1199 -0.0606 224 LYS A CE 1780 N NZ . LYS A 224 ? 1.1990 1.1740 1.3215 -0.0456 0.1028 -0.0630 224 LYS A NZ 1781 N N . ASP A 225 ? 1.1477 1.0515 1.2568 -0.0557 0.1702 -0.0677 225 ASP A N 1782 C CA . ASP A 225 ? 1.1810 1.0635 1.2808 -0.0537 0.1874 -0.0652 225 ASP A CA 1783 C C . ASP A 225 ? 1.2002 1.0666 1.2698 -0.0411 0.1873 -0.0540 225 ASP A C 1784 O O . ASP A 225 ? 1.1800 1.0521 1.2351 -0.0379 0.1729 -0.0510 225 ASP A O 1785 C CB . ASP A 225 ? 1.2090 1.0952 1.3146 -0.0618 0.1866 -0.0720 225 ASP A CB 1786 C CG . ASP A 225 ? 1.2644 1.1290 1.3656 -0.0614 0.2067 -0.0711 225 ASP A CG 1787 O OD1 . ASP A 225 ? 1.2857 1.1306 1.3663 -0.0512 0.2161 -0.0618 225 ASP A OD1 1788 O OD2 . ASP A 225 ? 1.2209 1.0879 1.3388 -0.0710 0.2132 -0.0798 225 ASP A OD2 1789 N N . LEU A 226 ? 1.2316 1.0781 1.2920 -0.0338 0.2035 -0.0481 226 LEU A N 1790 C CA . LEU A 226 ? 1.2533 1.0845 1.2850 -0.0206 0.2037 -0.0377 226 LEU A CA 1791 C C . LEU A 226 ? 1.2575 1.0798 1.2706 -0.0167 0.2030 -0.0346 226 LEU A C 1792 O O . LEU A 226 ? 1.2506 1.0696 1.2421 -0.0076 0.1945 -0.0282 226 LEU A O 1793 C CB . LEU A 226 ? 1.2889 1.0998 1.3151 -0.0134 0.2226 -0.0325 226 LEU A CB 1794 C CG . LEU A 226 ? 1.2937 1.1123 1.3341 -0.0145 0.2223 -0.0337 226 LEU A CG 1795 C CD1 . LEU A 226 ? 1.3441 1.1481 1.3962 -0.0156 0.2448 -0.0345 226 LEU A CD1 1796 C CD2 . LEU A 226 ? 1.2632 1.0799 1.2833 -0.0036 0.2127 -0.0260 226 LEU A CD2 1797 N N . GLU A 227 ? 1.2596 1.0781 1.2818 -0.0237 0.2121 -0.0396 227 GLU A N 1798 C CA . GLU A 227 ? 1.2214 1.0336 1.2288 -0.0214 0.2108 -0.0377 227 GLU A CA 1799 C C . GLU A 227 ? 1.1874 1.0193 1.1962 -0.0261 0.1903 -0.0410 227 GLU A C 1800 O O . GLU A 227 ? 1.1430 0.9721 1.1343 -0.0207 0.1840 -0.0369 227 GLU A O 1801 C CB . GLU A 227 ? 1.2638 1.0649 1.2805 -0.0276 0.2278 -0.0422 227 GLU A CB 1802 C CG . GLU A 227 ? 1.3031 1.0772 1.3040 -0.0179 0.2481 -0.0349 227 GLU A CG 1803 C CD . GLU A 227 ? 1.3141 1.0754 1.3174 -0.0219 0.2630 -0.0377 227 GLU A CD 1804 O OE1 . GLU A 227 ? 1.2935 1.0456 1.2772 -0.0152 0.2624 -0.0328 227 GLU A OE1 1805 O OE2 . GLU A 227 ? 1.2736 1.0346 1.2990 -0.0320 0.2748 -0.0452 227 GLU A OE2 1806 N N . CYS A 228 ? 1.1538 1.0055 1.1829 -0.0356 0.1803 -0.0483 228 CYS A N 1807 C CA . CYS A 228 ? 1.1092 0.9795 1.1384 -0.0390 0.1604 -0.0508 228 CYS A CA 1808 C C . CYS A 228 ? 1.0688 0.9409 1.0803 -0.0296 0.1485 -0.0434 228 CYS A C 1809 O O . CYS A 228 ? 1.0703 0.9459 1.0694 -0.0269 0.1378 -0.0410 228 CYS A O 1810 C CB . CYS A 228 ? 1.0815 0.9720 1.1349 -0.0496 0.1524 -0.0599 228 CYS A CB 1811 S SG . CYS A 228 ? 1.0035 0.9157 1.0561 -0.0530 0.1289 -0.0627 228 CYS A SG 1812 N N . VAL A 229 ? 1.0521 0.9213 1.0631 -0.0246 0.1510 -0.0399 229 VAL A N 1813 C CA . VAL A 229 ? 1.0387 0.9093 1.0338 -0.0160 0.1402 -0.0336 229 VAL A CA 1814 C C . VAL A 229 ? 1.0658 0.9231 1.0367 -0.0059 0.1411 -0.0268 229 VAL A C 1815 O O . VAL A 229 ? 1.1050 0.9688 1.0650 -0.0023 0.1277 -0.0244 229 VAL A O 1816 C CB . VAL A 229 ? 0.9993 0.8663 0.9969 -0.0118 0.1450 -0.0310 229 VAL A CB 1817 C CG1 . VAL A 229 ? 0.9941 0.8583 0.9720 -0.0015 0.1363 -0.0242 229 VAL A CG1 1818 C CG2 . VAL A 229 ? 1.0030 0.8880 1.0236 -0.0206 0.1387 -0.0375 229 VAL A CG2 1819 N N . THR A 230 ? 1.0586 0.8975 1.0214 -0.0012 0.1570 -0.0238 230 THR A N 1820 C CA . THR A 230 ? 1.0408 0.8666 0.9802 0.0094 0.1587 -0.0173 230 THR A CA 1821 C C . THR A 230 ? 1.0448 0.8790 0.9809 0.0065 0.1482 -0.0191 230 THR A C 1822 O O . THR A 230 ? 1.0959 0.9293 1.0157 0.0142 0.1404 -0.0148 230 THR A O 1823 C CB . THR A 230 ? 1.0658 0.8696 0.9982 0.0144 0.1792 -0.0143 230 THR A CB 1824 O OG1 . THR A 230 ? 1.0673 0.8630 1.0037 0.0166 0.1898 -0.0128 230 THR A OG1 1825 C CG2 . THR A 230 ? 1.0729 0.8627 0.9794 0.0274 0.1810 -0.0071 230 THR A CG2 1826 N N . ASN A 231 ? 1.0349 0.8776 0.9871 -0.0044 0.1481 -0.0257 231 ASN A N 1827 C CA . ASN A 231 ? 1.0147 0.8653 0.9652 -0.0080 0.1390 -0.0278 231 ASN A CA 1828 C C . ASN A 231 ? 1.0230 0.8921 0.9765 -0.0110 0.1203 -0.0295 231 ASN A C 1829 O O . ASN A 231 ? 1.0317 0.9043 0.9750 -0.0081 0.1111 -0.0276 231 ASN A O 1830 C CB . ASN A 231 ? 1.0446 0.8961 1.0100 -0.0184 0.1463 -0.0347 231 ASN A CB 1831 C CG . ASN A 231 ? 1.0806 0.9123 1.0396 -0.0151 0.1646 -0.0326 231 ASN A CG 1832 O OD1 . ASN A 231 ? 1.0691 0.8879 1.0090 -0.0045 0.1686 -0.0257 231 ASN A OD1 1833 N ND2 . ASN A 231 ? 1.0995 0.9284 1.0745 -0.0237 0.1761 -0.0386 231 ASN A ND2 1834 N N . LEU A 232 ? 0.9868 0.8675 0.9544 -0.0165 0.1149 -0.0331 232 LEU A N 1835 C CA . LEU A 232 ? 0.9805 0.8770 0.9494 -0.0181 0.0980 -0.0339 232 LEU A CA 1836 C C . LEU A 232 ? 0.9817 0.8743 0.9329 -0.0079 0.0918 -0.0273 232 LEU A C 1837 O O . LEU A 232 ? 1.0140 0.9148 0.9598 -0.0073 0.0797 -0.0267 232 LEU A O 1838 C CB . LEU A 232 ? 0.9628 0.8711 0.9484 -0.0240 0.0941 -0.0380 232 LEU A CB 1839 C CG . LEU A 232 ? 0.9676 0.8862 0.9720 -0.0349 0.0941 -0.0463 232 LEU A CG 1840 C CD1 . LEU A 232 ? 0.9567 0.8866 0.9784 -0.0393 0.0915 -0.0503 232 LEU A CD1 1841 C CD2 . LEU A 232 ? 0.9665 0.8957 0.9693 -0.0390 0.0821 -0.0489 232 LEU A CD2 1842 N N . GLN A 233 ? 0.9934 0.8732 0.9355 0.0001 0.1005 -0.0227 233 GLN A N 1843 C CA . GLN A 233 ? 1.0213 0.8964 0.9456 0.0106 0.0953 -0.0171 233 GLN A CA 1844 C C . GLN A 233 ? 1.0233 0.8951 0.9344 0.0153 0.0925 -0.0150 233 GLN A C 1845 O O . GLN A 233 ? 0.9566 0.8342 0.8594 0.0193 0.0812 -0.0134 233 GLN A O 1846 C CB . GLN A 233 ? 1.0776 0.9373 0.9930 0.0191 0.1069 -0.0128 233 GLN A CB 1847 C CG . GLN A 233 ? 1.0803 0.9436 1.0056 0.0170 0.1074 -0.0137 233 GLN A CG 1848 C CD . GLN A 233 ? 1.0676 0.9142 0.9842 0.0252 0.1207 -0.0094 233 GLN A CD 1849 O OE1 . GLN A 233 ? 1.0890 0.9363 1.0085 0.0265 0.1206 -0.0087 233 GLN A OE1 1850 N NE2 . GLN A 233 ? 1.0479 0.8784 0.9529 0.0313 0.1329 -0.0062 233 GLN A NE2 1851 N N . GLU A 234 ? 1.0141 0.8766 0.9240 0.0147 0.1032 -0.0151 234 GLU A N 1852 C CA . GLU A 234 ? 1.0247 0.8846 0.9238 0.0187 0.1013 -0.0134 234 GLU A CA 1853 C C . GLU A 234 ? 0.9927 0.8687 0.8987 0.0116 0.0876 -0.0169 234 GLU A C 1854 O O . GLU A 234 ? 0.9348 0.8149 0.8320 0.0163 0.0786 -0.0150 234 GLU A O 1855 C CB . GLU A 234 ? 1.1042 0.9510 1.0026 0.0182 0.1163 -0.0133 234 GLU A CB 1856 C CG . GLU A 234 ? 1.2062 1.0516 1.0972 0.0199 0.1152 -0.0126 234 GLU A CG 1857 C CD . GLU A 234 ? 1.3563 1.1969 1.2284 0.0327 0.1113 -0.0071 234 GLU A CD 1858 O OE1 . GLU A 234 ? 1.4295 1.2753 1.2964 0.0377 0.1022 -0.0054 234 GLU A OE1 1859 O OE2 . GLU A 234 ? 1.4483 1.2803 1.3111 0.0379 0.1172 -0.0048 234 GLU A OE2 1860 N N . VAL A 235 ? 0.9720 0.8571 0.8937 0.0007 0.0860 -0.0223 235 VAL A N 1861 C CA . VAL A 235 ? 0.9351 0.8349 0.8629 -0.0057 0.0733 -0.0256 235 VAL A CA 1862 C C . VAL A 235 ? 0.9199 0.8284 0.8439 -0.0026 0.0606 -0.0238 235 VAL A C 1863 O O . VAL A 235 ? 0.9075 0.8215 0.8264 -0.0012 0.0519 -0.0231 235 VAL A O 1864 C CB . VAL A 235 ? 0.9215 0.8307 0.8663 -0.0168 0.0722 -0.0319 235 VAL A CB 1865 C CG1 . VAL A 235 ? 0.8499 0.7733 0.7982 -0.0218 0.0586 -0.0345 235 VAL A CG1 1866 C CG2 . VAL A 235 ? 0.9358 0.8381 0.8862 -0.0217 0.0836 -0.0353 235 VAL A CG2 1867 N N . ALA A 236 ? 0.9125 0.8221 0.8398 -0.0015 0.0600 -0.0233 236 ALA A N 1868 C CA . ALA A 236 ? 0.9189 0.8350 0.8421 0.0019 0.0492 -0.0215 236 ALA A CA 1869 C C . ALA A 236 ? 0.9236 0.8349 0.8314 0.0110 0.0461 -0.0178 236 ALA A C 1870 O O . ALA A 236 ? 0.9216 0.8409 0.8274 0.0115 0.0355 -0.0179 236 ALA A O 1871 C CB . ALA A 236 ? 0.9143 0.8285 0.8406 0.0036 0.0517 -0.0207 236 ALA A CB 1872 N N . ARG A 237 ? 0.9380 0.8365 0.8355 0.0185 0.0555 -0.0147 237 ARG A N 1873 C CA . ARG A 237 ? 0.9487 0.8430 0.8315 0.0283 0.0526 -0.0115 237 ARG A CA 1874 C C . ARG A 237 ? 0.9167 0.8169 0.7991 0.0265 0.0473 -0.0126 237 ARG A C 1875 O O . ARG A 237 ? 0.9795 0.8847 0.8561 0.0309 0.0387 -0.0121 237 ARG A O 1876 C CB . ARG A 237 ? 1.0208 0.8989 0.8913 0.0377 0.0647 -0.0076 237 ARG A CB 1877 C CG . ARG A 237 ? 1.0955 0.9695 0.9495 0.0496 0.0612 -0.0045 237 ARG A CG 1878 C CD . ARG A 237 ? 1.1850 1.0422 1.0258 0.0591 0.0742 -0.0004 237 ARG A CD 1879 N NE . ARG A 237 ? 1.2324 1.0857 1.0763 0.0554 0.0819 -0.0008 237 ARG A NE 1880 C CZ . ARG A 237 ? 1.2064 1.0636 1.0475 0.0568 0.0778 -0.0010 237 ARG A CZ 1881 N NH1 . ARG A 237 ? 1.1701 1.0363 1.0063 0.0614 0.0658 -0.0011 237 ARG A NH1 1882 N NH2 . ARG A 237 ? 1.1906 1.0426 1.0344 0.0532 0.0863 -0.0013 237 ARG A NH2 1883 N N . ILE A 238 ? 0.8717 0.7712 0.7606 0.0201 0.0528 -0.0145 238 ILE A N 1884 C CA . ILE A 238 ? 0.8484 0.7520 0.7364 0.0186 0.0493 -0.0154 238 ILE A CA 1885 C C . ILE A 238 ? 0.8240 0.7419 0.7193 0.0125 0.0368 -0.0180 238 ILE A C 1886 O O . ILE A 238 ? 0.8552 0.7782 0.7468 0.0153 0.0297 -0.0176 238 ILE A O 1887 C CB . ILE A 238 ? 0.8360 0.7347 0.7290 0.0128 0.0586 -0.0172 238 ILE A CB 1888 C CG1 . ILE A 238 ? 0.8569 0.7397 0.7416 0.0196 0.0725 -0.0141 238 ILE A CG1 1889 C CG2 . ILE A 238 ? 0.8410 0.7444 0.7331 0.0112 0.0545 -0.0181 238 ILE A CG2 1890 C CD1 . ILE A 238 ? 0.8702 0.7466 0.7610 0.0133 0.0834 -0.0165 238 ILE A CD1 1891 N N . VAL A 239 ? 0.7956 0.7196 0.7013 0.0047 0.0345 -0.0208 239 VAL A N 1892 C CA . VAL A 239 ? 0.8310 0.7670 0.7432 -0.0012 0.0240 -0.0231 239 VAL A CA 1893 C C . VAL A 239 ? 0.8470 0.7877 0.7555 0.0031 0.0152 -0.0218 239 VAL A C 1894 O O . VAL A 239 ? 0.8450 0.7919 0.7530 0.0027 0.0080 -0.0222 239 VAL A O 1895 C CB . VAL A 239 ? 0.8507 0.7920 0.7743 -0.0094 0.0238 -0.0264 239 VAL A CB 1896 C CG1 . VAL A 239 ? 0.8637 0.8162 0.7919 -0.0138 0.0130 -0.0280 239 VAL A CG1 1897 C CG2 . VAL A 239 ? 0.8565 0.7952 0.7852 -0.0151 0.0309 -0.0293 239 VAL A CG2 1898 N N . GLY A 240 ? 0.8555 0.7928 0.7618 0.0070 0.0163 -0.0203 240 GLY A N 1899 C CA . GLY A 240 ? 0.8778 0.8198 0.7824 0.0096 0.0080 -0.0199 240 GLY A CA 1900 C C . GLY A 240 ? 0.8758 0.8133 0.7692 0.0192 0.0066 -0.0179 240 GLY A C 1901 O O . GLY A 240 ? 0.8516 0.7941 0.7438 0.0210 -0.0012 -0.0185 240 GLY A O 1902 N N . ASN A 241 ? 0.8944 0.8223 0.7794 0.0258 0.0143 -0.0157 241 ASN A N 1903 C CA . ASN A 241 ? 0.9482 0.8705 0.8211 0.0364 0.0136 -0.0137 241 ASN A CA 1904 C C . ASN A 241 ? 0.9322 0.8490 0.7952 0.0442 0.0169 -0.0121 241 ASN A C 1905 O O . ASN A 241 ? 1.0793 0.9868 0.9306 0.0538 0.0215 -0.0095 241 ASN A O 1906 C CB . ASN A 241 ? 0.9895 0.9025 0.8584 0.0401 0.0205 -0.0117 241 ASN A CB 1907 C CG . ASN A 241 ? 1.0693 0.9806 0.9284 0.0484 0.0154 -0.0109 241 ASN A CG 1908 O OD1 . ASN A 241 ? 1.0223 0.9243 0.8681 0.0586 0.0193 -0.0086 241 ASN A OD1 1909 N ND2 . ASN A 241 ? 1.0820 1.0016 0.9466 0.0446 0.0067 -0.0131 241 ASN A ND2 1910 N N . SER A 242 ? 0.8919 0.8142 0.7589 0.0408 0.0148 -0.0133 242 SER A N 1911 C CA . SER A 242 ? 0.9119 0.8291 0.7704 0.0481 0.0187 -0.0116 242 SER A CA 1912 C C . SER A 242 ? 0.9249 0.8518 0.7866 0.0473 0.0112 -0.0135 242 SER A C 1913 O O . SER A 242 ? 0.9388 0.8625 0.7958 0.0519 0.0151 -0.0122 242 SER A O 1914 C CB . SER A 242 ? 0.9433 0.8513 0.8026 0.0453 0.0307 -0.0101 242 SER A CB 1915 O OG . SER A 242 ? 0.9711 0.8857 0.8403 0.0361 0.0295 -0.0125 242 SER A OG 1916 N N . GLY A 243 ? 0.8934 0.8316 0.7634 0.0418 0.0016 -0.0164 243 GLY A N 1917 C CA . GLY A 243 ? 0.8982 0.8458 0.7724 0.0411 -0.0052 -0.0186 243 GLY A CA 1918 C C . GLY A 243 ? 0.9303 0.8850 0.8156 0.0305 -0.0072 -0.0205 243 GLY A C 1919 O O . GLY A 243 ? 0.9684 0.9316 0.8587 0.0289 -0.0132 -0.0226 243 GLY A O 1920 N N . LEU A 244 ? 0.9170 0.8685 0.8064 0.0232 -0.0020 -0.0202 244 LEU A N 1921 C CA . LEU A 244 ? 0.8547 0.8121 0.7528 0.0138 -0.0039 -0.0221 244 LEU A CA 1922 C C . LEU A 244 ? 0.8593 0.8242 0.7635 0.0091 -0.0117 -0.0238 244 LEU A C 1923 O O . LEU A 244 ? 0.8544 0.8188 0.7570 0.0115 -0.0141 -0.0236 244 LEU A O 1924 C CB . LEU A 244 ? 0.8350 0.7874 0.7357 0.0079 0.0032 -0.0221 244 LEU A CB 1925 C CG . LEU A 244 ? 0.7814 0.7250 0.6772 0.0107 0.0125 -0.0207 244 LEU A CG 1926 C CD1 . LEU A 244 ? 0.7786 0.7180 0.6788 0.0040 0.0192 -0.0219 244 LEU A CD1 1927 C CD2 . LEU A 244 ? 0.7642 0.7105 0.6601 0.0105 0.0120 -0.0210 244 LEU A CD2 1928 N N . ASN A 245 ? 0.8575 0.8283 0.7677 0.0028 -0.0149 -0.0253 245 ASN A N 1929 C CA . ASN A 245 ? 0.8353 0.8118 0.7507 -0.0016 -0.0210 -0.0266 245 ASN A CA 1930 C C . ASN A 245 ? 0.8507 0.8265 0.7693 -0.0079 -0.0193 -0.0267 245 ASN A C 1931 O O . ASN A 245 ? 0.8362 0.8132 0.7574 -0.0132 -0.0181 -0.0276 245 ASN A O 1932 C CB . ASN A 245 ? 0.8072 0.7897 0.7270 -0.0043 -0.0250 -0.0280 245 ASN A CB 1933 C CG . ASN A 245 ? 0.7850 0.7721 0.7091 -0.0077 -0.0307 -0.0291 245 ASN A CG 1934 O OD1 . ASN A 245 ? 0.7282 0.7143 0.6526 -0.0096 -0.0315 -0.0286 245 ASN A OD1 1935 N ND2 . ASN A 245 ? 0.7919 0.7838 0.7200 -0.0081 -0.0342 -0.0306 245 ASN A ND2 1936 N N . ILE A 246 ? 0.8305 0.8046 0.7488 -0.0069 -0.0194 -0.0262 246 ILE A N 1937 C CA . ILE A 246 ? 0.8002 0.7745 0.7226 -0.0119 -0.0178 -0.0267 246 ILE A CA 1938 C C . ILE A 246 ? 0.8168 0.7970 0.7435 -0.0178 -0.0228 -0.0279 246 ILE A C 1939 O O . ILE A 246 ? 0.8153 0.7970 0.7453 -0.0224 -0.0217 -0.0291 246 ILE A O 1940 C CB . ILE A 246 ? 0.7779 0.7496 0.6996 -0.0089 -0.0171 -0.0258 246 ILE A CB 1941 C CG1 . ILE A 246 ? 0.8024 0.7741 0.7295 -0.0133 -0.0137 -0.0268 246 ILE A CG1 1942 C CG2 . ILE A 246 ? 0.7708 0.7462 0.6930 -0.0079 -0.0237 -0.0257 246 ILE A CG2 1943 C CD1 . ILE A 246 ? 0.8293 0.7970 0.7562 -0.0100 -0.0104 -0.0257 246 ILE A CD1 1944 N N . TYR A 247 ? 0.8254 0.8089 0.7522 -0.0173 -0.0278 -0.0278 247 TYR A N 1945 C CA . TYR A 247 ? 0.8666 0.8541 0.7961 -0.0218 -0.0316 -0.0283 247 TYR A CA 1946 C C . TYR A 247 ? 0.8585 0.8464 0.7878 -0.0250 -0.0298 -0.0291 247 TYR A C 1947 O O . TYR A 247 ? 0.8720 0.8617 0.8019 -0.0290 -0.0312 -0.0295 247 TYR A O 1948 C CB . TYR A 247 ? 0.9316 0.9211 0.8617 -0.0202 -0.0361 -0.0282 247 TYR A CB 1949 C CG . TYR A 247 ? 1.0195 1.0091 0.9502 -0.0191 -0.0390 -0.0277 247 TYR A CG 1950 C CD1 . TYR A 247 ? 0.9989 0.9864 0.9289 -0.0169 -0.0372 -0.0270 247 TYR A CD1 1951 C CD2 . TYR A 247 ? 1.0804 1.0717 1.0127 -0.0201 -0.0427 -0.0278 247 TYR A CD2 1952 C CE1 . TYR A 247 ? 1.0297 1.0170 0.9601 -0.0156 -0.0395 -0.0264 247 TYR A CE1 1953 C CE2 . TYR A 247 ? 1.1725 1.1633 1.1050 -0.0189 -0.0449 -0.0273 247 TYR A CE2 1954 C CZ . TYR A 247 ? 1.1501 1.1391 1.0815 -0.0166 -0.0436 -0.0265 247 TYR A CZ 1955 O OH . TYR A 247 ? 1.1757 1.1640 1.1073 -0.0153 -0.0455 -0.0258 247 TYR A OH 1956 N N . ASN A 248 ? 0.8209 0.8069 0.7485 -0.0227 -0.0267 -0.0290 248 ASN A N 1957 C CA . ASN A 248 ? 0.7833 0.7691 0.7105 -0.0252 -0.0245 -0.0296 248 ASN A CA 1958 C C . ASN A 248 ? 0.7809 0.7631 0.7056 -0.0217 -0.0197 -0.0293 248 ASN A C 1959 O O . ASN A 248 ? 0.7897 0.7728 0.7140 -0.0173 -0.0204 -0.0289 248 ASN A O 1960 C CB . ASN A 248 ? 0.7646 0.7535 0.6937 -0.0262 -0.0277 -0.0297 248 ASN A CB 1961 C CG . ASN A 248 ? 0.7582 0.7465 0.6869 -0.0280 -0.0247 -0.0300 248 ASN A CG 1962 O OD1 . ASN A 248 ? 0.7554 0.7407 0.6819 -0.0283 -0.0204 -0.0302 248 ASN A OD1 1963 N ND2 . ASN A 248 ? 0.7788 0.7692 0.7099 -0.0294 -0.0262 -0.0301 248 ASN A ND2 1964 N N . LEU A 249 ? 0.7341 0.7125 0.6575 -0.0235 -0.0146 -0.0298 249 LEU A N 1965 C CA . LEU A 249 ? 0.7156 0.6887 0.6358 -0.0199 -0.0085 -0.0291 249 LEU A CA 1966 C C . LEU A 249 ? 0.7034 0.6763 0.6221 -0.0174 -0.0071 -0.0286 249 LEU A C 1967 O O . LEU A 249 ? 0.7577 0.7270 0.6730 -0.0119 -0.0034 -0.0274 249 LEU A O 1968 C CB . LEU A 249 ? 0.7117 0.6808 0.6323 -0.0241 -0.0029 -0.0307 249 LEU A CB 1969 C CG . LEU A 249 ? 0.6998 0.6615 0.6170 -0.0216 0.0052 -0.0302 249 LEU A CG 1970 C CD1 . LEU A 249 ? 0.7203 0.6773 0.6342 -0.0148 0.0082 -0.0280 249 LEU A CD1 1971 C CD2 . LEU A 249 ? 0.7311 0.6900 0.6505 -0.0275 0.0100 -0.0330 249 LEU A CD2 1972 N N . TYR A 250 ? 0.6983 0.6749 0.6192 -0.0209 -0.0094 -0.0293 250 TYR A N 1973 C CA . TYR A 250 ? 0.7299 0.7068 0.6506 -0.0190 -0.0076 -0.0290 250 TYR A CA 1974 C C . TYR A 250 ? 0.7064 0.6893 0.6308 -0.0158 -0.0126 -0.0290 250 TYR A C 1975 O O . TYR A 250 ? 0.6951 0.6801 0.6215 -0.0143 -0.0117 -0.0292 250 TYR A O 1976 C CB . TYR A 250 ? 0.7444 0.7202 0.6650 -0.0246 -0.0052 -0.0299 250 TYR A CB 1977 C CG . TYR A 250 ? 0.7295 0.6997 0.6471 -0.0273 -0.0002 -0.0309 250 TYR A CG 1978 C CD1 . TYR A 250 ? 0.7646 0.7291 0.6793 -0.0241 0.0062 -0.0303 250 TYR A CD1 1979 C CD2 . TYR A 250 ? 0.7453 0.7161 0.6634 -0.0327 -0.0017 -0.0328 250 TYR A CD2 1980 C CE1 . TYR A 250 ? 0.8260 0.7848 0.7391 -0.0271 0.0118 -0.0318 250 TYR A CE1 1981 C CE2 . TYR A 250 ? 0.7813 0.7480 0.6985 -0.0356 0.0026 -0.0348 250 TYR A CE2 1982 C CZ . TYR A 250 ? 0.7947 0.7552 0.7099 -0.0332 0.0098 -0.0345 250 TYR A CZ 1983 O OH . TYR A 250 ? 0.8639 0.8199 0.7793 -0.0367 0.0150 -0.0371 250 TYR A OH 1984 N N . ALA A 251 ? 0.6825 0.6683 0.6086 -0.0149 -0.0175 -0.0293 251 ALA A N 1985 C CA . ALA A 251 ? 0.7172 0.7087 0.6474 -0.0122 -0.0226 -0.0303 251 ALA A CA 1986 C C . ALA A 251 ? 0.7802 0.7718 0.7076 -0.0045 -0.0239 -0.0302 251 ALA A C 1987 O O . ALA A 251 ? 0.8057 0.7924 0.7279 -0.0021 -0.0219 -0.0289 251 ALA A O 1988 C CB . ALA A 251 ? 0.6949 0.6889 0.6282 -0.0160 -0.0270 -0.0310 251 ALA A CB 1989 N N . PRO A 252 ? 0.8334 0.8306 0.7643 -0.0003 -0.0274 -0.0318 252 PRO A N 1990 C CA . PRO A 252 ? 0.8442 0.8422 0.7714 0.0079 -0.0299 -0.0322 252 PRO A CA 1991 C C . PRO A 252 ? 0.8622 0.8598 0.7882 0.0079 -0.0340 -0.0328 252 PRO A C 1992 O O . PRO A 252 ? 0.8114 0.8112 0.7422 0.0021 -0.0365 -0.0338 252 PRO A O 1993 C CB . PRO A 252 ? 0.8541 0.8605 0.7880 0.0107 -0.0340 -0.0352 252 PRO A CB 1994 C CG . PRO A 252 ? 0.8265 0.8368 0.7692 0.0027 -0.0351 -0.0367 252 PRO A CG 1995 C CD . PRO A 252 ? 0.8162 0.8200 0.7555 -0.0031 -0.0297 -0.0340 252 PRO A CD 1996 N N . CYS A 253 ? 0.9372 0.9313 0.8560 0.0150 -0.0341 -0.0320 253 CYS A N 1997 C CA . CYS A 253 ? 0.9734 0.9665 0.8901 0.0160 -0.0374 -0.0325 253 CYS A CA 1998 C C . CYS A 253 ? 0.9614 0.9616 0.8816 0.0194 -0.0446 -0.0363 253 CYS A C 1999 O O . CYS A 253 ? 0.9505 0.9531 0.8680 0.0268 -0.0465 -0.0375 253 CYS A O 2000 C CB . CYS A 253 ? 1.0204 1.0051 0.9269 0.0224 -0.0333 -0.0298 253 CYS A CB 2001 S SG . CYS A 253 ? 1.0755 1.0575 0.9781 0.0246 -0.0363 -0.0300 253 CYS A SG 2002 N N . ALA A 254 ? 0.9719 0.9755 0.8983 0.0142 -0.0485 -0.0384 254 ALA A N 2003 C CA . ALA A 254 ? 1.0245 1.0349 0.9558 0.0162 -0.0552 -0.0429 254 ALA A CA 2004 C C . ALA A 254 ? 1.0980 1.1076 1.0211 0.0260 -0.0585 -0.0442 254 ALA A C 2005 O O . ALA A 254 ? 1.0406 1.0438 0.9559 0.0286 -0.0576 -0.0424 254 ALA A O 2006 C CB . ALA A 254 ? 1.0191 1.0299 0.9555 0.0098 -0.0573 -0.0441 254 ALA A CB 2007 N N . GLY A 255 ? 1.1470 1.1632 1.0719 0.0318 -0.0623 -0.0475 255 GLY A N 2008 C CA . GLY A 255 ? 1.2115 1.2283 1.1285 0.0418 -0.0669 -0.0498 255 GLY A CA 2009 C C . GLY A 255 ? 1.2403 1.2489 1.1434 0.0508 -0.0624 -0.0454 255 GLY A C 2010 O O . GLY A 255 ? 1.2883 1.2906 1.1806 0.0571 -0.0626 -0.0444 255 GLY A O 2011 N N . GLY A 256 ? 1.1846 1.1924 1.0875 0.0517 -0.0575 -0.0428 256 GLY A N 2012 C CA . GLY A 256 ? 1.1892 1.1893 1.0792 0.0612 -0.0526 -0.0389 256 GLY A CA 2013 C C . GLY A 256 ? 1.1981 1.1853 1.0784 0.0612 -0.0449 -0.0338 256 GLY A C 2014 O O . GLY A 256 ? 1.2400 1.2247 1.1234 0.0539 -0.0440 -0.0332 256 GLY A O 2015 N N . VAL A 257 ? 1.2086 1.1872 1.0773 0.0695 -0.0389 -0.0301 257 VAL A N 2016 C CA . VAL A 257 ? 1.2864 1.2521 1.1468 0.0695 -0.0299 -0.0253 257 VAL A CA 2017 C C . VAL A 257 ? 1.4407 1.3988 1.2872 0.0800 -0.0300 -0.0242 257 VAL A C 2018 O O . VAL A 257 ? 1.3898 1.3457 1.2256 0.0916 -0.0304 -0.0236 257 VAL A O 2019 C CB . VAL A 257 ? 1.2013 1.1599 1.0590 0.0697 -0.0203 -0.0215 257 VAL A CB 2020 C CG1 . VAL A 257 ? 1.1118 1.0763 0.9823 0.0583 -0.0199 -0.0227 257 VAL A CG1 2021 C CG2 . VAL A 257 ? 1.2405 1.1984 1.0897 0.0814 -0.0199 -0.0206 257 VAL A CG2 2022 N N . PRO A 258 ? 1.6569 1.6112 1.5031 0.0764 -0.0296 -0.0239 258 PRO A N 2023 C CA . PRO A 258 ? 1.7827 1.7306 1.6165 0.0854 -0.0306 -0.0235 258 PRO A CA 2024 C C . PRO A 258 ? 1.7965 1.7330 1.6134 0.0985 -0.0242 -0.0197 258 PRO A C 2025 O O . PRO A 258 ? 1.8321 1.7609 1.6465 0.0986 -0.0148 -0.0158 258 PRO A O 2026 C CB . PRO A 258 ? 1.7801 1.7222 1.6169 0.0781 -0.0261 -0.0217 258 PRO A CB 2027 C CG . PRO A 258 ? 1.7294 1.6806 1.5820 0.0653 -0.0290 -0.0238 258 PRO A CG 2028 C CD . PRO A 258 ? 1.6928 1.6488 1.5501 0.0639 -0.0285 -0.0241 258 PRO A CD 2029 N N . ARG A 268 ? 1.3649 1.3233 1.2381 0.0421 -0.0725 -0.0506 298 ARG A N 2030 C CA . ARG A 268 ? 1.3036 1.2664 1.1892 0.0326 -0.0710 -0.0490 298 ARG A CA 2031 C C . ARG A 268 ? 1.2389 1.2027 1.1268 0.0307 -0.0661 -0.0438 298 ARG A C 2032 O O . ARG A 268 ? 1.2759 1.2410 1.1602 0.0346 -0.0658 -0.0437 298 ARG A O 2033 C CB . ARG A 268 ? 1.2874 1.2583 1.1827 0.0281 -0.0762 -0.0548 298 ARG A CB 2034 C CG . ARG A 268 ? 1.2496 1.2232 1.1561 0.0190 -0.0742 -0.0532 298 ARG A CG 2035 C CD . ARG A 268 ? 1.2223 1.2020 1.1385 0.0143 -0.0781 -0.0593 298 ARG A CD 2036 N NE . ARG A 268 ? 1.2196 1.2064 1.1426 0.0119 -0.0785 -0.0599 298 ARG A NE 2037 C CZ . ARG A 268 ? 1.3017 1.2946 1.2252 0.0156 -0.0824 -0.0641 298 ARG A CZ 2038 N NH1 . ARG A 268 ? 1.4099 1.4030 1.3267 0.0226 -0.0869 -0.0684 298 ARG A NH1 2039 N NH2 . ARG A 268 ? 1.2969 1.2958 1.2273 0.0129 -0.0818 -0.0640 298 ARG A NH2 2040 N N . MET A 269 ? 1.2991 1.2623 1.1927 0.0249 -0.0624 -0.0400 299 MET A N 2041 C CA . MET A 269 ? 1.2549 1.2198 1.1520 0.0220 -0.0581 -0.0360 299 MET A CA 2042 C C . MET A 269 ? 1.1832 1.1547 1.0896 0.0151 -0.0599 -0.0372 299 MET A C 2043 O O . MET A 269 ? 1.0818 1.0544 0.9939 0.0099 -0.0602 -0.0368 299 MET A O 2044 C CB . MET A 269 ? 1.2694 1.2304 1.1673 0.0203 -0.0531 -0.0316 299 MET A CB 2045 C CG . MET A 269 ? 1.2861 1.2500 1.1896 0.0158 -0.0495 -0.0287 299 MET A CG 2046 S SD . MET A 269 ? 1.2678 1.2300 1.1752 0.0136 -0.0447 -0.0248 299 MET A SD 2047 C CE . MET A 269 ? 1.2829 1.2393 1.1845 0.0188 -0.0381 -0.0228 299 MET A CE 2048 N N . ASP A 270 ? 1.1687 1.1442 1.0760 0.0157 -0.0606 -0.0383 300 ASP A N 2049 C CA . ASP A 270 ? 1.1207 1.1014 1.0359 0.0096 -0.0603 -0.0382 300 ASP A CA 2050 C C . ASP A 270 ? 1.0733 1.0523 0.9880 0.0081 -0.0553 -0.0339 300 ASP A C 2051 O O . ASP A 270 ? 1.0458 1.0203 0.9547 0.0123 -0.0520 -0.0318 300 ASP A O 2052 C CB . ASP A 270 ? 1.1168 1.1027 1.0339 0.0110 -0.0631 -0.0416 300 ASP A CB 2053 C CG . ASP A 270 ? 1.1604 1.1497 1.0806 0.0117 -0.0685 -0.0472 300 ASP A CG 2054 O OD1 . ASP A 270 ? 1.2170 1.2029 1.1327 0.0150 -0.0704 -0.0488 300 ASP A OD1 2055 O OD2 . ASP A 270 ? 1.2143 1.2097 1.1420 0.0090 -0.0707 -0.0506 300 ASP A OD2 2056 N N . PRO A 271 ? 1.0421 1.0242 0.9627 0.0021 -0.0542 -0.0328 301 PRO A N 2057 C CA . PRO A 271 ? 1.0226 1.0044 0.9432 0.0006 -0.0501 -0.0302 301 PRO A CA 2058 C C . PRO A 271 ? 1.0190 1.0010 0.9364 0.0044 -0.0489 -0.0309 301 PRO A C 2059 O O . PRO A 271 ? 1.0579 1.0428 0.9758 0.0061 -0.0522 -0.0337 301 PRO A O 2060 C CB . PRO A 271 ? 1.0423 1.0278 0.9688 -0.0057 -0.0505 -0.0299 301 PRO A CB 2061 C CG . PRO A 271 ? 1.0082 0.9942 0.9373 -0.0075 -0.0536 -0.0313 301 PRO A CG 2062 C CD . PRO A 271 ? 1.0092 0.9946 0.9361 -0.0031 -0.0564 -0.0341 301 PRO A CD 2063 N N . PRO A 272 ? 1.0410 1.0198 0.9556 0.0056 -0.0439 -0.0287 302 PRO A N 2064 C CA . PRO A 272 ? 1.1023 1.0799 1.0125 0.0103 -0.0420 -0.0289 302 PRO A CA 2065 C C . PRO A 272 ? 1.0825 1.0649 0.9972 0.0070 -0.0428 -0.0301 302 PRO A C 2066 O O . PRO A 272 ? 1.0162 1.0011 0.9362 0.0006 -0.0425 -0.0298 302 PRO A O 2067 C CB . PRO A 272 ? 1.0891 1.0606 0.9958 0.0117 -0.0351 -0.0262 302 PRO A CB 2068 C CG . PRO A 272 ? 1.0924 1.0646 1.0045 0.0061 -0.0340 -0.0252 302 PRO A CG 2069 C CD . PRO A 272 ? 1.0854 1.0627 1.0023 0.0020 -0.0397 -0.0266 302 PRO A CD 2070 N N . CYS A 273 ? 1.0556 1.0391 0.9674 0.0119 -0.0437 -0.0313 303 CYS A N 2071 C CA . CYS A 273 ? 1.0566 1.0450 0.9729 0.0100 -0.0444 -0.0327 303 CYS A CA 2072 C C . CYS A 273 ? 1.0304 1.0248 0.9551 0.0041 -0.0485 -0.0350 303 CYS A C 2073 O O . CYS A 273 ? 1.0819 1.0795 1.0113 0.0007 -0.0478 -0.0356 303 CYS A O 2074 C CB . CYS A 273 ? 1.0452 1.0309 0.9612 0.0072 -0.0384 -0.0303 303 CYS A CB 2075 S SG . CYS A 273 ? 1.0990 1.0771 1.0056 0.0148 -0.0322 -0.0279 303 CYS A SG 2076 N N . THR A 274 ? 0.9869 0.9818 0.9131 0.0033 -0.0520 -0.0364 304 THR A N 2077 C CA . THR A 274 ? 0.9808 0.9794 0.9145 -0.0022 -0.0546 -0.0384 304 THR A CA 2078 C C . THR A 274 ? 0.9349 0.9374 0.8718 0.0001 -0.0597 -0.0429 304 THR A C 2079 O O . THR A 274 ? 0.9328 0.9333 0.8652 0.0044 -0.0620 -0.0439 304 THR A O 2080 C CB . THR A 274 ? 1.0198 1.0151 0.9535 -0.0063 -0.0537 -0.0362 304 THR A CB 2081 O OG1 . THR A 274 ? 1.0018 0.9940 0.9321 -0.0071 -0.0497 -0.0329 304 THR A OG1 2082 C CG2 . THR A 274 ? 1.0464 1.0435 0.9862 -0.0123 -0.0540 -0.0367 304 THR A CG2 2083 N N . ASN A 275 ? 0.9518 0.9599 0.8968 -0.0025 -0.0612 -0.0461 305 ASN A N 2084 C CA . ASN A 275 ? 0.9517 0.9646 0.9028 -0.0020 -0.0659 -0.0516 305 ASN A CA 2085 C C . ASN A 275 ? 0.9174 0.9281 0.8732 -0.0080 -0.0655 -0.0521 305 ASN A C 2086 O O . ASN A 275 ? 0.8714 0.8813 0.8315 -0.0136 -0.0623 -0.0504 305 ASN A O 2087 C CB . ASN A 275 ? 0.9470 0.9675 0.9066 -0.0023 -0.0671 -0.0553 305 ASN A CB 2088 C CG . ASN A 275 ? 0.9853 1.0125 0.9524 -0.0010 -0.0726 -0.0623 305 ASN A CG 2089 O OD1 . ASN A 275 ? 1.0683 1.0938 1.0347 -0.0009 -0.0752 -0.0646 305 ASN A OD1 2090 N ND2 . ASN A 275 ? 1.0285 1.0638 1.0036 0.0001 -0.0743 -0.0661 305 ASN A ND2 2091 N N . THR A 276 ? 0.9163 0.9250 0.8702 -0.0063 -0.0683 -0.0541 306 THR A N 2092 C CA . THR A 276 ? 0.9311 0.9364 0.8883 -0.0112 -0.0674 -0.0543 306 THR A CA 2093 C C . THR A 276 ? 0.9663 0.9756 0.9321 -0.0125 -0.0707 -0.0611 306 THR A C 2094 O O . THR A 276 ? 0.9394 0.9450 0.9070 -0.0153 -0.0703 -0.0624 306 THR A O 2095 C CB . THR A 276 ? 0.9072 0.9059 0.8561 -0.0090 -0.0670 -0.0510 306 THR A CB 2096 O OG1 . THR A 276 ? 0.9134 0.9121 0.8585 -0.0038 -0.0710 -0.0546 306 THR A OG1 2097 C CG2 . THR A 276 ? 0.9152 0.9110 0.8571 -0.0072 -0.0640 -0.0455 306 THR A CG2 2098 N N . THR A 277 ? 0.9677 0.9846 0.9392 -0.0106 -0.0737 -0.0660 307 THR A N 2099 C CA . THR A 277 ? 0.9711 0.9934 0.9522 -0.0117 -0.0775 -0.0739 307 THR A CA 2100 C C . THR A 277 ? 0.9454 0.9669 0.9376 -0.0197 -0.0735 -0.0753 307 THR A C 2101 O O . THR A 277 ? 1.0087 1.0277 1.0049 -0.0225 -0.0736 -0.0787 307 THR A O 2102 C CB . THR A 277 ? 1.0088 1.0411 0.9947 -0.0073 -0.0820 -0.0790 307 THR A CB 2103 O OG1 . THR A 277 ? 1.0213 1.0524 0.9948 0.0008 -0.0844 -0.0764 307 THR A OG1 2104 C CG2 . THR A 277 ? 1.0275 1.0668 1.0234 -0.0075 -0.0874 -0.0886 307 THR A CG2 2105 N N . ALA A 278 ? 0.9065 0.9290 0.9030 -0.0232 -0.0692 -0.0725 308 ALA A N 2106 C CA . ALA A 278 ? 0.8941 0.9150 0.9007 -0.0303 -0.0642 -0.0736 308 ALA A CA 2107 C C . ALA A 278 ? 0.8919 0.9035 0.8955 -0.0335 -0.0610 -0.0714 308 ALA A C 2108 O O . ALA A 278 ? 0.8700 0.8808 0.8822 -0.0373 -0.0596 -0.0760 308 ALA A O 2109 C CB . ALA A 278 ? 0.8890 0.9089 0.8955 -0.0326 -0.0591 -0.0686 308 ALA A CB 2110 N N . ALA A 279 ? 0.9447 0.9496 0.9365 -0.0317 -0.0596 -0.0645 309 ALA A N 2111 C CA . ALA A 279 ? 0.9370 0.9330 0.9247 -0.0339 -0.0563 -0.0613 309 ALA A CA 2112 C C . ALA A 279 ? 0.9432 0.9375 0.9304 -0.0322 -0.0595 -0.0653 309 ALA A C 2113 O O . ALA A 279 ? 0.9487 0.9376 0.9393 -0.0355 -0.0566 -0.0667 309 ALA A O 2114 C CB . ALA A 279 ? 0.9459 0.9371 0.9222 -0.0319 -0.0547 -0.0535 309 ALA A CB 2115 N N . SER A 280 ? 0.9604 0.9582 0.9424 -0.0268 -0.0650 -0.0670 310 SER A N 2116 C CA . SER A 280 ? 0.9566 0.9526 0.9363 -0.0243 -0.0685 -0.0711 310 SER A CA 2117 C C . SER A 280 ? 0.9288 0.9288 0.9205 -0.0276 -0.0701 -0.0800 310 SER A C 2118 O O . SER A 280 ? 0.9296 0.9242 0.9234 -0.0301 -0.0686 -0.0825 310 SER A O 2119 C CB . SER A 280 ? 0.9659 0.9647 0.9369 -0.0171 -0.0737 -0.0713 310 SER A CB 2120 O OG . SER A 280 ? 1.0352 1.0298 1.0010 -0.0142 -0.0761 -0.0736 310 SER A OG 2121 N N . THR A 281 ? 0.8916 0.9009 0.8918 -0.0276 -0.0729 -0.0850 311 THR A N 2122 C CA . THR A 281 ? 0.8911 0.9062 0.9057 -0.0314 -0.0743 -0.0944 311 THR A CA 2123 C C . THR A 281 ? 0.9276 0.9355 0.9496 -0.0387 -0.0669 -0.0940 311 THR A C 2124 O O . THR A 281 ? 0.9669 0.9732 0.9958 -0.0417 -0.0668 -0.1004 311 THR A O 2125 C CB . THR A 281 ? 0.9015 0.9278 0.9262 -0.0314 -0.0762 -0.0981 311 THR A CB 2126 O OG1 . THR A 281 ? 0.9365 0.9688 0.9536 -0.0235 -0.0830 -0.0989 311 THR A OG1 2127 C CG2 . THR A 281 ? 0.9006 0.9340 0.9433 -0.0361 -0.0771 -0.1086 311 THR A CG2 2128 N N . TYR A 282 ? 0.9601 0.9628 0.9797 -0.0413 -0.0605 -0.0866 312 TYR A N 2129 C CA . TYR A 282 ? 0.9799 0.9746 1.0051 -0.0475 -0.0525 -0.0855 312 TYR A CA 2130 C C . TYR A 282 ? 0.9991 0.9833 1.0169 -0.0473 -0.0505 -0.0832 312 TYR A C 2131 O O . TYR A 282 ? 1.0118 0.9922 1.0372 -0.0512 -0.0476 -0.0884 312 TYR A O 2132 C CB . TYR A 282 ? 0.9863 0.9771 1.0081 -0.0491 -0.0465 -0.0778 312 TYR A CB 2133 C CG . TYR A 282 ? 0.9750 0.9559 1.0003 -0.0542 -0.0376 -0.0759 312 TYR A CG 2134 C CD1 . TYR A 282 ? 0.9785 0.9609 1.0186 -0.0598 -0.0327 -0.0814 312 TYR A CD1 2135 C CD2 . TYR A 282 ? 0.9870 0.9569 1.0009 -0.0532 -0.0337 -0.0688 312 TYR A CD2 2136 C CE1 . TYR A 282 ? 0.9990 0.9705 1.0414 -0.0641 -0.0232 -0.0795 312 TYR A CE1 2137 C CE2 . TYR A 282 ? 0.9946 0.9541 1.0099 -0.0568 -0.0250 -0.0666 312 TYR A CE2 2138 C CZ . TYR A 282 ? 0.9915 0.9511 1.0206 -0.0623 -0.0193 -0.0718 312 TYR A CZ 2139 O OH . TYR A 282 ? 1.0078 0.9553 1.0374 -0.0655 -0.0094 -0.0692 312 TYR A OH 2140 N N . LEU A 283 ? 0.9895 0.9692 0.9934 -0.0429 -0.0515 -0.0758 313 LEU A N 2141 C CA . LEU A 283 ? 0.9522 0.9216 0.9483 -0.0421 -0.0488 -0.0723 313 LEU A CA 2142 C C . LEU A 283 ? 0.9644 0.9329 0.9607 -0.0406 -0.0528 -0.0785 313 LEU A C 2143 O O . LEU A 283 ? 0.9568 0.9163 0.9498 -0.0412 -0.0494 -0.0773 313 LEU A O 2144 C CB . LEU A 283 ? 0.9290 0.8954 0.9118 -0.0377 -0.0493 -0.0634 313 LEU A CB 2145 C CG . LEU A 283 ? 0.9099 0.8741 0.8898 -0.0390 -0.0447 -0.0565 313 LEU A CG 2146 C CD1 . LEU A 283 ? 0.8713 0.8364 0.8404 -0.0345 -0.0471 -0.0500 313 LEU A CD1 2147 C CD2 . LEU A 283 ? 0.9155 0.8695 0.8953 -0.0419 -0.0373 -0.0536 313 LEU A CD2 2148 N N . ASN A 284 ? 0.9717 0.9491 0.9707 -0.0381 -0.0598 -0.0851 314 ASN A N 2149 C CA . ASN A 284 ? 0.9553 0.9325 0.9543 -0.0364 -0.0642 -0.0922 314 ASN A CA 2150 C C . ASN A 284 ? 0.9621 0.9411 0.9758 -0.0422 -0.0631 -0.1022 314 ASN A C 2151 O O . ASN A 284 ? 0.9851 0.9622 0.9996 -0.0420 -0.0654 -0.1086 314 ASN A O 2152 C CB . ASN A 284 ? 0.9595 0.9446 0.9526 -0.0297 -0.0725 -0.0948 314 ASN A CB 2153 C CG . ASN A 284 ? 0.9454 0.9261 0.9235 -0.0239 -0.0728 -0.0862 314 ASN A CG 2154 O OD1 . ASN A 284 ? 0.9300 0.9025 0.9004 -0.0222 -0.0712 -0.0832 314 ASN A OD1 2155 N ND2 . ASN A 284 ? 0.9298 0.9158 0.9044 -0.0208 -0.0744 -0.0823 314 ASN A ND2 2156 N N . ASN A 285 ? 1.0164 0.9991 1.0423 -0.0474 -0.0591 -0.1039 315 ASN A N 2157 C CA . ASN A 285 ? 1.0224 1.0053 1.0644 -0.0542 -0.0555 -0.1126 315 ASN A CA 2158 C C . ASN A 285 ? 1.0265 0.9959 1.0654 -0.0568 -0.0492 -0.1115 315 ASN A C 2159 O O . ASN A 285 ? 1.0194 0.9784 1.0513 -0.0574 -0.0420 -0.1026 315 ASN A O 2160 C CB . ASN A 285 ? 1.0358 1.0206 1.0888 -0.0595 -0.0491 -0.1113 315 ASN A CB 2161 C CG . ASN A 285 ? 1.0607 1.0449 1.1317 -0.0671 -0.0436 -0.1202 315 ASN A CG 2162 O OD1 . ASN A 285 ? 1.0611 1.0422 1.1362 -0.0691 -0.0439 -0.1271 315 ASN A OD1 2163 N ND2 . ASN A 285 ? 1.0639 1.0506 1.1463 -0.0717 -0.0379 -0.1203 315 ASN A ND2 2164 N N . PRO A 286 ? 1.0691 1.0382 1.1128 -0.0580 -0.0519 -0.1206 316 PRO A N 2165 C CA . PRO A 286 ? 1.0902 1.0455 1.1303 -0.0601 -0.0457 -0.1198 316 PRO A CA 2166 C C . PRO A 286 ? 1.0847 1.0294 1.1307 -0.0661 -0.0336 -0.1159 316 PRO A C 2167 O O . PRO A 286 ? 1.0366 0.9680 1.0734 -0.0655 -0.0271 -0.1092 316 PRO A O 2168 C CB . PRO A 286 ? 1.0879 1.0473 1.1376 -0.0623 -0.0503 -0.1332 316 PRO A CB 2169 C CG . PRO A 286 ? 1.0885 1.0632 1.1391 -0.0576 -0.0615 -0.1387 316 PRO A CG 2170 C CD . PRO A 286 ? 1.0524 1.0339 1.1048 -0.0572 -0.0609 -0.1327 316 PRO A CD 2171 N N . TYR A 287 ? 1.0793 1.0296 1.1399 -0.0714 -0.0303 -0.1198 317 TYR A N 2172 C CA . TYR A 287 ? 1.0984 1.0381 1.1644 -0.0768 -0.0179 -0.1161 317 TYR A CA 2173 C C . TYR A 287 ? 1.0515 0.9843 1.1029 -0.0730 -0.0137 -0.1023 317 TYR A C 2174 O O . TYR A 287 ? 1.0407 0.9598 1.0870 -0.0740 -0.0041 -0.0960 317 TYR A O 2175 C CB . TYR A 287 ? 1.1055 1.0534 1.1923 -0.0836 -0.0150 -0.1246 317 TYR A CB 2176 C CG . TYR A 287 ? 1.1631 1.1183 1.2662 -0.0878 -0.0189 -0.1394 317 TYR A CG 2177 C CD1 . TYR A 287 ? 1.2237 1.1681 1.3332 -0.0930 -0.0116 -0.1448 317 TYR A CD1 2178 C CD2 . TYR A 287 ? 1.1802 1.1530 1.2919 -0.0863 -0.0301 -0.1483 317 TYR A CD2 2179 C CE1 . TYR A 287 ? 1.2617 1.2133 1.3867 -0.0973 -0.0156 -0.1594 317 TYR A CE1 2180 C CE2 . TYR A 287 ? 1.2120 1.1926 1.3384 -0.0897 -0.0348 -0.1627 317 TYR A CE2 2181 C CZ . TYR A 287 ? 1.2576 1.2280 1.3911 -0.0955 -0.0277 -0.1686 317 TYR A CZ 2182 O OH . TYR A 287 ? 1.3492 1.3279 1.4978 -0.0991 -0.0328 -0.1838 317 TYR A OH 2183 N N . VAL A 288 ? 1.0111 0.9531 1.0553 -0.0682 -0.0209 -0.0979 318 VAL A N 2184 C CA . VAL A 288 ? 0.9688 0.9057 0.9989 -0.0642 -0.0185 -0.0858 318 VAL A CA 2185 C C . VAL A 288 ? 0.9920 0.9191 1.0071 -0.0596 -0.0181 -0.0791 318 VAL A C 2186 O O . VAL A 288 ? 1.0016 0.9184 1.0081 -0.0583 -0.0115 -0.0708 318 VAL A O 2187 C CB . VAL A 288 ? 0.9366 0.8855 0.9630 -0.0604 -0.0262 -0.0835 318 VAL A CB 2188 C CG1 . VAL A 288 ? 0.9109 0.8549 0.9222 -0.0560 -0.0249 -0.0721 318 VAL A CG1 2189 C CG2 . VAL A 288 ? 0.9144 0.8717 0.9545 -0.0645 -0.0250 -0.0882 318 VAL A CG2 2190 N N . ARG A 289 ? 1.0164 0.9465 1.0278 -0.0565 -0.0251 -0.0827 319 ARG A N 2191 C CA . ARG A 289 ? 0.9984 0.9196 0.9971 -0.0521 -0.0247 -0.0772 319 ARG A CA 2192 C C . ARG A 289 ? 1.0145 0.9212 1.0140 -0.0550 -0.0147 -0.0761 319 ARG A C 2193 O O . ARG A 289 ? 0.9862 0.8833 0.9746 -0.0516 -0.0104 -0.0675 319 ARG A O 2194 C CB . ARG A 289 ? 0.9822 0.9080 0.9784 -0.0489 -0.0328 -0.0830 319 ARG A CB 2195 C CG . ARG A 289 ? 0.9514 0.8878 0.9415 -0.0436 -0.0414 -0.0811 319 ARG A CG 2196 C CD . ARG A 289 ? 0.9637 0.9037 0.9506 -0.0399 -0.0489 -0.0872 319 ARG A CD 2197 N NE . ARG A 289 ? 0.9722 0.9024 0.9489 -0.0365 -0.0473 -0.0838 319 ARG A NE 2198 C CZ . ARG A 289 ? 0.9328 0.8631 0.8982 -0.0303 -0.0513 -0.0800 319 ARG A CZ 2199 N NH1 . ARG A 289 ? 0.9410 0.8800 0.9030 -0.0264 -0.0571 -0.0790 319 ARG A NH1 2200 N NH2 . ARG A 289 ? 0.9142 0.8352 0.8719 -0.0277 -0.0489 -0.0770 319 ARG A NH2 2201 N N . LYS A 290 ? 1.0596 0.9649 1.0724 -0.0611 -0.0110 -0.0850 320 LYS A N 2202 C CA . LYS A 290 ? 1.0584 0.9489 1.0737 -0.0648 -0.0001 -0.0852 320 LYS A CA 2203 C C . LYS A 290 ? 1.0079 0.8895 1.0192 -0.0651 0.0094 -0.0762 320 LYS A C 2204 O O . LYS A 290 ? 1.0692 0.9371 1.0712 -0.0627 0.0167 -0.0694 320 LYS A O 2205 C CB . LYS A 290 ? 1.0712 0.9639 1.1046 -0.0722 0.0017 -0.0981 320 LYS A CB 2206 C CG . LYS A 290 ? 1.1043 0.9842 1.1392 -0.0748 0.0082 -0.1021 320 LYS A CG 2207 C CD . LYS A 290 ? 1.1454 1.0310 1.1984 -0.0816 0.0067 -0.1172 320 LYS A CD 2208 C CE . LYS A 290 ? 1.1185 1.0200 1.1730 -0.0789 -0.0075 -0.1252 320 LYS A CE 2209 N NZ . LYS A 290 ? 1.1050 1.0172 1.1794 -0.0852 -0.0107 -0.1400 320 LYS A NZ 2210 N N . ALA A 291 ? 0.9223 0.8115 0.9396 -0.0671 0.0092 -0.0761 321 ALA A N 2211 C CA . ALA A 291 ? 0.9029 0.7844 0.9159 -0.0671 0.0179 -0.0681 321 ALA A CA 2212 C C . ALA A 291 ? 0.9075 0.7847 0.9022 -0.0598 0.0166 -0.0566 321 ALA A C 2213 O O . ALA A 291 ? 0.9457 0.8118 0.9325 -0.0580 0.0248 -0.0491 321 ALA A O 2214 C CB . ALA A 291 ? 0.8965 0.7888 0.9190 -0.0701 0.0163 -0.0707 321 ALA A CB 2215 N N . LEU A 292 ? 0.9309 0.8174 0.9192 -0.0553 0.0063 -0.0556 322 LEU A N 2216 C CA . LEU A 292 ? 0.8967 0.7825 0.8698 -0.0484 0.0031 -0.0461 322 LEU A CA 2217 C C . LEU A 292 ? 0.9020 0.7808 0.8672 -0.0443 0.0028 -0.0439 322 LEU A C 2218 O O . LEU A 292 ? 0.8255 0.7069 0.7807 -0.0386 -0.0020 -0.0382 322 LEU A O 2219 C CB . LEU A 292 ? 0.8623 0.7626 0.8343 -0.0461 -0.0070 -0.0464 322 LEU A CB 2220 C CG . LEU A 292 ? 0.8681 0.7765 0.8462 -0.0489 -0.0077 -0.0476 322 LEU A CG 2221 C CD1 . LEU A 292 ? 0.8645 0.7864 0.8424 -0.0466 -0.0176 -0.0494 322 LEU A CD1 2222 C CD2 . LEU A 292 ? 0.8776 0.7797 0.8470 -0.0470 -0.0021 -0.0392 322 LEU A CD2 2223 N N . ASN A 293 ? 0.9517 0.8218 0.9222 -0.0475 0.0081 -0.0488 323 ASN A N 2224 C CA . ASN A 293 ? 0.9609 0.8215 0.9236 -0.0438 0.0100 -0.0463 323 ASN A CA 2225 C C . ASN A 293 ? 0.9643 0.8333 0.9214 -0.0391 0.0002 -0.0460 323 ASN A C 2226 O O . ASN A 293 ? 0.9667 0.8315 0.9135 -0.0334 0.0000 -0.0395 323 ASN A O 2227 C CB . ASN A 293 ? 0.9630 0.8114 0.9142 -0.0393 0.0177 -0.0360 323 ASN A CB 2228 C CG . ASN A 293 ? 1.0026 0.8421 0.9575 -0.0431 0.0281 -0.0352 323 ASN A CG 2229 O OD1 . ASN A 293 ? 1.0556 0.8895 1.0211 -0.0492 0.0344 -0.0420 323 ASN A OD1 2230 N ND2 . ASN A 293 ? 1.0049 0.8432 0.9515 -0.0397 0.0301 -0.0274 323 ASN A ND2 2231 N N . ILE A 294 ? 0.9845 0.8654 0.9483 -0.0409 -0.0076 -0.0530 324 ILE A N 2232 C CA . ILE A 294 ? 0.9992 0.8871 0.9576 -0.0364 -0.0160 -0.0533 324 ILE A CA 2233 C C . ILE A 294 ? 1.0106 0.8935 0.9707 -0.0371 -0.0163 -0.0600 324 ILE A C 2234 O O . ILE A 294 ? 1.0583 0.9417 1.0286 -0.0424 -0.0155 -0.0690 324 ILE A O 2235 C CB . ILE A 294 ? 1.0119 0.9140 0.9744 -0.0367 -0.0242 -0.0571 324 ILE A CB 2236 C CG1 . ILE A 294 ? 0.9976 0.9044 0.9596 -0.0370 -0.0235 -0.0517 324 ILE A CG1 2237 C CG2 . ILE A 294 ? 1.0205 0.9276 0.9755 -0.0312 -0.0313 -0.0560 324 ILE A CG2 2238 C CD1 . ILE A 294 ? 0.9887 0.8937 0.9396 -0.0317 -0.0232 -0.0419 324 ILE A CD1 2239 N N . PRO A 295 ? 0.9786 0.8568 0.9294 -0.0319 -0.0172 -0.0562 325 PRO A N 2240 C CA . PRO A 295 ? 0.9989 0.8725 0.9500 -0.0322 -0.0180 -0.0629 325 PRO A CA 2241 C C . PRO A 295 ? 1.0161 0.9006 0.9715 -0.0328 -0.0268 -0.0717 325 PRO A C 2242 O O . PRO A 295 ? 0.9735 0.8678 0.9261 -0.0297 -0.0330 -0.0696 325 PRO A O 2243 C CB . PRO A 295 ? 0.9971 0.8651 0.9365 -0.0254 -0.0177 -0.0556 325 PRO A CB 2244 C CG . PRO A 295 ? 0.9720 0.8379 0.9067 -0.0229 -0.0137 -0.0455 325 PRO A CG 2245 C CD . PRO A 295 ? 0.9896 0.8657 0.9298 -0.0258 -0.0167 -0.0460 325 PRO A CD 2246 N N . GLU A 296 ? 1.0739 0.9563 1.0356 -0.0363 -0.0271 -0.0816 326 GLU A N 2247 C CA . GLU A 296 ? 1.0994 0.9922 1.0662 -0.0369 -0.0355 -0.0915 326 GLU A CA 2248 C C . GLU A 296 ? 1.0389 0.9360 0.9948 -0.0298 -0.0430 -0.0903 326 GLU A C 2249 O O . GLU A 296 ? 0.9899 0.8978 0.9462 -0.0278 -0.0499 -0.0926 326 GLU A O 2250 C CB . GLU A 296 ? 1.1953 1.0838 1.1706 -0.0419 -0.0340 -0.1029 326 GLU A CB 2251 C CG . GLU A 296 ? 1.2785 1.1794 1.2630 -0.0439 -0.0422 -0.1149 326 GLU A CG 2252 C CD . GLU A 296 ? 1.3206 1.2176 1.3154 -0.0497 -0.0404 -0.1272 326 GLU A CD 2253 O OE1 . GLU A 296 ? 1.2779 1.1628 1.2673 -0.0493 -0.0360 -0.1275 326 GLU A OE1 2254 O OE2 . GLU A 296 ? 1.3363 1.2427 1.3452 -0.0546 -0.0432 -0.1370 326 GLU A OE2 2255 N N . GLN A 297 ? 1.0291 0.9172 0.9750 -0.0255 -0.0408 -0.0861 327 GLN A N 2256 C CA . GLN A 297 ? 1.0085 0.8984 0.9438 -0.0187 -0.0467 -0.0857 327 GLN A CA 2257 C C . GLN A 297 ? 0.9699 0.8680 0.9001 -0.0142 -0.0503 -0.0787 327 GLN A C 2258 O O . GLN A 297 ? 0.9626 0.8633 0.8852 -0.0088 -0.0551 -0.0793 327 GLN A O 2259 C CB . GLN A 297 ? 1.0227 0.9005 0.9489 -0.0151 -0.0424 -0.0821 327 GLN A CB 2260 C CG . GLN A 297 ? 1.0705 0.9438 0.9912 -0.0120 -0.0372 -0.0701 327 GLN A CG 2261 C CD . GLN A 297 ? 1.1048 0.9710 1.0302 -0.0161 -0.0293 -0.0662 327 GLN A CD 2262 O OE1 . GLN A 297 ? 1.0275 0.8925 0.9618 -0.0221 -0.0268 -0.0720 327 GLN A OE1 2263 N NE2 . GLN A 297 ? 1.1110 0.9722 1.0306 -0.0123 -0.0249 -0.0565 327 GLN A NE2 2264 N N . LEU A 298 ? 0.9837 0.8850 0.9174 -0.0161 -0.0476 -0.0722 328 LEU A N 2265 C CA . LEU A 298 ? 0.9606 0.8689 0.8901 -0.0124 -0.0503 -0.0657 328 LEU A CA 2266 C C . LEU A 298 ? 0.9341 0.8530 0.8657 -0.0116 -0.0570 -0.0709 328 LEU A C 2267 O O . LEU A 298 ? 0.9596 0.8831 0.8997 -0.0157 -0.0591 -0.0782 328 LEU A O 2268 C CB . LEU A 298 ? 0.9607 0.8697 0.8932 -0.0148 -0.0459 -0.0583 328 LEU A CB 2269 C CG . LEU A 298 ? 0.9548 0.8545 0.8831 -0.0135 -0.0397 -0.0511 328 LEU A CG 2270 C CD1 . LEU A 298 ? 0.9361 0.8369 0.8671 -0.0157 -0.0362 -0.0453 328 LEU A CD1 2271 C CD2 . LEU A 298 ? 0.9335 0.8322 0.8534 -0.0071 -0.0407 -0.0455 328 LEU A CD2 2272 N N . PRO A 299 ? 0.9025 0.8252 0.8268 -0.0062 -0.0600 -0.0670 329 PRO A N 2273 C CA . PRO A 299 ? 0.8839 0.8155 0.8082 -0.0040 -0.0659 -0.0709 329 PRO A CA 2274 C C . PRO A 299 ? 0.9151 0.8548 0.8484 -0.0084 -0.0664 -0.0714 329 PRO A C 2275 O O . PRO A 299 ? 0.9582 0.8963 0.8964 -0.0127 -0.0619 -0.0674 329 PRO A O 2276 C CB . PRO A 299 ? 0.8534 0.7846 0.7680 0.0021 -0.0660 -0.0644 329 PRO A CB 2277 C CG . PRO A 299 ? 0.8219 0.7481 0.7355 0.0016 -0.0606 -0.0564 329 PRO A CG 2278 C CD . PRO A 299 ? 0.8735 0.7926 0.7904 -0.0019 -0.0573 -0.0583 329 PRO A CD 2279 N N . GLN A 300 ? 0.9565 0.9044 0.8911 -0.0067 -0.0716 -0.0759 330 GLN A N 2280 C CA . GLN A 300 ? 0.9733 0.9293 0.9168 -0.0104 -0.0722 -0.0769 330 GLN A CA 2281 C C . GLN A 300 ? 0.9689 0.9249 0.9104 -0.0109 -0.0684 -0.0677 330 GLN A C 2282 O O . GLN A 300 ? 0.9160 0.8687 0.8494 -0.0070 -0.0671 -0.0617 330 GLN A O 2283 C CB . GLN A 300 ? 1.0625 1.0273 1.0059 -0.0067 -0.0788 -0.0825 330 GLN A CB 2284 C CG . GLN A 300 ? 1.1760 1.1417 1.1083 0.0004 -0.0805 -0.0776 330 GLN A CG 2285 C CD . GLN A 300 ? 1.3223 1.2970 1.2555 0.0037 -0.0855 -0.0814 330 GLN A CD 2286 O OE1 . GLN A 300 ? 1.3979 1.3789 1.3379 0.0029 -0.0901 -0.0898 330 GLN A OE1 2287 N NE2 . GLN A 300 ? 1.3419 1.3176 1.2688 0.0077 -0.0845 -0.0755 330 GLN A NE2 2288 N N . TRP A 301 ? 0.9230 0.8831 0.8725 -0.0156 -0.0665 -0.0671 331 TRP A N 2289 C CA . TRP A 301 ? 0.9018 0.8631 0.8495 -0.0160 -0.0638 -0.0596 331 TRP A CA 2290 C C . TRP A 301 ? 0.9148 0.8829 0.8598 -0.0125 -0.0671 -0.0591 331 TRP A C 2291 O O . TRP A 301 ? 0.9957 0.9700 0.9448 -0.0121 -0.0707 -0.0646 331 TRP A O 2292 C CB . TRP A 301 ? 0.8994 0.8608 0.8551 -0.0220 -0.0598 -0.0590 331 TRP A CB 2293 C CG . TRP A 301 ? 0.8423 0.8040 0.7954 -0.0225 -0.0569 -0.0517 331 TRP A CG 2294 C CD1 . TRP A 301 ? 0.8432 0.7992 0.7922 -0.0226 -0.0530 -0.0455 331 TRP A CD1 2295 C CD2 . TRP A 301 ? 0.7935 0.7617 0.7477 -0.0226 -0.0579 -0.0504 331 TRP A CD2 2296 N NE1 . TRP A 301 ? 0.8135 0.7724 0.7609 -0.0229 -0.0521 -0.0409 331 TRP A NE1 2297 C CE2 . TRP A 301 ? 0.7676 0.7335 0.7182 -0.0232 -0.0547 -0.0437 331 TRP A CE2 2298 C CE3 . TRP A 301 ? 0.7975 0.7731 0.7551 -0.0219 -0.0612 -0.0543 331 TRP A CE3 2299 C CZ2 . TRP A 301 ? 0.7484 0.7188 0.6987 -0.0237 -0.0545 -0.0412 331 TRP A CZ2 2300 C CZ3 . TRP A 301 ? 0.8207 0.8003 0.7780 -0.0222 -0.0605 -0.0512 331 TRP A CZ3 2301 C CH2 . TRP A 301 ? 0.7740 0.7507 0.7276 -0.0234 -0.0570 -0.0448 331 TRP A CH2 2302 N N . ASP A 302 ? 0.8909 0.8579 0.8295 -0.0098 -0.0656 -0.0526 332 ASP A N 2303 C CA . ASP A 302 ? 0.8270 0.7987 0.7628 -0.0071 -0.0667 -0.0506 332 ASP A CA 2304 C C . ASP A 302 ? 0.8301 0.8021 0.7665 -0.0097 -0.0631 -0.0445 332 ASP A C 2305 O O . ASP A 302 ? 0.7552 0.7230 0.6898 -0.0105 -0.0606 -0.0404 332 ASP A O 2306 C CB . ASP A 302 ? 0.8446 0.8137 0.7713 -0.0008 -0.0676 -0.0490 332 ASP A CB 2307 C CG . ASP A 302 ? 0.9101 0.8784 0.8335 0.0032 -0.0715 -0.0549 332 ASP A CG 2308 O OD1 . ASP A 302 ? 0.9380 0.9113 0.8666 0.0021 -0.0750 -0.0609 332 ASP A OD1 2309 O OD2 . ASP A 302 ? 0.9994 0.9624 0.9150 0.0078 -0.0712 -0.0537 332 ASP A OD2 2310 N N . MET A 303 ? 0.8876 0.8645 0.8258 -0.0106 -0.0631 -0.0439 333 MET A N 2311 C CA . MET A 303 ? 0.9122 0.8895 0.8502 -0.0128 -0.0603 -0.0389 333 MET A CA 2312 C C . MET A 303 ? 0.9088 0.8837 0.8414 -0.0099 -0.0590 -0.0346 333 MET A C 2313 O O . MET A 303 ? 0.9775 0.9515 0.9101 -0.0116 -0.0571 -0.0309 333 MET A O 2314 C CB . MET A 303 ? 0.9483 0.9308 0.8884 -0.0137 -0.0603 -0.0393 333 MET A CB 2315 C CG . MET A 303 ? 1.0002 0.9831 0.9408 -0.0169 -0.0574 -0.0354 333 MET A CG 2316 S SD . MET A 303 ? 1.1560 1.1431 1.0957 -0.0162 -0.0568 -0.0347 333 MET A SD 2317 C CE . MET A 303 ? 1.1956 1.1867 1.1422 -0.0188 -0.0574 -0.0388 333 MET A CE 2318 N N . CYS A 304 ? 0.8974 0.8714 0.8255 -0.0053 -0.0598 -0.0351 334 CYS A N 2319 C CA . CYS A 304 ? 0.9137 0.8847 0.8379 -0.0025 -0.0578 -0.0315 334 CYS A CA 2320 C C . CYS A 304 ? 0.8753 0.8416 0.7946 0.0018 -0.0586 -0.0328 334 CYS A C 2321 O O . CYS A 304 ? 0.8895 0.8554 0.8069 0.0040 -0.0612 -0.0369 334 CYS A O 2322 C CB . CYS A 304 ? 0.9016 0.8745 0.8242 -0.0011 -0.0558 -0.0293 334 CYS A CB 2323 S SG . CYS A 304 ? 1.0070 0.9851 0.9339 -0.0057 -0.0552 -0.0289 334 CYS A SG 2324 N N . ASN A 305 ? 0.8769 0.8399 0.7944 0.0034 -0.0564 -0.0297 335 ASN A N 2325 C CA . ASN A 305 ? 0.8671 0.8245 0.7792 0.0080 -0.0560 -0.0302 335 ASN A CA 2326 C C . ASN A 305 ? 0.8861 0.8420 0.7945 0.0120 -0.0529 -0.0276 335 ASN A C 2327 O O . ASN A 305 ? 0.8030 0.7602 0.7146 0.0110 -0.0500 -0.0242 335 ASN A O 2328 C CB . ASN A 305 ? 0.8858 0.8400 0.7993 0.0070 -0.0548 -0.0282 335 ASN A CB 2329 C CG . ASN A 305 ? 0.9335 0.8813 0.8416 0.0111 -0.0547 -0.0297 335 ASN A CG 2330 O OD1 . ASN A 305 ? 0.9769 0.9218 0.8790 0.0158 -0.0541 -0.0301 335 ASN A OD1 2331 N ND2 . ASN A 305 ? 0.9488 0.8931 0.8579 0.0095 -0.0548 -0.0303 335 ASN A ND2 2332 N N . PHE A 306 ? 0.9838 0.9369 0.8854 0.0169 -0.0533 -0.0296 336 PHE A N 2333 C CA . PHE A 306 ? 1.0887 1.0378 0.9849 0.0218 -0.0491 -0.0273 336 PHE A CA 2334 C C . PHE A 306 ? 1.0768 1.0212 0.9724 0.0237 -0.0453 -0.0244 336 PHE A C 2335 O O . PHE A 306 ? 1.0322 0.9762 0.9299 0.0241 -0.0406 -0.0213 336 PHE A O 2336 C CB . PHE A 306 ? 1.2199 1.1654 1.1066 0.0283 -0.0505 -0.0299 336 PHE A CB 2337 C CG . PHE A 306 ? 1.4050 1.3481 1.2872 0.0306 -0.0551 -0.0342 336 PHE A CG 2338 C CD1 . PHE A 306 ? 1.5469 1.4953 1.4332 0.0276 -0.0606 -0.0390 336 PHE A CD1 2339 C CD2 . PHE A 306 ? 1.4689 1.4044 1.3433 0.0357 -0.0536 -0.0340 336 PHE A CD2 2340 C CE1 . PHE A 306 ? 1.5906 1.5372 1.4741 0.0292 -0.0647 -0.0440 336 PHE A CE1 2341 C CE2 . PHE A 306 ? 1.5090 1.4421 1.3791 0.0377 -0.0579 -0.0387 336 PHE A CE2 2342 C CZ . PHE A 306 ? 1.5660 1.5049 1.4410 0.0342 -0.0636 -0.0441 336 PHE A CZ 2343 N N . LEU A 307 ? 1.0815 1.0225 0.9752 0.0244 -0.0471 -0.0255 337 LEU A N 2344 C CA . LEU A 307 ? 1.1127 1.0493 1.0062 0.0264 -0.0435 -0.0227 337 LEU A CA 2345 C C . LEU A 307 ? 1.0750 1.0170 0.9779 0.0224 -0.0413 -0.0193 337 LEU A C 2346 O O . LEU A 307 ? 1.0920 1.0336 0.9971 0.0238 -0.0368 -0.0168 337 LEU A O 2347 C CB . LEU A 307 ? 1.1946 1.1271 1.0859 0.0267 -0.0457 -0.0246 337 LEU A CB 2348 C CG . LEU A 307 ? 1.2599 1.1873 1.1421 0.0307 -0.0487 -0.0292 337 LEU A CG 2349 C CD1 . LEU A 307 ? 1.2602 1.1843 1.1428 0.0291 -0.0506 -0.0315 337 LEU A CD1 2350 C CD2 . LEU A 307 ? 1.2665 1.1868 1.1388 0.0380 -0.0453 -0.0282 337 LEU A CD2 2351 N N . VAL A 308 ? 1.0176 0.9645 0.9261 0.0175 -0.0444 -0.0196 338 VAL A N 2352 C CA . VAL A 308 ? 0.9520 0.9047 0.8684 0.0142 -0.0435 -0.0169 338 VAL A CA 2353 C C . VAL A 308 ? 0.9004 0.8569 0.8202 0.0137 -0.0408 -0.0160 338 VAL A C 2354 O O . VAL A 308 ? 0.9094 0.8675 0.8339 0.0144 -0.0375 -0.0141 338 VAL A O 2355 C CB . VAL A 308 ? 0.9233 0.8802 0.8430 0.0096 -0.0470 -0.0175 338 VAL A CB 2356 C CG1 . VAL A 308 ? 0.8982 0.8615 0.8244 0.0070 -0.0467 -0.0151 338 VAL A CG1 2357 C CG2 . VAL A 308 ? 0.9327 0.8850 0.8505 0.0097 -0.0483 -0.0180 338 VAL A CG2 2358 N N . ASN A 309 ? 0.8650 0.8229 0.7831 0.0125 -0.0417 -0.0177 339 ASN A N 2359 C CA . ASN A 309 ? 0.8683 0.8292 0.7896 0.0114 -0.0387 -0.0172 339 ASN A CA 2360 C C . ASN A 309 ? 0.8583 0.8144 0.7780 0.0155 -0.0329 -0.0159 339 ASN A C 2361 O O . ASN A 309 ? 0.8771 0.8361 0.8037 0.0141 -0.0293 -0.0148 339 ASN A O 2362 C CB . ASN A 309 ? 0.8994 0.8612 0.8177 0.0105 -0.0402 -0.0191 339 ASN A CB 2363 C CG . ASN A 309 ? 0.9099 0.8747 0.8320 0.0085 -0.0369 -0.0188 339 ASN A CG 2364 O OD1 . ASN A 309 ? 0.9291 0.8897 0.8486 0.0115 -0.0320 -0.0182 339 ASN A OD1 2365 N ND2 . ASN A 309 ? 0.9353 0.9064 0.8630 0.0035 -0.0389 -0.0192 339 ASN A ND2 2366 N N . LEU A 310 ? 0.8605 0.8090 0.7711 0.0208 -0.0318 -0.0163 340 LEU A N 2367 C CA . LEU A 310 ? 0.8820 0.8237 0.7890 0.0256 -0.0252 -0.0147 340 LEU A CA 2368 C C . LEU A 310 ? 0.9071 0.8485 0.8198 0.0260 -0.0219 -0.0127 340 LEU A C 2369 O O . LEU A 310 ? 0.9207 0.8602 0.8368 0.0272 -0.0154 -0.0112 340 LEU A O 2370 C CB . LEU A 310 ? 0.9097 0.8428 0.8037 0.0321 -0.0254 -0.0156 340 LEU A CB 2371 C CG . LEU A 310 ? 0.9456 0.8785 0.8335 0.0337 -0.0271 -0.0174 340 LEU A CG 2372 C CD1 . LEU A 310 ? 0.9916 0.9175 0.8664 0.0408 -0.0292 -0.0192 340 LEU A CD1 2373 C CD2 . LEU A 310 ? 0.9125 0.8439 0.8016 0.0341 -0.0205 -0.0156 340 LEU A CD2 2374 N N . GLN A 311 ? 0.9387 0.8816 0.8527 0.0251 -0.0258 -0.0126 341 GLN A N 2375 C CA . GLN A 311 ? 0.8974 0.8404 0.8169 0.0261 -0.0231 -0.0105 341 GLN A CA 2376 C C . GLN A 311 ? 0.8864 0.8395 0.8184 0.0216 -0.0242 -0.0099 341 GLN A C 2377 O O . GLN A 311 ? 0.9599 0.9149 0.8976 0.0225 -0.0229 -0.0084 341 GLN A O 2378 C CB . GLN A 311 ? 0.8993 0.8380 0.8135 0.0281 -0.0261 -0.0106 341 GLN A CB 2379 C CG . GLN A 311 ? 0.9237 0.8522 0.8256 0.0336 -0.0249 -0.0116 341 GLN A CG 2380 C CD . GLN A 311 ? 0.9582 0.8822 0.8560 0.0351 -0.0272 -0.0122 341 GLN A CD 2381 O OE1 . GLN A 311 ? 1.0329 0.9589 0.9304 0.0322 -0.0324 -0.0142 341 GLN A OE1 2382 N NE2 . GLN A 311 ? 1.0308 0.9483 0.9257 0.0394 -0.0228 -0.0105 341 GLN A NE2 2383 N N . TYR A 312 ? 0.8599 0.8195 0.7959 0.0172 -0.0265 -0.0112 342 TYR A N 2384 C CA . TYR A 312 ? 0.8110 0.7806 0.7571 0.0132 -0.0291 -0.0113 342 TYR A CA 2385 C C . TYR A 312 ? 0.8466 0.8212 0.8032 0.0120 -0.0245 -0.0117 342 TYR A C 2386 O O . TYR A 312 ? 0.8806 0.8531 0.8373 0.0114 -0.0201 -0.0127 342 TYR A O 2387 C CB . TYR A 312 ? 0.7378 0.7117 0.6830 0.0090 -0.0337 -0.0128 342 TYR A CB 2388 C CG . TYR A 312 ? 0.7033 0.6859 0.6551 0.0060 -0.0377 -0.0127 342 TYR A CG 2389 C CD1 . TYR A 312 ? 0.7101 0.7009 0.6712 0.0034 -0.0371 -0.0140 342 TYR A CD1 2390 C CD2 . TYR A 312 ? 0.6697 0.6520 0.6181 0.0060 -0.0419 -0.0116 342 TYR A CD2 2391 C CE1 . TYR A 312 ? 0.6883 0.6873 0.6541 0.0016 -0.0415 -0.0143 342 TYR A CE1 2392 C CE2 . TYR A 312 ? 0.6851 0.6742 0.6375 0.0045 -0.0453 -0.0112 342 TYR A CE2 2393 C CZ . TYR A 312 ? 0.6818 0.6796 0.6423 0.0026 -0.0456 -0.0125 342 TYR A CZ 2394 O OH . TYR A 312 ? 0.6489 0.6536 0.6119 0.0020 -0.0497 -0.0123 342 TYR A OH 2395 N N . ARG A 313 ? 0.9118 0.8934 0.8775 0.0117 -0.0254 -0.0113 343 ARG A N 2396 C CA . ARG A 313 ? 0.9763 0.9645 0.9548 0.0103 -0.0214 -0.0126 343 ARG A CA 2397 C C . ARG A 313 ? 0.9555 0.9556 0.9426 0.0058 -0.0262 -0.0150 343 ARG A C 2398 O O . ARG A 313 ? 0.9367 0.9429 0.9254 0.0061 -0.0318 -0.0145 343 ARG A O 2399 C CB . ARG A 313 ? 1.0378 1.0264 1.0217 0.0139 -0.0190 -0.0109 343 ARG A CB 2400 C CG . ARG A 313 ? 1.1289 1.1217 1.1260 0.0134 -0.0125 -0.0123 343 ARG A CG 2401 C CD . ARG A 313 ? 1.1708 1.1519 1.1631 0.0164 -0.0035 -0.0111 343 ARG A CD 2402 N NE . ARG A 313 ? 1.2170 1.2021 1.2237 0.0164 0.0032 -0.0120 343 ARG A NE 2403 C CZ . ARG A 313 ? 1.2831 1.2706 1.2964 0.0193 0.0045 -0.0107 343 ARG A CZ 2404 N NH1 . ARG A 313 ? 1.2840 1.2692 1.2896 0.0227 -0.0001 -0.0080 343 ARG A NH1 2405 N NH2 . ARG A 313 ? 1.3551 1.3472 1.3834 0.0187 0.0112 -0.0121 343 ARG A NH2 2406 N N . ARG A 314 ? 0.9582 0.9607 0.9498 0.0022 -0.0237 -0.0177 344 ARG A N 2407 C CA . ARG A 314 ? 0.8976 0.9106 0.8964 -0.0022 -0.0279 -0.0209 344 ARG A CA 2408 C C . ARG A 314 ? 0.8820 0.9055 0.8968 -0.0034 -0.0267 -0.0237 344 ARG A C 2409 O O . ARG A 314 ? 1.0069 1.0291 1.0295 -0.0041 -0.0194 -0.0252 344 ARG A O 2410 C CB . ARG A 314 ? 0.8993 0.9095 0.8958 -0.0057 -0.0251 -0.0230 344 ARG A CB 2411 C CG . ARG A 314 ? 0.9496 0.9524 0.9325 -0.0051 -0.0274 -0.0212 344 ARG A CG 2412 C CD . ARG A 314 ? 0.9701 0.9673 0.9503 -0.0066 -0.0220 -0.0224 344 ARG A CD 2413 N NE . ARG A 314 ? 0.9455 0.9389 0.9155 -0.0070 -0.0250 -0.0219 344 ARG A NE 2414 C CZ . ARG A 314 ? 0.9071 0.8925 0.8667 -0.0035 -0.0247 -0.0199 344 ARG A CZ 2415 N NH1 . ARG A 314 ? 0.9303 0.9092 0.8862 0.0010 -0.0218 -0.0181 344 ARG A NH1 2416 N NH2 . ARG A 314 ? 0.8711 0.8550 0.8241 -0.0044 -0.0276 -0.0202 344 ARG A NH2 2417 N N . LEU A 315 ? 0.8278 0.8618 0.8477 -0.0034 -0.0334 -0.0248 345 LEU A N 2418 C CA . LEU A 315 ? 0.7784 0.8244 0.8144 -0.0036 -0.0336 -0.0278 345 LEU A CA 2419 C C . LEU A 315 ? 0.7748 0.8325 0.8196 -0.0081 -0.0376 -0.0333 345 LEU A C 2420 O O . LEU A 315 ? 0.8081 0.8724 0.8672 -0.0110 -0.0340 -0.0379 345 LEU A O 2421 C CB . LEU A 315 ? 0.7721 0.8223 0.8080 0.0011 -0.0386 -0.0251 345 LEU A CB 2422 C CG . LEU A 315 ? 0.7636 0.8021 0.7897 0.0057 -0.0355 -0.0200 345 LEU A CG 2423 C CD1 . LEU A 315 ? 0.7791 0.8213 0.8037 0.0104 -0.0407 -0.0172 345 LEU A CD1 2424 C CD2 . LEU A 315 ? 0.7753 0.8091 0.8081 0.0066 -0.0267 -0.0199 345 LEU A CD2 2425 N N . TYR A 316 ? 0.7871 0.8468 0.8233 -0.0086 -0.0447 -0.0332 346 TYR A N 2426 C CA . TYR A 316 ? 0.7903 0.8603 0.8327 -0.0125 -0.0490 -0.0386 346 TYR A CA 2427 C C . TYR A 316 ? 0.8105 0.8750 0.8516 -0.0177 -0.0439 -0.0411 346 TYR A C 2428 O O . TYR A 316 ? 0.8467 0.9003 0.8756 -0.0177 -0.0417 -0.0379 346 TYR A O 2429 C CB . TYR A 316 ? 0.7681 0.8411 0.8004 -0.0106 -0.0576 -0.0373 346 TYR A CB 2430 C CG . TYR A 316 ? 0.7742 0.8518 0.8061 -0.0047 -0.0624 -0.0344 346 TYR A CG 2431 C CD1 . TYR A 316 ? 0.7753 0.8666 0.8211 -0.0030 -0.0656 -0.0379 346 TYR A CD1 2432 C CD2 . TYR A 316 ? 0.7874 0.8558 0.8056 -0.0007 -0.0637 -0.0285 346 TYR A CD2 2433 C CE1 . TYR A 316 ? 0.8116 0.9067 0.8562 0.0033 -0.0698 -0.0349 346 TYR A CE1 2434 C CE2 . TYR A 316 ? 0.7726 0.8437 0.7893 0.0050 -0.0673 -0.0255 346 TYR A CE2 2435 C CZ . TYR A 316 ? 0.7986 0.8828 0.8278 0.0074 -0.0704 -0.0283 346 TYR A CZ 2436 O OH . TYR A 316 ? 0.7886 0.8749 0.8156 0.0140 -0.0737 -0.0248 346 TYR A OH 2437 N N . ARG A 317 ? 0.8402 0.9130 0.8950 -0.0220 -0.0421 -0.0473 347 ARG A N 2438 C CA . ARG A 317 ? 0.8877 0.9560 0.9442 -0.0271 -0.0360 -0.0505 347 ARG A CA 2439 C C . ARG A 317 ? 0.8960 0.9705 0.9504 -0.0308 -0.0420 -0.0548 347 ARG A C 2440 O O . ARG A 317 ? 0.8510 0.9210 0.9038 -0.0350 -0.0381 -0.0571 347 ARG A O 2441 C CB . ARG A 317 ? 0.9549 1.0275 1.0296 -0.0298 -0.0285 -0.0550 347 ARG A CB 2442 C CG . ARG A 317 ? 1.0025 1.0645 1.0780 -0.0330 -0.0175 -0.0557 347 ARG A CG 2443 C CD . ARG A 317 ? 1.0152 1.0611 1.0740 -0.0292 -0.0130 -0.0487 347 ARG A CD 2444 N NE . ARG A 317 ? 1.0737 1.1162 1.1270 -0.0235 -0.0143 -0.0434 347 ARG A NE 2445 C CZ . ARG A 317 ? 1.1333 1.1631 1.1729 -0.0194 -0.0113 -0.0379 347 ARG A CZ 2446 N NH1 . ARG A 317 ? 1.1565 1.1761 1.1862 -0.0199 -0.0071 -0.0367 347 ARG A NH1 2447 N NH2 . ARG A 317 ? 1.1166 1.1439 1.1520 -0.0145 -0.0128 -0.0339 347 ARG A NH2 2448 N N . SER A 318 ? 0.8793 0.9638 0.9332 -0.0287 -0.0513 -0.0559 348 SER A N 2449 C CA . SER A 318 ? 0.8642 0.9549 0.9151 -0.0312 -0.0577 -0.0601 348 SER A CA 2450 C C . SER A 318 ? 0.8572 0.9546 0.9015 -0.0261 -0.0674 -0.0583 348 SER A C 2451 O O . SER A 318 ? 0.8574 0.9619 0.9083 -0.0221 -0.0702 -0.0578 348 SER A O 2452 C CB . SER A 318 ? 0.8728 0.9745 0.9406 -0.0363 -0.0568 -0.0691 348 SER A CB 2453 O OG . SER A 318 ? 0.9804 1.0895 1.0453 -0.0379 -0.0642 -0.0739 348 SER A OG 2454 N N . MET A 319 ? 0.8605 0.9552 0.8916 -0.0258 -0.0720 -0.0574 349 MET A N 2455 C CA . MET A 319 ? 0.8680 0.9665 0.8899 -0.0202 -0.0803 -0.0549 349 MET A CA 2456 C C . MET A 319 ? 0.8582 0.9702 0.8847 -0.0202 -0.0879 -0.0617 349 MET A C 2457 O O . MET A 319 ? 0.8928 1.0073 0.9093 -0.0154 -0.0949 -0.0602 349 MET A O 2458 C CB . MET A 319 ? 0.8678 0.9541 0.8714 -0.0190 -0.0802 -0.0492 349 MET A CB 2459 C CG . MET A 319 ? 0.8690 0.9433 0.8672 -0.0178 -0.0746 -0.0427 349 MET A CG 2460 S SD . MET A 319 ? 0.9012 0.9750 0.8968 -0.0106 -0.0769 -0.0371 349 MET A SD 2461 C CE . MET A 319 ? 0.8739 0.9522 0.8861 -0.0111 -0.0721 -0.0389 349 MET A CE 2462 N N . ASN A 320 ? 0.8305 0.9510 0.8721 -0.0254 -0.0864 -0.0694 350 ASN A N 2463 C CA . ASN A 320 ? 0.8420 0.9772 0.8907 -0.0257 -0.0941 -0.0775 350 ASN A CA 2464 C C . ASN A 320 ? 0.8767 1.0237 0.9268 -0.0181 -0.1029 -0.0773 350 ASN A C 2465 O O . ASN A 320 ? 0.9546 1.1077 0.9968 -0.0145 -0.1113 -0.0795 350 ASN A O 2466 C CB . ASN A 320 ? 0.8533 0.9965 0.9224 -0.0324 -0.0897 -0.0860 350 ASN A CB 2467 C CG . ASN A 320 ? 0.8427 1.0011 0.9201 -0.0340 -0.0973 -0.0961 350 ASN A CG 2468 O OD1 . ASN A 320 ? 0.8900 1.0635 0.9817 -0.0321 -0.1023 -0.1013 350 ASN A OD1 2469 N ND2 . ASN A 320 ? 0.8530 1.0080 0.9215 -0.0373 -0.0985 -0.0991 350 ASN A ND2 2470 N N . SER A 321 ? 0.8431 0.9929 0.9025 -0.0151 -0.1010 -0.0747 351 SER A N 2471 C CA . SER A 321 ? 0.8602 1.0207 0.9212 -0.0073 -0.1088 -0.0740 351 SER A CA 2472 C C . SER A 321 ? 0.8714 1.0236 0.9103 -0.0004 -0.1132 -0.0666 351 SER A C 2473 O O . SER A 321 ? 0.9515 1.1112 0.9839 0.0048 -0.1217 -0.0683 351 SER A O 2474 C CB . SER A 321 ? 0.8387 1.0002 0.9111 -0.0050 -0.1044 -0.0709 351 SER A CB 2475 O OG . SER A 321 ? 0.8753 1.0432 0.9681 -0.0114 -0.0989 -0.0774 351 SER A OG 2476 N N . GLN A 322 ? 0.8601 0.9961 0.8873 -0.0004 -0.1070 -0.0586 352 GLN A N 2477 C CA . GLN A 322 ? 0.8627 0.9891 0.8709 0.0058 -0.1090 -0.0510 352 GLN A CA 2478 C C . GLN A 322 ? 0.8777 1.0036 0.8722 0.0068 -0.1143 -0.0526 352 GLN A C 2479 O O . GLN A 322 ? 0.8805 1.0056 0.8623 0.0142 -0.1193 -0.0491 352 GLN A O 2480 C CB . GLN A 322 ? 0.8840 0.9935 0.8841 0.0038 -0.1008 -0.0439 352 GLN A CB 2481 C CG . GLN A 322 ? 0.8719 0.9792 0.8804 0.0053 -0.0960 -0.0405 352 GLN A CG 2482 C CD . GLN A 322 ? 0.8625 0.9737 0.8879 -0.0006 -0.0905 -0.0452 352 GLN A CD 2483 O OE1 . GLN A 322 ? 0.8862 1.0013 0.9178 -0.0064 -0.0897 -0.0510 352 GLN A OE1 2484 N NE2 . GLN A 322 ? 0.8469 0.9561 0.8793 0.0009 -0.0860 -0.0425 352 GLN A NE2 2485 N N . TYR A 323 ? 0.8738 0.9990 0.8699 0.0000 -0.1125 -0.0575 353 TYR A N 2486 C CA . TYR A 323 ? 0.9151 1.0375 0.8970 0.0002 -0.1162 -0.0588 353 TYR A CA 2487 C C . TYR A 323 ? 0.9509 1.0886 0.9351 0.0044 -0.1261 -0.0655 353 TYR A C 2488 O O . TYR A 323 ? 1.0041 1.1401 0.9724 0.0106 -0.1314 -0.0635 353 TYR A O 2489 C CB . TYR A 323 ? 0.9168 1.0328 0.8990 -0.0081 -0.1107 -0.0617 353 TYR A CB 2490 C CG . TYR A 323 ? 0.9374 1.0365 0.9086 -0.0099 -0.1034 -0.0542 353 TYR A CG 2491 C CD1 . TYR A 323 ? 0.9502 1.0395 0.9035 -0.0068 -0.1039 -0.0493 353 TYR A CD1 2492 C CD2 . TYR A 323 ? 0.9520 1.0451 0.9309 -0.0143 -0.0958 -0.0525 353 TYR A CD2 2493 C CE1 . TYR A 323 ? 0.9804 1.0559 0.9259 -0.0087 -0.0974 -0.0436 353 TYR A CE1 2494 C CE2 . TYR A 323 ? 0.9630 1.0424 0.9327 -0.0155 -0.0901 -0.0467 353 TYR A CE2 2495 C CZ . TYR A 323 ? 0.9854 1.0566 0.9394 -0.0130 -0.0911 -0.0425 353 TYR A CZ 2496 O OH . TYR A 323 ? 1.0081 1.0668 0.9548 -0.0145 -0.0855 -0.0375 353 TYR A OH 2497 N N . LEU A 324 ? 0.9019 1.0545 0.9058 0.0014 -0.1284 -0.0736 354 LEU A N 2498 C CA . LEU A 324 ? 0.9018 1.0715 0.9107 0.0057 -0.1387 -0.0811 354 LEU A CA 2499 C C . LEU A 324 ? 0.9499 1.1230 0.9516 0.0167 -0.1445 -0.0758 354 LEU A C 2500 O O . LEU A 324 ? 1.0281 1.2064 1.0185 0.0240 -0.1529 -0.0770 354 LEU A O 2501 C CB . LEU A 324 ? 0.8772 1.0626 0.9118 0.0000 -0.1389 -0.0910 354 LEU A CB 2502 C CG . LEU A 324 ? 0.8404 1.0240 0.8837 -0.0107 -0.1333 -0.0978 354 LEU A CG 2503 C CD1 . LEU A 324 ? 0.8143 1.0107 0.8847 -0.0163 -0.1306 -0.1059 354 LEU A CD1 2504 C CD2 . LEU A 324 ? 0.7991 0.9855 0.8326 -0.0115 -0.1395 -0.1041 354 LEU A CD2 2505 N N . LYS A 325 ? 0.9622 1.1313 0.9692 0.0184 -0.1396 -0.0697 355 LYS A N 2506 C CA . LYS A 325 ? 1.0046 1.1742 1.0042 0.0288 -0.1432 -0.0635 355 LYS A CA 2507 C C . LYS A 325 ? 1.0326 1.1877 1.0061 0.0350 -0.1436 -0.0556 355 LYS A C 2508 O O . LYS A 325 ? 1.1248 1.2823 1.0882 0.0450 -0.1493 -0.0526 355 LYS A O 2509 C CB . LYS A 325 ? 1.0219 1.1865 1.0306 0.0283 -0.1361 -0.0580 355 LYS A CB 2510 C CG . LYS A 325 ? 1.1150 1.2846 1.1230 0.0385 -0.1399 -0.0537 355 LYS A CG 2511 C CD . LYS A 325 ? 1.1558 1.3207 1.1739 0.0373 -0.1324 -0.0493 355 LYS A CD 2512 C CE . LYS A 325 ? 1.1413 1.3202 1.1850 0.0318 -0.1311 -0.0569 355 LYS A CE 2513 N NZ . LYS A 325 ? 1.1577 1.3348 1.2101 0.0343 -0.1259 -0.0523 355 LYS A NZ 2514 N N . LEU A 326 ? 1.0117 1.1516 0.9748 0.0295 -0.1371 -0.0522 356 LEU A N 2515 C CA . LEU A 326 ? 1.0215 1.1470 0.9612 0.0343 -0.1362 -0.0454 356 LEU A CA 2516 C C . LEU A 326 ? 0.9841 1.1139 0.9132 0.0362 -0.1428 -0.0504 356 LEU A C 2517 O O . LEU A 326 ? 0.9860 1.1084 0.8956 0.0437 -0.1449 -0.0459 356 LEU A O 2518 C CB . LEU A 326 ? 1.0493 1.1576 0.9834 0.0277 -0.1265 -0.0401 356 LEU A CB 2519 C CG . LEU A 326 ? 1.0544 1.1543 0.9923 0.0276 -0.1198 -0.0336 356 LEU A CG 2520 C CD1 . LEU A 326 ? 1.0220 1.1121 0.9636 0.0186 -0.1117 -0.0329 356 LEU A CD1 2521 C CD2 . LEU A 326 ? 1.0353 1.1237 0.9567 0.0357 -0.1185 -0.0251 356 LEU A CD2 2522 N N . LEU A 327 ? 0.9196 1.0603 0.8610 0.0296 -0.1456 -0.0598 357 LEU A N 2523 C CA . LEU A 327 ? 0.9482 1.0934 0.8805 0.0306 -0.1520 -0.0658 357 LEU A CA 2524 C C . LEU A 327 ? 0.9931 1.1546 0.9258 0.0395 -0.1635 -0.0711 357 LEU A C 2525 O O . LEU A 327 ? 0.9945 1.1563 0.9115 0.0449 -0.1695 -0.0729 357 LEU A O 2526 C CB . LEU A 327 ? 0.9466 1.0964 0.8920 0.0196 -0.1499 -0.0745 357 LEU A CB 2527 C CG . LEU A 327 ? 0.9159 1.0490 0.8546 0.0123 -0.1403 -0.0702 357 LEU A CG 2528 C CD1 . LEU A 327 ? 0.9017 1.0398 0.8584 0.0016 -0.1363 -0.0777 357 LEU A CD1 2529 C CD2 . LEU A 327 ? 0.9250 1.0481 0.8415 0.0151 -0.1413 -0.0683 357 LEU A CD2 2530 N N . SER A 328 ? 1.0810 1.2565 1.0317 0.0412 -0.1666 -0.0738 358 SER A N 2531 C CA . SER A 328 ? 1.1387 1.3327 1.0934 0.0499 -0.1783 -0.0798 358 SER A CA 2532 C C . SER A 328 ? 1.1737 1.3611 1.1037 0.0634 -0.1829 -0.0725 358 SER A C 2533 O O . SER A 328 ? 1.1569 1.3530 1.0779 0.0704 -0.1925 -0.0775 358 SER A O 2534 C CB . SER A 328 ? 1.1196 1.3270 1.0971 0.0504 -0.1788 -0.0815 358 SER A CB 2535 O OG . SER A 328 ? 1.1282 1.3241 1.0984 0.0558 -0.1734 -0.0704 358 SER A OG 2536 N N . SER A 329 ? 1.2244 1.3958 1.1432 0.0671 -0.1757 -0.0611 359 SER A N 2537 C CA . SER A 329 ? 1.2522 1.4138 1.1467 0.0799 -0.1775 -0.0529 359 SER A CA 2538 C C . SER A 329 ? 1.2303 1.3822 1.1026 0.0817 -0.1787 -0.0529 359 SER A C 2539 O O . SER A 329 ? 1.2745 1.4270 1.1290 0.0932 -0.1853 -0.0517 359 SER A O 2540 C CB . SER A 329 ? 1.2826 1.4260 1.1700 0.0809 -0.1673 -0.0412 359 SER A CB 2541 O OG . SER A 329 ? 1.3671 1.4924 1.2445 0.0737 -0.1584 -0.0370 359 SER A OG 2542 N N . GLN A 330 ? 1.2155 1.3578 1.0880 0.0709 -0.1719 -0.0538 360 GLN A N 2543 C CA . GLN A 330 ? 1.2498 1.3805 1.1019 0.0711 -0.1708 -0.0533 360 GLN A CA 2544 C C . GLN A 330 ? 1.1961 1.3066 1.0227 0.0794 -0.1651 -0.0419 360 GLN A C 2545 O O . GLN A 330 ? 1.1130 1.2153 0.9196 0.0837 -0.1659 -0.0410 360 GLN A O 2546 C CB . GLN A 330 ? 1.2941 1.4393 1.1428 0.0751 -0.1823 -0.0632 360 GLN A CB 2547 C CG . GLN A 330 ? 1.3399 1.5008 1.2116 0.0641 -0.1854 -0.0753 360 GLN A CG 2548 C CD . GLN A 330 ? 1.4462 1.6252 1.3179 0.0695 -0.1986 -0.0862 360 GLN A CD 2549 O OE1 . GLN A 330 ? 1.4489 1.6463 1.3347 0.0739 -0.2068 -0.0915 360 GLN A OE1 2550 N NE2 . GLN A 330 ? 1.5427 1.7167 1.3979 0.0700 -0.2010 -0.0896 360 GLN A NE2 2551 N N . LYS A 331 ? 1.2135 1.3148 1.0409 0.0811 -0.1584 -0.0334 361 LYS A N 2552 C CA . LYS A 331 ? 1.2429 1.3229 1.0494 0.0863 -0.1503 -0.0228 361 LYS A CA 2553 C C . LYS A 331 ? 1.1898 1.2550 0.9981 0.0751 -0.1393 -0.0198 361 LYS A C 2554 O O . LYS A 331 ? 1.1785 1.2258 0.9706 0.0773 -0.1317 -0.0125 361 LYS A O 2555 C CB . LYS A 331 ? 1.2912 1.3677 1.0975 0.0938 -0.1480 -0.0154 361 LYS A CB 2556 C CG . LYS A 331 ? 1.3148 1.4073 1.1226 0.1050 -0.1586 -0.0180 361 LYS A CG 2557 C CD . LYS A 331 ? 1.3318 1.4190 1.1394 0.1120 -0.1548 -0.0099 361 LYS A CD 2558 C CE . LYS A 331 ? 1.3791 1.4820 1.1870 0.1246 -0.1653 -0.0119 361 LYS A CE 2559 N NZ . LYS A 331 ? 1.3927 1.4896 1.1999 0.1319 -0.1611 -0.0037 361 LYS A NZ 2560 N N . TYR A 332 ? 1.1266 1.1993 0.9548 0.0635 -0.1381 -0.0256 362 TYR A N 2561 C CA . TYR A 332 ? 1.0446 1.1054 0.8781 0.0537 -0.1279 -0.0224 362 TYR A CA 2562 C C . TYR A 332 ? 1.0308 1.0902 0.8661 0.0446 -0.1259 -0.0274 362 TYR A C 2563 O O . TYR A 332 ? 1.0365 1.1090 0.8831 0.0400 -0.1311 -0.0359 362 TYR A O 2564 C CB . TYR A 332 ? 1.0169 1.0834 0.8706 0.0488 -0.1256 -0.0225 362 TYR A CB 2565 C CG . TYR A 332 ? 1.0178 1.0857 0.8709 0.0576 -0.1272 -0.0176 362 TYR A CG 2566 C CD1 . TYR A 332 ? 1.0377 1.0909 0.8732 0.0654 -0.1229 -0.0090 362 TYR A CD1 2567 C CD2 . TYR A 332 ? 0.9896 1.0730 0.8596 0.0585 -0.1323 -0.0215 362 TYR A CD2 2568 C CE1 . TYR A 332 ? 1.0256 1.0793 0.8598 0.0740 -0.1239 -0.0043 362 TYR A CE1 2569 C CE2 . TYR A 332 ? 0.9692 1.0539 0.8385 0.0671 -0.1337 -0.0170 362 TYR A CE2 2570 C CZ . TYR A 332 ? 0.9932 1.0629 0.8441 0.0749 -0.1295 -0.0083 362 TYR A CZ 2571 O OH . TYR A 332 ? 1.0147 1.0844 0.8639 0.0838 -0.1301 -0.0034 362 TYR A OH 2572 N N . GLN A 333 ? 0.9780 1.0211 0.8028 0.0418 -0.1176 -0.0223 363 GLN A N 2573 C CA . GLN A 333 ? 0.9928 1.0321 0.8175 0.0338 -0.1142 -0.0257 363 GLN A CA 2574 C C . GLN A 333 ? 0.9468 0.9847 0.7879 0.0236 -0.1078 -0.0261 363 GLN A C 2575 O O . GLN A 333 ? 0.9538 0.9812 0.7944 0.0224 -0.1009 -0.0201 363 GLN A O 2576 C CB . GLN A 333 ? 1.0796 1.1020 0.8837 0.0373 -0.1084 -0.0197 363 GLN A CB 2577 C CG . GLN A 333 ? 1.2007 1.2184 1.0006 0.0312 -0.1053 -0.0229 363 GLN A CG 2578 C CD . GLN A 333 ? 1.3171 1.3162 1.1029 0.0318 -0.0959 -0.0159 363 GLN A CD 2579 O OE1 . GLN A 333 ? 1.3230 1.3122 1.1021 0.0366 -0.0912 -0.0088 363 GLN A OE1 2580 N NE2 . GLN A 333 ? 1.3620 1.3560 1.1440 0.0268 -0.0923 -0.0180 363 GLN A NE2 2581 N N . ILE A 334 ? 0.9042 0.9523 0.7593 0.0165 -0.1099 -0.0333 364 ILE A N 2582 C CA . ILE A 334 ? 0.8592 0.9075 0.7302 0.0082 -0.1047 -0.0341 364 ILE A CA 2583 C C . ILE A 334 ? 0.8164 0.8596 0.6880 0.0005 -0.0998 -0.0366 364 ILE A C 2584 O O . ILE A 334 ? 0.8304 0.8777 0.6993 -0.0009 -0.1029 -0.0421 364 ILE A O 2585 C CB . ILE A 334 ? 0.8962 0.9597 0.7854 0.0060 -0.1092 -0.0402 364 ILE A CB 2586 C CG1 . ILE A 334 ? 0.9131 0.9823 0.8034 0.0137 -0.1137 -0.0376 364 ILE A CG1 2587 C CG2 . ILE A 334 ? 0.8999 0.9622 0.8037 -0.0018 -0.1030 -0.0408 364 ILE A CG2 2588 C CD1 . ILE A 334 ? 0.9227 1.0085 0.8304 0.0128 -0.1191 -0.0443 364 ILE A CD1 2589 N N . LEU A 335 ? 0.7767 0.8115 0.6521 -0.0040 -0.0926 -0.0330 365 LEU A N 2590 C CA . LEU A 335 ? 0.7938 0.8241 0.6714 -0.0109 -0.0875 -0.0350 365 LEU A CA 2591 C C . LEU A 335 ? 0.8187 0.8502 0.7106 -0.0164 -0.0835 -0.0356 365 LEU A C 2592 O O . LEU A 335 ? 0.8498 0.8777 0.7450 -0.0155 -0.0809 -0.0314 365 LEU A O 2593 C CB . LEU A 335 ? 0.8014 0.8184 0.6666 -0.0104 -0.0818 -0.0298 365 LEU A CB 2594 C CG . LEU A 335 ? 0.7759 0.7874 0.6429 -0.0167 -0.0760 -0.0309 365 LEU A CG 2595 C CD1 . LEU A 335 ? 0.7836 0.7974 0.6454 -0.0183 -0.0780 -0.0360 365 LEU A CD1 2596 C CD2 . LEU A 335 ? 0.8050 0.8042 0.6643 -0.0161 -0.0696 -0.0250 365 LEU A CD2 2597 N N . LEU A 336 ? 0.8122 0.8479 0.7119 -0.0219 -0.0825 -0.0410 366 LEU A N 2598 C CA . LEU A 336 ? 0.7985 0.8327 0.7087 -0.0267 -0.0773 -0.0411 366 LEU A CA 2599 C C . LEU A 336 ? 0.8108 0.8378 0.7163 -0.0305 -0.0724 -0.0413 366 LEU A C 2600 O O . LEU A 336 ? 0.8744 0.9028 0.7765 -0.0324 -0.0734 -0.0455 366 LEU A O 2601 C CB . LEU A 336 ? 0.8104 0.8544 0.7344 -0.0297 -0.0786 -0.0470 366 LEU A CB 2602 C CG . LEU A 336 ? 0.7709 0.8203 0.7040 -0.0272 -0.0803 -0.0458 366 LEU A CG 2603 C CD1 . LEU A 336 ? 0.7731 0.8295 0.7031 -0.0216 -0.0873 -0.0461 366 LEU A CD1 2604 C CD2 . LEU A 336 ? 0.7886 0.8444 0.7366 -0.0314 -0.0782 -0.0509 366 LEU A CD2 2605 N N . TYR A 337 ? 0.7875 0.8070 0.6927 -0.0314 -0.0674 -0.0371 367 TYR A N 2606 C CA . TYR A 337 ? 0.7959 0.8091 0.6983 -0.0347 -0.0624 -0.0371 367 TYR A CA 2607 C C . TYR A 337 ? 0.7628 0.7747 0.6741 -0.0374 -0.0580 -0.0368 367 TYR A C 2608 O O . TYR A 337 ? 0.7051 0.7180 0.6217 -0.0359 -0.0581 -0.0348 367 TYR A O 2609 C CB . TYR A 337 ? 0.7887 0.7935 0.6807 -0.0326 -0.0603 -0.0325 367 TYR A CB 2610 C CG . TYR A 337 ? 0.8167 0.8174 0.7102 -0.0307 -0.0585 -0.0278 367 TYR A CG 2611 C CD1 . TYR A 337 ? 0.8102 0.8118 0.7016 -0.0266 -0.0616 -0.0253 367 TYR A CD1 2612 C CD2 . TYR A 337 ? 0.7995 0.7957 0.6966 -0.0328 -0.0538 -0.0262 367 TYR A CD2 2613 C CE1 . TYR A 337 ? 0.8081 0.8052 0.7009 -0.0251 -0.0595 -0.0214 367 TYR A CE1 2614 C CE2 . TYR A 337 ? 0.7706 0.7635 0.6697 -0.0314 -0.0525 -0.0229 367 TYR A CE2 2615 C CZ . TYR A 337 ? 0.7954 0.7884 0.6923 -0.0278 -0.0551 -0.0206 367 TYR A CZ 2616 O OH . TYR A 337 ? 0.8187 0.8077 0.7176 -0.0267 -0.0534 -0.0178 367 TYR A OH 2617 N N . ASN A 338 ? 0.7922 0.8016 0.7042 -0.0407 -0.0540 -0.0388 368 ASN A N 2618 C CA . ASN A 338 ? 0.8449 0.8528 0.7641 -0.0423 -0.0496 -0.0387 368 ASN A CA 2619 C C . ASN A 338 ? 0.8317 0.8336 0.7476 -0.0439 -0.0447 -0.0379 368 ASN A C 2620 O O . ASN A 338 ? 0.7850 0.7854 0.6963 -0.0457 -0.0436 -0.0399 368 ASN A O 2621 C CB . ASN A 338 ? 0.8797 0.8925 0.8070 -0.0447 -0.0489 -0.0433 368 ASN A CB 2622 C CG . ASN A 338 ? 0.8857 0.9042 0.8201 -0.0430 -0.0517 -0.0436 368 ASN A CG 2623 O OD1 . ASN A 338 ? 0.8806 0.9038 0.8139 -0.0410 -0.0569 -0.0438 368 ASN A OD1 2624 N ND2 . ASN A 338 ? 0.9519 0.9695 0.8932 -0.0433 -0.0480 -0.0435 368 ASN A ND2 2625 N N . GLY A 339 ? 0.8085 0.8075 0.7270 -0.0428 -0.0420 -0.0353 369 GLY A N 2626 C CA . GLY A 339 ? 0.7914 0.7864 0.7094 -0.0438 -0.0373 -0.0351 369 GLY A CA 2627 C C . GLY A 339 ? 0.7588 0.7539 0.6803 -0.0457 -0.0339 -0.0382 369 GLY A C 2628 O O . GLY A 339 ? 0.7877 0.7846 0.7146 -0.0451 -0.0334 -0.0389 369 GLY A O 2629 N N . ASP A 340 ? 0.7504 0.7428 0.6690 -0.0478 -0.0306 -0.0399 370 ASP A N 2630 C CA . ASP A 340 ? 0.7927 0.7842 0.7144 -0.0500 -0.0266 -0.0433 370 ASP A CA 2631 C C . ASP A 340 ? 0.7818 0.7690 0.7056 -0.0484 -0.0208 -0.0419 370 ASP A C 2632 O O . ASP A 340 ? 0.7403 0.7248 0.6656 -0.0500 -0.0159 -0.0442 370 ASP A O 2633 C CB . ASP A 340 ? 0.7897 0.7800 0.7069 -0.0532 -0.0257 -0.0468 370 ASP A CB 2634 C CG . ASP A 340 ? 0.8393 0.8241 0.7510 -0.0530 -0.0220 -0.0450 370 ASP A CG 2635 O OD1 . ASP A 340 ? 0.9746 0.9580 0.8861 -0.0504 -0.0214 -0.0411 370 ASP A OD1 2636 O OD2 . ASP A 340 ? 0.9028 0.8851 0.8109 -0.0555 -0.0196 -0.0478 370 ASP A OD2 2637 N N . VAL A 341 ? 0.8080 0.7944 0.7317 -0.0450 -0.0214 -0.0383 371 VAL A N 2638 C CA . VAL A 341 ? 0.8222 0.8054 0.7471 -0.0418 -0.0172 -0.0368 371 VAL A CA 2639 C C . VAL A 341 ? 0.8074 0.7921 0.7350 -0.0383 -0.0195 -0.0349 371 VAL A C 2640 O O . VAL A 341 ? 0.8179 0.8003 0.7450 -0.0344 -0.0175 -0.0332 371 VAL A O 2641 C CB . VAL A 341 ? 0.8415 0.8223 0.7637 -0.0402 -0.0151 -0.0351 371 VAL A CB 2642 C CG1 . VAL A 341 ? 0.8365 0.8145 0.7556 -0.0434 -0.0116 -0.0370 371 VAL A CG1 2643 C CG2 . VAL A 341 ? 0.8526 0.8361 0.7747 -0.0393 -0.0196 -0.0333 371 VAL A CG2 2644 N N . ASP A 342 ? 0.7678 0.7562 0.6976 -0.0393 -0.0236 -0.0354 372 ASP A N 2645 C CA . ASP A 342 ? 0.7912 0.7806 0.7235 -0.0364 -0.0253 -0.0340 372 ASP A CA 2646 C C . ASP A 342 ? 0.7932 0.7814 0.7292 -0.0365 -0.0213 -0.0355 372 ASP A C 2647 O O . ASP A 342 ? 0.8253 0.8151 0.7644 -0.0402 -0.0201 -0.0385 372 ASP A O 2648 C CB . ASP A 342 ? 0.7896 0.7832 0.7226 -0.0369 -0.0311 -0.0334 372 ASP A CB 2649 C CG . ASP A 342 ? 0.7801 0.7745 0.7158 -0.0341 -0.0326 -0.0322 372 ASP A CG 2650 O OD1 . ASP A 342 ? 0.7588 0.7501 0.6938 -0.0308 -0.0304 -0.0310 372 ASP A OD1 2651 O OD2 . ASP A 342 ? 0.7458 0.7437 0.6837 -0.0347 -0.0358 -0.0325 372 ASP A OD2 2652 N N . MET A 343 ? 0.7609 0.7460 0.6968 -0.0324 -0.0192 -0.0337 373 MET A N 2653 C CA . MET A 343 ? 0.7644 0.7471 0.7038 -0.0320 -0.0142 -0.0346 373 MET A CA 2654 C C . MET A 343 ? 0.7685 0.7532 0.7109 -0.0302 -0.0166 -0.0336 373 MET A C 2655 O O . MET A 343 ? 0.8014 0.7851 0.7484 -0.0306 -0.0126 -0.0347 373 MET A O 2656 C CB . MET A 343 ? 0.7602 0.7354 0.6956 -0.0279 -0.0076 -0.0330 373 MET A CB 2657 C CG . MET A 343 ? 0.7746 0.7469 0.7076 -0.0297 -0.0037 -0.0340 373 MET A CG 2658 S SD . MET A 343 ? 0.7798 0.7422 0.7074 -0.0242 0.0052 -0.0320 373 MET A SD 2659 C CE . MET A 343 ? 0.7680 0.7301 0.6899 -0.0162 0.0011 -0.0284 373 MET A CE 2660 N N . ALA A 344 ? 0.7587 0.7459 0.6990 -0.0283 -0.0224 -0.0318 374 ALA A N 2661 C CA . ALA A 344 ? 0.7929 0.7826 0.7360 -0.0270 -0.0253 -0.0310 374 ALA A CA 2662 C C . ALA A 344 ? 0.7673 0.7631 0.7168 -0.0309 -0.0274 -0.0334 374 ALA A C 2663 O O . ALA A 344 ? 0.7656 0.7625 0.7204 -0.0307 -0.0257 -0.0341 374 ALA A O 2664 C CB . ALA A 344 ? 0.8056 0.7963 0.7452 -0.0248 -0.0308 -0.0290 374 ALA A CB 2665 N N . CYS A 345 ? 0.8061 0.8058 0.7548 -0.0340 -0.0311 -0.0347 375 CYS A N 2666 C CA . CYS A 345 ? 0.8367 0.8431 0.7905 -0.0370 -0.0341 -0.0377 375 CYS A CA 2667 C C . CYS A 345 ? 0.8160 0.8236 0.7686 -0.0409 -0.0339 -0.0407 375 CYS A C 2668 O O . CYS A 345 ? 0.8410 0.8508 0.7894 -0.0416 -0.0382 -0.0407 375 CYS A O 2669 C CB . CYS A 345 ? 0.8396 0.8497 0.7917 -0.0354 -0.0405 -0.0358 375 CYS A CB 2670 S SG . CYS A 345 ? 0.8567 0.8662 0.8115 -0.0313 -0.0409 -0.0331 375 CYS A SG 2671 N N . ASN A 346 ? 0.7752 0.7804 0.7309 -0.0432 -0.0281 -0.0434 376 ASN A N 2672 C CA . ASN A 346 ? 0.7910 0.7947 0.7436 -0.0463 -0.0266 -0.0457 376 ASN A CA 2673 C C . ASN A 346 ? 0.7953 0.8058 0.7489 -0.0492 -0.0318 -0.0495 376 ASN A C 2674 O O . ASN A 346 ? 0.7745 0.7915 0.7340 -0.0496 -0.0352 -0.0516 376 ASN A O 2675 C CB . ASN A 346 ? 0.8217 0.8203 0.7774 -0.0479 -0.0184 -0.0478 376 ASN A CB 2676 C CG . ASN A 346 ? 0.8324 0.8353 0.7979 -0.0516 -0.0164 -0.0530 376 ASN A CG 2677 O OD1 . ASN A 346 ? 0.8287 0.8359 0.7964 -0.0556 -0.0185 -0.0577 376 ASN A OD1 2678 N ND2 . ASN A 346 ? 0.8124 0.8140 0.7841 -0.0503 -0.0123 -0.0526 376 ASN A ND2 2679 N N . PHE A 347 ? 0.8154 0.8242 0.7626 -0.0509 -0.0325 -0.0503 377 PHE A N 2680 C CA . PHE A 347 ? 0.7867 0.8009 0.7315 -0.0525 -0.0381 -0.0534 377 PHE A CA 2681 C C . PHE A 347 ? 0.7769 0.7977 0.7302 -0.0560 -0.0388 -0.0601 377 PHE A C 2682 O O . PHE A 347 ? 0.7614 0.7897 0.7157 -0.0557 -0.0451 -0.0628 377 PHE A O 2683 C CB . PHE A 347 ? 0.7515 0.7611 0.6874 -0.0536 -0.0371 -0.0533 377 PHE A CB 2684 C CG . PHE A 347 ? 0.7762 0.7825 0.7138 -0.0573 -0.0314 -0.0573 377 PHE A CG 2685 C CD1 . PHE A 347 ? 0.7913 0.7908 0.7289 -0.0569 -0.0245 -0.0551 377 PHE A CD1 2686 C CD2 . PHE A 347 ? 0.7994 0.8096 0.7385 -0.0609 -0.0329 -0.0636 377 PHE A CD2 2687 C CE1 . PHE A 347 ? 0.8061 0.8015 0.7448 -0.0600 -0.0183 -0.0585 377 PHE A CE1 2688 C CE2 . PHE A 347 ? 0.7997 0.8062 0.7407 -0.0647 -0.0271 -0.0677 377 PHE A CE2 2689 C CZ . PHE A 347 ? 0.8073 0.8058 0.7479 -0.0643 -0.0193 -0.0649 377 PHE A CZ 2690 N N . MET A 348 ? 0.7799 0.7979 0.7394 -0.0589 -0.0321 -0.0630 378 MET A N 2691 C CA . MET A 348 ? 0.8319 0.8561 0.8010 -0.0632 -0.0318 -0.0705 378 MET A CA 2692 C C . MET A 348 ? 0.8024 0.8349 0.7817 -0.0623 -0.0351 -0.0720 378 MET A C 2693 O O . MET A 348 ? 0.8569 0.8987 0.8421 -0.0641 -0.0402 -0.0777 378 MET A O 2694 C CB . MET A 348 ? 0.8338 0.8518 0.8079 -0.0668 -0.0224 -0.0734 378 MET A CB 2695 C CG . MET A 348 ? 0.8441 0.8684 0.8291 -0.0722 -0.0217 -0.0823 378 MET A CG 2696 S SD . MET A 348 ? 0.8788 0.8937 0.8660 -0.0771 -0.0104 -0.0863 378 MET A SD 2697 C CE . MET A 348 ? 0.8818 0.8932 0.8547 -0.0775 -0.0137 -0.0863 378 MET A CE 2698 N N . GLY A 349 ? 0.8187 0.8481 0.8000 -0.0592 -0.0324 -0.0671 379 GLY A N 2699 C CA . GLY A 349 ? 0.7788 0.8151 0.7694 -0.0577 -0.0347 -0.0675 379 GLY A CA 2700 C C . GLY A 349 ? 0.7578 0.8033 0.7464 -0.0558 -0.0445 -0.0684 379 GLY A C 2701 O O . GLY A 349 ? 0.7147 0.7701 0.7129 -0.0568 -0.0482 -0.0734 379 GLY A O 2702 N N . ASP A 350 ? 0.7771 0.8192 0.7534 -0.0526 -0.0485 -0.0636 380 ASP A N 2703 C CA . ASP A 350 ? 0.8140 0.8626 0.7857 -0.0496 -0.0571 -0.0634 380 ASP A CA 2704 C C . ASP A 350 ? 0.8441 0.8986 0.8140 -0.0518 -0.0617 -0.0696 380 ASP A C 2705 O O . ASP A 350 ? 0.8849 0.9484 0.8563 -0.0497 -0.0687 -0.0723 380 ASP A O 2706 C CB . ASP A 350 ? 0.8125 0.8544 0.7719 -0.0457 -0.0585 -0.0563 380 ASP A CB 2707 C CG . ASP A 350 ? 0.8046 0.8438 0.7660 -0.0425 -0.0570 -0.0512 380 ASP A CG 2708 O OD1 . ASP A 350 ? 0.7922 0.8377 0.7610 -0.0409 -0.0594 -0.0521 380 ASP A OD1 2709 O OD2 . ASP A 350 ? 0.8514 0.8826 0.8073 -0.0415 -0.0537 -0.0468 380 ASP A OD2 2710 N N . GLU A 351 ? 0.8486 0.8982 0.8153 -0.0556 -0.0578 -0.0722 381 GLU A N 2711 C CA . GLU A 351 ? 0.8896 0.9448 0.8555 -0.0581 -0.0617 -0.0794 381 GLU A CA 2712 C C . GLU A 351 ? 0.9152 0.9815 0.8968 -0.0611 -0.0634 -0.0875 381 GLU A C 2713 O O . GLU A 351 ? 0.9079 0.9841 0.8906 -0.0604 -0.0710 -0.0929 381 GLU A O 2714 C CB . GLU A 351 ? 0.9317 0.9788 0.8921 -0.0619 -0.0562 -0.0810 381 GLU A CB 2715 C CG . GLU A 351 ? 1.0013 1.0525 0.9572 -0.0638 -0.0608 -0.0879 381 GLU A CG 2716 C CD . GLU A 351 ? 1.0550 1.0964 1.0001 -0.0657 -0.0563 -0.0872 381 GLU A CD 2717 O OE1 . GLU A 351 ? 0.9795 1.0122 0.9249 -0.0671 -0.0483 -0.0836 381 GLU A OE1 2718 O OE2 . GLU A 351 ? 1.1304 1.1729 1.0663 -0.0652 -0.0608 -0.0903 381 GLU A OE2 2719 N N . TRP A 352 ? 0.8896 0.9543 0.8833 -0.0642 -0.0560 -0.0885 382 TRP A N 2720 C CA . TRP A 352 ? 0.8259 0.9010 0.8371 -0.0673 -0.0561 -0.0959 382 TRP A CA 2721 C C . TRP A 352 ? 0.8042 0.8897 0.8201 -0.0627 -0.0637 -0.0950 382 TRP A C 2722 O O . TRP A 352 ? 0.8265 0.9246 0.8526 -0.0637 -0.0691 -0.1022 382 TRP A O 2723 C CB . TRP A 352 ? 0.8306 0.8997 0.8522 -0.0700 -0.0455 -0.0951 382 TRP A CB 2724 C CG . TRP A 352 ? 0.8227 0.8828 0.8443 -0.0750 -0.0365 -0.0976 382 TRP A CG 2725 C CD1 . TRP A 352 ? 0.8307 0.8887 0.8460 -0.0780 -0.0370 -0.1017 382 TRP A CD1 2726 C CD2 . TRP A 352 ? 0.8212 0.8725 0.8491 -0.0769 -0.0251 -0.0963 382 TRP A CD2 2727 N NE1 . TRP A 352 ? 0.8548 0.9032 0.8725 -0.0820 -0.0264 -0.1029 382 TRP A NE1 2728 C CE2 . TRP A 352 ? 0.8468 0.8908 0.8720 -0.0811 -0.0188 -0.0995 382 TRP A CE2 2729 C CE3 . TRP A 352 ? 0.8150 0.8633 0.8498 -0.0750 -0.0191 -0.0926 382 TRP A CE3 2730 C CZ2 . TRP A 352 ? 0.8244 0.8578 0.8533 -0.0832 -0.0066 -0.0989 382 TRP A CZ2 2731 C CZ3 . TRP A 352 ? 0.8474 0.8849 0.8851 -0.0768 -0.0070 -0.0919 382 TRP A CZ3 2732 C CH2 . TRP A 352 ? 0.8398 0.8698 0.8744 -0.0808 -0.0008 -0.0949 382 TRP A CH2 2733 N N . PHE A 353 ? 0.7908 0.8713 0.7998 -0.0577 -0.0638 -0.0864 383 PHE A N 2734 C CA . PHE A 353 ? 0.8115 0.9001 0.8240 -0.0528 -0.0700 -0.0846 383 PHE A CA 2735 C C . PHE A 353 ? 0.8654 0.9625 0.8709 -0.0493 -0.0804 -0.0870 383 PHE A C 2736 O O . PHE A 353 ? 0.8967 1.0065 0.9114 -0.0475 -0.0865 -0.0915 383 PHE A O 2737 C CB . PHE A 353 ? 0.7811 0.8611 0.7853 -0.0482 -0.0680 -0.0750 383 PHE A CB 2738 C CG . PHE A 353 ? 0.7711 0.8578 0.7762 -0.0426 -0.0743 -0.0724 383 PHE A CG 2739 C CD1 . PHE A 353 ? 0.7764 0.8692 0.7953 -0.0420 -0.0728 -0.0734 383 PHE A CD1 2740 C CD2 . PHE A 353 ? 0.7769 0.8630 0.7687 -0.0376 -0.0807 -0.0686 383 PHE A CD2 2741 C CE1 . PHE A 353 ? 0.7844 0.8832 0.8042 -0.0364 -0.0782 -0.0708 383 PHE A CE1 2742 C CE2 . PHE A 353 ? 0.7959 0.8873 0.7879 -0.0318 -0.0859 -0.0657 383 PHE A CE2 2743 C CZ . PHE A 353 ? 0.7790 0.8771 0.7851 -0.0312 -0.0849 -0.0669 383 PHE A CZ 2744 N N . VAL A 354 ? 0.8816 0.9717 0.8708 -0.0479 -0.0822 -0.0841 384 VAL A N 2745 C CA . VAL A 354 ? 0.8956 0.9915 0.8751 -0.0437 -0.0913 -0.0860 384 VAL A CA 2746 C C . VAL A 354 ? 0.8951 1.0026 0.8832 -0.0472 -0.0957 -0.0970 384 VAL A C 2747 O O . VAL A 354 ? 0.9314 1.0514 0.9239 -0.0438 -0.1039 -0.1013 384 VAL A O 2748 C CB . VAL A 354 ? 0.9324 1.0169 0.8925 -0.0417 -0.0907 -0.0807 384 VAL A CB 2749 C CG1 . VAL A 354 ? 0.9592 1.0486 0.9080 -0.0372 -0.0993 -0.0833 384 VAL A CG1 2750 C CG2 . VAL A 354 ? 0.9455 1.0203 0.8981 -0.0380 -0.0875 -0.0708 384 VAL A CG2 2751 N N . ASP A 355 ? 0.8832 0.9868 0.8743 -0.0537 -0.0903 -0.1019 385 ASP A N 2752 C CA . ASP A 355 ? 0.8993 1.0129 0.8995 -0.0583 -0.0935 -0.1135 385 ASP A CA 2753 C C . ASP A 355 ? 0.8916 1.0203 0.9120 -0.0591 -0.0968 -0.1202 385 ASP A C 2754 O O . ASP A 355 ? 0.9027 1.0448 0.9282 -0.0585 -0.1052 -0.1287 385 ASP A O 2755 C CB . ASP A 355 ? 0.9119 1.0175 0.9153 -0.0659 -0.0846 -0.1173 385 ASP A CB 2756 C CG . ASP A 355 ? 0.9753 1.0691 0.9598 -0.0654 -0.0831 -0.1138 385 ASP A CG 2757 O OD1 . ASP A 355 ? 1.0579 1.1499 1.0269 -0.0596 -0.0890 -0.1093 385 ASP A OD1 2758 O OD2 . ASP A 355 ? 1.1043 1.1897 1.0892 -0.0707 -0.0752 -0.1151 385 ASP A OD2 2759 N N . SER A 356 ? 0.8917 1.0189 0.9235 -0.0599 -0.0905 -0.1164 386 SER A N 2760 C CA . SER A 356 ? 0.8723 1.0132 0.9249 -0.0609 -0.0920 -0.1222 386 SER A CA 2761 C C . SER A 356 ? 0.8741 1.0251 0.9255 -0.0528 -0.1015 -0.1194 386 SER A C 2762 O O . SER A 356 ? 0.8531 1.0161 0.9216 -0.0526 -0.1033 -0.1235 386 SER A O 2763 C CB . SER A 356 ? 0.8426 0.9767 0.9075 -0.0647 -0.0804 -0.1194 386 SER A CB 2764 O OG . SER A 356 ? 0.8123 0.9373 0.8682 -0.0596 -0.0780 -0.1084 386 SER A OG 2765 N N . LEU A 357 ? 0.8904 1.0363 0.9221 -0.0461 -0.1069 -0.1125 387 LEU A N 2766 C CA . LEU A 357 ? 0.9072 1.0630 0.9358 -0.0378 -0.1167 -0.1110 387 LEU A CA 2767 C C . LEU A 357 ? 0.9311 1.1026 0.9626 -0.0362 -0.1275 -0.1214 387 LEU A C 2768 O O . LEU A 357 ? 0.9508 1.1339 0.9843 -0.0294 -0.1359 -0.1222 387 LEU A O 2769 C CB . LEU A 357 ? 0.8790 1.0231 0.8852 -0.0308 -0.1181 -0.1003 387 LEU A CB 2770 C CG . LEU A 357 ? 0.8305 0.9627 0.8341 -0.0297 -0.1107 -0.0902 387 LEU A CG 2771 C CD1 . LEU A 357 ? 0.8636 0.9850 0.8460 -0.0234 -0.1122 -0.0812 387 LEU A CD1 2772 C CD2 . LEU A 357 ? 0.8490 0.9897 0.8671 -0.0272 -0.1112 -0.0896 387 LEU A CD2 2773 N N . ASN A 358 ? 0.9480 1.1199 0.9793 -0.0419 -0.1274 -0.1293 388 ASN A N 2774 C CA . ASN A 358 ? 1.0004 1.1864 1.0325 -0.0406 -0.1380 -0.1401 388 ASN A CA 2775 C C . ASN A 358 ? 1.0343 1.2227 1.0475 -0.0296 -0.1485 -0.1360 388 ASN A C 2776 O O . ASN A 358 ? 1.1263 1.3290 1.1462 -0.0236 -0.1568 -0.1385 388 ASN A O 2777 C CB . ASN A 358 ? 0.9990 1.2044 1.0575 -0.0438 -0.1415 -0.1513 388 ASN A CB 2778 C CG . ASN A 358 ? 1.0096 1.2139 1.0872 -0.0550 -0.1317 -0.1584 388 ASN A CG 2779 O OD1 . ASN A 358 ? 0.9731 1.1631 1.0433 -0.0604 -0.1233 -0.1563 388 ASN A OD1 2780 N ND2 . ASN A 358 ? 1.0143 1.2336 1.1171 -0.0584 -0.1321 -0.1669 388 ASN A ND2 2781 N N . GLN A 359 ? 1.0182 1.1923 1.0079 -0.0266 -0.1474 -0.1293 389 GLN A N 2782 C CA . GLN A 359 ? 1.0243 1.1982 0.9937 -0.0162 -0.1560 -0.1254 389 GLN A CA 2783 C C . GLN A 359 ? 1.0819 1.2564 1.0398 -0.0168 -0.1609 -0.1330 389 GLN A C 2784 O O . GLN A 359 ? 1.0385 1.2106 1.0029 -0.0256 -0.1560 -0.1391 389 GLN A O 2785 C CB . GLN A 359 ? 1.0215 1.1772 0.9725 -0.0119 -0.1499 -0.1115 389 GLN A CB 2786 C CG . GLN A 359 ? 1.0029 1.1568 0.9640 -0.0112 -0.1449 -0.1041 389 GLN A CG 2787 C CD . GLN A 359 ? 0.9753 1.1438 0.9439 -0.0037 -0.1531 -0.1054 389 GLN A CD 2788 O OE1 . GLN A 359 ? 1.0502 1.2195 1.0036 0.0058 -0.1600 -0.1022 389 GLN A OE1 2789 N NE2 . GLN A 359 ? 0.9228 1.1026 0.9146 -0.0076 -0.1520 -0.1100 389 GLN A NE2 2790 N N . LYS A 360 ? 1.1660 1.3433 1.1063 -0.0070 -0.1703 -0.1326 390 LYS A N 2791 C CA . LYS A 360 ? 1.2746 1.4516 1.2007 -0.0061 -0.1757 -0.1395 390 LYS A CA 2792 C C . LYS A 360 ? 1.2882 1.4441 1.1958 -0.0087 -0.1665 -0.1321 390 LYS A C 2793 O O . LYS A 360 ? 1.3189 1.4616 1.2084 -0.0024 -0.1636 -0.1209 390 LYS A O 2794 C CB . LYS A 360 ? 1.3673 1.5520 1.2774 0.0065 -0.1881 -0.1405 390 LYS A CB 2795 C CG . LYS A 360 ? 1.4690 1.6567 1.3662 0.0079 -0.1955 -0.1501 390 LYS A CG 2796 C CD . LYS A 360 ? 1.5509 1.7529 1.4394 0.0202 -0.2100 -0.1548 390 LYS A CD 2797 C CE . LYS A 360 ? 1.5367 1.7488 1.4216 0.0198 -0.2193 -0.1689 390 LYS A CE 2798 N NZ . LYS A 360 ? 1.5422 1.7729 1.4248 0.0312 -0.2347 -0.1757 390 LYS A NZ 2799 N N . MET A 361 ? 1.2773 1.4303 1.1904 -0.0180 -0.1617 -0.1386 391 MET A N 2800 C CA . MET A 361 ? 1.3112 1.4457 1.2084 -0.0209 -0.1533 -0.1331 391 MET A CA 2801 C C . MET A 361 ? 1.2968 1.4243 1.1668 -0.0117 -0.1585 -0.1302 391 MET A C 2802 O O . MET A 361 ? 1.3394 1.4771 1.2039 -0.0070 -0.1687 -0.1384 391 MET A O 2803 C CB . MET A 361 ? 1.4020 1.5365 1.3094 -0.0314 -0.1487 -0.1424 391 MET A CB 2804 C CG . MET A 361 ? 1.5503 1.6676 1.4395 -0.0334 -0.1420 -0.1389 391 MET A CG 2805 S SD . MET A 361 ? 1.7688 1.8809 1.6733 -0.0466 -0.1310 -0.1445 391 MET A SD 2806 C CE . MET A 361 ? 1.6511 1.7514 1.5613 -0.0486 -0.1193 -0.1313 391 MET A CE 2807 N N . GLU A 362 ? 1.2559 1.3660 1.1092 -0.0088 -0.1513 -0.1187 392 GLU A N 2808 C CA . GLU A 362 ? 1.2818 1.3815 1.1082 -0.0009 -0.1533 -0.1148 392 GLU A CA 2809 C C . GLU A 362 ? 1.3247 1.4101 1.1424 -0.0070 -0.1448 -0.1145 392 GLU A C 2810 O O . GLU A 362 ? 1.4355 1.5238 1.2499 -0.0095 -0.1480 -0.1237 392 GLU A O 2811 C CB . GLU A 362 ? 1.2570 1.3472 1.0701 0.0079 -0.1512 -0.1022 392 GLU A CB 2812 C CG . GLU A 362 ? 1.2770 1.3803 1.0925 0.0167 -0.1611 -0.1029 392 GLU A CG 2813 C CD . GLU A 362 ? 1.3147 1.4069 1.1092 0.0280 -0.1604 -0.0918 392 GLU A CD 2814 O OE1 . GLU A 362 ? 1.3393 1.4137 1.1212 0.0276 -0.1510 -0.0830 392 GLU A OE1 2815 O OE2 . GLU A 362 ? 1.3173 1.4185 1.1085 0.0374 -0.1688 -0.0918 392 GLU A OE2 2816 N N . VAL A 363 ? 1.2965 1.3673 1.1113 -0.0094 -0.1342 -0.1044 393 VAL A N 2817 C CA . VAL A 363 ? 1.2914 1.3491 1.0998 -0.0152 -0.1254 -0.1035 393 VAL A CA 2818 C C . VAL A 363 ? 1.2389 1.3004 1.0690 -0.0263 -0.1198 -0.1086 393 VAL A C 2819 O O . VAL A 363 ? 1.1955 1.2601 1.0415 -0.0294 -0.1165 -0.1054 393 VAL A O 2820 C CB . VAL A 363 ? 1.3243 1.3648 1.1203 -0.0127 -0.1163 -0.0910 393 VAL A CB 2821 C CG1 . VAL A 363 ? 1.3563 1.3843 1.1457 -0.0180 -0.1077 -0.0907 393 VAL A CG1 2822 C CG2 . VAL A 363 ? 1.3347 1.3695 1.1094 -0.0014 -0.1200 -0.0849 393 VAL A CG2 2823 N N . GLN A 364 ? 1.2564 1.3163 1.0857 -0.0318 -0.1182 -0.1162 394 GLN A N 2824 C CA . GLN A 364 ? 1.2105 1.2710 1.0575 -0.0420 -0.1112 -0.1207 394 GLN A CA 2825 C C . GLN A 364 ? 1.1669 1.2139 1.0141 -0.0446 -0.0998 -0.1105 394 GLN A C 2826 O O . GLN A 364 ? 1.2004 1.2368 1.0330 -0.0398 -0.0970 -0.1018 394 GLN A O 2827 C CB . GLN A 364 ? 1.2644 1.3241 1.1073 -0.0464 -0.1115 -0.1308 394 GLN A CB 2828 C CG . GLN A 364 ? 1.3867 1.4615 1.2321 -0.0450 -0.1231 -0.1432 394 GLN A CG 2829 C CD . GLN A 364 ? 1.4756 1.5491 1.2970 -0.0351 -0.1317 -0.1432 394 GLN A CD 2830 O OE1 . GLN A 364 ? 1.5114 1.5838 1.3226 -0.0264 -0.1352 -0.1353 394 GLN A OE1 2831 N NE2 . GLN A 364 ? 1.4805 1.5535 1.2923 -0.0360 -0.1348 -0.1521 394 GLN A NE2 2832 N N . ARG A 365 ? 1.1170 1.1642 0.9809 -0.0521 -0.0931 -0.1120 395 ARG A N 2833 C CA . ARG A 365 ? 1.0448 1.0811 0.9105 -0.0540 -0.0832 -0.1030 395 ARG A CA 2834 C C . ARG A 365 ? 1.0259 1.0486 0.8775 -0.0547 -0.0766 -0.1000 395 ARG A C 2835 O O . ARG A 365 ? 1.0405 1.0613 0.8909 -0.0589 -0.0746 -0.1067 395 ARG A O 2836 C CB . ARG A 365 ? 1.0140 1.0532 0.8993 -0.0609 -0.0774 -0.1057 395 ARG A CB 2837 C CG . ARG A 365 ? 0.9908 1.0221 0.8800 -0.0614 -0.0694 -0.0965 395 ARG A CG 2838 C CD . ARG A 365 ? 0.9990 1.0317 0.9051 -0.0675 -0.0630 -0.0997 395 ARG A CD 2839 N NE . ARG A 365 ? 0.9309 0.9598 0.8429 -0.0665 -0.0580 -0.0919 395 ARG A NE 2840 C CZ . ARG A 365 ? 0.9001 0.9190 0.8090 -0.0670 -0.0504 -0.0861 395 ARG A CZ 2841 N NH1 . ARG A 365 ? 0.9370 0.9478 0.8372 -0.0685 -0.0460 -0.0864 395 ARG A NH1 2842 N NH2 . ARG A 365 ? 0.8561 0.8732 0.7705 -0.0655 -0.0473 -0.0800 395 ARG A NH2 2843 N N . ARG A 366 ? 1.0296 1.0428 0.8716 -0.0508 -0.0727 -0.0904 396 ARG A N 2844 C CA . ARG A 366 ? 1.0768 1.0771 0.9063 -0.0510 -0.0659 -0.0869 396 ARG A CA 2845 C C . ARG A 366 ? 1.0165 1.0089 0.8476 -0.0503 -0.0586 -0.0771 396 ARG A C 2846 O O . ARG A 366 ? 1.0401 1.0364 0.8797 -0.0491 -0.0596 -0.0730 396 ARG A O 2847 C CB . ARG A 366 ? 1.1793 1.1754 0.9885 -0.0450 -0.0702 -0.0868 396 ARG A CB 2848 C CG . ARG A 366 ? 1.2520 1.2503 1.0545 -0.0375 -0.0758 -0.0814 396 ARG A CG 2849 C CD . ARG A 366 ? 1.3274 1.3149 1.1082 -0.0308 -0.0749 -0.0764 396 ARG A CD 2850 N NE . ARG A 366 ? 1.4159 1.4041 1.1920 -0.0239 -0.0783 -0.0701 396 ARG A NE 2851 C CZ . ARG A 366 ? 1.4655 1.4461 1.2414 -0.0222 -0.0725 -0.0610 396 ARG A CZ 2852 N NH1 . ARG A 366 ? 1.4484 1.4210 1.2288 -0.0265 -0.0634 -0.0570 396 ARG A NH1 2853 N NH2 . ARG A 366 ? 1.5060 1.4873 1.2775 -0.0158 -0.0757 -0.0562 396 ARG A NH2 2854 N N . PRO A 367 ? 0.9799 0.9614 0.8030 -0.0510 -0.0514 -0.0738 397 PRO A N 2855 C CA . PRO A 367 ? 0.9315 0.9053 0.7540 -0.0495 -0.0450 -0.0651 397 PRO A CA 2856 C C . PRO A 367 ? 0.9276 0.8991 0.7410 -0.0434 -0.0477 -0.0592 397 PRO A C 2857 O O . PRO A 367 ? 0.9750 0.9484 0.7781 -0.0393 -0.0538 -0.0612 397 PRO A O 2858 C CB . PRO A 367 ? 0.9480 0.9116 0.7612 -0.0507 -0.0382 -0.0648 397 PRO A CB 2859 C CG . PRO A 367 ? 0.9714 0.9376 0.7876 -0.0553 -0.0385 -0.0732 397 PRO A CG 2860 C CD . PRO A 367 ? 0.9985 0.9757 0.8183 -0.0550 -0.0476 -0.0795 397 PRO A CD 2861 N N . TRP A 368 ? 0.9369 0.9043 0.7540 -0.0425 -0.0431 -0.0522 398 TRP A N 2862 C CA . TRP A 368 ? 0.9686 0.9295 0.7754 -0.0373 -0.0423 -0.0459 398 TRP A CA 2863 C C . TRP A 368 ? 0.9755 0.9282 0.7845 -0.0385 -0.0336 -0.0404 398 TRP A C 2864 O O . TRP A 368 ? 0.9887 0.9437 0.8106 -0.0422 -0.0304 -0.0401 398 TRP A O 2865 C CB . TRP A 368 ? 0.9385 0.9055 0.7492 -0.0339 -0.0479 -0.0437 398 TRP A CB 2866 C CG . TRP A 368 ? 0.9415 0.9130 0.7679 -0.0365 -0.0467 -0.0416 398 TRP A CG 2867 C CD1 . TRP A 368 ? 0.9702 0.9503 0.8102 -0.0400 -0.0491 -0.0455 398 TRP A CD1 2868 C CD2 . TRP A 368 ? 0.9445 0.9119 0.7746 -0.0354 -0.0429 -0.0355 398 TRP A CD2 2869 N NE1 . TRP A 368 ? 0.9348 0.9160 0.7852 -0.0406 -0.0471 -0.0417 398 TRP A NE1 2870 C CE2 . TRP A 368 ? 0.9190 0.8930 0.7640 -0.0380 -0.0437 -0.0360 398 TRP A CE2 2871 C CE3 . TRP A 368 ? 0.9814 0.9398 0.8040 -0.0325 -0.0382 -0.0299 398 TRP A CE3 2872 C CZ2 . TRP A 368 ? 0.9300 0.9025 0.7819 -0.0377 -0.0410 -0.0316 398 TRP A CZ2 2873 C CZ3 . TRP A 368 ? 0.9925 0.9497 0.8236 -0.0330 -0.0351 -0.0259 398 TRP A CZ3 2874 C CH2 . TRP A 368 ? 0.9549 0.9194 0.8003 -0.0355 -0.0370 -0.0270 398 TRP A CH2 2875 N N . LEU A 369 ? 0.9818 0.9248 0.7782 -0.0350 -0.0296 -0.0363 399 LEU A N 2876 C CA . LEU A 369 ? 1.0042 0.9392 0.8022 -0.0365 -0.0206 -0.0323 399 LEU A CA 2877 C C . LEU A 369 ? 1.0280 0.9590 0.8291 -0.0346 -0.0169 -0.0262 399 LEU A C 2878 O O . LEU A 369 ? 1.0472 0.9786 0.8444 -0.0308 -0.0204 -0.0239 399 LEU A O 2879 C CB . LEU A 369 ? 1.0412 0.9664 0.8236 -0.0350 -0.0162 -0.0327 399 LEU A CB 2880 C CG . LEU A 369 ? 1.0447 0.9721 0.8212 -0.0366 -0.0196 -0.0394 399 LEU A CG 2881 C CD1 . LEU A 369 ? 1.0536 0.9698 0.8127 -0.0343 -0.0149 -0.0391 399 LEU A CD1 2882 C CD2 . LEU A 369 ? 1.0269 0.9596 0.8180 -0.0425 -0.0178 -0.0428 399 LEU A CD2 2883 N N . VAL A 370 ? 1.0252 0.9527 0.8339 -0.0371 -0.0097 -0.0239 400 VAL A N 2884 C CA . VAL A 370 ? 1.0226 0.9457 0.8356 -0.0361 -0.0047 -0.0190 400 VAL A CA 2885 C C . VAL A 370 ? 1.0213 0.9362 0.8333 -0.0373 0.0045 -0.0172 400 VAL A C 2886 O O . VAL A 370 ? 1.0505 0.9669 0.8664 -0.0401 0.0067 -0.0197 400 VAL A O 2887 C CB . VAL A 370 ? 1.0009 0.9324 0.8313 -0.0386 -0.0069 -0.0191 400 VAL A CB 2888 C CG1 . VAL A 370 ? 1.0012 0.9285 0.8384 -0.0387 -0.0009 -0.0154 400 VAL A CG1 2889 C CG2 . VAL A 370 ? 0.9745 0.9127 0.8055 -0.0368 -0.0150 -0.0201 400 VAL A CG2 2890 N N . LYS A 371 ? 1.0453 0.9512 0.8521 -0.0350 0.0106 -0.0130 401 LYS A N 2891 C CA . LYS A 371 ? 1.1550 1.0528 0.9621 -0.0361 0.0205 -0.0111 401 LYS A CA 2892 C C . LYS A 371 ? 1.1581 1.0606 0.9847 -0.0394 0.0240 -0.0105 401 LYS A C 2893 O O . LYS A 371 ? 1.2433 1.1476 1.0763 -0.0391 0.0228 -0.0090 401 LYS A O 2894 C CB . LYS A 371 ? 1.2592 1.1436 1.0505 -0.0317 0.0266 -0.0068 401 LYS A CB 2895 C CG . LYS A 371 ? 1.3604 1.2348 1.1482 -0.0322 0.0373 -0.0051 401 LYS A CG 2896 C CD . LYS A 371 ? 1.4499 1.3094 1.2180 -0.0268 0.0433 -0.0009 401 LYS A CD 2897 C CE . LYS A 371 ? 1.4648 1.3135 1.2276 -0.0270 0.0543 0.0005 401 LYS A CE 2898 N NZ . LYS A 371 ? 1.4899 1.3240 1.2277 -0.0207 0.0582 0.0035 401 LYS A NZ 2899 N N . TYR A 372 ? 1.1520 1.0568 0.9879 -0.0423 0.0281 -0.0121 402 TYR A N 2900 C CA . TYR A 372 ? 1.1464 1.0565 1.0010 -0.0450 0.0313 -0.0123 402 TYR A CA 2901 C C . TYR A 372 ? 1.2525 1.1554 1.1097 -0.0457 0.0419 -0.0106 402 TYR A C 2902 O O . TYR A 372 ? 1.3675 1.2620 1.2126 -0.0446 0.0468 -0.0097 402 TYR A O 2903 C CB . TYR A 372 ? 1.1154 1.0363 0.9813 -0.0471 0.0267 -0.0157 402 TYR A CB 2904 C CG . TYR A 372 ? 1.0661 0.9947 0.9333 -0.0468 0.0174 -0.0174 402 TYR A CG 2905 C CD1 . TYR A 372 ? 1.0311 0.9653 0.9086 -0.0469 0.0140 -0.0172 402 TYR A CD1 2906 C CD2 . TYR A 372 ? 1.0382 0.9685 0.8972 -0.0465 0.0124 -0.0196 402 TYR A CD2 2907 C CE1 . TYR A 372 ? 0.9890 0.9296 0.8676 -0.0464 0.0063 -0.0185 402 TYR A CE1 2908 C CE2 . TYR A 372 ? 1.0301 0.9674 0.8916 -0.0463 0.0048 -0.0213 402 TYR A CE2 2909 C CZ . TYR A 372 ? 1.0332 0.9755 0.9043 -0.0461 0.0019 -0.0204 402 TYR A CZ 2910 O OH . TYR A 372 ? 1.0384 0.9871 0.9117 -0.0458 -0.0050 -0.0219 402 TYR A OH 2911 N N . GLY A 373 ? 1.3829 1.2891 1.2563 -0.0477 0.0456 -0.0106 403 GLY A N 2912 C CA . GLY A 373 ? 1.4829 1.3844 1.3635 -0.0490 0.0560 -0.0098 403 GLY A CA 2913 C C . GLY A 373 ? 1.5442 1.4499 1.4300 -0.0500 0.0577 -0.0119 403 GLY A C 2914 O O . GLY A 373 ? 1.5600 1.4768 1.4581 -0.0511 0.0527 -0.0147 403 GLY A O 2915 N N . ASP A 374 ? 1.6199 1.5159 1.4948 -0.0491 0.0650 -0.0103 404 ASP A N 2916 C CA . ASP A 374 ? 1.6850 1.5823 1.5618 -0.0496 0.0680 -0.0117 404 ASP A CA 2917 C C . ASP A 374 ? 1.6157 1.5150 1.4815 -0.0488 0.0610 -0.0136 404 ASP A C 2918 O O . ASP A 374 ? 1.6161 1.5084 1.4702 -0.0481 0.0646 -0.0135 404 ASP A O 2919 C CB . ASP A 374 ? 1.7275 1.6360 1.6271 -0.0514 0.0692 -0.0140 404 ASP A CB 2920 C CG . ASP A 374 ? 1.7846 1.6919 1.6869 -0.0513 0.0759 -0.0144 404 ASP A CG 2921 O OD1 . ASP A 374 ? 1.7641 1.6782 1.6694 -0.0509 0.0719 -0.0164 404 ASP A OD1 2922 O OD2 . ASP A 374 ? 1.7881 1.6870 1.6892 -0.0514 0.0858 -0.0125 404 ASP A OD2 2923 N N . SER A 375 ? 1.4700 1.3783 1.3397 -0.0491 0.0516 -0.0155 405 SER A N 2924 C CA . SER A 375 ? 1.3851 1.2961 1.2471 -0.0490 0.0453 -0.0178 405 SER A CA 2925 C C . SER A 375 ? 1.3677 1.2701 1.2093 -0.0475 0.0439 -0.0177 405 SER A C 2926 O O . SER A 375 ? 1.3772 1.2799 1.2119 -0.0479 0.0409 -0.0204 405 SER A O 2927 C CB . SER A 375 ? 1.3514 1.2727 1.2218 -0.0494 0.0364 -0.0196 405 SER A CB 2928 O OG . SER A 375 ? 1.3397 1.2696 1.2265 -0.0500 0.0364 -0.0207 405 SER A OG 2929 N N . GLY A 376 ? 1.3373 1.2317 1.1688 -0.0456 0.0460 -0.0150 406 GLY A N 2930 C CA . GLY A 376 ? 1.2984 1.1854 1.1095 -0.0430 0.0435 -0.0151 406 GLY A CA 2931 C C . GLY A 376 ? 1.2843 1.1790 1.0940 -0.0426 0.0328 -0.0172 406 GLY A C 2932 O O . GLY A 376 ? 1.2599 1.1630 1.0826 -0.0437 0.0286 -0.0173 406 GLY A O 2933 N N . GLU A 377 ? 1.2145 1.1065 1.0088 -0.0408 0.0283 -0.0194 407 GLU A N 2934 C CA . GLU A 377 ? 1.1713 1.0714 0.9652 -0.0405 0.0183 -0.0221 407 GLU A CA 2935 C C . GLU A 377 ? 1.1300 1.0398 0.9363 -0.0443 0.0145 -0.0263 407 GLU A C 2936 O O . GLU A 377 ? 1.1256 1.0340 0.9325 -0.0463 0.0181 -0.0285 407 GLU A O 2937 C CB . GLU A 377 ? 1.2172 1.1126 0.9917 -0.0371 0.0141 -0.0239 407 GLU A CB 2938 C CG . GLU A 377 ? 1.2779 1.1648 1.0396 -0.0319 0.0158 -0.0194 407 GLU A CG 2939 C CD . GLU A 377 ? 1.3113 1.1995 1.0585 -0.0275 0.0072 -0.0213 407 GLU A CD 2940 O OE1 . GLU A 377 ? 1.3508 1.2376 1.0860 -0.0266 0.0043 -0.0254 407 GLU A OE1 2941 O OE2 . GLU A 377 ? 1.3228 1.2133 1.0705 -0.0247 0.0034 -0.0189 407 GLU A OE2 2942 N N . GLN A 378 ? 1.0339 0.9527 0.8497 -0.0449 0.0081 -0.0271 408 GLN A N 2943 C CA . GLN A 378 ? 1.0057 0.9328 0.8319 -0.0477 0.0047 -0.0307 408 GLN A CA 2944 C C . GLN A 378 ? 0.9867 0.9205 0.8122 -0.0474 -0.0038 -0.0335 408 GLN A C 2945 O O . GLN A 378 ? 1.0243 0.9579 0.8436 -0.0446 -0.0077 -0.0320 408 GLN A O 2946 C CB . GLN A 378 ? 0.9958 0.9281 0.8382 -0.0488 0.0064 -0.0288 408 GLN A CB 2947 C CG . GLN A 378 ? 1.0029 0.9314 0.8501 -0.0494 0.0144 -0.0269 408 GLN A CG 2948 C CD . GLN A 378 ? 1.0035 0.9301 0.8492 -0.0509 0.0180 -0.0295 408 GLN A CD 2949 O OE1 . GLN A 378 ? 0.9784 0.9079 0.8236 -0.0522 0.0148 -0.0330 408 GLN A OE1 2950 N NE2 . GLN A 378 ? 1.0010 0.9223 0.8467 -0.0508 0.0255 -0.0279 408 GLN A NE2 2951 N N . ILE A 379 ? 0.9429 0.8825 0.7753 -0.0500 -0.0061 -0.0375 409 ILE A N 2952 C CA . ILE A 379 ? 0.9215 0.8686 0.7569 -0.0503 -0.0134 -0.0406 409 ILE A CA 2953 C C . ILE A 379 ? 0.8925 0.8455 0.7400 -0.0499 -0.0154 -0.0380 409 ILE A C 2954 O O . ILE A 379 ? 0.8207 0.7756 0.6783 -0.0512 -0.0125 -0.0373 409 ILE A O 2955 C CB . ILE A 379 ? 0.9374 0.8871 0.7755 -0.0536 -0.0137 -0.0463 409 ILE A CB 2956 C CG1 . ILE A 379 ? 0.9922 0.9367 0.8167 -0.0537 -0.0135 -0.0500 409 ILE A CG1 2957 C CG2 . ILE A 379 ? 0.9450 0.9035 0.7909 -0.0546 -0.0199 -0.0496 409 ILE A CG2 2958 C CD1 . ILE A 379 ? 1.0223 0.9665 0.8489 -0.0576 -0.0112 -0.0556 409 ILE A CD1 2959 N N . ALA A 380 ? 0.8857 0.8412 0.7314 -0.0474 -0.0204 -0.0364 410 ALA A N 2960 C CA . ALA A 380 ? 0.8733 0.8337 0.7293 -0.0468 -0.0225 -0.0340 410 ALA A CA 2961 C C . ALA A 380 ? 0.8702 0.8385 0.7334 -0.0480 -0.0275 -0.0375 410 ALA A C 2962 O O . ALA A 380 ? 0.8924 0.8646 0.7654 -0.0482 -0.0280 -0.0365 410 ALA A O 2963 C CB . ALA A 380 ? 0.8604 0.8183 0.7112 -0.0434 -0.0241 -0.0302 410 ALA A CB 2964 N N . GLY A 381 ? 0.8917 0.8624 0.7502 -0.0487 -0.0310 -0.0419 411 GLY A N 2965 C CA . GLY A 381 ? 0.9145 0.8927 0.7810 -0.0504 -0.0348 -0.0462 411 GLY A CA 2966 C C . GLY A 381 ? 0.9151 0.8966 0.7755 -0.0507 -0.0396 -0.0517 411 GLY A C 2967 O O . GLY A 381 ? 0.9272 0.9038 0.7762 -0.0500 -0.0390 -0.0527 411 GLY A O 2968 N N . PHE A 382 ? 0.8709 0.8605 0.7390 -0.0516 -0.0442 -0.0556 412 PHE A N 2969 C CA . PHE A 382 ? 0.8609 0.8561 0.7259 -0.0519 -0.0499 -0.0619 412 PHE A CA 2970 C C . PHE A 382 ? 0.9068 0.9093 0.7727 -0.0482 -0.0573 -0.0615 412 PHE A C 2971 O O . PHE A 382 ? 0.9399 0.9448 0.8135 -0.0471 -0.0574 -0.0579 412 PHE A O 2972 C CB . PHE A 382 ? 0.8151 0.8140 0.6901 -0.0571 -0.0481 -0.0685 412 PHE A CB 2973 C CG . PHE A 382 ? 0.8243 0.8157 0.6959 -0.0602 -0.0413 -0.0698 412 PHE A CG 2974 C CD1 . PHE A 382 ? 0.8224 0.8080 0.6979 -0.0610 -0.0341 -0.0654 412 PHE A CD1 2975 C CD2 . PHE A 382 ? 0.8516 0.8413 0.7148 -0.0615 -0.0422 -0.0753 412 PHE A CD2 2976 C CE1 . PHE A 382 ? 0.8380 0.8164 0.7100 -0.0632 -0.0277 -0.0662 412 PHE A CE1 2977 C CE2 . PHE A 382 ? 0.8633 0.8451 0.7226 -0.0642 -0.0355 -0.0762 412 PHE A CE2 2978 C CZ . PHE A 382 ? 0.8471 0.8233 0.7111 -0.0650 -0.0280 -0.0715 412 PHE A CZ 2979 N N . VAL A 383 ? 0.9314 0.9374 0.7889 -0.0456 -0.0635 -0.0653 413 VAL A N 2980 C CA . VAL A 383 ? 0.9455 0.9590 0.8025 -0.0409 -0.0711 -0.0652 413 VAL A CA 2981 C C . VAL A 383 ? 0.9892 1.0131 0.8481 -0.0412 -0.0786 -0.0740 413 VAL A C 2982 O O . VAL A 383 ? 1.0715 1.0940 0.9228 -0.0423 -0.0795 -0.0791 413 VAL A O 2983 C CB . VAL A 383 ? 0.9362 0.9427 0.7777 -0.0344 -0.0720 -0.0589 413 VAL A CB 2984 C CG1 . VAL A 383 ? 0.9514 0.9526 0.7768 -0.0324 -0.0728 -0.0611 413 VAL A CG1 2985 C CG2 . VAL A 383 ? 0.9364 0.9496 0.7781 -0.0289 -0.0788 -0.0573 413 VAL A CG2 2986 N N . LYS A 384 ? 0.9889 1.0234 0.8584 -0.0400 -0.0839 -0.0760 414 LYS A N 2987 C CA . LYS A 384 ? 0.9893 1.0363 0.8648 -0.0404 -0.0915 -0.0850 414 LYS A CA 2988 C C . LYS A 384 ? 1.0096 1.0631 0.8819 -0.0331 -0.0991 -0.0826 414 LYS A C 2989 O O . LYS A 384 ? 1.0529 1.1089 0.9342 -0.0321 -0.0983 -0.0785 414 LYS A O 2990 C CB . LYS A 384 ? 1.0252 1.0791 0.9210 -0.0470 -0.0887 -0.0901 414 LYS A CB 2991 C CG . LYS A 384 ? 1.0897 1.1565 0.9960 -0.0499 -0.0944 -0.1013 414 LYS A CG 2992 C CD . LYS A 384 ? 1.0932 1.1649 1.0203 -0.0562 -0.0896 -0.1049 414 LYS A CD 2993 C CE . LYS A 384 ? 1.1661 1.2483 1.1052 -0.0614 -0.0924 -0.1173 414 LYS A CE 2994 N NZ . LYS A 384 ? 1.1878 1.2627 1.1274 -0.0682 -0.0851 -0.1219 414 LYS A NZ 2995 N N . GLU A 385 ? 1.0491 1.1048 0.9078 -0.0272 -0.1061 -0.0848 415 GLU A N 2996 C CA . GLU A 385 ? 1.0706 1.1315 0.9240 -0.0188 -0.1131 -0.0818 415 GLU A CA 2997 C C . GLU A 385 ? 1.0620 1.1402 0.9254 -0.0173 -0.1230 -0.0908 415 GLU A C 2998 O O . GLU A 385 ? 1.1765 1.2617 1.0425 -0.0203 -0.1269 -0.1002 415 GLU A O 2999 C CB . GLU A 385 ? 1.1249 1.1758 0.9544 -0.0109 -0.1143 -0.0767 415 GLU A CB 3000 C CG . GLU A 385 ? 1.1319 1.1666 0.9527 -0.0110 -0.1047 -0.0669 415 GLU A CG 3001 C CD . GLU A 385 ? 1.1405 1.1656 0.9408 -0.0018 -0.1049 -0.0597 415 GLU A CD 3002 O OE1 . GLU A 385 ? 1.0856 1.1134 0.8846 0.0043 -0.1084 -0.0559 415 GLU A OE1 3003 O OE2 . GLU A 385 ? 1.2199 1.2336 1.0050 -0.0007 -0.1008 -0.0575 415 GLU A OE2 3004 N N . PHE A 386 ? 0.9933 1.0787 0.8634 -0.0128 -0.1268 -0.0880 416 PHE A N 3005 C CA . PHE A 386 ? 0.9959 1.0980 0.8733 -0.0088 -0.1371 -0.0950 416 PHE A CA 3006 C C . PHE A 386 ? 0.9930 1.0930 0.8543 0.0027 -0.1422 -0.0882 416 PHE A C 3007 O O . PHE A 386 ? 0.9534 1.0390 0.8012 0.0059 -0.1364 -0.0785 416 PHE A O 3008 C CB . PHE A 386 ? 1.0091 1.1218 0.9110 -0.0135 -0.1360 -0.0976 416 PHE A CB 3009 C CG . PHE A 386 ? 0.9939 1.1070 0.9116 -0.0243 -0.1295 -0.1033 416 PHE A CG 3010 C CD1 . PHE A 386 ? 0.9321 1.0328 0.8518 -0.0294 -0.1190 -0.0970 416 PHE A CD1 3011 C CD2 . PHE A 386 ? 0.9766 1.1026 0.9075 -0.0290 -0.1337 -0.1154 416 PHE A CD2 3012 C CE1 . PHE A 386 ? 0.9101 1.0103 0.8429 -0.0382 -0.1125 -0.1018 416 PHE A CE1 3013 C CE2 . PHE A 386 ? 0.9499 1.0747 0.8948 -0.0387 -0.1265 -0.1205 416 PHE A CE2 3014 C CZ . PHE A 386 ? 0.9219 1.0334 0.8671 -0.0430 -0.1157 -0.1133 416 PHE A CZ 3015 N N . SER A 387 ? 1.0322 1.1464 0.8954 0.0092 -0.1525 -0.0932 417 SER A N 3016 C CA . SER A 387 ? 1.0487 1.1603 0.8962 0.0212 -0.1567 -0.0861 417 SER A CA 3017 C C . SER A 387 ? 1.0363 1.1434 0.8916 0.0216 -0.1509 -0.0771 417 SER A C 3018 O O . SER A 387 ? 1.0133 1.1313 0.8891 0.0182 -0.1516 -0.0798 417 SER A O 3019 C CB . SER A 387 ? 1.0354 1.1639 0.8825 0.0293 -0.1697 -0.0935 417 SER A CB 3020 O OG . SER A 387 ? 1.0003 1.1438 0.8691 0.0284 -0.1731 -0.0965 417 SER A OG 3021 N N . HIS A 388 ? 1.0454 1.1357 0.8849 0.0251 -0.1443 -0.0668 418 HIS A N 3022 C CA . HIS A 388 ? 1.1078 1.1912 0.9509 0.0263 -0.1384 -0.0578 418 HIS A CA 3023 C C . HIS A 388 ? 1.1270 1.2062 0.9856 0.0162 -0.1298 -0.0565 418 HIS A C 3024 O O . HIS A 388 ? 1.2675 1.3398 1.1281 0.0166 -0.1245 -0.0494 418 HIS A O 3025 C CB . HIS A 388 ? 1.0946 1.1902 0.9456 0.0332 -0.1450 -0.0579 418 HIS A CB 3026 C CG . HIS A 388 ? 1.1338 1.2318 0.9675 0.0455 -0.1530 -0.0570 418 HIS A CG 3027 N ND1 . HIS A 388 ? 1.1717 1.2844 1.0055 0.0490 -0.1636 -0.0663 418 HIS A ND1 3028 C CD2 . HIS A 388 ? 1.1391 1.2260 0.9539 0.0556 -0.1516 -0.0482 418 HIS A CD2 3029 C CE1 . HIS A 388 ? 1.1982 1.3092 1.0130 0.0614 -0.1690 -0.0630 418 HIS A CE1 3030 N NE2 . HIS A 388 ? 1.1832 1.2780 0.9859 0.0657 -0.1614 -0.0517 418 HIS A NE2 3031 N N . ILE A 389 ? 1.1122 1.1951 0.9810 0.0074 -0.1282 -0.0632 419 ILE A N 3032 C CA . ILE A 389 ? 1.0594 1.1375 0.9411 -0.0010 -0.1198 -0.0617 419 ILE A CA 3033 C C . ILE A 389 ? 1.0419 1.1139 0.9216 -0.0082 -0.1150 -0.0648 419 ILE A C 3034 O O . ILE A 389 ? 1.0787 1.1578 0.9611 -0.0110 -0.1187 -0.0730 419 ILE A O 3035 C CB . ILE A 389 ? 1.0663 1.1571 0.9701 -0.0049 -0.1211 -0.0663 419 ILE A CB 3036 C CG1 . ILE A 389 ? 1.0141 1.0977 0.9280 -0.0118 -0.1120 -0.0631 419 ILE A CG1 3037 C CG2 . ILE A 389 ? 1.0952 1.1997 1.0097 -0.0086 -0.1266 -0.0775 419 ILE A CG2 3038 C CD1 . ILE A 389 ? 1.0009 1.0926 0.9323 -0.0128 -0.1117 -0.0639 419 ILE A CD1 3039 N N . ALA A 390 ? 0.9740 1.0329 0.8497 -0.0110 -0.1067 -0.0585 420 ALA A N 3040 C CA . ALA A 390 ? 0.9411 0.9927 0.8142 -0.0171 -0.1011 -0.0600 420 ALA A CA 3041 C C . ALA A 390 ? 0.8988 0.9481 0.7857 -0.0237 -0.0941 -0.0589 420 ALA A C 3042 O O . ALA A 390 ? 0.8964 0.9433 0.7876 -0.0225 -0.0916 -0.0536 420 ALA A O 3043 C CB . ALA A 390 ? 0.9578 0.9954 0.8128 -0.0137 -0.0970 -0.0534 420 ALA A CB 3044 N N . PHE A 391 ? 0.8558 0.9050 0.7484 -0.0302 -0.0907 -0.0639 421 PHE A N 3045 C CA . PHE A 391 ? 0.7963 0.8397 0.6971 -0.0354 -0.0828 -0.0616 421 PHE A CA 3046 C C . PHE A 391 ? 0.8269 0.8593 0.7178 -0.0374 -0.0771 -0.0593 421 PHE A C 3047 O O . PHE A 391 ? 0.8930 0.9241 0.7759 -0.0380 -0.0782 -0.0628 421 PHE A O 3048 C CB . PHE A 391 ? 0.7513 0.8015 0.6675 -0.0412 -0.0812 -0.0683 421 PHE A CB 3049 C CG . PHE A 391 ? 0.7118 0.7551 0.6342 -0.0453 -0.0729 -0.0657 421 PHE A CG 3050 C CD1 . PHE A 391 ? 0.6791 0.7205 0.6067 -0.0439 -0.0703 -0.0605 421 PHE A CD1 3051 C CD2 . PHE A 391 ? 0.7009 0.7390 0.6224 -0.0498 -0.0676 -0.0682 421 PHE A CD2 3052 C CE1 . PHE A 391 ? 0.6589 0.6940 0.5907 -0.0465 -0.0633 -0.0581 421 PHE A CE1 3053 C CE2 . PHE A 391 ? 0.6975 0.7291 0.6234 -0.0523 -0.0602 -0.0654 421 PHE A CE2 3054 C CZ . PHE A 391 ? 0.6639 0.6943 0.5948 -0.0505 -0.0583 -0.0605 421 PHE A CZ 3055 N N . LEU A 392 ? 0.8327 0.8575 0.7249 -0.0385 -0.0710 -0.0538 422 LEU A N 3056 C CA . LEU A 392 ? 0.8514 0.8664 0.7351 -0.0397 -0.0657 -0.0511 422 LEU A CA 3057 C C . LEU A 392 ? 0.8246 0.8353 0.7160 -0.0427 -0.0592 -0.0483 422 LEU A C 3058 O O . LEU A 392 ? 0.8309 0.8428 0.7287 -0.0415 -0.0590 -0.0454 422 LEU A O 3059 C CB . LEU A 392 ? 0.9055 0.9144 0.7765 -0.0345 -0.0665 -0.0455 422 LEU A CB 3060 C CG . LEU A 392 ? 0.9109 0.9090 0.7730 -0.0346 -0.0606 -0.0414 422 LEU A CG 3061 C CD1 . LEU A 392 ? 0.9935 0.9868 0.8399 -0.0295 -0.0626 -0.0393 422 LEU A CD1 3062 C CD2 . LEU A 392 ? 0.8845 0.8783 0.7519 -0.0348 -0.0562 -0.0360 422 LEU A CD2 3063 N N . THR A 393 ? 0.7878 0.7935 0.6781 -0.0459 -0.0540 -0.0494 423 THR A N 3064 C CA . THR A 393 ? 0.7673 0.7687 0.6632 -0.0477 -0.0480 -0.0468 423 THR A CA 3065 C C . THR A 393 ? 0.7882 0.7818 0.6772 -0.0465 -0.0443 -0.0422 423 THR A C 3066 O O . THR A 393 ? 0.8224 0.8123 0.7014 -0.0453 -0.0446 -0.0415 423 THR A O 3067 C CB . THR A 393 ? 0.7690 0.7696 0.6696 -0.0517 -0.0436 -0.0508 423 THR A CB 3068 O OG1 . THR A 393 ? 0.7542 0.7505 0.6462 -0.0530 -0.0419 -0.0527 423 THR A OG1 3069 C CG2 . THR A 393 ? 0.7784 0.7861 0.6879 -0.0539 -0.0456 -0.0563 423 THR A CG2 3070 N N . ILE A 394 ? 0.7626 0.7540 0.6571 -0.0466 -0.0407 -0.0392 424 ILE A N 3071 C CA . ILE A 394 ? 0.7608 0.7462 0.6523 -0.0462 -0.0364 -0.0359 424 ILE A CA 3072 C C . ILE A 394 ? 0.7380 0.7218 0.6343 -0.0481 -0.0314 -0.0369 424 ILE A C 3073 O O . ILE A 394 ? 0.7512 0.7365 0.6545 -0.0476 -0.0304 -0.0361 424 ILE A O 3074 C CB . ILE A 394 ? 0.7782 0.7627 0.6718 -0.0439 -0.0371 -0.0318 424 ILE A CB 3075 C CG1 . ILE A 394 ? 0.8247 0.8087 0.7114 -0.0412 -0.0407 -0.0302 424 ILE A CG1 3076 C CG2 . ILE A 394 ? 0.7722 0.7517 0.6655 -0.0441 -0.0323 -0.0295 424 ILE A CG2 3077 C CD1 . ILE A 394 ? 0.8098 0.8002 0.6989 -0.0400 -0.0462 -0.0318 424 ILE A CD1 3078 N N . LYS A 395 ? 0.7668 0.7470 0.6584 -0.0498 -0.0281 -0.0384 425 LYS A N 3079 C CA . LYS A 395 ? 0.7881 0.7663 0.6830 -0.0513 -0.0231 -0.0396 425 LYS A CA 3080 C C . LYS A 395 ? 0.7972 0.7742 0.6969 -0.0495 -0.0203 -0.0363 425 LYS A C 3081 O O . LYS A 395 ? 0.8348 0.8099 0.7328 -0.0485 -0.0197 -0.0338 425 LYS A O 3082 C CB . LYS A 395 ? 0.8353 0.8088 0.7230 -0.0531 -0.0199 -0.0415 425 LYS A CB 3083 C CG . LYS A 395 ? 0.8504 0.8209 0.7407 -0.0544 -0.0140 -0.0428 425 LYS A CG 3084 C CD . LYS A 395 ? 0.9128 0.8790 0.7956 -0.0567 -0.0115 -0.0460 425 LYS A CD 3085 C CE . LYS A 395 ? 0.9591 0.9205 0.8339 -0.0556 -0.0098 -0.0435 425 LYS A CE 3086 N NZ . LYS A 395 ? 0.9971 0.9562 0.8759 -0.0542 -0.0049 -0.0398 425 LYS A NZ 3087 N N . GLY A 396 ? 0.7747 0.7528 0.6803 -0.0488 -0.0184 -0.0366 426 GLY A N 3088 C CA . GLY A 396 ? 0.7649 0.7431 0.6750 -0.0462 -0.0167 -0.0342 426 GLY A CA 3089 C C . GLY A 396 ? 0.7468 0.7282 0.6606 -0.0442 -0.0206 -0.0323 426 GLY A C 3090 O O . GLY A 396 ? 0.7944 0.7765 0.7119 -0.0424 -0.0199 -0.0309 426 GLY A O 3091 N N . ALA A 397 ? 0.6896 0.6732 0.6029 -0.0444 -0.0248 -0.0324 427 ALA A N 3092 C CA . ALA A 397 ? 0.6525 0.6384 0.5691 -0.0425 -0.0282 -0.0307 427 ALA A CA 3093 C C . ALA A 397 ? 0.6645 0.6528 0.5849 -0.0410 -0.0298 -0.0312 427 ALA A C 3094 O O . ALA A 397 ? 0.6810 0.6699 0.6014 -0.0421 -0.0293 -0.0331 427 ALA A O 3095 C CB . ALA A 397 ? 0.6475 0.6330 0.5600 -0.0429 -0.0311 -0.0296 427 ALA A CB 3096 N N . GLY A 398 ? 0.6640 0.6534 0.5877 -0.0386 -0.0314 -0.0300 428 GLY A N 3097 C CA . GLY A 398 ? 0.6692 0.6600 0.5957 -0.0364 -0.0324 -0.0301 428 GLY A CA 3098 C C . GLY A 398 ? 0.7077 0.7003 0.6346 -0.0363 -0.0362 -0.0295 428 GLY A C 3099 O O . GLY A 398 ? 0.6633 0.6565 0.5876 -0.0379 -0.0380 -0.0294 428 GLY A O 3100 N N . HIS A 399 ? 0.7450 0.7382 0.6744 -0.0337 -0.0372 -0.0290 429 HIS A N 3101 C CA . HIS A 399 ? 0.7803 0.7750 0.7107 -0.0328 -0.0404 -0.0283 429 HIS A CA 3102 C C . HIS A 399 ? 0.8111 0.8055 0.7400 -0.0330 -0.0429 -0.0268 429 HIS A C 3103 O O . HIS A 399 ? 0.9273 0.9228 0.8554 -0.0328 -0.0453 -0.0260 429 HIS A O 3104 C CB . HIS A 399 ? 0.8116 0.8056 0.7440 -0.0294 -0.0402 -0.0278 429 HIS A CB 3105 C CG . HIS A 399 ? 0.7803 0.7755 0.7144 -0.0283 -0.0421 -0.0273 429 HIS A CG 3106 N ND1 . HIS A 399 ? 0.7825 0.7800 0.7188 -0.0297 -0.0416 -0.0283 429 HIS A ND1 3107 C CD2 . HIS A 399 ? 0.7705 0.7652 0.7050 -0.0260 -0.0442 -0.0261 429 HIS A CD2 3108 C CE1 . HIS A 399 ? 0.7796 0.7784 0.7180 -0.0280 -0.0434 -0.0275 429 HIS A CE1 3109 N NE2 . HIS A 399 ? 0.7826 0.7791 0.7191 -0.0257 -0.0449 -0.0259 429 HIS A NE2 3110 N N . MET A 400 ? 0.8229 0.8157 0.7518 -0.0333 -0.0420 -0.0265 430 MET A N 3111 C CA . MET A 400 ? 0.8228 0.8139 0.7508 -0.0337 -0.0430 -0.0252 430 MET A CA 3112 C C . MET A 400 ? 0.7708 0.7598 0.6958 -0.0359 -0.0407 -0.0249 430 MET A C 3113 O O . MET A 400 ? 0.7500 0.7382 0.6772 -0.0366 -0.0385 -0.0254 430 MET A O 3114 C CB . MET A 400 ? 0.8767 0.8675 0.8087 -0.0323 -0.0435 -0.0258 430 MET A CB 3115 C CG . MET A 400 ? 0.9278 0.9191 0.8607 -0.0298 -0.0458 -0.0255 430 MET A CG 3116 S SD . MET A 400 ? 1.0539 1.0459 0.9906 -0.0272 -0.0469 -0.0275 430 MET A SD 3117 C CE . MET A 400 ? 1.0412 1.0320 0.9814 -0.0294 -0.0465 -0.0284 430 MET A CE 3118 N N . VAL A 401 ? 0.7466 0.7352 0.6666 -0.0365 -0.0414 -0.0243 431 VAL A N 3119 C CA . VAL A 401 ? 0.7386 0.7246 0.6533 -0.0381 -0.0392 -0.0241 431 VAL A CA 3120 C C . VAL A 401 ? 0.7132 0.6949 0.6275 -0.0386 -0.0363 -0.0226 431 VAL A C 3121 O O . VAL A 401 ? 0.7281 0.7085 0.6434 -0.0400 -0.0330 -0.0232 431 VAL A O 3122 C CB . VAL A 401 ? 0.7601 0.7466 0.6685 -0.0376 -0.0417 -0.0240 431 VAL A CB 3123 C CG1 . VAL A 401 ? 0.7955 0.7775 0.6959 -0.0379 -0.0397 -0.0230 431 VAL A CG1 3124 C CG2 . VAL A 401 ? 0.7663 0.7572 0.6767 -0.0386 -0.0430 -0.0268 431 VAL A CG2 3125 N N . PRO A 402 ? 0.7012 0.6803 0.6147 -0.0374 -0.0368 -0.0208 432 PRO A N 3126 C CA . PRO A 402 ? 0.7226 0.6966 0.6364 -0.0383 -0.0328 -0.0196 432 PRO A CA 3127 C C . PRO A 402 ? 0.7578 0.7335 0.6806 -0.0399 -0.0305 -0.0216 432 PRO A C 3128 O O . PRO A 402 ? 0.8360 0.8082 0.7604 -0.0414 -0.0262 -0.0214 432 PRO A O 3129 C CB . PRO A 402 ? 0.7134 0.6845 0.6262 -0.0365 -0.0338 -0.0177 432 PRO A CB 3130 C CG . PRO A 402 ? 0.7149 0.6891 0.6234 -0.0343 -0.0383 -0.0171 432 PRO A CG 3131 C CD . PRO A 402 ? 0.7186 0.6988 0.6313 -0.0353 -0.0403 -0.0197 432 PRO A CD 3132 N N . THR A 403 ? 0.7456 0.7265 0.6743 -0.0392 -0.0332 -0.0237 433 THR A N 3133 C CA . THR A 403 ? 0.7439 0.7280 0.6809 -0.0397 -0.0323 -0.0262 433 THR A CA 3134 C C . THR A 403 ? 0.7667 0.7519 0.7033 -0.0403 -0.0298 -0.0269 433 THR A C 3135 O O . THR A 403 ? 0.7430 0.7282 0.6841 -0.0416 -0.0266 -0.0278 433 THR A O 3136 C CB . THR A 403 ? 0.7230 0.7115 0.6641 -0.0373 -0.0362 -0.0280 433 THR A CB 3137 O OG1 . THR A 403 ? 0.7224 0.7093 0.6625 -0.0365 -0.0384 -0.0272 433 THR A OG1 3138 C CG2 . THR A 403 ? 0.7034 0.6958 0.6528 -0.0369 -0.0362 -0.0311 433 THR A CG2 3139 N N . ASP A 404 ? 0.7754 0.7616 0.7074 -0.0396 -0.0310 -0.0267 434 ASP A N 3140 C CA . ASP A 404 ? 0.7796 0.7659 0.7105 -0.0401 -0.0283 -0.0273 434 ASP A CA 3141 C C . ASP A 404 ? 0.7739 0.7556 0.6996 -0.0422 -0.0245 -0.0262 434 ASP A C 3142 O O . ASP A 404 ? 0.7671 0.7483 0.6948 -0.0430 -0.0208 -0.0266 434 ASP A O 3143 C CB . ASP A 404 ? 0.8008 0.7883 0.7286 -0.0392 -0.0296 -0.0278 434 ASP A CB 3144 C CG . ASP A 404 ? 0.8381 0.8287 0.7698 -0.0364 -0.0321 -0.0286 434 ASP A CG 3145 O OD1 . ASP A 404 ? 0.8242 0.8170 0.7610 -0.0346 -0.0327 -0.0295 434 ASP A OD1 3146 O OD2 . ASP A 404 ? 0.8762 0.8670 0.8059 -0.0357 -0.0336 -0.0285 434 ASP A OD2 3147 N N . LYS A 405 ? 0.7556 0.7339 0.6743 -0.0426 -0.0253 -0.0246 435 LYS A N 3148 C CA . LYS A 405 ? 0.7414 0.7142 0.6524 -0.0436 -0.0219 -0.0233 435 LYS A CA 3149 C C . LYS A 405 ? 0.8012 0.7694 0.7075 -0.0427 -0.0217 -0.0209 435 LYS A C 3150 O O . LYS A 405 ? 0.8216 0.7884 0.7200 -0.0413 -0.0243 -0.0199 435 LYS A O 3151 C CB . LYS A 405 ? 0.7073 0.6800 0.6106 -0.0438 -0.0232 -0.0241 435 LYS A CB 3152 C CG . LYS A 405 ? 0.7006 0.6762 0.6070 -0.0445 -0.0226 -0.0264 435 LYS A CG 3153 C CD . LYS A 405 ? 0.7037 0.6774 0.6118 -0.0453 -0.0175 -0.0266 435 LYS A CD 3154 C CE . LYS A 405 ? 0.7133 0.6893 0.6242 -0.0452 -0.0166 -0.0284 435 LYS A CE 3155 N NZ . LYS A 405 ? 0.7386 0.7120 0.6492 -0.0458 -0.0113 -0.0286 435 LYS A NZ 3156 N N . PRO A 406 ? 0.8115 0.7773 0.7233 -0.0434 -0.0184 -0.0202 436 PRO A N 3157 C CA . PRO A 406 ? 0.7999 0.7597 0.7071 -0.0423 -0.0169 -0.0176 436 PRO A CA 3158 C C . PRO A 406 ? 0.8215 0.7738 0.7157 -0.0411 -0.0140 -0.0151 436 PRO A C 3159 O O . PRO A 406 ? 0.8517 0.8011 0.7371 -0.0384 -0.0161 -0.0130 436 PRO A O 3160 C CB . PRO A 406 ? 0.7926 0.7511 0.7099 -0.0442 -0.0124 -0.0184 436 PRO A CB 3161 C CG . PRO A 406 ? 0.7849 0.7494 0.7114 -0.0458 -0.0119 -0.0213 436 PRO A CG 3162 C CD . PRO A 406 ? 0.7907 0.7601 0.7142 -0.0447 -0.0165 -0.0223 436 PRO A CD 3163 N N . LEU A 407 ? 0.8283 0.7774 0.7206 -0.0423 -0.0091 -0.0152 437 LEU A N 3164 C CA . LEU A 407 ? 0.8511 0.7917 0.7299 -0.0406 -0.0055 -0.0127 437 LEU A CA 3165 C C . LEU A 407 ? 0.8841 0.8264 0.7519 -0.0383 -0.0113 -0.0131 437 LEU A C 3166 O O . LEU A 407 ? 0.8765 0.8135 0.7325 -0.0349 -0.0120 -0.0107 437 LEU A O 3167 C CB . LEU A 407 ? 0.8428 0.7799 0.7217 -0.0424 0.0007 -0.0131 437 LEU A CB 3168 C CG . LEU A 407 ? 0.8722 0.7992 0.7356 -0.0402 0.0051 -0.0105 437 LEU A CG 3169 C CD1 . LEU A 407 ? 0.8617 0.7798 0.7185 -0.0376 0.0088 -0.0067 437 LEU A CD1 3170 C CD2 . LEU A 407 ? 0.9163 0.8396 0.7813 -0.0421 0.0122 -0.0108 437 LEU A CD2 3171 N N . ALA A 408 ? 0.8701 0.8197 0.7419 -0.0398 -0.0154 -0.0162 438 ALA A N 3172 C CA . ALA A 408 ? 0.8421 0.7950 0.7066 -0.0384 -0.0210 -0.0179 438 ALA A CA 3173 C C . ALA A 408 ? 0.8543 0.8101 0.7184 -0.0358 -0.0263 -0.0169 438 ALA A C 3174 O O . ALA A 408 ? 0.9313 0.8868 0.7859 -0.0329 -0.0298 -0.0167 438 ALA A O 3175 C CB . ALA A 408 ? 0.8173 0.7769 0.6885 -0.0410 -0.0230 -0.0216 438 ALA A CB 3176 N N . ALA A 409 ? 0.8507 0.8096 0.7249 -0.0365 -0.0269 -0.0165 439 ALA A N 3177 C CA . ALA A 409 ? 0.8476 0.8088 0.7224 -0.0341 -0.0312 -0.0154 439 ALA A CA 3178 C C . ALA A 409 ? 0.8779 0.8314 0.7428 -0.0305 -0.0294 -0.0116 439 ALA A C 3179 O O . ALA A 409 ? 0.8897 0.8443 0.7489 -0.0269 -0.0335 -0.0106 439 ALA A O 3180 C CB . ALA A 409 ? 0.7906 0.7552 0.6773 -0.0355 -0.0315 -0.0159 439 ALA A CB 3181 N N . PHE A 410 ? 0.9341 0.8796 0.7974 -0.0311 -0.0226 -0.0095 440 PHE A N 3182 C CA . PHE A 410 ? 0.9659 0.9017 0.8189 -0.0274 -0.0188 -0.0054 440 PHE A CA 3183 C C . PHE A 410 ? 0.9675 0.9000 0.8046 -0.0234 -0.0204 -0.0045 440 PHE A C 3184 O O . PHE A 410 ? 1.0269 0.9569 0.8543 -0.0183 -0.0229 -0.0021 440 PHE A O 3185 C CB . PHE A 410 ? 0.9769 0.9043 0.8332 -0.0295 -0.0098 -0.0038 440 PHE A CB 3186 C CG . PHE A 410 ? 0.9956 0.9112 0.8415 -0.0257 -0.0043 0.0007 440 PHE A CG 3187 C CD1 . PHE A 410 ? 1.0135 0.9267 0.8621 -0.0242 -0.0039 0.0025 440 PHE A CD1 3188 C CD2 . PHE A 410 ? 0.9968 0.9029 0.8291 -0.0231 0.0009 0.0032 440 PHE A CD2 3189 C CE1 . PHE A 410 ? 1.0188 0.9198 0.8569 -0.0202 0.0020 0.0071 440 PHE A CE1 3190 C CE2 . PHE A 410 ? 1.0189 0.9125 0.8400 -0.0187 0.0068 0.0079 440 PHE A CE2 3191 C CZ . PHE A 410 ? 1.0538 0.9447 0.8778 -0.0172 0.0076 0.0099 440 PHE A CZ 3192 N N . THR A 411 ? 0.9205 0.8530 0.7546 -0.0253 -0.0192 -0.0065 441 THR A N 3193 C CA . THR A 411 ? 0.9043 0.8339 0.7229 -0.0217 -0.0210 -0.0067 441 THR A CA 3194 C C . THR A 411 ? 0.9061 0.8439 0.7217 -0.0187 -0.0302 -0.0087 441 THR A C 3195 O O . THR A 411 ? 0.9397 0.8743 0.7420 -0.0129 -0.0326 -0.0070 441 THR A O 3196 C CB . THR A 411 ? 0.8680 0.7988 0.6867 -0.0252 -0.0196 -0.0100 441 THR A CB 3197 O OG1 . THR A 411 ? 0.8716 0.7948 0.6925 -0.0274 -0.0108 -0.0080 441 THR A OG1 3198 C CG2 . THR A 411 ? 0.8863 0.8151 0.6893 -0.0216 -0.0226 -0.0112 441 THR A CG2 3199 N N . MET A 412 ? 0.9186 0.8670 0.7468 -0.0222 -0.0349 -0.0124 442 MET A N 3200 C CA . MET A 412 ? 0.9126 0.8705 0.7419 -0.0204 -0.0432 -0.0153 442 MET A CA 3201 C C . MET A 412 ? 0.8782 0.8344 0.7030 -0.0150 -0.0453 -0.0117 442 MET A C 3202 O O . MET A 412 ? 0.9400 0.8982 0.7555 -0.0099 -0.0504 -0.0119 442 MET A O 3203 C CB . MET A 412 ? 0.9131 0.8801 0.7583 -0.0251 -0.0454 -0.0186 442 MET A CB 3204 C CG . MET A 412 ? 0.9277 0.9046 0.7780 -0.0238 -0.0526 -0.0212 442 MET A CG 3205 S SD . MET A 412 ? 0.9337 0.9170 0.8013 -0.0277 -0.0526 -0.0225 442 MET A SD 3206 C CE . MET A 412 ? 0.9643 0.9415 0.8327 -0.0253 -0.0498 -0.0171 442 MET A CE 3207 N N . PHE A 413 ? 0.8330 0.7859 0.6649 -0.0160 -0.0415 -0.0086 443 PHE A N 3208 C CA . PHE A 413 ? 0.8545 0.8049 0.6840 -0.0114 -0.0423 -0.0050 443 PHE A CA 3209 C C . PHE A 413 ? 0.8971 0.8370 0.7093 -0.0050 -0.0395 -0.0007 443 PHE A C 3210 O O . PHE A 413 ? 0.8566 0.7976 0.6607 0.0011 -0.0440 0.0007 443 PHE A O 3211 C CB . PHE A 413 ? 0.8240 0.7716 0.6646 -0.0147 -0.0376 -0.0034 443 PHE A CB 3212 C CG . PHE A 413 ? 0.8251 0.7682 0.6635 -0.0106 -0.0368 0.0003 443 PHE A CG 3213 C CD1 . PHE A 413 ? 0.8298 0.7800 0.6709 -0.0078 -0.0430 -0.0001 443 PHE A CD1 3214 C CD2 . PHE A 413 ? 0.8974 0.8286 0.7317 -0.0097 -0.0291 0.0041 443 PHE A CD2 3215 C CE1 . PHE A 413 ? 0.8711 0.8164 0.7098 -0.0038 -0.0418 0.0036 443 PHE A CE1 3216 C CE2 . PHE A 413 ? 0.8880 0.8138 0.7201 -0.0060 -0.0274 0.0077 443 PHE A CE2 3217 C CZ . PHE A 413 ? 0.8831 0.8158 0.7169 -0.0028 -0.0339 0.0075 443 PHE A CZ 3218 N N . SER A 414 ? 0.9455 0.8752 0.7518 -0.0060 -0.0319 0.0013 444 SER A N 3219 C CA . SER A 414 ? 1.0022 0.9197 0.7902 0.0003 -0.0277 0.0056 444 SER A CA 3220 C C . SER A 414 ? 1.0180 0.9390 0.7918 0.0061 -0.0347 0.0040 444 SER A C 3221 O O . SER A 414 ? 1.0271 0.9431 0.7869 0.0140 -0.0360 0.0074 444 SER A O 3222 C CB . SER A 414 ? 1.0133 0.9207 0.7988 -0.0026 -0.0184 0.0069 444 SER A CB 3223 O OG . SER A 414 ? 1.1047 0.9985 0.8724 0.0038 -0.0127 0.0118 444 SER A OG 3224 N N . ARG A 415 ? 0.9913 0.9208 0.7688 0.0023 -0.0393 -0.0013 445 ARG A N 3225 C CA . ARG A 415 ? 1.0199 0.9548 0.7863 0.0067 -0.0468 -0.0047 445 ARG A CA 3226 C C . ARG A 415 ? 1.0047 0.9514 0.7753 0.0101 -0.0563 -0.0068 445 ARG A C 3227 O O . ARG A 415 ? 0.9884 0.9390 0.7482 0.0161 -0.0630 -0.0087 445 ARG A O 3228 C CB . ARG A 415 ? 1.0112 0.9514 0.7821 0.0008 -0.0481 -0.0105 445 ARG A CB 3229 C CG . ARG A 415 ? 1.0591 0.9873 0.8223 -0.0007 -0.0393 -0.0084 445 ARG A CG 3230 C CD . ARG A 415 ? 1.0924 1.0250 0.8625 -0.0073 -0.0388 -0.0135 445 ARG A CD 3231 N NE . ARG A 415 ? 1.1567 1.0772 0.9177 -0.0077 -0.0302 -0.0112 445 ARG A NE 3232 C CZ . ARG A 415 ? 1.1624 1.0828 0.9260 -0.0125 -0.0274 -0.0144 445 ARG A CZ 3233 N NH1 . ARG A 415 ? 1.1114 1.0425 0.8864 -0.0174 -0.0321 -0.0200 445 ARG A NH1 3234 N NH2 . ARG A 415 ? 1.2421 1.1509 0.9969 -0.0121 -0.0191 -0.0117 445 ARG A NH2 3235 N N . PHE A 416 ? 0.9676 0.9203 0.7541 0.0065 -0.0570 -0.0068 446 PHE A N 3236 C CA . PHE A 416 ? 0.9747 0.9386 0.7678 0.0092 -0.0648 -0.0085 446 PHE A CA 3237 C C . PHE A 416 ? 1.0261 0.9827 0.8077 0.0177 -0.0639 -0.0026 446 PHE A C 3238 O O . PHE A 416 ? 1.0485 1.0094 0.8210 0.0250 -0.0704 -0.0030 446 PHE A O 3239 C CB . PHE A 416 ? 0.9622 0.9330 0.7750 0.0026 -0.0644 -0.0102 446 PHE A CB 3240 C CG . PHE A 416 ? 0.9075 0.8866 0.7276 0.0055 -0.0698 -0.0102 446 PHE A CG 3241 C CD1 . PHE A 416 ? 0.9003 0.8924 0.7251 0.0066 -0.0780 -0.0153 446 PHE A CD1 3242 C CD2 . PHE A 416 ? 0.9026 0.8767 0.7263 0.0067 -0.0663 -0.0056 446 PHE A CD2 3243 C CE1 . PHE A 416 ? 0.9011 0.9011 0.7338 0.0093 -0.0824 -0.0153 446 PHE A CE1 3244 C CE2 . PHE A 416 ? 0.8785 0.8597 0.7088 0.0095 -0.0706 -0.0054 446 PHE A CE2 3245 C CZ . PHE A 416 ? 0.8853 0.8795 0.7202 0.0109 -0.0786 -0.0101 446 PHE A CZ 3246 N N . LEU A 417 ? 1.0371 0.9825 0.8191 0.0170 -0.0557 0.0027 447 LEU A N 3247 C CA . LEU A 417 ? 1.0675 1.0031 0.8382 0.0248 -0.0526 0.0089 447 LEU A CA 3248 C C . LEU A 417 ? 1.0827 1.0114 0.8313 0.0339 -0.0535 0.0113 447 LEU A C 3249 O O . LEU A 417 ? 1.0523 0.9797 0.7909 0.0428 -0.0564 0.0145 447 LEU A O 3250 C CB . LEU A 417 ? 1.0564 0.9789 0.8297 0.0216 -0.0417 0.0134 447 LEU A CB 3251 C CG . LEU A 417 ? 1.0530 0.9785 0.8432 0.0167 -0.0403 0.0133 447 LEU A CG 3252 C CD1 . LEU A 417 ? 1.0910 1.0016 0.8792 0.0163 -0.0296 0.0182 447 LEU A CD1 3253 C CD2 . LEU A 417 ? 1.0703 1.0041 0.8640 0.0210 -0.0471 0.0134 447 LEU A CD2 3254 N N . ASN A 418 ? 1.1439 1.0675 0.8844 0.0323 -0.0506 0.0100 448 ASN A N 3255 C CA . ASN A 418 ? 1.2002 1.1150 0.9178 0.0410 -0.0503 0.0124 448 ASN A CA 3256 C C . ASN A 418 ? 1.2694 1.1964 0.9809 0.0445 -0.0615 0.0063 448 ASN A C 3257 O O . ASN A 418 ? 1.3241 1.2451 1.0185 0.0490 -0.0614 0.0060 448 ASN A O 3258 C CB . ASN A 418 ? 1.1663 1.0668 0.8768 0.0380 -0.0397 0.0147 448 ASN A CB 3259 C CG . ASN A 418 ? 1.1505 1.0379 0.8651 0.0359 -0.0281 0.0206 448 ASN A CG 3260 O OD1 . ASN A 418 ? 1.1646 1.0415 0.8682 0.0432 -0.0240 0.0264 448 ASN A OD1 3261 N ND2 . ASN A 418 ? 1.1303 1.0182 0.8608 0.0264 -0.0228 0.0189 448 ASN A ND2 3262 N N . LYS A 419 ? 1.3557 1.2995 1.0811 0.0425 -0.0710 0.0010 449 LYS A N 3263 C CA . LYS A 419 ? 1.5003 1.4574 1.2225 0.0455 -0.0821 -0.0058 449 LYS A CA 3264 C C . LYS A 419 ? 1.5498 1.5046 1.2638 0.0429 -0.0818 -0.0101 449 LYS A C 3265 O O . LYS A 419 ? 1.5040 1.4627 1.2050 0.0490 -0.0889 -0.0138 449 LYS A O 3266 C CB . LYS A 419 ? 1.5801 1.5370 1.2850 0.0586 -0.0881 -0.0033 449 LYS A CB 3267 C CG . LYS A 419 ? 1.6403 1.5936 1.3458 0.0643 -0.0860 0.0032 449 LYS A CG 3268 C CD . LYS A 419 ? 1.7330 1.6878 1.4208 0.0781 -0.0931 0.0047 449 LYS A CD 3269 C CE . LYS A 419 ? 1.7757 1.7178 1.4542 0.0862 -0.0868 0.0140 449 LYS A CE 3270 N NZ . LYS A 419 ? 1.7728 1.7202 1.4714 0.0809 -0.0854 0.0151 449 LYS A NZ 3271 N N . GLN A 420 ? 1.6431 1.5917 1.3643 0.0342 -0.0738 -0.0099 450 GLN A N 3272 C CA . GLN A 420 ? 1.7146 1.6580 1.4269 0.0318 -0.0712 -0.0127 450 GLN A CA 3273 C C . GLN A 420 ? 1.7064 1.6625 1.4348 0.0226 -0.0755 -0.0211 450 GLN A C 3274 O O . GLN A 420 ? 1.6603 1.6256 1.4084 0.0164 -0.0767 -0.0230 450 GLN A O 3275 C CB . GLN A 420 ? 1.7169 1.6437 1.4252 0.0291 -0.0584 -0.0066 450 GLN A CB 3276 C CG . GLN A 420 ? 1.7358 1.6459 1.4213 0.0386 -0.0523 0.0004 450 GLN A CG 3277 C CD . GLN A 420 ? 1.7909 1.6865 1.4791 0.0358 -0.0393 0.0072 450 GLN A CD 3278 O OE1 . GLN A 420 ? 1.8374 1.7353 1.5433 0.0266 -0.0349 0.0061 450 GLN A OE1 3279 N NE2 . GLN A 420 ? 1.8358 1.7161 1.5063 0.0440 -0.0328 0.0141 450 GLN A NE2 3280 N N . PRO A 421 ? 1.7545 1.7102 1.4739 0.0220 -0.0772 -0.0261 451 PRO A N 3281 C CA . PRO A 421 ? 1.6945 1.6596 1.4283 0.0129 -0.0791 -0.0337 451 PRO A CA 3282 C C . PRO A 421 ? 1.6000 1.5586 1.3453 0.0046 -0.0692 -0.0309 451 PRO A C 3283 O O . PRO A 421 ? 1.5031 1.4482 1.2400 0.0058 -0.0606 -0.0249 451 PRO A O 3284 C CB . PRO A 421 ? 1.7310 1.6936 1.4483 0.0156 -0.0819 -0.0386 451 PRO A CB 3285 C CG . PRO A 421 ? 1.7415 1.6880 1.4361 0.0239 -0.0764 -0.0313 451 PRO A CG 3286 C CD . PRO A 421 ? 1.7533 1.6983 1.4479 0.0297 -0.0764 -0.0246 451 PRO A CD 3287 N N . TYR A 422 ? 1.5234 1.4916 1.2879 -0.0031 -0.0702 -0.0353 452 TYR A N 3288 C CA . TYR A 422 ? 1.4860 1.4500 1.2630 -0.0100 -0.0620 -0.0326 452 TYR A CA 3289 C C . TYR A 422 ? 1.5747 1.5320 1.3475 -0.0140 -0.0562 -0.0343 452 TYR A C 3290 O O . TYR A 422 ? 1.6363 1.5852 1.4111 -0.0164 -0.0479 -0.0300 452 TYR A O 3291 C CB . TYR A 422 ? 1.3736 1.3491 1.1712 -0.0155 -0.0647 -0.0358 452 TYR A CB 3292 C CG . TYR A 422 ? 1.3292 1.3112 1.1321 -0.0117 -0.0698 -0.0339 452 TYR A CG 3293 C CD1 . TYR A 422 ? 1.2931 1.2849 1.0940 -0.0076 -0.0787 -0.0380 452 TYR A CD1 3294 C CD2 . TYR A 422 ? 1.2631 1.2420 1.0733 -0.0122 -0.0658 -0.0285 452 TYR A CD2 3295 C CE1 . TYR A 422 ? 1.2446 1.2424 1.0505 -0.0038 -0.0831 -0.0362 452 TYR A CE1 3296 C CE2 . TYR A 422 ? 1.2446 1.2287 1.0591 -0.0086 -0.0699 -0.0268 452 TYR A CE2 3297 C CZ . TYR A 422 ? 1.2847 1.2782 1.0970 -0.0043 -0.0784 -0.0304 452 TYR A CZ 3298 O OH . TYR A 422 ? 1.2572 1.2562 1.0741 -0.0003 -0.0825 -0.0286 452 TYR A OH 3299 N N . ALA B 1 ? 1.6409 1.6312 1.5539 0.2739 -0.0156 -0.0994 1 ALA B N 3300 C CA . ALA B 1 ? 1.5820 1.5905 1.5182 0.2536 -0.0106 -0.1049 1 ALA B CA 3301 C C . ALA B 1 ? 1.5309 1.5518 1.4892 0.2477 -0.0059 -0.1149 1 ALA B C 3302 O O . ALA B 1 ? 1.4906 1.5254 1.4624 0.2604 -0.0125 -0.1263 1 ALA B O 3303 C CB . ALA B 1 ? 1.5284 1.5593 1.4792 0.2550 -0.0200 -0.1132 1 ALA B CB 3304 N N . PRO B 2 ? 1.4606 1.4772 1.4223 0.2290 0.0054 -0.1110 2 PRO B N 3305 C CA . PRO B 2 ? 1.3995 1.4299 1.3821 0.2214 0.0112 -0.1203 2 PRO B CA 3306 C C . PRO B 2 ? 1.3568 1.4161 1.3675 0.2141 0.0085 -0.1316 2 PRO B C 3307 O O . PRO B 2 ? 1.3354 1.3992 1.3511 0.1987 0.0121 -0.1283 2 PRO B O 3308 C CB . PRO B 2 ? 1.3885 1.4035 1.3615 0.2040 0.0234 -0.1111 2 PRO B CB 3309 C CG . PRO B 2 ? 1.3856 1.3899 1.3440 0.1969 0.0234 -0.1001 2 PRO B CG 3310 C CD . PRO B 2 ? 1.4282 1.4289 1.3753 0.2141 0.0131 -0.0984 2 PRO B CD 3311 N N . ASP B 3 ? 1.3389 1.4172 1.3686 0.2255 0.0021 -0.1450 3 ASP B N 3312 C CA . ASP B 3 ? 1.3637 1.4704 1.4223 0.2216 -0.0021 -0.1572 3 ASP B CA 3313 C C . ASP B 3 ? 1.3434 1.4610 1.4195 0.1997 0.0092 -0.1585 3 ASP B C 3314 O O . ASP B 3 ? 1.3099 1.4403 1.4004 0.1888 0.0088 -0.1604 3 ASP B O 3315 C CB . ASP B 3 ? 1.4590 1.5841 1.5359 0.2384 -0.0103 -0.1723 3 ASP B CB 3316 C CG . ASP B 3 ? 1.4953 1.6127 1.5561 0.2615 -0.0237 -0.1722 3 ASP B CG 3317 O OD1 . ASP B 3 ? 1.5003 1.5921 1.5329 0.2697 -0.0230 -0.1611 3 ASP B OD1 3318 O OD2 . ASP B 3 ? 1.4736 1.6107 1.5503 0.2718 -0.0350 -0.1837 3 ASP B OD2 3319 N N . GLN B 4 ? 1.2914 1.4026 1.3646 0.1938 0.0194 -0.1570 4 GLN B N 3320 C CA . GLN B 4 ? 1.2497 1.3701 1.3361 0.1747 0.0311 -0.1579 4 GLN B CA 3321 C C . GLN B 4 ? 1.2321 1.3416 1.3074 0.1576 0.0363 -0.1459 4 GLN B C 3322 O O . GLN B 4 ? 1.2083 1.3288 1.2973 0.1420 0.0430 -0.1468 4 GLN B O 3323 C CB . GLN B 4 ? 1.2703 1.3839 1.3517 0.1742 0.0401 -0.1587 4 GLN B CB 3324 C CG . GLN B 4 ? 1.2591 1.3438 1.3116 0.1713 0.0453 -0.1457 4 GLN B CG 3325 C CD . GLN B 4 ? 1.2964 1.3617 1.3299 0.1893 0.0387 -0.1423 4 GLN B CD 3326 O OE1 . GLN B 4 ? 1.3269 1.3974 1.3634 0.2053 0.0284 -0.1472 4 GLN B OE1 3327 N NE2 . GLN B 4 ? 1.3524 1.3945 1.3656 0.1869 0.0447 -0.1337 4 GLN B NE2 3328 N N . ASP B 5 ? 1.2353 1.3234 1.2861 0.1611 0.0331 -0.1348 5 ASP B N 3329 C CA . ASP B 5 ? 1.2521 1.3302 1.2923 0.1475 0.0359 -0.1242 5 ASP B CA 3330 C C . ASP B 5 ? 1.2572 1.3475 1.3091 0.1464 0.0281 -0.1267 5 ASP B C 3331 O O . ASP B 5 ? 1.2804 1.3659 1.3282 0.1342 0.0302 -0.1197 5 ASP B O 3332 C CB . ASP B 5 ? 1.2697 1.3213 1.2810 0.1517 0.0359 -0.1121 5 ASP B CB 3333 C CG . ASP B 5 ? 1.2678 1.3043 1.2670 0.1478 0.0450 -0.1079 5 ASP B CG 3334 O OD1 . ASP B 5 ? 1.3259 1.3726 1.3374 0.1428 0.0512 -0.1145 5 ASP B OD1 3335 O OD2 . ASP B 5 ? 1.2130 1.2276 1.1907 0.1492 0.0464 -0.0983 5 ASP B OD2 3336 N N . GLU B 6 ? 1.2443 1.3502 1.3106 0.1594 0.0184 -0.1372 6 GLU B N 3337 C CA . GLU B 6 ? 1.2872 1.4050 1.3654 0.1593 0.0100 -0.1411 6 GLU B CA 3338 C C . GLU B 6 ? 1.2636 1.3934 1.3619 0.1402 0.0165 -0.1426 6 GLU B C 3339 O O . GLU B 6 ? 1.2916 1.4309 1.4040 0.1321 0.0248 -0.1469 6 GLU B O 3340 C CB . GLU B 6 ? 1.3680 1.5039 1.4624 0.1761 -0.0015 -0.1547 6 GLU B CB 3341 C CG . GLU B 6 ? 1.4128 1.5630 1.5227 0.1758 -0.0108 -0.1610 6 GLU B CG 3342 C CD . GLU B 6 ? 1.4747 1.6336 1.5858 0.1969 -0.0254 -0.1702 6 GLU B CD 3343 O OE1 . GLU B 6 ? 1.4610 1.6258 1.5756 0.2109 -0.0292 -0.1777 6 GLU B OE1 3344 O OE2 . GLU B 6 ? 1.4498 1.6101 1.5585 0.2000 -0.0337 -0.1704 6 GLU B OE2 3345 N N . ILE B 7 ? 1.1791 1.3074 1.2772 0.1333 0.0131 -0.1387 7 ILE B N 3346 C CA . ILE B 7 ? 1.1561 1.2931 1.2717 0.1158 0.0182 -0.1389 7 ILE B CA 3347 C C . ILE B 7 ? 1.2002 1.3600 1.3452 0.1191 0.0101 -0.1524 7 ILE B C 3348 O O . ILE B 7 ? 1.1369 1.2991 1.2817 0.1289 -0.0010 -0.1559 7 ILE B O 3349 C CB . ILE B 7 ? 1.1398 1.2619 1.2402 0.1068 0.0182 -0.1276 7 ILE B CB 3350 C CG1 . ILE B 7 ? 1.1550 1.2550 1.2271 0.1043 0.0251 -0.1151 7 ILE B CG1 3351 C CG2 . ILE B 7 ? 1.1255 1.2547 1.2433 0.0890 0.0234 -0.1271 7 ILE B CG2 3352 C CD1 . ILE B 7 ? 1.1245 1.2099 1.1801 0.0991 0.0235 -0.1049 7 ILE B CD1 3353 N N . GLN B 8 ? 1.2257 1.4024 1.3963 0.1106 0.0163 -0.1602 8 GLN B N 3354 C CA . GLN B 8 ? 1.2953 1.4958 1.4975 0.1142 0.0093 -0.1751 8 GLN B CA 3355 C C . GLN B 8 ? 1.2712 1.4762 1.4892 0.1016 0.0077 -0.1752 8 GLN B C 3356 O O . GLN B 8 ? 1.2709 1.4761 1.4884 0.1087 -0.0036 -0.1779 8 GLN B O 3357 C CB . GLN B 8 ? 1.3819 1.6002 1.6068 0.1115 0.0170 -0.1847 8 GLN B CB 3358 C CG . GLN B 8 ? 1.4032 1.6212 1.6188 0.1276 0.0153 -0.1889 8 GLN B CG 3359 C CD . GLN B 8 ? 1.4264 1.6519 1.6446 0.1484 -0.0002 -0.1988 8 GLN B CD 3360 O OE1 . GLN B 8 ? 1.3921 1.6354 1.6341 0.1507 -0.0087 -0.2099 8 GLN B OE1 3361 N NE2 . GLN B 8 ? 1.4556 1.6672 1.6492 0.1639 -0.0043 -0.1949 8 GLN B NE2 3362 N N . ARG B 9 ? 1.2513 1.4591 1.4822 0.0835 0.0189 -0.1721 9 ARG B N 3363 C CA . ARG B 9 ? 1.2086 1.4187 1.4550 0.0705 0.0183 -0.1714 9 ARG B CA 3364 C C . ARG B 9 ? 1.1195 1.3101 1.3460 0.0558 0.0280 -0.1555 9 ARG B C 3365 O O . ARG B 9 ? 1.1245 1.3128 1.3480 0.0457 0.0405 -0.1502 9 ARG B O 3366 C CB . ARG B 9 ? 1.2400 1.4726 1.5242 0.0617 0.0227 -0.1829 9 ARG B CB 3367 C CG . ARG B 9 ? 1.2727 1.5274 1.5806 0.0764 0.0122 -0.2007 9 ARG B CG 3368 C CD . ARG B 9 ? 1.2273 1.4856 1.5419 0.0853 -0.0033 -0.2078 9 ARG B CD 3369 N NE . ARG B 9 ? 1.1832 1.4556 1.5323 0.0728 -0.0027 -0.2157 9 ARG B NE 3370 C CZ . ARG B 9 ? 1.2120 1.5082 1.5955 0.0774 -0.0099 -0.2334 9 ARG B CZ 3371 N NH1 . ARG B 9 ? 1.2276 1.5371 1.6148 0.0961 -0.0201 -0.2457 9 ARG B NH1 3372 N NH2 . ARG B 9 ? 1.2563 1.5626 1.6711 0.0635 -0.0076 -0.2390 9 ARG B NH2 3373 N N . LEU B 10 ? 1.0601 1.2375 1.2729 0.0552 0.0217 -0.1486 10 LEU B N 3374 C CA . LEU B 10 ? 1.0683 1.2261 1.2597 0.0436 0.0286 -0.1337 10 LEU B CA 3375 C C . LEU B 10 ? 1.0503 1.2091 1.2587 0.0276 0.0318 -0.1314 10 LEU B C 3376 O O . LEU B 10 ? 1.0743 1.2366 1.2954 0.0287 0.0227 -0.1362 10 LEU B O 3377 C CB . LEU B 10 ? 1.0826 1.2245 1.2476 0.0530 0.0205 -0.1271 10 LEU B CB 3378 C CG . LEU B 10 ? 1.0798 1.2009 1.2175 0.0456 0.0270 -0.1125 10 LEU B CG 3379 C CD1 . LEU B 10 ? 1.0742 1.1902 1.1977 0.0460 0.0363 -0.1087 10 LEU B CD1 3380 C CD2 . LEU B 10 ? 1.0873 1.1964 1.2050 0.0546 0.0183 -0.1079 10 LEU B CD2 3381 N N . PRO B 11 ? 1.0609 1.2163 1.2693 0.0131 0.0448 -0.1244 11 PRO B N 3382 C CA . PRO B 11 ? 1.1022 1.2569 1.3261 -0.0024 0.0492 -0.1210 11 PRO B CA 3383 C C . PRO B 11 ? 1.1389 1.2788 1.3524 -0.0046 0.0415 -0.1140 11 PRO B C 3384 O O . PRO B 11 ? 1.1525 1.2767 1.3386 -0.0016 0.0401 -0.1049 11 PRO B O 3385 C CB . PRO B 11 ? 1.0907 1.2380 1.3022 -0.0145 0.0642 -0.1108 11 PRO B CB 3386 C CG . PRO B 11 ? 1.0739 1.2286 1.2798 -0.0062 0.0685 -0.1155 11 PRO B CG 3387 C CD . PRO B 11 ? 1.0557 1.2091 1.2515 0.0111 0.0562 -0.1204 11 PRO B CD 3388 N N . GLY B 12 ? 1.1340 1.2792 1.3707 -0.0098 0.0366 -0.1189 12 GLY B N 3389 C CA . GLY B 12 ? 1.1180 1.2501 1.3481 -0.0124 0.0293 -0.1134 12 GLY B CA 3390 C C . GLY B 12 ? 1.1903 1.3286 1.4271 0.0008 0.0142 -0.1235 12 GLY B C 3391 O O . GLY B 12 ? 1.2033 1.3329 1.4372 0.0002 0.0070 -0.1212 12 GLY B O 3392 N N . LEU B 13 ? 1.2343 1.3875 1.4788 0.0137 0.0091 -0.1349 13 LEU B N 3393 C CA . LEU B 13 ? 1.2219 1.3839 1.4749 0.0273 -0.0055 -0.1465 13 LEU B CA 3394 C C . LEU B 13 ? 1.1890 1.3699 1.4806 0.0242 -0.0095 -0.1609 13 LEU B C 3395 O O . LEU B 13 ? 1.1496 1.3444 1.4604 0.0211 -0.0033 -0.1674 13 LEU B O 3396 C CB . LEU B 13 ? 1.2304 1.3969 1.4680 0.0449 -0.0104 -0.1507 13 LEU B CB 3397 C CG . LEU B 13 ? 1.2595 1.4080 1.4605 0.0512 -0.0100 -0.1388 13 LEU B CG 3398 C CD1 . LEU B 13 ? 1.3062 1.4590 1.4947 0.0686 -0.0144 -0.1434 13 LEU B CD1 3399 C CD2 . LEU B 13 ? 1.2858 1.4242 1.4769 0.0526 -0.0181 -0.1354 13 LEU B CD2 3400 N N . ALA B 14 ? 1.1659 1.3474 1.4698 0.0249 -0.0197 -0.1666 14 ALA B N 3401 C CA . ALA B 14 ? 1.1742 1.3740 1.5157 0.0240 -0.0259 -0.1825 14 ALA B CA 3402 C C . ALA B 14 ? 1.1652 1.3840 1.5141 0.0414 -0.0348 -0.1973 14 ALA B C 3403 O O . ALA B 14 ? 1.1286 1.3653 1.5045 0.0399 -0.0325 -0.2081 14 ALA B O 3404 C CB . ALA B 14 ? 1.2099 1.4049 1.5604 0.0227 -0.0362 -0.1858 14 ALA B CB 3405 N N . LYS B 15 ? 1.2078 1.4225 1.5327 0.0580 -0.0448 -0.1976 15 LYS B N 3406 C CA . LYS B 15 ? 1.3133 1.5436 1.6399 0.0769 -0.0544 -0.2103 15 LYS B CA 3407 C C . LYS B 15 ? 1.2984 1.5175 1.5884 0.0882 -0.0519 -0.2004 15 LYS B C 3408 O O . LYS B 15 ? 1.2338 1.4342 1.4950 0.0876 -0.0497 -0.1873 15 LYS B O 3409 C CB . LYS B 15 ? 1.3403 1.5794 1.6761 0.0891 -0.0713 -0.2236 15 LYS B CB 3410 C CG . LYS B 15 ? 1.3622 1.5865 1.6641 0.1001 -0.0780 -0.2160 15 LYS B CG 3411 C CD . LYS B 15 ? 1.4183 1.6482 1.7320 0.1056 -0.0920 -0.2269 15 LYS B CD 3412 C CE . LYS B 15 ? 1.4500 1.6635 1.7304 0.1125 -0.0955 -0.2171 15 LYS B CE 3413 N NZ . LYS B 15 ? 1.4871 1.7029 1.7798 0.1132 -0.1064 -0.2255 15 LYS B NZ 3414 N N . GLN B 16 ? 1.3293 1.5600 1.6222 0.0986 -0.0523 -0.2074 16 GLN B N 3415 C CA . GLN B 16 ? 1.2637 1.4834 1.5255 0.1077 -0.0479 -0.1981 16 GLN B CA 3416 C C . GLN B 16 ? 1.2110 1.4210 1.4439 0.1243 -0.0578 -0.1950 16 GLN B C 3417 O O . GLN B 16 ? 1.2069 1.4253 1.4473 0.1335 -0.0704 -0.2049 16 GLN B O 3418 C CB . GLN B 16 ? 1.2657 1.5010 1.5404 0.1153 -0.0466 -0.2075 16 GLN B CB 3419 C CG . GLN B 16 ? 1.2860 1.5271 1.5804 0.0985 -0.0325 -0.2064 16 GLN B CG 3420 C CD . GLN B 16 ? 1.3005 1.5208 1.5698 0.0863 -0.0186 -0.1883 16 GLN B CD 3421 O OE1 . GLN B 16 ? 1.3460 1.5534 1.5867 0.0940 -0.0164 -0.1799 16 GLN B OE1 3422 N NE2 . GLN B 16 ? 1.2926 1.5096 1.5730 0.0675 -0.0092 -0.1825 16 GLN B NE2 3423 N N . PRO B 17 ? 1.1602 1.3524 1.3602 0.1276 -0.0517 -0.1814 17 PRO B N 3424 C CA . PRO B 17 ? 1.1327 1.3131 1.3023 0.1418 -0.0583 -0.1758 17 PRO B CA 3425 C C . PRO B 17 ? 1.1382 1.3300 1.3063 0.1632 -0.0701 -0.1869 17 PRO B C 3426 O O . PRO B 17 ? 1.1707 1.3739 1.3514 0.1687 -0.0703 -0.1948 17 PRO B O 3427 C CB . PRO B 17 ? 1.1502 1.3114 1.2919 0.1387 -0.0469 -0.1605 17 PRO B CB 3428 C CG . PRO B 17 ? 1.1396 1.2993 1.2941 0.1194 -0.0347 -0.1557 17 PRO B CG 3429 C CD . PRO B 17 ? 1.1390 1.3202 1.3294 0.1158 -0.0371 -0.1699 17 PRO B CD 3430 N N . SER B 18 ? 1.1563 1.3445 1.3078 0.1757 -0.0798 -0.1874 18 SER B N 3431 C CA . SER B 18 ? 1.1957 1.3917 1.3385 0.1981 -0.0915 -0.1959 18 SER B CA 3432 C C . SER B 18 ? 1.2608 1.4408 1.3707 0.2091 -0.0868 -0.1845 18 SER B C 3433 O O . SER B 18 ? 1.3872 1.5708 1.4862 0.2286 -0.0954 -0.1895 18 SER B O 3434 C CB . SER B 18 ? 1.1991 1.3972 1.3348 0.2073 -0.1031 -0.2003 18 SER B CB 3435 O OG . SER B 18 ? 1.1469 1.3248 1.2511 0.2062 -0.0979 -0.1852 18 SER B OG 3436 N N . PHE B 19 ? 1.2267 1.3888 1.3214 0.1968 -0.0736 -0.1695 19 PHE B N 3437 C CA . PHE B 19 ? 1.2017 1.3454 1.2653 0.2045 -0.0677 -0.1572 19 PHE B CA 3438 C C . PHE B 19 ? 1.1896 1.3297 1.2588 0.1952 -0.0565 -0.1535 19 PHE B C 3439 O O . PHE B 19 ? 1.1681 1.3138 1.2576 0.1786 -0.0498 -0.1548 19 PHE B O 3440 C CB . PHE B 19 ? 1.2152 1.3393 1.2527 0.1991 -0.0623 -0.1426 19 PHE B CB 3441 C CG . PHE B 19 ? 1.2500 1.3696 1.2974 0.1774 -0.0537 -0.1367 19 PHE B CG 3442 C CD1 . PHE B 19 ? 1.2685 1.3983 1.3356 0.1693 -0.0586 -0.1434 19 PHE B CD1 3443 C CD2 . PHE B 19 ? 1.2910 1.3957 1.3277 0.1655 -0.0411 -0.1248 19 PHE B CD2 3444 C CE1 . PHE B 19 ? 1.2505 1.3747 1.3252 0.1503 -0.0511 -0.1372 19 PHE B CE1 3445 C CE2 . PHE B 19 ? 1.2465 1.3467 1.2904 0.1468 -0.0339 -0.1193 19 PHE B CE2 3446 C CZ . PHE B 19 ? 1.2382 1.3478 1.3006 0.1394 -0.0389 -0.1250 19 PHE B CZ 3447 N N . ARG B 20 ? 1.2179 1.3479 1.2684 0.2063 -0.0543 -0.1487 20 ARG B N 3448 C CA . ARG B 20 ? 1.2174 1.3414 1.2693 0.1983 -0.0434 -0.1444 20 ARG B CA 3449 C C . ARG B 20 ? 1.1680 1.2722 1.2032 0.1828 -0.0313 -0.1292 20 ARG B C 3450 O O . ARG B 20 ? 1.0971 1.1874 1.1113 0.1834 -0.0311 -0.1198 20 ARG B O 3451 C CB . ARG B 20 ? 1.3146 1.4330 1.3526 0.2158 -0.0455 -0.1447 20 ARG B CB 3452 C CG . ARG B 20 ? 1.3515 1.4900 1.4061 0.2324 -0.0579 -0.1605 20 ARG B CG 3453 C CD . ARG B 20 ? 1.3886 1.5224 1.4347 0.2465 -0.0580 -0.1614 20 ARG B CD 3454 N NE . ARG B 20 ? 1.4348 1.5784 1.4794 0.2693 -0.0723 -0.1712 20 ARG B NE 3455 C CZ . ARG B 20 ? 1.4266 1.5582 1.4436 0.2851 -0.0793 -0.1654 20 ARG B CZ 3456 N NH1 . ARG B 20 ? 1.4574 1.5674 1.4473 0.2803 -0.0728 -0.1498 20 ARG B NH1 3457 N NH2 . ARG B 20 ? 1.4239 1.5660 1.4404 0.3064 -0.0930 -0.1754 20 ARG B NH2 3458 N N . GLN B 21 ? 1.1554 1.2594 1.2007 0.1691 -0.0213 -0.1277 21 GLN B N 3459 C CA . GLN B 21 ? 1.1172 1.2038 1.1478 0.1553 -0.0100 -0.1150 21 GLN B CA 3460 C C . GLN B 21 ? 1.1513 1.2363 1.1856 0.1500 -0.0006 -0.1149 21 GLN B C 3461 O O . GLN B 21 ? 1.2309 1.3325 1.2878 0.1483 -0.0002 -0.1247 21 GLN B O 3462 C CB . GLN B 21 ? 1.0617 1.1510 1.1027 0.1385 -0.0076 -0.1127 21 GLN B CB 3463 C CG . GLN B 21 ? 1.0091 1.1186 1.0814 0.1307 -0.0090 -0.1236 21 GLN B CG 3464 C CD . GLN B 21 ? 1.0223 1.1302 1.1021 0.1134 -0.0053 -0.1191 21 GLN B CD 3465 O OE1 . GLN B 21 ? 0.9537 1.0467 1.0156 0.1084 -0.0032 -0.1090 21 GLN B OE1 3466 N NE2 . GLN B 21 ? 1.0306 1.1536 1.1374 0.1042 -0.0044 -0.1267 21 GLN B NE2 3467 N N . TYR B 22 ? 1.1288 1.1944 1.1419 0.1474 0.0069 -0.1043 22 TYR B N 3468 C CA . TYR B 22 ? 1.1539 1.2153 1.1664 0.1444 0.0153 -0.1039 22 TYR B CA 3469 C C . TYR B 22 ? 1.1288 1.1783 1.1333 0.1274 0.0257 -0.0947 22 TYR B C 3470 O O . TYR B 22 ? 1.0974 1.1353 1.0884 0.1223 0.0261 -0.0861 22 TYR B O 3471 C CB . TYR B 22 ? 1.2276 1.2749 1.2209 0.1601 0.0138 -0.1009 22 TYR B CB 3472 C CG . TYR B 22 ? 1.3266 1.3844 1.3249 0.1793 0.0029 -0.1098 22 TYR B CG 3473 C CD1 . TYR B 22 ? 1.3278 1.3866 1.3190 0.1892 -0.0066 -0.1096 22 TYR B CD1 3474 C CD2 . TYR B 22 ? 1.3708 1.4380 1.3806 0.1883 0.0016 -0.1191 22 TYR B CD2 3475 C CE1 . TYR B 22 ? 1.3153 1.3839 1.3096 0.2078 -0.0174 -0.1182 22 TYR B CE1 3476 C CE2 . TYR B 22 ? 1.3798 1.4570 1.3941 0.2068 -0.0093 -0.1279 22 TYR B CE2 3477 C CZ . TYR B 22 ? 1.3422 1.4199 1.3482 0.2166 -0.0191 -0.1273 22 TYR B CZ 3478 O OH . TYR B 22 ? 1.4069 1.4947 1.4160 0.2361 -0.0309 -0.1365 22 TYR B OH 3479 N N . SER B 23 ? 1.1102 1.1639 1.1232 0.1190 0.0337 -0.0972 23 SER B N 3480 C CA . SER B 23 ? 1.0458 1.0884 1.0496 0.1043 0.0433 -0.0894 23 SER B CA 3481 C C . SER B 23 ? 1.0383 1.0776 1.0398 0.1044 0.0508 -0.0914 23 SER B C 3482 O O . SER B 23 ? 1.0422 1.0968 1.0607 0.1050 0.0528 -0.1002 23 SER B O 3483 C CB . SER B 23 ? 1.0481 1.1012 1.0664 0.0889 0.0462 -0.0899 23 SER B CB 3484 O OG . SER B 23 ? 1.0182 1.0627 1.0282 0.0761 0.0556 -0.0839 23 SER B OG 3485 N N . GLY B 24 ? 1.0377 1.0577 1.0196 0.1034 0.0553 -0.0839 24 GLY B N 3486 C CA . GLY B 24 ? 1.0494 1.0638 1.0272 0.1043 0.0621 -0.0859 24 GLY B CA 3487 C C . GLY B 24 ? 1.0722 1.0648 1.0296 0.0999 0.0668 -0.0771 24 GLY B C 3488 O O . GLY B 24 ? 1.0989 1.0846 1.0487 0.0907 0.0675 -0.0699 24 GLY B O 3489 N N . TYR B 25 ? 1.0908 1.0724 1.0403 0.1069 0.0696 -0.0782 25 TYR B N 3490 C CA . TYR B 25 ? 1.0918 1.0534 1.0250 0.1016 0.0751 -0.0718 25 TYR B CA 3491 C C . TYR B 25 ? 1.1031 1.0448 1.0220 0.1133 0.0734 -0.0674 25 TYR B C 3492 O O . TYR B 25 ? 1.1579 1.0993 1.0786 0.1265 0.0708 -0.0720 25 TYR B O 3493 C CB . TYR B 25 ? 1.1006 1.0658 1.0376 0.0945 0.0828 -0.0771 25 TYR B CB 3494 C CG . TYR B 25 ? 1.0710 1.0475 1.0140 0.0796 0.0865 -0.0766 25 TYR B CG 3495 C CD1 . TYR B 25 ? 1.0391 1.0362 0.9991 0.0772 0.0862 -0.0821 25 TYR B CD1 3496 C CD2 . TYR B 25 ? 1.0705 1.0365 1.0022 0.0682 0.0901 -0.0703 25 TYR B CD2 3497 C CE1 . TYR B 25 ? 1.0382 1.0436 1.0026 0.0635 0.0900 -0.0803 25 TYR B CE1 3498 C CE2 . TYR B 25 ? 1.0512 1.0260 0.9864 0.0555 0.0930 -0.0690 25 TYR B CE2 3499 C CZ . TYR B 25 ? 1.0576 1.0512 1.0084 0.0531 0.0932 -0.0734 25 TYR B CZ 3500 O OH . TYR B 25 ? 1.1156 1.1160 1.0688 0.0405 0.0965 -0.0708 25 TYR B OH 3501 N N . LEU B 26 ? 1.0851 1.0101 0.9901 0.1084 0.0751 -0.0585 26 LEU B N 3502 C CA . LEU B 26 ? 1.1743 1.0778 1.0648 0.1168 0.0755 -0.0528 26 LEU B CA 3503 C C . LEU B 26 ? 1.1892 1.0781 1.0737 0.1097 0.0826 -0.0522 26 LEU B C 3504 O O . LEU B 26 ? 1.1523 1.0433 1.0376 0.0963 0.0864 -0.0518 26 LEU B O 3505 C CB . LEU B 26 ? 1.2181 1.1131 1.0982 0.1163 0.0732 -0.0434 26 LEU B CB 3506 C CG . LEU B 26 ? 1.2828 1.1926 1.1682 0.1213 0.0659 -0.0441 26 LEU B CG 3507 C CD1 . LEU B 26 ? 1.3540 1.2537 1.2272 0.1207 0.0649 -0.0348 26 LEU B CD1 3508 C CD2 . LEU B 26 ? 1.3184 1.2344 1.2074 0.1379 0.0598 -0.0494 26 LEU B CD2 3509 N N . LYS B 27 ? 1.2481 1.1218 1.1265 0.1191 0.0839 -0.0525 27 LYS B N 3510 C CA . LYS B 27 ? 1.3671 1.2253 1.2404 0.1134 0.0901 -0.0528 27 LYS B CA 3511 C C . LYS B 27 ? 1.3959 1.2362 1.2580 0.1066 0.0928 -0.0433 27 LYS B C 3512 O O . LYS B 27 ? 1.4712 1.3008 1.3247 0.1134 0.0910 -0.0357 27 LYS B O 3513 C CB . LYS B 27 ? 1.4455 1.2915 1.3167 0.1263 0.0903 -0.0564 27 LYS B CB 3514 C CG . LYS B 27 ? 1.4943 1.3576 1.3783 0.1313 0.0894 -0.0679 27 LYS B CG 3515 C CD . LYS B 27 ? 1.5394 1.3894 1.4221 0.1382 0.0921 -0.0732 27 LYS B CD 3516 C CE . LYS B 27 ? 1.5482 1.3825 1.4238 0.1554 0.0879 -0.0699 27 LYS B CE 3517 N NZ . LYS B 27 ? 1.5315 1.3833 1.4156 0.1682 0.0810 -0.0751 27 LYS B NZ 3518 N N . GLY B 28 ? 1.4138 1.2516 1.2759 0.0934 0.0972 -0.0440 28 GLY B N 3519 C CA . GLY B 28 ? 1.4829 1.3038 1.3369 0.0864 0.1004 -0.0366 28 GLY B CA 3520 C C . GLY B 28 ? 1.4691 1.2709 1.3200 0.0863 0.1052 -0.0388 28 GLY B C 3521 O O . GLY B 28 ? 1.5921 1.3879 1.4433 0.0964 0.1051 -0.0425 28 GLY B O 3522 N N . SER B 29 ? 1.3818 1.1742 1.2308 0.0752 0.1089 -0.0373 29 SER B N 3523 C CA . SER B 29 ? 1.4095 1.1854 1.2580 0.0733 0.1132 -0.0412 29 SER B CA 3524 C C . SER B 29 ? 1.4256 1.2138 1.2802 0.0703 0.1135 -0.0525 29 SER B C 3525 O O . SER B 29 ? 1.5136 1.3223 1.3723 0.0671 0.1114 -0.0557 29 SER B O 3526 C CB . SER B 29 ? 1.4255 1.1895 1.2723 0.0620 0.1166 -0.0373 29 SER B CB 3527 O OG . SER B 29 ? 1.3704 1.1443 1.2215 0.0504 0.1168 -0.0442 29 SER B OG 3528 N N . GLY B 30 ? 1.3613 1.1367 1.2164 0.0716 0.1164 -0.0586 30 GLY B N 3529 C CA . GLY B 30 ? 1.3066 1.0922 1.1662 0.0688 0.1175 -0.0700 30 GLY B CA 3530 C C . GLY B 30 ? 1.2537 1.0612 1.1181 0.0741 0.1155 -0.0745 30 GLY B C 3531 O O . GLY B 30 ? 1.2435 1.0524 1.1094 0.0852 0.1130 -0.0727 30 GLY B O 3532 N N . SER B 31 ? 1.2115 1.0363 1.0783 0.0659 0.1164 -0.0801 31 SER B N 3533 C CA . SER B 31 ? 1.2306 1.0775 1.1037 0.0687 0.1159 -0.0846 31 SER B CA 3534 C C . SER B 31 ? 1.2162 1.0780 1.0904 0.0619 0.1136 -0.0785 31 SER B C 3535 O O . SER B 31 ? 1.1552 1.0353 1.0335 0.0574 0.1148 -0.0820 31 SER B O 3536 C CB . SER B 31 ? 1.2678 1.1240 1.1424 0.0652 0.1198 -0.0954 31 SER B CB 3537 O OG . SER B 31 ? 1.2499 1.1094 1.1193 0.0527 0.1211 -0.0951 31 SER B OG 3538 N N . LYS B 32 ? 1.2051 1.0590 1.0760 0.0614 0.1107 -0.0693 32 LYS B N 3539 C CA . LYS B 32 ? 1.1930 1.0594 1.0653 0.0557 0.1078 -0.0635 32 LYS B CA 3540 C C . LYS B 32 ? 1.1392 1.0160 1.0176 0.0649 0.1039 -0.0618 32 LYS B C 3541 O O . LYS B 32 ? 1.1050 0.9730 0.9821 0.0759 0.1020 -0.0601 32 LYS B O 3542 C CB . LYS B 32 ? 1.1806 1.0350 1.0468 0.0495 0.1068 -0.0555 32 LYS B CB 3543 C CG . LYS B 32 ? 1.1787 1.0222 1.0404 0.0409 0.1097 -0.0577 32 LYS B CG 3544 C CD . LYS B 32 ? 1.1980 1.0290 1.0561 0.0368 0.1091 -0.0501 32 LYS B CD 3545 C CE . LYS B 32 ? 1.2385 1.0589 1.0946 0.0284 0.1114 -0.0532 32 LYS B CE 3546 N NZ . LYS B 32 ? 1.2876 1.0911 1.1433 0.0333 0.1148 -0.0572 32 LYS B NZ 3547 N N . HIS B 33 ? 1.1072 1.0024 0.9922 0.0604 0.1024 -0.0623 33 HIS B N 3548 C CA . HIS B 33 ? 1.1506 1.0582 1.0439 0.0682 0.0982 -0.0626 33 HIS B CA 3549 C C . HIS B 33 ? 1.1202 1.0362 1.0156 0.0618 0.0947 -0.0571 33 HIS B C 3550 O O . HIS B 33 ? 1.1372 1.0643 1.0364 0.0523 0.0962 -0.0580 33 HIS B O 3551 C CB . HIS B 33 ? 1.1955 1.1201 1.0999 0.0705 0.1004 -0.0716 33 HIS B CB 3552 C CG . HIS B 33 ? 1.2502 1.1686 1.1548 0.0798 0.1025 -0.0782 33 HIS B CG 3553 N ND1 . HIS B 33 ? 1.2573 1.1731 1.1594 0.0757 0.1080 -0.0839 33 HIS B ND1 3554 C CD2 . HIS B 33 ? 1.2974 1.2114 1.2040 0.0937 0.0994 -0.0804 33 HIS B CD2 3555 C CE1 . HIS B 33 ? 1.3057 1.2156 1.2094 0.0864 0.1083 -0.0896 33 HIS B CE1 3556 N NE2 . HIS B 33 ? 1.3751 1.2835 1.2814 0.0976 0.1030 -0.0873 33 HIS B NE2 3557 N N . LEU B 34 ? 1.1410 1.0519 1.0336 0.0678 0.0900 -0.0516 34 LEU B N 3558 C CA . LEU B 34 ? 1.1106 1.0275 1.0045 0.0627 0.0862 -0.0466 34 LEU B CA 3559 C C . LEU B 34 ? 1.0919 1.0258 0.9975 0.0681 0.0813 -0.0499 34 LEU B C 3560 O O . LEU B 34 ? 1.0720 1.0070 0.9797 0.0802 0.0780 -0.0521 34 LEU B O 3561 C CB . LEU B 34 ? 1.0977 1.0000 0.9815 0.0659 0.0843 -0.0390 34 LEU B CB 3562 C CG . LEU B 34 ? 1.1319 1.0155 1.0057 0.0621 0.0890 -0.0358 34 LEU B CG 3563 C CD1 . LEU B 34 ? 1.1548 1.0271 1.0206 0.0641 0.0879 -0.0278 34 LEU B CD1 3564 C CD2 . LEU B 34 ? 1.1139 0.9989 0.9875 0.0488 0.0921 -0.0373 34 LEU B CD2 3565 N N . HIS B 35 ? 1.1074 1.0540 1.0209 0.0592 0.0806 -0.0503 35 HIS B N 3566 C CA . HIS B 35 ? 1.0741 1.0372 1.0012 0.0627 0.0759 -0.0540 35 HIS B CA 3567 C C . HIS B 35 ? 1.0258 0.9864 0.9500 0.0686 0.0690 -0.0498 35 HIS B C 3568 O O . HIS B 35 ? 0.9988 0.9513 0.9150 0.0633 0.0684 -0.0435 35 HIS B O 3569 C CB . HIS B 35 ? 1.0769 1.0523 1.0133 0.0506 0.0778 -0.0549 35 HIS B CB 3570 C CG . HIS B 35 ? 1.0548 1.0465 1.0074 0.0526 0.0732 -0.0589 35 HIS B CG 3571 N ND1 . HIS B 35 ? 1.0670 1.0646 1.0257 0.0440 0.0710 -0.0563 35 HIS B ND1 3572 C CD2 . HIS B 35 ? 1.0640 1.0671 1.0287 0.0624 0.0697 -0.0658 35 HIS B CD2 3573 C CE1 . HIS B 35 ? 1.0240 1.0359 0.9989 0.0478 0.0667 -0.0618 35 HIS B CE1 3574 N NE2 . HIS B 35 ? 1.0426 1.0590 1.0218 0.0590 0.0657 -0.0679 35 HIS B NE2 3575 N N . TYR B 36 ? 1.0502 1.0186 0.9812 0.0803 0.0637 -0.0540 36 TYR B N 3576 C CA . TYR B 36 ? 1.0518 1.0200 0.9799 0.0877 0.0566 -0.0515 36 TYR B CA 3577 C C . TYR B 36 ? 1.0118 0.9992 0.9573 0.0894 0.0506 -0.0581 36 TYR B C 3578 O O . TYR B 36 ? 0.9973 0.9978 0.9574 0.0884 0.0519 -0.0654 36 TYR B O 3579 C CB . TYR B 36 ? 1.1253 1.0829 1.0423 0.1027 0.0545 -0.0501 36 TYR B CB 3580 C CG . TYR B 36 ? 1.1529 1.1212 1.0795 0.1152 0.0505 -0.0584 36 TYR B CG 3581 C CD1 . TYR B 36 ? 1.1576 1.1381 1.0915 0.1251 0.0419 -0.0629 36 TYR B CD1 3582 C CD2 . TYR B 36 ? 1.1497 1.1165 1.0786 0.1179 0.0547 -0.0628 36 TYR B CD2 3583 C CE1 . TYR B 36 ? 1.1532 1.1446 1.0970 0.1372 0.0373 -0.0716 36 TYR B CE1 3584 C CE2 . TYR B 36 ? 1.1708 1.1484 1.1097 0.1300 0.0506 -0.0713 36 TYR B CE2 3585 C CZ . TYR B 36 ? 1.1511 1.1412 1.0977 0.1396 0.0418 -0.0756 36 TYR B CZ 3586 O OH . TYR B 36 ? 1.1169 1.1187 1.0746 0.1520 0.0370 -0.0851 36 TYR B OH 3587 N N . TRP B 37 ? 0.9494 0.9388 0.8942 0.0919 0.0443 -0.0562 37 TRP B N 3588 C CA . TRP B 37 ? 0.9460 0.9523 0.9069 0.0951 0.0370 -0.0630 37 TRP B CA 3589 C C . TRP B 37 ? 0.9991 1.0026 0.9509 0.1079 0.0295 -0.0617 37 TRP B C 3590 O O . TRP B 37 ? 1.0044 0.9998 0.9457 0.1055 0.0287 -0.0554 37 TRP B O 3591 C CB . TRP B 37 ? 0.9125 0.9250 0.8835 0.0810 0.0376 -0.0621 37 TRP B CB 3592 C CG . TRP B 37 ? 0.8762 0.9062 0.8677 0.0815 0.0314 -0.0700 37 TRP B CG 3593 C CD1 . TRP B 37 ? 0.8734 0.9138 0.8729 0.0941 0.0231 -0.0773 37 TRP B CD1 3594 C CD2 . TRP B 37 ? 0.8484 0.8870 0.8553 0.0687 0.0327 -0.0714 37 TRP B CD2 3595 N NE1 . TRP B 37 ? 0.8881 0.9438 0.9091 0.0894 0.0191 -0.0842 37 TRP B NE1 3596 C CE2 . TRP B 37 ? 0.8725 0.9266 0.8984 0.0736 0.0253 -0.0801 37 TRP B CE2 3597 C CE3 . TRP B 37 ? 0.8665 0.9006 0.8725 0.0540 0.0392 -0.0660 37 TRP B CE3 3598 C CZ2 . TRP B 37 ? 0.8939 0.9583 0.9393 0.0632 0.0250 -0.0834 37 TRP B CZ2 3599 C CZ3 . TRP B 37 ? 0.8637 0.9072 0.8867 0.0444 0.0389 -0.0682 37 TRP B CZ3 3600 C CH2 . TRP B 37 ? 0.8866 0.9446 0.9297 0.0486 0.0322 -0.0767 37 TRP B CH2 3601 N N . PHE B 38 ? 1.0492 1.0600 1.0050 0.1221 0.0237 -0.0683 38 PHE B N 3602 C CA . PHE B 38 ? 1.0591 1.0664 1.0029 0.1369 0.0167 -0.0672 38 PHE B CA 3603 C C . PHE B 38 ? 1.0632 1.0891 1.0231 0.1423 0.0068 -0.0764 38 PHE B C 3604 O O . PHE B 38 ? 0.9920 1.0328 0.9700 0.1451 0.0037 -0.0862 38 PHE B O 3605 C CB . PHE B 38 ? 1.1223 1.1230 1.0573 0.1507 0.0169 -0.0679 38 PHE B CB 3606 C CG . PHE B 38 ? 1.2079 1.2012 1.1257 0.1672 0.0110 -0.0649 38 PHE B CG 3607 C CD1 . PHE B 38 ? 1.2372 1.2133 1.1340 0.1669 0.0147 -0.0539 38 PHE B CD1 3608 C CD2 . PHE B 38 ? 1.2251 1.2288 1.1473 0.1836 0.0021 -0.0729 38 PHE B CD2 3609 C CE1 . PHE B 38 ? 1.2710 1.2397 1.1500 0.1823 0.0105 -0.0500 38 PHE B CE1 3610 C CE2 . PHE B 38 ? 1.2770 1.2730 1.1804 0.1999 -0.0032 -0.0695 38 PHE B CE2 3611 C CZ . PHE B 38 ? 1.2709 1.2490 1.1519 0.1991 0.0014 -0.0575 38 PHE B CZ 3612 N N . VAL B 39 ? 1.1318 1.1576 1.0864 0.1435 0.0019 -0.0743 39 VAL B N 3613 C CA . VAL B 39 ? 1.1447 1.1875 1.1138 0.1499 -0.0085 -0.0841 39 VAL B CA 3614 C C . VAL B 39 ? 1.2145 1.2554 1.1678 0.1683 -0.0163 -0.0844 39 VAL B C 3615 O O . VAL B 39 ? 1.2273 1.2569 1.1617 0.1702 -0.0152 -0.0763 39 VAL B O 3616 C CB . VAL B 39 ? 1.1505 1.1984 1.1304 0.1371 -0.0097 -0.0842 39 VAL B CB 3617 C CG1 . VAL B 39 ? 1.1823 1.2380 1.1832 0.1222 -0.0049 -0.0875 39 VAL B CG1 3618 C CG2 . VAL B 39 ? 1.1324 1.1646 1.0937 0.1308 -0.0047 -0.0729 39 VAL B CG2 3619 N N . GLU B 40 ? 1.2471 1.2996 1.2080 0.1822 -0.0241 -0.0940 40 GLU B N 3620 C CA . GLU B 40 ? 1.2397 1.2906 1.1840 0.2018 -0.0321 -0.0947 40 GLU B CA 3621 C C . GLU B 40 ? 1.1720 1.2290 1.1146 0.2040 -0.0393 -0.0969 40 GLU B C 3622 O O . GLU B 40 ? 1.0798 1.1495 1.0431 0.1946 -0.0425 -0.1037 40 GLU B O 3623 C CB . GLU B 40 ? 1.2933 1.3582 1.2493 0.2164 -0.0407 -0.1067 40 GLU B CB 3624 C CG . GLU B 40 ? 1.3198 1.3773 1.2730 0.2190 -0.0348 -0.1048 40 GLU B CG 3625 C CD . GLU B 40 ? 1.3523 1.4190 1.3081 0.2388 -0.0444 -0.1143 40 GLU B CD 3626 O OE1 . GLU B 40 ? 1.3248 1.4092 1.2929 0.2479 -0.0559 -0.1258 40 GLU B OE1 3627 O OE2 . GLU B 40 ? 1.3258 1.3819 1.2717 0.2457 -0.0408 -0.1109 40 GLU B OE2 3628 N N . SER B 41 ? 1.1786 1.2263 1.0965 0.2167 -0.0414 -0.0909 41 SER B N 3629 C CA . SER B 41 ? 1.1752 1.2298 1.0898 0.2216 -0.0488 -0.0941 41 SER B CA 3630 C C . SER B 41 ? 1.1991 1.2765 1.1378 0.2277 -0.0615 -0.1107 41 SER B C 3631 O O . SER B 41 ? 1.2688 1.3549 1.2137 0.2395 -0.0678 -0.1189 41 SER B O 3632 C CB . SER B 41 ? 1.1816 1.2254 1.0656 0.2385 -0.0502 -0.0872 41 SER B CB 3633 O OG . SER B 41 ? 1.1969 1.2519 1.0797 0.2470 -0.0597 -0.0939 41 SER B OG 3634 N N . GLN B 42 ? 1.2038 1.2909 1.1570 0.2199 -0.0656 -0.1163 42 GLN B N 3635 C CA . GLN B 42 ? 1.2289 1.3374 1.2065 0.2250 -0.0781 -0.1328 42 GLN B CA 3636 C C . GLN B 42 ? 1.2727 1.3878 1.2362 0.2477 -0.0898 -0.1395 42 GLN B C 3637 O O . GLN B 42 ? 1.2382 1.3715 1.2200 0.2560 -0.1016 -0.1545 42 GLN B O 3638 C CB . GLN B 42 ? 1.2321 1.3467 1.2272 0.2113 -0.0796 -0.1364 42 GLN B CB 3639 C CG . GLN B 42 ? 1.1943 1.3034 1.2039 0.1894 -0.0692 -0.1306 42 GLN B CG 3640 C CD . GLN B 42 ? 1.1720 1.2904 1.2056 0.1777 -0.0733 -0.1376 42 GLN B CD 3641 O OE1 . GLN B 42 ? 1.1616 1.2963 1.2160 0.1825 -0.0834 -0.1515 42 GLN B OE1 3642 N NE2 . GLN B 42 ? 1.1550 1.2626 1.1860 0.1627 -0.0658 -0.1284 42 GLN B NE2 3643 N N . LYS B 43 ? 1.3298 1.4300 1.2606 0.2574 -0.0865 -0.1283 43 LYS B N 3644 C CA . LYS B 43 ? 1.3652 1.4689 1.2764 0.2794 -0.0963 -0.1320 43 LYS B CA 3645 C C . LYS B 43 ? 1.3771 1.4637 1.2585 0.2917 -0.0909 -0.1203 43 LYS B C 3646 O O . LYS B 43 ? 1.3541 1.4221 1.2109 0.2891 -0.0808 -0.1054 43 LYS B O 3647 C CB . LYS B 43 ? 1.3972 1.4997 1.2966 0.2790 -0.0972 -0.1297 43 LYS B CB 3648 C CG . LYS B 43 ? 1.5349 1.6348 1.4039 0.3000 -0.1025 -0.1277 43 LYS B CG 3649 C CD . LYS B 43 ? 1.6013 1.7192 1.4764 0.3195 -0.1188 -0.1438 43 LYS B CD 3650 C CE . LYS B 43 ? 1.6375 1.7534 1.4808 0.3396 -0.1241 -0.1419 43 LYS B CE 3651 N NZ . LYS B 43 ? 1.7190 1.8518 1.5648 0.3609 -0.1407 -0.1575 43 LYS B NZ 3652 N N . ASP B 44 ? 1.3772 1.4700 1.2629 0.3044 -0.0976 -0.1274 44 ASP B N 3653 C CA . ASP B 44 ? 1.4266 1.5040 1.2853 0.3193 -0.0951 -0.1183 44 ASP B CA 3654 C C . ASP B 44 ? 1.4185 1.4732 1.2654 0.3068 -0.0793 -0.1020 44 ASP B C 3655 O O . ASP B 44 ? 1.4192 1.4553 1.2393 0.3072 -0.0708 -0.0877 44 ASP B O 3656 C CB . ASP B 44 ? 1.4948 1.5665 1.3212 0.3384 -0.1001 -0.1139 44 ASP B CB 3657 C CG . ASP B 44 ? 1.5806 1.6412 1.3827 0.3589 -0.1025 -0.1089 44 ASP B CG 3658 O OD1 . ASP B 44 ? 1.5672 1.6311 1.3827 0.3618 -0.1051 -0.1143 44 ASP B OD1 3659 O OD2 . ASP B 44 ? 1.6320 1.6802 1.4012 0.3724 -0.1016 -0.0994 44 ASP B OD2 3660 N N . PRO B 45 ? 1.4187 1.4755 1.2865 0.2959 -0.0750 -0.1047 45 PRO B N 3661 C CA . PRO B 45 ? 1.3955 1.4326 1.2550 0.2856 -0.0614 -0.0920 45 PRO B CA 3662 C C . PRO B 45 ? 1.4955 1.5108 1.3220 0.3001 -0.0577 -0.0796 45 PRO B C 3663 O O . PRO B 45 ? 1.6309 1.6262 1.4402 0.2921 -0.0459 -0.0655 45 PRO B O 3664 C CB . PRO B 45 ? 1.3774 1.4260 1.2635 0.2811 -0.0627 -0.1020 45 PRO B CB 3665 C CG . PRO B 45 ? 1.3396 1.4130 1.2549 0.2767 -0.0717 -0.1172 45 PRO B CG 3666 C CD . PRO B 45 ? 1.3748 1.4544 1.2776 0.2919 -0.0826 -0.1212 45 PRO B CD 3667 N N . GLU B 46 ? 1.5655 1.5845 1.3836 0.3214 -0.0677 -0.0851 46 GLU B N 3668 C CA . GLU B 46 ? 1.6285 1.6258 1.4155 0.3368 -0.0649 -0.0735 46 GLU B CA 3669 C C . GLU B 46 ? 1.6135 1.5931 1.3686 0.3397 -0.0583 -0.0587 46 GLU B C 3670 O O . GLU B 46 ? 1.5388 1.4953 1.2680 0.3466 -0.0513 -0.0453 46 GLU B O 3671 C CB . GLU B 46 ? 1.7265 1.7340 1.5107 0.3610 -0.0794 -0.0837 46 GLU B CB 3672 C CG . GLU B 46 ? 1.8110 1.7972 1.5715 0.3760 -0.0773 -0.0743 46 GLU B CG 3673 C CD . GLU B 46 ? 1.8930 1.8855 1.6398 0.4033 -0.0922 -0.0811 46 GLU B CD 3674 O OE1 . GLU B 46 ? 1.9720 1.9725 1.7069 0.4134 -0.0998 -0.0837 46 GLU B OE1 3675 O OE2 . GLU B 46 ? 1.9076 1.8971 1.6552 0.4155 -0.0966 -0.0843 46 GLU B OE2 3676 N N . ASN B 47 ? 1.6639 1.6542 1.4211 0.3350 -0.0606 -0.0615 47 ASN B N 3677 C CA . ASN B 47 ? 1.6835 1.6605 1.4128 0.3369 -0.0540 -0.0489 47 ASN B CA 3678 C C . ASN B 47 ? 1.5739 1.5532 1.3136 0.3160 -0.0459 -0.0461 47 ASN B C 3679 O O . ASN B 47 ? 1.5942 1.5665 1.3149 0.3165 -0.0408 -0.0379 47 ASN B O 3680 C CB . ASN B 47 ? 1.7591 1.7460 1.4718 0.3586 -0.0662 -0.0546 47 ASN B CB 3681 C CG . ASN B 47 ? 1.8590 1.8392 1.5538 0.3816 -0.0734 -0.0542 47 ASN B CG 3682 O OD1 . ASN B 47 ? 1.9121 1.8685 1.5795 0.3883 -0.0653 -0.0393 47 ASN B OD1 3683 N ND2 . ASN B 47 ? 1.8615 1.8623 1.5728 0.3936 -0.0886 -0.0708 47 ASN B ND2 3684 N N . SER B 48 ? 1.4683 1.4576 1.2376 0.2983 -0.0447 -0.0531 48 SER B N 3685 C CA . SER B 48 ? 1.3697 1.3574 1.1481 0.2776 -0.0360 -0.0487 48 SER B CA 3686 C C . SER B 48 ? 1.3368 1.3029 1.1078 0.2655 -0.0215 -0.0354 48 SER B C 3687 O O . SER B 48 ? 1.3242 1.2826 1.0963 0.2677 -0.0197 -0.0343 48 SER B O 3688 C CB . SER B 48 ? 1.3052 1.3127 1.1172 0.2647 -0.0416 -0.0618 48 SER B CB 3689 O OG . SER B 48 ? 1.3148 1.3404 1.1341 0.2719 -0.0530 -0.0729 48 SER B OG 3690 N N . PRO B 49 ? 1.3418 1.2982 1.1056 0.2530 -0.0115 -0.0260 49 PRO B N 3691 C CA . PRO B 49 ? 1.3594 1.2955 1.1169 0.2415 0.0018 -0.0142 49 PRO B CA 3692 C C . PRO B 49 ? 1.3173 1.2560 1.0981 0.2258 0.0046 -0.0185 49 PRO B C 3693 O O . PRO B 49 ? 1.2062 1.1627 1.0094 0.2218 -0.0027 -0.0299 49 PRO B O 3694 C CB . PRO B 49 ? 1.3718 1.3027 1.1216 0.2313 0.0100 -0.0064 49 PRO B CB 3695 C CG . PRO B 49 ? 1.4079 1.3516 1.1501 0.2432 0.0018 -0.0111 49 PRO B CG 3696 C CD . PRO B 49 ? 1.3718 1.3352 1.1321 0.2504 -0.0121 -0.0260 49 PRO B CD 3697 N N . VAL B 50 ? 1.3158 1.2363 1.0907 0.2169 0.0157 -0.0092 50 VAL B N 3698 C CA . VAL B 50 ? 1.3243 1.2445 1.1168 0.2021 0.0200 -0.0117 50 VAL B CA 3699 C C . VAL B 50 ? 1.3224 1.2371 1.1178 0.1840 0.0288 -0.0059 50 VAL B C 3700 O O . VAL B 50 ? 1.2603 1.1584 1.0406 0.1816 0.0377 0.0042 50 VAL B O 3701 C CB . VAL B 50 ? 1.3521 1.2562 1.1374 0.2069 0.0247 -0.0076 50 VAL B CB 3702 C CG1 . VAL B 50 ? 1.3504 1.2528 1.1514 0.1909 0.0308 -0.0095 50 VAL B CG1 3703 C CG2 . VAL B 50 ? 1.4044 1.3166 1.1909 0.2244 0.0149 -0.0153 50 VAL B CG2 3704 N N . VAL B 51 ? 1.3157 1.2444 1.1310 0.1715 0.0261 -0.0128 51 VAL B N 3705 C CA . VAL B 51 ? 1.2863 1.2126 1.1065 0.1549 0.0322 -0.0092 51 VAL B CA 3706 C C . VAL B 51 ? 1.2100 1.1345 1.0436 0.1410 0.0366 -0.0109 51 VAL B C 3707 O O . VAL B 51 ? 1.2611 1.1975 1.1103 0.1390 0.0320 -0.0189 51 VAL B O 3708 C CB . VAL B 51 ? 1.2948 1.2377 1.1258 0.1519 0.0251 -0.0153 51 VAL B CB 3709 C CG1 . VAL B 51 ? 1.3167 1.2593 1.1568 0.1345 0.0296 -0.0135 51 VAL B CG1 3710 C CG2 . VAL B 51 ? 1.3250 1.2687 1.1407 0.1643 0.0223 -0.0130 51 VAL B CG2 3711 N N . LEU B 52 ? 1.1173 1.0273 0.9448 0.1316 0.0458 -0.0038 52 LEU B N 3712 C CA . LEU B 52 ? 1.0402 0.9487 0.8786 0.1176 0.0501 -0.0054 52 LEU B CA 3713 C C . LEU B 52 ? 1.0381 0.9534 0.8846 0.1048 0.0498 -0.0058 52 LEU B C 3714 O O . LEU B 52 ? 1.0264 0.9375 0.8656 0.1032 0.0523 -0.0009 52 LEU B O 3715 C CB . LEU B 52 ? 1.0678 0.9569 0.8961 0.1146 0.0594 0.0012 52 LEU B CB 3716 C CG . LEU B 52 ? 1.0906 0.9767 0.9277 0.1001 0.0643 -0.0002 52 LEU B CG 3717 C CD1 . LEU B 52 ? 1.0952 0.9882 0.9422 0.1012 0.0620 -0.0073 52 LEU B CD1 3718 C CD2 . LEU B 52 ? 1.1088 0.9754 0.9361 0.0963 0.0734 0.0065 52 LEU B CD2 3719 N N . TRP B 53 ? 0.9995 0.9254 0.8611 0.0959 0.0470 -0.0116 53 TRP B N 3720 C CA . TRP B 53 ? 0.9414 0.8719 0.8101 0.0837 0.0465 -0.0116 53 TRP B CA 3721 C C . TRP B 53 ? 0.9062 0.8314 0.7788 0.0713 0.0518 -0.0111 53 TRP B C 3722 O O . TRP B 53 ? 0.9165 0.8456 0.7960 0.0698 0.0518 -0.0151 53 TRP B O 3723 C CB . TRP B 53 ? 0.9099 0.8567 0.7924 0.0835 0.0381 -0.0182 53 TRP B CB 3724 C CG . TRP B 53 ? 0.8841 0.8339 0.7740 0.0710 0.0374 -0.0180 53 TRP B CG 3725 C CD1 . TRP B 53 ? 0.8668 0.8197 0.7665 0.0603 0.0379 -0.0199 53 TRP B CD1 3726 C CD2 . TRP B 53 ? 0.9123 0.8616 0.7992 0.0686 0.0363 -0.0154 53 TRP B CD2 3727 N NE1 . TRP B 53 ? 0.8516 0.8052 0.7542 0.0517 0.0364 -0.0183 53 TRP B NE1 3728 C CE2 . TRP B 53 ? 0.9118 0.8638 0.8077 0.0566 0.0352 -0.0161 53 TRP B CE2 3729 C CE3 . TRP B 53 ? 0.9298 0.8771 0.8071 0.0757 0.0364 -0.0126 53 TRP B CE3 3730 C CZ2 . TRP B 53 ? 0.9205 0.8734 0.8171 0.0520 0.0334 -0.0148 53 TRP B CZ2 3731 C CZ3 . TRP B 53 ? 0.9234 0.8727 0.8021 0.0706 0.0354 -0.0115 53 TRP B CZ3 3732 C CH2 . TRP B 53 ? 0.9278 0.8799 0.8167 0.0590 0.0335 -0.0129 53 TRP B CH2 3733 N N . LEU B 54 ? 0.9011 0.8187 0.7697 0.0627 0.0562 -0.0068 54 LEU B N 3734 C CA . LEU B 54 ? 0.8827 0.7962 0.7544 0.0508 0.0601 -0.0071 54 LEU B CA 3735 C C . LEU B 54 ? 0.8629 0.7818 0.7402 0.0411 0.0574 -0.0071 54 LEU B C 3736 O O . LEU B 54 ? 0.8345 0.7516 0.7088 0.0406 0.0574 -0.0044 54 LEU B O 3737 C CB . LEU B 54 ? 0.8937 0.7920 0.7564 0.0489 0.0678 -0.0029 54 LEU B CB 3738 C CG . LEU B 54 ? 0.9363 0.8243 0.7922 0.0569 0.0719 -0.0019 54 LEU B CG 3739 C CD1 . LEU B 54 ? 0.9312 0.8031 0.7800 0.0528 0.0795 0.0024 54 LEU B CD1 3740 C CD2 . LEU B 54 ? 0.9435 0.8362 0.8057 0.0563 0.0713 -0.0074 54 LEU B CD2 3741 N N . ASN B 55 ? 0.8693 0.7945 0.7545 0.0338 0.0552 -0.0102 55 ASN B N 3742 C CA . ASN B 55 ? 0.8092 0.7362 0.6978 0.0240 0.0532 -0.0096 55 ASN B CA 3743 C C . ASN B 55 ? 0.8239 0.7412 0.7069 0.0169 0.0586 -0.0080 55 ASN B C 3744 O O . ASN B 55 ? 0.8220 0.7320 0.7003 0.0185 0.0638 -0.0080 55 ASN B O 3745 C CB . ASN B 55 ? 0.7948 0.7305 0.6923 0.0191 0.0493 -0.0124 55 ASN B CB 3746 C CG . ASN B 55 ? 0.8012 0.7465 0.7070 0.0228 0.0423 -0.0143 55 ASN B CG 3747 O OD1 . ASN B 55 ? 0.8421 0.7944 0.7541 0.0285 0.0400 -0.0177 55 ASN B OD1 3748 N ND2 . ASN B 55 ? 0.8044 0.7507 0.7114 0.0202 0.0384 -0.0132 55 ASN B ND2 3749 N N . GLY B 56 ? 0.8498 0.7670 0.7339 0.0096 0.0569 -0.0072 56 GLY B N 3750 C CA . GLY B 56 ? 0.8867 0.7959 0.7670 0.0031 0.0611 -0.0068 56 GLY B CA 3751 C C . GLY B 56 ? 0.8975 0.8071 0.7778 -0.0043 0.0608 -0.0090 56 GLY B C 3752 O O . GLY B 56 ? 0.8962 0.8064 0.7757 -0.0033 0.0629 -0.0106 56 GLY B O 3753 N N . GLY B 57 ? 0.8930 0.8027 0.7738 -0.0112 0.0582 -0.0093 57 GLY B N 3754 C CA . GLY B 57 ? 0.8693 0.7790 0.7477 -0.0181 0.0573 -0.0110 57 GLY B CA 3755 C C . GLY B 57 ? 0.8679 0.7723 0.7442 -0.0232 0.0582 -0.0128 57 GLY B C 3756 O O . GLY B 57 ? 0.8234 0.7302 0.7021 -0.0266 0.0536 -0.0129 57 GLY B O 3757 N N . PRO B 58 ? 0.8807 0.7778 0.7536 -0.0238 0.0639 -0.0150 58 PRO B N 3758 C CA . PRO B 58 ? 0.9076 0.8012 0.7775 -0.0199 0.0689 -0.0160 58 PRO B CA 3759 C C . PRO B 58 ? 0.9152 0.8137 0.7824 -0.0220 0.0682 -0.0177 58 PRO B C 3760 O O . PRO B 58 ? 0.9401 0.8402 0.8042 -0.0277 0.0654 -0.0189 58 PRO B O 3761 C CB . PRO B 58 ? 0.9218 0.8057 0.7897 -0.0220 0.0738 -0.0189 58 PRO B CB 3762 C CG . PRO B 58 ? 0.9244 0.8070 0.7960 -0.0261 0.0723 -0.0188 58 PRO B CG 3763 C CD . PRO B 58 ? 0.8740 0.7657 0.7476 -0.0284 0.0653 -0.0176 58 PRO B CD 3764 N N . GLY B 59 ? 0.8623 0.7634 0.7304 -0.0173 0.0706 -0.0178 59 GLY B N 3765 C CA . GLY B 59 ? 0.8365 0.7434 0.7032 -0.0193 0.0712 -0.0192 59 GLY B CA 3766 C C . GLY B 59 ? 0.8583 0.7743 0.7314 -0.0172 0.0686 -0.0171 59 GLY B C 3767 O O . GLY B 59 ? 0.8923 0.8138 0.7662 -0.0186 0.0705 -0.0181 59 GLY B O 3768 N N . CYS B 60 ? 0.8827 0.8005 0.7609 -0.0139 0.0645 -0.0146 60 CYS B N 3769 C CA . CYS B 60 ? 0.8807 0.8072 0.7667 -0.0119 0.0609 -0.0136 60 CYS B CA 3770 C C . CYS B 60 ? 0.8686 0.7988 0.7599 -0.0032 0.0618 -0.0154 60 CYS B C 3771 O O . CYS B 60 ? 0.8730 0.7978 0.7611 0.0026 0.0641 -0.0156 60 CYS B O 3772 C CB . CYS B 60 ? 0.8930 0.8208 0.7820 -0.0132 0.0546 -0.0111 60 CYS B CB 3773 S SG . CYS B 60 ? 0.9864 0.9109 0.8700 -0.0222 0.0516 -0.0095 60 CYS B SG 3774 N N . SER B 61 ? 0.8747 0.8139 0.7745 -0.0023 0.0598 -0.0166 61 SER B N 3775 C CA . SER B 61 ? 0.8464 0.7916 0.7528 0.0055 0.0604 -0.0198 61 SER B CA 3776 C C . SER B 61 ? 0.8135 0.7617 0.7241 0.0131 0.0550 -0.0199 61 SER B C 3777 O O . SER B 61 ? 0.7456 0.6969 0.6604 0.0109 0.0499 -0.0187 61 SER B O 3778 C CB . SER B 61 ? 0.8579 0.8132 0.7740 0.0021 0.0611 -0.0222 61 SER B CB 3779 O OG . SER B 61 ? 0.8664 0.8294 0.7912 0.0101 0.0608 -0.0268 61 SER B OG 3780 N N . SER B 62 ? 0.8521 0.7998 0.7616 0.0227 0.0558 -0.0217 62 SER B N 3781 C CA . SER B 62 ? 0.8715 0.8234 0.7839 0.0321 0.0505 -0.0227 62 SER B CA 3782 C C . SER B 62 ? 0.8944 0.8598 0.8211 0.0344 0.0457 -0.0277 62 SER B C 3783 O O . SER B 62 ? 0.8780 0.8488 0.8085 0.0423 0.0401 -0.0298 62 SER B O 3784 C CB . SER B 62 ? 0.8953 0.8406 0.7996 0.0425 0.0528 -0.0224 62 SER B CB 3785 O OG . SER B 62 ? 0.9393 0.8715 0.8323 0.0402 0.0575 -0.0178 62 SER B OG 3786 N N . LEU B 63 ? 0.9095 0.8808 0.8444 0.0277 0.0481 -0.0299 63 LEU B N 3787 C CA . LEU B 63 ? 0.9211 0.9052 0.8721 0.0278 0.0442 -0.0347 63 LEU B CA 3788 C C . LEU B 63 ? 0.9347 0.9203 0.8912 0.0214 0.0394 -0.0328 63 LEU B C 3789 O O . LEU B 63 ? 0.9368 0.9317 0.9072 0.0225 0.0345 -0.0368 63 LEU B O 3790 C CB . LEU B 63 ? 0.9225 0.9130 0.8815 0.0229 0.0498 -0.0378 63 LEU B CB 3791 C CG . LEU B 63 ? 0.9302 0.9210 0.8864 0.0303 0.0539 -0.0413 63 LEU B CG 3792 C CD1 . LEU B 63 ? 0.9493 0.9504 0.9173 0.0260 0.0588 -0.0460 63 LEU B CD1 3793 C CD2 . LEU B 63 ? 0.8857 0.8791 0.8430 0.0441 0.0484 -0.0449 63 LEU B CD2 3794 N N . ASP B 64 ? 0.9858 0.9623 0.9326 0.0148 0.0404 -0.0272 64 ASP B N 3795 C CA . ASP B 64 ? 1.0487 1.0248 0.9987 0.0109 0.0347 -0.0253 64 ASP B CA 3796 C C . ASP B 64 ? 1.0269 1.0066 0.9790 0.0208 0.0282 -0.0281 64 ASP B C 3797 O O . ASP B 64 ? 1.0420 1.0282 1.0052 0.0215 0.0219 -0.0311 64 ASP B O 3798 C CB . ASP B 64 ? 1.1113 1.0773 1.0496 0.0043 0.0362 -0.0198 64 ASP B CB 3799 C CG . ASP B 64 ? 1.1788 1.1446 1.1214 0.0000 0.0300 -0.0180 64 ASP B CG 3800 O OD1 . ASP B 64 ? 1.1765 1.1461 1.1291 -0.0047 0.0281 -0.0185 64 ASP B OD1 3801 O OD2 . ASP B 64 ? 1.3002 1.2617 1.2369 0.0013 0.0274 -0.0163 64 ASP B OD2 3802 N N . GLY B 65 ? 1.0242 0.9993 0.9654 0.0284 0.0300 -0.0271 65 GLY B N 3803 C CA . GLY B 65 ? 1.0134 0.9913 0.9530 0.0391 0.0250 -0.0291 65 GLY B CA 3804 C C . GLY B 65 ? 1.0079 0.9978 0.9607 0.0457 0.0194 -0.0361 65 GLY B C 3805 O O . GLY B 65 ? 0.9981 0.9943 0.9581 0.0490 0.0123 -0.0396 65 GLY B O 3806 N N . LEU B 66 ? 1.0098 1.0036 0.9671 0.0476 0.0223 -0.0392 66 LEU B N 3807 C CA . LEU B 66 ? 0.9658 0.9725 0.9382 0.0537 0.0171 -0.0471 66 LEU B CA 3808 C C . LEU B 66 ? 0.9075 0.9216 0.8971 0.0457 0.0130 -0.0502 66 LEU B C 3809 O O . LEU B 66 ? 0.8858 0.9074 0.8847 0.0508 0.0052 -0.0556 66 LEU B O 3810 C CB . LEU B 66 ? 0.9577 0.9679 0.9338 0.0556 0.0218 -0.0502 66 LEU B CB 3811 C CG . LEU B 66 ? 0.9825 1.0061 0.9715 0.0661 0.0158 -0.0593 66 LEU B CG 3812 C CD1 . LEU B 66 ? 1.0430 1.0677 1.0306 0.0716 0.0202 -0.0617 66 LEU B CD1 3813 C CD2 . LEU B 66 ? 1.0329 1.0691 1.0445 0.0598 0.0121 -0.0656 66 LEU B CD2 3814 N N . LEU B 67 ? 0.8923 0.9035 0.8853 0.0335 0.0182 -0.0468 67 LEU B N 3815 C CA . LEU B 67 ? 0.8835 0.9009 0.8941 0.0252 0.0163 -0.0492 67 LEU B CA 3816 C C . LEU B 67 ? 0.9126 0.9254 0.9244 0.0203 0.0111 -0.0465 67 LEU B C 3817 O O . LEU B 67 ? 0.8907 0.9085 0.9188 0.0156 0.0075 -0.0496 67 LEU B O 3818 C CB . LEU B 67 ? 0.8807 0.8967 0.8932 0.0146 0.0248 -0.0461 67 LEU B CB 3819 C CG . LEU B 67 ? 0.8959 0.9212 0.9164 0.0182 0.0291 -0.0518 67 LEU B CG 3820 C CD1 . LEU B 67 ? 0.8925 0.9145 0.9084 0.0089 0.0390 -0.0477 67 LEU B CD1 3821 C CD2 . LEU B 67 ? 0.9042 0.9439 0.9485 0.0196 0.0246 -0.0605 67 LEU B CD2 3822 N N . THR B 68 ? 0.8911 0.8948 0.8875 0.0213 0.0106 -0.0413 68 THR B N 3823 C CA . THR B 68 ? 0.8447 0.8445 0.8422 0.0175 0.0053 -0.0392 68 THR B CA 3824 C C . THR B 68 ? 0.8194 0.8185 0.8091 0.0262 0.0001 -0.0402 68 THR B C 3825 O O . THR B 68 ? 0.8224 0.8198 0.8146 0.0244 -0.0049 -0.0399 68 THR B O 3826 C CB . THR B 68 ? 0.8863 0.8756 0.8746 0.0070 0.0098 -0.0314 68 THR B CB 3827 O OG1 . THR B 68 ? 0.9272 0.9095 0.8986 0.0093 0.0132 -0.0274 68 THR B OG1 3828 C CG2 . THR B 68 ? 0.8768 0.8660 0.8683 -0.0012 0.0168 -0.0293 68 THR B CG2 3829 N N . GLU B 69 ? 0.8416 0.8417 0.8217 0.0359 0.0016 -0.0412 69 GLU B N 3830 C CA . GLU B 69 ? 0.8824 0.8814 0.8527 0.0441 -0.0015 -0.0411 69 GLU B CA 3831 C C . GLU B 69 ? 0.9412 0.9494 0.9139 0.0574 -0.0070 -0.0479 69 GLU B C 3832 O O . GLU B 69 ? 1.0513 1.0654 1.0303 0.0618 -0.0145 -0.0528 69 GLU B O 3833 C CB . GLU B 69 ? 0.8819 0.8713 0.8346 0.0442 0.0057 -0.0345 69 GLU B CB 3834 C CG . GLU B 69 ? 0.8465 0.8273 0.7951 0.0325 0.0105 -0.0286 69 GLU B CG 3835 C CD . GLU B 69 ? 0.8456 0.8179 0.7793 0.0331 0.0162 -0.0237 69 GLU B CD 3836 O OE1 . GLU B 69 ? 0.7921 0.7642 0.7215 0.0367 0.0144 -0.0231 69 GLU B OE1 3837 O OE2 . GLU B 69 ? 0.8686 0.8348 0.7957 0.0302 0.0228 -0.0209 69 GLU B OE2 3838 N N . HIS B 70 ? 0.8869 0.8960 0.8537 0.0648 -0.0041 -0.0486 70 HIS B N 3839 C CA . HIS B 70 ? 0.9030 0.9200 0.8686 0.0791 -0.0098 -0.0547 70 HIS B CA 3840 C C . HIS B 70 ? 0.9258 0.9489 0.8962 0.0858 -0.0100 -0.0594 70 HIS B C 3841 O O . HIS B 70 ? 0.9508 0.9770 0.9138 0.0991 -0.0130 -0.0623 70 HIS B O 3842 C CB . HIS B 70 ? 0.9161 0.9263 0.8617 0.0871 -0.0073 -0.0496 70 HIS B CB 3843 C CG . HIS B 70 ? 0.8678 0.8660 0.7988 0.0847 0.0022 -0.0415 70 HIS B CG 3844 N ND1 . HIS B 70 ? 0.8685 0.8570 0.7852 0.0831 0.0076 -0.0345 70 HIS B ND1 3845 C CD2 . HIS B 70 ? 0.8352 0.8297 0.7650 0.0835 0.0073 -0.0401 70 HIS B CD2 3846 C CE1 . HIS B 70 ? 0.8667 0.8453 0.7743 0.0809 0.0155 -0.0291 70 HIS B CE1 3847 N NE2 . HIS B 70 ? 0.8302 0.8120 0.7448 0.0815 0.0153 -0.0324 70 HIS B NE2 3848 N N . GLY B 71 ? 0.9586 0.9837 0.9410 0.0772 -0.0067 -0.0605 71 GLY B N 3849 C CA . GLY B 71 ? 0.9748 1.0081 0.9655 0.0830 -0.0071 -0.0664 71 GLY B CA 3850 C C . GLY B 71 ? 1.0262 1.0740 1.0343 0.0894 -0.0170 -0.0772 71 GLY B C 3851 O O . GLY B 71 ? 0.9854 1.0357 1.0003 0.0869 -0.0225 -0.0795 71 GLY B O 3852 N N . PRO B 72 ? 1.0981 1.1560 1.1146 0.0981 -0.0200 -0.0849 72 PRO B N 3853 C CA . PRO B 72 ? 1.0742 1.1479 1.1106 0.1043 -0.0299 -0.0973 72 PRO B CA 3854 C C . PRO B 72 ? 1.0582 1.1382 1.1189 0.0910 -0.0307 -0.1013 72 PRO B C 3855 O O . PRO B 72 ? 1.1121 1.2027 1.1898 0.0936 -0.0394 -0.1107 72 PRO B O 3856 C CB . PRO B 72 ? 1.1245 1.2065 1.1654 0.1137 -0.0304 -0.1034 72 PRO B CB 3857 C CG . PRO B 72 ? 1.1324 1.2034 1.1618 0.1076 -0.0193 -0.0946 72 PRO B CG 3858 C CD . PRO B 72 ? 1.1301 1.1849 1.1383 0.1030 -0.0144 -0.0831 72 PRO B CD 3859 N N . PHE B 73 ? 1.0448 1.1180 1.1073 0.0769 -0.0216 -0.0944 73 PHE B N 3860 C CA . PHE B 73 ? 1.0331 1.1093 1.1159 0.0634 -0.0208 -0.0958 73 PHE B CA 3861 C C . PHE B 73 ? 0.9871 1.0492 1.0588 0.0501 -0.0123 -0.0840 73 PHE B C 3862 O O . PHE B 73 ? 0.9871 1.0406 1.0416 0.0493 -0.0051 -0.0768 73 PHE B O 3863 C CB . PHE B 73 ? 1.0023 1.0914 1.1074 0.0605 -0.0185 -0.1035 73 PHE B CB 3864 C CG . PHE B 73 ? 0.9895 1.0800 1.0862 0.0664 -0.0129 -0.1031 73 PHE B CG 3865 C CD1 . PHE B 73 ? 0.9613 1.0409 1.0436 0.0590 -0.0024 -0.0935 73 PHE B CD1 3866 C CD2 . PHE B 73 ? 0.9797 1.0823 1.0826 0.0803 -0.0190 -0.1131 73 PHE B CD2 3867 C CE1 . PHE B 73 ? 0.9531 1.0335 1.0284 0.0649 0.0023 -0.0939 73 PHE B CE1 3868 C CE2 . PHE B 73 ? 0.9681 1.0712 1.0635 0.0866 -0.0144 -0.1129 73 PHE B CE2 3869 C CZ . PHE B 73 ? 0.9573 1.0490 1.0392 0.0787 -0.0035 -0.1033 73 PHE B CZ 3870 N N . LEU B 74 ? 0.9162 0.9755 0.9977 0.0404 -0.0140 -0.0825 74 LEU B N 3871 C CA . LEU B 74 ? 0.9098 0.9557 0.9806 0.0287 -0.0079 -0.0719 74 LEU B CA 3872 C C . LEU B 74 ? 0.9041 0.9511 0.9913 0.0154 -0.0027 -0.0707 74 LEU B C 3873 O O . LEU B 74 ? 0.8925 0.9467 1.0012 0.0128 -0.0072 -0.0772 74 LEU B O 3874 C CB . LEU B 74 ? 0.8686 0.9076 0.9337 0.0291 -0.0143 -0.0695 74 LEU B CB 3875 C CG . LEU B 74 ? 0.8780 0.9183 0.9312 0.0424 -0.0206 -0.0722 74 LEU B CG 3876 C CD1 . LEU B 74 ? 0.9039 0.9397 0.9569 0.0410 -0.0268 -0.0714 74 LEU B CD1 3877 C CD2 . LEU B 74 ? 0.8787 0.9115 0.9088 0.0466 -0.0142 -0.0654 74 LEU B CD2 3878 N N . VAL B 75 ? 0.8283 0.8675 0.9048 0.0069 0.0067 -0.0624 75 VAL B N 3879 C CA . VAL B 75 ? 0.8541 0.8914 0.9406 -0.0063 0.0130 -0.0586 75 VAL B CA 3880 C C . VAL B 75 ? 0.8913 0.9210 0.9832 -0.0128 0.0079 -0.0554 75 VAL B C 3881 O O . VAL B 75 ? 0.9183 0.9389 0.9964 -0.0105 0.0035 -0.0512 75 VAL B O 3882 C CB . VAL B 75 ? 0.8685 0.8973 0.9373 -0.0129 0.0235 -0.0497 75 VAL B CB 3883 C CG1 . VAL B 75 ? 0.8417 0.8560 0.8898 -0.0151 0.0224 -0.0409 75 VAL B CG1 3884 C CG2 . VAL B 75 ? 0.8684 0.8988 0.9479 -0.0249 0.0319 -0.0471 75 VAL B CG2 3885 N N . GLN B 76 ? 0.9132 0.9463 1.0258 -0.0212 0.0090 -0.0574 76 GLN B N 3886 C CA . GLN B 76 ? 0.9078 0.9326 1.0286 -0.0281 0.0045 -0.0545 76 GLN B CA 3887 C C . GLN B 76 ? 0.9032 0.9151 1.0143 -0.0407 0.0131 -0.0425 76 GLN B C 3888 O O . GLN B 76 ? 0.9288 0.9415 1.0320 -0.0447 0.0229 -0.0385 76 GLN B O 3889 C CB . GLN B 76 ? 0.9268 0.9620 1.0777 -0.0299 0.0005 -0.0642 76 GLN B CB 3890 C CG . GLN B 76 ? 0.9349 0.9849 1.0965 -0.0169 -0.0080 -0.0774 76 GLN B CG 3891 C CD . GLN B 76 ? 0.9519 0.9992 1.1063 -0.0072 -0.0193 -0.0805 76 GLN B CD 3892 O OE1 . GLN B 76 ? 1.0039 1.0518 1.1740 -0.0074 -0.0274 -0.0860 76 GLN B OE1 3893 N NE2 . GLN B 76 ? 0.9476 0.9927 1.0794 0.0016 -0.0197 -0.0778 76 GLN B NE2 3894 N N . PRO B 77 ? 0.8848 0.8849 0.9960 -0.0463 0.0092 -0.0371 77 PRO B N 3895 C CA . PRO B 77 ? 0.9023 0.8879 0.9984 -0.0559 0.0156 -0.0246 77 PRO B CA 3896 C C . PRO B 77 ? 1.0207 1.0066 1.1218 -0.0667 0.0276 -0.0197 77 PRO B C 3897 O O . PRO B 77 ? 1.0271 1.0031 1.1101 -0.0726 0.0345 -0.0097 77 PRO B O 3898 C CB . PRO B 77 ? 0.8923 0.8670 0.9942 -0.0584 0.0074 -0.0222 77 PRO B CB 3899 C CG . PRO B 77 ? 0.8686 0.8511 0.9793 -0.0477 -0.0038 -0.0326 77 PRO B CG 3900 C CD . PRO B 77 ? 0.8746 0.8738 0.9995 -0.0430 -0.0020 -0.0426 77 PRO B CD 3901 N N . ASP B 78 ? 1.1194 1.1174 1.2450 -0.0690 0.0302 -0.0272 78 ASP B N 3902 C CA . ASP B 78 ? 1.1399 1.1412 1.2727 -0.0792 0.0430 -0.0238 78 ASP B CA 3903 C C . ASP B 78 ? 1.1025 1.1115 1.2220 -0.0766 0.0519 -0.0240 78 ASP B C 3904 O O . ASP B 78 ? 1.2502 1.2627 1.3727 -0.0843 0.0634 -0.0212 78 ASP B O 3905 C CB . ASP B 78 ? 1.1480 1.1616 1.3145 -0.0826 0.0431 -0.0333 78 ASP B CB 3906 C CG . ASP B 78 ? 1.1798 1.2116 1.3601 -0.0713 0.0367 -0.0477 78 ASP B CG 3907 O OD1 . ASP B 78 ? 1.2299 1.2662 1.3941 -0.0626 0.0368 -0.0493 78 ASP B OD1 3908 O OD2 . ASP B 78 ? 1.1879 1.2290 1.3950 -0.0707 0.0311 -0.0577 78 ASP B OD2 3909 N N . GLY B 79 ? 1.0058 1.0175 1.1115 -0.0659 0.0472 -0.0275 79 GLY B N 3910 C CA . GLY B 79 ? 0.9904 1.0079 1.0834 -0.0626 0.0546 -0.0282 79 GLY B CA 3911 C C . GLY B 79 ? 0.9963 1.0318 1.1092 -0.0596 0.0583 -0.0386 79 GLY B C 3912 O O . GLY B 79 ? 0.9947 1.0358 1.0994 -0.0563 0.0643 -0.0403 79 GLY B O 3913 N N . VAL B 80 ? 1.0053 1.0502 1.1450 -0.0601 0.0539 -0.0466 80 VAL B N 3914 C CA . VAL B 80 ? 1.0518 1.1152 1.2151 -0.0590 0.0576 -0.0571 80 VAL B CA 3915 C C . VAL B 80 ? 1.0415 1.1169 1.2206 -0.0470 0.0456 -0.0702 80 VAL B C 3916 O O . VAL B 80 ? 1.0578 1.1470 1.2435 -0.0388 0.0455 -0.0790 80 VAL B O 3917 C CB . VAL B 80 ? 1.1006 1.1666 1.2864 -0.0726 0.0653 -0.0558 80 VAL B CB 3918 C CG1 . VAL B 80 ? 1.0889 1.1758 1.3071 -0.0711 0.0655 -0.0696 80 VAL B CG1 3919 C CG2 . VAL B 80 ? 1.1079 1.1672 1.2788 -0.0829 0.0797 -0.0449 80 VAL B CG2 3920 N N . THR B 81 ? 1.0130 1.0834 1.1980 -0.0453 0.0353 -0.0716 81 THR B N 3921 C CA . THR B 81 ? 1.0274 1.1091 1.2274 -0.0341 0.0232 -0.0842 81 THR B CA 3922 C C . THR B 81 ? 1.0131 1.0902 1.1898 -0.0206 0.0156 -0.0839 81 THR B C 3923 O O . THR B 81 ? 0.9840 1.0465 1.1390 -0.0217 0.0151 -0.0744 81 THR B O 3924 C CB . THR B 81 ? 1.0746 1.1531 1.2930 -0.0384 0.0154 -0.0870 81 THR B CB 3925 O OG1 . THR B 81 ? 1.1140 1.1900 1.3485 -0.0534 0.0243 -0.0828 81 THR B OG1 3926 C CG2 . THR B 81 ? 1.0700 1.1643 1.3107 -0.0280 0.0038 -0.1029 81 THR B CG2 3927 N N . LEU B 82 ? 1.0019 1.0920 1.1838 -0.0079 0.0097 -0.0944 82 LEU B N 3928 C CA . LEU B 82 ? 0.9292 1.0166 1.0922 0.0060 0.0017 -0.0954 82 LEU B CA 3929 C C . LEU B 82 ? 0.9810 1.0767 1.1593 0.0144 -0.0111 -0.1063 82 LEU B C 3930 O O . LEU B 82 ? 1.0222 1.1325 1.2259 0.0156 -0.0144 -0.1176 82 LEU B O 3931 C CB . LEU B 82 ? 0.8901 0.9847 1.0449 0.0160 0.0045 -0.0989 82 LEU B CB 3932 C CG . LEU B 82 ? 0.8738 0.9616 1.0117 0.0112 0.0162 -0.0904 82 LEU B CG 3933 C CD1 . LEU B 82 ? 0.8661 0.9580 0.9930 0.0247 0.0152 -0.0942 82 LEU B CD1 3934 C CD2 . LEU B 82 ? 0.8961 0.9657 1.0100 0.0050 0.0198 -0.0775 82 LEU B CD2 3935 N N . GLU B 83 ? 1.0393 1.1267 1.2029 0.0203 -0.0184 -0.1037 83 GLU B N 3936 C CA . GLU B 83 ? 1.0241 1.1194 1.1980 0.0305 -0.0312 -0.1145 83 GLU B CA 3937 C C . GLU B 83 ? 1.0331 1.1290 1.1852 0.0464 -0.0359 -0.1154 83 GLU B C 3938 O O . GLU B 83 ? 1.0125 1.0968 1.1399 0.0469 -0.0309 -0.1053 83 GLU B O 3939 C CB . GLU B 83 ? 0.9878 1.0739 1.1646 0.0248 -0.0365 -0.1119 83 GLU B CB 3940 C CG . GLU B 83 ? 1.0588 1.1446 1.2614 0.0113 -0.0350 -0.1134 83 GLU B CG 3941 C CD . GLU B 83 ? 1.1160 1.2194 1.3502 0.0126 -0.0389 -0.1278 83 GLU B CD 3942 O OE1 . GLU B 83 ? 1.1323 1.2489 1.3712 0.0262 -0.0477 -0.1396 83 GLU B OE1 3943 O OE2 . GLU B 83 ? 1.0979 1.2020 1.3527 -0.0002 -0.0330 -0.1274 83 GLU B OE2 3944 N N . TYR B 84 ? 1.0685 1.1776 1.2297 0.0593 -0.0455 -0.1277 84 TYR B N 3945 C CA . TYR B 84 ? 1.0806 1.1898 1.2201 0.0754 -0.0500 -0.1283 84 TYR B CA 3946 C C . TYR B 84 ? 1.0268 1.1247 1.1481 0.0768 -0.0526 -0.1218 84 TYR B C 3947 O O . TYR B 84 ? 1.0248 1.1191 1.1556 0.0691 -0.0555 -0.1217 84 TYR B O 3948 C CB . TYR B 84 ? 1.1220 1.2481 1.2740 0.0903 -0.0612 -0.1434 84 TYR B CB 3949 C CG . TYR B 84 ? 1.1807 1.3175 1.3409 0.0948 -0.0586 -0.1488 84 TYR B CG 3950 C CD1 . TYR B 84 ? 1.1953 1.3383 1.3786 0.0826 -0.0522 -0.1511 84 TYR B CD1 3951 C CD2 . TYR B 84 ? 1.1810 1.3215 1.3256 0.1115 -0.0621 -0.1515 84 TYR B CD2 3952 C CE1 . TYR B 84 ? 1.1970 1.3512 1.3896 0.0865 -0.0496 -0.1569 84 TYR B CE1 3953 C CE2 . TYR B 84 ? 1.1845 1.3348 1.3376 0.1160 -0.0602 -0.1569 84 TYR B CE2 3954 C CZ . TYR B 84 ? 1.1899 1.3478 1.3680 0.1033 -0.0539 -0.1602 84 TYR B CZ 3955 O OH . TYR B 84 ? 1.1529 1.3223 1.3425 0.1070 -0.0516 -0.1667 84 TYR B OH 3956 N N . ASN B 85 ? 1.0007 1.0926 1.0964 0.0865 -0.0513 -0.1163 85 ASN B N 3957 C CA . ASN B 85 ? 0.9667 1.0486 1.0435 0.0884 -0.0522 -0.1097 85 ASN B CA 3958 C C . ASN B 85 ? 0.9694 1.0584 1.0370 0.1057 -0.0611 -0.1168 85 ASN B C 3959 O O . ASN B 85 ? 0.9386 1.0279 0.9908 0.1165 -0.0597 -0.1155 85 ASN B O 3960 C CB . ASN B 85 ? 0.9475 1.0157 1.0015 0.0841 -0.0415 -0.0965 85 ASN B CB 3961 C CG . ASN B 85 ? 0.9650 1.0235 1.0000 0.0857 -0.0412 -0.0897 85 ASN B CG 3962 O OD1 . ASN B 85 ? 0.9760 1.0380 1.0136 0.0903 -0.0487 -0.0944 85 ASN B OD1 3963 N ND2 . ASN B 85 ? 0.9685 1.0156 0.9855 0.0819 -0.0323 -0.0792 85 ASN B ND2 3964 N N . PRO B 86 ? 0.9638 1.0578 1.0398 0.1088 -0.0702 -0.1240 86 PRO B N 3965 C CA . PRO B 86 ? 0.9534 1.0554 1.0204 0.1259 -0.0792 -0.1318 86 PRO B CA 3966 C C . PRO B 86 ? 0.9566 1.0493 0.9930 0.1333 -0.0746 -0.1223 86 PRO B C 3967 O O . PRO B 86 ? 0.9776 1.0754 1.0008 0.1487 -0.0796 -0.1263 86 PRO B O 3968 C CB . PRO B 86 ? 0.9728 1.0801 1.0567 0.1243 -0.0886 -0.1408 86 PRO B CB 3969 C CG . PRO B 86 ? 0.9622 1.0622 1.0625 0.1062 -0.0841 -0.1362 86 PRO B CG 3970 C CD . PRO B 86 ? 0.9469 1.0361 1.0354 0.0969 -0.0716 -0.1231 86 PRO B CD 3971 N N . TYR B 87 ? 0.9461 1.0254 0.9716 0.1225 -0.0651 -0.1100 87 TYR B N 3972 C CA . TYR B 87 ? 0.9176 0.9873 0.9166 0.1270 -0.0591 -0.1004 87 TYR B CA 3973 C C . TYR B 87 ? 0.9117 0.9719 0.8964 0.1250 -0.0488 -0.0906 87 TYR B C 3974 O O . TYR B 87 ? 0.9354 0.9849 0.9019 0.1234 -0.0413 -0.0809 87 TYR B O 3975 C CB . TYR B 87 ? 0.9007 0.9630 0.8985 0.1171 -0.0568 -0.0949 87 TYR B CB 3976 C CG . TYR B 87 ? 0.9159 0.9862 0.9303 0.1178 -0.0671 -0.1049 87 TYR B CG 3977 C CD1 . TYR B 87 ? 0.9371 1.0173 0.9481 0.1322 -0.0756 -0.1140 87 TYR B CD1 3978 C CD2 . TYR B 87 ? 0.8994 0.9670 0.9324 0.1047 -0.0685 -0.1055 87 TYR B CD2 3979 C CE1 . TYR B 87 ? 0.9059 0.9936 0.9330 0.1334 -0.0856 -0.1244 87 TYR B CE1 3980 C CE2 . TYR B 87 ? 0.8870 0.9608 0.9363 0.1056 -0.0783 -0.1149 87 TYR B CE2 3981 C CZ . TYR B 87 ? 0.8785 0.9626 0.9253 0.1200 -0.0870 -0.1249 87 TYR B CZ 3982 O OH . TYR B 87 ? 0.8464 0.9367 0.9098 0.1216 -0.0972 -0.1355 87 TYR B OH 3983 N N . SER B 88 ? 0.9236 0.9881 0.9177 0.1254 -0.0483 -0.0938 88 SER B N 3984 C CA . SER B 88 ? 0.9600 1.0154 0.9424 0.1233 -0.0388 -0.0855 88 SER B CA 3985 C C . SER B 88 ? 0.9616 1.0107 0.9192 0.1363 -0.0362 -0.0804 88 SER B C 3986 O O . SER B 88 ? 1.0581 1.1142 1.0100 0.1509 -0.0433 -0.0861 88 SER B O 3987 C CB . SER B 88 ? 0.9747 1.0379 0.9727 0.1229 -0.0394 -0.0916 88 SER B CB 3988 O OG . SER B 88 ? 0.9788 1.0332 0.9635 0.1236 -0.0310 -0.0844 88 SER B OG 3989 N N . TRP B 89 ? 0.9231 0.9587 0.8660 0.1312 -0.0261 -0.0697 89 TRP B N 3990 C CA . TRP B 89 ? 0.9581 0.9845 0.8771 0.1418 -0.0218 -0.0629 89 TRP B CA 3991 C C . TRP B 89 ? 0.9894 1.0188 0.9047 0.1549 -0.0245 -0.0665 89 TRP B C 3992 O O . TRP B 89 ? 1.0079 1.0332 0.9043 0.1685 -0.0249 -0.0637 89 TRP B O 3993 C CB . TRP B 89 ? 0.9381 0.9488 0.8451 0.1318 -0.0102 -0.0513 89 TRP B CB 3994 C CG . TRP B 89 ? 0.9489 0.9561 0.8537 0.1234 -0.0080 -0.0473 89 TRP B CG 3995 C CD1 . TRP B 89 ? 0.9502 0.9662 0.8666 0.1207 -0.0148 -0.0529 89 TRP B CD1 3996 C CD2 . TRP B 89 ? 0.9168 0.9112 0.8088 0.1167 0.0012 -0.0375 89 TRP B CD2 3997 N NE1 . TRP B 89 ? 0.9534 0.9633 0.8643 0.1133 -0.0104 -0.0472 89 TRP B NE1 3998 C CE2 . TRP B 89 ? 0.9214 0.9187 0.8179 0.1105 -0.0005 -0.0380 89 TRP B CE2 3999 C CE3 . TRP B 89 ? 0.9241 0.9051 0.8026 0.1152 0.0107 -0.0292 89 TRP B CE3 4000 C CZ2 . TRP B 89 ? 0.9224 0.9109 0.8109 0.1032 0.0067 -0.0308 89 TRP B CZ2 4001 C CZ3 . TRP B 89 ? 0.9276 0.8993 0.7987 0.1072 0.0181 -0.0220 89 TRP B CZ3 4002 C CH2 . TRP B 89 ? 0.9215 0.8976 0.7978 0.1013 0.0161 -0.0231 89 TRP B CH2 4003 N N . ASN B 90 ? 1.0266 1.0634 0.9598 0.1515 -0.0264 -0.0728 90 ASN B N 4004 C CA . ASN B 90 ? 1.0967 1.1385 1.0292 0.1647 -0.0302 -0.0780 90 ASN B CA 4005 C C . ASN B 90 ? 1.1771 1.2344 1.1162 0.1789 -0.0430 -0.0898 90 ASN B C 4006 O O . ASN B 90 ? 1.2467 1.3123 1.1909 0.1899 -0.0486 -0.0972 90 ASN B O 4007 C CB . ASN B 90 ? 1.0094 1.0554 0.9596 0.1569 -0.0273 -0.0815 90 ASN B CB 4008 C CG . ASN B 90 ? 1.0215 1.0857 0.9993 0.1542 -0.0352 -0.0942 90 ASN B CG 4009 O OD1 . ASN B 90 ? 1.0166 1.0857 1.0052 0.1473 -0.0387 -0.0970 90 ASN B OD1 4010 N ND2 . ASN B 90 ? 1.0567 1.1310 1.0473 0.1598 -0.0381 -0.1023 90 ASN B ND2 4011 N N . LEU B 91 ? 1.1522 1.2144 1.0926 0.1790 -0.0481 -0.0927 91 LEU B N 4012 C CA . LEU B 91 ? 1.1660 1.2415 1.1080 0.1944 -0.0603 -0.1035 91 LEU B CA 4013 C C . LEU B 91 ? 1.1986 1.2674 1.1124 0.2123 -0.0605 -0.0986 91 LEU B C 4014 O O . LEU B 91 ? 1.2927 1.3713 1.2055 0.2283 -0.0700 -0.1074 91 LEU B O 4015 C CB . LEU B 91 ? 1.1596 1.2406 1.1072 0.1911 -0.0653 -0.1075 91 LEU B CB 4016 C CG . LEU B 91 ? 1.1911 1.2820 1.1694 0.1778 -0.0694 -0.1160 91 LEU B CG 4017 C CD1 . LEU B 91 ? 1.1790 1.2707 1.1595 0.1735 -0.0725 -0.1172 91 LEU B CD1 4018 C CD2 . LEU B 91 ? 1.2008 1.3091 1.2015 0.1849 -0.0801 -0.1313 91 LEU B CD2 4019 N N . ILE B 92 ? 1.1214 1.1731 1.0127 0.2096 -0.0500 -0.0848 92 ILE B N 4020 C CA . ILE B 92 ? 1.1280 1.1700 0.9899 0.2250 -0.0480 -0.0775 92 ILE B CA 4021 C C . ILE B 92 ? 1.1263 1.1494 0.9730 0.2216 -0.0361 -0.0645 92 ILE B C 4022 O O . ILE B 92 ? 1.1837 1.1939 1.0048 0.2300 -0.0308 -0.0549 92 ILE B O 4023 C CB . ILE B 92 ? 1.1535 1.1929 0.9998 0.2269 -0.0463 -0.0730 92 ILE B CB 4024 C CG1 . ILE B 92 ? 1.1290 1.1587 0.9785 0.2079 -0.0357 -0.0643 92 ILE B CG1 4025 C CG2 . ILE B 92 ? 1.1393 1.1969 0.9973 0.2340 -0.0591 -0.0867 92 ILE B CG2 4026 C CD1 . ILE B 92 ? 1.1490 1.1752 0.9830 0.2086 -0.0317 -0.0587 92 ILE B CD1 4027 N N . ALA B 93 ? 1.0933 1.1141 0.9551 0.2094 -0.0315 -0.0642 93 ALA B N 4028 C CA . ALA B 93 ? 1.0728 1.0757 0.9219 0.2058 -0.0207 -0.0532 93 ALA B CA 4029 C C . ALA B 93 ? 1.0846 1.0902 0.9511 0.1992 -0.0195 -0.0575 93 ALA B C 4030 O O . ALA B 93 ? 1.0359 1.0555 0.9261 0.1914 -0.0238 -0.0665 93 ALA B O 4031 C CB . ALA B 93 ? 1.0573 1.0480 0.8996 0.1915 -0.0101 -0.0429 93 ALA B CB 4032 N N . ASN B 94 ? 1.1101 1.1019 0.9648 0.2026 -0.0132 -0.0508 94 ASN B N 4033 C CA . ASN B 94 ? 1.1432 1.1352 1.0120 0.1951 -0.0097 -0.0534 94 ASN B CA 4034 C C . ASN B 94 ? 1.1517 1.1315 1.0196 0.1774 0.0014 -0.0449 94 ASN B C 4035 O O . ASN B 94 ? 1.1673 1.1294 1.0171 0.1771 0.0093 -0.0346 94 ASN B O 4036 C CB . ASN B 94 ? 1.1885 1.1719 1.0456 0.2093 -0.0096 -0.0519 94 ASN B CB 4037 C CG . ASN B 94 ? 1.2177 1.2111 1.0704 0.2296 -0.0213 -0.0592 94 ASN B CG 4038 O OD1 . ASN B 94 ? 1.2093 1.2222 1.0820 0.2323 -0.0305 -0.0718 94 ASN B OD1 4039 N ND2 . ASN B 94 ? 1.2331 1.2130 1.0595 0.2440 -0.0210 -0.0514 94 ASN B ND2 4040 N N . VAL B 95 ? 1.1194 1.1084 1.0068 0.1627 0.0019 -0.0492 95 VAL B N 4041 C CA . VAL B 95 ? 1.1068 1.0867 0.9939 0.1460 0.0105 -0.0423 95 VAL B CA 4042 C C . VAL B 95 ? 1.0795 1.0561 0.9742 0.1380 0.0167 -0.0427 95 VAL B C 4043 O O . VAL B 95 ? 1.0901 1.0794 1.0023 0.1362 0.0136 -0.0509 95 VAL B O 4044 C CB . VAL B 95 ? 1.1007 1.0913 1.0023 0.1349 0.0072 -0.0458 95 VAL B CB 4045 C CG1 . VAL B 95 ? 1.1136 1.0930 1.0084 0.1219 0.0146 -0.0375 95 VAL B CG1 4046 C CG2 . VAL B 95 ? 1.0876 1.0884 0.9894 0.1449 -0.0020 -0.0509 95 VAL B CG2 4047 N N . LEU B 96 ? 1.0302 0.9901 0.9122 0.1334 0.0254 -0.0345 96 LEU B N 4048 C CA . LEU B 96 ? 1.0609 1.0162 0.9478 0.1261 0.0317 -0.0349 96 LEU B CA 4049 C C . LEU B 96 ? 1.0717 1.0236 0.9623 0.1087 0.0376 -0.0315 96 LEU B C 4050 O O . LEU B 96 ? 1.1279 1.0662 1.0066 0.1041 0.0432 -0.0242 96 LEU B O 4051 C CB . LEU B 96 ? 1.0517 0.9898 0.9226 0.1341 0.0368 -0.0294 96 LEU B CB 4052 C CG . LEU B 96 ? 1.0348 0.9667 0.9091 0.1289 0.0431 -0.0305 96 LEU B CG 4053 C CD1 . LEU B 96 ? 1.0491 0.9971 0.9407 0.1312 0.0394 -0.0407 96 LEU B CD1 4054 C CD2 . LEU B 96 ? 1.0377 0.9504 0.8958 0.1377 0.0475 -0.0246 96 LEU B CD2 4055 N N . TYR B 97 ? 1.0470 1.0111 0.9538 0.0994 0.0363 -0.0368 97 TYR B N 4056 C CA . TYR B 97 ? 0.9777 0.9394 0.8875 0.0837 0.0408 -0.0340 97 TYR B CA 4057 C C . TYR B 97 ? 0.9963 0.9509 0.9041 0.0785 0.0482 -0.0334 97 TYR B C 4058 O O . TYR B 97 ? 1.0693 1.0319 0.9867 0.0795 0.0487 -0.0391 97 TYR B O 4059 C CB . TYR B 97 ? 0.9497 0.9262 0.8768 0.0763 0.0366 -0.0391 97 TYR B CB 4060 C CG . TYR B 97 ? 0.9313 0.9148 0.8619 0.0805 0.0289 -0.0407 97 TYR B CG 4061 C CD1 . TYR B 97 ? 0.9451 0.9388 0.8816 0.0925 0.0218 -0.0470 97 TYR B CD1 4062 C CD2 . TYR B 97 ? 0.9051 0.8857 0.8335 0.0732 0.0280 -0.0367 97 TYR B CD2 4063 C CE1 . TYR B 97 ? 0.9510 0.9515 0.8906 0.0970 0.0143 -0.0496 97 TYR B CE1 4064 C CE2 . TYR B 97 ? 0.8811 0.8684 0.8130 0.0776 0.0208 -0.0390 97 TYR B CE2 4065 C CZ . TYR B 97 ? 0.8959 0.8931 0.8331 0.0895 0.0140 -0.0456 97 TYR B CZ 4066 O OH . TYR B 97 ? 0.9187 0.9232 0.8592 0.0949 0.0063 -0.0492 97 TYR B OH 4067 N N . LEU B 98 ? 0.9900 0.9305 0.8864 0.0730 0.0539 -0.0274 98 LEU B N 4068 C CA . LEU B 98 ? 1.0273 0.9593 0.9202 0.0695 0.0606 -0.0275 98 LEU B CA 4069 C C . LEU B 98 ? 1.0657 0.9962 0.9597 0.0551 0.0645 -0.0262 98 LEU B C 4070 O O . LEU B 98 ? 1.0646 0.9881 0.9526 0.0492 0.0653 -0.0215 98 LEU B O 4071 C CB . LEU B 98 ? 1.0097 0.9246 0.8885 0.0759 0.0643 -0.0224 98 LEU B CB 4072 C CG . LEU B 98 ? 0.9983 0.9037 0.8742 0.0750 0.0703 -0.0238 98 LEU B CG 4073 C CD1 . LEU B 98 ? 1.0205 0.9345 0.9041 0.0829 0.0687 -0.0307 98 LEU B CD1 4074 C CD2 . LEU B 98 ? 1.0388 0.9252 0.9014 0.0801 0.0742 -0.0178 98 LEU B CD2 4075 N N . GLU B 99 ? 1.0129 0.9500 0.9139 0.0499 0.0671 -0.0306 99 GLU B N 4076 C CA . GLU B 99 ? 0.9524 0.8876 0.8519 0.0375 0.0708 -0.0296 99 GLU B CA 4077 C C . GLU B 99 ? 0.9424 0.8636 0.8319 0.0360 0.0763 -0.0284 99 GLU B C 4078 O O . GLU B 99 ? 0.9512 0.8697 0.8400 0.0406 0.0796 -0.0319 99 GLU B O 4079 C CB . GLU B 99 ? 0.9520 0.8993 0.8612 0.0326 0.0725 -0.0342 99 GLU B CB 4080 C CG . GLU B 99 ? 1.0023 0.9623 0.9232 0.0307 0.0676 -0.0352 99 GLU B CG 4081 C CD . GLU B 99 ? 1.0084 0.9789 0.9385 0.0231 0.0709 -0.0382 99 GLU B CD 4082 O OE1 . GLU B 99 ? 0.9882 0.9646 0.9235 0.0263 0.0746 -0.0433 99 GLU B OE1 4083 O OE2 . GLU B 99 ? 0.9698 0.9422 0.9017 0.0142 0.0700 -0.0352 99 GLU B OE2 4084 N N . SER B 100 ? 0.9257 0.8384 0.8086 0.0298 0.0770 -0.0243 100 SER B N 4085 C CA . SER B 100 ? 0.9164 0.8150 0.7913 0.0285 0.0816 -0.0233 100 SER B CA 4086 C C . SER B 100 ? 0.8968 0.7916 0.7687 0.0182 0.0818 -0.0211 100 SER B C 4087 O O . SER B 100 ? 0.8195 0.7201 0.6938 0.0146 0.0778 -0.0188 100 SER B O 4088 C CB . SER B 100 ? 0.9493 0.8373 0.8188 0.0380 0.0822 -0.0198 100 SER B CB 4089 O OG . SER B 100 ? 0.9601 0.8349 0.8233 0.0340 0.0855 -0.0161 100 SER B OG 4090 N N . PRO B 101 ? 0.9715 0.8568 0.8387 0.0138 0.0858 -0.0228 101 PRO B N 4091 C CA . PRO B 101 ? 1.0008 0.8783 0.8657 0.0174 0.0904 -0.0265 101 PRO B CA 4092 C C . PRO B 101 ? 1.0250 0.9117 0.8925 0.0161 0.0917 -0.0322 101 PRO B C 4093 O O . PRO B 101 ? 1.0815 0.9802 0.9526 0.0122 0.0896 -0.0324 101 PRO B O 4094 C CB . PRO B 101 ? 1.0189 0.8850 0.8799 0.0108 0.0930 -0.0269 101 PRO B CB 4095 C CG . PRO B 101 ? 1.0052 0.8787 0.8669 0.0018 0.0896 -0.0262 101 PRO B CG 4096 C CD . PRO B 101 ? 0.9839 0.8662 0.8491 0.0045 0.0852 -0.0219 101 PRO B CD 4097 N N . ALA B 102 ? 1.0774 0.9582 0.9433 0.0193 0.0956 -0.0368 102 ALA B N 4098 C CA . ALA B 102 ? 1.0873 0.9769 0.9551 0.0183 0.0982 -0.0431 102 ALA B CA 4099 C C . ALA B 102 ? 1.0724 0.9706 0.9385 0.0083 0.0978 -0.0436 102 ALA B C 4100 O O . ALA B 102 ? 1.0580 0.9503 0.9186 0.0018 0.0975 -0.0433 102 ALA B O 4101 C CB . ALA B 102 ? 1.1187 0.9979 0.9832 0.0207 0.1024 -0.0485 102 ALA B CB 4102 N N . GLY B 103 ? 1.0613 0.9733 0.9324 0.0074 0.0979 -0.0443 103 GLY B N 4103 C CA . GLY B 103 ? 1.0813 1.0011 0.9497 -0.0012 0.0985 -0.0440 103 GLY B CA 4104 C C . GLY B 103 ? 1.0827 1.0097 0.9557 -0.0047 0.0942 -0.0384 103 GLY B C 4105 O O . GLY B 103 ? 1.0517 0.9867 0.9250 -0.0104 0.0951 -0.0374 103 GLY B O 4106 N N . VAL B 104 ? 1.0626 0.9857 0.9385 -0.0012 0.0898 -0.0346 104 VAL B N 4107 C CA . VAL B 104 ? 0.9662 0.8956 0.8476 -0.0031 0.0849 -0.0303 104 VAL B CA 4108 C C . VAL B 104 ? 0.9423 0.8837 0.8347 0.0007 0.0850 -0.0324 104 VAL B C 4109 O O . VAL B 104 ? 1.0131 0.9561 0.9098 0.0087 0.0862 -0.0360 104 VAL B O 4110 C CB . VAL B 104 ? 0.9319 0.8545 0.8130 0.0008 0.0806 -0.0268 104 VAL B CB 4111 C CG1 . VAL B 104 ? 0.9306 0.8604 0.8182 0.0001 0.0751 -0.0236 104 VAL B CG1 4112 C CG2 . VAL B 104 ? 0.9410 0.8530 0.8140 -0.0037 0.0808 -0.0253 104 VAL B CG2 4113 N N . GLY B 105 ? 0.8968 0.8463 0.7945 -0.0048 0.0834 -0.0304 105 GLY B N 4114 C CA . GLY B 105 ? 0.9124 0.8744 0.8236 -0.0027 0.0833 -0.0328 105 GLY B CA 4115 C C . GLY B 105 ? 0.9072 0.8766 0.8229 -0.0004 0.0895 -0.0387 105 GLY B C 4116 O O . GLY B 105 ? 0.8925 0.8629 0.8030 -0.0060 0.0951 -0.0394 105 GLY B O 4117 N N . PHE B 106 ? 0.9412 0.9164 0.8665 0.0086 0.0883 -0.0432 106 PHE B N 4118 C CA . PHE B 106 ? 0.9599 0.9429 0.8912 0.0128 0.0935 -0.0500 106 PHE B CA 4119 C C . PHE B 106 ? 1.0107 0.9835 0.9334 0.0204 0.0949 -0.0527 106 PHE B C 4120 O O . PHE B 106 ? 1.0637 1.0415 0.9907 0.0255 0.0986 -0.0590 106 PHE B O 4121 C CB . PHE B 106 ? 0.9221 0.9189 0.8709 0.0190 0.0905 -0.0548 106 PHE B CB 4122 C CG . PHE B 106 ? 0.9161 0.9244 0.8772 0.0110 0.0907 -0.0540 106 PHE B CG 4123 C CD1 . PHE B 106 ? 0.9445 0.9572 0.9052 0.0008 0.0981 -0.0530 106 PHE B CD1 4124 C CD2 . PHE B 106 ? 0.8807 0.8951 0.8538 0.0137 0.0839 -0.0545 106 PHE B CD2 4125 C CE1 . PHE B 106 ? 0.8833 0.9048 0.8554 -0.0069 0.0992 -0.0513 106 PHE B CE1 4126 C CE2 . PHE B 106 ? 0.8791 0.9030 0.8652 0.0059 0.0843 -0.0541 106 PHE B CE2 4127 C CZ . PHE B 106 ? 0.8779 0.9047 0.8637 -0.0047 0.0922 -0.0520 106 PHE B CZ 4128 N N . SER B 107 ? 1.0426 1.0011 0.9542 0.0212 0.0922 -0.0482 107 SER B N 4129 C CA . SER B 107 ? 1.0915 1.0378 0.9951 0.0274 0.0941 -0.0499 107 SER B CA 4130 C C . SER B 107 ? 1.0805 1.0230 0.9765 0.0211 0.0998 -0.0525 107 SER B C 4131 O O . SER B 107 ? 1.1017 1.0448 0.9926 0.0117 0.1008 -0.0499 107 SER B O 4132 C CB . SER B 107 ? 1.0868 1.0192 0.9824 0.0297 0.0903 -0.0441 107 SER B CB 4133 O OG . SER B 107 ? 1.0365 0.9726 0.9374 0.0369 0.0850 -0.0423 107 SER B OG 4134 N N . TYR B 108 ? 1.1039 1.0421 0.9984 0.0271 0.1031 -0.0579 108 TYR B N 4135 C CA . TYR B 108 ? 1.1404 1.0753 1.0279 0.0228 0.1083 -0.0622 108 TYR B CA 4136 C C . TYR B 108 ? 1.1699 1.0910 1.0531 0.0299 0.1094 -0.0657 108 TYR B C 4137 O O . TYR B 108 ? 1.1594 1.0726 1.0440 0.0383 0.1066 -0.0638 108 TYR B O 4138 C CB . TYR B 108 ? 1.1549 1.1055 1.0490 0.0216 0.1135 -0.0681 108 TYR B CB 4139 C CG . TYR B 108 ? 1.2072 1.1646 1.1121 0.0323 0.1141 -0.0745 108 TYR B CG 4140 C CD1 . TYR B 108 ? 1.2646 1.2308 1.1810 0.0376 0.1100 -0.0737 108 TYR B CD1 4141 C CD2 . TYR B 108 ? 1.2466 1.2019 1.1506 0.0377 0.1181 -0.0821 108 TYR B CD2 4142 C CE1 . TYR B 108 ? 1.2959 1.2690 1.2225 0.0483 0.1095 -0.0803 108 TYR B CE1 4143 C CE2 . TYR B 108 ? 1.2590 1.2208 1.1734 0.0484 0.1179 -0.0884 108 TYR B CE2 4144 C CZ . TYR B 108 ? 1.2807 1.2516 1.2063 0.0538 0.1134 -0.0874 108 TYR B CZ 4145 O OH . TYR B 108 ? 1.2961 1.2745 1.2326 0.0652 0.1122 -0.0944 108 TYR B OH 4146 N N . SER B 109 ? 1.2109 1.1283 1.0881 0.0266 0.1135 -0.0707 109 SER B N 4147 C CA . SER B 109 ? 1.3046 1.2107 1.1799 0.0334 0.1155 -0.0764 109 SER B CA 4148 C C . SER B 109 ? 1.2939 1.2094 1.1698 0.0331 0.1209 -0.0855 109 SER B C 4149 O O . SER B 109 ? 1.3004 1.2266 1.1737 0.0254 0.1235 -0.0861 109 SER B O 4150 C CB . SER B 109 ? 1.3171 1.2054 1.1839 0.0295 0.1147 -0.0744 109 SER B CB 4151 O OG . SER B 109 ? 1.2948 1.1859 1.1552 0.0204 0.1164 -0.0771 109 SER B OG 4152 N N . ASP B 110 ? 1.3363 1.2473 1.2150 0.0418 0.1226 -0.0924 110 ASP B N 4153 C CA . ASP B 110 ? 1.3522 1.2724 1.2319 0.0428 0.1280 -0.1023 110 ASP B CA 4154 C C . ASP B 110 ? 1.3181 1.2353 1.1870 0.0342 0.1306 -0.1052 110 ASP B C 4155 O O . ASP B 110 ? 1.2817 1.2122 1.1483 0.0299 0.1351 -0.1093 110 ASP B O 4156 C CB . ASP B 110 ? 1.4021 1.3143 1.2860 0.0545 0.1284 -0.1096 110 ASP B CB 4157 C CG . ASP B 110 ? 1.3929 1.3122 1.2879 0.0647 0.1259 -0.1094 110 ASP B CG 4158 O OD1 . ASP B 110 ? 1.2832 1.2173 1.1847 0.0623 0.1249 -0.1059 110 ASP B OD1 4159 O OD2 . ASP B 110 ? 1.4448 1.3543 1.3421 0.0756 0.1245 -0.1131 110 ASP B OD2 4160 N N . ASP B 111 ? 1.3079 1.2079 1.1702 0.0318 0.1278 -0.1032 111 ASP B N 4161 C CA . ASP B 111 ? 1.3477 1.2443 1.2002 0.0244 0.1289 -0.1071 111 ASP B CA 4162 C C . ASP B 111 ? 1.3515 1.2540 1.1974 0.0143 0.1269 -0.1001 111 ASP B C 4163 O O . ASP B 111 ? 1.3849 1.2874 1.2217 0.0085 0.1272 -0.1032 111 ASP B O 4164 C CB . ASP B 111 ? 1.3556 1.2316 1.2061 0.0257 0.1268 -0.1096 111 ASP B CB 4165 C CG . ASP B 111 ? 1.3352 1.1990 1.1871 0.0241 0.1226 -0.0998 111 ASP B CG 4166 O OD1 . ASP B 111 ? 1.3441 1.2122 1.2002 0.0267 0.1210 -0.0923 111 ASP B OD1 4167 O OD2 . ASP B 111 ? 1.3376 1.1876 1.1868 0.0203 0.1212 -0.1003 111 ASP B OD2 4168 N N . LYS B 112 ? 1.3893 1.2964 1.2396 0.0129 0.1244 -0.0912 112 LYS B N 4169 C CA . LYS B 112 ? 1.4339 1.3461 1.2790 0.0041 0.1220 -0.0842 112 LYS B CA 4170 C C . LYS B 112 ? 1.4229 1.3236 1.2606 -0.0016 0.1179 -0.0824 112 LYS B C 4171 O O . LYS B 112 ? 1.4870 1.3919 1.3184 -0.0085 0.1159 -0.0786 112 LYS B O 4172 C CB . LYS B 112 ? 1.5034 1.4304 1.3432 -0.0005 0.1265 -0.0862 112 LYS B CB 4173 C CG . LYS B 112 ? 1.5561 1.4978 1.4051 0.0032 0.1315 -0.0883 112 LYS B CG 4174 C CD . LYS B 112 ? 1.5701 1.5247 1.4187 -0.0037 0.1335 -0.0823 112 LYS B CD 4175 C CE . LYS B 112 ? 1.5878 1.5448 1.4213 -0.0108 0.1364 -0.0824 112 LYS B CE 4176 N NZ . LYS B 112 ? 1.6075 1.5763 1.4389 -0.0098 0.1449 -0.0896 112 LYS B NZ 4177 N N . PHE B 113 ? 1.4195 1.3056 1.2586 0.0010 0.1166 -0.0850 113 PHE B N 4178 C CA . PHE B 113 ? 1.4357 1.3117 1.2711 -0.0047 0.1128 -0.0836 113 PHE B CA 4179 C C . PHE B 113 ? 1.3758 1.2479 1.2162 -0.0052 0.1094 -0.0741 113 PHE B C 4180 O O . PHE B 113 ? 1.4118 1.2759 1.2578 0.0004 0.1099 -0.0716 113 PHE B O 4181 C CB . PHE B 113 ? 1.5126 1.3744 1.3489 -0.0026 0.1138 -0.0912 113 PHE B CB 4182 C CG . PHE B 113 ? 1.6695 1.5228 1.5039 -0.0093 0.1102 -0.0922 113 PHE B CG 4183 C CD1 . PHE B 113 ? 1.7554 1.6161 1.5818 -0.0157 0.1075 -0.0950 113 PHE B CD1 4184 C CD2 . PHE B 113 ? 1.7100 1.5481 1.5507 -0.0092 0.1097 -0.0906 113 PHE B CD2 4185 C CE1 . PHE B 113 ? 1.7904 1.6449 1.6166 -0.0213 0.1034 -0.0973 113 PHE B CE1 4186 C CE2 . PHE B 113 ? 1.7722 1.6041 1.6138 -0.0159 0.1068 -0.0927 113 PHE B CE2 4187 C CZ . PHE B 113 ? 1.8141 1.6548 1.6491 -0.0217 0.1031 -0.0966 113 PHE B CZ 4188 N N . TYR B 114 ? 1.2957 1.1736 1.1334 -0.0114 0.1058 -0.0688 114 TYR B N 4189 C CA . TYR B 114 ? 1.1417 1.0191 0.9843 -0.0115 0.1025 -0.0602 114 TYR B CA 4190 C C . TYR B 114 ? 1.0882 0.9575 0.9307 -0.0164 0.0989 -0.0579 114 TYR B C 4191 O O . TYR B 114 ? 1.0705 0.9397 0.9167 -0.0166 0.0964 -0.0513 114 TYR B O 4192 C CB . TYR B 114 ? 1.0953 0.9861 0.9377 -0.0138 0.1010 -0.0553 114 TYR B CB 4193 C CG . TYR B 114 ? 1.0823 0.9828 0.9287 -0.0090 0.1047 -0.0569 114 TYR B CG 4194 C CD1 . TYR B 114 ? 1.0197 0.9176 0.8729 -0.0007 0.1062 -0.0578 114 TYR B CD1 4195 C CD2 . TYR B 114 ? 1.0625 0.9750 0.9061 -0.0125 0.1069 -0.0573 114 TYR B CD2 4196 C CE1 . TYR B 114 ? 1.0058 0.9142 0.8647 0.0040 0.1091 -0.0604 114 TYR B CE1 4197 C CE2 . TYR B 114 ? 1.0291 0.9519 0.8788 -0.0087 0.1110 -0.0594 114 TYR B CE2 4198 C CZ . TYR B 114 ? 0.9804 0.9018 0.8387 -0.0004 0.1117 -0.0615 114 TYR B CZ 4199 O OH . TYR B 114 ? 0.9370 0.8702 0.8034 0.0037 0.1151 -0.0647 114 TYR B OH 4200 N N . ALA B 115 ? 1.1301 0.9936 0.9696 -0.0202 0.0987 -0.0642 115 ALA B N 4201 C CA . ALA B 115 ? 1.1380 0.9931 0.9807 -0.0245 0.0962 -0.0636 115 ALA B CA 4202 C C . ALA B 115 ? 1.1060 0.9494 0.9552 -0.0200 0.0993 -0.0604 115 ALA B C 4203 O O . ALA B 115 ? 1.0748 0.9116 0.9248 -0.0145 0.1032 -0.0633 115 ALA B O 4204 C CB . ALA B 115 ? 1.1481 0.9992 0.9882 -0.0287 0.0953 -0.0728 115 ALA B CB 4205 N N . THR B 116 ? 1.0932 0.9340 0.9466 -0.0217 0.0979 -0.0542 116 THR B N 4206 C CA . THR B 116 ? 1.0753 0.9048 0.9327 -0.0171 0.1014 -0.0493 116 THR B CA 4207 C C . THR B 116 ? 1.0374 0.8634 0.8994 -0.0221 0.1005 -0.0455 116 THR B C 4208 O O . THR B 116 ? 0.9524 0.7844 0.8156 -0.0289 0.0967 -0.0481 116 THR B O 4209 C CB . THR B 116 ? 1.0563 0.8906 0.9125 -0.0089 0.1017 -0.0436 116 THR B CB 4210 O OG1 . THR B 116 ? 1.0718 0.8934 0.9290 -0.0025 0.1054 -0.0395 116 THR B OG1 4211 C CG2 . THR B 116 ? 1.0001 0.8459 0.8569 -0.0103 0.0974 -0.0377 116 THR B CG2 4212 N N . ASN B 117 ? 1.0598 0.8761 0.9240 -0.0185 0.1042 -0.0396 117 ASN B N 4213 C CA . ASN B 117 ? 1.1073 0.9202 0.9765 -0.0230 0.1051 -0.0357 117 ASN B CA 4214 C C . ASN B 117 ? 1.1198 0.9267 0.9876 -0.0165 0.1086 -0.0267 117 ASN B C 4215 O O . ASN B 117 ? 1.1539 0.9566 1.0170 -0.0081 0.1103 -0.0242 117 ASN B O 4216 C CB . ASN B 117 ? 1.1745 0.9765 1.0498 -0.0294 0.1081 -0.0416 117 ASN B CB 4217 C CG . ASN B 117 ? 1.2500 1.0345 1.1255 -0.0252 0.1147 -0.0413 117 ASN B CG 4218 O OD1 . ASN B 117 ? 1.3303 1.1073 1.2027 -0.0186 0.1183 -0.0335 117 ASN B OD1 4219 N ND2 . ASN B 117 ? 1.2823 1.0595 1.1612 -0.0286 0.1157 -0.0500 117 ASN B ND2 4220 N N . ASP B 118 ? 1.1277 0.9346 0.9991 -0.0198 0.1097 -0.0224 118 ASP B N 4221 C CA . ASP B 118 ? 1.0681 0.8722 0.9362 -0.0135 0.1124 -0.0135 118 ASP B CA 4222 C C . ASP B 118 ? 1.1019 0.8897 0.9648 -0.0058 0.1186 -0.0093 118 ASP B C 4223 O O . ASP B 118 ? 1.0764 0.8648 0.9327 0.0036 0.1180 -0.0040 118 ASP B O 4224 C CB . ASP B 118 ? 1.0245 0.8291 0.8985 -0.0195 0.1147 -0.0107 118 ASP B CB 4225 C CG . ASP B 118 ? 0.9627 0.7836 0.8413 -0.0250 0.1078 -0.0139 118 ASP B CG 4226 O OD1 . ASP B 118 ? 0.8760 0.7083 0.7511 -0.0218 0.1017 -0.0138 118 ASP B OD1 4227 O OD2 . ASP B 118 ? 0.9653 0.7874 0.8519 -0.0325 0.1086 -0.0164 118 ASP B OD2 4228 N N . THR B 119 ? 1.1308 0.9038 0.9971 -0.0094 0.1238 -0.0120 119 THR B N 4229 C CA . THR B 119 ? 1.1730 0.9274 1.0344 -0.0023 0.1298 -0.0076 119 THR B CA 4230 C C . THR B 119 ? 1.1451 0.9007 1.0010 0.0066 0.1267 -0.0104 119 THR B C 4231 O O . THR B 119 ? 1.1896 0.9373 1.0384 0.0169 0.1283 -0.0049 119 THR B O 4232 C CB . THR B 119 ? 1.2287 0.9656 1.0967 -0.0089 0.1362 -0.0106 119 THR B CB 4233 O OG1 . THR B 119 ? 1.3185 1.0609 1.1933 -0.0160 0.1326 -0.0217 119 THR B OG1 4234 C CG2 . THR B 119 ? 1.2326 0.9653 1.1065 -0.0161 0.1419 -0.0058 119 THR B CG2 4235 N N . GLU B 120 ? 1.1005 0.8665 0.9592 0.0032 0.1222 -0.0192 120 GLU B N 4236 C CA . GLU B 120 ? 1.0828 0.8521 0.9380 0.0109 0.1199 -0.0230 120 GLU B CA 4237 C C . GLU B 120 ? 1.0728 0.8560 0.9242 0.0181 0.1156 -0.0191 120 GLU B C 4238 O O . GLU B 120 ? 1.0447 0.8261 0.8926 0.0283 0.1152 -0.0181 120 GLU B O 4239 C CB . GLU B 120 ? 1.0715 0.8489 0.9299 0.0053 0.1173 -0.0332 120 GLU B CB 4240 C CG . GLU B 120 ? 1.1343 0.9130 0.9902 0.0133 0.1169 -0.0380 120 GLU B CG 4241 C CD . GLU B 120 ? 1.1833 0.9696 1.0407 0.0086 0.1155 -0.0483 120 GLU B CD 4242 O OE1 . GLU B 120 ? 1.1690 0.9664 1.0270 0.0005 0.1125 -0.0507 120 GLU B OE1 4243 O OE2 . GLU B 120 ? 1.1981 0.9789 1.0552 0.0136 0.1173 -0.0541 120 GLU B OE2 4244 N N . VAL B 121 ? 1.0488 0.8459 0.9020 0.0133 0.1118 -0.0174 121 VAL B N 4245 C CA . VAL B 121 ? 1.0137 0.8243 0.8652 0.0194 0.1072 -0.0145 121 VAL B CA 4246 C C . VAL B 121 ? 1.0467 0.8497 0.8926 0.0290 0.1088 -0.0068 121 VAL B C 4247 O O . VAL B 121 ? 1.0393 0.8476 0.8827 0.0386 0.1059 -0.0060 121 VAL B O 4248 C CB . VAL B 121 ? 1.0182 0.8429 0.8730 0.0123 0.1027 -0.0142 121 VAL B CB 4249 C CG1 . VAL B 121 ? 1.0359 0.8728 0.8902 0.0188 0.0981 -0.0111 121 VAL B CG1 4250 C CG2 . VAL B 121 ? 1.0370 0.8699 0.8946 0.0044 0.1004 -0.0211 121 VAL B CG2 4251 N N . ALA B 122 ? 1.0574 0.8484 0.9014 0.0267 0.1136 -0.0013 122 ALA B N 4252 C CA . ALA B 122 ? 1.1096 0.8917 0.9458 0.0359 0.1162 0.0069 122 ALA B CA 4253 C C . ALA B 122 ? 1.1566 0.9278 0.9872 0.0469 0.1173 0.0072 122 ALA B C 4254 O O . ALA B 122 ? 1.1586 0.9334 0.9836 0.0582 0.1140 0.0098 122 ALA B O 4255 C CB . ALA B 122 ? 1.1290 0.8977 0.9647 0.0302 0.1234 0.0125 122 ALA B CB 4256 N N . GLN B 123 ? 1.2586 1.0166 1.0914 0.0440 0.1212 0.0036 123 GLN B N 4257 C CA . GLN B 123 ? 1.3293 1.0753 1.1579 0.0541 0.1222 0.0028 123 GLN B CA 4258 C C . GLN B 123 ? 1.3581 1.1198 1.1883 0.0617 0.1158 -0.0030 123 GLN B C 4259 O O . GLN B 123 ? 1.4068 1.1649 1.2322 0.0741 0.1141 -0.0016 123 GLN B O 4260 C CB . GLN B 123 ? 1.3249 1.0572 1.1584 0.0479 0.1266 -0.0025 123 GLN B CB 4261 C CG . GLN B 123 ? 1.3569 1.0742 1.1867 0.0583 0.1279 -0.0037 123 GLN B CG 4262 C CD . GLN B 123 ? 1.3958 1.0945 1.2154 0.0680 0.1316 0.0070 123 GLN B CD 4263 O OE1 . GLN B 123 ? 1.4531 1.1417 1.2700 0.0631 0.1369 0.0147 123 GLN B OE1 4264 N NE2 . GLN B 123 ? 1.3594 1.0536 1.1728 0.0821 0.1289 0.0077 123 GLN B NE2 4265 N N . SER B 124 ? 1.3370 1.1162 1.1745 0.0540 0.1123 -0.0097 124 SER B N 4266 C CA . SER B 124 ? 1.2687 1.0643 1.1101 0.0587 0.1074 -0.0158 124 SER B CA 4267 C C . SER B 124 ? 1.2301 1.0358 1.0693 0.0678 0.1026 -0.0118 124 SER B C 4268 O O . SER B 124 ? 1.2291 1.0394 1.0688 0.0783 0.0997 -0.0145 124 SER B O 4269 C CB . SER B 124 ? 1.2660 1.0768 1.1141 0.0473 0.1057 -0.0218 124 SER B CB 4270 O OG . SER B 124 ? 1.2675 1.0930 1.1201 0.0505 0.1029 -0.0278 124 SER B OG 4271 N N . ASN B 125 ? 1.2121 1.0223 1.0498 0.0641 0.1014 -0.0065 125 ASN B N 4272 C CA . ASN B 125 ? 1.1862 1.0059 1.0215 0.0726 0.0965 -0.0032 125 ASN B CA 4273 C C . ASN B 125 ? 1.2056 1.0121 1.0307 0.0864 0.0973 0.0020 125 ASN B C 4274 O O . ASN B 125 ? 1.1552 0.9693 0.9791 0.0979 0.0921 0.0009 125 ASN B O 4275 C CB . ASN B 125 ? 1.1916 1.0160 1.0262 0.0662 0.0959 0.0013 125 ASN B CB 4276 C CG . ASN B 125 ? 1.1804 1.0200 1.0241 0.0551 0.0928 -0.0033 125 ASN B CG 4277 O OD1 . ASN B 125 ? 1.2607 1.0996 1.1057 0.0457 0.0943 -0.0016 125 ASN B OD1 4278 N ND2 . ASN B 125 ? 1.1492 1.0027 0.9996 0.0563 0.0885 -0.0090 125 ASN B ND2 4279 N N . PHE B 126 ? 1.1980 0.9844 1.0159 0.0853 0.1038 0.0080 126 PHE B N 4280 C CA . PHE B 126 ? 1.2219 0.9918 1.0280 0.0981 0.1058 0.0147 126 PHE B CA 4281 C C . PHE B 126 ? 1.2644 1.0334 1.0712 0.1093 0.1025 0.0095 126 PHE B C 4282 O O . PHE B 126 ? 1.3451 1.1142 1.1448 0.1235 0.0983 0.0116 126 PHE B O 4283 C CB . PHE B 126 ? 1.2270 0.9737 1.0275 0.0932 0.1146 0.0214 126 PHE B CB 4284 C CG . PHE B 126 ? 1.2652 0.9919 1.0526 0.1063 0.1174 0.0290 126 PHE B CG 4285 C CD1 . PHE B 126 ? 1.3253 1.0524 1.1005 0.1175 0.1154 0.0363 126 PHE B CD1 4286 C CD2 . PHE B 126 ? 1.2837 0.9909 1.0700 0.1085 0.1214 0.0286 126 PHE B CD2 4287 C CE1 . PHE B 126 ? 1.3785 1.0860 1.1390 0.1308 0.1177 0.0443 126 PHE B CE1 4288 C CE2 . PHE B 126 ? 1.3751 1.0620 1.1482 0.1215 0.1236 0.0364 126 PHE B CE2 4289 C CZ . PHE B 126 ? 1.4035 1.0903 1.1629 0.1328 0.1218 0.0447 126 PHE B CZ 4290 N N . GLU B 127 ? 1.2106 0.9791 1.0255 0.1036 0.1040 0.0021 127 GLU B N 4291 C CA . GLU B 127 ? 1.2449 1.0130 1.0621 0.1137 0.1015 -0.0040 127 GLU B CA 4292 C C . GLU B 127 ? 1.2222 1.0140 1.0468 0.1197 0.0940 -0.0105 127 GLU B C 4293 O O . GLU B 127 ? 1.2474 1.0406 1.0713 0.1331 0.0900 -0.0133 127 GLU B O 4294 C CB . GLU B 127 ? 1.2573 1.0202 1.0816 0.1059 0.1054 -0.0112 127 GLU B CB 4295 C CG . GLU B 127 ? 1.2727 1.0093 1.0914 0.1030 0.1124 -0.0064 127 GLU B CG 4296 C CD . GLU B 127 ? 1.3079 1.0378 1.1329 0.1005 0.1147 -0.0151 127 GLU B CD 4297 O OE1 . GLU B 127 ? 1.2911 1.0293 1.1200 0.1087 0.1112 -0.0224 127 GLU B OE1 4298 O OE2 . GLU B 127 ? 1.3254 1.0430 1.1523 0.0905 0.1198 -0.0156 127 GLU B OE2 4299 N N . ALA B 128 ? 1.1843 0.9943 1.0167 0.1098 0.0920 -0.0133 128 ALA B N 4300 C CA . ALA B 128 ? 1.1997 1.0323 1.0409 0.1136 0.0853 -0.0190 128 ALA B CA 4301 C C . ALA B 128 ? 1.1729 1.0080 1.0076 0.1263 0.0797 -0.0148 128 ALA B C 4302 O O . ALA B 128 ? 1.1073 0.9548 0.9472 0.1363 0.0736 -0.0202 128 ALA B O 4303 C CB . ALA B 128 ? 1.2195 1.0674 1.0691 0.0996 0.0849 -0.0212 128 ALA B CB 4304 N N . LEU B 129 ? 1.2405 1.0644 1.0640 0.1258 0.0818 -0.0058 129 LEU B N 4305 C CA . LEU B 129 ? 1.2499 1.0737 1.0635 0.1386 0.0773 -0.0009 129 LEU B CA 4306 C C . LEU B 129 ? 1.3505 1.1609 1.1549 0.1548 0.0762 0.0004 129 LEU B C 4307 O O . LEU B 129 ? 1.4408 1.2596 1.2436 0.1686 0.0690 -0.0020 129 LEU B O 4308 C CB . LEU B 129 ? 1.2317 1.0451 1.0346 0.1338 0.0819 0.0088 129 LEU B CB 4309 C CG . LEU B 129 ? 1.2595 1.0819 1.0562 0.1400 0.0771 0.0121 129 LEU B CG 4310 C CD1 . LEU B 129 ? 1.2432 1.0901 1.0541 0.1354 0.0700 0.0042 129 LEU B CD1 4311 C CD2 . LEU B 129 ? 1.2739 1.0849 1.0616 0.1329 0.0841 0.0213 129 LEU B CD2 4312 N N . GLN B 130 ? 1.3583 1.1482 1.1576 0.1536 0.0827 0.0035 130 GLN B N 4313 C CA . GLN B 130 ? 1.3551 1.1315 1.1477 0.1685 0.0814 0.0036 130 GLN B CA 4314 C C . GLN B 130 ? 1.3499 1.1450 1.1555 0.1759 0.0743 -0.0082 130 GLN B C 4315 O O . GLN B 130 ? 1.4385 1.2371 1.2403 0.1919 0.0675 -0.0097 130 GLN B O 4316 C CB . GLN B 130 ? 1.3539 1.1069 1.1435 0.1635 0.0895 0.0064 130 GLN B CB 4317 C CG . GLN B 130 ? 1.3743 1.1045 1.1498 0.1605 0.0970 0.0190 130 GLN B CG 4318 C CD . GLN B 130 ? 1.4152 1.1186 1.1865 0.1601 0.1040 0.0223 130 GLN B CD 4319 O OE1 . GLN B 130 ? 1.4597 1.1629 1.2418 0.1526 0.1059 0.0147 130 GLN B OE1 4320 N NE2 . GLN B 130 ? 1.4550 1.1353 1.2102 0.1682 0.1080 0.0338 130 GLN B NE2 4321 N N . ASP B 131 ? 1.3299 1.1378 1.1508 0.1646 0.0758 -0.0169 131 ASP B N 4322 C CA . ASP B 131 ? 1.3323 1.1597 1.1677 0.1697 0.0707 -0.0286 131 ASP B CA 4323 C C . ASP B 131 ? 1.2950 1.1435 1.1360 0.1766 0.0622 -0.0321 131 ASP B C 4324 O O . ASP B 131 ? 1.3217 1.1833 1.1719 0.1868 0.0564 -0.0406 131 ASP B O 4325 C CB . ASP B 131 ? 1.3414 1.1806 1.1910 0.1544 0.0749 -0.0362 131 ASP B CB 4326 C CG . ASP B 131 ? 1.4244 1.2797 1.2883 0.1597 0.0724 -0.0483 131 ASP B CG 4327 O OD1 . ASP B 131 ? 1.4646 1.3116 1.3265 0.1726 0.0708 -0.0510 131 ASP B OD1 4328 O OD2 . ASP B 131 ? 1.4403 1.3165 1.3181 0.1509 0.0723 -0.0550 131 ASP B OD2 4329 N N . PHE B 132 ? 1.3175 1.1701 1.1547 0.1710 0.0613 -0.0267 132 PHE B N 4330 C CA . PHE B 132 ? 1.2678 1.1399 1.1107 0.1769 0.0530 -0.0305 132 PHE B CA 4331 C C . PHE B 132 ? 1.3247 1.1927 1.1577 0.1972 0.0461 -0.0299 132 PHE B C 4332 O O . PHE B 132 ? 1.2997 1.1852 1.1432 0.2067 0.0381 -0.0388 132 PHE B O 4333 C CB . PHE B 132 ? 1.1987 1.0727 1.0370 0.1682 0.0535 -0.0242 132 PHE B CB 4334 C CG . PHE B 132 ? 1.1823 1.0743 1.0252 0.1754 0.0445 -0.0281 132 PHE B CG 4335 C CD1 . PHE B 132 ? 1.1361 1.0513 0.9990 0.1706 0.0399 -0.0382 132 PHE B CD1 4336 C CD2 . PHE B 132 ? 1.1906 1.0763 1.0178 0.1870 0.0408 -0.0220 132 PHE B CD2 4337 C CE1 . PHE B 132 ? 1.1009 1.0326 0.9700 0.1769 0.0312 -0.0429 132 PHE B CE1 4338 C CE2 . PHE B 132 ? 1.1696 1.0726 1.0013 0.1941 0.0318 -0.0270 132 PHE B CE2 4339 C CZ . PHE B 132 ? 1.1266 1.0526 0.9802 0.1890 0.0266 -0.0379 132 PHE B CZ 4340 N N . PHE B 133 ? 1.4378 1.2824 1.2506 0.2040 0.0493 -0.0192 133 PHE B N 4341 C CA . PHE B 133 ? 1.5089 1.3464 1.3074 0.2243 0.0430 -0.0162 133 PHE B CA 4342 C C . PHE B 133 ? 1.5029 1.3370 1.3042 0.2377 0.0394 -0.0223 133 PHE B C 4343 O O . PHE B 133 ? 1.5044 1.3406 1.2992 0.2560 0.0311 -0.0240 133 PHE B O 4344 C CB . PHE B 133 ? 1.5302 1.3429 1.3050 0.2268 0.0487 -0.0016 133 PHE B CB 4345 C CG . PHE B 133 ? 1.5159 1.3346 1.2867 0.2185 0.0501 0.0034 133 PHE B CG 4346 C CD1 . PHE B 133 ? 1.4903 1.3291 1.2643 0.2249 0.0411 -0.0015 133 PHE B CD1 4347 C CD2 . PHE B 133 ? 1.4993 1.3043 1.2643 0.2046 0.0599 0.0122 133 PHE B CD2 4348 C CE1 . PHE B 133 ? 1.4771 1.3216 1.2477 0.2179 0.0420 0.0022 133 PHE B CE1 4349 C CE2 . PHE B 133 ? 1.4931 1.3047 1.2554 0.1974 0.0610 0.0161 133 PHE B CE2 4350 C CZ . PHE B 133 ? 1.4855 1.3166 1.2502 0.2043 0.0521 0.0112 133 PHE B CZ 4351 N N . ARG B 134 ? 1.4739 1.3037 1.2848 0.2296 0.0451 -0.0263 134 ARG B N 4352 C CA . ARG B 134 ? 1.5094 1.3410 1.3278 0.2412 0.0415 -0.0350 134 ARG B CA 4353 C C . ARG B 134 ? 1.5111 1.3737 1.3500 0.2448 0.0331 -0.0487 134 ARG B C 4354 O O . ARG B 134 ? 1.5770 1.4460 1.4193 0.2613 0.0253 -0.0556 134 ARG B O 4355 C CB . ARG B 134 ? 1.4672 1.2906 1.2933 0.2306 0.0496 -0.0381 134 ARG B CB 4356 C CG . ARG B 134 ? 1.4975 1.2901 1.3076 0.2263 0.0581 -0.0268 134 ARG B CG 4357 C CD . ARG B 134 ? 1.5346 1.3212 1.3539 0.2193 0.0639 -0.0330 134 ARG B CD 4358 N NE . ARG B 134 ? 1.5442 1.3106 1.3565 0.2055 0.0734 -0.0252 134 ARG B NE 4359 C CZ . ARG B 134 ? 1.5131 1.2851 1.3355 0.1884 0.0792 -0.0295 134 ARG B CZ 4360 N NH1 . ARG B 134 ? 1.3997 1.1959 1.2385 0.1821 0.0778 -0.0405 134 ARG B NH1 4361 N NH2 . ARG B 134 ? 1.5304 1.2832 1.3463 0.1777 0.0867 -0.0227 134 ARG B NH2 4362 N N . LEU B 135 ? 1.4124 1.2938 1.2654 0.2293 0.0347 -0.0526 135 LEU B N 4363 C CA . LEU B 135 ? 1.4359 1.3468 1.3109 0.2291 0.0285 -0.0652 135 LEU B CA 4364 C C . LEU B 135 ? 1.4170 1.3393 1.2898 0.2393 0.0187 -0.0660 135 LEU B C 4365 O O . LEU B 135 ? 1.4656 1.4084 1.3533 0.2482 0.0103 -0.0771 135 LEU B O 4366 C CB . LEU B 135 ? 1.4546 1.3787 1.3447 0.2079 0.0349 -0.0681 135 LEU B CB 4367 C CG . LEU B 135 ? 1.4398 1.3571 1.3341 0.1975 0.0440 -0.0698 135 LEU B CG 4368 C CD1 . LEU B 135 ? 1.4189 1.3403 1.3179 0.1767 0.0510 -0.0673 135 LEU B CD1 4369 C CD2 . LEU B 135 ? 1.4405 1.3741 1.3527 0.2034 0.0422 -0.0828 135 LEU B CD2 4370 N N . PHE B 136 ? 1.4255 1.3354 1.2805 0.2380 0.0197 -0.0550 136 PHE B N 4371 C CA . PHE B 136 ? 1.4350 1.3542 1.2849 0.2480 0.0107 -0.0552 136 PHE B CA 4372 C C . PHE B 136 ? 1.4876 1.3841 1.3095 0.2633 0.0095 -0.0440 136 PHE B C 4373 O O . PHE B 136 ? 1.5434 1.4316 1.3505 0.2604 0.0119 -0.0347 136 PHE B O 4374 C CB . PHE B 136 ? 1.3789 1.3065 1.2332 0.2323 0.0130 -0.0526 136 PHE B CB 4375 C CG . PHE B 136 ? 1.3209 1.2732 1.2020 0.2201 0.0117 -0.0637 136 PHE B CG 4376 C CD1 . PHE B 136 ? 1.2508 1.2036 1.1428 0.2032 0.0204 -0.0645 136 PHE B CD1 4377 C CD2 . PHE B 136 ? 1.2599 1.2344 1.1551 0.2253 0.0020 -0.0732 136 PHE B CD2 4378 C CE1 . PHE B 136 ? 1.1687 1.1427 1.0836 0.1917 0.0203 -0.0731 136 PHE B CE1 4379 C CE2 . PHE B 136 ? 1.2469 1.2426 1.1675 0.2131 0.0019 -0.0825 136 PHE B CE2 4380 C CZ . PHE B 136 ? 1.2018 1.1967 1.1315 0.1962 0.0115 -0.0818 136 PHE B CZ 4381 N N . PRO B 137 ? 1.5288 1.4153 1.3430 0.2800 0.0060 -0.0448 137 PRO B N 4382 C CA . PRO B 137 ? 1.5573 1.4190 1.3426 0.2949 0.0059 -0.0325 137 PRO B CA 4383 C C . PRO B 137 ? 1.5411 1.4090 1.3127 0.3076 -0.0025 -0.0304 137 PRO B C 4384 O O . PRO B 137 ? 1.4673 1.3155 1.2138 0.3123 0.0012 -0.0172 137 PRO B O 4385 C CB . PRO B 137 ? 1.6165 1.4708 1.4010 0.3112 0.0016 -0.0369 137 PRO B CB 4386 C CG . PRO B 137 ? 1.5905 1.4731 1.4045 0.3091 -0.0040 -0.0540 137 PRO B CG 4387 C CD . PRO B 137 ? 1.5522 1.4490 1.3837 0.2859 0.0026 -0.0567 137 PRO B CD 4388 N N . GLU B 138 ? 1.5063 1.4017 1.2951 0.3123 -0.0132 -0.0436 138 GLU B N 4389 C CA . GLU B 138 ? 1.5062 1.4118 1.2854 0.3247 -0.0229 -0.0448 138 GLU B CA 4390 C C . GLU B 138 ? 1.4852 1.3889 1.2557 0.3127 -0.0176 -0.0366 138 GLU B C 4391 O O . GLU B 138 ? 1.4556 1.3648 1.2143 0.3229 -0.0243 -0.0361 138 GLU B O 4392 C CB . GLU B 138 ? 1.4638 1.4012 1.2688 0.3305 -0.0356 -0.0631 138 GLU B CB 4393 C CG . GLU B 138 ? 1.3980 1.3574 1.2332 0.3098 -0.0330 -0.0725 138 GLU B CG 4394 C CD . GLU B 138 ? 1.3531 1.3162 1.2089 0.2989 -0.0267 -0.0782 138 GLU B CD 4395 O OE1 . GLU B 138 ? 1.2981 1.2398 1.1427 0.2957 -0.0179 -0.0696 138 GLU B OE1 4396 O OE2 . GLU B 138 ? 1.2580 1.2455 1.1418 0.2929 -0.0302 -0.0916 138 GLU B OE2 4397 N N . TYR B 139 ? 1.4809 1.3785 1.2581 0.2916 -0.0062 -0.0315 139 TYR B N 4398 C CA . TYR B 139 ? 1.4770 1.3720 1.2476 0.2789 -0.0002 -0.0239 139 TYR B CA 4399 C C . TYR B 139 ? 1.4990 1.3653 1.2467 0.2746 0.0118 -0.0075 139 TYR B C 4400 O O . TYR B 139 ? 1.4228 1.2857 1.1657 0.2630 0.0183 -0.0008 139 TYR B O 4401 C CB . TYR B 139 ? 1.3948 1.3062 1.1909 0.2578 0.0027 -0.0308 139 TYR B CB 4402 C CG . TYR B 139 ? 1.3523 1.2921 1.1702 0.2597 -0.0082 -0.0452 139 TYR B CG 4403 C CD1 . TYR B 139 ? 1.3830 1.3334 1.1956 0.2689 -0.0168 -0.0480 139 TYR B CD1 4404 C CD2 . TYR B 139 ? 1.3061 1.2623 1.1504 0.2522 -0.0096 -0.0565 139 TYR B CD2 4405 C CE1 . TYR B 139 ? 1.3539 1.3300 1.1885 0.2704 -0.0271 -0.0621 139 TYR B CE1 4406 C CE2 . TYR B 139 ? 1.2880 1.2695 1.1541 0.2529 -0.0188 -0.0697 139 TYR B CE2 4407 C CZ . TYR B 139 ? 1.3292 1.3205 1.1911 0.2620 -0.0279 -0.0727 139 TYR B CZ 4408 O OH . TYR B 139 ? 1.3204 1.3368 1.2060 0.2624 -0.0373 -0.0868 139 TYR B OH 4409 N N . LYS B 140 ? 1.5329 1.3787 1.2678 0.2839 0.0148 -0.0016 140 LYS B N 4410 C CA . LYS B 140 ? 1.5970 1.4137 1.3107 0.2809 0.0264 0.0139 140 LYS B CA 4411 C C . LYS B 140 ? 1.6105 1.4187 1.2988 0.2902 0.0271 0.0244 140 LYS B C 4412 O O . LYS B 140 ? 1.5541 1.3443 1.2291 0.2823 0.0382 0.0367 140 LYS B O 4413 C CB . LYS B 140 ? 1.6781 1.4736 1.3828 0.2914 0.0282 0.0176 140 LYS B CB 4414 C CG . LYS B 140 ? 1.6984 1.4936 1.4230 0.2795 0.0324 0.0112 140 LYS B CG 4415 C CD . LYS B 140 ? 1.7616 1.5326 1.4750 0.2908 0.0346 0.0160 140 LYS B CD 4416 C CE . LYS B 140 ? 1.7282 1.4961 1.4590 0.2783 0.0404 0.0104 140 LYS B CE 4417 N NZ . LYS B 140 ? 1.7373 1.4786 1.4566 0.2886 0.0432 0.0158 140 LYS B NZ 4418 N N . ASN B 141 ? 1.6505 1.4720 1.3320 0.3073 0.0156 0.0193 141 ASN B N 4419 C CA . ASN B 141 ? 1.7277 1.5422 1.3829 0.3184 0.0157 0.0287 141 ASN B CA 4420 C C . ASN B 141 ? 1.6174 1.4470 1.2781 0.3065 0.0173 0.0274 141 ASN B C 4421 O O . ASN B 141 ? 1.5078 1.3274 1.1481 0.3078 0.0236 0.0381 141 ASN B O 4422 C CB . ASN B 141 ? 1.8459 1.6689 1.4900 0.3433 0.0016 0.0229 141 ASN B CB 4423 C CG . ASN B 141 ? 1.9442 1.7492 1.5773 0.3587 -0.0004 0.0261 141 ASN B CG 4424 O OD1 . ASN B 141 ? 1.9728 1.7906 1.6137 0.3731 -0.0128 0.0149 141 ASN B OD1 4425 N ND2 . ASN B 141 ? 1.9569 1.7318 1.5731 0.3557 0.0117 0.0410 141 ASN B ND2 4426 N N . ASN B 142 ? 1.5100 1.3632 1.1982 0.2951 0.0121 0.0144 142 ASN B N 4427 C CA . ASN B 142 ? 1.4739 1.3441 1.1702 0.2859 0.0107 0.0105 142 ASN B CA 4428 C C . ASN B 142 ? 1.4357 1.2925 1.1249 0.2703 0.0243 0.0221 142 ASN B C 4429 O O . ASN B 142 ? 1.3861 1.2254 1.0751 0.2600 0.0346 0.0294 142 ASN B O 4430 C CB . ASN B 142 ? 1.4823 1.3764 1.2110 0.2743 0.0044 -0.0041 142 ASN B CB 4431 C CG . ASN B 142 ? 1.4860 1.3967 1.2262 0.2885 -0.0090 -0.0174 142 ASN B CG 4432 O OD1 . ASN B 142 ? 1.5562 1.4577 1.2895 0.3007 -0.0109 -0.0167 142 ASN B OD1 4433 N ND2 . ASN B 142 ? 1.4046 1.3401 1.1642 0.2869 -0.0184 -0.0301 142 ASN B ND2 4434 N N . LYS B 143 ? 1.4298 1.2953 1.1139 0.2689 0.0240 0.0229 143 LYS B N 4435 C CA . LYS B 143 ? 1.4289 1.2860 1.1101 0.2534 0.0360 0.0317 143 LYS B CA 4436 C C . LYS B 143 ? 1.3340 1.1974 1.0415 0.2326 0.0390 0.0262 143 LYS B C 4437 O O . LYS B 143 ? 1.2906 1.1730 1.0189 0.2292 0.0304 0.0142 143 LYS B O 4438 C CB . LYS B 143 ? 1.4512 1.3216 1.1266 0.2558 0.0332 0.0302 143 LYS B CB 4439 C CG . LYS B 143 ? 1.5066 1.3729 1.1542 0.2768 0.0301 0.0352 143 LYS B CG 4440 C CD . LYS B 143 ? 1.5634 1.4406 1.2047 0.2765 0.0305 0.0350 143 LYS B CD 4441 C CE . LYS B 143 ? 1.6113 1.4966 1.2331 0.2989 0.0205 0.0320 143 LYS B CE 4442 N NZ . LYS B 143 ? 1.6089 1.5024 1.2203 0.2999 0.0227 0.0332 143 LYS B NZ 4443 N N . LEU B 144 ? 1.2754 1.1222 0.9817 0.2193 0.0512 0.0348 144 LEU B N 4444 C CA . LEU B 144 ? 1.2438 1.0938 0.9719 0.2007 0.0545 0.0303 144 LEU B CA 4445 C C . LEU B 144 ? 1.2562 1.1072 0.9890 0.1847 0.0618 0.0337 144 LEU B C 4446 O O . LEU B 144 ? 1.3261 1.1613 1.0464 0.1813 0.0721 0.0440 144 LEU B O 4447 C CB . LEU B 144 ? 1.2562 1.0869 0.9826 0.1982 0.0613 0.0349 144 LEU B CB 4448 C CG . LEU B 144 ? 1.2415 1.0718 0.9860 0.1791 0.0666 0.0319 144 LEU B CG 4449 C CD1 . LEU B 144 ? 1.1944 1.0462 0.9605 0.1746 0.0580 0.0192 144 LEU B CD1 4450 C CD2 . LEU B 144 ? 1.2261 1.0352 0.9664 0.1780 0.0739 0.0368 144 LEU B CD2 4451 N N . PHE B 145 ? 1.2007 1.0701 0.9524 0.1748 0.0564 0.0250 145 PHE B N 4452 C CA . PHE B 145 ? 1.1920 1.0640 0.9509 0.1596 0.0617 0.0265 145 PHE B CA 4453 C C . PHE B 145 ? 1.1861 1.0600 0.9637 0.1433 0.0634 0.0222 145 PHE B C 4454 O O . PHE B 145 ? 1.1399 1.0232 0.9305 0.1425 0.0572 0.0143 145 PHE B O 4455 C CB . PHE B 145 ? 1.1656 1.0563 0.9293 0.1617 0.0541 0.0206 145 PHE B CB 4456 C CG . PHE B 145 ? 1.1598 1.0496 0.9038 0.1769 0.0531 0.0247 145 PHE B CG 4457 C CD1 . PHE B 145 ? 1.1574 1.0393 0.8883 0.1750 0.0622 0.0333 145 PHE B CD1 4458 C CD2 . PHE B 145 ? 1.1242 1.0217 0.8628 0.1934 0.0433 0.0196 145 PHE B CD2 4459 C CE1 . PHE B 145 ? 1.1643 1.0456 0.8749 0.1896 0.0620 0.0375 145 PHE B CE1 4460 C CE2 . PHE B 145 ? 1.1700 1.0669 0.8883 0.2086 0.0419 0.0231 145 PHE B CE2 4461 C CZ . PHE B 145 ? 1.1730 1.0615 0.8762 0.2068 0.0516 0.0325 145 PHE B CZ 4462 N N . LEU B 146 ? 1.1688 1.0343 0.9474 0.1306 0.0720 0.0272 146 LEU B N 4463 C CA . LEU B 146 ? 1.1307 0.9972 0.9244 0.1150 0.0740 0.0237 146 LEU B CA 4464 C C . LEU B 146 ? 1.1124 0.9921 0.9163 0.1055 0.0714 0.0204 146 LEU B C 4465 O O . LEU B 146 ? 1.0628 0.9403 0.8612 0.1035 0.0759 0.0250 146 LEU B O 4466 C CB . LEU B 146 ? 1.1299 0.9770 0.9183 0.1079 0.0850 0.0307 146 LEU B CB 4467 C CG . LEU B 146 ? 1.1414 0.9704 0.9166 0.1177 0.0895 0.0364 146 LEU B CG 4468 C CD1 . LEU B 146 ? 1.1475 0.9578 0.9204 0.1084 0.1006 0.0428 146 LEU B CD1 4469 C CD2 . LEU B 146 ? 1.1657 0.9980 0.9471 0.1227 0.0836 0.0298 146 LEU B CD2 4470 N N . THR B 147 ? 1.0980 0.9913 0.9169 0.1000 0.0642 0.0126 147 THR B N 4471 C CA . THR B 147 ? 1.0574 0.9626 0.8866 0.0917 0.0605 0.0092 147 THR B CA 4472 C C . THR B 147 ? 1.0266 0.9342 0.8689 0.0784 0.0601 0.0056 147 THR B C 4473 O O . THR B 147 ? 1.0085 0.9152 0.8549 0.0778 0.0596 0.0029 147 THR B O 4474 C CB . THR B 147 ? 1.0737 0.9949 0.9084 0.0993 0.0504 0.0029 147 THR B CB 4475 O OG1 . THR B 147 ? 1.0760 1.0044 0.9216 0.0996 0.0448 -0.0034 147 THR B OG1 4476 C CG2 . THR B 147 ? 1.0980 1.0185 0.9181 0.1148 0.0491 0.0052 147 THR B CG2 4477 N N . GLY B 148 ? 1.0300 0.9410 0.8784 0.0685 0.0603 0.0053 148 GLY B N 4478 C CA . GLY B 148 ? 0.9886 0.9015 0.8473 0.0562 0.0595 0.0025 148 GLY B CA 4479 C C . GLY B 148 ? 0.9591 0.8794 0.8250 0.0488 0.0561 0.0009 148 GLY B C 4480 O O . GLY B 148 ? 0.9062 0.8316 0.7706 0.0532 0.0541 0.0013 148 GLY B O 4481 N N . GLU B 149 ? 0.9494 0.8706 0.8227 0.0383 0.0551 -0.0009 149 GLU B N 4482 C CA . GLU B 149 ? 0.9438 0.8712 0.8243 0.0313 0.0509 -0.0026 149 GLU B CA 4483 C C . GLU B 149 ? 0.9090 0.8307 0.7910 0.0205 0.0541 -0.0022 149 GLU B C 4484 O O . GLU B 149 ? 0.8761 0.7911 0.7554 0.0180 0.0582 -0.0019 149 GLU B O 4485 C CB . GLU B 149 ? 0.9834 0.9207 0.8729 0.0313 0.0428 -0.0067 149 GLU B CB 4486 C CG . GLU B 149 ? 1.0050 0.9484 0.9020 0.0260 0.0369 -0.0085 149 GLU B CG 4487 C CD . GLU B 149 ? 1.0117 0.9617 0.9179 0.0241 0.0303 -0.0117 149 GLU B CD 4488 O OE1 . GLU B 149 ? 0.9447 0.9013 0.8549 0.0313 0.0260 -0.0146 149 GLU B OE1 4489 O OE2 . GLU B 149 ? 1.0831 1.0314 0.9924 0.0155 0.0294 -0.0114 149 GLU B OE2 4490 N N . SER B 150 ? 0.9845 0.9093 0.8709 0.0147 0.0519 -0.0029 150 SER B N 4491 C CA . SER B 150 ? 1.0323 0.9543 0.9214 0.0048 0.0521 -0.0041 150 SER B CA 4492 C C . SER B 150 ? 0.9704 0.8819 0.8548 0.0017 0.0603 -0.0026 150 SER B C 4493 O O . SER B 150 ? 0.9489 0.8560 0.8303 0.0044 0.0659 -0.0001 150 SER B O 4494 C CB . SER B 150 ? 1.0820 1.0067 0.9738 0.0014 0.0475 -0.0059 150 SER B CB 4495 O OG . SER B 150 ? 1.1597 1.0827 1.0525 -0.0070 0.0461 -0.0070 150 SER B OG 4496 N N . TYR B 151 ? 0.9768 0.8838 0.8603 -0.0035 0.0615 -0.0042 151 TYR B N 4497 C CA . TYR B 151 ? 0.9244 0.8209 0.8045 -0.0062 0.0688 -0.0039 151 TYR B CA 4498 C C . TYR B 151 ? 0.9250 0.8138 0.7989 0.0015 0.0749 -0.0005 151 TYR B C 4499 O O . TYR B 151 ? 0.9914 0.8698 0.8629 0.0001 0.0817 0.0006 151 TYR B O 4500 C CB . TYR B 151 ? 0.8792 0.7730 0.7583 -0.0116 0.0686 -0.0071 151 TYR B CB 4501 C CG . TYR B 151 ? 0.8321 0.7159 0.7103 -0.0159 0.0747 -0.0086 151 TYR B CG 4502 C CD1 . TYR B 151 ? 0.8125 0.6965 0.6955 -0.0229 0.0743 -0.0111 151 TYR B CD1 4503 C CD2 . TYR B 151 ? 0.8174 0.6918 0.6913 -0.0127 0.0805 -0.0081 151 TYR B CD2 4504 C CE1 . TYR B 151 ? 0.8026 0.6777 0.6870 -0.0272 0.0797 -0.0134 151 TYR B CE1 4505 C CE2 . TYR B 151 ? 0.8250 0.6891 0.6994 -0.0168 0.0861 -0.0098 151 TYR B CE2 4506 C CZ . TYR B 151 ? 0.8000 0.6646 0.6802 -0.0244 0.0858 -0.0126 151 TYR B CZ 4507 O OH . TYR B 151 ? 0.8031 0.6578 0.6860 -0.0290 0.0911 -0.0154 151 TYR B OH 4508 N N . ALA B 152 ? 0.9065 0.7998 0.7781 0.0100 0.0723 0.0008 152 ALA B N 4509 C CA . ALA B 152 ? 0.9050 0.7912 0.7693 0.0191 0.0770 0.0043 152 ALA B CA 4510 C C . ALA B 152 ? 0.9669 0.8488 0.8273 0.0215 0.0819 0.0087 152 ALA B C 4511 O O . ALA B 152 ? 1.0460 0.9200 0.8982 0.0290 0.0866 0.0129 152 ALA B O 4512 C CB . ALA B 152 ? 0.8443 0.7381 0.7079 0.0281 0.0718 0.0033 152 ALA B CB 4513 N N . GLY B 153 ? 0.9693 0.8564 0.8352 0.0154 0.0810 0.0078 153 GLY B N 4514 C CA . GLY B 153 ? 0.9621 0.8447 0.8264 0.0146 0.0879 0.0115 153 GLY B CA 4515 C C . GLY B 153 ? 0.9494 0.8175 0.8122 0.0099 0.0967 0.0134 153 GLY B C 4516 O O . GLY B 153 ? 0.9382 0.7988 0.7976 0.0107 0.1047 0.0180 153 GLY B O 4517 N N . ILE B 154 ? 0.9196 0.7839 0.7851 0.0050 0.0955 0.0097 154 ILE B N 4518 C CA . ILE B 154 ? 0.9516 0.8012 0.8157 0.0019 0.1026 0.0103 154 ILE B CA 4519 C C . ILE B 154 ? 0.9623 0.8033 0.8180 0.0104 0.1041 0.0125 154 ILE B C 4520 O O . ILE B 154 ? 0.9643 0.7910 0.8144 0.0135 0.1113 0.0168 154 ILE B O 4521 C CB . ILE B 154 ? 0.9500 0.8005 0.8215 -0.0079 0.1003 0.0037 154 ILE B CB 4522 C CG1 . ILE B 154 ? 0.9456 0.8055 0.8262 -0.0157 0.0973 0.0004 154 ILE B CG1 4523 C CG2 . ILE B 154 ? 1.0210 0.8563 0.8925 -0.0111 0.1075 0.0031 154 ILE B CG2 4524 C CD1 . ILE B 154 ? 0.9461 0.8019 0.8310 -0.0190 0.1047 0.0029 154 ILE B CD1 4525 N N . TYR B 155 ? 0.9582 0.8073 0.8135 0.0142 0.0974 0.0094 155 TYR B N 4526 C CA . TYR B 155 ? 1.0082 0.8514 0.8573 0.0228 0.0980 0.0101 155 TYR B CA 4527 C C . TYR B 155 ? 1.0075 0.8434 0.8470 0.0334 0.1016 0.0168 155 TYR B C 4528 O O . TYR B 155 ? 1.0488 0.8708 0.8820 0.0383 0.1065 0.0198 155 TYR B O 4529 C CB . TYR B 155 ? 0.9958 0.8521 0.8476 0.0263 0.0903 0.0060 155 TYR B CB 4530 C CG . TYR B 155 ? 0.9890 0.8521 0.8473 0.0179 0.0870 0.0003 155 TYR B CG 4531 C CD1 . TYR B 155 ? 1.0044 0.8601 0.8640 0.0104 0.0905 -0.0025 155 TYR B CD1 4532 C CD2 . TYR B 155 ? 1.0331 0.9097 0.8959 0.0179 0.0804 -0.0023 155 TYR B CD2 4533 C CE1 . TYR B 155 ? 0.9512 0.8134 0.8143 0.0038 0.0874 -0.0076 155 TYR B CE1 4534 C CE2 . TYR B 155 ? 1.0069 0.8888 0.8736 0.0105 0.0781 -0.0065 155 TYR B CE2 4535 C CZ . TYR B 155 ? 0.9522 0.8270 0.8180 0.0039 0.0816 -0.0089 155 TYR B CZ 4536 O OH . TYR B 155 ? 0.9891 0.8694 0.8564 -0.0024 0.0793 -0.0127 155 TYR B OH 4537 N N . ILE B 156 ? 1.0082 0.8529 0.8459 0.0375 0.0988 0.0191 156 ILE B N 4538 C CA . ILE B 156 ? 1.0793 0.9206 0.9059 0.0500 0.1000 0.0247 156 ILE B CA 4539 C C . ILE B 156 ? 1.1144 0.9395 0.9321 0.0513 0.1101 0.0325 156 ILE B C 4540 O O . ILE B 156 ? 1.1443 0.9574 0.9514 0.0605 0.1132 0.0373 156 ILE B O 4541 C CB . ILE B 156 ? 1.0739 0.9308 0.9012 0.0546 0.0933 0.0235 156 ILE B CB 4542 C CG1 . ILE B 156 ? 1.0508 0.9210 0.8850 0.0569 0.0838 0.0169 156 ILE B CG1 4543 C CG2 . ILE B 156 ? 1.1394 0.9926 0.9534 0.0668 0.0955 0.0295 156 ILE B CG2 4544 C CD1 . ILE B 156 ? 1.0635 0.9311 0.8931 0.0673 0.0818 0.0161 156 ILE B CD1 4545 N N . PRO B 157 ? 1.1080 0.9326 0.9302 0.0424 0.1153 0.0341 157 PRO B N 4546 C CA . PRO B 157 ? 1.1161 0.9244 0.9310 0.0426 0.1262 0.0419 157 PRO B CA 4547 C C . PRO B 157 ? 1.1353 0.9255 0.9498 0.0402 0.1318 0.0429 157 PRO B C 4548 O O . PRO B 157 ? 1.2610 1.0349 1.0645 0.0468 0.1385 0.0503 157 PRO B O 4549 C CB . PRO B 157 ? 1.1171 0.9312 0.9420 0.0312 0.1301 0.0407 157 PRO B CB 4550 C CG . PRO B 157 ? 1.0816 0.9158 0.9133 0.0305 0.1203 0.0347 157 PRO B CG 4551 C CD . PRO B 157 ? 1.0770 0.9150 0.9107 0.0327 0.1120 0.0294 157 PRO B CD 4552 N N . THR B 158 ? 1.1314 0.9236 0.9568 0.0315 0.1289 0.0356 158 THR B N 4553 C CA . THR B 158 ? 1.1230 0.8986 0.9493 0.0289 0.1336 0.0348 158 THR B CA 4554 C C . THR B 158 ? 1.1388 0.9070 0.9549 0.0417 0.1314 0.0367 158 THR B C 4555 O O . THR B 158 ? 1.1870 0.9362 0.9967 0.0456 0.1376 0.0413 158 THR B O 4556 C CB . THR B 158 ? 1.0876 0.8690 0.9264 0.0182 0.1298 0.0253 158 THR B CB 4557 O OG1 . THR B 158 ? 1.1455 0.9422 0.9857 0.0210 0.1204 0.0197 158 THR B OG1 4558 C CG2 . THR B 158 ? 1.0896 0.8776 0.9391 0.0063 0.1313 0.0226 158 THR B CG2 4559 N N . LEU B 159 ? 1.0874 0.8704 0.9026 0.0484 0.1225 0.0330 159 LEU B N 4560 C CA . LEU B 159 ? 1.1208 0.9008 0.9280 0.0615 0.1191 0.0336 159 LEU B CA 4561 C C . LEU B 159 ? 1.1592 0.9274 0.9514 0.0727 0.1234 0.0433 159 LEU B C 4562 O O . LEU B 159 ? 1.2362 0.9882 1.0199 0.0807 0.1265 0.0472 159 LEU B O 4563 C CB . LEU B 159 ? 1.0821 0.8827 0.8934 0.0658 0.1089 0.0276 159 LEU B CB 4564 C CG . LEU B 159 ? 1.0924 0.8935 0.8973 0.0803 0.1042 0.0270 159 LEU B CG 4565 C CD1 . LEU B 159 ? 1.0894 0.8770 0.8939 0.0824 0.1071 0.0252 159 LEU B CD1 4566 C CD2 . LEU B 159 ? 1.0784 0.9007 0.8914 0.0823 0.0948 0.0198 159 LEU B CD2 4567 N N . ALA B 160 ? 1.1693 0.9458 0.9577 0.0739 0.1234 0.0470 160 ALA B N 4568 C CA . ALA B 160 ? 1.1767 0.9451 0.9486 0.0857 0.1269 0.0561 160 ALA B CA 4569 C C . ALA B 160 ? 1.2050 0.9485 0.9685 0.0855 0.1381 0.0650 160 ALA B C 4570 O O . ALA B 160 ? 1.2858 1.0160 1.0342 0.0981 0.1398 0.0718 160 ALA B O 4571 C CB . ALA B 160 ? 1.1687 0.9499 0.9400 0.0838 0.1270 0.0579 160 ALA B CB 4572 N N . VAL B 161 ? 1.1925 0.9293 0.9661 0.0715 0.1453 0.0645 161 VAL B N 4573 C CA . VAL B 161 ? 1.2877 0.9999 1.0571 0.0691 0.1564 0.0719 161 VAL B CA 4574 C C . VAL B 161 ? 1.2859 0.9823 1.0499 0.0774 0.1549 0.0718 161 VAL B C 4575 O O . VAL B 161 ? 1.3357 1.0119 1.0863 0.0858 0.1608 0.0809 161 VAL B O 4576 C CB . VAL B 161 ? 1.3024 1.0125 1.0880 0.0517 0.1625 0.0681 161 VAL B CB 4577 C CG1 . VAL B 161 ? 1.3197 1.0036 1.1046 0.0486 0.1724 0.0729 161 VAL B CG1 4578 C CG2 . VAL B 161 ? 1.3255 1.0459 1.1142 0.0450 0.1670 0.0707 161 VAL B CG2 4579 N N . LEU B 162 ? 1.3022 1.0079 1.0761 0.0759 0.1471 0.0616 162 LEU B N 4580 C CA . LEU B 162 ? 1.3523 1.0460 1.1224 0.0848 0.1448 0.0600 162 LEU B CA 4581 C C . LEU B 162 ? 1.4049 1.0981 1.1591 0.1032 0.1399 0.0648 162 LEU B C 4582 O O . LEU B 162 ? 1.4904 1.1647 1.2343 0.1133 0.1420 0.0698 162 LEU B O 4583 C CB . LEU B 162 ? 1.2851 0.9925 1.0690 0.0798 0.1375 0.0475 162 LEU B CB 4584 C CG . LEU B 162 ? 1.2573 0.9650 1.0558 0.0636 0.1406 0.0409 162 LEU B CG 4585 C CD1 . LEU B 162 ? 1.3013 1.0241 1.1096 0.0609 0.1331 0.0294 162 LEU B CD1 4586 C CD2 . LEU B 162 ? 1.2943 0.9769 1.0930 0.0601 0.1494 0.0441 162 LEU B CD2 4587 N N . VAL B 163 ? 1.3780 1.0918 1.1307 0.1078 0.1328 0.0629 163 VAL B N 4588 C CA . VAL B 163 ? 1.3736 1.0905 1.1124 0.1254 0.1266 0.0656 163 VAL B CA 4589 C C . VAL B 163 ? 1.4140 1.1120 1.1331 0.1336 0.1344 0.0790 163 VAL B C 4590 O O . VAL B 163 ? 1.3966 1.0834 1.1004 0.1492 0.1325 0.0841 163 VAL B O 4591 C CB . VAL B 163 ? 1.3301 1.0736 1.0737 0.1268 0.1176 0.0597 163 VAL B CB 4592 C CG1 . VAL B 163 ? 1.3492 1.0965 1.0784 0.1455 0.1109 0.0620 163 VAL B CG1 4593 C CG2 . VAL B 163 ? 1.2732 1.0343 1.0349 0.1195 0.1104 0.0476 163 VAL B CG2 4594 N N . MET B 164 ? 1.4379 1.1327 1.1573 0.1232 0.1433 0.0847 164 MET B N 4595 C CA . MET B 164 ? 1.5191 1.1958 1.2208 0.1280 0.1533 0.0982 164 MET B CA 4596 C C . MET B 164 ? 1.5707 1.2178 1.2631 0.1330 0.1601 0.1059 164 MET B C 4597 O O . MET B 164 ? 1.5389 1.1694 1.2108 0.1450 0.1646 0.1173 164 MET B O 4598 C CB . MET B 164 ? 1.5031 1.1821 1.2131 0.1123 0.1629 0.1007 164 MET B CB 4599 C CG . MET B 164 ? 1.5314 1.1939 1.2248 0.1150 0.1753 0.1148 164 MET B CG 4600 S SD . MET B 164 ? 1.5320 1.2014 1.2403 0.0955 0.1858 0.1148 164 MET B SD 4601 C CE . MET B 164 ? 1.5192 1.1788 1.2498 0.0793 0.1883 0.1073 164 MET B CE 4602 N N . GLN B 165 ? 1.6149 1.2550 1.3217 0.1245 0.1605 0.0995 165 GLN B N 4603 C CA . GLN B 165 ? 1.6727 1.2848 1.3736 0.1289 0.1658 0.1047 165 GLN B CA 4604 C C . GLN B 165 ? 1.7266 1.3339 1.4152 0.1483 0.1571 0.1044 165 GLN B C 4605 O O . GLN B 165 ? 1.8632 1.4449 1.5410 0.1561 0.1614 0.1118 165 GLN B O 4606 C CB . GLN B 165 ? 1.6379 1.2458 1.3588 0.1144 0.1678 0.0959 165 GLN B CB 4607 C CG . GLN B 165 ? 1.6442 1.2517 1.3780 0.0957 0.1771 0.0962 165 GLN B CG 4608 C CD . GLN B 165 ? 1.6788 1.2907 1.4337 0.0822 0.1753 0.0838 165 GLN B CD 4609 O OE1 . GLN B 165 ? 1.6970 1.3068 1.4555 0.0866 0.1695 0.0767 165 GLN B OE1 4610 N NE2 . GLN B 165 ? 1.6965 1.3149 1.4652 0.0662 0.1802 0.0808 165 GLN B NE2 4611 N N . ASP B 166 ? 1.6929 1.3243 1.3843 0.1559 0.1449 0.0956 166 ASP B N 4612 C CA . ASP B 166 ? 1.6925 1.3228 1.3757 0.1742 0.1355 0.0930 166 ASP B CA 4613 C C . ASP B 166 ? 1.7528 1.3902 1.4172 0.1909 0.1299 0.0983 166 ASP B C 4614 O O . ASP B 166 ? 1.7893 1.4527 1.4596 0.1920 0.1215 0.0908 166 ASP B O 4615 C CB . ASP B 166 ? 1.6017 1.2536 1.3041 0.1713 0.1257 0.0775 166 ASP B CB 4616 C CG . ASP B 166 ? 1.5730 1.2263 1.2706 0.1896 0.1160 0.0730 166 ASP B CG 4617 O OD1 . ASP B 166 ? 1.5278 1.1642 1.2065 0.2052 0.1160 0.0818 166 ASP B OD1 4618 O OD2 . ASP B 166 ? 1.5497 1.2218 1.2628 0.1884 0.1084 0.0605 166 ASP B OD2 4619 N N . PRO B 167 ? 1.8678 1.4818 1.5094 0.2048 0.1339 0.1108 167 PRO B N 4620 C CA . PRO B 167 ? 1.8251 1.4444 1.4457 0.2212 0.1293 0.1168 167 PRO B CA 4621 C C . PRO B 167 ? 1.7739 1.4081 1.3930 0.2391 0.1140 0.1077 167 PRO B C 4622 O O . PRO B 167 ? 1.7498 1.3932 1.3542 0.2530 0.1078 0.1095 167 PRO B O 4623 C CB . PRO B 167 ? 1.8752 1.4613 1.4715 0.2292 0.1399 0.1339 167 PRO B CB 4624 C CG . PRO B 167 ? 1.8802 1.4433 1.4849 0.2236 0.1450 0.1343 167 PRO B CG 4625 C CD . PRO B 167 ? 1.8660 1.4476 1.4996 0.2083 0.1410 0.1189 167 PRO B CD 4626 N N . SER B 168 ? 1.6954 1.3329 1.3303 0.2388 0.1082 0.0973 168 SER B N 4627 C CA . SER B 168 ? 1.6776 1.3362 1.3196 0.2512 0.0939 0.0851 168 SER B CA 4628 C C . SER B 168 ? 1.6207 1.3118 1.2767 0.2443 0.0872 0.0751 168 SER B C 4629 O O . SER B 168 ? 1.6676 1.3766 1.3229 0.2570 0.0759 0.0683 168 SER B O 4630 C CB . SER B 168 ? 1.6839 1.3414 1.3432 0.2490 0.0910 0.0751 168 SER B CB 4631 O OG . SER B 168 ? 1.6090 1.2966 1.2884 0.2472 0.0810 0.0598 168 SER B OG 4632 N N . MET B 169 ? 1.5888 1.2875 1.2587 0.2244 0.0936 0.0736 169 MET B N 4633 C CA . MET B 169 ? 1.5278 1.2545 1.2104 0.2167 0.0882 0.0655 169 MET B CA 4634 C C . MET B 169 ? 1.5015 1.2296 1.1678 0.2205 0.0905 0.0737 169 MET B C 4635 O O . MET B 169 ? 1.4104 1.1212 1.0658 0.2147 0.1019 0.0850 169 MET B O 4636 C CB . MET B 169 ? 1.4746 1.2084 1.1780 0.1947 0.0933 0.0602 169 MET B CB 4637 C CG . MET B 169 ? 1.4906 1.2326 1.2129 0.1900 0.0891 0.0488 169 MET B CG 4638 S SD . MET B 169 ? 1.4628 1.2089 1.2047 0.1655 0.0959 0.0442 169 MET B SD 4639 C CE . MET B 169 ? 1.4720 1.2138 1.2251 0.1663 0.0944 0.0356 169 MET B CE 4640 N N . ASN B 170 ? 1.4836 1.2333 1.1497 0.2298 0.0800 0.0672 170 ASN B N 4641 C CA . ASN B 170 ? 1.4906 1.2443 1.1397 0.2372 0.0800 0.0731 170 ASN B CA 4642 C C . ASN B 170 ? 1.4494 1.2193 1.1106 0.2215 0.0827 0.0702 170 ASN B C 4643 O O . ASN B 170 ? 1.4911 1.2822 1.1562 0.2251 0.0743 0.0631 170 ASN B O 4644 C CB . ASN B 170 ? 1.4996 1.2682 1.1419 0.2572 0.0661 0.0664 170 ASN B CB 4645 C CG . ASN B 170 ? 1.5277 1.2973 1.1473 0.2687 0.0659 0.0731 170 ASN B CG 4646 O OD1 . ASN B 170 ? 1.5290 1.2827 1.1329 0.2652 0.0775 0.0856 170 ASN B OD1 4647 N ND2 . ASN B 170 ? 1.5352 1.3244 1.1538 0.2824 0.0528 0.0642 170 ASN B ND2 4648 N N . LEU B 171 ? 1.3808 1.1405 1.0489 0.2044 0.0939 0.0749 171 LEU B N 4649 C CA . LEU B 171 ? 1.3626 1.1362 1.0438 0.1886 0.0968 0.0720 171 LEU B CA 4650 C C . LEU B 171 ? 1.3726 1.1509 1.0386 0.1945 0.0988 0.0776 171 LEU B C 4651 O O . LEU B 171 ? 1.4122 1.1728 1.0590 0.1989 0.1083 0.0896 171 LEU B O 4652 C CB . LEU B 171 ? 1.3154 1.0748 1.0052 0.1710 0.1086 0.0763 171 LEU B CB 4653 C CG . LEU B 171 ? 1.2573 1.0284 0.9606 0.1542 0.1124 0.0739 171 LEU B CG 4654 C CD1 . LEU B 171 ? 1.1910 0.9859 0.9141 0.1484 0.1017 0.0610 171 LEU B CD1 4655 C CD2 . LEU B 171 ? 1.2425 0.9977 0.9528 0.1390 0.1238 0.0781 171 LEU B CD2 4656 N N . GLN B 172 ? 1.3609 1.1624 1.0354 0.1945 0.0903 0.0689 172 GLN B N 4657 C CA . GLN B 172 ? 1.4508 1.2588 1.1123 0.1997 0.0920 0.0727 172 GLN B CA 4658 C C . GLN B 172 ? 1.4791 1.2980 1.1547 0.1833 0.0965 0.0703 172 GLN B C 4659 O O . GLN B 172 ? 1.5244 1.3401 1.1891 0.1824 0.1049 0.0775 172 GLN B O 4660 C CB . GLN B 172 ? 1.5077 1.3324 1.1633 0.2168 0.0785 0.0651 172 GLN B CB 4661 C CG . GLN B 172 ? 1.5540 1.3660 1.1876 0.2368 0.0755 0.0704 172 GLN B CG 4662 C CD . GLN B 172 ? 1.5827 1.3734 1.1883 0.2434 0.0877 0.0862 172 GLN B CD 4663 O OE1 . GLN B 172 ? 1.5179 1.3137 1.1112 0.2464 0.0910 0.0898 172 GLN B OE1 4664 N NE2 . GLN B 172 ? 1.5865 1.3528 1.1819 0.2457 0.0948 0.0957 172 GLN B NE2 4665 N N . GLY B 173 ? 1.4956 1.3269 1.1949 0.1705 0.0914 0.0607 173 GLY B N 4666 C CA . GLY B 173 ? 1.4131 1.2534 1.1268 0.1547 0.0951 0.0583 173 GLY B CA 4667 C C . GLY B 173 ? 1.3563 1.2041 1.0935 0.1399 0.0914 0.0500 173 GLY B C 4668 O O . GLY B 173 ? 1.2871 1.1338 1.0313 0.1405 0.0867 0.0457 173 GLY B O 4669 N N . LEU B 174 ? 1.3468 1.2025 1.0958 0.1271 0.0937 0.0478 174 LEU B N 4670 C CA . LEU B 174 ? 1.3355 1.1995 1.1051 0.1134 0.0897 0.0402 174 LEU B CA 4671 C C . LEU B 174 ? 1.3029 1.1833 1.0836 0.1066 0.0857 0.0349 174 LEU B C 4672 O O . LEU B 174 ? 1.2851 1.1669 1.0601 0.1070 0.0906 0.0384 174 LEU B O 4673 C CB . LEU B 174 ? 1.3823 1.2315 1.1566 0.1012 0.0988 0.0440 174 LEU B CB 4674 C CG . LEU B 174 ? 1.4606 1.2997 1.2302 0.0945 0.1109 0.0516 174 LEU B CG 4675 C CD1 . LEU B 174 ? 1.4995 1.3487 1.2854 0.0800 0.1111 0.0468 174 LEU B CD1 4676 C CD2 . LEU B 174 ? 1.5511 1.3684 1.3156 0.0915 0.1206 0.0583 174 LEU B CD2 4677 N N . ALA B 175 ? 1.2696 1.1623 1.0662 0.1008 0.0770 0.0265 175 ALA B N 4678 C CA . ALA B 175 ? 1.1910 1.0979 0.9993 0.0942 0.0722 0.0211 175 ALA B CA 4679 C C . ALA B 175 ? 1.1276 1.0368 0.9522 0.0801 0.0701 0.0168 175 ALA B C 4680 O O . ALA B 175 ? 1.1473 1.0555 0.9772 0.0784 0.0669 0.0140 175 ALA B O 4681 C CB . ALA B 175 ? 1.2192 1.1408 1.0292 0.1043 0.0613 0.0146 175 ALA B CB 4682 N N . VAL B 176 ? 1.0545 0.9677 0.8868 0.0706 0.0717 0.0159 176 VAL B N 4683 C CA . VAL B 176 ? 0.9646 0.8792 0.8100 0.0577 0.0698 0.0124 176 VAL B CA 4684 C C . VAL B 176 ? 0.9495 0.8777 0.8061 0.0539 0.0621 0.0069 176 VAL B C 4685 O O . VAL B 176 ? 0.9421 0.8749 0.7988 0.0539 0.0636 0.0071 176 VAL B O 4686 C CB . VAL B 176 ? 0.9369 0.8407 0.7821 0.0485 0.0795 0.0165 176 VAL B CB 4687 C CG1 . VAL B 176 ? 0.9145 0.8218 0.7725 0.0360 0.0767 0.0122 176 VAL B CG1 4688 C CG2 . VAL B 176 ? 0.9545 0.8432 0.7912 0.0508 0.0860 0.0210 176 VAL B CG2 4689 N N . GLY B 177 ? 0.9192 0.8534 0.7853 0.0506 0.0542 0.0020 177 GLY B N 4690 C CA . GLY B 177 ? 0.8750 0.8201 0.7520 0.0471 0.0460 -0.0030 177 GLY B CA 4691 C C . GLY B 177 ? 0.8469 0.7902 0.7317 0.0349 0.0463 -0.0036 177 GLY B C 4692 O O . GLY B 177 ? 0.8270 0.7646 0.7129 0.0288 0.0476 -0.0031 177 GLY B O 4693 N N . ASN B 178 ? 0.8559 0.8048 0.7458 0.0321 0.0445 -0.0053 178 ASN B N 4694 C CA . ASN B 178 ? 0.8365 0.7843 0.7333 0.0218 0.0443 -0.0064 178 ASN B CA 4695 C C . ASN B 178 ? 0.8989 0.8361 0.7919 0.0156 0.0513 -0.0036 178 ASN B C 4696 O O . ASN B 178 ? 0.9343 0.8689 0.8300 0.0094 0.0489 -0.0048 178 ASN B O 4697 C CB . ASN B 178 ? 0.7958 0.7487 0.7011 0.0182 0.0346 -0.0101 178 ASN B CB 4698 C CG . ASN B 178 ? 0.7735 0.7361 0.6847 0.0229 0.0275 -0.0138 178 ASN B CG 4699 O OD1 . ASN B 178 ? 0.7858 0.7529 0.6961 0.0309 0.0243 -0.0153 178 ASN B OD1 4700 N ND2 . ASN B 178 ? 0.7619 0.7283 0.6799 0.0187 0.0246 -0.0161 178 ASN B ND2 4701 N N . GLY B 179 ? 0.9393 0.8698 0.8256 0.0177 0.0604 0.0001 179 GLY B N 4702 C CA . GLY B 179 ? 0.9098 0.8289 0.7926 0.0129 0.0676 0.0025 179 GLY B CA 4703 C C . GLY B 179 ? 0.9074 0.8251 0.7971 0.0032 0.0704 0.0008 179 GLY B C 4704 O O . GLY B 179 ? 0.8718 0.7971 0.7680 0.0012 0.0689 -0.0012 179 GLY B O 4705 N N . LEU B 180 ? 0.9244 0.8333 0.8136 -0.0024 0.0739 0.0006 180 LEU B N 4706 C CA . LEU B 180 ? 0.9550 0.8609 0.8505 -0.0113 0.0776 -0.0015 180 LEU B CA 4707 C C . LEU B 180 ? 0.9427 0.8379 0.8345 -0.0109 0.0889 0.0026 180 LEU B C 4708 O O . LEU B 180 ? 1.0458 0.9297 0.9329 -0.0111 0.0935 0.0043 180 LEU B O 4709 C CB . LEU B 180 ? 0.9982 0.9008 0.8950 -0.0173 0.0741 -0.0051 180 LEU B CB 4710 C CG . LEU B 180 ? 1.0464 0.9470 0.9504 -0.0265 0.0756 -0.0095 180 LEU B CG 4711 C CD1 . LEU B 180 ? 1.0110 0.9218 0.9247 -0.0297 0.0721 -0.0127 180 LEU B CD1 4712 C CD2 . LEU B 180 ? 1.0771 0.9765 0.9795 -0.0303 0.0704 -0.0132 180 LEU B CD2 4713 N N . SER B 181 ? 0.9099 0.8085 0.8040 -0.0102 0.0938 0.0044 181 SER B N 4714 C CA . SER B 181 ? 0.9065 0.7948 0.7972 -0.0103 0.1058 0.0096 181 SER B CA 4715 C C . SER B 181 ? 0.8586 0.7441 0.7609 -0.0211 0.1114 0.0064 181 SER B C 4716 O O . SER B 181 ? 0.8254 0.6978 0.7266 -0.0239 0.1208 0.0095 181 SER B O 4717 C CB . SER B 181 ? 0.9643 0.8581 0.8499 -0.0031 0.1094 0.0138 181 SER B CB 4718 O OG . SER B 181 ? 0.9554 0.8509 0.8300 0.0078 0.1043 0.0162 181 SER B OG 4719 N N . SER B 182 ? 0.8223 0.7198 0.7366 -0.0269 0.1054 -0.0001 182 SER B N 4720 C CA . SER B 182 ? 0.8659 0.7636 0.7938 -0.0371 0.1088 -0.0053 182 SER B CA 4721 C C . SER B 182 ? 0.8780 0.7868 0.8153 -0.0417 0.0975 -0.0136 182 SER B C 4722 O O . SER B 182 ? 0.8529 0.7741 0.7942 -0.0395 0.0911 -0.0159 182 SER B O 4723 C CB . SER B 182 ? 0.8897 0.7917 0.8247 -0.0390 0.1179 -0.0037 182 SER B CB 4724 O OG . SER B 182 ? 0.9197 0.8288 0.8719 -0.0484 0.1175 -0.0113 182 SER B OG 4725 N N . TYR B 183 ? 0.9573 0.8613 0.8978 -0.0475 0.0948 -0.0184 183 TYR B N 4726 C CA . TYR B 183 ? 1.0161 0.9296 0.9638 -0.0515 0.0838 -0.0262 183 TYR B CA 4727 C C . TYR B 183 ? 1.0067 0.9326 0.9691 -0.0553 0.0824 -0.0315 183 TYR B C 4728 O O . TYR B 183 ? 0.9846 0.9211 0.9502 -0.0540 0.0723 -0.0353 183 TYR B O 4729 C CB . TYR B 183 ? 1.0572 0.9636 1.0062 -0.0574 0.0825 -0.0314 183 TYR B CB 4730 C CG . TYR B 183 ? 1.0533 0.9502 0.9889 -0.0539 0.0817 -0.0284 183 TYR B CG 4731 C CD1 . TYR B 183 ? 0.9814 0.8824 0.9102 -0.0518 0.0721 -0.0297 183 TYR B CD1 4732 C CD2 . TYR B 183 ? 1.0929 0.9765 1.0233 -0.0528 0.0908 -0.0243 183 TYR B CD2 4733 C CE1 . TYR B 183 ? 0.9906 0.8845 0.9087 -0.0490 0.0722 -0.0276 183 TYR B CE1 4734 C CE2 . TYR B 183 ? 1.0635 0.9397 0.9831 -0.0492 0.0899 -0.0226 183 TYR B CE2 4735 C CZ . TYR B 183 ? 1.0114 0.8937 0.9254 -0.0475 0.0809 -0.0245 183 TYR B CZ 4736 O OH . TYR B 183 ? 1.0255 0.9018 0.9302 -0.0443 0.0810 -0.0234 183 TYR B OH 4737 N N . GLU B 184 ? 1.0280 0.9522 1.0000 -0.0601 0.0928 -0.0319 184 GLU B N 4738 C CA . GLU B 184 ? 1.0407 0.9777 1.0296 -0.0646 0.0927 -0.0382 184 GLU B CA 4739 C C . GLU B 184 ? 1.0253 0.9743 1.0136 -0.0582 0.0896 -0.0364 184 GLU B C 4740 O O . GLU B 184 ? 1.0430 1.0047 1.0402 -0.0584 0.0805 -0.0428 184 GLU B O 4741 C CB . GLU B 184 ? 1.0633 0.9956 1.0633 -0.0714 0.1065 -0.0382 184 GLU B CB 4742 C CG . GLU B 184 ? 1.0701 1.0169 1.0909 -0.0774 0.1070 -0.0464 184 GLU B CG 4743 C CD . GLU B 184 ? 1.1060 1.0479 1.1401 -0.0857 0.1214 -0.0468 184 GLU B CD 4744 O OE1 . GLU B 184 ? 1.0848 1.0121 1.1171 -0.0898 0.1267 -0.0457 184 GLU B OE1 4745 O OE2 . GLU B 184 ? 1.1248 1.0775 1.1718 -0.0882 0.1276 -0.0486 184 GLU B OE2 4746 N N . GLN B 185 ? 0.9886 0.9334 0.9660 -0.0519 0.0966 -0.0281 185 GLN B N 4747 C CA . GLN B 185 ? 0.9959 0.9521 0.9720 -0.0450 0.0940 -0.0269 185 GLN B CA 4748 C C . GLN B 185 ? 0.9604 0.9213 0.9306 -0.0394 0.0797 -0.0285 185 GLN B C 4749 O O . GLN B 185 ? 0.9369 0.9100 0.9131 -0.0365 0.0725 -0.0324 185 GLN B O 4750 C CB . GLN B 185 ? 1.0401 0.9904 1.0043 -0.0388 0.1047 -0.0180 185 GLN B CB 4751 C CG . GLN B 185 ? 1.1112 1.0632 1.0837 -0.0431 0.1185 -0.0167 185 GLN B CG 4752 C CD . GLN B 185 ? 1.2059 1.1448 1.1639 -0.0389 0.1312 -0.0063 185 GLN B CD 4753 O OE1 . GLN B 185 ? 1.2679 1.2110 1.2225 -0.0350 0.1394 -0.0023 185 GLN B OE1 4754 N NE2 . GLN B 185 ? 1.2420 1.1649 1.1907 -0.0391 0.1329 -0.0020 185 GLN B NE2 4755 N N . ASN B 186 ? 0.9191 0.8702 0.8785 -0.0381 0.0760 -0.0256 186 ASN B N 4756 C CA . ASN B 186 ? 0.8828 0.8366 0.8372 -0.0343 0.0637 -0.0266 186 ASN B CA 4757 C C . ASN B 186 ? 0.8883 0.8504 0.8532 -0.0384 0.0536 -0.0341 186 ASN B C 4758 O O . ASN B 186 ? 0.7782 0.7481 0.7450 -0.0346 0.0442 -0.0361 186 ASN B O 4759 C CB . ASN B 186 ? 0.8999 0.8422 0.8431 -0.0341 0.0631 -0.0233 186 ASN B CB 4760 C CG . ASN B 186 ? 0.9159 0.8602 0.8534 -0.0303 0.0524 -0.0229 186 ASN B CG 4761 O OD1 . ASN B 186 ? 0.9267 0.8791 0.8667 -0.0262 0.0460 -0.0238 186 ASN B OD1 4762 N ND2 . ASN B 186 ? 0.9750 0.9115 0.9050 -0.0316 0.0510 -0.0216 186 ASN B ND2 4763 N N . ASP B 187 ? 0.9195 0.8796 0.8914 -0.0458 0.0552 -0.0388 187 ASP B N 4764 C CA . ASP B 187 ? 0.9298 0.8967 0.9100 -0.0492 0.0447 -0.0464 187 ASP B CA 4765 C C . ASP B 187 ? 0.8904 0.8713 0.8855 -0.0492 0.0424 -0.0522 187 ASP B C 4766 O O . ASP B 187 ? 0.8921 0.8801 0.8899 -0.0464 0.0311 -0.0557 187 ASP B O 4767 C CB . ASP B 187 ? 1.0258 0.9869 1.0089 -0.0563 0.0464 -0.0508 187 ASP B CB 4768 C CG . ASP B 187 ? 1.1363 1.0856 1.1046 -0.0556 0.0456 -0.0469 187 ASP B CG 4769 O OD1 . ASP B 187 ? 1.2261 1.1704 1.1831 -0.0505 0.0473 -0.0399 187 ASP B OD1 4770 O OD2 . ASP B 187 ? 1.1782 1.1239 1.1466 -0.0600 0.0433 -0.0516 187 ASP B OD2 4771 N N . ASN B 188 ? 0.8661 0.8506 0.8706 -0.0518 0.0532 -0.0529 188 ASN B N 4772 C CA . ASN B 188 ? 0.8525 0.8519 0.8721 -0.0515 0.0525 -0.0586 188 ASN B CA 4773 C C . ASN B 188 ? 0.8483 0.8542 0.8630 -0.0428 0.0471 -0.0562 188 ASN B C 4774 O O . ASN B 188 ? 0.9060 0.9228 0.9295 -0.0405 0.0376 -0.0622 188 ASN B O 4775 C CB . ASN B 188 ? 0.8912 0.8924 0.9202 -0.0560 0.0677 -0.0581 188 ASN B CB 4776 C CG . ASN B 188 ? 0.8752 0.8725 0.9150 -0.0655 0.0728 -0.0630 188 ASN B CG 4777 O OD1 . ASN B 188 ? 0.9184 0.9211 0.9681 -0.0692 0.0638 -0.0717 188 ASN B OD1 4778 N ND2 . ASN B 188 ? 0.8398 0.8275 0.8781 -0.0692 0.0872 -0.0578 188 ASN B ND2 4779 N N . SER B 189 ? 0.7688 0.7680 0.7700 -0.0375 0.0524 -0.0482 189 SER B N 4780 C CA . SER B 189 ? 0.7307 0.7360 0.7277 -0.0289 0.0474 -0.0467 189 SER B CA 4781 C C . SER B 189 ? 0.7105 0.7155 0.7043 -0.0256 0.0324 -0.0483 189 SER B C 4782 O O . SER B 189 ? 0.7661 0.7795 0.7643 -0.0205 0.0248 -0.0514 189 SER B O 4783 C CB . SER B 189 ? 0.7269 0.7252 0.7098 -0.0234 0.0560 -0.0385 189 SER B CB 4784 O OG . SER B 189 ? 0.7028 0.6880 0.6731 -0.0234 0.0555 -0.0331 189 SER B OG 4785 N N . LEU B 190 ? 0.7298 0.7246 0.7157 -0.0284 0.0286 -0.0460 190 LEU B N 4786 C CA . LEU B 190 ? 0.7260 0.7186 0.7077 -0.0263 0.0156 -0.0462 190 LEU B CA 4787 C C . LEU B 190 ? 0.7628 0.7645 0.7561 -0.0267 0.0054 -0.0535 190 LEU B C 4788 O O . LEU B 190 ? 0.7964 0.8001 0.7897 -0.0222 -0.0049 -0.0543 190 LEU B O 4789 C CB . LEU B 190 ? 0.7430 0.7241 0.7148 -0.0304 0.0150 -0.0432 190 LEU B CB 4790 C CG . LEU B 190 ? 0.7725 0.7492 0.7375 -0.0291 0.0038 -0.0418 190 LEU B CG 4791 C CD1 . LEU B 190 ? 0.7772 0.7555 0.7403 -0.0226 -0.0010 -0.0391 190 LEU B CD1 4792 C CD2 . LEU B 190 ? 0.7705 0.7363 0.7238 -0.0324 0.0069 -0.0377 190 LEU B CD2 4793 N N . VAL B 191 ? 0.7977 0.8048 0.8017 -0.0318 0.0078 -0.0594 191 VAL B N 4794 C CA . VAL B 191 ? 0.7771 0.7933 0.7926 -0.0318 -0.0028 -0.0674 191 VAL B CA 4795 C C . VAL B 191 ? 0.7644 0.7929 0.7901 -0.0262 -0.0054 -0.0711 191 VAL B C 4796 O O . VAL B 191 ? 0.8303 0.8621 0.8588 -0.0219 -0.0177 -0.0742 191 VAL B O 4797 C CB . VAL B 191 ? 0.8023 0.8226 0.8288 -0.0388 0.0001 -0.0741 191 VAL B CB 4798 C CG1 . VAL B 191 ? 0.8068 0.8379 0.8460 -0.0376 -0.0119 -0.0833 191 VAL B CG1 4799 C CG2 . VAL B 191 ? 0.8273 0.8352 0.8426 -0.0434 0.0012 -0.0712 191 VAL B CG2 4800 N N . TYR B 192 ? 0.7532 0.7877 0.7833 -0.0257 0.0059 -0.0706 192 TYR B N 4801 C CA . TYR B 192 ? 0.7549 0.8008 0.7919 -0.0192 0.0046 -0.0737 192 TYR B CA 4802 C C . TYR B 192 ? 0.7198 0.7600 0.7461 -0.0120 -0.0035 -0.0694 192 TYR B C 4803 O O . TYR B 192 ? 0.6498 0.6961 0.6819 -0.0066 -0.0136 -0.0737 192 TYR B O 4804 C CB . TYR B 192 ? 0.7855 0.8366 0.8241 -0.0192 0.0199 -0.0717 192 TYR B CB 4805 C CG . TYR B 192 ? 0.8324 0.8929 0.8866 -0.0258 0.0290 -0.0773 192 TYR B CG 4806 C CD1 . TYR B 192 ? 0.8631 0.9160 0.9174 -0.0340 0.0375 -0.0754 192 TYR B CD1 4807 C CD2 . TYR B 192 ? 0.8723 0.9496 0.9422 -0.0239 0.0296 -0.0850 192 TYR B CD2 4808 C CE1 . TYR B 192 ? 0.8992 0.9605 0.9698 -0.0408 0.0462 -0.0809 192 TYR B CE1 4809 C CE2 . TYR B 192 ? 0.9012 0.9882 0.9874 -0.0306 0.0389 -0.0905 192 TYR B CE2 4810 C CZ . TYR B 192 ? 0.9345 1.0131 1.0213 -0.0394 0.0472 -0.0883 192 TYR B CZ 4811 O OH . TYR B 192 ? 0.9864 1.0743 1.0916 -0.0468 0.0568 -0.0941 192 TYR B OH 4812 N N . PHE B 193 ? 0.7152 0.7436 0.7271 -0.0120 0.0004 -0.0615 193 PHE B N 4813 C CA . PHE B 193 ? 0.7171 0.7402 0.7206 -0.0061 -0.0064 -0.0579 193 PHE B CA 4814 C C . PHE B 193 ? 0.7361 0.7574 0.7425 -0.0053 -0.0210 -0.0605 193 PHE B C 4815 O O . PHE B 193 ? 0.7496 0.7742 0.7596 0.0005 -0.0292 -0.0628 193 PHE B O 4816 C CB . PHE B 193 ? 0.7123 0.7229 0.7016 -0.0077 -0.0011 -0.0500 193 PHE B CB 4817 C CG . PHE B 193 ? 0.7343 0.7409 0.7168 -0.0019 -0.0062 -0.0468 193 PHE B CG 4818 C CD1 . PHE B 193 ? 0.7606 0.7616 0.7417 -0.0018 -0.0170 -0.0460 193 PHE B CD1 4819 C CD2 . PHE B 193 ? 0.7432 0.7513 0.7204 0.0033 0.0001 -0.0443 193 PHE B CD2 4820 C CE1 . PHE B 193 ? 0.7583 0.7556 0.7354 0.0024 -0.0211 -0.0435 193 PHE B CE1 4821 C CE2 . PHE B 193 ? 0.7424 0.7478 0.7152 0.0086 -0.0050 -0.0427 193 PHE B CE2 4822 C CZ . PHE B 193 ? 0.7804 0.7806 0.7544 0.0076 -0.0155 -0.0425 193 PHE B CZ 4823 N N . ALA B 194 ? 0.7462 0.7618 0.7508 -0.0107 -0.0243 -0.0604 194 ALA B N 4824 C CA . ALA B 194 ? 0.7123 0.7235 0.7158 -0.0099 -0.0376 -0.0612 194 ALA B CA 4825 C C . ALA B 194 ? 0.6906 0.7124 0.7076 -0.0054 -0.0468 -0.0689 194 ALA B C 4826 O O . ALA B 194 ? 0.7396 0.7583 0.7564 -0.0008 -0.0575 -0.0687 194 ALA B O 4827 C CB . ALA B 194 ? 0.7489 0.7537 0.7472 -0.0160 -0.0387 -0.0607 194 ALA B CB 4828 N N . TYR B 195 ? 0.6877 0.7218 0.7172 -0.0066 -0.0427 -0.0759 195 TYR B N 4829 C CA . TYR B 195 ? 0.7329 0.7790 0.7770 -0.0020 -0.0518 -0.0846 195 TYR B CA 4830 C C . TYR B 195 ? 0.7206 0.7714 0.7678 0.0054 -0.0540 -0.0856 195 TYR B C 4831 O O . TYR B 195 ? 0.7813 0.8320 0.8324 0.0109 -0.0663 -0.0885 195 TYR B O 4832 C CB . TYR B 195 ? 0.7516 0.8121 0.8111 -0.0054 -0.0457 -0.0927 195 TYR B CB 4833 C CG . TYR B 195 ? 0.7837 0.8589 0.8602 0.0000 -0.0540 -0.1028 195 TYR B CG 4834 C CD1 . TYR B 195 ? 0.8148 0.8885 0.8940 0.0040 -0.0701 -0.1065 195 TYR B CD1 4835 C CD2 . TYR B 195 ? 0.8172 0.9081 0.9068 0.0013 -0.0455 -0.1085 195 TYR B CD2 4836 C CE1 . TYR B 195 ? 0.8227 0.9099 0.9181 0.0098 -0.0783 -0.1163 195 TYR B CE1 4837 C CE2 . TYR B 195 ? 0.8076 0.9133 0.9137 0.0065 -0.0527 -0.1186 195 TYR B CE2 4838 C CZ . TYR B 195 ? 0.8354 0.9394 0.9450 0.0109 -0.0695 -0.1228 195 TYR B CZ 4839 O OH . TYR B 195 ? 0.8642 0.9833 0.9911 0.0168 -0.0770 -0.1335 195 TYR B OH 4840 N N . TYR B 196 ? 0.7238 0.7781 0.7686 0.0061 -0.0422 -0.0834 196 TYR B N 4841 C CA . TYR B 196 ? 0.7039 0.7657 0.7522 0.0137 -0.0426 -0.0861 196 TYR B CA 4842 C C . TYR B 196 ? 0.7203 0.7715 0.7592 0.0181 -0.0492 -0.0812 196 TYR B C 4843 O O . TYR B 196 ? 0.7710 0.8278 0.8137 0.0252 -0.0528 -0.0848 196 TYR B O 4844 C CB . TYR B 196 ? 0.7179 0.7881 0.7661 0.0135 -0.0274 -0.0858 196 TYR B CB 4845 C CG . TYR B 196 ? 0.7171 0.8013 0.7798 0.0102 -0.0216 -0.0928 196 TYR B CG 4846 C CD1 . TYR B 196 ? 0.7203 0.8196 0.7979 0.0153 -0.0266 -0.1022 196 TYR B CD1 4847 C CD2 . TYR B 196 ? 0.6931 0.7756 0.7562 0.0019 -0.0111 -0.0907 196 TYR B CD2 4848 C CE1 . TYR B 196 ? 0.7075 0.8211 0.8005 0.0119 -0.0208 -0.1094 196 TYR B CE1 4849 C CE2 . TYR B 196 ? 0.7042 0.7999 0.7829 -0.0018 -0.0054 -0.0977 196 TYR B CE2 4850 C CZ . TYR B 196 ? 0.7054 0.8173 0.7994 0.0029 -0.0100 -0.1070 196 TYR B CZ 4851 O OH . TYR B 196 ? 0.7056 0.8318 0.8171 -0.0014 -0.0038 -0.1146 196 TYR B OH 4852 N N . HIS B 197 ? 0.6886 0.7255 0.7165 0.0139 -0.0511 -0.0740 197 HIS B N 4853 C CA . HIS B 197 ? 0.6702 0.6966 0.6918 0.0167 -0.0586 -0.0697 197 HIS B CA 4854 C C . HIS B 197 ? 0.6887 0.7074 0.7116 0.0163 -0.0717 -0.0697 197 HIS B C 4855 O O . HIS B 197 ? 0.7201 0.7272 0.7369 0.0165 -0.0771 -0.0647 197 HIS B O 4856 C CB . HIS B 197 ? 0.6802 0.6959 0.6884 0.0127 -0.0512 -0.0613 197 HIS B CB 4857 C CG . HIS B 197 ? 0.6849 0.7051 0.6892 0.0152 -0.0405 -0.0601 197 HIS B CG 4858 N ND1 . HIS B 197 ? 0.7217 0.7490 0.7266 0.0135 -0.0293 -0.0610 197 HIS B ND1 4859 C CD2 . HIS B 197 ? 0.7055 0.7239 0.7051 0.0197 -0.0393 -0.0581 197 HIS B CD2 4860 C CE1 . HIS B 197 ? 0.7450 0.7738 0.7438 0.0173 -0.0217 -0.0588 197 HIS B CE1 4861 N NE2 . HIS B 197 ? 0.7510 0.7751 0.7465 0.0215 -0.0280 -0.0575 197 HIS B NE2 4862 N N . GLY B 198 ? 0.7167 0.7414 0.7476 0.0160 -0.0767 -0.0753 198 GLY B N 4863 C CA . GLY B 198 ? 0.7059 0.7253 0.7398 0.0188 -0.0913 -0.0770 198 GLY B CA 4864 C C . GLY B 198 ? 0.7294 0.7356 0.7520 0.0140 -0.0956 -0.0708 198 GLY B C 4865 O O . GLY B 198 ? 0.7038 0.7008 0.7240 0.0164 -0.1071 -0.0689 198 GLY B O 4866 N N . LEU B 199 ? 0.7404 0.7454 0.7558 0.0075 -0.0866 -0.0679 199 LEU B N 4867 C CA . LEU B 199 ? 0.7661 0.7591 0.7687 0.0030 -0.0892 -0.0620 199 LEU B CA 4868 C C . LEU B 199 ? 0.8215 0.8193 0.8274 0.0016 -0.0943 -0.0677 199 LEU B C 4869 O O . LEU B 199 ? 0.9099 0.8983 0.9045 -0.0003 -0.0991 -0.0641 199 LEU B O 4870 C CB . LEU B 199 ? 0.7465 0.7339 0.7381 -0.0027 -0.0768 -0.0556 199 LEU B CB 4871 C CG . LEU B 199 ? 0.7453 0.7321 0.7355 -0.0015 -0.0690 -0.0520 199 LEU B CG 4872 C CD1 . LEU B 199 ? 0.7404 0.7207 0.7193 -0.0068 -0.0585 -0.0459 199 LEU B CD1 4873 C CD2 . LEU B 199 ? 0.7763 0.7561 0.7663 0.0025 -0.0769 -0.0490 199 LEU B CD2 4874 N N . LEU B 200 ? 0.8388 0.8518 0.8598 0.0028 -0.0931 -0.0769 200 LEU B N 4875 C CA . LEU B 200 ? 0.8538 0.8740 0.8805 0.0001 -0.0951 -0.0837 200 LEU B CA 4876 C C . LEU B 200 ? 0.8485 0.8781 0.8884 0.0058 -0.1079 -0.0929 200 LEU B C 4877 O O . LEU B 200 ? 0.9353 0.9643 0.9739 0.0059 -0.1163 -0.0962 200 LEU B O 4878 C CB . LEU B 200 ? 0.8253 0.8562 0.8606 -0.0052 -0.0812 -0.0877 200 LEU B CB 4879 C CG . LEU B 200 ? 0.8401 0.8630 0.8639 -0.0112 -0.0680 -0.0803 200 LEU B CG 4880 C CD1 . LEU B 200 ? 0.8722 0.9039 0.9055 -0.0172 -0.0577 -0.0857 200 LEU B CD1 4881 C CD2 . LEU B 200 ? 0.8883 0.8960 0.8943 -0.0136 -0.0714 -0.0731 200 LEU B CD2 4882 N N . GLY B 201 ? 0.8332 0.8725 0.8862 0.0111 -0.1094 -0.0980 201 GLY B N 4883 C CA . GLY B 201 ? 0.8113 0.8614 0.8791 0.0172 -0.1212 -0.1079 201 GLY B CA 4884 C C . GLY B 201 ? 0.8155 0.8828 0.8992 0.0138 -0.1168 -0.1183 201 GLY B C 4885 O O . GLY B 201 ? 0.8179 0.8863 0.8998 0.0062 -0.1055 -0.1172 201 GLY B O 4886 N N . ASN B 202 ? 0.8605 0.9411 0.9611 0.0194 -0.1260 -0.1290 202 ASN B N 4887 C CA . ASN B 202 ? 0.8984 0.9996 1.0200 0.0169 -0.1207 -0.1407 202 ASN B CA 4888 C C . ASN B 202 ? 0.9407 1.0456 1.0662 0.0126 -0.1245 -0.1466 202 ASN B C 4889 O O . ASN B 202 ? 0.9200 1.0374 1.0588 0.0061 -0.1143 -0.1529 202 ASN B O 4890 C CB . ASN B 202 ? 0.9177 1.0336 1.0577 0.0252 -0.1289 -0.1510 202 ASN B CB 4891 C CG . ASN B 202 ? 1.0068 1.1461 1.1704 0.0222 -0.1198 -0.1628 202 ASN B CG 4892 O OD1 . ASN B 202 ? 1.0121 1.1654 1.1932 0.0251 -0.1286 -0.1746 202 ASN B OD1 4893 N ND2 . ASN B 202 ? 0.9598 1.1036 1.1244 0.0163 -0.1019 -0.1596 202 ASN B ND2 4894 N N . ARG B 203 ? 0.9860 1.0805 1.1004 0.0164 -0.1392 -0.1452 203 ARG B N 4895 C CA . ARG B 203 ? 1.0302 1.1280 1.1465 0.0133 -0.1440 -0.1514 203 ARG B CA 4896 C C . ARG B 203 ? 0.9555 1.0470 1.0625 0.0031 -0.1297 -0.1458 203 ARG B C 4897 O O . ARG B 203 ? 0.8867 0.9893 1.0071 -0.0030 -0.1229 -0.1536 203 ARG B O 4898 C CB . ARG B 203 ? 1.1432 1.2283 1.2440 0.0200 -0.1619 -0.1488 203 ARG B CB 4899 C CG . ARG B 203 ? 1.2777 1.3695 1.3896 0.0307 -0.1783 -0.1564 203 ARG B CG 4900 C CD . ARG B 203 ? 1.4339 1.5177 1.5343 0.0370 -0.1961 -0.1576 203 ARG B CD 4901 N NE . ARG B 203 ? 1.6215 1.7022 1.7234 0.0485 -0.2124 -0.1591 203 ARG B NE 4902 C CZ . ARG B 203 ? 1.6920 1.7904 1.8170 0.0552 -0.2209 -0.1724 203 ARG B CZ 4903 N NH1 . ARG B 203 ? 1.6811 1.8029 1.8310 0.0512 -0.2142 -0.1857 203 ARG B NH1 4904 N NH2 . ARG B 203 ? 1.7066 1.7988 1.8304 0.0662 -0.2362 -0.1725 203 ARG B NH2 4905 N N . LEU B 204 ? 0.9688 1.0426 1.0545 0.0015 -0.1247 -0.1326 204 LEU B N 4906 C CA . LEU B 204 ? 1.0095 1.0760 1.0852 -0.0071 -0.1113 -0.1267 204 LEU B CA 4907 C C . LEU B 204 ? 1.0294 1.1060 1.1188 -0.0129 -0.0942 -0.1286 204 LEU B C 4908 O O . LEU B 204 ? 1.1169 1.1967 1.2116 -0.0204 -0.0850 -0.1317 204 LEU B O 4909 C CB . LEU B 204 ? 0.9955 1.0419 1.0465 -0.0070 -0.1099 -0.1127 204 LEU B CB 4910 C CG . LEU B 204 ? 0.9831 1.0208 1.0225 -0.0147 -0.0963 -0.1058 204 LEU B CG 4911 C CD1 . LEU B 204 ? 1.0130 1.0523 1.0525 -0.0196 -0.0968 -0.1118 204 LEU B CD1 4912 C CD2 . LEU B 204 ? 0.9880 1.0079 1.0053 -0.0136 -0.0965 -0.0932 204 LEU B CD2 4913 N N . TRP B 205 ? 0.9320 1.0133 1.0270 -0.0094 -0.0900 -0.1270 205 TRP B N 4914 C CA . TRP B 205 ? 0.8872 0.9793 0.9947 -0.0138 -0.0740 -0.1290 205 TRP B CA 4915 C C . TRP B 205 ? 0.8705 0.9805 1.0015 -0.0180 -0.0716 -0.1418 205 TRP B C 4916 O O . TRP B 205 ? 0.8465 0.9589 0.9830 -0.0259 -0.0584 -0.1424 205 TRP B O 4917 C CB . TRP B 205 ? 0.8789 0.9759 0.9896 -0.0076 -0.0722 -0.1275 205 TRP B CB 4918 C CG . TRP B 205 ? 0.8667 0.9724 0.9848 -0.0111 -0.0547 -0.1271 205 TRP B CG 4919 C CD1 . TRP B 205 ? 0.8922 1.0152 1.0276 -0.0087 -0.0503 -0.1346 205 TRP B CD1 4920 C CD2 . TRP B 205 ? 0.8291 0.9262 0.9368 -0.0172 -0.0393 -0.1187 205 TRP B CD2 4921 N NE1 . TRP B 205 ? 0.8763 1.0015 1.0112 -0.0129 -0.0327 -0.1305 205 TRP B NE1 4922 C CE2 . TRP B 205 ? 0.8525 0.9614 0.9704 -0.0180 -0.0261 -0.1207 205 TRP B CE2 4923 C CE3 . TRP B 205 ? 0.8643 0.9449 0.9545 -0.0215 -0.0355 -0.1098 205 TRP B CE3 4924 C CZ2 . TRP B 205 ? 0.8701 0.9733 0.9804 -0.0226 -0.0097 -0.1133 205 TRP B CZ2 4925 C CZ3 . TRP B 205 ? 0.8642 0.9400 0.9485 -0.0260 -0.0195 -0.1033 205 TRP B CZ3 4926 C CH2 . TRP B 205 ? 0.8517 0.9380 0.9454 -0.0263 -0.0071 -0.1047 205 TRP B CH2 4927 N N . SER B 206 ? 0.9040 1.0261 1.0493 -0.0128 -0.0846 -0.1523 206 SER B N 4928 C CA . SER B 206 ? 0.9734 1.1140 1.1433 -0.0166 -0.0835 -0.1659 206 SER B CA 4929 C C . SER B 206 ? 0.9972 1.1333 1.1656 -0.0246 -0.0810 -0.1678 206 SER B C 4930 O O . SER B 206 ? 1.0463 1.1918 1.2308 -0.0326 -0.0691 -0.1735 206 SER B O 4931 C CB . SER B 206 ? 1.0364 1.1889 1.2195 -0.0085 -0.1013 -0.1772 206 SER B CB 4932 O OG . SER B 206 ? 1.1358 1.2978 1.3280 -0.0017 -0.1023 -0.1796 206 SER B OG 4933 N N . SER B 207 ? 0.9672 1.0889 1.1166 -0.0225 -0.0919 -0.1634 207 SER B N 4934 C CA . SER B 207 ? 0.9721 1.0897 1.1188 -0.0288 -0.0915 -0.1665 207 SER B CA 4935 C C . SER B 207 ? 0.9581 1.0691 1.1019 -0.0381 -0.0722 -0.1599 207 SER B C 4936 O O . SER B 207 ? 1.0281 1.1463 1.1873 -0.0459 -0.0641 -0.1671 207 SER B O 4937 C CB . SER B 207 ? 0.9885 1.0899 1.1105 -0.0245 -0.1044 -0.1605 207 SER B CB 4938 O OG . SER B 207 ? 0.9660 1.0719 1.0895 -0.0154 -0.1228 -0.1662 207 SER B OG 4939 N N . LEU B 208 ? 0.9219 1.0190 1.0468 -0.0371 -0.0654 -0.1466 208 LEU B N 4940 C CA . LEU B 208 ? 0.9198 1.0087 1.0391 -0.0441 -0.0479 -0.1389 208 LEU B CA 4941 C C . LEU B 208 ? 0.9430 1.0455 1.0846 -0.0501 -0.0336 -0.1446 208 LEU B C 4942 O O . LEU B 208 ? 1.0044 1.1055 1.1525 -0.0583 -0.0235 -0.1466 208 LEU B O 4943 C CB . LEU B 208 ? 0.8872 0.9632 0.9864 -0.0400 -0.0442 -0.1255 208 LEU B CB 4944 C CG . LEU B 208 ? 0.9100 0.9692 0.9855 -0.0373 -0.0527 -0.1175 208 LEU B CG 4945 C CD1 . LEU B 208 ? 0.9174 0.9686 0.9791 -0.0311 -0.0548 -0.1077 208 LEU B CD1 4946 C CD2 . LEU B 208 ? 0.9111 0.9587 0.9758 -0.0441 -0.0433 -0.1130 208 LEU B CD2 4947 N N . GLN B 209 ? 0.9478 1.0633 1.1016 -0.0459 -0.0326 -0.1475 209 GLN B N 4948 C CA . GLN B 209 ? 0.9592 1.0900 1.1356 -0.0511 -0.0192 -0.1536 209 GLN B CA 4949 C C . GLN B 209 ? 1.0023 1.1446 1.2014 -0.0582 -0.0198 -0.1668 209 GLN B C 4950 O O . GLN B 209 ? 0.9795 1.1238 1.1902 -0.0673 -0.0051 -0.1682 209 GLN B O 4951 C CB . GLN B 209 ? 0.9589 1.1052 1.1466 -0.0438 -0.0226 -0.1582 209 GLN B CB 4952 C CG . GLN B 209 ? 0.9473 1.0865 1.1186 -0.0377 -0.0180 -0.1473 209 GLN B CG 4953 C CD . GLN B 209 ? 0.9613 1.0995 1.1314 -0.0426 0.0025 -0.1406 209 GLN B CD 4954 O OE1 . GLN B 209 ? 0.9280 1.0815 1.1163 -0.0452 0.0124 -0.1464 209 GLN B OE1 4955 N NE2 . GLN B 209 ? 0.9654 1.0855 1.1140 -0.0438 0.0094 -0.1283 209 GLN B NE2 4956 N N . THR B 210 ? 1.0122 1.1620 1.2180 -0.0538 -0.0373 -0.1767 210 THR B N 4957 C CA . THR B 210 ? 1.0693 1.2324 1.2981 -0.0590 -0.0412 -0.1914 210 THR B CA 4958 C C . THR B 210 ? 1.0740 1.2260 1.2992 -0.0681 -0.0342 -0.1906 210 THR B C 4959 O O . THR B 210 ? 1.1676 1.3282 1.4145 -0.0772 -0.0236 -0.1982 210 THR B O 4960 C CB . THR B 210 ? 1.1015 1.2702 1.3309 -0.0506 -0.0637 -0.2003 210 THR B CB 4961 O OG1 . THR B 210 ? 1.1523 1.3337 1.3909 -0.0424 -0.0704 -0.2040 210 THR B OG1 4962 C CG2 . THR B 210 ? 1.1243 1.3059 1.3756 -0.0553 -0.0691 -0.2160 210 THR B CG2 4963 N N . HIS B 211 ? 1.0106 1.1438 1.2094 -0.0659 -0.0397 -0.1818 211 HIS B N 4964 C CA . HIS B 211 ? 1.0578 1.1805 1.2514 -0.0727 -0.0371 -0.1828 211 HIS B CA 4965 C C . HIS B 211 ? 1.0454 1.1531 1.2286 -0.0793 -0.0188 -0.1714 211 HIS B C 4966 O O . HIS B 211 ? 1.1238 1.2262 1.3119 -0.0871 -0.0120 -0.1744 211 HIS B O 4967 C CB . HIS B 211 ? 1.1214 1.2328 1.2917 -0.0663 -0.0533 -0.1805 211 HIS B CB 4968 C CG . HIS B 211 ? 1.1793 1.3025 1.3559 -0.0585 -0.0727 -0.1908 211 HIS B CG 4969 N ND1 . HIS B 211 ? 1.1962 1.3108 1.3509 -0.0491 -0.0871 -0.1848 211 HIS B ND1 4970 C CD2 . HIS B 211 ? 1.2251 1.3678 1.4278 -0.0585 -0.0800 -0.2066 211 HIS B CD2 4971 C CE1 . HIS B 211 ? 1.2151 1.3421 1.3804 -0.0429 -0.1030 -0.1959 211 HIS B CE1 4972 N NE2 . HIS B 211 ? 1.2252 1.3703 1.4202 -0.0482 -0.0995 -0.2098 211 HIS B NE2 4973 N N . CYS B 212 ? 1.0026 1.1032 1.1718 -0.0758 -0.0114 -0.1588 212 CYS B N 4974 C CA . CYS B 212 ? 0.9937 1.0792 1.1503 -0.0801 0.0042 -0.1471 212 CYS B CA 4975 C C . CYS B 212 ? 1.0185 1.1101 1.1881 -0.0841 0.0214 -0.1445 212 CYS B C 4976 O O . CYS B 212 ? 1.0597 1.1386 1.2193 -0.0873 0.0352 -0.1346 212 CYS B O 4977 C CB . CYS B 212 ? 0.9876 1.0588 1.1162 -0.0728 0.0007 -0.1339 212 CYS B CB 4978 S SG . CYS B 212 ? 0.9539 1.0168 1.0632 -0.0669 -0.0184 -0.1341 212 CYS B SG 4979 N N . CYS B 213 ? 1.0635 1.1739 1.2539 -0.0833 0.0207 -0.1528 213 CYS B N 4980 C CA . CYS B 213 ? 1.1083 1.2255 1.3082 -0.0856 0.0371 -0.1492 213 CYS B CA 4981 C C . CYS B 213 ? 1.1303 1.2685 1.3624 -0.0913 0.0411 -0.1626 213 CYS B C 4982 O O . CYS B 213 ? 1.1903 1.3439 1.4365 -0.0876 0.0275 -0.1742 213 CYS B O 4983 C CB . CYS B 213 ? 1.1259 1.2452 1.3129 -0.0757 0.0344 -0.1421 213 CYS B CB 4984 S SG . CYS B 213 ? 1.1481 1.2476 1.3012 -0.0671 0.0241 -0.1296 213 CYS B SG 4985 N N . SER B 214 ? 1.1677 1.3061 1.4118 -0.1001 0.0599 -0.1610 214 SER B N 4986 C CA . SER B 214 ? 1.2334 1.3926 1.5094 -0.1063 0.0675 -0.1725 214 SER B CA 4987 C C . SER B 214 ? 1.2320 1.3944 1.5073 -0.1065 0.0858 -0.1639 214 SER B C 4988 O O . SER B 214 ? 1.1787 1.3248 1.4390 -0.1095 0.1003 -0.1513 214 SER B O 4989 C CB . SER B 214 ? 1.2848 1.4427 1.5806 -0.1186 0.0744 -0.1802 214 SER B CB 4990 O OG . SER B 214 ? 1.3078 1.4482 1.5948 -0.1256 0.0931 -0.1685 214 SER B OG 4991 N N . GLN B 215 ? 1.2468 1.4303 1.5372 -0.1024 0.0845 -0.1710 215 GLN B N 4992 C CA . GLN B 215 ? 1.2475 1.4390 1.5420 -0.1031 0.1028 -0.1659 215 GLN B CA 4993 C C . GLN B 215 ? 1.2136 1.3878 1.4756 -0.0961 0.1091 -0.1488 215 GLN B C 4994 O O . GLN B 215 ? 1.1514 1.3191 1.4071 -0.0995 0.1281 -0.1390 215 GLN B O 4995 C CB . GLN B 215 ? 1.2812 1.4754 1.5975 -0.1167 0.1230 -0.1679 215 GLN B CB 4996 C CG . GLN B 215 ? 1.2706 1.4820 1.6218 -0.1249 0.1177 -0.1858 215 GLN B CG 4997 C CD . GLN B 215 ? 1.2908 1.5112 1.6688 -0.1377 0.1396 -0.1890 215 GLN B CD 4998 O OE1 . GLN B 215 ? 1.3393 1.5840 1.7487 -0.1414 0.1409 -0.2030 215 GLN B OE1 4999 N NE2 . GLN B 215 ? 1.2840 1.4844 1.6501 -0.1446 0.1573 -0.1760 215 GLN B NE2 5000 N N . ASN B 216 ? 1.2616 1.4280 1.5031 -0.0863 0.0927 -0.1454 216 ASN B N 5001 C CA . ASN B 216 ? 1.3001 1.4545 1.5133 -0.0774 0.0944 -0.1322 216 ASN B CA 5002 C C . ASN B 216 ? 1.2791 1.4103 1.4704 -0.0803 0.1056 -0.1179 216 ASN B C 5003 O O . ASN B 216 ? 1.2839 1.4088 1.4579 -0.0753 0.1147 -0.1075 216 ASN B O 5004 C CB . ASN B 216 ? 1.2912 1.4609 1.5084 -0.0723 0.1034 -0.1321 216 ASN B CB 5005 C CG . ASN B 216 ? 1.2271 1.4209 1.4675 -0.0688 0.0927 -0.1470 216 ASN B CG 5006 O OD1 . ASN B 216 ? 1.1170 1.3120 1.3569 -0.0631 0.0733 -0.1529 216 ASN B OD1 5007 N ND2 . ASN B 216 ? 1.2376 1.4506 1.4992 -0.0723 0.1053 -0.1534 216 ASN B ND2 5008 N N . LYS B 217 ? 1.2567 1.3756 1.4490 -0.0876 0.1044 -0.1184 217 LYS B N 5009 C CA . LYS B 217 ? 1.2594 1.3546 1.4284 -0.0880 0.1089 -0.1061 217 LYS B CA 5010 C C . LYS B 217 ? 1.2456 1.3331 1.4120 -0.0893 0.0937 -0.1109 217 LYS B C 5011 O O . LYS B 217 ? 1.2604 1.3532 1.4457 -0.0968 0.0911 -0.1211 217 LYS B O 5012 C CB . LYS B 217 ? 1.3389 1.4241 1.5104 -0.0968 0.1298 -0.0994 217 LYS B CB 5013 C CG . LYS B 217 ? 1.4071 1.4693 1.5507 -0.0934 0.1364 -0.0843 217 LYS B CG 5014 C CD . LYS B 217 ? 1.4548 1.5080 1.5973 -0.0988 0.1583 -0.0753 217 LYS B CD 5015 C CE . LYS B 217 ? 1.4848 1.5339 1.6478 -0.1119 0.1669 -0.0804 217 LYS B CE 5016 N NZ . LYS B 217 ? 1.4777 1.5055 1.6294 -0.1145 0.1642 -0.0765 217 LYS B NZ 5017 N N . CYS B 218 ? 1.2075 1.2837 1.3508 -0.0816 0.0833 -0.1041 218 CYS B N 5018 C CA . CYS B 218 ? 1.1121 1.1827 1.2493 -0.0804 0.0672 -0.1080 218 CYS B CA 5019 C C . CYS B 218 ? 1.0743 1.1254 1.1986 -0.0848 0.0721 -0.1017 218 CYS B C 5020 O O . CYS B 218 ? 1.0357 1.0745 1.1473 -0.0847 0.0843 -0.0912 218 CYS B O 5021 C CB . CYS B 218 ? 1.1201 1.1897 1.2405 -0.0698 0.0535 -0.1041 218 CYS B CB 5022 S SG . CYS B 218 ? 1.1502 1.2413 1.2856 -0.0631 0.0413 -0.1140 218 CYS B SG 5023 N N . ASN B 219 ? 1.0386 1.0870 1.1657 -0.0879 0.0622 -0.1086 219 ASN B N 5024 C CA . ASN B 219 ? 1.0095 1.0397 1.1207 -0.0897 0.0630 -0.1032 219 ASN B CA 5025 C C . ASN B 219 ? 1.0230 1.0504 1.1193 -0.0834 0.0461 -0.1036 219 ASN B C 5026 O O . ASN B 219 ? 1.0657 1.0993 1.1695 -0.0845 0.0346 -0.1133 219 ASN B O 5027 C CB . ASN B 219 ? 0.9838 1.0111 1.1101 -0.0996 0.0685 -0.1107 219 ASN B CB 5028 C CG . ASN B 219 ? 0.9512 0.9594 1.0613 -0.1010 0.0701 -0.1055 219 ASN B CG 5029 O OD1 . ASN B 219 ? 0.9223 0.9196 1.0104 -0.0949 0.0691 -0.0956 219 ASN B OD1 5030 N ND2 . ASN B 219 ? 0.9599 0.9648 1.0820 -0.1088 0.0722 -0.1133 219 ASN B ND2 5031 N N . PHE B 220 ? 0.9970 1.0157 1.0726 -0.0765 0.0447 -0.0933 220 PHE B N 5032 C CA . PHE B 220 ? 0.9971 1.0098 1.0564 -0.0715 0.0314 -0.0914 220 PHE B CA 5033 C C . PHE B 220 ? 1.0359 1.0319 1.0793 -0.0732 0.0361 -0.0852 220 PHE B C 5034 O O . PHE B 220 ? 1.0459 1.0354 1.0741 -0.0697 0.0278 -0.0823 220 PHE B O 5035 C CB . PHE B 220 ? 0.9665 0.9812 1.0153 -0.0629 0.0257 -0.0851 220 PHE B CB 5036 C CG . PHE B 220 ? 0.9454 0.9762 1.0087 -0.0598 0.0200 -0.0914 220 PHE B CG 5037 C CD1 . PHE B 220 ? 0.9245 0.9659 1.0010 -0.0607 0.0090 -0.1021 220 PHE B CD1 5038 C CD2 . PHE B 220 ? 0.9098 0.9459 0.9734 -0.0551 0.0252 -0.0873 220 PHE B CD2 5039 C CE1 . PHE B 220 ? 0.8815 0.9381 0.9721 -0.0572 0.0035 -0.1085 220 PHE B CE1 5040 C CE2 . PHE B 220 ? 0.8737 0.9252 0.9511 -0.0518 0.0202 -0.0939 220 PHE B CE2 5041 C CZ . PHE B 220 ? 0.8675 0.9294 0.9590 -0.0529 0.0094 -0.1045 220 PHE B CZ 5042 N N . TYR B 221 ? 1.0529 1.0418 1.1000 -0.0785 0.0498 -0.0829 221 TYR B N 5043 C CA . TYR B 221 ? 1.0978 1.0705 1.1309 -0.0795 0.0551 -0.0772 221 TYR B CA 5044 C C . TYR B 221 ? 1.0729 1.0419 1.1094 -0.0848 0.0507 -0.0855 221 TYR B C 5045 O O . TYR B 221 ? 1.0689 1.0326 1.0916 -0.0822 0.0426 -0.0852 221 TYR B O 5046 C CB . TYR B 221 ? 1.0940 1.0582 1.1275 -0.0817 0.0715 -0.0702 221 TYR B CB 5047 C CG . TYR B 221 ? 1.1357 1.0827 1.1566 -0.0825 0.0774 -0.0651 221 TYR B CG 5048 C CD1 . TYR B 221 ? 1.1114 1.0514 1.1140 -0.0771 0.0709 -0.0605 221 TYR B CD1 5049 C CD2 . TYR B 221 ? 1.1631 1.1007 1.1912 -0.0887 0.0897 -0.0648 221 TYR B CD2 5050 C CE1 . TYR B 221 ? 1.0887 1.0142 1.0808 -0.0773 0.0762 -0.0568 221 TYR B CE1 5051 C CE2 . TYR B 221 ? 1.1673 1.0886 1.1843 -0.0887 0.0946 -0.0606 221 TYR B CE2 5052 C CZ . TYR B 221 ? 1.1416 1.0577 1.1408 -0.0827 0.0875 -0.0570 221 TYR B CZ 5053 O OH . TYR B 221 ? 1.2050 1.1062 1.1944 -0.0823 0.0923 -0.0538 221 TYR B OH 5054 N N . ASP B 222 ? 1.0807 1.0526 1.1357 -0.0924 0.0566 -0.0932 222 ASP B N 5055 C CA . ASP B 222 ? 1.0981 1.0656 1.1578 -0.0978 0.0540 -0.1020 222 ASP B CA 5056 C C . ASP B 222 ? 1.0829 1.0650 1.1655 -0.1027 0.0481 -0.1158 222 ASP B C 5057 O O . ASP B 222 ? 1.1338 1.1146 1.2300 -0.1097 0.0510 -0.1245 222 ASP B O 5058 C CB . ASP B 222 ? 1.0972 1.0495 1.1571 -0.1028 0.0681 -0.0982 222 ASP B CB 5059 C CG . ASP B 222 ? 1.1150 1.0685 1.1903 -0.1076 0.0823 -0.0956 222 ASP B CG 5060 O OD1 . ASP B 222 ? 1.1161 1.0847 1.2073 -0.1092 0.0812 -0.1006 222 ASP B OD1 5061 O OD2 . ASP B 222 ? 1.0775 1.0167 1.1486 -0.1096 0.0949 -0.0884 222 ASP B OD2 5062 N N . ASN B 223 ? 1.1192 1.1155 1.2067 -0.0987 0.0392 -0.1185 223 ASN B N 5063 C CA . ASN B 223 ? 1.1720 1.1848 1.2825 -0.1020 0.0327 -0.1320 223 ASN B CA 5064 C C . ASN B 223 ? 1.2155 1.2293 1.3259 -0.1027 0.0202 -0.1431 223 ASN B C 5065 O O . ASN B 223 ? 1.1917 1.1997 1.2816 -0.0970 0.0103 -0.1401 223 ASN B O 5066 C CB . ASN B 223 ? 1.1684 1.1949 1.2810 -0.0955 0.0243 -0.1318 223 ASN B CB 5067 C CG . ASN B 223 ? 1.2134 1.2585 1.3541 -0.0992 0.0227 -0.1443 223 ASN B CG 5068 O OD1 . ASN B 223 ? 1.2708 1.3222 1.4259 -0.1034 0.0170 -0.1568 223 ASN B OD1 5069 N ND2 . ASN B 223 ? 1.2315 1.2865 1.3808 -0.0974 0.0278 -0.1418 223 ASN B ND2 5070 N N . LYS B 224 ? 1.2921 1.3138 1.4258 -0.1098 0.0209 -0.1561 224 LYS B N 5071 C CA . LYS B 224 ? 1.3205 1.3436 1.4559 -0.1108 0.0095 -0.1685 224 LYS B CA 5072 C C . LYS B 224 ? 1.2773 1.3182 1.4227 -0.1067 -0.0068 -0.1801 224 LYS B C 5073 O O . LYS B 224 ? 1.3269 1.3704 1.4704 -0.1052 -0.0190 -0.1903 224 LYS B O 5074 C CB . LYS B 224 ? 1.3777 1.3978 1.5333 -0.1210 0.0190 -0.1775 224 LYS B CB 5075 C CG . LYS B 224 ? 1.3984 1.3984 1.5424 -0.1243 0.0333 -0.1673 224 LYS B CG 5076 C CD . LYS B 224 ? 1.3978 1.3853 1.5155 -0.1191 0.0264 -0.1640 224 LYS B CD 5077 C CE . LYS B 224 ? 1.3866 1.3547 1.4932 -0.1212 0.0401 -0.1540 224 LYS B CE 5078 N NZ . LYS B 224 ? 1.3650 1.3273 1.4598 -0.1174 0.0494 -0.1378 224 LYS B NZ 5079 N N . ASP B 225 ? 1.2416 1.2948 1.3970 -0.1041 -0.0075 -0.1790 225 ASP B N 5080 C CA . ASP B 225 ? 1.2424 1.3121 1.4070 -0.0989 -0.0237 -0.1895 225 ASP B CA 5081 C C . ASP B 225 ? 1.2701 1.3328 1.4065 -0.0894 -0.0388 -0.1847 225 ASP B C 5082 O O . ASP B 225 ? 1.2874 1.3404 1.4028 -0.0844 -0.0372 -0.1710 225 ASP B O 5083 C CB . ASP B 225 ? 1.2070 1.2898 1.3857 -0.0970 -0.0207 -0.1879 225 ASP B CB 5084 C CG . ASP B 225 ? 1.2418 1.3439 1.4369 -0.0927 -0.0361 -0.2014 225 ASP B CG 5085 O OD1 . ASP B 225 ? 1.3460 1.4477 1.5283 -0.0859 -0.0528 -0.2052 225 ASP B OD1 5086 O OD2 . ASP B 225 ? 1.2981 1.4161 1.5187 -0.0956 -0.0316 -0.2083 225 ASP B OD2 5087 N N . LEU B 226 ? 1.3190 1.3868 1.4553 -0.0869 -0.0533 -0.1963 226 LEU B N 5088 C CA . LEU B 226 ? 1.3310 1.3910 1.4390 -0.0783 -0.0671 -0.1921 226 LEU B CA 5089 C C . LEU B 226 ? 1.2595 1.3230 1.3580 -0.0692 -0.0773 -0.1856 226 LEU B C 5090 O O . LEU B 226 ? 1.2675 1.3198 1.3397 -0.0631 -0.0824 -0.1751 226 LEU B O 5091 C CB . LEU B 226 ? 1.3800 1.4461 1.4909 -0.0772 -0.0805 -0.2074 226 LEU B CB 5092 C CG . LEU B 226 ? 1.4078 1.4669 1.5224 -0.0850 -0.0723 -0.2132 226 LEU B CG 5093 C CD1 . LEU B 226 ? 1.4489 1.5222 1.5878 -0.0883 -0.0805 -0.2338 226 LEU B CD1 5094 C CD2 . LEU B 226 ? 1.4111 1.4540 1.4935 -0.0812 -0.0741 -0.2052 226 LEU B CD2 5095 N N . GLU B 227 ? 1.2091 1.2883 1.3302 -0.0685 -0.0797 -0.1923 227 GLU B N 5096 C CA . GLU B 227 ? 1.2157 1.2984 1.3314 -0.0600 -0.0882 -0.1869 227 GLU B CA 5097 C C . GLU B 227 ? 1.1840 1.2571 1.2896 -0.0602 -0.0756 -0.1712 227 GLU B C 5098 O O . GLU B 227 ? 1.2230 1.2905 1.3127 -0.0531 -0.0818 -0.1621 227 GLU B O 5099 C CB . GLU B 227 ? 1.2242 1.3282 1.3693 -0.0589 -0.0944 -0.2003 227 GLU B CB 5100 C CG . GLU B 227 ? 1.2194 1.3345 1.3707 -0.0535 -0.1135 -0.2150 227 GLU B CG 5101 C CD . GLU B 227 ? 1.2576 1.3948 1.4392 -0.0516 -0.1195 -0.2281 227 GLU B CD 5102 O OE1 . GLU B 227 ? 1.3038 1.4461 1.4816 -0.0415 -0.1356 -0.2307 227 GLU B OE1 5103 O OE2 . GLU B 227 ? 1.2160 1.3656 1.4257 -0.0599 -0.1079 -0.2359 227 GLU B OE2 5104 N N . CYS B 228 ? 1.1385 1.2093 1.2532 -0.0681 -0.0583 -0.1681 228 CYS B N 5105 C CA . CYS B 228 ? 1.0804 1.1411 1.1833 -0.0679 -0.0461 -0.1535 228 CYS B CA 5106 C C . CYS B 228 ? 1.0473 1.0901 1.1210 -0.0652 -0.0472 -0.1422 228 CYS B C 5107 O O . CYS B 228 ? 1.0642 1.1002 1.1229 -0.0601 -0.0480 -0.1314 228 CYS B O 5108 C CB . CYS B 228 ? 1.1034 1.1639 1.2205 -0.0766 -0.0273 -0.1524 228 CYS B CB 5109 S SG . CYS B 228 ? 1.0838 1.1322 1.1858 -0.0755 -0.0123 -0.1352 228 CYS B SG 5110 N N . VAL B 229 ? 1.0660 1.1017 1.1326 -0.0686 -0.0473 -0.1454 229 VAL B N 5111 C CA . VAL B 229 ? 1.0355 1.0555 1.0753 -0.0665 -0.0473 -0.1357 229 VAL B CA 5112 C C . VAL B 229 ? 1.0357 1.0529 1.0572 -0.0581 -0.0613 -0.1308 229 VAL B C 5113 O O . VAL B 229 ? 1.0243 1.0307 1.0273 -0.0552 -0.0590 -0.1188 229 VAL B O 5114 C CB . VAL B 229 ? 1.0187 1.0334 1.0551 -0.0709 -0.0464 -0.1423 229 VAL B CB 5115 C CG1 . VAL B 229 ? 1.0172 1.0183 1.0251 -0.0673 -0.0491 -0.1340 229 VAL B CG1 5116 C CG2 . VAL B 229 ? 1.0091 1.0206 1.0588 -0.0791 -0.0301 -0.1428 229 VAL B CG2 5117 N N . THR B 230 ? 1.0627 1.0893 1.0899 -0.0540 -0.0757 -0.1400 230 THR B N 5118 C CA . THR B 230 ? 1.1275 1.1499 1.1368 -0.0456 -0.0895 -0.1351 230 THR B CA 5119 C C . THR B 230 ? 1.1141 1.1343 1.1213 -0.0417 -0.0879 -0.1248 230 THR B C 5120 O O . THR B 230 ? 1.1649 1.1745 1.1524 -0.0371 -0.0922 -0.1147 230 THR B O 5121 C CB . THR B 230 ? 1.1661 1.2002 1.1845 -0.0409 -0.1056 -0.1476 230 THR B CB 5122 O OG1 . THR B 230 ? 1.2667 1.3039 1.2885 -0.0445 -0.1074 -0.1585 230 THR B OG1 5123 C CG2 . THR B 230 ? 1.1953 1.2224 1.1923 -0.0316 -0.1203 -0.1415 230 THR B CG2 5124 N N . ASN B 231 ? 1.0989 1.1290 1.1267 -0.0437 -0.0811 -0.1275 231 ASN B N 5125 C CA . ASN B 231 ? 1.0679 1.0975 1.0958 -0.0400 -0.0790 -0.1195 231 ASN B CA 5126 C C . ASN B 231 ? 1.0627 1.0809 1.0789 -0.0425 -0.0657 -0.1075 231 ASN B C 5127 O O . ASN B 231 ? 1.0499 1.0613 1.0549 -0.0381 -0.0675 -0.0984 231 ASN B O 5128 C CB . ASN B 231 ? 1.0732 1.1191 1.1270 -0.0406 -0.0765 -0.1278 231 ASN B CB 5129 C CG . ASN B 231 ? 1.1123 1.1701 1.1774 -0.0353 -0.0920 -0.1386 231 ASN B CG 5130 O OD1 . ASN B 231 ? 1.1028 1.1547 1.1539 -0.0286 -0.1056 -0.1362 231 ASN B OD1 5131 N ND2 . ASN B 231 ? 1.0985 1.1730 1.1892 -0.0381 -0.0901 -0.1504 231 ASN B ND2 5132 N N . LEU B 232 ? 1.0517 1.0677 1.0713 -0.0492 -0.0528 -0.1078 232 LEU B N 5133 C CA . LEU B 232 ? 1.0577 1.0624 1.0651 -0.0507 -0.0411 -0.0969 232 LEU B CA 5134 C C . LEU B 232 ? 1.1129 1.1049 1.0970 -0.0480 -0.0461 -0.0891 232 LEU B C 5135 O O . LEU B 232 ? 1.1641 1.1489 1.1377 -0.0456 -0.0428 -0.0794 232 LEU B O 5136 C CB . LEU B 232 ? 1.0718 1.0744 1.0857 -0.0578 -0.0274 -0.0987 232 LEU B CB 5137 C CG . LEU B 232 ? 1.0773 1.0894 1.1116 -0.0611 -0.0172 -0.1020 232 LEU B CG 5138 C CD1 . LEU B 232 ? 1.0873 1.0954 1.1283 -0.0687 -0.0043 -0.1041 232 LEU B CD1 5139 C CD2 . LEU B 232 ? 1.0529 1.0642 1.0835 -0.0570 -0.0115 -0.0931 232 LEU B CD2 5140 N N . GLN B 233 ? 1.1370 1.1272 1.1134 -0.0479 -0.0545 -0.0936 233 GLN B N 5141 C CA . GLN B 233 ? 1.0974 1.0763 1.0508 -0.0450 -0.0597 -0.0864 233 GLN B CA 5142 C C . GLN B 233 ? 1.0428 1.0190 0.9890 -0.0389 -0.0682 -0.0794 233 GLN B C 5143 O O . GLN B 233 ? 1.0364 1.0025 0.9675 -0.0377 -0.0662 -0.0695 233 GLN B O 5144 C CB . GLN B 233 ? 1.1593 1.1387 1.1060 -0.0448 -0.0686 -0.0939 233 GLN B CB 5145 C CG . GLN B 233 ? 1.2205 1.1985 1.1688 -0.0507 -0.0603 -0.0994 233 GLN B CG 5146 C CD . GLN B 233 ? 1.2692 1.2494 1.2124 -0.0500 -0.0700 -0.1091 233 GLN B CD 5147 O OE1 . GLN B 233 ? 1.2725 1.2491 1.2115 -0.0535 -0.0652 -0.1128 233 GLN B OE1 5148 N NE2 . GLN B 233 ? 1.2519 1.2380 1.1952 -0.0446 -0.0842 -0.1136 233 GLN B NE2 5149 N N . GLU B 234 ? 0.9863 0.9715 0.9447 -0.0351 -0.0777 -0.0851 234 GLU B N 5150 C CA . GLU B 234 ? 1.0112 0.9936 0.9658 -0.0290 -0.0861 -0.0795 234 GLU B CA 5151 C C . GLU B 234 ? 0.9834 0.9633 0.9404 -0.0293 -0.0768 -0.0718 234 GLU B C 5152 O O . GLU B 234 ? 1.0003 0.9706 0.9451 -0.0270 -0.0780 -0.0628 234 GLU B O 5153 C CB . GLU B 234 ? 1.0719 1.0659 1.0418 -0.0245 -0.0977 -0.0887 234 GLU B CB 5154 C CG . GLU B 234 ? 1.1175 1.1106 1.0893 -0.0179 -0.1056 -0.0848 234 GLU B CG 5155 C CD . GLU B 234 ? 1.2121 1.1906 1.1630 -0.0137 -0.1143 -0.0755 234 GLU B CD 5156 O OE1 . GLU B 234 ? 1.2780 1.2455 1.2112 -0.0166 -0.1092 -0.0679 234 GLU B OE1 5157 O OE2 . GLU B 234 ? 1.3226 1.3004 1.2751 -0.0072 -0.1260 -0.0756 234 GLU B OE2 5158 N N . VAL B 235 ? 0.9369 0.9253 0.9094 -0.0320 -0.0673 -0.0756 235 VAL B N 5159 C CA . VAL B 235 ? 0.8963 0.8830 0.8700 -0.0316 -0.0580 -0.0691 235 VAL B CA 5160 C C . VAL B 235 ? 0.8708 0.8450 0.8275 -0.0336 -0.0514 -0.0599 235 VAL B C 5161 O O . VAL B 235 ? 0.8691 0.8378 0.8197 -0.0310 -0.0513 -0.0528 235 VAL B O 5162 C CB . VAL B 235 ? 0.8565 0.8522 0.8453 -0.0349 -0.0464 -0.0734 235 VAL B CB 5163 C CG1 . VAL B 235 ? 0.8331 0.8255 0.8187 -0.0337 -0.0368 -0.0660 235 VAL B CG1 5164 C CG2 . VAL B 235 ? 0.8489 0.8589 0.8565 -0.0329 -0.0513 -0.0825 235 VAL B CG2 5165 N N . ALA B 236 ? 0.9073 0.8778 0.8582 -0.0382 -0.0456 -0.0609 236 ALA B N 5166 C CA . ALA B 236 ? 0.9669 0.9267 0.9023 -0.0399 -0.0392 -0.0533 236 ALA B CA 5167 C C . ALA B 236 ? 1.0235 0.9752 0.9444 -0.0369 -0.0471 -0.0464 236 ALA B C 5168 O O . ALA B 236 ? 1.0559 1.0013 0.9694 -0.0366 -0.0427 -0.0389 236 ALA B O 5169 C CB . ALA B 236 ? 0.9594 0.9167 0.8904 -0.0446 -0.0345 -0.0572 236 ALA B CB 5170 N N . ARG B 237 ? 1.0887 1.0406 1.0061 -0.0346 -0.0586 -0.0491 237 ARG B N 5171 C CA . ARG B 237 ? 1.1168 1.0595 1.0195 -0.0318 -0.0660 -0.0418 237 ARG B CA 5172 C C . ARG B 237 ? 1.0311 0.9723 0.9391 -0.0282 -0.0689 -0.0367 237 ARG B C 5173 O O . ARG B 237 ? 1.0088 0.9410 0.9070 -0.0279 -0.0684 -0.0285 237 ARG B O 5174 C CB . ARG B 237 ? 1.1967 1.1394 1.0935 -0.0290 -0.0785 -0.0460 237 ARG B CB 5175 C CG . ARG B 237 ? 1.2996 1.2306 1.1782 -0.0260 -0.0856 -0.0373 237 ARG B CG 5176 C CD . ARG B 237 ? 1.4730 1.4044 1.3477 -0.0209 -0.1002 -0.0412 237 ARG B CD 5177 N NE . ARG B 237 ? 1.5490 1.4875 1.4404 -0.0165 -0.1083 -0.0459 237 ARG B NE 5178 C CZ . ARG B 237 ? 1.5869 1.5202 1.4805 -0.0129 -0.1127 -0.0401 237 ARG B CZ 5179 N NH1 . ARG B 237 ? 1.6137 1.5344 1.4948 -0.0139 -0.1095 -0.0290 237 ARG B NH1 5180 N NH2 . ARG B 237 ? 1.5593 1.5006 1.4692 -0.0085 -0.1201 -0.0462 237 ARG B NH2 5181 N N . ILE B 238 ? 0.9852 0.9356 0.9094 -0.0256 -0.0719 -0.0423 238 ILE B N 5182 C CA . ILE B 238 ? 0.9835 0.9332 0.9138 -0.0214 -0.0757 -0.0391 238 ILE B CA 5183 C C . ILE B 238 ? 0.9195 0.8673 0.8501 -0.0229 -0.0652 -0.0340 238 ILE B C 5184 O O . ILE B 238 ? 0.8581 0.7988 0.7844 -0.0217 -0.0665 -0.0276 238 ILE B O 5185 C CB . ILE B 238 ? 0.9834 0.9452 0.9316 -0.0177 -0.0807 -0.0474 238 ILE B CB 5186 C CG1 . ILE B 238 ? 1.0033 0.9676 0.9525 -0.0150 -0.0930 -0.0532 238 ILE B CG1 5187 C CG2 . ILE B 238 ? 0.9957 0.9567 0.9500 -0.0131 -0.0843 -0.0450 238 ILE B CG2 5188 C CD1 . ILE B 238 ? 0.9889 0.9674 0.9575 -0.0118 -0.0973 -0.0632 238 ILE B CD1 5189 N N . VAL B 239 ? 0.8715 0.8252 0.8074 -0.0255 -0.0551 -0.0369 239 VAL B N 5190 C CA . VAL B 239 ? 0.8860 0.8392 0.8228 -0.0256 -0.0456 -0.0332 239 VAL B CA 5191 C C . VAL B 239 ? 0.9124 0.8559 0.8359 -0.0282 -0.0411 -0.0261 239 VAL B C 5192 O O . VAL B 239 ? 0.9193 0.8596 0.8420 -0.0267 -0.0402 -0.0215 239 VAL B O 5193 C CB . VAL B 239 ? 0.8500 0.8103 0.7941 -0.0275 -0.0356 -0.0374 239 VAL B CB 5194 C CG1 . VAL B 239 ? 0.8521 0.8103 0.7936 -0.0270 -0.0259 -0.0330 239 VAL B CG1 5195 C CG2 . VAL B 239 ? 0.8644 0.8359 0.8232 -0.0248 -0.0384 -0.0441 239 VAL B CG2 5196 N N . GLY B 240 ? 0.9891 0.9289 0.9032 -0.0320 -0.0384 -0.0260 240 GLY B N 5197 C CA . GLY B 240 ? 0.9996 0.9324 0.9023 -0.0347 -0.0314 -0.0207 240 GLY B CA 5198 C C . GLY B 240 ? 1.0293 0.9537 0.9186 -0.0357 -0.0362 -0.0154 240 GLY B C 5199 O O . GLY B 240 ? 1.0710 0.9902 0.9525 -0.0375 -0.0308 -0.0101 240 GLY B O 5200 N N . ASN B 241 ? 1.0189 0.9420 0.9051 -0.0343 -0.0462 -0.0167 241 ASN B N 5201 C CA . ASN B 241 ? 1.0540 0.9685 0.9237 -0.0353 -0.0498 -0.0118 241 ASN B CA 5202 C C . ASN B 241 ? 0.9989 0.9080 0.8655 -0.0319 -0.0612 -0.0084 241 ASN B C 5203 O O . ASN B 241 ? 0.9800 0.8840 0.8338 -0.0311 -0.0673 -0.0071 241 ASN B O 5204 C CB . ASN B 241 ? 1.0814 0.9976 0.9436 -0.0369 -0.0500 -0.0174 241 ASN B CB 5205 C CG . ASN B 241 ? 1.1426 1.0507 0.9850 -0.0384 -0.0491 -0.0123 241 ASN B CG 5206 O OD1 . ASN B 241 ? 1.1228 1.0280 0.9541 -0.0367 -0.0571 -0.0129 241 ASN B OD1 5207 N ND2 . ASN B 241 ? 1.2171 1.1220 1.0544 -0.0413 -0.0392 -0.0075 241 ASN B ND2 5208 N N . SER B 242 ? 0.9292 0.8385 0.8066 -0.0295 -0.0642 -0.0068 242 SER B N 5209 C CA . SER B 242 ? 0.9275 0.8309 0.8040 -0.0257 -0.0755 -0.0040 242 SER B CA 5210 C C . SER B 242 ? 0.8953 0.7928 0.7773 -0.0250 -0.0760 0.0017 242 SER B C 5211 O O . SER B 242 ? 0.8832 0.7762 0.7683 -0.0212 -0.0858 0.0028 242 SER B O 5212 C CB . SER B 242 ? 0.9396 0.8518 0.8284 -0.0214 -0.0841 -0.0127 242 SER B CB 5213 O OG . SER B 242 ? 0.9756 0.8946 0.8811 -0.0193 -0.0830 -0.0159 242 SER B OG 5214 N N . GLY B 243 ? 0.8801 0.7778 0.7644 -0.0281 -0.0664 0.0047 243 GLY B N 5215 C CA . GLY B 243 ? 0.8889 0.7816 0.7799 -0.0280 -0.0665 0.0094 243 GLY B CA 5216 C C . GLY B 243 ? 0.8847 0.7864 0.7922 -0.0261 -0.0633 0.0045 243 GLY B C 5217 O O . GLY B 243 ? 0.9193 0.8182 0.8329 -0.0266 -0.0619 0.0073 243 GLY B O 5218 N N . LEU B 244 ? 0.8418 0.7543 0.7567 -0.0237 -0.0621 -0.0028 244 LEU B N 5219 C CA . LEU B 244 ? 0.7972 0.7184 0.7252 -0.0209 -0.0589 -0.0073 244 LEU B CA 5220 C C . LEU B 244 ? 0.8072 0.7302 0.7327 -0.0235 -0.0479 -0.0056 244 LEU B C 5221 O O . LEU B 244 ? 0.8532 0.7734 0.7683 -0.0273 -0.0419 -0.0031 244 LEU B O 5222 C CB . LEU B 244 ? 0.7588 0.6908 0.6946 -0.0177 -0.0597 -0.0150 244 LEU B CB 5223 C CG . LEU B 244 ? 0.7131 0.6469 0.6548 -0.0139 -0.0706 -0.0191 244 LEU B CG 5224 C CD1 . LEU B 244 ? 0.6990 0.6448 0.6486 -0.0123 -0.0688 -0.0269 244 LEU B CD1 5225 C CD2 . LEU B 244 ? 0.7317 0.6639 0.6829 -0.0096 -0.0774 -0.0195 244 LEU B CD2 5226 N N . ASN B 245 ? 0.7999 0.7280 0.7349 -0.0205 -0.0458 -0.0077 245 ASN B N 5227 C CA . ASN B 245 ? 0.7696 0.7005 0.7035 -0.0213 -0.0364 -0.0071 245 ASN B CA 5228 C C . ASN B 245 ? 0.8083 0.7473 0.7436 -0.0188 -0.0310 -0.0118 245 ASN B C 5229 O O . ASN B 245 ? 0.7246 0.6706 0.6680 -0.0139 -0.0320 -0.0159 245 ASN B O 5230 C CB . ASN B 245 ? 0.7541 0.6862 0.6970 -0.0191 -0.0375 -0.0073 245 ASN B CB 5231 C CG . ASN B 245 ? 0.7821 0.7164 0.7235 -0.0198 -0.0287 -0.0064 245 ASN B CG 5232 O OD1 . ASN B 245 ? 0.7409 0.6773 0.6759 -0.0203 -0.0217 -0.0068 245 ASN B OD1 5233 N ND2 . ASN B 245 ? 0.8292 0.7628 0.7773 -0.0200 -0.0292 -0.0055 245 ASN B ND2 5234 N N . ILE B 246 ? 0.8383 0.7758 0.7652 -0.0223 -0.0248 -0.0109 246 ILE B N 5235 C CA . ILE B 246 ? 0.8168 0.7596 0.7444 -0.0213 -0.0187 -0.0144 246 ILE B CA 5236 C C . ILE B 246 ? 0.7780 0.7250 0.7086 -0.0171 -0.0125 -0.0151 246 ILE B C 5237 O O . ILE B 246 ? 0.7927 0.7449 0.7262 -0.0143 -0.0090 -0.0178 246 ILE B O 5238 C CB . ILE B 246 ? 0.8346 0.7732 0.7531 -0.0262 -0.0134 -0.0137 246 ILE B CB 5239 C CG1 . ILE B 246 ? 0.8714 0.8145 0.7930 -0.0262 -0.0087 -0.0178 246 ILE B CG1 5240 C CG2 . ILE B 246 ? 0.8078 0.7423 0.7193 -0.0279 -0.0062 -0.0102 246 ILE B CG2 5241 C CD1 . ILE B 246 ? 0.8965 0.8360 0.8117 -0.0311 -0.0061 -0.0191 246 ILE B CD1 5242 N N . TYR B 247 ? 0.7507 0.6957 0.6805 -0.0165 -0.0111 -0.0125 247 TYR B N 5243 C CA . TYR B 247 ? 0.7793 0.7285 0.7115 -0.0114 -0.0067 -0.0135 247 TYR B CA 5244 C C . TYR B 247 ? 0.7377 0.6934 0.6791 -0.0053 -0.0129 -0.0171 247 TYR B C 5245 O O . TYR B 247 ? 0.6855 0.6465 0.6281 0.0004 -0.0101 -0.0193 247 TYR B O 5246 C CB . TYR B 247 ? 0.8501 0.7965 0.7807 -0.0129 -0.0041 -0.0109 247 TYR B CB 5247 C CG . TYR B 247 ? 0.9284 0.8712 0.8505 -0.0155 0.0043 -0.0089 247 TYR B CG 5248 C CD1 . TYR B 247 ? 0.9547 0.8936 0.8697 -0.0195 0.0076 -0.0085 247 TYR B CD1 5249 C CD2 . TYR B 247 ? 1.0740 1.0179 0.9965 -0.0137 0.0084 -0.0085 247 TYR B CD2 5250 C CE1 . TYR B 247 ? 1.0255 0.9608 0.9336 -0.0215 0.0150 -0.0075 247 TYR B CE1 5251 C CE2 . TYR B 247 ? 1.1856 1.1264 1.1011 -0.0153 0.0158 -0.0074 247 TYR B CE2 5252 C CZ . TYR B 247 ? 1.1654 1.1015 1.0734 -0.0192 0.0192 -0.0069 247 TYR B CZ 5253 O OH . TYR B 247 ? 1.1324 1.0651 1.0341 -0.0203 0.0263 -0.0066 247 TYR B OH 5254 N N . ASN B 248 ? 0.7028 0.6576 0.6500 -0.0062 -0.0214 -0.0179 248 ASN B N 5255 C CA . ASN B 248 ? 0.6874 0.6479 0.6442 -0.0004 -0.0282 -0.0222 248 ASN B CA 5256 C C . ASN B 248 ? 0.6881 0.6458 0.6496 -0.0019 -0.0373 -0.0229 248 ASN B C 5257 O O . ASN B 248 ? 0.6829 0.6340 0.6461 -0.0048 -0.0421 -0.0202 248 ASN B O 5258 C CB . ASN B 248 ? 0.6860 0.6475 0.6480 0.0021 -0.0294 -0.0229 248 ASN B CB 5259 C CG . ASN B 248 ? 0.6719 0.6385 0.6449 0.0079 -0.0377 -0.0283 248 ASN B CG 5260 O OD1 . ASN B 248 ? 0.6288 0.5980 0.6054 0.0101 -0.0428 -0.0314 248 ASN B OD1 5261 N ND2 . ASN B 248 ? 0.6913 0.6601 0.6707 0.0105 -0.0394 -0.0305 248 ASN B ND2 5262 N N . LEU B 249 ? 0.6723 0.6351 0.6364 0.0002 -0.0395 -0.0266 249 LEU B N 5263 C CA . LEU B 249 ? 0.6702 0.6312 0.6384 -0.0003 -0.0482 -0.0281 249 LEU B CA 5264 C C . LEU B 249 ? 0.6624 0.6205 0.6390 0.0023 -0.0579 -0.0293 249 LEU B C 5265 O O . LEU B 249 ? 0.7067 0.6588 0.6840 0.0008 -0.0654 -0.0281 249 LEU B O 5266 C CB . LEU B 249 ? 0.6859 0.6563 0.6586 0.0029 -0.0481 -0.0337 249 LEU B CB 5267 C CG . LEU B 249 ? 0.6763 0.6480 0.6557 0.0042 -0.0578 -0.0374 249 LEU B CG 5268 C CD1 . LEU B 249 ? 0.7013 0.6645 0.6738 -0.0013 -0.0607 -0.0335 249 LEU B CD1 5269 C CD2 . LEU B 249 ? 0.6401 0.6238 0.6258 0.0074 -0.0552 -0.0437 249 LEU B CD2 5270 N N . TYR B 250 ? 0.6546 0.6169 0.6376 0.0068 -0.0585 -0.0323 250 TYR B N 5271 C CA . TYR B 250 ? 0.6580 0.6181 0.6516 0.0098 -0.0681 -0.0352 250 TYR B CA 5272 C C . TYR B 250 ? 0.6833 0.6350 0.6782 0.0057 -0.0682 -0.0307 250 TYR B C 5273 O O . TYR B 250 ? 0.7349 0.6829 0.7395 0.0070 -0.0755 -0.0325 250 TYR B O 5274 C CB . TYR B 250 ? 0.6415 0.6129 0.6436 0.0182 -0.0704 -0.0434 250 TYR B CB 5275 C CG . TYR B 250 ? 0.6487 0.6284 0.6511 0.0215 -0.0702 -0.0476 250 TYR B CG 5276 C CD1 . TYR B 250 ? 0.6699 0.6479 0.6773 0.0218 -0.0783 -0.0497 250 TYR B CD1 5277 C CD2 . TYR B 250 ? 0.6856 0.6742 0.6830 0.0238 -0.0614 -0.0491 250 TYR B CD2 5278 C CE1 . TYR B 250 ? 0.6896 0.6766 0.6991 0.0243 -0.0778 -0.0543 250 TYR B CE1 5279 C CE2 . TYR B 250 ? 0.6601 0.6567 0.6590 0.0257 -0.0599 -0.0528 250 TYR B CE2 5280 C CZ . TYR B 250 ? 0.6982 0.6949 0.7041 0.0258 -0.0680 -0.0559 250 TYR B CZ 5281 O OH . TYR B 250 ? 0.7617 0.7681 0.7714 0.0275 -0.0664 -0.0606 250 TYR B OH 5282 N N . ALA B 251 ? 0.7273 0.6755 0.7130 0.0004 -0.0601 -0.0251 251 ALA B N 5283 C CA . ALA B 251 ? 0.7944 0.7353 0.7805 -0.0047 -0.0580 -0.0202 251 ALA B CA 5284 C C . ALA B 251 ? 0.8277 0.7567 0.8051 -0.0116 -0.0585 -0.0125 251 ALA B C 5285 O O . ALA B 251 ? 0.7875 0.7152 0.7547 -0.0132 -0.0569 -0.0105 251 ALA B O 5286 C CB . ALA B 251 ? 0.7941 0.7396 0.7756 -0.0055 -0.0484 -0.0195 251 ALA B CB 5287 N N . PRO B 252 ? 0.8926 0.8128 0.8736 -0.0158 -0.0603 -0.0082 252 PRO B N 5288 C CA . PRO B 252 ? 0.8991 0.8072 0.8691 -0.0221 -0.0595 0.0002 252 PRO B CA 5289 C C . PRO B 252 ? 0.8990 0.8081 0.8564 -0.0265 -0.0493 0.0041 252 PRO B C 5290 O O . PRO B 252 ? 0.8517 0.7682 0.8118 -0.0260 -0.0425 0.0016 252 PRO B O 5291 C CB . PRO B 252 ? 0.9252 0.8250 0.9041 -0.0256 -0.0615 0.0036 252 PRO B CB 5292 C CG . PRO B 252 ? 0.8995 0.8094 0.8915 -0.0233 -0.0585 -0.0026 252 PRO B CG 5293 C CD . PRO B 252 ? 0.8716 0.7929 0.8662 -0.0154 -0.0613 -0.0107 252 PRO B CD 5294 N N . CYS B 253 ? 0.9507 0.8522 0.8941 -0.0301 -0.0487 0.0097 253 CYS B N 5295 C CA . CYS B 253 ? 0.9738 0.8756 0.9044 -0.0342 -0.0396 0.0129 253 CYS B CA 5296 C C . CYS B 253 ? 1.0100 0.9052 0.9386 -0.0401 -0.0341 0.0194 253 CYS B C 5297 O O . CYS B 253 ? 1.0574 0.9420 0.9823 -0.0430 -0.0374 0.0256 253 CYS B O 5298 C CB . CYS B 253 ? 0.9880 0.8856 0.9046 -0.0348 -0.0421 0.0148 253 CYS B CB 5299 S SG . CYS B 253 ? 0.9850 0.8825 0.8851 -0.0392 -0.0319 0.0174 253 CYS B SG 5300 N N . ALA B 254 ? 1.0669 0.9684 0.9983 -0.0416 -0.0254 0.0180 254 ALA B N 5301 C CA . ALA B 254 ? 1.1125 1.0105 1.0446 -0.0474 -0.0188 0.0231 254 ALA B CA 5302 C C . ALA B 254 ? 1.1860 1.0728 1.1019 -0.0527 -0.0168 0.0318 254 ALA B C 5303 O O . ALA B 254 ? 1.1544 1.0409 1.0552 -0.0531 -0.0139 0.0327 254 ALA B O 5304 C CB . ALA B 254 ? 1.0879 0.9952 1.0214 -0.0476 -0.0094 0.0197 254 ALA B CB 5305 N N . GLY B 255 ? 1.2715 1.1487 1.1903 -0.0565 -0.0187 0.0379 255 GLY B N 5306 C CA . GLY B 255 ? 1.3664 1.2319 1.2688 -0.0616 -0.0155 0.0476 255 GLY B CA 5307 C C . GLY B 255 ? 1.4136 1.2697 1.3021 -0.0587 -0.0246 0.0510 255 GLY B C 5308 O O . GLY B 255 ? 1.4403 1.2925 1.3096 -0.0597 -0.0225 0.0549 255 GLY B O 5309 N N . GLY B 256 ? 1.3459 1.1990 1.2443 -0.0546 -0.0351 0.0486 256 GLY B N 5310 C CA . GLY B 256 ? 1.3675 1.2115 1.2557 -0.0510 -0.0452 0.0512 256 GLY B CA 5311 C C . GLY B 256 ? 1.3585 1.2097 1.2366 -0.0470 -0.0477 0.0459 256 GLY B C 5312 O O . GLY B 256 ? 1.3295 1.1918 1.2089 -0.0469 -0.0416 0.0402 256 GLY B O 5313 N N . VAL B 257 ? 1.3852 1.2292 1.2533 -0.0436 -0.0570 0.0477 257 VAL B N 5314 C CA . VAL B 257 ? 1.4274 1.2782 1.2874 -0.0399 -0.0604 0.0420 257 VAL B CA 5315 C C . VAL B 257 ? 1.5900 1.4342 1.4267 -0.0422 -0.0574 0.0479 257 VAL B C 5316 O O . VAL B 257 ? 1.6155 1.4468 1.4392 -0.0417 -0.0623 0.0557 257 VAL B O 5317 C CB . VAL B 257 ? 1.3328 1.1843 1.2003 -0.0334 -0.0734 0.0368 257 VAL B CB 5318 C CG1 . VAL B 257 ? 1.3128 1.1741 1.2019 -0.0310 -0.0743 0.0293 257 VAL B CG1 5319 C CG2 . VAL B 257 ? 1.3354 1.1714 1.1968 -0.0316 -0.0827 0.0442 257 VAL B CG2 5320 N N . PRO B 258 ? 1.6915 1.5440 1.5220 -0.0442 -0.0493 0.0443 258 PRO B N 5321 C CA . PRO B 258 ? 1.7948 1.6427 1.6034 -0.0464 -0.0447 0.0490 258 PRO B CA 5322 C C . PRO B 258 ? 1.7733 1.6112 1.5641 -0.0429 -0.0545 0.0531 258 PRO B C 5323 O O . PRO B 258 ? 1.7305 1.5700 1.5259 -0.0377 -0.0655 0.0481 258 PRO B O 5324 C CB . PRO B 258 ? 1.7702 1.6302 1.5795 -0.0464 -0.0396 0.0401 258 PRO B CB 5325 C CG . PRO B 258 ? 1.7095 1.5787 1.5396 -0.0466 -0.0356 0.0348 258 PRO B CG 5326 C CD . PRO B 258 ? 1.6683 1.5345 1.5117 -0.0439 -0.0440 0.0355 258 PRO B CD 5327 N N . ARG B 268 ? 1.3538 1.2718 1.1498 -0.0634 0.0715 0.0113 298 ARG B N 5328 C CA . ARG B 268 ? 1.3508 1.2729 1.1660 -0.0604 0.0705 0.0079 298 ARG B CA 5329 C C . ARG B 268 ? 1.3044 1.2224 1.1253 -0.0583 0.0606 0.0079 298 ARG B C 5330 O O . ARG B 268 ? 1.1343 1.0475 0.9514 -0.0600 0.0543 0.0129 298 ARG B O 5331 C CB . ARG B 268 ? 1.3321 1.2594 1.1608 -0.0625 0.0747 0.0114 298 ARG B CB 5332 C CG . ARG B 268 ? 1.2858 1.2189 1.1329 -0.0582 0.0742 0.0067 298 ARG B CG 5333 C CD . ARG B 268 ? 1.3234 1.2640 1.1853 -0.0600 0.0789 0.0079 298 ARG B CD 5334 N NE . ARG B 268 ? 1.3311 1.2703 1.2045 -0.0609 0.0724 0.0115 298 ARG B NE 5335 C CZ . ARG B 268 ? 1.3804 1.3154 1.2527 -0.0663 0.0714 0.0184 298 ARG B CZ 5336 N NH1 . ARG B 268 ? 1.3923 1.3237 1.2507 -0.0714 0.0770 0.0236 298 ARG B NH1 5337 N NH2 . ARG B 268 ? 1.3612 1.2948 1.2458 -0.0663 0.0648 0.0201 298 ARG B NH2 5338 N N . MET B 269 ? 1.3190 1.2386 1.1486 -0.0542 0.0596 0.0024 299 MET B N 5339 C CA . MET B 269 ? 1.2878 1.2051 1.1242 -0.0519 0.0518 0.0018 299 MET B CA 5340 C C . MET B 269 ? 1.2552 1.1765 1.1072 -0.0496 0.0506 0.0029 299 MET B C 5341 O O . MET B 269 ? 1.2801 1.2055 1.1401 -0.0460 0.0545 -0.0004 299 MET B O 5342 C CB . MET B 269 ? 1.3245 1.2402 1.1605 -0.0491 0.0519 -0.0043 299 MET B CB 5343 C CG . MET B 269 ? 1.3419 1.2568 1.1871 -0.0465 0.0461 -0.0052 299 MET B CG 5344 S SD . MET B 269 ? 1.3481 1.2601 1.1947 -0.0442 0.0480 -0.0114 299 MET B SD 5345 C CE . MET B 269 ? 1.4841 1.3931 1.3239 -0.0475 0.0407 -0.0132 299 MET B CE 5346 N N . ASP B 270 ? 1.2677 1.1877 1.1238 -0.0510 0.0447 0.0072 300 ASP B N 5347 C CA . ASP B 270 ? 1.2309 1.1543 1.1016 -0.0479 0.0411 0.0068 300 ASP B CA 5348 C C . ASP B 270 ? 1.2176 1.1391 1.0891 -0.0448 0.0351 0.0044 300 ASP B C 5349 O O . ASP B 270 ? 1.2359 1.1534 1.0984 -0.0463 0.0328 0.0039 300 ASP B O 5350 C CB . ASP B 270 ? 1.2770 1.1991 1.1528 -0.0509 0.0374 0.0118 300 ASP B CB 5351 C CG . ASP B 270 ? 1.3799 1.3047 1.2575 -0.0548 0.0445 0.0144 300 ASP B CG 5352 O OD1 . ASP B 270 ? 1.5410 1.4659 1.4084 -0.0569 0.0513 0.0144 300 ASP B OD1 5353 O OD2 . ASP B 270 ? 1.3659 1.2931 1.2558 -0.0559 0.0435 0.0159 300 ASP B OD2 5354 N N . PRO B 271 ? 1.2043 1.1295 1.0869 -0.0403 0.0328 0.0024 301 PRO B N 5355 C CA . PRO B 271 ? 1.1758 1.1001 1.0607 -0.0380 0.0267 0.0011 301 PRO B CA 5356 C C . PRO B 271 ? 1.2411 1.1625 1.1258 -0.0406 0.0191 0.0043 301 PRO B C 5357 O O . PRO B 271 ? 1.2433 1.1639 1.1302 -0.0429 0.0185 0.0078 301 PRO B O 5358 C CB . PRO B 271 ? 1.1589 1.0884 1.0549 -0.0323 0.0261 -0.0009 301 PRO B CB 5359 C CG . PRO B 271 ? 1.1352 1.0681 1.0338 -0.0308 0.0323 -0.0018 301 PRO B CG 5360 C CD . PRO B 271 ? 1.1869 1.1180 1.0803 -0.0367 0.0353 0.0008 301 PRO B CD 5361 N N . PRO B 272 ? 1.2386 1.1584 1.1216 -0.0401 0.0135 0.0031 302 PRO B N 5362 C CA . PRO B 272 ? 1.2196 1.1357 1.1013 -0.0417 0.0055 0.0061 302 PRO B CA 5363 C C . PRO B 272 ? 1.1412 1.0594 1.0352 -0.0392 0.0002 0.0066 302 PRO B C 5364 O O . PRO B 272 ? 1.0599 0.9837 0.9630 -0.0350 0.0007 0.0033 302 PRO B O 5365 C CB . PRO B 272 ? 1.2472 1.1630 1.1259 -0.0411 0.0010 0.0028 302 PRO B CB 5366 C CG . PRO B 272 ? 1.2446 1.1641 1.1262 -0.0393 0.0067 -0.0017 302 PRO B CG 5367 C CD . PRO B 272 ? 1.1935 1.1153 1.0786 -0.0375 0.0136 -0.0011 302 PRO B CD 5368 N N . CYS B 273 ? 1.1575 1.0706 1.0508 -0.0414 -0.0047 0.0110 303 CYS B N 5369 C CA . CYS B 273 ? 1.0675 0.9809 0.9729 -0.0397 -0.0103 0.0115 303 CYS B CA 5370 C C . CYS B 273 ? 1.0363 0.9550 0.9523 -0.0387 -0.0058 0.0100 303 CYS B C 5371 O O . CYS B 273 ? 1.0547 0.9760 0.9829 -0.0359 -0.0104 0.0079 303 CYS B O 5372 C CB . CYS B 273 ? 1.0187 0.9352 0.9311 -0.0349 -0.0181 0.0072 303 CYS B CB 5373 S SG . CYS B 273 ? 1.0882 0.9987 0.9923 -0.0355 -0.0266 0.0085 303 CYS B SG 5374 N N . THR B 274 ? 0.9978 0.9185 0.9097 -0.0406 0.0027 0.0103 304 THR B N 5375 C CA . THR B 274 ? 0.9927 0.9200 0.9150 -0.0389 0.0071 0.0078 304 THR B CA 5376 C C . THR B 274 ? 0.9715 0.8972 0.8939 -0.0447 0.0128 0.0117 304 THR B C 5377 O O . THR B 274 ? 0.9579 0.8804 0.8684 -0.0484 0.0184 0.0147 304 THR B O 5378 C CB . THR B 274 ? 0.9927 0.9252 0.9122 -0.0349 0.0128 0.0037 304 THR B CB 5379 O OG1 . THR B 274 ? 1.0001 0.9322 0.9159 -0.0317 0.0097 0.0016 304 THR B OG1 5380 C CG2 . THR B 274 ? 1.0039 0.9443 0.9353 -0.0299 0.0140 -0.0004 304 THR B CG2 5381 N N . ASN B 275 ? 0.9970 0.9253 0.9334 -0.0454 0.0117 0.0111 305 ASN B N 5382 C CA . ASN B 275 ? 1.0084 0.9377 0.9491 -0.0508 0.0186 0.0137 305 ASN B CA 5383 C C . ASN B 275 ? 0.9775 0.9173 0.9250 -0.0475 0.0246 0.0079 305 ASN B C 5384 O O . ASN B 275 ? 0.9222 0.8690 0.8816 -0.0418 0.0212 0.0021 305 ASN B O 5385 C CB . ASN B 275 ? 1.0539 0.9810 1.0091 -0.0537 0.0143 0.0151 305 ASN B CB 5386 C CG . ASN B 275 ? 1.1175 1.0438 1.0769 -0.0612 0.0222 0.0192 305 ASN B CG 5387 O OD1 . ASN B 275 ? 1.0664 0.9968 1.0205 -0.0633 0.0310 0.0194 305 ASN B OD1 5388 N ND2 . ASN B 275 ? 1.1948 1.1156 1.1648 -0.0654 0.0192 0.0223 305 ASN B ND2 5389 N N . THR B 276 ? 1.0049 0.9457 0.9441 -0.0503 0.0332 0.0091 306 THR B N 5390 C CA . THR B 276 ? 1.0627 1.0128 1.0074 -0.0466 0.0390 0.0036 306 THR B CA 5391 C C . THR B 276 ? 1.1161 1.0719 1.0711 -0.0517 0.0460 0.0037 306 THR B C 5392 O O . THR B 276 ? 1.1546 1.1178 1.1121 -0.0500 0.0524 -0.0002 306 THR B O 5393 C CB . THR B 276 ? 1.0853 1.0339 1.0148 -0.0448 0.0440 0.0029 306 THR B CB 5394 O OG1 . THR B 276 ? 1.0698 1.0147 0.9882 -0.0512 0.0507 0.0072 306 THR B OG1 5395 C CG2 . THR B 276 ? 1.0805 1.0230 1.0004 -0.0418 0.0384 0.0033 306 THR B CG2 5396 N N . THR B 277 ? 1.0795 1.0315 1.0411 -0.0580 0.0450 0.0080 307 THR B N 5397 C CA . THR B 277 ? 1.0700 1.0266 1.0415 -0.0644 0.0530 0.0091 307 THR B CA 5398 C C . THR B 277 ? 1.0497 1.0196 1.0430 -0.0605 0.0528 0.0004 307 THR B C 5399 O O . THR B 277 ? 1.0643 1.0432 1.0626 -0.0609 0.0605 -0.0031 307 THR B O 5400 C CB . THR B 277 ? 1.0756 1.0233 1.0501 -0.0723 0.0520 0.0165 307 THR B CB 5401 O OG1 . THR B 277 ? 1.1230 1.0582 1.0764 -0.0740 0.0499 0.0240 307 THR B OG1 5402 C CG2 . THR B 277 ? 1.0859 1.0372 1.0680 -0.0804 0.0627 0.0191 307 THR B CG2 5403 N N . ALA B 278 ? 0.9832 0.9550 0.9892 -0.0560 0.0437 -0.0038 308 ALA B N 5404 C CA . ALA B 278 ? 0.9947 0.9795 1.0223 -0.0517 0.0418 -0.0129 308 ALA B CA 5405 C C . ALA B 278 ? 1.0124 1.0071 1.0386 -0.0451 0.0463 -0.0189 308 ALA B C 5406 O O . ALA B 278 ? 1.0523 1.0576 1.0924 -0.0462 0.0515 -0.0237 308 ALA B O 5407 C CB . ALA B 278 ? 0.9731 0.9585 1.0088 -0.0449 0.0303 -0.0175 308 ALA B CB 5408 N N . ALA B 279 ? 1.0471 1.0381 1.0570 -0.0386 0.0446 -0.0187 309 ALA B N 5409 C CA . ALA B 279 ? 1.0302 1.0281 1.0375 -0.0310 0.0477 -0.0241 309 ALA B CA 5410 C C . ALA B 279 ? 1.0198 1.0193 1.0212 -0.0357 0.0584 -0.0226 309 ALA B C 5411 O O . ALA B 279 ? 1.0601 1.0697 1.0702 -0.0322 0.0623 -0.0286 309 ALA B O 5412 C CB . ALA B 279 ? 0.9901 0.9815 0.9818 -0.0235 0.0436 -0.0233 309 ALA B CB 5413 N N . SER B 280 ? 1.0233 1.0133 1.0094 -0.0428 0.0625 -0.0152 310 SER B N 5414 C CA . SER B 280 ? 1.0094 1.0003 0.9870 -0.0472 0.0727 -0.0136 310 SER B CA 5415 C C . SER B 280 ? 1.0784 1.0794 1.0728 -0.0531 0.0797 -0.0155 310 SER B C 5416 O O . SER B 280 ? 1.1025 1.1129 1.1019 -0.0515 0.0865 -0.0205 310 SER B O 5417 C CB . SER B 280 ? 1.0065 0.9853 0.9644 -0.0535 0.0745 -0.0053 310 SER B CB 5418 O OG . SER B 280 ? 1.0401 1.0198 0.9866 -0.0557 0.0836 -0.0050 310 SER B OG 5419 N N . THR B 281 ? 1.0783 1.0771 1.0825 -0.0598 0.0780 -0.0117 311 THR B N 5420 C CA . THR B 281 ? 1.0783 1.0865 1.1018 -0.0664 0.0847 -0.0134 311 THR B CA 5421 C C . THR B 281 ? 1.0354 1.0594 1.0784 -0.0594 0.0841 -0.0246 311 THR B C 5422 O O . THR B 281 ? 1.0258 1.0607 1.0786 -0.0619 0.0928 -0.0284 311 THR B O 5423 C CB . THR B 281 ? 1.0747 1.0778 1.1105 -0.0725 0.0801 -0.0096 311 THR B CB 5424 O OG1 . THR B 281 ? 1.1132 1.1009 1.1300 -0.0787 0.0809 0.0012 311 THR B OG1 5425 C CG2 . THR B 281 ? 1.0633 1.0768 1.1230 -0.0798 0.0873 -0.0124 311 THR B CG2 5426 N N . TYR B 282 ? 1.0120 1.0379 1.0599 -0.0500 0.0739 -0.0302 312 TYR B N 5427 C CA . TYR B 282 ? 1.0238 1.0644 1.0898 -0.0419 0.0713 -0.0411 312 TYR B CA 5428 C C . TYR B 282 ? 1.0448 1.0906 1.1029 -0.0359 0.0769 -0.0449 312 TYR B C 5429 O O . TYR B 282 ? 1.1428 1.2017 1.2154 -0.0360 0.0827 -0.0513 312 TYR B O 5430 C CB . TYR B 282 ? 1.0223 1.0628 1.0919 -0.0322 0.0589 -0.0455 312 TYR B CB 5431 C CG . TYR B 282 ? 1.0519 1.1074 1.1379 -0.0225 0.0555 -0.0569 312 TYR B CG 5432 C CD1 . TYR B 282 ? 1.0726 1.1413 1.1856 -0.0244 0.0539 -0.0646 312 TYR B CD1 5433 C CD2 . TYR B 282 ? 1.0768 1.1332 1.1518 -0.0112 0.0539 -0.0601 312 TYR B CD2 5434 C CE1 . TYR B 282 ? 1.1298 1.2134 1.2582 -0.0145 0.0498 -0.0760 312 TYR B CE1 5435 C CE2 . TYR B 282 ? 1.0937 1.1633 1.1822 -0.0010 0.0501 -0.0704 312 TYR B CE2 5436 C CZ . TYR B 282 ? 1.1436 1.2275 1.2587 -0.0023 0.0477 -0.0787 312 TYR B CZ 5437 O OH . TYR B 282 ? 1.1545 1.2526 1.2833 0.0088 0.0428 -0.0899 312 TYR B OH 5438 N N . LEU B 283 ? 1.0439 1.0796 1.0803 -0.0307 0.0753 -0.0416 313 LEU B N 5439 C CA . LEU B 283 ? 1.0078 1.0460 1.0360 -0.0235 0.0792 -0.0456 313 LEU B CA 5440 C C . LEU B 283 ? 1.0190 1.0600 1.0425 -0.0298 0.0910 -0.0447 313 LEU B C 5441 O O . LEU B 283 ? 0.9868 1.0338 1.0104 -0.0240 0.0948 -0.0504 313 LEU B O 5442 C CB . LEU B 283 ? 0.9814 1.0065 0.9887 -0.0174 0.0748 -0.0420 313 LEU B CB 5443 C CG . LEU B 283 ? 0.9656 0.9894 0.9751 -0.0081 0.0644 -0.0442 313 LEU B CG 5444 C CD1 . LEU B 283 ? 0.9472 0.9568 0.9361 -0.0058 0.0617 -0.0385 313 LEU B CD1 5445 C CD2 . LEU B 283 ? 0.9542 0.9885 0.9739 0.0031 0.0621 -0.0530 313 LEU B CD2 5446 N N . ASN B 284 ? 1.0610 1.0974 1.0795 -0.0410 0.0968 -0.0376 314 ASN B N 5447 C CA . ASN B 284 ? 1.0796 1.1198 1.0934 -0.0472 0.1088 -0.0365 314 ASN B CA 5448 C C . ASN B 284 ? 1.1229 1.1793 1.1604 -0.0518 0.1159 -0.0418 314 ASN B C 5449 O O . ASN B 284 ? 1.1223 1.1855 1.1589 -0.0555 0.1266 -0.0430 314 ASN B O 5450 C CB . ASN B 284 ? 1.0861 1.1136 1.0808 -0.0564 0.1122 -0.0260 314 ASN B CB 5451 C CG . ASN B 284 ? 1.0883 1.1026 1.0596 -0.0523 0.1080 -0.0228 314 ASN B CG 5452 O OD1 . ASN B 284 ? 1.1124 1.1270 1.0742 -0.0478 0.1113 -0.0264 314 ASN B OD1 5453 N ND2 . ASN B 284 ? 1.0556 1.0584 1.0188 -0.0538 0.1004 -0.0167 314 ASN B ND2 5454 N N . ASN B 285 ? 1.1302 1.1935 1.1895 -0.0516 0.1101 -0.0455 315 ASN B N 5455 C CA . ASN B 285 ? 1.1649 1.2459 1.2516 -0.0543 0.1153 -0.0531 315 ASN B CA 5456 C C . ASN B 285 ? 1.1447 1.2386 1.2361 -0.0460 0.1191 -0.0628 315 ASN B C 5457 O O . ASN B 285 ? 1.1592 1.2543 1.2502 -0.0342 0.1109 -0.0688 315 ASN B O 5458 C CB . ASN B 285 ? 1.1392 1.2262 1.2487 -0.0515 0.1051 -0.0587 315 ASN B CB 5459 C CG . ASN B 285 ? 1.1534 1.2602 1.2945 -0.0542 0.1096 -0.0684 315 ASN B CG 5460 O OD1 . ASN B 285 ? 1.1869 1.3044 1.3336 -0.0570 0.1203 -0.0716 315 ASN B OD1 5461 N ND2 . ASN B 285 ? 1.0862 1.1990 1.2492 -0.0530 0.1011 -0.0740 315 ASN B ND2 5462 N N . PRO B 286 ? 1.1606 1.2638 1.2560 -0.0519 0.1318 -0.0643 316 PRO B N 5463 C CA . PRO B 286 ? 1.1289 1.2442 1.2282 -0.0437 0.1357 -0.0739 316 PRO B CA 5464 C C . PRO B 286 ? 1.0931 1.2225 1.2156 -0.0328 0.1274 -0.0862 316 PRO B C 5465 O O . PRO B 286 ? 1.0770 1.2095 1.1962 -0.0213 0.1246 -0.0929 316 PRO B O 5466 C CB . PRO B 286 ? 1.1827 1.3097 1.2907 -0.0539 0.1510 -0.0743 316 PRO B CB 5467 C CG . PRO B 286 ? 1.1880 1.3020 1.2828 -0.0665 0.1558 -0.0613 316 PRO B CG 5468 C CD . PRO B 286 ? 1.1753 1.2783 1.2717 -0.0660 0.1434 -0.0570 316 PRO B CD 5469 N N . TYR B 287 ? 1.1259 1.2633 1.2715 -0.0359 0.1230 -0.0893 317 TYR B N 5470 C CA . TYR B 287 ? 1.1575 1.3091 1.3257 -0.0251 0.1137 -0.1017 317 TYR B CA 5471 C C . TYR B 287 ? 1.1559 1.2963 1.3094 -0.0122 0.0997 -0.1012 317 TYR B C 5472 O O . TYR B 287 ? 1.2952 1.4432 1.4546 0.0009 0.0929 -0.1103 317 TYR B O 5473 C CB . TYR B 287 ? 1.1694 1.3333 1.3681 -0.0328 0.1129 -0.1062 317 TYR B CB 5474 C CG . TYR B 287 ? 1.1775 1.3541 1.3931 -0.0455 0.1280 -0.1072 317 TYR B CG 5475 C CD1 . TYR B 287 ? 1.1616 1.3583 1.3952 -0.0418 0.1343 -0.1185 317 TYR B CD1 5476 C CD2 . TYR B 287 ? 1.1932 1.3611 1.4059 -0.0608 0.1364 -0.0963 317 TYR B CD2 5477 C CE1 . TYR B 287 ? 1.1635 1.3727 1.4126 -0.0536 0.1493 -0.1194 317 TYR B CE1 5478 C CE2 . TYR B 287 ? 1.2058 1.3845 1.4323 -0.0725 0.1515 -0.0961 317 TYR B CE2 5479 C CZ . TYR B 287 ? 1.2069 1.4068 1.4519 -0.0692 0.1583 -0.1078 317 TYR B CZ 5480 O OH . TYR B 287 ? 1.2797 1.4913 1.5388 -0.0813 0.1744 -0.1077 317 TYR B OH 5481 N N . VAL B 288 ? 1.0900 1.2122 1.2239 -0.0156 0.0959 -0.0907 318 VAL B N 5482 C CA . VAL B 288 ? 1.0659 1.1765 1.1835 -0.0045 0.0847 -0.0890 318 VAL B CA 5483 C C . VAL B 288 ? 1.0662 1.1701 1.1640 0.0040 0.0868 -0.0887 318 VAL B C 5484 O O . VAL B 288 ? 1.0727 1.1763 1.1676 0.0172 0.0792 -0.0933 318 VAL B O 5485 C CB . VAL B 288 ? 1.0420 1.1356 1.1439 -0.0108 0.0810 -0.0781 318 VAL B CB 5486 C CG1 . VAL B 288 ? 1.0282 1.1095 1.1107 -0.0002 0.0723 -0.0755 318 VAL B CG1 5487 C CG2 . VAL B 288 ? 1.0627 1.1614 1.1849 -0.0164 0.0761 -0.0796 318 VAL B CG2 5488 N N . ARG B 289 ? 1.0413 1.1393 1.1253 -0.0031 0.0969 -0.0834 319 ARG B N 5489 C CA . ARG B 289 ? 0.9981 1.0899 1.0652 0.0039 0.0999 -0.0841 319 ARG B CA 5490 C C . ARG B 289 ? 1.0040 1.1104 1.0862 0.0150 0.0992 -0.0959 319 ARG B C 5491 O O . ARG B 289 ? 0.9808 1.0815 1.0536 0.0270 0.0944 -0.0983 319 ARG B O 5492 C CB . ARG B 289 ? 0.9915 1.0786 1.0453 -0.0061 0.1114 -0.0787 319 ARG B CB 5493 C CG . ARG B 289 ? 0.9610 1.0304 0.9935 -0.0138 0.1107 -0.0672 319 ARG B CG 5494 C CD . ARG B 289 ? 0.9512 1.0174 0.9703 -0.0231 0.1216 -0.0626 319 ARG B CD 5495 N NE . ARG B 289 ? 0.9461 1.0102 0.9533 -0.0172 0.1257 -0.0665 319 ARG B NE 5496 C CZ . ARG B 289 ? 0.9511 1.0017 0.9357 -0.0185 0.1273 -0.0620 319 ARG B CZ 5497 N NH1 . ARG B 289 ? 0.9480 0.9863 0.9182 -0.0253 0.1251 -0.0530 319 ARG B NH1 5498 N NH2 . ARG B 289 ? 0.9264 0.9762 0.9036 -0.0127 0.1308 -0.0673 319 ARG B NH2 5499 N N . LYS B 290 ? 1.0468 1.1721 1.1533 0.0110 0.1039 -0.1033 320 LYS B N 5500 C CA . LYS B 290 ? 1.1097 1.2524 1.2354 0.0213 0.1026 -0.1161 320 LYS B CA 5501 C C . LYS B 290 ? 1.1180 1.2620 1.2494 0.0354 0.0886 -0.1215 320 LYS B C 5502 O O . LYS B 290 ? 1.1232 1.2687 1.2524 0.0491 0.0844 -0.1276 320 LYS B O 5503 C CB . LYS B 290 ? 1.1368 1.3002 1.2910 0.0124 0.1096 -0.1226 320 LYS B CB 5504 C CG . LYS B 290 ? 1.1808 1.3652 1.3564 0.0199 0.1124 -0.1365 320 LYS B CG 5505 C CD . LYS B 290 ? 1.1936 1.3985 1.4029 0.0205 0.1075 -0.1471 320 LYS B CD 5506 C CE . LYS B 290 ? 1.2037 1.4102 1.4255 0.0045 0.1116 -0.1418 320 LYS B CE 5507 N NZ . LYS B 290 ? 1.1468 1.3705 1.4010 0.0056 0.1044 -0.1521 320 LYS B NZ 5508 N N . ALA B 291 ? 1.0418 1.1853 1.1801 0.0324 0.0815 -0.1194 321 ALA B N 5509 C CA . ALA B 291 ? 1.0563 1.2021 1.1996 0.0453 0.0680 -0.1247 321 ALA B CA 5510 C C . ALA B 291 ? 1.0551 1.1828 1.1714 0.0566 0.0622 -0.1189 321 ALA B C 5511 O O . ALA B 291 ? 1.0647 1.1943 1.1810 0.0713 0.0528 -0.1242 321 ALA B O 5512 C CB . ALA B 291 ? 1.0366 1.1830 1.1899 0.0385 0.0624 -0.1227 321 ALA B CB 5513 N N . LEU B 292 ? 1.0441 1.1543 1.1378 0.0494 0.0680 -0.1080 322 LEU B N 5514 C CA . LEU B 292 ? 1.0124 1.1037 1.0805 0.0568 0.0648 -0.1011 322 LEU B CA 5515 C C . LEU B 292 ? 1.0183 1.1039 1.0753 0.0608 0.0712 -0.1018 322 LEU B C 5516 O O . LEU B 292 ? 1.1102 1.1781 1.1455 0.0628 0.0719 -0.0949 322 LEU B O 5517 C CB . LEU B 292 ? 1.0177 1.0936 1.0697 0.0460 0.0664 -0.0896 322 LEU B CB 5518 C CG . LEU B 292 ? 1.0180 1.0955 1.0773 0.0422 0.0595 -0.0877 322 LEU B CG 5519 C CD1 . LEU B 292 ? 1.0202 1.0839 1.0651 0.0303 0.0626 -0.0770 322 LEU B CD1 5520 C CD2 . LEU B 292 ? 1.0530 1.1280 1.1078 0.0560 0.0485 -0.0896 322 LEU B CD2 5521 N N . ASN B 293 ? 1.0199 1.1207 1.0927 0.0618 0.0762 -0.1106 323 ASN B N 5522 C CA . ASN B 293 ? 0.9938 1.0915 1.0592 0.0683 0.0810 -0.1139 323 ASN B CA 5523 C C . ASN B 293 ? 0.9867 1.0673 1.0300 0.0602 0.0885 -0.1052 323 ASN B C 5524 O O . ASN B 293 ? 1.0133 1.0806 1.0412 0.0674 0.0885 -0.1038 323 ASN B O 5525 C CB . ASN B 293 ? 0.9567 1.0489 1.0163 0.0863 0.0719 -0.1171 323 ASN B CB 5526 C CG . ASN B 293 ? 0.9602 1.0684 1.0392 0.0954 0.0624 -0.1256 323 ASN B CG 5527 O OD1 . ASN B 293 ? 0.9705 1.0992 1.0734 0.0937 0.0641 -0.1352 323 ASN B OD1 5528 N ND2 . ASN B 293 ? 0.9816 1.0815 1.0510 0.1053 0.0524 -0.1227 323 ASN B ND2 5529 N N . ILE B 294 ? 0.9752 1.0556 1.0170 0.0456 0.0945 -0.0995 324 ILE B N 5530 C CA . ILE B 294 ? 1.0080 1.0741 1.0298 0.0377 0.1010 -0.0922 324 ILE B CA 5531 C C . ILE B 294 ? 1.0760 1.1518 1.1021 0.0337 0.1115 -0.0977 324 ILE B C 5532 O O . ILE B 294 ? 1.1247 1.2172 1.1680 0.0278 0.1166 -0.1018 324 ILE B O 5533 C CB . ILE B 294 ? 0.9995 1.0595 1.0149 0.0247 0.1016 -0.0829 324 ILE B CB 5534 C CG1 . ILE B 294 ? 0.9796 1.0332 0.9939 0.0281 0.0914 -0.0787 324 ILE B CG1 5535 C CG2 . ILE B 294 ? 1.0222 1.0674 1.0159 0.0183 0.1067 -0.0763 324 ILE B CG2 5536 C CD1 . ILE B 294 ? 1.0009 1.0381 0.9978 0.0370 0.0862 -0.0751 324 ILE B CD1 5537 N N . PRO B 295 ? 1.1403 1.2061 1.1516 0.0370 0.1151 -0.0982 325 PRO B N 5538 C CA . PRO B 295 ? 1.1853 1.2601 1.1985 0.0328 0.1256 -0.1034 325 PRO B CA 5539 C C . PRO B 295 ? 1.1740 1.2504 1.1819 0.0176 0.1334 -0.0971 325 PRO B C 5540 O O . PRO B 295 ? 1.2067 1.2696 1.1999 0.0113 0.1309 -0.0880 325 PRO B O 5541 C CB . PRO B 295 ? 1.2041 1.2636 1.1997 0.0392 0.1260 -0.1042 325 PRO B CB 5542 C CG . PRO B 295 ? 1.1981 1.2455 1.1899 0.0503 0.1160 -0.1024 325 PRO B CG 5543 C CD . PRO B 295 ? 1.1774 1.2243 1.1717 0.0454 0.1101 -0.0954 325 PRO B CD 5544 N N . GLU B 296 ? 1.1940 1.2869 1.2137 0.0122 0.1428 -0.1020 326 GLU B N 5545 C CA . GLU B 296 ? 1.2016 1.2977 1.2181 -0.0017 0.1511 -0.0957 326 GLU B CA 5546 C C . GLU B 296 ? 1.2434 1.3245 1.2337 -0.0074 0.1546 -0.0889 326 GLU B C 5547 O O . GLU B 296 ? 1.3170 1.3907 1.2975 -0.0167 0.1548 -0.0796 326 GLU B O 5548 C CB . GLU B 296 ? 1.2264 1.3437 1.2602 -0.0055 0.1623 -0.1030 326 GLU B CB 5549 C CG . GLU B 296 ? 1.1986 1.3215 1.2349 -0.0201 0.1710 -0.0961 326 GLU B CG 5550 C CD . GLU B 296 ? 1.1964 1.3407 1.2502 -0.0242 0.1837 -0.1033 326 GLU B CD 5551 O OE1 . GLU B 296 ? 1.2117 1.3619 1.2618 -0.0192 0.1898 -0.1107 326 GLU B OE1 5552 O OE2 . GLU B 296 ? 1.2021 1.3574 1.2739 -0.0326 0.1880 -0.1019 326 GLU B OE2 5553 N N . GLN B 297 ? 1.2904 1.3670 1.2697 -0.0015 0.1569 -0.0940 327 GLN B N 5554 C CA . GLN B 297 ? 1.3373 1.4030 1.2934 -0.0067 0.1613 -0.0901 327 GLN B CA 5555 C C . GLN B 297 ? 1.2654 1.3119 1.2045 -0.0095 0.1534 -0.0808 327 GLN B C 5556 O O . GLN B 297 ? 1.2886 1.3272 1.2095 -0.0152 0.1561 -0.0768 327 GLN B O 5557 C CB . GLN B 297 ? 1.4060 1.4706 1.3558 0.0011 0.1644 -0.0992 327 GLN B CB 5558 C CG . GLN B 297 ? 1.4472 1.4966 1.3922 0.0116 0.1553 -0.1012 327 GLN B CG 5559 C CD . GLN B 297 ? 1.4899 1.5458 1.4532 0.0227 0.1502 -0.1074 327 GLN B CD 5560 O OE1 . GLN B 297 ? 1.4661 1.5384 1.4482 0.0224 0.1515 -0.1102 327 GLN B OE1 5561 N NE2 . GLN B 297 ? 1.4904 1.5329 1.4485 0.0328 0.1440 -0.1096 327 GLN B NE2 5562 N N . LEU B 298 ? 1.1560 1.1960 1.1008 -0.0051 0.1438 -0.0781 328 LEU B N 5563 C CA . LEU B 298 ? 1.1401 1.1631 1.0707 -0.0070 0.1365 -0.0702 328 LEU B CA 5564 C C . LEU B 298 ? 1.1039 1.1254 1.0288 -0.0182 0.1371 -0.0612 328 LEU B C 5565 O O . LEU B 298 ? 1.0706 1.1028 1.0077 -0.0233 0.1401 -0.0596 328 LEU B O 5566 C CB . LEU B 298 ? 1.1634 1.1815 1.1018 0.0008 0.1270 -0.0697 328 LEU B CB 5567 C CG . LEU B 298 ? 1.1627 1.1764 1.1024 0.0129 0.1244 -0.0761 328 LEU B CG 5568 C CD1 . LEU B 298 ? 1.1426 1.1534 1.0897 0.0206 0.1155 -0.0745 328 LEU B CD1 5569 C CD2 . LEU B 298 ? 1.1526 1.1504 1.0746 0.0136 0.1248 -0.0756 328 LEU B CD2 5570 N N . PRO B 299 ? 1.0566 1.0642 0.9636 -0.0218 0.1338 -0.0555 329 PRO B N 5571 C CA . PRO B 299 ? 1.0706 1.0749 0.9696 -0.0313 0.1337 -0.0468 329 PRO B CA 5572 C C . PRO B 299 ? 1.1003 1.1053 1.0116 -0.0330 0.1273 -0.0418 329 PRO B C 5573 O O . PRO B 299 ? 1.1790 1.1862 1.1028 -0.0262 0.1221 -0.0450 329 PRO B O 5574 C CB . PRO B 299 ? 1.0638 1.0532 0.9435 -0.0319 0.1292 -0.0441 329 PRO B CB 5575 C CG . PRO B 299 ? 1.0629 1.0460 0.9445 -0.0231 0.1251 -0.0495 329 PRO B CG 5576 C CD . PRO B 299 ? 1.0715 1.0656 0.9662 -0.0168 0.1298 -0.0572 329 PRO B CD 5577 N N . GLN B 300 ? 1.0784 1.0810 0.9853 -0.0414 0.1274 -0.0341 330 GLN B N 5578 C CA . GLN B 300 ? 1.0575 1.0605 0.9766 -0.0435 0.1215 -0.0297 330 GLN B CA 5579 C C . GLN B 300 ? 1.0221 1.0160 0.9399 -0.0376 0.1111 -0.0292 330 GLN B C 5580 O O . GLN B 300 ? 0.9631 0.9476 0.8674 -0.0348 0.1088 -0.0294 330 GLN B O 5581 C CB . GLN B 300 ? 1.0863 1.0850 0.9982 -0.0533 0.1231 -0.0208 330 GLN B CB 5582 C CG . GLN B 300 ? 1.0811 1.0658 0.9720 -0.0553 0.1182 -0.0150 330 GLN B CG 5583 C CD . GLN B 300 ? 1.0882 1.0669 0.9754 -0.0627 0.1159 -0.0057 330 GLN B CD 5584 O OE1 . GLN B 300 ? 1.0639 1.0478 0.9587 -0.0686 0.1216 -0.0024 330 GLN B OE1 5585 N NE2 . GLN B 300 ? 1.1212 1.0886 0.9974 -0.0624 0.1075 -0.0016 330 GLN B NE2 5586 N N . TRP B 301 ? 1.0384 1.0356 0.9708 -0.0356 0.1052 -0.0289 331 TRP B N 5587 C CA . TRP B 301 ? 1.0565 1.0460 0.9875 -0.0303 0.0959 -0.0278 331 TRP B CA 5588 C C . TRP B 301 ? 1.1187 1.0986 1.0402 -0.0364 0.0912 -0.0202 331 TRP B C 5589 O O . TRP B 301 ? 1.1700 1.1513 1.0951 -0.0433 0.0920 -0.0158 331 TRP B O 5590 C CB . TRP B 301 ? 1.0491 1.0470 0.9988 -0.0248 0.0909 -0.0315 331 TRP B CB 5591 C CG . TRP B 301 ? 1.0573 1.0487 1.0050 -0.0180 0.0821 -0.0309 331 TRP B CG 5592 C CD1 . TRP B 301 ? 1.0477 1.0366 0.9930 -0.0083 0.0798 -0.0344 331 TRP B CD1 5593 C CD2 . TRP B 301 ? 1.0720 1.0584 1.0198 -0.0200 0.0749 -0.0264 331 TRP B CD2 5594 N NE1 . TRP B 301 ? 0.9910 0.9741 0.9339 -0.0046 0.0725 -0.0319 331 TRP B NE1 5595 C CE2 . TRP B 301 ? 1.0428 1.0251 0.9879 -0.0115 0.0692 -0.0276 331 TRP B CE2 5596 C CE3 . TRP B 301 ? 1.0945 1.0790 1.0441 -0.0279 0.0729 -0.0213 331 TRP B CE3 5597 C CZ2 . TRP B 301 ? 1.0366 1.0147 0.9813 -0.0106 0.0618 -0.0247 331 TRP B CZ2 5598 C CZ3 . TRP B 301 ? 1.0759 1.0554 1.0256 -0.0267 0.0646 -0.0187 331 TRP B CZ3 5599 C CH2 . TRP B 301 ? 1.0336 1.0108 0.9812 -0.0182 0.0593 -0.0208 331 TRP B CH2 5600 N N . ASP B 302 ? 1.0660 1.0359 0.9762 -0.0336 0.0864 -0.0189 332 ASP B N 5601 C CA . ASP B 302 ? 1.0151 0.9765 0.9181 -0.0370 0.0801 -0.0133 332 ASP B CA 5602 C C . ASP B 302 ? 1.0316 0.9895 0.9376 -0.0303 0.0731 -0.0145 332 ASP B C 5603 O O . ASP B 302 ? 1.0150 0.9717 0.9196 -0.0240 0.0742 -0.0181 332 ASP B O 5604 C CB . ASP B 302 ? 1.0157 0.9687 0.9007 -0.0405 0.0817 -0.0114 332 ASP B CB 5605 C CG . ASP B 302 ? 1.0662 1.0215 0.9439 -0.0466 0.0886 -0.0096 332 ASP B CG 5606 O OD1 . ASP B 302 ? 1.0616 1.0217 0.9463 -0.0510 0.0910 -0.0064 332 ASP B OD1 5607 O OD2 . ASP B 302 ? 1.1425 1.0943 1.0069 -0.0471 0.0919 -0.0113 332 ASP B OD2 5608 N N . MET B 303 ? 1.0529 1.0086 0.9621 -0.0315 0.0663 -0.0111 333 MET B N 5609 C CA . MET B 303 ? 1.0456 0.9988 0.9566 -0.0253 0.0603 -0.0120 333 MET B CA 5610 C C . MET B 303 ? 1.0171 0.9619 0.9159 -0.0240 0.0612 -0.0121 333 MET B C 5611 O O . MET B 303 ? 0.9616 0.9045 0.8607 -0.0176 0.0607 -0.0140 333 MET B O 5612 C CB . MET B 303 ? 1.1184 1.0707 1.0342 -0.0271 0.0529 -0.0090 333 MET B CB 5613 C CG . MET B 303 ? 1.1378 1.0905 1.0577 -0.0198 0.0474 -0.0109 333 MET B CG 5614 S SD . MET B 303 ? 1.3327 1.2815 1.2526 -0.0221 0.0392 -0.0076 333 MET B SD 5615 C CE . MET B 303 ? 1.3893 1.3448 1.3250 -0.0237 0.0352 -0.0082 333 MET B CE 5616 N N . CYS B 304 ? 1.0344 0.9739 0.9224 -0.0299 0.0627 -0.0102 334 CYS B N 5617 C CA . CYS B 304 ? 1.0446 0.9770 0.9228 -0.0293 0.0643 -0.0119 334 CYS B CA 5618 C C . CYS B 304 ? 1.0476 0.9789 0.9166 -0.0329 0.0699 -0.0136 334 CYS B C 5619 O O . CYS B 304 ? 1.0876 1.0221 0.9543 -0.0373 0.0720 -0.0116 334 CYS B O 5620 C CB . CYS B 304 ? 1.0414 0.9682 0.9154 -0.0315 0.0586 -0.0098 334 CYS B CB 5621 S SG . CYS B 304 ? 1.0922 1.0218 0.9763 -0.0282 0.0515 -0.0077 334 CYS B SG 5622 N N . ASN B 305 ? 1.0210 0.9471 0.8844 -0.0308 0.0726 -0.0172 335 ASN B N 5623 C CA . ASN B 305 ? 1.0155 0.9398 0.8694 -0.0334 0.0772 -0.0203 335 ASN B CA 5624 C C . ASN B 305 ? 1.0864 1.0038 0.9314 -0.0368 0.0737 -0.0209 335 ASN B C 5625 O O . ASN B 305 ? 1.0418 0.9536 0.8882 -0.0350 0.0723 -0.0228 335 ASN B O 5626 C CB . ASN B 305 ? 1.0556 0.9789 0.9115 -0.0281 0.0824 -0.0254 335 ASN B CB 5627 C CG . ASN B 305 ? 1.0828 1.0072 0.9309 -0.0297 0.0880 -0.0298 335 ASN B CG 5628 O OD1 . ASN B 305 ? 1.1298 1.0517 0.9676 -0.0343 0.0874 -0.0302 335 ASN B OD1 5629 N ND2 . ASN B 305 ? 1.0763 1.0047 0.9291 -0.0252 0.0932 -0.0337 335 ASN B ND2 5630 N N . PHE B 306 ? 1.2024 1.1204 1.0383 -0.0417 0.0723 -0.0191 336 PHE B N 5631 C CA . PHE B 306 ? 1.2491 1.1621 1.0759 -0.0445 0.0682 -0.0209 336 PHE B CA 5632 C C . PHE B 306 ? 1.1744 1.0831 0.9977 -0.0431 0.0714 -0.0281 336 PHE B C 5633 O O . PHE B 306 ? 1.1087 1.0126 0.9325 -0.0438 0.0680 -0.0310 336 PHE B O 5634 C CB . PHE B 306 ? 1.3975 1.3116 1.2122 -0.0487 0.0667 -0.0177 336 PHE B CB 5635 C CG . PHE B 306 ? 1.5670 1.4857 1.3759 -0.0496 0.0743 -0.0176 336 PHE B CG 5636 C CD1 . PHE B 306 ? 1.6852 1.6092 1.5009 -0.0504 0.0776 -0.0128 336 PHE B CD1 5637 C CD2 . PHE B 306 ? 1.6597 1.5781 1.4572 -0.0497 0.0782 -0.0228 336 PHE B CD2 5638 C CE1 . PHE B 306 ? 1.7472 1.6765 1.5590 -0.0518 0.0855 -0.0129 336 PHE B CE1 5639 C CE2 . PHE B 306 ? 1.7601 1.6838 1.5521 -0.0504 0.0859 -0.0230 336 PHE B CE2 5640 C CZ . PHE B 306 ? 1.7765 1.7060 1.5760 -0.0517 0.0900 -0.0178 336 PHE B CZ 5641 N N . LEU B 307 ? 1.1134 1.0241 0.9346 -0.0413 0.0781 -0.0315 337 LEU B N 5642 C CA . LEU B 307 ? 1.1850 1.0909 1.0036 -0.0396 0.0811 -0.0391 337 LEU B CA 5643 C C . LEU B 307 ? 1.1683 1.0675 0.9963 -0.0369 0.0802 -0.0401 337 LEU B C 5644 O O . LEU B 307 ? 1.1649 1.0582 0.9925 -0.0386 0.0777 -0.0435 337 LEU B O 5645 C CB . LEU B 307 ? 1.2173 1.1270 1.0351 -0.0366 0.0885 -0.0429 337 LEU B CB 5646 C CG . LEU B 307 ? 1.2608 1.1777 1.0688 -0.0391 0.0921 -0.0424 337 LEU B CG 5647 C CD1 . LEU B 307 ? 1.2719 1.1943 1.0835 -0.0355 0.0999 -0.0465 337 LEU B CD1 5648 C CD2 . LEU B 307 ? 1.2379 1.1524 1.0314 -0.0420 0.0899 -0.0461 337 LEU B CD2 5649 N N . VAL B 308 ? 1.0996 0.9999 0.9361 -0.0325 0.0822 -0.0371 338 VAL B N 5650 C CA . VAL B 308 ? 1.0429 0.9364 0.8865 -0.0291 0.0822 -0.0365 338 VAL B CA 5651 C C . VAL B 308 ? 0.9794 0.8698 0.8244 -0.0329 0.0772 -0.0349 338 VAL B C 5652 O O . VAL B 308 ? 0.9724 0.8555 0.8187 -0.0339 0.0778 -0.0382 338 VAL B O 5653 C CB . VAL B 308 ? 1.0465 0.9438 0.8976 -0.0237 0.0827 -0.0321 338 VAL B CB 5654 C CG1 . VAL B 308 ? 1.0762 0.9662 0.9319 -0.0201 0.0823 -0.0300 338 VAL B CG1 5655 C CG2 . VAL B 308 ? 1.0635 0.9643 0.9160 -0.0189 0.0876 -0.0350 338 VAL B CG2 5656 N N . ASN B 309 ? 0.9612 0.8572 0.8068 -0.0351 0.0722 -0.0304 339 ASN B N 5657 C CA . ASN B 309 ? 0.9880 0.8827 0.8363 -0.0379 0.0669 -0.0291 339 ASN B CA 5658 C C . ASN B 309 ? 1.0161 0.9076 0.8600 -0.0423 0.0648 -0.0347 339 ASN B C 5659 O O . ASN B 309 ? 1.0249 0.9119 0.8741 -0.0435 0.0646 -0.0373 339 ASN B O 5660 C CB . ASN B 309 ? 0.9743 0.8752 0.8233 -0.0392 0.0613 -0.0241 339 ASN B CB 5661 C CG . ASN B 309 ? 0.9587 0.8595 0.8127 -0.0407 0.0558 -0.0231 339 ASN B CG 5662 O OD1 . ASN B 309 ? 0.9327 0.8333 0.7838 -0.0443 0.0514 -0.0254 339 ASN B OD1 5663 N ND2 . ASN B 309 ? 0.9199 0.8216 0.7815 -0.0373 0.0557 -0.0201 339 ASN B ND2 5664 N N . LEU B 310 ? 1.0496 0.9437 0.8841 -0.0445 0.0636 -0.0368 340 LEU B N 5665 C CA . LEU B 310 ? 1.1004 0.9926 0.9295 -0.0477 0.0606 -0.0432 340 LEU B CA 5666 C C . LEU B 310 ? 1.1182 1.0037 0.9499 -0.0473 0.0650 -0.0506 340 LEU B C 5667 O O . LEU B 310 ? 1.1065 0.9893 0.9409 -0.0501 0.0622 -0.0563 340 LEU B O 5668 C CB . LEU B 310 ? 1.1715 1.0675 0.9870 -0.0490 0.0591 -0.0435 340 LEU B CB 5669 C CG . LEU B 310 ? 1.1777 1.0778 0.9892 -0.0503 0.0535 -0.0365 340 LEU B CG 5670 C CD1 . LEU B 310 ? 1.2239 1.1265 1.0203 -0.0513 0.0543 -0.0355 340 LEU B CD1 5671 C CD2 . LEU B 310 ? 1.1594 1.0592 0.9743 -0.0521 0.0452 -0.0376 340 LEU B CD2 5672 N N . GLN B 311 ? 1.1096 0.9925 0.9419 -0.0438 0.0715 -0.0510 341 GLN B N 5673 C CA . GLN B 311 ? 1.1512 1.0261 0.9864 -0.0429 0.0759 -0.0578 341 GLN B CA 5674 C C . GLN B 311 ? 1.1734 1.0403 1.0193 -0.0414 0.0788 -0.0555 341 GLN B C 5675 O O . GLN B 311 ? 1.2612 1.1194 1.1102 -0.0401 0.0832 -0.0598 341 GLN B O 5676 C CB . GLN B 311 ? 1.1622 1.0376 0.9926 -0.0389 0.0814 -0.0602 341 GLN B CB 5677 C CG . GLN B 311 ? 1.1618 1.0436 0.9803 -0.0403 0.0806 -0.0639 341 GLN B CG 5678 C CD . GLN B 311 ? 1.1300 1.0135 0.9456 -0.0363 0.0870 -0.0670 341 GLN B CD 5679 O OE1 . GLN B 311 ? 1.0863 0.9743 0.9046 -0.0334 0.0901 -0.0620 341 GLN B OE1 5680 N NE2 . GLN B 311 ? 1.1557 1.0360 0.9673 -0.0357 0.0888 -0.0761 341 GLN B NE2 5681 N N . TYR B 312 ? 1.1608 1.0301 1.0117 -0.0412 0.0768 -0.0488 342 TYR B N 5682 C CA . TYR B 312 ? 1.1290 0.9915 0.9876 -0.0387 0.0805 -0.0450 342 TYR B CA 5683 C C . TYR B 312 ? 1.1227 0.9798 0.9887 -0.0434 0.0804 -0.0480 342 TYR B C 5684 O O . TYR B 312 ? 1.1121 0.9748 0.9802 -0.0478 0.0751 -0.0496 342 TYR B O 5685 C CB . TYR B 312 ? 1.0493 0.9178 0.9097 -0.0357 0.0786 -0.0371 342 TYR B CB 5686 C CG . TYR B 312 ? 0.9803 0.8424 0.8448 -0.0308 0.0831 -0.0325 342 TYR B CG 5687 C CD1 . TYR B 312 ? 0.9604 0.8179 0.8308 -0.0327 0.0845 -0.0307 342 TYR B CD1 5688 C CD2 . TYR B 312 ? 0.9755 0.8366 0.8378 -0.0239 0.0861 -0.0299 342 TYR B CD2 5689 C CE1 . TYR B 312 ? 0.9583 0.8092 0.8299 -0.0277 0.0892 -0.0255 342 TYR B CE1 5690 C CE2 . TYR B 312 ? 0.9825 0.8373 0.8464 -0.0181 0.0895 -0.0253 342 TYR B CE2 5691 C CZ . TYR B 312 ? 0.9740 0.8231 0.8414 -0.0199 0.0914 -0.0226 342 TYR B CZ 5692 O OH . TYR B 312 ? 0.9637 0.8058 0.8302 -0.0137 0.0954 -0.0171 342 TYR B OH 5693 N N . ARG B 313 ? 1.1847 1.0306 1.0553 -0.0423 0.0864 -0.0487 343 ARG B N 5694 C CA . ARG B 313 ? 1.2457 1.0851 1.1255 -0.0474 0.0882 -0.0519 343 ARG B CA 5695 C C . ARG B 313 ? 1.2348 1.0707 1.1199 -0.0459 0.0922 -0.0442 343 ARG B C 5696 O O . ARG B 313 ? 1.2445 1.0718 1.1275 -0.0406 0.0978 -0.0391 343 ARG B O 5697 C CB . ARG B 313 ? 1.3649 1.1925 1.2464 -0.0480 0.0928 -0.0585 343 ARG B CB 5698 C CG . ARG B 313 ? 1.5015 1.3237 1.3936 -0.0550 0.0934 -0.0654 343 ARG B CG 5699 C CD . ARG B 313 ? 1.5873 1.4171 1.4784 -0.0593 0.0866 -0.0757 343 ARG B CD 5700 N NE . ARG B 313 ? 1.6588 1.4817 1.5608 -0.0650 0.0876 -0.0851 343 ARG B NE 5701 C CZ . ARG B 313 ? 1.7223 1.5336 1.6265 -0.0647 0.0919 -0.0911 343 ARG B CZ 5702 N NH1 . ARG B 313 ? 1.6935 1.4988 1.5893 -0.0584 0.0956 -0.0885 343 ARG B NH1 5703 N NH2 . ARG B 313 ? 1.7620 1.5679 1.6784 -0.0707 0.0922 -0.1003 343 ARG B NH2 5704 N N . ARG B 314 ? 1.2473 1.0900 1.1385 -0.0498 0.0891 -0.0434 344 ARG B N 5705 C CA . ARG B 314 ? 1.2123 1.0542 1.1081 -0.0485 0.0927 -0.0364 344 ARG B CA 5706 C C . ARG B 314 ? 1.1752 1.0067 1.0805 -0.0532 0.0998 -0.0381 344 ARG B C 5707 O O . ARG B 314 ? 1.1291 0.9629 1.0434 -0.0601 0.0978 -0.0453 344 ARG B O 5708 C CB . ARG B 314 ? 1.2294 1.0846 1.1284 -0.0505 0.0861 -0.0358 344 ARG B CB 5709 C CG . ARG B 314 ? 1.2208 1.0853 1.1119 -0.0462 0.0798 -0.0326 344 ARG B CG 5710 C CD . ARG B 314 ? 1.3090 1.1848 1.2035 -0.0496 0.0715 -0.0349 344 ARG B CD 5711 N NE . ARG B 314 ? 1.3165 1.2002 1.2055 -0.0459 0.0659 -0.0307 344 ARG B NE 5712 C CZ . ARG B 314 ? 1.3522 1.2391 1.2338 -0.0457 0.0615 -0.0316 344 ARG B CZ 5713 N NH1 . ARG B 314 ? 1.3228 1.2066 1.1997 -0.0482 0.0616 -0.0368 344 ARG B NH1 5714 N NH2 . ARG B 314 ? 1.4008 1.2940 1.2796 -0.0429 0.0571 -0.0273 344 ARG B NH2 5715 N N . LEU B 315 ? 1.1841 1.0043 1.0879 -0.0493 0.1078 -0.0314 345 LEU B N 5716 C CA . LEU B 315 ? 1.1801 0.9872 1.0923 -0.0538 0.1163 -0.0317 345 LEU B CA 5717 C C . LEU B 315 ? 1.1559 0.9634 1.0729 -0.0548 0.1218 -0.0250 345 LEU B C 5718 O O . LEU B 315 ? 1.1358 0.9429 1.0653 -0.0625 0.1253 -0.0283 345 LEU B O 5719 C CB . LEU B 315 ? 1.2016 0.9918 1.1076 -0.0486 0.1225 -0.0288 345 LEU B CB 5720 C CG . LEU B 315 ? 1.2118 1.0015 1.1122 -0.0462 0.1182 -0.0353 345 LEU B CG 5721 C CD1 . LEU B 315 ? 1.2346 1.0084 1.1286 -0.0391 0.1240 -0.0314 345 LEU B CD1 5722 C CD2 . LEU B 315 ? 1.1964 0.9872 1.1055 -0.0544 0.1153 -0.0467 345 LEU B CD2 5723 N N . TYR B 316 ? 1.1413 0.9505 1.0491 -0.0470 0.1229 -0.0162 346 TYR B N 5724 C CA . TYR B 316 ? 1.1191 0.9298 1.0292 -0.0467 0.1284 -0.0096 346 TYR B CA 5725 C C . TYR B 316 ? 1.0844 0.9132 1.0014 -0.0502 0.1216 -0.0131 346 TYR B C 5726 O O . TYR B 316 ? 1.0812 0.9212 0.9940 -0.0472 0.1125 -0.0149 346 TYR B O 5727 C CB . TYR B 316 ? 1.1094 0.9160 1.0061 -0.0360 0.1311 0.0002 346 TYR B CB 5728 C CG . TYR B 316 ? 1.1259 0.9141 1.0147 -0.0308 0.1372 0.0044 346 TYR B CG 5729 C CD1 . TYR B 316 ? 1.1355 0.9070 1.0277 -0.0343 0.1476 0.0077 346 TYR B CD1 5730 C CD2 . TYR B 316 ? 1.1069 0.8942 0.9856 -0.0223 0.1327 0.0049 346 TYR B CD2 5731 C CE1 . TYR B 316 ? 1.1559 0.9087 1.0403 -0.0287 0.1527 0.0118 346 TYR B CE1 5732 C CE2 . TYR B 316 ? 1.1147 0.8854 0.9864 -0.0165 0.1374 0.0082 346 TYR B CE2 5733 C CZ . TYR B 316 ? 1.1514 0.9043 1.0253 -0.0193 0.1472 0.0119 346 TYR B CZ 5734 O OH . TYR B 316 ? 1.1556 0.8905 1.0220 -0.0126 0.1512 0.0153 346 TYR B OH 5735 N N . ARG B 317 ? 1.0918 0.9228 1.0205 -0.0565 0.1266 -0.0140 347 ARG B N 5736 C CA . ARG B 317 ? 1.0854 0.9329 1.0238 -0.0605 0.1212 -0.0185 347 ARG B CA 5737 C C . ARG B 317 ? 1.0722 0.9258 1.0081 -0.0559 0.1250 -0.0113 347 ARG B C 5738 O O . ARG B 317 ? 1.1160 0.9844 1.0579 -0.0566 0.1197 -0.0140 347 ARG B O 5739 C CB . ARG B 317 ? 1.1109 0.9581 1.0666 -0.0711 0.1244 -0.0263 347 ARG B CB 5740 C CG . ARG B 317 ? 1.1573 1.0209 1.1244 -0.0761 0.1148 -0.0358 347 ARG B CG 5741 C CD . ARG B 317 ? 1.1736 1.0439 1.1318 -0.0726 0.1022 -0.0395 347 ARG B CD 5742 N NE . ARG B 317 ? 1.1385 0.9978 1.0877 -0.0712 0.1019 -0.0405 347 ARG B NE 5743 C CZ . ARG B 317 ? 1.1177 0.9811 1.0587 -0.0689 0.0930 -0.0438 347 ARG B CZ 5744 N NH1 . ARG B 317 ? 1.0806 0.9569 1.0202 -0.0678 0.0833 -0.0455 347 ARG B NH1 5745 N NH2 . ARG B 317 ? 1.1803 1.0343 1.1140 -0.0676 0.0940 -0.0453 347 ARG B NH2 5746 N N . SER B 318 ? 1.0655 0.9077 0.9913 -0.0501 0.1337 -0.0022 348 SER B N 5747 C CA . SER B 318 ? 1.0406 0.8873 0.9611 -0.0444 0.1380 0.0049 348 SER B CA 5748 C C . SER B 318 ? 1.0347 0.8670 0.9391 -0.0354 0.1448 0.0149 348 SER B C 5749 O O . SER B 318 ? 1.0315 0.8472 0.9338 -0.0367 0.1516 0.0174 348 SER B O 5750 C CB . SER B 318 ? 1.0748 0.9245 1.0085 -0.0519 0.1469 0.0043 348 SER B CB 5751 O OG . SER B 318 ? 1.1411 0.9935 1.0678 -0.0461 0.1533 0.0119 348 SER B OG 5752 N N . MET B 319 ? 1.0451 0.8835 0.9383 -0.0256 0.1423 0.0199 349 MET B N 5753 C CA . MET B 319 ? 1.0691 0.8954 0.9455 -0.0151 0.1468 0.0289 349 MET B CA 5754 C C . MET B 319 ? 1.1144 0.9346 0.9849 -0.0127 0.1587 0.0375 349 MET B C 5755 O O . MET B 319 ? 1.0835 0.8959 0.9381 -0.0023 0.1619 0.0456 349 MET B O 5756 C CB . MET B 319 ? 1.0366 0.8728 0.9035 -0.0048 0.1364 0.0286 349 MET B CB 5757 C CG . MET B 319 ? 0.9847 0.8241 0.8544 -0.0060 0.1266 0.0220 349 MET B CG 5758 S SD . MET B 319 ? 0.9595 0.7807 0.8207 -0.0019 0.1295 0.0243 349 MET B SD 5759 C CE . MET B 319 ? 0.9832 0.7963 0.8573 -0.0151 0.1335 0.0184 349 MET B CE 5760 N N . ASN B 320 ? 1.1584 0.9827 1.0419 -0.0220 0.1654 0.0357 350 ASN B N 5761 C CA . ASN B 320 ? 1.2133 1.0320 1.0931 -0.0218 0.1788 0.0439 350 ASN B CA 5762 C C . ASN B 320 ? 1.2616 1.0563 1.1281 -0.0177 0.1897 0.0543 350 ASN B C 5763 O O . ASN B 320 ? 1.2733 1.0622 1.1237 -0.0088 0.1961 0.0639 350 ASN B O 5764 C CB . ASN B 320 ? 1.2313 1.0563 1.1315 -0.0349 0.1850 0.0386 350 ASN B CB 5765 C CG . ASN B 320 ? 1.2369 1.0596 1.1352 -0.0356 0.1995 0.0464 350 ASN B CG 5766 O OD1 . ASN B 320 ? 1.2983 1.1047 1.1983 -0.0410 0.2124 0.0520 350 ASN B OD1 5767 N ND2 . ASN B 320 ? 1.1808 1.0191 1.0750 -0.0300 0.1979 0.0469 350 ASN B ND2 5768 N N . SER B 321 ? 1.2705 1.0505 1.1425 -0.0234 0.1913 0.0523 351 SER B N 5769 C CA . SER B 321 ? 1.3260 1.0815 1.1863 -0.0194 0.2007 0.0617 351 SER B CA 5770 C C . SER B 321 ? 1.3125 1.0638 1.1510 -0.0036 0.1954 0.0680 351 SER B C 5771 O O . SER B 321 ? 1.3340 1.0743 1.1560 0.0049 0.2030 0.0788 351 SER B O 5772 C CB . SER B 321 ? 1.3285 1.0707 1.1991 -0.0270 0.2004 0.0562 351 SER B CB 5773 O OG . SER B 321 ? 1.3244 1.0724 1.2167 -0.0413 0.2035 0.0484 351 SER B OG 5774 N N . GLN B 322 ? 1.2718 1.0327 1.1105 0.0002 0.1822 0.0607 352 GLN B N 5775 C CA . GLN B 322 ? 1.2993 1.0567 1.1212 0.0142 0.1759 0.0641 352 GLN B CA 5776 C C . GLN B 322 ? 1.3172 1.0817 1.1243 0.0255 0.1761 0.0708 352 GLN B C 5777 O O . GLN B 322 ? 1.3873 1.1408 1.1767 0.0378 0.1776 0.0784 352 GLN B O 5778 C CB . GLN B 322 ? 1.2533 1.0238 1.0812 0.0147 0.1621 0.0541 352 GLN B CB 5779 C CG . GLN B 322 ? 1.2439 1.0058 1.0813 0.0074 0.1609 0.0478 352 GLN B CG 5780 C CD . GLN B 322 ? 1.2399 1.0074 1.0957 -0.0073 0.1621 0.0403 352 GLN B CD 5781 O OE1 . GLN B 322 ? 1.1611 0.9400 1.0243 -0.0127 0.1636 0.0394 352 GLN B OE1 5782 N NE2 . GLN B 322 ? 1.2866 1.0466 1.1502 -0.0134 0.1611 0.0341 352 GLN B NE2 5783 N N . TYR B 323 ? 1.3026 1.0852 1.1165 0.0220 0.1744 0.0674 353 TYR B N 5784 C CA . TYR B 323 ? 1.2963 1.0886 1.0972 0.0328 0.1733 0.0716 353 TYR B CA 5785 C C . TYR B 323 ? 1.3117 1.0906 1.0996 0.0359 0.1880 0.0835 353 TYR B C 5786 O O . TYR B 323 ? 1.3287 1.1033 1.0968 0.0494 0.1886 0.0907 353 TYR B O 5787 C CB . TYR B 323 ? 1.2746 1.0906 1.0875 0.0285 0.1664 0.0635 353 TYR B CB 5788 C CG . TYR B 323 ? 1.2365 1.0666 1.0535 0.0320 0.1509 0.0550 353 TYR B CG 5789 C CD1 . TYR B 323 ? 1.2031 1.0392 1.0078 0.0454 0.1434 0.0557 353 TYR B CD1 5790 C CD2 . TYR B 323 ? 1.2443 1.0817 1.0777 0.0220 0.1440 0.0461 353 TYR B CD2 5791 C CE1 . TYR B 323 ? 1.1797 1.0283 0.9900 0.0477 0.1302 0.0479 353 TYR B CE1 5792 C CE2 . TYR B 323 ? 1.2071 1.0561 1.0437 0.0246 0.1312 0.0394 353 TYR B CE2 5793 C CZ . TYR B 323 ? 1.2015 1.0560 1.0276 0.0370 0.1247 0.0403 353 TYR B CZ 5794 O OH . TYR B 323 ? 1.1694 1.0353 1.0007 0.0386 0.1126 0.0336 353 TYR B OH 5795 N N . LEU B 324 ? 1.3326 1.1046 1.1314 0.0237 0.1998 0.0854 354 LEU B N 5796 C CA . LEU B 324 ? 1.3895 1.1457 1.1766 0.0251 0.2159 0.0978 354 LEU B CA 5797 C C . LEU B 324 ? 1.4378 1.1687 1.2072 0.0340 0.2194 0.1072 354 LEU B C 5798 O O . LEU B 324 ? 1.5095 1.2301 1.2575 0.0452 0.2257 0.1183 354 LEU B O 5799 C CB . LEU B 324 ? 1.3644 1.1170 1.1705 0.0086 0.2279 0.0969 354 LEU B CB 5800 C CG . LEU B 324 ? 1.3428 1.1194 1.1670 0.0000 0.2265 0.0883 354 LEU B CG 5801 C CD1 . LEU B 324 ? 1.3327 1.1059 1.1798 -0.0170 0.2359 0.0846 354 LEU B CD1 5802 C CD2 . LEU B 324 ? 1.3778 1.1647 1.1894 0.0076 0.2320 0.0940 354 LEU B CD2 5803 N N . LYS B 325 ? 1.4484 1.1699 1.2262 0.0300 0.2145 0.1024 355 LYS B N 5804 C CA . LYS B 325 ? 1.4723 1.1710 1.2357 0.0389 0.2156 0.1092 355 LYS B CA 5805 C C . LYS B 325 ? 1.4073 1.1100 1.1502 0.0573 0.2061 0.1118 355 LYS B C 5806 O O . LYS B 325 ? 1.4413 1.1257 1.1654 0.0685 0.2098 0.1213 355 LYS B O 5807 C CB . LYS B 325 ? 1.5139 1.2069 1.2923 0.0314 0.2101 0.1005 355 LYS B CB 5808 C CG . LYS B 325 ? 1.6125 1.2780 1.3811 0.0367 0.2148 0.1073 355 LYS B CG 5809 C CD . LYS B 325 ? 1.6349 1.2962 1.4199 0.0284 0.2100 0.0972 355 LYS B CD 5810 C CE . LYS B 325 ? 1.6266 1.2839 1.4320 0.0108 0.2186 0.0934 355 LYS B CE 5811 N NZ . LYS B 325 ? 1.6526 1.2974 1.4688 0.0055 0.2165 0.0864 355 LYS B NZ 5812 N N . LEU B 326 ? 1.3998 1.1262 1.1468 0.0605 0.1936 0.1029 356 LEU B N 5813 C CA . LEU B 326 ? 1.4521 1.1856 1.1824 0.0774 0.1839 0.1036 356 LEU B CA 5814 C C . LEU B 326 ? 1.4971 1.2350 1.2106 0.0862 0.1891 0.1112 356 LEU B C 5815 O O . LEU B 326 ? 1.5637 1.2993 1.2573 0.1022 0.1853 0.1159 356 LEU B O 5816 C CB . LEU B 326 ? 1.4361 1.1926 1.1791 0.0768 0.1687 0.0907 356 LEU B CB 5817 C CG . LEU B 326 ? 1.4763 1.2302 1.2309 0.0726 0.1615 0.0831 356 LEU B CG 5818 C CD1 . LEU B 326 ? 1.4487 1.2244 1.2212 0.0643 0.1514 0.0712 356 LEU B CD1 5819 C CD2 . LEU B 326 ? 1.4835 1.2304 1.2250 0.0874 0.1549 0.0843 356 LEU B CD2 5820 N N . LEU B 327 ? 1.5031 1.2486 1.2248 0.0763 0.1975 0.1119 357 LEU B N 5821 C CA . LEU B 327 ? 1.5049 1.2567 1.2117 0.0836 0.2035 0.1183 357 LEU B CA 5822 C C . LEU B 327 ? 1.5587 1.2868 1.2462 0.0877 0.2193 0.1336 357 LEU B C 5823 O O . LEU B 327 ? 1.5816 1.3098 1.2477 0.1000 0.2225 0.1411 357 LEU B O 5824 C CB . LEU B 327 ? 1.4603 1.2309 1.1845 0.0717 0.2066 0.1122 357 LEU B CB 5825 C CG . LEU B 327 ? 1.4335 1.2296 1.1700 0.0722 0.1909 0.0990 357 LEU B CG 5826 C CD1 . LEU B 327 ? 1.4409 1.2512 1.2004 0.0568 0.1933 0.0917 357 LEU B CD1 5827 C CD2 . LEU B 327 ? 1.4007 1.2091 1.1201 0.0879 0.1847 0.0994 357 LEU B CD2 5828 N N . SER B 328 ? 1.5630 1.2707 1.2581 0.0775 0.2292 0.1382 358 SER B N 5829 C CA . SER B 328 ? 1.6643 1.3466 1.3432 0.0792 0.2457 0.1536 358 SER B CA 5830 C C . SER B 328 ? 1.7190 1.3870 1.3676 0.0994 0.2429 0.1633 358 SER B C 5831 O O . SER B 328 ? 1.7604 1.4190 1.3868 0.1077 0.2532 0.1757 358 SER B O 5832 C CB . SER B 328 ? 1.6633 1.3247 1.3572 0.0659 0.2537 0.1548 358 SER B CB 5833 O OG . SER B 328 ? 1.6319 1.2835 1.3247 0.0718 0.2431 0.1512 358 SER B OG 5834 N N . SER B 329 ? 1.6828 1.3495 1.3304 0.1077 0.2291 0.1575 359 SER B N 5835 C CA . SER B 329 ? 1.6980 1.3530 1.3191 0.1279 0.2238 0.1645 359 SER B CA 5836 C C . SER B 329 ? 1.7092 1.3809 1.3114 0.1423 0.2189 0.1655 359 SER B C 5837 O O . SER B 329 ? 1.7947 1.4534 1.3692 0.1575 0.2226 0.1768 359 SER B O 5838 C CB . SER B 329 ? 1.6723 1.3298 1.3007 0.1332 0.2083 0.1547 359 SER B CB 5839 O OG . SER B 329 ? 1.5916 1.2775 1.2283 0.1365 0.1936 0.1421 359 SER B OG 5840 N N . GLN B 330 ? 1.6124 1.3123 1.2294 0.1380 0.2102 0.1534 360 GLN B N 5841 C CA . GLN B 330 ? 1.6183 1.3378 1.2218 0.1508 0.2034 0.1510 360 GLN B CA 5842 C C . GLN B 330 ? 1.6246 1.3469 1.2118 0.1708 0.1887 0.1482 360 GLN B C 5843 O O . GLN B 330 ? 1.5519 1.2831 1.1204 0.1852 0.1850 0.1496 360 GLN B O 5844 C CB . GLN B 330 ? 1.7094 1.4235 1.2939 0.1536 0.2188 0.1631 360 GLN B CB 5845 C CG . GLN B 330 ? 1.7551 1.4794 1.3600 0.1351 0.2295 0.1607 360 GLN B CG 5846 C CD . GLN B 330 ? 1.8191 1.5388 1.4079 0.1358 0.2467 0.1724 360 GLN B CD 5847 O OE1 . GLN B 330 ? 1.8210 1.5393 1.4248 0.1200 0.2602 0.1745 360 GLN B OE1 5848 N NE2 . GLN B 330 ? 1.8465 1.5657 1.4056 0.1542 0.2464 0.1795 360 GLN B NE2 5849 N N . LYS B 331 ? 1.6955 1.4119 1.2914 0.1716 0.1798 0.1431 361 LYS B N 5850 C CA . LYS B 331 ? 1.6705 1.3943 1.2583 0.1885 0.1640 0.1369 361 LYS B CA 5851 C C . LYS B 331 ? 1.6127 1.3646 1.2229 0.1838 0.1498 0.1205 361 LYS B C 5852 O O . LYS B 331 ? 1.6412 1.4052 1.2481 0.1967 0.1361 0.1132 361 LYS B O 5853 C CB . LYS B 331 ? 1.7275 1.4316 1.3143 0.1924 0.1617 0.1390 361 LYS B CB 5854 C CG . LYS B 331 ? 1.8070 1.4794 1.3748 0.1951 0.1760 0.1553 361 LYS B CG 5855 C CD . LYS B 331 ? 1.8664 1.5209 1.4357 0.1993 0.1718 0.1552 361 LYS B CD 5856 C CE . LYS B 331 ? 1.9364 1.5569 1.4854 0.2038 0.1851 0.1719 361 LYS B CE 5857 N NZ . LYS B 331 ? 1.9005 1.5033 1.4509 0.2094 0.1801 0.1711 361 LYS B NZ 5858 N N . TYR B 332 ? 1.5639 1.3259 1.1971 0.1656 0.1528 0.1147 362 TYR B N 5859 C CA . TYR B 332 ? 1.4993 1.2828 1.1562 0.1585 0.1401 0.1000 362 TYR B CA 5860 C C . TYR B 332 ? 1.5225 1.3290 1.1888 0.1537 0.1369 0.0930 362 TYR B C 5861 O O . TYR B 332 ? 1.4696 1.2766 1.1396 0.1438 0.1471 0.0964 362 TYR B O 5862 C CB . TYR B 332 ? 1.4074 1.1837 1.0849 0.1423 0.1425 0.0967 362 TYR B CB 5863 C CG . TYR B 332 ? 1.3803 1.1334 1.0501 0.1466 0.1457 0.1027 362 TYR B CG 5864 C CD1 . TYR B 332 ? 1.3737 1.1243 1.0321 0.1629 0.1366 0.1017 362 TYR B CD1 5865 C CD2 . TYR B 332 ? 1.3442 1.0780 1.0191 0.1348 0.1575 0.1086 362 TYR B CD2 5866 C CE1 . TYR B 332 ? 1.3515 1.0808 1.0031 0.1677 0.1391 0.1067 362 TYR B CE1 5867 C CE2 . TYR B 332 ? 1.3546 1.0663 1.0226 0.1393 0.1603 0.1137 362 TYR B CE2 5868 C CZ . TYR B 332 ? 1.3568 1.0662 1.0129 0.1560 0.1509 0.1129 362 TYR B CZ 5869 O OH . TYR B 332 ? 1.3959 1.0835 1.0457 0.1613 0.1529 0.1173 362 TYR B OH 5870 N N . GLN B 333 ? 1.5608 1.3865 1.2328 0.1608 0.1225 0.0824 363 GLN B N 5871 C CA . GLN B 333 ? 1.5779 1.4258 1.2598 0.1582 0.1168 0.0741 363 GLN B CA 5872 C C . GLN B 333 ? 1.4925 1.3516 1.2020 0.1424 0.1111 0.0641 363 GLN B C 5873 O O . GLN B 333 ? 1.4621 1.3261 1.1821 0.1427 0.1011 0.0569 363 GLN B O 5874 C CB . GLN B 333 ? 1.6876 1.5489 1.3604 0.1754 0.1039 0.0677 363 GLN B CB 5875 C CG . GLN B 333 ? 1.8023 1.6853 1.4810 0.1766 0.0976 0.0595 363 GLN B CG 5876 C CD . GLN B 333 ? 1.9392 1.8382 1.6205 0.1890 0.0812 0.0483 363 GLN B CD 5877 O OE1 . GLN B 333 ? 2.0180 1.9130 1.6972 0.1968 0.0744 0.0466 363 GLN B OE1 5878 N NE2 . GLN B 333 ? 2.0092 1.9268 1.6970 0.1907 0.0744 0.0398 363 GLN B NE2 5879 N N . ILE B 334 ? 1.3981 1.2615 1.1190 0.1291 0.1175 0.0637 364 ILE B N 5880 C CA . ILE B 334 ? 1.3128 1.1833 1.0576 0.1136 0.1137 0.0560 364 ILE B CA 5881 C C . ILE B 334 ? 1.2140 1.1056 0.9719 0.1103 0.1061 0.0470 364 ILE B C 5882 O O . ILE B 334 ? 1.1804 1.0784 0.9333 0.1125 0.1104 0.0484 364 ILE B O 5883 C CB . ILE B 334 ? 1.3073 1.1653 1.0587 0.0992 0.1265 0.0615 364 ILE B CB 5884 C CG1 . ILE B 334 ? 1.2880 1.1235 1.0286 0.1014 0.1338 0.0699 364 ILE B CG1 5885 C CG2 . ILE B 334 ? 1.2965 1.1627 1.0707 0.0844 0.1218 0.0532 364 ILE B CG2 5886 C CD1 . ILE B 334 ? 1.2755 1.0966 1.0201 0.0891 0.1478 0.0763 364 ILE B CD1 5887 N N . LEU B 335 ? 1.0779 0.9793 0.8522 0.1052 0.0953 0.0380 365 LEU B N 5888 C CA . LEU B 335 ? 1.0246 0.9437 0.8132 0.1011 0.0872 0.0293 365 LEU B CA 5889 C C . LEU B 335 ? 1.0051 0.9261 0.8130 0.0861 0.0847 0.0247 365 LEU B C 5890 O O . LEU B 335 ? 0.9959 0.9120 0.8093 0.0823 0.0814 0.0232 365 LEU B O 5891 C CB . LEU B 335 ? 0.9879 0.9194 0.7774 0.1118 0.0740 0.0217 365 LEU B CB 5892 C CG . LEU B 335 ? 0.9569 0.9053 0.7622 0.1083 0.0641 0.0121 365 LEU B CG 5893 C CD1 . LEU B 335 ? 0.9570 0.9142 0.7570 0.1129 0.0667 0.0116 365 LEU B CD1 5894 C CD2 . LEU B 335 ? 0.9195 0.8771 0.7306 0.1156 0.0510 0.0041 365 LEU B CD2 5895 N N . LEU B 336 ? 0.9420 0.8707 0.7597 0.0782 0.0861 0.0221 366 LEU B N 5896 C CA . LEU B 336 ? 0.9026 0.8357 0.7378 0.0660 0.0813 0.0167 366 LEU B CA 5897 C C . LEU B 336 ? 0.9061 0.8552 0.7499 0.0686 0.0711 0.0090 366 LEU B C 5898 O O . LEU B 336 ? 0.9043 0.8613 0.7458 0.0727 0.0727 0.0081 366 LEU B O 5899 C CB . LEU B 336 ? 0.8866 0.8149 0.7281 0.0544 0.0907 0.0191 366 LEU B CB 5900 C CG . LEU B 336 ? 0.8881 0.8013 0.7295 0.0469 0.0974 0.0232 366 LEU B CG 5901 C CD1 . LEU B 336 ? 0.9405 0.8394 0.7659 0.0535 0.1074 0.0319 366 LEU B CD1 5902 C CD2 . LEU B 336 ? 0.8839 0.7970 0.7377 0.0340 0.1024 0.0216 366 LEU B CD2 5903 N N . TYR B 337 ? 0.9443 0.8978 0.7979 0.0664 0.0608 0.0035 367 TYR B N 5904 C CA . TYR B 337 ? 0.9208 0.8877 0.7848 0.0676 0.0503 -0.0039 367 TYR B CA 5905 C C . TYR B 337 ? 0.8670 0.8347 0.7456 0.0560 0.0452 -0.0073 367 TYR B C 5906 O O . TYR B 337 ? 0.8292 0.7889 0.7091 0.0494 0.0470 -0.0052 367 TYR B O 5907 C CB . TYR B 337 ? 0.9161 0.8885 0.7777 0.0784 0.0416 -0.0079 367 TYR B CB 5908 C CG . TYR B 337 ? 0.8895 0.8572 0.7547 0.0763 0.0380 -0.0084 367 TYR B CG 5909 C CD1 . TYR B 337 ? 0.8775 0.8352 0.7323 0.0797 0.0437 -0.0033 367 TYR B CD1 5910 C CD2 . TYR B 337 ? 0.8651 0.8384 0.7443 0.0713 0.0289 -0.0140 367 TYR B CD2 5911 C CE1 . TYR B 337 ? 0.8925 0.8475 0.7515 0.0783 0.0406 -0.0047 367 TYR B CE1 5912 C CE2 . TYR B 337 ? 0.8461 0.8163 0.7291 0.0691 0.0266 -0.0146 367 TYR B CE2 5913 C CZ . TYR B 337 ? 0.8552 0.8172 0.7286 0.0727 0.0324 -0.0104 367 TYR B CZ 5914 O OH . TYR B 337 ? 0.8211 0.7815 0.6992 0.0707 0.0305 -0.0118 367 TYR B OH 5915 N N . ASN B 338 ? 0.8661 0.8434 0.7548 0.0542 0.0389 -0.0126 368 ASN B N 5916 C CA . ASN B 338 ? 0.9076 0.8854 0.8085 0.0440 0.0338 -0.0153 368 ASN B CA 5917 C C . ASN B 338 ? 0.8756 0.8628 0.7871 0.0460 0.0222 -0.0220 368 ASN B C 5918 O O . ASN B 338 ? 0.9386 0.9345 0.8510 0.0527 0.0196 -0.0257 368 ASN B O 5919 C CB . ASN B 338 ? 0.9373 0.9143 0.8417 0.0364 0.0402 -0.0142 368 ASN B CB 5920 C CG . ASN B 338 ? 0.9794 0.9447 0.8789 0.0298 0.0496 -0.0089 368 ASN B CG 5921 O OD1 . ASN B 338 ? 1.0075 0.9660 0.8964 0.0338 0.0578 -0.0039 368 ASN B OD1 5922 N ND2 . ASN B 338 ? 0.9504 0.9132 0.8574 0.0201 0.0482 -0.0102 368 ASN B ND2 5923 N N . GLY B 339 ? 0.7897 0.7746 0.7087 0.0403 0.0155 -0.0233 369 GLY B N 5924 C CA . GLY B 339 ? 0.7581 0.7488 0.6884 0.0396 0.0051 -0.0286 369 GLY B CA 5925 C C . GLY B 339 ? 0.7369 0.7303 0.6732 0.0346 0.0045 -0.0303 369 GLY B C 5926 O O . GLY B 339 ? 0.7291 0.7173 0.6650 0.0269 0.0086 -0.0275 369 GLY B O 5927 N N . ASP B 340 ? 0.7240 0.7263 0.6667 0.0395 -0.0010 -0.0357 370 ASP B N 5928 C CA . ASP B 340 ? 0.7403 0.7473 0.6893 0.0362 -0.0011 -0.0382 370 ASP B CA 5929 C C . ASP B 340 ? 0.7297 0.7348 0.6889 0.0303 -0.0104 -0.0406 370 ASP B C 5930 O O . ASP B 340 ? 0.7227 0.7329 0.6891 0.0288 -0.0128 -0.0441 370 ASP B O 5931 C CB . ASP B 340 ? 0.7586 0.7769 0.7090 0.0447 -0.0012 -0.0433 370 ASP B CB 5932 C CG . ASP B 340 ? 0.7943 0.8184 0.7527 0.0509 -0.0130 -0.0500 370 ASP B CG 5933 O OD1 . ASP B 340 ? 0.7030 0.7221 0.6648 0.0496 -0.0199 -0.0500 370 ASP B OD1 5934 O OD2 . ASP B 340 ? 0.8429 0.8771 0.8051 0.0569 -0.0150 -0.0558 370 ASP B OD2 5935 N N . VAL B 341 ? 0.7206 0.7186 0.6803 0.0271 -0.0154 -0.0385 371 VAL B N 5936 C CA . VAL B 341 ? 0.7306 0.7238 0.6962 0.0208 -0.0226 -0.0384 371 VAL B CA 5937 C C . VAL B 341 ? 0.7706 0.7539 0.7295 0.0128 -0.0186 -0.0325 371 VAL B C 5938 O O . VAL B 341 ? 0.7891 0.7665 0.7496 0.0081 -0.0243 -0.0310 371 VAL B O 5939 C CB . VAL B 341 ? 0.7205 0.7139 0.6941 0.0238 -0.0333 -0.0416 371 VAL B CB 5940 C CG1 . VAL B 341 ? 0.7500 0.7538 0.7306 0.0316 -0.0377 -0.0487 371 VAL B CG1 5941 C CG2 . VAL B 341 ? 0.7240 0.7146 0.6956 0.0254 -0.0328 -0.0399 371 VAL B CG2 5942 N N . ASP B 342 ? 0.7596 0.7406 0.7104 0.0118 -0.0088 -0.0293 372 ASP B N 5943 C CA . ASP B 342 ? 0.7595 0.7321 0.7039 0.0050 -0.0042 -0.0249 372 ASP B CA 5944 C C . ASP B 342 ? 0.7880 0.7600 0.7329 -0.0003 -0.0014 -0.0256 372 ASP B C 5945 O O . ASP B 342 ? 0.8621 0.8397 0.8095 0.0012 0.0028 -0.0277 372 ASP B O 5946 C CB . ASP B 342 ? 0.7558 0.7252 0.6920 0.0072 0.0045 -0.0217 372 ASP B CB 5947 C CG . ASP B 342 ? 0.7761 0.7373 0.7060 0.0006 0.0101 -0.0183 372 ASP B CG 5948 O OD1 . ASP B 342 ? 0.7781 0.7355 0.7085 -0.0048 0.0058 -0.0177 372 ASP B OD1 5949 O OD2 . ASP B 342 ? 0.7639 0.7218 0.6878 0.0012 0.0185 -0.0161 372 ASP B OD2 5950 N N . MET B 343 ? 0.7686 0.7345 0.7111 -0.0067 -0.0034 -0.0240 373 MET B N 5951 C CA . MET B 343 ? 0.7928 0.7585 0.7365 -0.0119 -0.0018 -0.0258 373 MET B CA 5952 C C . MET B 343 ? 0.8013 0.7599 0.7375 -0.0168 0.0057 -0.0233 373 MET B C 5953 O O . MET B 343 ? 0.8699 0.8286 0.8079 -0.0210 0.0084 -0.0256 373 MET B O 5954 C CB . MET B 343 ? 0.8190 0.7842 0.7660 -0.0143 -0.0120 -0.0277 373 MET B CB 5955 C CG . MET B 343 ? 0.8106 0.7827 0.7667 -0.0094 -0.0201 -0.0313 373 MET B CG 5956 S SD . MET B 343 ? 0.8236 0.7948 0.7841 -0.0108 -0.0327 -0.0339 373 MET B SD 5957 C CE . MET B 343 ? 0.8547 0.8133 0.8037 -0.0149 -0.0349 -0.0271 373 MET B CE 5958 N N . ALA B 344 ? 0.7628 0.7159 0.6920 -0.0162 0.0088 -0.0195 374 ALA B N 5959 C CA . ALA B 344 ? 0.7642 0.7108 0.6864 -0.0193 0.0169 -0.0176 374 ALA B CA 5960 C C . ALA B 344 ? 0.7850 0.7318 0.7076 -0.0178 0.0260 -0.0176 374 ALA B C 5961 O O . ALA B 344 ? 0.7801 0.7233 0.7024 -0.0223 0.0310 -0.0186 374 ALA B O 5962 C CB . ALA B 344 ? 0.7729 0.7154 0.6893 -0.0177 0.0183 -0.0143 374 ALA B CB 5963 N N . CYS B 345 ? 0.8633 0.8137 0.7861 -0.0113 0.0281 -0.0165 375 CYS B N 5964 C CA . CYS B 345 ? 0.8653 0.8151 0.7866 -0.0091 0.0374 -0.0152 375 CYS B CA 5965 C C . CYS B 345 ? 0.8276 0.7866 0.7533 -0.0035 0.0360 -0.0168 375 CYS B C 5966 O O . CYS B 345 ? 0.8653 0.8257 0.7863 0.0037 0.0378 -0.0150 375 CYS B O 5967 C CB . CYS B 345 ? 0.8787 0.8215 0.7908 -0.0051 0.0439 -0.0110 375 CYS B CB 5968 S SG . CYS B 345 ? 0.8778 0.8099 0.7850 -0.0113 0.0478 -0.0100 375 CYS B SG 5969 N N . ASN B 346 ? 0.8335 0.7992 0.7680 -0.0062 0.0325 -0.0209 376 ASN B N 5970 C CA . ASN B 346 ? 0.8370 0.8127 0.7770 -0.0006 0.0285 -0.0239 376 ASN B CA 5971 C C . ASN B 346 ? 0.8086 0.7868 0.7442 0.0048 0.0376 -0.0218 376 ASN B C 5972 O O . ASN B 346 ? 0.8697 0.8421 0.8011 0.0023 0.0478 -0.0185 376 ASN B O 5973 C CB . ASN B 346 ? 0.8637 0.8465 0.8149 -0.0045 0.0229 -0.0294 376 ASN B CB 5974 C CG . ASN B 346 ? 0.8816 0.8675 0.8382 -0.0086 0.0317 -0.0310 376 ASN B CG 5975 O OD1 . ASN B 346 ? 0.8743 0.8667 0.8328 -0.0050 0.0374 -0.0315 376 ASN B OD1 5976 N ND2 . ASN B 346 ? 0.9286 0.9102 0.8881 -0.0162 0.0330 -0.0322 376 ASN B ND2 5977 N N . PHE B 347 ? 0.7840 0.7700 0.7199 0.0127 0.0340 -0.0238 377 PHE B N 5978 C CA . PHE B 347 ? 0.7721 0.7607 0.7005 0.0200 0.0419 -0.0214 377 PHE B CA 5979 C C . PHE B 347 ? 0.8113 0.8022 0.7420 0.0167 0.0527 -0.0207 377 PHE B C 5980 O O . PHE B 347 ? 0.7796 0.7659 0.7010 0.0193 0.0632 -0.0155 377 PHE B O 5981 C CB . PHE B 347 ? 0.7438 0.7424 0.6737 0.0291 0.0346 -0.0257 377 PHE B CB 5982 C CG . PHE B 347 ? 0.7434 0.7533 0.6846 0.0287 0.0308 -0.0319 377 PHE B CG 5983 C CD1 . PHE B 347 ? 0.7243 0.7369 0.6762 0.0256 0.0197 -0.0367 377 PHE B CD1 5984 C CD2 . PHE B 347 ? 0.7680 0.7856 0.7089 0.0317 0.0389 -0.0327 377 PHE B CD2 5985 C CE1 . PHE B 347 ? 0.7432 0.7663 0.7063 0.0259 0.0158 -0.0430 377 PHE B CE1 5986 C CE2 . PHE B 347 ? 0.7395 0.7689 0.6922 0.0315 0.0358 -0.0393 377 PHE B CE2 5987 C CZ . PHE B 347 ? 0.7361 0.7684 0.7003 0.0289 0.0237 -0.0448 377 PHE B CZ 5988 N N . MET B 348 ? 0.7975 0.7953 0.7409 0.0110 0.0502 -0.0258 378 MET B N 5989 C CA . MET B 348 ? 0.8310 0.8336 0.7799 0.0076 0.0603 -0.0264 378 MET B CA 5990 C C . MET B 348 ? 0.8710 0.8624 0.8171 0.0003 0.0710 -0.0215 378 MET B C 5991 O O . MET B 348 ? 0.9719 0.9617 0.9150 0.0001 0.0834 -0.0178 378 MET B O 5992 C CB . MET B 348 ? 0.8811 0.8952 0.8465 0.0034 0.0543 -0.0344 378 MET B CB 5993 C CG . MET B 348 ? 0.9210 0.9428 0.8946 0.0000 0.0653 -0.0361 378 MET B CG 5994 S SD . MET B 348 ? 1.0174 1.0574 1.0103 0.0000 0.0571 -0.0470 378 MET B SD 5995 C CE . MET B 348 ? 0.9692 1.0183 0.9557 0.0126 0.0527 -0.0486 378 MET B CE 5996 N N . GLY B 349 ? 0.8666 0.8498 0.8136 -0.0055 0.0668 -0.0216 379 GLY B N 5997 C CA . GLY B 349 ? 0.8657 0.8373 0.8105 -0.0122 0.0757 -0.0181 379 GLY B CA 5998 C C . GLY B 349 ? 0.8775 0.8396 0.8085 -0.0070 0.0860 -0.0101 379 GLY B C 5999 O O . GLY B 349 ? 0.8615 0.8181 0.7922 -0.0104 0.0979 -0.0067 379 GLY B O 6000 N N . ASP B 350 ? 0.8932 0.8533 0.8130 0.0014 0.0814 -0.0073 380 ASP B N 6001 C CA . ASP B 350 ? 0.9347 0.8862 0.8398 0.0083 0.0895 0.0000 380 ASP B CA 6002 C C . ASP B 350 ? 0.9497 0.9074 0.8503 0.0142 0.0972 0.0022 380 ASP B C 6003 O O . ASP B 350 ? 1.0273 0.9760 0.9174 0.0167 0.1083 0.0092 380 ASP B O 6004 C CB . ASP B 350 ? 0.9693 0.9188 0.8652 0.0162 0.0815 0.0009 380 ASP B CB 6005 C CG . ASP B 350 ? 0.9931 0.9327 0.8880 0.0118 0.0793 0.0016 380 ASP B CG 6006 O OD1 . ASP B 350 ? 1.0006 0.9296 0.8943 0.0064 0.0873 0.0045 380 ASP B OD1 6007 O OD2 . ASP B 350 ? 1.0403 0.9826 0.9361 0.0136 0.0697 -0.0010 380 ASP B OD2 6008 N N . GLU B 351 ? 0.8815 0.8537 0.7893 0.0169 0.0917 -0.0033 381 GLU B N 6009 C CA . GLU B 351 ? 0.9459 0.9255 0.8502 0.0218 0.1000 -0.0019 381 GLU B CA 6010 C C . GLU B 351 ? 0.9583 0.9348 0.8689 0.0131 0.1138 0.0005 381 GLU B C 6011 O O . GLU B 351 ? 1.0217 0.9942 0.9227 0.0160 0.1263 0.0070 381 GLU B O 6012 C CB . GLU B 351 ? 0.9601 0.9567 0.8730 0.0260 0.0913 -0.0098 381 GLU B CB 6013 C CG . GLU B 351 ? 1.0102 1.0154 0.9164 0.0335 0.0993 -0.0087 381 GLU B CG 6014 C CD . GLU B 351 ? 1.0319 1.0523 0.9418 0.0417 0.0888 -0.0165 381 GLU B CD 6015 O OE1 . GLU B 351 ? 1.0017 1.0279 0.9245 0.0390 0.0765 -0.0236 381 GLU B OE1 6016 O OE2 . GLU B 351 ? 1.0694 1.0956 0.9687 0.0512 0.0929 -0.0154 381 GLU B OE2 6017 N N . TRP B 352 ? 0.9204 0.8989 0.8472 0.0025 0.1115 -0.0046 382 TRP B N 6018 C CA . TRP B 352 ? 0.9325 0.9080 0.8688 -0.0072 0.1238 -0.0037 382 TRP B CA 6019 C C . TRP B 352 ? 0.9928 0.9493 0.9181 -0.0091 0.1341 0.0050 382 TRP B C 6020 O O . TRP B 352 ? 1.0909 1.0419 1.0156 -0.0124 0.1483 0.0101 382 TRP B O 6021 C CB . TRP B 352 ? 0.8841 0.8638 0.8389 -0.0175 0.1171 -0.0119 382 TRP B CB 6022 C CG . TRP B 352 ? 0.8783 0.8761 0.8482 -0.0179 0.1091 -0.0211 382 TRP B CG 6023 C CD1 . TRP B 352 ? 0.8659 0.8771 0.8362 -0.0110 0.1086 -0.0234 382 TRP B CD1 6024 C CD2 . TRP B 352 ? 0.8451 0.8495 0.8317 -0.0251 0.1002 -0.0298 382 TRP B CD2 6025 N NE1 . TRP B 352 ? 0.8706 0.8960 0.8578 -0.0134 0.0996 -0.0331 382 TRP B NE1 6026 C CE2 . TRP B 352 ? 0.8730 0.8944 0.8701 -0.0219 0.0942 -0.0369 382 TRP B CE2 6027 C CE3 . TRP B 352 ? 0.8076 0.8054 0.8006 -0.0331 0.0961 -0.0327 382 TRP B CE3 6028 C CZ2 . TRP B 352 ? 0.8638 0.8951 0.8775 -0.0261 0.0839 -0.0464 382 TRP B CZ2 6029 C CZ3 . TRP B 352 ? 0.8334 0.8413 0.8417 -0.0372 0.0860 -0.0421 382 TRP B CZ3 6030 C CH2 . TRP B 352 ? 0.8472 0.8714 0.8657 -0.0336 0.0799 -0.0486 382 TRP B CH2 6031 N N . PHE B 353 ? 1.0261 0.9724 0.9440 -0.0075 0.1272 0.0065 383 PHE B N 6032 C CA . PHE B 353 ? 1.0164 0.9442 0.9245 -0.0087 0.1353 0.0138 383 PHE B CA 6033 C C . PHE B 353 ? 0.9892 0.9097 0.8795 0.0003 0.1453 0.0234 383 PHE B C 6034 O O . PHE B 353 ? 0.9825 0.8902 0.8686 -0.0025 0.1583 0.0302 383 PHE B O 6035 C CB . PHE B 353 ? 1.0147 0.9353 0.9175 -0.0068 0.1252 0.0129 383 PHE B CB 6036 C CG . PHE B 353 ? 1.0364 0.9385 0.9280 -0.0056 0.1324 0.0200 383 PHE B CG 6037 C CD1 . PHE B 353 ? 1.0210 0.9122 0.9200 -0.0152 0.1383 0.0196 383 PHE B CD1 6038 C CD2 . PHE B 353 ? 1.0158 0.9114 0.8899 0.0056 0.1328 0.0265 383 PHE B CD2 6039 C CE1 . PHE B 353 ? 1.0357 0.9089 0.9249 -0.0136 0.1446 0.0257 383 PHE B CE1 6040 C CE2 . PHE B 353 ? 1.0293 0.9073 0.8931 0.0076 0.1388 0.0328 383 PHE B CE2 6041 C CZ . PHE B 353 ? 1.0563 0.9227 0.9277 -0.0020 0.1449 0.0326 383 PHE B CZ 6042 N N . VAL B 354 ? 0.9643 0.8925 0.8439 0.0117 0.1390 0.0237 384 VAL B N 6043 C CA . VAL B 354 ? 0.9938 0.9160 0.8540 0.0224 0.1467 0.0322 384 VAL B CA 6044 C C . VAL B 354 ? 1.0458 0.9721 0.9072 0.0201 0.1604 0.0355 384 VAL B C 6045 O O . VAL B 354 ? 1.1068 1.0196 0.9580 0.0202 0.1739 0.0447 384 VAL B O 6046 C CB . VAL B 354 ? 0.9805 0.9123 0.8305 0.0354 0.1357 0.0299 384 VAL B CB 6047 C CG1 . VAL B 354 ? 0.9902 0.9182 0.8196 0.0473 0.1437 0.0378 384 VAL B CG1 6048 C CG2 . VAL B 354 ? 0.9601 0.8867 0.8080 0.0381 0.1242 0.0279 384 VAL B CG2 6049 N N . ASP B 355 ? 1.0928 1.0372 0.9673 0.0177 0.1574 0.0279 385 ASP B N 6050 C CA . ASP B 355 ? 1.0921 1.0438 0.9710 0.0147 0.1707 0.0294 385 ASP B CA 6051 C C . ASP B 355 ? 1.0928 1.0317 0.9791 0.0029 0.1855 0.0345 385 ASP B C 6052 O O . ASP B 355 ? 1.2181 1.1520 1.0970 0.0031 0.2011 0.0423 385 ASP B O 6053 C CB . ASP B 355 ? 1.0782 1.0517 0.9759 0.0116 0.1637 0.0181 385 ASP B CB 6054 C CG . ASP B 355 ? 1.1033 1.0903 0.9935 0.0241 0.1524 0.0136 385 ASP B CG 6055 O OD1 . ASP B 355 ? 1.0591 1.0403 0.9294 0.0354 0.1509 0.0189 385 ASP B OD1 6056 O OD2 . ASP B 355 ? 1.0872 1.0909 0.9923 0.0228 0.1447 0.0040 385 ASP B OD2 6057 N N . SER B 356 ? 1.0250 0.9578 0.9247 -0.0068 0.1810 0.0303 386 SER B N 6058 C CA . SER B 356 ? 1.0598 0.9806 0.9694 -0.0186 0.1936 0.0332 386 SER B CA 6059 C C . SER B 356 ? 1.0560 0.9526 0.9483 -0.0159 0.2023 0.0447 386 SER B C 6060 O O . SER B 356 ? 1.0532 0.9370 0.9527 -0.0252 0.2132 0.0479 386 SER B O 6061 C CB . SER B 356 ? 1.0353 0.9603 0.9671 -0.0301 0.1851 0.0227 386 SER B CB 6062 O OG . SER B 356 ? 1.0697 0.9855 0.9954 -0.0280 0.1739 0.0218 386 SER B OG 6063 N N . LEU B 357 ? 1.0538 0.9438 0.9244 -0.0031 0.1974 0.0505 387 LEU B N 6064 C CA . LEU B 357 ? 1.1182 0.9857 0.9699 0.0017 0.2067 0.0625 387 LEU B CA 6065 C C . LEU B 357 ? 1.2235 1.0850 1.0636 0.0041 0.2243 0.0731 387 LEU B C 6066 O O . LEU B 357 ? 1.2984 1.1387 1.1251 0.0059 0.2347 0.0839 387 LEU B O 6067 C CB . LEU B 357 ? 1.1218 0.9850 0.9540 0.0158 0.1958 0.0649 387 LEU B CB 6068 C CG . LEU B 357 ? 1.1483 1.0098 0.9872 0.0139 0.1820 0.0581 387 LEU B CG 6069 C CD1 . LEU B 357 ? 1.1645 1.0242 0.9856 0.0282 0.1724 0.0601 387 LEU B CD1 6070 C CD2 . LEU B 357 ? 1.1485 0.9915 0.9933 0.0049 0.1883 0.0603 387 LEU B CD2 6071 N N . ASN B 358 ? 1.2338 1.1132 1.0778 0.0049 0.2279 0.0705 388 ASN B N 6072 C CA . ASN B 358 ? 1.3029 1.1793 1.1342 0.0081 0.2450 0.0805 388 ASN B CA 6073 C C . ASN B 358 ? 1.3343 1.1937 1.1340 0.0226 0.2486 0.0933 388 ASN B C 6074 O O . ASN B 358 ? 1.3871 1.2246 1.1771 0.0210 0.2610 0.1044 388 ASN B O 6075 C CB . ASN B 358 ? 1.3867 1.2532 1.2325 -0.0065 0.2626 0.0845 388 ASN B CB 6076 C CG . ASN B 358 ? 1.3947 1.2804 1.2713 -0.0199 0.2618 0.0722 388 ASN B CG 6077 O OD1 . ASN B 358 ? 1.4139 1.3213 1.2992 -0.0174 0.2502 0.0618 388 ASN B OD1 6078 N ND2 . ASN B 358 ? 1.4417 1.3192 1.3358 -0.0340 0.2741 0.0728 388 ASN B ND2 6079 N N . GLN B 359 ? 1.3121 1.1815 1.0965 0.0370 0.2372 0.0912 389 GLN B N 6080 C CA . GLN B 359 ? 1.3435 1.2007 1.0976 0.0527 0.2390 0.1017 389 GLN B CA 6081 C C . GLN B 359 ? 1.4477 1.3191 1.1889 0.0616 0.2449 0.1036 389 GLN B C 6082 O O . GLN B 359 ? 1.4524 1.3441 1.2098 0.0561 0.2447 0.0951 389 GLN B O 6083 C CB . GLN B 359 ? 1.3083 1.1670 1.0560 0.0630 0.2201 0.0963 389 GLN B CB 6084 C CG . GLN B 359 ? 1.2742 1.1204 1.0339 0.0549 0.2142 0.0938 389 GLN B CG 6085 C CD . GLN B 359 ? 1.2771 1.0961 1.0264 0.0530 0.2272 0.1061 389 GLN B CD 6086 O OE1 . GLN B 359 ? 1.3114 1.1166 1.0363 0.0657 0.2298 0.1158 389 GLN B OE1 6087 N NE2 . GLN B 359 ? 1.2256 1.0363 0.9935 0.0375 0.2347 0.1053 389 GLN B NE2 6088 N N . LYS B 360 ? 1.6268 1.4876 1.3382 0.0760 0.2499 0.1144 390 LYS B N 6089 C CA . LYS B 360 ? 1.7523 1.6260 1.4471 0.0867 0.2555 0.1166 390 LYS B CA 6090 C C . LYS B 360 ? 1.7422 1.6389 1.4391 0.0966 0.2369 0.1035 390 LYS B C 6091 O O . LYS B 360 ? 1.8232 1.7174 1.5087 0.1082 0.2229 0.1015 390 LYS B O 6092 C CB . LYS B 360 ? 1.8439 1.6986 1.5037 0.1007 0.2649 0.1322 390 LYS B CB 6093 C CG . LYS B 360 ? 1.9198 1.7853 1.5602 0.1105 0.2749 0.1365 390 LYS B CG 6094 C CD . LYS B 360 ? 2.0309 1.8731 1.6380 0.1202 0.2901 0.1550 390 LYS B CD 6095 C CE . LYS B 360 ? 2.0700 1.9206 1.6618 0.1241 0.3068 0.1615 390 LYS B CE 6096 N NZ . LYS B 360 ? 2.1080 1.9323 1.6700 0.1295 0.3252 0.1815 390 LYS B NZ 6097 N N . MET B 361 ? 1.7315 1.6505 1.4447 0.0919 0.2364 0.0939 391 MET B N 6098 C CA . MET B 361 ? 1.7570 1.6978 1.4735 0.1010 0.2196 0.0811 391 MET B CA 6099 C C . MET B 361 ? 1.7534 1.6946 1.4392 0.1207 0.2175 0.0854 391 MET B C 6100 O O . MET B 361 ? 1.9238 1.8599 1.5894 0.1262 0.2325 0.0956 391 MET B O 6101 C CB . MET B 361 ? 1.8342 1.7976 1.5709 0.0938 0.2221 0.0713 391 MET B CB 6102 C CG . MET B 361 ? 1.9567 1.9421 1.6926 0.1055 0.2078 0.0595 391 MET B CG 6103 S SD . MET B 361 ? 2.1688 2.1792 1.9384 0.0947 0.2022 0.0438 391 MET B SD 6104 C CE . MET B 361 ? 2.0936 2.1004 1.8839 0.0874 0.1821 0.0351 391 MET B CE 6105 N N . GLU B 362 ? 1.7129 1.6602 1.3954 0.1314 0.1989 0.0775 392 GLU B N 6106 C CA . GLU B 362 ? 1.7343 1.6862 1.3906 0.1512 0.1934 0.0779 392 GLU B CA 6107 C C . GLU B 362 ? 1.6376 1.6155 1.3041 0.1566 0.1811 0.0629 392 GLU B C 6108 O O . GLU B 362 ? 1.6071 1.5977 1.2694 0.1593 0.1894 0.0617 392 GLU B O 6109 C CB . GLU B 362 ? 1.7608 1.6994 1.4045 0.1609 0.1820 0.0803 392 GLU B CB 6110 C CG . GLU B 362 ? 1.8384 1.7503 1.4644 0.1607 0.1948 0.0964 392 GLU B CG 6111 C CD . GLU B 362 ? 1.9089 1.8098 1.5145 0.1763 0.1846 0.0994 392 GLU B CD 6112 O OE1 . GLU B 362 ? 1.8838 1.7980 1.4933 0.1850 0.1670 0.0879 392 GLU B OE1 6113 O OE2 . GLU B 362 ? 1.9603 1.8390 1.5467 0.1800 0.1942 0.1130 392 GLU B OE2 6114 N N . VAL B 363 ? 1.5349 1.5205 1.2158 0.1578 0.1620 0.0513 393 VAL B N 6115 C CA . VAL B 363 ? 1.4764 1.4849 1.1699 0.1620 0.1492 0.0364 393 VAL B CA 6116 C C . VAL B 363 ? 1.4550 1.4728 1.1790 0.1454 0.1493 0.0291 393 VAL B C 6117 O O . VAL B 363 ? 1.4880 1.4973 1.2291 0.1326 0.1469 0.0294 393 VAL B O 6118 C CB . VAL B 363 ? 1.4547 1.4673 1.1510 0.1709 0.1285 0.0269 393 VAL B CB 6119 C CG1 . VAL B 363 ? 1.4144 1.4493 1.1234 0.1757 0.1158 0.0116 393 VAL B CG1 6120 C CG2 . VAL B 363 ? 1.4799 1.4830 1.1476 0.1876 0.1267 0.0332 393 VAL B CG2 6121 N N . GLN B 364 ? 1.4096 1.4456 1.1401 0.1464 0.1516 0.0220 394 GLN B N 6122 C CA . GLN B 364 ? 1.3549 1.4027 1.1143 0.1331 0.1500 0.0132 394 GLN B CA 6123 C C . GLN B 364 ? 1.2653 1.3186 1.0438 0.1314 0.1294 0.0015 394 GLN B C 6124 O O . GLN B 364 ? 1.2341 1.2868 1.0042 0.1419 0.1169 -0.0018 394 GLN B O 6125 C CB . GLN B 364 ? 1.3838 1.4513 1.1443 0.1373 0.1562 0.0072 394 GLN B CB 6126 C CG . GLN B 364 ? 1.4644 1.5282 1.2076 0.1378 0.1784 0.0187 394 GLN B CG 6127 C CD . GLN B 364 ? 1.5221 1.5831 1.2310 0.1560 0.1820 0.0251 394 GLN B CD 6128 O OE1 . GLN B 364 ? 1.5755 1.6208 1.2663 0.1629 0.1786 0.0326 394 GLN B OE1 6129 N NE2 . GLN B 364 ? 1.4893 1.5660 1.1888 0.1642 0.1891 0.0221 394 GLN B NE2 6130 N N . ARG B 365 ? 1.1640 1.2221 0.9681 0.1182 0.1260 -0.0045 395 ARG B N 6131 C CA . ARG B 365 ? 1.1206 1.1809 0.9424 0.1150 0.1079 -0.0136 395 ARG B CA 6132 C C . ARG B 365 ? 1.0805 1.1568 0.9054 0.1261 0.0939 -0.0259 395 ARG B C 6133 O O . ARG B 365 ? 1.0078 1.0992 0.8386 0.1284 0.0957 -0.0326 395 ARG B O 6134 C CB . ARG B 365 ? 1.0869 1.1487 0.9336 0.0993 0.1078 -0.0171 395 ARG B CB 6135 C CG . ARG B 365 ? 1.0448 1.1028 0.9063 0.0937 0.0923 -0.0223 395 ARG B CG 6136 C CD . ARG B 365 ? 1.0066 1.0678 0.8906 0.0801 0.0918 -0.0264 395 ARG B CD 6137 N NE . ARG B 365 ? 0.9715 1.0236 0.8653 0.0727 0.0815 -0.0272 395 ARG B NE 6138 C CZ . ARG B 365 ? 0.9897 1.0464 0.8949 0.0732 0.0661 -0.0351 395 ARG B CZ 6139 N NH1 . ARG B 365 ? 0.9855 1.0556 0.8955 0.0811 0.0576 -0.0440 395 ARG B NH1 6140 N NH2 . ARG B 365 ? 1.0054 1.0525 0.9173 0.0657 0.0593 -0.0341 395 ARG B NH2 6141 N N . ARG B 366 ? 1.0765 1.1500 0.8991 0.1327 0.0798 -0.0296 396 ARG B N 6142 C CA . ARG B 366 ? 1.1034 1.1908 0.9302 0.1432 0.0654 -0.0420 396 ARG B CA 6143 C C . ARG B 366 ? 1.0193 1.1029 0.8591 0.1412 0.0489 -0.0477 396 ARG B C 6144 O O . ARG B 366 ? 0.9745 1.0449 0.8166 0.1331 0.0492 -0.0415 396 ARG B O 6145 C CB . ARG B 366 ? 1.1851 1.2769 0.9876 0.1603 0.0673 -0.0414 396 ARG B CB 6146 C CG . ARG B 366 ? 1.2643 1.3410 1.0471 0.1653 0.0702 -0.0314 396 ARG B CG 6147 C CD . ARG B 366 ? 1.3492 1.4310 1.1137 0.1835 0.0623 -0.0356 396 ARG B CD 6148 N NE . ARG B 366 ? 1.4567 1.5234 1.2062 0.1873 0.0628 -0.0270 396 ARG B NE 6149 C CZ . ARG B 366 ? 1.4637 1.5263 1.2207 0.1880 0.0502 -0.0308 396 ARG B CZ 6150 N NH1 . ARG B 366 ? 1.4504 1.5219 1.2291 0.1851 0.0357 -0.0427 396 ARG B NH1 6151 N NH2 . ARG B 366 ? 1.5258 1.5751 1.2687 0.1918 0.0522 -0.0226 396 ARG B NH2 6152 N N . PRO B 367 ? 0.9880 1.0831 0.8369 0.1483 0.0349 -0.0598 397 PRO B N 6153 C CA . PRO B 367 ? 0.9297 1.0223 0.7884 0.1494 0.0194 -0.0659 397 PRO B CA 6154 C C . PRO B 367 ? 0.9513 1.0364 0.7942 0.1575 0.0179 -0.0616 397 PRO B C 6155 O O . PRO B 367 ? 0.9628 1.0464 0.7847 0.1659 0.0268 -0.0556 397 PRO B O 6156 C CB . PRO B 367 ? 0.9004 1.0083 0.7670 0.1589 0.0078 -0.0796 397 PRO B CB 6157 C CG . PRO B 367 ? 0.9205 1.0381 0.7920 0.1563 0.0151 -0.0818 397 PRO B CG 6158 C CD . PRO B 367 ? 0.9656 1.0769 0.8222 0.1522 0.0334 -0.0694 397 PRO B CD 6159 N N . TRP B 368 ? 0.9665 1.0468 0.8197 0.1548 0.0071 -0.0645 398 TRP B N 6160 C CA . TRP B 368 ? 0.9801 1.0581 0.8231 0.1649 0.0015 -0.0651 398 TRP B CA 6161 C C . TRP B 368 ? 0.9786 1.0614 0.8404 0.1651 -0.0146 -0.0762 398 TRP B C 6162 O O . TRP B 368 ? 0.9516 1.0318 0.8323 0.1536 -0.0191 -0.0780 398 TRP B O 6163 C CB . TRP B 368 ? 0.9902 1.0530 0.8224 0.1605 0.0100 -0.0532 398 TRP B CB 6164 C CG . TRP B 368 ? 0.9996 1.0527 0.8474 0.1457 0.0088 -0.0500 398 TRP B CG 6165 C CD1 . TRP B 368 ? 1.0087 1.0557 0.8642 0.1321 0.0162 -0.0446 398 TRP B CD1 6166 C CD2 . TRP B 368 ? 0.9741 1.0230 0.8307 0.1436 0.0004 -0.0521 398 TRP B CD2 6167 N NE1 . TRP B 368 ? 0.9819 1.0208 0.8487 0.1221 0.0124 -0.0431 398 TRP B NE1 6168 C CE2 . TRP B 368 ? 0.9322 0.9721 0.8000 0.1286 0.0034 -0.0473 398 TRP B CE2 6169 C CE3 . TRP B 368 ? 0.9974 1.0503 0.8545 0.1529 -0.0095 -0.0584 398 TRP B CE3 6170 C CZ2 . TRP B 368 ? 0.8987 0.9334 0.7769 0.1226 -0.0020 -0.0478 398 TRP B CZ2 6171 C CZ3 . TRP B 368 ? 0.9694 1.0175 0.8391 0.1463 -0.0149 -0.0593 398 TRP B CZ3 6172 C CH2 . TRP B 368 ? 0.9008 0.9397 0.7802 0.1313 -0.0107 -0.0536 398 TRP B CH2 6173 N N . LEU B 369 ? 1.0068 1.0966 0.8633 0.1784 -0.0233 -0.0837 399 LEU B N 6174 C CA . LEU B 369 ? 0.9803 1.0778 0.8558 0.1806 -0.0389 -0.0966 399 LEU B CA 6175 C C . LEU B 369 ? 0.9774 1.0706 0.8588 0.1808 -0.0461 -0.0980 399 LEU B C 6176 O O . LEU B 369 ? 0.9693 1.0556 0.8369 0.1835 -0.0404 -0.0905 399 LEU B O 6177 C CB . LEU B 369 ? 1.0004 1.1125 0.8706 0.1958 -0.0458 -0.1082 399 LEU B CB 6178 C CG . LEU B 369 ? 1.0108 1.1300 0.8730 0.1984 -0.0382 -0.1080 399 LEU B CG 6179 C CD1 . LEU B 369 ? 1.0539 1.1883 0.9093 0.2151 -0.0457 -0.1204 399 LEU B CD1 6180 C CD2 . LEU B 369 ? 0.9975 1.1160 0.8804 0.1852 -0.0390 -0.1096 399 LEU B CD2 6181 N N . VAL B 370 ? 0.9617 1.0588 0.8653 0.1774 -0.0582 -0.1078 400 VAL B N 6182 C CA . VAL B 370 ? 0.9617 1.0578 0.8756 0.1774 -0.0660 -0.1118 400 VAL B CA 6183 C C . VAL B 370 ? 0.9780 1.0854 0.9093 0.1835 -0.0807 -0.1275 400 VAL B C 6184 O O . VAL B 370 ? 1.0085 1.1191 0.9517 0.1802 -0.0849 -0.1330 400 VAL B O 6185 C CB . VAL B 370 ? 0.9622 1.0466 0.8894 0.1608 -0.0629 -0.1045 400 VAL B CB 6186 C CG1 . VAL B 370 ? 0.9798 1.0656 0.9229 0.1598 -0.0717 -0.1107 400 VAL B CG1 6187 C CG2 . VAL B 370 ? 0.9511 1.0244 0.8615 0.1560 -0.0493 -0.0905 400 VAL B CG2 6188 N N . LYS B 371 ? 1.0151 1.1288 0.9486 0.1928 -0.0890 -0.1354 401 LYS B N 6189 C CA . LYS B 371 ? 1.0939 1.2185 1.0461 0.1987 -0.1036 -0.1516 401 LYS B CA 6190 C C . LYS B 371 ? 1.0551 1.1747 1.0338 0.1856 -0.1089 -0.1538 401 LYS B C 6191 O O . LYS B 371 ? 1.0231 1.1374 1.0032 0.1808 -0.1057 -0.1484 401 LYS B O 6192 C CB . LYS B 371 ? 1.1818 1.3172 1.1230 0.2165 -0.1103 -0.1603 401 LYS B CB 6193 C CG . LYS B 371 ? 1.2421 1.3913 1.1976 0.2263 -0.1252 -0.1788 401 LYS B CG 6194 C CD . LYS B 371 ? 1.3269 1.4874 1.2650 0.2463 -0.1308 -0.1866 401 LYS B CD 6195 C CE . LYS B 371 ? 1.3732 1.5486 1.3225 0.2578 -0.1455 -0.2059 401 LYS B CE 6196 N NZ . LYS B 371 ? 1.3683 1.5546 1.2921 0.2787 -0.1482 -0.2115 401 LYS B NZ 6197 N N . TYR B 372 ? 1.0765 1.1971 1.0759 0.1799 -0.1166 -0.1614 402 TYR B N 6198 C CA . TYR B 372 ? 1.0832 1.1988 1.1084 0.1678 -0.1218 -0.1638 402 TYR B CA 6199 C C . TYR B 372 ? 1.2014 1.3275 1.2472 0.1747 -0.1364 -0.1813 402 TYR B C 6200 O O . TYR B 372 ? 1.2616 1.3981 1.3036 0.1873 -0.1433 -0.1919 402 TYR B O 6201 C CB . TYR B 372 ? 1.0281 1.1330 1.0620 0.1538 -0.1186 -0.1570 402 TYR B CB 6202 C CG . TYR B 372 ? 1.0137 1.1080 1.0318 0.1451 -0.1051 -0.1409 402 TYR B CG 6203 C CD1 . TYR B 372 ? 0.9748 1.0692 0.9741 0.1484 -0.0974 -0.1350 402 TYR B CD1 6204 C CD2 . TYR B 372 ? 1.0203 1.1050 1.0428 0.1334 -0.0997 -0.1322 402 TYR B CD2 6205 C CE1 . TYR B 372 ? 0.9581 1.0428 0.9448 0.1401 -0.0852 -0.1212 402 TYR B CE1 6206 C CE2 . TYR B 372 ? 0.9698 1.0449 0.9783 0.1257 -0.0879 -0.1186 402 TYR B CE2 6207 C CZ . TYR B 372 ? 0.9233 0.9982 0.9145 0.1290 -0.0810 -0.1133 402 TYR B CZ 6208 O OH . TYR B 372 ? 0.9023 0.9679 0.8815 0.1212 -0.0697 -0.1010 402 TYR B OH 6209 N N . GLY B 373 ? 1.3293 1.4530 1.3974 0.1664 -0.1407 -0.1845 403 GLY B N 6210 C CA . GLY B 373 ? 1.4078 1.5401 1.5007 0.1700 -0.1544 -0.2012 403 GLY B CA 6211 C C . GLY B 373 ? 1.5749 1.7048 1.6817 0.1670 -0.1610 -0.2074 403 GLY B C 6212 O O . GLY B 373 ? 1.5692 1.6867 1.6852 0.1533 -0.1577 -0.1995 403 GLY B O 6213 N N . ASP B 374 ? 1.7500 1.8917 1.8568 0.1809 -0.1707 -0.2217 404 ASP B N 6214 C CA . ASP B 374 ? 1.8624 2.0040 1.9818 0.1814 -0.1785 -0.2304 404 ASP B CA 6215 C C . ASP B 374 ? 1.8029 1.9407 1.9035 0.1816 -0.1709 -0.2215 404 ASP B C 6216 O O . ASP B 374 ? 1.7487 1.8950 1.8454 0.1921 -0.1762 -0.2310 404 ASP B O 6217 C CB . ASP B 374 ? 1.9166 2.0476 2.0663 0.1670 -0.1836 -0.2320 404 ASP B CB 6218 C CG . ASP B 374 ? 1.9097 2.0434 2.0780 0.1712 -0.1961 -0.2469 404 ASP B CG 6219 O OD1 . ASP B 374 ? 1.7975 1.9213 1.9689 0.1647 -0.1953 -0.2422 404 ASP B OD1 6220 O OD2 . ASP B 374 ? 1.8501 1.9959 2.0300 0.1816 -0.2073 -0.2640 404 ASP B OD2 6221 N N . SER B 375 ? 1.6510 1.7771 1.7409 0.1702 -0.1588 -0.2044 405 SER B N 6222 C CA . SER B 375 ? 1.5586 1.6811 1.6330 0.1687 -0.1509 -0.1957 405 SER B CA 6223 C C . SER B 375 ? 1.5182 1.6520 1.5676 0.1830 -0.1463 -0.1968 405 SER B C 6224 O O . SER B 375 ? 1.5250 1.6601 1.5653 0.1844 -0.1418 -0.1943 405 SER B O 6225 C CB . SER B 375 ? 1.4941 1.6028 1.5614 0.1544 -0.1389 -0.1780 405 SER B CB 6226 O OG . SER B 375 ? 1.5277 1.6247 1.6149 0.1412 -0.1421 -0.1755 405 SER B OG 6227 N N . GLY B 376 ? 1.4286 1.5706 1.4667 0.1936 -0.1469 -0.2003 406 GLY B N 6228 C CA . GLY B 376 ? 1.4040 1.5550 1.4155 0.2073 -0.1413 -0.1994 406 GLY B CA 6229 C C . GLY B 376 ? 1.3427 1.4845 1.3336 0.2006 -0.1254 -0.1812 406 GLY B C 6230 O O . GLY B 376 ? 1.2408 1.3710 1.2363 0.1878 -0.1199 -0.1707 406 GLY B O 6231 N N . GLU B 377 ? 1.2893 1.4363 1.2579 0.2091 -0.1177 -0.1778 407 GLU B N 6232 C CA . GLU B 377 ? 1.2958 1.4342 1.2454 0.2031 -0.1022 -0.1613 407 GLU B CA 6233 C C . GLU B 377 ? 1.1892 1.3197 1.1482 0.1889 -0.0968 -0.1544 407 GLU B C 6234 O O . GLU B 377 ? 1.1499 1.2853 1.1198 0.1891 -0.1019 -0.1620 407 GLU B O 6235 C CB . GLU B 377 ? 1.3833 1.5292 1.3053 0.2168 -0.0945 -0.1591 407 GLU B CB 6236 C CG . GLU B 377 ? 1.4839 1.6335 1.3906 0.2299 -0.0971 -0.1609 407 GLU B CG 6237 C CD . GLU B 377 ? 1.5449 1.6928 1.4200 0.2379 -0.0839 -0.1498 407 GLU B CD 6238 O OE1 . GLU B 377 ? 1.6104 1.7653 1.4719 0.2451 -0.0789 -0.1506 407 GLU B OE1 6239 O OE2 . GLU B 377 ? 1.5673 1.7065 1.4313 0.2371 -0.0784 -0.1401 407 GLU B OE2 6240 N N . GLN B 378 ? 1.0665 1.1849 1.0216 0.1770 -0.0871 -0.1407 408 GLN B N 6241 C CA . GLN B 378 ? 0.9686 1.0793 0.9299 0.1640 -0.0812 -0.1333 408 GLN B CA 6242 C C . GLN B 378 ? 0.9566 1.0612 0.8992 0.1600 -0.0660 -0.1195 408 GLN B C 6243 O O . GLN B 378 ? 0.9740 1.0765 0.9002 0.1650 -0.0600 -0.1139 408 GLN B O 6244 C CB . GLN B 378 ? 0.9150 1.0152 0.8953 0.1508 -0.0861 -0.1311 408 GLN B CB 6245 C CG . GLN B 378 ? 0.8884 0.9917 0.8907 0.1519 -0.1005 -0.1436 408 GLN B CG 6246 C CD . GLN B 378 ? 0.8843 0.9922 0.8956 0.1533 -0.1056 -0.1507 408 GLN B CD 6247 O OE1 . GLN B 378 ? 0.8626 0.9691 0.8685 0.1492 -0.0985 -0.1449 408 GLN B OE1 6248 N NE2 . GLN B 378 ? 0.8719 0.9858 0.8984 0.1594 -0.1183 -0.1642 408 GLN B NE2 6249 N N . ILE B 379 ? 0.9314 1.0327 0.8773 0.1511 -0.0602 -0.1147 409 ILE B N 6250 C CA . ILE B 379 ? 0.9113 1.0059 0.8438 0.1448 -0.0459 -0.1022 409 ILE B CA 6251 C C . ILE B 379 ? 0.9022 0.9834 0.8400 0.1324 -0.0441 -0.0939 409 ILE B C 6252 O O . ILE B 379 ? 0.8817 0.9581 0.8350 0.1229 -0.0494 -0.0946 409 ILE B O 6253 C CB . ILE B 379 ? 0.8929 0.9917 0.8289 0.1409 -0.0410 -0.1022 409 ILE B CB 6254 C CG1 . ILE B 379 ? 0.9025 1.0152 0.8285 0.1541 -0.0393 -0.1089 409 ILE B CG1 6255 C CG2 . ILE B 379 ? 0.8935 0.9836 0.8220 0.1308 -0.0275 -0.0900 409 ILE B CG2 6256 C CD1 . ILE B 379 ? 0.9128 1.0335 0.8472 0.1521 -0.0376 -0.1132 409 ILE B CD1 6257 N N . ALA B 380 ? 0.9502 1.0252 0.8742 0.1333 -0.0368 -0.0860 410 ALA B N 6258 C CA . ALA B 380 ? 0.9499 1.0129 0.8773 0.1225 -0.0342 -0.0784 410 ALA B CA 6259 C C . ALA B 380 ? 0.9049 0.9599 0.8274 0.1122 -0.0228 -0.0686 410 ALA B C 6260 O O . ALA B 380 ? 0.9110 0.9570 0.8399 0.1012 -0.0219 -0.0638 410 ALA B O 6261 C CB . ALA B 380 ? 0.9719 1.0322 0.8890 0.1287 -0.0331 -0.0760 410 ALA B CB 6262 N N . GLY B 381 ? 0.8962 0.9548 0.8075 0.1158 -0.0141 -0.0660 411 GLY B N 6263 C CA . GLY B 381 ? 0.8570 0.9099 0.7661 0.1062 -0.0031 -0.0583 411 GLY B CA 6264 C C . GLY B 381 ? 0.8412 0.8988 0.7359 0.1125 0.0078 -0.0553 411 GLY B C 6265 O O . GLY B 381 ? 0.7936 0.8609 0.6816 0.1241 0.0057 -0.0606 411 GLY B O 6266 N N . PHE B 382 ? 0.8464 0.8971 0.7363 0.1047 0.0199 -0.0470 412 PHE B N 6267 C CA . PHE B 382 ? 0.8732 0.9264 0.7501 0.1085 0.0327 -0.0424 412 PHE B CA 6268 C C . PHE B 382 ? 0.8832 0.9233 0.7446 0.1073 0.0441 -0.0313 412 PHE B C 6269 O O . PHE B 382 ? 0.9318 0.9611 0.7966 0.0995 0.0439 -0.0272 412 PHE B O 6270 C CB . PHE B 382 ? 0.8815 0.9402 0.7703 0.0998 0.0376 -0.0440 412 PHE B CB 6271 C CG . PHE B 382 ? 0.8348 0.9075 0.7363 0.1038 0.0278 -0.0551 412 PHE B CG 6272 C CD1 . PHE B 382 ? 0.7720 0.8448 0.6902 0.0991 0.0147 -0.0613 412 PHE B CD1 6273 C CD2 . PHE B 382 ? 0.8155 0.9007 0.7115 0.1126 0.0318 -0.0593 412 PHE B CD2 6274 C CE1 . PHE B 382 ? 0.7617 0.8460 0.6921 0.1033 0.0052 -0.0717 412 PHE B CE1 6275 C CE2 . PHE B 382 ? 0.7992 0.8975 0.7073 0.1171 0.0223 -0.0705 412 PHE B CE2 6276 C CZ . PHE B 382 ? 0.7798 0.8772 0.7056 0.1125 0.0086 -0.0769 412 PHE B CZ 6277 N N . VAL B 383 ? 0.9231 0.9636 0.7667 0.1156 0.0540 -0.0265 413 VAL B N 6278 C CA . VAL B 383 ? 0.9410 0.9674 0.7674 0.1164 0.0652 -0.0151 413 VAL B CA 6279 C C . VAL B 383 ? 0.9646 0.9899 0.7797 0.1162 0.0816 -0.0078 413 VAL B C 6280 O O . VAL B 383 ? 0.9702 1.0071 0.7803 0.1234 0.0841 -0.0111 413 VAL B O 6281 C CB . VAL B 383 ? 0.9361 0.9600 0.7467 0.1301 0.0597 -0.0146 413 VAL B CB 6282 C CG1 . VAL B 383 ? 0.9874 1.0232 0.7852 0.1447 0.0586 -0.0188 413 VAL B CG1 6283 C CG2 . VAL B 383 ? 0.9495 0.9567 0.7445 0.1303 0.0694 -0.0031 413 VAL B CG2 6284 N N . LYS B 384 ? 0.9786 0.9897 0.7904 0.1078 0.0931 0.0017 414 LYS B N 6285 C CA . LYS B 384 ? 1.0696 1.0765 0.8734 0.1046 0.1102 0.0098 414 LYS B CA 6286 C C . LYS B 384 ? 1.1442 1.1326 0.9290 0.1079 0.1184 0.0214 414 LYS B C 6287 O O . LYS B 384 ? 1.1800 1.1561 0.9703 0.1000 0.1179 0.0245 414 LYS B O 6288 C CB . LYS B 384 ? 1.0911 1.0981 0.9154 0.0882 0.1151 0.0086 414 LYS B CB 6289 C CG . LYS B 384 ? 1.1672 1.1744 0.9907 0.0826 0.1324 0.0140 414 LYS B CG 6290 C CD . LYS B 384 ? 1.2081 1.2155 1.0544 0.0664 0.1350 0.0112 414 LYS B CD 6291 C CE . LYS B 384 ? 1.2881 1.3025 1.1408 0.0604 0.1501 0.0125 414 LYS B CE 6292 N NZ . LYS B 384 ? 1.2940 1.3297 1.1624 0.0605 0.1448 0.0013 414 LYS B NZ 6293 N N . GLU B 385 ? 1.1912 1.1771 0.9530 0.1201 0.1255 0.0277 415 GLU B N 6294 C CA . GLU B 385 ? 1.2729 1.2399 1.0147 0.1253 0.1324 0.0392 415 GLU B CA 6295 C C . GLU B 385 ? 1.2905 1.2446 1.0237 0.1191 0.1522 0.0514 415 GLU B C 6296 O O . GLU B 385 ? 1.4003 1.3622 1.1320 0.1182 0.1623 0.0525 415 GLU B O 6297 C CB . GLU B 385 ? 1.3834 1.3526 1.1025 0.1443 0.1263 0.0394 415 GLU B CB 6298 C CG . GLU B 385 ? 1.4138 1.3920 1.1412 0.1505 0.1071 0.0284 415 GLU B CG 6299 C CD . GLU B 385 ? 1.4609 1.4352 1.1669 0.1679 0.1010 0.0302 415 GLU B CD 6300 O OE1 . GLU B 385 ? 1.4403 1.3980 1.1354 0.1696 0.1047 0.0386 415 GLU B OE1 6301 O OE2 . GLU B 385 ? 1.4914 1.4796 1.1924 0.1802 0.0914 0.0221 415 GLU B OE2 6302 N N . PHE B 386 ? 1.2780 1.2123 1.0074 0.1143 0.1578 0.0599 416 PHE B N 6303 C CA . PHE B 386 ? 1.2805 1.1978 0.9987 0.1103 0.1761 0.0729 416 PHE B CA 6304 C C . PHE B 386 ? 1.3384 1.2376 1.0320 0.1226 0.1764 0.0823 416 PHE B C 6305 O O . PHE B 386 ? 1.2986 1.2006 0.9864 0.1334 0.1625 0.0777 416 PHE B O 6306 C CB . PHE B 386 ? 1.2695 1.1770 1.0078 0.0923 0.1824 0.0740 416 PHE B CB 6307 C CG . PHE B 386 ? 1.2396 1.1633 1.0033 0.0797 0.1816 0.0646 416 PHE B CG 6308 C CD1 . PHE B 386 ? 1.2730 1.2020 1.0412 0.0734 0.1960 0.0671 416 PHE B CD1 6309 C CD2 . PHE B 386 ? 1.2059 1.1395 0.9892 0.0741 0.1668 0.0534 416 PHE B CD2 6310 C CE1 . PHE B 386 ? 1.2645 1.2096 1.0574 0.0625 0.1944 0.0574 416 PHE B CE1 6311 C CE2 . PHE B 386 ? 1.1734 1.1213 0.9793 0.0636 0.1650 0.0447 416 PHE B CE2 6312 C CZ . PHE B 386 ? 1.2123 1.1664 1.0236 0.0580 0.1783 0.0462 416 PHE B CZ 6313 N N . SER B 387 ? 1.4246 1.3049 1.1051 0.1209 0.1923 0.0955 417 SER B N 6314 C CA . SER B 387 ? 1.4945 1.3556 1.1497 0.1332 0.1942 0.1059 417 SER B CA 6315 C C . SER B 387 ? 1.4777 1.3285 1.1429 0.1298 0.1842 0.1029 417 SER B C 6316 O O . SER B 387 ? 1.4180 1.2584 1.0982 0.1157 0.1900 0.1044 417 SER B O 6317 C CB . SER B 387 ? 1.5172 1.3594 1.1590 0.1296 0.2153 0.1211 417 SER B CB 6318 O OG . SER B 387 ? 1.5701 1.3950 1.1814 0.1449 0.2188 0.1329 417 SER B OG 6319 N N . HIS B 388 ? 1.4566 1.3125 1.1152 0.1425 0.1690 0.0974 418 HIS B N 6320 C CA . HIS B 388 ? 1.4694 1.3179 1.1365 0.1413 0.1589 0.0937 418 HIS B CA 6321 C C . HIS B 388 ? 1.3902 1.2507 1.0863 0.1273 0.1500 0.0819 418 HIS B C 6322 O O . HIS B 388 ? 1.3969 1.2538 1.1010 0.1258 0.1417 0.0779 418 HIS B O 6323 C CB . HIS B 388 ? 1.5657 1.3877 1.2247 0.1383 0.1697 0.1052 418 HIS B CB 6324 C CG . HIS B 388 ? 1.6499 1.4564 1.2783 0.1537 0.1767 0.1177 418 HIS B CG 6325 N ND1 . HIS B 388 ? 1.7612 1.5589 1.3749 0.1535 0.1931 0.1292 418 HIS B ND1 6326 C CD2 . HIS B 388 ? 1.6807 1.4792 1.2900 0.1703 0.1694 0.1205 418 HIS B CD2 6327 C CE1 . HIS B 388 ? 1.8360 1.6195 1.4207 0.1696 0.1958 0.1395 418 HIS B CE1 6328 N NE2 . HIS B 388 ? 1.8099 1.5938 1.3916 0.1805 0.1809 0.1341 418 HIS B NE2 6329 N N . ILE B 389 ? 1.3314 1.2063 1.0428 0.1175 0.1517 0.0764 419 ILE B N 6330 C CA . ILE B 389 ? 1.2285 1.1143 0.9655 0.1052 0.1429 0.0657 419 ILE B CA 6331 C C . ILE B 389 ? 1.1688 1.0769 0.9164 0.1050 0.1361 0.0563 419 ILE B C 6332 O O . ILE B 389 ? 1.1344 1.0487 0.8807 0.1034 0.1445 0.0579 419 ILE B O 6333 C CB . ILE B 389 ? 1.1971 1.0724 0.9485 0.0885 0.1524 0.0683 419 ILE B CB 6334 C CG1 . ILE B 389 ? 1.1561 1.0410 0.9308 0.0776 0.1419 0.0577 419 ILE B CG1 6335 C CG2 . ILE B 389 ? 1.2358 1.1129 0.9892 0.0817 0.1664 0.0724 419 ILE B CG2 6336 C CD1 . ILE B 389 ? 1.1785 1.0503 0.9643 0.0643 0.1478 0.0593 419 ILE B CD1 6337 N N . ALA B 390 ? 1.1505 1.0703 0.9091 0.1064 0.1209 0.0463 420 ALA B N 6338 C CA . ALA B 390 ? 1.0907 1.0305 0.8605 0.1070 0.1119 0.0362 420 ALA B CA 6339 C C . ALA B 390 ? 1.0387 0.9838 0.8321 0.0937 0.1049 0.0287 420 ALA B C 6340 O O . ALA B 390 ? 0.9872 0.9245 0.7860 0.0891 0.1010 0.0285 420 ALA B O 6341 C CB . ALA B 390 ? 1.0688 1.0173 0.8309 0.1216 0.0993 0.0306 420 ALA B CB 6342 N N . PHE B 391 ? 1.0671 1.0253 0.8738 0.0880 0.1034 0.0226 421 PHE B N 6343 C CA . PHE B 391 ? 1.0525 1.0181 0.8799 0.0785 0.0934 0.0143 421 PHE B CA 6344 C C . PHE B 391 ? 1.0223 1.0036 0.8553 0.0856 0.0805 0.0050 421 PHE B C 6345 O O . PHE B 391 ? 1.0483 1.0392 0.8754 0.0935 0.0815 0.0030 421 PHE B O 6346 C CB . PHE B 391 ? 1.0473 1.0157 0.8892 0.0657 0.0996 0.0131 421 PHE B CB 6347 C CG . PHE B 391 ? 1.0155 0.9909 0.8762 0.0575 0.0886 0.0049 421 PHE B CG 6348 C CD1 . PHE B 391 ? 0.9760 0.9427 0.8419 0.0506 0.0844 0.0050 421 PHE B CD1 6349 C CD2 . PHE B 391 ? 0.9695 0.9599 0.8414 0.0577 0.0819 -0.0029 421 PHE B CD2 6350 C CE1 . PHE B 391 ? 0.9319 0.9041 0.8126 0.0438 0.0744 -0.0014 421 PHE B CE1 6351 C CE2 . PHE B 391 ? 0.9230 0.9180 0.8105 0.0510 0.0713 -0.0095 421 PHE B CE2 6352 C CZ . PHE B 391 ? 0.9158 0.9015 0.8070 0.0440 0.0678 -0.0083 421 PHE B CZ 6353 N N . LEU B 392 ? 0.9862 0.9700 0.8310 0.0824 0.0687 -0.0008 422 LEU B N 6354 C CA . LEU B 392 ? 0.9698 0.9662 0.8204 0.0894 0.0560 -0.0095 422 LEU B CA 6355 C C . LEU B 392 ? 0.8999 0.8988 0.7686 0.0804 0.0458 -0.0154 422 LEU B C 6356 O O . LEU B 392 ? 0.8783 0.8683 0.7501 0.0731 0.0461 -0.0126 422 LEU B O 6357 C CB . LEU B 392 ? 0.9956 0.9903 0.8337 0.1017 0.0516 -0.0091 422 LEU B CB 6358 C CG . LEU B 392 ? 0.9813 0.9873 0.8251 0.1100 0.0378 -0.0185 422 LEU B CG 6359 C CD1 . LEU B 392 ? 1.0210 1.0289 0.8472 0.1257 0.0375 -0.0179 422 LEU B CD1 6360 C CD2 . LEU B 392 ? 0.9814 0.9846 0.8374 0.1045 0.0291 -0.0215 422 LEU B CD2 6361 N N . THR B 393 ? 0.8675 0.8780 0.7476 0.0811 0.0373 -0.0233 423 THR B N 6362 C CA . THR B 393 ? 0.8048 0.8169 0.7009 0.0736 0.0272 -0.0283 423 THR B CA 6363 C C . THR B 393 ? 0.8098 0.8272 0.7105 0.0804 0.0152 -0.0347 423 THR B C 6364 O O . THR B 393 ? 0.8832 0.9069 0.7770 0.0917 0.0129 -0.0378 423 THR B O 6365 C CB . THR B 393 ? 0.8059 0.8262 0.7145 0.0689 0.0246 -0.0334 423 THR B CB 6366 O OG1 . THR B 393 ? 0.7789 0.8110 0.6874 0.0787 0.0205 -0.0397 423 THR B OG1 6367 C CG2 . THR B 393 ? 0.8299 0.8472 0.7381 0.0612 0.0359 -0.0290 423 THR B CG2 6368 N N . ILE B 394 ? 0.7724 0.7871 0.6848 0.0735 0.0076 -0.0368 424 ILE B N 6369 C CA . ILE B 394 ? 0.7395 0.7591 0.6608 0.0775 -0.0040 -0.0435 424 ILE B CA 6370 C C . ILE B 394 ? 0.7181 0.7405 0.6545 0.0715 -0.0121 -0.0483 424 ILE B C 6371 O O . ILE B 394 ? 0.7150 0.7308 0.6576 0.0618 -0.0133 -0.0457 424 ILE B O 6372 C CB . ILE B 394 ? 0.7411 0.7542 0.6627 0.0755 -0.0055 -0.0413 424 ILE B CB 6373 C CG1 . ILE B 394 ? 0.7718 0.7829 0.6789 0.0840 0.0002 -0.0380 424 ILE B CG1 6374 C CG2 . ILE B 394 ? 0.7638 0.7822 0.6982 0.0778 -0.0172 -0.0487 424 ILE B CG2 6375 C CD1 . ILE B 394 ? 0.8156 0.8173 0.7106 0.0804 0.0124 -0.0293 424 ILE B CD1 6376 N N . LYS B 395 ? 0.6926 0.7248 0.6341 0.0781 -0.0180 -0.0555 425 LYS B N 6377 C CA . LYS B 395 ? 0.6839 0.7189 0.6388 0.0741 -0.0253 -0.0602 425 LYS B CA 6378 C C . LYS B 395 ? 0.6902 0.7194 0.6564 0.0687 -0.0344 -0.0615 425 LYS B C 6379 O O . LYS B 395 ? 0.7116 0.7419 0.6807 0.0728 -0.0394 -0.0646 425 LYS B O 6380 C CB . LYS B 395 ? 0.6897 0.7366 0.6477 0.0838 -0.0303 -0.0688 425 LYS B CB 6381 C CG . LYS B 395 ? 0.6846 0.7350 0.6567 0.0812 -0.0382 -0.0745 425 LYS B CG 6382 C CD . LYS B 395 ? 0.6876 0.7511 0.6605 0.0909 -0.0397 -0.0825 425 LYS B CD 6383 C CE . LYS B 395 ? 0.6922 0.7623 0.6653 0.1019 -0.0472 -0.0903 425 LYS B CE 6384 N NZ . LYS B 395 ? 0.7017 0.7679 0.6902 0.0998 -0.0599 -0.0955 425 LYS B NZ 6385 N N . GLY B 396 ? 0.7149 0.7382 0.6874 0.0595 -0.0361 -0.0590 426 GLY B N 6386 C CA . GLY B 396 ? 0.7068 0.7231 0.6887 0.0535 -0.0436 -0.0587 426 GLY B CA 6387 C C . GLY B 396 ? 0.7169 0.7253 0.6944 0.0483 -0.0395 -0.0528 426 GLY B C 6388 O O . GLY B 396 ? 0.7180 0.7221 0.7033 0.0448 -0.0449 -0.0530 426 GLY B O 6389 N N . ALA B 397 ? 0.7372 0.7436 0.7029 0.0478 -0.0297 -0.0476 427 ALA B N 6390 C CA . ALA B 397 ? 0.7424 0.7416 0.7038 0.0430 -0.0252 -0.0423 427 ALA B CA 6391 C C . ALA B 397 ? 0.7431 0.7343 0.6989 0.0340 -0.0189 -0.0361 427 ALA B C 6392 O O . ALA B 397 ? 0.7787 0.7707 0.7309 0.0328 -0.0148 -0.0351 427 ALA B O 6393 C CB . ALA B 397 ? 0.7286 0.7303 0.6808 0.0505 -0.0197 -0.0418 427 ALA B CB 6394 N N . GLY B 398 ? 0.7383 0.7226 0.6940 0.0275 -0.0180 -0.0324 428 GLY B N 6395 C CA . GLY B 398 ? 0.7545 0.7314 0.7048 0.0191 -0.0131 -0.0274 428 GLY B CA 6396 C C . GLY B 398 ? 0.7640 0.7374 0.7043 0.0191 -0.0035 -0.0237 428 GLY B C 6397 O O . GLY B 398 ? 0.7675 0.7440 0.7030 0.0261 0.0002 -0.0243 428 GLY B O 6398 N N . HIS B 399 ? 0.7876 0.7539 0.7240 0.0116 0.0000 -0.0199 429 HIS B N 6399 C CA . HIS B 399 ? 0.7923 0.7535 0.7199 0.0104 0.0088 -0.0167 429 HIS B CA 6400 C C . HIS B 399 ? 0.7866 0.7492 0.7124 0.0163 0.0108 -0.0169 429 HIS B C 6401 O O . HIS B 399 ? 0.7959 0.7556 0.7141 0.0194 0.0175 -0.0150 429 HIS B O 6402 C CB . HIS B 399 ? 0.8147 0.7691 0.7396 0.0016 0.0103 -0.0141 429 HIS B CB 6403 C CG . HIS B 399 ? 0.8460 0.7946 0.7628 -0.0006 0.0188 -0.0118 429 HIS B CG 6404 N ND1 . HIS B 399 ? 0.8733 0.8205 0.7873 -0.0008 0.0237 -0.0116 429 HIS B ND1 6405 C CD2 . HIS B 399 ? 0.8864 0.8300 0.7983 -0.0032 0.0234 -0.0101 429 HIS B CD2 6406 C CE1 . HIS B 399 ? 0.9364 0.8769 0.8443 -0.0034 0.0307 -0.0098 429 HIS B CE1 6407 N NE2 . HIS B 399 ? 0.9104 0.8489 0.8166 -0.0044 0.0304 -0.0091 429 HIS B NE2 6408 N N . MET B 400 ? 0.8144 0.7810 0.7480 0.0179 0.0047 -0.0195 430 MET B N 6409 C CA . MET B 400 ? 0.8241 0.7936 0.7587 0.0233 0.0055 -0.0211 430 MET B CA 6410 C C . MET B 400 ? 0.8098 0.7878 0.7503 0.0320 -0.0008 -0.0262 430 MET B C 6411 O O . MET B 400 ? 0.9029 0.8849 0.8544 0.0317 -0.0077 -0.0299 430 MET B O 6412 C CB . MET B 400 ? 0.8724 0.8403 0.8124 0.0172 0.0051 -0.0205 430 MET B CB 6413 C CG . MET B 400 ? 0.9382 0.8988 0.8698 0.0112 0.0126 -0.0163 430 MET B CG 6414 S SD . MET B 400 ? 1.0210 0.9784 0.9559 0.0013 0.0129 -0.0142 430 MET B SD 6415 C CE . MET B 400 ? 1.0022 0.9673 0.9489 0.0051 0.0108 -0.0182 430 MET B CE 6416 N N . VAL B 401 ? 0.7876 0.7675 0.7203 0.0398 0.0017 -0.0264 431 VAL B N 6417 C CA . VAL B 401 ? 0.7758 0.7641 0.7107 0.0494 -0.0036 -0.0314 431 VAL B CA 6418 C C . VAL B 401 ? 0.7812 0.7761 0.7249 0.0547 -0.0100 -0.0371 431 VAL B C 6419 O O . VAL B 401 ? 0.7857 0.7865 0.7404 0.0559 -0.0181 -0.0426 431 VAL B O 6420 C CB . VAL B 401 ? 0.8242 0.8120 0.7456 0.0572 0.0026 -0.0290 431 VAL B CB 6421 C CG1 . VAL B 401 ? 0.8426 0.8393 0.7627 0.0696 -0.0022 -0.0343 431 VAL B CG1 6422 C CG2 . VAL B 401 ? 0.8180 0.8031 0.7361 0.0523 0.0069 -0.0261 431 VAL B CG2 6423 N N . PRO B 402 ? 0.7838 0.7782 0.7245 0.0579 -0.0069 -0.0366 432 PRO B N 6424 C CA . PRO B 402 ? 0.7643 0.7669 0.7153 0.0636 -0.0133 -0.0434 432 PRO B CA 6425 C C . PRO B 402 ? 0.7951 0.8000 0.7635 0.0557 -0.0190 -0.0468 432 PRO B C 6426 O O . PRO B 402 ? 0.8915 0.9045 0.8719 0.0601 -0.0258 -0.0540 432 PRO B O 6427 C CB . PRO B 402 ? 0.7804 0.7804 0.7256 0.0659 -0.0077 -0.0413 432 PRO B CB 6428 C CG . PRO B 402 ? 0.8181 0.8091 0.7468 0.0661 0.0007 -0.0341 432 PRO B CG 6429 C CD . PRO B 402 ? 0.7958 0.7824 0.7249 0.0568 0.0020 -0.0308 432 PRO B CD 6430 N N . THR B 403 ? 0.7610 0.7585 0.7305 0.0443 -0.0160 -0.0417 433 THR B N 6431 C CA . THR B 403 ? 0.7517 0.7488 0.7356 0.0362 -0.0205 -0.0430 433 THR B CA 6432 C C . THR B 403 ? 0.7366 0.7353 0.7274 0.0370 -0.0285 -0.0463 433 THR B C 6433 O O . THR B 403 ? 0.7300 0.7331 0.7353 0.0376 -0.0355 -0.0520 433 THR B O 6434 C CB . THR B 403 ? 0.7360 0.7238 0.7156 0.0246 -0.0146 -0.0356 433 THR B CB 6435 O OG1 . THR B 403 ? 0.7149 0.7004 0.6860 0.0243 -0.0066 -0.0326 433 THR B OG1 6436 C CG2 . THR B 403 ? 0.7071 0.6934 0.6999 0.0165 -0.0176 -0.0357 433 THR B CG2 6437 N N . ASP B 404 ? 0.7365 0.7318 0.7183 0.0368 -0.0272 -0.0433 434 ASP B N 6438 C CA . ASP B 404 ? 0.7444 0.7414 0.7322 0.0381 -0.0345 -0.0467 434 ASP B CA 6439 C C . ASP B 404 ? 0.7411 0.7484 0.7326 0.0499 -0.0405 -0.0551 434 ASP B C 6440 O O . ASP B 404 ? 0.6874 0.6982 0.6913 0.0515 -0.0489 -0.0612 434 ASP B O 6441 C CB . ASP B 404 ? 0.7696 0.7618 0.7477 0.0350 -0.0311 -0.0420 434 ASP B CB 6442 C CG . ASP B 404 ? 0.8217 0.8043 0.7959 0.0241 -0.0267 -0.0349 434 ASP B CG 6443 O OD1 . ASP B 404 ? 0.8089 0.7875 0.7900 0.0179 -0.0287 -0.0335 434 ASP B OD1 6444 O OD2 . ASP B 404 ? 0.8378 0.8168 0.8020 0.0217 -0.0210 -0.0309 434 ASP B OD2 6445 N N . LYS B 405 ? 0.7400 0.7516 0.7205 0.0584 -0.0364 -0.0555 435 LYS B N 6446 C CA . LYS B 405 ? 0.7944 0.8158 0.7743 0.0709 -0.0414 -0.0630 435 LYS B CA 6447 C C . LYS B 405 ? 0.8358 0.8608 0.8091 0.0789 -0.0389 -0.0640 435 LYS B C 6448 O O . LYS B 405 ? 0.8692 0.8935 0.8266 0.0854 -0.0331 -0.0606 435 LYS B O 6449 C CB . LYS B 405 ? 0.8087 0.8317 0.7771 0.0759 -0.0387 -0.0618 435 LYS B CB 6450 C CG . LYS B 405 ? 0.7948 0.8151 0.7686 0.0693 -0.0409 -0.0611 435 LYS B CG 6451 C CD . LYS B 405 ? 0.7896 0.8148 0.7790 0.0711 -0.0521 -0.0695 435 LYS B CD 6452 C CE . LYS B 405 ? 0.8068 0.8280 0.8010 0.0648 -0.0545 -0.0682 435 LYS B CE 6453 N NZ . LYS B 405 ? 0.8024 0.8286 0.8100 0.0690 -0.0652 -0.0771 435 LYS B NZ 6454 N N . PRO B 406 ? 0.8264 0.8550 0.8120 0.0786 -0.0430 -0.0687 436 PRO B N 6455 C CA . PRO B 406 ? 0.7900 0.8229 0.7707 0.0868 -0.0415 -0.0705 436 PRO B CA 6456 C C . PRO B 406 ? 0.8093 0.8503 0.7805 0.1021 -0.0454 -0.0759 436 PRO B C 6457 O O . PRO B 406 ? 0.7430 0.7820 0.6977 0.1095 -0.0401 -0.0720 436 PRO B O 6458 C CB . PRO B 406 ? 0.7954 0.8333 0.7960 0.0832 -0.0468 -0.0768 436 PRO B CB 6459 C CG . PRO B 406 ? 0.7910 0.8265 0.8064 0.0738 -0.0513 -0.0781 436 PRO B CG 6460 C CD . PRO B 406 ? 0.8100 0.8374 0.8143 0.0692 -0.0476 -0.0710 436 PRO B CD 6461 N N . LEU B 407 ? 0.8306 0.8798 0.8110 0.1074 -0.0546 -0.0848 437 LEU B N 6462 C CA . LEU B 407 ? 0.8740 0.9324 0.8454 0.1230 -0.0593 -0.0914 437 LEU B CA 6463 C C . LEU B 407 ? 0.8719 0.9261 0.8204 0.1281 -0.0514 -0.0840 437 LEU B C 6464 O O . LEU B 407 ? 0.8739 0.9293 0.8062 0.1392 -0.0488 -0.0825 437 LEU B O 6465 C CB . LEU B 407 ? 0.8732 0.9411 0.8589 0.1273 -0.0707 -0.1031 437 LEU B CB 6466 C CG . LEU B 407 ? 0.8887 0.9673 0.8644 0.1444 -0.0764 -0.1111 437 LEU B CG 6467 C CD1 . LEU B 407 ? 0.9420 1.0254 0.9125 0.1544 -0.0779 -0.1140 437 LEU B CD1 6468 C CD2 . LEU B 407 ? 0.9030 0.9910 0.8958 0.1478 -0.0884 -0.1241 437 LEU B CD2 6469 N N . ALA B 408 ? 0.8480 0.8971 0.7957 0.1199 -0.0473 -0.0791 438 ALA B N 6470 C CA . ALA B 408 ? 0.8872 0.9321 0.8163 0.1222 -0.0383 -0.0717 438 ALA B CA 6471 C C . ALA B 408 ? 0.9016 0.9366 0.8166 0.1203 -0.0280 -0.0617 438 ALA B C 6472 O O . ALA B 408 ? 0.9444 0.9773 0.8414 0.1282 -0.0217 -0.0571 438 ALA B O 6473 C CB . ALA B 408 ? 0.9089 0.9506 0.8434 0.1121 -0.0363 -0.0691 438 ALA B CB 6474 N N . ALA B 409 ? 0.8952 0.9238 0.8184 0.1101 -0.0260 -0.0585 439 ALA B N 6475 C CA . ALA B 409 ? 0.8841 0.9030 0.7962 0.1079 -0.0168 -0.0501 439 ALA B CA 6476 C C . ALA B 409 ? 0.9017 0.9232 0.8047 0.1208 -0.0180 -0.0519 439 ALA B C 6477 O O . ALA B 409 ? 0.9098 0.9236 0.7964 0.1249 -0.0103 -0.0449 439 ALA B O 6478 C CB . ALA B 409 ? 0.8709 0.8844 0.7945 0.0952 -0.0155 -0.0480 439 ALA B CB 6479 N N . PHE B 410 ? 0.9214 0.9533 0.8356 0.1273 -0.0280 -0.0615 440 PHE B N 6480 C CA . PHE B 410 ? 0.9327 0.9690 0.8396 0.1410 -0.0312 -0.0650 440 PHE B CA 6481 C C . PHE B 410 ? 0.9218 0.9596 0.8085 0.1547 -0.0303 -0.0638 440 PHE B C 6482 O O . PHE B 410 ? 0.8870 0.9190 0.7558 0.1633 -0.0254 -0.0583 440 PHE B O 6483 C CB . PHE B 410 ? 0.9340 0.9829 0.8606 0.1445 -0.0430 -0.0774 440 PHE B CB 6484 C CG . PHE B 410 ? 0.9796 1.0344 0.9008 0.1588 -0.0475 -0.0824 440 PHE B CG 6485 C CD1 . PHE B 410 ? 1.0397 1.0904 0.9611 0.1579 -0.0438 -0.0795 440 PHE B CD1 6486 C CD2 . PHE B 410 ? 1.0170 1.0817 0.9319 0.1741 -0.0557 -0.0902 440 PHE B CD2 6487 C CE1 . PHE B 410 ? 1.0714 1.1276 0.9877 0.1722 -0.0487 -0.0844 440 PHE B CE1 6488 C CE2 . PHE B 410 ? 1.0556 1.1259 0.9643 0.1887 -0.0608 -0.0951 440 PHE B CE2 6489 C CZ . PHE B 410 ? 1.1088 1.1747 1.0185 0.1878 -0.0575 -0.0922 440 PHE B CZ 6490 N N . THR B 411 ? 0.9346 0.9796 0.8237 0.1568 -0.0347 -0.0688 441 THR B N 6491 C CA . THR B 411 ? 0.9864 1.0344 0.8564 0.1696 -0.0334 -0.0682 441 THR B CA 6492 C C . THR B 411 ? 1.0060 1.0412 0.8553 0.1681 -0.0196 -0.0549 441 THR B C 6493 O O . THR B 411 ? 1.0981 1.1301 0.9270 0.1800 -0.0160 -0.0507 441 THR B O 6494 C CB . THR B 411 ? 0.9514 1.0079 0.8286 0.1688 -0.0379 -0.0745 441 THR B CB 6495 O OG1 . THR B 411 ? 0.9764 1.0444 0.8725 0.1717 -0.0512 -0.0877 441 THR B OG1 6496 C CG2 . THR B 411 ? 0.9519 1.0116 0.8080 0.1813 -0.0345 -0.0731 441 THR B CG2 6497 N N . MET B 412 ? 0.9946 1.0222 0.8495 0.1535 -0.0123 -0.0487 442 MET B N 6498 C CA . MET B 412 ? 1.0167 1.0321 0.8566 0.1493 0.0009 -0.0370 442 MET B CA 6499 C C . MET B 412 ? 1.0383 1.0434 0.8655 0.1543 0.0057 -0.0305 442 MET B C 6500 O O . MET B 412 ? 1.0732 1.0713 0.8803 0.1622 0.0130 -0.0233 442 MET B O 6501 C CB . MET B 412 ? 1.0035 1.0132 0.8564 0.1320 0.0053 -0.0336 442 MET B CB 6502 C CG . MET B 412 ? 1.0355 1.0317 0.8776 0.1251 0.0186 -0.0226 442 MET B CG 6503 S SD . MET B 412 ? 1.0310 1.0201 0.8888 0.1066 0.0210 -0.0203 442 MET B SD 6504 C CE . MET B 412 ? 1.0361 1.0219 0.8979 0.1077 0.0171 -0.0217 442 MET B CE 6505 N N . PHE B 413 ? 1.0377 1.0420 0.8773 0.1497 0.0016 -0.0332 443 PHE B N 6506 C CA . PHE B 413 ? 1.0274 1.0227 0.8590 0.1534 0.0051 -0.0287 443 PHE B CA 6507 C C . PHE B 413 ? 1.0387 1.0371 0.8551 0.1720 0.0007 -0.0306 443 PHE B C 6508 O O . PHE B 413 ? 1.0291 1.0164 0.8266 0.1788 0.0075 -0.0224 443 PHE B O 6509 C CB . PHE B 413 ? 1.0263 1.0242 0.8775 0.1449 0.0002 -0.0337 443 PHE B CB 6510 C CG . PHE B 413 ? 1.0272 1.0185 0.8738 0.1490 0.0024 -0.0313 443 PHE B CG 6511 C CD1 . PHE B 413 ? 1.0267 1.0028 0.8624 0.1444 0.0131 -0.0215 443 PHE B CD1 6512 C CD2 . PHE B 413 ? 1.0400 1.0407 0.8944 0.1576 -0.0064 -0.0396 443 PHE B CD2 6513 C CE1 . PHE B 413 ? 1.0662 1.0357 0.8978 0.1490 0.0147 -0.0198 443 PHE B CE1 6514 C CE2 . PHE B 413 ? 1.0695 1.0649 0.9204 0.1623 -0.0048 -0.0382 443 PHE B CE2 6515 C CZ . PHE B 413 ? 1.0890 1.0684 0.9280 0.1582 0.0056 -0.0281 443 PHE B CZ 6516 N N . SER B 414 ? 1.0733 1.0864 0.8979 0.1804 -0.0110 -0.0417 444 SER B N 6517 C CA . SER B 414 ? 1.1313 1.1500 0.9418 0.1995 -0.0174 -0.0456 444 SER B CA 6518 C C . SER B 414 ? 1.1605 1.1728 0.9441 0.2090 -0.0099 -0.0373 444 SER B C 6519 O O . SER B 414 ? 1.1621 1.1678 0.9256 0.2220 -0.0080 -0.0324 444 SER B O 6520 C CB . SER B 414 ? 1.1609 1.1976 0.9863 0.2054 -0.0312 -0.0601 444 SER B CB 6521 O OG . SER B 414 ? 1.2402 1.2832 1.0528 0.2243 -0.0386 -0.0652 444 SER B OG 6522 N N . ARG B 415 ? 1.1562 1.1705 0.9399 0.2028 -0.0055 -0.0358 445 ARG B N 6523 C CA . ARG B 415 ? 1.1939 1.2031 0.9540 0.2095 0.0035 -0.0276 445 ARG B CA 6524 C C . ARG B 415 ? 1.2160 1.2060 0.9620 0.2037 0.0183 -0.0129 445 ARG B C 6525 O O . ARG B 415 ? 1.3249 1.3074 1.0479 0.2118 0.0267 -0.0043 445 ARG B O 6526 C CB . ARG B 415 ? 1.1665 1.1848 0.9342 0.2034 0.0042 -0.0313 445 ARG B CB 6527 C CG . ARG B 415 ? 1.1998 1.2359 0.9769 0.2123 -0.0099 -0.0457 445 ARG B CG 6528 C CD . ARG B 415 ? 1.1812 1.2265 0.9712 0.2049 -0.0112 -0.0513 445 ARG B CD 6529 N NE . ARG B 415 ? 1.1911 1.2526 0.9878 0.2156 -0.0247 -0.0654 445 ARG B NE 6530 C CZ . ARG B 415 ? 1.2349 1.3069 1.0439 0.2130 -0.0296 -0.0736 445 ARG B CZ 6531 N NH1 . ARG B 415 ? 1.1689 1.2377 0.9849 0.2002 -0.0222 -0.0693 445 ARG B NH1 6532 N NH2 . ARG B 415 ? 1.3043 1.3903 1.1192 0.2239 -0.0425 -0.0872 445 ARG B NH2 6533 N N . PHE B 416 ? 1.1834 1.1655 0.9434 0.1896 0.0217 -0.0102 446 PHE B N 6534 C CA . PHE B 416 ? 1.1839 1.1476 0.9344 0.1829 0.0346 0.0020 446 PHE B CA 6535 C C . PHE B 416 ? 1.2463 1.2008 0.9821 0.1955 0.0337 0.0057 446 PHE B C 6536 O O . PHE B 416 ? 1.2554 1.1972 0.9689 0.2031 0.0423 0.0158 446 PHE B O 6537 C CB . PHE B 416 ? 1.1193 1.0796 0.8905 0.1645 0.0368 0.0016 446 PHE B CB 6538 C CG . PHE B 416 ? 1.0976 1.0398 0.8631 0.1580 0.0473 0.0113 446 PHE B CG 6539 C CD1 . PHE B 416 ? 1.1366 1.0668 0.8917 0.1527 0.0604 0.0212 446 PHE B CD1 6540 C CD2 . PHE B 416 ? 1.0706 1.0083 0.8431 0.1564 0.0444 0.0097 446 PHE B CD2 6541 C CE1 . PHE B 416 ? 1.1292 1.0421 0.8808 0.1463 0.0696 0.0292 446 PHE B CE1 6542 C CE2 . PHE B 416 ? 1.0658 0.9869 0.8340 0.1505 0.0535 0.0175 446 PHE B CE2 6543 C CZ . PHE B 416 ? 1.1007 1.0089 0.8586 0.1455 0.0658 0.0271 446 PHE B CZ 6544 N N . LEU B 417 ? 1.2765 1.2377 1.0252 0.1979 0.0234 -0.0025 447 LEU B N 6545 C CA . LEU B 417 ? 1.3462 1.3013 1.0842 0.2110 0.0203 -0.0014 447 LEU B CA 6546 C C . LEU B 417 ? 1.3969 1.3514 1.1093 0.2305 0.0188 0.0013 447 LEU B C 6547 O O . LEU B 417 ? 1.4495 1.3900 1.1427 0.2402 0.0231 0.0095 447 LEU B O 6548 C CB . LEU B 417 ? 1.3023 1.2710 1.0605 0.2127 0.0074 -0.0140 447 LEU B CB 6549 C CG . LEU B 417 ? 1.2952 1.2607 1.0728 0.1986 0.0091 -0.0152 447 LEU B CG 6550 C CD1 . LEU B 417 ? 1.2641 1.2417 1.0559 0.2053 -0.0023 -0.0263 447 LEU B CD1 6551 C CD2 . LEU B 417 ? 1.3079 1.2534 1.0743 0.1946 0.0206 -0.0038 447 LEU B CD2 6552 N N . ASN B 418 ? 1.4257 1.3947 1.1370 0.2368 0.0125 -0.0055 448 ASN B N 6553 C CA . ASN B 418 ? 1.4518 1.4233 1.1387 0.2566 0.0093 -0.0048 448 ASN B CA 6554 C C . ASN B 418 ? 1.4490 1.4115 1.1130 0.2578 0.0223 0.0067 448 ASN B C 6555 O O . ASN B 418 ? 1.4890 1.4588 1.1366 0.2713 0.0196 0.0049 448 ASN B O 6556 C CB . ASN B 418 ? 1.4175 1.4113 1.1159 0.2650 -0.0060 -0.0208 448 ASN B CB 6557 C CG . ASN B 418 ? 1.3766 1.3797 1.0954 0.2668 -0.0187 -0.0323 448 ASN B CG 6558 O OD1 . ASN B 418 ? 1.3961 1.3951 1.1053 0.2790 -0.0225 -0.0319 448 ASN B OD1 6559 N ND2 . ASN B 418 ? 1.3823 1.3974 1.1296 0.2546 -0.0248 -0.0424 448 ASN B ND2 6560 N N . LYS B 419 ? 1.4996 1.4468 1.1629 0.2439 0.0366 0.0181 449 LYS B N 6561 C CA . LYS B 419 ? 1.6313 1.5692 1.2746 0.2436 0.0509 0.0298 449 LYS B CA 6562 C C . LYS B 419 ? 1.6889 1.6435 1.3287 0.2487 0.0484 0.0237 449 LYS B C 6563 O O . LYS B 419 ? 1.6454 1.5960 1.2610 0.2578 0.0565 0.0314 449 LYS B O 6564 C CB . LYS B 419 ? 1.7307 1.6512 1.3426 0.2586 0.0574 0.0421 449 LYS B CB 6565 C CG . LYS B 419 ? 1.7728 1.6784 1.3834 0.2611 0.0561 0.0461 449 LYS B CG 6566 C CD . LYS B 419 ? 1.8221 1.7084 1.3995 0.2761 0.0637 0.0598 449 LYS B CD 6567 C CE . LYS B 419 ? 1.8463 1.7241 1.4190 0.2876 0.0557 0.0592 449 LYS B CE 6568 N NZ . LYS B 419 ? 1.8418 1.7115 1.4363 0.2725 0.0578 0.0587 449 LYS B NZ 6569 N N . GLN B 420 ? 1.7587 1.7312 1.4220 0.2432 0.0376 0.0101 450 GLN B N 6570 C CA . GLN B 420 ? 1.8234 1.8134 1.4860 0.2495 0.0324 0.0015 450 GLN B CA 6571 C C . GLN B 420 ? 1.8862 1.8805 1.5631 0.2336 0.0401 0.0017 450 GLN B C 6572 O O . GLN B 420 ? 1.8115 1.7997 1.5064 0.2166 0.0444 0.0041 450 GLN B O 6573 C CB . GLN B 420 ? 1.8035 1.8111 1.4834 0.2557 0.0138 -0.0150 450 GLN B CB 6574 C CG . GLN B 420 ? 1.8228 1.8343 1.4852 0.2772 0.0038 -0.0194 450 GLN B CG 6575 C CD . GLN B 420 ? 1.7814 1.8049 1.4660 0.2795 -0.0127 -0.0338 450 GLN B CD 6576 O OE1 . GLN B 420 ? 1.6479 1.6786 1.3606 0.2658 -0.0174 -0.0415 450 GLN B OE1 6577 N NE2 . GLN B 420 ? 1.8275 1.8532 1.4996 0.2972 -0.0215 -0.0375 450 GLN B NE2 6578 N N . PRO B 421 ? 1.9231 1.9285 1.5919 0.2395 0.0417 -0.0012 451 PRO B N 6579 C CA . PRO B 421 ? 1.8223 1.8349 1.5071 0.2259 0.0469 -0.0035 451 PRO B CA 6580 C C . PRO B 421 ? 1.6732 1.6981 1.3882 0.2174 0.0332 -0.0171 451 PRO B C 6581 O O . PRO B 421 ? 1.5980 1.6327 1.3185 0.2265 0.0190 -0.0279 451 PRO B O 6582 C CB . PRO B 421 ? 1.8660 1.8894 1.5329 0.2383 0.0498 -0.0053 451 PRO B CB 6583 C CG . PRO B 421 ? 1.9002 1.9289 1.5509 0.2583 0.0384 -0.0109 451 PRO B CG 6584 C CD . PRO B 421 ? 1.9179 1.9312 1.5630 0.2599 0.0376 -0.0040 451 PRO B CD 6585 N N . TYR B 422 ? 1.5818 1.6058 1.3162 0.2003 0.0374 -0.0167 452 TYR B N 6586 C CA . TYR B 422 ? 1.4894 1.5206 1.2517 0.1904 0.0258 -0.0270 452 TYR B CA 6587 C C . TYR B 422 ? 1.4807 1.5295 1.2535 0.1945 0.0164 -0.0396 452 TYR B C 6588 O O . TYR B 422 ? 1.3253 1.3821 1.1151 0.1948 0.0029 -0.0504 452 TYR B O 6589 C CB . TYR B 422 ? 1.3789 1.4012 1.1565 0.1714 0.0329 -0.0215 452 TYR B CB 6590 C CG . TYR B 422 ? 1.3734 1.3783 1.1431 0.1668 0.0415 -0.0104 452 TYR B CG 6591 C CD1 . TYR B 422 ? 1.3869 1.3801 1.1375 0.1679 0.0561 0.0014 452 TYR B CD1 6592 C CD2 . TYR B 422 ? 1.3254 1.3251 1.1068 0.1611 0.0356 -0.0119 452 TYR B CD2 6593 C CE1 . TYR B 422 ? 1.3687 1.3449 1.1127 0.1640 0.0636 0.0110 452 TYR B CE1 6594 C CE2 . TYR B 422 ? 1.3141 1.2983 1.0885 0.1576 0.0432 -0.0028 452 TYR B CE2 6595 C CZ . TYR B 422 ? 1.3571 1.3291 1.1130 0.1592 0.0567 0.0085 452 TYR B CZ 6596 O OH . TYR B 422 ? 1.3921 1.3473 1.1413 0.1560 0.0641 0.0173 452 TYR B OH # 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 ALA 1 1 1 ALA ALA A . n A 1 2 PRO 2 2 2 PRO PRO A . n A 1 3 ASP 3 3 3 ASP ASP A . n A 1 4 GLN 4 4 4 GLN GLN A . n A 1 5 ASP 5 5 5 ASP ASP A . n A 1 6 GLU 6 6 6 GLU GLU A . n A 1 7 ILE 7 7 7 ILE ILE A . n A 1 8 GLN 8 8 8 GLN GLN A . n A 1 9 ARG 9 9 9 ARG ARG A . n A 1 10 LEU 10 10 10 LEU LEU A . n A 1 11 PRO 11 11 11 PRO PRO A . n A 1 12 GLY 12 12 12 GLY GLY A . n A 1 13 LEU 13 13 13 LEU LEU A . n A 1 14 ALA 14 14 14 ALA ALA A . n A 1 15 LYS 15 15 15 LYS LYS A . n A 1 16 GLN 16 16 16 GLN GLN A . n A 1 17 PRO 17 17 17 PRO PRO A . n A 1 18 SER 18 18 18 SER SER A . n A 1 19 PHE 19 19 19 PHE PHE A . n A 1 20 ARG 20 20 20 ARG ARG A . n A 1 21 GLN 21 21 21 GLN GLN A . n A 1 22 TYR 22 22 22 TYR TYR A . n A 1 23 SER 23 23 23 SER SER A . n A 1 24 GLY 24 24 24 GLY GLY A . n A 1 25 TYR 25 25 25 TYR TYR A . n A 1 26 LEU 26 26 26 LEU LEU A . n A 1 27 LYS 27 27 27 LYS LYS A . n A 1 28 GLY 28 28 28 GLY GLY A . n A 1 29 SER 29 29 29 SER SER A . n A 1 30 GLY 30 30 30 GLY GLY A . n A 1 31 SER 31 31 31 SER SER A . n A 1 32 LYS 32 32 32 LYS LYS A . n A 1 33 HIS 33 33 33 HIS HIS A . n A 1 34 LEU 34 34 34 LEU LEU A . n A 1 35 HIS 35 35 35 HIS HIS A . n A 1 36 TYR 36 36 36 TYR TYR A . n A 1 37 TRP 37 37 37 TRP TRP A . n A 1 38 PHE 38 38 38 PHE PHE A . n A 1 39 VAL 39 39 39 VAL VAL A . n A 1 40 GLU 40 40 40 GLU GLU A . n A 1 41 SER 41 41 41 SER SER A . n A 1 42 GLN 42 42 42 GLN GLN A . n A 1 43 LYS 43 43 43 LYS LYS A . n A 1 44 ASP 44 44 44 ASP ASP A . n A 1 45 PRO 45 45 45 PRO PRO A . n A 1 46 GLU 46 46 46 GLU GLU A . n A 1 47 ASN 47 47 47 ASN ASN A . n A 1 48 SER 48 48 48 SER SER A . n A 1 49 PRO 49 49 49 PRO PRO A . n A 1 50 VAL 50 50 50 VAL VAL A . n A 1 51 VAL 51 51 51 VAL VAL A . n A 1 52 LEU 52 52 52 LEU LEU A . n A 1 53 TRP 53 53 53 TRP TRP A . n A 1 54 LEU 54 54 54 LEU LEU A . n A 1 55 ASN 55 55 55 ASN ASN A . n A 1 56 GLY 56 56 56 GLY GLY A . n A 1 57 GLY 57 57 57 GLY GLY A . n A 1 58 PRO 58 58 58 PRO PRO A . n A 1 59 GLY 59 59 59 GLY GLY A . n A 1 60 CYS 60 60 60 CYS CYS A . n A 1 61 SER 61 61 61 SER SER A . n A 1 62 SER 62 62 62 SER SER A . n A 1 63 LEU 63 63 63 LEU LEU A . n A 1 64 ASP 64 64 64 ASP ASP A . n A 1 65 GLY 65 65 65 GLY GLY A . n A 1 66 LEU 66 66 66 LEU LEU A . n A 1 67 LEU 67 67 67 LEU LEU A . n A 1 68 THR 68 68 68 THR THR A . n A 1 69 GLU 69 69 69 GLU GLU A . n A 1 70 HIS 70 70 70 HIS HIS A . n A 1 71 GLY 71 71 71 GLY GLY A . n A 1 72 PRO 72 72 72 PRO PRO A . n A 1 73 PHE 73 73 73 PHE PHE A . n A 1 74 LEU 74 74 74 LEU LEU A . n A 1 75 VAL 75 75 75 VAL VAL A . n A 1 76 GLN 76 76 76 GLN GLN A . n A 1 77 PRO 77 77 77 PRO PRO A . n A 1 78 ASP 78 78 78 ASP ASP A . n A 1 79 GLY 79 79 79 GLY GLY A . n A 1 80 VAL 80 80 80 VAL VAL A . n A 1 81 THR 81 81 81 THR THR A . n A 1 82 LEU 82 82 82 LEU LEU A . n A 1 83 GLU 83 83 83 GLU GLU A . n A 1 84 TYR 84 84 84 TYR TYR A . n A 1 85 ASN 85 85 85 ASN ASN A . n A 1 86 PRO 86 86 86 PRO PRO A . n A 1 87 TYR 87 87 87 TYR TYR A . n A 1 88 SER 88 88 88 SER SER A . n A 1 89 TRP 89 89 89 TRP TRP A . n A 1 90 ASN 90 90 90 ASN ASN A . n A 1 91 LEU 91 91 91 LEU LEU A . n A 1 92 ILE 92 92 92 ILE ILE A . n A 1 93 ALA 93 93 93 ALA ALA A . n A 1 94 ASN 94 94 94 ASN ASN A . n A 1 95 VAL 95 95 95 VAL VAL A . n A 1 96 LEU 96 96 96 LEU LEU A . n A 1 97 TYR 97 97 97 TYR TYR A . n A 1 98 LEU 98 98 98 LEU LEU A . n A 1 99 GLU 99 99 99 GLU GLU A . n A 1 100 SER 100 100 100 SER SER A . n A 1 101 PRO 101 101 101 PRO PRO A . n A 1 102 ALA 102 102 102 ALA ALA A . n A 1 103 GLY 103 103 103 GLY GLY A . n A 1 104 VAL 104 104 104 VAL VAL A . n A 1 105 GLY 105 105 105 GLY GLY A . n A 1 106 PHE 106 106 106 PHE PHE A . n A 1 107 SER 107 107 107 SER SER A . n A 1 108 TYR 108 108 108 TYR TYR A . n A 1 109 SER 109 109 109 SER SER A . n A 1 110 ASP 110 110 110 ASP ASP A . n A 1 111 ASP 111 111 111 ASP ASP A . n A 1 112 LYS 112 112 112 LYS LYS A . n A 1 113 PHE 113 113 113 PHE PHE A . n A 1 114 TYR 114 114 114 TYR TYR A . n A 1 115 ALA 115 115 115 ALA ALA A . n A 1 116 THR 116 116 116 THR THR A . n A 1 117 ASN 117 117 117 ASN ASN A . n A 1 118 ASP 118 118 118 ASP ASP A . n A 1 119 THR 119 119 119 THR THR A . n A 1 120 GLU 120 120 120 GLU GLU A . n A 1 121 VAL 121 121 121 VAL VAL A . n A 1 122 ALA 122 122 122 ALA ALA A . n A 1 123 GLN 123 123 123 GLN GLN A . n A 1 124 SER 124 124 124 SER SER A . n A 1 125 ASN 125 125 125 ASN ASN A . n A 1 126 PHE 126 126 126 PHE PHE A . n A 1 127 GLU 127 127 127 GLU GLU A . n A 1 128 ALA 128 128 128 ALA ALA A . n A 1 129 LEU 129 129 129 LEU LEU A . n A 1 130 GLN 130 130 130 GLN GLN A . n A 1 131 ASP 131 131 131 ASP ASP A . n A 1 132 PHE 132 132 132 PHE PHE A . n A 1 133 PHE 133 133 133 PHE PHE A . n A 1 134 ARG 134 134 134 ARG ARG A . n A 1 135 LEU 135 135 135 LEU LEU A . n A 1 136 PHE 136 136 136 PHE PHE A . n A 1 137 PRO 137 137 137 PRO PRO A . n A 1 138 GLU 138 138 138 GLU GLU A . n A 1 139 TYR 139 139 139 TYR TYR A . n A 1 140 LYS 140 140 140 LYS LYS A . n A 1 141 ASN 141 141 141 ASN ASN A . n A 1 142 ASN 142 142 142 ASN ASN A . n A 1 143 LYS 143 143 143 LYS LYS A . n A 1 144 LEU 144 144 144 LEU LEU A . n A 1 145 PHE 145 145 145 PHE PHE A . n A 1 146 LEU 146 146 146 LEU LEU A . n A 1 147 THR 147 147 147 THR THR A . n A 1 148 GLY 148 148 148 GLY GLY A . n A 1 149 GLU 149 149 149 GLU GLU A . n A 1 150 SER 150 150 150 SER SER A . n A 1 151 TYR 151 151 151 TYR TYR A . n A 1 152 ALA 152 152 152 ALA ALA A . n A 1 153 GLY 153 153 153 GLY GLY A . n A 1 154 ILE 154 154 154 ILE ILE A . n A 1 155 TYR 155 155 155 TYR TYR A . n A 1 156 ILE 156 156 156 ILE ILE A . n A 1 157 PRO 157 157 157 PRO PRO A . n A 1 158 THR 158 158 158 THR THR A . n A 1 159 LEU 159 159 159 LEU LEU A . n A 1 160 ALA 160 160 160 ALA ALA A . n A 1 161 VAL 161 161 161 VAL VAL A . n A 1 162 LEU 162 162 162 LEU LEU A . n A 1 163 VAL 163 163 163 VAL VAL A . n A 1 164 MET 164 164 164 MET MET A . n A 1 165 GLN 165 165 165 GLN GLN A . n A 1 166 ASP 166 166 166 ASP ASP A . n A 1 167 PRO 167 167 167 PRO PRO A . n A 1 168 SER 168 168 168 SER SER A . n A 1 169 MET 169 169 169 MET MET A . n A 1 170 ASN 170 170 170 ASN ASN A . n A 1 171 LEU 171 171 171 LEU LEU A . n A 1 172 GLN 172 172 172 GLN GLN A . n A 1 173 GLY 173 173 173 GLY GLY A . n A 1 174 LEU 174 174 174 LEU LEU A . n A 1 175 ALA 175 175 175 ALA ALA A . n A 1 176 VAL 176 176 176 VAL VAL A . n A 1 177 GLY 177 177 177 GLY GLY A . n A 1 178 ASN 178 178 178 ASN ASN A . n A 1 179 GLY 179 179 179 GLY GLY A . n A 1 180 LEU 180 180 180 LEU LEU A . n A 1 181 SER 181 181 181 SER SER A . n A 1 182 SER 182 182 182 SER SER A . n A 1 183 TYR 183 183 183 TYR TYR A . n A 1 184 GLU 184 184 184 GLU GLU A . n A 1 185 GLN 185 185 185 GLN GLN A . n A 1 186 ASN 186 186 186 ASN ASN A . n A 1 187 ASP 187 187 187 ASP ASP A . n A 1 188 ASN 188 188 188 ASN ASN A . n A 1 189 SER 189 189 189 SER SER A . n A 1 190 LEU 190 190 190 LEU LEU A . n A 1 191 VAL 191 191 191 VAL VAL A . n A 1 192 TYR 192 192 192 TYR TYR A . n A 1 193 PHE 193 193 193 PHE PHE A . n A 1 194 ALA 194 194 194 ALA ALA A . n A 1 195 TYR 195 195 195 TYR TYR A . n A 1 196 TYR 196 196 196 TYR TYR A . n A 1 197 HIS 197 197 197 HIS HIS A . n A 1 198 GLY 198 198 198 GLY GLY A . n A 1 199 LEU 199 199 199 LEU LEU A . n A 1 200 LEU 200 200 200 LEU LEU A . n A 1 201 GLY 201 201 201 GLY GLY A . n A 1 202 ASN 202 202 202 ASN ASN A . n A 1 203 ARG 203 203 203 ARG ARG A . n A 1 204 LEU 204 204 204 LEU LEU A . n A 1 205 TRP 205 205 205 TRP TRP A . n A 1 206 SER 206 206 206 SER SER A . n A 1 207 SER 207 207 207 SER SER A . n A 1 208 LEU 208 208 208 LEU LEU A . n A 1 209 GLN 209 209 209 GLN GLN A . n A 1 210 THR 210 210 210 THR THR A . n A 1 211 HIS 211 211 211 HIS HIS A . n A 1 212 CYS 212 212 212 CYS CYS A . n A 1 213 CYS 213 213 213 CYS CYS A . n A 1 214 SER 214 214 214 SER SER A . n A 1 215 GLN 215 215 215 GLN GLN A . n A 1 216 ASN 216 216 216 ASN ASN A . n A 1 217 LYS 217 217 217 LYS LYS A . n A 1 218 CYS 218 218 218 CYS CYS A . n A 1 219 ASN 219 219 219 ASN ASN A . n A 1 220 PHE 220 220 220 PHE PHE A . n A 1 221 TYR 221 221 221 TYR TYR A . n A 1 222 ASP 222 222 222 ASP ASP A . n A 1 223 ASN 223 223 223 ASN ASN A . n A 1 224 LYS 224 224 224 LYS LYS A . n A 1 225 ASP 225 225 225 ASP ASP A . n A 1 226 LEU 226 226 226 LEU LEU A . n A 1 227 GLU 227 227 227 GLU GLU A . n A 1 228 CYS 228 228 228 CYS CYS A . n A 1 229 VAL 229 229 229 VAL VAL A . n A 1 230 THR 230 230 230 THR THR A . n A 1 231 ASN 231 231 231 ASN ASN A . n A 1 232 LEU 232 232 232 LEU LEU A . n A 1 233 GLN 233 233 233 GLN GLN A . n A 1 234 GLU 234 234 234 GLU GLU A . n A 1 235 VAL 235 235 235 VAL VAL A . n A 1 236 ALA 236 236 236 ALA ALA A . n A 1 237 ARG 237 237 237 ARG ARG A . n A 1 238 ILE 238 238 238 ILE ILE A . n A 1 239 VAL 239 239 239 VAL VAL A . n A 1 240 GLY 240 240 240 GLY GLY A . n A 1 241 ASN 241 241 241 ASN ASN A . n A 1 242 SER 242 242 242 SER SER A . n A 1 243 GLY 243 243 243 GLY GLY A . n A 1 244 LEU 244 244 244 LEU LEU A . n A 1 245 ASN 245 245 245 ASN ASN A . n A 1 246 ILE 246 246 246 ILE ILE A . n A 1 247 TYR 247 247 247 TYR TYR A . n A 1 248 ASN 248 248 248 ASN ASN A . n A 1 249 LEU 249 249 249 LEU LEU A . n A 1 250 TYR 250 250 250 TYR TYR A . n A 1 251 ALA 251 251 251 ALA ALA A . n A 1 252 PRO 252 252 252 PRO PRO A . n A 1 253 CYS 253 253 253 CYS CYS A . n A 1 254 ALA 254 254 254 ALA ALA A . n A 1 255 GLY 255 255 255 GLY GLY A . n A 1 256 GLY 256 256 256 GLY GLY A . n A 1 257 VAL 257 257 257 VAL VAL A . n A 1 258 PRO 258 258 258 PRO PRO A . n A 1 259 SER 259 289 ? ? ? A . n A 1 260 HIS 260 290 ? ? ? A . n A 1 261 PHE 261 291 ? ? ? A . n A 1 262 ARG 262 292 ? ? ? A . n A 1 263 SER 263 293 ? ? ? A . n A 1 264 GLY 264 294 ? ? ? A . n A 1 265 ASP 265 295 ? ? ? A . n A 1 266 LYS 266 296 ? ? ? A . n A 1 267 VAL 267 297 ? ? ? A . n A 1 268 ARG 268 298 298 ARG ARG A . n A 1 269 MET 269 299 299 MET MET A . n A 1 270 ASP 270 300 300 ASP ASP A . n A 1 271 PRO 271 301 301 PRO PRO A . n A 1 272 PRO 272 302 302 PRO PRO A . n A 1 273 CYS 273 303 303 CYS CYS A . n A 1 274 THR 274 304 304 THR THR A . n A 1 275 ASN 275 305 305 ASN ASN A . n A 1 276 THR 276 306 306 THR THR A . n A 1 277 THR 277 307 307 THR THR A . n A 1 278 ALA 278 308 308 ALA ALA A . n A 1 279 ALA 279 309 309 ALA ALA A . n A 1 280 SER 280 310 310 SER SER A . n A 1 281 THR 281 311 311 THR THR A . n A 1 282 TYR 282 312 312 TYR TYR A . n A 1 283 LEU 283 313 313 LEU LEU A . n A 1 284 ASN 284 314 314 ASN ASN A . n A 1 285 ASN 285 315 315 ASN ASN A . n A 1 286 PRO 286 316 316 PRO PRO A . n A 1 287 TYR 287 317 317 TYR TYR A . n A 1 288 VAL 288 318 318 VAL VAL A . n A 1 289 ARG 289 319 319 ARG ARG A . n A 1 290 LYS 290 320 320 LYS LYS A . n A 1 291 ALA 291 321 321 ALA ALA A . n A 1 292 LEU 292 322 322 LEU LEU A . n A 1 293 ASN 293 323 323 ASN ASN A . n A 1 294 ILE 294 324 324 ILE ILE A . n A 1 295 PRO 295 325 325 PRO PRO A . n A 1 296 GLU 296 326 326 GLU GLU A . n A 1 297 GLN 297 327 327 GLN GLN A . n A 1 298 LEU 298 328 328 LEU LEU A . n A 1 299 PRO 299 329 329 PRO PRO A . n A 1 300 GLN 300 330 330 GLN GLN A . n A 1 301 TRP 301 331 331 TRP TRP A . n A 1 302 ASP 302 332 332 ASP ASP A . n A 1 303 MET 303 333 333 MET MET A . n A 1 304 CYS 304 334 334 CYS CYS A . n A 1 305 ASN 305 335 335 ASN ASN A . n A 1 306 PHE 306 336 336 PHE PHE A . n A 1 307 LEU 307 337 337 LEU LEU A . n A 1 308 VAL 308 338 338 VAL VAL A . n A 1 309 ASN 309 339 339 ASN ASN A . n A 1 310 LEU 310 340 340 LEU LEU A . n A 1 311 GLN 311 341 341 GLN GLN A . n A 1 312 TYR 312 342 342 TYR TYR A . n A 1 313 ARG 313 343 343 ARG ARG A . n A 1 314 ARG 314 344 344 ARG ARG A . n A 1 315 LEU 315 345 345 LEU LEU A . n A 1 316 TYR 316 346 346 TYR TYR A . n A 1 317 ARG 317 347 347 ARG ARG A . n A 1 318 SER 318 348 348 SER SER A . n A 1 319 MET 319 349 349 MET MET A . n A 1 320 ASN 320 350 350 ASN ASN A . n A 1 321 SER 321 351 351 SER SER A . n A 1 322 GLN 322 352 352 GLN GLN A . n A 1 323 TYR 323 353 353 TYR TYR A . n A 1 324 LEU 324 354 354 LEU LEU A . n A 1 325 LYS 325 355 355 LYS LYS A . n A 1 326 LEU 326 356 356 LEU LEU A . n A 1 327 LEU 327 357 357 LEU LEU A . n A 1 328 SER 328 358 358 SER SER A . n A 1 329 SER 329 359 359 SER SER A . n A 1 330 GLN 330 360 360 GLN GLN A . n A 1 331 LYS 331 361 361 LYS LYS A . n A 1 332 TYR 332 362 362 TYR TYR A . n A 1 333 GLN 333 363 363 GLN GLN A . n A 1 334 ILE 334 364 364 ILE ILE A . n A 1 335 LEU 335 365 365 LEU LEU A . n A 1 336 LEU 336 366 366 LEU LEU A . n A 1 337 TYR 337 367 367 TYR TYR A . n A 1 338 ASN 338 368 368 ASN ASN A . n A 1 339 GLY 339 369 369 GLY GLY A . n A 1 340 ASP 340 370 370 ASP ASP A . n A 1 341 VAL 341 371 371 VAL VAL A . n A 1 342 ASP 342 372 372 ASP ASP A . n A 1 343 MET 343 373 373 MET MET A . n A 1 344 ALA 344 374 374 ALA ALA A . n A 1 345 CYS 345 375 375 CYS CYS A . n A 1 346 ASN 346 376 376 ASN ASN A . n A 1 347 PHE 347 377 377 PHE PHE A . n A 1 348 MET 348 378 378 MET MET A . n A 1 349 GLY 349 379 379 GLY GLY A . n A 1 350 ASP 350 380 380 ASP ASP A . n A 1 351 GLU 351 381 381 GLU GLU A . n A 1 352 TRP 352 382 382 TRP TRP A . n A 1 353 PHE 353 383 383 PHE PHE A . n A 1 354 VAL 354 384 384 VAL VAL A . n A 1 355 ASP 355 385 385 ASP ASP A . n A 1 356 SER 356 386 386 SER SER A . n A 1 357 LEU 357 387 387 LEU LEU A . n A 1 358 ASN 358 388 388 ASN ASN A . n A 1 359 GLN 359 389 389 GLN GLN A . n A 1 360 LYS 360 390 390 LYS LYS A . n A 1 361 MET 361 391 391 MET MET A . n A 1 362 GLU 362 392 392 GLU GLU A . n A 1 363 VAL 363 393 393 VAL VAL A . n A 1 364 GLN 364 394 394 GLN GLN A . n A 1 365 ARG 365 395 395 ARG ARG A . n A 1 366 ARG 366 396 396 ARG ARG A . n A 1 367 PRO 367 397 397 PRO PRO A . n A 1 368 TRP 368 398 398 TRP TRP A . n A 1 369 LEU 369 399 399 LEU LEU A . n A 1 370 VAL 370 400 400 VAL VAL A . n A 1 371 LYS 371 401 401 LYS LYS A . n A 1 372 TYR 372 402 402 TYR TYR A . n A 1 373 GLY 373 403 403 GLY GLY A . n A 1 374 ASP 374 404 404 ASP ASP A . n A 1 375 SER 375 405 405 SER SER A . n A 1 376 GLY 376 406 406 GLY GLY A . n A 1 377 GLU 377 407 407 GLU GLU A . n A 1 378 GLN 378 408 408 GLN GLN A . n A 1 379 ILE 379 409 409 ILE ILE A . n A 1 380 ALA 380 410 410 ALA ALA A . n A 1 381 GLY 381 411 411 GLY GLY A . n A 1 382 PHE 382 412 412 PHE PHE A . n A 1 383 VAL 383 413 413 VAL VAL A . n A 1 384 LYS 384 414 414 LYS LYS A . n A 1 385 GLU 385 415 415 GLU GLU A . n A 1 386 PHE 386 416 416 PHE PHE A . n A 1 387 SER 387 417 417 SER SER A . n A 1 388 HIS 388 418 418 HIS HIS A . n A 1 389 ILE 389 419 419 ILE ILE A . n A 1 390 ALA 390 420 420 ALA ALA A . n A 1 391 PHE 391 421 421 PHE PHE A . n A 1 392 LEU 392 422 422 LEU LEU A . n A 1 393 THR 393 423 423 THR THR A . n A 1 394 ILE 394 424 424 ILE ILE A . n A 1 395 LYS 395 425 425 LYS LYS A . n A 1 396 GLY 396 426 426 GLY GLY A . n A 1 397 ALA 397 427 427 ALA ALA A . n A 1 398 GLY 398 428 428 GLY GLY A . n A 1 399 HIS 399 429 429 HIS HIS A . n A 1 400 MET 400 430 430 MET MET A . n A 1 401 VAL 401 431 431 VAL VAL A . n A 1 402 PRO 402 432 432 PRO PRO A . n A 1 403 THR 403 433 433 THR THR A . n A 1 404 ASP 404 434 434 ASP ASP A . n A 1 405 LYS 405 435 435 LYS LYS A . n A 1 406 PRO 406 436 436 PRO PRO A . n A 1 407 LEU 407 437 437 LEU LEU A . n A 1 408 ALA 408 438 438 ALA ALA A . n A 1 409 ALA 409 439 439 ALA ALA A . n A 1 410 PHE 410 440 440 PHE PHE A . n A 1 411 THR 411 441 441 THR THR A . n A 1 412 MET 412 442 442 MET MET A . n A 1 413 PHE 413 443 443 PHE PHE A . n A 1 414 SER 414 444 444 SER SER A . n A 1 415 ARG 415 445 445 ARG ARG A . n A 1 416 PHE 416 446 446 PHE PHE A . n A 1 417 LEU 417 447 447 LEU LEU A . n A 1 418 ASN 418 448 448 ASN ASN A . n A 1 419 LYS 419 449 449 LYS LYS A . n A 1 420 GLN 420 450 450 GLN GLN A . n A 1 421 PRO 421 451 451 PRO PRO A . n A 1 422 TYR 422 452 452 TYR TYR A . n A 1 423 HIS 423 453 ? ? ? A . n A 1 424 HIS 424 454 ? ? ? A . n A 1 425 HIS 425 455 ? ? ? A . n A 1 426 HIS 426 456 ? ? ? A . n A 1 427 HIS 427 457 ? ? ? A . n A 1 428 HIS 428 458 ? ? ? A . n B 1 1 ALA 1 1 1 ALA ALA B . n B 1 2 PRO 2 2 2 PRO PRO B . n B 1 3 ASP 3 3 3 ASP ASP B . n B 1 4 GLN 4 4 4 GLN GLN B . n B 1 5 ASP 5 5 5 ASP ASP B . n B 1 6 GLU 6 6 6 GLU GLU B . n B 1 7 ILE 7 7 7 ILE ILE B . n B 1 8 GLN 8 8 8 GLN GLN B . n B 1 9 ARG 9 9 9 ARG ARG B . n B 1 10 LEU 10 10 10 LEU LEU B . n B 1 11 PRO 11 11 11 PRO PRO B . n B 1 12 GLY 12 12 12 GLY GLY B . n B 1 13 LEU 13 13 13 LEU LEU B . n B 1 14 ALA 14 14 14 ALA ALA B . n B 1 15 LYS 15 15 15 LYS LYS B . n B 1 16 GLN 16 16 16 GLN GLN B . n B 1 17 PRO 17 17 17 PRO PRO B . n B 1 18 SER 18 18 18 SER SER B . n B 1 19 PHE 19 19 19 PHE PHE B . n B 1 20 ARG 20 20 20 ARG ARG B . n B 1 21 GLN 21 21 21 GLN GLN B . n B 1 22 TYR 22 22 22 TYR TYR B . n B 1 23 SER 23 23 23 SER SER B . n B 1 24 GLY 24 24 24 GLY GLY B . n B 1 25 TYR 25 25 25 TYR TYR B . n B 1 26 LEU 26 26 26 LEU LEU B . n B 1 27 LYS 27 27 27 LYS LYS B . n B 1 28 GLY 28 28 28 GLY GLY B . n B 1 29 SER 29 29 29 SER SER B . n B 1 30 GLY 30 30 30 GLY GLY B . n B 1 31 SER 31 31 31 SER SER B . n B 1 32 LYS 32 32 32 LYS LYS B . n B 1 33 HIS 33 33 33 HIS HIS B . n B 1 34 LEU 34 34 34 LEU LEU B . n B 1 35 HIS 35 35 35 HIS HIS B . n B 1 36 TYR 36 36 36 TYR TYR B . n B 1 37 TRP 37 37 37 TRP TRP B . n B 1 38 PHE 38 38 38 PHE PHE B . n B 1 39 VAL 39 39 39 VAL VAL B . n B 1 40 GLU 40 40 40 GLU GLU B . n B 1 41 SER 41 41 41 SER SER B . n B 1 42 GLN 42 42 42 GLN GLN B . n B 1 43 LYS 43 43 43 LYS LYS B . n B 1 44 ASP 44 44 44 ASP ASP B . n B 1 45 PRO 45 45 45 PRO PRO B . n B 1 46 GLU 46 46 46 GLU GLU B . n B 1 47 ASN 47 47 47 ASN ASN B . n B 1 48 SER 48 48 48 SER SER B . n B 1 49 PRO 49 49 49 PRO PRO B . n B 1 50 VAL 50 50 50 VAL VAL B . n B 1 51 VAL 51 51 51 VAL VAL B . n B 1 52 LEU 52 52 52 LEU LEU B . n B 1 53 TRP 53 53 53 TRP TRP B . n B 1 54 LEU 54 54 54 LEU LEU B . n B 1 55 ASN 55 55 55 ASN ASN B . n B 1 56 GLY 56 56 56 GLY GLY B . n B 1 57 GLY 57 57 57 GLY GLY B . n B 1 58 PRO 58 58 58 PRO PRO B . n B 1 59 GLY 59 59 59 GLY GLY B . n B 1 60 CYS 60 60 60 CYS CYS B . n B 1 61 SER 61 61 61 SER SER B . n B 1 62 SER 62 62 62 SER SER B . n B 1 63 LEU 63 63 63 LEU LEU B . n B 1 64 ASP 64 64 64 ASP ASP B . n B 1 65 GLY 65 65 65 GLY GLY B . n B 1 66 LEU 66 66 66 LEU LEU B . n B 1 67 LEU 67 67 67 LEU LEU B . n B 1 68 THR 68 68 68 THR THR B . n B 1 69 GLU 69 69 69 GLU GLU B . n B 1 70 HIS 70 70 70 HIS HIS B . n B 1 71 GLY 71 71 71 GLY GLY B . n B 1 72 PRO 72 72 72 PRO PRO B . n B 1 73 PHE 73 73 73 PHE PHE B . n B 1 74 LEU 74 74 74 LEU LEU B . n B 1 75 VAL 75 75 75 VAL VAL B . n B 1 76 GLN 76 76 76 GLN GLN B . n B 1 77 PRO 77 77 77 PRO PRO B . n B 1 78 ASP 78 78 78 ASP ASP B . n B 1 79 GLY 79 79 79 GLY GLY B . n B 1 80 VAL 80 80 80 VAL VAL B . n B 1 81 THR 81 81 81 THR THR B . n B 1 82 LEU 82 82 82 LEU LEU B . n B 1 83 GLU 83 83 83 GLU GLU B . n B 1 84 TYR 84 84 84 TYR TYR B . n B 1 85 ASN 85 85 85 ASN ASN B . n B 1 86 PRO 86 86 86 PRO PRO B . n B 1 87 TYR 87 87 87 TYR TYR B . n B 1 88 SER 88 88 88 SER SER B . n B 1 89 TRP 89 89 89 TRP TRP B . n B 1 90 ASN 90 90 90 ASN ASN B . n B 1 91 LEU 91 91 91 LEU LEU B . n B 1 92 ILE 92 92 92 ILE ILE B . n B 1 93 ALA 93 93 93 ALA ALA B . n B 1 94 ASN 94 94 94 ASN ASN B . n B 1 95 VAL 95 95 95 VAL VAL B . n B 1 96 LEU 96 96 96 LEU LEU B . n B 1 97 TYR 97 97 97 TYR TYR B . n B 1 98 LEU 98 98 98 LEU LEU B . n B 1 99 GLU 99 99 99 GLU GLU B . n B 1 100 SER 100 100 100 SER SER B . n B 1 101 PRO 101 101 101 PRO PRO B . n B 1 102 ALA 102 102 102 ALA ALA B . n B 1 103 GLY 103 103 103 GLY GLY B . n B 1 104 VAL 104 104 104 VAL VAL B . n B 1 105 GLY 105 105 105 GLY GLY B . n B 1 106 PHE 106 106 106 PHE PHE B . n B 1 107 SER 107 107 107 SER SER B . n B 1 108 TYR 108 108 108 TYR TYR B . n B 1 109 SER 109 109 109 SER SER B . n B 1 110 ASP 110 110 110 ASP ASP B . n B 1 111 ASP 111 111 111 ASP ASP B . n B 1 112 LYS 112 112 112 LYS LYS B . n B 1 113 PHE 113 113 113 PHE PHE B . n B 1 114 TYR 114 114 114 TYR TYR B . n B 1 115 ALA 115 115 115 ALA ALA B . n B 1 116 THR 116 116 116 THR THR B . n B 1 117 ASN 117 117 117 ASN ASN B . n B 1 118 ASP 118 118 118 ASP ASP B . n B 1 119 THR 119 119 119 THR THR B . n B 1 120 GLU 120 120 120 GLU GLU B . n B 1 121 VAL 121 121 121 VAL VAL B . n B 1 122 ALA 122 122 122 ALA ALA B . n B 1 123 GLN 123 123 123 GLN GLN B . n B 1 124 SER 124 124 124 SER SER B . n B 1 125 ASN 125 125 125 ASN ASN B . n B 1 126 PHE 126 126 126 PHE PHE B . n B 1 127 GLU 127 127 127 GLU GLU B . n B 1 128 ALA 128 128 128 ALA ALA B . n B 1 129 LEU 129 129 129 LEU LEU B . n B 1 130 GLN 130 130 130 GLN GLN B . n B 1 131 ASP 131 131 131 ASP ASP B . n B 1 132 PHE 132 132 132 PHE PHE B . n B 1 133 PHE 133 133 133 PHE PHE B . n B 1 134 ARG 134 134 134 ARG ARG B . n B 1 135 LEU 135 135 135 LEU LEU B . n B 1 136 PHE 136 136 136 PHE PHE B . n B 1 137 PRO 137 137 137 PRO PRO B . n B 1 138 GLU 138 138 138 GLU GLU B . n B 1 139 TYR 139 139 139 TYR TYR B . n B 1 140 LYS 140 140 140 LYS LYS B . n B 1 141 ASN 141 141 141 ASN ASN B . n B 1 142 ASN 142 142 142 ASN ASN B . n B 1 143 LYS 143 143 143 LYS LYS B . n B 1 144 LEU 144 144 144 LEU LEU B . n B 1 145 PHE 145 145 145 PHE PHE B . n B 1 146 LEU 146 146 146 LEU LEU B . n B 1 147 THR 147 147 147 THR THR B . n B 1 148 GLY 148 148 148 GLY GLY B . n B 1 149 GLU 149 149 149 GLU GLU B . n B 1 150 SER 150 150 150 SER SER B . n B 1 151 TYR 151 151 151 TYR TYR B . n B 1 152 ALA 152 152 152 ALA ALA B . n B 1 153 GLY 153 153 153 GLY GLY B . n B 1 154 ILE 154 154 154 ILE ILE B . n B 1 155 TYR 155 155 155 TYR TYR B . n B 1 156 ILE 156 156 156 ILE ILE B . n B 1 157 PRO 157 157 157 PRO PRO B . n B 1 158 THR 158 158 158 THR THR B . n B 1 159 LEU 159 159 159 LEU LEU B . n B 1 160 ALA 160 160 160 ALA ALA B . n B 1 161 VAL 161 161 161 VAL VAL B . n B 1 162 LEU 162 162 162 LEU LEU B . n B 1 163 VAL 163 163 163 VAL VAL B . n B 1 164 MET 164 164 164 MET MET B . n B 1 165 GLN 165 165 165 GLN GLN B . n B 1 166 ASP 166 166 166 ASP ASP B . n B 1 167 PRO 167 167 167 PRO PRO B . n B 1 168 SER 168 168 168 SER SER B . n B 1 169 MET 169 169 169 MET MET B . n B 1 170 ASN 170 170 170 ASN ASN B . n B 1 171 LEU 171 171 171 LEU LEU B . n B 1 172 GLN 172 172 172 GLN GLN B . n B 1 173 GLY 173 173 173 GLY GLY B . n B 1 174 LEU 174 174 174 LEU LEU B . n B 1 175 ALA 175 175 175 ALA ALA B . n B 1 176 VAL 176 176 176 VAL VAL B . n B 1 177 GLY 177 177 177 GLY GLY B . n B 1 178 ASN 178 178 178 ASN ASN B . n B 1 179 GLY 179 179 179 GLY GLY B . n B 1 180 LEU 180 180 180 LEU LEU B . n B 1 181 SER 181 181 181 SER SER B . n B 1 182 SER 182 182 182 SER SER B . n B 1 183 TYR 183 183 183 TYR TYR B . n B 1 184 GLU 184 184 184 GLU GLU B . n B 1 185 GLN 185 185 185 GLN GLN B . n B 1 186 ASN 186 186 186 ASN ASN B . n B 1 187 ASP 187 187 187 ASP ASP B . n B 1 188 ASN 188 188 188 ASN ASN B . n B 1 189 SER 189 189 189 SER SER B . n B 1 190 LEU 190 190 190 LEU LEU B . n B 1 191 VAL 191 191 191 VAL VAL B . n B 1 192 TYR 192 192 192 TYR TYR B . n B 1 193 PHE 193 193 193 PHE PHE B . n B 1 194 ALA 194 194 194 ALA ALA B . n B 1 195 TYR 195 195 195 TYR TYR B . n B 1 196 TYR 196 196 196 TYR TYR B . n B 1 197 HIS 197 197 197 HIS HIS B . n B 1 198 GLY 198 198 198 GLY GLY B . n B 1 199 LEU 199 199 199 LEU LEU B . n B 1 200 LEU 200 200 200 LEU LEU B . n B 1 201 GLY 201 201 201 GLY GLY B . n B 1 202 ASN 202 202 202 ASN ASN B . n B 1 203 ARG 203 203 203 ARG ARG B . n B 1 204 LEU 204 204 204 LEU LEU B . n B 1 205 TRP 205 205 205 TRP TRP B . n B 1 206 SER 206 206 206 SER SER B . n B 1 207 SER 207 207 207 SER SER B . n B 1 208 LEU 208 208 208 LEU LEU B . n B 1 209 GLN 209 209 209 GLN GLN B . n B 1 210 THR 210 210 210 THR THR B . n B 1 211 HIS 211 211 211 HIS HIS B . n B 1 212 CYS 212 212 212 CYS CYS B . n B 1 213 CYS 213 213 213 CYS CYS B . n B 1 214 SER 214 214 214 SER SER B . n B 1 215 GLN 215 215 215 GLN GLN B . n B 1 216 ASN 216 216 216 ASN ASN B . n B 1 217 LYS 217 217 217 LYS LYS B . n B 1 218 CYS 218 218 218 CYS CYS B . n B 1 219 ASN 219 219 219 ASN ASN B . n B 1 220 PHE 220 220 220 PHE PHE B . n B 1 221 TYR 221 221 221 TYR TYR B . n B 1 222 ASP 222 222 222 ASP ASP B . n B 1 223 ASN 223 223 223 ASN ASN B . n B 1 224 LYS 224 224 224 LYS LYS B . n B 1 225 ASP 225 225 225 ASP ASP B . n B 1 226 LEU 226 226 226 LEU LEU B . n B 1 227 GLU 227 227 227 GLU GLU B . n B 1 228 CYS 228 228 228 CYS CYS B . n B 1 229 VAL 229 229 229 VAL VAL B . n B 1 230 THR 230 230 230 THR THR B . n B 1 231 ASN 231 231 231 ASN ASN B . n B 1 232 LEU 232 232 232 LEU LEU B . n B 1 233 GLN 233 233 233 GLN GLN B . n B 1 234 GLU 234 234 234 GLU GLU B . n B 1 235 VAL 235 235 235 VAL VAL B . n B 1 236 ALA 236 236 236 ALA ALA B . n B 1 237 ARG 237 237 237 ARG ARG B . n B 1 238 ILE 238 238 238 ILE ILE B . n B 1 239 VAL 239 239 239 VAL VAL B . n B 1 240 GLY 240 240 240 GLY GLY B . n B 1 241 ASN 241 241 241 ASN ASN B . n B 1 242 SER 242 242 242 SER SER B . n B 1 243 GLY 243 243 243 GLY GLY B . n B 1 244 LEU 244 244 244 LEU LEU B . n B 1 245 ASN 245 245 245 ASN ASN B . n B 1 246 ILE 246 246 246 ILE ILE B . n B 1 247 TYR 247 247 247 TYR TYR B . n B 1 248 ASN 248 248 248 ASN ASN B . n B 1 249 LEU 249 249 249 LEU LEU B . n B 1 250 TYR 250 250 250 TYR TYR B . n B 1 251 ALA 251 251 251 ALA ALA B . n B 1 252 PRO 252 252 252 PRO PRO B . n B 1 253 CYS 253 253 253 CYS CYS B . n B 1 254 ALA 254 254 254 ALA ALA B . n B 1 255 GLY 255 255 255 GLY GLY B . n B 1 256 GLY 256 256 256 GLY GLY B . n B 1 257 VAL 257 257 257 VAL VAL B . n B 1 258 PRO 258 258 258 PRO PRO B . n B 1 259 SER 259 289 ? ? ? B . n B 1 260 HIS 260 290 ? ? ? B . n B 1 261 PHE 261 291 ? ? ? B . n B 1 262 ARG 262 292 ? ? ? B . n B 1 263 SER 263 293 ? ? ? B . n B 1 264 GLY 264 294 ? ? ? B . n B 1 265 ASP 265 295 ? ? ? B . n B 1 266 LYS 266 296 ? ? ? B . n B 1 267 VAL 267 297 ? ? ? B . n B 1 268 ARG 268 298 298 ARG ARG B . n B 1 269 MET 269 299 299 MET MET B . n B 1 270 ASP 270 300 300 ASP ASP B . n B 1 271 PRO 271 301 301 PRO PRO B . n B 1 272 PRO 272 302 302 PRO PRO B . n B 1 273 CYS 273 303 303 CYS CYS B . n B 1 274 THR 274 304 304 THR THR B . n B 1 275 ASN 275 305 305 ASN ASN B . n B 1 276 THR 276 306 306 THR THR B . n B 1 277 THR 277 307 307 THR THR B . n B 1 278 ALA 278 308 308 ALA ALA B . n B 1 279 ALA 279 309 309 ALA ALA B . n B 1 280 SER 280 310 310 SER SER B . n B 1 281 THR 281 311 311 THR THR B . n B 1 282 TYR 282 312 312 TYR TYR B . n B 1 283 LEU 283 313 313 LEU LEU B . n B 1 284 ASN 284 314 314 ASN ASN B . n B 1 285 ASN 285 315 315 ASN ASN B . n B 1 286 PRO 286 316 316 PRO PRO B . n B 1 287 TYR 287 317 317 TYR TYR B . n B 1 288 VAL 288 318 318 VAL VAL B . n B 1 289 ARG 289 319 319 ARG ARG B . n B 1 290 LYS 290 320 320 LYS LYS B . n B 1 291 ALA 291 321 321 ALA ALA B . n B 1 292 LEU 292 322 322 LEU LEU B . n B 1 293 ASN 293 323 323 ASN ASN B . n B 1 294 ILE 294 324 324 ILE ILE B . n B 1 295 PRO 295 325 325 PRO PRO B . n B 1 296 GLU 296 326 326 GLU GLU B . n B 1 297 GLN 297 327 327 GLN GLN B . n B 1 298 LEU 298 328 328 LEU LEU B . n B 1 299 PRO 299 329 329 PRO PRO B . n B 1 300 GLN 300 330 330 GLN GLN B . n B 1 301 TRP 301 331 331 TRP TRP B . n B 1 302 ASP 302 332 332 ASP ASP B . n B 1 303 MET 303 333 333 MET MET B . n B 1 304 CYS 304 334 334 CYS CYS B . n B 1 305 ASN 305 335 335 ASN ASN B . n B 1 306 PHE 306 336 336 PHE PHE B . n B 1 307 LEU 307 337 337 LEU LEU B . n B 1 308 VAL 308 338 338 VAL VAL B . n B 1 309 ASN 309 339 339 ASN ASN B . n B 1 310 LEU 310 340 340 LEU LEU B . n B 1 311 GLN 311 341 341 GLN GLN B . n B 1 312 TYR 312 342 342 TYR TYR B . n B 1 313 ARG 313 343 343 ARG ARG B . n B 1 314 ARG 314 344 344 ARG ARG B . n B 1 315 LEU 315 345 345 LEU LEU B . n B 1 316 TYR 316 346 346 TYR TYR B . n B 1 317 ARG 317 347 347 ARG ARG B . n B 1 318 SER 318 348 348 SER SER B . n B 1 319 MET 319 349 349 MET MET B . n B 1 320 ASN 320 350 350 ASN ASN B . n B 1 321 SER 321 351 351 SER SER B . n B 1 322 GLN 322 352 352 GLN GLN B . n B 1 323 TYR 323 353 353 TYR TYR B . n B 1 324 LEU 324 354 354 LEU LEU B . n B 1 325 LYS 325 355 355 LYS LYS B . n B 1 326 LEU 326 356 356 LEU LEU B . n B 1 327 LEU 327 357 357 LEU LEU B . n B 1 328 SER 328 358 358 SER SER B . n B 1 329 SER 329 359 359 SER SER B . n B 1 330 GLN 330 360 360 GLN GLN B . n B 1 331 LYS 331 361 361 LYS LYS B . n B 1 332 TYR 332 362 362 TYR TYR B . n B 1 333 GLN 333 363 363 GLN GLN B . n B 1 334 ILE 334 364 364 ILE ILE B . n B 1 335 LEU 335 365 365 LEU LEU B . n B 1 336 LEU 336 366 366 LEU LEU B . n B 1 337 TYR 337 367 367 TYR TYR B . n B 1 338 ASN 338 368 368 ASN ASN B . n B 1 339 GLY 339 369 369 GLY GLY B . n B 1 340 ASP 340 370 370 ASP ASP B . n B 1 341 VAL 341 371 371 VAL VAL B . n B 1 342 ASP 342 372 372 ASP ASP B . n B 1 343 MET 343 373 373 MET MET B . n B 1 344 ALA 344 374 374 ALA ALA B . n B 1 345 CYS 345 375 375 CYS CYS B . n B 1 346 ASN 346 376 376 ASN ASN B . n B 1 347 PHE 347 377 377 PHE PHE B . n B 1 348 MET 348 378 378 MET MET B . n B 1 349 GLY 349 379 379 GLY GLY B . n B 1 350 ASP 350 380 380 ASP ASP B . n B 1 351 GLU 351 381 381 GLU GLU B . n B 1 352 TRP 352 382 382 TRP TRP B . n B 1 353 PHE 353 383 383 PHE PHE B . n B 1 354 VAL 354 384 384 VAL VAL B . n B 1 355 ASP 355 385 385 ASP ASP B . n B 1 356 SER 356 386 386 SER SER B . n B 1 357 LEU 357 387 387 LEU LEU B . n B 1 358 ASN 358 388 388 ASN ASN B . n B 1 359 GLN 359 389 389 GLN GLN B . n B 1 360 LYS 360 390 390 LYS LYS B . n B 1 361 MET 361 391 391 MET MET B . n B 1 362 GLU 362 392 392 GLU GLU B . n B 1 363 VAL 363 393 393 VAL VAL B . n B 1 364 GLN 364 394 394 GLN GLN B . n B 1 365 ARG 365 395 395 ARG ARG B . n B 1 366 ARG 366 396 396 ARG ARG B . n B 1 367 PRO 367 397 397 PRO PRO B . n B 1 368 TRP 368 398 398 TRP TRP B . n B 1 369 LEU 369 399 399 LEU LEU B . n B 1 370 VAL 370 400 400 VAL VAL B . n B 1 371 LYS 371 401 401 LYS LYS B . n B 1 372 TYR 372 402 402 TYR TYR B . n B 1 373 GLY 373 403 403 GLY GLY B . n B 1 374 ASP 374 404 404 ASP ASP B . n B 1 375 SER 375 405 405 SER SER B . n B 1 376 GLY 376 406 406 GLY GLY B . n B 1 377 GLU 377 407 407 GLU GLU B . n B 1 378 GLN 378 408 408 GLN GLN B . n B 1 379 ILE 379 409 409 ILE ILE B . n B 1 380 ALA 380 410 410 ALA ALA B . n B 1 381 GLY 381 411 411 GLY GLY B . n B 1 382 PHE 382 412 412 PHE PHE B . n B 1 383 VAL 383 413 413 VAL VAL B . n B 1 384 LYS 384 414 414 LYS LYS B . n B 1 385 GLU 385 415 415 GLU GLU B . n B 1 386 PHE 386 416 416 PHE PHE B . n B 1 387 SER 387 417 417 SER SER B . n B 1 388 HIS 388 418 418 HIS HIS B . n B 1 389 ILE 389 419 419 ILE ILE B . n B 1 390 ALA 390 420 420 ALA ALA B . n B 1 391 PHE 391 421 421 PHE PHE B . n B 1 392 LEU 392 422 422 LEU LEU B . n B 1 393 THR 393 423 423 THR THR B . n B 1 394 ILE 394 424 424 ILE ILE B . n B 1 395 LYS 395 425 425 LYS LYS B . n B 1 396 GLY 396 426 426 GLY GLY B . n B 1 397 ALA 397 427 427 ALA ALA B . n B 1 398 GLY 398 428 428 GLY GLY B . n B 1 399 HIS 399 429 429 HIS HIS B . n B 1 400 MET 400 430 430 MET MET B . n B 1 401 VAL 401 431 431 VAL VAL B . n B 1 402 PRO 402 432 432 PRO PRO B . n B 1 403 THR 403 433 433 THR THR B . n B 1 404 ASP 404 434 434 ASP ASP B . n B 1 405 LYS 405 435 435 LYS LYS B . n B 1 406 PRO 406 436 436 PRO PRO B . n B 1 407 LEU 407 437 437 LEU LEU B . n B 1 408 ALA 408 438 438 ALA ALA B . n B 1 409 ALA 409 439 439 ALA ALA B . n B 1 410 PHE 410 440 440 PHE PHE B . n B 1 411 THR 411 441 441 THR THR B . n B 1 412 MET 412 442 442 MET MET B . n B 1 413 PHE 413 443 443 PHE PHE B . n B 1 414 SER 414 444 444 SER SER B . n B 1 415 ARG 415 445 445 ARG ARG B . n B 1 416 PHE 416 446 446 PHE PHE B . n B 1 417 LEU 417 447 447 LEU LEU B . n B 1 418 ASN 418 448 448 ASN ASN B . n B 1 419 LYS 419 449 449 LYS LYS B . n B 1 420 GLN 420 450 450 GLN GLN B . n B 1 421 PRO 421 451 451 PRO PRO B . n B 1 422 TYR 422 452 452 TYR TYR B . n B 1 423 HIS 423 453 ? ? ? B . n B 1 424 HIS 424 454 ? ? ? B . n B 1 425 HIS 425 455 ? ? ? B . n B 1 426 HIS 426 456 ? ? ? B . n B 1 427 HIS 427 457 ? ? ? B . n B 1 428 HIS 428 458 ? ? ? B . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code C 2 NAG 1 501 501 NAG NAG A . D 2 NAG 2 502 502 NAG NAG A . E 3 BMA 3 503 503 BMA BMA A . F 2 NAG 1 504 506 NAG NAG A . G 2 NAG 1 501 501 NAG NAG B . H 2 NAG 1 502 505 NAG NAG B . # 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 B ASN 275 B ASN 305 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 117 A ASN 117 ? ASN 'GLYCOSYLATION SITE' 3 B ASN 117 B ASN 117 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 275 A ASN 305 ? 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 dimeric _pdbx_struct_assembly.oligomeric_count 2 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H # 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)' 4890 ? 1 MORE 1 ? 1 'SSA (A^2)' 32520 ? # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2014-03-12 2 'Structure model' 1 1 2015-04-15 3 'Structure model' 1 2 2017-08-23 # _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 3 'Structure model' 'Data collection' # _pdbx_audit_revision_category.ordinal 1 _pdbx_audit_revision_category.revision_ordinal 3 _pdbx_audit_revision_category.data_content_type 'Structure model' _pdbx_audit_revision_category.category diffrn_detector # _pdbx_audit_revision_item.ordinal 1 _pdbx_audit_revision_item.revision_ordinal 3 _pdbx_audit_revision_item.data_content_type 'Structure model' _pdbx_audit_revision_item.item '_diffrn_detector.detector' # 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 17.0301 -26.5758 -6.3634 0.1198 0.1154 0.0426 -0.0224 -0.0565 -0.0173 0.5283 0.9471 0.6241 -0.4361 -0.4927 0.2699 -0.0045 0.1108 0.0257 -0.1067 0.0012 0.0364 -0.0831 -0.0983 0.0033 'X-RAY DIFFRACTION' 2 ? refined 38.4834 -62.8614 -10.3275 0.1415 0.0711 0.0229 0.0357 0.0490 -0.0044 1.2212 1.1240 0.8569 -0.4457 0.0490 0.5418 -0.2384 -0.1357 -0.0374 0.0916 0.1648 -0.0309 0.2153 0.0612 0.0736 # 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 1 ? ? A 182 ? ? ? ? 'X-RAY DIFFRACTION' 2 1 A 183 ? ? A 303 ? ? ? ? 'X-RAY DIFFRACTION' 3 1 A 304 ? ? A 452 ? ? ? ? 'X-RAY DIFFRACTION' 4 2 B 1 ? ? B 182 ? ? ? ? 'X-RAY DIFFRACTION' 5 2 B 183 ? ? B 303 ? ? ? ? 'X-RAY DIFFRACTION' 6 2 B 304 ? ? B 452 ? ? ? ? # _phasing.method MR # loop_ _software.pdbx_ordinal _software.name _software.version _software.date _software.type _software.contact_author _software.contact_author_email _software.classification _software.location _software.language _software.citation_id 1 DENZO . ? program 'Zbyszek Otwinowski' hkl@hkl-xray.com 'data reduction' http://www.hkl-xray.com/ ? ? 2 SCALEPACK . ? program 'Zbyszek Otwinowski' hkl@hkl-xray.com 'data scaling' http://www.hkl-xray.com/ ? ? 3 PHASER . ? program 'Randy J. Read' cimr-phaser@lists.cam.ac.uk phasing http://www-structmed.cimr.cam.ac.uk/phaser/ ? ? 4 REFMAC 5.7.0029 ? program 'Garib N. Murshudov' garib@ysbl.york.ac.uk refinement http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 5 PDB_EXTRACT 3.11 'April 22, 2011' package PDB deposit@deposit.rcsb.org 'data extraction' http://sw-tools.pdb.org/apps/PDB_EXTRACT/ C++ ? # _pdbx_entry_details.entry_id 4MWT _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details ;AN UNIDENTIFIED PROTEASE CONVERTED THE ZYMOGEN INTO ACTIVE ENZYME. PUTATIVE TERMINI ASSUME PROTEOLYTIC REMOVAL OF 263-292, CONSISTENT WITH MASS SPECTROMETRY AND N-TERMINAL SEQUENCING DATA. ; _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? # 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 GLN A 8 ? ? -86.33 -79.43 2 1 ASP A 44 ? ? 59.78 75.27 3 1 HIS A 70 ? ? -144.34 23.32 4 1 LYS A 112 ? ? 59.57 16.24 5 1 PHE A 136 ? ? -119.90 64.74 6 1 SER A 150 ? ? 61.72 -131.99 7 1 ASN A 170 ? ? -91.07 59.56 8 1 ASN A 178 ? ? 34.02 59.87 9 1 GLN A 215 ? ? 35.22 85.19 10 1 ASN A 216 ? ? 83.36 13.43 11 1 SER A 242 ? ? -144.71 13.74 12 1 ASN A 248 ? ? -161.67 100.19 13 1 ASN A 388 ? ? 47.33 74.60 14 1 GLU A 392 ? ? -108.30 -83.22 15 1 ASP A 404 ? ? 79.56 -48.74 16 1 HIS A 418 ? ? 76.65 -6.27 17 1 GLN B 8 ? ? -85.62 -78.95 18 1 ASP B 44 ? ? 58.42 75.78 19 1 HIS B 70 ? ? -144.60 23.65 20 1 LYS B 112 ? ? 59.35 17.53 21 1 SER B 150 ? ? 61.83 -131.97 22 1 ASN B 170 ? ? -90.30 59.00 23 1 ASN B 178 ? ? 33.40 60.88 24 1 SER B 242 ? ? -144.30 13.73 25 1 ASN B 248 ? ? -161.46 100.05 26 1 ASN B 388 ? ? 48.16 74.49 27 1 GLU B 392 ? ? -108.82 -83.36 28 1 ASP B 404 ? ? 78.71 -47.44 29 1 HIS B 418 ? ? 73.01 -3.09 # 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 SER 289 ? A SER 259 2 1 Y 1 A HIS 290 ? A HIS 260 3 1 Y 1 A PHE 291 ? A PHE 261 4 1 Y 1 A ARG 292 ? A ARG 262 5 1 Y 1 A SER 293 ? A SER 263 6 1 Y 1 A GLY 294 ? A GLY 264 7 1 Y 1 A ASP 295 ? A ASP 265 8 1 Y 1 A LYS 296 ? A LYS 266 9 1 Y 1 A VAL 297 ? A VAL 267 10 1 Y 1 A HIS 453 ? A HIS 423 11 1 Y 1 A HIS 454 ? A HIS 424 12 1 Y 1 A HIS 455 ? A HIS 425 13 1 Y 1 A HIS 456 ? A HIS 426 14 1 Y 1 A HIS 457 ? A HIS 427 15 1 Y 1 A HIS 458 ? A HIS 428 16 1 Y 1 B SER 289 ? B SER 259 17 1 Y 1 B HIS 290 ? B HIS 260 18 1 Y 1 B PHE 291 ? B PHE 261 19 1 Y 1 B ARG 292 ? B ARG 262 20 1 Y 1 B SER 293 ? B SER 263 21 1 Y 1 B GLY 294 ? B GLY 264 22 1 Y 1 B ASP 295 ? B ASP 265 23 1 Y 1 B LYS 296 ? B LYS 266 24 1 Y 1 B VAL 297 ? B VAL 267 25 1 Y 1 B HIS 453 ? B HIS 423 26 1 Y 1 B HIS 454 ? B HIS 424 27 1 Y 1 B HIS 455 ? B HIS 425 28 1 Y 1 B HIS 456 ? B HIS 426 29 1 Y 1 B HIS 457 ? B HIS 427 30 1 Y 1 B HIS 458 ? B HIS 428 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 BETA-D-MANNOSE BMA #