data_1OJJ # _entry.id 1OJJ # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.279 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 1OJJ PDBE EBI-12650 WWPDB D_1290012650 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 1A39 unspecified 'HUMICOLA INSOLENS ENDOCELLULASE EGI S37W, P39W DOUBLE-MUTANT' PDB 1DYM unspecified 'HUMICOLA INSOLENS ENDOCELLULASE CEL7B (EG 1) E197A MUTANT' PDB 1OJI unspecified 'ANATOMY OF GLYCOSYNTHESIS: STRUCTURE AND KINETICS OF THE HUMICOLA INSOLENS CEL7BE197A AND E197S GLYCOSYNTHASE MUTANTS' PDB 1OJK unspecified 'ANATOMY OF GLYCOSYNTHESIS: STRUCTURE AND KINETICS OF THE HUMICOLA INSOLENS CEL7BE197A AND E197S GLYCOSYNTHASE MUTANTS' PDB 2A39 unspecified 'HUMICOLA INSOLENS ENDOCELLULASE EGI NATIVE STRUCTURE' # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 1OJJ _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2003-07-10 _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Ducros, V.M.-A.' 1 'Tarling, C.A.' 2 'Zechel, D.L.' 3 'Brzozowski, A.M.' 4 'Frandsen, T.P.' 5 'Von Ossowski, I.' 6 'Schulein, M.' 7 'Withers, S.G.' 8 'Davies, G.J.' 9 # _citation.id primary _citation.title 'Anatomy of Glycosynthesis: Structure and Kinetics of the Humicola Insolens Cel7B E197A and E197S Glycosynthase Mutants' _citation.journal_abbrev Chem.Biol. _citation.journal_volume 10 _citation.page_first 619 _citation.page_last ? _citation.year 2003 _citation.journal_id_ASTM CBOLE2 _citation.country UK _citation.journal_id_ISSN 1074-5521 _citation.journal_id_CSD 2050 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 12890535 _citation.pdbx_database_id_DOI '10.1016/S1074-5521(03)00143-1' # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Ducros, V.M.-A.' 1 primary 'Tarling, C.A.' 2 primary 'Zechel, D.L.' 3 primary 'Brzozowski, A.M.' 4 primary 'Frandsen, T.P.' 5 primary 'Von Ossowski, I.' 6 primary 'Schulein, M.' 7 primary 'Withers, S.G.' 8 primary 'Davies, G.J.' 9 # _cell.entry_id 1OJJ _cell.length_a 66.364 _cell.length_b 74.746 _cell.length_c 85.820 _cell.angle_alpha 90.00 _cell.angle_beta 102.51 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _cell.pdbx_unique_axis ? # _symmetry.entry_id 1OJJ _symmetry.space_group_name_H-M 'P 1 21 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 4 # 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 'ENDOGLUCANASE I' 44568.109 2 3.2.1.4 YES ? ? 2 non-polymer man BETA-D-GLUCOSE 180.156 2 ? ? ? ? 3 non-polymer man BETA-D-GALACTOSE 180.156 4 ? ? ? ? 4 non-polymer man ALPHA-D-GLUCOSE 180.156 2 ? ? ? ? 5 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 2 ? ? ? ? 6 water nat water 18.015 642 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name ENDO-1,4-BETA-GLUCANASE # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer yes _entity_poly.pdbx_seq_one_letter_code ;(PCA)KPGETKEVHPQLTTFRCTKRGGCKPATNFIVLDSLSHPIHRAEGLGPGGCGDWGNPPPKDVCPDVESCAKNCIME GIPDYSQYGVTTNGTSLRLQHILPDGRVPSPRVYLLDKTKRRYEMLHLTGFEFTFDVDATKLPCGMNSALYLSEMHPTGA KSKYNPGGAYYGTGYCDAQCFVTPFINGLGNIEGKGSCCNSMDIWEANSRASHVAPHTCNKKGLYLCEGEECAFEGVCDK NGCGWNNYRVNVTDYYGRGEEFKVNTLKPFTVVTQFLANRRGKLEKIHRFYVQDGKVIESFYTNKEGVPYTNMIDDEFCE ATGSRKYMELGATQGMGEALTRGMVLAMSIWWDQGGNMEWLDHGEAGPCAKGEGAPSNIVQVEPFPEVTYTNLRWGEIGS TYQELQ ; _entity_poly.pdbx_seq_one_letter_code_can ;EKPGETKEVHPQLTTFRCTKRGGCKPATNFIVLDSLSHPIHRAEGLGPGGCGDWGNPPPKDVCPDVESCAKNCIMEGIPD YSQYGVTTNGTSLRLQHILPDGRVPSPRVYLLDKTKRRYEMLHLTGFEFTFDVDATKLPCGMNSALYLSEMHPTGAKSKY NPGGAYYGTGYCDAQCFVTPFINGLGNIEGKGSCCNSMDIWEANSRASHVAPHTCNKKGLYLCEGEECAFEGVCDKNGCG WNNYRVNVTDYYGRGEEFKVNTLKPFTVVTQFLANRRGKLEKIHRFYVQDGKVIESFYTNKEGVPYTNMIDDEFCEATGS RKYMELGATQGMGEALTRGMVLAMSIWWDQGGNMEWLDHGEAGPCAKGEGAPSNIVQVEPFPEVTYTNLRWGEIGSTYQE LQ ; _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 PCA n 1 2 LYS n 1 3 PRO n 1 4 GLY n 1 5 GLU n 1 6 THR n 1 7 LYS n 1 8 GLU n 1 9 VAL n 1 10 HIS n 1 11 PRO n 1 12 GLN n 1 13 LEU n 1 14 THR n 1 15 THR n 1 16 PHE n 1 17 ARG n 1 18 CYS n 1 19 THR n 1 20 LYS n 1 21 ARG n 1 22 GLY n 1 23 GLY n 1 24 CYS n 1 25 LYS n 1 26 PRO n 1 27 ALA n 1 28 THR n 1 29 ASN n 1 30 PHE n 1 31 ILE n 1 32 VAL n 1 33 LEU n 1 34 ASP n 1 35 SER n 1 36 LEU n 1 37 SER n 1 38 HIS n 1 39 PRO n 1 40 ILE n 1 41 HIS n 1 42 ARG n 1 43 ALA n 1 44 GLU n 1 45 GLY n 1 46 LEU n 1 47 GLY n 1 48 PRO n 1 49 GLY n 1 50 GLY n 1 51 CYS n 1 52 GLY n 1 53 ASP n 1 54 TRP n 1 55 GLY n 1 56 ASN n 1 57 PRO n 1 58 PRO n 1 59 PRO n 1 60 LYS n 1 61 ASP n 1 62 VAL n 1 63 CYS n 1 64 PRO n 1 65 ASP n 1 66 VAL n 1 67 GLU n 1 68 SER n 1 69 CYS n 1 70 ALA n 1 71 LYS n 1 72 ASN n 1 73 CYS n 1 74 ILE n 1 75 MET n 1 76 GLU n 1 77 GLY n 1 78 ILE n 1 79 PRO n 1 80 ASP n 1 81 TYR n 1 82 SER n 1 83 GLN n 1 84 TYR n 1 85 GLY n 1 86 VAL n 1 87 THR n 1 88 THR n 1 89 ASN n 1 90 GLY n 1 91 THR n 1 92 SER n 1 93 LEU n 1 94 ARG n 1 95 LEU n 1 96 GLN n 1 97 HIS n 1 98 ILE n 1 99 LEU n 1 100 PRO n 1 101 ASP n 1 102 GLY n 1 103 ARG n 1 104 VAL n 1 105 PRO n 1 106 SER n 1 107 PRO n 1 108 ARG n 1 109 VAL n 1 110 TYR n 1 111 LEU n 1 112 LEU n 1 113 ASP n 1 114 LYS n 1 115 THR n 1 116 LYS n 1 117 ARG n 1 118 ARG n 1 119 TYR n 1 120 GLU n 1 121 MET n 1 122 LEU n 1 123 HIS n 1 124 LEU n 1 125 THR n 1 126 GLY n 1 127 PHE n 1 128 GLU n 1 129 PHE n 1 130 THR n 1 131 PHE n 1 132 ASP n 1 133 VAL n 1 134 ASP n 1 135 ALA n 1 136 THR n 1 137 LYS n 1 138 LEU n 1 139 PRO n 1 140 CYS n 1 141 GLY n 1 142 MET n 1 143 ASN n 1 144 SER n 1 145 ALA n 1 146 LEU n 1 147 TYR n 1 148 LEU n 1 149 SER n 1 150 GLU n 1 151 MET n 1 152 HIS n 1 153 PRO n 1 154 THR n 1 155 GLY n 1 156 ALA n 1 157 LYS n 1 158 SER n 1 159 LYS n 1 160 TYR n 1 161 ASN n 1 162 PRO n 1 163 GLY n 1 164 GLY n 1 165 ALA n 1 166 TYR n 1 167 TYR n 1 168 GLY n 1 169 THR n 1 170 GLY n 1 171 TYR n 1 172 CYS n 1 173 ASP n 1 174 ALA n 1 175 GLN n 1 176 CYS n 1 177 PHE n 1 178 VAL n 1 179 THR n 1 180 PRO n 1 181 PHE n 1 182 ILE n 1 183 ASN n 1 184 GLY n 1 185 LEU n 1 186 GLY n 1 187 ASN n 1 188 ILE n 1 189 GLU n 1 190 GLY n 1 191 LYS n 1 192 GLY n 1 193 SER n 1 194 CYS n 1 195 CYS n 1 196 ASN n 1 197 SER n 1 198 MET n 1 199 ASP n 1 200 ILE n 1 201 TRP n 1 202 GLU n 1 203 ALA n 1 204 ASN n 1 205 SER n 1 206 ARG n 1 207 ALA n 1 208 SER n 1 209 HIS n 1 210 VAL n 1 211 ALA n 1 212 PRO n 1 213 HIS n 1 214 THR n 1 215 CYS n 1 216 ASN n 1 217 LYS n 1 218 LYS n 1 219 GLY n 1 220 LEU n 1 221 TYR n 1 222 LEU n 1 223 CYS n 1 224 GLU n 1 225 GLY n 1 226 GLU n 1 227 GLU n 1 228 CYS n 1 229 ALA n 1 230 PHE n 1 231 GLU n 1 232 GLY n 1 233 VAL n 1 234 CYS n 1 235 ASP n 1 236 LYS n 1 237 ASN n 1 238 GLY n 1 239 CYS n 1 240 GLY n 1 241 TRP n 1 242 ASN n 1 243 ASN n 1 244 TYR n 1 245 ARG n 1 246 VAL n 1 247 ASN n 1 248 VAL n 1 249 THR n 1 250 ASP n 1 251 TYR n 1 252 TYR n 1 253 GLY n 1 254 ARG n 1 255 GLY n 1 256 GLU n 1 257 GLU n 1 258 PHE n 1 259 LYS n 1 260 VAL n 1 261 ASN n 1 262 THR n 1 263 LEU n 1 264 LYS n 1 265 PRO n 1 266 PHE n 1 267 THR n 1 268 VAL n 1 269 VAL n 1 270 THR n 1 271 GLN n 1 272 PHE n 1 273 LEU n 1 274 ALA n 1 275 ASN n 1 276 ARG n 1 277 ARG n 1 278 GLY n 1 279 LYS n 1 280 LEU n 1 281 GLU n 1 282 LYS n 1 283 ILE n 1 284 HIS n 1 285 ARG n 1 286 PHE n 1 287 TYR n 1 288 VAL n 1 289 GLN n 1 290 ASP n 1 291 GLY n 1 292 LYS n 1 293 VAL n 1 294 ILE n 1 295 GLU n 1 296 SER n 1 297 PHE n 1 298 TYR n 1 299 THR n 1 300 ASN n 1 301 LYS n 1 302 GLU n 1 303 GLY n 1 304 VAL n 1 305 PRO n 1 306 TYR n 1 307 THR n 1 308 ASN n 1 309 MET n 1 310 ILE n 1 311 ASP n 1 312 ASP n 1 313 GLU n 1 314 PHE n 1 315 CYS n 1 316 GLU n 1 317 ALA n 1 318 THR n 1 319 GLY n 1 320 SER n 1 321 ARG n 1 322 LYS n 1 323 TYR n 1 324 MET n 1 325 GLU n 1 326 LEU n 1 327 GLY n 1 328 ALA n 1 329 THR n 1 330 GLN n 1 331 GLY n 1 332 MET n 1 333 GLY n 1 334 GLU n 1 335 ALA n 1 336 LEU n 1 337 THR n 1 338 ARG n 1 339 GLY n 1 340 MET n 1 341 VAL n 1 342 LEU n 1 343 ALA n 1 344 MET n 1 345 SER n 1 346 ILE n 1 347 TRP n 1 348 TRP n 1 349 ASP n 1 350 GLN n 1 351 GLY n 1 352 GLY n 1 353 ASN n 1 354 MET n 1 355 GLU n 1 356 TRP n 1 357 LEU n 1 358 ASP n 1 359 HIS n 1 360 GLY n 1 361 GLU n 1 362 ALA n 1 363 GLY n 1 364 PRO n 1 365 CYS n 1 366 ALA n 1 367 LYS n 1 368 GLY n 1 369 GLU n 1 370 GLY n 1 371 ALA n 1 372 PRO n 1 373 SER n 1 374 ASN n 1 375 ILE n 1 376 VAL n 1 377 GLN n 1 378 VAL n 1 379 GLU n 1 380 PRO n 1 381 PHE n 1 382 PRO n 1 383 GLU n 1 384 VAL n 1 385 THR n 1 386 TYR n 1 387 THR n 1 388 ASN n 1 389 LEU n 1 390 ARG n 1 391 TRP n 1 392 GLY n 1 393 GLU n 1 394 ILE n 1 395 GLY n 1 396 SER n 1 397 THR n 1 398 TYR n 1 399 GLN n 1 400 GLU n 1 401 LEU n 1 402 GLN n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name ? _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene ? _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'HUMICOLA INSOLENS' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 34413 _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 'ASPERGILLUS ORYZAE' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 5062 _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type ? _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name ? _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code GUN1_HUMIN _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_align_begin ? _struct_ref.pdbx_db_accession P56680 _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 1OJJ A 1 ? 402 ? P56680 1 ? 402 ? 1 402 2 1 1OJJ B 1 ? 402 ? P56680 1 ? 402 ? 1 402 # 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 1OJJ SER A 197 ? UNP P56680 GLU 197 'engineered mutation' 197 1 2 1OJJ SER B 197 ? UNP P56680 GLU 197 'engineered mutation' 197 2 # 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 BGC saccharide . BETA-D-GLUCOSE ? 'C6 H12 O6' 180.156 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GAL D-saccharide . BETA-D-GALACTOSE ? 'C6 H12 O6' 180.156 GLC saccharide . ALPHA-D-GLUCOSE ? 'C6 H12 O6' 180.156 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 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 PCA 'L-peptide linking' n 'PYROGLUTAMIC ACID' ? 'C5 H7 N O3' 129.114 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 1OJJ _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.4 _exptl_crystal.density_percent_sol 47.5 _exptl_crystal.description ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 7.00 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details 'HANGING DROPS 20MM TRIS-HCL PH7-8.5, 280 15-30% POLYETHYLENE GLYCOL 4000, pH 7.00' # _diffrn.id 1 _diffrn.ambient_temp 100.0 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type MARRESEARCH _diffrn_detector.pdbx_collection_date ? _diffrn_detector.details MIRRORS # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.93400 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'ESRF BEAMLINE ID14-1' _diffrn_source.pdbx_synchrotron_site ESRF _diffrn_source.pdbx_synchrotron_beamline ID14-1 _diffrn_source.pdbx_wavelength 0.93400 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 1OJJ _reflns.observed_criterion_sigma_I ? _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 15.000 _reflns.d_resolution_high 1.400 _reflns.number_obs 157771 _reflns.number_all ? _reflns.percent_possible_obs 99.0 _reflns.pdbx_Rmerge_I_obs 0.03300 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 35.0000 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 3.600 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 1.40 _reflns_shell.d_res_low 1.45 _reflns_shell.percent_possible_all 96.0 _reflns_shell.Rmerge_I_obs 0.30000 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 3.500 _reflns_shell.pdbx_redundancy 3.20 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 1OJJ _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 149738 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 84.52 _refine.ls_d_res_high 1.40 _refine.ls_percent_reflns_obs 98.7 _refine.ls_R_factor_obs 0.150 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.149 _refine.ls_R_factor_R_free 0.173 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.000 _refine.ls_number_reflns_R_free 7945 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.970 _refine.correlation_coeff_Fo_to_Fc_free 0.960 _refine.B_iso_mean 11.65 _refine.aniso_B[1][1] 0.17000 _refine.aniso_B[2][2] -0.31000 _refine.aniso_B[3][3] 0.03000 _refine.aniso_B[1][2] 0.00000 _refine.aniso_B[1][3] -0.25000 _refine.aniso_B[2][3] 0.00000 _refine.solvent_model_details 'BABINET MODEL WITH MASK' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' _refine.pdbx_starting_model 'PDB ENTRY 1DYM' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.060 _refine.pdbx_overall_ESU_R_Free 0.053 _refine.overall_SU_ML 0.029 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 1.543 _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 6170 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 120 _refine_hist.number_atoms_solvent 642 _refine_hist.number_atoms_total 6932 _refine_hist.d_res_high 1.40 _refine_hist.d_res_low 84.52 # 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 0.012 0.022 ? 6530 'X-RAY DIFFRACTION' ? r_bond_other_d 0.001 0.020 ? 5579 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.569 1.963 ? 8873 'X-RAY DIFFRACTION' ? r_angle_other_deg 0.848 3.000 ? 13057 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 6.234 5.000 ? 794 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 31.314 24.181 ? 299 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 12.129 15.000 ? 1040 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 17.231 15.000 ? 36 'X-RAY DIFFRACTION' ? r_chiral_restr 0.096 0.200 ? 942 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.007 0.020 ? 7228 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.001 0.020 ? 1302 'X-RAY DIFFRACTION' ? r_nbd_refined 0.213 0.200 ? 1110 'X-RAY DIFFRACTION' ? r_nbd_other 0.189 0.200 ? 5477 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other 0.083 0.200 ? 3415 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined 0.089 0.200 ? 358 '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 0.211 0.200 ? 12 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other 0.179 0.200 ? 56 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined 0.208 0.200 ? 27 '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 1.426 1.500 ? 5084 'X-RAY DIFFRACTION' ? r_mcbond_other 0.472 1.500 ? 1638 'X-RAY DIFFRACTION' ? r_mcangle_it 1.664 2.000 ? 6357 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it 2.602 3.000 ? 3055 'X-RAY DIFFRACTION' ? r_scbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_it 3.398 4.500 ? 2516 'X-RAY DIFFRACTION' ? r_scangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.40 _refine_ls_shell.d_res_low 1.44 _refine_ls_shell.number_reflns_R_work 10236 _refine_ls_shell.R_factor_R_work 0.1570 _refine_ls_shell.percent_reflns_obs ? _refine_ls_shell.R_factor_R_free 0.2060 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 517 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct_ncs_oper.id 1 _struct_ncs_oper.code given _struct_ncs_oper.details ? _struct_ncs_oper.matrix[1][1] 0.999440 _struct_ncs_oper.matrix[1][2] -0.031900 _struct_ncs_oper.matrix[1][3] -0.010070 _struct_ncs_oper.matrix[2][1] 0.032340 _struct_ncs_oper.matrix[2][2] 0.998350 _struct_ncs_oper.matrix[2][3] 0.047440 _struct_ncs_oper.matrix[3][1] 0.008540 _struct_ncs_oper.matrix[3][2] -0.047740 _struct_ncs_oper.matrix[3][3] 0.998820 _struct_ncs_oper.vector[1] 23.90932 _struct_ncs_oper.vector[2] 0.50131 _struct_ncs_oper.vector[3] 42.00525 # _struct.entry_id 1OJJ _struct.title 'Anatomy of glycosynthesis: Structure and kinetics of the Humicola insolens Cel7BE197A and E197S glycosynthase mutants' _struct.pdbx_descriptor 'ENDOGLUCANASE I (E.C.3.2.1.4)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 1OJJ _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'HYDROLASE, CELLULOSE DEGRADATION, GLYCOSYNTHASE' # 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 3 ? E N N 4 ? F N N 3 ? G N N 5 ? H N N 5 ? I N N 2 ? J N N 3 ? K N N 4 ? L N N 3 ? M N N 6 ? N N N 6 ? # _struct_biol.id 1 # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 SER A 35 ? HIS A 38 ? SER A 35 HIS A 38 5 ? 4 HELX_P HELX_P2 2 ASP A 65 ? ASN A 72 ? ASP A 65 ASN A 72 1 ? 8 HELX_P HELX_P3 3 ASP A 80 ? TYR A 84 ? ASP A 80 TYR A 84 5 ? 5 HELX_P HELX_P4 4 GLY A 163 ? GLY A 168 ? GLY A 163 GLY A 168 5 ? 6 HELX_P HELX_P5 5 GLU A 224 ? ALA A 229 ? GLU A 224 ALA A 229 5 ? 6 HELX_P HELX_P6 6 ASN A 242 ? ASN A 247 ? ASN A 242 ASN A 247 5 ? 6 HELX_P HELX_P7 7 ASP A 311 ? THR A 318 ? ASP A 311 THR A 318 1 ? 8 HELX_P HELX_P8 8 SER A 320 ? LEU A 326 ? SER A 320 LEU A 326 1 ? 7 HELX_P HELX_P9 9 GLY A 327 ? GLY A 339 ? GLY A 327 GLY A 339 1 ? 13 HELX_P HELX_P10 10 MET A 354 ? HIS A 359 ? MET A 354 HIS A 359 1 ? 6 HELX_P HELX_P11 11 GLY A 360 ? GLY A 363 ? GLY A 360 GLY A 363 5 ? 4 HELX_P HELX_P12 12 ALA A 371 ? GLU A 379 ? ALA A 371 GLU A 379 1 ? 9 HELX_P HELX_P13 13 SER B 35 ? HIS B 38 ? SER B 35 HIS B 38 5 ? 4 HELX_P HELX_P14 14 ASP B 65 ? ASN B 72 ? ASP B 65 ASN B 72 1 ? 8 HELX_P HELX_P15 15 ASP B 80 ? TYR B 84 ? ASP B 80 TYR B 84 5 ? 5 HELX_P HELX_P16 16 GLY B 163 ? GLY B 168 ? GLY B 163 GLY B 168 5 ? 6 HELX_P HELX_P17 17 GLU B 224 ? ALA B 229 ? GLU B 224 ALA B 229 5 ? 6 HELX_P HELX_P18 18 ASN B 242 ? ASN B 247 ? ASN B 242 ASN B 247 5 ? 6 HELX_P HELX_P19 19 ASP B 311 ? THR B 318 ? ASP B 311 THR B 318 1 ? 8 HELX_P HELX_P20 20 SER B 320 ? LEU B 326 ? SER B 320 LEU B 326 1 ? 7 HELX_P HELX_P21 21 GLY B 327 ? GLY B 339 ? GLY B 327 GLY B 339 1 ? 13 HELX_P HELX_P22 22 MET B 354 ? HIS B 359 ? MET B 354 HIS B 359 1 ? 6 HELX_P HELX_P23 23 GLY B 360 ? GLY B 363 ? GLY B 360 GLY B 363 5 ? 4 HELX_P HELX_P24 24 ALA B 371 ? GLU B 379 ? ALA B 371 GLU B 379 1 ? 9 # _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 18 SG ? ? ? 1_555 A CYS 24 SG ? ? A CYS 18 A CYS 24 1_555 ? ? ? ? ? ? ? 2.112 ? disulf2 disulf ? ? A CYS 51 SG ? ? ? 1_555 A CYS 73 SG ? ? A CYS 51 A CYS 73 1_555 ? ? ? ? ? ? ? 2.025 ? disulf3 disulf ? ? A CYS 63 SG ? ? ? 1_555 A CYS 69 SG ? ? A CYS 63 A CYS 69 1_555 ? ? ? ? ? ? ? 2.086 ? disulf4 disulf ? ? A CYS 140 SG ? ? ? 1_555 A CYS 365 SG ? ? A CYS 140 A CYS 365 1_555 ? ? ? ? ? ? ? 2.046 ? disulf5 disulf ? ? A CYS 172 SG ? ? ? 1_555 A CYS 195 SG ? ? A CYS 172 A CYS 195 1_555 ? ? ? ? ? ? ? 2.056 ? disulf6 disulf ? ? A CYS 176 SG ? ? ? 1_555 A CYS 194 SG ? ? A CYS 176 A CYS 194 1_555 ? ? ? ? ? ? ? 2.058 ? disulf7 disulf ? ? A CYS 215 SG ? ? ? 1_555 A CYS 234 SG ? ? A CYS 215 A CYS 234 1_555 ? ? ? ? ? ? ? 2.023 ? disulf8 disulf ? ? A CYS 223 SG ? ? ? 1_555 A CYS 228 SG ? ? A CYS 223 A CYS 228 1_555 ? ? ? ? ? ? ? 2.067 ? disulf9 disulf ? ? A CYS 239 SG ? ? ? 1_555 A CYS 315 SG ? ? A CYS 239 A CYS 315 1_555 ? ? ? ? ? ? ? 2.039 ? disulf10 disulf ? ? B CYS 18 SG ? ? ? 1_555 B CYS 24 SG ? ? B CYS 18 B CYS 24 1_555 ? ? ? ? ? ? ? 2.076 ? disulf11 disulf ? ? B CYS 51 SG ? ? ? 1_555 B CYS 73 SG ? ? B CYS 51 B CYS 73 1_555 ? ? ? ? ? ? ? 2.019 ? disulf12 disulf ? ? B CYS 63 SG ? ? ? 1_555 B CYS 69 SG ? ? B CYS 63 B CYS 69 1_555 ? ? ? ? ? ? ? 2.068 ? disulf13 disulf ? ? B CYS 140 SG ? ? ? 1_555 B CYS 365 SG ? ? B CYS 140 B CYS 365 1_555 ? ? ? ? ? ? ? 2.059 ? disulf14 disulf ? ? B CYS 172 SG ? ? ? 1_555 B CYS 195 SG ? ? B CYS 172 B CYS 195 1_555 ? ? ? ? ? ? ? 2.024 ? disulf15 disulf ? ? B CYS 176 SG ? ? ? 1_555 B CYS 194 SG ? ? B CYS 176 B CYS 194 1_555 ? ? ? ? ? ? ? 2.034 ? disulf16 disulf ? ? B CYS 215 SG ? ? ? 1_555 B CYS 234 SG ? ? B CYS 215 B CYS 234 1_555 ? ? ? ? ? ? ? 2.044 ? disulf17 disulf ? ? B CYS 223 SG ? ? ? 1_555 B CYS 228 SG ? ? B CYS 223 B CYS 228 1_555 ? ? ? ? ? ? ? 2.052 ? disulf18 disulf ? ? B CYS 239 SG ? ? ? 1_555 B CYS 315 SG ? ? B CYS 239 B CYS 315 1_555 ? ? ? ? ? ? ? 2.027 ? covale1 covale ? ? A PCA 1 C ? ? ? 1_555 A LYS 2 N ? ? A PCA 1 A LYS 2 1_555 ? ? ? ? ? ? ? 1.326 ? covale2 covale ? ? A ASN 247 ND2 ? ? ? 1_555 G NAG . C1 ? ? A ASN 247 A NAG 1404 1_555 ? ? ? ? ? ? ? 1.462 ? covale3 covale ? ? C BGC . O4 ? ? ? 1_555 D GAL . C1 ? ? A BGC 1400 A GAL 1403 1_555 ? ? ? ? ? ? ? 1.442 ? covale4 covale ? ? E GLC . O4 ? ? ? 1_555 F GAL . C1 ? ? A GLC 1401 A GAL 1402 1_555 ? ? ? ? ? ? ? 1.424 ? covale5 covale ? ? B PCA 1 C ? ? ? 1_555 B LYS 2 N ? ? B PCA 1 B LYS 2 1_555 ? ? ? ? ? ? ? 1.325 ? covale6 covale ? ? B ASN 247 ND2 ? ? ? 1_555 H NAG . C1 ? ? B ASN 247 B NAG 1399 1_555 ? ? ? ? ? ? ? 1.440 ? covale7 covale ? ? I BGC . O4 ? ? ? 1_555 J GAL . C1 ? ? B BGC 1401 B GAL 1404 1_555 ? ? ? ? ? ? ? 1.431 ? covale8 covale ? ? K GLC . O4 ? ? ? 1_555 L GAL . C1 ? ? B GLC 1402 B GAL 1403 1_555 ? ? ? ? ? ? ? 1.430 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA ? 7 ? AB ? 7 ? AC ? 2 ? AD ? 3 ? AE ? 2 ? AF ? 2 ? BA ? 10 ? BB ? 7 ? BC ? 2 ? BD ? 3 ? BE ? 2 ? BF ? 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 AA 1 2 ? anti-parallel AA 2 3 ? anti-parallel AA 3 4 ? parallel AA 4 5 ? anti-parallel AA 5 6 ? anti-parallel AA 6 7 ? anti-parallel AB 1 2 ? anti-parallel AB 2 3 ? anti-parallel AB 3 4 ? anti-parallel AB 4 5 ? anti-parallel AB 5 6 ? anti-parallel AB 6 7 ? anti-parallel AC 1 2 ? anti-parallel AD 1 2 ? anti-parallel AD 2 3 ? anti-parallel AE 1 2 ? anti-parallel AF 1 2 ? parallel BA 1 2 ? anti-parallel BA 2 3 ? anti-parallel BA 3 4 ? parallel BA 4 5 ? anti-parallel BA 5 6 ? anti-parallel BA 6 7 ? anti-parallel BA 7 8 ? anti-parallel BA 8 9 ? anti-parallel BA 9 10 ? anti-parallel BB 1 2 ? anti-parallel BB 2 3 ? anti-parallel BB 3 4 ? anti-parallel BB 4 5 ? anti-parallel BB 5 6 ? anti-parallel BB 6 7 ? anti-parallel BC 1 2 ? anti-parallel BD 1 2 ? anti-parallel BD 2 3 ? anti-parallel BE 1 2 ? anti-parallel BF 1 2 ? parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id AA 1 VAL A 86 ? ASN A 89 ? VAL A 86 ASN A 89 AA 2 SER A 92 ? GLN A 96 ? SER A 92 GLN A 96 AA 3 GLU A 383 ? GLY A 392 ? GLU A 383 GLY A 392 AA 4 GLN A 12 ? THR A 19 ? GLN A 12 THR A 19 AA 5 GLY A 23 ? LEU A 33 ? GLY A 23 LEU A 33 AA 6 ARG A 108 ? LEU A 112 ? ARG A 108 LEU A 112 AA 7 MET A 340 ? TRP A 347 ? MET A 340 TRP A 347 AB 1 VAL A 86 ? ASN A 89 ? VAL A 86 ASN A 89 AB 2 SER A 92 ? GLN A 96 ? SER A 92 GLN A 96 AB 3 GLU A 383 ? GLY A 392 ? GLU A 383 GLY A 392 AB 4 GLU A 128 ? ASP A 134 ? GLU A 128 ASP A 134 AB 5 PHE A 266 ? ALA A 274 ? PHE A 266 ALA A 274 AB 6 LEU A 280 ? GLN A 289 ? LEU A 280 GLN A 289 AB 7 LYS A 292 ? ILE A 294 ? LYS A 292 ILE A 294 AC 1 ILE A 40 ? ARG A 42 ? ILE A 40 ARG A 42 AC 2 CYS A 73 ? MET A 75 ? CYS A 73 MET A 75 AD 1 PHE A 177 ? VAL A 178 ? PHE A 177 VAL A 178 AD 2 GLY A 192 ? CYS A 194 ? GLY A 192 CYS A 194 AD 3 TYR A 221 ? CYS A 223 ? TYR A 221 CYS A 223 AE 1 PHE A 181 ? ILE A 182 ? PHE A 181 ILE A 182 AE 2 LEU A 185 ? GLY A 186 ? LEU A 185 GLY A 186 AF 1 TYR A 252 ? GLY A 253 ? TYR A 252 GLY A 253 AF 2 VAL A 260 ? ASN A 261 ? VAL A 260 ASN A 261 BA 1 VAL B 86 ? ASN B 89 ? VAL B 86 ASN B 89 BA 2 SER B 92 ? GLN B 96 ? SER B 92 GLN B 96 BA 3 GLU B 383 ? GLY B 392 ? GLU B 383 GLY B 392 BA 4 GLN B 12 ? THR B 19 ? GLN B 12 THR B 19 BA 5 GLY B 23 ? LEU B 33 ? GLY B 23 LEU B 33 BA 6 ARG B 108 ? LEU B 112 ? ARG B 108 LEU B 112 BA 7 VAL B 341 ? TRP B 347 ? VAL B 341 TRP B 347 BA 8 ASN B 143 ? SER B 149 ? ASN B 143 SER B 149 BA 9 SER B 197 ? ALA B 203 ? SER B 197 ALA B 203 BA 10 SER B 208 ? HIS B 213 ? SER B 208 HIS B 213 BB 1 VAL B 86 ? ASN B 89 ? VAL B 86 ASN B 89 BB 2 SER B 92 ? GLN B 96 ? SER B 92 GLN B 96 BB 3 GLU B 383 ? GLY B 392 ? GLU B 383 GLY B 392 BB 4 GLU B 128 ? ASP B 134 ? GLU B 128 ASP B 134 BB 5 PHE B 266 ? ALA B 274 ? PHE B 266 ALA B 274 BB 6 LEU B 280 ? GLN B 289 ? LEU B 280 GLN B 289 BB 7 LYS B 292 ? ILE B 294 ? LYS B 292 ILE B 294 BC 1 ILE B 40 ? ARG B 42 ? ILE B 40 ARG B 42 BC 2 CYS B 73 ? MET B 75 ? CYS B 73 MET B 75 BD 1 PHE B 177 ? VAL B 178 ? PHE B 177 VAL B 178 BD 2 GLY B 192 ? CYS B 194 ? GLY B 192 CYS B 194 BD 3 TYR B 221 ? CYS B 223 ? TYR B 221 CYS B 223 BE 1 PHE B 181 ? ILE B 182 ? PHE B 181 ILE B 182 BE 2 LEU B 185 ? GLY B 186 ? LEU B 185 GLY B 186 BF 1 TYR B 252 ? GLY B 253 ? TYR B 252 GLY B 253 BF 2 VAL B 260 ? ASN B 261 ? VAL B 260 ASN B 261 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id AA 1 2 N ASN A 89 ? N ASN A 89 O SER A 92 ? O SER A 92 AA 2 3 N LEU A 95 ? N LEU A 95 O VAL A 384 ? O VAL A 384 AA 3 4 N TRP A 391 ? N TRP A 391 O PHE A 16 ? O PHE A 16 AA 4 5 N THR A 19 ? N THR A 19 O GLY A 23 ? O GLY A 23 AA 5 6 N VAL A 32 ? N VAL A 32 O TYR A 110 ? O TYR A 110 AA 6 7 N LEU A 111 ? N LEU A 111 O LEU A 342 ? O LEU A 342 AB 1 2 N ASN A 89 ? N ASN A 89 O SER A 92 ? O SER A 92 AB 2 3 N LEU A 95 ? N LEU A 95 O VAL A 384 ? O VAL A 384 AB 3 4 N GLY A 392 ? N GLY A 392 O GLU A 128 ? O GLU A 128 AB 4 5 N VAL A 133 ? N VAL A 133 O PHE A 266 ? O PHE A 266 AB 5 6 O LEU A 273 ? O LEU A 273 N GLU A 281 ? N GLU A 281 AB 6 7 N GLN A 289 ? N GLN A 289 O LYS A 292 ? O LYS A 292 AC 1 2 N HIS A 41 ? N HIS A 41 O ILE A 74 ? O ILE A 74 AD 1 2 O PHE A 177 ? O PHE A 177 N SER A 193 ? N SER A 193 AD 2 3 N CYS A 194 ? N CYS A 194 O TYR A 221 ? O TYR A 221 AE 1 2 N ILE A 182 ? N ILE A 182 O LEU A 185 ? O LEU A 185 AF 1 2 N GLY A 253 ? N GLY A 253 O VAL A 260 ? O VAL A 260 BA 1 2 N ASN B 89 ? N ASN B 89 O SER B 92 ? O SER B 92 BA 2 3 N LEU B 95 ? N LEU B 95 O VAL B 384 ? O VAL B 384 BA 3 4 N TRP B 391 ? N TRP B 391 O PHE B 16 ? O PHE B 16 BA 4 5 N THR B 19 ? N THR B 19 O GLY B 23 ? O GLY B 23 BA 5 6 N VAL B 32 ? N VAL B 32 O TYR B 110 ? O TYR B 110 BA 6 7 N LEU B 111 ? N LEU B 111 O LEU B 342 ? O LEU B 342 BA 7 8 N TRP B 347 ? N TRP B 347 O ASN B 143 ? O ASN B 143 BA 8 9 N LEU B 148 ? N LEU B 148 O MET B 198 ? O MET B 198 BA 9 10 N GLU B 202 ? N GLU B 202 O HIS B 209 ? O HIS B 209 BB 1 2 N ASN B 89 ? N ASN B 89 O SER B 92 ? O SER B 92 BB 2 3 N LEU B 95 ? N LEU B 95 O VAL B 384 ? O VAL B 384 BB 3 4 N GLY B 392 ? N GLY B 392 O GLU B 128 ? O GLU B 128 BB 4 5 N VAL B 133 ? N VAL B 133 O PHE B 266 ? O PHE B 266 BB 5 6 O LEU B 273 ? O LEU B 273 N GLU B 281 ? N GLU B 281 BB 6 7 N GLN B 289 ? N GLN B 289 O LYS B 292 ? O LYS B 292 BC 1 2 N HIS B 41 ? N HIS B 41 O ILE B 74 ? O ILE B 74 BD 1 2 O PHE B 177 ? O PHE B 177 N SER B 193 ? N SER B 193 BD 2 3 N CYS B 194 ? N CYS B 194 O TYR B 221 ? O TYR B 221 BE 1 2 N ILE B 182 ? N ILE B 182 O LEU B 185 ? O LEU B 185 BF 1 2 N GLY B 253 ? N GLY B 253 O VAL B 260 ? O VAL B 260 # 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 BGC A1400' AC2 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE GAL A1403' AC3 Software ? ? ? ? 13 'BINDING SITE FOR RESIDUE GLC A1401' AC4 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE GAL A1402' AC5 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A1404' AC6 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG B1399' AC7 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE BGC B1401' AC8 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE GAL B1404' AC9 Software ? ? ? ? 13 'BINDING SITE FOR RESIDUE GLC B1402' BC1 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE GAL B1403' # 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 HIS A 209 ? HIS A 209 . ? 1_555 ? 2 AC1 5 ASN A 237 ? ASN A 237 . ? 1_555 ? 3 AC1 5 ARG A 245 ? ARG A 245 . ? 1_555 ? 4 AC1 5 GAL D . ? GAL A 1403 . ? 1_555 ? 5 AC1 5 HOH M . ? HOH A 2219 . ? 1_555 ? 6 AC2 9 GLN A 175 ? GLN A 175 . ? 1_555 ? 7 AC2 9 HIS A 213 ? HIS A 213 . ? 1_555 ? 8 AC2 9 LYS A 236 ? LYS A 236 . ? 1_555 ? 9 AC2 9 ASN A 237 ? ASN A 237 . ? 1_555 ? 10 AC2 9 TRP A 356 ? TRP A 356 . ? 1_555 ? 11 AC2 9 BGC C . ? BGC A 1400 . ? 1_555 ? 12 AC2 9 HOH M . ? HOH A 2172 . ? 1_555 ? 13 AC2 9 HOH M . ? HOH A 2331 . ? 1_555 ? 14 AC2 9 HOH M . ? HOH A 2332 . ? 1_555 ? 15 AC3 13 ASN A 143 ? ASN A 143 . ? 1_555 ? 16 AC3 13 ALA A 145 ? ALA A 145 . ? 1_555 ? 17 AC3 13 TYR A 147 ? TYR A 147 . ? 1_555 ? 18 AC3 13 TYR A 171 ? TYR A 171 . ? 1_555 ? 19 AC3 13 ASP A 173 ? ASP A 173 . ? 1_555 ? 20 AC3 13 GLN A 175 ? GLN A 175 . ? 1_555 ? 21 AC3 13 PHE A 177 ? PHE A 177 . ? 1_555 ? 22 AC3 13 SER A 197 ? SER A 197 . ? 1_555 ? 23 AC3 13 ASP A 199 ? ASP A 199 . ? 1_555 ? 24 AC3 13 GLU A 202 ? GLU A 202 . ? 1_555 ? 25 AC3 13 TRP A 347 ? TRP A 347 . ? 1_555 ? 26 AC3 13 GAL F . ? GAL A 1402 . ? 1_555 ? 27 AC3 13 HOH M . ? HOH A 2330 . ? 1_555 ? 28 AC4 9 ARG A 108 ? ARG A 108 . ? 1_555 ? 29 AC4 9 TYR A 147 ? TYR A 147 . ? 1_555 ? 30 AC4 9 SER A 345 ? SER A 345 . ? 1_555 ? 31 AC4 9 TRP A 347 ? TRP A 347 . ? 1_555 ? 32 AC4 9 GLC E . ? GLC A 1401 . ? 1_555 ? 33 AC4 9 HOH M . ? HOH A 2118 . ? 1_555 ? 34 AC4 9 HOH M . ? HOH A 2328 . ? 1_555 ? 35 AC4 9 HOH M . ? HOH A 2329 . ? 1_555 ? 36 AC4 9 HOH M . ? HOH A 2330 . ? 1_555 ? 37 AC5 5 ASN A 247 ? ASN A 247 . ? 1_555 ? 38 AC5 5 ASN A 300 ? ASN A 300 . ? 1_555 ? 39 AC5 5 LYS A 301 ? LYS A 301 . ? 1_555 ? 40 AC5 5 GLU A 302 ? GLU A 302 . ? 1_555 ? 41 AC5 5 HOH M . ? HOH A 2333 . ? 1_555 ? 42 AC6 5 ASN B 247 ? ASN B 247 . ? 1_555 ? 43 AC6 5 ASN B 300 ? ASN B 300 . ? 1_555 ? 44 AC6 5 LYS B 301 ? LYS B 301 . ? 1_555 ? 45 AC6 5 GLU B 302 ? GLU B 302 . ? 1_555 ? 46 AC6 5 HOH N . ? HOH B 2199 . ? 1_555 ? 47 AC7 4 HIS B 209 ? HIS B 209 . ? 1_555 ? 48 AC7 4 ASN B 237 ? ASN B 237 . ? 1_555 ? 49 AC7 4 ARG B 245 ? ARG B 245 . ? 1_555 ? 50 AC7 4 GAL J . ? GAL B 1404 . ? 1_555 ? 51 AC8 8 GLN B 175 ? GLN B 175 . ? 1_555 ? 52 AC8 8 HIS B 213 ? HIS B 213 . ? 1_555 ? 53 AC8 8 LYS B 236 ? LYS B 236 . ? 1_555 ? 54 AC8 8 ASN B 237 ? ASN B 237 . ? 1_555 ? 55 AC8 8 TRP B 356 ? TRP B 356 . ? 1_555 ? 56 AC8 8 BGC I . ? BGC B 1401 . ? 1_555 ? 57 AC8 8 HOH N . ? HOH B 2161 . ? 1_555 ? 58 AC8 8 HOH N . ? HOH B 2309 . ? 1_555 ? 59 AC9 13 ASN B 143 ? ASN B 143 . ? 1_555 ? 60 AC9 13 ALA B 145 ? ALA B 145 . ? 1_555 ? 61 AC9 13 TYR B 147 ? TYR B 147 . ? 1_555 ? 62 AC9 13 TYR B 171 ? TYR B 171 . ? 1_555 ? 63 AC9 13 ASP B 173 ? ASP B 173 . ? 1_555 ? 64 AC9 13 GLN B 175 ? GLN B 175 . ? 1_555 ? 65 AC9 13 PHE B 177 ? PHE B 177 . ? 1_555 ? 66 AC9 13 SER B 197 ? SER B 197 . ? 1_555 ? 67 AC9 13 ASP B 199 ? ASP B 199 . ? 1_555 ? 68 AC9 13 GLU B 202 ? GLU B 202 . ? 1_555 ? 69 AC9 13 TRP B 347 ? TRP B 347 . ? 1_555 ? 70 AC9 13 GAL L . ? GAL B 1403 . ? 1_555 ? 71 AC9 13 HOH N . ? HOH B 2305 . ? 1_555 ? 72 BC1 9 ARG B 108 ? ARG B 108 . ? 1_555 ? 73 BC1 9 TYR B 147 ? TYR B 147 . ? 1_555 ? 74 BC1 9 SER B 345 ? SER B 345 . ? 1_555 ? 75 BC1 9 TRP B 347 ? TRP B 347 . ? 1_555 ? 76 BC1 9 GLC K . ? GLC B 1402 . ? 1_555 ? 77 BC1 9 HOH N . ? HOH B 2305 . ? 1_555 ? 78 BC1 9 HOH N . ? HOH B 2306 . ? 1_555 ? 79 BC1 9 HOH N . ? HOH B 2307 . ? 1_555 ? 80 BC1 9 HOH N . ? HOH B 2308 . ? 1_555 ? # _database_PDB_matrix.entry_id 1OJJ _database_PDB_matrix.origx[1][1] 1.000000 _database_PDB_matrix.origx[1][2] 0.000000 _database_PDB_matrix.origx[1][3] 0.000000 _database_PDB_matrix.origx[2][1] 0.000000 _database_PDB_matrix.origx[2][2] 1.000000 _database_PDB_matrix.origx[2][3] 0.000000 _database_PDB_matrix.origx[3][1] 0.000000 _database_PDB_matrix.origx[3][2] 0.000000 _database_PDB_matrix.origx[3][3] 1.000000 _database_PDB_matrix.origx_vector[1] 0.00000 _database_PDB_matrix.origx_vector[2] 0.00000 _database_PDB_matrix.origx_vector[3] 0.00000 # _atom_sites.entry_id 1OJJ _atom_sites.fract_transf_matrix[1][1] 0.015068 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.003343 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.013379 _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] 0.011936 _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 HETATM 1 N N . PCA A 1 1 ? -2.324 11.816 6.041 1.00 11.43 ? 1 PCA A N 1 HETATM 2 C CA . PCA A 1 1 ? -2.698 13.081 6.617 1.00 10.35 ? 1 PCA A CA 1 HETATM 3 C CB . PCA A 1 1 ? -1.937 13.209 7.924 1.00 10.47 ? 1 PCA A CB 1 HETATM 4 C CG . PCA A 1 1 ? -0.812 12.190 7.897 1.00 10.31 ? 1 PCA A CG 1 HETATM 5 C CD . PCA A 1 1 ? -1.178 11.333 6.718 1.00 11.01 ? 1 PCA A CD 1 HETATM 6 O OE . PCA A 1 1 ? -0.605 10.318 6.318 1.00 12.53 ? 1 PCA A OE 1 HETATM 7 C C . PCA A 1 1 ? -2.485 14.226 5.641 1.00 10.43 ? 1 PCA A C 1 HETATM 8 O O . PCA A 1 1 ? -1.660 14.155 4.749 1.00 11.92 ? 1 PCA A O 1 ATOM 9 N N . LYS A 1 2 ? -3.251 15.297 5.795 1.00 10.01 ? 2 LYS A N 1 ATOM 10 C CA . LYS A 1 2 ? -3.200 16.448 4.875 1.00 10.55 ? 2 LYS A CA 1 ATOM 11 C C . LYS A 1 2 ? -1.970 17.306 5.110 1.00 9.59 ? 2 LYS A C 1 ATOM 12 O O . LYS A 1 2 ? -1.740 17.740 6.235 1.00 9.78 ? 2 LYS A O 1 ATOM 13 C CB . LYS A 1 2 ? -4.446 17.300 5.109 1.00 11.83 ? 2 LYS A CB 1 ATOM 14 C CG . LYS A 1 2 ? -4.563 18.494 4.186 1.00 13.70 ? 2 LYS A CG 1 ATOM 15 C CD . LYS A 1 2 ? -5.887 19.217 4.441 1.00 16.00 ? 2 LYS A CD 1 ATOM 16 C CE . LYS A 1 2 ? -6.159 20.249 3.376 1.00 20.73 ? 2 LYS A CE 1 ATOM 17 N NZ . LYS A 1 2 ? -7.381 21.017 3.749 1.00 22.88 ? 2 LYS A NZ 1 ATOM 18 N N . PRO A 1 3 ? -1.156 17.564 4.082 1.00 9.54 ? 3 PRO A N 1 ATOM 19 C CA . PRO A 1 3 ? -0.034 18.473 4.271 1.00 9.84 ? 3 PRO A CA 1 ATOM 20 C C . PRO A 1 3 ? -0.401 19.845 4.797 1.00 10.69 ? 3 PRO A C 1 ATOM 21 O O . PRO A 1 3 ? -1.399 20.447 4.354 1.00 11.38 ? 3 PRO A O 1 ATOM 22 C CB . PRO A 1 3 ? 0.552 18.579 2.876 1.00 9.78 ? 3 PRO A CB 1 ATOM 23 C CG . PRO A 1 3 ? 0.254 17.197 2.300 1.00 10.14 ? 3 PRO A CG 1 ATOM 24 C CD . PRO A 1 3 ? -1.158 16.977 2.717 1.00 9.61 ? 3 PRO A CD 1 ATOM 25 N N . GLY A 1 4 ? 0.400 20.333 5.745 1.00 10.02 ? 4 GLY A N 1 ATOM 26 C CA . GLY A 1 4 ? 0.188 21.654 6.342 1.00 10.28 ? 4 GLY A CA 1 ATOM 27 C C . GLY A 1 4 ? 0.852 22.771 5.556 1.00 10.62 ? 4 GLY A C 1 ATOM 28 O O . GLY A 1 4 ? 1.327 22.566 4.444 1.00 11.14 ? 4 GLY A O 1 ATOM 29 N N . GLU A 1 5 ? 0.828 23.973 6.131 1.00 10.50 ? 5 GLU A N 1 ATOM 30 C CA . GLU A 1 5 ? 1.460 25.144 5.517 1.00 11.24 ? 5 GLU A CA 1 ATOM 31 C C . GLU A 1 5 ? 2.964 25.226 5.635 1.00 11.90 ? 5 GLU A C 1 ATOM 32 O O . GLU A 1 5 ? 3.596 26.000 4.923 1.00 14.38 ? 5 GLU A O 1 ATOM 33 C CB . GLU A 1 5 ? 0.860 26.410 6.122 1.00 11.23 ? 5 GLU A CB 1 ATOM 34 C CG . GLU A 1 5 ? -0.564 26.693 5.658 1.00 11.56 ? 5 GLU A CG 1 ATOM 35 C CD . GLU A 1 5 ? -0.594 27.260 4.255 1.00 12.00 ? 5 GLU A CD 1 ATOM 36 O OE1 . GLU A 1 5 ? 0.245 28.114 3.888 1.00 15.10 ? 5 GLU A OE1 1 ATOM 37 O OE2 . GLU A 1 5 ? -1.436 26.814 3.469 1.00 12.81 ? 5 GLU A OE2 1 ATOM 38 N N . THR A 1 6 ? 3.558 24.524 6.587 1.00 11.35 ? 6 THR A N 1 ATOM 39 C CA . THR A 1 6 ? 4.995 24.658 6.799 1.00 11.96 ? 6 THR A CA 1 ATOM 40 C C . THR A 1 6 ? 5.767 23.950 5.690 1.00 12.35 ? 6 THR A C 1 ATOM 41 O O . THR A 1 6 ? 5.429 22.835 5.286 1.00 12.28 ? 6 THR A O 1 ATOM 42 C CB . THR A 1 6 ? 5.386 24.076 8.137 1.00 12.34 ? 6 THR A CB 1 ATOM 43 O OG1 . THR A 1 6 ? 4.550 24.599 9.173 1.00 14.15 ? 6 THR A OG1 1 ATOM 44 C CG2 . THR A 1 6 ? 6.831 24.451 8.538 1.00 11.84 ? 6 THR A CG2 1 ATOM 45 N N . LYS A 1 7 ? 6.814 24.597 5.200 1.00 11.95 ? 7 LYS A N 1 ATOM 46 C CA . LYS A 1 7 ? 7.607 24.053 4.102 1.00 12.47 ? 7 LYS A CA 1 ATOM 47 C C . LYS A 1 7 ? 8.411 22.862 4.553 1.00 11.82 ? 7 LYS A C 1 ATOM 48 O O . LYS A 1 7 ? 8.943 22.815 5.658 1.00 12.30 ? 7 LYS A O 1 ATOM 49 C CB . LYS A 1 7 ? 8.578 25.094 3.527 1.00 13.41 ? 7 LYS A CB 1 ATOM 50 C CG . LYS A 1 7 ? 7.913 26.274 2.848 1.00 14.98 ? 7 LYS A CG 1 ATOM 51 C CD . LYS A 1 7 ? 7.101 25.842 1.613 1.00 16.36 ? 7 LYS A CD 1 ATOM 52 C CE . LYS A 1 7 ? 6.693 27.011 0.726 1.00 16.00 ? 7 LYS A CE 1 ATOM 53 N NZ . LYS A 1 7 ? 5.781 26.532 -0.394 1.00 17.28 ? 7 LYS A NZ 1 ATOM 54 N N . GLU A 1 8 ? 8.515 21.910 3.643 1.00 10.98 ? 8 GLU A N 1 ATOM 55 C CA . GLU A 1 8 ? 9.422 20.764 3.748 1.00 10.73 ? 8 GLU A CA 1 ATOM 56 C C . GLU A 1 8 ? 10.737 21.084 3.054 1.00 10.85 ? 8 GLU A C 1 ATOM 57 O O . GLU A 1 8 ? 10.750 21.333 1.837 1.00 12.35 ? 8 GLU A O 1 ATOM 58 C CB . GLU A 1 8 ? 8.761 19.540 3.103 1.00 10.84 ? 8 GLU A CB 1 ATOM 59 C CG . GLU A 1 8 ? 9.547 18.232 3.250 1.00 9.79 ? 8 GLU A CG 1 ATOM 60 C CD . GLU A 1 8 ? 9.345 17.517 4.557 1.00 9.30 ? 8 GLU A CD 1 ATOM 61 O OE1 . GLU A 1 8 ? 8.642 18.031 5.437 1.00 10.20 ? 8 GLU A OE1 1 ATOM 62 O OE2 . GLU A 1 8 ? 9.886 16.388 4.724 1.00 10.17 ? 8 GLU A OE2 1 ATOM 63 N N . VAL A 1 9 ? 11.833 21.107 3.810 1.00 10.72 ? 9 VAL A N 1 ATOM 64 C CA . VAL A 1 9 ? 13.163 21.420 3.223 1.00 11.02 ? 9 VAL A CA 1 ATOM 65 C C . VAL A 1 9 ? 14.046 20.178 3.347 1.00 10.26 ? 9 VAL A C 1 ATOM 66 O O . VAL A 1 9 ? 14.649 19.944 4.381 1.00 10.05 ? 9 VAL A O 1 ATOM 67 C CB . VAL A 1 9 ? 13.802 22.649 3.902 1.00 11.68 ? 9 VAL A CB 1 ATOM 68 C CG1 . VAL A 1 9 ? 15.179 22.943 3.351 1.00 14.20 ? 9 VAL A CG1 1 ATOM 69 C CG2 . VAL A 1 9 ? 12.858 23.851 3.723 1.00 12.42 ? 9 VAL A CG2 1 ATOM 70 N N . HIS A 1 10 ? 14.068 19.381 2.292 1.00 9.41 ? 10 HIS A N 1 ATOM 71 C CA . HIS A 1 10 ? 14.768 18.109 2.339 1.00 9.76 ? 10 HIS A CA 1 ATOM 72 C C . HIS A 1 10 ? 16.269 18.310 2.259 1.00 9.28 ? 10 HIS A C 1 ATOM 73 O O . HIS A 1 10 ? 16.752 19.050 1.380 1.00 11.14 ? 10 HIS A O 1 ATOM 74 C CB . HIS A 1 10 ? 14.396 17.242 1.141 1.00 9.37 ? 10 HIS A CB 1 ATOM 75 C CG . HIS A 1 10 ? 12.954 16.867 1.038 1.00 8.82 ? 10 HIS A CG 1 ATOM 76 N ND1 . HIS A 1 10 ? 12.094 17.447 0.133 1.00 10.63 ? 10 HIS A ND1 1 ATOM 77 C CD2 . HIS A 1 10 ? 12.239 15.909 1.677 1.00 9.26 ? 10 HIS A CD2 1 ATOM 78 C CE1 . HIS A 1 10 ? 10.902 16.883 0.249 1.00 10.82 ? 10 HIS A CE1 1 ATOM 79 N NE2 . HIS A 1 10 ? 10.965 15.937 1.169 1.00 9.80 ? 10 HIS A NE2 1 ATOM 80 N N . PRO A 1 11 ? 17.033 17.663 3.125 1.00 9.15 ? 11 PRO A N 1 ATOM 81 C CA . PRO A 1 11 ? 18.479 17.651 2.920 1.00 9.59 ? 11 PRO A CA 1 ATOM 82 C C . PRO A 1 11 ? 18.852 17.000 1.603 1.00 9.67 ? 11 PRO A C 1 ATOM 83 O O . PRO A 1 11 ? 18.294 15.971 1.229 1.00 9.89 ? 11 PRO A O 1 ATOM 84 C CB . PRO A 1 11 ? 18.999 16.839 4.111 1.00 10.47 ? 11 PRO A CB 1 ATOM 85 C CG . PRO A 1 11 ? 17.937 16.964 5.153 1.00 10.32 ? 11 PRO A CG 1 ATOM 86 C CD . PRO A 1 11 ? 16.655 16.972 4.379 1.00 9.60 ? 11 PRO A CD 1 ATOM 87 N N . GLN A 1 12 ? 19.826 17.584 0.909 1.00 10.29 ? 12 GLN A N 1 ATOM 88 C CA . GLN A 1 12 ? 20.342 17.009 -0.304 1.00 11.04 ? 12 GLN A CA 1 ATOM 89 C C . GLN A 1 12 ? 21.496 16.074 0.027 1.00 10.26 ? 12 GLN A C 1 ATOM 90 O O . GLN A 1 12 ? 22.312 16.375 0.895 1.00 11.62 ? 12 GLN A O 1 ATOM 91 C CB . GLN A 1 12 ? 20.833 18.135 -1.206 1.00 12.03 ? 12 GLN A CB 1 ATOM 92 C CG . GLN A 1 12 ? 21.133 17.750 -2.613 1.00 12.97 ? 12 GLN A CG 1 ATOM 93 C CD . GLN A 1 12 ? 21.421 18.920 -3.514 1.00 14.72 ? 12 GLN A CD 1 ATOM 94 O OE1 . GLN A 1 12 ? 20.571 19.809 -3.734 1.00 17.81 ? 12 GLN A OE1 1 ATOM 95 N NE2 . GLN A 1 12 ? 22.630 18.937 -4.038 1.00 18.31 ? 12 GLN A NE2 1 ATOM 96 N N . LEU A 1 13 ? 21.596 14.970 -0.708 1.00 9.98 ? 13 LEU A N 1 ATOM 97 C CA . LEU A 1 13 ? 22.666 14.002 -0.523 1.00 10.16 ? 13 LEU A CA 1 ATOM 98 C C . LEU A 1 13 ? 23.164 13.540 -1.878 1.00 10.38 ? 13 LEU A C 1 ATOM 99 O O . LEU A 1 13 ? 22.385 13.055 -2.691 1.00 10.52 ? 13 LEU A O 1 ATOM 100 C CB . LEU A 1 13 ? 22.190 12.795 0.297 1.00 10.47 ? 13 LEU A CB 1 ATOM 101 C CG . LEU A 1 13 ? 23.258 11.741 0.627 1.00 9.78 ? 13 LEU A CG 1 ATOM 102 C CD1 . LEU A 1 13 ? 24.269 12.272 1.619 1.00 10.45 ? 13 LEU A CD1 1 ATOM 103 C CD2 . LEU A 1 13 ? 22.659 10.423 1.126 1.00 11.09 ? 13 LEU A CD2 1 ATOM 104 N N . THR A 1 14 ? 24.467 13.681 -2.102 1.00 10.33 ? 14 THR A N 1 ATOM 105 C CA . THR A 1 14 ? 25.081 13.143 -3.320 1.00 10.03 ? 14 THR A CA 1 ATOM 106 C C . THR A 1 14 ? 25.415 11.664 -3.097 1.00 9.79 ? 14 THR A C 1 ATOM 107 O O . THR A 1 14 ? 26.055 11.310 -2.114 1.00 10.19 ? 14 THR A O 1 ATOM 108 C CB . THR A 1 14 ? 26.346 13.914 -3.683 1.00 9.91 ? 14 THR A CB 1 ATOM 109 O OG1 . THR A 1 14 ? 25.984 15.264 -3.966 1.00 12.50 ? 14 THR A OG1 1 ATOM 110 C CG2 . THR A 1 14 ? 26.995 13.355 -4.932 1.00 11.18 ? 14 THR A CG2 1 ATOM 111 N N . THR A 1 15 ? 24.987 10.820 -4.031 1.00 9.67 ? 15 THR A N 1 ATOM 112 C CA . THR A 1 15 ? 25.278 9.375 -4.039 1.00 9.65 ? 15 THR A CA 1 ATOM 113 C C . THR A 1 15 ? 25.930 9.058 -5.378 1.00 10.00 ? 15 THR A C 1 ATOM 114 O O . THR A 1 15 ? 26.173 9.974 -6.167 1.00 10.10 ? 15 THR A O 1 ATOM 115 C CB . THR A 1 15 ? 23.992 8.547 -3.832 1.00 9.51 ? 15 THR A CB 1 ATOM 116 O OG1 . THR A 1 15 ? 23.121 8.746 -4.950 1.00 11.30 ? 15 THR A OG1 1 ATOM 117 C CG2 . THR A 1 15 ? 23.221 8.984 -2.589 1.00 8.93 ? 15 THR A CG2 1 ATOM 118 N N . PHE A 1 16 ? 26.204 7.783 -5.651 1.00 9.28 ? 16 PHE A N 1 ATOM 119 C CA . PHE A 1 16 ? 26.921 7.421 -6.883 1.00 9.56 ? 16 PHE A CA 1 ATOM 120 C C . PHE A 1 16 ? 26.309 6.193 -7.546 1.00 9.91 ? 16 PHE A C 1 ATOM 121 O O . PHE A 1 16 ? 25.733 5.321 -6.884 1.00 10.51 ? 16 PHE A O 1 ATOM 122 C CB . PHE A 1 16 ? 28.420 7.154 -6.635 1.00 10.64 ? 16 PHE A CB 1 ATOM 123 C CG . PHE A 1 16 ? 29.149 8.309 -6.006 1.00 9.79 ? 16 PHE A CG 1 ATOM 124 C CD1 . PHE A 1 16 ? 29.871 9.208 -6.790 1.00 11.20 ? 16 PHE A CD1 1 ATOM 125 C CD2 . PHE A 1 16 ? 29.138 8.500 -4.626 1.00 10.21 ? 16 PHE A CD2 1 ATOM 126 C CE1 . PHE A 1 16 ? 30.512 10.290 -6.210 1.00 11.03 ? 16 PHE A CE1 1 ATOM 127 C CE2 . PHE A 1 16 ? 29.781 9.575 -4.036 1.00 10.66 ? 16 PHE A CE2 1 ATOM 128 C CZ . PHE A 1 16 ? 30.483 10.472 -4.846 1.00 11.42 ? 16 PHE A CZ 1 ATOM 129 N N . ARG A 1 17 ? 26.455 6.162 -8.861 1.00 10.40 ? 17 ARG A N 1 ATOM 130 C CA . ARG A 1 17 ? 26.106 5.009 -9.681 1.00 11.15 ? 17 ARG A CA 1 ATOM 131 C C . ARG A 1 17 ? 27.389 4.542 -10.332 1.00 11.20 ? 17 ARG A C 1 ATOM 132 O O . ARG A 1 17 ? 28.113 5.355 -10.912 1.00 11.61 ? 17 ARG A O 1 ATOM 133 C CB . ARG A 1 17 ? 25.098 5.370 -10.751 1.00 11.65 ? 17 ARG A CB 1 ATOM 134 C CG . ARG A 1 17 ? 23.837 6.064 -10.245 1.00 12.43 ? 17 ARG A CG 1 ATOM 135 C CD . ARG A 1 17 ? 22.924 5.196 -9.352 1.00 12.12 ? 17 ARG A CD 1 ATOM 136 N NE . ARG A 1 17 ? 21.876 6.059 -8.848 1.00 11.75 ? 17 ARG A NE 1 ATOM 137 C CZ . ARG A 1 17 ? 21.989 6.896 -7.815 1.00 11.73 ? 17 ARG A CZ 1 ATOM 138 N NH1 . ARG A 1 17 ? 23.057 6.891 -7.043 1.00 10.98 ? 17 ARG A NH1 1 ATOM 139 N NH2 . ARG A 1 17 ? 20.998 7.734 -7.540 1.00 11.84 ? 17 ARG A NH2 1 ATOM 140 N N . CYS A 1 18 ? 27.678 3.254 -10.234 1.00 11.16 ? 18 CYS A N 1 ATOM 141 C CA . CYS A 1 18 ? 29.001 2.751 -10.584 1.00 12.27 ? 18 CYS A CA 1 ATOM 142 C C . CYS A 1 18 ? 28.957 1.684 -11.680 1.00 12.70 ? 18 CYS A C 1 ATOM 143 O O . CYS A 1 18 ? 28.075 0.820 -11.704 1.00 12.72 ? 18 CYS A O 1 ATOM 144 C CB . CYS A 1 18 ? 29.683 2.184 -9.334 1.00 12.34 ? 18 CYS A CB 1 ATOM 145 S SG . CYS A 1 18 ? 29.693 3.278 -7.887 1.00 13.41 ? 18 CYS A SG 1 ATOM 146 N N . THR A 1 19 ? 29.943 1.757 -12.585 1.00 12.94 ? 19 THR A N 1 ATOM 147 C CA . THR A 1 19 ? 30.205 0.713 -13.560 1.00 14.54 ? 19 THR A CA 1 ATOM 148 C C . THR A 1 19 ? 31.703 0.474 -13.599 1.00 15.29 ? 19 THR A C 1 ATOM 149 O O . THR A 1 19 ? 32.501 1.323 -13.181 1.00 14.43 ? 19 THR A O 1 ATOM 150 C CB . THR A 1 19 ? 29.723 1.098 -14.981 1.00 14.43 ? 19 THR A CB 1 ATOM 151 O OG1 . THR A 1 19 ? 30.418 2.267 -15.461 1.00 14.84 ? 19 THR A OG1 1 ATOM 152 C CG2 . THR A 1 19 ? 28.294 1.465 -14.998 1.00 14.63 ? 19 THR A CG2 1 ATOM 153 N N . LYS A 1 20 ? 32.082 -0.689 -14.129 1.00 17.33 ? 20 LYS A N 1 ATOM 154 C CA . LYS A 1 20 ? 33.495 -1.004 -14.314 1.00 19.57 ? 20 LYS A CA 1 ATOM 155 C C . LYS A 1 20 ? 34.172 -0.002 -15.255 1.00 19.41 ? 20 LYS A C 1 ATOM 156 O O . LYS A 1 20 ? 35.244 0.510 -14.928 1.00 19.80 ? 20 LYS A O 1 ATOM 157 C CB . LYS A 1 20 ? 33.684 -2.447 -14.811 1.00 19.89 ? 20 LYS A CB 1 ATOM 158 C CG . LYS A 1 20 ? 33.429 -3.485 -13.706 1.00 23.92 ? 20 LYS A CG 1 ATOM 159 C CD . LYS A 1 20 ? 34.430 -4.654 -13.691 1.00 25.22 ? 20 LYS A CD 1 ATOM 160 C CE . LYS A 1 20 ? 33.865 -5.901 -14.308 1.00 29.84 ? 20 LYS A CE 1 ATOM 161 N NZ . LYS A 1 20 ? 34.631 -7.081 -13.804 1.00 30.49 ? 20 LYS A NZ 1 ATOM 162 N N . ARG A 1 21 ? 33.489 0.335 -16.345 1.00 20.97 ? 21 ARG A N 1 ATOM 163 C CA . ARG A 1 21 ? 34.053 1.198 -17.416 1.00 21.45 ? 21 ARG A CA 1 ATOM 164 C C . ARG A 1 21 ? 34.161 2.655 -16.966 1.00 20.56 ? 21 ARG A C 1 ATOM 165 O O . ARG A 1 21 ? 35.157 3.323 -17.218 1.00 19.91 ? 21 ARG A O 1 ATOM 166 C CB . ARG A 1 21 ? 33.178 1.080 -18.678 1.00 22.12 ? 21 ARG A CB 1 ATOM 167 C CG . ARG A 1 21 ? 33.630 1.845 -19.942 1.00 25.51 ? 21 ARG A CG 1 ATOM 168 C CD . ARG A 1 21 ? 33.560 1.020 -21.272 1.00 29.51 ? 21 ARG A CD 1 ATOM 169 N NE . ARG A 1 21 ? 32.287 0.336 -21.518 1.00 34.66 ? 21 ARG A NE 1 ATOM 170 C CZ . ARG A 1 21 ? 32.127 -0.725 -22.326 1.00 35.50 ? 21 ARG A CZ 1 ATOM 171 N NH1 . ARG A 1 21 ? 33.157 -1.243 -22.995 1.00 38.99 ? 21 ARG A NH1 1 ATOM 172 N NH2 . ARG A 1 21 ? 30.927 -1.280 -22.467 1.00 38.02 ? 21 ARG A NH2 1 ATOM 173 N N . GLY A 1 22 ? 33.139 3.151 -16.271 1.00 18.31 ? 22 GLY A N 1 ATOM 174 C CA . GLY A 1 22 ? 33.062 4.577 -15.936 1.00 17.96 ? 22 GLY A CA 1 ATOM 175 C C . GLY A 1 22 ? 33.358 4.958 -14.500 1.00 16.35 ? 22 GLY A C 1 ATOM 176 O O . GLY A 1 22 ? 33.374 6.152 -14.158 1.00 16.09 ? 22 GLY A O 1 ATOM 177 N N . GLY A 1 23 ? 33.587 3.965 -13.649 1.00 15.13 ? 23 GLY A N 1 ATOM 178 C CA . GLY A 1 23 ? 33.775 4.203 -12.217 1.00 14.72 ? 23 GLY A CA 1 ATOM 179 C C . GLY A 1 23 ? 32.460 4.628 -11.570 1.00 13.88 ? 23 GLY A C 1 ATOM 180 O O . GLY A 1 23 ? 31.381 4.366 -12.102 1.00 13.84 ? 23 GLY A O 1 ATOM 181 N N . CYS A 1 24 ? 32.579 5.271 -10.422 1.00 12.84 ? 24 CYS A N 1 ATOM 182 C CA . CYS A 1 24 ? 31.422 5.791 -9.710 1.00 13.34 ? 24 CYS A CA 1 ATOM 183 C C . CYS A 1 24 ? 31.186 7.240 -10.106 1.00 13.70 ? 24 CYS A C 1 ATOM 184 O O . CYS A 1 24 ? 32.109 8.061 -10.042 1.00 15.60 ? 24 CYS A O 1 ATOM 185 C CB . CYS A 1 24 ? 31.679 5.698 -8.224 1.00 13.07 ? 24 CYS A CB 1 ATOM 186 S SG . CYS A 1 24 ? 31.668 3.984 -7.638 1.00 15.31 ? 24 CYS A SG 1 ATOM 187 N N . LYS A 1 25 ? 29.974 7.537 -10.529 1.00 12.54 ? 25 LYS A N 1 ATOM 188 C CA . LYS A 1 25 ? 29.584 8.863 -11.019 1.00 13.36 ? 25 LYS A CA 1 ATOM 189 C C . LYS A 1 25 ? 28.502 9.465 -10.129 1.00 11.73 ? 25 LYS A C 1 ATOM 190 O O . LYS A 1 25 ? 27.561 8.760 -9.735 1.00 12.15 ? 25 LYS A O 1 ATOM 191 C CB . LYS A 1 25 ? 29.091 8.745 -12.440 1.00 14.33 ? 25 LYS A CB 1 ATOM 192 C CG . LYS A 1 25 ? 30.219 8.381 -13.423 1.00 15.78 ? 25 LYS A CG 1 ATOM 193 C CD . LYS A 1 25 ? 29.697 8.242 -14.852 1.00 17.11 ? 25 LYS A CD 1 ATOM 194 C CE . LYS A 1 25 ? 30.820 8.199 -15.873 1.00 20.77 ? 25 LYS A CE 1 ATOM 195 N NZ . LYS A 1 25 ? 31.273 9.584 -16.272 1.00 24.80 ? 25 LYS A NZ 1 ATOM 196 N N . PRO A 1 26 ? 28.639 10.731 -9.765 1.00 11.66 ? 26 PRO A N 1 ATOM 197 C CA . PRO A 1 26 ? 27.752 11.334 -8.768 1.00 11.79 ? 26 PRO A CA 1 ATOM 198 C C . PRO A 1 26 ? 26.329 11.540 -9.272 1.00 11.96 ? 26 PRO A C 1 ATOM 199 O O . PRO A 1 26 ? 26.090 11.735 -10.473 1.00 13.46 ? 26 PRO A O 1 ATOM 200 C CB . PRO A 1 26 ? 28.422 12.664 -8.469 1.00 11.73 ? 26 PRO A CB 1 ATOM 201 C CG . PRO A 1 26 ? 29.132 12.973 -9.754 1.00 12.17 ? 26 PRO A CG 1 ATOM 202 C CD . PRO A 1 26 ? 29.676 11.679 -10.236 1.00 12.36 ? 26 PRO A CD 1 ATOM 203 N N . ALA A 1 27 ? 25.389 11.506 -8.329 1.00 11.71 ? 27 ALA A N 1 ATOM 204 C CA . ALA A 1 27 ? 23.971 11.700 -8.616 1.00 11.91 ? 27 ALA A CA 1 ATOM 205 C C . ALA A 1 27 ? 23.369 12.453 -7.447 1.00 11.31 ? 27 ALA A C 1 ATOM 206 O O . ALA A 1 27 ? 23.800 12.295 -6.300 1.00 12.05 ? 27 ALA A O 1 ATOM 207 C CB . ALA A 1 27 ? 23.280 10.345 -8.809 1.00 12.65 ? 27 ALA A CB 1 ATOM 208 N N . THR A 1 28 ? 22.388 13.303 -7.738 1.00 11.77 ? 28 THR A N 1 ATOM 209 C CA . THR A 1 28 ? 21.718 14.067 -6.717 1.00 11.28 ? 28 THR A CA 1 ATOM 210 C C . THR A 1 28 ? 20.512 13.321 -6.190 1.00 10.71 ? 28 THR A C 1 ATOM 211 O O . THR A 1 28 ? 19.623 12.927 -6.962 1.00 11.47 ? 28 THR A O 1 ATOM 212 C CB . THR A 1 28 ? 21.273 15.415 -7.281 1.00 12.41 ? 28 THR A CB 1 ATOM 213 O OG1 . THR A 1 28 ? 22.434 16.171 -7.645 1.00 14.89 ? 28 THR A OG1 1 ATOM 214 C CG2 . THR A 1 28 ? 20.581 16.237 -6.223 1.00 13.47 ? 28 THR A CG2 1 ATOM 215 N N . ASN A 1 29 ? 20.472 13.167 -4.867 1.00 9.76 ? 29 ASN A N 1 ATOM 216 C CA . ASN A 1 29 ? 19.317 12.608 -4.183 1.00 9.71 ? 29 ASN A CA 1 ATOM 217 C C . ASN A 1 29 ? 18.895 13.534 -3.035 1.00 9.26 ? 29 ASN A C 1 ATOM 218 O O . ASN A 1 29 ? 19.600 14.491 -2.705 1.00 9.78 ? 29 ASN A O 1 ATOM 219 C CB . ASN A 1 29 ? 19.639 11.208 -3.682 1.00 9.65 ? 29 ASN A CB 1 ATOM 220 C CG . ASN A 1 29 ? 19.683 10.189 -4.812 1.00 10.16 ? 29 ASN A CG 1 ATOM 221 O OD1 . ASN A 1 29 ? 20.746 9.779 -5.283 1.00 10.64 ? 29 ASN A OD1 1 ATOM 222 N ND2 . ASN A 1 29 ? 18.497 9.807 -5.288 1.00 10.09 ? 29 ASN A ND2 1 ATOM 223 N N . PHE A 1 30 ? 17.746 13.231 -2.433 1.00 8.72 ? 30 PHE A N 1 ATOM 224 C CA . PHE A 1 30 ? 17.239 13.960 -1.256 1.00 8.76 ? 30 PHE A CA 1 ATOM 225 C C . PHE A 1 30 ? 16.854 12.986 -0.159 1.00 8.59 ? 30 PHE A C 1 ATOM 226 O O . PHE A 1 30 ? 16.724 11.801 -0.414 1.00 9.19 ? 30 PHE A O 1 ATOM 227 C CB . PHE A 1 30 ? 16.088 14.895 -1.645 1.00 9.70 ? 30 PHE A CB 1 ATOM 228 C CG . PHE A 1 30 ? 16.533 15.987 -2.567 1.00 9.64 ? 30 PHE A CG 1 ATOM 229 C CD1 . PHE A 1 30 ? 17.108 17.135 -2.065 1.00 9.47 ? 30 PHE A CD1 1 ATOM 230 C CD2 . PHE A 1 30 ? 16.433 15.827 -3.936 1.00 10.90 ? 30 PHE A CD2 1 ATOM 231 C CE1 . PHE A 1 30 ? 17.584 18.111 -2.938 1.00 11.14 ? 30 PHE A CE1 1 ATOM 232 C CE2 . PHE A 1 30 ? 16.880 16.813 -4.806 1.00 11.91 ? 30 PHE A CE2 1 ATOM 233 C CZ . PHE A 1 30 ? 17.452 17.947 -4.304 1.00 11.69 ? 30 PHE A CZ 1 ATOM 234 N N . ILE A 1 31 ? 16.765 13.503 1.058 1.00 8.81 ? 31 ILE A N 1 ATOM 235 C CA . ILE A 1 31 ? 16.454 12.740 2.265 1.00 8.30 ? 31 ILE A CA 1 ATOM 236 C C . ILE A 1 31 ? 15.121 13.197 2.833 1.00 8.58 ? 31 ILE A C 1 ATOM 237 O O . ILE A 1 31 ? 14.894 14.403 2.960 1.00 9.73 ? 31 ILE A O 1 ATOM 238 C CB . ILE A 1 31 ? 17.585 12.974 3.297 1.00 8.64 ? 31 ILE A CB 1 ATOM 239 C CG1 . ILE A 1 31 ? 18.875 12.299 2.814 1.00 9.96 ? 31 ILE A CG1 1 ATOM 240 C CG2 . ILE A 1 31 ? 17.213 12.492 4.672 1.00 9.24 ? 31 ILE A CG2 1 ATOM 241 C CD1 . ILE A 1 31 ? 18.835 10.751 2.772 1.00 10.98 ? 31 ILE A CD1 1 ATOM 242 N N . VAL A 1 32 ? 14.233 12.244 3.188 1.00 8.12 ? 32 VAL A N 1 ATOM 243 C CA . VAL A 1 32 ? 12.929 12.558 3.781 1.00 7.87 ? 32 VAL A CA 1 ATOM 244 C C . VAL A 1 32 ? 12.718 11.733 5.044 1.00 7.56 ? 32 VAL A C 1 ATOM 245 O O . VAL A 1 32 ? 12.949 10.526 5.062 1.00 8.45 ? 32 VAL A O 1 ATOM 246 C CB . VAL A 1 32 ? 11.759 12.391 2.760 1.00 8.06 ? 32 VAL A CB 1 ATOM 247 C CG1 . VAL A 1 32 ? 11.559 10.944 2.291 1.00 8.27 ? 32 VAL A CG1 1 ATOM 248 C CG2 . VAL A 1 32 ? 10.473 12.966 3.331 1.00 8.75 ? 32 VAL A CG2 1 ATOM 249 N N . LEU A 1 33 ? 12.274 12.407 6.111 1.00 7.44 ? 33 LEU A N 1 ATOM 250 C CA . LEU A 1 33 ? 11.924 11.752 7.345 1.00 8.15 ? 33 LEU A CA 1 ATOM 251 C C . LEU A 1 33 ? 10.614 10.984 7.179 1.00 7.77 ? 33 LEU A C 1 ATOM 252 O O . LEU A 1 33 ? 9.740 11.353 6.390 1.00 7.83 ? 33 LEU A O 1 ATOM 253 C CB . LEU A 1 33 ? 11.792 12.792 8.459 1.00 9.28 ? 33 LEU A CB 1 ATOM 254 C CG . LEU A 1 33 ? 13.088 13.105 9.190 1.00 13.85 ? 33 LEU A CG 1 ATOM 255 C CD1 . LEU A 1 33 ? 13.041 14.447 9.829 1.00 15.94 ? 33 LEU A CD1 1 ATOM 256 C CD2 . LEU A 1 33 ? 13.386 12.009 10.258 1.00 11.46 ? 33 LEU A CD2 1 ATOM 257 N N . ASP A 1 34 ? 10.446 9.927 7.972 1.00 8.01 ? 34 ASP A N 1 ATOM 258 C CA . ASP A 1 34 ? 9.166 9.206 7.928 1.00 8.00 ? 34 ASP A CA 1 ATOM 259 C C . ASP A 1 34 ? 8.020 10.186 8.099 1.00 7.90 ? 34 ASP A C 1 ATOM 260 O O . ASP A 1 34 ? 8.081 11.110 8.900 1.00 8.76 ? 34 ASP A O 1 ATOM 261 C CB . ASP A 1 34 ? 9.065 8.133 8.995 1.00 7.06 ? 34 ASP A CB 1 ATOM 262 C CG . ASP A 1 34 ? 7.793 7.353 8.873 1.00 7.95 ? 34 ASP A CG 1 ATOM 263 O OD1 . ASP A 1 34 ? 7.689 6.623 7.875 1.00 8.57 ? 34 ASP A OD1 1 ATOM 264 O OD2 . ASP A 1 34 ? 6.862 7.441 9.694 1.00 7.99 ? 34 ASP A OD2 1 ATOM 265 N N . SER A 1 35 ? 6.927 9.931 7.387 1.00 7.66 ? 35 SER A N 1 ATOM 266 C CA . SER A 1 35 ? 5.738 10.776 7.466 1.00 8.12 ? 35 SER A CA 1 ATOM 267 C C . SER A 1 35 ? 5.267 11.007 8.903 1.00 7.89 ? 35 SER A C 1 ATOM 268 O O . SER A 1 35 ? 4.970 12.136 9.292 1.00 8.32 ? 35 SER A O 1 ATOM 269 C CB . SER A 1 35 ? 4.585 10.192 6.630 1.00 8.43 ? 35 SER A CB 1 ATOM 270 O OG . SER A 1 35 ? 4.168 8.911 7.128 1.00 8.75 ? 35 SER A OG 1 ATOM 271 N N . LEU A 1 36 ? 5.199 9.943 9.688 1.00 7.79 ? 36 LEU A N 1 ATOM 272 C CA . LEU A 1 36 ? 4.651 10.029 11.034 1.00 9.17 ? 36 LEU A CA 1 ATOM 273 C C . LEU A 1 36 ? 5.619 10.554 12.071 1.00 9.33 ? 36 LEU A C 1 ATOM 274 O O . LEU A 1 36 ? 5.267 10.714 13.240 1.00 11.81 ? 36 LEU A O 1 ATOM 275 C CB . LEU A 1 36 ? 4.027 8.713 11.453 1.00 8.81 ? 36 LEU A CB 1 ATOM 276 C CG . LEU A 1 36 ? 2.899 8.229 10.525 1.00 10.27 ? 36 LEU A CG 1 ATOM 277 C CD1 . LEU A 1 36 ? 2.333 6.919 11.046 1.00 11.30 ? 36 LEU A CD1 1 ATOM 278 C CD2 . LEU A 1 36 ? 1.803 9.280 10.375 1.00 11.99 ? 36 LEU A CD2 1 ATOM 279 N N . SER A 1 37 ? 6.831 10.869 11.633 1.00 8.29 ? 37 SER A N 1 ATOM 280 C CA . SER A 1 37 ? 7.821 11.613 12.407 1.00 8.54 ? 37 SER A CA 1 ATOM 281 C C . SER A 1 37 ? 7.743 13.122 12.166 1.00 8.94 ? 37 SER A C 1 ATOM 282 O O . SER A 1 37 ? 8.353 13.919 12.896 1.00 10.13 ? 37 SER A O 1 ATOM 283 C CB . SER A 1 37 ? 9.224 11.091 12.112 1.00 9.66 ? 37 SER A CB 1 ATOM 284 O OG . SER A 1 37 ? 9.274 9.719 12.468 1.00 11.74 ? 37 SER A OG 1 ATOM 285 N N . HIS A 1 38 ? 6.993 13.526 11.144 1.00 8.57 ? 38 HIS A N 1 ATOM 286 C CA . HIS A 1 38 ? 6.645 14.938 10.943 1.00 9.12 ? 38 HIS A CA 1 ATOM 287 C C . HIS A 1 38 ? 5.645 15.355 12.011 1.00 9.82 ? 38 HIS A C 1 ATOM 288 O O . HIS A 1 38 ? 4.955 14.496 12.552 1.00 10.17 ? 38 HIS A O 1 ATOM 289 C CB . HIS A 1 38 ? 6.032 15.153 9.561 1.00 8.98 ? 38 HIS A CB 1 ATOM 290 C CG . HIS A 1 38 ? 6.994 15.011 8.420 1.00 8.16 ? 38 HIS A CG 1 ATOM 291 N ND1 . HIS A 1 38 ? 7.613 13.820 8.085 1.00 8.01 ? 38 HIS A ND1 1 ATOM 292 C CD2 . HIS A 1 38 ? 7.461 15.937 7.557 1.00 9.31 ? 38 HIS A CD2 1 ATOM 293 C CE1 . HIS A 1 38 ? 8.400 14.031 7.042 1.00 8.62 ? 38 HIS A CE1 1 ATOM 294 N NE2 . HIS A 1 38 ? 8.311 15.301 6.687 1.00 9.74 ? 38 HIS A NE2 1 ATOM 295 N N . PRO A 1 39 ? 5.544 16.650 12.341 1.00 9.13 ? 39 PRO A N 1 ATOM 296 C CA . PRO A 1 39 ? 4.495 17.047 13.288 1.00 10.02 ? 39 PRO A CA 1 ATOM 297 C C . PRO A 1 39 ? 3.114 16.725 12.724 1.00 10.23 ? 39 PRO A C 1 ATOM 298 O O . PRO A 1 39 ? 2.800 17.092 11.604 1.00 11.33 ? 39 PRO A O 1 ATOM 299 C CB . PRO A 1 39 ? 4.701 18.570 13.443 1.00 10.69 ? 39 PRO A CB 1 ATOM 300 C CG . PRO A 1 39 ? 6.106 18.786 13.044 1.00 9.81 ? 39 PRO A CG 1 ATOM 301 C CD . PRO A 1 39 ? 6.387 17.795 11.934 1.00 10.49 ? 39 PRO A CD 1 ATOM 302 N N . ILE A 1 40 ? 2.291 16.060 13.528 1.00 10.81 ? 40 ILE A N 1 ATOM 303 C CA . ILE A 1 40 ? 0.923 15.702 13.153 1.00 11.36 ? 40 ILE A CA 1 ATOM 304 C C . ILE A 1 40 ? -0.003 16.336 14.172 1.00 11.30 ? 40 ILE A C 1 ATOM 305 O O . ILE A 1 40 ? 0.136 16.126 15.379 1.00 12.08 ? 40 ILE A O 1 ATOM 306 C CB . ILE A 1 40 ? 0.697 14.161 13.180 1.00 12.16 ? 40 ILE A CB 1 ATOM 307 C CG1 . ILE A 1 40 ? 1.707 13.364 12.346 1.00 14.88 ? 40 ILE A CG1 1 ATOM 308 C CG2 . ILE A 1 40 ? -0.763 13.828 12.769 1.00 13.52 ? 40 ILE A CG2 1 ATOM 309 C CD1 . ILE A 1 40 ? 1.716 13.697 10.906 1.00 15.45 ? 40 ILE A CD1 1 ATOM 310 N N . HIS A 1 41 ? -0.934 17.148 13.694 1.00 10.70 ? 41 HIS A N 1 ATOM 311 C CA . HIS A 1 41 ? -1.881 17.836 14.560 1.00 10.82 ? 41 HIS A CA 1 ATOM 312 C C . HIS A 1 41 ? -3.247 17.815 13.902 1.00 10.31 ? 41 HIS A C 1 ATOM 313 O O . HIS A 1 41 ? -3.427 17.159 12.887 1.00 11.07 ? 41 HIS A O 1 ATOM 314 C CB . HIS A 1 41 ? -1.404 19.250 14.929 1.00 10.61 ? 41 HIS A CB 1 ATOM 315 C CG . HIS A 1 41 ? -1.287 20.180 13.761 1.00 10.91 ? 41 HIS A CG 1 ATOM 316 N ND1 . HIS A 1 41 ? -2.333 20.965 13.313 1.00 12.31 ? 41 HIS A ND1 1 ATOM 317 C CD2 . HIS A 1 41 ? -0.242 20.441 12.939 1.00 12.66 ? 41 HIS A CD2 1 ATOM 318 C CE1 . HIS A 1 41 ? -1.932 21.662 12.265 1.00 12.54 ? 41 HIS A CE1 1 ATOM 319 N NE2 . HIS A 1 41 ? -0.666 21.363 12.021 1.00 12.69 ? 41 HIS A NE2 1 ATOM 320 N N . ARG A 1 42 ? -4.218 18.518 14.492 1.00 9.75 ? 42 ARG A N 1 ATOM 321 C CA . ARG A 1 42 ? -5.595 18.468 14.001 1.00 9.76 ? 42 ARG A CA 1 ATOM 322 C C . ARG A 1 42 ? -5.924 19.739 13.233 1.00 10.09 ? 42 ARG A C 1 ATOM 323 O O . ARG A 1 42 ? -5.248 20.766 13.353 1.00 10.53 ? 42 ARG A O 1 ATOM 324 C CB . ARG A 1 42 ? -6.568 18.211 15.150 1.00 9.89 ? 42 ARG A CB 1 ATOM 325 C CG . ARG A 1 42 ? -6.301 16.895 15.824 1.00 10.39 ? 42 ARG A CG 1 ATOM 326 C CD . ARG A 1 42 ? -7.047 16.702 17.120 1.00 10.98 ? 42 ARG A CD 1 ATOM 327 N NE . ARG A 1 42 ? -6.726 15.384 17.624 1.00 10.68 ? 42 ARG A NE 1 ATOM 328 C CZ . ARG A 1 42 ? -7.540 14.572 18.264 1.00 11.33 ? 42 ARG A CZ 1 ATOM 329 N NH1 . ARG A 1 42 ? -8.744 14.955 18.619 1.00 13.24 ? 42 ARG A NH1 1 ATOM 330 N NH2 . ARG A 1 42 ? -7.123 13.350 18.579 1.00 12.59 ? 42 ARG A NH2 1 ATOM 331 N N . ALA A 1 43 ? -6.989 19.655 12.444 1.00 9.79 ? 43 ALA A N 1 ATOM 332 C CA . ALA A 1 43 ? -7.464 20.789 11.651 1.00 10.41 ? 43 ALA A CA 1 ATOM 333 C C . ALA A 1 43 ? -7.930 21.930 12.543 1.00 11.03 ? 43 ALA A C 1 ATOM 334 O O . ALA A 1 43 ? -8.130 21.777 13.764 1.00 10.96 ? 43 ALA A O 1 ATOM 335 C CB . ALA A 1 43 ? -8.590 20.349 10.724 1.00 11.56 ? 43 ALA A CB 1 ATOM 336 N N . GLU A 1 44 ? -8.140 23.091 11.924 1.00 10.71 ? 44 GLU A N 1 ATOM 337 C CA . GLU A 1 44 ? -8.515 24.294 12.661 1.00 11.66 ? 44 GLU A CA 1 ATOM 338 C C . GLU A 1 44 ? -9.748 24.084 13.516 1.00 11.52 ? 44 GLU A C 1 ATOM 339 O O . GLU A 1 44 ? -10.719 23.446 13.108 1.00 11.31 ? 44 GLU A O 1 ATOM 340 C CB . GLU A 1 44 ? -8.715 25.463 11.665 1.00 12.12 ? 44 GLU A CB 1 ATOM 341 C CG . GLU A 1 44 ? -7.372 25.969 11.122 1.00 13.34 ? 44 GLU A CG 1 ATOM 342 C CD . GLU A 1 44 ? -7.420 26.824 9.859 1.00 13.70 ? 44 GLU A CD 1 ATOM 343 O OE1 . GLU A 1 44 ? -8.421 26.771 9.082 1.00 13.91 ? 44 GLU A OE1 1 ATOM 344 O OE2 . GLU A 1 44 ? -6.400 27.530 9.638 1.00 14.08 ? 44 GLU A OE2 1 ATOM 345 N N . GLY A 1 45 ? -9.683 24.616 14.731 1.00 11.57 ? 45 GLY A N 1 ATOM 346 C CA . GLY A 1 45 ? -10.782 24.557 15.659 1.00 12.87 ? 45 GLY A CA 1 ATOM 347 C C . GLY A 1 45 ? -10.976 23.264 16.418 1.00 13.39 ? 45 GLY A C 1 ATOM 348 O O . GLY A 1 45 ? -11.828 23.223 17.305 1.00 15.52 ? 45 GLY A O 1 ATOM 349 N N . LEU A 1 46 ? -10.242 22.203 16.059 1.00 12.14 ? 46 LEU A N 1 ATOM 350 C CA . LEU A 1 46 ? -10.434 20.887 16.675 1.00 11.87 ? 46 LEU A CA 1 ATOM 351 C C . LEU A 1 46 ? -9.608 20.651 17.934 1.00 12.03 ? 46 LEU A C 1 ATOM 352 O O . LEU A 1 46 ? -9.672 19.562 18.529 1.00 13.11 ? 46 LEU A O 1 ATOM 353 C CB . LEU A 1 46 ? -10.140 19.796 15.649 1.00 11.27 ? 46 LEU A CB 1 ATOM 354 C CG . LEU A 1 46 ? -11.020 19.806 14.395 1.00 12.16 ? 46 LEU A CG 1 ATOM 355 C CD1 . LEU A 1 46 ? -10.706 18.570 13.589 1.00 12.41 ? 46 LEU A CD1 1 ATOM 356 C CD2 . LEU A 1 46 ? -12.516 19.895 14.736 1.00 13.44 ? 46 LEU A CD2 1 ATOM 357 N N . GLY A 1 47 ? -8.848 21.651 18.377 1.00 12.07 ? 47 GLY A N 1 ATOM 358 C CA . GLY A 1 47 ? -8.048 21.510 19.605 1.00 12.47 ? 47 GLY A CA 1 ATOM 359 C C . GLY A 1 47 ? -6.695 20.880 19.374 1.00 12.24 ? 47 GLY A C 1 ATOM 360 O O . GLY A 1 47 ? -6.321 20.551 18.236 1.00 12.25 ? 47 GLY A O 1 ATOM 361 N N . PRO A 1 48 ? -5.953 20.689 20.452 1.00 12.36 ? 48 PRO A N 1 ATOM 362 C CA . PRO A 1 48 ? -4.588 20.206 20.396 1.00 12.67 ? 48 PRO A CA 1 ATOM 363 C C . PRO A 1 48 ? -4.533 18.692 20.303 1.00 13.34 ? 48 PRO A C 1 ATOM 364 O O . PRO A 1 48 ? -5.541 18.013 20.460 1.00 13.69 ? 48 PRO A O 1 ATOM 365 C CB . PRO A 1 48 ? -4.033 20.655 21.747 1.00 12.88 ? 48 PRO A CB 1 ATOM 366 C CG . PRO A 1 48 ? -5.209 20.536 22.645 1.00 13.23 ? 48 PRO A CG 1 ATOM 367 C CD . PRO A 1 48 ? -6.381 20.975 21.835 1.00 13.35 ? 48 PRO A CD 1 ATOM 368 N N . GLY A 1 49 ? -3.335 18.190 20.074 1.00 13.87 ? 49 GLY A N 1 ATOM 369 C CA . GLY A 1 49 ? -3.079 16.761 20.038 1.00 13.88 ? 49 GLY A CA 1 ATOM 370 C C . GLY A 1 49 ? -2.926 16.242 18.633 1.00 13.94 ? 49 GLY A C 1 ATOM 371 O O . GLY A 1 49 ? -3.159 16.940 17.654 1.00 12.58 ? 49 GLY A O 1 ATOM 372 N N . GLY A 1 50 ? -2.544 14.980 18.540 1.00 14.56 ? 50 GLY A N 1 ATOM 373 C CA . GLY A 1 50 ? -2.244 14.345 17.260 1.00 13.56 ? 50 GLY A CA 1 ATOM 374 C C . GLY A 1 50 ? -3.346 13.462 16.746 1.00 13.13 ? 50 GLY A C 1 ATOM 375 O O . GLY A 1 50 ? -4.513 13.608 17.117 1.00 12.76 ? 50 GLY A O 1 ATOM 376 N N . CYS A 1 51 ? -2.962 12.534 15.878 1.00 11.71 ? 51 CYS A N 1 ATOM 377 C CA . CYS A 1 51 ? -3.905 11.580 15.280 1.00 11.72 ? 51 CYS A CA 1 ATOM 378 C C . CYS A 1 51 ? -3.425 10.168 15.470 1.00 11.83 ? 51 CYS A C 1 ATOM 379 O O . CYS A 1 51 ? -3.547 9.333 14.562 1.00 12.55 ? 51 CYS A O 1 ATOM 380 C CB . CYS A 1 51 ? -4.165 11.875 13.810 1.00 11.12 ? 51 CYS A CB 1 ATOM 381 S SG . CYS A 1 51 ? -5.161 13.384 13.607 1.00 11.26 ? 51 CYS A SG 1 ATOM 382 N N . GLY A 1 52 ? -2.923 9.879 16.674 1.00 11.86 ? 52 GLY A N 1 ATOM 383 C CA . GLY A 1 52 ? -2.586 8.519 17.082 1.00 12.48 ? 52 GLY A CA 1 ATOM 384 C C . GLY A 1 52 ? -1.106 8.270 17.240 1.00 12.52 ? 52 GLY A C 1 ATOM 385 O O . GLY A 1 52 ? -0.248 8.943 16.642 1.00 13.04 ? 52 GLY A O 1 ATOM 386 N N . ASP A 1 53 ? -0.816 7.299 18.092 1.00 13.29 ? 53 ASP A N 1 ATOM 387 C CA . ASP A 1 53 ? 0.545 6.917 18.423 1.00 13.63 ? 53 ASP A CA 1 ATOM 388 C C . ASP A 1 53 ? 0.885 5.584 17.729 1.00 12.95 ? 53 ASP A C 1 ATOM 389 O O . ASP A 1 53 ? 0.019 4.800 17.393 1.00 12.37 ? 53 ASP A O 1 ATOM 390 C CB . ASP A 1 53 ? 0.683 6.776 19.952 1.00 15.56 ? 53 ASP A CB 1 ATOM 391 C CG . ASP A 1 53 ? 0.494 8.091 20.695 1.00 19.45 ? 53 ASP A CG 1 ATOM 392 O OD1 . ASP A 1 53 ? 1.038 9.113 20.264 1.00 23.63 ? 53 ASP A OD1 1 ATOM 393 O OD2 . ASP A 1 53 ? -0.172 8.159 21.741 1.00 26.77 ? 53 ASP A OD2 1 ATOM 394 N N . TRP A 1 54 ? 2.175 5.306 17.618 1.00 12.57 ? 54 TRP A N 1 ATOM 395 C CA . TRP A 1 54 ? 2.679 4.068 17.033 1.00 12.36 ? 54 TRP A CA 1 ATOM 396 C C . TRP A 1 54 ? 2.052 2.880 17.737 1.00 13.22 ? 54 TRP A C 1 ATOM 397 O O . TRP A 1 54 ? 1.941 2.858 18.962 1.00 13.89 ? 54 TRP A O 1 ATOM 398 C CB . TRP A 1 54 ? 4.196 4.016 17.199 1.00 13.55 ? 54 TRP A CB 1 ATOM 399 C CG . TRP A 1 54 ? 4.856 2.885 16.527 1.00 12.79 ? 54 TRP A CG 1 ATOM 400 C CD1 . TRP A 1 54 ? 5.167 2.784 15.212 1.00 15.16 ? 54 TRP A CD1 1 ATOM 401 C CD2 . TRP A 1 54 ? 5.340 1.706 17.145 1.00 15.40 ? 54 TRP A CD2 1 ATOM 402 N NE1 . TRP A 1 54 ? 5.811 1.596 14.966 1.00 13.26 ? 54 TRP A NE1 1 ATOM 403 C CE2 . TRP A 1 54 ? 5.935 0.920 16.145 1.00 15.66 ? 54 TRP A CE2 1 ATOM 404 C CE3 . TRP A 1 54 ? 5.339 1.227 18.460 1.00 18.39 ? 54 TRP A CE3 1 ATOM 405 C CZ2 . TRP A 1 54 ? 6.510 -0.319 16.410 1.00 18.63 ? 54 TRP A CZ2 1 ATOM 406 C CZ3 . TRP A 1 54 ? 5.938 0.013 18.726 1.00 18.05 ? 54 TRP A CZ3 1 ATOM 407 C CH2 . TRP A 1 54 ? 6.498 -0.748 17.709 1.00 19.28 ? 54 TRP A CH2 1 ATOM 408 N N . GLY A 1 55 ? 1.638 1.899 16.951 1.00 11.97 ? 55 GLY A N 1 ATOM 409 C CA . GLY A 1 55 ? 1.032 0.684 17.501 1.00 11.97 ? 55 GLY A CA 1 ATOM 410 C C . GLY A 1 55 ? -0.471 0.637 17.469 1.00 12.26 ? 55 GLY A C 1 ATOM 411 O O . GLY A 1 55 ? -1.063 -0.404 17.767 1.00 13.41 ? 55 GLY A O 1 ATOM 412 N N . ASN A 1 56 ? -1.095 1.765 17.122 1.00 12.12 ? 56 ASN A N 1 ATOM 413 C CA . ASN A 1 56 ? -2.531 1.923 17.243 1.00 12.29 ? 56 ASN A CA 1 ATOM 414 C C . ASN A 1 56 ? -3.178 2.439 15.985 1.00 12.02 ? 56 ASN A C 1 ATOM 415 O O . ASN A 1 56 ? -2.504 3.106 15.205 1.00 11.70 ? 56 ASN A O 1 ATOM 416 C CB . ASN A 1 56 ? -2.826 2.964 18.334 1.00 13.77 ? 56 ASN A CB 1 ATOM 417 C CG . ASN A 1 56 ? -2.366 2.529 19.695 1.00 17.72 ? 56 ASN A CG 1 ATOM 418 O OD1 . ASN A 1 56 ? -2.692 1.437 20.159 1.00 19.99 ? 56 ASN A OD1 1 ATOM 419 N ND2 . ASN A 1 56 ? -1.583 3.389 20.347 1.00 25.23 ? 56 ASN A ND2 1 ATOM 420 N N . PRO A 1 57 ? -4.467 2.177 15.799 1.00 11.62 ? 57 PRO A N 1 ATOM 421 C CA . PRO A 1 57 ? -5.252 2.933 14.823 1.00 11.51 ? 57 PRO A CA 1 ATOM 422 C C . PRO A 1 57 ? -5.316 4.399 15.262 1.00 11.62 ? 57 PRO A C 1 ATOM 423 O O . PRO A 1 57 ? -5.065 4.726 16.436 1.00 12.25 ? 57 PRO A O 1 ATOM 424 C CB . PRO A 1 57 ? -6.643 2.284 14.865 1.00 12.05 ? 57 PRO A CB 1 ATOM 425 C CG . PRO A 1 57 ? -6.664 1.438 16.062 1.00 14.52 ? 57 PRO A CG 1 ATOM 426 C CD . PRO A 1 57 ? -5.296 1.275 16.622 1.00 12.03 ? 57 PRO A CD 1 ATOM 427 N N . PRO A 1 58 ? -5.714 5.277 14.344 1.00 10.90 ? 58 PRO A N 1 ATOM 428 C CA . PRO A 1 58 ? -5.921 6.674 14.708 1.00 11.64 ? 58 PRO A CA 1 ATOM 429 C C . PRO A 1 58 ? -7.214 6.792 15.559 1.00 12.49 ? 58 PRO A C 1 ATOM 430 O O . PRO A 1 58 ? -8.061 5.910 15.504 1.00 11.90 ? 58 PRO A O 1 ATOM 431 C CB . PRO A 1 58 ? -6.055 7.362 13.341 1.00 11.07 ? 58 PRO A CB 1 ATOM 432 C CG . PRO A 1 58 ? -6.741 6.322 12.476 1.00 9.97 ? 58 PRO A CG 1 ATOM 433 C CD . PRO A 1 58 ? -6.144 4.990 12.956 1.00 11.08 ? 58 PRO A CD 1 ATOM 434 N N . PRO A 1 59 ? -7.347 7.852 16.351 1.00 12.43 ? 59 PRO A N 1 ATOM 435 C CA . PRO A 1 59 ? -8.488 7.989 17.234 1.00 14.11 ? 59 PRO A CA 1 ATOM 436 C C . PRO A 1 59 ? -9.784 8.199 16.478 1.00 14.54 ? 59 PRO A C 1 ATOM 437 O O . PRO A 1 59 ? -9.811 8.911 15.475 1.00 13.71 ? 59 PRO A O 1 ATOM 438 C CB . PRO A 1 59 ? -8.129 9.203 18.080 1.00 14.16 ? 59 PRO A CB 1 ATOM 439 C CG . PRO A 1 59 ? -7.165 9.966 17.298 1.00 14.67 ? 59 PRO A CG 1 ATOM 440 C CD . PRO A 1 59 ? -6.387 8.955 16.492 1.00 13.86 ? 59 PRO A CD 1 ATOM 441 N N . LYS A 1 60 ? -10.874 7.600 16.973 1.00 15.32 ? 60 LYS A N 1 ATOM 442 C CA . LYS A 1 60 ? -12.154 7.658 16.281 1.00 17.44 ? 60 LYS A CA 1 ATOM 443 C C . LYS A 1 60 ? -12.803 9.041 16.289 1.00 16.95 ? 60 LYS A C 1 ATOM 444 O O . LYS A 1 60 ? -13.634 9.326 15.423 1.00 16.92 ? 60 LYS A O 1 ATOM 445 C CB . LYS A 1 60 ? -13.141 6.643 16.874 1.00 18.54 ? 60 LYS A CB 1 ATOM 446 C CG . LYS A 1 60 ? -12.877 5.183 16.511 1.00 21.53 ? 60 LYS A CG 1 ATOM 447 C CD . LYS A 1 60 ? -13.761 4.289 17.368 1.00 23.24 ? 60 LYS A CD 1 ATOM 448 C CE . LYS A 1 60 ? -13.318 2.805 17.410 1.00 27.21 ? 60 LYS A CE 1 ATOM 449 N NZ . LYS A 1 60 ? -12.649 2.372 18.699 1.00 30.12 ? 60 LYS A NZ 1 ATOM 450 N N . ASP A 1 61 ? -12.406 9.902 17.221 1.00 16.71 ? 61 ASP A N 1 ATOM 451 C CA . ASP A 1 61 ? -13.037 11.222 17.288 1.00 18.00 ? 61 ASP A CA 1 ATOM 452 C C . ASP A 1 61 ? -12.793 12.027 16.020 1.00 17.43 ? 61 ASP A C 1 ATOM 453 O O . ASP A 1 61 ? -13.712 12.618 15.469 1.00 19.15 ? 61 ASP A O 1 ATOM 454 C CB . ASP A 1 61 ? -12.680 12.000 18.571 1.00 18.90 ? 61 ASP A CB 1 ATOM 455 C CG . ASP A 1 61 ? -11.188 12.282 18.765 1.00 20.03 ? 61 ASP A CG 1 ATOM 456 O OD1 . ASP A 1 61 ? -10.296 11.691 18.109 1.00 20.34 ? 61 ASP A OD1 1 ATOM 457 O OD2 . ASP A 1 61 ? -10.760 13.088 19.638 1.00 21.04 ? 61 ASP A OD2 1 ATOM 458 N N . VAL A 1 62 ? -11.568 12.012 15.527 1.00 14.96 ? 62 VAL A N 1 ATOM 459 C CA . VAL A 1 62 ? -11.200 12.720 14.290 1.00 14.42 ? 62 VAL A CA 1 ATOM 460 C C . VAL A 1 62 ? -11.101 11.798 13.074 1.00 12.59 ? 62 VAL A C 1 ATOM 461 O O . VAL A 1 62 ? -11.178 12.266 11.938 1.00 11.34 ? 62 VAL A O 1 ATOM 462 C CB . VAL A 1 62 ? -9.886 13.561 14.428 1.00 14.95 ? 62 VAL A CB 1 ATOM 463 C CG1 . VAL A 1 62 ? -10.152 14.847 15.222 1.00 17.50 ? 62 VAL A CG1 1 ATOM 464 C CG2 . VAL A 1 62 ? -8.755 12.748 15.029 1.00 15.85 ? 62 VAL A CG2 1 ATOM 465 N N . CYS A 1 63 ? -10.975 10.488 13.301 1.00 11.84 ? 63 CYS A N 1 ATOM 466 C CA . CYS A 1 63 ? -10.764 9.519 12.225 1.00 11.81 ? 63 CYS A CA 1 ATOM 467 C C . CYS A 1 63 ? -11.803 8.399 12.273 1.00 12.42 ? 63 CYS A C 1 ATOM 468 O O . CYS A 1 63 ? -11.449 7.240 12.417 1.00 11.88 ? 63 CYS A O 1 ATOM 469 C CB . CYS A 1 63 ? -9.334 8.954 12.301 1.00 10.92 ? 63 CYS A CB 1 ATOM 470 S SG . CYS A 1 63 ? -8.113 10.277 11.997 1.00 10.76 ? 63 CYS A SG 1 ATOM 471 N N . PRO A 1 64 ? -13.097 8.718 12.165 1.00 13.01 ? 64 PRO A N 1 ATOM 472 C CA . PRO A 1 64 ? -14.114 7.659 12.127 1.00 13.81 ? 64 PRO A CA 1 ATOM 473 C C . PRO A 1 64 ? -14.038 6.820 10.859 1.00 14.06 ? 64 PRO A C 1 ATOM 474 O O . PRO A 1 64 ? -14.481 5.676 10.821 1.00 15.55 ? 64 PRO A O 1 ATOM 475 C CB . PRO A 1 64 ? -15.435 8.441 12.197 1.00 14.61 ? 64 PRO A CB 1 ATOM 476 C CG . PRO A 1 64 ? -15.127 9.794 11.634 1.00 13.93 ? 64 PRO A CG 1 ATOM 477 C CD . PRO A 1 64 ? -13.697 10.071 12.130 1.00 13.79 ? 64 PRO A CD 1 ATOM 478 N N . ASP A 1 65 ? -13.476 7.421 9.814 1.00 12.85 ? 65 ASP A N 1 ATOM 479 C CA . ASP A 1 65 ? -13.301 6.800 8.516 1.00 13.27 ? 65 ASP A CA 1 ATOM 480 C C . ASP A 1 65 ? -12.133 7.480 7.809 1.00 12.64 ? 65 ASP A C 1 ATOM 481 O O . ASP A 1 65 ? -11.631 8.506 8.269 1.00 12.29 ? 65 ASP A O 1 ATOM 482 C CB . ASP A 1 65 ? -14.581 6.840 7.662 1.00 14.13 ? 65 ASP A CB 1 ATOM 483 C CG . ASP A 1 65 ? -15.217 8.203 7.619 1.00 16.85 ? 65 ASP A CG 1 ATOM 484 O OD1 . ASP A 1 65 ? -14.524 9.184 7.333 1.00 16.90 ? 65 ASP A OD1 1 ATOM 485 O OD2 . ASP A 1 65 ? -16.448 8.359 7.809 1.00 23.20 ? 65 ASP A OD2 1 ATOM 486 N N . VAL A 1 66 ? -11.683 6.883 6.716 1.00 12.05 ? 66 VAL A N 1 ATOM 487 C CA . VAL A 1 66 ? -10.493 7.374 6.005 1.00 12.53 ? 66 VAL A CA 1 ATOM 488 C C . VAL A 1 66 ? -10.698 8.805 5.511 1.00 12.50 ? 66 VAL A C 1 ATOM 489 O O . VAL A 1 66 ? -9.832 9.666 5.633 1.00 11.20 ? 66 VAL A O 1 ATOM 490 C CB . VAL A 1 66 ? -10.075 6.438 4.842 1.00 12.46 ? 66 VAL A CB 1 ATOM 491 C CG1 . VAL A 1 66 ? -9.027 7.098 3.947 1.00 13.67 ? 66 VAL A CG1 1 ATOM 492 C CG2 . VAL A 1 66 ? -9.593 5.080 5.376 1.00 15.14 ? 66 VAL A CG2 1 ATOM 493 N N . GLU A 1 67 ? -11.868 9.058 4.935 1.00 12.91 ? 67 GLU A N 1 ATOM 494 C CA . GLU A 1 67 ? -12.160 10.354 4.347 1.00 14.56 ? 67 GLU A CA 1 ATOM 495 C C . GLU A 1 67 ? -12.113 11.475 5.383 1.00 13.60 ? 67 GLU A C 1 ATOM 496 O O . GLU A 1 67 ? -11.541 12.529 5.118 1.00 13.27 ? 67 GLU A O 1 ATOM 497 C CB A GLU A 1 67 ? -13.554 10.340 3.730 0.50 15.67 ? 67 GLU A CB 1 ATOM 498 C CB B GLU A 1 67 ? -13.510 10.275 3.631 0.50 14.97 ? 67 GLU A CB 1 ATOM 499 C CG A GLU A 1 67 ? -13.693 9.383 2.580 0.50 17.91 ? 67 GLU A CG 1 ATOM 500 C CG B GLU A 1 67 ? -13.872 11.476 2.777 0.50 14.70 ? 67 GLU A CG 1 ATOM 501 C CD A GLU A 1 67 ? -15.112 9.168 2.126 0.50 18.85 ? 67 GLU A CD 1 ATOM 502 C CD B GLU A 1 67 ? -15.218 11.317 2.079 0.50 16.81 ? 67 GLU A CD 1 ATOM 503 O OE1 A GLU A 1 67 ? -15.732 10.158 1.673 0.50 22.77 ? 67 GLU A OE1 1 ATOM 504 O OE1 B GLU A 1 67 ? -15.599 12.210 1.304 0.50 17.11 ? 67 GLU A OE1 1 ATOM 505 O OE2 A GLU A 1 67 ? -15.578 8.000 2.160 0.50 22.88 ? 67 GLU A OE2 1 ATOM 506 O OE2 B GLU A 1 67 ? -15.896 10.305 2.313 0.50 20.26 ? 67 GLU A OE2 1 ATOM 507 N N . SER A 1 68 ? -12.656 11.238 6.574 1.00 13.03 ? 68 SER A N 1 ATOM 508 C CA . SER A 1 68 ? -12.686 12.257 7.615 1.00 13.22 ? 68 SER A CA 1 ATOM 509 C C . SER A 1 68 ? -11.280 12.466 8.165 1.00 12.45 ? 68 SER A C 1 ATOM 510 O O . SER A 1 68 ? -10.857 13.598 8.440 1.00 12.03 ? 68 SER A O 1 ATOM 511 C CB . SER A 1 68 ? -13.616 11.837 8.743 1.00 14.51 ? 68 SER A CB 1 ATOM 512 O OG . SER A 1 68 ? -14.934 11.678 8.262 1.00 17.05 ? 68 SER A OG 1 ATOM 513 N N . CYS A 1 69 ? -10.562 11.368 8.375 1.00 11.61 ? 69 CYS A N 1 ATOM 514 C CA . CYS A 1 69 ? -9.198 11.413 8.877 1.00 11.37 ? 69 CYS A CA 1 ATOM 515 C C . CYS A 1 69 ? -8.293 12.272 7.969 1.00 10.44 ? 69 CYS A C 1 ATOM 516 O O . CYS A 1 69 ? -7.417 13.017 8.430 1.00 10.48 ? 69 CYS A O 1 ATOM 517 C CB . CYS A 1 69 ? -8.650 9.961 8.985 1.00 11.73 ? 69 CYS A CB 1 ATOM 518 S SG . CYS A 1 69 ? -7.280 9.773 10.152 1.00 11.73 ? 69 CYS A SG 1 ATOM 519 N N . ALA A 1 70 ? -8.529 12.161 6.661 1.00 9.44 ? 70 ALA A N 1 ATOM 520 C CA . ALA A 1 70 ? -7.724 12.851 5.649 1.00 9.73 ? 70 ALA A CA 1 ATOM 521 C C . ALA A 1 70 ? -7.847 14.357 5.741 1.00 9.70 ? 70 ALA A C 1 ATOM 522 O O . ALA A 1 70 ? -6.985 15.089 5.260 1.00 11.05 ? 70 ALA A O 1 ATOM 523 C CB . ALA A 1 70 ? -8.129 12.401 4.252 1.00 9.97 ? 70 ALA A CB 1 ATOM 524 N N . LYS A 1 71 ? -8.976 14.819 6.271 1.00 9.56 ? 71 LYS A N 1 ATOM 525 C CA . LYS A 1 71 ? -9.266 16.257 6.353 1.00 10.25 ? 71 LYS A CA 1 ATOM 526 C C . LYS A 1 71 ? -9.033 16.825 7.772 1.00 10.07 ? 71 LYS A C 1 ATOM 527 O O . LYS A 1 71 ? -8.789 18.035 7.937 1.00 9.89 ? 71 LYS A O 1 ATOM 528 C CB . LYS A 1 71 ? -10.706 16.514 5.944 1.00 10.01 ? 71 LYS A CB 1 ATOM 529 C CG . LYS A 1 71 ? -10.950 16.188 4.492 1.00 12.11 ? 71 LYS A CG 1 ATOM 530 C CD . LYS A 1 71 ? -12.382 16.410 3.989 1.00 13.25 ? 71 LYS A CD 1 ATOM 531 C CE . LYS A 1 71 ? -13.351 15.468 4.628 1.00 15.36 ? 71 LYS A CE 1 ATOM 532 N NZ . LYS A 1 71 ? -14.594 15.333 3.806 1.00 17.52 ? 71 LYS A NZ 1 ATOM 533 N N . ASN A 1 72 ? -9.090 15.963 8.791 1.00 9.74 ? 72 ASN A N 1 ATOM 534 C CA . ASN A 1 72 ? -8.976 16.398 10.195 1.00 9.64 ? 72 ASN A CA 1 ATOM 535 C C . ASN A 1 72 ? -7.566 16.315 10.763 1.00 9.47 ? 72 ASN A C 1 ATOM 536 O O . ASN A 1 72 ? -7.303 16.879 11.806 1.00 10.09 ? 72 ASN A O 1 ATOM 537 C CB . ASN A 1 72 ? -9.897 15.555 11.086 1.00 9.37 ? 72 ASN A CB 1 ATOM 538 C CG . ASN A 1 72 ? -11.374 15.865 10.877 1.00 9.62 ? 72 ASN A CG 1 ATOM 539 O OD1 . ASN A 1 72 ? -11.746 16.966 10.430 1.00 10.77 ? 72 ASN A OD1 1 ATOM 540 N ND2 . ASN A 1 72 ? -12.217 14.902 11.214 1.00 10.45 ? 72 ASN A ND2 1 ATOM 541 N N . CYS A 1 73 ? -6.677 15.586 10.089 1.00 9.45 ? 73 CYS A N 1 ATOM 542 C CA . CYS A 1 73 ? -5.306 15.388 10.534 1.00 9.27 ? 73 CYS A CA 1 ATOM 543 C C . CYS A 1 73 ? -4.353 16.035 9.559 1.00 9.38 ? 73 CYS A C 1 ATOM 544 O O . CYS A 1 73 ? -4.453 15.811 8.354 1.00 10.21 ? 73 CYS A O 1 ATOM 545 C CB . CYS A 1 73 ? -5.029 13.896 10.634 1.00 9.33 ? 73 CYS A CB 1 ATOM 546 S SG . CYS A 1 73 ? -6.119 13.061 11.853 1.00 10.24 ? 73 CYS A SG 1 ATOM 547 N N . ILE A 1 74 ? -3.450 16.856 10.103 1.00 9.42 ? 74 ILE A N 1 ATOM 548 C CA . ILE A 1 74 ? -2.534 17.702 9.355 1.00 9.63 ? 74 ILE A CA 1 ATOM 549 C C . ILE A 1 74 ? -1.104 17.283 9.629 1.00 9.01 ? 74 ILE A C 1 ATOM 550 O O . ILE A 1 74 ? -0.701 17.091 10.788 1.00 10.27 ? 74 ILE A O 1 ATOM 551 C CB . ILE A 1 74 ? -2.709 19.175 9.748 1.00 9.93 ? 74 ILE A CB 1 ATOM 552 C CG1 . ILE A 1 74 ? -4.194 19.597 9.776 1.00 11.41 ? 74 ILE A CG1 1 ATOM 553 C CG2 . ILE A 1 74 ? -1.862 20.058 8.849 1.00 10.77 ? 74 ILE A CG2 1 ATOM 554 C CD1 . ILE A 1 74 ? -4.905 19.500 8.441 1.00 12.58 ? 74 ILE A CD1 1 ATOM 555 N N . MET A 1 75 ? -0.338 17.124 8.553 1.00 9.23 ? 75 MET A N 1 ATOM 556 C CA . MET A 1 75 ? 1.073 16.716 8.615 1.00 9.32 ? 75 MET A CA 1 ATOM 557 C C . MET A 1 75 ? 1.923 17.899 8.160 1.00 9.26 ? 75 MET A C 1 ATOM 558 O O . MET A 1 75 ? 1.861 18.284 6.998 1.00 9.01 ? 75 MET A O 1 ATOM 559 C CB . MET A 1 75 ? 1.269 15.517 7.696 1.00 10.27 ? 75 MET A CB 1 ATOM 560 C CG . MET A 1 75 ? 2.711 15.113 7.481 1.00 10.70 ? 75 MET A CG 1 ATOM 561 S SD . MET A 1 75 ? 2.805 13.555 6.539 1.00 10.88 ? 75 MET A SD 1 ATOM 562 C CE . MET A 1 75 ? 1.914 13.916 5.060 1.00 11.10 ? 75 MET A CE 1 ATOM 563 N N . GLU A 1 76 ? 2.690 18.483 9.076 1.00 9.37 ? 76 GLU A N 1 ATOM 564 C CA . GLU A 1 76 ? 3.487 19.671 8.740 1.00 9.93 ? 76 GLU A CA 1 ATOM 565 C C . GLU A 1 76 ? 4.785 19.314 8.057 1.00 10.31 ? 76 GLU A C 1 ATOM 566 O O . GLU A 1 76 ? 5.450 18.346 8.427 1.00 10.85 ? 76 GLU A O 1 ATOM 567 C CB . GLU A 1 76 ? 3.822 20.477 10.004 1.00 10.74 ? 76 GLU A CB 1 ATOM 568 C CG . GLU A 1 76 ? 2.617 21.116 10.657 1.00 10.52 ? 76 GLU A CG 1 ATOM 569 C CD . GLU A 1 76 ? 1.922 22.139 9.767 1.00 11.39 ? 76 GLU A CD 1 ATOM 570 O OE1 . GLU A 1 76 ? 2.534 22.719 8.852 1.00 11.27 ? 76 GLU A OE1 1 ATOM 571 O OE2 . GLU A 1 76 ? 0.746 22.389 10.014 1.00 13.97 ? 76 GLU A OE2 1 ATOM 572 N N . GLY A 1 77 ? 5.192 20.148 7.111 1.00 9.80 ? 77 GLY A N 1 ATOM 573 C CA . GLY A 1 77 ? 6.539 20.104 6.582 1.00 9.77 ? 77 GLY A CA 1 ATOM 574 C C . GLY A 1 77 ? 7.552 20.422 7.653 1.00 9.89 ? 77 GLY A C 1 ATOM 575 O O . GLY A 1 77 ? 7.244 21.151 8.619 1.00 9.92 ? 77 GLY A O 1 ATOM 576 N N . ILE A 1 78 ? 8.758 19.882 7.493 1.00 9.83 ? 78 ILE A N 1 ATOM 577 C CA . ILE A 1 78 ? 9.877 20.153 8.377 1.00 10.05 ? 78 ILE A CA 1 ATOM 578 C C . ILE A 1 78 ? 10.867 21.060 7.627 1.00 10.21 ? 78 ILE A C 1 ATOM 579 O O . ILE A 1 78 ? 11.462 20.634 6.641 1.00 10.74 ? 78 ILE A O 1 ATOM 580 C CB . ILE A 1 78 ? 10.581 18.832 8.783 1.00 9.98 ? 78 ILE A CB 1 ATOM 581 C CG1 . ILE A 1 78 ? 9.666 17.980 9.653 1.00 10.74 ? 78 ILE A CG1 1 ATOM 582 C CG2 . ILE A 1 78 ? 11.921 19.137 9.484 1.00 10.38 ? 78 ILE A CG2 1 ATOM 583 C CD1 . ILE A 1 78 ? 10.177 16.555 9.823 1.00 10.52 ? 78 ILE A CD1 1 ATOM 584 N N . PRO A 1 79 ? 11.012 22.305 8.073 1.00 10.65 ? 79 PRO A N 1 ATOM 585 C CA . PRO A 1 79 ? 11.889 23.259 7.399 1.00 10.74 ? 79 PRO A CA 1 ATOM 586 C C . PRO A 1 79 ? 13.331 23.235 7.884 1.00 11.54 ? 79 PRO A C 1 ATOM 587 O O . PRO A 1 79 ? 14.204 23.822 7.253 1.00 13.20 ? 79 PRO A O 1 ATOM 588 C CB . PRO A 1 79 ? 11.209 24.597 7.721 1.00 12.22 ? 79 PRO A CB 1 ATOM 589 C CG . PRO A 1 79 ? 10.617 24.427 9.025 1.00 12.01 ? 79 PRO A CG 1 ATOM 590 C CD . PRO A 1 79 ? 10.175 22.975 9.086 1.00 11.61 ? 79 PRO A CD 1 ATOM 591 N N . ASP A 1 80 ? 13.586 22.508 8.960 1.00 11.33 ? 80 ASP A N 1 ATOM 592 C CA . ASP A 1 80 ? 14.929 22.394 9.518 1.00 10.88 ? 80 ASP A CA 1 ATOM 593 C C . ASP A 1 80 ? 15.115 20.979 10.040 1.00 9.85 ? 80 ASP A C 1 ATOM 594 O O . ASP A 1 80 ? 14.770 20.671 11.180 1.00 10.58 ? 80 ASP A O 1 ATOM 595 C CB . ASP A 1 80 ? 15.132 23.423 10.624 1.00 11.39 ? 80 ASP A CB 1 ATOM 596 C CG . ASP A 1 80 ? 16.486 23.356 11.255 1.00 12.84 ? 80 ASP A CG 1 ATOM 597 O OD1 . ASP A 1 80 ? 17.320 22.525 10.800 1.00 13.55 ? 80 ASP A OD1 1 ATOM 598 O OD2 . ASP A 1 80 ? 16.754 24.096 12.251 1.00 15.00 ? 80 ASP A OD2 1 ATOM 599 N N . TYR A 1 81 ? 15.677 20.120 9.187 1.00 10.16 ? 81 TYR A N 1 ATOM 600 C CA . TYR A 1 81 ? 15.864 18.702 9.516 1.00 10.14 ? 81 TYR A CA 1 ATOM 601 C C . TYR A 1 81 ? 16.842 18.476 10.660 1.00 10.31 ? 81 TYR A C 1 ATOM 602 O O . TYR A 1 81 ? 16.797 17.443 11.318 1.00 10.26 ? 81 TYR A O 1 ATOM 603 C CB . TYR A 1 81 ? 16.306 17.907 8.268 1.00 9.72 ? 81 TYR A CB 1 ATOM 604 C CG . TYR A 1 81 ? 15.163 17.247 7.523 1.00 9.97 ? 81 TYR A CG 1 ATOM 605 C CD1 . TYR A 1 81 ? 14.091 17.975 7.006 1.00 9.95 ? 81 TYR A CD1 1 ATOM 606 C CD2 . TYR A 1 81 ? 15.191 15.887 7.287 1.00 9.03 ? 81 TYR A CD2 1 ATOM 607 C CE1 . TYR A 1 81 ? 13.073 17.344 6.315 1.00 9.78 ? 81 TYR A CE1 1 ATOM 608 C CE2 . TYR A 1 81 ? 14.167 15.255 6.632 1.00 9.44 ? 81 TYR A CE2 1 ATOM 609 C CZ . TYR A 1 81 ? 13.109 15.984 6.127 1.00 8.56 ? 81 TYR A CZ 1 ATOM 610 O OH . TYR A 1 81 ? 12.069 15.327 5.473 1.00 8.82 ? 81 TYR A OH 1 ATOM 611 N N . SER A 1 82 ? 17.681 19.465 10.958 1.00 10.09 ? 82 SER A N 1 ATOM 612 C CA . SER A 1 82 ? 18.619 19.337 12.082 1.00 10.60 ? 82 SER A CA 1 ATOM 613 C C . SER A 1 82 ? 17.933 19.208 13.438 1.00 10.84 ? 82 SER A C 1 ATOM 614 O O . SER A 1 82 ? 18.468 18.650 14.387 1.00 11.65 ? 82 SER A O 1 ATOM 615 C CB . SER A 1 82 ? 19.648 20.484 12.086 1.00 11.05 ? 82 SER A CB 1 ATOM 616 O OG . SER A 1 82 ? 19.083 21.691 12.626 1.00 12.41 ? 82 SER A OG 1 ATOM 617 N N . GLN A 1 83 ? 16.683 19.663 13.513 1.00 10.53 ? 83 GLN A N 1 ATOM 618 C CA . GLN A 1 83 ? 15.872 19.507 14.711 1.00 11.44 ? 83 GLN A CA 1 ATOM 619 C C . GLN A 1 83 ? 15.479 18.065 14.994 1.00 11.25 ? 83 GLN A C 1 ATOM 620 O O . GLN A 1 83 ? 14.997 17.765 16.079 1.00 12.69 ? 83 GLN A O 1 ATOM 621 C CB . GLN A 1 83 ? 14.611 20.363 14.622 1.00 12.84 ? 83 GLN A CB 1 ATOM 622 C CG . GLN A 1 83 ? 14.873 21.836 14.456 1.00 14.40 ? 83 GLN A CG 1 ATOM 623 C CD . GLN A 1 83 ? 15.658 22.423 15.572 1.00 16.63 ? 83 GLN A CD 1 ATOM 624 O OE1 . GLN A 1 83 ? 15.427 22.104 16.736 1.00 19.13 ? 83 GLN A OE1 1 ATOM 625 N NE2 . GLN A 1 83 ? 16.580 23.298 15.234 1.00 19.89 ? 83 GLN A NE2 1 ATOM 626 N N . TYR A 1 84 ? 15.686 17.191 13.996 1.00 9.71 ? 84 TYR A N 1 ATOM 627 C CA . TYR A 1 84 ? 15.361 15.777 14.104 1.00 10.18 ? 84 TYR A CA 1 ATOM 628 C C . TYR A 1 84 ? 16.623 14.950 14.040 1.00 9.96 ? 84 TYR A C 1 ATOM 629 O O . TYR A 1 84 ? 16.572 13.743 13.852 1.00 10.31 ? 84 TYR A O 1 ATOM 630 C CB . TYR A 1 84 ? 14.379 15.362 12.995 1.00 9.77 ? 84 TYR A CB 1 ATOM 631 C CG . TYR A 1 84 ? 13.045 16.034 13.163 1.00 10.47 ? 84 TYR A CG 1 ATOM 632 C CD1 . TYR A 1 84 ? 12.856 17.347 12.726 1.00 11.87 ? 84 TYR A CD1 1 ATOM 633 C CD2 . TYR A 1 84 ? 11.986 15.387 13.757 1.00 11.55 ? 84 TYR A CD2 1 ATOM 634 C CE1 . TYR A 1 84 ? 11.663 17.986 12.913 1.00 12.57 ? 84 TYR A CE1 1 ATOM 635 C CE2 . TYR A 1 84 ? 10.780 16.025 13.935 1.00 12.02 ? 84 TYR A CE2 1 ATOM 636 C CZ . TYR A 1 84 ? 10.622 17.327 13.519 1.00 11.48 ? 84 TYR A CZ 1 ATOM 637 O OH . TYR A 1 84 ? 9.385 17.933 13.683 1.00 13.71 ? 84 TYR A OH 1 ATOM 638 N N . GLY A 1 85 ? 17.766 15.595 14.235 1.00 9.71 ? 85 GLY A N 1 ATOM 639 C CA . GLY A 1 85 ? 19.047 14.896 14.160 1.00 9.54 ? 85 GLY A CA 1 ATOM 640 C C . GLY A 1 85 ? 19.509 14.464 12.793 1.00 10.18 ? 85 GLY A C 1 ATOM 641 O O . GLY A 1 85 ? 20.348 13.555 12.688 1.00 9.24 ? 85 GLY A O 1 ATOM 642 N N . VAL A 1 86 ? 18.999 15.115 11.747 1.00 9.78 ? 86 VAL A N 1 ATOM 643 C CA . VAL A 1 86 ? 19.320 14.707 10.376 1.00 9.86 ? 86 VAL A CA 1 ATOM 644 C C . VAL A 1 86 ? 20.011 15.856 9.662 1.00 10.22 ? 86 VAL A C 1 ATOM 645 O O . VAL A 1 86 ? 19.424 16.913 9.532 1.00 9.99 ? 86 VAL A O 1 ATOM 646 C CB . VAL A 1 86 ? 18.057 14.289 9.574 1.00 9.52 ? 86 VAL A CB 1 ATOM 647 C CG1 . VAL A 1 86 ? 18.433 13.871 8.153 1.00 9.87 ? 86 VAL A CG1 1 ATOM 648 C CG2 . VAL A 1 86 ? 17.346 13.151 10.258 1.00 10.71 ? 86 VAL A CG2 1 ATOM 649 N N . THR A 1 87 ? 21.264 15.648 9.234 1.00 9.56 ? 87 THR A N 1 ATOM 650 C CA . THR A 1 87 ? 21.987 16.648 8.451 1.00 9.48 ? 87 THR A CA 1 ATOM 651 C C . THR A 1 87 ? 22.767 15.950 7.368 1.00 9.72 ? 87 THR A C 1 ATOM 652 O O . THR A 1 87 ? 23.128 14.775 7.519 1.00 10.02 ? 87 THR A O 1 ATOM 653 C CB . THR A 1 87 ? 22.964 17.513 9.308 1.00 9.55 ? 87 THR A CB 1 ATOM 654 O OG1 . THR A 1 87 ? 23.873 16.668 10.021 1.00 10.83 ? 87 THR A OG1 1 ATOM 655 C CG2 . THR A 1 87 ? 22.247 18.368 10.340 1.00 10.48 ? 87 THR A CG2 1 ATOM 656 N N . THR A 1 88 ? 23.050 16.684 6.286 1.00 9.71 ? 88 THR A N 1 ATOM 657 C CA . THR A 1 88 ? 23.946 16.191 5.243 1.00 10.51 ? 88 THR A CA 1 ATOM 658 C C . THR A 1 88 ? 25.038 17.197 4.969 1.00 11.25 ? 88 THR A C 1 ATOM 659 O O . THR A 1 88 ? 24.887 18.390 5.236 1.00 12.65 ? 88 THR A O 1 ATOM 660 C CB . THR A 1 88 ? 23.202 15.910 3.934 1.00 10.66 ? 88 THR A CB 1 ATOM 661 O OG1 . THR A 1 88 ? 22.543 17.103 3.488 1.00 10.88 ? 88 THR A OG1 1 ATOM 662 C CG2 . THR A 1 88 ? 22.119 14.844 4.137 1.00 11.61 ? 88 THR A CG2 1 ATOM 663 N N . ASN A 1 89 ? 26.122 16.673 4.411 1.00 11.96 ? 89 ASN A N 1 ATOM 664 C CA . ASN A 1 89 ? 27.280 17.455 3.969 1.00 12.06 ? 89 ASN A CA 1 ATOM 665 C C . ASN A 1 89 ? 27.867 16.731 2.762 1.00 11.63 ? 89 ASN A C 1 ATOM 666 O O . ASN A 1 89 ? 28.592 15.773 2.916 1.00 11.89 ? 89 ASN A O 1 ATOM 667 C CB . ASN A 1 89 ? 28.304 17.542 5.096 1.00 12.57 ? 89 ASN A CB 1 ATOM 668 C CG . ASN A 1 89 ? 29.516 18.380 4.758 1.00 15.32 ? 89 ASN A CG 1 ATOM 669 O OD1 . ASN A 1 89 ? 29.659 18.914 3.669 1.00 17.77 ? 89 ASN A OD1 1 ATOM 670 N ND2 . ASN A 1 89 ? 30.410 18.496 5.732 1.00 20.00 ? 89 ASN A ND2 1 ATOM 671 N N . GLY A 1 90 ? 27.510 17.153 1.554 1.00 11.78 ? 90 GLY A N 1 ATOM 672 C CA . GLY A 1 90 ? 28.009 16.542 0.336 1.00 11.90 ? 90 GLY A CA 1 ATOM 673 C C . GLY A 1 90 ? 27.496 15.135 0.191 1.00 11.29 ? 90 GLY A C 1 ATOM 674 O O . GLY A 1 90 ? 26.305 14.939 -0.041 1.00 11.89 ? 90 GLY A O 1 ATOM 675 N N . THR A 1 91 ? 28.385 14.158 0.367 1.00 10.21 ? 91 THR A N 1 ATOM 676 C CA . THR A 1 91 ? 28.032 12.735 0.293 1.00 10.35 ? 91 THR A CA 1 ATOM 677 C C . THR A 1 91 ? 27.817 12.078 1.648 1.00 10.23 ? 91 THR A C 1 ATOM 678 O O . THR A 1 91 ? 27.600 10.851 1.705 1.00 9.95 ? 91 THR A O 1 ATOM 679 C CB . THR A 1 91 ? 29.131 11.966 -0.417 1.00 10.91 ? 91 THR A CB 1 ATOM 680 O OG1 . THR A 1 91 ? 30.299 11.993 0.403 1.00 11.09 ? 91 THR A OG1 1 ATOM 681 C CG2 . THR A 1 91 ? 29.503 12.573 -1.792 1.00 11.30 ? 91 THR A CG2 1 ATOM 682 N N . SER A 1 92 ? 27.830 12.856 2.734 1.00 10.45 ? 92 SER A N 1 ATOM 683 C CA . SER A 1 92 ? 27.640 12.319 4.071 1.00 10.82 ? 92 SER A CA 1 ATOM 684 C C . SER A 1 92 ? 26.245 12.642 4.627 1.00 10.24 ? 92 SER A C 1 ATOM 685 O O . SER A 1 92 ? 25.748 13.777 4.485 1.00 10.38 ? 92 SER A O 1 ATOM 686 C CB A SER A 1 92 ? 28.684 12.909 5.024 0.50 10.78 ? 92 SER A CB 1 ATOM 687 C CB B SER A 1 92 ? 28.705 12.841 5.026 0.50 12.05 ? 92 SER A CB 1 ATOM 688 O OG A SER A 1 92 ? 29.958 12.292 4.846 0.50 8.31 ? 92 SER A OG 1 ATOM 689 O OG B SER A 1 92 ? 28.563 14.219 5.253 0.50 16.46 ? 92 SER A OG 1 ATOM 690 N N . LEU A 1 93 ? 25.649 11.634 5.270 1.00 9.25 ? 93 LEU A N 1 ATOM 691 C CA . LEU A 1 93 ? 24.417 11.750 6.029 1.00 9.46 ? 93 LEU A CA 1 ATOM 692 C C . LEU A 1 93 ? 24.726 11.420 7.484 1.00 8.99 ? 93 LEU A C 1 ATOM 693 O O . LEU A 1 93 ? 25.165 10.313 7.794 1.00 9.63 ? 93 LEU A O 1 ATOM 694 C CB . LEU A 1 93 ? 23.383 10.761 5.481 1.00 9.85 ? 93 LEU A CB 1 ATOM 695 C CG . LEU A 1 93 ? 22.105 10.593 6.292 1.00 9.56 ? 93 LEU A CG 1 ATOM 696 C CD1 . LEU A 1 93 ? 21.273 11.874 6.308 1.00 9.84 ? 93 LEU A CD1 1 ATOM 697 C CD2 . LEU A 1 93 ? 21.311 9.439 5.729 1.00 11.05 ? 93 LEU A CD2 1 ATOM 698 N N . ARG A 1 94 ? 24.468 12.371 8.378 1.00 9.17 ? 94 ARG A N 1 ATOM 699 C CA . ARG A 1 94 ? 24.649 12.196 9.815 1.00 9.61 ? 94 ARG A CA 1 ATOM 700 C C . ARG A 1 94 ? 23.279 12.037 10.476 1.00 9.36 ? 94 ARG A C 1 ATOM 701 O O . ARG A 1 94 ? 22.401 12.904 10.305 1.00 9.50 ? 94 ARG A O 1 ATOM 702 C CB . ARG A 1 94 ? 25.391 13.414 10.372 1.00 9.77 ? 94 ARG A CB 1 ATOM 703 C CG . ARG A 1 94 ? 25.691 13.326 11.842 1.00 10.16 ? 94 ARG A CG 1 ATOM 704 C CD . ARG A 1 94 ? 26.186 14.664 12.406 1.00 11.34 ? 94 ARG A CD 1 ATOM 705 N NE . ARG A 1 94 ? 26.612 14.580 13.793 1.00 12.37 ? 94 ARG A NE 1 ATOM 706 C CZ . ARG A 1 94 ? 26.725 15.621 14.592 1.00 14.96 ? 94 ARG A CZ 1 ATOM 707 N NH1 . ARG A 1 94 ? 26.373 16.826 14.180 1.00 15.71 ? 94 ARG A NH1 1 ATOM 708 N NH2 . ARG A 1 94 ? 27.127 15.429 15.823 1.00 15.02 ? 94 ARG A NH2 1 ATOM 709 N N . LEU A 1 95 ? 23.128 10.962 11.238 1.00 9.19 ? 95 LEU A N 1 ATOM 710 C CA . LEU A 1 95 ? 21.955 10.699 12.043 1.00 9.30 ? 95 LEU A CA 1 ATOM 711 C C . LEU A 1 95 ? 22.320 10.700 13.515 1.00 9.88 ? 95 LEU A C 1 ATOM 712 O O . LEU A 1 95 ? 23.057 9.833 13.980 1.00 10.00 ? 95 LEU A O 1 ATOM 713 C CB . LEU A 1 95 ? 21.322 9.343 11.686 1.00 9.25 ? 95 LEU A CB 1 ATOM 714 C CG . LEU A 1 95 ? 20.920 9.104 10.231 1.00 9.65 ? 95 LEU A CG 1 ATOM 715 C CD1 . LEU A 1 95 ? 20.315 7.721 10.057 1.00 10.40 ? 95 LEU A CD1 1 ATOM 716 C CD2 . LEU A 1 95 ? 19.950 10.195 9.714 1.00 10.76 ? 95 LEU A CD2 1 ATOM 717 N N . GLN A 1 96 ? 21.808 11.688 14.236 1.00 9.43 ? 96 GLN A N 1 ATOM 718 C CA . GLN A 1 96 ? 22.005 11.824 15.673 1.00 9.80 ? 96 GLN A CA 1 ATOM 719 C C . GLN A 1 96 ? 20.823 11.217 16.381 1.00 9.08 ? 96 GLN A C 1 ATOM 720 O O . GLN A 1 96 ? 19.660 11.602 16.130 1.00 9.78 ? 96 GLN A O 1 ATOM 721 C CB . GLN A 1 96 ? 22.087 13.289 16.052 1.00 10.37 ? 96 GLN A CB 1 ATOM 722 C CG . GLN A 1 96 ? 23.304 14.010 15.531 1.00 10.23 ? 96 GLN A CG 1 ATOM 723 C CD . GLN A 1 96 ? 23.085 15.492 15.576 1.00 10.52 ? 96 GLN A CD 1 ATOM 724 O OE1 . GLN A 1 96 ? 22.512 16.059 14.645 1.00 11.55 ? 96 GLN A OE1 1 ATOM 725 N NE2 . GLN A 1 96 ? 23.473 16.125 16.682 1.00 14.24 ? 96 GLN A NE2 1 ATOM 726 N N . HIS A 1 97 ? 21.075 10.254 17.270 1.00 9.33 ? 97 HIS A N 1 ATOM 727 C CA . HIS A 1 97 ? 19.981 9.629 18.038 1.00 9.72 ? 97 HIS A CA 1 ATOM 728 C C . HIS A 1 97 ? 19.402 10.573 19.113 1.00 9.95 ? 97 HIS A C 1 ATOM 729 O O . HIS A 1 97 ? 18.187 10.630 19.315 1.00 10.01 ? 97 HIS A O 1 ATOM 730 C CB . HIS A 1 97 ? 20.506 8.374 18.721 1.00 9.57 ? 97 HIS A CB 1 ATOM 731 C CG . HIS A 1 97 ? 19.430 7.554 19.320 1.00 9.82 ? 97 HIS A CG 1 ATOM 732 N ND1 . HIS A 1 97 ? 19.426 7.098 20.628 1.00 12.57 ? 97 HIS A ND1 1 ATOM 733 C CD2 . HIS A 1 97 ? 18.299 7.084 18.750 1.00 7.76 ? 97 HIS A CD2 1 ATOM 734 C CE1 . HIS A 1 97 ? 18.322 6.386 20.820 1.00 7.21 ? 97 HIS A CE1 1 ATOM 735 N NE2 . HIS A 1 97 ? 17.625 6.375 19.700 1.00 13.30 ? 97 HIS A NE2 1 ATOM 736 N N . ILE A 1 98 ? 20.315 11.280 19.796 1.00 10.37 ? 98 ILE A N 1 ATOM 737 C CA . ILE A 1 98 ? 20.011 12.200 20.890 1.00 10.59 ? 98 ILE A CA 1 ATOM 738 C C . ILE A 1 98 ? 20.678 13.524 20.572 1.00 10.73 ? 98 ILE A C 1 ATOM 739 O O . ILE A 1 98 ? 21.850 13.548 20.160 1.00 11.73 ? 98 ILE A O 1 ATOM 740 C CB . ILE A 1 98 ? 20.499 11.646 22.246 1.00 10.63 ? 98 ILE A CB 1 ATOM 741 C CG1 . ILE A 1 98 ? 19.961 10.236 22.487 1.00 11.43 ? 98 ILE A CG1 1 ATOM 742 C CG2 . ILE A 1 98 ? 20.130 12.584 23.386 1.00 10.51 ? 98 ILE A CG2 1 ATOM 743 C CD1 . ILE A 1 98 ? 20.392 9.638 23.800 1.00 12.12 ? 98 ILE A CD1 1 ATOM 744 N N . LEU A 1 99 ? 19.925 14.616 20.742 1.00 11.28 ? 99 LEU A N 1 ATOM 745 C CA . LEU A 1 99 ? 20.444 15.974 20.514 1.00 12.81 ? 99 LEU A CA 1 ATOM 746 C C . LEU A 1 99 ? 21.026 16.548 21.802 1.00 13.84 ? 99 LEU A C 1 ATOM 747 O O . LEU A 1 99 ? 20.692 16.079 22.879 1.00 12.69 ? 99 LEU A O 1 ATOM 748 C CB . LEU A 1 99 ? 19.343 16.859 19.951 1.00 13.02 ? 99 LEU A CB 1 ATOM 749 C CG . LEU A 1 99 ? 18.726 16.371 18.641 1.00 13.42 ? 99 LEU A CG 1 ATOM 750 C CD1 . LEU A 1 99 ? 17.604 17.268 18.224 1.00 14.28 ? 99 LEU A CD1 1 ATOM 751 C CD2 . LEU A 1 99 ? 19.774 16.356 17.588 1.00 16.50 ? 99 LEU A CD2 1 ATOM 752 N N . PRO A 1 100 ? 21.905 17.542 21.705 1.00 14.88 ? 100 PRO A N 1 ATOM 753 C CA . PRO A 1 100 ? 22.468 18.153 22.928 1.00 15.29 ? 100 PRO A CA 1 ATOM 754 C C . PRO A 1 100 ? 21.424 18.564 23.964 1.00 15.20 ? 100 PRO A C 1 ATOM 755 O O . PRO A 1 100 ? 21.696 18.444 25.154 1.00 16.39 ? 100 PRO A O 1 ATOM 756 C CB . PRO A 1 100 ? 23.237 19.349 22.386 1.00 16.30 ? 100 PRO A CB 1 ATOM 757 C CG . PRO A 1 100 ? 23.694 18.904 21.094 1.00 16.94 ? 100 PRO A CG 1 ATOM 758 C CD . PRO A 1 100 ? 22.541 18.095 20.499 1.00 15.98 ? 100 PRO A CD 1 ATOM 759 N N . ASP A 1 101 ? 20.246 19.015 23.531 1.00 14.64 ? 101 ASP A N 1 ATOM 760 C CA . ASP A 1 101 ? 19.191 19.423 24.452 1.00 15.21 ? 101 ASP A CA 1 ATOM 761 C C . ASP A 1 101 ? 18.374 18.290 25.061 1.00 14.75 ? 101 ASP A C 1 ATOM 762 O O . ASP A 1 101 ? 17.470 18.532 25.867 1.00 15.39 ? 101 ASP A O 1 ATOM 763 C CB . ASP A 1 101 ? 18.281 20.465 23.808 1.00 16.10 ? 101 ASP A CB 1 ATOM 764 C CG . ASP A 1 101 ? 17.555 19.970 22.590 1.00 18.67 ? 101 ASP A CG 1 ATOM 765 O OD1 . ASP A 1 101 ? 17.193 18.765 22.469 1.00 17.68 ? 101 ASP A OD1 1 ATOM 766 O OD2 . ASP A 1 101 ? 17.274 20.787 21.691 1.00 25.31 ? 101 ASP A OD2 1 ATOM 767 N N . GLY A 1 102 ? 18.729 17.051 24.735 1.00 14.05 ? 102 GLY A N 1 ATOM 768 C CA . GLY A 1 102 ? 18.137 15.867 25.357 1.00 13.25 ? 102 GLY A CA 1 ATOM 769 C C . GLY A 1 102 ? 16.972 15.264 24.587 1.00 12.69 ? 102 GLY A C 1 ATOM 770 O O . GLY A 1 102 ? 16.468 14.208 24.989 1.00 13.34 ? 102 GLY A O 1 ATOM 771 N N . ARG A 1 103 ? 16.552 15.891 23.484 1.00 12.29 ? 103 ARG A N 1 ATOM 772 C CA . ARG A 1 103 ? 15.556 15.247 22.633 1.00 12.30 ? 103 ARG A CA 1 ATOM 773 C C . ARG A 1 103 ? 16.157 13.971 22.038 1.00 11.72 ? 103 ARG A C 1 ATOM 774 O O . ARG A 1 103 ? 17.363 13.922 21.756 1.00 11.06 ? 103 ARG A O 1 ATOM 775 C CB . ARG A 1 103 ? 15.070 16.171 21.507 1.00 12.75 ? 103 ARG A CB 1 ATOM 776 C CG . ARG A 1 103 ? 14.134 17.300 21.963 1.00 13.33 ? 103 ARG A CG 1 ATOM 777 C CD . ARG A 1 103 ? 13.790 18.253 20.828 1.00 13.91 ? 103 ARG A CD 1 ATOM 778 N NE . ARG A 1 103 ? 14.965 19.045 20.450 1.00 16.38 ? 103 ARG A NE 1 ATOM 779 C CZ . ARG A 1 103 ? 15.040 19.868 19.398 1.00 17.14 ? 103 ARG A CZ 1 ATOM 780 N NH1 . ARG A 1 103 ? 14.000 20.009 18.589 1.00 18.90 ? 103 ARG A NH1 1 ATOM 781 N NH2 . ARG A 1 103 ? 16.151 20.553 19.164 1.00 19.14 ? 103 ARG A NH2 1 ATOM 782 N N . VAL A 1 104 ? 15.307 12.973 21.822 1.00 11.43 ? 104 VAL A N 1 ATOM 783 C CA . VAL A 1 104 ? 15.719 11.671 21.266 1.00 11.08 ? 104 VAL A CA 1 ATOM 784 C C . VAL A 1 104 ? 14.961 11.455 19.964 1.00 10.84 ? 104 VAL A C 1 ATOM 785 O O . VAL A 1 104 ? 13.971 10.717 19.930 1.00 11.78 ? 104 VAL A O 1 ATOM 786 C CB . VAL A 1 104 ? 15.431 10.507 22.253 1.00 11.30 ? 104 VAL A CB 1 ATOM 787 C CG1 . VAL A 1 104 ? 16.041 9.237 21.744 1.00 12.20 ? 104 VAL A CG1 1 ATOM 788 C CG2 . VAL A 1 104 ? 16.000 10.808 23.636 1.00 12.32 ? 104 VAL A CG2 1 ATOM 789 N N . PRO A 1 105 ? 15.368 12.137 18.895 1.00 10.02 ? 105 PRO A N 1 ATOM 790 C CA . PRO A 1 105 ? 14.617 12.021 17.639 1.00 9.66 ? 105 PRO A CA 1 ATOM 791 C C . PRO A 1 105 ? 14.669 10.646 16.988 1.00 9.84 ? 105 PRO A C 1 ATOM 792 O O . PRO A 1 105 ? 13.756 10.295 16.264 1.00 9.91 ? 105 PRO A O 1 ATOM 793 C CB . PRO A 1 105 ? 15.251 13.108 16.758 1.00 10.25 ? 105 PRO A CB 1 ATOM 794 C CG . PRO A 1 105 ? 16.611 13.341 17.308 1.00 10.06 ? 105 PRO A CG 1 ATOM 795 C CD . PRO A 1 105 ? 16.417 13.175 18.790 1.00 9.96 ? 105 PRO A CD 1 ATOM 796 N N . SER A 1 106 ? 15.723 9.877 17.232 1.00 9.69 ? 106 SER A N 1 ATOM 797 C CA . SER A 1 106 ? 15.839 8.520 16.671 1.00 9.42 ? 106 SER A CA 1 ATOM 798 C C . SER A 1 106 ? 15.370 8.480 15.210 1.00 9.41 ? 106 SER A C 1 ATOM 799 O O . SER A 1 106 ? 14.461 7.714 14.850 1.00 9.43 ? 106 SER A O 1 ATOM 800 C CB . SER A 1 106 ? 15.048 7.548 17.563 1.00 9.65 ? 106 SER A CB 1 ATOM 801 O OG . SER A 1 106 ? 15.284 6.179 17.234 1.00 9.35 ? 106 SER A OG 1 ATOM 802 N N . PRO A 1 107 ? 15.973 9.307 14.350 1.00 8.63 ? 107 PRO A N 1 ATOM 803 C CA . PRO A 1 107 ? 15.427 9.487 13.010 1.00 8.68 ? 107 PRO A CA 1 ATOM 804 C C . PRO A 1 107 ? 15.462 8.257 12.116 1.00 8.35 ? 107 PRO A C 1 ATOM 805 O O . PRO A 1 107 ? 16.433 7.502 12.124 1.00 9.03 ? 107 PRO A O 1 ATOM 806 C CB . PRO A 1 107 ? 16.287 10.590 12.415 1.00 9.11 ? 107 PRO A CB 1 ATOM 807 C CG . PRO A 1 107 ? 17.571 10.504 13.167 1.00 8.89 ? 107 PRO A CG 1 ATOM 808 C CD . PRO A 1 107 ? 17.154 10.160 14.565 1.00 9.44 ? 107 PRO A CD 1 ATOM 809 N N . ARG A 1 108 ? 14.404 8.127 11.299 1.00 8.15 ? 108 ARG A N 1 ATOM 810 C CA . ARG A 1 108 ? 14.330 7.187 10.171 1.00 7.96 ? 108 ARG A CA 1 ATOM 811 C C . ARG A 1 108 ? 14.025 7.990 8.908 1.00 7.74 ? 108 ARG A C 1 ATOM 812 O O . ARG A 1 108 ? 13.046 8.740 8.875 1.00 8.12 ? 108 ARG A O 1 ATOM 813 C CB . ARG A 1 108 ? 13.275 6.087 10.401 1.00 7.93 ? 108 ARG A CB 1 ATOM 814 C CG . ARG A 1 108 ? 13.222 5.105 9.234 1.00 9.14 ? 108 ARG A CG 1 ATOM 815 C CD . ARG A 1 108 ? 12.321 3.897 9.453 1.00 9.69 ? 108 ARG A CD 1 ATOM 816 N NE . ARG A 1 108 ? 10.906 4.259 9.377 1.00 9.49 ? 108 ARG A NE 1 ATOM 817 C CZ . ARG A 1 108 ? 10.073 4.362 10.408 1.00 9.79 ? 108 ARG A CZ 1 ATOM 818 N NH1 . ARG A 1 108 ? 10.439 4.106 11.657 1.00 10.63 ? 108 ARG A NH1 1 ATOM 819 N NH2 . ARG A 1 108 ? 8.825 4.706 10.169 1.00 9.38 ? 108 ARG A NH2 1 ATOM 820 N N . VAL A 1 109 ? 14.853 7.800 7.883 1.00 7.26 ? 109 VAL A N 1 ATOM 821 C CA . VAL A 1 109 ? 14.762 8.529 6.628 1.00 7.31 ? 109 VAL A CA 1 ATOM 822 C C . VAL A 1 109 ? 14.777 7.618 5.432 1.00 7.25 ? 109 VAL A C 1 ATOM 823 O O . VAL A 1 109 ? 15.276 6.497 5.521 1.00 7.95 ? 109 VAL A O 1 ATOM 824 C CB . VAL A 1 109 ? 15.910 9.592 6.471 1.00 7.72 ? 109 VAL A CB 1 ATOM 825 C CG1 . VAL A 1 109 ? 15.846 10.606 7.610 1.00 9.21 ? 109 VAL A CG1 1 ATOM 826 C CG2 . VAL A 1 109 ? 17.302 8.958 6.402 1.00 7.77 ? 109 VAL A CG2 1 ATOM 827 N N . TYR A 1 110 ? 14.248 8.125 4.318 1.00 7.47 ? 110 TYR A N 1 ATOM 828 C CA . TYR A 1 110 ? 14.275 7.430 3.011 1.00 7.04 ? 110 TYR A CA 1 ATOM 829 C C . TYR A 1 110 ? 14.981 8.276 1.972 1.00 7.30 ? 110 TYR A C 1 ATOM 830 O O . TYR A 1 110 ? 15.035 9.516 2.073 1.00 8.21 ? 110 TYR A O 1 ATOM 831 C CB . TYR A 1 110 ? 12.847 7.045 2.508 1.00 7.40 ? 110 TYR A CB 1 ATOM 832 C CG . TYR A 1 110 ? 11.982 6.558 3.632 1.00 6.71 ? 110 TYR A CG 1 ATOM 833 C CD1 . TYR A 1 110 ? 12.364 5.476 4.394 1.00 7.27 ? 110 TYR A CD1 1 ATOM 834 C CD2 . TYR A 1 110 ? 10.827 7.232 4.001 1.00 7.63 ? 110 TYR A CD2 1 ATOM 835 C CE1 . TYR A 1 110 ? 11.642 5.091 5.497 1.00 8.31 ? 110 TYR A CE1 1 ATOM 836 C CE2 . TYR A 1 110 ? 10.074 6.826 5.082 1.00 8.30 ? 110 TYR A CE2 1 ATOM 837 C CZ . TYR A 1 110 ? 10.504 5.780 5.845 1.00 7.77 ? 110 TYR A CZ 1 ATOM 838 O OH . TYR A 1 110 ? 9.823 5.420 6.983 1.00 8.29 ? 110 TYR A OH 1 ATOM 839 N N . LEU A 1 111 ? 15.491 7.609 0.943 1.00 7.52 ? 111 LEU A N 1 ATOM 840 C CA . LEU A 1 111 ? 16.180 8.284 -0.134 1.00 7.87 ? 111 LEU A CA 1 ATOM 841 C C . LEU A 1 111 ? 15.183 8.593 -1.270 1.00 8.36 ? 111 LEU A C 1 ATOM 842 O O . LEU A 1 111 ? 14.602 7.705 -1.881 1.00 8.87 ? 111 LEU A O 1 ATOM 843 C CB . LEU A 1 111 ? 17.329 7.418 -0.642 1.00 8.66 ? 111 LEU A CB 1 ATOM 844 C CG . LEU A 1 111 ? 18.323 8.148 -1.549 1.00 8.74 ? 111 LEU A CG 1 ATOM 845 C CD1 . LEU A 1 111 ? 19.191 9.052 -0.728 1.00 8.92 ? 111 LEU A CD1 1 ATOM 846 C CD2 . LEU A 1 111 ? 19.171 7.146 -2.298 1.00 10.01 ? 111 LEU A CD2 1 ATOM 847 N N . LEU A 1 112 ? 15.019 9.885 -1.555 1.00 8.48 ? 112 LEU A N 1 ATOM 848 C CA . LEU A 1 112 ? 14.209 10.377 -2.665 1.00 9.03 ? 112 LEU A CA 1 ATOM 849 C C . LEU A 1 112 ? 15.046 10.541 -3.903 1.00 9.90 ? 112 LEU A C 1 ATOM 850 O O . LEU A 1 112 ? 16.238 10.850 -3.805 1.00 9.43 ? 112 LEU A O 1 ATOM 851 C CB . LEU A 1 112 ? 13.596 11.728 -2.317 1.00 9.13 ? 112 LEU A CB 1 ATOM 852 C CG . LEU A 1 112 ? 12.483 11.736 -1.301 1.00 9.63 ? 112 LEU A CG 1 ATOM 853 C CD1 . LEU A 1 112 ? 12.172 13.146 -0.843 1.00 10.19 ? 112 LEU A CD1 1 ATOM 854 C CD2 . LEU A 1 112 ? 11.225 11.095 -1.857 1.00 9.86 ? 112 LEU A CD2 1 ATOM 855 N N . ASP A 1 113 ? 14.396 10.424 -5.060 1.00 9.33 ? 113 ASP A N 1 ATOM 856 C CA . ASP A 1 113 ? 15.053 10.743 -6.317 1.00 10.18 ? 113 ASP A CA 1 ATOM 857 C C . ASP A 1 113 ? 15.166 12.263 -6.471 1.00 11.30 ? 113 ASP A C 1 ATOM 858 O O . ASP A 1 113 ? 14.747 13.060 -5.590 1.00 10.63 ? 113 ASP A O 1 ATOM 859 C CB . ASP A 1 113 ? 14.400 10.022 -7.513 1.00 10.99 ? 113 ASP A CB 1 ATOM 860 C CG . ASP A 1 113 ? 13.142 10.667 -8.042 1.00 11.72 ? 113 ASP A CG 1 ATOM 861 O OD1 . ASP A 1 113 ? 12.809 11.811 -7.676 1.00 10.98 ? 113 ASP A OD1 1 ATOM 862 O OD2 . ASP A 1 113 ? 12.439 10.005 -8.869 1.00 13.52 ? 113 ASP A OD2 1 ATOM 863 N N . LYS A 1 114 ? 15.818 12.680 -7.552 1.00 11.86 ? 114 LYS A N 1 ATOM 864 C CA . LYS A 1 114 ? 16.138 14.084 -7.748 1.00 14.31 ? 114 LYS A CA 1 ATOM 865 C C . LYS A 1 114 ? 14.926 15.011 -7.884 1.00 14.25 ? 114 LYS A C 1 ATOM 866 O O . LYS A 1 114 ? 15.079 16.239 -7.792 1.00 15.73 ? 114 LYS A O 1 ATOM 867 C CB . LYS A 1 114 ? 17.057 14.244 -8.968 1.00 15.66 ? 114 LYS A CB 1 ATOM 868 C CG . LYS A 1 114 ? 16.464 13.872 -10.313 1.00 18.28 ? 114 LYS A CG 1 ATOM 869 C CD . LYS A 1 114 ? 17.564 13.854 -11.427 1.00 19.32 ? 114 LYS A CD 1 ATOM 870 C CE . LYS A 1 114 ? 16.990 13.411 -12.732 1.00 23.24 ? 114 LYS A CE 1 ATOM 871 N NZ . LYS A 1 114 ? 17.954 13.687 -13.852 1.00 24.36 ? 114 LYS A NZ 1 ATOM 872 N N . THR A 1 115 ? 13.751 14.440 -8.116 1.00 12.92 ? 115 THR A N 1 ATOM 873 C CA . THR A 1 115 ? 12.517 15.232 -8.225 1.00 12.98 ? 115 THR A CA 1 ATOM 874 C C . THR A 1 115 ? 11.844 15.504 -6.897 1.00 12.04 ? 115 THR A C 1 ATOM 875 O O . THR A 1 115 ? 10.937 16.326 -6.832 1.00 12.56 ? 115 THR A O 1 ATOM 876 C CB . THR A 1 115 ? 11.490 14.557 -9.121 1.00 13.47 ? 115 THR A CB 1 ATOM 877 O OG1 . THR A 1 115 ? 10.868 13.428 -8.436 1.00 13.03 ? 115 THR A OG1 1 ATOM 878 C CG2 . THR A 1 115 ? 12.107 14.064 -10.450 1.00 15.60 ? 115 THR A CG2 1 ATOM 879 N N . LYS A 1 116 ? 12.269 14.787 -5.856 1.00 10.70 ? 116 LYS A N 1 ATOM 880 C CA . LYS A 1 116 ? 11.665 14.832 -4.506 1.00 11.10 ? 116 LYS A CA 1 ATOM 881 C C . LYS A 1 116 ? 10.264 14.214 -4.439 1.00 10.84 ? 116 LYS A C 1 ATOM 882 O O . LYS A 1 116 ? 9.668 14.181 -3.348 1.00 12.30 ? 116 LYS A O 1 ATOM 883 C CB . LYS A 1 116 ? 11.601 16.252 -3.895 1.00 11.05 ? 116 LYS A CB 1 ATOM 884 C CG . LYS A 1 116 ? 12.941 16.959 -3.785 1.00 12.16 ? 116 LYS A CG 1 ATOM 885 C CD . LYS A 1 116 ? 12.742 18.426 -3.369 1.00 12.51 ? 116 LYS A CD 1 ATOM 886 C CE . LYS A 1 116 ? 14.039 19.105 -3.071 1.00 13.82 ? 116 LYS A CE 1 ATOM 887 N NZ . LYS A 1 116 ? 13.816 20.551 -2.659 1.00 14.25 ? 116 LYS A NZ 1 ATOM 888 N N . ARG A 1 117 ? 9.754 13.670 -5.535 1.00 12.30 ? 117 ARG A N 1 ATOM 889 C CA . ARG A 1 117 ? 8.365 13.168 -5.527 1.00 13.06 ? 117 ARG A CA 1 ATOM 890 C C . ARG A 1 117 ? 8.220 11.683 -5.777 1.00 11.21 ? 117 ARG A C 1 ATOM 891 O O . ARG A 1 117 ? 7.111 11.171 -5.811 1.00 12.49 ? 117 ARG A O 1 ATOM 892 C CB . ARG A 1 117 ? 7.474 13.982 -6.457 1.00 15.18 ? 117 ARG A CB 1 ATOM 893 C CG . ARG A 1 117 ? 7.200 15.384 -5.874 1.00 19.62 ? 117 ARG A CG 1 ATOM 894 C CD . ARG A 1 117 ? 7.182 16.496 -6.854 1.00 22.77 ? 117 ARG A CD 1 ATOM 895 N NE . ARG A 1 117 ? 6.882 17.788 -6.214 1.00 24.59 ? 117 ARG A NE 1 ATOM 896 C CZ . ARG A 1 117 ? 7.775 18.736 -5.921 1.00 27.75 ? 117 ARG A CZ 1 ATOM 897 N NH1 . ARG A 1 117 ? 9.077 18.570 -6.168 1.00 26.93 ? 117 ARG A NH1 1 ATOM 898 N NH2 . ARG A 1 117 ? 7.361 19.874 -5.366 1.00 27.55 ? 117 ARG A NH2 1 ATOM 899 N N . ARG A 1 118 ? 9.347 10.999 -5.873 1.00 11.23 ? 118 ARG A N 1 ATOM 900 C CA . ARG A 1 118 ? 9.367 9.551 -5.987 1.00 10.84 ? 118 ARG A CA 1 ATOM 901 C C . ARG A 1 118 ? 10.595 9.064 -5.232 1.00 9.32 ? 118 ARG A C 1 ATOM 902 O O . ARG A 1 118 ? 11.651 9.692 -5.306 1.00 9.37 ? 118 ARG A O 1 ATOM 903 C CB A ARG A 1 118 ? 9.454 9.166 -7.460 0.50 10.88 ? 118 ARG A CB 1 ATOM 904 C CB B ARG A 1 118 ? 9.483 9.185 -7.470 0.50 11.30 ? 118 ARG A CB 1 ATOM 905 C CG A ARG A 1 118 ? 9.520 7.705 -7.770 0.50 12.36 ? 118 ARG A CG 1 ATOM 906 C CG B ARG A 1 118 ? 8.975 7.843 -7.893 0.50 13.69 ? 118 ARG A CG 1 ATOM 907 C CD A ARG A 1 118 ? 9.557 7.443 -9.277 0.50 12.61 ? 118 ARG A CD 1 ATOM 908 C CD B ARG A 1 118 ? 8.712 7.772 -9.401 0.50 15.52 ? 118 ARG A CD 1 ATOM 909 N NE A ARG A 1 118 ? 9.064 6.119 -9.603 0.50 14.58 ? 118 ARG A NE 1 ATOM 910 N NE B ARG A 1 118 ? 7.974 6.581 -9.704 0.50 18.89 ? 118 ARG A NE 1 ATOM 911 C CZ A ARG A 1 118 ? 9.801 5.077 -9.955 0.50 14.57 ? 118 ARG A CZ 1 ATOM 912 C CZ B ARG A 1 118 ? 6.710 6.519 -10.057 0.50 16.11 ? 118 ARG A CZ 1 ATOM 913 N NH1 A ARG A 1 118 ? 11.125 5.138 -10.063 0.50 17.35 ? 118 ARG A NH1 1 ATOM 914 N NH1 B ARG A 1 118 ? 5.972 7.612 -10.279 0.50 13.69 ? 118 ARG A NH1 1 ATOM 915 N NH2 A ARG A 1 118 ? 9.183 3.942 -10.203 0.50 11.09 ? 118 ARG A NH2 1 ATOM 916 N NH2 B ARG A 1 118 ? 6.199 5.334 -10.274 0.50 18.12 ? 118 ARG A NH2 1 ATOM 917 N N . TYR A 1 119 ? 10.477 7.963 -4.504 1.00 8.87 ? 119 TYR A N 1 ATOM 918 C CA . TYR A 1 119 ? 11.651 7.358 -3.903 1.00 8.58 ? 119 TYR A CA 1 ATOM 919 C C . TYR A 1 119 ? 12.617 6.886 -4.977 1.00 8.77 ? 119 TYR A C 1 ATOM 920 O O . TYR A 1 119 ? 12.203 6.511 -6.083 1.00 9.89 ? 119 TYR A O 1 ATOM 921 C CB . TYR A 1 119 ? 11.268 6.169 -2.984 1.00 8.30 ? 119 TYR A CB 1 ATOM 922 C CG . TYR A 1 119 ? 10.417 6.583 -1.810 1.00 7.37 ? 119 TYR A CG 1 ATOM 923 C CD1 . TYR A 1 119 ? 10.900 7.460 -0.867 1.00 8.61 ? 119 TYR A CD1 1 ATOM 924 C CD2 . TYR A 1 119 ? 9.144 6.074 -1.635 1.00 8.07 ? 119 TYR A CD2 1 ATOM 925 C CE1 . TYR A 1 119 ? 10.135 7.856 0.201 1.00 8.21 ? 119 TYR A CE1 1 ATOM 926 C CE2 . TYR A 1 119 ? 8.364 6.457 -0.564 1.00 7.68 ? 119 TYR A CE2 1 ATOM 927 C CZ . TYR A 1 119 ? 8.860 7.354 0.361 1.00 7.38 ? 119 TYR A CZ 1 ATOM 928 O OH . TYR A 1 119 ? 8.102 7.791 1.440 1.00 9.22 ? 119 TYR A OH 1 ATOM 929 N N . GLU A 1 120 ? 13.910 6.923 -4.661 1.00 8.99 ? 120 GLU A N 1 ATOM 930 C CA . GLU A 1 120 ? 14.904 6.349 -5.549 1.00 9.51 ? 120 GLU A CA 1 ATOM 931 C C . GLU A 1 120 ? 14.750 4.855 -5.480 1.00 10.02 ? 120 GLU A C 1 ATOM 932 O O . GLU A 1 120 ? 14.967 4.271 -4.444 1.00 13.08 ? 120 GLU A O 1 ATOM 933 C CB . GLU A 1 120 ? 16.299 6.769 -5.104 1.00 10.12 ? 120 GLU A CB 1 ATOM 934 C CG . GLU A 1 120 ? 17.417 6.293 -6.009 1.00 11.01 ? 120 GLU A CG 1 ATOM 935 C CD . GLU A 1 120 ? 17.443 6.985 -7.342 1.00 13.56 ? 120 GLU A CD 1 ATOM 936 O OE1 . GLU A 1 120 ? 17.414 8.227 -7.435 1.00 12.94 ? 120 GLU A OE1 1 ATOM 937 O OE2 . GLU A 1 120 ? 17.537 6.268 -8.357 1.00 19.34 ? 120 GLU A OE2 1 ATOM 938 N N . MET A 1 121 ? 14.329 4.217 -6.551 1.00 9.87 ? 121 MET A N 1 ATOM 939 C CA . MET A 1 121 ? 14.092 2.781 -6.504 1.00 9.67 ? 121 MET A CA 1 ATOM 940 C C . MET A 1 121 ? 15.380 2.063 -6.871 1.00 10.52 ? 121 MET A C 1 ATOM 941 O O . MET A 1 121 ? 15.939 2.267 -7.950 1.00 11.66 ? 121 MET A O 1 ATOM 942 C CB . MET A 1 121 ? 12.933 2.364 -7.434 1.00 10.55 ? 121 MET A CB 1 ATOM 943 C CG . MET A 1 121 ? 11.637 3.088 -7.142 1.00 10.24 ? 121 MET A CG 1 ATOM 944 S SD . MET A 1 121 ? 11.032 2.946 -5.399 1.00 10.72 ? 121 MET A SD 1 ATOM 945 C CE . MET A 1 121 ? 10.699 1.218 -5.269 1.00 9.95 ? 121 MET A CE 1 ATOM 946 N N . LEU A 1 122 ? 15.811 1.198 -5.968 1.00 9.39 ? 122 LEU A N 1 ATOM 947 C CA . LEU A 1 122 ? 17.007 0.406 -6.183 1.00 9.73 ? 122 LEU A CA 1 ATOM 948 C C . LEU A 1 122 ? 16.612 -1.011 -6.606 1.00 9.78 ? 122 LEU A C 1 ATOM 949 O O . LEU A 1 122 ? 15.699 -1.599 -6.024 1.00 9.38 ? 122 LEU A O 1 ATOM 950 C CB . LEU A 1 122 ? 17.847 0.334 -4.927 1.00 9.96 ? 122 LEU A CB 1 ATOM 951 C CG . LEU A 1 122 ? 18.477 1.653 -4.477 1.00 11.67 ? 122 LEU A CG 1 ATOM 952 C CD1 . LEU A 1 122 ? 17.504 2.400 -3.623 1.00 13.89 ? 122 LEU A CD1 1 ATOM 953 C CD2 . LEU A 1 122 ? 19.783 1.460 -3.720 1.00 12.70 ? 122 LEU A CD2 1 ATOM 954 N N . HIS A 1 123 ? 17.326 -1.538 -7.609 1.00 9.76 ? 123 HIS A N 1 ATOM 955 C CA . HIS A 1 123 ? 17.071 -2.864 -8.175 1.00 10.04 ? 123 HIS A CA 1 ATOM 956 C C . HIS A 1 123 ? 18.384 -3.635 -8.104 1.00 10.05 ? 123 HIS A C 1 ATOM 957 O O . HIS A 1 123 ? 19.188 -3.588 -9.039 1.00 12.75 ? 123 HIS A O 1 ATOM 958 C CB . HIS A 1 123 ? 16.546 -2.758 -9.611 1.00 10.16 ? 123 HIS A CB 1 ATOM 959 C CG . HIS A 1 123 ? 15.320 -1.915 -9.753 1.00 10.67 ? 123 HIS A CG 1 ATOM 960 N ND1 . HIS A 1 123 ? 14.057 -2.455 -9.846 1.00 11.79 ? 123 HIS A ND1 1 ATOM 961 C CD2 . HIS A 1 123 ? 15.164 -0.573 -9.903 1.00 13.01 ? 123 HIS A CD2 1 ATOM 962 C CE1 . HIS A 1 123 ? 13.178 -1.481 -10.027 1.00 12.37 ? 123 HIS A CE1 1 ATOM 963 N NE2 . HIS A 1 123 ? 13.820 -0.330 -10.029 1.00 14.89 ? 123 HIS A NE2 1 ATOM 964 N N . LEU A 1 124 ? 18.625 -4.331 -6.989 1.00 10.36 ? 124 LEU A N 1 ATOM 965 C CA . LEU A 1 124 ? 19.977 -4.769 -6.633 1.00 10.28 ? 124 LEU A CA 1 ATOM 966 C C . LEU A 1 124 ? 20.355 -6.204 -6.965 1.00 9.83 ? 124 LEU A C 1 ATOM 967 O O . LEU A 1 124 ? 21.525 -6.541 -6.890 1.00 9.45 ? 124 LEU A O 1 ATOM 968 C CB . LEU A 1 124 ? 20.253 -4.493 -5.165 1.00 10.97 ? 124 LEU A CB 1 ATOM 969 C CG . LEU A 1 124 ? 20.361 -2.994 -4.855 1.00 12.15 ? 124 LEU A CG 1 ATOM 970 C CD1 . LEU A 1 124 ? 20.529 -2.819 -3.359 1.00 13.83 ? 124 LEU A CD1 1 ATOM 971 C CD2 . LEU A 1 124 ? 21.468 -2.273 -5.604 1.00 13.39 ? 124 LEU A CD2 1 ATOM 972 N N . THR A 1 125 ? 19.413 -7.041 -7.396 1.00 10.04 ? 125 THR A N 1 ATOM 973 C CA . THR A 1 125 ? 19.754 -8.420 -7.771 1.00 10.02 ? 125 THR A CA 1 ATOM 974 C C . THR A 1 125 ? 20.709 -8.375 -8.959 1.00 9.91 ? 125 THR A C 1 ATOM 975 O O . THR A 1 125 ? 20.384 -7.782 -9.998 1.00 11.50 ? 125 THR A O 1 ATOM 976 C CB . THR A 1 125 ? 18.505 -9.177 -8.137 1.00 10.46 ? 125 THR A CB 1 ATOM 977 O OG1 . THR A 1 125 ? 17.647 -9.209 -7.007 1.00 12.40 ? 125 THR A OG1 1 ATOM 978 C CG2 . THR A 1 125 ? 18.782 -10.626 -8.485 1.00 11.72 ? 125 THR A CG2 1 ATOM 979 N N . GLY A 1 126 ? 21.887 -8.984 -8.791 1.00 9.61 ? 126 GLY A N 1 ATOM 980 C CA . GLY A 1 126 ? 22.962 -8.983 -9.797 1.00 10.65 ? 126 GLY A CA 1 ATOM 981 C C . GLY A 1 126 ? 23.861 -7.770 -9.732 1.00 11.17 ? 126 GLY A C 1 ATOM 982 O O . GLY A 1 126 ? 24.686 -7.575 -10.627 1.00 12.00 ? 126 GLY A O 1 ATOM 983 N N . PHE A 1 127 ? 23.745 -6.966 -8.672 1.00 10.21 ? 127 PHE A N 1 ATOM 984 C CA . PHE A 1 127 ? 24.518 -5.731 -8.486 1.00 10.75 ? 127 PHE A CA 1 ATOM 985 C C . PHE A 1 127 ? 25.062 -5.679 -7.065 1.00 10.26 ? 127 PHE A C 1 ATOM 986 O O . PHE A 1 127 ? 24.868 -6.595 -6.283 1.00 9.70 ? 127 PHE A O 1 ATOM 987 C CB . PHE A 1 127 ? 23.634 -4.521 -8.811 1.00 11.29 ? 127 PHE A CB 1 ATOM 988 C CG . PHE A 1 127 ? 23.163 -4.509 -10.250 1.00 11.70 ? 127 PHE A CG 1 ATOM 989 C CD1 . PHE A 1 127 ? 23.989 -4.065 -11.278 1.00 13.33 ? 127 PHE A CD1 1 ATOM 990 C CD2 . PHE A 1 127 ? 21.927 -4.989 -10.583 1.00 12.54 ? 127 PHE A CD2 1 ATOM 991 C CE1 . PHE A 1 127 ? 23.563 -4.116 -12.594 1.00 14.72 ? 127 PHE A CE1 1 ATOM 992 C CE2 . PHE A 1 127 ? 21.493 -5.017 -11.915 1.00 14.31 ? 127 PHE A CE2 1 ATOM 993 C CZ . PHE A 1 127 ? 22.293 -4.578 -12.902 1.00 14.62 ? 127 PHE A CZ 1 ATOM 994 N N . GLU A 1 128 ? 25.743 -4.584 -6.737 1.00 10.36 ? 128 GLU A N 1 ATOM 995 C CA . GLU A 1 128 ? 26.274 -4.396 -5.407 1.00 11.02 ? 128 GLU A CA 1 ATOM 996 C C . GLU A 1 128 ? 25.993 -2.994 -4.901 1.00 10.23 ? 128 GLU A C 1 ATOM 997 O O . GLU A 1 128 ? 25.816 -2.056 -5.686 1.00 10.68 ? 128 GLU A O 1 ATOM 998 C CB . GLU A 1 128 ? 27.750 -4.753 -5.338 1.00 13.41 ? 128 GLU A CB 1 ATOM 999 C CG . GLU A 1 128 ? 28.681 -3.735 -5.923 1.00 13.88 ? 128 GLU A CG 1 ATOM 1000 C CD . GLU A 1 128 ? 30.142 -4.171 -6.028 1.00 13.00 ? 128 GLU A CD 1 ATOM 1001 O OE1 . GLU A 1 128 ? 30.414 -5.377 -6.066 1.00 13.39 ? 128 GLU A OE1 1 ATOM 1002 O OE2 . GLU A 1 128 ? 31.027 -3.284 -6.136 1.00 12.14 ? 128 GLU A OE2 1 ATOM 1003 N N . PHE A 1 129 ? 25.859 -2.909 -3.579 1.00 9.73 ? 129 PHE A N 1 ATOM 1004 C CA . PHE A 1 129 ? 25.608 -1.663 -2.857 1.00 9.90 ? 129 PHE A CA 1 ATOM 1005 C C . PHE A 1 129 ? 26.681 -1.501 -1.811 1.00 9.52 ? 129 PHE A C 1 ATOM 1006 O O . PHE A 1 129 ? 26.938 -2.431 -1.052 1.00 9.98 ? 129 PHE A O 1 ATOM 1007 C CB . PHE A 1 129 ? 24.227 -1.699 -2.172 1.00 10.27 ? 129 PHE A CB 1 ATOM 1008 C CG . PHE A 1 129 ? 23.844 -0.410 -1.486 1.00 9.38 ? 129 PHE A CG 1 ATOM 1009 C CD1 . PHE A 1 129 ? 24.306 -0.119 -0.212 1.00 9.68 ? 129 PHE A CD1 1 ATOM 1010 C CD2 . PHE A 1 129 ? 23.050 0.523 -2.112 1.00 9.96 ? 129 PHE A CD2 1 ATOM 1011 C CE1 . PHE A 1 129 ? 23.988 1.072 0.400 1.00 11.10 ? 129 PHE A CE1 1 ATOM 1012 C CE2 . PHE A 1 129 ? 22.713 1.725 -1.497 1.00 10.54 ? 129 PHE A CE2 1 ATOM 1013 C CZ . PHE A 1 129 ? 23.195 1.994 -0.235 1.00 10.42 ? 129 PHE A CZ 1 ATOM 1014 N N . THR A 1 130 ? 27.264 -0.308 -1.747 1.00 10.18 ? 130 THR A N 1 ATOM 1015 C CA . THR A 1 130 ? 28.417 -0.021 -0.891 1.00 9.99 ? 130 THR A CA 1 ATOM 1016 C C . THR A 1 130 ? 28.250 1.329 -0.217 1.00 9.71 ? 130 THR A C 1 ATOM 1017 O O . THR A 1 130 ? 27.638 2.240 -0.756 1.00 10.13 ? 130 THR A O 1 ATOM 1018 C CB . THR A 1 130 ? 29.670 -0.048 -1.778 1.00 10.95 ? 130 THR A CB 1 ATOM 1019 O OG1 . THR A 1 130 ? 29.836 -1.415 -2.199 1.00 10.71 ? 130 THR A OG1 1 ATOM 1020 C CG2 . THR A 1 130 ? 30.940 0.327 -1.005 1.00 10.89 ? 130 THR A CG2 1 ATOM 1021 N N . PHE A 1 131 ? 28.786 1.430 0.986 1.00 9.11 ? 131 PHE A N 1 ATOM 1022 C CA . PHE A 1 131 ? 28.792 2.697 1.703 1.00 9.36 ? 131 PHE A CA 1 ATOM 1023 C C . PHE A 1 131 ? 29.951 2.731 2.658 1.00 9.21 ? 131 PHE A C 1 ATOM 1024 O O . PHE A 1 131 ? 30.485 1.695 3.020 1.00 9.62 ? 131 PHE A O 1 ATOM 1025 C CB . PHE A 1 131 ? 27.458 2.948 2.439 1.00 9.42 ? 131 PHE A CB 1 ATOM 1026 C CG . PHE A 1 131 ? 27.141 1.952 3.515 1.00 8.53 ? 131 PHE A CG 1 ATOM 1027 C CD1 . PHE A 1 131 ? 26.597 0.707 3.208 1.00 8.55 ? 131 PHE A CD1 1 ATOM 1028 C CD2 . PHE A 1 131 ? 27.377 2.252 4.861 1.00 9.58 ? 131 PHE A CD2 1 ATOM 1029 C CE1 . PHE A 1 131 ? 26.297 -0.182 4.203 1.00 9.07 ? 131 PHE A CE1 1 ATOM 1030 C CE2 . PHE A 1 131 ? 27.090 1.330 5.848 1.00 9.56 ? 131 PHE A CE2 1 ATOM 1031 C CZ . PHE A 1 131 ? 26.556 0.113 5.506 1.00 9.39 ? 131 PHE A CZ 1 ATOM 1032 N N . ASP A 1 132 ? 30.319 3.947 3.067 1.00 9.60 ? 132 ASP A N 1 ATOM 1033 C CA . ASP A 1 132 ? 31.306 4.165 4.119 1.00 10.10 ? 132 ASP A CA 1 ATOM 1034 C C . ASP A 1 132 ? 30.584 4.539 5.405 1.00 9.61 ? 132 ASP A C 1 ATOM 1035 O O . ASP A 1 132 ? 29.497 5.134 5.351 1.00 9.78 ? 132 ASP A O 1 ATOM 1036 C CB . ASP A 1 132 ? 32.292 5.277 3.743 1.00 9.63 ? 132 ASP A CB 1 ATOM 1037 C CG . ASP A 1 132 ? 32.958 5.083 2.413 1.00 12.40 ? 132 ASP A CG 1 ATOM 1038 O OD1 . ASP A 1 132 ? 33.069 3.961 1.883 1.00 12.93 ? 132 ASP A OD1 1 ATOM 1039 O OD2 . ASP A 1 132 ? 33.421 6.076 1.838 1.00 14.11 ? 132 ASP A OD2 1 ATOM 1040 N N . VAL A 1 133 ? 31.135 4.155 6.548 1.00 9.83 ? 133 VAL A N 1 ATOM 1041 C CA . VAL A 1 133 ? 30.451 4.403 7.797 1.00 9.84 ? 133 VAL A CA 1 ATOM 1042 C C . VAL A 1 133 ? 31.431 4.753 8.919 1.00 10.11 ? 133 VAL A C 1 ATOM 1043 O O . VAL A 1 133 ? 32.585 4.292 8.936 1.00 11.30 ? 133 VAL A O 1 ATOM 1044 C CB . VAL A 1 133 ? 29.576 3.171 8.205 1.00 10.06 ? 133 VAL A CB 1 ATOM 1045 C CG1 . VAL A 1 133 ? 30.412 1.940 8.532 1.00 10.22 ? 133 VAL A CG1 1 ATOM 1046 C CG2 . VAL A 1 133 ? 28.642 3.504 9.351 1.00 10.56 ? 133 VAL A CG2 1 ATOM 1047 N N . ASP A 1 134 ? 30.969 5.598 9.841 1.00 11.43 ? 134 ASP A N 1 ATOM 1048 C CA . ASP A 1 134 ? 31.658 5.858 11.101 1.00 11.91 ? 134 ASP A CA 1 ATOM 1049 C C . ASP A 1 134 ? 30.712 5.358 12.192 1.00 10.96 ? 134 ASP A C 1 ATOM 1050 O O . ASP A 1 134 ? 29.663 5.961 12.436 1.00 10.65 ? 134 ASP A O 1 ATOM 1051 C CB . ASP A 1 134 ? 31.959 7.340 11.234 1.00 12.49 ? 134 ASP A CB 1 ATOM 1052 C CG . ASP A 1 134 ? 32.653 7.687 12.522 1.00 14.42 ? 134 ASP A CG 1 ATOM 1053 O OD1 . ASP A 1 134 ? 32.589 6.909 13.512 1.00 14.38 ? 134 ASP A OD1 1 ATOM 1054 O OD2 . ASP A 1 134 ? 33.278 8.777 12.633 1.00 21.76 ? 134 ASP A OD2 1 ATOM 1055 N N . ALA A 1 135 ? 31.086 4.245 12.826 1.00 10.57 ? 135 ALA A N 1 ATOM 1056 C CA . ALA A 1 135 ? 30.281 3.563 13.841 1.00 10.92 ? 135 ALA A CA 1 ATOM 1057 C C . ALA A 1 135 ? 30.818 3.774 15.260 1.00 10.64 ? 135 ALA A C 1 ATOM 1058 O O . ALA A 1 135 ? 30.339 3.172 16.210 1.00 10.75 ? 135 ALA A O 1 ATOM 1059 C CB . ALA A 1 135 ? 30.213 2.066 13.538 1.00 11.43 ? 135 ALA A CB 1 ATOM 1060 N N . THR A 1 136 ? 31.790 4.676 15.419 1.00 11.31 ? 136 THR A N 1 ATOM 1061 C CA . THR A 1 136 ? 32.481 4.835 16.715 1.00 12.50 ? 136 THR A CA 1 ATOM 1062 C C . THR A 1 136 ? 31.558 5.179 17.886 1.00 12.00 ? 136 THR A C 1 ATOM 1063 O O . THR A 1 136 ? 31.792 4.731 19.016 1.00 12.98 ? 136 THR A O 1 ATOM 1064 C CB . THR A 1 136 ? 33.597 5.909 16.619 1.00 13.28 ? 136 THR A CB 1 ATOM 1065 O OG1 . THR A 1 136 ? 33.074 7.183 16.177 1.00 15.78 ? 136 THR A OG1 1 ATOM 1066 C CG2 . THR A 1 136 ? 34.671 5.519 15.609 1.00 14.95 ? 136 THR A CG2 1 ATOM 1067 N N . LYS A 1 137 ? 30.529 5.981 17.623 1.00 12.07 ? 137 LYS A N 1 ATOM 1068 C CA . LYS A 1 137 ? 29.623 6.431 18.668 1.00 12.16 ? 137 LYS A CA 1 ATOM 1069 C C . LYS A 1 137 ? 28.366 5.577 18.815 1.00 10.36 ? 137 LYS A C 1 ATOM 1070 O O . LYS A 1 137 ? 27.334 6.043 19.258 1.00 11.15 ? 137 LYS A O 1 ATOM 1071 C CB . LYS A 1 137 ? 29.297 7.904 18.458 1.00 12.13 ? 137 LYS A CB 1 ATOM 1072 C CG . LYS A 1 137 ? 30.535 8.801 18.639 1.00 15.46 ? 137 LYS A CG 1 ATOM 1073 C CD . LYS A 1 137 ? 30.247 10.250 18.406 1.00 16.97 ? 137 LYS A CD 1 ATOM 1074 C CE . LYS A 1 137 ? 29.464 10.843 19.548 1.00 20.17 ? 137 LYS A CE 1 ATOM 1075 N NZ . LYS A 1 137 ? 29.088 12.282 19.327 1.00 22.67 ? 137 LYS A NZ 1 ATOM 1076 N N . LEU A 1 138 ? 28.502 4.290 18.505 1.00 10.90 ? 138 LEU A N 1 ATOM 1077 C CA . LEU A 1 138 ? 27.414 3.335 18.625 1.00 10.35 ? 138 LEU A CA 1 ATOM 1078 C C . LEU A 1 138 ? 27.837 2.225 19.608 1.00 10.29 ? 138 LEU A C 1 ATOM 1079 O O . LEU A 1 138 ? 28.489 1.259 19.214 1.00 10.88 ? 138 LEU A O 1 ATOM 1080 C CB . LEU A 1 138 ? 27.105 2.725 17.254 1.00 9.76 ? 138 LEU A CB 1 ATOM 1081 C CG . LEU A 1 138 ? 26.643 3.717 16.196 1.00 10.23 ? 138 LEU A CG 1 ATOM 1082 C CD1 . LEU A 1 138 ? 26.481 3.024 14.870 1.00 10.66 ? 138 LEU A CD1 1 ATOM 1083 C CD2 . LEU A 1 138 ? 25.276 4.313 16.552 1.00 11.33 ? 138 LEU A CD2 1 ATOM 1084 N N . PRO A 1 139 ? 27.487 2.358 20.880 1.00 10.56 ? 139 PRO A N 1 ATOM 1085 C CA . PRO A 1 139 ? 27.781 1.301 21.844 1.00 10.85 ? 139 PRO A CA 1 ATOM 1086 C C . PRO A 1 139 ? 26.790 0.168 21.795 1.00 11.15 ? 139 PRO A C 1 ATOM 1087 O O . PRO A 1 139 ? 25.785 0.227 21.060 1.00 11.87 ? 139 PRO A O 1 ATOM 1088 C CB . PRO A 1 139 ? 27.700 2.033 23.189 1.00 11.91 ? 139 PRO A CB 1 ATOM 1089 C CG . PRO A 1 139 ? 26.630 3.062 22.949 1.00 11.79 ? 139 PRO A CG 1 ATOM 1090 C CD . PRO A 1 139 ? 26.874 3.534 21.538 1.00 11.35 ? 139 PRO A CD 1 ATOM 1091 N N . CYS A 1 140 ? 27.044 -0.842 22.621 1.00 10.80 ? 140 CYS A N 1 ATOM 1092 C CA . CYS A 1 140 ? 26.078 -1.910 22.874 1.00 11.00 ? 140 CYS A CA 1 ATOM 1093 C C . CYS A 1 140 ? 24.662 -1.388 22.979 1.00 11.20 ? 140 CYS A C 1 ATOM 1094 O O . CYS A 1 140 ? 24.422 -0.375 23.638 1.00 11.83 ? 140 CYS A O 1 ATOM 1095 C CB . CYS A 1 140 ? 26.383 -2.574 24.219 1.00 11.97 ? 140 CYS A CB 1 ATOM 1096 S SG . CYS A 1 140 ? 27.912 -3.528 24.289 1.00 12.58 ? 140 CYS A SG 1 ATOM 1097 N N . GLY A 1 141 ? 23.720 -2.065 22.332 1.00 10.76 ? 141 GLY A N 1 ATOM 1098 C CA . GLY A 1 141 ? 22.306 -1.689 22.412 1.00 10.17 ? 141 GLY A CA 1 ATOM 1099 C C . GLY A 1 141 ? 21.830 -0.741 21.322 1.00 10.09 ? 141 GLY A C 1 ATOM 1100 O O . GLY A 1 141 ? 20.611 -0.647 21.098 1.00 10.80 ? 141 GLY A O 1 ATOM 1101 N N . MET A 1 142 ? 22.738 -0.025 20.670 1.00 10.30 ? 142 MET A N 1 ATOM 1102 C CA . MET A 1 142 ? 22.335 0.839 19.559 1.00 9.93 ? 142 MET A CA 1 ATOM 1103 C C . MET A 1 142 ? 22.243 0.052 18.263 1.00 10.54 ? 142 MET A C 1 ATOM 1104 O O . MET A 1 142 ? 23.027 -0.851 18.022 1.00 10.64 ? 142 MET A O 1 ATOM 1105 C CB . MET A 1 142 ? 23.318 1.995 19.374 1.00 10.53 ? 142 MET A CB 1 ATOM 1106 C CG . MET A 1 142 ? 23.288 3.048 20.474 1.00 11.57 ? 142 MET A CG 1 ATOM 1107 S SD . MET A 1 142 ? 21.666 3.851 20.709 1.00 10.84 ? 142 MET A SD 1 ATOM 1108 C CE . MET A 1 142 ? 21.270 4.444 19.084 1.00 9.91 ? 142 MET A CE 1 ATOM 1109 N N . ASN A 1 143 ? 21.276 0.424 17.423 1.00 9.85 ? 143 ASN A N 1 ATOM 1110 C CA . ASN A 1 143 ? 21.164 -0.140 16.075 1.00 9.23 ? 143 ASN A CA 1 ATOM 1111 C C . ASN A 1 143 ? 21.221 1.026 15.083 1.00 8.34 ? 143 ASN A C 1 ATOM 1112 O O . ASN A 1 143 ? 20.314 1.882 15.048 1.00 9.45 ? 143 ASN A O 1 ATOM 1113 C CB . ASN A 1 143 ? 19.854 -0.914 15.947 1.00 9.02 ? 143 ASN A CB 1 ATOM 1114 C CG . ASN A 1 143 ? 19.702 -1.660 14.632 1.00 8.80 ? 143 ASN A CG 1 ATOM 1115 O OD1 . ASN A 1 143 ? 20.213 -1.244 13.596 1.00 10.49 ? 143 ASN A OD1 1 ATOM 1116 N ND2 . ASN A 1 143 ? 18.942 -2.764 14.672 1.00 9.40 ? 143 ASN A ND2 1 ATOM 1117 N N . SER A 1 144 ? 22.319 1.108 14.318 1.00 8.60 ? 144 SER A N 1 ATOM 1118 C CA . SER A 1 144 ? 22.320 1.927 13.128 1.00 9.00 ? 144 SER A CA 1 ATOM 1119 C C . SER A 1 144 ? 21.916 1.004 11.982 1.00 8.72 ? 144 SER A C 1 ATOM 1120 O O . SER A 1 144 ? 22.516 -0.055 11.794 1.00 8.54 ? 144 SER A O 1 ATOM 1121 C CB . SER A 1 144 ? 23.659 2.616 12.895 1.00 9.07 ? 144 SER A CB 1 ATOM 1122 O OG . SER A 1 144 ? 24.698 1.751 12.471 1.00 9.02 ? 144 SER A OG 1 ATOM 1123 N N . ALA A 1 145 ? 20.890 1.401 11.228 1.00 8.19 ? 145 ALA A N 1 ATOM 1124 C CA . ALA A 1 145 ? 20.326 0.551 10.189 1.00 8.26 ? 145 ALA A CA 1 ATOM 1125 C C . ALA A 1 145 ? 20.366 1.248 8.831 1.00 8.23 ? 145 ALA A C 1 ATOM 1126 O O . ALA A 1 145 ? 20.217 2.482 8.723 1.00 8.34 ? 145 ALA A O 1 ATOM 1127 C CB . ALA A 1 145 ? 18.897 0.168 10.550 1.00 8.98 ? 145 ALA A CB 1 ATOM 1128 N N . LEU A 1 146 ? 20.564 0.431 7.809 1.00 7.62 ? 146 LEU A N 1 ATOM 1129 C CA . LEU A 1 146 ? 20.570 0.849 6.414 1.00 8.12 ? 146 LEU A CA 1 ATOM 1130 C C . LEU A 1 146 ? 19.980 -0.349 5.703 1.00 8.23 ? 146 LEU A C 1 ATOM 1131 O O . LEU A 1 146 ? 20.538 -1.437 5.747 1.00 8.56 ? 146 LEU A O 1 ATOM 1132 C CB . LEU A 1 146 ? 21.985 1.231 5.959 1.00 8.74 ? 146 LEU A CB 1 ATOM 1133 C CG . LEU A 1 146 ? 22.123 1.718 4.527 1.00 8.29 ? 146 LEU A CG 1 ATOM 1134 C CD1 . LEU A 1 146 ? 23.351 2.616 4.354 1.00 9.68 ? 146 LEU A CD1 1 ATOM 1135 C CD2 . LEU A 1 146 ? 22.182 0.595 3.568 1.00 9.54 ? 146 LEU A CD2 1 ATOM 1136 N N . TYR A 1 147 ? 18.800 -0.200 5.115 1.00 8.19 ? 147 TYR A N 1 ATOM 1137 C CA . TYR A 1 147 ? 18.047 -1.365 4.664 1.00 8.27 ? 147 TYR A CA 1 ATOM 1138 C C . TYR A 1 147 ? 17.046 -0.985 3.596 1.00 8.09 ? 147 TYR A C 1 ATOM 1139 O O . TYR A 1 147 ? 16.870 0.188 3.286 1.00 8.84 ? 147 TYR A O 1 ATOM 1140 C CB . TYR A 1 147 ? 17.353 -2.013 5.850 1.00 8.71 ? 147 TYR A CB 1 ATOM 1141 C CG . TYR A 1 147 ? 16.291 -1.196 6.564 1.00 8.24 ? 147 TYR A CG 1 ATOM 1142 C CD1 . TYR A 1 147 ? 16.639 -0.182 7.438 1.00 8.94 ? 147 TYR A CD1 1 ATOM 1143 C CD2 . TYR A 1 147 ? 14.947 -1.467 6.383 1.00 8.48 ? 147 TYR A CD2 1 ATOM 1144 C CE1 . TYR A 1 147 ? 15.701 0.522 8.126 1.00 8.03 ? 147 TYR A CE1 1 ATOM 1145 C CE2 . TYR A 1 147 ? 13.978 -0.749 7.074 1.00 8.31 ? 147 TYR A CE2 1 ATOM 1146 C CZ . TYR A 1 147 ? 14.360 0.213 7.963 1.00 7.85 ? 147 TYR A CZ 1 ATOM 1147 O OH . TYR A 1 147 ? 13.424 0.910 8.687 1.00 8.34 ? 147 TYR A OH 1 ATOM 1148 N N . LEU A 1 148 ? 16.448 -1.990 2.985 1.00 7.56 ? 148 LEU A N 1 ATOM 1149 C CA . LEU A 1 148 ? 15.522 -1.802 1.878 1.00 7.87 ? 148 LEU A CA 1 ATOM 1150 C C . LEU A 1 148 ? 14.171 -2.346 2.260 1.00 8.20 ? 148 LEU A C 1 ATOM 1151 O O . LEU A 1 148 ? 14.088 -3.398 2.870 1.00 8.52 ? 148 LEU A O 1 ATOM 1152 C CB . LEU A 1 148 ? 16.031 -2.608 0.688 1.00 8.48 ? 148 LEU A CB 1 ATOM 1153 C CG . LEU A 1 148 ? 17.423 -2.290 0.183 1.00 10.65 ? 148 LEU A CG 1 ATOM 1154 C CD1 . LEU A 1 148 ? 17.805 -3.322 -0.869 1.00 13.13 ? 148 LEU A CD1 1 ATOM 1155 C CD2 . LEU A 1 148 ? 17.447 -0.900 -0.403 1.00 13.75 ? 148 LEU A CD2 1 ATOM 1156 N N . SER A 1 149 ? 13.118 -1.606 1.946 1.00 7.51 ? 149 SER A N 1 ATOM 1157 C CA . SER A 1 149 ? 11.740 -2.071 2.123 1.00 7.87 ? 149 SER A CA 1 ATOM 1158 C C . SER A 1 149 ? 10.996 -1.920 0.806 1.00 7.78 ? 149 SER A C 1 ATOM 1159 O O . SER A 1 149 ? 11.247 -0.966 0.048 1.00 8.50 ? 149 SER A O 1 ATOM 1160 C CB . SER A 1 149 ? 10.989 -1.294 3.209 1.00 8.12 ? 149 SER A CB 1 ATOM 1161 O OG . SER A 1 149 ? 11.267 -1.823 4.514 1.00 11.33 ? 149 SER A OG 1 ATOM 1162 N N . GLU A 1 150 ? 10.049 -2.819 0.549 1.00 7.77 ? 150 GLU A N 1 ATOM 1163 C CA . GLU A 1 150 ? 9.291 -2.773 -0.715 1.00 7.87 ? 150 GLU A CA 1 ATOM 1164 C C . GLU A 1 150 ? 8.099 -1.815 -0.629 1.00 8.15 ? 150 GLU A C 1 ATOM 1165 O O . GLU A 1 150 ? 6.932 -2.211 -0.762 1.00 8.88 ? 150 GLU A O 1 ATOM 1166 C CB . GLU A 1 150 ? 8.882 -4.172 -1.202 1.00 7.75 ? 150 GLU A CB 1 ATOM 1167 C CG . GLU A 1 150 ? 8.630 -4.150 -2.709 1.00 7.99 ? 150 GLU A CG 1 ATOM 1168 C CD . GLU A 1 150 ? 8.093 -5.423 -3.343 1.00 7.62 ? 150 GLU A CD 1 ATOM 1169 O OE1 . GLU A 1 150 ? 7.982 -6.462 -2.648 1.00 9.93 ? 150 GLU A OE1 1 ATOM 1170 O OE2 . GLU A 1 150 ? 7.799 -5.352 -4.570 1.00 9.40 ? 150 GLU A OE2 1 ATOM 1171 N N . MET A 1 151 ? 8.434 -0.543 -0.402 1.00 7.85 ? 151 MET A N 1 ATOM 1172 C CA . MET A 1 151 ? 7.486 0.551 -0.358 1.00 8.31 ? 151 MET A CA 1 ATOM 1173 C C . MET A 1 151 ? 7.119 0.985 -1.772 1.00 8.20 ? 151 MET A C 1 ATOM 1174 O O . MET A 1 151 ? 7.819 0.707 -2.751 1.00 8.70 ? 151 MET A O 1 ATOM 1175 C CB . MET A 1 151 ? 8.072 1.718 0.417 1.00 8.52 ? 151 MET A CB 1 ATOM 1176 C CG . MET A 1 151 ? 8.355 1.412 1.865 1.00 8.10 ? 151 MET A CG 1 ATOM 1177 S SD . MET A 1 151 ? 9.550 2.508 2.661 1.00 8.61 ? 151 MET A SD 1 ATOM 1178 C CE . MET A 1 151 ? 8.848 4.191 2.332 1.00 9.18 ? 151 MET A CE 1 ATOM 1179 N N . HIS A 1 152 ? 5.950 1.608 -1.881 1.00 8.51 ? 152 HIS A N 1 ATOM 1180 C CA . HIS A 1 152 ? 5.431 2.076 -3.152 1.00 9.01 ? 152 HIS A CA 1 ATOM 1181 C C . HIS A 1 152 ? 6.254 3.283 -3.610 1.00 8.68 ? 152 HIS A C 1 ATOM 1182 O O . HIS A 1 152 ? 6.606 4.132 -2.778 1.00 8.91 ? 152 HIS A O 1 ATOM 1183 C CB . HIS A 1 152 ? 3.973 2.491 -2.971 1.00 9.31 ? 152 HIS A CB 1 ATOM 1184 C CG . HIS A 1 152 ? 3.304 2.922 -4.228 1.00 9.09 ? 152 HIS A CG 1 ATOM 1185 N ND1 . HIS A 1 152 ? 3.457 4.182 -4.759 1.00 8.82 ? 152 HIS A ND1 1 ATOM 1186 C CD2 . HIS A 1 152 ? 2.462 2.257 -5.053 1.00 10.93 ? 152 HIS A CD2 1 ATOM 1187 C CE1 . HIS A 1 152 ? 2.755 4.262 -5.875 1.00 9.93 ? 152 HIS A CE1 1 ATOM 1188 N NE2 . HIS A 1 152 ? 2.136 3.112 -6.071 1.00 11.43 ? 152 HIS A NE2 1 ATOM 1189 N N . PRO A 1 153 ? 6.595 3.401 -4.904 1.00 8.82 ? 153 PRO A N 1 ATOM 1190 C CA . PRO A 1 153 ? 7.536 4.454 -5.305 1.00 9.24 ? 153 PRO A CA 1 ATOM 1191 C C . PRO A 1 153 ? 7.110 5.893 -5.055 1.00 9.08 ? 153 PRO A C 1 ATOM 1192 O O . PRO A 1 153 ? 7.961 6.749 -4.909 1.00 9.27 ? 153 PRO A O 1 ATOM 1193 C CB . PRO A 1 153 ? 7.731 4.219 -6.803 1.00 9.73 ? 153 PRO A CB 1 ATOM 1194 C CG . PRO A 1 153 ? 7.405 2.807 -7.013 1.00 13.10 ? 153 PRO A CG 1 ATOM 1195 C CD . PRO A 1 153 ? 6.274 2.492 -6.025 1.00 9.14 ? 153 PRO A CD 1 ATOM 1196 N N . THR A 1 154 ? 5.824 6.186 -5.070 1.00 8.66 ? 154 THR A N 1 ATOM 1197 C CA . THR A 1 154 ? 5.383 7.546 -4.720 1.00 8.96 ? 154 THR A CA 1 ATOM 1198 C C . THR A 1 154 ? 4.819 7.616 -3.318 1.00 9.06 ? 154 THR A C 1 ATOM 1199 O O . THR A 1 154 ? 4.124 8.570 -2.952 1.00 9.81 ? 154 THR A O 1 ATOM 1200 C CB . THR A 1 154 ? 4.346 8.085 -5.704 1.00 9.07 ? 154 THR A CB 1 ATOM 1201 O OG1 . THR A 1 154 ? 3.141 7.308 -5.609 1.00 10.43 ? 154 THR A OG1 1 ATOM 1202 C CG2 . THR A 1 154 ? 4.883 7.989 -7.122 1.00 12.01 ? 154 THR A CG2 1 ATOM 1203 N N . GLY A 1 155 ? 5.127 6.613 -2.504 1.00 9.26 ? 155 GLY A N 1 ATOM 1204 C CA . GLY A 1 155 ? 4.540 6.547 -1.177 1.00 9.43 ? 155 GLY A CA 1 ATOM 1205 C C . GLY A 1 155 ? 3.035 6.370 -1.238 1.00 9.22 ? 155 GLY A C 1 ATOM 1206 O O . GLY A 1 155 ? 2.326 6.739 -0.311 1.00 9.73 ? 155 GLY A O 1 ATOM 1207 N N . ALA A 1 156 ? 2.559 5.799 -2.337 1.00 9.73 ? 156 ALA A N 1 ATOM 1208 C CA . ALA A 1 156 ? 1.131 5.598 -2.605 1.00 9.14 ? 156 ALA A CA 1 ATOM 1209 C C . ALA A 1 156 ? 0.384 6.927 -2.577 1.00 8.88 ? 156 ALA A C 1 ATOM 1210 O O . ALA A 1 156 ? -0.670 7.084 -1.962 1.00 9.58 ? 156 ALA A O 1 ATOM 1211 C CB . ALA A 1 156 ? 0.511 4.594 -1.672 1.00 9.73 ? 156 ALA A CB 1 ATOM 1212 N N . LYS A 1 157 ? 0.908 7.922 -3.287 1.00 9.01 ? 157 LYS A N 1 ATOM 1213 C CA . LYS A 1 157 ? 0.203 9.178 -3.423 1.00 9.61 ? 157 LYS A CA 1 ATOM 1214 C C . LYS A 1 157 ? -1.199 8.866 -3.989 1.00 9.31 ? 157 LYS A C 1 ATOM 1215 O O . LYS A 1 157 ? -1.345 8.084 -4.893 1.00 10.70 ? 157 LYS A O 1 ATOM 1216 C CB . LYS A 1 157 ? 0.970 10.090 -4.359 1.00 9.20 ? 157 LYS A CB 1 ATOM 1217 C CG . LYS A 1 157 ? 0.368 11.461 -4.550 1.00 10.38 ? 157 LYS A CG 1 ATOM 1218 C CD . LYS A 1 157 ? 1.121 12.275 -5.581 1.00 13.53 ? 157 LYS A CD 1 ATOM 1219 C CE . LYS A 1 157 ? 0.466 13.605 -5.857 1.00 16.89 ? 157 LYS A CE 1 ATOM 1220 N NZ . LYS A 1 157 ? 1.024 14.646 -4.987 1.00 23.64 ? 157 LYS A NZ 1 ATOM 1221 N N . SER A 1 158 ? -2.213 9.524 -3.460 1.00 9.67 ? 158 SER A N 1 ATOM 1222 C CA . SER A 1 158 ? -3.601 9.248 -3.803 1.00 10.62 ? 158 SER A CA 1 ATOM 1223 C C . SER A 1 158 ? -4.475 10.424 -3.364 1.00 11.25 ? 158 SER A C 1 ATOM 1224 O O . SER A 1 158 ? -4.001 11.387 -2.791 1.00 11.21 ? 158 SER A O 1 ATOM 1225 C CB . SER A 1 158 ? -4.093 7.961 -3.124 1.00 10.71 ? 158 SER A CB 1 ATOM 1226 O OG . SER A 1 158 ? -4.164 8.102 -1.711 1.00 10.81 ? 158 SER A OG 1 ATOM 1227 N N . LYS A 1 159 ? -5.769 10.351 -3.645 1.00 13.24 ? 159 LYS A N 1 ATOM 1228 C CA . LYS A 1 159 ? -6.701 11.424 -3.315 1.00 13.70 ? 159 LYS A CA 1 ATOM 1229 C C . LYS A 1 159 ? -6.629 11.841 -1.849 1.00 12.19 ? 159 LYS A C 1 ATOM 1230 O O . LYS A 1 159 ? -6.599 13.030 -1.543 1.00 13.17 ? 159 LYS A O 1 ATOM 1231 C CB . LYS A 1 159 ? -8.122 10.996 -3.681 1.00 15.88 ? 159 LYS A CB 1 ATOM 1232 C CG . LYS A 1 159 ? -9.261 11.880 -3.159 1.00 18.56 ? 159 LYS A CG 1 ATOM 1233 C CD . LYS A 1 159 ? -10.572 11.189 -3.570 1.00 19.95 ? 159 LYS A CD 1 ATOM 1234 C CE . LYS A 1 159 ? -11.785 12.041 -3.562 1.00 24.52 ? 159 LYS A CE 1 ATOM 1235 N NZ . LYS A 1 159 ? -12.913 11.134 -3.913 1.00 27.06 ? 159 LYS A NZ 1 ATOM 1236 N N . TYR A 1 160 ? -6.630 10.877 -0.936 1.00 11.21 ? 160 TYR A N 1 ATOM 1237 C CA . TYR A 1 160 ? -6.589 11.197 0.489 1.00 11.19 ? 160 TYR A CA 1 ATOM 1238 C C . TYR A 1 160 ? -5.159 11.336 1.025 1.00 9.86 ? 160 TYR A C 1 ATOM 1239 O O . TYR A 1 160 ? -4.975 11.793 2.143 1.00 9.20 ? 160 TYR A O 1 ATOM 1240 C CB . TYR A 1 160 ? -7.371 10.143 1.304 1.00 12.69 ? 160 TYR A CB 1 ATOM 1241 C CG . TYR A 1 160 ? -8.846 10.074 0.984 1.00 14.81 ? 160 TYR A CG 1 ATOM 1242 C CD1 . TYR A 1 160 ? -9.621 11.226 0.928 1.00 14.02 ? 160 TYR A CD1 1 ATOM 1243 C CD2 . TYR A 1 160 ? -9.455 8.855 0.718 1.00 16.61 ? 160 TYR A CD2 1 ATOM 1244 C CE1 . TYR A 1 160 ? -10.988 11.172 0.608 1.00 16.26 ? 160 TYR A CE1 1 ATOM 1245 C CE2 . TYR A 1 160 ? -10.814 8.793 0.404 1.00 17.13 ? 160 TYR A CE2 1 ATOM 1246 C CZ . TYR A 1 160 ? -11.550 9.954 0.321 1.00 17.07 ? 160 TYR A CZ 1 ATOM 1247 O OH . TYR A 1 160 ? -12.900 9.874 0.011 1.00 19.43 ? 160 TYR A OH 1 ATOM 1248 N N . ASN A 1 161 ? -4.169 10.931 0.210 1.00 9.27 ? 161 ASN A N 1 ATOM 1249 C CA . ASN A 1 161 ? -2.727 11.110 0.499 1.00 8.98 ? 161 ASN A CA 1 ATOM 1250 C C . ASN A 1 161 ? -2.036 11.926 -0.580 1.00 9.16 ? 161 ASN A C 1 ATOM 1251 O O . ASN A 1 161 ? -1.242 11.393 -1.359 1.00 8.70 ? 161 ASN A O 1 ATOM 1252 C CB . ASN A 1 161 ? -2.054 9.733 0.625 1.00 8.70 ? 161 ASN A CB 1 ATOM 1253 C CG . ASN A 1 161 ? -0.550 9.792 0.805 1.00 9.09 ? 161 ASN A CG 1 ATOM 1254 O OD1 . ASN A 1 161 ? 0.185 8.835 0.418 1.00 11.33 ? 161 ASN A OD1 1 ATOM 1255 N ND2 . ASN A 1 161 ? -0.072 10.856 1.370 1.00 6.73 ? 161 ASN A ND2 1 ATOM 1256 N N . PRO A 1 162 ? -2.320 13.220 -0.658 1.00 8.97 ? 162 PRO A N 1 ATOM 1257 C CA . PRO A 1 162 ? -1.656 14.039 -1.667 1.00 9.49 ? 162 PRO A CA 1 ATOM 1258 C C . PRO A 1 162 ? -0.164 14.238 -1.390 1.00 9.67 ? 162 PRO A C 1 ATOM 1259 O O . PRO A 1 162 ? 0.593 14.550 -2.303 1.00 11.30 ? 162 PRO A O 1 ATOM 1260 C CB . PRO A 1 162 ? -2.420 15.370 -1.588 1.00 10.29 ? 162 PRO A CB 1 ATOM 1261 C CG . PRO A 1 162 ? -2.925 15.414 -0.213 1.00 9.88 ? 162 PRO A CG 1 ATOM 1262 C CD . PRO A 1 162 ? -3.273 13.991 0.146 1.00 9.98 ? 162 PRO A CD 1 ATOM 1263 N N . GLY A 1 163 ? 0.255 14.101 -0.140 1.00 9.48 ? 163 GLY A N 1 ATOM 1264 C CA . GLY A 1 163 ? 1.655 14.320 0.215 1.00 9.82 ? 163 GLY A CA 1 ATOM 1265 C C . GLY A 1 163 ? 2.617 13.325 -0.428 1.00 9.64 ? 163 GLY A C 1 ATOM 1266 O O . GLY A 1 163 ? 3.608 13.712 -1.048 1.00 10.18 ? 163 GLY A O 1 ATOM 1267 N N . GLY A 1 164 ? 2.322 12.040 -0.289 1.00 9.00 ? 164 GLY A N 1 ATOM 1268 C CA . GLY A 1 164 ? 3.135 11.002 -0.902 1.00 8.53 ? 164 GLY A CA 1 ATOM 1269 C C . GLY A 1 164 ? 4.566 10.952 -0.390 1.00 8.89 ? 164 GLY A C 1 ATOM 1270 O O . GLY A 1 164 ? 4.873 11.350 0.749 1.00 9.39 ? 164 GLY A O 1 ATOM 1271 N N . ALA A 1 165 ? 5.460 10.512 -1.268 1.00 8.55 ? 165 ALA A N 1 ATOM 1272 C CA . ALA A 1 165 ? 6.855 10.328 -0.932 1.00 8.39 ? 165 ALA A CA 1 ATOM 1273 C C . ALA A 1 165 ? 7.562 11.621 -0.512 1.00 8.54 ? 165 ALA A C 1 ATOM 1274 O O . ALA A 1 165 ? 8.519 11.585 0.269 1.00 8.31 ? 165 ALA A O 1 ATOM 1275 C CB . ALA A 1 165 ? 7.599 9.683 -2.113 1.00 8.99 ? 165 ALA A CB 1 ATOM 1276 N N . TYR A 1 166 ? 7.099 12.763 -1.040 1.00 8.58 ? 166 TYR A N 1 ATOM 1277 C CA . TYR A 1 166 ? 7.647 14.063 -0.663 1.00 8.12 ? 166 TYR A CA 1 ATOM 1278 C C . TYR A 1 166 ? 7.556 14.262 0.852 1.00 8.04 ? 166 TYR A C 1 ATOM 1279 O O . TYR A 1 166 ? 8.372 14.999 1.408 1.00 8.78 ? 166 TYR A O 1 ATOM 1280 C CB . TYR A 1 166 ? 6.876 15.172 -1.398 1.00 8.96 ? 166 TYR A CB 1 ATOM 1281 C CG . TYR A 1 166 ? 7.385 16.592 -1.301 1.00 8.56 ? 166 TYR A CG 1 ATOM 1282 C CD1 . TYR A 1 166 ? 8.245 17.119 -2.267 1.00 9.00 ? 166 TYR A CD1 1 ATOM 1283 C CD2 . TYR A 1 166 ? 6.977 17.421 -0.303 1.00 10.12 ? 166 TYR A CD2 1 ATOM 1284 C CE1 . TYR A 1 166 ? 8.660 18.436 -2.226 1.00 10.39 ? 166 TYR A CE1 1 ATOM 1285 C CE2 . TYR A 1 166 ? 7.407 18.726 -0.229 1.00 11.82 ? 166 TYR A CE2 1 ATOM 1286 C CZ . TYR A 1 166 ? 8.252 19.226 -1.183 1.00 12.01 ? 166 TYR A CZ 1 ATOM 1287 O OH . TYR A 1 166 ? 8.642 20.564 -1.098 1.00 13.75 ? 166 TYR A OH 1 ATOM 1288 N N . TYR A 1 167 ? 6.569 13.639 1.523 1.00 8.11 ? 167 TYR A N 1 ATOM 1289 C CA . TYR A 1 167 ? 6.430 13.721 2.968 1.00 8.18 ? 167 TYR A CA 1 ATOM 1290 C C . TYR A 1 167 ? 6.750 12.381 3.651 1.00 7.96 ? 167 TYR A C 1 ATOM 1291 O O . TYR A 1 167 ? 6.516 12.216 4.836 1.00 9.36 ? 167 TYR A O 1 ATOM 1292 C CB . TYR A 1 167 ? 5.016 14.175 3.365 1.00 9.30 ? 167 TYR A CB 1 ATOM 1293 C CG . TYR A 1 167 ? 4.750 15.632 3.055 1.00 8.58 ? 167 TYR A CG 1 ATOM 1294 C CD1 . TYR A 1 167 ? 4.251 16.014 1.828 1.00 8.97 ? 167 TYR A CD1 1 ATOM 1295 C CD2 . TYR A 1 167 ? 4.943 16.613 4.013 1.00 10.45 ? 167 TYR A CD2 1 ATOM 1296 C CE1 . TYR A 1 167 ? 4.014 17.331 1.529 1.00 9.50 ? 167 TYR A CE1 1 ATOM 1297 C CE2 . TYR A 1 167 ? 4.706 17.954 3.709 1.00 10.94 ? 167 TYR A CE2 1 ATOM 1298 C CZ . TYR A 1 167 ? 4.245 18.298 2.461 1.00 10.15 ? 167 TYR A CZ 1 ATOM 1299 O OH . TYR A 1 167 ? 3.983 19.630 2.166 1.00 12.07 ? 167 TYR A OH 1 ATOM 1300 N N . GLY A 1 168 ? 7.347 11.441 2.922 1.00 7.83 ? 168 GLY A N 1 ATOM 1301 C CA . GLY A 1 168 ? 7.776 10.184 3.508 1.00 7.96 ? 168 GLY A CA 1 ATOM 1302 C C . GLY A 1 168 ? 6.686 9.198 3.835 1.00 7.73 ? 168 GLY A C 1 ATOM 1303 O O . GLY A 1 168 ? 6.855 8.405 4.761 1.00 7.20 ? 168 GLY A O 1 ATOM 1304 N N . THR A 1 169 ? 5.579 9.207 3.097 1.00 7.93 ? 169 THR A N 1 ATOM 1305 C CA . THR A 1 169 ? 4.500 8.249 3.347 1.00 7.77 ? 169 THR A CA 1 ATOM 1306 C C . THR A 1 169 ? 4.807 6.863 2.784 1.00 8.09 ? 169 THR A C 1 ATOM 1307 O O . THR A 1 169 ? 5.676 6.683 1.924 1.00 8.22 ? 169 THR A O 1 ATOM 1308 C CB . THR A 1 169 ? 3.145 8.719 2.797 1.00 7.79 ? 169 THR A CB 1 ATOM 1309 O OG1 . THR A 1 169 ? 3.199 8.775 1.366 1.00 8.61 ? 169 THR A OG1 1 ATOM 1310 C CG2 . THR A 1 169 ? 2.767 10.127 3.287 1.00 7.96 ? 169 THR A CG2 1 ATOM 1311 N N . GLY A 1 170 ? 4.087 5.871 3.304 1.00 7.87 ? 170 GLY A N 1 ATOM 1312 C CA . GLY A 1 170 ? 4.155 4.537 2.743 1.00 7.79 ? 170 GLY A CA 1 ATOM 1313 C C . GLY A 1 170 ? 5.100 3.528 3.405 1.00 7.30 ? 170 GLY A C 1 ATOM 1314 O O . GLY A 1 170 ? 5.341 2.473 2.856 1.00 8.40 ? 170 GLY A O 1 ATOM 1315 N N . TYR A 1 171 ? 5.679 3.850 4.567 1.00 7.42 ? 171 TYR A N 1 ATOM 1316 C CA . TYR A 1 171 ? 6.583 2.908 5.214 1.00 7.48 ? 171 TYR A CA 1 ATOM 1317 C C . TYR A 1 171 ? 5.934 1.553 5.492 1.00 7.56 ? 171 TYR A C 1 ATOM 1318 O O . TYR A 1 171 ? 4.777 1.476 5.895 1.00 8.05 ? 171 TYR A O 1 ATOM 1319 C CB . TYR A 1 171 ? 7.127 3.486 6.536 1.00 8.02 ? 171 TYR A CB 1 ATOM 1320 C CG . TYR A 1 171 ? 8.140 2.586 7.165 1.00 7.47 ? 171 TYR A CG 1 ATOM 1321 C CD1 . TYR A 1 171 ? 9.395 2.391 6.567 1.00 7.97 ? 171 TYR A CD1 1 ATOM 1322 C CD2 . TYR A 1 171 ? 7.845 1.844 8.283 1.00 7.73 ? 171 TYR A CD2 1 ATOM 1323 C CE1 . TYR A 1 171 ? 10.309 1.531 7.097 1.00 8.01 ? 171 TYR A CE1 1 ATOM 1324 C CE2 . TYR A 1 171 ? 8.760 0.977 8.805 1.00 8.59 ? 171 TYR A CE2 1 ATOM 1325 C CZ . TYR A 1 171 ? 9.995 0.817 8.217 1.00 8.28 ? 171 TYR A CZ 1 ATOM 1326 O OH . TYR A 1 171 ? 10.932 -0.076 8.737 1.00 8.28 ? 171 TYR A OH 1 ATOM 1327 N N . CYS A 1 172 ? 6.730 0.500 5.334 1.00 7.95 ? 172 CYS A N 1 ATOM 1328 C CA . CYS A 1 172 ? 6.388 -0.849 5.741 1.00 7.74 ? 172 CYS A CA 1 ATOM 1329 C C . CYS A 1 172 ? 7.677 -1.611 6.023 1.00 7.79 ? 172 CYS A C 1 ATOM 1330 O O . CYS A 1 172 ? 8.766 -1.200 5.603 1.00 7.86 ? 172 CYS A O 1 ATOM 1331 C CB . CYS A 1 172 ? 5.555 -1.540 4.647 1.00 8.36 ? 172 CYS A CB 1 ATOM 1332 S SG . CYS A 1 172 ? 6.365 -1.599 3.038 1.00 8.42 ? 172 CYS A SG 1 ATOM 1333 N N . ASP A 1 173 ? 7.568 -2.718 6.737 1.00 7.70 ? 173 ASP A N 1 ATOM 1334 C CA . ASP A 1 173 ? 8.692 -3.611 6.930 1.00 7.98 ? 173 ASP A CA 1 ATOM 1335 C C . ASP A 1 173 ? 8.177 -5.002 7.319 1.00 7.50 ? 173 ASP A C 1 ATOM 1336 O O . ASP A 1 173 ? 6.963 -5.236 7.383 1.00 8.13 ? 173 ASP A O 1 ATOM 1337 C CB . ASP A 1 173 ? 9.748 -3.045 7.896 1.00 7.97 ? 173 ASP A CB 1 ATOM 1338 C CG . ASP A 1 173 ? 9.250 -2.892 9.294 1.00 8.60 ? 173 ASP A CG 1 ATOM 1339 O OD1 . ASP A 1 173 ? 8.385 -3.708 9.719 1.00 8.31 ? 173 ASP A OD1 1 ATOM 1340 O OD2 . ASP A 1 173 ? 9.679 -1.979 10.044 1.00 8.70 ? 173 ASP A OD2 1 ATOM 1341 N N . ALA A 1 174 ? 9.102 -5.923 7.539 1.00 7.84 ? 174 ALA A N 1 ATOM 1342 C CA . ALA A 1 174 ? 8.760 -7.334 7.754 1.00 8.23 ? 174 ALA A CA 1 ATOM 1343 C C . ALA A 1 174 ? 8.168 -7.626 9.134 1.00 8.93 ? 174 ALA A C 1 ATOM 1344 O O . ALA A 1 174 ? 7.827 -8.780 9.413 1.00 9.16 ? 174 ALA A O 1 ATOM 1345 C CB . ALA A 1 174 ? 9.953 -8.213 7.490 1.00 9.60 ? 174 ALA A CB 1 ATOM 1346 N N . GLN A 1 175 ? 8.026 -6.597 9.977 1.00 8.47 ? 175 GLN A N 1 ATOM 1347 C CA . GLN A 1 175 ? 7.419 -6.758 11.291 1.00 8.56 ? 175 GLN A CA 1 ATOM 1348 C C . GLN A 1 175 ? 5.914 -6.546 11.308 1.00 8.27 ? 175 GLN A C 1 ATOM 1349 O O . GLN A 1 175 ? 5.274 -6.846 12.309 1.00 9.64 ? 175 GLN A O 1 ATOM 1350 C CB . GLN A 1 175 ? 8.060 -5.841 12.340 1.00 8.75 ? 175 GLN A CB 1 ATOM 1351 C CG . GLN A 1 175 ? 9.547 -5.989 12.468 1.00 9.91 ? 175 GLN A CG 1 ATOM 1352 C CD . GLN A 1 175 ? 10.046 -7.438 12.679 1.00 9.41 ? 175 GLN A CD 1 ATOM 1353 O OE1 . GLN A 1 175 ? 9.471 -8.184 13.482 1.00 11.62 ? 175 GLN A OE1 1 ATOM 1354 N NE2 . GLN A 1 175 ? 11.087 -7.836 11.939 1.00 10.27 ? 175 GLN A NE2 1 ATOM 1355 N N . CYS A 1 176 ? 5.329 -6.036 10.222 1.00 8.48 ? 176 CYS A N 1 ATOM 1356 C CA . CYS A 1 176 ? 3.881 -5.863 10.130 1.00 8.64 ? 176 CYS A CA 1 ATOM 1357 C C . CYS A 1 176 ? 3.341 -5.018 11.296 1.00 8.80 ? 176 CYS A C 1 ATOM 1358 O O . CYS A 1 176 ? 2.267 -5.340 11.834 1.00 9.34 ? 176 CYS A O 1 ATOM 1359 C CB . CYS A 1 176 ? 3.190 -7.222 10.080 1.00 8.34 ? 176 CYS A CB 1 ATOM 1360 S SG . CYS A 1 176 ? 3.450 -8.197 8.583 1.00 9.33 ? 176 CYS A SG 1 ATOM 1361 N N . PHE A 1 177 ? 4.045 -3.949 11.682 1.00 8.57 ? 177 PHE A N 1 ATOM 1362 C CA . PHE A 1 177 ? 3.597 -3.095 12.768 1.00 9.04 ? 177 PHE A CA 1 ATOM 1363 C C . PHE A 1 177 ? 2.326 -2.335 12.411 1.00 8.70 ? 177 PHE A C 1 ATOM 1364 O O . PHE A 1 177 ? 2.089 -1.960 11.248 1.00 9.26 ? 177 PHE A O 1 ATOM 1365 C CB . PHE A 1 177 ? 4.650 -2.053 13.157 1.00 9.31 ? 177 PHE A CB 1 ATOM 1366 C CG . PHE A 1 177 ? 5.926 -2.600 13.763 1.00 10.27 ? 177 PHE A CG 1 ATOM 1367 C CD1 . PHE A 1 177 ? 5.893 -3.437 14.871 1.00 11.41 ? 177 PHE A CD1 1 ATOM 1368 C CD2 . PHE A 1 177 ? 7.154 -2.213 13.266 1.00 9.88 ? 177 PHE A CD2 1 ATOM 1369 C CE1 . PHE A 1 177 ? 7.069 -3.884 15.458 1.00 11.71 ? 177 PHE A CE1 1 ATOM 1370 C CE2 . PHE A 1 177 ? 8.335 -2.661 13.858 1.00 9.83 ? 177 PHE A CE2 1 ATOM 1371 C CZ . PHE A 1 177 ? 8.304 -3.466 14.955 1.00 10.94 ? 177 PHE A CZ 1 ATOM 1372 N N . VAL A 1 178 ? 1.532 -2.051 13.433 1.00 9.85 ? 178 VAL A N 1 ATOM 1373 C CA . VAL A 1 178 ? 0.365 -1.211 13.291 1.00 10.05 ? 178 VAL A CA 1 ATOM 1374 C C . VAL A 1 178 ? 0.764 0.246 13.462 1.00 9.91 ? 178 VAL A C 1 ATOM 1375 O O . VAL A 1 178 ? 1.286 0.625 14.511 1.00 10.40 ? 178 VAL A O 1 ATOM 1376 C CB . VAL A 1 178 ? -0.693 -1.584 14.358 1.00 9.53 ? 178 VAL A CB 1 ATOM 1377 C CG1 . VAL A 1 178 ? -1.905 -0.683 14.214 1.00 10.48 ? 178 VAL A CG1 1 ATOM 1378 C CG2 . VAL A 1 178 ? -1.097 -3.018 14.224 1.00 10.83 ? 178 VAL A CG2 1 ATOM 1379 N N . THR A 1 179 ? 0.500 1.064 12.445 1.00 8.90 ? 179 THR A N 1 ATOM 1380 C CA . THR A 1 179 ? 0.704 2.513 12.540 1.00 9.33 ? 179 THR A CA 1 ATOM 1381 C C . THR A 1 179 ? -0.618 3.215 12.251 1.00 8.60 ? 179 THR A C 1 ATOM 1382 O O . THR A 1 179 ? -1.464 2.686 11.513 1.00 9.59 ? 179 THR A O 1 ATOM 1383 C CB . THR A 1 179 ? 1.811 2.972 11.581 1.00 9.37 ? 179 THR A CB 1 ATOM 1384 O OG1 . THR A 1 179 ? 1.547 2.512 10.241 1.00 9.05 ? 179 THR A OG1 1 ATOM 1385 C CG2 . THR A 1 179 ? 3.201 2.394 12.017 1.00 10.97 ? 179 THR A CG2 1 ATOM 1386 N N . PRO A 1 180 ? -0.825 4.405 12.828 1.00 9.25 ? 180 PRO A N 1 ATOM 1387 C CA . PRO A 1 180 ? -2.140 5.072 12.659 1.00 9.39 ? 180 PRO A CA 1 ATOM 1388 C C . PRO A 1 180 ? -2.476 5.512 11.244 1.00 9.66 ? 180 PRO A C 1 ATOM 1389 O O . PRO A 1 180 ? -3.632 5.717 10.933 1.00 8.95 ? 180 PRO A O 1 ATOM 1390 C CB . PRO A 1 180 ? -2.076 6.271 13.641 1.00 11.13 ? 180 PRO A CB 1 ATOM 1391 C CG . PRO A 1 180 ? -0.640 6.406 13.992 1.00 11.96 ? 180 PRO A CG 1 ATOM 1392 C CD . PRO A 1 180 ? 0.015 5.070 13.825 1.00 9.05 ? 180 PRO A CD 1 ATOM 1393 N N . PHE A 1 181 ? -1.462 5.648 10.398 1.00 8.83 ? 181 PHE A N 1 ATOM 1394 C CA . PHE A 1 181 ? -1.645 5.829 8.958 1.00 8.51 ? 181 PHE A CA 1 ATOM 1395 C C . PHE A 1 181 ? -0.798 4.796 8.251 1.00 8.28 ? 181 PHE A C 1 ATOM 1396 O O . PHE A 1 181 ? 0.325 4.493 8.709 1.00 8.16 ? 181 PHE A O 1 ATOM 1397 C CB . PHE A 1 181 ? -1.222 7.219 8.499 1.00 8.75 ? 181 PHE A CB 1 ATOM 1398 C CG . PHE A 1 181 ? -2.074 8.332 9.067 1.00 8.76 ? 181 PHE A CG 1 ATOM 1399 C CD1 . PHE A 1 181 ? -1.948 8.757 10.378 1.00 9.37 ? 181 PHE A CD1 1 ATOM 1400 C CD2 . PHE A 1 181 ? -3.046 8.926 8.281 1.00 9.62 ? 181 PHE A CD2 1 ATOM 1401 C CE1 . PHE A 1 181 ? -2.779 9.751 10.886 1.00 10.48 ? 181 PHE A CE1 1 ATOM 1402 C CE2 . PHE A 1 181 ? -3.883 9.920 8.796 1.00 10.70 ? 181 PHE A CE2 1 ATOM 1403 C CZ . PHE A 1 181 ? -3.750 10.307 10.099 1.00 10.65 ? 181 PHE A CZ 1 ATOM 1404 N N . ILE A 1 182 ? -1.327 4.251 7.168 1.00 8.52 ? 182 ILE A N 1 ATOM 1405 C CA . ILE A 1 182 ? -0.586 3.350 6.290 1.00 8.33 ? 182 ILE A CA 1 ATOM 1406 C C . ILE A 1 182 ? -0.813 3.853 4.873 1.00 8.58 ? 182 ILE A C 1 ATOM 1407 O O . ILE A 1 182 ? -1.960 4.118 4.502 1.00 8.77 ? 182 ILE A O 1 ATOM 1408 C CB . ILE A 1 182 ? -1.096 1.871 6.436 1.00 9.29 ? 182 ILE A CB 1 ATOM 1409 C CG1 . ILE A 1 182 ? -0.797 1.334 7.844 1.00 10.23 ? 182 ILE A CG1 1 ATOM 1410 C CG2 . ILE A 1 182 ? -0.496 0.991 5.333 1.00 9.39 ? 182 ILE A CG2 1 ATOM 1411 C CD1 . ILE A 1 182 ? -1.345 -0.055 8.139 1.00 11.03 ? 182 ILE A CD1 1 ATOM 1412 N N . ASN A 1 183 ? 0.253 4.020 4.091 1.00 8.13 ? 183 ASN A N 1 ATOM 1413 C CA . ASN A 1 183 ? 0.128 4.565 2.730 1.00 8.50 ? 183 ASN A CA 1 ATOM 1414 C C . ASN A 1 183 ? -0.591 5.915 2.759 1.00 8.38 ? 183 ASN A C 1 ATOM 1415 O O . ASN A 1 183 ? -1.322 6.275 1.850 1.00 8.76 ? 183 ASN A O 1 ATOM 1416 C CB . ASN A 1 183 ? -0.532 3.556 1.788 1.00 8.52 ? 183 ASN A CB 1 ATOM 1417 C CG . ASN A 1 183 ? 0.460 2.630 1.152 1.00 8.99 ? 183 ASN A CG 1 ATOM 1418 O OD1 . ASN A 1 183 ? 1.664 2.919 1.141 1.00 9.74 ? 183 ASN A OD1 1 ATOM 1419 N ND2 . ASN A 1 183 ? -0.031 1.549 0.564 1.00 11.51 ? 183 ASN A ND2 1 ATOM 1420 N N . GLY A 1 184 ? -0.319 6.687 3.804 1.00 8.53 ? 184 GLY A N 1 ATOM 1421 C CA . GLY A 1 184 ? -0.877 8.011 3.955 1.00 8.82 ? 184 GLY A CA 1 ATOM 1422 C C . GLY A 1 184 ? -2.359 8.058 4.240 1.00 9.32 ? 184 GLY A C 1 ATOM 1423 O O . GLY A 1 184 ? -2.945 9.140 4.140 1.00 10.80 ? 184 GLY A O 1 ATOM 1424 N N . LEU A 1 185 ? -2.956 6.931 4.620 1.00 8.74 ? 185 LEU A N 1 ATOM 1425 C CA . LEU A 1 185 ? -4.395 6.843 4.872 1.00 9.44 ? 185 LEU A CA 1 ATOM 1426 C C . LEU A 1 185 ? -4.632 6.402 6.310 1.00 9.19 ? 185 LEU A C 1 ATOM 1427 O O . LEU A 1 185 ? -3.933 5.502 6.829 1.00 9.77 ? 185 LEU A O 1 ATOM 1428 C CB . LEU A 1 185 ? -5.039 5.801 3.950 1.00 10.03 ? 185 LEU A CB 1 ATOM 1429 C CG . LEU A 1 185 ? -4.778 5.968 2.453 1.00 10.73 ? 185 LEU A CG 1 ATOM 1430 C CD1 . LEU A 1 185 ? -5.393 4.832 1.661 1.00 12.67 ? 185 LEU A CD1 1 ATOM 1431 C CD2 . LEU A 1 185 ? -5.323 7.318 2.026 1.00 11.51 ? 185 LEU A CD2 1 ATOM 1432 N N . GLY A 1 186 ? -5.648 6.986 6.946 1.00 9.61 ? 186 GLY A N 1 ATOM 1433 C CA . GLY A 1 186 ? -5.977 6.559 8.315 1.00 9.54 ? 186 GLY A CA 1 ATOM 1434 C C . GLY A 1 186 ? -6.226 5.046 8.361 1.00 9.41 ? 186 GLY A C 1 ATOM 1435 O O . GLY A 1 186 ? -6.997 4.508 7.585 1.00 10.64 ? 186 GLY A O 1 ATOM 1436 N N . ASN A 1 187 ? -5.583 4.368 9.308 1.00 9.34 ? 187 ASN A N 1 ATOM 1437 C CA . ASN A 1 187 ? -5.623 2.909 9.405 1.00 10.17 ? 187 ASN A CA 1 ATOM 1438 C C . ASN A 1 187 ? -6.744 2.528 10.389 1.00 10.17 ? 187 ASN A C 1 ATOM 1439 O O . ASN A 1 187 ? -6.509 2.085 11.513 1.00 10.64 ? 187 ASN A O 1 ATOM 1440 C CB . ASN A 1 187 ? -4.274 2.413 9.910 1.00 10.03 ? 187 ASN A CB 1 ATOM 1441 C CG . ASN A 1 187 ? -4.184 0.920 10.059 1.00 9.82 ? 187 ASN A CG 1 ATOM 1442 O OD1 . ASN A 1 187 ? -4.979 0.162 9.505 1.00 9.88 ? 187 ASN A OD1 1 ATOM 1443 N ND2 . ASN A 1 187 ? -3.204 0.496 10.850 1.00 9.74 ? 187 ASN A ND2 1 ATOM 1444 N N . ILE A 1 188 ? -7.973 2.731 9.934 1.00 11.57 ? 188 ILE A N 1 ATOM 1445 C CA . ILE A 1 188 ? -9.148 2.679 10.793 1.00 12.07 ? 188 ILE A CA 1 ATOM 1446 C C . ILE A 1 188 ? -9.294 1.321 11.458 1.00 12.61 ? 188 ILE A C 1 ATOM 1447 O O . ILE A 1 188 ? -9.679 1.238 12.631 1.00 12.92 ? 188 ILE A O 1 ATOM 1448 C CB . ILE A 1 188 ? -10.380 2.971 9.955 1.00 12.34 ? 188 ILE A CB 1 ATOM 1449 C CG1 . ILE A 1 188 ? -10.189 4.217 9.070 1.00 12.78 ? 188 ILE A CG1 1 ATOM 1450 C CG2 . ILE A 1 188 ? -11.619 3.125 10.851 1.00 13.59 ? 188 ILE A CG2 1 ATOM 1451 C CD1 . ILE A 1 188 ? -9.851 5.475 9.797 1.00 13.16 ? 188 ILE A CD1 1 ATOM 1452 N N . GLU A 1 189 ? -8.977 0.259 10.720 1.00 12.80 ? 189 GLU A N 1 ATOM 1453 C CA . GLU A 1 189 ? -9.119 -1.101 11.252 1.00 13.81 ? 189 GLU A CA 1 ATOM 1454 C C . GLU A 1 189 ? -7.896 -1.625 11.999 1.00 13.06 ? 189 GLU A C 1 ATOM 1455 O O . GLU A 1 189 ? -7.873 -2.771 12.464 1.00 13.71 ? 189 GLU A O 1 ATOM 1456 C CB . GLU A 1 189 ? -9.499 -2.069 10.130 1.00 14.32 ? 189 GLU A CB 1 ATOM 1457 C CG . GLU A 1 189 ? -10.822 -1.736 9.453 1.00 16.41 ? 189 GLU A CG 1 ATOM 1458 C CD . GLU A 1 189 ? -11.199 -2.698 8.362 1.00 19.95 ? 189 GLU A CD 1 ATOM 1459 O OE1 . GLU A 1 189 ? -11.050 -3.928 8.565 1.00 29.01 ? 189 GLU A OE1 1 ATOM 1460 O OE2 . GLU A 1 189 ? -11.656 -2.234 7.286 1.00 28.15 ? 189 GLU A OE2 1 ATOM 1461 N N . GLY A 1 190 ? -6.855 -0.814 12.129 1.00 12.12 ? 190 GLY A N 1 ATOM 1462 C CA . GLY A 1 190 ? -5.704 -1.227 12.912 1.00 11.65 ? 190 GLY A CA 1 ATOM 1463 C C . GLY A 1 190 ? -4.949 -2.403 12.289 1.00 11.34 ? 190 GLY A C 1 ATOM 1464 O O . GLY A 1 190 ? -4.471 -3.284 13.009 1.00 11.61 ? 190 GLY A O 1 ATOM 1465 N N . LYS A 1 191 ? -4.831 -2.414 10.960 1.00 10.31 ? 191 LYS A N 1 ATOM 1466 C CA . LYS A 1 191 ? -4.051 -3.425 10.229 1.00 11.04 ? 191 LYS A CA 1 ATOM 1467 C C . LYS A 1 191 ? -2.555 -3.169 10.404 1.00 10.15 ? 191 LYS A C 1 ATOM 1468 O O . LYS A 1 191 ? -2.129 -2.095 10.795 1.00 9.55 ? 191 LYS A O 1 ATOM 1469 C CB . LYS A 1 191 ? -4.437 -3.394 8.754 1.00 12.08 ? 191 LYS A CB 1 ATOM 1470 C CG . LYS A 1 191 ? -5.915 -3.705 8.565 1.00 15.14 ? 191 LYS A CG 1 ATOM 1471 C CD . LYS A 1 191 ? -6.277 -4.128 7.182 1.00 16.56 ? 191 LYS A CD 1 ATOM 1472 C CE . LYS A 1 191 ? -7.771 -4.568 7.112 1.00 18.86 ? 191 LYS A CE 1 ATOM 1473 N NZ . LYS A 1 191 ? -8.142 -4.823 5.706 1.00 21.05 ? 191 LYS A NZ 1 ATOM 1474 N N . GLY A 1 192 ? -1.756 -4.184 10.128 1.00 9.50 ? 192 GLY A N 1 ATOM 1475 C CA . GLY A 1 192 ? -0.297 -4.021 10.153 1.00 9.65 ? 192 GLY A CA 1 ATOM 1476 C C . GLY A 1 192 ? 0.246 -3.727 8.771 1.00 9.07 ? 192 GLY A C 1 ATOM 1477 O O . GLY A 1 192 ? -0.360 -4.055 7.746 1.00 9.66 ? 192 GLY A O 1 ATOM 1478 N N . SER A 1 193 ? 1.400 -3.072 8.746 1.00 8.34 ? 193 SER A N 1 ATOM 1479 C CA . SER A 1 193 ? 2.009 -2.605 7.516 1.00 8.57 ? 193 SER A CA 1 ATOM 1480 C C . SER A 1 193 ? 3.185 -3.486 7.111 1.00 8.19 ? 193 SER A C 1 ATOM 1481 O O . SER A 1 193 ? 4.294 -3.320 7.612 1.00 8.76 ? 193 SER A O 1 ATOM 1482 C CB . SER A 1 193 ? 2.461 -1.169 7.691 1.00 8.96 ? 193 SER A CB 1 ATOM 1483 O OG . SER A 1 193 ? 2.931 -0.691 6.459 1.00 9.37 ? 193 SER A OG 1 ATOM 1484 N N . CYS A 1 194 ? 2.921 -4.470 6.258 1.00 7.80 ? 194 CYS A N 1 ATOM 1485 C CA . CYS A 1 194 ? 3.872 -5.520 5.958 1.00 8.18 ? 194 CYS A CA 1 ATOM 1486 C C . CYS A 1 194 ? 4.548 -5.341 4.608 1.00 8.13 ? 194 CYS A C 1 ATOM 1487 O O . CYS A 1 194 ? 3.912 -5.023 3.605 1.00 8.76 ? 194 CYS A O 1 ATOM 1488 C CB . CYS A 1 194 ? 3.134 -6.870 5.845 1.00 8.92 ? 194 CYS A CB 1 ATOM 1489 S SG . CYS A 1 194 ? 2.126 -7.336 7.263 1.00 9.27 ? 194 CYS A SG 1 ATOM 1490 N N . CYS A 1 195 ? 5.838 -5.622 4.550 1.00 7.85 ? 195 CYS A N 1 ATOM 1491 C CA . CYS A 1 195 ? 6.512 -5.824 3.242 1.00 8.11 ? 195 CYS A CA 1 ATOM 1492 C C . CYS A 1 195 ? 7.877 -6.466 3.400 1.00 8.39 ? 195 CYS A C 1 ATOM 1493 O O . CYS A 1 195 ? 8.477 -6.436 4.470 1.00 8.52 ? 195 CYS A O 1 ATOM 1494 C CB . CYS A 1 195 ? 6.642 -4.537 2.408 1.00 8.71 ? 195 CYS A CB 1 ATOM 1495 S SG . CYS A 1 195 ? 7.612 -3.229 3.161 1.00 8.57 ? 195 CYS A SG 1 ATOM 1496 N N . ASN A 1 196 ? 8.345 -7.026 2.296 1.00 8.73 ? 196 ASN A N 1 ATOM 1497 C CA . ASN A 1 196 ? 9.681 -7.574 2.202 1.00 8.95 ? 196 ASN A CA 1 ATOM 1498 C C . ASN A 1 196 ? 10.692 -6.530 2.648 1.00 8.92 ? 196 ASN A C 1 ATOM 1499 O O . ASN A 1 196 ? 10.566 -5.351 2.310 1.00 9.19 ? 196 ASN A O 1 ATOM 1500 C CB . ASN A 1 196 ? 9.993 -7.922 0.731 1.00 10.51 ? 196 ASN A CB 1 ATOM 1501 C CG . ASN A 1 196 ? 9.332 -9.186 0.258 1.00 10.35 ? 196 ASN A CG 1 ATOM 1502 O OD1 . ASN A 1 196 ? 9.762 -10.285 0.573 1.00 12.23 ? 196 ASN A OD1 1 ATOM 1503 N ND2 . ASN A 1 196 ? 8.327 -9.043 -0.598 1.00 13.51 ? 196 ASN A ND2 1 ATOM 1504 N N . SER A 1 197 ? 11.711 -6.957 3.381 1.00 8.51 ? 197 SER A N 1 ATOM 1505 C CA . SER A 1 197 ? 12.751 -6.051 3.871 1.00 9.25 ? 197 SER A CA 1 ATOM 1506 C C . SER A 1 197 ? 14.103 -6.730 3.751 1.00 9.12 ? 197 SER A C 1 ATOM 1507 O O . SER A 1 197 ? 14.241 -7.852 4.231 1.00 10.36 ? 197 SER A O 1 ATOM 1508 C CB . SER A 1 197 ? 12.545 -5.680 5.322 1.00 11.91 ? 197 SER A CB 1 ATOM 1509 O OG . SER A 1 197 ? 11.357 -4.975 5.574 1.00 15.42 ? 197 SER A OG 1 ATOM 1510 N N . MET A 1 198 ? 15.076 -6.054 3.148 1.00 8.33 ? 198 MET A N 1 ATOM 1511 C CA . MET A 1 198 ? 16.452 -6.573 3.069 1.00 8.43 ? 198 MET A CA 1 ATOM 1512 C C . MET A 1 198 ? 17.327 -5.749 3.994 1.00 8.28 ? 198 MET A C 1 ATOM 1513 O O . MET A 1 198 ? 17.564 -4.576 3.717 1.00 8.65 ? 198 MET A O 1 ATOM 1514 C CB . MET A 1 198 ? 16.970 -6.489 1.631 1.00 8.78 ? 198 MET A CB 1 ATOM 1515 C CG . MET A 1 198 ? 18.488 -6.809 1.505 1.00 9.84 ? 198 MET A CG 1 ATOM 1516 S SD . MET A 1 198 ? 18.888 -8.472 2.044 1.00 9.51 ? 198 MET A SD 1 ATOM 1517 C CE . MET A 1 198 ? 20.571 -8.237 2.766 1.00 10.03 ? 198 MET A CE 1 ATOM 1518 N N . ASP A 1 199 ? 17.732 -6.325 5.124 1.00 8.46 ? 199 ASP A N 1 ATOM 1519 C CA . ASP A 1 199 ? 18.544 -5.573 6.069 1.00 8.63 ? 199 ASP A CA 1 ATOM 1520 C C . ASP A 1 199 ? 20.000 -5.680 5.656 1.00 8.32 ? 199 ASP A C 1 ATOM 1521 O O . ASP A 1 199 ? 20.710 -6.628 6.040 1.00 8.37 ? 199 ASP A O 1 ATOM 1522 C CB . ASP A 1 199 ? 18.327 -6.053 7.498 1.00 9.09 ? 199 ASP A CB 1 ATOM 1523 C CG . ASP A 1 199 ? 16.872 -5.965 7.931 1.00 10.31 ? 199 ASP A CG 1 ATOM 1524 O OD1 . ASP A 1 199 ? 16.009 -5.515 7.146 1.00 13.28 ? 199 ASP A OD1 1 ATOM 1525 O OD2 . ASP A 1 199 ? 16.506 -6.415 9.014 1.00 13.13 ? 199 ASP A OD2 1 ATOM 1526 N N . ILE A 1 200 ? 20.449 -4.719 4.840 1.00 8.66 ? 200 ILE A N 1 ATOM 1527 C CA . ILE A 1 200 ? 21.836 -4.658 4.413 1.00 8.38 ? 200 ILE A CA 1 ATOM 1528 C C . ILE A 1 200 ? 22.700 -4.526 5.648 1.00 7.94 ? 200 ILE A C 1 ATOM 1529 O O . ILE A 1 200 ? 23.652 -5.285 5.821 1.00 9.03 ? 200 ILE A O 1 ATOM 1530 C CB . ILE A 1 200 ? 22.037 -3.478 3.433 1.00 8.24 ? 200 ILE A CB 1 ATOM 1531 C CG1 . ILE A 1 200 ? 21.279 -3.743 2.135 1.00 8.99 ? 200 ILE A CG1 1 ATOM 1532 C CG2 . ILE A 1 200 ? 23.512 -3.236 3.145 1.00 8.97 ? 200 ILE A CG2 1 ATOM 1533 C CD1 . ILE A 1 200 ? 21.276 -2.604 1.163 1.00 10.36 ? 200 ILE A CD1 1 ATOM 1534 N N . TRP A 1 201 ? 22.351 -3.593 6.523 1.00 8.52 ? 201 TRP A N 1 ATOM 1535 C CA . TRP A 1 201 ? 23.199 -3.249 7.665 1.00 8.36 ? 201 TRP A CA 1 ATOM 1536 C C . TRP A 1 201 ? 22.345 -2.943 8.880 1.00 8.66 ? 201 TRP A C 1 ATOM 1537 O O . TRP A 1 201 ? 21.492 -2.080 8.827 1.00 8.91 ? 201 TRP A O 1 ATOM 1538 C CB . TRP A 1 201 ? 24.068 -2.043 7.270 1.00 8.99 ? 201 TRP A CB 1 ATOM 1539 C CG . TRP A 1 201 ? 24.716 -1.209 8.362 1.00 8.83 ? 201 TRP A CG 1 ATOM 1540 C CD1 . TRP A 1 201 ? 24.152 -0.156 8.992 1.00 9.43 ? 201 TRP A CD1 1 ATOM 1541 C CD2 . TRP A 1 201 ? 26.079 -1.280 8.862 1.00 8.80 ? 201 TRP A CD2 1 ATOM 1542 N NE1 . TRP A 1 201 ? 25.038 0.400 9.883 1.00 9.44 ? 201 TRP A NE1 1 ATOM 1543 C CE2 . TRP A 1 201 ? 26.236 -0.248 9.800 1.00 8.95 ? 201 TRP A CE2 1 ATOM 1544 C CE3 . TRP A 1 201 ? 27.167 -2.118 8.618 1.00 10.01 ? 201 TRP A CE3 1 ATOM 1545 C CZ2 . TRP A 1 201 ? 27.408 -0.046 10.512 1.00 9.18 ? 201 TRP A CZ2 1 ATOM 1546 C CZ3 . TRP A 1 201 ? 28.349 -1.903 9.337 1.00 10.33 ? 201 TRP A CZ3 1 ATOM 1547 C CH2 . TRP A 1 201 ? 28.452 -0.868 10.244 1.00 10.42 ? 201 TRP A CH2 1 ATOM 1548 N N . GLU A 1 202 ? 22.579 -3.687 9.956 1.00 8.72 ? 202 GLU A N 1 ATOM 1549 C CA . GLU A 1 202 ? 22.106 -3.349 11.296 1.00 8.44 ? 202 GLU A CA 1 ATOM 1550 C C . GLU A 1 202 ? 23.325 -3.575 12.169 1.00 8.95 ? 202 GLU A C 1 ATOM 1551 O O . GLU A 1 202 ? 23.816 -4.705 12.263 1.00 9.51 ? 202 GLU A O 1 ATOM 1552 C CB . GLU A 1 202 ? 20.932 -4.229 11.743 1.00 8.44 ? 202 GLU A CB 1 ATOM 1553 C CG . GLU A 1 202 ? 19.646 -3.989 10.943 1.00 9.08 ? 202 GLU A CG 1 ATOM 1554 C CD . GLU A 1 202 ? 18.526 -4.879 11.400 1.00 10.69 ? 202 GLU A CD 1 ATOM 1555 O OE1 . GLU A 1 202 ? 17.767 -4.440 12.303 1.00 10.64 ? 202 GLU A OE1 1 ATOM 1556 O OE2 . GLU A 1 202 ? 18.429 -6.003 10.840 1.00 11.17 ? 202 GLU A OE2 1 ATOM 1557 N N . ALA A 1 203 ? 23.855 -2.511 12.752 1.00 8.94 ? 203 ALA A N 1 ATOM 1558 C CA . ALA A 1 203 ? 25.146 -2.640 13.400 1.00 9.12 ? 203 ALA A CA 1 ATOM 1559 C C . ALA A 1 203 ? 25.428 -1.538 14.385 1.00 9.48 ? 203 ALA A C 1 ATOM 1560 O O . ALA A 1 203 ? 24.840 -0.446 14.347 1.00 9.62 ? 203 ALA A O 1 ATOM 1561 C CB . ALA A 1 203 ? 26.259 -2.695 12.339 1.00 10.11 ? 203 ALA A CB 1 ATOM 1562 N N . ASN A 1 204 ? 26.393 -1.814 15.257 1.00 9.59 ? 204 ASN A N 1 ATOM 1563 C CA . ASN A 1 204 ? 26.994 -0.810 16.111 1.00 10.17 ? 204 ASN A CA 1 ATOM 1564 C C . ASN A 1 204 ? 28.486 -1.073 16.114 1.00 10.52 ? 204 ASN A C 1 ATOM 1565 O O . ASN A 1 204 ? 28.991 -1.785 15.238 1.00 10.95 ? 204 ASN A O 1 ATOM 1566 C CB . ASN A 1 204 ? 26.338 -0.821 17.494 1.00 10.24 ? 204 ASN A CB 1 ATOM 1567 C CG . ASN A 1 204 ? 26.365 -2.169 18.156 1.00 9.79 ? 204 ASN A CG 1 ATOM 1568 O OD1 . ASN A 1 204 ? 27.375 -2.867 18.114 1.00 10.52 ? 204 ASN A OD1 1 ATOM 1569 N ND2 . ASN A 1 204 ? 25.273 -2.516 18.841 1.00 9.74 ? 204 ASN A ND2 1 ATOM 1570 N N . SER A 1 205 ? 29.224 -0.492 17.058 1.00 10.10 ? 205 SER A N 1 ATOM 1571 C CA . SER A 1 205 ? 30.689 -0.686 17.054 1.00 10.74 ? 205 SER A CA 1 ATOM 1572 C C . SER A 1 205 ? 31.113 -2.054 17.594 1.00 11.18 ? 205 SER A C 1 ATOM 1573 O O . SER A 1 205 ? 32.294 -2.382 17.544 1.00 11.06 ? 205 SER A O 1 ATOM 1574 C CB . SER A 1 205 ? 31.397 0.443 17.828 1.00 11.18 ? 205 SER A CB 1 ATOM 1575 O OG . SER A 1 205 ? 31.141 0.381 19.225 1.00 11.30 ? 205 SER A OG 1 ATOM 1576 N N . ARG A 1 206 ? 30.160 -2.819 18.120 1.00 10.72 ? 206 ARG A N 1 ATOM 1577 C CA . ARG A 1 206 ? 30.431 -4.102 18.736 1.00 10.95 ? 206 ARG A CA 1 ATOM 1578 C C . ARG A 1 206 ? 29.992 -5.309 17.882 1.00 10.48 ? 206 ARG A C 1 ATOM 1579 O O . ARG A 1 206 ? 30.490 -6.408 18.078 1.00 11.37 ? 206 ARG A O 1 ATOM 1580 C CB . ARG A 1 206 ? 29.726 -4.184 20.093 1.00 10.16 ? 206 ARG A CB 1 ATOM 1581 C CG . ARG A 1 206 ? 29.900 -2.942 20.971 1.00 10.95 ? 206 ARG A CG 1 ATOM 1582 C CD . ARG A 1 206 ? 31.357 -2.517 21.210 1.00 12.51 ? 206 ARG A CD 1 ATOM 1583 N NE . ARG A 1 206 ? 32.177 -3.543 21.847 1.00 12.76 ? 206 ARG A NE 1 ATOM 1584 C CZ . ARG A 1 206 ? 32.157 -3.803 23.152 1.00 13.09 ? 206 ARG A CZ 1 ATOM 1585 N NH1 . ARG A 1 206 ? 31.365 -3.124 23.969 1.00 14.30 ? 206 ARG A NH1 1 ATOM 1586 N NH2 . ARG A 1 206 ? 32.953 -4.767 23.647 1.00 13.63 ? 206 ARG A NH2 1 ATOM 1587 N N . ALA A 1 207 ? 29.014 -5.136 16.988 1.00 10.01 ? 207 ALA A N 1 ATOM 1588 C CA . ALA A 1 207 ? 28.509 -6.236 16.164 1.00 10.37 ? 207 ALA A CA 1 ATOM 1589 C C . ALA A 1 207 ? 27.927 -5.705 14.877 1.00 10.11 ? 207 ALA A C 1 ATOM 1590 O O . ALA A 1 207 ? 27.411 -4.584 14.803 1.00 10.14 ? 207 ALA A O 1 ATOM 1591 C CB . ALA A 1 207 ? 27.459 -7.006 16.913 1.00 10.69 ? 207 ALA A CB 1 ATOM 1592 N N . SER A 1 208 ? 28.033 -6.540 13.854 1.00 9.37 ? 208 SER A N 1 ATOM 1593 C CA . SER A 1 208 ? 27.522 -6.267 12.518 1.00 9.69 ? 208 SER A CA 1 ATOM 1594 C C . SER A 1 208 ? 26.644 -7.418 12.017 1.00 9.57 ? 208 SER A C 1 ATOM 1595 O O . SER A 1 208 ? 27.082 -8.557 11.930 1.00 10.14 ? 208 SER A O 1 ATOM 1596 C CB . SER A 1 208 ? 28.675 -6.029 11.560 1.00 9.99 ? 208 SER A CB 1 ATOM 1597 O OG . SER A 1 208 ? 28.242 -5.844 10.212 1.00 9.89 ? 208 SER A OG 1 ATOM 1598 N N . HIS A 1 209 ? 25.400 -7.087 11.674 1.00 9.29 ? 209 HIS A N 1 ATOM 1599 C CA . HIS A 1 209 ? 24.375 -8.052 11.280 1.00 9.21 ? 209 HIS A CA 1 ATOM 1600 C C . HIS A 1 209 ? 23.811 -7.720 9.896 1.00 8.83 ? 209 HIS A C 1 ATOM 1601 O O . HIS A 1 209 ? 23.579 -6.546 9.564 1.00 8.85 ? 209 HIS A O 1 ATOM 1602 C CB . HIS A 1 209 ? 23.302 -7.962 12.352 1.00 9.09 ? 209 HIS A CB 1 ATOM 1603 C CG . HIS A 1 209 ? 22.094 -8.799 12.136 1.00 10.36 ? 209 HIS A CG 1 ATOM 1604 N ND1 . HIS A 1 209 ? 21.918 -10.006 12.773 1.00 12.06 ? 209 HIS A ND1 1 ATOM 1605 C CD2 . HIS A 1 209 ? 20.939 -8.541 11.475 1.00 11.92 ? 209 HIS A CD2 1 ATOM 1606 C CE1 . HIS A 1 209 ? 20.722 -10.483 12.467 1.00 13.04 ? 209 HIS A CE1 1 ATOM 1607 N NE2 . HIS A 1 209 ? 20.110 -9.621 11.677 1.00 11.90 ? 209 HIS A NE2 1 ATOM 1608 N N . VAL A 1 210 ? 23.626 -8.752 9.075 1.00 8.11 ? 210 VAL A N 1 ATOM 1609 C CA . VAL A 1 210 ? 22.969 -8.669 7.782 1.00 8.68 ? 210 VAL A CA 1 ATOM 1610 C C . VAL A 1 210 ? 21.811 -9.650 7.799 1.00 8.89 ? 210 VAL A C 1 ATOM 1611 O O . VAL A 1 210 ? 21.970 -10.743 8.296 1.00 9.09 ? 210 VAL A O 1 ATOM 1612 C CB . VAL A 1 210 ? 23.943 -9.059 6.646 1.00 8.83 ? 210 VAL A CB 1 ATOM 1613 C CG1 . VAL A 1 210 ? 23.280 -8.934 5.281 1.00 8.94 ? 210 VAL A CG1 1 ATOM 1614 C CG2 . VAL A 1 210 ? 25.246 -8.210 6.713 1.00 9.43 ? 210 VAL A CG2 1 ATOM 1615 N N . ALA A 1 211 ? 20.639 -9.295 7.253 1.00 8.29 ? 211 ALA A N 1 ATOM 1616 C CA . ALA A 1 211 ? 19.517 -10.252 7.215 1.00 8.59 ? 211 ALA A CA 1 ATOM 1617 C C . ALA A 1 211 ? 18.495 -9.926 6.161 1.00 8.17 ? 211 ALA A C 1 ATOM 1618 O O . ALA A 1 211 ? 17.818 -8.897 6.289 1.00 8.28 ? 211 ALA A O 1 ATOM 1619 C CB . ALA A 1 211 ? 18.818 -10.312 8.553 1.00 9.50 ? 211 ALA A CB 1 ATOM 1620 N N . PRO A 1 212 ? 18.283 -10.820 5.195 1.00 8.06 ? 212 PRO A N 1 ATOM 1621 C CA . PRO A 1 212 ? 17.081 -10.738 4.383 1.00 8.45 ? 212 PRO A CA 1 ATOM 1622 C C . PRO A 1 212 ? 15.852 -11.208 5.170 1.00 8.86 ? 212 PRO A C 1 ATOM 1623 O O . PRO A 1 212 ? 15.966 -12.159 5.942 1.00 8.95 ? 212 PRO A O 1 ATOM 1624 C CB . PRO A 1 212 ? 17.380 -11.669 3.206 1.00 7.78 ? 212 PRO A CB 1 ATOM 1625 C CG . PRO A 1 212 ? 18.339 -12.703 3.768 1.00 9.37 ? 212 PRO A CG 1 ATOM 1626 C CD . PRO A 1 212 ? 19.152 -11.947 4.774 1.00 8.62 ? 212 PRO A CD 1 ATOM 1627 N N . HIS A 1 213 ? 14.703 -10.556 4.951 1.00 8.38 ? 213 HIS A N 1 ATOM 1628 C CA . HIS A 1 213 ? 13.407 -10.952 5.543 1.00 8.53 ? 213 HIS A CA 1 ATOM 1629 C C . HIS A 1 213 ? 12.378 -11.059 4.424 1.00 8.54 ? 213 HIS A C 1 ATOM 1630 O O . HIS A 1 213 ? 12.022 -10.031 3.828 1.00 9.79 ? 213 HIS A O 1 ATOM 1631 C CB . HIS A 1 213 ? 12.881 -9.904 6.520 1.00 8.60 ? 213 HIS A CB 1 ATOM 1632 C CG . HIS A 1 213 ? 13.709 -9.681 7.742 1.00 8.93 ? 213 HIS A CG 1 ATOM 1633 N ND1 . HIS A 1 213 ? 13.250 -9.974 9.011 1.00 9.63 ? 213 HIS A ND1 1 ATOM 1634 C CD2 . HIS A 1 213 ? 14.909 -9.072 7.917 1.00 9.44 ? 213 HIS A CD2 1 ATOM 1635 C CE1 . HIS A 1 213 ? 14.144 -9.578 9.906 1.00 9.71 ? 213 HIS A CE1 1 ATOM 1636 N NE2 . HIS A 1 213 ? 15.175 -9.062 9.267 1.00 10.18 ? 213 HIS A NE2 1 ATOM 1637 N N . THR A 1 214 ? 11.889 -12.272 4.130 1.00 7.75 ? 214 THR A N 1 ATOM 1638 C CA . THR A 1 214 ? 10.901 -12.464 3.079 1.00 9.18 ? 214 THR A CA 1 ATOM 1639 C C . THR A 1 214 ? 9.469 -12.314 3.582 1.00 8.87 ? 214 THR A C 1 ATOM 1640 O O . THR A 1 214 ? 9.173 -12.572 4.752 1.00 9.87 ? 214 THR A O 1 ATOM 1641 C CB . THR A 1 214 ? 11.026 -13.836 2.476 1.00 8.95 ? 214 THR A CB 1 ATOM 1642 O OG1 . THR A 1 214 ? 11.151 -14.796 3.540 1.00 9.00 ? 214 THR A OG1 1 ATOM 1643 C CG2 . THR A 1 214 ? 12.292 -13.963 1.627 1.00 10.41 ? 214 THR A CG2 1 ATOM 1644 N N . CYS A 1 215 ? 8.588 -11.909 2.666 1.00 8.68 ? 215 CYS A N 1 ATOM 1645 C CA . CYS A 1 215 ? 7.155 -12.003 2.864 1.00 9.16 ? 215 CYS A CA 1 ATOM 1646 C C . CYS A 1 215 ? 6.547 -12.705 1.648 1.00 9.75 ? 215 CYS A C 1 ATOM 1647 O O . CYS A 1 215 ? 7.079 -12.612 0.549 1.00 9.93 ? 215 CYS A O 1 ATOM 1648 C CB . CYS A 1 215 ? 6.510 -10.629 3.026 1.00 9.65 ? 215 CYS A CB 1 ATOM 1649 S SG . CYS A 1 215 ? 7.212 -9.614 4.325 1.00 9.65 ? 215 CYS A SG 1 ATOM 1650 N N . ASN A 1 216 ? 5.382 -13.329 1.822 1.00 9.76 ? 216 ASN A N 1 ATOM 1651 C CA . ASN A 1 216 ? 4.711 -14.012 0.686 1.00 9.83 ? 216 ASN A CA 1 ATOM 1652 C C . ASN A 1 216 ? 3.715 -13.118 -0.051 1.00 10.55 ? 216 ASN A C 1 ATOM 1653 O O . ASN A 1 216 ? 2.813 -13.613 -0.729 1.00 11.64 ? 216 ASN A O 1 ATOM 1654 C CB . ASN A 1 216 ? 4.040 -15.339 1.127 1.00 10.17 ? 216 ASN A CB 1 ATOM 1655 C CG . ASN A 1 216 ? 2.919 -15.148 2.106 1.00 10.97 ? 216 ASN A CG 1 ATOM 1656 O OD1 . ASN A 1 216 ? 2.479 -14.036 2.375 1.00 10.66 ? 216 ASN A OD1 1 ATOM 1657 N ND2 . ASN A 1 216 ? 2.439 -16.264 2.663 1.00 14.36 ? 216 ASN A ND2 1 ATOM 1658 N N . LYS A 1 217 ? 3.880 -11.811 0.129 1.00 11.05 ? 217 LYS A N 1 ATOM 1659 C CA . LYS A 1 217 ? 3.076 -10.773 -0.507 1.00 10.92 ? 217 LYS A CA 1 ATOM 1660 C C . LYS A 1 217 ? 4.014 -9.779 -1.167 1.00 10.96 ? 217 LYS A C 1 ATOM 1661 O O . LYS A 1 217 ? 5.102 -9.515 -0.621 1.00 13.00 ? 217 LYS A O 1 ATOM 1662 C CB . LYS A 1 217 ? 2.196 -10.048 0.514 1.00 11.80 ? 217 LYS A CB 1 ATOM 1663 C CG . LYS A 1 217 ? 1.244 -10.952 1.257 1.00 13.41 ? 217 LYS A CG 1 ATOM 1664 C CD . LYS A 1 217 ? 0.189 -11.545 0.354 1.00 14.66 ? 217 LYS A CD 1 ATOM 1665 C CE . LYS A 1 217 ? -0.784 -12.468 1.081 1.00 15.11 ? 217 LYS A CE 1 ATOM 1666 N NZ . LYS A 1 217 ? -0.170 -13.828 1.319 1.00 19.71 ? 217 LYS A NZ 1 ATOM 1667 N N . LYS A 1 218 ? 3.611 -9.218 -2.309 1.00 10.41 ? 218 LYS A N 1 ATOM 1668 C CA . LYS A 1 218 ? 4.375 -8.208 -3.031 1.00 9.61 ? 218 LYS A CA 1 ATOM 1669 C C . LYS A 1 218 ? 4.029 -6.807 -2.582 1.00 9.53 ? 218 LYS A C 1 ATOM 1670 O O . LYS A 1 218 ? 2.858 -6.453 -2.493 1.00 11.26 ? 218 LYS A O 1 ATOM 1671 C CB . LYS A 1 218 ? 4.107 -8.309 -4.529 1.00 9.93 ? 218 LYS A CB 1 ATOM 1672 C CG . LYS A 1 218 ? 4.413 -9.683 -5.110 1.00 10.32 ? 218 LYS A CG 1 ATOM 1673 C CD . LYS A 1 218 ? 4.224 -9.668 -6.609 1.00 10.69 ? 218 LYS A CD 1 ATOM 1674 C CE . LYS A 1 218 ? 4.368 -11.080 -7.178 1.00 11.98 ? 218 LYS A CE 1 ATOM 1675 N NZ . LYS A 1 218 ? 4.127 -11.054 -8.653 1.00 14.35 ? 218 LYS A NZ 1 ATOM 1676 N N . GLY A 1 219 ? 5.047 -5.978 -2.373 1.00 9.36 ? 219 GLY A N 1 ATOM 1677 C CA . GLY A 1 219 ? 4.827 -4.591 -1.903 1.00 9.05 ? 219 GLY A CA 1 ATOM 1678 C C . GLY A 1 219 ? 4.153 -4.546 -0.558 1.00 8.86 ? 219 GLY A C 1 ATOM 1679 O O . GLY A 1 219 ? 4.208 -5.497 0.216 1.00 10.52 ? 219 GLY A O 1 ATOM 1680 N N . LEU A 1 220 ? 3.524 -3.426 -0.245 1.00 9.24 ? 220 LEU A N 1 ATOM 1681 C CA . LEU A 1 220 ? 2.884 -3.240 1.028 1.00 8.91 ? 220 LEU A CA 1 ATOM 1682 C C . LEU A 1 220 ? 1.570 -4.008 1.115 1.00 8.98 ? 220 LEU A C 1 ATOM 1683 O O . LEU A 1 220 ? 0.679 -3.836 0.280 1.00 9.95 ? 220 LEU A O 1 ATOM 1684 C CB . LEU A 1 220 ? 2.680 -1.739 1.291 1.00 8.80 ? 220 LEU A CB 1 ATOM 1685 C CG . LEU A 1 220 ? 2.339 -1.366 2.733 1.00 9.34 ? 220 LEU A CG 1 ATOM 1686 C CD1 . LEU A 1 220 ? 2.722 0.086 3.017 1.00 8.91 ? 220 LEU A CD1 1 ATOM 1687 C CD2 . LEU A 1 220 ? 0.887 -1.599 3.035 1.00 11.06 ? 220 LEU A CD2 1 ATOM 1688 N N . TYR A 1 221 ? 1.477 -4.872 2.119 1.00 9.39 ? 221 TYR A N 1 ATOM 1689 C CA . TYR A 1 221 ? 0.271 -5.641 2.384 1.00 8.97 ? 221 TYR A CA 1 ATOM 1690 C C . TYR A 1 221 ? -0.258 -5.289 3.757 1.00 9.28 ? 221 TYR A C 1 ATOM 1691 O O . TYR A 1 221 ? 0.464 -5.325 4.732 1.00 9.26 ? 221 TYR A O 1 ATOM 1692 C CB . TYR A 1 221 ? 0.599 -7.134 2.338 1.00 9.49 ? 221 TYR A CB 1 ATOM 1693 C CG . TYR A 1 221 ? -0.590 -8.054 2.493 1.00 10.05 ? 221 TYR A CG 1 ATOM 1694 C CD1 . TYR A 1 221 ? -1.420 -8.322 1.413 1.00 11.87 ? 221 TYR A CD1 1 ATOM 1695 C CD2 . TYR A 1 221 ? -0.890 -8.642 3.705 1.00 10.39 ? 221 TYR A CD2 1 ATOM 1696 C CE1 . TYR A 1 221 ? -2.490 -9.198 1.523 1.00 12.31 ? 221 TYR A CE1 1 ATOM 1697 C CE2 . TYR A 1 221 ? -1.966 -9.487 3.828 1.00 11.36 ? 221 TYR A CE2 1 ATOM 1698 C CZ . TYR A 1 221 ? -2.768 -9.766 2.729 1.00 12.57 ? 221 TYR A CZ 1 ATOM 1699 O OH . TYR A 1 221 ? -3.846 -10.649 2.805 1.00 14.85 ? 221 TYR A OH 1 ATOM 1700 N N . LEU A 1 222 ? -1.516 -4.906 3.819 1.00 10.01 ? 222 LEU A N 1 ATOM 1701 C CA . LEU A 1 222 ? -2.174 -4.614 5.079 1.00 10.41 ? 222 LEU A CA 1 ATOM 1702 C C . LEU A 1 222 ? -2.696 -5.903 5.680 1.00 10.54 ? 222 LEU A C 1 ATOM 1703 O O . LEU A 1 222 ? -3.635 -6.502 5.175 1.00 11.93 ? 222 LEU A O 1 ATOM 1704 C CB . LEU A 1 222 ? -3.316 -3.605 4.898 1.00 10.66 ? 222 LEU A CB 1 ATOM 1705 C CG . LEU A 1 222 ? -2.867 -2.145 4.661 1.00 12.60 ? 222 LEU A CG 1 ATOM 1706 C CD1 . LEU A 1 222 ? -2.635 -1.884 3.186 1.00 15.19 ? 222 LEU A CD1 1 ATOM 1707 C CD2 . LEU A 1 222 ? -3.863 -1.164 5.205 1.00 13.34 ? 222 LEU A CD2 1 ATOM 1708 N N . CYS A 1 223 ? -2.043 -6.357 6.740 1.00 10.04 ? 223 CYS A N 1 ATOM 1709 C CA . CYS A 1 223 ? -2.398 -7.645 7.351 1.00 10.53 ? 223 CYS A CA 1 ATOM 1710 C C . CYS A 1 223 ? -3.474 -7.491 8.401 1.00 11.40 ? 223 CYS A C 1 ATOM 1711 O O . CYS A 1 223 ? -3.549 -6.480 9.098 1.00 10.88 ? 223 CYS A O 1 ATOM 1712 C CB . CYS A 1 223 ? -1.147 -8.307 7.960 1.00 9.90 ? 223 CYS A CB 1 ATOM 1713 S SG . CYS A 1 223 ? -0.376 -7.377 9.308 1.00 9.91 ? 223 CYS A SG 1 ATOM 1714 N N . GLU A 1 224 ? -4.242 -8.560 8.590 1.00 11.86 ? 224 GLU A N 1 ATOM 1715 C CA . GLU A 1 224 ? -5.159 -8.616 9.722 1.00 14.29 ? 224 GLU A CA 1 ATOM 1716 C C . GLU A 1 224 ? -4.983 -9.890 10.534 1.00 14.07 ? 224 GLU A C 1 ATOM 1717 O O . GLU A 1 224 ? -4.647 -10.936 9.997 1.00 13.59 ? 224 GLU A O 1 ATOM 1718 C CB . GLU A 1 224 ? -6.605 -8.425 9.282 1.00 16.83 ? 224 GLU A CB 1 ATOM 1719 C CG . GLU A 1 224 ? -7.156 -9.383 8.288 1.00 20.05 ? 224 GLU A CG 1 ATOM 1720 C CD . GLU A 1 224 ? -8.588 -9.010 7.835 1.00 21.86 ? 224 GLU A CD 1 ATOM 1721 O OE1 . GLU A 1 224 ? -9.183 -8.056 8.382 1.00 28.59 ? 224 GLU A OE1 1 ATOM 1722 O OE2 . GLU A 1 224 ? -9.091 -9.660 6.899 1.00 31.49 ? 224 GLU A OE2 1 ATOM 1723 N N . GLY A 1 225 ? -5.144 -9.764 11.839 1.00 13.93 ? 225 GLY A N 1 ATOM 1724 C CA . GLY A 1 225 ? -5.137 -10.918 12.732 1.00 14.66 ? 225 GLY A CA 1 ATOM 1725 C C . GLY A 1 225 ? -3.876 -11.718 12.587 1.00 14.49 ? 225 GLY A C 1 ATOM 1726 O O . GLY A 1 225 ? -2.792 -11.176 12.664 1.00 14.25 ? 225 GLY A O 1 ATOM 1727 N N . GLU A 1 226 ? -4.026 -13.016 12.356 1.00 15.58 ? 226 GLU A N 1 ATOM 1728 C CA . GLU A 1 226 ? -2.906 -13.920 12.323 1.00 16.11 ? 226 GLU A CA 1 ATOM 1729 C C . GLU A 1 226 ? -1.940 -13.655 11.163 1.00 14.37 ? 226 GLU A C 1 ATOM 1730 O O . GLU A 1 226 ? -0.778 -14.077 11.209 1.00 12.97 ? 226 GLU A O 1 ATOM 1731 C CB . GLU A 1 226 ? -3.395 -15.365 12.313 1.00 18.40 ? 226 GLU A CB 1 ATOM 1732 C CG . GLU A 1 226 ? -3.780 -15.798 13.728 1.00 24.16 ? 226 GLU A CG 1 ATOM 1733 C CD . GLU A 1 226 ? -2.558 -15.918 14.642 1.00 30.48 ? 226 GLU A CD 1 ATOM 1734 O OE1 . GLU A 1 226 ? -1.515 -16.429 14.178 1.00 34.92 ? 226 GLU A OE1 1 ATOM 1735 O OE2 . GLU A 1 226 ? -2.600 -15.487 15.823 1.00 35.88 ? 226 GLU A OE2 1 ATOM 1736 N N . GLU A 1 227 ? -2.396 -12.952 10.137 1.00 12.58 ? 227 GLU A N 1 ATOM 1737 C CA . GLU A 1 227 ? -1.495 -12.575 9.042 1.00 11.87 ? 227 GLU A CA 1 ATOM 1738 C C . GLU A 1 227 ? -0.328 -11.733 9.528 1.00 11.15 ? 227 GLU A C 1 ATOM 1739 O O . GLU A 1 227 ? 0.733 -11.765 8.921 1.00 10.99 ? 227 GLU A O 1 ATOM 1740 C CB . GLU A 1 227 ? -2.244 -11.780 7.967 1.00 12.19 ? 227 GLU A CB 1 ATOM 1741 C CG . GLU A 1 227 ? -3.328 -12.543 7.234 1.00 13.35 ? 227 GLU A CG 1 ATOM 1742 C CD . GLU A 1 227 ? -3.904 -11.713 6.101 1.00 13.28 ? 227 GLU A CD 1 ATOM 1743 O OE1 . GLU A 1 227 ? -4.225 -10.543 6.383 1.00 13.99 ? 227 GLU A OE1 1 ATOM 1744 O OE2 . GLU A 1 227 ? -3.973 -12.206 4.939 1.00 16.72 ? 227 GLU A OE2 1 ATOM 1745 N N . CYS A 1 228 ? -0.536 -10.962 10.593 1.00 10.27 ? 228 CYS A N 1 ATOM 1746 C CA . CYS A 1 228 ? 0.494 -10.089 11.151 1.00 10.54 ? 228 CYS A CA 1 ATOM 1747 C C . CYS A 1 228 ? 1.447 -10.786 12.103 1.00 11.09 ? 228 CYS A C 1 ATOM 1748 O O . CYS A 1 228 ? 2.447 -10.199 12.520 1.00 11.28 ? 228 CYS A O 1 ATOM 1749 C CB . CYS A 1 228 ? -0.137 -8.929 11.915 1.00 10.26 ? 228 CYS A CB 1 ATOM 1750 S SG . CYS A 1 228 ? -1.377 -7.967 11.018 1.00 11.52 ? 228 CYS A SG 1 ATOM 1751 N N . ALA A 1 229 ? 1.140 -12.037 12.439 1.00 11.32 ? 229 ALA A N 1 ATOM 1752 C CA . ALA A 1 229 ? 1.852 -12.775 13.472 1.00 11.37 ? 229 ALA A CA 1 ATOM 1753 C C . ALA A 1 229 ? 3.002 -13.634 12.921 1.00 11.53 ? 229 ALA A C 1 ATOM 1754 O O . ALA A 1 229 ? 3.306 -13.621 11.730 1.00 10.68 ? 229 ALA A O 1 ATOM 1755 C CB . ALA A 1 229 ? 0.858 -13.607 14.262 1.00 12.53 ? 229 ALA A CB 1 ATOM 1756 N N . PHE A 1 230 ? 3.642 -14.395 13.799 1.00 11.72 ? 230 PHE A N 1 ATOM 1757 C CA . PHE A 1 230 ? 4.859 -15.109 13.422 1.00 11.40 ? 230 PHE A CA 1 ATOM 1758 C C . PHE A 1 230 ? 4.618 -16.116 12.305 1.00 10.55 ? 230 PHE A C 1 ATOM 1759 O O . PHE A 1 230 ? 5.494 -16.280 11.438 1.00 10.16 ? 230 PHE A O 1 ATOM 1760 C CB . PHE A 1 230 ? 5.446 -15.830 14.628 1.00 11.96 ? 230 PHE A CB 1 ATOM 1761 C CG . PHE A 1 230 ? 6.758 -16.470 14.362 1.00 12.06 ? 230 PHE A CG 1 ATOM 1762 C CD1 . PHE A 1 230 ? 7.927 -15.734 14.475 1.00 12.99 ? 230 PHE A CD1 1 ATOM 1763 C CD2 . PHE A 1 230 ? 6.825 -17.805 13.995 1.00 12.61 ? 230 PHE A CD2 1 ATOM 1764 C CE1 . PHE A 1 230 ? 9.144 -16.321 14.252 1.00 15.05 ? 230 PHE A CE1 1 ATOM 1765 C CE2 . PHE A 1 230 ? 8.052 -18.394 13.749 1.00 13.64 ? 230 PHE A CE2 1 ATOM 1766 C CZ . PHE A 1 230 ? 9.202 -17.652 13.861 1.00 13.17 ? 230 PHE A CZ 1 ATOM 1767 N N . GLU A 1 231 ? 3.467 -16.808 12.307 1.00 10.88 ? 231 GLU A N 1 ATOM 1768 C CA . GLU A 1 231 ? 3.141 -17.758 11.225 1.00 11.72 ? 231 GLU A CA 1 ATOM 1769 C C . GLU A 1 231 ? 2.330 -17.135 10.096 1.00 11.76 ? 231 GLU A C 1 ATOM 1770 O O . GLU A 1 231 ? 1.649 -17.821 9.328 1.00 12.47 ? 231 GLU A O 1 ATOM 1771 C CB . GLU A 1 231 ? 2.408 -18.977 11.766 1.00 12.39 ? 231 GLU A CB 1 ATOM 1772 C CG . GLU A 1 231 ? 3.172 -19.757 12.830 1.00 12.65 ? 231 GLU A CG 1 ATOM 1773 C CD . GLU A 1 231 ? 4.390 -20.504 12.347 1.00 13.37 ? 231 GLU A CD 1 ATOM 1774 O OE1 . GLU A 1 231 ? 4.647 -20.614 11.130 1.00 13.29 ? 231 GLU A OE1 1 ATOM 1775 O OE2 . GLU A 1 231 ? 5.075 -21.060 13.218 1.00 16.08 ? 231 GLU A OE2 1 ATOM 1776 N N . GLY A 1 232 ? 2.431 -15.809 9.962 1.00 10.42 ? 232 GLY A N 1 ATOM 1777 C CA . GLY A 1 232 ? 1.691 -15.044 8.977 1.00 10.67 ? 232 GLY A CA 1 ATOM 1778 C C . GLY A 1 232 ? 2.459 -14.789 7.682 1.00 9.72 ? 232 GLY A C 1 ATOM 1779 O O . GLY A 1 232 ? 3.150 -15.667 7.151 1.00 11.01 ? 232 GLY A O 1 ATOM 1780 N N . VAL A 1 233 ? 2.308 -13.576 7.149 1.00 9.57 ? 233 VAL A N 1 ATOM 1781 C CA . VAL A 1 233 ? 2.785 -13.280 5.803 1.00 9.49 ? 233 VAL A CA 1 ATOM 1782 C C . VAL A 1 233 ? 4.253 -12.846 5.708 1.00 9.29 ? 233 VAL A C 1 ATOM 1783 O O . VAL A 1 233 ? 4.825 -12.873 4.611 1.00 9.21 ? 233 VAL A O 1 ATOM 1784 C CB . VAL A 1 233 ? 1.871 -12.229 5.094 1.00 9.51 ? 233 VAL A CB 1 ATOM 1785 C CG1 . VAL A 1 233 ? 0.416 -12.741 5.031 1.00 11.80 ? 233 VAL A CG1 1 ATOM 1786 C CG2 . VAL A 1 233 ? 1.948 -10.871 5.771 1.00 9.90 ? 233 VAL A CG2 1 ATOM 1787 N N . CYS A 1 234 ? 4.852 -12.427 6.823 1.00 9.24 ? 234 CYS A N 1 ATOM 1788 C CA . CYS A 1 234 ? 6.221 -11.950 6.810 1.00 8.41 ? 234 CYS A CA 1 ATOM 1789 C C . CYS A 1 234 ? 7.106 -12.661 7.831 1.00 9.04 ? 234 CYS A C 1 ATOM 1790 O O . CYS A 1 234 ? 6.659 -13.130 8.889 1.00 9.97 ? 234 CYS A O 1 ATOM 1791 C CB . CYS A 1 234 ? 6.281 -10.446 7.076 1.00 9.18 ? 234 CYS A CB 1 ATOM 1792 S SG . CYS A 1 234 ? 5.769 -9.386 5.725 1.00 9.27 ? 234 CYS A SG 1 ATOM 1793 N N . ASP A 1 235 ? 8.376 -12.712 7.460 1.00 8.79 ? 235 ASP A N 1 ATOM 1794 C CA . ASP A 1 235 ? 9.469 -13.312 8.248 1.00 8.78 ? 235 ASP A CA 1 ATOM 1795 C C . ASP A 1 235 ? 10.058 -12.297 9.217 1.00 8.78 ? 235 ASP A C 1 ATOM 1796 O O . ASP A 1 235 ? 10.886 -11.450 8.861 1.00 9.12 ? 235 ASP A O 1 ATOM 1797 C CB . ASP A 1 235 ? 10.524 -13.813 7.262 1.00 8.84 ? 235 ASP A CB 1 ATOM 1798 C CG . ASP A 1 235 ? 11.829 -14.179 7.885 1.00 9.01 ? 235 ASP A CG 1 ATOM 1799 O OD1 . ASP A 1 235 ? 11.861 -14.623 9.079 1.00 9.43 ? 235 ASP A OD1 1 ATOM 1800 O OD2 . ASP A 1 235 ? 12.873 -14.077 7.182 1.00 9.25 ? 235 ASP A OD2 1 ATOM 1801 N N . LYS A 1 236 ? 9.621 -12.370 10.474 1.00 9.34 ? 236 LYS A N 1 ATOM 1802 C CA . LYS A 1 236 ? 10.044 -11.421 11.500 1.00 9.58 ? 236 LYS A CA 1 ATOM 1803 C C . LYS A 1 236 ? 11.521 -11.562 11.830 1.00 9.52 ? 236 LYS A C 1 ATOM 1804 O O . LYS A 1 236 ? 12.247 -10.569 12.040 1.00 10.05 ? 236 LYS A O 1 ATOM 1805 C CB . LYS A 1 236 ? 9.199 -11.604 12.756 1.00 9.83 ? 236 LYS A CB 1 ATOM 1806 C CG . LYS A 1 236 ? 7.738 -11.215 12.575 1.00 9.20 ? 236 LYS A CG 1 ATOM 1807 C CD . LYS A 1 236 ? 6.919 -11.411 13.863 1.00 9.62 ? 236 LYS A CD 1 ATOM 1808 C CE . LYS A 1 236 ? 5.419 -11.184 13.705 1.00 10.17 ? 236 LYS A CE 1 ATOM 1809 N NZ . LYS A 1 236 ? 5.143 -9.740 13.366 1.00 11.47 ? 236 LYS A NZ 1 ATOM 1810 N N . ASN A 1 237 ? 11.986 -12.800 11.913 1.00 10.27 ? 237 ASN A N 1 ATOM 1811 C CA . ASN A 1 237 ? 13.363 -13.032 12.374 1.00 10.49 ? 237 ASN A CA 1 ATOM 1812 C C . ASN A 1 237 ? 14.428 -12.749 11.315 1.00 10.17 ? 237 ASN A C 1 ATOM 1813 O O . ASN A 1 237 ? 15.488 -12.253 11.643 1.00 11.56 ? 237 ASN A O 1 ATOM 1814 C CB . ASN A 1 237 ? 13.542 -14.476 12.878 1.00 10.17 ? 237 ASN A CB 1 ATOM 1815 C CG . ASN A 1 237 ? 12.747 -14.788 14.143 1.00 13.50 ? 237 ASN A CG 1 ATOM 1816 O OD1 . ASN A 1 237 ? 12.106 -13.924 14.699 1.00 14.93 ? 237 ASN A OD1 1 ATOM 1817 N ND2 . ASN A 1 237 ? 12.760 -16.055 14.565 1.00 14.86 ? 237 ASN A ND2 1 ATOM 1818 N N . GLY A 1 238 ? 14.130 -13.075 10.058 1.00 9.12 ? 238 GLY A N 1 ATOM 1819 C CA . GLY A 1 238 ? 15.092 -12.942 8.977 1.00 9.27 ? 238 GLY A CA 1 ATOM 1820 C C . GLY A 1 238 ? 16.081 -14.087 8.973 1.00 9.76 ? 238 GLY A C 1 ATOM 1821 O O . GLY A 1 238 ? 16.056 -14.953 9.881 1.00 12.48 ? 238 GLY A O 1 ATOM 1822 N N . CYS A 1 239 ? 16.926 -14.123 7.950 1.00 8.91 ? 239 CYS A N 1 ATOM 1823 C CA . CYS A 1 239 ? 18.065 -15.045 7.949 1.00 9.39 ? 239 CYS A CA 1 ATOM 1824 C C . CYS A 1 239 ? 19.316 -14.258 8.351 1.00 9.64 ? 239 CYS A C 1 ATOM 1825 O O . CYS A 1 239 ? 19.921 -13.550 7.540 1.00 10.40 ? 239 CYS A O 1 ATOM 1826 C CB . CYS A 1 239 ? 18.256 -15.690 6.591 1.00 9.37 ? 239 CYS A CB 1 ATOM 1827 S SG . CYS A 1 239 ? 19.737 -16.708 6.521 1.00 11.02 ? 239 CYS A SG 1 ATOM 1828 N N . GLY A 1 240 ? 19.691 -14.374 9.622 1.00 9.65 ? 240 GLY A N 1 ATOM 1829 C CA . GLY A 1 240 ? 20.732 -13.549 10.194 1.00 9.24 ? 240 GLY A CA 1 ATOM 1830 C C . GLY A 1 240 ? 22.146 -14.007 9.879 1.00 9.38 ? 240 GLY A C 1 ATOM 1831 O O . GLY A 1 240 ? 22.445 -15.210 9.919 1.00 10.17 ? 240 GLY A O 1 ATOM 1832 N N . TRP A 1 241 ? 23.011 -13.035 9.589 1.00 9.47 ? 241 TRP A N 1 ATOM 1833 C CA . TRP A 1 241 ? 24.427 -13.251 9.307 1.00 9.55 ? 241 TRP A CA 1 ATOM 1834 C C . TRP A 1 241 ? 25.246 -12.303 10.199 1.00 9.81 ? 241 TRP A C 1 ATOM 1835 O O . TRP A 1 241 ? 25.166 -11.086 10.074 1.00 10.33 ? 241 TRP A O 1 ATOM 1836 C CB . TRP A 1 241 ? 24.662 -12.928 7.840 1.00 10.27 ? 241 TRP A CB 1 ATOM 1837 C CG . TRP A 1 241 ? 26.079 -13.046 7.319 1.00 9.77 ? 241 TRP A CG 1 ATOM 1838 C CD1 . TRP A 1 241 ? 26.939 -12.018 7.017 1.00 9.75 ? 241 TRP A CD1 1 ATOM 1839 C CD2 . TRP A 1 241 ? 26.778 -14.256 6.969 1.00 9.60 ? 241 TRP A CD2 1 ATOM 1840 N NE1 . TRP A 1 241 ? 28.123 -12.521 6.528 1.00 9.99 ? 241 TRP A NE1 1 ATOM 1841 C CE2 . TRP A 1 241 ? 28.043 -13.887 6.475 1.00 8.55 ? 241 TRP A CE2 1 ATOM 1842 C CE3 . TRP A 1 241 ? 26.462 -15.606 7.039 1.00 10.50 ? 241 TRP A CE3 1 ATOM 1843 C CZ2 . TRP A 1 241 ? 28.988 -14.830 6.040 1.00 10.45 ? 241 TRP A CZ2 1 ATOM 1844 C CZ3 . TRP A 1 241 ? 27.384 -16.537 6.588 1.00 10.65 ? 241 TRP A CZ3 1 ATOM 1845 C CH2 . TRP A 1 241 ? 28.647 -16.150 6.152 1.00 11.17 ? 241 TRP A CH2 1 ATOM 1846 N N . ASN A 1 242 ? 25.959 -12.891 11.155 1.00 9.25 ? 242 ASN A N 1 ATOM 1847 C CA . ASN A 1 242 ? 26.735 -12.132 12.162 1.00 9.65 ? 242 ASN A CA 1 ATOM 1848 C C . ASN A 1 242 ? 27.918 -13.020 12.508 1.00 10.31 ? 242 ASN A C 1 ATOM 1849 O O . ASN A 1 242 ? 27.727 -14.167 12.921 1.00 10.64 ? 242 ASN A O 1 ATOM 1850 C CB . ASN A 1 242 ? 25.861 -11.878 13.379 1.00 9.93 ? 242 ASN A CB 1 ATOM 1851 C CG . ASN A 1 242 ? 26.575 -11.219 14.546 1.00 10.01 ? 242 ASN A CG 1 ATOM 1852 O OD1 . ASN A 1 242 ? 27.802 -11.248 14.644 1.00 11.02 ? 242 ASN A OD1 1 ATOM 1853 N ND2 . ASN A 1 242 ? 25.789 -10.588 15.433 1.00 9.99 ? 242 ASN A ND2 1 ATOM 1854 N N . ASN A 1 243 ? 29.132 -12.512 12.340 1.00 10.12 ? 243 ASN A N 1 ATOM 1855 C CA . ASN A 1 243 ? 30.310 -13.356 12.607 1.00 10.62 ? 243 ASN A CA 1 ATOM 1856 C C . ASN A 1 243 ? 30.258 -14.057 13.967 1.00 10.84 ? 243 ASN A C 1 ATOM 1857 O O . ASN A 1 243 ? 30.652 -15.226 14.083 1.00 11.11 ? 243 ASN A O 1 ATOM 1858 C CB . ASN A 1 243 ? 31.616 -12.554 12.448 1.00 11.54 ? 243 ASN A CB 1 ATOM 1859 C CG . ASN A 1 243 ? 31.684 -11.296 13.309 1.00 11.70 ? 243 ASN A CG 1 ATOM 1860 O OD1 . ASN A 1 243 ? 31.234 -10.224 12.897 1.00 12.28 ? 243 ASN A OD1 1 ATOM 1861 N ND2 . ASN A 1 243 ? 32.337 -11.410 14.457 1.00 12.40 ? 243 ASN A ND2 1 ATOM 1862 N N . TYR A 1 244 ? 29.781 -13.388 15.005 1.00 11.44 ? 244 TYR A N 1 ATOM 1863 C CA . TYR A 1 244 ? 29.708 -14.000 16.324 1.00 11.90 ? 244 TYR A CA 1 ATOM 1864 C C . TYR A 1 244 ? 28.821 -15.222 16.374 1.00 11.21 ? 244 TYR A C 1 ATOM 1865 O O . TYR A 1 244 ? 29.167 -16.246 17.017 1.00 12.23 ? 244 TYR A O 1 ATOM 1866 C CB . TYR A 1 244 ? 29.208 -12.998 17.359 1.00 12.52 ? 244 TYR A CB 1 ATOM 1867 C CG . TYR A 1 244 ? 30.252 -12.088 17.882 1.00 14.13 ? 244 TYR A CG 1 ATOM 1868 C CD1 . TYR A 1 244 ? 31.121 -12.504 18.846 1.00 14.25 ? 244 TYR A CD1 1 ATOM 1869 C CD2 . TYR A 1 244 ? 30.373 -10.797 17.404 1.00 14.41 ? 244 TYR A CD2 1 ATOM 1870 C CE1 . TYR A 1 244 ? 32.093 -11.646 19.371 1.00 15.00 ? 244 TYR A CE1 1 ATOM 1871 C CE2 . TYR A 1 244 ? 31.343 -9.934 17.910 1.00 14.84 ? 244 TYR A CE2 1 ATOM 1872 C CZ . TYR A 1 244 ? 32.208 -10.374 18.874 1.00 14.93 ? 244 TYR A CZ 1 ATOM 1873 O OH . TYR A 1 244 ? 33.145 -9.503 19.368 1.00 15.13 ? 244 TYR A OH 1 ATOM 1874 N N . ARG A 1 245 ? 27.712 -15.176 15.645 1.00 11.90 ? 245 ARG A N 1 ATOM 1875 C CA . ARG A 1 245 ? 26.753 -16.248 15.660 1.00 12.07 ? 245 ARG A CA 1 ATOM 1876 C C . ARG A 1 245 ? 27.284 -17.499 14.958 1.00 12.41 ? 245 ARG A C 1 ATOM 1877 O O . ARG A 1 245 ? 26.731 -18.583 15.129 1.00 13.05 ? 245 ARG A O 1 ATOM 1878 C CB . ARG A 1 245 ? 25.446 -15.825 14.996 1.00 12.20 ? 245 ARG A CB 1 ATOM 1879 C CG . ARG A 1 245 ? 24.592 -14.866 15.822 1.00 11.69 ? 245 ARG A CG 1 ATOM 1880 C CD . ARG A 1 245 ? 23.290 -14.555 15.110 1.00 11.63 ? 245 ARG A CD 1 ATOM 1881 N NE . ARG A 1 245 ? 22.420 -13.682 15.881 1.00 12.07 ? 245 ARG A NE 1 ATOM 1882 C CZ . ARG A 1 245 ? 21.633 -14.095 16.870 1.00 12.42 ? 245 ARG A CZ 1 ATOM 1883 N NH1 . ARG A 1 245 ? 21.568 -15.374 17.245 1.00 14.51 ? 245 ARG A NH1 1 ATOM 1884 N NH2 . ARG A 1 245 ? 20.909 -13.207 17.525 1.00 13.96 ? 245 ARG A NH2 1 ATOM 1885 N N . VAL A 1 246 ? 28.308 -17.329 14.142 1.00 12.26 ? 246 VAL A N 1 ATOM 1886 C CA . VAL A 1 246 ? 28.967 -18.431 13.445 1.00 12.61 ? 246 VAL A CA 1 ATOM 1887 C C . VAL A 1 246 ? 30.389 -18.687 13.971 1.00 13.04 ? 246 VAL A C 1 ATOM 1888 O O . VAL A 1 246 ? 31.218 -19.307 13.304 1.00 12.47 ? 246 VAL A O 1 ATOM 1889 C CB . VAL A 1 246 ? 28.896 -18.271 11.896 1.00 12.80 ? 246 VAL A CB 1 ATOM 1890 C CG1 . VAL A 1 246 ? 27.432 -18.289 11.455 1.00 13.81 ? 246 VAL A CG1 1 ATOM 1891 C CG2 . VAL A 1 246 ? 29.610 -17.039 11.408 1.00 11.40 ? 246 VAL A CG2 1 ATOM 1892 N N . ASN A 1 247 ? 30.628 -18.237 15.199 1.00 13.81 ? 247 ASN A N 1 ATOM 1893 C CA . ASN A 1 247 ? 31.828 -18.612 15.993 1.00 14.06 ? 247 ASN A CA 1 ATOM 1894 C C . ASN A 1 247 ? 33.128 -18.023 15.440 1.00 14.14 ? 247 ASN A C 1 ATOM 1895 O O . ASN A 1 247 ? 34.190 -18.666 15.434 1.00 14.70 ? 247 ASN A O 1 ATOM 1896 C CB . ASN A 1 247 ? 31.930 -20.145 16.127 1.00 14.27 ? 247 ASN A CB 1 ATOM 1897 C CG . ASN A 1 247 ? 32.991 -20.586 17.125 1.00 15.31 ? 247 ASN A CG 1 ATOM 1898 O OD1 . ASN A 1 247 ? 33.193 -19.944 18.162 1.00 16.62 ? 247 ASN A OD1 1 ATOM 1899 N ND2 . ASN A 1 247 ? 33.685 -21.688 16.793 1.00 16.56 ? 247 ASN A ND2 1 ATOM 1900 N N . VAL A 1 248 ? 33.045 -16.785 14.988 1.00 13.89 ? 248 VAL A N 1 ATOM 1901 C CA . VAL A 1 248 ? 34.191 -16.008 14.567 1.00 14.53 ? 248 VAL A CA 1 ATOM 1902 C C . VAL A 1 248 ? 34.205 -14.753 15.429 1.00 15.08 ? 248 VAL A C 1 ATOM 1903 O O . VAL A 1 248 ? 33.299 -13.920 15.330 1.00 17.01 ? 248 VAL A O 1 ATOM 1904 C CB . VAL A 1 248 ? 34.126 -15.652 13.084 1.00 14.78 ? 248 VAL A CB 1 ATOM 1905 C CG1 . VAL A 1 248 ? 35.362 -14.828 12.658 1.00 15.33 ? 248 VAL A CG1 1 ATOM 1906 C CG2 . VAL A 1 248 ? 34.014 -16.923 12.264 1.00 14.78 ? 248 VAL A CG2 1 ATOM 1907 N N . THR A 1 249 ? 35.197 -14.610 16.309 1.00 15.02 ? 249 THR A N 1 ATOM 1908 C CA . THR A 1 249 ? 35.157 -13.526 17.327 1.00 15.12 ? 249 THR A CA 1 ATOM 1909 C C . THR A 1 249 ? 36.111 -12.392 17.070 1.00 14.44 ? 249 THR A C 1 ATOM 1910 O O . THR A 1 249 ? 36.007 -11.351 17.713 1.00 15.96 ? 249 THR A O 1 ATOM 1911 C CB . THR A 1 249 ? 35.436 -14.051 18.732 1.00 16.41 ? 249 THR A CB 1 ATOM 1912 O OG1 . THR A 1 249 ? 36.740 -14.639 18.767 1.00 18.47 ? 249 THR A OG1 1 ATOM 1913 C CG2 . THR A 1 249 ? 34.471 -15.127 19.137 1.00 18.10 ? 249 THR A CG2 1 ATOM 1914 N N . ASP A 1 250 ? 37.049 -12.568 16.150 1.00 14.05 ? 250 ASP A N 1 ATOM 1915 C CA . ASP A 1 250 ? 38.093 -11.569 15.941 1.00 14.34 ? 250 ASP A CA 1 ATOM 1916 C C . ASP A 1 250 ? 37.905 -10.745 14.693 1.00 13.46 ? 250 ASP A C 1 ATOM 1917 O O . ASP A 1 250 ? 38.847 -10.117 14.207 1.00 13.53 ? 250 ASP A O 1 ATOM 1918 C CB . ASP A 1 250 ? 39.483 -12.231 15.926 1.00 15.24 ? 250 ASP A CB 1 ATOM 1919 C CG . ASP A 1 250 ? 39.637 -13.273 14.852 1.00 17.70 ? 250 ASP A CG 1 ATOM 1920 O OD1 . ASP A 1 250 ? 38.623 -13.729 14.265 1.00 18.13 ? 250 ASP A OD1 1 ATOM 1921 O OD2 . ASP A 1 250 ? 40.767 -13.716 14.545 1.00 22.70 ? 250 ASP A OD2 1 ATOM 1922 N N . TYR A 1 251 ? 36.679 -10.727 14.156 1.00 12.64 ? 251 TYR A N 1 ATOM 1923 C CA . TYR A 1 251 ? 36.445 -10.141 12.841 1.00 12.36 ? 251 TYR A CA 1 ATOM 1924 C C . TYR A 1 251 ? 36.082 -8.661 12.867 1.00 12.00 ? 251 TYR A C 1 ATOM 1925 O O . TYR A 1 251 ? 36.458 -7.905 11.976 1.00 12.10 ? 251 TYR A O 1 ATOM 1926 C CB . TYR A 1 251 ? 35.344 -10.911 12.086 1.00 11.87 ? 251 TYR A CB 1 ATOM 1927 C CG . TYR A 1 251 ? 35.245 -10.524 10.631 1.00 12.17 ? 251 TYR A CG 1 ATOM 1928 C CD1 . TYR A 1 251 ? 36.150 -10.997 9.716 1.00 10.99 ? 251 TYR A CD1 1 ATOM 1929 C CD2 . TYR A 1 251 ? 34.257 -9.664 10.174 1.00 12.04 ? 251 TYR A CD2 1 ATOM 1930 C CE1 . TYR A 1 251 ? 36.101 -10.651 8.385 1.00 11.63 ? 251 TYR A CE1 1 ATOM 1931 C CE2 . TYR A 1 251 ? 34.201 -9.281 8.856 1.00 11.86 ? 251 TYR A CE2 1 ATOM 1932 C CZ . TYR A 1 251 ? 35.108 -9.786 7.948 1.00 10.83 ? 251 TYR A CZ 1 ATOM 1933 O OH . TYR A 1 251 ? 35.047 -9.389 6.635 1.00 12.79 ? 251 TYR A OH 1 ATOM 1934 N N . TYR A 1 252 ? 35.353 -8.247 13.895 1.00 11.89 ? 252 TYR A N 1 ATOM 1935 C CA . TYR A 1 252 ? 34.677 -6.950 13.869 1.00 11.64 ? 252 TYR A CA 1 ATOM 1936 C C . TYR A 1 252 ? 34.547 -6.433 15.287 1.00 11.58 ? 252 TYR A C 1 ATOM 1937 O O . TYR A 1 252 ? 33.917 -7.077 16.110 1.00 11.86 ? 252 TYR A O 1 ATOM 1938 C CB . TYR A 1 252 ? 33.280 -7.117 13.226 1.00 11.26 ? 252 TYR A CB 1 ATOM 1939 C CG . TYR A 1 252 ? 32.469 -5.843 13.128 1.00 10.61 ? 252 TYR A CG 1 ATOM 1940 C CD1 . TYR A 1 252 ? 31.704 -5.396 14.191 1.00 10.60 ? 252 TYR A CD1 1 ATOM 1941 C CD2 . TYR A 1 252 ? 32.482 -5.093 11.977 1.00 11.20 ? 252 TYR A CD2 1 ATOM 1942 C CE1 . TYR A 1 252 ? 30.943 -4.227 14.079 1.00 10.20 ? 252 TYR A CE1 1 ATOM 1943 C CE2 . TYR A 1 252 ? 31.726 -3.917 11.873 1.00 10.48 ? 252 TYR A CE2 1 ATOM 1944 C CZ . TYR A 1 252 ? 30.988 -3.484 12.939 1.00 9.97 ? 252 TYR A CZ 1 ATOM 1945 O OH . TYR A 1 252 ? 30.232 -2.317 12.814 1.00 10.61 ? 252 TYR A OH 1 ATOM 1946 N N . GLY A 1 253 ? 35.152 -5.279 15.587 1.00 12.05 ? 253 GLY A N 1 ATOM 1947 C CA . GLY A 1 253 ? 35.061 -4.775 16.952 1.00 12.16 ? 253 GLY A CA 1 ATOM 1948 C C . GLY A 1 253 ? 35.959 -3.587 17.203 1.00 11.65 ? 253 GLY A C 1 ATOM 1949 O O . GLY A 1 253 ? 36.656 -3.109 16.305 1.00 11.93 ? 253 GLY A O 1 ATOM 1950 N N . ARG A 1 254 ? 35.890 -3.087 18.437 1.00 12.59 ? 254 ARG A N 1 ATOM 1951 C CA . ARG A 1 254 ? 36.637 -1.882 18.826 1.00 13.39 ? 254 ARG A CA 1 ATOM 1952 C C . ARG A 1 254 ? 38.098 -2.236 19.156 1.00 14.21 ? 254 ARG A C 1 ATOM 1953 O O . ARG A 1 254 ? 38.384 -2.730 20.243 1.00 15.71 ? 254 ARG A O 1 ATOM 1954 C CB . ARG A 1 254 ? 35.992 -1.237 20.047 1.00 13.33 ? 254 ARG A CB 1 ATOM 1955 C CG . ARG A 1 254 ? 34.587 -0.709 19.804 1.00 12.72 ? 254 ARG A CG 1 ATOM 1956 C CD . ARG A 1 254 ? 33.947 -0.117 21.034 1.00 12.65 ? 254 ARG A CD 1 ATOM 1957 N NE . ARG A 1 254 ? 34.542 1.159 21.425 1.00 13.79 ? 254 ARG A NE 1 ATOM 1958 C CZ . ARG A 1 254 ? 34.205 2.331 20.921 1.00 12.81 ? 254 ARG A CZ 1 ATOM 1959 N NH1 . ARG A 1 254 ? 33.242 2.416 20.022 1.00 13.50 ? 254 ARG A NH1 1 ATOM 1960 N NH2 . ARG A 1 254 ? 34.787 3.449 21.324 1.00 15.56 ? 254 ARG A NH2 1 ATOM 1961 N N . GLY A 1 255 ? 38.996 -1.975 18.219 1.00 15.74 ? 255 GLY A N 1 ATOM 1962 C CA . GLY A 1 255 ? 40.444 -2.160 18.464 1.00 16.52 ? 255 GLY A CA 1 ATOM 1963 C C . GLY A 1 255 ? 41.173 -2.815 17.303 1.00 17.91 ? 255 GLY A C 1 ATOM 1964 O O . GLY A 1 255 ? 40.567 -3.423 16.395 1.00 16.70 ? 255 GLY A O 1 ATOM 1965 N N . GLU A 1 256 ? 42.501 -2.722 17.349 1.00 19.00 ? 256 GLU A N 1 ATOM 1966 C CA . GLU A 1 256 ? 43.357 -3.225 16.276 1.00 20.27 ? 256 GLU A CA 1 ATOM 1967 C C . GLU A 1 256 ? 43.382 -4.748 16.182 1.00 19.94 ? 256 GLU A C 1 ATOM 1968 O O . GLU A 1 256 ? 43.818 -5.288 15.161 1.00 20.99 ? 256 GLU A O 1 ATOM 1969 C CB . GLU A 1 256 ? 44.798 -2.720 16.469 1.00 21.16 ? 256 GLU A CB 1 ATOM 1970 C CG . GLU A 1 256 ? 44.968 -1.253 16.161 1.00 23.71 ? 256 GLU A CG 1 ATOM 1971 C CD . GLU A 1 256 ? 46.417 -0.821 16.191 1.00 25.47 ? 256 GLU A CD 1 ATOM 1972 O OE1 . GLU A 1 256 ? 47.148 -1.313 17.066 1.00 31.11 ? 256 GLU A OE1 1 ATOM 1973 O OE2 . GLU A 1 256 ? 46.801 0.035 15.355 1.00 33.38 ? 256 GLU A OE2 1 ATOM 1974 N N . GLU A 1 257 ? 42.915 -5.432 17.225 1.00 19.21 ? 257 GLU A N 1 ATOM 1975 C CA . GLU A 1 257 ? 42.861 -6.887 17.225 1.00 19.21 ? 257 GLU A CA 1 ATOM 1976 C C . GLU A 1 257 ? 41.688 -7.452 16.424 1.00 18.61 ? 257 GLU A C 1 ATOM 1977 O O . GLU A 1 257 ? 41.549 -8.672 16.335 1.00 19.30 ? 257 GLU A O 1 ATOM 1978 C CB . GLU A 1 257 ? 42.801 -7.451 18.651 1.00 20.29 ? 257 GLU A CB 1 ATOM 1979 C CG . GLU A 1 257 ? 41.534 -7.177 19.442 1.00 21.70 ? 257 GLU A CG 1 ATOM 1980 C CD . GLU A 1 257 ? 41.532 -5.848 20.180 1.00 23.31 ? 257 GLU A CD 1 ATOM 1981 O OE1 . GLU A 1 257 ? 42.150 -4.856 19.725 1.00 24.00 ? 257 GLU A OE1 1 ATOM 1982 O OE2 . GLU A 1 257 ? 40.876 -5.806 21.226 1.00 26.45 ? 257 GLU A OE2 1 ATOM 1983 N N . PHE A 1 258 ? 40.831 -6.576 15.883 1.00 16.72 ? 258 PHE A N 1 ATOM 1984 C CA . PHE A 1 258 ? 39.727 -7.006 15.012 1.00 15.74 ? 258 PHE A CA 1 ATOM 1985 C C . PHE A 1 258 ? 40.073 -6.686 13.563 1.00 15.47 ? 258 PHE A C 1 ATOM 1986 O O . PHE A 1 258 ? 40.693 -5.656 13.262 1.00 17.02 ? 258 PHE A O 1 ATOM 1987 C CB . PHE A 1 258 ? 38.439 -6.278 15.408 1.00 14.30 ? 258 PHE A CB 1 ATOM 1988 C CG . PHE A 1 258 ? 37.966 -6.598 16.806 1.00 13.72 ? 258 PHE A CG 1 ATOM 1989 C CD1 . PHE A 1 258 ? 37.260 -7.756 17.065 1.00 12.99 ? 258 PHE A CD1 1 ATOM 1990 C CD2 . PHE A 1 258 ? 38.260 -5.753 17.880 1.00 13.73 ? 258 PHE A CD2 1 ATOM 1991 C CE1 . PHE A 1 258 ? 36.833 -8.074 18.351 1.00 13.39 ? 258 PHE A CE1 1 ATOM 1992 C CE2 . PHE A 1 258 ? 37.839 -6.051 19.154 1.00 13.37 ? 258 PHE A CE2 1 ATOM 1993 C CZ . PHE A 1 258 ? 37.124 -7.203 19.411 1.00 12.83 ? 258 PHE A CZ 1 ATOM 1994 N N . LYS A 1 259 ? 39.683 -7.571 12.657 1.00 15.09 ? 259 LYS A N 1 ATOM 1995 C CA . LYS A 1 259 ? 39.943 -7.355 11.241 1.00 16.19 ? 259 LYS A CA 1 ATOM 1996 C C . LYS A 1 259 ? 39.334 -6.046 10.735 1.00 15.05 ? 259 LYS A C 1 ATOM 1997 O O . LYS A 1 259 ? 39.977 -5.334 9.948 1.00 16.63 ? 259 LYS A O 1 ATOM 1998 C CB . LYS A 1 259 ? 39.481 -8.531 10.387 1.00 17.15 ? 259 LYS A CB 1 ATOM 1999 C CG . LYS A 1 259 ? 40.214 -9.805 10.811 1.00 20.30 ? 259 LYS A CG 1 ATOM 2000 C CD . LYS A 1 259 ? 40.136 -10.907 9.849 1.00 20.97 ? 259 LYS A CD 1 ATOM 2001 C CE . LYS A 1 259 ? 41.277 -11.917 10.126 1.00 22.40 ? 259 LYS A CE 1 ATOM 2002 N NZ . LYS A 1 259 ? 41.346 -12.226 11.571 1.00 22.89 ? 259 LYS A NZ 1 ATOM 2003 N N . VAL A 1 260 ? 38.102 -5.762 11.176 1.00 14.15 ? 260 VAL A N 1 ATOM 2004 C CA . VAL A 1 260 ? 37.436 -4.495 10.916 1.00 13.39 ? 260 VAL A CA 1 ATOM 2005 C C . VAL A 1 260 ? 37.393 -3.785 12.263 1.00 12.38 ? 260 VAL A C 1 ATOM 2006 O O . VAL A 1 260 ? 36.750 -4.238 13.204 1.00 13.30 ? 260 VAL A O 1 ATOM 2007 C CB . VAL A 1 260 ? 35.996 -4.689 10.362 1.00 12.70 ? 260 VAL A CB 1 ATOM 2008 C CG1 . VAL A 1 260 ? 35.328 -3.346 10.120 1.00 13.80 ? 260 VAL A CG1 1 ATOM 2009 C CG2 . VAL A 1 260 ? 36.005 -5.533 9.098 1.00 14.20 ? 260 VAL A CG2 1 ATOM 2010 N N . ASN A 1 261 ? 38.171 -2.710 12.373 1.00 12.88 ? 261 ASN A N 1 ATOM 2011 C CA . ASN A 1 261 ? 38.355 -1.951 13.610 1.00 13.00 ? 261 ASN A CA 1 ATOM 2012 C C . ASN A 1 261 ? 37.381 -0.789 13.661 1.00 11.99 ? 261 ASN A C 1 ATOM 2013 O O . ASN A 1 261 ? 37.548 0.197 12.965 1.00 13.33 ? 261 ASN A O 1 ATOM 2014 C CB . ASN A 1 261 ? 39.821 -1.457 13.686 1.00 13.09 ? 261 ASN A CB 1 ATOM 2015 C CG . ASN A 1 261 ? 40.099 -0.609 14.900 1.00 13.84 ? 261 ASN A CG 1 ATOM 2016 O OD1 . ASN A 1 261 ? 39.237 -0.409 15.785 1.00 14.58 ? 261 ASN A OD1 1 ATOM 2017 N ND2 . ASN A 1 261 ? 41.345 -0.073 14.954 1.00 16.26 ? 261 ASN A ND2 1 ATOM 2018 N N . THR A 1 262 ? 36.345 -0.937 14.485 1.00 12.05 ? 262 THR A N 1 ATOM 2019 C CA . THR A 1 262 ? 35.268 0.042 14.515 1.00 11.70 ? 262 THR A CA 1 ATOM 2020 C C . THR A 1 262 ? 35.609 1.333 15.256 1.00 12.58 ? 262 THR A C 1 ATOM 2021 O O . THR A 1 262 ? 34.759 2.214 15.356 1.00 12.47 ? 262 THR A O 1 ATOM 2022 C CB . THR A 1 262 ? 34.022 -0.569 15.137 1.00 11.01 ? 262 THR A CB 1 ATOM 2023 O OG1 . THR A 1 262 ? 34.324 -0.996 16.464 1.00 11.87 ? 262 THR A OG1 1 ATOM 2024 C CG2 . THR A 1 262 ? 33.514 -1.805 14.336 1.00 11.41 ? 262 THR A CG2 1 ATOM 2025 N N . LEU A 1 263 ? 36.838 1.463 15.763 1.00 13.41 ? 263 LEU A N 1 ATOM 2026 C CA . LEU A 1 263 ? 37.326 2.765 16.244 1.00 13.37 ? 263 LEU A CA 1 ATOM 2027 C C . LEU A 1 263 ? 37.635 3.733 15.103 1.00 14.00 ? 263 LEU A C 1 ATOM 2028 O O . LEU A 1 263 ? 37.846 4.926 15.360 1.00 14.71 ? 263 LEU A O 1 ATOM 2029 C CB . LEU A 1 263 ? 38.577 2.600 17.142 1.00 14.37 ? 263 LEU A CB 1 ATOM 2030 C CG . LEU A 1 263 ? 38.358 1.768 18.394 1.00 14.71 ? 263 LEU A CG 1 ATOM 2031 C CD1 . LEU A 1 263 ? 39.656 1.582 19.142 1.00 15.63 ? 263 LEU A CD1 1 ATOM 2032 C CD2 . LEU A 1 263 ? 37.344 2.376 19.298 1.00 15.63 ? 263 LEU A CD2 1 ATOM 2033 N N . LYS A 1 264 ? 37.675 3.240 13.867 1.00 13.28 ? 264 LYS A N 1 ATOM 2034 C CA . LYS A 1 264 ? 37.935 4.062 12.697 1.00 14.26 ? 264 LYS A CA 1 ATOM 2035 C C . LYS A 1 264 ? 36.847 3.821 11.636 1.00 13.05 ? 264 LYS A C 1 ATOM 2036 O O . LYS A 1 264 ? 36.198 2.754 11.641 1.00 12.77 ? 264 LYS A O 1 ATOM 2037 C CB . LYS A 1 264 ? 39.297 3.709 12.091 1.00 15.22 ? 264 LYS A CB 1 ATOM 2038 C CG . LYS A 1 264 ? 40.466 3.770 13.071 1.00 18.31 ? 264 LYS A CG 1 ATOM 2039 C CD . LYS A 1 264 ? 41.809 3.493 12.378 1.00 20.35 ? 264 LYS A CD 1 ATOM 2040 C CE . LYS A 1 264 ? 41.969 2.061 11.933 1.00 24.41 ? 264 LYS A CE 1 ATOM 2041 N NZ . LYS A 1 264 ? 43.352 1.775 11.389 1.00 26.08 ? 264 LYS A NZ 1 ATOM 2042 N N . PRO A 1 265 ? 36.653 4.769 10.721 1.00 13.37 ? 265 PRO A N 1 ATOM 2043 C CA . PRO A 1 265 ? 35.721 4.542 9.610 1.00 12.80 ? 265 PRO A CA 1 ATOM 2044 C C . PRO A 1 265 ? 36.120 3.389 8.712 1.00 12.45 ? 265 PRO A C 1 ATOM 2045 O O . PRO A 1 265 ? 37.291 3.005 8.639 1.00 13.56 ? 265 PRO A O 1 ATOM 2046 C CB . PRO A 1 265 ? 35.728 5.874 8.847 1.00 13.16 ? 265 PRO A CB 1 ATOM 2047 C CG . PRO A 1 265 ? 36.225 6.881 9.861 1.00 15.34 ? 265 PRO A CG 1 ATOM 2048 C CD . PRO A 1 265 ? 37.250 6.114 10.647 1.00 13.40 ? 265 PRO A CD 1 ATOM 2049 N N . PHE A 1 266 ? 35.144 2.840 8.009 1.00 11.92 ? 266 PHE A N 1 ATOM 2050 C CA . PHE A 1 266 ? 35.376 1.725 7.084 1.00 11.38 ? 266 PHE A CA 1 ATOM 2051 C C . PHE A 1 266 ? 34.306 1.687 6.017 1.00 10.92 ? 266 PHE A C 1 ATOM 2052 O O . PHE A 1 266 ? 33.307 2.390 6.100 1.00 11.81 ? 266 PHE A O 1 ATOM 2053 C CB . PHE A 1 266 ? 35.517 0.378 7.801 1.00 10.89 ? 266 PHE A CB 1 ATOM 2054 C CG . PHE A 1 266 ? 34.381 0.040 8.707 1.00 10.61 ? 266 PHE A CG 1 ATOM 2055 C CD1 . PHE A 1 266 ? 34.380 0.468 10.032 1.00 10.85 ? 266 PHE A CD1 1 ATOM 2056 C CD2 . PHE A 1 266 ? 33.297 -0.699 8.257 1.00 11.68 ? 266 PHE A CD2 1 ATOM 2057 C CE1 . PHE A 1 266 ? 33.330 0.180 10.876 1.00 11.02 ? 266 PHE A CE1 1 ATOM 2058 C CE2 . PHE A 1 266 ? 32.246 -0.999 9.098 1.00 11.38 ? 266 PHE A CE2 1 ATOM 2059 C CZ . PHE A 1 266 ? 32.260 -0.579 10.404 1.00 11.44 ? 266 PHE A CZ 1 ATOM 2060 N N . THR A 1 267 ? 34.539 0.870 5.005 1.00 10.91 ? 267 THR A N 1 ATOM 2061 C CA . THR A 1 267 ? 33.657 0.693 3.879 1.00 10.99 ? 267 THR A CA 1 ATOM 2062 C C . THR A 1 267 ? 33.014 -0.676 3.972 1.00 10.55 ? 267 THR A C 1 ATOM 2063 O O . THR A 1 267 ? 33.661 -1.646 4.316 1.00 10.72 ? 267 THR A O 1 ATOM 2064 C CB . THR A 1 267 ? 34.467 0.804 2.594 1.00 11.99 ? 267 THR A CB 1 ATOM 2065 O OG1 . THR A 1 267 ? 35.004 2.141 2.471 1.00 13.38 ? 267 THR A OG1 1 ATOM 2066 C CG2 . THR A 1 267 ? 33.636 0.587 1.344 1.00 12.15 ? 267 THR A CG2 1 ATOM 2067 N N . VAL A 1 268 ? 31.739 -0.726 3.596 1.00 9.81 ? 268 VAL A N 1 ATOM 2068 C CA . VAL A 1 268 ? 30.893 -1.920 3.713 1.00 9.90 ? 268 VAL A CA 1 ATOM 2069 C C . VAL A 1 268 ? 30.329 -2.253 2.333 1.00 9.29 ? 268 VAL A C 1 ATOM 2070 O O . VAL A 1 268 ? 29.600 -1.441 1.761 1.00 10.18 ? 268 VAL A O 1 ATOM 2071 C CB . VAL A 1 268 ? 29.729 -1.607 4.672 1.00 9.32 ? 268 VAL A CB 1 ATOM 2072 C CG1 . VAL A 1 268 ? 28.858 -2.816 4.885 1.00 9.84 ? 268 VAL A CG1 1 ATOM 2073 C CG2 . VAL A 1 268 ? 30.252 -1.073 6.027 1.00 9.30 ? 268 VAL A CG2 1 ATOM 2074 N N . VAL A 1 269 ? 30.703 -3.424 1.795 1.00 8.94 ? 269 VAL A N 1 ATOM 2075 C CA . VAL A 1 269 ? 30.295 -3.841 0.447 1.00 9.93 ? 269 VAL A CA 1 ATOM 2076 C C . VAL A 1 269 ? 29.329 -5.015 0.545 1.00 9.43 ? 269 VAL A C 1 ATOM 2077 O O . VAL A 1 269 ? 29.558 -5.970 1.288 1.00 10.19 ? 269 VAL A O 1 ATOM 2078 C CB . VAL A 1 269 ? 31.508 -4.272 -0.437 1.00 10.20 ? 269 VAL A CB 1 ATOM 2079 C CG1 . VAL A 1 269 ? 31.047 -4.635 -1.830 1.00 11.30 ? 269 VAL A CG1 1 ATOM 2080 C CG2 . VAL A 1 269 ? 32.566 -3.185 -0.458 1.00 11.04 ? 269 VAL A CG2 1 ATOM 2081 N N . THR A 1 270 ? 28.209 -4.924 -0.178 1.00 9.46 ? 270 THR A N 1 ATOM 2082 C CA . THR A 1 270 ? 27.198 -5.989 -0.200 1.00 10.13 ? 270 THR A CA 1 ATOM 2083 C C . THR A 1 270 ? 26.853 -6.342 -1.634 1.00 9.74 ? 270 THR A C 1 ATOM 2084 O O . THR A 1 270 ? 26.340 -5.522 -2.363 1.00 10.72 ? 270 THR A O 1 ATOM 2085 C CB . THR A 1 270 ? 25.957 -5.568 0.548 1.00 9.49 ? 270 THR A CB 1 ATOM 2086 O OG1 . THR A 1 270 ? 26.344 -5.075 1.848 1.00 9.67 ? 270 THR A OG1 1 ATOM 2087 C CG2 . THR A 1 270 ? 25.065 -6.791 0.819 1.00 9.68 ? 270 THR A CG2 1 ATOM 2088 N N . GLN A 1 271 ? 27.139 -7.579 -2.030 1.00 9.97 ? 271 GLN A N 1 ATOM 2089 C CA . GLN A 1 271 ? 26.870 -8.064 -3.385 1.00 10.51 ? 271 GLN A CA 1 ATOM 2090 C C . GLN A 1 271 ? 25.694 -9.036 -3.368 1.00 10.00 ? 271 GLN A C 1 ATOM 2091 O O . GLN A 1 271 ? 25.593 -9.884 -2.491 1.00 10.48 ? 271 GLN A O 1 ATOM 2092 C CB . GLN A 1 271 ? 28.089 -8.780 -3.981 1.00 10.91 ? 271 GLN A CB 1 ATOM 2093 C CG . GLN A 1 271 ? 29.378 -7.941 -3.949 1.00 11.01 ? 271 GLN A CG 1 ATOM 2094 C CD . GLN A 1 271 ? 30.554 -8.676 -4.537 1.00 11.39 ? 271 GLN A CD 1 ATOM 2095 O OE1 . GLN A 1 271 ? 30.718 -9.895 -4.343 1.00 13.00 ? 271 GLN A OE1 1 ATOM 2096 N NE2 . GLN A 1 271 ? 31.356 -7.946 -5.285 1.00 13.36 ? 271 GLN A NE2 1 ATOM 2097 N N . PHE A 1 272 ? 24.818 -8.876 -4.349 1.00 9.83 ? 272 PHE A N 1 ATOM 2098 C CA . PHE A 1 272 ? 23.626 -9.683 -4.513 1.00 9.72 ? 272 PHE A CA 1 ATOM 2099 C C . PHE A 1 272 ? 23.820 -10.536 -5.760 1.00 9.35 ? 272 PHE A C 1 ATOM 2100 O O . PHE A 1 272 ? 23.537 -10.109 -6.865 1.00 10.18 ? 272 PHE A O 1 ATOM 2101 C CB . PHE A 1 272 ? 22.404 -8.748 -4.611 1.00 9.66 ? 272 PHE A CB 1 ATOM 2102 C CG . PHE A 1 272 ? 22.139 -7.953 -3.336 1.00 9.59 ? 272 PHE A CG 1 ATOM 2103 C CD1 . PHE A 1 272 ? 21.365 -8.480 -2.326 1.00 9.76 ? 272 PHE A CD1 1 ATOM 2104 C CD2 . PHE A 1 272 ? 22.697 -6.702 -3.144 1.00 10.77 ? 272 PHE A CD2 1 ATOM 2105 C CE1 . PHE A 1 272 ? 21.147 -7.783 -1.161 1.00 10.06 ? 272 PHE A CE1 1 ATOM 2106 C CE2 . PHE A 1 272 ? 22.480 -6.012 -1.985 1.00 10.81 ? 272 PHE A CE2 1 ATOM 2107 C CZ . PHE A 1 272 ? 21.707 -6.556 -0.980 1.00 11.12 ? 272 PHE A CZ 1 ATOM 2108 N N . LEU A 1 273 ? 24.367 -11.733 -5.559 1.00 10.93 ? 273 LEU A N 1 ATOM 2109 C CA . LEU A 1 273 ? 24.840 -12.573 -6.646 1.00 11.20 ? 273 LEU A CA 1 ATOM 2110 C C . LEU A 1 273 ? 23.717 -13.448 -7.176 1.00 11.52 ? 273 LEU A C 1 ATOM 2111 O O . LEU A 1 273 ? 23.056 -14.153 -6.423 1.00 12.00 ? 273 LEU A O 1 ATOM 2112 C CB . LEU A 1 273 ? 26.034 -13.402 -6.173 1.00 12.00 ? 273 LEU A CB 1 ATOM 2113 C CG . LEU A 1 273 ? 27.175 -12.572 -5.568 1.00 14.37 ? 273 LEU A CG 1 ATOM 2114 C CD1 . LEU A 1 273 ? 28.312 -13.499 -5.139 1.00 16.75 ? 273 LEU A CD1 1 ATOM 2115 C CD2 . LEU A 1 273 ? 27.696 -11.545 -6.529 1.00 15.06 ? 273 LEU A CD2 1 ATOM 2116 N N . ALA A 1 274 ? 23.509 -13.380 -8.478 1.00 12.67 ? 274 ALA A N 1 ATOM 2117 C CA . ALA A 1 274 ? 22.443 -14.107 -9.140 1.00 14.62 ? 274 ALA A CA 1 ATOM 2118 C C . ALA A 1 274 ? 22.957 -15.370 -9.841 1.00 16.17 ? 274 ALA A C 1 ATOM 2119 O O . ALA A 1 274 ? 24.134 -15.459 -10.198 1.00 17.07 ? 274 ALA A O 1 ATOM 2120 C CB . ALA A 1 274 ? 21.736 -13.206 -10.108 1.00 15.73 ? 274 ALA A CB 1 ATOM 2121 N N . ASN A 1 275 ? 22.062 -16.336 -10.008 1.00 17.73 ? 275 ASN A N 1 ATOM 2122 C CA . ASN A 1 275 ? 22.397 -17.573 -10.747 1.00 20.53 ? 275 ASN A CA 1 ATOM 2123 C C . ASN A 1 275 ? 22.199 -17.335 -12.234 1.00 22.50 ? 275 ASN A C 1 ATOM 2124 O O . ASN A 1 275 ? 21.872 -16.241 -12.656 1.00 20.67 ? 275 ASN A O 1 ATOM 2125 C CB . ASN A 1 275 ? 21.623 -18.774 -10.211 1.00 19.77 ? 275 ASN A CB 1 ATOM 2126 C CG . ASN A 1 275 ? 20.128 -18.621 -10.329 1.00 20.36 ? 275 ASN A CG 1 ATOM 2127 O OD1 . ASN A 1 275 ? 19.641 -17.891 -11.178 1.00 17.59 ? 275 ASN A OD1 1 ATOM 2128 N ND2 . ASN A 1 275 ? 19.405 -19.287 -9.442 1.00 21.65 ? 275 ASN A ND2 1 ATOM 2129 N N . ARG A 1 276 ? 22.433 -18.342 -13.071 1.00 26.09 ? 276 ARG A N 1 ATOM 2130 C CA . ARG A 1 276 ? 22.458 -18.026 -14.503 1.00 28.29 ? 276 ARG A CA 1 ATOM 2131 C C . ARG A 1 276 ? 21.076 -17.748 -15.118 1.00 29.84 ? 276 ARG A C 1 ATOM 2132 O O . ARG A 1 276 ? 20.982 -17.267 -16.242 1.00 31.91 ? 276 ARG A O 1 ATOM 2133 C CB . ARG A 1 276 ? 23.285 -19.033 -15.321 1.00 30.19 ? 276 ARG A CB 1 ATOM 2134 C CG . ARG A 1 276 ? 24.762 -18.604 -15.426 1.00 33.84 ? 276 ARG A CG 1 ATOM 2135 C CD . ARG A 1 276 ? 25.315 -18.557 -16.839 1.00 38.40 ? 276 ARG A CD 1 ATOM 2136 N NE . ARG A 1 276 ? 25.722 -19.884 -17.297 1.00 40.95 ? 276 ARG A NE 1 ATOM 2137 C CZ . ARG A 1 276 ? 25.616 -20.332 -18.548 1.00 42.45 ? 276 ARG A CZ 1 ATOM 2138 N NH1 . ARG A 1 276 ? 25.099 -19.574 -19.515 1.00 43.21 ? 276 ARG A NH1 1 ATOM 2139 N NH2 . ARG A 1 276 ? 26.023 -21.564 -18.832 1.00 42.37 ? 276 ARG A NH2 1 ATOM 2140 N N . ARG A 1 277 ? 20.011 -17.991 -14.367 1.00 29.95 ? 277 ARG A N 1 ATOM 2141 C CA . ARG A 1 277 ? 18.693 -17.548 -14.828 1.00 29.59 ? 277 ARG A CA 1 ATOM 2142 C C . ARG A 1 277 ? 18.158 -16.300 -14.183 1.00 27.15 ? 277 ARG A C 1 ATOM 2143 O O . ARG A 1 277 ? 16.975 -15.998 -14.337 1.00 27.69 ? 277 ARG A O 1 ATOM 2144 C CB . ARG A 1 277 ? 17.688 -18.645 -14.643 1.00 30.65 ? 277 ARG A CB 1 ATOM 2145 C CG . ARG A 1 277 ? 17.841 -19.728 -15.699 1.00 33.81 ? 277 ARG A CG 1 ATOM 2146 C CD . ARG A 1 277 ? 17.449 -21.052 -15.183 1.00 38.01 ? 277 ARG A CD 1 ATOM 2147 N NE . ARG A 1 277 ? 17.949 -21.190 -13.821 1.00 39.19 ? 277 ARG A NE 1 ATOM 2148 C CZ . ARG A 1 277 ? 17.804 -22.274 -13.089 1.00 41.14 ? 277 ARG A CZ 1 ATOM 2149 N NH1 . ARG A 1 277 ? 17.203 -23.355 -13.580 1.00 42.21 ? 277 ARG A NH1 1 ATOM 2150 N NH2 . ARG A 1 277 ? 18.299 -22.285 -11.862 1.00 41.59 ? 277 ARG A NH2 1 ATOM 2151 N N . GLY A 1 278 ? 19.024 -15.581 -13.467 1.00 22.77 ? 278 GLY A N 1 ATOM 2152 C CA . GLY A 1 278 ? 18.737 -14.215 -13.099 1.00 19.90 ? 278 GLY A CA 1 ATOM 2153 C C . GLY A 1 278 ? 18.130 -14.065 -11.709 1.00 17.76 ? 278 GLY A C 1 ATOM 2154 O O . GLY A 1 278 ? 17.805 -12.979 -11.301 1.00 19.41 ? 278 GLY A O 1 ATOM 2155 N N . LYS A 1 279 ? 18.008 -15.168 -10.998 1.00 14.89 ? 279 LYS A N 1 ATOM 2156 C CA . LYS A 1 279 ? 17.461 -15.168 -9.635 1.00 13.03 ? 279 LYS A CA 1 ATOM 2157 C C . LYS A 1 279 ? 18.562 -15.055 -8.586 1.00 11.46 ? 279 LYS A C 1 ATOM 2158 O O . LYS A 1 279 ? 19.672 -15.566 -8.757 1.00 12.44 ? 279 LYS A O 1 ATOM 2159 C CB . LYS A 1 279 ? 16.633 -16.433 -9.388 1.00 12.15 ? 279 LYS A CB 1 ATOM 2160 C CG . LYS A 1 279 ? 15.422 -16.595 -10.340 1.00 12.08 ? 279 LYS A CG 1 ATOM 2161 C CD . LYS A 1 279 ? 14.409 -15.474 -10.253 1.00 11.63 ? 279 LYS A CD 1 ATOM 2162 C CE . LYS A 1 279 ? 13.243 -15.695 -11.203 1.00 12.15 ? 279 LYS A CE 1 ATOM 2163 N NZ . LYS A 1 279 ? 12.140 -14.720 -10.925 1.00 11.63 ? 279 LYS A NZ 1 ATOM 2164 N N . LEU A 1 280 ? 18.253 -14.407 -7.474 1.00 9.85 ? 280 LEU A N 1 ATOM 2165 C CA . LEU A 1 280 ? 19.228 -14.266 -6.394 1.00 10.45 ? 280 LEU A CA 1 ATOM 2166 C C . LEU A 1 280 ? 19.566 -15.615 -5.774 1.00 10.65 ? 280 LEU A C 1 ATOM 2167 O O . LEU A 1 280 ? 18.670 -16.373 -5.448 1.00 10.46 ? 280 LEU A O 1 ATOM 2168 C CB . LEU A 1 280 ? 18.661 -13.336 -5.313 1.00 9.95 ? 280 LEU A CB 1 ATOM 2169 C CG . LEU A 1 280 ? 19.614 -12.933 -4.199 1.00 9.47 ? 280 LEU A CG 1 ATOM 2170 C CD1 . LEU A 1 280 ? 20.753 -12.112 -4.676 1.00 8.96 ? 280 LEU A CD1 1 ATOM 2171 C CD2 . LEU A 1 280 ? 18.864 -12.173 -3.111 1.00 9.23 ? 280 LEU A CD2 1 ATOM 2172 N N . GLU A 1 281 ? 20.866 -15.876 -5.602 1.00 11.72 ? 281 GLU A N 1 ATOM 2173 C CA . GLU A 1 281 ? 21.386 -17.105 -5.000 1.00 13.02 ? 281 GLU A CA 1 ATOM 2174 C C . GLU A 1 281 ? 22.196 -16.875 -3.721 1.00 11.70 ? 281 GLU A C 1 ATOM 2175 O O . GLU A 1 281 ? 22.141 -17.670 -2.806 1.00 11.62 ? 281 GLU A O 1 ATOM 2176 C CB . GLU A 1 281 ? 22.295 -17.766 -6.050 1.00 14.84 ? 281 GLU A CB 1 ATOM 2177 C CG . GLU A 1 281 ? 22.895 -19.094 -5.737 1.00 17.55 ? 281 GLU A CG 1 ATOM 2178 C CD . GLU A 1 281 ? 23.659 -19.609 -6.941 1.00 18.99 ? 281 GLU A CD 1 ATOM 2179 O OE1 . GLU A 1 281 ? 24.656 -18.965 -7.396 1.00 25.18 ? 281 GLU A OE1 1 ATOM 2180 O OE2 . GLU A 1 281 ? 23.244 -20.646 -7.449 1.00 27.77 ? 281 GLU A OE2 1 ATOM 2181 N N . LYS A 1 282 ? 22.969 -15.786 -3.666 1.00 11.52 ? 282 LYS A N 1 ATOM 2182 C CA . LYS A 1 282 ? 23.900 -15.578 -2.576 1.00 12.90 ? 282 LYS A CA 1 ATOM 2183 C C . LYS A 1 282 ? 23.981 -14.093 -2.269 1.00 10.99 ? 282 LYS A C 1 ATOM 2184 O O . LYS A 1 282 ? 23.902 -13.262 -3.168 1.00 11.43 ? 282 LYS A O 1 ATOM 2185 C CB . LYS A 1 282 ? 25.327 -16.040 -2.976 1.00 14.24 ? 282 LYS A CB 1 ATOM 2186 C CG . LYS A 1 282 ? 25.511 -17.489 -3.371 1.00 18.24 ? 282 LYS A CG 1 ATOM 2187 C CD . LYS A 1 282 ? 26.905 -17.727 -3.882 1.00 19.34 ? 282 LYS A CD 1 ATOM 2188 C CE . LYS A 1 282 ? 27.095 -19.142 -4.419 1.00 24.02 ? 282 LYS A CE 1 ATOM 2189 N NZ . LYS A 1 282 ? 26.379 -20.106 -3.561 1.00 28.78 ? 282 LYS A NZ 1 ATOM 2190 N N . ILE A 1 283 ? 24.191 -13.772 -1.000 1.00 10.33 ? 283 ILE A N 1 ATOM 2191 C CA . ILE A 1 283 ? 24.455 -12.392 -0.586 1.00 10.26 ? 283 ILE A CA 1 ATOM 2192 C C . ILE A 1 283 ? 25.810 -12.402 0.087 1.00 10.93 ? 283 ILE A C 1 ATOM 2193 O O . ILE A 1 283 ? 26.055 -13.208 1.002 1.00 10.32 ? 283 ILE A O 1 ATOM 2194 C CB . ILE A 1 283 ? 23.376 -11.869 0.384 1.00 10.12 ? 283 ILE A CB 1 ATOM 2195 C CG1 . ILE A 1 283 ? 21.975 -11.943 -0.229 1.00 10.71 ? 283 ILE A CG1 1 ATOM 2196 C CG2 . ILE A 1 283 ? 23.729 -10.428 0.849 1.00 11.84 ? 283 ILE A CG2 1 ATOM 2197 C CD1 . ILE A 1 283 ? 20.853 -11.720 0.737 1.00 11.23 ? 283 ILE A CD1 1 ATOM 2198 N N . HIS A 1 284 ? 26.698 -11.521 -0.390 1.00 10.85 ? 284 HIS A N 1 ATOM 2199 C CA . HIS A 1 284 ? 28.118 -11.536 0.006 1.00 10.40 ? 284 HIS A CA 1 ATOM 2200 C C . HIS A 1 284 ? 28.516 -10.171 0.616 1.00 10.15 ? 284 HIS A C 1 ATOM 2201 O O . HIS A 1 284 ? 28.337 -9.113 -0.033 1.00 10.96 ? 284 HIS A O 1 ATOM 2202 C CB . HIS A 1 284 ? 28.948 -11.784 -1.245 1.00 10.78 ? 284 HIS A CB 1 ATOM 2203 C CG . HIS A 1 284 ? 30.434 -11.785 -1.056 1.00 11.95 ? 284 HIS A CG 1 ATOM 2204 N ND1 . HIS A 1 284 ? 31.276 -11.370 -2.061 1.00 12.08 ? 284 HIS A ND1 1 ATOM 2205 C CD2 . HIS A 1 284 ? 31.225 -12.200 -0.042 1.00 11.08 ? 284 HIS A CD2 1 ATOM 2206 C CE1 . HIS A 1 284 ? 32.530 -11.524 -1.662 1.00 13.12 ? 284 HIS A CE1 1 ATOM 2207 N NE2 . HIS A 1 284 ? 32.531 -12.030 -0.446 1.00 12.40 ? 284 HIS A NE2 1 ATOM 2208 N N . ARG A 1 285 ? 28.990 -10.211 1.861 1.00 9.59 ? 285 ARG A N 1 ATOM 2209 C CA . ARG A 1 285 ? 29.416 -9.014 2.593 1.00 9.80 ? 285 ARG A CA 1 ATOM 2210 C C . ARG A 1 285 ? 30.908 -9.059 2.868 1.00 10.51 ? 285 ARG A C 1 ATOM 2211 O O . ARG A 1 285 ? 31.403 -10.010 3.472 1.00 10.87 ? 285 ARG A O 1 ATOM 2212 C CB . ARG A 1 285 ? 28.670 -8.932 3.918 1.00 10.18 ? 285 ARG A CB 1 ATOM 2213 C CG . ARG A 1 285 ? 29.281 -7.974 4.947 1.00 10.47 ? 285 ARG A CG 1 ATOM 2214 C CD . ARG A 1 285 ? 29.419 -6.548 4.499 1.00 10.73 ? 285 ARG A CD 1 ATOM 2215 N NE . ARG A 1 285 ? 28.116 -5.971 4.185 1.00 8.49 ? 285 ARG A NE 1 ATOM 2216 C CZ . ARG A 1 285 ? 27.241 -5.596 5.099 1.00 10.31 ? 285 ARG A CZ 1 ATOM 2217 N NH1 . ARG A 1 285 ? 27.521 -5.669 6.388 1.00 9.96 ? 285 ARG A NH1 1 ATOM 2218 N NH2 . ARG A 1 285 ? 26.076 -5.104 4.717 1.00 10.91 ? 285 ARG A NH2 1 ATOM 2219 N N . PHE A 1 286 ? 31.605 -8.012 2.443 1.00 10.36 ? 286 PHE A N 1 ATOM 2220 C CA . PHE A 1 286 ? 33.010 -7.843 2.832 1.00 10.57 ? 286 PHE A CA 1 ATOM 2221 C C . PHE A 1 286 ? 33.256 -6.362 3.080 1.00 10.94 ? 286 PHE A C 1 ATOM 2222 O O . PHE A 1 286 ? 32.337 -5.547 2.910 1.00 11.59 ? 286 PHE A O 1 ATOM 2223 C CB . PHE A 1 286 ? 33.973 -8.489 1.812 1.00 11.65 ? 286 PHE A CB 1 ATOM 2224 C CG . PHE A 1 286 ? 33.904 -7.920 0.435 1.00 11.56 ? 286 PHE A CG 1 ATOM 2225 C CD1 . PHE A 1 286 ? 33.040 -8.439 -0.509 1.00 12.98 ? 286 PHE A CD1 1 ATOM 2226 C CD2 . PHE A 1 286 ? 34.752 -6.886 0.049 1.00 13.09 ? 286 PHE A CD2 1 ATOM 2227 C CE1 . PHE A 1 286 ? 32.992 -7.915 -1.779 1.00 14.64 ? 286 PHE A CE1 1 ATOM 2228 C CE2 . PHE A 1 286 ? 34.692 -6.362 -1.247 1.00 13.62 ? 286 PHE A CE2 1 ATOM 2229 C CZ . PHE A 1 286 ? 33.802 -6.892 -2.143 1.00 14.67 ? 286 PHE A CZ 1 ATOM 2230 N N . TYR A 1 287 ? 34.459 -6.014 3.526 1.00 10.36 ? 287 TYR A N 1 ATOM 2231 C CA . TYR A 1 287 ? 34.718 -4.678 3.992 1.00 10.82 ? 287 TYR A CA 1 ATOM 2232 C C . TYR A 1 287 ? 36.000 -4.158 3.349 1.00 10.97 ? 287 TYR A C 1 ATOM 2233 O O . TYR A 1 287 ? 36.763 -4.918 2.749 1.00 12.85 ? 287 TYR A O 1 ATOM 2234 C CB . TYR A 1 287 ? 34.820 -4.662 5.527 1.00 10.16 ? 287 TYR A CB 1 ATOM 2235 C CG . TYR A 1 287 ? 33.560 -5.151 6.246 1.00 10.07 ? 287 TYR A CG 1 ATOM 2236 C CD1 . TYR A 1 287 ? 33.282 -6.502 6.392 1.00 10.41 ? 287 TYR A CD1 1 ATOM 2237 C CD2 . TYR A 1 287 ? 32.613 -4.239 6.722 1.00 9.99 ? 287 TYR A CD2 1 ATOM 2238 C CE1 . TYR A 1 287 ? 32.113 -6.936 7.012 1.00 9.73 ? 287 TYR A CE1 1 ATOM 2239 C CE2 . TYR A 1 287 ? 31.463 -4.665 7.333 1.00 10.14 ? 287 TYR A CE2 1 ATOM 2240 C CZ . TYR A 1 287 ? 31.206 -6.009 7.477 1.00 9.18 ? 287 TYR A CZ 1 ATOM 2241 O OH . TYR A 1 287 ? 30.031 -6.453 8.061 1.00 10.29 ? 287 TYR A OH 1 ATOM 2242 N N . VAL A 1 288 ? 36.239 -2.863 3.467 1.00 11.55 ? 288 VAL A N 1 ATOM 2243 C CA . VAL A 1 288 ? 37.528 -2.254 3.075 1.00 12.41 ? 288 VAL A CA 1 ATOM 2244 C C . VAL A 1 288 ? 37.873 -1.258 4.173 1.00 13.21 ? 288 VAL A C 1 ATOM 2245 O O . VAL A 1 288 ? 37.018 -0.484 4.636 1.00 12.81 ? 288 VAL A O 1 ATOM 2246 C CB . VAL A 1 288 ? 37.482 -1.497 1.731 1.00 13.01 ? 288 VAL A CB 1 ATOM 2247 C CG1 . VAL A 1 288 ? 38.876 -1.099 1.268 1.00 14.24 ? 288 VAL A CG1 1 ATOM 2248 C CG2 . VAL A 1 288 ? 36.816 -2.304 0.628 1.00 13.27 ? 288 VAL A CG2 1 ATOM 2249 N N . GLN A 1 289 ? 39.122 -1.263 4.626 1.00 13.58 ? 289 GLN A N 1 ATOM 2250 C CA . GLN A 1 289 ? 39.548 -0.309 5.659 1.00 14.95 ? 289 GLN A CA 1 ATOM 2251 C C . GLN A 1 289 ? 41.018 -0.029 5.435 1.00 16.28 ? 289 GLN A C 1 ATOM 2252 O O . GLN A 1 289 ? 41.799 -0.954 5.158 1.00 15.97 ? 289 GLN A O 1 ATOM 2253 C CB . GLN A 1 289 ? 39.266 -0.837 7.079 1.00 14.08 ? 289 GLN A CB 1 ATOM 2254 C CG . GLN A 1 289 ? 39.494 0.212 8.205 1.00 14.32 ? 289 GLN A CG 1 ATOM 2255 C CD . GLN A 1 289 ? 39.042 -0.234 9.581 1.00 13.07 ? 289 GLN A CD 1 ATOM 2256 O OE1 . GLN A 1 289 ? 39.346 -1.345 10.032 1.00 14.89 ? 289 GLN A OE1 1 ATOM 2257 N NE2 . GLN A 1 289 ? 38.309 0.653 10.273 1.00 12.59 ? 289 GLN A NE2 1 ATOM 2258 N N . ASP A 1 290 ? 41.374 1.246 5.540 1.00 17.99 ? 290 ASP A N 1 ATOM 2259 C CA . ASP A 1 290 ? 42.759 1.703 5.337 1.00 19.58 ? 290 ASP A CA 1 ATOM 2260 C C . ASP A 1 290 ? 43.243 1.255 3.962 1.00 19.94 ? 290 ASP A C 1 ATOM 2261 O O . ASP A 1 290 ? 44.427 0.954 3.766 1.00 22.19 ? 290 ASP A O 1 ATOM 2262 C CB . ASP A 1 290 ? 43.647 1.208 6.479 1.00 21.11 ? 290 ASP A CB 1 ATOM 2263 C CG . ASP A 1 290 ? 43.199 1.724 7.839 1.00 24.34 ? 290 ASP A CG 1 ATOM 2264 O OD1 . ASP A 1 290 ? 42.841 2.910 7.959 1.00 30.12 ? 290 ASP A OD1 1 ATOM 2265 O OD2 . ASP A 1 290 ? 43.147 1.006 8.853 1.00 31.41 ? 290 ASP A OD2 1 ATOM 2266 N N . GLY A 1 291 ? 42.338 1.255 2.997 1.00 20.14 ? 291 GLY A N 1 ATOM 2267 C CA . GLY A 1 291 ? 42.680 0.944 1.618 1.00 20.59 ? 291 GLY A CA 1 ATOM 2268 C C . GLY A 1 291 ? 42.872 -0.531 1.307 1.00 20.85 ? 291 GLY A C 1 ATOM 2269 O O . GLY A 1 291 ? 43.247 -0.858 0.188 1.00 23.47 ? 291 GLY A O 1 ATOM 2270 N N . LYS A 1 292 ? 42.628 -1.409 2.278 1.00 19.85 ? 292 LYS A N 1 ATOM 2271 C CA . LYS A 1 292 ? 42.814 -2.852 2.121 1.00 20.26 ? 292 LYS A CA 1 ATOM 2272 C C . LYS A 1 292 ? 41.463 -3.543 2.134 1.00 18.34 ? 292 LYS A C 1 ATOM 2273 O O . LYS A 1 292 ? 40.654 -3.299 3.019 1.00 17.16 ? 292 LYS A O 1 ATOM 2274 C CB . LYS A 1 292 ? 43.633 -3.415 3.273 1.00 21.85 ? 292 LYS A CB 1 ATOM 2275 C CG . LYS A 1 292 ? 45.055 -2.924 3.289 1.00 23.78 ? 292 LYS A CG 1 ATOM 2276 C CD . LYS A 1 292 ? 45.766 -3.391 4.527 1.00 24.97 ? 292 LYS A CD 1 ATOM 2277 C CE . LYS A 1 292 ? 47.017 -2.586 4.756 1.00 27.91 ? 292 LYS A CE 1 ATOM 2278 N NZ . LYS A 1 292 ? 47.772 -2.502 3.493 1.00 31.37 ? 292 LYS A NZ 1 ATOM 2279 N N . VAL A 1 293 ? 41.240 -4.429 1.176 1.00 17.78 ? 293 VAL A N 1 ATOM 2280 C CA . VAL A 1 293 ? 40.063 -5.289 1.188 1.00 17.39 ? 293 VAL A CA 1 ATOM 2281 C C . VAL A 1 293 ? 40.176 -6.304 2.316 1.00 16.27 ? 293 VAL A C 1 ATOM 2282 O O . VAL A 1 293 ? 41.221 -6.960 2.510 1.00 17.31 ? 293 VAL A O 1 ATOM 2283 C CB . VAL A 1 293 ? 39.885 -6.008 -0.157 1.00 17.86 ? 293 VAL A CB 1 ATOM 2284 C CG1 . VAL A 1 293 ? 38.769 -7.058 -0.095 1.00 18.64 ? 293 VAL A CG1 1 ATOM 2285 C CG2 . VAL A 1 293 ? 39.622 -5.001 -1.251 1.00 18.40 ? 293 VAL A CG2 1 ATOM 2286 N N . ILE A 1 294 ? 39.098 -6.415 3.083 1.00 15.08 ? 294 ILE A N 1 ATOM 2287 C CA . ILE A 1 294 ? 38.966 -7.373 4.154 1.00 14.74 ? 294 ILE A CA 1 ATOM 2288 C C . ILE A 1 294 ? 37.899 -8.356 3.720 1.00 14.33 ? 294 ILE A C 1 ATOM 2289 O O . ILE A 1 294 ? 36.721 -8.054 3.740 1.00 14.16 ? 294 ILE A O 1 ATOM 2290 C CB . ILE A 1 294 ? 38.584 -6.665 5.460 1.00 15.19 ? 294 ILE A CB 1 ATOM 2291 C CG1 . ILE A 1 294 ? 39.674 -5.660 5.831 1.00 15.62 ? 294 ILE A CG1 1 ATOM 2292 C CG2 . ILE A 1 294 ? 38.379 -7.656 6.581 1.00 14.51 ? 294 ILE A CG2 1 ATOM 2293 C CD1 . ILE A 1 294 ? 39.204 -4.552 6.695 1.00 16.40 ? 294 ILE A CD1 1 ATOM 2294 N N . GLU A 1 295 ? 38.311 -9.536 3.307 1.00 13.42 ? 295 GLU A N 1 ATOM 2295 C CA . GLU A 1 295 ? 37.383 -10.527 2.816 1.00 13.72 ? 295 GLU A CA 1 ATOM 2296 C C . GLU A 1 295 ? 36.448 -10.984 3.916 1.00 12.60 ? 295 GLU A C 1 ATOM 2297 O O . GLU A 1 295 ? 36.754 -10.907 5.103 1.00 13.23 ? 295 GLU A O 1 ATOM 2298 C CB . GLU A 1 295 ? 38.166 -11.724 2.234 1.00 14.37 ? 295 GLU A CB 1 ATOM 2299 C CG . GLU A 1 295 ? 39.057 -11.398 1.040 1.00 17.34 ? 295 GLU A CG 1 ATOM 2300 C CD . GLU A 1 295 ? 38.338 -11.013 -0.248 1.00 20.75 ? 295 GLU A CD 1 ATOM 2301 O OE1 . GLU A 1 295 ? 37.087 -11.086 -0.351 1.00 21.74 ? 295 GLU A OE1 1 ATOM 2302 O OE2 . GLU A 1 295 ? 39.038 -10.626 -1.214 1.00 23.81 ? 295 GLU A OE2 1 ATOM 2303 N N . SER A 1 296 ? 35.280 -11.479 3.531 1.00 11.84 ? 296 SER A N 1 ATOM 2304 C CA . SER A 1 296 ? 34.390 -12.049 4.509 1.00 12.29 ? 296 SER A CA 1 ATOM 2305 C C . SER A 1 296 ? 35.051 -13.192 5.256 1.00 11.96 ? 296 SER A C 1 ATOM 2306 O O . SER A 1 296 ? 35.822 -13.974 4.672 1.00 12.66 ? 296 SER A O 1 ATOM 2307 C CB . SER A 1 296 ? 33.125 -12.583 3.829 1.00 13.00 ? 296 SER A CB 1 ATOM 2308 O OG . SER A 1 296 ? 32.200 -13.018 4.814 1.00 12.37 ? 296 SER A OG 1 ATOM 2309 N N . PHE A 1 297 ? 34.713 -13.312 6.534 1.00 11.97 ? 297 PHE A N 1 ATOM 2310 C CA . PHE A 1 297 ? 34.908 -14.555 7.270 1.00 11.75 ? 297 PHE A CA 1 ATOM 2311 C C . PHE A 1 297 ? 34.107 -15.662 6.615 1.00 12.06 ? 297 PHE A C 1 ATOM 2312 O O . PHE A 1 297 ? 33.142 -15.405 5.870 1.00 12.02 ? 297 PHE A O 1 ATOM 2313 C CB . PHE A 1 297 ? 34.447 -14.420 8.724 1.00 12.32 ? 297 PHE A CB 1 ATOM 2314 C CG . PHE A 1 297 ? 33.022 -13.945 8.862 1.00 11.75 ? 297 PHE A CG 1 ATOM 2315 C CD1 . PHE A 1 297 ? 31.975 -14.834 8.916 1.00 12.24 ? 297 PHE A CD1 1 ATOM 2316 C CD2 . PHE A 1 297 ? 32.757 -12.593 8.901 1.00 11.76 ? 297 PHE A CD2 1 ATOM 2317 C CE1 . PHE A 1 297 ? 30.667 -14.365 9.033 1.00 11.64 ? 297 PHE A CE1 1 ATOM 2318 C CE2 . PHE A 1 297 ? 31.453 -12.131 8.995 1.00 12.65 ? 297 PHE A CE2 1 ATOM 2319 C CZ . PHE A 1 297 ? 30.419 -13.021 9.057 1.00 13.00 ? 297 PHE A CZ 1 ATOM 2320 N N . TYR A 1 298 ? 34.534 -16.882 6.916 1.00 12.28 ? 298 TYR A N 1 ATOM 2321 C CA . TYR A 1 298 ? 33.763 -18.091 6.685 1.00 12.59 ? 298 TYR A CA 1 ATOM 2322 C C . TYR A 1 298 ? 33.162 -18.507 8.026 1.00 12.26 ? 298 TYR A C 1 ATOM 2323 O O . TYR A 1 298 ? 33.739 -18.256 9.113 1.00 13.15 ? 298 TYR A O 1 ATOM 2324 C CB . TYR A 1 298 ? 34.641 -19.220 6.108 1.00 12.63 ? 298 TYR A CB 1 ATOM 2325 C CG . TYR A 1 298 ? 35.050 -18.997 4.676 1.00 13.39 ? 298 TYR A CG 1 ATOM 2326 C CD1 . TYR A 1 298 ? 36.063 -18.085 4.342 1.00 14.34 ? 298 TYR A CD1 1 ATOM 2327 C CD2 . TYR A 1 298 ? 34.439 -19.717 3.628 1.00 14.59 ? 298 TYR A CD2 1 ATOM 2328 C CE1 . TYR A 1 298 ? 36.457 -17.904 3.035 1.00 14.95 ? 298 TYR A CE1 1 ATOM 2329 C CE2 . TYR A 1 298 ? 34.841 -19.523 2.308 1.00 14.99 ? 298 TYR A CE2 1 ATOM 2330 C CZ . TYR A 1 298 ? 35.841 -18.612 2.020 1.00 14.31 ? 298 TYR A CZ 1 ATOM 2331 O OH . TYR A 1 298 ? 36.245 -18.366 0.700 1.00 17.39 ? 298 TYR A OH 1 ATOM 2332 N N . THR A 1 299 ? 32.019 -19.187 7.982 1.00 12.34 ? 299 THR A N 1 ATOM 2333 C CA . THR A 1 299 ? 31.443 -19.757 9.166 1.00 12.52 ? 299 THR A CA 1 ATOM 2334 C C . THR A 1 299 ? 32.460 -20.720 9.801 1.00 13.52 ? 299 THR A C 1 ATOM 2335 O O . THR A 1 299 ? 33.345 -21.274 9.110 1.00 14.70 ? 299 THR A O 1 ATOM 2336 C CB . THR A 1 299 ? 30.155 -20.495 8.865 1.00 12.14 ? 299 THR A CB 1 ATOM 2337 O OG1 . THR A 1 299 ? 30.400 -21.584 7.950 1.00 11.84 ? 299 THR A OG1 1 ATOM 2338 C CG2 . THR A 1 299 ? 29.090 -19.597 8.211 1.00 12.01 ? 299 THR A CG2 1 ATOM 2339 N N . ASN A 1 300 ? 32.364 -20.871 11.113 1.00 13.83 ? 300 ASN A N 1 ATOM 2340 C CA . ASN A 1 300 ? 33.404 -21.574 11.872 1.00 14.01 ? 300 ASN A CA 1 ATOM 2341 C C . ASN A 1 300 ? 32.766 -22.363 12.996 1.00 14.51 ? 300 ASN A C 1 ATOM 2342 O O . ASN A 1 300 ? 33.323 -22.433 14.092 1.00 15.27 ? 300 ASN A O 1 ATOM 2343 C CB . ASN A 1 300 ? 34.407 -20.548 12.399 1.00 14.71 ? 300 ASN A CB 1 ATOM 2344 C CG . ASN A 1 300 ? 35.630 -21.181 13.012 1.00 15.63 ? 300 ASN A CG 1 ATOM 2345 O OD1 . ASN A 1 300 ? 36.263 -22.023 12.387 1.00 18.28 ? 300 ASN A OD1 1 ATOM 2346 N ND2 . ASN A 1 300 ? 35.997 -20.752 14.230 1.00 17.74 ? 300 ASN A ND2 1 ATOM 2347 N N . LYS A 1 301 ? 31.609 -22.969 12.737 1.00 15.33 ? 301 LYS A N 1 ATOM 2348 C CA . LYS A 1 301 ? 30.744 -23.494 13.792 1.00 15.91 ? 301 LYS A CA 1 ATOM 2349 C C . LYS A 1 301 ? 30.195 -24.884 13.482 1.00 16.27 ? 301 LYS A C 1 ATOM 2350 O O . LYS A 1 301 ? 29.592 -25.099 12.439 1.00 15.57 ? 301 LYS A O 1 ATOM 2351 C CB . LYS A 1 301 ? 29.575 -22.541 14.054 1.00 16.78 ? 301 LYS A CB 1 ATOM 2352 C CG . LYS A 1 301 ? 28.714 -22.958 15.255 1.00 16.43 ? 301 LYS A CG 1 ATOM 2353 C CD . LYS A 1 301 ? 27.753 -21.868 15.686 1.00 17.81 ? 301 LYS A CD 1 ATOM 2354 C CE . LYS A 1 301 ? 26.804 -22.338 16.782 1.00 19.15 ? 301 LYS A CE 1 ATOM 2355 N NZ . LYS A 1 301 ? 27.541 -22.837 17.988 1.00 19.86 ? 301 LYS A NZ 1 ATOM 2356 N N . GLU A 1 302 ? 30.349 -25.814 14.423 1.00 16.97 ? 302 GLU A N 1 ATOM 2357 C CA . GLU A 1 302 ? 29.853 -27.168 14.227 1.00 17.81 ? 302 GLU A CA 1 ATOM 2358 C C . GLU A 1 302 ? 28.361 -27.145 13.929 1.00 17.31 ? 302 GLU A C 1 ATOM 2359 O O . GLU A 1 302 ? 27.584 -26.471 14.618 1.00 18.29 ? 302 GLU A O 1 ATOM 2360 C CB . GLU A 1 302 ? 30.125 -28.032 15.466 1.00 18.81 ? 302 GLU A CB 1 ATOM 2361 C CG . GLU A 1 302 ? 31.585 -28.341 15.719 1.00 19.93 ? 302 GLU A CG 1 ATOM 2362 C CD . GLU A 1 302 ? 31.811 -29.177 16.980 1.00 21.67 ? 302 GLU A CD 1 ATOM 2363 O OE1 . GLU A 1 302 ? 30.898 -29.918 17.390 1.00 26.03 ? 302 GLU A OE1 1 ATOM 2364 O OE2 . GLU A 1 302 ? 32.909 -29.061 17.532 1.00 26.33 ? 302 GLU A OE2 1 ATOM 2365 N N . GLY A 1 303 ? 27.956 -27.864 12.886 1.00 17.19 ? 303 GLY A N 1 ATOM 2366 C CA . GLY A 1 303 ? 26.572 -27.950 12.500 1.00 16.75 ? 303 GLY A CA 1 ATOM 2367 C C . GLY A 1 303 ? 26.097 -26.853 11.566 1.00 16.78 ? 303 GLY A C 1 ATOM 2368 O O . GLY A 1 303 ? 24.937 -26.876 11.129 1.00 17.00 ? 303 GLY A O 1 ATOM 2369 N N . VAL A 1 304 ? 26.968 -25.897 11.266 1.00 15.07 ? 304 VAL A N 1 ATOM 2370 C CA . VAL A 1 304 ? 26.654 -24.802 10.345 1.00 15.51 ? 304 VAL A CA 1 ATOM 2371 C C . VAL A 1 304 ? 27.441 -25.054 9.074 1.00 14.82 ? 304 VAL A C 1 ATOM 2372 O O . VAL A 1 304 ? 28.663 -25.215 9.115 1.00 13.74 ? 304 VAL A O 1 ATOM 2373 C CB . VAL A 1 304 ? 27.054 -23.438 10.915 1.00 15.54 ? 304 VAL A CB 1 ATOM 2374 C CG1 . VAL A 1 304 ? 26.740 -22.319 9.913 1.00 15.45 ? 304 VAL A CG1 1 ATOM 2375 C CG2 . VAL A 1 304 ? 26.374 -23.187 12.245 1.00 16.89 ? 304 VAL A CG2 1 ATOM 2376 N N . PRO A 1 305 ? 26.788 -25.035 7.928 1.00 15.03 ? 305 PRO A N 1 ATOM 2377 C CA . PRO A 1 305 ? 27.478 -25.223 6.670 1.00 15.12 ? 305 PRO A CA 1 ATOM 2378 C C . PRO A 1 305 ? 28.644 -24.261 6.500 1.00 14.79 ? 305 PRO A C 1 ATOM 2379 O O . PRO A 1 305 ? 28.505 -23.110 6.886 1.00 15.19 ? 305 PRO A O 1 ATOM 2380 C CB . PRO A 1 305 ? 26.387 -24.910 5.645 1.00 16.07 ? 305 PRO A CB 1 ATOM 2381 C CG . PRO A 1 305 ? 25.105 -25.195 6.373 1.00 16.78 ? 305 PRO A CG 1 ATOM 2382 C CD . PRO A 1 305 ? 25.337 -24.816 7.750 1.00 15.55 ? 305 PRO A CD 1 ATOM 2383 N N . TYR A 1 306 ? 29.770 -24.731 5.957 1.00 14.32 ? 306 TYR A N 1 ATOM 2384 C CA . TYR A 1 306 ? 30.959 -23.910 5.746 1.00 13.75 ? 306 TYR A CA 1 ATOM 2385 C C . TYR A 1 306 ? 30.676 -23.004 4.556 1.00 13.50 ? 306 TYR A C 1 ATOM 2386 O O . TYR A 1 306 ? 30.514 -23.489 3.434 1.00 14.70 ? 306 TYR A O 1 ATOM 2387 C CB . TYR A 1 306 ? 32.211 -24.786 5.499 1.00 13.80 ? 306 TYR A CB 1 ATOM 2388 C CG . TYR A 1 306 ? 33.480 -23.980 5.500 1.00 13.49 ? 306 TYR A CG 1 ATOM 2389 C CD1 . TYR A 1 306 ? 34.028 -23.516 6.696 1.00 14.17 ? 306 TYR A CD1 1 ATOM 2390 C CD2 . TYR A 1 306 ? 34.099 -23.624 4.305 1.00 13.16 ? 306 TYR A CD2 1 ATOM 2391 C CE1 . TYR A 1 306 ? 35.174 -22.724 6.700 1.00 13.66 ? 306 TYR A CE1 1 ATOM 2392 C CE2 . TYR A 1 306 ? 35.241 -22.851 4.299 1.00 12.92 ? 306 TYR A CE2 1 ATOM 2393 C CZ . TYR A 1 306 ? 35.802 -22.432 5.485 1.00 13.75 ? 306 TYR A CZ 1 ATOM 2394 O OH . TYR A 1 306 ? 36.931 -21.662 5.449 1.00 15.16 ? 306 TYR A OH 1 ATOM 2395 N N . THR A 1 307 ? 30.630 -21.687 4.791 1.00 12.17 ? 307 THR A N 1 ATOM 2396 C CA . THR A 1 307 ? 30.286 -20.750 3.744 1.00 12.73 ? 307 THR A CA 1 ATOM 2397 C C . THR A 1 307 ? 30.795 -19.370 4.123 1.00 11.53 ? 307 THR A C 1 ATOM 2398 O O . THR A 1 307 ? 30.931 -19.072 5.311 1.00 12.28 ? 307 THR A O 1 ATOM 2399 C CB . THR A 1 307 ? 28.733 -20.731 3.529 1.00 12.68 ? 307 THR A CB 1 ATOM 2400 O OG1 . THR A 1 307 ? 28.387 -19.810 2.493 1.00 14.13 ? 307 THR A OG1 1 ATOM 2401 C CG2 . THR A 1 307 ? 27.958 -20.239 4.763 1.00 13.78 ? 307 THR A CG2 1 ATOM 2402 N N . ASN A 1 308 ? 31.034 -18.518 3.127 1.00 11.89 ? 308 ASN A N 1 ATOM 2403 C CA . ASN A 1 308 ? 31.325 -17.091 3.340 1.00 11.83 ? 308 ASN A CA 1 ATOM 2404 C C . ASN A 1 308 ? 30.213 -16.192 2.783 1.00 12.81 ? 308 ASN A C 1 ATOM 2405 O O . ASN A 1 308 ? 30.414 -14.988 2.635 1.00 12.26 ? 308 ASN A O 1 ATOM 2406 C CB . ASN A 1 308 ? 32.681 -16.698 2.735 1.00 12.49 ? 308 ASN A CB 1 ATOM 2407 C CG . ASN A 1 308 ? 32.738 -16.864 1.247 1.00 12.82 ? 308 ASN A CG 1 ATOM 2408 O OD1 . ASN A 1 308 ? 31.897 -17.537 0.633 1.00 13.32 ? 308 ASN A OD1 1 ATOM 2409 N ND2 . ASN A 1 308 ? 33.759 -16.245 0.634 1.00 12.61 ? 308 ASN A ND2 1 ATOM 2410 N N . MET A 1 309 ? 29.059 -16.779 2.491 1.00 11.76 ? 309 MET A N 1 ATOM 2411 C CA . MET A 1 309 ? 27.938 -16.035 1.928 1.00 12.00 ? 309 MET A CA 1 ATOM 2412 C C . MET A 1 309 ? 26.607 -16.562 2.465 1.00 11.03 ? 309 MET A C 1 ATOM 2413 O O . MET A 1 309 ? 26.474 -17.752 2.791 1.00 11.26 ? 309 MET A O 1 ATOM 2414 C CB . MET A 1 309 ? 27.958 -16.098 0.402 1.00 12.93 ? 309 MET A CB 1 ATOM 2415 C CG . MET A 1 309 ? 29.237 -15.528 -0.228 1.00 14.35 ? 309 MET A CG 1 ATOM 2416 S SD . MET A 1 309 ? 29.149 -15.557 -1.979 1.00 15.83 ? 309 MET A SD 1 ATOM 2417 C CE . MET A 1 309 ? 30.811 -15.192 -2.363 1.00 15.39 ? 309 MET A CE 1 ATOM 2418 N N . ILE A 1 310 ? 25.613 -15.670 2.518 1.00 10.58 ? 310 ILE A N 1 ATOM 2419 C CA . ILE A 1 310 ? 24.251 -16.054 2.868 1.00 10.94 ? 310 ILE A CA 1 ATOM 2420 C C . ILE A 1 310 ? 23.622 -16.761 1.660 1.00 11.28 ? 310 ILE A C 1 ATOM 2421 O O . ILE A 1 310 ? 23.644 -16.221 0.544 1.00 11.91 ? 310 ILE A O 1 ATOM 2422 C CB . ILE A 1 310 ? 23.415 -14.798 3.259 1.00 10.55 ? 310 ILE A CB 1 ATOM 2423 C CG1 . ILE A 1 310 ? 24.088 -14.009 4.376 1.00 11.16 ? 310 ILE A CG1 1 ATOM 2424 C CG2 . ILE A 1 310 ? 22.003 -15.179 3.702 1.00 12.76 ? 310 ILE A CG2 1 ATOM 2425 C CD1 . ILE A 1 310 ? 23.408 -12.637 4.599 1.00 11.90 ? 310 ILE A CD1 1 ATOM 2426 N N . ASP A 1 311 ? 23.055 -17.943 1.885 1.00 11.12 ? 311 ASP A N 1 ATOM 2427 C CA . ASP A 1 311 ? 22.321 -18.662 0.854 1.00 10.76 ? 311 ASP A CA 1 ATOM 2428 C C . ASP A 1 311 ? 21.289 -19.562 1.505 1.00 9.97 ? 311 ASP A C 1 ATOM 2429 O O . ASP A 1 311 ? 21.225 -19.645 2.741 1.00 9.96 ? 311 ASP A O 1 ATOM 2430 C CB . ASP A 1 311 ? 23.251 -19.400 -0.110 1.00 10.34 ? 311 ASP A CB 1 ATOM 2431 C CG . ASP A 1 311 ? 24.105 -20.481 0.534 1.00 11.41 ? 311 ASP A CG 1 ATOM 2432 O OD1 . ASP A 1 311 ? 23.858 -20.931 1.658 1.00 11.91 ? 311 ASP A OD1 1 ATOM 2433 O OD2 . ASP A 1 311 ? 25.050 -20.971 -0.125 1.00 14.12 ? 311 ASP A OD2 1 ATOM 2434 N N . ASP A 1 312 ? 20.468 -20.235 0.692 1.00 9.75 ? 312 ASP A N 1 ATOM 2435 C CA . ASP A 1 312 ? 19.430 -21.085 1.241 1.00 10.51 ? 312 ASP A CA 1 ATOM 2436 C C . ASP A 1 312 ? 19.981 -22.185 2.151 1.00 10.56 ? 312 ASP A C 1 ATOM 2437 O O . ASP A 1 312 ? 19.394 -22.485 3.173 1.00 11.39 ? 312 ASP A O 1 ATOM 2438 C CB . ASP A 1 312 ? 18.628 -21.715 0.117 1.00 9.20 ? 312 ASP A CB 1 ATOM 2439 C CG . ASP A 1 312 ? 17.609 -20.796 -0.495 1.00 11.17 ? 312 ASP A CG 1 ATOM 2440 O OD1 . ASP A 1 312 ? 17.389 -19.660 0.007 1.00 11.58 ? 312 ASP A OD1 1 ATOM 2441 O OD2 . ASP A 1 312 ? 16.980 -21.181 -1.519 1.00 12.26 ? 312 ASP A OD2 1 ATOM 2442 N N . GLU A 1 313 ? 21.085 -22.811 1.750 1.00 11.55 ? 313 GLU A N 1 ATOM 2443 C CA . GLU A 1 313 ? 21.669 -23.858 2.588 1.00 12.47 ? 313 GLU A CA 1 ATOM 2444 C C . GLU A 1 313 ? 21.963 -23.345 3.995 1.00 11.73 ? 313 GLU A C 1 ATOM 2445 O O . GLU A 1 313 ? 21.601 -23.974 4.995 1.00 12.76 ? 313 GLU A O 1 ATOM 2446 C CB . GLU A 1 313 ? 22.924 -24.428 1.939 1.00 13.33 ? 313 GLU A CB 1 ATOM 2447 C CG . GLU A 1 313 ? 23.588 -25.527 2.753 1.00 15.71 ? 313 GLU A CG 1 ATOM 2448 C CD . GLU A 1 313 ? 24.952 -25.955 2.249 1.00 18.71 ? 313 GLU A CD 1 ATOM 2449 O OE1 . GLU A 1 313 ? 25.762 -25.131 1.761 1.00 25.27 ? 313 GLU A OE1 1 ATOM 2450 O OE2 . GLU A 1 313 ? 25.255 -27.148 2.461 1.00 25.75 ? 313 GLU A OE2 1 ATOM 2451 N N . PHE A 1 314 ? 22.628 -22.194 4.061 1.00 11.08 ? 314 PHE A N 1 ATOM 2452 C CA . PHE A 1 314 ? 22.937 -21.595 5.340 1.00 10.86 ? 314 PHE A CA 1 ATOM 2453 C C . PHE A 1 314 ? 21.676 -21.219 6.122 1.00 10.44 ? 314 PHE A C 1 ATOM 2454 O O . PHE A 1 314 ? 21.551 -21.491 7.310 1.00 10.07 ? 314 PHE A O 1 ATOM 2455 C CB . PHE A 1 314 ? 23.824 -20.360 5.133 1.00 11.06 ? 314 PHE A CB 1 ATOM 2456 C CG . PHE A 1 314 ? 24.025 -19.545 6.382 1.00 10.35 ? 314 PHE A CG 1 ATOM 2457 C CD1 . PHE A 1 314 ? 24.962 -19.919 7.328 1.00 11.27 ? 314 PHE A CD1 1 ATOM 2458 C CD2 . PHE A 1 314 ? 23.243 -18.433 6.632 1.00 10.91 ? 314 PHE A CD2 1 ATOM 2459 C CE1 . PHE A 1 314 ? 25.123 -19.191 8.485 1.00 10.94 ? 314 PHE A CE1 1 ATOM 2460 C CE2 . PHE A 1 314 ? 23.408 -17.707 7.797 1.00 11.48 ? 314 PHE A CE2 1 ATOM 2461 C CZ . PHE A 1 314 ? 24.358 -18.085 8.716 1.00 11.38 ? 314 PHE A CZ 1 ATOM 2462 N N . CYS A 1 315 ? 20.740 -20.568 5.443 1.00 10.30 ? 315 CYS A N 1 ATOM 2463 C CA . CYS A 1 315 ? 19.536 -20.112 6.121 1.00 11.09 ? 315 CYS A CA 1 ATOM 2464 C C . CYS A 1 315 ? 18.694 -21.247 6.699 1.00 12.03 ? 315 CYS A C 1 ATOM 2465 O O . CYS A 1 315 ? 18.214 -21.173 7.827 1.00 12.64 ? 315 CYS A O 1 ATOM 2466 C CB . CYS A 1 315 ? 18.717 -19.213 5.205 1.00 11.29 ? 315 CYS A CB 1 ATOM 2467 S SG . CYS A 1 315 ? 19.620 -17.693 4.739 1.00 11.08 ? 315 CYS A SG 1 ATOM 2468 N N . GLU A 1 316 ? 18.542 -22.308 5.938 1.00 13.17 ? 316 GLU A N 1 ATOM 2469 C CA . GLU A 1 316 ? 17.803 -23.465 6.412 1.00 13.82 ? 316 GLU A CA 1 ATOM 2470 C C . GLU A 1 316 ? 18.500 -24.134 7.579 1.00 13.65 ? 316 GLU A C 1 ATOM 2471 O O . GLU A 1 316 ? 17.863 -24.487 8.556 1.00 14.00 ? 316 GLU A O 1 ATOM 2472 C CB . GLU A 1 316 ? 17.628 -24.474 5.280 1.00 15.14 ? 316 GLU A CB 1 ATOM 2473 C CG . GLU A 1 316 ? 16.574 -25.549 5.565 1.00 19.02 ? 316 GLU A CG 1 ATOM 2474 C CD . GLU A 1 316 ? 15.465 -25.540 4.542 1.00 26.43 ? 316 GLU A CD 1 ATOM 2475 O OE1 . GLU A 1 316 ? 15.724 -25.736 3.325 1.00 31.20 ? 316 GLU A OE1 1 ATOM 2476 O OE2 . GLU A 1 316 ? 14.313 -25.349 4.952 1.00 32.48 ? 316 GLU A OE2 1 ATOM 2477 N N . ALA A 1 317 ? 19.813 -24.302 7.481 1.00 13.36 ? 317 ALA A N 1 ATOM 2478 C CA . ALA A 1 317 ? 20.592 -25.003 8.512 1.00 14.08 ? 317 ALA A CA 1 ATOM 2479 C C . ALA A 1 317 ? 20.613 -24.254 9.829 1.00 14.28 ? 317 ALA A C 1 ATOM 2480 O O . ALA A 1 317 ? 20.729 -24.857 10.897 1.00 15.71 ? 317 ALA A O 1 ATOM 2481 C CB . ALA A 1 317 ? 22.002 -25.238 8.020 1.00 14.61 ? 317 ALA A CB 1 ATOM 2482 N N . THR A 1 318 ? 20.491 -22.932 9.781 1.00 14.15 ? 318 THR A N 1 ATOM 2483 C CA . THR A 1 318 ? 20.526 -22.109 10.990 1.00 13.48 ? 318 THR A CA 1 ATOM 2484 C C . THR A 1 318 ? 19.111 -21.808 11.527 1.00 13.72 ? 318 THR A C 1 ATOM 2485 O O . THR A 1 318 ? 18.931 -20.955 12.396 1.00 15.88 ? 318 THR A O 1 ATOM 2486 C CB . THR A 1 318 ? 21.333 -20.825 10.783 1.00 13.78 ? 318 THR A CB 1 ATOM 2487 O OG1 . THR A 1 318 ? 20.820 -20.094 9.665 1.00 14.13 ? 318 THR A OG1 1 ATOM 2488 C CG2 . THR A 1 318 ? 22.802 -21.130 10.453 1.00 14.52 ? 318 THR A CG2 1 ATOM 2489 N N . GLY A 1 319 ? 18.101 -22.501 11.006 1.00 12.93 ? 319 GLY A N 1 ATOM 2490 C CA . GLY A 1 319 ? 16.779 -22.429 11.591 1.00 12.30 ? 319 GLY A CA 1 ATOM 2491 C C . GLY A 1 319 ? 15.882 -21.281 11.145 1.00 12.24 ? 319 GLY A C 1 ATOM 2492 O O . GLY A 1 319 ? 14.923 -20.933 11.829 1.00 13.18 ? 319 GLY A O 1 ATOM 2493 N N . SER A 1 320 ? 16.200 -20.680 10.003 1.00 11.63 ? 320 SER A N 1 ATOM 2494 C CA . SER A 1 320 ? 15.452 -19.542 9.471 1.00 11.13 ? 320 SER A CA 1 ATOM 2495 C C . SER A 1 320 ? 14.211 -20.021 8.733 1.00 10.82 ? 320 SER A C 1 ATOM 2496 O O . SER A 1 320 ? 14.084 -19.876 7.521 1.00 11.26 ? 320 SER A O 1 ATOM 2497 C CB . SER A 1 320 ? 16.342 -18.719 8.541 1.00 11.57 ? 320 SER A CB 1 ATOM 2498 O OG . SER A 1 320 ? 17.571 -18.383 9.157 1.00 14.64 ? 320 SER A OG 1 ATOM 2499 N N . ARG A 1 321 ? 13.278 -20.602 9.485 1.00 10.76 ? 321 ARG A N 1 ATOM 2500 C CA . ARG A 1 321 ? 12.201 -21.346 8.876 1.00 10.45 ? 321 ARG A CA 1 ATOM 2501 C C . ARG A 1 321 ? 11.251 -20.442 8.113 1.00 9.89 ? 321 ARG A C 1 ATOM 2502 O O . ARG A 1 321 ? 10.880 -20.759 6.986 1.00 10.42 ? 321 ARG A O 1 ATOM 2503 C CB . ARG A 1 321 ? 11.453 -22.171 9.940 1.00 10.96 ? 321 ARG A CB 1 ATOM 2504 C CG . ARG A 1 321 ? 10.249 -22.898 9.377 1.00 12.36 ? 321 ARG A CG 1 ATOM 2505 C CD . ARG A 1 321 ? 9.640 -23.857 10.366 1.00 13.06 ? 321 ARG A CD 1 ATOM 2506 N NE . ARG A 1 321 ? 9.171 -23.202 11.587 1.00 13.08 ? 321 ARG A NE 1 ATOM 2507 C CZ . ARG A 1 321 ? 7.999 -22.585 11.733 1.00 13.42 ? 321 ARG A CZ 1 ATOM 2508 N NH1 . ARG A 1 321 ? 7.122 -22.501 10.736 1.00 13.30 ? 321 ARG A NH1 1 ATOM 2509 N NH2 . ARG A 1 321 ? 7.701 -22.042 12.910 1.00 14.65 ? 321 ARG A NH2 1 ATOM 2510 N N . LYS A 1 322 ? 10.818 -19.335 8.723 1.00 9.57 ? 322 LYS A N 1 ATOM 2511 C CA . LYS A 1 322 ? 9.877 -18.475 7.997 1.00 9.40 ? 322 LYS A CA 1 ATOM 2512 C C . LYS A 1 322 ? 10.521 -17.824 6.771 1.00 9.40 ? 322 LYS A C 1 ATOM 2513 O O . LYS A 1 322 ? 9.850 -17.615 5.769 1.00 9.08 ? 322 LYS A O 1 ATOM 2514 C CB . LYS A 1 322 ? 9.243 -17.438 8.912 1.00 9.30 ? 322 LYS A CB 1 ATOM 2515 C CG . LYS A 1 322 ? 8.455 -18.042 10.089 1.00 9.57 ? 322 LYS A CG 1 ATOM 2516 C CD . LYS A 1 322 ? 7.406 -19.061 9.720 1.00 10.55 ? 322 LYS A CD 1 ATOM 2517 C CE . LYS A 1 322 ? 6.313 -18.497 8.836 1.00 10.95 ? 322 LYS A CE 1 ATOM 2518 N NZ . LYS A 1 322 ? 5.260 -19.549 8.555 1.00 11.86 ? 322 LYS A NZ 1 ATOM 2519 N N . TYR A 1 323 ? 11.810 -17.524 6.846 1.00 8.88 ? 323 TYR A N 1 ATOM 2520 C CA . TYR A 1 323 ? 12.524 -17.013 5.680 1.00 9.10 ? 323 TYR A CA 1 ATOM 2521 C C . TYR A 1 323 ? 12.343 -17.941 4.494 1.00 8.92 ? 323 TYR A C 1 ATOM 2522 O O . TYR A 1 323 ? 12.030 -17.514 3.382 1.00 9.21 ? 323 TYR A O 1 ATOM 2523 C CB . TYR A 1 323 ? 14.001 -16.858 5.986 1.00 8.99 ? 323 TYR A CB 1 ATOM 2524 C CG . TYR A 1 323 ? 14.856 -16.484 4.796 1.00 8.73 ? 323 TYR A CG 1 ATOM 2525 C CD1 . TYR A 1 323 ? 14.892 -15.169 4.333 1.00 9.24 ? 323 TYR A CD1 1 ATOM 2526 C CD2 . TYR A 1 323 ? 15.634 -17.428 4.122 1.00 8.77 ? 323 TYR A CD2 1 ATOM 2527 C CE1 . TYR A 1 323 ? 15.642 -14.834 3.255 1.00 9.60 ? 323 TYR A CE1 1 ATOM 2528 C CE2 . TYR A 1 323 ? 16.414 -17.069 3.035 1.00 9.14 ? 323 TYR A CE2 1 ATOM 2529 C CZ . TYR A 1 323 ? 16.440 -15.765 2.633 1.00 9.06 ? 323 TYR A CZ 1 ATOM 2530 O OH . TYR A 1 323 ? 17.218 -15.323 1.595 1.00 9.99 ? 323 TYR A OH 1 ATOM 2531 N N . MET A 1 324 ? 12.544 -19.230 4.746 1.00 9.73 ? 324 MET A N 1 ATOM 2532 C CA . MET A 1 324 ? 12.438 -20.243 3.713 1.00 10.33 ? 324 MET A CA 1 ATOM 2533 C C . MET A 1 324 ? 10.977 -20.451 3.276 1.00 10.58 ? 324 MET A C 1 ATOM 2534 O O . MET A 1 324 ? 10.687 -20.529 2.072 1.00 11.99 ? 324 MET A O 1 ATOM 2535 C CB . MET A 1 324 ? 13.050 -21.561 4.218 1.00 10.03 ? 324 MET A CB 1 ATOM 2536 C CG . MET A 1 324 ? 14.572 -21.489 4.512 1.00 10.73 ? 324 MET A CG 1 ATOM 2537 S SD . MET A 1 324 ? 15.575 -20.976 3.078 1.00 12.19 ? 324 MET A SD 1 ATOM 2538 C CE . MET A 1 324 ? 15.386 -22.407 1.970 1.00 12.87 ? 324 MET A CE 1 ATOM 2539 N N . GLU A 1 325 ? 10.063 -20.517 4.233 1.00 10.50 ? 325 GLU A N 1 ATOM 2540 C CA . GLU A 1 325 ? 8.653 -20.729 3.926 1.00 10.93 ? 325 GLU A CA 1 ATOM 2541 C C . GLU A 1 325 ? 8.020 -19.604 3.142 1.00 10.77 ? 325 GLU A C 1 ATOM 2542 O O . GLU A 1 325 ? 7.124 -19.842 2.343 1.00 11.98 ? 325 GLU A O 1 ATOM 2543 C CB . GLU A 1 325 ? 7.843 -20.954 5.216 1.00 11.45 ? 325 GLU A CB 1 ATOM 2544 C CG . GLU A 1 325 ? 8.129 -22.277 5.912 1.00 11.94 ? 325 GLU A CG 1 ATOM 2545 C CD . GLU A 1 325 ? 7.223 -22.504 7.105 1.00 13.26 ? 325 GLU A CD 1 ATOM 2546 O OE1 . GLU A 1 325 ? 6.283 -21.720 7.296 1.00 16.61 ? 325 GLU A OE1 1 ATOM 2547 O OE2 . GLU A 1 325 ? 7.445 -23.499 7.822 1.00 16.79 ? 325 GLU A OE2 1 ATOM 2548 N N . LEU A 1 326 ? 8.512 -18.390 3.342 1.00 10.00 ? 326 LEU A N 1 ATOM 2549 C CA . LEU A 1 326 ? 7.859 -17.211 2.754 1.00 10.14 ? 326 LEU A CA 1 ATOM 2550 C C . LEU A 1 326 ? 8.564 -16.702 1.505 1.00 10.07 ? 326 LEU A C 1 ATOM 2551 O O . LEU A 1 326 ? 8.196 -15.630 1.005 1.00 11.28 ? 326 LEU A O 1 ATOM 2552 C CB . LEU A 1 326 ? 7.734 -16.095 3.787 1.00 9.42 ? 326 LEU A CB 1 ATOM 2553 C CG . LEU A 1 326 ? 6.826 -16.480 4.968 1.00 9.24 ? 326 LEU A CG 1 ATOM 2554 C CD1 . LEU A 1 326 ? 6.982 -15.476 6.046 1.00 10.27 ? 326 LEU A CD1 1 ATOM 2555 C CD2 . LEU A 1 326 ? 5.362 -16.651 4.520 1.00 10.82 ? 326 LEU A CD2 1 ATOM 2556 N N . GLY A 1 327 ? 9.519 -17.468 0.975 1.00 10.20 ? 327 GLY A N 1 ATOM 2557 C CA . GLY A 1 327 ? 10.062 -17.216 -0.366 1.00 10.25 ? 327 GLY A CA 1 ATOM 2558 C C . GLY A 1 327 ? 11.513 -17.590 -0.601 1.00 10.21 ? 327 GLY A C 1 ATOM 2559 O O . GLY A 1 327 ? 11.940 -17.683 -1.748 1.00 9.97 ? 327 GLY A O 1 ATOM 2560 N N . ALA A 1 328 ? 12.271 -17.746 0.482 1.00 8.84 ? 328 ALA A N 1 ATOM 2561 C CA . ALA A 1 328 ? 13.688 -18.107 0.391 1.00 9.21 ? 328 ALA A CA 1 ATOM 2562 C C . ALA A 1 328 ? 14.493 -17.022 -0.344 1.00 9.34 ? 328 ALA A C 1 ATOM 2563 O O . ALA A 1 328 ? 14.008 -15.916 -0.565 1.00 9.43 ? 328 ALA A O 1 ATOM 2564 C CB . ALA A 1 328 ? 13.876 -19.505 -0.245 1.00 9.14 ? 328 ALA A CB 1 ATOM 2565 N N . THR A 1 329 ? 15.725 -17.341 -0.735 1.00 8.67 ? 329 THR A N 1 ATOM 2566 C CA . THR A 1 329 ? 16.608 -16.347 -1.347 1.00 8.45 ? 329 THR A CA 1 ATOM 2567 C C . THR A 1 329 ? 16.057 -15.877 -2.690 1.00 8.81 ? 329 THR A C 1 ATOM 2568 O O . THR A 1 329 ? 16.104 -14.677 -2.998 1.00 8.76 ? 329 THR A O 1 ATOM 2569 C CB . THR A 1 329 ? 18.051 -16.873 -1.412 1.00 8.90 ? 329 THR A CB 1 ATOM 2570 O OG1 . THR A 1 329 ? 18.496 -17.193 -0.078 1.00 9.14 ? 329 THR A OG1 1 ATOM 2571 C CG2 . THR A 1 329 ? 19.000 -15.823 -1.932 1.00 9.38 ? 329 THR A CG2 1 ATOM 2572 N N . GLN A 1 330 ? 15.464 -16.793 -3.457 1.00 8.23 ? 330 GLN A N 1 ATOM 2573 C CA . GLN A 1 330 ? 14.832 -16.402 -4.720 1.00 8.75 ? 330 GLN A CA 1 ATOM 2574 C C . GLN A 1 330 ? 13.736 -15.359 -4.476 1.00 8.26 ? 330 GLN A C 1 ATOM 2575 O O . GLN A 1 330 ? 13.632 -14.376 -5.205 1.00 9.06 ? 330 GLN A O 1 ATOM 2576 C CB . GLN A 1 330 ? 14.262 -17.621 -5.461 1.00 9.29 ? 330 GLN A CB 1 ATOM 2577 C CG . GLN A 1 330 ? 13.509 -17.228 -6.727 1.00 8.86 ? 330 GLN A CG 1 ATOM 2578 C CD . GLN A 1 330 ? 13.132 -18.399 -7.602 1.00 9.36 ? 330 GLN A CD 1 ATOM 2579 O OE1 . GLN A 1 330 ? 13.775 -19.442 -7.549 1.00 12.15 ? 330 GLN A OE1 1 ATOM 2580 N NE2 . GLN A 1 330 ? 12.083 -18.236 -8.399 1.00 10.34 ? 330 GLN A NE2 1 ATOM 2581 N N . GLY A 1 331 ? 12.880 -15.582 -3.483 1.00 8.87 ? 331 GLY A N 1 ATOM 2582 C CA . GLY A 1 331 ? 11.809 -14.653 -3.171 1.00 8.20 ? 331 GLY A CA 1 ATOM 2583 C C . GLY A 1 331 ? 12.325 -13.305 -2.718 1.00 8.67 ? 331 GLY A C 1 ATOM 2584 O O . GLY A 1 331 ? 11.809 -12.262 -3.149 1.00 9.05 ? 331 GLY A O 1 ATOM 2585 N N . MET A 1 332 ? 13.363 -13.298 -1.886 1.00 8.51 ? 332 MET A N 1 ATOM 2586 C CA . MET A 1 332 ? 13.986 -12.018 -1.500 1.00 8.75 ? 332 MET A CA 1 ATOM 2587 C C . MET A 1 332 ? 14.467 -11.298 -2.754 1.00 8.25 ? 332 MET A C 1 ATOM 2588 O O . MET A 1 332 ? 14.205 -10.104 -2.928 1.00 9.01 ? 332 MET A O 1 ATOM 2589 C CB . MET A 1 332 ? 15.148 -12.237 -0.536 1.00 8.89 ? 332 MET A CB 1 ATOM 2590 C CG . MET A 1 332 ? 15.823 -10.949 -0.107 1.00 8.99 ? 332 MET A CG 1 ATOM 2591 S SD . MET A 1 332 ? 15.039 -10.052 1.244 1.00 10.70 ? 332 MET A SD 1 ATOM 2592 C CE . MET A 1 332 ? 13.732 -9.066 0.425 1.00 11.08 ? 332 MET A CE 1 ATOM 2593 N N . GLY A 1 333 ? 15.140 -12.035 -3.642 1.00 8.55 ? 333 GLY A N 1 ATOM 2594 C CA . GLY A 1 333 ? 15.648 -11.424 -4.872 1.00 8.37 ? 333 GLY A CA 1 ATOM 2595 C C . GLY A 1 333 ? 14.571 -10.921 -5.807 1.00 8.44 ? 333 GLY A C 1 ATOM 2596 O O . GLY A 1 333 ? 14.794 -9.956 -6.539 1.00 8.10 ? 333 GLY A O 1 ATOM 2597 N N . GLU A 1 334 ? 13.415 -11.570 -5.816 1.00 8.43 ? 334 GLU A N 1 ATOM 2598 C CA . GLU A 1 334 ? 12.323 -11.109 -6.656 1.00 8.54 ? 334 GLU A CA 1 ATOM 2599 C C . GLU A 1 334 ? 11.815 -9.761 -6.167 1.00 8.59 ? 334 GLU A C 1 ATOM 2600 O O . GLU A 1 334 ? 11.488 -8.892 -6.975 1.00 8.88 ? 334 GLU A O 1 ATOM 2601 C CB . GLU A 1 334 ? 11.210 -12.178 -6.739 1.00 8.52 ? 334 GLU A CB 1 ATOM 2602 C CG . GLU A 1 334 ? 11.654 -13.313 -7.679 1.00 8.90 ? 334 GLU A CG 1 ATOM 2603 C CD . GLU A 1 334 ? 10.814 -14.563 -7.663 1.00 11.04 ? 334 GLU A CD 1 ATOM 2604 O OE1 . GLU A 1 334 ? 9.950 -14.657 -6.785 1.00 16.25 ? 334 GLU A OE1 1 ATOM 2605 O OE2 . GLU A 1 334 ? 11.032 -15.446 -8.533 1.00 11.13 ? 334 GLU A OE2 1 ATOM 2606 N N . ALA A 1 335 ? 11.771 -9.568 -4.857 1.00 8.84 ? 335 ALA A N 1 ATOM 2607 C CA . ALA A 1 335 ? 11.443 -8.232 -4.311 1.00 8.46 ? 335 ALA A CA 1 ATOM 2608 C C . ALA A 1 335 ? 12.504 -7.206 -4.693 1.00 8.13 ? 335 ALA A C 1 ATOM 2609 O O . ALA A 1 335 ? 12.177 -6.092 -5.146 1.00 8.62 ? 335 ALA A O 1 ATOM 2610 C CB . ALA A 1 335 ? 11.310 -8.307 -2.794 1.00 9.22 ? 335 ALA A CB 1 ATOM 2611 N N . LEU A 1 336 ? 13.773 -7.575 -4.552 1.00 8.95 ? 336 LEU A N 1 ATOM 2612 C CA . LEU A 1 336 ? 14.858 -6.676 -4.929 1.00 9.01 ? 336 LEU A CA 1 ATOM 2613 C C . LEU A 1 336 ? 14.760 -6.271 -6.401 1.00 9.29 ? 336 LEU A C 1 ATOM 2614 O O . LEU A 1 336 ? 14.999 -5.133 -6.736 1.00 9.99 ? 336 LEU A O 1 ATOM 2615 C CB . LEU A 1 336 ? 16.249 -7.295 -4.637 1.00 9.38 ? 336 LEU A CB 1 ATOM 2616 C CG . LEU A 1 336 ? 16.588 -7.656 -3.196 1.00 12.02 ? 336 LEU A CG 1 ATOM 2617 C CD1 . LEU A 1 336 ? 17.973 -8.204 -3.102 1.00 14.25 ? 336 LEU A CD1 1 ATOM 2618 C CD2 . LEU A 1 336 ? 16.472 -6.499 -2.304 1.00 14.43 ? 336 LEU A CD2 1 ATOM 2619 N N . THR A 1 337 ? 14.443 -7.229 -7.268 1.00 8.77 ? 337 THR A N 1 ATOM 2620 C CA . THR A 1 337 ? 14.314 -6.971 -8.711 1.00 9.36 ? 337 THR A CA 1 ATOM 2621 C C . THR A 1 337 ? 13.129 -6.067 -9.021 1.00 9.86 ? 337 THR A C 1 ATOM 2622 O O . THR A 1 337 ? 13.223 -5.195 -9.899 1.00 11.44 ? 337 THR A O 1 ATOM 2623 C CB . THR A 1 337 ? 14.215 -8.307 -9.455 1.00 10.00 ? 337 THR A CB 1 ATOM 2624 O OG1 . THR A 1 337 ? 15.475 -8.971 -9.345 1.00 10.39 ? 337 THR A OG1 1 ATOM 2625 C CG2 . THR A 1 337 ? 13.919 -8.127 -10.956 1.00 10.62 ? 337 THR A CG2 1 ATOM 2626 N N . ARG A 1 338 ? 12.008 -6.226 -8.302 1.00 9.10 ? 338 ARG A N 1 ATOM 2627 C CA . ARG A 1 338 ? 10.848 -5.343 -8.513 1.00 9.19 ? 338 ARG A CA 1 ATOM 2628 C C . ARG A 1 338 ? 11.168 -3.896 -8.155 1.00 10.10 ? 338 ARG A C 1 ATOM 2629 O O . ARG A 1 338 ? 10.634 -2.981 -8.755 1.00 11.73 ? 338 ARG A O 1 ATOM 2630 C CB . ARG A 1 338 ? 9.626 -5.802 -7.702 1.00 8.88 ? 338 ARG A CB 1 ATOM 2631 C CG . ARG A 1 338 ? 8.954 -7.056 -8.245 1.00 9.48 ? 338 ARG A CG 1 ATOM 2632 C CD . ARG A 1 338 ? 7.678 -7.406 -7.544 1.00 9.82 ? 338 ARG A CD 1 ATOM 2633 N NE . ARG A 1 338 ? 7.832 -7.653 -6.122 1.00 10.30 ? 338 ARG A NE 1 ATOM 2634 C CZ . ARG A 1 338 ? 7.989 -8.838 -5.556 1.00 9.32 ? 338 ARG A CZ 1 ATOM 2635 N NH1 . ARG A 1 338 ? 8.079 -9.935 -6.294 1.00 10.02 ? 338 ARG A NH1 1 ATOM 2636 N NH2 . ARG A 1 338 ? 8.050 -8.959 -4.249 1.00 9.14 ? 338 ARG A NH2 1 ATOM 2637 N N . GLY A 1 339 ? 12.076 -3.705 -7.202 1.00 9.92 ? 339 GLY A N 1 ATOM 2638 C CA . GLY A 1 339 ? 12.497 -2.371 -6.766 1.00 9.60 ? 339 GLY A CA 1 ATOM 2639 C C . GLY A 1 339 ? 12.182 -2.139 -5.310 1.00 9.32 ? 339 GLY A C 1 ATOM 2640 O O . GLY A 1 339 ? 11.096 -2.474 -4.827 1.00 9.67 ? 339 GLY A O 1 ATOM 2641 N N . MET A 1 340 ? 13.128 -1.529 -4.598 1.00 8.85 ? 340 MET A N 1 ATOM 2642 C CA . MET A 1 340 ? 13.007 -1.284 -3.162 1.00 9.14 ? 340 MET A CA 1 ATOM 2643 C C . MET A 1 340 ? 13.448 0.132 -2.825 1.00 8.39 ? 340 MET A C 1 ATOM 2644 O O . MET A 1 340 ? 14.214 0.750 -3.560 1.00 9.51 ? 340 MET A O 1 ATOM 2645 C CB A MET A 1 340 ? 13.967 -2.204 -2.388 0.50 8.94 ? 340 MET A CB 1 ATOM 2646 C CB B MET A 1 340 ? 13.745 -2.380 -2.391 0.50 9.97 ? 340 MET A CB 1 ATOM 2647 C CG A MET A 1 340 ? 13.858 -3.688 -2.664 0.50 7.92 ? 340 MET A CG 1 ATOM 2648 C CG B MET A 1 340 ? 13.076 -3.726 -2.680 0.50 12.07 ? 340 MET A CG 1 ATOM 2649 S SD A MET A 1 340 ? 12.352 -4.450 -1.956 0.50 5.17 ? 340 MET A SD 1 ATOM 2650 S SD B MET A 1 340 ? 13.448 -5.173 -1.698 0.50 14.35 ? 340 MET A SD 1 ATOM 2651 C CE A MET A 1 340 ? 13.010 -4.890 -0.271 0.50 5.38 ? 340 MET A CE 1 ATOM 2652 C CE B MET A 1 340 ? 12.899 -4.687 -0.072 0.50 13.05 ? 340 MET A CE 1 ATOM 2653 N N . VAL A 1 341 ? 12.911 0.642 -1.727 1.00 8.31 ? 341 VAL A N 1 ATOM 2654 C CA . VAL A 1 341 ? 13.256 1.939 -1.170 1.00 7.72 ? 341 VAL A CA 1 ATOM 2655 C C . VAL A 1 341 ? 14.322 1.777 -0.086 1.00 7.83 ? 341 VAL A C 1 ATOM 2656 O O . VAL A 1 341 ? 14.270 0.863 0.743 1.00 7.98 ? 341 VAL A O 1 ATOM 2657 C CB . VAL A 1 341 ? 11.988 2.602 -0.600 1.00 7.57 ? 341 VAL A CB 1 ATOM 2658 C CG1 . VAL A 1 341 ? 12.303 3.898 0.117 1.00 8.07 ? 341 VAL A CG1 1 ATOM 2659 C CG2 . VAL A 1 341 ? 10.978 2.835 -1.731 1.00 8.93 ? 341 VAL A CG2 1 ATOM 2660 N N . LEU A 1 342 ? 15.286 2.687 -0.098 1.00 7.67 ? 342 LEU A N 1 ATOM 2661 C CA . LEU A 1 342 ? 16.351 2.719 0.904 1.00 7.74 ? 342 LEU A CA 1 ATOM 2662 C C . LEU A 1 342 ? 15.937 3.512 2.135 1.00 7.35 ? 342 LEU A C 1 ATOM 2663 O O . LEU A 1 342 ? 15.578 4.693 2.021 1.00 8.35 ? 342 LEU A O 1 ATOM 2664 C CB . LEU A 1 342 ? 17.622 3.323 0.285 1.00 7.99 ? 342 LEU A CB 1 ATOM 2665 C CG . LEU A 1 342 ? 18.848 3.403 1.202 1.00 9.48 ? 342 LEU A CG 1 ATOM 2666 C CD1 . LEU A 1 342 ? 19.385 2.010 1.538 1.00 10.39 ? 342 LEU A CD1 1 ATOM 2667 C CD2 . LEU A 1 342 ? 19.963 4.265 0.601 1.00 10.10 ? 342 LEU A CD2 1 ATOM 2668 N N . ALA A 1 343 ? 16.031 2.856 3.289 1.00 8.13 ? 343 ALA A N 1 ATOM 2669 C CA . ALA A 1 343 ? 15.748 3.445 4.578 1.00 7.74 ? 343 ALA A CA 1 ATOM 2670 C C . ALA A 1 343 ? 17.006 3.419 5.435 1.00 8.00 ? 343 ALA A C 1 ATOM 2671 O O . ALA A 1 343 ? 17.748 2.455 5.416 1.00 8.33 ? 343 ALA A O 1 ATOM 2672 C CB . ALA A 1 343 ? 14.660 2.673 5.285 1.00 9.06 ? 343 ALA A CB 1 ATOM 2673 N N . MET A 1 344 ? 17.219 4.480 6.198 1.00 8.02 ? 344 MET A N 1 ATOM 2674 C CA . MET A 1 344 ? 18.347 4.598 7.127 1.00 8.04 ? 344 MET A CA 1 ATOM 2675 C C . MET A 1 344 ? 17.831 5.128 8.451 1.00 7.65 ? 344 MET A C 1 ATOM 2676 O O . MET A 1 344 ? 17.009 6.060 8.463 1.00 8.70 ? 344 MET A O 1 ATOM 2677 C CB . MET A 1 344 ? 19.399 5.503 6.515 1.00 8.77 ? 344 MET A CB 1 ATOM 2678 C CG . MET A 1 344 ? 20.150 4.835 5.361 1.00 8.24 ? 344 MET A CG 1 ATOM 2679 S SD . MET A 1 344 ? 21.140 5.942 4.348 1.00 10.70 ? 344 MET A SD 1 ATOM 2680 C CE . MET A 1 344 ? 19.858 6.817 3.465 1.00 10.69 ? 344 MET A CE 1 ATOM 2681 N N . SER A 1 345 ? 18.269 4.517 9.557 1.00 7.82 ? 345 SER A N 1 ATOM 2682 C CA . SER A 1 345 ? 17.764 4.916 10.872 1.00 7.87 ? 345 SER A CA 1 ATOM 2683 C C . SER A 1 345 ? 18.762 4.674 11.962 1.00 7.91 ? 345 SER A C 1 ATOM 2684 O O . SER A 1 345 ? 19.764 4.007 11.759 1.00 8.37 ? 345 SER A O 1 ATOM 2685 C CB . SER A 1 345 ? 16.460 4.185 11.197 1.00 8.00 ? 345 SER A CB 1 ATOM 2686 O OG . SER A 1 345 ? 16.698 2.809 11.438 1.00 9.21 ? 345 SER A OG 1 ATOM 2687 N N . ILE A 1 346 ? 18.475 5.233 13.126 1.00 8.33 ? 346 ILE A N 1 ATOM 2688 C CA . ILE A 1 346 ? 19.232 4.962 14.326 1.00 8.54 ? 346 ILE A CA 1 ATOM 2689 C C . ILE A 1 346 ? 18.227 4.810 15.442 1.00 8.68 ? 346 ILE A C 1 ATOM 2690 O O . ILE A 1 346 ? 17.339 5.640 15.564 1.00 8.64 ? 346 ILE A O 1 ATOM 2691 C CB . ILE A 1 346 ? 20.283 6.081 14.566 1.00 8.92 ? 346 ILE A CB 1 ATOM 2692 C CG1 . ILE A 1 346 ? 21.191 5.708 15.754 1.00 9.93 ? 346 ILE A CG1 1 ATOM 2693 C CG2 . ILE A 1 346 ? 19.642 7.452 14.741 1.00 9.33 ? 346 ILE A CG2 1 ATOM 2694 C CD1 . ILE A 1 346 ? 22.387 6.602 15.901 1.00 9.95 ? 346 ILE A CD1 1 ATOM 2695 N N . TRP A 1 347 ? 18.364 3.752 16.229 1.00 8.74 ? 347 TRP A N 1 ATOM 2696 C CA . TRP A 1 347 ? 17.330 3.432 17.224 1.00 8.95 ? 347 TRP A CA 1 ATOM 2697 C C . TRP A 1 347 ? 17.859 2.549 18.356 1.00 9.61 ? 347 TRP A C 1 ATOM 2698 O O . TRP A 1 347 ? 18.935 1.962 18.239 1.00 9.65 ? 347 TRP A O 1 ATOM 2699 C CB . TRP A 1 347 ? 16.096 2.819 16.527 1.00 9.53 ? 347 TRP A CB 1 ATOM 2700 C CG . TRP A 1 347 ? 16.249 1.493 15.881 1.00 9.24 ? 347 TRP A CG 1 ATOM 2701 C CD1 . TRP A 1 347 ? 16.826 1.224 14.652 1.00 9.01 ? 347 TRP A CD1 1 ATOM 2702 C CD2 . TRP A 1 347 ? 15.764 0.235 16.368 1.00 9.19 ? 347 TRP A CD2 1 ATOM 2703 N NE1 . TRP A 1 347 ? 16.707 -0.116 14.358 1.00 10.31 ? 347 TRP A NE1 1 ATOM 2704 C CE2 . TRP A 1 347 ? 16.061 -0.743 15.394 1.00 9.54 ? 347 TRP A CE2 1 ATOM 2705 C CE3 . TRP A 1 347 ? 15.057 -0.165 17.507 1.00 10.03 ? 347 TRP A CE3 1 ATOM 2706 C CZ2 . TRP A 1 347 ? 15.677 -2.076 15.540 1.00 9.48 ? 347 TRP A CZ2 1 ATOM 2707 C CZ3 . TRP A 1 347 ? 14.688 -1.494 17.648 1.00 10.02 ? 347 TRP A CZ3 1 ATOM 2708 C CH2 . TRP A 1 347 ? 15.023 -2.431 16.692 1.00 9.53 ? 347 TRP A CH2 1 ATOM 2709 N N . TRP A 1 348 ? 17.106 2.500 19.456 1.00 9.75 ? 348 TRP A N 1 ATOM 2710 C CA . TRP A 1 348 ? 17.413 1.647 20.602 1.00 9.89 ? 348 TRP A CA 1 ATOM 2711 C C . TRP A 1 348 ? 16.141 0.927 21.031 1.00 10.52 ? 348 TRP A C 1 ATOM 2712 O O . TRP A 1 348 ? 15.045 1.192 20.513 1.00 11.30 ? 348 TRP A O 1 ATOM 2713 C CB . TRP A 1 348 ? 18.078 2.412 21.746 1.00 10.86 ? 348 TRP A CB 1 ATOM 2714 C CG . TRP A 1 348 ? 17.301 3.495 22.401 1.00 10.86 ? 348 TRP A CG 1 ATOM 2715 C CD1 . TRP A 1 348 ? 15.940 3.726 22.374 1.00 12.12 ? 348 TRP A CD1 1 ATOM 2716 C CD2 . TRP A 1 348 ? 17.853 4.468 23.272 1.00 11.77 ? 348 TRP A CD2 1 ATOM 2717 N NE1 . TRP A 1 348 ? 15.645 4.824 23.148 1.00 12.94 ? 348 TRP A NE1 1 ATOM 2718 C CE2 . TRP A 1 348 ? 16.809 5.313 23.690 1.00 11.61 ? 348 TRP A CE2 1 ATOM 2719 C CE3 . TRP A 1 348 ? 19.154 4.761 23.692 1.00 11.65 ? 348 TRP A CE3 1 ATOM 2720 C CZ2 . TRP A 1 348 ? 17.035 6.401 24.545 1.00 12.91 ? 348 TRP A CZ2 1 ATOM 2721 C CZ3 . TRP A 1 348 ? 19.371 5.832 24.522 1.00 12.45 ? 348 TRP A CZ3 1 ATOM 2722 C CH2 . TRP A 1 348 ? 18.331 6.643 24.933 1.00 12.20 ? 348 TRP A CH2 1 ATOM 2723 N N . ASP A 1 349 ? 16.287 0.007 21.978 1.00 11.63 ? 349 ASP A N 1 ATOM 2724 C CA . ASP A 1 349 ? 15.274 -1.006 22.276 1.00 12.21 ? 349 ASP A CA 1 ATOM 2725 C C . ASP A 1 349 ? 15.044 -1.096 23.790 1.00 13.20 ? 349 ASP A C 1 ATOM 2726 O O . ASP A 1 349 ? 15.741 -1.837 24.488 1.00 13.65 ? 349 ASP A O 1 ATOM 2727 C CB . ASP A 1 349 ? 15.769 -2.334 21.697 1.00 12.26 ? 349 ASP A CB 1 ATOM 2728 C CG . ASP A 1 349 ? 14.902 -3.518 22.044 1.00 13.03 ? 349 ASP A CG 1 ATOM 2729 O OD1 . ASP A 1 349 ? 13.707 -3.331 22.419 1.00 16.55 ? 349 ASP A OD1 1 ATOM 2730 O OD2 . ASP A 1 349 ? 15.373 -4.681 21.913 1.00 13.72 ? 349 ASP A OD2 1 ATOM 2731 N N . GLN A 1 350 ? 14.060 -0.341 24.285 1.00 14.74 ? 350 GLN A N 1 ATOM 2732 C CA . GLN A 1 350 ? 13.716 -0.360 25.708 1.00 15.61 ? 350 GLN A CA 1 ATOM 2733 C C . GLN A 1 350 ? 13.266 -1.737 26.189 1.00 16.52 ? 350 GLN A C 1 ATOM 2734 O O . GLN A 1 350 ? 13.614 -2.129 27.307 1.00 18.10 ? 350 GLN A O 1 ATOM 2735 C CB A GLN A 1 350 ? 12.645 0.699 25.992 0.50 15.76 ? 350 GLN A CB 1 ATOM 2736 C CB B GLN A 1 350 ? 12.616 0.665 26.001 0.50 16.05 ? 350 GLN A CB 1 ATOM 2737 C CG A GLN A 1 350 ? 12.174 0.805 27.455 0.50 16.38 ? 350 GLN A CG 1 ATOM 2738 C CG B GLN A 1 350 ? 13.036 2.132 25.835 0.50 17.85 ? 350 GLN A CG 1 ATOM 2739 C CD A GLN A 1 350 ? 13.278 0.963 28.459 0.50 18.95 ? 350 GLN A CD 1 ATOM 2740 C CD B GLN A 1 350 ? 13.761 2.731 27.033 0.50 20.04 ? 350 GLN A CD 1 ATOM 2741 O OE1 A GLN A 1 350 ? 14.281 1.629 28.191 0.50 19.61 ? 350 GLN A OE1 1 ATOM 2742 O OE1 B GLN A 1 350 ? 14.025 3.947 27.058 0.50 22.95 ? 350 GLN A OE1 1 ATOM 2743 N NE2 A GLN A 1 350 ? 13.088 0.376 29.648 0.50 19.34 ? 350 GLN A NE2 1 ATOM 2744 N NE2 B GLN A 1 350 ? 14.109 1.901 28.004 0.50 19.76 ? 350 GLN A NE2 1 ATOM 2745 N N . GLY A 1 351 ? 12.524 -2.465 25.375 1.00 16.82 ? 351 GLY A N 1 ATOM 2746 C CA . GLY A 1 351 ? 12.058 -3.778 25.798 1.00 18.42 ? 351 GLY A CA 1 ATOM 2747 C C . GLY A 1 351 ? 13.223 -4.703 26.036 1.00 19.52 ? 351 GLY A C 1 ATOM 2748 O O . GLY A 1 351 ? 13.475 -5.142 27.173 1.00 25.04 ? 351 GLY A O 1 ATOM 2749 N N . GLY A 1 352 ? 13.980 -4.928 24.985 1.00 18.37 ? 352 GLY A N 1 ATOM 2750 C CA . GLY A 1 352 ? 14.867 -6.062 24.896 1.00 15.66 ? 352 GLY A CA 1 ATOM 2751 C C . GLY A 1 352 ? 16.328 -5.754 24.713 1.00 14.41 ? 352 GLY A C 1 ATOM 2752 O O . GLY A 1 352 ? 17.095 -6.676 24.487 1.00 13.15 ? 352 GLY A O 1 ATOM 2753 N N . ASN A 1 353 ? 16.723 -4.485 24.826 1.00 12.57 ? 353 ASN A N 1 ATOM 2754 C CA . ASN A 1 353 ? 18.138 -4.075 24.844 1.00 12.65 ? 353 ASN A CA 1 ATOM 2755 C C . ASN A 1 353 ? 18.933 -4.439 23.569 1.00 12.00 ? 353 ASN A C 1 ATOM 2756 O O . ASN A 1 353 ? 20.152 -4.429 23.573 1.00 12.07 ? 353 ASN A O 1 ATOM 2757 C CB . ASN A 1 353 ? 18.889 -4.640 26.071 1.00 12.61 ? 353 ASN A CB 1 ATOM 2758 C CG . ASN A 1 353 ? 18.345 -4.176 27.409 1.00 13.39 ? 353 ASN A CG 1 ATOM 2759 O OD1 . ASN A 1 353 ? 18.703 -4.759 28.478 1.00 16.00 ? 353 ASN A OD1 1 ATOM 2760 N ND2 . ASN A 1 353 ? 17.484 -3.206 27.392 1.00 13.02 ? 353 ASN A ND2 1 ATOM 2761 N N . MET A 1 354 ? 18.241 -4.737 22.476 1.00 11.84 ? 354 MET A N 1 ATOM 2762 C CA . MET A 1 354 ? 18.897 -5.120 21.206 1.00 11.41 ? 354 MET A CA 1 ATOM 2763 C C . MET A 1 354 ? 19.804 -6.351 21.403 1.00 10.83 ? 354 MET A C 1 ATOM 2764 O O . MET A 1 354 ? 20.782 -6.541 20.691 1.00 10.29 ? 354 MET A O 1 ATOM 2765 C CB . MET A 1 354 ? 19.690 -3.946 20.622 1.00 11.67 ? 354 MET A CB 1 ATOM 2766 C CG . MET A 1 354 ? 19.697 -3.841 19.110 1.00 11.56 ? 354 MET A CG 1 ATOM 2767 S SD . MET A 1 354 ? 18.104 -3.266 18.421 1.00 10.53 ? 354 MET A SD 1 ATOM 2768 C CE . MET A 1 354 ? 18.089 -1.593 19.028 1.00 10.89 ? 354 MET A CE 1 ATOM 2769 N N . GLU A 1 355 ? 19.431 -7.246 22.306 1.00 11.47 ? 355 GLU A N 1 ATOM 2770 C CA . GLU A 1 355 ? 20.298 -8.395 22.619 1.00 11.60 ? 355 GLU A CA 1 ATOM 2771 C C . GLU A 1 355 ? 20.576 -9.263 21.413 1.00 10.78 ? 355 GLU A C 1 ATOM 2772 O O . GLU A 1 355 ? 21.674 -9.824 21.306 1.00 11.06 ? 355 GLU A O 1 ATOM 2773 C CB . GLU A 1 355 ? 19.714 -9.297 23.727 1.00 11.86 ? 355 GLU A CB 1 ATOM 2774 C CG . GLU A 1 355 ? 19.766 -8.694 25.113 1.00 12.42 ? 355 GLU A CG 1 ATOM 2775 C CD . GLU A 1 355 ? 19.186 -9.572 26.194 1.00 14.25 ? 355 GLU A CD 1 ATOM 2776 O OE1 . GLU A 1 355 ? 18.749 -10.727 25.916 1.00 17.93 ? 355 GLU A OE1 1 ATOM 2777 O OE2 . GLU A 1 355 ? 19.172 -9.072 27.336 1.00 16.70 ? 355 GLU A OE2 1 ATOM 2778 N N . TRP A 1 356 ? 19.620 -9.352 20.486 1.00 10.65 ? 356 TRP A N 1 ATOM 2779 C CA . TRP A 1 356 ? 19.797 -10.162 19.299 1.00 10.70 ? 356 TRP A CA 1 ATOM 2780 C C . TRP A 1 356 ? 20.909 -9.661 18.382 1.00 10.86 ? 356 TRP A C 1 ATOM 2781 O O . TRP A 1 356 ? 21.399 -10.399 17.523 1.00 10.66 ? 356 TRP A O 1 ATOM 2782 C CB . TRP A 1 356 ? 18.479 -10.259 18.502 1.00 10.93 ? 356 TRP A CB 1 ATOM 2783 C CG . TRP A 1 356 ? 17.983 -8.909 18.045 1.00 11.02 ? 356 TRP A CG 1 ATOM 2784 C CD1 . TRP A 1 356 ? 17.133 -8.085 18.698 1.00 12.57 ? 356 TRP A CD1 1 ATOM 2785 C CD2 . TRP A 1 356 ? 18.398 -8.196 16.865 1.00 11.58 ? 356 TRP A CD2 1 ATOM 2786 N NE1 . TRP A 1 356 ? 16.971 -6.911 17.999 1.00 12.06 ? 356 TRP A NE1 1 ATOM 2787 C CE2 . TRP A 1 356 ? 17.735 -6.961 16.865 1.00 12.53 ? 356 TRP A CE2 1 ATOM 2788 C CE3 . TRP A 1 356 ? 19.250 -8.500 15.792 1.00 12.22 ? 356 TRP A CE3 1 ATOM 2789 C CZ2 . TRP A 1 356 ? 17.889 -6.028 15.843 1.00 13.57 ? 356 TRP A CZ2 1 ATOM 2790 C CZ3 . TRP A 1 356 ? 19.421 -7.570 14.792 1.00 12.62 ? 356 TRP A CZ3 1 ATOM 2791 C CH2 . TRP A 1 356 ? 18.732 -6.355 14.819 1.00 13.16 ? 356 TRP A CH2 1 ATOM 2792 N N . LEU A 1 357 ? 21.275 -8.391 18.524 1.00 10.42 ? 357 LEU A N 1 ATOM 2793 C CA . LEU A 1 357 ? 22.309 -7.780 17.707 1.00 10.48 ? 357 LEU A CA 1 ATOM 2794 C C . LEU A 1 357 ? 23.713 -8.052 18.253 1.00 11.05 ? 357 LEU A C 1 ATOM 2795 O O . LEU A 1 357 ? 24.621 -8.361 17.471 1.00 11.56 ? 357 LEU A O 1 ATOM 2796 C CB . LEU A 1 357 ? 22.079 -6.272 17.545 1.00 10.43 ? 357 LEU A CB 1 ATOM 2797 C CG . LEU A 1 357 ? 23.098 -5.477 16.726 1.00 10.56 ? 357 LEU A CG 1 ATOM 2798 C CD1 . LEU A 1 357 ? 23.291 -6.041 15.330 1.00 12.11 ? 357 LEU A CD1 1 ATOM 2799 C CD2 . LEU A 1 357 ? 22.694 -4.013 16.646 1.00 11.64 ? 357 LEU A CD2 1 ATOM 2800 N N . ASP A 1 358 ? 23.902 -7.951 19.576 1.00 10.58 ? 358 ASP A N 1 ATOM 2801 C CA . ASP A 1 358 ? 25.261 -7.861 20.091 1.00 11.28 ? 358 ASP A CA 1 ATOM 2802 C C . ASP A 1 358 ? 25.529 -8.567 21.419 1.00 11.38 ? 358 ASP A C 1 ATOM 2803 O O . ASP A 1 358 ? 26.605 -8.351 22.006 1.00 11.90 ? 358 ASP A O 1 ATOM 2804 C CB . ASP A 1 358 ? 25.668 -6.384 20.173 1.00 11.00 ? 358 ASP A CB 1 ATOM 2805 C CG . ASP A 1 358 ? 24.773 -5.571 21.081 1.00 10.95 ? 358 ASP A CG 1 ATOM 2806 O OD1 . ASP A 1 358 ? 24.188 -6.178 22.015 1.00 10.93 ? 358 ASP A OD1 1 ATOM 2807 O OD2 . ASP A 1 358 ? 24.624 -4.331 20.917 1.00 10.35 ? 358 ASP A OD2 1 ATOM 2808 N N . HIS A 1 359 ? 24.612 -9.417 21.871 1.00 11.85 ? 359 HIS A N 1 ATOM 2809 C CA . HIS A 1 359 ? 24.748 -10.080 23.172 1.00 12.85 ? 359 HIS A CA 1 ATOM 2810 C C . HIS A 1 359 ? 24.672 -11.572 22.970 1.00 13.07 ? 359 HIS A C 1 ATOM 2811 O O . HIS A 1 359 ? 23.939 -12.054 22.103 1.00 12.73 ? 359 HIS A O 1 ATOM 2812 C CB . HIS A 1 359 ? 23.640 -9.604 24.119 1.00 12.97 ? 359 HIS A CB 1 ATOM 2813 C CG . HIS A 1 359 ? 23.481 -10.457 25.335 1.00 13.54 ? 359 HIS A CG 1 ATOM 2814 N ND1 . HIS A 1 359 ? 24.353 -10.431 26.403 1.00 15.74 ? 359 HIS A ND1 1 ATOM 2815 C CD2 . HIS A 1 359 ? 22.521 -11.350 25.651 1.00 16.08 ? 359 HIS A CD2 1 ATOM 2816 C CE1 . HIS A 1 359 ? 23.931 -11.285 27.322 1.00 18.13 ? 359 HIS A CE1 1 ATOM 2817 N NE2 . HIS A 1 359 ? 22.825 -11.867 26.886 1.00 18.14 ? 359 HIS A NE2 1 ATOM 2818 N N . GLY A 1 360 ? 25.418 -12.327 23.776 1.00 13.98 ? 360 GLY A N 1 ATOM 2819 C CA . GLY A 1 360 ? 25.257 -13.781 23.801 1.00 13.94 ? 360 GLY A CA 1 ATOM 2820 C C . GLY A 1 360 ? 25.888 -14.413 22.612 1.00 14.56 ? 360 GLY A C 1 ATOM 2821 O O . GLY A 1 360 ? 27.100 -14.272 22.372 1.00 16.55 ? 360 GLY A O 1 ATOM 2822 N N . GLU A 1 361 ? 25.057 -15.078 21.809 1.00 13.95 ? 361 GLU A N 1 ATOM 2823 C CA . GLU A 1 361 ? 25.517 -15.593 20.523 1.00 14.29 ? 361 GLU A CA 1 ATOM 2824 C C . GLU A 1 361 ? 25.945 -14.535 19.506 1.00 13.25 ? 361 GLU A C 1 ATOM 2825 O O . GLU A 1 361 ? 26.658 -14.822 18.559 1.00 13.33 ? 361 GLU A O 1 ATOM 2826 C CB . GLU A 1 361 ? 24.425 -16.471 19.911 1.00 15.07 ? 361 GLU A CB 1 ATOM 2827 C CG . GLU A 1 361 ? 24.316 -17.810 20.612 1.00 18.31 ? 361 GLU A CG 1 ATOM 2828 C CD . GLU A 1 361 ? 25.662 -18.502 20.698 1.00 20.17 ? 361 GLU A CD 1 ATOM 2829 O OE1 . GLU A 1 361 ? 26.111 -19.056 19.677 1.00 20.08 ? 361 GLU A OE1 1 ATOM 2830 O OE2 . GLU A 1 361 ? 26.283 -18.486 21.770 1.00 20.63 ? 361 GLU A OE2 1 ATOM 2831 N N . ALA A 1 362 ? 25.482 -13.297 19.708 1.00 12.49 ? 362 ALA A N 1 ATOM 2832 C CA . ALA A 1 362 ? 25.584 -12.245 18.718 1.00 12.60 ? 362 ALA A CA 1 ATOM 2833 C C . ALA A 1 362 ? 26.696 -11.224 18.964 1.00 12.11 ? 362 ALA A C 1 ATOM 2834 O O . ALA A 1 362 ? 27.004 -10.404 18.098 1.00 12.05 ? 362 ALA A O 1 ATOM 2835 C CB . ALA A 1 362 ? 24.248 -11.546 18.608 1.00 11.95 ? 362 ALA A CB 1 ATOM 2836 N N . GLY A 1 363 ? 27.345 -11.272 20.135 1.00 12.24 ? 363 GLY A N 1 ATOM 2837 C CA . GLY A 1 363 ? 28.407 -10.308 20.393 1.00 12.86 ? 363 GLY A CA 1 ATOM 2838 C C . GLY A 1 363 ? 28.903 -10.277 21.812 1.00 13.02 ? 363 GLY A C 1 ATOM 2839 O O . GLY A 1 363 ? 28.575 -11.127 22.618 1.00 14.29 ? 363 GLY A O 1 ATOM 2840 N N . PRO A 1 364 ? 29.723 -9.286 22.097 1.00 12.73 ? 364 PRO A N 1 ATOM 2841 C CA . PRO A 1 364 ? 30.421 -9.224 23.389 1.00 13.35 ? 364 PRO A CA 1 ATOM 2842 C C . PRO A 1 364 ? 29.686 -8.464 24.488 1.00 13.65 ? 364 PRO A C 1 ATOM 2843 O O . PRO A 1 364 ? 30.226 -8.316 25.580 1.00 15.06 ? 364 PRO A O 1 ATOM 2844 C CB . PRO A 1 364 ? 31.700 -8.490 23.011 1.00 13.42 ? 364 PRO A CB 1 ATOM 2845 C CG . PRO A 1 364 ? 31.235 -7.499 21.976 1.00 13.70 ? 364 PRO A CG 1 ATOM 2846 C CD . PRO A 1 364 ? 30.161 -8.215 21.184 1.00 12.65 ? 364 PRO A CD 1 ATOM 2847 N N . CYS A 1 365 ? 28.492 -7.940 24.220 1.00 13.68 ? 365 CYS A N 1 ATOM 2848 C CA . CYS A 1 365 ? 27.806 -7.063 25.159 1.00 13.22 ? 365 CYS A CA 1 ATOM 2849 C C . CYS A 1 365 ? 27.225 -7.855 26.305 1.00 13.44 ? 365 CYS A C 1 ATOM 2850 O O . CYS A 1 365 ? 26.657 -8.928 26.086 1.00 13.77 ? 365 CYS A O 1 ATOM 2851 C CB . CYS A 1 365 ? 26.713 -6.267 24.407 1.00 12.72 ? 365 CYS A CB 1 ATOM 2852 S SG . CYS A 1 365 ? 27.445 -5.169 23.160 1.00 12.81 ? 365 CYS A SG 1 ATOM 2853 N N . ALA A 1 366 ? 27.325 -7.315 27.529 1.00 14.06 ? 366 ALA A N 1 ATOM 2854 C CA . ALA A 1 366 ? 26.824 -8.001 28.716 1.00 14.65 ? 366 ALA A CA 1 ATOM 2855 C C . ALA A 1 366 ? 25.323 -7.823 28.886 1.00 15.01 ? 366 ALA A C 1 ATOM 2856 O O . ALA A 1 366 ? 24.738 -6.899 28.333 1.00 15.03 ? 366 ALA A O 1 ATOM 2857 C CB . ALA A 1 366 ? 27.534 -7.476 29.951 1.00 14.62 ? 366 ALA A CB 1 ATOM 2858 N N . LYS A 1 367 ? 24.706 -8.698 29.674 1.00 16.44 ? 367 LYS A N 1 ATOM 2859 C CA . LYS A 1 367 ? 23.330 -8.524 30.113 1.00 16.02 ? 367 LYS A CA 1 ATOM 2860 C C . LYS A 1 367 ? 23.180 -7.127 30.711 1.00 15.87 ? 367 LYS A C 1 ATOM 2861 O O . LYS A 1 367 ? 24.015 -6.675 31.502 1.00 16.37 ? 367 LYS A O 1 ATOM 2862 C CB . LYS A 1 367 ? 22.948 -9.601 31.139 1.00 18.02 ? 367 LYS A CB 1 ATOM 2863 C CG . LYS A 1 367 ? 21.480 -9.689 31.404 1.00 19.57 ? 367 LYS A CG 1 ATOM 2864 C CD . LYS A 1 367 ? 20.718 -10.410 30.301 1.00 22.10 ? 367 LYS A CD 1 ATOM 2865 C CE . LYS A 1 367 ? 19.201 -10.304 30.471 1.00 22.31 ? 367 LYS A CE 1 ATOM 2866 N NZ . LYS A 1 367 ? 18.493 -10.943 29.324 1.00 23.42 ? 367 LYS A NZ 1 ATOM 2867 N N . GLY A 1 368 ? 22.135 -6.419 30.284 1.00 14.56 ? 368 GLY A N 1 ATOM 2868 C CA . GLY A 1 368 ? 21.864 -5.076 30.758 1.00 14.71 ? 368 GLY A CA 1 ATOM 2869 C C . GLY A 1 368 ? 22.655 -3.970 30.086 1.00 14.40 ? 368 GLY A C 1 ATOM 2870 O O . GLY A 1 368 ? 22.302 -2.790 30.204 1.00 15.01 ? 368 GLY A O 1 ATOM 2871 N N . GLU A 1 369 ? 23.722 -4.306 29.364 1.00 13.58 ? 369 GLU A N 1 ATOM 2872 C CA . GLU A 1 369 ? 24.631 -3.295 28.853 1.00 13.54 ? 369 GLU A CA 1 ATOM 2873 C C . GLU A 1 369 ? 23.974 -2.428 27.769 1.00 13.58 ? 369 GLU A C 1 ATOM 2874 O O . GLU A 1 369 ? 24.270 -1.247 27.651 1.00 13.39 ? 369 GLU A O 1 ATOM 2875 C CB . GLU A 1 369 ? 25.930 -3.926 28.360 1.00 13.77 ? 369 GLU A CB 1 ATOM 2876 C CG . GLU A 1 369 ? 27.015 -2.925 28.069 1.00 13.84 ? 369 GLU A CG 1 ATOM 2877 C CD . GLU A 1 369 ? 28.376 -3.523 27.814 1.00 14.13 ? 369 GLU A CD 1 ATOM 2878 O OE1 . GLU A 1 369 ? 28.547 -4.781 27.849 1.00 14.19 ? 369 GLU A OE1 1 ATOM 2879 O OE2 . GLU A 1 369 ? 29.276 -2.714 27.572 1.00 17.87 ? 369 GLU A OE2 1 ATOM 2880 N N . GLY A 1 370 ? 23.070 -3.034 27.007 1.00 13.20 ? 370 GLY A N 1 ATOM 2881 C CA . GLY A 1 370 ? 22.388 -2.343 25.910 1.00 13.15 ? 370 GLY A CA 1 ATOM 2882 C C . GLY A 1 370 ? 21.079 -1.679 26.271 1.00 12.92 ? 370 GLY A C 1 ATOM 2883 O O . GLY A 1 370 ? 20.391 -1.173 25.413 1.00 13.56 ? 370 GLY A O 1 ATOM 2884 N N . ALA A 1 371 ? 20.729 -1.649 27.555 1.00 13.14 ? 371 ALA A N 1 ATOM 2885 C CA . ALA A 1 371 ? 19.566 -0.893 28.009 1.00 12.99 ? 371 ALA A CA 1 ATOM 2886 C C . ALA A 1 371 ? 19.783 0.587 27.718 1.00 12.52 ? 371 ALA A C 1 ATOM 2887 O O . ALA A 1 371 ? 20.873 1.093 27.976 1.00 12.98 ? 371 ALA A O 1 ATOM 2888 C CB . ALA A 1 371 ? 19.355 -1.090 29.493 1.00 13.71 ? 371 ALA A CB 1 ATOM 2889 N N . PRO A 1 372 ? 18.770 1.276 27.189 1.00 12.40 ? 372 PRO A N 1 ATOM 2890 C CA . PRO A 1 372 ? 18.861 2.723 26.993 1.00 12.98 ? 372 PRO A CA 1 ATOM 2891 C C . PRO A 1 372 ? 19.379 3.502 28.201 1.00 14.34 ? 372 PRO A C 1 ATOM 2892 O O . PRO A 1 372 ? 20.169 4.425 28.041 1.00 14.07 ? 372 PRO A O 1 ATOM 2893 C CB . PRO A 1 372 ? 17.428 3.106 26.619 1.00 13.03 ? 372 PRO A CB 1 ATOM 2894 C CG . PRO A 1 372 ? 16.950 1.940 25.863 1.00 12.83 ? 372 PRO A CG 1 ATOM 2895 C CD . PRO A 1 372 ? 17.499 0.740 26.664 1.00 12.97 ? 372 PRO A CD 1 ATOM 2896 N N . SER A 1 373 ? 18.962 3.102 29.403 1.00 15.01 ? 373 SER A N 1 ATOM 2897 C CA . SER A 1 373 ? 19.432 3.774 30.615 1.00 15.46 ? 373 SER A CA 1 ATOM 2898 C C . SER A 1 373 ? 20.950 3.660 30.800 1.00 15.51 ? 373 SER A C 1 ATOM 2899 O O . SER A 1 373 ? 21.563 4.541 31.381 1.00 16.45 ? 373 SER A O 1 ATOM 2900 C CB . SER A 1 373 ? 18.721 3.205 31.835 1.00 16.52 ? 373 SER A CB 1 ATOM 2901 O OG . SER A 1 373 ? 19.012 1.828 32.016 1.00 19.03 ? 373 SER A OG 1 ATOM 2902 N N . ASN A 1 374 ? 21.552 2.559 30.334 1.00 14.42 ? 374 ASN A N 1 ATOM 2903 C CA . ASN A 1 374 ? 23.005 2.420 30.344 1.00 13.91 ? 374 ASN A CA 1 ATOM 2904 C C . ASN A 1 374 ? 23.697 3.040 29.131 1.00 13.59 ? 374 ASN A C 1 ATOM 2905 O O . ASN A 1 374 ? 24.770 3.599 29.250 1.00 13.94 ? 374 ASN A O 1 ATOM 2906 C CB . ASN A 1 374 ? 23.439 0.952 30.479 1.00 14.04 ? 374 ASN A CB 1 ATOM 2907 C CG . ASN A 1 374 ? 24.913 0.822 30.775 1.00 14.44 ? 374 ASN A CG 1 ATOM 2908 O OD1 . ASN A 1 374 ? 25.406 1.383 31.772 1.00 15.45 ? 374 ASN A OD1 1 ATOM 2909 N ND2 . ASN A 1 374 ? 25.646 0.140 29.896 1.00 14.23 ? 374 ASN A ND2 1 ATOM 2910 N N . ILE A 1 375 ? 23.090 2.918 27.945 1.00 12.88 ? 375 ILE A N 1 ATOM 2911 C CA . ILE A 1 375 ? 23.652 3.536 26.743 1.00 12.52 ? 375 ILE A CA 1 ATOM 2912 C C . ILE A 1 375 ? 24.060 4.979 27.017 1.00 12.48 ? 375 ILE A C 1 ATOM 2913 O O . ILE A 1 375 ? 25.151 5.378 26.666 1.00 13.17 ? 375 ILE A O 1 ATOM 2914 C CB . ILE A 1 375 ? 22.649 3.439 25.554 1.00 11.86 ? 375 ILE A CB 1 ATOM 2915 C CG1 . ILE A 1 375 ? 22.555 1.992 25.068 1.00 12.57 ? 375 ILE A CG1 1 ATOM 2916 C CG2 . ILE A 1 375 ? 23.095 4.327 24.403 1.00 12.44 ? 375 ILE A CG2 1 ATOM 2917 C CD1 . ILE A 1 375 ? 21.459 1.763 24.072 1.00 12.70 ? 375 ILE A CD1 1 ATOM 2918 N N . VAL A 1 376 ? 23.174 5.768 27.618 1.00 13.11 ? 376 VAL A N 1 ATOM 2919 C CA . VAL A 1 376 ? 23.465 7.179 27.806 1.00 13.62 ? 376 VAL A CA 1 ATOM 2920 C C . VAL A 1 376 ? 24.552 7.470 28.831 1.00 14.08 ? 376 VAL A C 1 ATOM 2921 O O . VAL A 1 376 ? 25.152 8.544 28.813 1.00 15.58 ? 376 VAL A O 1 ATOM 2922 C CB . VAL A 1 376 ? 22.219 7.996 28.140 1.00 13.71 ? 376 VAL A CB 1 ATOM 2923 C CG1 . VAL A 1 376 ? 21.209 7.902 27.010 1.00 15.53 ? 376 VAL A CG1 1 ATOM 2924 C CG2 . VAL A 1 376 ? 21.605 7.618 29.481 1.00 14.75 ? 376 VAL A CG2 1 ATOM 2925 N N . GLN A 1 377 ? 24.848 6.488 29.662 1.00 14.77 ? 377 GLN A N 1 ATOM 2926 C CA . GLN A 1 377 ? 25.956 6.589 30.593 1.00 15.26 ? 377 GLN A CA 1 ATOM 2927 C C . GLN A 1 377 ? 27.274 6.249 29.913 1.00 15.94 ? 377 GLN A C 1 ATOM 2928 O O . GLN A 1 377 ? 28.315 6.628 30.397 1.00 18.59 ? 377 GLN A O 1 ATOM 2929 C CB . GLN A 1 377 ? 25.735 5.666 31.807 1.00 16.27 ? 377 GLN A CB 1 ATOM 2930 C CG . GLN A 1 377 ? 24.457 5.913 32.585 1.00 18.12 ? 377 GLN A CG 1 ATOM 2931 C CD . GLN A 1 377 ? 24.409 7.273 33.256 1.00 20.90 ? 377 GLN A CD 1 ATOM 2932 O OE1 . GLN A 1 377 ? 25.450 7.842 33.620 1.00 18.50 ? 377 GLN A OE1 1 ATOM 2933 N NE2 . GLN A 1 377 ? 23.196 7.814 33.411 1.00 22.35 ? 377 GLN A NE2 1 ATOM 2934 N N . VAL A 1 378 ? 27.230 5.504 28.815 1.00 15.64 ? 378 VAL A N 1 ATOM 2935 C CA . VAL A 1 378 ? 28.409 5.140 28.051 1.00 14.83 ? 378 VAL A CA 1 ATOM 2936 C C . VAL A 1 378 ? 28.725 6.147 26.935 1.00 14.82 ? 378 VAL A C 1 ATOM 2937 O O . VAL A 1 378 ? 29.842 6.602 26.752 1.00 16.30 ? 378 VAL A O 1 ATOM 2938 C CB . VAL A 1 378 ? 28.231 3.727 27.415 1.00 14.88 ? 378 VAL A CB 1 ATOM 2939 C CG1 . VAL A 1 378 ? 29.390 3.431 26.459 1.00 15.30 ? 378 VAL A CG1 1 ATOM 2940 C CG2 . VAL A 1 378 ? 28.107 2.662 28.515 1.00 15.23 ? 378 VAL A CG2 1 ATOM 2941 N N . GLU A 1 379 ? 27.698 6.479 26.171 1.00 13.84 ? 379 GLU A N 1 ATOM 2942 C CA . GLU A 1 379 ? 27.799 7.423 25.070 1.00 13.78 ? 379 GLU A CA 1 ATOM 2943 C C . GLU A 1 379 ? 26.551 8.306 25.155 1.00 13.35 ? 379 GLU A C 1 ATOM 2944 O O . GLU A 1 379 ? 25.445 7.870 24.773 1.00 12.99 ? 379 GLU A O 1 ATOM 2945 C CB A GLU A 1 379 ? 27.873 6.637 23.747 0.50 13.99 ? 379 GLU A CB 1 ATOM 2946 C CB B GLU A 1 379 ? 27.825 6.739 23.699 0.50 13.41 ? 379 GLU A CB 1 ATOM 2947 C CG A GLU A 1 379 ? 28.253 7.442 22.510 0.50 15.03 ? 379 GLU A CG 1 ATOM 2948 C CG B GLU A 1 379 ? 27.721 7.749 22.553 0.50 12.05 ? 379 GLU A CG 1 ATOM 2949 C CD A GLU A 1 379 ? 29.757 7.735 22.380 0.50 15.63 ? 379 GLU A CD 1 ATOM 2950 C CD B GLU A 1 379 ? 28.710 8.898 22.719 0.50 10.89 ? 379 GLU A CD 1 ATOM 2951 O OE1 A GLU A 1 379 ? 30.628 6.797 22.327 0.50 17.40 ? 379 GLU A OE1 1 ATOM 2952 O OE1 B GLU A 1 379 ? 29.916 8.614 22.739 0.50 15.04 ? 379 GLU A OE1 1 ATOM 2953 O OE2 A GLU A 1 379 ? 30.071 8.946 22.309 0.50 17.87 ? 379 GLU A OE2 1 ATOM 2954 O OE2 B GLU A 1 379 ? 28.285 10.065 22.898 0.50 10.46 ? 379 GLU A OE2 1 ATOM 2955 N N . PRO A 1 380 ? 26.679 9.532 25.678 1.00 13.43 ? 380 PRO A N 1 ATOM 2956 C CA . PRO A 1 380 ? 25.483 10.360 25.889 1.00 13.14 ? 380 PRO A CA 1 ATOM 2957 C C . PRO A 1 380 ? 24.766 10.775 24.600 1.00 12.67 ? 380 PRO A C 1 ATOM 2958 O O . PRO A 1 380 ? 23.564 11.040 24.618 1.00 13.60 ? 380 PRO A O 1 ATOM 2959 C CB . PRO A 1 380 ? 26.033 11.582 26.665 1.00 13.85 ? 380 PRO A CB 1 ATOM 2960 C CG . PRO A 1 380 ? 27.385 11.663 26.316 1.00 13.61 ? 380 PRO A CG 1 ATOM 2961 C CD . PRO A 1 380 ? 27.900 10.224 26.145 1.00 14.42 ? 380 PRO A CD 1 ATOM 2962 N N . PHE A 1 381 ? 25.494 10.839 23.493 1.00 12.33 ? 381 PHE A N 1 ATOM 2963 C CA . PHE A 1 381 ? 24.922 11.281 22.219 1.00 11.73 ? 381 PHE A CA 1 ATOM 2964 C C . PHE A 1 381 ? 25.284 10.343 21.075 1.00 11.23 ? 381 PHE A C 1 ATOM 2965 O O . PHE A 1 381 ? 26.082 10.691 20.195 1.00 12.16 ? 381 PHE A O 1 ATOM 2966 C CB . PHE A 1 381 ? 25.361 12.714 21.933 1.00 12.33 ? 381 PHE A CB 1 ATOM 2967 C CG . PHE A 1 381 ? 25.040 13.659 23.068 1.00 12.49 ? 381 PHE A CG 1 ATOM 2968 C CD1 . PHE A 1 381 ? 23.734 14.059 23.304 1.00 13.58 ? 381 PHE A CD1 1 ATOM 2969 C CD2 . PHE A 1 381 ? 26.045 14.126 23.898 1.00 14.53 ? 381 PHE A CD2 1 ATOM 2970 C CE1 . PHE A 1 381 ? 23.430 14.890 24.379 1.00 13.58 ? 381 PHE A CE1 1 ATOM 2971 C CE2 . PHE A 1 381 ? 25.738 14.978 24.966 1.00 14.43 ? 381 PHE A CE2 1 ATOM 2972 C CZ . PHE A 1 381 ? 24.459 15.347 25.203 1.00 14.61 ? 381 PHE A CZ 1 ATOM 2973 N N . PRO A 1 382 ? 24.684 9.149 21.057 1.00 10.30 ? 382 PRO A N 1 ATOM 2974 C CA . PRO A 1 382 ? 24.966 8.216 19.959 1.00 10.22 ? 382 PRO A CA 1 ATOM 2975 C C . PRO A 1 382 ? 24.597 8.818 18.596 1.00 10.15 ? 382 PRO A C 1 ATOM 2976 O O . PRO A 1 382 ? 23.617 9.546 18.468 1.00 10.96 ? 382 PRO A O 1 ATOM 2977 C CB . PRO A 1 382 ? 24.085 7.006 20.288 1.00 10.09 ? 382 PRO A CB 1 ATOM 2978 C CG . PRO A 1 382 ? 23.771 7.124 21.751 1.00 10.74 ? 382 PRO A CG 1 ATOM 2979 C CD . PRO A 1 382 ? 23.699 8.583 21.975 1.00 10.83 ? 382 PRO A CD 1 ATOM 2980 N N . GLU A 1 383 ? 25.369 8.454 17.585 1.00 9.89 ? 383 GLU A N 1 ATOM 2981 C CA . GLU A 1 383 ? 25.169 8.938 16.217 1.00 10.13 ? 383 GLU A CA 1 ATOM 2982 C C . GLU A 1 383 ? 25.911 8.018 15.252 1.00 9.97 ? 383 GLU A C 1 ATOM 2983 O O . GLU A 1 383 ? 26.798 7.243 15.656 1.00 10.53 ? 383 GLU A O 1 ATOM 2984 C CB . GLU A 1 383 ? 25.657 10.371 16.074 1.00 10.21 ? 383 GLU A CB 1 ATOM 2985 C CG . GLU A 1 383 ? 27.143 10.558 16.381 1.00 10.89 ? 383 GLU A CG 1 ATOM 2986 C CD . GLU A 1 383 ? 27.606 11.930 15.966 1.00 11.50 ? 383 GLU A CD 1 ATOM 2987 O OE1 . GLU A 1 383 ? 27.766 12.163 14.751 1.00 13.28 ? 383 GLU A OE1 1 ATOM 2988 O OE2 . GLU A 1 383 ? 27.807 12.774 16.862 1.00 13.47 ? 383 GLU A OE2 1 ATOM 2989 N N . VAL A 1 384 ? 25.504 8.108 13.988 1.00 9.68 ? 384 VAL A N 1 ATOM 2990 C CA . VAL A 1 384 ? 26.151 7.392 12.888 1.00 9.28 ? 384 VAL A CA 1 ATOM 2991 C C . VAL A 1 384 ? 26.245 8.345 11.720 1.00 9.99 ? 384 VAL A C 1 ATOM 2992 O O . VAL A 1 384 ? 25.396 9.209 11.568 1.00 9.82 ? 384 VAL A O 1 ATOM 2993 C CB . VAL A 1 384 ? 25.378 6.102 12.503 1.00 9.19 ? 384 VAL A CB 1 ATOM 2994 C CG1 . VAL A 1 384 ? 24.022 6.438 11.970 1.00 10.05 ? 384 VAL A CG1 1 ATOM 2995 C CG2 . VAL A 1 384 ? 26.171 5.207 11.523 1.00 9.35 ? 384 VAL A CG2 1 ATOM 2996 N N . THR A 1 385 ? 27.283 8.182 10.909 1.00 9.72 ? 385 THR A N 1 ATOM 2997 C CA . THR A 1 385 ? 27.383 8.861 9.624 1.00 9.56 ? 385 THR A CA 1 ATOM 2998 C C . THR A 1 385 ? 27.623 7.843 8.520 1.00 9.48 ? 385 THR A C 1 ATOM 2999 O O . THR A 1 385 ? 28.538 7.028 8.620 1.00 9.81 ? 385 THR A O 1 ATOM 3000 C CB . THR A 1 385 ? 28.501 9.918 9.656 1.00 10.87 ? 385 THR A CB 1 ATOM 3001 O OG1 . THR A 1 385 ? 28.240 10.868 10.691 1.00 11.56 ? 385 THR A OG1 1 ATOM 3002 C CG2 . THR A 1 385 ? 28.569 10.700 8.356 1.00 11.34 ? 385 THR A CG2 1 ATOM 3003 N N . TYR A 1 386 ? 26.790 7.911 7.483 1.00 9.55 ? 386 TYR A N 1 ATOM 3004 C CA . TYR A 1 386 ? 26.900 7.094 6.268 1.00 9.72 ? 386 TYR A CA 1 ATOM 3005 C C . TYR A 1 386 ? 27.396 8.024 5.165 1.00 9.88 ? 386 TYR A C 1 ATOM 3006 O O . TYR A 1 386 ? 26.848 9.110 4.976 1.00 10.94 ? 386 TYR A O 1 ATOM 3007 C CB . TYR A 1 386 ? 25.536 6.538 5.848 1.00 9.59 ? 386 TYR A CB 1 ATOM 3008 C CG . TYR A 1 386 ? 24.865 5.638 6.858 1.00 8.52 ? 386 TYR A CG 1 ATOM 3009 C CD1 . TYR A 1 386 ? 25.469 4.465 7.277 1.00 9.11 ? 386 TYR A CD1 1 ATOM 3010 C CD2 . TYR A 1 386 ? 23.594 5.916 7.356 1.00 10.04 ? 386 TYR A CD2 1 ATOM 3011 C CE1 . TYR A 1 386 ? 24.843 3.615 8.177 1.00 8.95 ? 386 TYR A CE1 1 ATOM 3012 C CE2 . TYR A 1 386 ? 22.962 5.072 8.242 1.00 10.51 ? 386 TYR A CE2 1 ATOM 3013 C CZ . TYR A 1 386 ? 23.594 3.927 8.666 1.00 8.82 ? 386 TYR A CZ 1 ATOM 3014 O OH . TYR A 1 386 ? 22.972 3.070 9.543 1.00 9.49 ? 386 TYR A OH 1 ATOM 3015 N N . THR A 1 387 ? 28.410 7.592 4.426 1.00 10.08 ? 387 THR A N 1 ATOM 3016 C CA . THR A 1 387 ? 29.053 8.426 3.424 1.00 10.29 ? 387 THR A CA 1 ATOM 3017 C C . THR A 1 387 ? 29.243 7.680 2.104 1.00 9.94 ? 387 THR A C 1 ATOM 3018 O O . THR A 1 387 ? 29.536 6.489 2.105 1.00 10.06 ? 387 THR A O 1 ATOM 3019 C CB . THR A 1 387 ? 30.403 8.913 3.988 1.00 10.43 ? 387 THR A CB 1 ATOM 3020 O OG1 . THR A 1 387 ? 30.169 9.628 5.218 1.00 11.84 ? 387 THR A OG1 1 ATOM 3021 C CG2 . THR A 1 387 ? 31.062 9.900 3.071 1.00 11.63 ? 387 THR A CG2 1 ATOM 3022 N N . ASN A 1 388 ? 29.104 8.397 0.984 1.00 9.57 ? 388 ASN A N 1 ATOM 3023 C CA . ASN A 1 388 ? 29.429 7.840 -0.348 1.00 10.24 ? 388 ASN A CA 1 ATOM 3024 C C . ASN A 1 388 ? 28.569 6.596 -0.635 1.00 10.16 ? 388 ASN A C 1 ATOM 3025 O O . ASN A 1 388 ? 29.069 5.564 -1.042 1.00 10.60 ? 388 ASN A O 1 ATOM 3026 C CB . ASN A 1 388 ? 30.935 7.511 -0.478 1.00 10.36 ? 388 ASN A CB 1 ATOM 3027 C CG . ASN A 1 388 ? 31.802 8.728 -0.390 1.00 11.37 ? 388 ASN A CG 1 ATOM 3028 O OD1 . ASN A 1 388 ? 31.426 9.812 -0.866 1.00 12.05 ? 388 ASN A OD1 1 ATOM 3029 N ND2 . ASN A 1 388 ? 33.002 8.557 0.183 1.00 13.14 ? 388 ASN A ND2 1 ATOM 3030 N N . LEU A 1 389 ? 27.263 6.714 -0.439 1.00 10.15 ? 389 LEU A N 1 ATOM 3031 C CA . LEU A 1 389 ? 26.352 5.663 -0.850 1.00 10.95 ? 389 LEU A CA 1 ATOM 3032 C C . LEU A 1 389 ? 26.523 5.457 -2.340 1.00 10.22 ? 389 LEU A C 1 ATOM 3033 O O . LEU A 1 389 ? 26.437 6.408 -3.102 1.00 11.11 ? 389 LEU A O 1 ATOM 3034 C CB . LEU A 1 389 ? 24.891 6.045 -0.577 1.00 11.09 ? 389 LEU A CB 1 ATOM 3035 C CG . LEU A 1 389 ? 24.443 6.434 0.823 1.00 14.45 ? 389 LEU A CG 1 ATOM 3036 C CD1 . LEU A 1 389 ? 22.942 6.589 0.906 1.00 13.64 ? 389 LEU A CD1 1 ATOM 3037 C CD2 . LEU A 1 389 ? 24.897 5.469 1.813 1.00 16.73 ? 389 LEU A CD2 1 ATOM 3038 N N . ARG A 1 390 ? 26.715 4.211 -2.764 1.00 10.66 ? 390 ARG A N 1 ATOM 3039 C CA . ARG A 1 390 ? 27.042 3.959 -4.141 1.00 10.60 ? 390 ARG A CA 1 ATOM 3040 C C . ARG A 1 390 ? 26.643 2.542 -4.532 1.00 10.23 ? 390 ARG A C 1 ATOM 3041 O O . ARG A 1 390 ? 26.841 1.597 -3.762 1.00 11.28 ? 390 ARG A O 1 ATOM 3042 C CB . ARG A 1 390 ? 28.532 4.229 -4.352 1.00 11.20 ? 390 ARG A CB 1 ATOM 3043 C CG . ARG A 1 390 ? 29.515 3.406 -3.557 1.00 11.60 ? 390 ARG A CG 1 ATOM 3044 C CD . ARG A 1 390 ? 30.870 4.062 -3.540 1.00 11.89 ? 390 ARG A CD 1 ATOM 3045 N NE . ARG A 1 390 ? 31.993 3.374 -2.895 1.00 12.07 ? 390 ARG A NE 1 ATOM 3046 C CZ . ARG A 1 390 ? 32.339 3.475 -1.630 1.00 12.54 ? 390 ARG A CZ 1 ATOM 3047 N NH1 . ARG A 1 390 ? 31.578 4.147 -0.769 1.00 12.45 ? 390 ARG A NH1 1 ATOM 3048 N NH2 . ARG A 1 390 ? 33.453 2.883 -1.208 1.00 15.71 ? 390 ARG A NH2 1 ATOM 3049 N N . TRP A 1 391 ? 26.123 2.378 -5.735 1.00 9.57 ? 391 TRP A N 1 ATOM 3050 C CA . TRP A 1 391 ? 25.676 1.066 -6.171 1.00 9.81 ? 391 TRP A CA 1 ATOM 3051 C C . TRP A 1 391 ? 25.824 0.892 -7.671 1.00 9.79 ? 391 TRP A C 1 ATOM 3052 O O . TRP A 1 391 ? 25.840 1.862 -8.438 1.00 10.83 ? 391 TRP A O 1 ATOM 3053 C CB . TRP A 1 391 ? 24.236 0.753 -5.700 1.00 10.33 ? 391 TRP A CB 1 ATOM 3054 C CG . TRP A 1 391 ? 23.156 1.690 -6.132 1.00 9.49 ? 391 TRP A CG 1 ATOM 3055 C CD1 . TRP A 1 391 ? 22.268 1.492 -7.153 1.00 10.53 ? 391 TRP A CD1 1 ATOM 3056 C CD2 . TRP A 1 391 ? 22.757 2.911 -5.501 1.00 9.26 ? 391 TRP A CD2 1 ATOM 3057 N NE1 . TRP A 1 391 ? 21.363 2.528 -7.219 1.00 11.44 ? 391 TRP A NE1 1 ATOM 3058 C CE2 . TRP A 1 391 ? 21.634 3.412 -6.212 1.00 11.66 ? 391 TRP A CE2 1 ATOM 3059 C CE3 . TRP A 1 391 ? 23.210 3.622 -4.385 1.00 9.58 ? 391 TRP A CE3 1 ATOM 3060 C CZ2 . TRP A 1 391 ? 20.971 4.569 -5.836 1.00 11.40 ? 391 TRP A CZ2 1 ATOM 3061 C CZ3 . TRP A 1 391 ? 22.549 4.799 -4.025 1.00 10.44 ? 391 TRP A CZ3 1 ATOM 3062 C CH2 . TRP A 1 391 ? 21.456 5.253 -4.753 1.00 11.17 ? 391 TRP A CH2 1 ATOM 3063 N N . GLY A 1 392 ? 25.954 -0.356 -8.094 1.00 10.14 ? 392 GLY A N 1 ATOM 3064 C CA . GLY A 1 392 ? 26.105 -0.649 -9.501 1.00 10.25 ? 392 GLY A CA 1 ATOM 3065 C C . GLY A 1 392 ? 26.755 -1.987 -9.756 1.00 11.08 ? 392 GLY A C 1 ATOM 3066 O O . GLY A 1 392 ? 26.548 -2.962 -9.017 1.00 11.42 ? 392 GLY A O 1 ATOM 3067 N N . GLU A 1 393 ? 27.571 -2.036 -10.808 1.00 11.60 ? 393 GLU A N 1 ATOM 3068 C CA . GLU A 1 393 ? 28.117 -3.297 -11.299 1.00 12.61 ? 393 GLU A CA 1 ATOM 3069 C C . GLU A 1 393 ? 29.013 -3.973 -10.277 1.00 12.19 ? 393 GLU A C 1 ATOM 3070 O O . GLU A 1 393 ? 29.779 -3.321 -9.568 1.00 12.47 ? 393 GLU A O 1 ATOM 3071 C CB . GLU A 1 393 ? 28.879 -3.034 -12.591 1.00 12.93 ? 393 GLU A CB 1 ATOM 3072 C CG . GLU A 1 393 ? 27.964 -2.624 -13.718 1.00 17.12 ? 393 GLU A CG 1 ATOM 3073 C CD . GLU A 1 393 ? 28.679 -2.358 -15.020 1.00 17.02 ? 393 GLU A CD 1 ATOM 3074 O OE1 . GLU A 1 393 ? 29.953 -2.464 -15.079 1.00 18.54 ? 393 GLU A OE1 1 ATOM 3075 O OE2 . GLU A 1 393 ? 27.925 -2.041 -15.973 1.00 22.18 ? 393 GLU A OE2 1 ATOM 3076 N N . ILE A 1 394 ? 28.905 -5.305 -10.195 1.00 12.96 ? 394 ILE A N 1 ATOM 3077 C CA . ILE A 1 394 ? 29.751 -6.089 -9.337 1.00 13.45 ? 394 ILE A CA 1 ATOM 3078 C C . ILE A 1 394 ? 31.216 -5.744 -9.601 1.00 13.34 ? 394 ILE A C 1 ATOM 3079 O O . ILE A 1 394 ? 31.665 -5.723 -10.740 1.00 14.94 ? 394 ILE A O 1 ATOM 3080 C CB . ILE A 1 394 ? 29.508 -7.599 -9.575 1.00 14.44 ? 394 ILE A CB 1 ATOM 3081 C CG1 . ILE A 1 394 ? 28.082 -7.999 -9.228 1.00 17.93 ? 394 ILE A CG1 1 ATOM 3082 C CG2 . ILE A 1 394 ? 30.501 -8.441 -8.788 1.00 14.31 ? 394 ILE A CG2 1 ATOM 3083 C CD1 . ILE A 1 394 ? 27.736 -7.867 -7.848 1.00 18.02 ? 394 ILE A CD1 1 ATOM 3084 N N . GLY A 1 395 ? 31.930 -5.456 -8.530 1.00 13.53 ? 395 GLY A N 1 ATOM 3085 C CA . GLY A 1 395 ? 33.342 -5.130 -8.563 1.00 13.70 ? 395 GLY A CA 1 ATOM 3086 C C . GLY A 1 395 ? 33.656 -3.663 -8.767 1.00 14.94 ? 395 GLY A C 1 ATOM 3087 O O . GLY A 1 395 ? 34.833 -3.272 -8.676 1.00 17.47 ? 395 GLY A O 1 ATOM 3088 N N . SER A 1 396 ? 32.657 -2.837 -9.065 1.00 13.84 ? 396 SER A N 1 ATOM 3089 C CA . SER A 1 396 ? 32.898 -1.448 -9.466 1.00 14.34 ? 396 SER A CA 1 ATOM 3090 C C . SER A 1 396 ? 32.822 -0.409 -8.369 1.00 13.76 ? 396 SER A C 1 ATOM 3091 O O . SER A 1 396 ? 33.236 0.731 -8.573 1.00 14.69 ? 396 SER A O 1 ATOM 3092 C CB . SER A 1 396 ? 31.945 -1.030 -10.599 1.00 14.22 ? 396 SER A CB 1 ATOM 3093 O OG . SER A 1 396 ? 30.618 -0.795 -10.156 1.00 14.29 ? 396 SER A OG 1 ATOM 3094 N N . THR A 1 397 ? 32.281 -0.755 -7.205 1.00 14.52 ? 397 THR A N 1 ATOM 3095 C CA . THR A 1 397 ? 32.062 0.274 -6.180 1.00 15.10 ? 397 THR A CA 1 ATOM 3096 C C . THR A 1 397 ? 33.220 0.485 -5.242 1.00 16.10 ? 397 THR A C 1 ATOM 3097 O O . THR A 1 397 ? 33.212 1.446 -4.481 1.00 16.49 ? 397 THR A O 1 ATOM 3098 C CB . THR A 1 397 ? 30.843 -0.026 -5.289 1.00 14.47 ? 397 THR A CB 1 ATOM 3099 O OG1 . THR A 1 397 ? 31.053 -1.250 -4.570 1.00 13.45 ? 397 THR A OG1 1 ATOM 3100 C CG2 . THR A 1 397 ? 29.563 -0.149 -6.108 1.00 14.96 ? 397 THR A CG2 1 ATOM 3101 N N . TYR A 1 398 ? 34.228 -0.365 -5.272 1.00 17.17 ? 398 TYR A N 1 ATOM 3102 C CA . TYR A 1 398 ? 35.281 -0.274 -4.260 1.00 19.11 ? 398 TYR A CA 1 ATOM 3103 C C . TYR A 1 398 ? 36.639 -0.321 -4.910 1.00 21.74 ? 398 TYR A C 1 ATOM 3104 O O . TYR A 1 398 ? 36.726 -0.271 -6.124 1.00 24.48 ? 398 TYR A O 1 ATOM 3105 C CB . TYR A 1 398 ? 35.142 -1.396 -3.228 1.00 19.15 ? 398 TYR A CB 1 ATOM 3106 C CG . TYR A 1 398 ? 35.189 -2.770 -3.844 1.00 18.08 ? 398 TYR A CG 1 ATOM 3107 C CD1 . TYR A 1 398 ? 34.053 -3.347 -4.389 1.00 17.68 ? 398 TYR A CD1 1 ATOM 3108 C CD2 . TYR A 1 398 ? 36.375 -3.470 -3.938 1.00 18.97 ? 398 TYR A CD2 1 ATOM 3109 C CE1 . TYR A 1 398 ? 34.090 -4.578 -4.978 1.00 18.37 ? 398 TYR A CE1 1 ATOM 3110 C CE2 . TYR A 1 398 ? 36.416 -4.703 -4.533 1.00 19.74 ? 398 TYR A CE2 1 ATOM 3111 C CZ . TYR A 1 398 ? 35.279 -5.257 -5.044 1.00 19.16 ? 398 TYR A CZ 1 ATOM 3112 O OH . TYR A 1 398 ? 35.325 -6.493 -5.661 1.00 21.37 ? 398 TYR A OH 1 ATOM 3113 N N . GLN A 1 399 ? 37.665 -0.421 -4.231 1.00 25.56 ? 399 GLN A N 1 HETATM 3114 N N . PCA B 1 1 ? 21.399 12.579 47.262 1.00 13.70 ? 1 PCA B N 1 HETATM 3115 C CA . PCA B 1 1 ? 20.931 13.849 47.805 1.00 12.99 ? 1 PCA B CA 1 HETATM 3116 C CB . PCA B 1 1 ? 21.696 14.078 49.114 1.00 12.62 ? 1 PCA B CB 1 HETATM 3117 C CG . PCA B 1 1 ? 22.831 13.071 49.130 1.00 11.58 ? 1 PCA B CG 1 HETATM 3118 C CD . PCA B 1 1 ? 22.556 12.161 47.975 1.00 13.11 ? 1 PCA B CD 1 HETATM 3119 O OE . PCA B 1 1 ? 23.205 11.159 47.682 1.00 13.98 ? 1 PCA B OE 1 HETATM 3120 C C . PCA B 1 1 ? 21.130 14.989 46.785 1.00 13.91 ? 1 PCA B C 1 HETATM 3121 O O . PCA B 1 1 ? 21.982 14.904 45.915 1.00 14.55 ? 1 PCA B O 1 ATOM 3122 N N . LYS B 1 2 ? 20.361 16.061 46.907 1.00 13.53 ? 2 LYS B N 1 ATOM 3123 C CA . LYS B 1 2 ? 20.436 17.185 45.975 1.00 13.90 ? 2 LYS B CA 1 ATOM 3124 C C . LYS B 1 2 ? 21.682 18.030 46.208 1.00 12.94 ? 2 LYS B C 1 ATOM 3125 O O . LYS B 1 2 ? 21.887 18.497 47.315 1.00 12.33 ? 2 LYS B O 1 ATOM 3126 C CB . LYS B 1 2 ? 19.200 18.068 46.226 1.00 14.39 ? 2 LYS B CB 1 ATOM 3127 C CG . LYS B 1 2 ? 19.013 19.233 45.288 1.00 17.84 ? 2 LYS B CG 1 ATOM 3128 C CD . LYS B 1 2 ? 17.861 20.111 45.808 1.00 19.66 ? 2 LYS B CD 1 ATOM 3129 C CE . LYS B 1 2 ? 16.789 20.268 44.830 1.00 24.45 ? 2 LYS B CE 1 ATOM 3130 N NZ . LYS B 1 2 ? 15.743 21.141 45.396 1.00 25.34 ? 2 LYS B NZ 1 ATOM 3131 N N . PRO B 1 3 ? 22.492 18.309 45.171 1.00 12.32 ? 3 PRO B N 1 ATOM 3132 C CA . PRO B 1 3 ? 23.592 19.256 45.325 1.00 12.58 ? 3 PRO B CA 1 ATOM 3133 C C . PRO B 1 3 ? 23.126 20.605 45.843 1.00 13.07 ? 3 PRO B C 1 ATOM 3134 O O . PRO B 1 3 ? 22.131 21.149 45.361 1.00 13.65 ? 3 PRO B O 1 ATOM 3135 C CB . PRO B 1 3 ? 24.173 19.352 43.918 1.00 12.58 ? 3 PRO B CB 1 ATOM 3136 C CG . PRO B 1 3 ? 23.884 17.985 43.388 1.00 12.62 ? 3 PRO B CG 1 ATOM 3137 C CD . PRO B 1 3 ? 22.500 17.677 43.842 1.00 12.49 ? 3 PRO B CD 1 ATOM 3138 N N . GLY B 1 4 ? 23.868 21.149 46.782 1.00 12.74 ? 4 GLY B N 1 ATOM 3139 C CA . GLY B 1 4 ? 23.557 22.474 47.365 1.00 12.89 ? 4 GLY B CA 1 ATOM 3140 C C . GLY B 1 4 ? 24.232 23.614 46.637 1.00 13.03 ? 4 GLY B C 1 ATOM 3141 O O . GLY B 1 4 ? 24.750 23.453 45.533 1.00 13.37 ? 4 GLY B O 1 ATOM 3142 N N . GLU B 1 5 ? 24.206 24.780 47.267 1.00 13.32 ? 5 GLU B N 1 ATOM 3143 C CA . GLU B 1 5 ? 24.737 25.984 46.674 1.00 14.58 ? 5 GLU B CA 1 ATOM 3144 C C . GLU B 1 5 ? 26.240 26.059 46.578 1.00 16.25 ? 5 GLU B C 1 ATOM 3145 O O . GLU B 1 5 ? 26.773 26.607 45.608 1.00 18.89 ? 5 GLU B O 1 ATOM 3146 C CB . GLU B 1 5 ? 24.234 27.188 47.467 1.00 15.25 ? 5 GLU B CB 1 ATOM 3147 C CG . GLU B 1 5 ? 22.825 27.542 47.096 1.00 16.57 ? 5 GLU B CG 1 ATOM 3148 C CD . GLU B 1 5 ? 22.735 28.057 45.682 1.00 18.30 ? 5 GLU B CD 1 ATOM 3149 O OE1 . GLU B 1 5 ? 23.531 28.947 45.318 1.00 20.52 ? 5 GLU B OE1 1 ATOM 3150 O OE2 . GLU B 1 5 ? 21.884 27.575 44.928 1.00 17.93 ? 5 GLU B OE2 1 ATOM 3151 N N . THR B 1 6 ? 26.927 25.544 47.589 1.00 16.30 ? 6 THR B N 1 ATOM 3152 C CA . THR B 1 6 ? 28.363 25.763 47.697 1.00 16.46 ? 6 THR B CA 1 ATOM 3153 C C . THR B 1 6 ? 29.096 25.041 46.593 1.00 16.73 ? 6 THR B C 1 ATOM 3154 O O . THR B 1 6 ? 28.818 23.877 46.298 1.00 15.01 ? 6 THR B O 1 ATOM 3155 C CB . THR B 1 6 ? 28.870 25.273 49.068 1.00 16.92 ? 6 THR B CB 1 ATOM 3156 O OG1 . THR B 1 6 ? 28.081 25.850 50.116 1.00 18.94 ? 6 THR B OG1 1 ATOM 3157 C CG2 . THR B 1 6 ? 30.288 25.753 49.312 1.00 18.05 ? 6 THR B CG2 1 ATOM 3158 N N . LYS B 1 7 ? 30.077 25.710 46.027 1.00 17.83 ? 7 LYS B N 1 ATOM 3159 C CA . LYS B 1 7 ? 30.806 25.142 44.917 1.00 18.60 ? 7 LYS B CA 1 ATOM 3160 C C . LYS B 1 7 ? 31.764 24.044 45.394 1.00 17.12 ? 7 LYS B C 1 ATOM 3161 O O . LYS B 1 7 ? 32.417 24.150 46.433 1.00 18.38 ? 7 LYS B O 1 ATOM 3162 C CB . LYS B 1 7 ? 31.558 26.215 44.137 1.00 20.57 ? 7 LYS B CB 1 ATOM 3163 C CG . LYS B 1 7 ? 31.585 25.924 42.648 1.00 23.45 ? 7 LYS B CG 1 ATOM 3164 C CD . LYS B 1 7 ? 32.385 26.965 41.874 1.00 25.40 ? 7 LYS B CD 1 ATOM 3165 C CE . LYS B 1 7 ? 33.870 26.651 41.911 1.00 30.04 ? 7 LYS B CE 1 ATOM 3166 N NZ . LYS B 1 7 ? 34.139 25.242 41.408 1.00 32.26 ? 7 LYS B NZ 1 ATOM 3167 N N . GLU B 1 8 ? 31.792 22.964 44.637 1.00 14.43 ? 8 GLU B N 1 ATOM 3168 C CA . GLU B 1 8 ? 32.749 21.886 44.818 1.00 14.03 ? 8 GLU B CA 1 ATOM 3169 C C . GLU B 1 8 ? 34.041 22.249 44.087 1.00 12.92 ? 8 GLU B C 1 ATOM 3170 O O . GLU B 1 8 ? 34.009 22.534 42.893 1.00 15.06 ? 8 GLU B O 1 ATOM 3171 C CB . GLU B 1 8 ? 32.167 20.595 44.239 1.00 13.18 ? 8 GLU B CB 1 ATOM 3172 C CG . GLU B 1 8 ? 32.988 19.348 44.522 1.00 12.59 ? 8 GLU B CG 1 ATOM 3173 C CD . GLU B 1 8 ? 32.747 18.713 45.874 1.00 11.91 ? 8 GLU B CD 1 ATOM 3174 O OE1 . GLU B 1 8 ? 31.933 19.250 46.642 1.00 11.50 ? 8 GLU B OE1 1 ATOM 3175 O OE2 . GLU B 1 8 ? 33.354 17.637 46.135 1.00 12.36 ? 8 GLU B OE2 1 ATOM 3176 N N . VAL B 1 9 ? 35.161 22.264 44.800 1.00 11.97 ? 9 VAL B N 1 ATOM 3177 C CA . VAL B 1 9 ? 36.458 22.597 44.234 1.00 12.31 ? 9 VAL B CA 1 ATOM 3178 C C . VAL B 1 9 ? 37.365 21.374 44.402 1.00 11.75 ? 9 VAL B C 1 ATOM 3179 O O . VAL B 1 9 ? 37.952 21.147 45.467 1.00 11.06 ? 9 VAL B O 1 ATOM 3180 C CB . VAL B 1 9 ? 37.070 23.854 44.887 1.00 12.96 ? 9 VAL B CB 1 ATOM 3181 C CG1 . VAL B 1 9 ? 38.443 24.151 44.308 1.00 14.63 ? 9 VAL B CG1 1 ATOM 3182 C CG2 . VAL B 1 9 ? 36.157 25.050 44.652 1.00 13.97 ? 9 VAL B CG2 1 ATOM 3183 N N . HIS B 1 10 ? 37.461 20.568 43.358 1.00 11.02 ? 10 HIS B N 1 ATOM 3184 C CA . HIS B 1 10 ? 38.227 19.324 43.445 1.00 10.86 ? 10 HIS B CA 1 ATOM 3185 C C . HIS B 1 10 ? 39.724 19.606 43.354 1.00 10.44 ? 10 HIS B C 1 ATOM 3186 O O . HIS B 1 10 ? 40.168 20.308 42.427 1.00 11.07 ? 10 HIS B O 1 ATOM 3187 C CB . HIS B 1 10 ? 37.893 18.414 42.272 1.00 10.44 ? 10 HIS B CB 1 ATOM 3188 C CG . HIS B 1 10 ? 36.452 18.039 42.171 1.00 10.24 ? 10 HIS B CG 1 ATOM 3189 N ND1 . HIS B 1 10 ? 35.592 18.616 41.266 1.00 12.21 ? 10 HIS B ND1 1 ATOM 3190 C CD2 . HIS B 1 10 ? 35.736 17.091 42.821 1.00 10.65 ? 10 HIS B CD2 1 ATOM 3191 C CE1 . HIS B 1 10 ? 34.399 18.055 41.382 1.00 10.47 ? 10 HIS B CE1 1 ATOM 3192 N NE2 . HIS B 1 10 ? 34.464 17.117 42.308 1.00 11.18 ? 10 HIS B NE2 1 ATOM 3193 N N . PRO B 1 11 ? 40.536 19.030 44.234 1.00 10.43 ? 11 PRO B N 1 ATOM 3194 C CA . PRO B 1 11 ? 41.972 19.047 44.011 1.00 10.44 ? 11 PRO B CA 1 ATOM 3195 C C . PRO B 1 11 ? 42.343 18.332 42.730 1.00 11.10 ? 11 PRO B C 1 ATOM 3196 O O . PRO B 1 11 ? 41.748 17.312 42.388 1.00 11.00 ? 11 PRO B O 1 ATOM 3197 C CB . PRO B 1 11 ? 42.527 18.295 45.231 1.00 11.01 ? 11 PRO B CB 1 ATOM 3198 C CG . PRO B 1 11 ? 41.464 18.438 46.297 1.00 10.91 ? 11 PRO B CG 1 ATOM 3199 C CD . PRO B 1 11 ? 40.181 18.395 45.519 1.00 10.01 ? 11 PRO B CD 1 ATOM 3200 N N . GLN B 1 12 ? 43.338 18.855 42.029 1.00 11.62 ? 12 GLN B N 1 ATOM 3201 C CA . GLN B 1 12 ? 43.879 18.213 40.857 1.00 11.63 ? 12 GLN B CA 1 ATOM 3202 C C . GLN B 1 12 ? 45.029 17.310 41.243 1.00 11.10 ? 12 GLN B C 1 ATOM 3203 O O . GLN B 1 12 ? 45.831 17.657 42.112 1.00 11.82 ? 12 GLN B O 1 ATOM 3204 C CB . GLN B 1 12 ? 44.370 19.292 39.880 1.00 12.22 ? 12 GLN B CB 1 ATOM 3205 C CG . GLN B 1 12 ? 44.642 18.820 38.476 1.00 13.69 ? 12 GLN B CG 1 ATOM 3206 C CD . GLN B 1 12 ? 44.891 19.983 37.498 1.00 16.03 ? 12 GLN B CD 1 ATOM 3207 O OE1 . GLN B 1 12 ? 44.065 20.901 37.367 1.00 23.24 ? 12 GLN B OE1 1 ATOM 3208 N NE2 . GLN B 1 12 ? 46.005 19.942 36.844 1.00 22.42 ? 12 GLN B NE2 1 ATOM 3209 N N . LEU B 1 13 ? 45.136 16.160 40.587 1.00 10.57 ? 13 LEU B N 1 ATOM 3210 C CA . LEU B 1 13 ? 46.242 15.238 40.803 1.00 10.53 ? 13 LEU B CA 1 ATOM 3211 C C . LEU B 1 13 ? 46.723 14.757 39.444 1.00 10.29 ? 13 LEU B C 1 ATOM 3212 O O . LEU B 1 13 ? 45.933 14.213 38.654 1.00 10.77 ? 13 LEU B O 1 ATOM 3213 C CB . LEU B 1 13 ? 45.795 14.044 41.668 1.00 9.57 ? 13 LEU B CB 1 ATOM 3214 C CG . LEU B 1 13 ? 46.916 13.083 42.036 1.00 10.61 ? 13 LEU B CG 1 ATOM 3215 C CD1 . LEU B 1 13 ? 47.931 13.719 42.977 1.00 11.31 ? 13 LEU B CD1 1 ATOM 3216 C CD2 . LEU B 1 13 ? 46.340 11.817 42.673 1.00 11.07 ? 13 LEU B CD2 1 ATOM 3217 N N . THR B 1 14 ? 48.016 14.955 39.169 1.00 10.10 ? 14 THR B N 1 ATOM 3218 C CA . THR B 1 14 ? 48.640 14.395 37.972 1.00 10.07 ? 14 THR B CA 1 ATOM 3219 C C . THR B 1 14 ? 49.072 12.970 38.252 1.00 9.94 ? 14 THR B C 1 ATOM 3220 O O . THR B 1 14 ? 49.743 12.702 39.275 1.00 10.59 ? 14 THR B O 1 ATOM 3221 C CB . THR B 1 14 ? 49.838 15.255 37.560 1.00 10.22 ? 14 THR B CB 1 ATOM 3222 O OG1 . THR B 1 14 ? 49.360 16.565 37.222 1.00 12.11 ? 14 THR B OG1 1 ATOM 3223 C CG2 . THR B 1 14 ? 50.553 14.654 36.339 1.00 10.76 ? 14 THR B CG2 1 ATOM 3224 N N . THR B 1 15 ? 48.657 12.057 37.377 1.00 9.85 ? 15 THR B N 1 ATOM 3225 C CA . THR B 1 15 ? 49.015 10.652 37.451 1.00 9.68 ? 15 THR B CA 1 ATOM 3226 C C . THR B 1 15 ? 49.694 10.264 36.134 1.00 10.43 ? 15 THR B C 1 ATOM 3227 O O . THR B 1 15 ? 49.927 11.126 35.285 1.00 11.08 ? 15 THR B O 1 ATOM 3228 C CB . THR B 1 15 ? 47.794 9.767 37.734 1.00 10.46 ? 15 THR B CB 1 ATOM 3229 O OG1 . THR B 1 15 ? 46.893 9.869 36.639 1.00 10.82 ? 15 THR B OG1 1 ATOM 3230 C CG2 . THR B 1 15 ? 47.029 10.250 38.956 1.00 11.15 ? 15 THR B CG2 1 ATOM 3231 N N . PHE B 1 16 ? 50.023 8.987 35.952 1.00 10.56 ? 16 PHE B N 1 ATOM 3232 C CA . PHE B 1 16 ? 50.729 8.568 34.737 1.00 10.46 ? 16 PHE B CA 1 ATOM 3233 C C . PHE B 1 16 ? 50.168 7.292 34.132 1.00 10.57 ? 16 PHE B C 1 ATOM 3234 O O . PHE B 1 16 ? 49.654 6.411 34.838 1.00 10.20 ? 16 PHE B O 1 ATOM 3235 C CB . PHE B 1 16 ? 52.229 8.362 35.013 1.00 10.88 ? 16 PHE B CB 1 ATOM 3236 C CG . PHE B 1 16 ? 52.926 9.589 35.545 1.00 10.00 ? 16 PHE B CG 1 ATOM 3237 C CD1 . PHE B 1 16 ? 53.615 10.463 34.696 1.00 10.71 ? 16 PHE B CD1 1 ATOM 3238 C CD2 . PHE B 1 16 ? 52.894 9.879 36.899 1.00 10.69 ? 16 PHE B CD2 1 ATOM 3239 C CE1 . PHE B 1 16 ? 54.211 11.576 35.184 1.00 10.45 ? 16 PHE B CE1 1 ATOM 3240 C CE2 . PHE B 1 16 ? 53.506 11.005 37.391 1.00 11.17 ? 16 PHE B CE2 1 ATOM 3241 C CZ . PHE B 1 16 ? 54.177 11.858 36.524 1.00 11.76 ? 16 PHE B CZ 1 ATOM 3242 N N . ARG B 1 17 ? 50.315 7.184 32.806 1.00 11.36 ? 17 ARG B N 1 ATOM 3243 C CA . ARG B 1 17 ? 49.992 5.964 32.059 1.00 11.23 ? 17 ARG B CA 1 ATOM 3244 C C . ARG B 1 17 ? 51.307 5.535 31.426 1.00 11.21 ? 17 ARG B C 1 ATOM 3245 O O . ARG B 1 17 ? 51.986 6.369 30.800 1.00 12.16 ? 17 ARG B O 1 ATOM 3246 C CB . ARG B 1 17 ? 48.964 6.226 30.954 1.00 11.46 ? 17 ARG B CB 1 ATOM 3247 C CG . ARG B 1 17 ? 47.680 6.868 31.460 1.00 11.92 ? 17 ARG B CG 1 ATOM 3248 C CD . ARG B 1 17 ? 46.879 6.031 32.474 1.00 12.12 ? 17 ARG B CD 1 ATOM 3249 N NE . ARG B 1 17 ? 45.757 6.855 32.898 1.00 12.31 ? 17 ARG B NE 1 ATOM 3250 C CZ . ARG B 1 17 ? 45.825 7.762 33.872 1.00 11.60 ? 17 ARG B CZ 1 ATOM 3251 N NH1 . ARG B 1 17 ? 46.921 7.890 34.610 1.00 10.81 ? 17 ARG B NH1 1 ATOM 3252 N NH2 . ARG B 1 17 ? 44.797 8.565 34.113 1.00 12.10 ? 17 ARG B NH2 1 ATOM 3253 N N . CYS B 1 18 ? 51.683 4.275 31.599 1.00 11.65 ? 18 CYS B N 1 ATOM 3254 C CA . CYS B 1 18 ? 53.023 3.801 31.262 1.00 12.18 ? 18 CYS B CA 1 ATOM 3255 C C . CYS B 1 18 ? 52.986 2.658 30.229 1.00 12.08 ? 18 CYS B C 1 ATOM 3256 O O . CYS B 1 18 ? 52.127 1.779 30.279 1.00 11.90 ? 18 CYS B O 1 ATOM 3257 C CB . CYS B 1 18 ? 53.745 3.315 32.530 1.00 12.48 ? 18 CYS B CB 1 ATOM 3258 S SG . CYS B 1 18 ? 53.768 4.526 33.886 1.00 13.50 ? 18 CYS B SG 1 ATOM 3259 N N . THR B 1 19 ? 53.931 2.688 29.289 1.00 13.13 ? 19 THR B N 1 ATOM 3260 C CA . THR B 1 19 ? 54.181 1.562 28.387 1.00 15.11 ? 19 THR B CA 1 ATOM 3261 C C . THR B 1 19 ? 55.672 1.318 28.348 1.00 16.05 ? 19 THR B C 1 ATOM 3262 O O . THR B 1 19 ? 56.456 2.214 28.644 1.00 15.20 ? 19 THR B O 1 ATOM 3263 C CB . THR B 1 19 ? 53.669 1.818 26.942 1.00 15.51 ? 19 THR B CB 1 ATOM 3264 O OG1 . THR B 1 19 ? 54.345 2.949 26.378 1.00 16.63 ? 19 THR B OG1 1 ATOM 3265 C CG2 . THR B 1 19 ? 52.200 2.154 26.920 1.00 15.74 ? 19 THR B CG2 1 ATOM 3266 N N . LYS B 1 20 ? 56.071 0.122 27.916 1.00 18.38 ? 20 LYS B N 1 ATOM 3267 C CA . LYS B 1 20 ? 57.497 -0.146 27.756 1.00 20.16 ? 20 LYS B CA 1 ATOM 3268 C C . LYS B 1 20 ? 58.146 0.737 26.689 1.00 20.95 ? 20 LYS B C 1 ATOM 3269 O O . LYS B 1 20 ? 59.238 1.248 26.919 1.00 21.68 ? 20 LYS B O 1 ATOM 3270 C CB . LYS B 1 20 ? 57.761 -1.627 27.474 1.00 21.85 ? 20 LYS B CB 1 ATOM 3271 C CG . LYS B 1 20 ? 57.669 -2.485 28.743 1.00 25.90 ? 20 LYS B CG 1 ATOM 3272 C CD . LYS B 1 20 ? 58.853 -3.429 28.946 1.00 29.15 ? 20 LYS B CD 1 ATOM 3273 C CE . LYS B 1 20 ? 58.610 -4.778 28.335 1.00 31.04 ? 20 LYS B CE 1 ATOM 3274 N NZ . LYS B 1 20 ? 59.436 -5.795 29.049 1.00 31.28 ? 20 LYS B NZ 1 ATOM 3275 N N . ARG B 1 21 ? 57.452 0.941 25.564 1.00 21.74 ? 21 ARG B N 1 ATOM 3276 C CA . ARG B 1 21 ? 57.972 1.755 24.451 1.00 22.59 ? 21 ARG B CA 1 ATOM 3277 C C . ARG B 1 21 ? 58.005 3.242 24.763 1.00 21.88 ? 21 ARG B C 1 ATOM 3278 O O . ARG B 1 21 ? 58.936 3.952 24.363 1.00 22.41 ? 21 ARG B O 1 ATOM 3279 C CB . ARG B 1 21 ? 57.147 1.520 23.182 1.00 22.51 ? 21 ARG B CB 1 ATOM 3280 C CG . ARG B 1 21 ? 57.544 2.410 21.982 1.00 25.44 ? 21 ARG B CG 1 ATOM 3281 C CD . ARG B 1 21 ? 57.623 1.652 20.673 1.00 30.45 ? 21 ARG B CD 1 ATOM 3282 N NE . ARG B 1 21 ? 56.493 0.754 20.445 1.00 36.47 ? 21 ARG B NE 1 ATOM 3283 C CZ . ARG B 1 21 ? 56.557 -0.415 19.791 1.00 39.91 ? 21 ARG B CZ 1 ATOM 3284 N NH1 . ARG B 1 21 ? 57.711 -0.875 19.295 1.00 42.07 ? 21 ARG B NH1 1 ATOM 3285 N NH2 . ARG B 1 21 ? 55.452 -1.139 19.636 1.00 39.96 ? 21 ARG B NH2 1 ATOM 3286 N N . GLY B 1 22 ? 56.973 3.733 25.454 1.00 20.60 ? 22 GLY B N 1 ATOM 3287 C CA . GLY B 1 22 ? 56.829 5.151 25.673 1.00 19.42 ? 22 GLY B CA 1 ATOM 3288 C C . GLY B 1 22 ? 57.187 5.671 27.052 1.00 18.51 ? 22 GLY B C 1 ATOM 3289 O O . GLY B 1 22 ? 57.246 6.884 27.242 1.00 19.27 ? 22 GLY B O 1 ATOM 3290 N N . GLY B 1 23 ? 57.467 4.782 28.000 1.00 17.34 ? 23 GLY B N 1 ATOM 3291 C CA . GLY B 1 23 ? 57.635 5.209 29.393 1.00 16.12 ? 23 GLY B CA 1 ATOM 3292 C C . GLY B 1 23 ? 56.325 5.731 29.997 1.00 14.83 ? 23 GLY B C 1 ATOM 3293 O O . GLY B 1 23 ? 55.235 5.428 29.519 1.00 14.52 ? 23 GLY B O 1 ATOM 3294 N N . CYS B 1 24 ? 56.457 6.533 31.039 1.00 14.63 ? 24 CYS B N 1 ATOM 3295 C CA . CYS B 1 24 ? 55.302 7.047 31.785 1.00 14.03 ? 24 CYS B CA 1 ATOM 3296 C C . CYS B 1 24 ? 54.944 8.468 31.356 1.00 13.94 ? 24 CYS B C 1 ATOM 3297 O O . CYS B 1 24 ? 55.807 9.351 31.344 1.00 15.60 ? 24 CYS B O 1 ATOM 3298 C CB . CYS B 1 24 ? 55.607 6.999 33.299 1.00 14.54 ? 24 CYS B CB 1 ATOM 3299 S SG . CYS B 1 24 ? 55.691 5.306 33.953 1.00 15.58 ? 24 CYS B SG 1 ATOM 3300 N N . LYS B 1 25 ? 53.704 8.674 30.930 1.00 13.22 ? 25 LYS B N 1 ATOM 3301 C CA . LYS B 1 25 ? 53.252 9.964 30.418 1.00 13.46 ? 25 LYS B CA 1 ATOM 3302 C C . LYS B 1 25 ? 52.169 10.514 31.348 1.00 12.74 ? 25 LYS B C 1 ATOM 3303 O O . LYS B 1 25 ? 51.299 9.769 31.793 1.00 13.09 ? 25 LYS B O 1 ATOM 3304 C CB . LYS B 1 25 ? 52.707 9.776 29.015 1.00 14.39 ? 25 LYS B CB 1 ATOM 3305 C CG . LYS B 1 25 ? 53.777 9.258 28.046 1.00 15.99 ? 25 LYS B CG 1 ATOM 3306 C CD . LYS B 1 25 ? 53.241 9.165 26.650 1.00 18.40 ? 25 LYS B CD 1 ATOM 3307 C CE . LYS B 1 25 ? 54.405 8.979 25.692 1.00 22.27 ? 25 LYS B CE 1 ATOM 3308 N NZ . LYS B 1 25 ? 55.049 10.282 25.324 1.00 27.53 ? 25 LYS B NZ 1 ATOM 3309 N N . PRO B 1 26 ? 52.247 11.791 31.665 1.00 12.56 ? 26 PRO B N 1 ATOM 3310 C CA . PRO B 1 26 ? 51.303 12.375 32.622 1.00 12.26 ? 26 PRO B CA 1 ATOM 3311 C C . PRO B 1 26 ? 49.868 12.527 32.109 1.00 12.73 ? 26 PRO B C 1 ATOM 3312 O O . PRO B 1 26 ? 49.625 12.710 30.905 1.00 14.30 ? 26 PRO B O 1 ATOM 3313 C CB . PRO B 1 26 ? 51.896 13.741 32.914 1.00 12.54 ? 26 PRO B CB 1 ATOM 3314 C CG . PRO B 1 26 ? 52.697 14.066 31.674 1.00 14.13 ? 26 PRO B CG 1 ATOM 3315 C CD . PRO B 1 26 ? 53.223 12.772 31.157 1.00 12.32 ? 26 PRO B CD 1 ATOM 3316 N N . ALA B 1 27 ? 48.937 12.458 33.049 1.00 12.60 ? 27 ALA B N 1 ATOM 3317 C CA . ALA B 1 27 ? 47.521 12.592 32.798 1.00 12.39 ? 27 ALA B CA 1 ATOM 3318 C C . ALA B 1 27 ? 46.921 13.447 33.906 1.00 11.98 ? 27 ALA B C 1 ATOM 3319 O O . ALA B 1 27 ? 47.306 13.338 35.045 1.00 11.45 ? 27 ALA B O 1 ATOM 3320 C CB . ALA B 1 27 ? 46.860 11.211 32.796 1.00 13.02 ? 27 ALA B CB 1 ATOM 3321 N N . THR B 1 28 ? 45.957 14.281 33.565 1.00 11.88 ? 28 THR B N 1 ATOM 3322 C CA . THR B 1 28 ? 45.261 15.095 34.525 1.00 11.84 ? 28 THR B CA 1 ATOM 3323 C C . THR B 1 28 ? 44.080 14.324 35.102 1.00 11.63 ? 28 THR B C 1 ATOM 3324 O O . THR B 1 28 ? 43.195 13.856 34.381 1.00 12.59 ? 28 THR B O 1 ATOM 3325 C CB . THR B 1 28 ? 44.772 16.368 33.857 1.00 12.58 ? 28 THR B CB 1 ATOM 3326 O OG1 . THR B 1 28 ? 45.927 17.135 33.454 1.00 16.49 ? 28 THR B OG1 1 ATOM 3327 C CG2 . THR B 1 28 ? 44.014 17.225 34.827 1.00 14.42 ? 28 THR B CG2 1 ATOM 3328 N N . ASN B 1 29 ? 44.065 14.251 36.421 1.00 10.45 ? 29 ASN B N 1 ATOM 3329 C CA . ASN B 1 29 ? 42.961 13.675 37.144 1.00 10.12 ? 29 ASN B CA 1 ATOM 3330 C C . ASN B 1 29 ? 42.511 14.624 38.264 1.00 9.61 ? 29 ASN B C 1 ATOM 3331 O O . ASN B 1 29 ? 43.174 15.631 38.551 1.00 10.19 ? 29 ASN B O 1 ATOM 3332 C CB . ASN B 1 29 ? 43.354 12.292 37.709 1.00 9.38 ? 29 ASN B CB 1 ATOM 3333 C CG . ASN B 1 29 ? 43.414 11.219 36.649 1.00 9.98 ? 29 ASN B CG 1 ATOM 3334 O OD1 . ASN B 1 29 ? 44.509 10.787 36.224 1.00 11.40 ? 29 ASN B OD1 1 ATOM 3335 N ND2 . ASN B 1 29 ? 42.237 10.783 36.194 1.00 10.57 ? 29 ASN B ND2 1 ATOM 3336 N N . PHE B 1 30 ? 41.372 14.304 38.878 1.00 9.33 ? 30 PHE B N 1 ATOM 3337 C CA . PHE B 1 30 ? 40.866 15.080 40.014 1.00 9.80 ? 30 PHE B CA 1 ATOM 3338 C C . PHE B 1 30 ? 40.511 14.158 41.177 1.00 9.49 ? 30 PHE B C 1 ATOM 3339 O O . PHE B 1 30 ? 40.418 12.932 40.989 1.00 9.95 ? 30 PHE B O 1 ATOM 3340 C CB . PHE B 1 30 ? 39.692 15.988 39.584 1.00 11.18 ? 30 PHE B CB 1 ATOM 3341 C CG . PHE B 1 30 ? 40.098 17.070 38.620 1.00 11.22 ? 30 PHE B CG 1 ATOM 3342 C CD1 . PHE B 1 30 ? 40.643 18.236 39.101 1.00 12.24 ? 30 PHE B CD1 1 ATOM 3343 C CD2 . PHE B 1 30 ? 40.040 16.893 37.246 1.00 11.04 ? 30 PHE B CD2 1 ATOM 3344 C CE1 . PHE B 1 30 ? 41.081 19.245 38.232 1.00 12.44 ? 30 PHE B CE1 1 ATOM 3345 C CE2 . PHE B 1 30 ? 40.474 17.879 36.389 1.00 12.66 ? 30 PHE B CE2 1 ATOM 3346 C CZ . PHE B 1 30 ? 41.002 19.058 36.879 1.00 12.66 ? 30 PHE B CZ 1 ATOM 3347 N N . ILE B 1 31 ? 40.358 14.747 42.352 1.00 9.13 ? 31 ILE B N 1 ATOM 3348 C CA . ILE B 1 31 ? 40.068 14.048 43.595 1.00 9.02 ? 31 ILE B CA 1 ATOM 3349 C C . ILE B 1 31 ? 38.725 14.492 44.136 1.00 8.85 ? 31 ILE B C 1 ATOM 3350 O O . ILE B 1 31 ? 38.450 15.687 44.215 1.00 9.94 ? 31 ILE B O 1 ATOM 3351 C CB . ILE B 1 31 ? 41.217 14.330 44.593 1.00 9.01 ? 31 ILE B CB 1 ATOM 3352 C CG1 . ILE B 1 31 ? 42.524 13.667 44.098 1.00 10.71 ? 31 ILE B CG1 1 ATOM 3353 C CG2 . ILE B 1 31 ? 40.850 13.910 45.992 1.00 9.99 ? 31 ILE B CG2 1 ATOM 3354 C CD1 . ILE B 1 31 ? 42.536 12.187 44.189 1.00 11.29 ? 31 ILE B CD1 1 ATOM 3355 N N . VAL B 1 32 ? 37.919 13.516 44.562 1.00 8.14 ? 32 VAL B N 1 ATOM 3356 C CA . VAL B 1 32 ? 36.604 13.809 45.130 1.00 8.62 ? 32 VAL B CA 1 ATOM 3357 C C . VAL B 1 32 ? 36.381 13.040 46.430 1.00 8.27 ? 32 VAL B C 1 ATOM 3358 O O . VAL B 1 32 ? 36.645 11.859 46.515 1.00 8.95 ? 32 VAL B O 1 ATOM 3359 C CB . VAL B 1 32 ? 35.458 13.531 44.113 1.00 8.13 ? 32 VAL B CB 1 ATOM 3360 C CG1 . VAL B 1 32 ? 35.305 12.064 43.785 1.00 8.96 ? 32 VAL B CG1 1 ATOM 3361 C CG2 . VAL B 1 32 ? 34.131 14.094 44.609 1.00 8.64 ? 32 VAL B CG2 1 ATOM 3362 N N . LEU B 1 33 ? 35.862 13.726 47.442 1.00 8.75 ? 33 LEU B N 1 ATOM 3363 C CA . LEU B 1 33 ? 35.532 13.102 48.711 1.00 8.47 ? 33 LEU B CA 1 ATOM 3364 C C . LEU B 1 33 ? 34.247 12.298 48.587 1.00 8.21 ? 33 LEU B C 1 ATOM 3365 O O . LEU B 1 33 ? 33.364 12.653 47.799 1.00 9.10 ? 33 LEU B O 1 ATOM 3366 C CB A LEU B 1 33 ? 35.366 14.174 49.796 0.50 9.14 ? 33 LEU B CB 1 ATOM 3367 C CB B LEU B 1 33 ? 35.383 14.191 49.789 0.50 8.76 ? 33 LEU B CB 1 ATOM 3368 C CG A LEU B 1 33 ? 36.674 14.621 50.461 0.50 10.09 ? 33 LEU B CG 1 ATOM 3369 C CG B LEU B 1 33 ? 35.485 13.754 51.259 0.50 8.15 ? 33 LEU B CG 1 ATOM 3370 C CD1 A LEU B 1 33 ? 36.528 16.029 51.047 0.50 11.28 ? 33 LEU B CD1 1 ATOM 3371 C CD1 B LEU B 1 33 ? 36.884 13.336 51.672 0.50 8.43 ? 33 LEU B CD1 1 ATOM 3372 C CD2 A LEU B 1 33 ? 37.097 13.610 51.535 0.50 10.38 ? 33 LEU B CD2 1 ATOM 3373 C CD2 B LEU B 1 33 ? 34.966 14.833 52.182 0.50 7.72 ? 33 LEU B CD2 1 ATOM 3374 N N . ASP B 1 34 ? 34.117 11.262 49.404 1.00 8.24 ? 34 ASP B N 1 ATOM 3375 C CA . ASP B 1 34 ? 32.870 10.530 49.404 1.00 8.12 ? 34 ASP B CA 1 ATOM 3376 C C . ASP B 1 34 ? 31.663 11.452 49.543 1.00 8.23 ? 34 ASP B C 1 ATOM 3377 O O . ASP B 1 34 ? 31.679 12.384 50.338 1.00 8.60 ? 34 ASP B O 1 ATOM 3378 C CB . ASP B 1 34 ? 32.809 9.467 50.495 1.00 8.04 ? 34 ASP B CB 1 ATOM 3379 C CG . ASP B 1 34 ? 31.575 8.640 50.379 1.00 8.95 ? 34 ASP B CG 1 ATOM 3380 O OD1 . ASP B 1 34 ? 31.505 7.869 49.396 1.00 9.70 ? 34 ASP B OD1 1 ATOM 3381 O OD2 . ASP B 1 34 ? 30.613 8.731 51.202 1.00 9.76 ? 34 ASP B OD2 1 ATOM 3382 N N . SER B 1 35 ? 30.594 11.161 48.794 1.00 8.51 ? 35 SER B N 1 ATOM 3383 C CA . SER B 1 35 ? 29.366 11.958 48.849 1.00 9.35 ? 35 SER B CA 1 ATOM 3384 C C . SER B 1 35 ? 28.904 12.187 50.288 1.00 9.01 ? 35 SER B C 1 ATOM 3385 O O . SER B 1 35 ? 28.582 13.311 50.664 1.00 9.71 ? 35 SER B O 1 ATOM 3386 C CB . SER B 1 35 ? 28.266 11.267 48.043 1.00 9.97 ? 35 SER B CB 1 ATOM 3387 O OG . SER B 1 35 ? 27.927 9.983 48.560 1.00 11.17 ? 35 SER B OG 1 ATOM 3388 N N . LEU B 1 36 ? 28.862 11.121 51.086 1.00 9.05 ? 36 LEU B N 1 ATOM 3389 C CA . LEU B 1 36 ? 28.295 11.209 52.429 1.00 10.10 ? 36 LEU B CA 1 ATOM 3390 C C . LEU B 1 36 ? 29.255 11.791 53.458 1.00 9.87 ? 36 LEU B C 1 ATOM 3391 O O . LEU B 1 36 ? 28.909 11.923 54.647 1.00 10.72 ? 36 LEU B O 1 ATOM 3392 C CB . LEU B 1 36 ? 27.709 9.861 52.884 1.00 10.16 ? 36 LEU B CB 1 ATOM 3393 C CG . LEU B 1 36 ? 26.604 9.326 51.956 1.00 11.41 ? 36 LEU B CG 1 ATOM 3394 C CD1 . LEU B 1 36 ? 26.061 7.987 52.422 1.00 12.85 ? 36 LEU B CD1 1 ATOM 3395 C CD2 . LEU B 1 36 ? 25.507 10.323 51.756 1.00 13.66 ? 36 LEU B CD2 1 ATOM 3396 N N . SER B 1 37 ? 30.445 12.178 53.013 1.00 9.13 ? 37 SER B N 1 ATOM 3397 C CA . SER B 1 37 ? 31.370 12.954 53.825 1.00 9.80 ? 37 SER B CA 1 ATOM 3398 C C . SER B 1 37 ? 31.221 14.453 53.559 1.00 9.77 ? 37 SER B C 1 ATOM 3399 O O . SER B 1 37 ? 31.782 15.268 54.282 1.00 11.27 ? 37 SER B O 1 ATOM 3400 C CB . SER B 1 37 ? 32.792 12.500 53.559 1.00 10.46 ? 37 SER B CB 1 ATOM 3401 O OG . SER B 1 37 ? 32.933 11.122 53.882 1.00 12.01 ? 37 SER B OG 1 ATOM 3402 N N . HIS B 1 38 ? 30.466 14.827 52.524 1.00 9.92 ? 38 HIS B N 1 ATOM 3403 C CA . HIS B 1 38 ? 30.060 16.205 52.343 1.00 10.61 ? 38 HIS B CA 1 ATOM 3404 C C . HIS B 1 38 ? 29.021 16.563 53.401 1.00 11.21 ? 38 HIS B C 1 ATOM 3405 O O . HIS B 1 38 ? 28.363 15.686 53.938 1.00 11.14 ? 38 HIS B O 1 ATOM 3406 C CB . HIS B 1 38 ? 29.467 16.411 50.941 1.00 10.91 ? 38 HIS B CB 1 ATOM 3407 C CG . HIS B 1 38 ? 30.459 16.269 49.827 1.00 10.43 ? 38 HIS B CG 1 ATOM 3408 N ND1 . HIS B 1 38 ? 31.084 15.082 49.506 1.00 9.90 ? 38 HIS B ND1 1 ATOM 3409 C CD2 . HIS B 1 38 ? 30.888 17.170 48.920 1.00 9.73 ? 38 HIS B CD2 1 ATOM 3410 C CE1 . HIS B 1 38 ? 31.888 15.280 48.467 1.00 10.48 ? 38 HIS B CE1 1 ATOM 3411 N NE2 . HIS B 1 38 ? 31.769 16.535 48.078 1.00 9.99 ? 38 HIS B NE2 1 ATOM 3412 N N . PRO B 1 39 ? 28.836 17.837 53.713 1.00 11.36 ? 39 PRO B N 1 ATOM 3413 C CA . PRO B 1 39 ? 27.725 18.200 54.607 1.00 12.46 ? 39 PRO B CA 1 ATOM 3414 C C . PRO B 1 39 ? 26.373 17.827 54.013 1.00 12.99 ? 39 PRO B C 1 ATOM 3415 O O . PRO B 1 39 ? 26.090 18.195 52.879 1.00 12.93 ? 39 PRO B O 1 ATOM 3416 C CB . PRO B 1 39 ? 27.879 19.715 54.783 1.00 13.40 ? 39 PRO B CB 1 ATOM 3417 C CG . PRO B 1 39 ? 29.272 20.023 54.390 1.00 12.48 ? 39 PRO B CG 1 ATOM 3418 C CD . PRO B 1 39 ? 29.644 19.005 53.338 1.00 12.41 ? 39 PRO B CD 1 ATOM 3419 N N . ILE B 1 40 ? 25.567 17.085 54.772 1.00 13.72 ? 40 ILE B N 1 ATOM 3420 C CA . ILE B 1 40 ? 24.243 16.645 54.370 1.00 14.92 ? 40 ILE B CA 1 ATOM 3421 C C . ILE B 1 40 ? 23.241 17.263 55.345 1.00 15.27 ? 40 ILE B C 1 ATOM 3422 O O . ILE B 1 40 ? 23.294 17.016 56.555 1.00 16.78 ? 40 ILE B O 1 ATOM 3423 C CB . ILE B 1 40 ? 24.083 15.105 54.450 1.00 15.80 ? 40 ILE B CB 1 ATOM 3424 C CG1 . ILE B 1 40 ? 25.178 14.342 53.706 1.00 17.15 ? 40 ILE B CG1 1 ATOM 3425 C CG2 . ILE B 1 40 ? 22.689 14.691 53.941 1.00 16.34 ? 40 ILE B CG2 1 ATOM 3426 C CD1 . ILE B 1 40 ? 25.183 14.570 52.237 1.00 17.96 ? 40 ILE B CD1 1 ATOM 3427 N N . HIS B 1 41 ? 22.353 18.086 54.829 1.00 15.21 ? 41 HIS B N 1 ATOM 3428 C CA . HIS B 1 41 ? 21.377 18.730 55.695 1.00 16.23 ? 41 HIS B CA 1 ATOM 3429 C C . HIS B 1 41 ? 20.021 18.730 55.012 1.00 15.98 ? 41 HIS B C 1 ATOM 3430 O O . HIS B 1 41 ? 19.893 18.475 53.841 1.00 16.65 ? 41 HIS B O 1 ATOM 3431 C CB . HIS B 1 41 ? 21.864 20.117 56.088 1.00 18.32 ? 41 HIS B CB 1 ATOM 3432 C CG . HIS B 1 41 ? 22.136 21.013 54.938 1.00 21.78 ? 41 HIS B CG 1 ATOM 3433 N ND1 . HIS B 1 41 ? 21.412 22.159 54.712 1.00 25.41 ? 41 HIS B ND1 1 ATOM 3434 C CD2 . HIS B 1 41 ? 23.062 20.949 53.955 1.00 24.35 ? 41 HIS B CD2 1 ATOM 3435 C CE1 . HIS B 1 41 ? 21.873 22.758 53.626 1.00 26.57 ? 41 HIS B CE1 1 ATOM 3436 N NE2 . HIS B 1 41 ? 22.873 22.041 53.147 1.00 25.12 ? 41 HIS B NE2 1 ATOM 3437 N N . ARG B 1 42 ? 18.983 19.023 55.773 1.00 15.54 ? 42 ARG B N 1 ATOM 3438 C CA . ARG B 1 42 ? 17.651 19.077 55.208 1.00 15.28 ? 42 ARG B CA 1 ATOM 3439 C C . ARG B 1 42 ? 17.365 20.370 54.437 1.00 14.88 ? 42 ARG B C 1 ATOM 3440 O O . ARG B 1 42 ? 17.962 21.415 54.671 1.00 15.77 ? 42 ARG B O 1 ATOM 3441 C CB . ARG B 1 42 ? 16.640 18.895 56.332 1.00 15.10 ? 42 ARG B CB 1 ATOM 3442 C CG . ARG B 1 42 ? 16.793 17.556 57.003 1.00 15.96 ? 42 ARG B CG 1 ATOM 3443 C CD . ARG B 1 42 ? 15.989 17.401 58.265 1.00 16.25 ? 42 ARG B CD 1 ATOM 3444 N NE . ARG B 1 42 ? 16.156 16.040 58.779 1.00 16.86 ? 42 ARG B NE 1 ATOM 3445 C CZ . ARG B 1 42 ? 15.241 15.340 59.415 1.00 18.09 ? 42 ARG B CZ 1 ATOM 3446 N NH1 . ARG B 1 42 ? 14.053 15.852 59.714 1.00 21.32 ? 42 ARG B NH1 1 ATOM 3447 N NH2 . ARG B 1 42 ? 15.536 14.099 59.767 1.00 20.18 ? 42 ARG B NH2 1 ATOM 3448 N N . ALA B 1 43 ? 16.391 20.280 53.529 1.00 15.59 ? 43 ALA B N 1 ATOM 3449 C CA . ALA B 1 43 ? 15.891 21.439 52.803 1.00 15.99 ? 43 ALA B CA 1 ATOM 3450 C C . ALA B 1 43 ? 15.311 22.474 53.744 1.00 16.37 ? 43 ALA B C 1 ATOM 3451 O O . ALA B 1 43 ? 14.982 22.185 54.893 1.00 15.82 ? 43 ALA B O 1 ATOM 3452 C CB . ALA B 1 43 ? 14.817 21.007 51.782 1.00 15.55 ? 43 ALA B CB 1 ATOM 3453 N N . GLU B 1 44 ? 15.126 23.685 53.232 1.00 19.56 ? 44 GLU B N 1 ATOM 3454 C CA . GLU B 1 44 ? 14.665 24.792 54.039 1.00 19.83 ? 44 GLU B CA 1 ATOM 3455 C C . GLU B 1 44 ? 13.358 24.477 54.703 1.00 18.63 ? 44 GLU B C 1 ATOM 3456 O O . GLU B 1 44 ? 12.474 23.826 54.132 1.00 18.16 ? 44 GLU B O 1 ATOM 3457 C CB . GLU B 1 44 ? 14.498 26.080 53.212 1.00 20.95 ? 44 GLU B CB 1 ATOM 3458 C CG . GLU B 1 44 ? 14.180 27.287 54.093 1.00 23.59 ? 44 GLU B CG 1 ATOM 3459 C CD . GLU B 1 44 ? 14.371 28.618 53.394 1.00 25.96 ? 44 GLU B CD 1 ATOM 3460 O OE1 . GLU B 1 44 ? 15.232 28.698 52.480 1.00 32.12 ? 44 GLU B OE1 1 ATOM 3461 O OE2 . GLU B 1 44 ? 13.634 29.600 53.737 1.00 32.18 ? 44 GLU B OE2 1 ATOM 3462 N N . GLY B 1 45 ? 13.255 24.914 55.941 1.00 18.75 ? 45 GLY B N 1 ATOM 3463 C CA . GLY B 1 45 ? 12.040 24.743 56.699 1.00 18.36 ? 45 GLY B CA 1 ATOM 3464 C C . GLY B 1 45 ? 11.791 23.375 57.283 1.00 18.58 ? 45 GLY B C 1 ATOM 3465 O O . GLY B 1 45 ? 10.791 23.168 57.953 1.00 21.04 ? 45 GLY B O 1 ATOM 3466 N N . LEU B 1 46 ? 12.669 22.406 57.020 1.00 17.85 ? 46 LEU B N 1 ATOM 3467 C CA . LEU B 1 46 ? 12.443 21.034 57.477 1.00 16.87 ? 46 LEU B CA 1 ATOM 3468 C C . LEU B 1 46 ? 13.197 20.741 58.762 1.00 17.38 ? 46 LEU B C 1 ATOM 3469 O O . LEU B 1 46 ? 13.083 19.672 59.290 1.00 18.55 ? 46 LEU B O 1 ATOM 3470 C CB . LEU B 1 46 ? 12.839 20.022 56.394 1.00 16.25 ? 46 LEU B CB 1 ATOM 3471 C CG . LEU B 1 46 ? 12.020 20.127 55.097 1.00 16.22 ? 46 LEU B CG 1 ATOM 3472 C CD1 . LEU B 1 46 ? 12.424 18.993 54.196 1.00 15.45 ? 46 LEU B CD1 1 ATOM 3473 C CD2 . LEU B 1 46 ? 10.524 20.080 55.365 1.00 16.40 ? 46 LEU B CD2 1 ATOM 3474 N N . GLY B 1 47 ? 13.968 21.708 59.220 1.00 17.17 ? 47 GLY B N 1 ATOM 3475 C CA . GLY B 1 47 ? 14.601 21.621 60.532 1.00 16.65 ? 47 GLY B CA 1 ATOM 3476 C C . GLY B 1 47 ? 15.963 20.979 60.481 1.00 15.82 ? 47 GLY B C 1 ATOM 3477 O O . GLY B 1 47 ? 16.465 20.636 59.421 1.00 15.89 ? 47 GLY B O 1 ATOM 3478 N N . PRO B 1 48 ? 16.550 20.771 61.655 1.00 15.50 ? 48 PRO B N 1 ATOM 3479 C CA . PRO B 1 48 ? 17.873 20.193 61.769 1.00 16.06 ? 48 PRO B CA 1 ATOM 3480 C C . PRO B 1 48 ? 17.778 18.641 61.725 1.00 16.30 ? 48 PRO B C 1 ATOM 3481 O O . PRO B 1 48 ? 16.675 18.093 61.664 1.00 18.54 ? 48 PRO B O 1 ATOM 3482 C CB . PRO B 1 48 ? 18.311 20.713 63.147 1.00 16.46 ? 48 PRO B CB 1 ATOM 3483 C CG . PRO B 1 48 ? 17.041 20.671 63.967 1.00 16.47 ? 48 PRO B CG 1 ATOM 3484 C CD . PRO B 1 48 ? 15.967 21.075 62.983 1.00 15.81 ? 48 PRO B CD 1 ATOM 3485 N N . GLY B 1 49 ? 18.911 17.954 61.765 1.00 18.34 ? 49 GLY B N 1 ATOM 3486 C CA . GLY B 1 49 ? 18.949 16.502 61.938 1.00 18.48 ? 49 GLY B CA 1 ATOM 3487 C C . GLY B 1 49 ? 19.541 15.624 60.861 1.00 19.71 ? 49 GLY B C 1 ATOM 3488 O O . GLY B 1 49 ? 19.710 14.417 61.066 1.00 22.54 ? 49 GLY B O 1 ATOM 3489 N N . GLY B 1 50 ? 19.857 16.197 59.718 1.00 19.72 ? 50 GLY B N 1 ATOM 3490 C CA . GLY B 1 50 ? 20.512 15.435 58.643 1.00 17.93 ? 50 GLY B CA 1 ATOM 3491 C C . GLY B 1 50 ? 19.612 14.398 58.001 1.00 16.21 ? 50 GLY B C 1 ATOM 3492 O O . GLY B 1 50 ? 18.419 14.339 58.284 1.00 15.77 ? 50 GLY B O 1 ATOM 3493 N N . CYS B 1 51 ? 20.194 13.555 57.162 1.00 15.13 ? 51 CYS B N 1 ATOM 3494 C CA . CYS B 1 51 ? 19.427 12.546 56.461 1.00 14.93 ? 51 CYS B CA 1 ATOM 3495 C C . CYS B 1 51 ? 19.981 11.143 56.674 1.00 14.12 ? 51 CYS B C 1 ATOM 3496 O O . CYS B 1 51 ? 19.905 10.284 55.790 1.00 13.58 ? 51 CYS B O 1 ATOM 3497 C CB . CYS B 1 51 ? 19.311 12.918 54.983 1.00 14.55 ? 51 CYS B CB 1 ATOM 3498 S SG . CYS B 1 51 ? 18.234 14.345 54.693 1.00 14.08 ? 51 CYS B SG 1 ATOM 3499 N N . GLY B 1 52 ? 20.477 10.909 57.887 1.00 15.10 ? 52 GLY B N 1 ATOM 3500 C CA . GLY B 1 52 ? 20.852 9.585 58.340 1.00 15.30 ? 52 GLY B CA 1 ATOM 3501 C C . GLY B 1 52 ? 22.341 9.432 58.583 1.00 15.10 ? 52 GLY B C 1 ATOM 3502 O O . GLY B 1 52 ? 23.185 10.089 57.945 1.00 15.34 ? 52 GLY B O 1 ATOM 3503 N N . ASP B 1 53 ? 22.648 8.560 59.528 1.00 15.76 ? 53 ASP B N 1 ATOM 3504 C CA . ASP B 1 53 ? 24.015 8.257 59.891 1.00 16.24 ? 53 ASP B CA 1 ATOM 3505 C C . ASP B 1 53 ? 24.437 6.948 59.250 1.00 15.06 ? 53 ASP B C 1 ATOM 3506 O O . ASP B 1 53 ? 23.621 6.115 58.872 1.00 14.89 ? 53 ASP B O 1 ATOM 3507 C CB . ASP B 1 53 ? 24.155 8.124 61.404 1.00 17.96 ? 53 ASP B CB 1 ATOM 3508 C CG . ASP B 1 53 ? 23.781 9.384 62.148 1.00 22.11 ? 53 ASP B CG 1 ATOM 3509 O OD1 . ASP B 1 53 ? 24.266 10.472 61.784 1.00 25.31 ? 53 ASP B OD1 1 ATOM 3510 O OD2 . ASP B 1 53 ? 23.029 9.342 63.139 1.00 30.03 ? 53 ASP B OD2 1 ATOM 3511 N N . TRP B 1 54 ? 25.747 6.748 59.182 1.00 14.85 ? 54 TRP B N 1 ATOM 3512 C CA . TRP B 1 54 ? 26.315 5.526 58.638 1.00 14.50 ? 54 TRP B CA 1 ATOM 3513 C C . TRP B 1 54 ? 25.737 4.320 59.384 1.00 14.78 ? 54 TRP B C 1 ATOM 3514 O O . TRP B 1 54 ? 25.608 4.337 60.631 1.00 15.23 ? 54 TRP B O 1 ATOM 3515 C CB . TRP B 1 54 ? 27.832 5.596 58.797 1.00 14.95 ? 54 TRP B CB 1 ATOM 3516 C CG . TRP B 1 54 ? 28.577 4.458 58.183 1.00 15.08 ? 54 TRP B CG 1 ATOM 3517 C CD1 . TRP B 1 54 ? 28.994 4.334 56.885 1.00 15.04 ? 54 TRP B CD1 1 ATOM 3518 C CD2 . TRP B 1 54 ? 28.986 3.268 58.845 1.00 16.76 ? 54 TRP B CD2 1 ATOM 3519 N NE1 . TRP B 1 54 ? 29.660 3.143 56.712 1.00 14.95 ? 54 TRP B NE1 1 ATOM 3520 C CE2 . TRP B 1 54 ? 29.685 2.480 57.909 1.00 16.76 ? 54 TRP B CE2 1 ATOM 3521 C CE3 . TRP B 1 54 ? 28.863 2.791 60.158 1.00 19.29 ? 54 TRP B CE3 1 ATOM 3522 C CZ2 . TRP B 1 54 ? 30.218 1.231 58.232 1.00 18.76 ? 54 TRP B CZ2 1 ATOM 3523 C CZ3 . TRP B 1 54 ? 29.385 1.548 60.472 1.00 19.08 ? 54 TRP B CZ3 1 ATOM 3524 C CH2 . TRP B 1 54 ? 30.052 0.782 59.513 1.00 19.01 ? 54 TRP B CH2 1 ATOM 3525 N N . GLY B 1 55 ? 25.392 3.294 58.619 1.00 13.86 ? 55 GLY B N 1 ATOM 3526 C CA . GLY B 1 55 ? 24.826 2.071 59.158 1.00 14.36 ? 55 GLY B CA 1 ATOM 3527 C C . GLY B 1 55 ? 23.312 1.997 59.132 1.00 14.22 ? 55 GLY B C 1 ATOM 3528 O O . GLY B 1 55 ? 22.738 0.953 59.447 1.00 15.24 ? 55 GLY B O 1 ATOM 3529 N N . ASN B 1 56 ? 22.666 3.085 58.733 1.00 14.06 ? 56 ASN B N 1 ATOM 3530 C CA . ASN B 1 56 ? 21.206 3.208 58.789 1.00 14.46 ? 56 ASN B CA 1 ATOM 3531 C C . ASN B 1 56 ? 20.589 3.623 57.468 1.00 14.07 ? 56 ASN B C 1 ATOM 3532 O O . ASN B 1 56 ? 21.243 4.274 56.645 1.00 13.97 ? 56 ASN B O 1 ATOM 3533 C CB A ASN B 1 56 ? 20.845 4.256 59.834 0.50 15.00 ? 56 ASN B CB 1 ATOM 3534 C CB B ASN B 1 56 ? 20.809 4.265 59.828 0.50 14.82 ? 56 ASN B CB 1 ATOM 3535 C CG A ASN B 1 56 ? 21.358 3.897 61.190 0.50 16.53 ? 56 ASN B CG 1 ATOM 3536 C CG B ASN B 1 56 ? 21.065 3.827 61.253 0.50 15.51 ? 56 ASN B CG 1 ATOM 3537 O OD1 A ASN B 1 56 ? 20.812 3.018 61.842 0.50 18.73 ? 56 ASN B OD1 1 ATOM 3538 O OD1 B ASN B 1 56 ? 21.257 2.646 61.539 0.50 18.10 ? 56 ASN B OD1 1 ATOM 3539 N ND2 A ASN B 1 56 ? 22.446 4.534 61.606 0.50 17.61 ? 56 ASN B ND2 1 ATOM 3540 N ND2 B ASN B 1 56 ? 21.073 4.790 62.158 0.50 14.92 ? 56 ASN B ND2 1 ATOM 3541 N N . PRO B 1 57 ? 19.303 3.321 57.287 1.00 13.66 ? 57 PRO B N 1 ATOM 3542 C CA . PRO B 1 57 ? 18.522 3.947 56.235 1.00 14.22 ? 57 PRO B CA 1 ATOM 3543 C C . PRO B 1 57 ? 18.355 5.416 56.598 1.00 14.04 ? 57 PRO B C 1 ATOM 3544 O O . PRO B 1 57 ? 18.603 5.807 57.748 1.00 15.55 ? 57 PRO B O 1 ATOM 3545 C CB . PRO B 1 57 ? 17.179 3.206 56.290 1.00 14.17 ? 57 PRO B CB 1 ATOM 3546 C CG . PRO B 1 57 ? 17.142 2.567 57.593 1.00 15.44 ? 57 PRO B CG 1 ATOM 3547 C CD . PRO B 1 57 ? 18.496 2.428 58.133 1.00 14.65 ? 57 PRO B CD 1 ATOM 3548 N N . PRO B 1 58 ? 17.928 6.237 55.650 1.00 13.73 ? 58 PRO B N 1 ATOM 3549 C CA . PRO B 1 58 ? 17.663 7.625 55.965 1.00 13.94 ? 58 PRO B CA 1 ATOM 3550 C C . PRO B 1 58 ? 16.346 7.721 56.763 1.00 14.85 ? 58 PRO B C 1 ATOM 3551 O O . PRO B 1 58 ? 15.545 6.793 56.717 1.00 14.76 ? 58 PRO B O 1 ATOM 3552 C CB . PRO B 1 58 ? 17.538 8.269 54.579 1.00 13.69 ? 58 PRO B CB 1 ATOM 3553 C CG . PRO B 1 58 ? 16.988 7.192 53.734 1.00 13.20 ? 58 PRO B CG 1 ATOM 3554 C CD . PRO B 1 58 ? 17.597 5.930 54.250 1.00 13.15 ? 58 PRO B CD 1 ATOM 3555 N N . PRO B 1 59 ? 16.163 8.791 57.520 1.00 15.35 ? 59 PRO B N 1 ATOM 3556 C CA . PRO B 1 59 ? 14.991 8.914 58.373 1.00 16.41 ? 59 PRO B CA 1 ATOM 3557 C C . PRO B 1 59 ? 13.706 9.018 57.571 1.00 16.80 ? 59 PRO B C 1 ATOM 3558 O O . PRO B 1 59 ? 13.655 9.699 56.548 1.00 16.74 ? 59 PRO B O 1 ATOM 3559 C CB . PRO B 1 59 ? 15.265 10.186 59.173 1.00 16.62 ? 59 PRO B CB 1 ATOM 3560 C CG . PRO B 1 59 ? 16.297 10.940 58.421 1.00 16.95 ? 59 PRO B CG 1 ATOM 3561 C CD . PRO B 1 59 ? 17.069 9.944 57.644 1.00 16.01 ? 59 PRO B CD 1 ATOM 3562 N N . LYS B 1 60 ? 12.645 8.381 58.074 1.00 17.42 ? 60 LYS B N 1 ATOM 3563 C CA . LYS B 1 60 ? 11.359 8.395 57.382 1.00 19.57 ? 60 LYS B CA 1 ATOM 3564 C C . LYS B 1 60 ? 10.674 9.765 57.355 1.00 19.29 ? 60 LYS B C 1 ATOM 3565 O O . LYS B 1 60 ? 9.864 10.004 56.452 1.00 19.57 ? 60 LYS B O 1 ATOM 3566 C CB . LYS B 1 60 ? 10.382 7.369 57.972 1.00 20.34 ? 60 LYS B CB 1 ATOM 3567 C CG . LYS B 1 60 ? 10.782 5.931 57.799 1.00 23.38 ? 60 LYS B CG 1 ATOM 3568 C CD . LYS B 1 60 ? 9.724 5.026 58.412 1.00 23.64 ? 60 LYS B CD 1 ATOM 3569 C CE . LYS B 1 60 ? 10.226 3.599 58.533 1.00 26.52 ? 60 LYS B CE 1 ATOM 3570 N NZ . LYS B 1 60 ? 9.116 2.610 58.767 1.00 27.75 ? 60 LYS B NZ 1 ATOM 3571 N N . ASP B 1 61 ? 10.973 10.656 58.301 1.00 19.82 ? 61 ASP B N 1 ATOM 3572 C CA . ASP B 1 61 ? 10.289 11.964 58.306 1.00 20.84 ? 61 ASP B CA 1 ATOM 3573 C C . ASP B 1 61 ? 10.553 12.724 56.997 1.00 20.74 ? 61 ASP B C 1 ATOM 3574 O O . ASP B 1 61 ? 9.607 13.202 56.367 1.00 23.78 ? 61 ASP B O 1 ATOM 3575 C CB . ASP B 1 61 ? 10.538 12.797 59.587 1.00 21.74 ? 61 ASP B CB 1 ATOM 3576 C CG . ASP B 1 61 ? 12.009 13.026 59.910 1.00 23.01 ? 61 ASP B CG 1 ATOM 3577 O OD1 . ASP B 1 61 ? 12.888 12.615 59.125 1.00 24.79 ? 61 ASP B OD1 1 ATOM 3578 O OD2 . ASP B 1 61 ? 12.391 13.615 60.962 1.00 23.73 ? 61 ASP B OD2 1 ATOM 3579 N N . VAL B 1 62 ? 11.796 12.733 56.514 1.00 18.68 ? 62 VAL B N 1 ATOM 3580 C CA . VAL B 1 62 ? 12.152 13.439 55.285 1.00 18.33 ? 62 VAL B CA 1 ATOM 3581 C C . VAL B 1 62 ? 12.349 12.515 54.087 1.00 17.05 ? 62 VAL B C 1 ATOM 3582 O O . VAL B 1 62 ? 12.327 12.973 52.934 1.00 16.94 ? 62 VAL B O 1 ATOM 3583 C CB . VAL B 1 62 ? 13.415 14.313 55.467 1.00 18.63 ? 62 VAL B CB 1 ATOM 3584 C CG1 . VAL B 1 62 ? 13.105 15.540 56.333 1.00 21.18 ? 62 VAL B CG1 1 ATOM 3585 C CG2 . VAL B 1 62 ? 14.589 13.495 56.037 1.00 19.13 ? 62 VAL B CG2 1 ATOM 3586 N N . CYS B 1 63 ? 12.515 11.219 54.342 1.00 15.67 ? 63 CYS B N 1 ATOM 3587 C CA . CYS B 1 63 ? 12.769 10.255 53.287 1.00 15.60 ? 63 CYS B CA 1 ATOM 3588 C C . CYS B 1 63 ? 11.811 9.057 53.351 1.00 16.56 ? 63 CYS B C 1 ATOM 3589 O O . CYS B 1 63 ? 12.231 7.927 53.539 1.00 16.30 ? 63 CYS B O 1 ATOM 3590 C CB . CYS B 1 63 ? 14.230 9.783 53.369 1.00 14.55 ? 63 CYS B CB 1 ATOM 3591 S SG . CYS B 1 63 ? 15.414 11.106 53.054 1.00 14.18 ? 63 CYS B SG 1 ATOM 3592 N N . PRO B 1 64 ? 10.511 9.301 53.197 1.00 16.82 ? 64 PRO B N 1 ATOM 3593 C CA . PRO B 1 64 ? 9.567 8.180 53.109 1.00 16.98 ? 64 PRO B CA 1 ATOM 3594 C C . PRO B 1 64 ? 9.711 7.360 51.808 1.00 17.13 ? 64 PRO B C 1 ATOM 3595 O O . PRO B 1 64 ? 9.318 6.198 51.772 1.00 17.89 ? 64 PRO B O 1 ATOM 3596 C CB . PRO B 1 64 ? 8.203 8.877 53.153 1.00 17.95 ? 64 PRO B CB 1 ATOM 3597 C CG . PRO B 1 64 ? 8.464 10.259 52.663 1.00 17.10 ? 64 PRO B CG 1 ATOM 3598 C CD . PRO B 1 64 ? 9.829 10.607 53.122 1.00 17.42 ? 64 PRO B CD 1 ATOM 3599 N N . ASP B 1 65 ? 10.241 7.992 50.756 1.00 16.96 ? 65 ASP B N 1 ATOM 3600 C CA . ASP B 1 65 ? 10.507 7.380 49.473 1.00 16.48 ? 65 ASP B CA 1 ATOM 3601 C C . ASP B 1 65 ? 11.666 8.123 48.793 1.00 15.93 ? 65 ASP B C 1 ATOM 3602 O O . ASP B 1 65 ? 12.080 9.167 49.278 1.00 15.12 ? 65 ASP B O 1 ATOM 3603 C CB . ASP B 1 65 ? 9.240 7.338 48.595 1.00 17.52 ? 65 ASP B CB 1 ATOM 3604 C CG . ASP B 1 65 ? 8.536 8.662 48.494 1.00 20.80 ? 65 ASP B CG 1 ATOM 3605 O OD1 . ASP B 1 65 ? 9.202 9.688 48.262 1.00 20.79 ? 65 ASP B OD1 1 ATOM 3606 O OD2 . ASP B 1 65 ? 7.285 8.740 48.592 1.00 25.93 ? 65 ASP B OD2 1 ATOM 3607 N N . VAL B 1 66 ? 12.151 7.582 47.681 1.00 15.90 ? 66 VAL B N 1 ATOM 3608 C CA . VAL B 1 66 ? 13.341 8.107 47.012 1.00 16.03 ? 66 VAL B CA 1 ATOM 3609 C C . VAL B 1 66 ? 13.119 9.512 46.464 1.00 16.25 ? 66 VAL B C 1 ATOM 3610 O O . VAL B 1 66 ? 13.955 10.398 46.592 1.00 14.86 ? 66 VAL B O 1 ATOM 3611 C CB . VAL B 1 66 ? 13.780 7.136 45.881 1.00 16.21 ? 66 VAL B CB 1 ATOM 3612 C CG1 . VAL B 1 66 ? 14.809 7.752 44.971 1.00 17.29 ? 66 VAL B CG1 1 ATOM 3613 C CG2 . VAL B 1 66 ? 14.281 5.838 46.469 1.00 16.55 ? 66 VAL B CG2 1 ATOM 3614 N N . GLU B 1 67 ? 11.927 9.723 45.931 1.00 17.00 ? 67 GLU B N 1 ATOM 3615 C CA . GLU B 1 67 ? 11.562 10.956 45.286 1.00 17.47 ? 67 GLU B CA 1 ATOM 3616 C C . GLU B 1 67 ? 11.576 12.100 46.314 1.00 16.84 ? 67 GLU B C 1 ATOM 3617 O O . GLU B 1 67 ? 12.180 13.184 46.086 1.00 16.88 ? 67 GLU B O 1 ATOM 3618 C CB . GLU B 1 67 ? 10.175 10.732 44.671 1.00 19.05 ? 67 GLU B CB 1 ATOM 3619 C CG . GLU B 1 67 ? 10.058 9.455 43.786 1.00 24.51 ? 67 GLU B CG 1 ATOM 3620 C CD . GLU B 1 67 ? 10.079 8.087 44.513 1.00 26.77 ? 67 GLU B CD 1 ATOM 3621 O OE1 . GLU B 1 67 ? 9.755 7.997 45.679 1.00 30.97 ? 67 GLU B OE1 1 ATOM 3622 O OE2 . GLU B 1 67 ? 10.415 7.076 43.894 1.00 33.70 ? 67 GLU B OE2 1 ATOM 3623 N N . SER B 1 68 ? 10.940 11.865 47.454 1.00 16.27 ? 68 SER B N 1 ATOM 3624 C CA . SER B 1 68 ? 10.915 12.839 48.517 1.00 16.37 ? 68 SER B CA 1 ATOM 3625 C C . SER B 1 68 ? 12.316 13.117 49.094 1.00 15.24 ? 68 SER B C 1 ATOM 3626 O O . SER B 1 68 ? 12.691 14.263 49.352 1.00 15.78 ? 68 SER B O 1 ATOM 3627 C CB . SER B 1 68 ? 9.973 12.393 49.640 1.00 16.75 ? 68 SER B CB 1 ATOM 3628 O OG . SER B 1 68 ? 8.641 12.234 49.196 1.00 18.95 ? 68 SER B OG 1 ATOM 3629 N N . CYS B 1 69 ? 13.089 12.062 49.311 1.00 14.94 ? 69 CYS B N 1 ATOM 3630 C CA . CYS B 1 69 ? 14.435 12.159 49.849 1.00 15.14 ? 69 CYS B CA 1 ATOM 3631 C C . CYS B 1 69 ? 15.323 13.018 48.950 1.00 13.65 ? 69 CYS B C 1 ATOM 3632 O O . CYS B 1 69 ? 16.155 13.792 49.433 1.00 14.42 ? 69 CYS B O 1 ATOM 3633 C CB . CYS B 1 69 ? 15.037 10.756 49.999 1.00 15.75 ? 69 CYS B CB 1 ATOM 3634 S SG . CYS B 1 69 ? 16.327 10.604 51.268 1.00 15.12 ? 69 CYS B SG 1 ATOM 3635 N N . ALA B 1 70 ? 15.129 12.887 47.639 1.00 13.61 ? 70 ALA B N 1 ATOM 3636 C CA . ALA B 1 70 ? 15.906 13.619 46.654 1.00 13.28 ? 70 ALA B CA 1 ATOM 3637 C C . ALA B 1 70 ? 15.697 15.107 46.678 1.00 12.96 ? 70 ALA B C 1 ATOM 3638 O O . ALA B 1 70 ? 16.566 15.853 46.226 1.00 14.12 ? 70 ALA B O 1 ATOM 3639 C CB . ALA B 1 70 ? 15.603 13.108 45.273 1.00 13.47 ? 70 ALA B CB 1 ATOM 3640 N N . LYS B 1 71 ? 14.537 15.557 47.167 1.00 13.22 ? 71 LYS B N 1 ATOM 3641 C CA . LYS B 1 71 ? 14.230 16.986 47.273 1.00 13.90 ? 71 LYS B CA 1 ATOM 3642 C C . LYS B 1 71 ? 14.421 17.523 48.695 1.00 13.07 ? 71 LYS B C 1 ATOM 3643 O O . LYS B 1 71 ? 14.550 18.737 48.899 1.00 14.27 ? 71 LYS B O 1 ATOM 3644 C CB . LYS B 1 71 ? 12.787 17.211 46.856 1.00 14.35 ? 71 LYS B CB 1 ATOM 3645 C CG . LYS B 1 71 ? 12.465 16.758 45.439 1.00 16.58 ? 71 LYS B CG 1 ATOM 3646 C CD . LYS B 1 71 ? 11.037 17.187 45.048 1.00 17.52 ? 71 LYS B CD 1 ATOM 3647 C CE . LYS B 1 71 ? 9.991 16.323 45.690 1.00 19.47 ? 71 LYS B CE 1 ATOM 3648 N NZ . LYS B 1 71 ? 8.706 16.418 44.927 1.00 21.17 ? 71 LYS B NZ 1 ATOM 3649 N N . ASN B 1 72 ? 14.401 16.633 49.685 1.00 12.32 ? 72 ASN B N 1 ATOM 3650 C CA . ASN B 1 72 ? 14.417 17.067 51.088 1.00 13.05 ? 72 ASN B CA 1 ATOM 3651 C C . ASN B 1 72 ? 15.806 17.034 51.717 1.00 13.21 ? 72 ASN B C 1 ATOM 3652 O O . ASN B 1 72 ? 15.992 17.540 52.819 1.00 13.60 ? 72 ASN B O 1 ATOM 3653 C CB . ASN B 1 72 ? 13.485 16.216 51.928 1.00 13.31 ? 72 ASN B CB 1 ATOM 3654 C CG . ASN B 1 72 ? 12.034 16.469 51.635 1.00 12.75 ? 72 ASN B CG 1 ATOM 3655 O OD1 . ASN B 1 72 ? 11.655 17.525 51.114 1.00 14.12 ? 72 ASN B OD1 1 ATOM 3656 N ND2 . ASN B 1 72 ? 11.198 15.502 51.993 1.00 14.98 ? 72 ASN B ND2 1 ATOM 3657 N N . CYS B 1 73 ? 16.767 16.416 51.030 1.00 12.85 ? 73 CYS B N 1 ATOM 3658 C CA . CYS B 1 73 ? 18.116 16.222 51.571 1.00 12.33 ? 73 CYS B CA 1 ATOM 3659 C C . CYS B 1 73 ? 19.090 16.849 50.600 1.00 12.18 ? 73 CYS B C 1 ATOM 3660 O O . CYS B 1 73 ? 19.053 16.559 49.380 1.00 12.83 ? 73 CYS B O 1 ATOM 3661 C CB . CYS B 1 73 ? 18.420 14.748 51.716 1.00 12.39 ? 73 CYS B CB 1 ATOM 3662 S SG . CYS B 1 73 ? 17.351 13.944 52.922 1.00 12.99 ? 73 CYS B SG 1 ATOM 3663 N N . ILE B 1 74 ? 19.961 17.681 51.150 1.00 12.14 ? 74 ILE B N 1 ATOM 3664 C CA . ILE B 1 74 ? 20.902 18.522 50.417 1.00 13.47 ? 74 ILE B CA 1 ATOM 3665 C C . ILE B 1 74 ? 22.343 18.144 50.748 1.00 14.03 ? 74 ILE B C 1 ATOM 3666 O O . ILE B 1 74 ? 22.702 17.995 51.917 1.00 15.02 ? 74 ILE B O 1 ATOM 3667 C CB . ILE B 1 74 ? 20.731 19.996 50.832 1.00 14.16 ? 74 ILE B CB 1 ATOM 3668 C CG1 . ILE B 1 74 ? 19.256 20.403 50.796 1.00 17.62 ? 74 ILE B CG1 1 ATOM 3669 C CG2 . ILE B 1 74 ? 21.670 20.881 50.006 1.00 15.28 ? 74 ILE B CG2 1 ATOM 3670 C CD1 . ILE B 1 74 ? 18.615 20.307 49.464 1.00 19.01 ? 74 ILE B CD1 1 ATOM 3671 N N . MET B 1 75 ? 23.161 18.028 49.707 1.00 12.89 ? 75 MET B N 1 ATOM 3672 C CA . MET B 1 75 ? 24.562 17.684 49.828 1.00 12.78 ? 75 MET B CA 1 ATOM 3673 C C . MET B 1 75 ? 25.390 18.904 49.419 1.00 11.99 ? 75 MET B C 1 ATOM 3674 O O . MET B 1 75 ? 25.391 19.305 48.247 1.00 12.45 ? 75 MET B O 1 ATOM 3675 C CB . MET B 1 75 ? 24.838 16.523 48.879 1.00 12.75 ? 75 MET B CB 1 ATOM 3676 C CG . MET B 1 75 ? 26.245 16.088 48.764 1.00 13.93 ? 75 MET B CG 1 ATOM 3677 S SD . MET B 1 75 ? 26.394 14.558 47.806 1.00 13.85 ? 75 MET B SD 1 ATOM 3678 C CE . MET B 1 75 ? 25.469 14.844 46.307 1.00 13.75 ? 75 MET B CE 1 ATOM 3679 N N . GLU B 1 76 ? 26.061 19.549 50.370 1.00 12.41 ? 76 GLU B N 1 ATOM 3680 C CA . GLU B 1 76 ? 26.801 20.773 50.062 1.00 13.01 ? 76 GLU B CA 1 ATOM 3681 C C . GLU B 1 76 ? 28.149 20.486 49.437 1.00 12.49 ? 76 GLU B C 1 ATOM 3682 O O . GLU B 1 76 ? 28.846 19.581 49.868 1.00 12.72 ? 76 GLU B O 1 ATOM 3683 C CB . GLU B 1 76 ? 27.040 21.612 51.322 1.00 15.02 ? 76 GLU B CB 1 ATOM 3684 C CG . GLU B 1 76 ? 25.837 22.288 51.922 1.00 18.01 ? 76 GLU B CG 1 ATOM 3685 C CD . GLU B 1 76 ? 25.169 23.301 51.000 1.00 17.52 ? 76 GLU B CD 1 ATOM 3686 O OE1 . GLU B 1 76 ? 25.843 23.999 50.183 1.00 18.17 ? 76 GLU B OE1 1 ATOM 3687 O OE2 . GLU B 1 76 ? 23.953 23.358 51.119 1.00 23.36 ? 76 GLU B OE2 1 ATOM 3688 N N . GLY B 1 77 ? 28.531 21.295 48.450 1.00 12.27 ? 77 GLY B N 1 ATOM 3689 C CA . GLY B 1 77 ? 29.836 21.232 47.886 1.00 12.13 ? 77 GLY B CA 1 ATOM 3690 C C . GLY B 1 77 ? 30.862 21.660 48.919 1.00 12.36 ? 77 GLY B C 1 ATOM 3691 O O . GLY B 1 77 ? 30.582 22.439 49.855 1.00 11.70 ? 77 GLY B O 1 ATOM 3692 N N . ILE B 1 78 ? 32.068 21.157 48.721 1.00 12.13 ? 78 ILE B N 1 ATOM 3693 C CA . ILE B 1 78 ? 33.220 21.462 49.563 1.00 12.17 ? 78 ILE B CA 1 ATOM 3694 C C . ILE B 1 78 ? 34.136 22.361 48.747 1.00 12.39 ? 78 ILE B C 1 ATOM 3695 O O . ILE B 1 78 ? 34.713 21.902 47.766 1.00 12.27 ? 78 ILE B O 1 ATOM 3696 C CB . ILE B 1 78 ? 33.944 20.163 49.990 1.00 11.95 ? 78 ILE B CB 1 ATOM 3697 C CG1 . ILE B 1 78 ? 33.063 19.343 50.923 1.00 12.08 ? 78 ILE B CG1 1 ATOM 3698 C CG2 . ILE B 1 78 ? 35.241 20.484 50.682 1.00 11.84 ? 78 ILE B CG2 1 ATOM 3699 C CD1 . ILE B 1 78 ? 33.578 17.977 51.214 1.00 13.03 ? 78 ILE B CD1 1 ATOM 3700 N N . PRO B 1 79 ? 34.281 23.625 49.148 1.00 12.33 ? 79 PRO B N 1 ATOM 3701 C CA . PRO B 1 79 ? 35.114 24.583 48.428 1.00 12.48 ? 79 PRO B CA 1 ATOM 3702 C C . PRO B 1 79 ? 36.569 24.580 48.832 1.00 13.03 ? 79 PRO B C 1 ATOM 3703 O O . PRO B 1 79 ? 37.404 25.147 48.115 1.00 13.65 ? 79 PRO B O 1 ATOM 3704 C CB . PRO B 1 79 ? 34.469 25.914 48.801 1.00 12.67 ? 79 PRO B CB 1 ATOM 3705 C CG . PRO B 1 79 ? 34.035 25.718 50.155 1.00 13.40 ? 79 PRO B CG 1 ATOM 3706 C CD . PRO B 1 79 ? 33.532 24.292 50.236 1.00 12.87 ? 79 PRO B CD 1 ATOM 3707 N N . ASP B 1 80 ? 36.885 23.901 49.929 1.00 12.52 ? 80 ASP B N 1 ATOM 3708 C CA . ASP B 1 80 ? 38.262 23.859 50.420 1.00 12.17 ? 80 ASP B CA 1 ATOM 3709 C C . ASP B 1 80 ? 38.529 22.499 51.039 1.00 12.04 ? 80 ASP B C 1 ATOM 3710 O O . ASP B 1 80 ? 38.212 22.241 52.205 1.00 12.06 ? 80 ASP B O 1 ATOM 3711 C CB . ASP B 1 80 ? 38.505 24.986 51.432 1.00 13.32 ? 80 ASP B CB 1 ATOM 3712 C CG . ASP B 1 80 ? 39.886 24.931 52.049 1.00 14.02 ? 80 ASP B CG 1 ATOM 3713 O OD1 . ASP B 1 80 ? 40.738 24.078 51.638 1.00 15.21 ? 80 ASP B OD1 1 ATOM 3714 O OD2 . ASP B 1 80 ? 40.187 25.740 52.958 1.00 17.16 ? 80 ASP B OD2 1 ATOM 3715 N N . TYR B 1 81 ? 39.104 21.623 50.221 1.00 11.53 ? 81 TYR B N 1 ATOM 3716 C CA . TYR B 1 81 ? 39.337 20.235 50.613 1.00 11.09 ? 81 TYR B CA 1 ATOM 3717 C C . TYR B 1 81 ? 40.323 20.093 51.756 1.00 11.42 ? 81 TYR B C 1 ATOM 3718 O O . TYR B 1 81 ? 40.338 19.057 52.439 1.00 10.75 ? 81 TYR B O 1 ATOM 3719 C CB . TYR B 1 81 ? 39.790 19.388 49.389 1.00 10.36 ? 81 TYR B CB 1 ATOM 3720 C CG . TYR B 1 81 ? 38.637 18.668 48.651 1.00 9.94 ? 81 TYR B CG 1 ATOM 3721 C CD1 . TYR B 1 81 ? 37.536 19.362 48.146 1.00 10.50 ? 81 TYR B CD1 1 ATOM 3722 C CD2 . TYR B 1 81 ? 38.686 17.304 48.433 1.00 9.43 ? 81 TYR B CD2 1 ATOM 3723 C CE1 . TYR B 1 81 ? 36.497 18.677 47.486 1.00 9.56 ? 81 TYR B CE1 1 ATOM 3724 C CE2 . TYR B 1 81 ? 37.706 16.645 47.764 1.00 9.93 ? 81 TYR B CE2 1 ATOM 3725 C CZ . TYR B 1 81 ? 36.595 17.319 47.322 1.00 10.05 ? 81 TYR B CZ 1 ATOM 3726 O OH . TYR B 1 81 ? 35.604 16.598 46.683 1.00 9.77 ? 81 TYR B OH 1 ATOM 3727 N N . SER B 1 82 ? 41.151 21.112 51.983 1.00 11.53 ? 82 SER B N 1 ATOM 3728 C CA . SER B 1 82 ? 42.105 21.054 53.098 1.00 12.07 ? 82 SER B CA 1 ATOM 3729 C C . SER B 1 82 ? 41.383 20.960 54.435 1.00 12.50 ? 82 SER B C 1 ATOM 3730 O O . SER B 1 82 ? 41.946 20.456 55.414 1.00 11.93 ? 82 SER B O 1 ATOM 3731 C CB . SER B 1 82 ? 43.080 22.237 53.088 1.00 12.30 ? 82 SER B CB 1 ATOM 3732 O OG . SER B 1 82 ? 42.448 23.456 53.463 1.00 13.51 ? 82 SER B OG 1 ATOM 3733 N N . GLN B 1 83 ? 40.138 21.417 54.484 1.00 12.62 ? 83 GLN B N 1 ATOM 3734 C CA . GLN B 1 83 ? 39.325 21.337 55.702 1.00 13.30 ? 83 GLN B CA 1 ATOM 3735 C C . GLN B 1 83 ? 38.820 19.927 55.983 1.00 13.32 ? 83 GLN B C 1 ATOM 3736 O O . GLN B 1 83 ? 38.174 19.702 56.993 1.00 13.66 ? 83 GLN B O 1 ATOM 3737 C CB . GLN B 1 83 ? 38.150 22.313 55.629 1.00 14.69 ? 83 GLN B CB 1 ATOM 3738 C CG . GLN B 1 83 ? 38.524 23.742 55.347 1.00 17.96 ? 83 GLN B CG 1 ATOM 3739 C CD . GLN B 1 83 ? 39.430 24.310 56.363 1.00 22.14 ? 83 GLN B CD 1 ATOM 3740 O OE1 . GLN B 1 83 ? 39.137 24.226 57.555 1.00 26.98 ? 83 GLN B OE1 1 ATOM 3741 N NE2 . GLN B 1 83 ? 40.548 24.872 55.928 1.00 26.04 ? 83 GLN B NE2 1 ATOM 3742 N N . TYR B 1 84 ? 39.109 18.978 55.076 1.00 11.31 ? 84 TYR B N 1 ATOM 3743 C CA . TYR B 1 84 ? 38.829 17.570 55.274 1.00 11.04 ? 84 TYR B CA 1 ATOM 3744 C C . TYR B 1 84 ? 40.112 16.759 55.201 1.00 9.90 ? 84 TYR B C 1 ATOM 3745 O O . TYR B 1 84 ? 40.062 15.552 55.059 1.00 10.61 ? 84 TYR B O 1 ATOM 3746 C CB . TYR B 1 84 ? 37.823 17.083 54.217 1.00 11.92 ? 84 TYR B CB 1 ATOM 3747 C CG . TYR B 1 84 ? 36.479 17.715 54.434 1.00 11.20 ? 84 TYR B CG 1 ATOM 3748 C CD1 . TYR B 1 84 ? 36.194 18.992 53.942 1.00 12.24 ? 84 TYR B CD1 1 ATOM 3749 C CD2 . TYR B 1 84 ? 35.477 17.054 55.140 1.00 12.35 ? 84 TYR B CD2 1 ATOM 3750 C CE1 . TYR B 1 84 ? 34.964 19.584 54.180 1.00 12.59 ? 84 TYR B CE1 1 ATOM 3751 C CE2 . TYR B 1 84 ? 34.243 17.650 55.378 1.00 13.73 ? 84 TYR B CE2 1 ATOM 3752 C CZ . TYR B 1 84 ? 33.994 18.908 54.894 1.00 12.70 ? 84 TYR B CZ 1 ATOM 3753 O OH . TYR B 1 84 ? 32.779 19.511 55.126 1.00 15.94 ? 84 TYR B OH 1 ATOM 3754 N N . GLY B 1 85 ? 41.257 17.412 55.359 1.00 9.46 ? 85 GLY B N 1 ATOM 3755 C CA . GLY B 1 85 ? 42.544 16.743 55.363 1.00 10.02 ? 85 GLY B CA 1 ATOM 3756 C C . GLY B 1 85 ? 43.008 16.230 54.025 1.00 9.56 ? 85 GLY B C 1 ATOM 3757 O O . GLY B 1 85 ? 43.869 15.356 53.969 1.00 10.19 ? 85 GLY B O 1 ATOM 3758 N N . VAL B 1 86 ? 42.510 16.824 52.940 1.00 9.66 ? 86 VAL B N 1 ATOM 3759 C CA . VAL B 1 86 ? 42.857 16.394 51.580 1.00 9.29 ? 86 VAL B CA 1 ATOM 3760 C C . VAL B 1 86 ? 43.504 17.547 50.833 1.00 9.41 ? 86 VAL B C 1 ATOM 3761 O O . VAL B 1 86 ? 42.894 18.595 50.654 1.00 10.02 ? 86 VAL B O 1 ATOM 3762 C CB . VAL B 1 86 ? 41.636 15.937 50.811 1.00 8.79 ? 86 VAL B CB 1 ATOM 3763 C CG1 . VAL B 1 86 ? 42.023 15.525 49.408 1.00 8.60 ? 86 VAL B CG1 1 ATOM 3764 C CG2 . VAL B 1 86 ? 40.937 14.774 51.525 1.00 9.94 ? 86 VAL B CG2 1 ATOM 3765 N N . THR B 1 87 ? 44.755 17.368 50.436 1.00 9.61 ? 87 THR B N 1 ATOM 3766 C CA . THR B 1 87 ? 45.438 18.352 49.604 1.00 10.32 ? 87 THR B CA 1 ATOM 3767 C C . THR B 1 87 ? 46.249 17.611 48.550 1.00 10.56 ? 87 THR B C 1 ATOM 3768 O O . THR B 1 87 ? 46.648 16.466 48.756 1.00 10.65 ? 87 THR B O 1 ATOM 3769 C CB . THR B 1 87 ? 46.411 19.269 50.430 1.00 10.70 ? 87 THR B CB 1 ATOM 3770 O OG1 . THR B 1 87 ? 47.343 18.470 51.191 1.00 11.73 ? 87 THR B OG1 1 ATOM 3771 C CG2 . THR B 1 87 ? 45.670 20.113 51.426 1.00 11.50 ? 87 THR B CG2 1 ATOM 3772 N N . THR B 1 88 ? 46.528 18.295 47.446 1.00 11.03 ? 88 THR B N 1 ATOM 3773 C CA . THR B 1 88 ? 47.443 17.788 46.445 1.00 11.43 ? 88 THR B CA 1 ATOM 3774 C C . THR B 1 88 ? 48.524 18.791 46.107 1.00 11.94 ? 88 THR B C 1 ATOM 3775 O O . THR B 1 88 ? 48.356 19.992 46.294 1.00 12.93 ? 88 THR B O 1 ATOM 3776 C CB . THR B 1 88 ? 46.719 17.400 45.143 1.00 11.20 ? 88 THR B CB 1 ATOM 3777 O OG1 . THR B 1 88 ? 46.066 18.570 44.615 1.00 11.90 ? 88 THR B OG1 1 ATOM 3778 C CG2 . THR B 1 88 ? 45.619 16.321 45.337 1.00 10.85 ? 88 THR B CG2 1 ATOM 3779 N N . ASN B 1 89 ? 49.615 18.275 45.567 1.00 12.72 ? 89 ASN B N 1 ATOM 3780 C CA . ASN B 1 89 ? 50.734 19.097 45.101 1.00 13.28 ? 89 ASN B CA 1 ATOM 3781 C C . ASN B 1 89 ? 51.340 18.366 43.915 1.00 12.66 ? 89 ASN B C 1 ATOM 3782 O O . ASN B 1 89 ? 52.150 17.476 44.085 1.00 13.17 ? 89 ASN B O 1 ATOM 3783 C CB . ASN B 1 89 ? 51.777 19.248 46.238 1.00 13.94 ? 89 ASN B CB 1 ATOM 3784 C CG . ASN B 1 89 ? 52.908 20.179 45.905 1.00 15.44 ? 89 ASN B CG 1 ATOM 3785 O OD1 . ASN B 1 89 ? 53.000 20.689 44.798 1.00 18.54 ? 89 ASN B OD1 1 ATOM 3786 N ND2 . ASN B 1 89 ? 53.794 20.407 46.889 1.00 17.94 ? 89 ASN B ND2 1 ATOM 3787 N N . GLY B 1 90 ? 50.924 18.735 42.715 1.00 12.86 ? 90 GLY B N 1 ATOM 3788 C CA . GLY B 1 90 ? 51.434 18.099 41.518 1.00 11.88 ? 90 GLY B CA 1 ATOM 3789 C C . GLY B 1 90 ? 50.992 16.656 41.417 1.00 10.96 ? 90 GLY B C 1 ATOM 3790 O O . GLY B 1 90 ? 49.811 16.379 41.166 1.00 11.18 ? 90 GLY B O 1 ATOM 3791 N N . THR B 1 91 ? 51.942 15.747 41.629 1.00 10.34 ? 91 THR B N 1 ATOM 3792 C CA . THR B 1 91 ? 51.697 14.316 41.587 1.00 10.22 ? 91 THR B CA 1 ATOM 3793 C C . THR B 1 91 ? 51.501 13.706 42.988 1.00 9.82 ? 91 THR B C 1 ATOM 3794 O O . THR B 1 91 ? 51.368 12.483 43.105 1.00 9.61 ? 91 THR B O 1 ATOM 3795 C CB . THR B 1 91 ? 52.831 13.570 40.893 1.00 10.94 ? 91 THR B CB 1 ATOM 3796 O OG1 . THR B 1 91 ? 54.015 13.659 41.689 1.00 11.43 ? 91 THR B OG1 1 ATOM 3797 C CG2 . THR B 1 91 ? 53.175 14.161 39.536 1.00 10.96 ? 91 THR B CG2 1 ATOM 3798 N N . SER B 1 92 ? 51.451 14.530 44.030 1.00 10.47 ? 92 SER B N 1 ATOM 3799 C CA . SER B 1 92 ? 51.289 14.012 45.410 1.00 10.20 ? 92 SER B CA 1 ATOM 3800 C C . SER B 1 92 ? 49.887 14.295 45.957 1.00 9.96 ? 92 SER B C 1 ATOM 3801 O O . SER B 1 92 ? 49.342 15.372 45.749 1.00 10.24 ? 92 SER B O 1 ATOM 3802 C CB . SER B 1 92 ? 52.327 14.644 46.353 1.00 11.70 ? 92 SER B CB 1 ATOM 3803 O OG . SER B 1 92 ? 53.640 14.169 46.078 1.00 15.30 ? 92 SER B OG 1 ATOM 3804 N N . LEU B 1 93 ? 49.344 13.304 46.668 1.00 9.54 ? 93 LEU B N 1 ATOM 3805 C CA . LEU B 1 93 ? 48.097 13.417 47.398 1.00 9.31 ? 93 LEU B CA 1 ATOM 3806 C C . LEU B 1 93 ? 48.419 13.172 48.868 1.00 8.86 ? 93 LEU B C 1 ATOM 3807 O O . LEU B 1 93 ? 48.898 12.079 49.228 1.00 10.06 ? 93 LEU B O 1 ATOM 3808 C CB . LEU B 1 93 ? 47.087 12.373 46.903 1.00 8.35 ? 93 LEU B CB 1 ATOM 3809 C CG . LEU B 1 93 ? 45.810 12.195 47.734 1.00 8.76 ? 93 LEU B CG 1 ATOM 3810 C CD1 . LEU B 1 93 ? 44.929 13.429 47.654 1.00 10.19 ? 93 LEU B CD1 1 ATOM 3811 C CD2 . LEU B 1 93 ? 45.067 10.975 47.266 1.00 9.67 ? 93 LEU B CD2 1 ATOM 3812 N N . ARG B 1 94 ? 48.072 14.150 49.710 1.00 9.57 ? 94 ARG B N 1 ATOM 3813 C CA . ARG B 1 94 ? 48.276 14.042 51.151 1.00 9.48 ? 94 ARG B CA 1 ATOM 3814 C C . ARG B 1 94 ? 46.928 13.849 51.819 1.00 9.50 ? 94 ARG B C 1 ATOM 3815 O O . ARG B 1 94 ? 46.019 14.683 51.628 1.00 9.83 ? 94 ARG B O 1 ATOM 3816 C CB . ARG B 1 94 ? 48.969 15.319 51.664 1.00 9.66 ? 94 ARG B CB 1 ATOM 3817 C CG . ARG B 1 94 ? 49.309 15.340 53.135 1.00 10.30 ? 94 ARG B CG 1 ATOM 3818 C CD . ARG B 1 94 ? 49.723 16.718 53.604 1.00 11.44 ? 94 ARG B CD 1 ATOM 3819 N NE . ARG B 1 94 ? 50.151 16.718 55.003 1.00 12.09 ? 94 ARG B NE 1 ATOM 3820 C CZ . ARG B 1 94 ? 50.242 17.802 55.756 1.00 13.84 ? 94 ARG B CZ 1 ATOM 3821 N NH1 . ARG B 1 94 ? 49.904 18.989 55.288 1.00 15.57 ? 94 ARG B NH1 1 ATOM 3822 N NH2 . ARG B 1 94 ? 50.665 17.679 57.004 1.00 15.04 ? 94 ARG B NH2 1 ATOM 3823 N N . LEU B 1 95 ? 46.818 12.817 52.660 1.00 9.68 ? 95 LEU B N 1 ATOM 3824 C CA . LEU B 1 95 ? 45.608 12.573 53.452 1.00 9.59 ? 95 LEU B CA 1 ATOM 3825 C C . LEU B 1 95 ? 45.964 12.658 54.927 1.00 9.68 ? 95 LEU B C 1 ATOM 3826 O O . LEU B 1 95 ? 46.811 11.898 55.433 1.00 10.54 ? 95 LEU B O 1 ATOM 3827 C CB . LEU B 1 95 ? 45.005 11.195 53.138 1.00 9.53 ? 95 LEU B CB 1 ATOM 3828 C CG . LEU B 1 95 ? 44.634 10.891 51.687 1.00 9.35 ? 95 LEU B CG 1 ATOM 3829 C CD1 . LEU B 1 95 ? 44.084 9.487 51.593 1.00 9.98 ? 95 LEU B CD1 1 ATOM 3830 C CD2 . LEU B 1 95 ? 43.583 11.852 51.190 1.00 9.87 ? 95 LEU B CD2 1 ATOM 3831 N N . GLN B 1 96 ? 45.360 13.637 55.579 1.00 9.77 ? 96 GLN B N 1 ATOM 3832 C CA . GLN B 1 96 ? 45.553 13.876 57.020 1.00 10.14 ? 96 GLN B CA 1 ATOM 3833 C C . GLN B 1 96 ? 44.360 13.316 57.776 1.00 10.06 ? 96 GLN B C 1 ATOM 3834 O O . GLN B 1 96 ? 43.230 13.664 57.493 1.00 10.18 ? 96 GLN B O 1 ATOM 3835 C CB . GLN B 1 96 ? 45.678 15.364 57.317 1.00 10.64 ? 96 GLN B CB 1 ATOM 3836 C CG . GLN B 1 96 ? 46.869 16.055 56.702 1.00 12.01 ? 96 GLN B CG 1 ATOM 3837 C CD . GLN B 1 96 ? 46.684 17.550 56.739 1.00 12.09 ? 96 GLN B CD 1 ATOM 3838 O OE1 . GLN B 1 96 ? 46.035 18.134 55.843 1.00 13.19 ? 96 GLN B OE1 1 ATOM 3839 N NE2 . GLN B 1 96 ? 47.223 18.189 57.776 1.00 16.15 ? 96 GLN B NE2 1 ATOM 3840 N N . HIS B 1 97 ? 44.627 12.452 58.754 1.00 9.60 ? 97 HIS B N 1 ATOM 3841 C CA . HIS B 1 97 ? 43.561 11.836 59.545 1.00 10.28 ? 97 HIS B CA 1 ATOM 3842 C C . HIS B 1 97 ? 42.899 12.804 60.534 1.00 10.57 ? 97 HIS B C 1 ATOM 3843 O O . HIS B 1 97 ? 41.684 12.767 60.726 1.00 10.57 ? 97 HIS B O 1 ATOM 3844 C CB . HIS B 1 97 ? 44.112 10.624 60.292 1.00 9.86 ? 97 HIS B CB 1 ATOM 3845 C CG . HIS B 1 97 ? 43.067 9.769 60.899 1.00 9.82 ? 97 HIS B CG 1 ATOM 3846 N ND1 . HIS B 1 97 ? 43.039 9.390 62.229 1.00 12.16 ? 97 HIS B ND1 1 ATOM 3847 C CD2 . HIS B 1 97 ? 41.974 9.244 60.326 1.00 8.24 ? 97 HIS B CD2 1 ATOM 3848 C CE1 . HIS B 1 97 ? 41.984 8.616 62.415 1.00 7.80 ? 97 HIS B CE1 1 ATOM 3849 N NE2 . HIS B 1 97 ? 41.318 8.526 61.281 1.00 12.22 ? 97 HIS B NE2 1 ATOM 3850 N N . ILE B 1 98 ? 43.751 13.588 61.183 1.00 11.85 ? 98 ILE B N 1 ATOM 3851 C CA . ILE B 1 98 ? 43.365 14.535 62.246 1.00 12.13 ? 98 ILE B CA 1 ATOM 3852 C C . ILE B 1 98 ? 43.855 15.916 61.862 1.00 12.53 ? 98 ILE B C 1 ATOM 3853 O O . ILE B 1 98 ? 44.960 16.032 61.350 1.00 13.40 ? 98 ILE B O 1 ATOM 3854 C CB . ILE B 1 98 ? 43.997 14.108 63.596 1.00 12.63 ? 98 ILE B CB 1 ATOM 3855 C CG1 . ILE B 1 98 ? 43.560 12.687 63.949 1.00 12.07 ? 98 ILE B CG1 1 ATOM 3856 C CG2 . ILE B 1 98 ? 43.604 15.081 64.736 1.00 13.75 ? 98 ILE B CG2 1 ATOM 3857 C CD1 . ILE B 1 98 ? 44.097 12.160 65.261 1.00 13.03 ? 98 ILE B CD1 1 ATOM 3858 N N . LEU B 1 99 ? 43.026 16.932 62.124 1.00 13.56 ? 99 LEU B N 1 ATOM 3859 C CA . LEU B 1 99 ? 43.320 18.327 61.794 1.00 15.61 ? 99 LEU B CA 1 ATOM 3860 C C . LEU B 1 99 ? 43.530 19.153 63.059 1.00 17.50 ? 99 LEU B C 1 ATOM 3861 O O . LEU B 1 99 ? 43.078 18.783 64.146 1.00 17.49 ? 99 LEU B O 1 ATOM 3862 C CB . LEU B 1 99 ? 42.156 18.929 61.008 1.00 15.62 ? 99 LEU B CB 1 ATOM 3863 C CG . LEU B 1 99 ? 41.942 18.311 59.611 1.00 14.44 ? 99 LEU B CG 1 ATOM 3864 C CD1 . LEU B 1 99 ? 40.731 18.930 58.987 1.00 16.71 ? 99 LEU B CD1 1 ATOM 3865 C CD2 . LEU B 1 99 ? 43.151 18.561 58.740 1.00 15.80 ? 99 LEU B CD2 1 ATOM 3866 N N . PRO B 1 100 ? 44.166 20.299 62.894 1.00 18.59 ? 100 PRO B N 1 ATOM 3867 C CA . PRO B 1 100 ? 44.374 21.206 64.035 1.00 19.10 ? 100 PRO B CA 1 ATOM 3868 C C . PRO B 1 100 ? 43.128 21.744 64.735 1.00 20.04 ? 100 PRO B C 1 ATOM 3869 O O . PRO B 1 100 ? 43.267 22.154 65.908 1.00 21.93 ? 100 PRO B O 1 ATOM 3870 C CB . PRO B 1 100 ? 45.142 22.384 63.427 1.00 19.95 ? 100 PRO B CB 1 ATOM 3871 C CG . PRO B 1 100 ? 45.473 22.041 62.094 1.00 19.60 ? 100 PRO B CG 1 ATOM 3872 C CD . PRO B 1 100 ? 44.792 20.798 61.659 1.00 19.10 ? 100 PRO B CD 1 ATOM 3873 N N . ASP B 1 101 ? 41.957 21.789 64.083 1.00 20.00 ? 101 ASP B N 1 ATOM 3874 C CA . ASP B 1 101 ? 40.673 22.171 64.710 1.00 19.57 ? 101 ASP B CA 1 ATOM 3875 C C . ASP B 1 101 ? 40.035 21.085 65.568 1.00 18.46 ? 101 ASP B C 1 ATOM 3876 O O . ASP B 1 101 ? 38.930 21.284 66.094 1.00 19.00 ? 101 ASP B O 1 ATOM 3877 C CB . ASP B 1 101 ? 39.650 22.696 63.664 1.00 19.77 ? 101 ASP B CB 1 ATOM 3878 C CG . ASP B 1 101 ? 39.124 21.622 62.698 1.00 21.00 ? 101 ASP B CG 1 ATOM 3879 O OD1 . ASP B 1 101 ? 39.528 20.442 62.789 1.00 19.09 ? 101 ASP B OD1 1 ATOM 3880 O OD2 . ASP B 1 101 ? 38.274 21.894 61.790 1.00 21.36 ? 101 ASP B OD2 1 ATOM 3881 N N . GLY B 1 102 ? 40.700 19.926 65.643 1.00 17.22 ? 102 GLY B N 1 ATOM 3882 C CA . GLY B 1 102 ? 40.268 18.850 66.496 1.00 16.62 ? 102 GLY B CA 1 ATOM 3883 C C . GLY B 1 102 ? 39.437 17.817 65.774 1.00 16.02 ? 102 GLY B C 1 ATOM 3884 O O . GLY B 1 102 ? 39.108 16.774 66.330 1.00 17.17 ? 102 GLY B O 1 ATOM 3885 N N . ARG B 1 103 ? 39.077 18.096 64.521 1.00 15.74 ? 103 ARG B N 1 ATOM 3886 C CA . ARG B 1 103 ? 38.282 17.141 63.782 1.00 14.94 ? 103 ARG B CA 1 ATOM 3887 C C . ARG B 1 103 ? 39.170 15.996 63.298 1.00 13.47 ? 103 ARG B C 1 ATOM 3888 O O . ARG B 1 103 ? 40.392 16.142 63.155 1.00 12.70 ? 103 ARG B O 1 ATOM 3889 C CB . ARG B 1 103 ? 37.544 17.826 62.625 1.00 15.13 ? 103 ARG B CB 1 ATOM 3890 C CG . ARG B 1 103 ? 36.319 18.658 63.118 1.00 16.56 ? 103 ARG B CG 1 ATOM 3891 C CD . ARG B 1 103 ? 35.684 19.568 62.080 1.00 17.73 ? 103 ARG B CD 1 ATOM 3892 N NE . ARG B 1 103 ? 35.540 18.900 60.781 1.00 19.51 ? 103 ARG B NE 1 ATOM 3893 C CZ . ARG B 1 103 ? 36.285 19.134 59.701 1.00 19.20 ? 103 ARG B CZ 1 ATOM 3894 N NH1 . ARG B 1 103 ? 37.274 20.008 59.717 1.00 19.76 ? 103 ARG B NH1 1 ATOM 3895 N NH2 . ARG B 1 103 ? 36.024 18.461 58.587 1.00 19.25 ? 103 ARG B NH2 1 ATOM 3896 N N . VAL B 1 104 ? 38.519 14.861 63.125 1.00 12.54 ? 104 VAL B N 1 ATOM 3897 C CA . VAL B 1 104 ? 39.150 13.653 62.619 1.00 11.71 ? 104 VAL B CA 1 ATOM 3898 C C . VAL B 1 104 ? 38.433 13.340 61.308 1.00 11.00 ? 104 VAL B C 1 ATOM 3899 O O . VAL B 1 104 ? 37.523 12.513 61.262 1.00 11.79 ? 104 VAL B O 1 ATOM 3900 C CB . VAL B 1 104 ? 39.002 12.484 63.636 1.00 11.82 ? 104 VAL B CB 1 ATOM 3901 C CG1 . VAL B 1 104 ? 39.693 11.256 63.155 1.00 11.63 ? 104 VAL B CG1 1 ATOM 3902 C CG2 . VAL B 1 104 ? 39.528 12.891 65.014 1.00 13.60 ? 104 VAL B CG2 1 ATOM 3903 N N . PRO B 1 105 ? 38.777 14.057 60.239 1.00 10.35 ? 105 PRO B N 1 ATOM 3904 C CA . PRO B 1 105 ? 38.060 13.860 59.001 1.00 10.47 ? 105 PRO B CA 1 ATOM 3905 C C . PRO B 1 105 ? 38.210 12.459 58.388 1.00 9.68 ? 105 PRO B C 1 ATOM 3906 O O . PRO B 1 105 ? 37.331 12.022 57.664 1.00 10.63 ? 105 PRO B O 1 ATOM 3907 C CB . PRO B 1 105 ? 38.639 14.912 58.060 1.00 10.84 ? 105 PRO B CB 1 ATOM 3908 C CG . PRO B 1 105 ? 39.941 15.228 58.612 1.00 10.69 ? 105 PRO B CG 1 ATOM 3909 C CD . PRO B 1 105 ? 39.776 15.128 60.104 1.00 10.70 ? 105 PRO B CD 1 ATOM 3910 N N . SER B 1 106 ? 39.319 11.773 58.654 1.00 9.35 ? 106 SER B N 1 ATOM 3911 C CA . SER B 1 106 ? 39.488 10.408 58.166 1.00 8.97 ? 106 SER B CA 1 ATOM 3912 C C . SER B 1 106 ? 39.059 10.296 56.704 1.00 8.51 ? 106 SER B C 1 ATOM 3913 O O . SER B 1 106 ? 38.213 9.488 56.377 1.00 8.81 ? 106 SER B O 1 ATOM 3914 C CB . SER B 1 106 ? 38.717 9.433 59.068 1.00 8.88 ? 106 SER B CB 1 ATOM 3915 O OG . SER B 1 106 ? 39.051 8.077 58.826 1.00 8.81 ? 106 SER B OG 1 ATOM 3916 N N . PRO B 1 107 ? 39.650 11.102 55.822 1.00 7.98 ? 107 PRO B N 1 ATOM 3917 C CA . PRO B 1 107 ? 39.106 11.186 54.473 1.00 8.14 ? 107 PRO B CA 1 ATOM 3918 C C . PRO B 1 107 ? 39.186 9.926 53.621 1.00 8.44 ? 107 PRO B C 1 ATOM 3919 O O . PRO B 1 107 ? 40.189 9.216 53.671 1.00 8.60 ? 107 PRO B O 1 ATOM 3920 C CB . PRO B 1 107 ? 39.914 12.336 53.843 1.00 8.82 ? 107 PRO B CB 1 ATOM 3921 C CG . PRO B 1 107 ? 41.212 12.325 54.588 1.00 8.02 ? 107 PRO B CG 1 ATOM 3922 C CD . PRO B 1 107 ? 40.757 12.062 56.011 1.00 8.90 ? 107 PRO B CD 1 ATOM 3923 N N . ARG B 1 108 ? 38.142 9.720 52.802 1.00 8.22 ? 108 ARG B N 1 ATOM 3924 C CA . ARG B 1 108 ? 38.110 8.750 51.726 1.00 8.11 ? 108 ARG B CA 1 ATOM 3925 C C . ARG B 1 108 ? 37.766 9.485 50.442 1.00 8.19 ? 108 ARG B C 1 ATOM 3926 O O . ARG B 1 108 ? 36.726 10.161 50.353 1.00 8.33 ? 108 ARG B O 1 ATOM 3927 C CB . ARG B 1 108 ? 37.106 7.639 51.993 1.00 8.43 ? 108 ARG B CB 1 ATOM 3928 C CG . ARG B 1 108 ? 37.036 6.636 50.868 1.00 8.64 ? 108 ARG B CG 1 ATOM 3929 C CD . ARG B 1 108 ? 36.210 5.433 51.153 1.00 8.87 ? 108 ARG B CD 1 ATOM 3930 N NE . ARG B 1 108 ? 34.768 5.698 51.059 1.00 9.00 ? 108 ARG B NE 1 ATOM 3931 C CZ . ARG B 1 108 ? 33.923 5.806 52.083 1.00 9.01 ? 108 ARG B CZ 1 ATOM 3932 N NH1 . ARG B 1 108 ? 34.308 5.632 53.338 1.00 10.01 ? 108 ARG B NH1 1 ATOM 3933 N NH2 . ARG B 1 108 ? 32.670 6.098 51.843 1.00 10.23 ? 108 ARG B NH2 1 ATOM 3934 N N . VAL B 1 109 ? 38.636 9.317 49.443 1.00 8.02 ? 109 VAL B N 1 ATOM 3935 C CA . VAL B 1 109 ? 38.488 9.981 48.170 1.00 8.33 ? 109 VAL B CA 1 ATOM 3936 C C . VAL B 1 109 ? 38.547 9.006 46.998 1.00 8.49 ? 109 VAL B C 1 ATOM 3937 O O . VAL B 1 109 ? 39.099 7.915 47.114 1.00 8.09 ? 109 VAL B O 1 ATOM 3938 C CB . VAL B 1 109 ? 39.575 11.067 47.978 1.00 8.81 ? 109 VAL B CB 1 ATOM 3939 C CG1 . VAL B 1 109 ? 39.506 12.132 49.064 1.00 8.64 ? 109 VAL B CG1 1 ATOM 3940 C CG2 . VAL B 1 109 ? 40.976 10.466 47.906 1.00 9.99 ? 109 VAL B CG2 1 ATOM 3941 N N . TYR B 1 110 ? 38.010 9.442 45.859 1.00 8.32 ? 110 TYR B N 1 ATOM 3942 C CA . TYR B 1 110 ? 38.086 8.690 44.611 1.00 8.65 ? 110 TYR B CA 1 ATOM 3943 C C . TYR B 1 110 ? 38.787 9.507 43.534 1.00 8.98 ? 110 TYR B C 1 ATOM 3944 O O . TYR B 1 110 ? 38.759 10.731 43.555 1.00 9.07 ? 110 TYR B O 1 ATOM 3945 C CB . TYR B 1 110 ? 36.672 8.257 44.116 1.00 8.02 ? 110 TYR B CB 1 ATOM 3946 C CG . TYR B 1 110 ? 35.799 7.811 45.257 1.00 8.13 ? 110 TYR B CG 1 ATOM 3947 C CD1 . TYR B 1 110 ? 36.199 6.764 46.067 1.00 8.75 ? 110 TYR B CD1 1 ATOM 3948 C CD2 . TYR B 1 110 ? 34.596 8.431 45.549 1.00 8.31 ? 110 TYR B CD2 1 ATOM 3949 C CE1 . TYR B 1 110 ? 35.484 6.416 47.180 1.00 9.12 ? 110 TYR B CE1 1 ATOM 3950 C CE2 . TYR B 1 110 ? 33.861 8.059 46.657 1.00 8.90 ? 110 TYR B CE2 1 ATOM 3951 C CZ . TYR B 1 110 ? 34.327 7.049 47.479 1.00 8.74 ? 110 TYR B CZ 1 ATOM 3952 O OH . TYR B 1 110 ? 33.646 6.689 48.628 1.00 9.05 ? 110 TYR B OH 1 ATOM 3953 N N . LEU B 1 111 ? 39.353 8.815 42.545 1.00 9.04 ? 111 LEU B N 1 ATOM 3954 C CA . LEU B 1 111 ? 40.000 9.463 41.398 1.00 8.79 ? 111 LEU B CA 1 ATOM 3955 C C . LEU B 1 111 ? 39.016 9.691 40.248 1.00 8.65 ? 111 LEU B C 1 ATOM 3956 O O . LEU B 1 111 ? 38.449 8.739 39.716 1.00 9.39 ? 111 LEU B O 1 ATOM 3957 C CB . LEU B 1 111 ? 41.181 8.627 40.949 1.00 9.12 ? 111 LEU B CB 1 ATOM 3958 C CG . LEU B 1 111 ? 42.174 9.356 40.042 1.00 9.12 ? 111 LEU B CG 1 ATOM 3959 C CD1 . LEU B 1 111 ? 42.974 10.358 40.827 1.00 10.38 ? 111 LEU B CD1 1 ATOM 3960 C CD2 . LEU B 1 111 ? 43.093 8.381 39.335 1.00 10.09 ? 111 LEU B CD2 1 ATOM 3961 N N . LEU B 1 112 ? 38.803 10.964 39.914 1.00 9.26 ? 112 LEU B N 1 ATOM 3962 C CA . LEU B 1 112 ? 37.970 11.359 38.794 1.00 9.44 ? 112 LEU B CA 1 ATOM 3963 C C . LEU B 1 112 ? 38.801 11.535 37.548 1.00 9.80 ? 112 LEU B C 1 ATOM 3964 O O . LEU B 1 112 ? 39.964 11.900 37.628 1.00 10.17 ? 112 LEU B O 1 ATOM 3965 C CB . LEU B 1 112 ? 37.341 12.725 39.081 1.00 10.08 ? 112 LEU B CB 1 ATOM 3966 C CG . LEU B 1 112 ? 36.213 12.759 40.116 1.00 9.44 ? 112 LEU B CG 1 ATOM 3967 C CD1 . LEU B 1 112 ? 35.867 14.156 40.495 1.00 9.65 ? 112 LEU B CD1 1 ATOM 3968 C CD2 . LEU B 1 112 ? 34.995 12.030 39.585 1.00 10.63 ? 112 LEU B CD2 1 ATOM 3969 N N . ASP B 1 113 ? 38.151 11.331 36.404 1.00 10.67 ? 113 ASP B N 1 ATOM 3970 C CA . ASP B 1 113 ? 38.783 11.619 35.125 1.00 11.28 ? 113 ASP B CA 1 ATOM 3971 C C . ASP B 1 113 ? 38.867 13.123 34.899 1.00 11.47 ? 113 ASP B C 1 ATOM 3972 O O . ASP B 1 113 ? 38.412 13.940 35.736 1.00 10.73 ? 113 ASP B O 1 ATOM 3973 C CB . ASP B 1 113 ? 38.141 10.794 33.985 1.00 11.62 ? 113 ASP B CB 1 ATOM 3974 C CG . ASP B 1 113 ? 36.901 11.381 33.396 1.00 11.89 ? 113 ASP B CG 1 ATOM 3975 O OD1 . ASP B 1 113 ? 36.485 12.514 33.740 1.00 11.91 ? 113 ASP B OD1 1 ATOM 3976 O OD2 . ASP B 1 113 ? 36.288 10.709 32.518 1.00 13.59 ? 113 ASP B OD2 1 ATOM 3977 N N . LYS B 1 114 ? 39.469 13.514 33.772 1.00 13.22 ? 114 LYS B N 1 ATOM 3978 C CA . LYS B 1 114 ? 39.709 14.910 33.496 1.00 14.42 ? 114 LYS B CA 1 ATOM 3979 C C . LYS B 1 114 ? 38.443 15.788 33.378 1.00 14.08 ? 114 LYS B C 1 ATOM 3980 O O . LYS B 1 114 ? 38.516 17.010 33.495 1.00 15.76 ? 114 LYS B O 1 ATOM 3981 C CB . LYS B 1 114 ? 40.612 15.056 32.260 1.00 16.09 ? 114 LYS B CB 1 ATOM 3982 C CG . LYS B 1 114 ? 39.999 14.530 30.975 1.00 19.19 ? 114 LYS B CG 1 ATOM 3983 C CD . LYS B 1 114 ? 41.014 14.471 29.836 1.00 20.23 ? 114 LYS B CD 1 ATOM 3984 C CE . LYS B 1 114 ? 40.325 14.380 28.495 1.00 23.43 ? 114 LYS B CE 1 ATOM 3985 N NZ . LYS B 1 114 ? 41.278 14.703 27.395 1.00 25.78 ? 114 LYS B NZ 1 ATOM 3986 N N . THR B 1 115 ? 37.285 15.174 33.156 1.00 12.62 ? 115 THR B N 1 ATOM 3987 C CA . THR B 1 115 ? 36.028 15.911 33.032 1.00 12.91 ? 115 THR B CA 1 ATOM 3988 C C . THR B 1 115 ? 35.374 16.228 34.362 1.00 12.74 ? 115 THR B C 1 ATOM 3989 O O . THR B 1 115 ? 34.400 16.976 34.411 1.00 13.25 ? 115 THR B O 1 ATOM 3990 C CB . THR B 1 115 ? 34.992 15.146 32.215 1.00 12.25 ? 115 THR B CB 1 ATOM 3991 O OG1 . THR B 1 115 ? 34.476 14.045 32.987 1.00 12.32 ? 115 THR B OG1 1 ATOM 3992 C CG2 . THR B 1 115 ? 35.561 14.565 30.899 1.00 12.07 ? 115 THR B CG2 1 ATOM 3993 N N . LYS B 1 116 ? 35.852 15.590 35.426 1.00 11.91 ? 116 LYS B N 1 ATOM 3994 C CA . LYS B 1 116 ? 35.249 15.659 36.774 1.00 12.47 ? 116 LYS B CA 1 ATOM 3995 C C . LYS B 1 116 ? 33.899 14.974 36.906 1.00 12.41 ? 116 LYS B C 1 ATOM 3996 O O . LYS B 1 116 ? 33.323 14.983 37.985 1.00 12.81 ? 116 LYS B O 1 ATOM 3997 C CB . LYS B 1 116 ? 35.153 17.106 37.273 1.00 12.48 ? 116 LYS B CB 1 ATOM 3998 C CG . LYS B 1 116 ? 36.473 17.854 37.350 1.00 13.27 ? 116 LYS B CG 1 ATOM 3999 C CD . LYS B 1 116 ? 36.226 19.295 37.758 1.00 14.26 ? 116 LYS B CD 1 ATOM 4000 C CE . LYS B 1 116 ? 37.534 20.041 37.923 1.00 15.79 ? 116 LYS B CE 1 ATOM 4001 N NZ . LYS B 1 116 ? 37.277 21.471 38.277 1.00 17.94 ? 116 LYS B NZ 1 ATOM 4002 N N . ARG B 1 117 ? 33.369 14.386 35.837 1.00 12.15 ? 117 ARG B N 1 ATOM 4003 C CA . ARG B 1 117 ? 32.015 13.835 35.890 1.00 12.85 ? 117 ARG B CA 1 ATOM 4004 C C . ARG B 1 117 ? 31.942 12.320 35.749 1.00 12.01 ? 117 ARG B C 1 ATOM 4005 O O . ARG B 1 117 ? 30.853 11.726 35.736 1.00 12.51 ? 117 ARG B O 1 ATOM 4006 C CB . ARG B 1 117 ? 31.129 14.490 34.843 1.00 15.11 ? 117 ARG B CB 1 ATOM 4007 C CG . ARG B 1 117 ? 30.713 15.890 35.260 1.00 18.99 ? 117 ARG B CG 1 ATOM 4008 C CD . ARG B 1 117 ? 31.123 16.922 34.334 1.00 25.90 ? 117 ARG B CD 1 ATOM 4009 N NE . ARG B 1 117 ? 30.534 18.213 34.683 1.00 27.26 ? 117 ARG B NE 1 ATOM 4010 C CZ . ARG B 1 117 ? 31.225 19.322 34.922 1.00 29.37 ? 117 ARG B CZ 1 ATOM 4011 N NH1 . ARG B 1 117 ? 32.554 19.338 34.846 1.00 29.24 ? 117 ARG B NH1 1 ATOM 4012 N NH2 . ARG B 1 117 ? 30.577 20.437 35.239 1.00 30.22 ? 117 ARG B NH2 1 ATOM 4013 N N . ARG B 1 118 ? 33.103 11.683 35.663 1.00 11.47 ? 118 ARG B N 1 ATOM 4014 C CA . ARG B 1 118 ? 33.200 10.237 35.594 1.00 11.81 ? 118 ARG B CA 1 ATOM 4015 C C . ARG B 1 118 ? 34.420 9.838 36.368 1.00 10.96 ? 118 ARG B C 1 ATOM 4016 O O . ARG B 1 118 ? 35.420 10.545 36.331 1.00 11.79 ? 118 ARG B O 1 ATOM 4017 C CB A ARG B 1 118 ? 33.353 9.826 34.120 0.50 12.69 ? 118 ARG B CB 1 ATOM 4018 C CB B ARG B 1 118 ? 33.399 9.740 34.178 0.50 12.09 ? 118 ARG B CB 1 ATOM 4019 C CG A ARG B 1 118 ? 33.001 8.379 33.764 0.50 13.09 ? 118 ARG B CG 1 ATOM 4020 C CG B ARG B 1 118 ? 32.457 10.297 33.167 0.50 12.36 ? 118 ARG B CG 1 ATOM 4021 C CD A ARG B 1 118 ? 32.930 8.093 32.253 0.50 15.11 ? 118 ARG B CD 1 ATOM 4022 C CD B ARG B 1 118 ? 32.752 9.782 31.769 0.50 13.29 ? 118 ARG B CD 1 ATOM 4023 N NE A ARG B 1 118 ? 32.376 6.758 31.979 0.50 15.66 ? 118 ARG B NE 1 ATOM 4024 N NE B ARG B 1 118 ? 32.382 8.385 31.710 0.50 14.98 ? 118 ARG B NE 1 ATOM 4025 C CZ A ARG B 1 118 ? 33.110 5.668 31.795 0.50 16.28 ? 118 ARG B CZ 1 ATOM 4026 C CZ B ARG B 1 118 ? 31.175 7.921 31.414 0.50 13.88 ? 118 ARG B CZ 1 ATOM 4027 N NH1 A ARG B 1 118 ? 34.421 5.735 31.859 0.50 18.57 ? 118 ARG B NH1 1 ATOM 4028 N NH1 B ARG B 1 118 ? 30.188 8.746 31.092 0.50 12.80 ? 118 ARG B NH1 1 ATOM 4029 N NH2 A ARG B 1 118 ? 32.532 4.500 31.562 0.50 17.54 ? 118 ARG B NH2 1 ATOM 4030 N NH2 B ARG B 1 118 ? 30.976 6.614 31.436 0.50 14.36 ? 118 ARG B NH2 1 ATOM 4031 N N . TYR B 1 119 ? 34.336 8.718 37.080 1.00 10.22 ? 119 TYR B N 1 ATOM 4032 C CA . TYR B 1 119 ? 35.530 8.156 37.699 1.00 9.77 ? 119 TYR B CA 1 ATOM 4033 C C . TYR B 1 119 ? 36.514 7.710 36.625 1.00 9.75 ? 119 TYR B C 1 ATOM 4034 O O . TYR B 1 119 ? 36.121 7.276 35.544 1.00 10.89 ? 119 TYR B O 1 ATOM 4035 C CB . TYR B 1 119 ? 35.140 6.991 38.634 1.00 9.07 ? 119 TYR B CB 1 ATOM 4036 C CG . TYR B 1 119 ? 34.300 7.461 39.781 1.00 8.83 ? 119 TYR B CG 1 ATOM 4037 C CD1 . TYR B 1 119 ? 34.761 8.403 40.663 1.00 9.26 ? 119 TYR B CD1 1 ATOM 4038 C CD2 . TYR B 1 119 ? 33.032 6.944 39.997 1.00 8.88 ? 119 TYR B CD2 1 ATOM 4039 C CE1 . TYR B 1 119 ? 33.974 8.842 41.727 1.00 7.83 ? 119 TYR B CE1 1 ATOM 4040 C CE2 . TYR B 1 119 ? 32.236 7.392 41.038 1.00 8.77 ? 119 TYR B CE2 1 ATOM 4041 C CZ . TYR B 1 119 ? 32.716 8.332 41.907 1.00 7.64 ? 119 TYR B CZ 1 ATOM 4042 O OH . TYR B 1 119 ? 31.932 8.800 42.949 1.00 9.13 ? 119 TYR B OH 1 ATOM 4043 N N . GLU B 1 120 ? 37.796 7.817 36.936 1.00 9.65 ? 120 GLU B N 1 ATOM 4044 C CA . GLU B 1 120 ? 38.822 7.210 36.100 1.00 10.32 ? 120 GLU B CA 1 ATOM 4045 C C . GLU B 1 120 ? 38.708 5.704 36.245 1.00 10.87 ? 120 GLU B C 1 ATOM 4046 O O . GLU B 1 120 ? 38.891 5.159 37.314 1.00 13.04 ? 120 GLU B O 1 ATOM 4047 C CB . GLU B 1 120 ? 40.194 7.707 36.543 1.00 10.62 ? 120 GLU B CB 1 ATOM 4048 C CG . GLU B 1 120 ? 41.358 7.173 35.733 1.00 11.87 ? 120 GLU B CG 1 ATOM 4049 C CD . GLU B 1 120 ? 41.386 7.738 34.341 1.00 13.73 ? 120 GLU B CD 1 ATOM 4050 O OE1 . GLU B 1 120 ? 41.225 8.975 34.159 1.00 13.88 ? 120 GLU B OE1 1 ATOM 4051 O OE2 . GLU B 1 120 ? 41.637 6.935 33.411 1.00 19.59 ? 120 GLU B OE2 1 ATOM 4052 N N . MET B 1 121 ? 38.348 5.000 35.182 1.00 10.43 ? 121 MET B N 1 ATOM 4053 C CA . MET B 1 121 ? 38.163 3.572 35.263 1.00 10.71 ? 121 MET B CA 1 ATOM 4054 C C . MET B 1 121 ? 39.477 2.866 34.945 1.00 10.30 ? 121 MET B C 1 ATOM 4055 O O . MET B 1 121 ? 40.046 3.067 33.872 1.00 11.65 ? 121 MET B O 1 ATOM 4056 C CB . MET B 1 121 ? 37.042 3.103 34.325 1.00 10.74 ? 121 MET B CB 1 ATOM 4057 C CG . MET B 1 121 ? 35.722 3.789 34.582 1.00 11.26 ? 121 MET B CG 1 ATOM 4058 S SD . MET B 1 121 ? 35.113 3.742 36.308 1.00 12.03 ? 121 MET B SD 1 ATOM 4059 C CE . MET B 1 121 ? 34.877 1.993 36.592 1.00 10.71 ? 121 MET B CE 1 ATOM 4060 N N . LEU B 1 122 ? 39.957 2.067 35.897 1.00 9.93 ? 122 LEU B N 1 ATOM 4061 C CA . LEU B 1 122 ? 41.175 1.301 35.720 1.00 10.42 ? 122 LEU B CA 1 ATOM 4062 C C . LEU B 1 122 ? 40.802 -0.131 35.361 1.00 9.87 ? 122 LEU B C 1 ATOM 4063 O O . LEU B 1 122 ? 39.901 -0.704 35.949 1.00 10.57 ? 122 LEU B O 1 ATOM 4064 C CB . LEU B 1 122 ? 42.043 1.333 36.993 1.00 10.58 ? 122 LEU B CB 1 ATOM 4065 C CG . LEU B 1 122 ? 42.625 2.703 37.398 1.00 10.96 ? 122 LEU B CG 1 ATOM 4066 C CD1 . LEU B 1 122 ? 41.626 3.529 38.187 1.00 14.04 ? 122 LEU B CD1 1 ATOM 4067 C CD2 . LEU B 1 122 ? 43.913 2.524 38.174 1.00 11.85 ? 122 LEU B CD2 1 ATOM 4068 N N . HIS B 1 123 ? 41.543 -0.697 34.420 1.00 10.03 ? 123 HIS B N 1 ATOM 4069 C CA . HIS B 1 123 ? 41.319 -2.070 33.908 1.00 10.47 ? 123 HIS B CA 1 ATOM 4070 C C . HIS B 1 123 ? 42.635 -2.793 34.000 1.00 11.39 ? 123 HIS B C 1 ATOM 4071 O O . HIS B 1 123 ? 43.424 -2.768 33.070 1.00 12.73 ? 123 HIS B O 1 ATOM 4072 C CB . HIS B 1 123 ? 40.812 -2.053 32.469 1.00 11.71 ? 123 HIS B CB 1 ATOM 4073 C CG . HIS B 1 123 ? 39.575 -1.235 32.259 1.00 11.29 ? 123 HIS B CG 1 ATOM 4074 N ND1 . HIS B 1 123 ? 38.307 -1.786 32.204 1.00 13.70 ? 123 HIS B ND1 1 ATOM 4075 C CD2 . HIS B 1 123 ? 39.414 0.098 32.041 1.00 13.32 ? 123 HIS B CD2 1 ATOM 4076 C CE1 . HIS B 1 123 ? 37.423 -0.823 31.983 1.00 13.45 ? 123 HIS B CE1 1 ATOM 4077 N NE2 . HIS B 1 123 ? 38.069 0.323 31.867 1.00 13.94 ? 123 HIS B NE2 1 ATOM 4078 N N . LEU B 1 124 ? 42.879 -3.415 35.156 1.00 10.81 ? 124 LEU B N 1 ATOM 4079 C CA . LEU B 1 124 ? 44.225 -3.785 35.548 1.00 10.80 ? 124 LEU B CA 1 ATOM 4080 C C . LEU B 1 124 ? 44.639 -5.238 35.297 1.00 10.68 ? 124 LEU B C 1 ATOM 4081 O O . LEU B 1 124 ? 45.821 -5.535 35.402 1.00 10.44 ? 124 LEU B O 1 ATOM 4082 C CB . LEU B 1 124 ? 44.475 -3.394 37.022 1.00 10.87 ? 124 LEU B CB 1 ATOM 4083 C CG . LEU B 1 124 ? 44.565 -1.892 37.281 1.00 13.43 ? 124 LEU B CG 1 ATOM 4084 C CD1 . LEU B 1 124 ? 44.792 -1.659 38.740 1.00 15.27 ? 124 LEU B CD1 1 ATOM 4085 C CD2 . LEU B 1 124 ? 45.651 -1.204 36.482 1.00 13.75 ? 124 LEU B CD2 1 ATOM 4086 N N . THR B 1 125 ? 43.713 -6.133 34.961 1.00 10.50 ? 125 THR B N 1 ATOM 4087 C CA . THR B 1 125 ? 44.103 -7.525 34.625 1.00 10.85 ? 125 THR B CA 1 ATOM 4088 C C . THR B 1 125 ? 45.066 -7.530 33.460 1.00 11.22 ? 125 THR B C 1 ATOM 4089 O O . THR B 1 125 ? 44.733 -7.027 32.393 1.00 12.41 ? 125 THR B O 1 ATOM 4090 C CB . THR B 1 125 ? 42.867 -8.358 34.316 1.00 10.83 ? 125 THR B CB 1 ATOM 4091 O OG1 . THR B 1 125 ? 42.026 -8.362 35.467 1.00 13.13 ? 125 THR B OG1 1 ATOM 4092 C CG2 . THR B 1 125 ? 43.248 -9.816 34.078 1.00 11.47 ? 125 THR B CG2 1 ATOM 4093 N N . GLY B 1 126 ? 46.257 -8.097 33.675 1.00 11.35 ? 126 GLY B N 1 ATOM 4094 C CA . GLY B 1 126 ? 47.339 -8.103 32.671 1.00 10.82 ? 126 GLY B CA 1 ATOM 4095 C C . GLY B 1 126 ? 48.234 -6.886 32.675 1.00 11.28 ? 126 GLY B C 1 ATOM 4096 O O . GLY B 1 126 ? 49.077 -6.735 31.785 1.00 13.45 ? 126 GLY B O 1 ATOM 4097 N N . PHE B 1 127 ? 48.061 -6.018 33.670 1.00 10.60 ? 127 PHE B N 1 ATOM 4098 C CA . PHE B 1 127 ? 48.788 -4.750 33.803 1.00 10.81 ? 127 PHE B CA 1 ATOM 4099 C C . PHE B 1 127 ? 49.329 -4.595 35.225 1.00 10.86 ? 127 PHE B C 1 ATOM 4100 O O . PHE B 1 127 ? 49.206 -5.493 36.052 1.00 11.65 ? 127 PHE B O 1 ATOM 4101 C CB . PHE B 1 127 ? 47.864 -3.598 33.393 1.00 11.76 ? 127 PHE B CB 1 ATOM 4102 C CG . PHE B 1 127 ? 47.405 -3.699 31.968 1.00 12.07 ? 127 PHE B CG 1 ATOM 4103 C CD1 . PHE B 1 127 ? 48.234 -3.283 30.924 1.00 14.01 ? 127 PHE B CD1 1 ATOM 4104 C CD2 . PHE B 1 127 ? 46.180 -4.250 31.661 1.00 14.68 ? 127 PHE B CD2 1 ATOM 4105 C CE1 . PHE B 1 127 ? 47.816 -3.395 29.626 1.00 14.71 ? 127 PHE B CE1 1 ATOM 4106 C CE2 . PHE B 1 127 ? 45.770 -4.383 30.345 1.00 15.33 ? 127 PHE B CE2 1 ATOM 4107 C CZ . PHE B 1 127 ? 46.593 -3.963 29.338 1.00 16.29 ? 127 PHE B CZ 1 ATOM 4108 N N . GLU B 1 128 ? 49.974 -3.465 35.504 1.00 9.94 ? 128 GLU B N 1 ATOM 4109 C CA . GLU B 1 128 ? 50.497 -3.203 36.849 1.00 11.08 ? 128 GLU B CA 1 ATOM 4110 C C . GLU B 1 128 ? 50.168 -1.774 37.276 1.00 10.69 ? 128 GLU B C 1 ATOM 4111 O O . GLU B 1 128 ? 49.991 -0.878 36.440 1.00 10.74 ? 128 GLU B O 1 ATOM 4112 C CB . GLU B 1 128 ? 51.991 -3.482 36.935 1.00 13.03 ? 128 GLU B CB 1 ATOM 4113 C CG . GLU B 1 128 ? 52.875 -2.471 36.265 1.00 13.28 ? 128 GLU B CG 1 ATOM 4114 C CD . GLU B 1 128 ? 54.342 -2.887 36.159 1.00 12.32 ? 128 GLU B CD 1 ATOM 4115 O OE1 . GLU B 1 128 ? 54.626 -4.103 36.165 1.00 13.76 ? 128 GLU B OE1 1 ATOM 4116 O OE2 . GLU B 1 128 ? 55.215 -1.993 35.988 1.00 13.33 ? 128 GLU B OE2 1 ATOM 4117 N N . PHE B 1 129 ? 50.062 -1.607 38.584 1.00 10.68 ? 129 PHE B N 1 ATOM 4118 C CA . PHE B 1 129 ? 49.771 -0.343 39.216 1.00 10.66 ? 129 PHE B CA 1 ATOM 4119 C C . PHE B 1 129 ? 50.850 -0.111 40.248 1.00 10.18 ? 129 PHE B C 1 ATOM 4120 O O . PHE B 1 129 ? 51.147 -1.005 41.043 1.00 10.54 ? 129 PHE B O 1 ATOM 4121 C CB . PHE B 1 129 ? 48.404 -0.386 39.912 1.00 10.57 ? 129 PHE B CB 1 ATOM 4122 C CG . PHE B 1 129 ? 47.998 0.925 40.545 1.00 9.77 ? 129 PHE B CG 1 ATOM 4123 C CD1 . PHE B 1 129 ? 48.483 1.284 41.788 1.00 10.82 ? 129 PHE B CD1 1 ATOM 4124 C CD2 . PHE B 1 129 ? 47.143 1.799 39.896 1.00 9.32 ? 129 PHE B CD2 1 ATOM 4125 C CE1 . PHE B 1 129 ? 48.153 2.503 42.364 1.00 10.87 ? 129 PHE B CE1 1 ATOM 4126 C CE2 . PHE B 1 129 ? 46.805 3.012 40.471 1.00 10.75 ? 129 PHE B CE2 1 ATOM 4127 C CZ . PHE B 1 129 ? 47.295 3.351 41.709 1.00 10.23 ? 129 PHE B CZ 1 ATOM 4128 N N . THR B 1 130 ? 51.421 1.091 40.227 1.00 10.28 ? 130 THR B N 1 ATOM 4129 C CA . THR B 1 130 ? 52.525 1.476 41.079 1.00 10.44 ? 130 THR B CA 1 ATOM 4130 C C . THR B 1 130 ? 52.303 2.834 41.705 1.00 9.69 ? 130 THR B C 1 ATOM 4131 O O . THR B 1 130 ? 51.691 3.725 41.120 1.00 10.02 ? 130 THR B O 1 ATOM 4132 C CB . THR B 1 130 ? 53.795 1.436 40.230 1.00 11.14 ? 130 THR B CB 1 ATOM 4133 O OG1 . THR B 1 130 ? 54.030 0.063 39.886 1.00 12.00 ? 130 THR B OG1 1 ATOM 4134 C CG2 . THR B 1 130 ? 55.021 1.919 40.971 1.00 10.96 ? 130 THR B CG2 1 ATOM 4135 N N . PHE B 1 131 ? 52.847 3.023 42.906 1.00 9.90 ? 131 PHE B N 1 ATOM 4136 C CA . PHE B 1 131 ? 52.839 4.339 43.543 1.00 9.70 ? 131 PHE B CA 1 ATOM 4137 C C . PHE B 1 131 ? 54.001 4.455 44.502 1.00 10.05 ? 131 PHE B C 1 ATOM 4138 O O . PHE B 1 131 ? 54.564 3.455 44.935 1.00 9.89 ? 131 PHE B O 1 ATOM 4139 C CB . PHE B 1 131 ? 51.489 4.598 44.267 1.00 9.14 ? 131 PHE B CB 1 ATOM 4140 C CG . PHE B 1 131 ? 51.205 3.650 45.389 1.00 9.49 ? 131 PHE B CG 1 ATOM 4141 C CD1 . PHE B 1 131 ? 50.710 2.383 45.114 1.00 9.85 ? 131 PHE B CD1 1 ATOM 4142 C CD2 . PHE B 1 131 ? 51.423 4.018 46.709 1.00 10.13 ? 131 PHE B CD2 1 ATOM 4143 C CE1 . PHE B 1 131 ? 50.439 1.493 46.151 1.00 10.00 ? 131 PHE B CE1 1 ATOM 4144 C CE2 . PHE B 1 131 ? 51.150 3.137 47.736 1.00 9.32 ? 131 PHE B CE2 1 ATOM 4145 C CZ . PHE B 1 131 ? 50.663 1.868 47.449 1.00 9.49 ? 131 PHE B CZ 1 ATOM 4146 N N . ASP B 1 132 ? 54.343 5.690 44.830 1.00 10.27 ? 132 ASP B N 1 ATOM 4147 C CA . ASP B 1 132 ? 55.308 5.953 45.877 1.00 10.26 ? 132 ASP B CA 1 ATOM 4148 C C . ASP B 1 132 ? 54.560 6.386 47.123 1.00 10.29 ? 132 ASP B C 1 ATOM 4149 O O . ASP B 1 132 ? 53.478 6.986 47.038 1.00 10.08 ? 132 ASP B O 1 ATOM 4150 C CB . ASP B 1 132 ? 56.269 7.070 45.485 1.00 10.26 ? 132 ASP B CB 1 ATOM 4151 C CG . ASP B 1 132 ? 56.904 6.874 44.138 1.00 12.58 ? 132 ASP B CG 1 ATOM 4152 O OD1 . ASP B 1 132 ? 57.096 5.723 43.688 1.00 13.07 ? 132 ASP B OD1 1 ATOM 4153 O OD2 . ASP B 1 132 ? 57.260 7.885 43.484 1.00 14.81 ? 132 ASP B OD2 1 ATOM 4154 N N . VAL B 1 133 ? 55.133 6.086 48.291 1.00 10.22 ? 133 VAL B N 1 ATOM 4155 C CA . VAL B 1 133 ? 54.428 6.346 49.547 1.00 10.02 ? 133 VAL B CA 1 ATOM 4156 C C . VAL B 1 133 ? 55.384 6.785 50.639 1.00 10.85 ? 133 VAL B C 1 ATOM 4157 O O . VAL B 1 133 ? 56.506 6.314 50.703 1.00 10.95 ? 133 VAL B O 1 ATOM 4158 C CB . VAL B 1 133 ? 53.580 5.103 49.984 1.00 10.29 ? 133 VAL B CB 1 ATOM 4159 C CG1 . VAL B 1 133 ? 54.443 3.958 50.415 1.00 10.26 ? 133 VAL B CG1 1 ATOM 4160 C CG2 . VAL B 1 133 ? 52.627 5.460 51.081 1.00 11.35 ? 133 VAL B CG2 1 ATOM 4161 N N . ASP B 1 134 ? 54.900 7.661 51.521 1.00 10.78 ? 134 ASP B N 1 ATOM 4162 C CA . ASP B 1 134 ? 55.568 7.986 52.791 1.00 10.64 ? 134 ASP B CA 1 ATOM 4163 C C . ASP B 1 134 ? 54.615 7.525 53.882 1.00 10.52 ? 134 ASP B C 1 ATOM 4164 O O . ASP B 1 134 ? 53.525 8.113 54.054 1.00 10.78 ? 134 ASP B O 1 ATOM 4165 C CB . ASP B 1 134 ? 55.802 9.482 52.894 1.00 10.84 ? 134 ASP B CB 1 ATOM 4166 C CG . ASP B 1 134 ? 56.517 9.897 54.156 1.00 14.07 ? 134 ASP B CG 1 ATOM 4167 O OD1 . ASP B 1 134 ? 56.502 9.168 55.152 1.00 14.08 ? 134 ASP B OD1 1 ATOM 4168 O OD2 . ASP B 1 134 ? 57.146 10.982 54.198 1.00 20.99 ? 134 ASP B OD2 1 ATOM 4169 N N . ALA B 1 135 ? 55.015 6.464 54.570 1.00 10.66 ? 135 ALA B N 1 ATOM 4170 C CA . ALA B 1 135 ? 54.225 5.818 55.617 1.00 10.63 ? 135 ALA B CA 1 ATOM 4171 C C . ALA B 1 135 ? 54.749 6.122 57.014 1.00 10.80 ? 135 ALA B C 1 ATOM 4172 O O . ALA B 1 135 ? 54.281 5.544 57.984 1.00 9.66 ? 135 ALA B O 1 ATOM 4173 C CB . ALA B 1 135 ? 54.193 4.287 55.391 1.00 11.55 ? 135 ALA B CB 1 ATOM 4174 N N . THR B 1 136 ? 55.703 7.044 57.126 1.00 11.38 ? 136 THR B N 1 ATOM 4175 C CA . THR B 1 136 ? 56.381 7.282 58.415 1.00 11.64 ? 136 THR B CA 1 ATOM 4176 C C . THR B 1 136 ? 55.452 7.686 59.559 1.00 11.33 ? 136 THR B C 1 ATOM 4177 O O . THR B 1 136 ? 55.705 7.320 60.724 1.00 12.25 ? 136 THR B O 1 ATOM 4178 C CB . THR B 1 136 ? 57.465 8.356 58.286 1.00 12.22 ? 136 THR B CB 1 ATOM 4179 O OG1 . THR B 1 136 ? 56.921 9.598 57.820 1.00 14.38 ? 136 THR B OG1 1 ATOM 4180 C CG2 . THR B 1 136 ? 58.565 7.955 57.313 1.00 13.96 ? 136 THR B CG2 1 ATOM 4181 N N . LYS B 1 137 ? 54.400 8.437 59.241 1.00 10.99 ? 137 LYS B N 1 ATOM 4182 C CA . LYS B 1 137 ? 53.479 8.931 60.256 1.00 11.18 ? 137 LYS B CA 1 ATOM 4183 C C . LYS B 1 137 ? 52.238 8.059 60.424 1.00 10.39 ? 137 LYS B C 1 ATOM 4184 O O . LYS B 1 137 ? 51.184 8.546 60.817 1.00 10.49 ? 137 LYS B O 1 ATOM 4185 C CB . LYS B 1 137 ? 53.085 10.377 59.945 1.00 11.65 ? 137 LYS B CB 1 ATOM 4186 C CG . LYS B 1 137 ? 54.250 11.315 60.027 1.00 14.91 ? 137 LYS B CG 1 ATOM 4187 C CD . LYS B 1 137 ? 53.808 12.759 60.096 1.00 18.04 ? 137 LYS B CD 1 ATOM 4188 C CE . LYS B 1 137 ? 54.431 13.500 61.248 1.00 25.58 ? 137 LYS B CE 1 ATOM 4189 N NZ . LYS B 1 137 ? 55.374 14.457 60.716 1.00 29.76 ? 137 LYS B NZ 1 ATOM 4190 N N . LEU B 1 138 ? 52.398 6.749 60.187 1.00 9.98 ? 138 LEU B N 1 ATOM 4191 C CA . LEU B 1 138 ? 51.330 5.781 60.373 1.00 9.98 ? 138 LEU B CA 1 ATOM 4192 C C . LEU B 1 138 ? 51.773 4.732 61.412 1.00 9.69 ? 138 LEU B C 1 ATOM 4193 O O . LEU B 1 138 ? 52.408 3.732 61.057 1.00 9.80 ? 138 LEU B O 1 ATOM 4194 C CB . LEU B 1 138 ? 50.996 5.083 59.050 1.00 9.92 ? 138 LEU B CB 1 ATOM 4195 C CG . LEU B 1 138 ? 50.528 5.984 57.913 1.00 10.03 ? 138 LEU B CG 1 ATOM 4196 C CD1 . LEU B 1 138 ? 50.497 5.247 56.598 1.00 9.23 ? 138 LEU B CD1 1 ATOM 4197 C CD2 . LEU B 1 138 ? 49.140 6.571 58.215 1.00 10.32 ? 138 LEU B CD2 1 ATOM 4198 N N . PRO B 1 139 ? 51.453 4.939 62.683 1.00 9.58 ? 139 PRO B N 1 ATOM 4199 C CA . PRO B 1 139 ? 51.766 3.948 63.684 1.00 9.94 ? 139 PRO B CA 1 ATOM 4200 C C . PRO B 1 139 ? 50.769 2.775 63.705 1.00 10.61 ? 139 PRO B C 1 ATOM 4201 O O . PRO B 1 139 ? 49.763 2.760 62.980 1.00 10.19 ? 139 PRO B O 1 ATOM 4202 C CB . PRO B 1 139 ? 51.682 4.757 64.981 1.00 10.15 ? 139 PRO B CB 1 ATOM 4203 C CG . PRO B 1 139 ? 50.588 5.715 64.693 1.00 10.26 ? 139 PRO B CG 1 ATOM 4204 C CD . PRO B 1 139 ? 50.793 6.126 63.278 1.00 9.86 ? 139 PRO B CD 1 ATOM 4205 N N . CYS B 1 140 ? 51.037 1.819 64.590 1.00 10.32 ? 140 CYS B N 1 ATOM 4206 C CA . CYS B 1 140 ? 50.117 0.745 64.875 1.00 10.08 ? 140 CYS B CA 1 ATOM 4207 C C . CYS B 1 140 ? 48.688 1.248 64.930 1.00 10.06 ? 140 CYS B C 1 ATOM 4208 O O . CYS B 1 140 ? 48.409 2.285 65.541 1.00 9.74 ? 140 CYS B O 1 ATOM 4209 C CB . CYS B 1 140 ? 50.416 0.127 66.235 1.00 10.81 ? 140 CYS B CB 1 ATOM 4210 S SG . CYS B 1 140 ? 52.002 -0.738 66.374 1.00 12.53 ? 140 CYS B SG 1 ATOM 4211 N N . GLY B 1 141 ? 47.785 0.487 64.332 1.00 9.06 ? 141 GLY B N 1 ATOM 4212 C CA . GLY B 1 141 ? 46.363 0.794 64.370 1.00 9.70 ? 141 GLY B CA 1 ATOM 4213 C C . GLY B 1 141 ? 45.847 1.687 63.272 1.00 9.59 ? 141 GLY B C 1 ATOM 4214 O O . GLY B 1 141 ? 44.640 1.723 63.037 1.00 9.87 ? 141 GLY B O 1 ATOM 4215 N N . MET B 1 142 ? 46.728 2.400 62.589 1.00 9.67 ? 142 MET B N 1 ATOM 4216 C CA . MET B 1 142 ? 46.304 3.188 61.439 1.00 9.66 ? 142 MET B CA 1 ATOM 4217 C C . MET B 1 142 ? 46.238 2.333 60.177 1.00 9.31 ? 142 MET B C 1 ATOM 4218 O O . MET B 1 142 ? 47.059 1.433 59.978 1.00 9.66 ? 142 MET B O 1 ATOM 4219 C CB . MET B 1 142 ? 47.274 4.344 61.205 1.00 9.69 ? 142 MET B CB 1 ATOM 4220 C CG . MET B 1 142 ? 47.223 5.457 62.233 1.00 10.39 ? 142 MET B CG 1 ATOM 4221 S SD . MET B 1 142 ? 45.586 6.222 62.459 1.00 10.49 ? 142 MET B SD 1 ATOM 4222 C CE . MET B 1 142 ? 45.179 6.684 60.771 1.00 9.52 ? 142 MET B CE 1 ATOM 4223 N N . ASN B 1 143 ? 45.265 2.632 59.316 1.00 9.37 ? 143 ASN B N 1 ATOM 4224 C CA . ASN B 1 143 ? 45.142 1.999 58.011 1.00 8.98 ? 143 ASN B CA 1 ATOM 4225 C C . ASN B 1 143 ? 45.152 3.096 56.960 1.00 8.85 ? 143 ASN B C 1 ATOM 4226 O O . ASN B 1 143 ? 44.228 3.926 56.876 1.00 9.24 ? 143 ASN B O 1 ATOM 4227 C CB . ASN B 1 143 ? 43.880 1.144 57.945 1.00 9.16 ? 143 ASN B CB 1 ATOM 4228 C CG . ASN B 1 143 ? 43.766 0.330 56.663 1.00 9.70 ? 143 ASN B CG 1 ATOM 4229 O OD1 . ASN B 1 143 ? 44.254 0.733 55.613 1.00 10.42 ? 143 ASN B OD1 1 ATOM 4230 N ND2 . ASN B 1 143 ? 43.055 -0.783 56.736 1.00 10.12 ? 143 ASN B ND2 1 ATOM 4231 N N . SER B 1 144 ? 46.259 3.170 56.210 1.00 8.31 ? 144 SER B N 1 ATOM 4232 C CA . SER B 1 144 ? 46.255 3.914 54.968 1.00 8.52 ? 144 SER B CA 1 ATOM 4233 C C . SER B 1 144 ? 45.901 2.946 53.861 1.00 7.78 ? 144 SER B C 1 ATOM 4234 O O . SER B 1 144 ? 46.528 1.880 53.726 1.00 8.51 ? 144 SER B O 1 ATOM 4235 C CB . SER B 1 144 ? 47.576 4.671 54.701 1.00 8.52 ? 144 SER B CB 1 ATOM 4236 O OG . SER B 1 144 ? 48.665 3.808 54.342 1.00 8.75 ? 144 SER B OG 1 ATOM 4237 N N . ALA B 1 145 ? 44.873 3.289 53.081 1.00 8.40 ? 145 ALA B N 1 ATOM 4238 C CA . ALA B 1 145 ? 44.339 2.393 52.092 1.00 8.01 ? 145 ALA B CA 1 ATOM 4239 C C . ALA B 1 145 ? 44.385 3.002 50.695 1.00 7.62 ? 145 ALA B C 1 ATOM 4240 O O . ALA B 1 145 ? 44.217 4.226 50.524 1.00 8.67 ? 145 ALA B O 1 ATOM 4241 C CB . ALA B 1 145 ? 42.911 1.981 52.450 1.00 8.56 ? 145 ALA B CB 1 ATOM 4242 N N . LEU B 1 146 ? 44.631 2.146 49.709 1.00 7.84 ? 146 LEU B N 1 ATOM 4243 C CA . LEU B 1 146 ? 44.616 2.498 48.284 1.00 8.42 ? 146 LEU B CA 1 ATOM 4244 C C . LEU B 1 146 ? 44.066 1.237 47.614 1.00 8.89 ? 146 LEU B C 1 ATOM 4245 O O . LEU B 1 146 ? 44.663 0.169 47.712 1.00 8.49 ? 146 LEU B O 1 ATOM 4246 C CB . LEU B 1 146 ? 46.022 2.899 47.816 1.00 9.27 ? 146 LEU B CB 1 ATOM 4247 C CG . LEU B 1 146 ? 46.184 3.313 46.340 1.00 8.95 ? 146 LEU B CG 1 ATOM 4248 C CD1 . LEU B 1 146 ? 47.372 4.248 46.169 1.00 9.44 ? 146 LEU B CD1 1 ATOM 4249 C CD2 . LEU B 1 146 ? 46.309 2.133 45.406 1.00 9.72 ? 146 LEU B CD2 1 ATOM 4250 N N . TYR B 1 147 ? 42.860 1.341 47.048 1.00 8.96 ? 147 TYR B N 1 ATOM 4251 C CA . TYR B 1 147 ? 42.161 0.144 46.638 1.00 9.14 ? 147 TYR B CA 1 ATOM 4252 C C . TYR B 1 147 ? 41.172 0.430 45.540 1.00 9.00 ? 147 TYR B C 1 ATOM 4253 O O . TYR B 1 147 ? 40.939 1.577 45.195 1.00 9.40 ? 147 TYR B O 1 ATOM 4254 C CB . TYR B 1 147 ? 41.466 -0.515 47.836 1.00 9.05 ? 147 TYR B CB 1 ATOM 4255 C CG . TYR B 1 147 ? 40.384 0.280 48.522 1.00 8.36 ? 147 TYR B CG 1 ATOM 4256 C CD1 . TYR B 1 147 ? 40.692 1.329 49.367 1.00 9.13 ? 147 TYR B CD1 1 ATOM 4257 C CD2 . TYR B 1 147 ? 39.051 -0.027 48.339 1.00 7.59 ? 147 TYR B CD2 1 ATOM 4258 C CE1 . TYR B 1 147 ? 39.706 2.049 50.026 1.00 8.19 ? 147 TYR B CE1 1 ATOM 4259 C CE2 . TYR B 1 147 ? 38.061 0.667 48.997 1.00 8.27 ? 147 TYR B CE2 1 ATOM 4260 C CZ . TYR B 1 147 ? 38.394 1.691 49.860 1.00 8.18 ? 147 TYR B CZ 1 ATOM 4261 O OH . TYR B 1 147 ? 37.409 2.395 50.525 1.00 8.42 ? 147 TYR B OH 1 ATOM 4262 N N . LEU B 1 148 ? 40.626 -0.629 44.974 1.00 9.20 ? 148 LEU B N 1 ATOM 4263 C CA . LEU B 1 148 ? 39.670 -0.506 43.892 1.00 9.33 ? 148 LEU B CA 1 ATOM 4264 C C . LEU B 1 148 ? 38.333 -1.060 44.320 1.00 9.01 ? 148 LEU B C 1 ATOM 4265 O O . LEU B 1 148 ? 38.256 -2.110 44.950 1.00 8.84 ? 148 LEU B O 1 ATOM 4266 C CB . LEU B 1 148 ? 40.164 -1.329 42.701 1.00 9.96 ? 148 LEU B CB 1 ATOM 4267 C CG . LEU B 1 148 ? 41.553 -0.982 42.170 1.00 11.98 ? 148 LEU B CG 1 ATOM 4268 C CD1 . LEU B 1 148 ? 42.039 -2.026 41.193 1.00 13.80 ? 148 LEU B CD1 1 ATOM 4269 C CD2 . LEU B 1 148 ? 41.557 0.397 41.550 1.00 14.88 ? 148 LEU B CD2 1 ATOM 4270 N N . SER B 1 149 ? 37.254 -0.380 43.930 1.00 8.42 ? 149 SER B N 1 ATOM 4271 C CA . SER B 1 149 ? 35.889 -0.894 44.131 1.00 9.54 ? 149 SER B CA 1 ATOM 4272 C C . SER B 1 149 ? 35.162 -0.802 42.798 1.00 8.99 ? 149 SER B C 1 ATOM 4273 O O . SER B 1 149 ? 35.425 0.105 41.989 1.00 8.90 ? 149 SER B O 1 ATOM 4274 C CB . SER B 1 149 ? 35.104 -0.095 45.171 1.00 10.71 ? 149 SER B CB 1 ATOM 4275 O OG . SER B 1 149 ? 35.417 -0.586 46.471 1.00 12.17 ? 149 SER B OG 1 ATOM 4276 N N . GLU B 1 150 ? 34.259 -1.752 42.560 1.00 9.19 ? 150 GLU B N 1 ATOM 4277 C CA . GLU B 1 150 ? 33.512 -1.778 41.314 1.00 9.77 ? 150 GLU B CA 1 ATOM 4278 C C . GLU B 1 150 ? 32.294 -0.853 41.356 1.00 10.02 ? 150 GLU B C 1 ATOM 4279 O O . GLU B 1 150 ? 31.156 -1.292 41.268 1.00 10.96 ? 150 GLU B O 1 ATOM 4280 C CB . GLU B 1 150 ? 33.118 -3.203 40.895 1.00 10.00 ? 150 GLU B CB 1 ATOM 4281 C CG . GLU B 1 150 ? 32.889 -3.273 39.396 1.00 10.28 ? 150 GLU B CG 1 ATOM 4282 C CD . GLU B 1 150 ? 32.404 -4.582 38.850 1.00 10.19 ? 150 GLU B CD 1 ATOM 4283 O OE1 . GLU B 1 150 ? 32.326 -5.576 39.590 1.00 11.62 ? 150 GLU B OE1 1 ATOM 4284 O OE2 . GLU B 1 150 ? 32.081 -4.570 37.630 1.00 11.89 ? 150 GLU B OE2 1 ATOM 4285 N N . MET B 1 151 ? 32.577 0.441 41.480 1.00 9.62 ? 151 MET B N 1 ATOM 4286 C CA . MET B 1 151 ? 31.601 1.505 41.481 1.00 9.65 ? 151 MET B CA 1 ATOM 4287 C C . MET B 1 151 ? 31.221 1.852 40.039 1.00 9.13 ? 151 MET B C 1 ATOM 4288 O O . MET B 1 151 ? 31.967 1.605 39.095 1.00 10.05 ? 151 MET B O 1 ATOM 4289 C CB . MET B 1 151 ? 32.183 2.740 42.170 1.00 10.02 ? 151 MET B CB 1 ATOM 4290 C CG . MET B 1 151 ? 32.409 2.516 43.665 1.00 9.95 ? 151 MET B CG 1 ATOM 4291 S SD . MET B 1 151 ? 33.581 3.642 44.445 1.00 10.05 ? 151 MET B SD 1 ATOM 4292 C CE . MET B 1 151 ? 32.843 5.238 44.093 1.00 10.46 ? 151 MET B CE 1 ATOM 4293 N N . HIS B 1 152 ? 30.040 2.434 39.907 1.00 9.51 ? 152 HIS B N 1 ATOM 4294 C CA . HIS B 1 152 ? 29.519 2.848 38.611 1.00 9.33 ? 152 HIS B CA 1 ATOM 4295 C C . HIS B 1 152 ? 30.302 4.038 38.080 1.00 9.47 ? 152 HIS B C 1 ATOM 4296 O O . HIS B 1 152 ? 30.604 4.944 38.852 1.00 9.97 ? 152 HIS B O 1 ATOM 4297 C CB . HIS B 1 152 ? 28.059 3.255 38.789 1.00 9.62 ? 152 HIS B CB 1 ATOM 4298 C CG . HIS B 1 152 ? 27.348 3.544 37.508 1.00 9.95 ? 152 HIS B CG 1 ATOM 4299 N ND1 . HIS B 1 152 ? 27.473 4.740 36.840 1.00 10.34 ? 152 HIS B ND1 1 ATOM 4300 C CD2 . HIS B 1 152 ? 26.500 2.782 36.784 1.00 11.94 ? 152 HIS B CD2 1 ATOM 4301 C CE1 . HIS B 1 152 ? 26.735 4.692 35.746 1.00 11.71 ? 152 HIS B CE1 1 ATOM 4302 N NE2 . HIS B 1 152 ? 26.124 3.524 35.699 1.00 12.16 ? 152 HIS B NE2 1 ATOM 4303 N N . PRO B 1 153 ? 30.653 4.065 36.787 1.00 10.06 ? 153 PRO B N 1 ATOM 4304 C CA . PRO B 1 153 ? 31.552 5.102 36.286 1.00 10.58 ? 153 PRO B CA 1 ATOM 4305 C C . PRO B 1 153 ? 31.105 6.544 36.441 1.00 10.30 ? 153 PRO B C 1 ATOM 4306 O O . PRO B 1 153 ? 31.952 7.431 36.587 1.00 11.21 ? 153 PRO B O 1 ATOM 4307 C CB . PRO B 1 153 ? 31.757 4.746 34.810 1.00 11.34 ? 153 PRO B CB 1 ATOM 4308 C CG . PRO B 1 153 ? 31.440 3.312 34.755 1.00 12.49 ? 153 PRO B CG 1 ATOM 4309 C CD . PRO B 1 153 ? 30.332 3.078 35.747 1.00 10.26 ? 153 PRO B CD 1 ATOM 4310 N N . THR B 1 154 ? 29.805 6.801 36.424 1.00 10.49 ? 154 THR B N 1 ATOM 4311 C CA . THR B 1 154 ? 29.313 8.179 36.633 1.00 11.04 ? 154 THR B CA 1 ATOM 4312 C C . THR B 1 154 ? 28.786 8.368 38.049 1.00 11.42 ? 154 THR B C 1 ATOM 4313 O O . THR B 1 154 ? 28.111 9.341 38.317 1.00 12.50 ? 154 THR B O 1 ATOM 4314 C CB . THR B 1 154 ? 28.220 8.568 35.628 1.00 11.50 ? 154 THR B CB 1 ATOM 4315 O OG1 . THR B 1 154 ? 27.035 7.789 35.885 1.00 11.04 ? 154 THR B OG1 1 ATOM 4316 C CG2 . THR B 1 154 ? 28.650 8.308 34.196 1.00 13.00 ? 154 THR B CG2 1 ATOM 4317 N N . GLY B 1 155 ? 29.066 7.422 38.930 1.00 11.51 ? 155 GLY B N 1 ATOM 4318 C CA . GLY B 1 155 ? 28.489 7.425 40.269 1.00 11.79 ? 155 GLY B CA 1 ATOM 4319 C C . GLY B 1 155 ? 26.978 7.198 40.227 1.00 11.57 ? 155 GLY B C 1 ATOM 4320 O O . GLY B 1 155 ? 26.242 7.582 41.140 1.00 11.17 ? 155 GLY B O 1 ATOM 4321 N N . ALA B 1 156 ? 26.535 6.534 39.161 1.00 11.68 ? 156 ALA B N 1 ATOM 4322 C CA . ALA B 1 156 ? 25.116 6.264 38.889 1.00 11.38 ? 156 ALA B CA 1 ATOM 4323 C C . ALA B 1 156 ? 24.309 7.559 38.825 1.00 11.78 ? 156 ALA B C 1 ATOM 4324 O O . ALA B 1 156 ? 23.239 7.685 39.445 1.00 11.60 ? 156 ALA B O 1 ATOM 4325 C CB . ALA B 1 156 ? 24.549 5.289 39.900 1.00 11.98 ? 156 ALA B CB 1 ATOM 4326 N N . LYS B 1 157 ? 24.818 8.520 38.060 1.00 12.20 ? 157 LYS B N 1 ATOM 4327 C CA . LYS B 1 157 ? 24.090 9.763 37.816 1.00 12.93 ? 157 LYS B CA 1 ATOM 4328 C C . LYS B 1 157 ? 22.707 9.396 37.275 1.00 13.10 ? 157 LYS B C 1 ATOM 4329 O O . LYS B 1 157 ? 22.584 8.557 36.385 1.00 13.27 ? 157 LYS B O 1 ATOM 4330 C CB . LYS B 1 157 ? 24.865 10.661 36.828 1.00 13.10 ? 157 LYS B CB 1 ATOM 4331 C CG . LYS B 1 157 ? 24.222 12.006 36.601 1.00 14.01 ? 157 LYS B CG 1 ATOM 4332 C CD . LYS B 1 157 ? 25.041 12.953 35.734 1.00 15.86 ? 157 LYS B CD 1 ATOM 4333 C CE . LYS B 1 157 ? 24.304 14.274 35.569 1.00 18.88 ? 157 LYS B CE 1 ATOM 4334 N NZ . LYS B 1 157 ? 23.102 14.028 34.729 1.00 25.08 ? 157 LYS B NZ 1 ATOM 4335 N N . SER B 1 158 ? 21.673 10.039 37.805 1.00 13.01 ? 158 SER B N 1 ATOM 4336 C CA . SER B 1 158 ? 20.302 9.708 37.452 1.00 14.76 ? 158 SER B CA 1 ATOM 4337 C C . SER B 1 158 ? 19.396 10.880 37.808 1.00 15.28 ? 158 SER B C 1 ATOM 4338 O O . SER B 1 158 ? 19.834 11.870 38.354 1.00 14.56 ? 158 SER B O 1 ATOM 4339 C CB . SER B 1 158 ? 19.846 8.453 38.173 1.00 14.24 ? 158 SER B CB 1 ATOM 4340 O OG . SER B 1 158 ? 19.745 8.686 39.583 1.00 15.32 ? 158 SER B OG 1 ATOM 4341 N N . LYS B 1 159 ? 18.132 10.768 37.390 1.00 17.63 ? 159 LYS B N 1 ATOM 4342 C CA . LYS B 1 159 ? 17.070 11.722 37.693 1.00 18.77 ? 159 LYS B CA 1 ATOM 4343 C C . LYS B 1 159 ? 17.183 12.334 39.099 1.00 16.95 ? 159 LYS B C 1 ATOM 4344 O O . LYS B 1 159 ? 17.255 13.569 39.295 1.00 17.12 ? 159 LYS B O 1 ATOM 4345 C CB . LYS B 1 159 ? 15.752 10.915 37.550 1.00 21.73 ? 159 LYS B CB 1 ATOM 4346 C CG . LYS B 1 159 ? 14.484 11.553 37.981 1.00 22.79 ? 159 LYS B CG 1 ATOM 4347 C CD . LYS B 1 159 ? 13.274 10.761 37.467 1.00 23.78 ? 159 LYS B CD 1 ATOM 4348 C CE . LYS B 1 159 ? 11.958 11.491 37.710 1.00 27.15 ? 159 LYS B CE 1 ATOM 4349 N NZ . LYS B 1 159 ? 10.834 10.860 36.934 1.00 28.88 ? 159 LYS B NZ 1 ATOM 4350 N N . TYR B 1 160 ? 17.195 11.450 40.090 1.00 15.68 ? 160 TYR B N 1 ATOM 4351 C CA . TYR B 1 160 ? 17.215 11.881 41.486 1.00 15.05 ? 160 TYR B CA 1 ATOM 4352 C C . TYR B 1 160 ? 18.606 12.024 42.097 1.00 14.05 ? 160 TYR B C 1 ATOM 4353 O O . TYR B 1 160 ? 18.735 12.484 43.223 1.00 13.22 ? 160 TYR B O 1 ATOM 4354 C CB . TYR B 1 160 ? 16.345 10.967 42.338 1.00 16.39 ? 160 TYR B CB 1 ATOM 4355 C CG . TYR B 1 160 ? 14.867 11.004 41.952 1.00 18.13 ? 160 TYR B CG 1 ATOM 4356 C CD1 . TYR B 1 160 ? 14.178 12.205 41.879 1.00 18.82 ? 160 TYR B CD1 1 ATOM 4357 C CD2 . TYR B 1 160 ? 14.173 9.837 41.693 1.00 19.92 ? 160 TYR B CD2 1 ATOM 4358 C CE1 . TYR B 1 160 ? 12.836 12.236 41.499 1.00 19.89 ? 160 TYR B CE1 1 ATOM 4359 C CE2 . TYR B 1 160 ? 12.830 9.859 41.337 1.00 19.86 ? 160 TYR B CE2 1 ATOM 4360 C CZ . TYR B 1 160 ? 12.186 11.065 41.240 1.00 19.70 ? 160 TYR B CZ 1 ATOM 4361 O OH . TYR B 1 160 ? 10.839 11.103 40.888 1.00 22.54 ? 160 TYR B OH 1 ATOM 4362 N N . ASN B 1 161 ? 19.614 11.633 41.329 1.00 13.09 ? 161 ASN B N 1 ATOM 4363 C CA . ASN B 1 161 ? 21.035 11.818 41.666 1.00 12.44 ? 161 ASN B CA 1 ATOM 4364 C C . ASN B 1 161 ? 21.737 12.610 40.583 1.00 12.58 ? 161 ASN B C 1 ATOM 4365 O O . ASN B 1 161 ? 22.552 12.067 39.839 1.00 12.13 ? 161 ASN B O 1 ATOM 4366 C CB . ASN B 1 161 ? 21.740 10.463 41.885 1.00 11.47 ? 161 ASN B CB 1 ATOM 4367 C CG . ASN B 1 161 ? 23.241 10.612 42.139 1.00 11.59 ? 161 ASN B CG 1 ATOM 4368 O OD1 . ASN B 1 161 ? 23.680 11.634 42.634 1.00 10.58 ? 161 ASN B OD1 1 ATOM 4369 N ND2 . ASN B 1 161 ? 24.041 9.585 41.751 1.00 12.01 ? 161 ASN B ND2 1 ATOM 4370 N N . PRO B 1 162 ? 21.432 13.904 40.459 1.00 12.49 ? 162 PRO B N 1 ATOM 4371 C CA . PRO B 1 162 ? 22.113 14.725 39.451 1.00 12.88 ? 162 PRO B CA 1 ATOM 4372 C C . PRO B 1 162 ? 23.586 14.962 39.760 1.00 13.10 ? 162 PRO B C 1 ATOM 4373 O O . PRO B 1 162 ? 24.386 15.261 38.850 1.00 13.29 ? 162 PRO B O 1 ATOM 4374 C CB . PRO B 1 162 ? 21.313 16.043 39.454 1.00 12.64 ? 162 PRO B CB 1 ATOM 4375 C CG . PRO B 1 162 ? 20.699 16.071 40.824 1.00 13.31 ? 162 PRO B CG 1 ATOM 4376 C CD . PRO B 1 162 ? 20.410 14.667 41.207 1.00 13.04 ? 162 PRO B CD 1 ATOM 4377 N N . GLY B 1 163 ? 23.957 14.828 41.035 1.00 12.08 ? 163 GLY B N 1 ATOM 4378 C CA . GLY B 1 163 ? 25.330 15.049 41.461 1.00 12.46 ? 163 GLY B CA 1 ATOM 4379 C C . GLY B 1 163 ? 26.324 14.084 40.862 1.00 11.95 ? 163 GLY B C 1 ATOM 4380 O O . GLY B 1 163 ? 27.331 14.506 40.320 1.00 11.50 ? 163 GLY B O 1 ATOM 4381 N N . GLY B 1 164 ? 26.041 12.791 40.996 1.00 11.12 ? 164 GLY B N 1 ATOM 4382 C CA . GLY B 1 164 ? 26.882 11.763 40.431 1.00 10.46 ? 164 GLY B CA 1 ATOM 4383 C C . GLY B 1 164 ? 28.316 11.773 40.933 1.00 10.21 ? 164 GLY B C 1 ATOM 4384 O O . GLY B 1 164 ? 28.594 12.200 42.069 1.00 10.75 ? 164 GLY B O 1 ATOM 4385 N N . ALA B 1 165 ? 29.245 11.318 40.087 1.00 9.21 ? 165 ALA B N 1 ATOM 4386 C CA . ALA B 1 165 ? 30.640 11.204 40.476 1.00 9.45 ? 165 ALA B CA 1 ATOM 4387 C C . ALA B 1 165 ? 31.267 12.545 40.855 1.00 9.15 ? 165 ALA B C 1 ATOM 4388 O O . ALA B 1 165 ? 32.215 12.582 41.631 1.00 9.05 ? 165 ALA B O 1 ATOM 4389 C CB . ALA B 1 165 ? 31.424 10.568 39.348 1.00 9.77 ? 165 ALA B CB 1 ATOM 4390 N N . TYR B 1 166 ? 30.768 13.654 40.315 1.00 9.98 ? 166 TYR B N 1 ATOM 4391 C CA . TYR B 1 166 ? 31.267 14.978 40.655 1.00 9.74 ? 166 TYR B CA 1 ATOM 4392 C C . TYR B 1 166 ? 31.176 15.249 42.152 1.00 9.98 ? 166 TYR B C 1 ATOM 4393 O O . TYR B 1 166 ? 31.961 16.017 42.693 1.00 10.07 ? 166 TYR B O 1 ATOM 4394 C CB . TYR B 1 166 ? 30.476 16.040 39.847 1.00 11.23 ? 166 TYR B CB 1 ATOM 4395 C CG . TYR B 1 166 ? 30.958 17.463 39.809 1.00 12.17 ? 166 TYR B CG 1 ATOM 4396 C CD1 . TYR B 1 166 ? 31.749 17.885 38.768 1.00 12.66 ? 166 TYR B CD1 1 ATOM 4397 C CD2 . TYR B 1 166 ? 30.576 18.392 40.768 1.00 11.67 ? 166 TYR B CD2 1 ATOM 4398 C CE1 . TYR B 1 166 ? 32.184 19.207 38.674 1.00 14.14 ? 166 TYR B CE1 1 ATOM 4399 C CE2 . TYR B 1 166 ? 30.990 19.722 40.690 1.00 12.84 ? 166 TYR B CE2 1 ATOM 4400 C CZ . TYR B 1 166 ? 31.798 20.123 39.636 1.00 13.27 ? 166 TYR B CZ 1 ATOM 4401 O OH . TYR B 1 166 ? 32.233 21.425 39.505 1.00 18.00 ? 166 TYR B OH 1 ATOM 4402 N N . TYR B 1 167 ? 30.236 14.583 42.813 1.00 9.37 ? 167 TYR B N 1 ATOM 4403 C CA . TYR B 1 167 ? 30.047 14.681 44.255 1.00 9.95 ? 167 TYR B CA 1 ATOM 4404 C C . TYR B 1 167 ? 30.401 13.383 44.969 1.00 9.44 ? 167 TYR B C 1 ATOM 4405 O O . TYR B 1 167 ? 30.100 13.230 46.140 1.00 10.21 ? 167 TYR B O 1 ATOM 4406 C CB . TYR B 1 167 ? 28.588 15.097 44.596 1.00 10.81 ? 167 TYR B CB 1 ATOM 4407 C CG . TYR B 1 167 ? 28.298 16.553 44.344 1.00 11.40 ? 167 TYR B CG 1 ATOM 4408 C CD1 . TYR B 1 167 ? 27.903 16.980 43.082 1.00 12.30 ? 167 TYR B CD1 1 ATOM 4409 C CD2 . TYR B 1 167 ? 28.474 17.514 45.334 1.00 12.90 ? 167 TYR B CD2 1 ATOM 4410 C CE1 . TYR B 1 167 ? 27.661 18.324 42.803 1.00 12.50 ? 167 TYR B CE1 1 ATOM 4411 C CE2 . TYR B 1 167 ? 28.220 18.866 45.066 1.00 12.69 ? 167 TYR B CE2 1 ATOM 4412 C CZ . TYR B 1 167 ? 27.825 19.263 43.789 1.00 12.57 ? 167 TYR B CZ 1 ATOM 4413 O OH . TYR B 1 167 ? 27.600 20.591 43.460 1.00 14.86 ? 167 TYR B OH 1 ATOM 4414 N N . GLY B 1 168 ? 31.044 12.446 44.275 1.00 8.77 ? 168 GLY B N 1 ATOM 4415 C CA . GLY B 1 168 ? 31.512 11.226 44.906 1.00 8.82 ? 168 GLY B CA 1 ATOM 4416 C C . GLY B 1 168 ? 30.436 10.230 45.281 1.00 8.65 ? 168 GLY B C 1 ATOM 4417 O O . GLY B 1 168 ? 30.613 9.505 46.256 1.00 8.82 ? 168 GLY B O 1 ATOM 4418 N N . THR B 1 169 ? 29.349 10.167 44.515 1.00 8.78 ? 169 THR B N 1 ATOM 4419 C CA . THR B 1 169 ? 28.296 9.200 44.788 1.00 9.00 ? 169 THR B CA 1 ATOM 4420 C C . THR B 1 169 ? 28.651 7.803 44.308 1.00 9.05 ? 169 THR B C 1 ATOM 4421 O O . THR B 1 169 ? 29.508 7.618 43.449 1.00 8.99 ? 169 THR B O 1 ATOM 4422 C CB . THR B 1 169 ? 26.920 9.618 44.188 1.00 9.53 ? 169 THR B CB 1 ATOM 4423 O OG1 . THR B 1 169 ? 26.979 9.653 42.744 1.00 9.52 ? 169 THR B OG1 1 ATOM 4424 C CG2 . THR B 1 169 ? 26.488 11.004 44.637 1.00 9.56 ? 169 THR B CG2 1 ATOM 4425 N N . GLY B 1 170 ? 27.965 6.809 44.854 1.00 9.12 ? 170 GLY B N 1 ATOM 4426 C CA . GLY B 1 170 ? 28.099 5.450 44.361 1.00 9.26 ? 170 GLY B CA 1 ATOM 4427 C C . GLY B 1 170 ? 29.089 4.528 45.062 1.00 8.57 ? 170 GLY B C 1 ATOM 4428 O O . GLY B 1 170 ? 29.367 3.446 44.559 1.00 9.42 ? 170 GLY B O 1 ATOM 4429 N N . TYR B 1 171 ? 29.617 4.917 46.234 1.00 8.31 ? 171 TYR B N 1 ATOM 4430 C CA . TYR B 1 171 ? 30.560 4.049 46.941 1.00 8.83 ? 171 TYR B CA 1 ATOM 4431 C C . TYR B 1 171 ? 29.966 2.678 47.283 1.00 9.00 ? 171 TYR B C 1 ATOM 4432 O O . TYR B 1 171 ? 28.783 2.563 47.651 1.00 8.84 ? 171 TYR B O 1 ATOM 4433 C CB . TYR B 1 171 ? 31.098 4.704 48.212 1.00 9.09 ? 171 TYR B CB 1 ATOM 4434 C CG . TYR B 1 171 ? 32.116 3.828 48.898 1.00 8.56 ? 171 TYR B CG 1 ATOM 4435 C CD1 . TYR B 1 171 ? 33.368 3.660 48.347 1.00 9.05 ? 171 TYR B CD1 1 ATOM 4436 C CD2 . TYR B 1 171 ? 31.831 3.134 50.064 1.00 8.57 ? 171 TYR B CD2 1 ATOM 4437 C CE1 . TYR B 1 171 ? 34.311 2.847 48.932 1.00 8.29 ? 171 TYR B CE1 1 ATOM 4438 C CE2 . TYR B 1 171 ? 32.785 2.322 50.661 1.00 8.20 ? 171 TYR B CE2 1 ATOM 4439 C CZ . TYR B 1 171 ? 34.013 2.162 50.059 1.00 8.70 ? 171 TYR B CZ 1 ATOM 4440 O OH . TYR B 1 171 ? 34.982 1.368 50.634 1.00 9.27 ? 171 TYR B OH 1 ATOM 4441 N N . CYS B 1 172 ? 30.807 1.655 47.186 1.00 8.99 ? 172 CYS B N 1 ATOM 4442 C CA . CYS B 1 172 ? 30.485 0.312 47.641 1.00 8.88 ? 172 CYS B CA 1 ATOM 4443 C C . CYS B 1 172 ? 31.787 -0.396 47.973 1.00 8.75 ? 172 CYS B C 1 ATOM 4444 O O . CYS B 1 172 ? 32.853 0.030 47.522 1.00 9.18 ? 172 CYS B O 1 ATOM 4445 C CB . CYS B 1 172 ? 29.714 -0.451 46.565 1.00 9.55 ? 172 CYS B CB 1 ATOM 4446 S SG . CYS B 1 172 ? 30.551 -0.582 44.966 1.00 10.27 ? 172 CYS B SG 1 ATOM 4447 N N . ASP B 1 173 ? 31.707 -1.471 48.732 1.00 9.12 ? 173 ASP B N 1 ATOM 4448 C CA . ASP B 1 173 ? 32.874 -2.326 48.937 1.00 9.52 ? 173 ASP B CA 1 ATOM 4449 C C . ASP B 1 173 ? 32.397 -3.698 49.391 1.00 9.55 ? 173 ASP B C 1 ATOM 4450 O O . ASP B 1 173 ? 31.191 -3.969 49.471 1.00 9.47 ? 173 ASP B O 1 ATOM 4451 C CB . ASP B 1 173 ? 33.901 -1.686 49.898 1.00 9.26 ? 173 ASP B CB 1 ATOM 4452 C CG . ASP B 1 173 ? 33.367 -1.447 51.292 1.00 9.66 ? 173 ASP B CG 1 ATOM 4453 O OD1 . ASP B 1 173 ? 32.508 -2.257 51.752 1.00 9.64 ? 173 ASP B OD1 1 ATOM 4454 O OD2 . ASP B 1 173 ? 33.803 -0.483 51.990 1.00 9.63 ? 173 ASP B OD2 1 ATOM 4455 N N . ALA B 1 174 ? 33.339 -4.581 49.669 1.00 9.33 ? 174 ALA B N 1 ATOM 4456 C CA . ALA B 1 174 ? 32.998 -5.953 49.963 1.00 9.66 ? 174 ALA B CA 1 ATOM 4457 C C . ALA B 1 174 ? 32.401 -6.182 51.347 1.00 9.52 ? 174 ALA B C 1 ATOM 4458 O O . ALA B 1 174 ? 32.091 -7.357 51.666 1.00 10.65 ? 174 ALA B O 1 ATOM 4459 C CB . ALA B 1 174 ? 34.218 -6.842 49.786 1.00 10.23 ? 174 ALA B CB 1 ATOM 4460 N N . GLN B 1 175 ? 32.276 -5.125 52.153 1.00 9.25 ? 175 GLN B N 1 ATOM 4461 C CA . GLN B 1 175 ? 31.652 -5.251 53.474 1.00 10.04 ? 175 GLN B CA 1 ATOM 4462 C C . GLN B 1 175 ? 30.135 -5.084 53.456 1.00 9.37 ? 175 GLN B C 1 ATOM 4463 O O . GLN B 1 175 ? 29.467 -5.349 54.473 1.00 10.56 ? 175 GLN B O 1 ATOM 4464 C CB . GLN B 1 175 ? 32.254 -4.297 54.497 1.00 10.42 ? 175 GLN B CB 1 ATOM 4465 C CG . GLN B 1 175 ? 33.757 -4.394 54.630 1.00 11.13 ? 175 GLN B CG 1 ATOM 4466 C CD . GLN B 1 175 ? 34.268 -5.779 54.900 1.00 11.77 ? 175 GLN B CD 1 ATOM 4467 O OE1 . GLN B 1 175 ? 33.753 -6.489 55.765 1.00 13.98 ? 175 GLN B OE1 1 ATOM 4468 N NE2 . GLN B 1 175 ? 35.273 -6.187 54.150 1.00 13.01 ? 175 GLN B NE2 1 ATOM 4469 N N . CYS B 1 176 ? 29.557 -4.666 52.330 1.00 9.40 ? 176 CYS B N 1 ATOM 4470 C CA . CYS B 1 176 ? 28.111 -4.568 52.226 1.00 9.99 ? 176 CYS B CA 1 ATOM 4471 C C . CYS B 1 176 ? 27.494 -3.689 53.321 1.00 10.68 ? 176 CYS B C 1 ATOM 4472 O O . CYS B 1 176 ? 26.432 -3.997 53.855 1.00 11.24 ? 176 CYS B O 1 ATOM 4473 C CB . CYS B 1 176 ? 27.455 -5.967 52.236 1.00 10.20 ? 176 CYS B CB 1 ATOM 4474 S SG . CYS B 1 176 ? 27.773 -6.980 50.774 1.00 11.46 ? 176 CYS B SG 1 ATOM 4475 N N . PHE B 1 177 ? 28.153 -2.581 53.656 1.00 10.22 ? 177 PHE B N 1 ATOM 4476 C CA . PHE B 1 177 ? 27.644 -1.693 54.687 1.00 10.17 ? 177 PHE B CA 1 ATOM 4477 C C . PHE B 1 177 ? 26.346 -1.005 54.269 1.00 10.29 ? 177 PHE B C 1 ATOM 4478 O O . PHE B 1 177 ? 26.157 -0.653 53.098 1.00 10.59 ? 177 PHE B O 1 ATOM 4479 C CB . PHE B 1 177 ? 28.649 -0.587 55.046 1.00 11.16 ? 177 PHE B CB 1 ATOM 4480 C CG . PHE B 1 177 ? 29.966 -1.080 55.660 1.00 10.77 ? 177 PHE B CG 1 ATOM 4481 C CD1 . PHE B 1 177 ? 29.968 -1.860 56.811 1.00 12.35 ? 177 PHE B CD1 1 ATOM 4482 C CD2 . PHE B 1 177 ? 31.197 -0.626 55.185 1.00 11.03 ? 177 PHE B CD2 1 ATOM 4483 C CE1 . PHE B 1 177 ? 31.140 -2.262 57.415 1.00 12.97 ? 177 PHE B CE1 1 ATOM 4484 C CE2 . PHE B 1 177 ? 32.388 -1.026 55.809 1.00 11.88 ? 177 PHE B CE2 1 ATOM 4485 C CZ . PHE B 1 177 ? 32.357 -1.839 56.926 1.00 13.07 ? 177 PHE B CZ 1 ATOM 4486 N N . VAL B 1 178 ? 25.491 -0.741 55.258 1.00 10.61 ? 178 VAL B N 1 ATOM 4487 C CA . VAL B 1 178 ? 24.276 0.032 55.044 1.00 11.05 ? 178 VAL B CA 1 ATOM 4488 C C . VAL B 1 178 ? 24.631 1.497 55.158 1.00 10.83 ? 178 VAL B C 1 ATOM 4489 O O . VAL B 1 178 ? 25.121 1.941 56.184 1.00 11.69 ? 178 VAL B O 1 ATOM 4490 C CB . VAL B 1 178 ? 23.228 -0.308 56.101 1.00 11.34 ? 178 VAL B CB 1 ATOM 4491 C CG1 . VAL B 1 178 ? 21.966 0.542 55.903 1.00 12.32 ? 178 VAL B CG1 1 ATOM 4492 C CG2 . VAL B 1 178 ? 22.908 -1.779 56.056 1.00 12.21 ? 178 VAL B CG2 1 ATOM 4493 N N . THR B 1 179 ? 24.387 2.248 54.096 1.00 11.38 ? 179 THR B N 1 ATOM 4494 C CA . THR B 1 179 ? 24.520 3.701 54.138 1.00 11.14 ? 179 THR B CA 1 ATOM 4495 C C . THR B 1 179 ? 23.199 4.367 53.773 1.00 11.24 ? 179 THR B C 1 ATOM 4496 O O . THR B 1 179 ? 22.388 3.773 53.034 1.00 11.49 ? 179 THR B O 1 ATOM 4497 C CB . THR B 1 179 ? 25.631 4.181 53.173 1.00 11.09 ? 179 THR B CB 1 ATOM 4498 O OG1 . THR B 1 179 ? 25.401 3.656 51.854 1.00 11.11 ? 179 THR B OG1 1 ATOM 4499 C CG2 . THR B 1 179 ? 26.989 3.621 53.576 1.00 12.29 ? 179 THR B CG2 1 ATOM 4500 N N . PRO B 1 180 ? 22.938 5.566 54.299 1.00 10.76 ? 180 PRO B N 1 ATOM 4501 C CA . PRO B 1 180 ? 21.599 6.151 54.098 1.00 11.40 ? 180 PRO B CA 1 ATOM 4502 C C . PRO B 1 180 ? 21.278 6.522 52.653 1.00 11.05 ? 180 PRO B C 1 ATOM 4503 O O . PRO B 1 180 ? 20.106 6.670 52.299 1.00 11.87 ? 180 PRO B O 1 ATOM 4504 C CB . PRO B 1 180 ? 21.602 7.394 54.998 1.00 12.77 ? 180 PRO B CB 1 ATOM 4505 C CG . PRO B 1 180 ? 23.015 7.668 55.277 1.00 12.03 ? 180 PRO B CG 1 ATOM 4506 C CD . PRO B 1 180 ? 23.744 6.351 55.256 1.00 11.02 ? 180 PRO B CD 1 ATOM 4507 N N . PHE B 1 181 ? 22.309 6.727 51.831 1.00 10.55 ? 181 PHE B N 1 ATOM 4508 C CA . PHE B 1 181 ? 22.156 6.836 50.376 1.00 10.62 ? 181 PHE B CA 1 ATOM 4509 C C . PHE B 1 181 ? 23.022 5.769 49.752 1.00 10.04 ? 181 PHE B C 1 ATOM 4510 O O . PHE B 1 181 ? 24.146 5.526 50.237 1.00 10.39 ? 181 PHE B O 1 ATOM 4511 C CB . PHE B 1 181 ? 22.559 8.235 49.878 1.00 10.67 ? 181 PHE B CB 1 ATOM 4512 C CG . PHE B 1 181 ? 21.629 9.316 50.373 1.00 10.51 ? 181 PHE B CG 1 ATOM 4513 C CD1 . PHE B 1 181 ? 21.756 9.785 51.657 1.00 11.83 ? 181 PHE B CD1 1 ATOM 4514 C CD2 . PHE B 1 181 ? 20.644 9.866 49.556 1.00 10.85 ? 181 PHE B CD2 1 ATOM 4515 C CE1 . PHE B 1 181 ? 20.897 10.750 52.159 1.00 12.03 ? 181 PHE B CE1 1 ATOM 4516 C CE2 . PHE B 1 181 ? 19.789 10.846 50.071 1.00 12.85 ? 181 PHE B CE2 1 ATOM 4517 C CZ . PHE B 1 181 ? 19.930 11.275 51.348 1.00 12.04 ? 181 PHE B CZ 1 ATOM 4518 N N . ILE B 1 182 ? 22.518 5.179 48.666 1.00 10.20 ? 182 ILE B N 1 ATOM 4519 C CA . ILE B 1 182 ? 23.276 4.260 47.814 1.00 10.79 ? 182 ILE B CA 1 ATOM 4520 C C . ILE B 1 182 ? 23.067 4.747 46.377 1.00 11.00 ? 182 ILE B C 1 ATOM 4521 O O . ILE B 1 182 ? 21.938 5.026 45.958 1.00 11.06 ? 182 ILE B O 1 ATOM 4522 C CB . ILE B 1 182 ? 22.850 2.797 47.986 1.00 11.18 ? 182 ILE B CB 1 ATOM 4523 C CG1 . ILE B 1 182 ? 23.230 2.308 49.403 1.00 11.51 ? 182 ILE B CG1 1 ATOM 4524 C CG2 . ILE B 1 182 ? 23.504 1.911 46.931 1.00 11.35 ? 182 ILE B CG2 1 ATOM 4525 C CD1 . ILE B 1 182 ? 22.776 0.906 49.733 1.00 12.40 ? 182 ILE B CD1 1 ATOM 4526 N N . ASN B 1 183 ? 24.155 4.872 45.612 1.00 10.08 ? 183 ASN B N 1 ATOM 4527 C CA . ASN B 1 183 ? 24.051 5.395 44.247 1.00 10.49 ? 183 ASN B CA 1 ATOM 4528 C C . ASN B 1 183 ? 23.333 6.750 44.205 1.00 10.38 ? 183 ASN B C 1 ATOM 4529 O O . ASN B 1 183 ? 22.598 7.066 43.269 1.00 11.25 ? 183 ASN B O 1 ATOM 4530 C CB . ASN B 1 183 ? 23.437 4.359 43.315 1.00 11.51 ? 183 ASN B CB 1 ATOM 4531 C CG . ASN B 1 183 ? 24.483 3.398 42.761 1.00 11.49 ? 183 ASN B CG 1 ATOM 4532 O OD1 . ASN B 1 183 ? 25.691 3.705 42.754 1.00 12.66 ? 183 ASN B OD1 1 ATOM 4533 N ND2 . ASN B 1 183 ? 24.030 2.265 42.262 1.00 14.41 ? 183 ASN B ND2 1 ATOM 4534 N N . GLY B 1 184 ? 23.572 7.575 45.220 1.00 10.83 ? 184 GLY B N 1 ATOM 4535 C CA . GLY B 1 184 ? 22.965 8.878 45.302 1.00 10.53 ? 184 GLY B CA 1 ATOM 4536 C C . GLY B 1 184 ? 21.488 8.921 45.558 1.00 10.84 ? 184 GLY B C 1 ATOM 4537 O O . GLY B 1 184 ? 20.880 10.003 45.405 1.00 12.07 ? 184 GLY B O 1 ATOM 4538 N N . LEU B 1 185 ? 20.905 7.786 45.950 1.00 10.78 ? 185 LEU B N 1 ATOM 4539 C CA . LEU B 1 185 ? 19.452 7.692 46.201 1.00 11.28 ? 185 LEU B CA 1 ATOM 4540 C C . LEU B 1 185 ? 19.198 7.266 47.632 1.00 11.70 ? 185 LEU B C 1 ATOM 4541 O O . LEU B 1 185 ? 19.914 6.449 48.170 1.00 11.06 ? 185 LEU B O 1 ATOM 4542 C CB . LEU B 1 185 ? 18.825 6.648 45.288 1.00 11.59 ? 185 LEU B CB 1 ATOM 4543 C CG . LEU B 1 185 ? 19.046 6.862 43.787 1.00 13.49 ? 185 LEU B CG 1 ATOM 4544 C CD1 . LEU B 1 185 ? 18.413 5.688 43.045 1.00 15.27 ? 185 LEU B CD1 1 ATOM 4545 C CD2 . LEU B 1 185 ? 18.509 8.189 43.313 1.00 15.09 ? 185 LEU B CD2 1 ATOM 4546 N N . GLY B 1 186 ? 18.143 7.793 48.238 1.00 11.62 ? 186 GLY B N 1 ATOM 4547 C CA . GLY B 1 186 ? 17.823 7.399 49.608 1.00 12.33 ? 186 GLY B CA 1 ATOM 4548 C C . GLY B 1 186 ? 17.605 5.904 49.701 1.00 12.41 ? 186 GLY B C 1 ATOM 4549 O O . GLY B 1 186 ? 16.887 5.323 48.876 1.00 13.70 ? 186 GLY B O 1 ATOM 4550 N N . ASN B 1 187 ? 18.251 5.265 50.682 1.00 12.06 ? 187 ASN B N 1 ATOM 4551 C CA . ASN B 1 187 ? 18.254 3.808 50.832 1.00 12.92 ? 187 ASN B CA 1 ATOM 4552 C C . ASN B 1 187 ? 17.112 3.438 51.775 1.00 13.60 ? 187 ASN B C 1 ATOM 4553 O O . ASN B 1 187 ? 17.304 3.032 52.924 1.00 12.48 ? 187 ASN B O 1 ATOM 4554 C CB . ASN B 1 187 ? 19.619 3.375 51.377 1.00 12.23 ? 187 ASN B CB 1 ATOM 4555 C CG . ASN B 1 187 ? 19.749 1.869 51.580 1.00 13.12 ? 187 ASN B CG 1 ATOM 4556 O OD1 . ASN B 1 187 ? 18.999 1.063 51.014 1.00 13.01 ? 187 ASN B OD1 1 ATOM 4557 N ND2 . ASN B 1 187 ? 20.714 1.485 52.417 1.00 12.64 ? 187 ASN B ND2 1 ATOM 4558 N N . ILE B 1 188 ? 15.906 3.572 51.235 1.00 14.42 ? 188 ILE B N 1 ATOM 4559 C CA . ILE B 1 188 ? 14.685 3.520 52.025 1.00 15.04 ? 188 ILE B CA 1 ATOM 4560 C C . ILE B 1 188 ? 14.563 2.185 52.753 1.00 15.19 ? 188 ILE B C 1 ATOM 4561 O O . ILE B 1 188 ? 14.138 2.139 53.915 1.00 16.45 ? 188 ILE B O 1 ATOM 4562 C CB . ILE B 1 188 ? 13.449 3.754 51.128 1.00 15.53 ? 188 ILE B CB 1 ATOM 4563 C CG1 . ILE B 1 188 ? 13.614 4.980 50.208 1.00 15.81 ? 188 ILE B CG1 1 ATOM 4564 C CG2 . ILE B 1 188 ? 12.207 3.900 52.003 1.00 17.07 ? 188 ILE B CG2 1 ATOM 4565 C CD1 . ILE B 1 188 ? 13.980 6.267 50.888 1.00 16.67 ? 188 ILE B CD1 1 ATOM 4566 N N . GLU B 1 189 ? 14.978 1.104 52.089 1.00 15.44 ? 189 GLU B N 1 ATOM 4567 C CA . GLU B 1 189 ? 14.839 -0.232 52.652 1.00 16.66 ? 189 GLU B CA 1 ATOM 4568 C C . GLU B 1 189 ? 16.041 -0.685 53.459 1.00 15.81 ? 189 GLU B C 1 ATOM 4569 O O . GLU B 1 189 ? 16.083 -1.832 53.929 1.00 16.32 ? 189 GLU B O 1 ATOM 4570 C CB . GLU B 1 189 ? 14.584 -1.239 51.557 1.00 17.85 ? 189 GLU B CB 1 ATOM 4571 C CG . GLU B 1 189 ? 13.252 -1.054 50.851 1.00 20.69 ? 189 GLU B CG 1 ATOM 4572 C CD . GLU B 1 189 ? 12.956 -2.171 49.879 1.00 22.94 ? 189 GLU B CD 1 ATOM 4573 O OE1 . GLU B 1 189 ? 13.253 -3.343 50.217 1.00 30.68 ? 189 GLU B OE1 1 ATOM 4574 O OE2 . GLU B 1 189 ? 12.417 -1.893 48.783 1.00 30.26 ? 189 GLU B OE2 1 ATOM 4575 N N . GLY B 1 190 ? 17.031 0.184 53.649 1.00 14.86 ? 190 GLY B N 1 ATOM 4576 C CA . GLY B 1 190 ? 18.168 -0.189 54.470 1.00 14.41 ? 190 GLY B CA 1 ATOM 4577 C C . GLY B 1 190 ? 19.000 -1.355 53.961 1.00 14.32 ? 190 GLY B C 1 ATOM 4578 O O . GLY B 1 190 ? 19.503 -2.158 54.759 1.00 14.21 ? 190 GLY B O 1 ATOM 4579 N N . LYS B 1 191 ? 19.214 -1.413 52.653 1.00 12.85 ? 191 LYS B N 1 ATOM 4580 C CA . LYS B 1 191 ? 20.061 -2.443 52.046 1.00 13.50 ? 191 LYS B CA 1 ATOM 4581 C C . LYS B 1 191 ? 21.527 -2.108 52.228 1.00 12.44 ? 191 LYS B C 1 ATOM 4582 O O . LYS B 1 191 ? 21.889 -0.985 52.542 1.00 12.12 ? 191 LYS B O 1 ATOM 4583 C CB . LYS B 1 191 ? 19.701 -2.583 50.566 1.00 14.52 ? 191 LYS B CB 1 ATOM 4584 C CG . LYS B 1 191 ? 18.252 -3.080 50.383 1.00 17.00 ? 191 LYS B CG 1 ATOM 4585 C CD . LYS B 1 191 ? 17.985 -3.770 49.075 1.00 17.81 ? 191 LYS B CD 1 ATOM 4586 C CE . LYS B 1 191 ? 16.508 -4.251 48.974 1.00 18.77 ? 191 LYS B CE 1 ATOM 4587 N NZ . LYS B 1 191 ? 16.141 -4.486 47.575 1.00 23.46 ? 191 LYS B NZ 1 ATOM 4588 N N . GLY B 1 192 ? 22.359 -3.123 52.044 1.00 11.79 ? 192 GLY B N 1 ATOM 4589 C CA . GLY B 1 192 ? 23.813 -2.933 52.093 1.00 11.49 ? 192 GLY B CA 1 ATOM 4590 C C . GLY B 1 192 ? 24.385 -2.652 50.700 1.00 11.73 ? 192 GLY B C 1 ATOM 4591 O O . GLY B 1 192 ? 23.825 -3.062 49.680 1.00 12.37 ? 192 GLY B O 1 ATOM 4592 N N . SER B 1 193 ? 25.519 -1.954 50.669 1.00 11.35 ? 193 SER B N 1 ATOM 4593 C CA . SER B 1 193 ? 26.136 -1.496 49.426 1.00 11.07 ? 193 SER B CA 1 ATOM 4594 C C . SER B 1 193 ? 27.359 -2.361 49.084 1.00 9.80 ? 193 SER B C 1 ATOM 4595 O O . SER B 1 193 ? 28.461 -2.108 49.588 1.00 10.45 ? 193 SER B O 1 ATOM 4596 C CB . SER B 1 193 ? 26.531 -0.030 49.553 1.00 10.65 ? 193 SER B CB 1 ATOM 4597 O OG . SER B 1 193 ? 26.986 0.461 48.294 1.00 11.18 ? 193 SER B OG 1 ATOM 4598 N N . CYS B 1 194 ? 27.134 -3.396 48.275 1.00 10.37 ? 194 CYS B N 1 ATOM 4599 C CA . CYS B 1 194 ? 28.120 -4.449 48.034 1.00 10.29 ? 194 CYS B CA 1 ATOM 4600 C C . CYS B 1 194 ? 28.804 -4.302 46.694 1.00 10.36 ? 194 CYS B C 1 ATOM 4601 O O . CYS B 1 194 ? 28.152 -4.036 45.692 1.00 11.25 ? 194 CYS B O 1 ATOM 4602 C CB . CYS B 1 194 ? 27.385 -5.791 47.962 1.00 11.12 ? 194 CYS B CB 1 ATOM 4603 S SG . CYS B 1 194 ? 26.446 -6.262 49.410 1.00 11.68 ? 194 CYS B SG 1 ATOM 4604 N N . CYS B 1 195 ? 30.102 -4.554 46.649 1.00 9.67 ? 195 CYS B N 1 ATOM 4605 C CA . CYS B 1 195 ? 30.771 -4.779 45.369 1.00 9.83 ? 195 CYS B CA 1 ATOM 4606 C C . CYS B 1 195 ? 32.135 -5.385 45.577 1.00 9.64 ? 195 CYS B C 1 ATOM 4607 O O . CYS B 1 195 ? 32.713 -5.289 46.666 1.00 10.36 ? 195 CYS B O 1 ATOM 4608 C CB . CYS B 1 195 ? 30.865 -3.517 44.500 1.00 10.37 ? 195 CYS B CB 1 ATOM 4609 S SG . CYS B 1 195 ? 31.814 -2.146 45.200 1.00 10.36 ? 195 CYS B SG 1 ATOM 4610 N N . ASN B 1 196 ? 32.643 -6.012 44.512 1.00 9.60 ? 196 ASN B N 1 ATOM 4611 C CA . ASN B 1 196 ? 34.017 -6.523 44.442 1.00 10.46 ? 196 ASN B CA 1 ATOM 4612 C C . ASN B 1 196 ? 34.989 -5.418 44.826 1.00 10.25 ? 196 ASN B C 1 ATOM 4613 O O . ASN B 1 196 ? 34.814 -4.285 44.394 1.00 11.14 ? 196 ASN B O 1 ATOM 4614 C CB . ASN B 1 196 ? 34.337 -6.941 43.004 1.00 11.68 ? 196 ASN B CB 1 ATOM 4615 C CG . ASN B 1 196 ? 33.707 -8.249 42.600 1.00 13.76 ? 196 ASN B CG 1 ATOM 4616 O OD1 . ASN B 1 196 ? 34.190 -9.336 42.930 1.00 15.58 ? 196 ASN B OD1 1 ATOM 4617 N ND2 . ASN B 1 196 ? 32.674 -8.154 41.797 1.00 16.87 ? 196 ASN B ND2 1 ATOM 4618 N N . SER B 1 197 ? 36.021 -5.761 45.590 1.00 10.03 ? 197 SER B N 1 ATOM 4619 C CA . SER B 1 197 ? 37.002 -4.784 46.028 1.00 10.53 ? 197 SER B CA 1 ATOM 4620 C C . SER B 1 197 ? 38.373 -5.419 45.947 1.00 10.08 ? 197 SER B C 1 ATOM 4621 O O . SER B 1 197 ? 38.552 -6.499 46.474 1.00 10.71 ? 197 SER B O 1 ATOM 4622 C CB . SER B 1 197 ? 36.789 -4.381 47.483 1.00 12.69 ? 197 SER B CB 1 ATOM 4623 O OG . SER B 1 197 ? 35.608 -3.679 47.713 1.00 16.14 ? 197 SER B OG 1 ATOM 4624 N N . MET B 1 198 ? 39.342 -4.751 45.330 1.00 9.40 ? 198 MET B N 1 ATOM 4625 C CA . MET B 1 198 ? 40.728 -5.221 45.295 1.00 9.20 ? 198 MET B CA 1 ATOM 4626 C C . MET B 1 198 ? 41.549 -4.307 46.189 1.00 10.03 ? 198 MET B C 1 ATOM 4627 O O . MET B 1 198 ? 41.767 -3.137 45.848 1.00 9.73 ? 198 MET B O 1 ATOM 4628 C CB . MET B 1 198 ? 41.281 -5.199 43.848 1.00 10.09 ? 198 MET B CB 1 ATOM 4629 C CG . MET B 1 198 ? 42.769 -5.473 43.745 1.00 10.62 ? 198 MET B CG 1 ATOM 4630 S SD . MET B 1 198 ? 43.237 -7.092 44.389 1.00 10.21 ? 198 MET B SD 1 ATOM 4631 C CE . MET B 1 198 ? 44.867 -6.785 45.125 1.00 10.11 ? 198 MET B CE 1 ATOM 4632 N N . ASP B 1 199 ? 41.999 -4.837 47.331 1.00 9.39 ? 199 ASP B N 1 ATOM 4633 C CA . ASP B 1 199 ? 42.780 -4.020 48.252 1.00 9.35 ? 199 ASP B CA 1 ATOM 4634 C C . ASP B 1 199 ? 44.236 -4.083 47.867 1.00 8.78 ? 199 ASP B C 1 ATOM 4635 O O . ASP B 1 199 ? 44.980 -4.962 48.294 1.00 8.91 ? 199 ASP B O 1 ATOM 4636 C CB . ASP B 1 199 ? 42.541 -4.432 49.710 1.00 9.81 ? 199 ASP B CB 1 ATOM 4637 C CG . ASP B 1 199 ? 41.091 -4.355 50.102 1.00 11.60 ? 199 ASP B CG 1 ATOM 4638 O OD1 . ASP B 1 199 ? 40.210 -3.982 49.287 1.00 14.30 ? 199 ASP B OD1 1 ATOM 4639 O OD2 . ASP B 1 199 ? 40.731 -4.736 51.186 1.00 14.60 ? 199 ASP B OD2 1 ATOM 4640 N N . ILE B 1 200 ? 44.633 -3.161 47.002 1.00 9.02 ? 200 ILE B N 1 ATOM 4641 C CA . ILE B 1 200 ? 46.025 -3.065 46.587 1.00 9.10 ? 200 ILE B CA 1 ATOM 4642 C C . ILE B 1 200 ? 46.894 -2.858 47.819 1.00 7.95 ? 200 ILE B C 1 ATOM 4643 O O . ILE B 1 200 ? 47.873 -3.576 48.024 1.00 8.75 ? 200 ILE B O 1 ATOM 4644 C CB . ILE B 1 200 ? 46.217 -1.946 45.554 1.00 8.45 ? 200 ILE B CB 1 ATOM 4645 C CG1 . ILE B 1 200 ? 45.474 -2.287 44.263 1.00 10.47 ? 200 ILE B CG1 1 ATOM 4646 C CG2 . ILE B 1 200 ? 47.711 -1.676 45.310 1.00 9.41 ? 200 ILE B CG2 1 ATOM 4647 C CD1 . ILE B 1 200 ? 45.465 -1.188 43.206 1.00 11.28 ? 200 ILE B CD1 1 ATOM 4648 N N . TRP B 1 201 ? 46.530 -1.881 48.654 1.00 8.85 ? 201 TRP B N 1 ATOM 4649 C CA . TRP B 1 201 ? 47.354 -1.475 49.779 1.00 8.65 ? 201 TRP B CA 1 ATOM 4650 C C . TRP B 1 201 ? 46.457 -1.150 50.957 1.00 8.70 ? 201 TRP B C 1 ATOM 4651 O O . TRP B 1 201 ? 45.583 -0.301 50.869 1.00 8.41 ? 201 TRP B O 1 ATOM 4652 C CB . TRP B 1 201 ? 48.197 -0.254 49.340 1.00 8.79 ? 201 TRP B CB 1 ATOM 4653 C CG . TRP B 1 201 ? 48.808 0.655 50.383 1.00 9.13 ? 201 TRP B CG 1 ATOM 4654 C CD1 . TRP B 1 201 ? 48.211 1.722 50.964 1.00 9.05 ? 201 TRP B CD1 1 ATOM 4655 C CD2 . TRP B 1 201 ? 50.151 0.633 50.895 1.00 9.00 ? 201 TRP B CD2 1 ATOM 4656 N NE1 . TRP B 1 201 ? 49.065 2.358 51.823 1.00 8.72 ? 201 TRP B NE1 1 ATOM 4657 C CE2 . TRP B 1 201 ? 50.280 1.729 51.771 1.00 8.33 ? 201 TRP B CE2 1 ATOM 4658 C CE3 . TRP B 1 201 ? 51.264 -0.179 50.682 1.00 9.86 ? 201 TRP B CE3 1 ATOM 4659 C CZ2 . TRP B 1 201 ? 51.444 2.001 52.460 1.00 10.12 ? 201 TRP B CZ2 1 ATOM 4660 C CZ3 . TRP B 1 201 ? 52.412 0.097 51.365 1.00 10.97 ? 201 TRP B CZ3 1 ATOM 4661 C CH2 . TRP B 1 201 ? 52.501 1.181 52.233 1.00 10.21 ? 201 TRP B CH2 1 ATOM 4662 N N . GLU B 1 202 ? 46.707 -1.823 52.079 1.00 9.39 ? 202 GLU B N 1 ATOM 4663 C CA . GLU B 1 202 ? 46.198 -1.433 53.392 1.00 8.93 ? 202 GLU B CA 1 ATOM 4664 C C . GLU B 1 202 ? 47.424 -1.588 54.268 1.00 8.37 ? 202 GLU B C 1 ATOM 4665 O O . GLU B 1 202 ? 47.938 -2.699 54.452 1.00 8.99 ? 202 GLU B O 1 ATOM 4666 C CB . GLU B 1 202 ? 45.057 -2.344 53.867 1.00 9.21 ? 202 GLU B CB 1 ATOM 4667 C CG . GLU B 1 202 ? 43.787 -2.142 53.054 1.00 10.92 ? 202 GLU B CG 1 ATOM 4668 C CD . GLU B 1 202 ? 42.680 -3.044 53.535 1.00 10.74 ? 202 GLU B CD 1 ATOM 4669 O OE1 . GLU B 1 202 ? 41.885 -2.596 54.398 1.00 12.02 ? 202 GLU B OE1 1 ATOM 4670 O OE2 . GLU B 1 202 ? 42.627 -4.227 53.079 1.00 11.97 ? 202 GLU B OE2 1 ATOM 4671 N N . ALA B 1 203 ? 47.914 -0.499 54.822 1.00 8.14 ? 203 ALA B N 1 ATOM 4672 C CA . ALA B 1 203 ? 49.207 -0.564 55.462 1.00 8.63 ? 203 ALA B CA 1 ATOM 4673 C C . ALA B 1 203 ? 49.466 0.603 56.394 1.00 8.30 ? 203 ALA B C 1 ATOM 4674 O O . ALA B 1 203 ? 48.855 1.671 56.282 1.00 8.72 ? 203 ALA B O 1 ATOM 4675 C CB . ALA B 1 203 ? 50.327 -0.610 54.419 1.00 9.38 ? 203 ALA B CB 1 ATOM 4676 N N . ASN B 1 204 ? 50.435 0.402 57.277 1.00 8.61 ? 204 ASN B N 1 ATOM 4677 C CA . ASN B 1 204 ? 51.011 1.466 58.073 1.00 9.23 ? 204 ASN B CA 1 ATOM 4678 C C . ASN B 1 204 ? 52.509 1.262 58.088 1.00 9.56 ? 204 ASN B C 1 ATOM 4679 O O . ASN B 1 204 ? 53.028 0.488 57.293 1.00 9.85 ? 204 ASN B O 1 ATOM 4680 C CB . ASN B 1 204 ? 50.371 1.514 59.463 1.00 9.59 ? 204 ASN B CB 1 ATOM 4681 C CG . ASN B 1 204 ? 50.416 0.205 60.199 1.00 9.17 ? 204 ASN B CG 1 ATOM 4682 O OD1 . ASN B 1 204 ? 51.443 -0.475 60.200 1.00 9.73 ? 204 ASN B OD1 1 ATOM 4683 N ND2 . ASN B 1 204 ? 49.310 -0.126 60.900 1.00 9.44 ? 204 ASN B ND2 1 ATOM 4684 N N . SER B 1 205 ? 53.238 1.922 58.988 1.00 9.96 ? 205 SER B N 1 ATOM 4685 C CA . SER B 1 205 ? 54.685 1.757 59.022 1.00 9.71 ? 205 SER B CA 1 ATOM 4686 C C . SER B 1 205 ? 55.115 0.426 59.669 1.00 9.85 ? 205 SER B C 1 ATOM 4687 O O . SER B 1 205 ? 56.295 0.096 59.679 1.00 10.35 ? 205 SER B O 1 ATOM 4688 C CB . SER B 1 205 ? 55.359 2.923 59.732 1.00 10.75 ? 205 SER B CB 1 ATOM 4689 O OG . SER B 1 205 ? 55.094 2.941 61.128 1.00 10.40 ? 205 SER B OG 1 ATOM 4690 N N . ARG B 1 206 ? 54.162 -0.339 60.193 1.00 9.80 ? 206 ARG B N 1 ATOM 4691 C CA . ARG B 1 206 ? 54.448 -1.581 60.900 1.00 9.81 ? 206 ARG B CA 1 ATOM 4692 C C . ARG B 1 206 ? 54.059 -2.846 60.128 1.00 10.13 ? 206 ARG B C 1 ATOM 4693 O O . ARG B 1 206 ? 54.586 -3.919 60.405 1.00 10.51 ? 206 ARG B O 1 ATOM 4694 C CB . ARG B 1 206 ? 53.764 -1.589 62.279 1.00 10.61 ? 206 ARG B CB 1 ATOM 4695 C CG . ARG B 1 206 ? 53.937 -0.281 63.069 1.00 10.99 ? 206 ARG B CG 1 ATOM 4696 C CD . ARG B 1 206 ? 55.389 0.166 63.320 1.00 11.53 ? 206 ARG B CD 1 ATOM 4697 N NE . ARG B 1 206 ? 56.199 -0.825 64.015 1.00 11.43 ? 206 ARG B NE 1 ATOM 4698 C CZ . ARG B 1 206 ? 56.196 -1.000 65.325 1.00 13.21 ? 206 ARG B CZ 1 ATOM 4699 N NH1 . ARG B 1 206 ? 55.395 -0.304 66.106 1.00 13.31 ? 206 ARG B NH1 1 ATOM 4700 N NH2 . ARG B 1 206 ? 56.981 -1.923 65.860 1.00 14.43 ? 206 ARG B NH2 1 ATOM 4701 N N . ALA B 1 207 ? 53.112 -2.741 59.199 1.00 9.34 ? 207 ALA B N 1 ATOM 4702 C CA . ALA B 1 207 ? 52.622 -3.888 58.437 1.00 9.94 ? 207 ALA B CA 1 ATOM 4703 C C . ALA B 1 207 ? 52.043 -3.455 57.118 1.00 9.71 ? 207 ALA B C 1 ATOM 4704 O O . ALA B 1 207 ? 51.515 -2.360 57.004 1.00 10.47 ? 207 ALA B O 1 ATOM 4705 C CB . ALA B 1 207 ? 51.588 -4.659 59.204 1.00 10.04 ? 207 ALA B CB 1 ATOM 4706 N N . SER B 1 208 ? 52.135 -4.349 56.138 1.00 10.12 ? 208 SER B N 1 ATOM 4707 C CA . SER B 1 208 ? 51.642 -4.133 54.775 1.00 9.83 ? 208 SER B CA 1 ATOM 4708 C C . SER B 1 208 ? 50.828 -5.338 54.342 1.00 9.93 ? 208 SER B C 1 ATOM 4709 O O . SER B 1 208 ? 51.309 -6.468 54.375 1.00 10.34 ? 208 SER B O 1 ATOM 4710 C CB . SER B 1 208 ? 52.825 -3.895 53.827 1.00 9.93 ? 208 SER B CB 1 ATOM 4711 O OG . SER B 1 208 ? 52.387 -3.823 52.480 1.00 10.49 ? 208 SER B OG 1 ATOM 4712 N N . HIS B 1 209 ? 49.588 -5.073 53.960 1.00 9.39 ? 209 HIS B N 1 ATOM 4713 C CA . HIS B 1 209 ? 48.583 -6.090 53.603 1.00 9.21 ? 209 HIS B CA 1 ATOM 4714 C C . HIS B 1 209 ? 48.037 -5.825 52.200 1.00 9.31 ? 209 HIS B C 1 ATOM 4715 O O . HIS B 1 209 ? 47.791 -4.671 51.824 1.00 9.27 ? 209 HIS B O 1 ATOM 4716 C CB . HIS B 1 209 ? 47.482 -5.957 54.657 1.00 9.75 ? 209 HIS B CB 1 ATOM 4717 C CG . HIS B 1 209 ? 46.281 -6.822 54.457 1.00 9.38 ? 209 HIS B CG 1 ATOM 4718 N ND1 . HIS B 1 209 ? 46.128 -8.015 55.123 1.00 11.65 ? 209 HIS B ND1 1 ATOM 4719 C CD2 . HIS B 1 209 ? 45.121 -6.597 53.800 1.00 10.95 ? 209 HIS B CD2 1 ATOM 4720 C CE1 . HIS B 1 209 ? 44.942 -8.522 54.823 1.00 12.49 ? 209 HIS B CE1 1 ATOM 4721 N NE2 . HIS B 1 209 ? 44.307 -7.674 54.035 1.00 13.02 ? 209 HIS B NE2 1 ATOM 4722 N N . VAL B 1 210 ? 47.886 -6.897 51.423 1.00 8.92 ? 210 VAL B N 1 ATOM 4723 C CA . VAL B 1 210 ? 47.248 -6.883 50.107 1.00 9.05 ? 210 VAL B CA 1 ATOM 4724 C C . VAL B 1 210 ? 46.125 -7.896 50.163 1.00 9.47 ? 210 VAL B C 1 ATOM 4725 O O . VAL B 1 210 ? 46.311 -8.977 50.729 1.00 9.25 ? 210 VAL B O 1 ATOM 4726 C CB . VAL B 1 210 ? 48.255 -7.307 49.002 1.00 9.37 ? 210 VAL B CB 1 ATOM 4727 C CG1 . VAL B 1 210 ? 47.632 -7.269 47.614 1.00 9.23 ? 210 VAL B CG1 1 ATOM 4728 C CG2 . VAL B 1 210 ? 49.519 -6.462 49.041 1.00 9.57 ? 210 VAL B CG2 1 ATOM 4729 N N . ALA B 1 211 ? 44.965 -7.598 49.576 1.00 9.21 ? 211 ALA B N 1 ATOM 4730 C CA . ALA B 1 211 ? 43.873 -8.584 49.573 1.00 9.30 ? 211 ALA B CA 1 ATOM 4731 C C . ALA B 1 211 ? 42.822 -8.361 48.512 1.00 9.70 ? 211 ALA B C 1 ATOM 4732 O O . ALA B 1 211 ? 42.100 -7.364 48.576 1.00 9.61 ? 211 ALA B O 1 ATOM 4733 C CB . ALA B 1 211 ? 43.176 -8.596 50.940 1.00 9.26 ? 211 ALA B CB 1 ATOM 4734 N N . PRO B 1 212 ? 42.646 -9.317 47.592 1.00 9.13 ? 212 PRO B N 1 ATOM 4735 C CA . PRO B 1 212 ? 41.458 -9.326 46.777 1.00 8.96 ? 212 PRO B CA 1 ATOM 4736 C C . PRO B 1 212 ? 40.246 -9.803 47.589 1.00 9.37 ? 212 PRO B C 1 ATOM 4737 O O . PRO B 1 212 ? 40.374 -10.698 48.427 1.00 9.71 ? 212 PRO B O 1 ATOM 4738 C CB . PRO B 1 212 ? 41.805 -10.307 45.670 1.00 9.03 ? 212 PRO B CB 1 ATOM 4739 C CG . PRO B 1 212 ? 42.760 -11.270 46.293 1.00 9.69 ? 212 PRO B CG 1 ATOM 4740 C CD . PRO B 1 212 ? 43.558 -10.420 47.229 1.00 9.61 ? 212 PRO B CD 1 ATOM 4741 N N . HIS B 1 213 ? 39.079 -9.197 47.346 1.00 9.50 ? 213 HIS B N 1 ATOM 4742 C CA . HIS B 1 213 ? 37.781 -9.581 47.943 1.00 9.96 ? 213 HIS B CA 1 ATOM 4743 C C . HIS B 1 213 ? 36.748 -9.752 46.827 1.00 10.61 ? 213 HIS B C 1 ATOM 4744 O O . HIS B 1 213 ? 36.376 -8.793 46.170 1.00 11.15 ? 213 HIS B O 1 ATOM 4745 C CB . HIS B 1 213 ? 37.225 -8.497 48.876 1.00 10.08 ? 213 HIS B CB 1 ATOM 4746 C CG . HIS B 1 213 ? 38.042 -8.172 50.101 1.00 10.03 ? 213 HIS B CG 1 ATOM 4747 N ND1 . HIS B 1 213 ? 37.594 -8.416 51.384 1.00 9.44 ? 213 HIS B ND1 1 ATOM 4748 C CD2 . HIS B 1 213 ? 39.224 -7.536 50.245 1.00 10.84 ? 213 HIS B CD2 1 ATOM 4749 C CE1 . HIS B 1 213 ? 38.479 -7.961 52.255 1.00 10.13 ? 213 HIS B CE1 1 ATOM 4750 N NE2 . HIS B 1 213 ? 39.489 -7.442 51.588 1.00 10.71 ? 213 HIS B NE2 1 ATOM 4751 N N . THR B 1 214 ? 36.281 -10.981 46.601 1.00 10.67 ? 214 THR B N 1 ATOM 4752 C CA . THR B 1 214 ? 35.298 -11.272 45.557 1.00 10.31 ? 214 THR B CA 1 ATOM 4753 C C . THR B 1 214 ? 33.871 -11.139 46.065 1.00 10.76 ? 214 THR B C 1 ATOM 4754 O O . THR B 1 214 ? 33.607 -11.255 47.270 1.00 11.40 ? 214 THR B O 1 ATOM 4755 C CB . THR B 1 214 ? 35.522 -12.679 45.021 1.00 10.21 ? 214 THR B CB 1 ATOM 4756 O OG1 . THR B 1 214 ? 35.608 -13.591 46.135 1.00 11.40 ? 214 THR B OG1 1 ATOM 4757 C CG2 . THR B 1 214 ? 36.847 -12.757 44.246 1.00 10.40 ? 214 THR B CG2 1 ATOM 4758 N N . CYS B 1 215 ? 32.963 -10.860 45.135 1.00 10.88 ? 215 CYS B N 1 ATOM 4759 C CA . CYS B 1 215 ? 31.521 -10.998 45.318 1.00 11.10 ? 215 CYS B CA 1 ATOM 4760 C C . CYS B 1 215 ? 30.979 -11.763 44.129 1.00 11.07 ? 215 CYS B C 1 ATOM 4761 O O . CYS B 1 215 ? 31.546 -11.672 43.051 1.00 12.32 ? 215 CYS B O 1 ATOM 4762 C CB . CYS B 1 215 ? 30.840 -9.624 45.371 1.00 10.84 ? 215 CYS B CB 1 ATOM 4763 S SG . CYS B 1 215 ? 31.514 -8.503 46.654 1.00 11.77 ? 215 CYS B SG 1 ATOM 4764 N N . ASN B 1 216 ? 29.836 -12.425 44.305 1.00 11.88 ? 216 ASN B N 1 ATOM 4765 C CA . ASN B 1 216 ? 29.218 -13.167 43.196 1.00 12.32 ? 216 ASN B CA 1 ATOM 4766 C C . ASN B 1 216 ? 28.216 -12.322 42.403 1.00 13.26 ? 216 ASN B C 1 ATOM 4767 O O . ASN B 1 216 ? 27.352 -12.861 41.704 1.00 14.98 ? 216 ASN B O 1 ATOM 4768 C CB . ASN B 1 216 ? 28.567 -14.497 43.682 1.00 11.91 ? 216 ASN B CB 1 ATOM 4769 C CG . ASN B 1 216 ? 27.406 -14.289 44.643 1.00 12.41 ? 216 ASN B CG 1 ATOM 4770 O OD1 . ASN B 1 216 ? 26.924 -13.167 44.832 1.00 14.35 ? 216 ASN B OD1 1 ATOM 4771 N ND2 . ASN B 1 216 ? 26.951 -15.386 45.268 1.00 13.63 ? 216 ASN B ND2 1 ATOM 4772 N N . LYS B 1 217 ? 28.319 -11.002 42.545 1.00 12.99 ? 217 LYS B N 1 ATOM 4773 C CA . LYS B 1 217 ? 27.514 -10.011 41.838 1.00 13.51 ? 217 LYS B CA 1 ATOM 4774 C C . LYS B 1 217 ? 28.448 -9.019 41.150 1.00 14.14 ? 217 LYS B C 1 ATOM 4775 O O . LYS B 1 217 ? 29.541 -8.739 41.673 1.00 15.95 ? 217 LYS B O 1 ATOM 4776 C CB . LYS B 1 217 ? 26.628 -9.255 42.826 1.00 15.72 ? 217 LYS B CB 1 ATOM 4777 C CG . LYS B 1 217 ? 25.716 -10.105 43.640 1.00 16.98 ? 217 LYS B CG 1 ATOM 4778 C CD . LYS B 1 217 ? 24.642 -10.709 42.778 1.00 18.63 ? 217 LYS B CD 1 ATOM 4779 C CE . LYS B 1 217 ? 23.657 -11.536 43.588 1.00 20.14 ? 217 LYS B CE 1 ATOM 4780 N NZ . LYS B 1 217 ? 24.173 -12.895 44.013 1.00 23.92 ? 217 LYS B NZ 1 ATOM 4781 N N . LYS B 1 218 ? 28.038 -8.497 39.990 1.00 13.38 ? 218 LYS B N 1 ATOM 4782 C CA . LYS B 1 218 ? 28.790 -7.486 39.235 1.00 13.19 ? 218 LYS B CA 1 ATOM 4783 C C . LYS B 1 218 ? 28.353 -6.080 39.612 1.00 12.85 ? 218 LYS B C 1 ATOM 4784 O O . LYS B 1 218 ? 27.171 -5.796 39.776 1.00 13.47 ? 218 LYS B O 1 ATOM 4785 C CB . LYS B 1 218 ? 28.595 -7.667 37.723 1.00 13.68 ? 218 LYS B CB 1 ATOM 4786 C CG . LYS B 1 218 ? 28.922 -9.046 37.195 1.00 13.97 ? 218 LYS B CG 1 ATOM 4787 C CD . LYS B 1 218 ? 28.804 -9.146 35.680 1.00 14.79 ? 218 LYS B CD 1 ATOM 4788 C CE . LYS B 1 218 ? 29.188 -10.520 35.190 1.00 16.46 ? 218 LYS B CE 1 ATOM 4789 N NZ . LYS B 1 218 ? 28.913 -10.737 33.741 1.00 17.99 ? 218 LYS B NZ 1 ATOM 4790 N N . GLY B 1 219 ? 29.333 -5.202 39.762 1.00 12.61 ? 219 GLY B N 1 ATOM 4791 C CA . GLY B 1 219 ? 29.054 -3.808 40.123 1.00 12.62 ? 219 GLY B CA 1 ATOM 4792 C C . GLY B 1 219 ? 28.454 -3.699 41.494 1.00 12.78 ? 219 GLY B C 1 ATOM 4793 O O . GLY B 1 219 ? 28.607 -4.585 42.331 1.00 13.29 ? 219 GLY B O 1 ATOM 4794 N N . LEU B 1 220 ? 27.748 -2.606 41.725 1.00 11.47 ? 220 LEU B N 1 ATOM 4795 C CA . LEU B 1 220 ? 27.136 -2.363 43.022 1.00 11.95 ? 220 LEU B CA 1 ATOM 4796 C C . LEU B 1 220 ? 25.851 -3.180 43.120 1.00 12.32 ? 220 LEU B C 1 ATOM 4797 O O . LEU B 1 220 ? 24.941 -3.042 42.291 1.00 12.87 ? 220 LEU B O 1 ATOM 4798 C CB . LEU B 1 220 ? 26.860 -0.887 43.228 1.00 11.49 ? 220 LEU B CB 1 ATOM 4799 C CG . LEU B 1 220 ? 26.504 -0.447 44.656 1.00 12.03 ? 220 LEU B CG 1 ATOM 4800 C CD1 . LEU B 1 220 ? 26.839 1.048 44.872 1.00 12.75 ? 220 LEU B CD1 1 ATOM 4801 C CD2 . LEU B 1 220 ? 25.054 -0.732 45.038 1.00 12.89 ? 220 LEU B CD2 1 ATOM 4802 N N . TYR B 1 221 ? 25.772 -3.999 44.151 1.00 11.92 ? 221 TYR B N 1 ATOM 4803 C CA . TYR B 1 221 ? 24.609 -4.801 44.430 1.00 12.17 ? 221 TYR B CA 1 ATOM 4804 C C . TYR B 1 221 ? 24.033 -4.414 45.774 1.00 12.34 ? 221 TYR B C 1 ATOM 4805 O O . TYR B 1 221 ? 24.748 -4.397 46.781 1.00 11.23 ? 221 TYR B O 1 ATOM 4806 C CB . TYR B 1 221 ? 25.005 -6.287 44.446 1.00 13.01 ? 221 TYR B CB 1 ATOM 4807 C CG . TYR B 1 221 ? 23.831 -7.202 44.743 1.00 13.22 ? 221 TYR B CG 1 ATOM 4808 C CD1 . TYR B 1 221 ? 22.889 -7.493 43.765 1.00 14.66 ? 221 TYR B CD1 1 ATOM 4809 C CD2 . TYR B 1 221 ? 23.640 -7.751 46.008 1.00 13.38 ? 221 TYR B CD2 1 ATOM 4810 C CE1 . TYR B 1 221 ? 21.798 -8.324 44.040 1.00 16.18 ? 221 TYR B CE1 1 ATOM 4811 C CE2 . TYR B 1 221 ? 22.536 -8.566 46.296 1.00 14.34 ? 221 TYR B CE2 1 ATOM 4812 C CZ . TYR B 1 221 ? 21.632 -8.841 45.301 1.00 14.83 ? 221 TYR B CZ 1 ATOM 4813 O OH . TYR B 1 221 ? 20.550 -9.661 45.555 1.00 19.50 ? 221 TYR B OH 1 ATOM 4814 N N . LEU B 1 222 ? 22.728 -4.126 45.814 1.00 12.78 ? 222 LEU B N 1 ATOM 4815 C CA . LEU B 1 222 ? 22.052 -3.782 47.067 1.00 12.73 ? 222 LEU B CA 1 ATOM 4816 C C . LEU B 1 222 ? 21.548 -5.056 47.728 1.00 13.20 ? 222 LEU B C 1 ATOM 4817 O O . LEU B 1 222 ? 20.592 -5.687 47.257 1.00 13.97 ? 222 LEU B O 1 ATOM 4818 C CB . LEU B 1 222 ? 20.864 -2.827 46.843 1.00 13.12 ? 222 LEU B CB 1 ATOM 4819 C CG . LEU B 1 222 ? 21.214 -1.382 46.459 1.00 13.97 ? 222 LEU B CG 1 ATOM 4820 C CD1 . LEU B 1 222 ? 21.474 -1.255 44.968 1.00 15.59 ? 222 LEU B CD1 1 ATOM 4821 C CD2 . LEU B 1 222 ? 20.115 -0.418 46.881 1.00 14.87 ? 222 LEU B CD2 1 ATOM 4822 N N . CYS B 1 223 ? 22.178 -5.423 48.831 1.00 13.09 ? 223 CYS B N 1 ATOM 4823 C CA . CYS B 1 223 ? 21.889 -6.687 49.498 1.00 13.43 ? 223 CYS B CA 1 ATOM 4824 C C . CYS B 1 223 ? 20.812 -6.530 50.547 1.00 14.03 ? 223 CYS B C 1 ATOM 4825 O O . CYS B 1 223 ? 20.676 -5.486 51.185 1.00 14.05 ? 223 CYS B O 1 ATOM 4826 C CB . CYS B 1 223 ? 23.180 -7.252 50.129 1.00 12.35 ? 223 CYS B CB 1 ATOM 4827 S SG . CYS B 1 223 ? 23.910 -6.241 51.456 1.00 12.33 ? 223 CYS B SG 1 ATOM 4828 N N . GLU B 1 224 ? 20.061 -7.609 50.768 1.00 14.56 ? 224 GLU B N 1 ATOM 4829 C CA . GLU B 1 224 ? 19.117 -7.619 51.879 1.00 16.52 ? 224 GLU B CA 1 ATOM 4830 C C . GLU B 1 224 ? 19.338 -8.838 52.763 1.00 15.95 ? 224 GLU B C 1 ATOM 4831 O O . GLU B 1 224 ? 19.742 -9.899 52.275 1.00 15.43 ? 224 GLU B O 1 ATOM 4832 C CB . GLU B 1 224 ? 17.687 -7.538 51.360 1.00 17.98 ? 224 GLU B CB 1 ATOM 4833 C CG . GLU B 1 224 ? 17.199 -8.704 50.550 1.00 20.98 ? 224 GLU B CG 1 ATOM 4834 C CD . GLU B 1 224 ? 15.814 -8.450 49.974 1.00 22.70 ? 224 GLU B CD 1 ATOM 4835 O OE1 . GLU B 1 224 ? 15.093 -7.631 50.560 1.00 28.18 ? 224 GLU B OE1 1 ATOM 4836 O OE2 . GLU B 1 224 ? 15.461 -9.054 48.935 1.00 30.44 ? 224 GLU B OE2 1 ATOM 4837 N N . GLY B 1 225 ? 19.132 -8.661 54.060 1.00 16.42 ? 225 GLY B N 1 ATOM 4838 C CA . GLY B 1 225 ? 19.168 -9.779 54.975 1.00 17.43 ? 225 GLY B CA 1 ATOM 4839 C C . GLY B 1 225 ? 20.493 -10.503 54.948 1.00 17.60 ? 225 GLY B C 1 ATOM 4840 O O . GLY B 1 225 ? 21.563 -9.890 55.010 1.00 17.78 ? 225 GLY B O 1 ATOM 4841 N N . GLU B 1 226 ? 20.417 -11.819 54.830 1.00 18.01 ? 226 GLU B N 1 ATOM 4842 C CA . GLU B 1 226 ? 21.577 -12.678 54.839 1.00 18.41 ? 226 GLU B CA 1 ATOM 4843 C C . GLU B 1 226 ? 22.558 -12.423 53.691 1.00 16.52 ? 226 GLU B C 1 ATOM 4844 O O . GLU B 1 226 ? 23.722 -12.797 53.787 1.00 16.28 ? 226 GLU B O 1 ATOM 4845 C CB . GLU B 1 226 ? 21.144 -14.159 54.802 1.00 19.56 ? 226 GLU B CB 1 ATOM 4846 C CG . GLU B 1 226 ? 20.535 -14.707 56.087 1.00 24.08 ? 226 GLU B CG 1 ATOM 4847 C CD . GLU B 1 226 ? 20.040 -16.144 55.929 1.00 25.10 ? 226 GLU B CD 1 ATOM 4848 O OE1 . GLU B 1 226 ? 20.329 -16.777 54.894 1.00 31.30 ? 226 GLU B OE1 1 ATOM 4849 O OE2 . GLU B 1 226 ? 19.359 -16.637 56.852 1.00 33.07 ? 226 GLU B OE2 1 ATOM 4850 N N . GLU B 1 227 ? 22.097 -11.805 52.605 1.00 15.41 ? 227 GLU B N 1 ATOM 4851 C CA . GLU B 1 227 ? 23.005 -11.493 51.504 1.00 15.21 ? 227 GLU B CA 1 ATOM 4852 C C . GLU B 1 227 ? 24.140 -10.570 51.960 1.00 14.56 ? 227 GLU B C 1 ATOM 4853 O O . GLU B 1 227 ? 25.225 -10.606 51.380 1.00 13.48 ? 227 GLU B O 1 ATOM 4854 C CB . GLU B 1 227 ? 22.269 -10.827 50.349 1.00 14.90 ? 227 GLU B CB 1 ATOM 4855 C CG . GLU B 1 227 ? 21.243 -11.699 49.650 1.00 17.41 ? 227 GLU B CG 1 ATOM 4856 C CD . GLU B 1 227 ? 20.403 -10.923 48.672 1.00 18.75 ? 227 GLU B CD 1 ATOM 4857 O OE1 . GLU B 1 227 ? 20.376 -9.693 48.714 1.00 17.32 ? 227 GLU B OE1 1 ATOM 4858 O OE2 . GLU B 1 227 ? 19.703 -11.553 47.867 1.00 28.45 ? 227 GLU B OE2 1 ATOM 4859 N N . CYS B 1 228 ? 23.890 -9.745 52.967 1.00 12.90 ? 228 CYS B N 1 ATOM 4860 C CA . CYS B 1 228 ? 24.896 -8.791 53.482 1.00 12.82 ? 228 CYS B CA 1 ATOM 4861 C C . CYS B 1 228 ? 25.844 -9.387 54.512 1.00 13.24 ? 228 CYS B C 1 ATOM 4862 O O . CYS B 1 228 ? 26.801 -8.730 54.914 1.00 13.67 ? 228 CYS B O 1 ATOM 4863 C CB . CYS B 1 228 ? 24.221 -7.563 54.129 1.00 13.00 ? 228 CYS B CB 1 ATOM 4864 S SG . CYS B 1 228 ? 22.897 -6.785 53.155 1.00 13.71 ? 228 CYS B SG 1 ATOM 4865 N N . ALA B 1 229 ? 25.552 -10.607 54.967 1.00 13.54 ? 229 ALA B N 1 ATOM 4866 C CA . ALA B 1 229 ? 26.289 -11.228 56.067 1.00 14.17 ? 229 ALA B CA 1 ATOM 4867 C C . ALA B 1 229 ? 27.521 -11.997 55.600 1.00 14.13 ? 229 ALA B C 1 ATOM 4868 O O . ALA B 1 229 ? 27.809 -12.072 54.397 1.00 14.08 ? 229 ALA B O 1 ATOM 4869 C CB . ALA B 1 229 ? 25.349 -12.130 56.865 1.00 15.93 ? 229 ALA B CB 1 ATOM 4870 N N . PHE B 1 230 ? 28.247 -12.578 56.557 1.00 13.88 ? 230 PHE B N 1 ATOM 4871 C CA . PHE B 1 230 ? 29.487 -13.308 56.210 1.00 13.62 ? 230 PHE B CA 1 ATOM 4872 C C . PHE B 1 230 ? 29.250 -14.407 55.169 1.00 13.73 ? 230 PHE B C 1 ATOM 4873 O O . PHE B 1 230 ? 30.058 -14.618 54.251 1.00 13.46 ? 230 PHE B O 1 ATOM 4874 C CB . PHE B 1 230 ? 30.125 -13.943 57.445 1.00 13.74 ? 230 PHE B CB 1 ATOM 4875 C CG . PHE B 1 230 ? 31.509 -14.488 57.196 1.00 13.88 ? 230 PHE B CG 1 ATOM 4876 C CD1 . PHE B 1 230 ? 32.612 -13.659 57.305 1.00 15.35 ? 230 PHE B CD1 1 ATOM 4877 C CD2 . PHE B 1 230 ? 31.689 -15.803 56.790 1.00 15.29 ? 230 PHE B CD2 1 ATOM 4878 C CE1 . PHE B 1 230 ? 33.875 -14.140 57.061 1.00 14.93 ? 230 PHE B CE1 1 ATOM 4879 C CE2 . PHE B 1 230 ? 32.969 -16.285 56.549 1.00 14.54 ? 230 PHE B CE2 1 ATOM 4880 C CZ . PHE B 1 230 ? 34.047 -15.442 56.659 1.00 15.32 ? 230 PHE B CZ 1 ATOM 4881 N N . GLU B 1 231 ? 28.114 -15.090 55.290 1.00 14.19 ? 231 GLU B N 1 ATOM 4882 C CA . GLU B 1 231 ? 27.743 -16.153 54.384 1.00 14.57 ? 231 GLU B CA 1 ATOM 4883 C C . GLU B 1 231 ? 27.000 -15.693 53.127 1.00 14.93 ? 231 GLU B C 1 ATOM 4884 O O . GLU B 1 231 ? 26.472 -16.498 52.372 1.00 15.99 ? 231 GLU B O 1 ATOM 4885 C CB A GLU B 1 231 ? 26.973 -17.277 55.073 0.50 14.88 ? 231 GLU B CB 1 ATOM 4886 C CB B GLU B 1 231 ? 26.881 -17.147 55.199 0.50 14.96 ? 231 GLU B CB 1 ATOM 4887 C CG A GLU B 1 231 ? 27.914 -18.254 55.753 0.50 14.70 ? 231 GLU B CG 1 ATOM 4888 C CG B GLU B 1 231 ? 25.531 -16.620 55.718 0.50 15.56 ? 231 GLU B CG 1 ATOM 4889 C CD A GLU B 1 231 ? 28.550 -19.280 54.829 0.50 16.38 ? 231 GLU B CD 1 ATOM 4890 C CD B GLU B 1 231 ? 25.517 -15.894 57.081 0.50 15.98 ? 231 GLU B CD 1 ATOM 4891 O OE1 A GLU B 1 231 ? 28.790 -19.029 53.624 0.50 16.97 ? 231 GLU B OE1 1 ATOM 4892 O OE1 B GLU B 1 231 ? 26.598 -15.476 57.658 0.50 9.07 ? 231 GLU B OE1 1 ATOM 4893 O OE2 A GLU B 1 231 ? 28.802 -20.379 55.328 0.50 15.46 ? 231 GLU B OE2 1 ATOM 4894 O OE2 B GLU B 1 231 ? 24.342 -15.724 57.574 0.50 16.47 ? 231 GLU B OE2 1 ATOM 4895 N N . GLY B 1 232 ? 27.064 -14.392 52.851 1.00 14.04 ? 232 GLY B N 1 ATOM 4896 C CA . GLY B 1 232 ? 26.317 -13.780 51.772 1.00 13.37 ? 232 GLY B CA 1 ATOM 4897 C C . GLY B 1 232 ? 27.050 -13.640 50.461 1.00 12.60 ? 232 GLY B C 1 ATOM 4898 O O . GLY B 1 232 ? 27.800 -14.514 50.069 1.00 14.44 ? 232 GLY B O 1 ATOM 4899 N N . VAL B 1 233 ? 26.801 -12.534 49.766 1.00 12.45 ? 233 VAL B N 1 ATOM 4900 C CA . VAL B 1 233 ? 27.237 -12.345 48.390 1.00 12.51 ? 233 VAL B CA 1 ATOM 4901 C C . VAL B 1 233 ? 28.671 -11.813 48.215 1.00 12.07 ? 233 VAL B C 1 ATOM 4902 O O . VAL B 1 233 ? 29.235 -11.879 47.112 1.00 11.46 ? 233 VAL B O 1 ATOM 4903 C CB . VAL B 1 233 ? 26.273 -11.399 47.594 1.00 12.22 ? 233 VAL B CB 1 ATOM 4904 C CG1 . VAL B 1 233 ? 24.831 -11.945 47.623 1.00 14.30 ? 233 VAL B CG1 1 ATOM 4905 C CG2 . VAL B 1 233 ? 26.354 -9.968 48.102 1.00 12.67 ? 233 VAL B CG2 1 ATOM 4906 N N . CYS B 1 234 ? 29.259 -11.310 49.304 1.00 11.41 ? 234 CYS B N 1 ATOM 4907 C CA . CYS B 1 234 ? 30.624 -10.775 49.257 1.00 10.76 ? 234 CYS B CA 1 ATOM 4908 C C . CYS B 1 234 ? 31.552 -11.411 50.294 1.00 11.16 ? 234 CYS B C 1 ATOM 4909 O O . CYS B 1 234 ? 31.108 -11.870 51.359 1.00 11.40 ? 234 CYS B O 1 ATOM 4910 C CB . CYS B 1 234 ? 30.610 -9.259 49.478 1.00 11.76 ? 234 CYS B CB 1 ATOM 4911 S SG . CYS B 1 234 ? 30.064 -8.264 48.075 1.00 11.69 ? 234 CYS B SG 1 ATOM 4912 N N . ASP B 1 235 ? 32.841 -11.385 49.964 1.00 11.01 ? 235 ASP B N 1 ATOM 4913 C CA . ASP B 1 235 ? 33.921 -11.928 50.774 1.00 10.59 ? 235 ASP B CA 1 ATOM 4914 C C . ASP B 1 235 ? 34.459 -10.828 51.693 1.00 10.28 ? 235 ASP B C 1 ATOM 4915 O O . ASP B 1 235 ? 35.249 -9.980 51.280 1.00 10.85 ? 235 ASP B O 1 ATOM 4916 C CB . ASP B 1 235 ? 34.978 -12.448 49.808 1.00 10.84 ? 235 ASP B CB 1 ATOM 4917 C CG . ASP B 1 235 ? 36.307 -12.739 50.445 1.00 10.40 ? 235 ASP B CG 1 ATOM 4918 O OD1 . ASP B 1 235 ? 36.378 -13.071 51.651 1.00 10.64 ? 235 ASP B OD1 1 ATOM 4919 O OD2 . ASP B 1 235 ? 37.344 -12.610 49.759 1.00 10.10 ? 235 ASP B OD2 1 ATOM 4920 N N . LYS B 1 236 ? 34.022 -10.824 52.950 1.00 10.19 ? 236 LYS B N 1 ATOM 4921 C CA . LYS B 1 236 ? 34.435 -9.801 53.937 1.00 10.55 ? 236 LYS B CA 1 ATOM 4922 C C . LYS B 1 236 ? 35.915 -9.899 54.290 1.00 10.89 ? 236 LYS B C 1 ATOM 4923 O O . LYS B 1 236 ? 36.600 -8.881 54.420 1.00 10.51 ? 236 LYS B O 1 ATOM 4924 C CB . LYS B 1 236 ? 33.578 -9.923 55.202 1.00 10.40 ? 236 LYS B CB 1 ATOM 4925 C CG . LYS B 1 236 ? 32.110 -9.590 55.001 1.00 11.04 ? 236 LYS B CG 1 ATOM 4926 C CD . LYS B 1 236 ? 31.345 -9.642 56.322 1.00 11.21 ? 236 LYS B CD 1 ATOM 4927 C CE . LYS B 1 236 ? 29.840 -9.467 56.174 1.00 12.04 ? 236 LYS B CE 1 ATOM 4928 N NZ . LYS B 1 236 ? 29.472 -8.087 55.697 1.00 13.32 ? 236 LYS B NZ 1 ATOM 4929 N N . ASN B 1 237 ? 36.423 -11.128 54.426 1.00 10.91 ? 237 ASN B N 1 ATOM 4930 C CA . ASN B 1 237 ? 37.802 -11.289 54.858 1.00 11.24 ? 237 ASN B CA 1 ATOM 4931 C C . ASN B 1 237 ? 38.820 -10.985 53.798 1.00 11.41 ? 237 ASN B C 1 ATOM 4932 O O . ASN B 1 237 ? 39.853 -10.384 54.100 1.00 12.26 ? 237 ASN B O 1 ATOM 4933 C CB . ASN B 1 237 ? 38.039 -12.719 55.324 1.00 13.03 ? 237 ASN B CB 1 ATOM 4934 C CG . ASN B 1 237 ? 37.441 -13.013 56.676 1.00 15.64 ? 237 ASN B CG 1 ATOM 4935 O OD1 . ASN B 1 237 ? 36.880 -12.144 57.316 1.00 16.91 ? 237 ASN B OD1 1 ATOM 4936 N ND2 . ASN B 1 237 ? 37.565 -14.280 57.112 1.00 17.60 ? 237 ASN B ND2 1 ATOM 4937 N N . GLY B 1 238 ? 38.525 -11.364 52.561 1.00 10.86 ? 238 GLY B N 1 ATOM 4938 C CA . GLY B 1 238 ? 39.518 -11.283 51.487 1.00 10.78 ? 238 GLY B CA 1 ATOM 4939 C C . GLY B 1 238 ? 40.548 -12.393 51.585 1.00 11.26 ? 238 GLY B C 1 ATOM 4940 O O . GLY B 1 238 ? 40.633 -13.130 52.599 1.00 13.56 ? 238 GLY B O 1 ATOM 4941 N N . CYS B 1 239 ? 41.350 -12.517 50.539 1.00 10.17 ? 239 CYS B N 1 ATOM 4942 C CA . CYS B 1 239 ? 42.506 -13.400 50.573 1.00 10.24 ? 239 CYS B CA 1 ATOM 4943 C C . CYS B 1 239 ? 43.737 -12.587 50.942 1.00 10.12 ? 239 CYS B C 1 ATOM 4944 O O . CYS B 1 239 ? 44.340 -11.916 50.105 1.00 10.71 ? 239 CYS B O 1 ATOM 4945 C CB . CYS B 1 239 ? 42.704 -14.084 49.238 1.00 10.07 ? 239 CYS B CB 1 ATOM 4946 S SG . CYS B 1 239 ? 44.191 -15.104 49.209 1.00 11.74 ? 239 CYS B SG 1 ATOM 4947 N N . GLY B 1 240 ? 44.090 -12.616 52.214 1.00 10.51 ? 240 GLY B N 1 ATOM 4948 C CA . GLY B 1 240 ? 45.109 -11.714 52.714 1.00 9.85 ? 240 GLY B CA 1 ATOM 4949 C C . GLY B 1 240 ? 46.524 -12.143 52.443 1.00 9.08 ? 240 GLY B C 1 ATOM 4950 O O . GLY B 1 240 ? 46.874 -13.319 52.586 1.00 10.46 ? 240 GLY B O 1 ATOM 4951 N N . TRP B 1 241 ? 47.366 -11.158 52.160 1.00 9.18 ? 241 TRP B N 1 ATOM 4952 C CA . TRP B 1 241 ? 48.792 -11.367 51.900 1.00 9.74 ? 241 TRP B CA 1 ATOM 4953 C C . TRP B 1 241 ? 49.552 -10.364 52.760 1.00 9.99 ? 241 TRP B C 1 ATOM 4954 O O . TRP B 1 241 ? 49.466 -9.159 52.518 1.00 9.75 ? 241 TRP B O 1 ATOM 4955 C CB . TRP B 1 241 ? 49.057 -11.125 50.419 1.00 10.17 ? 241 TRP B CB 1 ATOM 4956 C CG . TRP B 1 241 ? 50.462 -11.225 49.924 1.00 9.34 ? 241 TRP B CG 1 ATOM 4957 C CD1 . TRP B 1 241 ? 51.326 -10.182 49.599 1.00 10.12 ? 241 TRP B CD1 1 ATOM 4958 C CD2 . TRP B 1 241 ? 51.183 -12.433 49.649 1.00 9.83 ? 241 TRP B CD2 1 ATOM 4959 N NE1 . TRP B 1 241 ? 52.520 -10.687 49.128 1.00 11.18 ? 241 TRP B NE1 1 ATOM 4960 C CE2 . TRP B 1 241 ? 52.451 -12.065 49.143 1.00 10.14 ? 241 TRP B CE2 1 ATOM 4961 C CE3 . TRP B 1 241 ? 50.872 -13.792 49.752 1.00 10.97 ? 241 TRP B CE3 1 ATOM 4962 C CZ2 . TRP B 1 241 ? 53.405 -13.006 48.786 1.00 11.42 ? 241 TRP B CZ2 1 ATOM 4963 C CZ3 . TRP B 1 241 ? 51.830 -14.707 49.394 1.00 11.65 ? 241 TRP B CZ3 1 ATOM 4964 C CH2 . TRP B 1 241 ? 53.076 -14.313 48.914 1.00 11.56 ? 241 TRP B CH2 1 ATOM 4965 N N . ASN B 1 242 ? 50.289 -10.869 53.746 1.00 9.90 ? 242 ASN B N 1 ATOM 4966 C CA . ASN B 1 242 ? 51.034 -10.059 54.707 1.00 9.76 ? 242 ASN B CA 1 ATOM 4967 C C . ASN B 1 242 ? 52.245 -10.881 55.135 1.00 10.24 ? 242 ASN B C 1 ATOM 4968 O O . ASN B 1 242 ? 52.075 -12.007 55.588 1.00 10.37 ? 242 ASN B O 1 ATOM 4969 C CB . ASN B 1 242 ? 50.127 -9.734 55.909 1.00 10.19 ? 242 ASN B CB 1 ATOM 4970 C CG . ASN B 1 242 ? 50.818 -8.976 57.024 1.00 10.29 ? 242 ASN B CG 1 ATOM 4971 O OD1 . ASN B 1 242 ? 52.055 -8.954 57.151 1.00 11.02 ? 242 ASN B OD1 1 ATOM 4972 N ND2 . ASN B 1 242 ? 50.004 -8.370 57.886 1.00 9.98 ? 242 ASN B ND2 1 ATOM 4973 N N . ASN B 1 243 ? 53.452 -10.361 54.940 1.00 9.75 ? 243 ASN B N 1 ATOM 4974 C CA . ASN B 1 243 ? 54.659 -11.119 55.294 1.00 9.94 ? 243 ASN B CA 1 ATOM 4975 C C . ASN B 1 243 ? 54.595 -11.761 56.677 1.00 10.07 ? 243 ASN B C 1 ATOM 4976 O O . ASN B 1 243 ? 55.035 -12.888 56.853 1.00 11.26 ? 243 ASN B O 1 ATOM 4977 C CB . ASN B 1 243 ? 55.949 -10.285 55.147 1.00 9.89 ? 243 ASN B CB 1 ATOM 4978 C CG . ASN B 1 243 ? 55.940 -8.986 55.897 1.00 9.58 ? 243 ASN B CG 1 ATOM 4979 O OD1 . ASN B 1 243 ? 55.476 -7.953 55.386 1.00 10.89 ? 243 ASN B OD1 1 ATOM 4980 N ND2 . ASN B 1 243 ? 56.531 -8.987 57.072 1.00 11.22 ? 243 ASN B ND2 1 ATOM 4981 N N . TYR B 1 244 ? 54.066 -11.034 57.667 1.00 10.25 ? 244 TYR B N 1 ATOM 4982 C CA . TYR B 1 244 ? 54.001 -11.563 59.031 1.00 10.33 ? 244 TYR B CA 1 ATOM 4983 C C . TYR B 1 244 ? 53.118 -12.794 59.064 1.00 9.91 ? 244 TYR B C 1 ATOM 4984 O O . TYR B 1 244 ? 53.444 -13.763 59.748 1.00 10.59 ? 244 TYR B O 1 ATOM 4985 C CB . TYR B 1 244 ? 53.465 -10.526 60.018 1.00 10.78 ? 244 TYR B CB 1 ATOM 4986 C CG . TYR B 1 244 ? 54.490 -9.520 60.485 1.00 11.19 ? 244 TYR B CG 1 ATOM 4987 C CD1 . TYR B 1 244 ? 55.384 -9.852 61.503 1.00 11.26 ? 244 TYR B CD1 1 ATOM 4988 C CD2 . TYR B 1 244 ? 54.586 -8.248 59.932 1.00 11.07 ? 244 TYR B CD2 1 ATOM 4989 C CE1 . TYR B 1 244 ? 56.310 -8.976 61.948 1.00 12.07 ? 244 TYR B CE1 1 ATOM 4990 C CE2 . TYR B 1 244 ? 55.534 -7.335 60.391 1.00 12.00 ? 244 TYR B CE2 1 ATOM 4991 C CZ . TYR B 1 244 ? 56.397 -7.705 61.410 1.00 11.67 ? 244 TYR B CZ 1 ATOM 4992 O OH . TYR B 1 244 ? 57.355 -6.836 61.891 1.00 12.32 ? 244 TYR B OH 1 ATOM 4993 N N . ARG B 1 245 ? 51.984 -12.744 58.372 1.00 10.44 ? 245 ARG B N 1 ATOM 4994 C CA . ARG B 1 245 ? 51.052 -13.882 58.390 1.00 10.69 ? 245 ARG B CA 1 ATOM 4995 C C . ARG B 1 245 ? 51.637 -15.154 57.773 1.00 10.55 ? 245 ARG B C 1 ATOM 4996 O O . ARG B 1 245 ? 51.153 -16.268 58.055 1.00 10.68 ? 245 ARG B O 1 ATOM 4997 C CB . ARG B 1 245 ? 49.737 -13.567 57.666 1.00 10.89 ? 245 ARG B CB 1 ATOM 4998 C CG . ARG B 1 245 ? 48.843 -12.604 58.415 1.00 11.41 ? 245 ARG B CG 1 ATOM 4999 C CD . ARG B 1 245 ? 47.559 -12.320 57.649 1.00 11.00 ? 245 ARG B CD 1 ATOM 5000 N NE . ARG B 1 245 ? 46.685 -11.465 58.431 1.00 11.79 ? 245 ARG B NE 1 ATOM 5001 C CZ . ARG B 1 245 ? 45.848 -11.892 59.364 1.00 11.82 ? 245 ARG B CZ 1 ATOM 5002 N NH1 . ARG B 1 245 ? 45.728 -13.178 59.640 1.00 13.20 ? 245 ARG B NH1 1 ATOM 5003 N NH2 . ARG B 1 245 ? 45.122 -11.017 60.036 1.00 13.26 ? 245 ARG B NH2 1 ATOM 5004 N N . VAL B 1 246 ? 52.609 -14.997 56.883 1.00 11.46 ? 246 VAL B N 1 ATOM 5005 C CA . VAL B 1 246 ? 53.294 -16.130 56.266 1.00 11.32 ? 246 VAL B CA 1 ATOM 5006 C C . VAL B 1 246 ? 54.680 -16.372 56.866 1.00 11.47 ? 246 VAL B C 1 ATOM 5007 O O . VAL B 1 246 ? 55.511 -17.079 56.272 1.00 11.31 ? 246 VAL B O 1 ATOM 5008 C CB . VAL B 1 246 ? 53.296 -16.026 54.721 1.00 11.19 ? 246 VAL B CB 1 ATOM 5009 C CG1 . VAL B 1 246 ? 51.857 -15.961 54.195 1.00 11.62 ? 246 VAL B CG1 1 ATOM 5010 C CG2 . VAL B 1 246 ? 54.096 -14.843 54.213 1.00 10.97 ? 246 VAL B CG2 1 ATOM 5011 N N . ASN B 1 247 ? 54.913 -15.803 58.045 1.00 11.75 ? 247 ASN B N 1 ATOM 5012 C CA . ASN B 1 247 ? 56.092 -16.127 58.868 1.00 11.92 ? 247 ASN B CA 1 ATOM 5013 C C . ASN B 1 247 ? 57.401 -15.630 58.302 1.00 12.32 ? 247 ASN B C 1 ATOM 5014 O O . ASN B 1 247 ? 58.439 -16.316 58.352 1.00 12.29 ? 247 ASN B O 1 ATOM 5015 C CB . ASN B 1 247 ? 56.157 -17.628 59.115 1.00 12.19 ? 247 ASN B CB 1 ATOM 5016 C CG . ASN B 1 247 ? 57.132 -18.016 60.225 1.00 12.02 ? 247 ASN B CG 1 ATOM 5017 O OD1 . ASN B 1 247 ? 57.350 -17.273 61.195 1.00 12.17 ? 247 ASN B OD1 1 ATOM 5018 N ND2 . ASN B 1 247 ? 57.695 -19.218 60.079 1.00 13.12 ? 247 ASN B ND2 1 ATOM 5019 N N . VAL B 1 248 ? 57.356 -14.415 57.775 1.00 11.55 ? 248 VAL B N 1 ATOM 5020 C CA . VAL B 1 248 ? 58.559 -13.696 57.357 1.00 12.34 ? 248 VAL B CA 1 ATOM 5021 C C . VAL B 1 248 ? 58.550 -12.350 58.095 1.00 12.55 ? 248 VAL B C 1 ATOM 5022 O O . VAL B 1 248 ? 57.913 -11.384 57.665 1.00 13.88 ? 248 VAL B O 1 ATOM 5023 C CB . VAL B 1 248 ? 58.646 -13.496 55.816 1.00 12.06 ? 248 VAL B CB 1 ATOM 5024 C CG1 . VAL B 1 248 ? 59.941 -12.793 55.442 1.00 11.63 ? 248 VAL B CG1 1 ATOM 5025 C CG2 . VAL B 1 248 ? 58.537 -14.850 55.104 1.00 12.12 ? 248 VAL B CG2 1 ATOM 5026 N N . THR B 1 249 ? 59.217 -12.293 59.233 1.00 13.86 ? 249 THR B N 1 ATOM 5027 C CA . THR B 1 249 ? 59.028 -11.160 60.160 1.00 14.54 ? 249 THR B CA 1 ATOM 5028 C C . THR B 1 249 ? 59.984 -10.013 59.968 1.00 14.63 ? 249 THR B C 1 ATOM 5029 O O . THR B 1 249 ? 59.799 -8.970 60.620 1.00 14.99 ? 249 THR B O 1 ATOM 5030 C CB . THR B 1 249 ? 59.079 -11.618 61.617 1.00 15.11 ? 249 THR B CB 1 ATOM 5031 O OG1 . THR B 1 249 ? 60.369 -12.161 61.894 1.00 18.57 ? 249 THR B OG1 1 ATOM 5032 C CG2 . THR B 1 249 ? 58.086 -12.710 61.857 1.00 16.31 ? 249 THR B CG2 1 ATOM 5033 N N . ASP B 1 250 ? 60.949 -10.151 59.061 1.00 13.96 ? 250 ASP B N 1 ATOM 5034 C CA . ASP B 1 250 ? 61.995 -9.153 58.855 1.00 14.65 ? 250 ASP B CA 1 ATOM 5035 C C . ASP B 1 250 ? 61.912 -8.427 57.527 1.00 13.62 ? 250 ASP B C 1 ATOM 5036 O O . ASP B 1 250 ? 62.874 -7.796 57.096 1.00 14.72 ? 250 ASP B O 1 ATOM 5037 C CB . ASP B 1 250 ? 63.382 -9.795 59.025 1.00 15.34 ? 250 ASP B CB 1 ATOM 5038 C CG . ASP B 1 250 ? 63.677 -10.873 58.019 1.00 17.49 ? 250 ASP B CG 1 ATOM 5039 O OD1 . ASP B 1 250 ? 62.759 -11.312 57.321 1.00 18.76 ? 250 ASP B OD1 1 ATOM 5040 O OD2 . ASP B 1 250 ? 64.832 -11.380 57.890 1.00 22.68 ? 250 ASP B OD2 1 ATOM 5041 N N . TYR B 1 251 ? 60.749 -8.485 56.879 1.00 12.77 ? 251 TYR B N 1 ATOM 5042 C CA . TYR B 1 251 ? 60.593 -7.964 55.517 1.00 12.63 ? 251 TYR B CA 1 ATOM 5043 C C . TYR B 1 251 ? 60.249 -6.476 55.458 1.00 12.05 ? 251 TYR B C 1 ATOM 5044 O O . TYR B 1 251 ? 60.690 -5.788 54.560 1.00 12.38 ? 251 TYR B O 1 ATOM 5045 C CB . TYR B 1 251 ? 59.537 -8.763 54.756 1.00 11.89 ? 251 TYR B CB 1 ATOM 5046 C CG . TYR B 1 251 ? 59.465 -8.415 53.297 1.00 12.20 ? 251 TYR B CG 1 ATOM 5047 C CD1 . TYR B 1 251 ? 60.412 -8.900 52.418 1.00 12.54 ? 251 TYR B CD1 1 ATOM 5048 C CD2 . TYR B 1 251 ? 58.474 -7.584 52.798 1.00 11.78 ? 251 TYR B CD2 1 ATOM 5049 C CE1 . TYR B 1 251 ? 60.375 -8.580 51.088 1.00 12.03 ? 251 TYR B CE1 1 ATOM 5050 C CE2 . TYR B 1 251 ? 58.432 -7.254 51.481 1.00 11.73 ? 251 TYR B CE2 1 ATOM 5051 C CZ . TYR B 1 251 ? 59.389 -7.745 50.603 1.00 11.44 ? 251 TYR B CZ 1 ATOM 5052 O OH . TYR B 1 251 ? 59.318 -7.416 49.265 1.00 11.87 ? 251 TYR B OH 1 ATOM 5053 N N . TYR B 1 252 ? 59.444 -5.999 56.408 1.00 11.29 ? 252 TYR B N 1 ATOM 5054 C CA . TYR B 1 252 ? 58.813 -4.681 56.308 1.00 11.20 ? 252 TYR B CA 1 ATOM 5055 C C . TYR B 1 252 ? 58.640 -4.060 57.673 1.00 10.74 ? 252 TYR B C 1 ATOM 5056 O O . TYR B 1 252 ? 58.010 -4.661 58.534 1.00 11.15 ? 252 TYR B O 1 ATOM 5057 C CB . TYR B 1 252 ? 57.420 -4.869 55.670 1.00 10.79 ? 252 TYR B CB 1 ATOM 5058 C CG . TYR B 1 252 ? 56.590 -3.612 55.479 1.00 10.51 ? 252 TYR B CG 1 ATOM 5059 C CD1 . TYR B 1 252 ? 55.799 -3.112 56.495 1.00 10.14 ? 252 TYR B CD1 1 ATOM 5060 C CD2 . TYR B 1 252 ? 56.588 -2.926 54.267 1.00 10.40 ? 252 TYR B CD2 1 ATOM 5061 C CE1 . TYR B 1 252 ? 55.056 -1.964 56.320 1.00 9.72 ? 252 TYR B CE1 1 ATOM 5062 C CE2 . TYR B 1 252 ? 55.853 -1.780 54.093 1.00 9.72 ? 252 TYR B CE2 1 ATOM 5063 C CZ . TYR B 1 252 ? 55.077 -1.310 55.114 1.00 9.91 ? 252 TYR B CZ 1 ATOM 5064 O OH . TYR B 1 252 ? 54.341 -0.156 54.943 1.00 9.87 ? 252 TYR B OH 1 ATOM 5065 N N . GLY B 1 253 ? 59.191 -2.881 57.880 1.00 11.48 ? 253 GLY B N 1 ATOM 5066 C CA . GLY B 1 253 ? 59.073 -2.231 59.163 1.00 11.61 ? 253 GLY B CA 1 ATOM 5067 C C . GLY B 1 253 ? 59.985 -1.049 59.376 1.00 11.48 ? 253 GLY B C 1 ATOM 5068 O O . GLY B 1 253 ? 60.714 -0.611 58.462 1.00 11.62 ? 253 GLY B O 1 ATOM 5069 N N . ARG B 1 254 ? 59.923 -0.506 60.592 1.00 12.42 ? 254 ARG B N 1 ATOM 5070 C CA . ARG B 1 254 ? 60.645 0.724 60.950 1.00 12.68 ? 254 ARG B CA 1 ATOM 5071 C C . ARG B 1 254 ? 62.087 0.429 61.308 1.00 14.14 ? 254 ARG B C 1 ATOM 5072 O O . ARG B 1 254 ? 62.403 0.103 62.456 1.00 16.02 ? 254 ARG B O 1 ATOM 5073 C CB . ARG B 1 254 ? 59.959 1.436 62.126 1.00 12.62 ? 254 ARG B CB 1 ATOM 5074 C CG . ARG B 1 254 ? 58.532 1.884 61.863 1.00 12.07 ? 254 ARG B CG 1 ATOM 5075 C CD . ARG B 1 254 ? 57.891 2.565 63.035 1.00 12.58 ? 254 ARG B CD 1 ATOM 5076 N NE . ARG B 1 254 ? 58.461 3.881 63.319 1.00 12.22 ? 254 ARG B NE 1 ATOM 5077 C CZ . ARG B 1 254 ? 58.072 5.023 62.769 1.00 12.79 ? 254 ARG B CZ 1 ATOM 5078 N NH1 . ARG B 1 254 ? 57.101 5.068 61.865 1.00 12.46 ? 254 ARG B NH1 1 ATOM 5079 N NH2 . ARG B 1 254 ? 58.650 6.148 63.122 1.00 14.04 ? 254 ARG B NH2 1 ATOM 5080 N N . GLY B 1 255 ? 62.961 0.561 60.322 1.00 14.10 ? 255 GLY B N 1 ATOM 5081 C CA . GLY B 1 255 ? 64.399 0.436 60.582 1.00 15.97 ? 255 GLY B CA 1 ATOM 5082 C C . GLY B 1 255 ? 65.152 -0.287 59.501 1.00 16.72 ? 255 GLY B C 1 ATOM 5083 O O . GLY B 1 255 ? 64.586 -0.964 58.662 1.00 16.14 ? 255 GLY B O 1 ATOM 5084 N N . GLU B 1 256 ? 66.475 -0.168 59.565 1.00 18.41 ? 256 GLU B N 1 ATOM 5085 C CA . GLU B 1 256 ? 67.368 -0.760 58.585 1.00 19.74 ? 256 GLU B CA 1 ATOM 5086 C C . GLU B 1 256 ? 67.383 -2.294 58.629 1.00 19.08 ? 256 GLU B C 1 ATOM 5087 O O . GLU B 1 256 ? 67.830 -2.932 57.678 1.00 20.42 ? 256 GLU B O 1 ATOM 5088 C CB . GLU B 1 256 ? 68.797 -0.200 58.790 1.00 19.82 ? 256 GLU B CB 1 ATOM 5089 C CG . GLU B 1 256 ? 68.844 1.322 58.640 1.00 22.51 ? 256 GLU B CG 1 ATOM 5090 C CD . GLU B 1 256 ? 70.231 1.911 58.534 1.00 24.74 ? 256 GLU B CD 1 ATOM 5091 O OE1 . GLU B 1 256 ? 71.078 1.610 59.400 1.00 31.92 ? 256 GLU B OE1 1 ATOM 5092 O OE2 . GLU B 1 256 ? 70.437 2.712 57.604 1.00 29.89 ? 256 GLU B OE2 1 ATOM 5093 N N . GLU B 1 257 ? 66.871 -2.890 59.697 1.00 18.39 ? 257 GLU B N 1 ATOM 5094 C CA . GLU B 1 257 ? 66.823 -4.350 59.816 1.00 18.71 ? 257 GLU B CA 1 ATOM 5095 C C . GLU B 1 257 ? 65.698 -4.990 59.008 1.00 17.98 ? 257 GLU B C 1 ATOM 5096 O O . GLU B 1 257 ? 65.586 -6.224 58.948 1.00 18.98 ? 257 GLU B O 1 ATOM 5097 C CB . GLU B 1 257 ? 66.715 -4.784 61.279 1.00 19.96 ? 257 GLU B CB 1 ATOM 5098 C CG . GLU B 1 257 ? 65.384 -4.524 61.964 1.00 22.62 ? 257 GLU B CG 1 ATOM 5099 C CD . GLU B 1 257 ? 65.348 -3.232 62.763 1.00 25.32 ? 257 GLU B CD 1 ATOM 5100 O OE1 . GLU B 1 257 ? 65.959 -2.223 62.333 1.00 26.81 ? 257 GLU B OE1 1 ATOM 5101 O OE2 . GLU B 1 257 ? 64.694 -3.226 63.837 1.00 28.20 ? 257 GLU B OE2 1 ATOM 5102 N N . PHE B 1 258 ? 64.881 -4.158 58.371 1.00 15.90 ? 258 PHE B N 1 ATOM 5103 C CA . PHE B 1 258 ? 63.818 -4.656 57.506 1.00 15.36 ? 258 PHE B CA 1 ATOM 5104 C C . PHE B 1 258 ? 64.154 -4.428 56.046 1.00 14.80 ? 258 PHE B C 1 ATOM 5105 O O . PHE B 1 258 ? 64.776 -3.427 55.700 1.00 15.29 ? 258 PHE B O 1 ATOM 5106 C CB . PHE B 1 258 ? 62.529 -3.922 57.836 1.00 14.08 ? 258 PHE B CB 1 ATOM 5107 C CG . PHE B 1 258 ? 62.053 -4.138 59.235 1.00 13.19 ? 258 PHE B CG 1 ATOM 5108 C CD1 . PHE B 1 258 ? 61.321 -5.265 59.570 1.00 13.33 ? 258 PHE B CD1 1 ATOM 5109 C CD2 . PHE B 1 258 ? 62.314 -3.205 60.229 1.00 13.23 ? 258 PHE B CD2 1 ATOM 5110 C CE1 . PHE B 1 258 ? 60.884 -5.485 60.853 1.00 12.95 ? 258 PHE B CE1 1 ATOM 5111 C CE2 . PHE B 1 258 ? 61.847 -3.412 61.533 1.00 12.56 ? 258 PHE B CE2 1 ATOM 5112 C CZ . PHE B 1 258 ? 61.137 -4.556 61.843 1.00 13.03 ? 258 PHE B CZ 1 ATOM 5113 N N . LYS B 1 259 ? 63.740 -5.345 55.177 1.00 15.17 ? 259 LYS B N 1 ATOM 5114 C CA . LYS B 1 259 ? 64.040 -5.208 53.748 1.00 15.60 ? 259 LYS B CA 1 ATOM 5115 C C . LYS B 1 259 ? 63.441 -3.926 53.159 1.00 15.26 ? 259 LYS B C 1 ATOM 5116 O O . LYS B 1 259 ? 64.072 -3.256 52.359 1.00 15.97 ? 259 LYS B O 1 ATOM 5117 C CB . LYS B 1 259 ? 63.571 -6.437 52.958 1.00 17.05 ? 259 LYS B CB 1 ATOM 5118 C CG . LYS B 1 259 ? 64.111 -7.757 53.561 1.00 20.98 ? 259 LYS B CG 1 ATOM 5119 C CD . LYS B 1 259 ? 64.776 -8.674 52.586 1.00 23.97 ? 259 LYS B CD 1 ATOM 5120 C CE . LYS B 1 259 ? 65.859 -9.557 53.248 1.00 21.61 ? 259 LYS B CE 1 ATOM 5121 N NZ . LYS B 1 259 ? 65.567 -9.956 54.672 1.00 22.62 ? 259 LYS B NZ 1 ATOM 5122 N N . VAL B 1 260 ? 62.206 -3.613 53.549 1.00 13.74 ? 260 VAL B N 1 ATOM 5123 C CA . VAL B 1 260 ? 61.562 -2.340 53.218 1.00 13.74 ? 260 VAL B CA 1 ATOM 5124 C C . VAL B 1 260 ? 61.521 -1.543 54.517 1.00 12.43 ? 260 VAL B C 1 ATOM 5125 O O . VAL B 1 260 ? 60.897 -1.986 55.479 1.00 13.37 ? 260 VAL B O 1 ATOM 5126 C CB . VAL B 1 260 ? 60.134 -2.563 52.691 1.00 13.58 ? 260 VAL B CB 1 ATOM 5127 C CG1 . VAL B 1 260 ? 59.469 -1.229 52.327 1.00 12.83 ? 260 VAL B CG1 1 ATOM 5128 C CG2 . VAL B 1 260 ? 60.155 -3.480 51.493 1.00 14.24 ? 260 VAL B CG2 1 ATOM 5129 N N . ASN B 1 261 ? 62.261 -0.433 54.565 1.00 12.85 ? 261 ASN B N 1 ATOM 5130 C CA . ASN B 1 261 ? 62.410 0.401 55.769 1.00 12.39 ? 261 ASN B CA 1 ATOM 5131 C C . ASN B 1 261 ? 61.418 1.556 55.742 1.00 12.51 ? 261 ASN B C 1 ATOM 5132 O O . ASN B 1 261 ? 61.603 2.514 55.016 1.00 12.05 ? 261 ASN B O 1 ATOM 5133 C CB . ASN B 1 261 ? 63.861 0.898 55.844 1.00 13.28 ? 261 ASN B CB 1 ATOM 5134 C CG . ASN B 1 261 ? 64.104 1.834 56.992 1.00 14.26 ? 261 ASN B CG 1 ATOM 5135 O OD1 . ASN B 1 261 ? 63.235 2.064 57.810 1.00 14.21 ? 261 ASN B OD1 1 ATOM 5136 N ND2 . ASN B 1 261 ? 65.307 2.395 57.054 1.00 17.50 ? 261 ASN B ND2 1 ATOM 5137 N N . THR B 1 262 ? 60.375 1.471 56.558 1.00 11.88 ? 262 THR B N 1 ATOM 5138 C CA . THR B 1 262 ? 59.286 2.416 56.493 1.00 11.72 ? 262 THR B CA 1 ATOM 5139 C C . THR B 1 262 ? 59.617 3.746 57.169 1.00 11.52 ? 262 THR B C 1 ATOM 5140 O O . THR B 1 262 ? 58.788 4.638 57.223 1.00 11.49 ? 262 THR B O 1 ATOM 5141 C CB . THR B 1 262 ? 58.040 1.824 57.122 1.00 10.92 ? 262 THR B CB 1 ATOM 5142 O OG1 . THR B 1 262 ? 58.347 1.484 58.492 1.00 10.63 ? 262 THR B OG1 1 ATOM 5143 C CG2 . THR B 1 262 ? 57.602 0.522 56.426 1.00 11.47 ? 262 THR B CG2 1 ATOM 5144 N N . LEU B 1 263 ? 60.830 3.897 57.697 1.00 12.01 ? 263 LEU B N 1 ATOM 5145 C CA . LEU B 1 263 ? 61.300 5.212 58.124 1.00 12.42 ? 263 LEU B CA 1 ATOM 5146 C C . LEU B 1 263 ? 61.618 6.145 56.952 1.00 13.25 ? 263 LEU B C 1 ATOM 5147 O O . LEU B 1 263 ? 61.828 7.347 57.146 1.00 14.62 ? 263 LEU B O 1 ATOM 5148 C CB . LEU B 1 263 ? 62.548 5.076 59.010 1.00 13.45 ? 263 LEU B CB 1 ATOM 5149 C CG . LEU B 1 263 ? 62.334 4.332 60.313 1.00 13.55 ? 263 LEU B CG 1 ATOM 5150 C CD1 . LEU B 1 263 ? 63.676 4.203 61.005 1.00 15.59 ? 263 LEU B CD1 1 ATOM 5151 C CD2 . LEU B 1 263 ? 61.325 5.057 61.175 1.00 14.45 ? 263 LEU B CD2 1 ATOM 5152 N N . LYS B 1 264 ? 61.640 5.597 55.749 1.00 12.55 ? 264 LYS B N 1 ATOM 5153 C CA . LYS B 1 264 ? 61.913 6.355 54.521 1.00 14.31 ? 264 LYS B CA 1 ATOM 5154 C C . LYS B 1 264 ? 60.847 6.054 53.482 1.00 13.40 ? 264 LYS B C 1 ATOM 5155 O O . LYS B 1 264 ? 60.232 4.996 53.529 1.00 12.22 ? 264 LYS B O 1 ATOM 5156 C CB . LYS B 1 264 ? 63.296 5.988 53.946 1.00 15.43 ? 264 LYS B CB 1 ATOM 5157 C CG . LYS B 1 264 ? 64.429 6.186 54.946 1.00 17.50 ? 264 LYS B CG 1 ATOM 5158 C CD . LYS B 1 264 ? 65.770 5.911 54.347 1.00 18.99 ? 264 LYS B CD 1 ATOM 5159 C CE . LYS B 1 264 ? 66.006 4.495 54.017 1.00 22.51 ? 264 LYS B CE 1 ATOM 5160 N NZ . LYS B 1 264 ? 67.327 4.435 53.307 1.00 24.43 ? 264 LYS B NZ 1 ATOM 5161 N N . PRO B 1 265 ? 60.638 6.945 52.520 1.00 13.06 ? 265 PRO B N 1 ATOM 5162 C CA . PRO B 1 265 ? 59.672 6.652 51.459 1.00 13.03 ? 265 PRO B CA 1 ATOM 5163 C C . PRO B 1 265 ? 60.103 5.474 50.595 1.00 12.49 ? 265 PRO B C 1 ATOM 5164 O O . PRO B 1 265 ? 61.288 5.125 50.546 1.00 12.97 ? 265 PRO B O 1 ATOM 5165 C CB . PRO B 1 265 ? 59.623 7.953 50.653 1.00 13.24 ? 265 PRO B CB 1 ATOM 5166 C CG . PRO B 1 265 ? 60.144 9.007 51.595 1.00 15.42 ? 265 PRO B CG 1 ATOM 5167 C CD . PRO B 1 265 ? 61.197 8.306 52.406 1.00 13.75 ? 265 PRO B CD 1 ATOM 5168 N N . PHE B 1 266 ? 59.140 4.864 49.920 1.00 11.76 ? 266 PHE B N 1 ATOM 5169 C CA . PHE B 1 266 ? 59.423 3.742 49.035 1.00 11.12 ? 266 PHE B CA 1 ATOM 5170 C C . PHE B 1 266 ? 58.362 3.641 47.941 1.00 10.73 ? 266 PHE B C 1 ATOM 5171 O O . PHE B 1 266 ? 57.347 4.334 47.983 1.00 10.88 ? 266 PHE B O 1 ATOM 5172 C CB . PHE B 1 266 ? 59.563 2.411 49.802 1.00 11.34 ? 266 PHE B CB 1 ATOM 5173 C CG . PHE B 1 266 ? 58.421 2.113 50.736 1.00 10.79 ? 266 PHE B CG 1 ATOM 5174 C CD1 . PHE B 1 266 ? 58.375 2.634 52.015 1.00 12.03 ? 266 PHE B CD1 1 ATOM 5175 C CD2 . PHE B 1 266 ? 57.382 1.297 50.326 1.00 11.00 ? 266 PHE B CD2 1 ATOM 5176 C CE1 . PHE B 1 266 ? 57.303 2.353 52.877 1.00 10.99 ? 266 PHE B CE1 1 ATOM 5177 C CE2 . PHE B 1 266 ? 56.316 1.024 51.187 1.00 11.36 ? 266 PHE B CE2 1 ATOM 5178 C CZ . PHE B 1 266 ? 56.286 1.542 52.454 1.00 10.53 ? 266 PHE B CZ 1 ATOM 5179 N N . THR B 1 267 ? 58.620 2.766 46.971 1.00 10.59 ? 267 THR B N 1 ATOM 5180 C CA . THR B 1 267 ? 57.743 2.493 45.832 1.00 11.13 ? 267 THR B CA 1 ATOM 5181 C C . THR B 1 267 ? 57.123 1.109 45.984 1.00 10.14 ? 267 THR B C 1 ATOM 5182 O O . THR B 1 267 ? 57.767 0.150 46.427 1.00 10.66 ? 267 THR B O 1 ATOM 5183 C CB . THR B 1 267 ? 58.569 2.599 44.553 1.00 11.55 ? 267 THR B CB 1 ATOM 5184 O OG1 . THR B 1 267 ? 59.016 3.957 44.388 1.00 13.93 ? 267 THR B OG1 1 ATOM 5185 C CG2 . THR B 1 267 ? 57.760 2.286 43.320 1.00 12.55 ? 267 THR B CG2 1 ATOM 5186 N N . VAL B 1 268 ? 55.842 1.034 45.636 1.00 9.69 ? 268 VAL B N 1 ATOM 5187 C CA . VAL B 1 268 ? 54.988 -0.150 45.800 1.00 10.39 ? 268 VAL B CA 1 ATOM 5188 C C . VAL B 1 268 ? 54.476 -0.561 44.442 1.00 9.95 ? 268 VAL B C 1 ATOM 5189 O O . VAL B 1 268 ? 53.736 0.214 43.812 1.00 10.22 ? 268 VAL B O 1 ATOM 5190 C CB . VAL B 1 268 ? 53.816 0.184 46.738 1.00 9.39 ? 268 VAL B CB 1 ATOM 5191 C CG1 . VAL B 1 268 ? 52.951 -1.053 46.982 1.00 10.17 ? 268 VAL B CG1 1 ATOM 5192 C CG2 . VAL B 1 268 ? 54.329 0.770 48.072 1.00 10.32 ? 268 VAL B CG2 1 ATOM 5193 N N . VAL B 1 269 ? 54.907 -1.727 43.949 1.00 10.28 ? 269 VAL B N 1 ATOM 5194 C CA . VAL B 1 269 ? 54.498 -2.233 42.640 1.00 9.75 ? 269 VAL B CA 1 ATOM 5195 C C . VAL B 1 269 ? 53.546 -3.442 42.796 1.00 10.04 ? 269 VAL B C 1 ATOM 5196 O O . VAL B 1 269 ? 53.823 -4.344 43.595 1.00 9.68 ? 269 VAL B O 1 ATOM 5197 C CB . VAL B 1 269 ? 55.729 -2.697 41.819 1.00 10.42 ? 269 VAL B CB 1 ATOM 5198 C CG1 . VAL B 1 269 ? 55.268 -3.178 40.443 1.00 11.20 ? 269 VAL B CG1 1 ATOM 5199 C CG2 . VAL B 1 269 ? 56.744 -1.548 41.702 1.00 10.70 ? 269 VAL B CG2 1 ATOM 5200 N N . THR B 1 270 ? 52.433 -3.443 42.058 1.00 9.48 ? 270 THR B N 1 ATOM 5201 C CA . THR B 1 270 ? 51.467 -4.538 42.106 1.00 9.92 ? 270 THR B CA 1 ATOM 5202 C C . THR B 1 270 ? 51.095 -4.958 40.698 1.00 10.35 ? 270 THR B C 1 ATOM 5203 O O . THR B 1 270 ? 50.582 -4.168 39.922 1.00 10.40 ? 270 THR B O 1 ATOM 5204 C CB . THR B 1 270 ? 50.224 -4.124 42.860 1.00 9.97 ? 270 THR B CB 1 ATOM 5205 O OG1 . THR B 1 270 ? 50.609 -3.519 44.105 1.00 10.64 ? 270 THR B OG1 1 ATOM 5206 C CG2 . THR B 1 270 ? 49.369 -5.346 43.193 1.00 10.61 ? 270 THR B CG2 1 ATOM 5207 N N . GLN B 1 271 ? 51.427 -6.199 40.355 1.00 10.58 ? 271 GLN B N 1 ATOM 5208 C CA . GLN B 1 271 ? 51.171 -6.757 39.025 1.00 10.45 ? 271 GLN B CA 1 ATOM 5209 C C . GLN B 1 271 ? 50.034 -7.762 39.067 1.00 9.91 ? 271 GLN B C 1 ATOM 5210 O O . GLN B 1 271 ? 49.965 -8.604 39.988 1.00 11.32 ? 271 GLN B O 1 ATOM 5211 C CB . GLN B 1 271 ? 52.416 -7.464 38.459 1.00 10.95 ? 271 GLN B CB 1 ATOM 5212 C CG . GLN B 1 271 ? 53.667 -6.624 38.521 1.00 12.05 ? 271 GLN B CG 1 ATOM 5213 C CD . GLN B 1 271 ? 54.865 -7.306 37.914 1.00 11.81 ? 271 GLN B CD 1 ATOM 5214 O OE1 . GLN B 1 271 ? 55.084 -8.512 38.124 1.00 13.06 ? 271 GLN B OE1 1 ATOM 5215 N NE2 . GLN B 1 271 ? 55.640 -6.545 37.162 1.00 13.44 ? 271 GLN B NE2 1 ATOM 5216 N N . PHE B 1 272 ? 49.130 -7.643 38.091 1.00 10.59 ? 272 PHE B N 1 ATOM 5217 C CA . PHE B 1 272 ? 47.981 -8.518 37.959 1.00 10.57 ? 272 PHE B CA 1 ATOM 5218 C C . PHE B 1 272 ? 48.211 -9.435 36.757 1.00 11.12 ? 272 PHE B C 1 ATOM 5219 O O . PHE B 1 272 ? 47.895 -9.078 35.626 1.00 11.86 ? 272 PHE B O 1 ATOM 5220 C CB . PHE B 1 272 ? 46.716 -7.655 37.811 1.00 10.12 ? 272 PHE B CB 1 ATOM 5221 C CG . PHE B 1 272 ? 46.459 -6.805 39.006 1.00 9.66 ? 272 PHE B CG 1 ATOM 5222 C CD1 . PHE B 1 272 ? 45.719 -7.296 40.056 1.00 9.87 ? 272 PHE B CD1 1 ATOM 5223 C CD2 . PHE B 1 272 ? 47.015 -5.558 39.124 1.00 11.12 ? 272 PHE B CD2 1 ATOM 5224 C CE1 . PHE B 1 272 ? 45.492 -6.496 41.194 1.00 10.53 ? 272 PHE B CE1 1 ATOM 5225 C CE2 . PHE B 1 272 ? 46.815 -4.774 40.250 1.00 11.36 ? 272 PHE B CE2 1 ATOM 5226 C CZ . PHE B 1 272 ? 46.053 -5.239 41.270 1.00 12.21 ? 272 PHE B CZ 1 ATOM 5227 N N . LEU B 1 273 ? 48.757 -10.626 37.030 1.00 11.38 ? 273 LEU B N 1 ATOM 5228 C CA . LEU B 1 273 ? 49.282 -11.490 35.961 1.00 12.58 ? 273 LEU B CA 1 ATOM 5229 C C . LEU B 1 273 ? 48.214 -12.453 35.481 1.00 13.65 ? 273 LEU B C 1 ATOM 5230 O O . LEU B 1 273 ? 47.587 -13.146 36.277 1.00 12.75 ? 273 LEU B O 1 ATOM 5231 C CB . LEU B 1 273 ? 50.507 -12.267 36.457 1.00 12.62 ? 273 LEU B CB 1 ATOM 5232 C CG . LEU B 1 273 ? 51.694 -11.422 36.975 1.00 14.66 ? 273 LEU B CG 1 ATOM 5233 C CD1 . LEU B 1 273 ? 52.811 -12.324 37.514 1.00 17.09 ? 273 LEU B CD1 1 ATOM 5234 C CD2 . LEU B 1 273 ? 52.236 -10.443 35.938 1.00 16.84 ? 273 LEU B CD2 1 ATOM 5235 N N . ALA B 1 274 ? 47.996 -12.468 34.167 1.00 15.23 ? 274 ALA B N 1 ATOM 5236 C CA . ALA B 1 274 ? 46.949 -13.280 33.567 1.00 17.23 ? 274 ALA B CA 1 ATOM 5237 C C . ALA B 1 274 ? 47.503 -14.552 32.937 1.00 19.48 ? 274 ALA B C 1 ATOM 5238 O O . ALA B 1 274 ? 48.663 -14.584 32.545 1.00 20.48 ? 274 ALA B O 1 ATOM 5239 C CB . ALA B 1 274 ? 46.210 -12.456 32.563 1.00 17.97 ? 274 ALA B CB 1 ATOM 5240 N N . ASN B 1 275 ? 46.647 -15.570 32.844 1.00 20.88 ? 275 ASN B N 1 ATOM 5241 C CA . ASN B 1 275 ? 46.969 -16.799 32.116 1.00 23.11 ? 275 ASN B CA 1 ATOM 5242 C C . ASN B 1 275 ? 46.831 -16.562 30.635 1.00 25.57 ? 275 ASN B C 1 ATOM 5243 O O . ASN B 1 275 ? 46.475 -15.479 30.176 1.00 25.32 ? 275 ASN B O 1 ATOM 5244 C CB . ASN B 1 275 ? 46.115 -17.972 32.577 1.00 24.09 ? 275 ASN B CB 1 ATOM 5245 C CG . ASN B 1 275 ? 44.628 -17.785 32.344 1.00 25.04 ? 275 ASN B CG 1 ATOM 5246 O OD1 . ASN B 1 275 ? 44.193 -17.087 31.431 1.00 25.53 ? 275 ASN B OD1 1 ATOM 5247 N ND2 . ASN B 1 275 ? 43.845 -18.438 33.183 1.00 28.08 ? 275 ASN B ND2 1 ATOM 5248 N N . ARG B 1 276 ? 47.144 -17.581 29.846 1.00 29.00 ? 276 ARG B N 1 ATOM 5249 C CA . ARG B 1 276 ? 47.245 -17.339 28.414 1.00 31.17 ? 276 ARG B CA 1 ATOM 5250 C C . ARG B 1 276 ? 45.883 -16.952 27.820 1.00 31.97 ? 276 ARG B C 1 ATOM 5251 O O . ARG B 1 276 ? 45.807 -16.216 26.831 1.00 33.47 ? 276 ARG B O 1 ATOM 5252 C CB . ARG B 1 276 ? 47.937 -18.513 27.714 1.00 32.39 ? 276 ARG B CB 1 ATOM 5253 C CG . ARG B 1 276 ? 49.389 -18.660 28.174 1.00 35.53 ? 276 ARG B CG 1 ATOM 5254 C CD . ARG B 1 276 ? 50.454 -18.133 27.206 1.00 40.15 ? 276 ARG B CD 1 ATOM 5255 N NE . ARG B 1 276 ? 51.166 -19.241 26.556 1.00 42.45 ? 276 ARG B NE 1 ATOM 5256 C CZ . ARG B 1 276 ? 51.219 -19.478 25.240 1.00 43.76 ? 276 ARG B CZ 1 ATOM 5257 N NH1 . ARG B 1 276 ? 50.620 -18.678 24.356 1.00 44.72 ? 276 ARG B NH1 1 ATOM 5258 N NH2 . ARG B 1 276 ? 51.897 -20.532 24.802 1.00 43.73 ? 276 ARG B NH2 1 ATOM 5259 N N . ARG B 1 277 ? 44.811 -17.373 28.481 1.00 31.79 ? 277 ARG B N 1 ATOM 5260 C CA . ARG B 1 277 ? 43.449 -16.990 28.089 1.00 30.92 ? 277 ARG B CA 1 ATOM 5261 C C . ARG B 1 277 ? 42.974 -15.609 28.570 1.00 29.52 ? 277 ARG B C 1 ATOM 5262 O O . ARG B 1 277 ? 41.823 -15.218 28.318 1.00 30.51 ? 277 ARG B O 1 ATOM 5263 C CB . ARG B 1 277 ? 42.464 -18.019 28.636 1.00 31.62 ? 277 ARG B CB 1 ATOM 5264 C CG . ARG B 1 277 ? 42.731 -19.448 28.223 1.00 34.09 ? 277 ARG B CG 1 ATOM 5265 C CD . ARG B 1 277 ? 41.850 -20.428 28.947 1.00 36.30 ? 277 ARG B CD 1 ATOM 5266 N NE . ARG B 1 277 ? 40.467 -20.361 28.466 1.00 40.50 ? 277 ARG B NE 1 ATOM 5267 C CZ . ARG B 1 277 ? 39.867 -21.278 27.702 1.00 42.27 ? 277 ARG B CZ 1 ATOM 5268 N NH1 . ARG B 1 277 ? 40.514 -22.374 27.303 1.00 43.75 ? 277 ARG B NH1 1 ATOM 5269 N NH2 . ARG B 1 277 ? 38.599 -21.097 27.331 1.00 42.44 ? 277 ARG B NH2 1 ATOM 5270 N N . GLY B 1 278 ? 43.814 -14.878 29.292 1.00 26.65 ? 278 GLY B N 1 ATOM 5271 C CA . GLY B 1 278 ? 43.452 -13.529 29.728 1.00 24.41 ? 278 GLY B CA 1 ATOM 5272 C C . GLY B 1 278 ? 42.691 -13.433 31.053 1.00 21.74 ? 278 GLY B C 1 ATOM 5273 O O . GLY B 1 278 ? 42.175 -12.383 31.410 1.00 22.60 ? 278 GLY B O 1 ATOM 5274 N N . LYS B 1 279 ? 42.613 -14.524 31.788 1.00 18.44 ? 279 LYS B N 1 ATOM 5275 C CA . LYS B 1 279 ? 42.013 -14.473 33.118 1.00 16.77 ? 279 LYS B CA 1 ATOM 5276 C C . LYS B 1 279 ? 43.124 -14.281 34.147 1.00 14.82 ? 279 LYS B C 1 ATOM 5277 O O . LYS B 1 279 ? 44.250 -14.761 34.027 1.00 13.88 ? 279 LYS B O 1 ATOM 5278 C CB . LYS B 1 279 ? 41.200 -15.733 33.401 1.00 16.41 ? 279 LYS B CB 1 ATOM 5279 C CG . LYS B 1 279 ? 40.029 -15.936 32.442 1.00 16.82 ? 279 LYS B CG 1 ATOM 5280 C CD . LYS B 1 279 ? 38.993 -14.833 32.506 1.00 16.63 ? 279 LYS B CD 1 ATOM 5281 C CE . LYS B 1 279 ? 37.753 -15.170 31.643 1.00 17.03 ? 279 LYS B CE 1 ATOM 5282 N NZ . LYS B 1 279 ? 36.665 -14.178 31.877 1.00 17.52 ? 279 LYS B NZ 1 ATOM 5283 N N . LEU B 1 280 ? 42.785 -13.585 35.209 1.00 12.99 ? 280 LEU B N 1 ATOM 5284 C CA . LEU B 1 280 ? 43.746 -13.355 36.270 1.00 13.15 ? 280 LEU B CA 1 ATOM 5285 C C . LEU B 1 280 ? 44.127 -14.643 36.981 1.00 12.83 ? 280 LEU B C 1 ATOM 5286 O O . LEU B 1 280 ? 43.263 -15.415 37.366 1.00 13.22 ? 280 LEU B O 1 ATOM 5287 C CB . LEU B 1 280 ? 43.158 -12.371 37.266 1.00 12.27 ? 280 LEU B CB 1 ATOM 5288 C CG . LEU B 1 280 ? 44.078 -11.965 38.418 1.00 11.88 ? 280 LEU B CG 1 ATOM 5289 C CD1 . LEU B 1 280 ? 45.228 -11.100 37.882 1.00 11.62 ? 280 LEU B CD1 1 ATOM 5290 C CD2 . LEU B 1 280 ? 43.294 -11.185 39.446 1.00 11.69 ? 280 LEU B CD2 1 ATOM 5291 N N . GLU B 1 281 ? 45.434 -14.860 37.116 1.00 12.79 ? 281 GLU B N 1 ATOM 5292 C CA . GLU B 1 281 ? 45.994 -16.025 37.784 1.00 15.04 ? 281 GLU B CA 1 ATOM 5293 C C . GLU B 1 281 ? 46.769 -15.708 39.067 1.00 13.31 ? 281 GLU B C 1 ATOM 5294 O O . GLU B 1 281 ? 46.726 -16.476 40.020 1.00 13.59 ? 281 GLU B O 1 ATOM 5295 C CB . GLU B 1 281 ? 46.920 -16.781 36.809 1.00 15.55 ? 281 GLU B CB 1 ATOM 5296 C CG . GLU B 1 281 ? 46.189 -17.811 35.954 1.00 21.69 ? 281 GLU B CG 1 ATOM 5297 C CD . GLU B 1 281 ? 47.125 -18.856 35.365 1.00 22.32 ? 281 GLU B CD 1 ATOM 5298 O OE1 . GLU B 1 281 ? 48.329 -18.885 35.720 1.00 28.18 ? 281 GLU B OE1 1 ATOM 5299 O OE2 . GLU B 1 281 ? 46.631 -19.675 34.549 1.00 32.14 ? 281 GLU B OE2 1 ATOM 5300 N N . LYS B 1 282 ? 47.553 -14.638 39.067 1.00 13.22 ? 282 LYS B N 1 ATOM 5301 C CA . LYS B 1 282 ? 48.460 -14.318 40.169 1.00 14.14 ? 282 LYS B CA 1 ATOM 5302 C C . LYS B 1 282 ? 48.476 -12.832 40.426 1.00 12.33 ? 282 LYS B C 1 ATOM 5303 O O . LYS B 1 282 ? 48.393 -12.061 39.471 1.00 12.40 ? 282 LYS B O 1 ATOM 5304 C CB . LYS B 1 282 ? 49.918 -14.727 39.841 1.00 15.37 ? 282 LYS B CB 1 ATOM 5305 C CG . LYS B 1 282 ? 50.158 -16.193 39.580 1.00 19.53 ? 282 LYS B CG 1 ATOM 5306 C CD . LYS B 1 282 ? 51.463 -16.432 38.860 1.00 20.25 ? 282 LYS B CD 1 ATOM 5307 C CE . LYS B 1 282 ? 51.786 -17.935 38.749 1.00 23.59 ? 282 LYS B CE 1 ATOM 5308 N NZ . LYS B 1 282 ? 52.725 -18.165 37.625 1.00 27.56 ? 282 LYS B NZ 1 ATOM 5309 N N . ILE B 1 283 ? 48.646 -12.453 41.690 1.00 11.10 ? 283 ILE B N 1 ATOM 5310 C CA . ILE B 1 283 ? 48.867 -11.049 42.072 1.00 10.98 ? 283 ILE B CA 1 ATOM 5311 C C . ILE B 1 283 ? 50.235 -10.980 42.750 1.00 10.43 ? 283 ILE B C 1 ATOM 5312 O O . ILE B 1 283 ? 50.517 -11.716 43.694 1.00 11.61 ? 283 ILE B O 1 ATOM 5313 C CB . ILE B 1 283 ? 47.750 -10.522 42.975 1.00 11.04 ? 283 ILE B CB 1 ATOM 5314 C CG1 . ILE B 1 283 ? 46.401 -10.639 42.283 1.00 11.75 ? 283 ILE B CG1 1 ATOM 5315 C CG2 . ILE B 1 283 ? 48.015 -9.053 43.369 1.00 12.32 ? 283 ILE B CG2 1 ATOM 5316 C CD1 . ILE B 1 283 ? 45.223 -10.367 43.182 1.00 12.08 ? 283 ILE B CD1 1 ATOM 5317 N N . HIS B 1 284 ? 51.090 -10.128 42.213 1.00 10.65 ? 284 HIS B N 1 ATOM 5318 C CA . HIS B 1 284 ? 52.504 -10.049 42.589 1.00 10.94 ? 284 HIS B CA 1 ATOM 5319 C C . HIS B 1 284 ? 52.830 -8.654 43.136 1.00 10.28 ? 284 HIS B C 1 ATOM 5320 O O . HIS B 1 284 ? 52.633 -7.666 42.439 1.00 11.12 ? 284 HIS B O 1 ATOM 5321 C CB . HIS B 1 284 ? 53.354 -10.325 41.357 1.00 11.32 ? 284 HIS B CB 1 ATOM 5322 C CG . HIS B 1 284 ? 54.834 -10.292 41.584 1.00 11.90 ? 284 HIS B CG 1 ATOM 5323 N ND1 . HIS B 1 284 ? 55.710 -9.890 40.601 1.00 12.89 ? 284 HIS B ND1 1 ATOM 5324 C CD2 . HIS B 1 284 ? 55.598 -10.631 42.655 1.00 11.98 ? 284 HIS B CD2 1 ATOM 5325 C CE1 . HIS B 1 284 ? 56.951 -9.989 41.048 1.00 13.63 ? 284 HIS B CE1 1 ATOM 5326 N NE2 . HIS B 1 284 ? 56.917 -10.438 42.292 1.00 13.95 ? 284 HIS B NE2 1 ATOM 5327 N N . ARG B 1 285 ? 53.339 -8.601 44.358 1.00 10.39 ? 285 ARG B N 1 ATOM 5328 C CA . ARG B 1 285 ? 53.740 -7.363 45.021 1.00 10.27 ? 285 ARG B CA 1 ATOM 5329 C C . ARG B 1 285 ? 55.232 -7.357 45.293 1.00 10.38 ? 285 ARG B C 1 ATOM 5330 O O . ARG B 1 285 ? 55.752 -8.249 45.956 1.00 11.07 ? 285 ARG B O 1 ATOM 5331 C CB . ARG B 1 285 ? 52.971 -7.219 46.334 1.00 9.47 ? 285 ARG B CB 1 ATOM 5332 C CG . ARG B 1 285 ? 53.573 -6.216 47.332 1.00 9.72 ? 285 ARG B CG 1 ATOM 5333 C CD . ARG B 1 285 ? 53.677 -4.785 46.846 1.00 9.50 ? 285 ARG B CD 1 ATOM 5334 N NE . ARG B 1 285 ? 52.378 -4.243 46.487 1.00 9.67 ? 285 ARG B NE 1 ATOM 5335 C CZ . ARG B 1 285 ? 51.480 -3.824 47.368 1.00 10.17 ? 285 ARG B CZ 1 ATOM 5336 N NH1 . ARG B 1 285 ? 51.728 -3.857 48.661 1.00 9.95 ? 285 ARG B NH1 1 ATOM 5337 N NH2 . ARG B 1 285 ? 50.321 -3.368 46.939 1.00 10.63 ? 285 ARG B NH2 1 ATOM 5338 N N . PHE B 1 286 ? 55.908 -6.320 44.803 1.00 10.47 ? 286 PHE B N 1 ATOM 5339 C CA . PHE B 1 286 ? 57.273 -6.069 45.205 1.00 10.85 ? 286 PHE B CA 1 ATOM 5340 C C . PHE B 1 286 ? 57.486 -4.572 45.378 1.00 11.09 ? 286 PHE B C 1 ATOM 5341 O O . PHE B 1 286 ? 56.566 -3.788 45.146 1.00 11.32 ? 286 PHE B O 1 ATOM 5342 C CB . PHE B 1 286 ? 58.268 -6.720 44.233 1.00 11.23 ? 286 PHE B CB 1 ATOM 5343 C CG . PHE B 1 286 ? 58.222 -6.190 42.860 1.00 12.14 ? 286 PHE B CG 1 ATOM 5344 C CD1 . PHE B 1 286 ? 57.349 -6.714 41.948 1.00 12.33 ? 286 PHE B CD1 1 ATOM 5345 C CD2 . PHE B 1 286 ? 59.072 -5.171 42.477 1.00 13.14 ? 286 PHE B CD2 1 ATOM 5346 C CE1 . PHE B 1 286 ? 57.328 -6.222 40.648 1.00 14.33 ? 286 PHE B CE1 1 ATOM 5347 C CE2 . PHE B 1 286 ? 59.047 -4.677 41.169 1.00 14.21 ? 286 PHE B CE2 1 ATOM 5348 C CZ . PHE B 1 286 ? 58.180 -5.204 40.276 1.00 13.45 ? 286 PHE B CZ 1 ATOM 5349 N N . TYR B 1 287 ? 58.660 -4.180 45.874 1.00 10.96 ? 287 TYR B N 1 ATOM 5350 C CA . TYR B 1 287 ? 58.913 -2.803 46.282 1.00 11.65 ? 287 TYR B CA 1 ATOM 5351 C C . TYR B 1 287 ? 60.192 -2.310 45.631 1.00 12.02 ? 287 TYR B C 1 ATOM 5352 O O . TYR B 1 287 ? 60.966 -3.101 45.086 1.00 12.44 ? 287 TYR B O 1 ATOM 5353 C CB . TYR B 1 287 ? 59.020 -2.716 47.815 1.00 10.75 ? 287 TYR B CB 1 ATOM 5354 C CG . TYR B 1 287 ? 57.757 -3.200 48.523 1.00 10.61 ? 287 TYR B CG 1 ATOM 5355 C CD1 . TYR B 1 287 ? 57.561 -4.534 48.760 1.00 10.38 ? 287 TYR B CD1 1 ATOM 5356 C CD2 . TYR B 1 287 ? 56.757 -2.306 48.946 1.00 11.69 ? 287 TYR B CD2 1 ATOM 5357 C CE1 . TYR B 1 287 ? 56.416 -5.006 49.374 1.00 11.14 ? 287 TYR B CE1 1 ATOM 5358 C CE2 . TYR B 1 287 ? 55.606 -2.767 49.578 1.00 10.83 ? 287 TYR B CE2 1 ATOM 5359 C CZ . TYR B 1 287 ? 55.441 -4.113 49.790 1.00 10.40 ? 287 TYR B CZ 1 ATOM 5360 O OH . TYR B 1 287 ? 54.275 -4.568 50.363 1.00 10.44 ? 287 TYR B OH 1 ATOM 5361 N N . VAL B 1 288 ? 60.399 -1.004 45.700 1.00 11.73 ? 288 VAL B N 1 ATOM 5362 C CA . VAL B 1 288 ? 61.662 -0.378 45.288 1.00 12.63 ? 288 VAL B CA 1 ATOM 5363 C C . VAL B 1 288 ? 61.995 0.669 46.336 1.00 13.01 ? 288 VAL B C 1 ATOM 5364 O O . VAL B 1 288 ? 61.132 1.455 46.743 1.00 12.73 ? 288 VAL B O 1 ATOM 5365 C CB . VAL B 1 288 ? 61.594 0.296 43.917 1.00 13.32 ? 288 VAL B CB 1 ATOM 5366 C CG1 . VAL B 1 288 ? 62.987 0.745 43.450 1.00 15.20 ? 288 VAL B CG1 1 ATOM 5367 C CG2 . VAL B 1 288 ? 60.962 -0.625 42.883 1.00 14.24 ? 288 VAL B CG2 1 ATOM 5368 N N . GLN B 1 289 ? 63.238 0.684 46.797 1.00 13.37 ? 289 GLN B N 1 ATOM 5369 C CA . GLN B 1 289 ? 63.650 1.684 47.775 1.00 14.34 ? 289 GLN B CA 1 ATOM 5370 C C . GLN B 1 289 ? 65.122 1.991 47.560 1.00 15.84 ? 289 GLN B C 1 ATOM 5371 O O . GLN B 1 289 ? 65.921 1.078 47.334 1.00 15.80 ? 289 GLN B O 1 ATOM 5372 C CB . GLN B 1 289 ? 63.361 1.201 49.199 1.00 13.22 ? 289 GLN B CB 1 ATOM 5373 C CG . GLN B 1 289 ? 63.528 2.301 50.257 1.00 12.70 ? 289 GLN B CG 1 ATOM 5374 C CD . GLN B 1 289 ? 63.065 1.908 51.643 1.00 12.90 ? 289 GLN B CD 1 ATOM 5375 O OE1 . GLN B 1 289 ? 63.384 0.824 52.132 1.00 14.14 ? 289 GLN B OE1 1 ATOM 5376 N NE2 . GLN B 1 289 ? 62.309 2.807 52.293 1.00 13.42 ? 289 GLN B NE2 1 ATOM 5377 N N . ASP B 1 290 ? 65.428 3.289 47.587 1.00 17.40 ? 290 ASP B N 1 ATOM 5378 C CA . ASP B 1 290 ? 66.771 3.814 47.340 1.00 19.79 ? 290 ASP B CA 1 ATOM 5379 C C . ASP B 1 290 ? 67.336 3.296 46.023 1.00 20.46 ? 290 ASP B C 1 ATOM 5380 O O . ASP B 1 290 ? 68.539 3.011 45.914 1.00 22.22 ? 290 ASP B O 1 ATOM 5381 C CB . ASP B 1 290 ? 67.673 3.498 48.522 1.00 21.28 ? 290 ASP B CB 1 ATOM 5382 C CG . ASP B 1 290 ? 67.227 4.196 49.798 1.00 25.09 ? 290 ASP B CG 1 ATOM 5383 O OD1 . ASP B 1 290 ? 66.574 5.263 49.706 1.00 30.58 ? 290 ASP B OD1 1 ATOM 5384 O OD2 . ASP B 1 290 ? 67.453 3.745 50.941 1.00 31.31 ? 290 ASP B OD2 1 ATOM 5385 N N . GLY B 1 291 ? 66.462 3.191 45.022 1.00 20.38 ? 291 GLY B N 1 ATOM 5386 C CA . GLY B 1 291 ? 66.854 2.809 43.665 1.00 20.58 ? 291 GLY B CA 1 ATOM 5387 C C . GLY B 1 291 ? 67.036 1.327 43.422 1.00 20.51 ? 291 GLY B C 1 ATOM 5388 O O . GLY B 1 291 ? 67.428 0.934 42.311 1.00 21.44 ? 291 GLY B O 1 ATOM 5389 N N . LYS B 1 292 ? 66.736 0.498 44.431 1.00 19.37 ? 292 LYS B N 1 ATOM 5390 C CA . LYS B 1 292 ? 66.960 -0.935 44.377 1.00 19.84 ? 292 LYS B CA 1 ATOM 5391 C C . LYS B 1 292 ? 65.618 -1.667 44.474 1.00 18.33 ? 292 LYS B C 1 ATOM 5392 O O . LYS B 1 292 ? 64.808 -1.393 45.370 1.00 17.27 ? 292 LYS B O 1 ATOM 5393 C CB . LYS B 1 292 ? 67.888 -1.393 45.506 1.00 20.67 ? 292 LYS B CB 1 ATOM 5394 C CG . LYS B 1 292 ? 69.322 -0.834 45.412 1.00 24.15 ? 292 LYS B CG 1 ATOM 5395 C CD . LYS B 1 292 ? 70.193 -1.234 46.620 1.00 24.98 ? 292 LYS B CD 1 ATOM 5396 C CE . LYS B 1 292 ? 69.820 -0.448 47.865 1.00 28.72 ? 292 LYS B CE 1 ATOM 5397 N NZ . LYS B 1 292 ? 70.676 -0.735 49.065 1.00 29.98 ? 292 LYS B NZ 1 ATOM 5398 N N . VAL B 1 293 ? 65.371 -2.560 43.528 1.00 17.14 ? 293 VAL B N 1 ATOM 5399 C CA . VAL B 1 293 ? 64.227 -3.476 43.607 1.00 17.21 ? 293 VAL B CA 1 ATOM 5400 C C . VAL B 1 293 ? 64.383 -4.426 44.778 1.00 16.67 ? 293 VAL B C 1 ATOM 5401 O O . VAL B 1 293 ? 65.444 -5.039 44.968 1.00 17.27 ? 293 VAL B O 1 ATOM 5402 C CB . VAL B 1 293 ? 64.068 -4.294 42.298 1.00 18.25 ? 293 VAL B CB 1 ATOM 5403 C CG1 . VAL B 1 293 ? 63.038 -5.399 42.467 1.00 18.49 ? 293 VAL B CG1 1 ATOM 5404 C CG2 . VAL B 1 293 ? 63.717 -3.380 41.138 1.00 20.63 ? 293 VAL B CG2 1 ATOM 5405 N N . ILE B 1 294 ? 63.302 -4.554 45.541 1.00 15.17 ? 294 ILE B N 1 ATOM 5406 C CA . ILE B 1 294 ? 63.191 -5.460 46.690 1.00 14.89 ? 294 ILE B CA 1 ATOM 5407 C C . ILE B 1 294 ? 62.140 -6.488 46.304 1.00 13.94 ? 294 ILE B C 1 ATOM 5408 O O . ILE B 1 294 ? 60.952 -6.199 46.272 1.00 13.05 ? 294 ILE B O 1 ATOM 5409 C CB . ILE B 1 294 ? 62.792 -4.674 47.970 1.00 14.92 ? 294 ILE B CB 1 ATOM 5410 C CG1 . ILE B 1 294 ? 63.852 -3.605 48.283 1.00 15.36 ? 294 ILE B CG1 1 ATOM 5411 C CG2 . ILE B 1 294 ? 62.639 -5.619 49.135 1.00 15.43 ? 294 ILE B CG2 1 ATOM 5412 C CD1 . ILE B 1 294 ? 63.359 -2.506 49.161 1.00 16.89 ? 294 ILE B CD1 1 ATOM 5413 N N . GLU B 1 295 ? 62.573 -7.678 45.923 1.00 13.57 ? 295 GLU B N 1 ATOM 5414 C CA . GLU B 1 295 ? 61.665 -8.689 45.455 1.00 13.67 ? 295 GLU B CA 1 ATOM 5415 C C . GLU B 1 295 ? 60.776 -9.127 46.591 1.00 12.98 ? 295 GLU B C 1 ATOM 5416 O O . GLU B 1 295 ? 61.119 -8.960 47.763 1.00 13.14 ? 295 GLU B O 1 ATOM 5417 C CB . GLU B 1 295 ? 62.444 -9.878 44.929 1.00 14.29 ? 295 GLU B CB 1 ATOM 5418 C CG . GLU B 1 295 ? 63.406 -9.589 43.780 1.00 17.01 ? 295 GLU B CG 1 ATOM 5419 C CD . GLU B 1 295 ? 62.731 -9.259 42.470 1.00 19.47 ? 295 GLU B CD 1 ATOM 5420 O OE1 . GLU B 1 295 ? 61.483 -9.368 42.363 1.00 21.00 ? 295 GLU B OE1 1 ATOM 5421 O OE2 . GLU B 1 295 ? 63.473 -8.880 41.524 1.00 21.90 ? 295 GLU B OE2 1 ATOM 5422 N N . SER B 1 296 ? 59.645 -9.722 46.244 1.00 12.13 ? 296 SER B N 1 ATOM 5423 C CA . SER B 1 296 ? 58.753 -10.257 47.259 1.00 12.22 ? 296 SER B CA 1 ATOM 5424 C C . SER B 1 296 ? 59.427 -11.372 48.050 1.00 12.72 ? 296 SER B C 1 ATOM 5425 O O . SER B 1 296 ? 60.208 -12.159 47.513 1.00 12.81 ? 296 SER B O 1 ATOM 5426 C CB . SER B 1 296 ? 57.481 -10.832 46.629 1.00 12.46 ? 296 SER B CB 1 ATOM 5427 O OG . SER B 1 296 ? 56.588 -11.292 47.650 1.00 12.83 ? 296 SER B OG 1 ATOM 5428 N N . PHE B 1 297 ? 59.078 -11.457 49.324 1.00 12.62 ? 297 PHE B N 1 ATOM 5429 C CA . PHE B 1 297 ? 59.295 -12.635 50.132 1.00 12.03 ? 297 PHE B CA 1 ATOM 5430 C C . PHE B 1 297 ? 58.554 -13.823 49.540 1.00 12.01 ? 297 PHE B C 1 ATOM 5431 O O . PHE B 1 297 ? 57.578 -13.677 48.789 1.00 11.73 ? 297 PHE B O 1 ATOM 5432 C CB . PHE B 1 297 ? 58.813 -12.417 51.572 1.00 12.44 ? 297 PHE B CB 1 ATOM 5433 C CG . PHE B 1 297 ? 57.423 -11.937 51.645 1.00 11.22 ? 297 PHE B CG 1 ATOM 5434 C CD1 . PHE B 1 297 ? 56.364 -12.831 51.708 1.00 11.32 ? 297 PHE B CD1 1 ATOM 5435 C CD2 . PHE B 1 297 ? 57.140 -10.572 51.609 1.00 11.97 ? 297 PHE B CD2 1 ATOM 5436 C CE1 . PHE B 1 297 ? 55.042 -12.379 51.726 1.00 12.34 ? 297 PHE B CE1 1 ATOM 5437 C CE2 . PHE B 1 297 ? 55.848 -10.122 51.629 1.00 12.26 ? 297 PHE B CE2 1 ATOM 5438 C CZ . PHE B 1 297 ? 54.795 -11.012 51.679 1.00 11.80 ? 297 PHE B CZ 1 ATOM 5439 N N . TYR B 1 298 ? 59.031 -15.023 49.906 1.00 12.14 ? 298 TYR B N 1 ATOM 5440 C CA . TYR B 1 298 ? 58.272 -16.236 49.736 1.00 12.53 ? 298 TYR B CA 1 ATOM 5441 C C . TYR B 1 298 ? 57.673 -16.615 51.078 1.00 12.42 ? 298 TYR B C 1 ATOM 5442 O O . TYR B 1 298 ? 58.230 -16.297 52.146 1.00 13.45 ? 298 TYR B O 1 ATOM 5443 C CB . TYR B 1 298 ? 59.170 -17.373 49.224 1.00 13.45 ? 298 TYR B CB 1 ATOM 5444 C CG . TYR B 1 298 ? 59.533 -17.258 47.786 1.00 14.20 ? 298 TYR B CG 1 ATOM 5445 C CD1 . TYR B 1 298 ? 60.534 -16.399 47.375 1.00 14.05 ? 298 TYR B CD1 1 ATOM 5446 C CD2 . TYR B 1 298 ? 58.881 -18.015 46.824 1.00 15.14 ? 298 TYR B CD2 1 ATOM 5447 C CE1 . TYR B 1 298 ? 60.870 -16.291 46.036 1.00 14.66 ? 298 TYR B CE1 1 ATOM 5448 C CE2 . TYR B 1 298 ? 59.235 -17.918 45.500 1.00 14.01 ? 298 TYR B CE2 1 ATOM 5449 C CZ . TYR B 1 298 ? 60.206 -17.025 45.109 1.00 13.98 ? 298 TYR B CZ 1 ATOM 5450 O OH . TYR B 1 298 ? 60.587 -16.922 43.772 1.00 17.71 ? 298 TYR B OH 1 ATOM 5451 N N . THR B 1 299 ? 56.543 -17.295 51.039 1.00 11.77 ? 299 THR B N 1 ATOM 5452 C CA . THR B 1 299 ? 55.947 -17.810 52.262 1.00 12.02 ? 299 THR B CA 1 ATOM 5453 C C . THR B 1 299 ? 56.903 -18.760 52.989 1.00 12.97 ? 299 THR B C 1 ATOM 5454 O O . THR B 1 299 ? 57.750 -19.412 52.364 1.00 13.13 ? 299 THR B O 1 ATOM 5455 C CB . THR B 1 299 ? 54.613 -18.554 51.974 1.00 11.81 ? 299 THR B CB 1 ATOM 5456 O OG1 . THR B 1 299 ? 54.858 -19.670 51.093 1.00 12.42 ? 299 THR B OG1 1 ATOM 5457 C CG2 . THR B 1 299 ? 53.562 -17.659 51.270 1.00 12.44 ? 299 THR B CG2 1 ATOM 5458 N N . ASN B 1 300 ? 56.736 -18.834 54.296 1.00 12.73 ? 300 ASN B N 1 ATOM 5459 C CA . ASN B 1 300 ? 57.624 -19.643 55.147 1.00 13.26 ? 300 ASN B CA 1 ATOM 5460 C C . ASN B 1 300 ? 56.873 -20.253 56.314 1.00 12.90 ? 300 ASN B C 1 ATOM 5461 O O . ASN B 1 300 ? 57.323 -20.195 57.461 1.00 13.79 ? 300 ASN B O 1 ATOM 5462 C CB . ASN B 1 300 ? 58.803 -18.775 55.606 1.00 13.50 ? 300 ASN B CB 1 ATOM 5463 C CG . ASN B 1 300 ? 59.868 -19.559 56.286 1.00 15.84 ? 300 ASN B CG 1 ATOM 5464 O OD1 . ASN B 1 300 ? 60.321 -20.577 55.772 1.00 19.42 ? 300 ASN B OD1 1 ATOM 5465 N ND2 . ASN B 1 300 ? 60.277 -19.097 57.465 1.00 18.64 ? 300 ASN B ND2 1 ATOM 5466 N N . LYS B 1 301 ? 55.742 -20.884 56.032 1.00 13.57 ? 301 LYS B N 1 ATOM 5467 C CA . LYS B 1 301 ? 54.849 -21.346 57.085 1.00 14.45 ? 301 LYS B CA 1 ATOM 5468 C C . LYS B 1 301 ? 54.312 -22.724 56.789 1.00 15.21 ? 301 LYS B C 1 ATOM 5469 O O . LYS B 1 301 ? 53.804 -22.976 55.711 1.00 14.49 ? 301 LYS B O 1 ATOM 5470 C CB . LYS B 1 301 ? 53.685 -20.362 57.259 1.00 14.21 ? 301 LYS B CB 1 ATOM 5471 C CG . LYS B 1 301 ? 52.751 -20.693 58.440 1.00 14.40 ? 301 LYS B CG 1 ATOM 5472 C CD . LYS B 1 301 ? 51.664 -19.629 58.609 1.00 14.91 ? 301 LYS B CD 1 ATOM 5473 C CE . LYS B 1 301 ? 50.794 -19.835 59.839 1.00 16.51 ? 301 LYS B CE 1 ATOM 5474 N NZ . LYS B 1 301 ? 49.906 -20.971 59.738 1.00 18.81 ? 301 LYS B NZ 1 ATOM 5475 N N . GLU B 1 302 ? 54.406 -23.609 57.774 1.00 17.55 ? 302 GLU B N 1 ATOM 5476 C CA . GLU B 1 302 ? 53.860 -24.958 57.656 1.00 17.78 ? 302 GLU B CA 1 ATOM 5477 C C . GLU B 1 302 ? 52.421 -24.907 57.211 1.00 17.81 ? 302 GLU B C 1 ATOM 5478 O O . GLU B 1 302 ? 51.626 -24.171 57.795 1.00 18.59 ? 302 GLU B O 1 ATOM 5479 C CB . GLU B 1 302 ? 53.936 -25.628 59.030 1.00 19.86 ? 302 GLU B CB 1 ATOM 5480 C CG . GLU B 1 302 ? 53.479 -27.077 59.060 1.00 22.91 ? 302 GLU B CG 1 ATOM 5481 C CD . GLU B 1 302 ? 54.441 -27.960 59.832 1.00 30.53 ? 302 GLU B CD 1 ATOM 5482 O OE1 . GLU B 1 302 ? 55.667 -27.892 59.570 1.00 35.08 ? 302 GLU B OE1 1 ATOM 5483 O OE2 . GLU B 1 302 ? 53.969 -28.727 60.698 1.00 34.79 ? 302 GLU B OE2 1 ATOM 5484 N N . GLY B 1 303 ? 52.081 -25.711 56.197 1.00 17.17 ? 303 GLY B N 1 ATOM 5485 C CA . GLY B 1 303 ? 50.729 -25.778 55.695 1.00 17.09 ? 303 GLY B CA 1 ATOM 5486 C C . GLY B 1 303 ? 50.409 -24.792 54.587 1.00 16.56 ? 303 GLY B C 1 ATOM 5487 O O . GLY B 1 303 ? 49.334 -24.848 54.003 1.00 18.43 ? 303 GLY B O 1 ATOM 5488 N N . VAL B 1 304 ? 51.336 -23.888 54.293 1.00 15.73 ? 304 VAL B N 1 ATOM 5489 C CA . VAL B 1 304 ? 51.122 -22.878 53.265 1.00 15.91 ? 304 VAL B CA 1 ATOM 5490 C C . VAL B 1 304 ? 52.036 -23.232 52.103 1.00 15.99 ? 304 VAL B C 1 ATOM 5491 O O . VAL B 1 304 ? 53.248 -23.288 52.267 1.00 14.47 ? 304 VAL B O 1 ATOM 5492 C CB . VAL B 1 304 ? 51.425 -21.472 53.793 1.00 15.35 ? 304 VAL B CB 1 ATOM 5493 C CG1 . VAL B 1 304 ? 51.218 -20.418 52.694 1.00 15.94 ? 304 VAL B CG1 1 ATOM 5494 C CG2 . VAL B 1 304 ? 50.551 -21.128 55.018 1.00 16.93 ? 304 VAL B CG2 1 ATOM 5495 N N . PRO B 1 305 ? 51.462 -23.426 50.915 1.00 16.28 ? 305 PRO B N 1 ATOM 5496 C CA . PRO B 1 305 ? 52.259 -23.713 49.727 1.00 16.57 ? 305 PRO B CA 1 ATOM 5497 C C . PRO B 1 305 ? 53.343 -22.667 49.535 1.00 15.38 ? 305 PRO B C 1 ATOM 5498 O O . PRO B 1 305 ? 53.103 -21.479 49.764 1.00 16.33 ? 305 PRO B O 1 ATOM 5499 C CB . PRO B 1 305 ? 51.256 -23.530 48.576 1.00 18.46 ? 305 PRO B CB 1 ATOM 5500 C CG . PRO B 1 305 ? 49.969 -23.077 49.161 1.00 18.84 ? 305 PRO B CG 1 ATOM 5501 C CD . PRO B 1 305 ? 50.018 -23.293 50.613 1.00 18.07 ? 305 PRO B CD 1 ATOM 5502 N N . TYR B 1 306 ? 54.529 -23.096 49.129 1.00 14.55 ? 306 TYR B N 1 ATOM 5503 C CA . TYR B 1 306 ? 55.630 -22.189 48.892 1.00 13.81 ? 306 TYR B CA 1 ATOM 5504 C C . TYR B 1 306 ? 55.305 -21.307 47.691 1.00 13.42 ? 306 TYR B C 1 ATOM 5505 O O . TYR B 1 306 ? 55.079 -21.805 46.598 1.00 14.55 ? 306 TYR B O 1 ATOM 5506 C CB . TYR B 1 306 ? 56.910 -22.986 48.619 1.00 13.72 ? 306 TYR B CB 1 ATOM 5507 C CG . TYR B 1 306 ? 58.151 -22.154 48.469 1.00 12.36 ? 306 TYR B CG 1 ATOM 5508 C CD1 . TYR B 1 306 ? 58.751 -21.598 49.582 1.00 13.01 ? 306 TYR B CD1 1 ATOM 5509 C CD2 . TYR B 1 306 ? 58.757 -21.950 47.226 1.00 12.57 ? 306 TYR B CD2 1 ATOM 5510 C CE1 . TYR B 1 306 ? 59.890 -20.856 49.502 1.00 12.38 ? 306 TYR B CE1 1 ATOM 5511 C CE2 . TYR B 1 306 ? 59.898 -21.185 47.133 1.00 13.29 ? 306 TYR B CE2 1 ATOM 5512 C CZ . TYR B 1 306 ? 60.478 -20.642 48.273 1.00 12.26 ? 306 TYR B CZ 1 ATOM 5513 O OH . TYR B 1 306 ? 61.609 -19.875 48.196 1.00 14.27 ? 306 TYR B OH 1 ATOM 5514 N N . THR B 1 307 ? 55.254 -19.988 47.896 1.00 12.68 ? 307 THR B N 1 ATOM 5515 C CA . THR B 1 307 ? 54.853 -19.074 46.846 1.00 12.82 ? 307 THR B CA 1 ATOM 5516 C C . THR B 1 307 ? 55.342 -17.672 47.187 1.00 12.57 ? 307 THR B C 1 ATOM 5517 O O . THR B 1 307 ? 55.441 -17.316 48.356 1.00 12.23 ? 307 THR B O 1 ATOM 5518 C CB . THR B 1 307 ? 53.319 -19.073 46.671 1.00 13.53 ? 307 THR B CB 1 ATOM 5519 O OG1 . THR B 1 307 ? 53.002 -18.220 45.570 1.00 14.85 ? 307 THR B OG1 1 ATOM 5520 C CG2 . THR B 1 307 ? 52.574 -18.476 47.864 1.00 13.32 ? 307 THR B CG2 1 ATOM 5521 N N . ASN B 1 308 ? 55.582 -16.874 46.147 1.00 11.67 ? 308 ASN B N 1 ATOM 5522 C CA . ASN B 1 308 ? 55.818 -15.439 46.282 1.00 12.53 ? 308 ASN B CA 1 ATOM 5523 C C . ASN B 1 308 ? 54.708 -14.588 45.674 1.00 12.49 ? 308 ASN B C 1 ATOM 5524 O O . ASN B 1 308 ? 54.906 -13.378 45.475 1.00 12.89 ? 308 ASN B O 1 ATOM 5525 C CB . ASN B 1 308 ? 57.180 -15.027 45.681 1.00 13.00 ? 308 ASN B CB 1 ATOM 5526 C CG . ASN B 1 308 ? 57.261 -15.249 44.178 1.00 12.68 ? 308 ASN B CG 1 ATOM 5527 O OD1 . ASN B 1 308 ? 56.420 -15.944 43.585 1.00 13.75 ? 308 ASN B OD1 1 ATOM 5528 N ND2 . ASN B 1 308 ? 58.262 -14.635 43.548 1.00 13.74 ? 308 ASN B ND2 1 ATOM 5529 N N . MET B 1 309 ? 53.559 -15.197 45.391 1.00 12.83 ? 309 MET B N 1 ATOM 5530 C CA . MET B 1 309 ? 52.428 -14.489 44.781 1.00 12.96 ? 309 MET B CA 1 ATOM 5531 C C . MET B 1 309 ? 51.108 -15.029 45.314 1.00 12.39 ? 309 MET B C 1 ATOM 5532 O O . MET B 1 309 ? 50.990 -16.196 45.713 1.00 12.62 ? 309 MET B O 1 ATOM 5533 C CB . MET B 1 309 ? 52.471 -14.612 43.264 1.00 13.62 ? 309 MET B CB 1 ATOM 5534 C CG . MET B 1 309 ? 53.729 -13.996 42.631 1.00 14.58 ? 309 MET B CG 1 ATOM 5535 S SD . MET B 1 309 ? 53.672 -14.112 40.862 1.00 16.93 ? 309 MET B SD 1 ATOM 5536 C CE . MET B 1 309 ? 55.339 -13.800 40.504 1.00 16.93 ? 309 MET B CE 1 ATOM 5537 N N . ILE B 1 310 ? 50.115 -14.154 45.328 1.00 11.47 ? 310 ILE B N 1 ATOM 5538 C CA . ILE B 1 310 ? 48.742 -14.535 45.637 1.00 11.57 ? 310 ILE B CA 1 ATOM 5539 C C . ILE B 1 310 ? 48.154 -15.307 44.455 1.00 11.80 ? 310 ILE B C 1 ATOM 5540 O O . ILE B 1 310 ? 48.219 -14.834 43.327 1.00 12.52 ? 310 ILE B O 1 ATOM 5541 C CB . ILE B 1 310 ? 47.883 -13.290 45.904 1.00 11.68 ? 310 ILE B CB 1 ATOM 5542 C CG1 . ILE B 1 310 ? 48.461 -12.403 47.009 1.00 11.77 ? 310 ILE B CG1 1 ATOM 5543 C CG2 . ILE B 1 310 ? 46.454 -13.679 46.237 1.00 12.21 ? 310 ILE B CG2 1 ATOM 5544 C CD1 . ILE B 1 310 ? 47.701 -11.101 47.147 1.00 13.05 ? 310 ILE B CD1 1 ATOM 5545 N N . ASP B 1 311 ? 47.560 -16.469 44.724 1.00 11.70 ? 311 ASP B N 1 ATOM 5546 C CA . ASP B 1 311 ? 46.863 -17.262 43.702 1.00 11.54 ? 311 ASP B CA 1 ATOM 5547 C C . ASP B 1 311 ? 45.854 -18.162 44.400 1.00 11.62 ? 311 ASP B C 1 ATOM 5548 O O . ASP B 1 311 ? 45.757 -18.164 45.625 1.00 11.23 ? 311 ASP B O 1 ATOM 5549 C CB . ASP B 1 311 ? 47.833 -18.009 42.763 1.00 11.78 ? 311 ASP B CB 1 ATOM 5550 C CG . ASP B 1 311 ? 48.667 -19.071 43.449 1.00 13.12 ? 311 ASP B CG 1 ATOM 5551 O OD1 . ASP B 1 311 ? 48.416 -19.447 44.615 1.00 13.07 ? 311 ASP B OD1 1 ATOM 5552 O OD2 . ASP B 1 311 ? 49.637 -19.584 42.842 1.00 16.06 ? 311 ASP B OD2 1 ATOM 5553 N N . ASP B 1 312 ? 45.078 -18.909 43.635 1.00 11.10 ? 312 ASP B N 1 ATOM 5554 C CA . ASP B 1 312 ? 44.036 -19.745 44.210 1.00 11.90 ? 312 ASP B CA 1 ATOM 5555 C C . ASP B 1 312 ? 44.594 -20.772 45.193 1.00 11.84 ? 312 ASP B C 1 ATOM 5556 O O . ASP B 1 312 ? 43.997 -21.035 46.231 1.00 12.58 ? 312 ASP B O 1 ATOM 5557 C CB . ASP B 1 312 ? 43.283 -20.485 43.095 1.00 11.39 ? 312 ASP B CB 1 ATOM 5558 C CG . ASP B 1 312 ? 42.210 -19.649 42.430 1.00 11.80 ? 312 ASP B CG 1 ATOM 5559 O OD1 . ASP B 1 312 ? 41.988 -18.455 42.835 1.00 12.54 ? 312 ASP B OD1 1 ATOM 5560 O OD2 . ASP B 1 312 ? 41.560 -20.121 41.467 1.00 13.64 ? 312 ASP B OD2 1 ATOM 5561 N N . GLU B 1 313 ? 45.732 -21.371 44.852 1.00 12.46 ? 313 GLU B N 1 ATOM 5562 C CA . GLU B 1 313 ? 46.321 -22.382 45.736 1.00 13.43 ? 313 GLU B CA 1 ATOM 5563 C C . GLU B 1 313 ? 46.597 -21.791 47.112 1.00 12.93 ? 313 GLU B C 1 ATOM 5564 O O . GLU B 1 313 ? 46.225 -22.368 48.149 1.00 13.03 ? 313 GLU B O 1 ATOM 5565 C CB . GLU B 1 313 ? 47.603 -22.948 45.120 1.00 13.17 ? 313 GLU B CB 1 ATOM 5566 C CG . GLU B 1 313 ? 48.323 -23.923 46.048 1.00 16.15 ? 313 GLU B CG 1 ATOM 5567 C CD . GLU B 1 313 ? 49.682 -24.385 45.553 1.00 17.56 ? 313 GLU B CD 1 ATOM 5568 O OE1 . GLU B 1 313 ? 50.487 -23.553 45.045 1.00 23.02 ? 313 GLU B OE1 1 ATOM 5569 O OE2 . GLU B 1 313 ? 49.983 -25.591 45.755 1.00 22.19 ? 313 GLU B OE2 1 ATOM 5570 N N . PHE B 1 314 ? 47.222 -20.614 47.115 1.00 12.30 ? 314 PHE B N 1 ATOM 5571 C CA . PHE B 1 314 ? 47.514 -19.891 48.351 1.00 12.23 ? 314 PHE B CA 1 ATOM 5572 C C . PHE B 1 314 ? 46.230 -19.530 49.109 1.00 12.09 ? 314 PHE B C 1 ATOM 5573 O O . PHE B 1 314 ? 46.126 -19.718 50.344 1.00 11.79 ? 314 PHE B O 1 ATOM 5574 C CB . PHE B 1 314 ? 48.348 -18.627 48.042 1.00 11.75 ? 314 PHE B CB 1 ATOM 5575 C CG . PHE B 1 314 ? 48.506 -17.742 49.232 1.00 11.83 ? 314 PHE B CG 1 ATOM 5576 C CD1 . PHE B 1 314 ? 49.453 -18.041 50.213 1.00 11.81 ? 314 PHE B CD1 1 ATOM 5577 C CD2 . PHE B 1 314 ? 47.671 -16.654 49.411 1.00 12.01 ? 314 PHE B CD2 1 ATOM 5578 C CE1 . PHE B 1 314 ? 49.573 -17.242 51.352 1.00 12.02 ? 314 PHE B CE1 1 ATOM 5579 C CE2 . PHE B 1 314 ? 47.792 -15.865 50.548 1.00 11.54 ? 314 PHE B CE2 1 ATOM 5580 C CZ . PHE B 1 314 ? 48.758 -16.151 51.510 1.00 12.13 ? 314 PHE B CZ 1 ATOM 5581 N N . CYS B 1 315 ? 45.266 -18.961 48.394 1.00 11.83 ? 315 CYS B N 1 ATOM 5582 C CA . CYS B 1 315 ? 44.036 -18.507 49.041 1.00 12.17 ? 315 CYS B CA 1 ATOM 5583 C C . CYS B 1 315 ? 43.246 -19.662 49.668 1.00 12.38 ? 315 CYS B C 1 ATOM 5584 O O . CYS B 1 315 ? 42.767 -19.551 50.787 1.00 12.66 ? 315 CYS B O 1 ATOM 5585 C CB . CYS B 1 315 ? 43.185 -17.695 48.058 1.00 11.37 ? 315 CYS B CB 1 ATOM 5586 S SG . CYS B 1 315 ? 44.048 -16.199 47.509 1.00 11.72 ? 315 CYS B SG 1 ATOM 5587 N N . GLU B 1 316 ? 43.167 -20.794 48.971 1.00 13.87 ? 316 GLU B N 1 ATOM 5588 C CA . GLU B 1 316 ? 42.481 -21.964 49.497 1.00 14.27 ? 316 GLU B CA 1 ATOM 5589 C C . GLU B 1 316 ? 43.216 -22.504 50.740 1.00 14.55 ? 316 GLU B C 1 ATOM 5590 O O . GLU B 1 316 ? 42.599 -22.844 51.753 1.00 13.96 ? 316 GLU B O 1 ATOM 5591 C CB . GLU B 1 316 ? 42.451 -23.031 48.413 1.00 15.40 ? 316 GLU B CB 1 ATOM 5592 C CG . GLU B 1 316 ? 41.942 -24.388 48.842 1.00 17.90 ? 316 GLU B CG 1 ATOM 5593 C CD . GLU B 1 316 ? 40.456 -24.436 49.015 1.00 22.93 ? 316 GLU B CD 1 ATOM 5594 O OE1 . GLU B 1 316 ? 39.759 -23.597 48.423 1.00 24.81 ? 316 GLU B OE1 1 ATOM 5595 O OE2 . GLU B 1 316 ? 39.978 -25.351 49.723 1.00 27.85 ? 316 GLU B OE2 1 ATOM 5596 N N . ALA B 1 317 ? 44.538 -22.591 50.654 1.00 13.72 ? 317 ALA B N 1 ATOM 5597 C CA . ALA B 1 317 ? 45.333 -23.183 51.746 1.00 13.56 ? 317 ALA B CA 1 ATOM 5598 C C . ALA B 1 317 ? 45.305 -22.350 53.031 1.00 13.44 ? 317 ALA B C 1 ATOM 5599 O O . ALA B 1 317 ? 45.474 -22.884 54.126 1.00 15.28 ? 317 ALA B O 1 ATOM 5600 C CB . ALA B 1 317 ? 46.770 -23.376 51.308 1.00 13.90 ? 317 ALA B CB 1 ATOM 5601 N N . THR B 1 318 ? 45.099 -21.042 52.894 1.00 13.07 ? 318 THR B N 1 ATOM 5602 C CA . THR B 1 318 ? 45.060 -20.143 54.038 1.00 13.19 ? 318 THR B CA 1 ATOM 5603 C C . THR B 1 318 ? 43.629 -19.903 54.514 1.00 13.33 ? 318 THR B C 1 ATOM 5604 O O . THR B 1 318 ? 43.399 -19.050 55.351 1.00 14.83 ? 318 THR B O 1 ATOM 5605 C CB . THR B 1 318 ? 45.796 -18.810 53.742 1.00 13.46 ? 318 THR B CB 1 ATOM 5606 O OG1 . THR B 1 318 ? 45.254 -18.211 52.552 1.00 14.58 ? 318 THR B OG1 1 ATOM 5607 C CG2 . THR B 1 318 ? 47.276 -19.044 53.499 1.00 13.55 ? 318 THR B CG2 1 ATOM 5608 N N . GLY B 1 319 ? 42.660 -20.663 54.013 1.00 13.08 ? 319 GLY B N 1 ATOM 5609 C CA . GLY B 1 319 ? 41.318 -20.667 54.588 1.00 12.99 ? 319 GLY B CA 1 ATOM 5610 C C . GLY B 1 319 ? 40.425 -19.541 54.093 1.00 12.61 ? 319 GLY B C 1 ATOM 5611 O O . GLY B 1 319 ? 39.449 -19.191 54.757 1.00 14.33 ? 319 GLY B O 1 ATOM 5612 N N . SER B 1 320 ? 40.727 -19.016 52.904 1.00 12.38 ? 320 SER B N 1 ATOM 5613 C CA . SER B 1 320 ? 39.959 -17.914 52.294 1.00 11.93 ? 320 SER B CA 1 ATOM 5614 C C . SER B 1 320 ? 38.745 -18.483 51.582 1.00 11.70 ? 320 SER B C 1 ATOM 5615 O O . SER B 1 320 ? 38.602 -18.428 50.341 1.00 11.79 ? 320 SER B O 1 ATOM 5616 C CB . SER B 1 320 ? 40.853 -17.124 51.321 1.00 12.15 ? 320 SER B CB 1 ATOM 5617 O OG . SER B 1 320 ? 42.116 -16.766 51.911 1.00 13.93 ? 320 SER B OG 1 ATOM 5618 N N . ARG B 1 321 ? 37.837 -19.021 52.383 1.00 12.79 ? 321 ARG B N 1 ATOM 5619 C CA . ARG B 1 321 ? 36.758 -19.814 51.810 1.00 13.23 ? 321 ARG B CA 1 ATOM 5620 C C . ARG B 1 321 ? 35.770 -19.013 50.981 1.00 12.40 ? 321 ARG B C 1 ATOM 5621 O O . ARG B 1 321 ? 35.396 -19.425 49.890 1.00 12.19 ? 321 ARG B O 1 ATOM 5622 C CB . ARG B 1 321 ? 36.011 -20.586 52.892 1.00 14.11 ? 321 ARG B CB 1 ATOM 5623 C CG . ARG B 1 321 ? 34.808 -21.370 52.389 1.00 16.52 ? 321 ARG B CG 1 ATOM 5624 C CD . ARG B 1 321 ? 34.220 -22.233 53.468 1.00 18.38 ? 321 ARG B CD 1 ATOM 5625 N NE . ARG B 1 321 ? 33.660 -21.458 54.561 1.00 21.11 ? 321 ARG B NE 1 ATOM 5626 C CZ . ARG B 1 321 ? 32.445 -20.898 54.556 1.00 21.37 ? 321 ARG B CZ 1 ATOM 5627 N NH1 . ARG B 1 321 ? 31.640 -20.999 53.496 1.00 22.51 ? 321 ARG B NH1 1 ATOM 5628 N NH2 . ARG B 1 321 ? 32.043 -20.215 55.618 1.00 20.18 ? 321 ARG B NH2 1 ATOM 5629 N N . LYS B 1 322 ? 35.289 -17.892 51.515 1.00 12.34 ? 322 LYS B N 1 ATOM 5630 C CA . LYS B 1 322 ? 34.341 -17.104 50.739 1.00 11.76 ? 322 LYS B CA 1 ATOM 5631 C C . LYS B 1 322 ? 34.991 -16.496 49.497 1.00 11.78 ? 322 LYS B C 1 ATOM 5632 O O . LYS B 1 322 ? 34.355 -16.405 48.467 1.00 11.78 ? 322 LYS B O 1 ATOM 5633 C CB . LYS B 1 322 ? 33.698 -16.024 51.593 1.00 11.93 ? 322 LYS B CB 1 ATOM 5634 C CG . LYS B 1 322 ? 32.835 -16.528 52.746 1.00 12.87 ? 322 LYS B CG 1 ATOM 5635 C CD . LYS B 1 322 ? 31.729 -17.427 52.308 1.00 15.08 ? 322 LYS B CD 1 ATOM 5636 C CE . LYS B 1 322 ? 30.639 -16.736 51.602 1.00 17.67 ? 322 LYS B CE 1 ATOM 5637 N NZ . LYS B 1 322 ? 29.649 -17.808 51.161 1.00 21.21 ? 322 LYS B NZ 1 ATOM 5638 N N . TYR B 1 323 ? 36.259 -16.120 49.576 1.00 10.52 ? 323 TYR B N 1 ATOM 5639 C CA . TYR B 1 323 ? 36.988 -15.654 48.390 1.00 11.12 ? 323 TYR B CA 1 ATOM 5640 C C . TYR B 1 323 ? 36.847 -16.674 47.255 1.00 10.44 ? 323 TYR B C 1 ATOM 5641 O O . TYR B 1 323 ? 36.512 -16.334 46.104 1.00 10.86 ? 323 TYR B O 1 ATOM 5642 C CB . TYR B 1 323 ? 38.462 -15.463 48.726 1.00 10.96 ? 323 TYR B CB 1 ATOM 5643 C CG . TYR B 1 323 ? 39.324 -15.132 47.544 1.00 10.65 ? 323 TYR B CG 1 ATOM 5644 C CD1 . TYR B 1 323 ? 39.351 -13.856 47.019 1.00 10.18 ? 323 TYR B CD1 1 ATOM 5645 C CD2 . TYR B 1 323 ? 40.106 -16.096 46.928 1.00 10.46 ? 323 TYR B CD2 1 ATOM 5646 C CE1 . TYR B 1 323 ? 40.141 -13.537 45.965 1.00 10.61 ? 323 TYR B CE1 1 ATOM 5647 C CE2 . TYR B 1 323 ? 40.922 -15.770 45.828 1.00 10.22 ? 323 TYR B CE2 1 ATOM 5648 C CZ . TYR B 1 323 ? 40.927 -14.479 45.368 1.00 10.50 ? 323 TYR B CZ 1 ATOM 5649 O OH . TYR B 1 323 ? 41.719 -14.063 44.323 1.00 11.25 ? 323 TYR B OH 1 ATOM 5650 N N . MET B 1 324 ? 37.103 -17.941 47.586 1.00 10.84 ? 324 MET B N 1 ATOM 5651 C CA . MET B 1 324 ? 37.035 -19.018 46.597 1.00 12.55 ? 324 MET B CA 1 ATOM 5652 C C . MET B 1 324 ? 35.610 -19.302 46.124 1.00 12.58 ? 324 MET B C 1 ATOM 5653 O O . MET B 1 324 ? 35.364 -19.434 44.918 1.00 15.22 ? 324 MET B O 1 ATOM 5654 C CB . MET B 1 324 ? 37.684 -20.278 47.159 1.00 13.29 ? 324 MET B CB 1 ATOM 5655 C CG . MET B 1 324 ? 39.173 -20.127 47.478 1.00 12.14 ? 324 MET B CG 1 ATOM 5656 S SD . MET B 1 324 ? 40.223 -19.683 46.050 1.00 14.45 ? 324 MET B SD 1 ATOM 5657 C CE . MET B 1 324 ? 40.053 -21.221 45.102 1.00 14.94 ? 324 MET B CE 1 ATOM 5658 N N . GLU B 1 325 ? 34.664 -19.384 47.049 1.00 12.51 ? 325 GLU B N 1 ATOM 5659 C CA . GLU B 1 325 ? 33.273 -19.683 46.691 1.00 13.75 ? 325 GLU B CA 1 ATOM 5660 C C . GLU B 1 325 ? 32.592 -18.585 45.886 1.00 13.34 ? 325 GLU B C 1 ATOM 5661 O O . GLU B 1 325 ? 31.671 -18.862 45.118 1.00 15.23 ? 325 GLU B O 1 ATOM 5662 C CB . GLU B 1 325 ? 32.443 -19.924 47.951 1.00 13.99 ? 325 GLU B CB 1 ATOM 5663 C CG . GLU B 1 325 ? 32.842 -21.146 48.778 1.00 15.53 ? 325 GLU B CG 1 ATOM 5664 C CD . GLU B 1 325 ? 31.967 -21.360 50.010 1.00 17.34 ? 325 GLU B CD 1 ATOM 5665 O OE1 . GLU B 1 325 ? 31.090 -20.522 50.308 1.00 22.15 ? 325 GLU B OE1 1 ATOM 5666 O OE2 . GLU B 1 325 ? 32.168 -22.397 50.664 1.00 23.78 ? 325 GLU B OE2 1 ATOM 5667 N N . LEU B 1 326 ? 33.028 -17.341 46.067 1.00 12.61 ? 326 LEU B N 1 ATOM 5668 C CA . LEU B 1 326 ? 32.377 -16.192 45.426 1.00 13.08 ? 326 LEU B CA 1 ATOM 5669 C C . LEU B 1 326 ? 33.033 -15.760 44.128 1.00 13.57 ? 326 LEU B C 1 ATOM 5670 O O . LEU B 1 326 ? 32.634 -14.734 43.556 1.00 15.75 ? 326 LEU B O 1 ATOM 5671 C CB . LEU B 1 326 ? 32.259 -15.025 46.400 1.00 12.63 ? 326 LEU B CB 1 ATOM 5672 C CG . LEU B 1 326 ? 31.358 -15.314 47.600 1.00 12.30 ? 326 LEU B CG 1 ATOM 5673 C CD1 . LEU B 1 326 ? 31.492 -14.209 48.618 1.00 14.06 ? 326 LEU B CD1 1 ATOM 5674 C CD2 . LEU B 1 326 ? 29.897 -15.475 47.173 1.00 13.07 ? 326 LEU B CD2 1 ATOM 5675 N N . GLY B 1 327 ? 34.006 -16.516 43.628 1.00 13.78 ? 327 GLY B N 1 ATOM 5676 C CA . GLY B 1 327 ? 34.576 -16.210 42.307 1.00 12.97 ? 327 GLY B CA 1 ATOM 5677 C C . GLY B 1 327 ? 36.032 -16.549 42.118 1.00 12.18 ? 327 GLY B C 1 ATOM 5678 O O . GLY B 1 327 ? 36.482 -16.747 40.989 1.00 13.07 ? 327 GLY B O 1 ATOM 5679 N N . ALA B 1 328 ? 36.777 -16.624 43.213 1.00 11.65 ? 328 ALA B N 1 ATOM 5680 C CA . ALA B 1 328 ? 38.191 -16.951 43.209 1.00 11.70 ? 328 ALA B CA 1 ATOM 5681 C C . ALA B 1 328 ? 39.006 -15.896 42.403 1.00 11.39 ? 328 ALA B C 1 ATOM 5682 O O . ALA B 1 328 ? 38.495 -14.798 42.100 1.00 11.73 ? 328 ALA B O 1 ATOM 5683 C CB . ALA B 1 328 ? 38.413 -18.389 42.709 1.00 11.97 ? 328 ALA B CB 1 ATOM 5684 N N . THR B 1 329 ? 40.251 -16.209 42.041 1.00 10.81 ? 329 THR B N 1 ATOM 5685 C CA . THR B 1 329 ? 41.115 -15.225 41.404 1.00 10.67 ? 329 THR B CA 1 ATOM 5686 C C . THR B 1 329 ? 40.556 -14.839 40.031 1.00 10.58 ? 329 THR B C 1 ATOM 5687 O O . THR B 1 329 ? 40.611 -13.660 39.635 1.00 10.98 ? 329 THR B O 1 ATOM 5688 C CB . THR B 1 329 ? 42.561 -15.725 41.399 1.00 10.66 ? 329 THR B CB 1 ATOM 5689 O OG1 . THR B 1 329 ? 42.985 -15.944 42.747 1.00 11.16 ? 329 THR B OG1 1 ATOM 5690 C CG2 . THR B 1 329 ? 43.514 -14.699 40.838 1.00 11.62 ? 329 THR B CG2 1 ATOM 5691 N N . GLN B 1 330 ? 39.987 -15.808 39.320 1.00 10.98 ? 330 GLN B N 1 ATOM 5692 C CA . GLN B 1 330 ? 39.327 -15.501 38.055 1.00 11.03 ? 330 GLN B CA 1 ATOM 5693 C C . GLN B 1 330 ? 38.216 -14.473 38.237 1.00 10.93 ? 330 GLN B C 1 ATOM 5694 O O . GLN B 1 330 ? 38.111 -13.534 37.446 1.00 10.77 ? 330 GLN B O 1 ATOM 5695 C CB . GLN B 1 330 ? 38.750 -16.756 37.391 1.00 11.79 ? 330 GLN B CB 1 ATOM 5696 C CG . GLN B 1 330 ? 38.007 -16.456 36.088 1.00 12.55 ? 330 GLN B CG 1 ATOM 5697 C CD . GLN B 1 330 ? 37.600 -17.689 35.313 1.00 13.01 ? 330 GLN B CD 1 ATOM 5698 O OE1 . GLN B 1 330 ? 38.212 -18.735 35.439 1.00 14.52 ? 330 GLN B OE1 1 ATOM 5699 N NE2 . GLN B 1 330 ? 36.541 -17.567 34.536 1.00 12.16 ? 330 GLN B NE2 1 ATOM 5700 N N . GLY B 1 331 ? 37.382 -14.649 39.256 1.00 11.14 ? 331 GLY B N 1 ATOM 5701 C CA . GLY B 1 331 ? 36.299 -13.707 39.496 1.00 11.26 ? 331 GLY B CA 1 ATOM 5702 C C . GLY B 1 331 ? 36.807 -12.332 39.841 1.00 11.15 ? 331 GLY B C 1 ATOM 5703 O O . GLY B 1 331 ? 36.279 -11.339 39.360 1.00 12.41 ? 331 GLY B O 1 ATOM 5704 N N . MET B 1 332 ? 37.838 -12.253 40.679 1.00 10.74 ? 332 MET B N 1 ATOM 5705 C CA . MET B 1 332 ? 38.425 -10.945 40.990 1.00 10.86 ? 332 MET B CA 1 ATOM 5706 C C . MET B 1 332 ? 38.893 -10.275 39.706 1.00 10.34 ? 332 MET B C 1 ATOM 5707 O O . MET B 1 332 ? 38.636 -9.091 39.462 1.00 11.64 ? 332 MET B O 1 ATOM 5708 C CB . MET B 1 332 ? 39.603 -11.108 41.940 1.00 11.05 ? 332 MET B CB 1 ATOM 5709 C CG . MET B 1 332 ? 40.258 -9.764 42.339 1.00 10.67 ? 332 MET B CG 1 ATOM 5710 S SD . MET B 1 332 ? 39.438 -8.790 43.640 1.00 12.10 ? 332 MET B SD 1 ATOM 5711 C CE . MET B 1 332 ? 38.225 -7.837 42.746 1.00 12.48 ? 332 MET B CE 1 ATOM 5712 N N . GLY B 1 333 ? 39.589 -11.036 38.876 1.00 10.39 ? 333 GLY B N 1 ATOM 5713 C CA . GLY B 1 333 ? 40.097 -10.510 37.619 1.00 10.30 ? 333 GLY B CA 1 ATOM 5714 C C . GLY B 1 333 ? 39.009 -10.084 36.649 1.00 9.68 ? 333 GLY B C 1 ATOM 5715 O O . GLY B 1 333 ? 39.192 -9.134 35.873 1.00 10.14 ? 333 GLY B O 1 ATOM 5716 N N . GLU B 1 334 ? 37.872 -10.753 36.678 1.00 9.54 ? 334 GLU B N 1 ATOM 5717 C CA . GLU B 1 334 ? 36.756 -10.343 35.820 1.00 10.23 ? 334 GLU B CA 1 ATOM 5718 C C . GLU B 1 334 ? 36.206 -8.988 36.228 1.00 10.21 ? 334 GLU B C 1 ATOM 5719 O O . GLU B 1 334 ? 35.895 -8.161 35.377 1.00 10.81 ? 334 GLU B O 1 ATOM 5720 C CB . GLU B 1 334 ? 35.674 -11.425 35.822 1.00 10.45 ? 334 GLU B CB 1 ATOM 5721 C CG . GLU B 1 334 ? 36.099 -12.630 34.969 1.00 11.67 ? 334 GLU B CG 1 ATOM 5722 C CD . GLU B 1 334 ? 35.291 -13.898 35.131 1.00 13.52 ? 334 GLU B CD 1 ATOM 5723 O OE1 . GLU B 1 334 ? 34.501 -13.992 36.076 1.00 17.82 ? 334 GLU B OE1 1 ATOM 5724 O OE2 . GLU B 1 334 ? 35.493 -14.815 34.295 1.00 14.12 ? 334 GLU B OE2 1 ATOM 5725 N N . ALA B 1 335 ? 36.166 -8.719 37.532 1.00 10.34 ? 335 ALA B N 1 ATOM 5726 C CA . ALA B 1 335 ? 35.849 -7.375 38.010 1.00 10.03 ? 335 ALA B CA 1 ATOM 5727 C C . ALA B 1 335 ? 36.868 -6.355 37.553 1.00 9.60 ? 335 ALA B C 1 ATOM 5728 O O . ALA B 1 335 ? 36.527 -5.269 37.084 1.00 10.52 ? 335 ALA B O 1 ATOM 5729 C CB . ALA B 1 335 ? 35.719 -7.368 39.547 1.00 10.62 ? 335 ALA B CB 1 ATOM 5730 N N . LEU B 1 336 ? 38.142 -6.692 37.725 1.00 9.55 ? 336 LEU B N 1 ATOM 5731 C CA . LEU B 1 336 ? 39.203 -5.792 37.328 1.00 9.97 ? 336 LEU B CA 1 ATOM 5732 C C . LEU B 1 336 ? 39.096 -5.444 35.850 1.00 10.28 ? 336 LEU B C 1 ATOM 5733 O O . LEU B 1 336 ? 39.280 -4.283 35.466 1.00 11.07 ? 336 LEU B O 1 ATOM 5734 C CB . LEU B 1 336 ? 40.597 -6.319 37.658 1.00 10.33 ? 336 LEU B CB 1 ATOM 5735 C CG . LEU B 1 336 ? 40.891 -6.601 39.126 1.00 13.12 ? 336 LEU B CG 1 ATOM 5736 C CD1 . LEU B 1 336 ? 42.306 -7.087 39.296 1.00 14.49 ? 336 LEU B CD1 1 ATOM 5737 C CD2 . LEU B 1 336 ? 40.666 -5.446 39.980 1.00 16.76 ? 336 LEU B CD2 1 ATOM 5738 N N . THR B 1 337 ? 38.801 -6.446 35.022 1.00 10.30 ? 337 THR B N 1 ATOM 5739 C CA . THR B 1 337 ? 38.651 -6.238 33.582 1.00 10.90 ? 337 THR B CA 1 ATOM 5740 C C . THR B 1 337 ? 37.446 -5.395 33.224 1.00 10.32 ? 337 THR B C 1 ATOM 5741 O O . THR B 1 337 ? 37.521 -4.558 32.317 1.00 10.95 ? 337 THR B O 1 ATOM 5742 C CB . THR B 1 337 ? 38.561 -7.626 32.919 1.00 10.39 ? 337 THR B CB 1 ATOM 5743 O OG1 . THR B 1 337 ? 39.837 -8.280 33.028 1.00 12.64 ? 337 THR B OG1 1 ATOM 5744 C CG2 . THR B 1 337 ? 38.258 -7.528 31.419 1.00 11.38 ? 337 THR B CG2 1 ATOM 5745 N N . ARG B 1 338 ? 36.333 -5.597 33.928 1.00 10.65 ? 338 ARG B N 1 ATOM 5746 C CA . ARG B 1 338 ? 35.153 -4.747 33.694 1.00 10.86 ? 338 ARG B CA 1 ATOM 5747 C C . ARG B 1 338 ? 35.466 -3.289 33.961 1.00 11.01 ? 338 ARG B C 1 ATOM 5748 O O . ARG B 1 338 ? 34.913 -2.421 33.288 1.00 12.46 ? 338 ARG B O 1 ATOM 5749 C CB . ARG B 1 338 ? 33.942 -5.187 34.530 1.00 10.80 ? 338 ARG B CB 1 ATOM 5750 C CG . ARG B 1 338 ? 33.306 -6.493 34.053 1.00 10.84 ? 338 ARG B CG 1 ATOM 5751 C CD . ARG B 1 338 ? 32.034 -6.805 34.748 1.00 11.41 ? 338 ARG B CD 1 ATOM 5752 N NE . ARG B 1 338 ? 32.195 -6.996 36.192 1.00 11.79 ? 338 ARG B NE 1 ATOM 5753 C CZ . ARG B 1 338 ? 32.424 -8.152 36.819 1.00 10.98 ? 338 ARG B CZ 1 ATOM 5754 N NH1 . ARG B 1 338 ? 32.561 -9.307 36.159 1.00 11.75 ? 338 ARG B NH1 1 ATOM 5755 N NH2 . ARG B 1 338 ? 32.485 -8.157 38.134 1.00 12.26 ? 338 ARG B NH2 1 ATOM 5756 N N . GLY B 1 339 ? 36.348 -3.028 34.922 1.00 11.26 ? 339 GLY B N 1 ATOM 5757 C CA . GLY B 1 339 ? 36.726 -1.664 35.278 1.00 10.58 ? 339 GLY B CA 1 ATOM 5758 C C . GLY B 1 339 ? 36.393 -1.329 36.713 1.00 10.13 ? 339 GLY B C 1 ATOM 5759 O O . GLY B 1 339 ? 35.304 -1.628 37.188 1.00 10.56 ? 339 GLY B O 1 ATOM 5760 N N . MET B 1 340 ? 37.331 -0.669 37.396 1.00 9.85 ? 340 MET B N 1 ATOM 5761 C CA . MET B 1 340 ? 37.190 -0.345 38.813 1.00 9.93 ? 340 MET B CA 1 ATOM 5762 C C . MET B 1 340 ? 37.592 1.087 39.092 1.00 9.63 ? 340 MET B C 1 ATOM 5763 O O . MET B 1 340 ? 38.304 1.702 38.308 1.00 9.87 ? 340 MET B O 1 ATOM 5764 C CB A MET B 1 340 ? 38.115 -1.224 39.677 0.50 10.03 ? 340 MET B CB 1 ATOM 5765 C CB B MET B 1 340 ? 37.900 -1.394 39.691 0.50 10.78 ? 340 MET B CB 1 ATOM 5766 C CG A MET B 1 340 ? 38.068 -2.709 39.395 0.50 9.07 ? 340 MET B CG 1 ATOM 5767 C CG B MET B 1 340 ? 37.253 -2.787 39.505 0.50 12.10 ? 340 MET B CG 1 ATOM 5768 S SD A MET B 1 340 ? 36.603 -3.457 40.181 0.50 7.70 ? 340 MET B SD 1 ATOM 5769 S SD B MET B 1 340 ? 37.838 -4.151 40.495 0.50 14.68 ? 340 MET B SD 1 ATOM 5770 C CE A MET B 1 340 ? 37.240 -3.636 41.858 0.50 8.11 ? 340 MET B CE 1 ATOM 5771 C CE B MET B 1 340 ? 37.251 -3.701 42.112 0.50 14.90 ? 340 MET B CE 1 ATOM 5772 N N . VAL B 1 341 ? 37.069 1.608 40.200 1.00 8.88 ? 341 VAL B N 1 ATOM 5773 C CA . VAL B 1 341 ? 37.352 2.962 40.667 1.00 9.10 ? 341 VAL B CA 1 ATOM 5774 C C . VAL B 1 341 ? 38.388 2.904 41.779 1.00 8.71 ? 341 VAL B C 1 ATOM 5775 O O . VAL B 1 341 ? 38.326 2.030 42.653 1.00 9.34 ? 341 VAL B O 1 ATOM 5776 C CB . VAL B 1 341 ? 36.045 3.625 41.180 1.00 9.02 ? 341 VAL B CB 1 ATOM 5777 C CG1 . VAL B 1 341 ? 36.287 4.974 41.838 1.00 9.78 ? 341 VAL B CG1 1 ATOM 5778 C CG2 . VAL B 1 341 ? 35.033 3.755 40.033 1.00 11.24 ? 341 VAL B CG2 1 ATOM 5779 N N . LEU B 1 342 ? 39.343 3.829 41.737 1.00 8.47 ? 342 LEU B N 1 ATOM 5780 C CA . LEU B 1 342 ? 40.386 3.979 42.727 1.00 8.52 ? 342 LEU B CA 1 ATOM 5781 C C . LEU B 1 342 ? 39.936 4.844 43.896 1.00 8.13 ? 342 LEU B C 1 ATOM 5782 O O . LEU B 1 342 ? 39.508 5.981 43.719 1.00 9.26 ? 342 LEU B O 1 ATOM 5783 C CB . LEU B 1 342 ? 41.634 4.584 42.081 1.00 9.59 ? 342 LEU B CB 1 ATOM 5784 C CG . LEU B 1 342 ? 42.832 4.723 43.020 1.00 9.70 ? 342 LEU B CG 1 ATOM 5785 C CD1 . LEU B 1 342 ? 43.414 3.363 43.376 1.00 10.86 ? 342 LEU B CD1 1 ATOM 5786 C CD2 . LEU B 1 342 ? 43.900 5.588 42.387 1.00 10.72 ? 342 LEU B CD2 1 ATOM 5787 N N . ALA B 1 343 ? 39.982 4.227 45.079 1.00 8.19 ? 343 ALA B N 1 ATOM 5788 C CA . ALA B 1 343 ? 39.671 4.830 46.361 1.00 7.97 ? 343 ALA B CA 1 ATOM 5789 C C . ALA B 1 343 ? 40.933 4.891 47.220 1.00 8.15 ? 343 ALA B C 1 ATOM 5790 O O . ALA B 1 343 ? 41.725 3.954 47.233 1.00 8.63 ? 343 ALA B O 1 ATOM 5791 C CB . ALA B 1 343 ? 38.575 4.037 47.091 1.00 8.94 ? 343 ALA B CB 1 ATOM 5792 N N . MET B 1 344 ? 41.098 6.004 47.920 1.00 8.17 ? 344 MET B N 1 ATOM 5793 C CA . MET B 1 344 ? 42.245 6.212 48.830 1.00 7.98 ? 344 MET B CA 1 ATOM 5794 C C . MET B 1 344 ? 41.707 6.785 50.137 1.00 8.05 ? 344 MET B C 1 ATOM 5795 O O . MET B 1 344 ? 40.854 7.670 50.118 1.00 9.07 ? 344 MET B O 1 ATOM 5796 C CB . MET B 1 344 ? 43.299 7.107 48.176 1.00 7.96 ? 344 MET B CB 1 ATOM 5797 C CG . MET B 1 344 ? 44.010 6.391 47.035 1.00 8.75 ? 344 MET B CG 1 ATOM 5798 S SD . MET B 1 344 ? 44.977 7.462 45.999 1.00 10.74 ? 344 MET B SD 1 ATOM 5799 C CE . MET B 1 344 ? 43.662 8.327 45.125 1.00 10.18 ? 344 MET B CE 1 ATOM 5800 N N . SER B 1 345 ? 42.133 6.241 51.267 1.00 8.28 ? 345 SER B N 1 ATOM 5801 C CA . SER B 1 345 ? 41.604 6.678 52.562 1.00 8.52 ? 345 SER B CA 1 ATOM 5802 C C . SER B 1 345 ? 42.618 6.508 53.665 1.00 7.68 ? 345 SER B C 1 ATOM 5803 O O . SER B 1 345 ? 43.673 5.882 53.499 1.00 8.36 ? 345 SER B O 1 ATOM 5804 C CB . SER B 1 345 ? 40.341 5.891 52.929 1.00 9.18 ? 345 SER B CB 1 ATOM 5805 O OG . SER B 1 345 ? 40.657 4.542 53.215 1.00 9.61 ? 345 SER B OG 1 ATOM 5806 N N . ILE B 1 346 ? 42.291 7.106 54.794 1.00 8.63 ? 346 ILE B N 1 ATOM 5807 C CA . ILE B 1 346 ? 43.075 6.926 56.011 1.00 8.19 ? 346 ILE B CA 1 ATOM 5808 C C . ILE B 1 346 ? 42.044 6.777 57.142 1.00 8.09 ? 346 ILE B C 1 ATOM 5809 O O . ILE B 1 346 ? 41.121 7.584 57.237 1.00 8.88 ? 346 ILE B O 1 ATOM 5810 C CB . ILE B 1 346 ? 44.088 8.091 56.213 1.00 8.57 ? 346 ILE B CB 1 ATOM 5811 C CG1 . ILE B 1 346 ? 44.980 7.810 57.414 1.00 8.88 ? 346 ILE B CG1 1 ATOM 5812 C CG2 . ILE B 1 346 ? 43.382 9.460 56.352 1.00 8.18 ? 346 ILE B CG2 1 ATOM 5813 C CD1 . ILE B 1 346 ? 46.161 8.754 57.495 1.00 9.86 ? 346 ILE B CD1 1 ATOM 5814 N N . TRP B 1 347 ? 42.205 5.758 57.975 1.00 8.12 ? 347 TRP B N 1 ATOM 5815 C CA . TRP B 1 347 ? 41.221 5.458 58.987 1.00 8.60 ? 347 TRP B CA 1 ATOM 5816 C C . TRP B 1 347 ? 41.786 4.699 60.180 1.00 8.81 ? 347 TRP B C 1 ATOM 5817 O O . TRP B 1 347 ? 42.873 4.139 60.101 1.00 9.55 ? 347 TRP B O 1 ATOM 5818 C CB . TRP B 1 347 ? 40.002 4.753 58.350 1.00 8.82 ? 347 TRP B CB 1 ATOM 5819 C CG . TRP B 1 347 ? 40.211 3.402 57.754 1.00 9.19 ? 347 TRP B CG 1 ATOM 5820 C CD1 . TRP B 1 347 ? 40.772 3.122 56.549 1.00 9.78 ? 347 TRP B CD1 1 ATOM 5821 C CD2 . TRP B 1 347 ? 39.742 2.162 58.277 1.00 9.87 ? 347 TRP B CD2 1 ATOM 5822 N NE1 . TRP B 1 347 ? 40.715 1.779 56.304 1.00 9.71 ? 347 TRP B NE1 1 ATOM 5823 C CE2 . TRP B 1 347 ? 40.062 1.164 57.348 1.00 8.62 ? 347 TRP B CE2 1 ATOM 5824 C CE3 . TRP B 1 347 ? 39.056 1.792 59.445 1.00 10.24 ? 347 TRP B CE3 1 ATOM 5825 C CZ2 . TRP B 1 347 ? 39.746 -0.181 57.560 1.00 10.94 ? 347 TRP B CZ2 1 ATOM 5826 C CZ3 . TRP B 1 347 ? 38.747 0.458 59.641 1.00 10.09 ? 347 TRP B CZ3 1 ATOM 5827 C CH2 . TRP B 1 347 ? 39.091 -0.504 58.711 1.00 10.28 ? 347 TRP B CH2 1 ATOM 5828 N N . TRP B 1 348 ? 41.030 4.688 61.278 1.00 8.73 ? 348 TRP B N 1 ATOM 5829 C CA . TRP B 1 348 ? 41.381 3.901 62.463 1.00 9.11 ? 348 TRP B CA 1 ATOM 5830 C C . TRP B 1 348 ? 40.142 3.154 62.954 1.00 9.94 ? 348 TRP B C 1 ATOM 5831 O O . TRP B 1 348 ? 39.054 3.308 62.406 1.00 10.52 ? 348 TRP B O 1 ATOM 5832 C CB . TRP B 1 348 ? 42.041 4.750 63.567 1.00 9.20 ? 348 TRP B CB 1 ATOM 5833 C CG . TRP B 1 348 ? 41.229 5.831 64.213 1.00 10.21 ? 348 TRP B CG 1 ATOM 5834 C CD1 . TRP B 1 348 ? 39.885 6.014 64.143 1.00 11.48 ? 348 TRP B CD1 1 ATOM 5835 C CD2 . TRP B 1 348 ? 41.745 6.885 65.005 1.00 9.84 ? 348 TRP B CD2 1 ATOM 5836 N NE1 . TRP B 1 348 ? 39.524 7.120 64.872 1.00 11.86 ? 348 TRP B NE1 1 ATOM 5837 C CE2 . TRP B 1 348 ? 40.651 7.671 65.420 1.00 10.15 ? 348 TRP B CE2 1 ATOM 5838 C CE3 . TRP B 1 348 ? 43.020 7.248 65.424 1.00 10.76 ? 348 TRP B CE3 1 ATOM 5839 C CZ2 . TRP B 1 348 ? 40.797 8.820 66.196 1.00 10.38 ? 348 TRP B CZ2 1 ATOM 5840 C CZ3 . TRP B 1 348 ? 43.161 8.375 66.209 1.00 10.73 ? 348 TRP B CZ3 1 ATOM 5841 C CH2 . TRP B 1 348 ? 42.062 9.149 66.589 1.00 10.68 ? 348 TRP B CH2 1 ATOM 5842 N N . ASP B 1 349 ? 40.329 2.326 63.966 1.00 9.96 ? 349 ASP B N 1 ATOM 5843 C CA . ASP B 1 349 ? 39.332 1.324 64.338 1.00 10.96 ? 349 ASP B CA 1 ATOM 5844 C C . ASP B 1 349 ? 39.128 1.307 65.850 1.00 12.03 ? 349 ASP B C 1 ATOM 5845 O O . ASP B 1 349 ? 39.843 0.639 66.570 1.00 11.98 ? 349 ASP B O 1 ATOM 5846 C CB . ASP B 1 349 ? 39.841 -0.027 63.824 1.00 11.41 ? 349 ASP B CB 1 ATOM 5847 C CG . ASP B 1 349 ? 39.008 -1.228 64.242 1.00 12.15 ? 349 ASP B CG 1 ATOM 5848 O OD1 . ASP B 1 349 ? 37.826 -1.076 64.611 1.00 14.92 ? 349 ASP B OD1 1 ATOM 5849 O OD2 . ASP B 1 349 ? 39.502 -2.389 64.149 1.00 12.27 ? 349 ASP B OD2 1 ATOM 5850 N N . GLN B 1 350 ? 38.125 2.045 66.313 1.00 12.73 ? 350 GLN B N 1 ATOM 5851 C CA . GLN B 1 350 ? 37.817 2.094 67.725 1.00 14.65 ? 350 GLN B CA 1 ATOM 5852 C C . GLN B 1 350 ? 37.402 0.731 68.289 1.00 14.56 ? 350 GLN B C 1 ATOM 5853 O O . GLN B 1 350 ? 37.797 0.370 69.400 1.00 15.62 ? 350 GLN B O 1 ATOM 5854 C CB . GLN B 1 350 ? 36.695 3.094 67.969 1.00 15.98 ? 350 GLN B CB 1 ATOM 5855 C CG . GLN B 1 350 ? 36.649 3.588 69.357 1.00 21.25 ? 350 GLN B CG 1 ATOM 5856 C CD . GLN B 1 350 ? 37.795 4.583 69.573 1.00 24.87 ? 350 GLN B CD 1 ATOM 5857 O OE1 . GLN B 1 350 ? 38.644 4.326 70.362 1.00 25.82 ? 350 GLN B OE1 1 ATOM 5858 N NE2 . GLN B 1 350 ? 37.822 5.696 68.804 1.00 29.89 ? 350 GLN B NE2 1 ATOM 5859 N N . GLY B 1 351 ? 36.650 -0.038 67.525 1.00 14.83 ? 351 GLY B N 1 ATOM 5860 C CA . GLY B 1 351 ? 36.179 -1.328 68.027 1.00 16.74 ? 351 GLY B CA 1 ATOM 5861 C C . GLY B 1 351 ? 37.243 -2.397 68.231 1.00 18.11 ? 351 GLY B C 1 ATOM 5862 O O . GLY B 1 351 ? 37.219 -3.134 69.209 1.00 21.30 ? 351 GLY B O 1 ATOM 5863 N N . GLY B 1 352 ? 38.183 -2.463 67.314 1.00 16.30 ? 352 GLY B N 1 ATOM 5864 C CA . GLY B 1 352 ? 39.072 -3.594 67.166 1.00 14.26 ? 352 GLY B CA 1 ATOM 5865 C C . GLY B 1 352 ? 40.552 -3.289 67.004 1.00 12.46 ? 352 GLY B C 1 ATOM 5866 O O . GLY B 1 352 ? 41.337 -4.217 66.791 1.00 12.20 ? 352 GLY B O 1 ATOM 5867 N N . ASN B 1 353 ? 40.925 -2.004 67.034 1.00 11.03 ? 353 ASN B N 1 ATOM 5868 C CA . ASN B 1 353 ? 42.303 -1.565 67.004 1.00 11.30 ? 353 ASN B CA 1 ATOM 5869 C C . ASN B 1 353 ? 43.080 -1.977 65.740 1.00 10.55 ? 353 ASN B C 1 ATOM 5870 O O . ASN B 1 353 ? 44.306 -1.923 65.728 1.00 10.61 ? 353 ASN B O 1 ATOM 5871 C CB . ASN B 1 353 ? 43.071 -2.058 68.263 1.00 10.36 ? 353 ASN B CB 1 ATOM 5872 C CG . ASN B 1 353 ? 42.537 -1.512 69.559 1.00 11.22 ? 353 ASN B CG 1 ATOM 5873 O OD1 . ASN B 1 353 ? 42.917 -2.010 70.643 1.00 15.19 ? 353 ASN B OD1 1 ATOM 5874 N ND2 . ASN B 1 353 ? 41.658 -0.534 69.498 1.00 9.67 ? 353 ASN B ND2 1 ATOM 5875 N N . MET B 1 354 ? 42.385 -2.342 64.674 1.00 10.04 ? 354 MET B N 1 ATOM 5876 C CA . MET B 1 354 ? 43.043 -2.759 63.416 1.00 10.16 ? 354 MET B CA 1 ATOM 5877 C C . MET B 1 354 ? 43.973 -3.951 63.634 1.00 10.36 ? 354 MET B C 1 ATOM 5878 O O . MET B 1 354 ? 44.941 -4.127 62.915 1.00 10.60 ? 354 MET B O 1 ATOM 5879 C CB . MET B 1 354 ? 43.823 -1.609 62.757 1.00 10.28 ? 354 MET B CB 1 ATOM 5880 C CG . MET B 1 354 ? 43.770 -1.608 61.237 1.00 9.96 ? 354 MET B CG 1 ATOM 5881 S SD . MET B 1 354 ? 42.191 -1.119 60.518 1.00 10.33 ? 354 MET B SD 1 ATOM 5882 C CE . MET B 1 354 ? 42.124 0.607 61.037 1.00 10.60 ? 354 MET B CE 1 ATOM 5883 N N . GLU B 1 355 ? 43.635 -4.809 64.594 1.00 10.47 ? 355 GLU B N 1 ATOM 5884 C CA . GLU B 1 355 ? 44.549 -5.896 64.960 1.00 10.58 ? 355 GLU B CA 1 ATOM 5885 C C . GLU B 1 355 ? 44.845 -6.836 63.802 1.00 9.65 ? 355 GLU B C 1 ATOM 5886 O O . GLU B 1 355 ? 45.937 -7.397 63.716 1.00 10.20 ? 355 GLU B O 1 ATOM 5887 C CB . GLU B 1 355 ? 44.009 -6.725 66.138 1.00 10.84 ? 355 GLU B CB 1 ATOM 5888 C CG . GLU B 1 355 ? 44.077 -6.011 67.469 1.00 12.13 ? 355 GLU B CG 1 ATOM 5889 C CD . GLU B 1 355 ? 43.555 -6.844 68.621 1.00 13.50 ? 355 GLU B CD 1 ATOM 5890 O OE1 . GLU B 1 355 ? 43.142 -7.986 68.397 1.00 16.59 ? 355 GLU B OE1 1 ATOM 5891 O OE2 . GLU B 1 355 ? 43.579 -6.342 69.757 1.00 16.02 ? 355 GLU B OE2 1 ATOM 5892 N N . TRP B 1 356 ? 43.872 -7.046 62.917 1.00 10.24 ? 356 TRP B N 1 ATOM 5893 C CA . TRP B 1 356 ? 44.056 -7.931 61.770 1.00 9.93 ? 356 TRP B CA 1 ATOM 5894 C C . TRP B 1 356 ? 45.160 -7.425 60.820 1.00 9.73 ? 356 TRP B C 1 ATOM 5895 O O . TRP B 1 356 ? 45.645 -8.209 59.979 1.00 10.11 ? 356 TRP B O 1 ATOM 5896 C CB . TRP B 1 356 ? 42.731 -8.058 60.995 1.00 10.98 ? 356 TRP B CB 1 ATOM 5897 C CG . TRP B 1 356 ? 42.248 -6.724 60.459 1.00 10.74 ? 356 TRP B CG 1 ATOM 5898 C CD1 . TRP B 1 356 ? 41.390 -5.857 61.070 1.00 12.28 ? 356 TRP B CD1 1 ATOM 5899 C CD2 . TRP B 1 356 ? 42.619 -6.099 59.224 1.00 10.06 ? 356 TRP B CD2 1 ATOM 5900 N NE1 . TRP B 1 356 ? 41.197 -4.741 60.294 1.00 11.73 ? 356 TRP B NE1 1 ATOM 5901 C CE2 . TRP B 1 356 ? 41.945 -4.864 59.152 1.00 10.73 ? 356 TRP B CE2 1 ATOM 5902 C CE3 . TRP B 1 356 ? 43.434 -6.474 58.153 1.00 11.48 ? 356 TRP B CE3 1 ATOM 5903 C CZ2 . TRP B 1 356 ? 42.087 -3.990 58.076 1.00 12.66 ? 356 TRP B CZ2 1 ATOM 5904 C CZ3 . TRP B 1 356 ? 43.573 -5.609 57.089 1.00 12.74 ? 356 TRP B CZ3 1 ATOM 5905 C CH2 . TRP B 1 356 ? 42.890 -4.390 57.047 1.00 12.30 ? 356 TRP B CH2 1 ATOM 5906 N N . LEU B 1 357 ? 45.494 -6.134 60.898 1.00 10.13 ? 357 LEU B N 1 ATOM 5907 C CA . LEU B 1 357 ? 46.505 -5.560 60.019 1.00 10.04 ? 357 LEU B CA 1 ATOM 5908 C C . LEU B 1 357 ? 47.917 -5.768 60.582 1.00 10.37 ? 357 LEU B C 1 ATOM 5909 O O . LEU B 1 357 ? 48.823 -6.116 59.827 1.00 10.43 ? 357 LEU B O 1 ATOM 5910 C CB . LEU B 1 357 ? 46.230 -4.071 59.790 1.00 10.10 ? 357 LEU B CB 1 ATOM 5911 C CG . LEU B 1 357 ? 47.222 -3.334 58.898 1.00 10.28 ? 357 LEU B CG 1 ATOM 5912 C CD1 . LEU B 1 357 ? 47.387 -3.993 57.537 1.00 12.26 ? 357 LEU B CD1 1 ATOM 5913 C CD2 . LEU B 1 357 ? 46.829 -1.880 58.777 1.00 11.45 ? 357 LEU B CD2 1 ATOM 5914 N N . ASP B 1 358 ? 48.123 -5.541 61.890 1.00 9.57 ? 358 ASP B N 1 ATOM 5915 C CA . ASP B 1 358 ? 49.491 -5.361 62.406 1.00 10.58 ? 358 ASP B CA 1 ATOM 5916 C C . ASP B 1 358 ? 49.771 -5.986 63.769 1.00 10.34 ? 358 ASP B C 1 ATOM 5917 O O . ASP B 1 358 ? 50.814 -5.706 64.356 1.00 11.03 ? 358 ASP B O 1 ATOM 5918 C CB . ASP B 1 358 ? 49.839 -3.871 62.442 1.00 11.06 ? 358 ASP B CB 1 ATOM 5919 C CG . ASP B 1 358 ? 48.886 -3.064 63.276 1.00 11.01 ? 358 ASP B CG 1 ATOM 5920 O OD1 . ASP B 1 358 ? 48.295 -3.646 64.224 1.00 10.82 ? 358 ASP B OD1 1 ATOM 5921 O OD2 . ASP B 1 358 ? 48.703 -1.833 63.029 1.00 10.54 ? 358 ASP B OD2 1 ATOM 5922 N N . HIS B 1 359 ? 48.873 -6.845 64.250 1.00 10.95 ? 359 HIS B N 1 ATOM 5923 C CA . HIS B 1 359 ? 48.995 -7.448 65.587 1.00 11.43 ? 359 HIS B CA 1 ATOM 5924 C C . HIS B 1 359 ? 48.962 -8.969 65.505 1.00 12.05 ? 359 HIS B C 1 ATOM 5925 O O . HIS B 1 359 ? 48.222 -9.547 64.704 1.00 12.25 ? 359 HIS B O 1 ATOM 5926 C CB . HIS B 1 359 ? 47.836 -6.973 66.489 1.00 11.90 ? 359 HIS B CB 1 ATOM 5927 C CG . HIS B 1 359 ? 47.755 -7.689 67.805 1.00 12.00 ? 359 HIS B CG 1 ATOM 5928 N ND1 . HIS B 1 359 ? 48.662 -7.491 68.828 1.00 12.07 ? 359 HIS B ND1 1 ATOM 5929 C CD2 . HIS B 1 359 ? 46.904 -8.643 68.247 1.00 13.47 ? 359 HIS B CD2 1 ATOM 5930 C CE1 . HIS B 1 359 ? 48.348 -8.270 69.852 1.00 14.63 ? 359 HIS B CE1 1 ATOM 5931 N NE2 . HIS B 1 359 ? 47.287 -8.975 69.532 1.00 14.30 ? 359 HIS B NE2 1 ATOM 5932 N N . GLY B 1 360 ? 49.691 -9.623 66.408 1.00 12.99 ? 360 GLY B N 1 ATOM 5933 C CA . GLY B 1 360 ? 49.589 -11.080 66.556 1.00 13.75 ? 360 GLY B CA 1 ATOM 5934 C C . GLY B 1 360 ? 50.178 -11.791 65.365 1.00 13.82 ? 360 GLY B C 1 ATOM 5935 O O . GLY B 1 360 ? 51.378 -11.654 65.079 1.00 15.67 ? 360 GLY B O 1 ATOM 5936 N N . GLU B 1 361 ? 49.325 -12.514 64.649 1.00 14.21 ? 361 GLU B N 1 ATOM 5937 C CA . GLU B 1 361 ? 49.750 -13.219 63.431 1.00 14.39 ? 361 GLU B CA 1 ATOM 5938 C C . GLU B 1 361 ? 50.155 -12.239 62.344 1.00 14.13 ? 361 GLU B C 1 ATOM 5939 O O . GLU B 1 361 ? 50.888 -12.587 61.417 1.00 13.73 ? 361 GLU B O 1 ATOM 5940 C CB . GLU B 1 361 ? 48.618 -14.084 62.879 1.00 17.09 ? 361 GLU B CB 1 ATOM 5941 C CG . GLU B 1 361 ? 48.051 -15.078 63.878 1.00 21.14 ? 361 GLU B CG 1 ATOM 5942 C CD . GLU B 1 361 ? 48.340 -16.529 63.567 1.00 26.51 ? 361 GLU B CD 1 ATOM 5943 O OE1 . GLU B 1 361 ? 47.742 -17.039 62.596 1.00 32.37 ? 361 GLU B OE1 1 ATOM 5944 O OE2 . GLU B 1 361 ? 49.091 -17.191 64.325 1.00 28.52 ? 361 GLU B OE2 1 ATOM 5945 N N . ALA B 1 362 ? 49.691 -10.997 62.473 1.00 12.79 ? 362 ALA B N 1 ATOM 5946 C CA . ALA B 1 362 ? 49.812 -10.003 61.402 1.00 12.26 ? 362 ALA B CA 1 ATOM 5947 C C . ALA B 1 362 ? 50.886 -8.936 61.579 1.00 11.56 ? 362 ALA B C 1 ATOM 5948 O O . ALA B 1 362 ? 51.123 -8.154 60.669 1.00 11.38 ? 362 ALA B O 1 ATOM 5949 C CB . ALA B 1 362 ? 48.448 -9.356 61.180 1.00 11.86 ? 362 ALA B CB 1 ATOM 5950 N N . GLY B 1 363 ? 51.551 -8.867 62.732 1.00 11.19 ? 363 GLY B N 1 ATOM 5951 C CA . GLY B 1 363 ? 52.570 -7.854 62.900 1.00 11.79 ? 363 GLY B CA 1 ATOM 5952 C C . GLY B 1 363 ? 53.083 -7.691 64.299 1.00 11.67 ? 363 GLY B C 1 ATOM 5953 O O . GLY B 1 363 ? 52.766 -8.507 65.169 1.00 12.71 ? 363 GLY B O 1 ATOM 5954 N N . PRO B 1 364 ? 53.885 -6.639 64.505 1.00 11.45 ? 364 PRO B N 1 ATOM 5955 C CA . PRO B 1 364 ? 54.628 -6.461 65.750 1.00 12.09 ? 364 PRO B CA 1 ATOM 5956 C C . PRO B 1 364 ? 53.933 -5.614 66.817 1.00 12.58 ? 364 PRO B C 1 ATOM 5957 O O . PRO B 1 364 ? 54.502 -5.383 67.892 1.00 13.79 ? 364 PRO B O 1 ATOM 5958 C CB . PRO B 1 364 ? 55.879 -5.723 65.271 1.00 12.94 ? 364 PRO B CB 1 ATOM 5959 C CG . PRO B 1 364 ? 55.304 -4.734 64.251 1.00 12.24 ? 364 PRO B CG 1 ATOM 5960 C CD . PRO B 1 364 ? 54.268 -5.602 63.525 1.00 12.45 ? 364 PRO B CD 1 ATOM 5961 N N . CYS B 1 365 ? 52.736 -5.125 66.522 1.00 11.84 ? 365 CYS B N 1 ATOM 5962 C CA . CYS B 1 365 ? 52.047 -4.217 67.410 1.00 11.89 ? 365 CYS B CA 1 ATOM 5963 C C . CYS B 1 365 ? 51.514 -4.964 68.605 1.00 12.29 ? 365 CYS B C 1 ATOM 5964 O O . CYS B 1 365 ? 50.980 -6.059 68.467 1.00 12.97 ? 365 CYS B O 1 ATOM 5965 C CB . CYS B 1 365 ? 50.932 -3.523 66.650 1.00 11.19 ? 365 CYS B CB 1 ATOM 5966 S SG . CYS B 1 365 ? 51.575 -2.461 65.331 1.00 11.67 ? 365 CYS B SG 1 ATOM 5967 N N . ALA B 1 366 ? 51.669 -4.365 69.783 1.00 12.47 ? 366 ALA B N 1 ATOM 5968 C CA . ALA B 1 366 ? 51.195 -4.984 71.017 1.00 12.39 ? 366 ALA B CA 1 ATOM 5969 C C . ALA B 1 366 ? 49.709 -4.814 71.208 1.00 13.14 ? 366 ALA B C 1 ATOM 5970 O O . ALA B 1 366 ? 49.077 -3.934 70.616 1.00 12.29 ? 366 ALA B O 1 ATOM 5971 C CB . ALA B 1 366 ? 51.913 -4.383 72.198 1.00 12.58 ? 366 ALA B CB 1 ATOM 5972 N N . LYS B 1 367 ? 49.145 -5.662 72.053 1.00 13.57 ? 367 LYS B N 1 ATOM 5973 C CA . LYS B 1 367 ? 47.770 -5.517 72.459 1.00 13.41 ? 367 LYS B CA 1 ATOM 5974 C C . LYS B 1 367 ? 47.549 -4.121 73.025 1.00 13.01 ? 367 LYS B C 1 ATOM 5975 O O . LYS B 1 367 ? 48.309 -3.666 73.890 1.00 14.18 ? 367 LYS B O 1 ATOM 5976 C CB . LYS B 1 367 ? 47.429 -6.555 73.531 1.00 15.37 ? 367 LYS B CB 1 ATOM 5977 C CG . LYS B 1 367 ? 45.958 -6.623 73.876 1.00 16.42 ? 367 LYS B CG 1 ATOM 5978 C CD . LYS B 1 367 ? 45.167 -7.097 72.699 1.00 20.70 ? 367 LYS B CD 1 ATOM 5979 C CE . LYS B 1 367 ? 43.731 -7.353 72.993 1.00 22.72 ? 367 LYS B CE 1 ATOM 5980 N NZ . LYS B 1 367 ? 43.164 -8.025 71.795 1.00 24.65 ? 367 LYS B NZ 1 ATOM 5981 N N . GLY B 1 368 ? 46.521 -3.444 72.502 1.00 12.40 ? 368 GLY B N 1 ATOM 5982 C CA . GLY B 1 368 ? 46.180 -2.091 72.891 1.00 12.45 ? 368 GLY B CA 1 ATOM 5983 C C . GLY B 1 368 ? 46.941 -0.990 72.185 1.00 12.33 ? 368 GLY B C 1 ATOM 5984 O O . GLY B 1 368 ? 46.573 0.184 72.285 1.00 12.97 ? 368 GLY B O 1 ATOM 5985 N N . GLU B 1 369 ? 48.006 -1.331 71.477 1.00 12.53 ? 369 GLU B N 1 ATOM 5986 C CA . GLU B 1 369 ? 48.879 -0.313 70.912 1.00 12.17 ? 369 GLU B CA 1 ATOM 5987 C C . GLU B 1 369 ? 48.170 0.479 69.789 1.00 11.71 ? 369 GLU B C 1 ATOM 5988 O O . GLU B 1 369 ? 48.428 1.677 69.596 1.00 11.96 ? 369 GLU B O 1 ATOM 5989 C CB . GLU B 1 369 ? 50.165 -0.956 70.383 1.00 12.52 ? 369 GLU B CB 1 ATOM 5990 C CG . GLU B 1 369 ? 51.269 0.036 70.143 1.00 13.17 ? 369 GLU B CG 1 ATOM 5991 C CD . GLU B 1 369 ? 52.619 -0.540 69.849 1.00 13.45 ? 369 GLU B CD 1 ATOM 5992 O OE1 . GLU B 1 369 ? 52.839 -1.773 69.985 1.00 14.16 ? 369 GLU B OE1 1 ATOM 5993 O OE2 . GLU B 1 369 ? 53.468 0.284 69.439 1.00 17.73 ? 369 GLU B OE2 1 ATOM 5994 N N . GLY B 1 370 ? 47.284 -0.209 69.066 1.00 11.55 ? 370 GLY B N 1 ATOM 5995 C CA . GLY B 1 370 ? 46.537 0.375 67.964 1.00 11.76 ? 370 GLY B CA 1 ATOM 5996 C C . GLY B 1 370 ? 45.221 1.028 68.305 1.00 11.94 ? 370 GLY B C 1 ATOM 5997 O O . GLY B 1 370 ? 44.465 1.443 67.415 1.00 11.68 ? 370 GLY B O 1 ATOM 5998 N N . ALA B 1 371 ? 44.915 1.131 69.587 1.00 11.78 ? 371 ALA B N 1 ATOM 5999 C CA . ALA B 1 371 ? 43.726 1.870 70.024 1.00 11.55 ? 371 ALA B CA 1 ATOM 6000 C C . ALA B 1 371 ? 43.879 3.333 69.632 1.00 11.92 ? 371 ALA B C 1 ATOM 6001 O O . ALA B 1 371 ? 44.954 3.899 69.853 1.00 11.68 ? 371 ALA B O 1 ATOM 6002 C CB . ALA B 1 371 ? 43.592 1.763 71.517 1.00 12.79 ? 371 ALA B CB 1 ATOM 6003 N N . PRO B 1 372 ? 42.829 3.962 69.102 1.00 10.38 ? 372 PRO B N 1 ATOM 6004 C CA . PRO B 1 372 ? 42.911 5.414 68.827 1.00 10.75 ? 372 PRO B CA 1 ATOM 6005 C C . PRO B 1 372 ? 43.439 6.263 69.985 1.00 10.89 ? 372 PRO B C 1 ATOM 6006 O O . PRO B 1 372 ? 44.211 7.187 69.748 1.00 10.26 ? 372 PRO B O 1 ATOM 6007 C CB . PRO B 1 372 ? 41.470 5.772 68.448 1.00 10.37 ? 372 PRO B CB 1 ATOM 6008 C CG . PRO B 1 372 ? 41.000 4.531 67.740 1.00 10.26 ? 372 PRO B CG 1 ATOM 6009 C CD . PRO B 1 372 ? 41.559 3.383 68.589 1.00 11.26 ? 372 PRO B CD 1 ATOM 6010 N N . SER B 1 373 ? 43.049 5.946 71.215 1.00 11.74 ? 373 SER B N 1 ATOM 6011 C CA . SER B 1 373 ? 43.549 6.690 72.373 1.00 12.00 ? 373 SER B CA 1 ATOM 6012 C C . SER B 1 373 ? 45.055 6.581 72.514 1.00 12.44 ? 373 SER B C 1 ATOM 6013 O O . SER B 1 373 ? 45.681 7.488 73.057 1.00 13.62 ? 373 SER B O 1 ATOM 6014 C CB . SER B 1 373 ? 42.894 6.202 73.666 1.00 12.60 ? 373 SER B CB 1 ATOM 6015 O OG . SER B 1 373 ? 43.171 4.849 73.903 1.00 15.24 ? 373 SER B OG 1 ATOM 6016 N N . ASN B 1 374 ? 45.639 5.475 72.056 1.00 11.77 ? 374 ASN B N 1 ATOM 6017 C CA . ASN B 1 374 ? 47.102 5.325 72.071 1.00 11.31 ? 374 ASN B CA 1 ATOM 6018 C C . ASN B 1 374 ? 47.768 5.929 70.832 1.00 10.93 ? 374 ASN B C 1 ATOM 6019 O O . ASN B 1 374 ? 48.836 6.533 70.927 1.00 11.22 ? 374 ASN B O 1 ATOM 6020 C CB . ASN B 1 374 ? 47.529 3.852 72.272 1.00 11.13 ? 374 ASN B CB 1 ATOM 6021 C CG . ASN B 1 374 ? 48.992 3.745 72.638 1.00 12.50 ? 374 ASN B CG 1 ATOM 6022 O OD1 . ASN B 1 374 ? 49.392 4.237 73.691 1.00 13.69 ? 374 ASN B OD1 1 ATOM 6023 N ND2 . ASN B 1 374 ? 49.806 3.182 71.739 1.00 12.00 ? 374 ASN B ND2 1 ATOM 6024 N N . ILE B 1 375 ? 47.129 5.761 69.672 1.00 10.07 ? 375 ILE B N 1 ATOM 6025 C CA . ILE B 1 375 ? 47.643 6.318 68.418 1.00 10.26 ? 375 ILE B CA 1 ATOM 6026 C C . ILE B 1 375 ? 47.963 7.785 68.593 1.00 10.74 ? 375 ILE B C 1 ATOM 6027 O O . ILE B 1 375 ? 49.047 8.228 68.198 1.00 11.39 ? 375 ILE B O 1 ATOM 6028 C CB . ILE B 1 375 ? 46.635 6.105 67.265 1.00 9.94 ? 375 ILE B CB 1 ATOM 6029 C CG1 . ILE B 1 375 ? 46.587 4.622 66.873 1.00 9.88 ? 375 ILE B CG1 1 ATOM 6030 C CG2 . ILE B 1 375 ? 46.969 6.991 66.073 1.00 11.04 ? 375 ILE B CG2 1 ATOM 6031 C CD1 . ILE B 1 375 ? 45.453 4.252 65.903 1.00 10.06 ? 375 ILE B CD1 1 ATOM 6032 N N . VAL B 1 376 ? 47.051 8.546 69.200 1.00 11.13 ? 376 VAL B N 1 ATOM 6033 C CA . VAL B 1 376 ? 47.285 9.981 69.279 1.00 11.57 ? 376 VAL B CA 1 ATOM 6034 C C . VAL B 1 376 ? 48.442 10.365 70.211 1.00 11.85 ? 376 VAL B C 1 ATOM 6035 O O . VAL B 1 376 ? 49.008 11.441 70.081 1.00 12.46 ? 376 VAL B O 1 ATOM 6036 C CB . VAL B 1 376 ? 46.030 10.789 69.629 1.00 11.75 ? 376 VAL B CB 1 ATOM 6037 C CG1 . VAL B 1 376 ? 44.913 10.590 68.600 1.00 13.26 ? 376 VAL B CG1 1 ATOM 6038 C CG2 . VAL B 1 376 ? 45.517 10.461 70.998 1.00 12.28 ? 376 VAL B CG2 1 ATOM 6039 N N . GLN B 1 377 ? 48.811 9.479 71.131 1.00 11.53 ? 377 GLN B N 1 ATOM 6040 C CA . GLN B 1 377 ? 49.976 9.718 71.963 1.00 11.95 ? 377 GLN B CA 1 ATOM 6041 C C . GLN B 1 377 ? 51.261 9.451 71.202 1.00 12.11 ? 377 GLN B C 1 ATOM 6042 O O . GLN B 1 377 ? 52.277 10.098 71.469 1.00 14.02 ? 377 GLN B O 1 ATOM 6043 C CB . GLN B 1 377 ? 49.909 8.842 73.233 1.00 12.04 ? 377 GLN B CB 1 ATOM 6044 C CG . GLN B 1 377 ? 48.631 9.129 74.084 1.00 12.04 ? 377 GLN B CG 1 ATOM 6045 C CD . GLN B 1 377 ? 48.607 8.483 75.448 1.00 15.00 ? 377 GLN B CD 1 ATOM 6046 O OE1 . GLN B 1 377 ? 49.605 7.996 75.901 1.00 20.30 ? 377 GLN B OE1 1 ATOM 6047 N NE2 . GLN B 1 377 ? 47.482 8.600 76.166 1.00 17.85 ? 377 GLN B NE2 1 ATOM 6048 N N . VAL B 1 378 ? 51.248 8.467 70.302 1.00 11.60 ? 378 VAL B N 1 ATOM 6049 C CA . VAL B 1 378 ? 52.435 8.108 69.511 1.00 11.93 ? 378 VAL B CA 1 ATOM 6050 C C . VAL B 1 378 ? 52.642 9.086 68.357 1.00 11.42 ? 378 VAL B C 1 ATOM 6051 O O . VAL B 1 378 ? 53.739 9.581 68.132 1.00 13.11 ? 378 VAL B O 1 ATOM 6052 C CB . VAL B 1 378 ? 52.289 6.683 68.968 1.00 12.73 ? 378 VAL B CB 1 ATOM 6053 C CG1 . VAL B 1 378 ? 53.417 6.321 68.013 1.00 12.95 ? 378 VAL B CG1 1 ATOM 6054 C CG2 . VAL B 1 378 ? 52.227 5.692 70.140 1.00 12.85 ? 378 VAL B CG2 1 ATOM 6055 N N . GLU B 1 379 ? 51.550 9.399 67.664 1.00 11.93 ? 379 GLU B N 1 ATOM 6056 C CA . GLU B 1 379 ? 51.548 10.309 66.519 1.00 11.60 ? 379 GLU B CA 1 ATOM 6057 C C . GLU B 1 379 ? 50.270 11.143 66.557 1.00 11.03 ? 379 GLU B C 1 ATOM 6058 O O . GLU B 1 379 ? 49.212 10.648 66.165 1.00 10.38 ? 379 GLU B O 1 ATOM 6059 C CB . GLU B 1 379 ? 51.628 9.527 65.201 1.00 11.68 ? 379 GLU B CB 1 ATOM 6060 C CG . GLU B 1 379 ? 51.586 10.416 63.971 1.00 12.23 ? 379 GLU B CG 1 ATOM 6061 C CD . GLU B 1 379 ? 52.494 11.638 64.050 1.00 14.42 ? 379 GLU B CD 1 ATOM 6062 O OE1 . GLU B 1 379 ? 53.704 11.457 63.924 1.00 16.19 ? 379 GLU B OE1 1 ATOM 6063 O OE2 . GLU B 1 379 ? 52.005 12.777 64.298 1.00 14.41 ? 379 GLU B OE2 1 ATOM 6064 N N . PRO B 1 380 ? 50.333 12.376 67.062 1.00 11.24 ? 380 PRO B N 1 ATOM 6065 C CA . PRO B 1 380 ? 49.138 13.214 67.197 1.00 11.91 ? 380 PRO B CA 1 ATOM 6066 C C . PRO B 1 380 ? 48.475 13.569 65.868 1.00 11.63 ? 380 PRO B C 1 ATOM 6067 O O . PRO B 1 380 ? 47.299 13.911 65.850 1.00 12.88 ? 380 PRO B O 1 ATOM 6068 C CB . PRO B 1 380 ? 49.633 14.449 67.932 1.00 12.67 ? 380 PRO B CB 1 ATOM 6069 C CG . PRO B 1 380 ? 51.070 14.317 68.035 1.00 15.29 ? 380 PRO B CG 1 ATOM 6070 C CD . PRO B 1 380 ? 51.532 12.997 67.656 1.00 12.66 ? 380 PRO B CD 1 ATOM 6071 N N . PHE B 1 381 ? 49.210 13.471 64.769 1.00 11.06 ? 381 PHE B N 1 ATOM 6072 C CA . PHE B 1 381 ? 48.676 13.861 63.465 1.00 11.48 ? 381 PHE B CA 1 ATOM 6073 C C . PHE B 1 381 ? 49.047 12.834 62.408 1.00 11.29 ? 381 PHE B C 1 ATOM 6074 O O . PHE B 1 381 ? 49.927 13.080 61.561 1.00 12.02 ? 381 PHE B O 1 ATOM 6075 C CB . PHE B 1 381 ? 49.163 15.280 63.083 1.00 13.76 ? 381 PHE B CB 1 ATOM 6076 C CG . PHE B 1 381 ? 48.637 16.358 64.000 1.00 15.14 ? 381 PHE B CG 1 ATOM 6077 C CD1 . PHE B 1 381 ? 47.302 16.697 63.969 1.00 17.38 ? 381 PHE B CD1 1 ATOM 6078 C CD2 . PHE B 1 381 ? 49.463 16.972 64.924 1.00 16.47 ? 381 PHE B CD2 1 ATOM 6079 C CE1 . PHE B 1 381 ? 46.799 17.664 64.829 1.00 17.41 ? 381 PHE B CE1 1 ATOM 6080 C CE2 . PHE B 1 381 ? 48.949 17.950 65.804 1.00 17.56 ? 381 PHE B CE2 1 ATOM 6081 C CZ . PHE B 1 381 ? 47.645 18.278 65.756 1.00 18.60 ? 381 PHE B CZ 1 ATOM 6082 N N . PRO B 1 382 ? 48.394 11.665 62.453 1.00 10.35 ? 382 PRO B N 1 ATOM 6083 C CA . PRO B 1 382 ? 48.683 10.621 61.456 1.00 10.00 ? 382 PRO B CA 1 ATOM 6084 C C . PRO B 1 382 ? 48.332 11.103 60.060 1.00 9.59 ? 382 PRO B C 1 ATOM 6085 O O . PRO B 1 382 ? 47.327 11.781 59.882 1.00 9.93 ? 382 PRO B O 1 ATOM 6086 C CB . PRO B 1 382 ? 47.776 9.450 61.891 1.00 10.66 ? 382 PRO B CB 1 ATOM 6087 C CG . PRO B 1 382 ? 47.469 9.710 63.346 1.00 10.60 ? 382 PRO B CG 1 ATOM 6088 C CD . PRO B 1 382 ? 47.402 11.196 63.428 1.00 10.40 ? 382 PRO B CD 1 ATOM 6089 N N . GLU B 1 383 ? 49.154 10.737 59.093 1.00 9.57 ? 383 GLU B N 1 ATOM 6090 C CA . GLU B 1 383 ? 48.933 11.134 57.718 1.00 9.96 ? 383 GLU B CA 1 ATOM 6091 C C . GLU B 1 383 ? 49.687 10.205 56.789 1.00 9.85 ? 383 GLU B C 1 ATOM 6092 O O . GLU B 1 383 ? 50.608 9.502 57.225 1.00 9.88 ? 383 GLU B O 1 ATOM 6093 C CB . GLU B 1 383 ? 49.354 12.594 57.506 1.00 10.42 ? 383 GLU B CB 1 ATOM 6094 C CG . GLU B 1 383 ? 50.815 12.873 57.831 1.00 11.42 ? 383 GLU B CG 1 ATOM 6095 C CD . GLU B 1 383 ? 51.223 14.225 57.340 1.00 12.46 ? 383 GLU B CD 1 ATOM 6096 O OE1 . GLU B 1 383 ? 51.402 14.386 56.122 1.00 12.76 ? 383 GLU B OE1 1 ATOM 6097 O OE2 . GLU B 1 383 ? 51.355 15.124 58.180 1.00 13.87 ? 383 GLU B OE2 1 ATOM 6098 N N . VAL B 1 384 ? 49.285 10.207 55.507 1.00 9.25 ? 384 VAL B N 1 ATOM 6099 C CA . VAL B 1 384 ? 49.982 9.485 54.455 1.00 9.03 ? 384 VAL B CA 1 ATOM 6100 C C . VAL B 1 384 ? 50.041 10.349 53.218 1.00 9.77 ? 384 VAL B C 1 ATOM 6101 O O . VAL B 1 384 ? 49.166 11.156 53.000 1.00 9.68 ? 384 VAL B O 1 ATOM 6102 C CB . VAL B 1 384 ? 49.258 8.146 54.112 1.00 9.20 ? 384 VAL B CB 1 ATOM 6103 C CG1 . VAL B 1 384 ? 47.832 8.386 53.556 1.00 9.65 ? 384 VAL B CG1 1 ATOM 6104 C CG2 . VAL B 1 384 ? 50.106 7.265 53.193 1.00 9.74 ? 384 VAL B CG2 1 ATOM 6105 N N . THR B 1 385 ? 51.116 10.198 52.439 1.00 9.58 ? 385 THR B N 1 ATOM 6106 C CA . THR B 1 385 ? 51.207 10.835 51.129 1.00 9.63 ? 385 THR B CA 1 ATOM 6107 C C . THR B 1 385 ? 51.485 9.786 50.075 1.00 9.07 ? 385 THR B C 1 ATOM 6108 O O . THR B 1 385 ? 52.426 9.003 50.209 1.00 10.28 ? 385 THR B O 1 ATOM 6109 C CB . THR B 1 385 ? 52.322 11.899 51.118 1.00 10.24 ? 385 THR B CB 1 ATOM 6110 O OG1 . THR B 1 385 ? 52.013 12.897 52.099 1.00 12.32 ? 385 THR B OG1 1 ATOM 6111 C CG2 . THR B 1 385 ? 52.360 12.661 49.768 1.00 10.77 ? 385 THR B CG2 1 ATOM 6112 N N . TYR B 1 386 ? 50.650 9.776 49.044 1.00 9.47 ? 386 TYR B N 1 ATOM 6113 C CA . TYR B 1 386 ? 50.802 8.914 47.864 1.00 9.35 ? 386 TYR B CA 1 ATOM 6114 C C . TYR B 1 386 ? 51.270 9.811 46.713 1.00 9.40 ? 386 TYR B C 1 ATOM 6115 O O . TYR B 1 386 ? 50.677 10.860 46.450 1.00 11.11 ? 386 TYR B O 1 ATOM 6116 C CB . TYR B 1 386 ? 49.461 8.301 47.482 1.00 9.44 ? 386 TYR B CB 1 ATOM 6117 C CG . TYR B 1 386 ? 48.799 7.429 48.536 1.00 8.78 ? 386 TYR B CG 1 ATOM 6118 C CD1 . TYR B 1 386 ? 49.434 6.311 49.032 1.00 9.69 ? 386 TYR B CD1 1 ATOM 6119 C CD2 . TYR B 1 386 ? 47.504 7.692 48.982 1.00 9.04 ? 386 TYR B CD2 1 ATOM 6120 C CE1 . TYR B 1 386 ? 48.820 5.492 49.955 1.00 9.38 ? 386 TYR B CE1 1 ATOM 6121 C CE2 . TYR B 1 386 ? 46.873 6.876 49.888 1.00 9.50 ? 386 TYR B CE2 1 ATOM 6122 C CZ . TYR B 1 386 ? 47.530 5.776 50.381 1.00 8.34 ? 386 TYR B CZ 1 ATOM 6123 O OH . TYR B 1 386 ? 46.928 4.916 51.301 1.00 9.19 ? 386 TYR B OH 1 ATOM 6124 N N . THR B 1 387 ? 52.282 9.354 45.991 1.00 10.04 ? 387 THR B N 1 ATOM 6125 C CA . THR B 1 387 ? 52.904 10.168 44.958 1.00 10.12 ? 387 THR B CA 1 ATOM 6126 C C . THR B 1 387 ? 53.147 9.350 43.693 1.00 9.89 ? 387 THR B C 1 ATOM 6127 O O . THR B 1 387 ? 53.467 8.170 43.738 1.00 10.76 ? 387 THR B O 1 ATOM 6128 C CB . THR B 1 387 ? 54.238 10.705 45.491 1.00 10.35 ? 387 THR B CB 1 ATOM 6129 O OG1 . THR B 1 387 ? 53.982 11.513 46.648 1.00 11.58 ? 387 THR B OG1 1 ATOM 6130 C CG2 . THR B 1 387 ? 54.896 11.647 44.502 1.00 12.12 ? 387 THR B CG2 1 ATOM 6131 N N . ASN B 1 388 ? 53.009 10.006 42.557 1.00 9.56 ? 388 ASN B N 1 ATOM 6132 C CA . ASN B 1 388 ? 53.264 9.392 41.259 1.00 9.80 ? 388 ASN B CA 1 ATOM 6133 C C . ASN B 1 388 ? 52.472 8.110 41.002 1.00 10.80 ? 388 ASN B C 1 ATOM 6134 O O . ASN B 1 388 ? 53.033 7.086 40.637 1.00 11.03 ? 388 ASN B O 1 ATOM 6135 C CB . ASN B 1 388 ? 54.765 9.170 41.045 1.00 10.46 ? 388 ASN B CB 1 ATOM 6136 C CG . ASN B 1 388 ? 55.559 10.438 41.044 1.00 10.92 ? 388 ASN B CG 1 ATOM 6137 O OD1 . ASN B 1 388 ? 55.120 11.438 40.533 1.00 12.15 ? 388 ASN B OD1 1 ATOM 6138 N ND2 . ASN B 1 388 ? 56.772 10.380 41.605 1.00 14.33 ? 388 ASN B ND2 1 ATOM 6139 N N . LEU B 1 389 ? 51.162 8.196 41.165 1.00 10.48 ? 389 LEU B N 1 ATOM 6140 C CA . LEU B 1 389 ? 50.297 7.069 40.813 1.00 10.84 ? 389 LEU B CA 1 ATOM 6141 C C . LEU B 1 389 ? 50.457 6.785 39.332 1.00 11.07 ? 389 LEU B C 1 ATOM 6142 O O . LEU B 1 389 ? 50.366 7.695 38.511 1.00 10.66 ? 389 LEU B O 1 ATOM 6143 C CB . LEU B 1 389 ? 48.838 7.388 41.059 1.00 11.35 ? 389 LEU B CB 1 ATOM 6144 C CG . LEU B 1 389 ? 48.240 7.182 42.449 1.00 16.80 ? 389 LEU B CG 1 ATOM 6145 C CD1 . LEU B 1 389 ? 49.080 7.471 43.614 1.00 18.22 ? 389 LEU B CD1 1 ATOM 6146 C CD2 . LEU B 1 389 ? 46.853 7.826 42.553 1.00 13.87 ? 389 LEU B CD2 1 ATOM 6147 N N . ARG B 1 390 ? 50.721 5.533 38.994 1.00 11.01 ? 390 ARG B N 1 ATOM 6148 C CA . ARG B 1 390 ? 51.076 5.217 37.612 1.00 11.32 ? 390 ARG B CA 1 ATOM 6149 C C . ARG B 1 390 ? 50.733 3.775 37.285 1.00 11.00 ? 390 ARG B C 1 ATOM 6150 O O . ARG B 1 390 ? 50.946 2.875 38.099 1.00 12.43 ? 390 ARG B O 1 ATOM 6151 C CB . ARG B 1 390 ? 52.549 5.538 37.369 1.00 12.00 ? 390 ARG B CB 1 ATOM 6152 C CG . ARG B 1 390 ? 53.569 4.828 38.267 1.00 12.02 ? 390 ARG B CG 1 ATOM 6153 C CD . ARG B 1 390 ? 54.886 5.549 38.249 1.00 12.75 ? 390 ARG B CD 1 ATOM 6154 N NE . ARG B 1 390 ? 55.991 4.950 38.974 1.00 13.16 ? 390 ARG B NE 1 ATOM 6155 C CZ . ARG B 1 390 ? 56.297 5.156 40.252 1.00 13.48 ? 390 ARG B CZ 1 ATOM 6156 N NH1 . ARG B 1 390 ? 55.504 5.840 41.061 1.00 13.52 ? 390 ARG B NH1 1 ATOM 6157 N NH2 . ARG B 1 390 ? 57.391 4.627 40.749 1.00 15.22 ? 390 ARG B NH2 1 ATOM 6158 N N . TRP B 1 391 ? 50.128 3.550 36.128 1.00 10.24 ? 391 TRP B N 1 ATOM 6159 C CA . TRP B 1 391 ? 49.754 2.190 35.777 1.00 10.29 ? 391 TRP B CA 1 ATOM 6160 C C . TRP B 1 391 ? 49.919 1.962 34.298 1.00 10.28 ? 391 TRP B C 1 ATOM 6161 O O . TRP B 1 391 ? 49.890 2.899 33.507 1.00 10.63 ? 391 TRP B O 1 ATOM 6162 C CB . TRP B 1 391 ? 48.323 1.861 36.242 1.00 10.49 ? 391 TRP B CB 1 ATOM 6163 C CG . TRP B 1 391 ? 47.202 2.734 35.778 1.00 9.60 ? 391 TRP B CG 1 ATOM 6164 C CD1 . TRP B 1 391 ? 46.320 2.450 34.793 1.00 10.98 ? 391 TRP B CD1 1 ATOM 6165 C CD2 . TRP B 1 391 ? 46.736 3.951 36.385 1.00 10.21 ? 391 TRP B CD2 1 ATOM 6166 N NE1 . TRP B 1 391 ? 45.379 3.441 34.697 1.00 11.81 ? 391 TRP B NE1 1 ATOM 6167 C CE2 . TRP B 1 391 ? 45.608 4.376 35.667 1.00 10.14 ? 391 TRP B CE2 1 ATOM 6168 C CE3 . TRP B 1 391 ? 47.189 4.741 37.441 1.00 11.23 ? 391 TRP B CE3 1 ATOM 6169 C CZ2 . TRP B 1 391 ? 44.885 5.524 36.004 1.00 10.80 ? 391 TRP B CZ2 1 ATOM 6170 C CZ3 . TRP B 1 391 ? 46.479 5.897 37.776 1.00 11.11 ? 391 TRP B CZ3 1 ATOM 6171 C CH2 . TRP B 1 391 ? 45.364 6.280 37.048 1.00 11.02 ? 391 TRP B CH2 1 ATOM 6172 N N . GLY B 1 392 ? 50.090 0.695 33.929 1.00 10.26 ? 392 GLY B N 1 ATOM 6173 C CA . GLY B 1 392 ? 50.255 0.344 32.540 1.00 10.62 ? 392 GLY B CA 1 ATOM 6174 C C . GLY B 1 392 ? 50.906 -0.994 32.342 1.00 11.53 ? 392 GLY B C 1 ATOM 6175 O O . GLY B 1 392 ? 50.751 -1.906 33.136 1.00 11.97 ? 392 GLY B O 1 ATOM 6176 N N . GLU B 1 393 ? 51.693 -1.087 31.284 1.00 12.34 ? 393 GLU B N 1 ATOM 6177 C CA . GLU B 1 393 ? 52.286 -2.355 30.896 1.00 13.39 ? 393 GLU B CA 1 ATOM 6178 C C . GLU B 1 393 ? 53.211 -2.951 31.951 1.00 13.91 ? 393 GLU B C 1 ATOM 6179 O O . GLU B 1 393 ? 53.966 -2.236 32.629 1.00 13.62 ? 393 GLU B O 1 ATOM 6180 C CB . GLU B 1 393 ? 53.046 -2.175 29.571 1.00 14.13 ? 393 GLU B CB 1 ATOM 6181 C CG . GLU B 1 393 ? 52.099 -1.907 28.416 1.00 16.63 ? 393 GLU B CG 1 ATOM 6182 C CD . GLU B 1 393 ? 52.795 -1.690 27.090 1.00 17.16 ? 393 GLU B CD 1 ATOM 6183 O OE1 . GLU B 1 393 ? 54.046 -1.810 27.040 1.00 17.66 ? 393 GLU B OE1 1 ATOM 6184 O OE2 . GLU B 1 393 ? 52.046 -1.398 26.125 1.00 22.54 ? 393 GLU B OE2 1 ATOM 6185 N N . ILE B 1 394 ? 53.154 -4.274 32.063 1.00 14.15 ? 394 ILE B N 1 ATOM 6186 C CA . ILE B 1 394 ? 54.034 -4.993 32.960 1.00 14.72 ? 394 ILE B CA 1 ATOM 6187 C C . ILE B 1 394 ? 55.478 -4.603 32.699 1.00 14.58 ? 394 ILE B C 1 ATOM 6188 O O . ILE B 1 394 ? 55.945 -4.601 31.536 1.00 15.83 ? 394 ILE B O 1 ATOM 6189 C CB . ILE B 1 394 ? 53.858 -6.517 32.789 1.00 15.65 ? 394 ILE B CB 1 ATOM 6190 C CG1 . ILE B 1 394 ? 52.454 -6.954 33.194 1.00 18.31 ? 394 ILE B CG1 1 ATOM 6191 C CG2 . ILE B 1 394 ? 54.897 -7.280 33.585 1.00 16.21 ? 394 ILE B CG2 1 ATOM 6192 C CD1 . ILE B 1 394 ? 52.103 -6.635 34.575 1.00 19.06 ? 394 ILE B CD1 1 ATOM 6193 N N . GLY B 1 395 ? 56.179 -4.270 33.782 1.00 14.55 ? 395 GLY B N 1 ATOM 6194 C CA . GLY B 1 395 ? 57.567 -3.851 33.728 1.00 15.02 ? 395 GLY B CA 1 ATOM 6195 C C . GLY B 1 395 ? 57.836 -2.416 33.362 1.00 15.77 ? 395 GLY B C 1 ATOM 6196 O O . GLY B 1 395 ? 58.989 -2.018 33.350 1.00 18.55 ? 395 GLY B O 1 ATOM 6197 N N . SER B 1 396 ? 56.806 -1.629 33.074 1.00 14.19 ? 396 SER B N 1 ATOM 6198 C CA . SER B 1 396 ? 56.990 -0.263 32.585 1.00 14.09 ? 396 SER B CA 1 ATOM 6199 C C . SER B 1 396 ? 56.876 0.837 33.624 1.00 13.99 ? 396 SER B C 1 ATOM 6200 O O . SER B 1 396 ? 57.222 1.985 33.332 1.00 14.51 ? 396 SER B O 1 ATOM 6201 C CB . SER B 1 396 ? 56.014 0.064 31.460 1.00 14.45 ? 396 SER B CB 1 ATOM 6202 O OG . SER B 1 396 ? 54.696 0.281 31.920 1.00 14.18 ? 396 SER B OG 1 ATOM 6203 N N . THR B 1 397 ? 56.397 0.538 34.839 1.00 14.05 ? 397 THR B N 1 ATOM 6204 C CA . THR B 1 397 ? 56.114 1.612 35.805 1.00 15.10 ? 397 THR B CA 1 ATOM 6205 C C . THR B 1 397 ? 57.235 1.938 36.760 1.00 16.74 ? 397 THR B C 1 ATOM 6206 O O . THR B 1 397 ? 57.120 2.919 37.492 1.00 18.00 ? 397 THR B O 1 ATOM 6207 C CB . THR B 1 397 ? 54.848 1.316 36.640 1.00 13.89 ? 397 THR B CB 1 ATOM 6208 O OG1 . THR B 1 397 ? 55.052 0.124 37.430 1.00 14.06 ? 397 THR B OG1 1 ATOM 6209 C CG2 . THR B 1 397 ? 53.650 1.064 35.766 1.00 14.73 ? 397 THR B CG2 1 ATOM 6210 N N . TYR B 1 398 ? 58.282 1.124 36.803 1.00 17.45 ? 398 TYR B N 1 ATOM 6211 C CA . TYR B 1 398 ? 59.302 1.266 37.842 1.00 19.29 ? 398 TYR B CA 1 ATOM 6212 C C . TYR B 1 398 ? 60.703 1.233 37.274 1.00 22.11 ? 398 TYR B C 1 ATOM 6213 O O . TYR B 1 398 ? 60.884 1.170 36.049 1.00 24.44 ? 398 TYR B O 1 ATOM 6214 C CB . TYR B 1 398 ? 59.150 0.168 38.911 1.00 19.92 ? 398 TYR B CB 1 ATOM 6215 C CG . TYR B 1 398 ? 59.274 -1.215 38.366 1.00 19.22 ? 398 TYR B CG 1 ATOM 6216 C CD1 . TYR B 1 398 ? 58.172 -1.859 37.829 1.00 17.50 ? 398 TYR B CD1 1 ATOM 6217 C CD2 . TYR B 1 398 ? 60.498 -1.871 38.340 1.00 18.99 ? 398 TYR B CD2 1 ATOM 6218 C CE1 . TYR B 1 398 ? 58.272 -3.127 37.307 1.00 18.64 ? 398 TYR B CE1 1 ATOM 6219 C CE2 . TYR B 1 398 ? 60.618 -3.128 37.805 1.00 19.10 ? 398 TYR B CE2 1 ATOM 6220 C CZ . TYR B 1 398 ? 59.503 -3.764 37.277 1.00 19.43 ? 398 TYR B CZ 1 ATOM 6221 O OH . TYR B 1 398 ? 59.561 -5.034 36.735 1.00 21.86 ? 398 TYR B OH 1 ATOM 6222 N N . GLN B 1 399 ? 61.652 1.210 38.070 1.00 24.55 ? 399 GLN B N 1 HETATM 6223 C C2 . BGC C 2 . ? 16.110 -14.397 17.714 1.00 37.54 ? 1400 BGC A C2 1 HETATM 6224 C C3 . BGC C 2 . ? 15.398 -13.280 16.953 1.00 36.32 ? 1400 BGC A C3 1 HETATM 6225 C C4 . BGC C 2 . ? 16.324 -12.547 15.991 1.00 34.05 ? 1400 BGC A C4 1 HETATM 6226 C C5 . BGC C 2 . ? 17.274 -13.479 15.237 1.00 34.27 ? 1400 BGC A C5 1 HETATM 6227 C C6 . BGC C 2 . ? 18.417 -12.681 14.616 1.00 33.28 ? 1400 BGC A C6 1 HETATM 6228 C C1 . BGC C 2 . ? 16.918 -15.257 16.759 1.00 37.67 ? 1400 BGC A C1 1 HETATM 6229 O O1 . BGC C 2 . ? 17.609 -16.271 17.456 1.00 38.92 ? 1400 BGC A O1 1 HETATM 6230 O O2 . BGC C 2 . ? 15.145 -15.216 18.336 1.00 40.00 ? 1400 BGC A O2 1 HETATM 6231 O O3 . BGC C 2 . ? 14.848 -12.341 17.849 1.00 36.91 ? 1400 BGC A O3 1 HETATM 6232 O O4 . BGC C 2 . ? 15.545 -11.832 15.042 1.00 31.57 ? 1400 BGC A O4 1 HETATM 6233 O O5 . BGC C 2 . ? 17.854 -14.437 16.107 1.00 36.65 ? 1400 BGC A O5 1 HETATM 6234 O O6 . BGC C 2 . ? 19.186 -13.509 13.747 1.00 30.37 ? 1400 BGC A O6 1 HETATM 6235 C C1 . GAL D 3 . ? 15.455 -10.420 15.319 1.00 29.31 ? 1403 GAL A C1 1 HETATM 6236 C C2 . GAL D 3 . ? 15.174 -9.702 14.011 1.00 28.87 ? 1403 GAL A C2 1 HETATM 6237 C C3 . GAL D 3 . ? 15.098 -8.218 14.214 1.00 27.97 ? 1403 GAL A C3 1 HETATM 6238 C C4 . GAL D 3 . ? 14.116 -7.870 15.338 1.00 28.77 ? 1403 GAL A C4 1 HETATM 6239 C C5 . GAL D 3 . ? 14.359 -8.738 16.568 1.00 29.54 ? 1403 GAL A C5 1 HETATM 6240 C C6 . GAL D 3 . ? 13.277 -8.528 17.617 1.00 30.73 ? 1403 GAL A C6 1 HETATM 6241 O O2 . GAL D 3 . ? 16.222 -9.904 13.101 1.00 26.56 ? 1403 GAL A O2 1 HETATM 6242 O O3 . GAL D 3 . ? 14.724 -7.673 12.955 1.00 27.93 ? 1403 GAL A O3 1 HETATM 6243 O O4 . GAL D 3 . ? 12.800 -8.064 14.884 1.00 29.67 ? 1403 GAL A O4 1 HETATM 6244 O O5 . GAL D 3 . ? 14.414 -10.111 16.232 1.00 29.57 ? 1403 GAL A O5 1 HETATM 6245 O O6 . GAL D 3 . ? 13.725 -9.026 18.862 1.00 32.88 ? 1403 GAL A O6 1 HETATM 6246 C C1 . GLC E 4 . ? 14.134 -4.842 9.954 1.00 12.21 ? 1401 GLC A C1 1 HETATM 6247 C C2 . GLC E 4 . ? 12.882 -4.756 10.821 1.00 10.45 ? 1401 GLC A C2 1 HETATM 6248 C C3 . GLC E 4 . ? 12.435 -3.307 10.943 1.00 10.05 ? 1401 GLC A C3 1 HETATM 6249 C C4 . GLC E 4 . ? 13.573 -2.417 11.451 1.00 8.34 ? 1401 GLC A C4 1 HETATM 6250 C C5 . GLC E 4 . ? 14.742 -2.568 10.499 1.00 9.01 ? 1401 GLC A C5 1 HETATM 6251 C C6 . GLC E 4 . ? 15.959 -1.711 10.848 1.00 9.18 ? 1401 GLC A C6 1 HETATM 6252 O O1 . GLC E 4 . ? 13.825 -4.649 8.568 1.00 14.11 ? 1401 GLC A O1 1 HETATM 6253 O O2 . GLC E 4 . ? 11.965 -5.620 10.166 1.00 12.34 ? 1401 GLC A O2 1 HETATM 6254 O O3 . GLC E 4 . ? 11.303 -3.282 11.790 1.00 8.82 ? 1401 GLC A O3 1 HETATM 6255 O O4 . GLC E 4 . ? 13.077 -1.084 11.374 1.00 8.98 ? 1401 GLC A O4 1 HETATM 6256 O O5 . GLC E 4 . ? 15.135 -3.948 10.409 1.00 9.44 ? 1401 GLC A O5 1 HETATM 6257 O O6 . GLC E 4 . ? 16.458 -2.015 12.140 1.00 10.08 ? 1401 GLC A O6 1 HETATM 6258 C C1 . GAL F 3 . ? 13.289 -0.274 12.526 1.00 8.11 ? 1402 GAL A C1 1 HETATM 6259 C C2 . GAL F 3 . ? 13.200 1.182 12.152 1.00 8.80 ? 1402 GAL A C2 1 HETATM 6260 C C3 . GAL F 3 . ? 13.279 2.067 13.374 1.00 9.39 ? 1402 GAL A C3 1 HETATM 6261 C C4 . GAL F 3 . ? 12.273 1.615 14.413 1.00 9.43 ? 1402 GAL A C4 1 HETATM 6262 C C5 . GAL F 3 . ? 12.437 0.128 14.675 1.00 8.52 ? 1402 GAL A C5 1 HETATM 6263 C C6 . GAL F 3 . ? 11.465 -0.393 15.712 1.00 10.46 ? 1402 GAL A C6 1 HETATM 6264 O O2 . GAL F 3 . ? 14.270 1.503 11.263 1.00 9.13 ? 1402 GAL A O2 1 HETATM 6265 O O3 . GAL F 3 . ? 13.025 3.405 12.939 1.00 9.30 ? 1402 GAL A O3 1 HETATM 6266 O O4 . GAL F 3 . ? 10.930 1.871 14.031 1.00 9.88 ? 1402 GAL A O4 1 HETATM 6267 O O5 . GAL F 3 . ? 12.265 -0.587 13.457 1.00 9.25 ? 1402 GAL A O5 1 HETATM 6268 O O6 . GAL F 3 . ? 11.750 -1.730 16.141 1.00 13.67 ? 1402 GAL A O6 1 HETATM 6269 C C1 . NAG G 5 . ? 34.783 -22.111 17.660 1.00 18.84 ? 1404 NAG A C1 1 HETATM 6270 C C2 . NAG G 5 . ? 34.791 -23.633 17.528 1.00 20.49 ? 1404 NAG A C2 1 HETATM 6271 C C3 . NAG G 5 . ? 36.044 -24.170 18.240 1.00 22.49 ? 1404 NAG A C3 1 HETATM 6272 C C4 . NAG G 5 . ? 37.285 -23.494 17.686 1.00 24.10 ? 1404 NAG A C4 1 HETATM 6273 C C5 . NAG G 5 . ? 37.146 -21.988 17.790 1.00 23.33 ? 1404 NAG A C5 1 HETATM 6274 C C6 . NAG G 5 . ? 38.298 -21.227 17.155 1.00 24.40 ? 1404 NAG A C6 1 HETATM 6275 C C7 . NAG G 5 . ? 32.586 -24.756 17.439 1.00 21.76 ? 1404 NAG A C7 1 HETATM 6276 C C8 . NAG G 5 . ? 31.369 -25.170 18.207 1.00 22.55 ? 1404 NAG A C8 1 HETATM 6277 N N2 . NAG G 5 . ? 33.571 -24.160 18.109 1.00 19.78 ? 1404 NAG A N2 1 HETATM 6278 O O3 . NAG G 5 . ? 36.144 -25.567 18.099 1.00 26.26 ? 1404 NAG A O3 1 HETATM 6279 O O4 . NAG G 5 . ? 38.403 -23.899 18.455 1.00 27.32 ? 1404 NAG A O4 1 HETATM 6280 O O5 . NAG G 5 . ? 35.971 -21.598 17.105 1.00 20.67 ? 1404 NAG A O5 1 HETATM 6281 O O6 . NAG G 5 . ? 38.426 -21.523 15.780 1.00 25.71 ? 1404 NAG A O6 1 HETATM 6282 O O7 . NAG G 5 . ? 32.620 -24.975 16.233 1.00 21.25 ? 1404 NAG A O7 1 HETATM 6283 C C1 . NAG H 5 . ? 58.568 -19.756 61.090 1.00 15.76 ? 1399 NAG B C1 1 HETATM 6284 C C2 . NAG H 5 . ? 58.316 -21.269 61.142 1.00 15.19 ? 1399 NAG B C2 1 HETATM 6285 C C3 . NAG H 5 . ? 59.368 -21.956 62.033 1.00 16.82 ? 1399 NAG B C3 1 HETATM 6286 C C4 . NAG H 5 . ? 60.768 -21.508 61.655 1.00 18.15 ? 1399 NAG B C4 1 HETATM 6287 C C5 . NAG H 5 . ? 60.823 -19.989 61.711 1.00 20.26 ? 1399 NAG B C5 1 HETATM 6288 C C6 . NAG H 5 . ? 62.202 -19.401 61.434 1.00 23.86 ? 1399 NAG B C6 1 HETATM 6289 C C7 . NAG H 5 . ? 56.049 -22.241 61.052 1.00 14.41 ? 1399 NAG B C7 1 HETATM 6290 C C8 . NAG H 5 . ? 54.720 -22.369 61.741 1.00 14.71 ? 1399 NAG B C8 1 HETATM 6291 N N2 . NAG H 5 . ? 56.978 -21.519 61.670 1.00 14.40 ? 1399 NAG B N2 1 HETATM 6292 O O3 . NAG H 5 . ? 59.248 -23.356 61.919 1.00 17.36 ? 1399 NAG B O3 1 HETATM 6293 O O4 . NAG H 5 . ? 61.749 -22.048 62.546 1.00 21.78 ? 1399 NAG B O4 1 HETATM 6294 O O5 . NAG H 5 . ? 59.911 -19.500 60.736 1.00 16.93 ? 1399 NAG B O5 1 HETATM 6295 O O6 . NAG H 5 . ? 62.206 -18.087 61.941 1.00 27.68 ? 1399 NAG B O6 1 HETATM 6296 O O7 . NAG H 5 . ? 56.289 -22.804 59.963 1.00 15.69 ? 1399 NAG B O7 1 HETATM 6297 C C2 . BGC I 2 . ? 40.514 -12.369 60.298 1.00 33.94 ? 1401 BGC B C2 1 HETATM 6298 C C3 . BGC I 2 . ? 39.767 -11.312 59.507 1.00 32.44 ? 1401 BGC B C3 1 HETATM 6299 C C4 . BGC I 2 . ? 40.664 -10.610 58.490 1.00 30.19 ? 1401 BGC B C4 1 HETATM 6300 C C5 . BGC I 2 . ? 41.589 -11.559 57.727 1.00 31.63 ? 1401 BGC B C5 1 HETATM 6301 C C6 . BGC I 2 . ? 42.727 -10.782 57.071 1.00 32.45 ? 1401 BGC B C6 1 HETATM 6302 C C1 . BGC I 2 . ? 41.292 -13.264 59.360 1.00 34.65 ? 1401 BGC B C1 1 HETATM 6303 O O1 . BGC I 2 . ? 42.023 -14.182 60.139 1.00 36.49 ? 1401 BGC B O1 1 HETATM 6304 O O2 . BGC I 2 . ? 39.585 -13.140 61.038 1.00 36.13 ? 1401 BGC B O2 1 HETATM 6305 O O3 . BGC I 2 . ? 39.232 -10.382 60.421 1.00 33.24 ? 1401 BGC B O3 1 HETATM 6306 O O4 . BGC I 2 . ? 39.832 -9.979 57.537 1.00 25.60 ? 1401 BGC B O4 1 HETATM 6307 O O5 . BGC I 2 . ? 42.193 -12.488 58.597 1.00 33.31 ? 1401 BGC B O5 1 HETATM 6308 O O6 . BGC I 2 . ? 43.359 -11.570 56.077 1.00 32.03 ? 1401 BGC B O6 1 HETATM 6309 C C1 . GAL J 3 . ? 39.731 -8.566 57.737 1.00 23.85 ? 1404 GAL B C1 1 HETATM 6310 C C2 . GAL J 3 . ? 39.396 -7.918 56.413 1.00 23.78 ? 1404 GAL B C2 1 HETATM 6311 C C3 . GAL J 3 . ? 39.312 -6.428 56.552 1.00 23.10 ? 1404 GAL B C3 1 HETATM 6312 C C4 . GAL J 3 . ? 38.314 -6.051 57.660 1.00 23.63 ? 1404 GAL B C4 1 HETATM 6313 C C5 . GAL J 3 . ? 38.642 -6.839 58.917 1.00 25.05 ? 1404 GAL B C5 1 HETATM 6314 C C6 . GAL J 3 . ? 37.643 -6.575 60.038 1.00 26.91 ? 1404 GAL B C6 1 HETATM 6315 O O2 . GAL J 3 . ? 40.430 -8.146 55.499 1.00 20.40 ? 1404 GAL B O2 1 HETATM 6316 O O3 . GAL J 3 . ? 38.901 -5.928 55.296 1.00 23.61 ? 1404 GAL B O3 1 HETATM 6317 O O4 . GAL J 3 . ? 36.994 -6.297 57.218 1.00 25.15 ? 1404 GAL B O4 1 HETATM 6318 O O5 . GAL J 3 . ? 38.734 -8.232 58.665 1.00 24.87 ? 1404 GAL B O5 1 HETATM 6319 O O6 . GAL J 3 . ? 37.867 -7.553 61.033 1.00 29.10 ? 1404 GAL B O6 1 HETATM 6320 C C1 . GLC K 4 . ? 38.347 -3.253 52.068 1.00 14.25 ? 1402 GLC B C1 1 HETATM 6321 C C2 . GLC K 4 . ? 37.080 -3.181 52.925 1.00 12.09 ? 1402 GLC B C2 1 HETATM 6322 C C3 . GLC K 4 . ? 36.579 -1.754 52.988 1.00 10.00 ? 1402 GLC B C3 1 HETATM 6323 C C4 . GLC K 4 . ? 37.651 -0.774 53.451 1.00 9.61 ? 1402 GLC B C4 1 HETATM 6324 C C5 . GLC K 4 . ? 38.836 -0.945 52.529 1.00 10.15 ? 1402 GLC B C5 1 HETATM 6325 C C6 . GLC K 4 . ? 40.013 -0.035 52.859 1.00 9.60 ? 1402 GLC B C6 1 HETATM 6326 O O1 . GLC K 4 . ? 38.042 -3.091 50.692 1.00 15.48 ? 1402 GLC B O1 1 HETATM 6327 O O2 . GLC K 4 . ? 36.168 -4.060 52.290 1.00 12.64 ? 1402 GLC B O2 1 HETATM 6328 O O3 . GLC K 4 . ? 35.448 -1.688 53.854 1.00 9.71 ? 1402 GLC B O3 1 HETATM 6329 O O4 . GLC K 4 . ? 37.120 0.539 53.304 1.00 9.69 ? 1402 GLC B O4 1 HETATM 6330 O O5 . GLC K 4 . ? 39.305 -2.282 52.475 1.00 9.68 ? 1402 GLC B O5 1 HETATM 6331 O O6 . GLC K 4 . ? 40.524 -0.282 54.157 1.00 10.87 ? 1402 GLC B O6 1 HETATM 6332 C C1 . GAL L 3 . ? 37.316 1.395 54.433 1.00 9.19 ? 1403 GAL B C1 1 HETATM 6333 C C2 . GAL L 3 . ? 37.173 2.839 53.973 1.00 8.67 ? 1403 GAL B C2 1 HETATM 6334 C C3 . GAL L 3 . ? 37.223 3.790 55.152 1.00 8.95 ? 1403 GAL B C3 1 HETATM 6335 C C4 . GAL L 3 . ? 36.244 3.331 56.231 1.00 9.53 ? 1403 GAL B C4 1 HETATM 6336 C C5 . GAL L 3 . ? 36.459 1.857 56.547 1.00 10.12 ? 1403 GAL B C5 1 HETATM 6337 C C6 . GAL L 3 . ? 35.448 1.340 57.578 1.00 11.81 ? 1403 GAL B C6 1 HETATM 6338 O O2 . GAL L 3 . ? 38.200 3.156 53.054 1.00 9.30 ? 1403 GAL B O2 1 HETATM 6339 O O3 . GAL L 3 . ? 36.932 5.112 54.709 1.00 10.09 ? 1403 GAL B O3 1 HETATM 6340 O O4 . GAL L 3 . ? 34.896 3.520 55.843 1.00 10.68 ? 1403 GAL B O4 1 HETATM 6341 O O5 . GAL L 3 . ? 36.304 1.098 55.357 1.00 9.26 ? 1403 GAL B O5 1 HETATM 6342 O O6 . GAL L 3 . ? 35.793 0.062 58.069 1.00 13.84 ? 1403 GAL B O6 1 HETATM 6343 O O . HOH M 6 . ? -0.785 13.252 2.390 1.00 11.84 ? 2001 HOH A O 1 HETATM 6344 O O . HOH M 6 . ? 1.443 8.663 6.816 1.00 12.17 ? 2002 HOH A O 1 HETATM 6345 O O . HOH M 6 . ? -9.743 19.467 3.580 1.00 16.73 ? 2003 HOH A O 1 HETATM 6346 O O . HOH M 6 . ? -2.687 20.865 1.983 1.00 18.83 ? 2004 HOH A O 1 HETATM 6347 O O . HOH M 6 . ? -3.068 22.499 5.311 1.00 14.02 ? 2005 HOH A O 1 HETATM 6348 O O . HOH M 6 . ? 11.392 26.297 1.411 1.00 27.57 ? 2006 HOH A O 1 HETATM 6349 O O . HOH M 6 . ? 0.215 22.687 1.743 1.00 27.30 ? 2007 HOH A O 1 HETATM 6350 O O . HOH M 6 . ? 5.188 28.284 4.919 1.00 19.79 ? 2008 HOH A O 1 HETATM 6351 O O . HOH M 6 . ? -0.425 29.639 1.685 1.00 13.49 ? 2009 HOH A O 1 HETATM 6352 O O . HOH M 6 . ? -2.590 24.450 3.468 1.00 17.29 ? 2010 HOH A O 1 HETATM 6353 O O . HOH M 6 . ? 1.171 30.046 5.390 1.00 22.64 ? 2011 HOH A O 1 HETATM 6354 O O . HOH M 6 . ? 3.727 21.296 4.146 1.00 18.68 ? 2012 HOH A O 1 HETATM 6355 O O . HOH M 6 . ? 3.108 27.051 8.889 1.00 18.39 ? 2013 HOH A O 1 HETATM 6356 O O . HOH M 6 . ? 7.421 27.295 6.194 1.00 17.93 ? 2014 HOH A O 1 HETATM 6357 O O . HOH M 6 . ? 5.809 23.609 -0.832 1.00 22.43 ? 2015 HOH A O 1 HETATM 6358 O O . HOH M 6 . ? 24.547 -0.971 -13.032 1.00 22.28 ? 2016 HOH A O 1 HETATM 6359 O O . HOH M 6 . ? 27.139 5.316 -14.465 1.00 23.73 ? 2017 HOH A O 1 HETATM 6360 O O . HOH M 6 . ? 10.491 23.827 0.456 0.50 14.56 ? 2018 HOH A O 1 HETATM 6361 O O . HOH M 6 . ? 16.133 20.945 6.498 1.00 13.02 ? 2019 HOH A O 1 HETATM 6362 O O . HOH M 6 . ? 25.752 7.589 -13.973 0.50 12.37 ? 2020 HOH A O 1 HETATM 6363 O O . HOH M 6 . ? 26.228 10.083 -15.102 0.50 22.51 ? 2021 HOH A O 1 HETATM 6364 O O . HOH M 6 . ? 15.983 20.836 -0.576 1.00 15.69 ? 2022 HOH A O 1 HETATM 6365 O O . HOH M 6 . ? 12.530 20.147 -0.170 1.00 12.18 ? 2023 HOH A O 1 HETATM 6366 O O . HOH M 6 . ? 5.401 5.886 13.439 1.00 18.48 ? 2024 HOH A O 1 HETATM 6367 O O . HOH M 6 . ? 26.180 9.365 -0.190 1.00 10.83 ? 2025 HOH A O 1 HETATM 6368 O O . HOH M 6 . ? 28.074 16.704 -3.239 1.00 18.31 ? 2026 HOH A O 1 HETATM 6369 O O . HOH M 6 . ? -10.421 29.264 11.755 1.00 21.53 ? 2027 HOH A O 1 HETATM 6370 O O . HOH M 6 . ? 25.494 1.538 -12.428 1.00 18.27 ? 2028 HOH A O 1 HETATM 6371 O O . HOH M 6 . ? 29.815 4.651 -14.383 1.00 17.44 ? 2029 HOH A O 1 HETATM 6372 O O . HOH M 6 . ? 5.565 0.118 10.255 1.00 9.81 ? 2030 HOH A O 1 HETATM 6373 O O . HOH M 6 . ? 1.285 -3.454 20.085 1.00 34.71 ? 2031 HOH A O 1 HETATM 6374 O O . HOH M 6 . ? 34.041 7.859 -12.144 1.00 17.21 ? 2032 HOH A O 1 HETATM 6375 O O . HOH M 6 . ? 31.503 4.764 -19.491 1.00 30.77 ? 2033 HOH A O 1 HETATM 6376 O O . HOH M 6 . ? 33.154 10.639 -12.072 1.00 23.12 ? 2034 HOH A O 1 HETATM 6377 O O . HOH M 6 . ? 35.219 5.181 -9.256 1.00 23.77 ? 2035 HOH A O 1 HETATM 6378 O O . HOH M 6 . ? -6.079 16.437 1.466 1.00 20.61 ? 2036 HOH A O 1 HETATM 6379 O O . HOH M 6 . ? 25.216 8.921 -11.681 1.00 19.38 ? 2037 HOH A O 1 HETATM 6380 O O . HOH M 6 . ? 27.190 11.914 -13.010 1.00 21.64 ? 2038 HOH A O 1 HETATM 6381 O O . HOH M 6 . ? 21.606 13.708 -10.548 1.00 24.69 ? 2039 HOH A O 1 HETATM 6382 O O . HOH M 6 . ? 19.720 11.356 -9.236 1.00 19.08 ? 2040 HOH A O 1 HETATM 6383 O O . HOH M 6 . ? 7.496 7.568 12.374 1.00 11.03 ? 2041 HOH A O 1 HETATM 6384 O O . HOH M 6 . ? 5.121 5.205 9.318 1.00 10.54 ? 2042 HOH A O 1 HETATM 6385 O O . HOH M 6 . ? 2.892 10.845 14.754 1.00 24.95 ? 2043 HOH A O 1 HETATM 6386 O O . HOH M 6 . ? 9.941 12.811 14.999 1.00 14.06 ? 2044 HOH A O 1 HETATM 6387 O O . HOH M 6 . ? 11.884 9.262 12.543 1.00 10.89 ? 2045 HOH A O 1 HETATM 6388 O O . HOH M 6 . ? 5.488 13.419 14.960 1.00 23.47 ? 2046 HOH A O 1 HETATM 6389 O O . HOH M 6 . ? 3.405 14.972 16.108 1.00 22.79 ? 2047 HOH A O 1 HETATM 6390 O O . HOH M 6 . ? 0.266 17.413 17.913 1.00 27.63 ? 2048 HOH A O 1 HETATM 6391 O O . HOH M 6 . ? 2.273 20.707 15.323 1.00 27.85 ? 2049 HOH A O 1 HETATM 6392 O O . HOH M 6 . ? -3.726 22.671 15.563 1.00 31.36 ? 2050 HOH A O 1 HETATM 6393 O O . HOH M 6 . ? -4.679 23.211 12.207 1.00 19.76 ? 2051 HOH A O 1 HETATM 6394 O O . HOH M 6 . ? -10.956 27.419 9.626 1.00 11.48 ? 2052 HOH A O 1 HETATM 6395 O O . HOH M 6 . ? -7.555 23.210 9.040 1.00 20.17 ? 2053 HOH A O 1 HETATM 6396 O O . HOH M 6 . ? -7.390 26.471 15.369 1.00 21.56 ? 2054 HOH A O 1 HETATM 6397 O O . HOH M 6 . ? -10.656 17.021 18.229 1.00 19.33 ? 2055 HOH A O 1 HETATM 6398 O O . HOH M 6 . ? -6.380 22.309 16.017 1.00 15.09 ? 2056 HOH A O 1 HETATM 6399 O O . HOH M 6 . ? -8.026 24.130 17.387 1.00 24.74 ? 2057 HOH A O 1 HETATM 6400 O O . HOH M 6 . ? -8.237 17.815 20.205 1.00 14.09 ? 2058 HOH A O 1 HETATM 6401 O O . HOH M 6 . ? -3.962 19.519 17.139 1.00 11.62 ? 2059 HOH A O 1 HETATM 6402 O O . HOH M 6 . ? -0.394 11.514 15.506 1.00 17.12 ? 2060 HOH A O 1 HETATM 6403 O O . HOH M 6 . ? -2.265 11.528 19.015 1.00 20.54 ? 2061 HOH A O 1 HETATM 6404 O O . HOH M 6 . ? 2.020 8.346 15.210 1.00 28.62 ? 2062 HOH A O 1 HETATM 6405 O O . HOH M 6 . ? -2.902 6.214 19.816 1.00 20.30 ? 2063 HOH A O 1 HETATM 6406 O O . HOH M 6 . ? 3.960 7.462 18.401 1.00 26.05 ? 2064 HOH A O 1 HETATM 6407 O O . HOH M 6 . ? 3.142 4.154 21.086 1.00 23.01 ? 2065 HOH A O 1 HETATM 6408 O O . HOH M 6 . ? 6.834 1.366 12.283 1.00 11.02 ? 2066 HOH A O 1 HETATM 6409 O O . HOH M 6 . ? 4.674 -1.905 -4.623 1.00 16.06 ? 2067 HOH A O 1 HETATM 6410 O O . HOH M 6 . ? 0.074 -2.877 17.952 1.00 20.71 ? 2068 HOH A O 1 HETATM 6411 O O . HOH M 6 . ? -3.494 -1.819 17.722 1.00 32.35 ? 2069 HOH A O 1 HETATM 6412 O O . HOH M 6 . ? -2.634 -0.159 22.122 1.00 50.22 ? 2070 HOH A O 1 HETATM 6413 O O . HOH M 6 . ? -5.896 2.831 20.079 1.00 26.90 ? 2071 HOH A O 1 HETATM 6414 O O . HOH M 6 . ? -5.269 6.339 18.528 1.00 23.34 ? 2072 HOH A O 1 HETATM 6415 O O . HOH M 6 . ? -8.903 4.040 17.460 1.00 26.06 ? 2073 HOH A O 1 HETATM 6416 O O . HOH M 6 . ? -9.926 5.287 13.614 1.00 14.99 ? 2074 HOH A O 1 HETATM 6417 O O . HOH M 6 . ? -10.373 5.963 19.603 1.00 20.83 ? 2075 HOH A O 1 HETATM 6418 O O . HOH M 6 . ? -11.260 9.113 20.010 1.00 27.18 ? 2076 HOH A O 1 HETATM 6419 O O . HOH M 6 . ? -1.372 -6.744 14.687 1.00 21.79 ? 2077 HOH A O 1 HETATM 6420 O O . HOH M 6 . ? -12.899 4.141 6.297 1.00 21.89 ? 2078 HOH A O 1 HETATM 6421 O O . HOH M 6 . ? -13.872 7.034 4.150 1.00 22.06 ? 2079 HOH A O 1 HETATM 6422 O O . HOH M 6 . ? -16.946 12.803 10.091 1.00 27.55 ? 2080 HOH A O 1 HETATM 6423 O O . HOH M 6 . ? -5.203 14.498 3.169 1.00 10.68 ? 2081 HOH A O 1 HETATM 6424 O O . HOH M 6 . ? -15.849 13.246 5.337 1.00 31.37 ? 2082 HOH A O 1 HETATM 6425 O O . HOH M 6 . ? -9.453 20.035 6.114 1.00 16.35 ? 2083 HOH A O 1 HETATM 6426 O O . HOH M 6 . ? -14.027 17.883 11.839 1.00 16.50 ? 2084 HOH A O 1 HETATM 6427 O O . HOH M 6 . ? -0.446 24.268 8.698 1.00 13.49 ? 2085 HOH A O 1 HETATM 6428 O O . HOH M 6 . ? 7.521 21.857 11.233 1.00 13.67 ? 2086 HOH A O 1 HETATM 6429 O O . HOH M 6 . ? 14.051 26.438 6.068 1.00 25.32 ? 2087 HOH A O 1 HETATM 6430 O O . HOH M 6 . ? 19.009 21.729 8.720 1.00 22.96 ? 2088 HOH A O 1 HETATM 6431 O O . HOH M 6 . ? 14.924 25.910 13.143 1.00 27.55 ? 2089 HOH A O 1 HETATM 6432 O O . HOH M 6 . ? 12.169 21.840 11.733 1.00 15.47 ? 2090 HOH A O 1 HETATM 6433 O O . HOH M 6 . ? 19.143 24.978 12.843 1.00 28.23 ? 2091 HOH A O 1 HETATM 6434 O O . HOH M 6 . ? 19.814 22.694 15.186 1.00 41.36 ? 2092 HOH A O 1 HETATM 6435 O O . HOH M 6 . ? 9.577 20.708 12.607 1.00 17.83 ? 2093 HOH A O 1 HETATM 6436 O O . HOH M 6 . ? 19.467 19.264 7.897 1.00 14.50 ? 2094 HOH A O 1 HETATM 6437 O O . HOH M 6 . ? 25.737 17.999 11.602 1.00 17.42 ? 2095 HOH A O 1 HETATM 6438 O O . HOH M 6 . ? 22.788 15.212 12.036 1.00 11.44 ? 2096 HOH A O 1 HETATM 6439 O O . HOH M 6 . ? 26.050 16.432 8.134 1.00 16.25 ? 2097 HOH A O 1 HETATM 6440 O O . HOH M 6 . ? 23.274 -17.888 12.844 1.00 13.91 ? 2098 HOH A O 1 HETATM 6441 O O . HOH M 6 . ? 22.602 19.928 3.884 1.00 27.60 ? 2099 HOH A O 1 HETATM 6442 O O . HOH M 6 . ? 21.891 19.426 6.604 1.00 16.84 ? 2100 HOH A O 1 HETATM 6443 O O . HOH M 6 . ? 23.595 -21.562 17.096 1.00 39.17 ? 2101 HOH A O 1 HETATM 6444 O O . HOH M 6 . ? 23.260 -21.923 14.522 1.00 24.82 ? 2102 HOH A O 1 HETATM 6445 O O . HOH M 6 . ? 34.119 19.716 5.517 1.00 50.71 ? 2103 HOH A O 1 HETATM 6446 O O . HOH M 6 . ? 31.098 15.044 0.743 1.00 17.25 ? 2104 HOH A O 1 HETATM 6447 O O . HOH M 6 . ? 31.668 13.567 3.031 1.00 23.09 ? 2105 HOH A O 1 HETATM 6448 O O . HOH M 6 . ? 28.274 14.871 8.036 1.00 23.78 ? 2106 HOH A O 1 HETATM 6449 O O . HOH M 6 . ? 42.198 -8.795 7.378 1.00 39.65 ? 2107 HOH A O 1 HETATM 6450 O O . HOH M 6 . ? 27.178 17.306 18.119 1.00 30.40 ? 2108 HOH A O 1 HETATM 6451 O O . HOH M 6 . ? 23.062 19.089 17.048 1.00 25.86 ? 2109 HOH A O 1 HETATM 6452 O O . HOH M 6 . ? 21.357 18.564 14.415 1.00 19.01 ? 2110 HOH A O 1 HETATM 6453 O O . HOH M 6 . ? 24.105 14.857 19.233 1.00 18.34 ? 2111 HOH A O 1 HETATM 6454 O O . HOH M 6 . ? 20.093 20.450 20.791 1.00 25.92 ? 2112 HOH A O 1 HETATM 6455 O O . HOH M 6 . ? 13.921 13.683 25.790 1.00 33.24 ? 2113 HOH A O 1 HETATM 6456 O O . HOH M 6 . ? 17.435 12.922 27.063 1.00 22.65 ? 2114 HOH A O 1 HETATM 6457 O O . HOH M 6 . ? 12.697 8.365 20.691 1.00 19.04 ? 2115 HOH A O 1 HETATM 6458 O O . HOH M 6 . ? 11.461 8.680 16.199 1.00 14.94 ? 2116 HOH A O 1 HETATM 6459 O O . HOH M 6 . ? 12.339 11.504 14.161 1.00 11.32 ? 2117 HOH A O 1 HETATM 6460 O O . HOH M 6 . ? 13.469 5.170 15.030 1.00 11.86 ? 2118 HOH A O 1 HETATM 6461 O O . HOH M 6 . ? 11.426 6.880 14.105 1.00 12.54 ? 2119 HOH A O 1 HETATM 6462 O O . HOH M 6 . ? 14.719 4.342 19.220 1.00 11.75 ? 2120 HOH A O 1 HETATM 6463 O O . HOH M 6 . ? 12.071 4.671 17.486 0.50 11.52 ? 2121 HOH A O 1 HETATM 6464 O O . HOH M 6 . ? 8.961 5.684 13.620 1.00 13.23 ? 2122 HOH A O 1 HETATM 6465 O O . HOH M 6 . ? 6.437 4.040 11.574 1.00 11.69 ? 2123 HOH A O 1 HETATM 6466 O O . HOH M 6 . ? 20.126 -24.510 -1.787 1.00 29.96 ? 2124 HOH A O 1 HETATM 6467 O O . HOH M 6 . ? 11.499 10.419 -11.402 1.00 23.87 ? 2125 HOH A O 1 HETATM 6468 O O . HOH M 6 . ? 8.482 12.562 -9.759 1.00 27.86 ? 2126 HOH A O 1 HETATM 6469 O O . HOH M 6 . ? 14.297 22.996 -0.227 1.00 23.61 ? 2127 HOH A O 1 HETATM 6470 O O . HOH M 6 . ? 12.760 21.945 -4.890 1.00 28.57 ? 2128 HOH A O 1 HETATM 6471 O O . HOH M 6 . ? 16.343 21.835 -3.681 1.00 24.12 ? 2129 HOH A O 1 HETATM 6472 O O . HOH M 6 . ? 11.996 23.318 -1.608 0.50 14.20 ? 2130 HOH A O 1 HETATM 6473 O O . HOH M 6 . ? 4.551 11.706 -5.439 1.00 22.39 ? 2131 HOH A O 1 HETATM 6474 O O . HOH M 6 . ? 4.908 2.971 -11.183 1.00 23.46 ? 2132 HOH A O 1 HETATM 6475 O O . HOH M 6 . ? 12.620 7.325 -8.561 1.00 24.75 ? 2133 HOH A O 1 HETATM 6476 O O . HOH M 6 . ? 19.454 7.207 -10.034 1.00 25.17 ? 2134 HOH A O 1 HETATM 6477 O O . HOH M 6 . ? 15.137 4.891 -1.882 1.00 9.76 ? 2135 HOH A O 1 HETATM 6478 O O . HOH M 6 . ? 17.168 10.418 -9.186 1.00 18.20 ? 2136 HOH A O 1 HETATM 6479 O O . HOH M 6 . ? 18.583 3.400 -8.327 1.00 21.04 ? 2137 HOH A O 1 HETATM 6480 O O . HOH M 6 . ? 14.420 5.593 -9.090 1.00 23.19 ? 2138 HOH A O 1 HETATM 6481 O O . HOH M 6 . ? 16.659 -3.850 -4.819 1.00 10.75 ? 2139 HOH A O 1 HETATM 6482 O O . HOH M 6 . ? 14.742 -2.558 -13.372 1.00 38.45 ? 2140 HOH A O 1 HETATM 6483 O O . HOH M 6 . ? 20.174 -1.698 -10.897 1.00 30.75 ? 2141 HOH A O 1 HETATM 6484 O O . HOH M 6 . ? 19.164 0.183 -8.999 1.00 17.46 ? 2142 HOH A O 1 HETATM 6485 O O . HOH M 6 . ? 17.994 -6.251 -10.417 1.00 18.26 ? 2143 HOH A O 1 HETATM 6486 O O . HOH M 6 . ? 26.829 -6.386 -11.965 1.00 15.36 ? 2144 HOH A O 1 HETATM 6487 O O . HOH M 6 . ? 26.835 -2.414 1.619 1.00 10.11 ? 2145 HOH A O 1 HETATM 6488 O O . HOH M 6 . ? 34.455 7.921 3.716 1.00 23.65 ? 2146 HOH A O 1 HETATM 6489 O O . HOH M 6 . ? 35.173 5.752 -0.199 1.00 22.26 ? 2147 HOH A O 1 HETATM 6490 O O . HOH M 6 . ? 30.520 9.325 14.874 1.00 19.21 ? 2148 HOH A O 1 HETATM 6491 O O . HOH M 6 . ? 34.214 9.300 17.476 1.00 26.47 ? 2149 HOH A O 1 HETATM 6492 O O . HOH M 6 . ? 30.341 3.957 21.471 1.00 14.95 ? 2150 HOH A O 1 HETATM 6493 O O . HOH M 6 . ? 33.600 6.245 20.921 1.00 28.54 ? 2151 HOH A O 1 HETATM 6494 O O . HOH M 6 . ? 33.986 9.353 -4.202 1.00 29.74 ? 2152 HOH A O 1 HETATM 6495 O O . HOH M 6 . ? 29.782 -0.607 23.709 1.00 13.89 ? 2153 HOH A O 1 HETATM 6496 O O . HOH M 6 . ? 25.877 0.419 25.935 1.00 13.07 ? 2154 HOH A O 1 HETATM 6497 O O . HOH M 6 . ? 18.769 -0.974 23.047 1.00 11.46 ? 2155 HOH A O 1 HETATM 6498 O O . HOH M 6 . ? 5.228 -4.628 -5.566 1.00 16.89 ? 2156 HOH A O 1 HETATM 6499 O O . HOH M 6 . ? 7.200 -0.826 -4.987 1.00 12.74 ? 2157 HOH A O 1 HETATM 6500 O O . HOH M 6 . ? -2.686 6.115 -0.532 1.00 10.53 ? 2158 HOH A O 1 HETATM 6501 O O . HOH M 6 . ? -3.245 7.426 -6.766 1.00 22.49 ? 2159 HOH A O 1 HETATM 6502 O O . HOH M 6 . ? -0.165 5.805 -5.642 1.00 20.85 ? 2160 HOH A O 1 HETATM 6503 O O . HOH M 6 . ? -3.069 13.159 -4.763 1.00 25.06 ? 2161 HOH A O 1 HETATM 6504 O O . HOH M 6 . ? -6.955 8.074 -1.378 1.00 14.31 ? 2162 HOH A O 1 HETATM 6505 O O . HOH M 6 . ? -6.832 8.169 -5.376 1.00 23.75 ? 2163 HOH A O 1 HETATM 6506 O O . HOH M 6 . ? -5.649 15.173 -2.926 1.00 13.29 ? 2164 HOH A O 1 HETATM 6507 O O . HOH M 6 . ? 5.062 13.149 -3.400 1.00 19.04 ? 2165 HOH A O 1 HETATM 6508 O O . HOH M 6 . ? 10.462 21.532 -2.760 1.00 23.33 ? 2166 HOH A O 1 HETATM 6509 O O . HOH M 6 . ? 7.678 22.285 0.856 1.00 17.34 ? 2167 HOH A O 1 HETATM 6510 O O . HOH M 6 . ? 2.317 20.332 0.031 1.00 24.63 ? 2168 HOH A O 1 HETATM 6511 O O . HOH M 6 . ? 5.496 6.516 6.210 1.00 7.96 ? 2169 HOH A O 1 HETATM 6512 O O . HOH M 6 . ? 4.245 1.970 0.382 1.00 10.60 ? 2170 HOH A O 1 HETATM 6513 O O . HOH M 6 . ? 2.665 3.255 5.385 1.00 9.25 ? 2171 HOH A O 1 HETATM 6514 O O . HOH M 6 . ? 10.415 -9.581 15.702 1.00 26.48 ? 2172 HOH A O 1 HETATM 6515 O O . HOH M 6 . ? 1.319 -6.140 14.221 1.00 18.41 ? 2173 HOH A O 1 HETATM 6516 O O . HOH M 6 . ? 2.167 -3.190 16.042 1.00 20.43 ? 2174 HOH A O 1 HETATM 6517 O O . HOH M 6 . ? 3.755 1.561 8.669 1.00 10.57 ? 2175 HOH A O 1 HETATM 6518 O O . HOH M 6 . ? 2.935 4.844 7.658 1.00 9.69 ? 2176 HOH A O 1 HETATM 6519 O O . HOH M 6 . ? -4.057 2.191 4.151 1.00 17.84 ? 2177 HOH A O 1 HETATM 6520 O O . HOH M 6 . ? 1.502 0.138 -1.740 1.00 16.03 ? 2178 HOH A O 1 HETATM 6521 O O . HOH M 6 . ? -2.834 1.021 0.627 1.00 27.26 ? 2179 HOH A O 1 HETATM 6522 O O . HOH M 6 . ? 2.102 6.418 5.453 1.00 8.83 ? 2180 HOH A O 1 HETATM 6523 O O . HOH M 6 . ? -5.075 10.744 4.738 1.00 11.02 ? 2181 HOH A O 1 HETATM 6524 O O . HOH M 6 . ? -7.004 9.198 6.003 1.00 11.31 ? 2182 HOH A O 1 HETATM 6525 O O . HOH M 6 . ? -7.409 -0.164 8.301 1.00 18.04 ? 2183 HOH A O 1 HETATM 6526 O O . HOH M 6 . ? -10.819 2.959 14.445 1.00 18.29 ? 2184 HOH A O 1 HETATM 6527 O O . HOH M 6 . ? -7.388 -5.394 11.701 1.00 22.18 ? 2185 HOH A O 1 HETATM 6528 O O . HOH M 6 . ? -3.256 -5.824 13.110 1.00 23.47 ? 2186 HOH A O 1 HETATM 6529 O O . HOH M 6 . ? -4.789 -3.304 15.693 1.00 23.89 ? 2187 HOH A O 1 HETATM 6530 O O . HOH M 6 . ? 5.810 -2.634 9.814 1.00 9.16 ? 2188 HOH A O 1 HETATM 6531 O O . HOH M 6 . ? 33.046 -6.890 18.715 1.00 11.98 ? 2189 HOH A O 1 HETATM 6532 O O . HOH M 6 . ? 35.248 -6.055 22.490 1.00 21.74 ? 2190 HOH A O 1 HETATM 6533 O O . HOH M 6 . ? 34.180 -4.798 20.168 1.00 13.26 ? 2191 HOH A O 1 HETATM 6534 O O . HOH M 6 . ? 29.315 -9.858 10.900 1.00 11.56 ? 2192 HOH A O 1 HETATM 6535 O O . HOH M 6 . ? 22.893 -10.914 15.198 1.00 10.92 ? 2193 HOH A O 1 HETATM 6536 O O . HOH M 6 . ? 25.916 -5.202 8.702 1.00 9.86 ? 2194 HOH A O 1 HETATM 6537 O O . HOH M 6 . ? 7.055 -11.394 -1.892 1.00 17.46 ? 2195 HOH A O 1 HETATM 6538 O O . HOH M 6 . ? 0.050 -16.731 4.184 1.00 22.95 ? 2196 HOH A O 1 HETATM 6539 O O . HOH M 6 . ? 2.844 -13.950 -7.830 1.00 17.03 ? 2197 HOH A O 1 HETATM 6540 O O . HOH M 6 . ? 1.446 -4.384 -3.728 1.00 24.09 ? 2198 HOH A O 1 HETATM 6541 O O . HOH M 6 . ? 1.733 -9.541 -9.086 1.00 19.73 ? 2199 HOH A O 1 HETATM 6542 O O . HOH M 6 . ? 4.842 -13.743 -9.614 1.00 19.75 ? 2200 HOH A O 1 HETATM 6543 O O . HOH M 6 . ? 6.328 -7.146 0.222 1.00 14.92 ? 2201 HOH A O 1 HETATM 6544 O O . HOH M 6 . ? 0.371 -2.320 -1.952 1.00 21.76 ? 2202 HOH A O 1 HETATM 6545 O O . HOH M 6 . ? 4.306 -1.223 -1.926 1.00 14.46 ? 2203 HOH A O 1 HETATM 6546 O O . HOH M 6 . ? -1.081 -5.601 -1.056 1.00 16.01 ? 2204 HOH A O 1 HETATM 6547 O O . HOH M 6 . ? -3.011 -4.894 1.131 1.00 15.20 ? 2205 HOH A O 1 HETATM 6548 O O . HOH M 6 . ? -4.753 -6.212 2.539 1.00 22.41 ? 2206 HOH A O 1 HETATM 6549 O O . HOH M 6 . ? -5.735 -7.149 12.928 1.00 18.49 ? 2207 HOH A O 1 HETATM 6550 O O . HOH M 6 . ? 0.177 -16.517 12.223 1.00 16.84 ? 2208 HOH A O 1 HETATM 6551 O O . HOH M 6 . ? -2.735 -14.504 4.065 1.00 28.95 ? 2209 HOH A O 1 HETATM 6552 O O . HOH M 6 . ? -5.407 -8.735 4.879 1.00 22.00 ? 2210 HOH A O 1 HETATM 6553 O O . HOH M 6 . ? 3.750 -11.795 9.572 1.00 11.74 ? 2211 HOH A O 1 HETATM 6554 O O . HOH M 6 . ? 4.370 -21.123 15.790 1.00 18.87 ? 2212 HOH A O 1 HETATM 6555 O O . HOH M 6 . ? 3.339 -18.403 6.922 1.00 14.04 ? 2213 HOH A O 1 HETATM 6556 O O . HOH M 6 . ? 7.687 -14.627 10.962 1.00 9.69 ? 2214 HOH A O 1 HETATM 6557 O O . HOH M 6 . ? 10.552 -15.336 11.291 1.00 10.33 ? 2215 HOH A O 1 HETATM 6558 O O . HOH M 6 . ? 13.446 -16.830 9.439 1.00 11.33 ? 2216 HOH A O 1 HETATM 6559 O O . HOH M 6 . ? 5.402 -9.688 10.608 1.00 9.80 ? 2217 HOH A O 1 HETATM 6560 O O . HOH M 6 . ? 6.931 -8.156 14.888 1.00 19.58 ? 2218 HOH A O 1 HETATM 6561 O O . HOH M 6 . ? 18.215 -12.145 11.554 1.00 24.03 ? 2219 HOH A O 1 HETATM 6562 O O . HOH M 6 . ? 21.289 -17.555 10.797 1.00 15.08 ? 2220 HOH A O 1 HETATM 6563 O O . HOH M 6 . ? 24.577 -15.589 11.660 1.00 11.87 ? 2221 HOH A O 1 HETATM 6564 O O . HOH M 6 . ? 29.458 -8.959 14.536 1.00 11.82 ? 2222 HOH A O 1 HETATM 6565 O O . HOH M 6 . ? 35.155 -10.212 21.210 1.00 28.52 ? 2223 HOH A O 1 HETATM 6566 O O . HOH M 6 . ? 22.668 -17.844 15.951 1.00 23.53 ? 2224 HOH A O 1 HETATM 6567 O O . HOH M 6 . ? 25.006 -19.090 17.148 1.00 17.33 ? 2225 HOH A O 1 HETATM 6568 O O . HOH M 6 . ? 24.934 -20.037 13.364 1.00 13.00 ? 2226 HOH A O 1 HETATM 6569 O O . HOH M 6 . ? 32.041 -21.307 20.327 1.00 23.95 ? 2227 HOH A O 1 HETATM 6570 O O . HOH M 6 . ? 37.061 -16.819 16.458 1.00 26.50 ? 2228 HOH A O 1 HETATM 6571 O O . HOH M 6 . ? 38.477 -13.046 11.697 1.00 21.56 ? 2229 HOH A O 1 HETATM 6572 O O . HOH M 6 . ? 43.026 -13.022 15.832 1.00 28.01 ? 2230 HOH A O 1 HETATM 6573 O O . HOH M 6 . ? 34.254 -9.846 16.125 1.00 14.26 ? 2231 HOH A O 1 HETATM 6574 O O . HOH M 6 . ? 31.271 1.528 22.734 1.00 16.49 ? 2232 HOH A O 1 HETATM 6575 O O . HOH M 6 . ? 37.227 3.525 22.971 1.00 30.40 ? 2233 HOH A O 1 HETATM 6576 O O . HOH M 6 . ? 42.320 -3.850 12.000 1.00 25.81 ? 2234 HOH A O 1 HETATM 6577 O O . HOH M 6 . ? 41.905 -10.279 13.726 1.00 25.32 ? 2235 HOH A O 1 HETATM 6578 O O . HOH M 6 . ? 42.207 -6.472 8.727 1.00 25.95 ? 2236 HOH A O 1 HETATM 6579 O O . HOH M 6 . ? 42.546 1.934 16.847 1.00 23.81 ? 2237 HOH A O 1 HETATM 6580 O O . HOH M 6 . ? 43.009 -0.965 12.764 1.00 29.36 ? 2238 HOH A O 1 HETATM 6581 O O . HOH M 6 . ? 33.688 3.016 12.907 1.00 13.22 ? 2239 HOH A O 1 HETATM 6582 O O . HOH M 6 . ? 37.459 6.153 17.836 1.00 24.88 ? 2240 HOH A O 1 HETATM 6583 O O . HOH M 6 . ? 36.912 3.310 4.385 1.00 25.79 ? 2241 HOH A O 1 HETATM 6584 O O . HOH M 6 . ? 31.711 -11.636 -6.384 1.00 21.78 ? 2242 HOH A O 1 HETATM 6585 O O . HOH M 6 . ? 25.197 -11.774 -10.165 1.00 18.52 ? 2243 HOH A O 1 HETATM 6586 O O . HOH M 6 . ? 15.518 -18.050 -16.341 1.00 31.81 ? 2244 HOH A O 1 HETATM 6587 O O . HOH M 6 . ? 17.891 -18.976 -5.336 1.00 16.67 ? 2245 HOH A O 1 HETATM 6588 O O . HOH M 6 . ? 20.314 -19.618 -2.163 1.00 13.74 ? 2246 HOH A O 1 HETATM 6589 O O . HOH M 6 . ? 20.785 -21.076 -7.554 1.00 32.55 ? 2247 HOH A O 1 HETATM 6590 O O . HOH M 6 . ? 30.651 -10.883 6.063 1.00 11.61 ? 2248 HOH A O 1 HETATM 6591 O O . HOH M 6 . ? 29.731 -9.074 8.202 1.00 12.53 ? 2249 HOH A O 1 HETATM 6592 O O . HOH M 6 . ? 42.841 -2.674 6.962 1.00 25.17 ? 2250 HOH A O 1 HETATM 6593 O O . HOH M 6 . ? 39.720 2.168 2.773 1.00 25.94 ? 2251 HOH A O 1 HETATM 6594 O O . HOH M 6 . ? 43.331 -4.973 -0.764 1.00 25.55 ? 2252 HOH A O 1 HETATM 6595 O O . HOH M 6 . ? 41.101 -10.167 3.618 1.00 23.00 ? 2253 HOH A O 1 HETATM 6596 O O . HOH M 6 . ? 34.976 -12.205 0.832 1.00 12.37 ? 2254 HOH A O 1 HETATM 6597 O O . HOH M 6 . ? 39.212 -11.334 6.476 1.00 23.54 ? 2255 HOH A O 1 HETATM 6598 O O . HOH M 6 . ? 36.388 -9.434 -2.816 1.00 41.50 ? 2256 HOH A O 1 HETATM 6599 O O . HOH M 6 . ? 38.337 -14.968 5.231 1.00 23.78 ? 2257 HOH A O 1 HETATM 6600 O O . HOH M 6 . ? 35.772 -14.568 1.929 1.00 14.54 ? 2258 HOH A O 1 HETATM 6601 O O . HOH M 6 . ? 35.088 -19.609 -1.454 1.00 23.40 ? 2259 HOH A O 1 HETATM 6602 O O . HOH M 6 . ? 36.725 -24.397 13.715 1.00 21.32 ? 2260 HOH A O 1 HETATM 6603 O O . HOH M 6 . ? 28.042 -25.650 17.280 1.00 23.39 ? 2261 HOH A O 1 HETATM 6604 O O . HOH M 6 . ? 29.832 -29.198 11.151 1.00 23.33 ? 2262 HOH A O 1 HETATM 6605 O O . HOH M 6 . ? 30.828 -23.607 9.895 1.00 13.16 ? 2263 HOH A O 1 HETATM 6606 O O . HOH M 6 . ? 30.030 -27.796 8.751 1.00 26.70 ? 2264 HOH A O 1 HETATM 6607 O O . HOH M 6 . ? 37.894 -20.890 7.688 1.00 23.37 ? 2265 HOH A O 1 HETATM 6608 O O . HOH M 6 . ? 29.688 -27.435 4.952 1.00 21.89 ? 2266 HOH A O 1 HETATM 6609 O O . HOH M 6 . ? 29.359 -12.630 3.274 1.00 14.92 ? 2267 HOH A O 1 HETATM 6610 O O . HOH M 6 . ? 34.433 -16.355 -2.227 1.00 25.25 ? 2268 HOH A O 1 HETATM 6611 O O . HOH M 6 . ? 32.218 -19.256 -1.455 1.00 32.26 ? 2269 HOH A O 1 HETATM 6612 O O . HOH M 6 . ? 25.895 -22.317 2.993 1.00 19.42 ? 2270 HOH A O 1 HETATM 6613 O O . HOH M 6 . ? 17.855 -22.957 -3.264 1.00 26.64 ? 2271 HOH A O 1 HETATM 6614 O O . HOH M 6 . ? 15.982 -19.595 -3.396 1.00 10.80 ? 2272 HOH A O 1 HETATM 6615 O O . HOH M 6 . ? 22.031 -22.822 -1.079 1.00 17.82 ? 2273 HOH A O 1 HETATM 6616 O O . HOH M 6 . ? 20.720 -20.746 14.563 1.00 28.44 ? 2274 HOH A O 1 HETATM 6617 O O . HOH M 6 . ? 18.739 -16.867 11.072 1.00 21.40 ? 2275 HOH A O 1 HETATM 6618 O O . HOH M 6 . ? 11.676 -17.958 11.261 1.00 11.40 ? 2276 HOH A O 1 HETATM 6619 O O . HOH M 6 . ? 8.999 -25.598 7.189 1.00 22.76 ? 2277 HOH A O 1 HETATM 6620 O O . HOH M 6 . ? 5.764 -18.998 0.150 1.00 20.38 ? 2278 HOH A O 1 HETATM 6621 O O . HOH M 6 . ? 4.909 -24.356 8.613 1.00 28.46 ? 2279 HOH A O 1 HETATM 6622 O O . HOH M 6 . ? 6.401 -16.665 -0.838 1.00 28.64 ? 2280 HOH A O 1 HETATM 6623 O O . HOH M 6 . ? 15.497 -13.815 -7.252 1.00 10.25 ? 2281 HOH A O 1 HETATM 6624 O O . HOH M 6 . ? 9.085 -11.583 -3.548 1.00 14.40 ? 2282 HOH A O 1 HETATM 6625 O O . HOH M 6 . ? 8.031 -12.947 -5.610 1.00 20.99 ? 2283 HOH A O 1 HETATM 6626 O O . HOH M 6 . ? 16.955 -8.786 -11.623 1.00 20.84 ? 2284 HOH A O 1 HETATM 6627 O O . HOH M 6 . ? 14.985 -11.828 -9.116 1.00 12.30 ? 2285 HOH A O 1 HETATM 6628 O O . HOH M 6 . ? 9.476 -0.451 -8.247 1.00 22.88 ? 2286 HOH A O 1 HETATM 6629 O O . HOH M 6 . ? 8.607 -2.987 -5.824 1.00 10.56 ? 2287 HOH A O 1 HETATM 6630 O O . HOH M 6 . ? 12.605 2.658 18.546 0.50 15.39 ? 2288 HOH A O 1 HETATM 6631 O O . HOH M 6 . ? 11.766 -5.095 22.441 1.00 32.96 ? 2289 HOH A O 1 HETATM 6632 O O . HOH M 6 . ? 12.711 1.476 22.395 1.00 23.73 ? 2290 HOH A O 1 HETATM 6633 O O . HOH M 6 . ? 16.479 1.461 29.856 1.00 20.88 ? 2291 HOH A O 1 HETATM 6634 O O . HOH M 6 . ? 10.754 -1.613 23.211 1.00 29.43 ? 2292 HOH A O 1 HETATM 6635 O O . HOH M 6 . ? 15.845 -1.578 28.859 1.00 19.39 ? 2293 HOH A O 1 HETATM 6636 O O . HOH M 6 . ? 20.583 -6.965 28.017 1.00 14.31 ? 2294 HOH A O 1 HETATM 6637 O O . HOH M 6 . ? 22.637 -5.550 24.027 1.00 16.31 ? 2295 HOH A O 1 HETATM 6638 O O . HOH M 6 . ? 21.538 -13.945 28.151 1.00 28.40 ? 2296 HOH A O 1 HETATM 6639 O O . HOH M 6 . ? 21.039 -12.724 22.057 1.00 19.32 ? 2297 HOH A O 1 HETATM 6640 O O . HOH M 6 . ? 25.578 -21.805 19.777 1.00 27.66 ? 2298 HOH A O 1 HETATM 6641 O O . HOH M 6 . ? 22.236 -15.245 22.420 1.00 20.12 ? 2299 HOH A O 1 HETATM 6642 O O . HOH M 6 . ? 26.268 -17.145 24.172 1.00 29.82 ? 2300 HOH A O 1 HETATM 6643 O O . HOH M 6 . ? 28.459 -18.814 18.163 1.00 17.29 ? 2301 HOH A O 1 HETATM 6644 O O . HOH M 6 . ? 27.746 -11.342 25.261 1.00 16.39 ? 2302 HOH A O 1 HETATM 6645 O O . HOH M 6 . ? 22.743 -5.891 26.579 1.00 13.15 ? 2303 HOH A O 1 HETATM 6646 O O . HOH M 6 . ? 26.315 -11.040 30.409 1.00 18.64 ? 2304 HOH A O 1 HETATM 6647 O O . HOH M 6 . ? 25.511 -7.777 33.473 1.00 23.29 ? 2305 HOH A O 1 HETATM 6648 O O . HOH M 6 . ? 16.100 -11.540 30.846 1.00 25.52 ? 2306 HOH A O 1 HETATM 6649 O O . HOH M 6 . ? 21.327 -1.732 32.490 1.00 23.86 ? 2307 HOH A O 1 HETATM 6650 O O . HOH M 6 . ? 28.621 -0.386 26.141 1.00 15.29 ? 2308 HOH A O 1 HETATM 6651 O O . HOH M 6 . ? 31.637 -3.485 26.814 1.00 22.63 ? 2309 HOH A O 1 HETATM 6652 O O . HOH M 6 . ? 20.601 6.800 32.708 1.00 18.02 ? 2310 HOH A O 1 HETATM 6653 O O . HOH M 6 . ? 28.422 -0.458 30.568 1.00 23.97 ? 2311 HOH A O 1 HETATM 6654 O O . HOH M 6 . ? 24.218 2.332 33.901 1.00 16.83 ? 2312 HOH A O 1 HETATM 6655 O O . HOH M 6 . ? 25.930 10.398 32.730 1.00 18.39 ? 2313 HOH A O 1 HETATM 6656 O O . HOH M 6 . ? 22.067 11.674 26.856 1.00 17.69 ? 2314 HOH A O 1 HETATM 6657 O O . HOH M 6 . ? 28.407 10.056 13.245 1.00 13.17 ? 2315 HOH A O 1 HETATM 6658 O O . HOH M 6 . ? 29.416 6.796 15.061 1.00 13.47 ? 2316 HOH A O 1 HETATM 6659 O O . HOH M 6 . ? 30.409 14.351 17.255 1.00 39.47 ? 2317 HOH A O 1 HETATM 6660 O O . HOH M 6 . ? 29.224 13.432 10.438 1.00 18.23 ? 2318 HOH A O 1 HETATM 6661 O O . HOH M 6 . ? 30.920 8.030 7.265 1.00 14.01 ? 2319 HOH A O 1 HETATM 6662 O O . HOH M 6 . ? 33.358 11.243 -2.128 1.00 23.97 ? 2320 HOH A O 1 HETATM 6663 O O . HOH M 6 . ? 23.775 1.952 -10.479 1.00 18.27 ? 2321 HOH A O 1 HETATM 6664 O O . HOH M 6 . ? 30.632 -4.915 -15.416 1.00 25.84 ? 2322 HOH A O 1 HETATM 6665 O O . HOH M 6 . ? 31.206 -1.228 -17.360 1.00 21.25 ? 2323 HOH A O 1 HETATM 6666 O O . HOH M 6 . ? 28.292 -3.405 -18.298 1.00 46.16 ? 2324 HOH A O 1 HETATM 6667 O O . HOH M 6 . ? 37.336 -4.426 -8.277 1.00 36.44 ? 2325 HOH A O 1 HETATM 6668 O O . HOH M 6 . ? 34.963 2.698 -7.403 1.00 24.11 ? 2326 HOH A O 1 HETATM 6669 O O . HOH M 6 . ? 33.819 -8.557 -6.465 1.00 25.77 ? 2327 HOH A O 1 HETATM 6670 O O . HOH M 6 . ? 10.216 4.029 15.504 1.00 19.17 ? 2328 HOH A O 1 HETATM 6671 O O . HOH M 6 . ? 9.463 0.371 12.146 1.00 11.92 ? 2329 HOH A O 1 HETATM 6672 O O . HOH M 6 . ? 11.934 -3.817 14.466 1.00 13.70 ? 2330 HOH A O 1 HETATM 6673 O O . HOH M 6 . ? 11.233 -5.800 16.083 1.00 25.05 ? 2331 HOH A O 1 HETATM 6674 O O . HOH M 6 . ? 17.344 -8.473 11.121 1.00 14.10 ? 2332 HOH A O 1 HETATM 6675 O O . HOH M 6 . ? 34.387 -25.795 14.394 1.00 25.96 ? 2333 HOH A O 1 HETATM 6676 O O . HOH N 6 . ? 22.884 14.122 43.546 1.00 14.24 ? 2001 HOH B O 1 HETATM 6677 O O . HOH N 6 . ? 25.215 9.587 48.225 1.00 14.17 ? 2002 HOH B O 1 HETATM 6678 O O . HOH N 6 . ? 13.310 20.196 44.716 1.00 25.16 ? 2003 HOH B O 1 HETATM 6679 O O . HOH N 6 . ? 20.192 23.031 46.282 1.00 21.09 ? 2004 HOH B O 1 HETATM 6680 O O . HOH N 6 . ? 24.113 23.628 42.747 1.00 37.09 ? 2005 HOH B O 1 HETATM 6681 O O . HOH N 6 . ? 20.794 25.206 44.972 1.00 26.12 ? 2006 HOH B O 1 HETATM 6682 O O . HOH N 6 . ? 27.108 22.142 45.631 1.00 17.21 ? 2007 HOH B O 1 HETATM 6683 O O . HOH N 6 . ? 49.478 8.304 27.662 1.00 22.18 ? 2008 HOH B O 1 HETATM 6684 O O . HOH N 6 . ? 49.074 4.151 27.398 1.00 24.35 ? 2009 HOH B O 1 HETATM 6685 O O . HOH N 6 . ? 37.542 24.146 40.753 1.00 33.19 ? 2010 HOH B O 1 HETATM 6686 O O . HOH N 6 . ? 39.458 22.298 47.412 1.00 14.05 ? 2011 HOH B O 1 HETATM 6687 O O . HOH N 6 . ? 39.346 21.959 40.387 1.00 19.77 ? 2012 HOH B O 1 HETATM 6688 O O . HOH N 6 . ? 35.971 21.248 40.818 1.00 15.56 ? 2013 HOH B O 1 HETATM 6689 O O . HOH N 6 . ? 44.441 21.479 42.711 1.00 17.16 ? 2014 HOH B O 1 HETATM 6690 O O . HOH N 6 . ? 32.843 12.021 57.510 1.00 22.19 ? 2015 HOH B O 1 HETATM 6691 O O . HOH N 6 . ? 29.211 7.344 55.108 1.00 17.27 ? 2016 HOH B O 1 HETATM 6692 O O . HOH N 6 . ? 51.330 18.247 37.943 1.00 17.20 ? 2017 HOH B O 1 HETATM 6693 O O . HOH N 6 . ? 49.964 10.836 41.261 1.00 10.76 ? 2018 HOH B O 1 HETATM 6694 O O . HOH N 6 . ? 13.458 28.860 57.867 1.00 27.81 ? 2019 HOH B O 1 HETATM 6695 O O . HOH N 6 . ? 50.968 6.127 27.505 1.00 27.33 ? 2020 HOH B O 1 HETATM 6696 O O . HOH N 6 . ? 49.470 2.400 29.417 1.00 16.91 ? 2021 HOH B O 1 HETATM 6697 O O . HOH N 6 . ? 53.707 5.471 27.207 1.00 19.51 ? 2022 HOH B O 1 HETATM 6698 O O . HOH N 6 . ? 29.543 1.491 52.051 1.00 11.63 ? 2023 HOH B O 1 HETATM 6699 O O . HOH N 6 . ? 17.593 0.921 61.088 1.00 47.85 ? 2024 HOH B O 1 HETATM 6700 O O . HOH N 6 . ? 25.085 -1.834 62.046 1.00 42.06 ? 2025 HOH B O 1 HETATM 6701 O O . HOH N 6 . ? 13.064 2.513 47.291 1.00 30.90 ? 2026 HOH B O 1 HETATM 6702 O O . HOH N 6 . ? 59.108 7.043 31.919 1.00 28.58 ? 2027 HOH B O 1 HETATM 6703 O O . HOH N 6 . ? 56.490 11.853 32.353 1.00 20.05 ? 2028 HOH B O 1 HETATM 6704 O O . HOH N 6 . ? 17.419 17.145 42.362 1.00 25.47 ? 2029 HOH B O 1 HETATM 6705 O O . HOH N 6 . ? 53.914 12.583 24.252 1.00 36.78 ? 2030 HOH B O 1 HETATM 6706 O O . HOH N 6 . ? 48.845 9.724 29.875 1.00 19.32 ? 2031 HOH B O 1 HETATM 6707 O O . HOH N 6 . ? 50.984 12.916 28.468 1.00 21.31 ? 2032 HOH B O 1 HETATM 6708 O O . HOH N 6 . ? 43.396 12.251 32.175 1.00 22.36 ? 2033 HOH B O 1 HETATM 6709 O O . HOH N 6 . ? 45.109 14.130 30.672 1.00 24.45 ? 2034 HOH B O 1 HETATM 6710 O O . HOH N 6 . ? 43.021 18.093 31.073 1.00 48.97 ? 2035 HOH B O 1 HETATM 6711 O O . HOH N 6 . ? 28.979 6.429 50.891 1.00 10.55 ? 2036 HOH B O 1 HETATM 6712 O O . HOH N 6 . ? 30.308 11.320 57.074 1.00 26.92 ? 2037 HOH B O 1 HETATM 6713 O O . HOH N 6 . ? 26.502 11.731 56.016 1.00 26.17 ? 2038 HOH B O 1 HETATM 6714 O O . HOH N 6 . ? 31.199 8.977 53.904 1.00 11.20 ? 2039 HOH B O 1 HETATM 6715 O O . HOH N 6 . ? 35.546 10.797 54.070 1.00 11.30 ? 2040 HOH B O 1 HETATM 6716 O O . HOH N 6 . ? 33.496 14.370 56.441 1.00 13.48 ? 2041 HOH B O 1 HETATM 6717 O O . HOH N 6 . ? 34.930 8.981 60.051 1.00 16.23 ? 2042 HOH B O 1 HETATM 6718 O O . HOH N 6 . ? 29.103 14.899 56.561 1.00 30.90 ? 2043 HOH B O 1 HETATM 6719 O O . HOH N 6 . ? 32.928 5.300 59.864 1.00 28.63 ? 2044 HOH B O 1 HETATM 6720 O O . HOH N 6 . ? 26.641 16.223 57.420 1.00 27.60 ? 2045 HOH B O 1 HETATM 6721 O O . HOH N 6 . ? 19.608 22.920 56.789 1.00 26.78 ? 2046 HOH B O 1 HETATM 6722 O O . HOH N 6 . ? 18.894 23.442 53.204 1.00 26.74 ? 2047 HOH B O 1 HETATM 6723 O O . HOH N 6 . ? 28.703 11.890 29.460 1.00 23.21 ? 2048 HOH B O 1 HETATM 6724 O O . HOH N 6 . ? 17.305 28.620 51.638 1.00 22.28 ? 2049 HOH B O 1 HETATM 6725 O O . HOH N 6 . ? 15.079 27.359 50.382 1.00 18.72 ? 2050 HOH B O 1 HETATM 6726 O O . HOH N 6 . ? 15.079 26.481 57.563 1.00 28.08 ? 2051 HOH B O 1 HETATM 6727 O O . HOH N 6 . ? 48.117 15.784 71.664 1.00 25.99 ? 2052 HOH B O 1 HETATM 6728 O O . HOH N 6 . ? 20.969 12.375 60.243 1.00 25.28 ? 2053 HOH B O 1 HETATM 6729 O O . HOH N 6 . ? 22.304 12.110 63.747 1.00 35.43 ? 2054 HOH B O 1 HETATM 6730 O O . HOH N 6 . ? 27.593 9.048 59.618 1.00 30.91 ? 2055 HOH B O 1 HETATM 6731 O O . HOH N 6 . ? 26.734 5.735 62.601 1.00 26.91 ? 2056 HOH B O 1 HETATM 6732 O O . HOH N 6 . ? 30.736 2.831 54.035 1.00 11.19 ? 2057 HOH B O 1 HETATM 6733 O O . HOH N 6 . ? 28.952 -0.934 37.234 1.00 21.49 ? 2058 HOH B O 1 HETATM 6734 O O . HOH N 6 . ? 23.989 -1.516 59.695 1.00 21.90 ? 2059 HOH B O 1 HETATM 6735 O O . HOH N 6 . ? 20.531 -0.517 59.639 1.00 32.91 ? 2060 HOH B O 1 HETATM 6736 O O . HOH N 6 . ? 20.472 7.505 61.247 1.00 20.44 ? 2061 HOH B O 1 HETATM 6737 O O . HOH N 6 . ? 20.499 3.976 40.370 1.00 22.84 ? 2062 HOH B O 1 HETATM 6738 O O . HOH N 6 . ? 13.723 5.964 54.810 1.00 18.25 ? 2063 HOH B O 1 HETATM 6739 O O . HOH N 6 . ? 13.034 6.744 60.489 1.00 23.91 ? 2064 HOH B O 1 HETATM 6740 O O . HOH N 6 . ? 11.998 9.961 61.104 1.00 26.56 ? 2065 HOH B O 1 HETATM 6741 O O . HOH N 6 . ? 22.871 -5.367 56.819 1.00 21.43 ? 2066 HOH B O 1 HETATM 6742 O O . HOH N 6 . ? 11.076 4.741 47.307 1.00 25.51 ? 2067 HOH B O 1 HETATM 6743 O O . HOH N 6 . ? 15.655 3.451 43.710 1.00 34.49 ? 2068 HOH B O 1 HETATM 6744 O O . HOH N 6 . ? 18.406 15.280 44.161 1.00 16.54 ? 2069 HOH B O 1 HETATM 6745 O O . HOH N 6 . ? 9.150 18.324 52.280 1.00 21.07 ? 2070 HOH B O 1 HETATM 6746 O O . HOH N 6 . ? 60.011 -5.465 65.471 1.00 22.65 ? 2071 HOH B O 1 HETATM 6747 O O . HOH N 6 . ? 58.734 -5.225 68.119 1.00 27.98 ? 2072 HOH B O 1 HETATM 6748 O O . HOH N 6 . ? 22.656 24.920 49.682 1.00 17.11 ? 2073 HOH B O 1 HETATM 6749 O O . HOH N 6 . ? 30.704 23.180 52.478 1.00 17.75 ? 2074 HOH B O 1 HETATM 6750 O O . HOH N 6 . ? 40.010 25.579 47.329 1.00 32.69 ? 2075 HOH B O 1 HETATM 6751 O O . HOH N 6 . ? 38.409 27.430 53.905 1.00 36.39 ? 2076 HOH B O 1 HETATM 6752 O O . HOH N 6 . ? 35.673 23.398 52.708 1.00 18.52 ? 2077 HOH B O 1 HETATM 6753 O O . HOH N 6 . ? 32.446 22.044 54.364 1.00 21.37 ? 2078 HOH B O 1 HETATM 6754 O O . HOH N 6 . ? 42.889 20.824 48.868 1.00 16.16 ? 2079 HOH B O 1 HETATM 6755 O O . HOH N 6 . ? 46.258 17.119 53.282 1.00 11.70 ? 2080 HOH B O 1 HETATM 6756 O O . HOH N 6 . ? 49.597 18.207 49.285 1.00 16.90 ? 2081 HOH B O 1 HETATM 6757 O O . HOH N 6 . ? 49.171 19.982 52.610 1.00 18.70 ? 2082 HOH B O 1 HETATM 6758 O O . HOH N 6 . ? 45.244 20.920 47.524 1.00 16.10 ? 2083 HOH B O 1 HETATM 6759 O O . HOH N 6 . ? 57.589 21.801 47.370 1.00 38.32 ? 2084 HOH B O 1 HETATM 6760 O O . HOH N 6 . ? 48.193 18.554 40.792 1.00 21.38 ? 2085 HOH B O 1 HETATM 6761 O O . HOH N 6 . ? 62.312 -12.417 52.540 1.00 20.66 ? 2086 HOH B O 1 HETATM 6762 O O . HOH N 6 . ? 54.648 16.809 41.796 1.00 20.54 ? 2087 HOH B O 1 HETATM 6763 O O . HOH N 6 . ? 55.169 15.307 44.000 1.00 24.11 ? 2088 HOH B O 1 HETATM 6764 O O . HOH N 6 . ? 44.731 20.594 55.805 1.00 19.16 ? 2089 HOH B O 1 HETATM 6765 O O . HOH N 6 . ? 46.944 14.384 60.617 1.00 20.74 ? 2090 HOH B O 1 HETATM 6766 O O . HOH N 6 . ? 43.737 18.781 66.930 1.00 24.99 ? 2091 HOH B O 1 HETATM 6767 O O . HOH N 6 . ? 44.160 -19.871 38.375 1.00 26.04 ? 2092 HOH B O 1 HETATM 6768 O O . HOH N 6 . ? 36.434 20.223 66.782 1.00 20.13 ? 2093 HOH B O 1 HETATM 6769 O O . HOH N 6 . ? 35.610 14.769 63.638 1.00 24.15 ? 2094 HOH B O 1 HETATM 6770 O O . HOH N 6 . ? 36.273 10.182 62.151 1.00 17.57 ? 2095 HOH B O 1 HETATM 6771 O O . HOH N 6 . ? 35.133 10.362 57.711 1.00 13.39 ? 2096 HOH B O 1 HETATM 6772 O O . HOH N 6 . ? 35.978 13.149 55.504 1.00 11.42 ? 2097 HOH B O 1 HETATM 6773 O O . HOH N 6 . ? 35.158 8.508 55.708 1.00 12.74 ? 2098 HOH B O 1 HETATM 6774 O O . HOH N 6 . ? 35.929 6.544 59.155 1.00 17.40 ? 2099 HOH B O 1 HETATM 6775 O O . HOH N 6 . ? 38.575 6.350 60.917 1.00 11.40 ? 2100 HOH B O 1 HETATM 6776 O O . HOH N 6 . ? 57.572 -23.257 53.056 1.00 18.92 ? 2101 HOH B O 1 HETATM 6777 O O . HOH N 6 . ? 32.732 7.136 55.276 1.00 13.10 ? 2102 HOH B O 1 HETATM 6778 O O . HOH N 6 . ? 30.253 5.484 53.259 1.00 11.21 ? 2103 HOH B O 1 HETATM 6779 O O . HOH N 6 . ? 37.124 8.429 31.474 1.00 34.99 ? 2104 HOH B O 1 HETATM 6780 O O . HOH N 6 . ? 35.238 11.007 30.081 1.00 26.36 ? 2105 HOH B O 1 HETATM 6781 O O . HOH N 6 . ? 37.212 19.502 33.971 1.00 31.92 ? 2106 HOH B O 1 HETATM 6782 O O . HOH N 6 . ? 32.280 13.025 31.556 1.00 20.93 ? 2107 HOH B O 1 HETATM 6783 O O . HOH N 6 . ? 28.350 12.007 36.517 1.00 18.07 ? 2108 HOH B O 1 HETATM 6784 O O . HOH N 6 . ? 27.953 12.107 33.762 1.00 18.44 ? 2109 HOH B O 1 HETATM 6785 O O . HOH N 6 . ? 29.970 11.643 31.936 1.00 20.80 ? 2110 HOH B O 1 HETATM 6786 O O . HOH N 6 . ? 39.101 5.965 39.863 1.00 10.28 ? 2111 HOH B O 1 HETATM 6787 O O . HOH N 6 . ? 40.863 11.173 32.312 1.00 21.79 ? 2112 HOH B O 1 HETATM 6788 O O . HOH N 6 . ? 39.844 3.871 31.179 1.00 29.82 ? 2113 HOH B O 1 HETATM 6789 O O . HOH N 6 . ? 42.633 4.207 33.418 1.00 18.69 ? 2114 HOH B O 1 HETATM 6790 O O . HOH N 6 . ? 38.446 6.309 32.582 1.00 19.73 ? 2115 HOH B O 1 HETATM 6791 O O . HOH N 6 . ? 40.888 -2.920 37.292 1.00 11.68 ? 2116 HOH B O 1 HETATM 6792 O O . HOH N 6 . ? 40.024 2.145 73.192 1.00 33.37 ? 2117 HOH B O 1 HETATM 6793 O O . HOH N 6 . ? 44.339 -1.126 31.021 1.00 38.13 ? 2118 HOH B O 1 HETATM 6794 O O . HOH N 6 . ? 43.355 1.004 32.981 1.00 17.48 ? 2119 HOH B O 1 HETATM 6795 O O . HOH N 6 . ? 42.306 -5.628 31.893 1.00 19.92 ? 2120 HOH B O 1 HETATM 6796 O O . HOH N 6 . ? 51.144 -5.515 30.397 1.00 15.27 ? 2121 HOH B O 1 HETATM 6797 O O . HOH N 6 . ? 58.180 9.888 45.325 1.00 24.02 ? 2122 HOH B O 1 HETATM 6798 O O . HOH N 6 . ? 58.995 7.662 41.422 1.00 26.99 ? 2123 HOH B O 1 HETATM 6799 O O . HOH N 6 . ? 47.746 17.307 69.217 1.00 20.33 ? 2124 HOH B O 1 HETATM 6800 O O . HOH N 6 . ? 54.257 11.676 56.258 1.00 20.19 ? 2125 HOH B O 1 HETATM 6801 O O . HOH N 6 . ? 54.271 6.612 63.183 1.00 14.03 ? 2126 HOH B O 1 HETATM 6802 O O . HOH N 6 . ? 57.490 9.050 62.484 1.00 27.17 ? 2127 HOH B O 1 HETATM 6803 O O . HOH N 6 . ? 58.029 11.844 58.842 1.00 27.49 ? 2128 HOH B O 1 HETATM 6804 O O . HOH N 6 . ? 57.672 11.035 36.951 1.00 25.91 ? 2129 HOH B O 1 HETATM 6805 O O . HOH N 6 . ? 57.745 8.108 35.703 1.00 33.78 ? 2130 HOH B O 1 HETATM 6806 O O . HOH N 6 . ? 49.896 3.286 67.753 1.00 12.60 ? 2131 HOH B O 1 HETATM 6807 O O . HOH N 6 . ? 42.833 1.515 65.092 1.00 10.84 ? 2132 HOH B O 1 HETATM 6808 O O . HOH N 6 . ? 29.615 -3.821 36.611 1.00 23.49 ? 2133 HOH B O 1 HETATM 6809 O O . HOH N 6 . ? 31.459 -0.038 36.958 1.00 15.81 ? 2134 HOH B O 1 HETATM 6810 O O . HOH N 6 . ? 21.293 6.739 40.869 1.00 14.78 ? 2135 HOH B O 1 HETATM 6811 O O . HOH N 6 . ? 23.259 5.852 36.151 1.00 26.47 ? 2136 HOH B O 1 HETATM 6812 O O . HOH N 6 . ? 17.290 8.663 35.593 1.00 25.62 ? 2137 HOH B O 1 HETATM 6813 O O . HOH N 6 . ? 16.888 8.666 39.889 1.00 18.37 ? 2138 HOH B O 1 HETATM 6814 O O . HOH N 6 . ? 7.830 11.295 43.278 1.00 28.03 ? 2139 HOH B O 1 HETATM 6815 O O . HOH N 6 . ? 28.473 14.406 37.833 1.00 21.13 ? 2140 HOH B O 1 HETATM 6816 O O . HOH N 6 . ? 25.971 21.351 41.308 1.00 26.44 ? 2141 HOH B O 1 HETATM 6817 O O . HOH N 6 . ? 29.312 7.605 47.756 1.00 10.19 ? 2142 HOH B O 1 HETATM 6818 O O . HOH N 6 . ? 28.264 2.795 42.101 1.00 11.52 ? 2143 HOH B O 1 HETATM 6819 O O . HOH N 6 . ? 26.578 4.167 47.044 1.00 11.08 ? 2144 HOH B O 1 HETATM 6820 O O . HOH N 6 . ? 29.925 -1.285 51.808 1.00 10.52 ? 2145 HOH B O 1 HETATM 6821 O O . HOH N 6 . ? 31.387 -6.463 57.309 1.00 23.52 ? 2146 HOH B O 1 HETATM 6822 O O . HOH N 6 . ? 25.550 -4.728 56.319 1.00 19.96 ? 2147 HOH B O 1 HETATM 6823 O O . HOH N 6 . ? 26.042 -1.713 57.940 1.00 19.00 ? 2148 HOH B O 1 HETATM 6824 O O . HOH N 6 . ? 27.746 2.821 50.402 1.00 10.51 ? 2149 HOH B O 1 HETATM 6825 O O . HOH N 6 . ? 26.783 5.866 49.249 1.00 10.43 ? 2150 HOH B O 1 HETATM 6826 O O . HOH N 6 . ? 19.928 3.007 45.582 1.00 20.75 ? 2151 HOH B O 1 HETATM 6827 O O . HOH N 6 . ? 20.985 2.076 42.514 1.00 26.04 ? 2152 HOH B O 1 HETATM 6828 O O . HOH N 6 . ? 25.721 0.843 40.166 1.00 20.56 ? 2153 HOH B O 1 HETATM 6829 O O . HOH N 6 . ? 18.675 11.558 45.833 1.00 13.23 ? 2154 HOH B O 1 HETATM 6830 O O . HOH N 6 . ? 25.957 7.378 46.973 1.00 11.04 ? 2155 HOH B O 1 HETATM 6831 O O . HOH N 6 . ? 15.925 2.667 47.859 1.00 27.10 ? 2156 HOH B O 1 HETATM 6832 O O . HOH N 6 . ? 16.783 9.987 47.101 1.00 15.49 ? 2157 HOH B O 1 HETATM 6833 O O . HOH N 6 . ? 16.666 0.744 49.622 1.00 20.14 ? 2158 HOH B O 1 HETATM 6834 O O . HOH N 6 . ? 12.579 3.628 55.514 1.00 22.05 ? 2159 HOH B O 1 HETATM 6835 O O . HOH N 6 . ? 19.156 -1.939 57.539 1.00 27.89 ? 2160 HOH B O 1 HETATM 6836 O O . HOH N 6 . ? 41.559 -6.684 53.391 1.00 13.82 ? 2161 HOH B O 1 HETATM 6837 O O . HOH N 6 . ? 53.841 2.192 65.654 1.00 12.93 ? 2162 HOH B O 1 HETATM 6838 O O . HOH N 6 . ? 57.557 -2.859 68.555 1.00 25.83 ? 2163 HOH B O 1 HETATM 6839 O O . HOH N 6 . ? 59.493 -2.967 64.673 1.00 17.67 ? 2164 HOH B O 1 HETATM 6840 O O . HOH N 6 . ? 57.115 -4.310 61.047 1.00 10.26 ? 2165 HOH B O 1 HETATM 6841 O O . HOH N 6 . ? 58.230 -2.130 62.456 1.00 12.09 ? 2166 HOH B O 1 HETATM 6842 O O . HOH N 6 . ? 53.565 -7.737 53.369 1.00 10.39 ? 2167 HOH B O 1 HETATM 6843 O O . HOH N 6 . ? 50.054 -3.289 50.924 1.00 10.23 ? 2168 HOH B O 1 HETATM 6844 O O . HOH N 6 . ? 31.508 -10.621 40.461 1.00 24.94 ? 2169 HOH B O 1 HETATM 6845 O O . HOH N 6 . ? 33.954 -12.715 41.578 1.00 24.40 ? 2170 HOH B O 1 HETATM 6846 O O . HOH N 6 . ? 24.845 -6.834 40.715 1.00 17.04 ? 2171 HOH B O 1 HETATM 6847 O O . HOH N 6 . ? 29.322 -13.357 33.025 1.00 23.79 ? 2172 HOH B O 1 HETATM 6848 O O . HOH N 6 . ? 27.334 -13.436 35.018 1.00 20.63 ? 2173 HOH B O 1 HETATM 6849 O O . HOH N 6 . ? 26.258 -10.318 33.076 1.00 16.92 ? 2174 HOH B O 1 HETATM 6850 O O . HOH N 6 . ? 30.703 -6.269 42.423 1.00 16.52 ? 2175 HOH B O 1 HETATM 6851 O O . HOH N 6 . ? 23.128 -4.815 41.017 1.00 21.51 ? 2176 HOH B O 1 HETATM 6852 O O . HOH N 6 . ? 28.502 -0.469 39.993 1.00 19.78 ? 2177 HOH B O 1 HETATM 6853 O O . HOH N 6 . ? 19.481 -5.588 44.707 1.00 26.17 ? 2178 HOH B O 1 HETATM 6854 O O . HOH N 6 . ? 18.612 -7.450 47.553 1.00 29.41 ? 2179 HOH B O 1 HETATM 6855 O O . HOH N 6 . ? 21.267 -4.329 43.195 1.00 18.86 ? 2180 HOH B O 1 HETATM 6856 O O . HOH N 6 . ? 22.235 -8.079 57.104 1.00 26.25 ? 2181 HOH B O 1 HETATM 6857 O O . HOH N 6 . ? 18.426 -6.029 54.949 1.00 21.18 ? 2182 HOH B O 1 HETATM 6858 O O . HOH N 6 . ? 28.194 -10.460 52.033 1.00 13.64 ? 2183 HOH B O 1 HETATM 6859 O O . HOH N 6 . ? 27.857 -11.636 59.251 1.00 25.18 ? 2184 HOH B O 1 HETATM 6860 O O . HOH N 6 . ? 32.184 -13.111 53.570 1.00 11.96 ? 2185 HOH B O 1 HETATM 6861 O O . HOH N 6 . ? 26.603 -21.031 56.870 1.00 24.93 ? 2186 HOH B O 1 HETATM 6862 O O . HOH N 6 . ? 26.794 -14.238 60.129 1.00 27.78 ? 2187 HOH B O 1 HETATM 6863 O O . HOH N 6 . ? 35.054 -13.757 53.931 1.00 11.09 ? 2188 HOH B O 1 HETATM 6864 O O . HOH N 6 . ? 37.912 -15.329 52.127 1.00 13.09 ? 2189 HOH B O 1 HETATM 6865 O O . HOH N 6 . ? 29.783 -8.259 52.943 1.00 11.56 ? 2190 HOH B O 1 HETATM 6866 O O . HOH N 6 . ? 39.157 -16.223 55.763 1.00 29.20 ? 2191 HOH B O 1 HETATM 6867 O O . HOH N 6 . ? 48.986 -13.524 54.379 1.00 12.71 ? 2192 HOH B O 1 HETATM 6868 O O . HOH N 6 . ? 45.764 -15.586 53.647 1.00 15.24 ? 2193 HOH B O 1 HETATM 6869 O O . HOH N 6 . ? 53.637 -6.656 56.972 1.00 10.42 ? 2194 HOH B O 1 HETATM 6870 O O . HOH N 6 . ? 59.241 -7.455 63.796 1.00 18.90 ? 2195 HOH B O 1 HETATM 6871 O O . HOH N 6 . ? 49.466 -17.849 56.270 1.00 14.09 ? 2196 HOH B O 1 HETATM 6872 O O . HOH N 6 . ? 48.988 -16.546 59.761 1.00 19.35 ? 2197 HOH B O 1 HETATM 6873 O O . HOH N 6 . ? 46.730 -15.649 58.226 1.00 16.74 ? 2198 HOH B O 1 HETATM 6874 O O . HOH N 6 . ? 59.873 -16.424 61.965 1.00 19.06 ? 2199 HOH B O 1 HETATM 6875 O O . HOH N 6 . ? 60.683 -14.639 60.011 1.00 19.81 ? 2200 HOH B O 1 HETATM 6876 O O . HOH N 6 . ? 66.829 -10.546 59.364 1.00 31.11 ? 2201 HOH B O 1 HETATM 6877 O O . HOH N 6 . ? 62.825 -10.734 54.677 1.00 19.65 ? 2202 HOH B O 1 HETATM 6878 O O . HOH N 6 . ? 58.352 -7.392 58.764 1.00 12.92 ? 2203 HOH B O 1 HETATM 6879 O O . HOH N 6 . ? 61.436 -1.096 64.791 1.00 27.86 ? 2204 HOH B O 1 HETATM 6880 O O . HOH N 6 . ? 60.279 3.473 65.428 1.00 30.08 ? 2205 HOH B O 1 HETATM 6881 O O . HOH N 6 . ? 55.273 4.313 64.586 1.00 14.26 ? 2206 HOH B O 1 HETATM 6882 O O . HOH N 6 . ? 67.553 1.283 61.883 1.00 30.32 ? 2207 HOH B O 1 HETATM 6883 O O . HOH N 6 . ? 68.625 4.379 56.685 1.00 48.34 ? 2208 HOH B O 1 HETATM 6884 O O . HOH N 6 . ? 63.283 -5.495 64.982 1.00 46.15 ? 2209 HOH B O 1 HETATM 6885 O O . HOH N 6 . ? 66.333 -1.557 54.388 1.00 24.38 ? 2210 HOH B O 1 HETATM 6886 O O . HOH N 6 . ? 66.431 -4.274 51.288 1.00 26.50 ? 2211 HOH B O 1 HETATM 6887 O O . HOH N 6 . ? 65.829 -7.939 56.566 1.00 22.86 ? 2212 HOH B O 1 HETATM 6888 O O . HOH N 6 . ? 67.141 1.587 54.969 1.00 28.90 ? 2213 HOH B O 1 HETATM 6889 O O . HOH N 6 . ? 57.629 5.301 54.736 1.00 12.33 ? 2214 HOH B O 1 HETATM 6890 O O . HOH N 6 . ? 61.218 8.709 59.471 1.00 23.23 ? 2215 HOH B O 1 HETATM 6891 O O . HOH N 6 . ? 63.648 6.553 50.320 1.00 25.05 ? 2216 HOH B O 1 HETATM 6892 O O . HOH N 6 . ? 60.968 5.312 46.164 1.00 26.43 ? 2217 HOH B O 1 HETATM 6893 O O . HOH N 6 . ? 51.018 -0.856 43.774 1.00 10.48 ? 2218 HOH B O 1 HETATM 6894 O O . HOH N 6 . ? 56.130 -10.250 36.329 1.00 24.49 ? 2219 HOH B O 1 HETATM 6895 O O . HOH N 6 . ? 49.674 -10.829 32.347 1.00 22.98 ? 2220 HOH B O 1 HETATM 6896 O O . HOH N 6 . ? 42.339 -17.972 37.505 1.00 23.96 ? 2221 HOH B O 1 HETATM 6897 O O . HOH N 6 . ? 40.018 -13.018 35.364 1.00 12.48 ? 2222 HOH B O 1 HETATM 6898 O O . HOH N 6 . ? 44.881 -18.401 40.713 1.00 15.46 ? 2223 HOH B O 1 HETATM 6899 O O . HOH N 6 . ? 54.013 -7.204 50.620 1.00 12.10 ? 2224 HOH B O 1 HETATM 6900 O O . HOH N 6 . ? 60.746 -7.439 39.831 1.00 40.39 ? 2225 HOH B O 1 HETATM 6901 O O . HOH N 6 . ? 65.411 -8.342 46.370 1.00 22.16 ? 2226 HOH B O 1 HETATM 6902 O O . HOH N 6 . ? 63.552 -9.125 49.281 1.00 19.41 ? 2227 HOH B O 1 HETATM 6903 O O . HOH N 6 . ? 59.337 -10.562 43.552 1.00 13.53 ? 2228 HOH B O 1 HETATM 6904 O O . HOH N 6 . ? 55.006 -9.089 48.602 1.00 11.51 ? 2229 HOH B O 1 HETATM 6905 O O . HOH N 6 . ? 60.218 -12.868 44.764 1.00 15.42 ? 2230 HOH B O 1 HETATM 6906 O O . HOH N 6 . ? 62.725 -13.100 48.203 1.00 21.82 ? 2231 HOH B O 1 HETATM 6907 O O . HOH N 6 . ? 60.727 -16.942 53.124 1.00 19.25 ? 2232 HOH B O 1 HETATM 6908 O O . HOH N 6 . ? 62.947 -15.773 43.057 1.00 27.79 ? 2233 HOH B O 1 HETATM 6909 O O . HOH N 6 . ? 59.703 -21.000 53.093 1.00 24.80 ? 2234 HOH B O 1 HETATM 6910 O O . HOH N 6 . ? 48.192 -19.886 57.478 1.00 19.02 ? 2235 HOH B O 1 HETATM 6911 O O . HOH N 6 . ? 51.512 -23.211 60.356 1.00 23.41 ? 2236 HOH B O 1 HETATM 6912 O O . HOH N 6 . ? 55.264 -21.677 53.066 1.00 13.36 ? 2237 HOH B O 1 HETATM 6913 O O . HOH N 6 . ? 56.469 -17.593 41.576 1.00 27.80 ? 2238 HOH B O 1 HETATM 6914 O O . HOH N 6 . ? 53.686 -11.003 45.863 1.00 14.57 ? 2239 HOH B O 1 HETATM 6915 O O . HOH N 6 . ? 50.532 -20.816 45.969 1.00 21.28 ? 2240 HOH B O 1 HETATM 6916 O O . HOH N 6 . ? 40.494 -18.622 39.544 1.00 14.22 ? 2241 HOH B O 1 HETATM 6917 O O . HOH N 6 . ? 46.765 -21.641 42.087 1.00 19.53 ? 2242 HOH B O 1 HETATM 6918 O O . HOH N 6 . ? 45.714 -25.094 48.228 1.00 19.84 ? 2243 HOH B O 1 HETATM 6919 O O . HOH N 6 . ? 39.773 -22.275 52.108 1.00 24.40 ? 2244 HOH B O 1 HETATM 6920 O O . HOH N 6 . ? 47.222 -22.252 56.430 1.00 23.10 ? 2245 HOH B O 1 HETATM 6921 O O . HOH N 6 . ? 36.726 -17.947 56.197 1.00 21.64 ? 2246 HOH B O 1 HETATM 6922 O O . HOH N 6 . ? 36.160 -16.396 53.988 1.00 13.01 ? 2247 HOH B O 1 HETATM 6923 O O . HOH N 6 . ? 31.126 -15.782 41.610 1.00 35.69 ? 2248 HOH B O 1 HETATM 6924 O O . HOH N 6 . ? 38.074 -21.391 34.706 1.00 22.22 ? 2249 HOH B O 1 HETATM 6925 O O . HOH N 6 . ? 33.526 -10.734 39.003 1.00 17.65 ? 2250 HOH B O 1 HETATM 6926 O O . HOH N 6 . ? 35.361 -9.172 32.769 1.00 15.56 ? 2251 HOH B O 1 HETATM 6927 O O . HOH N 6 . ? 32.435 -12.301 36.837 1.00 25.44 ? 2252 HOH B O 1 HETATM 6928 O O . HOH N 6 . ? 31.353 -14.083 34.545 1.00 33.84 ? 2253 HOH B O 1 HETATM 6929 O O . HOH N 6 . ? 41.521 -8.305 30.741 1.00 29.28 ? 2254 HOH B O 1 HETATM 6930 O O . HOH N 6 . ? 39.476 -11.107 33.434 1.00 14.68 ? 2255 HOH B O 1 HETATM 6931 O O . HOH N 6 . ? 33.989 0.200 33.536 1.00 25.61 ? 2256 HOH B O 1 HETATM 6932 O O . HOH N 6 . ? 34.208 -2.904 30.730 1.00 30.09 ? 2257 HOH B O 1 HETATM 6933 O O . HOH N 6 . ? 32.811 -2.251 36.205 1.00 12.87 ? 2258 HOH B O 1 HETATM 6934 O O . HOH N 6 . ? 36.960 8.815 64.463 1.00 27.80 ? 2259 HOH B O 1 HETATM 6935 O O . HOH N 6 . ? 36.434 4.612 60.352 1.00 24.53 ? 2260 HOH B O 1 HETATM 6936 O O . HOH N 6 . ? 39.208 -3.029 61.487 1.00 22.23 ? 2261 HOH B O 1 HETATM 6937 O O . HOH N 6 . ? 35.918 -2.938 64.881 1.00 30.30 ? 2262 HOH B O 1 HETATM 6938 O O . HOH N 6 . ? 40.599 4.333 71.757 1.00 17.71 ? 2263 HOH B O 1 HETATM 6939 O O . HOH N 6 . ? 36.713 3.623 64.258 1.00 20.65 ? 2264 HOH B O 1 HETATM 6940 O O . HOH N 6 . ? 40.406 -6.720 66.768 1.00 26.16 ? 2265 HOH B O 1 HETATM 6941 O O . HOH N 6 . ? 42.265 -1.428 73.471 1.00 19.50 ? 2266 HOH B O 1 HETATM 6942 O O . HOH N 6 . ? 39.993 0.995 70.982 1.00 17.87 ? 2267 HOH B O 1 HETATM 6943 O O . HOH N 6 . ? 43.502 -10.103 66.799 1.00 25.46 ? 2268 HOH B O 1 HETATM 6944 O O . HOH N 6 . ? 44.997 -4.076 70.294 1.00 13.19 ? 2269 HOH B O 1 HETATM 6945 O O . HOH N 6 . ? 40.915 -7.234 64.170 1.00 24.01 ? 2270 HOH B O 1 HETATM 6946 O O . HOH N 6 . ? 47.109 -8.743 57.658 1.00 11.27 ? 2271 HOH B O 1 HETATM 6947 O O . HOH N 6 . ? 46.842 -2.874 66.241 1.00 15.06 ? 2272 HOH B O 1 HETATM 6948 O O . HOH N 6 . ? 45.345 -10.219 64.740 1.00 18.05 ? 2273 HOH B O 1 HETATM 6949 O O . HOH N 6 . ? 46.680 -10.974 71.250 1.00 25.97 ? 2274 HOH B O 1 HETATM 6950 O O . HOH N 6 . ? 53.456 -13.128 63.042 1.00 23.21 ? 2275 HOH B O 1 HETATM 6951 O O . HOH N 6 . ? 49.842 -15.583 66.287 1.00 21.64 ? 2276 HOH B O 1 HETATM 6952 O O . HOH N 6 . ? 46.486 -12.652 65.411 1.00 21.71 ? 2277 HOH B O 1 HETATM 6953 O O . HOH N 6 . ? 51.968 -8.511 67.809 1.00 15.15 ? 2278 HOH B O 1 HETATM 6954 O O . HOH N 6 . ? 47.050 -3.143 68.809 1.00 12.47 ? 2279 HOH B O 1 HETATM 6955 O O . HOH N 6 . ? 50.663 -7.957 72.739 1.00 20.95 ? 2280 HOH B O 1 HETATM 6956 O O . HOH N 6 . ? 45.818 1.460 74.644 1.00 21.34 ? 2281 HOH B O 1 HETATM 6957 O O . HOH N 6 . ? 55.902 -0.432 68.869 1.00 23.18 ? 2282 HOH B O 1 HETATM 6958 O O . HOH N 6 . ? 55.204 -3.135 69.515 1.00 31.76 ? 2283 HOH B O 1 HETATM 6959 O O . HOH N 6 . ? 52.607 2.580 68.067 1.00 14.31 ? 2284 HOH B O 1 HETATM 6960 O O . HOH N 6 . ? 45.233 4.666 75.574 1.00 23.65 ? 2285 HOH B O 1 HETATM 6961 O O . HOH N 6 . ? 44.662 9.431 74.548 1.00 24.26 ? 2286 HOH B O 1 HETATM 6962 O O . HOH N 6 . ? 51.438 5.900 74.525 1.00 20.98 ? 2287 HOH B O 1 HETATM 6963 O O . HOH N 6 . ? 47.787 4.576 75.791 1.00 27.99 ? 2288 HOH B O 1 HETATM 6964 O O . HOH N 6 . ? 51.084 11.094 75.886 1.00 21.12 ? 2289 HOH B O 1 HETATM 6965 O O . HOH N 6 . ? 55.825 8.932 66.541 1.00 23.44 ? 2290 HOH B O 1 HETATM 6966 O O . HOH N 6 . ? 55.731 12.907 65.198 1.00 40.52 ? 2291 HOH B O 1 HETATM 6967 O O . HOH N 6 . ? 55.126 9.159 63.906 1.00 19.94 ? 2292 HOH B O 1 HETATM 6968 O O . HOH N 6 . ? 46.137 15.360 67.860 1.00 20.87 ? 2293 HOH B O 1 HETATM 6969 O O . HOH N 6 . ? 51.513 15.067 60.758 1.00 24.95 ? 2294 HOH B O 1 HETATM 6970 O O . HOH N 6 . ? 48.959 16.369 59.472 1.00 19.92 ? 2295 HOH B O 1 HETATM 6971 O O . HOH N 6 . ? 53.235 9.088 56.630 1.00 11.98 ? 2296 HOH B O 1 HETATM 6972 O O . HOH N 6 . ? 52.726 15.490 51.721 1.00 17.92 ? 2297 HOH B O 1 HETATM 6973 O O . HOH N 6 . ? 52.158 12.194 54.663 1.00 14.82 ? 2298 HOH B O 1 HETATM 6974 O O . HOH N 6 . ? 54.755 10.046 48.803 1.00 13.32 ? 2299 HOH B O 1 HETATM 6975 O O . HOH N 6 . ? 56.771 13.139 39.009 1.00 19.84 ? 2300 HOH B O 1 HETATM 6976 O O . HOH N 6 . ? 57.295 8.059 38.610 1.00 29.55 ? 2301 HOH B O 1 HETATM 6977 O O . HOH N 6 . ? 47.732 2.672 31.477 1.00 18.47 ? 2302 HOH B O 1 HETATM 6978 O O . HOH N 6 . ? 54.791 -4.260 26.856 1.00 23.69 ? 2303 HOH B O 1 HETATM 6979 O O . HOH N 6 . ? 55.224 -0.771 24.769 1.00 19.55 ? 2304 HOH B O 1 HETATM 6980 O O . HOH N 6 . ? 36.120 -2.104 56.433 1.00 14.85 ? 2305 HOH B O 1 HETATM 6981 O O . HOH N 6 . ? 37.246 6.945 56.697 1.00 10.97 ? 2306 HOH B O 1 HETATM 6982 O O . HOH N 6 . ? 34.058 5.665 57.174 1.00 16.15 ? 2307 HOH B O 1 HETATM 6983 O O . HOH N 6 . ? 33.368 1.977 54.014 1.00 12.45 ? 2308 HOH B O 1 HETATM 6984 O O . HOH N 6 . ? 35.634 -3.971 58.235 1.00 24.93 ? 2309 HOH B O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . PCA A 1 ? 0.1547 0.1280 0.1514 0.0028 -0.0098 -0.0081 1 PCA A N 2 C CA . PCA A 1 ? 0.1293 0.1280 0.1356 0.0022 0.0061 -0.0008 1 PCA A CA 3 C CB . PCA A 1 ? 0.1383 0.1298 0.1296 -0.0008 0.0086 -0.0100 1 PCA A CB 4 C CG . PCA A 1 ? 0.1322 0.1242 0.1351 -0.0013 0.0090 0.0009 1 PCA A CG 5 C CD . PCA A 1 ? 0.1482 0.1274 0.1428 -0.0034 0.0038 -0.0008 1 PCA A CD 6 O OE . PCA A 1 ? 0.1717 0.1388 0.1655 0.0155 -0.0066 -0.0157 1 PCA A OE 7 C C . PCA A 1 ? 0.1306 0.1332 0.1324 -0.0013 0.0072 0.0006 1 PCA A C 8 O O . PCA A 1 ? 0.1486 0.1458 0.1583 0.0018 0.0142 -0.0028 1 PCA A O 9 N N . LYS A 2 ? 0.1214 0.1354 0.1233 0.0020 0.0152 0.0018 2 LYS A N 10 C CA . LYS A 2 ? 0.1324 0.1375 0.1307 0.0042 0.0061 0.0009 2 LYS A CA 11 C C . LYS A 2 ? 0.1244 0.1271 0.1126 0.0056 0.0065 0.0045 2 LYS A C 12 O O . LYS A 2 ? 0.1159 0.1281 0.1274 0.0014 -0.0082 0.0017 2 LYS A O 13 C CB . LYS A 2 ? 0.1495 0.1486 0.1514 0.0053 0.0056 0.0004 2 LYS A CB 14 C CG . LYS A 2 ? 0.1717 0.1731 0.1753 0.0021 0.0084 0.0171 2 LYS A CG 15 C CD . LYS A 2 ? 0.2025 0.1839 0.2213 0.0201 0.0054 0.0077 2 LYS A CD 16 C CE . LYS A 2 ? 0.2517 0.2513 0.2845 0.0157 0.0021 0.0220 2 LYS A CE 17 N NZ . LYS A 2 ? 0.2496 0.2761 0.3434 0.0232 -0.0002 0.0030 2 LYS A NZ 18 N N . PRO A 3 ? 0.1181 0.1290 0.1152 0.0034 0.0000 0.0017 3 PRO A N 19 C CA . PRO A 3 ? 0.1202 0.1303 0.1234 0.0017 -0.0015 0.0025 3 PRO A CA 20 C C . PRO A 3 ? 0.1372 0.1372 0.1315 0.0027 -0.0068 0.0006 3 PRO A C 21 O O . PRO A 3 ? 0.1346 0.1467 0.1509 0.0001 -0.0145 -0.0103 3 PRO A O 22 C CB . PRO A 3 ? 0.1179 0.1276 0.1261 -0.0001 -0.0005 0.0015 3 PRO A CB 23 C CG . PRO A 3 ? 0.1254 0.1370 0.1227 0.0046 0.0024 0.0050 3 PRO A CG 24 C CD . PRO A 3 ? 0.1218 0.1268 0.1164 0.0064 0.0013 0.0070 3 PRO A CD 25 N N . GLY A 4 ? 0.1209 0.1275 0.1322 0.0003 -0.0017 -0.0015 4 GLY A N 26 C CA . GLY A 4 ? 0.1244 0.1313 0.1347 -0.0001 0.0024 0.0001 4 GLY A CA 27 C C . GLY A 4 ? 0.1344 0.1342 0.1347 0.0015 -0.0043 0.0026 4 GLY A C 28 O O . GLY A 4 ? 0.1413 0.1348 0.1470 0.0010 -0.0003 -0.0074 4 GLY A O 29 N N . GLU A 5 ? 0.1258 0.1362 0.1367 0.0001 0.0036 0.0061 5 GLU A N 30 C CA . GLU A 5 ? 0.1425 0.1350 0.1496 -0.0001 -0.0039 0.0079 5 GLU A CA 31 C C . GLU A 5 ? 0.1421 0.1513 0.1588 0.0015 0.0081 0.0173 5 GLU A C 32 O O . GLU A 5 ? 0.1657 0.1739 0.2067 -0.0070 -0.0009 0.0458 5 GLU A O 33 C CB . GLU A 5 ? 0.1465 0.1188 0.1612 -0.0008 -0.0052 0.0015 5 GLU A CB 34 C CG . GLU A 5 ? 0.1487 0.1312 0.1591 0.0062 -0.0074 -0.0127 5 GLU A CG 35 C CD . GLU A 5 ? 0.1366 0.1414 0.1779 0.0198 -0.0093 0.0000 5 GLU A CD 36 O OE1 . GLU A 5 ? 0.1908 0.1707 0.2122 -0.0040 -0.0197 0.0267 5 GLU A OE1 37 O OE2 . GLU A 5 ? 0.1573 0.1734 0.1558 0.0197 -0.0236 -0.0080 5 GLU A OE2 38 N N . THR A 6 ? 0.1364 0.1329 0.1618 0.0043 0.0012 0.0084 6 THR A N 39 C CA . THR A 6 ? 0.1447 0.1485 0.1611 -0.0001 -0.0039 0.0021 6 THR A CA 40 C C . THR A 6 ? 0.1567 0.1460 0.1663 0.0068 -0.0117 -0.0037 6 THR A C 41 O O . THR A 6 ? 0.1580 0.1280 0.1803 0.0069 -0.0115 -0.0060 6 THR A O 42 C CB . THR A 6 ? 0.1459 0.1604 0.1625 0.0056 -0.0099 -0.0006 6 THR A CB 43 O OG1 . THR A 6 ? 0.1622 0.2087 0.1664 -0.0030 0.0013 0.0023 6 THR A OG1 44 C CG2 . THR A 6 ? 0.1398 0.1443 0.1657 0.0072 -0.0032 -0.0013 6 THR A CG2 45 N N . LYS A 7 ? 0.1543 0.1337 0.1660 0.0072 -0.0005 -0.0029 7 LYS A N 46 C CA . LYS A 7 ? 0.1617 0.1494 0.1627 0.0011 -0.0031 -0.0014 7 LYS A CA 47 C C . LYS A 7 ? 0.1497 0.1471 0.1519 0.0094 -0.0001 -0.0046 7 LYS A C 48 O O . LYS A 7 ? 0.1446 0.1503 0.1724 0.0077 0.0027 -0.0172 7 LYS A O 49 C CB . LYS A 7 ? 0.1663 0.1625 0.1808 0.0004 -0.0004 -0.0005 7 LYS A CB 50 C CG . LYS A 7 ? 0.1993 0.1806 0.1893 0.0087 -0.0104 0.0000 7 LYS A CG 51 C CD . LYS A 7 ? 0.1989 0.1994 0.2233 0.0162 -0.0057 -0.0060 7 LYS A CD 52 C CE . LYS A 7 ? 0.1948 0.2087 0.2042 -0.0082 -0.0083 0.0083 7 LYS A CE 53 N NZ . LYS A 7 ? 0.2152 0.2445 0.1968 0.0067 -0.0182 0.0028 7 LYS A NZ 54 N N . GLU A 8 ? 0.1461 0.1246 0.1462 0.0071 0.0010 -0.0067 8 GLU A N 55 C CA . GLU A 8 ? 0.1351 0.1338 0.1385 0.0068 -0.0050 0.0003 8 GLU A CA 56 C C . GLU A 8 ? 0.1422 0.1326 0.1374 0.0033 -0.0007 -0.0032 8 GLU A C 57 O O . GLU A 8 ? 0.1565 0.1700 0.1426 0.0024 -0.0075 0.0037 8 GLU A O 58 C CB . GLU A 8 ? 0.1447 0.1251 0.1418 0.0149 -0.0055 0.0002 8 GLU A CB 59 C CG . GLU A 8 ? 0.1300 0.1173 0.1246 0.0083 -0.0066 0.0034 8 GLU A CG 60 C CD . GLU A 8 ? 0.1038 0.1258 0.1236 -0.0035 -0.0032 0.0001 8 GLU A CD 61 O OE1 . GLU A 8 ? 0.1459 0.1172 0.1242 0.0087 0.0060 -0.0033 8 GLU A OE1 62 O OE2 . GLU A 8 ? 0.1242 0.1130 0.1488 0.0070 0.0031 -0.0001 8 GLU A OE2 63 N N . VAL A 9 ? 0.1419 0.1248 0.1405 0.0053 -0.0018 0.0011 9 VAL A N 64 C CA . VAL A 9 ? 0.1431 0.1348 0.1405 0.0083 0.0030 -0.0024 9 VAL A CA 65 C C . VAL A 9 ? 0.1245 0.1299 0.1353 0.0047 -0.0066 0.0031 9 VAL A C 66 O O . VAL A 9 ? 0.1316 0.1253 0.1249 0.0021 -0.0138 -0.0008 9 VAL A O 67 C CB . VAL A 9 ? 0.1414 0.1373 0.1650 0.0063 0.0058 -0.0021 9 VAL A CB 68 C CG1 . VAL A 9 ? 0.1893 0.1622 0.1879 -0.0088 0.0120 0.0005 9 VAL A CG1 69 C CG2 . VAL A 9 ? 0.1667 0.1379 0.1671 0.0055 0.0099 0.0144 9 VAL A CG2 70 N N . HIS A 10 ? 0.1091 0.1176 0.1307 0.0061 0.0058 0.0091 10 HIS A N 71 C CA . HIS A 10 ? 0.1160 0.1166 0.1381 0.0027 0.0001 0.0049 10 HIS A CA 72 C C . HIS A 10 ? 0.1205 0.1062 0.1258 -0.0117 0.0014 0.0002 10 HIS A C 73 O O . HIS A 10 ? 0.1406 0.1347 0.1476 -0.0026 0.0120 0.0116 10 HIS A O 74 C CB . HIS A 10 ? 0.1142 0.1121 0.1294 0.0117 0.0017 -0.0001 10 HIS A CB 75 C CG . HIS A 10 ? 0.1082 0.1132 0.1137 0.0025 0.0097 0.0046 10 HIS A CG 76 N ND1 . HIS A 10 ? 0.1205 0.1285 0.1547 0.0099 0.0049 0.0139 10 HIS A ND1 77 C CD2 . HIS A 10 ? 0.1150 0.1140 0.1228 0.0028 0.0085 0.0091 10 HIS A CD2 78 C CE1 . HIS A 10 ? 0.1173 0.1588 0.1350 -0.0108 0.0074 0.0127 10 HIS A CE1 79 N NE2 . HIS A 10 ? 0.1070 0.1138 0.1512 0.0045 -0.0057 -0.0073 10 HIS A NE2 80 N N . PRO A 11 ? 0.1072 0.1130 0.1273 -0.0070 0.0084 0.0036 11 PRO A N 81 C CA . PRO A 11 ? 0.1121 0.1181 0.1342 -0.0110 0.0035 0.0022 11 PRO A CA 82 C C . PRO A 11 ? 0.1134 0.1197 0.1342 -0.0068 0.0086 -0.0010 11 PRO A C 83 O O . PRO A 11 ? 0.1216 0.1117 0.1422 -0.0079 0.0134 -0.0038 11 PRO A O 84 C CB . PRO A 11 ? 0.1184 0.1314 0.1479 -0.0103 0.0006 -0.0006 11 PRO A CB 85 C CG . PRO A 11 ? 0.1311 0.1283 0.1325 -0.0027 -0.0072 0.0060 11 PRO A CG 86 C CD . PRO A 11 ? 0.1145 0.1263 0.1238 0.0006 -0.0014 0.0066 11 PRO A CD 87 N N . GLN A 12 ? 0.1266 0.1185 0.1456 -0.0095 0.0084 0.0047 12 GLN A N 88 C CA . GLN A 12 ? 0.1319 0.1359 0.1516 -0.0022 0.0044 0.0043 12 GLN A CA 89 C C . GLN A 12 ? 0.1140 0.1340 0.1416 -0.0117 0.0028 -0.0006 12 GLN A C 90 O O . GLN A 12 ? 0.1307 0.1533 0.1574 -0.0003 -0.0074 -0.0081 12 GLN A O 91 C CB . GLN A 12 ? 0.1539 0.1385 0.1646 -0.0130 0.0063 0.0019 12 GLN A CB 92 C CG . GLN A 12 ? 0.1647 0.1669 0.1609 0.0025 0.0101 0.0052 12 GLN A CG 93 C CD . GLN A 12 ? 0.1828 0.1819 0.1946 0.0098 0.0089 0.0158 12 GLN A CD 94 O OE1 . GLN A 12 ? 0.2214 0.2004 0.2546 0.0146 0.0384 0.0353 12 GLN A OE1 95 N NE2 . GLN A 12 ? 0.2301 0.2333 0.2320 0.0012 0.0403 0.0153 12 GLN A NE2 96 N N . LEU A 13 ? 0.1117 0.1314 0.1360 -0.0036 -0.0001 -0.0031 13 LEU A N 97 C CA . LEU A 13 ? 0.1150 0.1339 0.1368 -0.0060 0.0000 -0.0006 13 LEU A CA 98 C C . LEU A 13 ? 0.1238 0.1344 0.1362 -0.0050 0.0038 0.0039 13 LEU A C 99 O O . LEU A 13 ? 0.1081 0.1586 0.1330 -0.0078 0.0196 -0.0002 13 LEU A O 100 C CB . LEU A 13 ? 0.1212 0.1391 0.1373 -0.0062 -0.0016 0.0031 13 LEU A CB 101 C CG . LEU A 13 ? 0.1118 0.1373 0.1225 -0.0130 0.0011 0.0085 13 LEU A CG 102 C CD1 . LEU A 13 ? 0.1326 0.1332 0.1309 -0.0221 0.0033 0.0113 13 LEU A CD1 103 C CD2 . LEU A 13 ? 0.1414 0.1368 0.1431 -0.0047 -0.0037 0.0033 13 LEU A CD2 104 N N . THR A 14 ? 0.1264 0.1201 0.1457 -0.0165 0.0012 -0.0054 14 THR A N 105 C CA . THR A 14 ? 0.1156 0.1286 0.1368 -0.0153 0.0107 0.0043 14 THR A CA 106 C C . THR A 14 ? 0.1096 0.1304 0.1318 -0.0069 0.0056 0.0001 14 THR A C 107 O O . THR A 14 ? 0.1281 0.1280 0.1308 -0.0127 0.0106 0.0115 14 THR A O 108 C CB . THR A 14 ? 0.1108 0.1300 0.1356 -0.0190 0.0047 0.0035 14 THR A CB 109 O OG1 . THR A 14 ? 0.1353 0.1528 0.1865 -0.0123 0.0122 0.0148 14 THR A OG1 110 C CG2 . THR A 14 ? 0.1303 0.1387 0.1558 -0.0228 0.0057 -0.0004 14 THR A CG2 111 N N . THR A 15 ? 0.1148 0.1253 0.1270 -0.0104 0.0026 -0.0046 15 THR A N 112 C CA . THR A 15 ? 0.1169 0.1268 0.1230 -0.0085 0.0093 -0.0014 15 THR A CA 113 C C . THR A 15 ? 0.1157 0.1281 0.1359 -0.0048 0.0091 -0.0018 15 THR A C 114 O O . THR A 15 ? 0.1165 0.1295 0.1375 -0.0100 0.0183 0.0030 15 THR A O 115 C CB . THR A 15 ? 0.1163 0.1223 0.1227 -0.0027 0.0088 -0.0106 15 THR A CB 116 O OG1 . THR A 15 ? 0.1291 0.1593 0.1408 -0.0129 0.0047 -0.0120 15 THR A OG1 117 C CG2 . THR A 15 ? 0.1051 0.0951 0.1391 -0.0189 0.0112 -0.0057 15 THR A CG2 118 N N . PHE A 16 ? 0.1143 0.1146 0.1234 -0.0097 0.0134 -0.0012 16 PHE A N 119 C CA . PHE A 16 ? 0.1180 0.1234 0.1218 -0.0075 0.0144 0.0008 16 PHE A CA 120 C C . PHE A 16 ? 0.1244 0.1237 0.1282 -0.0053 0.0114 0.0023 16 PHE A C 121 O O . PHE A 16 ? 0.1259 0.1471 0.1261 -0.0250 0.0115 0.0125 16 PHE A O 122 C CB . PHE A 16 ? 0.1314 0.1364 0.1363 -0.0101 0.0104 0.0066 16 PHE A CB 123 C CG . PHE A 16 ? 0.1154 0.1350 0.1214 -0.0092 0.0120 0.0038 16 PHE A CG 124 C CD1 . PHE A 16 ? 0.1420 0.1496 0.1338 -0.0063 0.0199 -0.0007 16 PHE A CD1 125 C CD2 . PHE A 16 ? 0.1356 0.1321 0.1200 -0.0176 0.0078 0.0038 16 PHE A CD2 126 C CE1 . PHE A 16 ? 0.1157 0.1589 0.1443 -0.0184 0.0221 0.0039 16 PHE A CE1 127 C CE2 . PHE A 16 ? 0.1372 0.1525 0.1152 -0.0149 0.0177 -0.0006 16 PHE A CE2 128 C CZ . PHE A 16 ? 0.1413 0.1414 0.1510 -0.0168 0.0111 0.0016 16 PHE A CZ 129 N N . ARG A 17 ? 0.1306 0.1361 0.1283 0.0006 0.0167 0.0000 17 ARG A N 130 C CA . ARG A 17 ? 0.1374 0.1434 0.1428 -0.0064 0.0122 -0.0062 17 ARG A CA 131 C C . ARG A 17 ? 0.1402 0.1457 0.1395 -0.0043 0.0091 0.0008 17 ARG A C 132 O O . ARG A 17 ? 0.1484 0.1480 0.1447 -0.0046 0.0242 0.0130 17 ARG A O 133 C CB . ARG A 17 ? 0.1506 0.1513 0.1408 0.0051 0.0221 -0.0109 17 ARG A CB 134 C CG . ARG A 17 ? 0.1447 0.1675 0.1598 0.0126 -0.0016 -0.0126 17 ARG A CG 135 C CD . ARG A 17 ? 0.1390 0.1606 0.1609 -0.0040 -0.0035 -0.0254 17 ARG A CD 136 N NE . ARG A 17 ? 0.1278 0.1549 0.1636 -0.0046 0.0099 -0.0250 17 ARG A NE 137 C CZ . ARG A 17 ? 0.1315 0.1701 0.1438 -0.0055 -0.0002 -0.0028 17 ARG A CZ 138 N NH1 . ARG A 17 ? 0.1127 0.1614 0.1429 -0.0021 -0.0022 -0.0145 17 ARG A NH1 139 N NH2 . ARG A 17 ? 0.1230 0.1567 0.1701 -0.0140 0.0078 -0.0112 17 ARG A NH2 140 N N . CYS A 18 ? 0.1264 0.1429 0.1544 -0.0034 0.0184 -0.0018 18 CYS A N 141 C CA . CYS A 18 ? 0.1451 0.1575 0.1634 -0.0062 0.0170 -0.0017 18 CYS A CA 142 C C . CYS A 18 ? 0.1506 0.1652 0.1665 -0.0103 0.0197 -0.0031 18 CYS A C 143 O O . CYS A 18 ? 0.1556 0.1726 0.1548 -0.0203 0.0308 -0.0084 18 CYS A O 144 C CB . CYS A 18 ? 0.1481 0.1575 0.1631 -0.0097 0.0176 -0.0003 18 CYS A CB 145 S SG . CYS A 18 ? 0.1775 0.1637 0.1684 -0.0142 0.0316 -0.0087 18 CYS A SG 146 N N . THR A 19 ? 0.1636 0.1722 0.1558 -0.0057 0.0263 -0.0029 19 THR A N 147 C CA . THR A 19 ? 0.1861 0.1828 0.1834 -0.0082 0.0154 -0.0055 19 THR A CA 148 C C . THR A 19 ? 0.1920 0.2021 0.1866 -0.0065 0.0204 -0.0084 19 THR A C 149 O O . THR A 19 ? 0.1780 0.2085 0.1617 0.0038 0.0413 -0.0153 19 THR A O 150 C CB . THR A 19 ? 0.1872 0.1791 0.1819 -0.0094 0.0208 -0.0005 19 THR A CB 151 O OG1 . THR A 19 ? 0.1890 0.1820 0.1928 -0.0267 0.0172 0.0051 19 THR A OG1 152 C CG2 . THR A 19 ? 0.1884 0.1871 0.1802 -0.0168 0.0042 -0.0058 19 THR A CG2 153 N N . LYS A 20 ? 0.2220 0.2188 0.2176 -0.0014 0.0142 -0.0120 20 LYS A N 154 C CA . LYS A 20 ? 0.2448 0.2499 0.2485 0.0048 0.0175 -0.0068 20 LYS A CA 155 C C . LYS A 20 ? 0.2422 0.2477 0.2473 0.0080 0.0280 -0.0138 20 LYS A C 156 O O . LYS A 20 ? 0.2377 0.2596 0.2550 0.0157 0.0385 -0.0270 20 LYS A O 157 C CB . LYS A 20 ? 0.2550 0.2468 0.2539 0.0106 0.0168 -0.0080 20 LYS A CB 158 C CG . LYS A 20 ? 0.3015 0.2987 0.3083 0.0088 0.0145 0.0036 20 LYS A CG 159 C CD . LYS A 20 ? 0.3162 0.3051 0.3369 0.0074 0.0072 0.0021 20 LYS A CD 160 C CE . LYS A 20 ? 0.3876 0.3591 0.3869 0.0040 0.0033 -0.0022 20 LYS A CE 161 N NZ . LYS A 20 ? 0.3935 0.3572 0.4075 0.0225 0.0067 0.0123 20 LYS A NZ 162 N N . ARG A 21 ? 0.2618 0.2721 0.2626 0.0029 0.0261 -0.0061 21 ARG A N 163 C CA . ARG A 21 ? 0.2686 0.2713 0.2749 -0.0012 0.0231 -0.0008 21 ARG A CA 164 C C . ARG A 21 ? 0.2551 0.2586 0.2674 -0.0029 0.0254 -0.0006 21 ARG A C 165 O O . ARG A 21 ? 0.2386 0.2593 0.2582 0.0004 0.0432 -0.0039 21 ARG A O 166 C CB . ARG A 21 ? 0.2791 0.2870 0.2742 -0.0062 0.0218 -0.0005 21 ARG A CB 167 C CG . ARG A 21 ? 0.3238 0.3320 0.3132 0.0032 0.0187 0.0121 21 ARG A CG 168 C CD . ARG A 21 ? 0.3858 0.3845 0.3506 0.0053 0.0115 -0.0002 21 ARG A CD 169 N NE . ARG A 21 ? 0.4358 0.4381 0.4428 -0.0056 0.0000 -0.0098 21 ARG A NE 170 C CZ . ARG A 21 ? 0.4573 0.4503 0.4409 -0.0104 -0.0068 -0.0198 21 ARG A CZ 171 N NH1 . ARG A 21 ? 0.4887 0.4995 0.4931 0.0055 0.0018 -0.0100 21 ARG A NH1 172 N NH2 . ARG A 21 ? 0.4740 0.4831 0.4874 -0.0101 -0.0017 -0.0161 21 ARG A NH2 173 N N . GLY A 22 ? 0.2256 0.2356 0.2344 -0.0046 0.0309 -0.0024 22 GLY A N 174 C CA . GLY A 22 ? 0.2223 0.2311 0.2289 -0.0066 0.0223 0.0079 22 GLY A CA 175 C C . GLY A 22 ? 0.1954 0.2100 0.2158 -0.0040 0.0240 0.0001 22 GLY A C 176 O O . GLY A 22 ? 0.1895 0.2152 0.2066 -0.0107 0.0409 0.0088 22 GLY A O 177 N N . GLY A 23 ? 0.1797 0.1981 0.1970 -0.0046 0.0238 -0.0054 23 GLY A N 178 C CA . GLY A 23 ? 0.1677 0.1912 0.2003 0.0026 0.0186 -0.0006 23 GLY A CA 179 C C . GLY A 23 ? 0.1542 0.1888 0.1844 -0.0014 0.0169 0.0010 23 GLY A C 180 O O . GLY A 23 ? 0.1486 0.1854 0.1916 -0.0023 0.0324 -0.0007 23 GLY A O 181 N N . CYS A 24 ? 0.1360 0.1630 0.1888 0.0009 0.0268 0.0017 24 CYS A N 182 C CA . CYS A 24 ? 0.1526 0.1666 0.1874 0.0005 0.0188 0.0007 24 CYS A CA 183 C C . CYS A 24 ? 0.1628 0.1717 0.1858 -0.0096 0.0175 0.0055 24 CYS A C 184 O O . CYS A 24 ? 0.1651 0.1859 0.2416 -0.0290 0.0082 0.0052 24 CYS A O 185 C CB . CYS A 24 ? 0.1483 0.1617 0.1864 0.0062 0.0187 -0.0016 24 CYS A CB 186 S SG . CYS A 24 ? 0.1967 0.1794 0.2054 -0.0004 0.0226 0.0107 24 CYS A SG 187 N N . LYS A 25 ? 0.1572 0.1522 0.1670 -0.0071 0.0194 0.0066 25 LYS A N 188 C CA . LYS A 25 ? 0.1610 0.1645 0.1820 -0.0019 0.0149 0.0053 25 LYS A CA 189 C C . LYS A 25 ? 0.1447 0.1442 0.1566 -0.0056 0.0129 0.0039 25 LYS A C 190 O O . LYS A 25 ? 0.1454 0.1630 0.1531 -0.0141 0.0232 0.0079 25 LYS A O 191 C CB . LYS A 25 ? 0.1752 0.1750 0.1943 -0.0022 0.0134 0.0086 25 LYS A CB 192 C CG . LYS A 25 ? 0.2042 0.1949 0.2003 0.0100 0.0185 -0.0059 25 LYS A CG 193 C CD . LYS A 25 ? 0.2123 0.2313 0.2063 0.0049 0.0039 -0.0049 25 LYS A CD 194 C CE . LYS A 25 ? 0.2486 0.2775 0.2628 0.0060 0.0162 -0.0098 25 LYS A CE 195 N NZ . LYS A 25 ? 0.3081 0.3227 0.3114 -0.0423 0.0105 0.0000 25 LYS A NZ 196 N N . PRO A 26 ? 0.1366 0.1535 0.1527 -0.0091 0.0211 0.0073 26 PRO A N 197 C CA . PRO A 26 ? 0.1493 0.1436 0.1547 -0.0027 0.0131 0.0003 26 PRO A CA 198 C C . PRO A 26 ? 0.1511 0.1533 0.1499 -0.0069 0.0096 0.0064 26 PRO A C 199 O O . PRO A 26 ? 0.1604 0.1909 0.1601 0.0036 0.0234 0.0047 26 PRO A O 200 C CB . PRO A 26 ? 0.1458 0.1497 0.1501 -0.0139 0.0184 0.0031 26 PRO A CB 201 C CG . PRO A 26 ? 0.1532 0.1573 0.1519 -0.0119 0.0223 0.0014 26 PRO A CG 202 C CD . PRO A 26 ? 0.1448 0.1532 0.1717 -0.0103 0.0020 0.0059 26 PRO A CD 203 N N . ALA A 27 ? 0.1385 0.1585 0.1477 0.0051 0.0097 0.0026 27 ALA A N 204 C CA . ALA A 27 ? 0.1482 0.1476 0.1564 -0.0031 0.0042 0.0131 27 ALA A CA 205 C C . ALA A 27 ? 0.1345 0.1491 0.1461 0.0021 0.0013 0.0160 27 ALA A C 206 O O . ALA A 27 ? 0.1403 0.1623 0.1549 -0.0048 0.0114 0.0127 27 ALA A O 207 C CB . ALA A 27 ? 0.1513 0.1627 0.1666 -0.0021 -0.0010 -0.0019 27 ALA A CB 208 N N . THR A 28 ? 0.1438 0.1568 0.1465 0.0018 0.0035 0.0136 28 THR A N 209 C CA . THR A 28 ? 0.1346 0.1434 0.1504 -0.0004 0.0069 0.0149 28 THR A CA 210 C C . THR A 28 ? 0.1281 0.1453 0.1334 -0.0054 0.0070 0.0140 28 THR A C 211 O O . THR A 28 ? 0.1333 0.1701 0.1320 -0.0036 0.0074 0.0158 28 THR A O 212 C CB . THR A 28 ? 0.1595 0.1477 0.1641 0.0042 0.0121 0.0261 28 THR A CB 213 O OG1 . THR A 28 ? 0.1764 0.1840 0.2053 -0.0092 0.0384 0.0198 28 THR A OG1 214 C CG2 . THR A 28 ? 0.1828 0.1566 0.1721 0.0031 0.0092 0.0223 28 THR A CG2 215 N N . ASN A 29 ? 0.1112 0.1362 0.1234 -0.0075 0.0049 0.0085 29 ASN A N 216 C CA . ASN A 29 ? 0.1133 0.1249 0.1305 -0.0052 0.0072 0.0024 29 ASN A CA 217 C C . ASN A 29 ? 0.1153 0.1184 0.1180 -0.0069 0.0038 -0.0035 29 ASN A C 218 O O . ASN A 29 ? 0.1173 0.1221 0.1320 -0.0004 0.0074 -0.0048 29 ASN A O 219 C CB . ASN A 29 ? 0.1115 0.1212 0.1338 -0.0062 -0.0008 0.0047 29 ASN A CB 220 C CG . ASN A 29 ? 0.1161 0.1346 0.1350 0.0029 0.0194 -0.0043 29 ASN A CG 221 O OD1 . ASN A 29 ? 0.1123 0.1271 0.1648 -0.0204 0.0234 -0.0135 29 ASN A OD1 222 N ND2 . ASN A 29 ? 0.1346 0.1277 0.1208 -0.0207 -0.0022 0.0009 29 ASN A ND2 223 N N . PHE A 30 ? 0.1040 0.1198 0.1075 -0.0098 0.0050 0.0000 30 PHE A N 224 C CA . PHE A 30 ? 0.1032 0.1115 0.1179 -0.0073 0.0082 0.0019 30 PHE A CA 225 C C . PHE A 30 ? 0.1098 0.1033 0.1133 0.0013 0.0088 0.0014 30 PHE A C 226 O O . PHE A 30 ? 0.1141 0.1124 0.1226 -0.0087 0.0114 -0.0126 30 PHE A O 227 C CB . PHE A 30 ? 0.1109 0.1345 0.1230 -0.0075 0.0040 0.0084 30 PHE A CB 228 C CG . PHE A 30 ? 0.1173 0.1177 0.1309 -0.0039 -0.0029 0.0056 30 PHE A CG 229 C CD1 . PHE A 30 ? 0.1122 0.1266 0.1208 0.0063 -0.0043 0.0111 30 PHE A CD1 230 C CD2 . PHE A 30 ? 0.1378 0.1351 0.1409 0.0028 0.0041 0.0038 30 PHE A CD2 231 C CE1 . PHE A 30 ? 0.1344 0.1276 0.1612 -0.0181 -0.0024 0.0103 30 PHE A CE1 232 C CE2 . PHE A 30 ? 0.1564 0.1705 0.1256 -0.0119 -0.0140 0.0145 30 PHE A CE2 233 C CZ . PHE A 30 ? 0.1544 0.1388 0.1508 -0.0088 -0.0028 0.0253 30 PHE A CZ 234 N N . ILE A 31 ? 0.1136 0.1050 0.1161 -0.0081 0.0009 0.0022 31 ILE A N 235 C CA . ILE A 31 ? 0.1027 0.1074 0.1052 -0.0018 0.0021 0.0001 31 ILE A CA 236 C C . ILE A 31 ? 0.1043 0.1059 0.1158 -0.0004 0.0122 0.0021 31 ILE A C 237 O O . ILE A 31 ? 0.1201 0.1093 0.1400 -0.0181 0.0170 0.0035 31 ILE A O 238 C CB . ILE A 31 ? 0.0976 0.0999 0.1305 -0.0082 -0.0061 0.0029 31 ILE A CB 239 C CG1 . ILE A 31 ? 0.1140 0.1389 0.1255 -0.0019 0.0032 0.0165 31 ILE A CG1 240 C CG2 . ILE A 31 ? 0.1149 0.1124 0.1238 0.0047 -0.0042 -0.0118 31 ILE A CG2 241 C CD1 . ILE A 31 ? 0.1326 0.1464 0.1379 0.0191 -0.0076 0.0058 31 ILE A CD1 242 N N . VAL A 32 ? 0.0974 0.0952 0.1157 0.0039 0.0002 -0.0012 32 VAL A N 243 C CA . VAL A 32 ? 0.1010 0.0972 0.1005 0.0007 0.0027 -0.0049 32 VAL A CA 244 C C . VAL A 32 ? 0.0876 0.0988 0.1009 0.0058 -0.0036 -0.0069 32 VAL A C 245 O O . VAL A 32 ? 0.1128 0.1072 0.1010 0.0075 -0.0079 -0.0026 32 VAL A O 246 C CB . VAL A 32 ? 0.0995 0.0967 0.1100 0.0082 -0.0016 0.0009 32 VAL A CB 247 C CG1 . VAL A 32 ? 0.1082 0.1155 0.0905 0.0023 0.0016 0.0001 32 VAL A CG1 248 C CG2 . VAL A 32 ? 0.1075 0.1061 0.1185 0.0095 0.0046 0.0039 32 VAL A CG2 249 N N . LEU A 33 ? 0.0916 0.0911 0.0998 -0.0014 0.0027 -0.0075 33 LEU A N 250 C CA . LEU A 33 ? 0.0966 0.1032 0.1097 0.0034 0.0006 -0.0004 33 LEU A CA 251 C C . LEU A 33 ? 0.0950 0.1014 0.0986 -0.0008 0.0012 -0.0045 33 LEU A C 252 O O . LEU A 33 ? 0.1017 0.0986 0.0970 0.0060 0.0179 -0.0025 33 LEU A O 253 C CB . LEU A 33 ? 0.1236 0.1159 0.1131 0.0100 0.0080 0.0073 33 LEU A CB 254 C CG . LEU A 33 ? 0.1825 0.1583 0.1855 0.0164 0.0056 -0.0176 33 LEU A CG 255 C CD1 . LEU A 33 ? 0.2211 0.1693 0.2151 0.0028 -0.0014 -0.0168 33 LEU A CD1 256 C CD2 . LEU A 33 ? 0.1354 0.1508 0.1490 0.0000 0.0012 -0.0067 33 LEU A CD2 257 N N . ASP A 34 ? 0.0848 0.1138 0.1058 -0.0038 0.0017 0.0033 34 ASP A N 258 C CA . ASP A 34 ? 0.0975 0.1040 0.1025 -0.0034 0.0056 -0.0016 34 ASP A CA 259 C C . ASP A 34 ? 0.0955 0.1053 0.0991 -0.0015 0.0040 -0.0008 34 ASP A C 260 O O . ASP A 34 ? 0.1126 0.1104 0.1095 -0.0067 0.0037 -0.0083 34 ASP A O 261 C CB . ASP A 34 ? 0.0809 0.0912 0.0961 -0.0013 -0.0008 -0.0044 34 ASP A CB 262 C CG . ASP A 34 ? 0.0899 0.1060 0.1062 -0.0048 0.0042 -0.0003 34 ASP A CG 263 O OD1 . ASP A 34 ? 0.0929 0.1120 0.1205 0.0061 -0.0002 -0.0042 34 ASP A OD1 264 O OD2 . ASP A 34 ? 0.1038 0.1068 0.0929 0.0006 -0.0058 0.0013 34 ASP A OD2 265 N N . SER A 35 ? 0.1046 0.0914 0.0948 -0.0042 -0.0068 -0.0147 35 SER A N 266 C CA . SER A 35 ? 0.1061 0.0992 0.1030 0.0039 0.0035 -0.0017 35 SER A CA 267 C C . SER A 35 ? 0.0965 0.0948 0.1084 0.0003 0.0046 -0.0056 35 SER A C 268 O O . SER A 35 ? 0.1093 0.1054 0.1014 0.0145 -0.0015 -0.0061 35 SER A O 269 C CB . SER A 35 ? 0.1073 0.1099 0.1030 0.0115 0.0026 -0.0043 35 SER A CB 270 O OG . SER A 35 ? 0.0986 0.1272 0.1063 -0.0053 0.0050 -0.0007 35 SER A OG 271 N N . LEU A 36 ? 0.0934 0.0967 0.1056 0.0067 -0.0005 -0.0020 36 LEU A N 272 C CA . LEU A 36 ? 0.1121 0.1208 0.1155 0.0035 -0.0008 -0.0008 36 LEU A CA 273 C C . LEU A 36 ? 0.1128 0.1296 0.1119 0.0005 0.0041 -0.0049 36 LEU A C 274 O O . LEU A 36 ? 0.1488 0.1726 0.1272 -0.0085 0.0081 -0.0147 36 LEU A O 275 C CB . LEU A 36 ? 0.1075 0.1156 0.1113 -0.0025 0.0024 -0.0047 36 LEU A CB 276 C CG . LEU A 36 ? 0.1256 0.1427 0.1218 -0.0006 0.0083 -0.0103 36 LEU A CG 277 C CD1 . LEU A 36 ? 0.1329 0.1604 0.1358 -0.0097 0.0011 -0.0062 36 LEU A CD1 278 C CD2 . LEU A 36 ? 0.1590 0.1404 0.1560 -0.0089 -0.0010 0.0074 36 LEU A CD2 279 N N . SER A 37 ? 0.1013 0.1077 0.1058 -0.0034 0.0062 -0.0009 37 SER A N 280 C CA . SER A 37 ? 0.1033 0.1151 0.1058 0.0011 -0.0064 -0.0008 37 SER A CA 281 C C . SER A 37 ? 0.1120 0.1160 0.1117 -0.0020 -0.0062 -0.0039 37 SER A C 282 O O . SER A 37 ? 0.1244 0.1341 0.1263 0.0031 0.0000 -0.0176 37 SER A O 283 C CB . SER A 37 ? 0.1181 0.1196 0.1292 -0.0048 -0.0024 0.0032 37 SER A CB 284 O OG . SER A 37 ? 0.1465 0.1270 0.1722 0.0063 -0.0185 0.0085 37 SER A OG 285 N N . HIS A 38 ? 0.1082 0.1134 0.1039 0.0016 0.0030 -0.0018 38 HIS A N 286 C CA . HIS A 38 ? 0.1115 0.1155 0.1194 -0.0038 0.0015 -0.0036 38 HIS A CA 287 C C . HIS A 38 ? 0.1240 0.1247 0.1243 -0.0016 -0.0006 -0.0096 38 HIS A C 288 O O . HIS A 38 ? 0.1344 0.1151 0.1367 0.0097 0.0085 -0.0054 38 HIS A O 289 C CB . HIS A 38 ? 0.1046 0.1166 0.1198 0.0114 0.0026 -0.0088 38 HIS A CB 290 C CG . HIS A 38 ? 0.0962 0.1059 0.1078 -0.0010 -0.0021 -0.0141 38 HIS A CG 291 N ND1 . HIS A 38 ? 0.0856 0.1043 0.1142 -0.0006 0.0028 -0.0066 38 HIS A ND1 292 C CD2 . HIS A 38 ? 0.1276 0.0950 0.1311 0.0193 -0.0116 0.0009 38 HIS A CD2 293 C CE1 . HIS A 38 ? 0.1154 0.1027 0.1093 -0.0007 0.0019 0.0033 38 HIS A CE1 294 N NE2 . HIS A 38 ? 0.1200 0.1107 0.1394 0.0133 -0.0036 -0.0023 38 HIS A NE2 295 N N . PRO A 39 ? 0.1199 0.1166 0.1102 0.0008 0.0007 -0.0032 39 PRO A N 296 C CA . PRO A 39 ? 0.1245 0.1348 0.1215 0.0072 0.0010 -0.0057 39 PRO A CA 297 C C . PRO A 39 ? 0.1295 0.1381 0.1209 0.0088 -0.0018 -0.0047 39 PRO A C 298 O O . PRO A 39 ? 0.1448 0.1498 0.1356 -0.0003 -0.0050 0.0073 39 PRO A O 299 C CB . PRO A 39 ? 0.1430 0.1340 0.1290 0.0094 0.0040 -0.0035 39 PRO A CB 300 C CG . PRO A 39 ? 0.1363 0.1117 0.1247 0.0063 0.0035 -0.0040 39 PRO A CG 301 C CD . PRO A 39 ? 0.1403 0.1393 0.1189 -0.0009 0.0087 -0.0050 39 PRO A CD 302 N N . ILE A 40 ? 0.1312 0.1476 0.1317 0.0043 0.0000 0.0060 40 ILE A N 303 C CA . ILE A 40 ? 0.1333 0.1603 0.1379 0.0091 0.0015 0.0016 40 ILE A CA 304 C C . ILE A 40 ? 0.1347 0.1603 0.1342 0.0090 0.0053 0.0061 40 ILE A C 305 O O . ILE A 40 ? 0.1269 0.1940 0.1378 0.0300 0.0139 0.0141 40 ILE A O 306 C CB . ILE A 40 ? 0.1425 0.1696 0.1498 0.0061 0.0077 -0.0049 40 ILE A CB 307 C CG1 . ILE A 40 ? 0.1794 0.1846 0.2012 0.0071 0.0087 -0.0080 40 ILE A CG1 308 C CG2 . ILE A 40 ? 0.1560 0.1771 0.1805 0.0023 -0.0033 0.0001 40 ILE A CG2 309 C CD1 . ILE A 40 ? 0.2022 0.1804 0.2042 0.0068 0.0063 0.0047 40 ILE A CD1 310 N N . HIS A 41 ? 0.1222 0.1571 0.1269 0.0137 0.0029 0.0041 41 HIS A N 311 C CA . HIS A 41 ? 0.1278 0.1552 0.1277 0.0086 0.0038 -0.0011 41 HIS A CA 312 C C . HIS A 41 ? 0.1138 0.1467 0.1310 0.0145 0.0065 -0.0046 41 HIS A C 313 O O . HIS A 41 ? 0.1244 0.1533 0.1428 0.0231 0.0110 -0.0174 41 HIS A O 314 C CB . HIS A 41 ? 0.1139 0.1595 0.1294 0.0099 0.0149 -0.0035 41 HIS A CB 315 C CG . HIS A 41 ? 0.1253 0.1517 0.1375 0.0073 0.0154 -0.0002 41 HIS A CG 316 N ND1 . HIS A 41 ? 0.1446 0.1591 0.1639 0.0100 0.0215 0.0094 41 HIS A ND1 317 C CD2 . HIS A 41 ? 0.1295 0.1884 0.1631 0.0147 0.0144 0.0080 41 HIS A CD2 318 C CE1 . HIS A 41 ? 0.1584 0.1596 0.1582 0.0091 -0.0046 0.0120 41 HIS A CE1 319 N NE2 . HIS A 41 ? 0.1644 0.1598 0.1579 0.0151 0.0087 -0.0028 41 HIS A NE2 320 N N . ARG A 42 ? 0.1141 0.1331 0.1231 0.0217 0.0074 -0.0102 42 ARG A N 321 C CA . ARG A 42 ? 0.1210 0.1291 0.1207 0.0074 0.0043 -0.0037 42 ARG A CA 322 C C . ARG A 42 ? 0.1311 0.1282 0.1240 0.0054 0.0046 -0.0072 42 ARG A C 323 O O . ARG A 42 ? 0.1335 0.1360 0.1304 0.0099 0.0049 -0.0112 42 ARG A O 324 C CB . ARG A 42 ? 0.1240 0.1240 0.1276 0.0211 0.0067 -0.0028 42 ARG A CB 325 C CG . ARG A 42 ? 0.1185 0.1381 0.1380 0.0059 0.0083 0.0074 42 ARG A CG 326 C CD . ARG A 42 ? 0.1312 0.1481 0.1378 0.0058 0.0058 -0.0002 42 ARG A CD 327 N NE . ARG A 42 ? 0.1289 0.1477 0.1290 0.0109 -0.0017 0.0149 42 ARG A NE 328 C CZ . ARG A 42 ? 0.1463 0.1443 0.1399 0.0010 0.0040 0.0039 42 ARG A CZ 329 N NH1 . ARG A 42 ? 0.1657 0.1746 0.1625 0.0079 0.0094 0.0076 42 ARG A NH1 330 N NH2 . ARG A 42 ? 0.1585 0.1518 0.1681 0.0111 0.0182 0.0171 42 ARG A NH2 331 N N . ALA A 43 ? 0.1325 0.1170 0.1222 0.0071 -0.0069 -0.0071 43 ALA A N 332 C CA . ALA A 43 ? 0.1405 0.1305 0.1243 0.0035 -0.0009 0.0001 43 ALA A CA 333 C C . ALA A 43 ? 0.1512 0.1402 0.1276 0.0023 0.0011 0.0014 43 ALA A C 334 O O . ALA A 43 ? 0.1436 0.1463 0.1263 0.0042 0.0005 0.0118 43 ALA A O 335 C CB . ALA A 43 ? 0.1536 0.1504 0.1352 0.0045 -0.0045 0.0029 43 ALA A CB 336 N N . GLU A 44 ? 0.1487 0.1302 0.1280 0.0043 0.0123 0.0047 44 GLU A N 337 C CA . GLU A 44 ? 0.1489 0.1437 0.1501 0.0047 -0.0020 0.0000 44 GLU A CA 338 C C . GLU A 44 ? 0.1557 0.1352 0.1466 0.0034 -0.0027 -0.0011 44 GLU A C 339 O O . GLU A 44 ? 0.1537 0.1395 0.1364 0.0142 -0.0160 0.0017 44 GLU A O 340 C CB . GLU A 44 ? 0.1577 0.1386 0.1641 0.0038 -0.0060 -0.0002 44 GLU A CB 341 C CG . GLU A 44 ? 0.1706 0.1707 0.1655 0.0042 -0.0041 0.0062 44 GLU A CG 342 C CD . GLU A 44 ? 0.1698 0.1781 0.1725 -0.0006 0.0025 0.0115 44 GLU A CD 343 O OE1 . GLU A 44 ? 0.1603 0.1796 0.1884 -0.0030 -0.0159 0.0367 44 GLU A OE1 344 O OE2 . GLU A 44 ? 0.1620 0.1814 0.1913 0.0051 -0.0084 0.0368 44 GLU A OE2 345 N N . GLY A 45 ? 0.1555 0.1415 0.1425 0.0052 0.0019 0.0023 45 GLY A N 346 C CA . GLY A 45 ? 0.1638 0.1585 0.1667 0.0102 0.0081 0.0025 45 GLY A CA 347 C C . GLY A 45 ? 0.1724 0.1625 0.1737 0.0103 0.0152 0.0024 45 GLY A C 348 O O . GLY A 45 ? 0.1847 0.1993 0.2055 0.0214 0.0289 0.0042 45 GLY A O 349 N N . LEU A 46 ? 0.1544 0.1466 0.1600 0.0138 0.0110 0.0061 46 LEU A N 350 C CA . LEU A 46 ? 0.1415 0.1536 0.1558 0.0001 0.0084 0.0049 46 LEU A CA 351 C C . LEU A 46 ? 0.1541 0.1559 0.1472 0.0013 0.0050 0.0040 46 LEU A C 352 O O . LEU A 46 ? 0.1722 0.1599 0.1657 0.0014 -0.0038 0.0034 46 LEU A O 353 C CB . LEU A 46 ? 0.1281 0.1503 0.1496 0.0059 0.0076 0.0085 46 LEU A CB 354 C CG . LEU A 46 ? 0.1469 0.1605 0.1547 -0.0006 0.0115 -0.0153 46 LEU A CG 355 C CD1 . LEU A 46 ? 0.1713 0.1569 0.1430 0.0142 -0.0122 -0.0094 46 LEU A CD1 356 C CD2 . LEU A 46 ? 0.1624 0.1739 0.1741 0.0026 0.0074 0.0028 46 LEU A CD2 357 N N . GLY A 47 ? 0.1530 0.1617 0.1438 0.0006 -0.0001 0.0089 47 GLY A N 358 C CA . GLY A 47 ? 0.1710 0.1555 0.1473 -0.0020 0.0023 0.0042 47 GLY A CA 359 C C . GLY A 47 ? 0.1695 0.1530 0.1422 -0.0006 0.0038 -0.0004 47 GLY A C 360 O O . GLY A 47 ? 0.1609 0.1785 0.1260 0.0214 0.0070 -0.0159 47 GLY A O 361 N N . PRO A 48 ? 0.1679 0.1589 0.1426 0.0017 0.0041 -0.0123 48 PRO A N 362 C CA . PRO A 48 ? 0.1712 0.1635 0.1464 0.0000 -0.0043 0.0008 48 PRO A CA 363 C C . PRO A 48 ? 0.1814 0.1714 0.1539 -0.0010 -0.0012 0.0011 48 PRO A C 364 O O . PRO A 48 ? 0.1913 0.1591 0.1697 0.0115 -0.0184 -0.0023 48 PRO A O 365 C CB . PRO A 48 ? 0.1652 0.1638 0.1601 -0.0109 -0.0074 0.0000 48 PRO A CB 366 C CG . PRO A 48 ? 0.1864 0.1780 0.1382 0.0015 -0.0049 -0.0089 48 PRO A CG 367 C CD . PRO A 48 ? 0.1839 0.1659 0.1573 -0.0032 0.0053 -0.0132 48 PRO A CD 368 N N . GLY A 49 ? 0.1897 0.1689 0.1683 0.0051 -0.0075 0.0007 49 GLY A N 369 C CA . GLY A 49 ? 0.1886 0.1707 0.1678 0.0067 -0.0074 0.0020 49 GLY A CA 370 C C . GLY A 49 ? 0.1901 0.1745 0.1649 0.0098 -0.0054 0.0036 49 GLY A C 371 O O . GLY A 49 ? 0.1684 0.1613 0.1481 0.0114 -0.0049 0.0085 49 GLY A O 372 N N . GLY A 50 ? 0.2052 0.1801 0.1679 0.0089 -0.0114 -0.0009 50 GLY A N 373 C CA . GLY A 50 ? 0.1803 0.1692 0.1655 0.0055 -0.0026 -0.0048 50 GLY A CA 374 C C . GLY A 50 ? 0.1708 0.1673 0.1606 0.0045 0.0024 0.0001 50 GLY A C 375 O O . GLY A 50 ? 0.1665 0.1701 0.1480 0.0115 0.0082 -0.0023 50 GLY A O 376 N N . CYS A 51 ? 0.1613 0.1442 0.1393 0.0047 0.0088 -0.0039 51 CYS A N 377 C CA . CYS A 51 ? 0.1539 0.1523 0.1388 0.0030 0.0063 0.0010 51 CYS A CA 378 C C . CYS A 51 ? 0.1571 0.1518 0.1405 0.0074 -0.0022 -0.0007 51 CYS A C 379 O O . CYS A 51 ? 0.1919 0.1577 0.1273 0.0132 -0.0077 0.0034 51 CYS A O 380 C CB . CYS A 51 ? 0.1451 0.1355 0.1417 0.0118 0.0010 -0.0022 51 CYS A CB 381 S SG . CYS A 51 ? 0.1570 0.1327 0.1380 0.0203 0.0094 0.0040 51 CYS A SG 382 N N . GLY A 52 ? 0.1570 0.1504 0.1433 0.0076 0.0011 0.0031 52 GLY A N 383 C CA . GLY A 52 ? 0.1621 0.1577 0.1542 0.0069 0.0041 0.0010 52 GLY A CA 384 C C . GLY A 52 ? 0.1616 0.1545 0.1596 0.0004 -0.0020 0.0020 52 GLY A C 385 O O . GLY A 52 ? 0.1498 0.1655 0.1802 0.0052 -0.0108 0.0017 52 GLY A O 386 N N . ASP A 53 ? 0.1741 0.1697 0.1610 0.0103 -0.0034 -0.0003 53 ASP A N 387 C CA . ASP A 53 ? 0.1806 0.1727 0.1643 0.0120 -0.0049 -0.0026 53 ASP A CA 388 C C . ASP A 53 ? 0.1750 0.1670 0.1501 0.0090 -0.0079 0.0011 53 ASP A C 389 O O . ASP A 53 ? 0.1555 0.1640 0.1504 0.0081 -0.0028 0.0059 53 ASP A O 390 C CB . ASP A 53 ? 0.2091 0.1972 0.1847 0.0164 -0.0096 -0.0002 53 ASP A CB 391 C CG . ASP A 53 ? 0.2502 0.2530 0.2358 0.0183 -0.0086 -0.0085 53 ASP A CG 392 O OD1 . ASP A 53 ? 0.3083 0.2801 0.3091 -0.0016 -0.0277 -0.0237 53 ASP A OD1 393 O OD2 . ASP A 53 ? 0.3609 0.3531 0.3029 0.0139 0.0126 -0.0247 53 ASP A OD2 394 N N . TRP A 54 ? 0.1621 0.1658 0.1495 0.0054 -0.0010 -0.0066 54 TRP A N 395 C CA . TRP A 54 ? 0.1657 0.1567 0.1470 0.0013 -0.0066 -0.0017 54 TRP A CA 396 C C . TRP A 54 ? 0.1801 0.1690 0.1530 0.0076 0.0025 0.0009 54 TRP A C 397 O O . TRP A 54 ? 0.1984 0.1841 0.1450 0.0236 -0.0015 -0.0115 54 TRP A O 398 C CB . TRP A 54 ? 0.1813 0.1721 0.1614 0.0032 0.0039 0.0037 54 TRP A CB 399 C CG . TRP A 54 ? 0.1643 0.1676 0.1539 0.0048 -0.0070 -0.0075 54 TRP A CG 400 C CD1 . TRP A 54 ? 0.2045 0.1876 0.1835 0.0121 -0.0003 0.0022 54 TRP A CD1 401 C CD2 . TRP A 54 ? 0.2368 0.1910 0.1570 0.0195 0.0079 0.0045 54 TRP A CD2 402 N NE1 . TRP A 54 ? 0.1756 0.1627 0.1655 0.0082 -0.0047 -0.0067 54 TRP A NE1 403 C CE2 . TRP A 54 ? 0.2406 0.1772 0.1769 0.0260 -0.0024 0.0002 54 TRP A CE2 404 C CE3 . TRP A 54 ? 0.2891 0.2117 0.1978 0.0212 0.0057 0.0096 54 TRP A CE3 405 C CZ2 . TRP A 54 ? 0.2766 0.2148 0.2162 0.0328 -0.0045 0.0060 54 TRP A CZ2 406 C CZ3 . TRP A 54 ? 0.2673 0.2165 0.2020 0.0252 -0.0005 0.0035 54 TRP A CZ3 407 C CH2 . TRP A 54 ? 0.2866 0.2238 0.2222 0.0272 0.0015 0.0030 54 TRP A CH2 408 N N . GLY A 55 ? 0.1592 0.1471 0.1483 0.0055 0.0010 0.0019 55 GLY A N 409 C CA . GLY A 55 ? 0.1594 0.1490 0.1465 0.0028 0.0056 0.0017 55 GLY A CA 410 C C . GLY A 55 ? 0.1625 0.1479 0.1551 0.0093 0.0190 0.0033 55 GLY A C 411 O O . GLY A 55 ? 0.1665 0.1635 0.1795 0.0135 0.0276 0.0089 55 GLY A O 412 N N . ASN A 56 ? 0.1612 0.1512 0.1480 0.0118 0.0135 0.0068 56 ASN A N 413 C CA . ASN A 56 ? 0.1605 0.1586 0.1476 0.0026 0.0103 0.0027 56 ASN A CA 414 C C . ASN A 56 ? 0.1553 0.1520 0.1493 0.0050 0.0071 0.0012 56 ASN A C 415 O O . ASN A 56 ? 0.1394 0.1532 0.1519 -0.0041 0.0117 0.0016 56 ASN A O 416 C CB . ASN A 56 ? 0.1796 0.1904 0.1529 0.0107 0.0145 -0.0030 56 ASN A CB 417 C CG . ASN A 56 ? 0.2313 0.2366 0.2053 -0.0010 -0.0050 0.0133 56 ASN A CG 418 O OD1 . ASN A 56 ? 0.2960 0.2669 0.1963 0.0048 0.0245 0.0139 56 ASN A OD1 419 N ND2 . ASN A 56 ? 0.3648 0.3079 0.2858 -0.0285 -0.0323 0.0055 56 ASN A ND2 420 N N . PRO A 57 ? 0.1518 0.1437 0.1458 0.0009 0.0193 0.0126 57 PRO A N 421 C CA . PRO A 57 ? 0.1444 0.1518 0.1411 0.0021 0.0134 0.0024 57 PRO A CA 422 C C . PRO A 57 ? 0.1527 0.1514 0.1372 0.0015 0.0083 0.0029 57 PRO A C 423 O O . PRO A 57 ? 0.1613 0.1523 0.1518 0.0158 0.0052 0.0084 57 PRO A O 424 C CB . PRO A 57 ? 0.1593 0.1515 0.1471 -0.0070 0.0174 -0.0003 57 PRO A CB 425 C CG . PRO A 57 ? 0.1742 0.1793 0.1978 0.0021 0.0157 0.0272 57 PRO A CG 426 C CD . PRO A 57 ? 0.1535 0.1535 0.1499 0.0001 0.0229 0.0149 57 PRO A CD 427 N N . PRO A 58 ? 0.1418 0.1333 0.1387 0.0040 0.0074 0.0068 58 PRO A N 428 C CA . PRO A 58 ? 0.1492 0.1449 0.1479 0.0059 0.0101 0.0028 58 PRO A CA 429 C C . PRO A 58 ? 0.1606 0.1543 0.1596 0.0013 0.0087 -0.0028 58 PRO A C 430 O O . PRO A 58 ? 0.1550 0.1471 0.1498 0.0045 0.0169 -0.0039 58 PRO A O 431 C CB . PRO A 58 ? 0.1371 0.1318 0.1518 0.0074 0.0099 0.0133 58 PRO A CB 432 C CG . PRO A 58 ? 0.1217 0.1413 0.1155 0.0179 0.0141 0.0111 58 PRO A CG 433 C CD . PRO A 58 ? 0.1495 0.1268 0.1447 0.0045 0.0173 -0.0001 58 PRO A CD 434 N N . PRO A 59 ? 0.1603 0.1565 0.1552 0.0093 0.0187 -0.0033 59 PRO A N 435 C CA . PRO A 59 ? 0.1782 0.1799 0.1780 0.0082 0.0177 -0.0039 59 PRO A CA 436 C C . PRO A 59 ? 0.1819 0.1862 0.1843 0.0111 0.0204 0.0002 59 PRO A C 437 O O . PRO A 59 ? 0.1654 0.1804 0.1748 0.0223 0.0395 0.0039 59 PRO A O 438 C CB . PRO A 59 ? 0.1836 0.1820 0.1724 0.0126 0.0101 -0.0064 59 PRO A CB 439 C CG . PRO A 59 ? 0.1985 0.1682 0.1906 0.0079 0.0050 -0.0187 59 PRO A CG 440 C CD . PRO A 59 ? 0.1749 0.1749 0.1766 0.0146 0.0139 -0.0105 59 PRO A CD 441 N N . LYS A 60 ? 0.1932 0.1951 0.1938 0.0015 0.0312 0.0018 60 LYS A N 442 C CA . LYS A 60 ? 0.2175 0.2237 0.2214 0.0016 0.0180 0.0011 60 LYS A CA 443 C C . LYS A 60 ? 0.1992 0.2267 0.2178 0.0019 0.0218 0.0083 60 LYS A C 444 O O . LYS A 60 ? 0.2007 0.2210 0.2211 0.0112 0.0381 0.0080 60 LYS A O 445 C CB . LYS A 60 ? 0.2242 0.2449 0.2352 -0.0048 0.0214 0.0064 60 LYS A CB 446 C CG . LYS A 60 ? 0.2682 0.2695 0.2803 0.0002 0.0084 -0.0005 60 LYS A CG 447 C CD . LYS A 60 ? 0.2916 0.2822 0.3092 -0.0069 0.0178 0.0081 60 LYS A CD 448 C CE . LYS A 60 ? 0.3531 0.3165 0.3639 0.0045 -0.0001 0.0076 60 LYS A CE 449 N NZ . LYS A 60 ? 0.3918 0.3916 0.3608 -0.0047 -0.0005 0.0090 60 LYS A NZ 450 N N . ASP A 61 ? 0.2022 0.2107 0.2220 0.0130 0.0286 0.0093 61 ASP A N 451 C CA . ASP A 61 ? 0.2282 0.2209 0.2349 0.0091 0.0190 0.0090 61 ASP A CA 452 C C . ASP A 61 ? 0.2115 0.2220 0.2285 0.0153 0.0122 0.0121 61 ASP A C 453 O O . ASP A 61 ? 0.2141 0.2407 0.2728 0.0275 0.0056 0.0271 61 ASP A O 454 C CB . ASP A 61 ? 0.2529 0.2246 0.2405 0.0069 0.0274 0.0068 61 ASP A CB 455 C CG . ASP A 61 ? 0.2777 0.2564 0.2267 0.0051 0.0198 -0.0055 61 ASP A CG 456 O OD1 . ASP A 61 ? 0.2804 0.2218 0.2706 0.0679 0.0101 -0.0042 61 ASP A OD1 457 O OD2 . ASP A 61 ? 0.2892 0.2450 0.2650 -0.0182 0.0468 -0.0087 61 ASP A OD2 458 N N . VAL A 62 ? 0.1752 0.1902 0.2029 0.0196 0.0077 0.0084 62 VAL A N 459 C CA . VAL A 62 ? 0.1805 0.1800 0.1872 0.0119 0.0037 0.0025 62 VAL A CA 460 C C . VAL A 62 ? 0.1492 0.1579 0.1711 0.0110 0.0017 0.0065 62 VAL A C 461 O O . VAL A 62 ? 0.1389 0.1318 0.1601 0.0177 0.0020 0.0089 62 VAL A O 462 C CB . VAL A 62 ? 0.2005 0.1888 0.1787 0.0088 -0.0054 -0.0022 62 VAL A CB 463 C CG1 . VAL A 62 ? 0.2444 0.2036 0.2169 0.0001 -0.0172 -0.0062 62 VAL A CG1 464 C CG2 . VAL A 62 ? 0.2089 0.2030 0.1902 0.0064 0.0036 -0.0046 62 VAL A CG2 465 N N . CYS A 63 ? 0.1519 0.1401 0.1576 0.0042 0.0013 0.0000 63 CYS A N 466 C CA . CYS A 63 ? 0.1419 0.1438 0.1628 0.0057 0.0070 0.0027 63 CYS A CA 467 C C . CYS A 63 ? 0.1375 0.1512 0.1830 0.0002 0.0063 0.0067 63 CYS A C 468 O O . CYS A 63 ? 0.1409 0.1289 0.1814 0.0002 0.0179 0.0147 63 CYS A O 469 C CB . CYS A 63 ? 0.1386 0.1193 0.1569 0.0118 0.0060 -0.0064 63 CYS A CB 470 S SG . CYS A 63 ? 0.1238 0.1271 0.1577 0.0108 0.0126 0.0091 63 CYS A SG 471 N N . PRO A 64 ? 0.1453 0.1553 0.1935 0.0125 0.0070 0.0085 64 PRO A N 472 C CA . PRO A 64 ? 0.1598 0.1699 0.1950 0.0038 0.0075 0.0059 64 PRO A CA 473 C C . PRO A 64 ? 0.1608 0.1742 0.1991 0.0002 0.0051 0.0055 64 PRO A C 474 O O . PRO A 64 ? 0.1666 0.1964 0.2278 -0.0185 0.0130 0.0042 64 PRO A O 475 C CB . PRO A 64 ? 0.1691 0.1759 0.2100 0.0046 0.0131 0.0009 64 PRO A CB 476 C CG . PRO A 64 ? 0.1422 0.1763 0.2108 0.0092 -0.0013 0.0041 64 PRO A CG 477 C CD . PRO A 64 ? 0.1524 0.1677 0.2035 0.0096 -0.0067 0.0005 64 PRO A CD 478 N N . ASP A 65 ? 0.1439 0.1598 0.1842 -0.0049 0.0078 0.0134 65 ASP A N 479 C CA . ASP A 65 ? 0.1464 0.1680 0.1894 0.0014 -0.0054 0.0079 65 ASP A CA 480 C C . ASP A 65 ? 0.1388 0.1566 0.1845 0.0016 -0.0091 -0.0024 65 ASP A C 481 O O . ASP A 65 ? 0.1192 0.1468 0.2010 -0.0071 0.0001 -0.0085 65 ASP A O 482 C CB . ASP A 65 ? 0.1498 0.1732 0.2139 -0.0044 -0.0087 0.0120 65 ASP A CB 483 C CG . ASP A 65 ? 0.1739 0.1927 0.2735 0.0058 -0.0044 0.0234 65 ASP A CG 484 O OD1 . ASP A 65 ? 0.1640 0.2053 0.2727 0.0002 -0.0058 0.0374 65 ASP A OD1 485 O OD2 . ASP A 65 ? 0.2080 0.2770 0.3963 0.0051 0.0120 0.0182 65 ASP A OD2 486 N N . VAL A 66 ? 0.1332 0.1558 0.1687 -0.0004 -0.0010 -0.0050 66 VAL A N 487 C CA . VAL A 66 ? 0.1409 0.1598 0.1754 0.0022 -0.0068 0.0031 66 VAL A CA 488 C C . VAL A 66 ? 0.1429 0.1541 0.1778 -0.0004 -0.0077 0.0024 66 VAL A C 489 O O . VAL A 66 ? 0.1159 0.1426 0.1668 0.0076 -0.0115 -0.0056 66 VAL A O 490 C CB . VAL A 66 ? 0.1466 0.1606 0.1660 -0.0022 -0.0105 0.0078 66 VAL A CB 491 C CG1 . VAL A 66 ? 0.1734 0.1711 0.1749 0.0047 0.0063 0.0035 66 VAL A CG1 492 C CG2 . VAL A 66 ? 0.1846 0.1790 0.2114 0.0020 -0.0122 0.0050 66 VAL A CG2 493 N N . GLU A 67 ? 0.1338 0.1643 0.1921 -0.0028 -0.0060 0.0033 67 GLU A N 494 C CA . GLU A 67 ? 0.1700 0.1821 0.2009 -0.0012 -0.0032 0.0025 67 GLU A CA 495 C C . GLU A 67 ? 0.1551 0.1714 0.1902 0.0013 0.0043 0.0051 67 GLU A C 496 O O . GLU A 67 ? 0.1314 0.1584 0.2144 -0.0001 0.0104 0.0058 67 GLU A O 497 C CB A GLU A 67 ? 0.1816 0.1993 0.2142 0.0017 -0.0095 0.0055 67 GLU A CB 498 C CB B GLU A 67 ? 0.1742 0.1887 0.2056 0.0016 -0.0094 0.0040 67 GLU A CB 499 C CG A GLU A 67 ? 0.2198 0.2285 0.2320 0.0063 -0.0017 -0.0003 67 GLU A CG 500 C CG B GLU A 67 ? 0.1725 0.1806 0.2054 -0.0073 -0.0075 0.0095 67 GLU A CG 501 C CD A GLU A 67 ? 0.2264 0.2396 0.2499 -0.0023 -0.0090 -0.0029 67 GLU A CD 502 C CD B GLU A 67 ? 0.2014 0.2102 0.2271 0.0006 -0.0178 0.0040 67 GLU A CD 503 O OE1 A GLU A 67 ? 0.2788 0.2791 0.3071 0.0167 -0.0133 0.0099 67 GLU A OE1 504 O OE1 B GLU A 67 ? 0.2072 0.2076 0.2351 0.0069 -0.0372 0.0019 67 GLU A OE1 505 O OE2 A GLU A 67 ? 0.2906 0.2635 0.3149 -0.0096 -0.0124 0.0039 67 GLU A OE2 506 O OE2 B GLU A 67 ? 0.2348 0.2483 0.2866 0.0011 -0.0220 0.0141 67 GLU A OE2 507 N N . SER A 68 ? 0.1479 0.1677 0.1793 0.0013 -0.0021 0.0008 68 SER A N 508 C CA . SER A 68 ? 0.1594 0.1586 0.1842 0.0086 0.0019 0.0018 68 SER A CA 509 C C . SER A 68 ? 0.1538 0.1493 0.1700 0.0076 0.0017 -0.0039 68 SER A C 510 O O . SER A 68 ? 0.1366 0.1343 0.1861 0.0027 0.0236 -0.0026 68 SER A O 511 C CB . SER A 68 ? 0.1808 0.1704 0.2000 0.0065 0.0006 -0.0024 68 SER A CB 512 O OG . SER A 68 ? 0.1852 0.2109 0.2517 0.0103 0.0052 0.0049 68 SER A OG 513 N N . CYS A 69 ? 0.1413 0.1372 0.1623 0.0092 0.0130 -0.0030 69 CYS A N 514 C CA . CYS A 69 ? 0.1465 0.1367 0.1487 0.0059 0.0055 -0.0007 69 CYS A CA 515 C C . CYS A 69 ? 0.1282 0.1212 0.1471 0.0049 0.0003 -0.0024 69 CYS A C 516 O O . CYS A 69 ? 0.1319 0.1234 0.1429 0.0060 -0.0073 0.0032 69 CYS A O 517 C CB . CYS A 69 ? 0.1493 0.1371 0.1591 0.0040 -0.0014 0.0013 69 CYS A CB 518 S SG . CYS A 69 ? 0.1268 0.1465 0.1721 0.0124 0.0019 -0.0054 69 CYS A SG 519 N N . ALA A 70 ? 0.1079 0.1260 0.1245 0.0038 -0.0019 0.0041 70 ALA A N 520 C CA . ALA A 70 ? 0.1202 0.1203 0.1288 0.0094 0.0037 0.0031 70 ALA A CA 521 C C . ALA A 70 ? 0.1136 0.1231 0.1317 0.0027 0.0026 -0.0016 70 ALA A C 522 O O . ALA A 70 ? 0.1228 0.1381 0.1587 0.0000 0.0092 -0.0024 70 ALA A O 523 C CB . ALA A 70 ? 0.1222 0.1240 0.1327 0.0097 -0.0011 0.0080 70 ALA A CB 524 N N . LYS A 71 ? 0.1064 0.1288 0.1279 0.0087 0.0093 -0.0009 71 LYS A N 525 C CA . LYS A 71 ? 0.1235 0.1305 0.1352 0.0069 -0.0006 0.0029 71 LYS A CA 526 C C . LYS A 71 ? 0.1309 0.1236 0.1282 0.0011 -0.0068 -0.0018 71 LYS A C 527 O O . LYS A 71 ? 0.1482 0.1195 0.1080 0.0058 0.0032 0.0003 71 LYS A O 528 C CB . LYS A 71 ? 0.1165 0.1260 0.1378 0.0081 0.0008 -0.0008 71 LYS A CB 529 C CG . LYS A 71 ? 0.1553 0.1535 0.1512 0.0181 -0.0185 -0.0080 71 LYS A CG 530 C CD . LYS A 71 ? 0.1618 0.1678 0.1739 0.0223 -0.0106 -0.0054 71 LYS A CD 531 C CE . LYS A 71 ? 0.1679 0.2219 0.1938 0.0170 -0.0051 0.0076 71 LYS A CE 532 N NZ . LYS A 71 ? 0.2034 0.2129 0.2492 0.0025 -0.0300 -0.0084 71 LYS A NZ 533 N N . ASN A 72 ? 0.1189 0.1267 0.1242 0.0048 -0.0010 -0.0006 72 ASN A N 534 C CA . ASN A 72 ? 0.1176 0.1190 0.1294 0.0065 -0.0013 -0.0011 72 ASN A CA 535 C C . ASN A 72 ? 0.1176 0.1243 0.1178 0.0001 -0.0024 -0.0022 72 ASN A C 536 O O . ASN A 72 ? 0.1312 0.1171 0.1348 0.0147 -0.0027 -0.0101 72 ASN A O 537 C CB . ASN A 72 ? 0.1110 0.1192 0.1257 0.0015 -0.0050 -0.0040 72 ASN A CB 538 C CG . ASN A 72 ? 0.1158 0.1099 0.1398 0.0050 -0.0060 0.0086 72 ASN A CG 539 O OD1 . ASN A 72 ? 0.1338 0.1379 0.1376 0.0237 -0.0117 0.0099 72 ASN A OD1 540 N ND2 . ASN A 72 ? 0.1336 0.1200 0.1432 -0.0010 0.0040 -0.0092 72 ASN A ND2 541 N N . CYS A 73 ? 0.1060 0.1302 0.1228 0.0030 -0.0016 -0.0032 73 CYS A N 542 C CA . CYS A 73 ? 0.1142 0.1257 0.1122 0.0036 -0.0026 0.0030 73 CYS A CA 543 C C . CYS A 73 ? 0.1213 0.1236 0.1115 -0.0014 -0.0035 0.0014 73 CYS A C 544 O O . CYS A 73 ? 0.1432 0.1387 0.1061 0.0007 -0.0012 -0.0004 73 CYS A O 545 C CB . CYS A 73 ? 0.1052 0.1261 0.1231 0.0066 -0.0008 0.0027 73 CYS A CB 546 S SG . CYS A 73 ? 0.1182 0.1331 0.1378 0.0034 0.0126 0.0041 73 CYS A SG 547 N N . ILE A 74 ? 0.1228 0.1312 0.1037 -0.0040 -0.0003 0.0022 74 ILE A N 548 C CA . ILE A 74 ? 0.1185 0.1344 0.1130 0.0006 -0.0023 0.0056 74 ILE A CA 549 C C . ILE A 74 ? 0.1096 0.1333 0.0992 0.0011 0.0041 0.0049 74 ILE A C 550 O O . ILE A 74 ? 0.1076 0.1702 0.1122 0.0205 0.0028 0.0002 74 ILE A O 551 C CB . ILE A 74 ? 0.1112 0.1452 0.1205 0.0109 0.0008 0.0038 74 ILE A CB 552 C CG1 . ILE A 74 ? 0.1316 0.1521 0.1498 0.0191 0.0071 0.0056 74 ILE A CG1 553 C CG2 . ILE A 74 ? 0.1376 0.1404 0.1312 0.0064 0.0015 0.0144 74 ILE A CG2 554 C CD1 . ILE A 74 ? 0.1544 0.1586 0.1650 0.0182 -0.0005 -0.0014 74 ILE A CD1 555 N N . MET A 75 ? 0.1110 0.1283 0.1114 0.0080 0.0078 0.0022 75 MET A N 556 C CA . MET A 75 ? 0.1167 0.1229 0.1143 0.0067 0.0018 0.0031 75 MET A CA 557 C C . MET A 75 ? 0.1156 0.1205 0.1157 0.0045 0.0000 -0.0047 75 MET A C 558 O O . MET A 75 ? 0.0972 0.1169 0.1282 0.0069 0.0118 0.0088 75 MET A O 559 C CB . MET A 75 ? 0.1299 0.1231 0.1369 -0.0028 -0.0012 0.0035 75 MET A CB 560 C CG . MET A 75 ? 0.1300 0.1400 0.1366 0.0076 0.0047 0.0021 75 MET A CG 561 S SD . MET A 75 ? 0.1280 0.1446 0.1405 0.0212 0.0188 -0.0029 75 MET A SD 562 C CE . MET A 75 ? 0.1217 0.1352 0.1649 0.0048 -0.0011 -0.0124 75 MET A CE 563 N N . GLU A 76 ? 0.1226 0.1245 0.1087 -0.0061 0.0004 0.0034 76 GLU A N 564 C CA . GLU A 76 ? 0.1266 0.1263 0.1244 -0.0031 -0.0089 -0.0003 76 GLU A CA 565 C C . GLU A 76 ? 0.1361 0.1295 0.1259 -0.0006 -0.0074 -0.0039 76 GLU A C 566 O O . GLU A 76 ? 0.1323 0.1349 0.1448 0.0189 0.0063 0.0140 76 GLU A O 567 C CB . GLU A 76 ? 0.1366 0.1459 0.1254 0.0016 -0.0073 0.0029 76 GLU A CB 568 C CG . GLU A 76 ? 0.1258 0.1332 0.1407 0.0034 -0.0063 -0.0024 76 GLU A CG 569 C CD . GLU A 76 ? 0.1683 0.1239 0.1406 0.0102 0.0157 -0.0010 76 GLU A CD 570 O OE1 . GLU A 76 ? 0.1114 0.1582 0.1585 -0.0071 -0.0063 0.0226 76 GLU A OE1 571 O OE2 . GLU A 76 ? 0.1550 0.1773 0.1983 0.0013 -0.0017 0.0258 76 GLU A OE2 572 N N . GLY A 77 ? 0.1239 0.1163 0.1320 0.0055 -0.0096 0.0005 77 GLY A N 573 C CA . GLY A 77 ? 0.1253 0.1154 0.1304 -0.0055 -0.0017 0.0033 77 GLY A CA 574 C C . GLY A 77 ? 0.1255 0.1260 0.1240 0.0007 0.0002 -0.0016 77 GLY A C 575 O O . GLY A 77 ? 0.1147 0.1277 0.1343 0.0039 0.0049 -0.0118 77 GLY A O 576 N N . ILE A 78 ? 0.1247 0.1138 0.1350 -0.0041 0.0007 -0.0041 78 ILE A N 577 C CA . ILE A 78 ? 0.1250 0.1223 0.1342 -0.0029 0.0018 0.0022 78 ILE A CA 578 C C . ILE A 78 ? 0.1293 0.1224 0.1362 0.0024 0.0051 0.0037 78 ILE A C 579 O O . ILE A 78 ? 0.1426 0.1332 0.1323 -0.0086 0.0092 0.0159 78 ILE A O 580 C CB . ILE A 78 ? 0.1156 0.1233 0.1401 -0.0020 -0.0030 -0.0046 78 ILE A CB 581 C CG1 . ILE A 78 ? 0.1432 0.1092 0.1555 0.0022 -0.0096 0.0053 78 ILE A CG1 582 C CG2 . ILE A 78 ? 0.1248 0.1278 0.1418 -0.0006 -0.0078 -0.0086 78 ILE A CG2 583 C CD1 . ILE A 78 ? 0.1213 0.1251 0.1530 0.0001 -0.0089 0.0106 78 ILE A CD1 584 N N . PRO A 79 ? 0.1287 0.1294 0.1463 -0.0031 0.0010 0.0055 79 PRO A N 585 C CA . PRO A 79 ? 0.1317 0.1273 0.1491 -0.0023 -0.0018 0.0000 79 PRO A CA 586 C C . PRO A 79 ? 0.1413 0.1402 0.1567 -0.0041 -0.0009 -0.0026 79 PRO A C 587 O O . PRO A 79 ? 0.1621 0.1562 0.1830 -0.0175 -0.0054 0.0111 79 PRO A O 588 C CB . PRO A 79 ? 0.1593 0.1367 0.1680 0.0051 -0.0092 0.0086 79 PRO A CB 589 C CG . PRO A 79 ? 0.1371 0.1404 0.1786 -0.0118 -0.0081 -0.0132 79 PRO A CG 590 C CD . PRO A 79 ? 0.1417 0.1402 0.1590 -0.0101 -0.0012 0.0001 79 PRO A CD 591 N N . ASP A 80 ? 0.1390 0.1350 0.1563 -0.0051 -0.0092 -0.0063 80 ASP A N 592 C CA . ASP A 80 ? 0.1347 0.1276 0.1509 -0.0015 -0.0067 -0.0084 80 ASP A CA 593 C C . ASP A 80 ? 0.1178 0.1206 0.1359 0.0004 -0.0071 -0.0027 80 ASP A C 594 O O . ASP A 80 ? 0.1278 0.1212 0.1528 0.0028 -0.0144 -0.0163 80 ASP A O 595 C CB . ASP A 80 ? 0.1393 0.1343 0.1591 0.0002 -0.0125 -0.0148 80 ASP A CB 596 C CG . ASP A 80 ? 0.1520 0.1590 0.1767 0.0034 -0.0099 -0.0182 80 ASP A CG 597 O OD1 . ASP A 80 ? 0.1371 0.1621 0.2154 -0.0125 -0.0224 -0.0251 80 ASP A OD1 598 O OD2 . ASP A 80 ? 0.1992 0.1659 0.2045 -0.0050 -0.0284 -0.0271 80 ASP A OD2 599 N N . TYR A 81 ? 0.1221 0.1308 0.1331 -0.0017 -0.0004 0.0023 81 TYR A N 600 C CA . TYR A 81 ? 0.1291 0.1225 0.1334 0.0018 -0.0025 -0.0064 81 TYR A CA 601 C C . TYR A 81 ? 0.1318 0.1219 0.1380 0.0016 -0.0026 -0.0061 81 TYR A C 602 O O . TYR A 81 ? 0.1245 0.1234 0.1416 0.0043 -0.0025 -0.0046 81 TYR A O 603 C CB . TYR A 81 ? 0.1208 0.1185 0.1298 -0.0034 0.0043 -0.0107 81 TYR A CB 604 C CG . TYR A 81 ? 0.1246 0.1276 0.1263 0.0051 -0.0107 -0.0020 81 TYR A CG 605 C CD1 . TYR A 81 ? 0.1268 0.1132 0.1379 0.0051 0.0026 -0.0007 81 TYR A CD1 606 C CD2 . TYR A 81 ? 0.1153 0.0996 0.1281 -0.0006 -0.0055 0.0087 81 TYR A CD2 607 C CE1 . TYR A 81 ? 0.1184 0.1114 0.1417 0.0009 0.0014 0.0010 81 TYR A CE1 608 C CE2 . TYR A 81 ? 0.1111 0.1168 0.1306 -0.0009 -0.0151 -0.0031 81 TYR A CE2 609 C CZ . TYR A 81 ? 0.1062 0.1003 0.1184 0.0017 -0.0030 -0.0086 81 TYR A CZ 610 O OH . TYR A 81 ? 0.1196 0.0962 0.1191 -0.0058 -0.0064 -0.0113 81 TYR A OH 611 N N . SER A 82 ? 0.1274 0.1115 0.1443 0.0005 -0.0056 0.0044 82 SER A N 612 C CA . SER A 82 ? 0.1252 0.1278 0.1495 0.0010 -0.0140 -0.0030 82 SER A CA 613 C C . SER A 82 ? 0.1335 0.1264 0.1519 0.0018 -0.0197 -0.0008 82 SER A C 614 O O . SER A 82 ? 0.1537 0.1372 0.1515 0.0130 -0.0211 -0.0070 82 SER A O 615 C CB . SER A 82 ? 0.1298 0.1308 0.1589 -0.0034 -0.0170 -0.0093 82 SER A CB 616 O OG . SER A 82 ? 0.1470 0.1328 0.1915 -0.0011 -0.0153 -0.0020 82 SER A OG 617 N N . GLN A 83 ? 0.1242 0.1342 0.1417 0.0099 -0.0061 0.0006 83 GLN A N 618 C CA . GLN A 83 ? 0.1388 0.1479 0.1480 0.0046 -0.0044 -0.0049 83 GLN A CA 619 C C . GLN A 83 ? 0.1380 0.1493 0.1402 0.0062 0.0000 -0.0030 83 GLN A C 620 O O . GLN A 83 ? 0.1704 0.1579 0.1536 0.0064 -0.0008 -0.0155 83 GLN A O 621 C CB . GLN A 83 ? 0.1571 0.1626 0.1680 0.0073 -0.0021 -0.0018 83 GLN A CB 622 C CG . GLN A 83 ? 0.1994 0.1677 0.1801 0.0116 -0.0058 -0.0123 83 GLN A CG 623 C CD . GLN A 83 ? 0.2377 0.1897 0.2043 -0.0013 -0.0052 -0.0016 83 GLN A CD 624 O OE1 . GLN A 83 ? 0.3117 0.2052 0.2098 0.0095 -0.0091 -0.0072 83 GLN A OE1 625 N NE2 . GLN A 83 ? 0.2608 0.2302 0.2645 -0.0264 0.0005 0.0022 83 GLN A NE2 626 N N . TYR A 84 ? 0.1188 0.1264 0.1236 0.0019 -0.0060 -0.0085 84 TYR A N 627 C CA . TYR A 84 ? 0.1258 0.1321 0.1287 0.0000 -0.0018 -0.0062 84 TYR A CA 628 C C . TYR A 84 ? 0.1235 0.1262 0.1285 -0.0010 0.0006 -0.0054 84 TYR A C 629 O O . TYR A 84 ? 0.1408 0.1143 0.1364 -0.0008 -0.0036 -0.0117 84 TYR A O 630 C CB . TYR A 84 ? 0.1268 0.1249 0.1193 0.0004 -0.0036 -0.0044 84 TYR A CB 631 C CG . TYR A 84 ? 0.1306 0.1309 0.1363 -0.0002 0.0093 -0.0082 84 TYR A CG 632 C CD1 . TYR A 84 ? 0.1362 0.1507 0.1641 -0.0013 0.0003 0.0143 84 TYR A CD1 633 C CD2 . TYR A 84 ? 0.1554 0.1293 0.1542 -0.0074 0.0168 -0.0198 84 TYR A CD2 634 C CE1 . TYR A 84 ? 0.1586 0.1503 0.1684 0.0135 -0.0013 0.0118 84 TYR A CE1 635 C CE2 . TYR A 84 ? 0.1392 0.1529 0.1645 0.0020 -0.0049 0.0060 84 TYR A CE2 636 C CZ . TYR A 84 ? 0.1364 0.1468 0.1528 0.0042 0.0005 -0.0109 84 TYR A CZ 637 O OH . TYR A 84 ? 0.1623 0.1984 0.1603 0.0332 0.0016 -0.0201 84 TYR A OH 638 N N . GLY A 85 ? 0.1207 0.1188 0.1293 -0.0011 -0.0054 -0.0125 85 GLY A N 639 C CA . GLY A 85 ? 0.1174 0.1203 0.1246 0.0013 -0.0049 -0.0060 85 GLY A CA 640 C C . GLY A 85 ? 0.1338 0.1224 0.1305 0.0037 -0.0041 -0.0049 85 GLY A C 641 O O . GLY A 85 ? 0.1200 0.1058 0.1252 0.0052 0.0068 0.0032 85 GLY A O 642 N N . VAL A 86 ? 0.1278 0.1119 0.1316 0.0119 -0.0055 -0.0033 86 VAL A N 643 C CA . VAL A 86 ? 0.1252 0.1218 0.1274 -0.0003 -0.0040 0.0010 86 VAL A CA 644 C C . VAL A 86 ? 0.1290 0.1231 0.1361 0.0052 0.0029 0.0021 86 VAL A C 645 O O . VAL A 86 ? 0.1225 0.1154 0.1416 0.0092 -0.0054 0.0038 86 VAL A O 646 C CB . VAL A 86 ? 0.1273 0.1170 0.1171 0.0005 -0.0036 -0.0041 86 VAL A CB 647 C CG1 . VAL A 86 ? 0.1205 0.1289 0.1256 -0.0035 -0.0029 -0.0075 86 VAL A CG1 648 C CG2 . VAL A 86 ? 0.1450 0.1355 0.1263 0.0035 0.0005 0.0003 86 VAL A CG2 649 N N . THR A 87 ? 0.1202 0.1173 0.1254 -0.0065 0.0083 -0.0080 87 THR A N 650 C CA . THR A 87 ? 0.1172 0.1165 0.1262 -0.0079 -0.0069 -0.0031 87 THR A CA 651 C C . THR A 87 ? 0.1121 0.1194 0.1376 -0.0065 -0.0003 0.0030 87 THR A C 652 O O . THR A 87 ? 0.1218 0.1223 0.1365 0.0024 -0.0012 0.0014 87 THR A O 653 C CB . THR A 87 ? 0.1205 0.1121 0.1300 -0.0070 -0.0056 -0.0009 87 THR A CB 654 O OG1 . THR A 87 ? 0.1271 0.1436 0.1405 -0.0005 -0.0200 -0.0061 87 THR A OG1 655 C CG2 . THR A 87 ? 0.1251 0.1381 0.1349 0.0011 -0.0155 0.0013 87 THR A CG2 656 N N . THR A 88 ? 0.1154 0.1240 0.1294 -0.0059 -0.0016 -0.0029 88 THR A N 657 C CA . THR A 88 ? 0.1294 0.1284 0.1415 -0.0077 0.0034 -0.0042 88 THR A CA 658 C C . THR A 88 ? 0.1434 0.1336 0.1502 -0.0085 0.0051 -0.0038 88 THR A C 659 O O . THR A 88 ? 0.1671 0.1314 0.1821 -0.0056 0.0070 -0.0055 88 THR A O 660 C CB . THR A 88 ? 0.1387 0.1225 0.1436 -0.0009 0.0006 -0.0065 88 THR A CB 661 O OG1 . THR A 88 ? 0.1303 0.1373 0.1456 0.0022 -0.0021 -0.0033 88 THR A OG1 662 C CG2 . THR A 88 ? 0.1492 0.1423 0.1494 -0.0049 0.0068 -0.0060 88 THR A CG2 663 N N . ASN A 89 ? 0.1516 0.1353 0.1675 -0.0129 0.0144 -0.0131 89 ASN A N 664 C CA . ASN A 89 ? 0.1517 0.1438 0.1626 -0.0146 0.0069 -0.0008 89 ASN A CA 665 C C . ASN A 89 ? 0.1369 0.1447 0.1603 -0.0119 0.0077 -0.0010 89 ASN A C 666 O O . ASN A 89 ? 0.1543 0.1384 0.1590 -0.0132 -0.0010 0.0122 89 ASN A O 667 C CB . ASN A 89 ? 0.1703 0.1509 0.1561 -0.0185 0.0085 0.0000 89 ASN A CB 668 C CG . ASN A 89 ? 0.1821 0.2053 0.1947 -0.0227 -0.0047 0.0059 89 ASN A CG 669 O OD1 . ASN A 89 ? 0.2298 0.2323 0.2129 -0.0452 -0.0116 0.0172 89 ASN A OD1 670 N ND2 . ASN A 89 ? 0.2056 0.2918 0.2625 -0.0615 -0.0199 0.0097 89 ASN A ND2 671 N N . GLY A 90 ? 0.1476 0.1308 0.1691 -0.0122 0.0074 0.0023 90 GLY A N 672 C CA . GLY A 90 ? 0.1428 0.1404 0.1688 -0.0137 0.0058 0.0002 90 GLY A CA 673 C C . GLY A 90 ? 0.1313 0.1337 0.1638 -0.0087 0.0064 0.0046 90 GLY A C 674 O O . GLY A 90 ? 0.1174 0.1577 0.1766 -0.0063 0.0114 0.0054 90 GLY A O 675 N N . THR A 91 ? 0.1159 0.1263 0.1454 -0.0098 0.0074 0.0040 91 THR A N 676 C CA . THR A 91 ? 0.1225 0.1287 0.1419 -0.0095 0.0071 0.0008 91 THR A CA 677 C C . THR A 91 ? 0.1151 0.1316 0.1418 -0.0121 0.0102 -0.0011 91 THR A C 678 O O . THR A 91 ? 0.1027 0.1360 0.1392 -0.0191 0.0119 -0.0019 91 THR A O 679 C CB . THR A 91 ? 0.1351 0.1390 0.1403 -0.0055 0.0053 0.0048 91 THR A CB 680 O OG1 . THR A 91 ? 0.1115 0.1768 0.1329 -0.0213 0.0164 0.0128 91 THR A OG1 681 C CG2 . THR A 91 ? 0.1205 0.1507 0.1581 -0.0157 0.0237 0.0100 91 THR A CG2 682 N N . SER A 92 ? 0.1256 0.1215 0.1497 -0.0138 0.0061 0.0055 92 SER A N 683 C CA . SER A 92 ? 0.1327 0.1333 0.1449 -0.0032 0.0038 -0.0034 92 SER A CA 684 C C . SER A 92 ? 0.1255 0.1261 0.1371 0.0001 0.0034 0.0019 92 SER A C 685 O O . SER A 92 ? 0.1208 0.1303 0.1431 -0.0097 0.0038 0.0020 92 SER A O 686 C CB A SER A 92 ? 0.1284 0.1359 0.1450 0.0044 0.0000 -0.0041 92 SER A CB 687 C CB B SER A 92 ? 0.1481 0.1542 0.1554 -0.0012 -0.0017 -0.0013 92 SER A CB 688 O OG A SER A 92 ? 0.0678 0.1283 0.1196 0.0030 0.0061 -0.0175 92 SER A OG 689 O OG B SER A 92 ? 0.2074 0.1938 0.2243 0.0063 0.0026 -0.0042 92 SER A OG 690 N N . LEU A 93 ? 0.1110 0.1173 0.1228 -0.0026 0.0007 0.0012 93 LEU A N 691 C CA . LEU A 93 ? 0.1168 0.1136 0.1288 -0.0057 -0.0038 -0.0011 93 LEU A CA 692 C C . LEU A 93 ? 0.1041 0.1130 0.1245 -0.0075 0.0019 -0.0024 93 LEU A C 693 O O . LEU A 93 ? 0.1206 0.1201 0.1250 0.0058 -0.0033 0.0028 93 LEU A O 694 C CB . LEU A 93 ? 0.1153 0.1218 0.1371 -0.0091 -0.0044 -0.0014 93 LEU A CB 695 C CG . LEU A 93 ? 0.1325 0.1097 0.1208 -0.0083 0.0075 -0.0015 93 LEU A CG 696 C CD1 . LEU A 93 ? 0.1366 0.1185 0.1184 0.0042 0.0019 -0.0152 93 LEU A CD1 697 C CD2 . LEU A 93 ? 0.1484 0.1240 0.1472 -0.0205 -0.0037 -0.0020 93 LEU A CD2 698 N N . ARG A 94 ? 0.1120 0.1153 0.1209 -0.0049 -0.0038 -0.0053 94 ARG A N 699 C CA . ARG A 94 ? 0.1133 0.1210 0.1307 -0.0044 -0.0012 -0.0022 94 ARG A CA 700 C C . ARG A 94 ? 0.1097 0.1248 0.1208 -0.0011 0.0002 -0.0023 94 ARG A C 701 O O . ARG A 94 ? 0.1083 0.1210 0.1316 -0.0015 0.0009 0.0036 94 ARG A O 702 C CB . ARG A 94 ? 0.1122 0.1285 0.1303 0.0003 0.0056 -0.0096 94 ARG A CB 703 C CG . ARG A 94 ? 0.1299 0.1225 0.1336 0.0031 0.0002 -0.0033 94 ARG A CG 704 C CD . ARG A 94 ? 0.1473 0.1359 0.1477 -0.0019 -0.0063 -0.0058 94 ARG A CD 705 N NE . ARG A 94 ? 0.1621 0.1411 0.1668 -0.0023 -0.0146 -0.0298 94 ARG A NE 706 C CZ . ARG A 94 ? 0.2089 0.1697 0.1898 -0.0019 -0.0223 -0.0179 94 ARG A CZ 707 N NH1 . ARG A 94 ? 0.2302 0.1850 0.1815 -0.0039 -0.0275 -0.0217 94 ARG A NH1 708 N NH2 . ARG A 94 ? 0.2149 0.1646 0.1910 0.0121 -0.0111 -0.0232 94 ARG A NH2 709 N N . LEU A 95 ? 0.0981 0.1195 0.1315 0.0048 0.0019 -0.0069 95 LEU A N 710 C CA . LEU A 95 ? 0.1064 0.1191 0.1277 0.0000 -0.0004 -0.0099 95 LEU A CA 711 C C . LEU A 95 ? 0.1203 0.1246 0.1301 0.0014 -0.0004 -0.0058 95 LEU A C 712 O O . LEU A 95 ? 0.1342 0.1202 0.1255 0.0054 -0.0058 -0.0128 95 LEU A O 713 C CB . LEU A 95 ? 0.1099 0.1122 0.1292 -0.0003 0.0015 -0.0086 95 LEU A CB 714 C CG . LEU A 95 ? 0.1207 0.1231 0.1225 -0.0180 0.0053 -0.0038 95 LEU A CG 715 C CD1 . LEU A 95 ? 0.1276 0.1269 0.1406 0.0000 -0.0033 -0.0119 95 LEU A CD1 716 C CD2 . LEU A 95 ? 0.1348 0.1351 0.1387 -0.0211 -0.0099 -0.0069 95 LEU A CD2 717 N N . GLN A 96 ? 0.1126 0.1206 0.1249 0.0041 -0.0099 -0.0115 96 GLN A N 718 C CA . GLN A 96 ? 0.1291 0.1216 0.1216 0.0054 -0.0071 -0.0054 96 GLN A CA 719 C C . GLN A 96 ? 0.1191 0.1147 0.1110 0.0080 -0.0071 -0.0097 96 GLN A C 720 O O . GLN A 96 ? 0.1176 0.1349 0.1189 0.0066 -0.0128 -0.0118 96 GLN A O 721 C CB . GLN A 96 ? 0.1344 0.1370 0.1225 -0.0003 -0.0048 -0.0068 96 GLN A CB 722 C CG . GLN A 96 ? 0.1319 0.1310 0.1256 -0.0139 -0.0076 -0.0073 96 GLN A CG 723 C CD . GLN A 96 ? 0.1457 0.1260 0.1281 -0.0091 -0.0111 0.0011 96 GLN A CD 724 O OE1 . GLN A 96 ? 0.1706 0.1325 0.1356 0.0148 -0.0214 -0.0097 96 GLN A OE1 725 N NE2 . GLN A 96 ? 0.2265 0.1552 0.1591 -0.0156 -0.0276 -0.0265 96 GLN A NE2 726 N N . HIS A 97 ? 0.1235 0.1122 0.1187 0.0083 -0.0014 -0.0068 97 HIS A N 727 C CA . HIS A 97 ? 0.1317 0.1183 0.1191 0.0048 -0.0029 -0.0095 97 HIS A CA 728 C C . HIS A 97 ? 0.1177 0.1338 0.1266 -0.0008 0.0044 -0.0128 97 HIS A C 729 O O . HIS A 97 ? 0.1181 0.1351 0.1269 0.0095 -0.0075 -0.0155 97 HIS A O 730 C CB . HIS A 97 ? 0.1329 0.1161 0.1145 0.0105 -0.0037 -0.0083 97 HIS A CB 731 C CG . HIS A 97 ? 0.1324 0.1252 0.1153 0.0059 -0.0027 -0.0057 97 HIS A CG 732 N ND1 . HIS A 97 ? 0.1746 0.1594 0.1436 -0.0030 0.0147 -0.0029 97 HIS A ND1 733 C CD2 . HIS A 97 ? 0.1029 0.1067 0.0852 -0.0030 -0.0295 -0.0203 97 HIS A CD2 734 C CE1 . HIS A 97 ? 0.1006 0.1005 0.0727 0.0080 -0.0155 0.0077 97 HIS A CE1 735 N NE2 . HIS A 97 ? 0.1688 0.1804 0.1561 -0.0060 -0.0033 -0.0012 97 HIS A NE2 736 N N . ILE A 98 ? 0.1269 0.1419 0.1249 0.0037 -0.0057 -0.0171 98 ILE A N 737 C CA . ILE A 98 ? 0.1370 0.1380 0.1271 0.0017 -0.0030 -0.0051 98 ILE A CA 738 C C . ILE A 98 ? 0.1419 0.1412 0.1246 0.0006 -0.0010 -0.0037 98 ILE A C 739 O O . ILE A 98 ? 0.1537 0.1419 0.1501 -0.0012 -0.0110 -0.0002 98 ILE A O 740 C CB . ILE A 98 ? 0.1284 0.1516 0.1238 -0.0007 0.0002 -0.0088 98 ILE A CB 741 C CG1 . ILE A 98 ? 0.1368 0.1585 0.1390 0.0036 -0.0076 -0.0028 98 ILE A CG1 742 C CG2 . ILE A 98 ? 0.1316 0.1321 0.1356 0.0034 -0.0028 -0.0207 98 ILE A CG2 743 C CD1 . ILE A 98 ? 0.1570 0.1628 0.1404 -0.0004 -0.0115 0.0063 98 ILE A CD1 744 N N . LEU A 99 ? 0.1500 0.1410 0.1374 0.0000 -0.0001 -0.0050 99 LEU A N 745 C CA . LEU A 99 ? 0.1678 0.1656 0.1530 -0.0021 -0.0003 -0.0066 99 LEU A CA 746 C C . LEU A 99 ? 0.1738 0.1757 0.1764 -0.0006 -0.0072 -0.0099 99 LEU A C 747 O O . LEU A 99 ? 0.1622 0.1705 0.1493 0.0094 0.0003 -0.0307 99 LEU A O 748 C CB . LEU A 99 ? 0.1674 0.1666 0.1604 0.0005 0.0036 -0.0127 99 LEU A CB 749 C CG . LEU A 99 ? 0.1662 0.1638 0.1797 -0.0007 -0.0116 -0.0099 99 LEU A CG 750 C CD1 . LEU A 99 ? 0.1906 0.1765 0.1752 0.0136 0.0011 -0.0020 99 LEU A CD1 751 C CD2 . LEU A 99 ? 0.2077 0.2258 0.1933 0.0108 -0.0085 -0.0172 99 LEU A CD2 752 N N . PRO A 100 ? 0.1976 0.1892 0.1784 -0.0122 -0.0084 -0.0090 100 PRO A N 753 C CA . PRO A 100 ? 0.1990 0.1975 0.1842 -0.0093 -0.0054 -0.0094 100 PRO A CA 754 C C . PRO A 100 ? 0.2010 0.1899 0.1865 0.0000 -0.0071 -0.0101 100 PRO A C 755 O O . PRO A 100 ? 0.2207 0.2058 0.1963 0.0095 -0.0124 0.0034 100 PRO A O 756 C CB . PRO A 100 ? 0.2033 0.2135 0.2024 -0.0112 -0.0052 -0.0069 100 PRO A CB 757 C CG . PRO A 100 ? 0.2102 0.2185 0.2149 -0.0221 -0.0018 -0.0116 100 PRO A CG 758 C CD . PRO A 100 ? 0.2056 0.1967 0.2047 -0.0159 -0.0042 -0.0131 100 PRO A CD 759 N N . ASP A 101 ? 0.1978 0.1798 0.1786 -0.0031 0.0008 -0.0112 101 ASP A N 760 C CA . ASP A 101 ? 0.2041 0.1877 0.1861 0.0006 -0.0018 -0.0080 101 ASP A CA 761 C C . ASP A 101 ? 0.1914 0.1856 0.1832 0.0010 -0.0011 -0.0051 101 ASP A C 762 O O . ASP A 101 ? 0.2245 0.1764 0.1836 0.0066 0.0045 -0.0218 101 ASP A O 763 C CB . ASP A 101 ? 0.2245 0.1874 0.1998 0.0089 -0.0069 -0.0087 101 ASP A CB 764 C CG . ASP A 101 ? 0.2472 0.2177 0.2443 0.0013 -0.0307 -0.0020 101 ASP A CG 765 O OD1 . ASP A 101 ? 0.2328 0.2143 0.2245 0.0017 -0.0387 -0.0173 101 ASP A OD1 766 O OD2 . ASP A 101 ? 0.3757 0.2841 0.3017 -0.0219 -0.0439 0.0116 101 ASP A OD2 767 N N . GLY A 102 ? 0.1838 0.1844 0.1654 -0.0050 0.0007 -0.0117 102 GLY A N 768 C CA . GLY A 102 ? 0.1723 0.1766 0.1545 -0.0010 -0.0033 -0.0103 102 GLY A CA 769 C C . GLY A 102 ? 0.1648 0.1622 0.1549 -0.0025 0.0014 -0.0109 102 GLY A C 770 O O . GLY A 102 ? 0.1748 0.1740 0.1578 -0.0089 0.0094 -0.0090 102 GLY A O 771 N N . ARG A 103 ? 0.1727 0.1491 0.1451 -0.0040 0.0017 -0.0226 103 ARG A N 772 C CA . ARG A 103 ? 0.1526 0.1579 0.1567 0.0017 -0.0033 -0.0132 103 ARG A CA 773 C C . ARG A 103 ? 0.1434 0.1610 0.1406 -0.0014 -0.0035 -0.0200 103 ARG A C 774 O O . ARG A 103 ? 0.1339 0.1500 0.1361 0.0036 -0.0108 -0.0228 103 ARG A O 775 C CB . ARG A 103 ? 0.1734 0.1613 0.1497 0.0091 -0.0051 -0.0224 103 ARG A CB 776 C CG . ARG A 103 ? 0.1781 0.1609 0.1673 0.0058 -0.0069 -0.0210 103 ARG A CG 777 C CD . ARG A 103 ? 0.1751 0.1743 0.1789 0.0240 -0.0058 -0.0170 103 ARG A CD 778 N NE . ARG A 103 ? 0.2138 0.2105 0.1981 0.0089 -0.0083 -0.0004 103 ARG A NE 779 C CZ . ARG A 103 ? 0.2341 0.1950 0.2221 0.0015 0.0014 -0.0115 103 ARG A CZ 780 N NH1 . ARG A 103 ? 0.2806 0.2225 0.2148 0.0155 -0.0149 -0.0102 103 ARG A NH1 781 N NH2 . ARG A 103 ? 0.2585 0.2402 0.2282 0.0168 -0.0058 -0.0012 103 ARG A NH2 782 N N . VAL A 104 ? 0.1499 0.1482 0.1362 0.0002 0.0023 -0.0147 104 VAL A N 783 C CA . VAL A 104 ? 0.1346 0.1457 0.1406 0.0036 -0.0061 -0.0112 104 VAL A CA 784 C C . VAL A 104 ? 0.1383 0.1348 0.1385 0.0046 -0.0016 -0.0073 104 VAL A C 785 O O . VAL A 104 ? 0.1464 0.1478 0.1533 0.0026 -0.0112 -0.0120 104 VAL A O 786 C CB . VAL A 104 ? 0.1355 0.1556 0.1380 0.0100 -0.0120 -0.0112 104 VAL A CB 787 C CG1 . VAL A 104 ? 0.1676 0.1411 0.1548 0.0023 -0.0053 -0.0082 104 VAL A CG1 788 C CG2 . VAL A 104 ? 0.1450 0.1835 0.1396 -0.0019 -0.0020 0.0010 104 VAL A CG2 789 N N . PRO A 105 ? 0.1256 0.1240 0.1309 0.0018 -0.0021 -0.0046 105 PRO A N 790 C CA . PRO A 105 ? 0.1210 0.1224 0.1236 0.0081 -0.0033 -0.0055 105 PRO A CA 791 C C . PRO A 105 ? 0.1263 0.1217 0.1257 0.0003 -0.0064 0.0002 105 PRO A C 792 O O . PRO A 105 ? 0.1258 0.1308 0.1197 -0.0078 -0.0124 -0.0070 105 PRO A O 793 C CB . PRO A 105 ? 0.1307 0.1316 0.1270 0.0030 0.0010 -0.0090 105 PRO A CB 794 C CG . PRO A 105 ? 0.1387 0.1175 0.1260 0.0076 -0.0003 -0.0025 105 PRO A CG 795 C CD . PRO A 105 ? 0.1314 0.1200 0.1269 -0.0039 0.0025 -0.0130 105 PRO A CD 796 N N . SER A 106 ? 0.1201 0.1231 0.1249 0.0000 -0.0087 -0.0107 106 SER A N 797 C CA . SER A 106 ? 0.1214 0.1120 0.1244 0.0019 -0.0057 -0.0035 106 SER A CA 798 C C . SER A 106 ? 0.1207 0.1182 0.1184 -0.0081 -0.0042 0.0000 106 SER A C 799 O O . SER A 106 ? 0.1307 0.1030 0.1244 -0.0128 -0.0073 -0.0075 106 SER A O 800 C CB . SER A 106 ? 0.1164 0.1239 0.1263 0.0090 0.0005 -0.0055 106 SER A CB 801 O OG . SER A 106 ? 0.1254 0.1062 0.1234 -0.0084 -0.0003 -0.0089 106 SER A OG 802 N N . PRO A 107 ? 0.1169 0.1041 0.1068 -0.0033 -0.0100 -0.0012 107 PRO A N 803 C CA . PRO A 107 ? 0.1121 0.1098 0.1078 0.0035 -0.0101 -0.0033 107 PRO A CA 804 C C . PRO A 107 ? 0.1014 0.0997 0.1160 0.0069 -0.0071 -0.0049 107 PRO A C 805 O O . PRO A 107 ? 0.1027 0.1167 0.1234 0.0021 -0.0040 -0.0003 107 PRO A O 806 C CB . PRO A 107 ? 0.1065 0.1243 0.1151 0.0108 -0.0072 -0.0034 107 PRO A CB 807 C CG . PRO A 107 ? 0.1036 0.1096 0.1243 -0.0123 -0.0106 0.0009 107 PRO A CG 808 C CD . PRO A 107 ? 0.1229 0.1196 0.1161 -0.0044 -0.0033 -0.0080 107 PRO A CD 809 N N . ARG A 108 ? 0.0981 0.1015 0.1098 0.0037 -0.0117 -0.0073 108 ARG A N 810 C CA . ARG A 108 ? 0.0973 0.1012 0.1039 0.0034 -0.0020 -0.0047 108 ARG A CA 811 C C . ARG A 108 ? 0.0939 0.0993 0.1007 0.0095 -0.0061 -0.0091 108 ARG A C 812 O O . ARG A 108 ? 0.0879 0.1049 0.1155 0.0119 0.0034 -0.0085 108 ARG A O 813 C CB . ARG A 108 ? 0.0883 0.1040 0.1088 -0.0001 -0.0015 -0.0071 108 ARG A CB 814 C CG . ARG A 108 ? 0.1053 0.1202 0.1217 0.0031 -0.0035 -0.0078 108 ARG A CG 815 C CD . ARG A 108 ? 0.1149 0.1268 0.1263 -0.0015 -0.0077 0.0026 108 ARG A CD 816 N NE . ARG A 108 ? 0.1053 0.1257 0.1296 -0.0137 -0.0012 0.0009 108 ARG A NE 817 C CZ . ARG A 108 ? 0.1093 0.1334 0.1290 -0.0006 -0.0058 -0.0033 108 ARG A CZ 818 N NH1 . ARG A 108 ? 0.1134 0.1571 0.1333 0.0045 -0.0101 0.0069 108 ARG A NH1 819 N NH2 . ARG A 108 ? 0.0985 0.1394 0.1185 0.0134 -0.0167 0.0056 108 ARG A NH2 820 N N . VAL A 109 ? 0.0927 0.0948 0.0882 0.0106 -0.0082 -0.0090 109 VAL A N 821 C CA . VAL A 109 ? 0.0896 0.0942 0.0938 0.0072 -0.0033 -0.0043 109 VAL A CA 822 C C . VAL A 109 ? 0.0796 0.0986 0.0971 0.0013 -0.0066 -0.0031 109 VAL A C 823 O O . VAL A 109 ? 0.1098 0.0986 0.0933 0.0114 0.0021 0.0011 109 VAL A O 824 C CB . VAL A 109 ? 0.0936 0.0939 0.1058 0.0040 0.0023 0.0053 109 VAL A CB 825 C CG1 . VAL A 109 ? 0.1000 0.1259 0.1239 -0.0026 0.0012 0.0000 109 VAL A CG1 826 C CG2 . VAL A 109 ? 0.0903 0.0970 0.1080 0.0009 -0.0096 -0.0001 109 VAL A CG2 827 N N . TYR A 110 ? 0.0841 0.0952 0.1044 0.0027 -0.0026 0.0042 110 TYR A N 828 C CA . TYR A 110 ? 0.0850 0.0937 0.0887 0.0038 0.0067 -0.0030 110 TYR A CA 829 C C . TYR A 110 ? 0.0953 0.0909 0.0909 -0.0067 0.0044 -0.0040 110 TYR A C 830 O O . TYR A 110 ? 0.1080 0.0992 0.1048 0.0017 0.0206 -0.0057 110 TYR A O 831 C CB . TYR A 110 ? 0.0902 0.0993 0.0915 -0.0053 0.0020 -0.0038 110 TYR A CB 832 C CG . TYR A 110 ? 0.0860 0.0921 0.0769 0.0093 0.0083 -0.0080 110 TYR A CG 833 C CD1 . TYR A 110 ? 0.0853 0.0972 0.0935 0.0043 -0.0063 -0.0012 110 TYR A CD1 834 C CD2 . TYR A 110 ? 0.0958 0.0934 0.1004 0.0122 0.0038 0.0051 110 TYR A CD2 835 C CE1 . TYR A 110 ? 0.0983 0.1139 0.1033 0.0062 0.0073 0.0118 110 TYR A CE1 836 C CE2 . TYR A 110 ? 0.0945 0.1068 0.1139 0.0017 0.0070 -0.0002 110 TYR A CE2 837 C CZ . TYR A 110 ? 0.0924 0.1014 0.1014 0.0018 0.0070 0.0182 110 TYR A CZ 838 O OH . TYR A 110 ? 0.0978 0.1047 0.1123 -0.0166 0.0076 0.0095 110 TYR A OH 839 N N . LEU A 111 ? 0.0927 0.0954 0.0974 -0.0108 0.0043 -0.0056 111 LEU A N 840 C CA . LEU A 111 ? 0.0990 0.0978 0.1021 -0.0027 0.0040 0.0021 111 LEU A CA 841 C C . LEU A 111 ? 0.1012 0.1112 0.1050 -0.0032 0.0031 0.0014 111 LEU A C 842 O O . LEU A 111 ? 0.1037 0.1078 0.1253 -0.0043 0.0085 0.0044 111 LEU A O 843 C CB . LEU A 111 ? 0.1073 0.1131 0.1083 -0.0004 0.0051 0.0050 111 LEU A CB 844 C CG . LEU A 111 ? 0.1073 0.1127 0.1120 -0.0018 0.0002 0.0074 111 LEU A CG 845 C CD1 . LEU A 111 ? 0.1002 0.1153 0.1234 -0.0009 0.0161 0.0065 111 LEU A CD1 846 C CD2 . LEU A 111 ? 0.1237 0.1308 0.1257 -0.0073 0.0199 -0.0004 111 LEU A CD2 847 N N . LEU A 112 ? 0.1047 0.1056 0.1117 -0.0041 0.0056 0.0003 112 LEU A N 848 C CA . LEU A 112 ? 0.1088 0.1190 0.1151 -0.0003 0.0044 -0.0007 112 LEU A CA 849 C C . LEU A 112 ? 0.1219 0.1281 0.1260 -0.0049 0.0022 -0.0033 112 LEU A C 850 O O . LEU A 112 ? 0.1151 0.1250 0.1180 -0.0019 0.0056 -0.0029 112 LEU A O 851 C CB . LEU A 112 ? 0.1170 0.1265 0.1032 -0.0081 -0.0008 0.0043 112 LEU A CB 852 C CG . LEU A 112 ? 0.1278 0.1183 0.1197 0.0031 0.0114 0.0065 112 LEU A CG 853 C CD1 . LEU A 112 ? 0.1478 0.1077 0.1316 0.0151 0.0030 0.0159 112 LEU A CD1 854 C CD2 . LEU A 112 ? 0.1431 0.1154 0.1159 -0.0105 0.0024 0.0040 112 LEU A CD2 855 N N . ASP A 113 ? 0.1197 0.1217 0.1128 -0.0032 0.0037 0.0081 113 ASP A N 856 C CA . ASP A 113 ? 0.1237 0.1384 0.1244 0.0032 0.0035 0.0018 113 ASP A CA 857 C C . ASP A 113 ? 0.1364 0.1546 0.1382 -0.0053 0.0046 0.0007 113 ASP A C 858 O O . ASP A 113 ? 0.1347 0.1306 0.1386 -0.0133 0.0077 0.0055 113 ASP A O 859 C CB . ASP A 113 ? 0.1461 0.1413 0.1301 0.0029 0.0033 0.0092 113 ASP A CB 860 C CG . ASP A 113 ? 0.1669 0.1471 0.1311 -0.0028 0.0008 0.0016 113 ASP A CG 861 O OD1 . ASP A 113 ? 0.1379 0.1534 0.1258 -0.0034 0.0089 0.0072 113 ASP A OD1 862 O OD2 . ASP A 113 ? 0.1740 0.1915 0.1481 -0.0227 -0.0108 0.0160 113 ASP A OD2 863 N N . LYS A 114 ? 0.1448 0.1615 0.1440 -0.0056 0.0052 0.0082 114 LYS A N 864 C CA . LYS A 114 ? 0.1779 0.1817 0.1840 -0.0019 0.0072 0.0095 114 LYS A CA 865 C C . LYS A 114 ? 0.1869 0.1737 0.1806 -0.0017 0.0036 0.0110 114 LYS A C 866 O O . LYS A 114 ? 0.2308 0.1773 0.1894 -0.0127 -0.0111 0.0265 114 LYS A O 867 C CB . LYS A 114 ? 0.1777 0.2044 0.2129 -0.0032 0.0181 0.0132 114 LYS A CB 868 C CG . LYS A 114 ? 0.2192 0.2466 0.2286 -0.0030 0.0130 0.0180 114 LYS A CG 869 C CD . LYS A 114 ? 0.2398 0.2598 0.2342 0.0031 0.0178 0.0067 114 LYS A CD 870 C CE . LYS A 114 ? 0.2924 0.3196 0.2709 -0.0046 0.0086 0.0040 114 LYS A CE 871 N NZ . LYS A 114 ? 0.3134 0.3371 0.2750 0.0070 0.0327 0.0112 114 LYS A NZ 872 N N . THR A 115 ? 0.1663 0.1690 0.1555 0.0034 0.0025 0.0073 115 THR A N 873 C CA . THR A 115 ? 0.1749 0.1573 0.1608 0.0079 0.0034 0.0116 115 THR A CA 874 C C . THR A 115 ? 0.1559 0.1501 0.1512 0.0104 0.0069 0.0106 115 THR A C 875 O O . THR A 115 ? 0.1822 0.1399 0.1552 0.0122 0.0097 0.0185 115 THR A O 876 C CB . THR A 115 ? 0.1815 0.1609 0.1691 0.0035 0.0009 0.0155 115 THR A CB 877 O OG1 . THR A 115 ? 0.1494 0.1699 0.1756 -0.0008 -0.0005 0.0134 115 THR A OG1 878 C CG2 . THR A 115 ? 0.2022 0.2017 0.1885 0.0057 -0.0024 0.0141 115 THR A CG2 879 N N . LYS A 116 ? 0.1462 0.1232 0.1370 0.0125 0.0039 0.0142 116 LYS A N 880 C CA . LYS A 116 ? 0.1395 0.1398 0.1422 0.0039 0.0029 0.0039 116 LYS A CA 881 C C . LYS A 116 ? 0.1296 0.1391 0.1431 0.0045 0.0012 0.0076 116 LYS A C 882 O O . LYS A 116 ? 0.1508 0.1664 0.1501 0.0107 0.0062 0.0045 116 LYS A O 883 C CB . LYS A 116 ? 0.1400 0.1371 0.1426 0.0064 0.0086 0.0097 116 LYS A CB 884 C CG . LYS A 116 ? 0.1528 0.1594 0.1498 -0.0009 -0.0060 0.0043 116 LYS A CG 885 C CD . LYS A 116 ? 0.1558 0.1671 0.1522 -0.0040 0.0070 -0.0037 116 LYS A CD 886 C CE . LYS A 116 ? 0.1741 0.1785 0.1724 -0.0158 0.0166 -0.0057 116 LYS A CE 887 N NZ . LYS A 116 ? 0.1929 0.1657 0.1828 -0.0068 0.0067 0.0088 116 LYS A NZ 888 N N . ARG A 117 ? 0.1505 0.1563 0.1605 0.0053 0.0040 0.0107 117 ARG A N 889 C CA . ARG A 117 ? 0.1571 0.1669 0.1720 0.0007 0.0051 0.0025 117 ARG A CA 890 C C . ARG A 117 ? 0.1403 0.1413 0.1442 0.0031 0.0026 0.0079 117 ARG A C 891 O O . ARG A 117 ? 0.1575 0.1388 0.1781 0.0094 -0.0090 0.0094 117 ARG A O 892 C CB . ARG A 117 ? 0.1752 0.2070 0.1946 -0.0011 0.0012 0.0059 117 ARG A CB 893 C CG . ARG A 117 ? 0.2477 0.2485 0.2492 0.0123 -0.0019 -0.0001 117 ARG A CG 894 C CD . ARG A 117 ? 0.2879 0.2804 0.2968 0.0029 -0.0014 0.0103 117 ARG A CD 895 N NE . ARG A 117 ? 0.3034 0.2930 0.3378 0.0104 -0.0075 -0.0026 117 ARG A NE 896 C CZ . ARG A 117 ? 0.3494 0.3416 0.3634 -0.0008 -0.0031 -0.0111 117 ARG A CZ 897 N NH1 . ARG A 117 ? 0.3405 0.3498 0.3328 0.0140 0.0126 -0.0056 117 ARG A NH1 898 N NH2 . ARG A 117 ? 0.3557 0.3387 0.3521 0.0138 0.0024 -0.0059 117 ARG A NH2 899 N N . ARG A 118 ? 0.1325 0.1470 0.1470 -0.0011 0.0050 0.0052 118 ARG A N 900 C CA . ARG A 118 ? 0.1330 0.1396 0.1391 0.0042 0.0021 0.0027 118 ARG A CA 901 C C . ARG A 118 ? 0.1056 0.1203 0.1280 -0.0053 0.0032 0.0049 118 ARG A C 902 O O . ARG A 118 ? 0.0995 0.1283 0.1280 -0.0184 -0.0042 0.0100 118 ARG A O 903 C CB A ARG A 118 ? 0.1307 0.1449 0.1377 0.0001 0.0053 0.0019 118 ARG A CB 904 C CB B ARG A 118 ? 0.1375 0.1511 0.1406 0.0016 0.0066 0.0024 118 ARG A CB 905 C CG A ARG A 118 ? 0.1489 0.1622 0.1584 0.0095 0.0037 0.0012 118 ARG A CG 906 C CG B ARG A 118 ? 0.1753 0.1768 0.1681 0.0060 0.0080 -0.0004 118 ARG A CG 907 C CD A ARG A 118 ? 0.1572 0.1594 0.1626 0.0217 -0.0028 -0.0043 118 ARG A CD 908 C CD B ARG A 118 ? 0.2015 0.2086 0.1796 0.0060 0.0106 -0.0061 118 ARG A CD 909 N NE A ARG A 118 ? 0.1601 0.1941 0.1994 0.0000 -0.0016 0.0034 118 ARG A NE 910 N NE B ARG A 118 ? 0.2441 0.2664 0.2069 0.0052 -0.0008 -0.0121 118 ARG A NE 911 C CZ A ARG A 118 ? 0.2005 0.1909 0.1623 0.0061 -0.0038 0.0033 118 ARG A CZ 912 C CZ B ARG A 118 ? 0.2075 0.2361 0.1682 -0.0003 0.0042 -0.0096 118 ARG A CZ 913 N NH1 A ARG A 118 ? 0.2242 0.2278 0.2071 -0.0158 -0.0127 0.0074 118 ARG A NH1 914 N NH1 B ARG A 118 ? 0.1701 0.2114 0.1384 0.0031 -0.0003 -0.0066 118 ARG A NH1 915 N NH2 A ARG A 118 ? 0.1688 0.1395 0.1130 -0.0033 -0.0106 -0.0062 118 ARG A NH2 916 N NH2 B ARG A 118 ? 0.2516 0.2151 0.2217 0.0046 0.0168 0.0105 118 ARG A NH2 917 N N . TYR A 119 ? 0.0997 0.1215 0.1157 0.0005 0.0022 0.0031 119 TYR A N 918 C CA . TYR A 119 ? 0.1108 0.1117 0.1035 -0.0023 0.0006 0.0065 119 TYR A CA 919 C C . TYR A 119 ? 0.1140 0.1100 0.1091 -0.0049 -0.0015 0.0077 119 TYR A C 920 O O . TYR A 119 ? 0.1270 0.1167 0.1319 -0.0085 -0.0030 0.0033 119 TYR A O 921 C CB . TYR A 119 ? 0.1040 0.1115 0.0996 -0.0065 0.0061 0.0048 119 TYR A CB 922 C CG . TYR A 119 ? 0.1003 0.0873 0.0921 -0.0014 0.0060 0.0005 119 TYR A CG 923 C CD1 . TYR A 119 ? 0.1099 0.1109 0.1060 0.0004 0.0000 -0.0032 119 TYR A CD1 924 C CD2 . TYR A 119 ? 0.1077 0.0927 0.1059 0.0007 0.0088 0.0052 119 TYR A CD2 925 C CE1 . TYR A 119 ? 0.0804 0.1250 0.1063 0.0054 0.0004 -0.0033 119 TYR A CE1 926 C CE2 . TYR A 119 ? 0.0916 0.1024 0.0976 -0.0010 0.0045 0.0095 119 TYR A CE2 927 C CZ . TYR A 119 ? 0.0920 0.0892 0.0990 -0.0057 0.0214 -0.0009 119 TYR A CZ 928 O OH . TYR A 119 ? 0.1293 0.1191 0.1016 0.0076 0.0149 -0.0150 119 TYR A OH 929 N N . GLU A 120 ? 0.1126 0.1145 0.1144 -0.0099 0.0061 -0.0018 120 GLU A N 930 C CA . GLU A 120 ? 0.1259 0.1227 0.1127 -0.0021 0.0037 -0.0036 120 GLU A CA 931 C C . GLU A 120 ? 0.1381 0.1273 0.1153 -0.0037 -0.0011 0.0083 120 GLU A C 932 O O . GLU A 120 ? 0.2314 0.1364 0.1292 0.0125 -0.0282 0.0072 120 GLU A O 933 C CB . GLU A 120 ? 0.1282 0.1358 0.1203 -0.0018 0.0077 -0.0088 120 GLU A CB 934 C CG . GLU A 120 ? 0.1211 0.1365 0.1603 -0.0031 0.0121 -0.0287 120 GLU A CG 935 C CD . GLU A 120 ? 0.1638 0.1677 0.1835 -0.0231 0.0237 -0.0203 120 GLU A CD 936 O OE1 . GLU A 120 ? 0.1442 0.1830 0.1645 -0.0007 -0.0042 -0.0156 120 GLU A OE1 937 O OE2 . GLU A 120 ? 0.3098 0.2197 0.2051 -0.0585 0.0576 -0.0475 120 GLU A OE2 938 N N . MET A 121 ? 0.1321 0.1228 0.1199 -0.0036 -0.0009 0.0028 121 MET A N 939 C CA . MET A 121 ? 0.1194 0.1245 0.1233 0.0021 0.0024 0.0024 121 MET A CA 940 C C . MET A 121 ? 0.1284 0.1402 0.1308 0.0040 0.0099 0.0076 121 MET A C 941 O O . MET A 121 ? 0.1423 0.1492 0.1513 0.0154 0.0213 0.0083 121 MET A O 942 C CB . MET A 121 ? 0.1371 0.1314 0.1323 -0.0058 0.0001 0.0022 121 MET A CB 943 C CG . MET A 121 ? 0.1251 0.1143 0.1496 -0.0021 -0.0058 0.0024 121 MET A CG 944 S SD . MET A 121 ? 0.1334 0.1317 0.1421 0.0071 -0.0016 -0.0090 121 MET A SD 945 C CE . MET A 121 ? 0.1381 0.1184 0.1212 0.0178 -0.0050 -0.0015 121 MET A CE 946 N N . LEU A 122 ? 0.1150 0.1228 0.1187 0.0032 0.0055 0.0018 122 LEU A N 947 C CA . LEU A 122 ? 0.1224 0.1210 0.1261 0.0029 0.0127 -0.0016 122 LEU A CA 948 C C . LEU A 122 ? 0.1190 0.1251 0.1273 -0.0064 0.0133 -0.0052 122 LEU A C 949 O O . LEU A 122 ? 0.1233 0.1065 0.1263 -0.0126 0.0085 0.0074 122 LEU A O 950 C CB . LEU A 122 ? 0.1189 0.1215 0.1380 0.0085 0.0123 0.0002 122 LEU A CB 951 C CG . LEU A 122 ? 0.1535 0.1421 0.1477 0.0068 -0.0053 -0.0180 122 LEU A CG 952 C CD1 . LEU A 122 ? 0.1595 0.1927 0.1752 -0.0034 -0.0053 -0.0212 122 LEU A CD1 953 C CD2 . LEU A 122 ? 0.1782 0.1408 0.1635 0.0080 -0.0076 -0.0002 122 LEU A CD2 954 N N . HIS A 123 ? 0.1223 0.1181 0.1302 -0.0063 0.0144 -0.0089 123 HIS A N 955 C CA . HIS A 123 ? 0.1282 0.1236 0.1295 -0.0052 0.0089 -0.0041 123 HIS A CA 956 C C . HIS A 123 ? 0.1311 0.1206 0.1299 -0.0056 0.0145 -0.0064 123 HIS A C 957 O O . HIS A 123 ? 0.1689 0.1669 0.1485 0.0079 0.0267 -0.0010 123 HIS A O 958 C CB . HIS A 123 ? 0.1212 0.1304 0.1341 -0.0060 0.0156 -0.0060 123 HIS A CB 959 C CG . HIS A 123 ? 0.1428 0.1297 0.1326 -0.0036 -0.0074 0.0183 123 HIS A CG 960 N ND1 . HIS A 123 ? 0.1419 0.1581 0.1477 0.0049 -0.0067 -0.0013 123 HIS A ND1 961 C CD2 . HIS A 123 ? 0.1819 0.1476 0.1647 -0.0237 -0.0050 0.0134 123 HIS A CD2 962 C CE1 . HIS A 123 ? 0.1458 0.1681 0.1560 0.0039 -0.0031 0.0054 123 HIS A CE1 963 N NE2 . HIS A 123 ? 0.2183 0.1729 0.1744 0.0071 0.0044 -0.0030 123 HIS A NE2 964 N N . LEU A 124 ? 0.1299 0.1254 0.1380 -0.0075 0.0091 -0.0003 124 LEU A N 965 C CA . LEU A 124 ? 0.1262 0.1213 0.1429 -0.0064 0.0109 0.0000 124 LEU A CA 966 C C . LEU A 124 ? 0.1190 0.1189 0.1353 -0.0003 0.0065 -0.0029 124 LEU A C 967 O O . LEU A 124 ? 0.1044 0.1308 0.1238 -0.0011 0.0115 -0.0146 124 LEU A O 968 C CB . LEU A 124 ? 0.1178 0.1367 0.1623 -0.0084 0.0100 0.0013 124 LEU A CB 969 C CG . LEU A 124 ? 0.1302 0.1562 0.1751 -0.0002 0.0153 -0.0169 124 LEU A CG 970 C CD1 . LEU A 124 ? 0.1481 0.1882 0.1889 -0.0210 0.0206 -0.0217 124 LEU A CD1 971 C CD2 . LEU A 124 ? 0.1673 0.1565 0.1847 -0.0149 0.0054 -0.0143 124 LEU A CD2 972 N N . THR A 125 ? 0.1160 0.1356 0.1297 -0.0002 0.0056 -0.0057 125 THR A N 973 C CA . THR A 125 ? 0.1247 0.1299 0.1261 0.0000 0.0054 -0.0033 125 THR A CA 974 C C . THR A 125 ? 0.1242 0.1343 0.1179 0.0042 0.0014 -0.0093 125 THR A C 975 O O . THR A 125 ? 0.1448 0.1475 0.1446 0.0108 -0.0031 0.0111 125 THR A O 976 C CB . THR A 125 ? 0.1319 0.1305 0.1348 0.0054 0.0047 -0.0069 125 THR A CB 977 O OG1 . THR A 125 ? 0.1470 0.1634 0.1606 -0.0009 0.0147 -0.0079 125 THR A OG1 978 C CG2 . THR A 125 ? 0.1508 0.1429 0.1514 0.0010 -0.0022 -0.0092 125 THR A CG2 979 N N . GLY A 126 ? 0.1201 0.1311 0.1138 0.0037 0.0117 -0.0015 126 GLY A N 980 C CA . GLY A 126 ? 0.1330 0.1450 0.1265 -0.0036 0.0140 -0.0042 126 GLY A CA 981 C C . GLY A 126 ? 0.1458 0.1451 0.1335 -0.0061 0.0131 -0.0063 126 GLY A C 982 O O . GLY A 126 ? 0.1388 0.1777 0.1392 -0.0093 0.0351 -0.0147 126 GLY A O 983 N N . PHE A 127 ? 0.1293 0.1294 0.1290 -0.0035 0.0134 -0.0096 127 PHE A N 984 C CA . PHE A 127 ? 0.1363 0.1380 0.1341 -0.0023 0.0104 -0.0019 127 PHE A CA 985 C C . PHE A 127 ? 0.1266 0.1294 0.1335 -0.0054 0.0081 -0.0026 127 PHE A C 986 O O . PHE A 127 ? 0.1283 0.1179 0.1222 0.0007 0.0101 -0.0115 127 PHE A O 987 C CB . PHE A 127 ? 0.1379 0.1443 0.1466 -0.0015 0.0170 0.0011 127 PHE A CB 988 C CG . PHE A 127 ? 0.1421 0.1512 0.1510 -0.0024 0.0104 -0.0082 127 PHE A CG 989 C CD1 . PHE A 127 ? 0.1606 0.1787 0.1669 -0.0066 0.0051 0.0142 127 PHE A CD1 990 C CD2 . PHE A 127 ? 0.1337 0.1798 0.1627 0.0081 -0.0067 0.0008 127 PHE A CD2 991 C CE1 . PHE A 127 ? 0.1831 0.2162 0.1598 -0.0181 0.0196 0.0044 127 PHE A CE1 992 C CE2 . PHE A 127 ? 0.1743 0.1969 0.1724 0.0012 -0.0058 0.0031 127 PHE A CE2 993 C CZ . PHE A 127 ? 0.1860 0.2114 0.1579 0.0035 -0.0042 0.0036 127 PHE A CZ 994 N N . GLU A 128 ? 0.1345 0.1306 0.1285 -0.0126 0.0076 -0.0076 128 GLU A N 995 C CA . GLU A 128 ? 0.1377 0.1392 0.1417 -0.0016 0.0071 -0.0024 128 GLU A CA 996 C C . GLU A 128 ? 0.1256 0.1282 0.1346 -0.0094 0.0055 -0.0034 128 GLU A C 997 O O . GLU A 128 ? 0.1324 0.1452 0.1278 -0.0105 0.0114 -0.0039 128 GLU A O 998 C CB . GLU A 128 ? 0.1666 0.1691 0.1736 0.0020 -0.0059 -0.0074 128 GLU A CB 999 C CG . GLU A 128 ? 0.1699 0.1663 0.1912 0.0063 0.0303 -0.0060 128 GLU A CG 1000 C CD . GLU A 128 ? 0.1534 0.1559 0.1846 -0.0056 0.0227 -0.0037 128 GLU A CD 1001 O OE1 . GLU A 128 ? 0.1672 0.1590 0.1825 0.0029 0.0322 -0.0112 128 GLU A OE1 1002 O OE2 . GLU A 128 ? 0.1506 0.1488 0.1617 -0.0056 0.0374 -0.0181 128 GLU A OE2 1003 N N . PHE A 129 ? 0.1217 0.1222 0.1257 -0.0116 0.0034 -0.0057 129 PHE A N 1004 C CA . PHE A 129 ? 0.1272 0.1203 0.1286 -0.0005 0.0057 0.0025 129 PHE A CA 1005 C C . PHE A 129 ? 0.1123 0.1215 0.1279 -0.0072 0.0100 -0.0022 129 PHE A C 1006 O O . PHE A 129 ? 0.1121 0.1279 0.1389 0.0068 0.0017 -0.0058 129 PHE A O 1007 C CB . PHE A 129 ? 0.1307 0.1282 0.1310 -0.0006 0.0056 -0.0002 129 PHE A CB 1008 C CG . PHE A 129 ? 0.1147 0.1194 0.1223 0.0051 0.0137 -0.0029 129 PHE A CG 1009 C CD1 . PHE A 129 ? 0.1043 0.1315 0.1319 0.0133 0.0117 0.0076 129 PHE A CD1 1010 C CD2 . PHE A 129 ? 0.1373 0.1315 0.1095 -0.0097 0.0034 0.0011 129 PHE A CD2 1011 C CE1 . PHE A 129 ? 0.1473 0.1500 0.1243 -0.0066 0.0084 -0.0119 129 PHE A CE1 1012 C CE2 . PHE A 129 ? 0.1345 0.1384 0.1273 0.0148 0.0081 0.0146 129 PHE A CE2 1013 C CZ . PHE A 129 ? 0.1395 0.1116 0.1447 -0.0110 0.0225 -0.0011 129 PHE A CZ 1014 N N . THR A 130 ? 0.1238 0.1279 0.1350 0.0020 0.0096 -0.0004 130 THR A N 1015 C CA . THR A 130 ? 0.1246 0.1268 0.1280 -0.0014 0.0100 -0.0079 130 THR A CA 1016 C C . THR A 130 ? 0.1166 0.1268 0.1254 -0.0037 0.0068 -0.0011 130 THR A C 1017 O O . THR A 130 ? 0.1206 0.1333 0.1308 -0.0109 0.0007 0.0107 130 THR A O 1018 C CB . THR A 130 ? 0.1385 0.1339 0.1433 -0.0043 0.0022 -0.0025 130 THR A CB 1019 O OG1 . THR A 130 ? 0.1356 0.1189 0.1522 -0.0037 0.0245 -0.0070 130 THR A OG1 1020 C CG2 . THR A 130 ? 0.1323 0.1353 0.1460 0.0110 0.0109 -0.0140 130 THR A CG2 1021 N N . PHE A 131 ? 0.1076 0.1242 0.1142 -0.0062 0.0058 -0.0042 131 PHE A N 1022 C CA . PHE A 131 ? 0.1112 0.1216 0.1226 0.0021 0.0030 -0.0034 131 PHE A CA 1023 C C . PHE A 131 ? 0.1097 0.1149 0.1253 0.0017 0.0016 0.0017 131 PHE A C 1024 O O . PHE A 131 ? 0.1034 0.1143 0.1477 -0.0075 0.0027 -0.0079 131 PHE A O 1025 C CB . PHE A 131 ? 0.1145 0.1182 0.1251 -0.0033 0.0010 -0.0026 131 PHE A CB 1026 C CG . PHE A 131 ? 0.0907 0.1235 0.1098 -0.0110 0.0089 -0.0026 131 PHE A CG 1027 C CD1 . PHE A 131 ? 0.0918 0.1232 0.1096 0.0070 -0.0008 -0.0127 131 PHE A CD1 1028 C CD2 . PHE A 131 ? 0.1205 0.1205 0.1230 -0.0079 0.0027 -0.0034 131 PHE A CD2 1029 C CE1 . PHE A 131 ? 0.0922 0.1179 0.1344 0.0000 0.0118 -0.0138 131 PHE A CE1 1030 C CE2 . PHE A 131 ? 0.1104 0.1347 0.1178 -0.0134 -0.0040 -0.0057 131 PHE A CE2 1031 C CZ . PHE A 131 ? 0.1005 0.1177 0.1383 0.0148 -0.0030 0.0007 131 PHE A CZ 1032 N N . ASP A 132 ? 0.1109 0.1230 0.1308 -0.0047 0.0008 -0.0029 132 ASP A N 1033 C CA . ASP A 132 ? 0.1204 0.1232 0.1401 -0.0046 -0.0001 -0.0032 132 ASP A CA 1034 C C . ASP A 132 ? 0.1096 0.1283 0.1271 0.0014 -0.0021 0.0017 132 ASP A C 1035 O O . ASP A 132 ? 0.1120 0.1204 0.1390 -0.0048 0.0042 -0.0056 132 ASP A O 1036 C CB . ASP A 132 ? 0.1025 0.1193 0.1437 -0.0145 0.0009 -0.0034 132 ASP A CB 1037 C CG . ASP A 132 ? 0.1328 0.1578 0.1805 -0.0007 0.0102 -0.0068 132 ASP A CG 1038 O OD1 . ASP A 132 ? 0.1173 0.1770 0.1970 -0.0059 0.0268 -0.0177 132 ASP A OD1 1039 O OD2 . ASP A 132 ? 0.1683 0.1785 0.1892 -0.0147 0.0289 0.0181 132 ASP A OD2 1040 N N . VAL A 133 ? 0.1149 0.1317 0.1269 -0.0037 -0.0006 -0.0048 133 VAL A N 1041 C CA . VAL A 133 ? 0.1166 0.1277 0.1295 -0.0001 -0.0005 -0.0041 133 VAL A CA 1042 C C . VAL A 133 ? 0.1139 0.1379 0.1323 0.0003 -0.0034 -0.0084 133 VAL A C 1043 O O . VAL A 133 ? 0.1297 0.1473 0.1521 0.0048 -0.0115 -0.0124 133 VAL A O 1044 C CB . VAL A 133 ? 0.1194 0.1287 0.1339 -0.0008 -0.0042 0.0022 133 VAL A CB 1045 C CG1 . VAL A 133 ? 0.1237 0.1232 0.1412 -0.0093 0.0036 -0.0100 133 VAL A CG1 1046 C CG2 . VAL A 133 ? 0.1216 0.1327 0.1468 -0.0044 -0.0047 0.0084 133 VAL A CG2 1047 N N . ASP A 134 ? 0.1346 0.1497 0.1497 0.0014 -0.0095 -0.0084 134 ASP A N 1048 C CA . ASP A 134 ? 0.1429 0.1541 0.1552 -0.0019 -0.0051 -0.0051 134 ASP A CA 1049 C C . ASP A 134 ? 0.1364 0.1384 0.1415 -0.0017 -0.0022 -0.0130 134 ASP A C 1050 O O . ASP A 134 ? 0.1308 0.1448 0.1288 -0.0014 0.0034 -0.0173 134 ASP A O 1051 C CB . ASP A 134 ? 0.1518 0.1608 0.1617 -0.0004 -0.0027 -0.0115 134 ASP A CB 1052 C CG . ASP A 134 ? 0.1851 0.1764 0.1863 -0.0161 -0.0217 -0.0003 134 ASP A CG 1053 O OD1 . ASP A 134 ? 0.2030 0.1683 0.1750 -0.0316 -0.0213 -0.0121 134 ASP A OD1 1054 O OD2 . ASP A 134 ? 0.3094 0.2321 0.2852 -0.0676 -0.0218 -0.0077 134 ASP A OD2 1055 N N . ALA A 135 ? 0.1277 0.1320 0.1419 -0.0016 0.0002 -0.0128 135 ALA A N 1056 C CA . ALA A 135 ? 0.1250 0.1395 0.1501 0.0035 0.0024 -0.0059 135 ALA A CA 1057 C C . ALA A 135 ? 0.1124 0.1441 0.1475 0.0033 -0.0019 -0.0027 135 ALA A C 1058 O O . ALA A 135 ? 0.1154 0.1421 0.1508 0.0098 -0.0126 -0.0076 135 ALA A O 1059 C CB . ALA A 135 ? 0.1310 0.1420 0.1613 -0.0105 0.0057 -0.0108 135 ALA A CB 1060 N N . THR A 136 ? 0.1330 0.1473 0.1495 -0.0034 -0.0082 0.0038 136 THR A N 1061 C CA . THR A 136 ? 0.1442 0.1661 0.1646 0.0015 -0.0063 -0.0056 136 THR A CA 1062 C C . THR A 136 ? 0.1497 0.1615 0.1446 0.0044 -0.0068 -0.0050 136 THR A C 1063 O O . THR A 136 ? 0.1548 0.1752 0.1632 0.0079 -0.0109 -0.0147 136 THR A O 1064 C CB . THR A 136 ? 0.1483 0.1842 0.1718 -0.0006 -0.0075 0.0028 136 THR A CB 1065 O OG1 . THR A 136 ? 0.1884 0.1802 0.2310 -0.0058 -0.0020 -0.0129 136 THR A OG1 1066 C CG2 . THR A 136 ? 0.1641 0.2050 0.1987 0.0072 0.0053 0.0016 136 THR A CG2 1067 N N . LYS A 137 ? 0.1428 0.1682 0.1473 -0.0009 -0.0048 -0.0021 137 LYS A N 1068 C CA . LYS A 137 ? 0.1470 0.1593 0.1556 -0.0029 -0.0091 -0.0032 137 LYS A CA 1069 C C . LYS A 137 ? 0.1243 0.1318 0.1375 -0.0013 -0.0106 -0.0030 137 LYS A C 1070 O O . LYS A 137 ? 0.1449 0.1298 0.1488 -0.0094 -0.0053 -0.0034 137 LYS A O 1071 C CB . LYS A 137 ? 0.1481 0.1560 0.1568 -0.0004 -0.0162 -0.0134 137 LYS A CB 1072 C CG . LYS A 137 ? 0.1801 0.1903 0.2170 -0.0073 -0.0014 -0.0058 137 LYS A CG 1073 C CD . LYS A 137 ? 0.1970 0.2058 0.2418 -0.0079 -0.0153 0.0003 137 LYS A CD 1074 C CE . LYS A 137 ? 0.2595 0.2507 0.2560 -0.0065 -0.0072 -0.0022 137 LYS A CE 1075 N NZ . LYS A 137 ? 0.3334 0.2549 0.2730 0.0128 -0.0108 -0.0076 137 LYS A NZ 1076 N N . LEU A 138 ? 0.1320 0.1354 0.1467 0.0039 -0.0134 -0.0038 138 LEU A N 1077 C CA . LEU A 138 ? 0.1280 0.1322 0.1330 0.0033 -0.0078 -0.0023 138 LEU A CA 1078 C C . LEU A 138 ? 0.1279 0.1294 0.1336 0.0046 -0.0130 -0.0064 138 LEU A C 1079 O O . LEU A 138 ? 0.1363 0.1349 0.1419 0.0053 -0.0202 -0.0179 138 LEU A O 1080 C CB . LEU A 138 ? 0.1130 0.1283 0.1294 -0.0018 -0.0021 -0.0102 138 LEU A CB 1081 C CG . LEU A 138 ? 0.1252 0.1378 0.1255 0.0014 -0.0029 -0.0125 138 LEU A CG 1082 C CD1 . LEU A 138 ? 0.1422 0.1436 0.1190 0.0119 -0.0082 -0.0104 138 LEU A CD1 1083 C CD2 . LEU A 138 ? 0.1437 0.1401 0.1464 0.0056 0.0052 -0.0119 138 LEU A CD2 1084 N N . PRO A 139 ? 0.1330 0.1322 0.1357 0.0069 -0.0117 -0.0070 139 PRO A N 1085 C CA . PRO A 139 ? 0.1414 0.1389 0.1320 0.0020 -0.0070 -0.0053 139 PRO A CA 1086 C C . PRO A 139 ? 0.1435 0.1393 0.1405 0.0019 -0.0126 -0.0033 139 PRO A C 1087 O O . PRO A 139 ? 0.1497 0.1642 0.1370 0.0070 -0.0254 -0.0074 139 PRO A O 1088 C CB . PRO A 139 ? 0.1555 0.1557 0.1411 0.0064 -0.0079 -0.0103 139 PRO A CB 1089 C CG . PRO A 139 ? 0.1497 0.1520 0.1462 0.0058 -0.0126 -0.0164 139 PRO A CG 1090 C CD . PRO A 139 ? 0.1469 0.1432 0.1409 0.0057 -0.0120 -0.0119 139 PRO A CD 1091 N N . CYS A 140 ? 0.1425 0.1421 0.1254 0.0087 -0.0159 -0.0033 140 CYS A N 1092 C CA . CYS A 140 ? 0.1449 0.1439 0.1291 0.0073 -0.0130 -0.0014 140 CYS A CA 1093 C C . CYS A 140 ? 0.1456 0.1464 0.1334 0.0090 -0.0161 -0.0059 140 CYS A C 1094 O O . CYS A 140 ? 0.1642 0.1516 0.1334 0.0129 -0.0174 -0.0076 140 CYS A O 1095 C CB . CYS A 140 ? 0.1545 0.1620 0.1382 0.0074 -0.0140 0.0065 140 CYS A CB 1096 S SG . CYS A 140 ? 0.1649 0.1604 0.1524 0.0109 -0.0396 -0.0043 140 CYS A SG 1097 N N . GLY A 141 ? 0.1394 0.1441 0.1252 0.0090 -0.0107 -0.0083 141 GLY A N 1098 C CA . GLY A 141 ? 0.1355 0.1355 0.1152 0.0070 -0.0065 -0.0006 141 GLY A CA 1099 C C . GLY A 141 ? 0.1321 0.1358 0.1153 0.0059 -0.0098 0.0010 141 GLY A C 1100 O O . GLY A 141 ? 0.1215 0.1516 0.1371 -0.0026 -0.0079 0.0094 141 GLY A O 1101 N N . MET A 142 ? 0.1303 0.1454 0.1153 0.0172 -0.0151 0.0036 142 MET A N 1102 C CA . MET A 142 ? 0.1305 0.1350 0.1115 0.0161 -0.0070 0.0004 142 MET A CA 1103 C C . MET A 142 ? 0.1318 0.1467 0.1217 0.0112 -0.0095 -0.0050 142 MET A C 1104 O O . MET A 142 ? 0.1423 0.1496 0.1121 0.0185 -0.0113 0.0022 142 MET A O 1105 C CB . MET A 142 ? 0.1246 0.1502 0.1250 0.0182 -0.0042 -0.0023 142 MET A CB 1106 C CG . MET A 142 ? 0.1524 0.1514 0.1357 0.0065 -0.0081 -0.0031 142 MET A CG 1107 S SD . MET A 142 ? 0.1545 0.1413 0.1160 0.0110 -0.0115 -0.0150 142 MET A SD 1108 C CE . MET A 142 ? 0.1213 0.1260 0.1291 0.0016 -0.0107 -0.0028 142 MET A CE 1109 N N . ASN A 143 ? 0.1211 0.1368 0.1161 0.0215 -0.0068 -0.0080 143 ASN A N 1110 C CA . ASN A 143 ? 0.1211 0.1209 0.1087 0.0109 -0.0014 -0.0055 143 ASN A CA 1111 C C . ASN A 143 ? 0.1054 0.1115 0.0996 0.0133 0.0040 -0.0054 143 ASN A C 1112 O O . ASN A 143 ? 0.1213 0.1232 0.1144 0.0173 0.0011 0.0032 143 ASN A O 1113 C CB . ASN A 143 ? 0.1182 0.1161 0.1084 0.0162 -0.0054 -0.0074 143 ASN A CB 1114 C CG . ASN A 143 ? 0.0994 0.1226 0.1122 0.0107 -0.0086 0.0008 143 ASN A CG 1115 O OD1 . ASN A 143 ? 0.1198 0.1626 0.1161 0.0147 -0.0060 -0.0006 143 ASN A OD1 1116 N ND2 . ASN A 143 ? 0.0765 0.1409 0.1398 0.0049 0.0076 -0.0030 143 ASN A ND2 1117 N N . SER A 144 ? 0.1028 0.1233 0.1005 0.0076 -0.0030 0.0007 144 SER A N 1118 C CA . SER A 144 ? 0.1183 0.1133 0.1102 0.0040 -0.0048 -0.0023 144 SER A CA 1119 C C . SER A 144 ? 0.1085 0.1093 0.1133 0.0044 -0.0059 -0.0032 144 SER A C 1120 O O . SER A 144 ? 0.1025 0.1028 0.1189 0.0148 -0.0016 -0.0034 144 SER A O 1121 C CB . SER A 144 ? 0.1173 0.1116 0.1157 0.0000 -0.0125 0.0004 144 SER A CB 1122 O OG . SER A 144 ? 0.1080 0.1091 0.1255 -0.0008 -0.0159 -0.0072 144 SER A OG 1123 N N . ALA A 145 ? 0.0995 0.1112 0.1002 0.0072 -0.0090 -0.0031 145 ALA A N 1124 C CA . ALA A 145 ? 0.1000 0.1051 0.1087 0.0057 -0.0044 -0.0031 145 ALA A CA 1125 C C . ALA A 145 ? 0.0966 0.1047 0.1113 -0.0005 -0.0032 -0.0024 145 ALA A C 1126 O O . ALA A 145 ? 0.1020 0.1083 0.1065 0.0040 -0.0045 0.0029 145 ALA A O 1127 C CB . ALA A 145 ? 0.1050 0.1203 0.1158 0.0076 -0.0130 -0.0091 145 ALA A CB 1128 N N . LEU A 146 ? 0.0944 0.0823 0.1126 -0.0009 -0.0008 -0.0026 146 LEU A N 1129 C CA . LEU A 146 ? 0.0967 0.0994 0.1123 0.0003 -0.0010 -0.0036 146 LEU A CA 1130 C C . LEU A 146 ? 0.1047 0.0975 0.1102 0.0069 -0.0055 -0.0026 146 LEU A C 1131 O O . LEU A 146 ? 0.1066 0.1004 0.1180 0.0129 -0.0151 -0.0005 146 LEU A O 1132 C CB . LEU A 146 ? 0.1121 0.0966 0.1232 -0.0027 -0.0023 -0.0044 146 LEU A CB 1133 C CG . LEU A 146 ? 0.0922 0.0962 0.1266 0.0082 -0.0017 0.0021 146 LEU A CG 1134 C CD1 . LEU A 146 ? 0.1134 0.1232 0.1311 -0.0076 0.0123 0.0036 146 LEU A CD1 1135 C CD2 . LEU A 146 ? 0.1082 0.1287 0.1252 0.0027 -0.0049 -0.0037 146 LEU A CD2 1136 N N . TYR A 147 ? 0.1044 0.0948 0.1119 -0.0049 -0.0143 -0.0015 147 TYR A N 1137 C CA . TYR A 147 ? 0.0998 0.1008 0.1136 -0.0038 -0.0046 0.0019 147 TYR A CA 1138 C C . TYR A 147 ? 0.1054 0.1007 0.1010 -0.0074 -0.0070 0.0040 147 TYR A C 1139 O O . TYR A 147 ? 0.1167 0.1026 0.1165 -0.0042 -0.0029 0.0031 147 TYR A O 1140 C CB . TYR A 147 ? 0.1087 0.1087 0.1135 -0.0007 -0.0060 -0.0027 147 TYR A CB 1141 C CG . TYR A 147 ? 0.1103 0.0872 0.1155 -0.0036 -0.0040 0.0026 147 TYR A CG 1142 C CD1 . TYR A 147 ? 0.1128 0.1170 0.1098 -0.0039 -0.0002 -0.0079 147 TYR A CD1 1143 C CD2 . TYR A 147 ? 0.1030 0.1020 0.1170 -0.0108 0.0014 -0.0182 147 TYR A CD2 1144 C CE1 . TYR A 147 ? 0.0939 0.0957 0.1152 0.0001 -0.0075 0.0007 147 TYR A CE1 1145 C CE2 . TYR A 147 ? 0.0965 0.1114 0.1077 -0.0088 0.0009 -0.0055 147 TYR A CE2 1146 C CZ . TYR A 147 ? 0.0938 0.1042 0.1001 0.0050 0.0002 -0.0064 147 TYR A CZ 1147 O OH . TYR A 147 ? 0.1035 0.1138 0.0996 0.0102 0.0030 0.0075 147 TYR A OH 1148 N N . LEU A 148 ? 0.1008 0.0865 0.0997 -0.0004 -0.0049 0.0030 148 LEU A N 1149 C CA . LEU A 148 ? 0.0978 0.1040 0.0973 -0.0032 0.0029 0.0068 148 LEU A CA 1150 C C . LEU A 148 ? 0.1036 0.1013 0.1065 -0.0072 -0.0040 0.0055 148 LEU A C 1151 O O . LEU A 148 ? 0.1093 0.0964 0.1181 -0.0053 -0.0054 0.0145 148 LEU A O 1152 C CB . LEU A 148 ? 0.0959 0.1163 0.1097 -0.0007 0.0002 -0.0011 148 LEU A CB 1153 C CG . LEU A 148 ? 0.1216 0.1570 0.1259 -0.0077 0.0057 -0.0063 148 LEU A CG 1154 C CD1 . LEU A 148 ? 0.1499 0.1757 0.1733 0.0000 0.0181 -0.0134 148 LEU A CD1 1155 C CD2 . LEU A 148 ? 0.1669 0.1720 0.1834 -0.0157 0.0319 -0.0091 148 LEU A CD2 1156 N N . SER A 149 ? 0.0858 0.0897 0.1096 -0.0033 0.0005 -0.0013 149 SER A N 1157 C CA . SER A 149 ? 0.0933 0.1062 0.0995 -0.0047 0.0079 0.0007 149 SER A CA 1158 C C . SER A 149 ? 0.0883 0.1054 0.1018 -0.0021 0.0033 0.0034 149 SER A C 1159 O O . SER A 149 ? 0.1083 0.1102 0.1043 -0.0062 -0.0063 0.0110 149 SER A O 1160 C CB . SER A 149 ? 0.0968 0.1102 0.1015 0.0020 0.0026 -0.0046 149 SER A CB 1161 O OG . SER A 149 ? 0.1335 0.1747 0.1222 0.0249 -0.0130 -0.0199 149 SER A OG 1162 N N . GLU A 150 ? 0.1017 0.1003 0.0932 -0.0065 -0.0004 0.0056 150 GLU A N 1163 C CA . GLU A 150 ? 0.0987 0.1055 0.0946 -0.0022 0.0014 -0.0007 150 GLU A CA 1164 C C . GLU A 150 ? 0.0985 0.1066 0.1046 -0.0037 -0.0027 0.0027 150 GLU A C 1165 O O . GLU A 150 ? 0.0955 0.1175 0.1243 -0.0123 0.0035 -0.0144 150 GLU A O 1166 C CB . GLU A 150 ? 0.0999 0.0963 0.0980 -0.0070 -0.0103 0.0013 150 GLU A CB 1167 C CG . GLU A 150 ? 0.0945 0.1056 0.1032 0.0034 -0.0059 0.0033 150 GLU A CG 1168 C CD . GLU A 150 ? 0.0930 0.1026 0.0937 0.0004 0.0065 0.0002 150 GLU A CD 1169 O OE1 . GLU A 150 ? 0.1239 0.1282 0.1251 -0.0015 0.0070 0.0037 150 GLU A OE1 1170 O OE2 . GLU A 150 ? 0.1209 0.1093 0.1268 -0.0042 -0.0102 -0.0127 150 GLU A OE2 1171 N N . MET A 151 ? 0.0977 0.0940 0.1065 -0.0011 0.0083 -0.0005 151 MET A N 1172 C CA . MET A 151 ? 0.0976 0.1134 0.1044 0.0026 0.0028 0.0018 151 MET A CA 1173 C C . MET A 151 ? 0.1043 0.1112 0.0961 0.0058 -0.0006 -0.0003 151 MET A C 1174 O O . MET A 151 ? 0.1061 0.1200 0.1044 0.0104 -0.0007 0.0021 151 MET A O 1175 C CB . MET A 151 ? 0.1002 0.1096 0.1137 -0.0026 0.0108 0.0059 151 MET A CB 1176 C CG . MET A 151 ? 0.0969 0.1076 0.1031 0.0031 0.0007 0.0030 151 MET A CG 1177 S SD . MET A 151 ? 0.0985 0.1168 0.1117 0.0030 0.0073 -0.0039 151 MET A SD 1178 C CE . MET A 151 ? 0.1154 0.1064 0.1270 -0.0137 0.0112 -0.0113 151 MET A CE 1179 N N . HIS A 152 ? 0.1127 0.1054 0.1050 0.0112 -0.0034 -0.0057 152 HIS A N 1180 C CA . HIS A 152 ? 0.1177 0.1200 0.1045 -0.0020 -0.0022 -0.0063 152 HIS A CA 1181 C C . HIS A 152 ? 0.1087 0.1151 0.1057 -0.0008 -0.0036 -0.0018 152 HIS A C 1182 O O . HIS A 152 ? 0.1181 0.1185 0.1017 0.0011 -0.0083 -0.0045 152 HIS A O 1183 C CB . HIS A 152 ? 0.1280 0.1175 0.1081 0.0081 -0.0037 -0.0034 152 HIS A CB 1184 C CG . HIS A 152 ? 0.1213 0.1053 0.1187 -0.0025 -0.0168 0.0039 152 HIS A CG 1185 N ND1 . HIS A 152 ? 0.0998 0.1083 0.1268 -0.0092 -0.0123 0.0111 152 HIS A ND1 1186 C CD2 . HIS A 152 ? 0.1644 0.1043 0.1465 -0.0212 -0.0243 0.0145 152 HIS A CD2 1187 C CE1 . HIS A 152 ? 0.1389 0.1065 0.1320 -0.0161 -0.0201 0.0320 152 HIS A CE1 1188 N NE2 . HIS A 152 ? 0.1535 0.1306 0.1499 -0.0183 -0.0444 0.0365 152 HIS A NE2 1189 N N . PRO A 153 ? 0.1208 0.1138 0.1004 -0.0033 0.0008 -0.0012 153 PRO A N 1190 C CA . PRO A 153 ? 0.1120 0.1239 0.1149 0.0000 0.0016 -0.0060 153 PRO A CA 1191 C C . PRO A 153 ? 0.1204 0.1186 0.1060 -0.0018 -0.0020 -0.0030 153 PRO A C 1192 O O . PRO A 153 ? 0.1086 0.1195 0.1238 -0.0105 0.0098 0.0026 153 PRO A O 1193 C CB . PRO A 153 ? 0.1161 0.1372 0.1163 -0.0075 0.0020 0.0009 153 PRO A CB 1194 C CG . PRO A 153 ? 0.1773 0.1728 0.1474 -0.0136 0.0100 -0.0028 153 PRO A CG 1195 C CD . PRO A 153 ? 0.1254 0.1132 0.1084 0.0013 0.0084 0.0021 153 PRO A CD 1196 N N . THR A 154 ? 0.1049 0.1175 0.1064 -0.0076 -0.0046 -0.0111 154 THR A N 1197 C CA . THR A 154 ? 0.1121 0.1119 0.1165 -0.0029 -0.0076 -0.0029 154 THR A CA 1198 C C . THR A 154 ? 0.1157 0.1045 0.1238 -0.0005 0.0044 -0.0052 154 THR A C 1199 O O . THR A 154 ? 0.1272 0.1144 0.1311 0.0082 0.0029 -0.0155 154 THR A O 1200 C CB . THR A 154 ? 0.1028 0.1190 0.1227 -0.0006 -0.0089 -0.0049 154 THR A CB 1201 O OG1 . THR A 154 ? 0.1124 0.1355 0.1482 0.0037 -0.0063 -0.0086 154 THR A OG1 1202 C CG2 . THR A 154 ? 0.1438 0.1653 0.1472 0.0105 -0.0005 0.0119 154 THR A CG2 1203 N N . GLY A 155 ? 0.1125 0.1189 0.1202 0.0147 -0.0045 -0.0005 155 GLY A N 1204 C CA . GLY A 155 ? 0.1139 0.1197 0.1246 -0.0003 0.0000 -0.0009 155 GLY A CA 1205 C C . GLY A 155 ? 0.1079 0.1191 0.1231 0.0019 -0.0022 -0.0070 155 GLY A C 1206 O O . GLY A 155 ? 0.1164 0.1329 0.1201 0.0098 -0.0076 -0.0014 155 GLY A O 1207 N N . ALA A 156 ? 0.1128 0.1402 0.1164 0.0042 0.0024 -0.0020 156 ALA A N 1208 C CA . ALA A 156 ? 0.1117 0.1211 0.1141 -0.0065 -0.0001 -0.0013 156 ALA A CA 1209 C C . ALA A 156 ? 0.1066 0.1255 0.1052 0.0000 0.0031 0.0018 156 ALA A C 1210 O O . ALA A 156 ? 0.1102 0.1373 0.1165 -0.0031 0.0067 0.0027 156 ALA A O 1211 C CB . ALA A 156 ? 0.1361 0.1113 0.1223 -0.0017 -0.0126 -0.0057 156 ALA A CB 1212 N N . LYS A 157 ? 0.1094 0.1139 0.1189 -0.0009 0.0064 0.0002 157 LYS A N 1213 C CA . LYS A 157 ? 0.1199 0.1248 0.1201 -0.0030 0.0000 -0.0036 157 LYS A CA 1214 C C . LYS A 157 ? 0.1082 0.1272 0.1180 0.0052 -0.0018 0.0028 157 LYS A C 1215 O O . LYS A 157 ? 0.1197 0.1487 0.1379 0.0018 -0.0047 0.0033 157 LYS A O 1216 C CB . LYS A 157 ? 0.1058 0.1230 0.1206 -0.0025 0.0018 -0.0120 157 LYS A CB 1217 C CG . LYS A 157 ? 0.1355 0.1223 0.1365 -0.0092 -0.0029 -0.0059 157 LYS A CG 1218 C CD . LYS A 157 ? 0.1825 0.1600 0.1713 -0.0071 0.0103 0.0076 157 LYS A CD 1219 C CE . LYS A 157 ? 0.2307 0.2000 0.2107 0.0033 0.0081 0.0137 157 LYS A CE 1220 N NZ . LYS A 157 ? 0.3195 0.2923 0.2862 0.0002 -0.0093 -0.0155 157 LYS A NZ 1221 N N . SER A 158 ? 0.1161 0.1383 0.1130 0.0062 -0.0005 0.0026 158 SER A N 1222 C CA . SER A 158 ? 0.1304 0.1474 0.1257 -0.0031 -0.0072 0.0039 158 SER A CA 1223 C C . SER A 158 ? 0.1545 0.1460 0.1267 -0.0025 -0.0042 0.0095 158 SER A C 1224 O O . SER A 158 ? 0.1487 0.1463 0.1307 0.0030 0.0023 -0.0021 158 SER A O 1225 C CB . SER A 158 ? 0.1330 0.1579 0.1159 -0.0098 0.0005 0.0010 158 SER A CB 1226 O OG . SER A 158 ? 0.1335 0.1732 0.1041 -0.0183 -0.0077 0.0051 158 SER A OG 1227 N N . LYS A 159 ? 0.1698 0.1820 0.1512 -0.0005 -0.0056 0.0002 159 LYS A N 1228 C CA . LYS A 159 ? 0.1756 0.1741 0.1708 0.0031 -0.0058 0.0042 159 LYS A CA 1229 C C . LYS A 159 ? 0.1397 0.1566 0.1668 -0.0025 -0.0071 -0.0011 159 LYS A C 1230 O O . LYS A 159 ? 0.1648 0.1471 0.1883 0.0069 -0.0039 0.0171 159 LYS A O 1231 C CB . LYS A 159 ? 0.2044 0.2033 0.1955 0.0092 -0.0171 -0.0010 159 LYS A CB 1232 C CG . LYS A 159 ? 0.2355 0.2431 0.2263 0.0103 -0.0048 0.0056 159 LYS A CG 1233 C CD . LYS A 159 ? 0.2256 0.2700 0.2624 0.0013 -0.0025 -0.0003 159 LYS A CD 1234 C CE . LYS A 159 ? 0.2859 0.3212 0.3244 0.0145 -0.0037 0.0099 159 LYS A CE 1235 N NZ . LYS A 159 ? 0.3223 0.3481 0.3577 -0.0086 -0.0147 -0.0002 159 LYS A NZ 1236 N N . TYR A 160 ? 0.1234 0.1530 0.1495 0.0091 -0.0090 0.0052 160 TYR A N 1237 C CA . TYR A 160 ? 0.1341 0.1405 0.1503 0.0045 -0.0043 0.0005 160 TYR A CA 1238 C C . TYR A 160 ? 0.1170 0.1313 0.1261 0.0014 -0.0006 -0.0045 160 TYR A C 1239 O O . TYR A 160 ? 0.1032 0.1181 0.1282 0.0059 0.0158 0.0166 160 TYR A O 1240 C CB . TYR A 160 ? 0.1542 0.1589 0.1690 -0.0032 0.0016 -0.0016 160 TYR A CB 1241 C CG . TYR A 160 ? 0.1735 0.1899 0.1994 -0.0061 -0.0030 0.0001 160 TYR A CG 1242 C CD1 . TYR A 160 ? 0.1316 0.1995 0.2016 -0.0008 0.0029 0.0039 160 TYR A CD1 1243 C CD2 . TYR A 160 ? 0.1843 0.2119 0.2349 -0.0018 -0.0127 -0.0137 160 TYR A CD2 1244 C CE1 . TYR A 160 ? 0.1556 0.2213 0.2409 0.0023 0.0068 -0.0034 160 TYR A CE1 1245 C CE2 . TYR A 160 ? 0.1658 0.2181 0.2666 -0.0163 -0.0083 -0.0100 160 TYR A CE2 1246 C CZ . TYR A 160 ? 0.1693 0.2307 0.2484 -0.0046 -0.0057 -0.0167 160 TYR A CZ 1247 O OH . TYR A 160 ? 0.1831 0.2746 0.2805 -0.0224 -0.0091 -0.0022 160 TYR A OH 1248 N N . ASN A 161 ? 0.1120 0.1245 0.1157 0.0099 0.0003 -0.0032 161 ASN A N 1249 C CA . ASN A 161 ? 0.1139 0.1129 0.1141 0.0042 -0.0001 -0.0037 161 ASN A CA 1250 C C . ASN A 161 ? 0.1022 0.1185 0.1273 0.0009 -0.0025 -0.0001 161 ASN A C 1251 O O . ASN A 161 ? 0.1088 0.1039 0.1179 0.0069 0.0089 -0.0084 161 ASN A O 1252 C CB . ASN A 161 ? 0.1034 0.1100 0.1169 0.0100 0.0001 0.0000 161 ASN A CB 1253 C CG . ASN A 161 ? 0.1213 0.1152 0.1087 0.0037 0.0055 0.0017 161 ASN A CG 1254 O OD1 . ASN A 161 ? 0.1457 0.1475 0.1370 0.0192 0.0195 -0.0013 161 ASN A OD1 1255 N ND2 . ASN A 161 ? 0.0834 0.0792 0.0930 0.0120 0.0091 -0.0014 161 ASN A ND2 1256 N N . PRO A 162 ? 0.0988 0.1183 0.1234 0.0056 0.0014 -0.0013 162 PRO A N 1257 C CA . PRO A 162 ? 0.1169 0.1195 0.1243 -0.0020 0.0002 0.0000 162 PRO A CA 1258 C C . PRO A 162 ? 0.1175 0.1321 0.1177 -0.0007 0.0007 0.0052 162 PRO A C 1259 O O . PRO A 162 ? 0.1369 0.1600 0.1324 -0.0088 0.0056 0.0022 162 PRO A O 1260 C CB . PRO A 162 ? 0.1296 0.1219 0.1393 0.0030 -0.0065 0.0036 162 PRO A CB 1261 C CG . PRO A 162 ? 0.1277 0.1034 0.1440 0.0101 -0.0059 -0.0071 162 PRO A CG 1262 C CD . PRO A 162 ? 0.1126 0.1335 0.1329 -0.0014 0.0023 0.0009 162 PRO A CD 1263 N N . GLY A 163 ? 0.1191 0.1261 0.1150 -0.0052 -0.0019 0.0109 163 GLY A N 1264 C CA . GLY A 163 ? 0.1228 0.1219 0.1283 -0.0007 -0.0044 0.0039 163 GLY A CA 1265 C C . GLY A 163 ? 0.1174 0.1257 0.1231 -0.0067 0.0061 -0.0012 163 GLY A C 1266 O O . GLY A 163 ? 0.1261 0.1338 0.1269 -0.0114 0.0197 -0.0033 163 GLY A O 1267 N N . GLY A 164 ? 0.1087 0.1174 0.1156 -0.0038 -0.0018 0.0037 164 GLY A N 1268 C CA . GLY A 164 ? 0.1035 0.1104 0.1101 -0.0073 0.0072 0.0008 164 GLY A CA 1269 C C . GLY A 164 ? 0.1126 0.1191 0.1058 -0.0053 0.0082 -0.0002 164 GLY A C 1270 O O . GLY A 164 ? 0.1093 0.1280 0.1192 0.0014 0.0025 -0.0076 164 GLY A O 1271 N N . ALA A 165 ? 0.0991 0.1168 0.1090 0.0001 0.0101 0.0041 165 ALA A N 1272 C CA . ALA A 165 ? 0.0996 0.1078 0.1114 -0.0003 0.0033 0.0040 165 ALA A CA 1273 C C . ALA A 165 ? 0.1033 0.1181 0.1030 0.0020 0.0022 -0.0012 165 ALA A C 1274 O O . ALA A 165 ? 0.0853 0.1212 0.1089 -0.0024 0.0134 0.0010 165 ALA A O 1275 C CB . ALA A 165 ? 0.1039 0.1134 0.1242 -0.0013 -0.0014 0.0007 165 ALA A CB 1276 N N . TYR A 166 ? 0.1049 0.1091 0.1120 0.0000 0.0096 -0.0024 166 TYR A N 1277 C CA . TYR A 166 ? 0.0940 0.1017 0.1127 -0.0027 0.0043 0.0078 166 TYR A CA 1278 C C . TYR A 166 ? 0.0982 0.0955 0.1118 -0.0089 0.0043 -0.0008 166 TYR A C 1279 O O . TYR A 166 ? 0.1151 0.1083 0.1102 -0.0074 0.0032 -0.0006 166 TYR A O 1280 C CB . TYR A 166 ? 0.1115 0.1180 0.1108 -0.0033 -0.0023 0.0086 166 TYR A CB 1281 C CG . TYR A 166 ? 0.1074 0.1004 0.1175 0.0147 -0.0026 0.0157 166 TYR A CG 1282 C CD1 . TYR A 166 ? 0.1127 0.1001 0.1290 -0.0019 0.0064 -0.0002 166 TYR A CD1 1283 C CD2 . TYR A 166 ? 0.1234 0.1257 0.1351 -0.0041 0.0008 0.0120 166 TYR A CD2 1284 C CE1 . TYR A 166 ? 0.1119 0.1246 0.1583 -0.0126 0.0033 0.0288 166 TYR A CE1 1285 C CE2 . TYR A 166 ? 0.1410 0.1380 0.1700 -0.0146 -0.0090 -0.0013 166 TYR A CE2 1286 C CZ . TYR A 166 ? 0.1502 0.1247 0.1812 -0.0119 -0.0045 0.0050 166 TYR A CZ 1287 O OH . TYR A 166 ? 0.1754 0.1186 0.2283 -0.0041 -0.0302 0.0154 166 TYR A OH 1288 N N . TYR A 167 ? 0.0960 0.1022 0.1097 -0.0069 0.0063 0.0062 167 TYR A N 1289 C CA . TYR A 167 ? 0.0974 0.1038 0.1092 -0.0030 0.0009 0.0031 167 TYR A CA 1290 C C . TYR A 167 ? 0.0979 0.1007 0.1036 0.0019 0.0084 0.0043 167 TYR A C 1291 O O . TYR A 167 ? 0.1219 0.1180 0.1158 0.0166 0.0136 0.0092 167 TYR A O 1292 C CB . TYR A 167 ? 0.1143 0.1230 0.1159 0.0031 0.0045 0.0024 167 TYR A CB 1293 C CG . TYR A 167 ? 0.0954 0.1157 0.1148 -0.0016 -0.0043 -0.0029 167 TYR A CG 1294 C CD1 . TYR A 167 ? 0.1091 0.1146 0.1171 0.0058 0.0084 0.0057 167 TYR A CD1 1295 C CD2 . TYR A 167 ? 0.1415 0.1245 0.1308 0.0148 -0.0113 0.0011 167 TYR A CD2 1296 C CE1 . TYR A 167 ? 0.1184 0.1195 0.1229 0.0128 0.0051 -0.0045 167 TYR A CE1 1297 C CE2 . TYR A 167 ? 0.1403 0.1201 0.1549 0.0201 -0.0081 -0.0320 167 TYR A CE2 1298 C CZ . TYR A 167 ? 0.1195 0.1121 0.1540 0.0152 0.0018 -0.0089 167 TYR A CZ 1299 O OH . TYR A 167 ? 0.1227 0.1243 0.2114 -0.0004 0.0114 0.0126 167 TYR A OH 1300 N N . GLY A 168 ? 0.1072 0.0968 0.0935 -0.0006 0.0077 0.0002 168 GLY A N 1301 C CA . GLY A 168 ? 0.0932 0.1076 0.1014 -0.0019 -0.0007 0.0052 168 GLY A CA 1302 C C . GLY A 168 ? 0.0934 0.1014 0.0987 0.0026 0.0046 0.0063 168 GLY A C 1303 O O . GLY A 168 ? 0.0858 0.0977 0.0899 0.0016 -0.0022 0.0065 168 GLY A O 1304 N N . THR A 169 ? 0.1021 0.1002 0.0988 0.0054 0.0032 0.0081 169 THR A N 1305 C CA . THR A 169 ? 0.0949 0.0981 0.1018 0.0024 -0.0005 0.0051 169 THR A CA 1306 C C . THR A 169 ? 0.1060 0.1040 0.0974 0.0009 0.0060 0.0021 169 THR A C 1307 O O . THR A 169 ? 0.0959 0.1037 0.1127 -0.0030 0.0031 0.0036 169 THR A O 1308 C CB . THR A 169 ? 0.0968 0.0983 0.1008 0.0069 -0.0031 0.0036 169 THR A CB 1309 O OG1 . THR A 169 ? 0.0958 0.1273 0.1040 0.0143 -0.0114 0.0072 169 THR A OG1 1310 C CG2 . THR A 169 ? 0.1068 0.1062 0.0893 0.0124 -0.0008 -0.0039 169 THR A CG2 1311 N N . GLY A 170 ? 0.0982 0.0939 0.1068 -0.0032 -0.0015 -0.0019 170 GLY A N 1312 C CA . GLY A 170 ? 0.1009 0.0921 0.1029 -0.0002 0.0000 -0.0020 170 GLY A CA 1313 C C . GLY A 170 ? 0.0903 0.0909 0.0960 0.0039 -0.0015 -0.0030 170 GLY A C 1314 O O . GLY A 170 ? 0.1029 0.0946 0.1217 0.0063 -0.0162 0.0011 170 GLY A O 1315 N N . TYR A 171 ? 0.0861 0.0957 0.1001 0.0088 -0.0044 0.0020 171 TYR A N 1316 C CA . TYR A 171 ? 0.0962 0.0914 0.0963 0.0017 0.0024 0.0079 171 TYR A CA 1317 C C . TYR A 171 ? 0.0896 0.1002 0.0974 -0.0019 0.0035 0.0060 171 TYR A C 1318 O O . TYR A 171 ? 0.0920 0.0999 0.1137 0.0023 -0.0047 0.0072 171 TYR A O 1319 C CB . TYR A 171 ? 0.0888 0.1127 0.1030 -0.0005 -0.0007 0.0065 171 TYR A CB 1320 C CG . TYR A 171 ? 0.0974 0.0910 0.0951 0.0073 0.0015 0.0085 171 TYR A CG 1321 C CD1 . TYR A 171 ? 0.0952 0.1070 0.1004 -0.0035 -0.0069 0.0119 171 TYR A CD1 1322 C CD2 . TYR A 171 ? 0.0923 0.1114 0.0900 -0.0014 -0.0050 0.0038 171 TYR A CD2 1323 C CE1 . TYR A 171 ? 0.0881 0.1073 0.1086 -0.0059 0.0122 0.0094 171 TYR A CE1 1324 C CE2 . TYR A 171 ? 0.1258 0.1067 0.0935 0.0081 0.0001 0.0082 171 TYR A CE2 1325 C CZ . TYR A 171 ? 0.1157 0.0992 0.0998 0.0074 -0.0072 -0.0031 171 TYR A CZ 1326 O OH . TYR A 171 ? 0.1080 0.1045 0.1019 0.0162 -0.0078 0.0067 171 TYR A OH 1327 N N . CYS A 172 ? 0.0997 0.0967 0.1056 -0.0031 0.0054 0.0095 172 CYS A N 1328 C CA . CYS A 172 ? 0.1006 0.0940 0.0993 -0.0025 0.0045 0.0023 172 CYS A CA 1329 C C . CYS A 172 ? 0.1033 0.0854 0.1073 -0.0095 0.0021 0.0015 172 CYS A C 1330 O O . CYS A 172 ? 0.0991 0.0963 0.1029 -0.0012 0.0079 -0.0015 172 CYS A O 1331 C CB . CYS A 172 ? 0.1190 0.0938 0.1048 0.0000 0.0012 0.0019 172 CYS A CB 1332 S SG . CYS A 172 ? 0.1191 0.1022 0.0986 -0.0029 0.0004 0.0016 172 CYS A SG 1333 N N . ASP A 173 ? 0.0999 0.0931 0.0995 0.0037 0.0023 0.0066 173 ASP A N 1334 C CA . ASP A 173 ? 0.0933 0.0985 0.1113 0.0001 0.0039 0.0026 173 ASP A CA 1335 C C . ASP A 173 ? 0.0837 0.0975 0.1037 0.0016 -0.0003 0.0015 173 ASP A C 1336 O O . ASP A 173 ? 0.0849 0.1035 0.1204 -0.0051 -0.0078 0.0034 173 ASP A O 1337 C CB . ASP A 173 ? 0.1053 0.0944 0.1030 0.0065 0.0053 0.0033 173 ASP A CB 1338 C CG . ASP A 173 ? 0.1195 0.1029 0.1042 -0.0041 -0.0106 0.0005 173 ASP A CG 1339 O OD1 . ASP A 173 ? 0.1006 0.1084 0.1066 0.0070 -0.0023 0.0007 173 ASP A OD1 1340 O OD2 . ASP A 173 ? 0.1161 0.1163 0.0980 -0.0054 -0.0046 0.0033 173 ASP A OD2 1341 N N . ALA A 174 ? 0.0857 0.0915 0.1206 0.0087 -0.0029 0.0030 174 ALA A N 1342 C CA . ALA A 174 ? 0.0975 0.1016 0.1133 0.0044 0.0051 0.0053 174 ALA A CA 1343 C C . ALA A 174 ? 0.1099 0.1081 0.1211 -0.0024 0.0075 -0.0030 174 ALA A C 1344 O O . ALA A 174 ? 0.1168 0.1030 0.1281 0.0014 0.0125 -0.0095 174 ALA A O 1345 C CB . ALA A 174 ? 0.1084 0.1263 0.1297 0.0035 0.0080 0.0048 174 ALA A CB 1346 N N . GLN A 175 ? 0.1071 0.0972 0.1175 0.0032 0.0114 -0.0010 175 GLN A N 1347 C CA . GLN A 175 ? 0.1083 0.1099 0.1067 0.0047 0.0031 0.0042 175 GLN A CA 1348 C C . GLN A 175 ? 0.1051 0.0999 0.1090 -0.0021 0.0054 0.0070 175 GLN A C 1349 O O . GLN A 175 ? 0.1206 0.1266 0.1188 0.0030 0.0104 0.0056 175 GLN A O 1350 C CB . GLN A 175 ? 0.1165 0.1082 0.1076 -0.0071 0.0082 0.0026 175 GLN A CB 1351 C CG . GLN A 175 ? 0.1138 0.1314 0.1310 0.0051 -0.0071 0.0067 175 GLN A CG 1352 C CD . GLN A 175 ? 0.1025 0.1350 0.1201 -0.0133 -0.0100 0.0023 175 GLN A CD 1353 O OE1 . GLN A 175 ? 0.1559 0.1281 0.1574 -0.0243 -0.0065 0.0150 175 GLN A OE1 1354 N NE2 . GLN A 175 ? 0.1084 0.1437 0.1380 0.0056 -0.0241 -0.0051 175 GLN A NE2 1355 N N . CYS A 176 ? 0.1051 0.1130 0.1041 0.0051 0.0111 0.0169 176 CYS A N 1356 C CA . CYS A 176 ? 0.1121 0.1089 0.1070 0.0017 0.0113 0.0065 176 CYS A CA 1357 C C . CYS A 176 ? 0.1166 0.1020 0.1155 0.0017 0.0127 0.0015 176 CYS A C 1358 O O . CYS A 176 ? 0.1154 0.1189 0.1202 0.0066 0.0217 -0.0025 176 CYS A O 1359 C CB . CYS A 176 ? 0.1043 0.1057 0.1068 -0.0004 0.0108 0.0125 176 CYS A CB 1360 S SG . CYS A 176 ? 0.1174 0.1116 0.1255 0.0022 0.0061 0.0016 176 CYS A SG 1361 N N . PHE A 177 ? 0.1045 0.1124 0.1087 0.0073 0.0116 -0.0068 177 PHE A N 1362 C CA . PHE A 177 ? 0.1175 0.1215 0.1043 0.0030 0.0069 -0.0038 177 PHE A CA 1363 C C . PHE A 177 ? 0.1173 0.1149 0.0984 0.0021 0.0064 -0.0018 177 PHE A C 1364 O O . PHE A 177 ? 0.1168 0.1251 0.1099 0.0033 0.0007 0.0033 177 PHE A O 1365 C CB . PHE A 177 ? 0.1294 0.1175 0.1067 -0.0006 -0.0015 -0.0005 177 PHE A CB 1366 C CG . PHE A 177 ? 0.1382 0.1349 0.1170 0.0025 -0.0036 -0.0098 177 PHE A CG 1367 C CD1 . PHE A 177 ? 0.1415 0.1527 0.1392 0.0064 0.0011 0.0068 177 PHE A CD1 1368 C CD2 . PHE A 177 ? 0.1444 0.1177 0.1133 0.0240 -0.0075 -0.0027 177 PHE A CD2 1369 C CE1 . PHE A 177 ? 0.1551 0.1597 0.1299 0.0210 0.0056 0.0095 177 PHE A CE1 1370 C CE2 . PHE A 177 ? 0.1145 0.1341 0.1246 0.0000 0.0049 -0.0133 177 PHE A CE2 1371 C CZ . PHE A 177 ? 0.1381 0.1358 0.1417 0.0215 -0.0064 -0.0025 177 PHE A CZ 1372 N N . VAL A 178 ? 0.1293 0.1277 0.1170 0.0117 0.0122 0.0067 178 VAL A N 1373 C CA . VAL A 178 ? 0.1277 0.1341 0.1201 0.0076 0.0121 0.0030 178 VAL A CA 1374 C C . VAL A 178 ? 0.1152 0.1405 0.1206 0.0030 0.0106 0.0072 178 VAL A C 1375 O O . VAL A 178 ? 0.1527 0.1244 0.1181 0.0052 0.0091 0.0037 178 VAL A O 1376 C CB . VAL A 178 ? 0.1240 0.1292 0.1088 0.0064 0.0110 0.0038 178 VAL A CB 1377 C CG1 . VAL A 178 ? 0.1260 0.1371 0.1349 0.0163 0.0232 0.0064 178 VAL A CG1 1378 C CG2 . VAL A 178 ? 0.1433 0.1488 0.1193 -0.0053 0.0129 0.0201 178 VAL A CG2 1379 N N . THR A 179 ? 0.1144 0.1164 0.1071 0.0018 0.0085 0.0047 179 THR A N 1380 C CA . THR A 179 ? 0.1191 0.1214 0.1140 0.0070 0.0115 0.0081 179 THR A CA 1381 C C . THR A 179 ? 0.1112 0.1082 0.1072 0.0065 0.0082 -0.0013 179 THR A C 1382 O O . THR A 179 ? 0.1296 0.1119 0.1226 0.0059 0.0054 0.0094 179 THR A O 1383 C CB . THR A 179 ? 0.1113 0.1174 0.1273 0.0080 0.0100 0.0080 179 THR A CB 1384 O OG1 . THR A 179 ? 0.1137 0.1166 0.1133 0.0008 0.0135 0.0169 179 THR A OG1 1385 C CG2 . THR A 179 ? 0.1256 0.1573 0.1339 0.0095 0.0090 0.0097 179 THR A CG2 1386 N N . PRO A 180 ? 0.1189 0.1138 0.1185 0.0033 0.0054 0.0001 180 PRO A N 1387 C CA . PRO A 180 ? 0.1068 0.1280 0.1219 0.0032 0.0084 -0.0008 180 PRO A CA 1388 C C . PRO A 180 ? 0.1110 0.1284 0.1274 0.0025 0.0072 0.0063 180 PRO A C 1389 O O . PRO A 180 ? 0.1070 0.1180 0.1149 0.0111 0.0172 0.0028 180 PRO A O 1390 C CB . PRO A 180 ? 0.1355 0.1502 0.1369 0.0006 0.0069 -0.0096 180 PRO A CB 1391 C CG . PRO A 180 ? 0.1361 0.1477 0.1705 0.0026 0.0100 -0.0053 180 PRO A CG 1392 C CD . PRO A 180 ? 0.1077 0.1186 0.1176 0.0024 0.0144 -0.0090 180 PRO A CD 1393 N N . PHE A 181 ? 0.0943 0.1232 0.1179 0.0023 0.0089 -0.0025 181 PHE A N 1394 C CA . PHE A 181 ? 0.0975 0.1149 0.1108 0.0049 0.0028 0.0036 181 PHE A CA 1395 C C . PHE A 181 ? 0.0975 0.1118 0.1051 0.0024 0.0053 -0.0007 181 PHE A C 1396 O O . PHE A 181 ? 0.0927 0.1089 0.1084 0.0086 0.0085 0.0069 181 PHE A O 1397 C CB . PHE A 181 ? 0.1045 0.1185 0.1094 -0.0034 0.0000 -0.0018 181 PHE A CB 1398 C CG . PHE A 181 ? 0.1029 0.1121 0.1177 -0.0056 0.0018 -0.0024 181 PHE A CG 1399 C CD1 . PHE A 181 ? 0.1177 0.1134 0.1246 0.0132 -0.0053 -0.0037 181 PHE A CD1 1400 C CD2 . PHE A 181 ? 0.1185 0.1207 0.1260 0.0100 -0.0060 -0.0100 181 PHE A CD2 1401 C CE1 . PHE A 181 ? 0.1342 0.1222 0.1416 -0.0017 -0.0053 -0.0157 181 PHE A CE1 1402 C CE2 . PHE A 181 ? 0.1315 0.1194 0.1555 0.0064 -0.0042 0.0029 181 PHE A CE2 1403 C CZ . PHE A 181 ? 0.1365 0.1198 0.1482 0.0076 0.0080 0.0004 181 PHE A CZ 1404 N N . ILE A 182 ? 0.0995 0.1120 0.1120 0.0021 0.0005 0.0078 182 ILE A N 1405 C CA . ILE A 182 ? 0.0928 0.1095 0.1140 0.0004 0.0009 0.0020 182 ILE A CA 1406 C C . ILE A 182 ? 0.0905 0.1225 0.1127 0.0007 0.0057 -0.0007 182 ILE A C 1407 O O . ILE A 182 ? 0.0967 0.1215 0.1148 0.0125 -0.0024 0.0035 182 ILE A O 1408 C CB . ILE A 182 ? 0.1098 0.1261 0.1170 -0.0068 0.0024 0.0048 182 ILE A CB 1409 C CG1 . ILE A 182 ? 0.1298 0.1320 0.1269 0.0062 -0.0084 0.0084 182 ILE A CG1 1410 C CG2 . ILE A 182 ? 0.1074 0.1195 0.1295 0.0047 0.0030 0.0019 182 ILE A CG2 1411 C CD1 . ILE A 182 ? 0.1472 0.1302 0.1414 0.0075 0.0046 0.0107 182 ILE A CD1 1412 N N . ASN A 183 ? 0.0952 0.1116 0.1020 0.0077 0.0059 0.0071 183 ASN A N 1413 C CA . ASN A 183 ? 0.1018 0.1104 0.1104 0.0027 0.0045 0.0038 183 ASN A CA 1414 C C . ASN A 183 ? 0.1050 0.1074 0.1056 0.0036 0.0008 0.0026 183 ASN A C 1415 O O . ASN A 183 ? 0.1076 0.1114 0.1137 0.0059 -0.0073 0.0028 183 ASN A O 1416 C CB . ASN A 183 ? 0.1091 0.1093 0.1052 0.0098 0.0020 0.0131 183 ASN A CB 1417 C CG . ASN A 183 ? 0.1009 0.1141 0.1265 -0.0109 -0.0009 0.0056 183 ASN A CG 1418 O OD1 . ASN A 183 ? 0.1077 0.1347 0.1274 0.0142 -0.0036 -0.0014 183 ASN A OD1 1419 N ND2 . ASN A 183 ? 0.1734 0.1177 0.1461 0.0007 -0.0265 0.0109 183 ASN A ND2 1420 N N . GLY A 184 ? 0.1092 0.1072 0.1074 0.0050 -0.0042 0.0031 184 GLY A N 1421 C CA . GLY A 184 ? 0.1063 0.1150 0.1138 0.0069 -0.0016 0.0062 184 GLY A CA 1422 C C . GLY A 184 ? 0.1120 0.1197 0.1223 0.0056 0.0034 0.0083 184 GLY A C 1423 O O . GLY A 184 ? 0.1275 0.1273 0.1554 0.0179 0.0091 0.0118 184 GLY A O 1424 N N . LEU A 185 ? 0.1009 0.1111 0.1200 0.0076 0.0043 0.0053 185 LEU A N 1425 C CA . LEU A 185 ? 0.1089 0.1268 0.1229 0.0050 0.0052 0.0053 185 LEU A CA 1426 C C . LEU A 185 ? 0.1061 0.1210 0.1220 0.0083 0.0112 0.0091 185 LEU A C 1427 O O . LEU A 185 ? 0.1231 0.1250 0.1230 0.0038 0.0052 -0.0036 185 LEU A O 1428 C CB . LEU A 185 ? 0.1108 0.1369 0.1331 0.0036 0.0142 0.0033 185 LEU A CB 1429 C CG . LEU A 185 ? 0.1198 0.1461 0.1418 0.0023 0.0078 0.0082 185 LEU A CG 1430 C CD1 . LEU A 185 ? 0.1507 0.1729 0.1575 0.0125 0.0055 -0.0183 185 LEU A CD1 1431 C CD2 . LEU A 185 ? 0.1366 0.1658 0.1348 0.0104 -0.0008 0.0055 185 LEU A CD2 1432 N N . GLY A 186 ? 0.1163 0.1247 0.1241 0.0094 0.0086 0.0064 186 GLY A N 1433 C CA . GLY A 186 ? 0.1112 0.1268 0.1244 0.0014 0.0118 0.0002 186 GLY A CA 1434 C C . GLY A 186 ? 0.1112 0.1213 0.1251 0.0110 0.0093 -0.0047 186 GLY A C 1435 O O . GLY A 186 ? 0.1190 0.1305 0.1546 0.0187 -0.0022 0.0145 186 GLY A O 1436 N N . ASN A 187 ? 0.1130 0.1174 0.1242 0.0022 0.0044 -0.0030 187 ASN A N 1437 C CA . ASN A 187 ? 0.1212 0.1258 0.1394 0.0010 0.0090 -0.0006 187 ASN A CA 1438 C C . ASN A 187 ? 0.1231 0.1290 0.1341 -0.0003 0.0026 -0.0040 187 ASN A C 1439 O O . ASN A 187 ? 0.1306 0.1278 0.1457 0.0193 0.0181 -0.0010 187 ASN A O 1440 C CB . ASN A 187 ? 0.1230 0.1206 0.1374 0.0048 0.0017 0.0037 187 ASN A CB 1441 C CG . ASN A 187 ? 0.1117 0.1231 0.1383 -0.0102 0.0016 0.0017 187 ASN A CG 1442 O OD1 . ASN A 187 ? 0.1013 0.1345 0.1395 -0.0028 0.0044 -0.0046 187 ASN A OD1 1443 N ND2 . ASN A 187 ? 0.1088 0.1339 0.1274 0.0001 0.0217 0.0158 187 ASN A ND2 1444 N N . ILE A 188 ? 0.1305 0.1572 0.1518 0.0024 0.0088 -0.0017 188 ILE A N 1445 C CA . ILE A 188 ? 0.1411 0.1562 0.1610 -0.0013 0.0106 0.0024 188 ILE A CA 1446 C C . ILE A 188 ? 0.1454 0.1632 0.1703 -0.0009 0.0115 0.0047 188 ILE A C 1447 O O . ILE A 188 ? 0.1534 0.1556 0.1819 0.0029 0.0290 0.0076 188 ILE A O 1448 C CB . ILE A 188 ? 0.1465 0.1571 0.1650 0.0014 0.0081 0.0070 188 ILE A CB 1449 C CG1 . ILE A 188 ? 0.1533 0.1700 0.1621 -0.0018 0.0027 0.0102 188 ILE A CG1 1450 C CG2 . ILE A 188 ? 0.1501 0.1787 0.1874 -0.0011 0.0129 0.0031 188 ILE A CG2 1451 C CD1 . ILE A 188 ? 0.1706 0.1735 0.1556 0.0115 -0.0006 0.0096 188 ILE A CD1 1452 N N . GLU A 189 ? 0.1500 0.1601 0.1762 -0.0072 0.0063 0.0068 189 GLU A N 1453 C CA . GLU A 189 ? 0.1625 0.1678 0.1944 -0.0026 0.0071 0.0092 189 GLU A CA 1454 C C . GLU A 189 ? 0.1508 0.1554 0.1898 0.0008 0.0131 0.0044 189 GLU A C 1455 O O . GLU A 189 ? 0.1372 0.1588 0.2246 0.0126 0.0302 0.0092 189 GLU A O 1456 C CB . GLU A 189 ? 0.1686 0.1764 0.1990 -0.0015 0.0062 0.0074 189 GLU A CB 1457 C CG . GLU A 189 ? 0.1785 0.2122 0.2326 0.0064 -0.0020 0.0064 189 GLU A CG 1458 C CD . GLU A 189 ? 0.2449 0.2474 0.2655 0.0025 -0.0084 0.0000 189 GLU A CD 1459 O OE1 . GLU A 189 ? 0.3742 0.3194 0.4086 -0.0035 -0.0176 0.0084 189 GLU A OE1 1460 O OE2 . GLU A 189 ? 0.3917 0.3453 0.3323 0.0105 -0.0313 0.0050 189 GLU A OE2 1461 N N . GLY A 190 ? 0.1361 0.1453 0.1789 -0.0018 0.0189 0.0066 190 GLY A N 1462 C CA . GLY A 190 ? 0.1450 0.1438 0.1536 -0.0025 0.0131 0.0104 190 GLY A CA 1463 C C . GLY A 190 ? 0.1357 0.1407 0.1545 0.0027 0.0126 0.0122 190 GLY A C 1464 O O . GLY A 190 ? 0.1350 0.1469 0.1591 0.0133 0.0222 0.0212 190 GLY A O 1465 N N . LYS A 191 ? 0.1195 0.1256 0.1466 0.0097 0.0140 0.0113 191 LYS A N 1466 C CA . LYS A 191 ? 0.1303 0.1317 0.1574 -0.0035 0.0124 0.0037 191 LYS A CA 1467 C C . LYS A 191 ? 0.1210 0.1276 0.1369 -0.0027 0.0114 0.0038 191 LYS A C 1468 O O . LYS A 191 ? 0.1090 0.1169 0.1367 0.0073 0.0151 0.0022 191 LYS A O 1469 C CB . LYS A 191 ? 0.1381 0.1542 0.1667 0.0032 0.0177 -0.0076 191 LYS A CB 1470 C CG . LYS A 191 ? 0.1574 0.2009 0.2170 -0.0050 0.0063 -0.0061 191 LYS A CG 1471 C CD . LYS A 191 ? 0.1729 0.2280 0.2282 -0.0058 -0.0025 -0.0070 191 LYS A CD 1472 C CE . LYS A 191 ? 0.1836 0.2674 0.2655 -0.0014 -0.0017 -0.0083 191 LYS A CE 1473 N NZ . LYS A 191 ? 0.2163 0.3086 0.2749 -0.0036 -0.0123 -0.0184 191 LYS A NZ 1474 N N . GLY A 192 ? 0.1117 0.1140 0.1352 -0.0084 0.0121 0.0061 192 GLY A N 1475 C CA . GLY A 192 ? 0.1151 0.1171 0.1342 -0.0036 0.0053 0.0009 192 GLY A CA 1476 C C . GLY A 192 ? 0.1218 0.1045 0.1181 -0.0037 -0.0059 0.0000 192 GLY A C 1477 O O . GLY A 192 ? 0.1326 0.1076 0.1267 -0.0106 -0.0021 -0.0021 192 GLY A O 1478 N N . SER A 193 ? 0.1073 0.1047 0.1049 -0.0032 0.0037 -0.0026 193 SER A N 1479 C CA . SER A 193 ? 0.1102 0.1117 0.1035 -0.0025 0.0018 -0.0022 193 SER A CA 1480 C C . SER A 193 ? 0.0991 0.0990 0.1128 -0.0097 -0.0004 0.0043 193 SER A C 1481 O O . SER A 193 ? 0.0982 0.1160 0.1185 -0.0027 -0.0110 -0.0146 193 SER A O 1482 C CB . SER A 193 ? 0.1043 0.1168 0.1192 -0.0051 0.0062 -0.0013 193 SER A CB 1483 O OG . SER A 193 ? 0.1284 0.1152 0.1123 -0.0057 0.0102 0.0175 193 SER A OG 1484 N N . CYS A 194 ? 0.0913 0.1046 0.1004 -0.0005 -0.0043 0.0035 194 CYS A N 1485 C CA . CYS A 194 ? 0.0991 0.1058 0.1059 -0.0015 -0.0031 0.0004 194 CYS A CA 1486 C C . CYS A 194 ? 0.1013 0.1074 0.1002 -0.0069 -0.0029 0.0072 194 CYS A C 1487 O O . CYS A 194 ? 0.1035 0.1212 0.1080 -0.0006 -0.0098 0.0109 194 CYS A O 1488 C CB . CYS A 194 ? 0.1150 0.1025 0.1212 -0.0063 -0.0008 0.0098 194 CYS A CB 1489 S SG . CYS A 194 ? 0.1069 0.1183 0.1268 -0.0024 0.0003 0.0099 194 CYS A SG 1490 N N . CYS A 195 ? 0.0888 0.1054 0.1039 -0.0031 -0.0057 -0.0009 195 CYS A N 1491 C CA . CYS A 195 ? 0.0966 0.1033 0.1079 -0.0014 0.0012 0.0025 195 CYS A CA 1492 C C . CYS A 195 ? 0.0981 0.1149 0.1056 0.0007 0.0020 0.0095 195 CYS A C 1493 O O . CYS A 195 ? 0.1004 0.1109 0.1122 -0.0122 0.0066 0.0071 195 CYS A O 1494 C CB . CYS A 195 ? 0.1101 0.1143 0.1065 -0.0002 0.0086 0.0023 195 CYS A CB 1495 S SG . CYS A 195 ? 0.1091 0.1101 0.1064 -0.0080 0.0049 0.0018 195 CYS A SG 1496 N N . ASN A 196 ? 0.1035 0.1156 0.1125 0.0010 -0.0028 0.0063 196 ASN A N 1497 C CA . ASN A 196 ? 0.1059 0.1132 0.1207 0.0072 0.0018 0.0074 196 ASN A CA 1498 C C . ASN A 196 ? 0.1015 0.1124 0.1247 0.0055 0.0113 0.0098 196 ASN A C 1499 O O . ASN A 196 ? 0.1022 0.1080 0.1388 0.0055 0.0011 0.0179 196 ASN A O 1500 C CB . ASN A 196 ? 0.1257 0.1391 0.1344 0.0065 -0.0002 0.0029 196 ASN A CB 1501 C CG . ASN A 196 ? 0.1084 0.1442 0.1405 0.0046 -0.0077 -0.0026 196 ASN A CG 1502 O OD1 . ASN A 196 ? 0.1757 0.1587 0.1304 -0.0337 -0.0211 0.0216 196 ASN A OD1 1503 N ND2 . ASN A 196 ? 0.1279 0.1893 0.1961 0.0088 -0.0361 -0.0254 196 ASN A ND2 1504 N N . SER A 197 ? 0.0936 0.1021 0.1274 0.0037 0.0056 0.0048 197 SER A N 1505 C CA . SER A 197 ? 0.1026 0.1163 0.1324 0.0028 -0.0039 0.0023 197 SER A CA 1506 C C . SER A 197 ? 0.1059 0.1189 0.1214 0.0012 -0.0008 0.0041 197 SER A C 1507 O O . SER A 197 ? 0.1193 0.1227 0.1516 0.0025 -0.0033 0.0190 197 SER A O 1508 C CB . SER A 197 ? 0.1414 0.1536 0.1576 -0.0042 0.0066 -0.0030 197 SER A CB 1509 O OG . SER A 197 ? 0.1669 0.2099 0.2089 0.0003 -0.0134 -0.0016 197 SER A OG 1510 N N . MET A 198 ? 0.0964 0.1031 0.1168 0.0000 0.0009 0.0130 198 MET A N 1511 C CA . MET A 198 ? 0.1025 0.1024 0.1152 0.0038 -0.0063 0.0056 198 MET A CA 1512 C C . MET A 198 ? 0.0990 0.0949 0.1204 0.0095 0.0050 0.0031 198 MET A C 1513 O O . MET A 198 ? 0.1061 0.0984 0.1241 -0.0024 -0.0018 0.0148 198 MET A O 1514 C CB . MET A 198 ? 0.1068 0.1014 0.1252 -0.0019 -0.0004 -0.0048 198 MET A CB 1515 C CG . MET A 198 ? 0.1142 0.1205 0.1390 -0.0205 0.0079 0.0038 198 MET A CG 1516 S SD . MET A 198 ? 0.1096 0.1162 0.1353 0.0046 0.0052 -0.0016 198 MET A SD 1517 C CE . MET A 198 ? 0.1298 0.1209 0.1302 -0.0057 -0.0125 -0.0128 198 MET A CE 1518 N N . ASP A 199 ? 0.1031 0.0985 0.1197 0.0046 -0.0019 -0.0014 199 ASP A N 1519 C CA . ASP A 199 ? 0.1091 0.1013 0.1171 0.0115 -0.0049 0.0048 199 ASP A CA 1520 C C . ASP A 199 ? 0.1028 0.1001 0.1132 0.0015 0.0059 0.0101 199 ASP A C 1521 O O . ASP A 199 ? 0.0981 0.0973 0.1225 0.0049 0.0033 0.0037 199 ASP A O 1522 C CB . ASP A 199 ? 0.1190 0.1076 0.1188 0.0057 0.0065 -0.0002 199 ASP A CB 1523 C CG . ASP A 199 ? 0.1418 0.1263 0.1237 0.0364 0.0060 0.0030 199 ASP A CG 1524 O OD1 . ASP A 199 ? 0.1472 0.1896 0.1677 -0.0152 -0.0183 -0.0061 199 ASP A OD1 1525 O OD2 . ASP A 199 ? 0.1560 0.1553 0.1875 -0.0055 0.0369 0.0096 199 ASP A OD2 1526 N N . ILE A 200 ? 0.0975 0.1010 0.1305 0.0078 0.0000 0.0123 200 ILE A N 1527 C CA . ILE A 200 ? 0.1011 0.1053 0.1119 0.0033 0.0023 -0.0019 200 ILE A CA 1528 C C . ILE A 200 ? 0.0977 0.1005 0.1033 0.0053 0.0060 0.0062 200 ILE A C 1529 O O . ILE A 200 ? 0.1034 0.1175 0.1221 0.0219 -0.0077 -0.0023 200 ILE A O 1530 C CB . ILE A 200 ? 0.0893 0.1143 0.1091 0.0014 0.0011 0.0006 200 ILE A CB 1531 C CG1 . ILE A 200 ? 0.1095 0.1141 0.1177 0.0068 -0.0078 -0.0020 200 ILE A CG1 1532 C CG2 . ILE A 200 ? 0.0896 0.1230 0.1279 0.0098 -0.0038 0.0026 200 ILE A CG2 1533 C CD1 . ILE A 200 ? 0.1326 0.1347 0.1261 -0.0056 -0.0015 0.0075 200 ILE A CD1 1534 N N . TRP A 201 ? 0.1003 0.1113 0.1118 0.0022 -0.0025 -0.0035 201 TRP A N 1535 C CA . TRP A 201 ? 0.1077 0.1082 0.1016 0.0009 -0.0013 -0.0004 201 TRP A CA 1536 C C . TRP A 201 ? 0.1033 0.1115 0.1138 0.0014 -0.0027 -0.0043 201 TRP A C 1537 O O . TRP A 201 ? 0.1040 0.1149 0.1196 0.0048 -0.0037 -0.0097 201 TRP A O 1538 C CB . TRP A 201 ? 0.1070 0.1178 0.1167 -0.0040 -0.0014 -0.0001 201 TRP A CB 1539 C CG . TRP A 201 ? 0.1118 0.1048 0.1187 -0.0070 -0.0050 -0.0035 201 TRP A CG 1540 C CD1 . TRP A 201 ? 0.1115 0.1153 0.1313 -0.0001 -0.0010 0.0002 201 TRP A CD1 1541 C CD2 . TRP A 201 ? 0.1178 0.1038 0.1128 0.0200 -0.0008 0.0042 201 TRP A CD2 1542 N NE1 . TRP A 201 ? 0.1090 0.1179 0.1317 0.0119 -0.0048 -0.0163 201 TRP A NE1 1543 C CE2 . TRP A 201 ? 0.0948 0.1213 0.1236 0.0009 -0.0096 -0.0060 201 TRP A CE2 1544 C CE3 . TRP A 201 ? 0.1218 0.1086 0.1499 0.0000 0.0014 -0.0056 201 TRP A CE3 1545 C CZ2 . TRP A 201 ? 0.1240 0.1081 0.1164 -0.0107 -0.0078 -0.0036 201 TRP A CZ2 1546 C CZ3 . TRP A 201 ? 0.1146 0.1317 0.1462 0.0102 0.0036 0.0079 201 TRP A CZ3 1547 C CH2 . TRP A 201 ? 0.1082 0.1354 0.1521 -0.0125 0.0045 0.0091 201 TRP A CH2 1548 N N . GLU A 202 ? 0.1089 0.1065 0.1158 0.0117 -0.0083 -0.0079 202 GLU A N 1549 C CA . GLU A 202 ? 0.1022 0.1136 0.1047 0.0034 -0.0073 0.0028 202 GLU A CA 1550 C C . GLU A 202 ? 0.1073 0.1068 0.1259 0.0010 -0.0135 -0.0027 202 GLU A C 1551 O O . GLU A 202 ? 0.1129 0.1240 0.1243 0.0015 -0.0142 -0.0003 202 GLU A O 1552 C CB . GLU A 202 ? 0.1013 0.1172 0.1021 0.0104 -0.0004 -0.0146 202 GLU A CB 1553 C CG . GLU A 202 ? 0.1160 0.1254 0.1033 0.0074 -0.0063 -0.0068 202 GLU A CG 1554 C CD . GLU A 202 ? 0.1162 0.1568 0.1331 -0.0017 -0.0096 -0.0065 202 GLU A CD 1555 O OE1 . GLU A 202 ? 0.1299 0.1369 0.1374 0.0221 -0.0204 -0.0024 202 GLU A OE1 1556 O OE2 . GLU A 202 ? 0.1128 0.1548 0.1568 -0.0097 -0.0104 0.0108 202 GLU A OE2 1557 N N . ALA A 203 ? 0.1014 0.1088 0.1296 0.0088 -0.0064 -0.0083 203 ALA A N 1558 C CA . ALA A 203 ? 0.1102 0.1097 0.1264 -0.0009 -0.0085 0.0003 203 ALA A CA 1559 C C . ALA A 203 ? 0.1224 0.1154 0.1222 0.0045 -0.0193 -0.0041 203 ALA A C 1560 O O . ALA A 203 ? 0.1194 0.1231 0.1231 0.0148 -0.0099 -0.0122 203 ALA A O 1561 C CB . ALA A 203 ? 0.1213 0.1247 0.1378 0.0122 -0.0094 -0.0002 203 ALA A CB 1562 N N . ASN A 204 ? 0.1166 0.1142 0.1335 0.0160 -0.0238 -0.0058 204 ASN A N 1563 C CA . ASN A 204 ? 0.1309 0.1188 0.1367 0.0019 -0.0134 -0.0046 204 ASN A CA 1564 C C . ASN A 204 ? 0.1344 0.1375 0.1276 0.0047 -0.0118 -0.0115 204 ASN A C 1565 O O . ASN A 204 ? 0.1350 0.1360 0.1450 0.0099 -0.0289 -0.0136 204 ASN A O 1566 C CB . ASN A 204 ? 0.1299 0.1224 0.1368 0.0033 -0.0176 -0.0130 204 ASN A CB 1567 C CG . ASN A 204 ? 0.1284 0.1263 0.1171 -0.0142 -0.0104 -0.0261 204 ASN A CG 1568 O OD1 . ASN A 204 ? 0.1322 0.1405 0.1270 0.0038 -0.0209 -0.0222 204 ASN A OD1 1569 N ND2 . ASN A 204 ? 0.1237 0.1280 0.1182 0.0093 -0.0002 -0.0048 204 ASN A ND2 1570 N N . SER A 205 ? 0.1104 0.1364 0.1368 0.0048 -0.0144 -0.0134 205 SER A N 1571 C CA . SER A 205 ? 0.1228 0.1348 0.1504 -0.0023 -0.0122 -0.0053 205 SER A CA 1572 C C . SER A 205 ? 0.1317 0.1451 0.1479 0.0081 -0.0130 -0.0072 205 SER A C 1573 O O . SER A 205 ? 0.1207 0.1552 0.1444 0.0117 -0.0247 -0.0145 205 SER A O 1574 C CB . SER A 205 ? 0.1287 0.1493 0.1465 0.0011 -0.0174 -0.0082 205 SER A CB 1575 O OG . SER A 205 ? 0.1366 0.1498 0.1428 -0.0073 -0.0246 -0.0131 205 SER A OG 1576 N N . ARG A 206 ? 0.1257 0.1432 0.1383 0.0077 -0.0137 -0.0085 206 ARG A N 1577 C CA . ARG A 206 ? 0.1264 0.1407 0.1488 0.0048 -0.0116 -0.0050 206 ARG A CA 1578 C C . ARG A 206 ? 0.1221 0.1351 0.1407 0.0047 -0.0176 -0.0057 206 ARG A C 1579 O O . ARG A 206 ? 0.1396 0.1354 0.1567 0.0098 -0.0243 -0.0091 206 ARG A O 1580 C CB . ARG A 206 ? 0.1255 0.1167 0.1435 0.0080 -0.0100 0.0008 206 ARG A CB 1581 C CG . ARG A 206 ? 0.1454 0.1426 0.1279 -0.0009 -0.0093 -0.0101 206 ARG A CG 1582 C CD . ARG A 206 ? 0.1522 0.1667 0.1561 0.0107 -0.0139 -0.0025 206 ARG A CD 1583 N NE . ARG A 206 ? 0.1647 0.1580 0.1618 0.0257 -0.0268 -0.0167 206 ARG A NE 1584 C CZ . ARG A 206 ? 0.1499 0.1774 0.1699 0.0196 -0.0187 -0.0074 206 ARG A CZ 1585 N NH1 . ARG A 206 ? 0.1628 0.2058 0.1747 0.0088 -0.0246 0.0014 206 ARG A NH1 1586 N NH2 . ARG A 206 ? 0.1564 0.1789 0.1823 0.0153 -0.0355 0.0123 206 ARG A NH2 1587 N N . ALA A 207 ? 0.1155 0.1261 0.1384 0.0095 -0.0241 -0.0089 207 ALA A N 1588 C CA . ALA A 207 ? 0.1241 0.1327 0.1372 0.0061 -0.0137 -0.0044 207 ALA A CA 1589 C C . ALA A 207 ? 0.1252 0.1257 0.1331 0.0029 -0.0169 -0.0054 207 ALA A C 1590 O O . ALA A 207 ? 0.1303 0.1239 0.1311 0.0076 -0.0142 -0.0052 207 ALA A O 1591 C CB . ALA A 207 ? 0.1285 0.1418 0.1359 -0.0009 -0.0216 -0.0035 207 ALA A CB 1592 N N . SER A 208 ? 0.1153 0.1271 0.1135 0.0206 -0.0100 -0.0057 208 SER A N 1593 C CA . SER A 208 ? 0.1271 0.1247 0.1162 0.0043 -0.0126 0.0002 208 SER A CA 1594 C C . SER A 208 ? 0.1120 0.1264 0.1251 0.0063 -0.0056 -0.0018 208 SER A C 1595 O O . SER A 208 ? 0.1227 0.1248 0.1375 0.0056 -0.0116 -0.0131 208 SER A O 1596 C CB . SER A 208 ? 0.1201 0.1328 0.1264 0.0029 -0.0173 -0.0067 208 SER A CB 1597 O OG . SER A 208 ? 0.1254 0.1288 0.1215 0.0046 -0.0178 0.0018 208 SER A OG 1598 N N . HIS A 209 ? 0.1114 0.1189 0.1223 0.0070 -0.0048 0.0050 209 HIS A N 1599 C CA . HIS A 209 ? 0.1170 0.1163 0.1164 -0.0009 -0.0053 0.0003 209 HIS A CA 1600 C C . HIS A 209 ? 0.1003 0.1075 0.1275 0.0054 -0.0088 0.0000 209 HIS A C 1601 O O . HIS A 209 ? 0.1190 0.0956 0.1214 0.0123 -0.0099 -0.0014 209 HIS A O 1602 C CB . HIS A 209 ? 0.1102 0.1134 0.1218 -0.0021 -0.0057 0.0013 209 HIS A CB 1603 C CG . HIS A 209 ? 0.1289 0.1344 0.1303 -0.0005 -0.0086 0.0098 209 HIS A CG 1604 N ND1 . HIS A 209 ? 0.1363 0.1566 0.1654 -0.0191 -0.0004 -0.0086 209 HIS A ND1 1605 C CD2 . HIS A 209 ? 0.1336 0.1743 0.1450 -0.0113 0.0078 0.0027 209 HIS A CD2 1606 C CE1 . HIS A 209 ? 0.1449 0.1578 0.1927 -0.0318 0.0134 -0.0060 209 HIS A CE1 1607 N NE2 . HIS A 209 ? 0.1337 0.1799 0.1384 -0.0325 0.0134 -0.0092 209 HIS A NE2 1608 N N . VAL A 210 ? 0.0976 0.1054 0.1048 0.0006 -0.0080 0.0000 210 VAL A N 1609 C CA . VAL A 210 ? 0.1099 0.1072 0.1125 0.0081 -0.0093 -0.0007 210 VAL A CA 1610 C C . VAL A 210 ? 0.1120 0.1134 0.1122 0.0047 -0.0098 -0.0007 210 VAL A C 1611 O O . VAL A 210 ? 0.1160 0.1058 0.1233 0.0065 -0.0149 0.0113 210 VAL A O 1612 C CB . VAL A 210 ? 0.1071 0.1159 0.1126 -0.0015 -0.0085 -0.0024 210 VAL A CB 1613 C CG1 . VAL A 210 ? 0.1104 0.1114 0.1176 0.0232 0.0019 -0.0078 210 VAL A CG1 1614 C CG2 . VAL A 210 ? 0.1096 0.1205 0.1279 0.0034 -0.0026 -0.0101 210 VAL A CG2 1615 N N . ALA A 211 ? 0.0997 0.1010 0.1140 0.0034 -0.0116 0.0007 211 ALA A N 1616 C CA . ALA A 211 ? 0.1088 0.1035 0.1141 0.0021 -0.0083 0.0038 211 ALA A CA 1617 C C . ALA A 211 ? 0.0976 0.1017 0.1110 -0.0020 -0.0050 0.0011 211 ALA A C 1618 O O . ALA A 211 ? 0.1008 0.0998 0.1140 0.0011 -0.0072 0.0009 211 ALA A O 1619 C CB . ALA A 211 ? 0.1268 0.1236 0.1102 0.0089 -0.0169 0.0050 211 ALA A CB 1620 N N . PRO A 212 ? 0.0919 0.0992 0.1149 0.0018 0.0001 -0.0001 212 PRO A N 1621 C CA . PRO A 212 ? 0.1070 0.1073 0.1066 -0.0016 -0.0068 0.0039 212 PRO A CA 1622 C C . PRO A 212 ? 0.1148 0.1110 0.1107 0.0015 -0.0056 0.0068 212 PRO A C 1623 O O . PRO A 212 ? 0.1222 0.1096 0.1081 0.0025 -0.0054 0.0108 212 PRO A O 1624 C CB . PRO A 212 ? 0.0967 0.0968 0.1018 -0.0120 -0.0050 0.0094 212 PRO A CB 1625 C CG . PRO A 212 ? 0.1272 0.1143 0.1145 0.0092 -0.0061 -0.0037 212 PRO A CG 1626 C CD . PRO A 212 ? 0.1015 0.1121 0.1138 -0.0055 -0.0011 -0.0106 212 PRO A CD 1627 N N . HIS A 213 ? 0.1006 0.1069 0.1107 0.0014 0.0012 0.0138 213 HIS A N 1628 C CA . HIS A 213 ? 0.1100 0.1064 0.1076 -0.0031 0.0022 0.0076 213 HIS A CA 1629 C C . HIS A 213 ? 0.1064 0.1037 0.1142 0.0051 -0.0067 0.0143 213 HIS A C 1630 O O . HIS A 213 ? 0.1350 0.1014 0.1353 -0.0046 0.0008 0.0053 213 HIS A O 1631 C CB . HIS A 213 ? 0.1071 0.1061 0.1134 0.0000 0.0126 0.0092 213 HIS A CB 1632 C CG . HIS A 213 ? 0.1009 0.1104 0.1277 0.0186 0.0087 -0.0032 213 HIS A CG 1633 N ND1 . HIS A 213 ? 0.1295 0.1221 0.1143 0.0145 -0.0084 0.0004 213 HIS A ND1 1634 C CD2 . HIS A 213 ? 0.1195 0.1324 0.1065 -0.0235 0.0124 0.0028 213 HIS A CD2 1635 C CE1 . HIS A 213 ? 0.1135 0.1373 0.1180 -0.0041 0.0080 -0.0037 213 HIS A CE1 1636 N NE2 . HIS A 213 ? 0.1152 0.1384 0.1331 -0.0041 0.0138 -0.0217 213 HIS A NE2 1637 N N . THR A 214 ? 0.0976 0.0942 0.1027 0.0131 -0.0046 0.0097 214 THR A N 1638 C CA . THR A 214 ? 0.1159 0.1174 0.1155 0.0023 0.0005 0.0061 214 THR A CA 1639 C C . THR A 214 ? 0.1076 0.1268 0.1025 0.0019 0.0042 0.0167 214 THR A C 1640 O O . THR A 214 ? 0.1353 0.1342 0.1053 0.0025 0.0013 0.0193 214 THR A O 1641 C CB . THR A 214 ? 0.1256 0.1126 0.1016 -0.0016 -0.0010 0.0102 214 THR A CB 1642 O OG1 . THR A 214 ? 0.1183 0.1204 0.1031 0.0052 -0.0050 0.0194 214 THR A OG1 1643 C CG2 . THR A 214 ? 0.1228 0.1368 0.1360 0.0200 -0.0028 0.0060 214 THR A CG2 1644 N N . CYS A 215 ? 0.0959 0.1302 0.1035 -0.0015 -0.0011 0.0145 215 CYS A N 1645 C CA . CYS A 215 ? 0.1106 0.1220 0.1153 -0.0085 0.0070 0.0100 215 CYS A CA 1646 C C . CYS A 215 ? 0.1250 0.1277 0.1174 -0.0050 0.0026 0.0063 215 CYS A C 1647 O O . CYS A 215 ? 0.1190 0.1440 0.1140 -0.0094 0.0044 0.0048 215 CYS A O 1648 C CB . CYS A 215 ? 0.1139 0.1298 0.1228 -0.0048 -0.0071 0.0127 215 CYS A CB 1649 S SG . CYS A 215 ? 0.1258 0.1159 0.1249 -0.0176 0.0047 0.0027 215 CYS A SG 1650 N N . ASN A 216 ? 0.1228 0.1206 0.1271 -0.0081 -0.0029 0.0025 216 ASN A N 1651 C CA . ASN A 216 ? 0.1331 0.1137 0.1264 -0.0127 -0.0071 0.0023 216 ASN A CA 1652 C C . ASN A 216 ? 0.1302 0.1291 0.1415 -0.0098 -0.0178 0.0010 216 ASN A C 1653 O O . ASN A 216 ? 0.1533 0.1488 0.1401 -0.0152 -0.0316 0.0096 216 ASN A O 1654 C CB . ASN A 216 ? 0.1423 0.1040 0.1399 -0.0193 -0.0162 0.0026 216 ASN A CB 1655 C CG . ASN A 216 ? 0.1406 0.1225 0.1535 -0.0033 -0.0216 0.0046 216 ASN A CG 1656 O OD1 . ASN A 216 ? 0.1448 0.1245 0.1357 -0.0060 -0.0134 -0.0032 216 ASN A OD1 1657 N ND2 . ASN A 216 ? 0.1854 0.1465 0.2134 -0.0401 -0.0024 0.0238 216 ASN A ND2 1658 N N . LYS A 217 ? 0.1410 0.1303 0.1482 -0.0100 -0.0245 0.0041 217 LYS A N 1659 C CA . LYS A 217 ? 0.1407 0.1299 0.1444 0.0019 -0.0114 -0.0026 217 LYS A CA 1660 C C . LYS A 217 ? 0.1324 0.1290 0.1550 0.0023 -0.0147 -0.0030 217 LYS A C 1661 O O . LYS A 217 ? 0.1474 0.1480 0.1985 -0.0094 -0.0409 0.0099 217 LYS A O 1662 C CB . LYS A 217 ? 0.1611 0.1393 0.1477 0.0117 -0.0137 -0.0098 217 LYS A CB 1663 C CG . LYS A 217 ? 0.1864 0.1678 0.1550 0.0078 -0.0048 -0.0134 217 LYS A CG 1664 C CD . LYS A 217 ? 0.1717 0.2125 0.1724 -0.0018 -0.0085 0.0035 217 LYS A CD 1665 C CE . LYS A 217 ? 0.1908 0.1829 0.2002 -0.0039 -0.0077 -0.0136 217 LYS A CE 1666 N NZ . LYS A 217 ? 0.2237 0.2263 0.2988 -0.0040 -0.0290 0.0026 217 LYS A NZ 1667 N N . LYS A 218 ? 0.1258 0.1312 0.1385 0.0025 0.0006 -0.0084 218 LYS A N 1668 C CA . LYS A 218 ? 0.1159 0.1129 0.1364 0.0063 0.0004 -0.0083 218 LYS A CA 1669 C C . LYS A 218 ? 0.1144 0.1072 0.1403 -0.0015 0.0048 -0.0116 218 LYS A C 1670 O O . LYS A 218 ? 0.1224 0.1395 0.1657 -0.0097 -0.0079 -0.0212 218 LYS A O 1671 C CB . LYS A 218 ? 0.1207 0.1138 0.1426 0.0011 -0.0031 -0.0018 218 LYS A CB 1672 C CG . LYS A 218 ? 0.1273 0.1262 0.1385 0.0049 0.0123 -0.0070 218 LYS A CG 1673 C CD . LYS A 218 ? 0.1282 0.1267 0.1510 0.0000 -0.0047 -0.0113 218 LYS A CD 1674 C CE . LYS A 218 ? 0.1669 0.1199 0.1683 0.0016 -0.0034 -0.0142 218 LYS A CE 1675 N NZ . LYS A 218 ? 0.1964 0.1801 0.1685 0.0059 -0.0007 -0.0250 218 LYS A NZ 1676 N N . GLY A 219 ? 0.1135 0.1078 0.1342 -0.0036 0.0037 -0.0090 219 GLY A N 1677 C CA . GLY A 219 ? 0.1115 0.1118 0.1203 0.0040 -0.0087 0.0006 219 GLY A CA 1678 C C . GLY A 219 ? 0.1076 0.1103 0.1185 -0.0021 -0.0145 0.0011 219 GLY A C 1679 O O . GLY A 219 ? 0.1531 0.1180 0.1285 0.0137 -0.0170 0.0064 219 GLY A O 1680 N N . LEU A 220 ? 0.1211 0.1129 0.1169 0.0016 -0.0039 0.0005 220 LEU A N 1681 C CA . LEU A 220 ? 0.1055 0.1133 0.1197 0.0005 -0.0025 0.0033 220 LEU A CA 1682 C C . LEU A 220 ? 0.1082 0.1180 0.1149 -0.0008 0.0032 0.0057 220 LEU A C 1683 O O . LEU A 220 ? 0.1179 0.1257 0.1345 -0.0090 -0.0098 0.0061 220 LEU A O 1684 C CB . LEU A 220 ? 0.1103 0.1147 0.1094 0.0015 0.0057 0.0100 220 LEU A CB 1685 C CG . LEU A 220 ? 0.1225 0.1201 0.1119 0.0067 -0.0098 -0.0066 220 LEU A CG 1686 C CD1 . LEU A 220 ? 0.1426 0.1025 0.0933 0.0140 -0.0096 -0.0010 220 LEU A CD1 1687 C CD2 . LEU A 220 ? 0.1474 0.1329 0.1398 -0.0008 0.0144 -0.0016 220 LEU A CD2 1688 N N . TYR A 221 ? 0.1138 0.1185 0.1243 -0.0037 0.0043 0.0031 221 TYR A N 1689 C CA . TYR A 221 ? 0.1082 0.1162 0.1161 -0.0029 -0.0063 -0.0023 221 TYR A CA 1690 C C . TYR A 221 ? 0.1150 0.1188 0.1186 -0.0069 0.0004 0.0058 221 TYR A C 1691 O O . TYR A 221 ? 0.1121 0.1184 0.1210 -0.0027 -0.0041 0.0022 221 TYR A O 1692 C CB . TYR A 221 ? 0.1220 0.1225 0.1159 -0.0074 -0.0049 0.0040 221 TYR A CB 1693 C CG . TYR A 221 ? 0.1251 0.1219 0.1347 -0.0018 -0.0045 0.0069 221 TYR A CG 1694 C CD1 . TYR A 221 ? 0.1555 0.1472 0.1480 -0.0154 -0.0146 0.0185 221 TYR A CD1 1695 C CD2 . TYR A 221 ? 0.1105 0.1343 0.1499 -0.0031 -0.0065 0.0163 221 TYR A CD2 1696 C CE1 . TYR A 221 ? 0.1465 0.1702 0.1507 -0.0242 -0.0157 0.0163 221 TYR A CE1 1697 C CE2 . TYR A 221 ? 0.1363 0.1511 0.1443 -0.0266 0.0028 0.0214 221 TYR A CE2 1698 C CZ . TYR A 221 ? 0.1486 0.1675 0.1614 -0.0292 -0.0055 0.0199 221 TYR A CZ 1699 O OH . TYR A 221 ? 0.1644 0.1918 0.2079 -0.0322 -0.0002 0.0234 221 TYR A OH 1700 N N . LEU A 222 ? 0.1210 0.1313 0.1281 0.0030 -0.0109 -0.0016 222 LEU A N 1701 C CA . LEU A 222 ? 0.1242 0.1331 0.1382 -0.0026 -0.0010 0.0025 222 LEU A CA 1702 C C . LEU A 222 ? 0.1295 0.1274 0.1435 0.0030 -0.0019 0.0000 222 LEU A C 1703 O O . LEU A 222 ? 0.1447 0.1371 0.1712 0.0055 -0.0088 0.0039 222 LEU A O 1704 C CB . LEU A 222 ? 0.1268 0.1283 0.1498 -0.0058 -0.0006 0.0028 222 LEU A CB 1705 C CG . LEU A 222 ? 0.1478 0.1502 0.1805 -0.0043 0.0044 0.0041 222 LEU A CG 1706 C CD1 . LEU A 222 ? 0.1912 0.1888 0.1970 0.0150 -0.0129 -0.0090 222 LEU A CD1 1707 C CD2 . LEU A 222 ? 0.1741 0.1648 0.1679 0.0014 0.0037 -0.0009 222 LEU A CD2 1708 N N . CYS A 223 ? 0.1194 0.1189 0.1431 -0.0005 0.0006 0.0042 223 CYS A N 1709 C CA . CYS A 223 ? 0.1294 0.1281 0.1423 -0.0024 0.0077 0.0080 223 CYS A CA 1710 C C . CYS A 223 ? 0.1362 0.1381 0.1584 -0.0010 0.0068 0.0001 223 CYS A C 1711 O O . CYS A 223 ? 0.1142 0.1277 0.1716 0.0051 0.0199 0.0132 223 CYS A O 1712 C CB . CYS A 223 ? 0.1195 0.1202 0.1363 0.0001 0.0165 0.0078 223 CYS A CB 1713 S SG . CYS A 223 ? 0.1129 0.1213 0.1421 -0.0015 0.0206 0.0126 223 CYS A SG 1714 N N . GLU A 224 ? 0.1351 0.1413 0.1741 -0.0003 0.0130 0.0096 224 GLU A N 1715 C CA . GLU A 224 ? 0.1696 0.1777 0.1957 -0.0050 0.0147 0.0113 224 GLU A CA 1716 C C . GLU A 224 ? 0.1645 0.1678 0.2021 -0.0072 0.0188 0.0093 224 GLU A C 1717 O O . GLU A 224 ? 0.1597 0.1526 0.2038 -0.0006 0.0348 0.0140 224 GLU A O 1718 C CB . GLU A 224 ? 0.1955 0.2132 0.2304 0.0030 0.0120 0.0230 224 GLU A CB 1719 C CG . GLU A 224 ? 0.2309 0.2596 0.2713 0.0070 0.0102 0.0125 224 GLU A CG 1720 C CD . GLU A 224 ? 0.2426 0.2892 0.2987 -0.0050 -0.0104 0.0020 224 GLU A CD 1721 O OE1 . GLU A 224 ? 0.3121 0.3717 0.4024 0.0173 0.0121 -0.0160 224 GLU A OE1 1722 O OE2 . GLU A 224 ? 0.3866 0.4098 0.4000 -0.0177 -0.0228 -0.0141 224 GLU A OE2 1723 N N . GLY A 225 ? 0.1774 0.1514 0.2003 -0.0075 0.0183 0.0073 225 GLY A N 1724 C CA . GLY A 225 ? 0.1836 0.1773 0.1960 -0.0028 0.0202 0.0117 225 GLY A CA 1725 C C . GLY A 225 ? 0.1786 0.1792 0.1926 -0.0043 0.0145 0.0074 225 GLY A C 1726 O O . GLY A 225 ? 0.1763 0.1705 0.1945 -0.0172 0.0313 0.0129 225 GLY A O 1727 N N . GLU A 226 ? 0.1829 0.1927 0.2161 -0.0036 0.0243 0.0110 226 GLU A N 1728 C CA . GLU A 226 ? 0.1994 0.1975 0.2150 0.0006 0.0184 0.0110 226 GLU A CA 1729 C C . GLU A 226 ? 0.1790 0.1784 0.1885 0.0004 0.0192 0.0163 226 GLU A C 1730 O O . GLU A 226 ? 0.1656 0.1552 0.1720 -0.0111 0.0244 0.0426 226 GLU A O 1731 C CB . GLU A 226 ? 0.2258 0.2165 0.2565 0.0115 0.0218 0.0132 226 GLU A CB 1732 C CG . GLU A 226 ? 0.3162 0.2953 0.3062 0.0023 0.0271 0.0104 226 GLU A CG 1733 C CD . GLU A 226 ? 0.3924 0.3881 0.3775 0.0023 0.0047 0.0022 226 GLU A CD 1734 O OE1 . GLU A 226 ? 0.4302 0.4407 0.4559 0.0023 0.0245 -0.0011 226 GLU A OE1 1735 O OE2 . GLU A 226 ? 0.4739 0.4715 0.4176 -0.0094 0.0110 -0.0198 226 GLU A OE2 1736 N N . GLU A 227 ? 0.1595 0.1429 0.1755 -0.0009 0.0205 0.0115 227 GLU A N 1737 C CA . GLU A 227 ? 0.1457 0.1445 0.1606 0.0005 0.0097 0.0022 227 GLU A CA 1738 C C . GLU A 227 ? 0.1329 0.1383 0.1523 0.0046 0.0062 0.0043 227 GLU A C 1739 O O . GLU A 227 ? 0.1409 0.1284 0.1481 0.0093 0.0209 0.0112 227 GLU A O 1740 C CB . GLU A 227 ? 0.1457 0.1609 0.1565 0.0011 0.0071 0.0030 227 GLU A CB 1741 C CG . GLU A 227 ? 0.1862 0.1480 0.1729 -0.0188 0.0027 0.0050 227 GLU A CG 1742 C CD . GLU A 227 ? 0.1534 0.1680 0.1832 -0.0018 -0.0025 0.0000 227 GLU A CD 1743 O OE1 . GLU A 227 ? 0.1898 0.1505 0.1910 -0.0130 0.0026 -0.0013 227 GLU A OE1 1744 O OE2 . GLU A 227 ? 0.2415 0.1845 0.2093 -0.0209 -0.0070 0.0043 227 GLU A OE2 1745 N N . CYS A 228 ? 0.1266 0.1285 0.1351 0.0021 0.0115 0.0079 228 CYS A N 1746 C CA . CYS A 228 ? 0.1334 0.1349 0.1319 0.0013 0.0100 0.0049 228 CYS A CA 1747 C C . CYS A 228 ? 0.1362 0.1427 0.1421 0.0047 0.0139 0.0010 228 CYS A C 1748 O O . CYS A 228 ? 0.1467 0.1362 0.1453 0.0009 0.0088 0.0112 228 CYS A O 1749 C CB . CYS A 228 ? 0.1230 0.1311 0.1354 -0.0007 0.0144 0.0056 228 CYS A CB 1750 S SG . CYS A 228 ? 0.1392 0.1303 0.1682 0.0108 0.0220 0.0158 228 CYS A SG 1751 N N . ALA A 229 ? 0.1347 0.1437 0.1516 0.0026 0.0145 0.0059 229 ALA A N 1752 C CA . ALA A 229 ? 0.1463 0.1435 0.1422 0.0032 0.0144 0.0071 229 ALA A CA 1753 C C . ALA A 229 ? 0.1520 0.1454 0.1406 0.0107 0.0045 0.0090 229 ALA A C 1754 O O . ALA A 229 ? 0.1347 0.1370 0.1338 -0.0010 -0.0010 0.0062 229 ALA A O 1755 C CB . ALA A 229 ? 0.1621 0.1546 0.1590 0.0078 0.0226 0.0065 229 ALA A CB 1756 N N . PHE A 230 ? 0.1543 0.1409 0.1501 0.0174 0.0063 0.0166 230 PHE A N 1757 C CA . PHE A 230 ? 0.1505 0.1417 0.1409 0.0080 0.0131 0.0127 230 PHE A CA 1758 C C . PHE A 230 ? 0.1329 0.1265 0.1411 0.0028 0.0018 0.0136 230 PHE A C 1759 O O . PHE A 230 ? 0.1291 0.1069 0.1498 -0.0126 0.0099 0.0092 230 PHE A O 1760 C CB . PHE A 230 ? 0.1627 0.1486 0.1431 0.0072 -0.0013 0.0096 230 PHE A CB 1761 C CG . PHE A 230 ? 0.1723 0.1441 0.1416 0.0143 0.0003 0.0157 230 PHE A CG 1762 C CD1 . PHE A 230 ? 0.1856 0.1490 0.1588 0.0209 -0.0098 0.0243 230 PHE A CD1 1763 C CD2 . PHE A 230 ? 0.1853 0.1664 0.1272 0.0159 -0.0107 0.0084 230 PHE A CD2 1764 C CE1 . PHE A 230 ? 0.1912 0.2087 0.1720 -0.0043 0.0100 0.0168 230 PHE A CE1 1765 C CE2 . PHE A 230 ? 0.1952 0.1715 0.1513 0.0250 -0.0051 0.0015 230 PHE A CE2 1766 C CZ . PHE A 230 ? 0.1774 0.1889 0.1341 0.0201 0.0076 0.0033 230 PHE A CZ 1767 N N . GLU A 231 ? 0.1386 0.1340 0.1406 -0.0068 0.0167 0.0187 231 GLU A N 1768 C CA . GLU A 231 ? 0.1435 0.1382 0.1634 -0.0069 0.0152 0.0120 231 GLU A CA 1769 C C . GLU A 231 ? 0.1543 0.1350 0.1574 -0.0083 0.0041 0.0037 231 GLU A C 1770 O O . GLU A 231 ? 0.1644 0.1360 0.1733 -0.0125 0.0112 0.0129 231 GLU A O 1771 C CB . GLU A 231 ? 0.1609 0.1311 0.1787 -0.0048 0.0174 0.0122 231 GLU A CB 1772 C CG . GLU A 231 ? 0.1487 0.1638 0.1679 -0.0126 0.0313 0.0329 231 GLU A CG 1773 C CD . GLU A 231 ? 0.1901 0.1497 0.1680 -0.0014 0.0046 0.0161 231 GLU A CD 1774 O OE1 . GLU A 231 ? 0.1809 0.1430 0.1807 -0.0164 0.0363 0.0265 231 GLU A OE1 1775 O OE2 . GLU A 231 ? 0.2108 0.2076 0.1926 0.0211 -0.0016 0.0252 231 GLU A OE2 1776 N N . GLY A 232 ? 0.1368 0.1160 0.1430 -0.0081 0.0109 0.0092 232 GLY A N 1777 C CA . GLY A 232 ? 0.1374 0.1314 0.1363 -0.0037 0.0107 0.0086 232 GLY A CA 1778 C C . GLY A 232 ? 0.1269 0.1133 0.1292 0.0040 0.0161 0.0079 232 GLY A C 1779 O O . GLY A 232 ? 0.1470 0.1278 0.1433 -0.0011 0.0176 0.0170 232 GLY A O 1780 N N . VAL A 233 ? 0.1147 0.1190 0.1298 0.0017 0.0006 0.0119 233 VAL A N 1781 C CA . VAL A 233 ? 0.1160 0.1192 0.1253 -0.0041 0.0027 0.0050 233 VAL A CA 1782 C C . VAL A 233 ? 0.1178 0.1166 0.1184 -0.0077 0.0022 -0.0025 233 VAL A C 1783 O O . VAL A 233 ? 0.1146 0.1226 0.1128 -0.0181 -0.0054 -0.0174 233 VAL A O 1784 C CB . VAL A 233 ? 0.1149 0.1222 0.1241 -0.0066 0.0063 0.0130 233 VAL A CB 1785 C CG1 . VAL A 233 ? 0.1200 0.1600 0.1680 0.0045 0.0012 0.0069 233 VAL A CG1 1786 C CG2 . VAL A 233 ? 0.1183 0.1274 0.1303 0.0036 0.0131 0.0121 233 VAL A CG2 1787 N N . CYS A 234 ? 0.1242 0.1135 0.1133 -0.0060 0.0048 0.0069 234 CYS A N 1788 C CA . CYS A 234 ? 0.1081 0.1071 0.1043 0.0019 -0.0002 0.0041 234 CYS A CA 1789 C C . CYS A 234 ? 0.1206 0.1178 0.1051 -0.0006 0.0002 0.0098 234 CYS A C 1790 O O . CYS A 234 ? 0.1284 0.1270 0.1233 -0.0026 0.0122 0.0193 234 CYS A O 1791 C CB . CYS A 234 ? 0.1176 0.1117 0.1194 0.0029 0.0150 0.0069 234 CYS A CB 1792 S SG . CYS A 234 ? 0.1176 0.1118 0.1227 0.0034 0.0078 0.0155 234 CYS A SG 1793 N N . ASP A 235 ? 0.1093 0.1128 0.1117 0.0051 0.0001 0.0088 235 ASP A N 1794 C CA . ASP A 235 ? 0.1134 0.1141 0.1058 0.0034 -0.0001 0.0080 235 ASP A CA 1795 C C . ASP A 235 ? 0.1135 0.1119 0.1083 -0.0022 0.0010 0.0075 235 ASP A C 1796 O O . ASP A 235 ? 0.1148 0.1088 0.1228 -0.0021 0.0009 0.0148 235 ASP A O 1797 C CB . ASP A 235 ? 0.1124 0.1157 0.1076 0.0073 -0.0062 -0.0005 235 ASP A CB 1798 C CG . ASP A 235 ? 0.1128 0.1223 0.1072 0.0040 0.0043 0.0015 235 ASP A CG 1799 O OD1 . ASP A 235 ? 0.1109 0.1194 0.1277 0.0064 0.0055 0.0134 235 ASP A OD1 1800 O OD2 . ASP A 235 ? 0.0942 0.1174 0.1398 0.0065 0.0013 0.0064 235 ASP A OD2 1801 N N . LYS A 236 ? 0.1277 0.1133 0.1136 -0.0071 0.0063 0.0051 236 LYS A N 1802 C CA . LYS A 236 ? 0.1294 0.1168 0.1177 -0.0025 -0.0007 0.0049 236 LYS A CA 1803 C C . LYS A 236 ? 0.1279 0.1179 0.1158 -0.0024 0.0009 0.0021 236 LYS A C 1804 O O . LYS A 236 ? 0.1391 0.1271 0.1156 -0.0013 -0.0050 -0.0032 236 LYS A O 1805 C CB . LYS A 236 ? 0.1307 0.1204 0.1223 -0.0034 -0.0009 0.0007 236 LYS A CB 1806 C CG . LYS A 236 ? 0.1272 0.1159 0.1064 0.0095 0.0088 0.0086 236 LYS A CG 1807 C CD . LYS A 236 ? 0.1290 0.1289 0.1074 0.0016 0.0098 0.0068 236 LYS A CD 1808 C CE . LYS A 236 ? 0.1345 0.1407 0.1111 0.0037 0.0243 0.0124 236 LYS A CE 1809 N NZ . LYS A 236 ? 0.1645 0.1309 0.1401 0.0220 0.0223 0.0205 236 LYS A NZ 1810 N N . ASN A 237 ? 0.1398 0.1265 0.1235 -0.0008 -0.0054 -0.0027 237 ASN A N 1811 C CA . ASN A 237 ? 0.1342 0.1348 0.1295 -0.0004 -0.0065 0.0041 237 ASN A CA 1812 C C . ASN A 237 ? 0.1260 0.1267 0.1335 -0.0030 -0.0035 0.0055 237 ASN A C 1813 O O . ASN A 237 ? 0.1411 0.1634 0.1346 -0.0075 -0.0198 0.0098 237 ASN A O 1814 C CB . ASN A 237 ? 0.1294 0.1226 0.1341 0.0083 -0.0055 0.0040 237 ASN A CB 1815 C CG . ASN A 237 ? 0.1813 0.1577 0.1739 0.0039 -0.0025 0.0175 237 ASN A CG 1816 O OD1 . ASN A 237 ? 0.2257 0.1875 0.1539 0.0150 0.0167 0.0196 237 ASN A OD1 1817 N ND2 . ASN A 237 ? 0.2200 0.1673 0.1771 -0.0058 -0.0242 0.0209 237 ASN A ND2 1818 N N . GLY A 238 ? 0.1144 0.1098 0.1223 -0.0007 -0.0031 0.0151 238 GLY A N 1819 C CA . GLY A 238 ? 0.1153 0.1082 0.1284 0.0114 0.0000 0.0087 238 GLY A CA 1820 C C . GLY A 238 ? 0.1162 0.1246 0.1300 0.0200 -0.0010 0.0157 238 GLY A C 1821 O O . GLY A 238 ? 0.1498 0.1576 0.1665 0.0296 0.0223 0.0246 238 GLY A O 1822 N N . CYS A 239 ? 0.1134 0.1075 0.1177 0.0111 -0.0053 0.0081 239 CYS A N 1823 C CA . CYS A 239 ? 0.1159 0.1192 0.1214 0.0049 -0.0041 0.0059 239 CYS A CA 1824 C C . CYS A 239 ? 0.1185 0.1218 0.1256 0.0004 -0.0096 0.0049 239 CYS A C 1825 O O . CYS A 239 ? 0.1415 0.1273 0.1260 -0.0041 -0.0122 0.0020 239 CYS A O 1826 C CB . CYS A 239 ? 0.1205 0.1009 0.1343 0.0070 0.0016 -0.0026 239 CYS A CB 1827 S SG . CYS A 239 ? 0.1288 0.1366 0.1531 0.0176 -0.0224 -0.0066 239 CYS A SG 1828 N N . GLY A 240 ? 0.1231 0.1242 0.1191 0.0017 -0.0001 0.0043 240 GLY A N 1829 C CA . GLY A 240 ? 0.1152 0.1178 0.1178 -0.0004 0.0003 0.0002 240 GLY A CA 1830 C C . GLY A 240 ? 0.1171 0.1143 0.1249 0.0062 -0.0030 0.0037 240 GLY A C 1831 O O . GLY A 240 ? 0.1314 0.1143 0.1405 0.0052 -0.0181 0.0096 240 GLY A O 1832 N N . TRP A 241 ? 0.1120 0.1151 0.1327 0.0059 -0.0042 0.0006 241 TRP A N 1833 C CA . TRP A 241 ? 0.1165 0.1180 0.1281 0.0026 -0.0026 -0.0030 241 TRP A CA 1834 C C . TRP A 241 ? 0.1158 0.1265 0.1303 0.0000 -0.0077 0.0003 241 TRP A C 1835 O O . TRP A 241 ? 0.1274 0.1268 0.1383 -0.0009 -0.0130 0.0035 241 TRP A O 1836 C CB . TRP A 241 ? 0.1241 0.1288 0.1373 0.0037 0.0043 -0.0027 241 TRP A CB 1837 C CG . TRP A 241 ? 0.1068 0.1210 0.1431 0.0141 -0.0054 0.0038 241 TRP A CG 1838 C CD1 . TRP A 241 ? 0.1112 0.1153 0.1437 0.0097 0.0080 -0.0041 241 TRP A CD1 1839 C CD2 . TRP A 241 ? 0.1059 0.1201 0.1388 0.0104 -0.0105 0.0030 241 TRP A CD2 1840 N NE1 . TRP A 241 ? 0.1061 0.1236 0.1497 0.0051 -0.0116 0.0009 241 TRP A NE1 1841 C CE2 . TRP A 241 ? 0.0954 0.1090 0.1202 0.0063 0.0016 0.0005 241 TRP A CE2 1842 C CE3 . TRP A 241 ? 0.1033 0.1314 0.1643 0.0089 -0.0009 -0.0128 241 TRP A CE3 1843 C CZ2 . TRP A 241 ? 0.1202 0.1284 0.1482 0.0030 0.0017 -0.0024 241 TRP A CZ2 1844 C CZ3 . TRP A 241 ? 0.1356 0.1090 0.1601 0.0074 0.0016 -0.0149 241 TRP A CZ3 1845 C CH2 . TRP A 241 ? 0.1329 0.1296 0.1617 0.0150 0.0053 -0.0062 241 TRP A CH2 1846 N N . ASN A 242 ? 0.1170 0.1171 0.1172 0.0080 -0.0111 -0.0006 242 ASN A N 1847 C CA . ASN A 242 ? 0.1170 0.1190 0.1304 0.0010 -0.0123 0.0001 242 ASN A CA 1848 C C . ASN A 242 ? 0.1256 0.1234 0.1426 0.0018 -0.0098 0.0000 242 ASN A C 1849 O O . ASN A 242 ? 0.1328 0.1257 0.1459 -0.0090 -0.0242 0.0004 242 ASN A O 1850 C CB . ASN A 242 ? 0.1155 0.1196 0.1420 0.0051 -0.0169 -0.0024 242 ASN A CB 1851 C CG . ASN A 242 ? 0.1207 0.1338 0.1257 0.0116 -0.0036 0.0029 242 ASN A CG 1852 O OD1 . ASN A 242 ? 0.1237 0.1304 0.1643 0.0059 -0.0256 0.0020 242 ASN A OD1 1853 N ND2 . ASN A 242 ? 0.1432 0.1238 0.1126 0.0128 -0.0155 -0.0041 242 ASN A ND2 1854 N N . ASN A 243 ? 0.1255 0.1108 0.1479 0.0087 -0.0130 -0.0041 243 ASN A N 1855 C CA . ASN A 243 ? 0.1299 0.1265 0.1468 0.0148 -0.0102 -0.0057 243 ASN A CA 1856 C C . ASN A 243 ? 0.1404 0.1278 0.1433 0.0143 -0.0129 -0.0070 243 ASN A C 1857 O O . ASN A 243 ? 0.1368 0.1315 0.1538 0.0182 -0.0305 0.0001 243 ASN A O 1858 C CB . ASN A 243 ? 0.1420 0.1272 0.1692 0.0058 -0.0157 -0.0140 243 ASN A CB 1859 C CG . ASN A 243 ? 0.1524 0.1346 0.1574 0.0110 -0.0109 -0.0071 243 ASN A CG 1860 O OD1 . ASN A 243 ? 0.1425 0.1499 0.1741 0.0048 -0.0219 -0.0035 243 ASN A OD1 1861 N ND2 . ASN A 243 ? 0.1343 0.1643 0.1724 0.0157 -0.0192 -0.0078 243 ASN A ND2 1862 N N . TYR A 244 ? 0.1397 0.1362 0.1586 0.0137 -0.0132 0.0000 244 TYR A N 1863 C CA . TYR A 244 ? 0.1514 0.1486 0.1519 0.0069 -0.0144 -0.0021 244 TYR A CA 1864 C C . TYR A 244 ? 0.1477 0.1371 0.1411 0.0074 -0.0151 0.0107 244 TYR A C 1865 O O . TYR A 244 ? 0.1695 0.1413 0.1537 0.0243 -0.0302 0.0146 244 TYR A O 1866 C CB . TYR A 244 ? 0.1609 0.1559 0.1589 0.0049 -0.0108 -0.0024 244 TYR A CB 1867 C CG . TYR A 244 ? 0.1872 0.1695 0.1799 -0.0043 -0.0052 -0.0068 244 TYR A CG 1868 C CD1 . TYR A 244 ? 0.2163 0.1503 0.1748 0.0151 -0.0174 -0.0095 244 TYR A CD1 1869 C CD2 . TYR A 244 ? 0.1858 0.1514 0.2101 0.0024 -0.0225 -0.0013 244 TYR A CD2 1870 C CE1 . TYR A 244 ? 0.1847 0.1689 0.2162 0.0007 -0.0272 0.0085 244 TYR A CE1 1871 C CE2 . TYR A 244 ? 0.1998 0.1619 0.2019 -0.0060 -0.0238 -0.0126 244 TYR A CE2 1872 C CZ . TYR A 244 ? 0.1873 0.1711 0.2086 -0.0071 -0.0155 -0.0026 244 TYR A CZ 1873 O OH . TYR A 244 ? 0.2054 0.1709 0.1986 -0.0090 -0.0275 -0.0192 244 TYR A OH 1874 N N . ARG A 245 ? 0.1601 0.1447 0.1473 0.0123 -0.0242 0.0131 245 ARG A N 1875 C CA . ARG A 245 ? 0.1557 0.1511 0.1516 0.0069 -0.0107 0.0027 245 ARG A CA 1876 C C . ARG A 245 ? 0.1581 0.1463 0.1669 0.0068 -0.0082 0.0011 245 ARG A C 1877 O O . ARG A 245 ? 0.1789 0.1388 0.1780 0.0016 -0.0152 0.0041 245 ARG A O 1878 C CB . ARG A 245 ? 0.1610 0.1507 0.1517 0.0177 -0.0108 0.0035 245 ARG A CB 1879 C CG . ARG A 245 ? 0.1535 0.1442 0.1462 0.0105 -0.0126 0.0010 245 ARG A CG 1880 C CD . ARG A 245 ? 0.1378 0.1391 0.1650 -0.0060 0.0017 0.0005 245 ARG A CD 1881 N NE . ARG A 245 ? 0.1496 0.1540 0.1546 0.0215 0.0040 0.0108 245 ARG A NE 1882 C CZ . ARG A 245 ? 0.1507 0.1380 0.1828 -0.0116 0.0192 0.0072 245 ARG A CZ 1883 N NH1 . ARG A 245 ? 0.1834 0.1531 0.2147 -0.0067 0.0262 0.0161 245 ARG A NH1 1884 N NH2 . ARG A 245 ? 0.1651 0.1684 0.1967 0.0103 0.0246 0.0079 245 ARG A NH2 1885 N N . VAL A 246 ? 0.1684 0.1445 0.1528 0.0014 -0.0079 0.0009 246 VAL A N 1886 C CA . VAL A 246 ? 0.1629 0.1551 0.1609 0.0069 -0.0061 -0.0032 246 VAL A CA 1887 C C . VAL A 246 ? 0.1712 0.1667 0.1574 0.0115 -0.0097 -0.0069 246 VAL A C 1888 O O . VAL A 246 ? 0.1720 0.1492 0.1523 0.0205 -0.0097 -0.0029 246 VAL A O 1889 C CB . VAL A 246 ? 0.1589 0.1614 0.1661 0.0050 -0.0049 -0.0010 246 VAL A CB 1890 C CG1 . VAL A 246 ? 0.1684 0.1821 0.1741 0.0096 -0.0143 -0.0053 246 VAL A CG1 1891 C CG2 . VAL A 246 ? 0.1338 0.1435 0.1557 0.0164 -0.0264 -0.0006 246 VAL A CG2 1892 N N . ASN A 247 ? 0.1792 0.1766 0.1686 0.0090 -0.0185 -0.0100 247 ASN A N 1893 C CA . ASN A 247 ? 0.1821 0.1748 0.1773 0.0117 -0.0190 -0.0024 247 ASN A CA 1894 C C . ASN A 247 ? 0.1764 0.1758 0.1849 0.0115 -0.0217 -0.0089 247 ASN A C 1895 O O . ASN A 247 ? 0.1679 0.1838 0.2066 0.0217 -0.0275 -0.0105 247 ASN A O 1896 C CB . ASN A 247 ? 0.1849 0.1765 0.1807 0.0082 -0.0157 0.0000 247 ASN A CB 1897 C CG . ASN A 247 ? 0.2006 0.1975 0.1835 0.0059 -0.0098 0.0075 247 ASN A CG 1898 O OD1 . ASN A 247 ? 0.2292 0.1929 0.2092 0.0041 -0.0148 -0.0015 247 ASN A OD1 1899 N ND2 . ASN A 247 ? 0.2169 0.2213 0.1910 0.0326 -0.0366 0.0032 247 ASN A ND2 1900 N N . VAL A 248 ? 0.1748 0.1686 0.1841 0.0158 -0.0152 -0.0054 248 VAL A N 1901 C CA . VAL A 248 ? 0.1791 0.1768 0.1959 0.0122 -0.0126 -0.0072 248 VAL A CA 1902 C C . VAL A 248 ? 0.1859 0.1831 0.2040 0.0191 -0.0158 -0.0152 248 VAL A C 1903 O O . VAL A 248 ? 0.2008 0.2012 0.2442 0.0270 -0.0319 -0.0215 248 VAL A O 1904 C CB . VAL A 248 ? 0.1810 0.1830 0.1974 0.0139 -0.0085 -0.0064 248 VAL A CB 1905 C CG1 . VAL A 248 ? 0.2026 0.1850 0.1949 0.0131 -0.0098 -0.0029 248 VAL A CG1 1906 C CG2 . VAL A 248 ? 0.1915 0.1833 0.1864 0.0117 -0.0084 -0.0017 248 VAL A CG2 1907 N N . THR A 249 ? 0.1810 0.1883 0.2014 0.0153 -0.0192 -0.0142 249 THR A N 1908 C CA . THR A 249 ? 0.1919 0.1907 0.1916 0.0075 -0.0092 -0.0022 249 THR A CA 1909 C C . THR A 249 ? 0.1795 0.1896 0.1795 0.0081 -0.0181 -0.0058 249 THR A C 1910 O O . THR A 249 ? 0.2134 0.1906 0.2021 0.0079 -0.0196 -0.0112 249 THR A O 1911 C CB . THR A 249 ? 0.2039 0.2132 0.2062 0.0043 -0.0069 -0.0032 249 THR A CB 1912 O OG1 . THR A 249 ? 0.2273 0.2637 0.2105 0.0102 -0.0300 0.0181 249 THR A OG1 1913 C CG2 . THR A 249 ? 0.2258 0.2368 0.2249 -0.0010 0.0003 -0.0014 249 THR A CG2 1914 N N . ASP A 250 ? 0.1711 0.1787 0.1837 0.0069 -0.0158 -0.0011 250 ASP A N 1915 C CA . ASP A 250 ? 0.1714 0.1812 0.1922 0.0064 -0.0106 -0.0040 250 ASP A CA 1916 C C . ASP A 250 ? 0.1557 0.1709 0.1848 0.0083 -0.0070 -0.0017 250 ASP A C 1917 O O . ASP A 250 ? 0.1482 0.1744 0.1912 0.0049 -0.0205 0.0093 250 ASP A O 1918 C CB . ASP A 250 ? 0.1790 0.1979 0.2022 0.0100 -0.0148 0.0020 250 ASP A CB 1919 C CG . ASP A 250 ? 0.2081 0.2139 0.2503 0.0098 -0.0069 -0.0120 250 ASP A CG 1920 O OD1 . ASP A 250 ? 0.1908 0.2299 0.2679 0.0264 -0.0008 -0.0245 250 ASP A OD1 1921 O OD2 . ASP A 250 ? 0.2475 0.2646 0.3502 0.0282 -0.0158 -0.0155 250 ASP A OD2 1922 N N . TYR A 251 ? 0.1443 0.1652 0.1705 0.0047 -0.0079 -0.0139 251 TYR A N 1923 C CA . TYR A 251 ? 0.1442 0.1560 0.1692 0.0076 -0.0052 -0.0061 251 TYR A CA 1924 C C . TYR A 251 ? 0.1382 0.1572 0.1605 0.0047 -0.0106 -0.0054 251 TYR A C 1925 O O . TYR A 251 ? 0.1385 0.1530 0.1681 0.0141 0.0036 0.0008 251 TYR A O 1926 C CB . TYR A 251 ? 0.1402 0.1471 0.1637 0.0093 -0.0060 -0.0080 251 TYR A CB 1927 C CG . TYR A 251 ? 0.1528 0.1495 0.1598 0.0054 -0.0054 -0.0091 251 TYR A CG 1928 C CD1 . TYR A 251 ? 0.1236 0.1464 0.1474 0.0080 -0.0146 -0.0017 251 TYR A CD1 1929 C CD2 . TYR A 251 ? 0.1628 0.1536 0.1410 0.0208 0.0036 -0.0366 251 TYR A CD2 1930 C CE1 . TYR A 251 ? 0.1376 0.1482 0.1557 0.0059 -0.0025 -0.0001 251 TYR A CE1 1931 C CE2 . TYR A 251 ? 0.1485 0.1424 0.1594 0.0224 -0.0026 -0.0025 251 TYR A CE2 1932 C CZ . TYR A 251 ? 0.1338 0.1320 0.1457 0.0133 -0.0135 -0.0102 251 TYR A CZ 1933 O OH . TYR A 251 ? 0.1582 0.1668 0.1608 0.0054 0.0115 -0.0030 251 TYR A OH 1934 N N . TYR A 252 ? 0.1399 0.1560 0.1558 0.0127 -0.0068 -0.0029 252 TYR A N 1935 C CA . TYR A 252 ? 0.1347 0.1486 0.1588 0.0090 -0.0144 -0.0045 252 TYR A CA 1936 C C . TYR A 252 ? 0.1271 0.1498 0.1628 0.0121 -0.0152 -0.0013 252 TYR A C 1937 O O . TYR A 252 ? 0.1295 0.1590 0.1621 0.0143 -0.0206 -0.0078 252 TYR A O 1938 C CB . TYR A 252 ? 0.1258 0.1436 0.1582 0.0125 -0.0112 -0.0003 252 TYR A CB 1939 C CG . TYR A 252 ? 0.1314 0.1327 0.1390 0.0035 -0.0122 -0.0164 252 TYR A CG 1940 C CD1 . TYR A 252 ? 0.1102 0.1578 0.1345 0.0041 -0.0201 -0.0104 252 TYR A CD1 1941 C CD2 . TYR A 252 ? 0.1324 0.1516 0.1415 0.0148 -0.0069 -0.0186 252 TYR A CD2 1942 C CE1 . TYR A 252 ? 0.1230 0.1400 0.1245 0.0100 0.0016 -0.0169 252 TYR A CE1 1943 C CE2 . TYR A 252 ? 0.1205 0.1306 0.1470 0.0037 -0.0162 -0.0034 252 TYR A CE2 1944 C CZ . TYR A 252 ? 0.1173 0.1260 0.1353 0.0105 -0.0222 -0.0118 252 TYR A CZ 1945 O OH . TYR A 252 ? 0.1104 0.1353 0.1571 0.0223 -0.0165 -0.0087 252 TYR A OH 1946 N N . GLY A 253 ? 0.1353 0.1555 0.1671 0.0077 -0.0161 -0.0033 253 GLY A N 1947 C CA . GLY A 253 ? 0.1338 0.1578 0.1702 0.0086 -0.0156 -0.0033 253 GLY A CA 1948 C C . GLY A 253 ? 0.1225 0.1551 0.1650 0.0050 -0.0175 -0.0027 253 GLY A C 1949 O O . GLY A 253 ? 0.1205 0.1596 0.1731 -0.0018 -0.0332 -0.0087 253 GLY A O 1950 N N . ARG A 254 ? 0.1351 0.1726 0.1704 0.0051 -0.0151 -0.0067 254 ARG A N 1951 C CA . ARG A 254 ? 0.1503 0.1732 0.1853 0.0027 -0.0161 -0.0040 254 ARG A CA 1952 C C . ARG A 254 ? 0.1608 0.1868 0.1922 -0.0014 -0.0204 -0.0027 254 ARG A C 1953 O O . ARG A 254 ? 0.1717 0.2169 0.2082 0.0053 -0.0292 -0.0050 254 ARG A O 1954 C CB . ARG A 254 ? 0.1490 0.1716 0.1858 0.0025 -0.0222 -0.0081 254 ARG A CB 1955 C CG . ARG A 254 ? 0.1313 0.1721 0.1798 -0.0005 -0.0317 -0.0043 254 ARG A CG 1956 C CD . ARG A 254 ? 0.1449 0.1623 0.1732 0.0034 -0.0280 0.0027 254 ARG A CD 1957 N NE . ARG A 254 ? 0.1629 0.1713 0.1897 -0.0109 -0.0421 -0.0131 254 ARG A NE 1958 C CZ . ARG A 254 ? 0.1652 0.1530 0.1683 0.0054 -0.0447 -0.0203 254 ARG A CZ 1959 N NH1 . ARG A 254 ? 0.1568 0.1794 0.1765 0.0071 -0.0607 -0.0162 254 ARG A NH1 1960 N NH2 . ARG A 254 ? 0.1789 0.1865 0.2257 -0.0182 -0.0362 -0.0146 254 ARG A NH2 1961 N N . GLY A 255 ? 0.1681 0.2204 0.2095 0.0005 -0.0215 -0.0035 255 GLY A N 1962 C CA . GLY A 255 ? 0.1815 0.2233 0.2228 0.0006 -0.0207 -0.0052 255 GLY A CA 1963 C C . GLY A 255 ? 0.1993 0.2404 0.2407 0.0007 -0.0107 -0.0121 255 GLY A C 1964 O O . GLY A 255 ? 0.1826 0.2161 0.2355 0.0106 -0.0063 -0.0332 255 GLY A O 1965 N N . GLU A 256 ? 0.2066 0.2538 0.2613 -0.0037 -0.0162 -0.0127 256 GLU A N 1966 C CA . GLU A 256 ? 0.2291 0.2690 0.2717 -0.0010 -0.0117 -0.0054 256 GLU A CA 1967 C C . GLU A 256 ? 0.2189 0.2707 0.2677 0.0018 -0.0171 -0.0087 256 GLU A C 1968 O O . GLU A 256 ? 0.2188 0.2860 0.2925 0.0136 -0.0182 -0.0102 256 GLU A O 1969 C CB . GLU A 256 ? 0.2338 0.2840 0.2862 -0.0012 -0.0102 -0.0081 256 GLU A CB 1970 C CG . GLU A 256 ? 0.2678 0.3066 0.3262 -0.0096 -0.0010 0.0016 256 GLU A CG 1971 C CD . GLU A 256 ? 0.2930 0.3318 0.3428 -0.0184 -0.0066 0.0010 256 GLU A CD 1972 O OE1 . GLU A 256 ? 0.3676 0.3970 0.4174 -0.0116 -0.0294 0.0234 256 GLU A OE1 1973 O OE2 . GLU A 256 ? 0.4174 0.4214 0.4292 -0.0300 0.0004 0.0339 256 GLU A OE2 1974 N N . GLU A 257 ? 0.2115 0.2585 0.2599 0.0064 -0.0258 -0.0044 257 GLU A N 1975 C CA . GLU A 257 ? 0.2222 0.2511 0.2564 0.0045 -0.0178 -0.0026 257 GLU A CA 1976 C C . GLU A 257 ? 0.2144 0.2349 0.2576 0.0071 -0.0242 0.0010 257 GLU A C 1977 O O . GLU A 257 ? 0.2228 0.2409 0.2693 0.0081 -0.0424 -0.0041 257 GLU A O 1978 C CB . GLU A 257 ? 0.2455 0.2595 0.2660 0.0055 -0.0175 -0.0007 257 GLU A CB 1979 C CG . GLU A 257 ? 0.2632 0.2826 0.2784 0.0107 -0.0149 0.0007 257 GLU A CG 1980 C CD . GLU A 257 ? 0.2793 0.3033 0.3030 0.0076 -0.0186 0.0012 257 GLU A CD 1981 O OE1 . GLU A 257 ? 0.2753 0.2971 0.3394 0.0295 -0.0392 0.0048 257 GLU A OE1 1982 O OE2 . GLU A 257 ? 0.3121 0.3641 0.3286 0.0223 -0.0138 -0.0169 257 GLU A OE2 1983 N N . PHE A 258 ? 0.1943 0.2064 0.2346 0.0093 -0.0200 0.0036 258 PHE A N 1984 C CA . PHE A 258 ? 0.1775 0.2019 0.2184 0.0124 -0.0097 -0.0001 258 PHE A CA 1985 C C . PHE A 258 ? 0.1604 0.2042 0.2230 0.0170 -0.0083 0.0003 258 PHE A C 1986 O O . PHE A 258 ? 0.1679 0.2258 0.2529 0.0074 -0.0178 0.0028 258 PHE A O 1987 C CB . PHE A 258 ? 0.1564 0.1867 0.1999 0.0143 -0.0102 0.0035 258 PHE A CB 1988 C CG . PHE A 258 ? 0.1507 0.1813 0.1892 0.0288 -0.0216 -0.0045 258 PHE A CG 1989 C CD1 . PHE A 258 ? 0.1458 0.1723 0.1754 0.0259 -0.0136 -0.0077 258 PHE A CD1 1990 C CD2 . PHE A 258 ? 0.1560 0.1674 0.1981 0.0186 -0.0222 -0.0057 258 PHE A CD2 1991 C CE1 . PHE A 258 ? 0.1612 0.1662 0.1813 0.0102 -0.0220 0.0005 258 PHE A CE1 1992 C CE2 . PHE A 258 ? 0.1595 0.1513 0.1971 0.0235 -0.0254 -0.0007 258 PHE A CE2 1993 C CZ . PHE A 258 ? 0.1445 0.1630 0.1799 0.0218 -0.0095 -0.0024 258 PHE A CZ 1994 N N . LYS A 259 ? 0.1566 0.1922 0.2244 0.0037 -0.0107 0.0000 259 LYS A N 1995 C CA . LYS A 259 ? 0.1827 0.2081 0.2244 0.0047 -0.0013 0.0011 259 LYS A CA 1996 C C . LYS A 259 ? 0.1699 0.2008 0.2009 0.0018 -0.0052 0.0118 259 LYS A C 1997 O O . LYS A 259 ? 0.1587 0.2225 0.2504 -0.0011 -0.0062 0.0209 259 LYS A O 1998 C CB . LYS A 259 ? 0.2005 0.2256 0.2255 0.0017 -0.0018 -0.0016 259 LYS A CB 1999 C CG . LYS A 259 ? 0.2611 0.2455 0.2644 0.0096 -0.0036 -0.0006 259 LYS A CG 2000 C CD . LYS A 259 ? 0.2554 0.2562 0.2849 0.0101 -0.0008 -0.0083 259 LYS A CD 2001 C CE . LYS A 259 ? 0.2684 0.2726 0.3099 0.0288 0.0032 -0.0069 259 LYS A CE 2002 N NZ . LYS A 259 ? 0.2537 0.2883 0.3274 0.0258 -0.0169 -0.0070 259 LYS A NZ 2003 N N . VAL A 260 ? 0.1596 0.1871 0.1910 -0.0023 -0.0102 0.0016 260 VAL A N 2004 C CA . VAL A 260 ? 0.1491 0.1792 0.1803 -0.0022 -0.0044 -0.0009 260 VAL A CA 2005 C C . VAL A 260 ? 0.1338 0.1632 0.1731 0.0052 -0.0071 -0.0010 260 VAL A C 2006 O O . VAL A 260 ? 0.1538 0.1733 0.1780 0.0079 -0.0142 -0.0084 260 VAL A O 2007 C CB . VAL A 260 ? 0.1453 0.1630 0.1741 0.0035 -0.0087 -0.0027 260 VAL A CB 2008 C CG1 . VAL A 260 ? 0.1657 0.1651 0.1933 0.0049 -0.0058 -0.0049 260 VAL A CG1 2009 C CG2 . VAL A 260 ? 0.1769 0.1776 0.1849 0.0050 -0.0101 -0.0064 260 VAL A CG2 2010 N N . ASN A 261 ? 0.1398 0.1747 0.1746 -0.0083 -0.0032 -0.0092 261 ASN A N 2011 C CA . ASN A 261 ? 0.1374 0.1797 0.1768 -0.0051 -0.0057 -0.0080 261 ASN A CA 2012 C C . ASN A 261 ? 0.1336 0.1628 0.1590 -0.0117 -0.0086 -0.0073 261 ASN A C 2013 O O . ASN A 261 ? 0.1266 0.1748 0.2048 0.0012 -0.0106 -0.0106 261 ASN A O 2014 C CB . ASN A 261 ? 0.1436 0.1726 0.1809 -0.0012 -0.0062 -0.0085 261 ASN A CB 2015 C CG . ASN A 261 ? 0.1442 0.1981 0.1834 -0.0207 -0.0028 -0.0111 261 ASN A CG 2016 O OD1 . ASN A 261 ? 0.1561 0.2063 0.1913 -0.0184 -0.0178 -0.0145 261 ASN A OD1 2017 N ND2 . ASN A 261 ? 0.1366 0.2463 0.2347 -0.0286 -0.0110 -0.0026 261 ASN A ND2 2018 N N . THR A 262 ? 0.1336 0.1575 0.1668 0.0011 -0.0050 -0.0117 262 THR A N 2019 C CA . THR A 262 ? 0.1314 0.1520 0.1611 0.0028 -0.0096 -0.0038 262 THR A CA 2020 C C . THR A 262 ? 0.1418 0.1612 0.1747 0.0090 -0.0140 -0.0110 262 THR A C 2021 O O . THR A 262 ? 0.1384 0.1588 0.1763 0.0146 -0.0207 -0.0236 262 THR A O 2022 C CB . THR A 262 ? 0.1201 0.1463 0.1517 -0.0050 -0.0100 -0.0012 262 THR A CB 2023 O OG1 . THR A 262 ? 0.1254 0.1587 0.1666 0.0013 -0.0063 -0.0137 262 THR A OG1 2024 C CG2 . THR A 262 ? 0.1285 0.1480 0.1568 0.0109 -0.0149 -0.0025 262 THR A CG2 2025 N N . LEU A 263 ? 0.1468 0.1695 0.1929 -0.0009 -0.0180 -0.0080 263 LEU A N 2026 C CA . LEU A 263 ? 0.1542 0.1691 0.1845 -0.0018 -0.0152 -0.0090 263 LEU A CA 2027 C C . LEU A 263 ? 0.1606 0.1791 0.1923 -0.0087 -0.0129 -0.0073 263 LEU A C 2028 O O . LEU A 263 ? 0.1739 0.1673 0.2174 -0.0181 -0.0105 -0.0090 263 LEU A O 2029 C CB . LEU A 263 ? 0.1584 0.1865 0.2009 -0.0072 -0.0200 -0.0144 263 LEU A CB 2030 C CG . LEU A 263 ? 0.1633 0.1957 0.1996 -0.0076 -0.0282 -0.0189 263 LEU A CG 2031 C CD1 . LEU A 263 ? 0.1662 0.2151 0.2125 -0.0064 -0.0323 -0.0031 263 LEU A CD1 2032 C CD2 . LEU A 263 ? 0.1861 0.2039 0.2038 -0.0126 -0.0115 -0.0151 263 LEU A CD2 2033 N N . LYS A 264 ? 0.1487 0.1687 0.1869 -0.0121 -0.0124 -0.0136 264 LYS A N 2034 C CA . LYS A 264 ? 0.1668 0.1859 0.1888 -0.0045 -0.0128 -0.0088 264 LYS A CA 2035 C C . LYS A 264 ? 0.1558 0.1644 0.1756 -0.0135 -0.0103 -0.0089 264 LYS A C 2036 O O . LYS A 264 ? 0.1293 0.1600 0.1956 -0.0096 -0.0048 0.0013 264 LYS A O 2037 C CB . LYS A 264 ? 0.1817 0.1952 0.2014 -0.0171 -0.0051 -0.0037 264 LYS A CB 2038 C CG . LYS A 264 ? 0.2093 0.2447 0.2414 -0.0129 -0.0165 -0.0044 264 LYS A CG 2039 C CD . LYS A 264 ? 0.2252 0.2773 0.2705 -0.0056 -0.0059 -0.0089 264 LYS A CD 2040 C CE . LYS A 264 ? 0.2853 0.3208 0.3212 0.0060 0.0040 -0.0067 264 LYS A CE 2041 N NZ . LYS A 264 ? 0.2938 0.3487 0.3483 0.0165 -0.0015 -0.0134 264 LYS A NZ 2042 N N . PRO A 265 ? 0.1589 0.1734 0.1755 -0.0145 -0.0093 -0.0094 265 PRO A N 2043 C CA . PRO A 265 ? 0.1459 0.1651 0.1754 -0.0072 -0.0132 -0.0045 265 PRO A CA 2044 C C . PRO A 265 ? 0.1328 0.1588 0.1812 -0.0036 -0.0034 -0.0029 265 PRO A C 2045 O O . PRO A 265 ? 0.1257 0.1686 0.2208 0.0008 -0.0121 -0.0162 265 PRO A O 2046 C CB . PRO A 265 ? 0.1573 0.1657 0.1767 -0.0127 -0.0089 -0.0034 265 PRO A CB 2047 C CG . PRO A 265 ? 0.2019 0.1791 0.2016 -0.0128 -0.0168 -0.0047 265 PRO A CG 2048 C CD . PRO A 265 ? 0.1626 0.1669 0.1797 -0.0111 -0.0043 -0.0123 265 PRO A CD 2049 N N . PHE A 266 ? 0.1231 0.1526 0.1772 -0.0026 -0.0082 -0.0121 266 PHE A N 2050 C CA . PHE A 266 ? 0.1252 0.1516 0.1555 -0.0060 -0.0017 -0.0077 266 PHE A CA 2051 C C . PHE A 266 ? 0.1102 0.1473 0.1574 0.0005 0.0001 -0.0091 266 PHE A C 2052 O O . PHE A 266 ? 0.1221 0.1540 0.1724 0.0221 -0.0058 -0.0181 266 PHE A O 2053 C CB . PHE A 266 ? 0.1133 0.1541 0.1462 0.0000 -0.0137 -0.0132 266 PHE A CB 2054 C CG . PHE A 266 ? 0.1160 0.1450 0.1419 0.0032 -0.0032 -0.0075 266 PHE A CG 2055 C CD1 . PHE A 266 ? 0.1304 0.1387 0.1431 -0.0078 -0.0094 -0.0068 266 PHE A CD1 2056 C CD2 . PHE A 266 ? 0.1405 0.1471 0.1559 0.0046 -0.0108 -0.0210 266 PHE A CD2 2057 C CE1 . PHE A 266 ? 0.1419 0.1328 0.1437 -0.0059 -0.0120 -0.0060 266 PHE A CE1 2058 C CE2 . PHE A 266 ? 0.1208 0.1553 0.1562 0.0062 -0.0172 -0.0203 266 PHE A CE2 2059 C CZ . PHE A 266 ? 0.1107 0.1723 0.1516 0.0014 -0.0095 -0.0079 266 PHE A CZ 2060 N N . THR A 267 ? 0.1174 0.1485 0.1484 0.0015 0.0008 -0.0044 267 THR A N 2061 C CA . THR A 267 ? 0.1248 0.1378 0.1549 -0.0073 -0.0045 0.0026 267 THR A CA 2062 C C . THR A 267 ? 0.1244 0.1304 0.1457 -0.0018 0.0018 0.0048 267 THR A C 2063 O O . THR A 267 ? 0.1181 0.1327 0.1563 0.0040 -0.0139 -0.0043 267 THR A O 2064 C CB . THR A 267 ? 0.1469 0.1469 0.1615 -0.0008 -0.0015 -0.0005 267 THR A CB 2065 O OG1 . THR A 267 ? 0.1472 0.1506 0.2105 -0.0139 -0.0022 0.0045 267 THR A OG1 2066 C CG2 . THR A 267 ? 0.1319 0.1764 0.1532 -0.0061 0.0172 -0.0027 267 THR A CG2 2067 N N . VAL A 268 ? 0.1027 0.1325 0.1374 -0.0054 -0.0005 0.0014 268 VAL A N 2068 C CA . VAL A 268 ? 0.1180 0.1231 0.1349 0.0008 -0.0017 -0.0034 268 VAL A CA 2069 C C . VAL A 268 ? 0.1078 0.1141 0.1310 -0.0049 -0.0010 -0.0089 268 VAL A C 2070 O O . VAL A 268 ? 0.1102 0.1322 0.1442 0.0035 -0.0032 -0.0074 268 VAL A O 2071 C CB . VAL A 268 ? 0.0973 0.1187 0.1380 -0.0060 -0.0048 -0.0033 268 VAL A CB 2072 C CG1 . VAL A 268 ? 0.1018 0.1370 0.1350 -0.0079 0.0055 0.0113 268 VAL A CG1 2073 C CG2 . VAL A 268 ? 0.0884 0.1175 0.1474 -0.0053 0.0113 0.0025 268 VAL A CG2 2074 N N . VAL A 269 ? 0.0943 0.1145 0.1306 0.0037 0.0012 -0.0157 269 VAL A N 2075 C CA . VAL A 269 ? 0.1128 0.1311 0.1331 0.0038 0.0034 -0.0062 269 VAL A CA 2076 C C . VAL A 269 ? 0.1124 0.1238 0.1218 0.0002 0.0037 -0.0079 269 VAL A C 2077 O O . VAL A 269 ? 0.1129 0.1427 0.1313 -0.0060 -0.0001 0.0016 269 VAL A O 2078 C CB . VAL A 269 ? 0.1152 0.1298 0.1424 0.0055 0.0064 -0.0085 269 VAL A CB 2079 C CG1 . VAL A 269 ? 0.1337 0.1429 0.1525 -0.0091 0.0038 -0.0089 269 VAL A CG1 2080 C CG2 . VAL A 269 ? 0.1116 0.1630 0.1446 -0.0015 0.0171 -0.0195 269 VAL A CG2 2081 N N . THR A 270 ? 0.1121 0.1223 0.1250 0.0013 -0.0023 0.0024 270 THR A N 2082 C CA . THR A 270 ? 0.1213 0.1221 0.1412 0.0018 0.0004 -0.0102 270 THR A CA 2083 C C . THR A 270 ? 0.1214 0.1219 0.1265 0.0024 0.0012 0.0013 270 THR A C 2084 O O . THR A 270 ? 0.1358 0.1205 0.1510 0.0025 -0.0160 -0.0031 270 THR A O 2085 C CB . THR A 270 ? 0.1193 0.1172 0.1240 -0.0002 -0.0033 -0.0046 270 THR A CB 2086 O OG1 . THR A 270 ? 0.1022 0.1230 0.1418 0.0005 0.0076 -0.0031 270 THR A OG1 2087 C CG2 . THR A 270 ? 0.1087 0.1159 0.1431 0.0000 0.0015 0.0044 270 THR A CG2 2088 N N . GLN A 271 ? 0.1217 0.1178 0.1392 0.0009 -0.0056 -0.0038 271 GLN A N 2089 C CA . GLN A 271 ? 0.1260 0.1331 0.1401 0.0006 0.0048 -0.0061 271 GLN A CA 2090 C C . GLN A 271 ? 0.1181 0.1238 0.1379 -0.0004 0.0027 0.0011 271 GLN A C 2091 O O . GLN A 271 ? 0.1039 0.1447 0.1494 0.0097 0.0057 -0.0023 271 GLN A O 2092 C CB . GLN A 271 ? 0.1295 0.1335 0.1513 0.0029 0.0049 -0.0040 271 GLN A CB 2093 C CG . GLN A 271 ? 0.1169 0.1399 0.1615 0.0061 0.0029 0.0005 271 GLN A CG 2094 C CD . GLN A 271 ? 0.1441 0.1362 0.1524 0.0032 0.0172 -0.0015 271 GLN A CD 2095 O OE1 . GLN A 271 ? 0.1438 0.1637 0.1863 0.0168 0.0132 0.0001 271 GLN A OE1 2096 N NE2 . GLN A 271 ? 0.1677 0.1670 0.1729 -0.0127 0.0302 0.0084 271 GLN A NE2 2097 N N . PHE A 272 ? 0.1208 0.1231 0.1293 -0.0084 0.0046 -0.0010 272 PHE A N 2098 C CA . PHE A 272 ? 0.1142 0.1278 0.1273 -0.0023 0.0049 -0.0070 272 PHE A CA 2099 C C . PHE A 272 ? 0.1064 0.1262 0.1226 -0.0054 0.0040 -0.0053 272 PHE A C 2100 O O . PHE A 272 ? 0.1173 0.1414 0.1280 0.0128 0.0094 -0.0157 272 PHE A O 2101 C CB . PHE A 272 ? 0.1083 0.1324 0.1264 -0.0028 0.0076 -0.0080 272 PHE A CB 2102 C CG . PHE A 272 ? 0.1131 0.1235 0.1277 0.0007 0.0023 -0.0055 272 PHE A CG 2103 C CD1 . PHE A 272 ? 0.1087 0.1293 0.1329 -0.0048 0.0069 -0.0103 272 PHE A CD1 2104 C CD2 . PHE A 272 ? 0.1379 0.1205 0.1508 0.0074 0.0070 -0.0118 272 PHE A CD2 2105 C CE1 . PHE A 272 ? 0.1210 0.1307 0.1302 -0.0012 0.0217 -0.0026 272 PHE A CE1 2106 C CE2 . PHE A 272 ? 0.1300 0.1340 0.1464 -0.0122 -0.0054 -0.0158 272 PHE A CE2 2107 C CZ . PHE A 272 ? 0.1466 0.1261 0.1497 0.0041 0.0108 -0.0168 272 PHE A CZ 2108 N N . LEU A 273 ? 0.1341 0.1498 0.1312 0.0054 -0.0006 -0.0081 273 LEU A N 2109 C CA . LEU A 273 ? 0.1354 0.1487 0.1413 -0.0057 0.0092 -0.0071 273 LEU A CA 2110 C C . LEU A 273 ? 0.1397 0.1485 0.1495 -0.0024 0.0110 -0.0117 273 LEU A C 2111 O O . LEU A 273 ? 0.1417 0.1526 0.1613 0.0121 0.0165 -0.0124 273 LEU A O 2112 C CB . LEU A 273 ? 0.1521 0.1556 0.1479 0.0003 0.0124 -0.0108 273 LEU A CB 2113 C CG . LEU A 273 ? 0.1778 0.1906 0.1776 0.0001 0.0044 -0.0142 273 LEU A CG 2114 C CD1 . LEU A 273 ? 0.1882 0.2211 0.2268 -0.0095 0.0004 0.0103 273 LEU A CD1 2115 C CD2 . LEU A 273 ? 0.1764 0.1960 0.1998 0.0021 0.0050 -0.0209 273 LEU A CD2 2116 N N . ALA A 274 ? 0.1397 0.1799 0.1619 -0.0037 0.0167 -0.0054 274 ALA A N 2117 C CA . ALA A 274 ? 0.1764 0.1920 0.1870 -0.0049 0.0101 -0.0188 274 ALA A CA 2118 C C . ALA A 274 ? 0.1895 0.2141 0.2104 0.0044 0.0127 -0.0278 274 ALA A C 2119 O O . ALA A 274 ? 0.1983 0.2331 0.2172 -0.0067 0.0185 -0.0520 274 ALA A O 2120 C CB . ALA A 274 ? 0.1832 0.2148 0.1995 -0.0072 0.0049 -0.0164 274 ALA A CB 2121 N N . ASN A 275 ? 0.2163 0.2246 0.2325 0.0057 0.0166 -0.0395 275 ASN A N 2122 C CA . ASN A 275 ? 0.2517 0.2547 0.2736 0.0058 0.0111 -0.0257 275 ASN A CA 2123 C C . ASN A 275 ? 0.2734 0.2929 0.2884 0.0024 0.0098 -0.0224 275 ASN A C 2124 O O . ASN A 275 ? 0.2474 0.2886 0.2492 -0.0004 0.0313 -0.0406 275 ASN A O 2125 C CB . ASN A 275 ? 0.2403 0.2438 0.2667 0.0151 0.0077 -0.0276 275 ASN A CB 2126 C CG . ASN A 275 ? 0.2488 0.2477 0.2768 -0.0024 0.0068 -0.0282 275 ASN A CG 2127 O OD1 . ASN A 275 ? 0.1895 0.2325 0.2462 0.0004 0.0049 -0.0647 275 ASN A OD1 2128 N ND2 . ASN A 275 ? 0.2512 0.2528 0.3184 0.0063 0.0075 -0.0194 275 ASN A ND2 2129 N N . ARG A 276 ? 0.3238 0.3348 0.3324 0.0043 0.0068 -0.0214 276 ARG A N 2130 C CA . ARG A 276 ? 0.3558 0.3686 0.3504 0.0012 0.0017 -0.0099 276 ARG A CA 2131 C C . ARG A 276 ? 0.3726 0.3908 0.3703 0.0056 0.0022 -0.0055 276 ARG A C 2132 O O . ARG A 276 ? 0.4004 0.4254 0.3863 0.0036 -0.0033 -0.0051 276 ARG A O 2133 C CB . ARG A 276 ? 0.3793 0.3882 0.3792 0.0049 0.0031 -0.0095 276 ARG A CB 2134 C CG . ARG A 276 ? 0.4139 0.4346 0.4372 0.0006 -0.0020 -0.0037 276 ARG A CG 2135 C CD . ARG A 276 ? 0.4868 0.4930 0.4789 0.0007 0.0041 0.0013 276 ARG A CD 2136 N NE . ARG A 276 ? 0.5228 0.5159 0.5171 0.0011 0.0006 -0.0043 276 ARG A NE 2137 C CZ . ARG A 276 ? 0.5462 0.5381 0.5287 0.0015 0.0004 -0.0037 276 ARG A CZ 2138 N NH1 . ARG A 276 ? 0.5517 0.5440 0.5460 0.0051 -0.0037 0.0003 276 ARG A NH1 2139 N NH2 . ARG A 276 ? 0.5467 0.5350 0.5280 0.0023 -0.0018 -0.0057 276 ARG A NH2 2140 N N . ARG A 277 ? 0.3712 0.3930 0.3735 -0.0013 -0.0044 -0.0096 277 ARG A N 2141 C CA . ARG A 277 ? 0.3698 0.3865 0.3680 0.0015 -0.0022 -0.0085 277 ARG A CA 2142 C C . ARG A 277 ? 0.3376 0.3631 0.3306 -0.0028 -0.0004 -0.0075 277 ARG A C 2143 O O . ARG A 277 ? 0.3394 0.3930 0.3193 -0.0072 -0.0120 -0.0099 277 ARG A O 2144 C CB . ARG A 277 ? 0.3869 0.3900 0.3876 -0.0005 0.0040 -0.0024 277 ARG A CB 2145 C CG . ARG A 277 ? 0.4299 0.4291 0.4256 0.0002 -0.0022 -0.0108 277 ARG A CG 2146 C CD . ARG A 277 ? 0.4809 0.4729 0.4903 -0.0014 0.0040 0.0020 277 ARG A CD 2147 N NE . ARG A 277 ? 0.5000 0.4981 0.4906 0.0015 -0.0059 -0.0085 277 ARG A NE 2148 C CZ . ARG A 277 ? 0.5285 0.5214 0.5130 -0.0029 -0.0009 0.0051 277 ARG A CZ 2149 N NH1 . ARG A 277 ? 0.5409 0.5324 0.5303 -0.0010 -0.0021 -0.0035 277 ARG A NH1 2150 N NH2 . ARG A 277 ? 0.5352 0.5280 0.5171 -0.0017 -0.0012 -0.0009 277 ARG A NH2 2151 N N . GLY A 278 ? 0.2818 0.3172 0.2662 -0.0090 0.0027 -0.0079 278 GLY A N 2152 C CA . GLY A 278 ? 0.2520 0.2770 0.2269 -0.0083 0.0036 -0.0005 278 GLY A CA 2153 C C . GLY A 278 ? 0.2236 0.2482 0.2029 -0.0103 0.0007 0.0002 278 GLY A C 2154 O O . GLY A 278 ? 0.2613 0.2590 0.2169 -0.0129 -0.0088 0.0107 278 GLY A O 2155 N N . LYS A 279 ? 0.1846 0.2063 0.1748 -0.0047 -0.0094 -0.0091 279 LYS A N 2156 C CA . LYS A 279 ? 0.1572 0.1774 0.1603 -0.0038 -0.0042 -0.0111 279 LYS A CA 2157 C C . LYS A 279 ? 0.1308 0.1604 0.1442 0.0036 -0.0020 -0.0130 279 LYS A C 2158 O O . LYS A 279 ? 0.1449 0.1736 0.1538 0.0037 0.0010 -0.0297 279 LYS A O 2159 C CB . LYS A 279 ? 0.1499 0.1662 0.1454 0.0008 -0.0094 -0.0108 279 LYS A CB 2160 C CG . LYS A 279 ? 0.1342 0.1653 0.1595 -0.0045 -0.0096 -0.0101 279 LYS A CG 2161 C CD . LYS A 279 ? 0.1520 0.1472 0.1423 0.0007 -0.0098 0.0023 279 LYS A CD 2162 C CE . LYS A 279 ? 0.1611 0.1473 0.1530 -0.0083 -0.0066 0.0032 279 LYS A CE 2163 N NZ . LYS A 279 ? 0.1418 0.1612 0.1387 -0.0127 -0.0190 -0.0093 279 LYS A NZ 2164 N N . LEU A 280 ? 0.1062 0.1356 0.1321 -0.0027 -0.0001 -0.0062 280 LEU A N 2165 C CA . LEU A 280 ? 0.1210 0.1434 0.1323 0.0042 0.0006 -0.0052 280 LEU A CA 2166 C C . LEU A 280 ? 0.1307 0.1380 0.1357 -0.0051 0.0016 -0.0046 280 LEU A C 2167 O O . LEU A 280 ? 0.1376 0.1217 0.1382 0.0006 -0.0018 0.0045 280 LEU A O 2168 C CB . LEU A 280 ? 0.1119 0.1364 0.1297 0.0090 -0.0003 -0.0040 280 LEU A CB 2169 C CG . LEU A 280 ? 0.1050 0.1231 0.1315 -0.0071 0.0025 -0.0066 280 LEU A CG 2170 C CD1 . LEU A 280 ? 0.0993 0.1010 0.1400 -0.0042 0.0149 -0.0101 280 LEU A CD1 2171 C CD2 . LEU A 280 ? 0.1200 0.1220 0.1084 0.0035 0.0062 -0.0053 280 LEU A CD2 2172 N N . GLU A 281 ? 0.1481 0.1498 0.1474 -0.0072 -0.0049 -0.0089 281 GLU A N 2173 C CA . GLU A 281 ? 0.1611 0.1637 0.1699 0.0030 -0.0039 -0.0057 281 GLU A CA 2174 C C . GLU A 281 ? 0.1431 0.1444 0.1569 0.0050 0.0062 -0.0048 281 GLU A C 2175 O O . GLU A 281 ? 0.1570 0.1314 0.1531 -0.0012 0.0070 -0.0105 281 GLU A O 2176 C CB . GLU A 281 ? 0.1893 0.1891 0.1853 0.0077 -0.0208 -0.0110 281 GLU A CB 2177 C CG . GLU A 281 ? 0.2263 0.2163 0.2240 0.0062 0.0016 -0.0075 281 GLU A CG 2178 C CD . GLU A 281 ? 0.2393 0.2385 0.2436 0.0163 0.0171 -0.0248 281 GLU A CD 2179 O OE1 . GLU A 281 ? 0.3208 0.3071 0.3285 0.0075 0.0530 -0.0513 281 GLU A OE1 2180 O OE2 . GLU A 281 ? 0.3400 0.3434 0.3716 -0.0038 0.0031 -0.0404 281 GLU A OE2 2181 N N . LYS A 282 ? 0.1527 0.1316 0.1533 -0.0014 -0.0008 -0.0087 282 LYS A N 2182 C CA . LYS A 282 ? 0.1611 0.1651 0.1636 -0.0014 -0.0037 -0.0061 282 LYS A CA 2183 C C . LYS A 282 ? 0.1338 0.1425 0.1412 0.0006 -0.0054 0.0010 282 LYS A C 2184 O O . LYS A 282 ? 0.1511 0.1354 0.1476 0.0012 -0.0113 -0.0048 282 LYS A O 2185 C CB . LYS A 282 ? 0.1663 0.1909 0.1837 -0.0041 -0.0180 0.0000 282 LYS A CB 2186 C CG . LYS A 282 ? 0.2309 0.2410 0.2210 0.0059 -0.0076 -0.0176 282 LYS A CG 2187 C CD . LYS A 282 ? 0.2345 0.2483 0.2520 0.0067 -0.0009 -0.0164 282 LYS A CD 2188 C CE . LYS A 282 ? 0.3152 0.2785 0.3186 0.0028 0.0028 -0.0241 282 LYS A CE 2189 N NZ . LYS A 282 ? 0.3776 0.3529 0.3628 -0.0093 -0.0002 0.0017 282 LYS A NZ 2190 N N . ILE A 283 ? 0.1253 0.1307 0.1364 0.0014 -0.0026 -0.0010 283 ILE A N 2191 C CA . ILE A 283 ? 0.1233 0.1275 0.1388 0.0010 -0.0018 0.0002 283 ILE A CA 2192 C C . ILE A 283 ? 0.1397 0.1341 0.1412 0.0025 -0.0095 0.0040 283 ILE A C 2193 O O . ILE A 283 ? 0.1259 0.1270 0.1389 -0.0023 0.0019 0.0120 283 ILE A O 2194 C CB . ILE A 283 ? 0.1274 0.1270 0.1301 -0.0027 -0.0054 -0.0038 283 ILE A CB 2195 C CG1 . ILE A 283 ? 0.1202 0.1390 0.1477 0.0171 0.0046 -0.0122 283 ILE A CG1 2196 C CG2 . ILE A 283 ? 0.1463 0.1401 0.1632 0.0074 -0.0084 -0.0042 283 ILE A CG2 2197 C CD1 . ILE A 283 ? 0.1255 0.1424 0.1585 0.0187 0.0036 -0.0082 283 ILE A CD1 2198 N N . HIS A 284 ? 0.1281 0.1415 0.1425 0.0051 -0.0048 0.0074 284 HIS A N 2199 C CA . HIS A 284 ? 0.1180 0.1285 0.1486 0.0023 -0.0048 -0.0053 284 HIS A CA 2200 C C . HIS A 284 ? 0.1204 0.1223 0.1430 0.0012 -0.0039 -0.0044 284 HIS A C 2201 O O . HIS A 284 ? 0.1281 0.1329 0.1553 0.0022 -0.0190 -0.0083 284 HIS A O 2202 C CB . HIS A 284 ? 0.1236 0.1333 0.1526 -0.0042 -0.0019 -0.0011 284 HIS A CB 2203 C CG . HIS A 284 ? 0.1401 0.1506 0.1632 0.0090 0.0050 -0.0025 284 HIS A CG 2204 N ND1 . HIS A 284 ? 0.1187 0.1534 0.1868 0.0025 0.0023 -0.0005 284 HIS A ND1 2205 C CD2 . HIS A 284 ? 0.1047 0.1463 0.1699 -0.0031 0.0278 -0.0148 284 HIS A CD2 2206 C CE1 . HIS A 284 ? 0.1213 0.1771 0.1998 0.0075 0.0000 -0.0054 284 HIS A CE1 2207 N NE2 . HIS A 284 ? 0.1127 0.1660 0.1921 0.0053 0.0290 -0.0228 284 HIS A NE2 2208 N N . ARG A 285 ? 0.1096 0.1185 0.1363 0.0060 -0.0033 -0.0091 285 ARG A N 2209 C CA . ARG A 285 ? 0.1143 0.1242 0.1336 0.0032 -0.0029 -0.0032 285 ARG A CA 2210 C C . ARG A 285 ? 0.1259 0.1293 0.1439 0.0059 -0.0002 -0.0017 285 ARG A C 2211 O O . ARG A 285 ? 0.1383 0.1273 0.1473 0.0023 -0.0006 -0.0148 285 ARG A O 2212 C CB . ARG A 285 ? 0.1198 0.1362 0.1309 0.0000 -0.0076 -0.0034 285 ARG A CB 2213 C CG . ARG A 285 ? 0.1174 0.1410 0.1393 0.0014 -0.0094 -0.0123 285 ARG A CG 2214 C CD . ARG A 285 ? 0.1139 0.1336 0.1601 0.0087 -0.0116 -0.0073 285 ARG A CD 2215 N NE . ARG A 285 ? 0.0953 0.1025 0.1245 0.0008 -0.0024 -0.0140 285 ARG A NE 2216 C CZ . ARG A 285 ? 0.1130 0.1361 0.1426 0.0099 0.0005 -0.0022 285 ARG A CZ 2217 N NH1 . ARG A 285 ? 0.0975 0.1296 0.1510 0.0263 0.0101 -0.0079 285 ARG A NH1 2218 N NH2 . ARG A 285 ? 0.1242 0.1402 0.1501 0.0251 0.0054 0.0073 285 ARG A NH2 2219 N N . PHE A 286 ? 0.1145 0.1333 0.1455 0.0072 -0.0015 -0.0077 286 PHE A N 2220 C CA . PHE A 286 ? 0.1128 0.1342 0.1545 0.0091 -0.0027 -0.0118 286 PHE A CA 2221 C C . PHE A 286 ? 0.1199 0.1363 0.1594 0.0033 -0.0029 -0.0080 286 PHE A C 2222 O O . PHE A 286 ? 0.1186 0.1445 0.1770 0.0085 0.0054 -0.0066 286 PHE A O 2223 C CB . PHE A 286 ? 0.1277 0.1483 0.1667 0.0106 -0.0033 -0.0130 286 PHE A CB 2224 C CG . PHE A 286 ? 0.1319 0.1502 0.1569 0.0182 0.0195 -0.0169 286 PHE A CG 2225 C CD1 . PHE A 286 ? 0.1382 0.1714 0.1835 0.0030 0.0244 -0.0012 286 PHE A CD1 2226 C CD2 . PHE A 286 ? 0.1655 0.1615 0.1702 0.0183 0.0205 -0.0062 286 PHE A CD2 2227 C CE1 . PHE A 286 ? 0.1725 0.1948 0.1889 0.0170 0.0016 -0.0146 286 PHE A CE1 2228 C CE2 . PHE A 286 ? 0.1541 0.1728 0.1903 0.0131 0.0186 0.0004 286 PHE A CE2 2229 C CZ . PHE A 286 ? 0.1838 0.1924 0.1811 0.0193 0.0144 -0.0028 286 PHE A CZ 2230 N N . TYR A 287 ? 0.1118 0.1262 0.1556 0.0065 -0.0090 -0.0123 287 TYR A N 2231 C CA . TYR A 287 ? 0.1159 0.1351 0.1600 0.0040 0.0039 -0.0085 287 TYR A CA 2232 C C . TYR A 287 ? 0.1157 0.1437 0.1571 -0.0010 0.0050 -0.0116 287 TYR A C 2233 O O . TYR A 287 ? 0.1288 0.1658 0.1934 -0.0018 0.0196 -0.0199 287 TYR A O 2234 C CB . TYR A 287 ? 0.1028 0.1268 0.1564 -0.0009 -0.0043 -0.0047 287 TYR A CB 2235 C CG . TYR A 287 ? 0.0955 0.1402 0.1468 0.0051 0.0003 -0.0100 287 TYR A CG 2236 C CD1 . TYR A 287 ? 0.0998 0.1538 0.1416 0.0144 -0.0023 0.0006 287 TYR A CD1 2237 C CD2 . TYR A 287 ? 0.1089 0.1132 0.1574 -0.0044 -0.0034 -0.0157 287 TYR A CD2 2238 C CE1 . TYR A 287 ? 0.1235 0.1038 0.1420 0.0084 0.0038 -0.0053 287 TYR A CE1 2239 C CE2 . TYR A 287 ? 0.1021 0.1327 0.1503 -0.0030 -0.0075 -0.0073 287 TYR A CE2 2240 C CZ . TYR A 287 ? 0.1017 0.1208 0.1261 0.0069 0.0002 -0.0122 287 TYR A CZ 2241 O OH . TYR A 287 ? 0.1118 0.1413 0.1377 0.0116 -0.0079 -0.0075 287 TYR A OH 2242 N N . VAL A 288 ? 0.1203 0.1517 0.1667 -0.0016 0.0114 -0.0155 288 VAL A N 2243 C CA . VAL A 288 ? 0.1208 0.1649 0.1856 0.0033 0.0095 -0.0117 288 VAL A CA 2244 C C . VAL A 288 ? 0.1388 0.1709 0.1922 0.0037 0.0081 -0.0163 288 VAL A C 2245 O O . VAL A 288 ? 0.1196 0.1639 0.2031 -0.0008 0.0138 -0.0257 288 VAL A O 2246 C CB . VAL A 288 ? 0.1308 0.1756 0.1877 0.0064 0.0207 -0.0129 288 VAL A CB 2247 C CG1 . VAL A 288 ? 0.1537 0.1877 0.1994 -0.0086 0.0000 0.0031 288 VAL A CG1 2248 C CG2 . VAL A 288 ? 0.1334 0.1814 0.1892 0.0056 0.0167 0.0003 288 VAL A CG2 2249 N N . GLN A 289 ? 0.1452 0.1736 0.1971 0.0021 0.0000 -0.0202 289 GLN A N 2250 C CA . GLN A 289 ? 0.1665 0.1913 0.2100 -0.0038 -0.0023 -0.0160 289 GLN A CA 2251 C C . GLN A 289 ? 0.1772 0.2057 0.2356 -0.0026 0.0010 -0.0147 289 GLN A C 2252 O O . GLN A 289 ? 0.1524 0.1983 0.2558 -0.0201 0.0058 -0.0284 289 GLN A O 2253 C CB . GLN A 289 ? 0.1514 0.1809 0.2027 -0.0060 -0.0051 -0.0198 289 GLN A CB 2254 C CG . GLN A 289 ? 0.1502 0.1951 0.1986 -0.0016 0.0033 -0.0180 289 GLN A CG 2255 C CD . GLN A 289 ? 0.1296 0.1716 0.1953 0.0034 -0.0153 -0.0127 289 GLN A CD 2256 O OE1 . GLN A 289 ? 0.1736 0.1742 0.2179 0.0074 -0.0018 -0.0194 289 GLN A OE1 2257 N NE2 . GLN A 289 ? 0.1255 0.1596 0.1933 0.0033 -0.0137 -0.0340 289 GLN A NE2 2258 N N . ASP A 290 ? 0.1859 0.2328 0.2646 -0.0136 0.0054 -0.0121 290 ASP A N 2259 C CA . ASP A 290 ? 0.2208 0.2501 0.2727 -0.0094 0.0058 -0.0047 290 ASP A CA 2260 C C . ASP A 290 ? 0.2317 0.2499 0.2760 -0.0082 0.0048 -0.0073 290 ASP A C 2261 O O . ASP A 290 ? 0.2390 0.2868 0.3172 -0.0060 0.0106 -0.0213 290 ASP A O 2262 C CB . ASP A 290 ? 0.2421 0.2711 0.2886 -0.0152 -0.0010 -0.0085 290 ASP A CB 2263 C CG . ASP A 290 ? 0.2869 0.3164 0.3216 -0.0074 -0.0003 -0.0034 290 ASP A CG 2264 O OD1 . ASP A 290 ? 0.4106 0.3521 0.3815 0.0015 0.0093 -0.0296 290 ASP A OD1 2265 O OD2 . ASP A 290 ? 0.3907 0.4157 0.3868 -0.0064 -0.0038 0.0151 290 ASP A OD2 2266 N N . GLY A 291 ? 0.2413 0.2580 0.2660 -0.0069 0.0123 -0.0042 291 GLY A N 2267 C CA . GLY A 291 ? 0.2507 0.2624 0.2690 -0.0055 0.0090 -0.0048 291 GLY A CA 2268 C C . GLY A 291 ? 0.2575 0.2653 0.2693 -0.0036 0.0111 -0.0058 291 GLY A C 2269 O O . GLY A 291 ? 0.3024 0.2970 0.2924 -0.0064 0.0190 -0.0121 291 GLY A O 2270 N N . LYS A 292 ? 0.2360 0.2557 0.2625 -0.0038 0.0137 -0.0061 292 LYS A N 2271 C CA . LYS A 292 ? 0.2406 0.2594 0.2696 -0.0074 0.0085 -0.0046 292 LYS A CA 2272 C C . LYS A 292 ? 0.2155 0.2352 0.2459 -0.0126 0.0146 -0.0126 292 LYS A C 2273 O O . LYS A 292 ? 0.2001 0.2086 0.2434 -0.0074 0.0122 -0.0255 292 LYS A O 2274 C CB . LYS A 292 ? 0.2641 0.2786 0.2872 -0.0069 0.0100 -0.0002 292 LYS A CB 2275 C CG . LYS A 292 ? 0.2806 0.3038 0.3188 -0.0038 0.0030 -0.0043 292 LYS A CG 2276 C CD . LYS A 292 ? 0.3032 0.3235 0.3218 -0.0045 -0.0022 -0.0001 292 LYS A CD 2277 C CE . LYS A 292 ? 0.3335 0.3646 0.3624 -0.0139 -0.0032 -0.0019 292 LYS A CE 2278 N NZ . LYS A 292 ? 0.3910 0.4211 0.3797 -0.0048 0.0137 0.0056 292 LYS A NZ 2279 N N . VAL A 293 ? 0.1951 0.2391 0.2412 -0.0060 0.0149 -0.0118 293 VAL A N 2280 C CA . VAL A 293 ? 0.1989 0.2260 0.2357 0.0004 0.0075 -0.0065 293 VAL A CA 2281 C C . VAL A 293 ? 0.1804 0.2122 0.2256 0.0012 0.0090 -0.0073 293 VAL A C 2282 O O . VAL A 293 ? 0.1812 0.2194 0.2568 0.0090 0.0079 -0.0016 293 VAL A O 2283 C CB . VAL A 293 ? 0.2035 0.2383 0.2366 0.0010 0.0049 -0.0068 293 VAL A CB 2284 C CG1 . VAL A 293 ? 0.2331 0.2307 0.2443 0.0041 -0.0025 -0.0091 293 VAL A CG1 2285 C CG2 . VAL A 293 ? 0.2175 0.2358 0.2455 0.0048 0.0082 -0.0078 293 VAL A CG2 2286 N N . ILE A 294 ? 0.1619 0.1936 0.2174 0.0053 0.0112 -0.0144 294 ILE A N 2287 C CA . ILE A 294 ? 0.1583 0.1959 0.2057 0.0041 -0.0006 -0.0143 294 ILE A CA 2288 C C . ILE A 294 ? 0.1535 0.1818 0.2092 0.0021 0.0042 -0.0153 294 ILE A C 2289 O O . ILE A 294 ? 0.1294 0.1892 0.2193 0.0072 0.0032 -0.0256 294 ILE A O 2290 C CB . ILE A 294 ? 0.1608 0.1968 0.2192 -0.0041 0.0048 -0.0119 294 ILE A CB 2291 C CG1 . ILE A 294 ? 0.1797 0.2028 0.2110 -0.0066 -0.0152 -0.0163 294 ILE A CG1 2292 C CG2 . ILE A 294 ? 0.1550 0.2004 0.1959 0.0033 0.0006 -0.0168 294 ILE A CG2 2293 C CD1 . ILE A 294 ? 0.1975 0.2058 0.2198 0.0002 -0.0033 -0.0113 294 ILE A CD1 2294 N N . GLU A 295 ? 0.1438 0.1765 0.1893 0.0011 0.0037 -0.0177 295 GLU A N 2295 C CA . GLU A 295 ? 0.1637 0.1708 0.1868 0.0062 -0.0013 -0.0120 295 GLU A CA 2296 C C . GLU A 295 ? 0.1470 0.1568 0.1747 0.0140 -0.0052 -0.0166 295 GLU A C 2297 O O . GLU A 295 ? 0.1432 0.1762 0.1829 0.0184 -0.0026 -0.0200 295 GLU A O 2298 C CB . GLU A 295 ? 0.1774 0.1770 0.1916 0.0043 0.0003 -0.0087 295 GLU A CB 2299 C CG . GLU A 295 ? 0.1962 0.2281 0.2346 0.0051 0.0142 -0.0128 295 GLU A CG 2300 C CD . GLU A 295 ? 0.2491 0.2769 0.2624 0.0013 0.0109 0.0082 295 GLU A CD 2301 O OE1 . GLU A 295 ? 0.2439 0.2967 0.2852 -0.0163 0.0303 0.0090 295 GLU A OE1 2302 O OE2 . GLU A 295 ? 0.2886 0.3188 0.2973 -0.0113 0.0261 0.0155 295 GLU A OE2 2303 N N . SER A 296 ? 0.1311 0.1496 0.1688 0.0061 -0.0011 -0.0102 296 SER A N 2304 C CA . SER A 296 ? 0.1472 0.1554 0.1643 0.0063 -0.0035 -0.0114 296 SER A CA 2305 C C . SER A 296 ? 0.1450 0.1494 0.1599 0.0023 -0.0037 -0.0130 296 SER A C 2306 O O . SER A 296 ? 0.1506 0.1599 0.1704 0.0208 -0.0059 -0.0091 296 SER A O 2307 C CB . SER A 296 ? 0.1513 0.1626 0.1798 0.0077 -0.0001 -0.0205 296 SER A CB 2308 O OG . SER A 296 ? 0.1517 0.1288 0.1893 0.0123 -0.0007 -0.0139 296 SER A OG 2309 N N . PHE A 297 ? 0.1505 0.1362 0.1681 0.0088 -0.0075 0.0008 297 PHE A N 2310 C CA . PHE A 297 ? 0.1453 0.1377 0.1634 0.0052 -0.0133 -0.0028 297 PHE A CA 2311 C C . PHE A 297 ? 0.1445 0.1515 0.1621 0.0056 -0.0166 -0.0048 297 PHE A C 2312 O O . PHE A 297 ? 0.1446 0.1440 0.1682 0.0146 -0.0201 -0.0010 297 PHE A O 2313 C CB . PHE A 297 ? 0.1426 0.1542 0.1712 0.0077 -0.0111 0.0016 297 PHE A CB 2314 C CG . PHE A 297 ? 0.1457 0.1563 0.1442 0.0098 0.0035 -0.0067 297 PHE A CG 2315 C CD1 . PHE A 297 ? 0.1606 0.1503 0.1539 0.0175 -0.0051 -0.0115 297 PHE A CD1 2316 C CD2 . PHE A 297 ? 0.1526 0.1464 0.1478 0.0142 0.0019 -0.0130 297 PHE A CD2 2317 C CE1 . PHE A 297 ? 0.1384 0.1612 0.1424 -0.0088 0.0076 -0.0098 297 PHE A CE1 2318 C CE2 . PHE A 297 ? 0.1501 0.1580 0.1725 0.0242 0.0014 -0.0143 297 PHE A CE2 2319 C CZ . PHE A 297 ? 0.1522 0.1783 0.1633 0.0213 0.0011 0.0063 297 PHE A CZ 2320 N N . TYR A 298 ? 0.1458 0.1487 0.1718 0.0090 -0.0170 -0.0023 298 TYR A N 2321 C CA . TYR A 298 ? 0.1534 0.1455 0.1794 0.0148 -0.0086 -0.0059 298 TYR A CA 2322 C C . TYR A 298 ? 0.1472 0.1420 0.1766 0.0209 -0.0076 -0.0098 298 TYR A C 2323 O O . TYR A 298 ? 0.1735 0.1551 0.1708 0.0204 -0.0142 -0.0073 298 TYR A O 2324 C CB . TYR A 298 ? 0.1522 0.1388 0.1888 0.0248 -0.0094 -0.0016 298 TYR A CB 2325 C CG . TYR A 298 ? 0.1657 0.1402 0.2027 0.0327 -0.0098 -0.0150 298 TYR A CG 2326 C CD1 . TYR A 298 ? 0.1796 0.1598 0.2052 0.0407 0.0050 0.0096 298 TYR A CD1 2327 C CD2 . TYR A 298 ? 0.1898 0.1614 0.2029 0.0420 -0.0224 0.0058 298 TYR A CD2 2328 C CE1 . TYR A 298 ? 0.1931 0.1662 0.2086 0.0352 -0.0047 0.0055 298 TYR A CE1 2329 C CE2 . TYR A 298 ? 0.2120 0.1599 0.1975 0.0547 -0.0099 -0.0147 298 TYR A CE2 2330 C CZ . TYR A 298 ? 0.1901 0.1678 0.1856 0.0612 0.0039 -0.0055 298 TYR A CZ 2331 O OH . TYR A 298 ? 0.2373 0.2163 0.2070 0.0478 0.0128 -0.0113 298 TYR A OH 2332 N N . THR A 299 ? 0.1570 0.1399 0.1717 0.0148 -0.0090 -0.0115 299 THR A N 2333 C CA . THR A 299 ? 0.1564 0.1530 0.1664 0.0189 -0.0102 -0.0065 299 THR A CA 2334 C C . THR A 299 ? 0.1674 0.1717 0.1746 0.0227 -0.0040 -0.0047 299 THR A C 2335 O O . THR A 299 ? 0.1851 0.1710 0.2021 0.0270 -0.0108 -0.0082 299 THR A O 2336 C CB . THR A 299 ? 0.1565 0.1508 0.1540 0.0212 -0.0142 -0.0056 299 THR A CB 2337 O OG1 . THR A 299 ? 0.1523 0.1426 0.1549 0.0236 -0.0146 -0.0146 299 THR A OG1 2338 C CG2 . THR A 299 ? 0.1374 0.1391 0.1796 0.0137 -0.0017 -0.0002 299 THR A CG2 2339 N N . ASN A 300 ? 0.1712 0.1707 0.1834 0.0231 -0.0190 0.0019 300 ASN A N 2340 C CA . ASN A 300 ? 0.1811 0.1749 0.1763 0.0203 -0.0142 -0.0015 300 ASN A CA 2341 C C . ASN A 300 ? 0.1882 0.1741 0.1888 0.0124 -0.0083 -0.0003 300 ASN A C 2342 O O . ASN A 300 ? 0.2121 0.1839 0.1843 0.0116 -0.0241 0.0115 300 ASN A O 2343 C CB . ASN A 300 ? 0.1949 0.1716 0.1922 0.0211 -0.0130 0.0004 300 ASN A CB 2344 C CG . ASN A 300 ? 0.1956 0.2006 0.1973 0.0226 -0.0187 -0.0102 300 ASN A CG 2345 O OD1 . ASN A 300 ? 0.2278 0.2351 0.2314 0.0470 -0.0248 -0.0393 300 ASN A OD1 2346 N ND2 . ASN A 300 ? 0.2278 0.2315 0.2147 0.0303 -0.0335 -0.0126 300 ASN A ND2 2347 N N . LYS A 301 ? 0.2039 0.1879 0.1906 0.0093 -0.0151 0.0022 301 LYS A N 2348 C CA . LYS A 301 ? 0.2164 0.1939 0.1942 0.0043 -0.0063 -0.0037 301 LYS A CA 2349 C C . LYS A 301 ? 0.2332 0.1885 0.1965 0.0035 -0.0103 0.0041 301 LYS A C 2350 O O . LYS A 301 ? 0.2462 0.1599 0.1853 0.0096 -0.0186 0.0010 301 LYS A O 2351 C CB . LYS A 301 ? 0.2254 0.2080 0.2042 0.0034 -0.0078 -0.0008 301 LYS A CB 2352 C CG . LYS A 301 ? 0.2096 0.1975 0.2172 0.0005 -0.0033 -0.0036 301 LYS A CG 2353 C CD . LYS A 301 ? 0.2271 0.2250 0.2243 0.0101 0.0036 -0.0069 301 LYS A CD 2354 C CE . LYS A 301 ? 0.2487 0.2409 0.2378 0.0092 0.0032 0.0010 301 LYS A CE 2355 N NZ . LYS A 301 ? 0.2892 0.2236 0.2417 0.0071 -0.0018 0.0045 301 LYS A NZ 2356 N N . GLU A 302 ? 0.2484 0.1897 0.2066 0.0064 -0.0148 0.0035 302 GLU A N 2357 C CA . GLU A 302 ? 0.2476 0.2111 0.2177 -0.0005 -0.0017 0.0016 302 GLU A CA 2358 C C . GLU A 302 ? 0.2459 0.2001 0.2115 0.0039 0.0023 0.0079 302 GLU A C 2359 O O . GLU A 302 ? 0.2655 0.2191 0.2103 0.0105 0.0205 0.0127 302 GLU A O 2360 C CB . GLU A 302 ? 0.2592 0.2274 0.2280 0.0035 -0.0054 0.0010 302 GLU A CB 2361 C CG . GLU A 302 ? 0.2827 0.2350 0.2393 0.0165 -0.0046 0.0072 302 GLU A CG 2362 C CD . GLU A 302 ? 0.3016 0.2655 0.2559 0.0105 -0.0065 0.0060 302 GLU A CD 2363 O OE1 . GLU A 302 ? 0.3941 0.2937 0.3011 0.0029 -0.0077 0.0421 302 GLU A OE1 2364 O OE2 . GLU A 302 ? 0.3735 0.3145 0.3124 0.0442 -0.0383 0.0032 302 GLU A OE2 2365 N N . GLY A 303 ? 0.2386 0.1980 0.2166 0.0022 0.0007 0.0103 303 GLY A N 2366 C CA . GLY A 303 ? 0.2230 0.1981 0.2150 0.0022 0.0017 0.0071 303 GLY A CA 2367 C C . GLY A 303 ? 0.2175 0.2002 0.2196 0.0017 -0.0030 0.0086 303 GLY A C 2368 O O . GLY A 303 ? 0.2097 0.1961 0.2401 -0.0062 0.0002 0.0158 303 GLY A O 2369 N N . VAL A 304 ? 0.1915 0.1871 0.1938 0.0041 -0.0061 0.0046 304 VAL A N 2370 C CA . VAL A 304 ? 0.1933 0.1899 0.2061 0.0030 -0.0048 0.0028 304 VAL A CA 2371 C C . VAL A 304 ? 0.1898 0.1782 0.1948 0.0048 -0.0063 0.0044 304 VAL A C 2372 O O . VAL A 304 ? 0.1663 0.1565 0.1991 0.0054 -0.0084 -0.0070 304 VAL A O 2373 C CB . VAL A 304 ? 0.1969 0.1859 0.2075 0.0043 0.0033 0.0092 304 VAL A CB 2374 C CG1 . VAL A 304 ? 0.1867 0.1975 0.2025 0.0115 -0.0114 0.0095 304 VAL A CG1 2375 C CG2 . VAL A 304 ? 0.2189 0.1982 0.2244 0.0006 0.0047 -0.0107 304 VAL A CG2 2376 N N . PRO A 305 ? 0.1722 0.1981 0.2004 0.0020 -0.0075 -0.0012 305 PRO A N 2377 C CA . PRO A 305 ? 0.1842 0.1961 0.1940 0.0009 -0.0094 -0.0036 305 PRO A CA 2378 C C . PRO A 305 ? 0.1779 0.1950 0.1891 0.0014 -0.0064 -0.0044 305 PRO A C 2379 O O . PRO A 305 ? 0.1786 0.1987 0.1999 0.0108 -0.0135 -0.0004 305 PRO A O 2380 C CB . PRO A 305 ? 0.1969 0.2173 0.1962 0.0027 -0.0067 0.0000 305 PRO A CB 2381 C CG . PRO A 305 ? 0.1991 0.2236 0.2145 -0.0009 -0.0085 -0.0075 305 PRO A CG 2382 C CD . PRO A 305 ? 0.1836 0.2012 0.2060 0.0043 -0.0143 0.0049 305 PRO A CD 2383 N N . TYR A 306 ? 0.1816 0.1723 0.1899 0.0036 0.0013 -0.0071 306 TYR A N 2384 C CA . TYR A 306 ? 0.1736 0.1656 0.1832 0.0133 0.0025 -0.0090 306 TYR A CA 2385 C C . TYR A 306 ? 0.1813 0.1542 0.1775 0.0094 -0.0031 -0.0126 306 TYR A C 2386 O O . TYR A 306 ? 0.2022 0.1675 0.1887 0.0138 -0.0082 -0.0161 306 TYR A O 2387 C CB . TYR A 306 ? 0.1791 0.1535 0.1914 0.0216 0.0044 -0.0044 306 TYR A CB 2388 C CG . TYR A 306 ? 0.1750 0.1523 0.1852 0.0304 0.0101 0.0024 306 TYR A CG 2389 C CD1 . TYR A 306 ? 0.1763 0.1524 0.2093 0.0314 0.0047 0.0003 306 TYR A CD1 2390 C CD2 . TYR A 306 ? 0.1718 0.1367 0.1915 0.0304 0.0181 -0.0143 306 TYR A CD2 2391 C CE1 . TYR A 306 ? 0.1694 0.1552 0.1943 0.0305 -0.0026 -0.0047 306 TYR A CE1 2392 C CE2 . TYR A 306 ? 0.1636 0.1528 0.1745 0.0261 0.0385 -0.0122 306 TYR A CE2 2393 C CZ . TYR A 306 ? 0.1645 0.1603 0.1974 0.0241 0.0099 -0.0047 306 TYR A CZ 2394 O OH . TYR A 306 ? 0.1579 0.1739 0.2441 0.0452 0.0086 -0.0138 306 TYR A OH 2395 N N . THR A 307 ? 0.1580 0.1435 0.1609 0.0096 -0.0006 -0.0087 307 THR A N 2396 C CA . THR A 307 ? 0.1577 0.1511 0.1747 0.0122 -0.0056 -0.0088 307 THR A CA 2397 C C . THR A 307 ? 0.1364 0.1411 0.1605 0.0090 0.0000 -0.0093 307 THR A C 2398 O O . THR A 307 ? 0.1548 0.1423 0.1692 0.0188 -0.0090 -0.0030 307 THR A O 2399 C CB . THR A 307 ? 0.1614 0.1398 0.1805 -0.0117 -0.0071 -0.0147 307 THR A CB 2400 O OG1 . THR A 307 ? 0.1769 0.1784 0.1816 -0.0161 -0.0284 -0.0116 307 THR A OG1 2401 C CG2 . THR A 307 ? 0.1632 0.1787 0.1813 -0.0024 -0.0163 -0.0005 307 THR A CG2 2402 N N . ASN A 308 ? 0.1433 0.1442 0.1642 0.0102 -0.0056 -0.0093 308 ASN A N 2403 C CA . ASN A 308 ? 0.1393 0.1470 0.1630 0.0113 -0.0046 -0.0007 308 ASN A CA 2404 C C . ASN A 308 ? 0.1432 0.1562 0.1873 0.0102 -0.0052 0.0007 308 ASN A C 2405 O O . ASN A 308 ? 0.1256 0.1369 0.2032 0.0176 -0.0001 0.0059 308 ASN A O 2406 C CB . ASN A 308 ? 0.1452 0.1621 0.1672 0.0130 -0.0040 0.0042 308 ASN A CB 2407 C CG . ASN A 308 ? 0.1543 0.1603 0.1725 0.0171 -0.0013 0.0000 308 ASN A CG 2408 O OD1 . ASN A 308 ? 0.1499 0.1734 0.1827 0.0171 -0.0055 -0.0086 308 ASN A OD1 2409 N ND2 . ASN A 308 ? 0.1524 0.1408 0.1859 0.0211 -0.0087 0.0138 308 ASN A ND2 2410 N N . MET A 309 ? 0.1382 0.1416 0.1669 0.0065 0.0044 0.0058 309 MET A N 2411 C CA . MET A 309 ? 0.1372 0.1531 0.1656 0.0078 0.0007 0.0031 309 MET A CA 2412 C C . MET A 309 ? 0.1300 0.1288 0.1601 0.0065 0.0012 0.0054 309 MET A C 2413 O O . MET A 309 ? 0.1161 0.1367 0.1749 0.0165 -0.0127 0.0070 309 MET A O 2414 C CB . MET A 309 ? 0.1534 0.1626 0.1751 0.0101 0.0011 0.0021 309 MET A CB 2415 C CG . MET A 309 ? 0.1506 0.1819 0.2127 0.0147 -0.0012 -0.0133 309 MET A CG 2416 S SD . MET A 309 ? 0.1736 0.2248 0.2029 0.0141 0.0124 -0.0102 309 MET A SD 2417 C CE . MET A 309 ? 0.1817 0.1958 0.2073 0.0151 0.0180 -0.0039 309 MET A CE 2418 N N . ILE A 310 ? 0.1257 0.1287 0.1475 0.0082 -0.0043 -0.0018 310 ILE A N 2419 C CA . ILE A 310 ? 0.1389 0.1315 0.1453 0.0050 -0.0060 -0.0035 310 ILE A CA 2420 C C . ILE A 310 ? 0.1517 0.1321 0.1446 -0.0019 -0.0034 -0.0073 310 ILE A C 2421 O O . ILE A 310 ? 0.1577 0.1375 0.1572 -0.0102 -0.0059 -0.0086 310 ILE A O 2422 C CB . ILE A 310 ? 0.1198 0.1376 0.1433 0.0105 -0.0035 -0.0082 310 ILE A CB 2423 C CG1 . ILE A 310 ? 0.1400 0.1287 0.1552 0.0166 -0.0084 -0.0120 310 ILE A CG1 2424 C CG2 . ILE A 310 ? 0.1367 0.1632 0.1849 0.0106 0.0074 -0.0138 310 ILE A CG2 2425 C CD1 . ILE A 310 ? 0.1743 0.1427 0.1350 0.0155 -0.0216 -0.0068 310 ILE A CD1 2426 N N . ASP A 311 ? 0.1427 0.1458 0.1340 -0.0021 -0.0049 -0.0067 311 ASP A N 2427 C CA . ASP A 311 ? 0.1431 0.1290 0.1364 -0.0019 -0.0011 -0.0035 311 ASP A CA 2428 C C . ASP A 311 ? 0.1291 0.1194 0.1300 -0.0057 -0.0017 -0.0085 311 ASP A C 2429 O O . ASP A 311 ? 0.1453 0.1072 0.1259 -0.0029 -0.0161 -0.0095 311 ASP A O 2430 C CB . ASP A 311 ? 0.1314 0.1165 0.1447 -0.0063 0.0042 -0.0093 311 ASP A CB 2431 C CG . ASP A 311 ? 0.1357 0.1466 0.1512 0.0023 0.0095 -0.0072 311 ASP A CG 2432 O OD1 . ASP A 311 ? 0.1417 0.1445 0.1660 0.0205 0.0045 -0.0092 311 ASP A OD1 2433 O OD2 . ASP A 311 ? 0.1662 0.1709 0.1991 0.0130 0.0255 -0.0212 311 ASP A OD2 2434 N N . ASP A 312 ? 0.1247 0.1172 0.1287 -0.0003 -0.0060 -0.0058 312 ASP A N 2435 C CA . ASP A 312 ? 0.1327 0.1269 0.1396 0.0034 -0.0035 0.0028 312 ASP A CA 2436 C C . ASP A 312 ? 0.1371 0.1314 0.1327 -0.0050 -0.0051 -0.0028 312 ASP A C 2437 O O . ASP A 312 ? 0.1483 0.1320 0.1524 -0.0019 -0.0139 0.0001 312 ASP A O 2438 C CB . ASP A 312 ? 0.1156 0.1066 0.1273 -0.0012 0.0036 0.0041 312 ASP A CB 2439 C CG . ASP A 312 ? 0.1590 0.1166 0.1486 0.0017 -0.0095 0.0026 312 ASP A CG 2440 O OD1 . ASP A 312 ? 0.1599 0.1359 0.1442 0.0075 -0.0121 -0.0039 312 ASP A OD1 2441 O OD2 . ASP A 312 ? 0.1575 0.1441 0.1639 0.0051 -0.0207 -0.0018 312 ASP A OD2 2442 N N . GLU A 313 ? 0.1521 0.1451 0.1415 0.0076 -0.0088 0.0030 313 GLU A N 2443 C CA . GLU A 313 ? 0.1654 0.1502 0.1582 0.0002 -0.0095 0.0046 313 GLU A CA 2444 C C . GLU A 313 ? 0.1501 0.1445 0.1509 0.0038 -0.0097 0.0058 313 GLU A C 2445 O O . GLU A 313 ? 0.1658 0.1488 0.1701 0.0073 -0.0024 0.0001 313 GLU A O 2446 C CB . GLU A 313 ? 0.1738 0.1632 0.1693 0.0050 -0.0120 0.0089 313 GLU A CB 2447 C CG . GLU A 313 ? 0.2050 0.1882 0.2035 0.0200 -0.0046 0.0164 313 GLU A CG 2448 C CD . GLU A 313 ? 0.2352 0.2194 0.2563 0.0175 0.0080 0.0110 313 GLU A CD 2449 O OE1 . GLU A 313 ? 0.3245 0.2939 0.3415 0.0233 0.0324 0.0260 313 GLU A OE1 2450 O OE2 . GLU A 313 ? 0.3436 0.2527 0.3820 0.0298 0.0135 0.0106 313 GLU A OE2 2451 N N . PHE A 314 ? 0.1428 0.1374 0.1408 -0.0012 -0.0120 0.0003 314 PHE A N 2452 C CA . PHE A 314 ? 0.1412 0.1381 0.1332 0.0072 -0.0116 0.0003 314 PHE A CA 2453 C C . PHE A 314 ? 0.1429 0.1324 0.1214 0.0029 -0.0122 -0.0038 314 PHE A C 2454 O O . PHE A 314 ? 0.1298 0.1143 0.1383 0.0086 0.0050 0.0033 314 PHE A O 2455 C CB . PHE A 314 ? 0.1438 0.1429 0.1335 0.0058 -0.0127 -0.0014 314 PHE A CB 2456 C CG . PHE A 314 ? 0.1340 0.1328 0.1265 -0.0005 -0.0132 0.0003 314 PHE A CG 2457 C CD1 . PHE A 314 ? 0.1171 0.1594 0.1515 0.0185 -0.0151 -0.0012 314 PHE A CD1 2458 C CD2 . PHE A 314 ? 0.1246 0.1417 0.1480 0.0027 -0.0238 -0.0050 314 PHE A CD2 2459 C CE1 . PHE A 314 ? 0.1233 0.1459 0.1464 0.0059 -0.0103 0.0042 314 PHE A CE1 2460 C CE2 . PHE A 314 ? 0.1499 0.1417 0.1445 0.0002 -0.0088 -0.0041 314 PHE A CE2 2461 C CZ . PHE A 314 ? 0.1442 0.1313 0.1569 -0.0129 -0.0158 -0.0179 314 PHE A CZ 2462 N N . CYS A 315 ? 0.1378 0.1246 0.1287 0.0065 -0.0113 -0.0020 315 CYS A N 2463 C CA . CYS A 315 ? 0.1421 0.1413 0.1379 0.0057 -0.0053 -0.0017 315 CYS A CA 2464 C C . CYS A 315 ? 0.1531 0.1593 0.1444 0.0087 -0.0014 0.0035 315 CYS A C 2465 O O . CYS A 315 ? 0.1612 0.1757 0.1432 0.0131 0.0030 0.0139 315 CYS A O 2466 C CB . CYS A 315 ? 0.1445 0.1479 0.1365 0.0100 -0.0021 -0.0005 315 CYS A CB 2467 S SG . CYS A 315 ? 0.1461 0.1313 0.1435 0.0167 -0.0068 -0.0007 315 CYS A SG 2468 N N . GLU A 316 ? 0.1715 0.1624 0.1664 0.0024 0.0000 0.0051 316 GLU A N 2469 C CA . GLU A 316 ? 0.1777 0.1720 0.1752 -0.0058 0.0011 0.0037 316 GLU A CA 2470 C C . GLU A 316 ? 0.1767 0.1646 0.1771 -0.0014 0.0005 0.0022 316 GLU A C 2471 O O . GLU A 316 ? 0.1889 0.1637 0.1793 -0.0066 -0.0024 0.0048 316 GLU A O 2472 C CB . GLU A 316 ? 0.1974 0.1787 0.1988 -0.0165 0.0011 0.0005 316 GLU A CB 2473 C CG . GLU A 316 ? 0.2618 0.2169 0.2439 -0.0198 0.0084 0.0120 316 GLU A CG 2474 C CD . GLU A 316 ? 0.3225 0.3495 0.3321 -0.0091 -0.0042 0.0018 316 GLU A CD 2475 O OE1 . GLU A 316 ? 0.4119 0.4132 0.3602 -0.0180 0.0128 0.0016 316 GLU A OE1 2476 O OE2 . GLU A 316 ? 0.4038 0.4062 0.4238 0.0189 0.0323 0.0002 316 GLU A OE2 2477 N N . ALA A 317 ? 0.1781 0.1592 0.1703 0.0007 -0.0030 0.0063 317 ALA A N 2478 C CA . ALA A 317 ? 0.1871 0.1720 0.1758 0.0059 -0.0009 0.0115 317 ALA A CA 2479 C C . ALA A 317 ? 0.1885 0.1776 0.1763 0.0055 -0.0022 0.0162 317 ALA A C 2480 O O . ALA A 317 ? 0.2262 0.1934 0.1774 0.0319 0.0042 0.0240 317 ALA A O 2481 C CB . ALA A 317 ? 0.1987 0.1789 0.1772 0.0170 -0.0087 0.0071 317 ALA A CB 2482 N N . THR A 318 ? 0.1861 0.1728 0.1786 0.0144 -0.0060 0.0152 318 THR A N 2483 C CA . THR A 318 ? 0.1751 0.1719 0.1650 0.0072 -0.0060 0.0136 318 THR A CA 2484 C C . THR A 318 ? 0.1761 0.1733 0.1717 0.0064 -0.0100 0.0119 318 THR A C 2485 O O . THR A 318 ? 0.1803 0.2106 0.2124 0.0020 0.0051 -0.0107 318 THR A O 2486 C CB . THR A 318 ? 0.1802 0.1800 0.1632 0.0125 -0.0062 0.0109 318 THR A CB 2487 O OG1 . THR A 318 ? 0.1891 0.1773 0.1702 0.0023 -0.0246 0.0308 318 THR A OG1 2488 C CG2 . THR A 318 ? 0.1745 0.2017 0.1754 0.0057 -0.0136 0.0135 318 THR A CG2 2489 N N . GLY A 319 ? 0.1669 0.1657 0.1588 0.0082 -0.0126 0.0120 319 GLY A N 2490 C CA . GLY A 319 ? 0.1571 0.1605 0.1497 0.0080 -0.0120 0.0153 319 GLY A CA 2491 C C . GLY A 319 ? 0.1501 0.1574 0.1573 0.0111 -0.0046 0.0070 319 GLY A C 2492 O O . GLY A 319 ? 0.1511 0.1850 0.1646 0.0034 -0.0009 0.0131 319 GLY A O 2493 N N . SER A 320 ? 0.1480 0.1450 0.1488 0.0118 -0.0057 0.0050 320 SER A N 2494 C CA . SER A 320 ? 0.1450 0.1286 0.1493 0.0060 -0.0042 0.0052 320 SER A CA 2495 C C . SER A 320 ? 0.1379 0.1321 0.1409 0.0067 0.0009 0.0109 320 SER A C 2496 O O . SER A 320 ? 0.1397 0.1397 0.1483 0.0029 0.0056 0.0127 320 SER A O 2497 C CB . SER A 320 ? 0.1496 0.1376 0.1523 0.0025 -0.0060 0.0125 320 SER A CB 2498 O OG . SER A 320 ? 0.1884 0.1746 0.1930 -0.0120 -0.0114 0.0271 320 SER A OG 2499 N N . ARG A 321 ? 0.1396 0.1323 0.1367 -0.0020 0.0023 0.0099 321 ARG A N 2500 C CA . ARG A 321 ? 0.1358 0.1221 0.1389 0.0049 -0.0012 0.0071 321 ARG A CA 2501 C C . ARG A 321 ? 0.1311 0.1264 0.1181 0.0081 -0.0049 0.0030 321 ARG A C 2502 O O . ARG A 321 ? 0.1435 0.1230 0.1292 0.0077 -0.0065 0.0030 321 ARG A O 2503 C CB . ARG A 321 ? 0.1368 0.1404 0.1391 -0.0007 -0.0076 0.0124 321 ARG A CB 2504 C CG . ARG A 321 ? 0.1481 0.1444 0.1770 -0.0064 0.0008 0.0059 321 ARG A CG 2505 C CD . ARG A 321 ? 0.1694 0.1466 0.1803 0.0014 0.0066 0.0114 321 ARG A CD 2506 N NE . ARG A 321 ? 0.1700 0.1467 0.1800 0.0133 0.0136 0.0248 321 ARG A NE 2507 C CZ . ARG A 321 ? 0.1731 0.1574 0.1793 0.0061 0.0069 0.0098 321 ARG A CZ 2508 N NH1 . ARG A 321 ? 0.1865 0.1481 0.1708 -0.0118 0.0145 0.0176 321 ARG A NH1 2509 N NH2 . ARG A 321 ? 0.2020 0.1689 0.1856 0.0173 0.0035 0.0103 321 ARG A NH2 2510 N N . LYS A 322 ? 0.1266 0.1206 0.1163 0.0000 -0.0043 0.0036 322 LYS A N 2511 C CA . LYS A 322 ? 0.1221 0.1169 0.1180 0.0003 0.0013 0.0067 322 LYS A CA 2512 C C . LYS A 322 ? 0.1259 0.1153 0.1156 -0.0075 0.0006 -0.0037 322 LYS A C 2513 O O . LYS A 322 ? 0.1210 0.1134 0.1103 0.0010 0.0019 -0.0021 322 LYS A O 2514 C CB . LYS A 322 ? 0.1272 0.1128 0.1134 -0.0032 0.0044 0.0065 322 LYS A CB 2515 C CG . LYS A 322 ? 0.1137 0.1259 0.1238 0.0060 0.0131 0.0142 322 LYS A CG 2516 C CD . LYS A 322 ? 0.1273 0.1463 0.1270 0.0001 0.0170 0.0056 322 LYS A CD 2517 C CE . LYS A 322 ? 0.1519 0.1420 0.1221 -0.0030 0.0166 0.0000 322 LYS A CE 2518 N NZ . LYS A 322 ? 0.1335 0.1527 0.1642 -0.0142 0.0139 0.0106 322 LYS A NZ 2519 N N . TYR A 323 ? 0.1147 0.1145 0.1079 0.0072 0.0006 0.0086 323 TYR A N 2520 C CA . TYR A 323 ? 0.1106 0.1213 0.1138 -0.0007 0.0020 0.0041 323 TYR A CA 2521 C C . TYR A 323 ? 0.1090 0.1151 0.1146 0.0006 0.0013 0.0038 323 TYR A C 2522 O O . TYR A 323 ? 0.1087 0.1149 0.1262 0.0069 0.0003 0.0134 323 TYR A O 2523 C CB . TYR A 323 ? 0.1081 0.1215 0.1117 0.0016 -0.0007 0.0111 323 TYR A CB 2524 C CG . TYR A 323 ? 0.1152 0.1179 0.0984 0.0066 0.0074 0.0021 323 TYR A CG 2525 C CD1 . TYR A 323 ? 0.1223 0.1072 0.1214 0.0125 0.0009 -0.0068 323 TYR A CD1 2526 C CD2 . TYR A 323 ? 0.1083 0.1025 0.1222 -0.0028 -0.0083 0.0079 323 TYR A CD2 2527 C CE1 . TYR A 323 ? 0.1212 0.1078 0.1356 -0.0076 -0.0041 0.0012 323 TYR A CE1 2528 C CE2 . TYR A 323 ? 0.1204 0.1123 0.1143 0.0026 0.0020 0.0022 323 TYR A CE2 2529 C CZ . TYR A 323 ? 0.1220 0.1129 0.1094 -0.0095 -0.0034 0.0039 323 TYR A CZ 2530 O OH . TYR A 323 ? 0.1397 0.1350 0.1046 -0.0079 0.0059 -0.0049 323 TYR A OH 2531 N N . MET A 324 ? 0.1316 0.1204 0.1175 0.0046 -0.0111 0.0030 324 MET A N 2532 C CA . MET A 324 ? 0.1310 0.1336 0.1279 0.0045 -0.0029 -0.0009 324 MET A CA 2533 C C . MET A 324 ? 0.1282 0.1449 0.1287 -0.0036 -0.0038 0.0061 324 MET A C 2534 O O . MET A 324 ? 0.1318 0.1820 0.1415 -0.0056 -0.0037 -0.0064 324 MET A O 2535 C CB . MET A 324 ? 0.1335 0.1140 0.1335 -0.0020 0.0006 0.0018 324 MET A CB 2536 C CG . MET A 324 ? 0.1381 0.1325 0.1369 0.0175 -0.0037 -0.0019 324 MET A CG 2537 S SD . MET A 324 ? 0.1406 0.1459 0.1766 0.0122 0.0104 -0.0120 324 MET A SD 2538 C CE . MET A 324 ? 0.1850 0.1216 0.1822 0.0097 0.0064 -0.0005 324 MET A CE 2539 N N . GLU A 325 ? 0.1299 0.1423 0.1265 -0.0032 -0.0069 0.0040 325 GLU A N 2540 C CA . GLU A 325 ? 0.1406 0.1314 0.1434 -0.0029 -0.0021 -0.0018 325 GLU A CA 2541 C C . GLU A 325 ? 0.1342 0.1421 0.1329 -0.0055 0.0010 0.0017 325 GLU A C 2542 O O . GLU A 325 ? 0.1570 0.1276 0.1703 -0.0225 -0.0183 0.0079 325 GLU A O 2543 C CB . GLU A 325 ? 0.1406 0.1384 0.1558 -0.0034 0.0005 0.0019 325 GLU A CB 2544 C CG . GLU A 325 ? 0.1665 0.1378 0.1490 -0.0055 0.0046 -0.0067 325 GLU A CG 2545 C CD . GLU A 325 ? 0.1600 0.1584 0.1853 -0.0028 0.0149 0.0211 325 GLU A CD 2546 O OE1 . GLU A 325 ? 0.2382 0.1651 0.2277 0.0101 0.0568 0.0116 325 GLU A OE1 2547 O OE2 . GLU A 325 ? 0.2181 0.2204 0.1993 -0.0158 -0.0083 0.0405 325 GLU A OE2 2548 N N . LEU A 326 ? 0.1266 0.1263 0.1267 0.0008 0.0013 0.0004 326 LEU A N 2549 C CA . LEU A 326 ? 0.1282 0.1278 0.1291 -0.0019 0.0055 0.0048 326 LEU A CA 2550 C C . LEU A 326 ? 0.1264 0.1348 0.1214 0.0011 0.0097 0.0064 326 LEU A C 2551 O O . LEU A 326 ? 0.1434 0.1473 0.1376 0.0149 0.0140 0.0267 326 LEU A O 2552 C CB . LEU A 326 ? 0.1210 0.1109 0.1259 -0.0042 0.0065 0.0062 326 LEU A CB 2553 C CG . LEU A 326 ? 0.1203 0.1047 0.1260 0.0000 0.0036 0.0102 326 LEU A CG 2554 C CD1 . LEU A 326 ? 0.1300 0.1243 0.1359 -0.0088 0.0042 0.0098 326 LEU A CD1 2555 C CD2 . LEU A 326 ? 0.1319 0.1381 0.1409 -0.0093 0.0171 0.0075 326 LEU A CD2 2556 N N . GLY A 327 ? 0.1224 0.1390 0.1259 -0.0078 0.0022 0.0090 327 GLY A N 2557 C CA . GLY A 327 ? 0.1254 0.1415 0.1225 0.0005 0.0032 0.0086 327 GLY A CA 2558 C C . GLY A 327 ? 0.1286 0.1360 0.1230 -0.0048 0.0040 0.0060 327 GLY A C 2559 O O . GLY A 327 ? 0.1299 0.1283 0.1207 -0.0131 0.0037 -0.0004 327 GLY A O 2560 N N . ALA A 328 ? 0.1141 0.1128 0.1087 0.0013 -0.0001 0.0005 328 ALA A N 2561 C CA . ALA A 328 ? 0.1171 0.1200 0.1127 0.0000 0.0012 -0.0004 328 ALA A CA 2562 C C . ALA A 328 ? 0.1172 0.1216 0.1158 0.0022 0.0033 -0.0016 328 ALA A C 2563 O O . ALA A 328 ? 0.1121 0.1241 0.1219 0.0009 -0.0051 -0.0053 328 ALA A O 2564 C CB . ALA A 328 ? 0.1039 0.1186 0.1247 -0.0044 0.0080 0.0114 328 ALA A CB 2565 N N . THR A 329 ? 0.1061 0.1119 0.1115 0.0085 -0.0049 0.0061 329 THR A N 2566 C CA . THR A 329 ? 0.1099 0.1051 0.1060 0.0001 -0.0015 -0.0051 329 THR A CA 2567 C C . THR A 329 ? 0.1094 0.1130 0.1121 -0.0036 -0.0043 -0.0077 329 THR A C 2568 O O . THR A 329 ? 0.1040 0.1105 0.1180 -0.0124 -0.0009 0.0113 329 THR A O 2569 C CB . THR A 329 ? 0.1073 0.1212 0.1096 -0.0043 -0.0018 -0.0093 329 THR A CB 2570 O OG1 . THR A 329 ? 0.1171 0.1136 0.1166 -0.0009 0.0003 0.0034 329 THR A OG1 2571 C CG2 . THR A 329 ? 0.1175 0.1115 0.1271 0.0054 -0.0070 -0.0061 329 THR A CG2 2572 N N . GLN A 330 ? 0.1041 0.1045 0.1039 -0.0072 0.0023 -0.0057 330 GLN A N 2573 C CA . GLN A 330 ? 0.1081 0.1124 0.1118 -0.0076 -0.0010 -0.0004 330 GLN A CA 2574 C C . GLN A 330 ? 0.1030 0.1086 0.1019 -0.0104 -0.0039 -0.0057 330 GLN A C 2575 O O . GLN A 330 ? 0.1161 0.1201 0.1080 -0.0106 -0.0120 -0.0005 330 GLN A O 2576 C CB . GLN A 330 ? 0.1208 0.1160 0.1158 -0.0021 0.0024 -0.0049 330 GLN A CB 2577 C CG . GLN A 330 ? 0.1246 0.1091 0.1029 -0.0193 0.0053 0.0131 330 GLN A CG 2578 C CD . GLN A 330 ? 0.1268 0.1115 0.1172 -0.0082 -0.0078 0.0009 330 GLN A CD 2579 O OE1 . GLN A 330 ? 0.1469 0.1557 0.1589 0.0010 -0.0079 -0.0048 330 GLN A OE1 2580 N NE2 . GLN A 330 ? 0.1369 0.1231 0.1327 -0.0035 -0.0199 0.0093 330 GLN A NE2 2581 N N . GLY A 331 ? 0.1100 0.1127 0.1140 -0.0089 0.0008 0.0025 331 GLY A N 2582 C CA . GLY A 331 ? 0.1037 0.1143 0.0934 -0.0023 0.0004 -0.0011 331 GLY A CA 2583 C C . GLY A 331 ? 0.1140 0.1154 0.1000 -0.0010 -0.0004 0.0020 331 GLY A C 2584 O O . GLY A 331 ? 0.1076 0.1269 0.1091 -0.0038 -0.0098 0.0096 331 GLY A O 2585 N N . MET A 332 ? 0.1043 0.1097 0.1092 0.0081 0.0066 0.0031 332 MET A N 2586 C CA . MET A 332 ? 0.1117 0.1176 0.1028 0.0001 -0.0012 0.0006 332 MET A CA 2587 C C . MET A 332 ? 0.1005 0.1073 0.1054 -0.0018 0.0001 -0.0008 332 MET A C 2588 O O . MET A 332 ? 0.1033 0.1180 0.1208 0.0088 -0.0037 -0.0022 332 MET A O 2589 C CB . MET A 332 ? 0.0991 0.1233 0.1151 0.0093 0.0045 0.0033 332 MET A CB 2590 C CG . MET A 332 ? 0.1066 0.1172 0.1177 0.0156 0.0004 -0.0022 332 MET A CG 2591 S SD . MET A 332 ? 0.1391 0.1332 0.1340 0.0218 -0.0123 -0.0054 332 MET A SD 2592 C CE . MET A 332 ? 0.1620 0.1209 0.1381 0.0159 -0.0133 -0.0062 332 MET A CE 2593 N N . GLY A 333 ? 0.1138 0.1028 0.1080 0.0024 -0.0035 0.0021 333 GLY A N 2594 C CA . GLY A 333 ? 0.1059 0.0991 0.1130 -0.0029 -0.0020 -0.0033 333 GLY A CA 2595 C C . GLY A 333 ? 0.1055 0.1060 0.1092 -0.0025 0.0000 -0.0011 333 GLY A C 2596 O O . GLY A 333 ? 0.1000 0.1019 0.1058 -0.0099 0.0027 0.0010 333 GLY A O 2597 N N . GLU A 334 ? 0.1154 0.0936 0.1112 -0.0107 -0.0068 -0.0030 334 GLU A N 2598 C CA . GLU A 334 ? 0.1091 0.1044 0.1109 -0.0052 -0.0014 0.0038 334 GLU A CA 2599 C C . GLU A 334 ? 0.1081 0.1144 0.1035 -0.0050 -0.0057 -0.0032 334 GLU A C 2600 O O . GLU A 334 ? 0.1160 0.1112 0.1101 0.0002 -0.0084 0.0043 334 GLU A O 2601 C CB . GLU A 334 ? 0.1025 0.1143 0.1067 -0.0113 -0.0059 0.0006 334 GLU A CB 2602 C CG . GLU A 334 ? 0.1077 0.1220 0.1081 -0.0068 -0.0094 0.0008 334 GLU A CG 2603 C CD . GLU A 334 ? 0.1336 0.1439 0.1416 -0.0065 -0.0015 -0.0094 334 GLU A CD 2604 O OE1 . GLU A 334 ? 0.2227 0.1919 0.2026 -0.0730 0.0504 -0.0441 334 GLU A OE1 2605 O OE2 . GLU A 334 ? 0.1434 0.1322 0.1470 -0.0186 -0.0179 0.0053 334 GLU A OE2 2606 N N . ALA A 335 ? 0.1123 0.1208 0.1025 -0.0061 -0.0045 0.0007 335 ALA A N 2607 C CA . ALA A 335 ? 0.1065 0.1122 0.1026 0.0012 -0.0031 0.0000 335 ALA A CA 2608 C C . ALA A 335 ? 0.1045 0.1054 0.0989 0.0010 0.0030 -0.0018 335 ALA A C 2609 O O . ALA A 335 ? 0.1106 0.1067 0.1100 0.0041 -0.0030 0.0018 335 ALA A O 2610 C CB . ALA A 335 ? 0.1179 0.1202 0.1119 -0.0021 0.0085 -0.0147 335 ALA A CB 2611 N N . LEU A 336 ? 0.1188 0.1061 0.1150 -0.0001 0.0065 0.0035 336 LEU A N 2612 C CA . LEU A 336 ? 0.1152 0.1120 0.1150 -0.0080 0.0007 0.0014 336 LEU A CA 2613 C C . LEU A 336 ? 0.1230 0.1187 0.1111 -0.0116 0.0017 0.0000 336 LEU A C 2614 O O . LEU A 336 ? 0.1452 0.1194 0.1147 -0.0112 0.0028 0.0037 336 LEU A O 2615 C CB . LEU A 336 ? 0.1160 0.1090 0.1313 -0.0057 0.0097 -0.0070 336 LEU A CB 2616 C CG . LEU A 336 ? 0.1429 0.1542 0.1595 -0.0039 -0.0042 -0.0023 336 LEU A CG 2617 C CD1 . LEU A 336 ? 0.1660 0.1975 0.1776 0.0039 -0.0305 0.0001 336 LEU A CD1 2618 C CD2 . LEU A 336 ? 0.1981 0.1821 0.1680 0.0497 -0.0179 -0.0047 336 LEU A CD2 2619 N N . THR A 337 ? 0.1169 0.1046 0.1117 -0.0164 -0.0028 0.0018 337 THR A N 2620 C CA . THR A 337 ? 0.1218 0.1186 0.1150 -0.0137 0.0024 0.0027 337 THR A CA 2621 C C . THR A 337 ? 0.1334 0.1237 0.1172 -0.0092 0.0071 -0.0022 337 THR A C 2622 O O . THR A 337 ? 0.1654 0.1357 0.1336 -0.0105 0.0079 0.0071 337 THR A O 2623 C CB . THR A 337 ? 0.1205 0.1457 0.1135 -0.0122 0.0030 0.0017 337 THR A CB 2624 O OG1 . THR A 337 ? 0.1358 0.1336 0.1253 0.0070 0.0091 0.0123 337 THR A OG1 2625 C CG2 . THR A 337 ? 0.1313 0.1519 0.1202 -0.0218 -0.0009 -0.0005 337 THR A CG2 2626 N N . ARG A 338 ? 0.1170 0.1181 0.1106 -0.0046 0.0064 0.0000 338 ARG A N 2627 C CA . ARG A 338 ? 0.1269 0.1162 0.1059 0.0022 -0.0104 -0.0015 338 ARG A CA 2628 C C . ARG A 338 ? 0.1411 0.1237 0.1189 0.0000 -0.0185 -0.0014 338 ARG A C 2629 O O . ARG A 338 ? 0.1637 0.1433 0.1384 0.0034 -0.0302 -0.0068 338 ARG A O 2630 C CB . ARG A 338 ? 0.1133 0.1040 0.1200 0.0038 -0.0087 -0.0001 338 ARG A CB 2631 C CG . ARG A 338 ? 0.1112 0.1151 0.1336 0.0090 -0.0074 0.0061 338 ARG A CG 2632 C CD . ARG A 338 ? 0.1329 0.1169 0.1233 -0.0030 -0.0072 -0.0079 338 ARG A CD 2633 N NE . ARG A 338 ? 0.1294 0.1321 0.1295 0.0094 -0.0037 -0.0119 338 ARG A NE 2634 C CZ . ARG A 338 ? 0.1145 0.1138 0.1255 -0.0140 0.0092 -0.0083 338 ARG A CZ 2635 N NH1 . ARG A 338 ? 0.1413 0.1021 0.1372 0.0039 -0.0019 -0.0119 338 ARG A NH1 2636 N NH2 . ARG A 338 ? 0.1135 0.0944 0.1392 -0.0113 -0.0085 -0.0086 338 ARG A NH2 2637 N N . GLY A 339 ? 0.1359 0.1194 0.1213 -0.0015 -0.0175 -0.0065 339 GLY A N 2638 C CA . GLY A 339 ? 0.1232 0.1178 0.1235 -0.0042 -0.0010 -0.0055 339 GLY A CA 2639 C C . GLY A 339 ? 0.1185 0.1158 0.1196 -0.0039 -0.0017 -0.0007 339 GLY A C 2640 O O . GLY A 339 ? 0.1178 0.1287 0.1206 -0.0060 -0.0031 -0.0057 339 GLY A O 2641 N N . MET A 340 ? 0.1149 0.1149 0.1064 -0.0057 -0.0013 -0.0023 340 MET A N 2642 C CA . MET A 340 ? 0.1175 0.1148 0.1147 0.0005 0.0001 -0.0015 340 MET A CA 2643 C C . MET A 340 ? 0.0971 0.1137 0.1077 -0.0066 -0.0033 -0.0007 340 MET A C 2644 O O . MET A 340 ? 0.1278 0.1185 0.1148 -0.0108 0.0091 0.0004 340 MET A O 2645 C CB A MET A 340 ? 0.1180 0.1114 0.1100 0.0053 -0.0020 -0.0014 340 MET A CB 2646 C CB B MET A 340 ? 0.1337 0.1251 0.1199 0.0037 -0.0048 -0.0003 340 MET A CB 2647 C CG A MET A 340 ? 0.0901 0.1061 0.1047 -0.0201 0.0076 -0.0056 340 MET A CG 2648 C CG B MET A 340 ? 0.1701 0.1381 0.1501 0.0041 -0.0002 -0.0045 340 MET A CG 2649 S SD A MET A 340 ? 0.0411 0.0772 0.0778 -0.0090 -0.0008 -0.0037 340 MET A SD 2650 S SD B MET A 340 ? 0.2157 0.1684 0.1609 -0.0019 0.0014 0.0053 340 MET A SD 2651 C CE A MET A 340 ? 0.0429 0.0855 0.0760 -0.0094 0.0013 -0.0066 340 MET A CE 2652 C CE B MET A 340 ? 0.1714 0.1525 0.1717 -0.0055 -0.0060 -0.0028 340 MET A CE 2653 N N . VAL A 341 ? 0.1048 0.0986 0.1124 -0.0099 0.0036 0.0009 341 VAL A N 2654 C CA . VAL A 341 ? 0.0926 0.0952 0.1053 -0.0005 0.0062 0.0008 341 VAL A CA 2655 C C . VAL A 341 ? 0.0985 0.0931 0.1056 -0.0008 0.0043 0.0027 341 VAL A C 2656 O O . VAL A 341 ? 0.0903 0.1003 0.1125 -0.0056 -0.0049 0.0011 341 VAL A O 2657 C CB . VAL A 341 ? 0.0885 0.0986 0.1004 -0.0104 0.0175 0.0036 341 VAL A CB 2658 C CG1 . VAL A 341 ? 0.0973 0.0981 0.1110 0.0083 0.0123 -0.0026 341 VAL A CG1 2659 C CG2 . VAL A 341 ? 0.1018 0.1127 0.1244 -0.0024 -0.0004 0.0135 341 VAL A CG2 2660 N N . LEU A 342 ? 0.1003 0.0928 0.0984 0.0010 -0.0108 -0.0017 342 LEU A N 2661 C CA . LEU A 342 ? 0.0953 0.1008 0.0979 -0.0019 -0.0025 -0.0021 342 LEU A CA 2662 C C . LEU A 342 ? 0.0920 0.0890 0.0982 0.0029 0.0017 0.0062 342 LEU A C 2663 O O . LEU A 342 ? 0.1114 0.0993 0.1063 0.0106 0.0004 0.0012 342 LEU A O 2664 C CB . LEU A 342 ? 0.1012 0.0980 0.1042 -0.0053 0.0091 -0.0001 342 LEU A CB 2665 C CG . LEU A 342 ? 0.1229 0.1203 0.1170 -0.0022 0.0078 -0.0027 342 LEU A CG 2666 C CD1 . LEU A 342 ? 0.1118 0.1336 0.1492 -0.0137 -0.0032 0.0129 342 LEU A CD1 2667 C CD2 . LEU A 342 ? 0.1215 0.1482 0.1139 -0.0070 0.0013 -0.0040 342 LEU A CD2 2668 N N . ALA A 343 ? 0.1114 0.0955 0.1020 -0.0027 -0.0039 -0.0031 343 ALA A N 2669 C CA . ALA A 343 ? 0.1009 0.0977 0.0954 0.0002 0.0035 0.0024 343 ALA A CA 2670 C C . ALA A 343 ? 0.0927 0.0994 0.1115 -0.0032 0.0047 0.0026 343 ALA A C 2671 O O . ALA A 343 ? 0.1014 0.0928 0.1221 0.0065 -0.0023 0.0001 343 ALA A O 2672 C CB . ALA A 343 ? 0.1209 0.1082 0.1151 -0.0067 0.0105 0.0029 343 ALA A CB 2673 N N . MET A 344 ? 0.1027 0.1047 0.0973 0.0026 -0.0021 -0.0037 344 MET A N 2674 C CA . MET A 344 ? 0.0993 0.1007 0.1053 0.0061 0.0011 -0.0076 344 MET A CA 2675 C C . MET A 344 ? 0.0916 0.0970 0.1020 0.0055 -0.0023 -0.0028 344 MET A C 2676 O O . MET A 344 ? 0.0999 0.1109 0.1197 0.0187 -0.0015 -0.0087 344 MET A O 2677 C CB . MET A 344 ? 0.1119 0.1082 0.1128 0.0108 -0.0028 0.0021 344 MET A CB 2678 C CG . MET A 344 ? 0.0822 0.1146 0.1163 0.0031 0.0070 -0.0027 344 MET A CG 2679 S SD . MET A 344 ? 0.1241 0.1329 0.1495 -0.0018 0.0130 -0.0046 344 MET A SD 2680 C CE . MET A 344 ? 0.1326 0.1376 0.1356 -0.0018 0.0049 0.0102 344 MET A CE 2681 N N . SER A 345 ? 0.0954 0.0995 0.1021 0.0081 -0.0041 -0.0046 345 SER A N 2682 C CA . SER A 345 ? 0.0971 0.0972 0.1045 -0.0015 -0.0023 -0.0008 345 SER A CA 2683 C C . SER A 345 ? 0.1063 0.0950 0.0993 0.0016 -0.0030 -0.0075 345 SER A C 2684 O O . SER A 345 ? 0.0967 0.1097 0.1116 0.0064 -0.0048 -0.0110 345 SER A O 2685 C CB . SER A 345 ? 0.0942 0.1091 0.1004 -0.0037 -0.0083 -0.0072 345 SER A CB 2686 O OG . SER A 345 ? 0.1113 0.1150 0.1235 -0.0069 -0.0056 0.0018 345 SER A OG 2687 N N . ILE A 346 ? 0.1021 0.1154 0.0991 0.0105 -0.0079 -0.0112 346 ILE A N 2688 C CA . ILE A 346 ? 0.1068 0.1108 0.1065 0.0057 -0.0066 -0.0037 346 ILE A CA 2689 C C . ILE A 346 ? 0.1066 0.1117 0.1114 0.0082 -0.0051 -0.0021 346 ILE A C 2690 O O . ILE A 346 ? 0.0989 0.1127 0.1165 0.0079 -0.0098 -0.0039 346 ILE A O 2691 C CB . ILE A 346 ? 0.1116 0.1168 0.1106 -0.0001 -0.0023 -0.0024 346 ILE A CB 2692 C CG1 . ILE A 346 ? 0.1395 0.1220 0.1154 0.0061 -0.0067 -0.0039 346 ILE A CG1 2693 C CG2 . ILE A 346 ? 0.1130 0.1355 0.1060 0.0121 -0.0079 -0.0056 346 ILE A CG2 2694 C CD1 . ILE A 346 ? 0.1288 0.1265 0.1226 0.0004 -0.0080 -0.0020 346 ILE A CD1 2695 N N . TRP A 347 ? 0.1014 0.1214 0.1090 0.0015 -0.0021 0.0043 347 TRP A N 2696 C CA . TRP A 347 ? 0.1118 0.1190 0.1090 0.0034 -0.0023 0.0073 347 TRP A CA 2697 C C . TRP A 347 ? 0.1225 0.1315 0.1108 0.0125 -0.0012 0.0042 347 TRP A C 2698 O O . TRP A 347 ? 0.1174 0.1426 0.1065 0.0155 -0.0025 0.0072 347 TRP A O 2699 C CB . TRP A 347 ? 0.1272 0.1222 0.1127 0.0014 -0.0008 -0.0003 347 TRP A CB 2700 C CG . TRP A 347 ? 0.1106 0.1194 0.1209 0.0058 0.0004 0.0038 347 TRP A CG 2701 C CD1 . TRP A 347 ? 0.1104 0.1225 0.1093 0.0043 -0.0056 0.0063 347 TRP A CD1 2702 C CD2 . TRP A 347 ? 0.1099 0.1108 0.1284 0.0076 -0.0064 0.0034 347 TRP A CD2 2703 N NE1 . TRP A 347 ? 0.1379 0.1422 0.1116 0.0004 0.0003 0.0022 347 TRP A NE1 2704 C CE2 . TRP A 347 ? 0.1187 0.1302 0.1134 -0.0046 0.0008 -0.0048 347 TRP A CE2 2705 C CE3 . TRP A 347 ? 0.1214 0.1288 0.1307 0.0098 0.0000 -0.0028 347 TRP A CE3 2706 C CZ2 . TRP A 347 ? 0.1112 0.1225 0.1263 -0.0085 -0.0015 0.0046 347 TRP A CZ2 2707 C CZ3 . TRP A 347 ? 0.1324 0.1343 0.1140 0.0029 0.0143 -0.0050 347 TRP A CZ3 2708 C CH2 . TRP A 347 ? 0.1184 0.1104 0.1331 0.0079 -0.0026 -0.0076 347 TRP A CH2 2709 N N . TRP A 348 ? 0.1296 0.1266 0.1140 0.0108 0.0049 0.0053 348 TRP A N 2710 C CA . TRP A 348 ? 0.1251 0.1366 0.1139 0.0067 -0.0023 0.0004 348 TRP A CA 2711 C C . TRP A 348 ? 0.1398 0.1462 0.1137 0.0047 0.0032 -0.0012 348 TRP A C 2712 O O . TRP A 348 ? 0.1513 0.1498 0.1279 0.0103 -0.0060 0.0000 348 TRP A O 2713 C CB . TRP A 348 ? 0.1461 0.1489 0.1174 0.0035 0.0040 0.0027 348 TRP A CB 2714 C CG . TRP A 348 ? 0.1348 0.1503 0.1272 0.0015 0.0054 -0.0006 348 TRP A CG 2715 C CD1 . TRP A 348 ? 0.1631 0.1562 0.1410 0.0062 -0.0081 -0.0041 348 TRP A CD1 2716 C CD2 . TRP A 348 ? 0.1590 0.1492 0.1389 0.0092 -0.0011 0.0022 348 TRP A CD2 2717 N NE1 . TRP A 348 ? 0.1654 0.1788 0.1475 0.0107 -0.0084 -0.0176 348 TRP A NE1 2718 C CE2 . TRP A 348 ? 0.1569 0.1591 0.1249 0.0050 0.0030 -0.0112 348 TRP A CE2 2719 C CE3 . TRP A 348 ? 0.1500 0.1547 0.1376 0.0019 0.0009 0.0009 348 TRP A CE3 2720 C CZ2 . TRP A 348 ? 0.1723 0.1577 0.1603 0.0071 -0.0046 -0.0142 348 TRP A CZ2 2721 C CZ3 . TRP A 348 ? 0.1632 0.1695 0.1403 -0.0002 -0.0091 -0.0024 348 TRP A CZ3 2722 C CH2 . TRP A 348 ? 0.1725 0.1611 0.1298 0.0051 0.0035 -0.0149 348 TRP A CH2 2723 N N . ASP A 349 ? 0.1545 0.1558 0.1313 0.0066 -0.0076 0.0118 349 ASP A N 2724 C CA . ASP A 349 ? 0.1546 0.1651 0.1440 0.0021 -0.0032 0.0059 349 ASP A CA 2725 C C . ASP A 349 ? 0.1684 0.1724 0.1605 0.0041 0.0041 0.0148 349 ASP A C 2726 O O . ASP A 349 ? 0.1804 0.1747 0.1632 0.0143 0.0064 0.0117 349 ASP A O 2727 C CB . ASP A 349 ? 0.1625 0.1555 0.1478 -0.0096 -0.0005 0.0156 349 ASP A CB 2728 C CG . ASP A 349 ? 0.1602 0.1796 0.1553 -0.0055 -0.0032 0.0063 349 ASP A CG 2729 O OD1 . ASP A 349 ? 0.1630 0.2348 0.2309 -0.0020 0.0259 0.0138 349 ASP A OD1 2730 O OD2 . ASP A 349 ? 0.1557 0.1841 0.1813 0.0123 -0.0025 0.0276 349 ASP A OD2 2731 N N . GLN A 350 ? 0.1943 0.1930 0.1726 0.0139 0.0094 0.0075 350 GLN A N 2732 C CA . GLN A 350 ? 0.1986 0.2050 0.1893 0.0090 0.0107 0.0056 350 GLN A CA 2733 C C . GLN A 350 ? 0.2117 0.2166 0.1994 0.0118 0.0101 0.0037 350 GLN A C 2734 O O . GLN A 350 ? 0.2531 0.2257 0.2086 0.0046 0.0089 0.0266 350 GLN A O 2735 C CB A GLN A 350 ? 0.2025 0.2075 0.1886 0.0133 0.0108 0.0013 350 GLN A CB 2736 C CB B GLN A 350 ? 0.2048 0.2113 0.1937 0.0143 0.0101 0.0000 350 GLN A CB 2737 C CG A GLN A 350 ? 0.2105 0.2199 0.1920 0.0079 0.0160 0.0024 350 GLN A CG 2738 C CG B GLN A 350 ? 0.2240 0.2264 0.2275 0.0063 0.0132 -0.0019 350 GLN A CG 2739 C CD A GLN A 350 ? 0.2420 0.2474 0.2306 0.0046 0.0062 0.0002 350 GLN A CD 2740 C CD B GLN A 350 ? 0.2498 0.2530 0.2583 0.0046 0.0062 -0.0111 350 GLN A CD 2741 O OE1 A GLN A 350 ? 0.2283 0.2635 0.2530 0.0055 0.0133 -0.0193 350 GLN A OE1 2742 O OE1 B GLN A 350 ? 0.2882 0.2677 0.3161 0.0013 0.0026 -0.0069 350 GLN A OE1 2743 N NE2 A GLN A 350 ? 0.2358 0.2542 0.2445 0.0003 0.0170 0.0051 350 GLN A NE2 2744 N NE2 B GLN A 350 ? 0.2522 0.2443 0.2540 0.0041 0.0076 -0.0112 350 GLN A NE2 2745 N N . GLY A 351 ? 0.2069 0.2171 0.2150 0.0053 0.0167 0.0139 351 GLY A N 2746 C CA . GLY A 351 ? 0.2322 0.2360 0.2314 0.0050 0.0080 0.0098 351 GLY A CA 2747 C C . GLY A 351 ? 0.2532 0.2550 0.2336 0.0116 0.0041 0.0100 351 GLY A C 2748 O O . GLY A 351 ? 0.3326 0.3385 0.2802 0.0163 0.0071 0.0233 351 GLY A O 2749 N N . GLY A 352 ? 0.2303 0.2371 0.2304 0.0021 0.0084 0.0092 352 GLY A N 2750 C CA . GLY A 352 ? 0.2030 0.1991 0.1926 0.0007 0.0018 0.0033 352 GLY A CA 2751 C C . GLY A 352 ? 0.1893 0.1886 0.1696 0.0035 0.0023 0.0015 352 GLY A C 2752 O O . GLY A 352 ? 0.1727 0.1756 0.1511 0.0073 0.0071 0.0013 352 GLY A O 2753 N N . ASN A 353 ? 0.1715 0.1677 0.1384 0.0082 0.0087 0.0072 353 ASN A N 2754 C CA . ASN A 353 ? 0.1651 0.1686 0.1469 0.0051 0.0025 0.0035 353 ASN A CA 2755 C C . ASN A 353 ? 0.1538 0.1609 0.1413 0.0044 -0.0012 0.0012 353 ASN A C 2756 O O . ASN A 353 ? 0.1621 0.1661 0.1303 0.0199 -0.0106 0.0046 353 ASN A O 2757 C CB . ASN A 353 ? 0.1591 0.1723 0.1478 0.0138 0.0054 0.0031 353 ASN A CB 2758 C CG . ASN A 353 ? 0.1773 0.1852 0.1463 0.0060 0.0005 0.0179 353 ASN A CG 2759 O OD1 . ASN A 353 ? 0.2261 0.2231 0.1586 0.0130 0.0006 0.0328 353 ASN A OD1 2760 N ND2 . ASN A 353 ? 0.1839 0.1858 0.1247 0.0005 -0.0013 0.0024 353 ASN A ND2 2761 N N . MET A 354 ? 0.1510 0.1611 0.1377 0.0074 -0.0029 -0.0014 354 MET A N 2762 C CA . MET A 354 ? 0.1457 0.1529 0.1346 0.0052 -0.0038 -0.0029 354 MET A CA 2763 C C . MET A 354 ? 0.1339 0.1455 0.1319 0.0009 -0.0079 0.0033 354 MET A C 2764 O O . MET A 354 ? 0.1450 0.1355 0.1102 -0.0023 0.0003 0.0031 354 MET A O 2765 C CB . MET A 354 ? 0.1573 0.1508 0.1351 0.0085 -0.0107 0.0000 354 MET A CB 2766 C CG . MET A 354 ? 0.1452 0.1546 0.1392 0.0110 -0.0138 -0.0069 354 MET A CG 2767 S SD . MET A 354 ? 0.1288 0.1389 0.1322 0.0131 -0.0129 0.0163 354 MET A SD 2768 C CE . MET A 354 ? 0.1383 0.1431 0.1323 0.0042 -0.0014 0.0078 354 MET A CE 2769 N N . GLU A 355 ? 0.1403 0.1560 0.1392 -0.0003 0.0047 -0.0007 355 GLU A N 2770 C CA . GLU A 355 ? 0.1521 0.1484 0.1401 0.0032 -0.0005 0.0032 355 GLU A CA 2771 C C . GLU A 355 ? 0.1385 0.1440 0.1270 0.0079 -0.0099 0.0011 355 GLU A C 2772 O O . GLU A 355 ? 0.1444 0.1524 0.1235 0.0165 -0.0138 0.0073 355 GLU A O 2773 C CB . GLU A 355 ? 0.1619 0.1379 0.1507 -0.0123 0.0028 -0.0008 355 GLU A CB 2774 C CG . GLU A 355 ? 0.1661 0.1586 0.1470 -0.0084 0.0092 0.0061 355 GLU A CG 2775 C CD . GLU A 355 ? 0.2107 0.1795 0.1509 -0.0102 0.0067 0.0113 355 GLU A CD 2776 O OE1 . GLU A 355 ? 0.2942 0.2175 0.1692 -0.0152 -0.0176 0.0238 355 GLU A OE1 2777 O OE2 . GLU A 355 ? 0.2756 0.2118 0.1472 -0.0283 0.0075 0.0209 355 GLU A OE2 2778 N N . TRP A 356 ? 0.1358 0.1382 0.1304 0.0088 -0.0034 0.0039 356 TRP A N 2779 C CA . TRP A 356 ? 0.1449 0.1332 0.1283 0.0043 -0.0057 0.0034 356 TRP A CA 2780 C C . TRP A 356 ? 0.1384 0.1409 0.1334 0.0072 -0.0055 -0.0029 356 TRP A C 2781 O O . TRP A 356 ? 0.1490 0.1282 0.1276 0.0012 -0.0078 -0.0143 356 TRP A O 2782 C CB . TRP A 356 ? 0.1445 0.1414 0.1294 -0.0029 -0.0061 -0.0057 356 TRP A CB 2783 C CG . TRP A 356 ? 0.1485 0.1455 0.1244 0.0012 -0.0118 -0.0045 356 TRP A CG 2784 C CD1 . TRP A 356 ? 0.1655 0.1697 0.1422 0.0127 -0.0025 0.0097 356 TRP A CD1 2785 C CD2 . TRP A 356 ? 0.1519 0.1620 0.1259 0.0003 -0.0189 0.0000 356 TRP A CD2 2786 N NE1 . TRP A 356 ? 0.1543 0.1554 0.1483 0.0047 -0.0041 0.0039 356 TRP A NE1 2787 C CE2 . TRP A 356 ? 0.1701 0.1716 0.1344 -0.0025 -0.0227 -0.0018 356 TRP A CE2 2788 C CE3 . TRP A 356 ? 0.1559 0.1677 0.1404 0.0023 -0.0065 0.0022 356 TRP A CE3 2789 C CZ2 . TRP A 356 ? 0.1834 0.1654 0.1669 0.0081 -0.0073 0.0097 356 TRP A CZ2 2790 C CZ3 . TRP A 356 ? 0.1795 0.1645 0.1354 0.0058 -0.0017 -0.0044 356 TRP A CZ3 2791 C CH2 . TRP A 356 ? 0.1814 0.1659 0.1528 0.0074 0.0017 0.0172 356 TRP A CH2 2792 N N . LEU A 357 ? 0.1384 0.1361 0.1212 -0.0017 -0.0140 -0.0084 357 LEU A N 2793 C CA . LEU A 357 ? 0.1355 0.1369 0.1256 0.0063 -0.0081 -0.0036 357 LEU A CA 2794 C C . LEU A 357 ? 0.1334 0.1623 0.1241 0.0113 -0.0073 -0.0084 357 LEU A C 2795 O O . LEU A 357 ? 0.1342 0.1704 0.1343 0.0135 -0.0129 -0.0156 357 LEU A O 2796 C CB . LEU A 357 ? 0.1378 0.1380 0.1203 0.0095 -0.0091 -0.0101 357 LEU A CB 2797 C CG . LEU A 357 ? 0.1465 0.1246 0.1301 -0.0024 -0.0106 -0.0099 357 LEU A CG 2798 C CD1 . LEU A 357 ? 0.1689 0.1511 0.1398 -0.0054 0.0006 -0.0103 357 LEU A CD1 2799 C CD2 . LEU A 357 ? 0.1540 0.1384 0.1498 -0.0081 0.0002 -0.0004 357 LEU A CD2 2800 N N . ASP A 358 ? 0.1276 0.1427 0.1316 0.0071 -0.0028 -0.0009 358 ASP A N 2801 C CA . ASP A 358 ? 0.1422 0.1467 0.1396 0.0057 -0.0142 -0.0043 358 ASP A CA 2802 C C . ASP A 358 ? 0.1431 0.1467 0.1423 0.0076 -0.0103 -0.0046 358 ASP A C 2803 O O . ASP A 358 ? 0.1537 0.1659 0.1326 0.0194 -0.0215 -0.0177 358 ASP A O 2804 C CB . ASP A 358 ? 0.1363 0.1443 0.1370 0.0085 -0.0101 -0.0068 358 ASP A CB 2805 C CG . ASP A 358 ? 0.1386 0.1447 0.1326 0.0062 -0.0093 0.0029 358 ASP A CG 2806 O OD1 . ASP A 358 ? 0.1138 0.1635 0.1380 0.0092 -0.0076 -0.0083 358 ASP A OD1 2807 O OD2 . ASP A 358 ? 0.1328 0.1513 0.1088 0.0147 -0.0100 -0.0179 358 ASP A OD2 2808 N N . HIS A 359 ? 0.1566 0.1569 0.1368 0.0056 -0.0222 0.0035 359 HIS A N 2809 C CA . HIS A 359 ? 0.1678 0.1656 0.1546 0.0001 -0.0113 0.0036 359 HIS A CA 2810 C C . HIS A 359 ? 0.1754 0.1620 0.1591 0.0032 -0.0171 0.0057 359 HIS A C 2811 O O . HIS A 359 ? 0.1690 0.1652 0.1494 0.0005 -0.0183 0.0028 359 HIS A O 2812 C CB . HIS A 359 ? 0.1740 0.1681 0.1506 -0.0010 -0.0066 -0.0027 359 HIS A CB 2813 C CG . HIS A 359 ? 0.1804 0.1858 0.1482 0.0001 -0.0240 0.0027 359 HIS A CG 2814 N ND1 . HIS A 359 ? 0.2159 0.2201 0.1620 -0.0245 -0.0210 0.0009 359 HIS A ND1 2815 C CD2 . HIS A 359 ? 0.2166 0.2146 0.1795 -0.0292 -0.0266 0.0100 359 HIS A CD2 2816 C CE1 . HIS A 359 ? 0.2390 0.2561 0.1936 -0.0204 -0.0298 0.0249 359 HIS A CE1 2817 N NE2 . HIS A 359 ? 0.2350 0.2587 0.1954 -0.0164 -0.0162 0.0348 359 HIS A NE2 2818 N N . GLY A 360 ? 0.1885 0.1672 0.1754 0.0026 -0.0229 0.0043 360 GLY A N 2819 C CA . GLY A 360 ? 0.1863 0.1647 0.1785 0.0006 -0.0155 0.0088 360 GLY A CA 2820 C C . GLY A 360 ? 0.1874 0.1716 0.1940 0.0028 -0.0182 0.0050 360 GLY A C 2821 O O . GLY A 360 ? 0.2070 0.2120 0.2095 0.0027 -0.0143 0.0122 360 GLY A O 2822 N N . GLU A 361 ? 0.1770 0.1636 0.1894 0.0044 -0.0207 0.0072 361 GLU A N 2823 C CA . GLU A 361 ? 0.1809 0.1713 0.1907 0.0065 -0.0163 -0.0054 361 GLU A CA 2824 C C . GLU A 361 ? 0.1567 0.1783 0.1684 0.0097 -0.0143 -0.0041 361 GLU A C 2825 O O . GLU A 361 ? 0.1689 0.1624 0.1749 0.0194 -0.0338 -0.0194 361 GLU A O 2826 C CB . GLU A 361 ? 0.1849 0.1859 0.2016 -0.0004 -0.0094 -0.0071 361 GLU A CB 2827 C CG . GLU A 361 ? 0.2424 0.2243 0.2288 -0.0076 -0.0008 0.0005 361 GLU A CG 2828 C CD . GLU A 361 ? 0.2707 0.2383 0.2574 0.0036 0.0070 0.0007 361 GLU A CD 2829 O OE1 . GLU A 361 ? 0.2910 0.2391 0.2325 0.0169 0.0274 0.0138 361 GLU A OE1 2830 O OE2 . GLU A 361 ? 0.2707 0.2450 0.2679 -0.0056 0.0089 0.0157 361 GLU A OE2 2831 N N . ALA A 362 ? 0.1535 0.1566 0.1643 0.0030 -0.0160 -0.0136 362 ALA A N 2832 C CA . ALA A 362 ? 0.1562 0.1624 0.1599 0.0073 -0.0089 -0.0082 362 ALA A CA 2833 C C . ALA A 362 ? 0.1541 0.1553 0.1507 0.0078 -0.0120 -0.0042 362 ALA A C 2834 O O . ALA A 362 ? 0.1515 0.1463 0.1600 0.0223 -0.0258 -0.0074 362 ALA A O 2835 C CB . ALA A 362 ? 0.1471 0.1569 0.1500 0.0068 -0.0043 -0.0082 362 ALA A CB 2836 N N . GLY A 363 ? 0.1572 0.1542 0.1534 0.0113 -0.0183 -0.0010 363 GLY A N 2837 C CA . GLY A 363 ? 0.1708 0.1630 0.1548 0.0077 -0.0095 -0.0071 363 GLY A CA 2838 C C . GLY A 363 ? 0.1700 0.1643 0.1603 0.0026 -0.0149 -0.0028 363 GLY A C 2839 O O . GLY A 363 ? 0.1928 0.1754 0.1746 -0.0071 -0.0306 -0.0032 363 GLY A O 2840 N N . PRO A 364 ? 0.1590 0.1668 0.1578 0.0065 -0.0216 -0.0049 364 PRO A N 2841 C CA . PRO A 364 ? 0.1762 0.1731 0.1579 0.0063 -0.0193 -0.0047 364 PRO A CA 2842 C C . PRO A 364 ? 0.1712 0.1872 0.1600 0.0096 -0.0194 -0.0057 364 PRO A C 2843 O O . PRO A 364 ? 0.1962 0.2110 0.1650 0.0123 -0.0412 -0.0070 364 PRO A O 2844 C CB . PRO A 364 ? 0.1762 0.1726 0.1610 0.0102 -0.0205 -0.0030 364 PRO A CB 2845 C CG . PRO A 364 ? 0.1720 0.1774 0.1710 0.0000 -0.0270 -0.0059 364 PRO A CG 2846 C CD . PRO A 364 ? 0.1639 0.1619 0.1545 0.0058 -0.0192 -0.0132 364 PRO A CD 2847 N N . CYS A 365 ? 0.1777 0.1820 0.1598 0.0148 -0.0188 -0.0100 365 CYS A N 2848 C CA . CYS A 365 ? 0.1729 0.1722 0.1569 0.0032 -0.0138 -0.0068 365 CYS A CA 2849 C C . CYS A 365 ? 0.1844 0.1683 0.1579 0.0070 -0.0176 -0.0019 365 CYS A C 2850 O O . CYS A 365 ? 0.1904 0.1698 0.1630 0.0000 -0.0286 0.0142 365 CYS A O 2851 C CB . CYS A 365 ? 0.1660 0.1734 0.1439 0.0039 -0.0181 -0.0100 365 CYS A CB 2852 S SG . CYS A 365 ? 0.1762 0.1614 0.1492 0.0106 -0.0281 -0.0104 365 CYS A SG 2853 N N . ALA A 366 ? 0.1890 0.1789 0.1660 0.0047 -0.0146 0.0030 366 ALA A N 2854 C CA . ALA A 366 ? 0.1957 0.1872 0.1737 0.0014 -0.0081 0.0033 366 ALA A CA 2855 C C . ALA A 366 ? 0.2013 0.1894 0.1795 0.0007 -0.0080 0.0041 366 ALA A C 2856 O O . ALA A 366 ? 0.2095 0.1898 0.1715 0.0076 -0.0267 0.0093 366 ALA A O 2857 C CB . ALA A 366 ? 0.1861 0.2013 0.1679 0.0030 -0.0078 0.0070 366 ALA A CB 2858 N N . LYS A 367 ? 0.2160 0.2126 0.1957 0.0024 -0.0047 0.0136 367 LYS A N 2859 C CA . LYS A 367 ? 0.2114 0.2049 0.1920 0.0016 -0.0043 0.0100 367 LYS A CA 2860 C C . LYS A 367 ? 0.2045 0.2057 0.1927 -0.0002 -0.0063 0.0073 367 LYS A C 2861 O O . LYS A 367 ? 0.2248 0.2112 0.1858 0.0022 -0.0150 0.0107 367 LYS A O 2862 C CB . LYS A 367 ? 0.2402 0.2259 0.2184 -0.0005 -0.0087 0.0164 367 LYS A CB 2863 C CG . LYS A 367 ? 0.2611 0.2405 0.2420 0.0011 0.0117 0.0176 367 LYS A CG 2864 C CD . LYS A 367 ? 0.2836 0.2832 0.2726 -0.0010 -0.0036 0.0185 367 LYS A CD 2865 C CE . LYS A 367 ? 0.2844 0.2882 0.2750 -0.0028 -0.0131 0.0189 367 LYS A CE 2866 N NZ . LYS A 367 ? 0.3192 0.2944 0.2762 -0.0132 -0.0083 0.0133 367 LYS A NZ 2867 N N . GLY A 368 ? 0.1909 0.1876 0.1746 0.0076 -0.0044 0.0063 368 GLY A N 2868 C CA . GLY A 368 ? 0.1984 0.1933 0.1671 0.0078 -0.0111 -0.0010 368 GLY A CA 2869 C C . GLY A 368 ? 0.1962 0.1949 0.1559 0.0103 -0.0109 -0.0001 368 GLY A C 2870 O O . GLY A 368 ? 0.2205 0.2017 0.1479 0.0208 -0.0038 -0.0087 368 GLY A O 2871 N N . GLU A 369 ? 0.1879 0.1752 0.1530 0.0155 -0.0123 -0.0009 369 GLU A N 2872 C CA . GLU A 369 ? 0.1888 0.1763 0.1493 0.0081 -0.0131 -0.0026 369 GLU A CA 2873 C C . GLU A 369 ? 0.1867 0.1764 0.1526 0.0020 -0.0084 0.0014 369 GLU A C 2874 O O . GLU A 369 ? 0.1968 0.1755 0.1363 -0.0041 0.0006 -0.0069 369 GLU A O 2875 C CB . GLU A 369 ? 0.1925 0.1834 0.1472 0.0011 -0.0133 -0.0009 369 GLU A CB 2876 C CG . GLU A 369 ? 0.1948 0.1772 0.1538 0.0014 -0.0159 -0.0053 369 GLU A CG 2877 C CD . GLU A 369 ? 0.1953 0.1822 0.1593 0.0053 -0.0188 0.0003 369 GLU A CD 2878 O OE1 . GLU A 369 ? 0.1865 0.1793 0.1731 0.0033 -0.0267 -0.0082 369 GLU A OE1 2879 O OE2 . GLU A 369 ? 0.2262 0.2304 0.2223 0.0089 -0.0341 0.0063 369 GLU A OE2 2880 N N . GLY A 370 ? 0.1866 0.1673 0.1476 -0.0004 -0.0053 -0.0020 370 GLY A N 2881 C CA . GLY A 370 ? 0.1794 0.1717 0.1485 0.0039 -0.0078 0.0021 370 GLY A CA 2882 C C . GLY A 370 ? 0.1739 0.1665 0.1503 0.0001 -0.0092 -0.0023 370 GLY A C 2883 O O . GLY A 370 ? 0.1798 0.1809 0.1544 0.0066 -0.0155 0.0011 370 GLY A O 2884 N N . ALA A 371 ? 0.1862 0.1724 0.1407 0.0138 -0.0039 -0.0001 371 ALA A N 2885 C CA . ALA A 371 ? 0.1784 0.1700 0.1449 0.0037 -0.0008 0.0025 371 ALA A CA 2886 C C . ALA A 371 ? 0.1724 0.1643 0.1387 0.0037 0.0077 0.0058 371 ALA A C 2887 O O . ALA A 371 ? 0.1850 0.1622 0.1457 0.0118 0.0046 0.0039 371 ALA A O 2888 C CB . ALA A 371 ? 0.1822 0.1838 0.1548 0.0063 0.0049 0.0020 371 ALA A CB 2889 N N . PRO A 372 ? 0.1663 0.1672 0.1376 -0.0011 0.0064 0.0062 372 PRO A N 2890 C CA . PRO A 372 ? 0.1745 0.1673 0.1513 0.0068 0.0059 0.0020 372 PRO A CA 2891 C C . PRO A 372 ? 0.1945 0.1820 0.1684 0.0056 0.0010 0.0102 372 PRO A C 2892 O O . PRO A 372 ? 0.1887 0.1758 0.1701 0.0076 -0.0116 -0.0014 372 PRO A O 2893 C CB . PRO A 372 ? 0.1740 0.1738 0.1469 0.0066 0.0048 0.0013 372 PRO A CB 2894 C CG . PRO A 372 ? 0.1663 0.1735 0.1476 0.0075 -0.0006 0.0099 372 PRO A CG 2895 C CD . PRO A 372 ? 0.1764 0.1701 0.1461 0.0004 0.0034 0.0149 372 PRO A CD 2896 N N . SER A 373 ? 0.2065 0.1934 0.1705 0.0065 0.0056 0.0043 373 SER A N 2897 C CA . SER A 373 ? 0.2118 0.1942 0.1814 0.0066 -0.0019 0.0001 373 SER A CA 2898 C C . SER A 373 ? 0.2123 0.1988 0.1783 0.0058 -0.0036 -0.0010 373 SER A C 2899 O O . SER A 373 ? 0.2315 0.1974 0.1959 0.0139 -0.0162 -0.0063 373 SER A O 2900 C CB . SER A 373 ? 0.2317 0.2089 0.1871 0.0101 0.0054 -0.0044 373 SER A CB 2901 O OG . SER A 373 ? 0.2897 0.2407 0.1925 0.0213 0.0118 0.0171 373 SER A OG 2902 N N . ASN A 374 ? 0.2125 0.1756 0.1599 0.0080 -0.0108 -0.0039 374 ASN A N 2903 C CA . ASN A 374 ? 0.2007 0.1698 0.1581 0.0001 -0.0073 -0.0054 374 ASN A CA 2904 C C . ASN A 374 ? 0.1863 0.1710 0.1587 0.0000 -0.0098 -0.0080 374 ASN A C 2905 O O . ASN A 374 ? 0.1882 0.1866 0.1547 0.0011 -0.0225 -0.0069 374 ASN A O 2906 C CB . ASN A 374 ? 0.2021 0.1768 0.1543 0.0059 -0.0066 -0.0104 374 ASN A CB 2907 C CG . ASN A 374 ? 0.2031 0.1847 0.1609 0.0038 -0.0146 -0.0073 374 ASN A CG 2908 O OD1 . ASN A 374 ? 0.2470 0.2027 0.1373 0.0049 -0.0402 -0.0108 374 ASN A OD1 2909 N ND2 . ASN A 374 ? 0.1944 0.1876 0.1585 0.0119 -0.0191 -0.0130 374 ASN A ND2 2910 N N . ILE A 375 ? 0.1750 0.1625 0.1519 0.0036 -0.0125 -0.0070 375 ILE A N 2911 C CA . ILE A 375 ? 0.1683 0.1554 0.1520 0.0064 -0.0132 -0.0044 375 ILE A CA 2912 C C . ILE A 375 ? 0.1710 0.1621 0.1409 0.0043 -0.0123 -0.0029 375 ILE A C 2913 O O . ILE A 375 ? 0.1859 0.1701 0.1441 0.0006 -0.0213 -0.0090 375 ILE A O 2914 C CB . ILE A 375 ? 0.1515 0.1473 0.1517 0.0131 -0.0105 -0.0066 375 ILE A CB 2915 C CG1 . ILE A 375 ? 0.1709 0.1586 0.1480 0.0047 -0.0157 -0.0069 375 ILE A CG1 2916 C CG2 . ILE A 375 ? 0.1627 0.1548 0.1550 -0.0004 -0.0059 -0.0099 375 ILE A CG2 2917 C CD1 . ILE A 375 ? 0.1683 0.1628 0.1515 -0.0073 -0.0167 -0.0066 375 ILE A CD1 2918 N N . VAL A 376 ? 0.1704 0.1762 0.1515 0.0043 -0.0039 -0.0004 376 VAL A N 2919 C CA . VAL A 376 ? 0.1804 0.1742 0.1629 0.0000 -0.0152 -0.0016 376 VAL A CA 2920 C C . VAL A 376 ? 0.1863 0.1793 0.1693 0.0039 -0.0146 -0.0085 376 VAL A C 2921 O O . VAL A 376 ? 0.2107 0.1966 0.1846 -0.0078 -0.0314 0.0020 376 VAL A O 2922 C CB . VAL A 376 ? 0.1843 0.1664 0.1698 -0.0019 -0.0087 -0.0108 376 VAL A CB 2923 C CG1 . VAL A 376 ? 0.2096 0.1857 0.1948 0.0038 -0.0216 -0.0075 376 VAL A CG1 2924 C CG2 . VAL A 376 ? 0.1991 0.1819 0.1793 0.0050 -0.0076 -0.0095 376 VAL A CG2 2925 N N . GLN A 377 ? 0.2067 0.1748 0.1797 -0.0003 -0.0163 -0.0110 377 GLN A N 2926 C CA . GLN A 377 ? 0.1922 0.1931 0.1942 -0.0013 -0.0156 -0.0056 377 GLN A CA 2927 C C . GLN A 377 ? 0.2006 0.2054 0.1996 0.0025 -0.0128 -0.0037 377 GLN A C 2928 O O . GLN A 377 ? 0.2261 0.2543 0.2259 -0.0025 -0.0142 -0.0204 377 GLN A O 2929 C CB . GLN A 377 ? 0.2054 0.2147 0.1978 -0.0043 -0.0178 -0.0073 377 GLN A CB 2930 C CG . GLN A 377 ? 0.2313 0.2391 0.2180 -0.0052 -0.0147 -0.0060 377 GLN A CG 2931 C CD . GLN A 377 ? 0.2469 0.2716 0.2754 -0.0057 -0.0096 -0.0263 377 GLN A CD 2932 O OE1 . GLN A 377 ? 0.2213 0.2887 0.1929 -0.0173 -0.0171 -0.0099 377 GLN A OE1 2933 N NE2 . GLN A 377 ? 0.2647 0.3103 0.2740 -0.0047 0.0037 -0.0366 377 GLN A NE2 2934 N N . VAL A 378 ? 0.1970 0.2060 0.1913 -0.0015 -0.0143 -0.0019 378 VAL A N 2935 C CA . VAL A 378 ? 0.1878 0.1888 0.1866 0.0046 -0.0199 -0.0007 378 VAL A CA 2936 C C . VAL A 378 ? 0.1862 0.1843 0.1926 -0.0042 -0.0124 -0.0003 378 VAL A C 2937 O O . VAL A 378 ? 0.1997 0.2178 0.2015 0.0003 -0.0234 0.0016 378 VAL A O 2938 C CB . VAL A 378 ? 0.1940 0.1909 0.1802 -0.0062 -0.0247 -0.0034 378 VAL A CB 2939 C CG1 . VAL A 378 ? 0.2014 0.1872 0.1927 0.0047 -0.0324 -0.0057 378 VAL A CG1 2940 C CG2 . VAL A 378 ? 0.1891 0.1959 0.1936 -0.0018 -0.0251 -0.0022 378 VAL A CG2 2941 N N . GLU A 379 ? 0.1693 0.1776 0.1789 0.0032 -0.0104 -0.0002 379 GLU A N 2942 C CA . GLU A 379 ? 0.1754 0.1739 0.1741 0.0018 -0.0084 -0.0050 379 GLU A CA 2943 C C . GLU A 379 ? 0.1674 0.1719 0.1679 0.0020 -0.0088 -0.0061 379 GLU A C 2944 O O . GLU A 379 ? 0.1749 0.1749 0.1436 -0.0023 -0.0237 -0.0178 379 GLU A O 2945 C CB A GLU A 379 ? 0.1773 0.1757 0.1786 0.0048 -0.0070 -0.0042 379 GLU A CB 2946 C CB B GLU A 379 ? 0.1689 0.1688 0.1716 0.0061 -0.0069 -0.0032 379 GLU A CB 2947 C CG A GLU A 379 ? 0.1907 0.1927 0.1874 -0.0053 -0.0061 -0.0030 379 GLU A CG 2948 C CG B GLU A 379 ? 0.1442 0.1536 0.1598 0.0061 -0.0017 -0.0062 379 GLU A CG 2949 C CD A GLU A 379 ? 0.1925 0.2086 0.1927 -0.0098 0.0018 -0.0021 379 GLU A CD 2950 C CD B GLU A 379 ? 0.1276 0.1509 0.1351 0.0030 -0.0132 0.0000 379 GLU A CD 2951 O OE1 A GLU A 379 ? 0.2575 0.2146 0.1887 -0.0233 -0.0012 -0.0147 379 GLU A OE1 2952 O OE1 B GLU A 379 ? 0.1635 0.2019 0.2060 -0.0064 0.0067 0.0034 379 GLU A OE1 2953 O OE2 A GLU A 379 ? 0.2527 0.2183 0.2079 -0.0101 -0.0042 0.0079 379 GLU A OE2 2954 O OE2 B GLU A 379 ? 0.0834 0.1788 0.1352 0.0016 -0.0177 0.0046 379 GLU A OE2 2955 N N . PRO A 380 ? 0.1703 0.1703 0.1694 -0.0039 -0.0196 -0.0093 380 PRO A N 2956 C CA . PRO A 380 ? 0.1794 0.1640 0.1555 0.0025 -0.0122 -0.0144 380 PRO A CA 2957 C C . PRO A 380 ? 0.1663 0.1621 0.1527 0.0016 -0.0133 -0.0170 380 PRO A C 2958 O O . PRO A 380 ? 0.1842 0.1803 0.1521 0.0139 -0.0040 -0.0294 380 PRO A O 2959 C CB . PRO A 380 ? 0.1956 0.1621 0.1684 0.0069 -0.0167 -0.0154 380 PRO A CB 2960 C CG . PRO A 380 ? 0.1891 0.1671 0.1610 -0.0099 -0.0194 -0.0152 380 PRO A CG 2961 C CD . PRO A 380 ? 0.1821 0.1770 0.1885 0.0008 -0.0170 -0.0074 380 PRO A CD 2962 N N . PHE A 381 ? 0.1613 0.1579 0.1492 0.0066 -0.0127 -0.0180 381 PHE A N 2963 C CA . PHE A 381 ? 0.1509 0.1476 0.1471 0.0078 -0.0130 -0.0057 381 PHE A CA 2964 C C . PHE A 381 ? 0.1367 0.1458 0.1441 0.0098 -0.0110 0.0001 381 PHE A C 2965 O O . PHE A 381 ? 0.1614 0.1571 0.1433 -0.0004 -0.0026 -0.0160 381 PHE A O 2966 C CB . PHE A 381 ? 0.1666 0.1513 0.1504 0.0086 -0.0144 -0.0115 381 PHE A CB 2967 C CG . PHE A 381 ? 0.1739 0.1475 0.1529 0.0107 -0.0125 -0.0183 381 PHE A CG 2968 C CD1 . PHE A 381 ? 0.1895 0.1617 0.1646 0.0003 -0.0097 -0.0327 381 PHE A CD1 2969 C CD2 . PHE A 381 ? 0.1809 0.1864 0.1845 0.0115 -0.0092 -0.0228 381 PHE A CD2 2970 C CE1 . PHE A 381 ? 0.1681 0.1774 0.1703 0.0162 -0.0072 -0.0221 381 PHE A CE1 2971 C CE2 . PHE A 381 ? 0.1825 0.1800 0.1858 0.0050 -0.0199 -0.0310 381 PHE A CE2 2972 C CZ . PHE A 381 ? 0.1893 0.1805 0.1850 0.0144 -0.0099 -0.0313 381 PHE A CZ 2973 N N . PRO A 382 ? 0.1304 0.1328 0.1280 0.0139 -0.0098 -0.0051 382 PRO A N 2974 C CA . PRO A 382 ? 0.1359 0.1295 0.1226 0.0121 -0.0119 -0.0046 382 PRO A CA 2975 C C . PRO A 382 ? 0.1290 0.1310 0.1254 0.0068 -0.0149 -0.0036 382 PRO A C 2976 O O . PRO A 382 ? 0.1371 0.1434 0.1358 0.0009 -0.0104 -0.0220 382 PRO A O 2977 C CB . PRO A 382 ? 0.1374 0.1247 0.1212 0.0163 -0.0179 -0.0100 382 PRO A CB 2978 C CG . PRO A 382 ? 0.1400 0.1412 0.1265 0.0122 -0.0139 -0.0085 382 PRO A CG 2979 C CD . PRO A 382 ? 0.1412 0.1297 0.1405 0.0083 -0.0030 -0.0016 382 PRO A CD 2980 N N . GLU A 383 ? 0.1218 0.1358 0.1181 0.0041 -0.0112 -0.0033 383 GLU A N 2981 C CA . GLU A 383 ? 0.1240 0.1349 0.1258 0.0017 -0.0049 -0.0033 383 GLU A CA 2982 C C . GLU A 383 ? 0.1181 0.1339 0.1265 0.0030 -0.0095 -0.0051 383 GLU A C 2983 O O . GLU A 383 ? 0.1314 0.1456 0.1229 0.0100 -0.0016 -0.0123 383 GLU A O 2984 C CB . GLU A 383 ? 0.1265 0.1351 0.1261 0.0061 -0.0101 0.0028 383 GLU A CB 2985 C CG . GLU A 383 ? 0.1351 0.1388 0.1396 0.0114 -0.0090 -0.0068 383 GLU A CG 2986 C CD . GLU A 383 ? 0.1375 0.1482 0.1510 0.0005 -0.0066 -0.0058 383 GLU A CD 2987 O OE1 . GLU A 383 ? 0.1782 0.1548 0.1714 -0.0102 -0.0178 0.0045 383 GLU A OE1 2988 O OE2 . GLU A 383 ? 0.1801 0.1626 0.1689 0.0134 -0.0083 -0.0334 383 GLU A OE2 2989 N N . VAL A 384 ? 0.1222 0.1312 0.1144 0.0100 -0.0003 0.0007 384 VAL A N 2990 C CA . VAL A 384 ? 0.1139 0.1199 0.1185 0.0007 -0.0018 0.0001 384 VAL A CA 2991 C C . VAL A 384 ? 0.1192 0.1362 0.1239 0.0000 -0.0041 -0.0069 384 VAL A C 2992 O O . VAL A 384 ? 0.1240 0.1247 0.1243 0.0032 -0.0071 -0.0093 384 VAL A O 2993 C CB . VAL A 384 ? 0.1135 0.1208 0.1148 0.0004 0.0026 0.0022 384 VAL A CB 2994 C CG1 . VAL A 384 ? 0.1222 0.1281 0.1316 -0.0014 -0.0065 0.0123 384 VAL A CG1 2995 C CG2 . VAL A 384 ? 0.1054 0.1118 0.1378 0.0089 -0.0037 -0.0040 384 VAL A CG2 2996 N N . THR A 385 ? 0.1077 0.1314 0.1303 -0.0084 0.0021 -0.0063 385 THR A N 2997 C CA . THR A 385 ? 0.1074 0.1272 0.1284 -0.0043 0.0015 -0.0037 385 THR A CA 2998 C C . THR A 385 ? 0.1028 0.1260 0.1312 -0.0047 0.0042 -0.0055 385 THR A C 2999 O O . THR A 385 ? 0.1277 0.1171 0.1278 0.0030 -0.0018 0.0035 385 THR A O 3000 C CB . THR A 385 ? 0.1299 0.1354 0.1476 -0.0080 -0.0044 -0.0086 385 THR A CB 3001 O OG1 . THR A 385 ? 0.1297 0.1601 0.1491 -0.0082 -0.0019 -0.0134 385 THR A OG1 3002 C CG2 . THR A 385 ? 0.1367 0.1423 0.1516 -0.0104 0.0075 -0.0061 385 THR A CG2 3003 N N . TYR A 386 ? 0.1207 0.1189 0.1232 0.0037 0.0017 -0.0008 386 TYR A N 3004 C CA . TYR A 386 ? 0.1201 0.1213 0.1277 0.0020 0.0036 -0.0015 386 TYR A CA 3005 C C . TYR A 386 ? 0.1235 0.1296 0.1222 0.0024 0.0017 0.0022 386 TYR A C 3006 O O . TYR A 386 ? 0.1374 0.1355 0.1424 0.0046 0.0174 0.0114 386 TYR A O 3007 C CB . TYR A 386 ? 0.1298 0.1090 0.1256 -0.0012 0.0008 0.0012 386 TYR A CB 3008 C CG . TYR A 386 ? 0.1073 0.1085 0.1076 0.0028 0.0086 -0.0099 386 TYR A CG 3009 C CD1 . TYR A 386 ? 0.0945 0.1190 0.1324 0.0005 0.0130 0.0059 386 TYR A CD1 3010 C CD2 . TYR A 386 ? 0.0959 0.1391 0.1463 -0.0084 0.0022 0.0051 386 TYR A CD2 3011 C CE1 . TYR A 386 ? 0.1117 0.1020 0.1264 -0.0005 0.0025 0.0126 386 TYR A CE1 3012 C CE2 . TYR A 386 ? 0.1262 0.1333 0.1395 0.0050 0.0099 0.0047 386 TYR A CE2 3013 C CZ . TYR A 386 ? 0.1071 0.1181 0.1099 0.0013 0.0068 0.0148 386 TYR A CZ 3014 O OH . TYR A 386 ? 0.1193 0.1229 0.1184 -0.0091 -0.0024 0.0022 386 TYR A OH 3015 N N . THR A 387 ? 0.1267 0.1260 0.1301 0.0088 0.0086 -0.0017 387 THR A N 3016 C CA . THR A 387 ? 0.1225 0.1307 0.1377 0.0007 0.0081 -0.0027 387 THR A CA 3017 C C . THR A 387 ? 0.1087 0.1295 0.1392 -0.0021 0.0121 -0.0021 387 THR A C 3018 O O . THR A 387 ? 0.1176 0.1230 0.1414 -0.0186 0.0158 -0.0060 387 THR A O 3019 C CB . THR A 387 ? 0.1245 0.1337 0.1381 0.0006 0.0099 -0.0025 387 THR A CB 3020 O OG1 . THR A 387 ? 0.1310 0.1507 0.1679 -0.0166 -0.0041 -0.0195 387 THR A OG1 3021 C CG2 . THR A 387 ? 0.1329 0.1601 0.1488 -0.0034 0.0095 -0.0040 387 THR A CG2 3022 N N . ASN A 388 ? 0.1149 0.1213 0.1273 -0.0068 0.0079 -0.0081 388 ASN A N 3023 C CA . ASN A 388 ? 0.1237 0.1308 0.1343 -0.0025 0.0121 -0.0051 388 ASN A CA 3024 C C . ASN A 388 ? 0.1230 0.1265 0.1364 -0.0065 0.0097 -0.0087 388 ASN A C 3025 O O . ASN A 388 ? 0.1267 0.1305 0.1453 -0.0101 0.0213 -0.0045 388 ASN A O 3026 C CB . ASN A 388 ? 0.1251 0.1325 0.1360 -0.0015 0.0141 -0.0031 388 ASN A CB 3027 C CG . ASN A 388 ? 0.1158 0.1385 0.1777 0.0123 0.0109 -0.0015 388 ASN A CG 3028 O OD1 . ASN A 388 ? 0.1567 0.1206 0.1806 -0.0123 0.0002 -0.0041 388 ASN A OD1 3029 N ND2 . ASN A 388 ? 0.1313 0.1631 0.2046 0.0062 -0.0181 -0.0057 388 ASN A ND2 3030 N N . LEU A 389 ? 0.1249 0.1317 0.1289 -0.0100 0.0102 -0.0049 389 LEU A N 3031 C CA . LEU A 389 ? 0.1420 0.1385 0.1355 -0.0094 0.0005 -0.0041 389 LEU A CA 3032 C C . LEU A 389 ? 0.1335 0.1271 0.1276 -0.0093 0.0031 -0.0030 389 LEU A C 3033 O O . LEU A 389 ? 0.1480 0.1333 0.1407 -0.0148 0.0060 -0.0040 389 LEU A O 3034 C CB . LEU A 389 ? 0.1393 0.1366 0.1452 -0.0061 0.0001 -0.0029 389 LEU A CB 3035 C CG . LEU A 389 ? 0.1579 0.2101 0.1810 -0.0020 0.0078 -0.0040 389 LEU A CG 3036 C CD1 . LEU A 389 ? 0.1407 0.2122 0.1651 -0.0019 0.0248 -0.0043 389 LEU A CD1 3037 C CD2 . LEU A 389 ? 0.2007 0.2299 0.2049 0.0214 0.0209 0.0016 389 LEU A CD2 3038 N N . ARG A 390 ? 0.1368 0.1330 0.1353 -0.0067 0.0081 0.0033 390 ARG A N 3039 C CA . ARG A 390 ? 0.1381 0.1325 0.1320 -0.0034 -0.0019 -0.0029 390 ARG A CA 3040 C C . ARG A 390 ? 0.1337 0.1348 0.1201 -0.0066 0.0035 -0.0004 390 ARG A C 3041 O O . ARG A 390 ? 0.1686 0.1316 0.1283 -0.0102 -0.0030 0.0011 390 ARG A O 3042 C CB . ARG A 390 ? 0.1565 0.1363 0.1324 -0.0045 0.0092 -0.0008 390 ARG A CB 3043 C CG . ARG A 390 ? 0.1368 0.1454 0.1583 -0.0118 0.0073 -0.0191 390 ARG A CG 3044 C CD . ARG A 390 ? 0.1444 0.1511 0.1562 -0.0202 0.0076 -0.0097 390 ARG A CD 3045 N NE . ARG A 390 ? 0.1377 0.1515 0.1694 -0.0190 0.0338 0.0017 390 ARG A NE 3046 C CZ . ARG A 390 ? 0.1500 0.1522 0.1740 -0.0099 0.0128 0.0074 390 ARG A CZ 3047 N NH1 . ARG A 390 ? 0.1475 0.1556 0.1698 -0.0004 0.0093 0.0006 390 ARG A NH1 3048 N NH2 . ARG A 390 ? 0.1987 0.1776 0.2203 0.0025 0.0000 -0.0063 390 ARG A NH2 3049 N N . TRP A 391 ? 0.1178 0.1239 0.1216 -0.0032 0.0000 -0.0036 391 TRP A N 3050 C CA . TRP A 391 ? 0.1181 0.1300 0.1246 -0.0095 0.0080 -0.0042 391 TRP A CA 3051 C C . TRP A 391 ? 0.1140 0.1291 0.1287 -0.0042 0.0095 -0.0065 391 TRP A C 3052 O O . TRP A 391 ? 0.1372 0.1289 0.1452 -0.0164 0.0144 -0.0118 391 TRP A O 3053 C CB . TRP A 391 ? 0.1244 0.1379 0.1301 -0.0085 0.0044 -0.0022 391 TRP A CB 3054 C CG . TRP A 391 ? 0.1110 0.1336 0.1159 -0.0124 0.0188 -0.0029 391 TRP A CG 3055 C CD1 . TRP A 391 ? 0.1299 0.1318 0.1381 0.0028 -0.0002 -0.0040 391 TRP A CD1 3056 C CD2 . TRP A 391 ? 0.1000 0.1277 0.1239 -0.0093 0.0152 0.0138 391 TRP A CD2 3057 N NE1 . TRP A 391 ? 0.1316 0.1543 0.1487 0.0115 -0.0048 -0.0029 391 TRP A NE1 3058 C CE2 . TRP A 391 ? 0.1280 0.1497 0.1651 -0.0014 -0.0060 -0.0069 391 TRP A CE2 3059 C CE3 . TRP A 391 ? 0.1019 0.1274 0.1347 -0.0128 0.0141 -0.0004 391 TRP A CE3 3060 C CZ2 . TRP A 391 ? 0.1352 0.1492 0.1486 0.0007 0.0007 0.0048 391 TRP A CZ2 3061 C CZ3 . TRP A 391 ? 0.1281 0.1251 0.1434 -0.0079 0.0039 -0.0008 391 TRP A CZ3 3062 C CH2 . TRP A 391 ? 0.1401 0.1399 0.1441 0.0008 0.0153 -0.0081 391 TRP A CH2 3063 N N . GLY A 392 ? 0.1267 0.1281 0.1304 -0.0130 0.0092 -0.0032 392 GLY A N 3064 C CA . GLY A 392 ? 0.1227 0.1406 0.1259 -0.0133 0.0136 -0.0002 392 GLY A CA 3065 C C . GLY A 392 ? 0.1403 0.1488 0.1317 -0.0082 0.0126 -0.0036 392 GLY A C 3066 O O . GLY A 392 ? 0.1424 0.1421 0.1492 -0.0011 0.0213 -0.0110 392 GLY A O 3067 N N . GLU A 393 ? 0.1465 0.1514 0.1426 -0.0073 0.0188 -0.0107 393 GLU A N 3068 C CA . GLU A 393 ? 0.1599 0.1588 0.1601 -0.0051 0.0149 -0.0060 393 GLU A CA 3069 C C . GLU A 393 ? 0.1590 0.1512 0.1529 -0.0012 0.0172 -0.0116 393 GLU A C 3070 O O . GLU A 393 ? 0.1408 0.1717 0.1612 -0.0066 0.0223 -0.0017 393 GLU A O 3071 C CB . GLU A 393 ? 0.1813 0.1590 0.1511 -0.0038 0.0149 -0.0092 393 GLU A CB 3072 C CG . GLU A 393 ? 0.2190 0.2153 0.2159 -0.0043 0.0072 -0.0073 393 GLU A CG 3073 C CD . GLU A 393 ? 0.2378 0.2166 0.1921 -0.0007 0.0086 -0.0121 393 GLU A CD 3074 O OE1 . GLU A 393 ? 0.2669 0.2452 0.1923 -0.0237 0.0550 -0.0501 393 GLU A OE1 3075 O OE2 . GLU A 393 ? 0.3060 0.2964 0.2403 -0.0034 -0.0022 -0.0009 393 GLU A OE2 3076 N N . ILE A 394 ? 0.1660 0.1603 0.1661 -0.0014 0.0229 -0.0107 394 ILE A N 3077 C CA . ILE A 394 ? 0.1648 0.1707 0.1755 -0.0004 0.0146 -0.0104 394 ILE A CA 3078 C C . ILE A 394 ? 0.1633 0.1747 0.1687 0.0031 0.0169 -0.0050 394 ILE A C 3079 O O . ILE A 394 ? 0.1866 0.1987 0.1822 0.0047 0.0239 -0.0019 394 ILE A O 3080 C CB . ILE A 394 ? 0.1781 0.1802 0.1903 -0.0007 0.0077 -0.0032 394 ILE A CB 3081 C CG1 . ILE A 394 ? 0.2115 0.2260 0.2435 0.0083 0.0041 0.0112 394 ILE A CG1 3082 C CG2 . ILE A 394 ? 0.1808 0.1818 0.1809 0.0084 0.0040 -0.0074 394 ILE A CG2 3083 C CD1 . ILE A 394 ? 0.2170 0.2219 0.2455 0.0045 -0.0026 -0.0157 394 ILE A CD1 3084 N N . GLY A 395 ? 0.1543 0.1853 0.1744 -0.0015 0.0137 -0.0021 395 GLY A N 3085 C CA . GLY A 395 ? 0.1530 0.1734 0.1940 0.0025 0.0150 -0.0065 395 GLY A CA 3086 C C . GLY A 395 ? 0.1657 0.1879 0.2140 -0.0092 0.0106 0.0023 395 GLY A C 3087 O O . GLY A 395 ? 0.1578 0.2207 0.2850 -0.0138 0.0068 -0.0022 395 GLY A O 3088 N N . SER A 396 ? 0.1536 0.1824 0.1895 -0.0048 0.0247 -0.0079 396 SER A N 3089 C CA . SER A 396 ? 0.1731 0.1798 0.1918 -0.0023 0.0170 -0.0039 396 SER A CA 3090 C C . SER A 396 ? 0.1653 0.1709 0.1864 -0.0046 0.0209 -0.0028 396 SER A C 3091 O O . SER A 396 ? 0.1869 0.1724 0.1986 -0.0049 0.0362 -0.0060 396 SER A O 3092 C CB . SER A 396 ? 0.1623 0.1731 0.2047 -0.0048 0.0142 -0.0074 396 SER A CB 3093 O OG . SER A 396 ? 0.1656 0.1721 0.2052 -0.0012 0.0303 -0.0193 396 SER A OG 3094 N N . THR A 397 ? 0.1865 0.1802 0.1847 -0.0049 0.0188 -0.0001 397 THR A N 3095 C CA . THR A 397 ? 0.1955 0.1872 0.1907 -0.0053 0.0190 -0.0031 397 THR A CA 3096 C C . THR A 397 ? 0.2038 0.2053 0.2024 -0.0114 0.0134 -0.0022 397 THR A C 3097 O O . THR A 397 ? 0.2135 0.2071 0.2057 -0.0110 0.0218 -0.0194 397 THR A O 3098 C CB . THR A 397 ? 0.1841 0.1773 0.1881 -0.0031 0.0173 0.0056 397 THR A CB 3099 O OG1 . THR A 397 ? 0.1824 0.1717 0.1566 -0.0008 0.0357 -0.0014 397 THR A OG1 3100 C CG2 . THR A 397 ? 0.1887 0.1844 0.1950 -0.0009 0.0263 0.0080 397 THR A CG2 3101 N N . TYR A 398 ? 0.2276 0.2132 0.2116 -0.0066 0.0028 -0.0038 398 TYR A N 3102 C CA . TYR A 398 ? 0.2412 0.2413 0.2435 -0.0059 -0.0026 -0.0011 398 TYR A CA 3103 C C . TYR A 398 ? 0.2676 0.2840 0.2743 -0.0045 -0.0074 0.0030 398 TYR A C 3104 O O . TYR A 398 ? 0.3003 0.3287 0.3010 -0.0052 0.0060 -0.0007 398 TYR A O 3105 C CB . TYR A 398 ? 0.2437 0.2432 0.2408 -0.0050 -0.0004 -0.0020 398 TYR A CB 3106 C CG . TYR A 398 ? 0.2219 0.2245 0.2402 0.0076 0.0072 0.0054 398 TYR A CG 3107 C CD1 . TYR A 398 ? 0.2197 0.2221 0.2296 0.0042 0.0037 0.0002 398 TYR A CD1 3108 C CD2 . TYR A 398 ? 0.2145 0.2426 0.2634 0.0067 0.0053 0.0036 398 TYR A CD2 3109 C CE1 . TYR A 398 ? 0.2257 0.2215 0.2504 -0.0071 0.0061 0.0061 398 TYR A CE1 3110 C CE2 . TYR A 398 ? 0.2314 0.2460 0.2725 0.0009 0.0105 -0.0033 398 TYR A CE2 3111 C CZ . TYR A 398 ? 0.2410 0.2265 0.2603 0.0055 -0.0001 -0.0035 398 TYR A CZ 3112 O OH . TYR A 398 ? 0.2766 0.2304 0.3049 0.0004 0.0151 -0.0066 398 TYR A OH 3113 N N . GLN A 399 ? 0.2988 0.3362 0.3360 -0.0123 -0.0200 0.0045 399 GLN A N 3114 N N . PCA B 1 ? 0.1790 0.1761 0.1653 0.0040 -0.0099 -0.0039 1 PCA B N 3115 C CA . PCA B 1 ? 0.1636 0.1718 0.1578 0.0058 0.0029 0.0020 1 PCA B CA 3116 C CB . PCA B 1 ? 0.1582 0.1710 0.1504 0.0015 0.0047 0.0008 1 PCA B CB 3117 C CG . PCA B 1 ? 0.1273 0.1713 0.1414 -0.0003 0.0172 -0.0063 1 PCA B CG 3118 C CD . PCA B 1 ? 0.1604 0.1777 0.1599 0.0069 0.0086 -0.0069 1 PCA B CD 3119 O OE . PCA B 1 ? 0.1707 0.1675 0.1927 0.0106 0.0022 -0.0106 1 PCA B OE 3120 C C . PCA B 1 ? 0.1775 0.1797 0.1712 0.0007 0.0048 0.0036 1 PCA B C 3121 O O . PCA B 1 ? 0.1833 0.1956 0.1739 0.0046 0.0159 -0.0002 1 PCA B O 3122 N N . LYS B 2 ? 0.1740 0.1721 0.1679 0.0009 0.0135 0.0000 2 LYS B N 3123 C CA . LYS B 2 ? 0.1797 0.1768 0.1716 0.0041 0.0057 -0.0008 2 LYS B CA 3124 C C . LYS B 2 ? 0.1662 0.1701 0.1553 0.0063 0.0040 -0.0004 2 LYS B C 3125 O O . LYS B 2 ? 0.1645 0.1712 0.1325 0.0022 0.0111 0.0073 2 LYS B O 3126 C CB . LYS B 2 ? 0.1822 0.1836 0.1807 0.0046 -0.0059 0.0005 2 LYS B CB 3127 C CG . LYS B 2 ? 0.2289 0.2126 0.2364 0.0062 0.0066 0.0042 2 LYS B CG 3128 C CD . LYS B 2 ? 0.2501 0.2368 0.2601 0.0210 0.0032 -0.0050 2 LYS B CD 3129 C CE . LYS B 2 ? 0.3013 0.3193 0.3084 0.0120 0.0028 -0.0221 2 LYS B CE 3130 N NZ . LYS B 2 ? 0.2950 0.3250 0.3427 0.0435 0.0060 -0.0096 2 LYS B NZ 3131 N N . PRO B 3 ? 0.1527 0.1660 0.1491 0.0027 -0.0003 0.0000 3 PRO B N 3132 C CA . PRO B 3 ? 0.1539 0.1656 0.1584 0.0100 0.0041 0.0006 3 PRO B CA 3133 C C . PRO B 3 ? 0.1552 0.1778 0.1636 0.0158 0.0032 -0.0030 3 PRO B C 3134 O O . PRO B 3 ? 0.1384 0.1928 0.1872 0.0215 0.0004 -0.0080 3 PRO B O 3135 C CB . PRO B 3 ? 0.1477 0.1682 0.1619 0.0146 0.0034 0.0035 3 PRO B CB 3136 C CG . PRO B 3 ? 0.1557 0.1766 0.1472 0.0105 0.0077 -0.0057 3 PRO B CG 3137 C CD . PRO B 3 ? 0.1552 0.1657 0.1537 0.0024 0.0070 0.0002 3 PRO B CD 3138 N N . GLY B 4 ? 0.1462 0.1715 0.1663 0.0206 0.0069 -0.0054 4 GLY B N 3139 C CA . GLY B 4 ? 0.1579 0.1682 0.1637 0.0115 0.0107 -0.0035 4 GLY B CA 3140 C C . GLY B 4 ? 0.1639 0.1668 0.1641 0.0194 0.0013 0.0042 4 GLY B C 3141 O O . GLY B 4 ? 0.1671 0.1789 0.1617 0.0193 0.0058 0.0017 4 GLY B O 3142 N N . GLU B 5 ? 0.1677 0.1716 0.1668 0.0170 0.0028 0.0026 5 GLU B N 3143 C CA . GLU B 5 ? 0.1862 0.1796 0.1879 0.0149 0.0039 0.0020 5 GLU B CA 3144 C C . GLU B 5 ? 0.2037 0.2067 0.2067 0.0191 0.0038 0.0065 5 GLU B C 3145 O O . GLU B 5 ? 0.2273 0.2347 0.2558 0.0220 -0.0027 0.0333 5 GLU B O 3146 C CB . GLU B 5 ? 0.2052 0.1757 0.1982 0.0128 0.0028 0.0043 5 GLU B CB 3147 C CG . GLU B 5 ? 0.2109 0.2101 0.2083 0.0054 -0.0027 0.0063 5 GLU B CG 3148 C CD . GLU B 5 ? 0.2418 0.2109 0.2426 0.0163 -0.0114 0.0160 5 GLU B CD 3149 O OE1 . GLU B 5 ? 0.2305 0.2457 0.3033 -0.0001 -0.0387 0.0325 5 GLU B OE1 3150 O OE2 . GLU B 5 ? 0.2404 0.1960 0.2449 0.0166 -0.0415 0.0047 5 GLU B OE2 3151 N N . THR B 6 ? 0.2118 0.1922 0.2152 0.0171 -0.0075 -0.0082 6 THR B N 3152 C CA . THR B 6 ? 0.2099 0.1982 0.2169 0.0178 -0.0019 -0.0125 6 THR B CA 3153 C C . THR B 6 ? 0.2060 0.2062 0.2235 0.0147 -0.0053 -0.0079 6 THR B C 3154 O O . THR B 6 ? 0.1848 0.1787 0.2067 0.0161 -0.0246 -0.0059 6 THR B O 3155 C CB . THR B 6 ? 0.2190 0.2062 0.2175 0.0143 -0.0043 -0.0182 6 THR B CB 3156 O OG1 . THR B 6 ? 0.2339 0.2369 0.2485 0.0492 -0.0216 -0.0422 6 THR B OG1 3157 C CG2 . THR B 6 ? 0.2303 0.2061 0.2491 0.0218 -0.0127 -0.0215 6 THR B CG2 3158 N N . LYS B 7 ? 0.2311 0.2063 0.2400 0.0130 0.0019 -0.0029 7 LYS B N 3159 C CA . LYS B 7 ? 0.2376 0.2268 0.2422 0.0124 -0.0016 -0.0039 7 LYS B CA 3160 C C . LYS B 7 ? 0.2220 0.2123 0.2163 0.0182 -0.0076 -0.0083 7 LYS B C 3161 O O . LYS B 7 ? 0.2192 0.2252 0.2537 0.0350 -0.0153 -0.0393 7 LYS B O 3162 C CB . LYS B 7 ? 0.2558 0.2512 0.2744 0.0119 0.0099 -0.0011 7 LYS B CB 3163 C CG . LYS B 7 ? 0.3042 0.2887 0.2981 0.0055 0.0004 0.0032 7 LYS B CG 3164 C CD . LYS B 7 ? 0.3263 0.3176 0.3210 0.0000 0.0100 0.0073 7 LYS B CD 3165 C CE . LYS B 7 ? 0.3664 0.3831 0.3915 0.0072 -0.0008 0.0051 7 LYS B CE 3166 N NZ . LYS B 7 ? 0.4139 0.4114 0.4004 0.0065 0.0030 -0.0093 7 LYS B NZ 3167 N N . GLU B 8 ? 0.1949 0.1735 0.1797 0.0132 -0.0084 0.0006 8 GLU B N 3168 C CA . GLU B 8 ? 0.1838 0.1770 0.1719 0.0105 -0.0033 0.0029 8 GLU B CA 3169 C C . GLU B 8 ? 0.1668 0.1595 0.1646 0.0102 -0.0036 0.0027 8 GLU B C 3170 O O . GLU B 8 ? 0.1966 0.1932 0.1823 0.0178 0.0005 0.0003 8 GLU B O 3171 C CB . GLU B 8 ? 0.1728 0.1688 0.1589 0.0104 -0.0079 0.0031 8 GLU B CB 3172 C CG . GLU B 8 ? 0.1615 0.1668 0.1500 0.0104 -0.0019 0.0015 8 GLU B CG 3173 C CD . GLU B 8 ? 0.1262 0.1688 0.1572 -0.0011 -0.0001 -0.0016 8 GLU B CD 3174 O OE1 . GLU B 8 ? 0.1568 0.1535 0.1264 -0.0038 0.0057 0.0025 8 GLU B OE1 3175 O OE2 . GLU B 8 ? 0.1467 0.1652 0.1574 -0.0035 -0.0070 0.0209 8 GLU B OE2 3176 N N . VAL B 9 ? 0.1714 0.1368 0.1466 0.0074 -0.0018 0.0003 9 VAL B N 3177 C CA . VAL B 9 ? 0.1704 0.1449 0.1521 0.0067 0.0013 0.0007 9 VAL B CA 3178 C C . VAL B 9 ? 0.1613 0.1481 0.1371 0.0100 0.0016 0.0045 9 VAL B C 3179 O O . VAL B 9 ? 0.1631 0.1170 0.1402 0.0130 -0.0066 -0.0065 9 VAL B O 3180 C CB . VAL B 9 ? 0.1757 0.1551 0.1616 0.0082 -0.0019 0.0021 9 VAL B CB 3181 C CG1 . VAL B 9 ? 0.2010 0.1528 0.2019 -0.0118 -0.0059 0.0087 9 VAL B CG1 3182 C CG2 . VAL B 9 ? 0.1900 0.1524 0.1881 0.0188 0.0023 -0.0086 9 VAL B CG2 3183 N N . HIS B 10 ? 0.1546 0.1254 0.1388 0.0103 -0.0015 0.0042 10 HIS B N 3184 C CA . HIS B 10 ? 0.1436 0.1313 0.1378 0.0050 -0.0020 0.0074 10 HIS B CA 3185 C C . HIS B 10 ? 0.1346 0.1306 0.1315 0.0002 0.0040 0.0031 10 HIS B C 3186 O O . HIS B 10 ? 0.1566 0.1367 0.1273 0.0077 0.0058 0.0188 10 HIS B O 3187 C CB . HIS B 10 ? 0.1314 0.1320 0.1332 0.0111 -0.0008 0.0036 10 HIS B CB 3188 C CG . HIS B 10 ? 0.1362 0.1364 0.1164 -0.0101 -0.0022 0.0012 10 HIS B CG 3189 N ND1 . HIS B 10 ? 0.1592 0.1445 0.1599 0.0034 -0.0037 0.0093 10 HIS B ND1 3190 C CD2 . HIS B 10 ? 0.1327 0.1259 0.1457 -0.0033 0.0091 0.0057 10 HIS B CD2 3191 C CE1 . HIS B 10 ? 0.1126 0.1601 0.1250 0.0080 -0.0053 0.0001 10 HIS B CE1 3192 N NE2 . HIS B 10 ? 0.1386 0.1475 0.1385 -0.0076 0.0031 -0.0138 10 HIS B NE2 3193 N N . PRO B 11 ? 0.1444 0.1276 0.1240 0.0037 0.0090 0.0012 11 PRO B N 3194 C CA . PRO B 11 ? 0.1422 0.1236 0.1306 -0.0077 0.0009 0.0000 11 PRO B CA 3195 C C . PRO B 11 ? 0.1476 0.1311 0.1428 -0.0092 0.0068 0.0000 11 PRO B C 3196 O O . PRO B 11 ? 0.1536 0.1264 0.1376 -0.0230 0.0144 -0.0077 11 PRO B O 3197 C CB . PRO B 11 ? 0.1418 0.1353 0.1409 -0.0056 -0.0056 0.0008 11 PRO B CB 3198 C CG . PRO B 11 ? 0.1512 0.1283 0.1350 0.0111 -0.0056 -0.0045 11 PRO B CG 3199 C CD . PRO B 11 ? 0.1393 0.1236 0.1171 0.0077 0.0128 -0.0159 11 PRO B CD 3200 N N . GLN B 12 ? 0.1508 0.1336 0.1567 -0.0173 0.0125 -0.0027 12 GLN B N 3201 C CA . GLN B 12 ? 0.1540 0.1436 0.1443 -0.0114 0.0063 0.0033 12 GLN B CA 3202 C C . GLN B 12 ? 0.1441 0.1389 0.1386 -0.0157 0.0042 -0.0009 12 GLN B C 3203 O O . GLN B 12 ? 0.1512 0.1596 0.1380 -0.0024 -0.0124 -0.0099 12 GLN B O 3204 C CB . GLN B 12 ? 0.1551 0.1512 0.1579 -0.0201 0.0186 0.0058 12 GLN B CB 3205 C CG . GLN B 12 ? 0.1848 0.1749 0.1603 -0.0177 0.0156 0.0100 12 GLN B CG 3206 C CD . GLN B 12 ? 0.2189 0.1954 0.1945 -0.0049 0.0000 0.0181 12 GLN B CD 3207 O OE1 . GLN B 12 ? 0.3059 0.2684 0.3087 0.0124 0.0042 0.0417 12 GLN B OE1 3208 N NE2 . GLN B 12 ? 0.2772 0.2997 0.2750 -0.0241 0.0143 0.0069 12 GLN B NE2 3209 N N . LEU B 13 ? 0.1366 0.1356 0.1292 -0.0020 0.0019 -0.0004 13 LEU B N 3210 C CA . LEU B 13 ? 0.1292 0.1416 0.1290 -0.0074 0.0021 -0.0018 13 LEU B CA 3211 C C . LEU B 13 ? 0.1200 0.1403 0.1306 -0.0014 0.0051 -0.0112 13 LEU B C 3212 O O . LEU B 13 ? 0.1239 0.1563 0.1287 0.0031 0.0170 -0.0129 13 LEU B O 3213 C CB . LEU B 13 ? 0.1057 0.1366 0.1210 -0.0084 0.0097 -0.0016 13 LEU B CB 3214 C CG . LEU B 13 ? 0.1400 0.1414 0.1216 -0.0020 -0.0027 0.0022 13 LEU B CG 3215 C CD1 . LEU B 13 ? 0.1386 0.1487 0.1422 -0.0169 0.0115 0.0013 13 LEU B CD1 3216 C CD2 . LEU B 13 ? 0.1577 0.1424 0.1204 -0.0127 -0.0161 -0.0019 13 LEU B CD2 3217 N N . THR B 14 ? 0.1255 0.1312 0.1270 -0.0048 0.0050 -0.0081 14 THR B N 3218 C CA . THR B 14 ? 0.1242 0.1344 0.1240 -0.0059 0.0041 -0.0005 14 THR B CA 3219 C C . THR B 14 ? 0.1243 0.1320 0.1212 -0.0072 -0.0001 -0.0012 14 THR B C 3220 O O . THR B 14 ? 0.1344 0.1344 0.1334 -0.0201 -0.0050 0.0013 14 THR B O 3221 C CB . THR B 14 ? 0.1283 0.1376 0.1221 -0.0043 0.0027 -0.0055 14 THR B CB 3222 O OG1 . THR B 14 ? 0.1607 0.1388 0.1604 -0.0120 0.0223 0.0044 14 THR B OG1 3223 C CG2 . THR B 14 ? 0.1464 0.1267 0.1358 -0.0120 0.0121 0.0061 14 THR B CG2 3224 N N . THR B 15 ? 0.1180 0.1304 0.1258 -0.0015 -0.0030 -0.0034 15 THR B N 3225 C CA . THR B 15 ? 0.1112 0.1298 0.1269 -0.0040 0.0008 -0.0023 15 THR B CA 3226 C C . THR B 15 ? 0.1289 0.1349 0.1323 -0.0058 0.0075 -0.0016 15 THR B C 3227 O O . THR B 15 ? 0.1426 0.1422 0.1358 -0.0151 0.0114 0.0025 15 THR B O 3228 C CB . THR B 15 ? 0.1245 0.1383 0.1343 -0.0088 0.0022 -0.0022 15 THR B CB 3229 O OG1 . THR B 15 ? 0.1293 0.1452 0.1363 -0.0059 -0.0037 -0.0054 15 THR B OG1 3230 C CG2 . THR B 15 ? 0.1323 0.1474 0.1437 -0.0103 0.0032 -0.0030 15 THR B CG2 3231 N N . PHE B 16 ? 0.1432 0.1260 0.1318 -0.0159 0.0127 -0.0014 16 PHE B N 3232 C CA . PHE B 16 ? 0.1277 0.1406 0.1289 -0.0087 0.0132 0.0027 16 PHE B CA 3233 C C . PHE B 16 ? 0.1455 0.1334 0.1226 -0.0047 0.0142 0.0030 16 PHE B C 3234 O O . PHE B 16 ? 0.1326 0.1332 0.1215 -0.0205 0.0162 0.0000 16 PHE B O 3235 C CB . PHE B 16 ? 0.1320 0.1429 0.1383 -0.0021 0.0084 -0.0010 16 PHE B CB 3236 C CG . PHE B 16 ? 0.1275 0.1317 0.1205 -0.0099 0.0176 0.0104 16 PHE B CG 3237 C CD1 . PHE B 16 ? 0.1393 0.1416 0.1258 -0.0027 0.0207 0.0121 16 PHE B CD1 3238 C CD2 . PHE B 16 ? 0.1421 0.1395 0.1242 -0.0048 0.0248 -0.0071 16 PHE B CD2 3239 C CE1 . PHE B 16 ? 0.1210 0.1465 0.1293 -0.0138 0.0261 0.0230 16 PHE B CE1 3240 C CE2 . PHE B 16 ? 0.1445 0.1462 0.1335 -0.0052 0.0125 0.0070 16 PHE B CE2 3241 C CZ . PHE B 16 ? 0.1532 0.1404 0.1530 -0.0196 0.0087 0.0020 16 PHE B CZ 3242 N N . ARG B 17 ? 0.1564 0.1523 0.1227 -0.0134 0.0113 -0.0041 17 ARG B N 3243 C CA . ARG B 17 ? 0.1484 0.1400 0.1381 -0.0034 0.0118 -0.0044 17 ARG B CA 3244 C C . ARG B 17 ? 0.1443 0.1448 0.1367 -0.0118 0.0173 -0.0005 17 ARG B C 3245 O O . ARG B 17 ? 0.1593 0.1521 0.1507 -0.0257 0.0271 0.0032 17 ARG B O 3246 C CB . ARG B 17 ? 0.1484 0.1433 0.1436 -0.0013 0.0139 -0.0028 17 ARG B CB 3247 C CG . ARG B 17 ? 0.1469 0.1589 0.1469 0.0122 0.0134 -0.0041 17 ARG B CG 3248 C CD . ARG B 17 ? 0.1630 0.1412 0.1560 -0.0049 -0.0014 -0.0099 17 ARG B CD 3249 N NE . ARG B 17 ? 0.1480 0.1591 0.1606 -0.0048 0.0102 -0.0238 17 ARG B NE 3250 C CZ . ARG B 17 ? 0.1391 0.1648 0.1365 0.0004 0.0004 -0.0132 17 ARG B CZ 3251 N NH1 . ARG B 17 ? 0.1087 0.1667 0.1354 -0.0052 0.0190 -0.0140 17 ARG B NH1 3252 N NH2 . ARG B 17 ? 0.1260 0.1715 0.1622 -0.0082 0.0039 -0.0186 17 ARG B NH2 3253 N N . CYS B 18 ? 0.1425 0.1514 0.1486 -0.0091 0.0229 0.0036 18 CYS B N 3254 C CA . CYS B 18 ? 0.1534 0.1517 0.1577 -0.0030 0.0116 0.0007 18 CYS B CA 3255 C C . CYS B 18 ? 0.1553 0.1542 0.1495 -0.0114 0.0143 -0.0026 18 CYS B C 3256 O O . CYS B 18 ? 0.1563 0.1487 0.1469 -0.0033 0.0217 -0.0036 18 CYS B O 3257 C CB . CYS B 18 ? 0.1603 0.1582 0.1555 0.0035 0.0113 -0.0055 18 CYS B CB 3258 S SG . CYS B 18 ? 0.1799 0.1815 0.1514 -0.0104 0.0191 -0.0170 18 CYS B SG 3259 N N . THR B 19 ? 0.1705 0.1683 0.1599 -0.0004 0.0157 -0.0051 19 THR B N 3260 C CA . THR B 19 ? 0.2051 0.1921 0.1766 -0.0027 0.0078 -0.0080 19 THR B CA 3261 C C . THR B 19 ? 0.2137 0.2097 0.1864 -0.0029 0.0158 -0.0070 19 THR B C 3262 O O . THR B 19 ? 0.1860 0.2189 0.1725 -0.0053 0.0369 -0.0130 19 THR B O 3263 C CB . THR B 19 ? 0.2114 0.1985 0.1792 -0.0040 0.0072 -0.0080 19 THR B CB 3264 O OG1 . THR B 19 ? 0.2424 0.2165 0.1728 -0.0058 0.0270 -0.0069 19 THR B OG1 3265 C CG2 . THR B 19 ? 0.2204 0.2020 0.1755 -0.0021 0.0076 -0.0138 19 THR B CG2 3266 N N . LYS B 20 ? 0.2408 0.2301 0.2274 0.0009 0.0115 -0.0122 20 LYS B N 3267 C CA . LYS B 20 ? 0.2578 0.2556 0.2526 0.0039 0.0138 -0.0096 20 LYS B CA 3268 C C . LYS B 20 ? 0.2626 0.2688 0.2647 0.0013 0.0197 -0.0139 20 LYS B C 3269 O O . LYS B 20 ? 0.2690 0.2940 0.2605 0.0020 0.0321 -0.0386 20 LYS B O 3270 C CB . LYS B 20 ? 0.2798 0.2689 0.2813 0.0084 0.0140 -0.0121 20 LYS B CB 3271 C CG . LYS B 20 ? 0.3275 0.3294 0.3269 0.0037 0.0052 0.0011 20 LYS B CG 3272 C CD . LYS B 20 ? 0.3677 0.3587 0.3809 0.0082 0.0033 0.0018 20 LYS B CD 3273 C CE . LYS B 20 ? 0.4016 0.3841 0.3937 0.0034 -0.0006 0.0000 20 LYS B CE 3274 N NZ . LYS B 20 ? 0.3897 0.3842 0.4145 0.0222 0.0035 0.0016 20 LYS B NZ 3275 N N . ARG B 21 ? 0.2732 0.2820 0.2705 -0.0030 0.0223 -0.0045 21 ARG B N 3276 C CA . ARG B 21 ? 0.2869 0.2896 0.2816 -0.0038 0.0181 -0.0007 21 ARG B CA 3277 C C . ARG B 21 ? 0.2742 0.2838 0.2731 -0.0047 0.0237 -0.0036 21 ARG B C 3278 O O . ARG B 21 ? 0.2806 0.3013 0.2696 -0.0157 0.0293 -0.0064 21 ARG B O 3279 C CB . ARG B 21 ? 0.2877 0.2918 0.2757 -0.0089 0.0229 0.0037 21 ARG B CB 3280 C CG . ARG B 21 ? 0.3276 0.3272 0.3117 -0.0044 0.0183 0.0098 21 ARG B CG 3281 C CD . ARG B 21 ? 0.4021 0.4003 0.3546 0.0053 0.0094 -0.0022 21 ARG B CD 3282 N NE . ARG B 21 ? 0.4605 0.4751 0.4501 -0.0107 0.0028 -0.0021 21 ARG B NE 3283 C CZ . ARG B 21 ? 0.5086 0.5019 0.5057 -0.0054 0.0038 -0.0082 21 ARG B CZ 3284 N NH1 . ARG B 21 ? 0.5245 0.5420 0.5320 0.0002 0.0046 -0.0020 21 ARG B NH1 3285 N NH2 . ARG B 21 ? 0.5068 0.5039 0.5075 -0.0141 0.0048 -0.0140 21 ARG B NH2 3286 N N . GLY B 22 ? 0.2614 0.2702 0.2510 -0.0055 0.0318 -0.0025 22 GLY B N 3287 C CA . GLY B 22 ? 0.2486 0.2590 0.2303 -0.0075 0.0182 0.0021 22 GLY B CA 3288 C C . GLY B 22 ? 0.2338 0.2468 0.2226 -0.0024 0.0126 0.0001 22 GLY B C 3289 O O . GLY B 22 ? 0.2515 0.2592 0.2215 -0.0159 0.0255 0.0057 22 GLY B O 3290 N N . GLY B 23 ? 0.2163 0.2371 0.2053 -0.0045 0.0187 -0.0038 23 GLY B N 3291 C CA . GLY B 23 ? 0.1916 0.2211 0.1997 0.0000 0.0158 -0.0070 23 GLY B CA 3292 C C . GLY B 23 ? 0.1723 0.2095 0.1814 -0.0038 0.0174 -0.0025 23 GLY B C 3293 O O . GLY B 23 ? 0.1814 0.2097 0.1603 -0.0113 0.0300 -0.0009 23 GLY B O 3294 N N . CYS B 24 ? 0.1655 0.1973 0.1930 -0.0039 0.0193 -0.0006 24 CYS B N 3295 C CA . CYS B 24 ? 0.1608 0.1898 0.1824 -0.0027 0.0141 -0.0034 24 CYS B CA 3296 C C . CYS B 24 ? 0.1680 0.1832 0.1784 -0.0082 0.0143 -0.0046 24 CYS B C 3297 O O . CYS B 24 ? 0.1833 0.1829 0.2265 -0.0148 0.0083 -0.0043 24 CYS B O 3298 C CB . CYS B 24 ? 0.1606 0.2041 0.1878 -0.0039 0.0160 -0.0022 24 CYS B CB 3299 S SG . CYS B 24 ? 0.1900 0.2140 0.1878 0.0058 0.0080 0.0026 24 CYS B SG 3300 N N . LYS B 25 ? 0.1685 0.1675 0.1660 -0.0009 0.0175 -0.0079 25 LYS B N 3301 C CA . LYS B 25 ? 0.1629 0.1785 0.1697 -0.0020 0.0158 0.0003 25 LYS B CA 3302 C C . LYS B 25 ? 0.1595 0.1704 0.1539 -0.0051 0.0190 -0.0023 25 LYS B C 3303 O O . LYS B 25 ? 0.1784 0.1641 0.1549 -0.0211 0.0192 0.0104 25 LYS B O 3304 C CB . LYS B 25 ? 0.1847 0.1805 0.1815 -0.0023 0.0108 0.0072 25 LYS B CB 3305 C CG . LYS B 25 ? 0.2000 0.1999 0.2073 0.0158 0.0055 -0.0084 25 LYS B CG 3306 C CD . LYS B 25 ? 0.2498 0.2344 0.2149 0.0051 0.0089 -0.0054 25 LYS B CD 3307 C CE . LYS B 25 ? 0.2844 0.2936 0.2679 -0.0015 0.0213 -0.0006 25 LYS B CE 3308 N NZ . LYS B 25 ? 0.3759 0.3242 0.3458 -0.0162 -0.0014 0.0023 25 LYS B NZ 3309 N N . PRO B 26 ? 0.1523 0.1705 0.1542 -0.0115 0.0271 0.0092 26 PRO B N 3310 C CA . PRO B 26 ? 0.1540 0.1650 0.1467 -0.0002 0.0094 0.0001 26 PRO B CA 3311 C C . PRO B 26 ? 0.1530 0.1788 0.1519 -0.0001 0.0079 0.0027 26 PRO B C 3312 O O . PRO B 26 ? 0.1725 0.2156 0.1552 -0.0044 0.0164 0.0043 26 PRO B O 3313 C CB . PRO B 26 ? 0.1582 0.1620 0.1560 -0.0034 0.0054 0.0003 26 PRO B CB 3314 C CG . PRO B 26 ? 0.1806 0.1728 0.1834 -0.0148 0.0172 0.0024 26 PRO B CG 3315 C CD . PRO B 26 ? 0.1434 0.1604 0.1643 -0.0139 0.0244 0.0115 26 PRO B CD 3316 N N . ALA B 27 ? 0.1553 0.1778 0.1456 -0.0030 0.0045 -0.0005 27 ALA B N 3317 C CA . ALA B 27 ? 0.1567 0.1629 0.1510 0.0004 0.0020 0.0031 27 ALA B CA 3318 C C . ALA B 27 ? 0.1533 0.1578 0.1440 -0.0045 0.0032 0.0046 27 ALA B C 3319 O O . ALA B 27 ? 0.1503 0.1537 0.1309 0.0020 0.0016 0.0063 27 ALA B O 3320 C CB . ALA B 27 ? 0.1636 0.1657 0.1652 -0.0004 0.0010 -0.0043 27 ALA B CB 3321 N N . THR B 28 ? 0.1503 0.1618 0.1392 -0.0020 0.0026 0.0091 28 THR B N 3322 C CA . THR B 28 ? 0.1515 0.1502 0.1481 -0.0038 0.0023 0.0126 28 THR B CA 3323 C C . THR B 28 ? 0.1508 0.1545 0.1365 -0.0060 0.0065 0.0051 28 THR B C 3324 O O . THR B 28 ? 0.1418 0.1895 0.1468 -0.0140 0.0094 0.0117 28 THR B O 3325 C CB . THR B 28 ? 0.1706 0.1494 0.1576 0.0002 0.0151 0.0184 28 THR B CB 3326 O OG1 . THR B 28 ? 0.2094 0.1855 0.2317 -0.0213 0.0337 0.0313 28 THR B OG1 3327 C CG2 . THR B 28 ? 0.1956 0.1700 0.1821 0.0058 0.0137 0.0164 28 THR B CG2 3328 N N . ASN B 29 ? 0.1260 0.1469 0.1239 0.0011 0.0021 0.0067 29 ASN B N 3329 C CA . ASN B 29 ? 0.1295 0.1326 0.1223 -0.0098 0.0002 0.0043 29 ASN B CA 3330 C C . ASN B 29 ? 0.1275 0.1153 0.1220 -0.0130 0.0009 0.0012 29 ASN B C 3331 O O . ASN B 29 ? 0.1429 0.1186 0.1254 -0.0109 -0.0033 0.0076 29 ASN B O 3332 C CB . ASN B 29 ? 0.1248 0.1197 0.1119 -0.0078 0.0003 0.0009 29 ASN B CB 3333 C CG . ASN B 29 ? 0.1265 0.1314 0.1211 0.0036 0.0029 0.0000 29 ASN B CG 3334 O OD1 . ASN B 29 ? 0.1299 0.1671 0.1361 0.0149 0.0045 0.0046 29 ASN B OD1 3335 N ND2 . ASN B 29 ? 0.1201 0.1456 0.1357 -0.0036 0.0150 0.0076 29 ASN B ND2 3336 N N . PHE B 30 ? 0.1200 0.1131 0.1213 -0.0062 0.0091 0.0059 30 PHE B N 3337 C CA . PHE B 30 ? 0.1332 0.1159 0.1228 -0.0098 0.0038 0.0019 30 PHE B CA 3338 C C . PHE B 30 ? 0.1309 0.1158 0.1136 -0.0039 0.0041 0.0001 30 PHE B C 3339 O O . PHE B 30 ? 0.1495 0.1086 0.1199 -0.0027 -0.0035 -0.0065 30 PHE B O 3340 C CB . PHE B 30 ? 0.1445 0.1485 0.1315 -0.0022 0.0046 0.0039 30 PHE B CB 3341 C CG . PHE B 30 ? 0.1434 0.1437 0.1392 -0.0078 -0.0026 0.0023 30 PHE B CG 3342 C CD1 . PHE B 30 ? 0.1758 0.1330 0.1559 -0.0018 -0.0117 0.0105 30 PHE B CD1 3343 C CD2 . PHE B 30 ? 0.1365 0.1429 0.1401 -0.0073 -0.0102 0.0000 30 PHE B CD2 3344 C CE1 . PHE B 30 ? 0.1723 0.1347 0.1657 -0.0131 -0.0015 0.0063 30 PHE B CE1 3345 C CE2 . PHE B 30 ? 0.1800 0.1613 0.1396 -0.0102 -0.0063 0.0037 30 PHE B CE2 3346 C CZ . PHE B 30 ? 0.1758 0.1421 0.1630 0.0026 -0.0031 0.0172 30 PHE B CZ 3347 N N . ILE B 31 ? 0.1279 0.1122 0.1065 -0.0175 0.0041 0.0087 31 ILE B N 3348 C CA . ILE B 31 ? 0.1202 0.1087 0.1135 -0.0004 0.0041 0.0008 31 ILE B CA 3349 C C . ILE B 31 ? 0.1239 0.1093 0.1028 0.0002 0.0078 0.0057 31 ILE B C 3350 O O . ILE B 31 ? 0.1383 0.1030 0.1361 -0.0059 -0.0004 0.0046 31 ILE B O 3351 C CB . ILE B 31 ? 0.1143 0.1157 0.1121 -0.0020 0.0073 0.0011 31 ILE B CB 3352 C CG1 . ILE B 31 ? 0.1305 0.1439 0.1324 -0.0018 -0.0031 -0.0094 31 ILE B CG1 3353 C CG2 . ILE B 31 ? 0.1429 0.1213 0.1153 -0.0030 -0.0018 0.0022 31 ILE B CG2 3354 C CD1 . ILE B 31 ? 0.1293 0.1443 0.1550 0.0154 -0.0053 -0.0001 31 ILE B CD1 3355 N N . VAL B 32 ? 0.1050 0.0966 0.1076 0.0028 0.0008 -0.0025 32 VAL B N 3356 C CA . VAL B 32 ? 0.1104 0.1102 0.1069 0.0009 0.0025 -0.0057 32 VAL B CA 3357 C C . VAL B 32 ? 0.1055 0.1085 0.1001 0.0063 0.0013 -0.0107 32 VAL B C 3358 O O . VAL B 32 ? 0.1184 0.1151 0.1067 0.0082 -0.0021 -0.0104 32 VAL B O 3359 C CB . VAL B 32 ? 0.1057 0.1143 0.0888 0.0012 -0.0057 0.0002 32 VAL B CB 3360 C CG1 . VAL B 32 ? 0.1262 0.1349 0.0791 0.0010 -0.0025 -0.0040 32 VAL B CG1 3361 C CG2 . VAL B 32 ? 0.1016 0.1103 0.1162 0.0016 -0.0027 0.0013 32 VAL B CG2 3362 N N . LEU B 33 ? 0.1202 0.1101 0.1019 0.0063 0.0151 -0.0060 33 LEU B N 3363 C CA . LEU B 33 ? 0.1081 0.1067 0.1068 -0.0013 -0.0001 -0.0028 33 LEU B CA 3364 C C . LEU B 33 ? 0.1024 0.1101 0.0995 -0.0025 -0.0023 0.0000 33 LEU B C 3365 O O . LEU B 33 ? 0.1147 0.1216 0.1094 0.0211 -0.0045 0.0041 33 LEU B O 3366 C CB A LEU B 33 ? 0.1193 0.1181 0.1097 0.0065 0.0052 -0.0013 33 LEU B CB 3367 C CB B LEU B 33 ? 0.1144 0.1145 0.1038 0.0063 0.0046 -0.0009 33 LEU B CB 3368 C CG A LEU B 33 ? 0.1368 0.1187 0.1277 0.0036 -0.0030 -0.0074 33 LEU B CG 3369 C CG B LEU B 33 ? 0.1156 0.0966 0.0973 0.0044 -0.0017 -0.0023 33 LEU B CG 3370 C CD1 A LEU B 33 ? 0.1512 0.1230 0.1542 -0.0011 -0.0028 -0.0052 33 LEU B CD1 3371 C CD1 B LEU B 33 ? 0.1236 0.1002 0.0964 0.0044 0.0026 -0.0118 33 LEU B CD1 3372 C CD2 A LEU B 33 ? 0.1529 0.1183 0.1228 -0.0031 0.0040 -0.0056 33 LEU B CD2 3373 C CD2 B LEU B 33 ? 0.1044 0.1013 0.0876 -0.0091 -0.0012 -0.0085 33 LEU B CD2 3374 N N . ASP B 34 ? 0.0952 0.1185 0.0991 0.0021 -0.0021 0.0009 34 ASP B N 3375 C CA . ASP B 34 ? 0.1008 0.1128 0.0946 -0.0010 0.0034 -0.0025 34 ASP B CA 3376 C C . ASP B 34 ? 0.1029 0.1136 0.0961 0.0038 -0.0016 -0.0051 34 ASP B C 3377 O O . ASP B 34 ? 0.1044 0.1101 0.1122 -0.0026 0.0045 -0.0029 34 ASP B O 3378 C CB . ASP B 34 ? 0.0971 0.1118 0.0964 0.0035 0.0102 -0.0004 34 ASP B CB 3379 C CG . ASP B 34 ? 0.1162 0.1109 0.1131 0.0031 -0.0008 0.0107 34 ASP B CG 3380 O OD1 . ASP B 34 ? 0.1124 0.1307 0.1252 0.0002 -0.0030 0.0011 34 ASP B OD1 3381 O OD2 . ASP B 34 ? 0.1337 0.1229 0.1141 -0.0026 0.0077 0.0028 34 ASP B OD2 3382 N N . SER B 35 ? 0.1077 0.1093 0.1062 0.0041 -0.0009 -0.0047 35 SER B N 3383 C CA . SER B 35 ? 0.1092 0.1282 0.1175 0.0012 0.0054 -0.0016 35 SER B CA 3384 C C . SER B 35 ? 0.1088 0.1143 0.1190 0.0015 -0.0003 -0.0033 35 SER B C 3385 O O . SER B 35 ? 0.1256 0.1304 0.1126 0.0054 0.0073 -0.0120 35 SER B O 3386 C CB . SER B 35 ? 0.1186 0.1340 0.1261 0.0087 -0.0050 -0.0041 35 SER B CB 3387 O OG . SER B 35 ? 0.1315 0.1464 0.1464 -0.0085 -0.0129 0.0014 35 SER B OG 3388 N N . LEU B 36 ? 0.1172 0.1193 0.1074 0.0042 0.0029 -0.0010 36 LEU B N 3389 C CA . LEU B 36 ? 0.1275 0.1371 0.1191 0.0021 0.0045 -0.0029 36 LEU B CA 3390 C C . LEU B 36 ? 0.1192 0.1381 0.1176 -0.0013 0.0027 -0.0059 36 LEU B C 3391 O O . LEU B 36 ? 0.1227 0.1663 0.1182 0.0054 0.0059 0.0027 36 LEU B O 3392 C CB . LEU B 36 ? 0.1260 0.1380 0.1217 0.0050 0.0044 0.0003 36 LEU B CB 3393 C CG . LEU B 36 ? 0.1448 0.1483 0.1403 0.0070 0.0026 -0.0050 36 LEU B CG 3394 C CD1 . LEU B 36 ? 0.1609 0.1652 0.1618 -0.0125 0.0074 -0.0100 36 LEU B CD1 3395 C CD2 . LEU B 36 ? 0.1569 0.1799 0.1821 0.0066 -0.0069 -0.0119 36 LEU B CD2 3396 N N . SER B 37 ? 0.1159 0.1169 0.1140 -0.0047 0.0050 -0.0022 37 SER B N 3397 C CA . SER B 37 ? 0.1212 0.1342 0.1170 0.0028 -0.0043 -0.0039 37 SER B CA 3398 C C . SER B 37 ? 0.1161 0.1358 0.1192 -0.0042 -0.0004 -0.0034 37 SER B C 3399 O O . SER B 37 ? 0.1480 0.1366 0.1432 -0.0077 -0.0036 -0.0027 37 SER B O 3400 C CB . SER B 37 ? 0.1284 0.1330 0.1361 -0.0024 -0.0075 0.0051 37 SER B CB 3401 O OG . SER B 37 ? 0.1585 0.1287 0.1691 0.0130 -0.0118 -0.0033 37 SER B OG 3402 N N . HIS B 38 ? 0.1214 0.1348 0.1205 0.0087 0.0022 -0.0037 38 HIS B N 3403 C CA . HIS B 38 ? 0.1326 0.1406 0.1297 0.0022 0.0004 -0.0036 38 HIS B CA 3404 C C . HIS B 38 ? 0.1438 0.1441 0.1377 0.0041 0.0004 -0.0057 38 HIS B C 3405 O O . HIS B 38 ? 0.1392 0.1341 0.1497 0.0034 0.0208 -0.0093 38 HIS B O 3406 C CB . HIS B 38 ? 0.1402 0.1369 0.1371 0.0029 -0.0095 -0.0016 38 HIS B CB 3407 C CG . HIS B 38 ? 0.1437 0.1242 0.1281 0.0050 -0.0021 -0.0036 38 HIS B CG 3408 N ND1 . HIS B 38 ? 0.1294 0.1407 0.1061 0.0057 0.0035 -0.0040 38 HIS B ND1 3409 C CD2 . HIS B 38 ? 0.1453 0.1107 0.1138 0.0041 0.0125 -0.0091 38 HIS B CD2 3410 C CE1 . HIS B 38 ? 0.1370 0.1274 0.1338 0.0051 0.0143 0.0070 38 HIS B CE1 3411 N NE2 . HIS B 38 ? 0.1249 0.1326 0.1221 0.0171 -0.0009 -0.0093 38 HIS B NE2 3412 N N . PRO B 39 ? 0.1460 0.1429 0.1425 0.0076 0.0000 -0.0046 39 PRO B N 3413 C CA . PRO B 39 ? 0.1543 0.1623 0.1565 0.0076 0.0029 -0.0018 39 PRO B CA 3414 C C . PRO B 39 ? 0.1618 0.1672 0.1642 0.0090 -0.0018 -0.0047 39 PRO B C 3415 O O . PRO B 39 ? 0.1395 0.1848 0.1668 0.0059 -0.0042 0.0051 39 PRO B O 3416 C CB . PRO B 39 ? 0.1718 0.1748 0.1623 0.0109 -0.0087 -0.0154 39 PRO B CB 3417 C CG . PRO B 39 ? 0.1680 0.1502 0.1560 0.0000 -0.0071 -0.0129 39 PRO B CG 3418 C CD . PRO B 39 ? 0.1541 0.1543 0.1628 0.0118 -0.0045 -0.0074 39 PRO B CD 3419 N N . ILE B 40 ? 0.1672 0.1856 0.1684 0.0154 0.0036 0.0057 40 ILE B N 3420 C CA . ILE B 40 ? 0.1779 0.2059 0.1829 0.0090 0.0087 -0.0033 40 ILE B CA 3421 C C . ILE B 40 ? 0.1849 0.2129 0.1823 0.0111 0.0080 -0.0021 40 ILE B C 3422 O O . ILE B 40 ? 0.2032 0.2387 0.1956 0.0334 0.0157 0.0030 40 ILE B O 3423 C CB . ILE B 40 ? 0.1798 0.2181 0.2022 0.0013 -0.0003 -0.0059 40 ILE B CB 3424 C CG1 . ILE B 40 ? 0.1946 0.2302 0.2267 0.0007 -0.0022 -0.0077 40 ILE B CG1 3425 C CG2 . ILE B 40 ? 0.1880 0.2179 0.2146 -0.0012 -0.0028 0.0021 40 ILE B CG2 3426 C CD1 . ILE B 40 ? 0.1894 0.2617 0.2311 -0.0024 0.0031 0.0105 40 ILE B CD1 3427 N N . HIS B 41 ? 0.1724 0.2173 0.1882 0.0125 0.0228 -0.0068 41 HIS B N 3428 C CA . HIS B 41 ? 0.1947 0.2268 0.1951 0.0113 0.0159 -0.0080 41 HIS B CA 3429 C C . HIS B 41 ? 0.1902 0.2274 0.1896 0.0119 0.0130 -0.0042 41 HIS B C 3430 O O . HIS B 41 ? 0.1894 0.2515 0.1915 0.0246 0.0209 -0.0064 41 HIS B O 3431 C CB . HIS B 41 ? 0.2216 0.2520 0.2222 0.0159 0.0254 -0.0096 41 HIS B CB 3432 C CG . HIS B 41 ? 0.2839 0.2766 0.2667 0.0169 0.0092 0.0102 41 HIS B CG 3433 N ND1 . HIS B 41 ? 0.3233 0.3142 0.3277 0.0355 0.0396 0.0227 41 HIS B ND1 3434 C CD2 . HIS B 41 ? 0.3252 0.3149 0.2849 0.0185 0.0109 0.0060 41 HIS B CD2 3435 C CE1 . HIS B 41 ? 0.3467 0.3313 0.3313 0.0298 0.0206 0.0281 41 HIS B CE1 3436 N NE2 . HIS B 41 ? 0.3221 0.3021 0.3301 0.0269 0.0151 0.0136 41 HIS B NE2 3437 N N . ARG B 42 ? 0.1748 0.2368 0.1785 0.0156 0.0098 -0.0016 42 ARG B N 3438 C CA . ARG B 42 ? 0.1816 0.2173 0.1817 0.0047 0.0072 0.0015 42 ARG B CA 3439 C C . ARG B 42 ? 0.1774 0.2085 0.1795 -0.0008 0.0087 0.0007 42 ARG B C 3440 O O . ARG B 42 ? 0.1920 0.2330 0.1741 0.0084 0.0054 0.0075 42 ARG B O 3441 C CB . ARG B 42 ? 0.1770 0.2120 0.1845 0.0063 0.0125 0.0047 42 ARG B CB 3442 C CG . ARG B 42 ? 0.2011 0.2220 0.1832 0.0149 -0.0053 0.0047 42 ARG B CG 3443 C CD . ARG B 42 ? 0.2001 0.2249 0.1922 0.0156 0.0066 0.0010 42 ARG B CD 3444 N NE . ARG B 42 ? 0.2241 0.2223 0.1942 0.0117 0.0092 0.0110 42 ARG B NE 3445 C CZ . ARG B 42 ? 0.2443 0.2268 0.2163 -0.0016 -0.0031 0.0090 42 ARG B CZ 3446 N NH1 . ARG B 42 ? 0.2817 0.2767 0.2514 0.0000 0.0198 0.0105 42 ARG B NH1 3447 N NH2 . ARG B 42 ? 0.2859 0.2406 0.2403 0.0127 -0.0077 0.0078 42 ARG B NH2 3448 N N . ALA B 43 ? 0.1879 0.2159 0.1884 0.0052 0.0033 0.0094 43 ALA B N 3449 C CA . ALA B 43 ? 0.1985 0.2120 0.1970 -0.0001 0.0022 0.0129 43 ALA B CA 3450 C C . ALA B 43 ? 0.2099 0.2156 0.1965 0.0006 -0.0017 0.0127 43 ALA B C 3451 O O . ALA B 43 ? 0.1953 0.2105 0.1953 0.0048 -0.0027 0.0184 43 ALA B O 3452 C CB . ALA B 43 ? 0.1975 0.2149 0.1782 0.0014 0.0043 0.0109 43 ALA B CB 3453 N N . GLU B 44 ? 0.2569 0.2459 0.2402 0.0070 0.0017 0.0147 44 GLU B N 3454 C CA . GLU B 44 ? 0.2599 0.2402 0.2532 0.0098 -0.0054 0.0116 44 GLU B CA 3455 C C . GLU B 44 ? 0.2444 0.2189 0.2443 0.0177 -0.0082 0.0081 44 GLU B C 3456 O O . GLU B 44 ? 0.2357 0.1981 0.2559 0.0441 -0.0214 0.0095 44 GLU B O 3457 C CB . GLU B 44 ? 0.2788 0.2479 0.2694 0.0091 -0.0120 0.0154 44 GLU B CB 3458 C CG . GLU B 44 ? 0.3097 0.2857 0.3009 0.0117 -0.0011 0.0028 44 GLU B CG 3459 C CD . GLU B 44 ? 0.3478 0.2995 0.3388 0.0072 0.0062 0.0083 44 GLU B CD 3460 O OE1 . GLU B 44 ? 0.4176 0.4056 0.3969 0.0039 0.0230 -0.0006 44 GLU B OE1 3461 O OE2 . GLU B 44 ? 0.4209 0.3609 0.4408 0.0204 0.0471 -0.0328 44 GLU B OE2 3462 N N . GLY B 45 ? 0.2368 0.2373 0.2381 0.0133 -0.0063 0.0031 45 GLY B N 3463 C CA . GLY B 45 ? 0.2247 0.2415 0.2313 0.0066 -0.0020 -0.0022 45 GLY B CA 3464 C C . GLY B 45 ? 0.2257 0.2424 0.2379 0.0122 0.0032 0.0024 45 GLY B C 3465 O O . GLY B 45 ? 0.2488 0.2939 0.2567 0.0283 0.0129 0.0013 45 GLY B O 3466 N N . LEU B 46 ? 0.2039 0.2395 0.2346 0.0205 -0.0031 0.0023 46 LEU B N 3467 C CA . LEU B 46 ? 0.2077 0.2290 0.2044 0.0069 -0.0104 0.0016 46 LEU B CA 3468 C C . LEU B 46 ? 0.2175 0.2301 0.2127 0.0093 -0.0135 0.0039 46 LEU B C 3469 O O . LEU B 46 ? 0.2354 0.2560 0.2135 0.0029 -0.0194 0.0101 46 LEU B O 3470 C CB . LEU B 46 ? 0.1985 0.2206 0.1979 0.0127 -0.0027 0.0056 46 LEU B CB 3471 C CG . LEU B 46 ? 0.1989 0.2236 0.1936 0.0075 -0.0071 -0.0005 46 LEU B CG 3472 C CD1 . LEU B 46 ? 0.1883 0.2010 0.1974 -0.0019 -0.0104 0.0102 46 LEU B CD1 3473 C CD2 . LEU B 46 ? 0.2101 0.2275 0.1853 0.0144 -0.0139 0.0065 46 LEU B CD2 3474 N N . GLY B 47 ? 0.2127 0.2304 0.2090 0.0068 -0.0140 0.0096 47 GLY B N 3475 C CA . GLY B 47 ? 0.2153 0.2151 0.2021 0.0012 -0.0109 0.0004 47 GLY B CA 3476 C C . GLY B 47 ? 0.2014 0.2028 0.1968 -0.0063 -0.0054 0.0020 47 GLY B C 3477 O O . GLY B 47 ? 0.2093 0.2187 0.1756 -0.0049 -0.0141 0.0129 47 GLY B O 3478 N N . PRO B 48 ? 0.2067 0.1965 0.1855 -0.0067 -0.0038 0.0044 48 PRO B N 3479 C CA . PRO B 48 ? 0.2105 0.2091 0.1906 -0.0046 -0.0023 -0.0021 48 PRO B CA 3480 C C . PRO B 48 ? 0.2152 0.2152 0.1887 -0.0025 0.0007 -0.0002 48 PRO B C 3481 O O . PRO B 48 ? 0.2628 0.2238 0.2175 -0.0019 -0.0094 -0.0098 48 PRO B O 3482 C CB . PRO B 48 ? 0.2110 0.2198 0.1946 -0.0010 -0.0089 -0.0013 48 PRO B CB 3483 C CG . PRO B 48 ? 0.2221 0.1985 0.2048 0.0001 -0.0116 0.0028 48 PRO B CG 3484 C CD . PRO B 48 ? 0.2007 0.1932 0.2068 -0.0106 -0.0072 -0.0018 48 PRO B CD 3485 N N . GLY B 49 ? 0.2409 0.2386 0.2170 -0.0057 -0.0010 -0.0058 49 GLY B N 3486 C CA . GLY B 49 ? 0.2415 0.2354 0.2251 -0.0034 -0.0002 -0.0046 49 GLY B CA 3487 C C . GLY B 49 ? 0.2598 0.2511 0.2376 -0.0080 -0.0047 -0.0064 49 GLY B C 3488 O O . GLY B 49 ? 0.3182 0.2676 0.2705 -0.0143 -0.0014 -0.0091 49 GLY B O 3489 N N . GLY B 50 ? 0.2567 0.2546 0.2380 -0.0127 0.0075 -0.0102 50 GLY B N 3490 C CA . GLY B 50 ? 0.2330 0.2267 0.2216 -0.0047 0.0033 -0.0103 50 GLY B CA 3491 C C . GLY B 50 ? 0.2016 0.2130 0.2014 -0.0012 0.0014 -0.0056 50 GLY B C 3492 O O . GLY B 50 ? 0.2123 0.2031 0.1835 0.0088 0.0149 -0.0032 50 GLY B O 3493 N N . CYS B 51 ? 0.1925 0.2058 0.1764 0.0045 0.0052 0.0040 51 CYS B N 3494 C CA . CYS B 51 ? 0.1893 0.1971 0.1807 0.0081 0.0056 0.0028 51 CYS B CA 3495 C C . CYS B 51 ? 0.1735 0.1896 0.1731 0.0122 0.0050 -0.0021 51 CYS B C 3496 O O . CYS B 51 ? 0.1638 0.1987 0.1533 0.0191 0.0053 0.0031 51 CYS B O 3497 C CB . CYS B 51 ? 0.1873 0.1893 0.1762 0.0156 0.0011 0.0013 51 CYS B CB 3498 S SG . CYS B 51 ? 0.1845 0.1933 0.1570 0.0255 0.0194 0.0028 51 CYS B SG 3499 N N . GLY B 52 ? 0.1888 0.1986 0.1862 0.0113 0.0144 0.0041 52 GLY B N 3500 C CA . GLY B 52 ? 0.1924 0.2000 0.1887 0.0096 0.0072 0.0016 52 GLY B CA 3501 C C . GLY B 52 ? 0.1892 0.1946 0.1899 0.0091 0.0024 0.0032 52 GLY B C 3502 O O . GLY B 52 ? 0.1985 0.1956 0.1888 0.0178 -0.0104 0.0048 52 GLY B O 3503 N N . ASP B 53 ? 0.2021 0.2018 0.1947 0.0152 -0.0045 -0.0011 53 ASP B N 3504 C CA . ASP B 53 ? 0.2058 0.2134 0.1977 0.0077 -0.0009 0.0007 53 ASP B CA 3505 C C . ASP B 53 ? 0.1934 0.2001 0.1784 0.0057 -0.0032 -0.0015 53 ASP B C 3506 O O . ASP B 53 ? 0.1788 0.2057 0.1810 0.0108 0.0028 0.0021 53 ASP B O 3507 C CB . ASP B 53 ? 0.2295 0.2415 0.2113 0.0066 -0.0028 -0.0085 53 ASP B CB 3508 C CG . ASP B 53 ? 0.2936 0.2798 0.2666 0.0076 -0.0002 -0.0090 53 ASP B CG 3509 O OD1 . ASP B 53 ? 0.3500 0.2785 0.3332 0.0132 -0.0291 -0.0396 53 ASP B OD1 3510 O OD2 . ASP B 53 ? 0.3844 0.3869 0.3697 0.0148 0.0216 -0.0352 53 ASP B OD2 3511 N N . TRP B 54 ? 0.1917 0.1943 0.1782 0.0064 -0.0069 -0.0052 54 TRP B N 3512 C CA . TRP B 54 ? 0.1899 0.1885 0.1725 0.0018 -0.0013 -0.0018 54 TRP B CA 3513 C C . TRP B 54 ? 0.1988 0.1938 0.1689 0.0008 0.0009 -0.0028 54 TRP B C 3514 O O . TRP B 54 ? 0.2030 0.2073 0.1683 0.0142 0.0169 0.0010 54 TRP B O 3515 C CB . TRP B 54 ? 0.2040 0.1956 0.1680 0.0039 -0.0016 0.0049 54 TRP B CB 3516 C CG . TRP B 54 ? 0.2042 0.1875 0.1810 0.0107 0.0044 -0.0013 54 TRP B CG 3517 C CD1 . TRP B 54 ? 0.1902 0.1913 0.1900 0.0039 -0.0025 0.0034 54 TRP B CD1 3518 C CD2 . TRP B 54 ? 0.2384 0.2177 0.1807 0.0206 0.0025 0.0009 54 TRP B CD2 3519 N NE1 . TRP B 54 ? 0.1893 0.1806 0.1980 -0.0036 0.0124 0.0023 54 TRP B NE1 3520 C CE2 . TRP B 54 ? 0.2308 0.2093 0.1967 0.0259 0.0083 -0.0013 54 TRP B CE2 3521 C CE3 . TRP B 54 ? 0.2834 0.2314 0.2180 0.0335 0.0067 0.0046 54 TRP B CE3 3522 C CZ2 . TRP B 54 ? 0.2660 0.2341 0.2126 0.0244 0.0090 0.0088 54 TRP B CZ2 3523 C CZ3 . TRP B 54 ? 0.2773 0.2314 0.2161 0.0274 0.0086 0.0078 54 TRP B CZ3 3524 C CH2 . TRP B 54 ? 0.2819 0.2289 0.2115 0.0315 0.0083 0.0025 54 TRP B CH2 3525 N N . GLY B 55 ? 0.1784 0.1847 0.1632 -0.0039 0.0002 0.0007 55 GLY B N 3526 C CA . GLY B 55 ? 0.1821 0.1891 0.1743 0.0012 0.0052 0.0044 55 GLY B CA 3527 C C . GLY B 55 ? 0.1756 0.1914 0.1731 0.0084 0.0090 0.0053 55 GLY B C 3528 O O . GLY B 55 ? 0.1794 0.2049 0.1947 0.0187 0.0238 0.0162 55 GLY B O 3529 N N . ASN B 56 ? 0.1698 0.1915 0.1727 0.0084 0.0141 0.0159 56 ASN B N 3530 C CA . ASN B 56 ? 0.1735 0.1934 0.1822 0.0011 0.0088 0.0066 56 ASN B CA 3531 C C . ASN B 56 ? 0.1644 0.1875 0.1825 0.0057 0.0101 0.0093 56 ASN B C 3532 O O . ASN B 56 ? 0.1659 0.1820 0.1826 0.0153 0.0137 0.0096 56 ASN B O 3533 C CB A ASN B 56 ? 0.1838 0.1977 0.1882 0.0023 0.0109 0.0092 56 ASN B CB 3534 C CB B ASN B 56 ? 0.1805 0.1967 0.1858 0.0037 0.0108 0.0090 56 ASN B CB 3535 C CG A ASN B 56 ? 0.2089 0.2176 0.2015 0.0035 0.0012 0.0024 56 ASN B CG 3536 C CG B ASN B 56 ? 0.1900 0.2099 0.1891 0.0067 0.0044 0.0012 56 ASN B CG 3537 O OD1 A ASN B 56 ? 0.2469 0.2429 0.2219 0.0056 0.0284 0.0104 56 ASN B OD1 3538 O OD1 B ASN B 56 ? 0.2413 0.2261 0.2201 0.0105 0.0223 0.0096 56 ASN B OD1 3539 N ND2 A ASN B 56 ? 0.2363 0.2227 0.2100 -0.0168 0.0083 0.0058 56 ASN B ND2 3540 N ND2 B ASN B 56 ? 0.1748 0.2161 0.1757 0.0295 0.0138 -0.0088 56 ASN B ND2 3541 N N . PRO B 57 ? 0.1640 0.1809 0.1740 0.0032 0.0072 0.0148 57 PRO B N 3542 C CA . PRO B 57 ? 0.1689 0.1896 0.1817 0.0021 0.0063 0.0052 57 PRO B CA 3543 C C . PRO B 57 ? 0.1601 0.1916 0.1814 0.0029 0.0092 0.0021 57 PRO B C 3544 O O . PRO B 57 ? 0.1686 0.2244 0.1979 0.0131 0.0082 0.0040 57 PRO B O 3545 C CB . PRO B 57 ? 0.1733 0.1866 0.1783 0.0049 0.0023 0.0032 57 PRO B CB 3546 C CG . PRO B 57 ? 0.1813 0.2003 0.2049 -0.0074 0.0090 0.0214 57 PRO B CG 3547 C CD . PRO B 57 ? 0.1809 0.1868 0.1889 -0.0018 0.0100 0.0117 57 PRO B CD 3548 N N . PRO B 58 ? 0.1552 0.1919 0.1744 -0.0014 0.0116 0.0070 58 PRO B N 3549 C CA . PRO B 58 ? 0.1610 0.1891 0.1794 0.0014 0.0112 0.0047 58 PRO B CA 3550 C C . PRO B 58 ? 0.1735 0.1967 0.1938 0.0022 0.0090 0.0047 58 PRO B C 3551 O O . PRO B 58 ? 0.1731 0.1865 0.2010 0.0059 0.0159 0.0051 58 PRO B O 3552 C CB . PRO B 58 ? 0.1609 0.1810 0.1781 0.0030 0.0134 0.0067 58 PRO B CB 3553 C CG . PRO B 58 ? 0.1482 0.1890 0.1642 0.0041 0.0209 0.0096 58 PRO B CG 3554 C CD . PRO B 58 ? 0.1654 0.1739 0.1602 0.0029 0.0207 0.0018 58 PRO B CD 3555 N N . PRO B 59 ? 0.1824 0.2048 0.1958 0.0075 0.0181 0.0071 59 PRO B N 3556 C CA . PRO B 59 ? 0.1984 0.2221 0.2029 0.0029 0.0177 0.0042 59 PRO B CA 3557 C C . PRO B 59 ? 0.2025 0.2262 0.2095 0.0091 0.0176 0.0122 59 PRO B C 3558 O O . PRO B 59 ? 0.1793 0.2393 0.2174 0.0216 0.0273 0.0166 59 PRO B O 3559 C CB . PRO B 59 ? 0.2078 0.2149 0.2087 0.0094 0.0196 0.0053 59 PRO B CB 3560 C CG . PRO B 59 ? 0.2085 0.2245 0.2111 0.0050 0.0120 -0.0133 59 PRO B CG 3561 C CD . PRO B 59 ? 0.2005 0.2121 0.1955 0.0107 0.0062 -0.0062 59 PRO B CD 3562 N N . LYS B 60 ? 0.2038 0.2261 0.2320 0.0000 0.0171 0.0112 60 LYS B N 3563 C CA . LYS B 60 ? 0.2347 0.2550 0.2537 -0.0004 0.0082 0.0089 60 LYS B CA 3564 C C . LYS B 60 ? 0.2297 0.2505 0.2525 -0.0034 0.0127 0.0110 60 LYS B C 3565 O O . LYS B 60 ? 0.2236 0.2434 0.2763 0.0025 0.0127 0.0151 60 LYS B O 3566 C CB . LYS B 60 ? 0.2440 0.2681 0.2605 -0.0036 0.0124 0.0063 60 LYS B CB 3567 C CG . LYS B 60 ? 0.2825 0.2957 0.3100 0.0016 0.0045 0.0036 60 LYS B CG 3568 C CD . LYS B 60 ? 0.2967 0.2905 0.3109 -0.0081 0.0043 0.0054 60 LYS B CD 3569 C CE . LYS B 60 ? 0.3375 0.3109 0.3590 -0.0028 0.0018 0.0065 60 LYS B CE 3570 N NZ . LYS B 60 ? 0.3305 0.3395 0.3841 -0.0218 0.0055 0.0054 60 LYS B NZ 3571 N N . ASP B 61 ? 0.2349 0.2553 0.2626 0.0078 0.0172 0.0132 61 ASP B N 3572 C CA . ASP B 61 ? 0.2534 0.2648 0.2735 0.0064 0.0081 0.0094 61 ASP B CA 3573 C C . ASP B 61 ? 0.2430 0.2750 0.2698 0.0124 0.0078 0.0144 61 ASP B C 3574 O O . ASP B 61 ? 0.2646 0.3233 0.3155 0.0188 0.0079 0.0310 61 ASP B O 3575 C CB . ASP B 61 ? 0.2657 0.2779 0.2824 0.0115 0.0179 0.0083 61 ASP B CB 3576 C CG . ASP B 61 ? 0.2971 0.2881 0.2889 -0.0030 0.0081 -0.0066 61 ASP B CG 3577 O OD1 . ASP B 61 ? 0.3137 0.3000 0.3281 0.0155 0.0311 0.0042 61 ASP B OD1 3578 O OD2 . ASP B 61 ? 0.2951 0.3059 0.3007 0.0062 0.0008 -0.0022 61 ASP B OD2 3579 N N . VAL B 62 ? 0.2241 0.2391 0.2466 0.0131 0.0085 0.0117 62 VAL B N 3580 C CA . VAL B 62 ? 0.2243 0.2334 0.2388 0.0066 0.0029 0.0061 62 VAL B CA 3581 C C . VAL B 62 ? 0.2013 0.2180 0.2283 0.0071 0.0094 0.0105 62 VAL B C 3582 O O . VAL B 62 ? 0.1959 0.2159 0.2318 0.0177 0.0041 0.0074 62 VAL B O 3583 C CB . VAL B 62 ? 0.2333 0.2393 0.2351 0.0017 0.0034 0.0035 62 VAL B CB 3584 C CG1 . VAL B 62 ? 0.2733 0.2549 0.2763 -0.0051 0.0061 0.0020 62 VAL B CG1 3585 C CG2 . VAL B 62 ? 0.2478 0.2552 0.2236 0.0022 0.0027 0.0028 62 VAL B CG2 3586 N N . CYS B 63 ? 0.1760 0.2033 0.2158 0.0023 0.0131 0.0161 63 CYS B N 3587 C CA . CYS B 63 ? 0.1782 0.2013 0.2132 0.0025 0.0045 0.0125 63 CYS B CA 3588 C C . CYS B 63 ? 0.1931 0.2094 0.2267 0.0002 0.0024 0.0058 63 CYS B C 3589 O O . CYS B 63 ? 0.1800 0.2045 0.2345 -0.0037 0.0096 0.0199 63 CYS B O 3590 C CB . CYS B 63 ? 0.1668 0.1868 0.1989 0.0063 0.0064 0.0126 63 CYS B CB 3591 S SG . CYS B 63 ? 0.1452 0.1762 0.2174 0.0239 0.0270 0.0096 63 CYS B SG 3592 N N . PRO B 64 ? 0.1915 0.2079 0.2394 0.0028 0.0061 0.0049 64 PRO B N 3593 C CA . PRO B 64 ? 0.1941 0.2132 0.2377 0.0017 0.0053 0.0077 64 PRO B CA 3594 C C . PRO B 64 ? 0.1913 0.2156 0.2438 0.0038 0.0058 0.0070 64 PRO B C 3595 O O . PRO B 64 ? 0.1836 0.2201 0.2761 0.0117 0.0099 0.0069 64 PRO B O 3596 C CB . PRO B 64 ? 0.2052 0.2302 0.2465 0.0087 0.0059 0.0125 64 PRO B CB 3597 C CG . PRO B 64 ? 0.1942 0.2157 0.2397 0.0059 -0.0001 -0.0004 64 PRO B CG 3598 C CD . PRO B 64 ? 0.2008 0.2215 0.2393 0.0015 0.0069 0.0050 64 PRO B CD 3599 N N . ASP B 65 ? 0.1891 0.2123 0.2427 0.0083 0.0020 0.0097 65 ASP B N 3600 C CA . ASP B 65 ? 0.1781 0.2116 0.2362 0.0019 -0.0034 0.0047 65 ASP B CA 3601 C C . ASP B 65 ? 0.1811 0.1984 0.2255 0.0051 -0.0028 0.0032 65 ASP B C 3602 O O . ASP B 65 ? 0.1374 0.1953 0.2417 0.0166 -0.0061 -0.0010 65 ASP B O 3603 C CB . ASP B 65 ? 0.1958 0.2169 0.2528 0.0022 -0.0080 0.0042 65 ASP B CB 3604 C CG . ASP B 65 ? 0.2329 0.2471 0.3102 0.0047 0.0040 0.0048 65 ASP B CG 3605 O OD1 . ASP B 65 ? 0.2073 0.2422 0.3402 -0.0011 -0.0098 0.0245 65 ASP B OD1 3606 O OD2 . ASP B 65 ? 0.2515 0.3375 0.3959 0.0055 -0.0128 0.0123 65 ASP B OD2 3607 N N . VAL B 66 ? 0.1720 0.2054 0.2265 0.0070 -0.0076 0.0052 66 VAL B N 3608 C CA . VAL B 66 ? 0.1905 0.2041 0.2142 0.0063 0.0000 0.0002 66 VAL B CA 3609 C C . VAL B 66 ? 0.1917 0.2070 0.2186 0.0033 -0.0065 -0.0019 66 VAL B C 3610 O O . VAL B 66 ? 0.1560 0.1850 0.2235 0.0245 0.0032 -0.0038 66 VAL B O 3611 C CB . VAL B 66 ? 0.2047 0.1998 0.2114 0.0079 -0.0028 -0.0003 66 VAL B CB 3612 C CG1 . VAL B 66 ? 0.2242 0.2157 0.2168 0.0098 0.0001 -0.0019 66 VAL B CG1 3613 C CG2 . VAL B 66 ? 0.1983 0.2114 0.2191 0.0138 0.0000 -0.0027 66 VAL B CG2 3614 N N . GLU B 67 ? 0.1958 0.2141 0.2358 0.0082 -0.0048 0.0009 67 GLU B N 3615 C CA . GLU B 67 ? 0.2092 0.2211 0.2335 0.0006 -0.0007 0.0013 67 GLU B CA 3616 C C . GLU B 67 ? 0.1977 0.2070 0.2351 0.0022 -0.0009 0.0050 67 GLU B C 3617 O O . GLU B 67 ? 0.1833 0.2035 0.2544 0.0085 0.0081 0.0046 67 GLU B O 3618 C CB . GLU B 67 ? 0.2270 0.2419 0.2549 0.0035 -0.0074 0.0045 67 GLU B CB 3619 C CG . GLU B 67 ? 0.2980 0.3168 0.3163 -0.0029 -0.0069 -0.0085 67 GLU B CG 3620 C CD . GLU B 67 ? 0.3226 0.3395 0.3550 -0.0112 -0.0135 -0.0122 67 GLU B CD 3621 O OE1 . GLU B 67 ? 0.3695 0.4039 0.4032 -0.0273 -0.0188 0.0262 67 GLU B OE1 3622 O OE2 . GLU B 67 ? 0.4120 0.3845 0.4836 0.0035 -0.0061 0.0044 67 GLU B OE2 3623 N N . SER B 68 ? 0.1835 0.2053 0.2293 0.0071 -0.0062 0.0023 68 SER B N 3624 C CA . SER B 68 ? 0.1964 0.2057 0.2198 0.0062 -0.0004 0.0017 68 SER B CA 3625 C C . SER B 68 ? 0.1785 0.1886 0.2118 0.0016 0.0064 -0.0029 68 SER B C 3626 O O . SER B 68 ? 0.1742 0.1918 0.2336 0.0075 0.0162 0.0007 68 SER B O 3627 C CB . SER B 68 ? 0.1989 0.2128 0.2246 0.0077 0.0032 -0.0101 68 SER B CB 3628 O OG . SER B 68 ? 0.2165 0.2291 0.2744 0.0223 0.0035 0.0076 68 SER B OG 3629 N N . CYS B 69 ? 0.1792 0.1833 0.2052 0.0037 0.0096 0.0027 69 CYS B N 3630 C CA . CYS B 69 ? 0.1903 0.1924 0.1925 0.0015 0.0035 -0.0009 69 CYS B CA 3631 C C . CYS B 69 ? 0.1669 0.1765 0.1751 -0.0040 0.0021 -0.0070 69 CYS B C 3632 O O . CYS B 69 ? 0.1772 0.1929 0.1775 -0.0099 0.0012 -0.0058 69 CYS B O 3633 C CB . CYS B 69 ? 0.1964 0.2001 0.2018 0.0011 0.0052 -0.0021 69 CYS B CB 3634 S SG . CYS B 69 ? 0.1519 0.1970 0.2252 0.0155 0.0221 -0.0016 69 CYS B SG 3635 N N . ALA B 70 ? 0.1589 0.1766 0.1815 0.0072 -0.0081 -0.0076 70 ALA B N 3636 C CA . ALA B 70 ? 0.1572 0.1732 0.1741 0.0097 -0.0072 -0.0024 70 ALA B CA 3637 C C . ALA B 70 ? 0.1554 0.1735 0.1634 0.0054 -0.0004 -0.0038 70 ALA B C 3638 O O . ALA B 70 ? 0.1634 0.1808 0.1923 0.0072 -0.0028 0.0053 70 ALA B O 3639 C CB . ALA B 70 ? 0.1624 0.1750 0.1741 0.0169 0.0034 -0.0126 70 ALA B CB 3640 N N . LYS B 71 ? 0.1535 0.1734 0.1751 0.0082 -0.0001 -0.0045 71 LYS B N 3641 C CA . LYS B 71 ? 0.1718 0.1817 0.1746 0.0087 -0.0037 -0.0031 71 LYS B CA 3642 C C . LYS B 71 ? 0.1681 0.1652 0.1631 0.0091 0.0024 -0.0007 71 LYS B C 3643 O O . LYS B 71 ? 0.1936 0.1820 0.1666 0.0108 0.0092 -0.0013 71 LYS B O 3644 C CB . LYS B 71 ? 0.1765 0.1824 0.1863 0.0128 -0.0034 -0.0064 71 LYS B CB 3645 C CG . LYS B 71 ? 0.1987 0.2245 0.2066 0.0069 -0.0045 0.0029 71 LYS B CG 3646 C CD . LYS B 71 ? 0.2152 0.2324 0.2178 0.0119 -0.0151 -0.0058 71 LYS B CD 3647 C CE . LYS B 71 ? 0.2375 0.2511 0.2511 0.0069 -0.0112 -0.0110 71 LYS B CE 3648 N NZ . LYS B 71 ? 0.2181 0.3006 0.2857 -0.0024 -0.0213 0.0003 71 LYS B NZ 3649 N N . ASN B 72 ? 0.1566 0.1618 0.1497 0.0188 0.0005 0.0068 72 ASN B N 3650 C CA . ASN B 72 ? 0.1592 0.1694 0.1669 0.0096 -0.0052 -0.0011 72 ASN B CA 3651 C C . ASN B 72 ? 0.1609 0.1754 0.1654 0.0174 -0.0063 -0.0023 72 ASN B C 3652 O O . ASN B 72 ? 0.1539 0.1973 0.1652 0.0306 -0.0155 -0.0072 72 ASN B O 3653 C CB . ASN B 72 ? 0.1562 0.1807 0.1686 0.0068 -0.0094 0.0008 72 ASN B CB 3654 C CG . ASN B 72 ? 0.1557 0.1588 0.1699 0.0345 0.0054 0.0009 72 ASN B CG 3655 O OD1 . ASN B 72 ? 0.1859 0.1620 0.1885 0.0240 0.0135 0.0206 72 ASN B OD1 3656 N ND2 . ASN B 72 ? 0.1784 0.1956 0.1949 0.0316 0.0180 0.0033 72 ASN B ND2 3657 N N . CYS B 73 ? 0.1468 0.1768 0.1646 0.0159 0.0015 0.0049 73 CYS B N 3658 C CA . CYS B 73 ? 0.1545 0.1685 0.1454 0.0081 -0.0011 0.0007 73 CYS B CA 3659 C C . CYS B 73 ? 0.1518 0.1648 0.1458 0.0091 0.0038 0.0029 73 CYS B C 3660 O O . CYS B 73 ? 0.1685 0.1769 0.1418 0.0071 0.0086 -0.0172 73 CYS B O 3661 C CB . CYS B 73 ? 0.1546 0.1729 0.1430 0.0091 0.0017 0.0034 73 CYS B CB 3662 S SG . CYS B 73 ? 0.1553 0.1783 0.1599 0.0198 0.0132 0.0134 73 CYS B SG 3663 N N . ILE B 74 ? 0.1447 0.1671 0.1491 0.0133 0.0016 0.0034 74 ILE B N 3664 C CA . ILE B 74 ? 0.1612 0.1823 0.1682 0.0062 0.0061 0.0051 74 ILE B CA 3665 C C . ILE B 74 ? 0.1601 0.2051 0.1676 0.0055 0.0074 0.0039 74 ILE B C 3666 O O . ILE B 74 ? 0.1482 0.2529 0.1695 0.0129 0.0191 0.0008 74 ILE B O 3667 C CB . ILE B 74 ? 0.1643 0.1875 0.1863 -0.0046 0.0156 0.0019 74 ILE B CB 3668 C CG1 . ILE B 74 ? 0.2178 0.2190 0.2325 0.0219 -0.0029 0.0053 74 ILE B CG1 3669 C CG2 . ILE B 74 ? 0.1881 0.1872 0.2051 0.0030 0.0176 0.0069 74 ILE B CG2 3670 C CD1 . ILE B 74 ? 0.2330 0.2425 0.2468 0.0248 0.0054 -0.0080 74 ILE B CD1 3671 N N . MET B 75 ? 0.1575 0.1789 0.1531 0.0089 0.0070 0.0078 75 MET B N 3672 C CA . MET B 75 ? 0.1544 0.1710 0.1598 0.0049 0.0005 0.0003 75 MET B CA 3673 C C . MET B 75 ? 0.1443 0.1601 0.1511 0.0028 0.0001 -0.0048 75 MET B C 3674 O O . MET B 75 ? 0.1454 0.1831 0.1446 0.0098 -0.0116 -0.0101 75 MET B O 3675 C CB . MET B 75 ? 0.1538 0.1613 0.1691 -0.0035 0.0077 0.0056 75 MET B CB 3676 C CG . MET B 75 ? 0.1664 0.1865 0.1760 0.0106 0.0000 0.0122 75 MET B CG 3677 S SD . MET B 75 ? 0.1704 0.1840 0.1717 0.0245 0.0215 0.0061 75 MET B SD 3678 C CE . MET B 75 ? 0.1446 0.1922 0.1856 0.0209 0.0187 -0.0040 75 MET B CE 3679 N N . GLU B 76 ? 0.1475 0.1744 0.1495 0.0124 -0.0131 -0.0019 76 GLU B N 3680 C CA . GLU B 76 ? 0.1639 0.1715 0.1588 0.0085 -0.0057 0.0027 76 GLU B CA 3681 C C . GLU B 76 ? 0.1599 0.1573 0.1572 0.0012 -0.0029 0.0032 76 GLU B C 3682 O O . GLU B 76 ? 0.1691 0.1499 0.1639 0.0072 0.0049 0.0231 76 GLU B O 3683 C CB . GLU B 76 ? 0.1882 0.2017 0.1805 0.0043 -0.0197 -0.0018 76 GLU B CB 3684 C CG . GLU B 76 ? 0.2375 0.2344 0.2122 0.0075 -0.0093 -0.0044 76 GLU B CG 3685 C CD . GLU B 76 ? 0.2455 0.2148 0.2051 0.0299 -0.0108 -0.0137 76 GLU B CD 3686 O OE1 . GLU B 76 ? 0.1954 0.2546 0.2402 0.0419 -0.0151 -0.0276 76 GLU B OE1 3687 O OE2 . GLU B 76 ? 0.3018 0.2991 0.2863 0.0082 -0.0060 0.0057 76 GLU B OE2 3688 N N . GLY B 77 ? 0.1601 0.1512 0.1547 0.0050 -0.0062 0.0021 77 GLY B N 3689 C CA . GLY B 77 ? 0.1617 0.1438 0.1554 0.0050 -0.0027 0.0034 77 GLY B CA 3690 C C . GLY B 77 ? 0.1658 0.1502 0.1535 0.0054 -0.0052 0.0037 77 GLY B C 3691 O O . GLY B 77 ? 0.1476 0.1551 0.1416 0.0142 -0.0037 0.0012 77 GLY B O 3692 N N . ILE B 78 ? 0.1548 0.1487 0.1572 0.0079 0.0002 -0.0066 78 ILE B N 3693 C CA . ILE B 78 ? 0.1542 0.1491 0.1588 0.0083 -0.0007 -0.0021 78 ILE B CA 3694 C C . ILE B 78 ? 0.1642 0.1518 0.1546 0.0091 -0.0017 0.0004 78 ILE B C 3695 O O . ILE B 78 ? 0.1570 0.1616 0.1474 0.0113 0.0062 0.0088 78 ILE B O 3696 C CB . ILE B 78 ? 0.1501 0.1436 0.1602 0.0092 0.0036 0.0008 78 ILE B CB 3697 C CG1 . ILE B 78 ? 0.1613 0.1419 0.1555 0.0057 0.0037 -0.0085 78 ILE B CG1 3698 C CG2 . ILE B 78 ? 0.1456 0.1486 0.1557 0.0120 0.0064 0.0012 78 ILE B CG2 3699 C CD1 . ILE B 78 ? 0.1626 0.1642 0.1681 0.0058 0.0019 0.0033 78 ILE B CD1 3700 N N . PRO B 79 ? 0.1582 0.1491 0.1609 0.0062 0.0017 0.0057 79 PRO B N 3701 C CA . PRO B 79 ? 0.1650 0.1510 0.1580 0.0091 0.0063 0.0041 79 PRO B CA 3702 C C . PRO B 79 ? 0.1744 0.1535 0.1670 -0.0027 0.0005 0.0055 79 PRO B C 3703 O O . PRO B 79 ? 0.1733 0.1771 0.1679 -0.0062 0.0102 0.0100 79 PRO B O 3704 C CB . PRO B 79 ? 0.1681 0.1359 0.1771 0.0079 -0.0054 0.0122 79 PRO B CB 3705 C CG . PRO B 79 ? 0.1635 0.1571 0.1884 0.0169 -0.0034 -0.0049 79 PRO B CG 3706 C CD . PRO B 79 ? 0.1657 0.1522 0.1708 0.0090 -0.0082 -0.0002 79 PRO B CD 3707 N N . ASP B 80 ? 0.1742 0.1437 0.1577 0.0046 0.0000 -0.0053 80 ASP B N 3708 C CA . ASP B 80 ? 0.1693 0.1357 0.1571 0.0024 -0.0017 -0.0049 80 ASP B CA 3709 C C . ASP B 80 ? 0.1697 0.1364 0.1511 -0.0012 0.0025 0.0020 80 ASP B C 3710 O O . ASP B 80 ? 0.1769 0.1382 0.1429 0.0042 -0.0001 -0.0085 80 ASP B O 3711 C CB . ASP B 80 ? 0.1825 0.1481 0.1752 -0.0011 -0.0132 -0.0140 80 ASP B CB 3712 C CG . ASP B 80 ? 0.1862 0.1670 0.1793 0.0100 -0.0131 -0.0150 80 ASP B CG 3713 O OD1 . ASP B 80 ? 0.1803 0.1754 0.2219 -0.0030 -0.0329 -0.0185 80 ASP B OD1 3714 O OD2 . ASP B 80 ? 0.2389 0.1873 0.2256 -0.0003 -0.0466 -0.0310 80 ASP B OD2 3715 N N . TYR B 81 ? 0.1575 0.1352 0.1451 0.0029 0.0000 0.0008 81 TYR B N 3716 C CA . TYR B 81 ? 0.1527 0.1284 0.1402 0.0003 -0.0024 0.0020 81 TYR B CA 3717 C C . TYR B 81 ? 0.1586 0.1364 0.1389 -0.0006 0.0006 0.0003 81 TYR B C 3718 O O . TYR B 81 ? 0.1551 0.1206 0.1327 0.0148 -0.0057 0.0078 81 TYR B O 3719 C CB . TYR B 81 ? 0.1412 0.1221 0.1300 0.0044 -0.0043 -0.0042 81 TYR B CB 3720 C CG . TYR B 81 ? 0.1259 0.1255 0.1263 0.0014 -0.0036 0.0022 81 TYR B CG 3721 C CD1 . TYR B 81 ? 0.1507 0.1196 0.1287 0.0049 -0.0125 0.0132 81 TYR B CD1 3722 C CD2 . TYR B 81 ? 0.1301 0.1192 0.1089 0.0121 -0.0017 0.0054 81 TYR B CD2 3723 C CE1 . TYR B 81 ? 0.1288 0.1128 0.1216 0.0067 -0.0023 0.0068 81 TYR B CE1 3724 C CE2 . TYR B 81 ? 0.1252 0.1124 0.1395 0.0103 -0.0020 -0.0004 81 TYR B CE2 3725 C CZ . TYR B 81 ? 0.1289 0.1283 0.1243 0.0083 -0.0075 -0.0051 81 TYR B CZ 3726 O OH . TYR B 81 ? 0.1280 0.1154 0.1278 0.0078 0.0004 -0.0145 81 TYR B OH 3727 N N . SER B 82 ? 0.1634 0.1276 0.1468 -0.0023 -0.0068 0.0036 82 SER B N 3728 C CA . SER B 82 ? 0.1661 0.1400 0.1523 -0.0016 -0.0088 -0.0032 82 SER B CA 3729 C C . SER B 82 ? 0.1727 0.1441 0.1579 0.0029 -0.0093 -0.0041 82 SER B C 3730 O O . SER B 82 ? 0.1825 0.1376 0.1331 0.0177 -0.0255 -0.0058 82 SER B O 3731 C CB . SER B 82 ? 0.1584 0.1444 0.1643 -0.0026 -0.0119 -0.0062 82 SER B CB 3732 O OG . SER B 82 ? 0.1891 0.1425 0.1816 -0.0019 -0.0082 -0.0020 82 SER B OG 3733 N N . GLN B 83 ? 0.1712 0.1571 0.1511 0.0039 0.0014 -0.0001 83 GLN B N 3734 C CA . GLN B 83 ? 0.1870 0.1651 0.1532 0.0049 0.0025 -0.0012 83 GLN B CA 3735 C C . GLN B 83 ? 0.1910 0.1643 0.1506 0.0009 0.0105 -0.0106 83 GLN B C 3736 O O . GLN B 83 ? 0.2052 0.1595 0.1542 0.0147 0.0164 -0.0281 83 GLN B O 3737 C CB . GLN B 83 ? 0.2004 0.1829 0.1745 0.0037 0.0068 -0.0044 83 GLN B CB 3738 C CG . GLN B 83 ? 0.2548 0.2199 0.2075 0.0058 0.0061 0.0151 83 GLN B CG 3739 C CD . GLN B 83 ? 0.3000 0.2726 0.2687 -0.0021 0.0014 0.0093 83 GLN B CD 3740 O OE1 . GLN B 83 ? 0.3994 0.3463 0.2791 0.0067 0.0128 -0.0151 83 GLN B OE1 3741 N NE2 . GLN B 83 ? 0.3418 0.3438 0.3036 -0.0198 0.0113 -0.0093 83 GLN B NE2 3742 N N . TYR B 84 ? 0.1622 0.1409 0.1263 0.0063 -0.0017 -0.0136 84 TYR B N 3743 C CA . TYR B 84 ? 0.1516 0.1422 0.1256 0.0018 0.0021 -0.0074 84 TYR B CA 3744 C C . TYR B 84 ? 0.1313 0.1348 0.1097 0.0000 -0.0055 -0.0070 84 TYR B C 3745 O O . TYR B 84 ? 0.1386 0.1303 0.1341 0.0047 0.0066 -0.0023 84 TYR B O 3746 C CB . TYR B 84 ? 0.1620 0.1493 0.1414 -0.0034 0.0011 -0.0064 84 TYR B CB 3747 C CG . TYR B 84 ? 0.1553 0.1475 0.1225 -0.0018 -0.0142 -0.0051 84 TYR B CG 3748 C CD1 . TYR B 84 ? 0.1601 0.1581 0.1465 0.0072 0.0057 0.0035 84 TYR B CD1 3749 C CD2 . TYR B 84 ? 0.1501 0.1809 0.1380 0.0082 -0.0092 -0.0070 84 TYR B CD2 3750 C CE1 . TYR B 84 ? 0.1689 0.1676 0.1419 0.0144 -0.0079 0.0027 84 TYR B CE1 3751 C CE2 . TYR B 84 ? 0.1524 0.1967 0.1725 0.0016 0.0061 -0.0035 84 TYR B CE2 3752 C CZ . TYR B 84 ? 0.1343 0.1822 0.1657 0.0056 -0.0069 -0.0072 84 TYR B CZ 3753 O OH . TYR B 84 ? 0.1704 0.2314 0.2038 0.0233 -0.0026 -0.0111 84 TYR B OH 3754 N N . GLY B 85 ? 0.1354 0.1106 0.1132 0.0049 0.0017 -0.0178 85 GLY B N 3755 C CA . GLY B 85 ? 0.1343 0.1267 0.1194 0.0024 -0.0027 -0.0082 85 GLY B CA 3756 C C . GLY B 85 ? 0.1301 0.1201 0.1128 0.0067 -0.0022 -0.0085 85 GLY B C 3757 O O . GLY B 85 ? 0.1406 0.1357 0.1106 0.0187 -0.0069 -0.0048 85 GLY B O 3758 N N . VAL B 86 ? 0.1263 0.1246 0.1162 0.0089 0.0007 -0.0082 86 VAL B N 3759 C CA . VAL B 86 ? 0.1267 0.1179 0.1081 0.0044 0.0024 -0.0102 86 VAL B CA 3760 C C . VAL B 86 ? 0.1271 0.1154 0.1148 0.0050 -0.0018 -0.0088 86 VAL B C 3761 O O . VAL B 86 ? 0.1407 0.1034 0.1364 0.0062 -0.0025 -0.0013 86 VAL B O 3762 C CB . VAL B 86 ? 0.1134 0.1116 0.1088 0.0116 0.0071 -0.0107 86 VAL B CB 3763 C CG1 . VAL B 86 ? 0.1259 0.1078 0.0928 0.0043 0.0071 -0.0050 86 VAL B CG1 3764 C CG2 . VAL B 86 ? 0.1386 0.1338 0.1053 0.0077 0.0090 -0.0099 86 VAL B CG2 3765 N N . THR B 87 ? 0.1306 0.1221 0.1125 0.0014 0.0057 0.0022 87 THR B N 3766 C CA . THR B 87 ? 0.1371 0.1255 0.1295 -0.0045 0.0035 -0.0021 87 THR B CA 3767 C C . THR B 87 ? 0.1421 0.1310 0.1278 0.0017 0.0072 -0.0008 87 THR B C 3768 O O . THR B 87 ? 0.1327 0.1350 0.1369 -0.0002 0.0058 -0.0032 87 THR B O 3769 C CB . THR B 87 ? 0.1296 0.1365 0.1403 -0.0068 -0.0004 0.0045 87 THR B CB 3770 O OG1 . THR B 87 ? 0.1493 0.1378 0.1583 0.0004 -0.0015 -0.0032 87 THR B OG1 3771 C CG2 . THR B 87 ? 0.1526 0.1489 0.1353 -0.0099 -0.0137 0.0107 87 THR B CG2 3772 N N . THR B 88 ? 0.1460 0.1352 0.1378 0.0002 -0.0028 0.0055 88 THR B N 3773 C CA . THR B 88 ? 0.1486 0.1403 0.1453 -0.0010 0.0036 0.0009 88 THR B CA 3774 C C . THR B 88 ? 0.1572 0.1430 0.1533 -0.0048 -0.0017 0.0002 88 THR B C 3775 O O . THR B 88 ? 0.1819 0.1487 0.1607 -0.0072 0.0061 -0.0058 88 THR B O 3776 C CB . THR B 88 ? 0.1481 0.1392 0.1380 0.0054 0.0032 0.0005 88 THR B CB 3777 O OG1 . THR B 88 ? 0.1640 0.1403 0.1477 0.0115 0.0120 0.0193 88 THR B OG1 3778 C CG2 . THR B 88 ? 0.1510 0.1350 0.1263 0.0168 0.0128 -0.0007 88 THR B CG2 3779 N N . ASN B 89 ? 0.1666 0.1519 0.1645 -0.0108 0.0078 -0.0068 89 ASN B N 3780 C CA . ASN B 89 ? 0.1724 0.1646 0.1675 -0.0103 0.0075 -0.0030 89 ASN B CA 3781 C C . ASN B 89 ? 0.1593 0.1632 0.1584 -0.0113 0.0115 -0.0026 89 ASN B C 3782 O O . ASN B 89 ? 0.1820 0.1608 0.1573 -0.0182 0.0046 -0.0035 89 ASN B O 3783 C CB . ASN B 89 ? 0.1794 0.1750 0.1750 -0.0165 0.0046 -0.0081 89 ASN B CB 3784 C CG . ASN B 89 ? 0.1928 0.2024 0.1911 -0.0191 -0.0106 -0.0065 89 ASN B CG 3785 O OD1 . ASN B 89 ? 0.2220 0.2363 0.2459 -0.0585 -0.0130 0.0181 89 ASN B OD1 3786 N ND2 . ASN B 89 ? 0.2142 0.2379 0.2292 -0.0233 -0.0134 -0.0048 89 ASN B ND2 3787 N N . GLY B 90 ? 0.1629 0.1513 0.1741 -0.0164 0.0040 -0.0010 90 GLY B N 3788 C CA . GLY B 90 ? 0.1477 0.1458 0.1575 -0.0120 0.0077 0.0069 90 GLY B CA 3789 C C . GLY B 90 ? 0.1313 0.1345 0.1505 -0.0125 0.0095 0.0078 90 GLY B C 3790 O O . GLY B 90 ? 0.1258 0.1505 0.1485 -0.0139 0.0133 0.0088 90 GLY B O 3791 N N . THR B 91 ? 0.1155 0.1363 0.1408 -0.0144 0.0095 0.0093 91 THR B N 3792 C CA . THR B 91 ? 0.1249 0.1315 0.1317 -0.0065 0.0059 0.0034 91 THR B CA 3793 C C . THR B 91 ? 0.1179 0.1253 0.1296 -0.0025 0.0025 0.0094 91 THR B C 3794 O O . THR B 91 ? 0.1368 0.1135 0.1149 -0.0139 0.0090 0.0001 91 THR B O 3795 C CB . THR B 91 ? 0.1368 0.1444 0.1341 -0.0013 0.0051 0.0106 91 THR B CB 3796 O OG1 . THR B 91 ? 0.1353 0.1505 0.1485 -0.0239 0.0115 0.0089 91 THR B OG1 3797 C CG2 . THR B 91 ? 0.1349 0.1505 0.1310 -0.0053 0.0113 0.0100 91 THR B CG2 3798 N N . SER B 92 ? 0.1195 0.1420 0.1363 -0.0038 0.0103 0.0096 92 SER B N 3799 C CA . SER B 92 ? 0.1191 0.1394 0.1288 0.0029 0.0028 -0.0010 92 SER B CA 3800 C C . SER B 92 ? 0.1287 0.1253 0.1242 0.0016 0.0021 -0.0015 92 SER B C 3801 O O . SER B 92 ? 0.1311 0.1275 0.1305 -0.0019 0.0056 0.0055 92 SER B O 3802 C CB . SER B 92 ? 0.1302 0.1772 0.1372 -0.0013 0.0102 -0.0072 92 SER B CB 3803 O OG . SER B 92 ? 0.1636 0.2059 0.2116 0.0090 0.0044 -0.0124 92 SER B OG 3804 N N . LEU B 93 ? 0.1218 0.1188 0.1219 0.0023 0.0065 0.0010 93 LEU B N 3805 C CA . LEU B 93 ? 0.1185 0.1157 0.1192 -0.0033 0.0015 0.0028 93 LEU B CA 3806 C C . LEU B 93 ? 0.1086 0.1114 0.1166 0.0017 0.0047 -0.0006 93 LEU B C 3807 O O . LEU B 93 ? 0.1382 0.1236 0.1203 -0.0006 -0.0089 -0.0041 93 LEU B O 3808 C CB . LEU B 93 ? 0.1098 0.0974 0.1100 0.0000 0.0025 0.0099 93 LEU B CB 3809 C CG . LEU B 93 ? 0.1204 0.1033 0.1091 -0.0016 0.0084 -0.0031 93 LEU B CG 3810 C CD1 . LEU B 93 ? 0.1286 0.1282 0.1302 -0.0042 0.0119 0.0022 93 LEU B CD1 3811 C CD2 . LEU B 93 ? 0.1028 0.1271 0.1375 -0.0024 0.0031 -0.0029 93 LEU B CD2 3812 N N . ARG B 94 ? 0.1292 0.1235 0.1108 -0.0051 -0.0063 0.0020 94 ARG B N 3813 C CA . ARG B 94 ? 0.1266 0.1171 0.1165 0.0003 -0.0019 -0.0003 94 ARG B CA 3814 C C . ARG B 94 ? 0.1258 0.1167 0.1182 0.0032 -0.0020 0.0000 94 ARG B C 3815 O O . ARG B 94 ? 0.1238 0.1142 0.1353 0.0132 -0.0049 0.0102 94 ARG B O 3816 C CB . ARG B 94 ? 0.1310 0.1215 0.1142 -0.0025 -0.0043 0.0027 94 ARG B CB 3817 C CG . ARG B 94 ? 0.1397 0.1254 0.1261 -0.0109 -0.0008 0.0004 94 ARG B CG 3818 C CD . ARG B 94 ? 0.1522 0.1463 0.1361 -0.0034 -0.0042 -0.0100 94 ARG B CD 3819 N NE . ARG B 94 ? 0.1666 0.1597 0.1327 -0.0297 -0.0107 -0.0113 94 ARG B NE 3820 C CZ . ARG B 94 ? 0.2035 0.1661 0.1561 -0.0018 -0.0301 0.0005 94 ARG B CZ 3821 N NH1 . ARG B 94 ? 0.2423 0.1730 0.1760 -0.0095 -0.0359 -0.0230 94 ARG B NH1 3822 N NH2 . ARG B 94 ? 0.2452 0.1735 0.1524 -0.0116 -0.0367 0.0068 94 ARG B NH2 3823 N N . LEU B 95 ? 0.1198 0.1154 0.1323 0.0061 0.0069 -0.0030 95 LEU B N 3824 C CA . LEU B 95 ? 0.1264 0.1184 0.1194 -0.0039 0.0015 0.0004 95 LEU B CA 3825 C C . LEU B 95 ? 0.1325 0.1109 0.1244 -0.0083 -0.0019 -0.0024 95 LEU B C 3826 O O . LEU B 95 ? 0.1417 0.1332 0.1255 0.0011 0.0018 -0.0034 95 LEU B O 3827 C CB . LEU B 95 ? 0.1362 0.1027 0.1229 0.0026 0.0060 0.0001 95 LEU B CB 3828 C CG . LEU B 95 ? 0.1162 0.1190 0.1199 -0.0103 0.0059 -0.0074 95 LEU B CG 3829 C CD1 . LEU B 95 ? 0.1156 0.1258 0.1374 -0.0024 -0.0147 -0.0188 95 LEU B CD1 3830 C CD2 . LEU B 95 ? 0.1169 0.1231 0.1348 -0.0138 0.0079 0.0097 95 LEU B CD2 3831 N N . GLN B 96 ? 0.1319 0.1271 0.1120 0.0048 -0.0015 -0.0026 96 GLN B N 3832 C CA . GLN B 96 ? 0.1369 0.1315 0.1165 0.0008 -0.0030 -0.0055 96 GLN B CA 3833 C C . GLN B 96 ? 0.1345 0.1274 0.1201 0.0004 -0.0060 -0.0098 96 GLN B C 3834 O O . GLN B 96 ? 0.1411 0.1292 0.1163 0.0114 0.0034 -0.0127 96 GLN B O 3835 C CB . GLN B 96 ? 0.1432 0.1419 0.1190 -0.0013 0.0051 -0.0022 96 GLN B CB 3836 C CG . GLN B 96 ? 0.1537 0.1543 0.1481 0.0018 0.0028 0.0044 96 GLN B CG 3837 C CD . GLN B 96 ? 0.1667 0.1456 0.1470 -0.0164 -0.0063 -0.0073 96 GLN B CD 3838 O OE1 . GLN B 96 ? 0.1841 0.1594 0.1574 -0.0163 -0.0236 -0.0116 96 GLN B OE1 3839 N NE2 . GLN B 96 ? 0.2406 0.1893 0.1834 -0.0374 -0.0259 -0.0205 96 GLN B NE2 3840 N N . HIS B 97 ? 0.1241 0.1260 0.1146 0.0008 -0.0075 -0.0002 97 HIS B N 3841 C CA . HIS B 97 ? 0.1367 0.1328 0.1209 0.0027 -0.0027 -0.0075 97 HIS B CA 3842 C C . HIS B 97 ? 0.1386 0.1351 0.1279 0.0057 -0.0041 -0.0046 97 HIS B C 3843 O O . HIS B 97 ? 0.1523 0.1394 0.1097 -0.0009 0.0027 -0.0090 97 HIS B O 3844 C CB . HIS B 97 ? 0.1320 0.1271 0.1155 -0.0034 -0.0021 -0.0035 97 HIS B CB 3845 C CG . HIS B 97 ? 0.1417 0.1164 0.1147 0.0095 -0.0072 0.0075 97 HIS B CG 3846 N ND1 . HIS B 97 ? 0.1440 0.1656 0.1525 0.0061 0.0029 0.0081 97 HIS B ND1 3847 C CD2 . HIS B 97 ? 0.1164 0.1027 0.0938 -0.0034 -0.0169 -0.0036 97 HIS B CD2 3848 C CE1 . HIS B 97 ? 0.1153 0.1009 0.0799 -0.0076 -0.0028 0.0069 97 HIS B CE1 3849 N NE2 . HIS B 97 ? 0.1787 0.1463 0.1392 0.0208 0.0032 0.0150 97 HIS B NE2 3850 N N . ILE B 98 ? 0.1605 0.1469 0.1426 -0.0036 -0.0018 -0.0083 98 ILE B N 3851 C CA . ILE B 98 ? 0.1671 0.1544 0.1394 -0.0056 -0.0049 -0.0101 98 ILE B CA 3852 C C . ILE B 98 ? 0.1745 0.1642 0.1371 -0.0064 -0.0061 -0.0055 98 ILE B C 3853 O O . ILE B 98 ? 0.1861 0.1681 0.1547 -0.0113 -0.0069 -0.0168 98 ILE B O 3854 C CB . ILE B 98 ? 0.1788 0.1574 0.1436 -0.0011 -0.0028 -0.0024 98 ILE B CB 3855 C CG1 . ILE B 98 ? 0.1787 0.1488 0.1310 0.0041 -0.0062 -0.0121 98 ILE B CG1 3856 C CG2 . ILE B 98 ? 0.1996 0.1656 0.1572 -0.0013 -0.0118 -0.0069 98 ILE B CG2 3857 C CD1 . ILE B 98 ? 0.1778 0.1820 0.1352 -0.0018 -0.0091 -0.0125 98 ILE B CD1 3858 N N . LEU B 99 ? 0.1954 0.1649 0.1549 -0.0141 -0.0005 -0.0064 99 LEU B N 3859 C CA . LEU B 99 ? 0.2220 0.1925 0.1785 -0.0118 -0.0029 -0.0089 99 LEU B CA 3860 C C . LEU B 99 ? 0.2567 0.2109 0.1974 -0.0226 0.0007 -0.0107 99 LEU B C 3861 O O . LEU B 99 ? 0.2781 0.2073 0.1789 -0.0208 -0.0047 -0.0054 99 LEU B O 3862 C CB . LEU B 99 ? 0.2331 0.1883 0.1719 -0.0126 -0.0019 -0.0071 99 LEU B CB 3863 C CG . LEU B 99 ? 0.2170 0.1755 0.1561 0.0010 -0.0041 -0.0215 99 LEU B CG 3864 C CD1 . LEU B 99 ? 0.2373 0.2027 0.1948 0.0167 0.0044 0.0062 99 LEU B CD1 3865 C CD2 . LEU B 99 ? 0.2042 0.2060 0.1901 -0.0012 -0.0097 -0.0194 99 LEU B CD2 3866 N N . PRO B 100 ? 0.2726 0.2274 0.2062 -0.0289 -0.0010 -0.0118 100 PRO B N 3867 C CA . PRO B 100 ? 0.2748 0.2326 0.2183 -0.0235 -0.0046 -0.0131 100 PRO B CA 3868 C C . PRO B 100 ? 0.2779 0.2499 0.2333 -0.0298 -0.0093 -0.0104 100 PRO B C 3869 O O . PRO B 100 ? 0.3378 0.2789 0.2165 -0.0408 -0.0009 -0.0221 100 PRO B O 3870 C CB . PRO B 100 ? 0.2736 0.2474 0.2369 -0.0277 -0.0046 -0.0106 100 PRO B CB 3871 C CG . PRO B 100 ? 0.2779 0.2308 0.2360 -0.0265 0.0080 -0.0073 100 PRO B CG 3872 C CD . PRO B 100 ? 0.2636 0.2322 0.2297 -0.0274 0.0052 -0.0103 100 PRO B CD 3873 N N . ASP B 101 ? 0.2789 0.2474 0.2336 -0.0084 0.0003 -0.0009 101 ASP B N 3874 C CA . ASP B 101 ? 0.2710 0.2303 0.2423 -0.0091 -0.0021 -0.0035 101 ASP B CA 3875 C C . ASP B 101 ? 0.2500 0.2269 0.2243 0.0025 0.0078 0.0012 101 ASP B C 3876 O O . ASP B 101 ? 0.2818 0.2210 0.2191 0.0117 0.0092 -0.0196 101 ASP B O 3877 C CB . ASP B 101 ? 0.2746 0.2286 0.2479 -0.0014 0.0029 -0.0047 101 ASP B CB 3878 C CG . ASP B 101 ? 0.2865 0.2624 0.2487 0.0070 -0.0129 -0.0019 101 ASP B CG 3879 O OD1 . ASP B 101 ? 0.3224 0.2243 0.1784 0.0117 -0.0032 -0.0011 101 ASP B OD1 3880 O OD2 . ASP B 101 ? 0.2990 0.2565 0.2560 -0.0003 -0.0147 0.0116 101 ASP B OD2 3881 N N . GLY B 102 ? 0.2456 0.2030 0.2054 -0.0028 0.0011 -0.0191 102 GLY B N 3882 C CA . GLY B 102 ? 0.2323 0.2037 0.1955 -0.0011 -0.0044 -0.0089 102 GLY B CA 3883 C C . GLY B 102 ? 0.2364 0.1948 0.1773 -0.0033 -0.0068 -0.0064 102 GLY B C 3884 O O . GLY B 102 ? 0.2538 0.2026 0.1957 -0.0012 -0.0182 -0.0089 102 GLY B O 3885 N N . ARG B 103 ? 0.2328 0.1880 0.1771 0.0078 -0.0079 -0.0020 103 ARG B N 3886 C CA . ARG B 103 ? 0.2059 0.1888 0.1729 0.0083 -0.0001 -0.0081 103 ARG B CA 3887 C C . ARG B 103 ? 0.1950 0.1743 0.1423 0.0084 -0.0022 -0.0079 103 ARG B C 3888 O O . ARG B 103 ? 0.2109 0.1518 0.1197 0.0057 -0.0092 -0.0217 103 ARG B O 3889 C CB . ARG B 103 ? 0.2053 0.1891 0.1802 0.0104 -0.0032 -0.0073 103 ARG B CB 3890 C CG . ARG B 103 ? 0.2171 0.2165 0.1954 0.0100 -0.0007 -0.0076 103 ARG B CG 3891 C CD . ARG B 103 ? 0.2313 0.2280 0.2141 0.0126 -0.0046 -0.0088 103 ARG B CD 3892 N NE . ARG B 103 ? 0.2592 0.2651 0.2167 -0.0008 -0.0097 -0.0135 103 ARG B NE 3893 C CZ . ARG B 103 ? 0.2609 0.2431 0.2253 -0.0044 0.0004 -0.0064 103 ARG B CZ 3894 N NH1 . ARG B 103 ? 0.2724 0.2504 0.2280 0.0139 -0.0033 -0.0110 103 ARG B NH1 3895 N NH2 . ARG B 103 ? 0.2755 0.2499 0.2060 0.0000 0.0095 -0.0158 103 ARG B NH2 3896 N N . VAL B 104 ? 0.1703 0.1663 0.1397 0.0162 0.0035 -0.0091 104 VAL B N 3897 C CA . VAL B 104 ? 0.1559 0.1488 0.1399 0.0154 0.0026 -0.0069 104 VAL B CA 3898 C C . VAL B 104 ? 0.1430 0.1341 0.1406 0.0141 0.0093 -0.0093 104 VAL B C 3899 O O . VAL B 104 ? 0.1434 0.1585 0.1460 0.0062 0.0062 0.0033 104 VAL B O 3900 C CB . VAL B 104 ? 0.1652 0.1573 0.1266 0.0074 0.0048 -0.0112 104 VAL B CB 3901 C CG1 . VAL B 104 ? 0.1603 0.1435 0.1379 0.0056 -0.0001 0.0067 104 VAL B CG1 3902 C CG2 . VAL B 104 ? 0.1929 0.1863 0.1372 0.0094 -0.0024 -0.0167 104 VAL B CG2 3903 N N . PRO B 105 ? 0.1410 0.1282 0.1237 0.0183 0.0088 -0.0071 105 PRO B N 3904 C CA . PRO B 105 ? 0.1322 0.1335 0.1322 0.0141 -0.0016 -0.0082 105 PRO B CA 3905 C C . PRO B 105 ? 0.1288 0.1298 0.1092 0.0155 -0.0001 -0.0115 105 PRO B C 3906 O O . PRO B 105 ? 0.1333 0.1479 0.1225 0.0138 -0.0004 -0.0110 105 PRO B O 3907 C CB . PRO B 105 ? 0.1411 0.1295 0.1413 0.0139 -0.0030 -0.0073 105 PRO B CB 3908 C CG . PRO B 105 ? 0.1476 0.1280 0.1305 0.0045 0.0001 -0.0043 105 PRO B CG 3909 C CD . PRO B 105 ? 0.1493 0.1308 0.1261 0.0173 0.0156 -0.0101 105 PRO B CD 3910 N N . SER B 106 ? 0.1215 0.1259 0.1078 0.0090 -0.0086 0.0003 106 SER B N 3911 C CA . SER B 106 ? 0.1168 0.1177 0.1062 0.0052 -0.0036 -0.0057 106 SER B CA 3912 C C . SER B 106 ? 0.1119 0.1093 0.1020 0.0006 -0.0012 -0.0041 106 SER B C 3913 O O . SER B 106 ? 0.1238 0.1054 0.1052 -0.0028 0.0080 0.0016 106 SER B O 3914 C CB . SER B 106 ? 0.1133 0.1119 0.1121 0.0071 -0.0067 -0.0134 106 SER B CB 3915 O OG . SER B 106 ? 0.1197 0.1018 0.1131 -0.0054 -0.0033 0.0048 106 SER B OG 3916 N N . PRO B 107 ? 0.1095 0.0938 0.0998 0.0062 -0.0062 -0.0026 107 PRO B N 3917 C CA . PRO B 107 ? 0.1109 0.1038 0.0943 0.0039 -0.0063 -0.0019 107 PRO B CA 3918 C C . PRO B 107 ? 0.1067 0.1046 0.1091 0.0036 -0.0075 -0.0028 107 PRO B C 3919 O O . PRO B 107 ? 0.1152 0.0990 0.1124 0.0085 -0.0065 -0.0003 107 PRO B O 3920 C CB . PRO B 107 ? 0.1211 0.1129 0.1011 0.0035 -0.0014 0.0041 107 PRO B CB 3921 C CG . PRO B 107 ? 0.1165 0.0870 0.1011 -0.0007 0.0000 -0.0015 107 PRO B CG 3922 C CD . PRO B 107 ? 0.1174 0.1185 0.1019 0.0033 -0.0021 -0.0107 107 PRO B CD 3923 N N . ARG B 108 ? 0.0970 0.1092 0.1058 0.0050 -0.0004 -0.0058 108 ARG B N 3924 C CA . ARG B 108 ? 0.0965 0.1065 0.1051 0.0069 -0.0027 -0.0014 108 ARG B CA 3925 C C . ARG B 108 ? 0.0966 0.1140 0.1006 0.0041 0.0036 -0.0080 108 ARG B C 3926 O O . ARG B 108 ? 0.1071 0.1041 0.1052 0.0092 0.0109 -0.0055 108 ARG B O 3927 C CB . ARG B 108 ? 0.1083 0.1113 0.1004 0.0068 -0.0078 0.0006 108 ARG B CB 3928 C CG . ARG B 108 ? 0.1177 0.1091 0.1014 0.0055 -0.0023 -0.0108 108 ARG B CG 3929 C CD . ARG B 108 ? 0.1211 0.1155 0.1003 0.0034 0.0041 -0.0117 108 ARG B CD 3930 N NE . ARG B 108 ? 0.1061 0.1249 0.1108 -0.0051 0.0086 -0.0138 108 ARG B NE 3931 C CZ . ARG B 108 ? 0.1158 0.1222 0.1043 0.0028 0.0022 0.0117 108 ARG B CZ 3932 N NH1 . ARG B 108 ? 0.1429 0.1237 0.1136 0.0187 0.0036 0.0076 108 ARG B NH1 3933 N NH2 . ARG B 108 ? 0.1161 0.1604 0.1122 0.0088 0.0037 -0.0040 108 ARG B NH2 3934 N N . VAL B 109 ? 0.0947 0.1102 0.0998 0.0055 0.0152 -0.0007 109 VAL B N 3935 C CA . VAL B 109 ? 0.1000 0.1112 0.1051 0.0089 0.0054 0.0001 109 VAL B CA 3936 C C . VAL B 109 ? 0.1073 0.1054 0.1095 0.0023 0.0030 0.0008 109 VAL B C 3937 O O . VAL B 109 ? 0.0944 0.1093 0.1034 0.0024 -0.0039 0.0043 109 VAL B O 3938 C CB . VAL B 109 ? 0.1103 0.1090 0.1151 0.0024 0.0056 0.0005 109 VAL B CB 3939 C CG1 . VAL B 109 ? 0.1035 0.1089 0.1159 0.0018 0.0018 -0.0044 109 VAL B CG1 3940 C CG2 . VAL B 109 ? 0.1229 0.1294 0.1272 0.0049 0.0053 0.0075 109 VAL B CG2 3941 N N . TYR B 110 ? 0.1015 0.1140 0.1007 0.0058 -0.0037 -0.0025 110 TYR B N 3942 C CA . TYR B 110 ? 0.1228 0.1040 0.1017 0.0026 0.0020 -0.0020 110 TYR B CA 3943 C C . TYR B 110 ? 0.1235 0.1099 0.1077 -0.0001 0.0010 -0.0013 110 TYR B C 3944 O O . TYR B 110 ? 0.1354 0.1031 0.1058 0.0076 0.0029 -0.0101 110 TYR B O 3945 C CB . TYR B 110 ? 0.1089 0.0905 0.1053 -0.0022 -0.0016 -0.0019 110 TYR B CB 3946 C CG . TYR B 110 ? 0.1098 0.0964 0.1027 0.0052 0.0035 0.0001 110 TYR B CG 3947 C CD1 . TYR B 110 ? 0.1074 0.1043 0.1206 -0.0022 0.0008 0.0081 110 TYR B CD1 3948 C CD2 . TYR B 110 ? 0.1162 0.0984 0.1009 0.0005 -0.0061 -0.0014 110 TYR B CD2 3949 C CE1 . TYR B 110 ? 0.0967 0.1287 0.1209 -0.0124 -0.0003 0.0038 110 TYR B CE1 3950 C CE2 . TYR B 110 ? 0.0956 0.1208 0.1216 0.0046 0.0037 -0.0037 110 TYR B CE2 3951 C CZ . TYR B 110 ? 0.0986 0.1223 0.1111 -0.0014 0.0129 0.0050 110 TYR B CZ 3952 O OH . TYR B 110 ? 0.1239 0.1167 0.1029 -0.0027 0.0009 0.0044 110 TYR B OH 3953 N N . LEU B 111 ? 0.1270 0.1066 0.1099 -0.0002 0.0057 -0.0036 111 LEU B N 3954 C CA . LEU B 111 ? 0.1208 0.1103 0.1027 0.0023 0.0009 -0.0030 111 LEU B CA 3955 C C . LEU B 111 ? 0.1106 0.1115 0.1064 -0.0009 0.0047 -0.0030 111 LEU B C 3956 O O . LEU B 111 ? 0.1224 0.1102 0.1240 -0.0043 -0.0043 0.0077 111 LEU B O 3957 C CB . LEU B 111 ? 0.1146 0.1188 0.1130 -0.0065 0.0012 -0.0056 111 LEU B CB 3958 C CG . LEU B 111 ? 0.1205 0.1136 0.1121 0.0083 0.0049 0.0091 111 LEU B CG 3959 C CD1 . LEU B 111 ? 0.1334 0.1348 0.1261 -0.0044 0.0019 0.0126 111 LEU B CD1 3960 C CD2 . LEU B 111 ? 0.1280 0.1341 0.1213 -0.0083 0.0071 -0.0034 111 LEU B CD2 3961 N N . LEU B 112 ? 0.1194 0.1210 0.1113 0.0006 -0.0093 0.0000 112 LEU B N 3962 C CA . LEU B 112 ? 0.1163 0.1211 0.1211 0.0052 -0.0007 0.0028 112 LEU B CA 3963 C C . LEU B 112 ? 0.1194 0.1225 0.1303 0.0024 -0.0011 -0.0001 112 LEU B C 3964 O O . LEU B 112 ? 0.1267 0.1197 0.1398 0.0052 -0.0017 -0.0098 112 LEU B O 3965 C CB . LEU B 112 ? 0.1243 0.1181 0.1404 0.0016 0.0011 0.0081 112 LEU B CB 3966 C CG . LEU B 112 ? 0.1244 0.1200 0.1143 0.0108 0.0038 0.0099 112 LEU B CG 3967 C CD1 . LEU B 112 ? 0.1405 0.1259 0.1001 0.0041 -0.0012 0.0030 112 LEU B CD1 3968 C CD2 . LEU B 112 ? 0.1280 0.1364 0.1393 -0.0042 0.0088 0.0142 112 LEU B CD2 3969 N N . ASP B 113 ? 0.1447 0.1394 0.1212 -0.0062 0.0095 0.0033 113 ASP B N 3970 C CA . ASP B 113 ? 0.1384 0.1598 0.1303 -0.0001 0.0077 -0.0019 113 ASP B CA 3971 C C . ASP B 113 ? 0.1316 0.1658 0.1384 -0.0030 0.0107 -0.0048 113 ASP B C 3972 O O . ASP B 113 ? 0.1280 0.1461 0.1336 -0.0009 0.0020 0.0052 113 ASP B O 3973 C CB . ASP B 113 ? 0.1518 0.1646 0.1248 0.0067 -0.0002 -0.0083 113 ASP B CB 3974 C CG . ASP B 113 ? 0.1477 0.1644 0.1397 -0.0107 0.0071 -0.0021 113 ASP B CG 3975 O OD1 . ASP B 113 ? 0.1508 0.1568 0.1448 -0.0192 -0.0012 -0.0004 113 ASP B OD1 3976 O OD2 . ASP B 113 ? 0.1743 0.1872 0.1548 -0.0098 -0.0130 -0.0107 113 ASP B OD2 3977 N N . LYS B 114 ? 0.1636 0.1861 0.1523 0.0052 0.0070 0.0046 114 LYS B N 3978 C CA . LYS B 114 ? 0.1809 0.1938 0.1729 -0.0036 0.0035 0.0032 114 LYS B CA 3979 C C . LYS B 114 ? 0.1853 0.1866 0.1630 -0.0046 -0.0029 0.0083 114 LYS B C 3980 O O . LYS B 114 ? 0.2042 0.1998 0.1946 0.0013 -0.0225 0.0165 114 LYS B O 3981 C CB . LYS B 114 ? 0.1945 0.2147 0.2021 -0.0064 0.0113 0.0109 114 LYS B CB 3982 C CG . LYS B 114 ? 0.2230 0.2660 0.2400 -0.0114 -0.0017 0.0061 114 LYS B CG 3983 C CD . LYS B 114 ? 0.2576 0.2785 0.2324 0.0043 0.0074 -0.0009 114 LYS B CD 3984 C CE . LYS B 114 ? 0.3041 0.3217 0.2645 -0.0018 0.0019 -0.0029 114 LYS B CE 3985 N NZ . LYS B 114 ? 0.3302 0.3650 0.2843 -0.0055 0.0132 0.0155 114 LYS B NZ 3986 N N . THR B 115 ? 0.1647 0.1672 0.1476 -0.0053 0.0070 0.0118 115 THR B N 3987 C CA . THR B 115 ? 0.1673 0.1654 0.1577 -0.0025 -0.0013 0.0054 115 THR B CA 3988 C C . THR B 115 ? 0.1643 0.1632 0.1564 0.0037 -0.0015 0.0010 115 THR B C 3989 O O . THR B 115 ? 0.1734 0.1639 0.1662 0.0013 -0.0022 0.0119 115 THR B O 3990 C CB . THR B 115 ? 0.1568 0.1577 0.1507 0.0046 -0.0042 0.0047 115 THR B CB 3991 O OG1 . THR B 115 ? 0.1534 0.1533 0.1611 -0.0193 -0.0040 -0.0019 115 THR B OG1 3992 C CG2 . THR B 115 ? 0.1750 0.1482 0.1351 0.0043 -0.0125 0.0168 115 THR B CG2 3993 N N . LYS B 116 ? 0.1459 0.1606 0.1461 -0.0025 -0.0009 0.0032 116 LYS B N 3994 C CA . LYS B 116 ? 0.1603 0.1614 0.1518 0.0013 -0.0009 0.0037 116 LYS B CA 3995 C C . LYS B 116 ? 0.1552 0.1654 0.1509 0.0083 -0.0037 0.0048 116 LYS B C 3996 O O . LYS B 116 ? 0.1638 0.1823 0.1405 0.0009 -0.0018 0.0057 116 LYS B O 3997 C CB . LYS B 116 ? 0.1539 0.1599 0.1601 0.0032 -0.0028 0.0049 116 LYS B CB 3998 C CG . LYS B 116 ? 0.1594 0.1704 0.1742 0.0003 -0.0010 0.0115 116 LYS B CG 3999 C CD . LYS B 116 ? 0.1810 0.1825 0.1781 -0.0050 0.0010 0.0025 116 LYS B CD 4000 C CE . LYS B 116 ? 0.1941 0.1853 0.2203 -0.0070 -0.0081 0.0017 116 LYS B CE 4001 N NZ . LYS B 116 ? 0.2460 0.1813 0.2544 -0.0127 -0.0147 0.0112 116 LYS B NZ 4002 N N . ARG B 117 ? 0.1571 0.1560 0.1485 0.0081 0.0078 -0.0017 117 ARG B N 4003 C CA . ARG B 117 ? 0.1568 0.1694 0.1619 0.0004 -0.0046 0.0026 117 ARG B CA 4004 C C . ARG B 117 ? 0.1473 0.1624 0.1466 -0.0013 -0.0043 0.0049 117 ARG B C 4005 O O . ARG B 117 ? 0.1546 0.1580 0.1627 0.0026 -0.0069 0.0167 117 ARG B O 4006 C CB . ARG B 117 ? 0.1835 0.1996 0.1911 0.0102 0.0034 0.0030 117 ARG B CB 4007 C CG . ARG B 117 ? 0.2428 0.2321 0.2466 0.0170 -0.0007 -0.0052 117 ARG B CG 4008 C CD . ARG B 117 ? 0.3232 0.3308 0.3299 0.0014 0.0085 -0.0002 117 ARG B CD 4009 N NE . ARG B 117 ? 0.3520 0.3231 0.3604 0.0175 -0.0031 0.0000 117 ARG B NE 4010 C CZ . ARG B 117 ? 0.3694 0.3647 0.3817 -0.0002 0.0012 -0.0049 117 ARG B CZ 4011 N NH1 . ARG B 117 ? 0.3675 0.3657 0.3775 0.0078 0.0036 0.0016 117 ARG B NH1 4012 N NH2 . ARG B 117 ? 0.3858 0.3575 0.4048 0.0092 -0.0059 -0.0020 117 ARG B NH2 4013 N N . ARG B 118 ? 0.1434 0.1490 0.1431 0.0020 -0.0121 0.0017 118 ARG B N 4014 C CA . ARG B 118 ? 0.1432 0.1544 0.1511 -0.0003 -0.0057 0.0058 118 ARG B CA 4015 C C . ARG B 118 ? 0.1353 0.1372 0.1437 -0.0004 -0.0073 0.0088 118 ARG B C 4016 O O . ARG B 118 ? 0.1431 0.1539 0.1509 -0.0156 -0.0008 0.0325 118 ARG B O 4017 C CB A ARG B 118 ? 0.1589 0.1647 0.1584 -0.0028 -0.0062 0.0039 118 ARG B CB 4018 C CB B ARG B 118 ? 0.1495 0.1574 0.1523 -0.0062 -0.0088 0.0015 118 ARG B CB 4019 C CG A ARG B 118 ? 0.1752 0.1637 0.1585 0.0031 -0.0095 -0.0007 118 ARG B CG 4020 C CG B ARG B 118 ? 0.1468 0.1700 0.1528 -0.0023 -0.0117 -0.0003 118 ARG B CG 4021 C CD A ARG B 118 ? 0.2029 0.1984 0.1729 0.0007 -0.0114 -0.0005 118 ARG B CD 4022 C CD B ARG B 118 ? 0.1682 0.1762 0.1604 -0.0006 0.0003 0.0015 118 ARG B CD 4023 N NE A ARG B 118 ? 0.2172 0.1987 0.1791 0.0016 0.0019 0.0043 118 ARG B NE 4024 N NE B ARG B 118 ? 0.1918 0.1904 0.1867 0.0008 -0.0117 -0.0087 118 ARG B NE 4025 C CZ A ARG B 118 ? 0.2337 0.2134 0.1713 0.0008 0.0030 0.0019 118 ARG B CZ 4026 C CZ B ARG B 118 ? 0.1720 0.1852 0.1701 -0.0088 0.0022 -0.0035 118 ARG B CZ 4027 N NH1 A ARG B 118 ? 0.2517 0.2498 0.2040 0.0048 0.0067 -0.0011 118 ARG B NH1 4028 N NH1 B ARG B 118 ? 0.1669 0.1705 0.1489 -0.0045 0.0113 -0.0139 118 ARG B NH1 4029 N NH2 A ARG B 118 ? 0.2527 0.2207 0.1929 0.0037 0.0031 -0.0097 118 ARG B NH2 4030 N NH2 B ARG B 118 ? 0.1939 0.1827 0.1687 -0.0106 -0.0075 -0.0063 118 ARG B NH2 4031 N N . TYR B 119 ? 0.1287 0.1306 0.1289 -0.0013 0.0010 0.0040 119 TYR B N 4032 C CA . TYR B 119 ? 0.1254 0.1258 0.1196 0.0020 -0.0008 0.0028 119 TYR B CA 4033 C C . TYR B 119 ? 0.1343 0.1148 0.1212 -0.0034 -0.0002 0.0045 119 TYR B C 4034 O O . TYR B 119 ? 0.1466 0.1368 0.1302 0.0015 0.0047 -0.0023 119 TYR B O 4035 C CB . TYR B 119 ? 0.1167 0.1133 0.1143 -0.0034 0.0076 -0.0006 119 TYR B CB 4036 C CG . TYR B 119 ? 0.1191 0.1132 0.1033 0.0008 -0.0005 0.0111 119 TYR B CG 4037 C CD1 . TYR B 119 ? 0.1114 0.1192 0.1210 -0.0069 0.0076 -0.0102 119 TYR B CD1 4038 C CD2 . TYR B 119 ? 0.1127 0.1134 0.1111 -0.0033 0.0005 -0.0021 119 TYR B CD2 4039 C CE1 . TYR B 119 ? 0.0889 0.1019 0.1067 -0.0001 -0.0095 0.0032 119 TYR B CE1 4040 C CE2 . TYR B 119 ? 0.1177 0.1032 0.1122 0.0076 -0.0057 -0.0006 119 TYR B CE2 4041 C CZ . TYR B 119 ? 0.0976 0.0888 0.1039 -0.0057 0.0113 -0.0145 119 TYR B CZ 4042 O OH . TYR B 119 ? 0.1161 0.1253 0.1054 0.0027 0.0039 -0.0080 119 TYR B OH 4043 N N . GLU B 120 ? 0.1288 0.1233 0.1143 0.0009 0.0029 -0.0059 120 GLU B N 4044 C CA . GLU B 120 ? 0.1411 0.1349 0.1159 0.0037 0.0068 0.0004 120 GLU B CA 4045 C C . GLU B 120 ? 0.1465 0.1402 0.1262 0.0029 0.0009 -0.0090 120 GLU B C 4046 O O . GLU B 120 ? 0.2113 0.1517 0.1323 0.0098 -0.0179 -0.0099 120 GLU B O 4047 C CB . GLU B 120 ? 0.1392 0.1383 0.1259 0.0103 0.0146 -0.0029 120 GLU B CB 4048 C CG . GLU B 120 ? 0.1409 0.1483 0.1618 0.0017 0.0146 -0.0213 120 GLU B CG 4049 C CD . GLU B 120 ? 0.1815 0.1716 0.1685 -0.0122 0.0065 -0.0300 120 GLU B CD 4050 O OE1 . GLU B 120 ? 0.1800 0.2024 0.1450 -0.0023 -0.0226 -0.0045 120 GLU B OE1 4051 O OE2 . GLU B 120 ? 0.3190 0.2333 0.1918 -0.0184 0.0619 -0.0412 120 GLU B OE2 4052 N N . MET B 121 ? 0.1475 0.1371 0.1117 0.0024 -0.0015 -0.0091 121 MET B N 4053 C CA . MET B 121 ? 0.1406 0.1371 0.1289 0.0031 0.0017 -0.0009 121 MET B CA 4054 C C . MET B 121 ? 0.1306 0.1399 0.1209 0.0029 0.0039 0.0003 121 MET B C 4055 O O . MET B 121 ? 0.1481 0.1505 0.1441 0.0255 0.0166 -0.0022 121 MET B O 4056 C CB . MET B 121 ? 0.1421 0.1408 0.1252 0.0049 -0.0011 0.0065 121 MET B CB 4057 C CG . MET B 121 ? 0.1418 0.1479 0.1381 -0.0028 0.0007 -0.0004 121 MET B CG 4058 S SD . MET B 121 ? 0.1546 0.1542 0.1483 0.0039 -0.0048 -0.0138 121 MET B SD 4059 C CE . MET B 121 ? 0.1347 0.1336 0.1386 0.0047 -0.0066 -0.0099 121 MET B CE 4060 N N . LEU B 122 ? 0.1340 0.1247 0.1186 0.0038 0.0108 -0.0053 122 LEU B N 4061 C CA . LEU B 122 ? 0.1383 0.1280 0.1295 0.0009 0.0068 -0.0051 122 LEU B CA 4062 C C . LEU B 122 ? 0.1280 0.1198 0.1269 -0.0082 0.0130 -0.0037 122 LEU B C 4063 O O . LEU B 122 ? 0.1348 0.1327 0.1340 -0.0001 0.0229 -0.0028 122 LEU B O 4064 C CB . LEU B 122 ? 0.1408 0.1314 0.1297 0.0000 0.0052 0.0014 122 LEU B CB 4065 C CG . LEU B 122 ? 0.1421 0.1430 0.1310 0.0038 0.0002 -0.0093 122 LEU B CG 4066 C CD1 . LEU B 122 ? 0.1671 0.1856 0.1807 0.0019 -0.0058 -0.0148 122 LEU B CD1 4067 C CD2 . LEU B 122 ? 0.1619 0.1403 0.1478 0.0017 -0.0027 -0.0030 122 LEU B CD2 4068 N N . HIS B 123 ? 0.1342 0.1208 0.1259 -0.0034 0.0150 -0.0092 123 HIS B N 4069 C CA . HIS B 123 ? 0.1439 0.1263 0.1276 0.0037 0.0017 -0.0016 123 HIS B CA 4070 C C . HIS B 123 ? 0.1528 0.1442 0.1358 0.0009 0.0103 -0.0044 123 HIS B C 4071 O O . HIS B 123 ? 0.1711 0.1629 0.1497 0.0137 0.0233 -0.0099 123 HIS B O 4072 C CB . HIS B 123 ? 0.1616 0.1493 0.1338 -0.0011 -0.0053 -0.0099 123 HIS B CB 4073 C CG . HIS B 123 ? 0.1540 0.1516 0.1232 0.0005 -0.0155 -0.0115 123 HIS B CG 4074 N ND1 . HIS B 123 ? 0.1752 0.1792 0.1659 0.0033 0.0002 -0.0070 123 HIS B ND1 4075 C CD2 . HIS B 123 ? 0.1763 0.1521 0.1775 -0.0106 -0.0198 -0.0028 123 HIS B CD2 4076 C CE1 . HIS B 123 ? 0.1685 0.1888 0.1536 0.0011 -0.0094 -0.0084 123 HIS B CE1 4077 N NE2 . HIS B 123 ? 0.2044 0.1792 0.1459 0.0134 -0.0025 -0.0155 123 HIS B NE2 4078 N N . LEU B 124 ? 0.1469 0.1339 0.1299 0.0081 0.0064 -0.0023 124 LEU B N 4079 C CA . LEU B 124 ? 0.1384 0.1354 0.1365 0.0037 0.0060 -0.0084 124 LEU B CA 4080 C C . LEU B 124 ? 0.1371 0.1329 0.1356 0.0038 0.0022 -0.0024 124 LEU B C 4081 O O . LEU B 124 ? 0.1429 0.1305 0.1233 0.0145 0.0150 -0.0184 124 LEU B O 4082 C CB . LEU B 124 ? 0.1244 0.1439 0.1445 0.0033 -0.0029 -0.0099 124 LEU B CB 4083 C CG . LEU B 124 ? 0.1609 0.1644 0.1849 0.0002 -0.0007 -0.0072 124 LEU B CG 4084 C CD1 . LEU B 124 ? 0.1945 0.1853 0.2001 -0.0240 0.0133 -0.0083 124 LEU B CD1 4085 C CD2 . LEU B 124 ? 0.1976 0.1596 0.1650 0.0093 -0.0037 -0.0128 124 LEU B CD2 4086 N N . THR B 125 ? 0.1323 0.1268 0.1396 0.0129 0.0001 -0.0090 125 THR B N 4087 C CA . THR B 125 ? 0.1415 0.1293 0.1412 0.0021 0.0045 -0.0065 125 THR B CA 4088 C C . THR B 125 ? 0.1474 0.1317 0.1471 0.0000 0.0053 -0.0016 125 THR B C 4089 O O . THR B 125 ? 0.1656 0.1435 0.1621 0.0147 0.0089 -0.0020 125 THR B O 4090 C CB . THR B 125 ? 0.1405 0.1391 0.1320 -0.0018 0.0022 -0.0046 125 THR B CB 4091 O OG1 . THR B 125 ? 0.1621 0.1635 0.1730 -0.0011 0.0185 -0.0205 125 THR B OG1 4092 C CG2 . THR B 125 ? 0.1347 0.1440 0.1570 0.0003 -0.0024 -0.0050 125 THR B CG2 4093 N N . GLY B 126 ? 0.1538 0.1391 0.1382 0.0016 0.0159 0.0030 126 GLY B N 4094 C CA . GLY B 126 ? 0.1453 0.1359 0.1297 0.0049 0.0151 -0.0032 126 GLY B CA 4095 C C . GLY B 126 ? 0.1487 0.1505 0.1294 -0.0069 0.0198 -0.0114 126 GLY B C 4096 O O . GLY B 126 ? 0.1790 0.1786 0.1532 -0.0169 0.0441 -0.0235 126 GLY B O 4097 N N . PHE B 127 ? 0.1389 0.1274 0.1362 -0.0054 0.0193 -0.0108 127 PHE B N 4098 C CA . PHE B 127 ? 0.1366 0.1373 0.1366 -0.0032 0.0091 -0.0003 127 PHE B CA 4099 C C . PHE B 127 ? 0.1410 0.1325 0.1388 0.0013 0.0104 -0.0015 127 PHE B C 4100 O O . PHE B 127 ? 0.1615 0.1444 0.1364 -0.0067 0.0025 -0.0055 127 PHE B O 4101 C CB . PHE B 127 ? 0.1492 0.1522 0.1451 0.0009 0.0126 0.0045 127 PHE B CB 4102 C CG . PHE B 127 ? 0.1503 0.1643 0.1438 -0.0114 0.0047 0.0087 127 PHE B CG 4103 C CD1 . PHE B 127 ? 0.1927 0.1862 0.1533 -0.0101 0.0101 0.0016 127 PHE B CD1 4104 C CD2 . PHE B 127 ? 0.1743 0.2234 0.1599 -0.0145 -0.0114 0.0057 127 PHE B CD2 4105 C CE1 . PHE B 127 ? 0.2045 0.2039 0.1503 -0.0016 0.0036 0.0152 127 PHE B CE1 4106 C CE2 . PHE B 127 ? 0.1985 0.2253 0.1585 -0.0160 -0.0071 0.0084 127 PHE B CE2 4107 C CZ . PHE B 127 ? 0.2230 0.2418 0.1537 -0.0058 0.0000 0.0086 127 PHE B CZ 4108 N N . GLU B 128 ? 0.1287 0.1262 0.1227 -0.0025 0.0103 -0.0039 128 GLU B N 4109 C CA . GLU B 128 ? 0.1462 0.1358 0.1387 0.0038 0.0090 -0.0027 128 GLU B CA 4110 C C . GLU B 128 ? 0.1474 0.1291 0.1295 0.0017 0.0051 -0.0042 128 GLU B C 4111 O O . GLU B 128 ? 0.1569 0.1327 0.1184 -0.0058 0.0137 -0.0012 128 GLU B O 4112 C CB . GLU B 128 ? 0.1655 0.1597 0.1698 -0.0019 0.0026 -0.0069 128 GLU B CB 4113 C CG . GLU B 128 ? 0.1666 0.1614 0.1766 0.0037 0.0330 -0.0011 128 GLU B CG 4114 C CD . GLU B 128 ? 0.1526 0.1488 0.1664 -0.0079 0.0221 -0.0086 128 GLU B CD 4115 O OE1 . GLU B 128 ? 0.1724 0.1815 0.1689 0.0090 0.0282 0.0168 128 GLU B OE1 4116 O OE2 . GLU B 128 ? 0.1766 0.1777 0.1522 -0.0070 0.0412 -0.0216 128 GLU B OE2 4117 N N . PHE B 129 ? 0.1351 0.1362 0.1344 0.0018 0.0054 -0.0042 129 PHE B N 4118 C CA . PHE B 129 ? 0.1336 0.1319 0.1393 -0.0024 0.0069 -0.0058 129 PHE B CA 4119 C C . PHE B 129 ? 0.1383 0.1296 0.1187 0.0083 0.0121 -0.0073 129 PHE B C 4120 O O . PHE B 129 ? 0.1491 0.1280 0.1232 0.0039 0.0038 -0.0042 129 PHE B O 4121 C CB . PHE B 129 ? 0.1264 0.1346 0.1402 -0.0044 0.0006 -0.0053 129 PHE B CB 4122 C CG . PHE B 129 ? 0.1073 0.1314 0.1322 -0.0113 0.0063 -0.0057 129 PHE B CG 4123 C CD1 . PHE B 129 ? 0.1317 0.1372 0.1421 0.0029 -0.0071 0.0055 129 PHE B CD1 4124 C CD2 . PHE B 129 ? 0.1100 0.1274 0.1166 -0.0087 0.0035 -0.0057 129 PHE B CD2 4125 C CE1 . PHE B 129 ? 0.1337 0.1487 0.1306 -0.0010 0.0026 -0.0113 129 PHE B CE1 4126 C CE2 . PHE B 129 ? 0.1386 0.1380 0.1318 -0.0025 0.0041 0.0012 129 PHE B CE2 4127 C CZ . PHE B 129 ? 0.1242 0.1312 0.1331 -0.0067 0.0013 -0.0058 129 PHE B CZ 4128 N N . THR B 130 ? 0.1283 0.1398 0.1222 0.0019 0.0124 -0.0060 130 THR B N 4129 C CA . THR B 130 ? 0.1334 0.1370 0.1261 -0.0027 0.0115 -0.0023 130 THR B CA 4130 C C . THR B 130 ? 0.1187 0.1278 0.1216 -0.0089 0.0064 0.0018 130 THR B C 4131 O O . THR B 130 ? 0.1267 0.1382 0.1158 -0.0065 0.0106 0.0023 130 THR B O 4132 C CB . THR B 130 ? 0.1404 0.1453 0.1375 0.0029 0.0094 -0.0080 130 THR B CB 4133 O OG1 . THR B 130 ? 0.1628 0.1528 0.1402 0.0156 0.0150 -0.0105 130 THR B OG1 4134 C CG2 . THR B 130 ? 0.1469 0.1529 0.1164 -0.0042 0.0255 -0.0051 130 THR B CG2 4135 N N . PHE B 131 ? 0.1378 0.1243 0.1141 -0.0043 0.0024 -0.0028 131 PHE B N 4136 C CA . PHE B 131 ? 0.1233 0.1229 0.1221 -0.0015 0.0038 0.0002 131 PHE B CA 4137 C C . PHE B 131 ? 0.1251 0.1311 0.1256 0.0022 0.0088 -0.0003 131 PHE B C 4138 O O . PHE B 131 ? 0.1282 0.1239 0.1235 -0.0020 0.0102 0.0034 131 PHE B O 4139 C CB . PHE B 131 ? 0.1171 0.1055 0.1245 -0.0042 0.0046 -0.0066 131 PHE B CB 4140 C CG . PHE B 131 ? 0.1004 0.1355 0.1244 0.0005 0.0033 -0.0054 131 PHE B CG 4141 C CD1 . PHE B 131 ? 0.1167 0.1200 0.1377 -0.0056 0.0068 -0.0089 131 PHE B CD1 4142 C CD2 . PHE B 131 ? 0.1375 0.1168 0.1303 -0.0014 0.0053 -0.0047 131 PHE B CD2 4143 C CE1 . PHE B 131 ? 0.1241 0.1179 0.1378 0.0002 0.0053 -0.0151 131 PHE B CE1 4144 C CE2 . PHE B 131 ? 0.1207 0.1183 0.1148 -0.0085 0.0029 -0.0024 131 PHE B CE2 4145 C CZ . PHE B 131 ? 0.1084 0.1295 0.1225 -0.0109 0.0033 0.0086 131 PHE B CZ 4146 N N . ASP B 132 ? 0.1274 0.1341 0.1286 -0.0018 0.0050 0.0059 132 ASP B N 4147 C CA . ASP B 132 ? 0.1260 0.1361 0.1276 -0.0049 0.0043 0.0011 132 ASP B CA 4148 C C . ASP B 132 ? 0.1263 0.1350 0.1296 0.0026 0.0028 0.0008 132 ASP B C 4149 O O . ASP B 132 ? 0.1236 0.1382 0.1212 0.0016 0.0062 0.0114 132 ASP B O 4150 C CB . ASP B 132 ? 0.1203 0.1297 0.1396 -0.0102 -0.0009 -0.0092 132 ASP B CB 4151 C CG . ASP B 132 ? 0.1538 0.1611 0.1630 -0.0202 0.0094 0.0029 132 ASP B CG 4152 O OD1 . ASP B 132 ? 0.1392 0.1825 0.1749 -0.0179 0.0413 -0.0035 132 ASP B OD1 4153 O OD2 . ASP B 132 ? 0.1780 0.1815 0.2031 0.0085 0.0316 0.0415 132 ASP B OD2 4154 N N . VAL B 133 ? 0.1294 0.1303 0.1283 -0.0020 0.0034 -0.0070 133 VAL B N 4155 C CA . VAL B 133 ? 0.1240 0.1288 0.1279 -0.0010 0.0012 0.0026 133 VAL B CA 4156 C C . VAL B 133 ? 0.1262 0.1460 0.1401 -0.0007 0.0014 0.0001 133 VAL B C 4157 O O . VAL B 133 ? 0.1212 0.1465 0.1482 0.0122 0.0069 0.0008 133 VAL B O 4158 C CB . VAL B 133 ? 0.1283 0.1292 0.1334 -0.0052 -0.0059 -0.0019 133 VAL B CB 4159 C CG1 . VAL B 133 ? 0.1153 0.1342 0.1401 0.0006 0.0008 -0.0007 133 VAL B CG1 4160 C CG2 . VAL B 133 ? 0.1426 0.1421 0.1464 -0.0044 0.0081 -0.0028 133 VAL B CG2 4161 N N . ASP B 134 ? 0.1322 0.1394 0.1381 -0.0071 0.0018 -0.0022 134 ASP B N 4162 C CA . ASP B 134 ? 0.1258 0.1453 0.1331 -0.0065 0.0058 -0.0024 134 ASP B CA 4163 C C . ASP B 134 ? 0.1247 0.1488 0.1263 -0.0035 0.0053 -0.0065 134 ASP B C 4164 O O . ASP B 134 ? 0.1243 0.1449 0.1401 0.0020 -0.0034 -0.0099 134 ASP B O 4165 C CB . ASP B 134 ? 0.1318 0.1544 0.1255 -0.0130 0.0041 -0.0055 134 ASP B CB 4166 C CG . ASP B 134 ? 0.1882 0.1832 0.1631 -0.0221 -0.0105 -0.0032 134 ASP B CG 4167 O OD1 . ASP B 134 ? 0.1799 0.1687 0.1862 -0.0383 -0.0109 0.0030 134 ASP B OD1 4168 O OD2 . ASP B 134 ? 0.3201 0.2310 0.2464 -0.0686 -0.0255 -0.0085 134 ASP B OD2 4169 N N . ALA B 135 ? 0.1268 0.1487 0.1294 -0.0015 0.0036 -0.0030 135 ALA B N 4170 C CA . ALA B 135 ? 0.1300 0.1398 0.1338 0.0006 -0.0022 -0.0001 135 ALA B CA 4171 C C . ALA B 135 ? 0.1337 0.1399 0.1366 0.0027 -0.0039 0.0006 135 ALA B C 4172 O O . ALA B 135 ? 0.1027 0.1336 0.1306 0.0051 -0.0103 0.0107 135 ALA B O 4173 C CB . ALA B 135 ? 0.1491 0.1381 0.1516 -0.0027 -0.0040 0.0009 135 ALA B CB 4174 N N . THR B 136 ? 0.1383 0.1552 0.1388 -0.0050 -0.0099 0.0003 136 THR B N 4175 C CA . THR B 136 ? 0.1386 0.1566 0.1468 -0.0001 -0.0063 -0.0040 136 THR B CA 4176 C C . THR B 136 ? 0.1415 0.1554 0.1335 0.0031 -0.0064 0.0017 136 THR B C 4177 O O . THR B 136 ? 0.1609 0.1692 0.1353 0.0171 0.0005 0.0053 136 THR B O 4178 C CB . THR B 136 ? 0.1427 0.1732 0.1481 -0.0050 -0.0105 0.0016 136 THR B CB 4179 O OG1 . THR B 136 ? 0.1664 0.1773 0.2026 -0.0117 0.0071 -0.0058 136 THR B OG1 4180 C CG2 . THR B 136 ? 0.1644 0.1924 0.1736 -0.0073 -0.0045 -0.0051 136 THR B CG2 4181 N N . LYS B 137 ? 0.1340 0.1489 0.1343 0.0018 -0.0072 -0.0063 137 LYS B N 4182 C CA . LYS B 137 ? 0.1382 0.1508 0.1356 -0.0012 -0.0082 -0.0050 137 LYS B CA 4183 C C . LYS B 137 ? 0.1254 0.1372 0.1319 0.0073 0.0018 -0.0018 137 LYS B C 4184 O O . LYS B 137 ? 0.1390 0.1357 0.1238 0.0094 0.0079 -0.0107 137 LYS B O 4185 C CB . LYS B 137 ? 0.1407 0.1590 0.1430 0.0085 -0.0049 -0.0068 137 LYS B CB 4186 C CG . LYS B 137 ? 0.1833 0.1912 0.1921 0.0010 0.0052 0.0073 137 LYS B CG 4187 C CD . LYS B 137 ? 0.2295 0.2089 0.2471 -0.0042 -0.0106 0.0043 137 LYS B CD 4188 C CE . LYS B 137 ? 0.3380 0.3113 0.3224 -0.0031 -0.0101 -0.0089 137 LYS B CE 4189 N NZ . LYS B 137 ? 0.3498 0.3975 0.3833 -0.0131 0.0051 0.0105 137 LYS B NZ 4190 N N . LEU B 138 ? 0.1257 0.1228 0.1307 0.0029 -0.0032 -0.0036 138 LEU B N 4191 C CA . LEU B 138 ? 0.1356 0.1270 0.1165 -0.0025 -0.0043 0.0020 138 LEU B CA 4192 C C . LEU B 138 ? 0.1287 0.1143 0.1250 0.0092 -0.0070 -0.0030 138 LEU B C 4193 O O . LEU B 138 ? 0.1378 0.1144 0.1199 0.0156 -0.0128 -0.0072 138 LEU B O 4194 C CB . LEU B 138 ? 0.1328 0.1214 0.1227 0.0020 -0.0062 -0.0063 138 LEU B CB 4195 C CG . LEU B 138 ? 0.1286 0.1201 0.1322 -0.0072 -0.0055 -0.0019 138 LEU B CG 4196 C CD1 . LEU B 138 ? 0.1032 0.1126 0.1346 0.0133 -0.0093 -0.0040 138 LEU B CD1 4197 C CD2 . LEU B 138 ? 0.1375 0.1403 0.1142 -0.0035 0.0029 -0.0105 138 LEU B CD2 4198 N N . PRO B 139 ? 0.1288 0.1084 0.1268 0.0036 -0.0030 -0.0022 139 PRO B N 4199 C CA . PRO B 139 ? 0.1283 0.1294 0.1197 0.0027 0.0022 -0.0008 139 PRO B CA 4200 C C . PRO B 139 ? 0.1420 0.1271 0.1339 0.0027 -0.0074 -0.0016 139 PRO B C 4201 O O . PRO B 139 ? 0.1385 0.1294 0.1189 0.0128 0.0000 0.0027 139 PRO B O 4202 C CB . PRO B 139 ? 0.1420 0.1213 0.1221 0.0027 -0.0061 0.0068 139 PRO B CB 4203 C CG . PRO B 139 ? 0.1353 0.1316 0.1228 0.0160 0.0057 -0.0054 139 PRO B CG 4204 C CD . PRO B 139 ? 0.1282 0.1209 0.1253 0.0020 -0.0037 0.0002 139 PRO B CD 4205 N N . CYS B 140 ? 0.1336 0.1336 0.1248 0.0052 0.0031 -0.0002 140 CYS B N 4206 C CA . CYS B 140 ? 0.1294 0.1308 0.1227 0.0029 -0.0001 0.0000 140 CYS B CA 4207 C C . CYS B 140 ? 0.1347 0.1308 0.1164 0.0071 -0.0065 -0.0014 140 CYS B C 4208 O O . CYS B 140 ? 0.1217 0.1247 0.1237 0.0129 -0.0075 0.0000 140 CYS B O 4209 C CB . CYS B 140 ? 0.1399 0.1447 0.1261 0.0017 0.0020 -0.0024 140 CYS B CB 4210 S SG . CYS B 140 ? 0.1615 0.1646 0.1497 0.0243 -0.0052 0.0205 140 CYS B SG 4211 N N . GLY B 141 ? 0.1151 0.1183 0.1105 0.0008 -0.0075 -0.0018 141 GLY B N 4212 C CA . GLY B 141 ? 0.1265 0.1272 0.1148 0.0041 -0.0020 -0.0032 141 GLY B CA 4213 C C . GLY B 141 ? 0.1265 0.1251 0.1126 0.0000 -0.0027 -0.0065 141 GLY B C 4214 O O . GLY B 141 ? 0.1179 0.1331 0.1238 0.0021 -0.0092 0.0097 141 GLY B O 4215 N N . MET B 142 ? 0.1284 0.1241 0.1150 0.0031 -0.0083 0.0041 142 MET B N 4216 C CA . MET B 142 ? 0.1287 0.1254 0.1128 0.0037 -0.0038 0.0031 142 MET B CA 4217 C C . MET B 142 ? 0.1151 0.1224 0.1161 0.0006 0.0033 0.0036 142 MET B C 4218 O O . MET B 142 ? 0.1180 0.1236 0.1254 0.0164 -0.0095 0.0091 142 MET B O 4219 C CB . MET B 142 ? 0.1195 0.1308 0.1177 -0.0003 -0.0001 0.0095 142 MET B CB 4220 C CG . MET B 142 ? 0.1345 0.1415 0.1187 -0.0005 -0.0112 0.0093 142 MET B CG 4221 S SD . MET B 142 ? 0.1508 0.1309 0.1166 0.0084 -0.0065 -0.0024 142 MET B SD 4222 C CE . MET B 142 ? 0.1224 0.1276 0.1115 -0.0057 -0.0153 0.0082 142 MET B CE 4223 N N . ASN B 143 ? 0.1143 0.1257 0.1158 0.0049 0.0008 0.0048 143 ASN B N 4224 C CA . ASN B 143 ? 0.1074 0.1192 0.1145 0.0076 0.0035 -0.0011 143 ASN B CA 4225 C C . ASN B 143 ? 0.1051 0.1190 0.1120 0.0140 0.0061 -0.0007 143 ASN B C 4226 O O . ASN B 143 ? 0.1115 0.1253 0.1140 0.0161 0.0154 -0.0048 143 ASN B O 4227 C CB . ASN B 143 ? 0.1179 0.1103 0.1198 0.0007 0.0068 0.0048 143 ASN B CB 4228 C CG . ASN B 143 ? 0.1233 0.1196 0.1254 0.0022 0.0016 0.0011 143 ASN B CG 4229 O OD1 . ASN B 143 ? 0.1270 0.1441 0.1245 -0.0100 -0.0025 0.0117 143 ASN B OD1 4230 N ND2 . ASN B 143 ? 0.1115 0.1403 0.1326 -0.0061 0.0127 0.0030 143 ASN B ND2 4231 N N . SER B 144 ? 0.0982 0.1143 0.1030 0.0019 0.0031 -0.0027 144 SER B N 4232 C CA . SER B 144 ? 0.1086 0.1070 0.1079 0.0018 -0.0030 0.0016 144 SER B CA 4233 C C . SER B 144 ? 0.0999 0.0997 0.0958 0.0083 0.0030 0.0025 144 SER B C 4234 O O . SER B 144 ? 0.1099 0.1036 0.1098 0.0198 0.0002 -0.0066 144 SER B O 4235 C CB . SER B 144 ? 0.1089 0.1138 0.1007 0.0019 0.0034 0.0047 144 SER B CB 4236 O OG . SER B 144 ? 0.1053 0.1145 0.1125 0.0029 -0.0107 -0.0214 144 SER B OG 4237 N N . ALA B 145 ? 0.1122 0.1057 0.1010 0.0084 -0.0009 0.0005 145 ALA B N 4238 C CA . ALA B 145 ? 0.0978 0.0982 0.1082 0.0048 -0.0081 0.0000 145 ALA B CA 4239 C C . ALA B 145 ? 0.0941 0.1027 0.0924 0.0040 0.0031 -0.0007 145 ALA B C 4240 O O . ALA B 145 ? 0.1072 0.1142 0.1077 0.0032 -0.0038 -0.0086 145 ALA B O 4241 C CB . ALA B 145 ? 0.1194 0.0969 0.1088 0.0015 0.0013 -0.0089 145 ALA B CB 4242 N N . LEU B 146 ? 0.1010 0.0961 0.1006 0.0018 -0.0041 -0.0016 146 LEU B N 4243 C CA . LEU B 146 ? 0.1067 0.1061 0.1069 0.0009 -0.0015 0.0054 146 LEU B CA 4244 C C . LEU B 146 ? 0.1130 0.1150 0.1096 0.0092 -0.0006 0.0003 146 LEU B C 4245 O O . LEU B 146 ? 0.1097 0.1134 0.0992 0.0088 -0.0035 -0.0045 146 LEU B O 4246 C CB . LEU B 146 ? 0.1081 0.1233 0.1205 0.0048 -0.0066 0.0089 146 LEU B CB 4247 C CG . LEU B 146 ? 0.1084 0.1242 0.1071 0.0042 -0.0001 -0.0029 146 LEU B CG 4248 C CD1 . LEU B 146 ? 0.1112 0.1170 0.1304 0.0146 0.0176 0.0098 146 LEU B CD1 4249 C CD2 . LEU B 146 ? 0.1254 0.1245 0.1191 -0.0019 -0.0002 -0.0067 146 LEU B CD2 4250 N N . TYR B 147 ? 0.1225 0.1133 0.1045 -0.0065 -0.0098 -0.0034 147 TYR B N 4251 C CA . TYR B 147 ? 0.1210 0.1153 0.1108 -0.0033 -0.0037 -0.0025 147 TYR B CA 4252 C C . TYR B 147 ? 0.1105 0.1192 0.1122 -0.0019 -0.0060 -0.0036 147 TYR B C 4253 O O . TYR B 147 ? 0.1259 0.1223 0.1089 -0.0007 -0.0066 0.0045 147 TYR B O 4254 C CB . TYR B 147 ? 0.1181 0.1162 0.1094 -0.0003 0.0013 -0.0084 147 TYR B CB 4255 C CG . TYR B 147 ? 0.1136 0.1046 0.0993 -0.0076 0.0025 -0.0041 147 TYR B CG 4256 C CD1 . TYR B 147 ? 0.1125 0.1218 0.1123 -0.0005 -0.0079 0.0033 147 TYR B CD1 4257 C CD2 . TYR B 147 ? 0.1020 0.0910 0.0953 -0.0012 0.0000 -0.0019 147 TYR B CD2 4258 C CE1 . TYR B 147 ? 0.1186 0.0961 0.0965 -0.0002 -0.0023 0.0075 147 TYR B CE1 4259 C CE2 . TYR B 147 ? 0.0930 0.1088 0.1123 0.0000 -0.0044 0.0000 147 TYR B CE2 4260 C CZ . TYR B 147 ? 0.1076 0.1057 0.0974 0.0099 0.0088 0.0045 147 TYR B CZ 4261 O OH . TYR B 147 ? 0.1039 0.1072 0.1086 0.0054 0.0053 -0.0177 147 TYR B OH 4262 N N . LEU B 148 ? 0.1168 0.1116 0.1212 -0.0022 -0.0017 0.0051 148 LEU B N 4263 C CA . LEU B 148 ? 0.1255 0.1175 0.1115 -0.0014 -0.0024 -0.0045 148 LEU B CA 4264 C C . LEU B 148 ? 0.1178 0.1136 0.1108 0.0044 0.0003 0.0018 148 LEU B C 4265 O O . LEU B 148 ? 0.1034 0.1131 0.1191 0.0126 -0.0020 0.0052 148 LEU B O 4266 C CB . LEU B 148 ? 0.1357 0.1259 0.1167 0.0007 0.0085 -0.0023 148 LEU B CB 4267 C CG . LEU B 148 ? 0.1556 0.1770 0.1223 -0.0078 0.0099 -0.0098 148 LEU B CG 4268 C CD1 . LEU B 148 ? 0.1807 0.1650 0.1786 -0.0049 0.0221 -0.0017 148 LEU B CD1 4269 C CD2 . LEU B 148 ? 0.1801 0.1928 0.1922 0.0151 0.0196 -0.0119 148 LEU B CD2 4270 N N . SER B 149 ? 0.0977 0.1060 0.1159 0.0114 0.0001 0.0008 149 SER B N 4271 C CA . SER B 149 ? 0.1199 0.1238 0.1186 -0.0025 -0.0031 -0.0008 149 SER B CA 4272 C C . SER B 149 ? 0.1144 0.1209 0.1062 -0.0060 -0.0028 0.0012 149 SER B C 4273 O O . SER B 149 ? 0.1120 0.1164 0.1098 -0.0007 -0.0012 0.0015 149 SER B O 4274 C CB . SER B 149 ? 0.1352 0.1452 0.1265 -0.0098 -0.0082 -0.0074 149 SER B CB 4275 O OG . SER B 149 ? 0.1392 0.1873 0.1359 0.0252 -0.0160 -0.0065 149 SER B OG 4276 N N . GLU B 150 ? 0.1177 0.1185 0.1128 -0.0073 0.0011 -0.0011 150 GLU B N 4277 C CA . GLU B 150 ? 0.1293 0.1295 0.1124 -0.0007 -0.0044 -0.0013 150 GLU B CA 4278 C C . GLU B 150 ? 0.1212 0.1338 0.1255 -0.0031 -0.0058 0.0012 150 GLU B C 4279 O O . GLU B 150 ? 0.1208 0.1411 0.1542 -0.0113 -0.0020 -0.0047 150 GLU B O 4280 C CB . GLU B 150 ? 0.1222 0.1259 0.1318 -0.0010 -0.0074 0.0005 150 GLU B CB 4281 C CG . GLU B 150 ? 0.1310 0.1278 0.1316 -0.0060 0.0003 0.0013 150 GLU B CG 4282 C CD . GLU B 150 ? 0.1307 0.1484 0.1078 0.0008 0.0014 -0.0089 150 GLU B CD 4283 O OE1 . GLU B 150 ? 0.1624 0.1515 0.1273 -0.0048 -0.0096 -0.0129 150 GLU B OE1 4284 O OE2 . GLU B 150 ? 0.1586 0.1640 0.1290 -0.0045 -0.0295 -0.0166 150 GLU B OE2 4285 N N . MET B 151 ? 0.1138 0.1281 0.1234 -0.0005 -0.0036 -0.0040 151 MET B N 4286 C CA . MET B 151 ? 0.1189 0.1320 0.1158 0.0015 -0.0017 -0.0018 151 MET B CA 4287 C C . MET B 151 ? 0.1062 0.1314 0.1089 0.0064 -0.0040 -0.0012 151 MET B C 4288 O O . MET B 151 ? 0.1256 0.1405 0.1154 0.0017 -0.0050 -0.0004 151 MET B O 4289 C CB . MET B 151 ? 0.1224 0.1326 0.1255 -0.0038 -0.0003 -0.0018 151 MET B CB 4290 C CG . MET B 151 ? 0.1294 0.1292 0.1193 -0.0111 0.0008 0.0014 151 MET B CG 4291 S SD . MET B 151 ? 0.1321 0.1337 0.1159 -0.0043 -0.0052 -0.0046 151 MET B SD 4292 C CE . MET B 151 ? 0.1343 0.1321 0.1308 -0.0011 -0.0020 -0.0149 151 MET B CE 4293 N N . HIS B 152 ? 0.1104 0.1337 0.1171 0.0041 -0.0071 -0.0031 152 HIS B N 4294 C CA . HIS B 152 ? 0.1151 0.1282 0.1113 -0.0006 -0.0086 -0.0050 152 HIS B CA 4295 C C . HIS B 152 ? 0.1243 0.1260 0.1094 0.0013 -0.0103 -0.0016 152 HIS B C 4296 O O . HIS B 152 ? 0.1357 0.1289 0.1142 -0.0056 -0.0140 -0.0116 152 HIS B O 4297 C CB . HIS B 152 ? 0.1199 0.1301 0.1154 -0.0023 -0.0080 0.0028 152 HIS B CB 4298 C CG . HIS B 152 ? 0.1334 0.1302 0.1141 0.0006 -0.0153 0.0085 152 HIS B CG 4299 N ND1 . HIS B 152 ? 0.1192 0.1399 0.1334 0.0035 -0.0103 -0.0047 152 HIS B ND1 4300 C CD2 . HIS B 152 ? 0.1623 0.1438 0.1473 -0.0031 -0.0111 0.0121 152 HIS B CD2 4301 C CE1 . HIS B 152 ? 0.1680 0.1347 0.1421 0.0032 -0.0381 0.0051 152 HIS B CE1 4302 N NE2 . HIS B 152 ? 0.1743 0.1604 0.1271 -0.0013 -0.0121 0.0136 152 HIS B NE2 4303 N N . PRO B 153 ? 0.1316 0.1320 0.1185 -0.0007 -0.0054 -0.0044 153 PRO B N 4304 C CA . PRO B 153 ? 0.1339 0.1401 0.1278 -0.0040 -0.0047 -0.0045 153 PRO B CA 4305 C C . PRO B 153 ? 0.1358 0.1323 0.1233 -0.0049 -0.0024 -0.0034 153 PRO B C 4306 O O . PRO B 153 ? 0.1357 0.1431 0.1471 -0.0103 -0.0183 -0.0005 153 PRO B O 4307 C CB . PRO B 153 ? 0.1436 0.1574 0.1296 -0.0069 -0.0002 0.0003 153 PRO B CB 4308 C CG . PRO B 153 ? 0.1692 0.1581 0.1471 0.0019 -0.0008 -0.0038 153 PRO B CG 4309 C CD . PRO B 153 ? 0.1392 0.1215 0.1288 0.0012 -0.0093 -0.0092 153 PRO B CD 4310 N N . THR B 154 ? 0.1365 0.1400 0.1219 -0.0044 -0.0117 -0.0083 154 THR B N 4311 C CA . THR B 154 ? 0.1329 0.1449 0.1415 0.0005 -0.0051 -0.0061 154 THR B CA 4312 C C . THR B 154 ? 0.1361 0.1482 0.1496 -0.0035 -0.0077 -0.0091 154 THR B C 4313 O O . THR B 154 ? 0.1627 0.1577 0.1543 0.0154 -0.0184 -0.0272 154 THR B O 4314 C CB . THR B 154 ? 0.1452 0.1420 0.1495 -0.0019 -0.0091 0.0039 154 THR B CB 4315 O OG1 . THR B 154 ? 0.1209 0.1587 0.1397 0.0048 -0.0076 0.0032 154 THR B OG1 4316 C CG2 . THR B 154 ? 0.1381 0.1809 0.1750 -0.0015 -0.0166 0.0091 154 THR B CG2 4317 N N . GLY B 155 ? 0.1371 0.1547 0.1453 -0.0016 -0.0139 -0.0080 155 GLY B N 4318 C CA . GLY B 155 ? 0.1419 0.1572 0.1489 0.0035 -0.0059 -0.0080 155 GLY B CA 4319 C C . GLY B 155 ? 0.1404 0.1522 0.1468 0.0000 -0.0058 -0.0063 155 GLY B C 4320 O O . GLY B 155 ? 0.1298 0.1596 0.1349 0.0068 -0.0117 -0.0001 155 GLY B O 4321 N N . ALA B 156 ? 0.1360 0.1662 0.1414 -0.0018 -0.0141 -0.0113 156 ALA B N 4322 C CA . ALA B 156 ? 0.1386 0.1534 0.1402 -0.0005 -0.0090 -0.0110 156 ALA B CA 4323 C C . ALA B 156 ? 0.1373 0.1613 0.1489 -0.0023 -0.0102 -0.0051 156 ALA B C 4324 O O . ALA B 156 ? 0.1314 0.1743 0.1350 0.0079 -0.0041 -0.0040 156 ALA B O 4325 C CB . ALA B 156 ? 0.1456 0.1500 0.1594 -0.0098 -0.0154 -0.0147 156 ALA B CB 4326 N N . LYS B 157 ? 0.1453 0.1706 0.1474 0.0065 -0.0080 -0.0013 157 LYS B N 4327 C CA . LYS B 157 ? 0.1594 0.1741 0.1576 0.0083 -0.0067 -0.0042 157 LYS B CA 4328 C C . LYS B 157 ? 0.1566 0.1795 0.1615 0.0102 -0.0085 -0.0102 157 LYS B C 4329 O O . LYS B 157 ? 0.1697 0.1769 0.1573 0.0243 -0.0128 -0.0065 157 LYS B O 4330 C CB . LYS B 157 ? 0.1609 0.1705 0.1661 0.0080 -0.0040 -0.0020 157 LYS B CB 4331 C CG . LYS B 157 ? 0.1770 0.1844 0.1707 0.0138 -0.0037 0.0040 157 LYS B CG 4332 C CD . LYS B 157 ? 0.2029 0.1999 0.1998 0.0071 -0.0022 0.0067 157 LYS B CD 4333 C CE . LYS B 157 ? 0.2449 0.2229 0.2495 0.0104 0.0109 0.0190 157 LYS B CE 4334 N NZ . LYS B 157 ? 0.3173 0.3102 0.3253 0.0084 -0.0036 -0.0033 157 LYS B NZ 4335 N N . SER B 158 ? 0.1561 0.1875 0.1506 0.0056 -0.0109 -0.0108 158 SER B N 4336 C CA . SER B 158 ? 0.1740 0.2098 0.1770 0.0071 -0.0111 -0.0122 158 SER B CA 4337 C C . SER B 158 ? 0.1794 0.2117 0.1892 0.0081 -0.0073 -0.0113 158 SER B C 4338 O O . SER B 158 ? 0.1579 0.2159 0.1794 0.0219 -0.0015 -0.0081 158 SER B O 4339 C CB . SER B 158 ? 0.1558 0.2132 0.1719 0.0021 -0.0127 -0.0162 158 SER B CB 4340 O OG . SER B 158 ? 0.1616 0.2544 0.1659 -0.0025 0.0087 -0.0162 158 SER B OG 4341 N N . LYS B 159 ? 0.2080 0.2487 0.2128 0.0041 -0.0140 -0.0055 159 LYS B N 4342 C CA . LYS B 159 ? 0.2319 0.2531 0.2279 0.0075 -0.0056 -0.0049 159 LYS B CA 4343 C C . LYS B 159 ? 0.2000 0.2262 0.2178 0.0046 -0.0082 -0.0051 159 LYS B C 4344 O O . LYS B 159 ? 0.1900 0.2452 0.2150 0.0158 -0.0183 0.0235 159 LYS B O 4345 C CB . LYS B 159 ? 0.2661 0.2925 0.2670 0.0030 -0.0094 -0.0085 159 LYS B CB 4346 C CG . LYS B 159 ? 0.2738 0.3031 0.2890 0.0076 -0.0012 -0.0041 159 LYS B CG 4347 C CD . LYS B 159 ? 0.2784 0.3142 0.3107 0.0032 -0.0133 -0.0055 159 LYS B CD 4348 C CE . LYS B 159 ? 0.3182 0.3577 0.3554 0.0052 0.0043 -0.0084 159 LYS B CE 4349 N NZ . LYS B 159 ? 0.3334 0.3864 0.3775 -0.0104 -0.0206 0.0007 159 LYS B NZ 4350 N N . TYR B 160 ? 0.1771 0.2153 0.2032 0.0093 -0.0106 0.0017 160 TYR B N 4351 C CA . TYR B 160 ? 0.1749 0.2019 0.1950 0.0120 -0.0063 -0.0034 160 TYR B CA 4352 C C . TYR B 160 ? 0.1712 0.1838 0.1788 0.0114 -0.0040 -0.0033 160 TYR B C 4353 O O . TYR B 160 ? 0.1490 0.1751 0.1779 0.0297 -0.0040 -0.0018 160 TYR B O 4354 C CB . TYR B 160 ? 0.1931 0.2188 0.2109 0.0046 -0.0030 0.0016 160 TYR B CB 4355 C CG . TYR B 160 ? 0.2055 0.2478 0.2354 0.0043 -0.0121 -0.0006 160 TYR B CG 4356 C CD1 . TYR B 160 ? 0.1940 0.2632 0.2577 -0.0096 0.0007 0.0045 160 TYR B CD1 4357 C CD2 . TYR B 160 ? 0.2205 0.2702 0.2661 0.0062 -0.0079 0.0000 160 TYR B CD2 4358 C CE1 . TYR B 160 ? 0.2106 0.2698 0.2750 0.0115 -0.0148 0.0053 160 TYR B CE1 4359 C CE2 . TYR B 160 ? 0.2065 0.2731 0.2748 -0.0117 -0.0003 0.0067 160 TYR B CE2 4360 C CZ . TYR B 160 ? 0.2054 0.2743 0.2689 0.0043 -0.0109 0.0031 160 TYR B CZ 4361 O OH . TYR B 160 ? 0.2081 0.3332 0.3150 0.0056 -0.0102 0.0102 160 TYR B OH 4362 N N . ASN B 161 ? 0.1567 0.1735 0.1671 0.0107 -0.0049 -0.0012 161 ASN B N 4363 C CA . ASN B 161 ? 0.1507 0.1595 0.1623 0.0119 -0.0019 -0.0034 161 ASN B CA 4364 C C . ASN B 161 ? 0.1552 0.1642 0.1585 0.0132 -0.0063 -0.0058 161 ASN B C 4365 O O . ASN B 161 ? 0.1496 0.1614 0.1497 0.0235 -0.0032 0.0003 161 ASN B O 4366 C CB . ASN B 161 ? 0.1427 0.1476 0.1455 0.0072 0.0024 -0.0077 161 ASN B CB 4367 C CG . ASN B 161 ? 0.1520 0.1527 0.1355 0.0056 -0.0076 -0.0069 161 ASN B CG 4368 O OD1 . ASN B 161 ? 0.1313 0.1431 0.1275 0.0120 0.0044 -0.0020 161 ASN B OD1 4369 N ND2 . ASN B 161 ? 0.1636 0.1614 0.1313 0.0313 0.0041 0.0107 161 ASN B ND2 4370 N N . PRO B 162 ? 0.1531 0.1613 0.1601 0.0110 -0.0056 -0.0047 162 PRO B N 4371 C CA . PRO B 162 ? 0.1590 0.1663 0.1638 0.0084 -0.0043 -0.0009 162 PRO B CA 4372 C C . PRO B 162 ? 0.1606 0.1749 0.1620 0.0051 -0.0001 0.0056 162 PRO B C 4373 O O . PRO B 162 ? 0.1509 0.1893 0.1647 0.0085 -0.0014 0.0067 162 PRO B O 4374 C CB . PRO B 162 ? 0.1529 0.1655 0.1616 0.0078 -0.0149 0.0034 162 PRO B CB 4375 C CG . PRO B 162 ? 0.1666 0.1787 0.1601 0.0056 -0.0084 -0.0095 162 PRO B CG 4376 C CD . PRO B 162 ? 0.1580 0.1753 0.1621 0.0121 -0.0007 -0.0087 162 PRO B CD 4377 N N . GLY B 163 ? 0.1437 0.1682 0.1470 0.0139 -0.0022 -0.0021 163 GLY B N 4378 C CA . GLY B 163 ? 0.1565 0.1605 0.1564 0.0055 -0.0014 -0.0009 163 GLY B CA 4379 C C . GLY B 163 ? 0.1499 0.1591 0.1449 -0.0017 -0.0046 -0.0032 163 GLY B C 4380 O O . GLY B 163 ? 0.1584 0.1382 0.1403 0.0127 -0.0127 0.0001 163 GLY B O 4381 N N . GLY B 164 ? 0.1427 0.1488 0.1309 0.0035 -0.0075 0.0014 164 GLY B N 4382 C CA . GLY B 164 ? 0.1373 0.1339 0.1260 -0.0047 -0.0033 -0.0007 164 GLY B CA 4383 C C . GLY B 164 ? 0.1273 0.1424 0.1182 -0.0008 0.0055 -0.0052 164 GLY B C 4384 O O . GLY B 164 ? 0.1440 0.1457 0.1186 -0.0041 0.0018 -0.0028 164 GLY B O 4385 N N . ALA B 165 ? 0.1059 0.1304 0.1136 0.0056 -0.0083 -0.0019 165 ALA B N 4386 C CA . ALA B 165 ? 0.1172 0.1269 0.1147 0.0092 -0.0065 0.0024 165 ALA B CA 4387 C C . ALA B 165 ? 0.1090 0.1281 0.1102 0.0029 -0.0106 0.0041 165 ALA B C 4388 O O . ALA B 165 ? 0.1049 0.1239 0.1150 0.0043 -0.0028 0.0000 165 ALA B O 4389 C CB . ALA B 165 ? 0.1184 0.1269 0.1256 -0.0010 -0.0052 -0.0007 165 ALA B CB 4390 N N . TYR B 166 ? 0.1295 0.1290 0.1206 0.0108 -0.0106 -0.0020 166 TYR B N 4391 C CA . TYR B 166 ? 0.1246 0.1245 0.1208 0.0063 -0.0068 0.0080 166 TYR B CA 4392 C C . TYR B 166 ? 0.1212 0.1232 0.1348 0.0106 -0.0035 -0.0032 166 TYR B C 4393 O O . TYR B 166 ? 0.1239 0.1330 0.1255 -0.0041 0.0125 -0.0072 166 TYR B O 4394 C CB . TYR B 166 ? 0.1449 0.1363 0.1452 0.0133 -0.0046 0.0109 166 TYR B CB 4395 C CG . TYR B 166 ? 0.1483 0.1583 0.1558 0.0120 -0.0126 0.0090 166 TYR B CG 4396 C CD1 . TYR B 166 ? 0.1454 0.1632 0.1724 -0.0044 -0.0075 0.0121 166 TYR B CD1 4397 C CD2 . TYR B 166 ? 0.1447 0.1316 0.1670 0.0067 -0.0084 0.0110 166 TYR B CD2 4398 C CE1 . TYR B 166 ? 0.1874 0.1579 0.1919 0.0125 0.0070 0.0266 166 TYR B CE1 4399 C CE2 . TYR B 166 ? 0.1676 0.1504 0.1696 0.0020 -0.0026 -0.0092 166 TYR B CE2 4400 C CZ . TYR B 166 ? 0.1531 0.1441 0.2067 -0.0105 -0.0077 0.0124 166 TYR B CZ 4401 O OH . TYR B 166 ? 0.2386 0.1652 0.2801 -0.0020 -0.0176 0.0244 166 TYR B OH 4402 N N . TYR B 167 ? 0.1145 0.1233 0.1182 0.0086 0.0003 -0.0019 167 TYR B N 4403 C CA . TYR B 167 ? 0.1293 0.1290 0.1194 0.0075 -0.0028 0.0013 167 TYR B CA 4404 C C . TYR B 167 ? 0.1312 0.1179 0.1095 0.0062 -0.0022 -0.0013 167 TYR B C 4405 O O . TYR B 167 ? 0.1330 0.1345 0.1204 0.0147 0.0085 0.0050 167 TYR B O 4406 C CB . TYR B 167 ? 0.1363 0.1420 0.1321 0.0103 0.0040 -0.0016 167 TYR B CB 4407 C CG . TYR B 167 ? 0.1381 0.1447 0.1503 0.0051 -0.0074 -0.0024 167 TYR B CG 4408 C CD1 . TYR B 167 ? 0.1578 0.1536 0.1557 0.0025 -0.0093 -0.0035 167 TYR B CD1 4409 C CD2 . TYR B 167 ? 0.1631 0.1641 0.1629 0.0201 -0.0248 0.0019 167 TYR B CD2 4410 C CE1 . TYR B 167 ? 0.1559 0.1580 0.1609 0.0231 -0.0072 0.0022 167 TYR B CE1 4411 C CE2 . TYR B 167 ? 0.1676 0.1411 0.1733 0.0146 -0.0075 -0.0233 167 TYR B CE2 4412 C CZ . TYR B 167 ? 0.1494 0.1429 0.1852 0.0021 0.0049 0.0055 167 TYR B CZ 4413 O OH . TYR B 167 ? 0.1839 0.1528 0.2277 0.0151 0.0065 0.0184 167 TYR B OH 4414 N N . GLY B 168 ? 0.1111 0.1180 0.1042 0.0088 -0.0101 -0.0006 168 GLY B N 4415 C CA . GLY B 168 ? 0.1083 0.1221 0.1045 0.0000 -0.0017 0.0076 168 GLY B CA 4416 C C . GLY B 168 ? 0.1074 0.1152 0.1059 0.0001 -0.0009 0.0083 168 GLY B C 4417 O O . GLY B 168 ? 0.1215 0.1036 0.1099 0.0082 -0.0022 0.0099 168 GLY B O 4418 N N . THR B 169 ? 0.1083 0.1218 0.1036 0.0048 -0.0017 0.0023 169 THR B N 4419 C CA . THR B 169 ? 0.1179 0.1163 0.1076 0.0030 -0.0004 0.0037 169 THR B CA 4420 C C . THR B 169 ? 0.1154 0.1173 0.1111 0.0063 -0.0019 0.0006 169 THR B C 4421 O O . THR B 169 ? 0.1091 0.1188 0.1137 0.0022 0.0039 0.0001 169 THR B O 4422 C CB . THR B 169 ? 0.1123 0.1324 0.1175 -0.0002 0.0042 0.0062 169 THR B CB 4423 O OG1 . THR B 169 ? 0.0956 0.1592 0.1068 0.0176 0.0007 0.0049 169 THR B OG1 4424 C CG2 . THR B 169 ? 0.1108 0.1453 0.1072 -0.0105 0.0104 0.0099 169 THR B CG2 4425 N N . GLY B 170 ? 0.1163 0.1243 0.1058 0.0004 -0.0003 0.0011 170 GLY B N 4426 C CA . GLY B 170 ? 0.1195 0.1189 0.1133 0.0018 -0.0059 0.0031 170 GLY B CA 4427 C C . GLY B 170 ? 0.1076 0.1046 0.1133 0.0001 0.0008 0.0044 170 GLY B C 4428 O O . GLY B 170 ? 0.1223 0.1176 0.1176 0.0035 0.0015 0.0000 170 GLY B O 4429 N N . TYR B 171 ? 0.1113 0.0997 0.1047 -0.0012 -0.0041 0.0028 171 TYR B N 4430 C CA . TYR B 171 ? 0.1110 0.1110 0.1133 0.0012 -0.0004 -0.0027 171 TYR B CA 4431 C C . TYR B 171 ? 0.1156 0.1187 0.1074 -0.0004 -0.0019 0.0018 171 TYR B C 4432 O O . TYR B 171 ? 0.1061 0.1147 0.1148 -0.0008 -0.0069 0.0073 171 TYR B O 4433 C CB . TYR B 171 ? 0.1165 0.1158 0.1130 -0.0016 -0.0031 0.0038 171 TYR B CB 4434 C CG . TYR B 171 ? 0.1114 0.1039 0.1098 0.0093 0.0006 -0.0015 171 TYR B CG 4435 C CD1 . TYR B 171 ? 0.1012 0.1228 0.1196 -0.0070 0.0064 0.0211 171 TYR B CD1 4436 C CD2 . TYR B 171 ? 0.0893 0.1218 0.1144 0.0091 0.0080 0.0001 171 TYR B CD2 4437 C CE1 . TYR B 171 ? 0.1039 0.1040 0.1068 -0.0022 0.0065 0.0069 171 TYR B CE1 4438 C CE2 . TYR B 171 ? 0.1034 0.0983 0.1096 -0.0024 0.0025 -0.0013 171 TYR B CE2 4439 C CZ . TYR B 171 ? 0.1113 0.1077 0.1113 -0.0023 -0.0036 0.0031 171 TYR B CZ 4440 O OH . TYR B 171 ? 0.1166 0.1165 0.1190 0.0023 -0.0061 0.0094 171 TYR B OH 4441 N N . CYS B 172 ? 0.1135 0.1163 0.1116 -0.0030 0.0082 -0.0020 172 CYS B N 4442 C CA . CYS B 172 ? 0.1099 0.1148 0.1124 -0.0017 0.0047 0.0037 172 CYS B CA 4443 C C . CYS B 172 ? 0.1158 0.1075 0.1089 -0.0006 -0.0010 0.0003 172 CYS B C 4444 O O . CYS B 172 ? 0.1190 0.1094 0.1202 0.0048 0.0106 0.0014 172 CYS B O 4445 C CB . CYS B 172 ? 0.1292 0.1083 0.1253 -0.0119 0.0016 0.0049 172 CYS B CB 4446 S SG . CYS B 172 ? 0.1392 0.1265 0.1244 -0.0089 -0.0101 -0.0019 172 CYS B SG 4447 N N . ASP B 173 ? 0.1180 0.1173 0.1111 0.0055 0.0038 -0.0044 173 ASP B N 4448 C CA . ASP B 173 ? 0.1232 0.1200 0.1183 0.0027 -0.0069 0.0011 173 ASP B CA 4449 C C . ASP B 173 ? 0.1100 0.1264 0.1264 -0.0005 -0.0001 0.0007 173 ASP B C 4450 O O . ASP B 173 ? 0.0974 0.1297 0.1324 0.0039 -0.0084 0.0075 173 ASP B O 4451 C CB . ASP B 173 ? 0.1169 0.1222 0.1124 0.0031 0.0067 0.0028 173 ASP B CB 4452 C CG . ASP B 173 ? 0.1254 0.1222 0.1195 0.0029 -0.0021 -0.0022 173 ASP B CG 4453 O OD1 . ASP B 173 ? 0.1030 0.1300 0.1330 0.0044 -0.0010 0.0062 173 ASP B OD1 4454 O OD2 . ASP B 173 ? 0.1126 0.1274 0.1259 -0.0066 0.0008 0.0048 173 ASP B OD2 4455 N N . ALA B 174 ? 0.1166 0.1176 0.1200 0.0004 -0.0071 0.0103 174 ALA B N 4456 C CA . ALA B 174 ? 0.1238 0.1144 0.1288 0.0032 0.0017 0.0050 174 ALA B CA 4457 C C . ALA B 174 ? 0.1139 0.1168 0.1310 -0.0002 0.0052 0.0023 174 ALA B C 4458 O O . ALA B 174 ? 0.1354 0.1365 0.1327 -0.0124 0.0015 0.0134 174 ALA B O 4459 C CB . ALA B 174 ? 0.1341 0.1167 0.1377 0.0064 -0.0018 0.0148 174 ALA B CB 4460 N N . GLN B 175 ? 0.1098 0.1223 0.1192 -0.0078 0.0027 0.0063 175 GLN B N 4461 C CA . GLN B 175 ? 0.1249 0.1293 0.1272 0.0023 0.0041 0.0095 175 GLN B CA 4462 C C . GLN B 175 ? 0.1118 0.1246 0.1197 -0.0107 0.0026 0.0087 175 GLN B C 4463 O O . GLN B 175 ? 0.1360 0.1377 0.1273 -0.0064 0.0058 0.0110 175 GLN B O 4464 C CB . GLN B 175 ? 0.1268 0.1296 0.1393 0.0015 0.0075 0.0084 175 GLN B CB 4465 C CG . GLN B 175 ? 0.1240 0.1496 0.1492 0.0015 0.0075 0.0023 175 GLN B CG 4466 C CD . GLN B 175 ? 0.1467 0.1521 0.1485 -0.0127 -0.0066 0.0016 175 GLN B CD 4467 O OE1 . GLN B 175 ? 0.1654 0.1892 0.1765 -0.0254 0.0077 0.0236 175 GLN B OE1 4468 N NE2 . GLN B 175 ? 0.1361 0.1720 0.1863 -0.0014 -0.0049 0.0027 175 GLN B NE2 4469 N N . CYS B 176 ? 0.1071 0.1287 0.1210 -0.0061 0.0079 0.0179 176 CYS B N 4470 C CA . CYS B 176 ? 0.1115 0.1279 0.1402 -0.0006 0.0031 0.0051 176 CYS B CA 4471 C C . CYS B 176 ? 0.1232 0.1413 0.1410 -0.0095 0.0041 0.0006 176 CYS B C 4472 O O . CYS B 176 ? 0.1169 0.1546 0.1553 -0.0025 0.0179 0.0150 176 CYS B O 4473 C CB . CYS B 176 ? 0.1084 0.1301 0.1487 -0.0032 0.0129 0.0095 176 CYS B CB 4474 S SG . CYS B 176 ? 0.1312 0.1365 0.1677 -0.0095 -0.0010 0.0115 176 CYS B SG 4475 N N . PHE B 177 ? 0.1222 0.1309 0.1350 -0.0050 0.0038 -0.0001 177 PHE B N 4476 C CA . PHE B 177 ? 0.1222 0.1318 0.1324 0.0052 0.0048 0.0032 177 PHE B CA 4477 C C . PHE B 177 ? 0.1232 0.1387 0.1290 0.0064 0.0040 0.0021 177 PHE B C 4478 O O . PHE B 177 ? 0.1270 0.1503 0.1251 0.0114 0.0099 -0.0008 177 PHE B O 4479 C CB . PHE B 177 ? 0.1386 0.1449 0.1405 0.0003 0.0010 -0.0018 177 PHE B CB 4480 C CG . PHE B 177 ? 0.1335 0.1438 0.1318 -0.0006 0.0043 0.0053 177 PHE B CG 4481 C CD1 . PHE B 177 ? 0.1469 0.1780 0.1441 -0.0059 0.0106 0.0166 177 PHE B CD1 4482 C CD2 . PHE B 177 ? 0.1493 0.1429 0.1268 -0.0033 -0.0023 -0.0107 177 PHE B CD2 4483 C CE1 . PHE B 177 ? 0.1669 0.1773 0.1484 -0.0030 0.0048 0.0263 177 PHE B CE1 4484 C CE2 . PHE B 177 ? 0.1510 0.1599 0.1405 -0.0068 -0.0033 -0.0080 177 PHE B CE2 4485 C CZ . PHE B 177 ? 0.1427 0.1861 0.1677 0.0033 -0.0107 0.0069 177 PHE B CZ 4486 N N . VAL B 178 ? 0.1316 0.1363 0.1351 0.0115 0.0047 0.0088 178 VAL B N 4487 C CA . VAL B 178 ? 0.1322 0.1476 0.1398 0.0102 0.0045 0.0053 178 VAL B CA 4488 C C . VAL B 178 ? 0.1171 0.1554 0.1388 0.0080 0.0057 0.0045 178 VAL B C 4489 O O . VAL B 178 ? 0.1324 0.1589 0.1528 0.0147 0.0125 -0.0008 178 VAL B O 4490 C CB . VAL B 178 ? 0.1368 0.1492 0.1448 0.0108 0.0015 0.0104 178 VAL B CB 4491 C CG1 . VAL B 178 ? 0.1217 0.1667 0.1797 0.0129 0.0087 -0.0013 178 VAL B CG1 4492 C CG2 . VAL B 178 ? 0.1440 0.1548 0.1651 -0.0040 0.0085 0.0088 178 VAL B CG2 4493 N N . THR B 179 ? 0.1271 0.1560 0.1491 0.0056 0.0026 0.0105 179 THR B N 4494 C CA . THR B 179 ? 0.1315 0.1464 0.1453 -0.0007 0.0012 0.0030 179 THR B CA 4495 C C . THR B 179 ? 0.1350 0.1446 0.1472 0.0010 0.0062 -0.0008 179 THR B C 4496 O O . THR B 179 ? 0.1305 0.1505 0.1555 -0.0009 0.0029 -0.0065 179 THR B O 4497 C CB . THR B 179 ? 0.1311 0.1447 0.1455 0.0057 0.0077 0.0024 179 THR B CB 4498 O OG1 . THR B 179 ? 0.1284 0.1460 0.1476 -0.0060 0.0082 0.0070 179 THR B OG1 4499 C CG2 . THR B 179 ? 0.1416 0.1746 0.1505 0.0151 0.0036 0.0050 179 THR B CG2 4500 N N . PRO B 180 ? 0.1266 0.1507 0.1313 0.0014 0.0089 -0.0051 180 PRO B N 4501 C CA . PRO B 180 ? 0.1322 0.1587 0.1421 0.0058 0.0030 0.0017 180 PRO B CA 4502 C C . PRO B 180 ? 0.1313 0.1555 0.1330 0.0112 0.0044 0.0008 180 PRO B C 4503 O O . PRO B 180 ? 0.1281 0.1683 0.1545 0.0080 0.0054 -0.0035 180 PRO B O 4504 C CB . PRO B 180 ? 0.1654 0.1779 0.1417 0.0094 0.0020 -0.0017 180 PRO B CB 4505 C CG . PRO B 180 ? 0.1501 0.1628 0.1441 0.0058 0.0183 0.0003 180 PRO B CG 4506 C CD . PRO B 180 ? 0.1278 0.1535 0.1374 -0.0016 0.0106 -0.0021 180 PRO B CD 4507 N N . PHE B 181 ? 0.1201 0.1521 0.1285 0.0035 0.0053 0.0019 181 PHE B N 4508 C CA . PHE B 181 ? 0.1276 0.1419 0.1341 0.0063 0.0057 0.0002 181 PHE B CA 4509 C C . PHE B 181 ? 0.1168 0.1314 0.1332 0.0087 0.0014 -0.0028 181 PHE B C 4510 O O . PHE B 181 ? 0.1050 0.1543 0.1354 -0.0031 -0.0027 0.0022 181 PHE B O 4511 C CB . PHE B 181 ? 0.1264 0.1478 0.1313 0.0041 0.0118 0.0005 181 PHE B CB 4512 C CG . PHE B 181 ? 0.1205 0.1388 0.1400 -0.0004 -0.0009 0.0069 181 PHE B CG 4513 C CD1 . PHE B 181 ? 0.1367 0.1654 0.1473 0.0132 0.0009 -0.0010 181 PHE B CD1 4514 C CD2 . PHE B 181 ? 0.1210 0.1469 0.1441 0.0122 0.0014 -0.0019 181 PHE B CD2 4515 C CE1 . PHE B 181 ? 0.1464 0.1590 0.1517 -0.0016 0.0178 -0.0079 181 PHE B CE1 4516 C CE2 . PHE B 181 ? 0.1492 0.1622 0.1767 0.0226 -0.0043 0.0007 181 PHE B CE2 4517 C CZ . PHE B 181 ? 0.1257 0.1590 0.1726 0.0126 0.0240 -0.0030 181 PHE B CZ 4518 N N . ILE B 182 ? 0.1177 0.1402 0.1297 0.0000 0.0037 0.0012 182 ILE B N 4519 C CA . ILE B 182 ? 0.1216 0.1420 0.1461 0.0058 0.0037 0.0000 182 ILE B CA 4520 C C . ILE B 182 ? 0.1208 0.1504 0.1466 0.0046 0.0047 0.0023 182 ILE B C 4521 O O . ILE B 182 ? 0.1099 0.1562 0.1540 0.0169 0.0082 0.0026 182 ILE B O 4522 C CB . ILE B 182 ? 0.1300 0.1524 0.1423 0.0028 0.0076 0.0045 182 ILE B CB 4523 C CG1 . ILE B 182 ? 0.1394 0.1454 0.1522 0.0030 0.0013 0.0087 182 ILE B CG1 4524 C CG2 . ILE B 182 ? 0.1440 0.1274 0.1597 0.0033 -0.0083 -0.0051 182 ILE B CG2 4525 C CD1 . ILE B 182 ? 0.1516 0.1551 0.1644 0.0104 0.0010 0.0095 182 ILE B CD1 4526 N N . ASN B 183 ? 0.1145 0.1413 0.1273 -0.0006 0.0087 -0.0003 183 ASN B N 4527 C CA . ASN B 183 ? 0.1235 0.1421 0.1329 0.0031 -0.0007 0.0010 183 ASN B CA 4528 C C . ASN B 183 ? 0.1248 0.1398 0.1298 0.0040 0.0001 -0.0055 183 ASN B C 4529 O O . ASN B 183 ? 0.1436 0.1500 0.1337 0.0143 -0.0029 -0.0120 183 ASN B O 4530 C CB . ASN B 183 ? 0.1412 0.1578 0.1381 0.0122 -0.0048 0.0053 183 ASN B CB 4531 C CG . ASN B 183 ? 0.1292 0.1548 0.1523 0.0064 -0.0001 0.0078 183 ASN B CG 4532 O OD1 . ASN B 183 ? 0.1443 0.1837 0.1531 0.0186 0.0001 -0.0105 183 ASN B OD1 4533 N ND2 . ASN B 183 ? 0.2123 0.1613 0.1738 0.0129 -0.0332 0.0029 183 ASN B ND2 4534 N N . GLY B 184 ? 0.1306 0.1434 0.1375 0.0066 -0.0002 -0.0084 184 GLY B N 4535 C CA . GLY B 184 ? 0.1261 0.1396 0.1342 0.0011 -0.0013 0.0023 184 GLY B CA 4536 C C . GLY B 184 ? 0.1321 0.1418 0.1376 0.0111 -0.0050 -0.0001 184 GLY B C 4537 O O . GLY B 184 ? 0.1414 0.1474 0.1696 0.0203 -0.0012 0.0060 184 GLY B O 4538 N N . LEU B 185 ? 0.1182 0.1513 0.1399 0.0071 -0.0005 0.0006 185 LEU B N 4539 C CA . LEU B 185 ? 0.1262 0.1553 0.1469 0.0060 0.0020 -0.0001 185 LEU B CA 4540 C C . LEU B 185 ? 0.1320 0.1629 0.1496 0.0052 -0.0007 0.0003 185 LEU B C 4541 O O . LEU B 185 ? 0.1335 0.1466 0.1399 -0.0004 -0.0035 0.0053 185 LEU B O 4542 C CB . LEU B 185 ? 0.1139 0.1600 0.1661 0.0152 -0.0040 -0.0052 185 LEU B CB 4543 C CG . LEU B 185 ? 0.1576 0.1792 0.1756 0.0064 -0.0097 -0.0050 185 LEU B CG 4544 C CD1 . LEU B 185 ? 0.1830 0.1996 0.1976 0.0017 -0.0063 -0.0078 185 LEU B CD1 4545 C CD2 . LEU B 185 ? 0.1852 0.2008 0.1873 0.0067 -0.0123 -0.0011 185 LEU B CD2 4546 N N . GLY B 186 ? 0.1246 0.1650 0.1518 0.0118 0.0023 0.0041 186 GLY B N 4547 C CA . GLY B 186 ? 0.1412 0.1696 0.1577 0.0043 0.0044 -0.0004 186 GLY B CA 4548 C C . GLY B 186 ? 0.1386 0.1673 0.1656 0.0079 0.0084 0.0006 186 GLY B C 4549 O O . GLY B 186 ? 0.1524 0.1821 0.1860 0.0041 -0.0001 0.0042 186 GLY B O 4550 N N . ASN B 187 ? 0.1304 0.1688 0.1588 0.0049 0.0048 -0.0048 187 ASN B N 4551 C CA . ASN B 187 ? 0.1465 0.1746 0.1697 0.0044 0.0037 0.0024 187 ASN B CA 4552 C C . ASN B 187 ? 0.1631 0.1805 0.1728 -0.0002 0.0021 0.0003 187 ASN B C 4553 O O . ASN B 187 ? 0.1349 0.1705 0.1685 -0.0042 0.0180 0.0162 187 ASN B O 4554 C CB . ASN B 187 ? 0.1403 0.1661 0.1582 0.0031 -0.0053 0.0031 187 ASN B CB 4555 C CG . ASN B 187 ? 0.1482 0.1703 0.1800 0.0046 0.0051 -0.0031 187 ASN B CG 4556 O OD1 . ASN B 187 ? 0.1372 0.1709 0.1860 -0.0052 0.0073 0.0036 187 ASN B OD1 4557 N ND2 . ASN B 187 ? 0.1310 0.1808 0.1683 -0.0181 0.0005 0.0036 187 ASN B ND2 4558 N N . ILE B 188 ? 0.1630 0.1984 0.1863 0.0071 0.0064 0.0082 188 ILE B N 4559 C CA . ILE B 188 ? 0.1713 0.2010 0.1991 0.0046 0.0076 0.0061 188 ILE B CA 4560 C C . ILE B 188 ? 0.1764 0.1967 0.2037 0.0060 0.0098 0.0054 188 ILE B C 4561 O O . ILE B 188 ? 0.1854 0.2128 0.2268 0.0169 0.0223 0.0202 188 ILE B O 4562 C CB . ILE B 188 ? 0.1805 0.2123 0.1972 0.0007 0.0011 0.0062 188 ILE B CB 4563 C CG1 . ILE B 188 ? 0.1807 0.2044 0.2154 0.0030 -0.0017 0.0010 188 ILE B CG1 4564 C CG2 . ILE B 188 ? 0.1904 0.2250 0.2330 -0.0018 0.0086 0.0014 188 ILE B CG2 4565 C CD1 . ILE B 188 ? 0.1891 0.2129 0.2312 0.0090 0.0008 0.0036 188 ILE B CD1 4566 N N . GLU B 189 ? 0.1700 0.1970 0.2196 0.0037 0.0078 0.0092 189 GLU B N 4567 C CA . GLU B 189 ? 0.1925 0.2112 0.2290 0.0002 0.0100 0.0109 189 GLU B CA 4568 C C . GLU B 189 ? 0.1808 0.1923 0.2275 0.0028 0.0133 0.0097 189 GLU B C 4569 O O . GLU B 189 ? 0.1701 0.1988 0.2509 0.0033 0.0352 0.0281 189 GLU B O 4570 C CB . GLU B 189 ? 0.2103 0.2256 0.2420 0.0000 0.0068 0.0097 189 GLU B CB 4571 C CG . GLU B 189 ? 0.2448 0.2605 0.2806 0.0033 -0.0091 0.0093 189 GLU B CG 4572 C CD . GLU B 189 ? 0.2818 0.2934 0.2964 -0.0053 -0.0106 -0.0006 189 GLU B CD 4573 O OE1 . GLU B 189 ? 0.3985 0.3569 0.4099 0.0142 -0.0149 0.0151 189 GLU B OE1 4574 O OE2 . GLU B 189 ? 0.4124 0.3700 0.3673 -0.0016 -0.0210 0.0142 189 GLU B OE2 4575 N N . GLY B 190 ? 0.1710 0.1823 0.2113 0.0002 0.0240 0.0052 190 GLY B N 4576 C CA . GLY B 190 ? 0.1687 0.1835 0.1954 -0.0013 0.0163 0.0041 190 GLY B CA 4577 C C . GLY B 190 ? 0.1656 0.1812 0.1970 -0.0055 0.0085 0.0063 190 GLY B C 4578 O O . GLY B 190 ? 0.1413 0.2007 0.1978 -0.0070 0.0205 0.0292 190 GLY B O 4579 N N . LYS B 191 ? 0.1401 0.1642 0.1839 0.0030 0.0027 0.0006 191 LYS B N 4580 C CA . LYS B 191 ? 0.1451 0.1789 0.1887 -0.0030 0.0090 0.0000 191 LYS B CA 4581 C C . LYS B 191 ? 0.1465 0.1538 0.1724 -0.0065 0.0073 0.0021 191 LYS B C 4582 O O . LYS B 191 ? 0.1436 0.1475 0.1694 0.0009 0.0125 0.0092 191 LYS B O 4583 C CB . LYS B 191 ? 0.1561 0.1925 0.2028 0.0018 0.0076 -0.0065 191 LYS B CB 4584 C CG . LYS B 191 ? 0.1591 0.2414 0.2453 0.0058 0.0053 -0.0058 191 LYS B CG 4585 C CD . LYS B 191 ? 0.1808 0.2448 0.2509 -0.0074 -0.0029 -0.0042 191 LYS B CD 4586 C CE . LYS B 191 ? 0.1772 0.2630 0.2726 -0.0045 0.0026 -0.0146 191 LYS B CE 4587 N NZ . LYS B 191 ? 0.2459 0.3355 0.3098 -0.0219 -0.0133 -0.0125 191 LYS B NZ 4588 N N . GLY B 192 ? 0.1354 0.1493 0.1632 -0.0036 0.0085 0.0135 192 GLY B N 4589 C CA . GLY B 192 ? 0.1350 0.1492 0.1521 -0.0039 0.0045 0.0068 192 GLY B CA 4590 C C . GLY B 192 ? 0.1435 0.1517 0.1505 -0.0080 0.0057 0.0054 192 GLY B C 4591 O O . GLY B 192 ? 0.1537 0.1542 0.1621 -0.0137 0.0106 0.0168 192 GLY B O 4592 N N . SER B 193 ? 0.1370 0.1450 0.1492 -0.0093 0.0008 0.0034 193 SER B N 4593 C CA . SER B 193 ? 0.1339 0.1405 0.1461 -0.0005 0.0025 0.0016 193 SER B CA 4594 C C . SER B 193 ? 0.1141 0.1243 0.1340 -0.0005 -0.0013 -0.0056 193 SER B C 4595 O O . SER B 193 ? 0.1212 0.1300 0.1456 -0.0109 -0.0019 -0.0013 193 SER B O 4596 C CB . SER B 193 ? 0.1197 0.1381 0.1467 -0.0052 0.0080 -0.0031 193 SER B CB 4597 O OG . SER B 193 ? 0.1466 0.1386 0.1395 -0.0057 0.0017 0.0087 193 SER B OG 4598 N N . CYS B 194 ? 0.1213 0.1380 0.1344 0.0020 -0.0110 -0.0045 194 CYS B N 4599 C CA . CYS B 194 ? 0.1220 0.1362 0.1325 -0.0047 -0.0081 0.0005 194 CYS B CA 4600 C C . CYS B 194 ? 0.1267 0.1345 0.1322 -0.0039 -0.0058 -0.0015 194 CYS B C 4601 O O . CYS B 194 ? 0.1355 0.1451 0.1468 -0.0157 -0.0099 0.0006 194 CYS B O 4602 C CB . CYS B 194 ? 0.1437 0.1404 0.1381 -0.0039 -0.0004 0.0019 194 CYS B CB 4603 S SG . CYS B 194 ? 0.1176 0.1586 0.1675 -0.0170 -0.0065 0.0135 194 CYS B SG 4604 N N . CYS B 195 ? 0.1149 0.1288 0.1237 -0.0090 -0.0050 0.0039 195 CYS B N 4605 C CA . CYS B 195 ? 0.1178 0.1283 0.1271 -0.0068 -0.0037 0.0021 195 CYS B CA 4606 C C . CYS B 195 ? 0.1148 0.1295 0.1217 -0.0021 -0.0131 -0.0011 195 CYS B C 4607 O O . CYS B 195 ? 0.1355 0.1311 0.1268 -0.0047 -0.0188 0.0106 195 CYS B O 4608 C CB . CYS B 195 ? 0.1312 0.1449 0.1176 -0.0126 -0.0027 0.0029 195 CYS B CB 4609 S SG . CYS B 195 ? 0.1349 0.1372 0.1214 -0.0206 -0.0003 -0.0079 195 CYS B SG 4610 N N . ASN B 196 ? 0.1110 0.1256 0.1282 -0.0073 -0.0070 -0.0014 196 ASN B N 4611 C CA . ASN B 196 ? 0.1295 0.1253 0.1425 0.0035 -0.0071 -0.0014 196 ASN B CA 4612 C C . ASN B 196 ? 0.1273 0.1259 0.1360 -0.0021 -0.0049 0.0057 196 ASN B C 4613 O O . ASN B 196 ? 0.1204 0.1339 0.1689 0.0028 -0.0061 0.0066 196 ASN B O 4614 C CB . ASN B 196 ? 0.1332 0.1571 0.1533 0.0032 0.0021 0.0058 196 ASN B CB 4615 C CG . ASN B 196 ? 0.1569 0.1678 0.1979 0.0067 0.0137 -0.0060 196 ASN B CG 4616 O OD1 . ASN B 196 ? 0.2056 0.1946 0.1915 -0.0066 -0.0200 0.0175 196 ASN B OD1 4617 N ND2 . ASN B 196 ? 0.2115 0.1969 0.2323 0.0141 -0.0213 -0.0253 196 ASN B ND2 4618 N N . SER B 197 ? 0.1232 0.1156 0.1422 -0.0054 -0.0041 -0.0045 197 SER B N 4619 C CA . SER B 197 ? 0.1302 0.1287 0.1410 -0.0044 -0.0042 -0.0013 197 SER B CA 4620 C C . SER B 197 ? 0.1235 0.1275 0.1318 -0.0001 -0.0003 0.0014 197 SER B C 4621 O O . SER B 197 ? 0.1377 0.1206 0.1486 -0.0037 0.0074 0.0154 197 SER B O 4622 C CB . SER B 197 ? 0.1579 0.1583 0.1658 -0.0067 0.0031 -0.0023 197 SER B CB 4623 O OG . SER B 197 ? 0.1854 0.2106 0.2172 -0.0070 -0.0023 -0.0049 197 SER B OG 4624 N N . MET B 198 ? 0.1134 0.1189 0.1247 -0.0039 -0.0060 0.0028 198 MET B N 4625 C CA . MET B 198 ? 0.1188 0.1103 0.1202 0.0026 -0.0016 0.0000 198 MET B CA 4626 C C . MET B 198 ? 0.1307 0.1234 0.1269 0.0033 -0.0053 0.0025 198 MET B C 4627 O O . MET B 198 ? 0.1192 0.1260 0.1243 0.0038 -0.0017 0.0081 198 MET B O 4628 C CB . MET B 198 ? 0.1317 0.1270 0.1244 0.0007 -0.0026 0.0020 198 MET B CB 4629 C CG . MET B 198 ? 0.1336 0.1378 0.1320 -0.0083 0.0002 0.0038 198 MET B CG 4630 S SD . MET B 198 ? 0.1155 0.1331 0.1393 0.0021 0.0031 -0.0031 198 MET B SD 4631 C CE . MET B 198 ? 0.1215 0.1213 0.1413 0.0221 0.0044 -0.0059 198 MET B CE 4632 N N . ASP B 199 ? 0.1224 0.1096 0.1246 0.0066 -0.0057 -0.0007 199 ASP B N 4633 C CA . ASP B 199 ? 0.1232 0.1128 0.1189 0.0046 0.0000 0.0026 199 ASP B CA 4634 C C . ASP B 199 ? 0.1148 0.1107 0.1082 0.0056 -0.0015 -0.0005 199 ASP B C 4635 O O . ASP B 199 ? 0.1130 0.1094 0.1159 0.0042 0.0093 0.0043 199 ASP B O 4636 C CB . ASP B 199 ? 0.1263 0.1271 0.1190 0.0037 0.0067 -0.0123 199 ASP B CB 4637 C CG . ASP B 199 ? 0.1574 0.1422 0.1410 0.0211 0.0047 -0.0052 199 ASP B CG 4638 O OD1 . ASP B 199 ? 0.1622 0.1882 0.1928 0.0073 -0.0122 -0.0044 199 ASP B OD1 4639 O OD2 . ASP B 199 ? 0.1998 0.1639 0.1908 -0.0069 0.0317 0.0205 199 ASP B OD2 4640 N N . ILE B 200 ? 0.1031 0.1171 0.1223 0.0080 0.0028 0.0027 200 ILE B N 4641 C CA . ILE B 200 ? 0.1096 0.1214 0.1144 0.0092 0.0022 -0.0024 200 ILE B CA 4642 C C . ILE B 200 ? 0.1012 0.0986 0.1022 0.0040 0.0010 -0.0046 200 ILE B C 4643 O O . ILE B 200 ? 0.1130 0.1110 0.1084 0.0107 -0.0023 -0.0102 200 ILE B O 4644 C CB . ILE B 200 ? 0.1026 0.1057 0.1126 -0.0006 0.0019 -0.0128 200 ILE B CB 4645 C CG1 . ILE B 200 ? 0.1292 0.1434 0.1250 0.0104 -0.0078 0.0080 200 ILE B CG1 4646 C CG2 . ILE B 200 ? 0.1110 0.1217 0.1248 0.0025 0.0087 -0.0070 200 ILE B CG2 4647 C CD1 . ILE B 200 ? 0.1513 0.1416 0.1357 -0.0050 -0.0047 0.0056 200 ILE B CD1 4648 N N . TRP B 201 ? 0.1127 0.1157 0.1077 0.0029 0.0012 -0.0061 201 TRP B N 4649 C CA . TRP B 201 ? 0.1096 0.1117 0.1072 0.0024 0.0008 0.0054 201 TRP B CA 4650 C C . TRP B 201 ? 0.1109 0.1144 0.1052 0.0112 -0.0009 0.0025 201 TRP B C 4651 O O . TRP B 201 ? 0.1060 0.1037 0.1096 0.0148 0.0017 -0.0001 201 TRP B O 4652 C CB . TRP B 201 ? 0.1123 0.1219 0.0997 -0.0046 0.0019 0.0052 201 TRP B CB 4653 C CG . TRP B 201 ? 0.1100 0.1154 0.1215 -0.0062 -0.0013 0.0016 201 TRP B CG 4654 C CD1 . TRP B 201 ? 0.1174 0.1151 0.1112 0.0073 -0.0097 -0.0005 201 TRP B CD1 4655 C CD2 . TRP B 201 ? 0.1114 0.1183 0.1121 -0.0036 0.0021 0.0014 201 TRP B CD2 4656 N NE1 . TRP B 201 ? 0.0938 0.1204 0.1171 0.0045 -0.0006 -0.0024 201 TRP B NE1 4657 C CE2 . TRP B 201 ? 0.1030 0.1030 0.1104 0.0018 0.0051 0.0024 201 TRP B CE2 4658 C CE3 . TRP B 201 ? 0.1155 0.1389 0.1203 -0.0051 0.0075 0.0154 201 TRP B CE3 4659 C CZ2 . TRP B 201 ? 0.1295 0.1334 0.1213 0.0012 -0.0071 -0.0006 201 TRP B CZ2 4660 C CZ3 . TRP B 201 ? 0.1267 0.1474 0.1426 0.0065 -0.0014 0.0068 201 TRP B CZ3 4661 C CH2 . TRP B 201 ? 0.1111 0.1430 0.1338 -0.0057 -0.0034 0.0081 201 TRP B CH2 4662 N N . GLU B 202 ? 0.1253 0.1130 0.1183 0.0085 0.0082 0.0037 202 GLU B N 4663 C CA . GLU B 202 ? 0.1110 0.1152 0.1132 0.0016 0.0033 0.0028 202 GLU B CA 4664 C C . GLU B 202 ? 0.1063 0.1059 0.1058 0.0018 0.0018 0.0038 202 GLU B C 4665 O O . GLU B 202 ? 0.1077 0.1134 0.1201 0.0059 0.0067 0.0109 202 GLU B O 4666 C CB . GLU B 202 ? 0.1163 0.1164 0.1171 0.0093 0.0080 0.0019 202 GLU B CB 4667 C CG . GLU B 202 ? 0.1386 0.1465 0.1297 0.0052 -0.0103 0.0022 202 GLU B CG 4668 C CD . GLU B 202 ? 0.1233 0.1485 0.1363 0.0055 -0.0111 -0.0039 202 GLU B CD 4669 O OE1 . GLU B 202 ? 0.1617 0.1642 0.1305 0.0171 -0.0078 0.0042 202 GLU B OE1 4670 O OE2 . GLU B 202 ? 0.1443 0.1383 0.1721 0.0261 0.0024 0.0026 202 GLU B OE2 4671 N N . ALA B 203 ? 0.0988 0.1016 0.1087 -0.0006 -0.0017 0.0013 203 ALA B N 4672 C CA . ALA B 203 ? 0.1028 0.1076 0.1175 0.0023 -0.0026 -0.0029 203 ALA B CA 4673 C C . ALA B 203 ? 0.1047 0.1030 0.1073 -0.0019 -0.0036 0.0017 203 ALA B C 4674 O O . ALA B 203 ? 0.1003 0.1036 0.1273 0.0069 -0.0054 -0.0020 203 ALA B O 4675 C CB . ALA B 203 ? 0.1099 0.1151 0.1312 -0.0041 -0.0011 -0.0053 203 ALA B CB 4676 N N . ASN B 204 ? 0.1013 0.1080 0.1177 0.0068 -0.0014 0.0016 204 ASN B N 4677 C CA . ASN B 204 ? 0.1116 0.1151 0.1239 0.0021 -0.0014 0.0016 204 ASN B CA 4678 C C . ASN B 204 ? 0.1217 0.1174 0.1242 0.0054 -0.0079 0.0019 204 ASN B C 4679 O O . ASN B 204 ? 0.1207 0.1234 0.1299 -0.0010 -0.0056 -0.0069 204 ASN B O 4680 C CB . ASN B 204 ? 0.1142 0.1195 0.1304 -0.0016 -0.0027 0.0067 204 ASN B CB 4681 C CG . ASN B 204 ? 0.1121 0.1060 0.1301 -0.0085 -0.0014 -0.0105 204 ASN B CG 4682 O OD1 . ASN B 204 ? 0.1067 0.1305 0.1323 0.0061 -0.0189 0.0063 204 ASN B OD1 4683 N ND2 . ASN B 204 ? 0.1139 0.1282 0.1164 -0.0080 -0.0071 -0.0125 204 ASN B ND2 4684 N N . SER B 205 ? 0.1199 0.1325 0.1260 0.0042 -0.0106 -0.0124 205 SER B N 4685 C CA . SER B 205 ? 0.1143 0.1243 0.1302 0.0000 -0.0057 -0.0006 205 SER B CA 4686 C C . SER B 205 ? 0.1162 0.1261 0.1316 0.0034 -0.0069 -0.0003 205 SER B C 4687 O O . SER B 205 ? 0.1116 0.1338 0.1476 0.0105 -0.0050 0.0009 205 SER B O 4688 C CB . SER B 205 ? 0.1363 0.1342 0.1378 -0.0038 -0.0085 -0.0074 205 SER B CB 4689 O OG . SER B 205 ? 0.1188 0.1528 0.1235 -0.0005 -0.0236 -0.0132 205 SER B OG 4690 N N . ARG B 206 ? 0.1158 0.1227 0.1338 0.0023 0.0016 -0.0020 206 ARG B N 4691 C CA . ARG B 206 ? 0.1155 0.1288 0.1282 0.0039 -0.0032 -0.0021 206 ARG B CA 4692 C C . ARG B 206 ? 0.1214 0.1311 0.1324 -0.0020 -0.0024 -0.0015 206 ARG B C 4693 O O . ARG B 206 ? 0.1420 0.1355 0.1215 0.0112 -0.0087 -0.0037 206 ARG B O 4694 C CB . ARG B 206 ? 0.1273 0.1416 0.1339 0.0077 -0.0090 -0.0002 206 ARG B CB 4695 C CG . ARG B 206 ? 0.1323 0.1395 0.1456 0.0068 -0.0050 -0.0041 206 ARG B CG 4696 C CD . ARG B 206 ? 0.1449 0.1395 0.1535 0.0051 -0.0180 -0.0066 206 ARG B CD 4697 N NE . ARG B 206 ? 0.1639 0.1436 0.1268 0.0117 -0.0205 -0.0076 206 ARG B NE 4698 C CZ . ARG B 206 ? 0.1784 0.1737 0.1495 0.0174 -0.0126 -0.0061 206 ARG B CZ 4699 N NH1 . ARG B 206 ? 0.1527 0.1809 0.1720 0.0180 -0.0203 -0.0080 206 ARG B NH1 4700 N NH2 . ARG B 206 ? 0.1841 0.1990 0.1649 0.0259 -0.0297 0.0073 206 ARG B NH2 4701 N N . ALA B 207 ? 0.1117 0.1258 0.1172 0.0110 -0.0012 0.0049 207 ALA B N 4702 C CA . ALA B 207 ? 0.1185 0.1280 0.1312 0.0075 -0.0009 -0.0008 207 ALA B CA 4703 C C . ALA B 207 ? 0.1225 0.1216 0.1248 0.0045 -0.0017 -0.0036 207 ALA B C 4704 O O . ALA B 207 ? 0.1363 0.1244 0.1369 0.0090 -0.0009 -0.0031 207 ALA B O 4705 C CB . ALA B 207 ? 0.1284 0.1254 0.1277 0.0075 -0.0095 -0.0030 207 ALA B CB 4706 N N . SER B 208 ? 0.1324 0.1271 0.1249 0.0023 -0.0105 -0.0120 208 SER B N 4707 C CA . SER B 208 ? 0.1296 0.1164 0.1275 0.0031 -0.0034 0.0050 208 SER B CA 4708 C C . SER B 208 ? 0.1305 0.1162 0.1306 0.0041 -0.0065 -0.0038 208 SER B C 4709 O O . SER B 208 ? 0.1359 0.1220 0.1348 0.0234 -0.0162 0.0054 208 SER B O 4710 C CB . SER B 208 ? 0.1277 0.1224 0.1271 0.0130 -0.0054 0.0032 208 SER B CB 4711 O OG . SER B 208 ? 0.1321 0.1439 0.1223 0.0034 -0.0096 0.0122 208 SER B OG 4712 N N . HIS B 209 ? 0.1201 0.1128 0.1235 0.0027 -0.0014 -0.0061 209 HIS B N 4713 C CA . HIS B 209 ? 0.1206 0.1050 0.1242 -0.0010 0.0030 -0.0027 209 HIS B CA 4714 C C . HIS B 209 ? 0.1077 0.1107 0.1351 0.0049 0.0002 -0.0044 209 HIS B C 4715 O O . HIS B 209 ? 0.1212 0.0985 0.1322 0.0012 -0.0007 0.0052 209 HIS B O 4716 C CB . HIS B 209 ? 0.1146 0.1300 0.1256 0.0014 -0.0017 -0.0056 209 HIS B CB 4717 C CG . HIS B 209 ? 0.1363 0.1048 0.1154 0.0005 0.0023 0.0006 209 HIS B CG 4718 N ND1 . HIS B 209 ? 0.1520 0.1354 0.1550 -0.0130 0.0208 -0.0135 209 HIS B ND1 4719 C CD2 . HIS B 209 ? 0.1471 0.1431 0.1259 -0.0060 0.0249 -0.0099 209 HIS B CD2 4720 C CE1 . HIS B 209 ? 0.1539 0.1551 0.1654 -0.0421 0.0214 -0.0101 209 HIS B CE1 4721 N NE2 . HIS B 209 ? 0.1735 0.1567 0.1644 -0.0071 0.0313 -0.0395 209 HIS B NE2 4722 N N . VAL B 210 ? 0.1105 0.1113 0.1168 0.0039 -0.0033 -0.0089 210 VAL B N 4723 C CA . VAL B 210 ? 0.1157 0.1118 0.1162 0.0027 -0.0007 -0.0032 210 VAL B CA 4724 C C . VAL B 210 ? 0.1231 0.1156 0.1209 0.0042 -0.0058 -0.0013 210 VAL B C 4725 O O . VAL B 210 ? 0.1255 0.1084 0.1173 0.0070 -0.0076 0.0004 210 VAL B O 4726 C CB . VAL B 210 ? 0.1082 0.1212 0.1262 0.0032 -0.0012 -0.0009 210 VAL B CB 4727 C CG1 . VAL B 210 ? 0.1306 0.1056 0.1144 0.0139 -0.0036 -0.0070 210 VAL B CG1 4728 C CG2 . VAL B 210 ? 0.1037 0.1264 0.1332 0.0069 0.0125 -0.0127 210 VAL B CG2 4729 N N . ALA B 211 ? 0.1221 0.1116 0.1162 0.0025 -0.0058 -0.0038 211 ALA B N 4730 C CA . ALA B 211 ? 0.1208 0.1150 0.1175 0.0004 0.0032 -0.0006 211 ALA B CA 4731 C C . ALA B 211 ? 0.1220 0.1216 0.1247 -0.0001 0.0004 -0.0056 211 ALA B C 4732 O O . ALA B 211 ? 0.1276 0.1136 0.1236 -0.0005 0.0052 -0.0044 211 ALA B O 4733 C CB . ALA B 211 ? 0.1219 0.1145 0.1153 -0.0092 0.0048 -0.0018 211 ALA B CB 4734 N N . PRO B 212 ? 0.1154 0.1127 0.1185 0.0029 -0.0007 -0.0018 212 PRO B N 4735 C CA . PRO B 212 ? 0.1111 0.1139 0.1154 0.0041 -0.0008 0.0021 212 PRO B CA 4736 C C . PRO B 212 ? 0.1237 0.1149 0.1173 0.0011 -0.0010 0.0053 212 PRO B C 4737 O O . PRO B 212 ? 0.1327 0.1131 0.1230 0.0055 0.0003 0.0087 212 PRO B O 4738 C CB . PRO B 212 ? 0.1167 0.1076 0.1187 -0.0027 0.0007 0.0078 212 PRO B CB 4739 C CG . PRO B 212 ? 0.1273 0.1219 0.1187 0.0116 0.0046 -0.0021 212 PRO B CG 4740 C CD . PRO B 212 ? 0.1250 0.1254 0.1145 0.0078 0.0017 -0.0014 212 PRO B CD 4741 N N . HIS B 213 ? 0.1183 0.1248 0.1177 0.0106 -0.0054 0.0046 213 HIS B N 4742 C CA . HIS B 213 ? 0.1316 0.1193 0.1273 -0.0008 -0.0014 0.0040 213 HIS B CA 4743 C C . HIS B 213 ? 0.1360 0.1286 0.1386 0.0025 -0.0013 0.0039 213 HIS B C 4744 O O . HIS B 213 ? 0.1416 0.1295 0.1525 -0.0116 -0.0204 0.0060 213 HIS B O 4745 C CB . HIS B 213 ? 0.1227 0.1306 0.1294 0.0067 0.0019 -0.0015 213 HIS B CB 4746 C CG . HIS B 213 ? 0.1330 0.1166 0.1314 0.0071 -0.0065 0.0055 213 HIS B CG 4747 N ND1 . HIS B 213 ? 0.0971 0.1257 0.1355 0.0000 -0.0079 -0.0047 213 HIS B ND1 4748 C CD2 . HIS B 213 ? 0.1553 0.1331 0.1234 -0.0174 0.0028 -0.0041 213 HIS B CD2 4749 C CE1 . HIS B 213 ? 0.1282 0.1514 0.1051 -0.0041 0.0144 -0.0089 213 HIS B CE1 4750 N NE2 . HIS B 213 ? 0.1440 0.1335 0.1294 -0.0033 0.0111 -0.0051 213 HIS B NE2 4751 N N . THR B 214 ? 0.1370 0.1305 0.1378 -0.0063 -0.0123 0.0131 214 THR B N 4752 C CA . THR B 214 ? 0.1385 0.1284 0.1246 -0.0014 -0.0007 0.0056 214 THR B CA 4753 C C . THR B 214 ? 0.1366 0.1364 0.1358 -0.0076 -0.0038 0.0093 214 THR B C 4754 O O . THR B 214 ? 0.1433 0.1501 0.1396 -0.0067 -0.0011 0.0160 214 THR B O 4755 C CB . THR B 214 ? 0.1309 0.1396 0.1172 0.0022 -0.0026 0.0017 214 THR B CB 4756 O OG1 . THR B 214 ? 0.1531 0.1289 0.1512 -0.0054 -0.0032 0.0053 214 THR B OG1 4757 C CG2 . THR B 214 ? 0.1259 0.1406 0.1286 0.0170 0.0058 0.0133 214 THR B CG2 4758 N N . CYS B 215 ? 0.1484 0.1413 0.1234 -0.0070 -0.0040 0.0175 215 CYS B N 4759 C CA . CYS B 215 ? 0.1419 0.1429 0.1370 -0.0048 -0.0055 0.0035 215 CYS B CA 4760 C C . CYS B 215 ? 0.1374 0.1347 0.1482 -0.0036 -0.0017 0.0003 215 CYS B C 4761 O O . CYS B 215 ? 0.1369 0.1629 0.1680 -0.0040 -0.0056 -0.0047 215 CYS B O 4762 C CB . CYS B 215 ? 0.1299 0.1509 0.1309 0.0027 -0.0170 0.0058 215 CYS B CB 4763 S SG . CYS B 215 ? 0.1415 0.1333 0.1723 -0.0252 -0.0049 0.0019 215 CYS B SG 4764 N N . ASN B 216 ? 0.1469 0.1488 0.1554 -0.0134 -0.0031 0.0016 216 ASN B N 4765 C CA . ASN B 216 ? 0.1620 0.1417 0.1642 -0.0150 -0.0071 0.0012 216 ASN B CA 4766 C C . ASN B 216 ? 0.1641 0.1626 0.1769 -0.0104 -0.0163 0.0002 216 ASN B C 4767 O O . ASN B 216 ? 0.1963 0.1770 0.1956 -0.0137 -0.0378 -0.0023 216 ASN B O 4768 C CB . ASN B 216 ? 0.1582 0.1315 0.1627 -0.0160 -0.0130 0.0047 216 ASN B CB 4769 C CG . ASN B 216 ? 0.1488 0.1381 0.1845 -0.0143 -0.0027 0.0113 216 ASN B CG 4770 O OD1 . ASN B 216 ? 0.1712 0.1566 0.2173 -0.0260 0.0066 -0.0253 216 ASN B OD1 4771 N ND2 . ASN B 216 ? 0.1820 0.1449 0.1906 -0.0288 -0.0073 0.0072 216 ASN B ND2 4772 N N . LYS B 217 ? 0.1669 0.1574 0.1690 -0.0115 -0.0162 0.0043 217 LYS B N 4773 C CA . LYS B 217 ? 0.1668 0.1694 0.1771 -0.0043 -0.0169 0.0024 217 LYS B CA 4774 C C . LYS B 217 ? 0.1760 0.1682 0.1930 -0.0077 -0.0223 0.0065 217 LYS B C 4775 O O . LYS B 217 ? 0.1980 0.1912 0.2168 -0.0253 -0.0411 0.0194 217 LYS B O 4776 C CB . LYS B 217 ? 0.2066 0.1942 0.1961 0.0019 -0.0149 -0.0027 217 LYS B CB 4777 C CG . LYS B 217 ? 0.2128 0.2141 0.2179 0.0132 -0.0029 -0.0072 217 LYS B CG 4778 C CD . LYS B 217 ? 0.2323 0.2325 0.2429 0.0003 -0.0089 -0.0138 217 LYS B CD 4779 C CE . LYS B 217 ? 0.2330 0.2652 0.2669 -0.0056 0.0032 -0.0105 217 LYS B CE 4780 N NZ . LYS B 217 ? 0.2609 0.3134 0.3346 -0.0026 -0.0054 -0.0035 217 LYS B NZ 4781 N N . LYS B 218 ? 0.1587 0.1701 0.1796 -0.0164 -0.0141 0.0051 218 LYS B N 4782 C CA . LYS B 218 ? 0.1652 0.1552 0.1807 -0.0066 -0.0089 0.0009 218 LYS B CA 4783 C C . LYS B 218 ? 0.1505 0.1551 0.1827 -0.0083 0.0000 -0.0058 218 LYS B C 4784 O O . LYS B 218 ? 0.1661 0.1557 0.1899 -0.0002 0.0032 -0.0144 218 LYS B O 4785 C CB . LYS B 218 ? 0.1746 0.1632 0.1818 -0.0054 -0.0044 0.0007 218 LYS B CB 4786 C CG . LYS B 218 ? 0.1751 0.1606 0.1950 -0.0043 -0.0136 -0.0021 218 LYS B CG 4787 C CD . LYS B 218 ? 0.1813 0.1809 0.1995 -0.0116 -0.0014 -0.0014 218 LYS B CD 4788 C CE . LYS B 218 ? 0.2082 0.2024 0.2146 -0.0071 -0.0051 -0.0129 218 LYS B CE 4789 N NZ . LYS B 218 ? 0.2342 0.2413 0.2077 -0.0206 0.0057 -0.0180 218 LYS B NZ 4790 N N . GLY B 219 ? 0.1534 0.1475 0.1780 -0.0118 -0.0034 -0.0065 219 GLY B N 4791 C CA . GLY B 219 ? 0.1543 0.1556 0.1696 0.0018 -0.0032 -0.0005 219 GLY B CA 4792 C C . GLY B 219 ? 0.1609 0.1577 0.1666 -0.0013 -0.0101 0.0018 219 GLY B C 4793 O O . GLY B 219 ? 0.1879 0.1674 0.1497 0.0124 -0.0169 0.0129 219 GLY B O 4794 N N . LEU B 220 ? 0.1436 0.1416 0.1506 0.0006 -0.0101 -0.0042 220 LEU B N 4795 C CA . LEU B 220 ? 0.1466 0.1594 0.1479 -0.0009 -0.0128 0.0038 220 LEU B CA 4796 C C . LEU B 220 ? 0.1488 0.1588 0.1603 -0.0001 -0.0103 0.0077 220 LEU B C 4797 O O . LEU B 220 ? 0.1526 0.1693 0.1670 -0.0067 -0.0231 0.0133 220 LEU B O 4798 C CB . LEU B 220 ? 0.1340 0.1591 0.1435 -0.0011 -0.0206 0.0070 220 LEU B CB 4799 C CG . LEU B 220 ? 0.1475 0.1506 0.1590 -0.0057 -0.0047 -0.0047 220 LEU B CG 4800 C CD1 . LEU B 220 ? 0.1721 0.1463 0.1660 0.0079 -0.0034 0.0034 220 LEU B CD1 4801 C CD2 . LEU B 220 ? 0.1666 0.1596 0.1635 -0.0079 -0.0002 -0.0068 220 LEU B CD2 4802 N N . TYR B 221 ? 0.1397 0.1554 0.1575 -0.0007 -0.0052 0.0043 221 TYR B N 4803 C CA . TYR B 221 ? 0.1430 0.1597 0.1595 -0.0050 -0.0093 0.0050 221 TYR B CA 4804 C C . TYR B 221 ? 0.1435 0.1628 0.1623 -0.0006 -0.0078 -0.0004 221 TYR B C 4805 O O . TYR B 221 ? 0.1349 0.1495 0.1420 -0.0169 -0.0049 0.0000 221 TYR B O 4806 C CB . TYR B 221 ? 0.1558 0.1715 0.1668 -0.0016 -0.0078 -0.0003 221 TYR B CB 4807 C CG . TYR B 221 ? 0.1613 0.1631 0.1777 -0.0046 -0.0005 0.0089 221 TYR B CG 4808 C CD1 . TYR B 221 ? 0.1900 0.1710 0.1959 -0.0177 -0.0045 0.0060 221 TYR B CD1 4809 C CD2 . TYR B 221 ? 0.1596 0.1523 0.1962 -0.0071 -0.0026 0.0100 221 TYR B CD2 4810 C CE1 . TYR B 221 ? 0.2059 0.1934 0.2154 -0.0296 -0.0118 0.0171 221 TYR B CE1 4811 C CE2 . TYR B 221 ? 0.1639 0.1822 0.1985 -0.0117 0.0012 0.0077 221 TYR B CE2 4812 C CZ . TYR B 221 ? 0.1650 0.1882 0.2101 -0.0196 -0.0109 0.0253 221 TYR B CZ 4813 O OH . TYR B 221 ? 0.2037 0.2407 0.2964 -0.0363 -0.0047 0.0405 221 TYR B OH 4814 N N . LEU B 222 ? 0.1379 0.1717 0.1759 -0.0128 -0.0136 -0.0057 222 LEU B N 4815 C CA . LEU B 222 ? 0.1490 0.1621 0.1726 -0.0045 -0.0071 0.0023 222 LEU B CA 4816 C C . LEU B 222 ? 0.1574 0.1671 0.1767 -0.0071 -0.0074 0.0011 222 LEU B C 4817 O O . LEU B 222 ? 0.1614 0.1713 0.1980 -0.0083 -0.0135 0.0107 222 LEU B O 4818 C CB . LEU B 222 ? 0.1402 0.1702 0.1878 -0.0046 -0.0086 -0.0049 222 LEU B CB 4819 C CG . LEU B 222 ? 0.1506 0.1710 0.2090 0.0015 -0.0141 0.0091 222 LEU B CG 4820 C CD1 . LEU B 222 ? 0.1689 0.1997 0.2236 -0.0018 -0.0175 0.0044 222 LEU B CD1 4821 C CD2 . LEU B 222 ? 0.1751 0.1810 0.2086 0.0003 -0.0082 -0.0034 222 LEU B CD2 4822 N N . CYS B 223 ? 0.1536 0.1602 0.1833 -0.0103 -0.0060 0.0083 223 CYS B N 4823 C CA . CYS B 223 ? 0.1607 0.1678 0.1816 -0.0048 -0.0037 0.0101 223 CYS B CA 4824 C C . CYS B 223 ? 0.1566 0.1760 0.2002 -0.0069 -0.0061 0.0069 223 CYS B C 4825 O O . CYS B 223 ? 0.1415 0.1784 0.2139 -0.0118 -0.0117 0.0120 223 CYS B O 4826 C CB . CYS B 223 ? 0.1405 0.1588 0.1696 -0.0122 0.0022 0.0180 223 CYS B CB 4827 S SG . CYS B 223 ? 0.1235 0.1565 0.1885 -0.0181 0.0042 0.0220 223 CYS B SG 4828 N N . GLU B 224 ? 0.1678 0.1753 0.2100 -0.0098 0.0067 0.0163 224 GLU B N 4829 C CA . GLU B 224 ? 0.1953 0.2056 0.2266 -0.0040 0.0055 0.0090 224 GLU B CA 4830 C C . GLU B 224 ? 0.1804 0.1998 0.2256 -0.0112 0.0068 0.0083 224 GLU B C 4831 O O . GLU B 224 ? 0.1690 0.1863 0.2310 -0.0200 0.0216 0.0134 224 GLU B O 4832 C CB . GLU B 224 ? 0.2111 0.2237 0.2480 0.0010 0.0043 0.0156 224 GLU B CB 4833 C CG . GLU B 224 ? 0.2483 0.2779 0.2707 0.0030 -0.0046 -0.0035 224 GLU B CG 4834 C CD . GLU B 224 ? 0.2568 0.2943 0.3112 -0.0015 -0.0091 -0.0073 224 GLU B CD 4835 O OE1 . GLU B 224 ? 0.3270 0.3526 0.3910 0.0086 0.0232 -0.0268 224 GLU B OE1 4836 O OE2 . GLU B 224 ? 0.3706 0.4133 0.3727 -0.0048 -0.0155 -0.0278 224 GLU B OE2 4837 N N . GLY B 225 ? 0.1908 0.1980 0.2348 -0.0006 0.0096 0.0167 225 GLY B N 4838 C CA . GLY B 225 ? 0.2078 0.2157 0.2386 -0.0035 0.0117 0.0152 225 GLY B CA 4839 C C . GLY B 225 ? 0.2092 0.2163 0.2431 -0.0024 0.0086 0.0097 225 GLY B C 4840 O O . GLY B 225 ? 0.2146 0.2216 0.2391 -0.0217 0.0217 0.0218 225 GLY B O 4841 N N . GLU B 226 ? 0.2166 0.2170 0.2508 -0.0151 0.0125 0.0094 226 GLU B N 4842 C CA . GLU B 226 ? 0.2259 0.2265 0.2470 -0.0052 0.0084 0.0076 226 GLU B CA 4843 C C . GLU B 226 ? 0.2052 0.1986 0.2236 -0.0075 0.0047 0.0073 226 GLU B C 4844 O O . GLU B 226 ? 0.1989 0.1768 0.2426 -0.0160 0.0135 0.0201 226 GLU B O 4845 C CB . GLU B 226 ? 0.2393 0.2365 0.2674 0.0005 0.0063 0.0072 226 GLU B CB 4846 C CG . GLU B 226 ? 0.3039 0.2974 0.3134 -0.0031 0.0093 0.0044 226 GLU B CG 4847 C CD . GLU B 226 ? 0.3171 0.3008 0.3357 -0.0147 0.0105 0.0098 226 GLU B CD 4848 O OE1 . GLU B 226 ? 0.4230 0.3522 0.4138 -0.0128 0.0132 -0.0097 226 GLU B OE1 4849 O OE2 . GLU B 226 ? 0.4207 0.4150 0.4205 -0.0211 0.0275 0.0272 226 GLU B OE2 4850 N N . GLU B 227 ? 0.1837 0.1918 0.2097 -0.0086 0.0052 0.0114 227 GLU B N 4851 C CA . GLU B 227 ? 0.1833 0.1866 0.2080 -0.0113 0.0045 -0.0005 227 GLU B CA 4852 C C . GLU B 227 ? 0.1724 0.1787 0.2020 -0.0076 0.0045 0.0045 227 GLU B C 4853 O O . GLU B 227 ? 0.1681 0.1556 0.1883 0.0010 0.0213 0.0102 227 GLU B O 4854 C CB . GLU B 227 ? 0.1717 0.1925 0.2019 -0.0163 0.0079 -0.0013 227 GLU B CB 4855 C CG . GLU B 227 ? 0.2012 0.2218 0.2385 -0.0219 -0.0031 -0.0071 227 GLU B CG 4856 C CD . GLU B 227 ? 0.2185 0.2265 0.2671 -0.0132 -0.0131 0.0007 227 GLU B CD 4857 O OE1 . GLU B 227 ? 0.1756 0.2136 0.2687 -0.0468 -0.0227 -0.0148 227 GLU B OE1 4858 O OE2 . GLU B 227 ? 0.3875 0.3405 0.3529 -0.0180 -0.0643 -0.0329 227 GLU B OE2 4859 N N . CYS B 228 ? 0.1492 0.1590 0.1816 -0.0002 0.0091 0.0133 228 CYS B N 4860 C CA . CYS B 228 ? 0.1469 0.1616 0.1783 -0.0003 0.0050 0.0064 228 CYS B CA 4861 C C . CYS B 228 ? 0.1598 0.1584 0.1849 0.0019 0.0030 0.0069 228 CYS B C 4862 O O . CYS B 228 ? 0.1526 0.1654 0.2012 0.0096 0.0100 0.0146 228 CYS B O 4863 C CB . CYS B 228 ? 0.1484 0.1642 0.1813 0.0043 0.0147 0.0062 228 CYS B CB 4864 S SG . CYS B 228 ? 0.1567 0.1635 0.2005 -0.0068 0.0106 0.0206 228 CYS B SG 4865 N N . ALA B 229 ? 0.1553 0.1677 0.1914 -0.0007 0.0034 0.0210 229 ALA B N 4866 C CA . ALA B 229 ? 0.1725 0.1765 0.1893 0.0005 0.0031 0.0129 229 ALA B CA 4867 C C . ALA B 229 ? 0.1685 0.1785 0.1896 0.0012 0.0029 0.0182 229 ALA B C 4868 O O . ALA B 229 ? 0.1634 0.1644 0.2071 0.0063 -0.0005 0.0295 229 ALA B O 4869 C CB . ALA B 229 ? 0.1926 0.1987 0.2137 0.0019 0.0015 0.0164 229 ALA B CB 4870 N N . PHE B 230 ? 0.1693 0.1776 0.1803 -0.0028 0.0091 0.0204 230 PHE B N 4871 C CA . PHE B 230 ? 0.1689 0.1732 0.1754 0.0001 0.0084 0.0207 230 PHE B CA 4872 C C . PHE B 230 ? 0.1717 0.1685 0.1815 -0.0043 0.0083 0.0188 230 PHE B C 4873 O O . PHE B 230 ? 0.1678 0.1521 0.1915 -0.0007 0.0082 0.0212 230 PHE B O 4874 C CB . PHE B 230 ? 0.1727 0.1730 0.1762 0.0077 0.0016 0.0219 230 PHE B CB 4875 C CG . PHE B 230 ? 0.1715 0.1723 0.1835 -0.0035 0.0119 0.0186 230 PHE B CG 4876 C CD1 . PHE B 230 ? 0.1902 0.1760 0.2168 -0.0037 0.0065 0.0252 230 PHE B CD1 4877 C CD2 . PHE B 230 ? 0.2017 0.1888 0.1902 0.0176 0.0043 0.0277 230 PHE B CD2 4878 C CE1 . PHE B 230 ? 0.1847 0.1944 0.1881 -0.0046 0.0131 0.0256 230 PHE B CE1 4879 C CE2 . PHE B 230 ? 0.1972 0.1696 0.1855 0.0122 0.0055 0.0276 230 PHE B CE2 4880 C CZ . PHE B 230 ? 0.1894 0.2107 0.1821 0.0123 0.0022 0.0198 230 PHE B CZ 4881 N N . GLU B 231 ? 0.1739 0.1776 0.1874 -0.0070 0.0117 0.0146 231 GLU B N 4882 C CA . GLU B 231 ? 0.1781 0.1786 0.1968 -0.0055 0.0077 0.0137 231 GLU B CA 4883 C C . GLU B 231 ? 0.1843 0.1808 0.2019 -0.0143 0.0045 0.0138 231 GLU B C 4884 O O . GLU B 231 ? 0.2159 0.1777 0.2139 -0.0182 -0.0021 0.0272 231 GLU B O 4885 C CB A GLU B 231 ? 0.1804 0.1831 0.2017 -0.0099 0.0031 0.0164 231 GLU B CB 4886 C CB B GLU B 231 ? 0.1794 0.1849 0.2040 -0.0090 0.0040 0.0161 231 GLU B CB 4887 C CG A GLU B 231 ? 0.1933 0.1719 0.1933 -0.0055 -0.0090 0.0100 231 GLU B CG 4888 C CG B GLU B 231 ? 0.1993 0.1882 0.2037 0.0030 0.0055 0.0132 231 GLU B CG 4889 C CD A GLU B 231 ? 0.2349 0.1882 0.1990 -0.0045 -0.0117 0.0078 231 GLU B CD 4890 C CD B GLU B 231 ? 0.1829 0.2062 0.2177 -0.0027 0.0037 0.0060 231 GLU B CD 4891 O OE1 A GLU B 231 ? 0.2255 0.1786 0.2407 -0.0174 0.0446 0.0146 231 GLU B OE1 4892 O OE1 B GLU B 231 ? 0.0934 0.1090 0.1420 0.0117 0.0318 0.0461 231 GLU B OE1 4893 O OE2 A GLU B 231 ? 0.2263 0.1597 0.2011 -0.0013 -0.0401 -0.0079 231 GLU B OE2 4894 O OE2 B GLU B 231 ? 0.2076 0.1791 0.2389 -0.0115 0.0396 0.0288 231 GLU B OE2 4895 N N . GLY B 232 ? 0.1662 0.1659 0.2014 -0.0051 0.0068 0.0159 232 GLY B N 4896 C CA . GLY B 232 ? 0.1562 0.1664 0.1853 -0.0063 0.0073 0.0122 232 GLY B CA 4897 C C . GLY B 232 ? 0.1475 0.1525 0.1786 -0.0106 0.0055 0.0088 232 GLY B C 4898 O O . GLY B 232 ? 0.1805 0.1639 0.2041 -0.0075 0.0136 0.0189 232 GLY B O 4899 N N . VAL B 233 ? 0.1403 0.1362 0.1962 -0.0108 -0.0014 0.0035 233 VAL B N 4900 C CA . VAL B 233 ? 0.1484 0.1509 0.1757 -0.0054 -0.0035 0.0013 233 VAL B CA 4901 C C . VAL B 233 ? 0.1469 0.1527 0.1588 -0.0092 0.0036 0.0005 233 VAL B C 4902 O O . VAL B 233 ? 0.1430 0.1392 0.1529 0.0040 -0.0067 0.0097 233 VAL B O 4903 C CB . VAL B 233 ? 0.1455 0.1531 0.1656 -0.0102 -0.0072 0.0042 233 VAL B CB 4904 C CG1 . VAL B 233 ? 0.1562 0.1935 0.1934 -0.0159 -0.0114 -0.0002 233 VAL B CG1 4905 C CG2 . VAL B 233 ? 0.1511 0.1611 0.1692 0.0067 -0.0077 0.0067 233 VAL B CG2 4906 N N . CYS B 234 ? 0.1314 0.1437 0.1584 -0.0079 0.0025 0.0075 234 CYS B N 4907 C CA . CYS B 234 ? 0.1300 0.1344 0.1443 -0.0088 0.0044 0.0024 234 CYS B CA 4908 C C . CYS B 234 ? 0.1434 0.1348 0.1459 -0.0064 0.0104 0.0094 234 CYS B C 4909 O O . CYS B 234 ? 0.1416 0.1464 0.1448 -0.0049 0.0057 0.0042 234 CYS B O 4910 C CB . CYS B 234 ? 0.1520 0.1406 0.1540 -0.0030 0.0083 0.0046 234 CYS B CB 4911 S SG . CYS B 234 ? 0.1507 0.1437 0.1494 -0.0057 0.0020 0.0039 234 CYS B SG 4912 N N . ASP B 235 ? 0.1389 0.1419 0.1373 0.0021 -0.0019 0.0061 235 ASP B N 4913 C CA . ASP B 235 ? 0.1313 0.1326 0.1384 -0.0027 0.0054 0.0040 235 ASP B CA 4914 C C . ASP B 235 ? 0.1304 0.1307 0.1294 -0.0076 0.0045 0.0068 235 ASP B C 4915 O O . ASP B 235 ? 0.1176 0.1389 0.1556 -0.0103 0.0151 0.0102 235 ASP B O 4916 C CB . ASP B 235 ? 0.1286 0.1366 0.1464 0.0013 0.0026 0.0033 235 ASP B CB 4917 C CG . ASP B 235 ? 0.1401 0.1275 0.1272 -0.0081 -0.0030 -0.0017 235 ASP B CG 4918 O OD1 . ASP B 235 ? 0.1300 0.1398 0.1344 0.0018 -0.0148 0.0047 235 ASP B OD1 4919 O OD2 . ASP B 235 ? 0.1043 0.1294 0.1499 0.0033 -0.0007 0.0074 235 ASP B OD2 4920 N N . LYS B 236 ? 0.1217 0.1309 0.1346 -0.0043 0.0059 0.0008 236 LYS B N 4921 C CA . LYS B 236 ? 0.1317 0.1365 0.1327 -0.0009 -0.0001 0.0038 236 LYS B CA 4922 C C . LYS B 236 ? 0.1390 0.1315 0.1432 0.0000 -0.0054 -0.0028 236 LYS B C 4923 O O . LYS B 236 ? 0.1323 0.1411 0.1259 -0.0066 -0.0022 -0.0073 236 LYS B O 4924 C CB . LYS B 236 ? 0.1325 0.1332 0.1293 -0.0041 -0.0036 0.0037 236 LYS B CB 4925 C CG . LYS B 236 ? 0.1445 0.1299 0.1448 0.0042 0.0047 0.0006 236 LYS B CG 4926 C CD . LYS B 236 ? 0.1401 0.1465 0.1391 0.0148 -0.0001 0.0123 236 LYS B CD 4927 C CE . LYS B 236 ? 0.1483 0.1595 0.1496 0.0112 0.0126 0.0178 236 LYS B CE 4928 N NZ . LYS B 236 ? 0.1950 0.1610 0.1500 0.0144 0.0016 0.0157 236 LYS B NZ 4929 N N . ASN B 237 ? 0.1374 0.1310 0.1458 -0.0047 -0.0037 -0.0042 237 ASN B N 4930 C CA . ASN B 237 ? 0.1411 0.1432 0.1426 -0.0016 -0.0034 -0.0001 237 ASN B CA 4931 C C . ASN B 237 ? 0.1412 0.1384 0.1536 -0.0038 0.0000 -0.0027 237 ASN B C 4932 O O . ASN B 237 ? 0.1329 0.1731 0.1596 -0.0172 0.0066 0.0060 237 ASN B O 4933 C CB . ASN B 237 ? 0.1660 0.1544 0.1748 -0.0048 -0.0079 0.0078 237 ASN B CB 4934 C CG . ASN B 237 ? 0.1912 0.2003 0.2027 -0.0070 -0.0004 0.0048 237 ASN B CG 4935 O OD1 . ASN B 237 ? 0.2231 0.2438 0.1754 0.0000 0.0089 0.0098 237 ASN B OD1 4936 N ND2 . ASN B 237 ? 0.2256 0.2142 0.2288 -0.0063 0.0010 0.0174 237 ASN B ND2 4937 N N . GLY B 238 ? 0.1303 0.1380 0.1444 -0.0035 0.0059 0.0023 238 GLY B N 4938 C CA . GLY B 238 ? 0.1350 0.1353 0.1392 0.0072 0.0033 0.0079 238 GLY B CA 4939 C C . GLY B 238 ? 0.1442 0.1396 0.1441 0.0133 0.0033 0.0130 238 GLY B C 4940 O O . GLY B 238 ? 0.1722 0.1750 0.1678 0.0448 0.0216 0.0283 238 GLY B O 4941 N N . CYS B 239 ? 0.1346 0.1243 0.1275 0.0095 -0.0049 0.0036 239 CYS B N 4942 C CA . CYS B 239 ? 0.1273 0.1256 0.1361 -0.0012 -0.0017 0.0065 239 CYS B CA 4943 C C . CYS B 239 ? 0.1271 0.1244 0.1329 -0.0001 -0.0031 0.0019 239 CYS B C 4944 O O . CYS B 239 ? 0.1410 0.1295 0.1363 0.0029 0.0021 0.0113 239 CYS B O 4945 C CB . CYS B 239 ? 0.1308 0.1029 0.1489 0.0010 -0.0077 0.0018 239 CYS B CB 4946 S SG . CYS B 239 ? 0.1471 0.1373 0.1614 0.0115 -0.0011 -0.0170 239 CYS B SG 4947 N N . GLY B 240 ? 0.1434 0.1185 0.1373 -0.0035 -0.0023 0.0019 240 GLY B N 4948 C CA . GLY B 240 ? 0.1256 0.1241 0.1243 0.0002 0.0023 0.0003 240 GLY B CA 4949 C C . GLY B 240 ? 0.1161 0.1130 0.1156 0.0074 0.0005 0.0004 240 GLY B C 4950 O O . GLY B 240 ? 0.1355 0.1131 0.1490 -0.0008 -0.0055 0.0080 240 GLY B O 4951 N N . TRP B 241 ? 0.1208 0.1085 0.1194 0.0067 0.0005 -0.0009 241 TRP B N 4952 C CA . TRP B 241 ? 0.1239 0.1198 0.1262 0.0028 -0.0019 0.0031 241 TRP B CA 4953 C C . TRP B 241 ? 0.1302 0.1182 0.1311 0.0010 -0.0087 0.0103 241 TRP B C 4954 O O . TRP B 241 ? 0.1372 0.1026 0.1306 0.0027 -0.0143 0.0054 241 TRP B O 4955 C CB . TRP B 241 ? 0.1308 0.1302 0.1253 0.0066 -0.0015 0.0048 241 TRP B CB 4956 C CG . TRP B 241 ? 0.1224 0.1102 0.1220 0.0069 -0.0053 0.0066 241 TRP B CG 4957 C CD1 . TRP B 241 ? 0.1143 0.1276 0.1423 0.0028 -0.0001 -0.0049 241 TRP B CD1 4958 C CD2 . TRP B 241 ? 0.1315 0.1145 0.1273 0.0109 -0.0138 0.0033 241 TRP B CD2 4959 N NE1 . TRP B 241 ? 0.1378 0.1414 0.1453 0.0130 0.0062 0.0209 241 TRP B NE1 4960 C CE2 . TRP B 241 ? 0.1227 0.1197 0.1427 0.0041 -0.0066 -0.0045 241 TRP B CE2 4961 C CE3 . TRP B 241 ? 0.1266 0.1437 0.1462 0.0075 0.0151 -0.0072 241 TRP B CE3 4962 C CZ2 . TRP B 241 ? 0.1312 0.1539 0.1487 -0.0029 0.0121 0.0013 241 TRP B CZ2 4963 C CZ3 . TRP B 241 ? 0.1480 0.1223 0.1720 0.0100 0.0033 -0.0024 241 TRP B CZ3 4964 C CH2 . TRP B 241 ? 0.1414 0.1393 0.1585 0.0209 0.0070 -0.0058 241 TRP B CH2 4965 N N . ASN B 242 ? 0.1217 0.1254 0.1289 0.0084 -0.0047 -0.0002 242 ASN B N 4966 C CA . ASN B 242 ? 0.1202 0.1211 0.1294 0.0027 -0.0011 0.0037 242 ASN B CA 4967 C C . ASN B 242 ? 0.1296 0.1253 0.1340 0.0050 0.0006 0.0072 242 ASN B C 4968 O O . ASN B 242 ? 0.1438 0.1133 0.1366 0.0074 -0.0065 0.0020 242 ASN B O 4969 C CB . ASN B 242 ? 0.1261 0.1262 0.1348 0.0063 0.0042 0.0012 242 ASN B CB 4970 C CG . ASN B 242 ? 0.1317 0.1265 0.1324 -0.0006 0.0091 -0.0001 242 ASN B CG 4971 O OD1 . ASN B 242 ? 0.1316 0.1438 0.1431 0.0097 0.0017 0.0062 242 ASN B OD1 4972 N ND2 . ASN B 242 ? 0.1409 0.1132 0.1248 0.0082 0.0049 -0.0065 242 ASN B ND2 4973 N N . ASN B 243 ? 0.1265 0.1136 0.1300 0.0058 -0.0064 0.0033 243 ASN B N 4974 C CA . ASN B 243 ? 0.1275 0.1183 0.1317 0.0064 -0.0026 0.0015 243 ASN B CA 4975 C C . ASN B 243 ? 0.1297 0.1222 0.1304 0.0116 -0.0049 -0.0031 243 ASN B C 4976 O O . ASN B 243 ? 0.1556 0.1314 0.1406 0.0103 -0.0032 0.0027 243 ASN B O 4977 C CB . ASN B 243 ? 0.1148 0.1306 0.1305 0.0104 -0.0102 -0.0023 243 ASN B CB 4978 C CG . ASN B 243 ? 0.1130 0.1242 0.1265 0.0055 0.0044 0.0075 243 ASN B CG 4979 O OD1 . ASN B 243 ? 0.1425 0.1200 0.1511 0.0111 -0.0185 -0.0061 243 ASN B OD1 4980 N ND2 . ASN B 243 ? 0.1425 0.1514 0.1321 0.0161 -0.0002 0.0126 243 ASN B ND2 4981 N N . TYR B 244 ? 0.1270 0.1370 0.1254 0.0156 0.0006 0.0015 244 TYR B N 4982 C CA . TYR B 244 ? 0.1347 0.1288 0.1288 0.0081 -0.0024 -0.0034 244 TYR B CA 4983 C C . TYR B 244 ? 0.1268 0.1255 0.1239 0.0083 -0.0045 0.0033 244 TYR B C 4984 O O . TYR B 244 ? 0.1412 0.1157 0.1454 0.0115 -0.0165 0.0064 244 TYR B O 4985 C CB . TYR B 244 ? 0.1394 0.1314 0.1385 0.0131 0.0027 -0.0074 244 TYR B CB 4986 C CG . TYR B 244 ? 0.1420 0.1411 0.1421 0.0079 -0.0176 -0.0033 244 TYR B CG 4987 C CD1 . TYR B 244 ? 0.1628 0.1178 0.1469 0.0138 -0.0204 0.0112 244 TYR B CD1 4988 C CD2 . TYR B 244 ? 0.1325 0.1530 0.1348 0.0147 0.0025 0.0021 244 TYR B CD2 4989 C CE1 . TYR B 244 ? 0.1509 0.1497 0.1579 0.0146 -0.0197 -0.0035 244 TYR B CE1 4990 C CE2 . TYR B 244 ? 0.1601 0.1542 0.1414 0.0063 -0.0009 0.0052 244 TYR B CE2 4991 C CZ . TYR B 244 ? 0.1514 0.1538 0.1379 0.0020 -0.0019 -0.0004 244 TYR B CZ 4992 O OH . TYR B 244 ? 0.1506 0.1561 0.1612 0.0058 -0.0121 -0.0099 244 TYR B OH 4993 N N . ARG B 245 ? 0.1340 0.1248 0.1375 0.0092 -0.0134 0.0010 245 ARG B N 4994 C CA . ARG B 245 ? 0.1372 0.1351 0.1336 0.0049 -0.0043 -0.0010 245 ARG B CA 4995 C C . ARG B 245 ? 0.1397 0.1307 0.1305 0.0063 0.0005 -0.0006 245 ARG B C 4996 O O . ARG B 245 ? 0.1326 0.1439 0.1290 0.0058 -0.0095 -0.0036 245 ARG B O 4997 C CB . ARG B 245 ? 0.1298 0.1393 0.1447 0.0060 -0.0082 -0.0092 245 ARG B CB 4998 C CG . ARG B 245 ? 0.1437 0.1524 0.1373 0.0010 0.0032 -0.0026 245 ARG B CG 4999 C CD . ARG B 245 ? 0.1595 0.1233 0.1350 0.0041 -0.0070 -0.0061 245 ARG B CD 5000 N NE . ARG B 245 ? 0.1533 0.1314 0.1631 0.0090 0.0042 -0.0090 245 ARG B NE 5001 C CZ . ARG B 245 ? 0.1553 0.1364 0.1572 -0.0018 0.0081 -0.0071 245 ARG B CZ 5002 N NH1 . ARG B 245 ? 0.1609 0.1423 0.1981 0.0070 0.0181 0.0020 245 ARG B NH1 5003 N NH2 . ARG B 245 ? 0.1662 0.1616 0.1758 0.0005 0.0143 -0.0188 245 ARG B NH2 5004 N N . VAL B 246 ? 0.1502 0.1375 0.1477 0.0009 -0.0017 0.0018 246 VAL B N 5005 C CA . VAL B 246 ? 0.1493 0.1403 0.1402 0.0067 -0.0006 -0.0022 246 VAL B CA 5006 C C . VAL B 246 ? 0.1562 0.1380 0.1414 0.0113 -0.0032 0.0020 246 VAL B C 5007 O O . VAL B 246 ? 0.1513 0.1381 0.1402 0.0244 -0.0065 -0.0083 246 VAL B O 5008 C CB . VAL B 246 ? 0.1541 0.1352 0.1358 0.0125 0.0034 -0.0013 246 VAL B CB 5009 C CG1 . VAL B 246 ? 0.1524 0.1551 0.1340 -0.0119 0.0102 -0.0096 246 VAL B CG1 5010 C CG2 . VAL B 246 ? 0.1549 0.1384 0.1232 0.0011 0.0002 -0.0188 246 VAL B CG2 5011 N N . ASN B 247 ? 0.1485 0.1468 0.1512 0.0173 -0.0151 -0.0027 247 ASN B N 5012 C CA . ASN B 247 ? 0.1525 0.1461 0.1542 0.0091 -0.0144 -0.0008 247 ASN B CA 5013 C C . ASN B 247 ? 0.1569 0.1556 0.1556 0.0139 -0.0050 -0.0017 247 ASN B C 5014 O O . ASN B 247 ? 0.1508 0.1545 0.1614 0.0308 -0.0199 0.0001 247 ASN B O 5015 C CB . ASN B 247 ? 0.1673 0.1382 0.1575 0.0082 -0.0093 0.0044 247 ASN B CB 5016 C CG . ASN B 247 ? 0.1599 0.1474 0.1491 0.0156 -0.0148 -0.0069 247 ASN B CG 5017 O OD1 . ASN B 247 ? 0.1703 0.1420 0.1501 0.0228 -0.0009 0.0134 247 ASN B OD1 5018 N ND2 . ASN B 247 ? 0.1970 0.1516 0.1497 0.0307 -0.0229 -0.0054 247 ASN B ND2 5019 N N . VAL B 248 ? 0.1528 0.1372 0.1486 0.0156 -0.0065 -0.0024 248 VAL B N 5020 C CA . VAL B 248 ? 0.1562 0.1531 0.1593 0.0113 -0.0093 0.0004 248 VAL B CA 5021 C C . VAL B 248 ? 0.1661 0.1504 0.1604 0.0123 -0.0014 -0.0012 248 VAL B C 5022 O O . VAL B 248 ? 0.1855 0.1483 0.1934 0.0208 -0.0274 -0.0171 248 VAL B O 5023 C CB . VAL B 248 ? 0.1580 0.1479 0.1523 0.0082 0.0061 -0.0009 248 VAL B CB 5024 C CG1 . VAL B 248 ? 0.1480 0.1536 0.1401 0.0092 -0.0030 0.0036 248 VAL B CG1 5025 C CG2 . VAL B 248 ? 0.1608 0.1419 0.1576 0.0217 0.0001 -0.0067 248 VAL B CG2 5026 N N . THR B 249 ? 0.1830 0.1570 0.1863 0.0150 -0.0154 -0.0100 249 THR B N 5027 C CA . THR B 249 ? 0.1912 0.1799 0.1815 0.0169 -0.0086 -0.0036 249 THR B CA 5028 C C . THR B 249 ? 0.1859 0.1860 0.1839 0.0147 -0.0158 -0.0033 249 THR B C 5029 O O . THR B 249 ? 0.1949 0.1734 0.2010 0.0220 -0.0182 -0.0162 249 THR B O 5030 C CB . THR B 249 ? 0.1973 0.1921 0.1847 0.0129 -0.0078 -0.0116 249 THR B CB 5031 O OG1 . THR B 249 ? 0.2556 0.2354 0.2144 0.0219 -0.0262 0.0119 249 THR B OG1 5032 C CG2 . THR B 249 ? 0.2186 0.1996 0.2013 0.0231 0.0019 0.0061 249 THR B CG2 5033 N N . ASP B 250 ? 0.1804 0.1811 0.1687 0.0170 -0.0211 -0.0019 250 ASP B N 5034 C CA . ASP B 250 ? 0.1833 0.1915 0.1816 0.0113 -0.0102 -0.0041 250 ASP B CA 5035 C C . ASP B 250 ? 0.1687 0.1748 0.1740 0.0026 -0.0020 -0.0035 250 ASP B C 5036 O O . ASP B 250 ? 0.1642 0.1846 0.2105 0.0083 -0.0052 0.0056 250 ASP B O 5037 C CB . ASP B 250 ? 0.1844 0.2050 0.1931 0.0134 -0.0158 -0.0047 250 ASP B CB 5038 C CG . ASP B 250 ? 0.1976 0.2338 0.2330 0.0237 -0.0076 -0.0099 250 ASP B CG 5039 O OD1 . ASP B 250 ? 0.1986 0.2542 0.2597 0.0558 -0.0306 -0.0082 250 ASP B OD1 5040 O OD2 . ASP B 250 ? 0.2113 0.3088 0.3414 0.0534 0.0011 -0.0105 250 ASP B OD2 5041 N N . TYR B 251 ? 0.1503 0.1711 0.1636 0.0106 -0.0011 -0.0026 251 TYR B N 5042 C CA . TYR B 251 ? 0.1512 0.1630 0.1655 0.0066 0.0019 0.0000 251 TYR B CA 5043 C C . TYR B 251 ? 0.1465 0.1594 0.1518 0.0042 -0.0011 -0.0017 251 TYR B C 5044 O O . TYR B 251 ? 0.1508 0.1453 0.1740 0.0162 0.0051 0.0061 251 TYR B O 5045 C CB . TYR B 251 ? 0.1449 0.1617 0.1450 0.0160 -0.0027 -0.0035 251 TYR B CB 5046 C CG . TYR B 251 ? 0.1418 0.1623 0.1593 0.0098 0.0023 0.0053 251 TYR B CG 5047 C CD1 . TYR B 251 ? 0.1474 0.1658 0.1633 0.0176 0.0016 -0.0113 251 TYR B CD1 5048 C CD2 . TYR B 251 ? 0.1455 0.1445 0.1573 0.0087 -0.0075 -0.0074 251 TYR B CD2 5049 C CE1 . TYR B 251 ? 0.1399 0.1706 0.1466 0.0078 0.0185 0.0002 251 TYR B CE1 5050 C CE2 . TYR B 251 ? 0.1343 0.1619 0.1494 0.0100 0.0031 -0.0049 251 TYR B CE2 5051 C CZ . TYR B 251 ? 0.1407 0.1475 0.1464 0.0112 0.0039 -0.0056 251 TYR B CZ 5052 O OH . TYR B 251 ? 0.1397 0.1499 0.1611 0.0136 0.0133 0.0031 251 TYR B OH 5053 N N . TYR B 252 ? 0.1350 0.1433 0.1506 0.0095 -0.0012 -0.0051 252 TYR B N 5054 C CA . TYR B 252 ? 0.1356 0.1457 0.1442 0.0083 -0.0049 -0.0042 252 TYR B CA 5055 C C . TYR B 252 ? 0.1268 0.1419 0.1391 0.0118 -0.0056 0.0032 252 TYR B C 5056 O O . TYR B 252 ? 0.1305 0.1542 0.1390 0.0055 -0.0047 0.0041 252 TYR B O 5057 C CB . TYR B 252 ? 0.1262 0.1434 0.1401 0.0111 -0.0075 -0.0082 252 TYR B CB 5058 C CG . TYR B 252 ? 0.1330 0.1339 0.1323 0.0045 -0.0114 -0.0098 252 TYR B CG 5059 C CD1 . TYR B 252 ? 0.1379 0.1309 0.1162 0.0152 -0.0127 0.0026 252 TYR B CD1 5060 C CD2 . TYR B 252 ? 0.1337 0.1349 0.1262 0.0110 -0.0010 0.0037 252 TYR B CD2 5061 C CE1 . TYR B 252 ? 0.1217 0.1233 0.1240 0.0140 -0.0019 -0.0008 252 TYR B CE1 5062 C CE2 . TYR B 252 ? 0.0997 0.1440 0.1254 0.0058 -0.0148 -0.0108 252 TYR B CE2 5063 C CZ . TYR B 252 ? 0.1075 0.1412 0.1275 0.0003 -0.0152 -0.0042 252 TYR B CZ 5064 O OH . TYR B 252 ? 0.1159 0.1314 0.1274 0.0099 -0.0115 0.0014 252 TYR B OH 5065 N N . GLY B 253 ? 0.1331 0.1605 0.1423 0.0026 0.0022 -0.0028 253 GLY B N 5066 C CA . GLY B 253 ? 0.1342 0.1546 0.1521 0.0124 -0.0005 -0.0048 253 GLY B CA 5067 C C . GLY B 253 ? 0.1346 0.1542 0.1474 0.0062 -0.0029 0.0000 253 GLY B C 5068 O O . GLY B 253 ? 0.1116 0.1669 0.1630 0.0127 -0.0010 0.0049 253 GLY B O 5069 N N . ARG B 254 ? 0.1514 0.1623 0.1581 -0.0003 -0.0004 -0.0039 254 ARG B N 5070 C CA . ARG B 254 ? 0.1507 0.1656 0.1652 0.0014 -0.0074 0.0022 254 ARG B CA 5071 C C . ARG B 254 ? 0.1665 0.1943 0.1761 -0.0013 -0.0085 0.0019 254 ARG B C 5072 O O . ARG B 254 ? 0.1749 0.2335 0.2001 0.0137 -0.0203 0.0109 254 ARG B O 5073 C CB . ARG B 254 ? 0.1467 0.1652 0.1674 -0.0021 -0.0138 -0.0017 254 ARG B CB 5074 C CG . ARG B 254 ? 0.1335 0.1630 0.1618 0.0154 -0.0059 -0.0053 254 ARG B CG 5075 C CD . ARG B 254 ? 0.1539 0.1664 0.1575 0.0100 -0.0206 0.0020 254 ARG B CD 5076 N NE . ARG B 254 ? 0.1450 0.1708 0.1486 0.0009 -0.0227 -0.0118 254 ARG B NE 5077 C CZ . ARG B 254 ? 0.1634 0.1666 0.1559 0.0020 -0.0137 -0.0066 254 ARG B CZ 5078 N NH1 . ARG B 254 ? 0.1785 0.1500 0.1449 -0.0012 -0.0292 -0.0108 254 ARG B NH1 5079 N NH2 . ARG B 254 ? 0.1778 0.1709 0.1846 -0.0074 -0.0292 -0.0037 254 ARG B NH2 5080 N N . GLY B 255 ? 0.1437 0.2116 0.1802 0.0005 -0.0118 0.0029 255 GLY B N 5081 C CA . GLY B 255 ? 0.1739 0.2176 0.2152 0.0038 -0.0110 0.0042 255 GLY B CA 5082 C C . GLY B 255 ? 0.1881 0.2274 0.2198 -0.0016 -0.0060 -0.0001 255 GLY B C 5083 O O . GLY B 255 ? 0.1767 0.2245 0.2118 0.0071 -0.0032 -0.0055 255 GLY B O 5084 N N . GLU B 256 ? 0.2026 0.2447 0.2521 -0.0012 -0.0122 0.0033 256 GLU B N 5085 C CA . GLU B 256 ? 0.2252 0.2611 0.2635 0.0004 -0.0082 -0.0003 256 GLU B CA 5086 C C . GLU B 256 ? 0.2114 0.2582 0.2553 -0.0016 -0.0143 -0.0064 256 GLU B C 5087 O O . GLU B 256 ? 0.2200 0.2763 0.2795 -0.0004 -0.0004 -0.0133 256 GLU B O 5088 C CB . GLU B 256 ? 0.2213 0.2610 0.2706 -0.0002 -0.0131 0.0009 256 GLU B CB 5089 C CG . GLU B 256 ? 0.2576 0.2844 0.3132 -0.0098 -0.0107 0.0022 256 GLU B CG 5090 C CD . GLU B 256 ? 0.2854 0.3252 0.3294 -0.0116 -0.0008 0.0102 256 GLU B CD 5091 O OE1 . GLU B 256 ? 0.3469 0.4520 0.4137 -0.0087 -0.0237 0.0046 256 GLU B OE1 5092 O OE2 . GLU B 256 ? 0.3577 0.3961 0.3816 -0.0284 0.0200 0.0254 256 GLU B OE2 5093 N N . GLU B 257 ? 0.1987 0.2468 0.2533 0.0011 -0.0139 -0.0040 257 GLU B N 5094 C CA . GLU B 257 ? 0.2186 0.2437 0.2484 0.0001 -0.0139 -0.0028 257 GLU B CA 5095 C C . GLU B 257 ? 0.2132 0.2291 0.2409 0.0033 -0.0189 -0.0004 257 GLU B C 5096 O O . GLU B 257 ? 0.2159 0.2425 0.2624 0.0109 -0.0341 0.0009 257 GLU B O 5097 C CB . GLU B 257 ? 0.2458 0.2543 0.2580 0.0019 -0.0184 -0.0001 257 GLU B CB 5098 C CG . GLU B 257 ? 0.2764 0.2883 0.2946 0.0057 -0.0096 0.0069 257 GLU B CG 5099 C CD . GLU B 257 ? 0.3245 0.3251 0.3124 0.0112 -0.0124 -0.0052 257 GLU B CD 5100 O OE1 . GLU B 257 ? 0.3437 0.3593 0.3156 0.0076 -0.0141 0.0076 257 GLU B OE1 5101 O OE2 . GLU B 257 ? 0.3309 0.3730 0.3674 0.0123 0.0096 0.0060 257 GLU B OE2 5102 N N . PHE B 258 ? 0.1894 0.2008 0.2139 0.0066 -0.0137 -0.0018 258 PHE B N 5103 C CA . PHE B 258 ? 0.1789 0.1957 0.2088 0.0100 -0.0095 -0.0024 258 PHE B CA 5104 C C . PHE B 258 ? 0.1578 0.1926 0.2119 0.0157 -0.0128 0.0055 258 PHE B C 5105 O O . PHE B 258 ? 0.1609 0.2046 0.2153 0.0038 -0.0161 0.0126 258 PHE B O 5106 C CB . PHE B 258 ? 0.1533 0.1925 0.1890 0.0097 -0.0112 -0.0039 258 PHE B CB 5107 C CG . PHE B 258 ? 0.1509 0.1675 0.1827 0.0249 -0.0125 -0.0001 258 PHE B CG 5108 C CD1 . PHE B 258 ? 0.1439 0.1709 0.1917 0.0209 -0.0102 -0.0037 258 PHE B CD1 5109 C CD2 . PHE B 258 ? 0.1586 0.1519 0.1919 0.0051 -0.0142 0.0013 258 PHE B CD2 5110 C CE1 . PHE B 258 ? 0.1490 0.1621 0.1806 0.0218 -0.0145 -0.0058 258 PHE B CE1 5111 C CE2 . PHE B 258 ? 0.1435 0.1544 0.1792 0.0153 -0.0241 -0.0035 258 PHE B CE2 5112 C CZ . PHE B 258 ? 0.1414 0.1829 0.1709 0.0071 -0.0198 -0.0066 258 PHE B CZ 5113 N N . LYS B 259 ? 0.1706 0.1994 0.2062 0.0178 -0.0033 0.0023 259 LYS B N 5114 C CA . LYS B 259 ? 0.1841 0.2054 0.2031 0.0130 -0.0007 0.0057 259 LYS B CA 5115 C C . LYS B 259 ? 0.1735 0.2000 0.2062 0.0110 0.0026 0.0057 259 LYS B C 5116 O O . LYS B 259 ? 0.1713 0.2240 0.2113 0.0145 0.0114 0.0128 259 LYS B O 5117 C CB . LYS B 259 ? 0.2077 0.2236 0.2164 0.0118 0.0043 0.0044 259 LYS B CB 5118 C CG . LYS B 259 ? 0.2743 0.2578 0.2648 0.0128 -0.0034 0.0095 259 LYS B CG 5119 C CD . LYS B 259 ? 0.3148 0.2997 0.2961 0.0172 0.0058 0.0130 259 LYS B CD 5120 C CE . LYS B 259 ? 0.2681 0.2552 0.2977 0.0205 0.0125 0.0081 259 LYS B CE 5121 N NZ . LYS B 259 ? 0.2781 0.2729 0.3082 0.0173 -0.0051 0.0180 259 LYS B NZ 5122 N N . VAL B 260 ? 0.1436 0.1923 0.1858 0.0039 -0.0006 -0.0013 260 VAL B N 5123 C CA . VAL B 260 ? 0.1623 0.1809 0.1785 -0.0019 -0.0067 -0.0010 260 VAL B CA 5124 C C . VAL B 260 ? 0.1388 0.1669 0.1666 0.0033 -0.0036 -0.0010 260 VAL B C 5125 O O . VAL B 260 ? 0.1548 0.1792 0.1740 0.0004 -0.0086 -0.0043 260 VAL B O 5126 C CB . VAL B 260 ? 0.1574 0.1822 0.1762 0.0066 0.0005 -0.0049 260 VAL B CB 5127 C CG1 . VAL B 260 ? 0.1497 0.1638 0.1737 0.0028 -0.0039 -0.0030 260 VAL B CG1 5128 C CG2 . VAL B 260 ? 0.1789 0.1747 0.1875 0.0004 0.0001 -0.0108 260 VAL B CG2 5129 N N . ASN B 261 ? 0.1409 0.1713 0.1759 0.0043 -0.0084 -0.0058 261 ASN B N 5130 C CA . ASN B 261 ? 0.1372 0.1655 0.1680 0.0010 -0.0039 0.0022 261 ASN B CA 5131 C C . ASN B 261 ? 0.1413 0.1654 0.1685 -0.0056 -0.0040 0.0017 261 ASN B C 5132 O O . ASN B 261 ? 0.1251 0.1611 0.1713 -0.0080 0.0001 -0.0010 261 ASN B O 5133 C CB . ASN B 261 ? 0.1447 0.1767 0.1832 0.0002 0.0020 -0.0037 261 ASN B CB 5134 C CG . ASN B 261 ? 0.1542 0.2023 0.1853 0.0008 -0.0054 -0.0079 261 ASN B CG 5135 O OD1 . ASN B 261 ? 0.1399 0.2156 0.1843 -0.0015 0.0060 0.0005 261 ASN B OD1 5136 N ND2 . ASN B 261 ? 0.1749 0.2473 0.2425 -0.0276 -0.0024 0.0014 261 ASN B ND2 5137 N N . THR B 262 ? 0.1461 0.1556 0.1494 0.0010 -0.0072 -0.0012 262 THR B N 5138 C CA . THR B 262 ? 0.1370 0.1534 0.1549 -0.0009 -0.0077 0.0017 262 THR B CA 5139 C C . THR B 262 ? 0.1338 0.1524 0.1514 0.0024 -0.0066 -0.0051 262 THR B C 5140 O O . THR B 262 ? 0.1231 0.1513 0.1620 -0.0095 -0.0174 -0.0032 262 THR B O 5141 C CB . THR B 262 ? 0.1295 0.1448 0.1405 0.0057 -0.0048 0.0003 262 THR B CB 5142 O OG1 . THR B 262 ? 0.1187 0.1414 0.1435 -0.0044 -0.0027 0.0058 262 THR B OG1 5143 C CG2 . THR B 262 ? 0.1236 0.1603 0.1517 0.0042 -0.0071 0.0082 262 THR B CG2 5144 N N . LEU B 263 ? 0.1336 0.1535 0.1692 -0.0028 -0.0105 -0.0004 263 LEU B N 5145 C CA . LEU B 263 ? 0.1456 0.1627 0.1636 -0.0056 -0.0043 -0.0009 263 LEU B CA 5146 C C . LEU B 263 ? 0.1544 0.1729 0.1761 -0.0066 -0.0020 0.0044 263 LEU B C 5147 O O . LEU B 263 ? 0.1739 0.1881 0.1933 -0.0112 -0.0033 -0.0041 263 LEU B O 5148 C CB . LEU B 263 ? 0.1587 0.1718 0.1802 -0.0048 -0.0116 0.0054 263 LEU B CB 5149 C CG . LEU B 263 ? 0.1608 0.1813 0.1726 -0.0097 -0.0072 0.0000 263 LEU B CG 5150 C CD1 . LEU B 263 ? 0.1823 0.2211 0.1888 -0.0202 -0.0132 0.0071 263 LEU B CD1 5151 C CD2 . LEU B 263 ? 0.1990 0.1777 0.1721 -0.0143 -0.0080 -0.0038 263 LEU B CD2 5152 N N . LYS B 264 ? 0.1382 0.1647 0.1739 -0.0108 -0.0066 -0.0097 264 LYS B N 5153 C CA . LYS B 264 ? 0.1720 0.1891 0.1823 -0.0045 -0.0058 -0.0025 264 LYS B CA 5154 C C . LYS B 264 ? 0.1614 0.1772 0.1704 -0.0061 -0.0052 -0.0031 264 LYS B C 5155 O O . LYS B 264 ? 0.1410 0.1593 0.1639 -0.0070 0.0132 -0.0011 264 LYS B O 5156 C CB . LYS B 264 ? 0.1804 0.2130 0.1927 -0.0038 -0.0028 -0.0020 264 LYS B CB 5157 C CG . LYS B 264 ? 0.2096 0.2397 0.2154 -0.0125 -0.0060 0.0041 264 LYS B CG 5158 C CD . LYS B 264 ? 0.2194 0.2665 0.2354 0.0060 -0.0087 0.0038 264 LYS B CD 5159 C CE . LYS B 264 ? 0.2561 0.3050 0.2940 -0.0027 0.0000 0.0068 264 LYS B CE 5160 N NZ . LYS B 264 ? 0.2615 0.3425 0.3241 -0.0029 0.0076 -0.0054 264 LYS B NZ 5161 N N . PRO B 265 ? 0.1611 0.1608 0.1741 -0.0097 -0.0034 -0.0022 265 PRO B N 5162 C CA . PRO B 265 ? 0.1645 0.1644 0.1660 -0.0018 -0.0018 -0.0022 265 PRO B CA 5163 C C . PRO B 265 ? 0.1538 0.1547 0.1660 -0.0006 0.0001 -0.0011 265 PRO B C 5164 O O . PRO B 265 ? 0.1506 0.1664 0.1758 -0.0009 -0.0052 0.0054 265 PRO B O 5165 C CB . PRO B 265 ? 0.1683 0.1668 0.1677 0.0010 0.0018 0.0043 265 PRO B CB 5166 C CG . PRO B 265 ? 0.1907 0.1895 0.2056 0.0000 -0.0094 -0.0008 265 PRO B CG 5167 C CD . PRO B 265 ? 0.1776 0.1707 0.1739 -0.0135 -0.0034 0.0003 265 PRO B CD 5168 N N . PHE B 266 ? 0.1380 0.1548 0.1541 -0.0031 -0.0025 0.0000 266 PHE B N 5169 C CA . PHE B 266 ? 0.1265 0.1515 0.1444 0.0013 0.0046 -0.0039 266 PHE B CA 5170 C C . PHE B 266 ? 0.1293 0.1453 0.1331 0.0060 0.0028 -0.0050 266 PHE B C 5171 O O . PHE B 266 ? 0.1172 0.1639 0.1321 0.0109 0.0141 -0.0118 266 PHE B O 5172 C CB . PHE B 266 ? 0.1313 0.1585 0.1410 -0.0042 0.0021 -0.0055 266 PHE B CB 5173 C CG . PHE B 266 ? 0.1225 0.1391 0.1481 0.0058 0.0057 0.0005 266 PHE B CG 5174 C CD1 . PHE B 266 ? 0.1406 0.1599 0.1565 -0.0025 -0.0076 0.0055 266 PHE B CD1 5175 C CD2 . PHE B 266 ? 0.1333 0.1331 0.1515 -0.0010 -0.0132 -0.0076 266 PHE B CD2 5176 C CE1 . PHE B 266 ? 0.1301 0.1450 0.1425 -0.0145 -0.0117 -0.0072 266 PHE B CE1 5177 C CE2 . PHE B 266 ? 0.1243 0.1632 0.1440 -0.0085 -0.0140 -0.0132 266 PHE B CE2 5178 C CZ . PHE B 266 ? 0.1238 0.1218 0.1543 -0.0026 0.0027 0.0051 266 PHE B CZ 5179 N N . THR B 267 ? 0.1323 0.1411 0.1288 0.0033 0.0041 -0.0109 267 THR B N 5180 C CA . THR B 267 ? 0.1326 0.1472 0.1430 0.0024 0.0061 -0.0005 267 THR B CA 5181 C C . THR B 267 ? 0.1238 0.1309 0.1303 0.0082 0.0076 -0.0015 267 THR B C 5182 O O . THR B 267 ? 0.1197 0.1404 0.1446 0.0027 0.0106 0.0032 267 THR B O 5183 C CB . THR B 267 ? 0.1531 0.1399 0.1456 0.0000 0.0101 0.0049 267 THR B CB 5184 O OG1 . THR B 267 ? 0.1751 0.1774 0.1767 -0.0248 0.0158 0.0117 267 THR B OG1 5185 C CG2 . THR B 267 ? 0.1604 0.1601 0.1562 0.0011 0.0082 -0.0010 267 THR B CG2 5186 N N . VAL B 268 ? 0.1181 0.1286 0.1213 -0.0034 0.0055 0.0010 268 VAL B N 5187 C CA . VAL B 268 ? 0.1256 0.1340 0.1348 0.0049 0.0065 -0.0008 268 VAL B CA 5188 C C . VAL B 268 ? 0.1194 0.1286 0.1300 0.0078 0.0070 -0.0046 268 VAL B C 5189 O O . VAL B 268 ? 0.1350 0.1304 0.1228 0.0079 0.0063 -0.0031 268 VAL B O 5190 C CB . VAL B 268 ? 0.1090 0.1243 0.1232 0.0027 -0.0008 -0.0056 268 VAL B CB 5191 C CG1 . VAL B 268 ? 0.1264 0.1273 0.1326 -0.0014 0.0014 -0.0033 268 VAL B CG1 5192 C CG2 . VAL B 268 ? 0.1347 0.1323 0.1250 -0.0039 0.0171 -0.0049 268 VAL B CG2 5193 N N . VAL B 269 ? 0.1267 0.1312 0.1326 0.0083 0.0016 0.0030 269 VAL B N 5194 C CA . VAL B 269 ? 0.1167 0.1273 0.1261 0.0078 0.0097 -0.0027 269 VAL B CA 5195 C C . VAL B 269 ? 0.1241 0.1247 0.1325 0.0066 0.0070 -0.0055 269 VAL B C 5196 O O . VAL B 269 ? 0.1124 0.1235 0.1316 0.0195 0.0194 -0.0065 269 VAL B O 5197 C CB . VAL B 269 ? 0.1166 0.1419 0.1374 0.0082 0.0080 -0.0101 269 VAL B CB 5198 C CG1 . VAL B 269 ? 0.1414 0.1530 0.1310 0.0173 0.0079 -0.0082 269 VAL B CG1 5199 C CG2 . VAL B 269 ? 0.1326 0.1412 0.1327 0.0024 -0.0018 -0.0114 269 VAL B CG2 5200 N N . THR B 270 ? 0.1230 0.1147 0.1224 0.0032 0.0080 -0.0038 270 THR B N 5201 C CA . THR B 270 ? 0.1222 0.1211 0.1334 0.0059 0.0072 -0.0058 270 THR B CA 5202 C C . THR B 270 ? 0.1339 0.1254 0.1340 0.0054 0.0004 -0.0026 270 THR B C 5203 O O . THR B 270 ? 0.1396 0.1140 0.1414 0.0100 0.0046 -0.0034 270 THR B O 5204 C CB . THR B 270 ? 0.1332 0.1064 0.1390 0.0035 0.0092 -0.0086 270 THR B CB 5205 O OG1 . THR B 270 ? 0.1334 0.1330 0.1377 0.0109 0.0033 -0.0003 270 THR B OG1 5206 C CG2 . THR B 270 ? 0.1257 0.1290 0.1484 -0.0054 0.0093 -0.0083 270 THR B CG2 5207 N N . GLN B 271 ? 0.1384 0.1220 0.1413 0.0134 -0.0031 -0.0020 271 GLN B N 5208 C CA . GLN B 271 ? 0.1338 0.1322 0.1309 0.0069 0.0077 -0.0047 271 GLN B CA 5209 C C . GLN B 271 ? 0.1296 0.1236 0.1233 0.0051 0.0110 -0.0020 271 GLN B C 5210 O O . GLN B 271 ? 0.1496 0.1523 0.1279 0.0080 -0.0027 0.0046 271 GLN B O 5211 C CB . GLN B 271 ? 0.1399 0.1423 0.1336 0.0199 0.0109 0.0006 271 GLN B CB 5212 C CG . GLN B 271 ? 0.1580 0.1475 0.1522 0.0163 0.0040 -0.0098 271 GLN B CG 5213 C CD . GLN B 271 ? 0.1518 0.1456 0.1511 0.0107 0.0066 -0.0044 271 GLN B CD 5214 O OE1 . GLN B 271 ? 0.1545 0.1604 0.1812 0.0160 0.0211 0.0130 271 GLN B OE1 5215 N NE2 . GLN B 271 ? 0.1511 0.1910 0.1685 0.0029 0.0173 -0.0064 271 GLN B NE2 5216 N N . PHE B 272 ? 0.1320 0.1400 0.1301 -0.0075 0.0102 -0.0037 272 PHE B N 5217 C CA . PHE B 272 ? 0.1316 0.1356 0.1342 0.0003 0.0095 -0.0074 272 PHE B CA 5218 C C . PHE B 272 ? 0.1497 0.1423 0.1304 -0.0019 0.0009 -0.0116 272 PHE B C 5219 O O . PHE B 272 ? 0.1626 0.1489 0.1391 0.0139 0.0057 -0.0108 272 PHE B O 5220 C CB . PHE B 272 ? 0.1278 0.1318 0.1249 -0.0016 0.0034 -0.0067 272 PHE B CB 5221 C CG . PHE B 272 ? 0.1141 0.1256 0.1270 0.0104 0.0054 -0.0007 272 PHE B CG 5222 C CD1 . PHE B 272 ? 0.1322 0.1242 0.1184 0.0054 0.0075 0.0035 272 PHE B CD1 5223 C CD2 . PHE B 272 ? 0.1621 0.1224 0.1379 0.0007 0.0224 0.0092 272 PHE B CD2 5224 C CE1 . PHE B 272 ? 0.1327 0.1484 0.1187 0.0138 0.0173 -0.0080 272 PHE B CE1 5225 C CE2 . PHE B 272 ? 0.1437 0.1365 0.1514 -0.0095 0.0030 -0.0055 272 PHE B CE2 5226 C CZ . PHE B 272 ? 0.1561 0.1616 0.1461 0.0060 -0.0030 -0.0194 272 PHE B CZ 5227 N N . LEU B 273 ? 0.1463 0.1503 0.1356 0.0031 0.0055 -0.0135 273 LEU B N 5228 C CA . LEU B 273 ? 0.1609 0.1639 0.1529 0.0005 0.0102 -0.0095 273 LEU B CA 5229 C C . LEU B 273 ? 0.1856 0.1588 0.1741 -0.0024 0.0106 -0.0117 273 LEU B C 5230 O O . LEU B 273 ? 0.1791 0.1374 0.1679 0.0050 0.0113 -0.0244 273 LEU B O 5231 C CB . LEU B 273 ? 0.1759 0.1547 0.1488 0.0031 0.0118 -0.0060 273 LEU B CB 5232 C CG . LEU B 273 ? 0.1682 0.1969 0.1920 0.0063 0.0069 -0.0061 273 LEU B CG 5233 C CD1 . LEU B 273 ? 0.1947 0.2389 0.2156 0.0055 0.0034 0.0069 273 LEU B CD1 5234 C CD2 . LEU B 273 ? 0.1977 0.2285 0.2134 -0.0010 -0.0026 -0.0029 273 LEU B CD2 5235 N N . ALA B 274 ? 0.1934 0.1940 0.1911 -0.0062 0.0071 -0.0095 274 ALA B N 5236 C CA . ALA B 274 ? 0.2140 0.2223 0.2183 -0.0045 0.0051 -0.0172 274 ALA B CA 5237 C C . ALA B 274 ? 0.2357 0.2486 0.2557 -0.0022 0.0094 -0.0256 274 ALA B C 5238 O O . ALA B 274 ? 0.2524 0.2577 0.2680 -0.0033 0.0135 -0.0529 274 ALA B O 5239 C CB . ALA B 274 ? 0.2281 0.2314 0.2233 -0.0161 -0.0023 -0.0096 274 ALA B CB 5240 N N . ASN B 275 ? 0.2614 0.2575 0.2741 0.0041 0.0217 -0.0366 275 ASN B N 5241 C CA . ASN B 275 ? 0.2918 0.2812 0.3050 0.0032 0.0093 -0.0241 275 ASN B CA 5242 C C . ASN B 275 ? 0.3197 0.3266 0.3252 0.0017 0.0081 -0.0196 275 ASN B C 5243 O O . ASN B 275 ? 0.3092 0.3376 0.3149 0.0038 0.0169 -0.0398 275 ASN B O 5244 C CB . ASN B 275 ? 0.2936 0.2995 0.3220 0.0037 0.0078 -0.0241 275 ASN B CB 5245 C CG . ASN B 275 ? 0.3102 0.3022 0.3389 0.0072 0.0010 -0.0325 275 ASN B CG 5246 O OD1 . ASN B 275 ? 0.3222 0.2883 0.3593 0.0024 -0.0118 -0.0546 275 ASN B OD1 5247 N ND2 . ASN B 275 ? 0.3436 0.3184 0.4045 0.0125 0.0103 -0.0275 275 ASN B ND2 5248 N N . ARG B 276 ? 0.3644 0.3672 0.3702 0.0047 0.0085 -0.0141 276 ARG B N 5249 C CA . ARG B 276 ? 0.3961 0.3994 0.3885 0.0010 0.0014 -0.0032 276 ARG B CA 5250 C C . ARG B 276 ? 0.4027 0.4123 0.3995 0.0025 0.0046 0.0010 276 ARG B C 5251 O O . ARG B 276 ? 0.4315 0.4362 0.4040 -0.0016 0.0016 0.0077 276 ARG B O 5252 C CB . ARG B 276 ? 0.4119 0.4112 0.4074 0.0021 0.0029 -0.0054 276 ARG B CB 5253 C CG . ARG B 276 ? 0.4444 0.4516 0.4537 0.0024 -0.0065 -0.0047 276 ARG B CG 5254 C CD . ARG B 276 ? 0.5058 0.5104 0.5093 -0.0037 0.0058 0.0041 276 ARG B CD 5255 N NE . ARG B 276 ? 0.5369 0.5368 0.5389 -0.0003 -0.0005 0.0004 276 ARG B NE 5256 C CZ . ARG B 276 ? 0.5570 0.5572 0.5483 0.0029 0.0009 -0.0040 276 ARG B CZ 5257 N NH1 . ARG B 276 ? 0.5734 0.5723 0.5534 0.0012 0.0011 0.0006 276 ARG B NH1 5258 N NH2 . ARG B 276 ? 0.5576 0.5585 0.5454 0.0067 0.0002 -0.0027 276 ARG B NH2 5259 N N . ARG B 277 ? 0.4032 0.4089 0.3956 -0.0009 0.0028 -0.0023 277 ARG B N 5260 C CA . ARG B 277 ? 0.3934 0.3964 0.3847 0.0008 0.0003 -0.0074 277 ARG B CA 5261 C C . ARG B 277 ? 0.3710 0.3852 0.3653 -0.0004 -0.0006 -0.0063 277 ARG B C 5262 O O . ARG B 277 ? 0.3839 0.4167 0.3584 0.0025 -0.0124 -0.0119 277 ARG B O 5263 C CB . ARG B 277 ? 0.4018 0.4017 0.3977 -0.0019 0.0031 -0.0036 277 ARG B CB 5264 C CG . ARG B 277 ? 0.4325 0.4295 0.4330 0.0012 0.0015 -0.0077 277 ARG B CG 5265 C CD . ARG B 277 ? 0.4700 0.4505 0.4586 -0.0038 0.0071 0.0000 277 ARG B CD 5266 N NE . ARG B 277 ? 0.5017 0.5182 0.5188 0.0033 -0.0038 -0.0019 277 ARG B NE 5267 C CZ . ARG B 277 ? 0.5309 0.5372 0.5379 -0.0008 -0.0057 -0.0066 277 ARG B CZ 5268 N NH1 . ARG B 277 ? 0.5495 0.5514 0.5612 0.0019 -0.0016 -0.0004 277 ARG B NH1 5269 N NH2 . ARG B 277 ? 0.5321 0.5340 0.5462 0.0005 -0.0036 -0.0127 277 ARG B NH2 5270 N N . GLY B 278 ? 0.3390 0.3541 0.3193 -0.0039 -0.0006 -0.0049 278 GLY B N 5271 C CA . GLY B 278 ? 0.3126 0.3259 0.2888 -0.0021 0.0038 0.0001 278 GLY B CA 5272 C C . GLY B 278 ? 0.2825 0.2889 0.2545 -0.0047 -0.0038 -0.0028 278 GLY B C 5273 O O . GLY B 278 ? 0.3021 0.2933 0.2634 -0.0008 -0.0122 0.0133 278 GLY B O 5274 N N . LYS B 279 ? 0.2379 0.2467 0.2159 -0.0078 -0.0065 -0.0188 279 LYS B N 5275 C CA . LYS B 279 ? 0.2122 0.2198 0.2053 -0.0038 -0.0058 -0.0123 279 LYS B CA 5276 C C . LYS B 279 ? 0.1900 0.1922 0.1808 -0.0002 -0.0006 -0.0129 279 LYS B C 5277 O O . LYS B 279 ? 0.1863 0.1795 0.1612 0.0015 0.0092 -0.0363 279 LYS B O 5278 C CB . LYS B 279 ? 0.2156 0.2161 0.1918 -0.0038 -0.0091 -0.0112 279 LYS B CB 5279 C CG . LYS B 279 ? 0.2064 0.2264 0.2061 -0.0083 -0.0090 -0.0127 279 LYS B CG 5280 C CD . LYS B 279 ? 0.2238 0.2141 0.1936 -0.0126 -0.0174 -0.0029 279 LYS B CD 5281 C CE . LYS B 279 ? 0.2119 0.2366 0.1986 -0.0157 -0.0097 0.0004 279 LYS B CE 5282 N NZ . LYS B 279 ? 0.2155 0.2423 0.2080 -0.0118 -0.0195 -0.0041 279 LYS B NZ 5283 N N . LEU B 280 ? 0.1657 0.1608 0.1670 0.0017 -0.0055 -0.0197 280 LEU B N 5284 C CA . LEU B 280 ? 0.1647 0.1659 0.1689 0.0045 -0.0022 -0.0098 280 LEU B CA 5285 C C . LEU B 280 ? 0.1665 0.1628 0.1582 0.0021 0.0071 -0.0114 280 LEU B C 5286 O O . LEU B 280 ? 0.1727 0.1499 0.1794 0.0062 0.0059 -0.0128 280 LEU B O 5287 C CB . LEU B 280 ? 0.1559 0.1482 0.1619 0.0040 0.0011 -0.0076 280 LEU B CB 5288 C CG . LEU B 280 ? 0.1425 0.1485 0.1602 0.0042 0.0011 -0.0029 280 LEU B CG 5289 C CD1 . LEU B 280 ? 0.1310 0.1483 0.1621 -0.0016 0.0096 -0.0083 280 LEU B CD1 5290 C CD2 . LEU B 280 ? 0.1471 0.1533 0.1438 -0.0023 -0.0029 -0.0092 280 LEU B CD2 5291 N N . GLU B 281 ? 0.1716 0.1578 0.1564 0.0110 0.0026 -0.0125 281 GLU B N 5292 C CA . GLU B 281 ? 0.1986 0.1855 0.1873 0.0047 -0.0026 -0.0041 281 GLU B CA 5293 C C . GLU B 281 ? 0.1815 0.1565 0.1674 0.0090 0.0005 -0.0049 281 GLU B C 5294 O O . GLU B 281 ? 0.2111 0.1395 0.1657 0.0051 0.0058 -0.0162 281 GLU B O 5295 C CB . GLU B 281 ? 0.2174 0.1839 0.1895 0.0118 -0.0119 -0.0144 281 GLU B CB 5296 C CG . GLU B 281 ? 0.2757 0.2682 0.2801 0.0023 -0.0073 -0.0166 281 GLU B CG 5297 C CD . GLU B 281 ? 0.2936 0.2767 0.2777 0.0081 0.0032 -0.0304 281 GLU B CD 5298 O OE1 . GLU B 281 ? 0.3321 0.4080 0.3306 0.0351 -0.0102 -0.0434 281 GLU B OE1 5299 O OE2 . GLU B 281 ? 0.4456 0.4078 0.3677 -0.0132 -0.0203 -0.0370 281 GLU B OE2 5300 N N . LYS B 282 ? 0.1789 0.1595 0.1639 -0.0039 -0.0032 -0.0042 282 LYS B N 5301 C CA . LYS B 282 ? 0.1840 0.1726 0.1803 0.0005 -0.0054 0.0000 282 LYS B CA 5302 C C . LYS B 282 ? 0.1550 0.1567 0.1567 0.0007 -0.0046 -0.0059 282 LYS B C 5303 O O . LYS B 282 ? 0.1840 0.1455 0.1416 -0.0109 0.0019 -0.0050 282 LYS B O 5304 C CB . LYS B 282 ? 0.1788 0.2042 0.2007 -0.0023 -0.0109 -0.0010 282 LYS B CB 5305 C CG . LYS B 282 ? 0.2384 0.2501 0.2534 -0.0033 -0.0072 -0.0142 282 LYS B CG 5306 C CD . LYS B 282 ? 0.2480 0.2495 0.2718 0.0076 0.0000 -0.0059 282 LYS B CD 5307 C CE . LYS B 282 ? 0.3035 0.2788 0.3140 0.0136 0.0053 -0.0102 282 LYS B CE 5308 N NZ . LYS B 282 ? 0.3439 0.3465 0.3567 0.0167 0.0150 -0.0175 282 LYS B NZ 5309 N N . ILE B 283 ? 0.1470 0.1362 0.1384 0.0060 0.0073 -0.0037 283 ILE B N 5310 C CA . ILE B 283 ? 0.1411 0.1352 0.1405 0.0020 -0.0010 -0.0010 283 ILE B CA 5311 C C . ILE B 283 ? 0.1437 0.1295 0.1227 0.0046 -0.0053 -0.0088 283 ILE B C 5312 O O . ILE B 283 ? 0.1570 0.1305 0.1537 0.0058 0.0050 -0.0029 283 ILE B O 5313 C CB . ILE B 283 ? 0.1519 0.1379 0.1295 -0.0004 0.0061 -0.0057 283 ILE B CB 5314 C CG1 . ILE B 283 ? 0.1521 0.1425 0.1516 0.0150 -0.0017 -0.0031 283 ILE B CG1 5315 C CG2 . ILE B 283 ? 0.1623 0.1442 0.1614 0.0013 0.0053 -0.0002 283 ILE B CG2 5316 C CD1 . ILE B 283 ? 0.1563 0.1564 0.1461 0.0056 -0.0093 -0.0108 283 ILE B CD1 5317 N N . HIS B 284 ? 0.1383 0.1328 0.1335 0.0141 0.0011 -0.0058 284 HIS B N 5318 C CA . HIS B 284 ? 0.1368 0.1350 0.1436 0.0037 0.0008 -0.0083 284 HIS B CA 5319 C C . HIS B 284 ? 0.1339 0.1250 0.1314 0.0056 0.0066 -0.0058 284 HIS B C 5320 O O . HIS B 284 ? 0.1507 0.1301 0.1417 0.0134 0.0110 0.0006 284 HIS B O 5321 C CB . HIS B 284 ? 0.1562 0.1410 0.1329 0.0022 -0.0029 -0.0146 284 HIS B CB 5322 C CG . HIS B 284 ? 0.1524 0.1525 0.1472 0.0095 0.0016 -0.0137 284 HIS B CG 5323 N ND1 . HIS B 284 ? 0.1490 0.1619 0.1786 0.0079 0.0069 -0.0042 284 HIS B ND1 5324 C CD2 . HIS B 284 ? 0.1495 0.1435 0.1622 0.0239 0.0135 -0.0187 284 HIS B CD2 5325 C CE1 . HIS B 284 ? 0.1391 0.1991 0.1795 0.0043 0.0091 -0.0069 284 HIS B CE1 5326 N NE2 . HIS B 284 ? 0.1746 0.1747 0.1808 0.0107 0.0202 -0.0108 284 HIS B NE2 5327 N N . ARG B 285 ? 0.1295 0.1264 0.1389 0.0014 0.0108 -0.0043 285 ARG B N 5328 C CA . ARG B 285 ? 0.1269 0.1312 0.1320 0.0012 0.0063 -0.0015 285 ARG B CA 5329 C C . ARG B 285 ? 0.1257 0.1275 0.1409 0.0090 0.0071 0.0087 285 ARG B C 5330 O O . ARG B 285 ? 0.1300 0.1372 0.1531 0.0135 0.0173 0.0068 285 ARG B O 5331 C CB . ARG B 285 ? 0.1087 0.1311 0.1198 0.0070 0.0004 -0.0029 285 ARG B CB 5332 C CG . ARG B 285 ? 0.1118 0.1242 0.1332 0.0029 0.0012 -0.0009 285 ARG B CG 5333 C CD . ARG B 285 ? 0.1118 0.1277 0.1211 0.0063 -0.0019 0.0013 285 ARG B CD 5334 N NE . ARG B 285 ? 0.1247 0.1287 0.1139 0.0148 0.0055 0.0010 285 ARG B NE 5335 C CZ . ARG B 285 ? 0.1229 0.1330 0.1302 0.0114 0.0027 -0.0054 285 ARG B CZ 5336 N NH1 . ARG B 285 ? 0.1139 0.1212 0.1429 0.0146 0.0132 -0.0061 285 ARG B NH1 5337 N NH2 . ARG B 285 ? 0.1243 0.1474 0.1319 0.0125 0.0003 0.0061 285 ARG B NH2 5338 N N . PHE B 286 ? 0.1235 0.1390 0.1352 -0.0016 0.0078 -0.0034 286 PHE B N 5339 C CA . PHE B 286 ? 0.1222 0.1471 0.1427 0.0080 0.0080 -0.0038 286 PHE B CA 5340 C C . PHE B 286 ? 0.1304 0.1511 0.1397 0.0071 -0.0001 -0.0010 286 PHE B C 5341 O O . PHE B 286 ? 0.1210 0.1407 0.1683 0.0185 0.0100 -0.0024 286 PHE B O 5342 C CB . PHE B 286 ? 0.1278 0.1497 0.1489 0.0108 0.0102 -0.0069 286 PHE B CB 5343 C CG . PHE B 286 ? 0.1388 0.1615 0.1608 0.0195 0.0121 -0.0124 286 PHE B CG 5344 C CD1 . PHE B 286 ? 0.1474 0.1673 0.1535 0.0091 0.0204 -0.0094 286 PHE B CD1 5345 C CD2 . PHE B 286 ? 0.1737 0.1684 0.1569 0.0170 0.0248 -0.0099 286 PHE B CD2 5346 C CE1 . PHE B 286 ? 0.1879 0.1880 0.1686 0.0178 0.0010 -0.0107 286 PHE B CE1 5347 C CE2 . PHE B 286 ? 0.1782 0.1757 0.1860 0.0052 0.0241 0.0072 286 PHE B CE2 5348 C CZ . PHE B 286 ? 0.1793 0.1839 0.1478 0.0279 0.0158 0.0023 286 PHE B CZ 5349 N N . TYR B 287 ? 0.1262 0.1397 0.1505 0.0022 0.0014 -0.0086 287 TYR B N 5350 C CA . TYR B 287 ? 0.1311 0.1531 0.1584 0.0012 0.0019 -0.0043 287 TYR B CA 5351 C C . TYR B 287 ? 0.1365 0.1585 0.1614 0.0064 0.0122 -0.0052 287 TYR B C 5352 O O . TYR B 287 ? 0.1289 0.1650 0.1788 0.0062 0.0292 -0.0166 287 TYR B O 5353 C CB . TYR B 287 ? 0.1228 0.1385 0.1472 0.0073 0.0083 0.0016 287 TYR B CB 5354 C CG . TYR B 287 ? 0.1156 0.1498 0.1375 0.0041 -0.0003 -0.0031 287 TYR B CG 5355 C CD1 . TYR B 287 ? 0.1092 0.1400 0.1452 0.0098 -0.0185 -0.0148 287 TYR B CD1 5356 C CD2 . TYR B 287 ? 0.1394 0.1599 0.1447 0.0091 -0.0018 -0.0066 287 TYR B CD2 5357 C CE1 . TYR B 287 ? 0.1456 0.1276 0.1500 0.0101 0.0089 -0.0040 287 TYR B CE1 5358 C CE2 . TYR B 287 ? 0.1387 0.1290 0.1436 -0.0042 0.0078 -0.0104 287 TYR B CE2 5359 C CZ . TYR B 287 ? 0.1165 0.1432 0.1354 0.0053 0.0016 -0.0058 287 TYR B CZ 5360 O OH . TYR B 287 ? 0.1261 0.1460 0.1245 0.0046 0.0026 0.0047 287 TYR B OH 5361 N N . VAL B 288 ? 0.1280 0.1579 0.1598 -0.0011 0.0134 -0.0086 288 VAL B N 5362 C CA . VAL B 288 ? 0.1374 0.1670 0.1753 -0.0007 0.0100 -0.0013 288 VAL B CA 5363 C C . VAL B 288 ? 0.1506 0.1684 0.1750 0.0012 0.0088 -0.0013 288 VAL B C 5364 O O . VAL B 288 ? 0.1408 0.1633 0.1796 0.0038 0.0041 -0.0038 288 VAL B O 5365 C CB . VAL B 288 ? 0.1380 0.1838 0.1842 0.0054 0.0022 -0.0057 288 VAL B CB 5366 C CG1 . VAL B 288 ? 0.1679 0.2045 0.2050 -0.0066 0.0132 0.0090 288 VAL B CG1 5367 C CG2 . VAL B 288 ? 0.1599 0.2001 0.1809 -0.0070 0.0051 -0.0120 288 VAL B CG2 5368 N N . GLN B 289 ? 0.1599 0.1693 0.1786 0.0006 0.0065 0.0014 289 GLN B N 5369 C CA . GLN B 289 ? 0.1676 0.1870 0.1904 -0.0007 0.0063 0.0011 289 GLN B CA 5370 C C . GLN B 289 ? 0.1806 0.2080 0.2129 -0.0004 0.0047 0.0011 289 GLN B C 5371 O O . GLN B 289 ? 0.1680 0.2123 0.2198 -0.0150 0.0081 0.0019 289 GLN B O 5372 C CB . GLN B 289 ? 0.1471 0.1799 0.1750 0.0016 -0.0009 0.0045 289 GLN B CB 5373 C CG . GLN B 289 ? 0.1325 0.1772 0.1726 -0.0011 0.0147 0.0026 289 GLN B CG 5374 C CD . GLN B 289 ? 0.1483 0.1703 0.1715 0.0009 -0.0065 -0.0103 289 GLN B CD 5375 O OE1 . GLN B 289 ? 0.1462 0.2066 0.1845 0.0142 0.0156 0.0067 289 GLN B OE1 5376 N NE2 . GLN B 289 ? 0.1309 0.1812 0.1975 0.0006 -0.0092 -0.0219 289 GLN B NE2 5377 N N . ASP B 290 ? 0.1929 0.2290 0.2391 -0.0111 0.0086 -0.0036 290 ASP B N 5378 C CA . ASP B 290 ? 0.2325 0.2574 0.2618 -0.0087 0.0103 -0.0006 290 ASP B CA 5379 C C . ASP B 290 ? 0.2381 0.2705 0.2686 -0.0015 0.0084 -0.0053 290 ASP B C 5380 O O . ASP B 290 ? 0.2416 0.3069 0.2957 -0.0017 0.0224 -0.0045 290 ASP B O 5381 C CB . ASP B 290 ? 0.2461 0.2778 0.2847 -0.0126 0.0074 0.0000 290 ASP B CB 5382 C CG . ASP B 290 ? 0.3101 0.3286 0.3144 -0.0058 0.0032 -0.0067 290 ASP B CG 5383 O OD1 . ASP B 290 ? 0.4142 0.3659 0.3817 0.0000 0.0066 -0.0077 290 ASP B OD1 5384 O OD2 . ASP B 290 ? 0.3848 0.4122 0.3925 0.0000 -0.0059 0.0180 290 ASP B OD2 5385 N N . GLY B 291 ? 0.2485 0.2692 0.2564 -0.0031 0.0130 -0.0025 291 GLY B N 5386 C CA . GLY B 291 ? 0.2590 0.2654 0.2574 -0.0029 0.0121 -0.0015 291 GLY B CA 5387 C C . GLY B 291 ? 0.2641 0.2621 0.2528 -0.0004 0.0139 -0.0005 291 GLY B C 5388 O O . GLY B 291 ? 0.2902 0.2647 0.2595 -0.0052 0.0211 -0.0039 291 GLY B O 5389 N N . LYS B 292 ? 0.2369 0.2574 0.2415 -0.0059 0.0196 -0.0009 292 LYS B N 5390 C CA . LYS B 292 ? 0.2380 0.2594 0.2562 -0.0072 0.0125 0.0001 292 LYS B CA 5391 C C . LYS B 292 ? 0.2191 0.2406 0.2365 -0.0061 0.0145 0.0012 292 LYS B C 5392 O O . LYS B 292 ? 0.1877 0.2349 0.2336 0.0043 0.0160 0.0021 292 LYS B O 5393 C CB . LYS B 292 ? 0.2471 0.2704 0.2677 -0.0076 0.0140 -0.0021 292 LYS B CB 5394 C CG . LYS B 292 ? 0.2861 0.3113 0.3200 -0.0142 0.0068 -0.0005 292 LYS B CG 5395 C CD . LYS B 292 ? 0.3006 0.3272 0.3212 -0.0007 0.0007 0.0028 292 LYS B CD 5396 C CE . LYS B 292 ? 0.3674 0.3652 0.3585 0.0062 -0.0022 -0.0034 292 LYS B CE 5397 N NZ . LYS B 292 ? 0.3734 0.4043 0.3611 -0.0051 -0.0090 -0.0054 292 LYS B NZ 5398 N N . VAL B 293 ? 0.2004 0.2242 0.2266 -0.0035 0.0223 -0.0028 293 VAL B N 5399 C CA . VAL B 293 ? 0.2031 0.2269 0.2236 0.0034 0.0101 -0.0022 293 VAL B CA 5400 C C . VAL B 293 ? 0.1937 0.2205 0.2190 0.0124 0.0108 -0.0047 293 VAL B C 5401 O O . VAL B 293 ? 0.1864 0.2358 0.2339 0.0190 0.0120 0.0070 293 VAL B O 5402 C CB . VAL B 293 ? 0.2162 0.2409 0.2361 0.0049 0.0105 -0.0044 293 VAL B CB 5403 C CG1 . VAL B 293 ? 0.2327 0.2420 0.2278 -0.0039 0.0044 -0.0032 293 VAL B CG1 5404 C CG2 . VAL B 293 ? 0.2592 0.2687 0.2557 0.0004 0.0045 -0.0024 293 VAL B CG2 5405 N N . ILE B 294 ? 0.1764 0.1978 0.2020 0.0094 0.0108 0.0068 294 ILE B N 5406 C CA . ILE B 294 ? 0.1753 0.1953 0.1951 0.0053 0.0081 0.0000 294 ILE B CA 5407 C C . ILE B 294 ? 0.1669 0.1745 0.1882 0.0068 0.0096 0.0002 294 ILE B C 5408 O O . ILE B 294 ? 0.1433 0.1695 0.1828 0.0101 0.0093 0.0023 294 ILE B O 5409 C CB . ILE B 294 ? 0.1742 0.1956 0.1971 -0.0023 0.0026 -0.0021 294 ILE B CB 5410 C CG1 . ILE B 294 ? 0.1950 0.1937 0.1947 0.0008 -0.0075 -0.0025 294 ILE B CG1 5411 C CG2 . ILE B 294 ? 0.1731 0.2053 0.2076 0.0019 0.0083 0.0001 294 ILE B CG2 5412 C CD1 . ILE B 294 ? 0.2040 0.2088 0.2289 0.0002 0.0063 -0.0002 294 ILE B CD1 5413 N N . GLU B 295 ? 0.1472 0.1761 0.1921 0.0124 0.0064 -0.0034 295 GLU B N 5414 C CA . GLU B 295 ? 0.1659 0.1730 0.1802 0.0088 0.0096 -0.0009 295 GLU B CA 5415 C C . GLU B 295 ? 0.1563 0.1652 0.1714 0.0069 0.0041 -0.0022 295 GLU B C 5416 O O . GLU B 295 ? 0.1530 0.1644 0.1815 0.0145 0.0021 -0.0038 295 GLU B O 5417 C CB . GLU B 295 ? 0.1710 0.1746 0.1973 0.0075 0.0121 0.0012 295 GLU B CB 5418 C CG . GLU B 295 ? 0.2058 0.2174 0.2230 0.0094 0.0230 -0.0029 295 GLU B CG 5419 C CD . GLU B 295 ? 0.2327 0.2591 0.2478 -0.0018 0.0119 0.0128 295 GLU B CD 5420 O OE1 . GLU B 295 ? 0.2443 0.2787 0.2746 0.0095 0.0188 -0.0054 295 GLU B OE1 5421 O OE2 . GLU B 295 ? 0.2561 0.3129 0.2630 0.0042 0.0322 0.0223 295 GLU B OE2 5422 N N . SER B 296 ? 0.1481 0.1598 0.1527 0.0107 0.0000 -0.0027 296 SER B N 5423 C CA . SER B 296 ? 0.1556 0.1491 0.1594 0.0092 0.0065 -0.0004 296 SER B CA 5424 C C . SER B 296 ? 0.1587 0.1614 0.1632 0.0156 0.0046 -0.0012 296 SER B C 5425 O O . SER B 296 ? 0.1607 0.1655 0.1603 0.0229 0.0135 0.0029 296 SER B O 5426 C CB . SER B 296 ? 0.1634 0.1532 0.1565 0.0071 0.0074 -0.0056 296 SER B CB 5427 O OG . SER B 296 ? 0.1545 0.1519 0.1809 0.0166 0.0039 0.0050 296 SER B OG 5428 N N . PHE B 297 ? 0.1619 0.1506 0.1668 0.0177 0.0030 -0.0023 297 PHE B N 5429 C CA . PHE B 297 ? 0.1490 0.1494 0.1584 0.0127 -0.0002 0.0013 297 PHE B CA 5430 C C . PHE B 297 ? 0.1495 0.1446 0.1622 0.0200 -0.0038 -0.0040 297 PHE B C 5431 O O . PHE B 297 ? 0.1454 0.1386 0.1615 0.0209 -0.0046 0.0013 297 PHE B O 5432 C CB . PHE B 297 ? 0.1595 0.1476 0.1654 0.0178 -0.0025 0.0043 297 PHE B CB 5433 C CG . PHE B 297 ? 0.1361 0.1487 0.1415 -0.0022 0.0033 0.0001 297 PHE B CG 5434 C CD1 . PHE B 297 ? 0.1407 0.1318 0.1573 -0.0040 -0.0016 0.0238 297 PHE B CD1 5435 C CD2 . PHE B 297 ? 0.1535 0.1493 0.1520 -0.0053 -0.0044 0.0101 297 PHE B CD2 5436 C CE1 . PHE B 297 ? 0.1620 0.1510 0.1558 0.0044 0.0123 0.0002 297 PHE B CE1 5437 C CE2 . PHE B 297 ? 0.1648 0.1461 0.1548 0.0144 0.0116 0.0031 297 PHE B CE2 5438 C CZ . PHE B 297 ? 0.1521 0.1488 0.1474 0.0275 0.0082 0.0009 297 PHE B CZ 5439 N N . TYR B 298 ? 0.1599 0.1346 0.1665 0.0153 0.0048 0.0058 298 TYR B N 5440 C CA . TYR B 298 ? 0.1558 0.1489 0.1712 0.0165 0.0018 0.0000 298 TYR B CA 5441 C C . TYR B 298 ? 0.1610 0.1430 0.1677 0.0185 -0.0026 -0.0033 298 TYR B C 5442 O O . TYR B 298 ? 0.1622 0.1666 0.1821 0.0244 -0.0019 -0.0036 298 TYR B O 5443 C CB . TYR B 298 ? 0.1684 0.1545 0.1878 0.0176 0.0052 -0.0058 298 TYR B CB 5444 C CG . TYR B 298 ? 0.1786 0.1589 0.2018 0.0296 0.0032 -0.0129 298 TYR B CG 5445 C CD1 . TYR B 298 ? 0.1771 0.1694 0.1873 0.0338 0.0056 -0.0001 298 TYR B CD1 5446 C CD2 . TYR B 298 ? 0.1808 0.1833 0.2110 0.0295 -0.0044 0.0006 298 TYR B CD2 5447 C CE1 . TYR B 298 ? 0.1851 0.1828 0.1891 0.0279 0.0151 -0.0045 298 TYR B CE1 5448 C CE2 . TYR B 298 ? 0.1873 0.1593 0.1856 0.0333 -0.0022 -0.0172 298 TYR B CE2 5449 C CZ . TYR B 298 ? 0.1639 0.1788 0.1885 0.0381 0.0083 0.0044 298 TYR B CZ 5450 O OH . TYR B 298 ? 0.2316 0.2281 0.2130 0.0473 0.0205 -0.0115 298 TYR B OH 5451 N N . THR B 299 ? 0.1485 0.1429 0.1556 0.0268 -0.0048 -0.0046 299 THR B N 5452 C CA . THR B 299 ? 0.1572 0.1386 0.1607 0.0207 0.0009 -0.0012 299 THR B CA 5453 C C . THR B 299 ? 0.1661 0.1616 0.1649 0.0231 -0.0024 -0.0013 299 THR B C 5454 O O . THR B 299 ? 0.1803 0.1618 0.1568 0.0261 -0.0075 0.0067 299 THR B O 5455 C CB . THR B 299 ? 0.1542 0.1430 0.1515 0.0203 -0.0017 -0.0134 299 THR B CB 5456 O OG1 . THR B 299 ? 0.1858 0.1468 0.1391 0.0178 0.0061 -0.0206 299 THR B OG1 5457 C CG2 . THR B 299 ? 0.1745 0.1468 0.1513 0.0135 -0.0050 -0.0147 299 THR B CG2 5458 N N . ASN B 300 ? 0.1689 0.1528 0.1618 0.0176 -0.0080 0.0001 300 ASN B N 5459 C CA . ASN B 300 ? 0.1740 0.1650 0.1645 0.0198 -0.0046 -0.0067 300 ASN B CA 5460 C C . ASN B 300 ? 0.1718 0.1541 0.1642 0.0151 -0.0112 -0.0048 300 ASN B C 5461 O O . ASN B 300 ? 0.1932 0.1724 0.1581 0.0240 -0.0214 -0.0048 300 ASN B O 5462 C CB . ASN B 300 ? 0.1727 0.1734 0.1666 0.0168 0.0017 -0.0116 300 ASN B CB 5463 C CG . ASN B 300 ? 0.2045 0.2169 0.1801 0.0186 -0.0082 -0.0132 300 ASN B CG 5464 O OD1 . ASN B 300 ? 0.2326 0.2660 0.2391 0.0594 -0.0053 -0.0212 300 ASN B OD1 5465 N ND2 . ASN B 300 ? 0.2247 0.2983 0.1851 -0.0069 -0.0287 -0.0125 300 ASN B ND2 5466 N N . LYS B 301 ? 0.1780 0.1687 0.1688 0.0176 -0.0101 0.0037 301 LYS B N 5467 C CA . LYS B 301 ? 0.1873 0.1770 0.1844 0.0144 -0.0059 -0.0007 301 LYS B CA 5468 C C . LYS B 301 ? 0.2016 0.1873 0.1887 0.0091 -0.0050 -0.0005 301 LYS B C 5469 O O . LYS B 301 ? 0.1928 0.1714 0.1863 0.0173 -0.0051 -0.0059 301 LYS B O 5470 C CB . LYS B 301 ? 0.1751 0.1799 0.1848 0.0158 -0.0023 -0.0039 301 LYS B CB 5471 C CG . LYS B 301 ? 0.1830 0.1739 0.1901 0.0224 -0.0030 0.0038 301 LYS B CG 5472 C CD . LYS B 301 ? 0.2009 0.1790 0.1865 0.0197 -0.0021 -0.0083 301 LYS B CD 5473 C CE . LYS B 301 ? 0.2098 0.2247 0.1928 0.0145 0.0014 0.0003 301 LYS B CE 5474 N NZ . LYS B 301 ? 0.2543 0.2598 0.2004 -0.0047 0.0190 0.0194 301 LYS B NZ 5475 N N . GLU B 302 ? 0.2412 0.2100 0.2154 0.0059 -0.0085 -0.0020 302 GLU B N 5476 C CA . GLU B 302 ? 0.2378 0.2158 0.2218 0.0003 -0.0024 0.0045 302 GLU B CA 5477 C C . GLU B 302 ? 0.2435 0.2152 0.2177 -0.0013 -0.0033 0.0062 302 GLU B C 5478 O O . GLU B 302 ? 0.2589 0.2106 0.2367 -0.0056 -0.0054 0.0163 302 GLU B O 5479 C CB . GLU B 302 ? 0.2647 0.2400 0.2498 0.0009 -0.0052 0.0071 302 GLU B CB 5480 C CG . GLU B 302 ? 0.3076 0.2723 0.2907 -0.0052 -0.0054 0.0092 302 GLU B CG 5481 C CD . GLU B 302 ? 0.3843 0.3878 0.3876 0.0086 -0.0154 0.0188 302 GLU B CD 5482 O OE1 . GLU B 302 ? 0.4186 0.4688 0.4454 -0.0043 0.0202 0.0029 302 GLU B OE1 5483 O OE2 . GLU B 302 ? 0.4482 0.4455 0.4281 -0.0224 0.0156 0.0210 302 GLU B OE2 5484 N N . GLY B 303 ? 0.2363 0.2020 0.2139 0.0012 0.0021 0.0070 303 GLY B N 5485 C CA . GLY B 303 ? 0.2299 0.2074 0.2118 -0.0011 0.0001 0.0062 303 GLY B CA 5486 C C . GLY B 303 ? 0.2180 0.2019 0.2091 0.0019 -0.0020 0.0034 303 GLY B C 5487 O O . GLY B 303 ? 0.2294 0.2236 0.2473 -0.0132 -0.0044 0.0111 303 GLY B O 5488 N N . VAL B 304 ? 0.2102 0.1952 0.1923 0.0033 0.0036 0.0007 304 VAL B N 5489 C CA . VAL B 304 ? 0.2030 0.2015 0.1999 0.0013 -0.0015 0.0011 304 VAL B CA 5490 C C . VAL B 304 ? 0.2030 0.1996 0.2049 0.0034 -0.0018 0.0013 304 VAL B C 5491 O O . VAL B 304 ? 0.1927 0.1777 0.1793 0.0169 0.0025 0.0005 304 VAL B O 5492 C CB . VAL B 304 ? 0.2024 0.1913 0.1894 0.0061 -0.0030 0.0024 304 VAL B CB 5493 C CG1 . VAL B 304 ? 0.2107 0.1824 0.2122 0.0079 -0.0010 0.0127 304 VAL B CG1 5494 C CG2 . VAL B 304 ? 0.2165 0.2088 0.2177 0.0042 0.0034 -0.0043 304 VAL B CG2 5495 N N . PRO B 305 ? 0.1943 0.2260 0.1982 0.0023 0.0018 -0.0047 305 PRO B N 5496 C CA . PRO B 305 ? 0.2051 0.2194 0.2050 -0.0007 0.0023 -0.0029 305 PRO B CA 5497 C C . PRO B 305 ? 0.1824 0.2064 0.1954 0.0012 0.0066 -0.0089 305 PRO B C 5498 O O . PRO B 305 ? 0.1892 0.2129 0.2181 0.0136 0.0081 0.0160 305 PRO B O 5499 C CB . PRO B 305 ? 0.2199 0.2589 0.2225 -0.0114 -0.0028 -0.0049 305 PRO B CB 5500 C CG . PRO B 305 ? 0.2335 0.2495 0.2328 0.0012 -0.0070 0.0079 305 PRO B CG 5501 C CD . PRO B 305 ? 0.2178 0.2546 0.2141 -0.0023 0.0017 -0.0023 305 PRO B CD 5502 N N . TYR B 306 ? 0.1877 0.1836 0.1814 0.0116 0.0070 -0.0128 306 TYR B N 5503 C CA . TYR B 306 ? 0.1822 0.1654 0.1770 0.0135 0.0066 -0.0091 306 TYR B CA 5504 C C . TYR B 306 ? 0.1778 0.1571 0.1748 0.0200 -0.0023 -0.0105 306 TYR B C 5505 O O . TYR B 306 ? 0.1950 0.1640 0.1937 0.0243 -0.0014 -0.0067 306 TYR B O 5506 C CB . TYR B 306 ? 0.1788 0.1668 0.1757 0.0191 0.0072 -0.0126 306 TYR B CB 5507 C CG . TYR B 306 ? 0.1650 0.1482 0.1561 0.0312 0.0129 -0.0065 306 TYR B CG 5508 C CD1 . TYR B 306 ? 0.1802 0.1557 0.1584 0.0157 0.0097 -0.0007 306 TYR B CD1 5509 C CD2 . TYR B 306 ? 0.1715 0.1488 0.1572 0.0273 0.0061 0.0044 306 TYR B CD2 5510 C CE1 . TYR B 306 ? 0.1590 0.1671 0.1442 0.0154 -0.0114 -0.0116 306 TYR B CE1 5511 C CE2 . TYR B 306 ? 0.1778 0.1599 0.1670 0.0211 0.0101 -0.0097 306 TYR B CE2 5512 C CZ . TYR B 306 ? 0.1644 0.1419 0.1593 0.0292 0.0052 0.0018 306 TYR B CZ 5513 O OH . TYR B 306 ? 0.1781 0.1646 0.1994 0.0321 0.0112 0.0039 306 TYR B OH 5514 N N . THR B 307 ? 0.1674 0.1461 0.1683 0.0148 0.0010 -0.0086 307 THR B N 5515 C CA . THR B 307 ? 0.1634 0.1528 0.1707 0.0078 0.0011 -0.0064 307 THR B CA 5516 C C . THR B 307 ? 0.1556 0.1539 0.1680 0.0101 -0.0020 -0.0068 307 THR B C 5517 O O . THR B 307 ? 0.1581 0.1466 0.1600 0.0230 -0.0049 -0.0003 307 THR B O 5518 C CB . THR B 307 ? 0.1807 0.1558 0.1774 0.0091 -0.0010 -0.0022 307 THR B CB 5519 O OG1 . THR B 307 ? 0.1872 0.1802 0.1967 0.0126 -0.0173 0.0106 307 THR B OG1 5520 C CG2 . THR B 307 ? 0.1737 0.1549 0.1775 -0.0094 -0.0074 0.0079 307 THR B CG2 5521 N N . ASN B 308 ? 0.1430 0.1478 0.1523 0.0151 0.0100 -0.0074 308 ASN B N 5522 C CA . ASN B 308 ? 0.1516 0.1509 0.1736 0.0053 0.0058 -0.0005 308 ASN B CA 5523 C C . ASN B 308 ? 0.1564 0.1560 0.1620 0.0051 0.0040 -0.0048 308 ASN B C 5524 O O . ASN B 308 ? 0.1539 0.1571 0.1786 0.0120 0.0202 -0.0032 308 ASN B O 5525 C CB . ASN B 308 ? 0.1600 0.1530 0.1807 0.0111 0.0083 0.0087 308 ASN B CB 5526 C CG . ASN B 308 ? 0.1565 0.1379 0.1871 0.0108 -0.0060 0.0026 308 ASN B CG 5527 O OD1 . ASN B 308 ? 0.1570 0.1830 0.1822 0.0132 -0.0011 -0.0098 308 ASN B OD1 5528 N ND2 . ASN B 308 ? 0.1837 0.1543 0.1841 0.0183 0.0020 0.0273 308 ASN B ND2 5529 N N . MET B 309 ? 0.1588 0.1597 0.1688 0.0155 0.0081 0.0012 309 MET B N 5530 C CA . MET B 309 ? 0.1607 0.1604 0.1711 0.0091 0.0032 -0.0014 309 MET B CA 5531 C C . MET B 309 ? 0.1546 0.1526 0.1635 0.0099 0.0090 0.0036 309 MET B C 5532 O O . MET B 309 ? 0.1606 0.1500 0.1687 0.0091 0.0041 -0.0104 309 MET B O 5533 C CB . MET B 309 ? 0.1684 0.1685 0.1805 0.0183 -0.0072 -0.0001 309 MET B CB 5534 C CG . MET B 309 ? 0.1733 0.1908 0.1896 0.0065 -0.0031 -0.0266 309 MET B CG 5535 S SD . MET B 309 ? 0.2255 0.2173 0.2002 0.0241 0.0187 0.0009 309 MET B SD 5536 C CE . MET B 309 ? 0.2183 0.1957 0.2291 0.0105 0.0153 0.0014 309 MET B CE 5537 N N . ILE B 310 ? 0.1449 0.1275 0.1633 0.0092 0.0047 0.0004 310 ILE B N 5538 C CA . ILE B 310 ? 0.1574 0.1369 0.1450 0.0045 0.0003 -0.0003 310 ILE B CA 5539 C C . ILE B 310 ? 0.1659 0.1339 0.1484 0.0020 -0.0027 -0.0019 310 ILE B C 5540 O O . ILE B 310 ? 0.1857 0.1380 0.1516 0.0016 -0.0035 -0.0045 310 ILE B O 5541 C CB . ILE B 310 ? 0.1548 0.1338 0.1549 0.0031 0.0019 -0.0051 310 ILE B CB 5542 C CG1 . ILE B 310 ? 0.1695 0.1372 0.1403 0.0116 -0.0108 0.0066 310 ILE B CG1 5543 C CG2 . ILE B 310 ? 0.1486 0.1470 0.1681 0.0085 0.0049 -0.0124 310 ILE B CG2 5544 C CD1 . ILE B 310 ? 0.1830 0.1568 0.1561 0.0106 -0.0105 -0.0030 310 ILE B CD1 5545 N N . ASP B 311 ? 0.1607 0.1452 0.1388 -0.0039 -0.0044 0.0024 311 ASP B N 5546 C CA . ASP B 311 ? 0.1579 0.1411 0.1393 0.0031 0.0045 -0.0052 311 ASP B CA 5547 C C . ASP B 311 ? 0.1589 0.1358 0.1468 -0.0017 -0.0043 -0.0051 311 ASP B C 5548 O O . ASP B 311 ? 0.1620 0.1303 0.1341 0.0003 -0.0081 -0.0042 311 ASP B O 5549 C CB . ASP B 311 ? 0.1442 0.1504 0.1529 0.0037 0.0067 -0.0052 311 ASP B CB 5550 C CG . ASP B 311 ? 0.1756 0.1607 0.1620 0.0120 0.0156 -0.0082 311 ASP B CG 5551 O OD1 . ASP B 311 ? 0.1902 0.1303 0.1760 0.0078 0.0121 -0.0083 311 ASP B OD1 5552 O OD2 . ASP B 311 ? 0.1984 0.2008 0.2109 0.0245 0.0385 -0.0035 311 ASP B OD2 5553 N N . ASP B 312 ? 0.1561 0.1292 0.1365 -0.0008 -0.0011 -0.0139 312 ASP B N 5554 C CA . ASP B 312 ? 0.1627 0.1381 0.1511 0.0021 -0.0021 -0.0040 312 ASP B CA 5555 C C . ASP B 312 ? 0.1625 0.1438 0.1433 0.0050 0.0007 -0.0051 312 ASP B C 5556 O O . ASP B 312 ? 0.1834 0.1399 0.1545 0.0074 -0.0025 0.0004 312 ASP B O 5557 C CB . ASP B 312 ? 0.1760 0.1173 0.1393 -0.0013 -0.0050 -0.0061 312 ASP B CB 5558 C CG . ASP B 312 ? 0.1688 0.1301 0.1494 -0.0096 -0.0053 -0.0066 312 ASP B CG 5559 O OD1 . ASP B 312 ? 0.1894 0.1306 0.1563 -0.0015 -0.0204 -0.0072 312 ASP B OD1 5560 O OD2 . ASP B 312 ? 0.1872 0.1558 0.1750 -0.0045 -0.0286 0.0047 312 ASP B OD2 5561 N N . GLU B 313 ? 0.1571 0.1560 0.1601 0.0053 -0.0067 0.0003 313 GLU B N 5562 C CA . GLU B 313 ? 0.1774 0.1636 0.1692 -0.0009 -0.0047 0.0013 313 GLU B CA 5563 C C . GLU B 313 ? 0.1737 0.1570 0.1604 0.0034 -0.0045 0.0047 313 GLU B C 5564 O O . GLU B 313 ? 0.1764 0.1438 0.1747 0.0071 0.0083 -0.0004 313 GLU B O 5565 C CB . GLU B 313 ? 0.1788 0.1613 0.1601 0.0031 -0.0169 -0.0028 313 GLU B CB 5566 C CG . GLU B 313 ? 0.2130 0.1933 0.2073 0.0158 -0.0072 0.0067 313 GLU B CG 5567 C CD . GLU B 313 ? 0.2190 0.2197 0.2283 0.0149 0.0045 0.0115 313 GLU B CD 5568 O OE1 . GLU B 313 ? 0.2990 0.2733 0.3022 0.0005 -0.0025 0.0255 313 GLU B OE1 5569 O OE2 . GLU B 313 ? 0.3074 0.2306 0.3050 0.0110 -0.0071 -0.0127 313 GLU B OE2 5570 N N . PHE B 314 ? 0.1607 0.1515 0.1550 -0.0017 -0.0049 -0.0019 314 PHE B N 5571 C CA . PHE B 314 ? 0.1587 0.1558 0.1501 -0.0004 -0.0028 0.0032 314 PHE B CA 5572 C C . PHE B 314 ? 0.1603 0.1515 0.1473 0.0070 -0.0084 0.0028 314 PHE B C 5573 O O . PHE B 314 ? 0.1563 0.1413 0.1502 0.0114 -0.0088 0.0110 314 PHE B O 5574 C CB . PHE B 314 ? 0.1575 0.1451 0.1437 0.0035 -0.0025 0.0007 314 PHE B CB 5575 C CG . PHE B 314 ? 0.1519 0.1476 0.1496 -0.0031 -0.0128 -0.0061 314 PHE B CG 5576 C CD1 . PHE B 314 ? 0.1639 0.1478 0.1368 0.0083 -0.0100 0.0060 314 PHE B CD1 5577 C CD2 . PHE B 314 ? 0.1526 0.1566 0.1468 0.0054 -0.0031 -0.0015 314 PHE B CD2 5578 C CE1 . PHE B 314 ? 0.1676 0.1392 0.1499 0.0030 -0.0020 -0.0015 314 PHE B CE1 5579 C CE2 . PHE B 314 ? 0.1515 0.1520 0.1350 0.0105 -0.0025 0.0039 314 PHE B CE2 5580 C CZ . PHE B 314 ? 0.1535 0.1556 0.1516 0.0038 -0.0036 -0.0066 314 PHE B CZ 5581 N N . CYS B 315 ? 0.1528 0.1531 0.1435 0.0025 -0.0047 0.0082 315 CYS B N 5582 C CA . CYS B 315 ? 0.1596 0.1539 0.1490 0.0028 -0.0010 0.0023 315 CYS B CA 5583 C C . CYS B 315 ? 0.1650 0.1535 0.1519 0.0025 -0.0042 0.0025 315 CYS B C 5584 O O . CYS B 315 ? 0.1785 0.1469 0.1555 0.0063 -0.0055 0.0096 315 CYS B O 5585 C CB . CYS B 315 ? 0.1449 0.1578 0.1292 -0.0022 0.0029 0.0001 315 CYS B CB 5586 S SG . CYS B 315 ? 0.1615 0.1335 0.1502 0.0089 0.0004 0.0062 315 CYS B SG 5587 N N . GLU B 316 ? 0.1911 0.1647 0.1712 -0.0005 0.0000 0.0042 316 GLU B N 5588 C CA . GLU B 316 ? 0.1902 0.1706 0.1812 -0.0005 -0.0013 0.0101 316 GLU B CA 5589 C C . GLU B 316 ? 0.1966 0.1768 0.1793 -0.0026 -0.0006 0.0065 316 GLU B C 5590 O O . GLU B 316 ? 0.1986 0.1406 0.1909 -0.0043 0.0082 0.0099 316 GLU B O 5591 C CB . GLU B 316 ? 0.2074 0.1817 0.1957 -0.0128 -0.0064 0.0123 316 GLU B CB 5592 C CG . GLU B 316 ? 0.2498 0.1977 0.2324 -0.0137 -0.0078 0.0123 316 GLU B CG 5593 C CD . GLU B 316 ? 0.2912 0.2804 0.2995 -0.0020 0.0018 0.0142 316 GLU B CD 5594 O OE1 . GLU B 316 ? 0.3216 0.2664 0.3544 -0.0081 -0.0074 0.0240 316 GLU B OE1 5595 O OE2 . GLU B 316 ? 0.3777 0.3288 0.3517 -0.0192 0.0121 0.0398 316 GLU B OE2 5596 N N . ALA B 317 ? 0.1879 0.1577 0.1754 -0.0030 -0.0007 0.0096 317 ALA B N 5597 C CA . ALA B 317 ? 0.1795 0.1642 0.1713 0.0014 -0.0028 0.0082 317 ALA B CA 5598 C C . ALA B 317 ? 0.1772 0.1598 0.1733 0.0031 -0.0061 0.0054 317 ALA B C 5599 O O . ALA B 317 ? 0.2229 0.1624 0.1951 0.0123 -0.0028 0.0130 317 ALA B O 5600 C CB . ALA B 317 ? 0.1794 0.1631 0.1853 0.0088 -0.0039 0.0126 317 ALA B CB 5601 N N . THR B 318 ? 0.1809 0.1490 0.1665 0.0072 0.0000 0.0076 318 THR B N 5602 C CA . THR B 318 ? 0.1748 0.1689 0.1574 0.0020 -0.0102 0.0077 318 THR B CA 5603 C C . THR B 318 ? 0.1824 0.1665 0.1575 0.0082 -0.0044 0.0065 318 THR B C 5604 O O . THR B 318 ? 0.1949 0.1908 0.1776 0.0073 0.0086 -0.0097 318 THR B O 5605 C CB . THR B 318 ? 0.1844 0.1698 0.1571 0.0098 -0.0025 0.0012 318 THR B CB 5606 O OG1 . THR B 318 ? 0.1981 0.1852 0.1706 -0.0018 -0.0133 0.0129 318 THR B OG1 5607 C CG2 . THR B 318 ? 0.1865 0.1863 0.1419 0.0027 -0.0069 0.0025 318 THR B CG2 5608 N N . GLY B 319 ? 0.1647 0.1655 0.1668 0.0073 0.0052 0.0113 319 GLY B N 5609 C CA . GLY B 319 ? 0.1623 0.1688 0.1625 0.0090 0.0021 0.0156 319 GLY B CA 5610 C C . GLY B 319 ? 0.1558 0.1584 0.1646 0.0087 0.0061 0.0138 319 GLY B C 5611 O O . GLY B 319 ? 0.1742 0.1879 0.1821 0.0141 0.0136 0.0261 319 GLY B O 5612 N N . SER B 320 ? 0.1541 0.1613 0.1550 0.0021 0.0023 0.0134 320 SER B N 5613 C CA . SER B 320 ? 0.1523 0.1480 0.1529 0.0041 0.0017 0.0064 320 SER B CA 5614 C C . SER B 320 ? 0.1598 0.1369 0.1476 0.0059 0.0076 0.0014 320 SER B C 5615 O O . SER B 320 ? 0.1702 0.1265 0.1513 0.0033 0.0066 0.0048 320 SER B O 5616 C CB . SER B 320 ? 0.1542 0.1484 0.1587 -0.0031 0.0004 0.0110 320 SER B CB 5617 O OG . SER B 320 ? 0.1669 0.1841 0.1779 0.0038 -0.0096 0.0246 320 SER B OG 5618 N N . ARG B 321 ? 0.1698 0.1510 0.1652 0.0046 -0.0003 0.0090 321 ARG B N 5619 C CA . ARG B 321 ? 0.1700 0.1560 0.1763 0.0014 -0.0013 0.0039 321 ARG B CA 5620 C C . ARG B 321 ? 0.1641 0.1435 0.1633 -0.0092 -0.0026 0.0067 321 ARG B C 5621 O O . ARG B 321 ? 0.1638 0.1394 0.1599 -0.0040 0.0105 0.0038 321 ARG B O 5622 C CB . ARG B 321 ? 0.1755 0.1725 0.1881 0.0032 -0.0043 0.0118 321 ARG B CB 5623 C CG . ARG B 321 ? 0.2061 0.1988 0.2224 0.0012 -0.0020 0.0103 321 ARG B CG 5624 C CD . ARG B 321 ? 0.2335 0.2199 0.2447 -0.0096 0.0032 0.0159 321 ARG B CD 5625 N NE . ARG B 321 ? 0.2707 0.2647 0.2664 -0.0034 0.0138 0.0160 321 ARG B NE 5626 C CZ . ARG B 321 ? 0.2774 0.2644 0.2700 0.0018 0.0035 0.0067 321 ARG B CZ 5627 N NH1 . ARG B 321 ? 0.2814 0.2927 0.2810 -0.0026 0.0069 0.0018 321 ARG B NH1 5628 N NH2 . ARG B 321 ? 0.2636 0.2459 0.2570 -0.0022 0.0311 0.0145 321 ARG B NH2 5629 N N . LYS B 322 ? 0.1572 0.1498 0.1617 -0.0012 -0.0018 0.0053 322 LYS B N 5630 C CA . LYS B 322 ? 0.1515 0.1446 0.1506 -0.0021 -0.0066 0.0059 322 LYS B CA 5631 C C . LYS B 322 ? 0.1547 0.1363 0.1562 -0.0054 -0.0060 0.0048 322 LYS B C 5632 O O . LYS B 322 ? 0.1459 0.1433 0.1581 -0.0095 -0.0125 -0.0014 322 LYS B O 5633 C CB . LYS B 322 ? 0.1496 0.1546 0.1488 0.0057 0.0014 0.0084 322 LYS B CB 5634 C CG . LYS B 322 ? 0.1718 0.1672 0.1500 -0.0077 -0.0019 0.0209 322 LYS B CG 5635 C CD . LYS B 322 ? 0.2062 0.1725 0.1943 -0.0291 0.0300 0.0067 322 LYS B CD 5636 C CE . LYS B 322 ? 0.2317 0.2426 0.1970 -0.0527 0.0108 0.0143 322 LYS B CE 5637 N NZ . LYS B 322 ? 0.2453 0.3285 0.2321 -0.0756 -0.0046 -0.0043 322 LYS B NZ 5638 N N . TYR B 323 ? 0.1343 0.1231 0.1423 0.0016 0.0023 0.0080 323 TYR B N 5639 C CA . TYR B 323 ? 0.1397 0.1390 0.1436 0.0015 -0.0015 0.0036 323 TYR B CA 5640 C C . TYR B 323 ? 0.1331 0.1307 0.1326 -0.0013 -0.0002 0.0028 323 TYR B C 5641 O O . TYR B 323 ? 0.1357 0.1406 0.1361 -0.0119 0.0046 0.0009 323 TYR B O 5642 C CB . TYR B 323 ? 0.1360 0.1289 0.1516 0.0032 0.0036 0.0032 323 TYR B CB 5643 C CG . TYR B 323 ? 0.1292 0.1324 0.1431 -0.0039 -0.0058 0.0020 323 TYR B CG 5644 C CD1 . TYR B 323 ? 0.1348 0.1206 0.1313 -0.0005 -0.0028 -0.0017 323 TYR B CD1 5645 C CD2 . TYR B 323 ? 0.1343 0.1241 0.1390 0.0114 0.0063 0.0099 323 TYR B CD2 5646 C CE1 . TYR B 323 ? 0.1383 0.1127 0.1519 0.0002 0.0025 -0.0009 323 TYR B CE1 5647 C CE2 . TYR B 323 ? 0.1153 0.1286 0.1443 0.0013 0.0015 -0.0044 323 TYR B CE2 5648 C CZ . TYR B 323 ? 0.1557 0.1250 0.1180 -0.0065 0.0114 -0.0081 323 TYR B CZ 5649 O OH . TYR B 323 ? 0.1564 0.1400 0.1308 -0.0051 0.0130 -0.0043 323 TYR B OH 5650 N N . MET B 324 ? 0.1398 0.1356 0.1361 -0.0012 0.0036 0.0019 324 MET B N 5651 C CA . MET B 324 ? 0.1632 0.1548 0.1586 0.0030 0.0003 -0.0023 324 MET B CA 5652 C C . MET B 324 ? 0.1649 0.1525 0.1606 -0.0041 0.0014 0.0000 324 MET B C 5653 O O . MET B 324 ? 0.1897 0.2080 0.1804 -0.0172 0.0011 -0.0075 324 MET B O 5654 C CB . MET B 324 ? 0.1860 0.1510 0.1680 -0.0049 0.0009 -0.0004 324 MET B CB 5655 C CG . MET B 324 ? 0.1757 0.1225 0.1627 0.0062 0.0120 -0.0125 324 MET B CG 5656 S SD . MET B 324 ? 0.1818 0.1532 0.2141 0.0132 0.0129 -0.0215 324 MET B SD 5657 C CE . MET B 324 ? 0.2068 0.1601 0.2007 -0.0200 0.0091 -0.0160 324 MET B CE 5658 N N . GLU B 325 ? 0.1670 0.1514 0.1568 -0.0080 -0.0001 0.0044 325 GLU B N 5659 C CA . GLU B 325 ? 0.1762 0.1633 0.1828 -0.0066 -0.0053 0.0002 325 GLU B CA 5660 C C . GLU B 325 ? 0.1648 0.1660 0.1757 -0.0155 -0.0159 0.0041 325 GLU B C 5661 O O . GLU B 325 ? 0.1973 0.1782 0.2030 -0.0229 -0.0353 0.0011 325 GLU B O 5662 C CB . GLU B 325 ? 0.1770 0.1679 0.1864 -0.0155 -0.0090 0.0068 325 GLU B CB 5663 C CG . GLU B 325 ? 0.1999 0.1757 0.2145 0.0015 0.0090 0.0057 325 GLU B CG 5664 C CD . GLU B 325 ? 0.2350 0.2071 0.2166 -0.0013 0.0083 0.0121 325 GLU B CD 5665 O OE1 . GLU B 325 ? 0.3336 0.2396 0.2684 0.0051 0.0518 0.0139 325 GLU B OE1 5666 O OE2 . GLU B 325 ? 0.3483 0.2772 0.2780 0.0020 0.0051 0.0304 325 GLU B OE2 5667 N N . LEU B 326 ? 0.1617 0.1573 0.1601 -0.0070 -0.0022 0.0040 326 LEU B N 5668 C CA . LEU B 326 ? 0.1633 0.1647 0.1689 -0.0036 -0.0019 0.0007 326 LEU B CA 5669 C C . LEU B 326 ? 0.1664 0.1730 0.1760 -0.0063 -0.0016 0.0030 326 LEU B C 5670 O O . LEU B 326 ? 0.1861 0.2028 0.2093 0.0168 0.0025 0.0178 326 LEU B O 5671 C CB . LEU B 326 ? 0.1587 0.1614 0.1596 -0.0132 -0.0023 0.0007 326 LEU B CB 5672 C CG . LEU B 326 ? 0.1540 0.1440 0.1692 0.0052 -0.0008 -0.0050 326 LEU B CG 5673 C CD1 . LEU B 326 ? 0.1910 0.1839 0.1592 0.0009 0.0014 -0.0049 326 LEU B CD1 5674 C CD2 . LEU B 326 ? 0.1667 0.1727 0.1569 -0.0034 -0.0065 -0.0040 326 LEU B CD2 5675 N N . GLY B 327 ? 0.1694 0.1836 0.1704 -0.0100 -0.0036 0.0032 327 GLY B N 5676 C CA . GLY B 327 ? 0.1673 0.1650 0.1602 -0.0099 -0.0008 0.0021 327 GLY B CA 5677 C C . GLY B 327 ? 0.1627 0.1487 0.1514 -0.0079 0.0017 0.0006 327 GLY B C 5678 O O . GLY B 327 ? 0.1928 0.1504 0.1532 -0.0056 0.0123 0.0060 327 GLY B O 5679 N N . ALA B 328 ? 0.1610 0.1373 0.1443 -0.0089 -0.0006 0.0050 328 ALA B N 5680 C CA . ALA B 328 ? 0.1577 0.1443 0.1425 -0.0024 0.0038 -0.0028 328 ALA B CA 5681 C C . ALA B 328 ? 0.1502 0.1434 0.1389 0.0025 0.0024 -0.0065 328 ALA B C 5682 O O . ALA B 328 ? 0.1567 0.1456 0.1434 0.0130 -0.0020 -0.0050 328 ALA B O 5683 C CB . ALA B 328 ? 0.1562 0.1453 0.1531 0.0017 0.0020 0.0120 328 ALA B CB 5684 N N . THR B 329 ? 0.1429 0.1329 0.1346 -0.0007 0.0022 -0.0085 329 THR B N 5685 C CA . THR B 329 ? 0.1456 0.1261 0.1335 0.0007 0.0019 -0.0104 329 THR B CA 5686 C C . THR B 329 ? 0.1341 0.1280 0.1396 -0.0017 0.0028 -0.0041 329 THR B C 5687 O O . THR B 329 ? 0.1418 0.1273 0.1478 -0.0079 -0.0011 -0.0017 329 THR B O 5688 C CB . THR B 329 ? 0.1508 0.1292 0.1248 0.0049 -0.0002 -0.0094 329 THR B CB 5689 O OG1 . THR B 329 ? 0.1635 0.1323 0.1281 0.0129 -0.0036 -0.0100 329 THR B OG1 5690 C CG2 . THR B 329 ? 0.1597 0.1291 0.1526 -0.0050 0.0000 -0.0201 329 THR B CG2 5691 N N . GLN B 330 ? 0.1438 0.1335 0.1397 -0.0002 0.0074 -0.0097 330 GLN B N 5692 C CA . GLN B 330 ? 0.1481 0.1320 0.1391 -0.0021 0.0025 -0.0057 330 GLN B CA 5693 C C . GLN B 330 ? 0.1441 0.1373 0.1339 -0.0013 0.0069 -0.0065 330 GLN B C 5694 O O . GLN B 330 ? 0.1462 0.1246 0.1381 0.0049 0.0086 -0.0091 330 GLN B O 5695 C CB . GLN B 330 ? 0.1541 0.1430 0.1509 -0.0059 0.0052 -0.0096 330 GLN B CB 5696 C CG . GLN B 330 ? 0.1635 0.1540 0.1591 -0.0124 0.0036 -0.0139 330 GLN B CG 5697 C CD . GLN B 330 ? 0.1671 0.1508 0.1763 -0.0021 -0.0115 -0.0181 330 GLN B CD 5698 O OE1 . GLN B 330 ? 0.1795 0.1657 0.2063 0.0037 -0.0181 -0.0210 330 GLN B OE1 5699 N NE2 . GLN B 330 ? 0.1588 0.1475 0.1555 -0.0193 -0.0103 0.0003 330 GLN B NE2 5700 N N . GLY B 331 ? 0.1461 0.1403 0.1368 -0.0003 -0.0036 -0.0019 331 GLY B N 5701 C CA . GLY B 331 ? 0.1450 0.1447 0.1378 0.0018 -0.0040 -0.0040 331 GLY B CA 5702 C C . GLY B 331 ? 0.1436 0.1432 0.1365 0.0018 -0.0060 -0.0006 331 GLY B C 5703 O O . GLY B 331 ? 0.1608 0.1408 0.1698 0.0048 -0.0047 0.0091 331 GLY B O 5704 N N . MET B 332 ? 0.1420 0.1290 0.1369 0.0053 -0.0126 0.0008 332 MET B N 5705 C CA . MET B 332 ? 0.1422 0.1335 0.1370 0.0031 -0.0030 -0.0075 332 MET B CA 5706 C C . MET B 332 ? 0.1353 0.1263 0.1310 0.0037 -0.0060 -0.0092 332 MET B C 5707 O O . MET B 332 ? 0.1647 0.1384 0.1388 0.0000 -0.0104 -0.0139 332 MET B O 5708 C CB . MET B 332 ? 0.1505 0.1339 0.1352 0.0132 0.0025 -0.0060 332 MET B CB 5709 C CG . MET B 332 ? 0.1336 0.1426 0.1290 0.0056 0.0030 -0.0086 332 MET B CG 5710 S SD . MET B 332 ? 0.1721 0.1517 0.1358 0.0278 -0.0206 -0.0224 332 MET B SD 5711 C CE . MET B 332 ? 0.1795 0.1410 0.1536 0.0184 -0.0241 -0.0188 332 MET B CE 5712 N N . GLY B 333 ? 0.1300 0.1265 0.1381 -0.0003 -0.0088 -0.0093 333 GLY B N 5713 C CA . GLY B 333 ? 0.1331 0.1266 0.1317 0.0051 -0.0031 -0.0010 333 GLY B CA 5714 C C . GLY B 333 ? 0.1177 0.1241 0.1258 -0.0033 -0.0036 0.0000 333 GLY B C 5715 O O . GLY B 333 ? 0.1418 0.1244 0.1188 -0.0132 -0.0024 0.0005 333 GLY B O 5716 N N . GLU B 334 ? 0.1244 0.1202 0.1177 -0.0026 0.0008 -0.0045 334 GLU B N 5717 C CA . GLU B 334 ? 0.1333 0.1327 0.1224 0.0034 -0.0013 0.0005 334 GLU B CA 5718 C C . GLU B 334 ? 0.1391 0.1298 0.1190 -0.0057 -0.0017 -0.0015 334 GLU B C 5719 O O . GLU B 334 ? 0.1555 0.1306 0.1243 0.0060 -0.0059 -0.0082 334 GLU B O 5720 C CB . GLU B 334 ? 0.1291 0.1352 0.1326 0.0063 0.0033 0.0037 334 GLU B CB 5721 C CG . GLU B 334 ? 0.1567 0.1399 0.1467 -0.0069 0.0118 -0.0031 334 GLU B CG 5722 C CD . GLU B 334 ? 0.1777 0.1549 0.1808 -0.0034 0.0047 -0.0134 334 GLU B CD 5723 O OE1 . GLU B 334 ? 0.2145 0.2063 0.2560 -0.0416 0.0338 -0.0133 334 GLU B OE1 5724 O OE2 . GLU B 334 ? 0.1781 0.1639 0.1945 -0.0180 -0.0188 -0.0299 334 GLU B OE2 5725 N N . ALA B 335 ? 0.1458 0.1302 0.1169 0.0013 -0.0050 -0.0017 335 ALA B N 5726 C CA . ALA B 335 ? 0.1356 0.1298 0.1157 0.0021 -0.0009 -0.0024 335 ALA B CA 5727 C C . ALA B 335 ? 0.1352 0.1185 0.1109 0.0011 -0.0083 -0.0118 335 ALA B C 5728 O O . ALA B 335 ? 0.1388 0.1326 0.1281 0.0071 -0.0120 0.0010 335 ALA B O 5729 C CB . ALA B 335 ? 0.1515 0.1402 0.1117 0.0002 -0.0018 -0.0056 335 ALA B CB 5730 N N . LEU B 336 ? 0.1287 0.1159 0.1182 0.0051 -0.0114 -0.0030 336 LEU B N 5731 C CA . LEU B 336 ? 0.1424 0.1189 0.1172 -0.0053 -0.0022 -0.0086 336 LEU B CA 5732 C C . LEU B 336 ? 0.1551 0.1198 0.1157 -0.0033 -0.0010 0.0008 336 LEU B C 5733 O O . LEU B 336 ? 0.1773 0.1250 0.1183 -0.0176 0.0004 0.0008 336 LEU B O 5734 C CB . LEU B 336 ? 0.1541 0.1122 0.1262 -0.0001 -0.0008 -0.0095 336 LEU B CB 5735 C CG . LEU B 336 ? 0.1651 0.1757 0.1575 0.0044 -0.0093 -0.0037 336 LEU B CG 5736 C CD1 . LEU B 336 ? 0.1853 0.1897 0.1754 0.0076 -0.0173 -0.0157 336 LEU B CD1 5737 C CD2 . LEU B 336 ? 0.2234 0.2145 0.1988 0.0302 -0.0201 0.0073 336 LEU B CD2 5738 N N . THR B 337 ? 0.1449 0.1262 0.1202 -0.0002 -0.0128 0.0004 337 THR B N 5739 C CA . THR B 337 ? 0.1443 0.1364 0.1333 0.0005 -0.0033 -0.0039 337 THR B CA 5740 C C . THR B 337 ? 0.1400 0.1287 0.1232 -0.0065 -0.0080 -0.0044 337 THR B C 5741 O O . THR B 337 ? 0.1567 0.1274 0.1320 -0.0069 0.0022 -0.0019 337 THR B O 5742 C CB . THR B 337 ? 0.1328 0.1394 0.1226 0.0021 0.0017 -0.0146 337 THR B CB 5743 O OG1 . THR B 337 ? 0.1516 0.1629 0.1657 0.0073 -0.0064 -0.0133 337 THR B OG1 5744 C CG2 . THR B 337 ? 0.1548 0.1443 0.1330 0.0007 0.0030 -0.0005 337 THR B CG2 5745 N N . ARG B 338 ? 0.1411 0.1348 0.1286 -0.0014 -0.0111 -0.0072 338 ARG B N 5746 C CA . ARG B 338 ? 0.1463 0.1328 0.1334 0.0008 -0.0093 -0.0041 338 ARG B CA 5747 C C . ARG B 338 ? 0.1545 0.1357 0.1282 0.0042 -0.0174 -0.0123 338 ARG B C 5748 O O . ARG B 338 ? 0.2008 0.1364 0.1362 0.0129 -0.0292 -0.0100 338 ARG B O 5749 C CB . ARG B 338 ? 0.1343 0.1371 0.1388 -0.0082 -0.0162 -0.0050 338 ARG B CB 5750 C CG . ARG B 338 ? 0.1485 0.1301 0.1333 0.0027 -0.0155 -0.0212 338 ARG B CG 5751 C CD . ARG B 338 ? 0.1603 0.1433 0.1299 -0.0014 -0.0138 -0.0163 338 ARG B CD 5752 N NE . ARG B 338 ? 0.1700 0.1475 0.1303 0.0150 -0.0142 -0.0082 338 ARG B NE 5753 C CZ . ARG B 338 ? 0.1503 0.1282 0.1387 -0.0003 -0.0108 -0.0145 338 ARG B CZ 5754 N NH1 . ARG B 338 ? 0.1650 0.1166 0.1647 0.0052 -0.0023 -0.0119 338 ARG B NH1 5755 N NH2 . ARG B 338 ? 0.1483 0.1541 0.1633 0.0086 -0.0098 -0.0087 338 ARG B NH2 5756 N N . GLY B 339 ? 0.1536 0.1362 0.1377 -0.0023 -0.0116 -0.0083 339 GLY B N 5757 C CA . GLY B 339 ? 0.1491 0.1300 0.1225 -0.0050 -0.0051 -0.0046 339 GLY B CA 5758 C C . GLY B 339 ? 0.1344 0.1273 0.1230 -0.0084 0.0032 -0.0018 339 GLY B C 5759 O O . GLY B 339 ? 0.1477 0.1371 0.1164 -0.0130 -0.0003 -0.0183 339 GLY B O 5760 N N . MET B 340 ? 0.1252 0.1372 0.1117 -0.0071 0.0013 -0.0037 340 MET B N 5761 C CA . MET B 340 ? 0.1329 0.1259 0.1185 -0.0018 -0.0040 -0.0041 340 MET B CA 5762 C C . MET B 340 ? 0.1271 0.1216 0.1171 -0.0028 0.0011 -0.0036 340 MET B C 5763 O O . MET B 340 ? 0.1283 0.1294 0.1172 0.0010 0.0063 -0.0111 340 MET B O 5764 C CB A MET B 340 ? 0.1339 0.1252 0.1219 0.0038 -0.0020 -0.0044 340 MET B CB 5765 C CB B MET B 340 ? 0.1481 0.1358 0.1256 0.0004 -0.0009 0.0003 340 MET B CB 5766 C CG A MET B 340 ? 0.1209 0.1162 0.1076 0.0022 -0.0060 -0.0050 340 MET B CG 5767 C CG B MET B 340 ? 0.1717 0.1542 0.1339 -0.0004 -0.0033 -0.0049 340 MET B CG 5768 S SD A MET B 340 ? 0.1008 0.0994 0.0922 -0.0008 -0.0106 -0.0189 340 MET B SD 5769 S SD B MET B 340 ? 0.2240 0.1632 0.1704 0.0071 0.0059 -0.0074 340 MET B SD 5770 C CE A MET B 340 ? 0.1010 0.1192 0.0876 -0.0026 0.0012 -0.0270 340 MET B CE 5771 C CE B MET B 340 ? 0.2006 0.1914 0.1741 -0.0023 -0.0029 -0.0059 340 MET B CE 5772 N N . VAL B 341 ? 0.1164 0.1157 0.1054 -0.0096 -0.0033 -0.0019 341 VAL B N 5773 C CA . VAL B 341 ? 0.1188 0.1121 0.1149 -0.0013 0.0004 0.0009 341 VAL B CA 5774 C C . VAL B 341 ? 0.1137 0.1063 0.1109 -0.0042 0.0015 0.0002 341 VAL B C 5775 O O . VAL B 341 ? 0.1281 0.1138 0.1128 -0.0036 -0.0102 0.0072 341 VAL B O 5776 C CB . VAL B 341 ? 0.1066 0.1195 0.1166 -0.0026 0.0015 0.0042 341 VAL B CB 5777 C CG1 . VAL B 341 ? 0.1205 0.1245 0.1264 0.0015 0.0064 0.0037 341 VAL B CG1 5778 C CG2 . VAL B 341 ? 0.1541 0.1328 0.1400 -0.0041 -0.0167 -0.0033 341 VAL B CG2 5779 N N . LEU B 342 ? 0.1086 0.1135 0.0994 -0.0031 0.0052 0.0009 342 LEU B N 5780 C CA . LEU B 342 ? 0.1113 0.1049 0.1074 0.0022 0.0043 -0.0023 342 LEU B CA 5781 C C . LEU B 342 ? 0.1084 0.0953 0.1050 -0.0006 0.0015 -0.0029 342 LEU B C 5782 O O . LEU B 342 ? 0.1213 0.1193 0.1113 0.0075 -0.0047 0.0020 342 LEU B O 5783 C CB . LEU B 342 ? 0.1254 0.1208 0.1181 0.0054 0.0074 -0.0104 342 LEU B CB 5784 C CG . LEU B 342 ? 0.1161 0.1320 0.1203 -0.0047 0.0064 -0.0033 342 LEU B CG 5785 C CD1 . LEU B 342 ? 0.1138 0.1550 0.1435 -0.0064 -0.0139 0.0079 342 LEU B CD1 5786 C CD2 . LEU B 342 ? 0.1395 0.1294 0.1384 -0.0130 0.0046 0.0040 342 LEU B CD2 5787 N N . ALA B 343 ? 0.1087 0.1039 0.0985 0.0046 -0.0003 -0.0019 343 ALA B N 5788 C CA . ALA B 343 ? 0.1022 0.1007 0.0999 -0.0011 -0.0019 -0.0039 343 ALA B CA 5789 C C . ALA B 343 ? 0.1025 0.1045 0.1024 0.0064 0.0022 0.0033 343 ALA B C 5790 O O . ALA B 343 ? 0.1073 0.1107 0.1098 0.0066 -0.0102 -0.0030 343 ALA B O 5791 C CB . ALA B 343 ? 0.1218 0.1115 0.1061 0.0099 0.0056 0.0134 343 ALA B CB 5792 N N . MET B 344 ? 0.0995 0.1070 0.1038 0.0107 -0.0045 -0.0070 344 MET B N 5793 C CA . MET B 344 ? 0.1010 0.1036 0.0986 0.0023 0.0007 -0.0017 344 MET B CA 5794 C C . MET B 344 ? 0.1057 0.0989 0.1012 0.0034 -0.0034 -0.0077 344 MET B C 5795 O O . MET B 344 ? 0.1105 0.1184 0.1156 0.0081 -0.0073 -0.0079 344 MET B O 5796 C CB . MET B 344 ? 0.0974 0.0971 0.1078 -0.0013 -0.0025 -0.0103 344 MET B CB 5797 C CG . MET B 344 ? 0.1140 0.1101 0.1083 0.0068 0.0147 -0.0001 344 MET B CG 5798 S SD . MET B 344 ? 0.1365 0.1400 0.1315 -0.0123 0.0133 0.0070 344 MET B SD 5799 C CE . MET B 344 ? 0.1371 0.1247 0.1248 -0.0110 0.0113 -0.0007 344 MET B CE 5800 N N . SER B 345 ? 0.0988 0.1056 0.1102 0.0120 -0.0031 -0.0096 345 SER B N 5801 C CA . SER B 345 ? 0.1151 0.1052 0.1030 0.0024 -0.0048 -0.0077 345 SER B CA 5802 C C . SER B 345 ? 0.0897 0.0968 0.1051 -0.0002 0.0014 -0.0075 345 SER B C 5803 O O . SER B 345 ? 0.1050 0.1033 0.1092 0.0137 -0.0032 -0.0030 345 SER B O 5804 C CB . SER B 345 ? 0.1247 0.1125 0.1117 0.0095 -0.0023 -0.0151 345 SER B CB 5805 O OG . SER B 345 ? 0.1227 0.1162 0.1261 0.0049 -0.0119 -0.0102 345 SER B OG 5806 N N . ILE B 346 ? 0.1134 0.1109 0.1037 0.0074 -0.0033 -0.0076 346 ILE B N 5807 C CA . ILE B 346 ? 0.1005 0.1079 0.1026 0.0074 0.0004 -0.0067 346 ILE B CA 5808 C C . ILE B 346 ? 0.1028 0.1073 0.0970 0.0086 0.0023 -0.0034 346 ILE B C 5809 O O . ILE B 346 ? 0.1247 0.1150 0.0977 0.0190 -0.0051 -0.0026 346 ILE B O 5810 C CB . ILE B 346 ? 0.1139 0.1098 0.1018 0.0057 0.0021 -0.0068 346 ILE B CB 5811 C CG1 . ILE B 346 ? 0.0923 0.1194 0.1255 0.0123 0.0022 -0.0086 346 ILE B CG1 5812 C CG2 . ILE B 346 ? 0.1156 0.1038 0.0913 0.0026 0.0076 -0.0034 346 ILE B CG2 5813 C CD1 . ILE B 346 ? 0.1106 0.1290 0.1350 0.0019 0.0005 -0.0130 346 ILE B CD1 5814 N N . TRP B 347 ? 0.0979 0.1119 0.0986 0.0053 -0.0002 0.0001 347 TRP B N 5815 C CA . TRP B 347 ? 0.1078 0.1206 0.0983 0.0081 -0.0008 -0.0033 347 TRP B CA 5816 C C . TRP B 347 ? 0.1146 0.1212 0.0988 0.0111 0.0108 -0.0003 347 TRP B C 5817 O O . TRP B 347 ? 0.1183 0.1489 0.0954 0.0172 0.0107 0.0063 347 TRP B O 5818 C CB . TRP B 347 ? 0.1139 0.1165 0.1044 0.0050 0.0028 0.0014 347 TRP B CB 5819 C CG . TRP B 347 ? 0.1123 0.1247 0.1120 0.0012 -0.0020 0.0015 347 TRP B CG 5820 C CD1 . TRP B 347 ? 0.1192 0.1370 0.1154 0.0090 -0.0034 0.0034 347 TRP B CD1 5821 C CD2 . TRP B 347 ? 0.1194 0.1346 0.1207 -0.0002 -0.0015 -0.0016 347 TRP B CD2 5822 N NE1 . TRP B 347 ? 0.1181 0.1345 0.1163 0.0038 0.0055 0.0033 347 TRP B NE1 5823 C CE2 . TRP B 347 ? 0.0957 0.1157 0.1159 0.0037 -0.0049 0.0103 347 TRP B CE2 5824 C CE3 . TRP B 347 ? 0.1270 0.1299 0.1320 0.0086 -0.0004 0.0028 347 TRP B CE3 5825 C CZ2 . TRP B 347 ? 0.1587 0.1246 0.1322 -0.0046 0.0045 -0.0041 347 TRP B CZ2 5826 C CZ3 . TRP B 347 ? 0.1192 0.1380 0.1260 -0.0097 0.0060 0.0084 347 TRP B CZ3 5827 C CH2 . TRP B 347 ? 0.1246 0.1140 0.1518 -0.0078 0.0037 0.0041 347 TRP B CH2 5828 N N . TRP B 348 ? 0.1178 0.1184 0.0952 0.0109 0.0172 0.0151 348 TRP B N 5829 C CA . TRP B 348 ? 0.1139 0.1248 0.1071 0.0078 -0.0026 0.0071 348 TRP B CA 5830 C C . TRP B 348 ? 0.1217 0.1351 0.1207 0.0016 0.0001 0.0045 348 TRP B C 5831 O O . TRP B 348 ? 0.1246 0.1498 0.1251 0.0051 -0.0039 0.0032 348 TRP B O 5832 C CB . TRP B 348 ? 0.1199 0.1220 0.1076 0.0122 0.0043 0.0068 348 TRP B CB 5833 C CG . TRP B 348 ? 0.1271 0.1368 0.1239 0.0112 -0.0017 -0.0041 348 TRP B CG 5834 C CD1 . TRP B 348 ? 0.1450 0.1488 0.1423 0.0007 -0.0087 -0.0091 348 TRP B CD1 5835 C CD2 . TRP B 348 ? 0.1196 0.1395 0.1147 0.0191 -0.0034 0.0083 348 TRP B CD2 5836 N NE1 . TRP B 348 ? 0.1426 0.1545 0.1532 0.0037 -0.0056 -0.0085 348 TRP B NE1 5837 C CE2 . TRP B 348 ? 0.1394 0.1219 0.1241 0.0185 0.0080 -0.0122 348 TRP B CE2 5838 C CE3 . TRP B 348 ? 0.1399 0.1424 0.1265 0.0027 -0.0021 -0.0023 348 TRP B CE3 5839 C CZ2 . TRP B 348 ? 0.1344 0.1357 0.1240 0.0153 -0.0080 -0.0005 348 TRP B CZ2 5840 C CZ3 . TRP B 348 ? 0.1416 0.1340 0.1318 0.0104 -0.0127 -0.0040 348 TRP B CZ3 5841 C CH2 . TRP B 348 ? 0.1370 0.1388 0.1299 0.0041 -0.0121 -0.0029 348 TRP B CH2 5842 N N . ASP B 349 ? 0.1211 0.1430 0.1141 -0.0033 -0.0035 0.0067 349 ASP B N 5843 C CA . ASP B 349 ? 0.1356 0.1508 0.1301 -0.0056 -0.0003 0.0093 349 ASP B CA 5844 C C . ASP B 349 ? 0.1508 0.1648 0.1411 0.0045 0.0080 0.0076 349 ASP B C 5845 O O . ASP B 349 ? 0.1467 0.1688 0.1396 0.0056 0.0140 0.0181 349 ASP B O 5846 C CB . ASP B 349 ? 0.1465 0.1494 0.1375 -0.0083 0.0043 0.0131 349 ASP B CB 5847 C CG . ASP B 349 ? 0.1511 0.1591 0.1513 -0.0012 0.0065 0.0118 349 ASP B CG 5848 O OD1 . ASP B 349 ? 0.1597 0.1839 0.2229 -0.0059 0.0316 0.0026 349 ASP B OD1 5849 O OD2 . ASP B 349 ? 0.1415 0.1590 0.1656 -0.0047 0.0116 0.0082 349 ASP B OD2 5850 N N . GLN B 350 ? 0.1473 0.1833 0.1529 0.0162 0.0019 0.0067 350 GLN B N 5851 C CA . GLN B 350 ? 0.1755 0.2035 0.1773 0.0042 0.0078 0.0067 350 GLN B CA 5852 C C . GLN B 350 ? 0.1751 0.1991 0.1786 0.0052 0.0048 0.0105 350 GLN B C 5853 O O . GLN B 350 ? 0.1907 0.2281 0.1746 -0.0143 0.0116 0.0138 350 GLN B O 5854 C CB . GLN B 350 ? 0.1862 0.2158 0.2049 0.0123 0.0064 0.0046 350 GLN B CB 5855 C CG . GLN B 350 ? 0.2638 0.2872 0.2563 0.0116 0.0089 -0.0008 350 GLN B CG 5856 C CD . GLN B 350 ? 0.3158 0.3101 0.3191 0.0010 0.0023 -0.0281 350 GLN B CD 5857 O OE1 . GLN B 350 ? 0.3240 0.3451 0.3119 0.0077 0.0156 -0.0161 350 GLN B OE1 5858 N NE2 . GLN B 350 ? 0.3633 0.4018 0.3703 0.0096 0.0024 -0.0006 350 GLN B NE2 5859 N N . GLY B 351 ? 0.1830 0.2007 0.1794 -0.0016 0.0197 0.0148 351 GLY B N 5860 C CA . GLY B 351 ? 0.2082 0.2133 0.2145 -0.0003 0.0082 0.0093 351 GLY B CA 5861 C C . GLY B 351 ? 0.2349 0.2285 0.2248 0.0036 0.0082 0.0154 351 GLY B C 5862 O O . GLY B 351 ? 0.2697 0.2758 0.2636 -0.0034 0.0115 0.0311 351 GLY B O 5863 N N . GLY B 352 ? 0.1946 0.2102 0.2143 -0.0035 0.0123 0.0205 352 GLY B N 5864 C CA . GLY B 352 ? 0.1822 0.1812 0.1782 -0.0052 0.0038 0.0108 352 GLY B CA 5865 C C . GLY B 352 ? 0.1639 0.1630 0.1466 0.0008 -0.0011 0.0105 352 GLY B C 5866 O O . GLY B 352 ? 0.1618 0.1595 0.1423 0.0016 -0.0039 0.0237 352 GLY B O 5867 N N . ASN B 353 ? 0.1496 0.1516 0.1179 -0.0011 0.0034 0.0156 353 ASN B N 5868 C CA . ASN B 353 ? 0.1482 0.1464 0.1345 0.0006 0.0000 0.0030 353 ASN B CA 5869 C C . ASN B 353 ? 0.1382 0.1324 0.1301 0.0016 0.0042 -0.0010 353 ASN B C 5870 O O . ASN B 353 ? 0.1378 0.1414 0.1236 -0.0043 0.0136 -0.0061 353 ASN B O 5871 C CB . ASN B 353 ? 0.1300 0.1324 0.1310 -0.0049 -0.0020 -0.0004 353 ASN B CB 5872 C CG . ASN B 353 ? 0.1504 0.1460 0.1296 0.0114 -0.0040 0.0144 353 ASN B CG 5873 O OD1 . ASN B 353 ? 0.2111 0.2212 0.1448 0.0143 -0.0091 0.0190 353 ASN B OD1 5874 N ND2 . ASN B 353 ? 0.1266 0.1269 0.1137 -0.0002 -0.0061 0.0137 353 ASN B ND2 5875 N N . MET B 354 ? 0.1206 0.1350 0.1257 0.0038 0.0071 0.0078 354 MET B N 5876 C CA . MET B 354 ? 0.1345 0.1219 0.1294 0.0106 0.0047 -0.0007 354 MET B CA 5877 C C . MET B 354 ? 0.1231 0.1354 0.1348 0.0126 0.0004 0.0041 354 MET B C 5878 O O . MET B 354 ? 0.1329 0.1348 0.1351 0.0057 0.0000 0.0074 354 MET B O 5879 C CB . MET B 354 ? 0.1297 0.1253 0.1354 0.0113 -0.0001 -0.0072 354 MET B CB 5880 C CG . MET B 354 ? 0.1300 0.1166 0.1317 0.0203 0.0054 0.0060 354 MET B CG 5881 S SD . MET B 354 ? 0.1360 0.1309 0.1255 0.0033 0.0019 0.0030 354 MET B SD 5882 C CE . MET B 354 ? 0.1503 0.1441 0.1083 0.0131 -0.0086 0.0017 354 MET B CE 5883 N N . GLU B 355 ? 0.1307 0.1333 0.1337 0.0148 0.0081 0.0092 355 GLU B N 5884 C CA . GLU B 355 ? 0.1401 0.1317 0.1300 0.0066 0.0006 0.0080 355 GLU B CA 5885 C C . GLU B 355 ? 0.1258 0.1250 0.1155 0.0124 0.0022 0.0105 355 GLU B C 5886 O O . GLU B 355 ? 0.1190 0.1386 0.1296 0.0094 -0.0073 0.0094 355 GLU B O 5887 C CB . GLU B 355 ? 0.1463 0.1222 0.1432 0.0031 0.0027 0.0043 355 GLU B CB 5888 C CG . GLU B 355 ? 0.1537 0.1621 0.1450 -0.0045 0.0051 -0.0001 355 GLU B CG 5889 C CD . GLU B 355 ? 0.1949 0.1690 0.1487 -0.0059 0.0045 0.0062 355 GLU B CD 5890 O OE1 . GLU B 355 ? 0.2619 0.2133 0.1549 -0.0320 0.0178 0.0143 355 GLU B OE1 5891 O OE2 . GLU B 355 ? 0.2458 0.2109 0.1517 -0.0180 0.0161 0.0004 355 GLU B OE2 5892 N N . TRP B 356 ? 0.1315 0.1239 0.1337 0.0033 0.0029 0.0041 356 TRP B N 5893 C CA . TRP B 356 ? 0.1305 0.1236 0.1231 0.0029 0.0045 0.0100 356 TRP B CA 5894 C C . TRP B 356 ? 0.1316 0.1209 0.1170 0.0055 -0.0007 0.0009 356 TRP B C 5895 O O . TRP B 356 ? 0.1311 0.1203 0.1324 0.0139 0.0139 0.0017 356 TRP B O 5896 C CB . TRP B 356 ? 0.1410 0.1384 0.1378 0.0004 0.0062 0.0027 356 TRP B CB 5897 C CG . TRP B 356 ? 0.1407 0.1369 0.1302 -0.0039 0.0073 0.0123 356 TRP B CG 5898 C CD1 . TRP B 356 ? 0.1673 0.1626 0.1367 0.0027 0.0053 0.0101 356 TRP B CD1 5899 C CD2 . TRP B 356 ? 0.1446 0.1276 0.1099 -0.0046 0.0059 -0.0026 356 TRP B CD2 5900 N NE1 . TRP B 356 ? 0.1652 0.1389 0.1415 0.0118 0.0051 -0.0023 356 TRP B NE1 5901 C CE2 . TRP B 356 ? 0.1408 0.1384 0.1285 -0.0099 0.0034 0.0121 356 TRP B CE2 5902 C CE3 . TRP B 356 ? 0.1661 0.1420 0.1279 0.0120 0.0153 0.0016 356 TRP B CE3 5903 C CZ2 . TRP B 356 ? 0.1840 0.1495 0.1473 0.0141 -0.0022 0.0206 356 TRP B CZ2 5904 C CZ3 . TRP B 356 ? 0.1839 0.1586 0.1413 0.0120 0.0163 0.0118 356 TRP B CZ3 5905 C CH2 . TRP B 356 ? 0.1747 0.1454 0.1471 0.0048 0.0097 0.0113 356 TRP B CH2 5906 N N . LEU B 357 ? 0.1224 0.1373 0.1249 -0.0009 -0.0051 0.0001 357 LEU B N 5907 C CA . LEU B 357 ? 0.1343 0.1241 0.1228 0.0033 -0.0012 0.0051 357 LEU B CA 5908 C C . LEU B 357 ? 0.1315 0.1336 0.1288 0.0061 0.0036 -0.0023 357 LEU B C 5909 O O . LEU B 357 ? 0.1338 0.1413 0.1210 0.0116 0.0050 -0.0096 357 LEU B O 5910 C CB . LEU B 357 ? 0.1334 0.1294 0.1209 0.0019 -0.0044 0.0015 357 LEU B CB 5911 C CG . LEU B 357 ? 0.1270 0.1334 0.1302 0.0002 -0.0009 -0.0048 357 LEU B CG 5912 C CD1 . LEU B 357 ? 0.1665 0.1579 0.1412 0.0024 0.0092 -0.0057 357 LEU B CD1 5913 C CD2 . LEU B 357 ? 0.1457 0.1348 0.1543 0.0060 0.0040 0.0130 357 LEU B CD2 5914 N N . ASP B 358 ? 0.1183 0.1185 0.1267 0.0111 -0.0071 0.0030 358 ASP B N 5915 C CA . ASP B 358 ? 0.1339 0.1342 0.1335 0.0042 0.0003 0.0011 358 ASP B CA 5916 C C . ASP B 358 ? 0.1301 0.1370 0.1256 0.0080 -0.0029 -0.0013 358 ASP B C 5917 O O . ASP B 358 ? 0.1605 0.1476 0.1107 0.0048 -0.0053 0.0033 358 ASP B O 5918 C CB . ASP B 358 ? 0.1434 0.1453 0.1316 0.0024 0.0021 0.0041 358 ASP B CB 5919 C CG . ASP B 358 ? 0.1456 0.1443 0.1282 0.0052 -0.0061 0.0132 358 ASP B CG 5920 O OD1 . ASP B 358 ? 0.1128 0.1566 0.1416 -0.0009 0.0052 -0.0065 358 ASP B OD1 5921 O OD2 . ASP B 358 ? 0.1292 0.1456 0.1257 0.0072 0.0098 0.0027 358 ASP B OD2 5922 N N . HIS B 359 ? 0.1384 0.1455 0.1319 0.0066 -0.0139 0.0041 359 HIS B N 5923 C CA . HIS B 359 ? 0.1430 0.1552 0.1357 0.0044 -0.0040 0.0004 359 HIS B CA 5924 C C . HIS B 359 ? 0.1551 0.1563 0.1463 0.0072 -0.0056 0.0006 359 HIS B C 5925 O O . HIS B 359 ? 0.1680 0.1490 0.1482 0.0139 -0.0037 0.0096 359 HIS B O 5926 C CB . HIS B 359 ? 0.1438 0.1608 0.1475 0.0077 -0.0024 0.0022 359 HIS B CB 5927 C CG . HIS B 359 ? 0.1453 0.1662 0.1442 0.0084 -0.0099 0.0044 359 HIS B CG 5928 N ND1 . HIS B 359 ? 0.1712 0.1775 0.1096 0.0023 -0.0031 0.0112 359 HIS B ND1 5929 C CD2 . HIS B 359 ? 0.1764 0.1904 0.1448 0.0004 -0.0040 0.0108 359 HIS B CD2 5930 C CE1 . HIS B 359 ? 0.1990 0.2006 0.1561 0.0051 0.0066 0.0108 359 HIS B CE1 5931 N NE2 . HIS B 359 ? 0.2131 0.1784 0.1516 -0.0015 -0.0013 0.0176 359 HIS B NE2 5932 N N . GLY B 360 ? 0.1720 0.1614 0.1601 0.0053 -0.0018 0.0053 360 GLY B N 5933 C CA . GLY B 360 ? 0.1827 0.1726 0.1672 0.0062 -0.0045 0.0055 360 GLY B CA 5934 C C . GLY B 360 ? 0.1823 0.1708 0.1719 0.0057 0.0020 0.0113 360 GLY B C 5935 O O . GLY B 360 ? 0.1938 0.1996 0.2019 0.0245 -0.0029 0.0019 360 GLY B O 5936 N N . GLU B 361 ? 0.1858 0.1735 0.1803 0.0154 -0.0029 0.0079 361 GLU B N 5937 C CA . GLU B 361 ? 0.1853 0.1843 0.1770 0.0075 -0.0003 0.0022 361 GLU B CA 5938 C C . GLU B 361 ? 0.1881 0.1708 0.1780 0.0100 0.0028 0.0010 361 GLU B C 5939 O O . GLU B 361 ? 0.1754 0.1696 0.1765 0.0257 -0.0096 -0.0063 361 GLU B O 5940 C CB . GLU B 361 ? 0.2348 0.2031 0.2114 -0.0017 -0.0023 -0.0033 361 GLU B CB 5941 C CG . GLU B 361 ? 0.2723 0.2700 0.2609 -0.0005 0.0129 0.0081 361 GLU B CG 5942 C CD . GLU B 361 ? 0.3579 0.3215 0.3278 0.0011 -0.0116 -0.0077 361 GLU B CD 5943 O OE1 . GLU B 361 ? 0.4512 0.4064 0.3723 -0.0175 -0.0522 0.0052 361 GLU B OE1 5944 O OE2 . GLU B 361 ? 0.3109 0.4048 0.3679 0.0190 -0.0254 -0.0261 361 GLU B OE2 5945 N N . ALA B 362 ? 0.1768 0.1495 0.1594 0.0087 -0.0023 -0.0041 362 ALA B N 5946 C CA . ALA B 362 ? 0.1635 0.1578 0.1443 0.0040 0.0033 -0.0036 362 ALA B CA 5947 C C . ALA B 362 ? 0.1486 0.1512 0.1392 0.0116 0.0036 -0.0037 362 ALA B C 5948 O O . ALA B 362 ? 0.1525 0.1437 0.1360 0.0134 0.0019 -0.0118 362 ALA B O 5949 C CB . ALA B 362 ? 0.1541 0.1469 0.1493 0.0009 0.0052 0.0039 362 ALA B CB 5950 N N . GLY B 363 ? 0.1455 0.1419 0.1376 0.0056 0.0025 -0.0067 363 GLY B N 5951 C CA . GLY B 363 ? 0.1474 0.1549 0.1455 0.0076 -0.0046 -0.0010 363 GLY B CA 5952 C C . GLY B 363 ? 0.1499 0.1562 0.1370 0.0042 0.0009 0.0066 363 GLY B C 5953 O O . GLY B 363 ? 0.1601 0.1793 0.1432 0.0135 -0.0060 0.0138 363 GLY B O 5954 N N . PRO B 364 ? 0.1457 0.1501 0.1392 0.0073 -0.0048 0.0005 364 PRO B N 5955 C CA . PRO B 364 ? 0.1519 0.1655 0.1417 0.0083 -0.0063 0.0032 364 PRO B CA 5956 C C . PRO B 364 ? 0.1602 0.1729 0.1449 0.0085 -0.0090 -0.0066 364 PRO B C 5957 O O . PRO B 364 ? 0.1879 0.1900 0.1458 0.0055 -0.0138 -0.0061 364 PRO B O 5958 C CB . PRO B 364 ? 0.1626 0.1771 0.1516 0.0014 -0.0039 0.0039 364 PRO B CB 5959 C CG . PRO B 364 ? 0.1465 0.1666 0.1517 0.0084 0.0033 -0.0014 364 PRO B CG 5960 C CD . PRO B 364 ? 0.1605 0.1667 0.1456 0.0068 -0.0001 -0.0021 364 PRO B CD 5961 N N . CYS B 365 ? 0.1629 0.1513 0.1355 0.0082 -0.0147 -0.0021 365 CYS B N 5962 C CA . CYS B 365 ? 0.1535 0.1567 0.1414 0.0078 -0.0038 0.0035 365 CYS B CA 5963 C C . CYS B 365 ? 0.1663 0.1494 0.1510 0.0040 0.0043 -0.0007 365 CYS B C 5964 O O . CYS B 365 ? 0.1814 0.1565 0.1548 0.0062 0.0044 0.0067 365 CYS B O 5965 C CB . CYS B 365 ? 0.1518 0.1452 0.1279 0.0187 -0.0007 0.0025 365 CYS B CB 5966 S SG . CYS B 365 ? 0.1573 0.1487 0.1374 0.0123 -0.0075 0.0004 365 CYS B SG 5967 N N . ALA B 366 ? 0.1738 0.1550 0.1450 0.0114 -0.0019 0.0136 366 ALA B N 5968 C CA . ALA B 366 ? 0.1673 0.1622 0.1409 0.0085 0.0033 0.0076 366 ALA B CA 5969 C C . ALA B 366 ? 0.1757 0.1747 0.1490 0.0107 0.0058 0.0087 366 ALA B C 5970 O O . ALA B 366 ? 0.1557 0.1757 0.1356 0.0201 -0.0019 0.0078 366 ALA B O 5971 C CB . ALA B 366 ? 0.1651 0.1705 0.1421 0.0132 -0.0009 0.0120 366 ALA B CB 5972 N N . LYS B 367 ? 0.1849 0.1700 0.1607 0.0102 0.0019 0.0197 367 LYS B N 5973 C CA . LYS B 367 ? 0.1828 0.1710 0.1554 0.0056 0.0013 0.0151 367 LYS B CA 5974 C C . LYS B 367 ? 0.1784 0.1702 0.1455 0.0058 -0.0025 0.0108 367 LYS B C 5975 O O . LYS B 367 ? 0.2023 0.1736 0.1627 0.0189 0.0032 0.0014 367 LYS B O 5976 C CB . LYS B 367 ? 0.2149 0.1933 0.1755 0.0025 0.0062 0.0214 367 LYS B CB 5977 C CG . LYS B 367 ? 0.2178 0.1996 0.2063 0.0012 0.0072 0.0171 367 LYS B CG 5978 C CD . LYS B 367 ? 0.2543 0.2728 0.2594 -0.0092 -0.0059 0.0188 367 LYS B CD 5979 C CE . LYS B 367 ? 0.2768 0.3009 0.2854 -0.0063 0.0050 0.0117 367 LYS B CE 5980 N NZ . LYS B 367 ? 0.3201 0.3242 0.2919 -0.0313 -0.0051 0.0268 367 LYS B NZ 5981 N N . GLY B 368 ? 0.1727 0.1656 0.1329 0.0152 0.0042 0.0063 368 GLY B N 5982 C CA . GLY B 368 ? 0.1640 0.1647 0.1441 0.0056 -0.0072 0.0076 368 GLY B CA 5983 C C . GLY B 368 ? 0.1661 0.1597 0.1424 0.0129 -0.0046 0.0055 368 GLY B C 5984 O O . GLY B 368 ? 0.1945 0.1544 0.1436 0.0248 -0.0014 0.0059 368 GLY B O 5985 N N . GLU B 369 ? 0.1578 0.1587 0.1594 0.0102 -0.0039 0.0069 369 GLU B N 5986 C CA . GLU B 369 ? 0.1635 0.1540 0.1445 0.0019 -0.0037 0.0052 369 GLU B CA 5987 C C . GLU B 369 ? 0.1591 0.1471 0.1384 0.0035 0.0001 0.0059 369 GLU B C 5988 O O . GLU B 369 ? 0.1692 0.1524 0.1327 -0.0046 0.0055 0.0094 369 GLU B O 5989 C CB . GLU B 369 ? 0.1675 0.1600 0.1480 0.0003 -0.0032 0.0072 369 GLU B CB 5990 C CG . GLU B 369 ? 0.1706 0.1733 0.1564 0.0073 -0.0002 -0.0021 369 GLU B CG 5991 C CD . GLU B 369 ? 0.1691 0.1739 0.1678 0.0042 0.0059 0.0072 369 GLU B CD 5992 O OE1 . GLU B 369 ? 0.1851 0.1715 0.1813 -0.0082 -0.0052 0.0105 369 GLU B OE1 5993 O OE2 . GLU B 369 ? 0.1965 0.2056 0.2713 0.0002 0.0111 0.0104 369 GLU B OE2 5994 N N . GLY B 370 ? 0.1555 0.1442 0.1390 0.0043 0.0006 0.0048 370 GLY B N 5995 C CA . GLY B 370 ? 0.1625 0.1458 0.1383 0.0051 -0.0032 0.0051 370 GLY B CA 5996 C C . GLY B 370 ? 0.1587 0.1553 0.1395 -0.0006 0.0013 0.0049 370 GLY B C 5997 O O . GLY B 370 ? 0.1482 0.1441 0.1512 -0.0088 -0.0102 0.0071 370 GLY B O 5998 N N . ALA B 371 ? 0.1580 0.1544 0.1350 0.0023 0.0063 0.0084 371 ALA B N 5999 C CA . ALA B 371 ? 0.1531 0.1469 0.1387 0.0030 -0.0020 0.0012 371 ALA B CA 6000 C C . ALA B 371 ? 0.1570 0.1533 0.1423 -0.0044 0.0015 0.0017 371 ALA B C 6001 O O . ALA B 371 ? 0.1531 0.1511 0.1394 -0.0032 -0.0066 -0.0003 371 ALA B O 6002 C CB . ALA B 371 ? 0.1621 0.1691 0.1545 -0.0018 -0.0037 0.0063 371 ALA B CB 6003 N N . PRO B 372 ? 0.1302 0.1391 0.1251 -0.0089 0.0012 0.0032 372 PRO B N 6004 C CA . PRO B 372 ? 0.1342 0.1420 0.1322 0.0000 0.0005 0.0005 372 PRO B CA 6005 C C . PRO B 372 ? 0.1333 0.1438 0.1366 0.0007 0.0023 0.0038 372 PRO B C 6006 O O . PRO B 372 ? 0.1275 0.1417 0.1206 -0.0024 -0.0106 -0.0023 372 PRO B O 6007 C CB . PRO B 372 ? 0.1330 0.1354 0.1254 0.0095 0.0046 -0.0027 372 PRO B CB 6008 C CG . PRO B 372 ? 0.1162 0.1359 0.1377 0.0000 0.0022 0.0008 372 PRO B CG 6009 C CD . PRO B 372 ? 0.1477 0.1505 0.1295 -0.0037 -0.0097 0.0029 372 PRO B CD 6010 N N . SER B 373 ? 0.1454 0.1632 0.1372 -0.0050 -0.0054 -0.0046 373 SER B N 6011 C CA . SER B 373 ? 0.1470 0.1670 0.1419 -0.0008 -0.0018 -0.0023 373 SER B CA 6012 C C . SER B 373 ? 0.1545 0.1705 0.1474 0.0022 -0.0026 0.0019 373 SER B C 6013 O O . SER B 373 ? 0.1676 0.1953 0.1544 0.0110 -0.0131 -0.0074 373 SER B O 6014 C CB . SER B 373 ? 0.1505 0.1862 0.1421 -0.0056 -0.0011 -0.0043 373 SER B CB 6015 O OG . SER B 373 ? 0.1941 0.2129 0.1721 -0.0159 0.0096 0.0072 373 SER B OG 6016 N N . ASN B 374 ? 0.1511 0.1624 0.1335 -0.0009 -0.0005 0.0005 374 ASN B N 6017 C CA . ASN B 374 ? 0.1427 0.1517 0.1352 0.0002 -0.0039 0.0023 374 ASN B CA 6018 C C . ASN B 374 ? 0.1344 0.1463 0.1343 -0.0055 -0.0010 -0.0046 374 ASN B C 6019 O O . ASN B 374 ? 0.1243 0.1647 0.1374 0.0043 0.0038 0.0014 374 ASN B O 6020 C CB . ASN B 374 ? 0.1363 0.1598 0.1267 0.0031 -0.0007 -0.0013 374 ASN B CB 6021 C CG . ASN B 374 ? 0.1554 0.1591 0.1602 0.0076 -0.0096 0.0038 374 ASN B CG 6022 O OD1 . ASN B 374 ? 0.1871 0.1611 0.1716 0.0114 -0.0221 -0.0081 374 ASN B OD1 6023 N ND2 . ASN B 374 ? 0.1695 0.1377 0.1485 0.0208 -0.0176 0.0231 374 ASN B ND2 6024 N N . ILE B 375 ? 0.1171 0.1444 0.1212 0.0000 0.0029 0.0020 375 ILE B N 6025 C CA . ILE B 375 ? 0.1310 0.1331 0.1257 0.0004 -0.0013 0.0040 375 ILE B CA 6026 C C . ILE B 375 ? 0.1369 0.1445 0.1266 -0.0023 -0.0040 0.0006 375 ILE B C 6027 O O . ILE B 375 ? 0.1373 0.1598 0.1357 -0.0074 0.0001 -0.0019 375 ILE B O 6028 C CB . ILE B 375 ? 0.1179 0.1262 0.1336 0.0034 -0.0014 0.0053 375 ILE B CB 6029 C CG1 . ILE B 375 ? 0.1229 0.1203 0.1321 0.0081 -0.0042 0.0027 375 ILE B CG1 6030 C CG2 . ILE B 375 ? 0.1383 0.1421 0.1390 0.0036 0.0010 0.0020 375 ILE B CG2 6031 C CD1 . ILE B 375 ? 0.1448 0.1247 0.1128 -0.0093 -0.0029 0.0054 375 ILE B CD1 6032 N N . VAL B 376 ? 0.1458 0.1455 0.1314 -0.0017 -0.0106 -0.0008 376 VAL B N 6033 C CA . VAL B 376 ? 0.1540 0.1449 0.1407 0.0014 -0.0094 -0.0022 376 VAL B CA 6034 C C . VAL B 376 ? 0.1636 0.1495 0.1372 0.0019 -0.0079 -0.0059 376 VAL B C 6035 O O . VAL B 376 ? 0.1713 0.1586 0.1433 -0.0065 -0.0200 0.0047 376 VAL B O 6036 C CB . VAL B 376 ? 0.1536 0.1405 0.1520 0.0053 -0.0159 -0.0076 376 VAL B CB 6037 C CG1 . VAL B 376 ? 0.1742 0.1603 0.1691 0.0129 -0.0313 0.0036 376 VAL B CG1 6038 C CG2 . VAL B 376 ? 0.1713 0.1416 0.1537 0.0199 -0.0026 -0.0074 376 VAL B CG2 6039 N N . GLN B 377 ? 0.1573 0.1393 0.1413 0.0040 -0.0053 -0.0070 377 GLN B N 6040 C CA . GLN B 377 ? 0.1507 0.1577 0.1456 0.0040 -0.0040 -0.0014 377 GLN B CA 6041 C C . GLN B 377 ? 0.1455 0.1678 0.1466 -0.0023 -0.0073 -0.0045 377 GLN B C 6042 O O . GLN B 377 ? 0.1469 0.2002 0.1854 -0.0151 0.0048 -0.0282 377 GLN B O 6043 C CB . GLN B 377 ? 0.1418 0.1707 0.1450 0.0130 -0.0111 0.0028 377 GLN B CB 6044 C CG . GLN B 377 ? 0.1411 0.1662 0.1500 0.0140 0.0070 -0.0033 377 GLN B CG 6045 C CD . GLN B 377 ? 0.1812 0.2121 0.1764 0.0079 0.0090 0.0158 377 GLN B CD 6046 O OE1 . GLN B 377 ? 0.2030 0.3634 0.2046 0.0085 -0.0069 0.0584 377 GLN B OE1 6047 N NE2 . GLN B 377 ? 0.2034 0.2636 0.2112 0.0003 0.0093 0.0049 377 GLN B NE2 6048 N N . VAL B 378 ? 0.1415 0.1604 0.1388 0.0003 -0.0078 0.0009 378 VAL B N 6049 C CA . VAL B 378 ? 0.1441 0.1671 0.1418 0.0029 -0.0064 0.0026 378 VAL B CA 6050 C C . VAL B 378 ? 0.1387 0.1525 0.1425 0.0025 -0.0079 0.0014 378 VAL B C 6051 O O . VAL B 378 ? 0.1540 0.1871 0.1570 0.0130 -0.0128 0.0086 378 VAL B O 6052 C CB . VAL B 378 ? 0.1634 0.1739 0.1463 -0.0003 -0.0011 0.0065 378 VAL B CB 6053 C CG1 . VAL B 378 ? 0.1453 0.1937 0.1530 0.0066 -0.0051 -0.0013 378 VAL B CG1 6054 C CG2 . VAL B 378 ? 0.1579 0.1692 0.1611 -0.0018 -0.0035 0.0110 378 VAL B CG2 6055 N N . GLU B 379 ? 0.1468 0.1623 0.1442 0.0008 -0.0124 -0.0046 379 GLU B N 6056 C CA . GLU B 379 ? 0.1442 0.1559 0.1407 0.0019 -0.0017 -0.0076 379 GLU B CA 6057 C C . GLU B 379 ? 0.1425 0.1498 0.1266 0.0034 0.0013 -0.0028 379 GLU B C 6058 O O . GLU B 379 ? 0.1338 0.1370 0.1233 0.0016 -0.0076 -0.0136 379 GLU B O 6059 C CB . GLU B 379 ? 0.1456 0.1551 0.1431 0.0071 -0.0122 -0.0080 379 GLU B CB 6060 C CG . GLU B 379 ? 0.1603 0.1599 0.1444 0.0015 -0.0038 -0.0056 379 GLU B CG 6061 C CD . GLU B 379 ? 0.1758 0.1964 0.1756 -0.0025 -0.0060 0.0025 379 GLU B CD 6062 O OE1 . GLU B 379 ? 0.1861 0.1965 0.2323 0.0201 0.0167 0.0025 379 GLU B OE1 6063 O OE2 . GLU B 379 ? 0.1832 0.2146 0.1496 0.0148 -0.0200 0.0074 379 GLU B OE2 6064 N N . PRO B 380 ? 0.1319 0.1541 0.1409 -0.0039 -0.0099 -0.0086 380 PRO B N 6065 C CA . PRO B 380 ? 0.1526 0.1574 0.1424 -0.0004 -0.0040 -0.0143 380 PRO B CA 6066 C C . PRO B 380 ? 0.1513 0.1455 0.1449 0.0029 -0.0072 -0.0120 380 PRO B C 6067 O O . PRO B 380 ? 0.1679 0.1741 0.1473 0.0180 -0.0077 -0.0225 380 PRO B O 6068 C CB . PRO B 380 ? 0.1673 0.1700 0.1441 0.0066 -0.0061 -0.0153 380 PRO B CB 6069 C CG . PRO B 380 ? 0.1871 0.1919 0.2018 -0.0089 -0.0114 -0.0391 380 PRO B CG 6070 C CD . PRO B 380 ? 0.1583 0.1615 0.1610 -0.0056 -0.0086 -0.0111 380 PRO B CD 6071 N N . PHE B 381 ? 0.1431 0.1371 0.1400 0.0107 -0.0046 -0.0105 381 PHE B N 6072 C CA . PHE B 381 ? 0.1595 0.1417 0.1346 0.0030 -0.0047 -0.0067 381 PHE B CA 6073 C C . PHE B 381 ? 0.1541 0.1428 0.1319 0.0022 0.0022 -0.0070 381 PHE B C 6074 O O . PHE B 381 ? 0.1799 0.1454 0.1314 -0.0075 -0.0012 -0.0070 381 PHE B O 6075 C CB . PHE B 381 ? 0.1889 0.1704 0.1635 0.0021 -0.0069 -0.0072 381 PHE B CB 6076 C CG . PHE B 381 ? 0.2061 0.1837 0.1853 0.0010 -0.0029 -0.0148 381 PHE B CG 6077 C CD1 . PHE B 381 ? 0.2292 0.1978 0.2334 0.0092 -0.0044 -0.0216 381 PHE B CD1 6078 C CD2 . PHE B 381 ? 0.2288 0.1861 0.2110 0.0106 -0.0143 -0.0202 381 PHE B CD2 6079 C CE1 . PHE B 381 ? 0.2093 0.2110 0.2409 0.0092 -0.0048 -0.0323 381 PHE B CE1 6080 C CE2 . PHE B 381 ? 0.2342 0.2099 0.2231 0.0021 0.0003 -0.0349 381 PHE B CE2 6081 C CZ . PHE B 381 ? 0.2495 0.2211 0.2361 0.0172 -0.0083 -0.0403 381 PHE B CZ 6082 N N . PRO B 382 ? 0.1326 0.1347 0.1257 0.0018 0.0020 -0.0079 382 PRO B N 6083 C CA . PRO B 382 ? 0.1333 0.1254 0.1210 0.0055 0.0007 -0.0044 382 PRO B CA 6084 C C . PRO B 382 ? 0.1143 0.1277 0.1220 0.0030 0.0019 -0.0036 382 PRO B C 6085 O O . PRO B 382 ? 0.1293 0.1366 0.1110 0.0096 -0.0029 -0.0074 382 PRO B O 6086 C CB . PRO B 382 ? 0.1359 0.1281 0.1408 0.0097 -0.0028 -0.0051 382 PRO B CB 6087 C CG . PRO B 382 ? 0.1364 0.1322 0.1338 0.0020 -0.0012 0.0048 382 PRO B CG 6088 C CD . PRO B 382 ? 0.1350 0.1404 0.1197 0.0097 -0.0014 -0.0076 382 PRO B CD 6089 N N . GLU B 383 ? 0.1320 0.1207 0.1106 0.0036 -0.0008 -0.0124 383 GLU B N 6090 C CA . GLU B 383 ? 0.1253 0.1293 0.1237 0.0016 0.0000 0.0009 383 GLU B CA 6091 C C . GLU B 383 ? 0.1352 0.1236 0.1154 0.0078 -0.0074 -0.0039 383 GLU B C 6092 O O . GLU B 383 ? 0.1376 0.1294 0.1082 -0.0040 -0.0130 -0.0002 383 GLU B O 6093 C CB . GLU B 383 ? 0.1286 0.1370 0.1300 0.0065 -0.0022 0.0001 383 GLU B CB 6094 C CG . GLU B 383 ? 0.1421 0.1524 0.1394 -0.0040 -0.0102 -0.0060 383 GLU B CG 6095 C CD . GLU B 383 ? 0.1670 0.1592 0.1470 -0.0125 -0.0072 0.0000 383 GLU B CD 6096 O OE1 . GLU B 383 ? 0.1888 0.1467 0.1491 -0.0153 -0.0094 -0.0032 383 GLU B OE1 6097 O OE2 . GLU B 383 ? 0.2100 0.1619 0.1550 -0.0210 -0.0268 0.0007 383 GLU B OE2 6098 N N . VAL B 384 ? 0.1182 0.1259 0.1073 0.0091 -0.0043 -0.0027 384 VAL B N 6099 C CA . VAL B 384 ? 0.1126 0.1163 0.1142 0.0079 0.0003 -0.0004 384 VAL B CA 6100 C C . VAL B 384 ? 0.1269 0.1206 0.1233 0.0021 0.0031 -0.0018 384 VAL B C 6101 O O . VAL B 384 ? 0.1216 0.1316 0.1145 0.0057 0.0109 -0.0046 384 VAL B O 6102 C CB . VAL B 384 ? 0.1087 0.1195 0.1213 0.0027 0.0050 0.0027 384 VAL B CB 6103 C CG1 . VAL B 384 ? 0.1327 0.1199 0.1140 0.0113 0.0001 -0.0041 384 VAL B CG1 6104 C CG2 . VAL B 384 ? 0.1156 0.1224 0.1317 -0.0003 -0.0078 -0.0108 384 VAL B CG2 6105 N N . THR B 385 ? 0.1109 0.1292 0.1237 0.0012 0.0007 -0.0010 385 THR B N 6106 C CA . THR B 385 ? 0.1172 0.1249 0.1236 -0.0038 0.0076 0.0011 385 THR B CA 6107 C C . THR B 385 ? 0.1118 0.1200 0.1126 -0.0066 0.0059 0.0035 385 THR B C 6108 O O . THR B 385 ? 0.1235 0.1438 0.1230 -0.0072 0.0017 -0.0038 385 THR B O 6109 C CB . THR B 385 ? 0.1258 0.1286 0.1346 -0.0011 0.0032 0.0007 385 THR B CB 6110 O OG1 . THR B 385 ? 0.1613 0.1546 0.1522 -0.0064 0.0107 -0.0126 385 THR B OG1 6111 C CG2 . THR B 385 ? 0.1362 0.1444 0.1286 -0.0090 0.0013 -0.0023 385 THR B CG2 6112 N N . TYR B 386 ? 0.1193 0.1297 0.1107 -0.0055 -0.0010 0.0061 386 TYR B N 6113 C CA . TYR B 386 ? 0.1226 0.1174 0.1150 0.0019 0.0056 0.0091 386 TYR B CA 6114 C C . TYR B 386 ? 0.1185 0.1222 0.1165 0.0028 0.0042 0.0128 386 TYR B C 6115 O O . TYR B 386 ? 0.1550 0.1333 0.1339 0.0112 0.0159 0.0179 386 TYR B O 6116 C CB . TYR B 386 ? 0.1274 0.1137 0.1174 -0.0006 0.0019 0.0070 386 TYR B CB 6117 C CG . TYR B 386 ? 0.1236 0.1049 0.1050 0.0024 0.0111 -0.0032 386 TYR B CG 6118 C CD1 . TYR B 386 ? 0.1374 0.1115 0.1192 0.0115 0.0149 -0.0083 386 TYR B CD1 6119 C CD2 . TYR B 386 ? 0.1108 0.1093 0.1234 0.0036 0.0027 0.0098 386 TYR B CD2 6120 C CE1 . TYR B 386 ? 0.1157 0.1121 0.1284 0.0050 0.0117 0.0005 386 TYR B CE1 6121 C CE2 . TYR B 386 ? 0.1175 0.1127 0.1307 -0.0118 -0.0045 0.0031 386 TYR B CE2 6122 C CZ . TYR B 386 ? 0.0963 0.1079 0.1123 -0.0052 0.0058 0.0100 386 TYR B CZ 6123 O OH . TYR B 386 ? 0.1228 0.1237 0.1024 -0.0070 0.0060 0.0115 386 TYR B OH 6124 N N . THR B 387 ? 0.1351 0.1281 0.1181 0.0013 0.0129 0.0054 387 THR B N 6125 C CA . THR B 387 ? 0.1399 0.1274 0.1171 -0.0048 0.0035 0.0088 387 THR B CA 6126 C C . THR B 387 ? 0.1300 0.1181 0.1277 -0.0055 0.0017 0.0026 387 THR B C 6127 O O . THR B 387 ? 0.1361 0.1372 0.1353 -0.0020 0.0156 0.0004 387 THR B O 6128 C CB . THR B 387 ? 0.1409 0.1253 0.1268 -0.0025 0.0092 0.0022 387 THR B CB 6129 O OG1 . THR B 387 ? 0.1517 0.1617 0.1265 -0.0071 0.0055 -0.0096 387 THR B OG1 6130 C CG2 . THR B 387 ? 0.1486 0.1605 0.1513 -0.0157 0.0023 -0.0020 387 THR B CG2 6131 N N . ASN B 388 ? 0.1245 0.1149 0.1239 -0.0091 0.0079 0.0111 388 ASN B N 6132 C CA . ASN B 388 ? 0.1288 0.1218 0.1217 -0.0064 0.0067 0.0051 388 ASN B CA 6133 C C . ASN B 388 ? 0.1456 0.1304 0.1341 -0.0017 0.0037 -0.0023 388 ASN B C 6134 O O . ASN B 388 ? 0.1351 0.1444 0.1393 -0.0024 0.0226 0.0021 388 ASN B O 6135 C CB . ASN B 388 ? 0.1378 0.1332 0.1265 -0.0135 0.0084 0.0092 388 ASN B CB 6136 C CG . ASN B 388 ? 0.1248 0.1451 0.1450 -0.0070 0.0064 -0.0079 388 ASN B CG 6137 O OD1 . ASN B 388 ? 0.1568 0.1620 0.1426 -0.0041 0.0085 0.0080 388 ASN B OD1 6138 N ND2 . ASN B 388 ? 0.1690 0.1916 0.1839 -0.0037 -0.0243 -0.0026 388 ASN B ND2 6139 N N . LEU B 389 ? 0.1363 0.1312 0.1306 -0.0093 0.0035 0.0034 389 LEU B N 6140 C CA . LEU B 389 ? 0.1450 0.1370 0.1298 -0.0131 0.0074 0.0029 389 LEU B CA 6141 C C . LEU B 389 ? 0.1561 0.1339 0.1304 -0.0096 0.0044 -0.0014 389 LEU B C 6142 O O . LEU B 389 ? 0.1387 0.1323 0.1339 -0.0200 0.0153 -0.0015 389 LEU B O 6143 C CB . LEU B 389 ? 0.1512 0.1477 0.1320 -0.0004 0.0116 -0.0086 389 LEU B CB 6144 C CG . LEU B 389 ? 0.2035 0.2504 0.1843 0.0046 0.0195 -0.0022 389 LEU B CG 6145 C CD1 . LEU B 389 ? 0.2047 0.2729 0.2145 0.0226 0.0115 0.0071 389 LEU B CD1 6146 C CD2 . LEU B 389 ? 0.1591 0.2100 0.1578 -0.0063 0.0094 -0.0023 389 LEU B CD2 6147 N N . ARG B 390 ? 0.1558 0.1400 0.1222 -0.0097 0.0196 -0.0018 390 ARG B N 6148 C CA . ARG B 390 ? 0.1577 0.1406 0.1316 -0.0019 0.0077 -0.0068 390 ARG B CA 6149 C C . ARG B 390 ? 0.1584 0.1295 0.1300 -0.0031 0.0017 -0.0030 390 ARG B C 6150 O O . ARG B 390 ? 0.1994 0.1396 0.1333 -0.0047 -0.0081 -0.0027 390 ARG B O 6151 C CB . ARG B 390 ? 0.1637 0.1444 0.1476 -0.0050 0.0069 -0.0024 390 ARG B CB 6152 C CG . ARG B 390 ? 0.1499 0.1636 0.1429 -0.0080 0.0166 0.0019 390 ARG B CG 6153 C CD . ARG B 390 ? 0.1620 0.1549 0.1674 0.0009 0.0071 -0.0107 390 ARG B CD 6154 N NE . ARG B 390 ? 0.1588 0.1758 0.1654 -0.0106 0.0118 -0.0048 390 ARG B NE 6155 C CZ . ARG B 390 ? 0.1702 0.1747 0.1670 -0.0126 -0.0003 0.0085 390 ARG B CZ 6156 N NH1 . ARG B 390 ? 0.1557 0.1869 0.1711 0.0030 0.0130 0.0046 390 ARG B NH1 6157 N NH2 . ARG B 390 ? 0.1748 0.1980 0.2054 -0.0064 0.0108 0.0103 390 ARG B NH2 6158 N N . TRP B 391 ? 0.1436 0.1209 0.1242 -0.0111 0.0022 -0.0068 391 TRP B N 6159 C CA . TRP B 391 ? 0.1346 0.1273 0.1288 -0.0050 0.0081 -0.0057 391 TRP B CA 6160 C C . TRP B 391 ? 0.1379 0.1296 0.1230 -0.0038 0.0037 -0.0037 391 TRP B C 6161 O O . TRP B 391 ? 0.1460 0.1282 0.1296 -0.0011 0.0094 -0.0050 391 TRP B O 6162 C CB . TRP B 391 ? 0.1394 0.1316 0.1274 -0.0007 0.0066 0.0000 391 TRP B CB 6163 C CG . TRP B 391 ? 0.1163 0.1160 0.1322 -0.0078 0.0042 -0.0036 391 TRP B CG 6164 C CD1 . TRP B 391 ? 0.1492 0.1331 0.1347 0.0054 -0.0008 -0.0116 391 TRP B CD1 6165 C CD2 . TRP B 391 ? 0.1234 0.1371 0.1271 -0.0017 0.0066 -0.0047 391 TRP B CD2 6166 N NE1 . TRP B 391 ? 0.1475 0.1507 0.1503 0.0012 -0.0018 -0.0080 391 TRP B NE1 6167 C CE2 . TRP B 391 ? 0.1395 0.1194 0.1262 0.0052 0.0045 0.0025 391 TRP B CE2 6168 C CE3 . TRP B 391 ? 0.1568 0.1362 0.1334 -0.0002 0.0011 0.0003 391 TRP B CE3 6169 C CZ2 . TRP B 391 ? 0.1382 0.1329 0.1390 0.0037 0.0050 0.0038 391 TRP B CZ2 6170 C CZ3 . TRP B 391 ? 0.1495 0.1355 0.1368 -0.0017 0.0050 -0.0032 391 TRP B CZ3 6171 C CH2 . TRP B 391 ? 0.1404 0.1328 0.1454 0.0179 0.0063 -0.0071 391 TRP B CH2 6172 N N . GLY B 392 ? 0.1419 0.1279 0.1200 -0.0022 0.0053 0.0021 392 GLY B N 6173 C CA . GLY B 392 ? 0.1436 0.1353 0.1244 -0.0030 0.0071 -0.0020 392 GLY B CA 6174 C C . GLY B 392 ? 0.1549 0.1439 0.1393 0.0020 0.0050 0.0000 392 GLY B C 6175 O O . GLY B 392 ? 0.1644 0.1462 0.1439 0.0046 0.0167 -0.0016 392 GLY B O 6176 N N . GLU B 393 ? 0.1669 0.1584 0.1434 0.0076 0.0117 -0.0023 393 GLU B N 6177 C CA . GLU B 393 ? 0.1741 0.1711 0.1635 0.0098 0.0112 -0.0055 393 GLU B CA 6178 C C . GLU B 393 ? 0.1768 0.1818 0.1697 0.0076 0.0131 -0.0074 393 GLU B C 6179 O O . GLU B 393 ? 0.1577 0.1801 0.1796 0.0051 0.0262 -0.0150 393 GLU B O 6180 C CB . GLU B 393 ? 0.1823 0.1800 0.1743 0.0132 0.0180 -0.0013 393 GLU B CB 6181 C CG . GLU B 393 ? 0.2217 0.2140 0.1960 0.0099 0.0162 0.0075 393 GLU B CG 6182 C CD . GLU B 393 ? 0.2235 0.2324 0.1960 0.0154 0.0197 -0.0075 393 GLU B CD 6183 O OE1 . GLU B 393 ? 0.2322 0.2593 0.1795 0.0060 0.0467 -0.0364 393 GLU B OE1 6184 O OE2 . GLU B 393 ? 0.3067 0.3105 0.2391 0.0105 0.0138 0.0049 393 GLU B OE2 6185 N N . ILE B 394 ? 0.1795 0.1891 0.1691 0.0063 0.0140 -0.0064 394 ILE B N 6186 C CA . ILE B 394 ? 0.1871 0.1879 0.1841 0.0074 0.0096 -0.0041 394 ILE B CA 6187 C C . ILE B 394 ? 0.1881 0.1862 0.1796 0.0049 0.0114 -0.0009 394 ILE B C 6188 O O . ILE B 394 ? 0.2138 0.2047 0.1827 0.0090 0.0238 -0.0059 394 ILE B O 6189 C CB . ILE B 394 ? 0.2037 0.1940 0.1969 0.0040 0.0077 0.0000 394 ILE B CB 6190 C CG1 . ILE B 394 ? 0.2302 0.2263 0.2390 0.0024 0.0063 0.0116 394 ILE B CG1 6191 C CG2 . ILE B 394 ? 0.2101 0.2033 0.2022 0.0066 0.0014 -0.0054 394 ILE B CG2 6192 C CD1 . ILE B 394 ? 0.2518 0.2240 0.2485 0.0039 0.0058 -0.0001 394 ILE B CD1 6193 N N . GLY B 395 ? 0.1831 0.1826 0.1868 0.0062 0.0117 -0.0097 395 GLY B N 6194 C CA . GLY B 395 ? 0.1864 0.1907 0.1936 0.0048 0.0123 -0.0063 395 GLY B CA 6195 C C . GLY B 395 ? 0.1875 0.2061 0.2054 -0.0029 0.0070 -0.0038 395 GLY B C 6196 O O . GLY B 395 ? 0.1994 0.2299 0.2753 -0.0091 0.0206 0.0055 395 GLY B O 6197 N N . SER B 396 ? 0.1751 0.1803 0.1837 0.0058 0.0189 -0.0085 396 SER B N 6198 C CA . SER B 396 ? 0.1750 0.1803 0.1798 -0.0026 0.0172 -0.0019 396 SER B CA 6199 C C . SER B 396 ? 0.1829 0.1743 0.1743 0.0008 0.0213 -0.0026 396 SER B C 6200 O O . SER B 396 ? 0.1828 0.1927 0.1754 -0.0038 0.0328 0.0021 396 SER B O 6201 C CB . SER B 396 ? 0.1892 0.1805 0.1793 -0.0053 0.0125 -0.0055 396 SER B CB 6202 O OG . SER B 396 ? 0.1822 0.1574 0.1991 0.0003 0.0207 -0.0069 396 SER B OG 6203 N N . THR B 397 ? 0.1964 0.1646 0.1729 -0.0077 0.0186 0.0048 397 THR B N 6204 C CA . THR B 397 ? 0.1998 0.1822 0.1914 0.0016 0.0191 -0.0012 397 THR B CA 6205 C C . THR B 397 ? 0.2263 0.2054 0.2042 -0.0041 0.0154 -0.0111 397 THR B C 6206 O O . THR B 397 ? 0.2509 0.2251 0.2079 -0.0077 0.0250 -0.0254 397 THR B O 6207 C CB . THR B 397 ? 0.1937 0.1626 0.1714 0.0149 0.0241 0.0010 397 THR B CB 6208 O OG1 . THR B 397 ? 0.2002 0.1666 0.1672 0.0116 0.0302 0.0021 397 THR B OG1 6209 C CG2 . THR B 397 ? 0.1971 0.1609 0.2017 0.0116 0.0315 0.0072 397 THR B CG2 6210 N N . TYR B 398 ? 0.2278 0.2289 0.2063 -0.0051 0.0089 -0.0070 398 TYR B N 6211 C CA . TYR B 398 ? 0.2402 0.2546 0.2380 -0.0041 0.0024 -0.0031 398 TYR B CA 6212 C C . TYR B 398 ? 0.2708 0.3007 0.2685 -0.0046 0.0015 -0.0035 398 TYR B C 6213 O O . TYR B 398 ? 0.2961 0.3430 0.2891 -0.0018 0.0218 0.0042 398 TYR B O 6214 C CB . TYR B 398 ? 0.2523 0.2610 0.2435 -0.0025 0.0040 -0.0034 398 TYR B CB 6215 C CG . TYR B 398 ? 0.2416 0.2528 0.2360 -0.0059 0.0072 0.0052 398 TYR B CG 6216 C CD1 . TYR B 398 ? 0.2144 0.2510 0.1995 -0.0128 0.0098 0.0067 398 TYR B CD1 6217 C CD2 . TYR B 398 ? 0.2350 0.2560 0.2304 -0.0119 -0.0003 0.0142 398 TYR B CD2 6218 C CE1 . TYR B 398 ? 0.2160 0.2570 0.2351 -0.0035 0.0157 0.0023 398 TYR B CE1 6219 C CE2 . TYR B 398 ? 0.2326 0.2545 0.2386 0.0076 0.0164 0.0103 398 TYR B CE2 6220 C CZ . TYR B 398 ? 0.2474 0.2574 0.2334 0.0063 0.0128 -0.0052 398 TYR B CZ 6221 O OH . TYR B 398 ? 0.2829 0.2581 0.2895 -0.0019 0.0129 -0.0004 398 TYR B OH 6222 N N . GLN B 399 ? 0.2921 0.3339 0.3068 -0.0143 -0.0071 -0.0053 399 GLN B N 6223 C C2 . BGC C . ? 0.4765 0.4780 0.4716 0.0010 -0.0056 0.0084 1400 BGC A C2 6224 C C3 . BGC C . ? 0.4580 0.4654 0.4566 -0.0002 -0.0054 0.0043 1400 BGC A C3 6225 C C4 . BGC C . ? 0.4352 0.4293 0.4291 0.0023 -0.0112 0.0027 1400 BGC A C4 6226 C C5 . BGC C . ? 0.4246 0.4382 0.4391 0.0034 -0.0028 0.0051 1400 BGC A C5 6227 C C6 . BGC C . ? 0.4251 0.4137 0.4257 0.0004 0.0016 0.0048 1400 BGC A C6 6228 C C1 . BGC C . ? 0.4749 0.4810 0.4751 -0.0012 -0.0051 0.0101 1400 BGC A C1 6229 O O1 . BGC C . ? 0.4919 0.4838 0.5030 0.0058 -0.0017 0.0073 1400 BGC A O1 6230 O O2 . BGC C . ? 0.4984 0.5197 0.5017 -0.0059 -0.0039 0.0112 1400 BGC A O2 6231 O O3 . BGC C . ? 0.4724 0.4770 0.4530 0.0022 -0.0049 0.0025 1400 BGC A O3 6232 O O4 . BGC C . ? 0.3986 0.3976 0.4033 -0.0073 -0.0219 -0.0036 1400 BGC A O4 6233 O O5 . BGC C . ? 0.4650 0.4607 0.4666 -0.0014 -0.0137 0.0143 1400 BGC A O5 6234 O O6 . BGC C . ? 0.3792 0.3611 0.4133 -0.0049 -0.0011 0.0206 1400 BGC A O6 6235 C C1 . GAL D . ? 0.3674 0.3851 0.3611 0.0037 -0.0057 0.0015 1403 GAL A C1 6236 C C2 . GAL D . ? 0.3571 0.3771 0.3625 -0.0030 0.0053 0.0047 1403 GAL A C2 6237 C C3 . GAL D . ? 0.3404 0.3721 0.3501 0.0099 0.0016 -0.0029 1403 GAL A C3 6238 C C4 . GAL D . ? 0.3554 0.3808 0.3567 -0.0011 0.0045 0.0071 1403 GAL A C4 6239 C C5 . GAL D . ? 0.3713 0.3855 0.3655 0.0024 -0.0048 0.0003 1403 GAL A C5 6240 C C6 . GAL D . ? 0.3764 0.4147 0.3761 0.0071 -0.0020 0.0003 1403 GAL A C6 6241 O O2 . GAL D . ? 0.3340 0.3504 0.3246 -0.0163 -0.0026 -0.0043 1403 GAL A O2 6242 O O3 . GAL D . ? 0.3450 0.3705 0.3456 0.0145 -0.0017 -0.0128 1403 GAL A O3 6243 O O4 . GAL D . ? 0.3722 0.3928 0.3622 -0.0011 -0.0041 0.0054 1403 GAL A O4 6244 O O5 . GAL D . ? 0.3703 0.3796 0.3736 -0.0007 -0.0080 -0.0050 1403 GAL A O5 6245 O O6 . GAL D . ? 0.4165 0.4666 0.3661 0.0097 0.0061 0.0106 1403 GAL A O6 6246 C C1 . GLC E . ? 0.1301 0.1709 0.1629 -0.0034 0.0212 0.0111 1401 GLC A C1 6247 C C2 . GLC E . ? 0.1035 0.1454 0.1480 0.0139 0.0067 -0.0096 1401 GLC A C2 6248 C C3 . GLC E . ? 0.1321 0.1243 0.1252 -0.0064 0.0040 0.0041 1401 GLC A C3 6249 C C4 . GLC E . ? 0.1053 0.1159 0.0955 0.0059 0.0010 0.0085 1401 GLC A C4 6250 C C5 . GLC E . ? 0.1093 0.1163 0.1166 0.0033 0.0028 0.0023 1401 GLC A C5 6251 C C6 . GLC E . ? 0.1125 0.1178 0.1184 0.0087 -0.0036 0.0048 1401 GLC A C6 6252 O O1 . GLC E . ? 0.1721 0.1945 0.1692 0.0079 0.0062 0.0390 1401 GLC A O1 6253 O O2 . GLC E . ? 0.1699 0.1495 0.1493 -0.0097 0.0095 -0.0119 1401 GLC A O2 6254 O O3 . GLC E . ? 0.1130 0.1178 0.1043 -0.0104 0.0007 0.0002 1401 GLC A O3 6255 O O4 . GLC E . ? 0.1061 0.1178 0.1171 0.0083 -0.0044 -0.0081 1401 GLC A O4 6256 O O5 . GLC E . ? 0.1161 0.1156 0.1269 0.0180 -0.0129 -0.0098 1401 GLC A O5 6257 O O6 . GLC E . ? 0.1148 0.1414 0.1265 0.0008 -0.0175 -0.0082 1401 GLC A O6 6258 C C1 . GAL F . ? 0.0815 0.1055 0.1211 -0.0008 -0.0007 -0.0098 1402 GAL A C1 6259 C C2 . GAL F . ? 0.1073 0.1163 0.1108 0.0043 -0.0038 -0.0023 1402 GAL A C2 6260 C C3 . GAL F . ? 0.1218 0.1189 0.1157 0.0084 -0.0095 0.0029 1402 GAL A C3 6261 C C4 . GAL F . ? 0.1090 0.1312 0.1179 -0.0052 -0.0049 -0.0220 1402 GAL A C4 6262 C C5 . GAL F . ? 0.1037 0.1245 0.0955 -0.0064 -0.0010 0.0050 1402 GAL A C5 6263 C C6 . GAL F . ? 0.1337 0.1339 0.1299 -0.0132 0.0042 0.0107 1402 GAL A C6 6264 O O2 . GAL F . ? 0.1010 0.1113 0.1343 -0.0013 0.0033 -0.0001 1402 GAL A O2 6265 O O3 . GAL F . ? 0.1143 0.1041 0.1348 0.0064 -0.0097 0.0120 1402 GAL A O3 6266 O O4 . GAL F . ? 0.1064 0.1467 0.1220 -0.0045 -0.0089 0.0015 1402 GAL A O4 6267 O O5 . GAL F . ? 0.1180 0.1338 0.0994 -0.0065 0.0127 -0.0055 1402 GAL A O5 6268 O O6 . GAL F . ? 0.1945 0.1507 0.1739 -0.0024 -0.0069 0.0210 1402 GAL A O6 6269 C C1 . NAG G . ? 0.2409 0.2576 0.2174 0.0133 -0.0440 0.0074 1404 NAG A C1 6270 C C2 . NAG G . ? 0.2532 0.2774 0.2476 0.0261 -0.0321 0.0073 1404 NAG A C2 6271 C C3 . NAG G . ? 0.2804 0.2879 0.2862 0.0315 -0.0312 0.0115 1404 NAG A C3 6272 C C4 . NAG G . ? 0.2917 0.3179 0.3058 0.0253 -0.0335 0.0081 1404 NAG A C4 6273 C C5 . NAG G . ? 0.2742 0.3144 0.2977 0.0295 -0.0427 0.0066 1404 NAG A C5 6274 C C6 . NAG G . ? 0.2939 0.3220 0.3111 0.0191 -0.0220 -0.0050 1404 NAG A C6 6275 C C7 . NAG G . ? 0.3019 0.2604 0.2643 0.0185 -0.0108 -0.0008 1404 NAG A C7 6276 C C8 . NAG G . ? 0.3104 0.2669 0.2793 0.0048 -0.0218 0.0022 1404 NAG A C8 6277 N N2 . NAG G . ? 0.2930 0.2095 0.2487 0.0213 -0.0308 0.0286 1404 NAG A N2 6278 O O3 . NAG G . ? 0.3461 0.3151 0.3364 0.0353 -0.0358 0.0019 1404 NAG A O3 6279 O O4 . NAG G . ? 0.3209 0.3532 0.3638 0.0421 -0.0590 0.0172 1404 NAG A O4 6280 O O5 . NAG G . ? 0.2281 0.2971 0.2600 0.0389 -0.0623 0.0081 1404 NAG A O5 6281 O O6 . NAG G . ? 0.2900 0.3571 0.3297 0.0185 -0.0325 -0.0143 1404 NAG A O6 6282 O O7 . NAG G . ? 0.3172 0.2561 0.2342 0.0319 -0.0413 0.0048 1404 NAG A O7 6283 C C1 . NAG H . ? 0.2256 0.1985 0.1745 0.0106 -0.0255 0.0079 1399 NAG B C1 6284 C C2 . NAG H . ? 0.2234 0.1960 0.1576 0.0201 -0.0323 0.0004 1399 NAG B C2 6285 C C3 . NAG H . ? 0.2326 0.1954 0.2108 0.0255 -0.0387 0.0091 1399 NAG B C3 6286 C C4 . NAG H . ? 0.2366 0.2279 0.2251 0.0244 -0.0314 0.0251 1399 NAG B C4 6287 C C5 . NAG H . ? 0.2647 0.2499 0.2551 0.0135 -0.0331 0.0147 1399 NAG B C5 6288 C C6 . NAG H . ? 0.2845 0.3144 0.3075 0.0144 -0.0169 0.0064 1399 NAG B C6 6289 C C7 . NAG H . ? 0.2223 0.1634 0.1616 0.0205 -0.0174 0.0118 1399 NAG B C7 6290 C C8 . NAG H . ? 0.2161 0.1732 0.1693 0.0165 -0.0273 -0.0134 1399 NAG B C8 6291 N N2 . NAG H . ? 0.2228 0.1498 0.1745 0.0122 -0.0297 0.0115 1399 NAG B N2 6292 O O3 . NAG H . ? 0.2715 0.1936 0.1942 0.0374 -0.0321 0.0080 1399 NAG B O3 6293 O O4 . NAG H . ? 0.2435 0.2859 0.2981 0.0648 -0.0592 0.0188 1399 NAG B O4 6294 O O5 . NAG H . ? 0.2078 0.2210 0.2142 0.0291 -0.0348 0.0090 1399 NAG B O5 6295 O O6 . NAG H . ? 0.3260 0.3437 0.3818 0.0010 -0.0172 0.0037 1399 NAG B O6 6296 O O7 . NAG H . ? 0.2694 0.1725 0.1540 0.0231 -0.0330 -0.0120 1399 NAG B O7 6297 C C2 . BGC I . ? 0.4358 0.4306 0.4229 0.0010 -0.0031 0.0080 1401 BGC B C2 6298 C C3 . BGC I . ? 0.4140 0.4173 0.4013 0.0016 0.0011 0.0050 1401 BGC B C3 6299 C C4 . BGC I . ? 0.3856 0.3793 0.3819 -0.0022 -0.0173 0.0022 1401 BGC B C4 6300 C C5 . BGC I . ? 0.4017 0.4032 0.3969 0.0014 -0.0030 0.0033 1401 BGC B C5 6301 C C6 . BGC I . ? 0.4123 0.4096 0.4109 -0.0012 -0.0013 0.0051 1401 BGC B C6 6302 C C1 . BGC I . ? 0.4355 0.4439 0.4369 -0.0004 0.0025 0.0132 1401 BGC B C1 6303 O O1 . BGC I . ? 0.4648 0.4603 0.4612 0.0106 -0.0064 0.0117 1401 BGC B O1 6304 O O2 . BGC I . ? 0.4700 0.4647 0.4378 -0.0053 0.0014 0.0115 1401 BGC B O2 6305 O O3 . BGC I . ? 0.4355 0.4278 0.3995 0.0039 -0.0034 0.0007 1401 BGC B O3 6306 O O4 . BGC I . ? 0.3398 0.3116 0.3210 -0.0297 -0.0116 0.0079 1401 BGC B O4 6307 O O5 . BGC I . ? 0.4214 0.4130 0.4312 0.0038 -0.0065 0.0121 1401 BGC B O5 6308 O O6 . BGC I . ? 0.4129 0.3976 0.4062 -0.0166 0.0123 0.0146 1401 BGC B O6 6309 C C1 . GAL J . ? 0.3121 0.3059 0.2880 0.0022 -0.0075 -0.0022 1404 GAL B C1 6310 C C2 . GAL J . ? 0.2888 0.3255 0.2891 0.0023 -0.0010 -0.0005 1404 GAL B C2 6311 C C3 . GAL J . ? 0.2759 0.3144 0.2874 0.0003 0.0071 -0.0141 1404 GAL B C3 6312 C C4 . GAL J . ? 0.2812 0.3234 0.2932 -0.0013 0.0118 -0.0097 1404 GAL B C4 6313 C C5 . GAL J . ? 0.3002 0.3240 0.3273 -0.0029 0.0073 -0.0055 1404 GAL B C5 6314 C C6 . GAL J . ? 0.3214 0.3602 0.3409 0.0040 0.0152 0.0045 1404 GAL B C6 6315 O O2 . GAL J . ? 0.2494 0.2881 0.2376 -0.0057 -0.0063 -0.0140 1404 GAL B O2 6316 O O3 . GAL J . ? 0.2816 0.3261 0.2893 0.0026 -0.0068 -0.0317 1404 GAL B O3 6317 O O4 . GAL J . ? 0.3227 0.3222 0.3107 -0.0055 0.0006 -0.0033 1404 GAL B O4 6318 O O5 . GAL J . ? 0.2911 0.3212 0.3325 -0.0152 -0.0034 0.0113 1404 GAL B O5 6319 O O6 . GAL J . ? 0.3567 0.3784 0.3705 0.0042 0.0004 0.0173 1404 GAL B O6 6320 C C1 . GLC K . ? 0.1473 0.1881 0.2057 -0.0121 0.0124 0.0021 1402 GLC B C1 6321 C C2 . GLC K . ? 0.1351 0.1550 0.1692 0.0048 0.0050 -0.0104 1402 GLC B C2 6322 C C3 . GLC K . ? 0.1232 0.1186 0.1378 -0.0049 0.0013 0.0029 1402 GLC B C3 6323 C C4 . GLC K . ? 0.1097 0.1250 0.1301 0.0097 -0.0012 -0.0031 1402 GLC B C4 6324 C C5 . GLC K . ? 0.1208 0.1305 0.1342 0.0055 0.0077 0.0036 1402 GLC B C5 6325 C C6 . GLC K . ? 0.1078 0.1331 0.1238 0.0088 0.0062 -0.0047 1402 GLC B C6 6326 O O1 . GLC K . ? 0.1889 0.2083 0.1906 0.0062 0.0073 0.0232 1402 GLC B O1 6327 O O2 . GLC K . ? 0.1554 0.1431 0.1816 -0.0194 -0.0104 -0.0214 1402 GLC B O2 6328 O O3 . GLC K . ? 0.1122 0.1249 0.1315 -0.0149 0.0151 -0.0025 1402 GLC B O3 6329 O O4 . GLC K . ? 0.1223 0.1310 0.1147 0.0025 0.0019 -0.0004 1402 GLC B O4 6330 O O5 . GLC K . ? 0.1259 0.1203 0.1214 0.0044 0.0023 -0.0055 1402 GLC B O5 6331 O O6 . GLC K . ? 0.1220 0.1512 0.1397 -0.0053 -0.0074 -0.0097 1402 GLC B O6 6332 C C1 . GAL L . ? 0.0988 0.1186 0.1318 0.0092 0.0104 0.0030 1403 GAL B C1 6333 C C2 . GAL L . ? 0.1222 0.1095 0.0977 0.0012 -0.0042 -0.0010 1403 GAL B C2 6334 C C3 . GAL L . ? 0.1073 0.1200 0.1125 -0.0056 -0.0087 -0.0097 1403 GAL B C3 6335 C C4 . GAL L . ? 0.1036 0.1329 0.1253 0.0114 0.0021 0.0022 1403 GAL B C4 6336 C C5 . GAL L . ? 0.1308 0.1295 0.1241 -0.0085 0.0047 0.0043 1403 GAL B C5 6337 C C6 . GAL L . ? 0.1618 0.1597 0.1273 -0.0019 0.0203 0.0026 1403 GAL B C6 6338 O O2 . GAL L . ? 0.1154 0.1137 0.1241 -0.0034 0.0035 0.0049 1403 GAL B O2 6339 O O3 . GAL L . ? 0.1061 0.1332 0.1439 0.0046 -0.0022 0.0059 1403 GAL B O3 6340 O O4 . GAL L . ? 0.1224 0.1515 0.1317 -0.0005 -0.0033 0.0077 1403 GAL B O4 6341 O O5 . GAL L . ? 0.1155 0.1174 0.1186 -0.0003 0.0136 -0.0021 1403 GAL B O5 6342 O O6 . GAL L . ? 0.2137 0.1678 0.1444 -0.0061 0.0077 0.0026 1403 GAL B O6 6343 O O . HOH M . ? 0.1710 0.1235 0.1551 -0.0039 -0.0139 -0.0086 2001 HOH A O 6344 O O . HOH M . ? 0.1490 0.1505 0.1629 -0.0054 0.0028 -0.0224 2002 HOH A O 6345 O O . HOH M . ? 0.2076 0.2571 0.1706 0.0399 -0.0157 0.0080 2003 HOH A O 6346 O O . HOH M . ? 0.2802 0.2607 0.1742 -0.0278 -0.0315 0.0181 2004 HOH A O 6347 O O . HOH M . ? 0.1794 0.1815 0.1716 0.0255 -0.0138 0.0032 2005 HOH A O 6348 O O . HOH M . ? 0.3402 0.3150 0.3923 0.0053 0.0145 0.0351 2006 HOH A O 6349 O O . HOH M . ? 0.3646 0.3376 0.3349 -0.0064 -0.0256 0.0664 2007 HOH A O 6350 O O . HOH M . ? 0.2660 0.2254 0.2605 -0.0013 -0.0153 -0.0105 2008 HOH A O 6351 O O . HOH M . ? 0.1718 0.1531 0.1875 -0.0014 -0.0101 -0.0339 2009 HOH A O 6352 O O . HOH M . ? 0.2602 0.1928 0.2040 0.0169 0.0121 0.0093 2010 HOH A O 6353 O O . HOH M . ? 0.3443 0.2527 0.2630 -0.0224 -0.0228 -0.0118 2011 HOH A O 6354 O O . HOH M . ? 0.1786 0.1901 0.3411 0.0145 -0.0163 -0.0738 2012 HOH A O 6355 O O . HOH M . ? 0.2287 0.2195 0.2504 0.0249 0.0022 -0.0422 2013 HOH A O 6356 O O . HOH M . ? 0.2405 0.1753 0.2653 -0.0455 0.0133 0.0006 2014 HOH A O 6357 O O . HOH M . ? 0.3210 0.2783 0.2528 0.0235 -0.0093 -0.0149 2015 HOH A O 6358 O O . HOH M . ? 0.3239 0.2263 0.2963 -0.0222 0.0256 -0.0117 2016 HOH A O 6359 O O . HOH M . ? 0.2932 0.2708 0.3374 0.0076 0.0396 -0.0350 2017 HOH A O 6360 O O . HOH M . ? 0.2265 0.1618 0.1647 -0.0058 -0.0069 0.0219 2018 HOH A O 6361 O O . HOH M . ? 0.1723 0.1444 0.1776 -0.0133 -0.0146 0.0081 2019 HOH A O 6362 O O . HOH M . ? 0.1664 0.1666 0.1368 0.0220 -0.0164 -0.0134 2020 HOH A O 6363 O O . HOH M . ? 0.2673 0.3014 0.2863 0.0052 -0.0096 -0.0012 2021 HOH A O 6364 O O . HOH M . ? 0.1939 0.1784 0.2238 -0.0097 -0.0283 0.0480 2022 HOH A O 6365 O O . HOH M . ? 0.1628 0.1414 0.1585 -0.0029 -0.0101 0.0139 2023 HOH A O 6366 O O . HOH M . ? 0.2633 0.2007 0.2382 -0.0137 0.0440 0.0335 2024 HOH A O 6367 O O . HOH M . ? 0.1023 0.1386 0.1703 -0.0233 -0.0034 -0.0033 2025 HOH A O 6368 O O . HOH M . ? 0.1884 0.2285 0.2788 0.0612 0.0183 -0.0001 2026 HOH A O 6369 O O . HOH M . ? 0.2339 0.3030 0.2811 -0.0315 -0.0138 -0.0570 2027 HOH A O 6370 O O . HOH M . ? 0.1921 0.2828 0.2192 -0.0213 0.0410 -0.0006 2028 HOH A O 6371 O O . HOH M . ? 0.2373 0.1959 0.2294 -0.0192 0.0262 0.0158 2029 HOH A O 6372 O O . HOH M . ? 0.1301 0.1221 0.1204 -0.0098 0.0088 -0.0042 2030 HOH A O 6373 O O . HOH M . ? 0.4166 0.4602 0.4420 -0.0003 0.0025 0.0223 2031 HOH A O 6374 O O . HOH M . ? 0.2458 0.1771 0.2310 -0.0262 0.0317 0.0040 2032 HOH A O 6375 O O . HOH M . ? 0.3789 0.4080 0.3820 -0.0189 0.0019 0.0091 2033 HOH A O 6376 O O . HOH M . ? 0.3413 0.2394 0.2978 -0.0482 -0.0003 -0.0099 2034 HOH A O 6377 O O . HOH M . ? 0.2297 0.3394 0.3338 0.0041 -0.0107 -0.0024 2035 HOH A O 6378 O O . HOH M . ? 0.3142 0.2207 0.2480 0.0393 0.0393 0.0371 2036 HOH A O 6379 O O . HOH M . ? 0.2269 0.2728 0.2366 -0.0057 0.0214 -0.0026 2037 HOH A O 6380 O O . HOH M . ? 0.2625 0.3105 0.2490 -0.0148 0.0187 0.0328 2038 HOH A O 6381 O O . HOH M . ? 0.3323 0.3634 0.2422 0.0279 -0.0035 0.0282 2039 HOH A O 6382 O O . HOH M . ? 0.2102 0.2707 0.2440 -0.0022 -0.0012 -0.0425 2040 HOH A O 6383 O O . HOH M . ? 0.1470 0.1413 0.1308 0.0040 0.0160 0.0109 2041 HOH A O 6384 O O . HOH M . ? 0.1140 0.1505 0.1357 -0.0114 -0.0074 0.0064 2042 HOH A O 6385 O O . HOH M . ? 0.3261 0.3327 0.2891 -0.0091 0.0195 0.0075 2043 HOH A O 6386 O O . HOH M . ? 0.1791 0.1752 0.1796 -0.0007 -0.0106 -0.0020 2044 HOH A O 6387 O O . HOH M . ? 0.1212 0.1494 0.1431 0.0184 -0.0068 -0.0106 2045 HOH A O 6388 O O . HOH M . ? 0.3249 0.3218 0.2448 0.0464 0.0174 0.0353 2046 HOH A O 6389 O O . HOH M . ? 0.2632 0.3491 0.2535 0.0069 -0.0338 0.0461 2047 HOH A O 6390 O O . HOH M . ? 0.3336 0.4289 0.2872 -0.0136 -0.0050 0.0240 2048 HOH A O 6391 O O . HOH M . ? 0.2807 0.4041 0.3731 0.0166 0.0071 -0.0340 2049 HOH A O 6392 O O . HOH M . ? 0.3500 0.4468 0.3945 0.0081 0.0069 0.0019 2050 HOH A O 6393 O O . HOH M . ? 0.2710 0.2103 0.2694 -0.0340 -0.0183 0.0315 2051 HOH A O 6394 O O . HOH M . ? 0.1392 0.1583 0.1387 0.0101 -0.0316 0.0089 2052 HOH A O 6395 O O . HOH M . ? 0.3094 0.2828 0.1740 -0.0550 0.0167 0.0097 2053 HOH A O 6396 O O . HOH M . ? 0.2853 0.2784 0.2555 -0.0190 -0.0109 -0.0142 2054 HOH A O 6397 O O . HOH M . ? 0.2530 0.2297 0.2515 0.0054 0.0023 0.0200 2055 HOH A O 6398 O O . HOH M . ? 0.1784 0.2135 0.1814 0.0345 0.0006 -0.0016 2056 HOH A O 6399 O O . HOH M . ? 0.2797 0.2957 0.3646 -0.0315 -0.0506 0.0182 2057 HOH A O 6400 O O . HOH M . ? 0.2028 0.1281 0.2044 0.0052 0.0196 0.0026 2058 HOH A O 6401 O O . HOH M . ? 0.1631 0.1679 0.1102 -0.0024 -0.0039 0.0042 2059 HOH A O 6402 O O . HOH M . ? 0.1880 0.2136 0.2487 0.0213 0.0445 0.0056 2060 HOH A O 6403 O O . HOH M . ? 0.2996 0.2281 0.2525 0.0244 -0.0021 -0.0156 2061 HOH A O 6404 O O . HOH M . ? 0.3193 0.3586 0.4095 -0.0196 0.0479 -0.0272 2062 HOH A O 6405 O O . HOH M . ? 0.2627 0.2477 0.2606 0.0167 0.0566 -0.0033 2063 HOH A O 6406 O O . HOH M . ? 0.2799 0.2937 0.4160 0.0015 -0.0051 -0.0364 2064 HOH A O 6407 O O . HOH M . ? 0.3305 0.3407 0.2029 -0.0028 -0.0012 -0.0400 2065 HOH A O 6408 O O . HOH M . ? 0.1469 0.1381 0.1334 0.0068 0.0046 -0.0067 2066 HOH A O 6409 O O . HOH M . ? 0.1652 0.2222 0.2227 0.0019 0.0056 -0.0032 2067 HOH A O 6410 O O . HOH M . ? 0.2633 0.2332 0.2904 0.0425 0.0165 0.0187 2068 HOH A O 6411 O O . HOH M . ? 0.4183 0.4375 0.3733 -0.0119 0.0043 0.0123 2069 HOH A O 6412 O O . HOH M . ? 0.6386 0.6367 0.6328 0.0011 -0.0021 -0.0003 2070 HOH A O 6413 O O . HOH M . ? 0.3251 0.3956 0.3012 -0.0270 0.0495 -0.0021 2071 HOH A O 6414 O O . HOH M . ? 0.3256 0.2829 0.2782 0.0134 0.0049 -0.0023 2072 HOH A O 6415 O O . HOH M . ? 0.3358 0.3265 0.3276 0.0053 0.0515 0.0496 2073 HOH A O 6416 O O . HOH M . ? 0.1780 0.1757 0.2158 -0.0055 0.0194 0.0173 2074 HOH A O 6417 O O . HOH M . ? 0.2825 0.2440 0.2647 0.0232 0.0344 0.0622 2075 HOH A O 6418 O O . HOH M . ? 0.3797 0.3239 0.3290 0.0358 0.0318 -0.0030 2076 HOH A O 6419 O O . HOH M . ? 0.3002 0.3062 0.2212 -0.0122 0.0739 0.0326 2077 HOH A O 6420 O O . HOH M . ? 0.2514 0.2318 0.3481 -0.0252 -0.0240 -0.0328 2078 HOH A O 6421 O O . HOH M . ? 0.2708 0.2899 0.2773 -0.0486 -0.0327 0.0045 2079 HOH A O 6422 O O . HOH M . ? 0.3747 0.3020 0.3701 0.0130 0.0526 -0.0012 2080 HOH A O 6423 O O . HOH M . ? 0.1213 0.1372 0.1472 0.0140 0.0052 -0.0083 2081 HOH A O 6424 O O . HOH M . ? 0.3750 0.4147 0.4021 0.0215 0.0075 0.0124 2082 HOH A O 6425 O O . HOH M . ? 0.2535 0.1789 0.1885 0.0237 -0.0118 0.0262 2083 HOH A O 6426 O O . HOH M . ? 0.1881 0.1856 0.2532 0.0387 0.0244 -0.0057 2084 HOH A O 6427 O O . HOH M . ? 0.1654 0.1672 0.1799 0.0544 0.0216 -0.0145 2085 HOH A O 6428 O O . HOH M . ? 0.1866 0.1679 0.1649 0.0089 -0.0161 -0.0046 2086 HOH A O 6429 O O . HOH M . ? 0.3466 0.2553 0.3598 -0.0254 0.0196 0.0304 2087 HOH A O 6430 O O . HOH M . ? 0.3389 0.2410 0.2924 0.0204 0.0044 -0.0051 2088 HOH A O 6431 O O . HOH M . ? 0.3609 0.3273 0.3584 0.0331 -0.0197 -0.0373 2089 HOH A O 6432 O O . HOH M . ? 0.1790 0.2298 0.1788 0.0309 -0.0076 -0.0144 2090 HOH A O 6433 O O . HOH M . ? 0.3324 0.3558 0.3842 -0.0216 -0.0389 -0.0081 2091 HOH A O 6434 O O . HOH M . ? 0.5352 0.5066 0.5298 0.0024 -0.0157 -0.0117 2092 HOH A O 6435 O O . HOH M . ? 0.2275 0.1983 0.2513 0.0333 -0.0208 -0.0168 2093 HOH A O 6436 O O . HOH M . ? 0.1519 0.1857 0.2134 0.0030 -0.0162 0.0330 2094 HOH A O 6437 O O . HOH M . ? 0.2359 0.1860 0.2398 -0.0417 -0.0592 0.0010 2095 HOH A O 6438 O O . HOH M . ? 0.1513 0.1355 0.1477 -0.0084 0.0115 -0.0083 2096 HOH A O 6439 O O . HOH M . ? 0.1597 0.2300 0.2277 -0.0043 0.0017 0.0002 2097 HOH A O 6440 O O . HOH M . ? 0.1794 0.1454 0.2036 0.0045 -0.0140 0.0171 2098 HOH A O 6441 O O . HOH M . ? 0.3814 0.2934 0.3738 0.0018 -0.0583 0.0137 2099 HOH A O 6442 O O . HOH M . ? 0.2046 0.1739 0.2610 0.0058 0.0263 0.0038 2100 HOH A O 6443 O O . HOH M . ? 0.5165 0.4868 0.4848 -0.0090 -0.0039 -0.0145 2101 HOH A O 6444 O O . HOH M . ? 0.3685 0.2824 0.2918 -0.0376 0.0003 0.0212 2102 HOH A O 6445 O O . HOH M . ? 0.6341 0.6411 0.6514 -0.0009 0.0058 0.0089 2103 HOH A O 6446 O O . HOH M . ? 0.1692 0.2239 0.2620 -0.0102 0.0142 -0.0078 2104 HOH A O 6447 O O . HOH M . ? 0.2773 0.2786 0.3212 0.0172 -0.0131 0.0450 2105 HOH A O 6448 O O . HOH M . ? 0.3215 0.2813 0.3007 0.0152 0.0186 0.0304 2106 HOH A O 6449 O O . HOH M . ? 0.4737 0.5099 0.5228 0.0253 0.0155 -0.0146 2107 HOH A O 6450 O O . HOH M . ? 0.4252 0.3829 0.3469 -0.0197 -0.0101 -0.0318 2108 HOH A O 6451 O O . HOH M . ? 0.4148 0.2509 0.3168 -0.0123 0.0216 -0.0393 2109 HOH A O 6452 O O . HOH M . ? 0.2427 0.2082 0.2714 0.0201 -0.0046 0.0247 2110 HOH A O 6453 O O . HOH M . ? 0.2332 0.2357 0.2278 -0.0295 -0.0141 0.0099 2111 HOH A O 6454 O O . HOH M . ? 0.3350 0.3263 0.3235 -0.0044 0.0156 0.0170 2112 HOH A O 6455 O O . HOH M . ? 0.4052 0.4443 0.4133 -0.0139 0.0286 -0.0070 2113 HOH A O 6456 O O . HOH M . ? 0.2801 0.3243 0.2559 -0.0029 0.0000 0.0169 2114 HOH A O 6457 O O . HOH M . ? 0.2164 0.2557 0.2510 -0.0205 -0.0077 0.0223 2115 HOH A O 6458 O O . HOH M . ? 0.1429 0.2139 0.2109 -0.0224 -0.0059 0.0012 2116 HOH A O 6459 O O . HOH M . ? 0.1382 0.1360 0.1559 -0.0077 -0.0394 0.0019 2117 HOH A O 6460 O O . HOH M . ? 0.1596 0.1315 0.1594 -0.0040 -0.0187 -0.0058 2118 HOH A O 6461 O O . HOH M . ? 0.1502 0.1655 0.1607 0.0050 -0.0107 0.0113 2119 HOH A O 6462 O O . HOH M . ? 0.1668 0.1489 0.1306 0.0160 -0.0030 -0.0004 2120 HOH A O 6463 O O . HOH M . ? 0.1383 0.1474 0.1519 -0.0139 0.0200 0.0233 2121 HOH A O 6464 O O . HOH M . ? 0.1640 0.1689 0.1697 0.0018 0.0154 0.0151 2122 HOH A O 6465 O O . HOH M . ? 0.1332 0.1532 0.1575 -0.0084 -0.0104 0.0119 2123 HOH A O 6466 O O . HOH M . ? 0.3790 0.3752 0.3840 0.0056 0.0108 -0.0258 2124 HOH A O 6467 O O . HOH M . ? 0.3004 0.3235 0.2830 -0.0175 -0.0381 0.0029 2125 HOH A O 6468 O O . HOH M . ? 0.3463 0.3774 0.3346 0.0097 -0.0240 0.0048 2126 HOH A O 6469 O O . HOH M . ? 0.3158 0.2905 0.2905 0.0167 -0.0037 0.0047 2127 HOH A O 6470 O O . HOH M . ? 0.3804 0.3535 0.3514 0.0239 -0.0144 0.0383 2128 HOH A O 6471 O O . HOH M . ? 0.2931 0.2749 0.3485 -0.0503 0.0191 0.0060 2129 HOH A O 6472 O O . HOH M . ? 0.1442 0.1967 0.1986 -0.0018 0.0091 0.0122 2130 HOH A O 6473 O O . HOH M . ? 0.2641 0.2635 0.3230 0.0209 -0.0139 -0.0802 2131 HOH A O 6474 O O . HOH M . ? 0.2463 0.3250 0.3201 0.0172 -0.0333 0.0328 2132 HOH A O 6475 O O . HOH M . ? 0.3135 0.3124 0.3145 0.0025 -0.0062 0.0132 2133 HOH A O 6476 O O . HOH M . ? 0.2778 0.3919 0.2865 -0.0056 0.0094 -0.0062 2134 HOH A O 6477 O O . HOH M . ? 0.1225 0.1207 0.1273 -0.0026 -0.0038 0.0112 2135 HOH A O 6478 O O . HOH M . ? 0.2033 0.2582 0.2296 -0.0236 0.0438 0.0080 2136 HOH A O 6479 O O . HOH M . ? 0.2274 0.2938 0.2783 -0.0253 -0.0214 0.0244 2137 HOH A O 6480 O O . HOH M . ? 0.3589 0.2738 0.2481 -0.0075 -0.0055 0.0097 2138 HOH A O 6481 O O . HOH M . ? 0.1312 0.1317 0.1451 -0.0043 0.0118 -0.0027 2139 HOH A O 6482 O O . HOH M . ? 0.5177 0.5028 0.4403 -0.0059 0.0014 -0.0195 2140 HOH A O 6483 O O . HOH M . ? 0.3813 0.3788 0.4082 0.0050 0.0227 -0.0048 2141 HOH A O 6484 O O . HOH M . ? 0.2164 0.2082 0.2388 -0.0277 0.0658 0.0216 2142 HOH A O 6485 O O . HOH M . ? 0.2440 0.2331 0.2166 0.0392 -0.0341 -0.0342 2143 HOH A O 6486 O O . HOH M . ? 0.2000 0.1822 0.2011 -0.0353 0.0386 -0.0344 2144 HOH A O 6487 O O . HOH M . ? 0.1278 0.1200 0.1361 0.0000 0.0114 -0.0111 2145 HOH A O 6488 O O . HOH M . ? 0.2679 0.2899 0.3405 -0.0415 -0.0190 -0.0070 2146 HOH A O 6489 O O . HOH M . ? 0.2607 0.2878 0.2970 -0.0137 0.0551 -0.0070 2147 HOH A O 6490 O O . HOH M . ? 0.2502 0.2383 0.2413 0.0247 -0.0476 0.0047 2148 HOH A O 6491 O O . HOH M . ? 0.3152 0.2894 0.4011 -0.0169 -0.0322 -0.0342 2149 HOH A O 6492 O O . HOH M . ? 0.1520 0.2392 0.1767 0.0208 -0.0217 0.0059 2150 HOH A O 6493 O O . HOH M . ? 0.3469 0.3451 0.3922 -0.0159 -0.0208 -0.0046 2151 HOH A O 6494 O O . HOH M . ? 0.3984 0.3383 0.3933 -0.0015 0.0129 0.0226 2152 HOH A O 6495 O O . HOH M . ? 0.1977 0.1668 0.1632 0.0127 -0.0569 -0.0264 2153 HOH A O 6496 O O . HOH M . ? 0.1958 0.1664 0.1343 0.0136 -0.0225 -0.0274 2154 HOH A O 6497 O O . HOH M . ? 0.1437 0.1462 0.1454 0.0274 -0.0118 0.0050 2155 HOH A O 6498 O O . HOH M . ? 0.1611 0.2400 0.2405 -0.0041 -0.0350 0.0216 2156 HOH A O 6499 O O . HOH M . ? 0.1636 0.1467 0.1736 0.0014 0.0083 -0.0030 2157 HOH A O 6500 O O . HOH M . ? 0.1117 0.1532 0.1352 0.0027 0.0025 0.0117 2158 HOH A O 6501 O O . HOH M . ? 0.2777 0.3180 0.2585 0.0259 -0.0151 -0.0299 2159 HOH A O 6502 O O . HOH M . ? 0.2817 0.2793 0.2311 0.0439 -0.0345 -0.0388 2160 HOH A O 6503 O O . HOH M . ? 0.3089 0.3163 0.3269 -0.0285 -0.0214 0.0169 2161 HOH A O 6504 O O . HOH M . ? 0.1824 0.1867 0.1744 -0.0033 0.0244 -0.0035 2162 HOH A O 6505 O O . HOH M . ? 0.2818 0.3277 0.2925 -0.0088 -0.0749 -0.0370 2163 HOH A O 6506 O O . HOH M . ? 0.1444 0.1635 0.1969 0.0235 -0.0155 0.0017 2164 HOH A O 6507 O O . HOH M . ? 0.2394 0.2792 0.2047 -0.0817 0.0051 -0.0069 2165 HOH A O 6508 O O . HOH M . ? 0.3173 0.2325 0.3365 -0.0079 0.0257 0.0113 2166 HOH A O 6509 O O . HOH M . ? 0.2385 0.1914 0.2287 -0.0063 -0.0512 0.0026 2167 HOH A O 6510 O O . HOH M . ? 0.3503 0.2785 0.3068 0.0088 -0.0150 0.0003 2168 HOH A O 6511 O O . HOH M . ? 0.0957 0.0901 0.1165 0.0012 -0.0035 0.0063 2169 HOH A O 6512 O O . HOH M . ? 0.1328 0.1578 0.1120 0.0107 0.0076 -0.0180 2170 HOH A O 6513 O O . HOH M . ? 0.0897 0.1450 0.1167 0.0115 0.0074 0.0112 2171 HOH A O 6514 O O . HOH M . ? 0.3785 0.3235 0.3041 0.0179 -0.0599 0.0077 2172 HOH A O 6515 O O . HOH M . ? 0.2154 0.2736 0.2102 0.0038 0.0759 0.0181 2173 HOH A O 6516 O O . HOH M . ? 0.2715 0.3247 0.1799 0.0682 0.0268 0.0724 2174 HOH A O 6517 O O . HOH M . ? 0.1304 0.1385 0.1324 0.0026 -0.0016 0.0045 2175 HOH A O 6518 O O . HOH M . ? 0.1210 0.1197 0.1274 -0.0062 0.0086 0.0021 2176 HOH A O 6519 O O . HOH M . ? 0.2238 0.1916 0.2622 -0.0324 -0.0825 0.0346 2177 HOH A O 6520 O O . HOH M . ? 0.2732 0.1684 0.1672 -0.0030 0.0424 0.0002 2178 HOH A O 6521 O O . HOH M . ? 0.2192 0.4020 0.4143 -0.0281 -0.0269 -0.0038 2179 HOH A O 6522 O O . HOH M . ? 0.0992 0.1140 0.1220 -0.0024 -0.0056 0.0077 2180 HOH A O 6523 O O . HOH M . ? 0.1289 0.1449 0.1447 0.0143 -0.0021 -0.0041 2181 HOH A O 6524 O O . HOH M . ? 0.1287 0.1386 0.1624 0.0124 -0.0138 0.0014 2182 HOH A O 6525 O O . HOH M . ? 0.1895 0.2084 0.2874 0.0098 0.0017 -0.0318 2183 HOH A O 6526 O O . HOH M . ? 0.2664 0.1989 0.2296 -0.0044 0.0553 0.0104 2184 HOH A O 6527 O O . HOH M . ? 0.2752 0.2529 0.3145 0.0161 0.0344 0.0178 2185 HOH A O 6528 O O . HOH M . ? 0.3099 0.2674 0.3144 0.0280 0.0140 0.0172 2186 HOH A O 6529 O O . HOH M . ? 0.3006 0.3520 0.2551 -0.0084 0.0429 0.0133 2187 HOH A O 6530 O O . HOH M . ? 0.1108 0.1250 0.1122 -0.0077 0.0235 0.0169 2188 HOH A O 6531 O O . HOH M . ? 0.1473 0.1547 0.1532 0.0082 -0.0318 -0.0193 2189 HOH A O 6532 O O . HOH M . ? 0.2721 0.3332 0.2208 0.0631 -0.0068 -0.0094 2190 HOH A O 6533 O O . HOH M . ? 0.1675 0.1501 0.1862 0.0267 -0.0395 -0.0172 2191 HOH A O 6534 O O . HOH M . ? 0.1282 0.1333 0.1778 -0.0098 0.0092 -0.0053 2192 HOH A O 6535 O O . HOH M . ? 0.1244 0.1273 0.1629 0.0057 -0.0168 -0.0087 2193 HOH A O 6536 O O . HOH M . ? 0.1146 0.1313 0.1286 0.0062 0.0087 -0.0005 2194 HOH A O 6537 O O . HOH M . ? 0.2399 0.2127 0.2105 0.0298 0.0295 0.0128 2195 HOH A O 6538 O O . HOH M . ? 0.2294 0.2776 0.3647 -0.0150 0.0159 0.0235 2196 HOH A O 6539 O O . HOH M . ? 0.2126 0.2073 0.2269 0.0316 -0.0138 0.0256 2197 HOH A O 6540 O O . HOH M . ? 0.2331 0.3312 0.3509 0.0163 -0.0037 0.0204 2198 HOH A O 6541 O O . HOH M . ? 0.2320 0.2586 0.2591 -0.0007 -0.0299 0.0482 2199 HOH A O 6542 O O . HOH M . ? 0.3248 0.1826 0.2431 -0.0025 0.0369 -0.0013 2200 HOH A O 6543 O O . HOH M . ? 0.2105 0.1785 0.1778 0.0558 -0.0847 -0.0402 2201 HOH A O 6544 O O . HOH M . ? 0.3219 0.2600 0.2449 -0.0332 -0.0569 0.0225 2202 HOH A O 6545 O O . HOH M . ? 0.1791 0.1738 0.1965 -0.0012 -0.0009 0.0099 2203 HOH A O 6546 O O . HOH M . ? 0.2010 0.2029 0.2043 -0.0117 0.0009 0.0032 2204 HOH A O 6547 O O . HOH M . ? 0.1812 0.1829 0.2132 -0.0117 -0.0225 -0.0127 2205 HOH A O 6548 O O . HOH M . ? 0.2486 0.3187 0.2839 -0.0366 -0.0029 0.0051 2206 HOH A O 6549 O O . HOH M . ? 0.2469 0.1933 0.2622 0.0106 0.0397 0.0053 2207 HOH A O 6550 O O . HOH M . ? 0.2085 0.1850 0.2461 0.0218 0.0440 0.0376 2208 HOH A O 6551 O O . HOH M . ? 0.3802 0.3615 0.3583 0.0192 -0.0550 -0.0478 2209 HOH A O 6552 O O . HOH M . ? 0.2801 0.2571 0.2986 0.0339 0.0136 -0.0284 2210 HOH A O 6553 O O . HOH M . ? 0.1631 0.1355 0.1474 -0.0244 0.0281 0.0008 2211 HOH A O 6554 O O . HOH M . ? 0.3077 0.2292 0.1801 -0.0080 -0.0041 0.0235 2212 HOH A O 6555 O O . HOH M . ? 0.1874 0.1620 0.1840 0.0025 0.0237 0.0128 2213 HOH A O 6556 O O . HOH M . ? 0.1275 0.1083 0.1322 0.0069 0.0187 0.0091 2214 HOH A O 6557 O O . HOH M . ? 0.1284 0.1269 0.1370 0.0038 0.0021 0.0170 2215 HOH A O 6558 O O . HOH M . ? 0.1564 0.1338 0.1401 0.0177 -0.0081 0.0181 2216 HOH A O 6559 O O . HOH M . ? 0.1409 0.1197 0.1118 0.0110 0.0106 0.0116 2217 HOH A O 6560 O O . HOH M . ? 0.2816 0.2245 0.2378 -0.0481 0.0111 0.0175 2218 HOH A O 6561 O O . HOH M . ? 0.2612 0.2792 0.3723 -0.0276 0.0078 -0.0078 2219 HOH A O 6562 O O . HOH M . ? 0.1890 0.1865 0.1972 -0.0124 -0.0076 0.0379 2220 HOH A O 6563 O O . HOH M . ? 0.1494 0.1483 0.1532 0.0203 -0.0244 0.0090 2221 HOH A O 6564 O O . HOH M . ? 0.1390 0.1394 0.1705 0.0114 -0.0393 -0.0141 2222 HOH A O 6565 O O . HOH M . ? 0.3568 0.3483 0.3783 -0.0063 -0.0894 0.0379 2223 HOH A O 6566 O O . HOH M . ? 0.2330 0.2429 0.4180 0.0155 0.0632 0.0115 2224 HOH A O 6567 O O . HOH M . ? 0.2247 0.2076 0.2260 -0.0037 0.0420 -0.0343 2225 HOH A O 6568 O O . HOH M . ? 0.1739 0.1538 0.1659 0.0252 -0.0090 -0.0106 2226 HOH A O 6569 O O . HOH M . ? 0.3177 0.2995 0.2928 -0.0121 -0.0205 -0.0042 2227 HOH A O 6570 O O . HOH M . ? 0.3379 0.3408 0.3279 0.0599 -0.0333 -0.0190 2228 HOH A O 6571 O O . HOH M . ? 0.2438 0.3002 0.2749 0.0342 -0.0251 0.0101 2229 HOH A O 6572 O O . HOH M . ? 0.3051 0.3504 0.4086 0.0099 -0.0354 -0.0122 2230 HOH A O 6573 O O . HOH M . ? 0.1862 0.1672 0.1884 -0.0144 -0.0136 -0.0004 2231 HOH A O 6574 O O . HOH M . ? 0.2169 0.2063 0.2031 0.0343 -0.0143 -0.0017 2232 HOH A O 6575 O O . HOH M . ? 0.3326 0.4448 0.3775 -0.0029 -0.0500 -0.0075 2233 HOH A O 6576 O O . HOH M . ? 0.2636 0.3440 0.3732 -0.0084 0.0002 -0.0034 2234 HOH A O 6577 O O . HOH M . ? 0.2609 0.3758 0.3253 0.0168 -0.0180 -0.0180 2235 HOH A O 6578 O O . HOH M . ? 0.2436 0.3933 0.3488 0.0322 0.0186 0.0081 2236 HOH A O 6579 O O . HOH M . ? 0.2481 0.3301 0.3264 -0.0407 -0.0291 -0.0300 2237 HOH A O 6580 O O . HOH M . ? 0.3258 0.4020 0.3877 0.0040 -0.0129 -0.0192 2238 HOH A O 6581 O O . HOH M . ? 0.1346 0.1665 0.2010 -0.0030 -0.0163 -0.0123 2239 HOH A O 6582 O O . HOH M . ? 0.3625 0.2902 0.2925 -0.0263 -0.0262 -0.0486 2240 HOH A O 6583 O O . HOH M . ? 0.2948 0.3804 0.3045 -0.0408 -0.0363 0.0012 2241 HOH A O 6584 O O . HOH M . ? 0.2591 0.2784 0.2900 0.0168 0.0422 -0.0479 2242 HOH A O 6585 O O . HOH M . ? 0.2665 0.2414 0.1955 -0.0324 0.0449 -0.0246 2243 HOH A O 6586 O O . HOH M . ? 0.3617 0.4458 0.4012 -0.0018 0.0094 -0.0153 2244 HOH A O 6587 O O . HOH M . ? 0.1859 0.1964 0.2508 -0.0145 0.0476 -0.0127 2245 HOH A O 6588 O O . HOH M . ? 0.1433 0.1842 0.1943 -0.0228 -0.0229 0.0183 2246 HOH A O 6589 O O . HOH M . ? 0.4037 0.4250 0.4079 0.0027 0.0054 -0.0402 2247 HOH A O 6590 O O . HOH M . ? 0.1348 0.1486 0.1576 0.0145 -0.0087 -0.0091 2248 HOH A O 6591 O O . HOH M . ? 0.1551 0.1380 0.1829 0.0258 0.0090 0.0024 2249 HOH A O 6592 O O . HOH M . ? 0.2625 0.3201 0.3734 0.0275 -0.0065 0.0026 2250 HOH A O 6593 O O . HOH M . ? 0.3064 0.3298 0.3494 -0.0150 -0.0158 -0.0017 2251 HOH A O 6594 O O . HOH M . ? 0.2872 0.3741 0.3093 -0.0122 0.0677 -0.0453 2252 HOH A O 6595 O O . HOH M . ? 0.1817 0.2967 0.3953 0.0387 0.0075 -0.0370 2253 HOH A O 6596 O O . HOH M . ? 0.1375 0.1463 0.1862 0.0210 -0.0091 -0.0400 2254 HOH A O 6597 O O . HOH M . ? 0.2225 0.3586 0.3131 0.0349 0.0007 0.0152 2255 HOH A O 6598 O O . HOH M . ? 0.4824 0.5354 0.5589 0.0360 -0.0005 0.0043 2256 HOH A O 6599 O O . HOH M . ? 0.2173 0.3296 0.3566 0.0654 -0.0286 -0.0298 2257 HOH A O 6600 O O . HOH M . ? 0.1632 0.1674 0.2216 0.0128 -0.0142 -0.0298 2258 HOH A O 6601 O O . HOH M . ? 0.2922 0.3063 0.2906 0.0250 0.0063 -0.0123 2259 HOH A O 6602 O O . HOH M . ? 0.2850 0.2710 0.2540 -0.0643 -0.0053 0.0035 2260 HOH A O 6603 O O . HOH M . ? 0.3708 0.2514 0.2664 -0.0005 0.0069 0.0123 2261 HOH A O 6604 O O . HOH M . ? 0.2967 0.2780 0.3118 0.0163 0.0267 -0.0350 2262 HOH A O 6605 O O . HOH M . ? 0.1722 0.1536 0.1741 0.0115 -0.0175 -0.0152 2263 HOH A O 6606 O O . HOH M . ? 0.3328 0.3368 0.3449 0.0159 -0.0172 -0.0044 2264 HOH A O 6607 O O . HOH M . ? 0.2965 0.2893 0.3021 -0.0106 -0.0092 -0.0093 2265 HOH A O 6608 O O . HOH M . ? 0.2534 0.2080 0.3700 -0.0076 0.0386 -0.0366 2266 HOH A O 6609 O O . HOH M . ? 0.2374 0.1307 0.1988 0.0339 -0.0214 0.0053 2267 HOH A O 6610 O O . HOH M . ? 0.3585 0.3630 0.2378 0.0092 0.0237 -0.0060 2268 HOH A O 6611 O O . HOH M . ? 0.4225 0.4009 0.4019 -0.0009 -0.0051 -0.0062 2269 HOH A O 6612 O O . HOH M . ? 0.2071 0.2811 0.2496 0.0255 -0.0325 -0.0179 2270 HOH A O 6613 O O . HOH M . ? 0.3400 0.3019 0.3702 0.0219 -0.0150 -0.0528 2271 HOH A O 6614 O O . HOH M . ? 0.1329 0.1245 0.1527 0.0012 -0.0215 -0.0216 2272 HOH A O 6615 O O . HOH M . ? 0.2438 0.2293 0.2038 0.0064 0.0109 -0.0205 2273 HOH A O 6616 O O . HOH M . ? 0.3157 0.4368 0.3279 -0.0093 -0.0122 0.0101 2274 HOH A O 6617 O O . HOH M . ? 0.2920 0.2404 0.2808 -0.0003 0.0158 0.0630 2275 HOH A O 6618 O O . HOH M . ? 0.1470 0.1548 0.1314 0.0019 0.0031 0.0020 2276 HOH A O 6619 O O . HOH M . ? 0.3524 0.2366 0.2758 0.0402 0.0037 -0.0286 2277 HOH A O 6620 O O . HOH M . ? 0.2891 0.2361 0.2490 0.0094 -0.0134 0.0184 2278 HOH A O 6621 O O . HOH M . ? 0.3683 0.3699 0.3428 -0.0306 0.0094 0.0116 2279 HOH A O 6622 O O . HOH M . ? 0.3546 0.3823 0.3509 0.0216 -0.0004 -0.0048 2280 HOH A O 6623 O O . HOH M . ? 0.1246 0.1374 0.1274 -0.0039 -0.0043 -0.0001 2281 HOH A O 6624 O O . HOH M . ? 0.1698 0.1777 0.1997 -0.0061 -0.0123 -0.0021 2282 HOH A O 6625 O O . HOH M . ? 0.2746 0.2777 0.2452 -0.0667 -0.0102 -0.0046 2283 HOH A O 6626 O O . HOH M . ? 0.2138 0.3473 0.2307 -0.0325 0.0226 -0.0192 2284 HOH A O 6627 O O . HOH M . ? 0.1608 0.1553 0.1510 0.0025 -0.0011 0.0036 2285 HOH A O 6628 O O . HOH M . ? 0.3276 0.2250 0.3164 0.0110 -0.0283 -0.0187 2286 HOH A O 6629 O O . HOH M . ? 0.1369 0.1384 0.1257 0.0007 0.0101 0.0082 2287 HOH A O 6630 O O . HOH M . ? 0.1512 0.2534 0.1802 -0.0233 -0.0102 0.0008 2288 HOH A O 6631 O O . HOH M . ? 0.4140 0.3925 0.4459 -0.0171 -0.0210 0.0068 2289 HOH A O 6632 O O . HOH M . ? 0.2847 0.2962 0.3208 0.0378 -0.0128 0.0281 2290 HOH A O 6633 O O . HOH M . ? 0.2708 0.2980 0.2243 -0.0229 0.0162 0.0168 2291 HOH A O 6634 O O . HOH M . ? 0.3902 0.3608 0.3672 -0.0031 -0.0313 0.0051 2292 HOH A O 6635 O O . HOH M . ? 0.2409 0.3025 0.1933 0.0262 0.0159 0.0024 2293 HOH A O 6636 O O . HOH M . ? 0.2154 0.1940 0.1340 0.0286 -0.0165 0.0380 2294 HOH A O 6637 O O . HOH M . ? 0.2166 0.2518 0.1512 0.0657 -0.0201 0.0161 2295 HOH A O 6638 O O . HOH M . ? 0.3341 0.3353 0.4094 -0.0185 -0.0147 0.0105 2296 HOH A O 6639 O O . HOH M . ? 0.2579 0.2172 0.2588 -0.0130 -0.0251 0.0045 2297 HOH A O 6640 O O . HOH M . ? 0.3815 0.3504 0.3188 -0.0056 0.0458 -0.0158 2298 HOH A O 6641 O O . HOH M . ? 0.2686 0.2307 0.2650 -0.0134 0.0161 0.0235 2299 HOH A O 6642 O O . HOH M . ? 0.4130 0.3860 0.3337 -0.0345 0.0006 -0.0145 2300 HOH A O 6643 O O . HOH M . ? 0.2324 0.2123 0.2120 -0.0250 -0.0386 -0.0015 2301 HOH A O 6644 O O . HOH M . ? 0.2079 0.1957 0.2192 -0.0023 -0.0485 0.0072 2302 HOH A O 6645 O O . HOH M . ? 0.1893 0.1719 0.1383 0.0079 -0.0062 -0.0122 2303 HOH A O 6646 O O . HOH M . ? 0.2824 0.2165 0.2092 0.0209 -0.0120 0.0251 2304 HOH A O 6647 O O . HOH M . ? 0.3615 0.3021 0.2211 0.0062 -0.0397 0.0195 2305 HOH A O 6648 O O . HOH M . ? 0.3382 0.2882 0.3429 -0.0045 -0.0122 -0.0276 2306 HOH A O 6649 O O . HOH M . ? 0.3605 0.3287 0.2171 0.0441 0.0211 0.0138 2307 HOH A O 6650 O O . HOH M . ? 0.2226 0.1829 0.1754 0.0092 -0.0299 -0.0018 2308 HOH A O 6651 O O . HOH M . ? 0.2794 0.3538 0.2264 0.0296 -0.0382 0.0035 2309 HOH A O 6652 O O . HOH M . ? 0.2137 0.2644 0.2063 0.0065 0.0117 -0.0559 2310 HOH A O 6653 O O . HOH M . ? 0.2710 0.3117 0.3278 0.0034 -0.0384 0.0050 2311 HOH A O 6654 O O . HOH M . ? 0.1956 0.2408 0.2030 -0.0025 -0.0375 -0.0307 2312 HOH A O 6655 O O . HOH M . ? 0.2574 0.2391 0.2019 0.0142 -0.0406 -0.0236 2313 HOH A O 6656 O O . HOH M . ? 0.2611 0.2212 0.1895 0.0272 0.0213 -0.0225 2314 HOH A O 6657 O O . HOH M . ? 0.2107 0.1489 0.1406 0.0071 -0.0022 -0.0127 2315 HOH A O 6658 O O . HOH M . ? 0.1402 0.1948 0.1767 0.0053 -0.0126 -0.0111 2316 HOH A O 6659 O O . HOH M . ? 0.4669 0.5303 0.5023 0.0014 -0.0012 0.0088 2317 HOH A O 6660 O O . HOH M . ? 0.1988 0.2118 0.2820 -0.0142 0.0263 -0.0071 2318 HOH A O 6661 O O . HOH M . ? 0.1720 0.1833 0.1767 0.0008 0.0022 0.0091 2319 HOH A O 6662 O O . HOH M . ? 0.2839 0.2936 0.3330 -0.0235 0.0305 0.0634 2320 HOH A O 6663 O O . HOH M . ? 0.2274 0.2511 0.2155 0.0186 -0.0020 -0.0081 2321 HOH A O 6664 O O . HOH M . ? 0.3577 0.3128 0.3111 -0.0105 0.0291 -0.0187 2322 HOH A O 6665 O O . HOH M . ? 0.3115 0.2634 0.2324 -0.0280 0.0374 -0.0385 2323 HOH A O 6666 O O . HOH M . ? 0.6007 0.5803 0.5728 -0.0090 0.0058 -0.0047 2324 HOH A O 6667 O O . HOH M . ? 0.4353 0.4891 0.4600 0.0112 0.0031 0.0016 2325 HOH A O 6668 O O . HOH M . ? 0.2031 0.3522 0.3607 -0.0166 0.0365 0.0115 2326 HOH A O 6669 O O . HOH M . ? 0.2140 0.3895 0.3753 0.0472 0.0620 -0.0025 2327 HOH A O 6670 O O . HOH M . ? 0.2525 0.2446 0.2310 0.0074 -0.0049 -0.0124 2328 HOH A O 6671 O O . HOH M . ? 0.1344 0.1834 0.1350 0.0192 -0.0068 -0.0037 2329 HOH A O 6672 O O . HOH M . ? 0.2030 0.1616 0.1558 -0.0081 -0.0210 0.0076 2330 HOH A O 6673 O O . HOH M . ? 0.3359 0.2953 0.3202 0.0120 -0.0221 0.0391 2331 HOH A O 6674 O O . HOH M . ? 0.1473 0.2040 0.1843 -0.0202 -0.0121 -0.0266 2332 HOH A O 6675 O O . HOH M . ? 0.2967 0.3139 0.3756 -0.0521 -0.0243 0.0262 2333 HOH A O 6676 O O . HOH N . ? 0.1803 0.1982 0.1625 0.0125 -0.0136 -0.0144 2001 HOH B O 6677 O O . HOH N . ? 0.1505 0.1876 0.2001 -0.0100 0.0109 -0.0344 2002 HOH B O 6678 O O . HOH N . ? 0.3094 0.3601 0.2864 0.0164 -0.0201 0.0539 2003 HOH B O 6679 O O . HOH N . ? 0.2432 0.2840 0.2740 0.0413 -0.0104 -0.0081 2004 HOH B O 6680 O O . HOH N . ? 0.4783 0.4739 0.4570 0.0107 -0.0278 0.0200 2005 HOH B O 6681 O O . HOH N . ? 0.3508 0.2417 0.4000 0.0317 -0.0380 0.0237 2006 HOH B O 6682 O O . HOH N . ? 0.1950 0.1818 0.2769 0.0222 -0.0232 -0.0302 2007 HOH B O 6683 O O . HOH N . ? 0.3181 0.2758 0.2489 0.0181 -0.0224 -0.0214 2008 HOH B O 6684 O O . HOH N . ? 0.3184 0.3341 0.2727 -0.0037 0.0194 0.0027 2009 HOH B O 6685 O O . HOH N . ? 0.4629 0.3792 0.4190 0.0031 -0.0064 0.0075 2010 HOH B O 6686 O O . HOH N . ? 0.1879 0.1877 0.1579 -0.0069 0.0028 0.0243 2011 HOH B O 6687 O O . HOH N . ? 0.2797 0.2201 0.2512 -0.0059 -0.0188 0.0451 2012 HOH B O 6688 O O . HOH N . ? 0.2271 0.1654 0.1985 0.0196 -0.0327 0.0089 2013 HOH B O 6689 O O . HOH N . ? 0.2471 0.1892 0.2155 -0.0573 0.0036 -0.0183 2014 HOH B O 6690 O O . HOH N . ? 0.2726 0.2799 0.2904 0.0132 0.0025 0.0079 2015 HOH B O 6691 O O . HOH N . ? 0.2604 0.1740 0.2214 0.0018 0.0459 0.0223 2016 HOH B O 6692 O O . HOH N . ? 0.2290 0.2002 0.2242 0.0591 -0.0062 0.0235 2017 HOH B O 6693 O O . HOH N . ? 0.1261 0.1324 0.1500 -0.0095 0.0057 0.0068 2018 HOH B O 6694 O O . HOH N . ? 0.3303 0.3750 0.3511 0.0046 -0.0227 0.0150 2019 HOH B O 6695 O O . HOH N . ? 0.3235 0.3246 0.3903 0.0087 0.0466 -0.0114 2020 HOH B O 6696 O O . HOH N . ? 0.1864 0.2324 0.2234 -0.0305 0.0248 -0.0105 2021 HOH B O 6697 O O . HOH N . ? 0.3163 0.2277 0.1970 0.0132 0.0368 0.0086 2022 HOH B O 6698 O O . HOH N . ? 0.1380 0.1472 0.1566 -0.0086 -0.0076 0.0083 2023 HOH B O 6699 O O . HOH N . ? 0.6296 0.5947 0.5937 0.0057 0.0053 0.0134 2024 HOH B O 6700 O O . HOH N . ? 0.5420 0.5519 0.5040 -0.0068 -0.0030 0.0018 2025 HOH B O 6701 O O . HOH N . ? 0.3824 0.3856 0.4061 -0.0191 -0.0265 0.0036 2026 HOH B O 6702 O O . HOH N . ? 0.2859 0.4043 0.3956 0.0012 0.0157 -0.0238 2027 HOH B O 6703 O O . HOH N . ? 0.2898 0.2143 0.2578 0.0002 0.0120 -0.0270 2028 HOH B O 6704 O O . HOH N . ? 0.3553 0.2932 0.3191 0.0348 0.0413 0.0149 2029 HOH B O 6705 O O . HOH N . ? 0.4772 0.4494 0.4707 -0.0087 0.0071 0.0172 2030 HOH B O 6706 O O . HOH N . ? 0.2592 0.2370 0.2378 -0.0215 0.0228 -0.0123 2031 HOH B O 6707 O O . HOH N . ? 0.2716 0.3326 0.2054 0.0303 0.0185 0.0096 2032 HOH B O 6708 O O . HOH N . ? 0.2836 0.3220 0.2437 -0.0080 -0.0016 -0.0471 2033 HOH B O 6709 O O . HOH N . ? 0.2812 0.3926 0.2552 0.0234 -0.0276 0.0302 2034 HOH B O 6710 O O . HOH N . ? 0.6235 0.6225 0.6143 0.0010 0.0006 0.0061 2035 HOH B O 6711 O O . HOH N . ? 0.1340 0.1314 0.1352 -0.0025 -0.0049 0.0019 2036 HOH B O 6712 O O . HOH N . ? 0.3437 0.4089 0.2703 -0.0003 0.0262 0.0447 2037 HOH B O 6713 O O . HOH N . ? 0.3259 0.3450 0.3234 0.0214 0.0623 0.0003 2038 HOH B O 6714 O O . HOH N . ? 0.1379 0.1595 0.1279 0.0142 0.0139 0.0015 2039 HOH B O 6715 O O . HOH N . ? 0.1207 0.1734 0.1352 0.0165 -0.0140 -0.0155 2040 HOH B O 6716 O O . HOH N . ? 0.1698 0.1959 0.1464 0.0322 -0.0081 -0.0202 2041 HOH B O 6717 O O . HOH N . ? 0.2050 0.2065 0.2049 -0.0035 0.0003 -0.0070 2042 HOH B O 6718 O O . HOH N . ? 0.4031 0.4209 0.3501 0.0044 0.0079 0.0053 2043 HOH B O 6719 O O . HOH N . ? 0.3386 0.3891 0.3601 -0.0091 0.0144 -0.0093 2044 HOH B O 6720 O O . HOH N . ? 0.3725 0.3936 0.2822 -0.0117 -0.0070 0.0249 2045 HOH B O 6721 O O . HOH N . ? 0.3258 0.3769 0.3146 0.0248 -0.0023 -0.0067 2046 HOH B O 6722 O O . HOH N . ? 0.3621 0.3714 0.2825 -0.0376 0.0218 0.0266 2047 HOH B O 6723 O O . HOH N . ? 0.3049 0.2997 0.2772 -0.0108 -0.0317 -0.0050 2048 HOH B O 6724 O O . HOH N . ? 0.2994 0.2827 0.2642 -0.0508 -0.0075 -0.0079 2049 HOH B O 6725 O O . HOH N . ? 0.2840 0.2039 0.2231 0.0179 0.0300 -0.0150 2050 HOH B O 6726 O O . HOH N . ? 0.3313 0.3650 0.3707 -0.0019 -0.0217 0.0130 2051 HOH B O 6727 O O . HOH N . ? 0.3610 0.3259 0.3005 0.0139 -0.0011 -0.0334 2052 HOH B O 6728 O O . HOH N . ? 0.3509 0.3414 0.2682 0.0419 -0.0035 -0.0155 2053 HOH B O 6729 O O . HOH N . ? 0.4412 0.4505 0.4545 0.0065 -0.0041 -0.0081 2054 HOH B O 6730 O O . HOH N . ? 0.3511 0.3472 0.4760 -0.0092 -0.0168 -0.0114 2055 HOH B O 6731 O O . HOH N . ? 0.3359 0.3402 0.3464 -0.0152 -0.0006 -0.0240 2056 HOH B O 6732 O O . HOH N . ? 0.1483 0.1360 0.1407 0.0060 0.0199 -0.0049 2057 HOH B O 6733 O O . HOH N . ? 0.2663 0.3110 0.2391 -0.0238 0.0056 -0.0170 2058 HOH B O 6734 O O . HOH N . ? 0.2976 0.2669 0.2676 0.0329 0.0486 0.0323 2059 HOH B O 6735 O O . HOH N . ? 0.4406 0.4110 0.3986 -0.0161 -0.0174 0.0206 2060 HOH B O 6736 O O . HOH N . ? 0.2954 0.2227 0.2582 0.0146 0.0544 0.0105 2061 HOH B O 6737 O O . HOH N . ? 0.2673 0.2759 0.3244 -0.0341 -0.0043 -0.0414 2062 HOH B O 6738 O O . HOH N . ? 0.1971 0.2443 0.2517 -0.0076 0.0127 0.0008 2063 HOH B O 6739 O O . HOH N . ? 0.3236 0.3059 0.2789 -0.0230 0.0018 0.0237 2064 HOH B O 6740 O O . HOH N . ? 0.3424 0.3478 0.3188 0.0156 0.0197 0.0098 2065 HOH B O 6741 O O . HOH N . ? 0.2718 0.2699 0.2726 -0.0431 0.0413 0.0285 2066 HOH B O 6742 O O . HOH N . ? 0.2774 0.3189 0.3727 -0.0353 -0.0129 -0.0270 2067 HOH B O 6743 O O . HOH N . ? 0.4392 0.4030 0.4681 -0.0223 -0.0121 -0.0193 2068 HOH B O 6744 O O . HOH N . ? 0.1832 0.2236 0.2215 0.0175 -0.0010 -0.0072 2069 HOH B O 6745 O O . HOH N . ? 0.2777 0.2302 0.2923 0.0307 -0.0017 -0.0055 2070 HOH B O 6746 O O . HOH N . ? 0.2963 0.2681 0.2962 0.0047 -0.0461 0.0110 2071 HOH B O 6747 O O . HOH N . ? 0.3363 0.3937 0.3328 0.0246 -0.0176 -0.0045 2072 HOH B O 6748 O O . HOH N . ? 0.2294 0.2180 0.2026 0.0505 0.0157 0.0269 2073 HOH B O 6749 O O . HOH N . ? 0.2415 0.2402 0.1925 0.0239 -0.0059 -0.0243 2074 HOH B O 6750 O O . HOH N . ? 0.3920 0.4333 0.4166 -0.0467 -0.0053 0.0067 2075 HOH B O 6751 O O . HOH N . ? 0.4351 0.4605 0.4869 -0.0059 -0.0019 -0.0218 2076 HOH B O 6752 O O . HOH N . ? 0.2604 0.2298 0.2131 0.0416 -0.0059 -0.0252 2077 HOH B O 6753 O O . HOH N . ? 0.2494 0.2292 0.3332 0.0582 -0.0522 -0.0310 2078 HOH B O 6754 O O . HOH N . ? 0.1963 0.2051 0.2126 -0.0117 0.0056 0.0161 2079 HOH B O 6755 O O . HOH N . ? 0.1544 0.1335 0.1565 -0.0009 -0.0081 0.0036 2080 HOH B O 6756 O O . HOH N . ? 0.1870 0.2503 0.2048 -0.0330 0.0091 0.0292 2081 HOH B O 6757 O O . HOH N . ? 0.2686 0.2064 0.2353 -0.0347 -0.0681 0.0234 2082 HOH B O 6758 O O . HOH N . ? 0.2335 0.1384 0.2398 0.0240 0.0104 0.0239 2083 HOH B O 6759 O O . HOH N . ? 0.4648 0.4693 0.5217 -0.0118 -0.0027 0.0092 2084 HOH B O 6760 O O . HOH N . ? 0.2408 0.2418 0.3296 -0.0062 0.0017 0.0326 2085 HOH B O 6761 O O . HOH N . ? 0.2591 0.2499 0.2758 0.0038 -0.0050 -0.0049 2086 HOH B O 6762 O O . HOH N . ? 0.1723 0.2734 0.3346 -0.0383 0.0064 -0.0276 2087 HOH B O 6763 O O . HOH N . ? 0.2862 0.3193 0.3104 0.0051 -0.0071 0.0101 2088 HOH B O 6764 O O . HOH N . ? 0.2480 0.2306 0.2493 0.0172 -0.0237 0.0212 2089 HOH B O 6765 O O . HOH N . ? 0.2791 0.2411 0.2676 0.0449 -0.0619 -0.0456 2090 HOH B O 6766 O O . HOH N . ? 0.3117 0.3595 0.2780 -0.0209 0.0195 -0.0104 2091 HOH B O 6767 O O . HOH N . ? 0.3342 0.3009 0.3542 -0.0027 -0.0109 0.0111 2092 HOH B O 6768 O O . HOH N . ? 0.2815 0.2728 0.2103 0.0036 0.0095 0.0582 2093 HOH B O 6769 O O . HOH N . ? 0.2578 0.3285 0.3314 0.0222 0.0377 -0.0027 2094 HOH B O 6770 O O . HOH N . ? 0.2325 0.2410 0.1941 -0.0120 -0.0058 0.0121 2095 HOH B O 6771 O O . HOH N . ? 0.1444 0.1922 0.1721 -0.0120 -0.0166 0.0048 2096 HOH B O 6772 O O . HOH N . ? 0.1451 0.1435 0.1452 0.0051 -0.0077 0.0059 2097 HOH B O 6773 O O . HOH N . ? 0.1940 0.1514 0.1383 0.0014 -0.0054 0.0035 2098 HOH B O 6774 O O . HOH N . ? 0.2200 0.2444 0.1965 -0.0019 0.0295 0.0245 2099 HOH B O 6775 O O . HOH N . ? 0.1479 0.1610 0.1240 0.0318 -0.0117 0.0187 2100 HOH B O 6776 O O . HOH N . ? 0.2158 0.2473 0.2556 0.0492 0.0187 -0.0101 2101 HOH B O 6777 O O . HOH N . ? 0.1727 0.1730 0.1519 0.0055 0.0028 -0.0004 2102 HOH B O 6778 O O . HOH N . ? 0.1388 0.1396 0.1475 -0.0155 -0.0022 0.0160 2103 HOH B O 6779 O O . HOH N . ? 0.4597 0.4247 0.4447 -0.0010 -0.0296 -0.0148 2104 HOH B O 6780 O O . HOH N . ? 0.3794 0.3533 0.2688 -0.0091 -0.0390 -0.0319 2105 HOH B O 6781 O O . HOH N . ? 0.4308 0.3449 0.4370 0.0137 0.0082 0.0096 2106 HOH B O 6782 O O . HOH N . ? 0.2559 0.3077 0.2316 0.0013 -0.0416 -0.0156 2107 HOH B O 6783 O O . HOH N . ? 0.2116 0.2775 0.1974 -0.0286 -0.0122 -0.0065 2108 HOH B O 6784 O O . HOH N . ? 0.2797 0.2402 0.1806 -0.0016 -0.0124 0.0077 2109 HOH B O 6785 O O . HOH N . ? 0.2450 0.2891 0.2561 -0.0029 -0.0189 -0.0423 2110 HOH B O 6786 O O . HOH N . ? 0.1538 0.1300 0.1064 0.0001 0.0027 0.0005 2111 HOH B O 6787 O O . HOH N . ? 0.2410 0.3112 0.2756 -0.0031 0.0458 -0.0008 2112 HOH B O 6788 O O . HOH N . ? 0.4102 0.3730 0.3498 0.0088 -0.0260 0.0175 2113 HOH B O 6789 O O . HOH N . ? 0.2131 0.2743 0.2227 -0.0433 -0.0058 0.0192 2114 HOH B O 6790 O O . HOH N . ? 0.3298 0.2228 0.1970 0.0037 0.0183 0.0012 2115 HOH B O 6791 O O . HOH N . ? 0.1547 0.1543 0.1348 -0.0054 0.0130 -0.0041 2116 HOH B O 6792 O O . HOH N . ? 0.4398 0.4534 0.3747 0.0194 0.0166 -0.0184 2117 HOH B O 6793 O O . HOH N . ? 0.4773 0.4676 0.5038 0.0074 0.0082 0.0172 2118 HOH B O 6794 O O . HOH N . ? 0.2302 0.2208 0.2130 -0.0396 0.0738 -0.0010 2119 HOH B O 6795 O O . HOH N . ? 0.2579 0.2593 0.2394 0.0323 -0.0296 -0.0224 2120 HOH B O 6796 O O . HOH N . ? 0.1991 0.1915 0.1893 -0.0205 0.0275 -0.0119 2121 HOH B O 6797 O O . HOH N . ? 0.3144 0.2919 0.3063 -0.0294 -0.0323 -0.0021 2122 HOH B O 6798 O O . HOH N . ? 0.3463 0.3478 0.3314 -0.0381 0.0595 -0.0255 2123 HOH B O 6799 O O . HOH N . ? 0.3030 0.2336 0.2357 -0.0261 -0.0216 -0.0473 2124 HOH B O 6800 O O . HOH N . ? 0.2481 0.2409 0.2779 0.0278 -0.0312 -0.0097 2125 HOH B O 6801 O O . HOH N . ? 0.1538 0.2157 0.1633 0.0031 -0.0119 0.0040 2126 HOH B O 6802 O O . HOH N . ? 0.3342 0.3571 0.3408 -0.0440 0.0084 0.0231 2127 HOH B O 6803 O O . HOH N . ? 0.3441 0.3243 0.3760 -0.0012 -0.0215 -0.0121 2128 HOH B O 6804 O O . HOH N . ? 0.3543 0.3054 0.3247 -0.0189 0.0169 0.0208 2129 HOH B O 6805 O O . HOH N . ? 0.3996 0.4405 0.4433 -0.0331 -0.0392 -0.0109 2130 HOH B O 6806 O O . HOH N . ? 0.1699 0.1610 0.1479 0.0192 0.0028 -0.0060 2131 HOH B O 6807 O O . HOH N . ? 0.1182 0.1614 0.1321 0.0020 -0.0135 0.0082 2132 HOH B O 6808 O O . HOH N . ? 0.2888 0.3041 0.2995 -0.0189 -0.0321 -0.0121 2133 HOH B O 6809 O O . HOH N . ? 0.2097 0.1894 0.2014 0.0152 -0.0268 -0.0175 2134 HOH B O 6810 O O . HOH N . ? 0.1414 0.2565 0.1635 -0.0230 -0.0179 0.0087 2135 HOH B O 6811 O O . HOH N . ? 0.3469 0.3418 0.3168 0.0326 -0.0012 -0.0051 2136 HOH B O 6812 O O . HOH N . ? 0.3104 0.3868 0.2759 -0.0252 -0.0556 -0.0164 2137 HOH B O 6813 O O . HOH N . ? 0.2228 0.2532 0.2219 -0.0076 0.0031 -0.0208 2138 HOH B O 6814 O O . HOH N . ? 0.3091 0.3738 0.3818 0.0321 -0.0292 0.0250 2139 HOH B O 6815 O O . HOH N . ? 0.2814 0.3015 0.2198 -0.0737 -0.0038 -0.0222 2140 HOH B O 6816 O O . HOH N . ? 0.3557 0.3250 0.3238 0.0255 -0.0197 0.0582 2141 HOH B O 6817 O O . HOH N . ? 0.1318 0.1425 0.1129 0.0081 0.0122 0.0042 2142 HOH B O 6818 O O . HOH N . ? 0.1411 0.1754 0.1210 0.0028 -0.0227 -0.0125 2143 HOH B O 6819 O O . HOH N . ? 0.1245 0.1522 0.1443 0.0056 -0.0013 0.0004 2144 HOH B O 6820 O O . HOH N . ? 0.1240 0.1419 0.1336 -0.0064 0.0044 0.0103 2145 HOH B O 6821 O O . HOH N . ? 0.3398 0.2632 0.2906 -0.0094 0.0237 0.0326 2146 HOH B O 6822 O O . HOH N . ? 0.2453 0.2965 0.2164 0.0013 0.0504 0.0323 2147 HOH B O 6823 O O . HOH N . ? 0.2227 0.2886 0.2104 0.0348 0.0301 0.0359 2148 HOH B O 6824 O O . HOH N . ? 0.1427 0.1345 0.1222 0.0113 -0.0102 -0.0008 2149 HOH B O 6825 O O . HOH N . ? 0.1245 0.1426 0.1290 -0.0114 0.0085 -0.0090 2150 HOH B O 6826 O O . HOH N . ? 0.2315 0.1875 0.3691 -0.0318 -0.0786 0.0265 2151 HOH B O 6827 O O . HOH N . ? 0.2607 0.3342 0.3945 -0.0351 -0.0478 -0.0006 2152 HOH B O 6828 O O . HOH N . ? 0.3196 0.2536 0.2080 0.0155 0.0251 -0.0189 2153 HOH B O 6829 O O . HOH N . ? 0.1540 0.1794 0.1690 0.0202 -0.0116 -0.0010 2154 HOH B O 6830 O O . HOH N . ? 0.1230 0.1666 0.1298 -0.0032 -0.0103 -0.0053 2155 HOH B O 6831 O O . HOH N . ? 0.3657 0.3482 0.3155 0.0386 -0.0582 -0.0286 2156 HOH B O 6832 O O . HOH N . ? 0.1837 0.2176 0.1869 0.0224 -0.0190 -0.0027 2157 HOH B O 6833 O O . HOH N . ? 0.2035 0.2732 0.2884 0.0053 -0.0032 -0.0081 2158 HOH B O 6834 O O . HOH N . ? 0.2871 0.2584 0.2922 0.0066 0.0299 0.0027 2159 HOH B O 6835 O O . HOH N . ? 0.3803 0.3620 0.3172 -0.0136 0.0013 0.0180 2160 HOH B O 6836 O O . HOH N . ? 0.1882 0.1744 0.1623 -0.0065 -0.0003 -0.0125 2161 HOH B O 6837 O O . HOH N . ? 0.1797 0.1714 0.1400 0.0266 -0.0199 0.0043 2162 HOH B O 6838 O O . HOH N . ? 0.3357 0.3691 0.2764 0.0289 -0.0210 0.0015 2163 HOH B O 6839 O O . HOH N . ? 0.2186 0.2426 0.2101 0.0441 -0.0300 0.0007 2164 HOH B O 6840 O O . HOH N . ? 0.1139 0.1396 0.1360 0.0135 0.0010 -0.0036 2165 HOH B O 6841 O O . HOH N . ? 0.1457 0.1436 0.1698 0.0128 -0.0011 -0.0032 2166 HOH B O 6842 O O . HOH N . ? 0.1442 0.1239 0.1264 0.0220 0.0146 0.0084 2167 HOH B O 6843 O O . HOH N . ? 0.1318 0.1351 0.1217 0.0106 0.0033 -0.0049 2168 HOH B O 6844 O O . HOH N . ? 0.3032 0.3323 0.3119 0.0186 -0.0021 0.0271 2169 HOH B O 6845 O O . HOH N . ? 0.2641 0.4123 0.2504 0.0692 0.0217 0.0421 2170 HOH B O 6846 O O . HOH N . ? 0.1850 0.2217 0.2408 0.0225 -0.0069 -0.0131 2171 HOH B O 6847 O O . HOH N . ? 0.3377 0.2588 0.3073 0.0150 -0.0095 0.0178 2172 HOH B O 6848 O O . HOH N . ? 0.2232 0.2696 0.2910 0.0145 0.0103 0.0213 2173 HOH B O 6849 O O . HOH N . ? 0.1943 0.2466 0.2018 -0.0097 -0.0210 0.0107 2174 HOH B O 6850 O O . HOH N . ? 0.2199 0.1995 0.2080 0.0377 -0.0881 -0.0406 2175 HOH B O 6851 O O . HOH N . ? 0.3022 0.2681 0.2468 -0.0331 -0.0223 -0.0090 2176 HOH B O 6852 O O . HOH N . ? 0.2452 0.2501 0.2562 -0.0231 -0.0425 0.0058 2177 HOH B O 6853 O O . HOH N . ? 0.2660 0.3862 0.3421 -0.0179 -0.0007 -0.0054 2178 HOH B O 6854 O O . HOH N . ? 0.3523 0.3753 0.3897 -0.0728 -0.0220 0.0122 2179 HOH B O 6855 O O . HOH N . ? 0.2138 0.2688 0.2336 -0.0011 -0.0560 -0.0172 2180 HOH B O 6856 O O . HOH N . ? 0.3343 0.3619 0.3011 -0.0032 0.0191 -0.0010 2181 HOH B O 6857 O O . HOH N . ? 0.2813 0.2360 0.2873 0.0017 0.0312 -0.0120 2182 HOH B O 6858 O O . HOH N . ? 0.1856 0.1354 0.1969 -0.0133 0.0063 0.0092 2183 HOH B O 6859 O O . HOH N . ? 0.3019 0.3604 0.2942 0.0469 0.0078 0.0062 2184 HOH B O 6860 O O . HOH N . ? 0.1437 0.1464 0.1643 -0.0105 0.0005 0.0019 2185 HOH B O 6861 O O . HOH N . ? 0.3183 0.3430 0.2856 -0.0250 -0.0284 -0.0356 2186 HOH B O 6862 O O . HOH N . ? 0.3918 0.3553 0.3084 -0.0008 -0.0013 0.0225 2187 HOH B O 6863 O O . HOH N . ? 0.1353 0.1419 0.1441 0.0011 -0.0005 0.0160 2188 HOH B O 6864 O O . HOH N . ? 0.1397 0.1866 0.1709 0.0124 0.0140 0.0223 2189 HOH B O 6865 O O . HOH N . ? 0.1383 0.1560 0.1449 0.0115 0.0121 0.0243 2190 HOH B O 6866 O O . HOH N . ? 0.3737 0.3327 0.4030 -0.0014 -0.0038 0.0148 2191 HOH B O 6867 O O . HOH N . ? 0.1535 0.1578 0.1716 0.0172 -0.0222 -0.0018 2192 HOH B O 6868 O O . HOH N . ? 0.2231 0.1495 0.2061 0.0004 0.0018 0.0400 2193 HOH B O 6869 O O . HOH N . ? 0.1418 0.1242 0.1296 0.0124 -0.0192 -0.0081 2194 HOH B O 6870 O O . HOH N . ? 0.2238 0.2507 0.2433 0.0286 -0.0171 0.0236 2195 HOH B O 6871 O O . HOH N . ? 0.1911 0.1766 0.1674 0.0056 -0.0120 0.0150 2196 HOH B O 6872 O O . HOH N . ? 0.2227 0.2934 0.2190 -0.0314 0.0185 0.0181 2197 HOH B O 6873 O O . HOH N . ? 0.2101 0.1680 0.2578 0.0251 0.0141 -0.0020 2198 HOH B O 6874 O O . HOH N . ? 0.2096 0.2557 0.2588 0.0324 -0.0325 -0.0050 2199 HOH B O 6875 O O . HOH N . ? 0.2585 0.2454 0.2487 0.0369 -0.0295 -0.0097 2200 HOH B O 6876 O O . HOH N . ? 0.3389 0.3910 0.4521 0.0171 -0.0224 0.0064 2201 HOH B O 6877 O O . HOH N . ? 0.2204 0.2576 0.2687 0.0208 -0.0070 0.0217 2202 HOH B O 6878 O O . HOH N . ? 0.1545 0.1675 0.1687 -0.0044 -0.0126 -0.0199 2203 HOH B O 6879 O O . HOH N . ? 0.3635 0.3255 0.3692 -0.0051 -0.0223 -0.0043 2204 HOH B O 6880 O O . HOH N . ? 0.3770 0.4148 0.3509 0.0206 -0.0756 -0.0011 2205 HOH B O 6881 O O . HOH N . ? 0.1566 0.1981 0.1867 0.0017 0.0132 0.0254 2206 HOH B O 6882 O O . HOH N . ? 0.3363 0.4009 0.4148 0.0041 -0.0224 -0.0312 2207 HOH B O 6883 O O . HOH N . ? 0.5822 0.6220 0.6325 -0.0066 0.0091 0.0026 2208 HOH B O 6884 O O . HOH N . ? 0.5783 0.5876 0.5874 0.0006 -0.0092 -0.0047 2209 HOH B O 6885 O O . HOH N . ? 0.2561 0.3322 0.3379 -0.0221 0.0219 0.0277 2210 HOH B O 6886 O O . HOH N . ? 0.2590 0.3793 0.3683 0.0493 0.0322 0.0256 2211 HOH B O 6887 O O . HOH N . ? 0.2288 0.3330 0.3065 0.0437 -0.0135 -0.0026 2212 HOH B O 6888 O O . HOH N . ? 0.3216 0.4179 0.3584 0.0121 0.0032 -0.0127 2213 HOH B O 6889 O O . HOH N . ? 0.1298 0.1807 0.1580 0.0098 -0.0055 -0.0009 2214 HOH B O 6890 O O . HOH N . ? 0.3276 0.3155 0.2394 -0.0011 -0.0162 -0.0097 2215 HOH B O 6891 O O . HOH N . ? 0.3013 0.3008 0.3494 -0.0003 0.0197 -0.0296 2216 HOH B O 6892 O O . HOH N . ? 0.3409 0.3689 0.2942 -0.0662 -0.0184 0.0294 2217 HOH B O 6893 O O . HOH N . ? 0.1355 0.1162 0.1462 0.0129 0.0146 -0.0125 2218 HOH B O 6894 O O . HOH N . ? 0.2936 0.3113 0.3255 0.0405 0.0289 -0.0292 2219 HOH B O 6895 O O . HOH N . ? 0.3464 0.2835 0.2432 -0.0157 0.0794 -0.0176 2220 HOH B O 6896 O O . HOH N . ? 0.2984 0.2351 0.3768 0.0015 0.0262 -0.0192 2221 HOH B O 6897 O O . HOH N . ? 0.1600 0.1464 0.1678 0.0007 -0.0142 -0.0178 2222 HOH B O 6898 O O . HOH N . ? 0.2307 0.1858 0.1708 -0.0165 -0.0206 -0.0099 2223 HOH B O 6899 O O . HOH N . ? 0.1639 0.1503 0.1456 0.0156 0.0199 0.0128 2224 HOH B O 6900 O O . HOH N . ? 0.4743 0.5214 0.5389 0.0331 0.0018 -0.0159 2225 HOH B O 6901 O O . HOH N . ? 0.2019 0.2878 0.3521 0.0601 -0.0192 -0.0082 2226 HOH B O 6902 O O . HOH N . ? 0.1805 0.2828 0.2739 0.0357 0.0045 0.0064 2227 HOH B O 6903 O O . HOH N . ? 0.1685 0.1779 0.1674 0.0101 0.0021 -0.0079 2228 HOH B O 6904 O O . HOH N . ? 0.1450 0.1379 0.1544 0.0184 0.0089 -0.0199 2229 HOH B O 6905 O O . HOH N . ? 0.1872 0.1912 0.2075 0.0205 -0.0007 0.0081 2230 HOH B O 6906 O O . HOH N . ? 0.2282 0.2799 0.3208 0.0567 -0.0154 -0.0241 2231 HOH B O 6907 O O . HOH N . ? 0.2220 0.2339 0.2753 0.0144 0.0039 -0.0066 2232 HOH B O 6908 O O . HOH N . ? 0.4116 0.3163 0.3279 0.0189 0.0192 -0.0075 2233 HOH B O 6909 O O . HOH N . ? 0.3243 0.3122 0.3056 0.0719 -0.0003 -0.0120 2234 HOH B O 6910 O O . HOH N . ? 0.2520 0.2370 0.2333 -0.0280 -0.0022 0.0087 2235 HOH B O 6911 O O . HOH N . ? 0.3092 0.2777 0.3026 -0.0026 0.0077 0.0109 2236 HOH B O 6912 O O . HOH N . ? 0.1867 0.1615 0.1591 0.0313 -0.0173 -0.0195 2237 HOH B O 6913 O O . HOH N . ? 0.3651 0.3328 0.3585 0.0239 -0.0156 -0.0097 2238 HOH B O 6914 O O . HOH N . ? 0.2523 0.1452 0.1562 0.0313 -0.0003 0.0214 2239 HOH B O 6915 O O . HOH N . ? 0.2497 0.2881 0.2706 0.0029 -0.0230 0.0151 2240 HOH B O 6916 O O . HOH N . ? 0.2048 0.1629 0.1725 0.0036 -0.0186 -0.0113 2241 HOH B O 6917 O O . HOH N . ? 0.2733 0.2595 0.2092 0.0188 0.0081 -0.0358 2242 HOH B O 6918 O O . HOH N . ? 0.2824 0.2016 0.2699 0.0045 0.0143 -0.0110 2243 HOH B O 6919 O O . HOH N . ? 0.3028 0.3143 0.3097 0.0145 -0.0040 0.0014 2244 HOH B O 6920 O O . HOH N . ? 0.3095 0.2689 0.2990 0.0008 -0.0093 0.0106 2245 HOH B O 6921 O O . HOH N . ? 0.2801 0.2903 0.2515 0.0341 -0.0140 0.0376 2246 HOH B O 6922 O O . HOH N . ? 0.1834 0.1665 0.1441 -0.0037 -0.0058 0.0237 2247 HOH B O 6923 O O . HOH N . ? 0.4404 0.4707 0.4450 -0.0160 -0.0148 -0.0025 2248 HOH B O 6924 O O . HOH N . ? 0.2875 0.2338 0.3226 0.0160 -0.0523 0.0252 2249 HOH B O 6925 O O . HOH N . ? 0.2139 0.2123 0.2443 -0.0284 -0.0131 0.0119 2250 HOH B O 6926 O O . HOH N . ? 0.2016 0.2190 0.1702 -0.0084 -0.0022 0.0128 2251 HOH B O 6927 O O . HOH N . ? 0.3003 0.3068 0.3595 -0.0187 0.0123 0.0201 2252 HOH B O 6928 O O . HOH N . ? 0.4343 0.4077 0.4436 0.0116 -0.0174 0.0223 2253 HOH B O 6929 O O . HOH N . ? 0.3676 0.4182 0.3266 -0.0011 0.0025 -0.0334 2254 HOH B O 6930 O O . HOH N . ? 0.2203 0.1748 0.1627 -0.0163 0.0061 0.0043 2255 HOH B O 6931 O O . HOH N . ? 0.3639 0.2896 0.3195 0.0291 -0.0261 -0.0086 2256 HOH B O 6932 O O . HOH N . ? 0.4246 0.3791 0.3395 -0.0003 -0.0413 -0.0034 2257 HOH B O 6933 O O . HOH N . ? 0.1746 0.1730 0.1413 0.0078 -0.0148 -0.0126 2258 HOH B O 6934 O O . HOH N . ? 0.3626 0.3619 0.3316 0.0172 0.0087 0.0284 2259 HOH B O 6935 O O . HOH N . ? 0.2766 0.3379 0.3175 -0.0276 -0.0265 0.0069 2260 HOH B O 6936 O O . HOH N . ? 0.2520 0.3303 0.2623 0.0487 -0.0121 -0.0427 2261 HOH B O 6937 O O . HOH N . ? 0.3669 0.3701 0.4142 -0.0138 -0.0006 0.0109 2262 HOH B O 6938 O O . HOH N . ? 0.2118 0.2818 0.1794 -0.0309 0.0289 0.0124 2263 HOH B O 6939 O O . HOH N . ? 0.2350 0.2913 0.2583 0.0369 -0.0253 0.0150 2264 HOH B O 6940 O O . HOH N . ? 0.3219 0.3417 0.3303 0.0016 0.0305 -0.0117 2265 HOH B O 6941 O O . HOH N . ? 0.2787 0.2937 0.1684 0.0253 0.0341 0.0133 2266 HOH B O 6942 O O . HOH N . ? 0.2022 0.2847 0.1919 0.0417 0.0202 -0.0241 2267 HOH B O 6943 O O . HOH N . ? 0.3751 0.2717 0.3206 0.0023 0.0382 0.0038 2268 HOH B O 6944 O O . HOH N . ? 0.1910 0.1500 0.1601 0.0132 -0.0085 0.0097 2269 HOH B O 6945 O O . HOH N . ? 0.2710 0.3617 0.2793 -0.0182 -0.0062 0.0462 2270 HOH B O 6946 O O . HOH N . ? 0.1394 0.1280 0.1605 0.0145 -0.0088 0.0097 2271 HOH B O 6947 O O . HOH N . ? 0.2001 0.2470 0.1248 0.0280 0.0069 -0.0155 2272 HOH B O 6948 O O . HOH N . ? 0.2176 0.2071 0.2611 -0.0128 0.0246 0.0000 2273 HOH B O 6949 O O . HOH N . ? 0.3383 0.3174 0.3309 -0.0301 0.0057 0.0194 2274 HOH B O 6950 O O . HOH N . ? 0.3838 0.2330 0.2648 0.0050 -0.0481 -0.0059 2275 HOH B O 6951 O O . HOH N . ? 0.2805 0.2683 0.2732 0.0161 -0.0099 0.0584 2276 HOH B O 6952 O O . HOH N . ? 0.2992 0.2032 0.3222 0.0446 0.0241 0.0109 2277 HOH B O 6953 O O . HOH N . ? 0.2116 0.1953 0.1686 0.0117 -0.0050 -0.0210 2278 HOH B O 6954 O O . HOH N . ? 0.1463 0.1786 0.1488 0.0115 -0.0058 0.0139 2279 HOH B O 6955 O O . HOH N . ? 0.2967 0.2409 0.2582 0.0099 -0.0196 0.0215 2280 HOH B O 6956 O O . HOH N . ? 0.3493 0.2691 0.1924 0.0280 0.0313 -0.0019 2281 HOH B O 6957 O O . HOH N . ? 0.2641 0.3847 0.2318 -0.0008 -0.0236 0.0238 2282 HOH B O 6958 O O . HOH N . ? 0.4131 0.4111 0.3826 0.0302 0.0001 -0.0521 2283 HOH B O 6959 O O . HOH N . ? 0.2047 0.1871 0.1518 0.0141 0.0173 -0.0270 2284 HOH B O 6960 O O . HOH N . ? 0.2583 0.3964 0.2437 0.0301 -0.0093 0.0258 2285 HOH B O 6961 O O . HOH N . ? 0.2915 0.3170 0.3131 0.0625 0.0071 -0.0605 2286 HOH B O 6962 O O . HOH N . ? 0.2228 0.3070 0.2671 -0.0197 -0.0376 0.0048 2287 HOH B O 6963 O O . HOH N . ? 0.3138 0.4749 0.2748 0.0020 -0.0182 0.0329 2288 HOH B O 6964 O O . HOH N . ? 0.3103 0.2498 0.2422 0.0407 0.0149 -0.0214 2289 HOH B O 6965 O O . HOH N . ? 0.2720 0.3528 0.2656 -0.0195 0.0119 -0.0039 2290 HOH B O 6966 O O . HOH N . ? 0.4856 0.5166 0.5374 -0.0124 0.0002 -0.0066 2291 HOH B O 6967 O O . HOH N . ? 0.2592 0.2314 0.2667 -0.0161 0.0102 -0.0509 2292 HOH B O 6968 O O . HOH N . ? 0.2655 0.3380 0.1894 0.0522 -0.0113 -0.0737 2293 HOH B O 6969 O O . HOH N . ? 0.3891 0.3005 0.2582 -0.0547 0.0070 -0.0364 2294 HOH B O 6970 O O . HOH N . ? 0.3074 0.2654 0.1838 0.0122 -0.0157 -0.0022 2295 HOH B O 6971 O O . HOH N . ? 0.1402 0.1872 0.1274 0.0237 0.0015 0.0003 2296 HOH B O 6972 O O . HOH N . ? 0.2365 0.1738 0.2704 -0.0349 0.0299 0.0125 2297 HOH B O 6973 O O . HOH N . ? 0.2153 0.1773 0.1702 0.0166 -0.0017 -0.0131 2298 HOH B O 6974 O O . HOH N . ? 0.1493 0.1945 0.1623 -0.0079 0.0004 0.0179 2299 HOH B O 6975 O O . HOH N . ? 0.2260 0.2718 0.2560 -0.0327 0.0366 0.0549 2300 HOH B O 6976 O O . HOH N . ? 0.3920 0.3575 0.3733 -0.0201 0.0170 0.0135 2301 HOH B O 6977 O O . HOH N . ? 0.2707 0.2261 0.2048 0.0361 -0.0189 0.0062 2302 HOH B O 6978 O O . HOH N . ? 0.3652 0.2573 0.2775 0.0192 0.0360 -0.0347 2303 HOH B O 6979 O O . HOH N . ? 0.2725 0.2743 0.1959 -0.0067 0.0747 -0.0060 2304 HOH B O 6980 O O . HOH N . ? 0.2028 0.1572 0.2042 0.0014 -0.0156 -0.0093 2305 HOH B O 6981 O O . HOH N . ? 0.1425 0.1103 0.1640 -0.0011 0.0100 -0.0037 2306 HOH B O 6982 O O . HOH N . ? 0.2007 0.1888 0.2238 0.0280 -0.0022 -0.0233 2307 HOH B O 6983 O O . HOH N . ? 0.1555 0.1833 0.1340 0.0103 -0.0127 -0.0107 2308 HOH B O 6984 O O . HOH N . ? 0.3056 0.3083 0.3334 -0.0004 -0.0111 0.0276 2309 HOH B O # 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 PCA 1 1 1 PCA PCA A . n A 1 2 LYS 2 2 2 LYS LYS A . n A 1 3 PRO 3 3 3 PRO PRO A . n A 1 4 GLY 4 4 4 GLY GLY A . n A 1 5 GLU 5 5 5 GLU GLU A . n A 1 6 THR 6 6 6 THR THR A . n A 1 7 LYS 7 7 7 LYS LYS A . n A 1 8 GLU 8 8 8 GLU GLU A . n A 1 9 VAL 9 9 9 VAL VAL A . n A 1 10 HIS 10 10 10 HIS HIS A . n A 1 11 PRO 11 11 11 PRO PRO A . n A 1 12 GLN 12 12 12 GLN GLN A . n A 1 13 LEU 13 13 13 LEU LEU A . n A 1 14 THR 14 14 14 THR THR A . n A 1 15 THR 15 15 15 THR THR A . n A 1 16 PHE 16 16 16 PHE PHE A . n A 1 17 ARG 17 17 17 ARG ARG A . n A 1 18 CYS 18 18 18 CYS CYS A . n A 1 19 THR 19 19 19 THR THR A . n A 1 20 LYS 20 20 20 LYS LYS A . n A 1 21 ARG 21 21 21 ARG ARG A . n A 1 22 GLY 22 22 22 GLY GLY A . n A 1 23 GLY 23 23 23 GLY GLY A . n A 1 24 CYS 24 24 24 CYS CYS A . n A 1 25 LYS 25 25 25 LYS LYS A . n A 1 26 PRO 26 26 26 PRO PRO A . n A 1 27 ALA 27 27 27 ALA ALA A . n A 1 28 THR 28 28 28 THR THR A . n A 1 29 ASN 29 29 29 ASN ASN A . n A 1 30 PHE 30 30 30 PHE PHE A . n A 1 31 ILE 31 31 31 ILE ILE A . n A 1 32 VAL 32 32 32 VAL VAL A . n A 1 33 LEU 33 33 33 LEU LEU A . n A 1 34 ASP 34 34 34 ASP ASP A . n A 1 35 SER 35 35 35 SER SER A . n A 1 36 LEU 36 36 36 LEU LEU A . n A 1 37 SER 37 37 37 SER SER A . n A 1 38 HIS 38 38 38 HIS HIS A . n A 1 39 PRO 39 39 39 PRO PRO A . n A 1 40 ILE 40 40 40 ILE ILE A . n A 1 41 HIS 41 41 41 HIS HIS A . n A 1 42 ARG 42 42 42 ARG ARG A . n A 1 43 ALA 43 43 43 ALA ALA A . n A 1 44 GLU 44 44 44 GLU GLU A . n A 1 45 GLY 45 45 45 GLY GLY A . n A 1 46 LEU 46 46 46 LEU LEU A . n A 1 47 GLY 47 47 47 GLY GLY A . n A 1 48 PRO 48 48 48 PRO PRO A . n A 1 49 GLY 49 49 49 GLY GLY A . n A 1 50 GLY 50 50 50 GLY GLY A . n A 1 51 CYS 51 51 51 CYS CYS A . n A 1 52 GLY 52 52 52 GLY GLY A . n A 1 53 ASP 53 53 53 ASP ASP A . n A 1 54 TRP 54 54 54 TRP TRP A . n A 1 55 GLY 55 55 55 GLY GLY A . n A 1 56 ASN 56 56 56 ASN ASN A . n A 1 57 PRO 57 57 57 PRO PRO A . n A 1 58 PRO 58 58 58 PRO PRO A . n A 1 59 PRO 59 59 59 PRO PRO A . n A 1 60 LYS 60 60 60 LYS LYS A . n A 1 61 ASP 61 61 61 ASP ASP A . n A 1 62 VAL 62 62 62 VAL VAL A . n A 1 63 CYS 63 63 63 CYS CYS A . n A 1 64 PRO 64 64 64 PRO PRO A . n A 1 65 ASP 65 65 65 ASP ASP A . n A 1 66 VAL 66 66 66 VAL VAL A . n A 1 67 GLU 67 67 67 GLU GLU A . n A 1 68 SER 68 68 68 SER SER A . n A 1 69 CYS 69 69 69 CYS CYS A . n A 1 70 ALA 70 70 70 ALA ALA A . n A 1 71 LYS 71 71 71 LYS LYS A . n A 1 72 ASN 72 72 72 ASN ASN A . n A 1 73 CYS 73 73 73 CYS CYS A . n A 1 74 ILE 74 74 74 ILE ILE A . n A 1 75 MET 75 75 75 MET MET A . n A 1 76 GLU 76 76 76 GLU GLU A . n A 1 77 GLY 77 77 77 GLY GLY A . n A 1 78 ILE 78 78 78 ILE ILE A . n A 1 79 PRO 79 79 79 PRO PRO A . n A 1 80 ASP 80 80 80 ASP ASP A . n A 1 81 TYR 81 81 81 TYR TYR A . n A 1 82 SER 82 82 82 SER SER A . n A 1 83 GLN 83 83 83 GLN GLN A . n A 1 84 TYR 84 84 84 TYR TYR A . n A 1 85 GLY 85 85 85 GLY GLY A . n A 1 86 VAL 86 86 86 VAL VAL A . n A 1 87 THR 87 87 87 THR THR A . n A 1 88 THR 88 88 88 THR THR A . n A 1 89 ASN 89 89 89 ASN ASN A . n A 1 90 GLY 90 90 90 GLY GLY A . n A 1 91 THR 91 91 91 THR THR A . n A 1 92 SER 92 92 92 SER SER A . n A 1 93 LEU 93 93 93 LEU LEU A . n A 1 94 ARG 94 94 94 ARG ARG A . n A 1 95 LEU 95 95 95 LEU LEU A . n A 1 96 GLN 96 96 96 GLN GLN A . n A 1 97 HIS 97 97 97 HIS HIS A . n A 1 98 ILE 98 98 98 ILE ILE A . n A 1 99 LEU 99 99 99 LEU LEU A . n A 1 100 PRO 100 100 100 PRO PRO A . n A 1 101 ASP 101 101 101 ASP ASP A . n A 1 102 GLY 102 102 102 GLY GLY A . n A 1 103 ARG 103 103 103 ARG ARG A . n A 1 104 VAL 104 104 104 VAL VAL A . n A 1 105 PRO 105 105 105 PRO PRO A . n A 1 106 SER 106 106 106 SER SER A . n A 1 107 PRO 107 107 107 PRO PRO A . n A 1 108 ARG 108 108 108 ARG ARG A . n A 1 109 VAL 109 109 109 VAL VAL A . n A 1 110 TYR 110 110 110 TYR TYR A . n A 1 111 LEU 111 111 111 LEU LEU A . n A 1 112 LEU 112 112 112 LEU LEU A . n A 1 113 ASP 113 113 113 ASP ASP A . n A 1 114 LYS 114 114 114 LYS LYS A . n A 1 115 THR 115 115 115 THR THR A . n A 1 116 LYS 116 116 116 LYS LYS A . n A 1 117 ARG 117 117 117 ARG ARG A . n A 1 118 ARG 118 118 118 ARG ARG A . n A 1 119 TYR 119 119 119 TYR TYR A . n A 1 120 GLU 120 120 120 GLU GLU A . n A 1 121 MET 121 121 121 MET MET A . n A 1 122 LEU 122 122 122 LEU LEU A . n A 1 123 HIS 123 123 123 HIS HIS A . n A 1 124 LEU 124 124 124 LEU LEU A . n A 1 125 THR 125 125 125 THR THR A . n A 1 126 GLY 126 126 126 GLY GLY A . n A 1 127 PHE 127 127 127 PHE PHE A . n A 1 128 GLU 128 128 128 GLU GLU A . n A 1 129 PHE 129 129 129 PHE PHE A . n A 1 130 THR 130 130 130 THR THR A . n A 1 131 PHE 131 131 131 PHE PHE A . n A 1 132 ASP 132 132 132 ASP ASP A . n A 1 133 VAL 133 133 133 VAL VAL A . n A 1 134 ASP 134 134 134 ASP ASP A . n A 1 135 ALA 135 135 135 ALA ALA A . n A 1 136 THR 136 136 136 THR THR A . n A 1 137 LYS 137 137 137 LYS LYS A . n A 1 138 LEU 138 138 138 LEU LEU A . n A 1 139 PRO 139 139 139 PRO PRO A . n A 1 140 CYS 140 140 140 CYS CYS A . n A 1 141 GLY 141 141 141 GLY GLY A . n A 1 142 MET 142 142 142 MET MET A . n A 1 143 ASN 143 143 143 ASN ASN A . n A 1 144 SER 144 144 144 SER SER A . n A 1 145 ALA 145 145 145 ALA ALA A . n A 1 146 LEU 146 146 146 LEU LEU A . n A 1 147 TYR 147 147 147 TYR TYR A . n A 1 148 LEU 148 148 148 LEU LEU A . n A 1 149 SER 149 149 149 SER SER A . n A 1 150 GLU 150 150 150 GLU GLU A . n A 1 151 MET 151 151 151 MET MET A . n A 1 152 HIS 152 152 152 HIS HIS A . n A 1 153 PRO 153 153 153 PRO PRO A . n A 1 154 THR 154 154 154 THR THR A . n A 1 155 GLY 155 155 155 GLY GLY A . n A 1 156 ALA 156 156 156 ALA ALA A . n A 1 157 LYS 157 157 157 LYS LYS A . n A 1 158 SER 158 158 158 SER SER A . n A 1 159 LYS 159 159 159 LYS LYS A . n A 1 160 TYR 160 160 160 TYR TYR A . n A 1 161 ASN 161 161 161 ASN ASN A . n A 1 162 PRO 162 162 162 PRO PRO A . n A 1 163 GLY 163 163 163 GLY GLY A . n A 1 164 GLY 164 164 164 GLY GLY A . n A 1 165 ALA 165 165 165 ALA ALA A . n A 1 166 TYR 166 166 166 TYR TYR A . n A 1 167 TYR 167 167 167 TYR TYR A . n A 1 168 GLY 168 168 168 GLY GLY A . n A 1 169 THR 169 169 169 THR THR A . n A 1 170 GLY 170 170 170 GLY GLY A . n A 1 171 TYR 171 171 171 TYR TYR A . n A 1 172 CYS 172 172 172 CYS CYS A . n A 1 173 ASP 173 173 173 ASP ASP A . n A 1 174 ALA 174 174 174 ALA ALA A . n A 1 175 GLN 175 175 175 GLN GLN A . n A 1 176 CYS 176 176 176 CYS CYS A . n A 1 177 PHE 177 177 177 PHE PHE A . n A 1 178 VAL 178 178 178 VAL VAL A . n A 1 179 THR 179 179 179 THR THR A . n A 1 180 PRO 180 180 180 PRO PRO A . n A 1 181 PHE 181 181 181 PHE PHE A . n A 1 182 ILE 182 182 182 ILE ILE A . n A 1 183 ASN 183 183 183 ASN ASN A . n A 1 184 GLY 184 184 184 GLY GLY A . n A 1 185 LEU 185 185 185 LEU LEU A . n A 1 186 GLY 186 186 186 GLY GLY A . n A 1 187 ASN 187 187 187 ASN ASN A . n A 1 188 ILE 188 188 188 ILE ILE A . n A 1 189 GLU 189 189 189 GLU GLU A . n A 1 190 GLY 190 190 190 GLY GLY A . n A 1 191 LYS 191 191 191 LYS LYS A . n A 1 192 GLY 192 192 192 GLY GLY A . n A 1 193 SER 193 193 193 SER SER A . n A 1 194 CYS 194 194 194 CYS CYS A . n A 1 195 CYS 195 195 195 CYS CYS A . n A 1 196 ASN 196 196 196 ASN ASN A . n A 1 197 SER 197 197 197 SER SER A . n A 1 198 MET 198 198 198 MET MET A . n A 1 199 ASP 199 199 199 ASP ASP A . n A 1 200 ILE 200 200 200 ILE ILE A . n A 1 201 TRP 201 201 201 TRP TRP A . n A 1 202 GLU 202 202 202 GLU GLU A . n A 1 203 ALA 203 203 203 ALA ALA A . n A 1 204 ASN 204 204 204 ASN ASN A . n A 1 205 SER 205 205 205 SER SER A . n A 1 206 ARG 206 206 206 ARG ARG A . n A 1 207 ALA 207 207 207 ALA ALA A . n A 1 208 SER 208 208 208 SER SER A . n A 1 209 HIS 209 209 209 HIS HIS A . n A 1 210 VAL 210 210 210 VAL VAL A . n A 1 211 ALA 211 211 211 ALA ALA A . n A 1 212 PRO 212 212 212 PRO PRO A . n A 1 213 HIS 213 213 213 HIS HIS A . n A 1 214 THR 214 214 214 THR THR A . n A 1 215 CYS 215 215 215 CYS CYS 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 LYS 218 218 218 LYS LYS A . n A 1 219 GLY 219 219 219 GLY GLY A . n A 1 220 LEU 220 220 220 LEU LEU A . n A 1 221 TYR 221 221 221 TYR TYR A . n A 1 222 LEU 222 222 222 LEU LEU A . n A 1 223 CYS 223 223 223 CYS CYS A . n A 1 224 GLU 224 224 224 GLU GLU A . n A 1 225 GLY 225 225 225 GLY GLY A . n A 1 226 GLU 226 226 226 GLU GLU 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 ALA 229 229 229 ALA ALA A . n A 1 230 PHE 230 230 230 PHE PHE A . n A 1 231 GLU 231 231 231 GLU GLU A . n A 1 232 GLY 232 232 232 GLY GLY A . n A 1 233 VAL 233 233 233 VAL VAL A . n A 1 234 CYS 234 234 234 CYS CYS A . n A 1 235 ASP 235 235 235 ASP ASP A . n A 1 236 LYS 236 236 236 LYS LYS A . n A 1 237 ASN 237 237 237 ASN ASN A . n A 1 238 GLY 238 238 238 GLY GLY A . n A 1 239 CYS 239 239 239 CYS CYS A . n A 1 240 GLY 240 240 240 GLY GLY A . n A 1 241 TRP 241 241 241 TRP TRP A . n A 1 242 ASN 242 242 242 ASN ASN A . n A 1 243 ASN 243 243 243 ASN ASN A . n A 1 244 TYR 244 244 244 TYR TYR A . n A 1 245 ARG 245 245 245 ARG ARG A . n A 1 246 VAL 246 246 246 VAL VAL A . n A 1 247 ASN 247 247 247 ASN ASN A . n A 1 248 VAL 248 248 248 VAL VAL A . n A 1 249 THR 249 249 249 THR THR A . n A 1 250 ASP 250 250 250 ASP ASP A . n A 1 251 TYR 251 251 251 TYR TYR A . n A 1 252 TYR 252 252 252 TYR TYR A . n A 1 253 GLY 253 253 253 GLY GLY A . n A 1 254 ARG 254 254 254 ARG ARG A . n A 1 255 GLY 255 255 255 GLY GLY A . n A 1 256 GLU 256 256 256 GLU GLU A . n A 1 257 GLU 257 257 257 GLU GLU A . n A 1 258 PHE 258 258 258 PHE PHE A . n A 1 259 LYS 259 259 259 LYS LYS A . n A 1 260 VAL 260 260 260 VAL VAL A . n A 1 261 ASN 261 261 261 ASN ASN A . n A 1 262 THR 262 262 262 THR THR A . n A 1 263 LEU 263 263 263 LEU LEU A . n A 1 264 LYS 264 264 264 LYS LYS A . n A 1 265 PRO 265 265 265 PRO PRO A . n A 1 266 PHE 266 266 266 PHE PHE A . n A 1 267 THR 267 267 267 THR THR A . n A 1 268 VAL 268 268 268 VAL VAL A . n A 1 269 VAL 269 269 269 VAL VAL A . n A 1 270 THR 270 270 270 THR THR A . n A 1 271 GLN 271 271 271 GLN GLN A . n A 1 272 PHE 272 272 272 PHE PHE A . n A 1 273 LEU 273 273 273 LEU LEU A . n A 1 274 ALA 274 274 274 ALA ALA A . n A 1 275 ASN 275 275 275 ASN ASN A . n A 1 276 ARG 276 276 276 ARG ARG A . n A 1 277 ARG 277 277 277 ARG ARG A . n A 1 278 GLY 278 278 278 GLY GLY A . n A 1 279 LYS 279 279 279 LYS LYS A . n A 1 280 LEU 280 280 280 LEU LEU A . n A 1 281 GLU 281 281 281 GLU GLU A . n A 1 282 LYS 282 282 282 LYS LYS A . n A 1 283 ILE 283 283 283 ILE ILE A . n A 1 284 HIS 284 284 284 HIS HIS A . n A 1 285 ARG 285 285 285 ARG ARG A . n A 1 286 PHE 286 286 286 PHE PHE A . n A 1 287 TYR 287 287 287 TYR TYR A . n A 1 288 VAL 288 288 288 VAL VAL A . n A 1 289 GLN 289 289 289 GLN GLN A . n A 1 290 ASP 290 290 290 ASP ASP A . n A 1 291 GLY 291 291 291 GLY GLY A . n A 1 292 LYS 292 292 292 LYS LYS A . n A 1 293 VAL 293 293 293 VAL VAL A . n A 1 294 ILE 294 294 294 ILE ILE A . n A 1 295 GLU 295 295 295 GLU GLU A . n A 1 296 SER 296 296 296 SER SER A . n A 1 297 PHE 297 297 297 PHE PHE A . n A 1 298 TYR 298 298 298 TYR TYR A . n A 1 299 THR 299 299 299 THR THR A . n A 1 300 ASN 300 300 300 ASN ASN A . n A 1 301 LYS 301 301 301 LYS LYS A . n A 1 302 GLU 302 302 302 GLU GLU A . n A 1 303 GLY 303 303 303 GLY GLY A . n A 1 304 VAL 304 304 304 VAL VAL A . n A 1 305 PRO 305 305 305 PRO PRO A . n A 1 306 TYR 306 306 306 TYR TYR A . n A 1 307 THR 307 307 307 THR THR A . n A 1 308 ASN 308 308 308 ASN ASN A . n A 1 309 MET 309 309 309 MET MET A . n A 1 310 ILE 310 310 310 ILE ILE A . n A 1 311 ASP 311 311 311 ASP ASP A . n A 1 312 ASP 312 312 312 ASP ASP A . n A 1 313 GLU 313 313 313 GLU GLU A . n A 1 314 PHE 314 314 314 PHE PHE A . n A 1 315 CYS 315 315 315 CYS CYS A . n A 1 316 GLU 316 316 316 GLU GLU A . n A 1 317 ALA 317 317 317 ALA ALA A . n A 1 318 THR 318 318 318 THR THR A . n A 1 319 GLY 319 319 319 GLY GLY A . n A 1 320 SER 320 320 320 SER SER A . n A 1 321 ARG 321 321 321 ARG ARG A . n A 1 322 LYS 322 322 322 LYS LYS A . n A 1 323 TYR 323 323 323 TYR TYR A . n A 1 324 MET 324 324 324 MET MET A . n A 1 325 GLU 325 325 325 GLU GLU A . n A 1 326 LEU 326 326 326 LEU LEU A . n A 1 327 GLY 327 327 327 GLY GLY A . n A 1 328 ALA 328 328 328 ALA ALA A . n A 1 329 THR 329 329 329 THR THR A . n A 1 330 GLN 330 330 330 GLN GLN A . n A 1 331 GLY 331 331 331 GLY GLY A . n A 1 332 MET 332 332 332 MET MET A . n A 1 333 GLY 333 333 333 GLY GLY A . n A 1 334 GLU 334 334 334 GLU GLU A . n A 1 335 ALA 335 335 335 ALA ALA A . n A 1 336 LEU 336 336 336 LEU LEU A . n A 1 337 THR 337 337 337 THR THR A . n A 1 338 ARG 338 338 338 ARG ARG A . n A 1 339 GLY 339 339 339 GLY GLY A . n A 1 340 MET 340 340 340 MET MET A . n A 1 341 VAL 341 341 341 VAL VAL A . n A 1 342 LEU 342 342 342 LEU LEU A . n A 1 343 ALA 343 343 343 ALA ALA A . n A 1 344 MET 344 344 344 MET MET A . n A 1 345 SER 345 345 345 SER SER A . n A 1 346 ILE 346 346 346 ILE ILE A . n A 1 347 TRP 347 347 347 TRP TRP A . n A 1 348 TRP 348 348 348 TRP TRP A . n A 1 349 ASP 349 349 349 ASP ASP A . n A 1 350 GLN 350 350 350 GLN GLN A . n A 1 351 GLY 351 351 351 GLY GLY A . n A 1 352 GLY 352 352 352 GLY GLY A . n A 1 353 ASN 353 353 353 ASN ASN A . n A 1 354 MET 354 354 354 MET MET A . n A 1 355 GLU 355 355 355 GLU GLU A . n A 1 356 TRP 356 356 356 TRP TRP A . n A 1 357 LEU 357 357 357 LEU LEU A . n A 1 358 ASP 358 358 358 ASP ASP A . n A 1 359 HIS 359 359 359 HIS HIS A . n A 1 360 GLY 360 360 360 GLY GLY A . n A 1 361 GLU 361 361 361 GLU GLU A . n A 1 362 ALA 362 362 362 ALA ALA A . n A 1 363 GLY 363 363 363 GLY GLY A . n A 1 364 PRO 364 364 364 PRO PRO A . n A 1 365 CYS 365 365 365 CYS CYS A . n A 1 366 ALA 366 366 366 ALA ALA A . n A 1 367 LYS 367 367 367 LYS LYS A . n A 1 368 GLY 368 368 368 GLY GLY A . n A 1 369 GLU 369 369 369 GLU GLU A . n A 1 370 GLY 370 370 370 GLY GLY A . n A 1 371 ALA 371 371 371 ALA ALA A . n A 1 372 PRO 372 372 372 PRO PRO A . n A 1 373 SER 373 373 373 SER SER A . n A 1 374 ASN 374 374 374 ASN ASN A . n A 1 375 ILE 375 375 375 ILE ILE A . n A 1 376 VAL 376 376 376 VAL VAL A . n A 1 377 GLN 377 377 377 GLN GLN A . n A 1 378 VAL 378 378 378 VAL VAL A . n A 1 379 GLU 379 379 379 GLU GLU A . n A 1 380 PRO 380 380 380 PRO PRO A . n A 1 381 PHE 381 381 381 PHE PHE A . n A 1 382 PRO 382 382 382 PRO PRO A . n A 1 383 GLU 383 383 383 GLU GLU A . n A 1 384 VAL 384 384 384 VAL VAL A . n A 1 385 THR 385 385 385 THR THR A . n A 1 386 TYR 386 386 386 TYR TYR A . n A 1 387 THR 387 387 387 THR THR A . n A 1 388 ASN 388 388 388 ASN ASN A . n A 1 389 LEU 389 389 389 LEU LEU A . n A 1 390 ARG 390 390 390 ARG ARG A . n A 1 391 TRP 391 391 391 TRP TRP A . n A 1 392 GLY 392 392 392 GLY GLY A . n A 1 393 GLU 393 393 393 GLU GLU A . n A 1 394 ILE 394 394 394 ILE ILE A . n A 1 395 GLY 395 395 395 GLY GLY A . n A 1 396 SER 396 396 396 SER SER A . n A 1 397 THR 397 397 397 THR THR A . n A 1 398 TYR 398 398 398 TYR TYR A . n A 1 399 GLN 399 399 399 GLN GLN A . n A 1 400 GLU 400 400 ? ? ? A . n A 1 401 LEU 401 401 ? ? ? A . n A 1 402 GLN 402 402 ? ? ? A . n B 1 1 PCA 1 1 1 PCA PCA B . n B 1 2 LYS 2 2 2 LYS LYS B . n B 1 3 PRO 3 3 3 PRO PRO B . n B 1 4 GLY 4 4 4 GLY GLY B . n B 1 5 GLU 5 5 5 GLU GLU B . n B 1 6 THR 6 6 6 THR THR B . n B 1 7 LYS 7 7 7 LYS LYS B . n B 1 8 GLU 8 8 8 GLU GLU B . n B 1 9 VAL 9 9 9 VAL VAL B . n B 1 10 HIS 10 10 10 HIS HIS B . n B 1 11 PRO 11 11 11 PRO PRO B . n B 1 12 GLN 12 12 12 GLN GLN B . n B 1 13 LEU 13 13 13 LEU LEU B . n B 1 14 THR 14 14 14 THR THR B . n B 1 15 THR 15 15 15 THR THR B . n B 1 16 PHE 16 16 16 PHE PHE B . n B 1 17 ARG 17 17 17 ARG ARG B . n B 1 18 CYS 18 18 18 CYS CYS B . n B 1 19 THR 19 19 19 THR THR B . n B 1 20 LYS 20 20 20 LYS LYS B . n B 1 21 ARG 21 21 21 ARG ARG B . n B 1 22 GLY 22 22 22 GLY GLY B . n B 1 23 GLY 23 23 23 GLY GLY B . n B 1 24 CYS 24 24 24 CYS CYS B . n B 1 25 LYS 25 25 25 LYS LYS B . n B 1 26 PRO 26 26 26 PRO PRO B . n B 1 27 ALA 27 27 27 ALA ALA B . n B 1 28 THR 28 28 28 THR THR B . n B 1 29 ASN 29 29 29 ASN ASN B . n B 1 30 PHE 30 30 30 PHE PHE B . n B 1 31 ILE 31 31 31 ILE ILE B . n B 1 32 VAL 32 32 32 VAL VAL B . n B 1 33 LEU 33 33 33 LEU LEU B . n B 1 34 ASP 34 34 34 ASP ASP B . n B 1 35 SER 35 35 35 SER SER B . n B 1 36 LEU 36 36 36 LEU LEU B . n B 1 37 SER 37 37 37 SER SER B . n B 1 38 HIS 38 38 38 HIS HIS B . n B 1 39 PRO 39 39 39 PRO PRO B . n B 1 40 ILE 40 40 40 ILE ILE B . n B 1 41 HIS 41 41 41 HIS HIS B . n B 1 42 ARG 42 42 42 ARG ARG B . n B 1 43 ALA 43 43 43 ALA ALA B . n B 1 44 GLU 44 44 44 GLU GLU B . n B 1 45 GLY 45 45 45 GLY GLY B . n B 1 46 LEU 46 46 46 LEU LEU B . n B 1 47 GLY 47 47 47 GLY GLY B . n B 1 48 PRO 48 48 48 PRO PRO B . n B 1 49 GLY 49 49 49 GLY GLY B . n B 1 50 GLY 50 50 50 GLY GLY B . n B 1 51 CYS 51 51 51 CYS CYS B . n B 1 52 GLY 52 52 52 GLY GLY B . n B 1 53 ASP 53 53 53 ASP ASP B . n B 1 54 TRP 54 54 54 TRP TRP B . n B 1 55 GLY 55 55 55 GLY GLY B . n B 1 56 ASN 56 56 56 ASN ASN B . n B 1 57 PRO 57 57 57 PRO PRO B . n B 1 58 PRO 58 58 58 PRO PRO B . n B 1 59 PRO 59 59 59 PRO PRO B . n B 1 60 LYS 60 60 60 LYS LYS B . n B 1 61 ASP 61 61 61 ASP ASP B . n B 1 62 VAL 62 62 62 VAL VAL B . n B 1 63 CYS 63 63 63 CYS CYS B . n B 1 64 PRO 64 64 64 PRO PRO B . n B 1 65 ASP 65 65 65 ASP ASP B . n B 1 66 VAL 66 66 66 VAL VAL B . n B 1 67 GLU 67 67 67 GLU GLU B . n B 1 68 SER 68 68 68 SER SER B . n B 1 69 CYS 69 69 69 CYS CYS B . n B 1 70 ALA 70 70 70 ALA ALA B . n B 1 71 LYS 71 71 71 LYS LYS B . n B 1 72 ASN 72 72 72 ASN ASN B . n B 1 73 CYS 73 73 73 CYS CYS B . n B 1 74 ILE 74 74 74 ILE ILE B . n B 1 75 MET 75 75 75 MET MET B . n B 1 76 GLU 76 76 76 GLU GLU B . n B 1 77 GLY 77 77 77 GLY GLY B . n B 1 78 ILE 78 78 78 ILE ILE B . n B 1 79 PRO 79 79 79 PRO PRO B . n B 1 80 ASP 80 80 80 ASP ASP B . n B 1 81 TYR 81 81 81 TYR TYR B . n B 1 82 SER 82 82 82 SER SER B . n B 1 83 GLN 83 83 83 GLN GLN B . n B 1 84 TYR 84 84 84 TYR TYR B . n B 1 85 GLY 85 85 85 GLY GLY B . n B 1 86 VAL 86 86 86 VAL VAL B . n B 1 87 THR 87 87 87 THR THR B . n B 1 88 THR 88 88 88 THR THR B . n B 1 89 ASN 89 89 89 ASN ASN B . n B 1 90 GLY 90 90 90 GLY GLY B . n B 1 91 THR 91 91 91 THR THR B . n B 1 92 SER 92 92 92 SER SER B . n B 1 93 LEU 93 93 93 LEU LEU B . n B 1 94 ARG 94 94 94 ARG ARG B . n B 1 95 LEU 95 95 95 LEU LEU B . n B 1 96 GLN 96 96 96 GLN GLN B . n B 1 97 HIS 97 97 97 HIS HIS B . n B 1 98 ILE 98 98 98 ILE ILE B . n B 1 99 LEU 99 99 99 LEU LEU B . n B 1 100 PRO 100 100 100 PRO PRO B . n B 1 101 ASP 101 101 101 ASP ASP B . n B 1 102 GLY 102 102 102 GLY GLY B . n B 1 103 ARG 103 103 103 ARG ARG B . n B 1 104 VAL 104 104 104 VAL VAL B . n B 1 105 PRO 105 105 105 PRO PRO B . n B 1 106 SER 106 106 106 SER SER B . n B 1 107 PRO 107 107 107 PRO PRO B . n B 1 108 ARG 108 108 108 ARG ARG B . n B 1 109 VAL 109 109 109 VAL VAL B . n B 1 110 TYR 110 110 110 TYR TYR B . n B 1 111 LEU 111 111 111 LEU LEU B . n B 1 112 LEU 112 112 112 LEU LEU B . n B 1 113 ASP 113 113 113 ASP ASP B . n B 1 114 LYS 114 114 114 LYS LYS B . n B 1 115 THR 115 115 115 THR THR B . n B 1 116 LYS 116 116 116 LYS LYS B . n B 1 117 ARG 117 117 117 ARG ARG B . n B 1 118 ARG 118 118 118 ARG ARG B . n B 1 119 TYR 119 119 119 TYR TYR B . n B 1 120 GLU 120 120 120 GLU GLU B . n B 1 121 MET 121 121 121 MET MET B . n B 1 122 LEU 122 122 122 LEU LEU B . n B 1 123 HIS 123 123 123 HIS HIS B . n B 1 124 LEU 124 124 124 LEU LEU B . n B 1 125 THR 125 125 125 THR THR B . n B 1 126 GLY 126 126 126 GLY GLY B . n B 1 127 PHE 127 127 127 PHE PHE B . n B 1 128 GLU 128 128 128 GLU GLU B . n B 1 129 PHE 129 129 129 PHE PHE B . n B 1 130 THR 130 130 130 THR THR B . n B 1 131 PHE 131 131 131 PHE PHE B . n B 1 132 ASP 132 132 132 ASP ASP B . n B 1 133 VAL 133 133 133 VAL VAL B . n B 1 134 ASP 134 134 134 ASP ASP B . n B 1 135 ALA 135 135 135 ALA ALA B . n B 1 136 THR 136 136 136 THR THR B . n B 1 137 LYS 137 137 137 LYS LYS B . n B 1 138 LEU 138 138 138 LEU LEU B . n B 1 139 PRO 139 139 139 PRO PRO B . n B 1 140 CYS 140 140 140 CYS CYS B . n B 1 141 GLY 141 141 141 GLY GLY B . n B 1 142 MET 142 142 142 MET MET B . n B 1 143 ASN 143 143 143 ASN ASN B . n B 1 144 SER 144 144 144 SER SER B . n B 1 145 ALA 145 145 145 ALA ALA B . n B 1 146 LEU 146 146 146 LEU LEU B . n B 1 147 TYR 147 147 147 TYR TYR B . n B 1 148 LEU 148 148 148 LEU LEU B . n B 1 149 SER 149 149 149 SER SER B . n B 1 150 GLU 150 150 150 GLU GLU B . n B 1 151 MET 151 151 151 MET MET B . n B 1 152 HIS 152 152 152 HIS HIS B . n B 1 153 PRO 153 153 153 PRO PRO B . n B 1 154 THR 154 154 154 THR THR B . n B 1 155 GLY 155 155 155 GLY GLY B . n B 1 156 ALA 156 156 156 ALA ALA B . n B 1 157 LYS 157 157 157 LYS LYS B . n B 1 158 SER 158 158 158 SER SER B . n B 1 159 LYS 159 159 159 LYS LYS B . n B 1 160 TYR 160 160 160 TYR TYR B . n B 1 161 ASN 161 161 161 ASN ASN B . n B 1 162 PRO 162 162 162 PRO PRO B . n B 1 163 GLY 163 163 163 GLY GLY B . n B 1 164 GLY 164 164 164 GLY GLY B . n B 1 165 ALA 165 165 165 ALA ALA B . n B 1 166 TYR 166 166 166 TYR TYR B . n B 1 167 TYR 167 167 167 TYR TYR B . n B 1 168 GLY 168 168 168 GLY GLY B . n B 1 169 THR 169 169 169 THR THR B . n B 1 170 GLY 170 170 170 GLY GLY B . n B 1 171 TYR 171 171 171 TYR TYR B . n B 1 172 CYS 172 172 172 CYS CYS B . n B 1 173 ASP 173 173 173 ASP ASP B . n B 1 174 ALA 174 174 174 ALA ALA B . n B 1 175 GLN 175 175 175 GLN GLN B . n B 1 176 CYS 176 176 176 CYS CYS B . n B 1 177 PHE 177 177 177 PHE PHE B . n B 1 178 VAL 178 178 178 VAL VAL B . n B 1 179 THR 179 179 179 THR THR B . n B 1 180 PRO 180 180 180 PRO PRO B . n B 1 181 PHE 181 181 181 PHE PHE B . n B 1 182 ILE 182 182 182 ILE ILE B . n B 1 183 ASN 183 183 183 ASN ASN B . n B 1 184 GLY 184 184 184 GLY GLY B . n B 1 185 LEU 185 185 185 LEU LEU B . n B 1 186 GLY 186 186 186 GLY GLY B . n B 1 187 ASN 187 187 187 ASN ASN B . n B 1 188 ILE 188 188 188 ILE ILE B . n B 1 189 GLU 189 189 189 GLU GLU B . n B 1 190 GLY 190 190 190 GLY GLY B . n B 1 191 LYS 191 191 191 LYS LYS B . n B 1 192 GLY 192 192 192 GLY GLY B . n B 1 193 SER 193 193 193 SER SER B . n B 1 194 CYS 194 194 194 CYS CYS B . n B 1 195 CYS 195 195 195 CYS CYS B . n B 1 196 ASN 196 196 196 ASN ASN B . n B 1 197 SER 197 197 197 SER SER B . n B 1 198 MET 198 198 198 MET MET B . n B 1 199 ASP 199 199 199 ASP ASP B . n B 1 200 ILE 200 200 200 ILE ILE B . n B 1 201 TRP 201 201 201 TRP TRP B . n B 1 202 GLU 202 202 202 GLU GLU B . n B 1 203 ALA 203 203 203 ALA ALA B . n B 1 204 ASN 204 204 204 ASN ASN B . n B 1 205 SER 205 205 205 SER SER B . n B 1 206 ARG 206 206 206 ARG ARG B . n B 1 207 ALA 207 207 207 ALA ALA B . n B 1 208 SER 208 208 208 SER SER B . n B 1 209 HIS 209 209 209 HIS HIS B . n B 1 210 VAL 210 210 210 VAL VAL B . n B 1 211 ALA 211 211 211 ALA ALA B . n B 1 212 PRO 212 212 212 PRO PRO B . n B 1 213 HIS 213 213 213 HIS HIS B . n B 1 214 THR 214 214 214 THR THR B . n B 1 215 CYS 215 215 215 CYS CYS 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 LYS 218 218 218 LYS LYS B . n B 1 219 GLY 219 219 219 GLY GLY B . n B 1 220 LEU 220 220 220 LEU LEU B . n B 1 221 TYR 221 221 221 TYR TYR B . n B 1 222 LEU 222 222 222 LEU LEU B . n B 1 223 CYS 223 223 223 CYS CYS B . n B 1 224 GLU 224 224 224 GLU GLU B . n B 1 225 GLY 225 225 225 GLY GLY B . n B 1 226 GLU 226 226 226 GLU GLU 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 ALA 229 229 229 ALA ALA B . n B 1 230 PHE 230 230 230 PHE PHE B . n B 1 231 GLU 231 231 231 GLU GLU B . n B 1 232 GLY 232 232 232 GLY GLY B . n B 1 233 VAL 233 233 233 VAL VAL B . n B 1 234 CYS 234 234 234 CYS CYS B . n B 1 235 ASP 235 235 235 ASP ASP B . n B 1 236 LYS 236 236 236 LYS LYS B . n B 1 237 ASN 237 237 237 ASN ASN B . n B 1 238 GLY 238 238 238 GLY GLY B . n B 1 239 CYS 239 239 239 CYS CYS B . n B 1 240 GLY 240 240 240 GLY GLY B . n B 1 241 TRP 241 241 241 TRP TRP B . n B 1 242 ASN 242 242 242 ASN ASN B . n B 1 243 ASN 243 243 243 ASN ASN B . n B 1 244 TYR 244 244 244 TYR TYR B . n B 1 245 ARG 245 245 245 ARG ARG B . n B 1 246 VAL 246 246 246 VAL VAL B . n B 1 247 ASN 247 247 247 ASN ASN B . n B 1 248 VAL 248 248 248 VAL VAL B . n B 1 249 THR 249 249 249 THR THR B . n B 1 250 ASP 250 250 250 ASP ASP B . n B 1 251 TYR 251 251 251 TYR TYR B . n B 1 252 TYR 252 252 252 TYR TYR B . n B 1 253 GLY 253 253 253 GLY GLY B . n B 1 254 ARG 254 254 254 ARG ARG B . n B 1 255 GLY 255 255 255 GLY GLY B . n B 1 256 GLU 256 256 256 GLU GLU B . n B 1 257 GLU 257 257 257 GLU GLU B . n B 1 258 PHE 258 258 258 PHE PHE B . n B 1 259 LYS 259 259 259 LYS LYS B . n B 1 260 VAL 260 260 260 VAL VAL B . n B 1 261 ASN 261 261 261 ASN ASN B . n B 1 262 THR 262 262 262 THR THR B . n B 1 263 LEU 263 263 263 LEU LEU B . n B 1 264 LYS 264 264 264 LYS LYS B . n B 1 265 PRO 265 265 265 PRO PRO B . n B 1 266 PHE 266 266 266 PHE PHE B . n B 1 267 THR 267 267 267 THR THR B . n B 1 268 VAL 268 268 268 VAL VAL B . n B 1 269 VAL 269 269 269 VAL VAL B . n B 1 270 THR 270 270 270 THR THR B . n B 1 271 GLN 271 271 271 GLN GLN B . n B 1 272 PHE 272 272 272 PHE PHE B . n B 1 273 LEU 273 273 273 LEU LEU B . n B 1 274 ALA 274 274 274 ALA ALA B . n B 1 275 ASN 275 275 275 ASN ASN B . n B 1 276 ARG 276 276 276 ARG ARG B . n B 1 277 ARG 277 277 277 ARG ARG B . n B 1 278 GLY 278 278 278 GLY GLY B . n B 1 279 LYS 279 279 279 LYS LYS B . n B 1 280 LEU 280 280 280 LEU LEU B . n B 1 281 GLU 281 281 281 GLU GLU B . n B 1 282 LYS 282 282 282 LYS LYS B . n B 1 283 ILE 283 283 283 ILE ILE B . n B 1 284 HIS 284 284 284 HIS HIS B . n B 1 285 ARG 285 285 285 ARG ARG B . n B 1 286 PHE 286 286 286 PHE PHE B . n B 1 287 TYR 287 287 287 TYR TYR B . n B 1 288 VAL 288 288 288 VAL VAL B . n B 1 289 GLN 289 289 289 GLN GLN B . n B 1 290 ASP 290 290 290 ASP ASP B . n B 1 291 GLY 291 291 291 GLY GLY B . n B 1 292 LYS 292 292 292 LYS LYS B . n B 1 293 VAL 293 293 293 VAL VAL B . n B 1 294 ILE 294 294 294 ILE ILE B . n B 1 295 GLU 295 295 295 GLU GLU B . n B 1 296 SER 296 296 296 SER SER B . n B 1 297 PHE 297 297 297 PHE PHE B . n B 1 298 TYR 298 298 298 TYR TYR B . n B 1 299 THR 299 299 299 THR THR B . n B 1 300 ASN 300 300 300 ASN ASN B . n B 1 301 LYS 301 301 301 LYS LYS B . n B 1 302 GLU 302 302 302 GLU GLU B . n B 1 303 GLY 303 303 303 GLY GLY B . n B 1 304 VAL 304 304 304 VAL VAL B . n B 1 305 PRO 305 305 305 PRO PRO B . n B 1 306 TYR 306 306 306 TYR TYR B . n B 1 307 THR 307 307 307 THR THR B . n B 1 308 ASN 308 308 308 ASN ASN B . n B 1 309 MET 309 309 309 MET MET B . n B 1 310 ILE 310 310 310 ILE ILE B . n B 1 311 ASP 311 311 311 ASP ASP B . n B 1 312 ASP 312 312 312 ASP ASP B . n B 1 313 GLU 313 313 313 GLU GLU B . n B 1 314 PHE 314 314 314 PHE PHE B . n B 1 315 CYS 315 315 315 CYS CYS B . n B 1 316 GLU 316 316 316 GLU GLU B . n B 1 317 ALA 317 317 317 ALA ALA B . n B 1 318 THR 318 318 318 THR THR B . n B 1 319 GLY 319 319 319 GLY GLY B . n B 1 320 SER 320 320 320 SER SER B . n B 1 321 ARG 321 321 321 ARG ARG B . n B 1 322 LYS 322 322 322 LYS LYS B . n B 1 323 TYR 323 323 323 TYR TYR B . n B 1 324 MET 324 324 324 MET MET B . n B 1 325 GLU 325 325 325 GLU GLU B . n B 1 326 LEU 326 326 326 LEU LEU B . n B 1 327 GLY 327 327 327 GLY GLY B . n B 1 328 ALA 328 328 328 ALA ALA B . n B 1 329 THR 329 329 329 THR THR B . n B 1 330 GLN 330 330 330 GLN GLN B . n B 1 331 GLY 331 331 331 GLY GLY B . n B 1 332 MET 332 332 332 MET MET B . n B 1 333 GLY 333 333 333 GLY GLY B . n B 1 334 GLU 334 334 334 GLU GLU B . n B 1 335 ALA 335 335 335 ALA ALA B . n B 1 336 LEU 336 336 336 LEU LEU B . n B 1 337 THR 337 337 337 THR THR B . n B 1 338 ARG 338 338 338 ARG ARG B . n B 1 339 GLY 339 339 339 GLY GLY B . n B 1 340 MET 340 340 340 MET MET B . n B 1 341 VAL 341 341 341 VAL VAL B . n B 1 342 LEU 342 342 342 LEU LEU B . n B 1 343 ALA 343 343 343 ALA ALA B . n B 1 344 MET 344 344 344 MET MET B . n B 1 345 SER 345 345 345 SER SER B . n B 1 346 ILE 346 346 346 ILE ILE B . n B 1 347 TRP 347 347 347 TRP TRP B . n B 1 348 TRP 348 348 348 TRP TRP B . n B 1 349 ASP 349 349 349 ASP ASP B . n B 1 350 GLN 350 350 350 GLN GLN B . n B 1 351 GLY 351 351 351 GLY GLY B . n B 1 352 GLY 352 352 352 GLY GLY B . n B 1 353 ASN 353 353 353 ASN ASN B . n B 1 354 MET 354 354 354 MET MET B . n B 1 355 GLU 355 355 355 GLU GLU B . n B 1 356 TRP 356 356 356 TRP TRP B . n B 1 357 LEU 357 357 357 LEU LEU B . n B 1 358 ASP 358 358 358 ASP ASP B . n B 1 359 HIS 359 359 359 HIS HIS B . n B 1 360 GLY 360 360 360 GLY GLY B . n B 1 361 GLU 361 361 361 GLU GLU B . n B 1 362 ALA 362 362 362 ALA ALA B . n B 1 363 GLY 363 363 363 GLY GLY B . n B 1 364 PRO 364 364 364 PRO PRO B . n B 1 365 CYS 365 365 365 CYS CYS B . n B 1 366 ALA 366 366 366 ALA ALA B . n B 1 367 LYS 367 367 367 LYS LYS B . n B 1 368 GLY 368 368 368 GLY GLY B . n B 1 369 GLU 369 369 369 GLU GLU B . n B 1 370 GLY 370 370 370 GLY GLY B . n B 1 371 ALA 371 371 371 ALA ALA B . n B 1 372 PRO 372 372 372 PRO PRO B . n B 1 373 SER 373 373 373 SER SER B . n B 1 374 ASN 374 374 374 ASN ASN B . n B 1 375 ILE 375 375 375 ILE ILE B . n B 1 376 VAL 376 376 376 VAL VAL B . n B 1 377 GLN 377 377 377 GLN GLN B . n B 1 378 VAL 378 378 378 VAL VAL B . n B 1 379 GLU 379 379 379 GLU GLU B . n B 1 380 PRO 380 380 380 PRO PRO B . n B 1 381 PHE 381 381 381 PHE PHE B . n B 1 382 PRO 382 382 382 PRO PRO B . n B 1 383 GLU 383 383 383 GLU GLU B . n B 1 384 VAL 384 384 384 VAL VAL B . n B 1 385 THR 385 385 385 THR THR B . n B 1 386 TYR 386 386 386 TYR TYR B . n B 1 387 THR 387 387 387 THR THR B . n B 1 388 ASN 388 388 388 ASN ASN B . n B 1 389 LEU 389 389 389 LEU LEU B . n B 1 390 ARG 390 390 390 ARG ARG B . n B 1 391 TRP 391 391 391 TRP TRP B . n B 1 392 GLY 392 392 392 GLY GLY B . n B 1 393 GLU 393 393 393 GLU GLU B . n B 1 394 ILE 394 394 394 ILE ILE B . n B 1 395 GLY 395 395 395 GLY GLY B . n B 1 396 SER 396 396 396 SER SER B . n B 1 397 THR 397 397 397 THR THR B . n B 1 398 TYR 398 398 398 TYR TYR B . n B 1 399 GLN 399 399 399 GLN GLN B . n B 1 400 GLU 400 400 ? ? ? B . n B 1 401 LEU 401 401 ? ? ? B . n B 1 402 GLN 402 402 ? ? ? 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 BGC 1 1400 1400 BGC BGC A . D 3 GAL 2 1403 1403 GAL GAL A . E 4 GLC 1 1401 1401 GLC GLC A . F 3 GAL 2 1402 1402 GAL GAL A . G 5 NAG 1 1404 1404 NAG NAG A . H 5 NAG 1 1399 1399 NAG NAG B . I 2 BGC 1 1401 1401 BGC BGC B . J 3 GAL 2 1404 1404 GAL GAL B . K 4 GLC 1 1402 1402 GLC GLC B . L 3 GAL 2 1403 1403 GAL GAL B . M 6 HOH 1 2001 2001 HOH HOH A . M 6 HOH 2 2002 2002 HOH HOH A . M 6 HOH 3 2003 2003 HOH HOH A . M 6 HOH 4 2004 2004 HOH HOH A . M 6 HOH 5 2005 2005 HOH HOH A . M 6 HOH 6 2006 2006 HOH HOH A . M 6 HOH 7 2007 2007 HOH HOH A . M 6 HOH 8 2008 2008 HOH HOH A . M 6 HOH 9 2009 2009 HOH HOH A . M 6 HOH 10 2010 2010 HOH HOH A . M 6 HOH 11 2011 2011 HOH HOH A . M 6 HOH 12 2012 2012 HOH HOH A . M 6 HOH 13 2013 2013 HOH HOH A . M 6 HOH 14 2014 2014 HOH HOH A . M 6 HOH 15 2015 2015 HOH HOH A . M 6 HOH 16 2016 2016 HOH HOH A . M 6 HOH 17 2017 2017 HOH HOH A . M 6 HOH 18 2018 2018 HOH HOH A . M 6 HOH 19 2019 2019 HOH HOH A . M 6 HOH 20 2020 2020 HOH HOH A . M 6 HOH 21 2021 2021 HOH HOH A . M 6 HOH 22 2022 2022 HOH HOH A . M 6 HOH 23 2023 2023 HOH HOH A . M 6 HOH 24 2024 2024 HOH HOH A . M 6 HOH 25 2025 2025 HOH HOH A . M 6 HOH 26 2026 2026 HOH HOH A . M 6 HOH 27 2027 2027 HOH HOH A . M 6 HOH 28 2028 2028 HOH HOH A . M 6 HOH 29 2029 2029 HOH HOH A . M 6 HOH 30 2030 2030 HOH HOH A . M 6 HOH 31 2031 2031 HOH HOH A . M 6 HOH 32 2032 2032 HOH HOH A . M 6 HOH 33 2033 2033 HOH HOH A . M 6 HOH 34 2034 2034 HOH HOH A . M 6 HOH 35 2035 2035 HOH HOH A . M 6 HOH 36 2036 2036 HOH HOH A . M 6 HOH 37 2037 2037 HOH HOH A . M 6 HOH 38 2038 2038 HOH HOH A . M 6 HOH 39 2039 2039 HOH HOH A . M 6 HOH 40 2040 2040 HOH HOH A . M 6 HOH 41 2041 2041 HOH HOH A . M 6 HOH 42 2042 2042 HOH HOH A . M 6 HOH 43 2043 2043 HOH HOH A . M 6 HOH 44 2044 2044 HOH HOH A . M 6 HOH 45 2045 2045 HOH HOH A . M 6 HOH 46 2046 2046 HOH HOH A . M 6 HOH 47 2047 2047 HOH HOH A . M 6 HOH 48 2048 2048 HOH HOH A . M 6 HOH 49 2049 2049 HOH HOH A . M 6 HOH 50 2050 2050 HOH HOH A . M 6 HOH 51 2051 2051 HOH HOH A . M 6 HOH 52 2052 2052 HOH HOH A . M 6 HOH 53 2053 2053 HOH HOH A . M 6 HOH 54 2054 2054 HOH HOH A . M 6 HOH 55 2055 2055 HOH HOH A . M 6 HOH 56 2056 2056 HOH HOH A . M 6 HOH 57 2057 2057 HOH HOH A . M 6 HOH 58 2058 2058 HOH HOH A . M 6 HOH 59 2059 2059 HOH HOH A . M 6 HOH 60 2060 2060 HOH HOH A . M 6 HOH 61 2061 2061 HOH HOH A . M 6 HOH 62 2062 2062 HOH HOH A . M 6 HOH 63 2063 2063 HOH HOH A . M 6 HOH 64 2064 2064 HOH HOH A . M 6 HOH 65 2065 2065 HOH HOH A . M 6 HOH 66 2066 2066 HOH HOH A . M 6 HOH 67 2067 2067 HOH HOH A . M 6 HOH 68 2068 2068 HOH HOH A . M 6 HOH 69 2069 2069 HOH HOH A . M 6 HOH 70 2070 2070 HOH HOH A . M 6 HOH 71 2071 2071 HOH HOH A . M 6 HOH 72 2072 2072 HOH HOH A . M 6 HOH 73 2073 2073 HOH HOH A . M 6 HOH 74 2074 2074 HOH HOH A . M 6 HOH 75 2075 2075 HOH HOH A . M 6 HOH 76 2076 2076 HOH HOH A . M 6 HOH 77 2077 2077 HOH HOH A . M 6 HOH 78 2078 2078 HOH HOH A . M 6 HOH 79 2079 2079 HOH HOH A . M 6 HOH 80 2080 2080 HOH HOH A . M 6 HOH 81 2081 2081 HOH HOH A . M 6 HOH 82 2082 2082 HOH HOH A . M 6 HOH 83 2083 2083 HOH HOH A . M 6 HOH 84 2084 2084 HOH HOH A . M 6 HOH 85 2085 2085 HOH HOH A . M 6 HOH 86 2086 2086 HOH HOH A . M 6 HOH 87 2087 2087 HOH HOH A . M 6 HOH 88 2088 2088 HOH HOH A . M 6 HOH 89 2089 2089 HOH HOH A . M 6 HOH 90 2090 2090 HOH HOH A . M 6 HOH 91 2091 2091 HOH HOH A . M 6 HOH 92 2092 2092 HOH HOH A . M 6 HOH 93 2093 2093 HOH HOH A . M 6 HOH 94 2094 2094 HOH HOH A . M 6 HOH 95 2095 2095 HOH HOH A . M 6 HOH 96 2096 2096 HOH HOH A . M 6 HOH 97 2097 2097 HOH HOH A . M 6 HOH 98 2098 2098 HOH HOH A . M 6 HOH 99 2099 2099 HOH HOH A . M 6 HOH 100 2100 2100 HOH HOH A . M 6 HOH 101 2101 2101 HOH HOH A . M 6 HOH 102 2102 2102 HOH HOH A . M 6 HOH 103 2103 2103 HOH HOH A . M 6 HOH 104 2104 2104 HOH HOH A . M 6 HOH 105 2105 2105 HOH HOH A . M 6 HOH 106 2106 2106 HOH HOH A . M 6 HOH 107 2107 2107 HOH HOH A . M 6 HOH 108 2108 2108 HOH HOH A . M 6 HOH 109 2109 2109 HOH HOH A . M 6 HOH 110 2110 2110 HOH HOH A . M 6 HOH 111 2111 2111 HOH HOH A . M 6 HOH 112 2112 2112 HOH HOH A . M 6 HOH 113 2113 2113 HOH HOH A . M 6 HOH 114 2114 2114 HOH HOH A . M 6 HOH 115 2115 2115 HOH HOH A . M 6 HOH 116 2116 2116 HOH HOH A . M 6 HOH 117 2117 2117 HOH HOH A . M 6 HOH 118 2118 2118 HOH HOH A . M 6 HOH 119 2119 2119 HOH HOH A . M 6 HOH 120 2120 2120 HOH HOH A . M 6 HOH 121 2121 2121 HOH HOH A . M 6 HOH 122 2122 2122 HOH HOH A . M 6 HOH 123 2123 2123 HOH HOH A . M 6 HOH 124 2124 2124 HOH HOH A . M 6 HOH 125 2125 2125 HOH HOH A . M 6 HOH 126 2126 2126 HOH HOH A . M 6 HOH 127 2127 2127 HOH HOH A . M 6 HOH 128 2128 2128 HOH HOH A . M 6 HOH 129 2129 2129 HOH HOH A . M 6 HOH 130 2130 2130 HOH HOH A . M 6 HOH 131 2131 2131 HOH HOH A . M 6 HOH 132 2132 2132 HOH HOH A . M 6 HOH 133 2133 2133 HOH HOH A . M 6 HOH 134 2134 2134 HOH HOH A . M 6 HOH 135 2135 2135 HOH HOH A . M 6 HOH 136 2136 2136 HOH HOH A . M 6 HOH 137 2137 2137 HOH HOH A . M 6 HOH 138 2138 2138 HOH HOH A . M 6 HOH 139 2139 2139 HOH HOH A . M 6 HOH 140 2140 2140 HOH HOH A . M 6 HOH 141 2141 2141 HOH HOH A . M 6 HOH 142 2142 2142 HOH HOH A . M 6 HOH 143 2143 2143 HOH HOH A . M 6 HOH 144 2144 2144 HOH HOH A . M 6 HOH 145 2145 2145 HOH HOH A . M 6 HOH 146 2146 2146 HOH HOH A . M 6 HOH 147 2147 2147 HOH HOH A . M 6 HOH 148 2148 2148 HOH HOH A . M 6 HOH 149 2149 2149 HOH HOH A . M 6 HOH 150 2150 2150 HOH HOH A . M 6 HOH 151 2151 2151 HOH HOH A . M 6 HOH 152 2152 2152 HOH HOH A . M 6 HOH 153 2153 2153 HOH HOH A . M 6 HOH 154 2154 2154 HOH HOH A . M 6 HOH 155 2155 2155 HOH HOH A . M 6 HOH 156 2156 2156 HOH HOH A . M 6 HOH 157 2157 2157 HOH HOH A . M 6 HOH 158 2158 2158 HOH HOH A . M 6 HOH 159 2159 2159 HOH HOH A . M 6 HOH 160 2160 2160 HOH HOH A . M 6 HOH 161 2161 2161 HOH HOH A . M 6 HOH 162 2162 2162 HOH HOH A . M 6 HOH 163 2163 2163 HOH HOH A . M 6 HOH 164 2164 2164 HOH HOH A . M 6 HOH 165 2165 2165 HOH HOH A . M 6 HOH 166 2166 2166 HOH HOH A . M 6 HOH 167 2167 2167 HOH HOH A . M 6 HOH 168 2168 2168 HOH HOH A . M 6 HOH 169 2169 2169 HOH HOH A . M 6 HOH 170 2170 2170 HOH HOH A . M 6 HOH 171 2171 2171 HOH HOH A . M 6 HOH 172 2172 2172 HOH HOH A . M 6 HOH 173 2173 2173 HOH HOH A . M 6 HOH 174 2174 2174 HOH HOH A . M 6 HOH 175 2175 2175 HOH HOH A . M 6 HOH 176 2176 2176 HOH HOH A . M 6 HOH 177 2177 2177 HOH HOH A . M 6 HOH 178 2178 2178 HOH HOH A . M 6 HOH 179 2179 2179 HOH HOH A . M 6 HOH 180 2180 2180 HOH HOH A . M 6 HOH 181 2181 2181 HOH HOH A . M 6 HOH 182 2182 2182 HOH HOH A . M 6 HOH 183 2183 2183 HOH HOH A . M 6 HOH 184 2184 2184 HOH HOH A . M 6 HOH 185 2185 2185 HOH HOH A . M 6 HOH 186 2186 2186 HOH HOH A . M 6 HOH 187 2187 2187 HOH HOH A . M 6 HOH 188 2188 2188 HOH HOH A . M 6 HOH 189 2189 2189 HOH HOH A . M 6 HOH 190 2190 2190 HOH HOH A . M 6 HOH 191 2191 2191 HOH HOH A . M 6 HOH 192 2192 2192 HOH HOH A . M 6 HOH 193 2193 2193 HOH HOH A . M 6 HOH 194 2194 2194 HOH HOH A . M 6 HOH 195 2195 2195 HOH HOH A . M 6 HOH 196 2196 2196 HOH HOH A . M 6 HOH 197 2197 2197 HOH HOH A . M 6 HOH 198 2198 2198 HOH HOH A . M 6 HOH 199 2199 2199 HOH HOH A . M 6 HOH 200 2200 2200 HOH HOH A . M 6 HOH 201 2201 2201 HOH HOH A . M 6 HOH 202 2202 2202 HOH HOH A . M 6 HOH 203 2203 2203 HOH HOH A . M 6 HOH 204 2204 2204 HOH HOH A . M 6 HOH 205 2205 2205 HOH HOH A . M 6 HOH 206 2206 2206 HOH HOH A . M 6 HOH 207 2207 2207 HOH HOH A . M 6 HOH 208 2208 2208 HOH HOH A . M 6 HOH 209 2209 2209 HOH HOH A . M 6 HOH 210 2210 2210 HOH HOH A . M 6 HOH 211 2211 2211 HOH HOH A . M 6 HOH 212 2212 2212 HOH HOH A . M 6 HOH 213 2213 2213 HOH HOH A . M 6 HOH 214 2214 2214 HOH HOH A . M 6 HOH 215 2215 2215 HOH HOH A . M 6 HOH 216 2216 2216 HOH HOH A . M 6 HOH 217 2217 2217 HOH HOH A . M 6 HOH 218 2218 2218 HOH HOH A . M 6 HOH 219 2219 2219 HOH HOH A . M 6 HOH 220 2220 2220 HOH HOH A . M 6 HOH 221 2221 2221 HOH HOH A . M 6 HOH 222 2222 2222 HOH HOH A . M 6 HOH 223 2223 2223 HOH HOH A . M 6 HOH 224 2224 2224 HOH HOH A . M 6 HOH 225 2225 2225 HOH HOH A . M 6 HOH 226 2226 2226 HOH HOH A . M 6 HOH 227 2227 2227 HOH HOH A . M 6 HOH 228 2228 2228 HOH HOH A . M 6 HOH 229 2229 2229 HOH HOH A . M 6 HOH 230 2230 2230 HOH HOH A . M 6 HOH 231 2231 2231 HOH HOH A . M 6 HOH 232 2232 2232 HOH HOH A . M 6 HOH 233 2233 2233 HOH HOH A . M 6 HOH 234 2234 2234 HOH HOH A . M 6 HOH 235 2235 2235 HOH HOH A . M 6 HOH 236 2236 2236 HOH HOH A . M 6 HOH 237 2237 2237 HOH HOH A . M 6 HOH 238 2238 2238 HOH HOH A . M 6 HOH 239 2239 2239 HOH HOH A . M 6 HOH 240 2240 2240 HOH HOH A . M 6 HOH 241 2241 2241 HOH HOH A . M 6 HOH 242 2242 2242 HOH HOH A . M 6 HOH 243 2243 2243 HOH HOH A . M 6 HOH 244 2244 2244 HOH HOH A . M 6 HOH 245 2245 2245 HOH HOH A . M 6 HOH 246 2246 2246 HOH HOH A . M 6 HOH 247 2247 2247 HOH HOH A . M 6 HOH 248 2248 2248 HOH HOH A . M 6 HOH 249 2249 2249 HOH HOH A . M 6 HOH 250 2250 2250 HOH HOH A . M 6 HOH 251 2251 2251 HOH HOH A . M 6 HOH 252 2252 2252 HOH HOH A . M 6 HOH 253 2253 2253 HOH HOH A . M 6 HOH 254 2254 2254 HOH HOH A . M 6 HOH 255 2255 2255 HOH HOH A . M 6 HOH 256 2256 2256 HOH HOH A . M 6 HOH 257 2257 2257 HOH HOH A . M 6 HOH 258 2258 2258 HOH HOH A . M 6 HOH 259 2259 2259 HOH HOH A . M 6 HOH 260 2260 2260 HOH HOH A . M 6 HOH 261 2261 2261 HOH HOH A . M 6 HOH 262 2262 2262 HOH HOH A . M 6 HOH 263 2263 2263 HOH HOH A . M 6 HOH 264 2264 2264 HOH HOH A . M 6 HOH 265 2265 2265 HOH HOH A . M 6 HOH 266 2266 2266 HOH HOH A . M 6 HOH 267 2267 2267 HOH HOH A . M 6 HOH 268 2268 2268 HOH HOH A . M 6 HOH 269 2269 2269 HOH HOH A . M 6 HOH 270 2270 2270 HOH HOH A . M 6 HOH 271 2271 2271 HOH HOH A . M 6 HOH 272 2272 2272 HOH HOH A . M 6 HOH 273 2273 2273 HOH HOH A . M 6 HOH 274 2274 2274 HOH HOH A . M 6 HOH 275 2275 2275 HOH HOH A . M 6 HOH 276 2276 2276 HOH HOH A . M 6 HOH 277 2277 2277 HOH HOH A . M 6 HOH 278 2278 2278 HOH HOH A . M 6 HOH 279 2279 2279 HOH HOH A . M 6 HOH 280 2280 2280 HOH HOH A . M 6 HOH 281 2281 2281 HOH HOH A . M 6 HOH 282 2282 2282 HOH HOH A . M 6 HOH 283 2283 2283 HOH HOH A . M 6 HOH 284 2284 2284 HOH HOH A . M 6 HOH 285 2285 2285 HOH HOH A . M 6 HOH 286 2286 2286 HOH HOH A . M 6 HOH 287 2287 2287 HOH HOH A . M 6 HOH 288 2288 2288 HOH HOH A . M 6 HOH 289 2289 2289 HOH HOH A . M 6 HOH 290 2290 2290 HOH HOH A . M 6 HOH 291 2291 2291 HOH HOH A . M 6 HOH 292 2292 2292 HOH HOH A . M 6 HOH 293 2293 2293 HOH HOH A . M 6 HOH 294 2294 2294 HOH HOH A . M 6 HOH 295 2295 2295 HOH HOH A . M 6 HOH 296 2296 2296 HOH HOH A . M 6 HOH 297 2297 2297 HOH HOH A . M 6 HOH 298 2298 2298 HOH HOH A . M 6 HOH 299 2299 2299 HOH HOH A . M 6 HOH 300 2300 2300 HOH HOH A . M 6 HOH 301 2301 2301 HOH HOH A . M 6 HOH 302 2302 2302 HOH HOH A . M 6 HOH 303 2303 2303 HOH HOH A . M 6 HOH 304 2304 2304 HOH HOH A . M 6 HOH 305 2305 2305 HOH HOH A . M 6 HOH 306 2306 2306 HOH HOH A . M 6 HOH 307 2307 2307 HOH HOH A . M 6 HOH 308 2308 2308 HOH HOH A . M 6 HOH 309 2309 2309 HOH HOH A . M 6 HOH 310 2310 2310 HOH HOH A . M 6 HOH 311 2311 2311 HOH HOH A . M 6 HOH 312 2312 2312 HOH HOH A . M 6 HOH 313 2313 2313 HOH HOH A . M 6 HOH 314 2314 2314 HOH HOH A . M 6 HOH 315 2315 2315 HOH HOH A . M 6 HOH 316 2316 2316 HOH HOH A . M 6 HOH 317 2317 2317 HOH HOH A . M 6 HOH 318 2318 2318 HOH HOH A . M 6 HOH 319 2319 2319 HOH HOH A . M 6 HOH 320 2320 2320 HOH HOH A . M 6 HOH 321 2321 2321 HOH HOH A . M 6 HOH 322 2322 2322 HOH HOH A . M 6 HOH 323 2323 2323 HOH HOH A . M 6 HOH 324 2324 2324 HOH HOH A . M 6 HOH 325 2325 2325 HOH HOH A . M 6 HOH 326 2326 2326 HOH HOH A . M 6 HOH 327 2327 2327 HOH HOH A . M 6 HOH 328 2328 2328 HOH HOH A . M 6 HOH 329 2329 2329 HOH HOH A . M 6 HOH 330 2330 2330 HOH HOH A . M 6 HOH 331 2331 2331 HOH HOH A . M 6 HOH 332 2332 2332 HOH HOH A . M 6 HOH 333 2333 2333 HOH HOH A . N 6 HOH 1 2001 2001 HOH HOH B . N 6 HOH 2 2002 2002 HOH HOH B . N 6 HOH 3 2003 2003 HOH HOH B . N 6 HOH 4 2004 2004 HOH HOH B . N 6 HOH 5 2005 2005 HOH HOH B . N 6 HOH 6 2006 2006 HOH HOH B . N 6 HOH 7 2007 2007 HOH HOH B . N 6 HOH 8 2008 2008 HOH HOH B . N 6 HOH 9 2009 2009 HOH HOH B . N 6 HOH 10 2010 2010 HOH HOH B . N 6 HOH 11 2011 2011 HOH HOH B . N 6 HOH 12 2012 2012 HOH HOH B . N 6 HOH 13 2013 2013 HOH HOH B . N 6 HOH 14 2014 2014 HOH HOH B . N 6 HOH 15 2015 2015 HOH HOH B . N 6 HOH 16 2016 2016 HOH HOH B . N 6 HOH 17 2017 2017 HOH HOH B . N 6 HOH 18 2018 2018 HOH HOH B . N 6 HOH 19 2019 2019 HOH HOH B . N 6 HOH 20 2020 2020 HOH HOH B . N 6 HOH 21 2021 2021 HOH HOH B . N 6 HOH 22 2022 2022 HOH HOH B . N 6 HOH 23 2023 2023 HOH HOH B . N 6 HOH 24 2024 2024 HOH HOH B . N 6 HOH 25 2025 2025 HOH HOH B . N 6 HOH 26 2026 2026 HOH HOH B . N 6 HOH 27 2027 2027 HOH HOH B . N 6 HOH 28 2028 2028 HOH HOH B . N 6 HOH 29 2029 2029 HOH HOH B . N 6 HOH 30 2030 2030 HOH HOH B . N 6 HOH 31 2031 2031 HOH HOH B . N 6 HOH 32 2032 2032 HOH HOH B . N 6 HOH 33 2033 2033 HOH HOH B . N 6 HOH 34 2034 2034 HOH HOH B . N 6 HOH 35 2035 2035 HOH HOH B . N 6 HOH 36 2036 2036 HOH HOH B . N 6 HOH 37 2037 2037 HOH HOH B . N 6 HOH 38 2038 2038 HOH HOH B . N 6 HOH 39 2039 2039 HOH HOH B . N 6 HOH 40 2040 2040 HOH HOH B . N 6 HOH 41 2041 2041 HOH HOH B . N 6 HOH 42 2042 2042 HOH HOH B . N 6 HOH 43 2043 2043 HOH HOH B . N 6 HOH 44 2044 2044 HOH HOH B . N 6 HOH 45 2045 2045 HOH HOH B . N 6 HOH 46 2046 2046 HOH HOH B . N 6 HOH 47 2047 2047 HOH HOH B . N 6 HOH 48 2048 2048 HOH HOH B . N 6 HOH 49 2049 2049 HOH HOH B . N 6 HOH 50 2050 2050 HOH HOH B . N 6 HOH 51 2051 2051 HOH HOH B . N 6 HOH 52 2052 2052 HOH HOH B . N 6 HOH 53 2053 2053 HOH HOH B . N 6 HOH 54 2054 2054 HOH HOH B . N 6 HOH 55 2055 2055 HOH HOH B . N 6 HOH 56 2056 2056 HOH HOH B . N 6 HOH 57 2057 2057 HOH HOH B . N 6 HOH 58 2058 2058 HOH HOH B . N 6 HOH 59 2059 2059 HOH HOH B . N 6 HOH 60 2060 2060 HOH HOH B . N 6 HOH 61 2061 2061 HOH HOH B . N 6 HOH 62 2062 2062 HOH HOH B . N 6 HOH 63 2063 2063 HOH HOH B . N 6 HOH 64 2064 2064 HOH HOH B . N 6 HOH 65 2065 2065 HOH HOH B . N 6 HOH 66 2066 2066 HOH HOH B . N 6 HOH 67 2067 2067 HOH HOH B . N 6 HOH 68 2068 2068 HOH HOH B . N 6 HOH 69 2069 2069 HOH HOH B . N 6 HOH 70 2070 2070 HOH HOH B . N 6 HOH 71 2071 2071 HOH HOH B . N 6 HOH 72 2072 2072 HOH HOH B . N 6 HOH 73 2073 2073 HOH HOH B . N 6 HOH 74 2074 2074 HOH HOH B . N 6 HOH 75 2075 2075 HOH HOH B . N 6 HOH 76 2076 2076 HOH HOH B . N 6 HOH 77 2077 2077 HOH HOH B . N 6 HOH 78 2078 2078 HOH HOH B . N 6 HOH 79 2079 2079 HOH HOH B . N 6 HOH 80 2080 2080 HOH HOH B . N 6 HOH 81 2081 2081 HOH HOH B . N 6 HOH 82 2082 2082 HOH HOH B . N 6 HOH 83 2083 2083 HOH HOH B . N 6 HOH 84 2084 2084 HOH HOH B . N 6 HOH 85 2085 2085 HOH HOH B . N 6 HOH 86 2086 2086 HOH HOH B . N 6 HOH 87 2087 2087 HOH HOH B . N 6 HOH 88 2088 2088 HOH HOH B . N 6 HOH 89 2089 2089 HOH HOH B . N 6 HOH 90 2090 2090 HOH HOH B . N 6 HOH 91 2091 2091 HOH HOH B . N 6 HOH 92 2092 2092 HOH HOH B . N 6 HOH 93 2093 2093 HOH HOH B . N 6 HOH 94 2094 2094 HOH HOH B . N 6 HOH 95 2095 2095 HOH HOH B . N 6 HOH 96 2096 2096 HOH HOH B . N 6 HOH 97 2097 2097 HOH HOH B . N 6 HOH 98 2098 2098 HOH HOH B . N 6 HOH 99 2099 2099 HOH HOH B . N 6 HOH 100 2100 2100 HOH HOH B . N 6 HOH 101 2101 2101 HOH HOH B . N 6 HOH 102 2102 2102 HOH HOH B . N 6 HOH 103 2103 2103 HOH HOH B . N 6 HOH 104 2104 2104 HOH HOH B . N 6 HOH 105 2105 2105 HOH HOH B . N 6 HOH 106 2106 2106 HOH HOH B . N 6 HOH 107 2107 2107 HOH HOH B . N 6 HOH 108 2108 2108 HOH HOH B . N 6 HOH 109 2109 2109 HOH HOH B . N 6 HOH 110 2110 2110 HOH HOH B . N 6 HOH 111 2111 2111 HOH HOH B . N 6 HOH 112 2112 2112 HOH HOH B . N 6 HOH 113 2113 2113 HOH HOH B . N 6 HOH 114 2114 2114 HOH HOH B . N 6 HOH 115 2115 2115 HOH HOH B . N 6 HOH 116 2116 2116 HOH HOH B . N 6 HOH 117 2117 2117 HOH HOH B . N 6 HOH 118 2118 2118 HOH HOH B . N 6 HOH 119 2119 2119 HOH HOH B . N 6 HOH 120 2120 2120 HOH HOH B . N 6 HOH 121 2121 2121 HOH HOH B . N 6 HOH 122 2122 2122 HOH HOH B . N 6 HOH 123 2123 2123 HOH HOH B . N 6 HOH 124 2124 2124 HOH HOH B . N 6 HOH 125 2125 2125 HOH HOH B . N 6 HOH 126 2126 2126 HOH HOH B . N 6 HOH 127 2127 2127 HOH HOH B . N 6 HOH 128 2128 2128 HOH HOH B . N 6 HOH 129 2129 2129 HOH HOH B . N 6 HOH 130 2130 2130 HOH HOH B . N 6 HOH 131 2131 2131 HOH HOH B . N 6 HOH 132 2132 2132 HOH HOH B . N 6 HOH 133 2133 2133 HOH HOH B . N 6 HOH 134 2134 2134 HOH HOH B . N 6 HOH 135 2135 2135 HOH HOH B . N 6 HOH 136 2136 2136 HOH HOH B . N 6 HOH 137 2137 2137 HOH HOH B . N 6 HOH 138 2138 2138 HOH HOH B . N 6 HOH 139 2139 2139 HOH HOH B . N 6 HOH 140 2140 2140 HOH HOH B . N 6 HOH 141 2141 2141 HOH HOH B . N 6 HOH 142 2142 2142 HOH HOH B . N 6 HOH 143 2143 2143 HOH HOH B . N 6 HOH 144 2144 2144 HOH HOH B . N 6 HOH 145 2145 2145 HOH HOH B . N 6 HOH 146 2146 2146 HOH HOH B . N 6 HOH 147 2147 2147 HOH HOH B . N 6 HOH 148 2148 2148 HOH HOH B . N 6 HOH 149 2149 2149 HOH HOH B . N 6 HOH 150 2150 2150 HOH HOH B . N 6 HOH 151 2151 2151 HOH HOH B . N 6 HOH 152 2152 2152 HOH HOH B . N 6 HOH 153 2153 2153 HOH HOH B . N 6 HOH 154 2154 2154 HOH HOH B . N 6 HOH 155 2155 2155 HOH HOH B . N 6 HOH 156 2156 2156 HOH HOH B . N 6 HOH 157 2157 2157 HOH HOH B . N 6 HOH 158 2158 2158 HOH HOH B . N 6 HOH 159 2159 2159 HOH HOH B . N 6 HOH 160 2160 2160 HOH HOH B . N 6 HOH 161 2161 2161 HOH HOH B . N 6 HOH 162 2162 2162 HOH HOH B . N 6 HOH 163 2163 2163 HOH HOH B . N 6 HOH 164 2164 2164 HOH HOH B . N 6 HOH 165 2165 2165 HOH HOH B . N 6 HOH 166 2166 2166 HOH HOH B . N 6 HOH 167 2167 2167 HOH HOH B . N 6 HOH 168 2168 2168 HOH HOH B . N 6 HOH 169 2169 2169 HOH HOH B . N 6 HOH 170 2170 2170 HOH HOH B . N 6 HOH 171 2171 2171 HOH HOH B . N 6 HOH 172 2172 2172 HOH HOH B . N 6 HOH 173 2173 2173 HOH HOH B . N 6 HOH 174 2174 2174 HOH HOH B . N 6 HOH 175 2175 2175 HOH HOH B . N 6 HOH 176 2176 2176 HOH HOH B . N 6 HOH 177 2177 2177 HOH HOH B . N 6 HOH 178 2178 2178 HOH HOH B . N 6 HOH 179 2179 2179 HOH HOH B . N 6 HOH 180 2180 2180 HOH HOH B . N 6 HOH 181 2181 2181 HOH HOH B . N 6 HOH 182 2182 2182 HOH HOH B . N 6 HOH 183 2183 2183 HOH HOH B . N 6 HOH 184 2184 2184 HOH HOH B . N 6 HOH 185 2185 2185 HOH HOH B . N 6 HOH 186 2186 2186 HOH HOH B . N 6 HOH 187 2187 2187 HOH HOH B . N 6 HOH 188 2188 2188 HOH HOH B . N 6 HOH 189 2189 2189 HOH HOH B . N 6 HOH 190 2190 2190 HOH HOH B . N 6 HOH 191 2191 2191 HOH HOH B . N 6 HOH 192 2192 2192 HOH HOH B . N 6 HOH 193 2193 2193 HOH HOH B . N 6 HOH 194 2194 2194 HOH HOH B . N 6 HOH 195 2195 2195 HOH HOH B . N 6 HOH 196 2196 2196 HOH HOH B . N 6 HOH 197 2197 2197 HOH HOH B . N 6 HOH 198 2198 2198 HOH HOH B . N 6 HOH 199 2199 2199 HOH HOH B . N 6 HOH 200 2200 2200 HOH HOH B . N 6 HOH 201 2201 2201 HOH HOH B . N 6 HOH 202 2202 2202 HOH HOH B . N 6 HOH 203 2203 2203 HOH HOH B . N 6 HOH 204 2204 2204 HOH HOH B . N 6 HOH 205 2205 2205 HOH HOH B . N 6 HOH 206 2206 2206 HOH HOH B . N 6 HOH 207 2207 2207 HOH HOH B . N 6 HOH 208 2208 2208 HOH HOH B . N 6 HOH 209 2209 2209 HOH HOH B . N 6 HOH 210 2210 2210 HOH HOH B . N 6 HOH 211 2211 2211 HOH HOH B . N 6 HOH 212 2212 2212 HOH HOH B . N 6 HOH 213 2213 2213 HOH HOH B . N 6 HOH 214 2214 2214 HOH HOH B . N 6 HOH 215 2215 2215 HOH HOH B . N 6 HOH 216 2216 2216 HOH HOH B . N 6 HOH 217 2217 2217 HOH HOH B . N 6 HOH 218 2218 2218 HOH HOH B . N 6 HOH 219 2219 2219 HOH HOH B . N 6 HOH 220 2220 2220 HOH HOH B . N 6 HOH 221 2221 2221 HOH HOH B . N 6 HOH 222 2222 2222 HOH HOH B . N 6 HOH 223 2223 2223 HOH HOH B . N 6 HOH 224 2224 2224 HOH HOH B . N 6 HOH 225 2225 2225 HOH HOH B . N 6 HOH 226 2226 2226 HOH HOH B . N 6 HOH 227 2227 2227 HOH HOH B . N 6 HOH 228 2228 2228 HOH HOH B . N 6 HOH 229 2229 2229 HOH HOH B . N 6 HOH 230 2230 2230 HOH HOH B . N 6 HOH 231 2231 2231 HOH HOH B . N 6 HOH 232 2232 2232 HOH HOH B . N 6 HOH 233 2233 2233 HOH HOH B . N 6 HOH 234 2234 2234 HOH HOH B . N 6 HOH 235 2235 2235 HOH HOH B . N 6 HOH 236 2236 2236 HOH HOH B . N 6 HOH 237 2237 2237 HOH HOH B . N 6 HOH 238 2238 2238 HOH HOH B . N 6 HOH 239 2239 2239 HOH HOH B . N 6 HOH 240 2240 2240 HOH HOH B . N 6 HOH 241 2241 2241 HOH HOH B . N 6 HOH 242 2242 2242 HOH HOH B . N 6 HOH 243 2243 2243 HOH HOH B . N 6 HOH 244 2244 2244 HOH HOH B . N 6 HOH 245 2245 2245 HOH HOH B . N 6 HOH 246 2246 2246 HOH HOH B . N 6 HOH 247 2247 2247 HOH HOH B . N 6 HOH 248 2248 2248 HOH HOH B . N 6 HOH 249 2249 2249 HOH HOH B . N 6 HOH 250 2250 2250 HOH HOH B . N 6 HOH 251 2251 2251 HOH HOH B . N 6 HOH 252 2252 2252 HOH HOH B . N 6 HOH 253 2253 2253 HOH HOH B . N 6 HOH 254 2254 2254 HOH HOH B . N 6 HOH 255 2255 2255 HOH HOH B . N 6 HOH 256 2256 2256 HOH HOH B . N 6 HOH 257 2257 2257 HOH HOH B . N 6 HOH 258 2258 2258 HOH HOH B . N 6 HOH 259 2259 2259 HOH HOH B . N 6 HOH 260 2260 2260 HOH HOH B . N 6 HOH 261 2261 2261 HOH HOH B . N 6 HOH 262 2262 2262 HOH HOH B . N 6 HOH 263 2263 2263 HOH HOH B . N 6 HOH 264 2264 2264 HOH HOH B . N 6 HOH 265 2265 2265 HOH HOH B . N 6 HOH 266 2266 2266 HOH HOH B . N 6 HOH 267 2267 2267 HOH HOH B . N 6 HOH 268 2268 2268 HOH HOH B . N 6 HOH 269 2269 2269 HOH HOH B . N 6 HOH 270 2270 2270 HOH HOH B . N 6 HOH 271 2271 2271 HOH HOH B . N 6 HOH 272 2272 2272 HOH HOH B . N 6 HOH 273 2273 2273 HOH HOH B . N 6 HOH 274 2274 2274 HOH HOH B . N 6 HOH 275 2275 2275 HOH HOH B . N 6 HOH 276 2276 2276 HOH HOH B . N 6 HOH 277 2277 2277 HOH HOH B . N 6 HOH 278 2278 2278 HOH HOH B . N 6 HOH 279 2279 2279 HOH HOH B . N 6 HOH 280 2280 2280 HOH HOH B . N 6 HOH 281 2281 2281 HOH HOH B . N 6 HOH 282 2282 2282 HOH HOH B . N 6 HOH 283 2283 2283 HOH HOH B . N 6 HOH 284 2284 2284 HOH HOH B . N 6 HOH 285 2285 2285 HOH HOH B . N 6 HOH 286 2286 2286 HOH HOH B . N 6 HOH 287 2287 2287 HOH HOH B . N 6 HOH 288 2288 2288 HOH HOH B . N 6 HOH 289 2289 2289 HOH HOH B . N 6 HOH 290 2290 2290 HOH HOH B . N 6 HOH 291 2291 2291 HOH HOH B . N 6 HOH 292 2292 2292 HOH HOH B . N 6 HOH 293 2293 2293 HOH HOH B . N 6 HOH 294 2294 2294 HOH HOH B . N 6 HOH 295 2295 2295 HOH HOH B . N 6 HOH 296 2296 2296 HOH HOH B . N 6 HOH 297 2297 2297 HOH HOH B . N 6 HOH 298 2298 2298 HOH HOH B . N 6 HOH 299 2299 2299 HOH HOH B . N 6 HOH 300 2300 2300 HOH HOH B . N 6 HOH 301 2301 2301 HOH HOH B . N 6 HOH 302 2302 2302 HOH HOH B . N 6 HOH 303 2303 2303 HOH HOH B . N 6 HOH 304 2304 2304 HOH HOH B . N 6 HOH 305 2305 2305 HOH HOH B . N 6 HOH 306 2306 2306 HOH HOH B . N 6 HOH 307 2307 2307 HOH HOH B . N 6 HOH 308 2308 2308 HOH HOH B . N 6 HOH 309 2309 2309 HOH HOH 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 A ASN 247 A ASN 247 ? ASN 'GLYCOSYLATION SITE' 2 B ASN 247 B ASN 247 ? ASN 'GLYCOSYLATION SITE' 3 A PCA 1 A PCA 1 ? GLU 'PYROGLUTAMIC ACID' 4 B PCA 1 B PCA 1 ? GLU 'PYROGLUTAMIC ACID' # loop_ _pdbx_struct_assembly.id _pdbx_struct_assembly.details _pdbx_struct_assembly.method_details _pdbx_struct_assembly.oligomeric_details _pdbx_struct_assembly.oligomeric_count 1 author_and_software_defined_assembly PQS monomeric 1 2 author_and_software_defined_assembly PQS monomeric 1 # loop_ _pdbx_struct_assembly_gen.assembly_id _pdbx_struct_assembly_gen.oper_expression _pdbx_struct_assembly_gen.asym_id_list 1 1 A,C,D,E,F,G,M 2 1 B,H,I,J,K,L,N # _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 2004-01-07 2 'Structure model' 1 1 2011-05-08 3 'Structure model' 1 2 2011-07-13 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Version format compliance' 2 3 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.1.9999 ? 1 DENZO 'data reduction' . ? 2 SCALEPACK 'data scaling' . ? 3 AMoRE phasing . ? 4 # _pdbx_database_remark.id 700 _pdbx_database_remark.text ; SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. ; # _pdbx_entry_details.entry_id 1OJJ _pdbx_entry_details.compound_details ;ENGINEERED RESIDUE GLU 197 SER N-LINKED N-ACETYLGLUCOSAMINE ON RESIDUE ASN 247, PYROGLUTAMATE POST-TRANSLATIONAL MODIFICATION ON RESIDUE 1 ; _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details ;PYROGLUTAMATE POST-TRANSLATIONAL MODIFICATION AT RESIDUE 1, MUTATION E197S, MISSING LAST FOUR RESIDUES. ; # _pdbx_validate_symm_contact.id 1 _pdbx_validate_symm_contact.PDB_model_num 1 _pdbx_validate_symm_contact.auth_atom_id_1 NZ _pdbx_validate_symm_contact.auth_asym_id_1 A _pdbx_validate_symm_contact.auth_comp_id_1 LYS _pdbx_validate_symm_contact.auth_seq_id_1 159 _pdbx_validate_symm_contact.PDB_ins_code_1 ? _pdbx_validate_symm_contact.label_alt_id_1 ? _pdbx_validate_symm_contact.site_symmetry_1 1_555 _pdbx_validate_symm_contact.auth_atom_id_2 OE2 _pdbx_validate_symm_contact.auth_asym_id_2 A _pdbx_validate_symm_contact.auth_comp_id_2 GLU _pdbx_validate_symm_contact.auth_seq_id_2 316 _pdbx_validate_symm_contact.PDB_ins_code_2 ? _pdbx_validate_symm_contact.label_alt_id_2 ? _pdbx_validate_symm_contact.site_symmetry_2 2_555 _pdbx_validate_symm_contact.dist 1.96 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 VAL A 104 ? ? -119.78 75.82 2 1 LYS A 137 ? ? -94.83 30.54 3 1 CYS A 140 ? ? -39.73 135.16 4 1 ASN A 300 ? ? -143.95 38.81 5 1 ALA A 328 ? ? 62.52 -166.64 6 1 ASP A 358 ? ? -143.86 13.06 7 1 VAL B 104 ? ? -117.71 78.07 8 1 LYS B 116 ? ? 68.99 -0.29 9 1 LYS B 137 ? ? -96.30 31.07 10 1 ASN B 300 ? ? -145.84 49.29 11 1 ALA B 328 ? ? 61.35 -164.63 12 1 ASP B 358 ? ? -141.65 12.85 # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 A GLN 399 ? CA ? A GLN 399 CA 2 1 Y 1 A GLN 399 ? C ? A GLN 399 C 3 1 Y 1 A GLN 399 ? O ? A GLN 399 O 4 1 Y 1 A GLN 399 ? CB ? A GLN 399 CB 5 1 Y 1 A GLN 399 ? CG ? A GLN 399 CG 6 1 Y 1 A GLN 399 ? CD ? A GLN 399 CD 7 1 Y 1 A GLN 399 ? OE1 ? A GLN 399 OE1 8 1 Y 1 A GLN 399 ? NE2 ? A GLN 399 NE2 9 1 Y 1 B GLN 399 ? CA ? B GLN 399 CA 10 1 Y 1 B GLN 399 ? C ? B GLN 399 C 11 1 Y 1 B GLN 399 ? O ? B GLN 399 O 12 1 Y 1 B GLN 399 ? CB ? B GLN 399 CB 13 1 Y 1 B GLN 399 ? CG ? B GLN 399 CG 14 1 Y 1 B GLN 399 ? CD ? B GLN 399 CD 15 1 Y 1 B GLN 399 ? OE1 ? B GLN 399 OE1 16 1 Y 1 B GLN 399 ? NE2 ? B GLN 399 NE2 # 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 GLU 400 ? A GLU 400 2 1 Y 1 A LEU 401 ? A LEU 401 3 1 Y 1 A GLN 402 ? A GLN 402 4 1 Y 1 B GLU 400 ? B GLU 400 5 1 Y 1 B LEU 401 ? B LEU 401 6 1 Y 1 B GLN 402 ? B GLN 402 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 BETA-D-GLUCOSE BGC 3 BETA-D-GALACTOSE GAL 4 ALPHA-D-GLUCOSE GLC 5 N-ACETYL-D-GLUCOSAMINE NAG 6 water HOH #