data_3QQB # _entry.id 3QQB # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.287 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 3QQB RCSB RCSB063968 WWPDB D_1000063968 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 3QQE . unspecified PDB 3QQI . unspecified PDB 3QQO . unspecified # _pdbx_database_status.entry_id 3QQB _pdbx_database_status.status_code REL _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.recvd_initial_deposition_date 2011-02-15 _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Xu, R.' 1 'Wilson, I.A.' 2 # _citation.id primary _citation.title 'Structural Characterization of an Early Fusion Intermediate of Influenza Virus Hemagglutinin.' _citation.journal_abbrev J.Virol. _citation.journal_volume 85 _citation.page_first 5172 _citation.page_last 5182 _citation.year 2011 _citation.journal_id_ASTM JOVIAM _citation.country US _citation.journal_id_ISSN 0022-538X _citation.journal_id_CSD 0825 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 21367895 _citation.pdbx_database_id_DOI 10.1128/JVI.02430-10 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Xu, R.' 1 primary 'Wilson, I.A.' 2 # _cell.entry_id 3QQB _cell.length_a 70.288 _cell.length_b 70.288 _cell.length_c 237.136 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 6 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 3QQB _symmetry.space_group_name_H-M 'P 63' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 173 _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man Hemagglutinin 36504.227 1 ? ? 'HA1 chain' ? 2 polymer man Hemagglutinin 20120.248 1 ? R106H 'HA2 chain ectodomain' ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? 4 non-polymer syn 1,2-ETHANEDIOL 62.068 1 ? ? ? ? 5 non-polymer syn 'DI(HYDROXYETHYL)ETHER' 106.120 1 ? ? ? ? 6 water nat water 18.015 540 ? ? ? ? # loop_ _entity_poly.entity_id _entity_poly.type _entity_poly.nstd_linkage _entity_poly.nstd_monomer _entity_poly.pdbx_seq_one_letter_code _entity_poly.pdbx_seq_one_letter_code_can _entity_poly.pdbx_strand_id _entity_poly.pdbx_target_identifier 1 'polypeptide(L)' no no ;PGDQICIGYHANNSTEKVDTILERNVTVTHAKDILEKTHNGKLCKLNGIPPLELGDCSIAGWLLGNPECDRLLSVPEWSY IMEKENPRDGLCYPGSFNDYEELKHLLSSVKHFEKVKILPKDRWTQHTTTGGSRACAVSGNPSFFRNMVWLTEKGSNYPV AKGSYNNTSGEQMLIIWGVHHPNDETEQRTLYQNVGTYVSVGTSTLNKRSTPEIATRPKVNGQGGRMEFSWTLLDMWDTI NFESTGNLIAPEYGFKISKRGSSGIMKTEGTLENCETKCQTPLGAINTTLPFHNVHPLTIGECPKYVKSEKLVLATGLRN VPQIESR ; ;PGDQICIGYHANNSTEKVDTILERNVTVTHAKDILEKTHNGKLCKLNGIPPLELGDCSIAGWLLGNPECDRLLSVPEWSY IMEKENPRDGLCYPGSFNDYEELKHLLSSVKHFEKVKILPKDRWTQHTTTGGSRACAVSGNPSFFRNMVWLTEKGSNYPV AKGSYNNTSGEQMLIIWGVHHPNDETEQRTLYQNVGTYVSVGTSTLNKRSTPEIATRPKVNGQGGRMEFSWTLLDMWDTI NFESTGNLIAPEYGFKISKRGSSGIMKTEGTLENCETKCQTPLGAINTTLPFHNVHPLTIGECPKYVKSEKLVLATGLRN VPQIESR ; A ? 2 'polypeptide(L)' no no ;GLFGAIAGFIEGGWQGMVDGWYGYHHSNDQGSGYAADKESTQKAFDGITNKVNSVIEKMNTQFEAVGKEFSNLERRLENL NKKMEDGFLDVWTYNAELLVLMENEHTLDFHDSNVKNLYDKVRMQLRDNVKELGNGCFEFYHKCDDECMNSVKNGTYDYP KYEEESKLNRNEIK ; ;GLFGAIAGFIEGGWQGMVDGWYGYHHSNDQGSGYAADKESTQKAFDGITNKVNSVIEKMNTQFEAVGKEFSNLERRLENL NKKMEDGFLDVWTYNAELLVLMENEHTLDFHDSNVKNLYDKVRMQLRDNVKELGNGCFEFYHKCDDECMNSVKNGTYDYP KYEEESKLNRNEIK ; B ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 PRO n 1 2 GLY n 1 3 ASP n 1 4 GLN n 1 5 ILE n 1 6 CYS n 1 7 ILE n 1 8 GLY n 1 9 TYR n 1 10 HIS n 1 11 ALA n 1 12 ASN n 1 13 ASN n 1 14 SER n 1 15 THR n 1 16 GLU n 1 17 LYS n 1 18 VAL n 1 19 ASP n 1 20 THR n 1 21 ILE n 1 22 LEU n 1 23 GLU n 1 24 ARG n 1 25 ASN n 1 26 VAL n 1 27 THR n 1 28 VAL n 1 29 THR n 1 30 HIS n 1 31 ALA n 1 32 LYS n 1 33 ASP n 1 34 ILE n 1 35 LEU n 1 36 GLU n 1 37 LYS n 1 38 THR n 1 39 HIS n 1 40 ASN n 1 41 GLY n 1 42 LYS n 1 43 LEU n 1 44 CYS n 1 45 LYS n 1 46 LEU n 1 47 ASN n 1 48 GLY n 1 49 ILE n 1 50 PRO n 1 51 PRO n 1 52 LEU n 1 53 GLU n 1 54 LEU n 1 55 GLY n 1 56 ASP n 1 57 CYS n 1 58 SER n 1 59 ILE n 1 60 ALA n 1 61 GLY n 1 62 TRP n 1 63 LEU n 1 64 LEU n 1 65 GLY n 1 66 ASN n 1 67 PRO n 1 68 GLU n 1 69 CYS n 1 70 ASP n 1 71 ARG n 1 72 LEU n 1 73 LEU n 1 74 SER n 1 75 VAL n 1 76 PRO n 1 77 GLU n 1 78 TRP n 1 79 SER n 1 80 TYR n 1 81 ILE n 1 82 MET n 1 83 GLU n 1 84 LYS n 1 85 GLU n 1 86 ASN n 1 87 PRO n 1 88 ARG n 1 89 ASP n 1 90 GLY n 1 91 LEU n 1 92 CYS n 1 93 TYR n 1 94 PRO n 1 95 GLY n 1 96 SER n 1 97 PHE n 1 98 ASN n 1 99 ASP n 1 100 TYR n 1 101 GLU n 1 102 GLU n 1 103 LEU n 1 104 LYS n 1 105 HIS n 1 106 LEU n 1 107 LEU n 1 108 SER n 1 109 SER n 1 110 VAL n 1 111 LYS n 1 112 HIS n 1 113 PHE n 1 114 GLU n 1 115 LYS n 1 116 VAL n 1 117 LYS n 1 118 ILE n 1 119 LEU n 1 120 PRO n 1 121 LYS n 1 122 ASP n 1 123 ARG n 1 124 TRP n 1 125 THR n 1 126 GLN n 1 127 HIS n 1 128 THR n 1 129 THR n 1 130 THR n 1 131 GLY n 1 132 GLY n 1 133 SER n 1 134 ARG n 1 135 ALA n 1 136 CYS n 1 137 ALA n 1 138 VAL n 1 139 SER n 1 140 GLY n 1 141 ASN n 1 142 PRO n 1 143 SER n 1 144 PHE n 1 145 PHE n 1 146 ARG n 1 147 ASN n 1 148 MET n 1 149 VAL n 1 150 TRP n 1 151 LEU n 1 152 THR n 1 153 GLU n 1 154 LYS n 1 155 GLY n 1 156 SER n 1 157 ASN n 1 158 TYR n 1 159 PRO n 1 160 VAL n 1 161 ALA n 1 162 LYS n 1 163 GLY n 1 164 SER n 1 165 TYR n 1 166 ASN n 1 167 ASN n 1 168 THR n 1 169 SER n 1 170 GLY n 1 171 GLU n 1 172 GLN n 1 173 MET n 1 174 LEU n 1 175 ILE n 1 176 ILE n 1 177 TRP n 1 178 GLY n 1 179 VAL n 1 180 HIS n 1 181 HIS n 1 182 PRO n 1 183 ASN n 1 184 ASP n 1 185 GLU n 1 186 THR n 1 187 GLU n 1 188 GLN n 1 189 ARG n 1 190 THR n 1 191 LEU n 1 192 TYR n 1 193 GLN n 1 194 ASN n 1 195 VAL n 1 196 GLY n 1 197 THR n 1 198 TYR n 1 199 VAL n 1 200 SER n 1 201 VAL n 1 202 GLY n 1 203 THR n 1 204 SER n 1 205 THR n 1 206 LEU n 1 207 ASN n 1 208 LYS n 1 209 ARG n 1 210 SER n 1 211 THR n 1 212 PRO n 1 213 GLU n 1 214 ILE n 1 215 ALA n 1 216 THR n 1 217 ARG n 1 218 PRO n 1 219 LYS n 1 220 VAL n 1 221 ASN n 1 222 GLY n 1 223 GLN n 1 224 GLY n 1 225 GLY n 1 226 ARG n 1 227 MET n 1 228 GLU n 1 229 PHE n 1 230 SER n 1 231 TRP n 1 232 THR n 1 233 LEU n 1 234 LEU n 1 235 ASP n 1 236 MET n 1 237 TRP n 1 238 ASP n 1 239 THR n 1 240 ILE n 1 241 ASN n 1 242 PHE n 1 243 GLU n 1 244 SER n 1 245 THR n 1 246 GLY n 1 247 ASN n 1 248 LEU n 1 249 ILE n 1 250 ALA n 1 251 PRO n 1 252 GLU n 1 253 TYR n 1 254 GLY n 1 255 PHE n 1 256 LYS n 1 257 ILE n 1 258 SER n 1 259 LYS n 1 260 ARG n 1 261 GLY n 1 262 SER n 1 263 SER n 1 264 GLY n 1 265 ILE n 1 266 MET n 1 267 LYS n 1 268 THR n 1 269 GLU n 1 270 GLY n 1 271 THR n 1 272 LEU n 1 273 GLU n 1 274 ASN n 1 275 CYS n 1 276 GLU n 1 277 THR n 1 278 LYS n 1 279 CYS n 1 280 GLN n 1 281 THR n 1 282 PRO n 1 283 LEU n 1 284 GLY n 1 285 ALA n 1 286 ILE n 1 287 ASN n 1 288 THR n 1 289 THR n 1 290 LEU n 1 291 PRO n 1 292 PHE n 1 293 HIS n 1 294 ASN n 1 295 VAL n 1 296 HIS n 1 297 PRO n 1 298 LEU n 1 299 THR n 1 300 ILE n 1 301 GLY n 1 302 GLU n 1 303 CYS n 1 304 PRO n 1 305 LYS n 1 306 TYR n 1 307 VAL n 1 308 LYS n 1 309 SER n 1 310 GLU n 1 311 LYS n 1 312 LEU n 1 313 VAL n 1 314 LEU n 1 315 ALA n 1 316 THR n 1 317 GLY n 1 318 LEU n 1 319 ARG n 1 320 ASN n 1 321 VAL n 1 322 PRO n 1 323 GLN n 1 324 ILE n 1 325 GLU n 1 326 SER n 1 327 ARG n 2 1 GLY n 2 2 LEU n 2 3 PHE n 2 4 GLY n 2 5 ALA n 2 6 ILE n 2 7 ALA n 2 8 GLY n 2 9 PHE n 2 10 ILE n 2 11 GLU n 2 12 GLY n 2 13 GLY n 2 14 TRP n 2 15 GLN n 2 16 GLY n 2 17 MET n 2 18 VAL n 2 19 ASP n 2 20 GLY n 2 21 TRP n 2 22 TYR n 2 23 GLY n 2 24 TYR n 2 25 HIS n 2 26 HIS n 2 27 SER n 2 28 ASN n 2 29 ASP n 2 30 GLN n 2 31 GLY n 2 32 SER n 2 33 GLY n 2 34 TYR n 2 35 ALA n 2 36 ALA n 2 37 ASP n 2 38 LYS n 2 39 GLU n 2 40 SER n 2 41 THR n 2 42 GLN n 2 43 LYS n 2 44 ALA n 2 45 PHE n 2 46 ASP n 2 47 GLY n 2 48 ILE n 2 49 THR n 2 50 ASN n 2 51 LYS n 2 52 VAL n 2 53 ASN n 2 54 SER n 2 55 VAL n 2 56 ILE n 2 57 GLU n 2 58 LYS n 2 59 MET n 2 60 ASN n 2 61 THR n 2 62 GLN n 2 63 PHE n 2 64 GLU n 2 65 ALA n 2 66 VAL n 2 67 GLY n 2 68 LYS n 2 69 GLU n 2 70 PHE n 2 71 SER n 2 72 ASN n 2 73 LEU n 2 74 GLU n 2 75 ARG n 2 76 ARG n 2 77 LEU n 2 78 GLU n 2 79 ASN n 2 80 LEU n 2 81 ASN n 2 82 LYS n 2 83 LYS n 2 84 MET n 2 85 GLU n 2 86 ASP n 2 87 GLY n 2 88 PHE n 2 89 LEU n 2 90 ASP n 2 91 VAL n 2 92 TRP n 2 93 THR n 2 94 TYR n 2 95 ASN n 2 96 ALA n 2 97 GLU n 2 98 LEU n 2 99 LEU n 2 100 VAL n 2 101 LEU n 2 102 MET n 2 103 GLU n 2 104 ASN n 2 105 GLU n 2 106 HIS n 2 107 THR n 2 108 LEU n 2 109 ASP n 2 110 PHE n 2 111 HIS n 2 112 ASP n 2 113 SER n 2 114 ASN n 2 115 VAL n 2 116 LYS n 2 117 ASN n 2 118 LEU n 2 119 TYR n 2 120 ASP n 2 121 LYS n 2 122 VAL n 2 123 ARG n 2 124 MET n 2 125 GLN n 2 126 LEU n 2 127 ARG n 2 128 ASP n 2 129 ASN n 2 130 VAL n 2 131 LYS n 2 132 GLU n 2 133 LEU n 2 134 GLY n 2 135 ASN n 2 136 GLY n 2 137 CYS n 2 138 PHE n 2 139 GLU n 2 140 PHE n 2 141 TYR n 2 142 HIS n 2 143 LYS n 2 144 CYS n 2 145 ASP n 2 146 ASP n 2 147 GLU n 2 148 CYS n 2 149 MET n 2 150 ASN n 2 151 SER n 2 152 VAL n 2 153 LYS n 2 154 ASN n 2 155 GLY n 2 156 THR n 2 157 TYR n 2 158 ASP n 2 159 TYR n 2 160 PRO n 2 161 LYS n 2 162 TYR n 2 163 GLU n 2 164 GLU n 2 165 GLU n 2 166 SER n 2 167 LYS n 2 168 LEU n 2 169 ASN n 2 170 ARG n 2 171 ASN n 2 172 GLU n 2 173 ILE n 2 174 LYS n # loop_ _entity_src_gen.entity_id _entity_src_gen.pdbx_src_id _entity_src_gen.pdbx_alt_source_flag _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 _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id _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 _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id _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 1 1 sample ? ? ? ? ? 'HA, hemagglutinin' ? 'A/Japan/305/1957 H2N2' ? ? ? ? 'Influenza A virus' 387161 ? ? ? ? ? ? ? ? 'Trichoplusia ni' 7111 ? ? ? ? ? ? Hi5 ? ? ? ? ? ? ? Baculovirus ? ? ? pFASTbac-HT ? ? 2 1 sample ? ? ? ? ? 'HA, hemagglutinin' ? 'A/Japan/305/1957 H2N2' ? ? ? ? 'Influenza A virus' 387161 ? ? ? ? ? ? ? ? 'Trichoplusia ni' 7111 ? ? ? ? ? ? Hi5 ? ? ? ? ? ? ? Baculovirus ? ? ? pFASTbac-HT ? ? # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.pdbx_db_accession _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_db_isoform 1 UNP C7S226_I57A0 C7S226 1 ;GDQICIGYHANNSTEKVDTILERNVTVTHAKDILEKTHNGKLCKLNGIPPLELGDCSIAGWLLGNPECDRLLSVPEWSYI MEKENPRDGLCYPGSFNDYEELKHLLSSVKHFEKVKILPKDRWTQHTTTGGSRACAVSGNPSFFRNMVWLTEKGSNYPVA KGSYNNTSGEQMLIIWGVHHPNDETEQRTLYQNVGTYVSVGTSTLNKRSTPEIATRPKVNGQGGRMEFSWTLLDMWDTIN FESTGNLIAPEYGFKISKRGSSGIMKTEGTLENCETKCQTPLGAINTTLPFHNVHPLTIGECPKYVKSEKLVLATGLRNV PQIESR ; 15 ? 2 UNP C7S226_I57A0 C7S226 2 ;GLFGAIAGFIEGGWQGMVDGWYGYHHSNDQGSGYAADKESTQKAFDGITNKVNSVIEKMNTQFEAVGKEFSNLERRLENL NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRMQLRDNVKELGNGCFEFYHKCDDECMNSVKNGTYDYP KYEEESKLNRNEIK ; 341 ? # 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 3QQB A 2 ? 327 ? C7S226 15 ? 340 ? 10 329 2 2 3QQB B 1 ? 174 ? C7S226 341 ? 514 ? 1 174 # 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 3QQB PRO A 1 ? UNP C7S226 ? ? 'EXPRESSION TAG' 9 1 2 3QQB HIS B 106 ? UNP C7S226 ARG 446 'ENGINEERED MUTATION' 106 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 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 EDO non-polymer . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL' 'C2 H6 O2' 62.068 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 PEG non-polymer . 'DI(HYDROXYETHYL)ETHER' ? 'C4 H10 O3' 106.120 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 3QQB _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.99 _exptl_crystal.density_percent_sol 58.82 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, SITTING DROP' _exptl_crystal_grow.temp 295.5 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 8.1 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '28% PEG 3000, 0.1M Tris, pH 8.1, VAPOR DIFFUSION, SITTING DROP, temperature 295.5K' # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'MARMOSAIC 325 mm CCD' _diffrn_detector.pdbx_collection_date 2009-01-09 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'Double crystal monochromator' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.91837 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'SSRL BEAMLINE BL9-2' _diffrn_source.pdbx_synchrotron_site SSRL _diffrn_source.pdbx_synchrotron_beamline BL9-2 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 0.91837 # _reflns.entry_id 3QQB _reflns.observed_criterion_sigma_I ? _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 35.0 _reflns.d_resolution_high 1.97 _reflns.number_obs 46401 _reflns.number_all ? _reflns.percent_possible_obs 99.7 _reflns.pdbx_Rmerge_I_obs 0.065 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 16.1 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 8.1 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 # loop_ _reflns_shell.d_res_high _reflns_shell.d_res_low _reflns_shell.percent_possible_all _reflns_shell.Rmerge_I_obs _reflns_shell.pdbx_Rsym_value _reflns_shell.meanI_over_sigI_obs _reflns_shell.pdbx_redundancy _reflns_shell.percent_possible_obs _reflns_shell.number_unique_all _reflns_shell.number_measured_all _reflns_shell.number_measured_obs _reflns_shell.number_unique_obs _reflns_shell.pdbx_chi_squared _reflns_shell.pdbx_diffrn_id _reflns_shell.pdbx_ordinal 1.970 2.040 99.200 0.432 ? ? 5.700 ? ? ? ? ? ? ? 1 2.040 2.120 99.900 0.345 ? ? 7.500 ? ? ? ? ? ? ? 2 2.120 2.220 99.900 0.262 ? ? 8.300 ? ? ? ? ? ? ? 3 2.220 2.340 99.900 0.206 ? ? 8.500 ? ? ? ? ? ? ? 4 2.340 2.480 100.000 0.151 ? ? 8.600 ? ? ? ? ? ? ? 5 2.480 2.670 100.000 0.115 ? ? 8.600 ? ? ? ? ? ? ? 6 2.670 2.940 100.000 0.080 ? ? 8.500 ? ? ? ? ? ? ? 7 2.940 3.370 99.900 0.063 ? ? 8.500 ? ? ? ? ? ? ? 8 3.370 4.240 99.800 0.047 ? ? 8.400 ? ? ? ? ? ? ? 9 4.240 35.000 98.600 0.038 ? ? 8.200 ? ? ? ? ? ? ? 10 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 3QQB _refine.ls_number_reflns_obs 44030 _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 35.00 _refine.ls_d_res_high 1.97 _refine.ls_percent_reflns_obs 99.72 _refine.ls_R_factor_obs 0.18713 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.18504 _refine.ls_R_factor_R_free 0.22680 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.1 _refine.ls_number_reflns_R_free 2346 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min 0.330 _refine.occupancy_max 1.000 _refine.correlation_coeff_Fo_to_Fc 0.961 _refine.correlation_coeff_Fo_to_Fc_free 0.939 _refine.B_iso_mean 37.403 _refine.aniso_B[1][1] 1.06 _refine.aniso_B[2][2] 1.06 _refine.aniso_B[3][3] -1.60 _refine.aniso_B[1][2] 0.53 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.156 _refine.pdbx_overall_ESU_R_Free 0.146 _refine.overall_SU_ML 0.101 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 7.940 _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 3929 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 67 _refine_hist.number_atoms_solvent 540 _refine_hist.number_atoms_total 4536 _refine_hist.d_res_high 1.97 _refine_hist.d_res_low 35.00 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.014 0.021 ? 4092 'X-RAY DIFFRACTION' ? r_bond_other_d ? ? ? ? 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.472 1.961 ? 5536 'X-RAY DIFFRACTION' ? r_angle_other_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 6.190 5.000 ? 494 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 34.798 25.178 ? 197 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 13.870 15.000 ? 699 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 19.594 15.000 ? 17 'X-RAY DIFFRACTION' ? r_chiral_restr 0.101 0.200 ? 595 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.006 0.021 ? 3109 'X-RAY DIFFRACTION' ? r_gen_planes_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_refined 0.202 0.200 ? 1774 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined 0.309 0.200 ? 2735 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined 0.181 0.200 ? 435 '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 0.180 0.200 ? 80 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined 0.267 0.200 ? 43 '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 0.841 1.500 ? 2453 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it 1.563 2.000 ? 3954 'X-RAY DIFFRACTION' ? r_scbond_it 2.486 3.000 ? 1639 'X-RAY DIFFRACTION' ? r_scangle_it 4.115 4.500 ? 1582 '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 1.97 _refine_ls_shell.d_res_low 2.023 _refine_ls_shell.number_reflns_R_work 3218 _refine_ls_shell.R_factor_R_work 0.247 _refine_ls_shell.percent_reflns_obs 98.05 _refine_ls_shell.R_factor_R_free 0.321 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 157 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.number_reflns_obs ? # _struct.entry_id 3QQB _struct.title 'Crystal structure of HA2 R106H mutant of H2 hemagglutinin, neutral pH form' _struct.pdbx_descriptor Hemagglutinin _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3QQB _struct_keywords.text 'viral envelope protein, hemagglutinin, viral fusion protein, VIRAL PROTEIN' _struct_keywords.pdbx_keywords 'VIRAL PROTEIN' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 3 ? E N N 3 ? F N N 4 ? G N N 3 ? H N N 5 ? I N N 6 ? J N N 6 ? # _struct_biol.id 1 _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 SER A 58 ? GLY A 65 ? SER A 65 GLY A 72 1 ? 8 HELX_P HELX_P2 2 ASN A 66 ? LEU A 73 ? ASN A 73 LEU A 80 5 ? 8 HELX_P HELX_P3 3 ASP A 99 ? SER A 108 ? ASP A 104 SER A 113 1 ? 10 HELX_P HELX_P4 4 PRO A 120 ? TRP A 124 ? PRO A 122 TRP A 127 5 ? 5 HELX_P HELX_P5 5 ASP A 184 ? GLN A 193 ? ASP A 187 GLN A 196 1 ? 10 HELX_P HELX_P6 6 ASP B 37 ? MET B 59 ? ASP B 37 MET B 59 1 ? 23 HELX_P HELX_P7 7 GLU B 74 ? ARG B 127 ? GLU B 74 ARG B 127 1 ? 54 HELX_P HELX_P8 8 ASP B 145 ? ASN B 154 ? ASP B 145 ASN B 154 1 ? 10 HELX_P HELX_P9 9 ASP B 158 ? GLU B 172 ? ASP B 158 GLU B 172 1 ? 15 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 6 SG ? ? ? 1_555 B CYS 137 SG ? ? A CYS 14 B CYS 137 1_555 ? ? ? ? ? ? ? 2.082 ? disulf2 disulf ? ? A CYS 44 SG ? ? ? 1_555 A CYS 275 SG ? ? A CYS 52 A CYS 277 1_555 ? ? ? ? ? ? ? 2.107 ? disulf3 disulf ? ? A CYS 57 SG ? ? ? 1_555 A CYS 69 SG ? ? A CYS 64 A CYS 76 1_555 ? ? ? ? ? ? ? 2.105 ? disulf4 disulf ? ? A CYS 279 SG ? ? ? 1_555 A CYS 303 SG ? ? A CYS 281 A CYS 305 1_555 ? ? ? ? ? ? ? 2.108 ? disulf5 disulf ? ? B CYS 144 SG ? ? ? 1_555 B CYS 148 SG ? ? B CYS 144 B CYS 148 1_555 ? ? ? ? ? ? ? 2.087 ? covale1 covale ? ? A ASN 166 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 169 A NAG 330 1_555 ? ? ? ? ? ? ? 1.448 ? covale2 covale ? ? C NAG . O4 ? ? ? 1_555 D NAG . C1 ? ? A NAG 330 A NAG 331 1_555 ? ? ? ? ? ? ? 1.452 ? covale3 covale ? ? A ASN 25 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 33 A NAG 332 1_555 ? ? ? ? ? ? ? 1.453 ? covale4 covale ? ? B ASN 154 ND2 ? ? ? 1_555 G NAG . C1 ? ? B ASN 154 B NAG 175 1_555 ? ? ? ? ? ? ? 1.458 ? # 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 A ? 5 ? B ? 2 ? C ? 2 ? D ? 3 ? E ? 2 ? F ? 3 ? G ? 5 ? H ? 5 ? I ? 2 ? J ? 4 ? K ? 3 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel A 4 5 ? anti-parallel B 1 2 ? anti-parallel C 1 2 ? anti-parallel D 1 2 ? parallel D 2 3 ? parallel E 1 2 ? parallel F 1 2 ? parallel F 2 3 ? parallel G 1 2 ? parallel G 2 3 ? anti-parallel G 3 4 ? anti-parallel G 4 5 ? anti-parallel H 1 2 ? parallel H 2 3 ? anti-parallel H 3 4 ? anti-parallel H 4 5 ? anti-parallel I 1 2 ? anti-parallel J 1 2 ? anti-parallel J 2 3 ? anti-parallel J 3 4 ? anti-parallel K 1 2 ? anti-parallel K 2 3 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 GLY B 31 ? ALA B 36 ? GLY B 31 ALA B 36 A 2 TYR B 22 ? ASN B 28 ? TYR B 22 ASN B 28 A 3 GLN A 4 ? TYR A 9 ? GLN A 12 TYR A 17 A 4 CYS B 137 ? PHE B 140 ? CYS B 137 PHE B 140 A 5 VAL B 130 ? GLU B 132 ? VAL B 130 GLU B 132 B 1 LYS A 17 ? VAL A 18 ? LYS A 25 VAL A 26 B 2 VAL A 26 ? THR A 27 ? VAL A 34 THR A 35 C 1 ALA A 31 ? ASP A 33 ? ALA A 39 ASP A 41 C 2 VAL A 313 ? ALA A 315 ? VAL A 315 ALA A 317 D 1 LEU A 35 ? GLU A 36 ? LEU A 43 GLU A 44 D 2 PHE A 292 ? HIS A 293 ? PHE A 294 HIS A 295 D 3 LYS A 305 ? TYR A 306 ? LYS A 307 TYR A 308 E 1 LEU A 43 ? LEU A 46 A LEU A 51 LEU A 53 E 2 LEU A 272 ? THR A 277 ? LEU A 274 THR A 279 F 1 LEU A 52 ? GLU A 53 ? LEU A 59 GLU A 60 F 2 ILE A 81 ? GLU A 83 ? ILE A 87 GLU A 89 F 3 ILE A 265 ? LYS A 267 ? ILE A 267 LYS A 269 G 1 GLY A 95 ? PHE A 97 ? GLY A 100 PHE A 102 G 2 ARG A 226 ? LEU A 234 ? ARG A 229 LEU A 237 G 3 MET A 173 ? HIS A 181 ? MET A 176 HIS A 184 G 4 GLY A 254 ? ARG A 260 ? GLY A 257 ARG A 263 G 5 VAL A 110 ? VAL A 116 ? VAL A 115 VAL A 118 H 1 GLY A 95 ? PHE A 97 ? GLY A 100 PHE A 102 H 2 ARG A 226 ? LEU A 234 ? ARG A 229 LEU A 237 H 3 MET A 173 ? HIS A 181 ? MET A 176 HIS A 184 H 4 LEU A 248 ? PRO A 251 ? LEU A 251 PRO A 254 H 5 MET A 148 ? TRP A 150 ? MET A 151 TRP A 153 I 1 SER A 133 ? VAL A 138 ? SER A 136 VAL A 141 I 2 ASN A 141 ? SER A 143 ? ASN A 144 SER A 146 J 1 ALA A 161 ? ASN A 166 ? ALA A 164 ASN A 169 J 2 THR A 239 ? SER A 244 ? THR A 242 SER A 247 J 3 VAL A 199 ? GLY A 202 ? VAL A 202 GLY A 205 J 4 ASN A 207 ? SER A 210 ? ASN A 210 SER A 213 K 1 GLY A 284 ? ILE A 286 ? GLY A 286 ILE A 288 K 2 CYS A 279 ? THR A 281 ? CYS A 281 THR A 283 K 3 ILE A 300 ? GLY A 301 ? ILE A 302 GLY A 303 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 O ALA B 35 ? O ALA B 35 N TYR B 24 ? N TYR B 24 A 2 3 O HIS B 25 ? O HIS B 25 N CYS A 6 ? N CYS A 14 A 3 4 N ILE A 5 ? N ILE A 13 O PHE B 138 ? O PHE B 138 A 4 5 O GLU B 139 ? O GLU B 139 N LYS B 131 ? N LYS B 131 B 1 2 N VAL A 18 ? N VAL A 26 O VAL A 26 ? O VAL A 34 C 1 2 N LYS A 32 ? N LYS A 40 O LEU A 314 ? O LEU A 316 D 1 2 N GLU A 36 ? N GLU A 44 O PHE A 292 ? O PHE A 294 D 2 3 N HIS A 293 ? N HIS A 295 O LYS A 305 ? O LYS A 307 E 1 2 N LEU A 43 ? N LEU A 51 O GLU A 273 ? O GLU A 275 F 1 2 N LEU A 52 ? N LEU A 59 O MET A 82 ? O MET A 88 F 2 3 N ILE A 81 ? N ILE A 87 O MET A 266 ? O MET A 268 G 1 2 N SER A 96 ? N SER A 101 O PHE A 229 ? O PHE A 232 G 2 3 O ARG A 226 ? O ARG A 229 N HIS A 181 ? N HIS A 184 G 3 4 N LEU A 174 ? N LEU A 177 O PHE A 255 ? O PHE A 258 G 4 5 O LYS A 259 ? O LYS A 262 N LYS A 111 ? N LYS A 116 H 1 2 N SER A 96 ? N SER A 101 O PHE A 229 ? O PHE A 232 H 2 3 O ARG A 226 ? O ARG A 229 N HIS A 181 ? N HIS A 184 H 3 4 N GLY A 178 ? N GLY A 181 O ILE A 249 ? O ILE A 252 H 4 5 O ALA A 250 ? O ALA A 253 N VAL A 149 ? N VAL A 152 I 1 2 N VAL A 138 ? N VAL A 141 O ASN A 141 ? O ASN A 144 J 1 2 N ALA A 161 ? N ALA A 164 O SER A 244 ? O SER A 247 J 2 3 O GLU A 243 ? O GLU A 246 N SER A 200 ? N SER A 203 J 3 4 N VAL A 199 ? N VAL A 202 O SER A 210 ? O SER A 213 K 1 2 O ILE A 286 ? O ILE A 288 N CYS A 279 ? N CYS A 281 K 2 3 N GLN A 280 ? N GLN A 282 O ILE A 300 ? O ILE A 302 # 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 ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG A 330' AC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 331' AC3 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 332' AC4 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE EDO A 1' AC5 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG B 175' AC6 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE PEG B 176' # 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 7 ASN A 166 ? ASN A 169 . ? 1_555 ? 2 AC1 7 TRP A 237 ? TRP A 240 . ? 1_555 ? 3 AC1 7 NAG D . ? NAG A 331 . ? 1_555 ? 4 AC1 7 HOH I . ? HOH A 375 . ? 1_555 ? 5 AC1 7 HOH I . ? HOH A 423 . ? 1_555 ? 6 AC1 7 HOH I . ? HOH A 476 . ? 1_555 ? 7 AC1 7 HOH I . ? HOH A 578 . ? 1_555 ? 8 AC2 3 NAG C . ? NAG A 330 . ? 1_555 ? 9 AC2 3 HOH I . ? HOH A 452 . ? 1_555 ? 10 AC2 3 HOH I . ? HOH A 700 . ? 1_555 ? 11 AC3 2 LYS A 17 ? LYS A 25 . ? 1_555 ? 12 AC3 2 ASN A 25 ? ASN A 33 . ? 1_555 ? 13 AC4 7 LEU A 119 ? LEU A 121 . ? 1_555 ? 14 AC4 7 PRO A 120 ? PRO A 122 . ? 1_555 ? 15 AC4 7 ARG A 123 ? ARG A 126 . ? 1_555 ? 16 AC4 7 TRP A 124 ? TRP A 127 . ? 1_555 ? 17 AC4 7 HOH I . ? HOH A 384 . ? 1_555 ? 18 AC4 7 HOH I . ? HOH A 558 . ? 1_555 ? 19 AC4 7 HOH I . ? HOH A 559 . ? 1_555 ? 20 AC5 3 GLU B 147 ? GLU B 147 . ? 1_555 ? 21 AC5 3 ASN B 150 ? ASN B 150 . ? 1_555 ? 22 AC5 3 ASN B 154 ? ASN B 154 . ? 1_555 ? 23 AC6 6 ILE A 324 ? ILE A 326 . ? 1_555 ? 24 AC6 6 TRP B 14 ? TRP B 14 . ? 1_555 ? 25 AC6 6 HIS B 25 ? HIS B 25 . ? 1_555 ? 26 AC6 6 ASN B 135 ? ASN B 135 . ? 1_555 ? 27 AC6 6 CYS B 137 ? CYS B 137 . ? 1_555 ? 28 AC6 6 HOH J . ? HOH B 355 . ? 1_555 ? # _atom_sites.entry_id 3QQB _atom_sites.fract_transf_matrix[1][1] 0.014227 _atom_sites.fract_transf_matrix[1][2] 0.008214 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.016428 _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] 0.004217 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . PRO A 1 1 ? 27.444 -3.683 -48.675 1.00 62.88 ? 9 PRO A N 1 ATOM 2 C CA . PRO A 1 1 ? 27.199 -3.288 -47.286 1.00 61.91 ? 9 PRO A CA 1 ATOM 3 C C . PRO A 1 1 ? 25.867 -3.840 -46.722 1.00 61.13 ? 9 PRO A C 1 ATOM 4 O O . PRO A 1 1 ? 24.894 -3.090 -46.571 1.00 61.09 ? 9 PRO A O 1 ATOM 5 C CB . PRO A 1 1 ? 27.192 -1.755 -47.368 1.00 62.06 ? 9 PRO A CB 1 ATOM 6 C CG . PRO A 1 1 ? 28.136 -1.447 -48.549 1.00 62.62 ? 9 PRO A CG 1 ATOM 7 C CD . PRO A 1 1 ? 28.283 -2.700 -49.384 1.00 63.09 ? 9 PRO A CD 1 ATOM 8 N N . GLY A 1 2 ? 25.852 -5.145 -46.406 1.00 59.95 ? 10 GLY A N 1 ATOM 9 C CA . GLY A 1 2 ? 24.637 -5.874 -45.992 1.00 57.71 ? 10 GLY A CA 1 ATOM 10 C C . GLY A 1 2 ? 23.932 -5.445 -44.702 1.00 55.37 ? 10 GLY A C 1 ATOM 11 O O . GLY A 1 2 ? 24.361 -4.512 -44.008 1.00 54.87 ? 10 GLY A O 1 ATOM 12 N N . ASP A 1 3 ? 22.819 -6.120 -44.404 1.00 53.43 ? 11 ASP A N 1 ATOM 13 C CA . ASP A 1 3 ? 22.069 -5.884 -43.174 1.00 50.95 ? 11 ASP A CA 1 ATOM 14 C C . ASP A 1 3 ? 22.914 -6.472 -42.028 1.00 49.16 ? 11 ASP A C 1 ATOM 15 O O . ASP A 1 3 ? 23.782 -7.319 -42.270 1.00 48.23 ? 11 ASP A O 1 ATOM 16 C CB . ASP A 1 3 ? 20.695 -6.576 -43.215 1.00 51.32 ? 11 ASP A CB 1 ATOM 17 C CG . ASP A 1 3 ? 19.775 -6.063 -44.352 1.00 51.68 ? 11 ASP A CG 1 ATOM 18 O OD1 . ASP A 1 3 ? 19.705 -4.839 -44.594 1.00 50.77 ? 11 ASP A OD1 1 ATOM 19 O OD2 . ASP A 1 3 ? 19.105 -6.913 -44.990 1.00 53.95 ? 11 ASP A OD2 1 ATOM 20 N N . GLN A 1 4 ? 22.656 -6.017 -40.802 1.00 47.74 ? 12 GLN A N 1 ATOM 21 C CA . GLN A 1 4 ? 23.409 -6.492 -39.637 1.00 46.62 ? 12 GLN A CA 1 ATOM 22 C C . GLN A 1 4 ? 22.549 -6.871 -38.434 1.00 45.08 ? 12 GLN A C 1 ATOM 23 O O . GLN A 1 4 ? 21.531 -6.238 -38.168 1.00 44.38 ? 12 GLN A O 1 ATOM 24 C CB . GLN A 1 4 ? 24.428 -5.437 -39.199 1.00 46.61 ? 12 GLN A CB 1 ATOM 25 C CG . GLN A 1 4 ? 25.763 -5.511 -39.944 1.00 49.61 ? 12 GLN A CG 1 ATOM 26 C CD . GLN A 1 4 ? 26.731 -4.435 -39.484 1.00 52.73 ? 12 GLN A CD 1 ATOM 27 O OE1 . GLN A 1 4 ? 26.714 -4.023 -38.322 1.00 50.83 ? 12 GLN A OE1 1 ATOM 28 N NE2 . GLN A 1 4 ? 27.588 -3.977 -40.399 1.00 53.48 ? 12 GLN A NE2 1 ATOM 29 N N . ILE A 1 5 ? 22.980 -7.906 -37.710 1.00 43.26 ? 13 ILE A N 1 ATOM 30 C CA . ILE A 1 5 ? 22.511 -8.100 -36.336 1.00 42.00 ? 13 ILE A CA 1 ATOM 31 C C . ILE A 1 5 ? 23.704 -8.116 -35.372 1.00 40.92 ? 13 ILE A C 1 ATOM 32 O O . ILE A 1 5 ? 24.756 -8.692 -35.680 1.00 39.75 ? 13 ILE A O 1 ATOM 33 C CB . ILE A 1 5 ? 21.588 -9.330 -36.192 1.00 41.69 ? 13 ILE A CB 1 ATOM 34 C CG1 . ILE A 1 5 ? 20.661 -9.150 -34.967 1.00 41.98 ? 13 ILE A CG1 1 ATOM 35 C CG2 . ILE A 1 5 ? 22.396 -10.646 -36.209 1.00 42.10 ? 13 ILE A CG2 1 ATOM 36 C CD1 . ILE A 1 5 ? 19.678 -10.298 -34.729 1.00 41.90 ? 13 ILE A CD1 1 ATOM 37 N N . CYS A 1 6 ? 23.541 -7.436 -34.231 1.00 40.91 ? 14 CYS A N 1 ATOM 38 C CA . CYS A 1 6 ? 24.610 -7.302 -33.242 1.00 40.74 ? 14 CYS A CA 1 ATOM 39 C C . CYS A 1 6 ? 24.155 -7.846 -31.888 1.00 39.13 ? 14 CYS A C 1 ATOM 40 O O . CYS A 1 6 ? 22.999 -7.682 -31.520 1.00 37.68 ? 14 CYS A O 1 ATOM 41 C CB . CYS A 1 6 ? 25.023 -5.838 -33.089 1.00 41.71 ? 14 CYS A CB 1 ATOM 42 S SG . CYS A 1 6 ? 25.597 -5.043 -34.668 1.00 48.58 ? 14 CYS A SG 1 ATOM 43 N N . ILE A 1 7 ? 25.068 -8.509 -31.185 1.00 37.50 ? 15 ILE A N 1 ATOM 44 C CA . ILE A 1 7 ? 24.809 -8.994 -29.820 1.00 37.34 ? 15 ILE A CA 1 ATOM 45 C C . ILE A 1 7 ? 25.450 -8.004 -28.875 1.00 36.46 ? 15 ILE A C 1 ATOM 46 O O . ILE A 1 7 ? 26.565 -7.575 -29.116 1.00 36.85 ? 15 ILE A O 1 ATOM 47 C CB . ILE A 1 7 ? 25.429 -10.390 -29.596 1.00 37.04 ? 15 ILE A CB 1 ATOM 48 C CG1 . ILE A 1 7 ? 25.015 -11.368 -30.701 1.00 39.73 ? 15 ILE A CG1 1 ATOM 49 C CG2 . ILE A 1 7 ? 25.116 -10.927 -28.182 1.00 37.17 ? 15 ILE A CG2 1 ATOM 50 C CD1 . ILE A 1 7 ? 23.552 -11.405 -31.025 1.00 42.73 ? 15 ILE A CD1 1 ATOM 51 N N . GLY A 1 8 ? 24.758 -7.630 -27.806 1.00 36.57 ? 16 GLY A N 1 ATOM 52 C CA . GLY A 1 8 ? 25.323 -6.704 -26.851 1.00 36.26 ? 16 GLY A CA 1 ATOM 53 C C . GLY A 1 8 ? 24.698 -6.806 -25.467 1.00 36.53 ? 16 GLY A C 1 ATOM 54 O O . GLY A 1 8 ? 23.895 -7.707 -25.205 1.00 36.92 ? 16 GLY A O 1 ATOM 55 N N . TYR A 1 9 ? 25.050 -5.856 -24.607 1.00 36.18 ? 17 TYR A N 1 ATOM 56 C CA . TYR A 1 9 ? 24.674 -5.890 -23.206 1.00 36.09 ? 17 TYR A CA 1 ATOM 57 C C . TYR A 1 9 ? 24.327 -4.532 -22.668 1.00 36.70 ? 17 TYR A C 1 ATOM 58 O O . TYR A 1 9 ? 24.798 -3.501 -23.159 1.00 37.71 ? 17 TYR A O 1 ATOM 59 C CB . TYR A 1 9 ? 25.778 -6.550 -22.351 1.00 35.42 ? 17 TYR A CB 1 ATOM 60 C CG . TYR A 1 9 ? 27.167 -6.032 -22.618 1.00 33.54 ? 17 TYR A CG 1 ATOM 61 C CD1 . TYR A 1 9 ? 27.659 -4.912 -21.955 1.00 33.92 ? 17 TYR A CD1 1 ATOM 62 C CD2 . TYR A 1 9 ? 27.981 -6.645 -23.546 1.00 33.41 ? 17 TYR A CD2 1 ATOM 63 C CE1 . TYR A 1 9 ? 28.945 -4.443 -22.201 1.00 33.02 ? 17 TYR A CE1 1 ATOM 64 C CE2 . TYR A 1 9 ? 29.262 -6.192 -23.791 1.00 34.76 ? 17 TYR A CE2 1 ATOM 65 C CZ . TYR A 1 9 ? 29.723 -5.071 -23.124 1.00 35.66 ? 17 TYR A CZ 1 ATOM 66 O OH . TYR A 1 9 ? 30.990 -4.613 -23.382 1.00 39.54 ? 17 TYR A OH 1 ATOM 67 N N . HIS A 1 10 ? 23.468 -4.555 -21.661 1.00 37.06 ? 18 HIS A N 1 ATOM 68 C CA . HIS A 1 10 ? 22.964 -3.387 -20.945 1.00 38.56 ? 18 HIS A CA 1 ATOM 69 C C . HIS A 1 10 ? 24.071 -2.524 -20.351 1.00 38.70 ? 18 HIS A C 1 ATOM 70 O O . HIS A 1 10 ? 25.104 -3.026 -19.894 1.00 39.08 ? 18 HIS A O 1 ATOM 71 C CB . HIS A 1 10 ? 22.063 -3.893 -19.813 1.00 38.14 ? 18 HIS A CB 1 ATOM 72 C CG . HIS A 1 10 ? 21.389 -2.822 -19.031 1.00 38.78 ? 18 HIS A CG 1 ATOM 73 N ND1 . HIS A 1 10 ? 20.341 -2.081 -19.530 1.00 39.71 ? 18 HIS A ND1 1 ATOM 74 C CD2 . HIS A 1 10 ? 21.578 -2.400 -17.758 1.00 39.39 ? 18 HIS A CD2 1 ATOM 75 C CE1 . HIS A 1 10 ? 19.933 -1.229 -18.606 1.00 41.47 ? 18 HIS A CE1 1 ATOM 76 N NE2 . HIS A 1 10 ? 20.664 -1.406 -17.520 1.00 39.67 ? 18 HIS A NE2 1 ATOM 77 N N . ALA A 1 11 ? 23.854 -1.220 -20.402 1.00 39.37 ? 19 ALA A N 1 ATOM 78 C CA . ALA A 1 11 ? 24.666 -0.245 -19.695 1.00 40.16 ? 19 ALA A CA 1 ATOM 79 C C . ALA A 1 11 ? 23.696 0.823 -19.252 1.00 40.36 ? 19 ALA A C 1 ATOM 80 O O . ALA A 1 11 ? 22.687 1.026 -19.915 1.00 40.89 ? 19 ALA A O 1 ATOM 81 C CB . ALA A 1 11 ? 25.743 0.339 -20.605 1.00 40.13 ? 19 ALA A CB 1 ATOM 82 N N . ASN A 1 12 ? 23.965 1.472 -18.118 1.00 40.50 ? 20 ASN A N 1 ATOM 83 C CA . ASN A 1 12 ? 23.103 2.536 -17.602 1.00 41.03 ? 20 ASN A CA 1 ATOM 84 C C . ASN A 1 12 ? 23.983 3.608 -16.977 1.00 41.80 ? 20 ASN A C 1 ATOM 85 O O . ASN A 1 12 ? 25.197 3.632 -17.250 1.00 41.57 ? 20 ASN A O 1 ATOM 86 C CB . ASN A 1 12 ? 22.072 2.004 -16.595 1.00 40.90 ? 20 ASN A CB 1 ATOM 87 C CG . ASN A 1 12 ? 22.714 1.203 -15.463 1.00 40.60 ? 20 ASN A CG 1 ATOM 88 O OD1 . ASN A 1 12 ? 23.919 1.257 -15.260 1.00 36.35 ? 20 ASN A OD1 1 ATOM 89 N ND2 . ASN A 1 12 ? 21.904 0.435 -14.747 1.00 41.82 ? 20 ASN A ND2 1 ATOM 90 N N . ASN A 1 13 ? 23.391 4.483 -16.160 1.00 42.46 ? 21 ASN A N 1 ATOM 91 C CA . ASN A 1 13 ? 24.140 5.534 -15.474 1.00 44.00 ? 21 ASN A CA 1 ATOM 92 C C . ASN A 1 13 ? 24.618 5.155 -14.049 1.00 44.23 ? 21 ASN A C 1 ATOM 93 O O . ASN A 1 13 ? 25.079 6.016 -13.296 1.00 43.96 ? 21 ASN A O 1 ATOM 94 C CB . ASN A 1 13 ? 23.335 6.851 -15.438 1.00 45.15 ? 21 ASN A CB 1 ATOM 95 C CG . ASN A 1 13 ? 21.927 6.682 -14.858 1.00 47.94 ? 21 ASN A CG 1 ATOM 96 O OD1 . ASN A 1 13 ? 21.630 5.683 -14.196 1.00 53.39 ? 21 ASN A OD1 1 ATOM 97 N ND2 . ASN A 1 13 ? 21.060 7.670 -15.092 1.00 50.87 ? 21 ASN A ND2 1 ATOM 98 N N . SER A 1 14 ? 24.513 3.872 -13.691 1.00 43.84 ? 22 SER A N 1 ATOM 99 C CA . SER A 1 14 ? 24.873 3.416 -12.347 1.00 43.32 ? 22 SER A CA 1 ATOM 100 C C . SER A 1 14 ? 26.329 3.733 -12.037 1.00 43.26 ? 22 SER A C 1 ATOM 101 O O . SER A 1 14 ? 27.208 3.562 -12.894 1.00 43.21 ? 22 SER A O 1 ATOM 102 C CB . SER A 1 14 ? 24.608 1.914 -12.192 1.00 43.26 ? 22 SER A CB 1 ATOM 103 O OG . SER A 1 14 ? 25.157 1.403 -10.988 1.00 42.99 ? 22 SER A OG 1 ATOM 104 N N . THR A 1 15 ? 26.575 4.218 -10.817 1.00 42.96 ? 23 THR A N 1 ATOM 105 C CA . THR A 1 15 ? 27.948 4.387 -10.322 1.00 42.79 ? 23 THR A CA 1 ATOM 106 C C . THR A 1 15 ? 28.202 3.500 -9.091 1.00 42.44 ? 23 THR A C 1 ATOM 107 O O . THR A 1 15 ? 29.194 3.672 -8.388 1.00 42.22 ? 23 THR A O 1 ATOM 108 C CB . THR A 1 15 ? 28.265 5.861 -9.980 1.00 42.96 ? 23 THR A CB 1 ATOM 109 O OG1 . THR A 1 15 ? 27.268 6.353 -9.084 1.00 42.11 ? 23 THR A OG1 1 ATOM 110 C CG2 . THR A 1 15 ? 28.309 6.733 -11.253 1.00 43.23 ? 23 THR A CG2 1 ATOM 111 N N . GLU A 1 16 ? 27.287 2.560 -8.853 1.00 42.29 ? 24 GLU A N 1 ATOM 112 C CA . GLU A 1 16 ? 27.421 1.534 -7.819 1.00 42.22 ? 24 GLU A CA 1 ATOM 113 C C . GLU A 1 16 ? 28.712 0.761 -8.022 1.00 41.35 ? 24 GLU A C 1 ATOM 114 O O . GLU A 1 16 ? 28.988 0.293 -9.127 1.00 41.22 ? 24 GLU A O 1 ATOM 115 C CB . GLU A 1 16 ? 26.225 0.577 -7.862 1.00 42.89 ? 24 GLU A CB 1 ATOM 116 C CG . GLU A 1 16 ? 24.872 1.259 -7.700 1.00 46.22 ? 24 GLU A CG 1 ATOM 117 C CD . GLU A 1 16 ? 24.794 2.068 -6.414 1.00 50.83 ? 24 GLU A CD 1 ATOM 118 O OE1 . GLU A 1 16 ? 24.664 1.432 -5.344 1.00 52.29 ? 24 GLU A OE1 1 ATOM 119 O OE2 . GLU A 1 16 ? 24.871 3.326 -6.470 1.00 53.73 ? 24 GLU A OE2 1 ATOM 120 N N . LYS A 1 17 ? 29.501 0.662 -6.952 1.00 39.98 ? 25 LYS A N 1 ATOM 121 C CA . LYS A 1 17 ? 30.803 0.002 -6.966 1.00 39.34 ? 25 LYS A CA 1 ATOM 122 C C . LYS A 1 17 ? 30.768 -1.309 -6.192 1.00 37.72 ? 25 LYS A C 1 ATOM 123 O O . LYS A 1 17 ? 30.064 -1.417 -5.190 1.00 36.97 ? 25 LYS A O 1 ATOM 124 C CB . LYS A 1 17 ? 31.857 0.916 -6.332 1.00 39.91 ? 25 LYS A CB 1 ATOM 125 C CG . LYS A 1 17 ? 32.053 2.247 -7.048 1.00 41.41 ? 25 LYS A CG 1 ATOM 126 C CD . LYS A 1 17 ? 32.689 2.000 -8.395 1.00 43.97 ? 25 LYS A CD 1 ATOM 127 C CE . LYS A 1 17 ? 33.369 3.228 -8.931 1.00 46.82 ? 25 LYS A CE 1 ATOM 128 N NZ . LYS A 1 17 ? 34.437 2.778 -9.863 1.00 49.73 ? 25 LYS A NZ 1 ATOM 129 N N . VAL A 1 18 ? 31.530 -2.299 -6.657 1.00 36.07 ? 26 VAL A N 1 ATOM 130 C CA . VAL A 1 18 ? 31.734 -3.540 -5.906 1.00 34.54 ? 26 VAL A CA 1 ATOM 131 C C . VAL A 1 18 ? 33.209 -3.925 -5.948 1.00 34.48 ? 26 VAL A C 1 ATOM 132 O O . VAL A 1 18 ? 33.939 -3.461 -6.809 1.00 34.53 ? 26 VAL A O 1 ATOM 133 C CB . VAL A 1 18 ? 30.891 -4.754 -6.437 1.00 34.50 ? 26 VAL A CB 1 ATOM 134 C CG1 . VAL A 1 18 ? 29.404 -4.471 -6.376 1.00 33.61 ? 26 VAL A CG1 1 ATOM 135 C CG2 . VAL A 1 18 ? 31.333 -5.179 -7.855 1.00 33.30 ? 26 VAL A CG2 1 ATOM 136 N N . ASP A 1 19 ? 33.636 -4.800 -5.038 1.00 33.89 ? 27 ASP A N 1 ATOM 137 C CA . ASP A 1 19 ? 34.974 -5.385 -5.119 1.00 33.98 ? 27 ASP A CA 1 ATOM 138 C C . ASP A 1 19 ? 34.880 -6.839 -5.537 1.00 33.55 ? 27 ASP A C 1 ATOM 139 O O . ASP A 1 19 ? 33.864 -7.511 -5.287 1.00 33.46 ? 27 ASP A O 1 ATOM 140 C CB . ASP A 1 19 ? 35.720 -5.275 -3.783 1.00 33.90 ? 27 ASP A CB 1 ATOM 141 C CG . ASP A 1 19 ? 35.921 -3.831 -3.337 1.00 36.46 ? 27 ASP A CG 1 ATOM 142 O OD1 . ASP A 1 19 ? 35.949 -2.913 -4.185 1.00 34.90 ? 27 ASP A OD1 1 ATOM 143 O OD2 . ASP A 1 19 ? 36.005 -3.607 -2.111 1.00 39.56 ? 27 ASP A OD2 1 ATOM 144 N N . THR A 1 20 ? 35.943 -7.322 -6.166 1.00 32.90 ? 28 THR A N 1 ATOM 145 C CA . THR A 1 20 ? 36.043 -8.707 -6.567 1.00 33.89 ? 28 THR A CA 1 ATOM 146 C C . THR A 1 20 ? 37.426 -9.138 -6.123 1.00 34.74 ? 28 THR A C 1 ATOM 147 O O . THR A 1 20 ? 38.148 -8.329 -5.540 1.00 35.46 ? 28 THR A O 1 ATOM 148 C CB . THR A 1 20 ? 35.933 -8.850 -8.107 1.00 34.10 ? 28 THR A CB 1 ATOM 149 O OG1 . THR A 1 20 ? 37.010 -8.127 -8.729 1.00 32.63 ? 28 THR A OG1 1 ATOM 150 C CG2 . THR A 1 20 ? 34.593 -8.330 -8.602 1.00 32.25 ? 28 THR A CG2 1 ATOM 151 N N . ILE A 1 21 ? 37.803 -10.372 -6.419 1.00 35.18 ? 29 ILE A N 1 ATOM 152 C CA . ILE A 1 21 ? 39.125 -10.882 -6.073 1.00 35.97 ? 29 ILE A CA 1 ATOM 153 C C . ILE A 1 21 ? 40.230 -10.203 -6.891 1.00 37.09 ? 29 ILE A C 1 ATOM 154 O O . ILE A 1 21 ? 41.272 -9.843 -6.344 1.00 37.03 ? 29 ILE A O 1 ATOM 155 C CB . ILE A 1 21 ? 39.207 -12.410 -6.237 1.00 36.32 ? 29 ILE A CB 1 ATOM 156 C CG1 . ILE A 1 21 ? 38.261 -13.144 -5.266 1.00 36.22 ? 29 ILE A CG1 1 ATOM 157 C CG2 . ILE A 1 21 ? 40.647 -12.917 -6.112 1.00 36.63 ? 29 ILE A CG2 1 ATOM 158 C CD1 . ILE A 1 21 ? 38.710 -13.198 -3.796 1.00 37.07 ? 29 ILE A CD1 1 ATOM 159 N N . LEU A 1 22 ? 39.993 -10.030 -8.194 1.00 36.89 ? 30 LEU A N 1 ATOM 160 C CA . LEU A 1 22 ? 41.006 -9.531 -9.117 1.00 38.20 ? 30 LEU A CA 1 ATOM 161 C C . LEU A 1 22 ? 41.076 -8.014 -9.205 1.00 38.15 ? 30 LEU A C 1 ATOM 162 O O . LEU A 1 22 ? 42.097 -7.473 -9.635 1.00 37.79 ? 30 LEU A O 1 ATOM 163 C CB . LEU A 1 22 ? 40.765 -10.104 -10.528 1.00 38.42 ? 30 LEU A CB 1 ATOM 164 C CG . LEU A 1 22 ? 41.469 -11.360 -11.055 1.00 40.01 ? 30 LEU A CG 1 ATOM 165 C CD1 . LEU A 1 22 ? 42.141 -12.249 -10.050 1.00 41.07 ? 30 LEU A CD1 1 ATOM 166 C CD2 . LEU A 1 22 ? 40.515 -12.157 -11.960 1.00 41.35 ? 30 LEU A CD2 1 ATOM 167 N N . GLU A 1 23 ? 40.001 -7.338 -8.802 1.00 38.09 ? 31 GLU A N 1 ATOM 168 C CA . GLU A 1 23 ? 39.861 -5.912 -9.040 1.00 39.60 ? 31 GLU A CA 1 ATOM 169 C C . GLU A 1 23 ? 38.958 -5.250 -8.013 1.00 39.57 ? 31 GLU A C 1 ATOM 170 O O . GLU A 1 23 ? 37.871 -5.745 -7.696 1.00 39.91 ? 31 GLU A O 1 ATOM 171 C CB . GLU A 1 23 ? 39.309 -5.674 -10.462 1.00 39.93 ? 31 GLU A CB 1 ATOM 172 C CG . GLU A 1 23 ? 39.180 -4.214 -10.871 1.00 40.88 ? 31 GLU A CG 1 ATOM 173 C CD . GLU A 1 23 ? 38.665 -4.030 -12.312 1.00 42.64 ? 31 GLU A CD 1 ATOM 174 O OE1 . GLU A 1 23 ? 38.391 -5.027 -13.026 1.00 42.25 ? 31 GLU A OE1 1 ATOM 175 O OE2 . GLU A 1 23 ? 38.527 -2.869 -12.724 1.00 44.81 ? 31 GLU A OE2 1 ATOM 176 N N . ARG A 1 24 ? 39.397 -4.108 -7.509 1.00 40.36 ? 32 ARG A N 1 ATOM 177 C CA . ARG A 1 24 ? 38.591 -3.345 -6.562 1.00 40.89 ? 32 ARG A CA 1 ATOM 178 C C . ARG A 1 24 ? 37.872 -2.205 -7.261 1.00 40.92 ? 32 ARG A C 1 ATOM 179 O O . ARG A 1 24 ? 38.307 -1.758 -8.320 1.00 41.59 ? 32 ARG A O 1 ATOM 180 C CB . ARG A 1 24 ? 39.479 -2.818 -5.434 1.00 41.03 ? 32 ARG A CB 1 ATOM 181 C CG . ARG A 1 24 ? 40.102 -3.928 -4.615 1.00 44.29 ? 32 ARG A CG 1 ATOM 182 C CD . ARG A 1 24 ? 40.999 -3.398 -3.520 1.00 50.95 ? 32 ARG A CD 1 ATOM 183 N NE . ARG A 1 24 ? 41.889 -4.448 -3.014 1.00 55.78 ? 32 ARG A NE 1 ATOM 184 C CZ . ARG A 1 24 ? 42.701 -4.313 -1.963 1.00 58.46 ? 32 ARG A CZ 1 ATOM 185 N NH1 . ARG A 1 24 ? 42.719 -3.174 -1.276 1.00 59.10 ? 32 ARG A NH1 1 ATOM 186 N NH2 . ARG A 1 24 ? 43.487 -5.323 -1.587 1.00 58.65 ? 32 ARG A NH2 1 ATOM 187 N N . ASN A 1 25 ? 36.760 -1.752 -6.682 1.00 40.56 ? 33 ASN A N 1 ATOM 188 C CA . ASN A 1 25 ? 36.105 -0.530 -7.147 1.00 41.61 ? 33 ASN A CA 1 ATOM 189 C C . ASN A 1 25 ? 35.518 -0.675 -8.575 1.00 40.45 ? 33 ASN A C 1 ATOM 190 O O . ASN A 1 25 ? 35.735 0.171 -9.442 1.00 40.44 ? 33 ASN A O 1 ATOM 191 C CB . ASN A 1 25 ? 37.114 0.639 -7.060 1.00 42.93 ? 33 ASN A CB 1 ATOM 192 C CG . ASN A 1 25 ? 36.459 2.000 -7.130 1.00 48.58 ? 33 ASN A CG 1 ATOM 193 O OD1 . ASN A 1 25 ? 35.318 2.178 -6.683 1.00 50.16 ? 33 ASN A OD1 1 ATOM 194 N ND2 . ASN A 1 25 ? 37.186 2.983 -7.691 1.00 57.57 ? 33 ASN A ND2 1 ATOM 195 N N . VAL A 1 26 ? 34.786 -1.762 -8.815 1.00 38.69 ? 34 VAL A N 1 ATOM 196 C CA . VAL A 1 26 ? 34.229 -2.024 -10.141 1.00 37.22 ? 34 VAL A CA 1 ATOM 197 C C . VAL A 1 26 ? 32.837 -1.427 -10.211 1.00 36.49 ? 34 VAL A C 1 ATOM 198 O O . VAL A 1 26 ? 32.019 -1.660 -9.324 1.00 36.35 ? 34 VAL A O 1 ATOM 199 C CB . VAL A 1 26 ? 34.169 -3.544 -10.441 1.00 37.29 ? 34 VAL A CB 1 ATOM 200 C CG1 . VAL A 1 26 ? 33.609 -3.817 -11.841 1.00 36.49 ? 34 VAL A CG1 1 ATOM 201 C CG2 . VAL A 1 26 ? 35.545 -4.158 -10.277 1.00 35.90 ? 34 VAL A CG2 1 ATOM 202 N N . THR A 1 27 ? 32.565 -0.662 -11.269 1.00 35.35 ? 35 THR A N 1 ATOM 203 C CA . THR A 1 27 ? 31.220 -0.147 -11.497 1.00 34.31 ? 35 THR A CA 1 ATOM 204 C C . THR A 1 27 ? 30.362 -1.214 -12.168 1.00 33.94 ? 35 THR A C 1 ATOM 205 O O . THR A 1 27 ? 30.760 -1.810 -13.162 1.00 34.16 ? 35 THR A O 1 ATOM 206 C CB . THR A 1 27 ? 31.228 1.142 -12.345 1.00 34.82 ? 35 THR A CB 1 ATOM 207 O OG1 . THR A 1 27 ? 32.157 2.076 -11.781 1.00 35.93 ? 35 THR A OG1 1 ATOM 208 C CG2 . THR A 1 27 ? 29.848 1.777 -12.385 1.00 33.40 ? 35 THR A CG2 1 ATOM 209 N N . VAL A 1 28 ? 29.184 -1.447 -11.612 1.00 32.92 ? 36 VAL A N 1 ATOM 210 C CA . VAL A 1 28 ? 28.273 -2.448 -12.132 1.00 32.96 ? 36 VAL A CA 1 ATOM 211 C C . VAL A 1 28 ? 26.905 -1.814 -12.380 1.00 32.90 ? 36 VAL A C 1 ATOM 212 O O . VAL A 1 28 ? 26.582 -0.787 -11.800 1.00 32.88 ? 36 VAL A O 1 ATOM 213 C CB . VAL A 1 28 ? 28.136 -3.663 -11.163 1.00 31.89 ? 36 VAL A CB 1 ATOM 214 C CG1 . VAL A 1 28 ? 29.452 -4.413 -11.066 1.00 31.01 ? 36 VAL A CG1 1 ATOM 215 C CG2 . VAL A 1 28 ? 27.601 -3.196 -9.741 1.00 33.25 ? 36 VAL A CG2 1 ATOM 216 N N . THR A 1 29 ? 26.102 -2.446 -13.229 1.00 33.89 ? 37 THR A N 1 ATOM 217 C CA . THR A 1 29 ? 24.793 -1.886 -13.622 1.00 33.55 ? 37 THR A CA 1 ATOM 218 C C . THR A 1 29 ? 23.758 -1.968 -12.511 1.00 34.09 ? 37 THR A C 1 ATOM 219 O O . THR A 1 29 ? 22.876 -1.097 -12.428 1.00 33.01 ? 37 THR A O 1 ATOM 220 C CB . THR A 1 29 ? 24.232 -2.565 -14.872 1.00 33.72 ? 37 THR A CB 1 ATOM 221 O OG1 . THR A 1 29 ? 24.015 -3.966 -14.615 1.00 33.65 ? 37 THR A OG1 1 ATOM 222 C CG2 . THR A 1 29 ? 25.208 -2.404 -16.042 1.00 33.05 ? 37 THR A CG2 1 ATOM 223 N N . HIS A 1 30 ? 23.850 -3.037 -11.699 1.00 34.09 ? 38 HIS A N 1 ATOM 224 C CA . HIS A 1 30 ? 22.979 -3.232 -10.511 1.00 34.63 ? 38 HIS A CA 1 ATOM 225 C C . HIS A 1 30 ? 23.778 -3.926 -9.394 1.00 34.39 ? 38 HIS A C 1 ATOM 226 O O . HIS A 1 30 ? 24.670 -4.737 -9.643 1.00 32.88 ? 38 HIS A O 1 ATOM 227 C CB . HIS A 1 30 ? 21.719 -4.068 -10.835 1.00 35.07 ? 38 HIS A CB 1 ATOM 228 C CG . HIS A 1 30 ? 20.937 -3.577 -12.025 1.00 36.67 ? 38 HIS A CG 1 ATOM 229 N ND1 . HIS A 1 30 ? 21.221 -3.962 -13.322 1.00 39.43 ? 38 HIS A ND1 1 ATOM 230 C CD2 . HIS A 1 30 ? 19.875 -2.738 -12.108 1.00 36.23 ? 38 HIS A CD2 1 ATOM 231 C CE1 . HIS A 1 30 ? 20.376 -3.374 -14.152 1.00 38.72 ? 38 HIS A CE1 1 ATOM 232 N NE2 . HIS A 1 30 ? 19.551 -2.623 -13.441 1.00 38.65 ? 38 HIS A NE2 1 ATOM 233 N N . ALA A 1 31 ? 23.437 -3.587 -8.159 1.00 35.32 ? 39 ALA A N 1 ATOM 234 C CA . ALA A 1 31 ? 24.163 -4.057 -6.984 1.00 35.73 ? 39 ALA A CA 1 ATOM 235 C C . ALA A 1 31 ? 23.165 -4.152 -5.831 1.00 36.49 ? 39 ALA A C 1 ATOM 236 O O . ALA A 1 31 ? 22.136 -3.475 -5.847 1.00 36.22 ? 39 ALA A O 1 ATOM 237 C CB . ALA A 1 31 ? 25.249 -3.071 -6.640 1.00 35.17 ? 39 ALA A CB 1 ATOM 238 N N . LYS A 1 32 ? 23.478 -4.982 -4.840 1.00 36.55 ? 40 LYS A N 1 ATOM 239 C CA . LYS A 1 32 ? 22.636 -5.132 -3.656 1.00 37.42 ? 40 LYS A CA 1 ATOM 240 C C . LYS A 1 32 ? 23.521 -4.963 -2.422 1.00 36.84 ? 40 LYS A C 1 ATOM 241 O O . LYS A 1 32 ? 24.387 -5.788 -2.156 1.00 36.89 ? 40 LYS A O 1 ATOM 242 C CB . LYS A 1 32 ? 21.943 -6.500 -3.663 1.00 37.71 ? 40 LYS A CB 1 ATOM 243 C CG . LYS A 1 32 ? 21.169 -6.852 -2.394 1.00 41.50 ? 40 LYS A CG 1 ATOM 244 C CD . LYS A 1 32 ? 19.977 -5.946 -2.188 1.00 45.16 ? 40 LYS A CD 1 ATOM 245 C CE . LYS A 1 32 ? 19.093 -6.434 -1.051 1.00 47.01 ? 40 LYS A CE 1 ATOM 246 N NZ . LYS A 1 32 ? 18.273 -5.283 -0.587 1.00 49.40 ? 40 LYS A NZ 1 ATOM 247 N N . ASP A 1 33 ? 23.315 -3.860 -1.715 1.00 36.66 ? 41 ASP A N 1 ATOM 248 C CA . ASP A 1 33 ? 23.942 -3.609 -0.422 1.00 36.54 ? 41 ASP A CA 1 ATOM 249 C C . ASP A 1 33 ? 23.270 -4.522 0.591 1.00 35.74 ? 41 ASP A C 1 ATOM 250 O O . ASP A 1 33 ? 22.049 -4.446 0.773 1.00 35.31 ? 41 ASP A O 1 ATOM 251 C CB . ASP A 1 33 ? 23.704 -2.161 -0.032 1.00 37.60 ? 41 ASP A CB 1 ATOM 252 C CG . ASP A 1 33 ? 24.516 -1.732 1.178 1.00 39.68 ? 41 ASP A CG 1 ATOM 253 O OD1 . ASP A 1 33 ? 25.065 -2.590 1.919 1.00 40.93 ? 41 ASP A OD1 1 ATOM 254 O OD2 . ASP A 1 33 ? 24.599 -0.511 1.375 1.00 42.79 ? 41 ASP A OD2 1 ATOM 255 N N . ILE A 1 34 ? 24.045 -5.387 1.240 1.00 34.31 ? 42 ILE A N 1 ATOM 256 C CA . ILE A 1 34 ? 23.451 -6.294 2.229 1.00 34.22 ? 42 ILE A CA 1 ATOM 257 C C . ILE A 1 34 ? 23.792 -5.969 3.705 1.00 33.54 ? 42 ILE A C 1 ATOM 258 O O . ILE A 1 34 ? 23.519 -6.767 4.599 1.00 34.45 ? 42 ILE A O 1 ATOM 259 C CB . ILE A 1 34 ? 23.723 -7.786 1.892 1.00 33.95 ? 42 ILE A CB 1 ATOM 260 C CG1 . ILE A 1 34 ? 25.221 -8.111 1.977 1.00 32.26 ? 42 ILE A CG1 1 ATOM 261 C CG2 . ILE A 1 34 ? 23.094 -8.155 0.513 1.00 34.31 ? 42 ILE A CG2 1 ATOM 262 C CD1 . ILE A 1 34 ? 25.546 -9.591 1.724 1.00 31.77 ? 42 ILE A CD1 1 ATOM 263 N N . LEU A 1 35 ? 24.342 -4.778 3.946 1.00 33.21 ? 43 LEU A N 1 ATOM 264 C CA . LEU A 1 35 ? 24.782 -4.378 5.274 1.00 32.74 ? 43 LEU A CA 1 ATOM 265 C C . LEU A 1 35 ? 24.018 -3.143 5.815 1.00 32.53 ? 43 LEU A C 1 ATOM 266 O O . LEU A 1 35 ? 24.116 -2.045 5.255 1.00 32.76 ? 43 LEU A O 1 ATOM 267 C CB . LEU A 1 35 ? 26.287 -4.102 5.254 1.00 32.55 ? 43 LEU A CB 1 ATOM 268 C CG . LEU A 1 35 ? 26.918 -3.668 6.585 1.00 33.21 ? 43 LEU A CG 1 ATOM 269 C CD1 . LEU A 1 35 ? 26.949 -4.839 7.570 1.00 32.91 ? 43 LEU A CD1 1 ATOM 270 C CD2 . LEU A 1 35 ? 28.315 -3.103 6.342 1.00 31.75 ? 43 LEU A CD2 1 ATOM 271 N N . GLU A 1 36 ? 23.262 -3.328 6.895 1.00 31.39 ? 44 GLU A N 1 ATOM 272 C CA . GLU A 1 36 ? 22.587 -2.206 7.542 1.00 31.09 ? 44 GLU A CA 1 ATOM 273 C C . GLU A 1 36 ? 23.603 -1.452 8.409 1.00 30.54 ? 44 GLU A C 1 ATOM 274 O O . GLU A 1 36 ? 24.292 -2.046 9.212 1.00 29.82 ? 44 GLU A O 1 ATOM 275 C CB . GLU A 1 36 ? 21.396 -2.666 8.375 1.00 30.89 ? 44 GLU A CB 1 ATOM 276 C CG . GLU A 1 36 ? 20.628 -1.508 9.046 1.00 32.38 ? 44 GLU A CG 1 ATOM 277 C CD . GLU A 1 36 ? 20.167 -0.472 8.019 1.00 35.18 ? 44 GLU A CD 1 ATOM 278 O OE1 . GLU A 1 36 ? 19.274 -0.788 7.230 1.00 34.51 ? 44 GLU A OE1 1 ATOM 279 O OE2 . GLU A 1 36 ? 20.737 0.633 7.975 1.00 37.22 ? 44 GLU A OE2 1 ATOM 280 N N . LYS A 1 37 ? 23.683 -0.145 8.234 1.00 30.59 ? 45 LYS A N 1 ATOM 281 C CA . LYS A 1 37 ? 24.665 0.661 8.937 1.00 31.38 ? 45 LYS A CA 1 ATOM 282 C C . LYS A 1 37 ? 23.974 1.741 9.799 1.00 31.93 ? 45 LYS A C 1 ATOM 283 O O . LYS A 1 37 ? 24.634 2.477 10.505 1.00 32.49 ? 45 LYS A O 1 ATOM 284 C CB . LYS A 1 37 ? 25.650 1.297 7.938 1.00 31.86 ? 45 LYS A CB 1 ATOM 285 C CG . LYS A 1 37 ? 26.291 0.287 6.982 1.00 31.35 ? 45 LYS A CG 1 ATOM 286 C CD . LYS A 1 37 ? 27.031 0.922 5.801 1.00 35.68 ? 45 LYS A CD 1 ATOM 287 C CE . LYS A 1 37 ? 26.143 1.088 4.537 1.00 39.00 ? 45 LYS A CE 1 ATOM 288 N NZ . LYS A 1 37 ? 25.525 -0.170 3.956 1.00 35.72 ? 45 LYS A NZ 1 ATOM 289 N N . THR A 1 38 ? 22.655 1.817 9.755 1.00 32.05 ? 46 THR A N 1 ATOM 290 C CA . THR A 1 38 ? 21.962 2.901 10.456 1.00 33.29 ? 46 THR A CA 1 ATOM 291 C C . THR A 1 38 ? 21.026 2.396 11.581 1.00 32.68 ? 46 THR A C 1 ATOM 292 O O . THR A 1 38 ? 20.570 1.239 11.578 1.00 32.43 ? 46 THR A O 1 ATOM 293 C CB . THR A 1 38 ? 21.144 3.764 9.490 1.00 32.99 ? 46 THR A CB 1 ATOM 294 O OG1 . THR A 1 38 ? 20.022 3.004 9.034 1.00 35.90 ? 46 THR A OG1 1 ATOM 295 C CG2 . THR A 1 38 ? 21.976 4.183 8.280 1.00 35.31 ? 46 THR A CG2 1 ATOM 296 N N . HIS A 1 39 ? 20.753 3.281 12.533 1.00 32.02 ? 47 HIS A N 1 ATOM 297 C CA . HIS A 1 39 ? 19.869 2.980 13.656 1.00 31.78 ? 47 HIS A CA 1 ATOM 298 C C . HIS A 1 39 ? 19.239 4.322 14.022 1.00 32.27 ? 47 HIS A C 1 ATOM 299 O O . HIS A 1 39 ? 19.716 5.363 13.530 1.00 33.10 ? 47 HIS A O 1 ATOM 300 C CB . HIS A 1 39 ? 20.668 2.416 14.819 1.00 31.45 ? 47 HIS A CB 1 ATOM 301 C CG . HIS A 1 39 ? 21.756 3.329 15.303 1.00 32.42 ? 47 HIS A CG 1 ATOM 302 N ND1 . HIS A 1 39 ? 21.523 4.362 16.186 1.00 35.08 ? 47 HIS A ND1 1 ATOM 303 C CD2 . HIS A 1 39 ? 23.074 3.388 14.999 1.00 33.66 ? 47 HIS A CD2 1 ATOM 304 C CE1 . HIS A 1 39 ? 22.653 5.007 16.415 1.00 36.24 ? 47 HIS A CE1 1 ATOM 305 N NE2 . HIS A 1 39 ? 23.612 4.428 15.715 1.00 33.57 ? 47 HIS A NE2 1 ATOM 306 N N . ASN A 1 40 ? 18.188 4.323 14.857 1.00 31.12 ? 48 ASN A N 1 ATOM 307 C CA . ASN A 1 40 ? 17.472 5.602 15.160 1.00 30.98 ? 48 ASN A CA 1 ATOM 308 C C . ASN A 1 40 ? 17.992 6.398 16.371 1.00 30.82 ? 48 ASN A C 1 ATOM 309 O O . ASN A 1 40 ? 17.424 7.413 16.734 1.00 31.58 ? 48 ASN A O 1 ATOM 310 C CB . ASN A 1 40 ? 15.976 5.360 15.307 1.00 30.12 ? 48 ASN A CB 1 ATOM 311 C CG . ASN A 1 40 ? 15.637 4.594 16.593 1.00 30.47 ? 48 ASN A CG 1 ATOM 312 O OD1 . ASN A 1 40 ? 16.523 4.252 17.381 1.00 27.03 ? 48 ASN A OD1 1 ATOM 313 N ND2 . ASN A 1 40 ? 14.365 4.325 16.797 1.00 29.36 ? 48 ASN A ND2 1 ATOM 314 N N . GLY A 1 41 ? 19.058 5.919 16.998 1.00 30.78 ? 49 GLY A N 1 ATOM 315 C CA . GLY A 1 41 ? 19.678 6.587 18.135 1.00 30.32 ? 49 GLY A CA 1 ATOM 316 C C . GLY A 1 41 ? 18.875 6.552 19.428 1.00 30.48 ? 49 GLY A C 1 ATOM 317 O O . GLY A 1 41 ? 19.251 7.212 20.392 1.00 30.68 ? 49 GLY A O 1 ATOM 318 N N . LYS A 1 42 ? 17.772 5.798 19.451 1.00 28.95 ? 50 LYS A N 1 ATOM 319 C CA . LYS A 1 42 ? 16.880 5.775 20.616 1.00 28.34 ? 50 LYS A CA 1 ATOM 320 C C . LYS A 1 42 ? 16.778 4.402 21.263 1.00 27.04 ? 50 LYS A C 1 ATOM 321 O O . LYS A 1 42 ? 16.894 3.370 20.587 1.00 25.97 ? 50 LYS A O 1 ATOM 322 C CB . LYS A 1 42 ? 15.471 6.192 20.213 1.00 28.07 ? 50 LYS A CB 1 ATOM 323 C CG . LYS A 1 42 ? 15.360 7.615 19.703 1.00 31.09 ? 50 LYS A CG 1 ATOM 324 C CD . LYS A 1 42 ? 13.974 7.846 19.119 1.00 33.29 ? 50 LYS A CD 1 ATOM 325 C CE . LYS A 1 42 ? 13.903 9.215 18.477 1.00 35.55 ? 50 LYS A CE 1 ATOM 326 N NZ . LYS A 1 42 ? 12.547 9.349 17.954 1.00 41.19 ? 50 LYS A NZ 1 ATOM 327 N N . LEU A 1 43 ? 16.530 4.416 22.570 1.00 26.30 ? 51 LEU A N 1 ATOM 328 C CA . LEU A 1 43 ? 16.062 3.234 23.286 1.00 26.47 ? 51 LEU A CA 1 ATOM 329 C C . LEU A 1 43 ? 14.526 3.170 23.222 1.00 25.91 ? 51 LEU A C 1 ATOM 330 O O . LEU A 1 43 ? 13.849 4.140 23.485 1.00 26.24 ? 51 LEU A O 1 ATOM 331 C CB . LEU A 1 43 ? 16.577 3.286 24.729 1.00 26.68 ? 51 LEU A CB 1 ATOM 332 C CG . LEU A 1 43 ? 18.102 3.480 24.768 1.00 28.55 ? 51 LEU A CG 1 ATOM 333 C CD1 . LEU A 1 43 ? 18.582 3.775 26.170 1.00 30.10 ? 51 LEU A CD1 1 ATOM 334 C CD2 . LEU A 1 43 ? 18.848 2.281 24.200 1.00 32.00 ? 51 LEU A CD2 1 ATOM 335 N N . CYS A 1 44 ? 14.000 2.000 22.891 1.00 26.06 ? 52 CYS A N 1 ATOM 336 C CA . CYS A 1 44 ? 12.615 1.839 22.474 1.00 27.36 ? 52 CYS A CA 1 ATOM 337 C C . CYS A 1 44 ? 11.958 0.663 23.196 1.00 27.25 ? 52 CYS A C 1 ATOM 338 O O . CYS A 1 44 ? 12.642 -0.199 23.756 1.00 24.54 ? 52 CYS A O 1 ATOM 339 C CB . CYS A 1 44 ? 12.599 1.511 20.962 1.00 28.69 ? 52 CYS A CB 1 ATOM 340 S SG . CYS A 1 44 ? 13.199 2.883 19.910 1.00 30.76 ? 52 CYS A SG 1 ATOM 341 N N . LYS A 1 45 ? 10.630 0.619 23.128 1.00 27.17 ? 53 LYS A N 1 ATOM 342 C CA . LYS A 1 45 ? 9.898 -0.580 23.465 1.00 28.75 ? 53 LYS A CA 1 ATOM 343 C C . LYS A 1 45 ? 10.298 -1.653 22.469 1.00 29.81 ? 53 LYS A C 1 ATOM 344 O O . LYS A 1 45 ? 10.584 -1.347 21.307 1.00 29.45 ? 53 LYS A O 1 ATOM 345 C CB . LYS A 1 45 ? 8.387 -0.330 23.354 1.00 29.67 ? 53 LYS A CB 1 ATOM 346 C CG . LYS A 1 45 ? 7.832 0.679 24.346 1.00 31.88 ? 53 LYS A CG 1 ATOM 347 C CD . LYS A 1 45 ? 6.272 0.718 24.249 1.00 35.02 ? 53 LYS A CD 1 ATOM 348 C CE . LYS A 1 45 ? 5.796 1.673 23.184 1.00 39.29 ? 53 LYS A CE 1 ATOM 349 N NZ . LYS A 1 45 ? 6.238 3.056 23.490 1.00 40.42 ? 53 LYS A NZ 1 ATOM 350 N N . LEU A 1 46 A 10.341 -2.907 22.923 1.00 30.75 ? 53 LEU A N 1 ATOM 351 C CA . LEU A 1 46 A 10.653 -4.031 22.059 1.00 32.53 ? 53 LEU A CA 1 ATOM 352 C C . LEU A 1 46 A 9.356 -4.836 21.886 1.00 34.04 ? 53 LEU A C 1 ATOM 353 O O . LEU A 1 46 A 8.829 -5.407 22.859 1.00 33.13 ? 53 LEU A O 1 ATOM 354 C CB . LEU A 1 46 A 11.787 -4.885 22.665 1.00 32.34 ? 53 LEU A CB 1 ATOM 355 C CG . LEU A 1 46 A 12.452 -6.016 21.848 1.00 33.97 ? 53 LEU A CG 1 ATOM 356 C CD1 . LEU A 1 46 A 13.152 -5.499 20.611 1.00 34.93 ? 53 LEU A CD1 1 ATOM 357 C CD2 . LEU A 1 46 A 13.456 -6.797 22.686 1.00 34.76 ? 53 LEU A CD2 1 ATOM 358 N N . ASN A 1 47 ? 8.820 -4.823 20.660 1.00 35.01 ? 54 ASN A N 1 ATOM 359 C CA . ASN A 1 47 ? 7.519 -5.441 20.351 1.00 36.45 ? 54 ASN A CA 1 ATOM 360 C C . ASN A 1 47 ? 6.410 -4.988 21.254 1.00 35.95 ? 54 ASN A C 1 ATOM 361 O O . ASN A 1 47 ? 5.615 -5.811 21.723 1.00 37.61 ? 54 ASN A O 1 ATOM 362 C CB . ASN A 1 47 ? 7.595 -6.961 20.439 1.00 37.44 ? 54 ASN A CB 1 ATOM 363 C CG . ASN A 1 47 ? 8.633 -7.523 19.556 1.00 40.73 ? 54 ASN A CG 1 ATOM 364 O OD1 . ASN A 1 47 ? 9.528 -8.246 20.007 1.00 45.46 ? 54 ASN A OD1 1 ATOM 365 N ND2 . ASN A 1 47 ? 8.564 -7.171 18.272 1.00 45.72 ? 54 ASN A ND2 1 ATOM 366 N N . GLY A 1 48 ? 6.359 -3.691 21.512 1.00 34.29 ? 55 GLY A N 1 ATOM 367 C CA . GLY A 1 48 ? 5.343 -3.123 22.362 1.00 33.40 ? 55 GLY A CA 1 ATOM 368 C C . GLY A 1 48 ? 5.609 -3.220 23.860 1.00 32.18 ? 55 GLY A C 1 ATOM 369 O O . GLY A 1 48 ? 4.864 -2.631 24.623 1.00 31.42 ? 55 GLY A O 1 ATOM 370 N N . ILE A 1 49 ? 6.670 -3.934 24.279 1.00 29.88 ? 56 ILE A N 1 ATOM 371 C CA . ILE A 1 49 ? 6.939 -4.121 25.712 1.00 28.47 ? 56 ILE A CA 1 ATOM 372 C C . ILE A 1 49 ? 8.139 -3.266 26.134 1.00 27.29 ? 56 ILE A C 1 ATOM 373 O O . ILE A 1 49 ? 9.215 -3.436 25.576 1.00 27.75 ? 56 ILE A O 1 ATOM 374 C CB . ILE A 1 49 ? 7.170 -5.618 26.036 1.00 28.14 ? 56 ILE A CB 1 ATOM 375 C CG1 . ILE A 1 49 ? 5.938 -6.443 25.613 1.00 30.14 ? 56 ILE A CG1 1 ATOM 376 C CG2 . ILE A 1 49 ? 7.498 -5.825 27.550 1.00 27.04 ? 56 ILE A CG2 1 ATOM 377 C CD1 . ILE A 1 49 ? 6.179 -7.956 25.684 1.00 31.46 ? 56 ILE A CD1 1 ATOM 378 N N . PRO A 1 50 ? 7.946 -2.341 27.100 1.00 27.03 ? 57 PRO A N 1 ATOM 379 C CA . PRO A 1 50 ? 8.988 -1.407 27.516 1.00 25.49 ? 57 PRO A CA 1 ATOM 380 C C . PRO A 1 50 ? 10.053 -2.120 28.320 1.00 24.95 ? 57 PRO A C 1 ATOM 381 O O . PRO A 1 50 ? 9.743 -3.101 28.999 1.00 23.70 ? 57 PRO A O 1 ATOM 382 C CB . PRO A 1 50 ? 8.262 -0.417 28.436 1.00 26.48 ? 57 PRO A CB 1 ATOM 383 C CG . PRO A 1 50 ? 6.762 -0.729 28.289 1.00 26.25 ? 57 PRO A CG 1 ATOM 384 C CD . PRO A 1 50 ? 6.668 -2.118 27.817 1.00 26.35 ? 57 PRO A CD 1 ATOM 385 N N . PRO A 1 51 ? 11.296 -1.614 28.258 1.00 23.49 ? 58 PRO A N 1 ATOM 386 C CA . PRO A 1 51 ? 12.348 -2.171 29.120 1.00 23.02 ? 58 PRO A CA 1 ATOM 387 C C . PRO A 1 51 ? 12.068 -1.761 30.551 1.00 22.76 ? 58 PRO A C 1 ATOM 388 O O . PRO A 1 51 ? 11.206 -0.886 30.791 1.00 23.42 ? 58 PRO A O 1 ATOM 389 C CB . PRO A 1 51 ? 13.635 -1.452 28.651 1.00 22.36 ? 58 PRO A CB 1 ATOM 390 C CG . PRO A 1 51 ? 13.145 -0.146 27.990 1.00 22.67 ? 58 PRO A CG 1 ATOM 391 C CD . PRO A 1 51 ? 11.801 -0.554 27.349 1.00 23.31 ? 58 PRO A CD 1 ATOM 392 N N . LEU A 1 52 ? 12.808 -2.373 31.469 1.00 21.80 ? 59 LEU A N 1 ATOM 393 C CA . LEU A 1 52 ? 12.842 -1.922 32.840 1.00 21.91 ? 59 LEU A CA 1 ATOM 394 C C . LEU A 1 52 ? 13.967 -0.892 32.893 1.00 22.02 ? 59 LEU A C 1 ATOM 395 O O . LEU A 1 52 ? 15.108 -1.225 32.672 1.00 20.84 ? 59 LEU A O 1 ATOM 396 C CB . LEU A 1 52 ? 13.140 -3.081 33.780 1.00 21.97 ? 59 LEU A CB 1 ATOM 397 C CG . LEU A 1 52 ? 13.451 -2.711 35.244 1.00 21.15 ? 59 LEU A CG 1 ATOM 398 C CD1 . LEU A 1 52 ? 12.322 -1.896 35.879 1.00 21.73 ? 59 LEU A CD1 1 ATOM 399 C CD2 . LEU A 1 52 ? 13.762 -4.022 36.004 1.00 18.96 ? 59 LEU A CD2 1 ATOM 400 N N . GLU A 1 53 ? 13.617 0.363 33.133 1.00 21.51 ? 60 GLU A N 1 ATOM 401 C CA . GLU A 1 53 ? 14.620 1.414 33.204 1.00 22.69 ? 60 GLU A CA 1 ATOM 402 C C . GLU A 1 53 ? 15.081 1.599 34.659 1.00 22.82 ? 60 GLU A C 1 ATOM 403 O O . GLU A 1 53 ? 14.355 2.145 35.485 1.00 22.59 ? 60 GLU A O 1 ATOM 404 C CB . GLU A 1 53 ? 14.055 2.728 32.644 1.00 23.52 ? 60 GLU A CB 1 ATOM 405 C CG . GLU A 1 53 ? 15.059 3.864 32.778 1.00 27.18 ? 60 GLU A CG 1 ATOM 406 C CD . GLU A 1 53 ? 14.880 5.003 31.806 1.00 30.98 ? 60 GLU A CD 1 ATOM 407 O OE1 . GLU A 1 53 ? 14.043 4.912 30.862 1.00 28.94 ? 60 GLU A OE1 1 ATOM 408 O OE2 . GLU A 1 53 ? 15.631 5.994 32.001 1.00 32.16 ? 60 GLU A OE2 1 ATOM 409 N N . LEU A 1 54 ? 16.286 1.131 34.983 1.00 22.11 ? 61 LEU A N 1 ATOM 410 C CA . LEU A 1 54 ? 16.762 1.234 36.384 1.00 21.63 ? 61 LEU A CA 1 ATOM 411 C C . LEU A 1 54 ? 17.127 2.673 36.831 1.00 22.21 ? 61 LEU A C 1 ATOM 412 O O . LEU A 1 54 ? 17.222 2.972 38.045 1.00 21.88 ? 61 LEU A O 1 ATOM 413 C CB . LEU A 1 54 ? 17.925 0.276 36.624 1.00 20.24 ? 61 LEU A CB 1 ATOM 414 C CG . LEU A 1 54 ? 17.642 -1.224 36.453 1.00 19.26 ? 61 LEU A CG 1 ATOM 415 C CD1 . LEU A 1 54 ? 18.964 -2.015 36.678 1.00 19.18 ? 61 LEU A CD1 1 ATOM 416 C CD2 . LEU A 1 54 ? 16.519 -1.662 37.444 1.00 20.18 ? 61 LEU A CD2 1 ATOM 417 N N . GLY A 1 55 ? 17.310 3.562 35.865 1.00 21.81 ? 62 GLY A N 1 ATOM 418 C CA . GLY A 1 55 ? 17.726 4.952 36.172 1.00 22.64 ? 62 GLY A CA 1 ATOM 419 C C . GLY A 1 55 ? 19.078 4.955 36.884 1.00 23.07 ? 62 GLY A C 1 ATOM 420 O O . GLY A 1 55 ? 20.079 4.457 36.346 1.00 23.13 ? 62 GLY A O 1 ATOM 421 N N . ASP A 1 56 ? 19.120 5.469 38.116 1.00 23.81 ? 63 ASP A N 1 ATOM 422 C CA . ASP A 1 56 ? 20.374 5.486 38.891 1.00 24.59 ? 63 ASP A CA 1 ATOM 423 C C . ASP A 1 56 ? 20.613 4.251 39.771 1.00 24.56 ? 63 ASP A C 1 ATOM 424 O O . ASP A 1 56 ? 21.612 4.199 40.503 1.00 24.50 ? 63 ASP A O 1 ATOM 425 C CB . ASP A 1 56 ? 20.491 6.761 39.750 1.00 25.27 ? 63 ASP A CB 1 ATOM 426 C CG . ASP A 1 56 ? 20.700 8.022 38.902 1.00 27.96 ? 63 ASP A CG 1 ATOM 427 O OD1 . ASP A 1 56 ? 21.496 8.011 37.946 1.00 29.07 ? 63 ASP A OD1 1 ATOM 428 O OD2 . ASP A 1 56 ? 20.036 9.018 39.197 1.00 29.93 ? 63 ASP A OD2 1 ATOM 429 N N . CYS A 1 57 ? 19.701 3.278 39.713 1.00 24.35 ? 64 CYS A N 1 ATOM 430 C CA . CYS A 1 57 ? 19.760 2.078 40.582 1.00 24.11 ? 64 CYS A CA 1 ATOM 431 C C . CYS A 1 57 ? 20.533 0.937 39.929 1.00 22.79 ? 64 CYS A C 1 ATOM 432 O O . CYS A 1 57 ? 20.534 0.793 38.709 1.00 23.21 ? 64 CYS A O 1 ATOM 433 C CB . CYS A 1 57 ? 18.336 1.612 40.926 1.00 25.22 ? 64 CYS A CB 1 ATOM 434 S SG . CYS A 1 57 ? 17.516 2.898 41.918 1.00 30.34 ? 64 CYS A SG 1 ATOM 435 N N . SER A 1 58 ? 21.212 0.148 40.731 1.00 20.76 ? 65 SER A N 1 ATOM 436 C CA . SER A 1 58 ? 21.813 -1.073 40.238 1.00 20.37 ? 65 SER A CA 1 ATOM 437 C C . SER A 1 58 ? 20.803 -2.195 40.434 1.00 20.25 ? 65 SER A C 1 ATOM 438 O O . SER A 1 58 ? 19.795 -2.011 41.104 1.00 20.08 ? 65 SER A O 1 ATOM 439 C CB . SER A 1 58 ? 23.094 -1.385 41.003 1.00 20.64 ? 65 SER A CB 1 ATOM 440 O OG . SER A 1 58 ? 22.800 -1.747 42.340 1.00 19.64 ? 65 SER A OG 1 ATOM 441 N N . ILE A 1 59 ? 21.065 -3.345 39.829 1.00 19.56 ? 66 ILE A N 1 ATOM 442 C CA . ILE A 1 59 ? 20.266 -4.548 40.069 1.00 19.53 ? 66 ILE A CA 1 ATOM 443 C C . ILE A 1 59 ? 20.136 -4.824 41.584 1.00 18.98 ? 66 ILE A C 1 ATOM 444 O O . ILE A 1 59 ? 19.032 -5.085 42.117 1.00 18.77 ? 66 ILE A O 1 ATOM 445 C CB . ILE A 1 59 ? 20.915 -5.755 39.330 1.00 20.22 ? 66 ILE A CB 1 ATOM 446 C CG1 . ILE A 1 59 ? 20.835 -5.525 37.797 1.00 19.70 ? 66 ILE A CG1 1 ATOM 447 C CG2 . ILE A 1 59 ? 20.260 -7.111 39.723 1.00 20.65 ? 66 ILE A CG2 1 ATOM 448 C CD1 . ILE A 1 59 ? 19.440 -5.680 37.246 1.00 22.04 ? 66 ILE A CD1 1 ATOM 449 N N . ALA A 1 60 ? 21.256 -4.747 42.281 1.00 17.76 ? 67 ALA A N 1 ATOM 450 C CA . ALA A 1 60 ? 21.258 -4.928 43.740 1.00 17.74 ? 67 ALA A CA 1 ATOM 451 C C . ALA A 1 60 ? 20.397 -3.886 44.457 1.00 17.64 ? 67 ALA A C 1 ATOM 452 O O . ALA A 1 60 ? 19.631 -4.250 45.353 1.00 18.05 ? 67 ALA A O 1 ATOM 453 C CB . ALA A 1 60 ? 22.713 -4.947 44.323 1.00 17.76 ? 67 ALA A CB 1 ATOM 454 N N . GLY A 1 61 ? 20.533 -2.610 44.094 1.00 18.01 ? 68 GLY A N 1 ATOM 455 C CA . GLY A 1 61 ? 19.691 -1.521 44.672 1.00 17.71 ? 68 GLY A CA 1 ATOM 456 C C . GLY A 1 61 ? 18.204 -1.801 44.517 1.00 17.99 ? 68 GLY A C 1 ATOM 457 O O . GLY A 1 61 ? 17.418 -1.648 45.451 1.00 18.67 ? 68 GLY A O 1 ATOM 458 N N . TRP A 1 62 ? 17.825 -2.213 43.319 1.00 17.48 ? 69 TRP A N 1 ATOM 459 C CA . TRP A 1 62 ? 16.462 -2.647 43.038 1.00 17.66 ? 69 TRP A CA 1 ATOM 460 C C . TRP A 1 62 ? 16.020 -3.796 43.942 1.00 17.30 ? 69 TRP A C 1 ATOM 461 O O . TRP A 1 62 ? 14.996 -3.684 44.634 1.00 18.91 ? 69 TRP A O 1 ATOM 462 C CB . TRP A 1 62 ? 16.367 -3.028 41.546 1.00 17.61 ? 69 TRP A CB 1 ATOM 463 C CG . TRP A 1 62 ? 15.126 -3.782 41.118 1.00 19.01 ? 69 TRP A CG 1 ATOM 464 C CD1 . TRP A 1 62 ? 13.828 -3.648 41.601 1.00 20.63 ? 69 TRP A CD1 1 ATOM 465 C CD2 . TRP A 1 62 ? 15.066 -4.778 40.090 1.00 18.52 ? 69 TRP A CD2 1 ATOM 466 N NE1 . TRP A 1 62 ? 12.982 -4.517 40.912 1.00 19.37 ? 69 TRP A NE1 1 ATOM 467 C CE2 . TRP A 1 62 ? 13.720 -5.226 40.001 1.00 18.91 ? 69 TRP A CE2 1 ATOM 468 C CE3 . TRP A 1 62 ? 16.018 -5.336 39.237 1.00 19.50 ? 69 TRP A CE3 1 ATOM 469 C CZ2 . TRP A 1 62 ? 13.313 -6.214 39.091 1.00 17.20 ? 69 TRP A CZ2 1 ATOM 470 C CZ3 . TRP A 1 62 ? 15.614 -6.355 38.348 1.00 18.06 ? 69 TRP A CZ3 1 ATOM 471 C CH2 . TRP A 1 62 ? 14.263 -6.763 38.283 1.00 19.45 ? 69 TRP A CH2 1 ATOM 472 N N . LEU A 1 63 ? 16.757 -4.908 43.944 1.00 16.98 ? 70 LEU A N 1 ATOM 473 C CA . LEU A 1 63 ? 16.227 -6.123 44.547 1.00 17.83 ? 70 LEU A CA 1 ATOM 474 C C . LEU A 1 63 ? 16.253 -6.027 46.101 1.00 17.82 ? 70 LEU A C 1 ATOM 475 O O . LEU A 1 63 ? 15.342 -6.500 46.757 1.00 16.58 ? 70 LEU A O 1 ATOM 476 C CB . LEU A 1 63 ? 16.979 -7.371 44.020 1.00 18.19 ? 70 LEU A CB 1 ATOM 477 C CG . LEU A 1 63 ? 16.768 -7.592 42.510 1.00 18.93 ? 70 LEU A CG 1 ATOM 478 C CD1 . LEU A 1 63 ? 17.645 -8.748 42.013 1.00 18.21 ? 70 LEU A CD1 1 ATOM 479 C CD2 . LEU A 1 63 ? 15.257 -7.798 42.153 1.00 18.42 ? 70 LEU A CD2 1 ATOM 480 N N . LEU A 1 64 ? 17.257 -5.334 46.646 1.00 16.80 ? 71 LEU A N 1 ATOM 481 C CA . LEU A 1 64 ? 17.335 -5.125 48.097 1.00 17.07 ? 71 LEU A CA 1 ATOM 482 C C . LEU A 1 64 ? 16.299 -4.071 48.545 1.00 18.69 ? 71 LEU A C 1 ATOM 483 O O . LEU A 1 64 ? 15.807 -4.106 49.685 1.00 18.25 ? 71 LEU A O 1 ATOM 484 C CB . LEU A 1 64 ? 18.736 -4.662 48.488 1.00 17.66 ? 71 LEU A CB 1 ATOM 485 C CG . LEU A 1 64 ? 19.819 -5.752 48.333 1.00 18.37 ? 71 LEU A CG 1 ATOM 486 C CD1 . LEU A 1 64 ? 21.163 -5.092 48.474 1.00 16.39 ? 71 LEU A CD1 1 ATOM 487 C CD2 . LEU A 1 64 ? 19.633 -6.860 49.374 1.00 18.76 ? 71 LEU A CD2 1 ATOM 488 N N . GLY A 1 65 ? 15.963 -3.167 47.636 1.00 18.13 ? 72 GLY A N 1 ATOM 489 C CA . GLY A 1 65 ? 15.036 -2.054 47.961 1.00 19.62 ? 72 GLY A CA 1 ATOM 490 C C . GLY A 1 65 ? 15.751 -0.873 48.591 1.00 19.06 ? 72 GLY A C 1 ATOM 491 O O . GLY A 1 65 ? 15.319 -0.360 49.639 1.00 19.25 ? 72 GLY A O 1 ATOM 492 N N . ASN A 1 66 ? 16.857 -0.469 47.990 1.00 18.83 ? 73 ASN A N 1 ATOM 493 C CA . ASN A 1 66 ? 17.557 0.787 48.371 1.00 19.29 ? 73 ASN A CA 1 ATOM 494 C C . ASN A 1 66 ? 16.482 1.884 48.326 1.00 19.49 ? 73 ASN A C 1 ATOM 495 O O . ASN A 1 66 ? 15.742 1.953 47.330 1.00 19.87 ? 73 ASN A O 1 ATOM 496 C CB . ASN A 1 66 ? 18.707 1.031 47.378 1.00 17.95 ? 73 ASN A CB 1 ATOM 497 C CG . ASN A 1 66 ? 19.458 2.375 47.613 1.00 19.77 ? 73 ASN A CG 1 ATOM 498 O OD1 . ASN A 1 66 ? 18.855 3.353 47.986 1.00 21.02 ? 73 ASN A OD1 1 ATOM 499 N ND2 . ASN A 1 66 ? 20.769 2.411 47.301 1.00 17.71 ? 73 ASN A ND2 1 ATOM 500 N N . PRO A 1 67 ? 16.304 2.658 49.418 1.00 20.42 ? 74 PRO A N 1 ATOM 501 C CA . PRO A 1 67 ? 15.174 3.588 49.391 1.00 22.02 ? 74 PRO A CA 1 ATOM 502 C C . PRO A 1 67 ? 15.209 4.613 48.272 1.00 23.20 ? 74 PRO A C 1 ATOM 503 O O . PRO A 1 67 ? 14.181 5.210 48.004 1.00 24.79 ? 74 PRO A O 1 ATOM 504 C CB . PRO A 1 67 ? 15.269 4.325 50.740 1.00 22.91 ? 74 PRO A CB 1 ATOM 505 C CG . PRO A 1 67 ? 15.869 3.324 51.645 1.00 21.90 ? 74 PRO A CG 1 ATOM 506 C CD . PRO A 1 67 ? 16.892 2.587 50.770 1.00 20.04 ? 74 PRO A CD 1 ATOM 507 N N . GLU A 1 68 ? 16.361 4.823 47.646 1.00 23.99 ? 75 GLU A N 1 ATOM 508 C CA . GLU A 1 68 ? 16.446 5.734 46.498 1.00 25.26 ? 75 GLU A CA 1 ATOM 509 C C . GLU A 1 68 ? 15.861 5.065 45.250 1.00 25.20 ? 75 GLU A C 1 ATOM 510 O O . GLU A 1 68 ? 15.713 5.714 44.218 1.00 24.84 ? 75 GLU A O 1 ATOM 511 C CB . GLU A 1 68 ? 17.893 6.161 46.224 1.00 25.60 ? 75 GLU A CB 1 ATOM 512 C CG . GLU A 1 68 ? 18.583 6.886 47.369 1.00 28.38 ? 75 GLU A CG 1 ATOM 513 C CD . GLU A 1 68 ? 18.078 8.314 47.615 1.00 36.40 ? 75 GLU A CD 1 ATOM 514 O OE1 . GLU A 1 68 ? 17.440 8.915 46.720 1.00 35.94 ? 75 GLU A OE1 1 ATOM 515 O OE2 . GLU A 1 68 ? 18.343 8.846 48.726 1.00 40.20 ? 75 GLU A OE2 1 ATOM 516 N N . CYS A 1 69 ? 15.501 3.784 45.363 1.00 24.54 ? 76 CYS A N 1 ATOM 517 C CA . CYS A 1 69 ? 14.978 3.023 44.230 1.00 25.54 ? 76 CYS A CA 1 ATOM 518 C C . CYS A 1 69 ? 13.477 2.731 44.364 1.00 25.06 ? 76 CYS A C 1 ATOM 519 O O . CYS A 1 69 ? 12.974 1.804 43.702 1.00 23.90 ? 76 CYS A O 1 ATOM 520 C CB . CYS A 1 69 ? 15.776 1.696 44.072 1.00 24.26 ? 76 CYS A CB 1 ATOM 521 S SG . CYS A 1 69 ? 17.542 2.057 43.847 1.00 30.92 ? 76 CYS A SG 1 ATOM 522 N N . ASP A 1 70 ? 12.767 3.519 45.188 1.00 25.29 ? 77 ASP A N 1 ATOM 523 C CA . ASP A 1 70 ? 11.363 3.199 45.531 1.00 25.70 ? 77 ASP A CA 1 ATOM 524 C C . ASP A 1 70 ? 10.392 3.128 44.357 1.00 25.66 ? 77 ASP A C 1 ATOM 525 O O . ASP A 1 70 ? 9.405 2.398 44.436 1.00 23.68 ? 77 ASP A O 1 ATOM 526 C CB . ASP A 1 70 ? 10.791 4.124 46.612 1.00 27.12 ? 77 ASP A CB 1 ATOM 527 C CG . ASP A 1 70 ? 11.211 3.701 47.997 1.00 29.98 ? 77 ASP A CG 1 ATOM 528 O OD1 . ASP A 1 70 ? 11.889 2.665 48.127 1.00 32.10 ? 77 ASP A OD1 1 ATOM 529 O OD2 . ASP A 1 70 ? 10.883 4.408 48.951 1.00 32.62 ? 77 ASP A OD2 1 ATOM 530 N N . ARG A 1 71 ? 10.661 3.869 43.280 1.00 25.84 ? 78 ARG A N 1 ATOM 531 C CA . ARG A 1 71 ? 9.870 3.733 42.060 1.00 27.39 ? 78 ARG A CA 1 ATOM 532 C C . ARG A 1 71 ? 9.839 2.284 41.536 1.00 26.49 ? 78 ARG A C 1 ATOM 533 O O . ARG A 1 71 ? 8.956 1.940 40.763 1.00 27.00 ? 78 ARG A O 1 ATOM 534 C CB . ARG A 1 71 ? 10.368 4.662 40.935 1.00 28.87 ? 78 ARG A CB 1 ATOM 535 C CG . ARG A 1 71 ? 11.759 4.330 40.401 1.00 31.66 ? 78 ARG A CG 1 ATOM 536 C CD . ARG A 1 71 ? 12.198 5.283 39.254 1.00 39.40 ? 78 ARG A CD 1 ATOM 537 N NE . ARG A 1 71 ? 13.667 5.352 39.046 1.00 44.23 ? 78 ARG A NE 1 ATOM 538 C CZ . ARG A 1 71 ? 14.617 5.383 40.002 1.00 45.35 ? 78 ARG A CZ 1 ATOM 539 N NH1 . ARG A 1 71 ? 14.287 5.367 41.297 1.00 46.22 ? 78 ARG A NH1 1 ATOM 540 N NH2 . ARG A 1 71 ? 15.925 5.471 39.671 1.00 43.83 ? 78 ARG A NH2 1 ATOM 541 N N . LEU A 1 72 ? 10.792 1.452 41.958 1.00 23.98 ? 79 LEU A N 1 ATOM 542 C CA . LEU A 1 72 ? 10.924 0.100 41.454 1.00 23.33 ? 79 LEU A CA 1 ATOM 543 C C . LEU A 1 72 ? 10.324 -0.948 42.424 1.00 23.31 ? 79 LEU A C 1 ATOM 544 O O . LEU A 1 72 ? 10.535 -2.143 42.249 1.00 22.67 ? 79 LEU A O 1 ATOM 545 C CB . LEU A 1 72 ? 12.412 -0.226 41.218 1.00 22.60 ? 79 LEU A CB 1 ATOM 546 C CG . LEU A 1 72 ? 13.264 0.721 40.344 1.00 22.89 ? 79 LEU A CG 1 ATOM 547 C CD1 . LEU A 1 72 ? 14.747 0.210 40.280 1.00 22.43 ? 79 LEU A CD1 1 ATOM 548 C CD2 . LEU A 1 72 ? 12.672 0.895 38.935 1.00 20.98 ? 79 LEU A CD2 1 ATOM 549 N N . LEU A 1 73 ? 9.626 -0.505 43.464 1.00 22.95 ? 80 LEU A N 1 ATOM 550 C CA . LEU A 1 73 ? 9.069 -1.442 44.450 1.00 23.75 ? 80 LEU A CA 1 ATOM 551 C C . LEU A 1 73 ? 8.061 -2.432 43.831 1.00 24.17 ? 80 LEU A C 1 ATOM 552 O O . LEU A 1 73 ? 7.925 -3.560 44.299 1.00 23.47 ? 80 LEU A O 1 ATOM 553 C CB . LEU A 1 73 ? 8.425 -0.694 45.635 1.00 23.98 ? 80 LEU A CB 1 ATOM 554 C CG . LEU A 1 73 ? 9.493 -0.163 46.594 1.00 23.97 ? 80 LEU A CG 1 ATOM 555 C CD1 . LEU A 1 73 ? 8.906 0.857 47.533 1.00 22.42 ? 80 LEU A CD1 1 ATOM 556 C CD2 . LEU A 1 73 ? 10.167 -1.344 47.378 1.00 24.61 ? 80 LEU A CD2 1 ATOM 557 N N . SER A 1 74 ? 7.361 -1.991 42.792 1.00 23.99 ? 81 SER A N 1 ATOM 558 C CA . SER A 1 74 ? 6.534 -2.905 42.024 1.00 25.39 ? 81 SER A CA 1 ATOM 559 C C . SER A 1 74 ? 6.727 -2.598 40.554 1.00 24.59 ? 81 SER A C 1 ATOM 560 O O . SER A 1 74 ? 6.417 -1.511 40.126 1.00 25.64 ? 81 SER A O 1 ATOM 561 C CB . SER A 1 74 ? 5.041 -2.798 42.392 1.00 25.60 ? 81 SER A CB 1 ATOM 562 O OG . SER A 1 74 ? 4.349 -3.745 41.591 1.00 28.48 ? 81 SER A OG 1 ATOM 563 N N . VAL A 1 75 A 7.247 -3.541 39.780 1.00 23.65 ? 81 VAL A N 1 ATOM 564 C CA . VAL A 1 75 A 7.414 -3.265 38.355 1.00 23.83 ? 81 VAL A CA 1 ATOM 565 C C . VAL A 1 75 A 6.694 -4.267 37.439 1.00 23.49 ? 81 VAL A C 1 ATOM 566 O O . VAL A 1 75 A 6.610 -5.456 37.740 1.00 23.34 ? 81 VAL A O 1 ATOM 567 C CB . VAL A 1 75 A 8.914 -3.136 37.934 1.00 24.03 ? 81 VAL A CB 1 ATOM 568 C CG1 . VAL A 1 75 A 9.629 -1.948 38.654 1.00 23.92 ? 81 VAL A CG1 1 ATOM 569 C CG2 . VAL A 1 75 A 9.648 -4.437 38.186 1.00 22.89 ? 81 VAL A CG2 1 ATOM 570 N N . PRO A 1 76 ? 6.228 -3.796 36.283 1.00 24.28 ? 82 PRO A N 1 ATOM 571 C CA . PRO A 1 76 ? 5.533 -4.723 35.376 1.00 24.35 ? 82 PRO A CA 1 ATOM 572 C C . PRO A 1 76 ? 6.518 -5.492 34.496 1.00 24.19 ? 82 PRO A C 1 ATOM 573 O O . PRO A 1 76 ? 7.726 -5.203 34.514 1.00 23.63 ? 82 PRO A O 1 ATOM 574 C CB . PRO A 1 76 ? 4.692 -3.785 34.531 1.00 25.42 ? 82 PRO A CB 1 ATOM 575 C CG . PRO A 1 76 ? 5.565 -2.523 34.437 1.00 24.88 ? 82 PRO A CG 1 ATOM 576 C CD . PRO A 1 76 ? 6.145 -2.390 35.823 1.00 24.32 ? 82 PRO A CD 1 ATOM 577 N N . GLU A 1 77 ? 6.018 -6.443 33.726 1.00 22.87 ? 83 GLU A N 1 ATOM 578 C CA . GLU A 1 77 ? 6.830 -7.230 32.820 1.00 24.54 ? 83 GLU A CA 1 ATOM 579 C C . GLU A 1 77 ? 7.725 -6.337 31.929 1.00 23.02 ? 83 GLU A C 1 ATOM 580 O O . GLU A 1 77 ? 7.305 -5.263 31.502 1.00 24.64 ? 83 GLU A O 1 ATOM 581 C CB . GLU A 1 77 ? 5.905 -8.105 31.962 1.00 25.26 ? 83 GLU A CB 1 ATOM 582 C CG . GLU A 1 77 ? 6.614 -8.937 30.938 1.00 30.64 ? 83 GLU A CG 1 ATOM 583 C CD . GLU A 1 77 ? 5.633 -9.566 29.915 1.00 36.93 ? 83 GLU A CD 1 ATOM 584 O OE1 . GLU A 1 77 ? 4.426 -9.617 30.179 1.00 40.33 ? 83 GLU A OE1 1 ATOM 585 O OE2 . GLU A 1 77 ? 6.091 -10.022 28.852 1.00 42.37 ? 83 GLU A OE2 1 ATOM 586 N N . TRP A 1 78 ? 8.953 -6.768 31.677 1.00 23.25 ? 84 TRP A N 1 ATOM 587 C CA . TRP A 1 78 ? 9.877 -6.006 30.814 1.00 22.64 ? 84 TRP A CA 1 ATOM 588 C C . TRP A 1 78 ? 10.399 -6.833 29.642 1.00 22.29 ? 84 TRP A C 1 ATOM 589 O O . TRP A 1 78 ? 10.351 -8.081 29.658 1.00 22.62 ? 84 TRP A O 1 ATOM 590 C CB . TRP A 1 78 ? 11.093 -5.474 31.617 1.00 22.16 ? 84 TRP A CB 1 ATOM 591 C CG . TRP A 1 78 ? 11.896 -6.578 32.302 1.00 20.69 ? 84 TRP A CG 1 ATOM 592 C CD1 . TRP A 1 78 ? 12.905 -7.310 31.755 1.00 22.57 ? 84 TRP A CD1 1 ATOM 593 C CD2 . TRP A 1 78 ? 11.715 -7.096 33.645 1.00 20.08 ? 84 TRP A CD2 1 ATOM 594 N NE1 . TRP A 1 78 ? 13.376 -8.225 32.662 1.00 22.51 ? 84 TRP A NE1 1 ATOM 595 C CE2 . TRP A 1 78 ? 12.654 -8.118 33.823 1.00 21.08 ? 84 TRP A CE2 1 ATOM 596 C CE3 . TRP A 1 78 ? 10.842 -6.781 34.707 1.00 19.99 ? 84 TRP A CE3 1 ATOM 597 C CZ2 . TRP A 1 78 ? 12.763 -8.851 35.027 1.00 21.92 ? 84 TRP A CZ2 1 ATOM 598 C CZ3 . TRP A 1 78 ? 10.955 -7.489 35.899 1.00 17.51 ? 84 TRP A CZ3 1 ATOM 599 C CH2 . TRP A 1 78 ? 11.895 -8.533 36.041 1.00 18.70 ? 84 TRP A CH2 1 ATOM 600 N N . SER A 1 79 ? 10.976 -6.135 28.663 1.00 22.74 ? 85 SER A N 1 ATOM 601 C CA . SER A 1 79 ? 11.566 -6.779 27.500 1.00 23.42 ? 85 SER A CA 1 ATOM 602 C C . SER A 1 79 ? 13.101 -6.815 27.540 1.00 23.39 ? 85 SER A C 1 ATOM 603 O O . SER A 1 79 ? 13.701 -7.668 26.925 1.00 23.06 ? 85 SER A O 1 ATOM 604 C CB . SER A 1 79 ? 11.098 -6.066 26.241 1.00 23.59 ? 85 SER A CB 1 ATOM 605 O OG . SER A 1 79 ? 11.361 -4.688 26.335 1.00 24.83 ? 85 SER A OG 1 ATOM 606 N N . TYR A 1 80 ? 13.710 -5.835 28.206 1.00 23.18 ? 86 TYR A N 1 ATOM 607 C CA . TYR A 1 80 ? 15.126 -5.862 28.548 1.00 22.73 ? 86 TYR A CA 1 ATOM 608 C C . TYR A 1 80 ? 15.326 -4.972 29.772 1.00 22.65 ? 86 TYR A C 1 ATOM 609 O O . TYR A 1 80 ? 14.397 -4.263 30.199 1.00 22.82 ? 86 TYR A O 1 ATOM 610 C CB . TYR A 1 80 ? 16.023 -5.455 27.345 1.00 23.23 ? 86 TYR A CB 1 ATOM 611 C CG . TYR A 1 80 ? 15.746 -4.112 26.709 1.00 22.49 ? 86 TYR A CG 1 ATOM 612 C CD1 . TYR A 1 80 ? 16.595 -3.030 26.934 1.00 23.32 ? 86 TYR A CD1 1 ATOM 613 C CD2 . TYR A 1 80 ? 14.667 -3.931 25.840 1.00 22.34 ? 86 TYR A CD2 1 ATOM 614 C CE1 . TYR A 1 80 ? 16.345 -1.784 26.361 1.00 25.08 ? 86 TYR A CE1 1 ATOM 615 C CE2 . TYR A 1 80 ? 14.409 -2.674 25.249 1.00 20.01 ? 86 TYR A CE2 1 ATOM 616 C CZ . TYR A 1 80 ? 15.250 -1.623 25.511 1.00 22.32 ? 86 TYR A CZ 1 ATOM 617 O OH . TYR A 1 80 ? 15.014 -0.394 24.944 1.00 25.33 ? 86 TYR A OH 1 ATOM 618 N N . ILE A 1 81 ? 16.514 -4.999 30.360 1.00 21.09 ? 87 ILE A N 1 ATOM 619 C CA . ILE A 1 81 ? 16.777 -4.122 31.511 1.00 21.69 ? 87 ILE A CA 1 ATOM 620 C C . ILE A 1 81 ? 17.853 -3.077 31.136 1.00 21.60 ? 87 ILE A C 1 ATOM 621 O O . ILE A 1 81 ? 18.860 -3.422 30.546 1.00 22.25 ? 87 ILE A O 1 ATOM 622 C CB . ILE A 1 81 ? 17.221 -4.950 32.736 1.00 19.95 ? 87 ILE A CB 1 ATOM 623 C CG1 . ILE A 1 81 ? 16.094 -5.918 33.133 1.00 20.26 ? 87 ILE A CG1 1 ATOM 624 C CG2 . ILE A 1 81 ? 17.576 -4.032 33.945 1.00 20.64 ? 87 ILE A CG2 1 ATOM 625 C CD1 . ILE A 1 81 ? 16.494 -6.880 34.240 1.00 21.49 ? 87 ILE A CD1 1 ATOM 626 N N . MET A 1 82 ? 17.619 -1.812 31.435 1.00 21.75 ? 88 MET A N 1 ATOM 627 C CA . MET A 1 82 ? 18.639 -0.781 31.164 1.00 21.65 ? 88 MET A CA 1 ATOM 628 C C . MET A 1 82 ? 19.345 -0.471 32.457 1.00 21.58 ? 88 MET A C 1 ATOM 629 O O . MET A 1 82 ? 18.719 -0.048 33.433 1.00 21.20 ? 88 MET A O 1 ATOM 630 C CB . MET A 1 82 ? 18.014 0.478 30.602 1.00 22.18 ? 88 MET A CB 1 ATOM 631 C CG . MET A 1 82 ? 17.283 0.268 29.255 1.00 22.13 ? 88 MET A CG 1 ATOM 632 S SD . MET A 1 82 ? 16.045 1.535 28.964 1.00 26.51 ? 88 MET A SD 1 ATOM 633 C CE . MET A 1 82 ? 16.936 3.065 29.327 1.00 27.03 ? 88 MET A CE 1 ATOM 634 N N . GLU A 1 83 ? 20.656 -0.687 32.484 1.00 21.28 ? 89 GLU A N 1 ATOM 635 C CA . GLU A 1 83 ? 21.429 -0.330 33.676 1.00 22.30 ? 89 GLU A CA 1 ATOM 636 C C . GLU A 1 83 ? 22.582 0.595 33.278 1.00 22.41 ? 89 GLU A C 1 ATOM 637 O O . GLU A 1 83 ? 23.203 0.388 32.234 1.00 22.87 ? 89 GLU A O 1 ATOM 638 C CB . GLU A 1 83 ? 21.990 -1.583 34.369 1.00 21.56 ? 89 GLU A CB 1 ATOM 639 C CG . GLU A 1 83 ? 22.564 -1.317 35.772 1.00 21.92 ? 89 GLU A CG 1 ATOM 640 C CD . GLU A 1 83 ? 23.236 -2.529 36.398 1.00 25.20 ? 89 GLU A CD 1 ATOM 641 O OE1 . GLU A 1 83 ? 23.911 -3.300 35.672 1.00 26.40 ? 89 GLU A OE1 1 ATOM 642 O OE2 . GLU A 1 83 ? 23.117 -2.700 37.636 1.00 23.70 ? 89 GLU A OE2 1 ATOM 643 N N . LYS A 1 84 ? 22.871 1.590 34.113 1.00 22.66 ? 90 LYS A N 1 ATOM 644 C CA . LYS A 1 84 ? 24.030 2.464 33.860 1.00 23.55 ? 90 LYS A CA 1 ATOM 645 C C . LYS A 1 84 ? 25.334 1.739 34.118 1.00 25.11 ? 90 LYS A C 1 ATOM 646 O O . LYS A 1 84 ? 25.355 0.707 34.798 1.00 24.34 ? 90 LYS A O 1 ATOM 647 C CB . LYS A 1 84 ? 23.947 3.731 34.688 1.00 23.26 ? 90 LYS A CB 1 ATOM 648 C CG . LYS A 1 84 ? 22.805 4.616 34.197 1.00 20.41 ? 90 LYS A CG 1 ATOM 649 C CD . LYS A 1 84 ? 22.741 5.940 34.924 1.00 24.47 ? 90 LYS A CD 1 ATOM 650 C CE . LYS A 1 84 ? 21.579 6.786 34.319 1.00 26.72 ? 90 LYS A CE 1 ATOM 651 N NZ . LYS A 1 84 ? 21.368 7.961 35.204 1.00 32.45 ? 90 LYS A NZ 1 ATOM 652 N N . GLU A 1 85 ? 26.421 2.277 33.571 1.00 26.92 ? 91 GLU A N 1 ATOM 653 C CA . GLU A 1 85 ? 27.736 1.667 33.748 1.00 29.56 ? 91 GLU A CA 1 ATOM 654 C C . GLU A 1 85 ? 28.121 1.623 35.229 1.00 28.73 ? 91 GLU A C 1 ATOM 655 O O . GLU A 1 85 ? 28.625 0.614 35.697 1.00 29.08 ? 91 GLU A O 1 ATOM 656 C CB . GLU A 1 85 ? 28.801 2.431 32.926 1.00 30.13 ? 91 GLU A CB 1 ATOM 657 C CG . GLU A 1 85 ? 30.199 1.796 32.996 1.00 35.66 ? 91 GLU A CG 1 ATOM 658 C CD . GLU A 1 85 ? 30.256 0.336 32.475 1.00 43.49 ? 91 GLU A CD 1 ATOM 659 O OE1 . GLU A 1 85 ? 29.465 -0.058 31.577 1.00 43.98 ? 91 GLU A OE1 1 ATOM 660 O OE2 . GLU A 1 85 ? 31.129 -0.420 32.966 1.00 47.41 ? 91 GLU A OE2 1 ATOM 661 N N . ASN A 1 86 ? 27.844 2.704 35.957 1.00 28.63 ? 92 ASN A N 1 ATOM 662 C CA . ASN A 1 86 ? 28.214 2.844 37.370 1.00 29.59 ? 92 ASN A CA 1 ATOM 663 C C . ASN A 1 86 ? 27.072 3.466 38.150 1.00 28.56 ? 92 ASN A C 1 ATOM 664 O O . ASN A 1 86 ? 27.169 4.650 38.502 1.00 27.69 ? 92 ASN A O 1 ATOM 665 C CB . ASN A 1 86 ? 29.433 3.803 37.525 1.00 31.23 ? 92 ASN A CB 1 ATOM 666 C CG . ASN A 1 86 ? 30.670 3.313 36.790 1.00 36.07 ? 92 ASN A CG 1 ATOM 667 O OD1 . ASN A 1 86 ? 31.098 3.922 35.797 1.00 43.25 ? 92 ASN A OD1 1 ATOM 668 N ND2 . ASN A 1 86 ? 31.229 2.187 37.239 1.00 39.59 ? 92 ASN A ND2 1 ATOM 669 N N . PRO A 1 87 ? 25.972 2.706 38.408 1.00 27.87 ? 93 PRO A N 1 ATOM 670 C CA . PRO A 1 87 ? 24.807 3.314 39.048 1.00 27.28 ? 93 PRO A CA 1 ATOM 671 C C . PRO A 1 87 ? 25.158 3.762 40.451 1.00 27.77 ? 93 PRO A C 1 ATOM 672 O O . PRO A 1 87 ? 25.847 3.034 41.160 1.00 27.79 ? 93 PRO A O 1 ATOM 673 C CB . PRO A 1 87 ? 23.795 2.150 39.140 1.00 28.20 ? 93 PRO A CB 1 ATOM 674 C CG . PRO A 1 87 ? 24.233 1.171 38.138 1.00 26.40 ? 93 PRO A CG 1 ATOM 675 C CD . PRO A 1 87 ? 25.742 1.285 38.091 1.00 27.91 ? 93 PRO A CD 1 ATOM 676 N N . ARG A 1 88 ? 24.664 4.926 40.853 1.00 27.28 ? 94 ARG A N 1 ATOM 677 C CA . ARG A 1 88 ? 24.950 5.502 42.177 1.00 28.77 ? 94 ARG A CA 1 ATOM 678 C C . ARG A 1 88 ? 24.304 4.745 43.329 1.00 27.24 ? 94 ARG A C 1 ATOM 679 O O . ARG A 1 88 ? 24.824 4.705 44.450 1.00 26.90 ? 94 ARG A O 1 ATOM 680 C CB . ARG A 1 88 ? 24.396 6.919 42.190 1.00 29.24 ? 94 ARG A CB 1 ATOM 681 C CG . ARG A 1 88 ? 25.003 7.830 43.216 1.00 35.83 ? 94 ARG A CG 1 ATOM 682 C CD . ARG A 1 88 ? 24.435 9.260 43.036 1.00 44.76 ? 94 ARG A CD 1 ATOM 683 N NE . ARG A 1 88 ? 24.814 9.833 41.738 1.00 48.89 ? 94 ARG A NE 1 ATOM 684 C CZ . ARG A 1 88 ? 24.009 9.922 40.678 1.00 51.79 ? 94 ARG A CZ 1 ATOM 685 N NH1 . ARG A 1 88 ? 22.754 9.492 40.751 1.00 53.70 ? 94 ARG A NH1 1 ATOM 686 N NH2 . ARG A 1 88 ? 24.455 10.457 39.544 1.00 51.47 ? 94 ARG A NH2 1 ATOM 687 N N . ASP A 1 89 ? 23.134 4.173 43.054 1.00 26.16 ? 95 ASP A N 1 ATOM 688 C CA . ASP A 1 89 ? 22.275 3.643 44.102 1.00 25.21 ? 95 ASP A CA 1 ATOM 689 C C . ASP A 1 89 ? 22.257 2.119 44.072 1.00 24.02 ? 95 ASP A C 1 ATOM 690 O O . ASP A 1 89 ? 21.435 1.513 43.387 1.00 23.64 ? 95 ASP A O 1 ATOM 691 C CB . ASP A 1 89 ? 20.857 4.215 43.953 1.00 25.64 ? 95 ASP A CB 1 ATOM 692 C CG . ASP A 1 89 ? 20.837 5.742 44.084 1.00 28.94 ? 95 ASP A CG 1 ATOM 693 O OD1 . ASP A 1 89 ? 21.437 6.231 45.059 1.00 27.58 ? 95 ASP A OD1 1 ATOM 694 O OD2 . ASP A 1 89 ? 20.241 6.437 43.220 1.00 29.29 ? 95 ASP A OD2 1 ATOM 695 N N . GLY A 1 90 A 23.139 1.524 44.864 1.00 22.66 ? 95 GLY A N 1 ATOM 696 C CA . GLY A 1 90 A 23.271 0.074 44.962 1.00 22.51 ? 95 GLY A CA 1 ATOM 697 C C . GLY A 1 90 A 23.191 -0.291 46.436 1.00 22.15 ? 95 GLY A C 1 ATOM 698 O O . GLY A 1 90 A 22.149 -0.147 47.063 1.00 19.68 ? 95 GLY A O 1 ATOM 699 N N . LEU A 1 91 ? 24.319 -0.714 46.993 1.00 21.65 ? 96 LEU A N 1 ATOM 700 C CA . LEU A 1 91 ? 24.391 -1.041 48.401 1.00 23.05 ? 96 LEU A CA 1 ATOM 701 C C . LEU A 1 91 ? 24.564 0.263 49.184 1.00 24.17 ? 96 LEU A C 1 ATOM 702 O O . LEU A 1 91 ? 25.709 0.721 49.363 1.00 23.62 ? 96 LEU A O 1 ATOM 703 C CB . LEU A 1 91 ? 25.585 -1.988 48.641 1.00 22.20 ? 96 LEU A CB 1 ATOM 704 C CG . LEU A 1 91 ? 25.337 -3.524 48.643 1.00 28.25 ? 96 LEU A CG 1 ATOM 705 C CD1 . LEU A 1 91 ? 24.544 -4.006 47.494 1.00 27.76 ? 96 LEU A CD1 1 ATOM 706 C CD2 . LEU A 1 91 ? 26.690 -4.241 48.654 1.00 29.12 ? 96 LEU A CD2 1 ATOM 707 N N . CYS A 1 92 ? 23.455 0.870 49.657 1.00 24.00 ? 97 CYS A N 1 ATOM 708 C CA . CYS A 1 92 ? 23.581 2.122 50.424 1.00 24.48 ? 97 CYS A CA 1 ATOM 709 C C . CYS A 1 92 ? 24.264 1.898 51.769 1.00 23.62 ? 97 CYS A C 1 ATOM 710 O O . CYS A 1 92 ? 25.164 2.668 52.141 1.00 23.63 ? 97 CYS A O 1 ATOM 711 C CB . CYS A 1 92 ? 22.225 2.823 50.626 1.00 23.98 ? 97 CYS A CB 1 ATOM 712 S SG . CYS A 1 92 ? 20.829 1.711 50.963 1.00 29.63 ? 97 CYS A SG 1 ATOM 713 N N . TYR A 1 93 ? 23.854 0.863 52.505 1.00 22.31 ? 98 TYR A N 1 ATOM 714 C CA . TYR A 1 93 ? 24.744 0.341 53.540 1.00 22.21 ? 98 TYR A CA 1 ATOM 715 C C . TYR A 1 93 ? 25.822 -0.466 52.808 1.00 22.00 ? 98 TYR A C 1 ATOM 716 O O . TYR A 1 93 ? 25.471 -1.412 52.082 1.00 22.25 ? 98 TYR A O 1 ATOM 717 C CB . TYR A 1 93 ? 23.999 -0.544 54.558 1.00 21.52 ? 98 TYR A CB 1 ATOM 718 C CG . TYR A 1 93 ? 24.819 -0.733 55.816 1.00 22.07 ? 98 TYR A CG 1 ATOM 719 C CD1 . TYR A 1 93 ? 24.614 0.082 56.936 1.00 24.95 ? 98 TYR A CD1 1 ATOM 720 C CD2 . TYR A 1 93 ? 25.874 -1.670 55.853 1.00 22.26 ? 98 TYR A CD2 1 ATOM 721 C CE1 . TYR A 1 93 ? 25.395 -0.068 58.079 1.00 25.12 ? 98 TYR A CE1 1 ATOM 722 C CE2 . TYR A 1 93 ? 26.666 -1.813 56.971 1.00 23.49 ? 98 TYR A CE2 1 ATOM 723 C CZ . TYR A 1 93 ? 26.423 -1.007 58.079 1.00 22.75 ? 98 TYR A CZ 1 ATOM 724 O OH . TYR A 1 93 ? 27.209 -1.175 59.184 1.00 21.45 ? 98 TYR A OH 1 ATOM 725 N N . PRO A 1 94 ? 27.116 -0.137 53.004 1.00 21.55 ? 99 PRO A N 1 ATOM 726 C CA . PRO A 1 94 ? 28.122 -0.783 52.137 1.00 22.22 ? 99 PRO A CA 1 ATOM 727 C C . PRO A 1 94 ? 28.316 -2.276 52.384 1.00 21.62 ? 99 PRO A C 1 ATOM 728 O O . PRO A 1 94 ? 28.034 -2.764 53.467 1.00 21.12 ? 99 PRO A O 1 ATOM 729 C CB . PRO A 1 94 ? 29.423 -0.044 52.491 1.00 22.05 ? 99 PRO A CB 1 ATOM 730 C CG . PRO A 1 94 ? 29.223 0.401 53.942 1.00 21.86 ? 99 PRO A CG 1 ATOM 731 C CD . PRO A 1 94 ? 27.741 0.783 53.988 1.00 22.22 ? 99 PRO A CD 1 ATOM 732 N N . GLY A 1 95 ? 28.827 -2.976 51.377 1.00 22.11 ? 100 GLY A N 1 ATOM 733 C CA . GLY A 1 95 ? 29.199 -4.372 51.561 1.00 21.95 ? 100 GLY A CA 1 ATOM 734 C C . GLY A 1 95 ? 29.457 -5.071 50.252 1.00 22.44 ? 100 GLY A C 1 ATOM 735 O O . GLY A 1 95 ? 30.144 -4.554 49.364 1.00 23.50 ? 100 GLY A O 1 ATOM 736 N N . SER A 1 96 ? 28.919 -6.271 50.139 1.00 21.82 ? 101 SER A N 1 ATOM 737 C CA . SER A 1 96 ? 29.195 -7.093 48.986 1.00 22.43 ? 101 SER A CA 1 ATOM 738 C C . SER A 1 96 ? 27.946 -7.947 48.699 1.00 22.12 ? 101 SER A C 1 ATOM 739 O O . SER A 1 96 ? 27.054 -8.077 49.546 1.00 21.50 ? 101 SER A O 1 ATOM 740 C CB . SER A 1 96 ? 30.426 -7.987 49.259 1.00 22.81 ? 101 SER A CB 1 ATOM 741 O OG . SER A 1 96 ? 30.149 -8.861 50.360 1.00 23.33 ? 101 SER A OG 1 ATOM 742 N N . PHE A 1 97 ? 27.915 -8.528 47.499 1.00 21.08 ? 102 PHE A N 1 ATOM 743 C CA . PHE A 1 97 ? 26.811 -9.320 47.040 1.00 20.94 ? 102 PHE A CA 1 ATOM 744 C C . PHE A 1 97 ? 27.447 -10.533 46.366 1.00 21.49 ? 102 PHE A C 1 ATOM 745 O O . PHE A 1 97 ? 27.985 -10.426 45.245 1.00 21.27 ? 102 PHE A O 1 ATOM 746 C CB . PHE A 1 97 ? 25.960 -8.486 46.050 1.00 20.39 ? 102 PHE A CB 1 ATOM 747 C CG . PHE A 1 97 ? 24.550 -8.967 45.928 1.00 20.48 ? 102 PHE A CG 1 ATOM 748 C CD1 . PHE A 1 97 ? 23.484 -8.143 46.284 1.00 18.47 ? 102 PHE A CD1 1 ATOM 749 C CD2 . PHE A 1 97 ? 24.292 -10.235 45.420 1.00 20.25 ? 102 PHE A CD2 1 ATOM 750 C CE1 . PHE A 1 97 ? 22.135 -8.578 46.170 1.00 20.63 ? 102 PHE A CE1 1 ATOM 751 C CE2 . PHE A 1 97 ? 22.939 -10.724 45.322 1.00 23.89 ? 102 PHE A CE2 1 ATOM 752 C CZ . PHE A 1 97 ? 21.866 -9.886 45.702 1.00 21.86 ? 102 PHE A CZ 1 ATOM 753 N N . ASN A 1 98 ? 27.392 -11.664 47.058 1.00 20.81 ? 103 ASN A N 1 ATOM 754 C CA . ASN A 1 98 ? 27.968 -12.909 46.559 1.00 21.28 ? 103 ASN A CA 1 ATOM 755 C C . ASN A 1 98 ? 27.283 -13.395 45.284 1.00 21.27 ? 103 ASN A C 1 ATOM 756 O O . ASN A 1 98 ? 26.046 -13.286 45.161 1.00 21.00 ? 103 ASN A O 1 ATOM 757 C CB . ASN A 1 98 ? 27.908 -13.989 47.636 1.00 20.45 ? 103 ASN A CB 1 ATOM 758 C CG . ASN A 1 98 ? 28.817 -13.692 48.816 1.00 21.56 ? 103 ASN A CG 1 ATOM 759 O OD1 . ASN A 1 98 ? 29.962 -13.294 48.646 1.00 22.30 ? 103 ASN A OD1 1 ATOM 760 N ND2 . ASN A 1 98 ? 28.319 -13.928 50.020 1.00 22.63 ? 103 ASN A ND2 1 ATOM 761 N N . ASP A 1 99 ? 28.090 -13.923 44.348 1.00 18.92 ? 104 ASP A N 1 ATOM 762 C CA . ASP A 1 99 ? 27.592 -14.457 43.079 1.00 18.88 ? 104 ASP A CA 1 ATOM 763 C C . ASP A 1 99 ? 26.697 -13.445 42.383 1.00 17.20 ? 104 ASP A C 1 ATOM 764 O O . ASP A 1 99 ? 25.613 -13.779 41.866 1.00 17.04 ? 104 ASP A O 1 ATOM 765 C CB . ASP A 1 99 ? 26.838 -15.777 43.332 1.00 19.68 ? 104 ASP A CB 1 ATOM 766 C CG . ASP A 1 99 ? 27.658 -16.714 44.137 1.00 25.74 ? 104 ASP A CG 1 ATOM 767 O OD1 . ASP A 1 99 ? 28.745 -17.078 43.643 1.00 27.32 ? 104 ASP A OD1 1 ATOM 768 O OD2 . ASP A 1 99 ? 27.265 -16.976 45.288 1.00 30.59 ? 104 ASP A OD2 1 ATOM 769 N N . TYR A 1 100 ? 27.117 -12.186 42.406 1.00 17.76 ? 105 TYR A N 1 ATOM 770 C CA . TYR A 1 100 ? 26.251 -11.101 41.873 1.00 17.75 ? 105 TYR A CA 1 ATOM 771 C C . TYR A 1 100 ? 26.142 -11.201 40.354 1.00 18.34 ? 105 TYR A C 1 ATOM 772 O O . TYR A 1 100 ? 25.074 -11.065 39.782 1.00 18.11 ? 105 TYR A O 1 ATOM 773 C CB . TYR A 1 100 ? 26.894 -9.763 42.214 1.00 16.61 ? 105 TYR A CB 1 ATOM 774 C CG . TYR A 1 100 ? 26.078 -8.541 41.859 1.00 17.53 ? 105 TYR A CG 1 ATOM 775 C CD1 . TYR A 1 100 ? 24.697 -8.493 42.100 1.00 17.73 ? 105 TYR A CD1 1 ATOM 776 C CD2 . TYR A 1 100 ? 26.700 -7.417 41.292 1.00 19.84 ? 105 TYR A CD2 1 ATOM 777 C CE1 . TYR A 1 100 ? 23.972 -7.329 41.794 1.00 20.47 ? 105 TYR A CE1 1 ATOM 778 C CE2 . TYR A 1 100 ? 25.987 -6.266 40.986 1.00 22.04 ? 105 TYR A CE2 1 ATOM 779 C CZ . TYR A 1 100 ? 24.623 -6.240 41.242 1.00 21.08 ? 105 TYR A CZ 1 ATOM 780 O OH . TYR A 1 100 ? 23.924 -5.112 40.938 1.00 21.97 ? 105 TYR A OH 1 ATOM 781 N N . GLU A 1 101 ? 27.262 -11.500 39.685 1.00 19.06 ? 106 GLU A N 1 ATOM 782 C CA . GLU A 1 101 ? 27.186 -11.675 38.214 1.00 19.84 ? 106 GLU A CA 1 ATOM 783 C C . GLU A 1 101 ? 26.330 -12.845 37.794 1.00 19.01 ? 106 GLU A C 1 ATOM 784 O O . GLU A 1 101 ? 25.700 -12.781 36.756 1.00 18.60 ? 106 GLU A O 1 ATOM 785 C CB . GLU A 1 101 ? 28.587 -11.791 37.595 1.00 19.67 ? 106 GLU A CB 1 ATOM 786 C CG . GLU A 1 101 ? 29.393 -10.499 37.776 1.00 24.55 ? 106 GLU A CG 1 ATOM 787 C CD . GLU A 1 101 ? 29.821 -10.257 39.219 1.00 28.20 ? 106 GLU A CD 1 ATOM 788 O OE1 . GLU A 1 101 ? 30.023 -11.214 40.011 1.00 29.17 ? 106 GLU A OE1 1 ATOM 789 O OE2 . GLU A 1 101 ? 29.954 -9.081 39.558 1.00 31.80 ? 106 GLU A OE2 1 ATOM 790 N N . GLU A 1 102 ? 26.359 -13.925 38.569 1.00 19.58 ? 107 GLU A N 1 ATOM 791 C CA . GLU A 1 102 ? 25.511 -15.085 38.301 1.00 20.08 ? 107 GLU A CA 1 ATOM 792 C C . GLU A 1 102 ? 24.032 -14.653 38.420 1.00 19.91 ? 107 GLU A C 1 ATOM 793 O O . GLU A 1 102 ? 23.177 -15.107 37.652 1.00 19.21 ? 107 GLU A O 1 ATOM 794 C CB . GLU A 1 102 ? 25.805 -16.222 39.285 1.00 18.63 ? 107 GLU A CB 1 ATOM 795 C CG . GLU A 1 102 ? 27.067 -17.085 38.952 1.00 22.24 ? 107 GLU A CG 1 ATOM 796 C CD . GLU A 1 102 ? 26.842 -17.925 37.706 1.00 23.09 ? 107 GLU A CD 1 ATOM 797 O OE1 . GLU A 1 102 ? 25.858 -18.699 37.696 1.00 22.31 ? 107 GLU A OE1 1 ATOM 798 O OE2 . GLU A 1 102 ? 27.637 -17.802 36.750 1.00 20.27 ? 107 GLU A OE2 1 ATOM 799 N N . LEU A 1 103 ? 23.729 -13.784 39.390 1.00 20.15 ? 108 LEU A N 1 ATOM 800 C CA . LEU A 1 103 ? 22.344 -13.289 39.536 1.00 20.67 ? 108 LEU A CA 1 ATOM 801 C C . LEU A 1 103 ? 21.906 -12.455 38.323 1.00 21.38 ? 108 LEU A C 1 ATOM 802 O O . LEU A 1 103 ? 20.791 -12.641 37.793 1.00 20.66 ? 108 LEU A O 1 ATOM 803 C CB . LEU A 1 103 ? 22.169 -12.510 40.855 1.00 20.74 ? 108 LEU A CB 1 ATOM 804 C CG . LEU A 1 103 ? 20.758 -11.930 41.064 1.00 23.04 ? 108 LEU A CG 1 ATOM 805 C CD1 . LEU A 1 103 ? 19.681 -13.046 40.982 1.00 24.37 ? 108 LEU A CD1 1 ATOM 806 C CD2 . LEU A 1 103 ? 20.690 -11.239 42.405 1.00 23.69 ? 108 LEU A CD2 1 ATOM 807 N N . LYS A 1 104 ? 22.793 -11.553 37.883 1.00 21.58 ? 109 LYS A N 1 ATOM 808 C CA . LYS A 1 104 ? 22.566 -10.778 36.670 1.00 22.10 ? 109 LYS A CA 1 ATOM 809 C C . LYS A 1 104 ? 22.371 -11.657 35.443 1.00 21.19 ? 109 LYS A C 1 ATOM 810 O O . LYS A 1 104 ? 21.489 -11.350 34.616 1.00 21.34 ? 109 LYS A O 1 ATOM 811 C CB . LYS A 1 104 ? 23.694 -9.723 36.443 1.00 22.27 ? 109 LYS A CB 1 ATOM 812 C CG . LYS A 1 104 ? 23.820 -8.745 37.651 1.00 25.05 ? 109 LYS A CG 1 ATOM 813 C CD . LYS A 1 104 ? 24.916 -7.662 37.487 1.00 26.90 ? 109 LYS A CD 1 ATOM 814 C CE . LYS A 1 104 ? 24.422 -6.440 36.752 1.00 32.14 ? 109 LYS A CE 1 ATOM 815 N NZ . LYS A 1 104 ? 25.548 -5.397 36.755 1.00 31.47 ? 109 LYS A NZ 1 ATOM 816 N N . HIS A 1 105 ? 23.147 -12.749 35.336 1.00 19.92 ? 110 HIS A N 1 ATOM 817 C CA . HIS A 1 105 ? 22.954 -13.695 34.225 1.00 20.92 ? 110 HIS A CA 1 ATOM 818 C C . HIS A 1 105 ? 21.560 -14.364 34.292 1.00 21.88 ? 110 HIS A C 1 ATOM 819 O O . HIS A 1 105 ? 20.917 -14.587 33.247 1.00 21.87 ? 110 HIS A O 1 ATOM 820 C CB . HIS A 1 105 ? 24.055 -14.782 34.178 1.00 19.88 ? 110 HIS A CB 1 ATOM 821 C CG . HIS A 1 105 ? 23.881 -15.743 33.053 1.00 21.18 ? 110 HIS A CG 1 ATOM 822 N ND1 . HIS A 1 105 ? 24.078 -15.386 31.736 1.00 22.16 ? 110 HIS A ND1 1 ATOM 823 C CD2 . HIS A 1 105 ? 23.504 -17.043 33.037 1.00 24.22 ? 110 HIS A CD2 1 ATOM 824 C CE1 . HIS A 1 105 ? 23.828 -16.422 30.958 1.00 25.93 ? 110 HIS A CE1 1 ATOM 825 N NE2 . HIS A 1 105 ? 23.482 -17.443 31.721 1.00 25.69 ? 110 HIS A NE2 1 ATOM 826 N N . LEU A 1 106 ? 21.113 -14.714 35.496 1.00 22.03 ? 111 LEU A N 1 ATOM 827 C CA . LEU A 1 106 ? 19.739 -15.236 35.656 1.00 25.00 ? 111 LEU A CA 1 ATOM 828 C C . LEU A 1 106 ? 18.714 -14.250 35.041 1.00 25.03 ? 111 LEU A C 1 ATOM 829 O O . LEU A 1 106 ? 17.794 -14.641 34.331 1.00 25.83 ? 111 LEU A O 1 ATOM 830 C CB . LEU A 1 106 ? 19.415 -15.497 37.141 1.00 25.34 ? 111 LEU A CB 1 ATOM 831 C CG . LEU A 1 106 ? 17.946 -15.902 37.412 1.00 28.62 ? 111 LEU A CG 1 ATOM 832 C CD1 . LEU A 1 106 ? 17.751 -17.326 36.924 1.00 30.09 ? 111 LEU A CD1 1 ATOM 833 C CD2 . LEU A 1 106 ? 17.610 -15.794 38.900 1.00 30.35 ? 111 LEU A CD2 1 ATOM 834 N N . LEU A 1 107 ? 18.903 -12.963 35.296 1.00 25.90 ? 112 LEU A N 1 ATOM 835 C CA . LEU A 1 107 ? 17.970 -11.948 34.787 1.00 27.30 ? 112 LEU A CA 1 ATOM 836 C C . LEU A 1 107 ? 17.793 -11.952 33.264 1.00 28.37 ? 112 LEU A C 1 ATOM 837 O O . LEU A 1 107 ? 16.698 -11.588 32.783 1.00 28.41 ? 112 LEU A O 1 ATOM 838 C CB . LEU A 1 107 ? 18.313 -10.554 35.333 1.00 26.80 ? 112 LEU A CB 1 ATOM 839 C CG . LEU A 1 107 ? 18.069 -10.467 36.838 1.00 28.29 ? 112 LEU A CG 1 ATOM 840 C CD1 . LEU A 1 107 ? 18.518 -9.115 37.347 1.00 31.04 ? 112 LEU A CD1 1 ATOM 841 C CD2 . LEU A 1 107 ? 16.584 -10.695 37.212 1.00 31.93 ? 112 LEU A CD2 1 ATOM 842 N N . SER A 1 108 ? 18.796 -12.446 32.519 1.00 27.88 ? 113 SER A N 1 ATOM 843 C CA . SER A 1 108 ? 18.697 -12.580 31.039 1.00 29.82 ? 113 SER A CA 1 ATOM 844 C C . SER A 1 108 ? 17.630 -13.527 30.550 1.00 30.05 ? 113 SER A C 1 ATOM 845 O O . SER A 1 108 ? 17.291 -13.540 29.349 1.00 31.67 ? 113 SER A O 1 ATOM 846 C CB . SER A 1 108 ? 20.035 -13.059 30.439 1.00 29.42 ? 113 SER A CB 1 ATOM 847 O OG . SER A 1 108 ? 20.987 -12.043 30.634 1.00 33.60 ? 113 SER A OG 1 ATOM 848 N N . SER A 1 109 ? 17.138 -14.389 31.427 1.00 29.51 ? 114 SER A N 1 ATOM 849 C CA . SER A 1 109 ? 16.058 -15.259 31.018 1.00 29.51 ? 114 SER A CA 1 ATOM 850 C C . SER A 1 109 ? 14.782 -15.003 31.810 1.00 28.97 ? 114 SER A C 1 ATOM 851 O O . SER A 1 109 ? 13.861 -15.808 31.750 1.00 30.47 ? 114 SER A O 1 ATOM 852 C CB . SER A 1 109 ? 16.458 -16.740 31.069 1.00 30.59 ? 114 SER A CB 1 ATOM 853 O OG . SER A 1 109 ? 17.163 -17.052 32.247 1.00 33.25 ? 114 SER A OG 1 ATOM 854 N N . VAL A 1 110 ? 14.746 -13.921 32.584 1.00 26.91 ? 115 VAL A N 1 ATOM 855 C CA . VAL A 1 110 ? 13.553 -13.578 33.380 1.00 25.83 ? 115 VAL A CA 1 ATOM 856 C C . VAL A 1 110 ? 12.962 -12.292 32.825 1.00 24.97 ? 115 VAL A C 1 ATOM 857 O O . VAL A 1 110 ? 13.712 -11.342 32.546 1.00 23.70 ? 115 VAL A O 1 ATOM 858 C CB . VAL A 1 110 ? 13.903 -13.396 34.873 1.00 25.59 ? 115 VAL A CB 1 ATOM 859 C CG1 . VAL A 1 110 ? 12.660 -12.984 35.679 1.00 26.54 ? 115 VAL A CG1 1 ATOM 860 C CG2 . VAL A 1 110 ? 14.527 -14.695 35.447 1.00 26.19 ? 115 VAL A CG2 1 ATOM 861 N N . LYS A 1 111 ? 11.634 -12.241 32.683 1.00 23.34 ? 116 LYS A N 1 ATOM 862 C CA . LYS A 1 111 ? 10.971 -11.055 32.151 1.00 23.72 ? 116 LYS A CA 1 ATOM 863 C C . LYS A 1 111 ? 9.973 -10.433 33.132 1.00 23.25 ? 116 LYS A C 1 ATOM 864 O O . LYS A 1 111 ? 9.433 -9.372 32.867 1.00 23.13 ? 116 LYS A O 1 ATOM 865 C CB . LYS A 1 111 ? 10.244 -11.366 30.852 1.00 24.77 ? 116 LYS A CB 1 ATOM 866 C CG . LYS A 1 111 ? 11.120 -11.615 29.641 1.00 26.50 ? 116 LYS A CG 1 ATOM 867 C CD . LYS A 1 111 ? 10.201 -12.199 28.564 1.00 33.81 ? 116 LYS A CD 1 ATOM 868 C CE . LYS A 1 111 ? 10.842 -12.197 27.217 1.00 35.79 ? 116 LYS A CE 1 ATOM 869 N NZ . LYS A 1 111 ? 9.924 -12.864 26.275 1.00 38.67 ? 116 LYS A NZ 1 ATOM 870 N N . HIS A 1 112 A 9.735 -11.096 34.266 1.00 23.35 ? 116 HIS A N 1 ATOM 871 C CA . HIS A 1 112 A 8.880 -10.506 35.290 1.00 23.18 ? 116 HIS A CA 1 ATOM 872 C C . HIS A 1 112 A 9.034 -11.237 36.583 1.00 22.58 ? 116 HIS A C 1 ATOM 873 O O . HIS A 1 112 A 9.268 -12.462 36.581 1.00 23.22 ? 116 HIS A O 1 ATOM 874 C CB . HIS A 1 112 A 7.395 -10.523 34.839 1.00 23.55 ? 116 HIS A CB 1 ATOM 875 C CG . HIS A 1 112 A 6.493 -9.670 35.684 1.00 24.78 ? 116 HIS A CG 1 ATOM 876 N ND1 . HIS A 1 112 A 5.287 -10.123 36.185 1.00 26.84 ? 116 HIS A ND1 1 ATOM 877 C CD2 . HIS A 1 112 A 6.640 -8.403 36.149 1.00 26.78 ? 116 HIS A CD2 1 ATOM 878 C CE1 . HIS A 1 112 A 4.715 -9.162 36.894 1.00 29.08 ? 116 HIS A CE1 1 ATOM 879 N NE2 . HIS A 1 112 A 5.509 -8.100 36.880 1.00 26.03 ? 116 HIS A NE2 1 ATOM 880 N N . PHE A 1 113 B 8.932 -10.488 37.684 1.00 21.17 ? 116 PHE A N 1 ATOM 881 C CA . PHE A 1 113 B 8.841 -11.063 39.010 1.00 21.76 ? 116 PHE A CA 1 ATOM 882 C C . PHE A 1 113 B 7.493 -10.738 39.624 1.00 22.73 ? 116 PHE A C 1 ATOM 883 O O . PHE A 1 113 B 6.874 -9.696 39.317 1.00 23.16 ? 116 PHE A O 1 ATOM 884 C CB . PHE A 1 113 B 9.886 -10.452 39.956 1.00 21.03 ? 116 PHE A CB 1 ATOM 885 C CG . PHE A 1 113 B 11.302 -10.922 39.714 1.00 21.50 ? 116 PHE A CG 1 ATOM 886 C CD1 . PHE A 1 113 B 11.615 -12.278 39.744 1.00 21.22 ? 116 PHE A CD1 1 ATOM 887 C CD2 . PHE A 1 113 B 12.335 -9.986 39.575 1.00 19.95 ? 116 PHE A CD2 1 ATOM 888 C CE1 . PHE A 1 113 B 12.946 -12.741 39.575 1.00 22.59 ? 116 PHE A CE1 1 ATOM 889 C CE2 . PHE A 1 113 B 13.664 -10.424 39.386 1.00 21.16 ? 116 PHE A CE2 1 ATOM 890 C CZ . PHE A 1 113 B 13.962 -11.823 39.394 1.00 23.04 ? 116 PHE A CZ 1 ATOM 891 N N . GLU A 1 114 C 7.058 -11.593 40.541 1.00 22.93 ? 116 GLU A N 1 ATOM 892 C CA . GLU A 1 114 C 6.023 -11.186 41.487 1.00 23.84 ? 116 GLU A CA 1 ATOM 893 C C . GLU A 1 114 C 6.659 -11.176 42.847 1.00 23.80 ? 116 GLU A C 1 ATOM 894 O O . GLU A 1 114 C 7.185 -12.213 43.319 1.00 21.92 ? 116 GLU A O 1 ATOM 895 C CB . GLU A 1 114 C 4.839 -12.169 41.521 1.00 24.45 ? 116 GLU A CB 1 ATOM 896 C CG . GLU A 1 114 C 3.903 -11.989 40.367 1.00 30.68 ? 116 GLU A CG 1 ATOM 897 C CD . GLU A 1 114 C 2.841 -13.117 40.313 1.00 35.70 ? 116 GLU A CD 1 ATOM 898 O OE1 . GLU A 1 114 C 2.359 -13.552 41.397 1.00 34.55 ? 116 GLU A OE1 1 ATOM 899 O OE2 . GLU A 1 114 C 2.538 -13.567 39.185 1.00 38.88 ? 116 GLU A OE2 1 ATOM 900 N N . LYS A 1 115 ? 6.616 -10.021 43.501 1.00 24.45 ? 117 LYS A N 1 ATOM 901 C CA . LYS A 1 115 ? 7.292 -9.933 44.776 1.00 25.10 ? 117 LYS A CA 1 ATOM 902 C C . LYS A 1 115 ? 6.312 -10.449 45.817 1.00 25.47 ? 117 LYS A C 1 ATOM 903 O O . LYS A 1 115 ? 5.197 -9.985 45.885 1.00 27.09 ? 117 LYS A O 1 ATOM 904 C CB . LYS A 1 115 ? 7.758 -8.491 45.039 1.00 25.33 ? 117 LYS A CB 1 ATOM 905 C CG . LYS A 1 115 ? 8.726 -8.364 46.205 1.00 24.73 ? 117 LYS A CG 1 ATOM 906 C CD . LYS A 1 115 ? 9.349 -6.913 46.282 1.00 26.03 ? 117 LYS A CD 1 ATOM 907 C CE . LYS A 1 115 ? 8.434 -5.916 46.958 1.00 23.87 ? 117 LYS A CE 1 ATOM 908 N NZ . LYS A 1 115 ? 9.147 -4.561 47.073 1.00 19.28 ? 117 LYS A NZ 1 ATOM 909 N N . VAL A 1 116 ? 6.726 -11.414 46.623 1.00 24.50 ? 118 VAL A N 1 ATOM 910 C CA . VAL A 1 116 ? 5.837 -12.096 47.558 1.00 23.61 ? 118 VAL A CA 1 ATOM 911 C C . VAL A 1 116 ? 6.336 -11.836 48.973 1.00 23.87 ? 118 VAL A C 1 ATOM 912 O O . VAL A 1 116 ? 7.529 -11.970 49.243 1.00 21.70 ? 118 VAL A O 1 ATOM 913 C CB . VAL A 1 116 ? 5.781 -13.644 47.281 1.00 23.99 ? 118 VAL A CB 1 ATOM 914 C CG1 . VAL A 1 116 ? 4.930 -14.376 48.350 1.00 24.39 ? 118 VAL A CG1 1 ATOM 915 C CG2 . VAL A 1 116 ? 5.195 -13.923 45.890 1.00 25.04 ? 118 VAL A CG2 1 ATOM 916 N N . LYS A 1 117 ? 5.450 -11.446 49.880 1.00 22.91 ? 119 LYS A N 1 ATOM 917 C CA . LYS A 1 117 ? 5.884 -11.183 51.276 1.00 24.95 ? 119 LYS A CA 1 ATOM 918 C C . LYS A 1 117 ? 5.996 -12.499 52.025 1.00 25.63 ? 119 LYS A C 1 ATOM 919 O O . LYS A 1 117 ? 5.064 -12.925 52.737 1.00 27.35 ? 119 LYS A O 1 ATOM 920 C CB . LYS A 1 117 ? 4.908 -10.243 52.016 1.00 24.94 ? 119 LYS A CB 1 ATOM 921 C CG . LYS A 1 117 ? 5.442 -9.805 53.424 1.00 25.61 ? 119 LYS A CG 1 ATOM 922 C CD . LYS A 1 117 ? 4.427 -8.911 54.157 1.00 29.81 ? 119 LYS A CD 1 ATOM 923 C CE . LYS A 1 117 ? 4.346 -7.575 53.452 1.00 30.93 ? 119 LYS A CE 1 ATOM 924 N NZ . LYS A 1 117 ? 3.673 -6.579 54.306 1.00 33.40 ? 119 LYS A NZ 1 ATOM 925 N N . ILE A 1 118 ? 7.145 -13.143 51.898 1.00 24.97 ? 120 ILE A N 1 ATOM 926 C CA . ILE A 1 118 ? 7.339 -14.462 52.437 1.00 24.75 ? 120 ILE A CA 1 ATOM 927 C C . ILE A 1 118 ? 7.573 -14.521 53.943 1.00 24.94 ? 120 ILE A C 1 ATOM 928 O O . ILE A 1 118 ? 7.269 -15.535 54.543 1.00 26.12 ? 120 ILE A O 1 ATOM 929 C CB . ILE A 1 118 ? 8.538 -15.200 51.709 1.00 23.69 ? 120 ILE A CB 1 ATOM 930 C CG1 . ILE A 1 118 ? 9.806 -14.400 51.869 1.00 23.14 ? 120 ILE A CG1 1 ATOM 931 C CG2 . ILE A 1 118 ? 8.195 -15.408 50.234 1.00 24.02 ? 120 ILE A CG2 1 ATOM 932 C CD1 . ILE A 1 118 ? 11.107 -15.204 51.517 1.00 26.60 ? 120 ILE A CD1 1 ATOM 933 N N . LEU A 1 119 ? 8.163 -13.483 54.535 1.00 24.44 ? 121 LEU A N 1 ATOM 934 C CA . LEU A 1 119 ? 8.497 -13.503 55.964 1.00 25.76 ? 121 LEU A CA 1 ATOM 935 C C . LEU A 1 119 ? 8.103 -12.178 56.632 1.00 25.92 ? 121 LEU A C 1 ATOM 936 O O . LEU A 1 119 ? 8.973 -11.376 56.988 1.00 25.68 ? 121 LEU A O 1 ATOM 937 C CB . LEU A 1 119 ? 10.003 -13.784 56.184 1.00 25.26 ? 121 LEU A CB 1 ATOM 938 C CG . LEU A 1 119 ? 10.493 -15.213 55.891 1.00 27.14 ? 121 LEU A CG 1 ATOM 939 C CD1 . LEU A 1 119 ? 11.997 -15.225 55.709 1.00 30.89 ? 121 LEU A CD1 1 ATOM 940 C CD2 . LEU A 1 119 ? 10.098 -16.207 56.986 1.00 28.76 ? 121 LEU A CD2 1 ATOM 941 N N . PRO A 1 120 ? 6.789 -11.948 56.804 1.00 27.71 ? 122 PRO A N 1 ATOM 942 C CA . PRO A 1 120 ? 6.292 -10.639 57.240 1.00 28.56 ? 122 PRO A CA 1 ATOM 943 C C . PRO A 1 120 ? 7.027 -10.225 58.482 1.00 29.11 ? 122 PRO A C 1 ATOM 944 O O . PRO A 1 120 ? 7.210 -11.039 59.390 1.00 29.62 ? 122 PRO A O 1 ATOM 945 C CB . PRO A 1 120 ? 4.808 -10.888 57.552 1.00 29.40 ? 122 PRO A CB 1 ATOM 946 C CG . PRO A 1 120 ? 4.452 -12.099 56.858 1.00 30.38 ? 122 PRO A CG 1 ATOM 947 C CD . PRO A 1 120 ? 5.706 -12.941 56.679 1.00 27.75 ? 122 PRO A CD 1 ATOM 948 N N . LYS A 1 121 ? 7.493 -8.983 58.470 1.00 30.39 ? 123 LYS A N 1 ATOM 949 C CA . LYS A 1 121 ? 8.252 -8.355 59.538 1.00 32.54 ? 123 LYS A CA 1 ATOM 950 C C . LYS A 1 121 ? 7.584 -8.486 60.911 1.00 33.22 ? 123 LYS A C 1 ATOM 951 O O . LYS A 1 121 ? 8.256 -8.702 61.924 1.00 32.11 ? 123 LYS A O 1 ATOM 952 C CB . LYS A 1 121 ? 8.377 -6.851 59.194 1.00 33.05 ? 123 LYS A CB 1 ATOM 953 C CG . LYS A 1 121 ? 9.637 -6.185 59.667 1.00 36.30 ? 123 LYS A CG 1 ATOM 954 C CD . LYS A 1 121 ? 9.654 -4.698 59.329 1.00 39.80 ? 123 LYS A CD 1 ATOM 955 C CE . LYS A 1 121 ? 9.238 -4.389 57.909 1.00 39.77 ? 123 LYS A CE 1 ATOM 956 N NZ . LYS A 1 121 ? 9.784 -3.073 57.457 1.00 41.08 ? 123 LYS A NZ 1 ATOM 957 N N . ASP A 1 122 ? 6.256 -8.327 60.932 1.00 35.09 ? 125 ASP A N 1 ATOM 958 C CA . ASP A 1 122 ? 5.480 -8.324 62.178 1.00 37.16 ? 125 ASP A CA 1 ATOM 959 C C . ASP A 1 122 ? 5.591 -9.630 62.960 1.00 37.60 ? 125 ASP A C 1 ATOM 960 O O . ASP A 1 122 ? 5.268 -9.667 64.139 1.00 38.82 ? 125 ASP A O 1 ATOM 961 C CB . ASP A 1 122 ? 3.999 -7.877 61.940 1.00 37.79 ? 125 ASP A CB 1 ATOM 962 C CG . ASP A 1 122 ? 3.119 -8.953 61.253 1.00 40.69 ? 125 ASP A CG 1 ATOM 963 O OD1 . ASP A 1 122 ? 3.619 -9.831 60.517 1.00 43.87 ? 125 ASP A OD1 1 ATOM 964 O OD2 . ASP A 1 122 ? 1.878 -8.922 61.448 1.00 46.85 ? 125 ASP A OD2 1 ATOM 965 N N . ARG A 1 123 ? 6.060 -10.696 62.310 1.00 37.58 ? 126 ARG A N 1 ATOM 966 C CA . ARG A 1 123 ? 6.149 -12.007 62.944 1.00 37.59 ? 126 ARG A CA 1 ATOM 967 C C . ARG A 1 123 ? 7.422 -12.211 63.792 1.00 36.94 ? 126 ARG A C 1 ATOM 968 O O . ARG A 1 123 ? 7.512 -13.200 64.526 1.00 36.21 ? 126 ARG A O 1 ATOM 969 C CB . ARG A 1 123 ? 5.990 -13.133 61.905 1.00 38.58 ? 126 ARG A CB 1 ATOM 970 C CG . ARG A 1 123 ? 4.535 -13.318 61.344 1.00 41.52 ? 126 ARG A CG 1 ATOM 971 C CD . ARG A 1 123 ? 3.598 -14.039 62.331 1.00 46.91 ? 126 ARG A CD 1 ATOM 972 N NE . ARG A 1 123 ? 2.201 -13.977 61.871 1.00 52.04 ? 126 ARG A NE 1 ATOM 973 C CZ . ARG A 1 123 ? 1.186 -14.696 62.360 1.00 52.03 ? 126 ARG A CZ 1 ATOM 974 N NH1 . ARG A 1 123 ? 1.363 -15.554 63.361 1.00 53.31 ? 126 ARG A NH1 1 ATOM 975 N NH2 . ARG A 1 123 ? -0.024 -14.544 61.845 1.00 53.04 ? 126 ARG A NH2 1 ATOM 976 N N . TRP A 1 124 ? 8.396 -11.296 63.687 1.00 35.95 ? 127 TRP A N 1 ATOM 977 C CA . TRP A 1 124 ? 9.585 -11.331 64.552 1.00 35.40 ? 127 TRP A CA 1 ATOM 978 C C . TRP A 1 124 ? 9.217 -10.677 65.882 1.00 37.74 ? 127 TRP A C 1 ATOM 979 O O . TRP A 1 124 ? 9.530 -9.497 66.124 1.00 37.38 ? 127 TRP A O 1 ATOM 980 C CB . TRP A 1 124 ? 10.777 -10.578 63.933 1.00 34.55 ? 127 TRP A CB 1 ATOM 981 C CG . TRP A 1 124 ? 11.285 -11.125 62.623 1.00 28.99 ? 127 TRP A CG 1 ATOM 982 C CD1 . TRP A 1 124 ? 11.165 -10.532 61.391 1.00 28.52 ? 127 TRP A CD1 1 ATOM 983 C CD2 . TRP A 1 124 ? 11.991 -12.359 62.409 1.00 29.08 ? 127 TRP A CD2 1 ATOM 984 N NE1 . TRP A 1 124 ? 11.758 -11.325 60.422 1.00 25.63 ? 127 TRP A NE1 1 ATOM 985 C CE2 . TRP A 1 124 ? 12.282 -12.443 61.022 1.00 27.03 ? 127 TRP A CE2 1 ATOM 986 C CE3 . TRP A 1 124 ? 12.417 -13.402 63.254 1.00 28.08 ? 127 TRP A CE3 1 ATOM 987 C CZ2 . TRP A 1 124 ? 12.975 -13.532 60.464 1.00 27.52 ? 127 TRP A CZ2 1 ATOM 988 C CZ3 . TRP A 1 124 ? 13.101 -14.480 62.700 1.00 27.55 ? 127 TRP A CZ3 1 ATOM 989 C CH2 . TRP A 1 124 ? 13.370 -14.541 61.314 1.00 28.23 ? 127 TRP A CH2 1 ATOM 990 N N . THR A 1 125 ? 8.519 -11.427 66.733 1.00 38.86 ? 128 THR A N 1 ATOM 991 C CA . THR A 1 125 ? 8.001 -10.849 67.971 1.00 40.64 ? 128 THR A CA 1 ATOM 992 C C . THR A 1 125 ? 9.069 -10.744 69.063 1.00 40.87 ? 128 THR A C 1 ATOM 993 O O . THR A 1 125 ? 8.968 -9.893 69.945 1.00 42.20 ? 128 THR A O 1 ATOM 994 C CB . THR A 1 125 ? 6.753 -11.598 68.477 1.00 40.39 ? 128 THR A CB 1 ATOM 995 O OG1 . THR A 1 125 ? 7.018 -13.003 68.503 1.00 41.25 ? 128 THR A OG1 1 ATOM 996 C CG2 . THR A 1 125 ? 5.580 -11.345 67.541 1.00 42.05 ? 128 THR A CG2 1 ATOM 997 N N . GLN A 1 126 ? 10.091 -11.597 68.998 1.00 40.76 ? 129 GLN A N 1 ATOM 998 C CA . GLN A 1 126 ? 11.144 -11.580 70.010 1.00 40.47 ? 129 GLN A CA 1 ATOM 999 C C . GLN A 1 126 ? 12.349 -10.673 69.651 1.00 39.59 ? 129 GLN A C 1 ATOM 1000 O O . GLN A 1 126 ? 13.344 -10.674 70.368 1.00 39.61 ? 129 GLN A O 1 ATOM 1001 C CB . GLN A 1 126 ? 11.628 -13.001 70.306 1.00 40.83 ? 129 GLN A CB 1 ATOM 1002 C CG . GLN A 1 126 ? 10.580 -14.004 70.818 1.00 43.96 ? 129 GLN A CG 1 ATOM 1003 C CD . GLN A 1 126 ? 11.244 -15.297 71.312 1.00 48.41 ? 129 GLN A CD 1 ATOM 1004 O OE1 . GLN A 1 126 ? 11.352 -16.284 70.574 1.00 50.52 ? 129 GLN A OE1 1 ATOM 1005 N NE2 . GLN A 1 126 ? 11.733 -15.276 72.556 1.00 50.25 ? 129 GLN A NE2 1 ATOM 1006 N N . HIS A 1 127 ? 12.255 -9.895 68.567 1.00 38.72 ? 130 HIS A N 1 ATOM 1007 C CA . HIS A 1 127 ? 13.380 -9.038 68.100 1.00 37.41 ? 130 HIS A CA 1 ATOM 1008 C C . HIS A 1 127 ? 12.907 -7.676 67.628 1.00 36.94 ? 130 HIS A C 1 ATOM 1009 O O . HIS A 1 127 ? 11.773 -7.531 67.191 1.00 37.23 ? 130 HIS A O 1 ATOM 1010 C CB . HIS A 1 127 ? 14.139 -9.694 66.939 1.00 36.44 ? 130 HIS A CB 1 ATOM 1011 C CG . HIS A 1 127 ? 14.782 -10.986 67.296 1.00 35.41 ? 130 HIS A CG 1 ATOM 1012 N ND1 . HIS A 1 127 ? 14.107 -12.186 67.264 1.00 36.66 ? 130 HIS A ND1 1 ATOM 1013 C CD2 . HIS A 1 127 ? 16.037 -11.272 67.712 1.00 35.86 ? 130 HIS A CD2 1 ATOM 1014 C CE1 . HIS A 1 127 ? 14.917 -13.157 67.642 1.00 33.78 ? 130 HIS A CE1 1 ATOM 1015 N NE2 . HIS A 1 127 ? 16.097 -12.629 67.913 1.00 36.50 ? 130 HIS A NE2 1 ATOM 1016 N N . THR A 1 128 ? 13.789 -6.682 67.696 1.00 36.41 ? 131 THR A N 1 ATOM 1017 C CA . THR A 1 128 ? 13.505 -5.361 67.142 1.00 36.11 ? 131 THR A CA 1 ATOM 1018 C C . THR A 1 128 ? 13.712 -5.427 65.620 1.00 35.26 ? 131 THR A C 1 ATOM 1019 O O . THR A 1 128 ? 14.649 -6.069 65.151 1.00 33.90 ? 131 THR A O 1 ATOM 1020 C CB . THR A 1 128 ? 14.419 -4.310 67.764 1.00 36.85 ? 131 THR A CB 1 ATOM 1021 O OG1 . THR A 1 128 ? 14.293 -4.360 69.194 1.00 39.32 ? 131 THR A OG1 1 ATOM 1022 C CG2 . THR A 1 128 ? 14.063 -2.907 67.299 1.00 38.18 ? 131 THR A CG2 1 ATOM 1023 N N . THR A 1 129 ? 12.835 -4.775 64.860 1.00 35.20 ? 132 THR A N 1 ATOM 1024 C CA . THR A 1 129 ? 12.907 -4.834 63.398 1.00 35.03 ? 132 THR A CA 1 ATOM 1025 C C . THR A 1 129 ? 12.958 -3.466 62.741 1.00 35.28 ? 132 THR A C 1 ATOM 1026 O O . THR A 1 129 ? 12.959 -3.369 61.517 1.00 35.41 ? 132 THR A O 1 ATOM 1027 C CB . THR A 1 129 ? 11.719 -5.604 62.778 1.00 35.23 ? 132 THR A CB 1 ATOM 1028 O OG1 . THR A 1 129 ? 10.502 -4.975 63.163 1.00 34.95 ? 132 THR A OG1 1 ATOM 1029 C CG2 . THR A 1 129 ? 11.682 -7.066 63.207 1.00 34.68 ? 132 THR A CG2 1 ATOM 1030 N N . THR A 1 130 ? 13.015 -2.411 63.545 1.00 35.60 ? 133 THR A N 1 ATOM 1031 C CA . THR A 1 130 ? 12.950 -1.039 63.045 1.00 35.94 ? 133 THR A CA 1 ATOM 1032 C C . THR A 1 130 ? 14.331 -0.434 62.749 1.00 36.10 ? 133 THR A C 1 ATOM 1033 O O . THR A 1 130 ? 14.425 0.714 62.287 1.00 36.70 ? 133 THR A O 1 ATOM 1034 C CB . THR A 1 130 ? 12.172 -0.129 64.028 1.00 37.10 ? 133 THR A CB 1 ATOM 1035 O OG1 . THR A 1 130 ? 12.682 -0.332 65.353 1.00 38.19 ? 133 THR A OG1 1 ATOM 1036 C CG2 . THR A 1 130 ? 10.681 -0.482 64.026 1.00 37.74 ? 133 THR A CG2 1 ATOM 1037 N N . GLY A 1 131 ? 15.382 -1.240 62.936 1.00 34.99 ? 134 GLY A N 1 ATOM 1038 C CA . GLY A 1 131 ? 16.778 -0.820 62.723 1.00 32.98 ? 134 GLY A CA 1 ATOM 1039 C C . GLY A 1 131 ? 17.060 -0.343 61.316 1.00 31.57 ? 134 GLY A C 1 ATOM 1040 O O . GLY A 1 131 ? 16.628 -0.974 60.320 1.00 29.85 ? 134 GLY A O 1 ATOM 1041 N N . GLY A 1 132 ? 17.767 0.796 61.262 1.00 30.73 ? 135 GLY A N 1 ATOM 1042 C CA . GLY A 1 132 ? 18.262 1.396 60.044 1.00 28.75 ? 135 GLY A CA 1 ATOM 1043 C C . GLY A 1 132 ? 19.608 2.065 60.270 1.00 28.66 ? 135 GLY A C 1 ATOM 1044 O O . GLY A 1 132 ? 20.260 1.865 61.300 1.00 29.15 ? 135 GLY A O 1 ATOM 1045 N N . SER A 1 133 ? 20.011 2.862 59.296 1.00 26.74 ? 136 SER A N 1 ATOM 1046 C CA . SER A 1 133 ? 21.321 3.470 59.248 1.00 26.05 ? 136 SER A CA 1 ATOM 1047 C C . SER A 1 133 ? 21.184 4.784 58.517 1.00 26.48 ? 136 SER A C 1 ATOM 1048 O O . SER A 1 133 ? 20.385 4.916 57.578 1.00 24.31 ? 136 SER A O 1 ATOM 1049 C CB . SER A 1 133 ? 22.281 2.586 58.446 1.00 24.79 ? 136 SER A CB 1 ATOM 1050 O OG . SER A 1 133 ? 23.558 3.176 58.349 1.00 24.43 ? 136 SER A OG 1 ATOM 1051 N N . ARG A 1 134 ? 22.006 5.731 58.944 1.00 27.41 ? 137 ARG A N 1 ATOM 1052 C CA . ARG A 1 134 ? 22.216 6.975 58.257 1.00 28.82 ? 137 ARG A CA 1 ATOM 1053 C C . ARG A 1 134 ? 22.712 6.761 56.848 1.00 28.54 ? 137 ARG A C 1 ATOM 1054 O O . ARG A 1 134 ? 22.539 7.625 55.998 1.00 27.61 ? 137 ARG A O 1 ATOM 1055 C CB . ARG A 1 134 ? 23.264 7.790 59.012 1.00 30.74 ? 137 ARG A CB 1 ATOM 1056 C CG . ARG A 1 134 ? 22.833 8.179 60.427 1.00 35.24 ? 137 ARG A CG 1 ATOM 1057 C CD . ARG A 1 134 ? 22.602 9.678 60.557 1.00 44.10 ? 137 ARG A CD 1 ATOM 1058 N NE . ARG A 1 134 ? 21.808 10.167 59.428 1.00 51.40 ? 137 ARG A NE 1 ATOM 1059 C CZ . ARG A 1 134 ? 20.663 10.840 59.541 1.00 52.66 ? 137 ARG A CZ 1 ATOM 1060 N NH1 . ARG A 1 134 ? 20.164 11.146 60.744 1.00 51.20 ? 137 ARG A NH1 1 ATOM 1061 N NH2 . ARG A 1 134 ? 20.029 11.218 58.438 1.00 54.26 ? 137 ARG A NH2 1 ATOM 1062 N N . ALA A 1 135 ? 23.353 5.619 56.596 1.00 26.63 ? 138 ALA A N 1 ATOM 1063 C CA . ALA A 1 135 ? 23.803 5.314 55.252 1.00 27.50 ? 138 ALA A CA 1 ATOM 1064 C C . ALA A 1 135 ? 22.639 5.113 54.265 1.00 26.93 ? 138 ALA A C 1 ATOM 1065 O O . ALA A 1 135 ? 22.842 5.238 53.057 1.00 28.07 ? 138 ALA A O 1 ATOM 1066 C CB . ALA A 1 135 ? 24.739 4.035 55.252 1.00 26.01 ? 138 ALA A CB 1 ATOM 1067 N N . CYS A 1 136 ? 21.466 4.739 54.773 1.00 26.24 ? 139 CYS A N 1 ATOM 1068 C CA . CYS A 1 136 ? 20.265 4.570 53.952 1.00 26.66 ? 139 CYS A CA 1 ATOM 1069 C C . CYS A 1 136 ? 19.215 5.602 54.399 1.00 27.00 ? 139 CYS A C 1 ATOM 1070 O O . CYS A 1 136 ? 18.031 5.257 54.474 1.00 26.19 ? 139 CYS A O 1 ATOM 1071 C CB . CYS A 1 136 ? 19.646 3.178 54.151 1.00 25.52 ? 139 CYS A CB 1 ATOM 1072 S SG . CYS A 1 136 ? 20.859 1.819 54.351 1.00 29.76 ? 139 CYS A SG 1 ATOM 1073 N N . ALA A 1 137 ? 19.655 6.809 54.758 1.00 26.98 ? 140 ALA A N 1 ATOM 1074 C CA . ALA A 1 137 ? 18.732 7.801 55.353 1.00 28.80 ? 140 ALA A CA 1 ATOM 1075 C C . ALA A 1 137 ? 17.650 8.179 54.383 1.00 29.01 ? 140 ALA A C 1 ATOM 1076 O O . ALA A 1 137 ? 17.900 8.236 53.179 1.00 30.09 ? 140 ALA A O 1 ATOM 1077 C CB . ALA A 1 137 ? 19.476 9.069 55.807 1.00 28.27 ? 140 ALA A CB 1 ATOM 1078 N N . VAL A 1 138 ? 16.463 8.468 54.919 1.00 29.88 ? 141 VAL A N 1 ATOM 1079 C CA . VAL A 1 138 ? 15.316 8.956 54.147 1.00 29.77 ? 141 VAL A CA 1 ATOM 1080 C C . VAL A 1 138 ? 14.749 10.167 54.906 1.00 30.06 ? 141 VAL A C 1 ATOM 1081 O O . VAL A 1 138 ? 14.467 10.077 56.105 1.00 29.66 ? 141 VAL A O 1 ATOM 1082 C CB . VAL A 1 138 ? 14.230 7.849 53.998 1.00 30.05 ? 141 VAL A CB 1 ATOM 1083 C CG1 . VAL A 1 138 ? 12.922 8.405 53.337 1.00 32.10 ? 141 VAL A CG1 1 ATOM 1084 C CG2 . VAL A 1 138 ? 14.792 6.675 53.197 1.00 29.88 ? 141 VAL A CG2 1 ATOM 1085 N N . SER A 1 139 ? 14.652 11.307 54.226 1.00 30.37 ? 142 SER A N 1 ATOM 1086 C CA . SER A 1 139 ? 14.181 12.532 54.861 1.00 31.75 ? 142 SER A CA 1 ATOM 1087 C C . SER A 1 139 ? 14.914 12.791 56.174 1.00 32.49 ? 142 SER A C 1 ATOM 1088 O O . SER A 1 139 ? 14.303 13.051 57.216 1.00 32.44 ? 142 SER A O 1 ATOM 1089 C CB . SER A 1 139 ? 12.667 12.468 55.056 1.00 31.91 ? 142 SER A CB 1 ATOM 1090 O OG . SER A 1 139 ? 12.072 12.249 53.794 1.00 31.43 ? 142 SER A OG 1 ATOM 1091 N N . GLY A 1 140 ? 16.242 12.672 56.112 1.00 32.75 ? 143 GLY A N 1 ATOM 1092 C CA . GLY A 1 140 ? 17.077 13.001 57.254 1.00 33.70 ? 143 GLY A CA 1 ATOM 1093 C C . GLY A 1 140 ? 17.047 12.016 58.397 1.00 33.85 ? 143 GLY A C 1 ATOM 1094 O O . GLY A 1 140 ? 17.686 12.252 59.419 1.00 34.96 ? 143 GLY A O 1 ATOM 1095 N N . ASN A 1 141 ? 16.315 10.911 58.254 1.00 32.45 ? 144 ASN A N 1 ATOM 1096 C CA . ASN A 1 141 ? 16.292 9.930 59.329 1.00 32.51 ? 144 ASN A CA 1 ATOM 1097 C C . ASN A 1 141 ? 16.862 8.586 58.884 1.00 30.55 ? 144 ASN A C 1 ATOM 1098 O O . ASN A 1 141 ? 16.661 8.192 57.728 1.00 29.40 ? 144 ASN A O 1 ATOM 1099 C CB . ASN A 1 141 ? 14.876 9.745 59.878 1.00 33.59 ? 144 ASN A CB 1 ATOM 1100 C CG . ASN A 1 141 ? 14.415 10.948 60.744 1.00 38.43 ? 144 ASN A CG 1 ATOM 1101 O OD1 . ASN A 1 141 ? 15.097 11.353 61.707 1.00 43.92 ? 144 ASN A OD1 1 ATOM 1102 N ND2 . ASN A 1 141 ? 13.259 11.491 60.420 1.00 40.40 ? 144 ASN A ND2 1 ATOM 1103 N N . PRO A 1 142 ? 17.550 7.878 59.807 1.00 29.44 ? 145 PRO A N 1 ATOM 1104 C CA . PRO A 1 142 ? 18.028 6.531 59.484 1.00 27.63 ? 145 PRO A CA 1 ATOM 1105 C C . PRO A 1 142 ? 16.911 5.655 58.902 1.00 25.96 ? 145 PRO A C 1 ATOM 1106 O O . PRO A 1 142 ? 15.779 5.640 59.385 1.00 25.32 ? 145 PRO A O 1 ATOM 1107 C CB . PRO A 1 142 ? 18.483 5.985 60.836 1.00 28.09 ? 145 PRO A CB 1 ATOM 1108 C CG . PRO A 1 142 ? 18.926 7.244 61.620 1.00 29.14 ? 145 PRO A CG 1 ATOM 1109 C CD . PRO A 1 142 ? 17.890 8.274 61.199 1.00 30.36 ? 145 PRO A CD 1 ATOM 1110 N N . SER A 1 143 ? 17.215 4.930 57.844 1.00 24.69 ? 146 SER A N 1 ATOM 1111 C CA . SER A 1 143 ? 16.252 3.959 57.333 1.00 23.60 ? 146 SER A CA 1 ATOM 1112 C C . SER A 1 143 ? 17.009 2.711 56.824 1.00 22.23 ? 146 SER A C 1 ATOM 1113 O O . SER A 1 143 ? 18.158 2.502 57.212 1.00 21.45 ? 146 SER A O 1 ATOM 1114 C CB . SER A 1 143 ? 15.369 4.624 56.260 1.00 24.07 ? 146 SER A CB 1 ATOM 1115 O OG . SER A 1 143 ? 14.247 3.811 55.975 1.00 28.31 ? 146 SER A OG 1 ATOM 1116 N N . PHE A 1 144 ? 16.392 1.926 55.943 1.00 20.74 ? 147 PHE A N 1 ATOM 1117 C CA . PHE A 1 144 ? 16.976 0.645 55.511 1.00 20.80 ? 147 PHE A CA 1 ATOM 1118 C C . PHE A 1 144 ? 16.367 0.147 54.198 1.00 19.84 ? 147 PHE A C 1 ATOM 1119 O O . PHE A 1 144 ? 15.267 0.571 53.787 1.00 18.74 ? 147 PHE A O 1 ATOM 1120 C CB . PHE A 1 144 ? 16.779 -0.457 56.603 1.00 20.40 ? 147 PHE A CB 1 ATOM 1121 C CG . PHE A 1 144 ? 17.817 -1.583 56.537 1.00 21.34 ? 147 PHE A CG 1 ATOM 1122 C CD1 . PHE A 1 144 ? 19.185 -1.300 56.551 1.00 18.38 ? 147 PHE A CD1 1 ATOM 1123 C CD2 . PHE A 1 144 ? 17.415 -2.917 56.476 1.00 17.81 ? 147 PHE A CD2 1 ATOM 1124 C CE1 . PHE A 1 144 ? 20.135 -2.329 56.474 1.00 21.76 ? 147 PHE A CE1 1 ATOM 1125 C CE2 . PHE A 1 144 ? 18.384 -3.967 56.434 1.00 18.74 ? 147 PHE A CE2 1 ATOM 1126 C CZ . PHE A 1 144 ? 19.722 -3.675 56.442 1.00 19.07 ? 147 PHE A CZ 1 ATOM 1127 N N . PHE A 1 145 ? 17.096 -0.751 53.548 1.00 18.77 ? 148 PHE A N 1 ATOM 1128 C CA . PHE A 1 145 ? 16.596 -1.466 52.374 1.00 19.01 ? 148 PHE A CA 1 ATOM 1129 C C . PHE A 1 145 ? 15.144 -1.905 52.621 1.00 17.99 ? 148 PHE A C 1 ATOM 1130 O O . PHE A 1 145 ? 14.826 -2.469 53.668 1.00 18.67 ? 148 PHE A O 1 ATOM 1131 C CB . PHE A 1 145 ? 17.437 -2.725 52.146 1.00 18.24 ? 148 PHE A CB 1 ATOM 1132 C CG . PHE A 1 145 ? 18.896 -2.444 51.835 1.00 19.32 ? 148 PHE A CG 1 ATOM 1133 C CD1 . PHE A 1 145 ? 19.275 -1.941 50.580 1.00 17.35 ? 148 PHE A CD1 1 ATOM 1134 C CD2 . PHE A 1 145 ? 19.882 -2.719 52.787 1.00 19.94 ? 148 PHE A CD2 1 ATOM 1135 C CE1 . PHE A 1 145 ? 20.627 -1.710 50.265 1.00 20.34 ? 148 PHE A CE1 1 ATOM 1136 C CE2 . PHE A 1 145 ? 21.246 -2.484 52.503 1.00 20.03 ? 148 PHE A CE2 1 ATOM 1137 C CZ . PHE A 1 145 ? 21.616 -1.976 51.231 1.00 20.78 ? 148 PHE A CZ 1 ATOM 1138 N N . ARG A 1 146 ? 14.263 -1.608 51.684 1.00 18.55 ? 149 ARG A N 1 ATOM 1139 C CA . ARG A 1 146 ? 12.819 -1.819 51.906 1.00 20.46 ? 149 ARG A CA 1 ATOM 1140 C C . ARG A 1 146 ? 12.453 -3.290 51.954 1.00 20.39 ? 149 ARG A C 1 ATOM 1141 O O . ARG A 1 146 ? 11.433 -3.667 52.576 1.00 19.69 ? 149 ARG A O 1 ATOM 1142 C CB . ARG A 1 146 ? 11.992 -1.181 50.770 1.00 20.67 ? 149 ARG A CB 1 ATOM 1143 C CG . ARG A 1 146 ? 11.463 0.232 51.069 1.00 24.89 ? 149 ARG A CG 1 ATOM 1144 C CD . ARG A 1 146 ? 12.548 1.249 51.119 1.00 27.60 ? 149 ARG A CD 1 ATOM 1145 N NE . ARG A 1 146 ? 11.962 2.593 51.172 1.00 30.48 ? 149 ARG A NE 1 ATOM 1146 C CZ . ARG A 1 146 ? 11.885 3.339 52.274 1.00 34.85 ? 149 ARG A CZ 1 ATOM 1147 N NH1 . ARG A 1 146 ? 12.374 2.911 53.431 1.00 35.82 ? 149 ARG A NH1 1 ATOM 1148 N NH2 . ARG A 1 146 ? 11.331 4.537 52.208 1.00 37.61 ? 149 ARG A NH2 1 ATOM 1149 N N . ASN A 1 147 ? 13.251 -4.113 51.272 1.00 19.48 ? 150 ASN A N 1 ATOM 1150 C CA . ASN A 1 147 ? 12.906 -5.545 51.166 1.00 19.70 ? 150 ASN A CA 1 ATOM 1151 C C . ASN A 1 147 ? 13.478 -6.430 52.261 1.00 20.07 ? 150 ASN A C 1 ATOM 1152 O O . ASN A 1 147 ? 13.169 -7.635 52.327 1.00 19.16 ? 150 ASN A O 1 ATOM 1153 C CB . ASN A 1 147 ? 13.255 -6.070 49.750 1.00 18.85 ? 150 ASN A CB 1 ATOM 1154 C CG . ASN A 1 147 ? 12.478 -5.313 48.650 1.00 17.67 ? 150 ASN A CG 1 ATOM 1155 O OD1 . ASN A 1 147 ? 11.348 -4.851 48.895 1.00 21.75 ? 150 ASN A OD1 1 ATOM 1156 N ND2 . ASN A 1 147 ? 13.044 -5.234 47.425 1.00 15.14 ? 150 ASN A ND2 1 ATOM 1157 N N . MET A 1 148 ? 14.309 -5.828 53.117 1.00 20.16 ? 151 MET A N 1 ATOM 1158 C CA . MET A 1 148 ? 15.099 -6.572 54.084 1.00 20.58 ? 151 MET A CA 1 ATOM 1159 C C . MET A 1 148 ? 14.725 -6.108 55.476 1.00 21.15 ? 151 MET A C 1 ATOM 1160 O O . MET A 1 148 ? 14.147 -5.049 55.639 1.00 22.09 ? 151 MET A O 1 ATOM 1161 C CB . MET A 1 148 ? 16.608 -6.340 53.871 1.00 19.88 ? 151 MET A CB 1 ATOM 1162 C CG . MET A 1 148 ? 17.043 -6.458 52.402 1.00 21.64 ? 151 MET A CG 1 ATOM 1163 S SD . MET A 1 148 ? 16.686 -8.128 51.727 1.00 20.76 ? 151 MET A SD 1 ATOM 1164 C CE . MET A 1 148 ? 17.833 -9.083 52.698 1.00 18.34 ? 151 MET A CE 1 ATOM 1165 N N . VAL A 1 149 ? 15.083 -6.913 56.472 1.00 20.91 ? 152 VAL A N 1 ATOM 1166 C CA . VAL A 1 149 ? 14.784 -6.636 57.843 1.00 21.17 ? 152 VAL A CA 1 ATOM 1167 C C . VAL A 1 149 ? 16.054 -6.755 58.657 1.00 21.43 ? 152 VAL A C 1 ATOM 1168 O O . VAL A 1 149 ? 16.716 -7.808 58.648 1.00 19.97 ? 152 VAL A O 1 ATOM 1169 C CB . VAL A 1 149 ? 13.717 -7.630 58.381 1.00 21.70 ? 152 VAL A CB 1 ATOM 1170 C CG1 . VAL A 1 149 ? 13.332 -7.233 59.823 1.00 23.42 ? 152 VAL A CG1 1 ATOM 1171 C CG2 . VAL A 1 149 ? 12.477 -7.659 57.463 1.00 21.65 ? 152 VAL A CG2 1 ATOM 1172 N N . TRP A 1 150 ? 16.373 -5.690 59.400 1.00 21.66 ? 153 TRP A N 1 ATOM 1173 C CA . TRP A 1 150 ? 17.559 -5.678 60.235 1.00 23.23 ? 153 TRP A CA 1 ATOM 1174 C C . TRP A 1 150 ? 17.131 -6.095 61.645 1.00 24.67 ? 153 TRP A C 1 ATOM 1175 O O . TRP A 1 150 ? 16.552 -5.279 62.387 1.00 25.78 ? 153 TRP A O 1 ATOM 1176 C CB . TRP A 1 150 ? 18.170 -4.272 60.273 1.00 22.78 ? 153 TRP A CB 1 ATOM 1177 C CG . TRP A 1 150 ? 19.585 -4.225 60.783 1.00 21.26 ? 153 TRP A CG 1 ATOM 1178 C CD1 . TRP A 1 150 ? 20.234 -5.170 61.570 1.00 22.86 ? 153 TRP A CD1 1 ATOM 1179 C CD2 . TRP A 1 150 ? 20.511 -3.152 60.598 1.00 23.25 ? 153 TRP A CD2 1 ATOM 1180 N NE1 . TRP A 1 150 ? 21.529 -4.749 61.829 1.00 23.55 ? 153 TRP A NE1 1 ATOM 1181 C CE2 . TRP A 1 150 ? 21.709 -3.503 61.262 1.00 21.83 ? 153 TRP A CE2 1 ATOM 1182 C CE3 . TRP A 1 150 ? 20.447 -1.924 59.914 1.00 24.57 ? 153 TRP A CE3 1 ATOM 1183 C CZ2 . TRP A 1 150 ? 22.837 -2.684 61.241 1.00 22.30 ? 153 TRP A CZ2 1 ATOM 1184 C CZ3 . TRP A 1 150 ? 21.576 -1.092 59.901 1.00 23.25 ? 153 TRP A CZ3 1 ATOM 1185 C CH2 . TRP A 1 150 ? 22.758 -1.479 60.545 1.00 22.87 ? 153 TRP A CH2 1 ATOM 1186 N N . LEU A 1 151 ? 17.372 -7.354 62.006 1.00 25.43 ? 154 LEU A N 1 ATOM 1187 C CA . LEU A 1 151 ? 16.957 -7.856 63.317 1.00 26.83 ? 154 LEU A CA 1 ATOM 1188 C C . LEU A 1 151 ? 17.985 -7.369 64.339 1.00 27.49 ? 154 LEU A C 1 ATOM 1189 O O . LEU A 1 151 ? 19.190 -7.566 64.154 1.00 26.12 ? 154 LEU A O 1 ATOM 1190 C CB . LEU A 1 151 ? 16.872 -9.392 63.331 1.00 27.43 ? 154 LEU A CB 1 ATOM 1191 C CG . LEU A 1 151 ? 15.614 -10.091 62.776 1.00 29.15 ? 154 LEU A CG 1 ATOM 1192 C CD1 . LEU A 1 151 ? 15.426 -9.868 61.306 1.00 31.66 ? 154 LEU A CD1 1 ATOM 1193 C CD2 . LEU A 1 151 ? 15.745 -11.603 62.976 1.00 32.90 ? 154 LEU A CD2 1 ATOM 1194 N N . THR A 1 152 ? 17.515 -6.723 65.407 1.00 29.05 ? 155 THR A N 1 ATOM 1195 C CA . THR A 1 152 ? 18.423 -6.347 66.496 1.00 31.18 ? 155 THR A CA 1 ATOM 1196 C C . THR A 1 152 ? 17.873 -6.776 67.867 1.00 33.50 ? 155 THR A C 1 ATOM 1197 O O . THR A 1 152 ? 16.762 -7.271 67.968 1.00 33.23 ? 155 THR A O 1 ATOM 1198 C CB . THR A 1 152 ? 18.751 -4.835 66.481 1.00 30.79 ? 155 THR A CB 1 ATOM 1199 O OG1 . THR A 1 152 ? 17.546 -4.077 66.513 1.00 30.16 ? 155 THR A OG1 1 ATOM 1200 C CG2 . THR A 1 152 ? 19.560 -4.452 65.226 1.00 30.37 ? 155 THR A CG2 1 ATOM 1201 N N . GLU A 1 153 ? 18.698 -6.609 68.898 1.00 37.06 ? 156 GLU A N 1 ATOM 1202 C CA . GLU A 1 153 ? 18.346 -6.812 70.318 1.00 40.03 ? 156 GLU A CA 1 ATOM 1203 C C . GLU A 1 153 ? 16.964 -6.262 70.697 1.00 40.50 ? 156 GLU A C 1 ATOM 1204 O O . GLU A 1 153 ? 16.591 -5.182 70.269 1.00 40.66 ? 156 GLU A O 1 ATOM 1205 C CB . GLU A 1 153 ? 19.453 -6.126 71.160 1.00 40.97 ? 156 GLU A CB 1 ATOM 1206 C CG . GLU A 1 153 ? 19.078 -5.739 72.582 1.00 44.65 ? 156 GLU A CG 1 ATOM 1207 C CD . GLU A 1 153 ? 18.476 -4.370 72.684 1.00 47.43 ? 156 GLU A CD 1 ATOM 1208 O OE1 . GLU A 1 153 ? 19.128 -3.383 72.295 1.00 49.81 ? 156 GLU A OE1 1 ATOM 1209 O OE2 . GLU A 1 153 ? 17.342 -4.277 73.181 1.00 51.16 ? 156 GLU A OE2 1 ATOM 1210 N N . LYS A 1 154 ? 16.209 -6.994 71.515 1.00 42.44 ? 157 LYS A N 1 ATOM 1211 C CA . LYS A 1 154 ? 14.987 -6.437 72.122 1.00 43.93 ? 157 LYS A CA 1 ATOM 1212 C C . LYS A 1 154 ? 14.988 -6.686 73.637 1.00 45.14 ? 157 LYS A C 1 ATOM 1213 O O . LYS A 1 154 ? 15.150 -7.832 74.071 1.00 45.20 ? 157 LYS A O 1 ATOM 1214 C CB . LYS A 1 154 ? 13.734 -7.037 71.488 1.00 43.74 ? 157 LYS A CB 1 ATOM 1215 C CG . LYS A 1 154 ? 12.438 -6.401 71.970 1.00 45.22 ? 157 LYS A CG 1 ATOM 1216 C CD . LYS A 1 154 ? 11.242 -6.997 71.263 1.00 47.88 ? 157 LYS A CD 1 ATOM 1217 C CE . LYS A 1 154 ? 9.980 -6.247 71.607 1.00 51.08 ? 157 LYS A CE 1 ATOM 1218 N NZ . LYS A 1 154 ? 8.848 -7.193 71.593 1.00 53.95 ? 157 LYS A NZ 1 ATOM 1219 N N . GLY A 1 155 ? 14.819 -5.618 74.425 1.00 46.44 ? 158 GLY A N 1 ATOM 1220 C CA . GLY A 1 155 ? 14.867 -5.711 75.897 1.00 47.65 ? 158 GLY A CA 1 ATOM 1221 C C . GLY A 1 155 ? 16.191 -6.310 76.344 1.00 48.44 ? 158 GLY A C 1 ATOM 1222 O O . GLY A 1 155 ? 16.221 -7.223 77.169 1.00 48.78 ? 158 GLY A O 1 ATOM 1223 N N . SER A 1 156 ? 17.281 -5.805 75.753 1.00 48.55 ? 159 SER A N 1 ATOM 1224 C CA . SER A 1 156 ? 18.654 -6.304 75.945 1.00 48.42 ? 159 SER A CA 1 ATOM 1225 C C . SER A 1 156 ? 18.876 -7.798 75.701 1.00 47.88 ? 159 SER A C 1 ATOM 1226 O O . SER A 1 156 ? 19.851 -8.368 76.189 1.00 48.49 ? 159 SER A O 1 ATOM 1227 C CB . SER A 1 156 ? 19.221 -5.867 77.299 1.00 49.00 ? 159 SER A CB 1 ATOM 1228 O OG . SER A 1 156 ? 19.252 -4.456 77.377 1.00 50.83 ? 159 SER A OG 1 ATOM 1229 N N . ASN A 1 157 ? 17.994 -8.427 74.921 1.00 46.99 ? 160 ASN A N 1 ATOM 1230 C CA . ASN A 1 157 ? 18.182 -9.822 74.533 1.00 45.41 ? 160 ASN A CA 1 ATOM 1231 C C . ASN A 1 157 ? 18.036 -10.069 73.044 1.00 43.32 ? 160 ASN A C 1 ATOM 1232 O O . ASN A 1 157 ? 17.267 -9.399 72.375 1.00 43.12 ? 160 ASN A O 1 ATOM 1233 C CB . ASN A 1 157 ? 17.211 -10.738 75.279 1.00 46.27 ? 160 ASN A CB 1 ATOM 1234 C CG . ASN A 1 157 ? 17.546 -10.847 76.738 1.00 48.57 ? 160 ASN A CG 1 ATOM 1235 O OD1 . ASN A 1 157 ? 17.220 -9.956 77.522 1.00 51.27 ? 160 ASN A OD1 1 ATOM 1236 N ND2 . ASN A 1 157 ? 18.222 -11.932 77.115 1.00 49.93 ? 160 ASN A ND2 1 ATOM 1237 N N . TYR A 1 158 ? 18.775 -11.045 72.543 1.00 41.28 ? 161 TYR A N 1 ATOM 1238 C CA . TYR A 1 158 ? 18.584 -11.514 71.180 1.00 39.73 ? 161 TYR A CA 1 ATOM 1239 C C . TYR A 1 158 ? 18.478 -13.037 71.242 1.00 38.97 ? 161 TYR A C 1 ATOM 1240 O O . TYR A 1 158 ? 19.482 -13.737 71.131 1.00 38.83 ? 161 TYR A O 1 ATOM 1241 C CB . TYR A 1 158 ? 19.729 -11.003 70.284 1.00 38.78 ? 161 TYR A CB 1 ATOM 1242 C CG . TYR A 1 158 ? 19.578 -11.214 68.780 1.00 35.90 ? 161 TYR A CG 1 ATOM 1243 C CD1 . TYR A 1 158 ? 19.559 -10.125 67.905 1.00 32.68 ? 161 TYR A CD1 1 ATOM 1244 C CD2 . TYR A 1 158 ? 19.504 -12.498 68.236 1.00 32.17 ? 161 TYR A CD2 1 ATOM 1245 C CE1 . TYR A 1 158 ? 19.450 -10.310 66.522 1.00 30.41 ? 161 TYR A CE1 1 ATOM 1246 C CE2 . TYR A 1 158 ? 19.387 -12.705 66.859 1.00 29.61 ? 161 TYR A CE2 1 ATOM 1247 C CZ . TYR A 1 158 ? 19.368 -11.598 66.009 1.00 29.50 ? 161 TYR A CZ 1 ATOM 1248 O OH . TYR A 1 158 ? 19.283 -11.799 64.647 1.00 28.45 ? 161 TYR A OH 1 ATOM 1249 N N . PRO A 1 159 ? 17.247 -13.563 71.445 1.00 39.05 ? 162 PRO A N 1 ATOM 1250 C CA . PRO A 1 159 ? 17.052 -15.018 71.373 1.00 39.11 ? 162 PRO A CA 1 ATOM 1251 C C . PRO A 1 159 ? 17.326 -15.536 69.965 1.00 39.59 ? 162 PRO A C 1 ATOM 1252 O O . PRO A 1 159 ? 17.382 -14.736 69.001 1.00 39.78 ? 162 PRO A O 1 ATOM 1253 C CB . PRO A 1 159 ? 15.580 -15.218 71.754 1.00 40.01 ? 162 PRO A CB 1 ATOM 1254 C CG . PRO A 1 159 ? 14.920 -13.898 71.541 1.00 39.12 ? 162 PRO A CG 1 ATOM 1255 C CD . PRO A 1 159 ? 15.993 -12.827 71.676 1.00 38.68 ? 162 PRO A CD 1 ATOM 1256 N N . VAL A 1 160 ? 17.535 -16.843 69.850 1.00 38.85 ? 163 VAL A N 1 ATOM 1257 C CA . VAL A 1 160 ? 17.790 -17.466 68.563 1.00 39.35 ? 163 VAL A CA 1 ATOM 1258 C C . VAL A 1 160 ? 16.655 -17.069 67.617 1.00 38.28 ? 163 VAL A C 1 ATOM 1259 O O . VAL A 1 160 ? 15.480 -17.186 67.955 1.00 38.52 ? 163 VAL A O 1 ATOM 1260 C CB . VAL A 1 160 ? 17.930 -19.006 68.645 1.00 39.15 ? 163 VAL A CB 1 ATOM 1261 C CG1 . VAL A 1 160 ? 18.235 -19.589 67.274 1.00 39.98 ? 163 VAL A CG1 1 ATOM 1262 C CG2 . VAL A 1 160 ? 19.042 -19.398 69.626 1.00 41.47 ? 163 VAL A CG2 1 ATOM 1263 N N . ALA A 1 161 ? 17.033 -16.541 66.456 1.00 37.18 ? 164 ALA A N 1 ATOM 1264 C CA . ALA A 1 161 ? 16.063 -16.072 65.472 1.00 35.42 ? 164 ALA A CA 1 ATOM 1265 C C . ALA A 1 161 ? 15.888 -17.182 64.459 1.00 34.72 ? 164 ALA A C 1 ATOM 1266 O O . ALA A 1 161 ? 16.863 -17.657 63.883 1.00 33.74 ? 164 ALA A O 1 ATOM 1267 C CB . ALA A 1 161 ? 16.581 -14.790 64.792 1.00 34.83 ? 164 ALA A CB 1 ATOM 1268 N N . LYS A 1 162 ? 14.648 -17.613 64.247 1.00 34.42 ? 165 LYS A N 1 ATOM 1269 C CA . LYS A 1 162 ? 14.392 -18.675 63.283 1.00 34.90 ? 165 LYS A CA 1 ATOM 1270 C C . LYS A 1 162 ? 13.181 -18.272 62.459 1.00 33.24 ? 165 LYS A C 1 ATOM 1271 O O . LYS A 1 162 ? 12.178 -17.867 63.012 1.00 33.13 ? 165 LYS A O 1 ATOM 1272 C CB . LYS A 1 162 ? 14.091 -20.019 63.963 1.00 36.53 ? 165 LYS A CB 1 ATOM 1273 C CG . LYS A 1 162 ? 14.928 -20.369 65.197 1.00 40.58 ? 165 LYS A CG 1 ATOM 1274 C CD . LYS A 1 162 ? 14.180 -21.451 66.042 1.00 46.66 ? 165 LYS A CD 1 ATOM 1275 C CE . LYS A 1 162 ? 14.300 -21.199 67.560 1.00 50.61 ? 165 LYS A CE 1 ATOM 1276 N NZ . LYS A 1 162 ? 14.224 -22.465 68.394 1.00 52.82 ? 165 LYS A NZ 1 ATOM 1277 N N . GLY A 1 163 ? 13.301 -18.365 61.144 1.00 31.52 ? 166 GLY A N 1 ATOM 1278 C CA . GLY A 1 163 ? 12.193 -18.095 60.247 1.00 30.63 ? 166 GLY A CA 1 ATOM 1279 C C . GLY A 1 163 ? 12.255 -19.161 59.186 1.00 30.44 ? 166 GLY A C 1 ATOM 1280 O O . GLY A 1 163 ? 13.336 -19.678 58.869 1.00 30.08 ? 166 GLY A O 1 ATOM 1281 N N . SER A 1 164 ? 11.102 -19.497 58.638 1.00 28.63 ? 167 SER A N 1 ATOM 1282 C CA . SER A 1 164 ? 11.038 -20.557 57.678 1.00 28.93 ? 167 SER A CA 1 ATOM 1283 C C . SER A 1 164 ? 9.989 -20.235 56.615 1.00 27.12 ? 167 SER A C 1 ATOM 1284 O O . SER A 1 164 ? 8.983 -19.628 56.938 1.00 26.93 ? 167 SER A O 1 ATOM 1285 C CB . SER A 1 164 ? 10.704 -21.875 58.397 1.00 29.80 ? 167 SER A CB 1 ATOM 1286 O OG . SER A 1 164 ? 10.576 -22.880 57.437 1.00 32.94 ? 167 SER A OG 1 ATOM 1287 N N . TYR A 1 165 ? 10.264 -20.578 55.357 1.00 25.46 ? 168 TYR A N 1 ATOM 1288 C CA . TYR A 1 165 ? 9.279 -20.406 54.274 1.00 24.82 ? 168 TYR A CA 1 ATOM 1289 C C . TYR A 1 165 ? 9.286 -21.576 53.302 1.00 24.63 ? 168 TYR A C 1 ATOM 1290 O O . TYR A 1 165 ? 10.334 -21.944 52.749 1.00 24.49 ? 168 TYR A O 1 ATOM 1291 C CB . TYR A 1 165 ? 9.515 -19.090 53.499 1.00 23.56 ? 168 TYR A CB 1 ATOM 1292 C CG . TYR A 1 165 ? 8.620 -18.951 52.292 1.00 23.30 ? 168 TYR A CG 1 ATOM 1293 C CD1 . TYR A 1 165 ? 7.247 -18.670 52.431 1.00 21.09 ? 168 TYR A CD1 1 ATOM 1294 C CD2 . TYR A 1 165 ? 9.140 -19.115 50.990 1.00 23.39 ? 168 TYR A CD2 1 ATOM 1295 C CE1 . TYR A 1 165 ? 6.420 -18.585 51.296 1.00 19.98 ? 168 TYR A CE1 1 ATOM 1296 C CE2 . TYR A 1 165 ? 8.338 -19.029 49.871 1.00 22.27 ? 168 TYR A CE2 1 ATOM 1297 C CZ . TYR A 1 165 ? 6.981 -18.756 50.028 1.00 22.02 ? 168 TYR A CZ 1 ATOM 1298 O OH . TYR A 1 165 ? 6.185 -18.677 48.913 1.00 24.17 ? 168 TYR A OH 1 ATOM 1299 N N . ASN A 1 166 ? 8.103 -22.128 53.057 1.00 24.91 ? 169 ASN A N 1 ATOM 1300 C CA . ASN A 1 166 ? 7.942 -23.178 52.085 1.00 24.96 ? 169 ASN A CA 1 ATOM 1301 C C . ASN A 1 166 ? 7.456 -22.552 50.777 1.00 24.69 ? 169 ASN A C 1 ATOM 1302 O O . ASN A 1 166 ? 6.432 -21.885 50.767 1.00 25.22 ? 169 ASN A O 1 ATOM 1303 C CB . ASN A 1 166 ? 6.944 -24.217 52.635 1.00 25.64 ? 169 ASN A CB 1 ATOM 1304 C CG . ASN A 1 166 ? 6.696 -25.372 51.681 1.00 29.60 ? 169 ASN A CG 1 ATOM 1305 O OD1 . ASN A 1 166 ? 7.021 -25.307 50.483 1.00 27.06 ? 169 ASN A OD1 1 ATOM 1306 N ND2 . ASN A 1 166 ? 6.102 -26.448 52.209 1.00 34.33 ? 169 ASN A ND2 1 ATOM 1307 N N . ASN A 1 167 ? 8.192 -22.748 49.686 1.00 24.11 ? 170 ASN A N 1 ATOM 1308 C CA . ASN A 1 167 ? 7.816 -22.125 48.424 1.00 25.28 ? 170 ASN A CA 1 ATOM 1309 C C . ASN A 1 167 ? 6.600 -22.809 47.810 1.00 26.23 ? 170 ASN A C 1 ATOM 1310 O O . ASN A 1 167 ? 6.725 -23.744 47.017 1.00 26.72 ? 170 ASN A O 1 ATOM 1311 C CB . ASN A 1 167 ? 8.999 -22.079 47.441 1.00 23.96 ? 170 ASN A CB 1 ATOM 1312 C CG . ASN A 1 167 ? 8.647 -21.388 46.128 1.00 25.46 ? 170 ASN A CG 1 ATOM 1313 O OD1 . ASN A 1 167 ? 7.561 -20.815 45.968 1.00 24.70 ? 170 ASN A OD1 1 ATOM 1314 N ND2 . ASN A 1 167 ? 9.566 -21.438 45.181 1.00 24.58 ? 170 ASN A ND2 1 ATOM 1315 N N . THR A 1 168 ? 5.422 -22.311 48.164 1.00 27.40 ? 171 THR A N 1 ATOM 1316 C CA . THR A 1 168 ? 4.180 -22.814 47.562 1.00 28.66 ? 171 THR A CA 1 ATOM 1317 C C . THR A 1 168 ? 3.685 -21.869 46.457 1.00 29.09 ? 171 THR A C 1 ATOM 1318 O O . THR A 1 168 ? 2.563 -21.999 46.005 1.00 28.05 ? 171 THR A O 1 ATOM 1319 C CB . THR A 1 168 ? 3.077 -22.970 48.630 1.00 28.45 ? 171 THR A CB 1 ATOM 1320 O OG1 . THR A 1 168 ? 2.851 -21.688 49.223 1.00 28.58 ? 171 THR A OG1 1 ATOM 1321 C CG2 . THR A 1 168 ? 3.519 -23.946 49.734 1.00 28.57 ? 171 THR A CG2 1 ATOM 1322 N N . SER A 1 169 ? 4.531 -20.937 46.011 1.00 28.75 ? 172 SER A N 1 ATOM 1323 C CA . SER A 1 169 ? 4.101 -19.899 45.051 1.00 28.84 ? 172 SER A CA 1 ATOM 1324 C C . SER A 1 169 ? 3.822 -20.404 43.630 1.00 29.74 ? 172 SER A C 1 ATOM 1325 O O . SER A 1 169 ? 3.223 -19.687 42.825 1.00 30.50 ? 172 SER A O 1 ATOM 1326 C CB . SER A 1 169 ? 5.164 -18.777 44.964 1.00 28.88 ? 172 SER A CB 1 ATOM 1327 O OG . SER A 1 169 ? 6.268 -19.235 44.185 1.00 26.14 ? 172 SER A OG 1 ATOM 1328 N N . GLY A 1 170 ? 4.267 -21.607 43.300 1.00 29.49 ? 173 GLY A N 1 ATOM 1329 C CA . GLY A 1 170 ? 4.085 -22.123 41.941 1.00 30.89 ? 173 GLY A CA 1 ATOM 1330 C C . GLY A 1 170 ? 5.230 -21.907 40.952 1.00 31.23 ? 173 GLY A C 1 ATOM 1331 O O . GLY A 1 170 ? 5.162 -22.372 39.814 1.00 31.55 ? 173 GLY A O 1 ATOM 1332 N N . GLU A 1 171 ? 6.293 -21.225 41.383 1.00 29.10 ? 174 GLU A N 1 ATOM 1333 C CA . GLU A 1 171 ? 7.479 -21.044 40.545 1.00 29.00 ? 174 GLU A CA 1 ATOM 1334 C C . GLU A 1 171 ? 8.743 -20.945 41.416 1.00 26.56 ? 174 GLU A C 1 ATOM 1335 O O . GLU A 1 171 ? 8.663 -20.803 42.630 1.00 25.86 ? 174 GLU A O 1 ATOM 1336 C CB . GLU A 1 171 ? 7.327 -19.820 39.617 1.00 29.63 ? 174 GLU A CB 1 ATOM 1337 C CG . GLU A 1 171 ? 7.071 -20.164 38.128 1.00 34.27 ? 174 GLU A CG 1 ATOM 1338 C CD . GLU A 1 171 ? 8.393 -20.472 37.351 1.00 42.55 ? 174 GLU A CD 1 ATOM 1339 O OE1 . GLU A 1 171 ? 9.423 -20.830 38.008 1.00 43.19 ? 174 GLU A OE1 1 ATOM 1340 O OE2 . GLU A 1 171 ? 8.411 -20.359 36.090 1.00 42.75 ? 174 GLU A OE2 1 ATOM 1341 N N . GLN A 1 172 ? 9.908 -21.066 40.803 1.00 25.11 ? 175 GLN A N 1 ATOM 1342 C CA . GLN A 1 172 ? 11.149 -20.858 41.534 1.00 24.17 ? 175 GLN A CA 1 ATOM 1343 C C . GLN A 1 172 ? 11.154 -19.431 42.054 1.00 22.65 ? 175 GLN A C 1 ATOM 1344 O O . GLN A 1 172 ? 10.640 -18.521 41.384 1.00 20.92 ? 175 GLN A O 1 ATOM 1345 C CB . GLN A 1 172 ? 12.347 -21.042 40.618 1.00 24.71 ? 175 GLN A CB 1 ATOM 1346 C CG . GLN A 1 172 ? 12.600 -22.484 40.270 1.00 28.29 ? 175 GLN A CG 1 ATOM 1347 C CD . GLN A 1 172 ? 13.802 -22.618 39.385 1.00 33.56 ? 175 GLN A CD 1 ATOM 1348 O OE1 . GLN A 1 172 ? 13.920 -21.935 38.351 1.00 35.08 ? 175 GLN A OE1 1 ATOM 1349 N NE2 . GLN A 1 172 ? 14.709 -23.497 39.776 1.00 31.50 ? 175 GLN A NE2 1 ATOM 1350 N N . MET A 1 173 ? 11.716 -19.251 43.247 1.00 21.47 ? 176 MET A N 1 ATOM 1351 C CA . MET A 1 173 ? 11.690 -17.933 43.871 1.00 21.99 ? 176 MET A CA 1 ATOM 1352 C C . MET A 1 173 ? 13.086 -17.450 44.294 1.00 21.42 ? 176 MET A C 1 ATOM 1353 O O . MET A 1 173 ? 13.800 -18.146 45.018 1.00 20.73 ? 176 MET A O 1 ATOM 1354 C CB . MET A 1 173 ? 10.771 -17.978 45.095 1.00 21.07 ? 176 MET A CB 1 ATOM 1355 C CG . MET A 1 173 ? 10.570 -16.577 45.735 1.00 22.32 ? 176 MET A CG 1 ATOM 1356 S SD . MET A 1 173 ? 9.706 -16.845 47.271 1.00 25.40 ? 176 MET A SD 1 ATOM 1357 C CE . MET A 1 173 ? 8.014 -16.934 46.642 1.00 23.81 ? 176 MET A CE 1 ATOM 1358 N N . LEU A 1 174 ? 13.439 -16.239 43.877 1.00 21.34 ? 177 LEU A N 1 ATOM 1359 C CA . LEU A 1 174 ? 14.730 -15.664 44.261 1.00 20.72 ? 177 LEU A CA 1 ATOM 1360 C C . LEU A 1 174 ? 14.603 -15.077 45.667 1.00 20.12 ? 177 LEU A C 1 ATOM 1361 O O . LEU A 1 174 ? 13.693 -14.253 45.929 1.00 21.18 ? 177 LEU A O 1 ATOM 1362 C CB . LEU A 1 174 ? 15.111 -14.597 43.257 1.00 20.67 ? 177 LEU A CB 1 ATOM 1363 C CG . LEU A 1 174 ? 16.237 -13.660 43.718 1.00 22.57 ? 177 LEU A CG 1 ATOM 1364 C CD1 . LEU A 1 174 ? 17.565 -14.413 43.629 1.00 20.60 ? 177 LEU A CD1 1 ATOM 1365 C CD2 . LEU A 1 174 ? 16.216 -12.451 42.836 1.00 24.12 ? 177 LEU A CD2 1 ATOM 1366 N N . ILE A 1 175 ? 15.479 -15.504 46.574 1.00 19.03 ? 178 ILE A N 1 ATOM 1367 C CA . ILE A 1 175 ? 15.495 -15.002 47.967 1.00 17.99 ? 178 ILE A CA 1 ATOM 1368 C C . ILE A 1 175 ? 16.886 -14.485 48.315 1.00 19.03 ? 178 ILE A C 1 ATOM 1369 O O . ILE A 1 175 ? 17.910 -15.154 48.001 1.00 18.21 ? 178 ILE A O 1 ATOM 1370 C CB . ILE A 1 175 ? 15.061 -16.083 48.957 1.00 17.94 ? 178 ILE A CB 1 ATOM 1371 C CG1 . ILE A 1 175 ? 13.664 -16.637 48.548 1.00 18.49 ? 178 ILE A CG1 1 ATOM 1372 C CG2 . ILE A 1 175 ? 15.072 -15.529 50.398 1.00 18.30 ? 178 ILE A CG2 1 ATOM 1373 C CD1 . ILE A 1 175 ? 13.038 -17.640 49.509 1.00 20.34 ? 178 ILE A CD1 1 ATOM 1374 N N . ILE A 1 176 ? 16.951 -13.306 48.936 1.00 16.84 ? 179 ILE A N 1 ATOM 1375 C CA . ILE A 1 176 ? 18.259 -12.697 49.259 1.00 18.08 ? 179 ILE A CA 1 ATOM 1376 C C . ILE A 1 176 ? 18.337 -12.573 50.781 1.00 18.02 ? 179 ILE A C 1 ATOM 1377 O O . ILE A 1 176 ? 17.321 -12.359 51.406 1.00 18.88 ? 179 ILE A O 1 ATOM 1378 C CB . ILE A 1 176 ? 18.356 -11.304 48.580 1.00 17.42 ? 179 ILE A CB 1 ATOM 1379 C CG1 . ILE A 1 176 ? 18.388 -11.446 47.052 1.00 17.81 ? 179 ILE A CG1 1 ATOM 1380 C CG2 . ILE A 1 176 ? 19.603 -10.520 49.070 1.00 18.22 ? 179 ILE A CG2 1 ATOM 1381 C CD1 . ILE A 1 176 ? 17.998 -10.108 46.284 1.00 17.45 ? 179 ILE A CD1 1 ATOM 1382 N N . TRP A 1 177 ? 19.499 -12.793 51.387 1.00 18.08 ? 180 TRP A N 1 ATOM 1383 C CA . TRP A 1 177 ? 19.674 -12.497 52.817 1.00 18.46 ? 180 TRP A CA 1 ATOM 1384 C C . TRP A 1 177 ? 21.092 -11.899 53.008 1.00 19.82 ? 180 TRP A C 1 ATOM 1385 O O . TRP A 1 177 ? 21.881 -11.884 52.060 1.00 19.01 ? 180 TRP A O 1 ATOM 1386 C CB . TRP A 1 177 ? 19.516 -13.745 53.666 1.00 18.62 ? 180 TRP A CB 1 ATOM 1387 C CG . TRP A 1 177 ? 20.563 -14.800 53.318 1.00 20.40 ? 180 TRP A CG 1 ATOM 1388 C CD1 . TRP A 1 177 ? 21.772 -14.997 53.934 1.00 25.19 ? 180 TRP A CD1 1 ATOM 1389 C CD2 . TRP A 1 177 ? 20.487 -15.764 52.257 1.00 23.35 ? 180 TRP A CD2 1 ATOM 1390 N NE1 . TRP A 1 177 ? 22.441 -16.039 53.331 1.00 25.77 ? 180 TRP A NE1 1 ATOM 1391 C CE2 . TRP A 1 177 ? 21.683 -16.525 52.296 1.00 25.85 ? 180 TRP A CE2 1 ATOM 1392 C CE3 . TRP A 1 177 ? 19.529 -16.057 51.282 1.00 23.75 ? 180 TRP A CE3 1 ATOM 1393 C CZ2 . TRP A 1 177 ? 21.950 -17.562 51.386 1.00 26.79 ? 180 TRP A CZ2 1 ATOM 1394 C CZ3 . TRP A 1 177 ? 19.787 -17.086 50.366 1.00 26.79 ? 180 TRP A CZ3 1 ATOM 1395 C CH2 . TRP A 1 177 ? 20.995 -17.831 50.433 1.00 26.83 ? 180 TRP A CH2 1 ATOM 1396 N N . GLY A 1 178 ? 21.389 -11.414 54.208 1.00 19.15 ? 181 GLY A N 1 ATOM 1397 C CA . GLY A 1 178 ? 22.708 -10.840 54.447 1.00 19.34 ? 181 GLY A CA 1 ATOM 1398 C C . GLY A 1 178 ? 23.202 -11.134 55.846 1.00 19.77 ? 181 GLY A C 1 ATOM 1399 O O . GLY A 1 178 ? 22.433 -11.576 56.721 1.00 19.32 ? 181 GLY A O 1 ATOM 1400 N N . VAL A 1 179 ? 24.488 -10.850 56.052 1.00 19.07 ? 182 VAL A N 1 ATOM 1401 C CA . VAL A 1 179 ? 25.087 -10.922 57.354 1.00 19.51 ? 182 VAL A CA 1 ATOM 1402 C C . VAL A 1 179 ? 25.811 -9.587 57.567 1.00 19.15 ? 182 VAL A C 1 ATOM 1403 O O . VAL A 1 179 ? 26.502 -9.123 56.682 1.00 18.95 ? 182 VAL A O 1 ATOM 1404 C CB . VAL A 1 179 ? 26.112 -12.097 57.447 1.00 19.12 ? 182 VAL A CB 1 ATOM 1405 C CG1 . VAL A 1 179 ? 27.267 -11.922 56.423 1.00 21.51 ? 182 VAL A CG1 1 ATOM 1406 C CG2 . VAL A 1 179 ? 26.708 -12.170 58.833 1.00 18.88 ? 182 VAL A CG2 1 ATOM 1407 N N . HIS A 1 180 ? 25.628 -8.994 58.739 1.00 19.82 ? 183 HIS A N 1 ATOM 1408 C CA . HIS A 1 180 ? 26.265 -7.733 59.096 1.00 21.39 ? 183 HIS A CA 1 ATOM 1409 C C . HIS A 1 180 ? 27.614 -8.026 59.773 1.00 21.95 ? 183 HIS A C 1 ATOM 1410 O O . HIS A 1 180 ? 27.671 -8.746 60.779 1.00 22.42 ? 183 HIS A O 1 ATOM 1411 C CB . HIS A 1 180 ? 25.355 -6.973 60.061 1.00 21.35 ? 183 HIS A CB 1 ATOM 1412 C CG . HIS A 1 180 ? 25.885 -5.631 60.446 1.00 22.65 ? 183 HIS A CG 1 ATOM 1413 N ND1 . HIS A 1 180 ? 25.813 -5.140 61.731 1.00 25.04 ? 183 HIS A ND1 1 ATOM 1414 C CD2 . HIS A 1 180 ? 26.523 -4.685 59.713 1.00 24.17 ? 183 HIS A CD2 1 ATOM 1415 C CE1 . HIS A 1 180 ? 26.392 -3.949 61.776 1.00 24.70 ? 183 HIS A CE1 1 ATOM 1416 N NE2 . HIS A 1 180 ? 26.837 -3.657 60.568 1.00 23.94 ? 183 HIS A NE2 1 ATOM 1417 N N . HIS A 1 181 ? 28.680 -7.511 59.182 1.00 21.59 ? 184 HIS A N 1 ATOM 1418 C CA . HIS A 1 181 ? 30.017 -7.561 59.746 1.00 23.22 ? 184 HIS A CA 1 ATOM 1419 C C . HIS A 1 181 ? 30.300 -6.204 60.374 1.00 23.16 ? 184 HIS A C 1 ATOM 1420 O O . HIS A 1 181 ? 30.575 -5.237 59.651 1.00 22.79 ? 184 HIS A O 1 ATOM 1421 C CB . HIS A 1 181 ? 31.049 -7.823 58.653 1.00 22.47 ? 184 HIS A CB 1 ATOM 1422 C CG . HIS A 1 181 ? 30.798 -9.086 57.874 1.00 25.33 ? 184 HIS A CG 1 ATOM 1423 N ND1 . HIS A 1 181 ? 30.932 -10.343 58.428 1.00 25.87 ? 184 HIS A ND1 1 ATOM 1424 C CD2 . HIS A 1 181 ? 30.447 -9.281 56.582 1.00 27.52 ? 184 HIS A CD2 1 ATOM 1425 C CE1 . HIS A 1 181 ? 30.640 -11.259 57.520 1.00 26.32 ? 184 HIS A CE1 1 ATOM 1426 N NE2 . HIS A 1 181 ? 30.377 -10.641 56.381 1.00 27.91 ? 184 HIS A NE2 1 ATOM 1427 N N . PRO A 1 182 ? 30.239 -6.125 61.716 1.00 23.77 ? 185 PRO A N 1 ATOM 1428 C CA . PRO A 1 182 ? 30.349 -4.823 62.367 1.00 25.04 ? 185 PRO A CA 1 ATOM 1429 C C . PRO A 1 182 ? 31.770 -4.255 62.338 1.00 27.09 ? 185 PRO A C 1 ATOM 1430 O O . PRO A 1 182 ? 32.732 -4.986 62.069 1.00 25.89 ? 185 PRO A O 1 ATOM 1431 C CB . PRO A 1 182 ? 29.936 -5.111 63.817 1.00 25.68 ? 185 PRO A CB 1 ATOM 1432 C CG . PRO A 1 182 ? 29.187 -6.460 63.747 1.00 24.04 ? 185 PRO A CG 1 ATOM 1433 C CD . PRO A 1 182 ? 29.961 -7.196 62.690 1.00 23.81 ? 185 PRO A CD 1 ATOM 1434 N N . ASN A 1 183 ? 31.877 -2.952 62.593 1.00 28.58 ? 186 ASN A N 1 ATOM 1435 C CA . ASN A 1 183 ? 33.178 -2.245 62.684 1.00 32.30 ? 186 ASN A CA 1 ATOM 1436 C C . ASN A 1 183 ? 33.943 -2.608 63.970 1.00 34.54 ? 186 ASN A C 1 ATOM 1437 O O . ASN A 1 183 ? 35.179 -2.770 63.948 1.00 34.34 ? 186 ASN A O 1 ATOM 1438 C CB . ASN A 1 183 ? 32.936 -0.721 62.532 1.00 32.65 ? 186 ASN A CB 1 ATOM 1439 C CG . ASN A 1 183 ? 34.231 0.097 62.418 1.00 35.88 ? 186 ASN A CG 1 ATOM 1440 O OD1 . ASN A 1 183 ? 34.986 0.012 61.435 1.00 39.15 ? 186 ASN A OD1 1 ATOM 1441 N ND2 . ASN A 1 183 ? 34.470 0.923 63.424 1.00 41.37 ? 186 ASN A ND2 1 ATOM 1442 N N . ASP A 1 184 ? 33.195 -2.820 65.066 1.00 37.13 ? 187 ASP A N 1 ATOM 1443 C CA . ASP A 1 184 ? 33.756 -2.967 66.419 1.00 40.02 ? 187 ASP A CA 1 ATOM 1444 C C . ASP A 1 184 ? 32.804 -3.708 67.384 1.00 41.28 ? 187 ASP A C 1 ATOM 1445 O O . ASP A 1 184 ? 31.697 -4.106 67.016 1.00 40.88 ? 187 ASP A O 1 ATOM 1446 C CB . ASP A 1 184 ? 34.143 -1.577 66.986 1.00 40.44 ? 187 ASP A CB 1 ATOM 1447 C CG . ASP A 1 184 ? 32.964 -0.608 67.007 1.00 42.59 ? 187 ASP A CG 1 ATOM 1448 O OD1 . ASP A 1 184 ? 31.962 -0.898 67.685 1.00 45.84 ? 187 ASP A OD1 1 ATOM 1449 O OD2 . ASP A 1 184 ? 33.014 0.430 66.317 1.00 46.29 ? 187 ASP A OD2 1 ATOM 1450 N N . GLU A 1 185 ? 33.246 -3.876 68.628 1.00 43.44 ? 188 GLU A N 1 ATOM 1451 C CA . GLU A 1 185 ? 32.514 -4.639 69.656 1.00 44.53 ? 188 GLU A CA 1 ATOM 1452 C C . GLU A 1 185 ? 31.359 -3.829 70.227 1.00 45.11 ? 188 GLU A C 1 ATOM 1453 O O . GLU A 1 185 ? 30.275 -4.355 70.505 1.00 44.91 ? 188 GLU A O 1 ATOM 1454 C CB . GLU A 1 185 ? 33.448 -5.040 70.799 1.00 45.60 ? 188 GLU A CB 1 ATOM 1455 C CG . GLU A 1 185 ? 34.932 -5.209 70.428 1.00 49.69 ? 188 GLU A CG 1 ATOM 1456 C CD . GLU A 1 185 ? 35.705 -3.878 70.287 1.00 52.97 ? 188 GLU A CD 1 ATOM 1457 O OE1 . GLU A 1 185 ? 36.058 -3.262 71.324 1.00 55.92 ? 188 GLU A OE1 1 ATOM 1458 O OE2 . GLU A 1 185 ? 35.984 -3.468 69.131 1.00 54.34 ? 188 GLU A OE2 1 ATOM 1459 N N . THR A 1 186 ? 31.588 -2.537 70.428 1.00 46.17 ? 189 THR A N 1 ATOM 1460 C CA . THR A 1 186 ? 30.515 -1.682 70.945 1.00 46.67 ? 189 THR A CA 1 ATOM 1461 C C . THR A 1 186 ? 29.290 -1.771 70.013 1.00 45.89 ? 189 THR A C 1 ATOM 1462 O O . THR A 1 186 ? 28.140 -1.909 70.474 1.00 46.56 ? 189 THR A O 1 ATOM 1463 C CB . THR A 1 186 ? 31.005 -0.233 71.161 1.00 47.45 ? 189 THR A CB 1 ATOM 1464 O OG1 . THR A 1 186 ? 31.192 0.410 69.890 1.00 49.23 ? 189 THR A OG1 1 ATOM 1465 C CG2 . THR A 1 186 ? 32.322 -0.260 71.916 1.00 47.52 ? 189 THR A CG2 1 ATOM 1466 N N . GLU A 1 187 ? 29.548 -1.768 68.708 1.00 44.54 ? 190 GLU A N 1 ATOM 1467 C CA . GLU A 1 187 ? 28.501 -1.985 67.718 1.00 43.51 ? 190 GLU A CA 1 ATOM 1468 C C . GLU A 1 187 ? 27.817 -3.383 67.814 1.00 42.21 ? 190 GLU A C 1 ATOM 1469 O O . GLU A 1 187 ? 26.588 -3.476 67.764 1.00 41.46 ? 190 GLU A O 1 ATOM 1470 C CB . GLU A 1 187 ? 29.063 -1.770 66.322 1.00 43.20 ? 190 GLU A CB 1 ATOM 1471 C CG . GLU A 1 187 ? 28.012 -1.819 65.261 1.00 45.15 ? 190 GLU A CG 1 ATOM 1472 C CD . GLU A 1 187 ? 28.523 -1.423 63.902 1.00 47.60 ? 190 GLU A CD 1 ATOM 1473 O OE1 . GLU A 1 187 ? 29.738 -1.561 63.614 1.00 48.22 ? 190 GLU A OE1 1 ATOM 1474 O OE2 . GLU A 1 187 ? 27.684 -0.985 63.104 1.00 50.11 ? 190 GLU A OE2 1 ATOM 1475 N N . GLN A 1 188 ? 28.616 -4.440 67.931 1.00 40.98 ? 191 GLN A N 1 ATOM 1476 C CA . GLN A 1 188 ? 28.098 -5.791 68.061 1.00 41.07 ? 191 GLN A CA 1 ATOM 1477 C C . GLN A 1 188 ? 27.191 -5.928 69.295 1.00 41.73 ? 191 GLN A C 1 ATOM 1478 O O . GLN A 1 188 ? 26.123 -6.554 69.234 1.00 41.01 ? 191 GLN A O 1 ATOM 1479 C CB . GLN A 1 188 ? 29.249 -6.804 68.115 1.00 40.30 ? 191 GLN A CB 1 ATOM 1480 C CG . GLN A 1 188 ? 28.824 -8.285 68.331 1.00 38.97 ? 191 GLN A CG 1 ATOM 1481 C CD . GLN A 1 188 ? 28.138 -8.928 67.117 1.00 35.57 ? 191 GLN A CD 1 ATOM 1482 O OE1 . GLN A 1 188 ? 28.345 -8.517 65.977 1.00 35.42 ? 191 GLN A OE1 1 ATOM 1483 N NE2 . GLN A 1 188 ? 27.337 -9.961 67.362 1.00 34.44 ? 191 GLN A NE2 1 ATOM 1484 N N . ARG A 1 189 ? 27.606 -5.312 70.403 1.00 42.39 ? 192 ARG A N 1 ATOM 1485 C CA . ARG A 1 189 ? 26.864 -5.414 71.642 1.00 42.84 ? 192 ARG A CA 1 ATOM 1486 C C . ARG A 1 189 ? 25.616 -4.535 71.631 1.00 43.23 ? 192 ARG A C 1 ATOM 1487 O O . ARG A 1 189 ? 24.539 -4.978 72.045 1.00 44.07 ? 192 ARG A O 1 ATOM 1488 C CB . ARG A 1 189 ? 27.767 -5.070 72.831 1.00 43.71 ? 192 ARG A CB 1 ATOM 1489 C CG . ARG A 1 189 ? 27.055 -5.015 74.179 1.00 46.96 ? 192 ARG A CG 1 ATOM 1490 C CD . ARG A 1 189 ? 27.846 -4.195 75.197 1.00 52.05 ? 192 ARG A CD 1 ATOM 1491 N NE . ARG A 1 189 ? 27.715 -2.757 74.943 1.00 55.64 ? 192 ARG A NE 1 ATOM 1492 C CZ . ARG A 1 189 ? 28.721 -1.966 74.585 1.00 56.91 ? 192 ARG A CZ 1 ATOM 1493 N NH1 . ARG A 1 189 ? 29.951 -2.464 74.447 1.00 58.13 ? 192 ARG A NH1 1 ATOM 1494 N NH2 . ARG A 1 189 ? 28.498 -0.672 74.369 1.00 57.26 ? 192 ARG A NH2 1 ATOM 1495 N N . THR A 1 190 ? 25.737 -3.293 71.176 1.00 43.01 ? 193 THR A N 1 ATOM 1496 C CA . THR A 1 190 ? 24.578 -2.408 71.216 1.00 43.15 ? 193 THR A CA 1 ATOM 1497 C C . THR A 1 190 ? 23.470 -2.954 70.293 1.00 42.12 ? 193 THR A C 1 ATOM 1498 O O . THR A 1 190 ? 22.286 -2.848 70.604 1.00 41.72 ? 193 THR A O 1 ATOM 1499 C CB . THR A 1 190 ? 24.929 -0.962 70.879 1.00 43.16 ? 193 THR A CB 1 ATOM 1500 O OG1 . THR A 1 190 ? 25.365 -0.877 69.517 1.00 46.66 ? 193 THR A OG1 1 ATOM 1501 C CG2 . THR A 1 190 ? 26.037 -0.443 71.794 1.00 44.21 ? 193 THR A CG2 1 ATOM 1502 N N . LEU A 1 191 ? 23.870 -3.558 69.169 1.00 41.15 ? 194 LEU A N 1 ATOM 1503 C CA . LEU A 1 191 ? 22.905 -4.099 68.204 1.00 39.50 ? 194 LEU A CA 1 ATOM 1504 C C . LEU A 1 191 ? 22.352 -5.489 68.541 1.00 38.72 ? 194 LEU A C 1 ATOM 1505 O O . LEU A 1 191 ? 21.167 -5.724 68.378 1.00 37.89 ? 194 LEU A O 1 ATOM 1506 C CB . LEU A 1 191 ? 23.511 -4.113 66.787 1.00 39.28 ? 194 LEU A CB 1 ATOM 1507 C CG . LEU A 1 191 ? 23.828 -2.767 66.130 1.00 39.46 ? 194 LEU A CG 1 ATOM 1508 C CD1 . LEU A 1 191 ? 24.407 -2.995 64.742 1.00 39.78 ? 194 LEU A CD1 1 ATOM 1509 C CD2 . LEU A 1 191 ? 22.607 -1.864 66.047 1.00 40.64 ? 194 LEU A CD2 1 ATOM 1510 N N . TYR A 1 192 ? 23.205 -6.397 69.002 1.00 38.24 ? 195 TYR A N 1 ATOM 1511 C CA . TYR A 1 192 ? 22.855 -7.826 69.034 1.00 38.87 ? 195 TYR A CA 1 ATOM 1512 C C . TYR A 1 192 ? 22.968 -8.475 70.401 1.00 40.68 ? 195 TYR A C 1 ATOM 1513 O O . TYR A 1 192 ? 22.619 -9.647 70.537 1.00 40.67 ? 195 TYR A O 1 ATOM 1514 C CB . TYR A 1 192 ? 23.721 -8.622 68.042 1.00 37.40 ? 195 TYR A CB 1 ATOM 1515 C CG . TYR A 1 192 ? 23.716 -8.020 66.655 1.00 33.13 ? 195 TYR A CG 1 ATOM 1516 C CD1 . TYR A 1 192 ? 22.534 -7.941 65.924 1.00 30.39 ? 195 TYR A CD1 1 ATOM 1517 C CD2 . TYR A 1 192 ? 24.877 -7.491 66.111 1.00 31.16 ? 195 TYR A CD2 1 ATOM 1518 C CE1 . TYR A 1 192 ? 22.509 -7.361 64.662 1.00 29.57 ? 195 TYR A CE1 1 ATOM 1519 C CE2 . TYR A 1 192 ? 24.878 -6.901 64.852 1.00 28.04 ? 195 TYR A CE2 1 ATOM 1520 C CZ . TYR A 1 192 ? 23.687 -6.842 64.139 1.00 26.88 ? 195 TYR A CZ 1 ATOM 1521 O OH . TYR A 1 192 ? 23.677 -6.279 62.904 1.00 25.47 ? 195 TYR A OH 1 ATOM 1522 N N . GLN A 1 193 ? 23.465 -7.715 71.384 1.00 42.49 ? 196 GLN A N 1 ATOM 1523 C CA . GLN A 1 193 ? 23.821 -8.222 72.742 1.00 44.78 ? 196 GLN A CA 1 ATOM 1524 C C . GLN A 1 193 ? 24.806 -9.382 72.779 1.00 44.74 ? 196 GLN A C 1 ATOM 1525 O O . GLN A 1 193 ? 25.781 -9.340 73.532 1.00 46.00 ? 196 GLN A O 1 ATOM 1526 C CB . GLN A 1 193 ? 22.576 -8.497 73.602 1.00 45.29 ? 196 GLN A CB 1 ATOM 1527 C CG . GLN A 1 193 ? 21.746 -7.232 73.864 1.00 48.09 ? 196 GLN A CG 1 ATOM 1528 C CD . GLN A 1 193 ? 22.452 -6.228 74.767 1.00 52.99 ? 196 GLN A CD 1 ATOM 1529 O OE1 . GLN A 1 193 ? 23.030 -6.619 75.785 1.00 56.47 ? 196 GLN A OE1 1 ATOM 1530 N NE2 . GLN A 1 193 ? 22.411 -4.933 74.403 1.00 51.96 ? 196 GLN A NE2 1 ATOM 1531 N N . ASN A 1 194 ? 24.570 -10.399 71.957 1.00 44.88 ? 197 ASN A N 1 ATOM 1532 C CA . ASN A 1 194 ? 25.428 -11.573 71.881 1.00 44.62 ? 197 ASN A CA 1 ATOM 1533 C C . ASN A 1 194 ? 26.741 -11.347 71.149 1.00 44.45 ? 197 ASN A C 1 ATOM 1534 O O . ASN A 1 194 ? 26.843 -10.553 70.197 1.00 43.77 ? 197 ASN A O 1 ATOM 1535 C CB . ASN A 1 194 ? 24.698 -12.735 71.192 1.00 44.78 ? 197 ASN A CB 1 ATOM 1536 C CG . ASN A 1 194 ? 23.330 -13.025 71.803 1.00 47.00 ? 197 ASN A CG 1 ATOM 1537 O OD1 . ASN A 1 194 ? 23.092 -12.748 72.979 1.00 49.62 ? 197 ASN A OD1 1 ATOM 1538 N ND2 . ASN A 1 194 ? 22.420 -13.588 70.994 1.00 48.07 ? 197 ASN A ND2 1 ATOM 1539 N N . VAL A 1 195 ? 27.741 -12.098 71.579 1.00 43.96 ? 198 VAL A N 1 ATOM 1540 C CA . VAL A 1 195 ? 29.003 -12.148 70.886 1.00 43.46 ? 198 VAL A CA 1 ATOM 1541 C C . VAL A 1 195 ? 29.187 -13.583 70.464 1.00 42.90 ? 198 VAL A C 1 ATOM 1542 O O . VAL A 1 195 ? 28.546 -14.470 71.013 1.00 44.09 ? 198 VAL A O 1 ATOM 1543 C CB . VAL A 1 195 ? 30.151 -11.640 71.786 1.00 44.58 ? 198 VAL A CB 1 ATOM 1544 C CG1 . VAL A 1 195 ? 30.062 -10.144 71.905 1.00 43.71 ? 198 VAL A CG1 1 ATOM 1545 C CG2 . VAL A 1 195 ? 30.083 -12.289 73.189 1.00 44.73 ? 198 VAL A CG2 1 ATOM 1546 N N . GLY A 1 196 ? 30.024 -13.819 69.468 1.00 42.00 ? 199 GLY A N 1 ATOM 1547 C CA . GLY A 1 196 ? 30.223 -15.161 68.958 1.00 39.85 ? 199 GLY A CA 1 ATOM 1548 C C . GLY A 1 196 ? 28.929 -15.668 68.320 1.00 39.10 ? 199 GLY A C 1 ATOM 1549 O O . GLY A 1 196 ? 28.406 -16.719 68.705 1.00 38.83 ? 199 GLY A O 1 ATOM 1550 N N . THR A 1 197 ? 28.433 -14.929 67.330 1.00 36.47 ? 200 THR A N 1 ATOM 1551 C CA . THR A 1 197 ? 27.157 -15.243 66.672 1.00 34.37 ? 200 THR A CA 1 ATOM 1552 C C . THR A 1 197 ? 27.340 -15.953 65.329 1.00 33.44 ? 200 THR A C 1 ATOM 1553 O O . THR A 1 197 ? 28.450 -16.133 64.856 1.00 32.68 ? 200 THR A O 1 ATOM 1554 C CB . THR A 1 197 ? 26.346 -13.932 66.445 1.00 34.35 ? 200 THR A CB 1 ATOM 1555 O OG1 . THR A 1 197 ? 27.107 -13.061 65.611 1.00 30.49 ? 200 THR A OG1 1 ATOM 1556 C CG2 . THR A 1 197 ? 26.082 -13.241 67.725 1.00 33.50 ? 200 THR A CG2 1 ATOM 1557 N N . TYR A 1 198 ? 26.234 -16.368 64.696 1.00 33.09 ? 201 TYR A N 1 ATOM 1558 C CA . TYR A 1 198 ? 26.294 -16.947 63.350 1.00 32.31 ? 201 TYR A CA 1 ATOM 1559 C C . TYR A 1 198 ? 24.978 -16.716 62.599 1.00 30.76 ? 201 TYR A C 1 ATOM 1560 O O . TYR A 1 198 ? 23.969 -16.439 63.189 1.00 28.99 ? 201 TYR A O 1 ATOM 1561 C CB . TYR A 1 198 ? 26.521 -18.468 63.423 1.00 33.30 ? 201 TYR A CB 1 ATOM 1562 C CG . TYR A 1 198 ? 25.351 -19.153 64.077 1.00 37.62 ? 201 TYR A CG 1 ATOM 1563 C CD1 . TYR A 1 198 ? 24.283 -19.646 63.326 1.00 38.64 ? 201 TYR A CD1 1 ATOM 1564 C CD2 . TYR A 1 198 ? 25.281 -19.244 65.469 1.00 41.81 ? 201 TYR A CD2 1 ATOM 1565 C CE1 . TYR A 1 198 ? 23.197 -20.238 63.953 1.00 41.96 ? 201 TYR A CE1 1 ATOM 1566 C CE2 . TYR A 1 198 ? 24.233 -19.826 66.087 1.00 43.93 ? 201 TYR A CE2 1 ATOM 1567 C CZ . TYR A 1 198 ? 23.189 -20.327 65.341 1.00 44.38 ? 201 TYR A CZ 1 ATOM 1568 O OH . TYR A 1 198 ? 22.155 -20.898 66.031 1.00 45.98 ? 201 TYR A OH 1 ATOM 1569 N N . VAL A 1 199 ? 25.035 -16.817 61.283 1.00 30.78 ? 202 VAL A N 1 ATOM 1570 C CA . VAL A 1 199 ? 23.848 -16.797 60.481 1.00 31.08 ? 202 VAL A CA 1 ATOM 1571 C C . VAL A 1 199 ? 23.861 -18.060 59.637 1.00 30.60 ? 202 VAL A C 1 ATOM 1572 O O . VAL A 1 199 ? 24.753 -18.227 58.806 1.00 31.69 ? 202 VAL A O 1 ATOM 1573 C CB . VAL A 1 199 ? 23.799 -15.556 59.553 1.00 29.94 ? 202 VAL A CB 1 ATOM 1574 C CG1 . VAL A 1 199 ? 22.558 -15.609 58.723 1.00 29.83 ? 202 VAL A CG1 1 ATOM 1575 C CG2 . VAL A 1 199 ? 23.855 -14.232 60.374 1.00 31.97 ? 202 VAL A CG2 1 ATOM 1576 N N . SER A 1 200 ? 22.850 -18.919 59.836 1.00 30.99 ? 203 SER A N 1 ATOM 1577 C CA . SER A 1 200 ? 22.662 -20.157 59.063 1.00 30.30 ? 203 SER A CA 1 ATOM 1578 C C . SER A 1 200 ? 21.449 -20.147 58.137 1.00 29.90 ? 203 SER A C 1 ATOM 1579 O O . SER A 1 200 ? 20.336 -19.807 58.561 1.00 29.24 ? 203 SER A O 1 ATOM 1580 C CB . SER A 1 200 ? 22.520 -21.376 59.987 1.00 30.72 ? 203 SER A CB 1 ATOM 1581 O OG . SER A 1 200 ? 23.617 -22.281 59.835 1.00 35.62 ? 203 SER A OG 1 ATOM 1582 N N . VAL A 1 201 ? 21.667 -20.551 56.883 1.00 28.83 ? 204 VAL A N 1 ATOM 1583 C CA . VAL A 1 201 ? 20.591 -20.708 55.915 1.00 27.92 ? 204 VAL A CA 1 ATOM 1584 C C . VAL A 1 201 ? 20.657 -22.150 55.396 1.00 28.94 ? 204 VAL A C 1 ATOM 1585 O O . VAL A 1 201 ? 21.751 -22.673 55.138 1.00 28.55 ? 204 VAL A O 1 ATOM 1586 C CB . VAL A 1 201 ? 20.724 -19.739 54.740 1.00 28.23 ? 204 VAL A CB 1 ATOM 1587 C CG1 . VAL A 1 201 ? 19.483 -19.837 53.831 1.00 27.97 ? 204 VAL A CG1 1 ATOM 1588 C CG2 . VAL A 1 201 ? 20.862 -18.286 55.262 1.00 26.39 ? 204 VAL A CG2 1 ATOM 1589 N N . GLY A 1 202 ? 19.497 -22.792 55.285 1.00 28.54 ? 205 GLY A N 1 ATOM 1590 C CA . GLY A 1 202 ? 19.426 -24.161 54.762 1.00 28.06 ? 205 GLY A CA 1 ATOM 1591 C C . GLY A 1 202 ? 18.163 -24.395 53.939 1.00 28.43 ? 205 GLY A C 1 ATOM 1592 O O . GLY A 1 202 ? 17.054 -24.006 54.332 1.00 27.25 ? 205 GLY A O 1 ATOM 1593 N N . THR A 1 203 ? 18.346 -24.999 52.778 1.00 27.59 ? 206 THR A N 1 ATOM 1594 C CA . THR A 1 203 ? 17.243 -25.549 52.016 1.00 28.57 ? 206 THR A CA 1 ATOM 1595 C C . THR A 1 203 ? 17.535 -27.074 51.862 1.00 29.28 ? 206 THR A C 1 ATOM 1596 O O . THR A 1 203 ? 18.413 -27.633 52.566 1.00 28.73 ? 206 THR A O 1 ATOM 1597 C CB . THR A 1 203 ? 17.149 -24.859 50.655 1.00 27.37 ? 206 THR A CB 1 ATOM 1598 O OG1 . THR A 1 203 ? 18.304 -25.195 49.875 1.00 30.16 ? 206 THR A OG1 1 ATOM 1599 C CG2 . THR A 1 203 ? 17.064 -23.308 50.788 1.00 30.38 ? 206 THR A CG2 1 ATOM 1600 N N . SER A 1 204 ? 16.846 -27.728 50.935 1.00 30.54 ? 207 SER A N 1 ATOM 1601 C CA . SER A 1 204 ? 17.131 -29.133 50.639 1.00 32.29 ? 207 SER A CA 1 ATOM 1602 C C . SER A 1 204 ? 18.541 -29.302 50.011 1.00 33.31 ? 207 SER A C 1 ATOM 1603 O O . SER A 1 204 ? 19.171 -30.343 50.197 1.00 31.83 ? 207 SER A O 1 ATOM 1604 C CB . SER A 1 204 ? 16.061 -29.684 49.706 1.00 33.04 ? 207 SER A CB 1 ATOM 1605 O OG . SER A 1 204 ? 16.246 -29.102 48.426 1.00 36.69 ? 207 SER A OG 1 ATOM 1606 N N . THR A 1 205 ? 19.029 -28.264 49.310 1.00 33.57 ? 208 THR A N 1 ATOM 1607 C CA . THR A 1 205 ? 20.319 -28.324 48.606 1.00 35.50 ? 208 THR A CA 1 ATOM 1608 C C . THR A 1 205 ? 21.359 -27.316 49.085 1.00 35.86 ? 208 THR A C 1 ATOM 1609 O O . THR A 1 205 ? 22.550 -27.462 48.776 1.00 37.39 ? 208 THR A O 1 ATOM 1610 C CB . THR A 1 205 ? 20.188 -28.025 47.122 1.00 35.20 ? 208 THR A CB 1 ATOM 1611 O OG1 . THR A 1 205 ? 19.692 -26.692 46.973 1.00 37.54 ? 208 THR A OG1 1 ATOM 1612 C CG2 . THR A 1 205 ? 19.277 -28.976 46.448 1.00 36.40 ? 208 THR A CG2 1 ATOM 1613 N N . LEU A 1 206 ? 20.946 -26.265 49.784 1.00 35.39 ? 209 LEU A N 1 ATOM 1614 C CA . LEU A 1 206 ? 21.918 -25.297 50.233 1.00 35.31 ? 209 LEU A CA 1 ATOM 1615 C C . LEU A 1 206 ? 22.101 -25.351 51.735 1.00 34.60 ? 209 LEU A C 1 ATOM 1616 O O . LEU A 1 206 ? 21.158 -25.539 52.483 1.00 33.53 ? 209 LEU A O 1 ATOM 1617 C CB . LEU A 1 206 ? 21.557 -23.884 49.729 1.00 36.23 ? 209 LEU A CB 1 ATOM 1618 C CG . LEU A 1 206 ? 22.516 -22.741 50.074 1.00 38.40 ? 209 LEU A CG 1 ATOM 1619 C CD1 . LEU A 1 206 ? 23.823 -22.837 49.278 1.00 40.36 ? 209 LEU A CD1 1 ATOM 1620 C CD2 . LEU A 1 206 ? 21.833 -21.408 49.818 1.00 41.30 ? 209 LEU A CD2 1 ATOM 1621 N N . ASN A 1 207 ? 23.348 -25.255 52.171 1.00 35.14 ? 210 ASN A N 1 ATOM 1622 C CA . ASN A 1 207 ? 23.686 -25.198 53.578 1.00 36.35 ? 210 ASN A CA 1 ATOM 1623 C C . ASN A 1 207 ? 24.763 -24.148 53.607 1.00 37.00 ? 210 ASN A C 1 ATOM 1624 O O . ASN A 1 207 ? 25.913 -24.407 53.257 1.00 36.83 ? 210 ASN A O 1 ATOM 1625 C CB . ASN A 1 207 ? 24.217 -26.532 54.116 1.00 35.42 ? 210 ASN A CB 1 ATOM 1626 C CG . ASN A 1 207 ? 24.632 -26.466 55.599 1.00 38.56 ? 210 ASN A CG 1 ATOM 1627 O OD1 . ASN A 1 207 ? 23.841 -26.074 56.480 1.00 40.43 ? 210 ASN A OD1 1 ATOM 1628 N ND2 . ASN A 1 207 ? 25.875 -26.895 55.894 1.00 39.50 ? 210 ASN A ND2 1 ATOM 1629 N N . LYS A 1 208 ? 24.392 -22.943 53.992 1.00 38.53 ? 211 LYS A N 1 ATOM 1630 C CA . LYS A 1 208 ? 25.367 -21.870 53.939 1.00 39.26 ? 211 LYS A CA 1 ATOM 1631 C C . LYS A 1 208 ? 25.390 -21.173 55.261 1.00 39.48 ? 211 LYS A C 1 ATOM 1632 O O . LYS A 1 208 ? 24.371 -20.715 55.724 1.00 39.78 ? 211 LYS A O 1 ATOM 1633 C CB . LYS A 1 208 ? 25.063 -20.900 52.804 1.00 39.66 ? 211 LYS A CB 1 ATOM 1634 C CG . LYS A 1 208 ? 26.229 -19.929 52.512 1.00 41.24 ? 211 LYS A CG 1 ATOM 1635 C CD . LYS A 1 208 ? 25.906 -18.943 51.390 1.00 43.14 ? 211 LYS A CD 1 ATOM 1636 C CE . LYS A 1 208 ? 26.730 -17.652 51.584 1.00 45.80 ? 211 LYS A CE 1 ATOM 1637 N NZ . LYS A 1 208 ? 27.074 -16.972 50.272 1.00 46.50 ? 211 LYS A NZ 1 ATOM 1638 N N . ARG A 1 209 ? 26.557 -21.099 55.877 1.00 40.48 ? 212 ARG A N 1 ATOM 1639 C CA . ARG A 1 209 ? 26.673 -20.326 57.106 1.00 41.67 ? 212 ARG A CA 1 ATOM 1640 C C . ARG A 1 209 ? 27.738 -19.213 57.137 1.00 42.71 ? 212 ARG A C 1 ATOM 1641 O O . ARG A 1 209 ? 28.786 -19.286 56.444 1.00 42.79 ? 212 ARG A O 1 ATOM 1642 C CB . ARG A 1 209 ? 26.846 -21.228 58.314 1.00 40.73 ? 212 ARG A CB 1 ATOM 1643 C CG . ARG A 1 209 ? 27.560 -20.472 59.401 1.00 41.51 ? 212 ARG A CG 1 ATOM 1644 C CD . ARG A 1 209 ? 27.690 -21.279 60.647 1.00 41.15 ? 212 ARG A CD 1 ATOM 1645 N NE . ARG A 1 209 ? 26.487 -22.027 60.925 1.00 40.38 ? 212 ARG A NE 1 ATOM 1646 C CZ . ARG A 1 209 ? 26.244 -22.618 62.095 1.00 42.77 ? 212 ARG A CZ 1 ATOM 1647 N NH1 . ARG A 1 209 ? 27.124 -22.499 63.075 1.00 41.74 ? 212 ARG A NH1 1 ATOM 1648 N NH2 . ARG A 1 209 ? 25.118 -23.302 62.290 1.00 40.83 ? 212 ARG A NH2 1 ATOM 1649 N N . SER A 1 210 ? 27.469 -18.215 57.993 1.00 42.99 ? 213 SER A N 1 ATOM 1650 C CA . SER A 1 210 ? 28.406 -17.134 58.288 1.00 42.72 ? 213 SER A CA 1 ATOM 1651 C C . SER A 1 210 ? 28.595 -16.873 59.791 1.00 42.48 ? 213 SER A C 1 ATOM 1652 O O . SER A 1 210 ? 27.636 -16.913 60.573 1.00 42.20 ? 213 SER A O 1 ATOM 1653 C CB . SER A 1 210 ? 27.923 -15.874 57.607 1.00 43.19 ? 213 SER A CB 1 ATOM 1654 O OG . SER A 1 210 ? 27.637 -16.145 56.239 1.00 44.66 ? 213 SER A OG 1 ATOM 1655 N N . THR A 1 211 ? 29.846 -16.633 60.189 1.00 41.10 ? 214 THR A N 1 ATOM 1656 C CA . THR A 1 211 ? 30.141 -16.013 61.475 1.00 40.80 ? 214 THR A CA 1 ATOM 1657 C C . THR A 1 211 ? 30.569 -14.554 61.140 1.00 39.22 ? 214 THR A C 1 ATOM 1658 O O . THR A 1 211 ? 31.402 -14.347 60.259 1.00 39.57 ? 214 THR A O 1 ATOM 1659 C CB . THR A 1 211 ? 31.263 -16.739 62.223 1.00 41.06 ? 214 THR A CB 1 ATOM 1660 O OG1 . THR A 1 211 ? 32.465 -16.587 61.482 1.00 43.95 ? 214 THR A OG1 1 ATOM 1661 C CG2 . THR A 1 211 ? 30.970 -18.250 62.364 1.00 42.35 ? 214 THR A CG2 1 ATOM 1662 N N . PRO A 1 212 ? 29.965 -13.553 61.791 1.00 37.50 ? 215 PRO A N 1 ATOM 1663 C CA . PRO A 1 212 ? 30.229 -12.141 61.426 1.00 36.79 ? 215 PRO A CA 1 ATOM 1664 C C . PRO A 1 212 ? 31.637 -11.731 61.814 1.00 37.02 ? 215 PRO A C 1 ATOM 1665 O O . PRO A 1 212 ? 32.156 -12.233 62.805 1.00 37.65 ? 215 PRO A O 1 ATOM 1666 C CB . PRO A 1 212 ? 29.214 -11.369 62.257 1.00 36.32 ? 215 PRO A CB 1 ATOM 1667 C CG . PRO A 1 212 ? 28.121 -12.394 62.565 1.00 36.26 ? 215 PRO A CG 1 ATOM 1668 C CD . PRO A 1 212 ? 28.861 -13.680 62.755 1.00 37.91 ? 215 PRO A CD 1 ATOM 1669 N N . GLU A 1 213 ? 32.242 -10.843 61.037 1.00 37.09 ? 216 GLU A N 1 ATOM 1670 C CA . GLU A 1 213 ? 33.601 -10.361 61.287 1.00 37.41 ? 216 GLU A CA 1 ATOM 1671 C C . GLU A 1 213 ? 33.640 -8.918 61.774 1.00 37.33 ? 216 GLU A C 1 ATOM 1672 O O . GLU A 1 213 ? 33.225 -7.989 61.068 1.00 37.10 ? 216 GLU A O 1 ATOM 1673 C CB . GLU A 1 213 ? 34.423 -10.521 60.037 1.00 36.99 ? 216 GLU A CB 1 ATOM 1674 C CG . GLU A 1 213 ? 34.377 -11.954 59.599 1.00 39.20 ? 216 GLU A CG 1 ATOM 1675 C CD . GLU A 1 213 ? 34.627 -12.149 58.149 1.00 40.57 ? 216 GLU A CD 1 ATOM 1676 O OE1 . GLU A 1 213 ? 34.881 -11.162 57.428 1.00 43.62 ? 216 GLU A OE1 1 ATOM 1677 O OE2 . GLU A 1 213 ? 34.586 -13.315 57.728 1.00 43.91 ? 216 GLU A OE2 1 ATOM 1678 N N . ILE A 1 214 ? 34.096 -8.748 63.013 1.00 36.26 ? 217 ILE A N 1 ATOM 1679 C CA . ILE A 1 214 ? 34.298 -7.439 63.572 1.00 35.35 ? 217 ILE A CA 1 ATOM 1680 C C . ILE A 1 214 ? 35.702 -6.990 63.226 1.00 35.92 ? 217 ILE A C 1 ATOM 1681 O O . ILE A 1 214 ? 36.681 -7.670 63.571 1.00 35.04 ? 217 ILE A O 1 ATOM 1682 C CB . ILE A 1 214 ? 34.082 -7.448 65.091 1.00 36.22 ? 217 ILE A CB 1 ATOM 1683 C CG1 . ILE A 1 214 ? 32.639 -7.873 65.392 1.00 33.63 ? 217 ILE A CG1 1 ATOM 1684 C CG2 . ILE A 1 214 ? 34.447 -6.075 65.657 1.00 35.55 ? 217 ILE A CG2 1 ATOM 1685 C CD1 . ILE A 1 214 ? 32.362 -8.296 66.809 1.00 38.29 ? 217 ILE A CD1 1 ATOM 1686 N N . ALA A 1 215 ? 35.802 -5.865 62.520 1.00 35.53 ? 218 ALA A N 1 ATOM 1687 C CA . ALA A 1 215 ? 37.085 -5.400 61.972 1.00 36.34 ? 218 ALA A CA 1 ATOM 1688 C C . ALA A 1 215 ? 36.965 -3.983 61.491 1.00 36.50 ? 218 ALA A C 1 ATOM 1689 O O . ALA A 1 215 ? 35.968 -3.614 60.904 1.00 35.49 ? 218 ALA A O 1 ATOM 1690 C CB . ALA A 1 215 ? 37.575 -6.282 60.807 1.00 35.25 ? 218 ALA A CB 1 ATOM 1691 N N . THR A 1 216 ? 38.040 -3.222 61.715 1.00 38.24 ? 219 THR A N 1 ATOM 1692 C CA . THR A 1 216 ? 38.188 -1.832 61.280 1.00 37.90 ? 219 THR A CA 1 ATOM 1693 C C . THR A 1 216 ? 38.409 -1.687 59.758 1.00 36.94 ? 219 THR A C 1 ATOM 1694 O O . THR A 1 216 ? 39.379 -2.194 59.198 1.00 37.86 ? 219 THR A O 1 ATOM 1695 C CB . THR A 1 216 ? 39.347 -1.188 62.124 1.00 39.70 ? 219 THR A CB 1 ATOM 1696 O OG1 . THR A 1 216 ? 38.797 -0.756 63.378 1.00 42.73 ? 219 THR A OG1 1 ATOM 1697 C CG2 . THR A 1 216 ? 40.051 -0.011 61.402 1.00 39.82 ? 219 THR A CG2 1 ATOM 1698 N N . ARG A 1 217 ? 37.502 -0.974 59.093 1.00 34.49 ? 220 ARG A N 1 ATOM 1699 C CA . ARG A 1 217 ? 37.536 -0.824 57.639 1.00 32.71 ? 220 ARG A CA 1 ATOM 1700 C C . ARG A 1 217 ? 37.372 0.655 57.274 1.00 31.96 ? 220 ARG A C 1 ATOM 1701 O O . ARG A 1 217 ? 36.840 1.407 58.084 1.00 28.97 ? 220 ARG A O 1 ATOM 1702 C CB . ARG A 1 217 ? 36.382 -1.611 57.027 1.00 31.98 ? 220 ARG A CB 1 ATOM 1703 C CG . ARG A 1 217 ? 36.369 -3.078 57.406 1.00 31.06 ? 220 ARG A CG 1 ATOM 1704 C CD . ARG A 1 217 ? 35.182 -3.812 56.791 1.00 29.13 ? 220 ARG A CD 1 ATOM 1705 N NE . ARG A 1 217 ? 34.939 -5.068 57.510 1.00 30.84 ? 220 ARG A NE 1 ATOM 1706 C CZ . ARG A 1 217 ? 34.199 -5.169 58.613 1.00 28.56 ? 220 ARG A CZ 1 ATOM 1707 N NH1 . ARG A 1 217 ? 33.619 -4.089 59.137 1.00 31.99 ? 220 ARG A NH1 1 ATOM 1708 N NH2 . ARG A 1 217 ? 34.062 -6.349 59.199 1.00 28.80 ? 220 ARG A NH2 1 ATOM 1709 N N . PRO A 1 218 ? 37.811 1.060 56.060 1.00 31.94 ? 221 PRO A N 1 ATOM 1710 C CA . PRO A 1 218 ? 37.603 2.454 55.711 1.00 32.03 ? 221 PRO A CA 1 ATOM 1711 C C . PRO A 1 218 ? 36.118 2.722 55.590 1.00 32.50 ? 221 PRO A C 1 ATOM 1712 O O . PRO A 1 218 ? 35.343 1.823 55.206 1.00 30.76 ? 221 PRO A O 1 ATOM 1713 C CB . PRO A 1 218 ? 38.276 2.590 54.344 1.00 32.39 ? 221 PRO A CB 1 ATOM 1714 C CG . PRO A 1 218 ? 38.556 1.245 53.883 1.00 32.38 ? 221 PRO A CG 1 ATOM 1715 C CD . PRO A 1 218 ? 38.666 0.377 55.068 1.00 32.12 ? 221 PRO A CD 1 ATOM 1716 N N . LYS A 1 219 ? 35.707 3.931 55.945 1.00 32.44 ? 222 LYS A N 1 ATOM 1717 C CA . LYS A 1 219 ? 34.287 4.245 55.841 1.00 32.12 ? 222 LYS A CA 1 ATOM 1718 C C . LYS A 1 219 ? 33.840 4.306 54.380 1.00 31.16 ? 222 LYS A C 1 ATOM 1719 O O . LYS A 1 219 ? 34.556 4.868 53.529 1.00 30.24 ? 222 LYS A O 1 ATOM 1720 C CB . LYS A 1 219 ? 33.989 5.548 56.541 1.00 32.61 ? 222 LYS A CB 1 ATOM 1721 C CG . LYS A 1 219 ? 34.045 5.414 58.035 1.00 34.61 ? 222 LYS A CG 1 ATOM 1722 C CD . LYS A 1 219 ? 33.534 6.733 58.657 1.00 36.91 ? 222 LYS A CD 1 ATOM 1723 C CE . LYS A 1 219 ? 34.042 6.891 60.047 1.00 41.22 ? 222 LYS A CE 1 ATOM 1724 N NZ . LYS A 1 219 ? 33.426 5.926 60.961 1.00 43.92 ? 222 LYS A NZ 1 ATOM 1725 N N . VAL A 1 220 ? 32.693 3.677 54.093 1.00 28.71 ? 223 VAL A N 1 ATOM 1726 C CA . VAL A 1 220 ? 32.036 3.806 52.790 1.00 28.73 ? 223 VAL A CA 1 ATOM 1727 C C . VAL A 1 220 ? 30.607 4.261 53.119 1.00 28.55 ? 223 VAL A C 1 ATOM 1728 O O . VAL A 1 220 ? 29.918 3.630 53.933 1.00 27.32 ? 223 VAL A O 1 ATOM 1729 C CB . VAL A 1 220 ? 32.022 2.472 51.992 1.00 28.64 ? 223 VAL A CB 1 ATOM 1730 C CG1 . VAL A 1 220 ? 31.247 2.624 50.654 1.00 27.95 ? 223 VAL A CG1 1 ATOM 1731 C CG2 . VAL A 1 220 ? 33.490 1.955 51.741 1.00 28.77 ? 223 VAL A CG2 1 ATOM 1732 N N . ASN A 1 221 ? 30.190 5.384 52.527 1.00 28.71 ? 224 ASN A N 1 ATOM 1733 C CA . ASN A 1 221 ? 28.905 6.038 52.883 1.00 28.87 ? 224 ASN A CA 1 ATOM 1734 C C . ASN A 1 221 ? 28.822 6.282 54.347 1.00 28.46 ? 224 ASN A C 1 ATOM 1735 O O . ASN A 1 221 ? 27.746 6.168 54.929 1.00 29.24 ? 224 ASN A O 1 ATOM 1736 C CB . ASN A 1 221 ? 27.698 5.192 52.482 1.00 29.07 ? 224 ASN A CB 1 ATOM 1737 C CG . ASN A 1 221 ? 27.590 5.025 50.997 1.00 32.16 ? 224 ASN A CG 1 ATOM 1738 O OD1 . ASN A 1 221 ? 28.080 5.860 50.249 1.00 34.21 ? 224 ASN A OD1 1 ATOM 1739 N ND2 . ASN A 1 221 ? 26.979 3.921 50.554 1.00 32.20 ? 224 ASN A ND2 1 ATOM 1740 N N . GLY A 1 222 ? 29.956 6.600 54.963 1.00 28.26 ? 225 GLY A N 1 ATOM 1741 C CA . GLY A 1 222 ? 29.999 6.828 56.405 1.00 26.97 ? 225 GLY A CA 1 ATOM 1742 C C . GLY A 1 222 ? 30.123 5.638 57.334 1.00 27.03 ? 225 GLY A C 1 ATOM 1743 O O . GLY A 1 222 ? 30.156 5.817 58.558 1.00 26.21 ? 225 GLY A O 1 ATOM 1744 N N . GLN A 1 223 ? 30.205 4.418 56.789 1.00 26.55 ? 226 GLN A N 1 ATOM 1745 C CA . GLN A 1 223 ? 30.144 3.225 57.629 1.00 26.06 ? 226 GLN A CA 1 ATOM 1746 C C . GLN A 1 223 ? 31.386 2.373 57.485 1.00 25.70 ? 226 GLN A C 1 ATOM 1747 O O . GLN A 1 223 ? 31.800 2.063 56.367 1.00 25.02 ? 226 GLN A O 1 ATOM 1748 C CB . GLN A 1 223 ? 28.908 2.352 57.264 1.00 26.43 ? 226 GLN A CB 1 ATOM 1749 C CG . GLN A 1 223 ? 27.517 3.038 57.464 1.00 29.24 ? 226 GLN A CG 1 ATOM 1750 C CD . GLN A 1 223 ? 27.323 3.581 58.881 1.00 32.61 ? 226 GLN A CD 1 ATOM 1751 O OE1 . GLN A 1 223 ? 27.683 2.935 59.854 1.00 32.88 ? 226 GLN A OE1 1 ATOM 1752 N NE2 . GLN A 1 223 ? 26.775 4.788 58.991 1.00 34.54 ? 226 GLN A NE2 1 ATOM 1753 N N . GLY A 1 224 ? 31.957 1.970 58.617 1.00 26.38 ? 227 GLY A N 1 ATOM 1754 C CA . GLY A 1 224 ? 33.040 0.983 58.638 1.00 26.62 ? 227 GLY A CA 1 ATOM 1755 C C . GLY A 1 224 ? 32.541 -0.468 58.608 1.00 26.36 ? 227 GLY A C 1 ATOM 1756 O O . GLY A 1 224 ? 33.287 -1.373 58.223 1.00 28.22 ? 227 GLY A O 1 ATOM 1757 N N . GLY A 1 225 ? 31.287 -0.702 58.988 1.00 26.13 ? 228 GLY A N 1 ATOM 1758 C CA . GLY A 1 225 ? 30.693 -2.052 58.941 1.00 24.75 ? 228 GLY A CA 1 ATOM 1759 C C . GLY A 1 225 ? 30.329 -2.452 57.517 1.00 24.25 ? 228 GLY A C 1 ATOM 1760 O O . GLY A 1 225 ? 30.462 -1.647 56.597 1.00 24.80 ? 228 GLY A O 1 ATOM 1761 N N . ARG A 1 226 ? 29.926 -3.701 57.307 1.00 22.64 ? 229 ARG A N 1 ATOM 1762 C CA . ARG A 1 226 ? 29.618 -4.183 55.958 1.00 21.88 ? 229 ARG A CA 1 ATOM 1763 C C . ARG A 1 226 ? 28.475 -5.175 56.067 1.00 21.96 ? 229 ARG A C 1 ATOM 1764 O O . ARG A 1 226 ? 28.348 -5.883 57.070 1.00 20.96 ? 229 ARG A O 1 ATOM 1765 C CB . ARG A 1 226 ? 30.825 -4.889 55.275 1.00 22.09 ? 229 ARG A CB 1 ATOM 1766 C CG . ARG A 1 226 ? 32.130 -4.006 55.126 1.00 20.65 ? 229 ARG A CG 1 ATOM 1767 C CD . ARG A 1 226 ? 32.047 -3.005 53.965 1.00 22.07 ? 229 ARG A CD 1 ATOM 1768 N NE . ARG A 1 226 ? 33.328 -2.310 53.753 1.00 24.26 ? 229 ARG A NE 1 ATOM 1769 C CZ . ARG A 1 226 ? 33.644 -1.090 54.177 1.00 25.38 ? 229 ARG A CZ 1 ATOM 1770 N NH1 . ARG A 1 226 ? 32.787 -0.345 54.895 1.00 23.49 ? 229 ARG A NH1 1 ATOM 1771 N NH2 . ARG A 1 226 ? 34.863 -0.614 53.881 1.00 23.64 ? 229 ARG A NH2 1 ATOM 1772 N N . MET A 1 227 ? 27.654 -5.209 55.024 1.00 20.91 ? 230 MET A N 1 ATOM 1773 C CA . MET A 1 227 ? 26.663 -6.244 54.909 1.00 20.89 ? 230 MET A CA 1 ATOM 1774 C C . MET A 1 227 ? 26.968 -7.082 53.679 1.00 20.10 ? 230 MET A C 1 ATOM 1775 O O . MET A 1 227 ? 27.028 -6.585 52.570 1.00 20.38 ? 230 MET A O 1 ATOM 1776 C CB . MET A 1 227 ? 25.257 -5.637 54.870 1.00 20.60 ? 230 MET A CB 1 ATOM 1777 C CG . MET A 1 227 ? 24.775 -5.272 56.267 1.00 19.44 ? 230 MET A CG 1 ATOM 1778 S SD . MET A 1 227 ? 23.231 -4.353 56.154 1.00 22.95 ? 230 MET A SD 1 ATOM 1779 C CE . MET A 1 227 ? 23.230 -3.774 57.856 1.00 19.56 ? 230 MET A CE 1 ATOM 1780 N N . GLU A 1 228 ? 27.162 -8.366 53.919 1.00 20.65 ? 231 GLU A N 1 ATOM 1781 C CA . GLU A 1 228 ? 27.455 -9.312 52.867 1.00 20.48 ? 231 GLU A CA 1 ATOM 1782 C C . GLU A 1 228 ? 26.176 -10.052 52.510 1.00 19.78 ? 231 GLU A C 1 ATOM 1783 O O . GLU A 1 228 ? 25.614 -10.784 53.344 1.00 20.63 ? 231 GLU A O 1 ATOM 1784 C CB . GLU A 1 228 ? 28.523 -10.301 53.361 1.00 20.11 ? 231 GLU A CB 1 ATOM 1785 C CG . GLU A 1 228 ? 28.808 -11.438 52.376 1.00 21.31 ? 231 GLU A CG 1 ATOM 1786 C CD . GLU A 1 228 ? 29.764 -12.474 52.952 1.00 28.20 ? 231 GLU A CD 1 ATOM 1787 O OE1 . GLU A 1 228 ? 30.397 -12.167 53.993 1.00 28.47 ? 231 GLU A OE1 1 ATOM 1788 O OE2 . GLU A 1 228 ? 29.863 -13.594 52.377 1.00 27.27 ? 231 GLU A OE2 1 ATOM 1789 N N . PHE A 1 229 ? 25.730 -9.876 51.268 1.00 19.66 ? 232 PHE A N 1 ATOM 1790 C CA . PHE A 1 229 ? 24.464 -10.482 50.837 1.00 20.19 ? 232 PHE A CA 1 ATOM 1791 C C . PHE A 1 229 ? 24.740 -11.711 49.990 1.00 20.60 ? 232 PHE A C 1 ATOM 1792 O O . PHE A 1 229 ? 25.771 -11.800 49.283 1.00 20.17 ? 232 PHE A O 1 ATOM 1793 C CB . PHE A 1 229 ? 23.618 -9.477 50.054 1.00 19.25 ? 232 PHE A CB 1 ATOM 1794 C CG . PHE A 1 229 ? 23.143 -8.358 50.883 1.00 19.38 ? 232 PHE A CG 1 ATOM 1795 C CD1 . PHE A 1 229 ? 22.010 -8.531 51.709 1.00 20.16 ? 232 PHE A CD1 1 ATOM 1796 C CD2 . PHE A 1 229 ? 23.806 -7.114 50.864 1.00 21.28 ? 232 PHE A CD2 1 ATOM 1797 C CE1 . PHE A 1 229 ? 21.547 -7.487 52.521 1.00 19.46 ? 232 PHE A CE1 1 ATOM 1798 C CE2 . PHE A 1 229 ? 23.337 -6.038 51.670 1.00 20.76 ? 232 PHE A CE2 1 ATOM 1799 C CZ . PHE A 1 229 ? 22.221 -6.217 52.490 1.00 17.76 ? 232 PHE A CZ 1 ATOM 1800 N N . SER A 1 230 ? 23.815 -12.650 50.079 1.00 21.12 ? 233 SER A N 1 ATOM 1801 C CA . SER A 1 230 ? 23.856 -13.885 49.324 1.00 21.12 ? 233 SER A CA 1 ATOM 1802 C C . SER A 1 230 ? 22.459 -14.137 48.808 1.00 21.35 ? 233 SER A C 1 ATOM 1803 O O . SER A 1 230 ? 21.518 -13.518 49.267 1.00 20.15 ? 233 SER A O 1 ATOM 1804 C CB . SER A 1 230 ? 24.306 -15.061 50.209 1.00 20.38 ? 233 SER A CB 1 ATOM 1805 O OG . SER A 1 230 ? 25.616 -14.847 50.723 1.00 22.16 ? 233 SER A OG 1 ATOM 1806 N N . TRP A 1 231 ? 22.320 -15.059 47.857 1.00 20.86 ? 234 TRP A N 1 ATOM 1807 C CA . TRP A 1 231 ? 21.015 -15.357 47.306 1.00 20.63 ? 234 TRP A CA 1 ATOM 1808 C C . TRP A 1 231 ? 20.928 -16.837 46.920 1.00 21.95 ? 234 TRP A C 1 ATOM 1809 O O . TRP A 1 231 ? 21.958 -17.544 46.805 1.00 20.01 ? 234 TRP A O 1 ATOM 1810 C CB . TRP A 1 231 ? 20.723 -14.447 46.111 1.00 19.95 ? 234 TRP A CB 1 ATOM 1811 C CG . TRP A 1 231 ? 21.642 -14.671 44.951 1.00 22.39 ? 234 TRP A CG 1 ATOM 1812 C CD1 . TRP A 1 231 ? 22.934 -14.147 44.770 1.00 20.79 ? 234 TRP A CD1 1 ATOM 1813 C CD2 . TRP A 1 231 ? 21.382 -15.485 43.806 1.00 24.22 ? 234 TRP A CD2 1 ATOM 1814 N NE1 . TRP A 1 231 ? 23.440 -14.594 43.592 1.00 23.21 ? 234 TRP A NE1 1 ATOM 1815 C CE2 . TRP A 1 231 ? 22.521 -15.407 42.972 1.00 24.60 ? 234 TRP A CE2 1 ATOM 1816 C CE3 . TRP A 1 231 ? 20.287 -16.268 43.392 1.00 24.76 ? 234 TRP A CE3 1 ATOM 1817 C CZ2 . TRP A 1 231 ? 22.603 -16.103 41.750 1.00 27.11 ? 234 TRP A CZ2 1 ATOM 1818 C CZ3 . TRP A 1 231 ? 20.374 -16.958 42.197 1.00 28.52 ? 234 TRP A CZ3 1 ATOM 1819 C CH2 . TRP A 1 231 ? 21.528 -16.868 41.383 1.00 24.09 ? 234 TRP A CH2 1 ATOM 1820 N N . THR A 1 232 ? 19.689 -17.278 46.722 1.00 22.72 ? 235 THR A N 1 ATOM 1821 C CA . THR A 1 232 ? 19.401 -18.611 46.251 1.00 24.12 ? 235 THR A CA 1 ATOM 1822 C C . THR A 1 232 ? 18.109 -18.541 45.431 1.00 25.06 ? 235 THR A C 1 ATOM 1823 O O . THR A 1 232 ? 17.254 -17.633 45.618 1.00 23.41 ? 235 THR A O 1 ATOM 1824 C CB . THR A 1 232 ? 19.299 -19.646 47.418 1.00 25.31 ? 235 THR A CB 1 ATOM 1825 O OG1 . THR A 1 232 ? 19.362 -20.987 46.886 1.00 27.30 ? 235 THR A OG1 1 ATOM 1826 C CG2 . THR A 1 232 ? 17.944 -19.530 48.202 1.00 24.69 ? 235 THR A CG2 1 ATOM 1827 N N . LEU A 1 233 ? 17.994 -19.470 44.484 1.00 26.30 ? 236 LEU A N 1 ATOM 1828 C CA . LEU A 1 233 ? 16.732 -19.735 43.821 1.00 27.40 ? 236 LEU A CA 1 ATOM 1829 C C . LEU A 1 233 ? 16.084 -20.924 44.562 1.00 28.33 ? 236 LEU A C 1 ATOM 1830 O O . LEU A 1 233 ? 16.583 -22.066 44.506 1.00 27.50 ? 236 LEU A O 1 ATOM 1831 C CB . LEU A 1 233 ? 16.986 -19.997 42.325 1.00 28.28 ? 236 LEU A CB 1 ATOM 1832 C CG . LEU A 1 233 ? 15.925 -19.806 41.232 1.00 31.34 ? 236 LEU A CG 1 ATOM 1833 C CD1 . LEU A 1 233 ? 15.240 -18.434 41.339 1.00 31.27 ? 236 LEU A CD1 1 ATOM 1834 C CD2 . LEU A 1 233 ? 16.558 -19.919 39.858 1.00 29.82 ? 236 LEU A CD2 1 ATOM 1835 N N . LEU A 1 234 ? 15.014 -20.641 45.319 1.00 26.95 ? 237 LEU A N 1 ATOM 1836 C CA . LEU A 1 234 ? 14.316 -21.656 46.094 1.00 26.02 ? 237 LEU A CA 1 ATOM 1837 C C . LEU A 1 234 ? 13.365 -22.413 45.182 1.00 27.04 ? 237 LEU A C 1 ATOM 1838 O O . LEU A 1 234 ? 12.462 -21.828 44.558 1.00 26.00 ? 237 LEU A O 1 ATOM 1839 C CB . LEU A 1 234 ? 13.570 -21.038 47.303 1.00 25.51 ? 237 LEU A CB 1 ATOM 1840 C CG . LEU A 1 234 ? 12.825 -21.994 48.251 1.00 26.92 ? 237 LEU A CG 1 ATOM 1841 C CD1 . LEU A 1 234 ? 13.791 -22.979 48.990 1.00 28.60 ? 237 LEU A CD1 1 ATOM 1842 C CD2 . LEU A 1 234 ? 12.003 -21.223 49.273 1.00 24.73 ? 237 LEU A CD2 1 ATOM 1843 N N . ASP A 1 235 ? 13.554 -23.731 45.087 1.00 27.41 ? 238 ASP A N 1 ATOM 1844 C CA . ASP A 1 235 ? 12.699 -24.511 44.193 1.00 28.41 ? 238 ASP A CA 1 ATOM 1845 C C . ASP A 1 235 ? 11.254 -24.569 44.698 1.00 27.01 ? 238 ASP A C 1 ATOM 1846 O O . ASP A 1 235 ? 10.983 -24.430 45.883 1.00 26.18 ? 238 ASP A O 1 ATOM 1847 C CB . ASP A 1 235 ? 13.232 -25.942 44.006 1.00 28.66 ? 238 ASP A CB 1 ATOM 1848 C CG . ASP A 1 235 ? 14.450 -26.015 43.086 1.00 33.26 ? 238 ASP A CG 1 ATOM 1849 O OD1 . ASP A 1 235 ? 14.735 -25.075 42.299 1.00 35.30 ? 238 ASP A OD1 1 ATOM 1850 O OD2 . ASP A 1 235 ? 15.119 -27.065 43.144 1.00 37.68 ? 238 ASP A OD2 1 ATOM 1851 N N . MET A 1 236 ? 10.323 -24.781 43.786 1.00 27.35 ? 239 MET A N 1 ATOM 1852 C CA . MET A 1 236 ? 8.931 -25.101 44.187 1.00 28.04 ? 239 MET A CA 1 ATOM 1853 C C . MET A 1 236 ? 8.888 -26.214 45.217 1.00 27.83 ? 239 MET A C 1 ATOM 1854 O O . MET A 1 236 ? 9.566 -27.237 45.052 1.00 28.94 ? 239 MET A O 1 ATOM 1855 C CB . MET A 1 236 ? 8.105 -25.507 42.967 1.00 28.43 ? 239 MET A CB 1 ATOM 1856 C CG . MET A 1 236 ? 8.070 -24.447 41.888 1.00 32.50 ? 239 MET A CG 1 ATOM 1857 S SD . MET A 1 236 ? 7.244 -24.957 40.368 1.00 43.47 ? 239 MET A SD 1 ATOM 1858 C CE . MET A 1 236 ? 8.364 -26.218 39.744 1.00 44.23 ? 239 MET A CE 1 ATOM 1859 N N . TRP A 1 237 ? 8.103 -25.992 46.268 1.00 27.23 ? 240 TRP A N 1 ATOM 1860 C CA . TRP A 1 237 ? 7.812 -26.961 47.335 1.00 27.93 ? 240 TRP A CA 1 ATOM 1861 C C . TRP A 1 237 ? 9.004 -27.199 48.268 1.00 27.26 ? 240 TRP A C 1 ATOM 1862 O O . TRP A 1 237 ? 8.881 -27.917 49.258 1.00 26.80 ? 240 TRP A O 1 ATOM 1863 C CB . TRP A 1 237 ? 7.205 -28.278 46.784 1.00 28.97 ? 240 TRP A CB 1 ATOM 1864 C CG . TRP A 1 237 ? 6.304 -28.049 45.590 1.00 30.16 ? 240 TRP A CG 1 ATOM 1865 C CD1 . TRP A 1 237 ? 6.540 -28.442 44.305 1.00 32.81 ? 240 TRP A CD1 1 ATOM 1866 C CD2 . TRP A 1 237 ? 5.062 -27.321 45.565 1.00 32.66 ? 240 TRP A CD2 1 ATOM 1867 N NE1 . TRP A 1 237 ? 5.512 -28.033 43.486 1.00 32.91 ? 240 TRP A NE1 1 ATOM 1868 C CE2 . TRP A 1 237 ? 4.594 -27.341 44.232 1.00 32.62 ? 240 TRP A CE2 1 ATOM 1869 C CE3 . TRP A 1 237 ? 4.296 -26.668 46.542 1.00 32.87 ? 240 TRP A CE3 1 ATOM 1870 C CZ2 . TRP A 1 237 ? 3.414 -26.715 43.842 1.00 32.46 ? 240 TRP A CZ2 1 ATOM 1871 C CZ3 . TRP A 1 237 ? 3.105 -26.057 46.160 1.00 34.16 ? 240 TRP A CZ3 1 ATOM 1872 C CH2 . TRP A 1 237 ? 2.676 -26.087 44.817 1.00 35.48 ? 240 TRP A CH2 1 ATOM 1873 N N . ASP A 1 238 ? 10.125 -26.529 47.993 1.00 26.70 ? 241 ASP A N 1 ATOM 1874 C CA . ASP A 1 238 ? 11.249 -26.549 48.917 1.00 26.58 ? 241 ASP A CA 1 ATOM 1875 C C . ASP A 1 238 ? 11.069 -25.468 49.981 1.00 27.05 ? 241 ASP A C 1 ATOM 1876 O O . ASP A 1 238 ? 10.366 -24.453 49.756 1.00 27.24 ? 241 ASP A O 1 ATOM 1877 C CB . ASP A 1 238 ? 12.602 -26.428 48.192 1.00 24.80 ? 241 ASP A CB 1 ATOM 1878 C CG . ASP A 1 238 ? 13.783 -26.932 49.056 1.00 26.08 ? 241 ASP A CG 1 ATOM 1879 O OD1 . ASP A 1 238 ? 13.551 -27.600 50.101 1.00 26.39 ? 241 ASP A OD1 1 ATOM 1880 O OD2 . ASP A 1 238 ? 14.948 -26.659 48.698 1.00 26.70 ? 241 ASP A OD2 1 ATOM 1881 N N . THR A 1 239 ? 11.698 -25.706 51.131 1.00 26.98 ? 242 THR A N 1 ATOM 1882 C CA . THR A 1 239 ? 11.665 -24.838 52.308 1.00 26.89 ? 242 THR A CA 1 ATOM 1883 C C . THR A 1 239 ? 13.042 -24.199 52.536 1.00 26.39 ? 242 THR A C 1 ATOM 1884 O O . THR A 1 239 ? 14.093 -24.861 52.391 1.00 23.92 ? 242 THR A O 1 ATOM 1885 C CB . THR A 1 239 ? 11.211 -25.634 53.532 1.00 27.52 ? 242 THR A CB 1 ATOM 1886 O OG1 . THR A 1 239 ? 9.851 -26.056 53.333 1.00 30.57 ? 242 THR A OG1 1 ATOM 1887 C CG2 . THR A 1 239 ? 11.267 -24.786 54.803 1.00 28.78 ? 242 THR A CG2 1 ATOM 1888 N N . ILE A 1 240 ? 13.050 -22.887 52.821 1.00 25.42 ? 243 ILE A N 1 ATOM 1889 C CA . ILE A 1 240 ? 14.296 -22.240 53.272 1.00 24.44 ? 243 ILE A CA 1 ATOM 1890 C C . ILE A 1 240 ? 14.183 -21.995 54.780 1.00 25.12 ? 243 ILE A C 1 ATOM 1891 O O . ILE A 1 240 ? 13.130 -21.572 55.264 1.00 26.12 ? 243 ILE A O 1 ATOM 1892 C CB . ILE A 1 240 ? 14.588 -20.926 52.483 1.00 24.25 ? 243 ILE A CB 1 ATOM 1893 C CG1 . ILE A 1 240 ? 15.957 -20.346 52.848 1.00 21.74 ? 243 ILE A CG1 1 ATOM 1894 C CG2 . ILE A 1 240 ? 13.436 -19.872 52.697 1.00 20.17 ? 243 ILE A CG2 1 ATOM 1895 C CD1 . ILE A 1 240 ? 16.516 -19.381 51.810 1.00 26.29 ? 243 ILE A CD1 1 ATOM 1896 N N . ASN A 1 241 ? 15.233 -22.282 55.537 1.00 25.58 ? 244 ASN A N 1 ATOM 1897 C CA . ASN A 1 241 ? 15.218 -22.023 56.991 1.00 26.38 ? 244 ASN A CA 1 ATOM 1898 C C . ASN A 1 241 ? 16.332 -21.043 57.365 1.00 26.38 ? 244 ASN A C 1 ATOM 1899 O O . ASN A 1 241 ? 17.505 -21.278 56.998 1.00 25.85 ? 244 ASN A O 1 ATOM 1900 C CB . ASN A 1 241 ? 15.421 -23.331 57.797 1.00 28.21 ? 244 ASN A CB 1 ATOM 1901 C CG . ASN A 1 241 ? 14.216 -24.287 57.717 1.00 30.12 ? 244 ASN A CG 1 ATOM 1902 O OD1 . ASN A 1 241 ? 13.126 -24.009 58.231 1.00 37.88 ? 244 ASN A OD1 1 ATOM 1903 N ND2 . ASN A 1 241 ? 14.418 -25.403 57.104 1.00 32.05 ? 244 ASN A ND2 1 ATOM 1904 N N . PHE A 1 242 ? 15.996 -20.001 58.131 1.00 24.74 ? 245 PHE A N 1 ATOM 1905 C CA . PHE A 1 242 ? 17.007 -19.057 58.605 1.00 25.37 ? 245 PHE A CA 1 ATOM 1906 C C . PHE A 1 242 ? 17.179 -19.321 60.078 1.00 26.39 ? 245 PHE A C 1 ATOM 1907 O O . PHE A 1 242 ? 16.210 -19.585 60.774 1.00 26.09 ? 245 PHE A O 1 ATOM 1908 C CB . PHE A 1 242 ? 16.568 -17.586 58.388 1.00 24.47 ? 245 PHE A CB 1 ATOM 1909 C CG . PHE A 1 242 ? 16.538 -17.192 56.942 1.00 25.43 ? 245 PHE A CG 1 ATOM 1910 C CD1 . PHE A 1 242 ? 17.708 -16.772 56.293 1.00 25.12 ? 245 PHE A CD1 1 ATOM 1911 C CD2 . PHE A 1 242 ? 15.371 -17.291 56.213 1.00 24.04 ? 245 PHE A CD2 1 ATOM 1912 C CE1 . PHE A 1 242 ? 17.689 -16.433 54.926 1.00 23.23 ? 245 PHE A CE1 1 ATOM 1913 C CE2 . PHE A 1 242 ? 15.334 -16.952 54.862 1.00 22.92 ? 245 PHE A CE2 1 ATOM 1914 C CZ . PHE A 1 242 ? 16.505 -16.533 54.211 1.00 23.40 ? 245 PHE A CZ 1 ATOM 1915 N N . GLU A 1 243 ? 18.408 -19.227 60.562 1.00 27.09 ? 246 GLU A N 1 ATOM 1916 C CA . GLU A 1 243 ? 18.625 -19.381 61.983 1.00 29.71 ? 246 GLU A CA 1 ATOM 1917 C C . GLU A 1 243 ? 19.788 -18.494 62.420 1.00 29.23 ? 246 GLU A C 1 ATOM 1918 O O . GLU A 1 243 ? 20.843 -18.547 61.803 1.00 30.48 ? 246 GLU A O 1 ATOM 1919 C CB . GLU A 1 243 ? 18.929 -20.858 62.262 1.00 30.23 ? 246 GLU A CB 1 ATOM 1920 C CG . GLU A 1 243 ? 18.940 -21.243 63.726 1.00 34.89 ? 246 GLU A CG 1 ATOM 1921 C CD . GLU A 1 243 ? 19.545 -22.631 63.906 1.00 41.67 ? 246 GLU A CD 1 ATOM 1922 O OE1 . GLU A 1 243 ? 18.933 -23.600 63.411 1.00 42.35 ? 246 GLU A OE1 1 ATOM 1923 O OE2 . GLU A 1 243 ? 20.647 -22.742 64.509 1.00 45.53 ? 246 GLU A OE2 1 ATOM 1924 N N . SER A 1 244 ? 19.611 -17.706 63.478 1.00 30.16 ? 247 SER A N 1 ATOM 1925 C CA . SER A 1 244 ? 20.677 -16.773 63.860 1.00 30.80 ? 247 SER A CA 1 ATOM 1926 C C . SER A 1 244 ? 20.685 -16.339 65.320 1.00 30.32 ? 247 SER A C 1 ATOM 1927 O O . SER A 1 244 ? 19.653 -16.060 65.907 1.00 30.90 ? 247 SER A O 1 ATOM 1928 C CB . SER A 1 244 ? 20.610 -15.504 62.979 1.00 30.70 ? 247 SER A CB 1 ATOM 1929 O OG . SER A 1 244 ? 21.607 -14.563 63.376 1.00 30.28 ? 247 SER A OG 1 ATOM 1930 N N . THR A 1 245 ? 21.890 -16.266 65.892 1.00 31.64 ? 248 THR A N 1 ATOM 1931 C CA . THR A 1 245 ? 22.090 -15.669 67.223 1.00 31.19 ? 248 THR A CA 1 ATOM 1932 C C . THR A 1 245 ? 22.461 -14.194 67.120 1.00 30.97 ? 248 THR A C 1 ATOM 1933 O O . THR A 1 245 ? 22.716 -13.505 68.128 1.00 31.38 ? 248 THR A O 1 ATOM 1934 C CB . THR A 1 245 ? 23.171 -16.431 68.005 1.00 31.78 ? 248 THR A CB 1 ATOM 1935 O OG1 . THR A 1 245 ? 24.322 -16.615 67.180 1.00 31.95 ? 248 THR A OG1 1 ATOM 1936 C CG2 . THR A 1 245 ? 22.646 -17.828 68.370 1.00 33.39 ? 248 THR A CG2 1 ATOM 1937 N N . GLY A 1 246 ? 22.482 -13.693 65.892 1.00 29.43 ? 249 GLY A N 1 ATOM 1938 C CA . GLY A 1 246 ? 22.749 -12.271 65.683 1.00 27.21 ? 249 GLY A CA 1 ATOM 1939 C C . GLY A 1 246 ? 23.338 -12.035 64.321 1.00 25.44 ? 249 GLY A C 1 ATOM 1940 O O . GLY A 1 246 ? 23.941 -12.936 63.729 1.00 23.90 ? 249 GLY A O 1 ATOM 1941 N N . ASN A 1 247 ? 23.224 -10.782 63.872 1.00 24.74 ? 250 ASN A N 1 ATOM 1942 C CA . ASN A 1 247 ? 23.849 -10.290 62.618 1.00 23.32 ? 250 ASN A CA 1 ATOM 1943 C C . ASN A 1 247 ? 23.118 -10.663 61.336 1.00 22.44 ? 250 ASN A C 1 ATOM 1944 O O . ASN A 1 247 ? 23.560 -10.348 60.238 1.00 22.16 ? 250 ASN A O 1 ATOM 1945 C CB . ASN A 1 247 ? 25.356 -10.595 62.529 1.00 23.28 ? 250 ASN A CB 1 ATOM 1946 C CG . ASN A 1 247 ? 26.107 -10.158 63.790 1.00 25.19 ? 250 ASN A CG 1 ATOM 1947 O OD1 . ASN A 1 247 ? 25.826 -10.657 64.894 1.00 25.04 ? 250 ASN A OD1 1 ATOM 1948 N ND2 . ASN A 1 247 ? 27.057 -9.222 63.637 1.00 23.48 ? 250 ASN A ND2 1 ATOM 1949 N N . LEU A 1 248 ? 21.975 -11.312 61.486 1.00 22.59 ? 251 LEU A N 1 ATOM 1950 C CA . LEU A 1 248 ? 21.122 -11.651 60.345 1.00 20.61 ? 251 LEU A CA 1 ATOM 1951 C C . LEU A 1 248 ? 20.397 -10.427 59.767 1.00 20.70 ? 251 LEU A C 1 ATOM 1952 O O . LEU A 1 248 ? 19.731 -9.677 60.496 1.00 20.92 ? 251 LEU A O 1 ATOM 1953 C CB . LEU A 1 248 ? 20.098 -12.751 60.764 1.00 20.59 ? 251 LEU A CB 1 ATOM 1954 C CG . LEU A 1 248 ? 18.945 -12.985 59.767 1.00 21.07 ? 251 LEU A CG 1 ATOM 1955 C CD1 . LEU A 1 248 ? 19.464 -13.600 58.445 1.00 20.21 ? 251 LEU A CD1 1 ATOM 1956 C CD2 . LEU A 1 248 ? 17.887 -13.898 60.391 1.00 23.49 ? 251 LEU A CD2 1 ATOM 1957 N N . ILE A 1 249 ? 20.520 -10.262 58.442 1.00 20.08 ? 252 ILE A N 1 ATOM 1958 C CA . ILE A 1 249 ? 19.700 -9.364 57.660 1.00 19.98 ? 252 ILE A CA 1 ATOM 1959 C C . ILE A 1 249 ? 18.715 -10.239 56.876 1.00 19.72 ? 252 ILE A C 1 ATOM 1960 O O . ILE A 1 249 ? 19.080 -10.870 55.891 1.00 20.31 ? 252 ILE A O 1 ATOM 1961 C CB . ILE A 1 249 ? 20.573 -8.462 56.711 1.00 19.43 ? 252 ILE A CB 1 ATOM 1962 C CG1 . ILE A 1 249 ? 21.727 -7.811 57.498 1.00 20.49 ? 252 ILE A CG1 1 ATOM 1963 C CG2 . ILE A 1 249 ? 19.673 -7.431 55.988 1.00 18.96 ? 252 ILE A CG2 1 ATOM 1964 C CD1 . ILE A 1 249 ? 21.310 -6.826 58.626 1.00 17.37 ? 252 ILE A CD1 1 ATOM 1965 N N . ALA A 1 250 ? 17.470 -10.300 57.350 1.00 18.27 ? 253 ALA A N 1 ATOM 1966 C CA . ALA A 1 250 ? 16.479 -11.228 56.780 1.00 18.52 ? 253 ALA A CA 1 ATOM 1967 C C . ALA A 1 250 ? 15.748 -10.636 55.584 1.00 17.61 ? 253 ALA A C 1 ATOM 1968 O O . ALA A 1 250 ? 15.493 -9.405 55.558 1.00 17.58 ? 253 ALA A O 1 ATOM 1969 C CB . ALA A 1 250 ? 15.465 -11.662 57.847 1.00 17.34 ? 253 ALA A CB 1 ATOM 1970 N N . PRO A 1 251 ? 15.416 -11.471 54.583 1.00 17.31 ? 254 PRO A N 1 ATOM 1971 C CA . PRO A 1 251 ? 14.486 -10.924 53.572 1.00 17.39 ? 254 PRO A CA 1 ATOM 1972 C C . PRO A 1 251 ? 13.101 -10.858 54.227 1.00 18.30 ? 254 PRO A C 1 ATOM 1973 O O . PRO A 1 251 ? 12.788 -11.705 55.076 1.00 18.27 ? 254 PRO A O 1 ATOM 1974 C CB . PRO A 1 251 ? 14.431 -12.014 52.503 1.00 18.01 ? 254 PRO A CB 1 ATOM 1975 C CG . PRO A 1 251 ? 14.743 -13.371 53.334 1.00 18.04 ? 254 PRO A CG 1 ATOM 1976 C CD . PRO A 1 251 ? 15.753 -12.901 54.353 1.00 18.35 ? 254 PRO A CD 1 ATOM 1977 N N . GLU A 1 252 ? 12.302 -9.867 53.838 1.00 18.07 ? 255 GLU A N 1 ATOM 1978 C CA . GLU A 1 252 ? 10.866 -9.912 54.114 1.00 18.92 ? 255 GLU A CA 1 ATOM 1979 C C . GLU A 1 252 ? 10.157 -10.476 52.904 1.00 19.15 ? 255 GLU A C 1 ATOM 1980 O O . GLU A 1 252 ? 9.049 -11.012 53.025 1.00 19.39 ? 255 GLU A O 1 ATOM 1981 C CB . GLU A 1 252 ? 10.295 -8.506 54.413 1.00 18.47 ? 255 GLU A CB 1 ATOM 1982 C CG . GLU A 1 252 ? 8.900 -8.602 55.003 1.00 23.23 ? 255 GLU A CG 1 ATOM 1983 C CD . GLU A 1 252 ? 8.257 -7.291 55.396 1.00 28.20 ? 255 GLU A CD 1 ATOM 1984 O OE1 . GLU A 1 252 ? 8.766 -6.217 54.995 1.00 27.87 ? 255 GLU A OE1 1 ATOM 1985 O OE2 . GLU A 1 252 ? 7.229 -7.380 56.122 1.00 27.93 ? 255 GLU A OE2 1 ATOM 1986 N N . TYR A 1 253 ? 10.780 -10.331 51.728 1.00 18.89 ? 256 TYR A N 1 ATOM 1987 C CA . TYR A 1 253 ? 10.156 -10.743 50.470 1.00 19.68 ? 256 TYR A CA 1 ATOM 1988 C C . TYR A 1 253 ? 10.913 -11.838 49.722 1.00 20.69 ? 256 TYR A C 1 ATOM 1989 O O . TYR A 1 253 ? 12.069 -12.052 49.988 1.00 21.38 ? 256 TYR A O 1 ATOM 1990 C CB . TYR A 1 253 ? 10.004 -9.540 49.531 1.00 19.19 ? 256 TYR A CB 1 ATOM 1991 C CG . TYR A 1 253 ? 9.067 -8.475 50.090 1.00 20.79 ? 256 TYR A CG 1 ATOM 1992 C CD1 . TYR A 1 253 ? 7.673 -8.515 49.847 1.00 21.41 ? 256 TYR A CD1 1 ATOM 1993 C CD2 . TYR A 1 253 ? 9.588 -7.428 50.857 1.00 24.33 ? 256 TYR A CD2 1 ATOM 1994 C CE1 . TYR A 1 253 ? 6.805 -7.481 50.383 1.00 23.62 ? 256 TYR A CE1 1 ATOM 1995 C CE2 . TYR A 1 253 ? 8.773 -6.420 51.387 1.00 23.44 ? 256 TYR A CE2 1 ATOM 1996 C CZ . TYR A 1 253 ? 7.397 -6.456 51.156 1.00 27.43 ? 256 TYR A CZ 1 ATOM 1997 O OH . TYR A 1 253 ? 6.684 -5.420 51.694 1.00 31.02 ? 256 TYR A OH 1 ATOM 1998 N N . GLY A 1 254 ? 10.231 -12.505 48.788 1.00 19.78 ? 257 GLY A N 1 ATOM 1999 C CA . GLY A 1 254 ? 10.868 -13.331 47.754 1.00 21.27 ? 257 GLY A CA 1 ATOM 2000 C C . GLY A 1 254 ? 10.409 -12.865 46.397 1.00 20.65 ? 257 GLY A C 1 ATOM 2001 O O . GLY A 1 254 ? 9.301 -12.326 46.268 1.00 22.93 ? 257 GLY A O 1 ATOM 2002 N N . PHE A 1 255 ? 11.234 -13.028 45.378 1.00 19.85 ? 258 PHE A N 1 ATOM 2003 C CA . PHE A 1 255 ? 10.801 -12.650 44.031 1.00 19.02 ? 258 PHE A CA 1 ATOM 2004 C C . PHE A 1 255 ? 10.484 -13.944 43.249 1.00 20.13 ? 258 PHE A C 1 ATOM 2005 O O . PHE A 1 255 ? 11.391 -14.640 42.827 1.00 18.25 ? 258 PHE A O 1 ATOM 2006 C CB . PHE A 1 255 ? 11.861 -11.846 43.287 1.00 19.12 ? 258 PHE A CB 1 ATOM 2007 C CG . PHE A 1 255 ? 12.129 -10.480 43.866 1.00 17.80 ? 258 PHE A CG 1 ATOM 2008 C CD1 . PHE A 1 255 ? 11.446 -9.362 43.374 1.00 20.66 ? 258 PHE A CD1 1 ATOM 2009 C CD2 . PHE A 1 255 ? 13.035 -10.305 44.900 1.00 20.25 ? 258 PHE A CD2 1 ATOM 2010 C CE1 . PHE A 1 255 ? 11.701 -8.062 43.865 1.00 23.29 ? 258 PHE A CE1 1 ATOM 2011 C CE2 . PHE A 1 255 ? 13.317 -8.992 45.423 1.00 19.88 ? 258 PHE A CE2 1 ATOM 2012 C CZ . PHE A 1 255 ? 12.634 -7.869 44.908 1.00 19.50 ? 258 PHE A CZ 1 ATOM 2013 N N . LYS A 1 256 ? 9.188 -14.252 43.087 1.00 19.56 ? 259 LYS A N 1 ATOM 2014 C CA . LYS A 1 256 ? 8.751 -15.402 42.319 1.00 20.79 ? 259 LYS A CA 1 ATOM 2015 C C . LYS A 1 256 ? 8.981 -15.071 40.826 1.00 21.58 ? 259 LYS A C 1 ATOM 2016 O O . LYS A 1 256 ? 8.547 -14.024 40.323 1.00 21.35 ? 259 LYS A O 1 ATOM 2017 C CB . LYS A 1 256 ? 7.244 -15.609 42.570 1.00 22.51 ? 259 LYS A CB 1 ATOM 2018 C CG . LYS A 1 256 ? 6.617 -16.729 41.762 1.00 24.42 ? 259 LYS A CG 1 ATOM 2019 C CD . LYS A 1 256 ? 5.060 -16.576 41.825 1.00 28.62 ? 259 LYS A CD 1 ATOM 2020 C CE . LYS A 1 256 ? 4.377 -17.105 40.600 1.00 33.75 ? 259 LYS A CE 1 ATOM 2021 N NZ . LYS A 1 256 ? 2.963 -17.543 40.952 1.00 32.56 ? 259 LYS A NZ 1 ATOM 2022 N N . ILE A 1 257 ? 9.667 -15.949 40.111 1.00 21.68 ? 260 ILE A N 1 ATOM 2023 C CA . ILE A 1 257 ? 9.826 -15.741 38.674 1.00 24.22 ? 260 ILE A CA 1 ATOM 2024 C C . ILE A 1 257 ? 8.463 -15.968 38.003 1.00 26.32 ? 260 ILE A C 1 ATOM 2025 O O . ILE A 1 257 ? 7.960 -17.093 37.984 1.00 27.88 ? 260 ILE A O 1 ATOM 2026 C CB . ILE A 1 257 ? 10.853 -16.719 38.110 1.00 24.95 ? 260 ILE A CB 1 ATOM 2027 C CG1 . ILE A 1 257 ? 12.212 -16.471 38.788 1.00 23.92 ? 260 ILE A CG1 1 ATOM 2028 C CG2 . ILE A 1 257 ? 10.891 -16.645 36.558 1.00 26.30 ? 260 ILE A CG2 1 ATOM 2029 C CD1 . ILE A 1 257 ? 13.319 -17.513 38.407 1.00 25.32 ? 260 ILE A CD1 1 ATOM 2030 N N . SER A 1 258 ? 7.857 -14.910 37.484 1.00 26.70 ? 261 SER A N 1 ATOM 2031 C CA . SER A 1 258 ? 6.489 -15.014 36.950 1.00 29.01 ? 261 SER A CA 1 ATOM 2032 C C . SER A 1 258 ? 6.453 -15.031 35.426 1.00 30.56 ? 261 SER A C 1 ATOM 2033 O O . SER A 1 258 ? 5.403 -15.336 34.828 1.00 30.87 ? 261 SER A O 1 ATOM 2034 C CB . SER A 1 258 ? 5.584 -13.895 37.460 1.00 28.18 ? 261 SER A CB 1 ATOM 2035 O OG . SER A 1 258 ? 6.202 -12.623 37.349 1.00 29.36 ? 261 SER A OG 1 ATOM 2036 N N . LYS A 1 259 ? 7.573 -14.672 34.801 1.00 31.20 ? 262 LYS A N 1 ATOM 2037 C CA . LYS A 1 259 ? 7.686 -14.746 33.355 1.00 31.87 ? 262 LYS A CA 1 ATOM 2038 C C . LYS A 1 259 ? 9.135 -14.996 32.939 1.00 32.09 ? 262 LYS A C 1 ATOM 2039 O O . LYS A 1 259 ? 10.062 -14.314 33.401 1.00 29.72 ? 262 LYS A O 1 ATOM 2040 C CB . LYS A 1 259 ? 7.120 -13.485 32.712 1.00 32.96 ? 262 LYS A CB 1 ATOM 2041 C CG . LYS A 1 259 ? 6.767 -13.638 31.247 1.00 37.22 ? 262 LYS A CG 1 ATOM 2042 C CD . LYS A 1 259 ? 5.360 -13.131 30.982 1.00 44.00 ? 262 LYS A CD 1 ATOM 2043 C CE . LYS A 1 259 ? 5.090 -12.931 29.479 1.00 48.15 ? 262 LYS A CE 1 ATOM 2044 N NZ . LYS A 1 259 ? 5.706 -13.982 28.589 1.00 49.30 ? 262 LYS A NZ 1 ATOM 2045 N N . ARG A 1 260 ? 9.307 -15.985 32.061 1.00 31.91 ? 263 ARG A N 1 ATOM 2046 C CA . ARG A 1 260 ? 10.612 -16.419 31.611 1.00 32.95 ? 263 ARG A CA 1 ATOM 2047 C C . ARG A 1 260 ? 10.726 -16.122 30.125 1.00 32.78 ? 263 ARG A C 1 ATOM 2048 O O . ARG A 1 260 ? 9.729 -16.102 29.414 1.00 31.70 ? 263 ARG A O 1 ATOM 2049 C CB . ARG A 1 260 ? 10.787 -17.920 31.841 1.00 33.94 ? 263 ARG A CB 1 ATOM 2050 C CG . ARG A 1 260 ? 10.987 -18.302 33.279 1.00 36.35 ? 263 ARG A CG 1 ATOM 2051 C CD . ARG A 1 260 ? 10.767 -19.780 33.461 1.00 38.04 ? 263 ARG A CD 1 ATOM 2052 N NE . ARG A 1 260 ? 10.938 -20.171 34.857 1.00 39.22 ? 263 ARG A NE 1 ATOM 2053 C CZ . ARG A 1 260 ? 12.108 -20.319 35.460 1.00 38.19 ? 263 ARG A CZ 1 ATOM 2054 N NH1 . ARG A 1 260 ? 13.236 -20.093 34.794 1.00 38.84 ? 263 ARG A NH1 1 ATOM 2055 N NH2 . ARG A 1 260 ? 12.151 -20.690 36.732 1.00 37.82 ? 263 ARG A NH2 1 ATOM 2056 N N . GLY A 1 261 A 11.936 -15.858 29.659 1.00 32.05 ? 263 GLY A N 1 ATOM 2057 C CA . GLY A 1 261 A 12.119 -15.665 28.240 1.00 32.34 ? 263 GLY A CA 1 ATOM 2058 C C . GLY A 1 261 A 13.414 -14.980 27.912 1.00 33.13 ? 263 GLY A C 1 ATOM 2059 O O . GLY A 1 261 A 14.158 -14.608 28.802 1.00 32.62 ? 263 GLY A O 1 ATOM 2060 N N . SER A 1 262 ? 13.663 -14.781 26.623 1.00 33.74 ? 264 SER A N 1 ATOM 2061 C CA . SER A 1 262 ? 14.895 -14.177 26.195 1.00 35.45 ? 264 SER A CA 1 ATOM 2062 C C . SER A 1 262 ? 14.861 -12.704 26.516 1.00 34.65 ? 264 SER A C 1 ATOM 2063 O O . SER A 1 262 ? 13.939 -11.990 26.121 1.00 35.57 ? 264 SER A O 1 ATOM 2064 C CB . SER A 1 262 ? 15.112 -14.388 24.701 1.00 35.88 ? 264 SER A CB 1 ATOM 2065 O OG . SER A 1 262 ? 16.492 -14.222 24.463 1.00 40.95 ? 264 SER A OG 1 ATOM 2066 N N . SER A 1 263 ? 15.864 -12.247 27.254 1.00 33.50 ? 265 SER A N 1 ATOM 2067 C CA . SER A 1 263 ? 15.879 -10.869 27.697 1.00 33.00 ? 265 SER A CA 1 ATOM 2068 C C . SER A 1 263 ? 17.342 -10.420 27.749 1.00 32.23 ? 265 SER A C 1 ATOM 2069 O O . SER A 1 263 ? 18.151 -10.915 26.958 1.00 32.98 ? 265 SER A O 1 ATOM 2070 C CB . SER A 1 263 ? 15.196 -10.785 29.051 1.00 32.47 ? 265 SER A CB 1 ATOM 2071 O OG . SER A 1 263 ? 15.020 -9.437 29.409 1.00 37.02 ? 265 SER A OG 1 ATOM 2072 N N . GLY A 1 264 ? 17.689 -9.520 28.662 1.00 30.45 ? 266 GLY A N 1 ATOM 2073 C CA . GLY A 1 264 ? 19.101 -9.179 28.889 1.00 29.44 ? 266 GLY A CA 1 ATOM 2074 C C . GLY A 1 264 ? 19.256 -7.801 29.493 1.00 28.18 ? 266 GLY A C 1 ATOM 2075 O O . GLY A 1 264 ? 18.298 -7.038 29.565 1.00 26.13 ? 266 GLY A O 1 ATOM 2076 N N . ILE A 1 265 ? 20.463 -7.491 29.949 1.00 27.54 ? 267 ILE A N 1 ATOM 2077 C CA . ILE A 1 265 ? 20.707 -6.208 30.586 1.00 27.75 ? 267 ILE A CA 1 ATOM 2078 C C . ILE A 1 265 ? 21.518 -5.430 29.595 1.00 28.28 ? 267 ILE A C 1 ATOM 2079 O O . ILE A 1 265 ? 22.574 -5.891 29.158 1.00 29.15 ? 267 ILE A O 1 ATOM 2080 C CB . ILE A 1 265 ? 21.480 -6.342 31.894 1.00 27.78 ? 267 ILE A CB 1 ATOM 2081 C CG1 . ILE A 1 265 ? 20.584 -6.962 32.966 1.00 28.37 ? 267 ILE A CG1 1 ATOM 2082 C CG2 . ILE A 1 265 ? 22.016 -4.943 32.350 1.00 28.92 ? 267 ILE A CG2 1 ATOM 2083 C CD1 . ILE A 1 265 ? 21.299 -7.346 34.281 1.00 30.92 ? 267 ILE A CD1 1 ATOM 2084 N N . MET A 1 266 ? 21.013 -4.281 29.203 1.00 27.11 ? 268 MET A N 1 ATOM 2085 C CA . MET A 1 266 ? 21.740 -3.444 28.312 1.00 28.39 ? 268 MET A CA 1 ATOM 2086 C C . MET A 1 266 ? 22.386 -2.291 29.102 1.00 28.01 ? 268 MET A C 1 ATOM 2087 O O . MET A 1 266 ? 21.710 -1.600 29.886 1.00 26.02 ? 268 MET A O 1 ATOM 2088 C CB . MET A 1 266 ? 20.807 -2.881 27.278 1.00 28.43 ? 268 MET A CB 1 ATOM 2089 C CG . MET A 1 266 ? 21.477 -1.877 26.413 1.00 33.32 ? 268 MET A CG 1 ATOM 2090 S SD . MET A 1 266 ? 20.327 -1.377 25.160 1.00 41.82 ? 268 MET A SD 1 ATOM 2091 C CE . MET A 1 266 ? 20.227 -2.910 24.238 1.00 31.02 ? 268 MET A CE 1 ATOM 2092 N N . LYS A 1 267 ? 23.691 -2.118 28.895 1.00 27.19 ? 269 LYS A N 1 ATOM 2093 C CA . LYS A 1 267 ? 24.425 -1.051 29.556 1.00 27.60 ? 269 LYS A CA 1 ATOM 2094 C C . LYS A 1 267 ? 24.282 0.228 28.764 1.00 27.50 ? 269 LYS A C 1 ATOM 2095 O O . LYS A 1 267 ? 24.675 0.287 27.594 1.00 27.56 ? 269 LYS A O 1 ATOM 2096 C CB . LYS A 1 267 ? 25.900 -1.447 29.744 1.00 28.71 ? 269 LYS A CB 1 ATOM 2097 C CG . LYS A 1 267 ? 26.103 -2.486 30.870 1.00 31.45 ? 269 LYS A CG 1 ATOM 2098 C CD . LYS A 1 267 ? 26.053 -1.771 32.239 1.00 34.60 ? 269 LYS A CD 1 ATOM 2099 C CE . LYS A 1 267 ? 26.357 -2.695 33.418 1.00 35.67 ? 269 LYS A CE 1 ATOM 2100 N NZ . LYS A 1 267 ? 26.206 -1.888 34.706 1.00 33.19 ? 269 LYS A NZ 1 ATOM 2101 N N . THR A 1 268 ? 23.672 1.240 29.377 1.00 26.28 ? 270 THR A N 1 ATOM 2102 C CA . THR A 1 268 ? 23.395 2.501 28.690 1.00 26.52 ? 270 THR A CA 1 ATOM 2103 C C . THR A 1 268 ? 23.151 3.584 29.716 1.00 26.88 ? 270 THR A C 1 ATOM 2104 O O . THR A 1 268 ? 22.626 3.296 30.820 1.00 25.52 ? 270 THR A O 1 ATOM 2105 C CB . THR A 1 268 ? 22.144 2.386 27.747 1.00 26.90 ? 270 THR A CB 1 ATOM 2106 O OG1 . THR A 1 268 ? 21.793 3.676 27.241 1.00 25.95 ? 270 THR A OG1 1 ATOM 2107 C CG2 . THR A 1 268 ? 20.928 1.797 28.483 1.00 28.16 ? 270 THR A CG2 1 ATOM 2108 N N . GLU A 1 269 ? 23.535 4.812 29.354 1.00 26.72 ? 271 GLU A N 1 ATOM 2109 C CA . GLU A 1 269 ? 23.287 6.006 30.145 1.00 27.69 ? 271 GLU A CA 1 ATOM 2110 C C . GLU A 1 269 ? 21.988 6.686 29.702 1.00 28.18 ? 271 GLU A C 1 ATOM 2111 O O . GLU A 1 269 ? 21.556 7.642 30.324 1.00 29.09 ? 271 GLU A O 1 ATOM 2112 C CB . GLU A 1 269 ? 24.475 6.991 30.041 1.00 28.70 ? 271 GLU A CB 1 ATOM 2113 C CG . GLU A 1 269 ? 25.849 6.314 30.264 1.00 29.22 ? 271 GLU A CG 1 ATOM 2114 C CD . GLU A 1 269 ? 25.919 5.539 31.606 1.00 30.11 ? 271 GLU A CD 1 ATOM 2115 O OE1 . GLU A 1 269 ? 25.625 6.140 32.646 1.00 29.78 ? 271 GLU A OE1 1 ATOM 2116 O OE2 . GLU A 1 269 ? 26.261 4.333 31.615 1.00 31.66 ? 271 GLU A OE2 1 ATOM 2117 N N . GLY A 1 270 ? 21.355 6.165 28.650 1.00 27.03 ? 272 GLY A N 1 ATOM 2118 C CA . GLY A 1 270 ? 20.204 6.817 28.032 1.00 27.20 ? 272 GLY A CA 1 ATOM 2119 C C . GLY A 1 270 ? 18.897 6.526 28.738 1.00 27.12 ? 272 GLY A C 1 ATOM 2120 O O . GLY A 1 270 ? 18.870 5.856 29.776 1.00 26.92 ? 272 GLY A O 1 ATOM 2121 N N . THR A 1 271 ? 17.818 7.055 28.174 1.00 26.72 ? 273 THR A N 1 ATOM 2122 C CA . THR A 1 271 ? 16.502 6.931 28.751 1.00 27.05 ? 273 THR A CA 1 ATOM 2123 C C . THR A 1 271 ? 15.516 6.447 27.683 1.00 26.16 ? 273 THR A C 1 ATOM 2124 O O . THR A 1 271 ? 15.732 6.652 26.473 1.00 26.36 ? 273 THR A O 1 ATOM 2125 C CB . THR A 1 271 ? 16.083 8.289 29.443 1.00 28.18 ? 273 THR A CB 1 ATOM 2126 O OG1 . THR A 1 271 ? 14.991 8.066 30.344 1.00 30.39 ? 273 THR A OG1 1 ATOM 2127 C CG2 . THR A 1 271 ? 15.710 9.351 28.416 1.00 28.69 ? 273 THR A CG2 1 ATOM 2128 N N . LEU A 1 272 ? 14.442 5.796 28.117 1.00 25.78 ? 274 LEU A N 1 ATOM 2129 C CA . LEU A 1 272 ? 13.476 5.228 27.181 1.00 25.77 ? 274 LEU A CA 1 ATOM 2130 C C . LEU A 1 272 ? 12.721 6.333 26.456 1.00 26.17 ? 274 LEU A C 1 ATOM 2131 O O . LEU A 1 272 ? 12.256 7.293 27.077 1.00 25.28 ? 274 LEU A O 1 ATOM 2132 C CB . LEU A 1 272 ? 12.464 4.318 27.904 1.00 26.20 ? 274 LEU A CB 1 ATOM 2133 C CG . LEU A 1 272 ? 11.263 3.760 27.112 1.00 25.03 ? 274 LEU A CG 1 ATOM 2134 C CD1 . LEU A 1 272 ? 11.760 2.852 25.984 1.00 24.63 ? 274 LEU A CD1 1 ATOM 2135 C CD2 . LEU A 1 272 ? 10.325 2.966 28.091 1.00 24.64 ? 274 LEU A CD2 1 ATOM 2136 N N . GLU A 1 273 ? 12.608 6.184 25.144 1.00 26.11 ? 275 GLU A N 1 ATOM 2137 C CA . GLU A 1 273 ? 11.814 7.107 24.352 1.00 28.14 ? 275 GLU A CA 1 ATOM 2138 C C . GLU A 1 273 ? 10.534 6.450 23.840 1.00 29.06 ? 275 GLU A C 1 ATOM 2139 O O . GLU A 1 273 ? 10.385 5.205 23.846 1.00 27.89 ? 275 GLU A O 1 ATOM 2140 C CB . GLU A 1 273 ? 12.665 7.711 23.229 1.00 28.62 ? 275 GLU A CB 1 ATOM 2141 C CG . GLU A 1 273 ? 13.716 8.697 23.768 1.00 30.53 ? 275 GLU A CG 1 ATOM 2142 C CD . GLU A 1 273 ? 14.597 9.304 22.671 1.00 33.82 ? 275 GLU A CD 1 ATOM 2143 O OE1 . GLU A 1 273 ? 14.053 9.954 21.745 1.00 35.52 ? 275 GLU A OE1 1 ATOM 2144 O OE2 . GLU A 1 273 ? 15.834 9.124 22.725 1.00 33.63 ? 275 GLU A OE2 1 ATOM 2145 N N . ASN A 1 274 ? 9.594 7.288 23.424 1.00 30.54 ? 276 ASN A N 1 ATOM 2146 C CA . ASN A 1 274 ? 8.310 6.804 22.919 1.00 32.66 ? 276 ASN A CA 1 ATOM 2147 C C . ASN A 1 274 ? 8.458 6.335 21.477 1.00 33.54 ? 276 ASN A C 1 ATOM 2148 O O . ASN A 1 274 ? 8.145 7.081 20.532 1.00 34.02 ? 276 ASN A O 1 ATOM 2149 C CB . ASN A 1 274 ? 7.217 7.891 23.040 1.00 33.00 ? 276 ASN A CB 1 ATOM 2150 C CG . ASN A 1 274 ? 5.829 7.355 22.684 1.00 35.46 ? 276 ASN A CG 1 ATOM 2151 O OD1 . ASN A 1 274 ? 5.658 6.158 22.451 1.00 36.10 ? 276 ASN A OD1 1 ATOM 2152 N ND2 . ASN A 1 274 ? 4.839 8.242 22.640 1.00 35.65 ? 276 ASN A ND2 1 ATOM 2153 N N . CYS A 1 275 ? 8.942 5.100 21.325 1.00 33.77 ? 277 CYS A N 1 ATOM 2154 C CA . CYS A 1 275 ? 9.221 4.472 20.040 1.00 34.73 ? 277 CYS A CA 1 ATOM 2155 C C . CYS A 1 275 ? 9.168 2.957 20.190 1.00 33.96 ? 277 CYS A C 1 ATOM 2156 O O . CYS A 1 275 ? 9.204 2.397 21.300 1.00 32.26 ? 277 CYS A O 1 ATOM 2157 C CB . CYS A 1 275 ? 10.608 4.857 19.456 1.00 35.05 ? 277 CYS A CB 1 ATOM 2158 S SG . CYS A 1 275 ? 12.058 4.529 20.563 1.00 42.83 ? 277 CYS A SG 1 ATOM 2159 N N . GLU A 1 276 ? 9.144 2.306 19.039 1.00 33.95 ? 278 GLU A N 1 ATOM 2160 C CA . GLU A 1 276 ? 8.821 0.917 18.934 1.00 35.05 ? 278 GLU A CA 1 ATOM 2161 C C . GLU A 1 276 ? 9.864 0.271 18.021 1.00 34.22 ? 278 GLU A C 1 ATOM 2162 O O . GLU A 1 276 ? 10.240 0.881 17.036 1.00 35.13 ? 278 GLU A O 1 ATOM 2163 C CB . GLU A 1 276 ? 7.407 0.849 18.332 1.00 36.55 ? 278 GLU A CB 1 ATOM 2164 C CG . GLU A 1 276 ? 6.981 -0.505 17.855 1.00 40.47 ? 278 GLU A CG 1 ATOM 2165 C CD . GLU A 1 276 ? 7.121 -1.540 18.936 1.00 44.16 ? 278 GLU A CD 1 ATOM 2166 O OE1 . GLU A 1 276 ? 6.932 -1.176 20.115 1.00 43.54 ? 278 GLU A OE1 1 ATOM 2167 O OE2 . GLU A 1 276 ? 7.424 -2.703 18.596 1.00 48.05 ? 278 GLU A OE2 1 ATOM 2168 N N . THR A 1 277 ? 10.337 -0.935 18.338 1.00 32.77 ? 279 THR A N 1 ATOM 2169 C CA . THR A 1 277 ? 11.282 -1.645 17.457 1.00 31.89 ? 279 THR A CA 1 ATOM 2170 C C . THR A 1 277 ? 11.219 -3.157 17.648 1.00 32.46 ? 279 THR A C 1 ATOM 2171 O O . THR A 1 277 ? 10.670 -3.636 18.636 1.00 32.55 ? 279 THR A O 1 ATOM 2172 C CB . THR A 1 277 ? 12.755 -1.192 17.701 1.00 31.46 ? 279 THR A CB 1 ATOM 2173 O OG1 . THR A 1 277 ? 13.604 -1.746 16.687 1.00 29.40 ? 279 THR A OG1 1 ATOM 2174 C CG2 . THR A 1 277 ? 13.259 -1.673 19.072 1.00 30.22 ? 279 THR A CG2 1 ATOM 2175 N N . LYS A 1 278 ? 11.821 -3.894 16.714 1.00 32.16 ? 280 LYS A N 1 ATOM 2176 C CA . LYS A 1 278 ? 11.949 -5.343 16.810 1.00 32.95 ? 280 LYS A CA 1 ATOM 2177 C C . LYS A 1 278 ? 13.356 -5.706 17.222 1.00 31.53 ? 280 LYS A C 1 ATOM 2178 O O . LYS A 1 278 ? 13.602 -6.828 17.627 1.00 31.62 ? 280 LYS A O 1 ATOM 2179 C CB . LYS A 1 278 ? 11.661 -6.006 15.453 1.00 34.40 ? 280 LYS A CB 1 ATOM 2180 C CG . LYS A 1 278 ? 10.238 -5.815 14.940 1.00 38.59 ? 280 LYS A CG 1 ATOM 2181 C CD . LYS A 1 278 ? 10.198 -6.166 13.437 1.00 44.51 ? 280 LYS A CD 1 ATOM 2182 C CE . LYS A 1 278 ? 8.878 -5.789 12.802 1.00 47.53 ? 280 LYS A CE 1 ATOM 2183 N NZ . LYS A 1 278 ? 9.087 -5.423 11.349 1.00 51.47 ? 280 LYS A NZ 1 ATOM 2184 N N . CYS A 1 279 ? 14.283 -4.752 17.089 1.00 30.60 ? 281 CYS A N 1 ATOM 2185 C CA . CYS A 1 279 ? 15.707 -4.988 17.315 1.00 30.15 ? 281 CYS A CA 1 ATOM 2186 C C . CYS A 1 279 ? 16.333 -3.765 17.992 1.00 28.72 ? 281 CYS A C 1 ATOM 2187 O O . CYS A 1 279 ? 16.450 -2.708 17.365 1.00 28.33 ? 281 CYS A O 1 ATOM 2188 C CB . CYS A 1 279 ? 16.447 -5.260 15.981 1.00 30.95 ? 281 CYS A CB 1 ATOM 2189 S SG . CYS A 1 279 ? 18.225 -5.464 16.172 1.00 36.15 ? 281 CYS A SG 1 ATOM 2190 N N . GLN A 1 280 ? 16.699 -3.914 19.263 1.00 26.69 ? 282 GLN A N 1 ATOM 2191 C CA . GLN A 1 280 ? 17.351 -2.853 20.035 1.00 26.77 ? 282 GLN A CA 1 ATOM 2192 C C . GLN A 1 280 ? 18.861 -3.081 20.212 1.00 26.46 ? 282 GLN A C 1 ATOM 2193 O O . GLN A 1 280 ? 19.292 -4.200 20.568 1.00 26.47 ? 282 GLN A O 1 ATOM 2194 C CB . GLN A 1 280 ? 16.716 -2.749 21.417 1.00 26.60 ? 282 GLN A CB 1 ATOM 2195 C CG . GLN A 1 280 ? 17.211 -1.550 22.202 1.00 25.36 ? 282 GLN A CG 1 ATOM 2196 C CD . GLN A 1 280 ? 16.740 -0.234 21.592 1.00 24.90 ? 282 GLN A CD 1 ATOM 2197 O OE1 . GLN A 1 280 ? 15.526 0.012 21.449 1.00 23.18 ? 282 GLN A OE1 1 ATOM 2198 N NE2 . GLN A 1 280 ? 17.691 0.611 21.221 1.00 22.29 ? 282 GLN A NE2 1 ATOM 2199 N N . THR A 1 281 ? 19.647 -2.028 19.968 1.00 26.24 ? 283 THR A N 1 ATOM 2200 C CA . THR A 1 281 ? 21.068 -2.001 20.348 1.00 27.54 ? 283 THR A CA 1 ATOM 2201 C C . THR A 1 281 ? 21.345 -0.869 21.350 1.00 28.39 ? 283 THR A C 1 ATOM 2202 O O . THR A 1 281 ? 20.549 0.038 21.497 1.00 29.69 ? 283 THR A O 1 ATOM 2203 C CB . THR A 1 281 ? 22.043 -1.818 19.146 1.00 26.96 ? 283 THR A CB 1 ATOM 2204 O OG1 . THR A 1 281 ? 22.311 -0.417 18.930 1.00 26.13 ? 283 THR A OG1 1 ATOM 2205 C CG2 . THR A 1 281 ? 21.470 -2.424 17.866 1.00 27.21 ? 283 THR A CG2 1 ATOM 2206 N N . PRO A 1 282 ? 22.496 -0.914 22.020 1.00 29.78 ? 284 PRO A N 1 ATOM 2207 C CA . PRO A 1 282 ? 22.825 0.141 22.971 1.00 30.53 ? 284 PRO A CA 1 ATOM 2208 C C . PRO A 1 282 ? 22.953 1.517 22.323 1.00 30.68 ? 284 PRO A C 1 ATOM 2209 O O . PRO A 1 282 ? 22.785 2.515 22.999 1.00 31.17 ? 284 PRO A O 1 ATOM 2210 C CB . PRO A 1 282 ? 24.158 -0.341 23.590 1.00 29.97 ? 284 PRO A CB 1 ATOM 2211 C CG . PRO A 1 282 ? 24.105 -1.827 23.455 1.00 30.74 ? 284 PRO A CG 1 ATOM 2212 C CD . PRO A 1 282 ? 23.402 -2.077 22.142 1.00 29.83 ? 284 PRO A CD 1 ATOM 2213 N N . LEU A 1 283 ? 23.190 1.578 21.015 1.00 30.94 ? 285 LEU A N 1 ATOM 2214 C CA . LEU A 1 283 ? 23.305 2.853 20.314 1.00 30.83 ? 285 LEU A CA 1 ATOM 2215 C C . LEU A 1 283 ? 21.968 3.403 19.845 1.00 29.90 ? 285 LEU A C 1 ATOM 2216 O O . LEU A 1 283 ? 21.840 4.596 19.634 1.00 30.85 ? 285 LEU A O 1 ATOM 2217 C CB . LEU A 1 283 ? 24.258 2.726 19.113 1.00 31.39 ? 285 LEU A CB 1 ATOM 2218 C CG . LEU A 1 283 ? 25.695 2.317 19.440 1.00 34.64 ? 285 LEU A CG 1 ATOM 2219 C CD1 . LEU A 1 283 ? 26.524 2.190 18.141 1.00 37.05 ? 285 LEU A CD1 1 ATOM 2220 C CD2 . LEU A 1 283 ? 26.345 3.333 20.392 1.00 37.24 ? 285 LEU A CD2 1 ATOM 2221 N N . GLY A 1 284 ? 20.982 2.524 19.694 1.00 28.93 ? 286 GLY A N 1 ATOM 2222 C CA . GLY A 1 284 ? 19.693 2.849 19.075 1.00 27.14 ? 286 GLY A CA 1 ATOM 2223 C C . GLY A 1 284 ? 19.072 1.616 18.427 1.00 26.16 ? 286 GLY A C 1 ATOM 2224 O O . GLY A 1 284 ? 19.708 0.563 18.348 1.00 25.74 ? 286 GLY A O 1 ATOM 2225 N N . ALA A 1 285 ? 17.852 1.767 17.923 1.00 26.06 ? 287 ALA A N 1 ATOM 2226 C CA . ALA A 1 285 ? 17.073 0.658 17.388 1.00 26.81 ? 287 ALA A CA 1 ATOM 2227 C C . ALA A 1 285 ? 17.300 0.515 15.884 1.00 27.58 ? 287 ALA A C 1 ATOM 2228 O O . ALA A 1 285 ? 17.545 1.495 15.202 1.00 27.58 ? 287 ALA A O 1 ATOM 2229 C CB . ALA A 1 285 ? 15.582 0.877 17.681 1.00 26.31 ? 287 ALA A CB 1 ATOM 2230 N N . ILE A 1 286 ? 17.212 -0.710 15.389 1.00 28.33 ? 288 ILE A N 1 ATOM 2231 C CA . ILE A 1 286 ? 17.411 -1.016 13.972 1.00 29.51 ? 288 ILE A CA 1 ATOM 2232 C C . ILE A 1 286 ? 16.073 -1.443 13.387 1.00 31.03 ? 288 ILE A C 1 ATOM 2233 O O . ILE A 1 286 ? 15.297 -2.138 14.036 1.00 31.25 ? 288 ILE A O 1 ATOM 2234 C CB . ILE A 1 286 ? 18.415 -2.193 13.826 1.00 29.74 ? 288 ILE A CB 1 ATOM 2235 C CG1 . ILE A 1 286 ? 19.846 -1.714 14.119 1.00 30.28 ? 288 ILE A CG1 1 ATOM 2236 C CG2 . ILE A 1 286 ? 18.295 -2.874 12.445 1.00 30.53 ? 288 ILE A CG2 1 ATOM 2237 C CD1 . ILE A 1 286 ? 20.927 -2.859 14.104 1.00 29.25 ? 288 ILE A CD1 1 ATOM 2238 N N . ASN A 1 287 ? 15.809 -0.997 12.161 1.00 33.00 ? 289 ASN A N 1 ATOM 2239 C CA . ASN A 1 287 ? 14.596 -1.320 11.401 1.00 35.11 ? 289 ASN A CA 1 ATOM 2240 C C . ASN A 1 287 ? 15.056 -1.507 9.959 1.00 35.77 ? 289 ASN A C 1 ATOM 2241 O O . ASN A 1 287 ? 15.280 -0.542 9.225 1.00 36.28 ? 289 ASN A O 1 ATOM 2242 C CB . ASN A 1 287 ? 13.583 -0.164 11.511 1.00 35.16 ? 289 ASN A CB 1 ATOM 2243 C CG . ASN A 1 287 ? 12.353 -0.337 10.602 1.00 37.65 ? 289 ASN A CG 1 ATOM 2244 O OD1 . ASN A 1 287 ? 11.924 -1.453 10.293 1.00 39.26 ? 289 ASN A OD1 1 ATOM 2245 N ND2 . ASN A 1 287 ? 11.771 0.793 10.182 1.00 43.03 ? 289 ASN A ND2 1 ATOM 2246 N N . THR A 1 288 ? 15.229 -2.754 9.577 1.00 36.27 ? 290 THR A N 1 ATOM 2247 C CA . THR A 1 288 ? 15.796 -3.082 8.299 1.00 37.93 ? 290 THR A CA 1 ATOM 2248 C C . THR A 1 288 ? 15.306 -4.467 7.938 1.00 39.03 ? 290 THR A C 1 ATOM 2249 O O . THR A 1 288 ? 14.855 -5.202 8.808 1.00 39.68 ? 290 THR A O 1 ATOM 2250 C CB . THR A 1 288 ? 17.341 -3.118 8.382 1.00 37.44 ? 290 THR A CB 1 ATOM 2251 O OG1 . THR A 1 288 ? 17.887 -3.324 7.076 1.00 38.16 ? 290 THR A OG1 1 ATOM 2252 C CG2 . THR A 1 288 ? 17.813 -4.234 9.287 1.00 36.79 ? 290 THR A CG2 1 ATOM 2253 N N . THR A 1 289 ? 15.392 -4.812 6.658 1.00 40.57 ? 291 THR A N 1 ATOM 2254 C CA . THR A 1 289 ? 15.216 -6.199 6.211 1.00 42.47 ? 291 THR A CA 1 ATOM 2255 C C . THR A 1 289 ? 16.536 -6.797 5.715 1.00 42.02 ? 291 THR A C 1 ATOM 2256 O O . THR A 1 289 ? 16.575 -7.956 5.294 1.00 42.63 ? 291 THR A O 1 ATOM 2257 C CB . THR A 1 289 ? 14.151 -6.332 5.084 1.00 43.00 ? 291 THR A CB 1 ATOM 2258 O OG1 . THR A 1 289 ? 14.442 -5.389 4.043 1.00 45.16 ? 291 THR A OG1 1 ATOM 2259 C CG2 . THR A 1 289 ? 12.739 -6.085 5.628 1.00 44.09 ? 291 THR A CG2 1 ATOM 2260 N N . LEU A 1 290 ? 17.609 -6.009 5.777 1.00 41.62 ? 292 LEU A N 1 ATOM 2261 C CA . LEU A 1 290 ? 18.942 -6.470 5.376 1.00 41.38 ? 292 LEU A CA 1 ATOM 2262 C C . LEU A 1 290 ? 19.464 -7.548 6.319 1.00 40.85 ? 292 LEU A C 1 ATOM 2263 O O . LEU A 1 290 ? 19.190 -7.492 7.521 1.00 41.44 ? 292 LEU A O 1 ATOM 2264 C CB . LEU A 1 290 ? 19.913 -5.289 5.298 1.00 40.87 ? 292 LEU A CB 1 ATOM 2265 C CG . LEU A 1 290 ? 19.527 -4.213 4.281 1.00 42.09 ? 292 LEU A CG 1 ATOM 2266 C CD1 . LEU A 1 290 ? 20.552 -3.105 4.309 1.00 41.36 ? 292 LEU A CD1 1 ATOM 2267 C CD2 . LEU A 1 290 ? 19.410 -4.797 2.869 1.00 42.71 ? 292 LEU A CD2 1 ATOM 2268 N N . PRO A 1 291 ? 20.207 -8.536 5.781 1.00 40.16 ? 293 PRO A N 1 ATOM 2269 C CA . PRO A 1 291 ? 20.676 -9.694 6.553 1.00 39.23 ? 293 PRO A CA 1 ATOM 2270 C C . PRO A 1 291 ? 21.798 -9.439 7.565 1.00 37.98 ? 293 PRO A C 1 ATOM 2271 O O . PRO A 1 291 ? 21.934 -10.218 8.527 1.00 37.95 ? 293 PRO A O 1 ATOM 2272 C CB . PRO A 1 291 ? 21.185 -10.656 5.463 1.00 39.44 ? 293 PRO A CB 1 ATOM 2273 C CG . PRO A 1 291 ? 21.542 -9.764 4.308 1.00 39.76 ? 293 PRO A CG 1 ATOM 2274 C CD . PRO A 1 291 ? 20.457 -8.723 4.332 1.00 40.76 ? 293 PRO A CD 1 ATOM 2275 N N . PHE A 1 292 ? 22.588 -8.385 7.342 1.00 36.07 ? 294 PHE A N 1 ATOM 2276 C CA . PHE A 1 292 ? 23.729 -8.028 8.193 1.00 34.63 ? 294 PHE A CA 1 ATOM 2277 C C . PHE A 1 292 ? 23.580 -6.599 8.691 1.00 33.05 ? 294 PHE A C 1 ATOM 2278 O O . PHE A 1 292 ? 22.886 -5.787 8.073 1.00 31.82 ? 294 PHE A O 1 ATOM 2279 C CB . PHE A 1 292 ? 25.053 -8.094 7.441 1.00 35.11 ? 294 PHE A CB 1 ATOM 2280 C CG . PHE A 1 292 ? 25.399 -9.453 6.929 1.00 37.66 ? 294 PHE A CG 1 ATOM 2281 C CD1 . PHE A 1 292 ? 26.171 -10.318 7.698 1.00 40.04 ? 294 PHE A CD1 1 ATOM 2282 C CD2 . PHE A 1 292 ? 24.963 -9.869 5.669 1.00 40.33 ? 294 PHE A CD2 1 ATOM 2283 C CE1 . PHE A 1 292 ? 26.513 -11.603 7.216 1.00 42.67 ? 294 PHE A CE1 1 ATOM 2284 C CE2 . PHE A 1 292 ? 25.290 -11.139 5.172 1.00 41.21 ? 294 PHE A CE2 1 ATOM 2285 C CZ . PHE A 1 292 ? 26.069 -12.008 5.945 1.00 42.31 ? 294 PHE A CZ 1 ATOM 2286 N N . HIS A 1 293 ? 24.247 -6.306 9.807 1.00 31.88 ? 295 HIS A N 1 ATOM 2287 C CA . HIS A 1 293 ? 24.364 -4.937 10.290 1.00 30.64 ? 295 HIS A CA 1 ATOM 2288 C C . HIS A 1 293 ? 25.725 -4.799 10.938 1.00 30.92 ? 295 HIS A C 1 ATOM 2289 O O . HIS A 1 293 ? 26.353 -5.804 11.344 1.00 30.89 ? 295 HIS A O 1 ATOM 2290 C CB . HIS A 1 293 ? 23.220 -4.560 11.250 1.00 30.22 ? 295 HIS A CB 1 ATOM 2291 C CG . HIS A 1 293 ? 23.408 -5.073 12.645 1.00 30.57 ? 295 HIS A CG 1 ATOM 2292 N ND1 . HIS A 1 293 ? 24.071 -4.356 13.622 1.00 30.98 ? 295 HIS A ND1 1 ATOM 2293 C CD2 . HIS A 1 293 ? 23.081 -6.263 13.207 1.00 31.05 ? 295 HIS A CD2 1 ATOM 2294 C CE1 . HIS A 1 293 ? 24.111 -5.068 14.738 1.00 30.77 ? 295 HIS A CE1 1 ATOM 2295 N NE2 . HIS A 1 293 ? 23.526 -6.234 14.509 1.00 31.60 ? 295 HIS A NE2 1 ATOM 2296 N N . ASN A 1 294 ? 26.187 -3.564 11.054 1.00 29.86 ? 296 ASN A N 1 ATOM 2297 C CA . ASN A 1 294 ? 27.451 -3.322 11.695 1.00 30.99 ? 296 ASN A CA 1 ATOM 2298 C C . ASN A 1 294 ? 27.320 -2.321 12.834 1.00 30.57 ? 296 ASN A C 1 ATOM 2299 O O . ASN A 1 294 ? 28.275 -1.646 13.162 1.00 30.95 ? 296 ASN A O 1 ATOM 2300 C CB . ASN A 1 294 ? 28.519 -2.886 10.663 1.00 31.16 ? 296 ASN A CB 1 ATOM 2301 C CG . ASN A 1 294 ? 28.310 -1.459 10.123 1.00 32.30 ? 296 ASN A CG 1 ATOM 2302 O OD1 . ASN A 1 294 ? 27.313 -0.804 10.400 1.00 32.32 ? 296 ASN A OD1 1 ATOM 2303 N ND2 . ASN A 1 294 ? 29.258 -0.999 9.319 1.00 32.96 ? 296 ASN A ND2 1 ATOM 2304 N N . VAL A 1 295 ? 26.131 -2.237 13.429 1.00 30.27 ? 297 VAL A N 1 ATOM 2305 C CA . VAL A 1 295 ? 25.834 -1.161 14.384 1.00 30.58 ? 297 VAL A CA 1 ATOM 2306 C C . VAL A 1 295 ? 26.517 -1.379 15.743 1.00 31.06 ? 297 VAL A C 1 ATOM 2307 O O . VAL A 1 295 ? 27.232 -0.505 16.208 1.00 31.72 ? 297 VAL A O 1 ATOM 2308 C CB . VAL A 1 295 ? 24.317 -0.916 14.556 1.00 30.35 ? 297 VAL A CB 1 ATOM 2309 C CG1 . VAL A 1 295 ? 24.046 0.018 15.764 1.00 29.24 ? 297 VAL A CG1 1 ATOM 2310 C CG2 . VAL A 1 295 ? 23.742 -0.279 13.285 1.00 28.88 ? 297 VAL A CG2 1 ATOM 2311 N N . HIS A 1 296 ? 26.314 -2.550 16.344 1.00 31.24 ? 298 HIS A N 1 ATOM 2312 C CA . HIS A 1 296 ? 26.847 -2.864 17.667 1.00 32.20 ? 298 HIS A CA 1 ATOM 2313 C C . HIS A 1 296 ? 26.676 -4.357 17.863 1.00 32.65 ? 298 HIS A C 1 ATOM 2314 O O . HIS A 1 296 ? 25.673 -4.923 17.432 1.00 32.95 ? 298 HIS A O 1 ATOM 2315 C CB . HIS A 1 296 ? 26.090 -2.062 18.757 1.00 32.22 ? 298 HIS A CB 1 ATOM 2316 C CG . HIS A 1 296 ? 26.759 -2.077 20.103 1.00 32.68 ? 298 HIS A CG 1 ATOM 2317 N ND1 . HIS A 1 296 ? 26.793 -3.198 20.910 1.00 33.25 ? 298 HIS A ND1 1 ATOM 2318 C CD2 . HIS A 1 296 ? 27.438 -1.115 20.771 1.00 31.69 ? 298 HIS A CD2 1 ATOM 2319 C CE1 . HIS A 1 296 ? 27.449 -2.919 22.023 1.00 30.95 ? 298 HIS A CE1 1 ATOM 2320 N NE2 . HIS A 1 296 ? 27.860 -1.667 21.958 1.00 32.45 ? 298 HIS A NE2 1 ATOM 2321 N N . PRO A 1 297 ? 27.667 -5.032 18.484 1.00 34.18 ? 299 PRO A N 1 ATOM 2322 C CA . PRO A 1 297 ? 27.523 -6.473 18.681 1.00 34.13 ? 299 PRO A CA 1 ATOM 2323 C C . PRO A 1 297 ? 26.443 -6.911 19.691 1.00 34.65 ? 299 PRO A C 1 ATOM 2324 O O . PRO A 1 297 ? 25.944 -8.040 19.616 1.00 34.52 ? 299 PRO A O 1 ATOM 2325 C CB . PRO A 1 297 ? 28.918 -6.901 19.154 1.00 34.27 ? 299 PRO A CB 1 ATOM 2326 C CG . PRO A 1 297 ? 29.507 -5.692 19.712 1.00 34.06 ? 299 PRO A CG 1 ATOM 2327 C CD . PRO A 1 297 ? 28.998 -4.556 18.904 1.00 33.90 ? 299 PRO A CD 1 ATOM 2328 N N . LEU A 1 298 ? 26.071 -6.045 20.625 1.00 35.87 ? 300 LEU A N 1 ATOM 2329 C CA . LEU A 1 298 ? 25.152 -6.485 21.680 1.00 36.55 ? 300 LEU A CA 1 ATOM 2330 C C . LEU A 1 298 ? 23.742 -6.009 21.408 1.00 36.62 ? 300 LEU A C 1 ATOM 2331 O O . LEU A 1 298 ? 23.353 -4.909 21.821 1.00 37.81 ? 300 LEU A O 1 ATOM 2332 C CB . LEU A 1 298 ? 25.638 -6.000 23.055 1.00 37.26 ? 300 LEU A CB 1 ATOM 2333 C CG . LEU A 1 298 ? 27.038 -6.431 23.529 1.00 38.31 ? 300 LEU A CG 1 ATOM 2334 C CD1 . LEU A 1 298 ? 27.460 -5.623 24.742 1.00 41.17 ? 300 LEU A CD1 1 ATOM 2335 C CD2 . LEU A 1 298 ? 27.124 -7.944 23.820 1.00 41.53 ? 300 LEU A CD2 1 ATOM 2336 N N . THR A 1 299 ? 22.963 -6.851 20.752 1.00 35.84 ? 301 THR A N 1 ATOM 2337 C CA . THR A 1 299 ? 21.609 -6.491 20.369 1.00 35.02 ? 301 THR A CA 1 ATOM 2338 C C . THR A 1 299 ? 20.594 -7.367 21.090 1.00 34.85 ? 301 THR A C 1 ATOM 2339 O O . THR A 1 299 ? 20.896 -8.501 21.465 1.00 34.38 ? 301 THR A O 1 ATOM 2340 C CB . THR A 1 299 ? 21.378 -6.605 18.832 1.00 34.92 ? 301 THR A CB 1 ATOM 2341 O OG1 . THR A 1 299 ? 21.306 -7.982 18.444 1.00 36.18 ? 301 THR A OG1 1 ATOM 2342 C CG2 . THR A 1 299 ? 22.476 -5.928 18.036 1.00 34.51 ? 301 THR A CG2 1 ATOM 2343 N N . ILE A 1 300 ? 19.377 -6.859 21.245 1.00 34.36 ? 302 ILE A N 1 ATOM 2344 C CA . ILE A 1 300 ? 18.288 -7.664 21.752 1.00 34.84 ? 302 ILE A CA 1 ATOM 2345 C C . ILE A 1 300 ? 17.107 -7.615 20.794 1.00 36.04 ? 302 ILE A C 1 ATOM 2346 O O . ILE A 1 300 ? 16.772 -6.551 20.261 1.00 34.82 ? 302 ILE A O 1 ATOM 2347 C CB . ILE A 1 300 ? 17.857 -7.219 23.192 1.00 35.53 ? 302 ILE A CB 1 ATOM 2348 C CG1 . ILE A 1 300 ? 19.103 -7.169 24.099 1.00 36.15 ? 302 ILE A CG1 1 ATOM 2349 C CG2 . ILE A 1 300 ? 16.769 -8.183 23.755 1.00 34.29 ? 302 ILE A CG2 1 ATOM 2350 C CD1 . ILE A 1 300 ? 18.930 -6.437 25.434 1.00 38.99 ? 302 ILE A CD1 1 ATOM 2351 N N . GLY A 1 301 ? 16.480 -8.773 20.580 1.00 36.09 ? 303 GLY A N 1 ATOM 2352 C CA . GLY A 1 301 ? 15.277 -8.876 19.763 1.00 37.99 ? 303 GLY A CA 1 ATOM 2353 C C . GLY A 1 301 ? 15.529 -9.691 18.499 1.00 39.77 ? 303 GLY A C 1 ATOM 2354 O O . GLY A 1 301 ? 16.409 -10.554 18.470 1.00 39.71 ? 303 GLY A O 1 ATOM 2355 N N . GLU A 1 302 ? 14.773 -9.399 17.448 1.00 40.87 ? 304 GLU A N 1 ATOM 2356 C CA . GLU A 1 302 ? 14.918 -10.124 16.178 1.00 42.49 ? 304 GLU A CA 1 ATOM 2357 C C . GLU A 1 302 ? 15.807 -9.296 15.261 1.00 42.03 ? 304 GLU A C 1 ATOM 2358 O O . GLU A 1 302 ? 15.350 -8.333 14.627 1.00 42.29 ? 304 GLU A O 1 ATOM 2359 C CB . GLU A 1 302 ? 13.543 -10.404 15.586 1.00 43.23 ? 304 GLU A CB 1 ATOM 2360 C CG . GLU A 1 302 ? 12.771 -11.409 16.463 1.00 48.07 ? 304 GLU A CG 1 ATOM 2361 C CD . GLU A 1 302 ? 11.287 -11.439 16.182 1.00 53.87 ? 304 GLU A CD 1 ATOM 2362 O OE1 . GLU A 1 302 ? 10.586 -10.445 16.505 1.00 55.15 ? 304 GLU A OE1 1 ATOM 2363 O OE2 . GLU A 1 302 ? 10.818 -12.474 15.649 1.00 57.34 ? 304 GLU A OE2 1 ATOM 2364 N N . CYS A 1 303 ? 17.084 -9.655 15.255 1.00 41.41 ? 305 CYS A N 1 ATOM 2365 C CA . CYS A 1 303 ? 18.131 -8.796 14.730 1.00 42.13 ? 305 CYS A CA 1 ATOM 2366 C C . CYS A 1 303 ? 18.828 -9.406 13.520 1.00 41.23 ? 305 CYS A C 1 ATOM 2367 O O . CYS A 1 303 ? 18.806 -10.626 13.353 1.00 41.01 ? 305 CYS A O 1 ATOM 2368 C CB . CYS A 1 303 ? 19.147 -8.460 15.823 1.00 41.75 ? 305 CYS A CB 1 ATOM 2369 S SG . CYS A 1 303 ? 18.465 -7.334 17.114 1.00 47.16 ? 305 CYS A SG 1 ATOM 2370 N N . PRO A 1 304 ? 19.426 -8.546 12.665 1.00 40.00 ? 306 PRO A N 1 ATOM 2371 C CA . PRO A 1 304 ? 20.259 -9.041 11.572 1.00 39.48 ? 306 PRO A CA 1 ATOM 2372 C C . PRO A 1 304 ? 21.487 -9.602 12.229 1.00 38.59 ? 306 PRO A C 1 ATOM 2373 O O . PRO A 1 304 ? 21.659 -9.437 13.427 1.00 37.82 ? 306 PRO A O 1 ATOM 2374 C CB . PRO A 1 304 ? 20.643 -7.762 10.801 1.00 38.38 ? 306 PRO A CB 1 ATOM 2375 C CG . PRO A 1 304 ? 19.704 -6.714 11.263 1.00 39.47 ? 306 PRO A CG 1 ATOM 2376 C CD . PRO A 1 304 ? 19.372 -7.070 12.681 1.00 39.94 ? 306 PRO A CD 1 ATOM 2377 N N . LYS A 1 305 ? 22.358 -10.223 11.460 1.00 38.23 ? 307 LYS A N 1 ATOM 2378 C CA A LYS A 1 305 ? 23.576 -10.719 12.037 1.00 38.62 ? 307 LYS A CA 1 ATOM 2379 C C . LYS A 1 305 ? 24.638 -9.639 11.977 1.00 38.10 ? 307 LYS A C 1 ATOM 2380 O O . LYS A 1 305 ? 24.772 -8.956 10.960 1.00 38.24 ? 307 LYS A O 1 ATOM 2381 C CB A LYS A 1 305 ? 24.020 -11.996 11.318 1.00 39.44 ? 307 LYS A CB 1 ATOM 2382 C CG A LYS A 1 305 ? 22.955 -13.126 11.361 1.00 43.14 ? 307 LYS A CG 1 ATOM 2383 C CD A LYS A 1 305 ? 22.809 -13.780 12.768 1.00 47.57 ? 307 LYS A CD 1 ATOM 2384 C CE A LYS A 1 305 ? 21.387 -14.241 13.042 1.00 50.05 ? 307 LYS A CE 1 ATOM 2385 N NZ A LYS A 1 305 ? 20.542 -13.064 13.436 1.00 52.30 ? 307 LYS A NZ 1 ATOM 2386 N N . TYR A 1 306 ? 25.388 -9.497 13.070 1.00 36.60 ? 308 TYR A N 1 ATOM 2387 C CA . TYR A 1 306 ? 26.422 -8.498 13.186 1.00 35.59 ? 308 TYR A CA 1 ATOM 2388 C C . TYR A 1 306 ? 27.784 -8.907 12.574 1.00 36.07 ? 308 TYR A C 1 ATOM 2389 O O . TYR A 1 306 ? 28.249 -10.035 12.755 1.00 35.51 ? 308 TYR A O 1 ATOM 2390 C CB . TYR A 1 306 ? 26.585 -8.133 14.656 1.00 34.79 ? 308 TYR A CB 1 ATOM 2391 C CG . TYR A 1 306 ? 27.702 -7.183 14.917 1.00 34.19 ? 308 TYR A CG 1 ATOM 2392 C CD1 . TYR A 1 306 ? 27.530 -5.800 14.728 1.00 33.14 ? 308 TYR A CD1 1 ATOM 2393 C CD2 . TYR A 1 306 ? 28.930 -7.648 15.375 1.00 33.28 ? 308 TYR A CD2 1 ATOM 2394 C CE1 . TYR A 1 306 ? 28.530 -4.942 14.960 1.00 33.98 ? 308 TYR A CE1 1 ATOM 2395 C CE2 . TYR A 1 306 ? 29.964 -6.772 15.618 1.00 34.62 ? 308 TYR A CE2 1 ATOM 2396 C CZ . TYR A 1 306 ? 29.773 -5.434 15.395 1.00 34.70 ? 308 TYR A CZ 1 ATOM 2397 O OH . TYR A 1 306 ? 30.805 -4.558 15.630 1.00 34.84 ? 308 TYR A OH 1 ATOM 2398 N N . VAL A 1 307 ? 28.413 -7.972 11.865 1.00 35.68 ? 309 VAL A N 1 ATOM 2399 C CA . VAL A 1 307 ? 29.774 -8.140 11.328 1.00 36.05 ? 309 VAL A CA 1 ATOM 2400 C C . VAL A 1 307 ? 30.497 -6.827 11.496 1.00 36.48 ? 309 VAL A C 1 ATOM 2401 O O . VAL A 1 307 ? 29.846 -5.774 11.566 1.00 36.78 ? 309 VAL A O 1 ATOM 2402 C CB . VAL A 1 307 ? 29.781 -8.500 9.801 1.00 36.46 ? 309 VAL A CB 1 ATOM 2403 C CG1 . VAL A 1 307 ? 29.205 -9.864 9.560 1.00 36.24 ? 309 VAL A CG1 1 ATOM 2404 C CG2 . VAL A 1 307 ? 29.009 -7.439 8.977 1.00 35.19 ? 309 VAL A CG2 1 ATOM 2405 N N . LYS A 1 308 ? 31.823 -6.875 11.530 1.00 37.30 ? 310 LYS A N 1 ATOM 2406 C CA . LYS A 1 308 ? 32.657 -5.680 11.646 1.00 39.13 ? 310 LYS A CA 1 ATOM 2407 C C . LYS A 1 308 ? 32.814 -4.866 10.347 1.00 39.59 ? 310 LYS A C 1 ATOM 2408 O O . LYS A 1 308 ? 33.385 -3.779 10.364 1.00 40.20 ? 310 LYS A O 1 ATOM 2409 C CB . LYS A 1 308 ? 34.061 -6.060 12.104 1.00 40.09 ? 310 LYS A CB 1 ATOM 2410 C CG . LYS A 1 308 ? 34.222 -6.428 13.559 1.00 42.54 ? 310 LYS A CG 1 ATOM 2411 C CD . LYS A 1 308 ? 35.726 -6.497 13.831 1.00 47.89 ? 310 LYS A CD 1 ATOM 2412 C CE . LYS A 1 308 ? 36.070 -6.516 15.302 1.00 51.69 ? 310 LYS A CE 1 ATOM 2413 N NZ . LYS A 1 308 ? 36.444 -7.893 15.752 1.00 54.67 ? 310 LYS A NZ 1 ATOM 2414 N N . SER A 1 309 ? 32.323 -5.394 9.231 1.00 39.10 ? 311 SER A N 1 ATOM 2415 C CA . SER A 1 309 ? 32.576 -4.817 7.907 1.00 39.28 ? 311 SER A CA 1 ATOM 2416 C C . SER A 1 309 ? 32.142 -3.359 7.792 1.00 39.00 ? 311 SER A C 1 ATOM 2417 O O . SER A 1 309 ? 31.152 -2.970 8.381 1.00 38.65 ? 311 SER A O 1 ATOM 2418 C CB . SER A 1 309 ? 31.822 -5.646 6.862 1.00 39.14 ? 311 SER A CB 1 ATOM 2419 O OG . SER A 1 309 ? 32.083 -7.027 7.051 1.00 38.43 ? 311 SER A OG 1 ATOM 2420 N N . GLU A 1 310 ? 32.866 -2.570 7.009 1.00 40.16 ? 312 GLU A N 1 ATOM 2421 C CA . GLU A 1 310 ? 32.415 -1.236 6.649 1.00 41.46 ? 312 GLU A CA 1 ATOM 2422 C C . GLU A 1 310 ? 31.453 -1.288 5.451 1.00 41.20 ? 312 GLU A C 1 ATOM 2423 O O . GLU A 1 310 ? 30.586 -0.421 5.280 1.00 41.10 ? 312 GLU A O 1 ATOM 2424 C CB . GLU A 1 310 ? 33.610 -0.346 6.332 1.00 42.88 ? 312 GLU A CB 1 ATOM 2425 C CG . GLU A 1 310 ? 34.579 -0.133 7.503 1.00 47.54 ? 312 GLU A CG 1 ATOM 2426 C CD . GLU A 1 310 ? 35.634 0.939 7.188 1.00 53.05 ? 312 GLU A CD 1 ATOM 2427 O OE1 . GLU A 1 310 ? 35.247 2.060 6.772 1.00 55.26 ? 312 GLU A OE1 1 ATOM 2428 O OE2 . GLU A 1 310 ? 36.847 0.661 7.350 1.00 55.00 ? 312 GLU A OE2 1 ATOM 2429 N N . LYS A 1 311 ? 31.601 -2.319 4.628 1.00 40.78 ? 313 LYS A N 1 ATOM 2430 C CA . LYS A 1 311 ? 30.762 -2.474 3.446 1.00 41.05 ? 313 LYS A CA 1 ATOM 2431 C C . LYS A 1 311 ? 30.584 -3.939 3.038 1.00 39.78 ? 313 LYS A C 1 ATOM 2432 O O . LYS A 1 311 ? 31.483 -4.754 3.173 1.00 40.38 ? 313 LYS A O 1 ATOM 2433 C CB . LYS A 1 311 ? 31.311 -1.640 2.275 1.00 41.47 ? 313 LYS A CB 1 ATOM 2434 C CG . LYS A 1 311 ? 32.799 -1.873 2.002 1.00 44.27 ? 313 LYS A CG 1 ATOM 2435 C CD . LYS A 1 311 ? 33.276 -1.086 0.784 1.00 47.10 ? 313 LYS A CD 1 ATOM 2436 C CE . LYS A 1 311 ? 34.779 -1.225 0.641 1.00 48.08 ? 313 LYS A CE 1 ATOM 2437 N NZ . LYS A 1 311 ? 35.248 -0.652 -0.638 1.00 51.01 ? 313 LYS A NZ 1 ATOM 2438 N N . LEU A 1 312 ? 29.391 -4.262 2.561 1.00 38.96 ? 314 LEU A N 1 ATOM 2439 C CA . LEU A 1 312 ? 29.107 -5.565 1.966 1.00 38.08 ? 314 LEU A CA 1 ATOM 2440 C C . LEU A 1 312 ? 28.101 -5.331 0.868 1.00 37.28 ? 314 LEU A C 1 ATOM 2441 O O . LEU A 1 312 ? 26.907 -5.116 1.142 1.00 36.16 ? 314 LEU A O 1 ATOM 2442 C CB . LEU A 1 312 ? 28.520 -6.543 2.980 1.00 37.94 ? 314 LEU A CB 1 ATOM 2443 C CG . LEU A 1 312 ? 29.454 -7.132 4.033 1.00 39.54 ? 314 LEU A CG 1 ATOM 2444 C CD1 . LEU A 1 312 ? 28.608 -7.836 5.075 1.00 38.98 ? 314 LEU A CD1 1 ATOM 2445 C CD2 . LEU A 1 312 ? 30.451 -8.088 3.397 1.00 38.39 ? 314 LEU A CD2 1 ATOM 2446 N N . VAL A 1 313 ? 28.592 -5.366 -0.373 1.00 36.64 ? 315 VAL A N 1 ATOM 2447 C CA . VAL A 1 313 ? 27.761 -5.085 -1.541 1.00 35.56 ? 315 VAL A CA 1 ATOM 2448 C C . VAL A 1 313 ? 27.997 -6.197 -2.539 1.00 35.03 ? 315 VAL A C 1 ATOM 2449 O O . VAL A 1 313 ? 29.129 -6.448 -2.955 1.00 34.24 ? 315 VAL A O 1 ATOM 2450 C CB . VAL A 1 313 ? 28.092 -3.715 -2.180 1.00 35.72 ? 315 VAL A CB 1 ATOM 2451 C CG1 . VAL A 1 313 ? 27.085 -3.378 -3.284 1.00 35.93 ? 315 VAL A CG1 1 ATOM 2452 C CG2 . VAL A 1 313 ? 28.099 -2.616 -1.135 1.00 36.49 ? 315 VAL A CG2 1 ATOM 2453 N N . LEU A 1 314 ? 26.914 -6.890 -2.860 1.00 34.46 ? 316 LEU A N 1 ATOM 2454 C CA . LEU A 1 314 ? 26.911 -7.943 -3.835 1.00 34.58 ? 316 LEU A CA 1 ATOM 2455 C C . LEU A 1 314 ? 26.625 -7.355 -5.210 1.00 34.56 ? 316 LEU A C 1 ATOM 2456 O O . LEU A 1 314 ? 25.732 -6.512 -5.370 1.00 34.56 ? 316 LEU A O 1 ATOM 2457 C CB . LEU A 1 314 ? 25.805 -8.941 -3.504 1.00 35.18 ? 316 LEU A CB 1 ATOM 2458 C CG . LEU A 1 314 ? 26.092 -10.070 -2.523 1.00 35.88 ? 316 LEU A CG 1 ATOM 2459 C CD1 . LEU A 1 314 ? 24.789 -10.801 -2.256 1.00 38.64 ? 316 LEU A CD1 1 ATOM 2460 C CD2 . LEU A 1 314 ? 27.130 -11.049 -3.048 1.00 35.33 ? 316 LEU A CD2 1 ATOM 2461 N N . ALA A 1 315 ? 27.402 -7.782 -6.195 1.00 34.52 ? 317 ALA A N 1 ATOM 2462 C CA . ALA A 1 315 ? 27.085 -7.500 -7.590 1.00 34.06 ? 317 ALA A CA 1 ATOM 2463 C C . ALA A 1 315 ? 25.871 -8.342 -7.968 1.00 34.09 ? 317 ALA A C 1 ATOM 2464 O O . ALA A 1 315 ? 25.805 -9.535 -7.639 1.00 34.37 ? 317 ALA A O 1 ATOM 2465 C CB . ALA A 1 315 ? 28.271 -7.856 -8.475 1.00 34.28 ? 317 ALA A CB 1 ATOM 2466 N N . THR A 1 316 ? 24.895 -7.720 -8.626 1.00 33.86 ? 318 THR A N 1 ATOM 2467 C CA . THR A 1 316 ? 23.795 -8.479 -9.208 1.00 33.41 ? 318 THR A CA 1 ATOM 2468 C C . THR A 1 316 ? 23.796 -8.303 -10.730 1.00 33.75 ? 318 THR A C 1 ATOM 2469 O O . THR A 1 316 ? 23.591 -9.269 -11.466 1.00 33.97 ? 318 THR A O 1 ATOM 2470 C CB . THR A 1 316 ? 22.415 -8.096 -8.614 1.00 33.37 ? 318 THR A CB 1 ATOM 2471 O OG1 . THR A 1 316 ? 22.211 -6.693 -8.757 1.00 32.13 ? 318 THR A OG1 1 ATOM 2472 C CG2 . THR A 1 316 ? 22.326 -8.488 -7.123 1.00 33.16 ? 318 THR A CG2 1 ATOM 2473 N N . GLY A 1 317 ? 24.027 -7.074 -11.183 1.00 33.77 ? 319 GLY A N 1 ATOM 2474 C CA . GLY A 1 317 ? 24.167 -6.782 -12.617 1.00 33.91 ? 319 GLY A CA 1 ATOM 2475 C C . GLY A 1 317 ? 25.561 -7.047 -13.148 1.00 34.49 ? 319 GLY A C 1 ATOM 2476 O O . GLY A 1 317 ? 26.371 -7.732 -12.513 1.00 33.39 ? 319 GLY A O 1 ATOM 2477 N N . LEU A 1 318 ? 25.849 -6.506 -14.333 1.00 35.00 ? 320 LEU A N 1 ATOM 2478 C CA . LEU A 1 318 ? 27.126 -6.776 -14.981 1.00 35.10 ? 320 LEU A CA 1 ATOM 2479 C C . LEU A 1 318 ? 27.980 -5.523 -14.881 1.00 34.95 ? 320 LEU A C 1 ATOM 2480 O O . LEU A 1 318 ? 27.516 -4.484 -14.421 1.00 34.14 ? 320 LEU A O 1 ATOM 2481 C CB . LEU A 1 318 ? 26.930 -7.189 -16.451 1.00 35.76 ? 320 LEU A CB 1 ATOM 2482 C CG . LEU A 1 318 ? 26.123 -6.246 -17.354 1.00 37.28 ? 320 LEU A CG 1 ATOM 2483 C CD1 . LEU A 1 318 ? 26.557 -6.447 -18.781 1.00 40.50 ? 320 LEU A CD1 1 ATOM 2484 C CD2 . LEU A 1 318 ? 24.647 -6.522 -17.223 1.00 36.93 ? 320 LEU A CD2 1 ATOM 2485 N N . ARG A 1 319 ? 29.232 -5.647 -15.299 1.00 35.33 ? 321 ARG A N 1 ATOM 2486 C CA . ARG A 1 319 ? 30.144 -4.533 -15.423 1.00 37.05 ? 321 ARG A CA 1 ATOM 2487 C C . ARG A 1 319 ? 29.502 -3.447 -16.287 1.00 38.35 ? 321 ARG A C 1 ATOM 2488 O O . ARG A 1 319 ? 29.019 -3.736 -17.402 1.00 38.29 ? 321 ARG A O 1 ATOM 2489 C CB . ARG A 1 319 ? 31.397 -5.041 -16.096 1.00 37.55 ? 321 ARG A CB 1 ATOM 2490 C CG . ARG A 1 319 ? 32.645 -4.673 -15.423 1.00 39.66 ? 321 ARG A CG 1 ATOM 2491 C CD . ARG A 1 319 ? 33.768 -5.343 -16.123 1.00 43.26 ? 321 ARG A CD 1 ATOM 2492 N NE . ARG A 1 319 ? 34.350 -6.378 -15.291 1.00 46.58 ? 321 ARG A NE 1 ATOM 2493 C CZ . ARG A 1 319 ? 35.388 -6.162 -14.511 1.00 44.73 ? 321 ARG A CZ 1 ATOM 2494 N NH1 . ARG A 1 319 ? 35.918 -4.946 -14.492 1.00 47.31 ? 321 ARG A NH1 1 ATOM 2495 N NH2 . ARG A 1 319 ? 35.882 -7.139 -13.768 1.00 42.87 ? 321 ARG A NH2 1 ATOM 2496 N N . ASN A 1 320 ? 29.465 -2.229 -15.760 1.00 39.03 ? 322 ASN A N 1 ATOM 2497 C CA . ASN A 1 320 ? 28.872 -1.100 -16.453 1.00 41.61 ? 322 ASN A CA 1 ATOM 2498 C C . ASN A 1 320 ? 29.925 -0.437 -17.303 1.00 43.71 ? 322 ASN A C 1 ATOM 2499 O O . ASN A 1 320 ? 30.783 0.270 -16.777 1.00 43.49 ? 322 ASN A O 1 ATOM 2500 C CB . ASN A 1 320 ? 28.271 -0.091 -15.472 1.00 40.87 ? 322 ASN A CB 1 ATOM 2501 C CG . ASN A 1 320 ? 27.311 0.868 -16.142 1.00 41.64 ? 322 ASN A CG 1 ATOM 2502 O OD1 . ASN A 1 320 ? 26.733 0.566 -17.193 1.00 37.99 ? 322 ASN A OD1 1 ATOM 2503 N ND2 . ASN A 1 320 ? 27.124 2.037 -15.527 1.00 41.99 ? 322 ASN A ND2 1 ATOM 2504 N N . VAL A 1 321 ? 29.862 -0.694 -18.612 1.00 46.10 ? 323 VAL A N 1 ATOM 2505 C CA . VAL A 1 321 ? 30.921 -0.318 -19.545 1.00 49.11 ? 323 VAL A CA 1 ATOM 2506 C C . VAL A 1 321 ? 30.476 0.872 -20.399 1.00 52.22 ? 323 VAL A C 1 ATOM 2507 O O . VAL A 1 321 ? 29.472 0.775 -21.122 1.00 52.78 ? 323 VAL A O 1 ATOM 2508 C CB . VAL A 1 321 ? 31.316 -1.498 -20.479 1.00 49.18 ? 323 VAL A CB 1 ATOM 2509 C CG1 . VAL A 1 321 ? 32.493 -1.118 -21.348 1.00 49.02 ? 323 VAL A CG1 1 ATOM 2510 C CG2 . VAL A 1 321 ? 31.639 -2.749 -19.675 1.00 48.07 ? 323 VAL A CG2 1 ATOM 2511 N N . PRO A 1 322 ? 31.222 1.997 -20.315 1.00 54.81 ? 324 PRO A N 1 ATOM 2512 C CA . PRO A 1 322 ? 31.016 3.211 -21.139 1.00 56.71 ? 324 PRO A CA 1 ATOM 2513 C C . PRO A 1 322 ? 30.725 2.930 -22.633 1.00 59.07 ? 324 PRO A C 1 ATOM 2514 O O . PRO A 1 322 ? 31.323 2.017 -23.233 1.00 59.48 ? 324 PRO A O 1 ATOM 2515 C CB . PRO A 1 322 ? 32.349 3.949 -20.997 1.00 56.57 ? 324 PRO A CB 1 ATOM 2516 C CG . PRO A 1 322 ? 32.837 3.565 -19.616 1.00 55.84 ? 324 PRO A CG 1 ATOM 2517 C CD . PRO A 1 322 ? 32.379 2.139 -19.400 1.00 54.54 ? 324 PRO A CD 1 ATOM 2518 N N . GLN A 1 323 ? 29.819 3.718 -23.217 1.00 61.24 ? 325 GLN A N 1 ATOM 2519 C CA . GLN A 1 323 ? 29.440 3.605 -24.646 1.00 63.76 ? 325 GLN A CA 1 ATOM 2520 C C . GLN A 1 323 ? 30.636 3.674 -25.631 1.00 64.72 ? 325 GLN A C 1 ATOM 2521 O O . GLN A 1 323 ? 31.716 4.172 -25.276 1.00 65.18 ? 325 GLN A O 1 ATOM 2522 C CB . GLN A 1 323 ? 28.372 4.670 -24.992 1.00 64.23 ? 325 GLN A CB 1 ATOM 2523 C CG . GLN A 1 323 ? 28.885 6.123 -25.207 1.00 66.23 ? 325 GLN A CG 1 ATOM 2524 C CD . GLN A 1 323 ? 29.758 6.671 -24.069 1.00 68.67 ? 325 GLN A CD 1 ATOM 2525 O OE1 . GLN A 1 323 ? 29.793 6.128 -22.959 1.00 69.01 ? 325 GLN A OE1 1 ATOM 2526 N NE2 . GLN A 1 323 ? 30.466 7.760 -24.351 1.00 69.95 ? 325 GLN A NE2 1 ATOM 2527 N N . ILE A 1 324 ? 30.447 3.156 -26.849 1.00 65.60 ? 326 ILE A N 1 ATOM 2528 C CA . ILE A 1 324 ? 31.424 3.342 -27.938 1.00 66.34 ? 326 ILE A CA 1 ATOM 2529 C C . ILE A 1 324 ? 30.898 4.344 -28.965 1.00 66.53 ? 326 ILE A C 1 ATOM 2530 O O . ILE A 1 324 ? 30.606 5.494 -28.626 1.00 66.82 ? 326 ILE A O 1 ATOM 2531 C CB . ILE A 1 324 ? 31.819 2.005 -28.636 1.00 66.66 ? 326 ILE A CB 1 ATOM 2532 C CG1 . ILE A 1 324 ? 32.691 1.129 -27.718 1.00 66.58 ? 326 ILE A CG1 1 ATOM 2533 C CG2 . ILE A 1 324 ? 32.517 2.264 -29.988 1.00 67.57 ? 326 ILE A CG2 1 ATOM 2534 C CD1 . ILE A 1 324 ? 33.839 1.857 -26.979 1.00 66.07 ? 326 ILE A CD1 1 ATOM 2535 N N . GLY B 2 1 ? 37.320 -9.691 -19.126 1.00 34.10 ? 1 GLY B N 1 ATOM 2536 C CA . GLY B 2 1 ? 36.855 -10.729 -18.172 1.00 31.67 ? 1 GLY B CA 1 ATOM 2537 C C . GLY B 2 1 ? 37.095 -12.113 -18.707 1.00 31.37 ? 1 GLY B C 1 ATOM 2538 O O . GLY B 2 1 ? 37.633 -12.303 -19.818 1.00 32.08 ? 1 GLY B O 1 ATOM 2539 N N . LEU B 2 2 ? 36.643 -13.087 -17.945 1.00 30.62 ? 2 LEU B N 1 ATOM 2540 C CA . LEU B 2 2 ? 37.043 -14.469 -18.154 1.00 31.31 ? 2 LEU B CA 1 ATOM 2541 C C . LEU B 2 2 ? 36.578 -15.013 -19.487 1.00 30.80 ? 2 LEU B C 1 ATOM 2542 O O . LEU B 2 2 ? 37.281 -15.803 -20.092 1.00 31.92 ? 2 LEU B O 1 ATOM 2543 C CB . LEU B 2 2 ? 36.502 -15.332 -17.013 1.00 30.97 ? 2 LEU B CB 1 ATOM 2544 C CG . LEU B 2 2 ? 37.363 -16.449 -16.427 1.00 31.99 ? 2 LEU B CG 1 ATOM 2545 C CD1 . LEU B 2 2 ? 38.801 -16.015 -16.065 1.00 29.91 ? 2 LEU B CD1 1 ATOM 2546 C CD2 . LEU B 2 2 ? 36.645 -17.048 -15.224 1.00 30.19 ? 2 LEU B CD2 1 ATOM 2547 N N . PHE B 2 3 ? 35.404 -14.575 -19.946 1.00 29.96 ? 3 PHE B N 1 ATOM 2548 C CA . PHE B 2 3 ? 34.842 -15.115 -21.185 1.00 30.27 ? 3 PHE B CA 1 ATOM 2549 C C . PHE B 2 3 ? 35.052 -14.244 -22.425 1.00 30.59 ? 3 PHE B C 1 ATOM 2550 O O . PHE B 2 3 ? 34.622 -14.586 -23.517 1.00 31.47 ? 3 PHE B O 1 ATOM 2551 C CB . PHE B 2 3 ? 33.390 -15.569 -20.955 1.00 28.97 ? 3 PHE B CB 1 ATOM 2552 C CG . PHE B 2 3 ? 33.305 -16.751 -20.033 1.00 29.43 ? 3 PHE B CG 1 ATOM 2553 C CD1 . PHE B 2 3 ? 33.427 -18.051 -20.539 1.00 29.45 ? 3 PHE B CD1 1 ATOM 2554 C CD2 . PHE B 2 3 ? 33.202 -16.576 -18.662 1.00 28.04 ? 3 PHE B CD2 1 ATOM 2555 C CE1 . PHE B 2 3 ? 33.384 -19.154 -19.703 1.00 29.53 ? 3 PHE B CE1 1 ATOM 2556 C CE2 . PHE B 2 3 ? 33.187 -17.673 -17.808 1.00 26.98 ? 3 PHE B CE2 1 ATOM 2557 C CZ . PHE B 2 3 ? 33.275 -18.963 -18.322 1.00 27.16 ? 3 PHE B CZ 1 ATOM 2558 N N . GLY B 2 4 ? 35.736 -13.120 -22.242 1.00 31.12 ? 4 GLY B N 1 ATOM 2559 C CA . GLY B 2 4 ? 36.201 -12.305 -23.352 1.00 31.77 ? 4 GLY B CA 1 ATOM 2560 C C . GLY B 2 4 ? 35.186 -11.472 -24.109 1.00 31.48 ? 4 GLY B C 1 ATOM 2561 O O . GLY B 2 4 ? 35.556 -10.820 -25.090 1.00 32.72 ? 4 GLY B O 1 ATOM 2562 N N . ALA B 2 5 ? 33.924 -11.485 -23.692 1.00 30.12 ? 5 ALA B N 1 ATOM 2563 C CA . ALA B 2 5 ? 32.896 -10.733 -24.406 1.00 30.17 ? 5 ALA B CA 1 ATOM 2564 C C . ALA B 2 5 ? 32.666 -9.329 -23.847 1.00 30.89 ? 5 ALA B C 1 ATOM 2565 O O . ALA B 2 5 ? 32.869 -8.346 -24.550 1.00 31.50 ? 5 ALA B O 1 ATOM 2566 C CB . ALA B 2 5 ? 31.573 -11.532 -24.492 1.00 29.29 ? 5 ALA B CB 1 ATOM 2567 N N . ILE B 2 6 ? 32.276 -9.242 -22.583 1.00 30.94 ? 6 ILE B N 1 ATOM 2568 C CA . ILE B 2 6 ? 31.997 -7.950 -21.928 1.00 32.13 ? 6 ILE B CA 1 ATOM 2569 C C . ILE B 2 6 ? 33.286 -7.173 -21.749 1.00 33.09 ? 6 ILE B C 1 ATOM 2570 O O . ILE B 2 6 ? 34.282 -7.734 -21.301 1.00 32.72 ? 6 ILE B O 1 ATOM 2571 C CB . ILE B 2 6 ? 31.273 -8.149 -20.573 1.00 31.50 ? 6 ILE B CB 1 ATOM 2572 C CG1 . ILE B 2 6 ? 29.872 -8.718 -20.816 1.00 31.02 ? 6 ILE B CG1 1 ATOM 2573 C CG2 . ILE B 2 6 ? 31.186 -6.834 -19.791 1.00 33.20 ? 6 ILE B CG2 1 ATOM 2574 C CD1 . ILE B 2 6 ? 29.173 -9.135 -19.542 1.00 31.78 ? 6 ILE B CD1 1 ATOM 2575 N N . ALA B 2 7 ? 33.261 -5.886 -22.117 1.00 34.31 ? 7 ALA B N 1 ATOM 2576 C CA . ALA B 2 7 ? 34.482 -5.081 -22.239 1.00 35.62 ? 7 ALA B CA 1 ATOM 2577 C C . ALA B 2 7 ? 35.584 -5.856 -22.979 1.00 35.85 ? 7 ALA B C 1 ATOM 2578 O O . ALA B 2 7 ? 36.763 -5.782 -22.626 1.00 36.07 ? 7 ALA B O 1 ATOM 2579 C CB . ALA B 2 7 ? 34.963 -4.600 -20.859 1.00 36.36 ? 7 ALA B CB 1 ATOM 2580 N N . GLY B 2 8 ? 35.178 -6.618 -24.000 1.00 35.34 ? 8 GLY B N 1 ATOM 2581 C CA . GLY B 2 8 ? 36.069 -7.532 -24.702 1.00 35.07 ? 8 GLY B CA 1 ATOM 2582 C C . GLY B 2 8 ? 35.913 -7.324 -26.185 1.00 35.61 ? 8 GLY B C 1 ATOM 2583 O O . GLY B 2 8 ? 36.099 -6.204 -26.670 1.00 36.19 ? 8 GLY B O 1 ATOM 2584 N N . PHE B 2 9 ? 35.543 -8.381 -26.913 1.00 34.84 ? 9 PHE B N 1 ATOM 2585 C CA . PHE B 2 9 ? 35.304 -8.223 -28.351 1.00 35.69 ? 9 PHE B CA 1 ATOM 2586 C C . PHE B 2 9 ? 34.026 -7.416 -28.558 1.00 35.11 ? 9 PHE B C 1 ATOM 2587 O O . PHE B 2 9 ? 33.881 -6.740 -29.572 1.00 35.44 ? 9 PHE B O 1 ATOM 2588 C CB . PHE B 2 9 ? 35.322 -9.550 -29.149 1.00 34.78 ? 9 PHE B CB 1 ATOM 2589 C CG . PHE B 2 9 ? 34.140 -10.460 -28.892 1.00 35.62 ? 9 PHE B CG 1 ATOM 2590 C CD1 . PHE B 2 9 ? 32.957 -10.319 -29.617 1.00 35.98 ? 9 PHE B CD1 1 ATOM 2591 C CD2 . PHE B 2 9 ? 34.243 -11.506 -27.990 1.00 33.72 ? 9 PHE B CD2 1 ATOM 2592 C CE1 . PHE B 2 9 ? 31.868 -11.179 -29.401 1.00 35.73 ? 9 PHE B CE1 1 ATOM 2593 C CE2 . PHE B 2 9 ? 33.156 -12.359 -27.761 1.00 35.96 ? 9 PHE B CE2 1 ATOM 2594 C CZ . PHE B 2 9 ? 31.968 -12.193 -28.459 1.00 33.51 ? 9 PHE B CZ 1 ATOM 2595 N N . ILE B 2 10 ? 33.113 -7.465 -27.585 1.00 33.98 ? 10 ILE B N 1 ATOM 2596 C CA . ILE B 2 10 ? 32.002 -6.524 -27.604 1.00 34.28 ? 10 ILE B CA 1 ATOM 2597 C C . ILE B 2 10 ? 32.441 -5.382 -26.698 1.00 35.41 ? 10 ILE B C 1 ATOM 2598 O O . ILE B 2 10 ? 32.337 -5.466 -25.463 1.00 34.37 ? 10 ILE B O 1 ATOM 2599 C CB . ILE B 2 10 ? 30.634 -7.150 -27.205 1.00 33.28 ? 10 ILE B CB 1 ATOM 2600 C CG1 . ILE B 2 10 ? 30.365 -8.417 -28.027 1.00 33.30 ? 10 ILE B CG1 1 ATOM 2601 C CG2 . ILE B 2 10 ? 29.526 -6.141 -27.426 1.00 33.28 ? 10 ILE B CG2 1 ATOM 2602 C CD1 . ILE B 2 10 ? 29.097 -9.166 -27.638 1.00 31.47 ? 10 ILE B CD1 1 ATOM 2603 N N . GLU B 2 11 ? 32.947 -4.326 -27.336 1.00 36.95 ? 11 GLU B N 1 ATOM 2604 C CA . GLU B 2 11 ? 33.696 -3.256 -26.667 1.00 39.02 ? 11 GLU B CA 1 ATOM 2605 C C . GLU B 2 11 ? 32.942 -2.484 -25.593 1.00 39.12 ? 11 GLU B C 1 ATOM 2606 O O . GLU B 2 11 ? 33.516 -2.152 -24.552 1.00 40.45 ? 11 GLU B O 1 ATOM 2607 C CB . GLU B 2 11 ? 34.209 -2.259 -27.693 1.00 40.90 ? 11 GLU B CB 1 ATOM 2608 C CG . GLU B 2 11 ? 35.379 -2.721 -28.490 1.00 45.03 ? 11 GLU B CG 1 ATOM 2609 C CD . GLU B 2 11 ? 36.063 -1.550 -29.152 1.00 51.72 ? 11 GLU B CD 1 ATOM 2610 O OE1 . GLU B 2 11 ? 37.109 -1.100 -28.628 1.00 56.53 ? 11 GLU B OE1 1 ATOM 2611 O OE2 . GLU B 2 11 ? 35.529 -1.041 -30.163 1.00 55.09 ? 11 GLU B OE2 1 ATOM 2612 N N . GLY B 2 12 ? 31.673 -2.182 -25.836 1.00 38.47 ? 12 GLY B N 1 ATOM 2613 C CA . GLY B 2 12 ? 30.914 -1.395 -24.873 1.00 39.25 ? 12 GLY B CA 1 ATOM 2614 C C . GLY B 2 12 ? 29.504 -1.890 -24.680 1.00 38.44 ? 12 GLY B C 1 ATOM 2615 O O . GLY B 2 12 ? 29.010 -2.703 -25.456 1.00 37.71 ? 12 GLY B O 1 ATOM 2616 N N . GLY B 2 13 ? 28.863 -1.399 -23.631 1.00 38.66 ? 13 GLY B N 1 ATOM 2617 C CA . GLY B 2 13 ? 27.464 -1.693 -23.368 1.00 38.77 ? 13 GLY B CA 1 ATOM 2618 C C . GLY B 2 13 ? 26.554 -0.731 -24.098 1.00 40.36 ? 13 GLY B C 1 ATOM 2619 O O . GLY B 2 13 ? 27.018 0.279 -24.643 1.00 41.68 ? 13 GLY B O 1 ATOM 2620 N N . TRP B 2 14 ? 25.260 -1.049 -24.106 1.00 40.63 ? 14 TRP B N 1 ATOM 2621 C CA . TRP B 2 14 ? 24.264 -0.247 -24.797 1.00 42.60 ? 14 TRP B CA 1 ATOM 2622 C C . TRP B 2 14 ? 23.316 0.458 -23.830 1.00 44.32 ? 14 TRP B C 1 ATOM 2623 O O . TRP B 2 14 ? 22.501 -0.196 -23.168 1.00 44.05 ? 14 TRP B O 1 ATOM 2624 C CB . TRP B 2 14 ? 23.425 -1.122 -25.725 1.00 41.45 ? 14 TRP B CB 1 ATOM 2625 C CG . TRP B 2 14 ? 24.113 -1.691 -26.897 1.00 40.58 ? 14 TRP B CG 1 ATOM 2626 C CD1 . TRP B 2 14 ? 25.192 -1.174 -27.560 1.00 40.34 ? 14 TRP B CD1 1 ATOM 2627 C CD2 . TRP B 2 14 ? 23.738 -2.887 -27.602 1.00 39.67 ? 14 TRP B CD2 1 ATOM 2628 N NE1 . TRP B 2 14 ? 25.521 -1.986 -28.624 1.00 38.88 ? 14 TRP B NE1 1 ATOM 2629 C CE2 . TRP B 2 14 ? 24.649 -3.045 -28.670 1.00 37.49 ? 14 TRP B CE2 1 ATOM 2630 C CE3 . TRP B 2 14 ? 22.728 -3.849 -27.423 1.00 39.35 ? 14 TRP B CE3 1 ATOM 2631 C CZ2 . TRP B 2 14 ? 24.586 -4.127 -29.559 1.00 36.57 ? 14 TRP B CZ2 1 ATOM 2632 C CZ3 . TRP B 2 14 ? 22.656 -4.926 -28.322 1.00 39.39 ? 14 TRP B CZ3 1 ATOM 2633 C CH2 . TRP B 2 14 ? 23.585 -5.052 -29.376 1.00 35.43 ? 14 TRP B CH2 1 ATOM 2634 N N . GLN B 2 15 ? 23.408 1.789 -23.775 1.00 46.54 ? 15 GLN B N 1 ATOM 2635 C CA . GLN B 2 15 ? 22.487 2.620 -22.993 1.00 48.35 ? 15 GLN B CA 1 ATOM 2636 C C . GLN B 2 15 ? 21.060 2.497 -23.515 1.00 48.54 ? 15 GLN B C 1 ATOM 2637 O O . GLN B 2 15 ? 20.111 2.540 -22.737 1.00 48.42 ? 15 GLN B O 1 ATOM 2638 C CB . GLN B 2 15 ? 22.916 4.099 -23.012 1.00 50.54 ? 15 GLN B CB 1 ATOM 2639 C CG . GLN B 2 15 ? 24.241 4.417 -22.312 1.00 52.58 ? 15 GLN B CG 1 ATOM 2640 C CD . GLN B 2 15 ? 24.115 4.556 -20.796 1.00 55.49 ? 15 GLN B CD 1 ATOM 2641 O OE1 . GLN B 2 15 ? 23.204 5.216 -20.280 1.00 57.65 ? 15 GLN B OE1 1 ATOM 2642 N NE2 . GLN B 2 15 ? 25.046 3.952 -20.079 1.00 55.86 ? 15 GLN B NE2 1 ATOM 2643 N N . GLY B 2 16 ? 20.919 2.347 -24.834 1.00 48.87 ? 16 GLY B N 1 ATOM 2644 C CA . GLY B 2 16 ? 19.616 2.273 -25.483 1.00 50.16 ? 16 GLY B CA 1 ATOM 2645 C C . GLY B 2 16 ? 18.873 0.958 -25.321 1.00 49.54 ? 16 GLY B C 1 ATOM 2646 O O . GLY B 2 16 ? 17.712 0.851 -25.715 1.00 50.23 ? 16 GLY B O 1 ATOM 2647 N N . MET B 2 17 ? 19.527 -0.058 -24.761 1.00 48.57 ? 17 MET B N 1 ATOM 2648 C CA . MET B 2 17 ? 18.820 -1.304 -24.451 1.00 48.33 ? 17 MET B CA 1 ATOM 2649 C C . MET B 2 17 ? 18.414 -1.346 -22.993 1.00 48.97 ? 17 MET B C 1 ATOM 2650 O O . MET B 2 17 ? 19.148 -1.852 -22.129 1.00 47.63 ? 17 MET B O 1 ATOM 2651 C CB . MET B 2 17 ? 19.641 -2.536 -24.789 1.00 46.51 ? 17 MET B CB 1 ATOM 2652 C CG . MET B 2 17 ? 18.843 -3.814 -24.612 1.00 46.79 ? 17 MET B CG 1 ATOM 2653 S SD . MET B 2 17 ? 19.794 -5.249 -25.107 1.00 47.08 ? 17 MET B SD 1 ATOM 2654 C CE . MET B 2 17 ? 20.964 -5.327 -23.735 1.00 44.38 ? 17 MET B CE 1 ATOM 2655 N N . VAL B 2 18 ? 17.220 -0.837 -22.734 1.00 51.13 ? 18 VAL B N 1 ATOM 2656 C CA . VAL B 2 18 ? 16.783 -0.601 -21.372 1.00 52.27 ? 18 VAL B CA 1 ATOM 2657 C C . VAL B 2 18 ? 15.981 -1.729 -20.740 1.00 51.72 ? 18 VAL B C 1 ATOM 2658 O O . VAL B 2 18 ? 15.763 -1.710 -19.530 1.00 52.39 ? 18 VAL B O 1 ATOM 2659 C CB . VAL B 2 18 ? 15.984 0.725 -21.266 1.00 54.60 ? 18 VAL B CB 1 ATOM 2660 C CG1 . VAL B 2 18 ? 16.865 1.896 -21.674 1.00 56.09 ? 18 VAL B CG1 1 ATOM 2661 C CG2 . VAL B 2 18 ? 14.718 0.664 -22.122 1.00 55.95 ? 18 VAL B CG2 1 ATOM 2662 N N . ASP B 2 19 ? 15.541 -2.708 -21.529 1.00 51.31 ? 19 ASP B N 1 ATOM 2663 C CA . ASP B 2 19 ? 14.636 -3.738 -20.977 1.00 51.49 ? 19 ASP B CA 1 ATOM 2664 C C . ASP B 2 19 ? 15.225 -5.149 -20.771 1.00 48.79 ? 19 ASP B C 1 ATOM 2665 O O . ASP B 2 19 ? 14.496 -6.148 -20.760 1.00 48.94 ? 19 ASP B O 1 ATOM 2666 C CB . ASP B 2 19 ? 13.293 -3.776 -21.734 1.00 53.36 ? 19 ASP B CB 1 ATOM 2667 C CG . ASP B 2 19 ? 13.432 -4.223 -23.168 1.00 55.25 ? 19 ASP B CG 1 ATOM 2668 O OD1 . ASP B 2 19 ? 14.571 -4.478 -23.623 1.00 57.81 ? 19 ASP B OD1 1 ATOM 2669 O OD2 . ASP B 2 19 ? 12.386 -4.296 -23.858 1.00 58.89 ? 19 ASP B OD2 1 ATOM 2670 N N . GLY B 2 20 ? 16.536 -5.222 -20.573 1.00 46.20 ? 20 GLY B N 1 ATOM 2671 C CA . GLY B 2 20 ? 17.166 -6.475 -20.185 1.00 43.26 ? 20 GLY B CA 1 ATOM 2672 C C . GLY B 2 20 ? 18.674 -6.393 -20.139 1.00 41.30 ? 20 GLY B C 1 ATOM 2673 O O . GLY B 2 20 ? 19.252 -5.359 -20.453 1.00 41.90 ? 20 GLY B O 1 ATOM 2674 N N . TRP B 2 21 ? 19.319 -7.496 -19.775 1.00 38.69 ? 21 TRP B N 1 ATOM 2675 C CA . TRP B 2 21 ? 20.760 -7.487 -19.586 1.00 36.35 ? 21 TRP B CA 1 ATOM 2676 C C . TRP B 2 21 ? 21.535 -7.738 -20.865 1.00 34.60 ? 21 TRP B C 1 ATOM 2677 O O . TRP B 2 21 ? 22.616 -7.199 -21.048 1.00 33.36 ? 21 TRP B O 1 ATOM 2678 C CB . TRP B 2 21 ? 21.168 -8.522 -18.538 1.00 36.24 ? 21 TRP B CB 1 ATOM 2679 C CG . TRP B 2 21 ? 21.104 -8.052 -17.120 1.00 38.06 ? 21 TRP B CG 1 ATOM 2680 C CD1 . TRP B 2 21 ? 21.316 -6.777 -16.651 1.00 39.93 ? 21 TRP B CD1 1 ATOM 2681 C CD2 . TRP B 2 21 ? 20.853 -8.871 -15.967 1.00 39.15 ? 21 TRP B CD2 1 ATOM 2682 N NE1 . TRP B 2 21 ? 21.211 -6.760 -15.261 1.00 42.29 ? 21 TRP B NE1 1 ATOM 2683 C CE2 . TRP B 2 21 ? 20.923 -8.030 -14.826 1.00 40.20 ? 21 TRP B CE2 1 ATOM 2684 C CE3 . TRP B 2 21 ? 20.585 -10.238 -15.787 1.00 37.72 ? 21 TRP B CE3 1 ATOM 2685 C CZ2 . TRP B 2 21 ? 20.717 -8.510 -13.533 1.00 38.85 ? 21 TRP B CZ2 1 ATOM 2686 C CZ3 . TRP B 2 21 ? 20.375 -10.713 -14.494 1.00 37.78 ? 21 TRP B CZ3 1 ATOM 2687 C CH2 . TRP B 2 21 ? 20.442 -9.849 -13.388 1.00 38.05 ? 21 TRP B CH2 1 ATOM 2688 N N . TYR B 2 22 ? 20.994 -8.600 -21.716 1.00 33.63 ? 22 TYR B N 1 ATOM 2689 C CA . TYR B 2 22 ? 21.652 -8.971 -22.967 1.00 33.26 ? 22 TYR B CA 1 ATOM 2690 C C . TYR B 2 22 ? 20.626 -8.919 -24.074 1.00 33.89 ? 22 TYR B C 1 ATOM 2691 O O . TYR B 2 22 ? 19.415 -9.048 -23.823 1.00 35.27 ? 22 TYR B O 1 ATOM 2692 C CB . TYR B 2 22 ? 22.231 -10.388 -22.892 1.00 32.18 ? 22 TYR B CB 1 ATOM 2693 C CG . TYR B 2 22 ? 22.579 -10.878 -21.494 1.00 30.56 ? 22 TYR B CG 1 ATOM 2694 C CD1 . TYR B 2 22 ? 23.622 -10.305 -20.771 1.00 29.63 ? 22 TYR B CD1 1 ATOM 2695 C CD2 . TYR B 2 22 ? 21.881 -11.937 -20.917 1.00 31.51 ? 22 TYR B CD2 1 ATOM 2696 C CE1 . TYR B 2 22 ? 23.945 -10.759 -19.468 1.00 31.12 ? 22 TYR B CE1 1 ATOM 2697 C CE2 . TYR B 2 22 ? 22.197 -12.400 -19.629 1.00 29.72 ? 22 TYR B CE2 1 ATOM 2698 C CZ . TYR B 2 22 ? 23.229 -11.807 -18.927 1.00 29.69 ? 22 TYR B CZ 1 ATOM 2699 O OH . TYR B 2 22 ? 23.556 -12.252 -17.682 1.00 30.87 ? 22 TYR B OH 1 ATOM 2700 N N . GLY B 2 23 ? 21.099 -8.704 -25.297 1.00 33.93 ? 23 GLY B N 1 ATOM 2701 C CA . GLY B 2 23 ? 20.206 -8.610 -26.423 1.00 34.58 ? 23 GLY B CA 1 ATOM 2702 C C . GLY B 2 23 ? 20.848 -8.227 -27.740 1.00 35.03 ? 23 GLY B C 1 ATOM 2703 O O . GLY B 2 23 ? 22.037 -8.501 -27.995 1.00 33.44 ? 23 GLY B O 1 ATOM 2704 N N . TYR B 2 24 ? 20.040 -7.568 -28.564 1.00 36.24 ? 24 TYR B N 1 ATOM 2705 C CA . TYR B 2 24 ? 20.361 -7.373 -29.974 1.00 37.19 ? 24 TYR B CA 1 ATOM 2706 C C . TYR B 2 24 ? 20.201 -5.937 -30.431 1.00 38.94 ? 24 TYR B C 1 ATOM 2707 O O . TYR B 2 24 ? 19.329 -5.208 -29.949 1.00 40.05 ? 24 TYR B O 1 ATOM 2708 C CB . TYR B 2 24 ? 19.427 -8.228 -30.840 1.00 37.12 ? 24 TYR B CB 1 ATOM 2709 C CG . TYR B 2 24 ? 19.278 -9.656 -30.393 1.00 37.06 ? 24 TYR B CG 1 ATOM 2710 C CD1 . TYR B 2 24 ? 20.173 -10.642 -30.827 1.00 37.52 ? 24 TYR B CD1 1 ATOM 2711 C CD2 . TYR B 2 24 ? 18.223 -10.038 -29.568 1.00 36.89 ? 24 TYR B CD2 1 ATOM 2712 C CE1 . TYR B 2 24 ? 20.026 -11.970 -30.429 1.00 37.23 ? 24 TYR B CE1 1 ATOM 2713 C CE2 . TYR B 2 24 ? 18.072 -11.353 -29.165 1.00 36.92 ? 24 TYR B CE2 1 ATOM 2714 C CZ . TYR B 2 24 ? 18.979 -12.314 -29.597 1.00 37.93 ? 24 TYR B CZ 1 ATOM 2715 O OH . TYR B 2 24 ? 18.832 -13.620 -29.184 1.00 40.93 ? 24 TYR B OH 1 ATOM 2716 N N . HIS B 2 25 ? 21.031 -5.541 -31.387 1.00 39.91 ? 25 HIS B N 1 ATOM 2717 C CA . HIS B 2 25 ? 20.733 -4.376 -32.201 1.00 41.77 ? 25 HIS B CA 1 ATOM 2718 C C . HIS B 2 25 ? 20.722 -4.869 -33.638 1.00 41.82 ? 25 HIS B C 1 ATOM 2719 O O . HIS B 2 25 ? 21.685 -5.507 -34.071 1.00 41.32 ? 25 HIS B O 1 ATOM 2720 C CB . HIS B 2 25 ? 21.781 -3.275 -32.030 1.00 42.27 ? 25 HIS B CB 1 ATOM 2721 C CG . HIS B 2 25 ? 21.479 -2.032 -32.802 1.00 44.07 ? 25 HIS B CG 1 ATOM 2722 N ND1 . HIS B 2 25 ? 20.735 -0.993 -32.282 1.00 46.17 ? 25 HIS B ND1 1 ATOM 2723 C CD2 . HIS B 2 25 ? 21.804 -1.665 -34.064 1.00 45.03 ? 25 HIS B CD2 1 ATOM 2724 C CE1 . HIS B 2 25 ? 20.626 -0.036 -33.185 1.00 46.66 ? 25 HIS B CE1 1 ATOM 2725 N NE2 . HIS B 2 25 ? 21.256 -0.424 -34.279 1.00 45.72 ? 25 HIS B NE2 1 ATOM 2726 N N . HIS B 2 26 ? 19.634 -4.598 -34.358 1.00 42.95 ? 26 HIS B N 1 ATOM 2727 C CA . HIS B 2 26 ? 19.520 -4.981 -35.776 1.00 43.66 ? 26 HIS B CA 1 ATOM 2728 C C . HIS B 2 26 ? 19.506 -3.745 -36.673 1.00 45.63 ? 26 HIS B C 1 ATOM 2729 O O . HIS B 2 26 ? 19.122 -2.647 -36.248 1.00 45.85 ? 26 HIS B O 1 ATOM 2730 C CB . HIS B 2 26 ? 18.231 -5.772 -36.036 1.00 43.69 ? 26 HIS B CB 1 ATOM 2731 C CG . HIS B 2 26 ? 17.007 -4.909 -36.097 1.00 46.56 ? 26 HIS B CG 1 ATOM 2732 N ND1 . HIS B 2 26 ? 16.273 -4.577 -34.975 1.00 47.73 ? 26 HIS B ND1 1 ATOM 2733 C CD2 . HIS B 2 26 ? 16.411 -4.277 -37.139 1.00 48.10 ? 26 HIS B CD2 1 ATOM 2734 C CE1 . HIS B 2 26 ? 15.268 -3.793 -35.326 1.00 50.32 ? 26 HIS B CE1 1 ATOM 2735 N NE2 . HIS B 2 26 ? 15.333 -3.590 -36.632 1.00 50.92 ? 26 HIS B NE2 1 ATOM 2736 N N . SER B 2 27 ? 19.869 -3.952 -37.936 1.00 46.10 ? 27 SER B N 1 ATOM 2737 C CA . SER B 2 27 ? 19.894 -2.880 -38.898 1.00 48.28 ? 27 SER B CA 1 ATOM 2738 C C . SER B 2 27 ? 19.543 -3.471 -40.257 1.00 48.20 ? 27 SER B C 1 ATOM 2739 O O . SER B 2 27 ? 20.264 -4.335 -40.752 1.00 47.65 ? 27 SER B O 1 ATOM 2740 C CB . SER B 2 27 ? 21.292 -2.257 -38.914 1.00 48.45 ? 27 SER B CB 1 ATOM 2741 O OG . SER B 2 27 ? 21.314 -1.070 -39.675 1.00 51.61 ? 27 SER B OG 1 ATOM 2742 N N . ASN B 2 28 ? 18.416 -3.040 -40.831 1.00 49.78 ? 28 ASN B N 1 ATOM 2743 C CA . ASN B 2 28 ? 18.024 -3.449 -42.192 1.00 50.25 ? 28 ASN B CA 1 ATOM 2744 C C . ASN B 2 28 ? 17.393 -2.306 -43.015 1.00 52.05 ? 28 ASN B C 1 ATOM 2745 O O . ASN B 2 28 ? 17.524 -1.134 -42.635 1.00 53.04 ? 28 ASN B O 1 ATOM 2746 C CB . ASN B 2 28 ? 17.152 -4.722 -42.169 1.00 49.08 ? 28 ASN B CB 1 ATOM 2747 C CG . ASN B 2 28 ? 15.888 -4.558 -41.368 1.00 50.08 ? 28 ASN B CG 1 ATOM 2748 O OD1 . ASN B 2 28 ? 15.406 -3.448 -41.168 1.00 54.33 ? 28 ASN B OD1 1 ATOM 2749 N ND2 . ASN B 2 28 ? 15.329 -5.672 -40.910 1.00 49.46 ? 28 ASN B ND2 1 ATOM 2750 N N . ASP B 2 29 ? 16.735 -2.644 -44.130 1.00 52.82 ? 29 ASP B N 1 ATOM 2751 C CA . ASP B 2 29 ? 16.025 -1.646 -44.963 1.00 55.27 ? 29 ASP B CA 1 ATOM 2752 C C . ASP B 2 29 ? 14.862 -0.981 -44.218 1.00 56.62 ? 29 ASP B C 1 ATOM 2753 O O . ASP B 2 29 ? 14.633 0.212 -44.370 1.00 58.37 ? 29 ASP B O 1 ATOM 2754 C CB . ASP B 2 29 ? 15.517 -2.259 -46.281 1.00 55.43 ? 29 ASP B CB 1 ATOM 2755 C CG . ASP B 2 29 ? 16.620 -2.439 -47.315 1.00 57.01 ? 29 ASP B CG 1 ATOM 2756 O OD1 . ASP B 2 29 ? 17.667 -1.761 -47.215 1.00 58.95 ? 29 ASP B OD1 1 ATOM 2757 O OD2 . ASP B 2 29 ? 16.434 -3.255 -48.251 1.00 59.28 ? 29 ASP B OD2 1 ATOM 2758 N N . GLN B 2 30 ? 14.145 -1.758 -43.404 1.00 56.61 ? 30 GLN B N 1 ATOM 2759 C CA . GLN B 2 30 ? 13.035 -1.243 -42.596 1.00 57.62 ? 30 GLN B CA 1 ATOM 2760 C C . GLN B 2 30 ? 13.476 -0.287 -41.489 1.00 57.96 ? 30 GLN B C 1 ATOM 2761 O O . GLN B 2 30 ? 12.647 0.428 -40.937 1.00 59.77 ? 30 GLN B O 1 ATOM 2762 C CB . GLN B 2 30 ? 12.237 -2.396 -41.985 1.00 57.50 ? 30 GLN B CB 1 ATOM 2763 C CG . GLN B 2 30 ? 11.281 -3.069 -42.941 1.00 57.81 ? 30 GLN B CG 1 ATOM 2764 C CD . GLN B 2 30 ? 11.178 -4.564 -42.711 1.00 57.70 ? 30 GLN B CD 1 ATOM 2765 O OE1 . GLN B 2 30 ? 12.152 -5.297 -42.879 1.00 56.50 ? 30 GLN B OE1 1 ATOM 2766 N NE2 . GLN B 2 30 ? 9.986 -5.030 -42.344 1.00 58.86 ? 30 GLN B NE2 1 ATOM 2767 N N . GLY B 2 31 ? 14.772 -0.280 -41.163 1.00 56.57 ? 31 GLY B N 1 ATOM 2768 C CA . GLY B 2 31 ? 15.306 0.558 -40.078 1.00 55.90 ? 31 GLY B CA 1 ATOM 2769 C C . GLY B 2 31 ? 16.083 -0.231 -39.032 1.00 53.88 ? 31 GLY B C 1 ATOM 2770 O O . GLY B 2 31 ? 16.491 -1.358 -39.285 1.00 52.45 ? 31 GLY B O 1 ATOM 2771 N N . SER B 2 32 ? 16.279 0.362 -37.854 1.00 53.79 ? 32 SER B N 1 ATOM 2772 C CA . SER B 2 32 ? 17.092 -0.243 -36.797 1.00 51.74 ? 32 SER B CA 1 ATOM 2773 C C . SER B 2 32 ? 16.514 -0.069 -35.388 1.00 51.84 ? 32 SER B C 1 ATOM 2774 O O . SER B 2 32 ? 15.573 0.698 -35.190 1.00 53.34 ? 32 SER B O 1 ATOM 2775 C CB . SER B 2 32 ? 18.523 0.303 -36.870 1.00 51.95 ? 32 SER B CB 1 ATOM 2776 O OG . SER B 2 32 ? 18.556 1.710 -36.720 1.00 52.91 ? 32 SER B OG 1 ATOM 2777 N N . GLY B 2 33 ? 17.077 -0.788 -34.410 1.00 50.10 ? 33 GLY B N 1 ATOM 2778 C CA . GLY B 2 33 ? 16.651 -0.667 -33.008 1.00 49.76 ? 33 GLY B CA 1 ATOM 2779 C C . GLY B 2 33 ? 17.206 -1.745 -32.082 1.00 47.94 ? 33 GLY B C 1 ATOM 2780 O O . GLY B 2 33 ? 17.816 -2.712 -32.540 1.00 46.66 ? 33 GLY B O 1 ATOM 2781 N N . TYR B 2 34 ? 16.990 -1.571 -30.778 1.00 47.80 ? 34 TYR B N 1 ATOM 2782 C CA . TYR B 2 34 ? 17.434 -2.521 -29.752 1.00 46.37 ? 34 TYR B CA 1 ATOM 2783 C C . TYR B 2 34 ? 16.302 -3.434 -29.295 1.00 46.56 ? 34 TYR B C 1 ATOM 2784 O O . TYR B 2 34 ? 15.138 -3.052 -29.339 1.00 48.02 ? 34 TYR B O 1 ATOM 2785 C CB . TYR B 2 34 ? 17.966 -1.774 -28.523 1.00 46.37 ? 34 TYR B CB 1 ATOM 2786 C CG . TYR B 2 34 ? 19.162 -0.900 -28.798 1.00 46.42 ? 34 TYR B CG 1 ATOM 2787 C CD1 . TYR B 2 34 ? 20.447 -1.418 -28.755 1.00 44.51 ? 34 TYR B CD1 1 ATOM 2788 C CD2 . TYR B 2 34 ? 19.005 0.458 -29.094 1.00 49.09 ? 34 TYR B CD2 1 ATOM 2789 C CE1 . TYR B 2 34 ? 21.555 -0.617 -29.000 1.00 44.50 ? 34 TYR B CE1 1 ATOM 2790 C CE2 . TYR B 2 34 ? 20.105 1.271 -29.343 1.00 48.68 ? 34 TYR B CE2 1 ATOM 2791 C CZ . TYR B 2 34 ? 21.378 0.728 -29.291 1.00 47.02 ? 34 TYR B CZ 1 ATOM 2792 O OH . TYR B 2 34 ? 22.475 1.518 -29.536 1.00 45.69 ? 34 TYR B OH 1 ATOM 2793 N N . ALA B 2 35 ? 16.650 -4.636 -28.842 1.00 45.49 ? 35 ALA B N 1 ATOM 2794 C CA . ALA B 2 35 ? 15.703 -5.525 -28.159 1.00 45.65 ? 35 ALA B CA 1 ATOM 2795 C C . ALA B 2 35 ? 16.458 -6.466 -27.229 1.00 44.69 ? 35 ALA B C 1 ATOM 2796 O O . ALA B 2 35 ? 17.494 -7.037 -27.602 1.00 43.40 ? 35 ALA B O 1 ATOM 2797 C CB . ALA B 2 35 ? 14.853 -6.319 -29.165 1.00 45.39 ? 35 ALA B CB 1 ATOM 2798 N N . ALA B 2 36 ? 15.940 -6.622 -26.017 1.00 45.82 ? 36 ALA B N 1 ATOM 2799 C CA . ALA B 2 36 ? 16.532 -7.539 -25.048 1.00 45.29 ? 36 ALA B CA 1 ATOM 2800 C C . ALA B 2 36 ? 16.262 -8.979 -25.465 1.00 45.47 ? 36 ALA B C 1 ATOM 2801 O O . ALA B 2 36 ? 15.241 -9.262 -26.088 1.00 46.30 ? 36 ALA B O 1 ATOM 2802 C CB . ALA B 2 36 ? 15.960 -7.281 -23.673 1.00 46.34 ? 36 ALA B CB 1 ATOM 2803 N N . ASP B 2 37 ? 17.178 -9.889 -25.142 1.00 44.76 ? 37 ASP B N 1 ATOM 2804 C CA . ASP B 2 37 ? 16.880 -11.306 -25.279 1.00 45.34 ? 37 ASP B CA 1 ATOM 2805 C C . ASP B 2 37 ? 16.213 -11.730 -23.976 1.00 46.36 ? 37 ASP B C 1 ATOM 2806 O O . ASP B 2 37 ? 16.842 -11.691 -22.916 1.00 44.68 ? 37 ASP B O 1 ATOM 2807 C CB . ASP B 2 37 ? 18.147 -12.120 -25.550 1.00 44.59 ? 37 ASP B CB 1 ATOM 2808 C CG . ASP B 2 37 ? 17.848 -13.582 -25.819 1.00 45.79 ? 37 ASP B CG 1 ATOM 2809 O OD1 . ASP B 2 37 ? 17.331 -13.899 -26.921 1.00 46.94 ? 37 ASP B OD1 1 ATOM 2810 O OD2 . ASP B 2 37 ? 18.123 -14.413 -24.925 1.00 45.05 ? 37 ASP B OD2 1 ATOM 2811 N N . LYS B 2 38 ? 14.932 -12.089 -24.047 1.00 47.94 ? 38 LYS B N 1 ATOM 2812 C CA . LYS B 2 38 ? 14.153 -12.345 -22.834 1.00 49.78 ? 38 LYS B CA 1 ATOM 2813 C C . LYS B 2 38 ? 14.577 -13.632 -22.127 1.00 48.89 ? 38 LYS B C 1 ATOM 2814 O O . LYS B 2 38 ? 14.695 -13.662 -20.901 1.00 49.32 ? 38 LYS B O 1 ATOM 2815 C CB . LYS B 2 38 ? 12.642 -12.358 -23.124 1.00 51.99 ? 38 LYS B CB 1 ATOM 2816 C CG . LYS B 2 38 ? 12.039 -10.995 -23.519 1.00 55.95 ? 38 LYS B CG 1 ATOM 2817 C CD . LYS B 2 38 ? 11.633 -10.159 -22.294 1.00 60.44 ? 38 LYS B CD 1 ATOM 2818 C CE . LYS B 2 38 ? 11.233 -8.724 -22.676 1.00 62.81 ? 38 LYS B CE 1 ATOM 2819 N NZ . LYS B 2 38 ? 10.456 -8.647 -23.969 1.00 64.50 ? 38 LYS B NZ 1 ATOM 2820 N N . GLU B 2 39 ? 14.814 -14.679 -22.905 1.00 48.20 ? 39 GLU B N 1 ATOM 2821 C CA . GLU B 2 39 ? 15.197 -15.974 -22.355 1.00 48.41 ? 39 GLU B CA 1 ATOM 2822 C C . GLU B 2 39 ? 16.534 -15.988 -21.607 1.00 46.07 ? 39 GLU B C 1 ATOM 2823 O O . GLU B 2 39 ? 16.597 -16.488 -20.495 1.00 45.76 ? 39 GLU B O 1 ATOM 2824 C CB . GLU B 2 39 ? 15.218 -17.032 -23.450 1.00 48.99 ? 39 GLU B CB 1 ATOM 2825 C CG . GLU B 2 39 ? 15.383 -18.447 -22.914 1.00 53.48 ? 39 GLU B CG 1 ATOM 2826 C CD . GLU B 2 39 ? 14.720 -19.488 -23.803 1.00 59.53 ? 39 GLU B CD 1 ATOM 2827 O OE1 . GLU B 2 39 ? 14.862 -19.404 -25.045 1.00 60.65 ? 39 GLU B OE1 1 ATOM 2828 O OE2 . GLU B 2 39 ? 14.054 -20.394 -23.247 1.00 64.12 ? 39 GLU B OE2 1 ATOM 2829 N N . SER B 2 40 ? 17.601 -15.481 -22.227 1.00 43.57 ? 40 SER B N 1 ATOM 2830 C CA . SER B 2 40 ? 18.903 -15.416 -21.543 1.00 41.68 ? 40 SER B CA 1 ATOM 2831 C C . SER B 2 40 ? 18.863 -14.507 -20.312 1.00 40.84 ? 40 SER B C 1 ATOM 2832 O O . SER B 2 40 ? 19.489 -14.808 -19.308 1.00 40.01 ? 40 SER B O 1 ATOM 2833 C CB . SER B 2 40 ? 20.018 -14.957 -22.481 1.00 40.82 ? 40 SER B CB 1 ATOM 2834 O OG . SER B 2 40 ? 19.722 -13.677 -23.030 1.00 41.29 ? 40 SER B OG 1 ATOM 2835 N N . THR B 2 41 ? 18.124 -13.400 -20.403 1.00 40.95 ? 41 THR B N 1 ATOM 2836 C CA . THR B 2 41 ? 17.998 -12.440 -19.302 1.00 41.25 ? 41 THR B CA 1 ATOM 2837 C C . THR B 2 41 ? 17.257 -13.081 -18.122 1.00 41.99 ? 41 THR B C 1 ATOM 2838 O O . THR B 2 41 ? 17.690 -12.973 -16.972 1.00 41.00 ? 41 THR B O 1 ATOM 2839 C CB . THR B 2 41 ? 17.282 -11.156 -19.778 1.00 41.82 ? 41 THR B CB 1 ATOM 2840 O OG1 . THR B 2 41 ? 18.053 -10.559 -20.826 1.00 42.05 ? 41 THR B OG1 1 ATOM 2841 C CG2 . THR B 2 41 ? 17.126 -10.150 -18.654 1.00 42.32 ? 41 THR B CG2 1 ATOM 2842 N N . GLN B 2 42 ? 16.153 -13.764 -18.427 1.00 43.14 ? 42 GLN B N 1 ATOM 2843 C CA . GLN B 2 42 ? 15.356 -14.438 -17.400 1.00 44.67 ? 42 GLN B CA 1 ATOM 2844 C C . GLN B 2 42 ? 16.170 -15.516 -16.680 1.00 43.31 ? 42 GLN B C 1 ATOM 2845 O O . GLN B 2 42 ? 16.169 -15.568 -15.451 1.00 43.36 ? 42 GLN B O 1 ATOM 2846 C CB . GLN B 2 42 ? 14.075 -15.027 -18.006 1.00 46.45 ? 42 GLN B CB 1 ATOM 2847 C CG . GLN B 2 42 ? 13.060 -15.567 -16.981 1.00 49.43 ? 42 GLN B CG 1 ATOM 2848 C CD . GLN B 2 42 ? 12.607 -14.516 -15.984 1.00 54.02 ? 42 GLN B CD 1 ATOM 2849 O OE1 . GLN B 2 42 ? 12.263 -13.389 -16.361 1.00 57.44 ? 42 GLN B OE1 1 ATOM 2850 N NE2 . GLN B 2 42 ? 12.605 -14.876 -14.702 1.00 53.90 ? 42 GLN B NE2 1 ATOM 2851 N N . LYS B 2 43 ? 16.879 -16.351 -17.443 1.00 42.72 ? 43 LYS B N 1 ATOM 2852 C CA . LYS B 2 43 ? 17.752 -17.378 -16.844 1.00 42.32 ? 43 LYS B CA 1 ATOM 2853 C C . LYS B 2 43 ? 18.808 -16.772 -15.902 1.00 40.45 ? 43 LYS B C 1 ATOM 2854 O O . LYS B 2 43 ? 19.015 -17.265 -14.774 1.00 40.11 ? 43 LYS B O 1 ATOM 2855 C CB . LYS B 2 43 ? 18.402 -18.253 -17.919 1.00 42.39 ? 43 LYS B CB 1 ATOM 2856 C CG . LYS B 2 43 ? 18.968 -19.562 -17.372 1.00 45.55 ? 43 LYS B CG 1 ATOM 2857 C CD . LYS B 2 43 ? 19.546 -20.432 -18.497 1.00 50.72 ? 43 LYS B CD 1 ATOM 2858 C CE . LYS B 2 43 ? 20.151 -21.758 -17.970 1.00 51.55 ? 43 LYS B CE 1 ATOM 2859 N NZ . LYS B 2 43 ? 20.903 -22.472 -19.067 1.00 53.67 ? 43 LYS B NZ 1 ATOM 2860 N N . ALA B 2 44 ? 19.442 -15.689 -16.347 1.00 38.62 ? 44 ALA B N 1 ATOM 2861 C CA . ALA B 2 44 ? 20.438 -14.988 -15.538 1.00 37.19 ? 44 ALA B CA 1 ATOM 2862 C C . ALA B 2 44 ? 19.796 -14.400 -14.294 1.00 37.56 ? 44 ALA B C 1 ATOM 2863 O O . ALA B 2 44 ? 20.366 -14.464 -13.198 1.00 36.90 ? 44 ALA B O 1 ATOM 2864 C CB . ALA B 2 44 ? 21.111 -13.888 -16.351 1.00 36.71 ? 44 ALA B CB 1 ATOM 2865 N N . PHE B 2 45 ? 18.599 -13.838 -14.461 1.00 38.14 ? 45 PHE B N 1 ATOM 2866 C CA . PHE B 2 45 ? 17.890 -13.237 -13.336 1.00 39.26 ? 45 PHE B CA 1 ATOM 2867 C C . PHE B 2 45 ? 17.558 -14.295 -12.284 1.00 38.67 ? 45 PHE B C 1 ATOM 2868 O O . PHE B 2 45 ? 17.753 -14.067 -11.099 1.00 38.91 ? 45 PHE B O 1 ATOM 2869 C CB . PHE B 2 45 ? 16.636 -12.481 -13.813 1.00 40.72 ? 45 PHE B CB 1 ATOM 2870 C CG . PHE B 2 45 ? 15.884 -11.778 -12.703 1.00 42.54 ? 45 PHE B CG 1 ATOM 2871 C CD1 . PHE B 2 45 ? 16.326 -10.557 -12.202 1.00 44.24 ? 45 PHE B CD1 1 ATOM 2872 C CD2 . PHE B 2 45 ? 14.724 -12.340 -12.166 1.00 45.38 ? 45 PHE B CD2 1 ATOM 2873 C CE1 . PHE B 2 45 ? 15.624 -9.902 -11.162 1.00 45.41 ? 45 PHE B CE1 1 ATOM 2874 C CE2 . PHE B 2 45 ? 14.014 -11.697 -11.141 1.00 45.45 ? 45 PHE B CE2 1 ATOM 2875 C CZ . PHE B 2 45 ? 14.474 -10.478 -10.635 1.00 45.89 ? 45 PHE B CZ 1 ATOM 2876 N N . ASP B 2 46 ? 17.084 -15.462 -12.724 1.00 39.24 ? 46 ASP B N 1 ATOM 2877 C CA . ASP B 2 46 ? 16.759 -16.560 -11.786 1.00 39.59 ? 46 ASP B CA 1 ATOM 2878 C C . ASP B 2 46 ? 18.003 -17.074 -11.050 1.00 38.16 ? 46 ASP B C 1 ATOM 2879 O O . ASP B 2 46 ? 17.983 -17.238 -9.811 1.00 38.36 ? 46 ASP B O 1 ATOM 2880 C CB . ASP B 2 46 ? 16.003 -17.696 -12.489 1.00 40.60 ? 46 ASP B CB 1 ATOM 2881 C CG . ASP B 2 46 ? 14.646 -17.247 -13.038 1.00 43.17 ? 46 ASP B CG 1 ATOM 2882 O OD1 . ASP B 2 46 ? 14.053 -16.291 -12.480 1.00 43.72 ? 46 ASP B OD1 1 ATOM 2883 O OD2 . ASP B 2 46 ? 14.189 -17.831 -14.043 1.00 44.19 ? 46 ASP B OD2 1 ATOM 2884 N N . GLY B 2 47 ? 19.082 -17.289 -11.807 1.00 35.94 ? 47 GLY B N 1 ATOM 2885 C CA . GLY B 2 47 ? 20.403 -17.605 -11.241 1.00 34.95 ? 47 GLY B CA 1 ATOM 2886 C C . GLY B 2 47 ? 20.894 -16.610 -10.199 1.00 34.25 ? 47 GLY B C 1 ATOM 2887 O O . GLY B 2 47 ? 21.256 -16.984 -9.086 1.00 33.22 ? 47 GLY B O 1 ATOM 2888 N N . ILE B 2 48 ? 20.877 -15.325 -10.540 1.00 34.68 ? 48 ILE B N 1 ATOM 2889 C CA . ILE B 2 48 ? 21.355 -14.306 -9.603 1.00 33.86 ? 48 ILE B CA 1 ATOM 2890 C C . ILE B 2 48 ? 20.457 -14.239 -8.349 1.00 35.26 ? 48 ILE B C 1 ATOM 2891 O O . ILE B 2 48 ? 20.967 -14.128 -7.226 1.00 34.52 ? 48 ILE B O 1 ATOM 2892 C CB . ILE B 2 48 ? 21.508 -12.916 -10.304 1.00 33.92 ? 48 ILE B CB 1 ATOM 2893 C CG1 . ILE B 2 48 ? 22.563 -12.973 -11.421 1.00 32.90 ? 48 ILE B CG1 1 ATOM 2894 C CG2 . ILE B 2 48 ? 21.904 -11.834 -9.314 1.00 33.75 ? 48 ILE B CG2 1 ATOM 2895 C CD1 . ILE B 2 48 ? 23.950 -13.347 -10.952 1.00 33.04 ? 48 ILE B CD1 1 ATOM 2896 N N . THR B 2 49 ? 19.134 -14.321 -8.542 1.00 36.94 ? 49 THR B N 1 ATOM 2897 C CA . THR B 2 49 ? 18.183 -14.350 -7.417 1.00 38.75 ? 49 THR B CA 1 ATOM 2898 C C . THR B 2 49 ? 18.496 -15.491 -6.453 1.00 39.25 ? 49 THR B C 1 ATOM 2899 O O . THR B 2 49 ? 18.569 -15.277 -5.242 1.00 39.38 ? 49 THR B O 1 ATOM 2900 C CB . THR B 2 49 ? 16.724 -14.449 -7.883 1.00 39.99 ? 49 THR B CB 1 ATOM 2901 O OG1 . THR B 2 49 ? 16.391 -13.288 -8.649 1.00 40.82 ? 49 THR B OG1 1 ATOM 2902 C CG2 . THR B 2 49 ? 15.756 -14.580 -6.678 1.00 41.02 ? 49 THR B CG2 1 ATOM 2903 N N . ASN B 2 50 ? 18.690 -16.692 -6.997 1.00 40.01 ? 50 ASN B N 1 ATOM 2904 C CA . ASN B 2 50 ? 19.100 -17.839 -6.194 1.00 41.17 ? 50 ASN B CA 1 ATOM 2905 C C . ASN B 2 50 ? 20.425 -17.612 -5.447 1.00 40.35 ? 50 ASN B C 1 ATOM 2906 O O . ASN B 2 50 ? 20.543 -17.953 -4.257 1.00 40.89 ? 50 ASN B O 1 ATOM 2907 C CB . ASN B 2 50 ? 19.191 -19.116 -7.042 1.00 41.76 ? 50 ASN B CB 1 ATOM 2908 C CG . ASN B 2 50 ? 19.249 -20.378 -6.179 1.00 44.92 ? 50 ASN B CG 1 ATOM 2909 O OD1 . ASN B 2 50 ? 20.311 -21.009 -6.037 1.00 47.28 ? 50 ASN B OD1 1 ATOM 2910 N ND2 . ASN B 2 50 ? 18.114 -20.735 -5.574 1.00 44.44 ? 50 ASN B ND2 1 ATOM 2911 N N . LYS B 2 51 ? 21.407 -17.022 -6.126 1.00 39.37 ? 51 LYS B N 1 ATOM 2912 C CA . LYS B 2 51 ? 22.706 -16.776 -5.504 1.00 39.39 ? 51 LYS B CA 1 ATOM 2913 C C . LYS B 2 51 ? 22.601 -15.913 -4.255 1.00 39.92 ? 51 LYS B C 1 ATOM 2914 O O . LYS B 2 51 ? 23.201 -16.236 -3.237 1.00 40.03 ? 51 LYS B O 1 ATOM 2915 C CB . LYS B 2 51 ? 23.690 -16.140 -6.489 1.00 38.28 ? 51 LYS B CB 1 ATOM 2916 C CG . LYS B 2 51 ? 24.958 -15.610 -5.823 1.00 37.61 ? 51 LYS B CG 1 ATOM 2917 C CD . LYS B 2 51 ? 25.921 -14.939 -6.806 1.00 35.42 ? 51 LYS B CD 1 ATOM 2918 C CE . LYS B 2 51 ? 26.311 -15.865 -7.964 1.00 32.91 ? 51 LYS B CE 1 ATOM 2919 N NZ . LYS B 2 51 ? 27.766 -15.702 -8.298 1.00 28.99 ? 51 LYS B NZ 1 ATOM 2920 N N . VAL B 2 52 ? 21.849 -14.818 -4.332 1.00 41.82 ? 52 VAL B N 1 ATOM 2921 C CA . VAL B 2 52 ? 21.777 -13.887 -3.210 1.00 43.19 ? 52 VAL B CA 1 ATOM 2922 C C . VAL B 2 52 ? 21.047 -14.519 -2.026 1.00 44.60 ? 52 VAL B C 1 ATOM 2923 O O . VAL B 2 52 ? 21.460 -14.339 -0.887 1.00 44.31 ? 52 VAL B O 1 ATOM 2924 C CB . VAL B 2 52 ? 21.156 -12.507 -3.580 1.00 43.96 ? 52 VAL B CB 1 ATOM 2925 C CG1 . VAL B 2 52 ? 21.818 -11.926 -4.821 1.00 43.37 ? 52 VAL B CG1 1 ATOM 2926 C CG2 . VAL B 2 52 ? 19.651 -12.591 -3.773 1.00 46.78 ? 52 VAL B CG2 1 ATOM 2927 N N . ASN B 2 53 ? 19.977 -15.262 -2.315 1.00 46.38 ? 53 ASN B N 1 ATOM 2928 C CA . ASN B 2 53 ? 19.290 -16.068 -1.316 1.00 47.95 ? 53 ASN B CA 1 ATOM 2929 C C . ASN B 2 53 ? 20.207 -17.079 -0.647 1.00 48.78 ? 53 ASN B C 1 ATOM 2930 O O . ASN B 2 53 ? 20.212 -17.187 0.591 1.00 49.50 ? 53 ASN B O 1 ATOM 2931 C CB . ASN B 2 53 ? 18.078 -16.766 -1.917 1.00 48.47 ? 53 ASN B CB 1 ATOM 2932 C CG . ASN B 2 53 ? 16.979 -15.796 -2.299 1.00 49.97 ? 53 ASN B CG 1 ATOM 2933 O OD1 . ASN B 2 53 ? 16.919 -14.681 -1.790 1.00 52.02 ? 53 ASN B OD1 1 ATOM 2934 N ND2 . ASN B 2 53 ? 16.106 -16.213 -3.209 1.00 49.75 ? 53 ASN B ND2 1 ATOM 2935 N N . SER B 2 54 ? 20.997 -17.796 -1.444 1.00 49.45 ? 54 SER B N 1 ATOM 2936 C CA . SER B 2 54 ? 21.935 -18.784 -0.917 1.00 50.65 ? 54 SER B CA 1 ATOM 2937 C C . SER B 2 54 ? 23.013 -18.199 -0.015 1.00 51.36 ? 54 SER B C 1 ATOM 2938 O O . SER B 2 54 ? 23.356 -18.814 0.993 1.00 51.76 ? 54 SER B O 1 ATOM 2939 C CB . SER B 2 54 ? 22.608 -19.566 -2.047 1.00 50.32 ? 54 SER B CB 1 ATOM 2940 O OG . SER B 2 54 ? 21.659 -20.336 -2.750 1.00 51.12 ? 54 SER B OG 1 ATOM 2941 N N . VAL B 2 55 ? 23.573 -17.041 -0.376 1.00 52.34 ? 55 VAL B N 1 ATOM 2942 C CA . VAL B 2 55 ? 24.626 -16.460 0.459 1.00 53.61 ? 55 VAL B CA 1 ATOM 2943 C C . VAL B 2 55 ? 23.992 -16.075 1.788 1.00 54.83 ? 55 VAL B C 1 ATOM 2944 O O . VAL B 2 55 ? 24.478 -16.482 2.842 1.00 54.87 ? 55 VAL B O 1 ATOM 2945 C CB . VAL B 2 55 ? 25.409 -15.245 -0.183 1.00 53.20 ? 55 VAL B CB 1 ATOM 2946 C CG1 . VAL B 2 55 ? 25.734 -15.496 -1.644 1.00 53.39 ? 55 VAL B CG1 1 ATOM 2947 C CG2 . VAL B 2 55 ? 24.667 -13.922 -0.001 1.00 54.38 ? 55 VAL B CG2 1 ATOM 2948 N N . ILE B 2 56 ? 22.879 -15.342 1.709 1.00 56.59 ? 56 ILE B N 1 ATOM 2949 C CA . ILE B 2 56 ? 22.100 -14.921 2.877 1.00 58.27 ? 56 ILE B CA 1 ATOM 2950 C C . ILE B 2 56 ? 21.679 -16.097 3.761 1.00 59.88 ? 56 ILE B C 1 ATOM 2951 O O . ILE B 2 56 ? 21.909 -16.080 4.980 1.00 59.92 ? 56 ILE B O 1 ATOM 2952 C CB . ILE B 2 56 ? 20.851 -14.094 2.452 1.00 58.93 ? 56 ILE B CB 1 ATOM 2953 C CG1 . ILE B 2 56 ? 21.283 -12.711 1.952 1.00 58.51 ? 56 ILE B CG1 1 ATOM 2954 C CG2 . ILE B 2 56 ? 19.816 -13.997 3.594 1.00 59.74 ? 56 ILE B CG2 1 ATOM 2955 C CD1 . ILE B 2 56 ? 20.153 -11.842 1.431 1.00 59.29 ? 56 ILE B CD1 1 ATOM 2956 N N . GLU B 2 57 ? 21.069 -17.116 3.154 1.00 61.73 ? 57 GLU B N 1 ATOM 2957 C CA . GLU B 2 57 ? 20.543 -18.251 3.925 1.00 63.92 ? 57 GLU B CA 1 ATOM 2958 C C . GLU B 2 57 ? 21.625 -19.090 4.628 1.00 64.24 ? 57 GLU B C 1 ATOM 2959 O O . GLU B 2 57 ? 21.358 -19.702 5.669 1.00 64.94 ? 57 GLU B O 1 ATOM 2960 C CB . GLU B 2 57 ? 19.587 -19.109 3.084 1.00 64.86 ? 57 GLU B CB 1 ATOM 2961 C CG . GLU B 2 57 ? 18.171 -18.521 3.012 1.00 67.01 ? 57 GLU B CG 1 ATOM 2962 C CD . GLU B 2 57 ? 17.336 -19.042 1.841 1.00 69.98 ? 57 GLU B CD 1 ATOM 2963 O OE1 . GLU B 2 57 ? 17.827 -19.880 1.048 1.00 69.85 ? 57 GLU B OE1 1 ATOM 2964 O OE2 . GLU B 2 57 ? 16.172 -18.597 1.711 1.00 71.81 ? 57 GLU B OE2 1 ATOM 2965 N N . LYS B 2 58 ? 22.845 -19.076 4.086 1.00 64.18 ? 58 LYS B N 1 ATOM 2966 C CA . LYS B 2 58 ? 23.969 -19.796 4.683 1.00 64.89 ? 58 LYS B CA 1 ATOM 2967 C C . LYS B 2 58 ? 24.537 -19.123 5.939 1.00 65.73 ? 58 LYS B C 1 ATOM 2968 O O . LYS B 2 58 ? 25.266 -19.756 6.713 1.00 65.62 ? 58 LYS B O 1 ATOM 2969 C CB . LYS B 2 58 ? 25.076 -20.046 3.650 1.00 64.06 ? 58 LYS B CB 1 ATOM 2970 C CG . LYS B 2 58 ? 24.808 -21.235 2.730 1.00 63.74 ? 58 LYS B CG 1 ATOM 2971 C CD . LYS B 2 58 ? 24.785 -22.543 3.508 1.00 63.57 ? 58 LYS B CD 1 ATOM 2972 C CE . LYS B 2 58 ? 24.340 -23.704 2.640 1.00 62.85 ? 58 LYS B CE 1 ATOM 2973 N NZ . LYS B 2 58 ? 22.865 -23.872 2.569 1.00 61.45 ? 58 LYS B NZ 1 ATOM 2974 N N . MET B 2 59 ? 24.191 -17.852 6.142 1.00 67.03 ? 59 MET B N 1 ATOM 2975 C CA . MET B 2 59 ? 24.621 -17.105 7.329 1.00 68.06 ? 59 MET B CA 1 ATOM 2976 C C . MET B 2 59 ? 23.464 -16.694 8.244 1.00 69.43 ? 59 MET B C 1 ATOM 2977 O O . MET B 2 59 ? 23.553 -15.688 8.953 1.00 69.76 ? 59 MET B O 1 ATOM 2978 C CB . MET B 2 59 ? 25.480 -15.901 6.928 1.00 67.44 ? 59 MET B CB 1 ATOM 2979 C CG . MET B 2 59 ? 26.901 -16.302 6.572 1.00 68.16 ? 59 MET B CG 1 ATOM 2980 S SD . MET B 2 59 ? 27.820 -15.246 5.424 1.00 71.44 ? 59 MET B SD 1 ATOM 2981 C CE . MET B 2 59 ? 26.620 -15.033 4.116 1.00 70.51 ? 59 MET B CE 1 ATOM 2982 N N . ASN B 2 60 ? 22.392 -17.490 8.235 1.00 70.96 ? 60 ASN B N 1 ATOM 2983 C CA . ASN B 2 60 ? 21.239 -17.270 9.122 1.00 72.39 ? 60 ASN B CA 1 ATOM 2984 C C . ASN B 2 60 ? 21.482 -17.742 10.559 1.00 72.40 ? 60 ASN B C 1 ATOM 2985 O O . ASN B 2 60 ? 20.928 -17.176 11.510 1.00 72.85 ? 60 ASN B O 1 ATOM 2986 C CB . ASN B 2 60 ? 19.965 -17.897 8.545 1.00 73.78 ? 60 ASN B CB 1 ATOM 2987 C CG . ASN B 2 60 ? 19.441 -17.140 7.332 1.00 75.10 ? 60 ASN B CG 1 ATOM 2988 O OD1 . ASN B 2 60 ? 19.841 -15.997 7.078 1.00 76.04 ? 60 ASN B OD1 1 ATOM 2989 N ND2 . ASN B 2 60 ? 18.540 -17.772 6.578 1.00 76.18 ? 60 ASN B ND2 1 ATOM 2990 N N . THR B 2 61 ? 22.289 -18.790 10.713 1.00 71.97 ? 61 THR B N 1 ATOM 2991 C CA . THR B 2 61 ? 22.882 -19.076 12.018 1.00 71.66 ? 61 THR B CA 1 ATOM 2992 C C . THR B 2 61 ? 24.379 -18.792 11.958 1.00 70.35 ? 61 THR B C 1 ATOM 2993 O O . THR B 2 61 ? 25.181 -19.574 11.415 1.00 70.27 ? 61 THR B O 1 ATOM 2994 C CB . THR B 2 61 ? 22.600 -20.501 12.571 1.00 72.39 ? 61 THR B CB 1 ATOM 2995 O OG1 . THR B 2 61 ? 21.260 -20.891 12.258 1.00 74.02 ? 61 THR B OG1 1 ATOM 2996 C CG2 . THR B 2 61 ? 22.779 -20.518 14.096 1.00 72.18 ? 61 THR B CG2 1 ATOM 2997 N N . GLN B 2 62 ? 24.718 -17.617 12.473 1.00 69.33 ? 62 GLN B N 1 ATOM 2998 C CA . GLN B 2 62 ? 26.087 -17.249 12.761 1.00 67.80 ? 62 GLN B CA 1 ATOM 2999 C C . GLN B 2 62 ? 26.144 -17.016 14.280 1.00 67.00 ? 62 GLN B C 1 ATOM 3000 O O . GLN B 2 62 ? 25.159 -17.277 14.984 1.00 67.87 ? 62 GLN B O 1 ATOM 3001 C CB . GLN B 2 62 ? 26.499 -16.013 11.937 1.00 67.39 ? 62 GLN B CB 1 ATOM 3002 C CG . GLN B 2 62 ? 26.089 -14.666 12.521 1.00 68.16 ? 62 GLN B CG 1 ATOM 3003 C CD . GLN B 2 62 ? 26.906 -13.505 11.972 1.00 68.50 ? 62 GLN B CD 1 ATOM 3004 O OE1 . GLN B 2 62 ? 27.188 -13.431 10.772 1.00 66.85 ? 62 GLN B OE1 1 ATOM 3005 N NE2 . GLN B 2 62 ? 27.284 -12.583 12.855 1.00 68.39 ? 62 GLN B NE2 1 ATOM 3006 N N . PHE B 2 63 ? 27.280 -16.550 14.792 1.00 65.31 ? 63 PHE B N 1 ATOM 3007 C CA . PHE B 2 63 ? 27.407 -16.281 16.224 1.00 63.92 ? 63 PHE B CA 1 ATOM 3008 C C . PHE B 2 63 ? 26.649 -15.028 16.667 1.00 63.46 ? 63 PHE B C 1 ATOM 3009 O O . PHE B 2 63 ? 26.514 -14.058 15.915 1.00 63.62 ? 63 PHE B O 1 ATOM 3010 C CB . PHE B 2 63 ? 28.870 -16.166 16.618 1.00 63.34 ? 63 PHE B CB 1 ATOM 3011 C CG . PHE B 2 63 ? 29.100 -16.106 18.105 1.00 63.71 ? 63 PHE B CG 1 ATOM 3012 C CD1 . PHE B 2 63 ? 28.932 -17.243 18.900 1.00 64.48 ? 63 PHE B CD1 1 ATOM 3013 C CD2 . PHE B 2 63 ? 29.506 -14.916 18.714 1.00 63.34 ? 63 PHE B CD2 1 ATOM 3014 C CE1 . PHE B 2 63 ? 29.154 -17.190 20.277 1.00 63.67 ? 63 PHE B CE1 1 ATOM 3015 C CE2 . PHE B 2 63 ? 29.734 -14.862 20.083 1.00 63.05 ? 63 PHE B CE2 1 ATOM 3016 C CZ . PHE B 2 63 ? 29.560 -16.000 20.867 1.00 62.72 ? 63 PHE B CZ 1 ATOM 3017 N N . GLU B 2 64 ? 26.143 -15.068 17.892 1.00 62.42 ? 64 GLU B N 1 ATOM 3018 C CA . GLU B 2 64 ? 25.546 -13.904 18.514 1.00 61.57 ? 64 GLU B CA 1 ATOM 3019 C C . GLU B 2 64 ? 26.225 -13.687 19.863 1.00 59.98 ? 64 GLU B C 1 ATOM 3020 O O . GLU B 2 64 ? 26.347 -14.624 20.662 1.00 59.84 ? 64 GLU B O 1 ATOM 3021 C CB . GLU B 2 64 ? 24.037 -14.100 18.686 1.00 62.81 ? 64 GLU B CB 1 ATOM 3022 C CG . GLU B 2 64 ? 23.283 -14.344 17.377 1.00 64.69 ? 64 GLU B CG 1 ATOM 3023 C CD . GLU B 2 64 ? 22.073 -15.250 17.554 1.00 68.17 ? 64 GLU B CD 1 ATOM 3024 O OE1 . GLU B 2 64 ? 21.574 -15.378 18.703 1.00 68.69 ? 64 GLU B OE1 1 ATOM 3025 O OE2 . GLU B 2 64 ? 21.621 -15.833 16.539 1.00 69.50 ? 64 GLU B OE2 1 ATOM 3026 N N . ALA B 2 65 ? 26.681 -12.457 20.093 1.00 58.08 ? 65 ALA B N 1 ATOM 3027 C CA . ALA B 2 65 ? 27.260 -12.054 21.374 1.00 56.34 ? 65 ALA B CA 1 ATOM 3028 C C . ALA B 2 65 ? 26.182 -11.895 22.456 1.00 56.09 ? 65 ALA B C 1 ATOM 3029 O O . ALA B 2 65 ? 25.191 -11.170 22.268 1.00 56.97 ? 65 ALA B O 1 ATOM 3030 C CB . ALA B 2 65 ? 28.057 -10.760 21.208 1.00 56.05 ? 65 ALA B CB 1 ATOM 3031 N N . VAL B 2 66 ? 26.380 -12.591 23.578 1.00 54.21 ? 66 VAL B N 1 ATOM 3032 C CA . VAL B 2 66 ? 25.516 -12.499 24.770 1.00 52.86 ? 66 VAL B CA 1 ATOM 3033 C C . VAL B 2 66 ? 26.210 -11.665 25.857 1.00 51.06 ? 66 VAL B C 1 ATOM 3034 O O . VAL B 2 66 ? 27.358 -11.972 26.245 1.00 51.25 ? 66 VAL B O 1 ATOM 3035 C CB . VAL B 2 66 ? 25.151 -13.928 25.328 1.00 53.61 ? 66 VAL B CB 1 ATOM 3036 C CG1 . VAL B 2 66 ? 24.696 -13.885 26.803 1.00 53.78 ? 66 VAL B CG1 1 ATOM 3037 C CG2 . VAL B 2 66 ? 24.101 -14.606 24.448 1.00 53.88 ? 66 VAL B CG2 1 ATOM 3038 N N . GLY B 2 67 ? 25.535 -10.628 26.356 1.00 48.67 ? 67 GLY B N 1 ATOM 3039 C CA . GLY B 2 67 ? 26.071 -9.832 27.459 1.00 45.25 ? 67 GLY B CA 1 ATOM 3040 C C . GLY B 2 67 ? 26.202 -10.618 28.764 1.00 42.65 ? 67 GLY B C 1 ATOM 3041 O O . GLY B 2 67 ? 25.223 -11.136 29.268 1.00 44.21 ? 67 GLY B O 1 ATOM 3042 N N . LYS B 2 68 ? 27.414 -10.723 29.295 1.00 38.67 ? 68 LYS B N 1 ATOM 3043 C CA . LYS B 2 68 ? 27.679 -11.352 30.581 1.00 35.64 ? 68 LYS B CA 1 ATOM 3044 C C . LYS B 2 68 ? 28.614 -10.432 31.326 1.00 32.82 ? 68 LYS B C 1 ATOM 3045 O O . LYS B 2 68 ? 29.308 -9.661 30.708 1.00 32.26 ? 68 LYS B O 1 ATOM 3046 C CB . LYS B 2 68 ? 28.430 -12.678 30.423 1.00 35.73 ? 68 LYS B CB 1 ATOM 3047 C CG . LYS B 2 68 ? 27.646 -13.810 29.875 1.00 36.64 ? 68 LYS B CG 1 ATOM 3048 C CD . LYS B 2 68 ? 28.506 -15.066 29.950 1.00 35.93 ? 68 LYS B CD 1 ATOM 3049 C CE . LYS B 2 68 ? 27.684 -16.200 29.476 1.00 36.40 ? 68 LYS B CE 1 ATOM 3050 N NZ . LYS B 2 68 ? 27.191 -15.948 28.088 1.00 35.86 ? 68 LYS B NZ 1 ATOM 3051 N N . GLU B 2 69 ? 28.641 -10.548 32.638 1.00 29.67 ? 69 GLU B N 1 ATOM 3052 C CA . GLU B 2 69 ? 29.532 -9.766 33.473 1.00 29.31 ? 69 GLU B CA 1 ATOM 3053 C C . GLU B 2 69 ? 30.410 -10.649 34.343 1.00 27.40 ? 69 GLU B C 1 ATOM 3054 O O . GLU B 2 69 ? 30.090 -11.817 34.587 1.00 26.06 ? 69 GLU B O 1 ATOM 3055 C CB . GLU B 2 69 ? 28.730 -8.746 34.310 1.00 30.87 ? 69 GLU B CB 1 ATOM 3056 C CG . GLU B 2 69 ? 27.964 -7.786 33.360 1.00 33.93 ? 69 GLU B CG 1 ATOM 3057 C CD . GLU B 2 69 ? 27.274 -6.669 34.076 1.00 40.16 ? 69 GLU B CD 1 ATOM 3058 O OE1 . GLU B 2 69 ? 27.784 -6.235 35.120 1.00 42.49 ? 69 GLU B OE1 1 ATOM 3059 O OE2 . GLU B 2 69 ? 26.216 -6.229 33.572 1.00 48.66 ? 69 GLU B OE2 1 ATOM 3060 N N . PHE B 2 70 ? 31.520 -10.084 34.805 1.00 26.29 ? 70 PHE B N 1 ATOM 3061 C CA . PHE B 2 70 ? 32.560 -10.825 35.500 1.00 25.69 ? 70 PHE B CA 1 ATOM 3062 C C . PHE B 2 70 ? 33.144 -9.956 36.593 1.00 27.54 ? 70 PHE B C 1 ATOM 3063 O O . PHE B 2 70 ? 33.292 -8.748 36.403 1.00 29.12 ? 70 PHE B O 1 ATOM 3064 C CB . PHE B 2 70 ? 33.659 -11.240 34.488 1.00 24.85 ? 70 PHE B CB 1 ATOM 3065 C CG . PHE B 2 70 ? 33.123 -12.031 33.328 1.00 23.52 ? 70 PHE B CG 1 ATOM 3066 C CD1 . PHE B 2 70 ? 32.972 -13.408 33.428 1.00 23.89 ? 70 PHE B CD1 1 ATOM 3067 C CD2 . PHE B 2 70 ? 32.749 -11.407 32.150 1.00 23.73 ? 70 PHE B CD2 1 ATOM 3068 C CE1 . PHE B 2 70 ? 32.471 -14.145 32.340 1.00 19.84 ? 70 PHE B CE1 1 ATOM 3069 C CE2 . PHE B 2 70 ? 32.203 -12.115 31.080 1.00 24.39 ? 70 PHE B CE2 1 ATOM 3070 C CZ . PHE B 2 70 ? 32.068 -13.507 31.174 1.00 22.37 ? 70 PHE B CZ 1 ATOM 3071 N N . SER B 2 71 ? 33.422 -10.549 37.741 1.00 26.63 ? 71 SER B N 1 ATOM 3072 C CA . SER B 2 71 ? 34.023 -9.829 38.843 1.00 29.10 ? 71 SER B CA 1 ATOM 3073 C C . SER B 2 71 ? 35.516 -9.543 38.580 1.00 29.59 ? 71 SER B C 1 ATOM 3074 O O . SER B 2 71 ? 36.115 -10.031 37.593 1.00 26.98 ? 71 SER B O 1 ATOM 3075 C CB . SER B 2 71 ? 33.881 -10.622 40.142 1.00 28.13 ? 71 SER B CB 1 ATOM 3076 O OG . SER B 2 71 ? 34.874 -11.643 40.201 1.00 31.00 ? 71 SER B OG 1 ATOM 3077 N N . ASN B 2 72 ? 36.120 -8.799 39.506 1.00 30.82 ? 72 ASN B N 1 ATOM 3078 C CA . ASN B 2 72 ? 37.528 -8.457 39.374 1.00 32.32 ? 72 ASN B CA 1 ATOM 3079 C C . ASN B 2 72 ? 38.440 -9.625 39.723 1.00 31.49 ? 72 ASN B C 1 ATOM 3080 O O . ASN B 2 72 ? 39.649 -9.544 39.496 1.00 31.02 ? 72 ASN B O 1 ATOM 3081 C CB . ASN B 2 72 ? 37.888 -7.149 40.127 1.00 34.32 ? 72 ASN B CB 1 ATOM 3082 C CG . ASN B 2 72 ? 37.843 -7.298 41.629 1.00 39.05 ? 72 ASN B CG 1 ATOM 3083 O OD1 . ASN B 2 72 ? 37.578 -8.384 42.171 1.00 43.60 ? 72 ASN B OD1 1 ATOM 3084 N ND2 . ASN B 2 72 ? 38.115 -6.192 42.339 1.00 43.92 ? 72 ASN B ND2 1 ATOM 3085 N N . LEU B 2 73 ? 37.867 -10.718 40.251 1.00 29.77 ? 73 LEU B N 1 ATOM 3086 C CA . LEU B 2 73 ? 38.637 -11.956 40.434 1.00 28.70 ? 73 LEU B CA 1 ATOM 3087 C C . LEU B 2 73 ? 38.287 -12.985 39.368 1.00 26.54 ? 73 LEU B C 1 ATOM 3088 O O . LEU B 2 73 ? 38.601 -14.176 39.492 1.00 25.94 ? 73 LEU B O 1 ATOM 3089 C CB . LEU B 2 73 ? 38.433 -12.547 41.834 1.00 30.51 ? 73 LEU B CB 1 ATOM 3090 C CG . LEU B 2 73 ? 39.032 -11.964 43.144 1.00 35.20 ? 73 LEU B CG 1 ATOM 3091 C CD1 . LEU B 2 73 ? 38.477 -10.576 43.496 1.00 40.21 ? 73 LEU B CD1 1 ATOM 3092 C CD2 . LEU B 2 73 ? 38.700 -12.913 44.294 1.00 35.66 ? 73 LEU B CD2 1 ATOM 3093 N N . GLU B 2 74 ? 37.673 -12.522 38.286 1.00 24.07 ? 74 GLU B N 1 ATOM 3094 C CA . GLU B 2 74 ? 37.346 -13.395 37.170 1.00 21.89 ? 74 GLU B CA 1 ATOM 3095 C C . GLU B 2 74 ? 37.870 -12.860 35.871 1.00 20.83 ? 74 GLU B C 1 ATOM 3096 O O . GLU B 2 74 ? 37.212 -12.982 34.828 1.00 19.48 ? 74 GLU B O 1 ATOM 3097 C CB . GLU B 2 74 ? 35.823 -13.576 37.081 1.00 21.73 ? 74 GLU B CB 1 ATOM 3098 C CG . GLU B 2 74 ? 35.255 -14.287 38.277 1.00 24.85 ? 74 GLU B CG 1 ATOM 3099 C CD . GLU B 2 74 ? 33.743 -14.452 38.134 1.00 28.15 ? 74 GLU B CD 1 ATOM 3100 O OE1 . GLU B 2 74 ? 33.080 -13.481 37.703 1.00 26.85 ? 74 GLU B OE1 1 ATOM 3101 O OE2 . GLU B 2 74 ? 33.263 -15.563 38.430 1.00 26.40 ? 74 GLU B OE2 1 ATOM 3102 N N . ARG B 2 75 ? 39.073 -12.271 35.907 1.00 20.04 ? 75 ARG B N 1 ATOM 3103 C CA . ARG B 2 75 ? 39.685 -11.700 34.683 1.00 19.66 ? 75 ARG B CA 1 ATOM 3104 C C . ARG B 2 75 ? 40.018 -12.726 33.614 1.00 17.90 ? 75 ARG B C 1 ATOM 3105 O O . ARG B 2 75 ? 39.929 -12.439 32.438 1.00 17.19 ? 75 ARG B O 1 ATOM 3106 C CB . ARG B 2 75 ? 40.974 -10.904 35.088 1.00 20.98 ? 75 ARG B CB 1 ATOM 3107 C CG . ARG B 2 75 ? 40.679 -9.724 36.061 1.00 26.29 ? 75 ARG B CG 1 ATOM 3108 C CD . ARG B 2 75 ? 40.081 -8.597 35.245 1.00 39.38 ? 75 ARG B CD 1 ATOM 3109 N NE . ARG B 2 75 ? 39.141 -7.758 35.977 1.00 48.32 ? 75 ARG B NE 1 ATOM 3110 C CZ . ARG B 2 75 ? 37.813 -7.781 35.825 1.00 53.14 ? 75 ARG B CZ 1 ATOM 3111 N NH1 . ARG B 2 75 ? 37.212 -8.632 34.982 1.00 50.61 ? 75 ARG B NH1 1 ATOM 3112 N NH2 . ARG B 2 75 ? 37.070 -6.944 36.548 1.00 56.67 ? 75 ARG B NH2 1 ATOM 3113 N N . ARG B 2 76 ? 40.440 -13.923 34.008 1.00 17.77 ? 76 ARG B N 1 ATOM 3114 C CA . ARG B 2 76 ? 40.778 -14.940 32.988 1.00 18.26 ? 76 ARG B CA 1 ATOM 3115 C C . ARG B 2 76 ? 39.501 -15.355 32.267 1.00 18.44 ? 76 ARG B C 1 ATOM 3116 O O . ARG B 2 76 ? 39.488 -15.487 31.048 1.00 18.50 ? 76 ARG B O 1 ATOM 3117 C CB . ARG B 2 76 ? 41.388 -16.183 33.638 1.00 18.47 ? 76 ARG B CB 1 ATOM 3118 C CG . ARG B 2 76 ? 42.886 -16.042 34.032 1.00 20.90 ? 76 ARG B CG 1 ATOM 3119 C CD . ARG B 2 76 ? 43.331 -17.146 34.961 1.00 19.34 ? 76 ARG B CD 1 ATOM 3120 N NE . ARG B 2 76 ? 42.443 -17.243 36.122 1.00 18.84 ? 76 ARG B NE 1 ATOM 3121 C CZ . ARG B 2 76 ? 42.106 -18.406 36.668 1.00 17.32 ? 76 ARG B CZ 1 ATOM 3122 N NH1 . ARG B 2 76 ? 42.646 -19.512 36.167 1.00 18.94 ? 76 ARG B NH1 1 ATOM 3123 N NH2 . ARG B 2 76 ? 41.284 -18.457 37.700 1.00 18.23 ? 76 ARG B NH2 1 ATOM 3124 N N . LEU B 2 77 ? 38.454 -15.617 33.044 1.00 18.56 ? 77 LEU B N 1 ATOM 3125 C CA . LEU B 2 77 ? 37.152 -15.993 32.432 1.00 19.44 ? 77 LEU B CA 1 ATOM 3126 C C . LEU B 2 77 ? 36.596 -14.869 31.532 1.00 18.82 ? 77 LEU B C 1 ATOM 3127 O O . LEU B 2 77 ? 36.097 -15.116 30.442 1.00 18.93 ? 77 LEU B O 1 ATOM 3128 C CB . LEU B 2 77 ? 36.179 -16.394 33.571 1.00 18.81 ? 77 LEU B CB 1 ATOM 3129 C CG . LEU B 2 77 ? 34.739 -16.799 33.170 1.00 23.19 ? 77 LEU B CG 1 ATOM 3130 C CD1 . LEU B 2 77 ? 34.735 -18.015 32.228 1.00 23.59 ? 77 LEU B CD1 1 ATOM 3131 C CD2 . LEU B 2 77 ? 33.915 -17.050 34.496 1.00 21.09 ? 77 LEU B CD2 1 ATOM 3132 N N . GLU B 2 78 ? 36.717 -13.615 31.986 1.00 20.50 ? 78 GLU B N 1 ATOM 3133 C CA . GLU B 2 78 ? 36.289 -12.475 31.185 1.00 20.66 ? 78 GLU B CA 1 ATOM 3134 C C . GLU B 2 78 ? 37.054 -12.435 29.871 1.00 20.60 ? 78 GLU B C 1 ATOM 3135 O O . GLU B 2 78 ? 36.489 -12.218 28.790 1.00 19.52 ? 78 GLU B O 1 ATOM 3136 C CB . GLU B 2 78 ? 36.472 -11.148 31.966 1.00 22.83 ? 78 GLU B CB 1 ATOM 3137 C CG . GLU B 2 78 ? 35.835 -9.957 31.189 1.00 27.76 ? 78 GLU B CG 1 ATOM 3138 C CD . GLU B 2 78 ? 36.104 -8.576 31.798 1.00 38.24 ? 78 GLU B CD 1 ATOM 3139 O OE1 . GLU B 2 78 ? 36.809 -8.468 32.825 1.00 42.41 ? 78 GLU B OE1 1 ATOM 3140 O OE2 . GLU B 2 78 ? 35.616 -7.571 31.221 1.00 42.86 ? 78 GLU B OE2 1 ATOM 3141 N N . ASN B 2 79 ? 38.363 -12.673 29.941 1.00 21.67 ? 79 ASN B N 1 ATOM 3142 C CA . ASN B 2 79 ? 39.185 -12.543 28.731 1.00 22.17 ? 79 ASN B CA 1 ATOM 3143 C C . ASN B 2 79 ? 38.852 -13.701 27.791 1.00 21.91 ? 79 ASN B C 1 ATOM 3144 O O . ASN B 2 79 ? 38.791 -13.534 26.579 1.00 21.10 ? 79 ASN B O 1 ATOM 3145 C CB . ASN B 2 79 ? 40.678 -12.547 29.125 1.00 23.48 ? 79 ASN B CB 1 ATOM 3146 C CG . ASN B 2 79 ? 41.594 -12.318 27.931 1.00 28.62 ? 79 ASN B CG 1 ATOM 3147 O OD1 . ASN B 2 79 ? 42.249 -13.240 27.440 1.00 30.15 ? 79 ASN B OD1 1 ATOM 3148 N ND2 . ASN B 2 79 ? 41.594 -11.094 27.427 1.00 31.77 ? 79 ASN B ND2 1 ATOM 3149 N N . LEU B 2 80 ? 38.577 -14.872 28.370 1.00 22.81 ? 80 LEU B N 1 ATOM 3150 C CA . LEU B 2 80 ? 38.168 -16.033 27.565 1.00 23.37 ? 80 LEU B CA 1 ATOM 3151 C C . LEU B 2 80 ? 36.866 -15.726 26.814 1.00 23.30 ? 80 LEU B C 1 ATOM 3152 O O . LEU B 2 80 ? 36.728 -15.982 25.593 1.00 23.04 ? 80 LEU B O 1 ATOM 3153 C CB . LEU B 2 80 ? 37.997 -17.265 28.488 1.00 23.80 ? 80 LEU B CB 1 ATOM 3154 C CG . LEU B 2 80 ? 37.963 -18.631 27.786 1.00 28.51 ? 80 LEU B CG 1 ATOM 3155 C CD1 . LEU B 2 80 ? 38.102 -19.771 28.799 1.00 32.55 ? 80 LEU B CD1 1 ATOM 3156 C CD2 . LEU B 2 80 ? 36.677 -18.783 26.998 1.00 31.35 ? 80 LEU B CD2 1 ATOM 3157 N N . ASN B 2 81 ? 35.917 -15.147 27.532 1.00 23.81 ? 81 ASN B N 1 ATOM 3158 C CA . ASN B 2 81 ? 34.627 -14.796 26.939 1.00 25.37 ? 81 ASN B CA 1 ATOM 3159 C C . ASN B 2 81 ? 34.810 -13.791 25.809 1.00 25.42 ? 81 ASN B C 1 ATOM 3160 O O . ASN B 2 81 ? 34.212 -13.944 24.719 1.00 25.49 ? 81 ASN B O 1 ATOM 3161 C CB . ASN B 2 81 ? 33.698 -14.203 28.006 1.00 24.94 ? 81 ASN B CB 1 ATOM 3162 C CG . ASN B 2 81 ? 32.274 -14.010 27.496 1.00 28.62 ? 81 ASN B CG 1 ATOM 3163 O OD1 . ASN B 2 81 ? 31.804 -12.880 27.362 1.00 30.72 ? 81 ASN B OD1 1 ATOM 3164 N ND2 . ASN B 2 81 ? 31.588 -15.115 27.223 1.00 29.09 ? 81 ASN B ND2 1 ATOM 3165 N N . LYS B 2 82 ? 35.644 -12.781 26.074 1.00 26.71 ? 82 LYS B N 1 ATOM 3166 C CA . LYS B 2 82 ? 35.973 -11.736 25.106 1.00 28.21 ? 82 LYS B CA 1 ATOM 3167 C C . LYS B 2 82 ? 36.647 -12.312 23.864 1.00 28.50 ? 82 LYS B C 1 ATOM 3168 O O . LYS B 2 82 ? 36.195 -12.044 22.740 1.00 28.58 ? 82 LYS B O 1 ATOM 3169 C CB . LYS B 2 82 ? 36.884 -10.673 25.739 1.00 29.73 ? 82 LYS B CB 1 ATOM 3170 C CG . LYS B 2 82 ? 37.449 -9.612 24.727 1.00 33.69 ? 82 LYS B CG 1 ATOM 3171 C CD . LYS B 2 82 ? 38.491 -8.716 25.442 1.00 39.43 ? 82 LYS B CD 1 ATOM 3172 C CE . LYS B 2 82 ? 38.674 -7.358 24.767 1.00 43.41 ? 82 LYS B CE 1 ATOM 3173 N NZ . LYS B 2 82 ? 39.155 -7.487 23.357 1.00 46.12 ? 82 LYS B NZ 1 ATOM 3174 N N . LYS B 2 83 ? 37.701 -13.111 24.068 1.00 28.73 ? 83 LYS B N 1 ATOM 3175 C CA . LYS B 2 83 ? 38.417 -13.765 22.959 1.00 30.26 ? 83 LYS B CA 1 ATOM 3176 C C . LYS B 2 83 ? 37.482 -14.618 22.144 1.00 29.82 ? 83 LYS B C 1 ATOM 3177 O O . LYS B 2 83 ? 37.639 -14.735 20.930 1.00 30.09 ? 83 LYS B O 1 ATOM 3178 C CB . LYS B 2 83 ? 39.523 -14.697 23.452 1.00 29.75 ? 83 LYS B CB 1 ATOM 3179 C CG . LYS B 2 83 ? 40.579 -14.081 24.344 1.00 35.64 ? 83 LYS B CG 1 ATOM 3180 C CD . LYS B 2 83 ? 41.504 -13.123 23.638 1.00 39.95 ? 83 LYS B CD 1 ATOM 3181 C CE . LYS B 2 83 ? 42.323 -13.803 22.536 1.00 44.81 ? 83 LYS B CE 1 ATOM 3182 N NZ . LYS B 2 83 ? 43.163 -12.781 21.840 1.00 46.21 ? 83 LYS B NZ 1 ATOM 3183 N N . MET B 2 84 ? 36.556 -15.277 22.824 1.00 29.84 ? 84 MET B N 1 ATOM 3184 C CA . MET B 2 84 ? 35.615 -16.136 22.132 1.00 31.76 ? 84 MET B CA 1 ATOM 3185 C C . MET B 2 84 ? 34.629 -15.345 21.282 1.00 32.40 ? 84 MET B C 1 ATOM 3186 O O . MET B 2 84 ? 34.421 -15.657 20.099 1.00 31.89 ? 84 MET B O 1 ATOM 3187 C CB . MET B 2 84 ? 34.842 -17.015 23.095 1.00 30.76 ? 84 MET B CB 1 ATOM 3188 C CG . MET B 2 84 ? 33.922 -17.876 22.297 1.00 36.80 ? 84 MET B CG 1 ATOM 3189 S SD . MET B 2 84 ? 32.659 -18.700 23.200 1.00 42.08 ? 84 MET B SD 1 ATOM 3190 C CE . MET B 2 84 ? 31.710 -17.368 23.946 1.00 42.13 ? 84 MET B CE 1 ATOM 3191 N N . GLU B 2 85 ? 34.011 -14.332 21.884 1.00 34.05 ? 85 GLU B N 1 ATOM 3192 C CA . GLU B 2 85 ? 32.997 -13.549 21.169 1.00 37.06 ? 85 GLU B CA 1 ATOM 3193 C C . GLU B 2 85 ? 33.654 -12.762 20.026 1.00 37.97 ? 85 GLU B C 1 ATOM 3194 O O . GLU B 2 85 ? 33.154 -12.786 18.888 1.00 40.01 ? 85 GLU B O 1 ATOM 3195 C CB . GLU B 2 85 ? 32.128 -12.718 22.152 1.00 37.30 ? 85 GLU B CB 1 ATOM 3196 C CG . GLU B 2 85 ? 31.266 -13.649 23.073 1.00 39.59 ? 85 GLU B CG 1 ATOM 3197 C CD . GLU B 2 85 ? 30.088 -12.961 23.795 1.00 43.31 ? 85 GLU B CD 1 ATOM 3198 O OE1 . GLU B 2 85 ? 30.214 -11.766 24.171 1.00 45.46 ? 85 GLU B OE1 1 ATOM 3199 O OE2 . GLU B 2 85 ? 29.045 -13.633 24.008 1.00 41.13 ? 85 GLU B OE2 1 ATOM 3200 N N . ASP B 2 86 ? 34.800 -12.137 20.302 1.00 39.29 ? 86 ASP B N 1 ATOM 3201 C CA . ASP B 2 86 ? 35.675 -11.567 19.266 1.00 40.12 ? 86 ASP B CA 1 ATOM 3202 C C . ASP B 2 86 ? 36.069 -12.576 18.166 1.00 39.95 ? 86 ASP B C 1 ATOM 3203 O O . ASP B 2 86 ? 36.125 -12.224 16.986 1.00 40.31 ? 86 ASP B O 1 ATOM 3204 C CB . ASP B 2 86 ? 36.995 -11.066 19.862 1.00 41.08 ? 86 ASP B CB 1 ATOM 3205 C CG . ASP B 2 86 ? 36.864 -9.757 20.637 1.00 44.54 ? 86 ASP B CG 1 ATOM 3206 O OD1 . ASP B 2 86 ? 35.738 -9.231 20.755 1.00 47.69 ? 86 ASP B OD1 1 ATOM 3207 O OD2 . ASP B 2 86 ? 37.908 -9.281 21.156 1.00 45.99 ? 86 ASP B OD2 1 ATOM 3208 N N . GLY B 2 87 ? 36.396 -13.803 18.559 1.00 38.87 ? 87 GLY B N 1 ATOM 3209 C CA . GLY B 2 87 ? 36.856 -14.814 17.603 1.00 37.80 ? 87 GLY B CA 1 ATOM 3210 C C . GLY B 2 87 ? 35.818 -15.169 16.573 1.00 37.07 ? 87 GLY B C 1 ATOM 3211 O O . GLY B 2 87 ? 36.120 -15.231 15.369 1.00 37.36 ? 87 GLY B O 1 ATOM 3212 N N . PHE B 2 88 ? 34.590 -15.385 17.035 1.00 35.90 ? 88 PHE B N 1 ATOM 3213 C CA . PHE B 2 88 ? 33.488 -15.715 16.148 1.00 35.73 ? 88 PHE B CA 1 ATOM 3214 C C . PHE B 2 88 ? 33.098 -14.535 15.270 1.00 36.37 ? 88 PHE B C 1 ATOM 3215 O O . PHE B 2 88 ? 32.817 -14.693 14.068 1.00 35.93 ? 88 PHE B O 1 ATOM 3216 C CB . PHE B 2 88 ? 32.295 -16.251 16.933 1.00 35.65 ? 88 PHE B CB 1 ATOM 3217 C CG . PHE B 2 88 ? 32.490 -17.664 17.426 1.00 34.17 ? 88 PHE B CG 1 ATOM 3218 C CD1 . PHE B 2 88 ? 32.753 -18.704 16.533 1.00 33.56 ? 88 PHE B CD1 1 ATOM 3219 C CD2 . PHE B 2 88 ? 32.415 -17.959 18.795 1.00 33.49 ? 88 PHE B CD2 1 ATOM 3220 C CE1 . PHE B 2 88 ? 32.963 -20.019 16.989 1.00 32.48 ? 88 PHE B CE1 1 ATOM 3221 C CE2 . PHE B 2 88 ? 32.611 -19.252 19.236 1.00 32.16 ? 88 PHE B CE2 1 ATOM 3222 C CZ . PHE B 2 88 ? 32.885 -20.284 18.338 1.00 33.09 ? 88 PHE B CZ 1 ATOM 3223 N N . LEU B 2 89 ? 33.113 -13.354 15.875 1.00 36.90 ? 89 LEU B N 1 ATOM 3224 C CA . LEU B 2 89 ? 32.917 -12.112 15.167 1.00 38.33 ? 89 LEU B CA 1 ATOM 3225 C C . LEU B 2 89 ? 33.906 -11.992 13.997 1.00 38.28 ? 89 LEU B C 1 ATOM 3226 O O . LEU B 2 89 ? 33.491 -11.702 12.868 1.00 38.60 ? 89 LEU B O 1 ATOM 3227 C CB . LEU B 2 89 ? 33.034 -10.930 16.133 1.00 39.29 ? 89 LEU B CB 1 ATOM 3228 C CG . LEU B 2 89 ? 33.116 -9.530 15.543 1.00 43.09 ? 89 LEU B CG 1 ATOM 3229 C CD1 . LEU B 2 89 ? 31.898 -9.265 14.655 1.00 44.55 ? 89 LEU B CD1 1 ATOM 3230 C CD2 . LEU B 2 89 ? 33.221 -8.491 16.642 1.00 46.49 ? 89 LEU B CD2 1 ATOM 3231 N N . ASP B 2 90 ? 35.191 -12.226 14.257 1.00 37.73 ? 90 ASP B N 1 ATOM 3232 C CA . ASP B 2 90 ? 36.189 -12.176 13.198 1.00 38.47 ? 90 ASP B CA 1 ATOM 3233 C C . ASP B 2 90 ? 36.013 -13.264 12.143 1.00 37.96 ? 90 ASP B C 1 ATOM 3234 O O . ASP B 2 90 ? 36.235 -13.023 10.941 1.00 37.57 ? 90 ASP B O 1 ATOM 3235 C CB . ASP B 2 90 ? 37.601 -12.215 13.763 1.00 38.67 ? 90 ASP B CB 1 ATOM 3236 C CG . ASP B 2 90 ? 37.905 -11.010 14.626 1.00 42.31 ? 90 ASP B CG 1 ATOM 3237 O OD1 . ASP B 2 90 ? 37.432 -9.882 14.320 1.00 43.19 ? 90 ASP B OD1 1 ATOM 3238 O OD2 . ASP B 2 90 ? 38.622 -11.191 15.630 1.00 45.17 ? 90 ASP B OD2 1 ATOM 3239 N N . VAL B 2 91 ? 35.609 -14.454 12.579 1.00 37.18 ? 91 VAL B N 1 ATOM 3240 C CA . VAL B 2 91 ? 35.313 -15.536 11.638 1.00 37.14 ? 91 VAL B CA 1 ATOM 3241 C C . VAL B 2 91 ? 34.159 -15.174 10.713 1.00 37.55 ? 91 VAL B C 1 ATOM 3242 O O . VAL B 2 91 ? 34.261 -15.351 9.501 1.00 37.25 ? 91 VAL B O 1 ATOM 3243 C CB . VAL B 2 91 ? 35.014 -16.856 12.364 1.00 37.69 ? 91 VAL B CB 1 ATOM 3244 C CG1 . VAL B 2 91 ? 34.228 -17.824 11.463 1.00 36.22 ? 91 VAL B CG1 1 ATOM 3245 C CG2 . VAL B 2 91 ? 36.315 -17.473 12.867 1.00 36.57 ? 91 VAL B CG2 1 ATOM 3246 N N . TRP B 2 92 ? 33.057 -14.682 11.278 1.00 37.98 ? 92 TRP B N 1 ATOM 3247 C CA . TRP B 2 92 ? 31.914 -14.320 10.459 1.00 39.56 ? 92 TRP B CA 1 ATOM 3248 C C . TRP B 2 92 ? 32.163 -13.082 9.580 1.00 38.97 ? 92 TRP B C 1 ATOM 3249 O O . TRP B 2 92 ? 31.647 -13.020 8.476 1.00 39.63 ? 92 TRP B O 1 ATOM 3250 C CB . TRP B 2 92 ? 30.614 -14.244 11.283 1.00 40.16 ? 92 TRP B CB 1 ATOM 3251 C CG . TRP B 2 92 ? 30.236 -15.601 11.793 1.00 43.19 ? 92 TRP B CG 1 ATOM 3252 C CD1 . TRP B 2 92 ? 30.428 -16.088 13.069 1.00 44.99 ? 92 TRP B CD1 1 ATOM 3253 C CD2 . TRP B 2 92 ? 29.661 -16.675 11.039 1.00 45.12 ? 92 TRP B CD2 1 ATOM 3254 N NE1 . TRP B 2 92 ? 29.996 -17.387 13.148 1.00 45.76 ? 92 TRP B NE1 1 ATOM 3255 C CE2 . TRP B 2 92 ? 29.517 -17.775 11.922 1.00 46.05 ? 92 TRP B CE2 1 ATOM 3256 C CE3 . TRP B 2 92 ? 29.246 -16.817 9.704 1.00 46.22 ? 92 TRP B CE3 1 ATOM 3257 C CZ2 . TRP B 2 92 ? 28.972 -19.000 11.515 1.00 47.60 ? 92 TRP B CZ2 1 ATOM 3258 C CZ3 . TRP B 2 92 ? 28.702 -18.044 9.297 1.00 47.02 ? 92 TRP B CZ3 1 ATOM 3259 C CH2 . TRP B 2 92 ? 28.576 -19.117 10.195 1.00 48.23 ? 92 TRP B CH2 1 ATOM 3260 N N . THR B 2 93 ? 32.979 -12.131 10.040 1.00 39.18 ? 93 THR B N 1 ATOM 3261 C CA . THR B 2 93 ? 33.315 -10.965 9.219 1.00 39.31 ? 93 THR B CA 1 ATOM 3262 C C . THR B 2 93 ? 34.079 -11.449 7.968 1.00 39.33 ? 93 THR B C 1 ATOM 3263 O O . THR B 2 93 ? 33.730 -11.107 6.837 1.00 38.68 ? 93 THR B O 1 ATOM 3264 C CB . THR B 2 93 ? 34.129 -9.892 10.017 1.00 40.35 ? 93 THR B CB 1 ATOM 3265 O OG1 . THR B 2 93 ? 33.344 -9.408 11.114 1.00 40.08 ? 93 THR B OG1 1 ATOM 3266 C CG2 . THR B 2 93 ? 34.512 -8.699 9.125 1.00 41.17 ? 93 THR B CG2 1 ATOM 3267 N N . TYR B 2 94 ? 35.100 -12.266 8.194 1.00 39.03 ? 94 TYR B N 1 ATOM 3268 C CA . TYR B 2 94 ? 35.872 -12.891 7.138 1.00 39.02 ? 94 TYR B CA 1 ATOM 3269 C C . TYR B 2 94 ? 34.978 -13.704 6.183 1.00 38.55 ? 94 TYR B C 1 ATOM 3270 O O . TYR B 2 94 ? 35.074 -13.548 4.964 1.00 38.21 ? 94 TYR B O 1 ATOM 3271 C CB . TYR B 2 94 ? 36.954 -13.770 7.764 1.00 39.89 ? 94 TYR B CB 1 ATOM 3272 C CG . TYR B 2 94 ? 37.676 -14.669 6.788 1.00 40.85 ? 94 TYR B CG 1 ATOM 3273 C CD1 . TYR B 2 94 ? 38.870 -14.277 6.206 1.00 43.22 ? 94 TYR B CD1 1 ATOM 3274 C CD2 . TYR B 2 94 ? 37.157 -15.917 6.450 1.00 42.42 ? 94 TYR B CD2 1 ATOM 3275 C CE1 . TYR B 2 94 ? 39.534 -15.103 5.283 1.00 44.29 ? 94 TYR B CE1 1 ATOM 3276 C CE2 . TYR B 2 94 ? 37.810 -16.752 5.543 1.00 44.70 ? 94 TYR B CE2 1 ATOM 3277 C CZ . TYR B 2 94 ? 38.999 -16.341 4.966 1.00 45.28 ? 94 TYR B CZ 1 ATOM 3278 O OH . TYR B 2 94 ? 39.640 -17.183 4.077 1.00 46.36 ? 94 TYR B OH 1 ATOM 3279 N N . ASN B 2 95 ? 34.103 -14.551 6.734 1.00 37.76 ? 95 ASN B N 1 ATOM 3280 C CA . ASN B 2 95 ? 33.193 -15.350 5.920 1.00 37.33 ? 95 ASN B CA 1 ATOM 3281 C C . ASN B 2 95 ? 32.291 -14.505 5.027 1.00 36.89 ? 95 ASN B C 1 ATOM 3282 O O . ASN B 2 95 ? 32.115 -14.804 3.837 1.00 36.79 ? 95 ASN B O 1 ATOM 3283 C CB . ASN B 2 95 ? 32.310 -16.260 6.777 1.00 37.48 ? 95 ASN B CB 1 ATOM 3284 C CG . ASN B 2 95 ? 33.031 -17.501 7.276 1.00 38.77 ? 95 ASN B CG 1 ATOM 3285 O OD1 . ASN B 2 95 ? 34.189 -17.771 6.928 1.00 38.33 ? 95 ASN B OD1 1 ATOM 3286 N ND2 . ASN B 2 95 ? 32.340 -18.262 8.132 1.00 39.33 ? 95 ASN B ND2 1 ATOM 3287 N N . ALA B 2 96 ? 31.702 -13.471 5.607 1.00 36.13 ? 96 ALA B N 1 ATOM 3288 C CA . ALA B 2 96 ? 30.831 -12.603 4.853 1.00 36.25 ? 96 ALA B CA 1 ATOM 3289 C C . ALA B 2 96 ? 31.639 -11.840 3.795 1.00 36.20 ? 96 ALA B C 1 ATOM 3290 O O . ALA B 2 96 ? 31.257 -11.806 2.629 1.00 35.84 ? 96 ALA B O 1 ATOM 3291 C CB . ALA B 2 96 ? 30.076 -11.663 5.776 1.00 36.25 ? 96 ALA B CB 1 ATOM 3292 N N . GLU B 2 97 ? 32.775 -11.273 4.185 1.00 35.73 ? 97 GLU B N 1 ATOM 3293 C CA . GLU B 2 97 ? 33.569 -10.487 3.254 1.00 36.18 ? 97 GLU B CA 1 ATOM 3294 C C . GLU B 2 97 ? 34.173 -11.300 2.111 1.00 35.99 ? 97 GLU B C 1 ATOM 3295 O O . GLU B 2 97 ? 34.171 -10.848 0.945 1.00 35.62 ? 97 GLU B O 1 ATOM 3296 C CB . GLU B 2 97 ? 34.628 -9.703 4.001 1.00 36.01 ? 97 GLU B CB 1 ATOM 3297 C CG . GLU B 2 97 ? 34.013 -8.550 4.747 1.00 37.46 ? 97 GLU B CG 1 ATOM 3298 C CD . GLU B 2 97 ? 35.016 -7.774 5.561 1.00 40.23 ? 97 GLU B CD 1 ATOM 3299 O OE1 . GLU B 2 97 ? 36.229 -8.045 5.434 1.00 42.46 ? 97 GLU B OE1 1 ATOM 3300 O OE2 . GLU B 2 97 ? 34.590 -6.885 6.328 1.00 40.66 ? 97 GLU B OE2 1 ATOM 3301 N N . LEU B 2 98 ? 34.666 -12.493 2.437 1.00 35.78 ? 98 LEU B N 1 ATOM 3302 C CA . LEU B 2 98 ? 35.232 -13.388 1.426 1.00 36.06 ? 98 LEU B CA 1 ATOM 3303 C C . LEU B 2 98 ? 34.163 -13.874 0.456 1.00 36.49 ? 98 LEU B C 1 ATOM 3304 O O . LEU B 2 98 ? 34.350 -13.802 -0.774 1.00 36.28 ? 98 LEU B O 1 ATOM 3305 C CB . LEU B 2 98 ? 35.967 -14.589 2.048 1.00 35.88 ? 98 LEU B CB 1 ATOM 3306 C CG . LEU B 2 98 ? 36.712 -15.422 0.971 1.00 37.36 ? 98 LEU B CG 1 ATOM 3307 C CD1 . LEU B 2 98 ? 37.753 -14.590 0.226 1.00 36.00 ? 98 LEU B CD1 1 ATOM 3308 C CD2 . LEU B 2 98 ? 37.375 -16.658 1.566 1.00 40.14 ? 98 LEU B CD2 1 ATOM 3309 N N . LEU B 2 99 ? 33.056 -14.378 1.001 1.00 36.38 ? 99 LEU B N 1 ATOM 3310 C CA . LEU B 2 99 ? 31.972 -14.920 0.191 1.00 37.42 ? 99 LEU B CA 1 ATOM 3311 C C . LEU B 2 99 ? 31.524 -13.888 -0.835 1.00 36.99 ? 99 LEU B C 1 ATOM 3312 O O . LEU B 2 99 ? 31.245 -14.221 -1.984 1.00 37.31 ? 99 LEU B O 1 ATOM 3313 C CB . LEU B 2 99 ? 30.786 -15.356 1.065 1.00 37.81 ? 99 LEU B CB 1 ATOM 3314 C CG . LEU B 2 99 ? 29.471 -15.872 0.445 1.00 39.86 ? 99 LEU B CG 1 ATOM 3315 C CD1 . LEU B 2 99 ? 29.664 -16.884 -0.679 1.00 41.12 ? 99 LEU B CD1 1 ATOM 3316 C CD2 . LEU B 2 99 ? 28.621 -16.495 1.534 1.00 40.47 ? 99 LEU B CD2 1 ATOM 3317 N N . VAL B 2 100 ? 31.494 -12.635 -0.414 1.00 36.34 ? 100 VAL B N 1 ATOM 3318 C CA . VAL B 2 100 ? 31.048 -11.564 -1.270 1.00 35.73 ? 100 VAL B CA 1 ATOM 3319 C C . VAL B 2 100 ? 32.052 -11.227 -2.376 1.00 35.32 ? 100 VAL B C 1 ATOM 3320 O O . VAL B 2 100 ? 31.648 -11.027 -3.521 1.00 34.48 ? 100 VAL B O 1 ATOM 3321 C CB . VAL B 2 100 ? 30.643 -10.337 -0.446 1.00 36.31 ? 100 VAL B CB 1 ATOM 3322 C CG1 . VAL B 2 100 ? 30.375 -9.132 -1.359 1.00 35.41 ? 100 VAL B CG1 1 ATOM 3323 C CG2 . VAL B 2 100 ? 29.397 -10.667 0.366 1.00 35.56 ? 100 VAL B CG2 1 ATOM 3324 N N . LEU B 2 101 ? 33.345 -11.157 -2.050 1.00 34.46 ? 101 LEU B N 1 ATOM 3325 C CA . LEU B 2 101 ? 34.359 -10.939 -3.090 1.00 34.02 ? 101 LEU B CA 1 ATOM 3326 C C . LEU B 2 101 ? 34.355 -12.071 -4.099 1.00 32.98 ? 101 LEU B C 1 ATOM 3327 O O . LEU B 2 101 ? 34.442 -11.819 -5.296 1.00 31.90 ? 101 LEU B O 1 ATOM 3328 C CB . LEU B 2 101 ? 35.771 -10.822 -2.510 1.00 34.81 ? 101 LEU B CB 1 ATOM 3329 C CG . LEU B 2 101 ? 36.179 -9.705 -1.556 1.00 35.91 ? 101 LEU B CG 1 ATOM 3330 C CD1 . LEU B 2 101 ? 37.664 -9.858 -1.191 1.00 37.30 ? 101 LEU B CD1 1 ATOM 3331 C CD2 . LEU B 2 101 ? 35.890 -8.315 -2.121 1.00 35.78 ? 101 LEU B CD2 1 ATOM 3332 N N . MET B 2 102 ? 34.273 -13.313 -3.610 1.00 31.70 ? 102 MET B N 1 ATOM 3333 C CA . MET B 2 102 ? 34.327 -14.494 -4.473 1.00 32.24 ? 102 MET B CA 1 ATOM 3334 C C . MET B 2 102 ? 33.098 -14.585 -5.355 1.00 31.61 ? 102 MET B C 1 ATOM 3335 O O . MET B 2 102 ? 33.184 -14.834 -6.575 1.00 31.18 ? 102 MET B O 1 ATOM 3336 C CB . MET B 2 102 ? 34.469 -15.781 -3.651 1.00 31.98 ? 102 MET B CB 1 ATOM 3337 C CG . MET B 2 102 ? 35.888 -16.093 -3.205 1.00 35.29 ? 102 MET B CG 1 ATOM 3338 S SD . MET B 2 102 ? 35.892 -17.622 -2.219 1.00 42.52 ? 102 MET B SD 1 ATOM 3339 C CE . MET B 2 102 ? 37.618 -18.120 -2.321 1.00 43.46 ? 102 MET B CE 1 ATOM 3340 N N . GLU B 2 103 ? 31.941 -14.345 -4.760 1.00 31.19 ? 103 GLU B N 1 ATOM 3341 C CA . GLU B 2 103 ? 30.734 -14.415 -5.559 1.00 31.34 ? 103 GLU B CA 1 ATOM 3342 C C . GLU B 2 103 ? 30.581 -13.233 -6.531 1.00 30.14 ? 103 GLU B C 1 ATOM 3343 O O . GLU B 2 103 ? 30.065 -13.417 -7.624 1.00 30.12 ? 103 GLU B O 1 ATOM 3344 C CB . GLU B 2 103 ? 29.510 -14.685 -4.679 1.00 32.10 ? 103 GLU B CB 1 ATOM 3345 C CG . GLU B 2 103 ? 29.493 -16.164 -4.161 1.00 35.53 ? 103 GLU B CG 1 ATOM 3346 C CD . GLU B 2 103 ? 29.591 -17.213 -5.303 1.00 41.29 ? 103 GLU B CD 1 ATOM 3347 O OE1 . GLU B 2 103 ? 29.061 -16.948 -6.407 1.00 42.67 ? 103 GLU B OE1 1 ATOM 3348 O OE2 . GLU B 2 103 ? 30.203 -18.298 -5.106 1.00 42.26 ? 103 GLU B OE2 1 ATOM 3349 N N . ASN B 2 104 ? 31.067 -12.047 -6.161 1.00 29.14 ? 104 ASN B N 1 ATOM 3350 C CA . ASN B 2 104 ? 31.103 -10.922 -7.094 1.00 28.96 ? 104 ASN B CA 1 ATOM 3351 C C . ASN B 2 104 ? 31.927 -11.281 -8.350 1.00 28.84 ? 104 ASN B C 1 ATOM 3352 O O . ASN B 2 104 ? 31.463 -11.073 -9.483 1.00 28.64 ? 104 ASN B O 1 ATOM 3353 C CB . ASN B 2 104 ? 31.651 -9.661 -6.410 1.00 29.07 ? 104 ASN B CB 1 ATOM 3354 C CG . ASN B 2 104 ? 30.628 -9.013 -5.474 1.00 30.51 ? 104 ASN B CG 1 ATOM 3355 O OD1 . ASN B 2 104 ? 29.479 -9.447 -5.410 1.00 29.36 ? 104 ASN B OD1 1 ATOM 3356 N ND2 . ASN B 2 104 ? 31.044 -7.983 -4.748 1.00 28.82 ? 104 ASN B ND2 1 ATOM 3357 N N . GLU B 2 105 ? 33.134 -11.830 -8.143 1.00 28.05 ? 105 GLU B N 1 ATOM 3358 C CA . GLU B 2 105 ? 33.959 -12.291 -9.265 1.00 28.94 ? 105 GLU B CA 1 ATOM 3359 C C . GLU B 2 105 ? 33.153 -13.247 -10.149 1.00 28.33 ? 105 GLU B C 1 ATOM 3360 O O . GLU B 2 105 ? 33.082 -13.058 -11.370 1.00 26.98 ? 105 GLU B O 1 ATOM 3361 C CB . GLU B 2 105 ? 35.264 -12.951 -8.764 1.00 29.85 ? 105 GLU B CB 1 ATOM 3362 C CG . GLU B 2 105 ? 36.366 -13.132 -9.873 1.00 32.39 ? 105 GLU B CG 1 ATOM 3363 C CD . GLU B 2 105 ? 37.136 -11.831 -10.208 1.00 36.06 ? 105 GLU B CD 1 ATOM 3364 O OE1 . GLU B 2 105 ? 37.552 -11.115 -9.268 1.00 35.34 ? 105 GLU B OE1 1 ATOM 3365 O OE2 . GLU B 2 105 ? 37.334 -11.523 -11.412 1.00 35.31 ? 105 GLU B OE2 1 ATOM 3366 N N . HIS B 2 106 ? 32.536 -14.267 -9.541 1.00 27.50 ? 106 HIS B N 1 ATOM 3367 C CA . HIS B 2 106 ? 31.774 -15.233 -10.314 1.00 28.58 ? 106 HIS B CA 1 ATOM 3368 C C . HIS B 2 106 ? 30.563 -14.613 -11.026 1.00 28.43 ? 106 HIS B C 1 ATOM 3369 O O . HIS B 2 106 ? 30.270 -14.975 -12.181 1.00 28.72 ? 106 HIS B O 1 ATOM 3370 C CB . HIS B 2 106 ? 31.355 -16.433 -9.448 1.00 29.17 ? 106 HIS B CB 1 ATOM 3371 C CG . HIS B 2 106 ? 32.508 -17.283 -8.992 1.00 32.49 ? 106 HIS B CG 1 ATOM 3372 N ND1 . HIS B 2 106 ? 33.600 -17.560 -9.790 1.00 36.56 ? 106 HIS B ND1 1 ATOM 3373 C CD2 . HIS B 2 106 ? 32.732 -17.926 -7.820 1.00 36.60 ? 106 HIS B CD2 1 ATOM 3374 C CE1 . HIS B 2 106 ? 34.442 -18.337 -9.137 1.00 39.04 ? 106 HIS B CE1 1 ATOM 3375 N NE2 . HIS B 2 106 ? 33.942 -18.566 -7.936 1.00 40.78 ? 106 HIS B NE2 1 ATOM 3376 N N . THR B 2 107 ? 29.855 -13.702 -10.343 1.00 27.95 ? 107 THR B N 1 ATOM 3377 C CA . THR B 2 107 ? 28.708 -13.013 -10.942 1.00 28.50 ? 107 THR B CA 1 ATOM 3378 C C . THR B 2 107 ? 29.101 -12.277 -12.223 1.00 28.21 ? 107 THR B C 1 ATOM 3379 O O . THR B 2 107 ? 28.425 -12.405 -13.255 1.00 28.12 ? 107 THR B O 1 ATOM 3380 C CB . THR B 2 107 ? 28.048 -12.043 -9.950 1.00 28.57 ? 107 THR B CB 1 ATOM 3381 O OG1 . THR B 2 107 ? 27.405 -12.808 -8.921 1.00 29.79 ? 107 THR B OG1 1 ATOM 3382 C CG2 . THR B 2 107 ? 27.019 -11.159 -10.649 1.00 29.34 ? 107 THR B CG2 1 ATOM 3383 N N . LEU B 2 108 ? 30.189 -11.510 -12.155 1.00 28.02 ? 108 LEU B N 1 ATOM 3384 C CA . LEU B 2 108 ? 30.638 -10.712 -13.305 1.00 28.72 ? 108 LEU B CA 1 ATOM 3385 C C . LEU B 2 108 ? 31.032 -11.615 -14.480 1.00 28.46 ? 108 LEU B C 1 ATOM 3386 O O . LEU B 2 108 ? 30.684 -11.345 -15.633 1.00 29.12 ? 108 LEU B O 1 ATOM 3387 C CB . LEU B 2 108 ? 31.769 -9.725 -12.906 1.00 28.90 ? 108 LEU B CB 1 ATOM 3388 C CG . LEU B 2 108 ? 31.355 -8.659 -11.876 1.00 29.07 ? 108 LEU B CG 1 ATOM 3389 C CD1 . LEU B 2 108 ? 32.401 -7.565 -11.711 1.00 29.40 ? 108 LEU B CD1 1 ATOM 3390 C CD2 . LEU B 2 108 ? 30.014 -8.010 -12.262 1.00 29.70 ? 108 LEU B CD2 1 ATOM 3391 N N . ASP B 2 109 ? 31.740 -12.697 -14.176 1.00 28.37 ? 109 ASP B N 1 ATOM 3392 C CA . ASP B 2 109 ? 32.076 -13.719 -15.176 1.00 27.75 ? 109 ASP B CA 1 ATOM 3393 C C . ASP B 2 109 ? 30.862 -14.502 -15.708 1.00 27.16 ? 109 ASP B C 1 ATOM 3394 O O . ASP B 2 109 ? 30.839 -14.930 -16.874 1.00 25.94 ? 109 ASP B O 1 ATOM 3395 C CB . ASP B 2 109 ? 33.156 -14.663 -14.629 1.00 27.80 ? 109 ASP B CB 1 ATOM 3396 C CG . ASP B 2 109 ? 34.498 -13.964 -14.449 1.00 29.80 ? 109 ASP B CG 1 ATOM 3397 O OD1 . ASP B 2 109 ? 34.780 -13.010 -15.203 1.00 33.28 ? 109 ASP B OD1 1 ATOM 3398 O OD2 . ASP B 2 109 ? 35.272 -14.352 -13.550 1.00 30.50 ? 109 ASP B OD2 1 ATOM 3399 N N . PHE B 2 110 ? 29.854 -14.668 -14.863 1.00 26.51 ? 110 PHE B N 1 ATOM 3400 C CA . PHE B 2 110 ? 28.614 -15.326 -15.270 1.00 27.07 ? 110 PHE B CA 1 ATOM 3401 C C . PHE B 2 110 ? 27.903 -14.493 -16.367 1.00 26.91 ? 110 PHE B C 1 ATOM 3402 O O . PHE B 2 110 ? 27.479 -15.027 -17.382 1.00 26.82 ? 110 PHE B O 1 ATOM 3403 C CB . PHE B 2 110 ? 27.724 -15.523 -14.029 1.00 26.69 ? 110 PHE B CB 1 ATOM 3404 C CG . PHE B 2 110 ? 26.346 -16.073 -14.316 1.00 27.61 ? 110 PHE B CG 1 ATOM 3405 C CD1 . PHE B 2 110 ? 26.174 -17.314 -14.927 1.00 28.09 ? 110 PHE B CD1 1 ATOM 3406 C CD2 . PHE B 2 110 ? 25.220 -15.369 -13.919 1.00 27.83 ? 110 PHE B CD2 1 ATOM 3407 C CE1 . PHE B 2 110 ? 24.889 -17.831 -15.161 1.00 29.76 ? 110 PHE B CE1 1 ATOM 3408 C CE2 . PHE B 2 110 ? 23.930 -15.881 -14.138 1.00 29.43 ? 110 PHE B CE2 1 ATOM 3409 C CZ . PHE B 2 110 ? 23.766 -17.117 -14.743 1.00 28.36 ? 110 PHE B CZ 1 ATOM 3410 N N . HIS B 2 111 ? 27.782 -13.190 -16.154 1.00 27.47 ? 111 HIS B N 1 ATOM 3411 C CA . HIS B 2 111 ? 27.195 -12.306 -17.166 1.00 28.30 ? 111 HIS B CA 1 ATOM 3412 C C . HIS B 2 111 ? 28.011 -12.365 -18.468 1.00 28.43 ? 111 HIS B C 1 ATOM 3413 O O . HIS B 2 111 ? 27.469 -12.405 -19.577 1.00 28.43 ? 111 HIS B O 1 ATOM 3414 C CB . HIS B 2 111 ? 27.162 -10.877 -16.629 1.00 29.12 ? 111 HIS B CB 1 ATOM 3415 C CG . HIS B 2 111 ? 26.132 -10.651 -15.572 1.00 30.09 ? 111 HIS B CG 1 ATOM 3416 N ND1 . HIS B 2 111 ? 24.779 -10.692 -15.834 1.00 33.34 ? 111 HIS B ND1 1 ATOM 3417 C CD2 . HIS B 2 111 ? 26.252 -10.374 -14.251 1.00 31.75 ? 111 HIS B CD2 1 ATOM 3418 C CE1 . HIS B 2 111 ? 24.108 -10.446 -14.720 1.00 32.59 ? 111 HIS B CE1 1 ATOM 3419 N NE2 . HIS B 2 111 ? 24.978 -10.246 -13.745 1.00 32.25 ? 111 HIS B NE2 1 ATOM 3420 N N . ASP B 2 112 ? 29.326 -12.410 -18.323 1.00 27.76 ? 112 ASP B N 1 ATOM 3421 C CA . ASP B 2 112 ? 30.236 -12.461 -19.473 1.00 28.12 ? 112 ASP B CA 1 ATOM 3422 C C . ASP B 2 112 ? 30.037 -13.759 -20.269 1.00 27.73 ? 112 ASP B C 1 ATOM 3423 O O . ASP B 2 112 ? 29.921 -13.719 -21.506 1.00 26.81 ? 112 ASP B O 1 ATOM 3424 C CB . ASP B 2 112 ? 31.678 -12.319 -18.947 1.00 28.53 ? 112 ASP B CB 1 ATOM 3425 C CG . ASP B 2 112 ? 32.709 -12.026 -20.028 1.00 30.65 ? 112 ASP B CG 1 ATOM 3426 O OD1 . ASP B 2 112 ? 32.385 -11.657 -21.199 1.00 30.06 ? 112 ASP B OD1 1 ATOM 3427 O OD2 . ASP B 2 112 ? 33.901 -12.146 -19.661 1.00 31.06 ? 112 ASP B OD2 1 ATOM 3428 N N . SER B 2 113 ? 29.972 -14.886 -19.566 1.00 26.98 ? 113 SER B N 1 ATOM 3429 C CA . SER B 2 113 ? 29.628 -16.183 -20.182 1.00 27.71 ? 113 SER B CA 1 ATOM 3430 C C . SER B 2 113 ? 28.277 -16.126 -20.904 1.00 26.76 ? 113 SER B C 1 ATOM 3431 O O . SER B 2 113 ? 28.142 -16.650 -21.998 1.00 27.57 ? 113 SER B O 1 ATOM 3432 C CB . SER B 2 113 ? 29.573 -17.285 -19.122 1.00 27.11 ? 113 SER B CB 1 ATOM 3433 O OG . SER B 2 113 ? 28.899 -18.448 -19.612 1.00 29.36 ? 113 SER B OG 1 ATOM 3434 N N . ASN B 2 114 ? 27.286 -15.486 -20.288 1.00 27.71 ? 114 ASN B N 1 ATOM 3435 C CA . ASN B 2 114 ? 25.937 -15.427 -20.858 1.00 28.18 ? 114 ASN B CA 1 ATOM 3436 C C . ASN B 2 114 ? 25.915 -14.666 -22.183 1.00 28.54 ? 114 ASN B C 1 ATOM 3437 O O . ASN B 2 114 ? 25.193 -15.036 -23.101 1.00 29.47 ? 114 ASN B O 1 ATOM 3438 C CB . ASN B 2 114 ? 24.952 -14.797 -19.877 1.00 28.16 ? 114 ASN B CB 1 ATOM 3439 C CG . ASN B 2 114 ? 24.659 -15.693 -18.678 1.00 27.95 ? 114 ASN B CG 1 ATOM 3440 O OD1 . ASN B 2 114 ? 24.863 -16.908 -18.724 1.00 27.41 ? 114 ASN B OD1 1 ATOM 3441 N ND2 . ASN B 2 114 ? 24.203 -15.086 -17.595 1.00 28.21 ? 114 ASN B ND2 1 ATOM 3442 N N . VAL B 2 115 ? 26.716 -13.609 -22.269 1.00 28.97 ? 115 VAL B N 1 ATOM 3443 C CA . VAL B 2 115 ? 26.821 -12.806 -23.491 1.00 28.14 ? 115 VAL B CA 1 ATOM 3444 C C . VAL B 2 115 ? 27.548 -13.593 -24.567 1.00 28.56 ? 115 VAL B C 1 ATOM 3445 O O . VAL B 2 115 ? 27.076 -13.697 -25.720 1.00 28.72 ? 115 VAL B O 1 ATOM 3446 C CB . VAL B 2 115 ? 27.576 -11.463 -23.240 1.00 28.54 ? 115 VAL B CB 1 ATOM 3447 C CG1 . VAL B 2 115 ? 27.864 -10.754 -24.583 1.00 27.14 ? 115 VAL B CG1 1 ATOM 3448 C CG2 . VAL B 2 115 ? 26.776 -10.550 -22.297 1.00 28.33 ? 115 VAL B CG2 1 ATOM 3449 N N . LYS B 2 116 ? 28.698 -14.144 -24.210 1.00 29.05 ? 116 LYS B N 1 ATOM 3450 C CA . LYS B 2 116 ? 29.438 -15.006 -25.148 1.00 29.83 ? 116 LYS B CA 1 ATOM 3451 C C . LYS B 2 116 ? 28.554 -16.152 -25.663 1.00 29.43 ? 116 LYS B C 1 ATOM 3452 O O . LYS B 2 116 ? 28.528 -16.442 -26.865 1.00 29.24 ? 116 LYS B O 1 ATOM 3453 C CB . LYS B 2 116 ? 30.731 -15.554 -24.508 1.00 29.89 ? 116 LYS B CB 1 ATOM 3454 C CG . LYS B 2 116 ? 31.421 -16.584 -25.423 1.00 33.62 ? 116 LYS B CG 1 ATOM 3455 C CD . LYS B 2 116 ? 32.689 -17.186 -24.847 1.00 39.64 ? 116 LYS B CD 1 ATOM 3456 C CE . LYS B 2 116 ? 33.449 -17.982 -25.929 1.00 41.51 ? 116 LYS B CE 1 ATOM 3457 N NZ . LYS B 2 116 ? 33.735 -17.104 -27.066 1.00 44.72 ? 116 LYS B NZ 1 ATOM 3458 N N . ASN B 2 117 ? 27.840 -16.806 -24.752 1.00 29.47 ? 117 ASN B N 1 ATOM 3459 C CA . ASN B 2 117 ? 26.949 -17.907 -25.130 1.00 30.39 ? 117 ASN B CA 1 ATOM 3460 C C . ASN B 2 117 ? 25.835 -17.521 -26.099 1.00 30.02 ? 117 ASN B C 1 ATOM 3461 O O . ASN B 2 117 ? 25.567 -18.266 -27.045 1.00 30.54 ? 117 ASN B O 1 ATOM 3462 C CB . ASN B 2 117 ? 26.373 -18.610 -23.904 1.00 30.37 ? 117 ASN B CB 1 ATOM 3463 C CG . ASN B 2 117 ? 27.384 -19.527 -23.234 1.00 31.78 ? 117 ASN B CG 1 ATOM 3464 O OD1 . ASN B 2 117 ? 28.468 -19.791 -23.770 1.00 32.34 ? 117 ASN B OD1 1 ATOM 3465 N ND2 . ASN B 2 117 ? 27.034 -20.013 -22.043 1.00 32.57 ? 117 ASN B ND2 1 ATOM 3466 N N . LEU B 2 118 ? 25.216 -16.364 -25.869 1.00 30.32 ? 118 LEU B N 1 ATOM 3467 C CA . LEU B 2 118 ? 24.185 -15.820 -26.765 1.00 30.46 ? 118 LEU B CA 1 ATOM 3468 C C . LEU B 2 118 ? 24.765 -15.488 -28.152 1.00 30.33 ? 118 LEU B C 1 ATOM 3469 O O . LEU B 2 118 ? 24.195 -15.850 -29.182 1.00 30.46 ? 118 LEU B O 1 ATOM 3470 C CB . LEU B 2 118 ? 23.512 -14.589 -26.140 1.00 30.81 ? 118 LEU B CB 1 ATOM 3471 C CG . LEU B 2 118 ? 22.454 -13.873 -26.995 1.00 33.16 ? 118 LEU B CG 1 ATOM 3472 C CD1 . LEU B 2 118 ? 21.260 -14.779 -27.287 1.00 35.16 ? 118 LEU B CD1 1 ATOM 3473 C CD2 . LEU B 2 118 ? 22.007 -12.594 -26.306 1.00 34.29 ? 118 LEU B CD2 1 ATOM 3474 N N . TYR B 2 119 ? 25.917 -14.830 -28.156 1.00 29.74 ? 119 TYR B N 1 ATOM 3475 C CA . TYR B 2 119 ? 26.672 -14.591 -29.379 1.00 30.04 ? 119 TYR B CA 1 ATOM 3476 C C . TYR B 2 119 ? 26.937 -15.881 -30.152 1.00 30.71 ? 119 TYR B C 1 ATOM 3477 O O . TYR B 2 119 ? 26.721 -15.932 -31.374 1.00 29.88 ? 119 TYR B O 1 ATOM 3478 C CB . TYR B 2 119 ? 27.982 -13.883 -29.046 1.00 29.45 ? 119 TYR B CB 1 ATOM 3479 C CG . TYR B 2 119 ? 28.801 -13.563 -30.256 1.00 30.37 ? 119 TYR B CG 1 ATOM 3480 C CD1 . TYR B 2 119 ? 28.561 -12.411 -31.003 1.00 32.31 ? 119 TYR B CD1 1 ATOM 3481 C CD2 . TYR B 2 119 ? 29.804 -14.426 -30.679 1.00 31.37 ? 119 TYR B CD2 1 ATOM 3482 C CE1 . TYR B 2 119 ? 29.326 -12.124 -32.165 1.00 31.31 ? 119 TYR B CE1 1 ATOM 3483 C CE2 . TYR B 2 119 ? 30.551 -14.154 -31.832 1.00 33.41 ? 119 TYR B CE2 1 ATOM 3484 C CZ . TYR B 2 119 ? 30.299 -13.003 -32.557 1.00 31.87 ? 119 TYR B CZ 1 ATOM 3485 O OH . TYR B 2 119 ? 31.051 -12.755 -33.660 1.00 34.22 ? 119 TYR B OH 1 ATOM 3486 N N . ASP B 2 120 ? 27.423 -16.907 -29.449 1.00 31.19 ? 120 ASP B N 1 ATOM 3487 C CA . ASP B 2 120 ? 27.769 -18.171 -30.087 1.00 33.33 ? 120 ASP B CA 1 ATOM 3488 C C . ASP B 2 120 ? 26.532 -18.865 -30.602 1.00 34.26 ? 120 ASP B C 1 ATOM 3489 O O . ASP B 2 120 ? 26.559 -19.413 -31.692 1.00 35.27 ? 120 ASP B O 1 ATOM 3490 C CB . ASP B 2 120 ? 28.510 -19.095 -29.137 1.00 33.70 ? 120 ASP B CB 1 ATOM 3491 C CG . ASP B 2 120 ? 29.959 -18.757 -29.027 1.00 36.03 ? 120 ASP B CG 1 ATOM 3492 O OD1 . ASP B 2 120 ? 30.528 -18.221 -30.009 1.00 40.14 ? 120 ASP B OD1 1 ATOM 3493 O OD2 . ASP B 2 120 ? 30.545 -19.048 -27.976 1.00 36.36 ? 120 ASP B OD2 1 ATOM 3494 N N . LYS B 2 121 ? 25.450 -18.809 -29.826 1.00 34.83 ? 121 LYS B N 1 ATOM 3495 C CA . LYS B 2 121 ? 24.164 -19.351 -30.262 1.00 36.84 ? 121 LYS B CA 1 ATOM 3496 C C . LYS B 2 121 ? 23.746 -18.743 -31.602 1.00 37.05 ? 121 LYS B C 1 ATOM 3497 O O . LYS B 2 121 ? 23.379 -19.465 -32.532 1.00 38.16 ? 121 LYS B O 1 ATOM 3498 C CB . LYS B 2 121 ? 23.088 -19.102 -29.198 1.00 36.67 ? 121 LYS B CB 1 ATOM 3499 C CG . LYS B 2 121 ? 21.932 -20.088 -29.265 1.00 40.93 ? 121 LYS B CG 1 ATOM 3500 C CD . LYS B 2 121 ? 20.820 -19.758 -28.264 1.00 44.07 ? 121 LYS B CD 1 ATOM 3501 C CE . LYS B 2 121 ? 19.673 -20.802 -28.330 1.00 47.67 ? 121 LYS B CE 1 ATOM 3502 N NZ . LYS B 2 121 ? 19.296 -21.229 -29.730 1.00 49.56 ? 121 LYS B NZ 1 ATOM 3503 N N . VAL B 2 122 ? 23.828 -17.418 -31.707 1.00 36.88 ? 122 VAL B N 1 ATOM 3504 C CA . VAL B 2 122 ? 23.463 -16.728 -32.946 1.00 36.82 ? 122 VAL B CA 1 ATOM 3505 C C . VAL B 2 122 ? 24.419 -17.104 -34.095 1.00 36.64 ? 122 VAL B C 1 ATOM 3506 O O . VAL B 2 122 ? 23.972 -17.499 -35.181 1.00 36.34 ? 122 VAL B O 1 ATOM 3507 C CB . VAL B 2 122 ? 23.359 -15.199 -32.713 1.00 37.06 ? 122 VAL B CB 1 ATOM 3508 C CG1 . VAL B 2 122 ? 23.291 -14.425 -34.040 1.00 36.36 ? 122 VAL B CG1 1 ATOM 3509 C CG2 . VAL B 2 122 ? 22.156 -14.884 -31.826 1.00 36.58 ? 122 VAL B CG2 1 ATOM 3510 N N . ARG B 2 123 ? 25.726 -17.001 -33.840 1.00 36.46 ? 123 ARG B N 1 ATOM 3511 C CA . ARG B 2 123 ? 26.768 -17.382 -34.794 1.00 37.03 ? 123 ARG B CA 1 ATOM 3512 C C . ARG B 2 123 ? 26.573 -18.797 -35.359 1.00 38.42 ? 123 ARG B C 1 ATOM 3513 O O . ARG B 2 123 ? 26.581 -18.994 -36.586 1.00 38.18 ? 123 ARG B O 1 ATOM 3514 C CB . ARG B 2 123 ? 28.163 -17.253 -34.145 1.00 36.83 ? 123 ARG B CB 1 ATOM 3515 C CG . ARG B 2 123 ? 29.321 -17.725 -35.018 1.00 37.24 ? 123 ARG B CG 1 ATOM 3516 C CD . ARG B 2 123 ? 30.681 -17.589 -34.347 1.00 38.44 ? 123 ARG B CD 1 ATOM 3517 N NE . ARG B 2 123 ? 30.833 -18.397 -33.133 1.00 40.29 ? 123 ARG B NE 1 ATOM 3518 C CZ . ARG B 2 123 ? 31.188 -19.687 -33.117 1.00 42.72 ? 123 ARG B CZ 1 ATOM 3519 N NH1 . ARG B 2 123 ? 31.418 -20.355 -34.254 1.00 41.64 ? 123 ARG B NH1 1 ATOM 3520 N NH2 . ARG B 2 123 ? 31.303 -20.317 -31.961 1.00 40.80 ? 123 ARG B NH2 1 ATOM 3521 N N . MET B 2 124 ? 26.420 -19.766 -34.460 1.00 39.69 ? 124 MET B N 1 ATOM 3522 C CA . MET B 2 124 ? 26.347 -21.173 -34.830 1.00 42.34 ? 124 MET B CA 1 ATOM 3523 C C . MET B 2 124 ? 25.074 -21.491 -35.599 1.00 43.07 ? 124 MET B C 1 ATOM 3524 O O . MET B 2 124 ? 24.992 -22.516 -36.275 1.00 44.50 ? 124 MET B O 1 ATOM 3525 C CB . MET B 2 124 ? 26.503 -22.082 -33.604 1.00 42.88 ? 124 MET B CB 1 ATOM 3526 C CG . MET B 2 124 ? 27.936 -22.123 -33.058 1.00 45.81 ? 124 MET B CG 1 ATOM 3527 S SD . MET B 2 124 ? 28.210 -23.205 -31.622 1.00 52.72 ? 124 MET B SD 1 ATOM 3528 C CE . MET B 2 124 ? 28.178 -24.825 -32.407 1.00 50.90 ? 124 MET B CE 1 ATOM 3529 N N . GLN B 2 125 ? 24.099 -20.587 -35.522 1.00 43.43 ? 125 GLN B N 1 ATOM 3530 C CA . GLN B 2 125 ? 22.873 -20.671 -36.320 1.00 43.81 ? 125 GLN B CA 1 ATOM 3531 C C . GLN B 2 125 ? 22.980 -19.999 -37.715 1.00 42.93 ? 125 GLN B C 1 ATOM 3532 O O . GLN B 2 125 ? 22.559 -20.578 -38.734 1.00 43.49 ? 125 GLN B O 1 ATOM 3533 C CB . GLN B 2 125 ? 21.680 -20.128 -35.507 1.00 44.34 ? 125 GLN B CB 1 ATOM 3534 C CG . GLN B 2 125 ? 20.322 -20.380 -36.177 1.00 48.42 ? 125 GLN B CG 1 ATOM 3535 C CD . GLN B 2 125 ? 19.132 -20.306 -35.220 1.00 50.28 ? 125 GLN B CD 1 ATOM 3536 O OE1 . GLN B 2 125 ? 18.607 -19.225 -34.948 1.00 49.91 ? 125 GLN B OE1 1 ATOM 3537 N NE2 . GLN B 2 125 ? 18.669 -21.468 -34.752 1.00 51.50 ? 125 GLN B NE2 1 ATOM 3538 N N . LEU B 2 126 ? 23.540 -18.791 -37.772 1.00 41.04 ? 126 LEU B N 1 ATOM 3539 C CA . LEU B 2 126 ? 23.721 -18.077 -39.042 1.00 39.96 ? 126 LEU B CA 1 ATOM 3540 C C . LEU B 2 126 ? 24.756 -18.703 -39.972 1.00 40.41 ? 126 LEU B C 1 ATOM 3541 O O . LEU B 2 126 ? 24.688 -18.529 -41.198 1.00 39.91 ? 126 LEU B O 1 ATOM 3542 C CB . LEU B 2 126 ? 24.097 -16.617 -38.793 1.00 38.83 ? 126 LEU B CB 1 ATOM 3543 C CG . LEU B 2 126 ? 23.116 -15.802 -37.949 1.00 38.01 ? 126 LEU B CG 1 ATOM 3544 C CD1 . LEU B 2 126 ? 23.660 -14.390 -37.710 1.00 35.89 ? 126 LEU B CD1 1 ATOM 3545 C CD2 . LEU B 2 126 ? 21.717 -15.778 -38.562 1.00 36.65 ? 126 LEU B CD2 1 ATOM 3546 N N . ARG B 2 127 ? 25.712 -19.416 -39.379 1.00 41.39 ? 127 ARG B N 1 ATOM 3547 C CA . ARG B 2 127 ? 26.809 -20.066 -40.103 1.00 42.89 ? 127 ARG B CA 1 ATOM 3548 C C . ARG B 2 127 ? 27.420 -19.133 -41.154 1.00 42.87 ? 127 ARG B C 1 ATOM 3549 O O . ARG B 2 127 ? 27.660 -17.955 -40.860 1.00 42.21 ? 127 ARG B O 1 ATOM 3550 C CB . ARG B 2 127 ? 26.351 -21.412 -40.688 1.00 43.85 ? 127 ARG B CB 1 ATOM 3551 C CG . ARG B 2 127 ? 26.014 -22.442 -39.611 1.00 45.15 ? 127 ARG B CG 1 ATOM 3552 C CD . ARG B 2 127 ? 25.211 -23.628 -40.163 1.00 47.64 ? 127 ARG B CD 1 ATOM 3553 N NE . ARG B 2 127 ? 25.887 -24.283 -41.283 1.00 51.52 ? 127 ARG B NE 1 ATOM 3554 C CZ . ARG B 2 127 ? 25.489 -25.426 -41.848 1.00 53.75 ? 127 ARG B CZ 1 ATOM 3555 N NH1 . ARG B 2 127 ? 24.412 -26.069 -41.399 1.00 52.49 ? 127 ARG B NH1 1 ATOM 3556 N NH2 . ARG B 2 127 ? 26.170 -25.933 -42.871 1.00 56.42 ? 127 ARG B NH2 1 ATOM 3557 N N . ASP B 2 128 ? 27.644 -19.629 -42.375 1.00 43.66 ? 128 ASP B N 1 ATOM 3558 C CA . ASP B 2 128 ? 28.240 -18.795 -43.420 1.00 43.48 ? 128 ASP B CA 1 ATOM 3559 C C . ASP B 2 128 ? 27.239 -17.943 -44.233 1.00 43.02 ? 128 ASP B C 1 ATOM 3560 O O . ASP B 2 128 ? 27.581 -17.424 -45.292 1.00 44.26 ? 128 ASP B O 1 ATOM 3561 C CB . ASP B 2 128 ? 29.158 -19.635 -44.338 1.00 44.59 ? 128 ASP B CB 1 ATOM 3562 C CG . ASP B 2 128 ? 28.391 -20.658 -45.165 1.00 45.13 ? 128 ASP B CG 1 ATOM 3563 O OD1 . ASP B 2 128 ? 27.216 -20.926 -44.835 1.00 45.88 ? 128 ASP B OD1 1 ATOM 3564 O OD2 . ASP B 2 128 ? 28.959 -21.191 -46.150 1.00 47.59 ? 128 ASP B OD2 1 ATOM 3565 N N . ASN B 2 129 ? 26.013 -17.786 -43.746 1.00 42.23 ? 129 ASN B N 1 ATOM 3566 C CA . ASN B 2 129 ? 25.096 -16.840 -44.362 1.00 41.31 ? 129 ASN B CA 1 ATOM 3567 C C . ASN B 2 129 ? 25.394 -15.391 -43.975 1.00 40.31 ? 129 ASN B C 1 ATOM 3568 O O . ASN B 2 129 ? 24.727 -14.460 -44.455 1.00 40.30 ? 129 ASN B O 1 ATOM 3569 C CB . ASN B 2 129 ? 23.630 -17.196 -44.046 1.00 42.19 ? 129 ASN B CB 1 ATOM 3570 C CG . ASN B 2 129 ? 23.124 -18.424 -44.819 1.00 43.97 ? 129 ASN B CG 1 ATOM 3571 O OD1 . ASN B 2 129 ? 23.821 -18.982 -45.668 1.00 45.10 ? 129 ASN B OD1 1 ATOM 3572 N ND2 . ASN B 2 129 ? 21.901 -18.844 -44.514 1.00 45.94 ? 129 ASN B ND2 1 ATOM 3573 N N . VAL B 2 130 ? 26.385 -15.205 -43.097 1.00 39.29 ? 130 VAL B N 1 ATOM 3574 C CA . VAL B 2 130 ? 26.798 -13.886 -42.593 1.00 37.96 ? 130 VAL B CA 1 ATOM 3575 C C . VAL B 2 130 ? 28.327 -13.748 -42.531 1.00 38.08 ? 130 VAL B C 1 ATOM 3576 O O . VAL B 2 130 ? 29.051 -14.741 -42.522 1.00 37.92 ? 130 VAL B O 1 ATOM 3577 C CB . VAL B 2 130 ? 26.229 -13.610 -41.156 1.00 37.46 ? 130 VAL B CB 1 ATOM 3578 C CG1 . VAL B 2 130 ? 24.696 -13.605 -41.148 1.00 36.49 ? 130 VAL B CG1 1 ATOM 3579 C CG2 . VAL B 2 130 ? 26.778 -14.627 -40.140 1.00 36.39 ? 130 VAL B CG2 1 ATOM 3580 N N . LYS B 2 131 ? 28.798 -12.501 -42.492 1.00 38.94 ? 131 LYS B N 1 ATOM 3581 C CA . LYS B 2 131 ? 30.189 -12.151 -42.185 1.00 40.48 ? 131 LYS B CA 1 ATOM 3582 C C . LYS B 2 131 ? 30.239 -11.898 -40.686 1.00 39.50 ? 131 LYS B C 1 ATOM 3583 O O . LYS B 2 131 ? 29.396 -11.180 -40.181 1.00 38.98 ? 131 LYS B O 1 ATOM 3584 C CB . LYS B 2 131 ? 30.583 -10.834 -42.880 1.00 41.55 ? 131 LYS B CB 1 ATOM 3585 C CG . LYS B 2 131 ? 31.484 -10.940 -44.093 1.00 44.93 ? 131 LYS B CG 1 ATOM 3586 C CD . LYS B 2 131 ? 31.700 -9.561 -44.737 1.00 49.13 ? 131 LYS B CD 1 ATOM 3587 C CE . LYS B 2 131 ? 30.740 -9.307 -45.921 1.00 51.78 ? 131 LYS B CE 1 ATOM 3588 N NZ . LYS B 2 131 ? 31.294 -9.738 -47.266 1.00 54.04 ? 131 LYS B NZ 1 ATOM 3589 N N . GLU B 2 132 ? 31.221 -12.475 -39.996 1.00 40.06 ? 132 GLU B N 1 ATOM 3590 C CA . GLU B 2 132 ? 31.481 -12.180 -38.583 1.00 40.10 ? 132 GLU B CA 1 ATOM 3591 C C . GLU B 2 132 ? 32.408 -10.958 -38.508 1.00 40.64 ? 132 GLU B C 1 ATOM 3592 O O . GLU B 2 132 ? 33.606 -11.090 -38.742 1.00 41.30 ? 132 GLU B O 1 ATOM 3593 C CB . GLU B 2 132 ? 32.211 -13.363 -37.944 1.00 40.74 ? 132 GLU B CB 1 ATOM 3594 C CG . GLU B 2 132 ? 31.475 -14.126 -36.881 1.00 41.30 ? 132 GLU B CG 1 ATOM 3595 C CD . GLU B 2 132 ? 32.443 -14.859 -35.951 1.00 43.91 ? 132 GLU B CD 1 ATOM 3596 O OE1 . GLU B 2 132 ? 32.456 -14.599 -34.721 1.00 41.68 ? 132 GLU B OE1 1 ATOM 3597 O OE2 . GLU B 2 132 ? 33.198 -15.696 -36.461 1.00 46.68 ? 132 GLU B OE2 1 ATOM 3598 N N . LEU B 2 133 ? 31.882 -9.783 -38.170 1.00 40.63 ? 133 LEU B N 1 ATOM 3599 C CA . LEU B 2 133 ? 32.706 -8.562 -38.191 1.00 41.95 ? 133 LEU B CA 1 ATOM 3600 C C . LEU B 2 133 ? 33.761 -8.433 -37.097 1.00 42.22 ? 133 LEU B C 1 ATOM 3601 O O . LEU B 2 133 ? 34.742 -7.712 -37.281 1.00 43.71 ? 133 LEU B O 1 ATOM 3602 C CB . LEU B 2 133 ? 31.858 -7.294 -38.278 1.00 42.06 ? 133 LEU B CB 1 ATOM 3603 C CG . LEU B 2 133 ? 30.965 -7.192 -39.515 1.00 43.07 ? 133 LEU B CG 1 ATOM 3604 C CD1 . LEU B 2 133 ? 30.096 -5.964 -39.385 1.00 44.70 ? 133 LEU B CD1 1 ATOM 3605 C CD2 . LEU B 2 133 ? 31.782 -7.144 -40.806 1.00 44.95 ? 133 LEU B CD2 1 ATOM 3606 N N . GLY B 2 134 ? 33.571 -9.123 -35.971 1.00 41.65 ? 134 GLY B N 1 ATOM 3607 C CA . GLY B 2 134 ? 34.576 -9.153 -34.908 1.00 41.41 ? 134 GLY B CA 1 ATOM 3608 C C . GLY B 2 134 ? 34.293 -8.266 -33.709 1.00 41.68 ? 134 GLY B C 1 ATOM 3609 O O . GLY B 2 134 ? 35.059 -8.256 -32.747 1.00 42.63 ? 134 GLY B O 1 ATOM 3610 N N . ASN B 2 135 ? 33.192 -7.525 -33.774 1.00 41.20 ? 135 ASN B N 1 ATOM 3611 C CA . ASN B 2 135 ? 32.804 -6.531 -32.771 1.00 40.94 ? 135 ASN B CA 1 ATOM 3612 C C . ASN B 2 135 ? 31.475 -6.912 -32.115 1.00 39.35 ? 135 ASN B C 1 ATOM 3613 O O . ASN B 2 135 ? 30.827 -6.076 -31.492 1.00 38.89 ? 135 ASN B O 1 ATOM 3614 C CB . ASN B 2 135 ? 32.648 -5.160 -33.458 1.00 41.92 ? 135 ASN B CB 1 ATOM 3615 C CG . ASN B 2 135 ? 31.625 -5.187 -34.589 1.00 43.11 ? 135 ASN B CG 1 ATOM 3616 O OD1 . ASN B 2 135 ? 31.227 -6.258 -35.052 1.00 42.25 ? 135 ASN B OD1 1 ATOM 3617 N ND2 . ASN B 2 135 ? 31.198 -4.005 -35.045 1.00 46.39 ? 135 ASN B ND2 1 ATOM 3618 N N . GLY B 2 136 ? 31.053 -8.163 -32.293 1.00 38.25 ? 136 GLY B N 1 ATOM 3619 C CA . GLY B 2 136 ? 29.748 -8.614 -31.797 1.00 37.30 ? 136 GLY B CA 1 ATOM 3620 C C . GLY B 2 136 ? 28.658 -8.598 -32.873 1.00 37.47 ? 136 GLY B C 1 ATOM 3621 O O . GLY B 2 136 ? 27.545 -9.050 -32.626 1.00 36.80 ? 136 GLY B O 1 ATOM 3622 N N . CYS B 2 137 ? 28.976 -8.070 -34.052 1.00 38.39 ? 137 CYS B N 1 ATOM 3623 C CA . CYS B 2 137 ? 27.996 -7.953 -35.149 1.00 39.02 ? 137 CYS B CA 1 ATOM 3624 C C . CYS B 2 137 ? 28.211 -8.947 -36.270 1.00 37.86 ? 137 CYS B C 1 ATOM 3625 O O . CYS B 2 137 ? 29.330 -9.330 -36.556 1.00 38.19 ? 137 CYS B O 1 ATOM 3626 C CB . CYS B 2 137 ? 28.030 -6.549 -35.763 1.00 40.63 ? 137 CYS B CB 1 ATOM 3627 S SG . CYS B 2 137 ? 27.671 -5.217 -34.623 1.00 46.22 ? 137 CYS B SG 1 ATOM 3628 N N . PHE B 2 138 ? 27.117 -9.324 -36.921 1.00 37.42 ? 138 PHE B N 1 ATOM 3629 C CA . PHE B 2 138 ? 27.135 -10.184 -38.097 1.00 37.22 ? 138 PHE B CA 1 ATOM 3630 C C . PHE B 2 138 ? 26.543 -9.425 -39.280 1.00 37.93 ? 138 PHE B C 1 ATOM 3631 O O . PHE B 2 138 ? 25.497 -8.806 -39.161 1.00 37.67 ? 138 PHE B O 1 ATOM 3632 C CB . PHE B 2 138 ? 26.284 -11.437 -37.868 1.00 36.17 ? 138 PHE B CB 1 ATOM 3633 C CG . PHE B 2 138 ? 26.685 -12.227 -36.667 1.00 34.50 ? 138 PHE B CG 1 ATOM 3634 C CD1 . PHE B 2 138 ? 27.678 -13.191 -36.769 1.00 34.38 ? 138 PHE B CD1 1 ATOM 3635 C CD2 . PHE B 2 138 ? 26.073 -12.012 -35.429 1.00 34.77 ? 138 PHE B CD2 1 ATOM 3636 C CE1 . PHE B 2 138 ? 28.057 -13.930 -35.669 1.00 32.18 ? 138 PHE B CE1 1 ATOM 3637 C CE2 . PHE B 2 138 ? 26.456 -12.760 -34.314 1.00 30.66 ? 138 PHE B CE2 1 ATOM 3638 C CZ . PHE B 2 138 ? 27.441 -13.719 -34.451 1.00 31.03 ? 138 PHE B CZ 1 ATOM 3639 N N . GLU B 2 139 ? 27.214 -9.485 -40.423 1.00 39.69 ? 139 GLU B N 1 ATOM 3640 C CA . GLU B 2 139 ? 26.702 -8.837 -41.630 1.00 40.82 ? 139 GLU B CA 1 ATOM 3641 C C . GLU B 2 139 ? 26.120 -9.902 -42.556 1.00 40.98 ? 139 GLU B C 1 ATOM 3642 O O . GLU B 2 139 ? 26.820 -10.834 -42.929 1.00 41.06 ? 139 GLU B O 1 ATOM 3643 C CB . GLU B 2 139 ? 27.827 -8.057 -42.295 1.00 41.75 ? 139 GLU B CB 1 ATOM 3644 C CG . GLU B 2 139 ? 27.383 -7.136 -43.445 1.00 45.09 ? 139 GLU B CG 1 ATOM 3645 C CD . GLU B 2 139 ? 28.561 -6.632 -44.247 1.00 49.52 ? 139 GLU B CD 1 ATOM 3646 O OE1 . GLU B 2 139 ? 29.444 -5.957 -43.676 1.00 51.59 ? 139 GLU B OE1 1 ATOM 3647 O OE2 . GLU B 2 139 ? 28.614 -6.921 -45.460 1.00 53.56 ? 139 GLU B OE2 1 ATOM 3648 N N . PHE B 2 140 ? 24.844 -9.763 -42.922 1.00 41.82 ? 140 PHE B N 1 ATOM 3649 C CA . PHE B 2 140 ? 24.127 -10.776 -43.708 1.00 42.08 ? 140 PHE B CA 1 ATOM 3650 C C . PHE B 2 140 ? 24.511 -10.782 -45.188 1.00 42.78 ? 140 PHE B C 1 ATOM 3651 O O . PHE B 2 140 ? 24.736 -9.733 -45.770 1.00 42.39 ? 140 PHE B O 1 ATOM 3652 C CB . PHE B 2 140 ? 22.621 -10.553 -43.603 1.00 42.51 ? 140 PHE B CB 1 ATOM 3653 C CG . PHE B 2 140 ? 22.031 -11.005 -42.303 1.00 42.12 ? 140 PHE B CG 1 ATOM 3654 C CD1 . PHE B 2 140 ? 21.459 -12.262 -42.186 1.00 41.06 ? 140 PHE B CD1 1 ATOM 3655 C CD2 . PHE B 2 140 ? 22.056 -10.176 -41.189 1.00 44.23 ? 140 PHE B CD2 1 ATOM 3656 C CE1 . PHE B 2 140 ? 20.922 -12.692 -40.981 1.00 42.58 ? 140 PHE B CE1 1 ATOM 3657 C CE2 . PHE B 2 140 ? 21.512 -10.599 -39.967 1.00 43.97 ? 140 PHE B CE2 1 ATOM 3658 C CZ . PHE B 2 140 ? 20.945 -11.859 -39.865 1.00 43.37 ? 140 PHE B CZ 1 ATOM 3659 N N . TYR B 2 141 ? 24.576 -11.974 -45.781 1.00 43.83 ? 141 TYR B N 1 ATOM 3660 C CA . TYR B 2 141 ? 24.797 -12.116 -47.237 1.00 45.14 ? 141 TYR B CA 1 ATOM 3661 C C . TYR B 2 141 ? 23.479 -12.147 -48.010 1.00 45.86 ? 141 TYR B C 1 ATOM 3662 O O . TYR B 2 141 ? 23.469 -12.153 -49.237 1.00 45.81 ? 141 TYR B O 1 ATOM 3663 C CB . TYR B 2 141 ? 25.601 -13.372 -47.552 1.00 44.77 ? 141 TYR B CB 1 ATOM 3664 C CG . TYR B 2 141 ? 27.073 -13.253 -47.270 1.00 45.49 ? 141 TYR B CG 1 ATOM 3665 C CD1 . TYR B 2 141 ? 27.857 -12.323 -47.947 1.00 46.02 ? 141 TYR B CD1 1 ATOM 3666 C CD2 . TYR B 2 141 ? 27.688 -14.085 -46.341 1.00 45.16 ? 141 TYR B CD2 1 ATOM 3667 C CE1 . TYR B 2 141 ? 29.205 -12.214 -47.701 1.00 47.21 ? 141 TYR B CE1 1 ATOM 3668 C CE2 . TYR B 2 141 ? 29.042 -13.987 -46.074 1.00 45.82 ? 141 TYR B CE2 1 ATOM 3669 C CZ . TYR B 2 141 ? 29.794 -13.050 -46.751 1.00 47.38 ? 141 TYR B CZ 1 ATOM 3670 O OH . TYR B 2 141 ? 31.129 -12.949 -46.505 1.00 45.83 ? 141 TYR B OH 1 ATOM 3671 N N . HIS B 2 142 ? 22.372 -12.183 -47.281 1.00 47.16 ? 142 HIS B N 1 ATOM 3672 C CA . HIS B 2 142 ? 21.035 -12.122 -47.860 1.00 48.56 ? 142 HIS B CA 1 ATOM 3673 C C . HIS B 2 142 ? 20.238 -11.043 -47.150 1.00 49.78 ? 142 HIS B C 1 ATOM 3674 O O . HIS B 2 142 ? 20.458 -10.800 -45.972 1.00 49.69 ? 142 HIS B O 1 ATOM 3675 C CB . HIS B 2 142 ? 20.337 -13.465 -47.688 1.00 48.73 ? 142 HIS B CB 1 ATOM 3676 C CG . HIS B 2 142 ? 20.104 -13.848 -46.259 1.00 48.19 ? 142 HIS B CG 1 ATOM 3677 N ND1 . HIS B 2 142 ? 18.998 -13.437 -45.549 1.00 47.03 ? 142 HIS B ND1 1 ATOM 3678 C CD2 . HIS B 2 142 ? 20.844 -14.591 -45.404 1.00 47.60 ? 142 HIS B CD2 1 ATOM 3679 C CE1 . HIS B 2 142 ? 19.056 -13.925 -44.327 1.00 46.10 ? 142 HIS B CE1 1 ATOM 3680 N NE2 . HIS B 2 142 ? 20.164 -14.634 -44.214 1.00 45.81 ? 142 HIS B NE2 1 ATOM 3681 N N . LYS B 2 143 ? 19.315 -10.385 -47.850 1.00 51.30 ? 143 LYS B N 1 ATOM 3682 C CA . LYS B 2 143 ? 18.472 -9.380 -47.189 1.00 52.35 ? 143 LYS B CA 1 ATOM 3683 C C . LYS B 2 143 ? 17.685 -10.014 -46.055 1.00 52.38 ? 143 LYS B C 1 ATOM 3684 O O . LYS B 2 143 ? 17.074 -11.066 -46.229 1.00 52.57 ? 143 LYS B O 1 ATOM 3685 C CB . LYS B 2 143 ? 17.544 -8.673 -48.170 1.00 53.58 ? 143 LYS B CB 1 ATOM 3686 C CG . LYS B 2 143 ? 18.268 -7.638 -48.996 1.00 54.60 ? 143 LYS B CG 1 ATOM 3687 C CD . LYS B 2 143 ? 17.401 -6.432 -49.235 1.00 57.85 ? 143 LYS B CD 1 ATOM 3688 C CE . LYS B 2 143 ? 18.050 -5.520 -50.279 1.00 58.88 ? 143 LYS B CE 1 ATOM 3689 N NZ . LYS B 2 143 ? 19.274 -4.850 -49.736 1.00 59.07 ? 143 LYS B NZ 1 ATOM 3690 N N . CYS B 2 144 ? 17.727 -9.380 -44.885 1.00 52.78 ? 144 CYS B N 1 ATOM 3691 C CA . CYS B 2 144 ? 17.090 -9.932 -43.692 1.00 52.46 ? 144 CYS B CA 1 ATOM 3692 C C . CYS B 2 144 ? 16.130 -8.906 -43.092 1.00 53.59 ? 144 CYS B C 1 ATOM 3693 O O . CYS B 2 144 ? 16.531 -7.999 -42.345 1.00 53.74 ? 144 CYS B O 1 ATOM 3694 C CB . CYS B 2 144 ? 18.149 -10.405 -42.674 1.00 51.98 ? 144 CYS B CB 1 ATOM 3695 S SG . CYS B 2 144 ? 17.484 -11.185 -41.146 1.00 51.70 ? 144 CYS B SG 1 ATOM 3696 N N . ASP B 2 145 ? 14.857 -9.054 -43.445 1.00 54.21 ? 145 ASP B N 1 ATOM 3697 C CA . ASP B 2 145 ? 13.822 -8.116 -43.031 1.00 55.44 ? 145 ASP B CA 1 ATOM 3698 C C . ASP B 2 145 ? 13.421 -8.353 -41.579 1.00 55.59 ? 145 ASP B C 1 ATOM 3699 O O . ASP B 2 145 ? 13.956 -9.248 -40.921 1.00 55.10 ? 145 ASP B O 1 ATOM 3700 C CB . ASP B 2 145 ? 12.608 -8.185 -43.974 1.00 56.07 ? 145 ASP B CB 1 ATOM 3701 C CG . ASP B 2 145 ? 11.852 -9.509 -43.886 1.00 55.98 ? 145 ASP B CG 1 ATOM 3702 O OD1 . ASP B 2 145 ? 11.954 -10.233 -42.876 1.00 54.72 ? 145 ASP B OD1 1 ATOM 3703 O OD2 . ASP B 2 145 ? 11.134 -9.829 -44.846 1.00 55.71 ? 145 ASP B OD2 1 ATOM 3704 N N . ASP B 2 146 ? 12.465 -7.572 -41.091 1.00 56.70 ? 146 ASP B N 1 ATOM 3705 C CA . ASP B 2 146 ? 12.076 -7.646 -39.690 1.00 57.00 ? 146 ASP B CA 1 ATOM 3706 C C . ASP B 2 146 ? 11.687 -9.029 -39.214 1.00 56.74 ? 146 ASP B C 1 ATOM 3707 O O . ASP B 2 146 ? 12.098 -9.441 -38.132 1.00 55.88 ? 146 ASP B O 1 ATOM 3708 C CB . ASP B 2 146 ? 10.988 -6.627 -39.366 1.00 58.71 ? 146 ASP B CB 1 ATOM 3709 C CG . ASP B 2 146 ? 11.550 -5.244 -39.159 1.00 58.88 ? 146 ASP B CG 1 ATOM 3710 O OD1 . ASP B 2 146 ? 12.783 -5.092 -39.224 1.00 57.51 ? 146 ASP B OD1 1 ATOM 3711 O OD2 . ASP B 2 146 ? 10.767 -4.306 -38.932 1.00 61.17 ? 146 ASP B OD2 1 ATOM 3712 N N . GLU B 2 147 ? 10.923 -9.753 -40.023 1.00 57.22 ? 147 GLU B N 1 ATOM 3713 C CA . GLU B 2 147 ? 10.504 -11.108 -39.657 1.00 57.93 ? 147 GLU B CA 1 ATOM 3714 C C . GLU B 2 147 ? 11.673 -12.096 -39.619 1.00 55.88 ? 147 GLU B C 1 ATOM 3715 O O . GLU B 2 147 ? 11.700 -13.005 -38.785 1.00 55.44 ? 147 GLU B O 1 ATOM 3716 C CB . GLU B 2 147 ? 9.408 -11.609 -40.603 1.00 59.50 ? 147 GLU B CB 1 ATOM 3717 C CG . GLU B 2 147 ? 8.083 -10.831 -40.509 1.00 64.21 ? 147 GLU B CG 1 ATOM 3718 C CD . GLU B 2 147 ? 7.421 -10.865 -39.112 1.00 69.22 ? 147 GLU B CD 1 ATOM 3719 O OE1 . GLU B 2 147 ? 7.784 -11.707 -38.250 1.00 70.92 ? 147 GLU B OE1 1 ATOM 3720 O OE2 . GLU B 2 147 ? 6.519 -10.031 -38.871 1.00 72.66 ? 147 GLU B OE2 1 ATOM 3721 N N . CYS B 2 148 ? 12.630 -11.908 -40.528 1.00 54.68 ? 148 CYS B N 1 ATOM 3722 C CA . CYS B 2 148 ? 13.865 -12.691 -40.548 1.00 53.09 ? 148 CYS B CA 1 ATOM 3723 C C . CYS B 2 148 ? 14.656 -12.412 -39.260 1.00 51.96 ? 148 CYS B C 1 ATOM 3724 O O . CYS B 2 148 ? 15.137 -13.347 -38.616 1.00 51.13 ? 148 CYS B O 1 ATOM 3725 C CB . CYS B 2 148 ? 14.695 -12.367 -41.797 1.00 52.68 ? 148 CYS B CB 1 ATOM 3726 S SG . CYS B 2 148 ? 16.451 -12.887 -41.773 1.00 54.44 ? 148 CYS B SG 1 ATOM 3727 N N . MET B 2 149 ? 14.761 -11.134 -38.887 1.00 51.30 ? 149 MET B N 1 ATOM 3728 C CA . MET B 2 149 ? 15.453 -10.735 -37.655 1.00 50.06 ? 149 MET B CA 1 ATOM 3729 C C . MET B 2 149 ? 14.833 -11.427 -36.453 1.00 49.77 ? 149 MET B C 1 ATOM 3730 O O . MET B 2 149 ? 15.540 -11.939 -35.585 1.00 48.76 ? 149 MET B O 1 ATOM 3731 C CB . MET B 2 149 ? 15.415 -9.217 -37.450 1.00 50.95 ? 149 MET B CB 1 ATOM 3732 C CG . MET B 2 149 ? 16.251 -8.393 -38.434 1.00 51.07 ? 149 MET B CG 1 ATOM 3733 S SD . MET B 2 149 ? 18.019 -8.752 -38.424 1.00 52.55 ? 149 MET B SD 1 ATOM 3734 C CE . MET B 2 149 ? 18.644 -7.454 -39.481 1.00 51.63 ? 149 MET B CE 1 ATOM 3735 N N . ASN B 2 150 ? 13.506 -11.460 -36.410 1.00 49.78 ? 150 ASN B N 1 ATOM 3736 C CA . ASN B 2 150 ? 12.825 -12.084 -35.287 1.00 49.78 ? 150 ASN B CA 1 ATOM 3737 C C . ASN B 2 150 ? 13.087 -13.582 -35.176 1.00 48.56 ? 150 ASN B C 1 ATOM 3738 O O . ASN B 2 150 ? 13.150 -14.118 -34.073 1.00 48.02 ? 150 ASN B O 1 ATOM 3739 C CB . ASN B 2 150 ? 11.326 -11.774 -35.305 1.00 51.59 ? 150 ASN B CB 1 ATOM 3740 C CG . ASN B 2 150 ? 11.031 -10.284 -35.148 1.00 52.80 ? 150 ASN B CG 1 ATOM 3741 O OD1 . ASN B 2 150 ? 11.859 -9.515 -34.647 1.00 52.04 ? 150 ASN B OD1 1 ATOM 3742 N ND2 . ASN B 2 150 ? 9.852 -9.872 -35.595 1.00 54.79 ? 150 ASN B ND2 1 ATOM 3743 N N . SER B 2 151 ? 13.248 -14.254 -36.311 1.00 47.65 ? 151 SER B N 1 ATOM 3744 C CA . SER B 2 151 ? 13.623 -15.673 -36.301 1.00 46.87 ? 151 SER B CA 1 ATOM 3745 C C . SER B 2 151 ? 15.015 -15.865 -35.704 1.00 45.16 ? 151 SER B C 1 ATOM 3746 O O . SER B 2 151 ? 15.236 -16.818 -34.943 1.00 45.28 ? 151 SER B O 1 ATOM 3747 C CB . SER B 2 151 ? 13.531 -16.305 -37.706 1.00 47.13 ? 151 SER B CB 1 ATOM 3748 O OG . SER B 2 151 ? 14.514 -15.785 -38.586 1.00 46.12 ? 151 SER B OG 1 ATOM 3749 N N . VAL B 2 152 ? 15.944 -14.963 -36.026 1.00 44.00 ? 152 VAL B N 1 ATOM 3750 C CA . VAL B 2 152 ? 17.292 -15.018 -35.408 1.00 43.28 ? 152 VAL B CA 1 ATOM 3751 C C . VAL B 2 152 ? 17.156 -14.857 -33.894 1.00 43.84 ? 152 VAL B C 1 ATOM 3752 O O . VAL B 2 152 ? 17.635 -15.700 -33.125 1.00 43.66 ? 152 VAL B O 1 ATOM 3753 C CB . VAL B 2 152 ? 18.262 -13.947 -35.952 1.00 42.42 ? 152 VAL B CB 1 ATOM 3754 C CG1 . VAL B 2 152 ? 19.657 -14.070 -35.280 1.00 41.36 ? 152 VAL B CG1 1 ATOM 3755 C CG2 . VAL B 2 152 ? 18.404 -14.063 -37.472 1.00 42.01 ? 152 VAL B CG2 1 ATOM 3756 N N . LYS B 2 153 ? 16.462 -13.795 -33.483 1.00 44.84 ? 153 LYS B N 1 ATOM 3757 C CA . LYS B 2 153 ? 16.302 -13.452 -32.052 1.00 46.57 ? 153 LYS B CA 1 ATOM 3758 C C . LYS B 2 153 ? 15.574 -14.496 -31.200 1.00 47.85 ? 153 LYS B C 1 ATOM 3759 O O . LYS B 2 153 ? 15.756 -14.529 -29.988 1.00 47.19 ? 153 LYS B O 1 ATOM 3760 C CB . LYS B 2 153 ? 15.598 -12.106 -31.887 1.00 46.93 ? 153 LYS B CB 1 ATOM 3761 C CG . LYS B 2 153 ? 16.298 -10.915 -32.515 1.00 47.36 ? 153 LYS B CG 1 ATOM 3762 C CD . LYS B 2 153 ? 15.645 -9.654 -32.015 1.00 48.85 ? 153 LYS B CD 1 ATOM 3763 C CE . LYS B 2 153 ? 15.424 -8.634 -33.100 1.00 50.76 ? 153 LYS B CE 1 ATOM 3764 N NZ . LYS B 2 153 ? 14.777 -7.443 -32.475 1.00 51.20 ? 153 LYS B NZ 1 ATOM 3765 N N . ASN B 2 154 ? 14.735 -15.333 -31.815 1.00 50.20 ? 154 ASN B N 1 ATOM 3766 C CA . ASN B 2 154 ? 14.098 -16.412 -31.043 1.00 53.07 ? 154 ASN B CA 1 ATOM 3767 C C . ASN B 2 154 ? 14.619 -17.819 -31.337 1.00 52.82 ? 154 ASN B C 1 ATOM 3768 O O . ASN B 2 154 ? 14.068 -18.803 -30.840 1.00 53.87 ? 154 ASN B O 1 ATOM 3769 C CB . ASN B 2 154 ? 12.553 -16.318 -31.006 1.00 55.26 ? 154 ASN B CB 1 ATOM 3770 C CG . ASN B 2 154 ? 11.894 -16.648 -32.327 1.00 61.12 ? 154 ASN B CG 1 ATOM 3771 O OD1 . ASN B 2 154 ? 12.564 -16.943 -33.325 1.00 61.80 ? 154 ASN B OD1 1 ATOM 3772 N ND2 . ASN B 2 154 ? 10.541 -16.597 -32.336 1.00 70.10 ? 154 ASN B ND2 1 ATOM 3773 N N . GLY B 2 155 ? 15.703 -17.901 -32.110 1.00 51.58 ? 155 GLY B N 1 ATOM 3774 C CA . GLY B 2 155 ? 16.429 -19.158 -32.289 1.00 51.19 ? 155 GLY B CA 1 ATOM 3775 C C . GLY B 2 155 ? 15.832 -20.085 -33.336 1.00 51.98 ? 155 GLY B C 1 ATOM 3776 O O . GLY B 2 155 ? 16.037 -21.296 -33.290 1.00 52.26 ? 155 GLY B O 1 ATOM 3777 N N . THR B 2 156 ? 15.096 -19.519 -34.284 1.00 52.00 ? 156 THR B N 1 ATOM 3778 C CA . THR B 2 156 ? 14.445 -20.320 -35.306 1.00 53.27 ? 156 THR B CA 1 ATOM 3779 C C . THR B 2 156 ? 14.811 -19.806 -36.692 1.00 52.60 ? 156 THR B C 1 ATOM 3780 O O . THR B 2 156 ? 14.018 -19.902 -37.629 1.00 53.53 ? 156 THR B O 1 ATOM 3781 C CB . THR B 2 156 ? 12.898 -20.349 -35.134 1.00 54.48 ? 156 THR B CB 1 ATOM 3782 O OG1 . THR B 2 156 ? 12.359 -19.051 -35.409 1.00 54.54 ? 156 THR B OG1 1 ATOM 3783 C CG2 . THR B 2 156 ? 12.499 -20.795 -33.723 1.00 55.72 ? 156 THR B CG2 1 ATOM 3784 N N . TYR B 2 157 ? 16.014 -19.246 -36.816 1.00 51.38 ? 157 TYR B N 1 ATOM 3785 C CA . TYR B 2 157 ? 16.542 -18.862 -38.117 1.00 50.68 ? 157 TYR B CA 1 ATOM 3786 C C . TYR B 2 157 ? 16.708 -20.125 -38.974 1.00 51.70 ? 157 TYR B C 1 ATOM 3787 O O . TYR B 2 157 ? 17.190 -21.167 -38.503 1.00 51.98 ? 157 TYR B O 1 ATOM 3788 C CB . TYR B 2 157 ? 17.873 -18.103 -37.982 1.00 49.18 ? 157 TYR B CB 1 ATOM 3789 C CG . TYR B 2 157 ? 18.570 -17.783 -39.299 1.00 47.46 ? 157 TYR B CG 1 ATOM 3790 C CD1 . TYR B 2 157 ? 18.236 -16.644 -40.031 1.00 44.85 ? 157 TYR B CD1 1 ATOM 3791 C CD2 . TYR B 2 157 ? 19.570 -18.620 -39.807 1.00 46.04 ? 157 TYR B CD2 1 ATOM 3792 C CE1 . TYR B 2 157 ? 18.876 -16.337 -41.219 1.00 43.27 ? 157 TYR B CE1 1 ATOM 3793 C CE2 . TYR B 2 157 ? 20.218 -18.322 -41.019 1.00 45.30 ? 157 TYR B CE2 1 ATOM 3794 C CZ . TYR B 2 157 ? 19.862 -17.180 -41.716 1.00 43.41 ? 157 TYR B CZ 1 ATOM 3795 O OH . TYR B 2 157 ? 20.484 -16.871 -42.905 1.00 40.35 ? 157 TYR B OH 1 ATOM 3796 N N . ASP B 2 158 ? 16.298 -20.009 -40.224 1.00 52.22 ? 158 ASP B N 1 ATOM 3797 C CA . ASP B 2 158 ? 16.220 -21.135 -41.139 1.00 53.84 ? 158 ASP B CA 1 ATOM 3798 C C . ASP B 2 158 ? 17.407 -21.033 -42.090 1.00 52.97 ? 158 ASP B C 1 ATOM 3799 O O . ASP B 2 158 ? 17.362 -20.277 -43.057 1.00 52.41 ? 158 ASP B O 1 ATOM 3800 C CB . ASP B 2 158 ? 14.878 -21.055 -41.878 1.00 54.85 ? 158 ASP B CB 1 ATOM 3801 C CG . ASP B 2 158 ? 14.519 -22.337 -42.629 1.00 56.75 ? 158 ASP B CG 1 ATOM 3802 O OD1 . ASP B 2 158 ? 15.417 -23.101 -43.041 1.00 56.53 ? 158 ASP B OD1 1 ATOM 3803 O OD2 . ASP B 2 158 ? 13.307 -22.559 -42.833 1.00 58.47 ? 158 ASP B OD2 1 ATOM 3804 N N . TYR B 2 159 ? 18.487 -21.752 -41.773 1.00 53.12 ? 159 TYR B N 1 ATOM 3805 C CA . TYR B 2 159 ? 19.706 -21.706 -42.598 1.00 53.21 ? 159 TYR B CA 1 ATOM 3806 C C . TYR B 2 159 ? 19.454 -22.216 -44.036 1.00 53.96 ? 159 TYR B C 1 ATOM 3807 O O . TYR B 2 159 ? 19.811 -21.521 -45.005 1.00 53.51 ? 159 TYR B O 1 ATOM 3808 C CB . TYR B 2 159 ? 20.889 -22.440 -41.934 1.00 53.06 ? 159 TYR B CB 1 ATOM 3809 C CG . TYR B 2 159 ? 22.121 -22.547 -42.818 1.00 52.60 ? 159 TYR B CG 1 ATOM 3810 C CD1 . TYR B 2 159 ? 23.040 -21.509 -42.883 1.00 51.98 ? 159 TYR B CD1 1 ATOM 3811 C CD2 . TYR B 2 159 ? 22.360 -23.687 -43.590 1.00 54.38 ? 159 TYR B CD2 1 ATOM 3812 C CE1 . TYR B 2 159 ? 24.168 -21.593 -43.693 1.00 53.39 ? 159 TYR B CE1 1 ATOM 3813 C CE2 . TYR B 2 159 ? 23.489 -23.784 -44.415 1.00 54.52 ? 159 TYR B CE2 1 ATOM 3814 C CZ . TYR B 2 159 ? 24.385 -22.731 -44.461 1.00 54.05 ? 159 TYR B CZ 1 ATOM 3815 O OH . TYR B 2 159 ? 25.504 -22.802 -45.254 1.00 53.39 ? 159 TYR B OH 1 ATOM 3816 N N . PRO B 2 160 ? 18.838 -23.418 -44.180 1.00 55.29 ? 160 PRO B N 1 ATOM 3817 C CA . PRO B 2 160 ? 18.543 -23.950 -45.518 1.00 56.03 ? 160 PRO B CA 1 ATOM 3818 C C . PRO B 2 160 ? 17.755 -22.971 -46.385 1.00 55.67 ? 160 PRO B C 1 ATOM 3819 O O . PRO B 2 160 ? 18.051 -22.847 -47.560 1.00 55.76 ? 160 PRO B O 1 ATOM 3820 C CB . PRO B 2 160 ? 17.710 -25.194 -45.213 1.00 57.30 ? 160 PRO B CB 1 ATOM 3821 C CG . PRO B 2 160 ? 18.246 -25.684 -43.927 1.00 57.09 ? 160 PRO B CG 1 ATOM 3822 C CD . PRO B 2 160 ? 18.507 -24.416 -43.134 1.00 56.66 ? 160 PRO B CD 1 ATOM 3823 N N . LYS B 2 161 ? 16.784 -22.279 -45.783 1.00 56.03 ? 161 LYS B N 1 ATOM 3824 C CA . LYS B 2 161 ? 15.945 -21.255 -46.431 1.00 56.02 ? 161 LYS B CA 1 ATOM 3825 C C . LYS B 2 161 ? 16.736 -20.162 -47.172 1.00 55.00 ? 161 LYS B C 1 ATOM 3826 O O . LYS B 2 161 ? 16.338 -19.718 -48.252 1.00 55.13 ? 161 LYS B O 1 ATOM 3827 C CB . LYS B 2 161 ? 15.039 -20.619 -45.365 1.00 56.24 ? 161 LYS B CB 1 ATOM 3828 C CG . LYS B 2 161 ? 13.941 -19.648 -45.843 1.00 57.64 ? 161 LYS B CG 1 ATOM 3829 C CD . LYS B 2 161 ? 12.960 -19.392 -44.676 1.00 60.24 ? 161 LYS B CD 1 ATOM 3830 C CE . LYS B 2 161 ? 11.685 -18.641 -45.066 1.00 62.21 ? 161 LYS B CE 1 ATOM 3831 N NZ . LYS B 2 161 ? 11.940 -17.435 -45.904 1.00 62.94 ? 161 LYS B NZ 1 ATOM 3832 N N . TYR B 2 162 ? 17.859 -19.740 -46.594 1.00 54.29 ? 162 TYR B N 1 ATOM 3833 C CA . TYR B 2 162 ? 18.654 -18.640 -47.156 1.00 53.50 ? 162 TYR B CA 1 ATOM 3834 C C . TYR B 2 162 ? 19.990 -19.092 -47.753 1.00 53.00 ? 162 TYR B C 1 ATOM 3835 O O . TYR B 2 162 ? 20.759 -18.276 -48.259 1.00 52.54 ? 162 TYR B O 1 ATOM 3836 C CB . TYR B 2 162 ? 18.879 -17.567 -46.082 1.00 52.99 ? 162 TYR B CB 1 ATOM 3837 C CG . TYR B 2 162 ? 17.603 -16.898 -45.603 1.00 53.90 ? 162 TYR B CG 1 ATOM 3838 C CD1 . TYR B 2 162 ? 17.018 -15.853 -46.330 1.00 53.77 ? 162 TYR B CD1 1 ATOM 3839 C CD2 . TYR B 2 162 ? 16.980 -17.311 -44.429 1.00 54.77 ? 162 TYR B CD2 1 ATOM 3840 C CE1 . TYR B 2 162 ? 15.849 -15.234 -45.891 1.00 55.18 ? 162 TYR B CE1 1 ATOM 3841 C CE2 . TYR B 2 162 ? 15.807 -16.698 -43.980 1.00 56.48 ? 162 TYR B CE2 1 ATOM 3842 C CZ . TYR B 2 162 ? 15.249 -15.661 -44.715 1.00 55.75 ? 162 TYR B CZ 1 ATOM 3843 O OH . TYR B 2 162 ? 14.094 -15.066 -44.266 1.00 57.65 ? 162 TYR B OH 1 ATOM 3844 N N . GLU B 2 163 ? 20.248 -20.395 -47.706 1.00 53.74 ? 163 GLU B N 1 ATOM 3845 C CA . GLU B 2 163 ? 21.545 -20.958 -48.096 1.00 54.08 ? 163 GLU B CA 1 ATOM 3846 C C . GLU B 2 163 ? 21.952 -20.580 -49.506 1.00 53.80 ? 163 GLU B C 1 ATOM 3847 O O . GLU B 2 163 ? 23.081 -20.146 -49.738 1.00 53.33 ? 163 GLU B O 1 ATOM 3848 C CB . GLU B 2 163 ? 21.541 -22.484 -47.947 1.00 54.99 ? 163 GLU B CB 1 ATOM 3849 C CG . GLU B 2 163 ? 22.830 -23.157 -48.437 1.00 56.81 ? 163 GLU B CG 1 ATOM 3850 C CD . GLU B 2 163 ? 23.028 -24.559 -47.883 1.00 59.28 ? 163 GLU B CD 1 ATOM 3851 O OE1 . GLU B 2 163 ? 22.077 -25.114 -47.285 1.00 60.11 ? 163 GLU B OE1 1 ATOM 3852 O OE2 . GLU B 2 163 ? 24.144 -25.108 -48.047 1.00 59.83 ? 163 GLU B OE2 1 ATOM 3853 N N . GLU B 2 164 ? 21.009 -20.736 -50.431 1.00 54.95 ? 164 GLU B N 1 ATOM 3854 C CA . GLU B 2 164 ? 21.261 -20.567 -51.863 1.00 55.36 ? 164 GLU B CA 1 ATOM 3855 C C . GLU B 2 164 ? 21.556 -19.106 -52.226 1.00 54.26 ? 164 GLU B C 1 ATOM 3856 O O . GLU B 2 164 ? 22.564 -18.810 -52.881 1.00 54.13 ? 164 GLU B O 1 ATOM 3857 C CB . GLU B 2 164 ? 20.087 -21.147 -52.679 1.00 56.55 ? 164 GLU B CB 1 ATOM 3858 C CG . GLU B 2 164 ? 19.806 -22.646 -52.375 1.00 59.47 ? 164 GLU B CG 1 ATOM 3859 C CD . GLU B 2 164 ? 18.549 -23.201 -53.048 1.00 62.63 ? 164 GLU B CD 1 ATOM 3860 O OE1 . GLU B 2 164 ? 18.573 -23.446 -54.278 1.00 63.86 ? 164 GLU B OE1 1 ATOM 3861 O OE2 . GLU B 2 164 ? 17.541 -23.419 -52.337 1.00 63.63 ? 164 GLU B OE2 1 ATOM 3862 N N . GLU B 2 165 ? 20.691 -18.203 -51.769 1.00 53.60 ? 165 GLU B N 1 ATOM 3863 C CA . GLU B 2 165 ? 20.865 -16.767 -51.984 1.00 52.96 ? 165 GLU B CA 1 ATOM 3864 C C . GLU B 2 165 ? 22.201 -16.252 -51.425 1.00 52.89 ? 165 GLU B C 1 ATOM 3865 O O . GLU B 2 165 ? 22.903 -15.530 -52.118 1.00 53.11 ? 165 GLU B O 1 ATOM 3866 C CB . GLU B 2 165 ? 19.694 -15.988 -51.360 1.00 52.86 ? 165 GLU B CB 1 ATOM 3867 C CG . GLU B 2 165 ? 19.810 -14.470 -51.528 1.00 53.10 ? 165 GLU B CG 1 ATOM 3868 C CD . GLU B 2 165 ? 18.747 -13.656 -50.773 1.00 55.53 ? 165 GLU B CD 1 ATOM 3869 O OE1 . GLU B 2 165 ? 17.811 -14.235 -50.147 1.00 54.67 ? 165 GLU B OE1 1 ATOM 3870 O OE2 . GLU B 2 165 ? 18.864 -12.405 -50.812 1.00 55.93 ? 165 GLU B OE2 1 ATOM 3871 N N . SER B 2 166 ? 22.553 -16.633 -50.188 1.00 52.51 ? 166 SER B N 1 ATOM 3872 C CA . SER B 2 166 ? 23.761 -16.102 -49.522 1.00 52.25 ? 166 SER B CA 1 ATOM 3873 C C . SER B 2 166 ? 25.044 -16.502 -50.256 1.00 52.77 ? 166 SER B C 1 ATOM 3874 O O . SER B 2 166 ? 25.910 -15.659 -50.536 1.00 51.90 ? 166 SER B O 1 ATOM 3875 C CB . SER B 2 166 ? 23.833 -16.560 -48.054 1.00 52.25 ? 166 SER B CB 1 ATOM 3876 O OG . SER B 2 166 ? 22.680 -16.171 -47.315 1.00 51.30 ? 166 SER B OG 1 ATOM 3877 N N . LYS B 2 167 ? 25.130 -17.796 -50.560 1.00 53.67 ? 167 LYS B N 1 ATOM 3878 C CA . LYS B 2 167 ? 26.239 -18.416 -51.290 1.00 54.98 ? 167 LYS B CA 1 ATOM 3879 C C . LYS B 2 167 ? 26.515 -17.730 -52.624 1.00 55.41 ? 167 LYS B C 1 ATOM 3880 O O . LYS B 2 167 ? 27.669 -17.485 -52.983 1.00 55.57 ? 167 LYS B O 1 ATOM 3881 C CB . LYS B 2 167 ? 25.924 -19.901 -51.511 1.00 55.80 ? 167 LYS B CB 1 ATOM 3882 C CG . LYS B 2 167 ? 26.956 -20.703 -52.320 1.00 57.51 ? 167 LYS B CG 1 ATOM 3883 C CD . LYS B 2 167 ? 26.403 -22.083 -52.690 1.00 59.44 ? 167 LYS B CD 1 ATOM 3884 C CE . LYS B 2 167 ? 26.227 -22.952 -51.442 1.00 60.52 ? 167 LYS B CE 1 ATOM 3885 N NZ . LYS B 2 167 ? 25.175 -24.001 -51.593 1.00 62.35 ? 167 LYS B NZ 1 ATOM 3886 N N . LEU B 2 168 ? 25.453 -17.423 -53.359 1.00 55.93 ? 168 LEU B N 1 ATOM 3887 C CA . LEU B 2 168 ? 25.603 -16.703 -54.614 1.00 56.65 ? 168 LEU B CA 1 ATOM 3888 C C . LEU B 2 168 ? 26.195 -15.305 -54.352 1.00 56.98 ? 168 LEU B C 1 ATOM 3889 O O . LEU B 2 168 ? 27.194 -14.907 -54.978 1.00 57.57 ? 168 LEU B O 1 ATOM 3890 C CB . LEU B 2 168 ? 24.260 -16.635 -55.359 1.00 56.79 ? 168 LEU B CB 1 ATOM 3891 C CG . LEU B 2 168 ? 23.635 -17.943 -55.893 1.00 57.44 ? 168 LEU B CG 1 ATOM 3892 C CD1 . LEU B 2 168 ? 22.113 -17.820 -56.091 1.00 57.24 ? 168 LEU B CD1 1 ATOM 3893 C CD2 . LEU B 2 168 ? 24.309 -18.384 -57.188 1.00 57.61 ? 168 LEU B CD2 1 ATOM 3894 N N . ASN B 2 169 ? 25.599 -14.589 -53.397 1.00 56.73 ? 169 ASN B N 1 ATOM 3895 C CA . ASN B 2 169 ? 26.017 -13.225 -53.043 1.00 57.21 ? 169 ASN B CA 1 ATOM 3896 C C . ASN B 2 169 ? 27.429 -13.162 -52.484 1.00 57.98 ? 169 ASN B C 1 ATOM 3897 O O . ASN B 2 169 ? 28.147 -12.182 -52.690 1.00 58.27 ? 169 ASN B O 1 ATOM 3898 C CB . ASN B 2 169 ? 25.067 -12.620 -52.011 1.00 56.60 ? 169 ASN B CB 1 ATOM 3899 C CG . ASN B 2 169 ? 23.652 -12.442 -52.534 1.00 56.71 ? 169 ASN B CG 1 ATOM 3900 O OD1 . ASN B 2 169 ? 22.686 -12.821 -51.871 1.00 54.49 ? 169 ASN B OD1 1 ATOM 3901 N ND2 . ASN B 2 169 ? 23.521 -11.852 -53.720 1.00 56.51 ? 169 ASN B ND2 1 ATOM 3902 N N . ARG B 2 170 ? 27.816 -14.214 -51.774 1.00 58.71 ? 170 ARG B N 1 ATOM 3903 C CA . ARG B 2 170 ? 29.106 -14.256 -51.124 1.00 60.48 ? 170 ARG B CA 1 ATOM 3904 C C . ARG B 2 170 ? 30.208 -14.376 -52.164 1.00 62.12 ? 170 ARG B C 1 ATOM 3905 O O . ARG B 2 170 ? 31.346 -13.993 -51.903 1.00 63.11 ? 170 ARG B O 1 ATOM 3906 C CB . ARG B 2 170 ? 29.164 -15.418 -50.122 1.00 59.86 ? 170 ARG B CB 1 ATOM 3907 C CG . ARG B 2 170 ? 30.417 -15.441 -49.260 1.00 59.96 ? 170 ARG B CG 1 ATOM 3908 C CD . ARG B 2 170 ? 30.366 -16.495 -48.177 1.00 56.99 ? 170 ARG B CD 1 ATOM 3909 N NE . ARG B 2 170 ? 30.239 -17.851 -48.702 1.00 57.34 ? 170 ARG B NE 1 ATOM 3910 C CZ . ARG B 2 170 ? 29.137 -18.599 -48.631 1.00 55.96 ? 170 ARG B CZ 1 ATOM 3911 N NH1 . ARG B 2 170 ? 28.029 -18.140 -48.056 1.00 54.87 ? 170 ARG B NH1 1 ATOM 3912 N NH2 . ARG B 2 170 ? 29.148 -19.821 -49.130 1.00 55.84 ? 170 ARG B NH2 1 ATOM 3913 N N . ASN B 2 171 ? 29.850 -14.874 -53.349 1.00 63.82 ? 171 ASN B N 1 ATOM 3914 C CA . ASN B 2 171 ? 30.831 -15.264 -54.374 1.00 65.88 ? 171 ASN B CA 1 ATOM 3915 C C . ASN B 2 171 ? 31.078 -14.301 -55.533 1.00 67.04 ? 171 ASN B C 1 ATOM 3916 O O . ASN B 2 171 ? 32.190 -14.255 -56.056 1.00 68.16 ? 171 ASN B O 1 ATOM 3917 C CB . ASN B 2 171 ? 30.483 -16.645 -54.941 1.00 66.05 ? 171 ASN B CB 1 ATOM 3918 C CG . ASN B 2 171 ? 30.642 -17.755 -53.917 1.00 66.85 ? 171 ASN B CG 1 ATOM 3919 O OD1 . ASN B 2 171 ? 31.366 -17.610 -52.929 1.00 67.26 ? 171 ASN B OD1 1 ATOM 3920 N ND2 . ASN B 2 171 ? 29.961 -18.877 -54.151 1.00 67.85 ? 171 ASN B ND2 1 ATOM 3921 N N . GLU B 2 172 ? 30.057 -13.554 -55.950 1.00 67.61 ? 172 GLU B N 1 ATOM 3922 C CA . GLU B 2 172 ? 30.136 -12.763 -57.197 1.00 68.83 ? 172 GLU B CA 1 ATOM 3923 C C . GLU B 2 172 ? 31.151 -11.613 -57.186 1.00 69.71 ? 172 GLU B C 1 ATOM 3924 O O . GLU B 2 172 ? 31.805 -11.345 -56.175 1.00 70.11 ? 172 GLU B O 1 ATOM 3925 C CB . GLU B 2 172 ? 28.758 -12.241 -57.596 1.00 68.65 ? 172 GLU B CB 1 ATOM 3926 C CG . GLU B 2 172 ? 28.059 -11.423 -56.516 1.00 69.88 ? 172 GLU B CG 1 ATOM 3927 C CD . GLU B 2 172 ? 26.645 -11.024 -56.909 1.00 72.34 ? 172 GLU B CD 1 ATOM 3928 O OE1 . GLU B 2 172 ? 26.106 -11.585 -57.893 1.00 72.68 ? 172 GLU B OE1 1 ATOM 3929 O OE2 . GLU B 2 172 ? 26.065 -10.152 -56.225 1.00 73.89 ? 172 GLU B OE2 1 HETATM 3930 C C1 . NAG C 3 . ? 5.776 -27.613 51.414 1.00 38.71 ? 330 NAG A C1 1 HETATM 3931 C C2 . NAG C 3 . ? 5.795 -28.904 52.248 1.00 43.28 ? 330 NAG A C2 1 HETATM 3932 C C3 . NAG C 3 . ? 5.308 -30.059 51.366 1.00 48.00 ? 330 NAG A C3 1 HETATM 3933 C C4 . NAG C 3 . ? 3.884 -29.684 50.954 1.00 50.98 ? 330 NAG A C4 1 HETATM 3934 C C5 . NAG C 3 . ? 3.948 -28.458 50.013 1.00 48.12 ? 330 NAG A C5 1 HETATM 3935 C C6 . NAG C 3 . ? 2.585 -28.014 49.463 1.00 47.27 ? 330 NAG A C6 1 HETATM 3936 C C7 . NAG C 3 . ? 7.297 -29.426 54.164 1.00 42.51 ? 330 NAG A C7 1 HETATM 3937 C C8 . NAG C 3 . ? 8.708 -29.716 54.578 1.00 41.60 ? 330 NAG A C8 1 HETATM 3938 N N2 . NAG C 3 . ? 7.086 -29.196 52.853 1.00 41.77 ? 330 NAG A N2 1 HETATM 3939 O O3 . NAG C 3 . ? 5.303 -31.267 52.088 1.00 49.19 ? 330 NAG A O3 1 HETATM 3940 O O4 . NAG C 3 . ? 3.024 -30.781 50.613 1.00 59.71 ? 330 NAG A O4 1 HETATM 3941 O O5 . NAG C 3 . ? 4.509 -27.386 50.768 1.00 41.82 ? 330 NAG A O5 1 HETATM 3942 O O6 . NAG C 3 . ? 1.625 -28.043 50.494 1.00 48.88 ? 330 NAG A O6 1 HETATM 3943 O O7 . NAG C 3 . ? 6.423 -29.417 55.039 1.00 45.51 ? 330 NAG A O7 1 HETATM 3944 C C1 . NAG D 3 . ? 3.333 -31.673 49.510 1.00 64.96 ? 331 NAG A C1 1 HETATM 3945 C C2 . NAG D 3 . ? 2.171 -31.591 48.485 1.00 66.71 ? 331 NAG A C2 1 HETATM 3946 C C3 . NAG D 3 . ? 2.572 -31.426 47.003 1.00 67.28 ? 331 NAG A C3 1 HETATM 3947 C C4 . NAG D 3 . ? 4.072 -31.410 46.702 1.00 67.21 ? 331 NAG A C4 1 HETATM 3948 C C5 . NAG D 3 . ? 4.882 -32.164 47.759 1.00 67.87 ? 331 NAG A C5 1 HETATM 3949 C C6 . NAG D 3 . ? 6.396 -32.180 47.527 1.00 68.25 ? 331 NAG A C6 1 HETATM 3950 C C7 . NAG D 3 . ? 0.613 -33.204 49.653 1.00 70.17 ? 331 NAG A C7 1 HETATM 3951 C C8 . NAG D 3 . ? -0.303 -34.380 49.440 1.00 70.24 ? 331 NAG A C8 1 HETATM 3952 N N2 . NAG D 3 . ? 1.240 -32.727 48.567 1.00 69.22 ? 331 NAG A N2 1 HETATM 3953 O O3 . NAG D 3 . ? 1.973 -30.267 46.451 1.00 67.93 ? 331 NAG A O3 1 HETATM 3954 O O4 . NAG D 3 . ? 4.266 -31.966 45.426 1.00 67.67 ? 331 NAG A O4 1 HETATM 3955 O O5 . NAG D 3 . ? 4.649 -31.516 48.993 1.00 66.99 ? 331 NAG A O5 1 HETATM 3956 O O6 . NAG D 3 . ? 6.728 -32.063 46.158 1.00 70.04 ? 331 NAG A O6 1 HETATM 3957 O O7 . NAG D 3 . ? 0.750 -32.741 50.785 1.00 71.68 ? 331 NAG A O7 1 HETATM 3958 C C1 . NAG E 3 . ? 36.709 4.349 -7.820 1.00 56.61 ? 332 NAG A C1 1 HETATM 3959 C C2 . NAG E 3 . ? 37.693 5.279 -7.091 1.00 61.86 ? 332 NAG A C2 1 HETATM 3960 C C3 . NAG E 3 . ? 37.678 6.753 -7.541 1.00 63.06 ? 332 NAG A C3 1 HETATM 3961 C C4 . NAG E 3 . ? 37.116 7.035 -8.947 1.00 64.20 ? 332 NAG A C4 1 HETATM 3962 C C5 . NAG E 3 . ? 35.957 6.092 -9.296 1.00 63.67 ? 332 NAG A C5 1 HETATM 3963 C C6 . NAG E 3 . ? 35.388 6.348 -10.697 1.00 64.78 ? 332 NAG A C6 1 HETATM 3964 C C7 . NAG E 3 . ? 38.192 4.660 -4.747 1.00 64.57 ? 332 NAG A C7 1 HETATM 3965 C C8 . NAG E 3 . ? 37.690 4.671 -3.332 1.00 64.35 ? 332 NAG A C8 1 HETATM 3966 N N2 . NAG E 3 . ? 37.386 5.204 -5.664 1.00 63.51 ? 332 NAG A N2 1 HETATM 3967 O O3 . NAG E 3 . ? 39.002 7.235 -7.484 1.00 63.96 ? 332 NAG A O3 1 HETATM 3968 O O4 . NAG E 3 . ? 36.718 8.395 -9.042 1.00 65.84 ? 332 NAG A O4 1 HETATM 3969 O O5 . NAG E 3 . ? 36.412 4.745 -9.160 1.00 61.54 ? 332 NAG A O5 1 HETATM 3970 O O6 . NAG E 3 . ? 35.672 5.276 -11.576 1.00 65.73 ? 332 NAG A O6 1 HETATM 3971 O O7 . NAG E 3 . ? 39.299 4.180 -5.011 1.00 65.48 ? 332 NAG A O7 1 HETATM 3972 C C1 . EDO F 4 . ? 9.838 -14.835 60.805 1.00 34.56 ? 1 EDO A C1 1 HETATM 3973 O O1 . EDO F 4 . ? 8.918 -15.890 61.083 1.00 34.74 ? 1 EDO A O1 1 HETATM 3974 C C2 . EDO F 4 . ? 9.125 -13.549 60.399 1.00 34.19 ? 1 EDO A C2 1 HETATM 3975 O O2 . EDO F 4 . ? 8.157 -13.811 59.383 1.00 31.88 ? 1 EDO A O2 1 HETATM 3976 C C1 . NAG G 3 . ? 9.660 -16.847 -33.471 1.00 62.09 ? 175 NAG B C1 1 HETATM 3977 C C2 . NAG G 3 . ? 8.253 -17.479 -33.285 1.00 65.97 ? 175 NAG B C2 1 HETATM 3978 C C3 . NAG G 3 . ? 7.294 -17.358 -34.487 1.00 67.49 ? 175 NAG B C3 1 HETATM 3979 C C4 . NAG G 3 . ? 7.452 -16.035 -35.250 1.00 67.43 ? 175 NAG B C4 1 HETATM 3980 C C5 . NAG G 3 . ? 8.947 -15.838 -35.551 1.00 66.93 ? 175 NAG B C5 1 HETATM 3981 C C6 . NAG G 3 . ? 9.268 -14.638 -36.446 1.00 67.13 ? 175 NAG B C6 1 HETATM 3982 C C7 . NAG G 3 . ? 8.652 -19.423 -31.826 1.00 67.65 ? 175 NAG B C7 1 HETATM 3983 C C8 . NAG G 3 . ? 8.813 -20.919 -31.789 1.00 67.19 ? 175 NAG B C8 1 HETATM 3984 N N2 . NAG G 3 . ? 8.422 -18.898 -33.028 1.00 66.73 ? 175 NAG B N2 1 HETATM 3985 O O3 . NAG G 3 . ? 5.944 -17.580 -34.097 1.00 68.51 ? 175 NAG B O3 1 HETATM 3986 O O4 . NAG G 3 . ? 6.666 -16.031 -36.430 1.00 68.00 ? 175 NAG B O4 1 HETATM 3987 O O5 . NAG G 3 . ? 9.639 -15.698 -34.317 1.00 64.96 ? 175 NAG B O5 1 HETATM 3988 O O6 . NAG G 3 . ? 8.642 -13.467 -35.953 1.00 68.12 ? 175 NAG B O6 1 HETATM 3989 O O7 . NAG G 3 . ? 8.728 -18.753 -30.793 1.00 68.36 ? 175 NAG B O7 1 HETATM 3990 C C1 . PEG H 5 . ? 31.001 -1.192 -32.263 1.00 52.04 ? 176 PEG B C1 1 HETATM 3991 O O1 . PEG H 5 . ? 31.327 0.139 -32.690 1.00 54.40 ? 176 PEG B O1 1 HETATM 3992 C C2 . PEG H 5 . ? 29.759 -1.684 -32.993 1.00 50.65 ? 176 PEG B C2 1 HETATM 3993 O O2 . PEG H 5 . ? 28.697 -1.906 -32.066 1.00 50.94 ? 176 PEG B O2 1 HETATM 3994 C C3 . PEG H 5 . ? 27.451 -2.217 -32.692 1.00 47.58 ? 176 PEG B C3 1 HETATM 3995 C C4 . PEG H 5 . ? 26.313 -1.653 -31.866 1.00 47.33 ? 176 PEG B C4 1 HETATM 3996 O O4 . PEG H 5 . ? 25.086 -1.602 -32.608 1.00 48.73 ? 176 PEG B O4 1 HETATM 3997 O O . HOH I 6 . ? 21.176 2.022 36.418 1.00 22.76 ? 2 HOH A O 1 HETATM 3998 O O . HOH I 6 . ? 29.879 -19.242 35.915 1.00 22.06 ? 3 HOH A O 1 HETATM 3999 O O . HOH I 6 . ? 11.600 -10.961 57.664 1.00 20.46 ? 4 HOH A O 1 HETATM 4000 O O . HOH I 6 . ? 9.325 -3.022 34.107 1.00 23.24 ? 5 HOH A O 1 HETATM 4001 O O . HOH I 6 . ? 28.803 -14.437 40.098 1.00 20.42 ? 6 HOH A O 1 HETATM 4002 O O . HOH I 6 . ? 20.267 -9.701 63.172 1.00 23.47 ? 8 HOH A O 1 HETATM 4003 O O . HOH I 6 . ? 13.248 0.681 47.062 1.00 20.59 ? 333 HOH A O 1 HETATM 4004 O O . HOH I 6 . ? 19.922 -24.944 66.278 1.00 46.17 ? 334 HOH A O 1 HETATM 4005 O O . HOH I 6 . ? 10.309 -4.816 42.449 1.00 22.71 ? 335 HOH A O 1 HETATM 4006 O O . HOH I 6 . ? 17.728 10.242 21.267 1.00 50.61 ? 336 HOH A O 1 HETATM 4007 O O . HOH I 6 . ? 2.870 -9.607 33.232 1.00 47.88 ? 337 HOH A O 1 HETATM 4008 O O . HOH I 6 . ? 8.536 -31.057 49.477 1.00 55.11 ? 338 HOH A O 1 HETATM 4009 O O . HOH I 6 . ? 26.517 -1.846 39.975 1.00 43.27 ? 339 HOH A O 1 HETATM 4010 O O . HOH I 6 . ? 23.753 6.558 38.540 1.00 25.34 ? 340 HOH A O 1 HETATM 4011 O O . HOH I 6 . ? 25.609 -13.691 53.128 1.00 26.01 ? 341 HOH A O 1 HETATM 4012 O O . HOH I 6 . ? 5.448 -23.939 44.504 1.00 33.79 ? 342 HOH A O 1 HETATM 4013 O O . HOH I 6 . ? 21.451 5.291 62.520 1.00 59.18 ? 343 HOH A O 1 HETATM 4014 O O . HOH I 6 . ? 17.946 -16.132 27.590 1.00 44.77 ? 344 HOH A O 1 HETATM 4015 O O . HOH I 6 . ? 30.505 -8.313 -16.185 1.00 27.10 ? 345 HOH A O 1 HETATM 4016 O O . HOH I 6 . ? 18.437 2.819 33.192 1.00 27.53 ? 346 HOH A O 1 HETATM 4017 O O . HOH I 6 . ? 6.843 2.856 44.430 1.00 43.37 ? 347 HOH A O 1 HETATM 4018 O O . HOH I 6 . ? 14.717 7.972 49.690 1.00 51.25 ? 348 HOH A O 1 HETATM 4019 O O . HOH I 6 . ? 31.008 -2.677 14.432 1.00 61.06 ? 349 HOH A O 1 HETATM 4020 O O . HOH I 6 . ? 18.701 9.457 41.970 1.00 50.50 ? 350 HOH A O 1 HETATM 4021 O O . HOH I 6 . ? 25.073 -3.583 39.055 1.00 24.84 ? 351 HOH A O 1 HETATM 4022 O O . HOH I 6 . ? 29.993 1.393 7.685 1.00 49.92 ? 352 HOH A O 1 HETATM 4023 O O . HOH I 6 . ? 24.947 5.167 6.578 1.00 52.22 ? 353 HOH A O 1 HETATM 4024 O O . HOH I 6 . ? 22.062 -14.928 28.248 1.00 51.97 ? 354 HOH A O 1 HETATM 4025 O O . HOH I 6 . ? 8.423 -7.535 38.880 1.00 24.02 ? 355 HOH A O 1 HETATM 4026 O O . HOH I 6 . ? 14.924 -3.178 59.671 1.00 24.13 ? 356 HOH A O 1 HETATM 4027 O O . HOH I 6 . ? 29.694 -1.381 49.010 1.00 26.11 ? 357 HOH A O 1 HETATM 4028 O O . HOH I 6 . ? 11.373 -4.110 45.123 1.00 25.93 ? 358 HOH A O 1 HETATM 4029 O O . HOH I 6 . ? 27.385 -23.557 50.612 1.00 38.30 ? 359 HOH A O 1 HETATM 4030 O O . HOH I 6 . ? 25.051 -15.917 46.994 1.00 22.11 ? 360 HOH A O 1 HETATM 4031 O O . HOH I 6 . ? 5.427 10.863 22.926 1.00 55.70 ? 361 HOH A O 1 HETATM 4032 O O . HOH I 6 . ? 22.263 -9.503 29.672 1.00 47.39 ? 362 HOH A O 1 HETATM 4033 O O . HOH I 6 . ? 16.656 6.929 23.956 1.00 26.90 ? 363 HOH A O 1 HETATM 4034 O O . HOH I 6 . ? 29.222 -1.846 34.896 1.00 62.06 ? 364 HOH A O 1 HETATM 4035 O O . HOH I 6 . ? 26.470 -11.699 34.190 1.00 22.95 ? 365 HOH A O 1 HETATM 4036 O O . HOH I 6 . ? 8.539 -2.780 31.470 1.00 25.86 ? 366 HOH A O 1 HETATM 4037 O O . HOH I 6 . ? 11.000 1.141 33.968 1.00 25.30 ? 367 HOH A O 1 HETATM 4038 O O . HOH I 6 . ? 22.157 4.857 47.441 1.00 27.13 ? 368 HOH A O 1 HETATM 4039 O O . HOH I 6 . ? 26.768 -7.820 75.421 1.00 61.74 ? 369 HOH A O 1 HETATM 4040 O O . HOH I 6 . ? 13.019 6.259 58.698 1.00 57.78 ? 370 HOH A O 1 HETATM 4041 O O . HOH I 6 . ? 25.934 0.525 42.061 1.00 56.98 ? 371 HOH A O 1 HETATM 4042 O O . HOH I 6 . ? 31.239 -7.720 52.685 1.00 27.65 ? 372 HOH A O 1 HETATM 4043 O O . HOH I 6 . ? 35.121 -4.296 52.690 1.00 26.58 ? 373 HOH A O 1 HETATM 4044 O O . HOH I 6 . ? 32.840 -7.007 19.546 1.00 53.44 ? 374 HOH A O 1 HETATM 4045 O O . HOH I 6 . ? 2.483 -25.906 52.491 1.00 47.40 ? 375 HOH A O 1 HETATM 4046 O O . HOH I 6 . ? 2.567 -5.786 31.806 1.00 47.40 ? 376 HOH A O 1 HETATM 4047 O O . HOH I 6 . ? 22.223 8.630 63.797 1.00 55.00 ? 377 HOH A O 1 HETATM 4048 O O . HOH I 6 . ? 8.621 -2.790 15.320 1.00 58.67 ? 378 HOH A O 1 HETATM 4049 O O . HOH I 6 . ? 4.025 -10.179 26.848 1.00 51.05 ? 379 HOH A O 1 HETATM 4050 O O . HOH I 6 . ? 4.537 0.515 36.187 1.00 41.75 ? 380 HOH A O 1 HETATM 4051 O O . HOH I 6 . ? 42.943 -5.463 -11.085 1.00 59.09 ? 381 HOH A O 1 HETATM 4052 O O . HOH I 6 . ? 19.428 0.281 65.311 1.00 54.08 ? 382 HOH A O 1 HETATM 4053 O O . HOH I 6 . ? 24.936 9.118 35.653 1.00 46.22 ? 383 HOH A O 1 HETATM 4054 O O . HOH I 6 . ? 9.877 -16.671 63.413 1.00 51.30 ? 384 HOH A O 1 HETATM 4055 O O . HOH I 6 . ? 4.359 -21.189 52.447 1.00 29.33 ? 385 HOH A O 1 HETATM 4056 O O . HOH I 6 . ? 31.757 -17.674 58.936 1.00 49.32 ? 386 HOH A O 1 HETATM 4057 O O . HOH I 6 . ? 7.087 -17.758 56.822 1.00 49.22 ? 387 HOH A O 1 HETATM 4058 O O . HOH I 6 . ? 17.383 3.503 11.006 1.00 53.10 ? 388 HOH A O 1 HETATM 4059 O O . HOH I 6 . ? 3.288 -3.012 26.785 1.00 51.33 ? 389 HOH A O 1 HETATM 4060 O O . HOH I 6 . ? 32.554 -3.578 50.696 1.00 35.49 ? 390 HOH A O 1 HETATM 4061 O O . HOH I 6 . ? 12.855 -1.632 44.906 1.00 31.23 ? 391 HOH A O 1 HETATM 4062 O O . HOH I 6 . ? 22.983 1.160 62.894 1.00 49.72 ? 392 HOH A O 1 HETATM 4063 O O . HOH I 6 . ? 29.900 -7.294 75.076 1.00 62.21 ? 393 HOH A O 1 HETATM 4064 O O . HOH I 6 . ? 23.810 -29.051 51.526 1.00 29.09 ? 394 HOH A O 1 HETATM 4065 O O . HOH I 6 . ? 31.181 -19.770 57.676 1.00 62.35 ? 395 HOH A O 1 HETATM 4066 O O . HOH I 6 . ? 27.908 -2.510 -19.496 1.00 32.92 ? 396 HOH A O 1 HETATM 4067 O O . HOH I 6 . ? 4.807 -4.230 30.844 1.00 31.29 ? 397 HOH A O 1 HETATM 4068 O O . HOH I 6 . ? 16.087 -17.633 27.349 1.00 48.87 ? 398 HOH A O 1 HETATM 4069 O O . HOH I 6 . ? 9.378 3.425 36.994 1.00 54.78 ? 399 HOH A O 1 HETATM 4070 O O . HOH I 6 . ? 34.260 3.416 61.718 1.00 46.65 ? 400 HOH A O 1 HETATM 4071 O O . HOH I 6 . ? 19.424 11.613 42.634 1.00 57.51 ? 401 HOH A O 1 HETATM 4072 O O . HOH I 6 . ? 27.166 5.689 45.194 1.00 44.58 ? 402 HOH A O 1 HETATM 4073 O O . HOH I 6 . ? 32.961 -9.751 43.385 1.00 53.92 ? 403 HOH A O 1 HETATM 4074 O O . HOH I 6 . ? 15.681 -23.019 63.854 1.00 45.08 ? 404 HOH A O 1 HETATM 4075 O O . HOH I 6 . ? 35.830 -7.428 18.419 1.00 61.24 ? 405 HOH A O 1 HETATM 4076 O O . HOH I 6 . ? 20.129 4.480 31.755 1.00 28.19 ? 406 HOH A O 1 HETATM 4077 O O . HOH I 6 . ? 13.595 -10.573 22.979 1.00 56.97 ? 407 HOH A O 1 HETATM 4078 O O . HOH I 6 . ? 29.666 7.973 60.115 1.00 52.46 ? 408 HOH A O 1 HETATM 4079 O O . HOH I 6 . ? 15.659 -24.990 46.486 1.00 26.44 ? 409 HOH A O 1 HETATM 4080 O O . HOH I 6 . ? 11.489 4.387 31.283 1.00 30.61 ? 410 HOH A O 1 HETATM 4081 O O . HOH I 6 . ? 0.378 -23.344 46.089 1.00 44.25 ? 411 HOH A O 1 HETATM 4082 O O . HOH I 6 . ? 0.394 -17.238 44.172 1.00 61.42 ? 412 HOH A O 1 HETATM 4083 O O . HOH I 6 . ? 25.817 -20.651 69.476 1.00 45.55 ? 413 HOH A O 1 HETATM 4084 O O . HOH I 6 . ? 8.558 -6.443 63.653 1.00 52.87 ? 414 HOH A O 1 HETATM 4085 O O . HOH I 6 . ? 11.076 5.213 34.042 1.00 57.67 ? 415 HOH A O 1 HETATM 4086 O O . HOH I 6 . ? 19.897 4.805 50.219 1.00 32.12 ? 416 HOH A O 1 HETATM 4087 O O . HOH I 6 . ? 28.176 0.710 -4.019 1.00 51.21 ? 417 HOH A O 1 HETATM 4088 O O . HOH I 6 . ? 33.185 2.325 70.299 1.00 68.52 ? 418 HOH A O 1 HETATM 4089 O O . HOH I 6 . ? 28.736 -20.727 65.794 1.00 67.95 ? 419 HOH A O 1 HETATM 4090 O O . HOH I 6 . ? 13.115 3.098 9.702 1.00 62.69 ? 420 HOH A O 1 HETATM 4091 O O . HOH I 6 . ? 11.928 -29.473 51.345 1.00 55.57 ? 421 HOH A O 1 HETATM 4092 O O . HOH I 6 . ? 28.267 0.992 48.708 1.00 31.45 ? 422 HOH A O 1 HETATM 4093 O O . HOH I 6 . ? 9.495 -28.225 51.648 1.00 29.52 ? 423 HOH A O 1 HETATM 4094 O O . HOH I 6 . ? 19.834 -16.688 32.330 1.00 29.60 ? 424 HOH A O 1 HETATM 4095 O O . HOH I 6 . ? 29.647 6.005 34.643 1.00 45.83 ? 425 HOH A O 1 HETATM 4096 O O . HOH I 6 . ? 3.320 -7.004 33.918 1.00 29.11 ? 426 HOH A O 1 HETATM 4097 O O . HOH I 6 . ? 3.035 -7.286 49.843 1.00 53.88 ? 427 HOH A O 1 HETATM 4098 O O . HOH I 6 . ? 7.588 -18.173 35.227 1.00 48.45 ? 428 HOH A O 1 HETATM 4099 O O . HOH I 6 . ? 25.017 -3.703 26.875 1.00 25.43 ? 429 HOH A O 1 HETATM 4100 O O . HOH I 6 . ? 19.049 8.800 34.140 1.00 57.92 ? 430 HOH A O 1 HETATM 4101 O O . HOH I 6 . ? 17.818 6.604 42.301 1.00 33.38 ? 431 HOH A O 1 HETATM 4102 O O . HOH I 6 . ? 25.213 -2.456 43.380 1.00 28.69 ? 432 HOH A O 1 HETATM 4103 O O . HOH I 6 . ? 10.895 -28.415 42.020 1.00 52.88 ? 433 HOH A O 1 HETATM 4104 O O . HOH I 6 . ? 18.026 -23.568 47.443 1.00 32.60 ? 434 HOH A O 1 HETATM 4105 O O . HOH I 6 . ? 27.064 5.438 34.859 1.00 28.61 ? 435 HOH A O 1 HETATM 4106 O O . HOH I 6 . ? 3.764 -6.305 38.375 1.00 30.97 ? 436 HOH A O 1 HETATM 4107 O O . HOH I 6 . ? 20.484 -20.894 43.316 1.00 31.21 ? 437 HOH A O 1 HETATM 4108 O O . HOH I 6 . ? 15.280 -9.997 6.534 1.00 63.06 ? 438 HOH A O 1 HETATM 4109 O O . HOH I 6 . ? 24.350 -12.578 75.613 1.00 53.87 ? 439 HOH A O 1 HETATM 4110 O O . HOH I 6 . ? 39.514 2.979 59.858 1.00 55.71 ? 440 HOH A O 1 HETATM 4111 O O . HOH I 6 . ? 7.188 -4.976 15.782 1.00 60.57 ? 441 HOH A O 1 HETATM 4112 O O . HOH I 6 . ? 23.537 3.538 25.180 1.00 49.92 ? 442 HOH A O 1 HETATM 4113 O O . HOH I 6 . ? 8.716 6.956 27.139 1.00 61.88 ? 443 HOH A O 1 HETATM 4114 O O . HOH I 6 . ? 29.711 4.058 17.613 1.00 59.25 ? 444 HOH A O 1 HETATM 4115 O O . HOH I 6 . ? 14.559 -2.850 73.579 1.00 59.70 ? 445 HOH A O 1 HETATM 4116 O O . HOH I 6 . ? 36.416 2.098 60.487 1.00 41.54 ? 446 HOH A O 1 HETATM 4117 O O . HOH I 6 . ? 33.997 -5.508 3.197 1.00 53.22 ? 447 HOH A O 1 HETATM 4118 O O . HOH I 6 . ? 17.608 -24.017 43.022 1.00 54.87 ? 448 HOH A O 1 HETATM 4119 O O . HOH I 6 . ? 5.839 -21.225 54.698 1.00 26.84 ? 449 HOH A O 1 HETATM 4120 O O . HOH I 6 . ? 13.586 -29.192 43.178 1.00 64.18 ? 450 HOH A O 1 HETATM 4121 O O . HOH I 6 . ? 37.032 0.608 -12.920 1.00 64.33 ? 451 HOH A O 1 HETATM 4122 O O . HOH I 6 . ? 2.900 -34.520 51.617 1.00 69.76 ? 452 HOH A O 1 HETATM 4123 O O . HOH I 6 . ? 17.940 -4.570 -16.471 1.00 52.67 ? 453 HOH A O 1 HETATM 4124 O O . HOH I 6 . ? 32.954 -18.072 44.583 1.00 57.50 ? 454 HOH A O 1 HETATM 4125 O O . HOH I 6 . ? 6.177 -4.720 62.199 1.00 46.05 ? 455 HOH A O 1 HETATM 4126 O O . HOH I 6 . ? 29.673 -16.669 41.319 1.00 29.01 ? 456 HOH A O 1 HETATM 4127 O O . HOH I 6 . ? 11.446 -25.743 41.199 1.00 39.60 ? 457 HOH A O 1 HETATM 4128 O O . HOH I 6 . ? 15.944 -2.498 4.984 1.00 57.01 ? 458 HOH A O 1 HETATM 4129 O O . HOH I 6 . ? 37.540 6.380 59.960 1.00 66.78 ? 459 HOH A O 1 HETATM 4130 O O . HOH I 6 . ? 29.803 5.464 31.255 1.00 54.72 ? 460 HOH A O 1 HETATM 4131 O O . HOH I 6 . ? 17.076 8.028 37.821 1.00 60.28 ? 461 HOH A O 1 HETATM 4132 O O . HOH I 6 . ? 37.071 6.194 53.552 1.00 52.63 ? 462 HOH A O 1 HETATM 4133 O O . HOH I 6 . ? 11.527 10.815 21.671 1.00 57.98 ? 463 HOH A O 1 HETATM 4134 O O . HOH I 6 . ? 27.510 -11.304 -6.621 1.00 30.90 ? 464 HOH A O 1 HETATM 4135 O O . HOH I 6 . ? 3.735 4.243 24.548 1.00 61.05 ? 465 HOH A O 1 HETATM 4136 O O . HOH I 6 . ? 18.275 10.962 49.954 1.00 54.43 ? 466 HOH A O 1 HETATM 4137 O O . HOH I 6 . ? 4.610 -5.913 48.012 1.00 57.14 ? 467 HOH A O 1 HETATM 4138 O O . HOH I 6 . ? 8.341 -26.160 55.649 1.00 33.68 ? 468 HOH A O 1 HETATM 4139 O O . HOH I 6 . ? 17.609 -0.798 -14.016 1.00 58.16 ? 469 HOH A O 1 HETATM 4140 O O . HOH I 6 . ? 36.019 4.606 51.179 1.00 55.44 ? 470 HOH A O 1 HETATM 4141 O O . HOH I 6 . ? 7.217 3.505 33.264 1.00 47.46 ? 471 HOH A O 1 HETATM 4142 O O . HOH I 6 . ? 14.546 11.747 26.245 1.00 50.50 ? 472 HOH A O 1 HETATM 4143 O O . HOH I 6 . ? 31.247 -11.267 49.542 1.00 31.08 ? 473 HOH A O 1 HETATM 4144 O O . HOH I 6 . ? 30.053 -7.492 45.747 1.00 36.04 ? 474 HOH A O 1 HETATM 4145 O O . HOH I 6 . ? 3.338 -0.642 28.712 1.00 46.56 ? 475 HOH A O 1 HETATM 4146 O O . HOH I 6 . ? 7.142 -32.766 52.466 1.00 74.08 ? 476 HOH A O 1 HETATM 4147 O O . HOH I 6 . ? 5.137 -6.017 56.470 1.00 32.21 ? 477 HOH A O 1 HETATM 4148 O O . HOH I 6 . ? 25.932 -26.770 47.567 1.00 42.70 ? 478 HOH A O 1 HETATM 4149 O O . HOH I 6 . ? 19.951 6.717 24.143 1.00 58.14 ? 479 HOH A O 1 HETATM 4150 O O . HOH I 6 . ? 33.894 -15.481 59.624 1.00 52.29 ? 480 HOH A O 1 HETATM 4151 O O . HOH I 6 . ? 11.559 -12.839 66.782 1.00 30.89 ? 481 HOH A O 1 HETATM 4152 O O . HOH I 6 . ? 12.203 -22.348 61.389 1.00 56.36 ? 482 HOH A O 1 HETATM 4153 O O . HOH I 6 . ? 8.656 -9.368 28.092 1.00 45.64 ? 483 HOH A O 1 HETATM 4154 O O . HOH I 6 . ? 11.712 -0.031 67.756 1.00 59.86 ? 484 HOH A O 1 HETATM 4155 O O . HOH I 6 . ? 9.306 -2.393 53.212 1.00 32.11 ? 485 HOH A O 1 HETATM 4156 O O . HOH I 6 . ? 14.739 15.188 60.034 1.00 56.12 ? 486 HOH A O 1 HETATM 4157 O O . HOH I 6 . ? 11.745 11.058 51.375 1.00 38.09 ? 487 HOH A O 1 HETATM 4158 O O . HOH I 6 . ? 6.597 4.270 46.544 1.00 55.92 ? 488 HOH A O 1 HETATM 4159 O O . HOH I 6 . ? 2.060 -11.460 45.562 1.00 55.67 ? 489 HOH A O 1 HETATM 4160 O O . HOH I 6 . ? 8.171 -6.202 41.303 1.00 28.09 ? 490 HOH A O 1 HETATM 4161 O O . HOH I 6 . ? 11.382 -19.661 66.701 1.00 57.98 ? 491 HOH A O 1 HETATM 4162 O O . HOH I 6 . ? 17.771 -8.944 9.177 1.00 50.61 ? 492 HOH A O 1 HETATM 4163 O O . HOH I 6 . ? 19.005 -23.202 41.015 1.00 58.05 ? 493 HOH A O 1 HETATM 4164 O O . HOH I 6 . ? 29.854 -0.640 17.861 1.00 55.22 ? 494 HOH A O 1 HETATM 4165 O O . HOH I 6 . ? 22.872 -8.545 16.181 1.00 36.00 ? 495 HOH A O 1 HETATM 4166 O O . HOH I 6 . ? 32.198 -5.244 47.484 1.00 38.86 ? 496 HOH A O 1 HETATM 4167 O O . HOH I 6 . ? 5.957 -7.388 42.400 1.00 31.93 ? 497 HOH A O 1 HETATM 4168 O O . HOH I 6 . ? 19.423 -22.646 58.988 1.00 35.43 ? 498 HOH A O 1 HETATM 4169 O O . HOH I 6 . ? 12.854 -9.538 25.202 1.00 31.94 ? 499 HOH A O 1 HETATM 4170 O O . HOH I 6 . ? 27.520 -1.761 2.445 1.00 42.17 ? 500 HOH A O 1 HETATM 4171 O O . HOH I 6 . ? 26.048 2.123 25.816 1.00 46.56 ? 501 HOH A O 1 HETATM 4172 O O . HOH I 6 . ? 5.929 -17.113 61.784 1.00 51.51 ? 502 HOH A O 1 HETATM 4173 O O . HOH I 6 . ? 12.593 5.825 14.591 1.00 58.25 ? 503 HOH A O 1 HETATM 4174 O O . HOH I 6 . ? 14.869 -22.000 61.221 1.00 38.19 ? 504 HOH A O 1 HETATM 4175 O O . HOH I 6 . ? 13.240 -3.228 57.542 1.00 35.84 ? 505 HOH A O 1 HETATM 4176 O O . HOH I 6 . ? 18.238 11.307 63.106 1.00 57.07 ? 506 HOH A O 1 HETATM 4177 O O . HOH I 6 . ? 17.739 -11.925 24.410 1.00 52.00 ? 507 HOH A O 1 HETATM 4178 O O . HOH I 6 . ? 12.154 10.278 26.568 1.00 56.60 ? 508 HOH A O 1 HETATM 4179 O O . HOH I 6 . ? 13.111 0.855 56.697 1.00 46.57 ? 509 HOH A O 1 HETATM 4180 O O . HOH I 6 . ? 14.970 1.311 59.198 1.00 34.55 ? 510 HOH A O 1 HETATM 4181 O O . HOH I 6 . ? 11.007 -4.628 55.304 1.00 29.66 ? 511 HOH A O 1 HETATM 4182 O O . HOH I 6 . ? 29.255 0.662 60.328 1.00 29.84 ? 512 HOH A O 1 HETATM 4183 O O . HOH I 6 . ? 32.473 -10.062 53.588 1.00 32.91 ? 513 HOH A O 1 HETATM 4184 O O . HOH I 6 . ? 22.888 6.765 25.614 1.00 57.45 ? 514 HOH A O 1 HETATM 4185 O O . HOH I 6 . ? 30.065 1.759 18.998 1.00 59.22 ? 515 HOH A O 1 HETATM 4186 O O . HOH I 6 . ? 26.359 -1.512 26.008 1.00 52.21 ? 516 HOH A O 1 HETATM 4187 O O . HOH I 6 . ? 26.704 -5.325 28.191 1.00 53.99 ? 517 HOH A O 1 HETATM 4188 O O . HOH I 6 . ? 30.481 -14.534 55.762 1.00 51.76 ? 518 HOH A O 1 HETATM 4189 O O . HOH I 6 . ? 6.543 2.703 28.154 1.00 53.33 ? 519 HOH A O 1 HETATM 4190 O O . HOH I 6 . ? 31.175 -15.312 46.316 1.00 55.91 ? 520 HOH A O 1 HETATM 4191 O O . HOH I 6 . ? 16.147 -3.431 64.297 1.00 35.90 ? 521 HOH A O 1 HETATM 4192 O O . HOH I 6 . ? 33.731 -1.097 -3.678 1.00 50.62 ? 522 HOH A O 1 HETATM 4193 O O . HOH I 6 . ? 11.733 -12.800 23.937 1.00 60.61 ? 523 HOH A O 1 HETATM 4194 O O . HOH I 6 . ? 9.694 6.316 30.654 1.00 53.84 ? 524 HOH A O 1 HETATM 4195 O O . HOH I 6 . ? 33.169 1.853 47.391 1.00 61.98 ? 525 HOH A O 1 HETATM 4196 O O . HOH I 6 . ? 23.722 5.077 61.371 1.00 33.44 ? 526 HOH A O 1 HETATM 4197 O O . HOH I 6 . ? 18.582 9.044 26.335 1.00 38.45 ? 527 HOH A O 1 HETATM 4198 O O . HOH I 6 . ? 31.929 6.554 50.367 1.00 37.27 ? 528 HOH A O 1 HETATM 4199 O O . HOH I 6 . ? 32.413 7.500 54.042 1.00 38.28 ? 529 HOH A O 1 HETATM 4200 O O . HOH I 6 . ? 8.985 -7.949 23.135 1.00 34.41 ? 530 HOH A O 1 HETATM 4201 O O . HOH I 6 . ? 1.237 -19.262 39.923 1.00 57.90 ? 531 HOH A O 1 HETATM 4202 O O . HOH I 6 . ? 18.108 0.663 11.092 1.00 33.10 ? 532 HOH A O 1 HETATM 4203 O O . HOH I 6 . ? 33.688 4.994 48.725 1.00 62.17 ? 533 HOH A O 1 HETATM 4204 O O . HOH I 6 . ? 4.003 -8.388 47.867 1.00 53.55 ? 534 HOH A O 1 HETATM 4205 O O . HOH I 6 . ? 29.990 -11.429 42.872 1.00 32.31 ? 535 HOH A O 1 HETATM 4206 O O . HOH I 6 . ? 25.427 -26.884 50.298 1.00 32.75 ? 536 HOH A O 1 HETATM 4207 O O . HOH I 6 . ? 21.754 -24.651 57.334 1.00 37.42 ? 537 HOH A O 1 HETATM 4208 O O . HOH I 6 . ? 25.942 7.037 36.847 1.00 35.07 ? 538 HOH A O 1 HETATM 4209 O O . HOH I 6 . ? 15.421 11.802 51.640 1.00 35.08 ? 539 HOH A O 1 HETATM 4210 O O . HOH I 6 . ? 15.352 2.184 13.680 1.00 37.02 ? 540 HOH A O 1 HETATM 4211 O O . HOH I 6 . ? 12.660 -3.049 14.126 1.00 31.49 ? 541 HOH A O 1 HETATM 4212 O O . HOH I 6 . ? 22.007 -0.365 4.113 1.00 60.99 ? 542 HOH A O 1 HETATM 4213 O O . HOH I 6 . ? 12.073 -3.074 70.334 1.00 62.94 ? 543 HOH A O 1 HETATM 4214 O O . HOH I 6 . ? 5.781 -5.432 44.333 1.00 31.14 ? 544 HOH A O 1 HETATM 4215 O O . HOH I 6 . ? 30.836 -13.888 44.464 1.00 31.72 ? 545 HOH A O 1 HETATM 4216 O O . HOH I 6 . ? 32.965 -8.549 -16.799 1.00 34.59 ? 546 HOH A O 1 HETATM 4217 O O . HOH I 6 . ? 8.990 -0.404 34.913 1.00 25.85 ? 547 HOH A O 1 HETATM 4218 O O . HOH I 6 . ? 6.945 -0.527 31.958 1.00 34.99 ? 548 HOH A O 1 HETATM 4219 O O . HOH I 6 . ? 3.578 -17.708 49.652 1.00 32.13 ? 549 HOH A O 1 HETATM 4220 O O . HOH I 6 . ? 4.365 -1.722 31.047 1.00 30.33 ? 550 HOH A O 1 HETATM 4221 O O . HOH I 6 . ? 31.104 -13.363 39.976 1.00 29.93 ? 551 HOH A O 1 HETATM 4222 O O . HOH I 6 . ? 7.413 -4.255 53.882 1.00 37.03 ? 552 HOH A O 1 HETATM 4223 O O . HOH I 6 . ? 24.629 2.630 60.719 1.00 33.62 ? 553 HOH A O 1 HETATM 4224 O O . HOH I 6 . ? 17.947 6.362 32.824 1.00 42.16 ? 554 HOH A O 1 HETATM 4225 O O . HOH I 6 . ? 20.278 9.185 43.483 1.00 45.44 ? 555 HOH A O 1 HETATM 4226 O O . HOH I 6 . ? 24.557 2.758 47.066 1.00 34.58 ? 556 HOH A O 1 HETATM 4227 O O . HOH I 6 . ? 9.937 10.097 23.519 1.00 38.55 ? 557 HOH A O 1 HETATM 4228 O O . HOH I 6 . ? 6.446 -15.823 59.000 1.00 34.52 ? 558 HOH A O 1 HETATM 4229 O O . HOH I 6 . ? 8.825 -18.351 59.838 1.00 34.16 ? 559 HOH A O 1 HETATM 4230 O O . HOH I 6 . ? 3.282 -23.703 53.467 1.00 39.57 ? 560 HOH A O 1 HETATM 4231 O O . HOH I 6 . ? 22.667 1.260 5.846 1.00 40.09 ? 561 HOH A O 1 HETATM 4232 O O . HOH I 6 . ? 19.500 -32.573 48.720 1.00 35.99 ? 562 HOH A O 1 HETATM 4233 O O . HOH I 6 . ? 31.681 2.934 61.023 1.00 42.77 ? 563 HOH A O 1 HETATM 4234 O O . HOH I 6 . ? 22.579 -17.632 36.911 1.00 41.50 ? 564 HOH A O 1 HETATM 4235 O O . HOH I 6 . ? 24.147 -18.694 48.557 1.00 39.15 ? 565 HOH A O 1 HETATM 4236 O O . HOH I 6 . ? 14.608 -4.540 11.848 1.00 44.88 ? 566 HOH A O 1 HETATM 4237 O O . HOH I 6 . ? 13.955 -10.673 73.138 1.00 53.51 ? 567 HOH A O 1 HETATM 4238 O O . HOH I 6 . ? 23.619 -19.076 39.300 1.00 41.76 ? 568 HOH A O 1 HETATM 4239 O O . HOH I 6 . ? 11.638 3.207 35.969 1.00 30.66 ? 569 HOH A O 1 HETATM 4240 O O . HOH I 6 . ? 31.685 -5.342 -2.961 1.00 28.95 ? 570 HOH A O 1 HETATM 4241 O O . HOH I 6 . ? 28.419 2.921 -18.872 1.00 47.88 ? 571 HOH A O 1 HETATM 4242 O O . HOH I 6 . ? 18.243 11.962 54.287 1.00 44.11 ? 572 HOH A O 1 HETATM 4243 O O . HOH I 6 . ? 26.073 -18.000 68.651 1.00 45.91 ? 573 HOH A O 1 HETATM 4244 O O . HOH I 6 . ? 20.977 -2.046 -2.382 1.00 43.08 ? 574 HOH A O 1 HETATM 4245 O O . HOH I 6 . ? 6.914 -3.401 48.185 1.00 38.92 ? 575 HOH A O 1 HETATM 4246 O O . HOH I 6 . ? 2.799 -11.188 49.564 1.00 36.63 ? 576 HOH A O 1 HETATM 4247 O O . HOH I 6 . ? 11.508 -8.238 18.499 1.00 43.85 ? 577 HOH A O 1 HETATM 4248 O O . HOH I 6 . ? 5.575 -26.464 55.318 1.00 35.96 ? 578 HOH A O 1 HETATM 4249 O O . HOH I 6 . ? 25.774 -15.682 55.095 1.00 38.71 ? 579 HOH A O 1 HETATM 4250 O O . HOH I 6 . ? 26.780 -0.790 45.609 1.00 35.15 ? 580 HOH A O 1 HETATM 4251 O O . HOH I 6 . ? 15.737 -9.346 31.700 1.00 34.17 ? 581 HOH A O 1 HETATM 4252 O O . HOH I 6 . ? 23.193 -4.817 25.325 1.00 39.95 ? 582 HOH A O 1 HETATM 4253 O O . HOH I 6 . ? 3.843 -3.743 38.844 1.00 44.22 ? 583 HOH A O 1 HETATM 4254 O O . HOH I 6 . ? 20.585 -0.382 63.268 1.00 45.17 ? 584 HOH A O 1 HETATM 4255 O O . HOH I 6 . ? 9.666 -9.098 25.448 1.00 45.41 ? 585 HOH A O 1 HETATM 4256 O O . HOH I 6 . ? 6.673 0.803 42.407 1.00 43.19 ? 586 HOH A O 1 HETATM 4257 O O . HOH I 6 . ? 41.051 -3.632 60.555 1.00 49.96 ? 587 HOH A O 1 HETATM 4258 O O . HOH I 6 . ? 28.504 0.245 1.096 1.00 38.35 ? 588 HOH A O 1 HETATM 4259 O O . HOH I 6 . ? 10.463 1.745 31.385 1.00 38.60 ? 589 HOH A O 1 HETATM 4260 O O . HOH I 6 . ? 26.342 6.832 57.023 1.00 38.98 ? 590 HOH A O 1 HETATM 4261 O O . HOH I 6 . ? 12.361 -27.280 57.935 1.00 35.20 ? 591 HOH A O 1 HETATM 4262 O O . HOH I 6 . ? 12.417 6.141 43.380 1.00 35.96 ? 592 HOH A O 1 HETATM 4263 O O . HOH I 6 . ? 12.447 8.171 29.606 1.00 43.70 ? 593 HOH A O 1 HETATM 4264 O O . HOH I 6 . ? 19.310 8.705 31.354 1.00 46.51 ? 594 HOH A O 1 HETATM 4265 O O . HOH I 6 . ? 16.318 16.450 56.960 1.00 45.16 ? 595 HOH A O 1 HETATM 4266 O O . HOH I 6 . ? 15.852 -11.385 22.289 1.00 55.61 ? 596 HOH A O 1 HETATM 4267 O O . HOH I 6 . ? 1.838 -11.720 59.563 1.00 46.76 ? 597 HOH A O 1 HETATM 4268 O O . HOH I 6 . ? 23.665 6.528 20.081 1.00 38.72 ? 598 HOH A O 1 HETATM 4269 O O . HOH I 6 . ? 1.912 -6.678 36.193 1.00 35.53 ? 599 HOH A O 1 HETATM 4270 O O . HOH I 6 . ? 29.984 -16.853 49.689 1.00 54.98 ? 600 HOH A O 1 HETATM 4271 O O . HOH I 6 . ? 8.336 3.789 24.815 1.00 38.53 ? 601 HOH A O 1 HETATM 4272 O O . HOH I 6 . ? 13.152 0.310 14.886 1.00 40.02 ? 602 HOH A O 1 HETATM 4273 O O . HOH I 6 . ? 8.106 -1.125 51.074 1.00 37.91 ? 603 HOH A O 1 HETATM 4274 O O . HOH I 6 . ? 27.955 -5.511 -30.725 1.00 43.30 ? 604 HOH A O 1 HETATM 4275 O O . HOH I 6 . ? 11.044 -2.229 59.780 1.00 47.37 ? 605 HOH A O 1 HETATM 4276 O O . HOH I 6 . ? 20.687 -18.862 33.982 1.00 44.25 ? 606 HOH A O 1 HETATM 4277 O O . HOH I 6 . ? 24.688 5.477 26.865 1.00 35.64 ? 607 HOH A O 1 HETATM 4278 O O . HOH I 6 . ? 4.774 -7.972 40.071 1.00 44.64 ? 608 HOH A O 1 HETATM 4279 O O . HOH I 6 . ? 8.371 3.641 49.801 1.00 35.32 ? 609 HOH A O 1 HETATM 4280 O O . HOH I 6 . ? 21.530 -0.063 -10.598 1.00 42.37 ? 610 HOH A O 1 HETATM 4281 O O . HOH I 6 . ? 30.179 -12.321 66.130 1.00 46.54 ? 611 HOH A O 1 HETATM 4282 O O . HOH I 6 . ? 6.998 -17.618 31.253 1.00 37.21 ? 612 HOH A O 1 HETATM 4283 O O . HOH I 6 . ? 29.894 -17.136 46.741 1.00 56.40 ? 613 HOH A O 1 HETATM 4284 O O . HOH I 6 . ? 15.947 -6.696 12.459 1.00 45.45 ? 614 HOH A O 1 HETATM 4285 O O . HOH I 6 . ? 8.253 -23.810 56.445 1.00 43.15 ? 615 HOH A O 1 HETATM 4286 O O . HOH I 6 . ? 34.878 -11.030 64.419 1.00 40.36 ? 616 HOH A O 1 HETATM 4287 O O . HOH I 6 . ? 28.756 -15.931 53.176 1.00 47.89 ? 617 HOH A O 1 HETATM 4288 O O . HOH I 6 . ? 22.396 -19.594 31.138 1.00 36.85 ? 618 HOH A O 1 HETATM 4289 O O . HOH I 6 . ? 7.707 1.913 30.648 1.00 36.72 ? 619 HOH A O 1 HETATM 4290 O O . HOH I 6 . ? 31.890 -5.997 -0.392 1.00 53.38 ? 620 HOH A O 1 HETATM 4291 O O . HOH I 6 . ? 2.234 -1.401 32.856 1.00 34.56 ? 621 HOH A O 1 HETATM 4292 O O . HOH I 6 . ? 21.813 -1.140 -8.162 1.00 44.36 ? 622 HOH A O 1 HETATM 4293 O O . HOH I 6 . ? 16.333 11.051 47.859 1.00 40.96 ? 623 HOH A O 1 HETATM 4294 O O . HOH I 6 . ? 37.549 5.859 56.421 1.00 41.44 ? 624 HOH A O 1 HETATM 4295 O O . HOH I 6 . ? 8.045 1.460 51.093 1.00 44.21 ? 625 HOH A O 1 HETATM 4296 O O . HOH I 6 . ? 22.324 8.556 45.878 1.00 38.58 ? 626 HOH A O 1 HETATM 4297 O O . HOH I 6 . ? 25.956 0.001 61.800 1.00 43.10 ? 627 HOH A O 1 HETATM 4298 O O . HOH I 6 . ? 12.000 10.852 58.604 1.00 46.69 ? 628 HOH A O 1 HETATM 4299 O O . HOH I 6 . ? 23.725 3.691 5.322 1.00 44.67 ? 629 HOH A O 1 HETATM 4300 O O . HOH I 6 . ? 13.235 -1.695 55.911 1.00 40.00 ? 630 HOH A O 1 HETATM 4301 O O . HOH I 6 . ? 26.866 3.000 29.435 1.00 38.07 ? 631 HOH A O 1 HETATM 4302 O O . HOH I 6 . ? 15.923 -21.077 36.618 1.00 52.35 ? 632 HOH A O 1 HETATM 4303 O O . HOH I 6 . ? 10.799 8.422 50.975 1.00 39.10 ? 633 HOH A O 1 HETATM 4304 O O . HOH I 6 . ? 26.979 1.575 11.410 1.00 39.44 ? 634 HOH A O 1 HETATM 4305 O O . HOH I 6 . ? 22.620 5.717 11.961 1.00 41.23 ? 635 HOH A O 1 HETATM 4306 O O . HOH I 6 . ? 25.174 8.541 33.081 1.00 45.39 ? 636 HOH A O 1 HETATM 4307 O O . HOH I 6 . ? 31.821 -14.936 51.214 1.00 42.95 ? 637 HOH A O 1 HETATM 4308 O O . HOH I 6 . ? 28.708 -2.512 46.306 1.00 35.67 ? 638 HOH A O 1 HETATM 4309 O O . HOH I 6 . ? 5.559 0.487 38.257 1.00 46.03 ? 639 HOH A O 1 HETATM 4310 O O . HOH I 6 . ? 21.223 -10.342 32.078 1.00 43.23 ? 640 HOH A O 1 HETATM 4311 O O . HOH I 6 . ? 10.499 -4.094 66.157 1.00 34.27 ? 641 HOH A O 1 HETATM 4312 O O . HOH I 6 . ? 11.679 -29.287 46.181 1.00 51.12 ? 642 HOH A O 1 HETATM 4313 O O . HOH I 6 . ? 31.097 -11.126 68.186 1.00 54.47 ? 643 HOH A O 1 HETATM 4314 O O . HOH I 6 . ? 14.225 -18.478 32.811 1.00 50.61 ? 644 HOH A O 1 HETATM 4315 O O . HOH I 6 . ? 29.862 -18.563 53.808 1.00 48.51 ? 645 HOH A O 1 HETATM 4316 O O . HOH I 6 . ? 27.771 -26.619 51.253 1.00 54.03 ? 646 HOH A O 1 HETATM 4317 O O . HOH I 6 . ? 8.823 4.110 16.801 1.00 44.55 ? 647 HOH A O 1 HETATM 4318 O O . HOH I 6 . ? 12.424 8.842 57.199 1.00 48.48 ? 648 HOH A O 1 HETATM 4319 O O . HOH I 6 . ? 13.038 6.792 46.137 1.00 38.43 ? 649 HOH A O 1 HETATM 4320 O O . HOH I 6 . ? 1.792 -12.942 43.500 1.00 44.05 ? 650 HOH A O 1 HETATM 4321 O O . HOH I 6 . ? 11.803 3.595 57.273 1.00 58.75 ? 651 HOH A O 1 HETATM 4322 O O . HOH I 6 . ? 6.742 0.594 33.981 1.00 52.03 ? 652 HOH A O 1 HETATM 4323 O O . HOH I 6 . ? 21.596 -21.451 45.658 1.00 45.83 ? 653 HOH A O 1 HETATM 4324 O O . HOH I 6 . ? 29.486 2.801 47.567 1.00 40.37 ? 654 HOH A O 1 HETATM 4325 O O . HOH I 6 . ? 24.448 4.657 -9.255 1.00 56.85 ? 655 HOH A O 1 HETATM 4326 O O . HOH I 6 . ? 32.100 -14.885 41.878 1.00 38.20 ? 656 HOH A O 1 HETATM 4327 O O . HOH I 6 . ? 20.544 -17.285 29.324 1.00 54.28 ? 657 HOH A O 1 HETATM 4328 O O . HOH I 6 . ? 37.013 -5.965 67.989 1.00 44.31 ? 658 HOH A O 1 HETATM 4329 O O . HOH I 6 . ? 18.797 15.854 55.791 1.00 51.12 ? 659 HOH A O 1 HETATM 4330 O O . HOH I 6 . ? 35.800 -13.326 54.505 1.00 43.52 ? 660 HOH A O 1 HETATM 4331 O O . HOH I 6 . ? 1.817 -9.971 39.073 1.00 54.52 ? 661 HOH A O 1 HETATM 4332 O O . HOH I 6 . ? 34.599 -0.452 -13.622 1.00 47.44 ? 662 HOH A O 1 HETATM 4333 O O . HOH I 6 . ? 17.263 9.973 44.110 1.00 48.36 ? 663 HOH A O 1 HETATM 4334 O O . HOH I 6 . ? 4.602 -7.266 58.826 1.00 54.58 ? 664 HOH A O 1 HETATM 4335 O O . HOH I 6 . ? 9.731 7.328 47.864 1.00 41.08 ? 665 HOH A O 1 HETATM 4336 O O . HOH I 6 . ? 32.134 -10.332 46.795 1.00 44.00 ? 666 HOH A O 1 HETATM 4337 O O . HOH I 6 . ? 21.494 4.700 23.761 1.00 58.29 ? 667 HOH A O 1 HETATM 4338 O O . HOH I 6 . ? 30.263 -18.344 65.110 1.00 54.93 ? 668 HOH A O 1 HETATM 4339 O O . HOH I 6 . ? 23.897 -20.299 46.322 1.00 44.25 ? 669 HOH A O 1 HETATM 4340 O O . HOH I 6 . ? 20.093 -12.204 8.871 1.00 49.85 ? 670 HOH A O 1 HETATM 4341 O O . HOH I 6 . ? 3.710 -16.987 36.633 1.00 46.81 ? 671 HOH A O 1 HETATM 4342 O O . HOH I 6 . ? 24.583 6.070 51.180 1.00 47.51 ? 672 HOH A O 1 HETATM 4343 O O . HOH I 6 . ? 31.344 -1.563 -2.541 1.00 38.19 ? 673 HOH A O 1 HETATM 4344 O O . HOH I 6 . ? 16.736 -5.360 -45.506 1.00 63.61 ? 674 HOH A O 1 HETATM 4345 O O . HOH I 6 . ? 20.198 -2.846 0.125 1.00 44.75 ? 675 HOH A O 1 HETATM 4346 O O . HOH I 6 . ? 12.687 -16.733 66.150 1.00 56.71 ? 676 HOH A O 1 HETATM 4347 O O . HOH I 6 . ? 10.098 -1.088 55.063 1.00 53.67 ? 677 HOH A O 1 HETATM 4348 O O . HOH I 6 . ? 0.633 -8.814 37.528 1.00 58.03 ? 678 HOH A O 1 HETATM 4349 O O . HOH I 6 . ? 1.914 -2.520 37.411 1.00 53.42 ? 679 HOH A O 1 HETATM 4350 O O . HOH I 6 . ? 20.525 -12.173 74.169 1.00 55.61 ? 680 HOH A O 1 HETATM 4351 O O . HOH I 6 . ? 17.594 -3.027 69.072 1.00 40.27 ? 681 HOH A O 1 HETATM 4352 O O . HOH I 6 . ? 3.724 -11.650 34.829 1.00 40.99 ? 682 HOH A O 1 HETATM 4353 O O . HOH I 6 . ? 5.849 3.702 20.396 1.00 44.02 ? 683 HOH A O 1 HETATM 4354 O O . HOH I 6 . ? 6.815 5.872 41.178 1.00 45.38 ? 684 HOH A O 1 HETATM 4355 O O . HOH I 6 . ? 10.989 -24.990 37.993 1.00 47.61 ? 685 HOH A O 1 HETATM 4356 O O . HOH I 6 . ? 7.563 0.843 36.846 1.00 46.92 ? 686 HOH A O 1 HETATM 4357 O O . HOH I 6 . ? 28.722 0.977 29.555 1.00 43.72 ? 687 HOH A O 1 HETATM 4358 O O . HOH I 6 . ? 18.043 6.879 50.864 1.00 49.52 ? 688 HOH A O 1 HETATM 4359 O O . HOH I 6 . ? 10.895 -30.987 48.345 1.00 60.95 ? 689 HOH A O 1 HETATM 4360 O O . HOH I 6 . ? 32.867 -5.250 17.353 1.00 55.66 ? 690 HOH A O 1 HETATM 4361 O O . HOH I 6 . ? 28.018 1.692 15.087 1.00 44.03 ? 691 HOH A O 1 HETATM 4362 O O . HOH I 6 . ? 19.088 10.981 28.677 1.00 55.18 ? 692 HOH A O 1 HETATM 4363 O O . HOH I 6 . ? 1.084 -3.904 32.832 1.00 54.20 ? 693 HOH A O 1 HETATM 4364 O O . HOH I 6 . ? 2.466 -15.985 45.358 1.00 38.13 ? 694 HOH A O 1 HETATM 4365 O O . HOH I 6 . ? 14.093 6.596 35.054 1.00 63.78 ? 695 HOH A O 1 HETATM 4366 O O . HOH I 6 . ? 31.219 -8.510 41.739 1.00 48.29 ? 696 HOH A O 1 HETATM 4367 O O . HOH I 6 . ? 9.350 -6.937 66.318 1.00 54.79 ? 697 HOH A O 1 HETATM 4368 O O . HOH I 6 . ? 2.245 -1.098 35.367 1.00 38.26 ? 698 HOH A O 1 HETATM 4369 O O . HOH I 6 . ? 16.325 -6.660 1.069 1.00 48.62 ? 699 HOH A O 1 HETATM 4370 O O . HOH I 6 . ? 5.230 -34.249 50.297 1.00 62.79 ? 700 HOH A O 1 HETATM 4371 O O . HOH I 6 . ? 23.793 -18.316 44.768 1.00 43.35 ? 701 HOH A O 1 HETATM 4372 O O . HOH I 6 . ? 32.515 -13.833 54.830 1.00 51.79 ? 702 HOH A O 1 HETATM 4373 O O . HOH I 6 . ? 3.583 -4.679 28.482 1.00 43.44 ? 703 HOH A O 1 HETATM 4374 O O . HOH I 6 . ? 1.337 -9.299 51.302 1.00 45.62 ? 704 HOH A O 1 HETATM 4375 O O . HOH I 6 . ? 23.193 -7.101 26.552 1.00 48.47 ? 705 HOH A O 1 HETATM 4376 O O . HOH I 6 . ? 10.700 -1.670 13.794 1.00 51.21 ? 706 HOH A O 1 HETATM 4377 O O . HOH I 6 . ? 11.645 -15.485 24.495 1.00 56.09 ? 707 HOH A O 1 HETATM 4378 O O . HOH I 6 . ? 28.368 -5.383 45.455 1.00 47.15 ? 708 HOH A O 1 HETATM 4379 O O . HOH I 6 . ? 24.367 -10.229 32.751 1.00 42.50 ? 709 HOH A O 1 HETATM 4380 O O . HOH J 6 . ? 38.289 -6.684 45.689 1.00 55.00 ? 177 HOH B O 1 HETATM 4381 O O . HOH J 6 . ? 39.863 -9.836 31.634 1.00 36.04 ? 178 HOH B O 1 HETATM 4382 O O . HOH J 6 . ? 38.729 -15.788 -7.985 1.00 43.06 ? 179 HOH B O 1 HETATM 4383 O O . HOH J 6 . ? 23.845 -12.695 30.818 1.00 46.26 ? 181 HOH B O 1 HETATM 4384 O O . HOH J 6 . ? 39.172 -16.686 38.987 1.00 27.90 ? 182 HOH B O 1 HETATM 4385 O O . HOH J 6 . ? 26.949 -10.362 17.975 1.00 51.15 ? 183 HOH B O 1 HETATM 4386 O O . HOH J 6 . ? 31.385 -10.181 -34.705 1.00 31.32 ? 184 HOH B O 1 HETATM 4387 O O . HOH J 6 . ? 28.108 -17.236 -38.315 1.00 29.00 ? 185 HOH B O 1 HETATM 4388 O O . HOH J 6 . ? 26.824 -3.976 -26.147 1.00 35.55 ? 187 HOH B O 1 HETATM 4389 O O . HOH J 6 . ? 35.348 -10.207 -21.237 1.00 31.39 ? 188 HOH B O 1 HETATM 4390 O O . HOH J 6 . ? 34.446 -17.926 38.250 1.00 28.25 ? 189 HOH B O 1 HETATM 4391 O O . HOH J 6 . ? 32.076 -3.878 -30.165 1.00 33.45 ? 190 HOH B O 1 HETATM 4392 O O . HOH J 6 . ? 37.137 -18.137 37.217 1.00 24.67 ? 191 HOH B O 1 HETATM 4393 O O . HOH J 6 . ? 37.304 -8.866 -11.421 1.00 34.34 ? 192 HOH B O 1 HETATM 4394 O O . HOH J 6 . ? 22.239 -18.059 -17.838 1.00 33.47 ? 193 HOH B O 1 HETATM 4395 O O . HOH J 6 . ? 22.467 -21.906 -32.510 1.00 49.41 ? 194 HOH B O 1 HETATM 4396 O O . HOH J 6 . ? 33.405 -8.183 0.591 1.00 41.19 ? 195 HOH B O 1 HETATM 4397 O O . HOH J 6 . ? 22.892 -3.463 -36.144 1.00 50.51 ? 196 HOH B O 1 HETATM 4398 O O . HOH J 6 . ? 41.758 -12.211 42.182 1.00 41.43 ? 197 HOH B O 1 HETATM 4399 O O . HOH J 6 . ? 38.799 -15.884 15.154 1.00 42.72 ? 198 HOH B O 1 HETATM 4400 O O . HOH J 6 . ? 39.764 -9.155 28.478 1.00 41.91 ? 199 HOH B O 1 HETATM 4401 O O . HOH J 6 . ? 27.475 -23.889 -36.504 1.00 45.15 ? 200 HOH B O 1 HETATM 4402 O O . HOH J 6 . ? 30.539 -2.409 -28.396 1.00 41.49 ? 201 HOH B O 1 HETATM 4403 O O . HOH J 6 . ? 39.606 -13.355 19.704 1.00 42.26 ? 202 HOH B O 1 HETATM 4404 O O . HOH J 6 . ? 18.319 -19.132 -50.762 1.00 47.17 ? 203 HOH B O 1 HETATM 4405 O O . HOH J 6 . ? 31.059 -19.500 -22.492 1.00 36.56 ? 204 HOH B O 1 HETATM 4406 O O . HOH J 6 . ? 32.040 -7.601 33.323 1.00 42.54 ? 205 HOH B O 1 HETATM 4407 O O . HOH J 6 . ? 23.209 -16.716 -22.683 1.00 37.21 ? 206 HOH B O 1 HETATM 4408 O O . HOH J 6 . ? 33.935 -10.715 28.217 1.00 40.31 ? 208 HOH B O 1 HETATM 4409 O O . HOH J 6 . ? 27.819 -3.538 -28.739 1.00 39.93 ? 209 HOH B O 1 HETATM 4410 O O . HOH J 6 . ? 38.054 -10.290 -25.556 1.00 41.05 ? 210 HOH B O 1 HETATM 4411 O O . HOH J 6 . ? 26.165 -21.013 -27.179 1.00 46.58 ? 211 HOH B O 1 HETATM 4412 O O . HOH J 6 . ? 30.952 -17.472 -13.065 1.00 35.63 ? 212 HOH B O 1 HETATM 4413 O O . HOH J 6 . ? 34.660 -13.826 42.186 1.00 38.61 ? 213 HOH B O 1 HETATM 4414 O O . HOH J 6 . ? 26.554 -18.872 -18.299 1.00 31.09 ? 214 HOH B O 1 HETATM 4415 O O . HOH J 6 . ? 29.213 -20.583 -26.196 1.00 38.11 ? 215 HOH B O 1 HETATM 4416 O O . HOH J 6 . ? 16.650 -17.225 -49.813 1.00 43.64 ? 216 HOH B O 1 HETATM 4417 O O . HOH J 6 . ? 29.622 -3.323 -37.129 1.00 57.38 ? 219 HOH B O 1 HETATM 4418 O O . HOH J 6 . ? 36.208 -5.518 -30.692 1.00 50.64 ? 221 HOH B O 1 HETATM 4419 O O . HOH J 6 . ? 34.414 -18.672 40.845 1.00 45.97 ? 224 HOH B O 1 HETATM 4420 O O . HOH J 6 . ? 13.160 -7.396 -35.435 1.00 55.50 ? 227 HOH B O 1 HETATM 4421 O O . HOH J 6 . ? 19.609 -17.766 -33.557 1.00 42.56 ? 235 HOH B O 1 HETATM 4422 O O . HOH J 6 . ? 16.763 -5.579 -32.393 1.00 44.66 ? 237 HOH B O 1 HETATM 4423 O O . HOH J 6 . ? 14.250 -4.564 -44.021 1.00 55.15 ? 239 HOH B O 1 HETATM 4424 O O . HOH J 6 . ? 29.342 -10.956 16.996 1.00 46.89 ? 246 HOH B O 1 HETATM 4425 O O . HOH J 6 . ? 14.045 -8.598 -21.055 1.00 65.92 ? 248 HOH B O 1 HETATM 4426 O O . HOH J 6 . ? 13.926 -2.723 -38.835 1.00 51.00 ? 249 HOH B O 1 HETATM 4427 O O . HOH J 6 . ? 15.876 0.979 -30.170 1.00 57.66 ? 256 HOH B O 1 HETATM 4428 O O . HOH J 6 . ? 22.591 -23.738 -52.013 1.00 54.18 ? 257 HOH B O 1 HETATM 4429 O O . HOH J 6 . ? 33.049 -14.645 -40.998 1.00 49.50 ? 266 HOH B O 1 HETATM 4430 O O . HOH J 6 . ? 36.792 -15.816 41.732 1.00 41.65 ? 268 HOH B O 1 HETATM 4431 O O . HOH J 6 . ? 34.753 -7.762 -18.605 1.00 40.85 ? 271 HOH B O 1 HETATM 4432 O O . HOH J 6 . ? 32.531 -20.665 -23.724 1.00 50.33 ? 272 HOH B O 1 HETATM 4433 O O . HOH J 6 . ? 21.640 -23.144 -38.737 1.00 54.25 ? 273 HOH B O 1 HETATM 4434 O O . HOH J 6 . ? 14.554 -10.139 -28.778 1.00 55.28 ? 275 HOH B O 1 HETATM 4435 O O . HOH J 6 . ? 34.189 -11.124 -16.875 1.00 43.28 ? 276 HOH B O 1 HETATM 4436 O O . HOH J 6 . ? 29.464 -22.557 -37.603 1.00 54.10 ? 277 HOH B O 1 HETATM 4437 O O . HOH J 6 . ? 22.493 2.211 -26.519 1.00 50.59 ? 278 HOH B O 1 HETATM 4438 O O . HOH J 6 . ? 24.521 -18.904 -21.021 1.00 38.49 ? 279 HOH B O 1 HETATM 4439 O O . HOH J 6 . ? 30.529 -17.887 -38.546 1.00 48.61 ? 280 HOH B O 1 HETATM 4440 O O . HOH J 6 . ? 38.441 -19.513 3.193 1.00 44.48 ? 283 HOH B O 1 HETATM 4441 O O . HOH J 6 . ? 27.114 -21.732 -48.726 1.00 71.53 ? 284 HOH B O 1 HETATM 4442 O O . HOH J 6 . ? 39.830 -13.169 16.720 1.00 49.57 ? 287 HOH B O 1 HETATM 4443 O O . HOH J 6 . ? 22.520 -13.072 21.819 1.00 65.15 ? 294 HOH B O 1 HETATM 4444 O O . HOH J 6 . ? 41.921 -7.628 40.823 1.00 52.10 ? 299 HOH B O 1 HETATM 4445 O O . HOH J 6 . ? 33.525 -18.133 -13.856 1.00 38.79 ? 300 HOH B O 1 HETATM 4446 O O . HOH J 6 . ? 29.302 -16.297 26.046 1.00 38.73 ? 301 HOH B O 1 HETATM 4447 O O . HOH J 6 . ? 12.905 -8.789 -30.443 1.00 57.79 ? 309 HOH B O 1 HETATM 4448 O O . HOH J 6 . ? 21.434 -16.598 -19.860 1.00 45.41 ? 310 HOH B O 1 HETATM 4449 O O . HOH J 6 . ? 37.073 -8.943 11.827 1.00 50.77 ? 312 HOH B O 1 HETATM 4450 O O . HOH J 6 . ? 23.418 -9.327 22.747 1.00 53.46 ? 314 HOH B O 1 HETATM 4451 O O . HOH J 6 . ? 34.195 -6.815 40.821 1.00 46.13 ? 318 HOH B O 1 HETATM 4452 O O . HOH J 6 . ? 18.870 -23.158 -39.176 1.00 53.15 ? 320 HOH B O 1 HETATM 4453 O O . HOH J 6 . ? 15.080 2.818 -37.724 1.00 67.86 ? 322 HOH B O 1 HETATM 4454 O O . HOH J 6 . ? 37.811 -11.183 10.222 1.00 53.46 ? 328 HOH B O 1 HETATM 4455 O O . HOH J 6 . ? 25.296 -20.065 -47.651 1.00 56.52 ? 332 HOH B O 1 HETATM 4456 O O . HOH J 6 . ? 21.657 -8.375 -46.243 1.00 52.79 ? 333 HOH B O 1 HETATM 4457 O O . HOH J 6 . ? 34.124 -2.842 -31.400 1.00 47.39 ? 335 HOH B O 1 HETATM 4458 O O . HOH J 6 . ? 27.923 1.079 -32.409 1.00 63.99 ? 340 HOH B O 1 HETATM 4459 O O . HOH J 6 . ? 18.397 -21.664 -49.744 1.00 59.00 ? 341 HOH B O 1 HETATM 4460 O O . HOH J 6 . ? 25.770 -9.820 -52.589 1.00 54.18 ? 342 HOH B O 1 HETATM 4461 O O . HOH J 6 . ? 35.247 -10.692 -12.887 1.00 48.72 ? 345 HOH B O 1 HETATM 4462 O O . HOH J 6 . ? 35.453 -12.102 44.407 1.00 44.29 ? 346 HOH B O 1 HETATM 4463 O O . HOH J 6 . ? 29.608 -10.809 26.822 1.00 61.10 ? 351 HOH B O 1 HETATM 4464 O O . HOH J 6 . ? 24.555 0.561 -31.984 1.00 56.73 ? 355 HOH B O 1 HETATM 4465 O O . HOH J 6 . ? 38.582 -12.127 -15.289 1.00 58.54 ? 356 HOH B O 1 HETATM 4466 O O . HOH J 6 . ? 33.880 -16.543 -33.247 1.00 51.84 ? 357 HOH B O 1 HETATM 4467 O O . HOH J 6 . ? 40.273 -10.963 21.194 1.00 57.43 ? 358 HOH B O 1 HETATM 4468 O O . HOH J 6 . ? 34.739 -6.908 33.837 1.00 67.54 ? 360 HOH B O 1 HETATM 4469 O O . HOH J 6 . ? 31.507 -19.939 -37.028 1.00 65.64 ? 363 HOH B O 1 HETATM 4470 O O . HOH J 6 . ? 28.543 -6.928 37.622 1.00 52.26 ? 365 HOH B O 1 HETATM 4471 O O . HOH J 6 . ? 21.133 -18.809 -59.644 1.00 43.75 ? 366 HOH B O 1 HETATM 4472 O O . HOH J 6 . ? 36.026 -2.395 -24.020 1.00 55.18 ? 367 HOH B O 1 HETATM 4473 O O . HOH J 6 . ? 30.275 -8.411 22.501 1.00 63.81 ? 368 HOH B O 1 HETATM 4474 O O . HOH J 6 . ? 11.670 -5.428 -35.235 1.00 61.69 ? 372 HOH B O 1 HETATM 4475 O O . HOH J 6 . ? 34.383 -18.898 4.358 1.00 50.56 ? 373 HOH B O 1 HETATM 4476 O O . HOH J 6 . ? 36.287 -5.773 7.821 1.00 52.08 ? 385 HOH B O 1 HETATM 4477 O O . HOH J 6 . ? 24.915 -11.400 15.597 1.00 53.97 ? 390 HOH B O 1 HETATM 4478 O O . HOH J 6 . ? 25.080 -7.363 30.720 1.00 58.70 ? 391 HOH B O 1 HETATM 4479 O O . HOH J 6 . ? 16.103 -13.038 -48.111 1.00 60.00 ? 394 HOH B O 1 HETATM 4480 O O . HOH J 6 . ? 27.953 -16.163 -57.029 1.00 53.58 ? 396 HOH B O 1 HETATM 4481 O O . HOH J 6 . ? 37.400 -3.939 -25.512 1.00 48.05 ? 397 HOH B O 1 HETATM 4482 O O . HOH J 6 . ? 35.475 -6.988 1.385 1.00 43.58 ? 406 HOH B O 1 HETATM 4483 O O . HOH J 6 . ? 28.286 -17.776 -10.205 1.00 42.06 ? 409 HOH B O 1 HETATM 4484 O O . HOH J 6 . ? 18.608 -17.579 -28.389 1.00 70.11 ? 410 HOH B O 1 HETATM 4485 O O . HOH J 6 . ? 19.789 1.763 -20.170 1.00 48.42 ? 416 HOH B O 1 HETATM 4486 O O . HOH J 6 . ? 26.045 -21.970 -29.690 1.00 44.65 ? 422 HOH B O 1 HETATM 4487 O O . HOH J 6 . ? 19.528 -17.416 -30.664 1.00 49.01 ? 426 HOH B O 1 HETATM 4488 O O . HOH J 6 . ? 21.223 -19.723 -14.229 1.00 58.10 ? 429 HOH B O 1 HETATM 4489 O O . HOH J 6 . ? 17.184 -19.074 -53.410 1.00 50.80 ? 431 HOH B O 1 HETATM 4490 O O . HOH J 6 . ? 22.028 -15.658 21.335 1.00 72.80 ? 432 HOH B O 1 HETATM 4491 O O . HOH J 6 . ? 28.482 -23.889 -42.611 1.00 64.09 ? 434 HOH B O 1 HETATM 4492 O O . HOH J 6 . ? 37.758 -13.620 -13.221 1.00 29.72 ? 435 HOH B O 1 HETATM 4493 O O . HOH J 6 . ? 35.231 -20.365 -14.639 0.33 45.11 ? 436 HOH B O 1 HETATM 4494 O O . HOH J 6 . ? 31.897 -10.320 23.944 1.00 46.50 ? 437 HOH B O 1 HETATM 4495 O O . HOH J 6 . ? 14.192 -2.641 -32.651 1.00 70.05 ? 446 HOH B O 1 HETATM 4496 O O . HOH J 6 . ? 15.795 -18.454 -8.638 1.00 59.95 ? 449 HOH B O 1 HETATM 4497 O O . HOH J 6 . ? 18.121 2.117 -18.326 1.00 54.14 ? 457 HOH B O 1 HETATM 4498 O O . HOH J 6 . ? 36.947 -5.814 -17.918 1.00 53.91 ? 464 HOH B O 1 HETATM 4499 O O . HOH J 6 . ? 21.213 -22.562 6.318 1.00 62.19 ? 468 HOH B O 1 HETATM 4500 O O . HOH J 6 . ? 11.850 -12.923 -31.917 1.00 55.91 ? 473 HOH B O 1 HETATM 4501 O O . HOH J 6 . ? 33.110 -1.955 -35.002 1.00 79.33 ? 474 HOH B O 1 HETATM 4502 O O . HOH J 6 . ? 34.858 -16.437 -12.090 1.00 36.68 ? 477 HOH B O 1 HETATM 4503 O O . HOH J 6 . ? 15.459 -15.950 -26.540 1.00 66.89 ? 481 HOH B O 1 HETATM 4504 O O . HOH J 6 . ? 14.884 -11.140 -7.447 1.00 54.35 ? 483 HOH B O 1 HETATM 4505 O O . HOH J 6 . ? 21.422 -22.672 -3.671 1.00 42.99 ? 487 HOH B O 1 HETATM 4506 O O . HOH J 6 . ? 8.837 -7.854 -42.070 1.00 64.16 ? 490 HOH B O 1 HETATM 4507 O O . HOH J 6 . ? 28.239 -0.773 -35.550 1.00 63.20 ? 495 HOH B O 1 HETATM 4508 O O . HOH J 6 . ? 38.305 -6.902 -29.409 1.00 46.07 ? 496 HOH B O 1 HETATM 4509 O O . HOH J 6 . ? 30.645 -5.148 -46.989 1.00 61.14 ? 497 HOH B O 1 HETATM 4510 O O . HOH J 6 . ? 31.460 -20.862 -46.640 1.00 57.29 ? 498 HOH B O 1 HETATM 4511 O O . HOH J 6 . ? 27.231 -25.371 -45.598 1.00 70.38 ? 499 HOH B O 1 HETATM 4512 O O . HOH J 6 . ? 23.597 -21.603 -23.603 1.00 47.11 ? 500 HOH B O 1 HETATM 4513 O O . HOH J 6 . ? 34.224 -18.376 0.656 1.00 53.58 ? 504 HOH B O 1 HETATM 4514 O O . HOH J 6 . ? 38.914 -7.936 -27.108 1.00 47.00 ? 505 HOH B O 1 HETATM 4515 O O . HOH J 6 . ? 21.306 -23.643 -1.204 1.00 58.48 ? 511 HOH B O 1 HETATM 4516 O O . HOH J 6 . ? 23.956 -8.210 -48.606 1.00 70.04 ? 513 HOH B O 1 HETATM 4517 O O . HOH J 6 . ? 20.568 -21.468 -56.074 1.00 65.69 ? 521 HOH B O 1 HETATM 4518 O O . HOH J 6 . ? 31.362 -18.544 -41.034 1.00 65.89 ? 527 HOH B O 1 HETATM 4519 O O . HOH J 6 . ? 14.014 -11.117 -16.170 1.00 68.45 ? 528 HOH B O 1 HETATM 4520 O O . HOH J 6 . ? 19.964 -25.403 -48.258 1.00 60.04 ? 529 HOH B O 1 HETATM 4521 O O . HOH J 6 . ? 33.183 -16.897 -30.035 1.00 63.39 ? 530 HOH B O 1 HETATM 4522 O O . HOH J 6 . ? 14.535 -12.880 -27.723 1.00 56.94 ? 532 HOH B O 1 HETATM 4523 O O . HOH J 6 . ? 32.849 -20.835 -28.734 1.00 65.72 ? 535 HOH B O 1 HETATM 4524 O O . HOH J 6 . ? 22.024 -17.819 -24.864 1.00 54.96 ? 536 HOH B O 1 HETATM 4525 O O . HOH J 6 . ? 23.208 -10.881 24.428 1.00 53.53 ? 538 HOH B O 1 HETATM 4526 O O . HOH J 6 . ? 37.943 -9.788 -14.920 1.00 54.25 ? 539 HOH B O 1 HETATM 4527 O O . HOH J 6 . ? 14.718 -17.529 -40.784 1.00 56.61 ? 540 HOH B O 1 HETATM 4528 O O . HOH J 6 . ? 19.064 -17.145 -25.772 1.00 52.05 ? 544 HOH B O 1 HETATM 4529 O O . HOH J 6 . ? 35.095 -20.290 -6.865 0.33 25.84 ? 545 HOH B O 1 HETATM 4530 O O . HOH J 6 . ? 36.325 -16.370 -6.888 1.00 52.29 ? 546 HOH B O 1 HETATM 4531 O O . HOH J 6 . ? 33.144 -20.025 -5.421 1.00 51.30 ? 547 HOH B O 1 HETATM 4532 O O . HOH J 6 . ? 35.143 -20.300 -23.444 0.33 52.60 ? 549 HOH B O 1 HETATM 4533 O O . HOH J 6 . ? 22.312 -20.147 -16.661 1.00 52.39 ? 550 HOH B O 1 HETATM 4534 O O . HOH J 6 . ? 34.533 -21.166 -33.434 0.33 37.91 ? 551 HOH B O 1 HETATM 4535 O O . HOH J 6 . ? 29.218 -19.166 -12.165 1.00 50.57 ? 552 HOH B O 1 HETATM 4536 O O . HOH J 6 . ? 32.034 -8.973 20.793 1.00 51.75 ? 604 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 . PRO A 1 ? 1.0619 0.6837 0.6434 0.2204 0.0394 -0.0535 9 PRO A N 2 C CA . PRO A 1 ? 1.0387 0.6754 0.6381 0.2149 0.0379 -0.0529 9 PRO A CA 3 C C . PRO A 1 ? 1.0259 0.6676 0.6291 0.2092 0.0291 -0.0567 9 PRO A C 4 O O . PRO A 1 ? 1.0217 0.6705 0.6289 0.2073 0.0243 -0.0579 9 PRO A O 5 C CB . PRO A 1 ? 1.0373 0.6799 0.6408 0.2164 0.0398 -0.0508 9 PRO A CB 6 C CG . PRO A 1 ? 1.0520 0.6839 0.6433 0.2230 0.0462 -0.0485 9 PRO A CG 7 C CD . PRO A 1 ? 1.0669 0.6857 0.6442 0.2258 0.0459 -0.0503 9 PRO A CD 8 N N . GLY A 2 ? 1.0126 0.6506 0.6144 0.2066 0.0274 -0.0585 10 GLY A N 9 C CA . GLY A 2 ? 0.9829 0.6236 0.5861 0.2010 0.0192 -0.0622 10 GLY A CA 10 C C . GLY A 2 ? 0.9424 0.5988 0.5624 0.1952 0.0154 -0.0624 10 GLY A C 11 O O . GLY A 2 ? 0.9289 0.5949 0.5607 0.1950 0.0189 -0.0597 10 GLY A O 12 N N . ASP A 3 ? 0.9168 0.5757 0.5374 0.1901 0.0080 -0.0657 11 ASP A N 13 C CA . ASP A 3 ? 0.8755 0.5488 0.5113 0.1844 0.0040 -0.0662 11 ASP A CA 14 C C . ASP A 3 ? 0.8479 0.5252 0.4945 0.1818 0.0080 -0.0645 11 ASP A C 15 O O . ASP A 3 ? 0.8414 0.5093 0.4816 0.1838 0.0120 -0.0640 11 ASP A O 16 C CB . ASP A 3 ? 0.8808 0.5552 0.5136 0.1795 -0.0048 -0.0700 11 ASP A CB 17 C CG . ASP A 3 ? 0.8900 0.5614 0.5120 0.1818 -0.0096 -0.0717 11 ASP A CG 18 O OD1 . ASP A 3 ? 0.8763 0.5522 0.5002 0.1852 -0.0083 -0.0701 11 ASP A OD1 19 O OD2 . ASP A 3 ? 0.9248 0.5889 0.5359 0.1801 -0.0149 -0.0747 11 ASP A OD2 20 N N . GLN A 4 ? 0.8202 0.5110 0.4824 0.1777 0.0071 -0.0637 12 GLN A N 21 C CA . GLN A 4 ? 0.8006 0.4965 0.4740 0.1751 0.0107 -0.0621 12 GLN A CA 22 C C . GLN A 4 ? 0.7737 0.4801 0.4588 0.1684 0.0055 -0.0636 12 GLN A C 23 O O . GLN A 4 ? 0.7602 0.4753 0.4506 0.1660 0.0007 -0.0647 12 GLN A O 24 C CB . GLN A 4 ? 0.7954 0.4975 0.4778 0.1775 0.0175 -0.0581 12 GLN A CB 25 C CG . GLN A 4 ? 0.8393 0.5320 0.5137 0.1831 0.0249 -0.0556 12 GLN A CG 26 C CD . GLN A 4 ? 0.8732 0.5730 0.5570 0.1846 0.0312 -0.0516 12 GLN A CD 27 O OE1 . GLN A 4 ? 0.8409 0.5519 0.5384 0.1808 0.0312 -0.0505 12 GLN A OE1 28 N NE2 . GLN A 4 ? 0.8876 0.5806 0.5635 0.1899 0.0367 -0.0494 12 GLN A NE2 29 N N . ILE A 5 ? 0.7497 0.4553 0.4385 0.1656 0.0067 -0.0637 13 ILE A N 30 C CA . ILE A 5 ? 0.7252 0.4423 0.4281 0.1597 0.0039 -0.0641 13 ILE A CA 31 C C . ILE A 5 ? 0.7067 0.4282 0.4199 0.1598 0.0103 -0.0609 13 ILE A C 32 O O . ILE A 5 ? 0.6964 0.4097 0.4040 0.1630 0.0153 -0.0596 13 ILE A O 33 C CB . ILE A 5 ? 0.7235 0.4378 0.4227 0.1546 -0.0023 -0.0675 13 ILE A CB 34 C CG1 . ILE A 5 ? 0.7177 0.4462 0.4311 0.1485 -0.0069 -0.0682 13 ILE A CG1 35 C CG2 . ILE A 5 ? 0.7346 0.4379 0.4270 0.1550 0.0006 -0.0676 13 ILE A CG2 36 C CD1 . ILE A 5 ? 0.7178 0.4452 0.4289 0.1426 -0.0134 -0.0714 13 ILE A CD1 37 N N . CYS A 6 ? 0.6973 0.4318 0.4251 0.1566 0.0101 -0.0597 14 CYS A N 38 C CA . CYS A 6 ? 0.6895 0.4300 0.4283 0.1563 0.0156 -0.0566 14 CYS A CA 39 C C . CYS A 6 ? 0.6623 0.4115 0.4127 0.1503 0.0126 -0.0575 14 CYS A C 40 O O . CYS A 6 ? 0.6405 0.3960 0.3951 0.1466 0.0069 -0.0595 14 CYS A O 41 C CB . CYS A 6 ? 0.6973 0.4447 0.4426 0.1582 0.0192 -0.0538 14 CYS A CB 42 S SG . CYS A 6 ? 0.7921 0.5296 0.5241 0.1653 0.0232 -0.0525 14 CYS A SG 43 N N . ILE A 7 ? 0.6400 0.3894 0.3952 0.1498 0.0165 -0.0558 15 ILE A N 44 C CA . ILE A 7 ? 0.6313 0.3890 0.3982 0.1445 0.0146 -0.0561 15 ILE A CA 45 C C . ILE A 7 ? 0.6121 0.3807 0.3922 0.1440 0.0185 -0.0530 15 ILE A C 46 O O . ILE A 7 ? 0.6176 0.3849 0.3973 0.1476 0.0243 -0.0501 15 ILE A O 47 C CB . ILE A 7 ? 0.6311 0.3818 0.3945 0.1443 0.0165 -0.0563 15 ILE A CB 48 C CG1 . ILE A 7 ? 0.6750 0.4119 0.4224 0.1456 0.0138 -0.0591 15 ILE A CG1 49 C CG2 . ILE A 7 ? 0.6261 0.3850 0.4010 0.1386 0.0144 -0.0567 15 ILE A CG2 50 C CD1 . ILE A 7 ? 0.7141 0.4513 0.4579 0.1419 0.0063 -0.0626 15 ILE A CD1 51 N N . GLY A 8 ? 0.6062 0.3855 0.3975 0.1394 0.0153 -0.0534 16 GLY A N 52 C CA . GLY A 8 ? 0.5951 0.3842 0.3984 0.1385 0.0186 -0.0506 16 GLY A CA 53 C C . GLY A 8 ? 0.5910 0.3903 0.4065 0.1330 0.0154 -0.0512 16 GLY A C 54 O O . GLY A 8 ? 0.5961 0.3951 0.4113 0.1298 0.0109 -0.0537 16 GLY A O 55 N N . TYR A 9 ? 0.5801 0.3882 0.4060 0.1319 0.0177 -0.0489 17 TYR A N 56 C CA . TYR A 9 ? 0.5718 0.3897 0.4098 0.1271 0.0158 -0.0489 17 TYR A CA 57 C C . TYR A 9 ? 0.5743 0.4004 0.4194 0.1261 0.0155 -0.0479 17 TYR A C 58 O O . TYR A 9 ? 0.5884 0.4133 0.4310 0.1290 0.0186 -0.0461 17 TYR A O 59 C CB . TYR A 9 ? 0.5606 0.3802 0.4049 0.1260 0.0199 -0.0468 17 TYR A CB 60 C CG . TYR A 9 ? 0.5372 0.3557 0.3812 0.1294 0.0263 -0.0434 17 TYR A CG 61 C CD1 . TYR A 9 ? 0.5368 0.3628 0.3891 0.1284 0.0291 -0.0408 17 TYR A CD1 62 C CD2 . TYR A 9 ? 0.5415 0.3512 0.3765 0.1335 0.0298 -0.0426 17 TYR A CD2 63 C CE1 . TYR A 9 ? 0.5257 0.3511 0.3778 0.1310 0.0350 -0.0375 17 TYR A CE1 64 C CE2 . TYR A 9 ? 0.5587 0.3682 0.3937 0.1366 0.0358 -0.0392 17 TYR A CE2 65 C CZ . TYR A 9 ? 0.5643 0.3822 0.4082 0.1351 0.0383 -0.0366 17 TYR A CZ 66 O OH . TYR A 9 ? 0.6133 0.4315 0.4573 0.1376 0.0442 -0.0331 17 TYR A OH 67 N N . HIS A 10 ? 0.5736 0.4076 0.4269 0.1220 0.0117 -0.0490 18 HIS A N 68 C CA . HIS A 10 ? 0.5873 0.4296 0.4480 0.1206 0.0108 -0.0482 18 HIS A CA 69 C C . HIS A 10 ? 0.5862 0.4314 0.4526 0.1208 0.0161 -0.0450 18 HIS A C 70 O O . HIS A 10 ? 0.5897 0.4351 0.4598 0.1201 0.0196 -0.0432 18 HIS A O 71 C CB . HIS A 10 ? 0.5766 0.4266 0.4458 0.1159 0.0066 -0.0497 18 HIS A CB 72 C CG . HIS A 10 ? 0.5795 0.4379 0.4558 0.1145 0.0051 -0.0492 18 HIS A CG 73 N ND1 . HIS A 10 ? 0.5919 0.4519 0.4648 0.1161 0.0018 -0.0503 18 HIS A ND1 74 C CD2 . HIS A 10 ? 0.5815 0.4472 0.4678 0.1117 0.0063 -0.0477 18 HIS A CD2 75 C CE1 . HIS A 10 ? 0.6093 0.4768 0.4895 0.1148 0.0014 -0.0494 18 HIS A CE1 76 N NE2 . HIS A 10 ? 0.5827 0.4535 0.4710 0.1120 0.0040 -0.0480 18 HIS A NE2 77 N N . ALA A 11 ? 0.5941 0.4413 0.4605 0.1220 0.0166 -0.0440 19 ALA A N 78 C CA . ALA A 11 ? 0.6009 0.4518 0.4732 0.1212 0.0207 -0.0411 19 ALA A CA 79 C C . ALA A 11 ? 0.6010 0.4565 0.4758 0.1205 0.0181 -0.0416 19 ALA A C 80 O O . ALA A 11 ? 0.6100 0.4640 0.4793 0.1225 0.0146 -0.0434 19 ALA A O 81 C CB . ALA A 11 ? 0.6048 0.4494 0.4705 0.1246 0.0257 -0.0389 19 ALA A CB 82 N N . ASN A 12 ? 0.5983 0.4594 0.4810 0.1178 0.0196 -0.0399 20 ASN A N 83 C CA . ASN A 12 ? 0.6030 0.4681 0.4877 0.1175 0.0177 -0.0401 20 ASN A CA 84 C C . ASN A 12 ? 0.6116 0.4773 0.4993 0.1163 0.0220 -0.0372 20 ASN A C 85 O O . ASN A 12 ? 0.6101 0.4727 0.4965 0.1165 0.0263 -0.0352 20 ASN A O 86 C CB . ASN A 12 ? 0.5962 0.4689 0.4886 0.1143 0.0133 -0.0418 20 ASN A CB 87 C CG . ASN A 12 ? 0.5880 0.4651 0.4895 0.1101 0.0144 -0.0410 20 ASN A CG 88 O OD1 . ASN A 12 ? 0.5340 0.4099 0.4372 0.1095 0.0186 -0.0389 20 ASN A OD1 89 N ND2 . ASN A 12 ? 0.5997 0.4823 0.5069 0.1073 0.0106 -0.0427 20 ASN A ND2 90 N N . ASN A 13 ? 0.6175 0.4871 0.5086 0.1151 0.0209 -0.0370 21 ASN A N 91 C CA . ASN A 13 ? 0.6362 0.5059 0.5296 0.1134 0.0245 -0.0344 21 ASN A CA 92 C C . ASN A 13 ? 0.6334 0.5096 0.5373 0.1085 0.0252 -0.0334 21 ASN A C 93 O O . ASN A 13 ? 0.6289 0.5061 0.5352 0.1063 0.0274 -0.0316 21 ASN A O 94 C CB . ASN A 13 ? 0.6526 0.5209 0.5418 0.1153 0.0236 -0.0344 21 ASN A CB 95 C CG . ASN A 13 ? 0.6847 0.5590 0.5776 0.1152 0.0188 -0.0365 21 ASN A CG 96 O OD1 . ASN A 13 ? 0.7493 0.6295 0.6495 0.1125 0.0164 -0.0376 21 ASN A OD1 97 N ND2 . ASN A 13 ? 0.7240 0.5969 0.6118 0.1183 0.0175 -0.0367 21 ASN A ND2 98 N N . SER A 14 ? 0.6253 0.5055 0.5346 0.1067 0.0232 -0.0347 22 SER A N 99 C CA . SER A 14 ? 0.6133 0.4999 0.5325 0.1023 0.0234 -0.0339 22 SER A CA 100 C C . SER A 14 ? 0.6119 0.4982 0.5333 0.1005 0.0282 -0.0309 22 SER A C 101 O O . SER A 14 ? 0.6141 0.4964 0.5313 0.1023 0.0312 -0.0297 22 SER A O 102 C CB . SER A 14 ? 0.6104 0.4997 0.5335 0.1011 0.0209 -0.0356 22 SER A CB 103 O OG . SER A 14 ? 0.6023 0.4969 0.5342 0.0973 0.0218 -0.0346 22 SER A OG 104 N N . THR A 15 ? 0.6045 0.4952 0.5324 0.0968 0.0290 -0.0295 23 THR A N 105 C CA . THR A 15 ? 0.6006 0.4930 0.5323 0.0941 0.0330 -0.0266 23 THR A CA 106 C C . THR A 15 ? 0.5905 0.4898 0.5320 0.0903 0.0323 -0.0263 23 THR A C 107 O O . THR A 15 ? 0.5850 0.4876 0.5313 0.0873 0.0349 -0.0239 23 THR A O 108 C CB . THR A 15 ? 0.6040 0.4945 0.5336 0.0925 0.0352 -0.0247 23 THR A CB 109 O OG1 . THR A 15 ? 0.5918 0.4844 0.5237 0.0912 0.0325 -0.0259 23 THR A OG1 110 C CG2 . THR A 15 ? 0.6135 0.4963 0.5328 0.0961 0.0370 -0.0243 23 THR A CG2 111 N N . GLU A 16 ? 0.5869 0.4886 0.5311 0.0905 0.0286 -0.0288 24 GLU A N 112 C CA . GLU A 16 ? 0.5814 0.4888 0.5339 0.0875 0.0276 -0.0289 24 GLU A CA 113 C C . GLU A 16 ? 0.5698 0.4775 0.5238 0.0876 0.0309 -0.0270 24 GLU A C 114 O O . GLU A 16 ? 0.5716 0.4747 0.5198 0.0908 0.0320 -0.0272 24 GLU A O 115 C CB . GLU A 16 ? 0.5894 0.4977 0.5424 0.0880 0.0233 -0.0319 24 GLU A CB 116 C CG . GLU A 16 ? 0.6315 0.5409 0.5835 0.0884 0.0199 -0.0337 24 GLU A CG 117 C CD . GLU A 16 ? 0.6866 0.6003 0.6442 0.0854 0.0201 -0.0326 24 GLU A CD 118 O OE1 . GLU A 16 ? 0.7009 0.6198 0.6658 0.0824 0.0188 -0.0328 24 GLU A OE1 119 O OE2 . GLU A 16 ? 0.7253 0.6366 0.6793 0.0861 0.0216 -0.0315 24 GLU A OE2 120 N N . LYS A 17 ? 0.5482 0.4613 0.5096 0.0843 0.0326 -0.0250 25 LYS A N 121 C CA . LYS A 17 ? 0.5386 0.4536 0.5024 0.0843 0.0359 -0.0226 25 LYS A CA 122 C C . LYS A 17 ? 0.5148 0.4336 0.4846 0.0830 0.0345 -0.0232 25 LYS A C 123 O O . LYS A 17 ? 0.5024 0.4247 0.4773 0.0803 0.0318 -0.0245 25 LYS A O 124 C CB . LYS A 17 ? 0.5433 0.4621 0.5109 0.0812 0.0391 -0.0193 25 LYS A CB 125 C CG . LYS A 17 ? 0.5658 0.4803 0.5270 0.0820 0.0410 -0.0182 25 LYS A CG 126 C CD . LYS A 17 ? 0.6017 0.5120 0.5568 0.0859 0.0438 -0.0173 25 LYS A CD 127 C CE . LYS A 17 ? 0.6403 0.5479 0.5908 0.0856 0.0470 -0.0150 25 LYS A CE 128 N NZ . LYS A 17 ? 0.6782 0.5850 0.6261 0.0884 0.0508 -0.0128 25 LYS A NZ 129 N N . VAL A 18 ? 0.4945 0.4124 0.4633 0.0852 0.0366 -0.0223 26 VAL A N 130 C CA . VAL A 18 ? 0.4724 0.3934 0.4464 0.0842 0.0361 -0.0223 26 VAL A CA 131 C C . VAL A 18 ? 0.4701 0.3938 0.4460 0.0854 0.0405 -0.0189 26 VAL A C 132 O O . VAL A 18 ? 0.4727 0.3946 0.4446 0.0876 0.0436 -0.0171 26 VAL A O 133 C CB . VAL A 18 ? 0.4752 0.3910 0.4447 0.0863 0.0334 -0.0254 26 VAL A CB 134 C CG1 . VAL A 18 ? 0.4646 0.3793 0.4329 0.0850 0.0288 -0.0286 26 VAL A CG1 135 C CG2 . VAL A 18 ? 0.4651 0.3739 0.4259 0.0910 0.0355 -0.0253 26 VAL A CG2 136 N N . ASP A 19 ? 0.4591 0.3874 0.4410 0.0841 0.0408 -0.0180 27 ASP A N 137 C CA . ASP A 19 ? 0.4588 0.3898 0.4422 0.0861 0.0448 -0.0148 27 ASP A CA 138 C C . ASP A 19 ? 0.4563 0.3824 0.4357 0.0896 0.0446 -0.0161 27 ASP A C 139 O O . ASP A 19 ? 0.4566 0.3795 0.4351 0.0887 0.0411 -0.0192 27 ASP A O 140 C CB . ASP A 19 ? 0.4515 0.3918 0.4444 0.0825 0.0458 -0.0121 27 ASP A CB 141 C CG . ASP A 19 ? 0.4816 0.4260 0.4777 0.0787 0.0462 -0.0106 27 ASP A CG 142 O OD1 . ASP A 19 ? 0.4646 0.4057 0.4557 0.0795 0.0473 -0.0103 27 ASP A OD1 143 O OD2 . ASP A 19 ? 0.5164 0.4669 0.5195 0.0747 0.0453 -0.0098 27 ASP A OD2 144 N N . THR A 20 ? 0.4493 0.3746 0.4260 0.0934 0.0485 -0.0137 28 THR A N 145 C CA . THR A 20 ? 0.4652 0.3851 0.4371 0.0972 0.0491 -0.0144 28 THR A CA 146 C C . THR A 20 ? 0.4722 0.3987 0.4489 0.0987 0.0533 -0.0103 28 THR A C 147 O O . THR A 20 ? 0.4763 0.4113 0.4598 0.0963 0.0550 -0.0073 28 THR A O 148 C CB . THR A 20 ? 0.4747 0.3852 0.4357 0.1018 0.0502 -0.0155 28 THR A CB 149 O OG1 . THR A 20 ? 0.4553 0.3685 0.4156 0.1040 0.0545 -0.0121 28 THR A OG1 150 C CG2 . THR A 20 ? 0.4545 0.3596 0.4109 0.1004 0.0460 -0.0193 28 THR A CG2 151 N N . ILE A 21 ? 0.4806 0.4029 0.4531 0.1029 0.0550 -0.0099 29 ILE A N 152 C CA . ILE A 21 ? 0.4873 0.4157 0.4635 0.1054 0.0592 -0.0058 29 ILE A CA 153 C C . ILE A 21 ? 0.5008 0.4325 0.4759 0.1082 0.0637 -0.0022 29 ILE A C 154 O O . ILE A 21 ? 0.4942 0.4361 0.4765 0.1073 0.0665 0.0017 29 ILE A O 155 C CB . ILE A 21 ? 0.4959 0.4176 0.4664 0.1098 0.0600 -0.0064 29 ILE A CB 156 C CG1 . ILE A 21 ? 0.4946 0.4142 0.4673 0.1065 0.0559 -0.0094 29 ILE A CG1 157 C CG2 . ILE A 21 ? 0.4971 0.4247 0.4700 0.1139 0.0650 -0.0017 29 ILE A CG2 158 C CD1 . ILE A 21 ? 0.4984 0.4283 0.4817 0.1033 0.0559 -0.0072 29 ILE A CD1 159 N N . LEU A 22 ? 0.5041 0.4276 0.4700 0.1115 0.0644 -0.0034 30 LEU A N 160 C CA . LEU A 22 ? 0.5210 0.4461 0.4843 0.1149 0.0690 -0.0001 30 LEU A CA 161 C C . LEU A 22 ? 0.5176 0.4475 0.4841 0.1111 0.0691 0.0008 30 LEU A C 162 O O . LEU A 22 ? 0.5112 0.4459 0.4785 0.1124 0.0731 0.0045 30 LEU A O 163 C CB . LEU A 22 ? 0.5319 0.4450 0.4828 0.1206 0.0700 -0.0018 30 LEU A CB 164 C CG . LEU A 22 ? 0.5556 0.4641 0.5003 0.1272 0.0735 -0.0003 30 LEU A CG 165 C CD1 . LEU A 22 ? 0.5650 0.4797 0.5157 0.1280 0.0750 0.0020 30 LEU A CD1 166 C CD2 . LEU A 22 ? 0.5816 0.4754 0.5141 0.1301 0.0712 -0.0045 30 LEU A CD2 167 N N . GLU A 23 ? 0.5169 0.4452 0.4848 0.1066 0.0648 -0.0022 31 GLU A N 168 C CA . GLU A 23 ? 0.5356 0.4651 0.5037 0.1036 0.0646 -0.0020 31 GLU A CA 169 C C . GLU A 23 ? 0.5326 0.4647 0.5061 0.0978 0.0603 -0.0041 31 GLU A C 170 O O . GLU A 23 ? 0.5385 0.4665 0.5112 0.0970 0.0564 -0.0077 31 GLU A O 171 C CB . GLU A 23 ? 0.5468 0.4661 0.5042 0.1071 0.0644 -0.0042 31 GLU A CB 172 C CG . GLU A 23 ? 0.5594 0.4784 0.5153 0.1049 0.0646 -0.0039 31 GLU A CG 173 C CD . GLU A 23 ? 0.5888 0.4975 0.5336 0.1088 0.0645 -0.0059 31 GLU A CD 174 O OE1 . GLU A 23 ? 0.5884 0.4900 0.5265 0.1131 0.0642 -0.0077 31 GLU A OE1 175 O OE2 . GLU A 23 ? 0.6175 0.5249 0.5600 0.1076 0.0647 -0.0057 31 GLU A OE2 176 N N . ARG A 24 ? 0.5388 0.4772 0.5173 0.0938 0.0612 -0.0019 32 ARG A N 177 C CA . ARG A 24 ? 0.5435 0.4837 0.5262 0.0885 0.0577 -0.0037 32 ARG A CA 178 C C . ARG A 24 ? 0.5480 0.4821 0.5246 0.0880 0.0564 -0.0055 32 ARG A C 179 O O . ARG A 24 ? 0.5594 0.4903 0.5304 0.0905 0.0591 -0.0043 32 ARG A O 180 C CB . ARG A 24 ? 0.5389 0.4894 0.5306 0.0839 0.0590 -0.0003 32 ARG A CB 181 C CG . ARG A 24 ? 0.5758 0.5328 0.5739 0.0843 0.0598 0.0013 32 ARG A CG 182 C CD . ARG A 24 ? 0.6537 0.6214 0.6605 0.0797 0.0610 0.0048 32 ARG A CD 183 N NE . ARG A 24 ? 0.7108 0.6854 0.7229 0.0814 0.0629 0.0074 32 ARG A NE 184 C CZ . ARG A 24 ? 0.7386 0.7235 0.7589 0.0779 0.0637 0.0105 32 ARG A CZ 185 N NH1 . ARG A 24 ? 0.7442 0.7330 0.7681 0.0721 0.0626 0.0112 32 ARG A NH1 186 N NH2 . ARG A 24 ? 0.7376 0.7286 0.7620 0.0804 0.0655 0.0130 32 ARG A NH2 187 N N . ASN A 25 ? 0.5436 0.4762 0.5211 0.0851 0.0526 -0.0083 33 ASN A N 188 C CA . ASN A 25 ? 0.5603 0.4881 0.5327 0.0843 0.0515 -0.0096 33 ASN A CA 189 C C . ASN A 25 ? 0.5517 0.4706 0.5144 0.0891 0.0511 -0.0118 33 ASN A C 190 O O . ASN A 25 ? 0.5547 0.4699 0.5118 0.0904 0.0530 -0.0109 33 ASN A O 191 C CB . ASN A 25 ? 0.5753 0.5067 0.5490 0.0815 0.0548 -0.0060 33 ASN A CB 192 C CG . ASN A 25 ? 0.6497 0.5767 0.6193 0.0795 0.0535 -0.0071 33 ASN A CG 193 O OD1 . ASN A 25 ? 0.6705 0.5953 0.6399 0.0786 0.0499 -0.0099 33 ASN A OD1 194 N ND2 . ASN A 25 ? 0.7651 0.6910 0.7312 0.0789 0.0566 -0.0046 33 ASN A ND2 195 N N . VAL A 26 ? 0.5314 0.4467 0.4919 0.0915 0.0486 -0.0146 34 VAL A N 196 C CA . VAL A 26 ? 0.5187 0.4256 0.4698 0.0959 0.0479 -0.0167 34 VAL A CA 197 C C . VAL A 26 ? 0.5116 0.4150 0.4597 0.0951 0.0437 -0.0200 34 VAL A C 198 O O . VAL A 26 ? 0.5075 0.4136 0.4601 0.0925 0.0403 -0.0218 34 VAL A O 199 C CB . VAL A 26 ? 0.5214 0.4252 0.4702 0.0989 0.0474 -0.0181 34 VAL A CB 200 C CG1 . VAL A 26 ? 0.5178 0.4123 0.4561 0.1031 0.0465 -0.0203 34 VAL A CG1 201 C CG2 . VAL A 26 ? 0.5012 0.4092 0.4534 0.1002 0.0516 -0.0146 34 VAL A CG2 202 N N . THR A 27 ? 0.5017 0.3994 0.4421 0.0975 0.0441 -0.0205 35 THR A N 203 C CA . THR A 27 ? 0.4909 0.3851 0.4275 0.0977 0.0402 -0.0235 35 THR A CA 204 C C . THR A 27 ? 0.4894 0.3790 0.4211 0.1004 0.0371 -0.0266 35 THR A C 205 O O . THR A 27 ? 0.4960 0.3804 0.4215 0.1038 0.0387 -0.0266 35 THR A O 206 C CB . THR A 27 ? 0.5011 0.3908 0.4308 0.0994 0.0417 -0.0228 35 THR A CB 207 O OG1 . THR A 27 ? 0.5128 0.4061 0.4461 0.0966 0.0450 -0.0197 35 THR A OG1 208 C CG2 . THR A 27 ? 0.4849 0.3723 0.4115 0.0996 0.0378 -0.0255 35 THR A CG2 209 N N . VAL A 28 ? 0.4751 0.3664 0.4092 0.0986 0.0327 -0.0292 36 VAL A N 210 C CA . VAL A 28 ? 0.4782 0.3657 0.4081 0.1000 0.0292 -0.0323 36 VAL A CA 211 C C . VAL A 28 ? 0.4787 0.3655 0.4057 0.1001 0.0251 -0.0347 36 VAL A C 212 O O . VAL A 28 ? 0.4763 0.3666 0.4064 0.0986 0.0246 -0.0342 36 VAL A O 213 C CB . VAL A 28 ? 0.4614 0.3525 0.3976 0.0973 0.0274 -0.0331 36 VAL A CB 214 C CG1 . VAL A 28 ? 0.4498 0.3409 0.3875 0.0981 0.0314 -0.0308 36 VAL A CG1 215 C CG2 . VAL A 28 ? 0.4731 0.3718 0.4184 0.0930 0.0254 -0.0332 36 VAL A CG2 216 N N . THR A 29 ? 0.4949 0.3772 0.4156 0.1020 0.0221 -0.0373 37 THR A N 217 C CA . THR A 29 ? 0.4917 0.3738 0.4089 0.1028 0.0181 -0.0395 37 THR A CA 218 C C . THR A 29 ? 0.4938 0.3828 0.4183 0.0993 0.0143 -0.0408 37 THR A C 219 O O . THR A 29 ? 0.4794 0.3709 0.4039 0.0996 0.0121 -0.0414 37 THR A O 220 C CB . THR A 29 ? 0.4991 0.3747 0.4072 0.1055 0.0157 -0.0418 37 THR A CB 221 O OG1 . THR A 29 ? 0.4979 0.3731 0.4073 0.1035 0.0136 -0.0434 37 THR A OG1 222 C CG2 . THR A 29 ? 0.4958 0.3639 0.3958 0.1094 0.0197 -0.0404 37 THR A CG2 223 N N . HIS A 30 ? 0.4910 0.3829 0.4212 0.0963 0.0135 -0.0412 38 HIS A N 224 C CA . HIS A 30 ? 0.4928 0.3919 0.4309 0.0926 0.0102 -0.0422 38 HIS A CA 225 C C . HIS A 30 ? 0.4862 0.3885 0.4318 0.0896 0.0122 -0.0408 38 HIS A C 226 O O . HIS A 30 ? 0.4688 0.3676 0.4127 0.0904 0.0145 -0.0401 38 HIS A O 227 C CB . HIS A 30 ? 0.4992 0.3982 0.4349 0.0917 0.0052 -0.0452 38 HIS A CB 228 C CG . HIS A 30 ? 0.5232 0.4190 0.4510 0.0948 0.0030 -0.0466 38 HIS A CG 229 N ND1 . HIS A 30 ? 0.5638 0.4518 0.4823 0.0977 0.0035 -0.0473 38 HIS A ND1 230 C CD2 . HIS A 30 ? 0.5165 0.4160 0.4439 0.0956 0.0002 -0.0473 38 HIS A CD2 231 C CE1 . HIS A 30 ? 0.5570 0.4440 0.4699 0.1000 0.0010 -0.0485 38 HIS A CE1 232 N NE2 . HIS A 30 ? 0.5520 0.4462 0.4703 0.0989 -0.0009 -0.0484 38 HIS A NE2 233 N N . ALA A 31 ? 0.4930 0.4021 0.4465 0.0866 0.0112 -0.0404 39 ALA A N 234 C CA . ALA A 31 ? 0.4945 0.4075 0.4556 0.0837 0.0130 -0.0390 39 ALA A CA 235 C C . ALA A 31 ? 0.4996 0.4191 0.4677 0.0802 0.0097 -0.0401 39 ALA A C 236 O O . ALA A 31 ? 0.4955 0.4173 0.4632 0.0804 0.0071 -0.0411 39 ALA A O 237 C CB . ALA A 31 ? 0.4862 0.4005 0.4496 0.0838 0.0170 -0.0360 39 ALA A CB 238 N N . LYS A 32 ? 0.4973 0.4198 0.4714 0.0774 0.0099 -0.0397 40 LYS A N 239 C CA . LYS A 32 ? 0.5039 0.4326 0.4850 0.0740 0.0072 -0.0404 40 LYS A CA 240 C C . LYS A 32 ? 0.4928 0.4256 0.4811 0.0717 0.0098 -0.0382 40 LYS A C 241 O O . LYS A 32 ? 0.4931 0.4251 0.4831 0.0712 0.0117 -0.0372 40 LYS A O 242 C CB . LYS A 32 ? 0.5080 0.4360 0.4887 0.0722 0.0041 -0.0426 40 LYS A CB 243 C CG . LYS A 32 ? 0.5514 0.4858 0.5395 0.0684 0.0017 -0.0432 40 LYS A CG 244 C CD . LYS A 32 ? 0.5953 0.5350 0.5853 0.0681 -0.0010 -0.0440 40 LYS A CD 245 C CE . LYS A 32 ? 0.6145 0.5605 0.6112 0.0644 -0.0036 -0.0448 40 LYS A CE 246 N NZ . LYS A 32 ? 0.6418 0.5937 0.6415 0.0648 -0.0048 -0.0445 40 LYS A NZ 247 N N . ASP A 33 ? 0.4881 0.4249 0.4799 0.0707 0.0100 -0.0372 41 ASP A N 248 C CA . ASP A 33 ? 0.4828 0.4239 0.4815 0.0680 0.0117 -0.0353 41 ASP A CA 249 C C . ASP A 33 ? 0.4693 0.4147 0.4738 0.0650 0.0092 -0.0365 41 ASP A C 250 O O . ASP A 33 ? 0.4627 0.4107 0.4681 0.0644 0.0061 -0.0381 41 ASP A O 251 C CB . ASP A 33 ? 0.4955 0.4383 0.4946 0.0679 0.0121 -0.0344 41 ASP A CB 252 C CG . ASP A 33 ? 0.5188 0.4651 0.5236 0.0651 0.0143 -0.0322 41 ASP A CG 253 O OD1 . ASP A 33 ? 0.5320 0.4809 0.5419 0.0629 0.0149 -0.0315 41 ASP A OD1 254 O OD2 . ASP A 33 ? 0.5588 0.5046 0.5623 0.0650 0.0154 -0.0312 41 ASP A OD2 255 N N . ILE A 34 ? 0.4496 0.3960 0.4581 0.0634 0.0106 -0.0355 42 ILE A N 256 C CA . ILE A 34 ? 0.4455 0.3954 0.4592 0.0604 0.0084 -0.0365 42 ILE A CA 257 C C . ILE A 34 ? 0.4326 0.3879 0.4538 0.0576 0.0094 -0.0349 42 ILE A C 258 O O . ILE A 34 ? 0.4417 0.3997 0.4673 0.0551 0.0082 -0.0353 42 ILE A O 259 C CB . ILE A 34 ? 0.4440 0.3902 0.4557 0.0605 0.0083 -0.0373 42 ILE A CB 260 C CG1 . ILE A 34 ? 0.4229 0.3677 0.4352 0.0616 0.0122 -0.0349 42 ILE A CG1 261 C CG2 . ILE A 34 ? 0.4530 0.3936 0.4568 0.0627 0.0065 -0.0395 42 ILE A CG2 262 C CD1 . ILE A 34 ? 0.4190 0.3594 0.4285 0.0622 0.0125 -0.0355 42 ILE A CD1 263 N N . LEU A 35 ? 0.4278 0.3842 0.4496 0.0577 0.0114 -0.0331 43 LEU A N 264 C CA . LEU A 35 ? 0.4184 0.3791 0.4462 0.0549 0.0124 -0.0314 43 LEU A CA 265 C C . LEU A 35 ? 0.4149 0.3776 0.4432 0.0542 0.0113 -0.0315 43 LEU A C 266 O O . LEU A 35 ? 0.4202 0.3803 0.4441 0.0558 0.0124 -0.0309 43 LEU A O 267 C CB . LEU A 35 ? 0.4160 0.3764 0.4441 0.0550 0.0160 -0.0287 43 LEU A CB 268 C CG . LEU A 35 ? 0.4210 0.3858 0.4548 0.0519 0.0171 -0.0266 43 LEU A CG 269 C CD1 . LEU A 35 ? 0.4141 0.3824 0.4536 0.0499 0.0164 -0.0267 43 LEU A CD1 270 C CD2 . LEU A 35 ? 0.4027 0.3676 0.4358 0.0519 0.0205 -0.0238 43 LEU A CD2 271 N N . GLU A 36 ? 0.3976 0.3643 0.4307 0.0520 0.0095 -0.0321 44 GLU A N 272 C CA . GLU A 36 ? 0.3930 0.3615 0.4266 0.0516 0.0088 -0.0320 44 GLU A CA 273 C C . GLU A 36 ? 0.3853 0.3542 0.4208 0.0495 0.0112 -0.0297 44 GLU A C 274 O O . GLU A 36 ? 0.3737 0.3451 0.4139 0.0472 0.0120 -0.0286 44 GLU A O 275 C CB . GLU A 36 ? 0.3876 0.3606 0.4254 0.0501 0.0061 -0.0334 44 GLU A CB 276 C CG . GLU A 36 ? 0.4059 0.3807 0.4437 0.0503 0.0055 -0.0331 44 GLU A CG 277 C CD . GLU A 36 ? 0.4446 0.4161 0.4757 0.0538 0.0055 -0.0335 44 GLU A CD 278 O OE1 . GLU A 36 ? 0.4365 0.4088 0.4657 0.0557 0.0033 -0.0351 44 GLU A OE1 279 O OE2 . GLU A 36 ? 0.4728 0.4408 0.5003 0.0545 0.0075 -0.0322 44 GLU A OE2 280 N N . LYS A 37 ? 0.3883 0.3545 0.4195 0.0504 0.0124 -0.0289 45 LYS A N 281 C CA . LYS A 37 ? 0.3983 0.3640 0.4301 0.0481 0.0146 -0.0267 45 LYS A CA 282 C C . LYS A 37 ? 0.4057 0.3709 0.4363 0.0473 0.0140 -0.0266 45 LYS A C 283 O O . LYS A 37 ? 0.4132 0.3775 0.4436 0.0450 0.0155 -0.0250 45 LYS A O 284 C CB . LYS A 37 ? 0.4074 0.3689 0.4340 0.0492 0.0171 -0.0253 45 LYS A CB 285 C CG . LYS A 37 ? 0.4010 0.3623 0.4276 0.0507 0.0180 -0.0253 45 LYS A CG 286 C CD . LYS A 37 ? 0.4593 0.4162 0.4800 0.0526 0.0203 -0.0242 45 LYS A CD 287 C CE . LYS A 37 ? 0.5049 0.4576 0.5193 0.0565 0.0191 -0.0261 45 LYS A CE 288 N NZ . LYS A 37 ? 0.4630 0.4162 0.4779 0.0584 0.0171 -0.0282 45 LYS A NZ 289 N N . THR A 38 ? 0.4072 0.3733 0.4370 0.0493 0.0119 -0.0283 46 THR A N 290 C CA . THR A 38 ? 0.4240 0.3891 0.4515 0.0496 0.0116 -0.0282 46 THR A CA 291 C C . THR A 38 ? 0.4127 0.3830 0.4457 0.0485 0.0097 -0.0289 46 THR A C 292 O O . THR A 38 ? 0.4066 0.3812 0.4443 0.0482 0.0079 -0.0301 46 THR A O 293 C CB . THR A 38 ? 0.4238 0.3852 0.4443 0.0537 0.0112 -0.0290 46 THR A CB 294 O OG1 . THR A 38 ? 0.4587 0.4241 0.4811 0.0558 0.0086 -0.0308 46 THR A OG1 295 C CG2 . THR A 38 ? 0.4569 0.4131 0.4717 0.0551 0.0131 -0.0284 46 THR A CG2 296 N N . HIS A 39 ? 0.4050 0.3744 0.4369 0.0479 0.0101 -0.0282 47 HIS A N 297 C CA . HIS A 39 ? 0.3990 0.3730 0.4354 0.0471 0.0086 -0.0287 47 HIS A CA 298 C C . HIS A 39 ? 0.4082 0.3788 0.4390 0.0492 0.0092 -0.0283 47 HIS A C 299 O O . HIS A 39 ? 0.4231 0.3874 0.4470 0.0502 0.0109 -0.0275 47 HIS A O 300 C CB . HIS A 39 ? 0.3922 0.3685 0.4343 0.0429 0.0092 -0.0277 47 HIS A CB 301 C CG . HIS A 39 ? 0.4069 0.3788 0.4460 0.0406 0.0113 -0.0259 47 HIS A CG 302 N ND1 . HIS A 39 ? 0.4427 0.4116 0.4784 0.0401 0.0119 -0.0252 47 HIS A ND1 303 C CD2 . HIS A 39 ? 0.4236 0.3934 0.4619 0.0387 0.0130 -0.0245 47 HIS A CD2 304 C CE1 . HIS A 39 ? 0.4596 0.4246 0.4925 0.0374 0.0137 -0.0236 47 HIS A CE1 305 N NE2 . HIS A 39 ? 0.4248 0.3909 0.4597 0.0364 0.0144 -0.0230 47 HIS A NE2 306 N N . ASN A 40 ? 0.3916 0.3660 0.4248 0.0499 0.0080 -0.0286 48 ASN A N 307 C CA . ASN A 40 ? 0.3931 0.3639 0.4200 0.0528 0.0087 -0.0282 48 ASN A CA 308 C C . ASN A 40 ? 0.3933 0.3597 0.4178 0.0505 0.0104 -0.0268 48 ASN A C 309 O O . ASN A 40 ? 0.4061 0.3687 0.4248 0.0529 0.0111 -0.0264 48 ASN A O 310 C CB . ASN A 40 ? 0.3793 0.3564 0.4086 0.0558 0.0068 -0.0291 48 ASN A CB 311 C CG . ASN A 40 ? 0.3792 0.3624 0.4160 0.0531 0.0059 -0.0290 48 ASN A CG 312 O OD1 . ASN A 40 ? 0.3349 0.3171 0.3747 0.0492 0.0066 -0.0284 48 ASN A OD1 313 N ND2 . ASN A 40 ? 0.3620 0.3516 0.4018 0.0551 0.0043 -0.0295 48 ASN A ND2 314 N N . GLY A 41 ? 0.3914 0.3581 0.4198 0.0460 0.0109 -0.0261 49 GLY A N 315 C CA . GLY A 41 ? 0.3876 0.3503 0.4139 0.0430 0.0123 -0.0247 49 GLY A CA 316 C C . GLY A 41 ? 0.3879 0.3533 0.4166 0.0429 0.0117 -0.0247 49 GLY A C 317 O O . GLY A 41 ? 0.3930 0.3541 0.4185 0.0408 0.0127 -0.0237 49 GLY A O 318 N N . LYS A 42 ? 0.3646 0.3369 0.3985 0.0450 0.0100 -0.0258 50 LYS A N 319 C CA . LYS A 42 ? 0.3550 0.3305 0.3911 0.0454 0.0095 -0.0257 50 LYS A CA 320 C C . LYS A 42 ? 0.3327 0.3160 0.3784 0.0426 0.0081 -0.0261 50 LYS A C 321 O O . LYS A 42 ? 0.3163 0.3037 0.3668 0.0418 0.0069 -0.0270 50 LYS A O 322 C CB . LYS A 42 ? 0.3517 0.3295 0.3853 0.0507 0.0088 -0.0262 50 LYS A CB 323 C CG . LYS A 42 ? 0.3961 0.3658 0.4193 0.0544 0.0104 -0.0257 50 LYS A CG 324 C CD . LYS A 42 ? 0.4232 0.3968 0.4449 0.0600 0.0095 -0.0262 50 LYS A CD 325 C CE . LYS A 42 ? 0.4582 0.4233 0.4689 0.0642 0.0111 -0.0257 50 LYS A CE 326 N NZ . LYS A 42 ? 0.5281 0.4984 0.5382 0.0698 0.0101 -0.0260 50 LYS A NZ 327 N N . LEU A 43 ? 0.3224 0.3068 0.3700 0.0412 0.0082 -0.0256 51 LEU A N 328 C CA . LEU A 43 ? 0.3192 0.3111 0.3751 0.0395 0.0069 -0.0260 51 LEU A CA 329 C C . LEU A 43 ? 0.3097 0.3074 0.3670 0.0430 0.0058 -0.0266 51 LEU A C 330 O O . LEU A 43 ? 0.3162 0.3119 0.3686 0.0463 0.0066 -0.0260 51 LEU A O 331 C CB . LEU A 43 ? 0.3221 0.3125 0.3791 0.0362 0.0077 -0.0249 51 LEU A CB 332 C CG . LEU A 43 ? 0.3481 0.3334 0.4032 0.0327 0.0087 -0.0241 51 LEU A CG 333 C CD1 . LEU A 43 ? 0.3686 0.3516 0.4232 0.0297 0.0095 -0.0229 51 LEU A CD1 334 C CD2 . LEU A 43 ? 0.3885 0.3776 0.4496 0.0305 0.0080 -0.0244 51 LEU A CD2 335 N N . CYS A 44 ? 0.3071 0.3119 0.3709 0.0423 0.0040 -0.0275 52 CYS A N 336 C CA . CYS A 44 ? 0.3208 0.3322 0.3864 0.0453 0.0025 -0.0281 52 CYS A CA 337 C C . CYS A 44 ? 0.3142 0.3335 0.3876 0.0429 0.0011 -0.0284 52 CYS A C 338 O O . CYS A 44 ? 0.2784 0.2977 0.3560 0.0390 0.0011 -0.0285 52 CYS A O 339 C CB . CYS A 44 ? 0.3377 0.3497 0.4024 0.0465 0.0013 -0.0293 52 CYS A CB 340 S SG . CYS A 44 ? 0.3701 0.3733 0.4251 0.0499 0.0028 -0.0290 52 CYS A SG 341 N N . LYS A 45 ? 0.3102 0.3365 0.3856 0.0453 0.0000 -0.0285 53 LYS A N 342 C CA . LYS A 45 ? 0.3249 0.3596 0.4077 0.0428 -0.0016 -0.0290 53 LYS A CA 343 C C . LYS A 45 ? 0.3375 0.3725 0.4226 0.0402 -0.0033 -0.0304 53 LYS A C 344 O O . LYS A 45 ? 0.3353 0.3671 0.4164 0.0420 -0.0036 -0.0310 53 LYS A O 345 C CB . LYS A 45 ? 0.3333 0.3763 0.4174 0.0461 -0.0027 -0.0286 53 LYS A CB 346 C CG . LYS A 45 ? 0.3621 0.4053 0.4438 0.0493 -0.0009 -0.0271 53 LYS A CG 347 C CD . LYS A 45 ? 0.3974 0.4511 0.4818 0.0525 -0.0020 -0.0265 53 LYS A CD 348 C CE . LYS A 45 ? 0.4536 0.5069 0.5323 0.0579 -0.0022 -0.0264 53 LYS A CE 349 N NZ . LYS A 45 ? 0.4737 0.5179 0.5440 0.0617 0.0004 -0.0254 53 LYS A NZ 350 N N . LEU A 46 A 0.3465 0.3846 0.4372 0.0362 -0.0043 -0.0308 53 LEU A N 351 C CA . LEU A 46 A 0.3686 0.4065 0.4608 0.0337 -0.0058 -0.0322 53 LEU A CA 352 C C . LEU A 46 A 0.3834 0.4298 0.4799 0.0325 -0.0082 -0.0328 53 LEU A C 353 O O . LEU A 46 A 0.3687 0.4199 0.4699 0.0302 -0.0085 -0.0324 53 LEU A O 354 C CB . LEU A 46 A 0.3669 0.4006 0.4612 0.0300 -0.0050 -0.0321 53 LEU A CB 355 C CG . LEU A 46 A 0.3884 0.4193 0.4828 0.0277 -0.0058 -0.0333 53 LEU A CG 356 C CD1 . LEU A 46 A 0.4040 0.4297 0.4933 0.0301 -0.0053 -0.0336 53 LEU A CD1 357 C CD2 . LEU A 46 A 0.3986 0.4265 0.4954 0.0246 -0.0047 -0.0328 53 LEU A CD2 358 N N . ASN A 47 ? 0.3957 0.4441 0.4902 0.0341 -0.0100 -0.0337 54 ASN A N 359 C CA . ASN A 47 ? 0.4098 0.4671 0.5078 0.0331 -0.0126 -0.0343 54 ASN A CA 360 C C . ASN A 47 ? 0.3997 0.4651 0.5011 0.0345 -0.0125 -0.0329 54 ASN A C 361 O O . ASN A 47 ? 0.4166 0.4892 0.5232 0.0315 -0.0138 -0.0329 54 ASN A O 362 C CB . ASN A 47 ? 0.4210 0.4788 0.5225 0.0279 -0.0141 -0.0353 54 ASN A CB 363 C CG . ASN A 47 ? 0.4666 0.5164 0.5645 0.0268 -0.0141 -0.0365 54 ASN A CG 364 O OD1 . ASN A 47 ? 0.5279 0.5728 0.6265 0.0241 -0.0131 -0.0366 54 ASN A OD1 365 N ND2 . ASN A 47 ? 0.5316 0.5801 0.6254 0.0292 -0.0151 -0.0373 54 ASN A ND2 366 N N . GLY A 48 ? 0.3801 0.4443 0.4782 0.0390 -0.0107 -0.0318 55 GLY A N 367 C CA . GLY A 48 ? 0.3659 0.4370 0.4661 0.0413 -0.0101 -0.0302 55 GLY A CA 368 C C . GLY A 48 ? 0.3498 0.4199 0.4527 0.0394 -0.0082 -0.0292 55 GLY A C 369 O O . GLY A 48 ? 0.3385 0.4131 0.4421 0.0419 -0.0072 -0.0278 55 GLY A O 370 N N . ILE A 49 ? 0.3223 0.3864 0.4262 0.0354 -0.0076 -0.0298 56 ILE A N 371 C CA . ILE A 49 ? 0.3040 0.3671 0.4104 0.0334 -0.0061 -0.0289 56 ILE A CA 372 C C . ILE A 49 ? 0.2939 0.3475 0.3954 0.0345 -0.0037 -0.0284 56 ILE A C 373 O O . ILE A 49 ? 0.3026 0.3498 0.4019 0.0333 -0.0036 -0.0291 56 ILE A O 374 C CB . ILE A 49 ? 0.2977 0.3620 0.4092 0.0279 -0.0072 -0.0297 56 ILE A CB 375 C CG1 . ILE A 49 ? 0.3186 0.3922 0.4344 0.0260 -0.0096 -0.0302 56 ILE A CG1 376 C CG2 . ILE A 49 ? 0.2835 0.3465 0.3974 0.0258 -0.0055 -0.0287 56 ILE A CG2 377 C CD1 . ILE A 49 ? 0.3344 0.4075 0.4535 0.0205 -0.0109 -0.0312 56 ILE A CD1 378 N N . PRO A 50 ? 0.2916 0.3442 0.3911 0.0369 -0.0019 -0.0270 57 PRO A N 379 C CA . PRO A 50 ? 0.2771 0.3205 0.3710 0.0378 0.0001 -0.0264 57 PRO A CA 380 C C . PRO A 50 ? 0.2707 0.3102 0.3669 0.0334 0.0006 -0.0265 57 PRO A C 381 O O . PRO A 50 ? 0.2515 0.2956 0.3532 0.0306 0.0000 -0.0265 57 PRO A O 382 C CB . PRO A 50 ? 0.2902 0.3344 0.3814 0.0413 0.0017 -0.0250 57 PRO A CB 383 C CG . PRO A 50 ? 0.2821 0.3373 0.3778 0.0431 0.0004 -0.0247 57 PRO A CG 384 C CD . PRO A 50 ? 0.2795 0.3399 0.3815 0.0389 -0.0017 -0.0259 57 PRO A CD 385 N N . PRO A 51 ? 0.2563 0.2878 0.3483 0.0329 0.0018 -0.0263 58 PRO A N 386 C CA . PRO A 51 ? 0.2508 0.2790 0.3447 0.0291 0.0024 -0.0260 58 PRO A CA 387 C C . PRO A 51 ? 0.2476 0.2757 0.3412 0.0290 0.0036 -0.0248 58 PRO A C 388 O O . PRO A 51 ? 0.2566 0.2856 0.3473 0.0324 0.0043 -0.0242 58 PRO A O 389 C CB . PRO A 51 ? 0.2467 0.2672 0.3353 0.0290 0.0034 -0.0258 58 PRO A CB 390 C CG . PRO A 51 ? 0.2538 0.2716 0.3359 0.0333 0.0040 -0.0256 58 PRO A CG 391 C CD . PRO A 51 ? 0.2583 0.2837 0.3436 0.0355 0.0025 -0.0264 58 PRO A CD 392 N N . LEU A 52 ? 0.2351 0.2617 0.3313 0.0256 0.0039 -0.0244 59 LEU A N 393 C CA . LEU A 52 ? 0.2377 0.2623 0.3325 0.0252 0.0051 -0.0233 59 LEU A CA 394 C C . LEU A 52 ? 0.2440 0.2603 0.3323 0.0251 0.0063 -0.0227 59 LEU A C 395 O O . LEU A 52 ? 0.2297 0.2434 0.3185 0.0225 0.0061 -0.0227 59 LEU A O 396 C CB . LEU A 52 ? 0.2358 0.2627 0.3361 0.0215 0.0049 -0.0231 59 LEU A CB 397 C CG . LEU A 52 ? 0.2270 0.2508 0.3257 0.0204 0.0061 -0.0219 59 LEU A CG 398 C CD1 . LEU A 52 ? 0.2348 0.2598 0.3309 0.0236 0.0070 -0.0212 59 LEU A CD1 399 C CD2 . LEU A 52 ? 0.1964 0.2229 0.3009 0.0168 0.0056 -0.0218 59 LEU A CD2 400 N N . GLU A 53 ? 0.2410 0.2532 0.3229 0.0280 0.0074 -0.0221 60 GLU A N 401 C CA . GLU A 53 ? 0.2612 0.2648 0.3359 0.0275 0.0085 -0.0215 60 GLU A CA 402 C C . GLU A 53 ? 0.2646 0.2647 0.3377 0.0251 0.0093 -0.0205 60 GLU A C 403 O O . GLU A 53 ? 0.2631 0.2620 0.3332 0.0271 0.0102 -0.0199 60 GLU A O 404 C CB . GLU A 53 ? 0.2758 0.2751 0.3427 0.0319 0.0094 -0.0214 60 GLU A CB 405 C CG . GLU A 53 ? 0.3283 0.3177 0.3867 0.0309 0.0106 -0.0207 60 GLU A CG 406 C CD . GLU A 53 ? 0.3809 0.3648 0.4314 0.0344 0.0114 -0.0209 60 GLU A CD 407 O OE1 . GLU A 53 ? 0.3531 0.3413 0.4049 0.0380 0.0109 -0.0215 60 GLU A OE1 408 O OE2 . GLU A 53 ? 0.4014 0.3764 0.4440 0.0334 0.0124 -0.0202 60 GLU A OE2 409 N N . LEU A 54 ? 0.2554 0.2540 0.3305 0.0210 0.0089 -0.0201 61 LEU A N 410 C CA . LEU A 54 ? 0.2507 0.2464 0.3245 0.0184 0.0094 -0.0191 61 LEU A CA 411 C C . LEU A 54 ? 0.2644 0.2510 0.3284 0.0187 0.0105 -0.0184 61 LEU A C 412 O O . LEU A 54 ? 0.2623 0.2456 0.3234 0.0174 0.0110 -0.0176 61 LEU A O 413 C CB . LEU A 54 ? 0.2308 0.2285 0.3098 0.0143 0.0086 -0.0188 61 LEU A CB 414 C CG . LEU A 54 ? 0.2130 0.2180 0.3006 0.0135 0.0077 -0.0194 61 LEU A CG 415 C CD1 . LEU A 54 ? 0.2107 0.2163 0.3017 0.0099 0.0072 -0.0188 61 LEU A CD1 416 C CD2 . LEU A 54 ? 0.2225 0.2312 0.3130 0.0143 0.0078 -0.0194 61 LEU A CD2 417 N N . GLY A 55 ? 0.2628 0.2448 0.3210 0.0202 0.0109 -0.0186 62 GLY A N 418 C CA . GLY A 55 ? 0.2801 0.2521 0.3278 0.0201 0.0120 -0.0179 62 GLY A CA 419 C C . GLY A 55 ? 0.2870 0.2557 0.3338 0.0147 0.0117 -0.0170 62 GLY A C 420 O O . GLY A 55 ? 0.2856 0.2568 0.3364 0.0118 0.0109 -0.0168 62 GLY A O 421 N N . ASP A 56 ? 0.2997 0.2632 0.3415 0.0134 0.0121 -0.0163 63 ASP A N 422 C CA . ASP A 56 ? 0.3109 0.2717 0.3516 0.0081 0.0115 -0.0153 63 ASP A CA 423 C C . ASP A 56 ? 0.3053 0.2732 0.3547 0.0057 0.0106 -0.0149 63 ASP A C 424 O O . ASP A 56 ? 0.3051 0.2717 0.3541 0.0014 0.0099 -0.0140 63 ASP A O 425 C CB . ASP A 56 ? 0.3269 0.2769 0.3561 0.0071 0.0124 -0.0146 63 ASP A CB 426 C CG . ASP A 56 ? 0.3671 0.3085 0.3865 0.0079 0.0132 -0.0147 63 ASP A CG 427 O OD1 . ASP A 56 ? 0.3804 0.3229 0.4012 0.0060 0.0128 -0.0146 63 ASP A OD1 428 O OD2 . ASP A 56 ? 0.3981 0.3312 0.4079 0.0107 0.0145 -0.0147 63 ASP A OD2 429 N N . CYS A 57 ? 0.2977 0.2728 0.3544 0.0082 0.0104 -0.0156 64 CYS A N 430 C CA . CYS A 57 ? 0.2901 0.2712 0.3544 0.0064 0.0097 -0.0154 64 CYS A CA 431 C C . CYS A 57 ? 0.2686 0.2561 0.3410 0.0044 0.0087 -0.0154 64 CYS A C 432 O O . CYS A 57 ? 0.2727 0.2623 0.3468 0.0058 0.0086 -0.0161 64 CYS A O 433 C CB . CYS A 57 ? 0.3018 0.2871 0.3693 0.0098 0.0102 -0.0159 64 CYS A CB 434 S SG . CYS A 57 ? 0.3726 0.3501 0.4302 0.0124 0.0117 -0.0155 64 CYS A SG 435 N N . SER A 58 ? 0.2405 0.2308 0.3171 0.0015 0.0081 -0.0147 65 SER A N 436 C CA . SER A 58 ? 0.2310 0.2275 0.3152 0.0004 0.0074 -0.0146 65 SER A CA 437 C C . SER A 58 ? 0.2258 0.2274 0.3160 0.0021 0.0073 -0.0154 65 SER A C 438 O O . SER A 58 ? 0.2242 0.2254 0.3133 0.0036 0.0078 -0.0157 65 SER A O 439 C CB . SER A 58 ? 0.2338 0.2310 0.3194 -0.0033 0.0068 -0.0131 65 SER A CB 440 O OG . SER A 58 ? 0.2207 0.2181 0.3071 -0.0042 0.0067 -0.0127 65 SER A OG 441 N N . ILE A 59 ? 0.2135 0.2199 0.3097 0.0019 0.0068 -0.0157 66 ILE A N 442 C CA . ILE A 59 ? 0.2097 0.2206 0.3115 0.0025 0.0066 -0.0164 66 ILE A CA 443 C C . ILE A 59 ? 0.2026 0.2134 0.3051 0.0011 0.0068 -0.0156 66 ILE A C 444 O O . ILE A 59 ? 0.1989 0.2114 0.3027 0.0022 0.0071 -0.0160 66 ILE A O 445 C CB . ILE A 59 ? 0.2157 0.2299 0.3225 0.0019 0.0062 -0.0165 66 ILE A CB 446 C CG1 . ILE A 59 ? 0.2094 0.2236 0.3154 0.0037 0.0061 -0.0175 66 ILE A CG1 447 C CG2 . ILE A 59 ? 0.2183 0.2360 0.3301 0.0017 0.0060 -0.0170 66 ILE A CG2 448 C CD1 . ILE A 59 ? 0.2381 0.2543 0.3450 0.0059 0.0058 -0.0190 66 ILE A CD1 449 N N . ALA A 60 ? 0.1879 0.1972 0.2894 -0.0013 0.0066 -0.0143 67 ALA A N 450 C CA . ALA A 60 ? 0.1880 0.1966 0.2893 -0.0027 0.0066 -0.0134 67 ALA A CA 451 C C . ALA A 60 ? 0.1899 0.1945 0.2857 -0.0016 0.0073 -0.0135 67 ALA A C 452 O O . ALA A 60 ? 0.1944 0.1999 0.2914 -0.0011 0.0078 -0.0135 67 ALA A O 453 C CB . ALA A 60 ? 0.1886 0.1966 0.2894 -0.0058 0.0060 -0.0119 67 ALA A CB 454 N N . GLY A 61 ? 0.1983 0.1981 0.2878 -0.0011 0.0076 -0.0135 68 GLY A N 455 C CA . GLY A 61 ? 0.1985 0.1931 0.2813 0.0006 0.0085 -0.0136 68 GLY A CA 456 C C . GLY A 61 ? 0.2000 0.1981 0.2852 0.0040 0.0093 -0.0145 68 GLY A C 457 O O . GLY A 61 ? 0.2095 0.2067 0.2930 0.0053 0.0101 -0.0142 68 GLY A O 458 N N . TRP A 62 ? 0.1909 0.1931 0.2800 0.0056 0.0090 -0.0154 69 TRP A N 459 C CA . TRP A 62 ? 0.1903 0.1975 0.2830 0.0083 0.0093 -0.0161 69 TRP A CA 460 C C . TRP A 62 ? 0.1825 0.1941 0.2807 0.0071 0.0093 -0.0159 69 TRP A C 461 O O . TRP A 62 ? 0.2025 0.2155 0.3004 0.0088 0.0102 -0.0156 69 TRP A O 462 C CB . TRP A 62 ? 0.1875 0.1982 0.2834 0.0093 0.0086 -0.0172 69 TRP A CB 463 C CG . TRP A 62 ? 0.2013 0.2185 0.3023 0.0109 0.0084 -0.0180 69 TRP A CG 464 C CD1 . TRP A 62 ? 0.2206 0.2410 0.3221 0.0131 0.0091 -0.0178 69 TRP A CD1 465 C CD2 . TRP A 62 ? 0.1919 0.2136 0.2981 0.0103 0.0073 -0.0189 69 TRP A CD2 466 N NE1 . TRP A 62 ? 0.2005 0.2277 0.3076 0.0134 0.0083 -0.0186 69 TRP A NE1 467 C CE2 . TRP A 62 ? 0.1937 0.2212 0.3034 0.0116 0.0072 -0.0194 69 TRP A CE2 468 C CE3 . TRP A 62 ? 0.2038 0.2251 0.3117 0.0088 0.0066 -0.0194 69 TRP A CE3 469 C CZ2 . TRP A 62 ? 0.1689 0.2011 0.2832 0.0110 0.0061 -0.0204 69 TRP A CZ2 470 C CZ3 . TRP A 62 ? 0.1828 0.2082 0.2950 0.0087 0.0057 -0.0204 69 TRP A CZ3 471 C CH2 . TRP A 62 ? 0.1978 0.2283 0.3129 0.0096 0.0054 -0.0210 69 TRP A CH2 472 N N . LEU A 63 ? 0.1759 0.1899 0.2790 0.0045 0.0085 -0.0158 70 LEU A N 473 C CA . LEU A 63 ? 0.1835 0.2018 0.2920 0.0036 0.0085 -0.0158 70 LEU A CA 474 C C . LEU A 63 ? 0.1847 0.2008 0.2914 0.0026 0.0092 -0.0147 70 LEU A C 475 O O . LEU A 63 ? 0.1674 0.1862 0.2763 0.0030 0.0098 -0.0145 70 LEU A O 476 C CB . LEU A 63 ? 0.1857 0.2062 0.2990 0.0016 0.0076 -0.0161 70 LEU A CB 477 C CG . LEU A 63 ? 0.1938 0.2165 0.3088 0.0026 0.0070 -0.0173 70 LEU A CG 478 C CD1 . LEU A 63 ? 0.1833 0.2067 0.3016 0.0010 0.0064 -0.0174 70 LEU A CD1 479 C CD2 . LEU A 63 ? 0.1851 0.2123 0.3024 0.0042 0.0070 -0.0181 70 LEU A CD2 480 N N . LEU A 64 ? 0.1750 0.1860 0.2770 0.0013 0.0091 -0.0139 71 LEU A N 481 C CA . LEU A 64 ? 0.1804 0.1884 0.2796 0.0004 0.0096 -0.0129 71 LEU A CA 482 C C . LEU A 64 ? 0.2037 0.2088 0.2975 0.0032 0.0109 -0.0128 71 LEU A C 483 O O . LEU A 64 ? 0.1988 0.2031 0.2913 0.0035 0.0118 -0.0121 71 LEU A O 484 C CB . LEU A 64 ? 0.1906 0.1941 0.2860 -0.0021 0.0089 -0.0120 71 LEU A CB 485 C CG . LEU A 64 ? 0.1969 0.2036 0.2974 -0.0045 0.0079 -0.0116 71 LEU A CG 486 C CD1 . LEU A 64 ? 0.1741 0.1776 0.2709 -0.0068 0.0070 -0.0106 71 LEU A CD1 487 C CD2 . LEU A 64 ? 0.1998 0.2088 0.3041 -0.0053 0.0080 -0.0110 71 LEU A CD2 488 N N . GLY A 65 ? 0.1983 0.2019 0.2887 0.0055 0.0112 -0.0133 72 GLY A N 489 C CA . GLY A 65 ? 0.2204 0.2206 0.3044 0.0088 0.0126 -0.0131 72 GLY A CA 490 C C . GLY A 65 ? 0.2194 0.2105 0.2942 0.0081 0.0129 -0.0125 72 GLY A C 491 O O . GLY A 65 ? 0.2249 0.2118 0.2944 0.0092 0.0140 -0.0118 72 GLY A O 492 N N . ASN A 66 ? 0.2185 0.2061 0.2908 0.0059 0.0119 -0.0126 73 ASN A N 493 C CA . ASN A 66 ? 0.2306 0.2089 0.2931 0.0047 0.0120 -0.0122 73 ASN A CA 494 C C . ASN A 66 ? 0.2372 0.2108 0.2923 0.0092 0.0137 -0.0123 73 ASN A C 495 O O . ASN A 66 ? 0.2403 0.2173 0.2973 0.0124 0.0141 -0.0129 73 ASN A O 496 C CB . ASN A 66 ? 0.2142 0.1914 0.2763 0.0022 0.0108 -0.0123 73 ASN A CB 497 C CG . ASN A 66 ? 0.2440 0.2114 0.2955 0.0003 0.0107 -0.0118 73 ASN A CG 498 O OD1 . ASN A 66 ? 0.2649 0.2254 0.3081 0.0026 0.0119 -0.0118 73 ASN A OD1 499 N ND2 . ASN A 66 ? 0.2181 0.1850 0.2698 -0.0036 0.0094 -0.0114 73 ASN A ND2 500 N N . PRO A 67 ? 0.2544 0.2205 0.3010 0.0098 0.0147 -0.0116 74 PRO A N 501 C CA . PRO A 67 ? 0.2781 0.2403 0.3180 0.0149 0.0166 -0.0116 74 PRO A CA 502 C C . PRO A 67 ? 0.2967 0.2541 0.3305 0.0169 0.0170 -0.0121 74 PRO A C 503 O O . PRO A 67 ? 0.3185 0.2749 0.3485 0.0219 0.0185 -0.0120 74 PRO A O 504 C CB . PRO A 67 ? 0.2958 0.2487 0.3259 0.0145 0.0176 -0.0108 74 PRO A CB 505 C CG . PRO A 67 ? 0.2799 0.2364 0.3158 0.0105 0.0164 -0.0104 74 PRO A CG 506 C CD . PRO A 67 ? 0.2518 0.2139 0.2955 0.0067 0.0143 -0.0108 74 PRO A CD 507 N N . GLU A 68 ? 0.3081 0.2627 0.3407 0.0132 0.0156 -0.0124 75 GLU A N 508 C CA . GLU A 68 ? 0.3274 0.2776 0.3545 0.0149 0.0159 -0.0128 75 GLU A CA 509 C C . GLU A 68 ? 0.3205 0.2802 0.3564 0.0174 0.0156 -0.0136 75 GLU A C 510 O O . GLU A 68 ? 0.3179 0.2754 0.3502 0.0197 0.0160 -0.0140 75 GLU A O 511 C CB . GLU A 68 ? 0.3348 0.2796 0.3582 0.0098 0.0146 -0.0127 75 GLU A CB 512 C CG . GLU A 68 ? 0.3764 0.3114 0.3903 0.0064 0.0145 -0.0120 75 GLU A CG 513 C CD . GLU A 68 ? 0.4869 0.4095 0.4865 0.0093 0.0162 -0.0118 75 GLU A CD 514 O OE1 . GLU A 68 ? 0.4829 0.4035 0.4790 0.0136 0.0174 -0.0123 75 GLU A OE1 515 O OE2 . GLU A 68 ? 0.5407 0.4549 0.5319 0.0074 0.0164 -0.0113 75 GLU A OE2 516 N N . CYS A 69 ? 0.3054 0.2750 0.3519 0.0170 0.0150 -0.0138 76 CYS A N 517 C CA . CYS A 69 ? 0.3123 0.2909 0.3672 0.0187 0.0144 -0.0146 76 CYS A CA 518 C C . CYS A 69 ? 0.3029 0.2879 0.3612 0.0230 0.0154 -0.0145 76 CYS A C 519 O O . CYS A 69 ? 0.2824 0.2763 0.3492 0.0234 0.0147 -0.0150 76 CYS A O 520 C CB . CYS A 69 ? 0.2907 0.2758 0.3551 0.0145 0.0127 -0.0148 76 CYS A CB 521 S SG . CYS A 69 ? 0.3780 0.3574 0.4391 0.0097 0.0116 -0.0145 76 CYS A SG 522 N N . ASP A 70 ? 0.3096 0.2900 0.3611 0.0262 0.0171 -0.0137 77 ASP A N 523 C CA . ASP A 70 ? 0.3113 0.2987 0.3664 0.0301 0.0183 -0.0132 77 ASP A CA 524 C C . ASP A 70 ? 0.3070 0.3019 0.3660 0.0339 0.0183 -0.0136 77 ASP A C 525 O O . ASP A 70 ? 0.2764 0.2807 0.3425 0.0353 0.0184 -0.0133 77 ASP A O 526 C CB . ASP A 70 ? 0.3344 0.3153 0.3806 0.0335 0.0205 -0.0121 77 ASP A CB 527 C CG . ASP A 70 ? 0.3714 0.3499 0.4177 0.0303 0.0206 -0.0115 77 ASP A CG 528 O OD1 . ASP A 70 ? 0.3944 0.3770 0.4480 0.0257 0.0190 -0.0119 77 ASP A OD1 529 O OD2 . ASP A 70 ? 0.4096 0.3817 0.4480 0.0325 0.0222 -0.0106 77 ASP A OD2 530 N N . ARG A 71 ? 0.3121 0.3031 0.3666 0.0354 0.0181 -0.0141 78 ARG A N 531 C CA . ARG A 71 ? 0.3279 0.3262 0.3864 0.0385 0.0176 -0.0146 78 ARG A CA 532 C C . ARG A 71 ? 0.3091 0.3178 0.3793 0.0353 0.0157 -0.0154 78 ARG A C 533 O O . ARG A 71 ? 0.3114 0.3281 0.3864 0.0375 0.0152 -0.0156 78 ARG A O 534 C CB . ARG A 71 ? 0.3511 0.3429 0.4029 0.0399 0.0175 -0.0152 78 ARG A CB 535 C CG . ARG A 71 ? 0.3869 0.3757 0.4403 0.0348 0.0159 -0.0161 78 ARG A CG 536 C CD . ARG A 71 ? 0.4894 0.4718 0.5358 0.0362 0.0160 -0.0165 78 ARG A CD 537 N NE . ARG A 71 ? 0.5530 0.5296 0.5977 0.0314 0.0151 -0.0168 78 ARG A NE 538 C CZ . ARG A 71 ? 0.5697 0.5412 0.6121 0.0272 0.0150 -0.0163 78 ARG A CZ 539 N NH1 . ARG A 71 ? 0.5815 0.5517 0.6226 0.0271 0.0157 -0.0156 78 ARG A NH1 540 N NH2 . ARG A 71 ? 0.5520 0.5197 0.5933 0.0230 0.0142 -0.0164 78 ARG A NH2 541 N N . LEU A 72 ? 0.2761 0.2843 0.3505 0.0302 0.0146 -0.0157 79 LEU A N 542 C CA . LEU A 72 ? 0.2623 0.2781 0.3461 0.0271 0.0129 -0.0165 79 LEU A CA 543 C C . LEU A 72 ? 0.2575 0.2798 0.3480 0.0255 0.0130 -0.0160 79 LEU A C 544 O O . LEU A 72 ? 0.2456 0.2726 0.3429 0.0223 0.0118 -0.0166 79 LEU A O 545 C CB . LEU A 72 ? 0.2544 0.2658 0.3385 0.0228 0.0118 -0.0171 79 LEU A CB 546 C CG . LEU A 72 ? 0.2624 0.2669 0.3402 0.0231 0.0117 -0.0174 79 LEU A CG 547 C CD1 . LEU A 72 ? 0.2567 0.2589 0.3363 0.0184 0.0107 -0.0176 79 LEU A CD1 548 C CD2 . LEU A 72 ? 0.2370 0.2448 0.3154 0.0261 0.0113 -0.0182 79 LEU A CD2 549 N N . LEU A 73 ? 0.2542 0.2759 0.3418 0.0278 0.0146 -0.0149 80 LEU A N 550 C CA . LEU A 73 ? 0.2605 0.2880 0.3539 0.0263 0.0150 -0.0143 80 LEU A CA 551 C C . LEU A 73 ? 0.2592 0.2977 0.3611 0.0262 0.0141 -0.0146 80 LEU A C 552 O O . LEU A 73 ? 0.2468 0.2900 0.3548 0.0231 0.0136 -0.0145 80 LEU A O 553 C CB . LEU A 73 ? 0.2660 0.2908 0.3541 0.0294 0.0172 -0.0129 80 LEU A CB 554 C CG . LEU A 73 ? 0.2717 0.2861 0.3528 0.0276 0.0176 -0.0126 80 LEU A CG 555 C CD1 . LEU A 73 ? 0.2564 0.2657 0.3296 0.0315 0.0199 -0.0114 80 LEU A CD1 556 C CD2 . LEU A 73 ? 0.2775 0.2932 0.3642 0.0226 0.0167 -0.0126 80 LEU A CD2 557 N N . SER A 74 ? 0.2557 0.2982 0.3574 0.0294 0.0138 -0.0148 81 SER A N 558 C CA . SER A 74 ? 0.2675 0.3202 0.3768 0.0286 0.0125 -0.0153 81 SER A CA 559 C C . SER A 74 ? 0.2579 0.3102 0.3660 0.0298 0.0112 -0.0164 81 SER A C 560 O O . SER A 74 ? 0.2736 0.3240 0.3765 0.0341 0.0119 -0.0161 81 SER A O 561 C CB . SER A 74 ? 0.2664 0.3279 0.3782 0.0318 0.0136 -0.0139 81 SER A CB 562 O OG . SER A 74 ? 0.2972 0.3685 0.4164 0.0300 0.0119 -0.0144 81 SER A OG 563 N N . VAL A 75 A 0.2442 0.2978 0.3566 0.0262 0.0093 -0.0177 81 VAL A N 564 C CA . VAL A 75 A 0.2470 0.3003 0.3581 0.0274 0.0081 -0.0187 81 VAL A CA 565 C C . VAL A 75 A 0.2376 0.2996 0.3551 0.0258 0.0062 -0.0196 81 VAL A C 566 O O . VAL A 75 A 0.2327 0.2983 0.3557 0.0220 0.0054 -0.0198 81 VAL A O 567 C CB . VAL A 75 A 0.2535 0.2980 0.3611 0.0254 0.0077 -0.0196 81 VAL A CB 568 C CG1 . VAL A 75 A 0.2578 0.2932 0.3577 0.0268 0.0093 -0.0188 81 VAL A CG1 569 C CG2 . VAL A 75 A 0.2376 0.2821 0.3500 0.0205 0.0067 -0.0202 81 VAL A CG2 570 N N . PRO A 76 ? 0.2471 0.3118 0.3634 0.0286 0.0054 -0.0200 82 PRO A N 571 C CA . PRO A 76 ? 0.2435 0.3162 0.3652 0.0269 0.0033 -0.0208 82 PRO A CA 572 C C . PRO A 76 ? 0.2427 0.3111 0.3650 0.0235 0.0017 -0.0225 82 PRO A C 573 O O . PRO A 76 ? 0.2397 0.2997 0.3583 0.0230 0.0023 -0.0228 82 PRO A O 574 C CB . PRO A 76 ? 0.2565 0.3333 0.3758 0.0318 0.0031 -0.0205 82 PRO A CB 575 C CG . PRO A 76 ? 0.2559 0.3224 0.3670 0.0350 0.0046 -0.0204 82 PRO A CG 576 C CD . PRO A 76 ? 0.2511 0.3120 0.3606 0.0337 0.0064 -0.0196 82 PRO A CD 577 N N . GLU A 77 ? 0.2228 0.2968 0.3492 0.0211 -0.0001 -0.0234 83 GLU A N 578 C CA . GLU A 77 ? 0.2454 0.3153 0.3717 0.0183 -0.0016 -0.0249 83 GLU A CA 579 C C . GLU A 77 ? 0.2304 0.2933 0.3510 0.0210 -0.0013 -0.0255 83 GLU A C 580 O O . GLU A 77 ? 0.2516 0.3153 0.3690 0.0251 -0.0009 -0.0251 83 GLU A O 581 C CB . GLU A 77 ? 0.2508 0.3281 0.3809 0.0163 -0.0039 -0.0257 83 GLU A CB 582 C CG . GLU A 77 ? 0.3207 0.3936 0.4498 0.0137 -0.0054 -0.0274 83 GLU A CG 583 C CD . GLU A 77 ? 0.3973 0.4770 0.5286 0.0123 -0.0079 -0.0283 83 GLU A CD 584 O OE1 . GLU A 77 ? 0.4361 0.5249 0.5710 0.0120 -0.0086 -0.0275 83 GLU A OE1 585 O OE2 . GLU A 77 ? 0.4682 0.5441 0.5974 0.0112 -0.0092 -0.0297 83 GLU A OE2 586 N N . TRP A 78 ? 0.2358 0.2921 0.3552 0.0189 -0.0013 -0.0262 84 TRP A N 587 C CA . TRP A 78 ? 0.2320 0.2817 0.3462 0.0210 -0.0009 -0.0266 84 TRP A CA 588 C C . TRP A 78 ? 0.2282 0.2761 0.3426 0.0193 -0.0023 -0.0280 84 TRP A C 589 O O . TRP A 78 ? 0.2307 0.2802 0.3485 0.0160 -0.0033 -0.0286 84 TRP A O 590 C CB . TRP A 78 ? 0.2293 0.2718 0.3406 0.0206 0.0007 -0.0258 84 TRP A CB 591 C CG . TRP A 78 ? 0.2103 0.2511 0.3247 0.0167 0.0008 -0.0258 84 TRP A CG 592 C CD1 . TRP A 78 ? 0.2352 0.2725 0.3497 0.0148 0.0004 -0.0263 84 TRP A CD1 593 C CD2 . TRP A 78 ? 0.2010 0.2434 0.3184 0.0146 0.0014 -0.0250 84 TRP A CD2 594 N NE1 . TRP A 78 ? 0.2338 0.2704 0.3510 0.0120 0.0008 -0.0259 84 TRP A NE1 595 C CE2 . TRP A 78 ? 0.2140 0.2536 0.3331 0.0116 0.0013 -0.0251 84 TRP A CE2 596 C CE3 . TRP A 78 ? 0.1983 0.2442 0.3169 0.0153 0.0021 -0.0240 84 TRP A CE3 597 C CZ2 . TRP A 78 ? 0.2237 0.2637 0.3455 0.0092 0.0018 -0.0245 84 TRP A CZ2 598 C CZ3 . TRP A 78 ? 0.1658 0.2121 0.2872 0.0127 0.0027 -0.0234 84 TRP A CZ3 599 C CH2 . TRP A 78 ? 0.1814 0.2247 0.3044 0.0096 0.0024 -0.0236 84 TRP A CH2 600 N N . SER A 79 ? 0.2367 0.2804 0.3468 0.0215 -0.0021 -0.0284 85 SER A N 601 C CA . SER A 79 ? 0.2465 0.2875 0.3556 0.0206 -0.0031 -0.0296 85 SER A CA 602 C C . SER A 79 ? 0.2492 0.2831 0.3562 0.0196 -0.0018 -0.0293 85 SER A C 603 O O . SER A 79 ? 0.2458 0.2775 0.3530 0.0182 -0.0023 -0.0300 85 SER A O 604 C CB . SER A 79 ? 0.2496 0.2913 0.3554 0.0238 -0.0039 -0.0302 85 SER A CB 605 O OG . SER A 79 ? 0.2678 0.3061 0.3692 0.0270 -0.0024 -0.0293 85 SER A OG 606 N N . TYR A 80 ? 0.2485 0.2791 0.3531 0.0206 -0.0002 -0.0281 86 TYR A N 607 C CA . TYR A 80 ? 0.2448 0.2703 0.3484 0.0191 0.0009 -0.0274 86 TYR A CA 608 C C . TYR A 80 ? 0.2448 0.2687 0.3470 0.0191 0.0022 -0.0260 86 TYR A C 609 O O . TYR A 80 ? 0.2467 0.2724 0.3478 0.0209 0.0024 -0.0258 86 TYR A O 610 C CB . TYR A 80 ? 0.2539 0.2751 0.3536 0.0204 0.0012 -0.0276 86 TYR A CB 611 C CG . TYR A 80 ? 0.2468 0.2661 0.3415 0.0236 0.0016 -0.0276 86 TYR A CG 612 C CD1 . TYR A 80 ? 0.2604 0.2747 0.3508 0.0240 0.0031 -0.0265 86 TYR A CD1 613 C CD2 . TYR A 80 ? 0.2442 0.2664 0.3380 0.0260 0.0005 -0.0285 86 TYR A CD2 614 C CE1 . TYR A 80 ? 0.2855 0.2969 0.3704 0.0269 0.0036 -0.0264 86 TYR A CE1 615 C CE2 . TYR A 80 ? 0.2172 0.2371 0.3057 0.0294 0.0010 -0.0284 86 TYR A CE2 616 C CZ . TYR A 80 ? 0.2500 0.2640 0.3338 0.0298 0.0026 -0.0274 86 TYR A CZ 617 O OH . TYR A 80 ? 0.2912 0.3019 0.3690 0.0331 0.0033 -0.0272 86 TYR A OH 618 N N . ILE A 81 ? 0.2263 0.2467 0.3281 0.0173 0.0031 -0.0251 87 ILE A N 619 C CA . ILE A 81 ? 0.2355 0.2535 0.3351 0.0169 0.0042 -0.0239 87 ILE A CA 620 C C . ILE A 81 ? 0.2379 0.2504 0.3323 0.0171 0.0051 -0.0232 87 ILE A C 621 O O . ILE A 81 ? 0.2464 0.2578 0.3412 0.0161 0.0052 -0.0230 87 ILE A O 622 C CB . ILE A 81 ? 0.2118 0.2308 0.3151 0.0140 0.0043 -0.0231 87 ILE A CB 623 C CG1 . ILE A 81 ? 0.2126 0.2366 0.3205 0.0135 0.0036 -0.0237 87 ILE A CG1 624 C CG2 . ILE A 81 ? 0.2226 0.2385 0.3229 0.0133 0.0053 -0.0218 87 ILE A CG2 625 C CD1 . ILE A 81 ? 0.2268 0.2515 0.3382 0.0107 0.0037 -0.0231 87 ILE A CD1 626 N N . MET A 82 ? 0.2426 0.2517 0.3318 0.0186 0.0059 -0.0227 88 MET A N 627 C CA . MET A 82 ? 0.2452 0.2484 0.3287 0.0181 0.0068 -0.0219 88 MET A CA 628 C C . MET A 82 ? 0.2456 0.2462 0.3280 0.0154 0.0074 -0.0206 88 MET A C 629 O O . MET A 82 ? 0.2417 0.2413 0.3223 0.0158 0.0077 -0.0203 88 MET A O 630 C CB . MET A 82 ? 0.2554 0.2549 0.3324 0.0214 0.0074 -0.0221 88 MET A CB 631 C CG . MET A 82 ? 0.2536 0.2558 0.3312 0.0244 0.0067 -0.0234 88 MET A CG 632 S SD . MET A 82 ? 0.3119 0.3121 0.3832 0.0292 0.0072 -0.0236 88 MET A SD 633 C CE . MET A 82 ? 0.3251 0.3152 0.3868 0.0287 0.0089 -0.0224 88 MET A CE 634 N N . GLU A 83 ? 0.2419 0.2416 0.3251 0.0126 0.0075 -0.0197 89 GLU A N 635 C CA . GLU A 83 ? 0.2560 0.2534 0.3377 0.0096 0.0078 -0.0183 89 GLU A CA 636 C C . GLU A 83 ? 0.2606 0.2534 0.3373 0.0078 0.0084 -0.0173 89 GLU A C 637 O O . GLU A 83 ? 0.2657 0.2595 0.3434 0.0079 0.0085 -0.0173 89 GLU A O 638 C CB . GLU A 83 ? 0.2430 0.2449 0.3313 0.0072 0.0073 -0.0177 89 GLU A CB 639 C CG . GLU A 83 ? 0.2484 0.2487 0.3355 0.0042 0.0074 -0.0164 89 GLU A CG 640 C CD . GLU A 83 ? 0.2865 0.2912 0.3797 0.0021 0.0069 -0.0156 89 GLU A CD 641 O OE1 . GLU A 83 ? 0.2995 0.3071 0.3962 0.0020 0.0069 -0.0154 89 GLU A OE1 642 O OE2 . GLU A 83 ? 0.2672 0.2721 0.3611 0.0008 0.0068 -0.0151 89 GLU A OE2 643 N N . LYS A 84 ? 0.2674 0.2551 0.3384 0.0060 0.0088 -0.0164 90 LYS A N 644 C CA . LYS A 84 ? 0.2817 0.2651 0.3478 0.0033 0.0092 -0.0152 90 LYS A CA 645 C C . LYS A 84 ? 0.2983 0.2862 0.3695 -0.0002 0.0088 -0.0138 90 LYS A C 646 O O . LYS A 84 ? 0.2849 0.2777 0.3621 -0.0008 0.0082 -0.0136 90 LYS A O 647 C CB . LYS A 84 ? 0.2835 0.2592 0.3410 0.0020 0.0097 -0.0147 90 LYS A CB 648 C CG . LYS A 84 ? 0.2512 0.2217 0.3023 0.0062 0.0105 -0.0158 90 LYS A CG 649 C CD . LYS A 84 ? 0.3092 0.2704 0.3501 0.0054 0.0112 -0.0153 90 LYS A CD 650 C CE . LYS A 84 ? 0.3415 0.2977 0.3757 0.0105 0.0123 -0.0163 90 LYS A CE 651 N NZ . LYS A 84 ? 0.4207 0.3674 0.4447 0.0104 0.0132 -0.0158 90 LYS A NZ 652 N N . GLU A 85 ? 0.3224 0.3090 0.3912 -0.0025 0.0092 -0.0127 91 GLU A N 653 C CA . GLU A 85 ? 0.3525 0.3442 0.4261 -0.0057 0.0089 -0.0109 91 GLU A CA 654 C C . GLU A 85 ? 0.3417 0.3340 0.4158 -0.0091 0.0081 -0.0098 91 GLU A C 655 O O . GLU A 85 ? 0.3421 0.3403 0.4224 -0.0100 0.0076 -0.0089 91 GLU A O 656 C CB . GLU A 85 ? 0.3614 0.3515 0.4315 -0.0078 0.0095 -0.0096 91 GLU A CB 657 C CG . GLU A 85 ? 0.4274 0.4244 0.5030 -0.0107 0.0094 -0.0075 91 GLU A CG 658 C CD . GLU A 85 ? 0.5216 0.5255 0.6052 -0.0078 0.0095 -0.0077 91 GLU A CD 659 O OE1 . GLU A 85 ? 0.5277 0.5311 0.6120 -0.0040 0.0098 -0.0094 91 GLU A OE1 660 O OE2 . GLU A 85 ? 0.5675 0.5774 0.6562 -0.0095 0.0092 -0.0061 91 GLU A OE2 661 N N . ASN A 86 ? 0.3451 0.3306 0.4119 -0.0106 0.0081 -0.0098 92 ASN A N 662 C CA . ASN A 86 ? 0.3580 0.3426 0.4236 -0.0141 0.0073 -0.0087 92 ASN A CA 663 C C . ASN A 86 ? 0.3491 0.3271 0.4088 -0.0125 0.0075 -0.0099 92 ASN A C 664 O O . ASN A 86 ? 0.3437 0.3139 0.3946 -0.0144 0.0077 -0.0095 92 ASN A O 665 C CB . ASN A 86 ? 0.3815 0.3632 0.4418 -0.0192 0.0070 -0.0069 92 ASN A CB 666 C CG . ASN A 86 ? 0.4386 0.4273 0.5044 -0.0210 0.0070 -0.0053 92 ASN A CG 667 O OD1 . ASN A 86 ? 0.5312 0.5181 0.5940 -0.0215 0.0077 -0.0049 92 ASN A OD1 668 N ND2 . ASN A 86 ? 0.4778 0.4747 0.5515 -0.0216 0.0064 -0.0042 92 ASN A ND2 669 N N . PRO A 87 ? 0.3382 0.3188 0.4019 -0.0090 0.0076 -0.0111 93 PRO A N 670 C CA . PRO A 87 ? 0.3343 0.3093 0.3926 -0.0067 0.0081 -0.0120 93 PRO A CA 671 C C . PRO A 87 ? 0.3435 0.3143 0.3972 -0.0100 0.0076 -0.0111 93 PRO A C 672 O O . PRO A 87 ? 0.3405 0.3160 0.3992 -0.0128 0.0067 -0.0101 93 PRO A O 673 C CB . PRO A 87 ? 0.3415 0.3227 0.4072 -0.0034 0.0080 -0.0131 93 PRO A CB 674 C CG . PRO A 87 ? 0.3142 0.3019 0.3870 -0.0030 0.0077 -0.0132 93 PRO A CG 675 C CD . PRO A 87 ? 0.3329 0.3215 0.4059 -0.0070 0.0073 -0.0116 93 PRO A CD 676 N N . ARG A 88 ? 0.3435 0.3054 0.3876 -0.0095 0.0083 -0.0113 94 ARG A N 677 C CA . ARG A 88 ? 0.3664 0.3224 0.4042 -0.0127 0.0080 -0.0105 94 ARG A CA 678 C C . ARG A 88 ? 0.3447 0.3038 0.3864 -0.0115 0.0078 -0.0106 94 ARG A C 679 O O . ARG A 88 ? 0.3412 0.2992 0.3816 -0.0148 0.0070 -0.0097 94 ARG A O 680 C CB . ARG A 88 ? 0.3802 0.3249 0.4057 -0.0112 0.0091 -0.0109 94 ARG A CB 681 C CG . ARG A 88 ? 0.4698 0.4058 0.4858 -0.0156 0.0087 -0.0100 94 ARG A CG 682 C CD . ARG A 88 ? 0.5915 0.5148 0.5940 -0.0136 0.0101 -0.0105 94 ARG A CD 683 N NE . ARG A 88 ? 0.6456 0.5666 0.6453 -0.0137 0.0106 -0.0106 94 ARG A NE 684 C CZ . ARG A 88 ? 0.6819 0.6036 0.6822 -0.0086 0.0117 -0.0116 94 ARG A CZ 685 N NH1 . ARG A 88 ? 0.7039 0.6288 0.7074 -0.0030 0.0125 -0.0125 94 ARG A NH1 686 N NH2 . ARG A 88 ? 0.6797 0.5989 0.6769 -0.0091 0.0121 -0.0116 94 ARG A NH2 687 N N . ASP A 89 ? 0.3283 0.2912 0.3745 -0.0068 0.0085 -0.0117 95 ASP A N 688 C CA . ASP A 89 ? 0.3150 0.2795 0.3633 -0.0051 0.0088 -0.0119 95 ASP A CA 689 C C . ASP A 89 ? 0.2928 0.2672 0.3525 -0.0050 0.0082 -0.0120 95 ASP A C 690 O O . ASP A 89 ? 0.2847 0.2640 0.3495 -0.0017 0.0085 -0.0130 95 ASP A O 691 C CB . ASP A 89 ? 0.3231 0.2842 0.3669 0.0000 0.0103 -0.0128 95 ASP A CB 692 C CG . ASP A 89 ? 0.3729 0.3225 0.4039 0.0002 0.0112 -0.0127 95 ASP A CG 693 O OD1 . ASP A 89 ? 0.3597 0.3033 0.3847 -0.0030 0.0109 -0.0119 95 ASP A OD1 694 O OD2 . ASP A 89 ? 0.3799 0.3263 0.4064 0.0038 0.0122 -0.0133 95 ASP A OD2 695 N N . GLY A 90 A 0.2736 0.2506 0.3365 -0.0085 0.0072 -0.0110 95 GLY A N 696 C CA . GLY A 90 A 0.2658 0.2511 0.3383 -0.0086 0.0066 -0.0109 95 GLY A CA 697 C C . GLY A 90 A 0.2612 0.2462 0.3339 -0.0099 0.0064 -0.0102 95 GLY A C 698 O O . GLY A 90 A 0.2315 0.2143 0.3019 -0.0077 0.0072 -0.0107 95 GLY A O 699 N N . LEU A 91 ? 0.2535 0.2407 0.3283 -0.0134 0.0053 -0.0089 96 LEU A N 700 C CA . LEU A 91 ? 0.2715 0.2583 0.3460 -0.0149 0.0049 -0.0081 96 LEU A CA 701 C C . LEU A 91 ? 0.2918 0.2700 0.3562 -0.0170 0.0047 -0.0077 96 LEU A C 702 O O . LEU A 91 ? 0.2864 0.2631 0.3478 -0.0210 0.0036 -0.0065 96 LEU A O 703 C CB . LEU A 91 ? 0.2566 0.2495 0.3371 -0.0176 0.0037 -0.0067 96 LEU A CB 704 C CG . LEU A 91 ? 0.3282 0.3278 0.4173 -0.0159 0.0039 -0.0069 96 LEU A CG 705 C CD1 . LEU A 91 ? 0.3198 0.3220 0.4128 -0.0127 0.0047 -0.0083 96 LEU A CD1 706 C CD2 . LEU A 91 ? 0.3359 0.3409 0.4295 -0.0181 0.0029 -0.0053 96 LEU A CD2 707 N N . CYS A 92 ? 0.2936 0.2661 0.3523 -0.0144 0.0059 -0.0084 97 CYS A N 708 C CA . CYS A 92 ? 0.3065 0.2693 0.3541 -0.0161 0.0060 -0.0080 97 CYS A CA 709 C C . CYS A 92 ? 0.2963 0.2582 0.3426 -0.0197 0.0048 -0.0069 97 CYS A C 710 O O . CYS A 92 ? 0.3003 0.2572 0.3401 -0.0238 0.0036 -0.0060 97 CYS A O 711 C CB . CYS A 92 ? 0.3044 0.2611 0.3456 -0.0118 0.0078 -0.0089 97 CYS A CB 712 S SG . CYS A 92 ? 0.3710 0.3345 0.4201 -0.0073 0.0091 -0.0095 97 CYS A SG 713 N N . TYR A 93 ? 0.2762 0.2429 0.3283 -0.0185 0.0049 -0.0067 98 TYR A N 714 C CA . TYR A 93 ? 0.2738 0.2425 0.3275 -0.0220 0.0035 -0.0054 98 TYR A CA 715 C C . TYR A 93 ? 0.2656 0.2426 0.3275 -0.0240 0.0022 -0.0046 98 TYR A C 716 O O . TYR A 93 ? 0.2640 0.2475 0.3339 -0.0214 0.0029 -0.0052 98 TYR A O 717 C CB . TYR A 93 ? 0.2632 0.2340 0.3202 -0.0201 0.0042 -0.0054 98 TYR A CB 718 C CG . TYR A 93 ? 0.2711 0.2411 0.3263 -0.0235 0.0028 -0.0041 98 TYR A CG 719 C CD1 . TYR A 93 ? 0.3135 0.2750 0.3592 -0.0245 0.0028 -0.0039 98 TYR A CD1 720 C CD2 . TYR A 93 ? 0.2688 0.2461 0.3309 -0.0259 0.0013 -0.0029 98 TYR A CD2 721 C CE1 . TYR A 93 ? 0.3167 0.2774 0.3603 -0.0279 0.0013 -0.0026 98 TYR A CE1 722 C CE2 . TYR A 93 ? 0.2849 0.2621 0.3453 -0.0291 -0.0001 -0.0015 98 TYR A CE2 723 C CZ . TYR A 93 ? 0.2814 0.2503 0.3326 -0.0303 -0.0002 -0.0014 98 TYR A CZ 724 O OH . TYR A 93 ? 0.2655 0.2344 0.3149 -0.0335 -0.0019 -0.0001 98 TYR A OH 725 N N . PRO A 94 ? 0.2604 0.2378 0.3205 -0.0284 0.0005 -0.0033 99 PRO A N 726 C CA . PRO A 94 ? 0.2637 0.2493 0.3312 -0.0297 -0.0002 -0.0024 99 PRO A CA 727 C C . PRO A 94 ? 0.2502 0.2441 0.3269 -0.0284 -0.0003 -0.0017 99 PRO A C 728 O O . PRO A 94 ? 0.2439 0.2375 0.3209 -0.0281 -0.0004 -0.0014 99 PRO A O 729 C CB . PRO A 94 ? 0.2634 0.2479 0.3264 -0.0350 -0.0020 -0.0007 99 PRO A CB 730 C CG . PRO A 94 ? 0.2656 0.2435 0.3214 -0.0369 -0.0026 -0.0005 99 PRO A CG 731 C CD . PRO A 94 ? 0.2739 0.2449 0.3253 -0.0327 -0.0006 -0.0023 99 PRO A CD 732 N N . GLY A 95 ? 0.2519 0.2526 0.3355 -0.0275 -0.0003 -0.0014 100 GLY A N 733 C CA . GLY A 95 ? 0.2449 0.2528 0.3362 -0.0264 -0.0004 -0.0005 100 GLY A CA 734 C C . GLY A 95 ? 0.2472 0.2606 0.3446 -0.0243 0.0001 -0.0006 100 GLY A C 735 O O . GLY A 95 ? 0.2603 0.2751 0.3574 -0.0255 0.0000 -0.0001 100 GLY A O 736 N N . SER A 96 ? 0.2367 0.2530 0.3394 -0.0214 0.0010 -0.0012 101 SER A N 737 C CA . SER A 96 ? 0.2409 0.2619 0.3490 -0.0193 0.0016 -0.0013 101 SER A CA 738 C C . SER A 96 ? 0.2365 0.2566 0.3473 -0.0160 0.0028 -0.0032 101 SER A C 739 O O . SER A 96 ? 0.2299 0.2474 0.3395 -0.0156 0.0031 -0.0039 101 SER A O 740 C CB . SER A 96 ? 0.2423 0.2696 0.3547 -0.0198 0.0010 0.0008 101 SER A CB 741 O OG . SER A 96 ? 0.2484 0.2759 0.3622 -0.0192 0.0010 0.0011 101 SER A OG 742 N N . PHE A 97 ? 0.2214 0.2439 0.3355 -0.0140 0.0034 -0.0038 102 PHE A N 743 C CA . PHE A 97 ? 0.2190 0.2410 0.3355 -0.0115 0.0043 -0.0055 102 PHE A CA 744 C C . PHE A 97 ? 0.2233 0.2490 0.3440 -0.0100 0.0047 -0.0049 102 PHE A C 745 O O . PHE A 97 ? 0.2198 0.2470 0.3412 -0.0092 0.0048 -0.0048 102 PHE A O 746 C CB . PHE A 97 ? 0.2136 0.2331 0.3278 -0.0103 0.0047 -0.0073 102 PHE A CB 747 C CG . PHE A 97 ? 0.2146 0.2332 0.3300 -0.0085 0.0053 -0.0090 102 PHE A CG 748 C CD1 . PHE A 97 ? 0.1913 0.2070 0.3035 -0.0080 0.0056 -0.0100 102 PHE A CD1 749 C CD2 . PHE A 97 ? 0.2097 0.2304 0.3290 -0.0071 0.0057 -0.0096 102 PHE A CD2 750 C CE1 . PHE A 97 ? 0.2179 0.2341 0.3317 -0.0064 0.0062 -0.0113 102 PHE A CE1 751 C CE2 . PHE A 97 ? 0.2555 0.2760 0.3761 -0.0060 0.0061 -0.0112 102 PHE A CE2 752 C CZ . PHE A 97 ? 0.2310 0.2500 0.3493 -0.0057 0.0063 -0.0119 102 PHE A CZ 753 N N . ASN A 98 ? 0.2138 0.2403 0.3367 -0.0094 0.0049 -0.0045 103 ASN A N 754 C CA . ASN A 98 ? 0.2179 0.2468 0.3439 -0.0076 0.0055 -0.0038 103 ASN A CA 755 C C . ASN A 98 ? 0.2178 0.2454 0.3446 -0.0056 0.0062 -0.0057 103 ASN A C 756 O O . ASN A 98 ? 0.2154 0.2407 0.3415 -0.0056 0.0063 -0.0075 103 ASN A O 757 C CB . ASN A 98 ? 0.2070 0.2357 0.3341 -0.0074 0.0058 -0.0031 103 ASN A CB 758 C CG . ASN A 98 ? 0.2206 0.2513 0.3471 -0.0090 0.0050 -0.0009 103 ASN A CG 759 O OD1 . ASN A 98 ? 0.2287 0.2628 0.3555 -0.0096 0.0044 0.0007 103 ASN A OD1 760 N ND2 . ASN A 98 ? 0.2351 0.2640 0.3607 -0.0098 0.0049 -0.0009 103 ASN A ND2 761 N N . ASP A 99 ? 0.1872 0.2165 0.3151 -0.0040 0.0066 -0.0050 104 ASP A N 762 C CA . ASP A 99 ? 0.1872 0.2150 0.3152 -0.0021 0.0072 -0.0066 104 ASP A CA 763 C C . ASP A 99 ? 0.1669 0.1932 0.2935 -0.0026 0.0068 -0.0085 104 ASP A C 764 O O . ASP A 99 ? 0.1656 0.1899 0.2920 -0.0019 0.0069 -0.0104 104 ASP A O 765 C CB . ASP A 99 ? 0.1980 0.2233 0.3265 -0.0014 0.0077 -0.0075 104 ASP A CB 766 C CG . ASP A 99 ? 0.2741 0.3002 0.4034 -0.0007 0.0082 -0.0057 104 ASP A CG 767 O OD1 . ASP A 99 ? 0.2933 0.3214 0.4230 0.0009 0.0087 -0.0042 104 ASP A OD1 768 O OD2 . ASP A 99 ? 0.3358 0.3611 0.4652 -0.0018 0.0081 -0.0054 104 ASP A OD2 769 N N . TYR A 100 ? 0.1743 0.2013 0.2993 -0.0038 0.0064 -0.0078 105 TYR A N 770 C CA . TYR A 100 ? 0.1755 0.2004 0.2983 -0.0039 0.0061 -0.0094 105 TYR A CA 771 C C . TYR A 100 ? 0.1831 0.2077 0.3057 -0.0021 0.0064 -0.0106 105 TYR A C 772 O O . TYR A 100 ? 0.1810 0.2041 0.3029 -0.0012 0.0063 -0.0124 105 TYR A O 773 C CB . TYR A 100 ? 0.1621 0.1868 0.2821 -0.0058 0.0057 -0.0083 105 TYR A CB 774 C CG . TYR A 100 ? 0.1760 0.1976 0.2924 -0.0058 0.0056 -0.0097 105 TYR A CG 775 C CD1 . TYR A 100 ? 0.1793 0.1991 0.2951 -0.0049 0.0057 -0.0112 105 TYR A CD1 776 C CD2 . TYR A 100 ? 0.2066 0.2271 0.3200 -0.0066 0.0055 -0.0091 105 TYR A CD2 777 C CE1 . TYR A 100 ? 0.2162 0.2332 0.3282 -0.0043 0.0057 -0.0122 105 TYR A CE1 778 C CE2 . TYR A 100 ? 0.2371 0.2539 0.3462 -0.0063 0.0055 -0.0102 105 TYR A CE2 779 C CZ . TYR A 100 ? 0.2258 0.2409 0.3342 -0.0049 0.0057 -0.0118 105 TYR A CZ 780 O OH . TYR A 100 ? 0.2397 0.2513 0.3436 -0.0040 0.0059 -0.0126 105 TYR A OH 781 N N . GLU A 101 ? 0.1913 0.2178 0.3148 -0.0013 0.0068 -0.0094 106 GLU A N 782 C CA . GLU A 101 ? 0.2017 0.2274 0.3246 0.0006 0.0073 -0.0104 106 GLU A CA 783 C C . GLU A 101 ? 0.1916 0.2155 0.3152 0.0020 0.0074 -0.0121 106 GLU A C 784 O O . GLU A 101 ? 0.1872 0.2096 0.3096 0.0031 0.0073 -0.0137 106 GLU A O 785 C CB . GLU A 101 ? 0.1984 0.2267 0.3219 0.0015 0.0079 -0.0085 106 GLU A CB 786 C CG . GLU A 101 ? 0.2600 0.2901 0.3824 -0.0004 0.0077 -0.0070 106 GLU A CG 787 C CD . GLU A 101 ? 0.3056 0.3374 0.4285 -0.0028 0.0071 -0.0054 106 GLU A CD 788 O OE1 . GLU A 101 ? 0.3167 0.3499 0.4417 -0.0026 0.0071 -0.0046 106 GLU A OE1 789 O OE2 . GLU A 101 ? 0.3522 0.3832 0.4728 -0.0051 0.0065 -0.0050 106 GLU A OE2 790 N N . GLU A 102 ? 0.1983 0.2221 0.3233 0.0019 0.0076 -0.0116 107 GLU A N 791 C CA . GLU A 102 ? 0.2055 0.2268 0.3305 0.0026 0.0077 -0.0131 107 GLU A CA 792 C C . GLU A 102 ? 0.2036 0.2243 0.3285 0.0014 0.0069 -0.0150 107 GLU A C 793 O O . GLU A 102 ? 0.1954 0.2147 0.3198 0.0017 0.0066 -0.0167 107 GLU A O 794 C CB . GLU A 102 ? 0.1870 0.2078 0.3130 0.0024 0.0082 -0.0120 107 GLU A CB 795 C CG . GLU A 102 ? 0.2327 0.2536 0.3584 0.0046 0.0092 -0.0103 107 GLU A CG 796 C CD . GLU A 102 ? 0.2454 0.2627 0.3689 0.0064 0.0097 -0.0116 107 GLU A CD 797 O OE1 . GLU A 102 ? 0.2371 0.2510 0.3596 0.0057 0.0095 -0.0133 107 GLU A OE1 798 O OE2 . GLU A 102 ? 0.2098 0.2277 0.3324 0.0084 0.0103 -0.0110 107 GLU A OE2 799 N N . LEU A 103 ? 0.2062 0.2280 0.3313 0.0000 0.0066 -0.0146 108 LEU A N 800 C CA . LEU A 103 ? 0.2128 0.2347 0.3378 -0.0004 0.0061 -0.0161 108 LEU A CA 801 C C . LEU A 103 ? 0.2224 0.2442 0.3457 0.0007 0.0057 -0.0173 108 LEU A C 802 O O . LEU A 103 ? 0.2130 0.2351 0.3365 0.0010 0.0052 -0.0188 108 LEU A O 803 C CB . LEU A 103 ? 0.2137 0.2360 0.3383 -0.0016 0.0061 -0.0152 108 LEU A CB 804 C CG . LEU A 103 ? 0.2428 0.2656 0.3670 -0.0016 0.0058 -0.0164 108 LEU A CG 805 C CD1 . LEU A 103 ? 0.2586 0.2823 0.3849 -0.0020 0.0057 -0.0175 108 LEU A CD1 806 C CD2 . LEU A 103 ? 0.2516 0.2739 0.3746 -0.0025 0.0061 -0.0154 108 LEU A CD2 807 N N . LYS A 104 ? 0.2256 0.2471 0.3472 0.0012 0.0059 -0.0165 109 LYS A N 808 C CA . LYS A 104 ? 0.2330 0.2539 0.3526 0.0026 0.0057 -0.0175 109 LYS A CA 809 C C . LYS A 104 ? 0.2216 0.2419 0.3414 0.0038 0.0055 -0.0187 109 LYS A C 810 O O . LYS A 104 ? 0.2239 0.2441 0.3426 0.0048 0.0050 -0.0202 109 LYS A O 811 C CB . LYS A 104 ? 0.2361 0.2565 0.3535 0.0025 0.0061 -0.0162 109 LYS A CB 812 C CG . LYS A 104 ? 0.2720 0.2918 0.3879 0.0008 0.0060 -0.0151 109 LYS A CG 813 C CD . LYS A 104 ? 0.2966 0.3156 0.4098 0.0000 0.0062 -0.0137 109 LYS A CD 814 C CE . LYS A 104 ? 0.3653 0.3815 0.4743 0.0008 0.0063 -0.0146 109 LYS A CE 815 N NZ . LYS A 104 ? 0.3584 0.3732 0.4642 -0.0009 0.0065 -0.0131 109 LYS A NZ 816 N N . HIS A 105 ? 0.2054 0.2252 0.3261 0.0041 0.0060 -0.0181 110 HIS A N 817 C CA . HIS A 105 ? 0.2190 0.2370 0.3389 0.0052 0.0059 -0.0193 110 HIS A CA 818 C C . HIS A 105 ? 0.2310 0.2487 0.3516 0.0042 0.0050 -0.0210 110 HIS A C 819 O O . HIS A 105 ? 0.2315 0.2483 0.3508 0.0047 0.0044 -0.0226 110 HIS A O 820 C CB . HIS A 105 ? 0.2062 0.2229 0.3261 0.0061 0.0069 -0.0181 110 HIS A CB 821 C CG . HIS A 105 ? 0.2244 0.2380 0.3423 0.0074 0.0069 -0.0193 110 HIS A CG 822 N ND1 . HIS A 105 ? 0.2378 0.2504 0.3535 0.0091 0.0070 -0.0199 110 HIS A ND1 823 C CD2 . HIS A 105 ? 0.2643 0.2748 0.3812 0.0071 0.0069 -0.0201 110 HIS A CD2 824 C CE1 . HIS A 105 ? 0.2876 0.2966 0.4010 0.0099 0.0070 -0.0211 110 HIS A CE1 825 N NE2 . HIS A 105 ? 0.2849 0.2923 0.3987 0.0086 0.0069 -0.0212 110 HIS A NE2 826 N N . LEU A 106 ? 0.2320 0.2506 0.3544 0.0026 0.0050 -0.0207 111 LEU A N 827 C CA . LEU A 106 ? 0.2690 0.2884 0.3924 0.0011 0.0042 -0.0220 111 LEU A CA 828 C C . LEU A 106 ? 0.2686 0.2905 0.3917 0.0017 0.0033 -0.0232 111 LEU A C 829 O O . LEU A 106 ? 0.2787 0.3011 0.4016 0.0013 0.0024 -0.0246 111 LEU A O 830 C CB . LEU A 106 ? 0.2723 0.2928 0.3977 -0.0005 0.0045 -0.0212 111 LEU A CB 831 C CG . LEU A 106 ? 0.3126 0.3351 0.4396 -0.0022 0.0038 -0.0223 111 LEU A CG 832 C CD1 . LEU A 106 ? 0.3324 0.3521 0.4585 -0.0035 0.0035 -0.0232 111 LEU A CD1 833 C CD2 . LEU A 106 ? 0.3334 0.3576 0.4622 -0.0035 0.0043 -0.0213 111 LEU A CD2 834 N N . LEU A 107 ? 0.2795 0.3024 0.4020 0.0026 0.0036 -0.0225 112 LEU A N 835 C CA . LEU A 107 ? 0.2968 0.3217 0.4184 0.0038 0.0030 -0.0233 112 LEU A CA 836 C C . LEU A 107 ? 0.3113 0.3355 0.4311 0.0052 0.0023 -0.0246 112 LEU A C 837 O O . LEU A 107 ? 0.3110 0.3377 0.4308 0.0058 0.0014 -0.0256 112 LEU A O 838 C CB . LEU A 107 ? 0.2913 0.3158 0.4111 0.0047 0.0037 -0.0223 112 LEU A CB 839 C CG . LEU A 107 ? 0.3095 0.3348 0.4305 0.0034 0.0041 -0.0213 112 LEU A CG 840 C CD1 . LEU A 107 ? 0.3458 0.3694 0.4639 0.0040 0.0047 -0.0203 112 LEU A CD1 841 C CD2 . LEU A 107 ? 0.3538 0.3825 0.4768 0.0032 0.0037 -0.0220 112 LEU A CD2 842 N N . SER A 108 ? 0.3065 0.3279 0.4250 0.0057 0.0026 -0.0246 113 SER A N 843 C CA . SER A 108 ? 0.3322 0.3522 0.4485 0.0071 0.0020 -0.0258 113 SER A CA 844 C C . SER A 108 ? 0.3347 0.3554 0.4514 0.0059 0.0007 -0.0274 113 SER A C 845 O O . SER A 108 ? 0.3561 0.3761 0.4707 0.0069 -0.0001 -0.0286 113 SER A O 846 C CB . SER A 108 ? 0.3288 0.3455 0.4435 0.0080 0.0029 -0.0252 113 SER A CB 847 O OG . SER A 108 ? 0.3819 0.3986 0.4959 0.0089 0.0039 -0.0237 113 SER A OG 848 N N . SER A 109 ? 0.3269 0.3485 0.4458 0.0037 0.0005 -0.0274 114 SER A N 849 C CA . SER A 109 ? 0.3265 0.3489 0.4456 0.0019 -0.0008 -0.0288 114 SER A CA 850 C C . SER A 109 ? 0.3169 0.3448 0.4391 0.0004 -0.0015 -0.0288 114 SER A C 851 O O . SER A 109 ? 0.3350 0.3645 0.4582 -0.0018 -0.0026 -0.0297 114 SER A O 852 C CB . SER A 109 ? 0.3422 0.3601 0.4600 0.0002 -0.0006 -0.0291 114 SER A CB 853 O OG . SER A 109 ? 0.3758 0.3926 0.4950 -0.0002 0.0006 -0.0276 114 SER A OG 854 N N . VAL A 110 ? 0.2895 0.3199 0.4130 0.0016 -0.0007 -0.0277 115 VAL A N 855 C CA . VAL A 110 ? 0.2730 0.3089 0.3992 0.0009 -0.0010 -0.0275 115 VAL A CA 856 C C . VAL A 110 ? 0.2615 0.3005 0.3867 0.0036 -0.0013 -0.0276 115 VAL A C 857 O O . VAL A 110 ? 0.2472 0.2835 0.3698 0.0059 -0.0006 -0.0272 115 VAL A O 858 C CB . VAL A 110 ? 0.2696 0.3052 0.3972 0.0004 0.0003 -0.0260 115 VAL A CB 859 C CG1 . VAL A 110 ? 0.2790 0.3201 0.4090 0.0002 0.0003 -0.0255 115 VAL A CG1 860 C CG2 . VAL A 110 ? 0.2781 0.3104 0.4063 -0.0018 0.0007 -0.0257 115 VAL A CG2 861 N N . LYS A 111 ? 0.2382 0.2830 0.3653 0.0034 -0.0024 -0.0280 116 LYS A N 862 C CA . LYS A 111 ? 0.2423 0.2905 0.3683 0.0065 -0.0027 -0.0280 116 LYS A CA 863 C C . LYS A 111 ? 0.2338 0.2875 0.3619 0.0074 -0.0020 -0.0269 116 LYS A C 864 O O . LYS A 111 ? 0.2319 0.2881 0.3585 0.0106 -0.0019 -0.0266 116 LYS A O 865 C CB . LYS A 111 ? 0.2547 0.3058 0.3804 0.0064 -0.0046 -0.0293 116 LYS A CB 866 C CG . LYS A 111 ? 0.2795 0.3251 0.4019 0.0069 -0.0051 -0.0304 116 LYS A CG 867 C CD . LYS A 111 ? 0.3710 0.4199 0.4935 0.0058 -0.0073 -0.0317 116 LYS A CD 868 C CE . LYS A 111 ? 0.3990 0.4432 0.5175 0.0071 -0.0078 -0.0328 116 LYS A CE 869 N NZ . LYS A 111 ? 0.4345 0.4816 0.5528 0.0054 -0.0102 -0.0342 116 LYS A NZ 870 N N . HIS A 112 A 0.2336 0.2889 0.3646 0.0050 -0.0015 -0.0262 116 HIS A N 871 C CA . HIS A 112 A 0.2293 0.2893 0.3619 0.0061 -0.0006 -0.0250 116 HIS A CA 872 C C . HIS A 112 A 0.2213 0.2805 0.3561 0.0035 0.0003 -0.0242 116 HIS A C 873 O O . HIS A 112 A 0.2294 0.2872 0.3657 0.0001 -0.0003 -0.0248 116 HIS A O 874 C CB . HIS A 112 A 0.2302 0.2990 0.3655 0.0065 -0.0018 -0.0250 116 HIS A CB 875 C CG . HIS A 112 A 0.2436 0.3178 0.3799 0.0091 -0.0005 -0.0236 116 HIS A CG 876 N ND1 . HIS A 112 A 0.2655 0.3481 0.4062 0.0077 -0.0008 -0.0228 116 HIS A ND1 877 C CD2 . HIS A 112 A 0.2709 0.3428 0.4038 0.0130 0.0010 -0.0226 116 HIS A CD2 878 C CE1 . HIS A 112 A 0.2930 0.3787 0.4332 0.0112 0.0007 -0.0213 116 HIS A CE1 879 N NE2 . HIS A 112 A 0.2583 0.3371 0.3933 0.0145 0.0018 -0.0212 116 HIS A NE2 880 N N . PHE A 113 B 0.2035 0.2629 0.3377 0.0051 0.0018 -0.0229 116 PHE A N 881 C CA . PHE A 113 B 0.2102 0.2699 0.3466 0.0030 0.0028 -0.0220 116 PHE A CA 882 C C . PHE A 113 B 0.2192 0.2864 0.3580 0.0040 0.0034 -0.0209 116 PHE A C 883 O O . PHE A 113 B 0.2240 0.2943 0.3614 0.0076 0.0036 -0.0205 116 PHE A O 884 C CB . PHE A 113 B 0.2041 0.2575 0.3373 0.0039 0.0042 -0.0211 116 PHE A CB 885 C CG . PHE A 113 B 0.2126 0.2597 0.3444 0.0024 0.0040 -0.0215 116 PHE A CG 886 C CD1 . PHE A 113 B 0.2087 0.2547 0.3426 -0.0006 0.0035 -0.0220 116 PHE A CD1 887 C CD2 . PHE A 113 B 0.1960 0.2380 0.3238 0.0041 0.0045 -0.0213 116 PHE A CD2 888 C CE1 . PHE A 113 B 0.2285 0.2690 0.3609 -0.0014 0.0035 -0.0221 116 PHE A CE1 889 C CE2 . PHE A 113 B 0.2133 0.2506 0.3401 0.0029 0.0043 -0.0214 116 PHE A CE2 890 C CZ . PHE A 113 B 0.2364 0.2733 0.3658 0.0003 0.0039 -0.0217 116 PHE A CZ 891 N N . GLU A 114 C 0.2198 0.2895 0.3618 0.0013 0.0038 -0.0203 116 GLU A N 892 C CA . GLU A 114 C 0.2288 0.3043 0.3725 0.0026 0.0051 -0.0188 116 GLU A CA 893 C C . GLU A 114 C 0.2305 0.3009 0.3727 0.0022 0.0067 -0.0179 116 GLU A C 894 O O . GLU A 114 C 0.2074 0.2747 0.3508 -0.0011 0.0067 -0.0180 116 GLU A O 895 C CB . GLU A 114 C 0.2319 0.3159 0.3809 -0.0004 0.0044 -0.0185 116 GLU A CB 896 C CG . GLU A 114 C 0.3077 0.3992 0.4585 0.0004 0.0028 -0.0190 116 GLU A CG 897 C CD . GLU A 114 C 0.3669 0.4665 0.5229 -0.0039 0.0017 -0.0188 116 GLU A CD 898 O OE1 . GLU A 114 C 0.3504 0.4531 0.5090 -0.0057 0.0029 -0.0176 116 GLU A OE1 899 O OE2 . GLU A 114 C 0.4059 0.5083 0.5629 -0.0057 -0.0004 -0.0200 116 GLU A OE2 900 N N . LYS A 115 ? 0.2404 0.3093 0.3793 0.0057 0.0083 -0.0168 117 LYS A N 901 C CA . LYS A 115 ? 0.2512 0.3145 0.3879 0.0053 0.0097 -0.0160 117 LYS A CA 902 C C . LYS A 115 ? 0.2530 0.3217 0.3930 0.0043 0.0108 -0.0147 117 LYS A C 903 O O . LYS A 115 ? 0.2709 0.3461 0.4121 0.0065 0.0115 -0.0138 117 LYS A O 904 C CB . LYS A 115 ? 0.2581 0.3158 0.3886 0.0091 0.0107 -0.0155 117 LYS A CB 905 C CG . LYS A 115 ? 0.2539 0.3045 0.3810 0.0081 0.0117 -0.0148 117 LYS A CG 906 C CD . LYS A 115 ? 0.2751 0.3187 0.3950 0.0111 0.0124 -0.0146 117 LYS A CD 907 C CE . LYS A 115 ? 0.2487 0.2930 0.3650 0.0149 0.0141 -0.0134 117 LYS A CE 908 N NZ . LYS A 115 ? 0.1963 0.2319 0.3042 0.0171 0.0148 -0.0132 117 LYS A NZ 909 N N . VAL A 116 ? 0.2410 0.3072 0.3824 0.0010 0.0110 -0.0145 118 VAL A N 910 C CA . VAL A 116 ? 0.2269 0.2981 0.3717 -0.0007 0.0121 -0.0134 118 VAL A CA 911 C C . VAL A 116 ? 0.2331 0.2990 0.3749 -0.0001 0.0138 -0.0123 118 VAL A C 912 O O . VAL A 116 ? 0.2088 0.2674 0.3480 -0.0011 0.0135 -0.0127 118 VAL A O 913 C CB . VAL A 116 ? 0.2300 0.3026 0.3788 -0.0056 0.0109 -0.0141 118 VAL A CB 914 C CG1 . VAL A 116 ? 0.2325 0.3095 0.3845 -0.0079 0.0121 -0.0128 118 VAL A CG1 915 C CG2 . VAL A 116 ? 0.2407 0.3187 0.3921 -0.0066 0.0091 -0.0152 118 VAL A CG2 916 N N . LYS A 117 ? 0.2195 0.2892 0.3615 0.0016 0.0155 -0.0108 119 LYS A N 917 C CA . LYS A 117 ? 0.2485 0.3126 0.3869 0.0023 0.0172 -0.0097 119 LYS A CA 918 C C . LYS A 117 ? 0.2562 0.3200 0.3975 -0.0017 0.0174 -0.0094 119 LYS A C 919 O O . LYS A 117 ? 0.2754 0.3442 0.4194 -0.0024 0.0187 -0.0082 119 LYS A O 920 C CB . LYS A 117 ? 0.2479 0.3152 0.3844 0.0062 0.0193 -0.0081 119 LYS A CB 921 C CG . LYS A 117 ? 0.2606 0.3206 0.3917 0.0073 0.0210 -0.0071 119 LYS A CG 922 C CD . LYS A 117 ? 0.3137 0.3764 0.4423 0.0116 0.0234 -0.0054 119 LYS A CD 923 C CE . LYS A 117 ? 0.3301 0.3911 0.4539 0.0161 0.0235 -0.0056 119 LYS A CE 924 N NZ . LYS A 117 ? 0.3633 0.4234 0.4820 0.0208 0.0260 -0.0040 119 LYS A NZ 925 N N . ILE A 118 ? 0.2501 0.3079 0.3906 -0.0041 0.0162 -0.0103 120 ILE A N 926 C CA . ILE A 118 ? 0.2470 0.3035 0.3896 -0.0079 0.0163 -0.0102 120 ILE A CA 927 C C . ILE A 118 ? 0.2515 0.3043 0.3919 -0.0079 0.0179 -0.0089 120 ILE A C 928 O O . ILE A 118 ? 0.2654 0.3191 0.4079 -0.0105 0.0185 -0.0084 120 ILE A O 929 C CB . ILE A 118 ? 0.2355 0.2868 0.3777 -0.0100 0.0146 -0.0115 120 ILE A CB 930 C CG1 . ILE A 118 ? 0.2322 0.2770 0.3700 -0.0081 0.0143 -0.0116 120 ILE A CG1 931 C CG2 . ILE A 118 ? 0.2377 0.2926 0.3822 -0.0106 0.0130 -0.0129 120 ILE A CG2 932 C CD1 . ILE A 118 ? 0.2780 0.3176 0.4151 -0.0099 0.0132 -0.0122 120 ILE A CD1 933 N N . LEU A 119 ? 0.2483 0.2963 0.3839 -0.0052 0.0184 -0.0084 121 LEU A N 934 C CA . LEU A 119 ? 0.2674 0.3110 0.4000 -0.0052 0.0197 -0.0072 121 LEU A CA 935 C C . LEU A 119 ? 0.2714 0.3138 0.3994 -0.0015 0.0212 -0.0063 121 LEU A C 936 O O . LEU A 119 ? 0.2724 0.3082 0.3950 -0.0003 0.0210 -0.0063 121 LEU A O 937 C CB . LEU A 119 ? 0.2645 0.3009 0.3944 -0.0066 0.0186 -0.0076 121 LEU A CB 938 C CG . LEU A 119 ? 0.2875 0.3232 0.4205 -0.0099 0.0177 -0.0081 121 LEU A CG 939 C CD1 . LEU A 119 ? 0.3376 0.3677 0.4681 -0.0101 0.0164 -0.0085 121 LEU A CD1 940 C CD2 . LEU A 119 ? 0.3076 0.3433 0.4417 -0.0118 0.0190 -0.0071 121 LEU A CD2 941 N N . PRO A 120 ? 0.2913 0.3400 0.4212 0.0002 0.0228 -0.0054 122 PRO A N 942 C CA . PRO A 120 ? 0.3040 0.3519 0.4291 0.0045 0.0244 -0.0044 122 PRO A CA 943 C C . PRO A 120 ? 0.3158 0.3553 0.4346 0.0051 0.0252 -0.0037 122 PRO A C 944 O O . PRO A 120 ? 0.3225 0.3607 0.4422 0.0028 0.0257 -0.0031 122 PRO A O 945 C CB . PRO A 120 ? 0.3103 0.3671 0.4396 0.0055 0.0263 -0.0030 122 PRO A CB 946 C CG . PRO A 120 ? 0.3182 0.3814 0.4545 0.0017 0.0251 -0.0036 122 PRO A CG 947 C CD . PRO A 120 ? 0.2871 0.3440 0.4233 -0.0019 0.0233 -0.0049 122 PRO A CD 948 N N . LYS A 121 ? 0.3363 0.3698 0.4484 0.0077 0.0252 -0.0039 123 LYS A N 949 C CA . LYS A 121 ? 0.3689 0.3935 0.4736 0.0083 0.0256 -0.0034 123 LYS A CA 950 C C . LYS A 121 ? 0.3783 0.4027 0.4812 0.0094 0.0279 -0.0018 123 LYS A C 951 O O . LYS A 121 ? 0.3671 0.3859 0.4668 0.0079 0.0279 -0.0014 123 LYS A O 952 C CB . LYS A 121 ? 0.3796 0.3990 0.4768 0.0117 0.0258 -0.0036 123 LYS A CB 953 C CG . LYS A 121 ? 0.4267 0.4360 0.5163 0.0107 0.0248 -0.0039 123 LYS A CG 954 C CD . LYS A 121 ? 0.4757 0.4792 0.5572 0.0139 0.0252 -0.0041 123 LYS A CD 955 C CE . LYS A 121 ? 0.4727 0.4809 0.5571 0.0156 0.0247 -0.0049 123 LYS A CE 956 N NZ . LYS A 121 ? 0.4948 0.4951 0.5708 0.0172 0.0243 -0.0055 123 LYS A NZ 957 N N . ASP A 122 ? 0.3991 0.4301 0.5041 0.0122 0.0299 -0.0008 125 ASP A N 958 C CA . ASP A 122 ? 0.4257 0.4573 0.5289 0.0140 0.0326 0.0008 125 ASP A CA 959 C C . ASP A 122 ? 0.4294 0.4623 0.5367 0.0102 0.0327 0.0013 125 ASP A C 960 O O . ASP A 122 ? 0.4464 0.4775 0.5511 0.0112 0.0347 0.0027 125 ASP A O 961 C CB . ASP A 122 ? 0.4303 0.4702 0.5354 0.0181 0.0348 0.0021 125 ASP A CB 962 C CG . ASP A 122 ? 0.4594 0.5114 0.5749 0.0158 0.0345 0.0023 125 ASP A CG 963 O OD1 . ASP A 122 ? 0.4975 0.5511 0.6180 0.0116 0.0323 0.0009 125 ASP A OD1 964 O OD2 . ASP A 122 ? 0.5339 0.5940 0.6522 0.0181 0.0366 0.0039 125 ASP A OD2 965 N N . ARG A 123 ? 0.4263 0.4617 0.5396 0.0062 0.0308 0.0002 126 ARG A N 966 C CA . ARG A 123 ? 0.4250 0.4613 0.5419 0.0026 0.0309 0.0007 126 ARG A CA 967 C C . ARG A 123 ? 0.4213 0.4487 0.5336 0.0009 0.0300 0.0005 126 ARG A C 968 O O . ARG A 123 ? 0.4116 0.4385 0.5255 -0.0013 0.0305 0.0011 126 ARG A O 969 C CB . ARG A 123 ? 0.4330 0.4754 0.5575 -0.0008 0.0295 -0.0002 126 ARG A CB 970 C CG . ARG A 123 ? 0.4646 0.5178 0.5950 -0.0004 0.0305 0.0003 126 ARG A CG 971 C CD . ARG A 123 ? 0.5306 0.5882 0.6636 -0.0015 0.0328 0.0021 126 ARG A CD 972 N NE . ARG A 123 ? 0.5901 0.6587 0.7283 -0.0006 0.0339 0.0030 126 ARG A NE 973 C CZ . ARG A 123 ? 0.5862 0.6619 0.7287 -0.0023 0.0356 0.0046 126 ARG A CZ 974 N NH1 . ARG A 123 ? 0.6036 0.6761 0.7458 -0.0050 0.0366 0.0053 126 ARG A NH1 975 N NH2 . ARG A 123 ? 0.5938 0.6804 0.7411 -0.0014 0.0363 0.0055 126 ARG A NH2 976 N N . TRP A 124 ? 0.4128 0.4335 0.5194 0.0019 0.0287 0.0000 127 TRP A N 977 C CA . TRP A 124 ? 0.4101 0.4229 0.5118 0.0005 0.0278 0.0000 127 TRP A CA 978 C C . TRP A 124 ? 0.4435 0.4518 0.5386 0.0029 0.0298 0.0013 127 TRP A C 979 O O . TRP A 124 ? 0.4435 0.4456 0.5311 0.0049 0.0298 0.0013 127 TRP A O 980 C CB . TRP A 124 ? 0.4023 0.4101 0.5002 0.0002 0.0255 -0.0010 127 TRP A CB 981 C CG . TRP A 124 ? 0.3288 0.3401 0.4323 -0.0017 0.0235 -0.0022 127 TRP A CG 982 C CD1 . TRP A 124 ? 0.3218 0.3353 0.4263 -0.0006 0.0227 -0.0032 127 TRP A CD1 983 C CD2 . TRP A 124 ? 0.3282 0.3405 0.4360 -0.0047 0.0222 -0.0026 127 TRP A CD2 984 N NE1 . TRP A 124 ? 0.2828 0.2988 0.3922 -0.0028 0.0210 -0.0042 127 TRP A NE1 985 C CE2 . TRP A 124 ? 0.3001 0.3152 0.4115 -0.0053 0.0207 -0.0038 127 TRP A CE2 986 C CE3 . TRP A 124 ? 0.3158 0.3266 0.4245 -0.0066 0.0223 -0.0019 127 TRP A CE3 987 C CZ2 . TRP A 124 ? 0.3046 0.3207 0.4199 -0.0076 0.0194 -0.0043 127 TRP A CZ2 988 C CZ3 . TRP A 124 ? 0.3074 0.3191 0.4200 -0.0089 0.0210 -0.0023 127 TRP A CZ3 989 C CH2 . TRP A 124 ? 0.3141 0.3284 0.4298 -0.0093 0.0196 -0.0036 127 TRP A CH2 990 N N . THR A 125 ? 0.4561 0.4669 0.5533 0.0026 0.0317 0.0025 128 THR A N 991 C CA . THR A 125 ? 0.4819 0.4890 0.5730 0.0052 0.0341 0.0039 128 THR A CA 992 C C . THR A 125 ? 0.4901 0.4881 0.5743 0.0042 0.0332 0.0042 128 THR A C 993 O O . THR A 125 ? 0.5116 0.5037 0.5881 0.0065 0.0345 0.0049 128 THR A O 994 C CB . THR A 125 ? 0.4749 0.4888 0.5707 0.0056 0.0367 0.0053 128 THR A CB 995 O OG1 . THR A 125 ? 0.4832 0.4993 0.5846 0.0016 0.0360 0.0052 128 THR A OG1 996 C CG2 . THR A 125 ? 0.4913 0.5141 0.5921 0.0075 0.0378 0.0054 128 THR A CG2 997 N N . GLN A 126 ? 0.4883 0.4852 0.5750 0.0008 0.0311 0.0036 129 GLN A N 998 C CA . GLN A 126 ? 0.4891 0.4785 0.5700 -0.0003 0.0301 0.0040 129 GLN A CA 999 C C . GLN A 126 ? 0.4814 0.4654 0.5572 -0.0010 0.0275 0.0032 129 GLN A C 1000 O O . GLN A 126 ? 0.4848 0.4635 0.5563 -0.0025 0.0260 0.0035 129 GLN A O 1001 C CB . GLN A 126 ? 0.4916 0.4825 0.5770 -0.0032 0.0294 0.0043 129 GLN A CB 1002 C CG . GLN A 126 ? 0.5285 0.5235 0.6181 -0.0034 0.0319 0.0053 129 GLN A CG 1003 C CD . GLN A 126 ? 0.5847 0.5783 0.6761 -0.0061 0.0312 0.0057 129 GLN A CD 1004 O OE1 . GLN A 126 ? 0.6082 0.6055 0.7055 -0.0081 0.0305 0.0052 129 GLN A OE1 1005 N NE2 . GLN A 126 ? 0.6118 0.5996 0.6976 -0.0059 0.0314 0.0067 129 GLN A NE2 1006 N N . HIS A 127 ? 0.4698 0.4552 0.5459 0.0000 0.0268 0.0022 130 HIS A N 1007 C CA . HIS A 127 ? 0.4564 0.4370 0.5280 -0.0010 0.0244 0.0014 130 HIS A CA 1008 C C . HIS A 127 ? 0.4531 0.4309 0.5193 0.0016 0.0251 0.0010 130 HIS A C 1009 O O . HIS A 127 ? 0.4545 0.4366 0.5232 0.0043 0.0270 0.0010 130 HIS A O 1010 C CB . HIS A 127 ? 0.4402 0.4254 0.5186 -0.0034 0.0222 0.0005 130 HIS A CB 1011 C CG . HIS A 127 ? 0.4251 0.4121 0.5079 -0.0058 0.0213 0.0009 130 HIS A CG 1012 N ND1 . HIS A 127 ? 0.4372 0.4292 0.5263 -0.0062 0.0226 0.0011 130 HIS A ND1 1013 C CD2 . HIS A 127 ? 0.4323 0.4166 0.5134 -0.0080 0.0194 0.0013 130 HIS A CD2 1014 C CE1 . HIS A 127 ? 0.4003 0.3918 0.4911 -0.0081 0.0216 0.0016 130 HIS A CE1 1015 N NE2 . HIS A 127 ? 0.4377 0.4251 0.5240 -0.0091 0.0196 0.0018 130 HIS A NE2 1016 N N . THR A 128 ? 0.4514 0.4220 0.5100 0.0008 0.0236 0.0006 131 THR A N 1017 C CA . THR A 128 ? 0.4509 0.4175 0.5034 0.0031 0.0240 0.0001 131 THR A CA 1018 C C . THR A 128 ? 0.4362 0.4083 0.4949 0.0025 0.0227 -0.0009 131 THR A C 1019 O O . THR A 128 ? 0.4166 0.3913 0.4801 -0.0005 0.0205 -0.0014 131 THR A O 1020 C CB . THR A 128 ? 0.4674 0.4236 0.5089 0.0018 0.0227 0.0002 131 THR A CB 1021 O OG1 . THR A 128 ? 0.5022 0.4534 0.5381 0.0022 0.0237 0.0012 131 THR A OG1 1022 C CG2 . THR A 128 ? 0.4889 0.4392 0.5223 0.0045 0.0235 -0.0002 131 THR A CG2 1023 N N . THR A 129 ? 0.4351 0.4088 0.4934 0.0057 0.0240 -0.0013 132 THR A N 1024 C CA . THR A 129 ? 0.4293 0.4082 0.4933 0.0054 0.0229 -0.0024 132 THR A CA 1025 C C . THR A 129 ? 0.4367 0.4103 0.4935 0.0073 0.0228 -0.0030 132 THR A C 1026 O O . THR A 129 ? 0.4359 0.4131 0.4964 0.0075 0.0221 -0.0038 132 THR A O 1027 C CB . THR A 129 ? 0.4257 0.4144 0.4985 0.0072 0.0243 -0.0024 132 THR A CB 1028 O OG1 . THR A 129 ? 0.4233 0.4120 0.4926 0.0114 0.0269 -0.0016 132 THR A OG1 1029 C CG2 . THR A 129 ? 0.4144 0.4084 0.4947 0.0048 0.0242 -0.0020 132 THR A CG2 1030 N N . THR A 130 ? 0.4473 0.4116 0.4934 0.0086 0.0236 -0.0025 133 THR A N 1031 C CA . THR A 130 ? 0.4568 0.4143 0.4942 0.0108 0.0241 -0.0029 133 THR A CA 1032 C C . THR A 130 ? 0.4629 0.4136 0.4949 0.0070 0.0215 -0.0035 133 THR A C 1033 O O . THR A 130 ? 0.4753 0.4194 0.4995 0.0081 0.0216 -0.0040 133 THR A O 1034 C CB . THR A 130 ? 0.4776 0.4273 0.5045 0.0148 0.0267 -0.0020 133 THR A CB 1035 O OG1 . THR A 130 ? 0.4948 0.4391 0.5172 0.0126 0.0263 -0.0014 133 THR A OG1 1036 C CG2 . THR A 130 ? 0.4814 0.4389 0.5134 0.0195 0.0295 -0.0012 133 THR A CG2 1037 N N . GLY A 131 ? 0.4464 0.3997 0.4833 0.0025 0.0192 -0.0035 134 GLY A N 1038 C CA . GLY A 131 ? 0.4236 0.3724 0.4569 -0.0017 0.0166 -0.0038 134 GLY A CA 1039 C C . GLY A 131 ? 0.4049 0.3550 0.4395 -0.0018 0.0158 -0.0047 134 GLY A C 1040 O O . GLY A 131 ? 0.3774 0.3358 0.4208 -0.0005 0.0160 -0.0052 134 GLY A O 1041 N N . GLY A 132 ? 0.4003 0.3417 0.4253 -0.0036 0.0148 -0.0048 135 GLY A N 1042 C CA . GLY A 132 ? 0.3756 0.3165 0.4000 -0.0046 0.0138 -0.0055 135 GLY A CA 1043 C C . GLY A 132 ? 0.3791 0.3133 0.3965 -0.0096 0.0116 -0.0052 135 GLY A C 1044 O O . GLY A 132 ? 0.3868 0.3187 0.4018 -0.0127 0.0103 -0.0045 135 GLY A O 1045 N N . SER A 133 ? 0.3570 0.2881 0.3709 -0.0104 0.0110 -0.0057 136 SER A N 1046 C CA . SER A 133 ? 0.3516 0.2780 0.3602 -0.0157 0.0088 -0.0054 136 SER A CA 1047 C C . SER A 133 ? 0.3630 0.2810 0.3621 -0.0147 0.0095 -0.0060 136 SER A C 1048 O O . SER A 133 ? 0.3341 0.2540 0.3353 -0.0106 0.0111 -0.0067 136 SER A O 1049 C CB . SER A 133 ? 0.3286 0.2652 0.3481 -0.0187 0.0068 -0.0052 136 SER A CB 1050 O OG . SER A 133 ? 0.3266 0.2600 0.3417 -0.0239 0.0047 -0.0046 136 SER A OG 1051 N N . ARG A 134 ? 0.3816 0.2899 0.3699 -0.0189 0.0082 -0.0056 137 ARG A N 1052 C CA . ARG A 134 ? 0.4057 0.3051 0.3843 -0.0197 0.0084 -0.0060 137 ARG A CA 1053 C C . ARG A 134 ? 0.3971 0.3038 0.3834 -0.0207 0.0076 -0.0064 137 ARG A C 1054 O O . ARG A 134 ? 0.3890 0.2904 0.3697 -0.0194 0.0084 -0.0069 137 ARG A O 1055 C CB . ARG A 134 ? 0.4369 0.3265 0.4043 -0.0257 0.0064 -0.0054 137 ARG A CB 1056 C CG . ARG A 134 ? 0.5007 0.3806 0.4577 -0.0250 0.0072 -0.0052 137 ARG A CG 1057 C CD . ARG A 134 ? 0.6241 0.4876 0.5636 -0.0245 0.0083 -0.0055 137 ARG A CD 1058 N NE . ARG A 134 ? 0.7174 0.5796 0.6560 -0.0195 0.0106 -0.0063 137 ARG A NE 1059 C CZ . ARG A 134 ? 0.7389 0.5930 0.6688 -0.0133 0.0135 -0.0067 137 ARG A CZ 1060 N NH1 . ARG A 134 ? 0.7263 0.5718 0.6469 -0.0115 0.0147 -0.0064 137 ARG A NH1 1061 N NH2 . ARG A 134 ? 0.7590 0.6134 0.6891 -0.0089 0.0152 -0.0073 137 ARG A NH2 1062 N N . ALA A 135 ? 0.3648 0.2832 0.3635 -0.0228 0.0061 -0.0059 138 ALA A N 1063 C CA . ALA A 135 ? 0.3708 0.2966 0.3773 -0.0234 0.0055 -0.0061 138 ALA A CA 1064 C C . ALA A 135 ? 0.3608 0.2903 0.3720 -0.0174 0.0075 -0.0072 138 ALA A C 1065 O O . ALA A 135 ? 0.3734 0.3055 0.3874 -0.0171 0.0075 -0.0076 138 ALA A O 1066 C CB . ALA A 135 ? 0.3439 0.2815 0.3626 -0.0264 0.0036 -0.0053 138 ALA A CB 1067 N N . CYS A 136 ? 0.3512 0.2818 0.3639 -0.0129 0.0092 -0.0076 139 CYS A N 1068 C CA . CYS A 136 ? 0.3538 0.2883 0.3706 -0.0073 0.0111 -0.0084 139 CYS A CA 1069 C C . CYS A 136 ? 0.3649 0.2900 0.3708 -0.0030 0.0133 -0.0086 139 CYS A C 1070 O O . CYS A 136 ? 0.3523 0.2813 0.3614 0.0017 0.0151 -0.0087 139 CYS A O 1071 C CB . CYS A 136 ? 0.3319 0.2771 0.3604 -0.0054 0.0114 -0.0084 139 CYS A CB 1072 S SG . CYS A 136 ? 0.3791 0.3332 0.4182 -0.0102 0.0091 -0.0078 139 CYS A SG 1073 N N . ALA A 137 ? 0.3730 0.2860 0.3659 -0.0049 0.0133 -0.0084 140 ALA A N 1074 C CA . ALA A 137 ? 0.4037 0.3061 0.3844 -0.0007 0.0155 -0.0083 140 ALA A CA 1075 C C . ALA A 137 ? 0.4061 0.3095 0.3865 0.0054 0.0176 -0.0089 140 ALA A C 1076 O O . ALA A 137 ? 0.4176 0.3242 0.4015 0.0052 0.0171 -0.0094 140 ALA A O 1077 C CB . ALA A 137 ? 0.4070 0.2947 0.3724 -0.0042 0.0150 -0.0081 140 ALA A CB 1078 N N . VAL A 138 ? 0.4195 0.3201 0.3954 0.0110 0.0201 -0.0086 141 VAL A N 1079 C CA . VAL A 138 ? 0.4187 0.3197 0.3927 0.0176 0.0223 -0.0088 141 VAL A CA 1080 C C . VAL A 138 ? 0.4323 0.3195 0.3904 0.0215 0.0247 -0.0083 141 VAL A C 1081 O O . VAL A 138 ? 0.4293 0.3135 0.3840 0.0221 0.0256 -0.0076 141 VAL A O 1082 C CB . VAL A 138 ? 0.4131 0.3281 0.4002 0.0216 0.0232 -0.0086 141 VAL A CB 1083 C CG1 . VAL A 138 ? 0.4396 0.3556 0.4242 0.0290 0.0257 -0.0085 141 VAL A CG1 1084 C CG2 . VAL A 138 ? 0.4023 0.3293 0.4035 0.0179 0.0210 -0.0092 141 VAL A CG2 1085 N N . SER A 139 ? 0.4427 0.3207 0.3904 0.0239 0.0258 -0.0085 142 SER A N 1086 C CA . SER A 139 ? 0.4708 0.3338 0.4015 0.0277 0.0282 -0.0080 142 SER A CA 1087 C C . SER A 139 ? 0.4867 0.3394 0.4084 0.0230 0.0273 -0.0077 142 SER A C 1088 O O . SER A 139 ? 0.4905 0.3372 0.4048 0.0262 0.0292 -0.0070 142 SER A O 1089 C CB . SER A 139 ? 0.4709 0.3385 0.4028 0.0361 0.0312 -0.0072 142 SER A CB 1090 O OG . SER A 139 ? 0.4588 0.3361 0.3989 0.0399 0.0315 -0.0075 142 SER A OG 1091 N N . GLY A 140 ? 0.4899 0.3414 0.4128 0.0152 0.0244 -0.0081 143 GLY A N 1092 C CA . GLY A 140 ? 0.5084 0.3499 0.4220 0.0097 0.0231 -0.0078 143 GLY A CA 1093 C C . GLY A 140 ? 0.5057 0.3538 0.4266 0.0084 0.0224 -0.0073 143 GLY A C 1094 O O . GLY A 140 ? 0.5250 0.3650 0.4381 0.0041 0.0213 -0.0070 143 GLY A O 1095 N N . ASN A 141 ? 0.4785 0.3409 0.4136 0.0117 0.0231 -0.0072 144 ASN A N 1096 C CA . ASN A 141 ? 0.4749 0.3434 0.4169 0.0103 0.0225 -0.0066 144 ASN A CA 1097 C C . ASN A 141 ? 0.4394 0.3230 0.3984 0.0065 0.0202 -0.0068 144 ASN A C 1098 O O . ASN A 141 ? 0.4188 0.3113 0.3869 0.0079 0.0201 -0.0073 144 ASN A O 1099 C CB . ASN A 141 ? 0.4875 0.3586 0.4300 0.0174 0.0257 -0.0060 144 ASN A CB 1100 C CG . ASN A 141 ? 0.5602 0.4152 0.4847 0.0210 0.0280 -0.0055 144 ASN A CG 1101 O OD1 . ASN A 141 ? 0.6366 0.4810 0.5511 0.0170 0.0271 -0.0054 144 ASN A OD1 1102 N ND2 . ASN A 141 ? 0.5870 0.4404 0.5072 0.0284 0.0311 -0.0051 144 ASN A ND2 1103 N N . PRO A 142 ? 0.4232 0.3093 0.3858 0.0020 0.0184 -0.0064 145 PRO A N 1104 C CA . PRO A 142 ? 0.3905 0.2904 0.3686 -0.0008 0.0166 -0.0064 145 PRO A CA 1105 C C . PRO A 142 ? 0.3616 0.2732 0.3514 0.0040 0.0182 -0.0066 145 PRO A C 1106 O O . PRO A 142 ? 0.3538 0.2656 0.3425 0.0089 0.0205 -0.0062 145 PRO A O 1107 C CB . PRO A 142 ? 0.3966 0.2959 0.3746 -0.0040 0.0155 -0.0057 145 PRO A CB 1108 C CG . PRO A 142 ? 0.4206 0.3044 0.3819 -0.0061 0.0153 -0.0055 145 PRO A CG 1109 C CD . PRO A 142 ? 0.4418 0.3178 0.3939 -0.0002 0.0181 -0.0058 145 PRO A CD 1110 N N . SER A 143 ? 0.3385 0.2599 0.3393 0.0028 0.0169 -0.0071 146 SER A N 1111 C CA . SER A 143 ? 0.3171 0.2500 0.3294 0.0063 0.0180 -0.0073 146 SER A CA 1112 C C . SER A 143 ? 0.2921 0.2353 0.3170 0.0025 0.0159 -0.0075 146 SER A C 1113 O O . SER A 143 ? 0.2826 0.2247 0.3075 -0.0021 0.0139 -0.0072 146 SER A O 1114 C CB . SER A 143 ? 0.3237 0.2567 0.3342 0.0112 0.0196 -0.0078 146 SER A CB 1115 O OG . SER A 143 ? 0.3708 0.3141 0.3907 0.0149 0.0208 -0.0077 146 SER A OG 1116 N N . PHE A 144 ? 0.2667 0.2196 0.3015 0.0046 0.0162 -0.0080 147 PHE A N 1117 C CA . PHE A 144 ? 0.2607 0.2228 0.3068 0.0018 0.0146 -0.0082 147 PHE A CA 1118 C C . PHE A 144 ? 0.2432 0.2133 0.2973 0.0040 0.0148 -0.0090 147 PHE A C 1119 O O . PHE A 144 ? 0.2294 0.2003 0.2823 0.0082 0.0163 -0.0092 147 PHE A O 1120 C CB . PHE A 144 ? 0.2524 0.2188 0.3039 0.0009 0.0147 -0.0075 147 PHE A CB 1121 C CG . PHE A 144 ? 0.2598 0.2318 0.3191 -0.0029 0.0128 -0.0073 147 PHE A CG 1122 C CD1 . PHE A 144 ? 0.2242 0.1932 0.2808 -0.0068 0.0109 -0.0070 147 PHE A CD1 1123 C CD2 . PHE A 144 ? 0.2092 0.1894 0.2781 -0.0026 0.0130 -0.0074 147 PHE A CD2 1124 C CE1 . PHE A 144 ? 0.2627 0.2374 0.3265 -0.0098 0.0093 -0.0065 147 PHE A CE1 1125 C CE2 . PHE A 144 ? 0.2174 0.2019 0.2925 -0.0057 0.0114 -0.0071 147 PHE A CE2 1126 C CZ . PHE A 144 ? 0.2232 0.2053 0.2959 -0.0089 0.0096 -0.0066 147 PHE A CZ 1127 N N . PHE A 145 ? 0.2249 0.2011 0.2869 0.0013 0.0132 -0.0093 148 PHE A N 1128 C CA . PHE A 145 ? 0.2227 0.2067 0.2929 0.0028 0.0131 -0.0101 148 PHE A CA 1129 C C . PHE A 145 ? 0.2069 0.1959 0.2806 0.0062 0.0147 -0.0101 148 PHE A C 1130 O O . PHE A 145 ? 0.2145 0.2047 0.2898 0.0058 0.0154 -0.0094 148 PHE A O 1131 C CB . PHE A 145 ? 0.2083 0.1981 0.2867 -0.0002 0.0116 -0.0101 148 PHE A CB 1132 C CG . PHE A 145 ? 0.2234 0.2106 0.2999 -0.0036 0.0101 -0.0098 148 PHE A CG 1133 C CD1 . PHE A 145 ? 0.1988 0.1856 0.2746 -0.0034 0.0096 -0.0104 148 PHE A CD1 1134 C CD2 . PHE A 145 ? 0.2320 0.2177 0.3078 -0.0068 0.0091 -0.0088 148 PHE A CD2 1135 C CE1 . PHE A 145 ? 0.2375 0.2230 0.3122 -0.0066 0.0082 -0.0099 148 PHE A CE1 1136 C CE2 . PHE A 145 ? 0.2338 0.2186 0.3086 -0.0101 0.0075 -0.0082 148 PHE A CE2 1137 C CZ . PHE A 145 ? 0.2434 0.2282 0.3177 -0.0100 0.0072 -0.0088 148 PHE A CZ 1138 N N . ARG A 146 ? 0.2127 0.2046 0.2874 0.0094 0.0154 -0.0106 149 ARG A N 1139 C CA . ARG A 146 ? 0.2343 0.2314 0.3116 0.0129 0.0170 -0.0103 149 ARG A CA 1140 C C . ARG A 146 ? 0.2272 0.2329 0.3143 0.0112 0.0166 -0.0104 149 ARG A C 1141 O O . ARG A 146 ? 0.2162 0.2261 0.3058 0.0127 0.0180 -0.0098 149 ARG A O 1142 C CB . ARG A 146 ? 0.2364 0.2358 0.3129 0.0167 0.0176 -0.0108 149 ARG A CB 1143 C CG . ARG A 146 ? 0.2956 0.2881 0.3620 0.0209 0.0194 -0.0103 149 ARG A CG 1144 C CD . ARG A 146 ? 0.3365 0.3183 0.3937 0.0194 0.0189 -0.0104 149 ARG A CD 1145 N NE . ARG A 146 ? 0.3788 0.3535 0.4258 0.0238 0.0207 -0.0100 149 ARG A NE 1146 C CZ . ARG A 146 ? 0.4399 0.4063 0.4778 0.0250 0.0221 -0.0092 149 ARG A CZ 1147 N NH1 . ARG A 146 ? 0.4529 0.4172 0.4906 0.0219 0.0218 -0.0087 149 ARG A NH1 1148 N NH2 . ARG A 146 ? 0.4804 0.4400 0.5085 0.0295 0.0239 -0.0089 149 ARG A NH2 1149 N N . ASN A 147 ? 0.2132 0.2214 0.3055 0.0082 0.0150 -0.0111 150 ASN A N 1150 C CA . ASN A 147 ? 0.2107 0.2262 0.3116 0.0066 0.0146 -0.0113 150 ASN A CA 1151 C C . ASN A 147 ? 0.2150 0.2296 0.3177 0.0037 0.0144 -0.0107 150 ASN A C 1152 O O . ASN A 147 ? 0.1999 0.2194 0.3087 0.0023 0.0143 -0.0107 150 ASN A O 1153 C CB . ASN A 147 ? 0.1972 0.2161 0.3027 0.0056 0.0131 -0.0125 150 ASN A CB 1154 C CG . ASN A 147 ? 0.1820 0.2029 0.2864 0.0087 0.0133 -0.0131 150 ASN A CG 1155 O OD1 . ASN A 147 ? 0.2333 0.2565 0.3365 0.0117 0.0146 -0.0126 150 ASN A OD1 1156 N ND2 . ASN A 147 ? 0.1498 0.1705 0.2547 0.0084 0.0121 -0.0140 150 ASN A ND2 1157 N N . MET A 148 ? 0.2202 0.2284 0.3172 0.0028 0.0143 -0.0100 151 MET A N 1158 C CA . MET A 148 ? 0.2256 0.2324 0.3236 0.0000 0.0138 -0.0093 151 MET A CA 1159 C C . MET A 148 ? 0.2359 0.2387 0.3288 0.0008 0.0151 -0.0083 151 MET A C 1160 O O . MET A 148 ? 0.2508 0.2503 0.3380 0.0034 0.0162 -0.0082 151 MET A O 1161 C CB . MET A 148 ? 0.2187 0.2219 0.3145 -0.0024 0.0122 -0.0092 151 MET A CB 1162 C CG . MET A 148 ? 0.2391 0.2449 0.3381 -0.0026 0.0111 -0.0101 151 MET A CG 1163 S SD . MET A 148 ? 0.2225 0.2354 0.3306 -0.0032 0.0109 -0.0107 151 MET A SD 1164 C CE . MET A 148 ? 0.1918 0.2037 0.3012 -0.0059 0.0102 -0.0097 151 MET A CE 1165 N N . VAL A 149 ? 0.2324 0.2350 0.3268 -0.0010 0.0150 -0.0076 152 VAL A N 1166 C CA . VAL A 149 ? 0.2385 0.2374 0.3283 -0.0005 0.0162 -0.0066 152 VAL A CA 1167 C C . VAL A 149 ? 0.2442 0.2388 0.3312 -0.0034 0.0149 -0.0059 152 VAL A C 1168 O O . VAL A 149 ? 0.2231 0.2205 0.3150 -0.0055 0.0139 -0.0058 152 VAL A O 1169 C CB . VAL A 149 ? 0.2418 0.2459 0.3367 0.0000 0.0177 -0.0061 152 VAL A CB 1170 C CG1 . VAL A 149 ? 0.2669 0.2666 0.3563 0.0012 0.0192 -0.0050 152 VAL A CG1 1171 C CG2 . VAL A 149 ? 0.2377 0.2480 0.3368 0.0023 0.0186 -0.0067 152 VAL A CG2 1172 N N . TRP A 150 ? 0.2523 0.2397 0.3309 -0.0033 0.0149 -0.0054 153 TRP A N 1173 C CA . TRP A 150 ? 0.2747 0.2580 0.3498 -0.0062 0.0135 -0.0047 153 TRP A CA 1174 C C . TRP A 150 ? 0.2940 0.2758 0.3675 -0.0059 0.0146 -0.0037 153 TRP A C 1175 O O . TRP A 150 ? 0.3122 0.2886 0.3787 -0.0041 0.0159 -0.0034 153 TRP A O 1176 C CB . TRP A 150 ? 0.2746 0.2503 0.3405 -0.0070 0.0127 -0.0047 153 TRP A CB 1177 C CG . TRP A 150 ? 0.2570 0.2301 0.3204 -0.0108 0.0105 -0.0039 153 TRP A CG 1178 C CD1 . TRP A 150 ? 0.2754 0.2509 0.3420 -0.0129 0.0096 -0.0030 153 TRP A CD1 1179 C CD2 . TRP A 150 ? 0.2863 0.2540 0.3429 -0.0132 0.0090 -0.0038 153 TRP A CD2 1180 N NE1 . TRP A 150 ? 0.2864 0.2593 0.3491 -0.0163 0.0074 -0.0023 153 TRP A NE1 1181 C CE2 . TRP A 150 ? 0.2682 0.2362 0.3248 -0.0168 0.0071 -0.0028 153 TRP A CE2 1182 C CE3 . TRP A 150 ? 0.3068 0.2694 0.3571 -0.0126 0.0092 -0.0045 153 TRP A CE3 1183 C CZ2 . TRP A 150 ? 0.2773 0.2416 0.3284 -0.0203 0.0051 -0.0023 153 TRP A CZ2 1184 C CZ3 . TRP A 150 ? 0.2939 0.2515 0.3380 -0.0162 0.0074 -0.0041 153 TRP A CZ3 1185 C CH2 . TRP A 150 ? 0.2883 0.2472 0.3332 -0.0202 0.0053 -0.0030 153 TRP A CH2 1186 N N . LEU A 151 ? 0.3003 0.2861 0.3796 -0.0073 0.0143 -0.0033 154 LEU A N 1187 C CA . LEU A 151 ? 0.3189 0.3034 0.3971 -0.0070 0.0155 -0.0024 154 LEU A CA 1188 C C . LEU A 151 ? 0.3316 0.3099 0.4029 -0.0091 0.0141 -0.0015 154 LEU A C 1189 O O . LEU A 151 ? 0.3136 0.2926 0.3860 -0.0116 0.0120 -0.0013 154 LEU A O 1190 C CB . LEU A 151 ? 0.3219 0.3121 0.4080 -0.0079 0.0157 -0.0021 154 LEU A CB 1191 C CG . LEU A 151 ? 0.3396 0.3357 0.4320 -0.0064 0.0173 -0.0026 154 LEU A CG 1192 C CD1 . LEU A 151 ? 0.3691 0.3688 0.4649 -0.0057 0.0168 -0.0038 154 LEU A CD1 1193 C CD2 . LEU A 151 ? 0.3841 0.3835 0.4822 -0.0079 0.0173 -0.0023 154 LEU A CD2 1194 N N . THR A 152 ? 0.3557 0.3282 0.4198 -0.0079 0.0153 -0.0010 155 THR A N 1195 C CA . THR A 152 ? 0.3870 0.3533 0.4441 -0.0101 0.0139 -0.0002 155 THR A CA 1196 C C . THR A 152 ? 0.4180 0.3821 0.4727 -0.0091 0.0155 0.0007 155 THR A C 1197 O O . THR A 152 ? 0.4124 0.3795 0.4705 -0.0067 0.0177 0.0007 155 THR A O 1198 C CB . THR A 152 ? 0.3882 0.3465 0.4352 -0.0106 0.0132 -0.0004 155 THR A CB 1199 O OG1 . THR A 152 ? 0.3829 0.3377 0.4253 -0.0069 0.0157 -0.0008 155 THR A OG1 1200 C CG2 . THR A 152 ? 0.3814 0.3417 0.4305 -0.0124 0.0114 -0.0011 155 THR A CG2 1201 N N . GLU A 153 ? 0.4666 0.4257 0.5155 -0.0112 0.0141 0.0015 156 GLU A N 1202 C CA . GLU A 153 ? 0.5071 0.4621 0.5515 -0.0105 0.0152 0.0024 156 GLU A CA 1203 C C . GLU A 153 ? 0.5157 0.4673 0.5557 -0.0067 0.0184 0.0024 156 GLU A C 1204 O O . GLU A 153 ? 0.5208 0.4686 0.5556 -0.0051 0.0190 0.0018 156 GLU A O 1205 C CB . GLU A 153 ? 0.5243 0.4722 0.5598 -0.0134 0.0129 0.0030 156 GLU A CB 1206 C CG . GLU A 153 ? 0.5766 0.5167 0.6030 -0.0124 0.0140 0.0037 156 GLU A CG 1207 C CD . GLU A 153 ? 0.6181 0.5497 0.6343 -0.0105 0.0154 0.0032 156 GLU A CD 1208 O OE1 . GLU A 153 ? 0.6519 0.5786 0.6621 -0.0125 0.0136 0.0028 156 GLU A OE1 1209 O OE2 . GLU A 153 ? 0.6668 0.5963 0.6806 -0.0069 0.0183 0.0035 156 GLU A OE2 1210 N N . LYS A 154 ? 0.5392 0.4923 0.5810 -0.0051 0.0204 0.0032 157 LYS A N 1211 C CA . LYS A 154 ? 0.5610 0.5106 0.5975 -0.0014 0.0235 0.0036 157 LYS A CA 1212 C C . LYS A 154 ? 0.5798 0.5244 0.6109 -0.0013 0.0243 0.0047 157 LYS A C 1213 O O . LYS A 154 ? 0.5775 0.5259 0.6140 -0.0026 0.0242 0.0054 157 LYS A O 1214 C CB . LYS A 154 ? 0.5531 0.5109 0.5980 0.0011 0.0260 0.0035 157 LYS A CB 1215 C CG . LYS A 154 ? 0.5740 0.5298 0.6142 0.0054 0.0293 0.0042 157 LYS A CG 1216 C CD . LYS A 154 ? 0.6014 0.5669 0.6506 0.0074 0.0314 0.0043 157 LYS A CD 1217 C CE . LYS A 154 ? 0.6438 0.6083 0.6884 0.0122 0.0347 0.0052 157 LYS A CE 1218 N NZ . LYS A 154 ? 0.6741 0.6481 0.7274 0.0132 0.0370 0.0061 157 LYS A NZ 1219 N N . GLY A 155 ? 0.6030 0.5384 0.6228 0.0001 0.0252 0.0050 158 GLY A N 1220 C CA . GLY A 155 ? 0.6229 0.5520 0.6357 0.0002 0.0258 0.0061 158 GLY A CA 1221 C C . GLY A 155 ? 0.6326 0.5614 0.6462 -0.0039 0.0226 0.0064 158 GLY A C 1222 O O . GLY A 155 ? 0.6358 0.5660 0.6515 -0.0043 0.0230 0.0073 158 GLY A O 1223 N N . SER A 156 ? 0.6349 0.5625 0.6471 -0.0070 0.0195 0.0057 159 SER A N 1224 C CA . SER A 156 ? 0.6323 0.5614 0.6461 -0.0112 0.0160 0.0061 159 SER A CA 1225 C C . SER A 156 ? 0.6185 0.5568 0.6437 -0.0119 0.0157 0.0065 159 SER A C 1226 O O . SER A 156 ? 0.6257 0.5650 0.6517 -0.0143 0.0136 0.0073 159 SER A O 1227 C CB . SER A 156 ? 0.6460 0.5664 0.6492 -0.0128 0.0148 0.0069 159 SER A CB 1228 O OG . SER A 156 ? 0.6761 0.5871 0.6681 -0.0130 0.0144 0.0063 159 SER A OG 1229 N N . ASN A 157 ? 0.6022 0.5472 0.6359 -0.0098 0.0178 0.0061 160 ASN A N 1230 C CA . ASN A 157 ? 0.5763 0.5291 0.6200 -0.0105 0.0176 0.0063 160 ASN A CA 1231 C C . ASN A 157 ? 0.5447 0.5044 0.5967 -0.0105 0.0175 0.0053 160 ASN A C 1232 O O . ASN A 157 ? 0.5422 0.5021 0.5940 -0.0087 0.0188 0.0045 160 ASN A O 1233 C CB . ASN A 157 ? 0.5859 0.5400 0.6320 -0.0087 0.0204 0.0071 160 ASN A CB 1234 C CG . ASN A 157 ? 0.6191 0.5675 0.6586 -0.0090 0.0203 0.0083 160 ASN A CG 1235 O OD1 . ASN A 157 ? 0.6585 0.6001 0.6893 -0.0079 0.0212 0.0085 160 ASN A OD1 1236 N ND2 . ASN A 157 ? 0.6344 0.5853 0.6774 -0.0105 0.0192 0.0091 160 ASN A ND2 1237 N N . TYR A 158 ? 0.5148 0.4798 0.5736 -0.0121 0.0160 0.0054 161 TYR A N 1238 C CA . TYR A 158 ? 0.4903 0.4617 0.5572 -0.0119 0.0161 0.0045 161 TYR A CA 1239 C C . TYR A 158 ? 0.4771 0.4528 0.5507 -0.0120 0.0169 0.0050 161 TYR A C 1240 O O . TYR A 158 ? 0.4739 0.4515 0.5500 -0.0133 0.0152 0.0055 161 TYR A O 1241 C CB . TYR A 158 ? 0.4778 0.4504 0.5451 -0.0138 0.0134 0.0041 161 TYR A CB 1242 C CG . TYR A 158 ? 0.4372 0.4153 0.5114 -0.0135 0.0133 0.0030 161 TYR A CG 1243 C CD1 . TYR A 158 ? 0.3973 0.3746 0.4696 -0.0133 0.0128 0.0020 161 TYR A CD1 1244 C CD2 . TYR A 158 ? 0.3856 0.3691 0.4674 -0.0133 0.0138 0.0029 161 TYR A CD2 1245 C CE1 . TYR A 158 ? 0.3651 0.3472 0.4432 -0.0130 0.0127 0.0010 161 TYR A CE1 1246 C CE2 . TYR A 158 ? 0.3499 0.3379 0.4373 -0.0131 0.0136 0.0019 161 TYR A CE2 1247 C CZ . TYR A 158 ? 0.3491 0.3367 0.4349 -0.0129 0.0130 0.0009 161 TYR A CZ 1248 O OH . TYR A 158 ? 0.3327 0.3245 0.4237 -0.0126 0.0128 0.0000 161 TYR A OH 1249 N N . PRO A 159 ? 0.4768 0.4540 0.5528 -0.0106 0.0195 0.0050 162 PRO A N 1250 C CA . PRO A 159 ? 0.4744 0.4551 0.5564 -0.0110 0.0204 0.0053 162 PRO A CA 1251 C C . PRO A 159 ? 0.4767 0.4623 0.5652 -0.0117 0.0194 0.0044 162 PRO A C 1252 O O . PRO A 159 ? 0.4783 0.4654 0.5675 -0.0116 0.0186 0.0034 162 PRO A O 1253 C CB . PRO A 159 ? 0.4852 0.4669 0.5681 -0.0097 0.0235 0.0055 162 PRO A CB 1254 C CG . PRO A 159 ? 0.4754 0.4561 0.5549 -0.0080 0.0242 0.0050 162 PRO A CG 1255 C CD . PRO A 159 ? 0.4734 0.4493 0.5467 -0.0085 0.0219 0.0048 162 PRO A CD 1256 N N . VAL A 160 ? 0.4653 0.4528 0.5579 -0.0125 0.0196 0.0047 163 VAL A N 1257 C CA . VAL A 160 ? 0.4686 0.4598 0.5666 -0.0130 0.0189 0.0038 163 VAL A CA 1258 C C . VAL A 160 ? 0.4528 0.4474 0.5540 -0.0126 0.0199 0.0026 163 VAL A C 1259 O O . VAL A 160 ? 0.4553 0.4508 0.5572 -0.0122 0.0220 0.0026 163 VAL A O 1260 C CB . VAL A 160 ? 0.4651 0.4565 0.5659 -0.0136 0.0195 0.0043 163 VAL A CB 1261 C CG1 . VAL A 160 ? 0.4730 0.4674 0.5784 -0.0139 0.0188 0.0034 163 VAL A CG1 1262 C CG2 . VAL A 160 ? 0.4965 0.4850 0.5941 -0.0135 0.0185 0.0058 163 VAL A CG2 1263 N N . ALA A 161 ? 0.4377 0.4344 0.5406 -0.0125 0.0185 0.0015 164 ALA A N 1264 C CA . ALA A 161 ? 0.4133 0.4134 0.5189 -0.0119 0.0192 0.0004 164 ALA A CA 1265 C C . ALA A 161 ? 0.4015 0.4049 0.5127 -0.0129 0.0192 -0.0003 164 ALA A C 1266 O O . ALA A 161 ? 0.3887 0.3920 0.5011 -0.0134 0.0178 -0.0004 164 ALA A O 1267 C CB . ALA A 161 ? 0.4068 0.4064 0.5102 -0.0113 0.0177 -0.0002 164 ALA A CB 1268 N N . LYS A 162 ? 0.3957 0.4022 0.5099 -0.0131 0.0208 -0.0006 165 LYS A N 1269 C CA . LYS A 162 ? 0.3994 0.4084 0.5181 -0.0145 0.0207 -0.0014 165 LYS A CA 1270 C C . LYS A 162 ? 0.3757 0.3896 0.4975 -0.0143 0.0213 -0.0023 165 LYS A C 1271 O O . LYS A 162 ? 0.3737 0.3896 0.4953 -0.0137 0.0228 -0.0018 165 LYS A O 1272 C CB . LYS A 162 ? 0.4203 0.4278 0.5396 -0.0161 0.0220 -0.0007 165 LYS A CB 1273 C CG . LYS A 162 ? 0.4744 0.4773 0.5901 -0.0158 0.0221 0.0006 165 LYS A CG 1274 C CD . LYS A 162 ? 0.5519 0.5534 0.6676 -0.0171 0.0241 0.0014 165 LYS A CD 1275 C CE . LYS A 162 ? 0.6044 0.6026 0.7159 -0.0163 0.0250 0.0028 165 LYS A CE 1276 N NZ . LYS A 162 ? 0.6338 0.6288 0.7442 -0.0174 0.0264 0.0039 165 LYS A NZ 1277 N N . GLY A 163 ? 0.3523 0.3684 0.4767 -0.0147 0.0201 -0.0035 166 GLY A N 1278 C CA . GLY A 163 ? 0.3382 0.3595 0.4658 -0.0147 0.0203 -0.0044 166 GLY A CA 1279 C C . GLY A 163 ? 0.3345 0.3568 0.4652 -0.0166 0.0195 -0.0054 166 GLY A C 1280 O O . GLY A 163 ? 0.3313 0.3502 0.4611 -0.0169 0.0185 -0.0057 166 GLY A O 1281 N N . SER A 164 ? 0.3089 0.3359 0.4429 -0.0179 0.0200 -0.0059 167 SER A N 1282 C CA . SER A 164 ? 0.3118 0.3391 0.4480 -0.0202 0.0192 -0.0069 167 SER A CA 1283 C C . SER A 164 ? 0.2857 0.3193 0.4252 -0.0206 0.0187 -0.0078 167 SER A C 1284 O O . SER A 164 ? 0.2811 0.3197 0.4222 -0.0199 0.0196 -0.0072 167 SER A O 1285 C CB . SER A 164 ? 0.3236 0.3487 0.4597 -0.0230 0.0204 -0.0062 167 SER A CB 1286 O OG . SER A 164 ? 0.3632 0.3877 0.5005 -0.0254 0.0196 -0.0073 167 SER A OG 1287 N N . TYR A 165 ? 0.2645 0.2979 0.4049 -0.0214 0.0172 -0.0092 168 TYR A N 1288 C CA . TYR A 165 ? 0.2534 0.2928 0.3969 -0.0222 0.0165 -0.0101 168 TYR A CA 1289 C C . TYR A 165 ? 0.2513 0.2891 0.3953 -0.0251 0.0154 -0.0113 168 TYR A C 1290 O O . TYR A 165 ? 0.2520 0.2845 0.3938 -0.0247 0.0146 -0.0120 168 TYR A O 1291 C CB . TYR A 165 ? 0.2369 0.2782 0.3800 -0.0190 0.0155 -0.0107 168 TYR A CB 1292 C CG . TYR A 165 ? 0.2307 0.2779 0.3766 -0.0195 0.0145 -0.0117 168 TYR A CG 1293 C CD1 . TYR A 165 ? 0.1991 0.2540 0.3481 -0.0197 0.0152 -0.0111 168 TYR A CD1 1294 C CD2 . TYR A 165 ? 0.2324 0.2780 0.3780 -0.0197 0.0129 -0.0132 168 TYR A CD2 1295 C CE1 . TYR A 165 ? 0.1820 0.2431 0.3338 -0.0203 0.0141 -0.0119 168 TYR A CE1 1296 C CE2 . TYR A 165 ? 0.2158 0.2666 0.3636 -0.0202 0.0118 -0.0141 168 TYR A CE2 1297 C CZ . TYR A 165 ? 0.2089 0.2676 0.3599 -0.0206 0.0123 -0.0135 168 TYR A CZ 1298 O OH . TYR A 165 ? 0.2334 0.2980 0.3868 -0.0212 0.0110 -0.0143 168 TYR A OH 1299 N N . ASN A 166 ? 0.2523 0.2949 0.3990 -0.0281 0.0155 -0.0114 169 ASN A N 1300 C CA . ASN A 166 ? 0.2536 0.2946 0.4002 -0.0314 0.0143 -0.0126 169 ASN A CA 1301 C C . ASN A 166 ? 0.2476 0.2941 0.3962 -0.0308 0.0127 -0.0138 169 ASN A C 1302 O O . ASN A 166 ? 0.2506 0.3050 0.4024 -0.0303 0.0128 -0.0133 169 ASN A O 1303 C CB . ASN A 166 ? 0.2612 0.3038 0.4089 -0.0358 0.0152 -0.0120 169 ASN A CB 1304 C CG . ASN A 166 ? 0.3126 0.3527 0.4592 -0.0400 0.0140 -0.0133 169 ASN A CG 1305 O OD1 . ASN A 166 ? 0.2810 0.3201 0.4268 -0.0395 0.0123 -0.0147 169 ASN A OD1 1306 N ND2 . ASN A 166 ? 0.3731 0.4119 0.5192 -0.0443 0.0148 -0.0127 169 ASN A ND2 1307 N N . ASN A 167 ? 0.2423 0.2847 0.3889 -0.0304 0.0113 -0.0152 170 ASN A N 1308 C CA . ASN A 167 ? 0.2551 0.3020 0.4032 -0.0295 0.0097 -0.0163 170 ASN A CA 1309 C C . ASN A 167 ? 0.2647 0.3167 0.4150 -0.0336 0.0087 -0.0168 170 ASN A C 1310 O O . ASN A 167 ? 0.2729 0.3208 0.4212 -0.0363 0.0076 -0.0180 170 ASN A O 1311 C CB . ASN A 167 ? 0.2414 0.2825 0.3865 -0.0276 0.0087 -0.0175 170 ASN A CB 1312 C CG . ASN A 167 ? 0.2586 0.3040 0.4048 -0.0264 0.0071 -0.0187 170 ASN A CG 1313 O OD1 . ASN A 167 ? 0.2453 0.2984 0.3946 -0.0264 0.0068 -0.0185 170 ASN A OD1 1314 N ND2 . ASN A 167 ? 0.2499 0.2905 0.3935 -0.0251 0.0063 -0.0197 170 ASN A ND2 1315 N N . THR A 168 ? 0.2752 0.3362 0.4295 -0.0339 0.0091 -0.0159 171 THR A N 1316 C CA . THR A 168 ? 0.2879 0.3558 0.4451 -0.0379 0.0080 -0.0161 171 THR A CA 1317 C C . THR A 168 ? 0.2903 0.3654 0.4496 -0.0356 0.0064 -0.0167 171 THR A C 1318 O O . THR A 168 ? 0.2733 0.3566 0.4358 -0.0381 0.0054 -0.0166 171 THR A O 1319 C CB . THR A 168 ? 0.2816 0.3566 0.4424 -0.0400 0.0095 -0.0143 171 THR A CB 1320 O OG1 . THR A 168 ? 0.2809 0.3612 0.4435 -0.0353 0.0107 -0.0130 171 THR A OG1 1321 C CG2 . THR A 168 ? 0.2865 0.3541 0.4447 -0.0423 0.0110 -0.0137 171 THR A CG2 1322 N N . SER A 169 ? 0.2876 0.3596 0.4449 -0.0311 0.0062 -0.0173 172 SER A N 1323 C CA . SER A 169 ? 0.2861 0.3644 0.4449 -0.0282 0.0051 -0.0178 172 SER A CA 1324 C C . SER A 169 ? 0.2973 0.3766 0.4559 -0.0307 0.0027 -0.0194 172 SER A C 1325 O O . SER A 169 ? 0.3042 0.3901 0.4644 -0.0289 0.0015 -0.0196 172 SER A O 1326 C CB . SER A 169 ? 0.2893 0.3628 0.4452 -0.0231 0.0056 -0.0180 172 SER A CB 1327 O OG . SER A 169 ? 0.2583 0.3238 0.4108 -0.0234 0.0046 -0.0194 172 SER A OG 1328 N N . GLY A 170 ? 0.2973 0.3697 0.4532 -0.0344 0.0019 -0.0205 173 GLY A N 1329 C CA . GLY A 170 ? 0.3158 0.3875 0.4702 -0.0368 -0.0003 -0.0221 173 GLY A CA 1330 C C . GLY A 170 ? 0.3241 0.3882 0.4743 -0.0340 -0.0010 -0.0236 173 GLY A C 1331 O O . GLY A 170 ? 0.3294 0.3917 0.4775 -0.0358 -0.0028 -0.0250 173 GLY A O 1332 N N . GLU A 171 ? 0.2990 0.3586 0.4478 -0.0298 0.0003 -0.0232 174 GLU A N 1333 C CA . GLU A 171 ? 0.3014 0.3539 0.4464 -0.0271 0.0000 -0.0242 174 GLU A CA 1334 C C . GLU A 171 ? 0.2734 0.3193 0.4164 -0.0248 0.0017 -0.0234 174 GLU A C 1335 O O . GLU A 171 ? 0.2636 0.3107 0.4081 -0.0247 0.0031 -0.0221 174 GLU A O 1336 C CB . GLU A 171 ? 0.3076 0.3647 0.4533 -0.0236 -0.0009 -0.0247 174 GLU A CB 1337 C CG . GLU A 171 ? 0.3670 0.4240 0.5110 -0.0249 -0.0031 -0.0263 174 GLU A CG 1338 C CD . GLU A 171 ? 0.4766 0.5241 0.6158 -0.0234 -0.0031 -0.0274 174 GLU A CD 1339 O OE1 . GLU A 171 ? 0.4876 0.5285 0.6248 -0.0227 -0.0017 -0.0269 174 GLU A OE1 1340 O OE2 . GLU A 171 ? 0.4800 0.5268 0.6172 -0.0227 -0.0046 -0.0287 174 GLU A OE2 1341 N N . GLN A 172 ? 0.2584 0.2976 0.3980 -0.0231 0.0016 -0.0241 175 GLN A N 1342 C CA . GLN A 172 ? 0.2486 0.2828 0.3866 -0.0206 0.0030 -0.0231 175 GLN A CA 1343 C C . GLN A 172 ? 0.2273 0.2659 0.3672 -0.0175 0.0037 -0.0222 175 GLN A C 1344 O O . GLN A 172 ? 0.2035 0.2466 0.3444 -0.0159 0.0029 -0.0226 175 GLN A O 1345 C CB . GLN A 172 ? 0.2588 0.2868 0.3932 -0.0188 0.0028 -0.0238 175 GLN A CB 1346 C CG . GLN A 172 ? 0.3074 0.3288 0.4384 -0.0211 0.0027 -0.0245 175 GLN A CG 1347 C CD . GLN A 172 ? 0.3773 0.3930 0.5047 -0.0186 0.0028 -0.0249 175 GLN A CD 1348 O OE1 . GLN A 172 ? 0.3962 0.4133 0.5233 -0.0167 0.0020 -0.0257 175 GLN A OE1 1349 N NE2 . GLN A 172 ? 0.3543 0.3635 0.4788 -0.0182 0.0039 -0.0243 175 GLN A NE2 1350 N N . MET A 173 ? 0.2131 0.2498 0.3528 -0.0167 0.0050 -0.0209 176 MET A N 1351 C CA . MET A 173 ? 0.2184 0.2581 0.3589 -0.0141 0.0057 -0.0199 176 MET A CA 1352 C C . MET A 173 ? 0.2135 0.2486 0.3517 -0.0121 0.0064 -0.0191 176 MET A C 1353 O O . MET A 173 ? 0.2063 0.2376 0.3436 -0.0129 0.0070 -0.0184 176 MET A O 1354 C CB . MET A 173 ? 0.2049 0.2482 0.3475 -0.0153 0.0067 -0.0188 176 MET A CB 1355 C CG . MET A 173 ? 0.2197 0.2658 0.3622 -0.0124 0.0076 -0.0179 176 MET A CG 1356 S SD . MET A 173 ? 0.2572 0.3061 0.4015 -0.0137 0.0091 -0.0164 176 MET A SD 1357 C CE . MET A 173 ? 0.2328 0.2909 0.3810 -0.0149 0.0085 -0.0167 176 MET A CE 1358 N N . LEU A 174 ? 0.2126 0.2483 0.3496 -0.0095 0.0062 -0.0191 177 LEU A N 1359 C CA . LEU A 174 ? 0.2068 0.2388 0.3416 -0.0081 0.0066 -0.0183 177 LEU A CA 1360 C C . LEU A 174 ? 0.1993 0.2315 0.3337 -0.0078 0.0076 -0.0170 177 LEU A C 1361 O O . LEU A 174 ? 0.2116 0.2469 0.3461 -0.0068 0.0080 -0.0168 177 LEU A O 1362 C CB . LEU A 174 ? 0.2067 0.2386 0.3398 -0.0059 0.0061 -0.0188 177 LEU A CB 1363 C CG . LEU A 174 ? 0.2325 0.2617 0.3631 -0.0047 0.0065 -0.0177 177 LEU A CG 1364 C CD1 . LEU A 174 ? 0.2087 0.2350 0.3390 -0.0052 0.0065 -0.0172 177 LEU A CD1 1365 C CD2 . LEU A 174 ? 0.2528 0.2823 0.3814 -0.0028 0.0061 -0.0182 177 LEU A CD2 1366 N N . ILE A 175 ? 0.1867 0.2159 0.3203 -0.0085 0.0081 -0.0159 178 ILE A N 1367 C CA . ILE A 175 ? 0.1741 0.2026 0.3066 -0.0084 0.0090 -0.0147 178 ILE A CA 1368 C C . ILE A 175 ? 0.1892 0.2145 0.3192 -0.0078 0.0088 -0.0137 178 ILE A C 1369 O O . ILE A 175 ? 0.1793 0.2029 0.3095 -0.0081 0.0085 -0.0135 178 ILE A O 1370 C CB . ILE A 175 ? 0.1731 0.2015 0.3070 -0.0102 0.0097 -0.0141 178 ILE A CB 1371 C CG1 . ILE A 175 ? 0.1778 0.2102 0.3145 -0.0115 0.0098 -0.0150 178 ILE A CG1 1372 C CG2 . ILE A 175 ? 0.1784 0.2059 0.3108 -0.0099 0.0107 -0.0128 178 ILE A CG2 1373 C CD1 . ILE A 175 ? 0.2006 0.2333 0.3387 -0.0137 0.0106 -0.0144 178 ILE A CD1 1374 N N . ILE A 176 ? 0.1626 0.1871 0.2900 -0.0070 0.0091 -0.0131 179 ILE A N 1375 C CA . ILE A 176 ? 0.1801 0.2018 0.3048 -0.0070 0.0087 -0.0121 179 ILE A CA 1376 C C . ILE A 176 ? 0.1805 0.2005 0.3034 -0.0077 0.0092 -0.0109 179 ILE A C 1377 O O . ILE A 176 ? 0.1914 0.2119 0.3139 -0.0074 0.0100 -0.0109 179 ILE A O 1378 C CB . ILE A 176 ? 0.1730 0.1939 0.2947 -0.0058 0.0083 -0.0125 179 ILE A CB 1379 C CG1 . ILE A 176 ? 0.1770 0.1994 0.3003 -0.0050 0.0078 -0.0136 179 ILE A CG1 1380 C CG2 . ILE A 176 ? 0.1853 0.2032 0.3035 -0.0065 0.0079 -0.0113 179 ILE A CG2 1381 C CD1 . ILE A 176 ? 0.1735 0.1954 0.2939 -0.0033 0.0077 -0.0143 179 ILE A CD1 1382 N N . TRP A 177 ? 0.1822 0.2005 0.3042 -0.0087 0.0088 -0.0097 180 TRP A N 1383 C CA . TRP A 177 ? 0.1886 0.2048 0.3079 -0.0094 0.0091 -0.0085 180 TRP A CA 1384 C C . TRP A 177 ? 0.2071 0.2218 0.3239 -0.0103 0.0080 -0.0074 180 TRP A C 1385 O O . TRP A 177 ? 0.1961 0.2120 0.3139 -0.0103 0.0073 -0.0074 180 TRP A O 1386 C CB . TRP A 177 ? 0.1899 0.2063 0.3113 -0.0101 0.0097 -0.0079 180 TRP A CB 1387 C CG . TRP A 177 ? 0.2116 0.2284 0.3350 -0.0104 0.0092 -0.0074 180 TRP A CG 1388 C CD1 . TRP A 177 ? 0.2728 0.2890 0.3952 -0.0109 0.0086 -0.0059 180 TRP A CD1 1389 C CD2 . TRP A 177 ? 0.2476 0.2655 0.3737 -0.0101 0.0092 -0.0082 180 TRP A CD2 1390 N NE1 . TRP A 177 ? 0.2791 0.2962 0.4037 -0.0104 0.0086 -0.0056 180 TRP A NE1 1391 C CE2 . TRP A 177 ? 0.2793 0.2968 0.4057 -0.0099 0.0090 -0.0071 180 TRP A CE2 1392 C CE3 . TRP A 177 ? 0.2517 0.2708 0.3796 -0.0099 0.0095 -0.0097 180 TRP A CE3 1393 C CZ2 . TRP A 177 ? 0.2908 0.3082 0.4187 -0.0092 0.0091 -0.0075 180 TRP A CZ2 1394 C CZ3 . TRP A 177 ? 0.2899 0.3088 0.4193 -0.0097 0.0094 -0.0103 180 TRP A CZ3 1395 C CH2 . TRP A 177 ? 0.2909 0.3084 0.4199 -0.0093 0.0093 -0.0092 180 TRP A CH2 1396 N N . GLY A 178 ? 0.2006 0.2129 0.3139 -0.0112 0.0079 -0.0064 181 GLY A N 1397 C CA . GLY A 178 ? 0.2041 0.2155 0.3150 -0.0126 0.0066 -0.0052 181 GLY A CA 1398 C C . GLY A 178 ? 0.2105 0.2207 0.3198 -0.0139 0.0063 -0.0037 181 GLY A C 1399 O O . GLY A 178 ? 0.2052 0.2143 0.3143 -0.0134 0.0072 -0.0037 181 GLY A O 1400 N N . VAL A 179 ? 0.2019 0.2127 0.3099 -0.0155 0.0049 -0.0024 182 VAL A N 1401 C CA . VAL A 179 ? 0.2085 0.2183 0.3142 -0.0169 0.0042 -0.0009 182 VAL A CA 1402 C C . VAL A 179 ? 0.2066 0.2140 0.3070 -0.0192 0.0028 -0.0003 182 VAL A C 1403 O O . VAL A 179 ? 0.2033 0.2125 0.3041 -0.0200 0.0021 -0.0001 182 VAL A O 1404 C CB . VAL A 179 ? 0.2010 0.2149 0.3106 -0.0168 0.0037 0.0005 182 VAL A CB 1405 C CG1 . VAL A 179 ? 0.2292 0.2470 0.3408 -0.0173 0.0027 0.0012 182 VAL A CG1 1406 C CG2 . VAL A 179 ? 0.1990 0.2121 0.3061 -0.0182 0.0028 0.0022 182 VAL A CG2 1407 N N . HIS A 180 ? 0.2183 0.2214 0.3133 -0.0203 0.0026 0.0000 183 HIS A N 1408 C CA . HIS A 180 ? 0.2415 0.2409 0.3301 -0.0230 0.0012 0.0006 183 HIS A CA 1409 C C . HIS A 180 ? 0.2475 0.2499 0.3364 -0.0256 -0.0006 0.0026 183 HIS A C 1410 O O . HIS A 180 ? 0.2531 0.2560 0.3426 -0.0254 -0.0007 0.0035 183 HIS A O 1411 C CB . HIS A 180 ? 0.2456 0.2380 0.3273 -0.0227 0.0020 0.0000 183 HIS A CB 1412 C CG . HIS A 180 ? 0.2668 0.2535 0.3402 -0.0255 0.0007 0.0004 183 HIS A CG 1413 N ND1 . HIS A 180 ? 0.3014 0.2822 0.3677 -0.0268 0.0004 0.0009 183 HIS A ND1 1414 C CD2 . HIS A 180 ? 0.2875 0.2730 0.3579 -0.0276 -0.0002 0.0004 183 HIS A CD2 1415 C CE1 . HIS A 180 ? 0.3011 0.2770 0.3602 -0.0297 -0.0008 0.0011 183 HIS A CE1 1416 N NE2 . HIS A 180 ? 0.2898 0.2685 0.3513 -0.0303 -0.0013 0.0009 183 HIS A NE2 1417 N N . HIS A 181 ? 0.2421 0.2472 0.3310 -0.0278 -0.0021 0.0035 184 HIS A N 1418 C CA . HIS A 181 ? 0.2615 0.2703 0.3503 -0.0307 -0.0042 0.0056 184 HIS A CA 1419 C C . HIS A 181 ? 0.2656 0.2685 0.3459 -0.0345 -0.0056 0.0059 184 HIS A C 1420 O O . HIS A 181 ? 0.2624 0.2637 0.3398 -0.0364 -0.0061 0.0056 184 HIS A O 1421 C CB . HIS A 181 ? 0.2478 0.2638 0.3419 -0.0311 -0.0048 0.0067 184 HIS A CB 1422 C CG . HIS A 181 ? 0.2801 0.3007 0.3814 -0.0274 -0.0033 0.0063 184 HIS A CG 1423 N ND1 . HIS A 181 ? 0.2847 0.3084 0.3897 -0.0255 -0.0029 0.0073 184 HIS A ND1 1424 C CD2 . HIS A 181 ? 0.3063 0.3282 0.4109 -0.0253 -0.0021 0.0051 184 HIS A CD2 1425 C CE1 . HIS A 181 ? 0.2879 0.3140 0.3978 -0.0225 -0.0015 0.0066 184 HIS A CE1 1426 N NE2 . HIS A 181 ? 0.3083 0.3336 0.4182 -0.0224 -0.0010 0.0053 184 HIS A NE2 1427 N N . PRO A 182 ? 0.2760 0.2752 0.3516 -0.0357 -0.0063 0.0065 185 PRO A N 1428 C CA . PRO A 182 ? 0.2979 0.2896 0.3639 -0.0392 -0.0075 0.0064 185 PRO A CA 1429 C C . PRO A 182 ? 0.3232 0.3182 0.3876 -0.0441 -0.0102 0.0082 185 PRO A C 1430 O O . PRO A 182 ? 0.3028 0.3068 0.3739 -0.0446 -0.0113 0.0099 185 PRO A O 1431 C CB . PRO A 182 ? 0.3085 0.2962 0.3708 -0.0387 -0.0075 0.0067 185 PRO A CB 1432 C CG . PRO A 182 ? 0.2840 0.2756 0.3537 -0.0343 -0.0054 0.0062 185 PRO A CG 1433 C CD . PRO A 182 ? 0.2753 0.2758 0.3533 -0.0338 -0.0058 0.0070 185 PRO A CD 1434 N N . ASN A 183 ? 0.3477 0.3352 0.4029 -0.0476 -0.0113 0.0079 186 ASN A N 1435 C CA . ASN A 183 ? 0.3953 0.3846 0.4472 -0.0534 -0.0141 0.0096 186 ASN A CA 1436 C C . ASN A 183 ? 0.4231 0.4152 0.4740 -0.0562 -0.0164 0.0115 186 ASN A C 1437 O O . ASN A 183 ? 0.4167 0.4170 0.4709 -0.0595 -0.0187 0.0137 186 ASN A O 1438 C CB . ASN A 183 ? 0.4069 0.3856 0.4479 -0.0564 -0.0143 0.0085 186 ASN A CB 1439 C CG . ASN A 183 ? 0.4485 0.4287 0.4859 -0.0630 -0.0171 0.0101 186 ASN A CG 1440 O OD1 . ASN A 183 ? 0.4853 0.4733 0.5286 -0.0642 -0.0175 0.0111 186 ASN A OD1 1441 N ND2 . ASN A 183 ? 0.5240 0.4965 0.5512 -0.0673 -0.0189 0.0104 186 ASN A ND2 1442 N N . ASP A 184 ? 0.4592 0.4454 0.5060 -0.0544 -0.0157 0.0109 187 ASP A N 1443 C CA . ASP A 184 ? 0.4970 0.4830 0.5403 -0.0570 -0.0179 0.0124 187 ASP A CA 1444 C C . ASP A 184 ? 0.5143 0.4967 0.5572 -0.0530 -0.0162 0.0117 187 ASP A C 1445 O O . ASP A 184 ? 0.5091 0.4895 0.5546 -0.0484 -0.0134 0.0101 187 ASP A O 1446 C CB . ASP A 184 ? 0.5093 0.4866 0.5406 -0.0628 -0.0201 0.0125 187 ASP A CB 1447 C CG . ASP A 184 ? 0.5442 0.5080 0.5658 -0.0613 -0.0180 0.0102 187 ASP A CG 1448 O OD1 . ASP A 184 ? 0.5879 0.5464 0.6073 -0.0576 -0.0161 0.0092 187 ASP A OD1 1449 O OD2 . ASP A 184 ? 0.5946 0.5533 0.6109 -0.0636 -0.0181 0.0094 187 ASP A OD2 1450 N N . GLU A 185 ? 0.5431 0.5249 0.5825 -0.0550 -0.0180 0.0130 188 GLU A N 1451 C CA . GLU A 185 ? 0.5580 0.5370 0.5969 -0.0516 -0.0166 0.0128 188 GLU A CA 1452 C C . GLU A 185 ? 0.5728 0.5392 0.6019 -0.0505 -0.0149 0.0110 188 GLU A C 1453 O O . GLU A 185 ? 0.5708 0.5345 0.6010 -0.0462 -0.0123 0.0100 188 GLU A O 1454 C CB . GLU A 185 ? 0.5707 0.5532 0.6085 -0.0541 -0.0193 0.0150 188 GLU A CB 1455 C CG . GLU A 185 ? 0.6171 0.6107 0.6602 -0.0576 -0.0222 0.0173 188 GLU A CG 1456 C CD . GLU A 185 ? 0.6618 0.6528 0.6979 -0.0640 -0.0250 0.0178 188 GLU A CD 1457 O OE1 . GLU A 185 ? 0.7038 0.6896 0.7313 -0.0682 -0.0273 0.0184 188 GLU A OE1 1458 O OE2 . GLU A 185 ? 0.6771 0.6711 0.7162 -0.0651 -0.0248 0.0175 188 GLU A OE2 1459 N N . THR A 186 ? 0.5924 0.5507 0.6112 -0.0545 -0.0164 0.0107 189 THR A N 1460 C CA . THR A 186 ? 0.6066 0.5520 0.6148 -0.0531 -0.0146 0.0091 189 THR A CA 1461 C C . THR A 186 ? 0.5956 0.5401 0.6077 -0.0479 -0.0110 0.0073 189 THR A C 1462 O O . THR A 186 ? 0.6066 0.5460 0.6164 -0.0439 -0.0084 0.0064 189 THR A O 1463 C CB . THR A 186 ? 0.6237 0.5596 0.6194 -0.0584 -0.0166 0.0090 189 THR A CB 1464 O OG1 . THR A 186 ? 0.6456 0.5823 0.6424 -0.0597 -0.0165 0.0083 189 THR A OG1 1465 C CG2 . THR A 186 ? 0.6239 0.5635 0.6179 -0.0641 -0.0205 0.0109 189 THR A CG2 1466 N N . GLU A 187 ? 0.5745 0.5248 0.5930 -0.0479 -0.0109 0.0070 190 GLU A N 1467 C CA . GLU A 187 ? 0.5594 0.5107 0.5828 -0.0432 -0.0079 0.0055 190 GLU A CA 1468 C C . GLU A 187 ? 0.5376 0.4954 0.5705 -0.0387 -0.0059 0.0054 190 GLU A C 1469 O O . GLU A 187 ? 0.5291 0.4840 0.5619 -0.0347 -0.0032 0.0042 190 GLU A O 1470 C CB . GLU A 187 ? 0.5520 0.5088 0.5805 -0.0445 -0.0085 0.0054 190 GLU A CB 1471 C CG . GLU A 187 ? 0.5753 0.5323 0.6076 -0.0401 -0.0058 0.0037 190 GLU A CG 1472 C CD . GLU A 187 ? 0.6042 0.5647 0.6394 -0.0414 -0.0063 0.0035 190 GLU A CD 1473 O OE1 . GLU A 187 ? 0.6089 0.5756 0.6476 -0.0449 -0.0085 0.0049 190 GLU A OE1 1474 O OE2 . GLU A 187 ? 0.6373 0.5948 0.6716 -0.0386 -0.0044 0.0021 190 GLU A OE2 1475 N N . GLN A 188 ? 0.5166 0.4831 0.5571 -0.0394 -0.0072 0.0068 191 GLN A N 1476 C CA . GLN A 188 ? 0.5135 0.4852 0.5618 -0.0357 -0.0055 0.0069 191 GLN A CA 1477 C C . GLN A 188 ? 0.5255 0.4910 0.5688 -0.0338 -0.0040 0.0067 191 GLN A C 1478 O O . GLN A 188 ? 0.5150 0.4809 0.5620 -0.0301 -0.0014 0.0059 191 GLN A O 1479 C CB . GLN A 188 ? 0.4983 0.4791 0.5536 -0.0368 -0.0074 0.0088 191 GLN A CB 1480 C CG . GLN A 188 ? 0.4775 0.4629 0.5400 -0.0332 -0.0057 0.0091 191 GLN A CG 1481 C CD . GLN A 188 ? 0.4307 0.4199 0.5007 -0.0300 -0.0035 0.0078 191 GLN A CD 1482 O OE1 . GLN A 188 ? 0.4273 0.4187 0.4995 -0.0304 -0.0037 0.0072 191 GLN A OE1 1483 N NE2 . GLN A 188 ? 0.4150 0.4047 0.4886 -0.0270 -0.0015 0.0075 191 GLN A NE2 1484 N N . ARG A 189 ? 0.5387 0.4983 0.5734 -0.0364 -0.0056 0.0074 192 ARG A N 1485 C CA . ARG A 189 ? 0.5484 0.5017 0.5776 -0.0348 -0.0043 0.0074 192 ARG A CA 1486 C C . ARG A 189 ? 0.5584 0.5031 0.5808 -0.0323 -0.0017 0.0059 192 ARG A C 1487 O O . ARG A 189 ? 0.5692 0.5125 0.5924 -0.0287 0.0008 0.0055 192 ARG A O 1488 C CB . ARG A 189 ? 0.5630 0.5127 0.5848 -0.0385 -0.0070 0.0087 192 ARG A CB 1489 C CG . ARG A 189 ? 0.6094 0.5511 0.6236 -0.0370 -0.0058 0.0087 192 ARG A CG 1490 C CD . ARG A 189 ? 0.6796 0.6146 0.6831 -0.0413 -0.0086 0.0096 192 ARG A CD 1491 N NE . ARG A 189 ? 0.7316 0.6573 0.7250 -0.0433 -0.0089 0.0085 192 ARG A NE 1492 C CZ . ARG A 189 ? 0.7491 0.6743 0.7388 -0.0482 -0.0118 0.0089 192 ARG A CZ 1493 N NH1 . ARG A 189 ? 0.7594 0.6940 0.7553 -0.0516 -0.0148 0.0104 192 ARG A NH1 1494 N NH2 . ARG A 189 ? 0.7602 0.6756 0.7398 -0.0497 -0.0117 0.0078 192 ARG A NH2 1495 N N . THR A 190 ? 0.5598 0.4987 0.5753 -0.0340 -0.0024 0.0052 193 THR A N 1496 C CA . THR A 190 ? 0.5672 0.4973 0.5750 -0.0312 0.0001 0.0040 193 THR A CA 1497 C C . THR A 190 ? 0.5495 0.4849 0.5657 -0.0265 0.0030 0.0030 193 THR A C 1498 O O . THR A 190 ? 0.5464 0.4783 0.5602 -0.0228 0.0058 0.0026 193 THR A O 1499 C CB . THR A 190 ? 0.5734 0.4952 0.5712 -0.0338 -0.0010 0.0034 193 THR A CB 1500 O OG1 . THR A 190 ? 0.6137 0.5414 0.6176 -0.0349 -0.0017 0.0030 193 THR A OG1 1501 C CG2 . THR A 190 ? 0.5912 0.5079 0.5805 -0.0391 -0.0041 0.0044 193 THR A CG2 1502 N N . LEU A 191 ? 0.5311 0.4753 0.5571 -0.0269 0.0024 0.0029 194 LEU A N 1503 C CA . LEU A 191 ? 0.5057 0.4554 0.5397 -0.0231 0.0047 0.0020 194 LEU A CA 1504 C C . LEU A 191 ? 0.4911 0.4468 0.5332 -0.0209 0.0062 0.0023 194 LEU A C 1505 O O . LEU A 191 ? 0.4795 0.4361 0.5239 -0.0175 0.0087 0.0017 194 LEU A O 1506 C CB . LEU A 191 ? 0.4988 0.4544 0.5390 -0.0243 0.0035 0.0015 194 LEU A CB 1507 C CG . LEU A 191 ? 0.5052 0.4554 0.5385 -0.0260 0.0027 0.0009 194 LEU A CG 1508 C CD1 . LEU A 191 ? 0.5044 0.4617 0.5451 -0.0269 0.0018 0.0007 194 LEU A CD1 1509 C CD2 . LEU A 191 ? 0.5248 0.4678 0.5514 -0.0226 0.0052 0.0000 194 LEU A CD2 1510 N N . TYR A 192 ? 0.4822 0.4422 0.5283 -0.0227 0.0046 0.0034 195 TYR A N 1511 C CA . TYR A 192 ? 0.4853 0.4516 0.5399 -0.0209 0.0058 0.0037 195 TYR A CA 1512 C C . TYR A 192 ? 0.5094 0.4741 0.5621 -0.0211 0.0058 0.0049 195 TYR A C 1513 O O . TYR A 192 ? 0.5060 0.4747 0.5646 -0.0196 0.0070 0.0052 195 TYR A O 1514 C CB . TYR A 192 ? 0.4612 0.4354 0.5243 -0.0219 0.0044 0.0040 195 TYR A CB 1515 C CG . TYR A 192 ? 0.4058 0.3818 0.4709 -0.0218 0.0043 0.0029 195 TYR A CG 1516 C CD1 . TYR A 192 ? 0.3704 0.3467 0.4376 -0.0191 0.0064 0.0016 195 TYR A CD1 1517 C CD2 . TYR A 192 ? 0.3806 0.3580 0.4450 -0.0246 0.0020 0.0033 195 TYR A CD2 1518 C CE1 . TYR A 192 ? 0.3591 0.3367 0.4276 -0.0189 0.0063 0.0006 195 TYR A CE1 1519 C CE2 . TYR A 192 ? 0.3404 0.3189 0.4060 -0.0246 0.0019 0.0024 195 TYR A CE2 1520 C CZ . TYR A 192 ? 0.3251 0.3034 0.3926 -0.0216 0.0041 0.0010 195 TYR A CZ 1521 O OH . TYR A 192 ? 0.3066 0.2858 0.3751 -0.0213 0.0041 0.0001 195 TYR A OH 1522 N N . GLN A 193 ? 0.5372 0.4957 0.5812 -0.0230 0.0044 0.0056 196 GLN A N 1523 C CA . GLN A 193 ? 0.5679 0.5245 0.6089 -0.0237 0.0037 0.0069 196 GLN A CA 1524 C C . GLN A 193 ? 0.5627 0.5264 0.6104 -0.0248 0.0021 0.0082 196 GLN A C 1525 O O . GLN A 193 ? 0.5800 0.5433 0.6244 -0.0271 -0.0001 0.0094 196 GLN A O 1526 C CB . GLN A 193 ? 0.5765 0.5291 0.6151 -0.0207 0.0067 0.0068 196 GLN A CB 1527 C CG . GLN A 193 ? 0.6177 0.5621 0.6473 -0.0195 0.0082 0.0060 196 GLN A CG 1528 C CD . GLN A 193 ? 0.6863 0.6223 0.7046 -0.0221 0.0062 0.0065 196 GLN A CD 1529 O OE1 . GLN A 193 ? 0.7316 0.6665 0.7475 -0.0236 0.0048 0.0076 196 GLN A OE1 1530 N NE2 . GLN A 193 ? 0.6779 0.6076 0.6887 -0.0228 0.0058 0.0056 196 GLN A NE2 1531 N N . ASN A 194 ? 0.5594 0.5296 0.6161 -0.0230 0.0033 0.0079 197 ASN A N 1532 C CA . ASN A 194 ? 0.5519 0.5284 0.6148 -0.0232 0.0022 0.0091 197 ASN A CA 1533 C C . ASN A 194 ? 0.5473 0.5289 0.6126 -0.0255 -0.0004 0.0098 197 ASN A C 1534 O O . ASN A 194 ? 0.5385 0.5206 0.6039 -0.0265 -0.0009 0.0090 197 ASN A O 1535 C CB . ASN A 194 ? 0.5501 0.5306 0.6207 -0.0206 0.0046 0.0085 197 ASN A CB 1536 C CG . ASN A 194 ? 0.5799 0.5567 0.6492 -0.0185 0.0074 0.0079 197 ASN A CG 1537 O OD1 . ASN A 194 ? 0.6166 0.5885 0.6800 -0.0185 0.0078 0.0085 197 ASN A OD1 1538 N ND2 . ASN A 194 ? 0.5906 0.5701 0.6655 -0.0169 0.0095 0.0069 197 ASN A ND2 1539 N N . VAL A 195 ? 0.5390 0.5248 0.6064 -0.0260 -0.0019 0.0115 198 VAL A N 1540 C CA . VAL A 195 ? 0.5291 0.5217 0.6004 -0.0276 -0.0042 0.0127 198 VAL A CA 1541 C C . VAL A 195 ? 0.5176 0.5159 0.5962 -0.0248 -0.0031 0.0134 198 VAL A C 1542 O O . VAL A 195 ? 0.5332 0.5296 0.6124 -0.0227 -0.0013 0.0133 198 VAL A O 1543 C CB . VAL A 195 ? 0.5448 0.5378 0.6112 -0.0308 -0.0073 0.0145 198 VAL A CB 1544 C CG1 . VAL A 195 ? 0.5384 0.5253 0.5971 -0.0339 -0.0084 0.0136 198 VAL A CG1 1545 C CG2 . VAL A 195 ? 0.5485 0.5391 0.6118 -0.0299 -0.0072 0.0156 198 VAL A CG2 1546 N N . GLY A 196 ? 0.5023 0.5072 0.5861 -0.0249 -0.0040 0.0140 199 GLY A N 1547 C CA . GLY A 196 ? 0.4715 0.4810 0.5615 -0.0220 -0.0029 0.0147 199 GLY A CA 1548 C C . GLY A 196 ? 0.4621 0.4687 0.5546 -0.0197 0.0000 0.0126 199 GLY A C 1549 O O . GLY A 196 ? 0.4588 0.4638 0.5524 -0.0177 0.0016 0.0127 199 GLY A O 1550 N N . THR A 197 ? 0.4288 0.4348 0.5221 -0.0203 0.0003 0.0110 200 THR A N 1551 C CA . THR A 197 ? 0.4021 0.4059 0.4977 -0.0186 0.0027 0.0090 200 THR A CA 1552 C C . THR A 197 ? 0.3870 0.3950 0.4883 -0.0171 0.0033 0.0086 200 THR A C 1553 O O . THR A 197 ? 0.3751 0.3878 0.4788 -0.0170 0.0021 0.0098 200 THR A O 1554 C CB . THR A 197 ? 0.4043 0.4043 0.4964 -0.0196 0.0030 0.0074 200 THR A CB 1555 O OG1 . THR A 197 ? 0.3546 0.3569 0.4467 -0.0212 0.0014 0.0074 200 THR A OG1 1556 C CG2 . THR A 197 ? 0.3975 0.3922 0.4830 -0.0207 0.0028 0.0077 200 THR A CG2 1557 N N . TYR A 198 ? 0.3823 0.3889 0.4859 -0.0158 0.0053 0.0069 201 TYR A N 1558 C CA . TYR A 198 ? 0.3699 0.3794 0.4781 -0.0145 0.0058 0.0062 201 TYR A CA 1559 C C . TYR A 198 ? 0.3503 0.3583 0.4598 -0.0143 0.0073 0.0041 201 TYR A C 1560 O O . TYR A 198 ? 0.3296 0.3347 0.4371 -0.0145 0.0083 0.0034 201 TYR A O 1561 C CB . TYR A 198 ? 0.3815 0.3916 0.4920 -0.0127 0.0068 0.0071 201 TYR A CB 1562 C CG . TYR A 198 ? 0.4378 0.4439 0.5474 -0.0123 0.0087 0.0064 201 TYR A CG 1563 C CD1 . TYR A 198 ? 0.4504 0.4554 0.5622 -0.0120 0.0103 0.0047 201 TYR A CD1 1564 C CD2 . TYR A 198 ? 0.4929 0.4964 0.5993 -0.0126 0.0089 0.0074 201 TYR A CD2 1565 C CE1 . TYR A 198 ? 0.4937 0.4956 0.6049 -0.0121 0.0121 0.0043 201 TYR A CE1 1566 C CE2 . TYR A 198 ? 0.5212 0.5212 0.6267 -0.0125 0.0107 0.0070 201 TYR A CE2 1567 C CZ . TYR A 198 ? 0.5262 0.5256 0.6342 -0.0123 0.0123 0.0055 201 TYR A CZ 1568 O OH . TYR A 198 ? 0.5477 0.5443 0.6549 -0.0126 0.0142 0.0053 201 TYR A OH 1569 N N . VAL A 199 ? 0.3488 0.3591 0.4614 -0.0137 0.0073 0.0032 202 VAL A N 1570 C CA . VAL A 199 ? 0.3523 0.3619 0.4666 -0.0132 0.0086 0.0013 202 VAL A CA 1571 C C . VAL A 199 ? 0.3448 0.3554 0.4624 -0.0121 0.0093 0.0009 202 VAL A C 1572 O O . VAL A 199 ? 0.3573 0.3703 0.4765 -0.0114 0.0086 0.0013 202 VAL A O 1573 C CB . VAL A 199 ? 0.3377 0.3483 0.4515 -0.0137 0.0078 0.0003 202 VAL A CB 1574 C CG1 . VAL A 199 ? 0.3357 0.3463 0.4514 -0.0130 0.0090 -0.0015 202 VAL A CG1 1575 C CG2 . VAL A 199 ? 0.3658 0.3739 0.4747 -0.0149 0.0070 0.0006 202 VAL A CG2 1576 N N . SER A 200 ? 0.3501 0.3588 0.4684 -0.0120 0.0108 0.0003 203 SER A N 1577 C CA . SER A 200 ? 0.3408 0.3490 0.4612 -0.0113 0.0117 -0.0002 203 SER A CA 1578 C C . SER A 200 ? 0.3350 0.3435 0.4572 -0.0119 0.0124 -0.0021 203 SER A C 1579 O O . SER A 200 ? 0.3268 0.3352 0.4489 -0.0127 0.0131 -0.0028 203 SER A O 1580 C CB . SER A 200 ? 0.3476 0.3527 0.4668 -0.0112 0.0129 0.0006 203 SER A CB 1581 O OG . SER A 200 ? 0.4099 0.4145 0.5287 -0.0096 0.0128 0.0018 203 SER A OG 1582 N N . VAL A 201 ? 0.3208 0.3300 0.4446 -0.0113 0.0122 -0.0030 204 VAL A N 1583 C CA . VAL A 201 ? 0.3085 0.3182 0.4340 -0.0120 0.0126 -0.0047 204 VAL A CA 1584 C C . VAL A 201 ? 0.3225 0.3293 0.4478 -0.0118 0.0132 -0.0050 204 VAL A C 1585 O O . VAL A 201 ? 0.3182 0.3239 0.4426 -0.0103 0.0131 -0.0041 204 VAL A O 1586 C CB . VAL A 201 ? 0.3112 0.3234 0.4377 -0.0114 0.0116 -0.0057 204 VAL A CB 1587 C CG1 . VAL A 201 ? 0.3071 0.3203 0.4353 -0.0122 0.0118 -0.0075 204 VAL A CG1 1588 C CG2 . VAL A 201 ? 0.2878 0.3014 0.4132 -0.0114 0.0109 -0.0053 204 VAL A CG2 1589 N N . GLY A 202 ? 0.3177 0.3233 0.4434 -0.0134 0.0140 -0.0060 205 GLY A N 1590 C CA . GLY A 202 ? 0.3133 0.3151 0.4378 -0.0139 0.0147 -0.0065 205 GLY A CA 1591 C C . GLY A 202 ? 0.3173 0.3197 0.4431 -0.0160 0.0147 -0.0083 205 GLY A C 1592 O O . GLY A 202 ? 0.3008 0.3060 0.4284 -0.0177 0.0150 -0.0086 205 GLY A O 1593 N N . THR A 203 ? 0.3077 0.3080 0.4326 -0.0159 0.0144 -0.0092 206 THR A N 1594 C CA . THR A 203 ? 0.3202 0.3199 0.4454 -0.0184 0.0143 -0.0108 206 THR A CA 1595 C C . THR A 203 ? 0.3330 0.3254 0.4540 -0.0189 0.0152 -0.0108 206 THR A C 1596 O O . THR A 203 ? 0.3282 0.3167 0.4466 -0.0172 0.0160 -0.0094 206 THR A O 1597 C CB . THR A 203 ? 0.3034 0.3061 0.4301 -0.0178 0.0131 -0.0122 206 THR A CB 1598 O OG1 . THR A 203 ? 0.3407 0.3402 0.4651 -0.0155 0.0129 -0.0121 206 THR A OG1 1599 C CG2 . THR A 203 ? 0.3387 0.3473 0.4682 -0.0166 0.0124 -0.0120 206 THR A CG2 1600 N N . SER A 204 ? 0.3501 0.3402 0.4699 -0.0211 0.0149 -0.0123 207 SER A N 1601 C CA . SER A 204 ? 0.3768 0.3586 0.4913 -0.0215 0.0156 -0.0124 207 SER A CA 1602 C C . SER A 204 ? 0.3918 0.3703 0.5035 -0.0174 0.0158 -0.0119 207 SER A C 1603 O O . SER A 204 ? 0.3769 0.3485 0.4838 -0.0161 0.0169 -0.0111 207 SER A O 1604 C CB . SER A 204 ? 0.3871 0.3674 0.5006 -0.0251 0.0150 -0.0142 207 SER A CB 1605 O OG . SER A 204 ? 0.4322 0.4149 0.5467 -0.0238 0.0137 -0.0154 207 SER A OG 1606 N N . THR A 205 ? 0.3925 0.3759 0.5070 -0.0153 0.0147 -0.0121 208 THR A N 1607 C CA . THR A 205 ? 0.4182 0.3999 0.5307 -0.0116 0.0149 -0.0115 208 THR A CA 1608 C C . THR A 205 ? 0.4199 0.4070 0.5353 -0.0088 0.0146 -0.0099 208 THR A C 1609 O O . THR A 205 ? 0.4401 0.4264 0.5541 -0.0055 0.0150 -0.0087 208 THR A O 1610 C CB . THR A 205 ? 0.4141 0.3965 0.5266 -0.0114 0.0139 -0.0131 208 THR A CB 1611 O OG1 . THR A 205 ? 0.4397 0.4295 0.5571 -0.0121 0.0127 -0.0137 208 THR A OG1 1612 C CG2 . THR A 205 ? 0.4323 0.4093 0.5414 -0.0142 0.0138 -0.0148 208 THR A CG2 1613 N N . LEU A 206 ? 0.4108 0.4035 0.5301 -0.0100 0.0140 -0.0097 209 LEU A N 1614 C CA . LEU A 206 ? 0.4077 0.4048 0.5289 -0.0079 0.0135 -0.0082 209 LEU A CA 1615 C C . LEU A 206 ? 0.3987 0.3960 0.5198 -0.0081 0.0140 -0.0066 209 LEU A C 1616 O O . LEU A 206 ? 0.3853 0.3818 0.5066 -0.0103 0.0144 -0.0069 209 LEU A O 1617 C CB . LEU A 206 ? 0.4166 0.4192 0.5409 -0.0085 0.0124 -0.0091 209 LEU A CB 1618 C CG . LEU A 206 ? 0.4421 0.4490 0.5679 -0.0071 0.0117 -0.0077 209 LEU A CG 1619 C CD1 . LEU A 206 ? 0.4670 0.4743 0.5922 -0.0045 0.0117 -0.0068 209 LEU A CD1 1620 C CD2 . LEU A 206 ? 0.4769 0.4875 0.6047 -0.0082 0.0108 -0.0088 209 LEU A CD2 1621 N N . ASN A 207 ? 0.4053 0.4037 0.5260 -0.0058 0.0140 -0.0047 210 ASN A N 1622 C CA . ASN A 207 ? 0.4205 0.4195 0.5409 -0.0057 0.0142 -0.0030 210 ASN A CA 1623 C C . ASN A 207 ? 0.4265 0.4307 0.5486 -0.0044 0.0131 -0.0017 210 ASN A C 1624 O O . ASN A 207 ? 0.4241 0.4294 0.5458 -0.0020 0.0132 -0.0003 210 ASN A O 1625 C CB . ASN A 207 ? 0.4115 0.4056 0.5285 -0.0041 0.0155 -0.0016 210 ASN A CB 1626 C CG . ASN A 207 ? 0.4512 0.4461 0.5678 -0.0038 0.0156 0.0002 210 ASN A CG 1627 O OD1 . ASN A 207 ? 0.4744 0.4698 0.5917 -0.0060 0.0155 0.0000 210 ASN A OD1 1628 N ND2 . ASN A 207 ? 0.4634 0.4587 0.5786 -0.0009 0.0158 0.0023 210 ASN A ND2 1629 N N . LYS A 208 ? 0.4442 0.4517 0.5680 -0.0060 0.0122 -0.0020 211 LYS A N 1630 C CA . LYS A 208 ? 0.4515 0.4635 0.5764 -0.0055 0.0111 -0.0010 211 LYS A CA 1631 C C . LYS A 208 ? 0.4542 0.4672 0.5785 -0.0067 0.0105 0.0000 211 LYS A C 1632 O O . LYS A 208 ? 0.4584 0.4705 0.5825 -0.0083 0.0106 -0.0010 211 LYS A O 1633 C CB . LYS A 208 ? 0.4555 0.4696 0.5818 -0.0060 0.0104 -0.0024 211 LYS A CB 1634 C CG . LYS A 208 ? 0.4738 0.4920 0.6008 -0.0055 0.0093 -0.0012 211 LYS A CG 1635 C CD . LYS A 208 ? 0.4972 0.5168 0.6249 -0.0059 0.0087 -0.0027 211 LYS A CD 1636 C CE . LYS A 208 ? 0.5299 0.5528 0.6575 -0.0068 0.0076 -0.0016 211 LYS A CE 1637 N NZ . LYS A 208 ? 0.5379 0.5627 0.6661 -0.0064 0.0072 -0.0021 211 LYS A NZ 1638 N N . ARG A 209 ? 0.4663 0.4815 0.5902 -0.0059 0.0099 0.0020 212 ARG A N 1639 C CA . ARG A 209 ? 0.4814 0.4975 0.6041 -0.0074 0.0090 0.0030 212 ARG A CA 1640 C C . ARG A 209 ? 0.4932 0.5136 0.6160 -0.0081 0.0073 0.0043 212 ARG A C 1641 O O . ARG A 209 ? 0.4926 0.5165 0.6168 -0.0069 0.0069 0.0054 212 ARG A O 1642 C CB . ARG A 209 ? 0.4708 0.4848 0.5919 -0.0068 0.0096 0.0044 212 ARG A CB 1643 C CG . ARG A 209 ? 0.4803 0.4966 0.6001 -0.0077 0.0082 0.0061 212 ARG A CG 1644 C CD . ARG A 209 ? 0.4771 0.4913 0.5950 -0.0071 0.0087 0.0075 212 ARG A CD 1645 N NE . ARG A 209 ? 0.4692 0.4786 0.5862 -0.0073 0.0104 0.0062 212 ARG A NE 1646 C CZ . ARG A 209 ? 0.5012 0.5076 0.6161 -0.0072 0.0111 0.0070 212 ARG A CZ 1647 N NH1 . ARG A 209 ? 0.4883 0.4961 0.6016 -0.0069 0.0102 0.0090 212 ARG A NH1 1648 N NH2 . ARG A 209 ? 0.4782 0.4805 0.5924 -0.0078 0.0128 0.0060 212 ARG A NH2 1649 N N . SER A 210 ? 0.4975 0.5173 0.6185 -0.0101 0.0065 0.0042 213 SER A N 1650 C CA . SER A 210 ? 0.4935 0.5162 0.6133 -0.0117 0.0048 0.0055 213 SER A CA 1651 C C . SER A 210 ? 0.4918 0.5133 0.6086 -0.0130 0.0040 0.0068 213 SER A C 1652 O O . SER A 210 ? 0.4904 0.5079 0.6052 -0.0134 0.0048 0.0060 213 SER A O 1653 C CB . SER A 210 ? 0.4999 0.5219 0.6188 -0.0131 0.0044 0.0040 213 SER A CB 1654 O OG . SER A 210 ? 0.5176 0.5402 0.6389 -0.0118 0.0051 0.0027 213 SER A OG 1655 N N . THR A 211 ? 0.4732 0.4985 0.5897 -0.0138 0.0024 0.0089 214 THR A N 1656 C CA . THR A 211 ? 0.4708 0.4953 0.5838 -0.0159 0.0010 0.0100 214 THR A CA 1657 C C . THR A 211 ? 0.4512 0.4767 0.5622 -0.0187 -0.0005 0.0099 214 THR A C 1658 O O . THR A 211 ? 0.4533 0.4834 0.5666 -0.0190 -0.0012 0.0106 214 THR A O 1659 C CB . THR A 211 ? 0.4727 0.5010 0.5862 -0.0151 0.0001 0.0126 214 THR A CB 1660 O OG1 . THR A 211 ? 0.5063 0.5412 0.6224 -0.0151 -0.0009 0.0142 214 THR A OG1 1661 C CG2 . THR A 211 ? 0.4890 0.5159 0.6040 -0.0119 0.0020 0.0128 214 THR A CG2 1662 N N . PRO A 212 ? 0.4326 0.4533 0.5389 -0.0208 -0.0009 0.0090 215 PRO A N 1663 C CA . PRO A 212 ? 0.4250 0.4448 0.5281 -0.0235 -0.0022 0.0086 215 PRO A CA 1664 C C . PRO A 212 ? 0.4267 0.4508 0.5288 -0.0262 -0.0046 0.0109 215 PRO A C 1665 O O . PRO A 212 ? 0.4343 0.4601 0.5360 -0.0265 -0.0055 0.0125 215 PRO A O 1666 C CB . PRO A 212 ? 0.4233 0.4359 0.5206 -0.0244 -0.0018 0.0073 215 PRO A CB 1667 C CG . PRO A 212 ? 0.4226 0.4332 0.5219 -0.0216 0.0002 0.0064 215 PRO A CG 1668 C CD . PRO A 212 ? 0.4406 0.4557 0.5439 -0.0203 0.0001 0.0080 215 PRO A CD 1669 N N . GLU A 213 ? 0.4270 0.4532 0.5288 -0.0284 -0.0057 0.0111 216 GLU A N 1670 C CA . GLU A 213 ? 0.4297 0.4609 0.5308 -0.0317 -0.0081 0.0134 216 GLU A CA 1671 C C . GLU A 213 ? 0.4328 0.4589 0.5266 -0.0360 -0.0097 0.0131 216 GLU A C 1672 O O . GLU A 213 ? 0.4322 0.4542 0.5232 -0.0370 -0.0093 0.0116 216 GLU A O 1673 C CB . GLU A 213 ? 0.4202 0.4586 0.5265 -0.0311 -0.0081 0.0143 216 GLU A CB 1674 C CG . GLU A 213 ? 0.4451 0.4872 0.5572 -0.0266 -0.0064 0.0146 216 GLU A CG 1675 C CD . GLU A 213 ? 0.4597 0.5057 0.5761 -0.0248 -0.0054 0.0144 216 GLU A CD 1676 O OE1 . GLU A 213 ? 0.4985 0.5449 0.6138 -0.0271 -0.0060 0.0141 216 GLU A OE1 1677 O OE2 . GLU A 213 ? 0.5000 0.5480 0.6202 -0.0211 -0.0039 0.0146 216 GLU A OE2 1678 N N . ILE A 214 ? 0.4208 0.4461 0.5107 -0.0385 -0.0115 0.0144 217 ILE A N 1679 C CA . ILE A 214 ? 0.4135 0.4337 0.4956 -0.0431 -0.0133 0.0144 217 ILE A CA 1680 C C . ILE A 214 ? 0.4180 0.4453 0.5013 -0.0471 -0.0158 0.0166 217 ILE A C 1681 O O . ILE A 214 ? 0.4026 0.4383 0.4901 -0.0473 -0.0171 0.0190 217 ILE A O 1682 C CB . ILE A 214 ? 0.4281 0.4433 0.5047 -0.0441 -0.0142 0.0147 217 ILE A CB 1683 C CG1 . ILE A 214 ? 0.3979 0.4064 0.4735 -0.0401 -0.0115 0.0127 217 ILE A CG1 1684 C CG2 . ILE A 214 ? 0.4245 0.4340 0.4920 -0.0494 -0.0164 0.0149 217 ILE A CG2 1685 C CD1 . ILE A 214 ? 0.4591 0.4642 0.5313 -0.0396 -0.0116 0.0132 217 ILE A CD1 1686 N N . ALA A 215 ? 0.4151 0.4397 0.4950 -0.0500 -0.0162 0.0159 218 ALA A N 1687 C CA . ALA A 215 ? 0.4224 0.4543 0.5040 -0.0540 -0.0182 0.0179 218 ALA A CA 1688 C C . ALA A 215 ? 0.4290 0.4540 0.5036 -0.0579 -0.0186 0.0168 218 ALA A C 1689 O O . ALA A 215 ? 0.4194 0.4372 0.4916 -0.0556 -0.0166 0.0144 218 ALA A O 1690 C CB . ALA A 215 ? 0.4021 0.4439 0.4932 -0.0507 -0.0170 0.0189 218 ALA A CB 1691 N N . THR A 216 ? 0.4513 0.4788 0.5226 -0.0637 -0.0213 0.0186 219 THR A N 1692 C CA . THR A 216 ? 0.4514 0.4728 0.5154 -0.0686 -0.0221 0.0180 219 THR A CA 1693 C C . THR A 216 ? 0.4362 0.4620 0.5050 -0.0677 -0.0208 0.0179 219 THR A C 1694 O O . THR A 216 ? 0.4417 0.4788 0.5180 -0.0680 -0.0213 0.0201 219 THR A O 1695 C CB . THR A 216 ? 0.4751 0.4988 0.5343 -0.0758 -0.0257 0.0204 219 THR A CB 1696 O OG1 . THR A 216 ? 0.5201 0.5334 0.5700 -0.0773 -0.0265 0.0193 219 THR A OG1 1697 C CG2 . THR A 216 ? 0.4782 0.5013 0.5333 -0.0817 -0.0270 0.0210 219 THR A CG2 1698 N N . ARG A 217 ? 0.4100 0.4265 0.4740 -0.0664 -0.0190 0.0155 220 ARG A N 1699 C CA . ARG A 217 ? 0.3853 0.4044 0.4530 -0.0650 -0.0175 0.0150 220 ARG A CA 1700 C C . ARG A 217 ? 0.3825 0.3915 0.4403 -0.0689 -0.0177 0.0139 220 ARG A C 1701 O O . ARG A 217 ? 0.3514 0.3497 0.3996 -0.0707 -0.0181 0.0127 220 ARG A O 1702 C CB . ARG A 217 ? 0.3750 0.3927 0.4474 -0.0581 -0.0146 0.0129 220 ARG A CB 1703 C CG . ARG A 217 ? 0.3581 0.3832 0.4388 -0.0540 -0.0141 0.0136 220 ARG A CG 1704 C CD . ARG A 217 ? 0.3331 0.3561 0.4175 -0.0479 -0.0114 0.0114 220 ARG A CD 1705 N NE . ARG A 217 ? 0.3521 0.3783 0.4411 -0.0446 -0.0109 0.0118 220 ARG A NE 1706 C CZ . ARG A 217 ? 0.3265 0.3469 0.4117 -0.0439 -0.0107 0.0109 220 ARG A CZ 1707 N NH1 . ARG A 217 ? 0.3760 0.3869 0.4525 -0.0460 -0.0110 0.0097 220 ARG A NH1 1708 N NH2 . ARG A 217 ? 0.3270 0.3507 0.4166 -0.0411 -0.0102 0.0114 220 ARG A NH2 1709 N N . PRO A 218 ? 0.3806 0.3925 0.4403 -0.0700 -0.0172 0.0142 221 PRO A N 1710 C CA . PRO A 218 ? 0.3886 0.3899 0.4381 -0.0734 -0.0171 0.0131 221 PRO A CA 1711 C C . PRO A 218 ? 0.4001 0.3902 0.4445 -0.0685 -0.0147 0.0101 221 PRO A C 1712 O O . PRO A 218 ? 0.3748 0.3679 0.4260 -0.0625 -0.0128 0.0089 221 PRO A O 1713 C CB . PRO A 218 ? 0.3894 0.3973 0.4437 -0.0742 -0.0166 0.0140 221 PRO A CB 1714 C CG . PRO A 218 ? 0.3812 0.4015 0.4477 -0.0697 -0.0157 0.0151 221 PRO A CG 1715 C CD . PRO A 218 ? 0.3754 0.3999 0.4450 -0.0689 -0.0169 0.0160 221 PRO A CD 1716 N N . LYS A 219 ? 0.4076 0.3850 0.4399 -0.0711 -0.0149 0.0089 222 LYS A N 1717 C CA . LYS A 219 ? 0.4088 0.3758 0.4358 -0.0661 -0.0125 0.0063 222 LYS A CA 1718 C C . LYS A 219 ? 0.3952 0.3631 0.4256 -0.0623 -0.0104 0.0052 222 LYS A C 1719 O O . LYS A 219 ? 0.3833 0.3526 0.4129 -0.0655 -0.0107 0.0059 222 LYS A O 1720 C CB . LYS A 219 ? 0.4246 0.3772 0.4369 -0.0693 -0.0129 0.0056 222 LYS A CB 1721 C CG . LYS A 219 ? 0.4523 0.4021 0.4605 -0.0712 -0.0144 0.0061 222 LYS A CG 1722 C CD . LYS A 219 ? 0.4924 0.4255 0.4844 -0.0732 -0.0142 0.0049 222 LYS A CD 1723 C CE . LYS A 219 ? 0.5501 0.4799 0.5359 -0.0779 -0.0167 0.0060 222 LYS A CE 1724 N NZ . LYS A 219 ? 0.5819 0.5145 0.5723 -0.0737 -0.0161 0.0057 222 LYS A NZ 1725 N N . VAL A 220 ? 0.3627 0.3307 0.3973 -0.0559 -0.0082 0.0035 223 VAL A N 1726 C CA . VAL A 220 ? 0.3626 0.3298 0.3989 -0.0518 -0.0062 0.0020 223 VAL A CA 1727 C C . VAL A 220 ? 0.3661 0.3231 0.3954 -0.0476 -0.0043 0.0000 223 VAL A C 1728 O O . VAL A 220 ? 0.3497 0.3071 0.3810 -0.0448 -0.0039 -0.0004 223 VAL A O 1729 C CB . VAL A 220 ? 0.3533 0.3320 0.4026 -0.0477 -0.0053 0.0021 223 VAL A CB 1730 C CG1 . VAL A 220 ? 0.3447 0.3219 0.3950 -0.0435 -0.0033 0.0004 223 VAL A CG1 1731 C CG2 . VAL A 220 ? 0.3491 0.3386 0.4054 -0.0513 -0.0070 0.0045 223 VAL A CG2 1732 N N . ASN A 221 ? 0.3741 0.3219 0.3948 -0.0472 -0.0033 -0.0009 224 ASN A N 1733 C CA . ASN A 221 ? 0.3826 0.3197 0.3946 -0.0433 -0.0015 -0.0026 224 ASN A CA 1734 C C . ASN A 221 ? 0.3819 0.3125 0.3867 -0.0452 -0.0022 -0.0022 224 ASN A C 1735 O O . ASN A 221 ? 0.3937 0.3206 0.3964 -0.0410 -0.0008 -0.0031 224 ASN A O 1736 C CB . ASN A 221 ? 0.3810 0.3228 0.4004 -0.0365 0.0003 -0.0038 224 ASN A CB 1737 C CG . ASN A 221 ? 0.4167 0.3634 0.4418 -0.0340 0.0012 -0.0045 224 ASN A CG 1738 O OD1 . ASN A 221 ? 0.4455 0.3884 0.4658 -0.0361 0.0011 -0.0043 224 ASN A OD1 1739 N ND2 . ASN A 221 ? 0.4112 0.3660 0.4463 -0.0298 0.0021 -0.0051 224 ASN A ND2 1740 N N . GLY A 222 ? 0.3809 0.3107 0.3820 -0.0516 -0.0045 -0.0008 225 GLY A N 1741 C CA . GLY A 222 ? 0.3690 0.2926 0.3629 -0.0540 -0.0056 -0.0004 225 GLY A CA 1742 C C . GLY A 222 ? 0.3642 0.2962 0.3663 -0.0535 -0.0065 0.0003 225 GLY A C 1743 O O . GLY A 222 ? 0.3578 0.2845 0.3536 -0.0555 -0.0074 0.0007 225 GLY A O 1744 N N . GLN A 223 ? 0.3496 0.2940 0.3651 -0.0509 -0.0063 0.0006 226 GLN A N 1745 C CA . GLN A 223 ? 0.3385 0.2899 0.3614 -0.0494 -0.0066 0.0012 226 GLN A CA 1746 C C . GLN A 223 ? 0.3268 0.2903 0.3593 -0.0523 -0.0086 0.0031 226 GLN A C 1747 O O . GLN A 223 ? 0.3136 0.2841 0.3528 -0.0518 -0.0083 0.0034 226 GLN A O 1748 C CB . GLN A 223 ? 0.3397 0.2946 0.3698 -0.0427 -0.0042 0.0000 226 GLN A CB 1749 C CG . GLN A 223 ? 0.3813 0.3262 0.4035 -0.0386 -0.0020 -0.0017 226 GLN A CG 1750 C CD . GLN A 223 ? 0.4303 0.3660 0.4424 -0.0400 -0.0023 -0.0014 226 GLN A CD 1751 O OE1 . GLN A 223 ? 0.4320 0.3708 0.4465 -0.0415 -0.0034 -0.0005 226 GLN A OE1 1752 N NE2 . GLN A 223 ? 0.4628 0.3866 0.4629 -0.0393 -0.0012 -0.0023 226 GLN A NE2 1753 N N . GLY A 224 ? 0.3346 0.3005 0.3673 -0.0549 -0.0103 0.0045 227 GLY A N 1754 C CA . GLY A 224 ? 0.3303 0.3085 0.3726 -0.0566 -0.0119 0.0065 227 GLY A CA 1755 C C . GLY A 224 ? 0.3210 0.3067 0.3735 -0.0513 -0.0106 0.0063 227 GLY A C 1756 O O . GLY A 224 ? 0.3383 0.3343 0.3997 -0.0510 -0.0111 0.0077 227 GLY A O 1757 N N . GLY A 225 ? 0.3203 0.3008 0.3714 -0.0471 -0.0087 0.0046 228 GLY A N 1758 C CA . GLY A 225 ? 0.2979 0.2844 0.3578 -0.0424 -0.0072 0.0043 228 GLY A CA 1759 C C . GLY A 225 ? 0.2880 0.2789 0.3546 -0.0391 -0.0056 0.0033 228 GLY A C 1760 O O . GLY A 225 ? 0.2964 0.2853 0.3605 -0.0400 -0.0055 0.0028 228 GLY A O 1761 N N . ARG A 226 ? 0.2630 0.2596 0.3376 -0.0354 -0.0045 0.0030 229 ARG A N 1762 C CA . ARG A 226 ? 0.2500 0.2506 0.3307 -0.0324 -0.0032 0.0021 229 ARG A CA 1763 C C . ARG A 226 ? 0.2494 0.2507 0.3343 -0.0283 -0.0014 0.0009 229 ARG A C 1764 O O . ARG A 226 ? 0.2362 0.2381 0.3221 -0.0279 -0.0014 0.0014 229 ARG A O 1765 C CB . ARG A 226 ? 0.2472 0.2569 0.3349 -0.0332 -0.0040 0.0037 229 ARG A CB 1766 C CG . ARG A 226 ? 0.2293 0.2407 0.3142 -0.0379 -0.0059 0.0054 229 ARG A CG 1767 C CD . ARG A 226 ? 0.2494 0.2576 0.3312 -0.0385 -0.0054 0.0045 229 ARG A CD 1768 N NE . ARG A 226 ? 0.2768 0.2878 0.3569 -0.0432 -0.0071 0.0063 229 ARG A NE 1769 C CZ . ARG A 226 ? 0.2958 0.3007 0.3676 -0.0476 -0.0083 0.0066 229 ARG A CZ 1770 N NH1 . ARG A 226 ? 0.2782 0.2729 0.3415 -0.0478 -0.0080 0.0052 229 ARG A NH1 1771 N NH2 . ARG A 226 ? 0.2724 0.2815 0.3440 -0.0521 -0.0099 0.0085 229 ARG A NH2 1772 N N . MET A 227 ? 0.2355 0.2365 0.3223 -0.0255 0.0000 -0.0006 230 MET A N 1773 C CA . MET A 227 ? 0.2330 0.2360 0.3248 -0.0221 0.0014 -0.0016 230 MET A CA 1774 C C . MET A 227 ? 0.2187 0.2275 0.3173 -0.0206 0.0017 -0.0018 230 MET A C 1775 O O . MET A 227 ? 0.2222 0.2312 0.3207 -0.0202 0.0018 -0.0024 230 MET A O 1776 C CB . MET A 227 ? 0.2322 0.2301 0.3203 -0.0199 0.0028 -0.0033 230 MET A CB 1777 C CG . MET A 227 ? 0.2210 0.2137 0.3036 -0.0203 0.0031 -0.0030 230 MET A CG 1778 S SD . MET A 227 ? 0.2693 0.2561 0.3466 -0.0172 0.0050 -0.0046 230 MET A SD 1779 C CE . MET A 227 ? 0.2314 0.2113 0.3005 -0.0187 0.0048 -0.0037 230 MET A CE 1780 N N . GLU A 228 ? 0.2226 0.2356 0.3264 -0.0196 0.0018 -0.0011 231 GLU A N 1781 C CA . GLU A 228 ? 0.2170 0.2347 0.3264 -0.0178 0.0023 -0.0012 231 GLU A CA 1782 C C . GLU A 228 ? 0.2074 0.2244 0.3194 -0.0153 0.0037 -0.0029 231 GLU A C 1783 O O . GLU A 228 ? 0.2181 0.2345 0.3309 -0.0147 0.0042 -0.0029 231 GLU A O 1784 C CB . GLU A 228 ? 0.2096 0.2318 0.3223 -0.0182 0.0017 0.0007 231 GLU A CB 1785 C CG . GLU A 228 ? 0.2218 0.2480 0.3397 -0.0158 0.0024 0.0008 231 GLU A CG 1786 C CD . GLU A 228 ? 0.3069 0.3371 0.4275 -0.0153 0.0021 0.0028 231 GLU A CD 1787 O OE1 . GLU A 228 ? 0.3105 0.3416 0.4293 -0.0173 0.0010 0.0044 231 GLU A OE1 1788 O OE2 . GLU A 228 ? 0.2934 0.3254 0.4172 -0.0129 0.0031 0.0029 231 GLU A OE2 1789 N N . PHE A 229 ? 0.2055 0.2228 0.3185 -0.0139 0.0042 -0.0042 232 PHE A N 1790 C CA . PHE A 229 ? 0.2116 0.2286 0.3268 -0.0119 0.0052 -0.0059 232 PHE A CA 1791 C C . PHE A 229 ? 0.2143 0.2343 0.3339 -0.0106 0.0055 -0.0060 232 PHE A C 1792 O O . PHE A 229 ? 0.2077 0.2299 0.3285 -0.0105 0.0051 -0.0052 232 PHE A O 1793 C CB . PHE A 229 ? 0.2012 0.2162 0.3140 -0.0110 0.0056 -0.0074 232 PHE A CB 1794 C CG . PHE A 229 ? 0.2058 0.2169 0.3134 -0.0115 0.0057 -0.0074 232 PHE A CG 1795 C CD1 . PHE A 229 ? 0.2163 0.2261 0.3233 -0.0106 0.0066 -0.0078 232 PHE A CD1 1796 C CD2 . PHE A 229 ? 0.2326 0.2406 0.3352 -0.0129 0.0050 -0.0069 232 PHE A CD2 1797 C CE1 . PHE A 229 ? 0.2108 0.2162 0.3122 -0.0106 0.0070 -0.0077 232 PHE A CE1 1798 C CE2 . PHE A 229 ? 0.2299 0.2326 0.3261 -0.0133 0.0053 -0.0069 232 PHE A CE2 1799 C CZ . PHE A 229 ? 0.1926 0.1940 0.2881 -0.0118 0.0063 -0.0073 232 PHE A CZ 1800 N N . SER A 230 ? 0.2202 0.2401 0.3420 -0.0097 0.0063 -0.0069 233 SER A N 1801 C CA . SER A 230 ? 0.2188 0.2399 0.3436 -0.0086 0.0067 -0.0073 233 SER A CA 1802 C C . SER A 230 ? 0.2216 0.2421 0.3473 -0.0080 0.0073 -0.0092 233 SER A C 1803 O O . SER A 230 ? 0.2069 0.2269 0.3315 -0.0082 0.0075 -0.0097 233 SER A O 1804 C CB . SER A 230 ? 0.2091 0.2302 0.3350 -0.0086 0.0071 -0.0061 233 SER A CB 1805 O OG . SER A 230 ? 0.2313 0.2540 0.3567 -0.0091 0.0064 -0.0041 233 SER A OG 1806 N N . TRP A 231 ? 0.2146 0.2355 0.3422 -0.0072 0.0075 -0.0100 234 TRP A N 1807 C CA . TRP A 231 ? 0.2114 0.2324 0.3400 -0.0071 0.0077 -0.0117 234 TRP A CA 1808 C C . TRP A 231 ? 0.2280 0.2479 0.3578 -0.0072 0.0081 -0.0121 234 TRP A C 1809 O O . TRP A 231 ? 0.2039 0.2227 0.3334 -0.0065 0.0083 -0.0112 234 TRP A O 1810 C CB . TRP A 231 ? 0.2027 0.2246 0.3307 -0.0062 0.0073 -0.0128 234 TRP A CB 1811 C CG . TRP A 231 ? 0.2336 0.2554 0.3617 -0.0053 0.0070 -0.0129 234 TRP A CG 1812 C CD1 . TRP A 231 ? 0.2135 0.2357 0.3406 -0.0049 0.0068 -0.0116 234 TRP A CD1 1813 C CD2 . TRP A 231 ? 0.2566 0.2780 0.3854 -0.0046 0.0070 -0.0141 234 TRP A CD2 1814 N NE1 . TRP A 231 ? 0.2439 0.2662 0.3714 -0.0037 0.0069 -0.0119 234 TRP A NE1 1815 C CE2 . TRP A 231 ? 0.2617 0.2830 0.3898 -0.0034 0.0069 -0.0135 234 TRP A CE2 1816 C CE3 . TRP A 231 ? 0.2634 0.2844 0.3929 -0.0051 0.0069 -0.0155 234 TRP A CE3 1817 C CZ2 . TRP A 231 ? 0.2940 0.3141 0.4218 -0.0023 0.0070 -0.0144 234 TRP A CZ2 1818 C CZ3 . TRP A 231 ? 0.3115 0.3313 0.4406 -0.0045 0.0067 -0.0165 234 TRP A CZ3 1819 C CH2 . TRP A 231 ? 0.2561 0.2750 0.3841 -0.0028 0.0069 -0.0159 234 TRP A CH2 1820 N N . THR A 232 ? 0.2374 0.2575 0.3681 -0.0080 0.0082 -0.0134 235 THR A N 1821 C CA . THR A 232 ? 0.2557 0.2739 0.3866 -0.0086 0.0084 -0.0141 235 THR A CA 1822 C C . THR A 232 ? 0.2667 0.2868 0.3987 -0.0094 0.0079 -0.0158 235 THR A C 1823 O O . THR A 232 ? 0.2444 0.2675 0.3773 -0.0095 0.0077 -0.0161 235 THR A O 1824 C CB . THR A 232 ? 0.2716 0.2877 0.4024 -0.0098 0.0092 -0.0133 235 THR A CB 1825 O OG1 . THR A 232 ? 0.2982 0.3109 0.4279 -0.0101 0.0095 -0.0138 235 THR A OG1 1826 C CG2 . THR A 232 ? 0.2626 0.2806 0.3947 -0.0115 0.0095 -0.0136 235 THR A CG2 1827 N N . LEU A 233 ? 0.2833 0.3014 0.4146 -0.0098 0.0077 -0.0169 236 LEU A N 1828 C CA . LEU A 233 ? 0.2965 0.3161 0.4286 -0.0113 0.0070 -0.0184 236 LEU A CA 1829 C C . LEU A 233 ? 0.3087 0.3267 0.4410 -0.0139 0.0075 -0.0183 236 LEU A C 1830 O O . LEU A 233 ? 0.3005 0.3136 0.4305 -0.0144 0.0080 -0.0182 236 LEU A O 1831 C CB . LEU A 233 ? 0.3086 0.3265 0.4391 -0.0105 0.0063 -0.0196 236 LEU A CB 1832 C CG . LEU A 233 ? 0.3464 0.3668 0.4774 -0.0113 0.0051 -0.0213 236 LEU A CG 1833 C CD1 . LEU A 233 ? 0.3430 0.3689 0.4761 -0.0104 0.0048 -0.0212 236 LEU A CD1 1834 C CD2 . LEU A 233 ? 0.3289 0.3465 0.4576 -0.0098 0.0046 -0.0221 236 LEU A CD2 1835 N N . LEU A 234 ? 0.2893 0.3110 0.4236 -0.0153 0.0077 -0.0181 237 LEU A N 1836 C CA . LEU A 234 ? 0.2777 0.2984 0.4123 -0.0181 0.0083 -0.0179 237 LEU A CA 1837 C C . LEU A 234 ? 0.2905 0.3116 0.4252 -0.0207 0.0075 -0.0193 237 LEU A C 1838 O O . LEU A 234 ? 0.2749 0.3013 0.4116 -0.0211 0.0065 -0.0201 237 LEU A O 1839 C CB . LEU A 234 ? 0.2690 0.2940 0.4060 -0.0185 0.0091 -0.0169 237 LEU A CB 1840 C CG . LEU A 234 ? 0.2869 0.3114 0.4244 -0.0213 0.0100 -0.0163 237 LEU A CG 1841 C CD1 . LEU A 234 ? 0.3113 0.3292 0.4459 -0.0215 0.0109 -0.0154 237 LEU A CD1 1842 C CD2 . LEU A 234 ? 0.2568 0.2863 0.3965 -0.0212 0.0108 -0.0153 237 LEU A CD2 1843 N N . ASP A 235 ? 0.2980 0.3134 0.4299 -0.0226 0.0077 -0.0196 238 ASP A N 1844 C CA . ASP A 235 ? 0.3112 0.3260 0.4422 -0.0257 0.0067 -0.0210 238 ASP A CA 1845 C C . ASP A 235 ? 0.2905 0.3111 0.4246 -0.0291 0.0065 -0.0209 238 ASP A C 1846 O O . ASP A 235 ? 0.2786 0.3014 0.4146 -0.0295 0.0076 -0.0197 238 ASP A O 1847 C CB . ASP A 235 ? 0.3190 0.3248 0.4449 -0.0270 0.0071 -0.0213 238 ASP A CB 1848 C CG . ASP A 235 ? 0.3801 0.3808 0.5025 -0.0238 0.0071 -0.0217 238 ASP A CG 1849 O OD1 . ASP A 235 ? 0.4045 0.4084 0.5282 -0.0215 0.0063 -0.0221 238 ASP A OD1 1850 O OD2 . ASP A 235 ? 0.4402 0.4332 0.5580 -0.0236 0.0080 -0.0215 238 ASP A OD2 1851 N N . MET A 236 ? 0.2936 0.3170 0.4283 -0.0317 0.0051 -0.0221 239 MET A N 1852 C CA . MET A 236 ? 0.2995 0.3286 0.4370 -0.0357 0.0048 -0.0219 239 MET A CA 1853 C C . MET A 236 ? 0.2991 0.3235 0.4349 -0.0387 0.0062 -0.0211 239 MET A C 1854 O O . MET A 236 ? 0.3177 0.3331 0.4485 -0.0395 0.0065 -0.0215 239 MET A O 1855 C CB . MET A 236 ? 0.3039 0.3350 0.4411 -0.0389 0.0029 -0.0234 239 MET A CB 1856 C CG . MET A 236 ? 0.3534 0.3892 0.4920 -0.0360 0.0015 -0.0242 239 MET A CG 1857 S SD . MET A 236 ? 0.4923 0.5296 0.6296 -0.0395 -0.0010 -0.0260 239 MET A SD 1858 C CE . MET A 236 ? 0.5092 0.5326 0.6386 -0.0403 -0.0009 -0.0272 239 MET A CE 1859 N N . TRP A 237 ? 0.2884 0.3184 0.4277 -0.0399 0.0071 -0.0198 240 TRP A N 1860 C CA . TRP A 237 ? 0.2986 0.3255 0.4368 -0.0432 0.0085 -0.0188 240 TRP A CA 1861 C C . TRP A 237 ? 0.2937 0.3132 0.4288 -0.0405 0.0101 -0.0179 240 TRP A C 1862 O O . TRP A 237 ? 0.2893 0.3058 0.4232 -0.0425 0.0115 -0.0169 240 TRP A O 1863 C CB . TRP A 237 ? 0.3141 0.3371 0.4493 -0.0488 0.0076 -0.0198 240 TRP A CB 1864 C CG . TRP A 237 ? 0.3264 0.3558 0.4636 -0.0510 0.0054 -0.0210 240 TRP A CG 1865 C CD1 . TRP A 237 ? 0.3627 0.3876 0.4963 -0.0518 0.0038 -0.0227 240 TRP A CD1 1866 C CD2 . TRP A 237 ? 0.3519 0.3935 0.4952 -0.0521 0.0047 -0.0205 240 TRP A CD2 1867 N NE1 . TRP A 237 ? 0.3599 0.3935 0.4969 -0.0538 0.0019 -0.0233 240 TRP A NE1 1868 C CE2 . TRP A 237 ? 0.3506 0.3948 0.4937 -0.0539 0.0024 -0.0219 240 TRP A CE2 1869 C CE3 . TRP A 237 ? 0.3498 0.4005 0.4983 -0.0516 0.0059 -0.0188 240 TRP A CE3 1870 C CZ2 . TRP A 237 ? 0.3429 0.3991 0.4913 -0.0550 0.0011 -0.0216 240 TRP A CZ2 1871 C CZ3 . TRP A 237 ? 0.3606 0.4229 0.5142 -0.0525 0.0048 -0.0184 240 TRP A CZ3 1872 C CH2 . TRP A 237 ? 0.3763 0.4417 0.5300 -0.0542 0.0024 -0.0198 240 TRP A CH2 1873 N N . ASP A 238 ? 0.2876 0.3050 0.4218 -0.0361 0.0100 -0.0180 241 ASP A N 1874 C CA . ASP A 238 ? 0.2884 0.3009 0.4205 -0.0333 0.0114 -0.0168 241 ASP A CA 1875 C C . ASP A 238 ? 0.2913 0.3095 0.4269 -0.0314 0.0122 -0.0155 241 ASP A C 1876 O O . ASP A 238 ? 0.2901 0.3156 0.4292 -0.0306 0.0117 -0.0156 241 ASP A O 1877 C CB . ASP A 238 ? 0.2684 0.2760 0.3977 -0.0298 0.0110 -0.0172 241 ASP A CB 1878 C CG . ASP A 238 ? 0.2877 0.2891 0.4139 -0.0277 0.0123 -0.0159 241 ASP A CG 1879 O OD1 . ASP A 238 ? 0.2929 0.2917 0.4180 -0.0294 0.0135 -0.0150 241 ASP A OD1 1880 O OD2 . ASP A 238 ? 0.2968 0.2960 0.4216 -0.0244 0.0122 -0.0157 241 ASP A OD2 1881 N N . THR A 239 ? 0.2922 0.3067 0.4262 -0.0304 0.0135 -0.0142 242 THR A N 1882 C CA . THR A 239 ? 0.2894 0.3072 0.4251 -0.0286 0.0145 -0.0128 242 THR A CA 1883 C C . THR A 239 ? 0.2845 0.2996 0.4186 -0.0249 0.0144 -0.0122 242 THR A C 1884 O O . THR A 239 ? 0.2560 0.2655 0.3871 -0.0239 0.0144 -0.0121 242 THR A O 1885 C CB . THR A 239 ? 0.2982 0.3141 0.4332 -0.0309 0.0160 -0.0117 242 THR A CB 1886 O OG1 . THR A 239 ? 0.3347 0.3548 0.4719 -0.0346 0.0160 -0.0120 242 THR A OG1 1887 C CG2 . THR A 239 ? 0.3131 0.3313 0.4489 -0.0288 0.0171 -0.0102 242 THR A CG2 1888 N N . ILE A 240 ? 0.2702 0.2896 0.4059 -0.0227 0.0142 -0.0118 243 ILE A N 1889 C CA . ILE A 240 ? 0.2591 0.2762 0.3930 -0.0199 0.0142 -0.0109 243 ILE A CA 1890 C C . ILE A 240 ? 0.2680 0.2850 0.4013 -0.0197 0.0153 -0.0095 243 ILE A C 1891 O O . ILE A 240 ? 0.2789 0.2996 0.4137 -0.0203 0.0160 -0.0092 243 ILE A O 1892 C CB . ILE A 240 ? 0.2555 0.2756 0.3901 -0.0177 0.0131 -0.0115 243 ILE A CB 1893 C CG1 . ILE A 240 ? 0.2251 0.2429 0.3577 -0.0156 0.0128 -0.0106 243 ILE A CG1 1894 C CG2 . ILE A 240 ? 0.2014 0.2269 0.3378 -0.0174 0.0134 -0.0115 243 ILE A CG2 1895 C CD1 . ILE A 240 ? 0.2823 0.3015 0.4149 -0.0139 0.0117 -0.0112 243 ILE A CD1 1896 N N . ASN A 241 ? 0.2759 0.2889 0.4068 -0.0188 0.0156 -0.0084 244 ASN A N 1897 C CA . ASN A 241 ? 0.2867 0.2991 0.4165 -0.0185 0.0166 -0.0070 244 ASN A CA 1898 C C . ASN A 241 ? 0.2876 0.2992 0.4155 -0.0163 0.0158 -0.0062 244 ASN A C 1899 O O . ASN A 241 ? 0.2817 0.2915 0.4087 -0.0153 0.0150 -0.0059 244 ASN A O 1900 C CB . ASN A 241 ? 0.3120 0.3197 0.4398 -0.0196 0.0176 -0.0061 244 ASN A CB 1901 C CG . ASN A 241 ? 0.3358 0.3437 0.4647 -0.0225 0.0186 -0.0066 244 ASN A CG 1902 O OD1 . ASN A 241 ? 0.4324 0.4438 0.5630 -0.0237 0.0195 -0.0063 244 ASN A OD1 1903 N ND2 . ASN A 241 ? 0.3619 0.3660 0.4895 -0.0237 0.0185 -0.0071 244 ASN A ND2 1904 N N . PHE A 242 ? 0.2666 0.2797 0.3937 -0.0156 0.0161 -0.0057 245 PHE A N 1905 C CA . PHE A 242 ? 0.2758 0.2876 0.4004 -0.0143 0.0153 -0.0049 245 PHE A CA 1906 C C . PHE A 242 ? 0.2904 0.2996 0.4126 -0.0145 0.0161 -0.0035 245 PHE A C 1907 O O . PHE A 242 ? 0.2865 0.2958 0.4089 -0.0151 0.0174 -0.0032 245 PHE A O 1908 C CB . PHE A 242 ? 0.2640 0.2778 0.3878 -0.0133 0.0150 -0.0054 245 PHE A CB 1909 C CG . PHE A 242 ? 0.2748 0.2909 0.4004 -0.0128 0.0141 -0.0066 245 PHE A CG 1910 C CD1 . PHE A 242 ? 0.2713 0.2868 0.3961 -0.0122 0.0128 -0.0067 245 PHE A CD1 1911 C CD2 . PHE A 242 ? 0.2552 0.2746 0.3834 -0.0130 0.0145 -0.0077 245 PHE A CD2 1912 C CE1 . PHE A 242 ? 0.2463 0.2636 0.3724 -0.0116 0.0120 -0.0079 245 PHE A CE1 1913 C CE2 . PHE A 242 ? 0.2399 0.2613 0.3695 -0.0125 0.0136 -0.0089 245 PHE A CE2 1914 C CZ . PHE A 242 ? 0.2469 0.2669 0.3753 -0.0117 0.0124 -0.0090 245 PHE A CZ 1915 N N . GLU A 243 ? 0.3006 0.3078 0.4207 -0.0139 0.0152 -0.0024 246 GLU A N 1916 C CA . GLU A 243 ? 0.3357 0.3403 0.4529 -0.0140 0.0157 -0.0010 246 GLU A CA 1917 C C . GLU A 243 ? 0.3308 0.3346 0.4452 -0.0135 0.0142 -0.0001 246 GLU A C 1918 O O . GLU A 243 ? 0.3460 0.3508 0.4610 -0.0132 0.0129 0.0001 246 GLU A O 1919 C CB . GLU A 243 ? 0.3428 0.3452 0.4603 -0.0143 0.0164 -0.0003 246 GLU A CB 1920 C CG . GLU A 243 ? 0.4037 0.4033 0.5185 -0.0144 0.0172 0.0010 246 GLU A CG 1921 C CD . GLU A 243 ? 0.4907 0.4875 0.6049 -0.0141 0.0177 0.0018 246 GLU A CD 1922 O OE1 . GLU A 243 ? 0.4993 0.4950 0.6147 -0.0150 0.0187 0.0011 246 GLU A OE1 1923 O OE2 . GLU A 243 ? 0.5406 0.5363 0.6527 -0.0131 0.0169 0.0032 246 GLU A OE2 1924 N N . SER A 244 ? 0.3443 0.3463 0.4552 -0.0135 0.0144 0.0004 247 SER A N 1925 C CA . SER A 244 ? 0.3538 0.3549 0.4614 -0.0137 0.0127 0.0012 247 SER A CA 1926 C C . SER A 244 ? 0.3505 0.3481 0.4532 -0.0139 0.0128 0.0023 247 SER A C 1927 O O . SER A 244 ? 0.3589 0.3549 0.4599 -0.0135 0.0143 0.0021 247 SER A O 1928 C CB . SER A 244 ? 0.3525 0.3545 0.4594 -0.0136 0.0119 0.0002 247 SER A CB 1929 O OG . SER A 244 ? 0.3490 0.3494 0.4519 -0.0144 0.0102 0.0010 247 SER A OG 1930 N N . THR A 245 ? 0.3683 0.3652 0.4687 -0.0145 0.0112 0.0036 248 THR A N 1931 C CA . THR A 245 ? 0.3655 0.3589 0.4604 -0.0151 0.0108 0.0046 248 THR A CA 1932 C C . THR A 245 ? 0.3647 0.3564 0.4553 -0.0160 0.0093 0.0043 248 THR A C 1933 O O . THR A 245 ? 0.3731 0.3611 0.4580 -0.0169 0.0086 0.0050 248 THR A O 1934 C CB . THR A 245 ? 0.3732 0.3667 0.4673 -0.0153 0.0097 0.0063 248 THR A CB 1935 O OG1 . THR A 245 ? 0.3731 0.3705 0.4701 -0.0155 0.0081 0.0068 248 THR A OG1 1936 C CG2 . THR A 245 ? 0.3930 0.3860 0.4894 -0.0143 0.0116 0.0066 248 THR A CG2 1937 N N . GLY A 246 ? 0.3438 0.3377 0.4366 -0.0161 0.0089 0.0033 249 GLY A N 1938 C CA . GLY A 246 ? 0.3179 0.3095 0.4062 -0.0171 0.0077 0.0029 249 GLY A CA 1939 C C . GLY A 246 ? 0.2932 0.2884 0.3848 -0.0175 0.0067 0.0023 249 GLY A C 1940 O O . GLY A 246 ? 0.2707 0.2701 0.3672 -0.0173 0.0062 0.0027 249 GLY A O 1941 N N . ASN A 247 ? 0.2863 0.2792 0.3742 -0.0180 0.0063 0.0016 250 ASN A N 1942 C CA . ASN A 247 ? 0.2670 0.2623 0.3566 -0.0187 0.0051 0.0011 250 ASN A CA 1943 C C . ASN A 247 ? 0.2530 0.2515 0.3478 -0.0168 0.0063 -0.0002 250 ASN A C 1944 O O . ASN A 247 ? 0.2483 0.2488 0.3447 -0.0171 0.0056 -0.0006 250 ASN A O 1945 C CB . ASN A 247 ? 0.2646 0.2637 0.3561 -0.0206 0.0031 0.0026 250 ASN A CB 1946 C CG . ASN A 247 ? 0.2915 0.2880 0.3776 -0.0228 0.0015 0.0040 250 ASN A CG 1947 O OD1 . ASN A 247 ? 0.2908 0.2853 0.3753 -0.0224 0.0020 0.0046 250 ASN A OD1 1948 N ND2 . ASN A 247 ? 0.2710 0.2672 0.3537 -0.0255 -0.0004 0.0046 250 ASN A ND2 1949 N N . LEU A 248 ? 0.2542 0.2529 0.3512 -0.0152 0.0081 -0.0008 251 LEU A N 1950 C CA . LEU A 248 ? 0.2266 0.2283 0.3282 -0.0137 0.0092 -0.0021 251 LEU A CA 1951 C C . LEU A 248 ? 0.2293 0.2292 0.3279 -0.0127 0.0097 -0.0032 251 LEU A C 1952 O O . LEU A 248 ? 0.2349 0.2312 0.3287 -0.0119 0.0106 -0.0032 251 LEU A O 1953 C CB . LEU A 248 ? 0.2248 0.2278 0.3296 -0.0128 0.0109 -0.0023 251 LEU A CB 1954 C CG . LEU A 248 ? 0.2286 0.2344 0.3372 -0.0116 0.0120 -0.0036 251 LEU A CG 1955 C CD1 . LEU A 248 ? 0.2153 0.2242 0.3282 -0.0118 0.0112 -0.0043 251 LEU A CD1 1956 C CD2 . LEU A 248 ? 0.2583 0.2651 0.3690 -0.0113 0.0137 -0.0035 251 LEU A CD2 1957 N N . ILE A 249 ? 0.2198 0.2221 0.3208 -0.0123 0.0092 -0.0041 252 ILE A N 1958 C CA . ILE A 249 ? 0.2192 0.2209 0.3188 -0.0107 0.0099 -0.0052 252 ILE A CA 1959 C C . ILE A 249 ? 0.2125 0.2188 0.3180 -0.0094 0.0108 -0.0062 252 ILE A C 1960 O O . ILE A 249 ? 0.2176 0.2268 0.3271 -0.0097 0.0102 -0.0067 252 ILE A O 1961 C CB . ILE A 249 ? 0.2134 0.2141 0.3108 -0.0115 0.0086 -0.0055 252 ILE A CB 1962 C CG1 . ILE A 249 ? 0.2297 0.2268 0.3220 -0.0139 0.0072 -0.0043 252 ILE A CG1 1963 C CG2 . ILE A 249 ? 0.2088 0.2079 0.3035 -0.0095 0.0094 -0.0066 252 ILE A CG2 1964 C CD1 . ILE A 249 ? 0.1948 0.1855 0.2793 -0.0138 0.0077 -0.0040 252 ILE A CD1 1965 N N . ALA A 250 ? 0.1939 0.2007 0.2995 -0.0081 0.0124 -0.0063 253 ALA A N 1966 C CA . ALA A 250 ? 0.1937 0.2052 0.3048 -0.0075 0.0132 -0.0070 253 ALA A CA 1967 C C . ALA A 250 ? 0.1809 0.1949 0.2930 -0.0059 0.0133 -0.0081 253 ALA A C 1968 O O . ALA A 250 ? 0.1828 0.1945 0.2904 -0.0043 0.0136 -0.0082 253 ALA A O 1969 C CB . ALA A 250 ? 0.1783 0.1905 0.2899 -0.0072 0.0148 -0.0064 253 ALA A CB 1970 N N . PRO A 251 ? 0.1740 0.1922 0.2913 -0.0062 0.0130 -0.0090 254 PRO A N 1971 C CA . PRO A 251 ? 0.1737 0.1950 0.2919 -0.0045 0.0132 -0.0099 254 PRO A CA 1972 C C . PRO A 251 ? 0.1841 0.2082 0.3029 -0.0032 0.0148 -0.0095 254 PRO A C 1973 O O . PRO A 251 ? 0.1828 0.2078 0.3034 -0.0044 0.0156 -0.0088 254 PRO A O 1974 C CB . PRO A 251 ? 0.1787 0.2035 0.3020 -0.0056 0.0125 -0.0109 254 PRO A CB 1975 C CG . PRO A 251 ? 0.1784 0.2027 0.3039 -0.0078 0.0127 -0.0102 254 PRO A CG 1976 C CD . PRO A 251 ? 0.1851 0.2050 0.3067 -0.0080 0.0126 -0.0091 254 PRO A CD 1977 N N . GLU A 252 ? 0.1813 0.2067 0.2982 -0.0006 0.0155 -0.0097 255 GLU A N 1978 C CA . GLU A 252 ? 0.1897 0.2202 0.3086 0.0008 0.0169 -0.0092 255 GLU A CA 1979 C C . GLU A 252 ? 0.1887 0.2257 0.3130 0.0005 0.0162 -0.0101 255 GLU A C 1980 O O . GLU A 252 ? 0.1884 0.2314 0.3167 0.0002 0.0170 -0.0097 255 GLU A O 1981 C CB . GLU A 252 ? 0.1866 0.2152 0.3000 0.0045 0.0182 -0.0086 255 GLU A CB 1982 C CG . GLU A 252 ? 0.2445 0.2784 0.3597 0.0063 0.0202 -0.0076 255 GLU A CG 1983 C CD . GLU A 252 ? 0.3100 0.3420 0.4193 0.0106 0.0219 -0.0067 255 GLU A CD 1984 O OE1 . GLU A 252 ? 0.3096 0.3361 0.4131 0.0124 0.0215 -0.0072 255 GLU A OE1 1985 O OE2 . GLU A 252 ? 0.3049 0.3409 0.4153 0.0122 0.0238 -0.0055 255 GLU A OE2 1986 N N . TYR A 253 ? 0.1857 0.2219 0.3101 0.0003 0.0148 -0.0112 256 TYR A N 1987 C CA . TYR A 253 ? 0.1924 0.2341 0.3210 0.0001 0.0139 -0.0122 256 TYR A CA 1988 C C . TYR A 253 ? 0.2045 0.2455 0.3359 -0.0026 0.0124 -0.0132 256 TYR A C 1989 O O . TYR A 253 ? 0.2154 0.2516 0.3452 -0.0037 0.0120 -0.0131 256 TYR A O 1990 C CB . TYR A 253 ? 0.1872 0.2289 0.3130 0.0032 0.0136 -0.0127 256 TYR A CB 1991 C CG . TYR A 253 ? 0.2081 0.2510 0.3308 0.0067 0.0152 -0.0117 256 TYR A CG 1992 C CD1 . TYR A 253 ? 0.2122 0.2630 0.3382 0.0084 0.0159 -0.0113 256 TYR A CD1 1993 C CD2 . TYR A 253 ? 0.2574 0.2935 0.3734 0.0084 0.0162 -0.0111 256 TYR A CD2 1994 C CE1 . TYR A 253 ? 0.2409 0.2929 0.3635 0.0125 0.0178 -0.0101 256 TYR A CE1 1995 C CE2 . TYR A 253 ? 0.2477 0.2834 0.3595 0.0121 0.0179 -0.0101 256 TYR A CE2 1996 C CZ . TYR A 253 ? 0.2943 0.3380 0.4095 0.0144 0.0188 -0.0096 256 TYR A CZ 1997 O OH . TYR A 253 ? 0.3419 0.3847 0.4521 0.0187 0.0208 -0.0084 256 TYR A OH 1998 N N . GLY A 254 ? 0.1901 0.2360 0.3255 -0.0036 0.0117 -0.0141 257 GLY A N 1999 C CA . GLY A 254 ? 0.2089 0.2535 0.3457 -0.0055 0.0102 -0.0152 257 GLY A CA 2000 C C . GLY A 254 ? 0.1997 0.2475 0.3370 -0.0040 0.0092 -0.0163 257 GLY A C 2001 O O . GLY A 254 ? 0.2266 0.2796 0.3649 -0.0024 0.0095 -0.0161 257 GLY A O 2002 N N . PHE A 255 ? 0.1908 0.2358 0.3273 -0.0043 0.0081 -0.0173 258 PHE A N 2003 C CA . PHE A 255 ? 0.1792 0.2271 0.3160 -0.0030 0.0071 -0.0184 258 PHE A CA 2004 C C . PHE A 255 ? 0.1918 0.2415 0.3314 -0.0058 0.0059 -0.0194 258 PHE A C 2005 O O . PHE A 255 ? 0.1697 0.2151 0.3085 -0.0070 0.0054 -0.0200 258 PHE A O 2006 C CB . PHE A 255 ? 0.1831 0.2266 0.3165 -0.0012 0.0066 -0.0188 258 PHE A CB 2007 C CG . PHE A 255 ? 0.1687 0.2095 0.2981 0.0012 0.0076 -0.0179 258 PHE A CG 2008 C CD1 . PHE A 255 ? 0.2050 0.2476 0.3323 0.0041 0.0078 -0.0180 258 PHE A CD1 2009 C CD2 . PHE A 255 ? 0.2020 0.2382 0.3291 0.0005 0.0083 -0.0170 258 PHE A CD2 2010 C CE1 . PHE A 255 ? 0.2413 0.2800 0.3636 0.0065 0.0088 -0.0173 258 PHE A CE1 2011 C CE2 . PHE A 255 ? 0.2000 0.2327 0.3223 0.0024 0.0090 -0.0163 258 PHE A CE2 2012 C CZ . PHE A 255 ? 0.1960 0.2294 0.3155 0.0054 0.0093 -0.0164 258 PHE A CZ 2013 N N . LYS A 256 ? 0.1814 0.2375 0.3240 -0.0068 0.0055 -0.0195 259 LYS A N 2014 C CA . LYS A 256 ? 0.1958 0.2536 0.3404 -0.0098 0.0042 -0.0205 259 LYS A CA 2015 C C . LYS A 256 ? 0.2064 0.2638 0.3496 -0.0085 0.0028 -0.0219 259 LYS A C 2016 O O . LYS A 256 ? 0.2025 0.2632 0.3452 -0.0056 0.0025 -0.0219 259 LYS A O 2017 C CB . LYS A 256 ? 0.2135 0.2797 0.3619 -0.0112 0.0041 -0.0200 259 LYS A CB 2018 C CG . LYS A 256 ? 0.2363 0.3051 0.3865 -0.0150 0.0025 -0.0210 259 LYS A CG 2019 C CD . LYS A 256 ? 0.2846 0.3640 0.4389 -0.0157 0.0022 -0.0203 259 LYS A CD 2020 C CE . LYS A 256 ? 0.3477 0.4313 0.5033 -0.0182 0.0000 -0.0214 259 LYS A CE 2021 N NZ . LYS A 256 ? 0.3278 0.4212 0.4879 -0.0212 -0.0002 -0.0204 259 LYS A NZ 2022 N N . ILE A 257 ? 0.2097 0.2624 0.3515 -0.0102 0.0019 -0.0229 260 ILE A N 2023 C CA . ILE A 257 ? 0.2426 0.2946 0.3827 -0.0091 0.0006 -0.0242 260 ILE A CA 2024 C C . ILE A 257 ? 0.2661 0.3251 0.4086 -0.0105 -0.0008 -0.0248 260 ILE A C 2025 O O . ILE A 257 ? 0.2852 0.3450 0.4289 -0.0143 -0.0016 -0.0253 260 ILE A O 2026 C CB . ILE A 257 ? 0.2550 0.3001 0.3927 -0.0104 0.0002 -0.0251 260 ILE A CB 2027 C CG1 . ILE A 257 ? 0.2444 0.2841 0.3803 -0.0089 0.0016 -0.0241 260 ILE A CG1 2028 C CG2 . ILE A 257 ? 0.2730 0.3174 0.4088 -0.0095 -0.0011 -0.0265 260 ILE A CG2 2029 C CD1 . ILE A 257 ? 0.2651 0.2982 0.3986 -0.0096 0.0017 -0.0245 260 ILE A CD1 2030 N N . SER A 258 ? 0.2692 0.3332 0.4121 -0.0077 -0.0012 -0.0248 261 SER A N 2031 C CA . SER A 258 ? 0.2947 0.3671 0.4403 -0.0088 -0.0027 -0.0250 261 SER A CA 2032 C C . SER A 258 ? 0.3149 0.3871 0.4588 -0.0085 -0.0046 -0.0265 261 SER A C 2033 O O . SER A 258 ? 0.3160 0.3947 0.4619 -0.0102 -0.0063 -0.0269 261 SER A O 2034 C CB . SER A 258 ? 0.2812 0.3609 0.4287 -0.0056 -0.0018 -0.0236 261 SER A CB 2035 O OG . SER A 258 ? 0.2984 0.3747 0.4425 -0.0011 -0.0008 -0.0234 261 SER A OG 2036 N N . LYS A 259 ? 0.3267 0.3920 0.4668 -0.0063 -0.0044 -0.0272 262 LYS A N 2037 C CA . LYS A 259 ? 0.3364 0.4002 0.4742 -0.0059 -0.0060 -0.0286 262 LYS A CA 2038 C C . LYS A 259 ? 0.3436 0.3981 0.4775 -0.0052 -0.0054 -0.0293 262 LYS A C 2039 O O . LYS A 259 ? 0.3153 0.3661 0.4478 -0.0029 -0.0039 -0.0285 262 LYS A O 2040 C CB . LYS A 259 ? 0.3487 0.4175 0.4861 -0.0020 -0.0064 -0.0284 262 LYS A CB 2041 C CG . LYS A 259 ? 0.4027 0.4728 0.5386 -0.0021 -0.0086 -0.0298 262 LYS A CG 2042 C CD . LYS A 259 ? 0.4842 0.5645 0.6228 -0.0011 -0.0098 -0.0294 262 LYS A CD 2043 C CE . LYS A 259 ? 0.5371 0.6187 0.6735 0.0000 -0.0119 -0.0306 262 LYS A CE 2044 N NZ . LYS A 259 ? 0.5550 0.6298 0.6884 -0.0029 -0.0132 -0.0323 262 LYS A NZ 2045 N N . ARG A 260 ? 0.3432 0.3941 0.4751 -0.0074 -0.0067 -0.0306 263 ARG A N 2046 C CA . ARG A 260 ? 0.3604 0.4029 0.4886 -0.0068 -0.0061 -0.0311 263 ARG A CA 2047 C C . ARG A 260 ? 0.3598 0.4008 0.4848 -0.0050 -0.0073 -0.0323 263 ARG A C 2048 O O . ARG A 260 ? 0.3444 0.3900 0.4699 -0.0058 -0.0091 -0.0331 263 ARG A O 2049 C CB . ARG A 260 ? 0.3748 0.4126 0.5019 -0.0105 -0.0062 -0.0316 263 ARG A CB 2050 C CG . ARG A 260 ? 0.4049 0.4421 0.5341 -0.0119 -0.0047 -0.0303 263 ARG A CG 2051 C CD . ARG A 260 ? 0.4279 0.4614 0.5559 -0.0160 -0.0051 -0.0308 263 ARG A CD 2052 N NE . ARG A 260 ? 0.4425 0.4753 0.5722 -0.0173 -0.0036 -0.0296 263 ARG A NE 2053 C CZ . ARG A 260 ? 0.4316 0.4592 0.5600 -0.0157 -0.0020 -0.0287 263 ARG A CZ 2054 N NH1 . ARG A 260 ? 0.4424 0.4653 0.5679 -0.0129 -0.0015 -0.0288 263 ARG A NH1 2055 N NH2 . ARG A 260 ? 0.4266 0.4538 0.5565 -0.0170 -0.0008 -0.0276 263 ARG A NH2 2056 N N . GLY A 261 A 0.3535 0.3886 0.4754 -0.0026 -0.0063 -0.0323 263 GLY A N 2057 C CA . GLY A 261 A 0.3590 0.3919 0.4775 -0.0010 -0.0072 -0.0334 263 GLY A CA 2058 C C . GLY A 261 A 0.3714 0.3998 0.4874 0.0022 -0.0057 -0.0329 263 GLY A C 2059 O O . GLY A 261 A 0.3649 0.3923 0.4820 0.0030 -0.0040 -0.0316 263 GLY A O 2060 N N . SER A 262 ? 0.3811 0.4070 0.4937 0.0040 -0.0063 -0.0338 264 SER A N 2061 C CA . SER A 262 ? 0.4050 0.4268 0.5150 0.0069 -0.0048 -0.0332 264 SER A CA 2062 C C . SER A 262 ? 0.3935 0.4184 0.5044 0.0092 -0.0040 -0.0322 264 SER A C 2063 O O . SER A 262 ? 0.4038 0.4326 0.5148 0.0103 -0.0051 -0.0327 264 SER A O 2064 C CB . SER A 262 ? 0.4131 0.4312 0.5188 0.0082 -0.0055 -0.0344 264 SER A CB 2065 O OG . SER A 262 ? 0.4796 0.4931 0.5831 0.0102 -0.0037 -0.0335 264 SER A OG 2066 N N . SER A 263 ? 0.3795 0.4026 0.4908 0.0099 -0.0023 -0.0308 265 SER A N 2067 C CA . SER A 263 ? 0.3726 0.3974 0.4838 0.0116 -0.0015 -0.0298 265 SER A CA 2068 C C . SER A 263 ? 0.3647 0.3856 0.4742 0.0125 0.0001 -0.0286 265 SER A C 2069 O O . SER A 263 ? 0.3758 0.3935 0.4835 0.0130 0.0004 -0.0288 265 SER A O 2070 C CB . SER A 263 ? 0.3636 0.3921 0.4781 0.0102 -0.0014 -0.0291 265 SER A CB 2071 O OG . SER A 263 ? 0.4212 0.4507 0.5345 0.0122 -0.0007 -0.0283 265 SER A OG 2072 N N . GLY A 264 ? 0.3420 0.3631 0.4516 0.0127 0.0011 -0.0273 266 GLY A N 2073 C CA . GLY A 264 ? 0.3306 0.3489 0.4391 0.0126 0.0025 -0.0259 266 GLY A CA 2074 C C . GLY A 264 ? 0.3153 0.3331 0.4221 0.0131 0.0032 -0.0249 266 GLY A C 2075 O O . GLY A 264 ? 0.2893 0.3083 0.3950 0.0142 0.0029 -0.0253 266 GLY A O 2076 N N . ILE A 265 ? 0.3080 0.3241 0.4142 0.0122 0.0043 -0.0234 267 ILE A N 2077 C CA . ILE A 265 ? 0.3120 0.3266 0.4157 0.0120 0.0050 -0.0223 267 ILE A CA 2078 C C . ILE A 265 ? 0.3208 0.3328 0.4209 0.0130 0.0056 -0.0219 267 ILE A C 2079 O O . ILE A 265 ? 0.3316 0.3434 0.4324 0.0126 0.0062 -0.0212 267 ILE A O 2080 C CB . ILE A 265 ? 0.3118 0.3266 0.4171 0.0097 0.0055 -0.0208 267 ILE A CB 2081 C CG1 . ILE A 265 ? 0.3175 0.3345 0.4258 0.0088 0.0050 -0.0211 267 ILE A CG1 2082 C CG2 . ILE A 265 ? 0.3286 0.3405 0.4298 0.0090 0.0061 -0.0196 267 ILE A CG2 2083 C CD1 . ILE A 265 ? 0.3490 0.3664 0.4593 0.0065 0.0054 -0.0197 267 ILE A CD1 2084 N N . MET A 266 ? 0.3081 0.3179 0.4040 0.0146 0.0057 -0.0223 268 MET A N 2085 C CA . MET A 266 ? 0.3267 0.3334 0.4185 0.0153 0.0065 -0.0219 268 MET A CA 2086 C C . MET A 266 ? 0.3241 0.3276 0.4124 0.0137 0.0073 -0.0204 268 MET A C 2087 O O . MET A 266 ? 0.3002 0.3022 0.3862 0.0138 0.0073 -0.0205 268 MET A O 2088 C CB . MET A 266 ? 0.3286 0.3342 0.4171 0.0183 0.0061 -0.0232 268 MET A CB 2089 C CG . MET A 266 ? 0.3937 0.3952 0.4771 0.0191 0.0070 -0.0227 268 MET A CG 2090 S SD . MET A 266 ? 0.5029 0.5035 0.5825 0.0230 0.0065 -0.0243 268 MET A SD 2091 C CE . MET A 266 ? 0.3635 0.3675 0.4475 0.0234 0.0054 -0.0255 268 MET A CE 2092 N N . LYS A 267 ? 0.3143 0.3169 0.4018 0.0120 0.0081 -0.0191 269 LYS A N 2093 C CA . LYS A 267 ? 0.3217 0.3212 0.4055 0.0097 0.0087 -0.0176 269 LYS A CA 2094 C C . LYS A 267 ? 0.3245 0.3188 0.4014 0.0110 0.0094 -0.0178 269 LYS A C 2095 O O . LYS A 267 ? 0.3258 0.3196 0.4016 0.0121 0.0098 -0.0179 269 LYS A O 2096 C CB . LYS A 267 ? 0.3341 0.3360 0.4205 0.0069 0.0092 -0.0157 269 LYS A CB 2097 C CG . LYS A 267 ? 0.3657 0.3717 0.4576 0.0053 0.0086 -0.0151 269 LYS A CG 2098 C CD . LYS A 267 ? 0.4070 0.4109 0.4967 0.0028 0.0084 -0.0144 269 LYS A CD 2099 C CE . LYS A 267 ? 0.4177 0.4254 0.5122 0.0011 0.0079 -0.0135 269 LYS A CE 2100 N NZ . LYS A 267 ? 0.3883 0.3930 0.4795 -0.0011 0.0076 -0.0130 269 LYS A NZ 2101 N N . THR A 268 ? 0.3121 0.3022 0.3840 0.0112 0.0095 -0.0180 270 THR A N 2102 C CA . THR A 268 ? 0.3196 0.3038 0.3839 0.0130 0.0102 -0.0182 270 THR A CA 2103 C C . THR A 268 ? 0.3282 0.3067 0.3863 0.0120 0.0106 -0.0177 270 THR A C 2104 O O . THR A 268 ? 0.3097 0.2897 0.3699 0.0117 0.0102 -0.0178 270 THR A O 2105 C CB . THR A 268 ? 0.3243 0.3093 0.3882 0.0175 0.0099 -0.0199 270 THR A CB 2106 O OG1 . THR A 268 ? 0.3170 0.2958 0.3729 0.0196 0.0107 -0.0201 270 THR A OG1 2107 C CG2 . THR A 268 ? 0.3378 0.3267 0.4055 0.0190 0.0090 -0.0208 270 THR A CG2 2108 N N . GLU A 269 ? 0.3312 0.3028 0.3813 0.0116 0.0116 -0.0172 271 GLU A N 2109 C CA . GLU A 269 ? 0.3487 0.3127 0.3906 0.0111 0.0122 -0.0168 271 GLU A CA 2110 C C . GLU A 269 ? 0.3580 0.3182 0.3943 0.0162 0.0127 -0.0179 271 GLU A C 2111 O O . GLU A 269 ? 0.3743 0.3278 0.4031 0.0170 0.0134 -0.0177 271 GLU A O 2112 C CB . GLU A 269 ? 0.3658 0.3235 0.4009 0.0072 0.0129 -0.0154 271 GLU A CB 2113 C CG . GLU A 269 ? 0.3686 0.3317 0.4098 0.0024 0.0124 -0.0140 271 GLU A CG 2114 C CD . GLU A 269 ? 0.3765 0.3441 0.4233 0.0003 0.0115 -0.0135 271 GLU A CD 2115 O OE1 . GLU A 269 ? 0.3755 0.3384 0.4176 -0.0007 0.0114 -0.0134 271 GLU A OE1 2116 O OE2 . GLU A 269 ? 0.3907 0.3661 0.4462 0.0000 0.0108 -0.0133 271 GLU A OE2 2117 N N . GLY A 270 ? 0.3409 0.3054 0.3807 0.0197 0.0124 -0.0190 272 GLY A N 2118 C CA . GLY A 270 ? 0.3456 0.3074 0.3803 0.0248 0.0128 -0.0199 272 GLY A CA 2119 C C . GLY A 270 ? 0.3425 0.3081 0.3796 0.0278 0.0124 -0.0205 272 GLY A C 2120 O O . GLY A 270 ? 0.3370 0.3064 0.3793 0.0257 0.0118 -0.0202 272 GLY A O 2121 N N . THR A 271 ? 0.3390 0.3037 0.3723 0.0327 0.0127 -0.0210 273 THR A N 2122 C CA . THR A 271 ? 0.3414 0.3100 0.3763 0.0361 0.0125 -0.0213 273 THR A CA 2123 C C . THR A 271 ? 0.3266 0.3020 0.3653 0.0401 0.0115 -0.0223 273 THR A C 2124 O O . THR A 271 ? 0.3303 0.3043 0.3668 0.0414 0.0115 -0.0227 273 THR A O 2125 C CB . THR A 271 ? 0.3621 0.3219 0.3864 0.0387 0.0142 -0.0205 273 THR A CB 2126 O OG1 . THR A 271 ? 0.3879 0.3520 0.4146 0.0411 0.0142 -0.0204 273 THR A OG1 2127 C CG2 . THR A 271 ? 0.3735 0.3274 0.3891 0.0431 0.0152 -0.0206 273 THR A CG2 2128 N N . LEU A 272 ? 0.3173 0.3004 0.3617 0.0418 0.0108 -0.0226 274 LEU A N 2129 C CA . LEU A 272 ? 0.3131 0.3038 0.3620 0.0447 0.0094 -0.0234 274 LEU A CA 2130 C C . LEU A 272 ? 0.3217 0.3093 0.3630 0.0503 0.0102 -0.0233 274 LEU A C 2131 O O . LEU A 272 ? 0.3141 0.2972 0.3489 0.0532 0.0117 -0.0224 274 LEU A O 2132 C CB . LEU A 272 ? 0.3130 0.3130 0.3695 0.0448 0.0085 -0.0235 274 LEU A CB 2133 C CG . LEU A 272 ? 0.2936 0.3026 0.3547 0.0476 0.0069 -0.0242 274 LEU A CG 2134 C CD1 . LEU A 272 ? 0.2863 0.2978 0.3516 0.0454 0.0053 -0.0254 274 LEU A CD1 2135 C CD2 . LEU A 272 ? 0.2834 0.3011 0.3517 0.0469 0.0063 -0.0239 274 LEU A CD2 2136 N N . GLU A 273 ? 0.3203 0.3099 0.3619 0.0520 0.0093 -0.0241 275 GLU A N 2137 C CA . GLU A 273 ? 0.3487 0.3365 0.3838 0.0576 0.0098 -0.0240 275 GLU A CA 2138 C C . GLU A 273 ? 0.3547 0.3535 0.3958 0.0605 0.0080 -0.0245 275 GLU A C 2139 O O . GLU A 273 ? 0.3343 0.3411 0.3843 0.0576 0.0062 -0.0252 275 GLU A O 2140 C CB . GLU A 273 ? 0.3594 0.3397 0.3881 0.0578 0.0104 -0.0243 275 GLU A CB 2141 C CG . GLU A 273 ? 0.3902 0.3590 0.4108 0.0557 0.0124 -0.0234 275 GLU A CG 2142 C CD . GLU A 273 ? 0.4364 0.3978 0.4507 0.0555 0.0132 -0.0235 275 GLU A CD 2143 O OE1 . GLU A 273 ? 0.4606 0.4198 0.4692 0.0601 0.0135 -0.0236 275 GLU A OE1 2144 O OE2 . GLU A 273 ? 0.4348 0.3930 0.4498 0.0507 0.0134 -0.0233 275 GLU A OE2 2145 N N . ASN A 274 ? 0.3752 0.3742 0.4110 0.0663 0.0085 -0.0240 276 ASN A N 2146 C CA . ASN A 274 ? 0.3967 0.4067 0.4376 0.0694 0.0068 -0.0241 276 ASN A CA 2147 C C . ASN A 274 ? 0.4066 0.4188 0.4489 0.0692 0.0049 -0.0254 276 ASN A C 2148 O O . ASN A 274 ? 0.4154 0.4253 0.4517 0.0737 0.0051 -0.0253 276 ASN A O 2149 C CB . ASN A 274 ? 0.4029 0.4132 0.4376 0.0763 0.0081 -0.0228 276 ASN A CB 2150 C CG . ASN A 274 ? 0.4275 0.4513 0.4685 0.0793 0.0062 -0.0226 276 ASN A CG 2151 O OD1 . ASN A 274 ? 0.4297 0.4621 0.4796 0.0756 0.0038 -0.0236 276 ASN A OD1 2152 N ND2 . ASN A 274 ? 0.4309 0.4565 0.4671 0.0859 0.0072 -0.0213 276 ASN A ND2 2153 N N . CYS A 275 ? 0.4057 0.4217 0.4554 0.0642 0.0033 -0.0265 277 CYS A N 2154 C CA . CYS A 275 ? 0.4170 0.4342 0.4682 0.0631 0.0016 -0.0278 277 CYS A CA 2155 C C . CYS A 275 ? 0.4017 0.4262 0.4621 0.0584 -0.0004 -0.0287 277 CYS A C 2156 O O . CYS A 275 ? 0.3777 0.4048 0.4431 0.0553 -0.0002 -0.0284 277 CYS A O 2157 C CB . CYS A 275 ? 0.4262 0.4332 0.4720 0.0615 0.0029 -0.0281 277 CYS A CB 2158 S SG . CYS A 275 ? 0.5260 0.5273 0.5739 0.0556 0.0043 -0.0277 277 CYS A SG 2159 N N . GLU A 276 ? 0.4004 0.4272 0.4622 0.0578 -0.0023 -0.0299 278 GLU A N 2160 C CA . GLU A 276 ? 0.4095 0.4433 0.4786 0.0541 -0.0046 -0.0309 278 GLU A CA 2161 C C . GLU A 276 ? 0.4011 0.4298 0.4693 0.0516 -0.0050 -0.0321 278 GLU A C 2162 O O . GLU A 276 ? 0.4161 0.4398 0.4787 0.0540 -0.0046 -0.0324 278 GLU A O 2163 C CB . GLU A 276 ? 0.4249 0.4679 0.4956 0.0569 -0.0068 -0.0311 278 GLU A CB 2164 C CG . GLU A 276 ? 0.4705 0.5201 0.5468 0.0533 -0.0096 -0.0323 278 GLU A CG 2165 C CD . GLU A 276 ? 0.5142 0.5664 0.5971 0.0483 -0.0098 -0.0324 278 GLU A CD 2166 O OE1 . GLU A 276 ? 0.5053 0.5589 0.5898 0.0487 -0.0083 -0.0312 278 GLU A OE1 2167 O OE2 . GLU A 276 ? 0.5626 0.6148 0.6482 0.0443 -0.0112 -0.0336 278 GLU A OE2 2168 N N . THR A 277 ? 0.3807 0.4103 0.4539 0.0470 -0.0057 -0.0328 279 THR A N 2169 C CA . THR A 277 ? 0.3713 0.3964 0.4437 0.0450 -0.0060 -0.0338 279 THR A CA 2170 C C . THR A 277 ? 0.3756 0.4041 0.4535 0.0407 -0.0076 -0.0348 279 THR A C 2171 O O . THR A 277 ? 0.3734 0.4069 0.4563 0.0386 -0.0081 -0.0344 279 THR A O 2172 C CB . THR A 277 ? 0.3697 0.3865 0.4390 0.0442 -0.0035 -0.0331 279 THR A CB 2173 O OG1 . THR A 277 ? 0.3455 0.3582 0.4131 0.0433 -0.0035 -0.0338 279 THR A OG1 2174 C CG2 . THR A 277 ? 0.3523 0.3694 0.4261 0.0406 -0.0025 -0.0323 279 THR A CG2 2175 N N . LYS A 278 ? 0.3734 0.3984 0.4499 0.0395 -0.0083 -0.0358 280 LYS A N 2176 C CA . LYS A 278 ? 0.3820 0.4078 0.4620 0.0356 -0.0095 -0.0367 280 LYS A CA 2177 C C . LYS A 278 ? 0.3660 0.3859 0.4461 0.0337 -0.0074 -0.0362 280 LYS A C 2178 O O . LYS A 278 ? 0.3662 0.3859 0.4492 0.0306 -0.0077 -0.0365 280 LYS A O 2179 C CB . LYS A 278 ? 0.4014 0.4266 0.4789 0.0356 -0.0116 -0.0383 280 LYS A CB 2180 C CG . LYS A 278 ? 0.4521 0.4843 0.5298 0.0370 -0.0141 -0.0389 280 LYS A CG 2181 C CD . LYS A 278 ? 0.5293 0.5590 0.6025 0.0378 -0.0159 -0.0403 280 LYS A CD 2182 C CE . LYS A 278 ? 0.5655 0.6021 0.6382 0.0397 -0.0184 -0.0407 280 LYS A CE 2183 N NZ . LYS A 278 ? 0.6189 0.6512 0.6852 0.0427 -0.0190 -0.0415 280 LYS A NZ 2184 N N . CYS A 279 ? 0.3570 0.3718 0.4335 0.0357 -0.0053 -0.0352 281 CYS A N 2185 C CA . CYS A 279 ? 0.3530 0.3629 0.4294 0.0343 -0.0033 -0.0344 281 CYS A CA 2186 C C . CYS A 279 ? 0.3364 0.3438 0.4111 0.0351 -0.0011 -0.0329 281 CYS A C 2187 O O . CYS A 279 ? 0.3340 0.3384 0.4038 0.0377 -0.0003 -0.0326 281 CYS A O 2188 C CB . CYS A 279 ? 0.3662 0.3712 0.4384 0.0355 -0.0029 -0.0350 281 CYS A CB 2189 S SG . CYS A 279 ? 0.4338 0.4339 0.5057 0.0344 -0.0002 -0.0336 281 CYS A SG 2190 N N . GLN A 280 ? 0.3091 0.3174 0.3873 0.0328 -0.0002 -0.0319 282 GLN A N 2191 C CA . GLN A 280 ? 0.3116 0.3172 0.3881 0.0327 0.0016 -0.0304 282 GLN A CA 2192 C C . GLN A 280 ? 0.3086 0.3110 0.3854 0.0307 0.0032 -0.0292 282 GLN A C 2193 O O . GLN A 280 ? 0.3071 0.3109 0.3877 0.0286 0.0030 -0.0292 282 GLN A O 2194 C CB . GLN A 280 ? 0.3073 0.3162 0.3869 0.0315 0.0014 -0.0298 282 GLN A CB 2195 C CG . GLN A 280 ? 0.2938 0.2991 0.3703 0.0316 0.0031 -0.0284 282 GLN A CG 2196 C CD . GLN A 280 ? 0.2911 0.2935 0.3614 0.0351 0.0036 -0.0284 282 GLN A CD 2197 O OE1 . GLN A 280 ? 0.2685 0.2740 0.3383 0.0376 0.0026 -0.0290 282 GLN A OE1 2198 N NE2 . GLN A 280 ? 0.2617 0.2583 0.3269 0.0353 0.0051 -0.0276 282 GLN A NE2 2199 N N . THR A 281 ? 0.3087 0.3069 0.3812 0.0314 0.0048 -0.0282 283 THR A N 2200 C CA . THR A 281 ? 0.3257 0.3220 0.3986 0.0292 0.0064 -0.0266 283 THR A CA 2201 C C . THR A 281 ? 0.3378 0.3320 0.4087 0.0279 0.0075 -0.0252 283 THR A C 2202 O O . THR A 281 ? 0.3559 0.3486 0.4234 0.0295 0.0073 -0.0255 283 THR A O 2203 C CB . THR A 281 ? 0.3205 0.3136 0.3901 0.0302 0.0077 -0.0261 283 THR A CB 2204 O OG1 . THR A 281 ? 0.3132 0.3022 0.3773 0.0309 0.0089 -0.0253 283 THR A OG1 2205 C CG2 . THR A 281 ? 0.3241 0.3171 0.3925 0.0327 0.0066 -0.0277 283 THR A CG2 2206 N N . PRO A 282 ? 0.3550 0.3490 0.4275 0.0251 0.0085 -0.0237 284 PRO A N 2207 C CA . PRO A 282 ? 0.3662 0.3576 0.4360 0.0233 0.0094 -0.0224 284 PRO A CA 2208 C C . PRO A 282 ? 0.3726 0.3583 0.4349 0.0245 0.0104 -0.0220 284 PRO A C 2209 O O . PRO A 282 ? 0.3812 0.3634 0.4394 0.0240 0.0109 -0.0215 284 PRO A O 2210 C CB . PRO A 282 ? 0.3574 0.3506 0.4307 0.0199 0.0101 -0.0207 284 PRO A CB 2211 C CG . PRO A 282 ? 0.3639 0.3613 0.4428 0.0202 0.0094 -0.0213 284 PRO A CG 2212 C CD . PRO A 282 ? 0.3532 0.3499 0.4303 0.0234 0.0088 -0.0230 284 PRO A CD 2213 N N . LEU A 283 ? 0.3771 0.3613 0.4370 0.0264 0.0108 -0.0224 285 LEU A N 2214 C CA . LEU A 283 ? 0.3802 0.3585 0.4325 0.0278 0.0119 -0.0221 285 LEU A CA 2215 C C . LEU A 283 ? 0.3704 0.3468 0.4186 0.0317 0.0112 -0.0235 285 LEU A C 2216 O O . LEU A 283 ? 0.3867 0.3576 0.4279 0.0331 0.0121 -0.0232 285 LEU A O 2217 C CB . LEU A 283 ? 0.3881 0.3654 0.4392 0.0280 0.0130 -0.0215 285 LEU A CB 2218 C CG . LEU A 283 ? 0.4272 0.4068 0.4818 0.0245 0.0140 -0.0197 285 LEU A CG 2219 C CD1 . LEU A 283 ? 0.4585 0.4374 0.5117 0.0256 0.0153 -0.0191 285 LEU A CD1 2220 C CD2 . LEU A 283 ? 0.4621 0.4389 0.5139 0.0210 0.0149 -0.0180 285 LEU A CD2 2221 N N . GLY A 284 ? 0.3551 0.3364 0.4075 0.0336 0.0096 -0.0249 286 GLY A N 2222 C CA . GLY A 284 ? 0.3333 0.3149 0.3830 0.0376 0.0087 -0.0262 286 GLY A CA 2223 C C . GLY A 284 ? 0.3175 0.3044 0.3720 0.0386 0.0068 -0.0276 286 GLY A C 2224 O O . GLY A 284 ? 0.3100 0.2991 0.3689 0.0365 0.0066 -0.0277 286 GLY A O 2225 N N . ALA A 285 ? 0.3160 0.3049 0.3692 0.0418 0.0056 -0.0287 287 ALA A N 2226 C CA . ALA A 285 ? 0.3224 0.3166 0.3796 0.0423 0.0035 -0.0302 287 ALA A CA 2227 C C . ALA A 285 ? 0.3339 0.3260 0.3879 0.0442 0.0032 -0.0310 287 ALA A C 2228 O O . ALA A 285 ? 0.3375 0.3248 0.3854 0.0465 0.0043 -0.0306 287 ALA A O 2229 C CB . ALA A 285 ? 0.3141 0.3131 0.3722 0.0446 0.0020 -0.0307 287 ALA A CB 2230 N N . ILE A 286 ? 0.3413 0.3361 0.3987 0.0433 0.0018 -0.0321 288 ILE A N 2231 C CA . ILE A 286 ? 0.3581 0.3506 0.4123 0.0449 0.0014 -0.0330 288 ILE A CA 2232 C C . ILE A 286 ? 0.3758 0.3726 0.4304 0.0465 -0.0012 -0.0345 288 ILE A C 2233 O O . ILE A 286 ? 0.3752 0.3773 0.4346 0.0448 -0.0028 -0.0350 288 ILE A O 2234 C CB . ILE A 286 ? 0.3605 0.3520 0.4173 0.0425 0.0018 -0.0330 288 ILE A CB 2235 C CG1 . ILE A 286 ? 0.3689 0.3567 0.4247 0.0413 0.0045 -0.0312 288 ILE A CG1 2236 C CG2 . ILE A 286 ? 0.3719 0.3619 0.4261 0.0440 0.0007 -0.0344 288 ILE A CG2 2237 C CD1 . ILE A 286 ? 0.3550 0.3426 0.4138 0.0394 0.0054 -0.0307 288 ILE A CD1 2238 N N . ASN A 287 ? 0.4032 0.3978 0.4527 0.0496 -0.0017 -0.0352 289 ASN A N 2239 C CA . ASN A 287 ? 0.4288 0.4275 0.4778 0.0513 -0.0044 -0.0366 289 ASN A CA 2240 C C . ASN A 287 ? 0.4403 0.4344 0.4844 0.0528 -0.0044 -0.0374 289 ASN A C 2241 O O . ASN A 287 ? 0.4499 0.4399 0.4883 0.0559 -0.0033 -0.0370 289 ASN A O 2242 C CB . ASN A 287 ? 0.4293 0.4305 0.4760 0.0547 -0.0047 -0.0361 289 ASN A CB 2243 C CG . ASN A 287 ? 0.4595 0.4656 0.5052 0.0570 -0.0075 -0.0373 289 ASN A CG 2244 O OD1 . ASN A 287 ? 0.4777 0.4875 0.5264 0.0549 -0.0098 -0.0385 289 ASN A OD1 2245 N ND2 . ASN A 287 ? 0.5294 0.5352 0.5703 0.0614 -0.0073 -0.0368 289 ASN A ND2 2246 N N . THR A 288 ? 0.4460 0.4401 0.4917 0.0508 -0.0056 -0.0384 290 THR A N 2247 C CA . THR A 288 ? 0.4704 0.4594 0.5113 0.0520 -0.0054 -0.0391 290 THR A CA 2248 C C . THR A 288 ? 0.4833 0.4740 0.5256 0.0499 -0.0079 -0.0408 290 THR A C 2249 O O . THR A 288 ? 0.4884 0.4834 0.5359 0.0469 -0.0091 -0.0410 290 THR A O 2250 C CB . THR A 288 ? 0.4662 0.4498 0.5063 0.0512 -0.0023 -0.0379 290 THR A CB 2251 O OG1 . THR A 288 ? 0.4788 0.4573 0.5137 0.0531 -0.0018 -0.0384 290 THR A OG1 2252 C CG2 . THR A 288 ? 0.4557 0.4407 0.5012 0.0477 -0.0021 -0.0377 290 THR A CG2 2253 N N . THR A 289 ? 0.5057 0.4926 0.5430 0.0514 -0.0087 -0.0419 291 THR A N 2254 C CA . THR A 289 ? 0.5303 0.5160 0.5671 0.0491 -0.0106 -0.0434 291 THR A CA 2255 C C . THR A 289 ? 0.5282 0.5066 0.5618 0.0493 -0.0083 -0.0431 291 THR A C 2256 O O . THR A 289 ? 0.5374 0.5129 0.5692 0.0479 -0.0094 -0.0443 291 THR A O 2257 C CB . THR A 289 ? 0.5379 0.5249 0.5707 0.0503 -0.0139 -0.0451 291 THR A CB 2258 O OG1 . THR A 289 ? 0.5687 0.5517 0.5954 0.0544 -0.0128 -0.0448 291 THR A OG1 2259 C CG2 . THR A 289 ? 0.5474 0.5433 0.5843 0.0495 -0.0166 -0.0453 291 THR A CG2 2260 N N . LEU A 290 ? 0.5245 0.4999 0.5571 0.0511 -0.0051 -0.0415 292 LEU A N 2261 C CA . LEU A 290 ? 0.5241 0.4938 0.5543 0.0516 -0.0025 -0.0407 292 LEU A CA 2262 C C . LEU A 290 ? 0.5157 0.4859 0.5504 0.0487 -0.0018 -0.0403 292 LEU A C 2263 O O . LEU A 290 ? 0.5197 0.4945 0.5601 0.0464 -0.0021 -0.0397 292 LEU A O 2264 C CB . LEU A 290 ? 0.5188 0.4865 0.5475 0.0536 0.0006 -0.0388 292 LEU A CB 2265 C CG . LEU A 290 ? 0.5369 0.5025 0.5599 0.0569 0.0004 -0.0391 292 LEU A CG 2266 C CD1 . LEU A 290 ? 0.5289 0.4921 0.5503 0.0582 0.0037 -0.0371 292 LEU A CD1 2267 C CD2 . LEU A 290 ? 0.5482 0.5093 0.5650 0.0589 -0.0006 -0.0406 292 LEU A CD2 2268 N N . PRO A 291 ? 0.5096 0.4748 0.5413 0.0490 -0.0007 -0.0404 293 PRO A N 2269 C CA . PRO A 291 ? 0.4971 0.4617 0.5318 0.0468 -0.0001 -0.0401 293 PRO A CA 2270 C C . PRO A 291 ? 0.4789 0.4455 0.5183 0.0462 0.0027 -0.0377 293 PRO A C 2271 O O . PRO A 291 ? 0.4768 0.4449 0.5202 0.0440 0.0028 -0.0373 293 PRO A O 2272 C CB . PRO A 291 ? 0.5042 0.4616 0.5324 0.0485 0.0004 -0.0408 293 PRO A CB 2273 C CG . PRO A 291 ? 0.5109 0.4655 0.5340 0.0519 0.0016 -0.0405 293 PRO A CG 2274 C CD . PRO A 291 ? 0.5217 0.4807 0.5460 0.0518 -0.0005 -0.0412 293 PRO A CD 2275 N N . PHE A 292 ? 0.4550 0.4215 0.4937 0.0481 0.0051 -0.0360 294 PHE A N 2276 C CA . PHE A 292 ? 0.4347 0.4034 0.4773 0.0474 0.0078 -0.0335 294 PHE A CA 2277 C C . PHE A 292 ? 0.4132 0.3849 0.4576 0.0469 0.0081 -0.0326 294 PHE A C 2278 O O . PHE A 292 ? 0.3990 0.3699 0.4401 0.0483 0.0071 -0.0335 294 PHE A O 2279 C CB . PHE A 292 ? 0.4431 0.4084 0.4825 0.0497 0.0109 -0.0319 294 PHE A CB 2280 C CG . PHE A 292 ? 0.4777 0.4389 0.5143 0.0509 0.0113 -0.0324 294 PHE A CG 2281 C CD1 . PHE A 292 ? 0.5064 0.4686 0.5462 0.0501 0.0128 -0.0310 294 PHE A CD1 2282 C CD2 . PHE A 292 ? 0.5155 0.4713 0.5455 0.0530 0.0103 -0.0342 294 PHE A CD2 2283 C CE1 . PHE A 292 ? 0.5426 0.4999 0.5787 0.0517 0.0135 -0.0314 294 PHE A CE1 2284 C CE2 . PHE A 292 ? 0.5297 0.4802 0.5556 0.0543 0.0108 -0.0347 294 PHE A CE2 2285 C CZ . PHE A 292 ? 0.5426 0.4936 0.5714 0.0538 0.0125 -0.0333 294 PHE A CZ 2286 N N . HIS A 293 ? 0.3958 0.3706 0.4447 0.0449 0.0096 -0.0308 295 HIS A N 2287 C CA . HIS A 293 ? 0.3794 0.3557 0.4289 0.0443 0.0104 -0.0295 295 HIS A CA 2288 C C . HIS A 293 ? 0.3815 0.3594 0.4339 0.0428 0.0129 -0.0269 295 HIS A C 2289 O O . HIS A 293 ? 0.3796 0.3589 0.4351 0.0420 0.0136 -0.0262 295 HIS A O 2290 C CB . HIS A 293 ? 0.3720 0.3516 0.4244 0.0427 0.0083 -0.0304 295 HIS A CB 2291 C CG . HIS A 293 ? 0.3733 0.3565 0.4317 0.0397 0.0082 -0.0297 295 HIS A CG 2292 N ND1 . HIS A 293 ? 0.3772 0.3620 0.4379 0.0379 0.0096 -0.0278 295 HIS A ND1 2293 C CD2 . HIS A 293 ? 0.3775 0.3626 0.4394 0.0382 0.0070 -0.0304 295 HIS A CD2 2294 C CE1 . HIS A 293 ? 0.3718 0.3597 0.4375 0.0356 0.0092 -0.0274 295 HIS A CE1 2295 N NE2 . HIS A 293 ? 0.3820 0.3699 0.4485 0.0358 0.0078 -0.0290 295 HIS A NE2 2296 N N . ASN A 294 ? 0.3686 0.3462 0.4196 0.0423 0.0143 -0.0255 296 ASN A N 2297 C CA . ASN A 294 ? 0.3812 0.3611 0.4350 0.0403 0.0165 -0.0229 296 ASN A CA 2298 C C . ASN A 294 ? 0.3749 0.3563 0.4302 0.0375 0.0162 -0.0221 296 ASN A C 2299 O O . ASN A 294 ? 0.3794 0.3614 0.4349 0.0356 0.0179 -0.0200 296 ASN A O 2300 C CB . ASN A 294 ? 0.3853 0.3630 0.4354 0.0418 0.0190 -0.0212 296 ASN A CB 2301 C CG . ASN A 294 ? 0.4027 0.3770 0.4475 0.0423 0.0195 -0.0212 296 ASN A CG 2302 O OD1 . ASN A 294 ? 0.4039 0.3768 0.4471 0.0422 0.0179 -0.0225 296 ASN A OD1 2303 N ND2 . ASN A 294 ? 0.4127 0.3852 0.4543 0.0431 0.0218 -0.0196 296 ASN A ND2 2304 N N . VAL A 295 ? 0.3706 0.3526 0.4269 0.0371 0.0141 -0.0237 297 VAL A N 2305 C CA . VAL A 295 ? 0.3746 0.3565 0.4306 0.0352 0.0139 -0.0232 297 VAL A CA 2306 C C . VAL A 295 ? 0.3778 0.3632 0.4388 0.0317 0.0143 -0.0216 297 VAL A C 2307 O O . VAL A 295 ? 0.3867 0.3716 0.4467 0.0296 0.0155 -0.0199 297 VAL A O 2308 C CB . VAL A 295 ? 0.3722 0.3539 0.4271 0.0365 0.0117 -0.0252 297 VAL A CB 2309 C CG1 . VAL A 295 ? 0.3581 0.3398 0.4131 0.0346 0.0117 -0.0246 297 VAL A CG1 2310 C CG2 . VAL A 295 ? 0.3567 0.3347 0.4056 0.0398 0.0115 -0.0263 297 VAL A CG2 2311 N N . HIS A 296 ? 0.3773 0.3661 0.4433 0.0311 0.0133 -0.0221 298 HIS A N 2312 C CA . HIS A 296 ? 0.3867 0.3790 0.4576 0.0281 0.0135 -0.0207 298 HIS A CA 2313 C C . HIS A 296 ? 0.3903 0.3849 0.4652 0.0285 0.0127 -0.0215 298 HIS A C 2314 O O . HIS A 296 ? 0.3945 0.3883 0.4689 0.0300 0.0112 -0.0235 298 HIS A O 2315 C CB . HIS A 296 ? 0.3870 0.3792 0.4579 0.0264 0.0125 -0.0211 298 HIS A CB 2316 C CG . HIS A 296 ? 0.3908 0.3856 0.4652 0.0231 0.0128 -0.0194 298 HIS A CG 2317 N ND1 . HIS A 296 ? 0.3950 0.3935 0.4747 0.0221 0.0122 -0.0193 298 HIS A ND1 2318 C CD2 . HIS A 296 ? 0.3789 0.3731 0.4520 0.0205 0.0136 -0.0177 298 HIS A CD2 2319 C CE1 . HIS A 296 ? 0.3645 0.3649 0.4463 0.0192 0.0126 -0.0176 298 HIS A CE1 2320 N NE2 . HIS A 296 ? 0.3857 0.3836 0.4635 0.0180 0.0134 -0.0166 298 HIS A NE2 2321 N N . PRO A 297 ? 0.4074 0.4050 0.4862 0.0271 0.0137 -0.0197 299 PRO A N 2322 C CA . PRO A 297 ? 0.4054 0.4041 0.4870 0.0276 0.0131 -0.0204 299 PRO A CA 2323 C C . PRO A 297 ? 0.4107 0.4107 0.4952 0.0261 0.0112 -0.0218 299 PRO A C 2324 O O . PRO A 297 ? 0.4089 0.4084 0.4943 0.0266 0.0103 -0.0231 299 PRO A O 2325 C CB . PRO A 297 ? 0.4051 0.4070 0.4898 0.0268 0.0149 -0.0178 299 PRO A CB 2326 C CG . PRO A 297 ? 0.4018 0.4054 0.4867 0.0244 0.0155 -0.0160 299 PRO A CG 2327 C CD . PRO A 297 ? 0.4026 0.4026 0.4827 0.0252 0.0154 -0.0170 299 PRO A CD 2328 N N . LEU A 298 ? 0.4255 0.4266 0.5108 0.0242 0.0107 -0.0216 300 LEU A N 2329 C CA . LEU A 298 ? 0.4324 0.4353 0.5208 0.0228 0.0092 -0.0225 300 LEU A CA 2330 C C . LEU A 298 ? 0.4342 0.4362 0.5207 0.0237 0.0076 -0.0245 300 LEU A C 2331 O O . LEU A 298 ? 0.4500 0.4517 0.5350 0.0234 0.0075 -0.0243 300 LEU A O 2332 C CB . LEU A 298 ? 0.4399 0.4449 0.5308 0.0201 0.0096 -0.0208 300 LEU A CB 2333 C CG . LEU A 298 ? 0.4515 0.4588 0.5450 0.0189 0.0109 -0.0185 300 LEU A CG 2334 C CD1 . LEU A 298 ? 0.4869 0.4958 0.5815 0.0160 0.0110 -0.0169 300 LEU A CD1 2335 C CD2 . LEU A 298 ? 0.4908 0.4995 0.5876 0.0192 0.0108 -0.0186 300 LEU A CD2 2336 N N . THR A 299 ? 0.4246 0.4263 0.5108 0.0249 0.0064 -0.0262 301 THR A N 2337 C CA . THR A 299 ? 0.4146 0.4166 0.4993 0.0260 0.0047 -0.0280 301 THR A CA 2338 C C . THR A 299 ? 0.4103 0.4152 0.4985 0.0244 0.0031 -0.0290 301 THR A C 2339 O O . THR A 299 ? 0.4034 0.4085 0.4941 0.0231 0.0031 -0.0290 301 THR A O 2340 C CB . THR A 299 ? 0.4154 0.4149 0.4961 0.0284 0.0043 -0.0293 301 THR A CB 2341 O OG1 . THR A 299 ? 0.4314 0.4303 0.5127 0.0281 0.0035 -0.0303 301 THR A OG1 2342 C CG2 . THR A 299 ? 0.4125 0.4090 0.4897 0.0298 0.0061 -0.0281 301 THR A CG2 2343 N N . ILE A 300 ? 0.4034 0.4105 0.4916 0.0249 0.0018 -0.0299 302 ILE A N 2344 C CA . ILE A 300 ? 0.4071 0.4178 0.4986 0.0234 0.0001 -0.0310 302 ILE A CA 2345 C C . ILE A 300 ? 0.4224 0.4346 0.5121 0.0249 -0.0016 -0.0325 302 ILE A C 2346 O O . ILE A 300 ? 0.4080 0.4201 0.4948 0.0272 -0.0016 -0.0326 302 ILE A O 2347 C CB . ILE A 300 ? 0.4138 0.4275 0.5083 0.0221 0.0003 -0.0301 302 ILE A CB 2348 C CG1 . ILE A 300 ? 0.4219 0.4339 0.5176 0.0206 0.0020 -0.0284 302 ILE A CG1 2349 C CG2 . ILE A 300 ? 0.3956 0.4133 0.4939 0.0202 -0.0011 -0.0310 302 ILE A CG2 2350 C CD1 . ILE A 300 ? 0.4570 0.4704 0.5540 0.0196 0.0025 -0.0273 302 ILE A CD1 2351 N N . GLY A 301 ? 0.4221 0.4358 0.5133 0.0233 -0.0032 -0.0338 303 GLY A N 2352 C CA . GLY A 301 ? 0.4456 0.4620 0.5358 0.0239 -0.0054 -0.0353 303 GLY A CA 2353 C C . GLY A 301 ? 0.4706 0.4830 0.5572 0.0241 -0.0063 -0.0365 303 GLY A C 2354 O O . GLY A 301 ? 0.4714 0.4797 0.5574 0.0231 -0.0053 -0.0364 303 GLY A O 2355 N N . GLU A 302 ? 0.4852 0.4986 0.5691 0.0257 -0.0079 -0.0377 304 GLU A N 2356 C CA . GLU A 302 ? 0.5085 0.5177 0.5881 0.0259 -0.0089 -0.0390 304 GLU A CA 2357 C C . GLU A 302 ? 0.5056 0.5104 0.5808 0.0293 -0.0072 -0.0386 304 GLU A C 2358 O O . GLU A 302 ? 0.5094 0.5153 0.5821 0.0318 -0.0077 -0.0387 304 GLU A O 2359 C CB . GLU A 302 ? 0.5166 0.5299 0.5958 0.0251 -0.0119 -0.0405 304 GLU A CB 2360 C CG . GLU A 302 ? 0.5751 0.5924 0.6587 0.0210 -0.0134 -0.0409 304 GLU A CG 2361 C CD . GLU A 302 ? 0.6457 0.6701 0.7307 0.0199 -0.0164 -0.0417 304 GLU A CD 2362 O OE1 . GLU A 302 ? 0.6592 0.6898 0.7465 0.0218 -0.0166 -0.0410 304 GLU A OE1 2363 O OE2 . GLU A 302 ? 0.6905 0.7140 0.7739 0.0171 -0.0185 -0.0431 304 GLU A OE2 2364 N N . CYS A 303 ? 0.4998 0.4997 0.5738 0.0295 -0.0051 -0.0378 305 CYS A N 2365 C CA . CYS A 303 ? 0.5110 0.5075 0.5820 0.0321 -0.0029 -0.0367 305 CYS A CA 2366 C C . CYS A 303 ? 0.5032 0.4940 0.5693 0.0336 -0.0023 -0.0372 305 CYS A C 2367 O O . CYS A 303 ? 0.5014 0.4900 0.5668 0.0323 -0.0031 -0.0381 305 CYS A O 2368 C CB . CYS A 303 ? 0.5051 0.5019 0.5791 0.0313 -0.0006 -0.0347 305 CYS A CB 2369 S SG . CYS A 303 ? 0.5708 0.5726 0.6485 0.0305 -0.0007 -0.0338 305 CYS A SG 2370 N N . PRO A 304 ? 0.4898 0.4779 0.5521 0.0363 -0.0010 -0.0366 306 PRO A N 2371 C CA . PRO A 304 ? 0.4865 0.4692 0.5442 0.0381 0.0001 -0.0367 306 PRO A CA 2372 C C . PRO A 304 ? 0.4748 0.4564 0.5347 0.0374 0.0025 -0.0351 306 PRO A C 2373 O O . PRO A 304 ? 0.4623 0.4473 0.5270 0.0356 0.0030 -0.0339 306 PRO A O 2374 C CB . PRO A 304 ? 0.4743 0.4555 0.5284 0.0410 0.0014 -0.0360 306 PRO A CB 2375 C CG . PRO A 304 ? 0.4863 0.4714 0.5419 0.0409 0.0003 -0.0361 306 PRO A CG 2376 C CD . PRO A 304 ? 0.4888 0.4782 0.5503 0.0380 -0.0002 -0.0358 306 PRO A CD 2377 N N . LYS A 305 ? 0.4730 0.4501 0.5293 0.0390 0.0040 -0.0347 307 LYS A N 2378 C CA A LYS A 305 ? 0.4774 0.4541 0.5358 0.0389 0.0064 -0.0328 307 LYS A CA 2379 C C . LYS A 305 ? 0.4702 0.4482 0.5290 0.0402 0.0089 -0.0306 307 LYS A C 2380 O O . LYS A 305 ? 0.4741 0.4499 0.5289 0.0424 0.0095 -0.0307 307 LYS A O 2381 C CB A LYS A 305 ? 0.4909 0.4622 0.5451 0.0404 0.0071 -0.0333 307 LYS A CB 2382 C CG A LYS A 305 ? 0.5390 0.5080 0.5918 0.0384 0.0044 -0.0356 307 LYS A CG 2383 C CD A LYS A 305 ? 0.5924 0.5644 0.6506 0.0354 0.0041 -0.0351 307 LYS A CD 2384 C CE A LYS A 305 ? 0.6231 0.5962 0.6820 0.0324 0.0009 -0.0373 307 LYS A CE 2385 N NZ A LYS A 305 ? 0.6482 0.6276 0.7110 0.0314 -0.0004 -0.0374 307 LYS A NZ 2386 N N . TYR A 306 ? 0.4485 0.4300 0.5120 0.0387 0.0103 -0.0286 308 TYR A N 2387 C CA . TYR A 306 ? 0.4348 0.4181 0.4991 0.0390 0.0125 -0.0263 308 TYR A CA 2388 C C . TYR A 306 ? 0.4419 0.4240 0.5046 0.0411 0.0153 -0.0243 308 TYR A C 2389 O O . TYR A 306 ? 0.4346 0.4162 0.4981 0.0417 0.0160 -0.0238 308 TYR A O 2390 C CB . TYR A 306 ? 0.4214 0.4092 0.4911 0.0360 0.0125 -0.0250 308 TYR A CB 2391 C CG . TYR A 306 ? 0.4128 0.4028 0.4835 0.0354 0.0146 -0.0224 308 TYR A CG 2392 C CD1 . TYR A 306 ? 0.4004 0.3897 0.4688 0.0350 0.0147 -0.0223 308 TYR A CD1 2393 C CD2 . TYR A 306 ? 0.3994 0.3921 0.4730 0.0350 0.0165 -0.0200 308 TYR A CD2 2394 C CE1 . TYR A 306 ? 0.4106 0.4013 0.4793 0.0338 0.0164 -0.0200 308 TYR A CE1 2395 C CE2 . TYR A 306 ? 0.4151 0.4105 0.4898 0.0338 0.0182 -0.0175 308 TYR A CE2 2396 C CZ . TYR A 306 ? 0.4174 0.4115 0.4894 0.0330 0.0182 -0.0176 308 TYR A CZ 2397 O OH . TYR A 306 ? 0.4183 0.4146 0.4908 0.0312 0.0198 -0.0151 308 TYR A OH 2398 N N . VAL A 307 ? 0.4379 0.4195 0.4982 0.0423 0.0169 -0.0231 309 VAL A N 2399 C CA . VAL A 307 ? 0.4429 0.4246 0.5022 0.0443 0.0199 -0.0207 309 VAL A CA 2400 C C . VAL A 307 ? 0.4470 0.4317 0.5073 0.0429 0.0214 -0.0186 309 VAL A C 2401 O O . VAL A 307 ? 0.4515 0.4353 0.5106 0.0416 0.0202 -0.0195 309 VAL A O 2402 C CB . VAL A 307 ? 0.4520 0.4283 0.5049 0.0479 0.0206 -0.0217 309 VAL A CB 2403 C CG1 . VAL A 307 ? 0.4513 0.4237 0.5020 0.0491 0.0193 -0.0237 309 VAL A CG1 2404 C CG2 . VAL A 307 ? 0.4383 0.4118 0.4870 0.0485 0.0195 -0.0233 309 VAL A CG2 2405 N N . LYS A 308 ? 0.4557 0.4435 0.5178 0.0432 0.0239 -0.0157 310 LYS A N 2406 C CA . LYS A 308 ? 0.4776 0.4684 0.5404 0.0413 0.0255 -0.0133 310 LYS A CA 2407 C C . LYS A 308 ? 0.4866 0.4737 0.5438 0.0432 0.0268 -0.0132 310 LYS A C 2408 O O . LYS A 308 ? 0.4941 0.4825 0.5508 0.0414 0.0280 -0.0115 310 LYS A O 2409 C CB . LYS A 308 ? 0.4864 0.4831 0.5534 0.0409 0.0278 -0.0099 310 LYS A CB 2410 C CG . LYS A 308 ? 0.5138 0.5155 0.5868 0.0381 0.0269 -0.0089 310 LYS A CG 2411 C CD . LYS A 308 ? 0.5781 0.5866 0.6547 0.0377 0.0294 -0.0051 310 LYS A CD 2412 C CE . LYS A 308 ? 0.6225 0.6368 0.7048 0.0342 0.0286 -0.0035 310 LYS A CE 2413 N NZ . LYS A 308 ? 0.6582 0.6752 0.7436 0.0363 0.0291 -0.0027 310 LYS A NZ 2414 N N . SER A 309 ? 0.4835 0.4657 0.5361 0.0467 0.0266 -0.0151 311 SER A N 2415 C CA . SER A 309 ? 0.4889 0.4674 0.5358 0.0492 0.0282 -0.0149 311 SER A CA 2416 C C . SER A 309 ? 0.4870 0.4635 0.5311 0.0476 0.0276 -0.0153 311 SER A C 2417 O O . SER A 309 ? 0.4828 0.4585 0.5272 0.0460 0.0253 -0.0170 311 SER A O 2418 C CB . SER A 309 ? 0.4908 0.4636 0.5327 0.0527 0.0271 -0.0174 311 SER A CB 2419 O OG . SER A 309 ? 0.4811 0.4543 0.5246 0.0541 0.0274 -0.0174 311 SER A OG 2420 N N . GLU A 310 ? 0.5033 0.4787 0.5440 0.0482 0.0299 -0.0136 312 GLU A N 2421 C CA . GLU A 310 ? 0.5226 0.4941 0.5586 0.0475 0.0296 -0.0142 312 GLU A CA 2422 C C . GLU A 310 ? 0.5234 0.4889 0.5531 0.0513 0.0284 -0.0168 312 GLU A C 2423 O O . GLU A 310 ? 0.5245 0.4864 0.5504 0.0514 0.0271 -0.0183 312 GLU A O 2424 C CB . GLU A 310 ? 0.5406 0.5132 0.5752 0.0462 0.0325 -0.0112 312 GLU A CB 2425 C CG . GLU A 310 ? 0.5955 0.5746 0.6359 0.0419 0.0335 -0.0083 312 GLU A CG 2426 C CD . GLU A 310 ? 0.6657 0.6457 0.7041 0.0396 0.0360 -0.0054 312 GLU A CD 2427 O OE1 . GLU A 310 ? 0.6975 0.6719 0.7300 0.0391 0.0360 -0.0061 312 GLU A OE1 2428 O OE2 . GLU A 310 ? 0.6870 0.6732 0.7293 0.0384 0.0381 -0.0024 312 GLU A OE2 2429 N N . LYS A 311 ? 0.5191 0.4830 0.5472 0.0545 0.0290 -0.0174 313 LYS A N 2430 C CA . LYS A 311 ? 0.5264 0.4846 0.5483 0.0579 0.0278 -0.0198 313 LYS A CA 2431 C C . LYS A 311 ? 0.5111 0.4678 0.5325 0.0603 0.0271 -0.0212 313 LYS A C 2432 O O . LYS A 311 ? 0.5172 0.4760 0.5410 0.0609 0.0289 -0.0195 313 LYS A O 2433 C CB . LYS A 311 ? 0.5350 0.4895 0.5509 0.0600 0.0302 -0.0187 313 LYS A CB 2434 C CG . LYS A 311 ? 0.5692 0.5263 0.5863 0.0605 0.0338 -0.0155 313 LYS A CG 2435 C CD . LYS A 311 ? 0.6085 0.5616 0.6193 0.0626 0.0362 -0.0144 313 LYS A CD 2436 C CE . LYS A 311 ? 0.6188 0.5761 0.6318 0.0626 0.0400 -0.0108 313 LYS A CE 2437 N NZ . LYS A 311 ? 0.6593 0.6127 0.6659 0.0651 0.0425 -0.0097 313 LYS A NZ 2438 N N . LEU A 312 ? 0.5030 0.4560 0.5210 0.0616 0.0243 -0.0241 314 LEU A N 2439 C CA . LEU A 312 ? 0.4939 0.4436 0.5092 0.0638 0.0234 -0.0258 314 LEU A CA 2440 C C . LEU A 312 ? 0.4877 0.4322 0.4964 0.0660 0.0214 -0.0283 314 LEU A C 2441 O O . LEU A 312 ? 0.4731 0.4184 0.4823 0.0648 0.0182 -0.0303 314 LEU A O 2442 C CB . LEU A 312 ? 0.4898 0.4418 0.5098 0.0616 0.0211 -0.0270 314 LEU A CB 2443 C CG . LEU A 312 ? 0.5066 0.4631 0.5326 0.0600 0.0228 -0.0249 314 LEU A CG 2444 C CD1 . LEU A 312 ? 0.4974 0.4559 0.5276 0.0574 0.0201 -0.0264 314 LEU A CD1 2445 C CD2 . LEU A 312 ? 0.4936 0.4477 0.5170 0.0630 0.0255 -0.0235 314 LEU A CD2 2446 N N . VAL A 313 ? 0.4833 0.4230 0.4857 0.0693 0.0232 -0.0279 315 VAL A N 2447 C CA . VAL A 313 ? 0.4737 0.4083 0.4690 0.0717 0.0215 -0.0301 315 VAL A CA 2448 C C . VAL A 313 ? 0.4708 0.3998 0.4604 0.0746 0.0220 -0.0309 315 VAL A C 2449 O O . VAL A 313 ? 0.4618 0.3893 0.4498 0.0767 0.0254 -0.0288 315 VAL A O 2450 C CB . VAL A 313 ? 0.4775 0.4106 0.4691 0.0731 0.0234 -0.0288 315 VAL A CB 2451 C CG1 . VAL A 313 ? 0.4841 0.4124 0.4686 0.0756 0.0212 -0.0311 315 VAL A CG1 2452 C CG2 . VAL A 313 ? 0.4840 0.4216 0.4805 0.0701 0.0236 -0.0275 315 VAL A CG2 2453 N N . LEU A 314 ? 0.4656 0.3916 0.4521 0.0746 0.0186 -0.0337 316 LEU A N 2454 C CA . LEU A 314 ? 0.4716 0.3909 0.4512 0.0770 0.0184 -0.0350 316 LEU A CA 2455 C C . LEU A 314 ? 0.4757 0.3899 0.4473 0.0802 0.0182 -0.0360 316 LEU A C 2456 O O . LEU A 314 ? 0.4755 0.3910 0.4464 0.0798 0.0159 -0.0372 316 LEU A O 2457 C CB . LEU A 314 ? 0.4794 0.3980 0.4592 0.0747 0.0145 -0.0378 316 LEU A CB 2458 C CG . LEU A 314 ? 0.4863 0.4062 0.4704 0.0727 0.0147 -0.0374 316 LEU A CG 2459 C CD1 . LEU A 314 ? 0.5215 0.4410 0.5055 0.0698 0.0103 -0.0403 316 LEU A CD1 2460 C CD2 . LEU A 314 ? 0.4829 0.3970 0.4622 0.0756 0.0177 -0.0363 316 LEU A CD2 2461 N N . ALA A 315 ? 0.4794 0.3877 0.4446 0.0836 0.0208 -0.0353 317 ALA A N 2462 C CA . ALA A 315 ? 0.4786 0.3806 0.4348 0.0868 0.0203 -0.0365 317 ALA A CA 2463 C C . ALA A 315 ? 0.4817 0.3799 0.4335 0.0860 0.0159 -0.0399 317 ALA A C 2464 O O . ALA A 315 ? 0.4860 0.3822 0.4377 0.0847 0.0150 -0.0408 317 ALA A O 2465 C CB . ALA A 315 ? 0.4851 0.3818 0.4356 0.0907 0.0244 -0.0347 317 ALA A CB 2466 N N . THR A 316 ? 0.4804 0.3777 0.4283 0.0865 0.0130 -0.0416 318 THR A N 2467 C CA . THR A 316 ? 0.4779 0.3712 0.4203 0.0859 0.0088 -0.0447 318 THR A CA 2468 C C . THR A 316 ? 0.4881 0.3739 0.4201 0.0898 0.0090 -0.0455 318 THR A C 2469 O O . THR A 316 ? 0.4957 0.3746 0.4202 0.0905 0.0077 -0.0472 318 THR A O 2470 C CB . THR A 316 ? 0.4735 0.3735 0.4207 0.0827 0.0043 -0.0464 318 THR A CB 2471 O OG1 . THR A 316 ? 0.4565 0.3598 0.4045 0.0842 0.0047 -0.0455 318 THR A OG1 2472 C CG2 . THR A 316 ? 0.4655 0.3720 0.4221 0.0787 0.0038 -0.0459 318 THR A CG2 2473 N N . GLY A 317 ? 0.4884 0.3751 0.4193 0.0922 0.0108 -0.0442 319 GLY A N 2474 C CA . GLY A 317 ? 0.4960 0.3755 0.4169 0.0963 0.0116 -0.0446 319 GLY A CA 2475 C C . GLY A 317 ? 0.5064 0.3806 0.4234 0.0995 0.0166 -0.0424 319 GLY A C 2476 O O . GLY A 317 ? 0.4908 0.3660 0.4117 0.0987 0.0191 -0.0410 319 GLY A O 2477 N N . LEU A 318 ? 0.5172 0.3860 0.4265 0.1033 0.0183 -0.0421 320 LEU A N 2478 C CA . LEU A 318 ? 0.5218 0.3854 0.4264 0.1068 0.0232 -0.0400 320 LEU A CA 2479 C C . LEU A 318 ? 0.5175 0.3849 0.4254 0.1078 0.0272 -0.0369 320 LEU A C 2480 O O . LEU A 318 ? 0.5042 0.3764 0.4163 0.1060 0.0260 -0.0368 320 LEU A O 2481 C CB . LEU A 318 ? 0.5376 0.3912 0.4298 0.1106 0.0226 -0.0416 320 LEU A CB 2482 C CG . LEU A 318 ? 0.5594 0.4111 0.4459 0.1122 0.0203 -0.0430 320 LEU A CG 2483 C CD1 . LEU A 318 ? 0.6072 0.4492 0.4821 0.1169 0.0223 -0.0430 320 LEU A CD1 2484 C CD2 . LEU A 318 ? 0.5545 0.4078 0.4409 0.1095 0.0142 -0.0462 320 LEU A CD2 2485 N N . ARG A 319 ? 0.5238 0.3888 0.4295 0.1106 0.0320 -0.0344 321 ARG A N 2486 C CA . ARG A 319 ? 0.5444 0.4118 0.4515 0.1116 0.0362 -0.0313 321 ARG A CA 2487 C C . ARG A 319 ? 0.5641 0.4281 0.4650 0.1132 0.0349 -0.0323 321 ARG A C 2488 O O . ARG A 319 ? 0.5687 0.4255 0.4605 0.1162 0.0334 -0.0343 321 ARG A O 2489 C CB . ARG A 319 ? 0.5533 0.4170 0.4562 0.1153 0.0410 -0.0290 321 ARG A CB 2490 C CG . ARG A 319 ? 0.5754 0.4459 0.4856 0.1143 0.0454 -0.0251 321 ARG A CG 2491 C CD . ARG A 319 ? 0.6235 0.4906 0.5292 0.1185 0.0499 -0.0229 321 ARG A CD 2492 N NE . ARG A 319 ? 0.6625 0.5333 0.5737 0.1179 0.0511 -0.0217 321 ARG A NE 2493 C CZ . ARG A 319 ? 0.6336 0.5127 0.5529 0.1165 0.0544 -0.0182 321 ARG A CZ 2494 N NH1 . ARG A 319 ? 0.6637 0.5475 0.5861 0.1152 0.0567 -0.0157 321 ARG A NH1 2495 N NH2 . ARG A 319 ? 0.6074 0.4899 0.5314 0.1164 0.0554 -0.0171 321 ARG A NH2 2496 N N . ASN A 320 ? 0.5696 0.4383 0.4751 0.1112 0.0353 -0.0311 322 ASN A N 2497 C CA . ASN A 320 ? 0.6051 0.4708 0.5050 0.1128 0.0344 -0.0318 322 ASN A CA 2498 C C . ASN A 320 ? 0.6346 0.4966 0.5293 0.1156 0.0393 -0.0292 322 ASN A C 2499 O O . ASN A 320 ? 0.6290 0.4950 0.5284 0.1138 0.0426 -0.0263 322 ASN A O 2500 C CB . ASN A 320 ? 0.5918 0.4632 0.4977 0.1096 0.0326 -0.0318 322 ASN A CB 2501 C CG . ASN A 320 ? 0.6047 0.4729 0.5044 0.1116 0.0304 -0.0332 322 ASN A CG 2502 O OD1 . ASN A 320 ? 0.5628 0.4256 0.4547 0.1146 0.0284 -0.0352 322 ASN A OD1 2503 N ND2 . ASN A 320 ? 0.6073 0.4783 0.5097 0.1099 0.0306 -0.0323 322 ASN A ND2 2504 N N . VAL A 321 ? 0.6708 0.5251 0.5556 0.1198 0.0396 -0.0301 323 VAL A N 2505 C CA . VAL A 321 ? 0.7122 0.5623 0.5913 0.1231 0.0445 -0.0276 323 VAL A CA 2506 C C . VAL A 321 ? 0.7556 0.6009 0.6273 0.1252 0.0444 -0.0279 323 VAL A C 2507 O O . VAL A 321 ? 0.7666 0.6071 0.6315 0.1273 0.0408 -0.0307 323 VAL A O 2508 C CB . VAL A 321 ? 0.7176 0.5613 0.5897 0.1269 0.0458 -0.0281 323 VAL A CB 2509 C CG1 . VAL A 321 ? 0.7183 0.5586 0.5854 0.1303 0.0514 -0.0250 323 VAL A CG1 2510 C CG2 . VAL A 321 ? 0.7004 0.5474 0.5784 0.1253 0.0457 -0.0280 323 VAL A CG2 2511 N N . PRO A 322 ? 0.7877 0.6344 0.6604 0.1244 0.0481 -0.0251 324 PRO A N 2512 C CA . PRO A 322 ? 0.8161 0.6574 0.6810 0.1266 0.0490 -0.0248 324 PRO A CA 2513 C C . PRO A 322 ? 0.8527 0.6853 0.7061 0.1318 0.0487 -0.0262 324 PRO A C 2514 O O . PRO A 322 ? 0.8601 0.6896 0.7103 0.1342 0.0507 -0.0259 324 PRO A O 2515 C CB . PRO A 322 ? 0.8129 0.6563 0.6800 0.1252 0.0546 -0.0207 324 PRO A CB 2516 C CG . PRO A 322 ? 0.7969 0.6492 0.6756 0.1206 0.0549 -0.0194 324 PRO A CG 2517 C CD . PRO A 322 ? 0.7792 0.6326 0.6603 0.1212 0.0519 -0.0217 324 PRO A CD 2518 N N . GLN A 323 ? 0.8839 0.7122 0.7306 0.1337 0.0464 -0.0278 325 GLN A N 2519 C CA . GLN A 323 ? 0.9225 0.7422 0.7576 0.1386 0.0457 -0.0293 325 GLN A CA 2520 C C . GLN A 323 ? 0.9387 0.7529 0.7673 0.1418 0.0512 -0.0268 325 GLN A C 2521 O O . GLN A 323 ? 0.9422 0.7594 0.7748 0.1401 0.0558 -0.0235 325 GLN A O 2522 C CB . GLN A 323 ? 0.9311 0.7482 0.7608 0.1401 0.0428 -0.0308 325 GLN A CB 2523 C CG . GLN A 323 ? 0.9586 0.7729 0.7847 0.1406 0.0467 -0.0282 325 GLN A CG 2524 C CD . GLN A 323 ? 0.9846 0.8048 0.8196 0.1361 0.0500 -0.0254 325 GLN A CD 2525 O OE1 . GLN A 323 ? 0.9834 0.8106 0.8279 0.1323 0.0487 -0.0255 325 GLN A OE1 2526 N NE2 . GLN A 323 ? 1.0032 0.8202 0.8344 0.1361 0.0542 -0.0227 325 GLN A NE2 2527 N N . ILE A 324 ? 0.9557 0.7623 0.7744 0.1462 0.0508 -0.0282 326 ILE A N 2528 C CA . ILE A 324 ? 0.9698 0.7701 0.7806 0.1500 0.0559 -0.0259 326 ILE A CA 2529 C C . ILE A 324 ? 0.9780 0.7713 0.7786 0.1533 0.0554 -0.0266 326 ILE A C 2530 O O . ILE A 324 ? 0.9808 0.7755 0.7825 0.1519 0.0552 -0.0260 326 ILE A O 2531 C CB . ILE A 324 ? 0.9771 0.7727 0.7829 0.1532 0.0568 -0.0265 326 ILE A CB 2532 C CG1 . ILE A 324 ? 0.9709 0.7729 0.7860 0.1508 0.0590 -0.0248 326 ILE A CG1 2533 C CG2 . ILE A 324 ? 0.9949 0.7823 0.7899 0.1582 0.0612 -0.0249 326 ILE A CG2 2534 C CD1 . ILE A 324 ? 0.9591 0.7685 0.7826 0.1480 0.0640 -0.0206 326 ILE A CD1 2535 N N . GLY B 1 ? 0.4637 0.5314 0.3003 -0.0244 -0.0157 0.0377 1 GLY B N 2536 C CA . GLY B 1 ? 0.4330 0.4926 0.2776 -0.0081 -0.0118 0.0321 1 GLY B CA 2537 C C . GLY B 1 ? 0.4195 0.4995 0.2728 0.0068 -0.0076 0.0281 1 GLY B C 2538 O O . GLY B 1 ? 0.4198 0.5239 0.2752 0.0069 -0.0074 0.0292 1 GLY B O 2539 N N . LEU B 2 ? 0.4136 0.4808 0.2687 0.0197 -0.0050 0.0234 2 LEU B N 2540 C CA . LEU B 2 ? 0.4183 0.4977 0.2734 0.0354 -0.0024 0.0193 2 LEU B CA 2541 C C . LEU B 2 ? 0.4122 0.4906 0.2673 0.0410 -0.0012 0.0174 2 LEU B C 2542 O O . LEU B 2 ? 0.4210 0.5185 0.2733 0.0518 -0.0005 0.0155 2 LEU B O 2543 C CB . LEU B 2 ? 0.4229 0.4793 0.2743 0.0449 -0.0009 0.0152 2 LEU B CB 2544 C CG . LEU B 2 ? 0.4347 0.5009 0.2796 0.0598 -0.0001 0.0123 2 LEU B CG 2545 C CD1 . LEU B 2 ? 0.3953 0.4983 0.2427 0.0583 -0.0011 0.0153 2 LEU B CD1 2546 C CD2 . LEU B 2 ? 0.4236 0.4604 0.2628 0.0637 0.0004 0.0095 2 LEU B CD2 2547 N N . PHE B 3 ? 0.4080 0.4655 0.2646 0.0350 -0.0012 0.0176 3 PHE B N 2548 C CA . PHE B 3 ? 0.4129 0.4680 0.2692 0.0394 0.0000 0.0156 3 PHE B CA 2549 C C . PHE B 3 ? 0.4104 0.4812 0.2706 0.0306 -0.0013 0.0194 3 PHE B C 2550 O O . PHE B 3 ? 0.4213 0.4923 0.2820 0.0333 -0.0004 0.0181 3 PHE B O 2551 C CB . PHE B 3 ? 0.4066 0.4337 0.2603 0.0407 0.0013 0.0125 3 PHE B CB 2552 C CG . PHE B 3 ? 0.4202 0.4327 0.2653 0.0491 0.0023 0.0087 3 PHE B CG 2553 C CD1 . PHE B 3 ? 0.4265 0.4324 0.2599 0.0593 0.0027 0.0050 3 PHE B CD1 2554 C CD2 . PHE B 3 ? 0.4056 0.4089 0.2507 0.0474 0.0020 0.0088 3 PHE B CD2 2555 C CE1 . PHE B 3 ? 0.4392 0.4249 0.2579 0.0666 0.0024 0.0018 3 PHE B CE1 2556 C CE2 . PHE B 3 ? 0.4006 0.3892 0.2353 0.0544 0.0024 0.0057 3 PHE B CE2 2557 C CZ . PHE B 3 ? 0.4113 0.3892 0.2313 0.0637 0.0023 0.0023 3 PHE B CZ 2558 N N . GLY B 4 ? 0.4133 0.4958 0.2734 0.0185 -0.0041 0.0244 4 GLY B N 2559 C CA . GLY B 4 ? 0.4157 0.5158 0.2755 0.0075 -0.0063 0.0290 4 GLY B CA 2560 C C . GLY B 4 ? 0.4199 0.4991 0.2770 0.0004 -0.0079 0.0308 4 GLY B C 2561 O O . GLY B 4 ? 0.4325 0.5237 0.2870 -0.0093 -0.0102 0.0349 4 GLY B O 2562 N N . ALA B 5 ? 0.4122 0.4634 0.2685 0.0054 -0.0070 0.0280 5 ALA B N 2563 C CA . ALA B 5 ? 0.4199 0.4540 0.2722 0.0025 -0.0085 0.0291 5 ALA B CA 2564 C C . ALA B 5 ? 0.4413 0.4522 0.2800 -0.0056 -0.0135 0.0326 5 ALA B C 2565 O O . ALA B 5 ? 0.4544 0.4598 0.2823 -0.0155 -0.0176 0.0370 5 ALA B O 2566 C CB . ALA B 5 ? 0.4108 0.4343 0.2678 0.0130 -0.0050 0.0241 5 ALA B CB 2567 N N . ILE B 6 ? 0.4482 0.4431 0.2839 -0.0017 -0.0137 0.0306 6 ILE B N 2568 C CA . ILE B 6 ? 0.4784 0.4457 0.2964 -0.0062 -0.0191 0.0329 6 ILE B CA 2569 C C . ILE B 6 ? 0.4940 0.4632 0.3001 -0.0226 -0.0237 0.0385 6 ILE B C 2570 O O . ILE B 6 ? 0.4788 0.4709 0.2933 -0.0262 -0.0218 0.0389 6 ILE B O 2571 C CB . ILE B 6 ? 0.4746 0.4287 0.2933 0.0032 -0.0179 0.0289 6 ILE B CB 2572 C CG1 . ILE B 6 ? 0.4660 0.4205 0.2920 0.0157 -0.0144 0.0244 6 ILE B CG1 2573 C CG2 . ILE B 6 ? 0.5133 0.4378 0.3102 0.0000 -0.0241 0.0309 6 ILE B CG2 2574 C CD1 . ILE B 6 ? 0.4759 0.4266 0.3049 0.0236 -0.0126 0.0205 6 ILE B CD1 2575 N N . ALA B 7 ? 0.5250 0.4699 0.3085 -0.0328 -0.0303 0.0429 7 ALA B N 2576 C CA . ALA B 7 ? 0.5462 0.4937 0.3134 -0.0543 -0.0358 0.0496 7 ALA B CA 2577 C C . ALA B 7 ? 0.5276 0.5221 0.3123 -0.0612 -0.0322 0.0516 7 ALA B C 2578 O O . ALA B 7 ? 0.5234 0.5407 0.3062 -0.0747 -0.0336 0.0552 7 ALA B O 2579 C CB . ALA B 7 ? 0.5648 0.4976 0.3191 -0.0615 -0.0391 0.0508 7 ALA B CB 2580 N N . GLY B 8 ? 0.5101 0.5216 0.3107 -0.0509 -0.0277 0.0489 8 GLY B N 2581 C CA . GLY B 8 ? 0.4865 0.5422 0.3036 -0.0505 -0.0239 0.0488 8 GLY B CA 2582 C C . GLY B 8 ? 0.4913 0.5541 0.3076 -0.0545 -0.0247 0.0511 8 GLY B C 2583 O O . GLY B 8 ? 0.5091 0.5590 0.3068 -0.0711 -0.0306 0.0570 8 GLY B O 2584 N N . PHE B 9 ? 0.4706 0.5497 0.3034 -0.0401 -0.0194 0.0465 9 PHE B N 2585 C CA . PHE B 9 ? 0.4791 0.5647 0.3123 -0.0426 -0.0198 0.0482 9 PHE B CA 2586 C C . PHE B 9 ? 0.4887 0.5349 0.3104 -0.0410 -0.0224 0.0483 9 PHE B C 2587 O O . PHE B 9 ? 0.4978 0.5383 0.3103 -0.0485 -0.0255 0.0519 9 PHE B O 2588 C CB . PHE B 9 ? 0.4526 0.5655 0.3030 -0.0283 -0.0142 0.0434 9 PHE B CB 2589 C CG . PHE B 9 ? 0.4672 0.5611 0.3250 -0.0114 -0.0099 0.0367 9 PHE B CG 2590 C CD1 . PHE B 9 ? 0.4775 0.5545 0.3352 -0.0079 -0.0092 0.0354 9 PHE B CD1 2591 C CD2 . PHE B 9 ? 0.4407 0.5365 0.3038 0.0000 -0.0067 0.0319 9 PHE B CD2 2592 C CE1 . PHE B 9 ? 0.4765 0.5415 0.3395 0.0039 -0.0055 0.0298 9 PHE B CE1 2593 C CE2 . PHE B 9 ? 0.4741 0.5520 0.3401 0.0112 -0.0034 0.0265 9 PHE B CE2 2594 C CZ . PHE B 9 ? 0.4475 0.5120 0.3136 0.0119 -0.0028 0.0256 9 PHE B CZ 2595 N N . ILE B 10 ? 0.4832 0.5041 0.3036 -0.0304 -0.0214 0.0443 10 ILE B N 2596 C CA . ILE B 10 ? 0.5041 0.4897 0.3086 -0.0271 -0.0250 0.0445 10 ILE B CA 2597 C C . ILE B 10 ? 0.5351 0.4940 0.3160 -0.0380 -0.0318 0.0485 10 ILE B C 2598 O O . ILE B 10 ? 0.5256 0.4743 0.3059 -0.0332 -0.0314 0.0461 10 ILE B O 2599 C CB . ILE B 10 ? 0.4907 0.4688 0.3047 -0.0089 -0.0207 0.0381 10 ILE B CB 2600 C CG1 . ILE B 10 ? 0.4759 0.4795 0.3098 -0.0020 -0.0146 0.0345 10 ILE B CG1 2601 C CG2 . ILE B 10 ? 0.5060 0.4559 0.3023 -0.0026 -0.0248 0.0383 10 ILE B CG2 2602 C CD1 . ILE B 10 ? 0.4509 0.4522 0.2926 0.0106 -0.0105 0.0289 10 ILE B CD1 2603 N N . GLU B 11 ? 0.5664 0.5122 0.3252 -0.0543 -0.0384 0.0549 11 GLU B N 2604 C CA . GLU B 11 ? 0.6095 0.5322 0.3407 -0.0723 -0.0460 0.0604 11 GLU B CA 2605 C C . GLU B 11 ? 0.6339 0.5103 0.3419 -0.0641 -0.0506 0.0584 11 GLU B C 2606 O O . GLU B 11 ? 0.6581 0.5240 0.3547 -0.0728 -0.0536 0.0599 11 GLU B O 2607 C CB . GLU B 11 ? 0.6455 0.5570 0.3514 -0.0930 -0.0533 0.0680 11 GLU B CB 2608 C CG . GLU B 11 ? 0.6767 0.6367 0.3974 -0.1089 -0.0512 0.0721 11 GLU B CG 2609 C CD . GLU B 11 ? 0.7770 0.7230 0.4652 -0.1366 -0.0602 0.0812 11 GLU B CD 2610 O OE1 . GLU B 11 ? 0.8406 0.7936 0.5138 -0.1593 -0.0648 0.0867 11 GLU B OE1 2611 O OE2 . GLU B 11 ? 0.8308 0.7568 0.5054 -0.1371 -0.0635 0.0832 11 GLU B OE2 2612 N N . GLY B 12 ? 0.6371 0.4880 0.3365 -0.0466 -0.0515 0.0549 12 GLY B N 2613 C CA . GLY B 12 ? 0.6697 0.4779 0.3435 -0.0350 -0.0566 0.0525 12 GLY B CA 2614 C C . GLY B 12 ? 0.6532 0.4659 0.3412 -0.0083 -0.0517 0.0453 12 GLY B C 2615 O O . GLY B 12 ? 0.6262 0.4679 0.3387 -0.0007 -0.0454 0.0428 12 GLY B O 2616 N N . GLY B 13 ? 0.6708 0.4566 0.3415 0.0049 -0.0549 0.0420 13 GLY B N 2617 C CA . GLY B 13 ? 0.6674 0.4595 0.3461 0.0301 -0.0515 0.0354 13 GLY B CA 2618 C C . GLY B 13 ? 0.7068 0.4703 0.3561 0.0444 -0.0576 0.0351 13 GLY B C 2619 O O . GLY B 13 ? 0.7466 0.4740 0.3629 0.0344 -0.0658 0.0401 13 GLY B O 2620 N N . TRP B 14 ? 0.7013 0.4820 0.3601 0.0671 -0.0540 0.0295 14 TRP B N 2621 C CA . TRP B 14 ? 0.7412 0.5030 0.3743 0.0859 -0.0589 0.0282 14 TRP B CA 2622 C C . TRP B 14 ? 0.7794 0.5190 0.3854 0.1117 -0.0639 0.0232 14 TRP B C 2623 O O . TRP B 14 ? 0.7579 0.5309 0.3848 0.1259 -0.0582 0.0179 14 TRP B O 2624 C CB . TRP B 14 ? 0.7018 0.5081 0.3648 0.0937 -0.0511 0.0256 14 TRP B CB 2625 C CG . TRP B 14 ? 0.6777 0.5031 0.3610 0.0750 -0.0473 0.0296 14 TRP B CG 2626 C CD1 . TRP B 14 ? 0.6863 0.4906 0.3558 0.0557 -0.0519 0.0358 14 TRP B CD1 2627 C CD2 . TRP B 14 ? 0.6393 0.5101 0.3579 0.0737 -0.0385 0.0277 14 TRP B CD2 2628 N NE1 . TRP B 14 ? 0.6477 0.4849 0.3443 0.0447 -0.0461 0.0375 14 TRP B NE1 2629 C CE2 . TRP B 14 ? 0.6080 0.4829 0.3336 0.0559 -0.0380 0.0323 14 TRP B CE2 2630 C CE3 . TRP B 14 ? 0.6147 0.5232 0.3571 0.0841 -0.0314 0.0226 14 TRP B CE3 2631 C CZ2 . TRP B 14 ? 0.5744 0.4859 0.3291 0.0510 -0.0308 0.0315 14 TRP B CZ2 2632 C CZ3 . TRP B 14 ? 0.5951 0.5371 0.3642 0.0762 -0.0246 0.0224 14 TRP B CZ3 2633 C CH2 . TRP B 14 ? 0.5433 0.4847 0.3179 0.0612 -0.0244 0.0265 14 TRP B CH2 2634 N N . GLN B 15 ? 0.8432 0.5257 0.3994 0.1176 -0.0751 0.0249 15 GLN B N 2635 C CA . GLN B 15 ? 0.8874 0.5414 0.4080 0.1470 -0.0818 0.0198 15 GLN B CA 2636 C C . GLN B 15 ? 0.8780 0.5625 0.4036 0.1764 -0.0790 0.0145 15 GLN B C 2637 O O . GLN B 15 ? 0.8731 0.5719 0.3946 0.2019 -0.0788 0.0084 15 GLN B O 2638 C CB . GLN B 15 ? 0.9619 0.5391 0.4191 0.1467 -0.0960 0.0231 15 GLN B CB 2639 C CG . GLN B 15 ? 1.0040 0.5472 0.4463 0.1184 -0.1007 0.0282 15 GLN B CG 2640 C CD . GLN B 15 ? 1.0482 0.5793 0.4809 0.1296 -0.1024 0.0238 15 GLN B CD 2641 O OE1 . GLN B 15 ? 1.0948 0.6006 0.4948 0.1599 -0.1083 0.0183 15 GLN B OE1 2642 N NE2 . GLN B 15 ? 1.0377 0.5877 0.4971 0.1065 -0.0976 0.0261 15 GLN B NE2 2643 N N . GLY B 16 ? 0.8748 0.5729 0.4091 0.1724 -0.0770 0.0169 16 GLY B N 2644 C CA . GLY B 16 ? 0.8798 0.6087 0.4173 0.1982 -0.0747 0.0126 16 GLY B CA 2645 C C . GLY B 16 ? 0.8311 0.6327 0.4183 0.2003 -0.0629 0.0087 16 GLY B C 2646 O O . GLY B 16 ? 0.8273 0.6630 0.4180 0.2212 -0.0606 0.0049 16 GLY B O 2647 N N . MET B 17 ? 0.7989 0.6249 0.4217 0.1781 -0.0557 0.0097 17 MET B N 2648 C CA . MET B 17 ? 0.7622 0.6493 0.4245 0.1781 -0.0459 0.0062 17 MET B CA 2649 C C . MET B 17 ? 0.7680 0.6638 0.4286 0.1900 -0.0459 0.0019 17 MET B C 2650 O O . MET B 17 ? 0.7469 0.6405 0.4220 0.1742 -0.0434 0.0028 17 MET B O 2651 C CB . MET B 17 ? 0.7187 0.6293 0.4189 0.1493 -0.0380 0.0093 17 MET B CB 2652 C CG . MET B 17 ? 0.6928 0.6592 0.4257 0.1475 -0.0292 0.0061 17 MET B CG 2653 S SD . MET B 17 ? 0.6790 0.6630 0.4466 0.1176 -0.0216 0.0091 17 MET B SD 2654 C CE . MET B 17 ? 0.6530 0.6123 0.4209 0.1065 -0.0228 0.0102 17 MET B CE 2655 N N . VAL B 18 ? 0.7966 0.7065 0.4394 0.2192 -0.0486 -0.0029 18 VAL B N 2656 C CA . VAL B 18 ? 0.8136 0.7266 0.4457 0.2360 -0.0507 -0.0074 18 VAL B CA 2657 C C . VAL B 18 ? 0.7735 0.7523 0.4393 0.2346 -0.0423 -0.0106 18 VAL B C 2658 O O . VAL B 18 ? 0.7805 0.7663 0.4435 0.2429 -0.0429 -0.0137 18 VAL B O 2659 C CB . VAL B 18 ? 0.8676 0.7544 0.4525 0.2731 -0.0603 -0.0116 18 VAL B CB 2660 C CG1 . VAL B 18 ? 0.9265 0.7358 0.4687 0.2713 -0.0706 -0.0079 18 VAL B CG1 2661 C CG2 . VAL B 18 ? 0.8684 0.8014 0.4557 0.2943 -0.0582 -0.0145 18 VAL B CG2 2662 N N . ASP B 19 ? 0.7429 0.7685 0.4379 0.2225 -0.0349 -0.0097 19 ASP B N 2663 C CA . ASP B 19 ? 0.7157 0.8044 0.4359 0.2196 -0.0280 -0.0123 19 ASP B CA 2664 C C . ASP B 19 ? 0.6651 0.7701 0.4186 0.1869 -0.0206 -0.0095 19 ASP B C 2665 O O . ASP B 19 ? 0.6439 0.7987 0.4167 0.1772 -0.0149 -0.0102 19 ASP B O 2666 C CB . ASP B 19 ? 0.7219 0.8628 0.4427 0.2355 -0.0262 -0.0147 19 ASP B CB 2667 C CG . ASP B 19 ? 0.7395 0.8861 0.4737 0.2202 -0.0228 -0.0113 19 ASP B CG 2668 O OD1 . ASP B 19 ? 0.7812 0.8917 0.5236 0.1988 -0.0221 -0.0073 19 ASP B OD1 2669 O OD2 . ASP B 19 ? 0.7704 0.9608 0.5062 0.2307 -0.0211 -0.0129 19 ASP B OD2 2670 N N . GLY B 20 ? 0.6454 0.7083 0.4016 0.1702 -0.0213 -0.0064 20 GLY B N 2671 C CA . GLY B 20 ? 0.5969 0.6687 0.3780 0.1446 -0.0156 -0.0045 20 GLY B CA 2672 C C . GLY B 20 ? 0.5868 0.6144 0.3678 0.1300 -0.0171 -0.0010 20 GLY B C 2673 O O . GLY B 20 ? 0.6134 0.6034 0.3752 0.1356 -0.0227 0.0006 20 GLY B O 2674 N N . TRP B 21 ? 0.5458 0.5785 0.3458 0.1105 -0.0126 0.0002 21 TRP B N 2675 C CA . TRP B 21 ? 0.5268 0.5266 0.3277 0.0979 -0.0137 0.0032 21 TRP B CA 2676 C C . TRP B 21 ? 0.5052 0.4970 0.3124 0.0858 -0.0126 0.0065 21 TRP B C 2677 O O . TRP B 21 ? 0.5009 0.4658 0.3009 0.0800 -0.0158 0.0095 21 TRP B O 2678 C CB . TRP B 21 ? 0.5183 0.5258 0.3330 0.0862 -0.0101 0.0027 21 TRP B CB 2679 C CG . TRP B 21 ? 0.5467 0.5463 0.3531 0.0944 -0.0126 0.0009 21 TRP B CG 2680 C CD1 . TRP B 21 ? 0.5868 0.5579 0.3724 0.1065 -0.0187 0.0006 21 TRP B CD1 2681 C CD2 . TRP B 21 ? 0.5516 0.5685 0.3673 0.0898 -0.0097 -0.0007 21 TRP B CD2 2682 N NE1 . TRP B 21 ? 0.6170 0.5889 0.4006 0.1110 -0.0193 -0.0014 21 TRP B NE1 2683 C CE2 . TRP B 21 ? 0.5741 0.5758 0.3773 0.1008 -0.0136 -0.0022 21 TRP B CE2 2684 C CE3 . TRP B 21 ? 0.5210 0.5612 0.3507 0.0766 -0.0048 -0.0009 21 TRP B CE3 2685 C CZ2 . TRP B 21 ? 0.5512 0.5654 0.3595 0.0996 -0.0121 -0.0039 21 TRP B CZ2 2686 C CZ3 . TRP B 21 ? 0.5178 0.5676 0.3499 0.0741 -0.0038 -0.0022 21 TRP B CZ3 2687 C CH2 . TRP B 21 ? 0.5277 0.5669 0.3512 0.0858 -0.0071 -0.0037 21 TRP B CH2 2688 N N . TYR B 22 ? 0.4801 0.4977 0.3000 0.0806 -0.0083 0.0061 22 TYR B N 2689 C CA . TYR B 22 ? 0.4741 0.4885 0.3010 0.0701 -0.0068 0.0086 22 TYR B CA 2690 C C . TYR B 22 ? 0.4752 0.5101 0.3023 0.0757 -0.0057 0.0079 22 TYR B C 2691 O O . TYR B 22 ? 0.4839 0.5450 0.3110 0.0832 -0.0044 0.0053 22 TYR B O 2692 C CB . TYR B 22 ? 0.4530 0.4751 0.2944 0.0555 -0.0022 0.0086 22 TYR B CB 2693 C CG . TYR B 22 ? 0.4333 0.4509 0.2767 0.0523 -0.0015 0.0075 22 TYR B CG 2694 C CD1 . TYR B 22 ? 0.4303 0.4263 0.2691 0.0523 -0.0043 0.0090 22 TYR B CD1 2695 C CD2 . TYR B 22 ? 0.4381 0.4730 0.2861 0.0473 0.0015 0.0054 22 TYR B CD2 2696 C CE1 . TYR B 22 ? 0.4494 0.4423 0.2905 0.0499 -0.0036 0.0080 22 TYR B CE1 2697 C CE2 . TYR B 22 ? 0.4171 0.4465 0.2656 0.0441 0.0019 0.0047 22 TYR B CE2 2698 C CZ . TYR B 22 ? 0.4243 0.4332 0.2705 0.0466 -0.0004 0.0058 22 TYR B CZ 2699 O OH . TYR B 22 ? 0.4405 0.4447 0.2873 0.0440 0.0000 0.0050 22 TYR B OH 2700 N N . GLY B 23 ? 0.4784 0.5053 0.3053 0.0718 -0.0063 0.0103 23 GLY B N 2701 C CA . GLY B 23 ? 0.4806 0.5257 0.3073 0.0770 -0.0055 0.0099 23 GLY B CA 2702 C C . GLY B 23 ? 0.4913 0.5235 0.3160 0.0728 -0.0070 0.0131 23 GLY B C 2703 O O . GLY B 23 ? 0.4737 0.4934 0.3035 0.0611 -0.0068 0.0155 23 GLY B O 2704 N N . TYR B 24 ? 0.5075 0.5459 0.3235 0.0836 -0.0087 0.0130 24 TYR B N 2705 C CA . TYR B 24 ? 0.5207 0.5555 0.3367 0.0793 -0.0092 0.0157 24 TYR B CA 2706 C C . TYR B 24 ? 0.5590 0.5696 0.3508 0.0921 -0.0158 0.0176 24 TYR B C 2707 O O . TYR B 24 ? 0.5793 0.5875 0.3548 0.1102 -0.0191 0.0153 24 TYR B O 2708 C CB . TYR B 24 ? 0.5038 0.5735 0.3329 0.0775 -0.0042 0.0139 24 TYR B CB 2709 C CG . TYR B 24 ? 0.4909 0.5815 0.3355 0.0654 0.0011 0.0117 24 TYR B CG 2710 C CD1 . TYR B 24 ? 0.4951 0.5809 0.3495 0.0509 0.0037 0.0126 24 TYR B CD1 2711 C CD2 . TYR B 24 ? 0.4804 0.5952 0.3259 0.0687 0.0029 0.0089 24 TYR B CD2 2712 C CE1 . TYR B 24 ? 0.4857 0.5821 0.3466 0.0404 0.0074 0.0105 24 TYR B CE1 2713 C CE2 . TYR B 24 ? 0.4734 0.6022 0.3273 0.0546 0.0068 0.0076 24 TYR B CE2 2714 C CZ . TYR B 24 ? 0.4887 0.6041 0.3483 0.0407 0.0087 0.0084 24 TYR B CZ 2715 O OH . TYR B 24 ? 0.5246 0.6454 0.3851 0.0274 0.0112 0.0070 24 TYR B OH 2716 N N . HIS B 25 ? 0.5788 0.5717 0.3656 0.0833 -0.0183 0.0216 25 HIS B N 2717 C CA . HIS B 25 ? 0.6171 0.5897 0.3802 0.0933 -0.0242 0.0237 25 HIS B CA 2718 C C . HIS B 25 ? 0.6062 0.5991 0.3836 0.0857 -0.0207 0.0252 25 HIS B C 2719 O O . HIS B 25 ? 0.5931 0.5912 0.3855 0.0688 -0.0181 0.0274 25 HIS B O 2720 C CB . HIS B 25 ? 0.6474 0.5742 0.3841 0.0868 -0.0322 0.0284 25 HIS B CB 2721 C CG . HIS B 25 ? 0.6913 0.5876 0.3955 0.0967 -0.0398 0.0308 25 HIS B CG 2722 N ND1 . HIS B 25 ? 0.7383 0.6066 0.4092 0.1185 -0.0466 0.0288 25 HIS B ND1 2723 C CD2 . HIS B 25 ? 0.7088 0.5965 0.4054 0.0890 -0.0423 0.0350 25 HIS B CD2 2724 C CE1 . HIS B 25 ? 0.7639 0.6033 0.4054 0.1242 -0.0534 0.0317 25 HIS B CE1 2725 N NE2 . HIS B 25 ? 0.7427 0.5942 0.4003 0.1054 -0.0507 0.0357 25 HIS B NE2 2726 N N . HIS B 26 ? 0.6176 0.6246 0.3896 0.0994 -0.0207 0.0237 26 HIS B N 2727 C CA . HIS B 26 ? 0.6164 0.6424 0.3999 0.0935 -0.0178 0.0251 26 HIS B CA 2728 C C . HIS B 26 ? 0.6591 0.6581 0.4164 0.1012 -0.0246 0.0285 26 HIS B C 2729 O O . HIS B 26 ? 0.6812 0.6522 0.4087 0.1176 -0.0313 0.0283 26 HIS B O 2730 C CB . HIS B 26 ? 0.5971 0.6669 0.3960 0.1005 -0.0119 0.0210 26 HIS B CB 2731 C CG . HIS B 26 ? 0.6374 0.7141 0.4176 0.1241 -0.0151 0.0190 26 HIS B CG 2732 N ND1 . HIS B 26 ? 0.6539 0.7359 0.4234 0.1408 -0.0167 0.0155 26 HIS B ND1 2733 C CD2 . HIS B 26 ? 0.6599 0.7396 0.4278 0.1362 -0.0174 0.0197 26 HIS B CD2 2734 C CE1 . HIS B 26 ? 0.6903 0.7803 0.4412 0.1639 -0.0199 0.0139 26 HIS B CE1 2735 N NE2 . HIS B 26 ? 0.6994 0.7866 0.4484 0.1616 -0.0205 0.0165 26 HIS B NE2 2736 N N . SER B 27 ? 0.6597 0.6663 0.4254 0.0906 -0.0232 0.0314 27 SER B N 2737 C CA . SER B 27 ? 0.7038 0.6854 0.4449 0.0950 -0.0295 0.0352 27 SER B CA 2738 C C . SER B 27 ? 0.6861 0.6993 0.4458 0.0914 -0.0247 0.0353 27 SER B C 2739 O O . SER B 27 ? 0.6659 0.6962 0.4481 0.0741 -0.0201 0.0363 27 SER B O 2740 C CB . SER B 27 ? 0.7234 0.6685 0.4488 0.0772 -0.0355 0.0411 27 SER B CB 2741 O OG . SER B 27 ? 0.7860 0.6967 0.4782 0.0802 -0.0437 0.0455 27 SER B OG 2742 N N . ASN B 28 ? 0.7065 0.7292 0.4556 0.1093 -0.0256 0.0337 28 ASN B N 2743 C CA . ASN B 28 ? 0.6986 0.7490 0.4614 0.1068 -0.0218 0.0341 28 ASN B CA 2744 C C . ASN B 28 ? 0.7367 0.7701 0.4709 0.1242 -0.0280 0.0358 28 ASN B C 2745 O O . ASN B 28 ? 0.7755 0.7651 0.4744 0.1348 -0.0366 0.0377 28 ASN B O 2746 C CB . ASN B 28 ? 0.6573 0.7584 0.4488 0.1062 -0.0131 0.0292 28 ASN B CB 2747 C CG . ASN B 28 ? 0.6658 0.7865 0.4502 0.1264 -0.0128 0.0249 28 ASN B CG 2748 O OD1 . ASN B 28 ? 0.7351 0.8369 0.4922 0.1475 -0.0189 0.0247 28 ASN B OD1 2749 N ND2 . ASN B 28 ? 0.6381 0.7971 0.4438 0.1204 -0.0062 0.0213 28 ASN B ND2 2750 N N . ASP B 29 ? 0.7320 0.7967 0.4780 0.1271 -0.0242 0.0352 29 ASP B N 2751 C CA . ASP B 29 ? 0.7757 0.8292 0.4951 0.1462 -0.0295 0.0363 29 ASP B CA 2752 C C . ASP B 29 ? 0.8003 0.8546 0.4961 0.1770 -0.0330 0.0320 29 ASP B C 2753 O O . ASP B 29 ? 0.8478 0.8651 0.5049 0.1962 -0.0416 0.0333 29 ASP B O 2754 C CB . ASP B 29 ? 0.7572 0.8510 0.4976 0.1425 -0.0238 0.0361 29 ASP B CB 2755 C CG . ASP B 29 ? 0.7778 0.8607 0.5274 0.1196 -0.0237 0.0411 29 ASP B CG 2756 O OD1 . ASP B 29 ? 0.8223 0.8637 0.5536 0.1095 -0.0300 0.0458 29 ASP B OD1 2757 O OD2 . ASP B 29 ? 0.7868 0.9048 0.5605 0.1111 -0.0176 0.0404 29 ASP B OD2 2758 N N . GLN B 30 ? 0.7797 0.8754 0.4958 0.1818 -0.0269 0.0270 30 GLN B N 2759 C CA . GLN B 30 ? 0.7948 0.9024 0.4918 0.2113 -0.0294 0.0224 30 GLN B CA 2760 C C . GLN B 30 ? 0.8279 0.8823 0.4920 0.2228 -0.0378 0.0225 30 GLN B C 2761 O O . GLN B 30 ? 0.8607 0.9122 0.4979 0.2525 -0.0425 0.0189 30 GLN B O 2762 C CB . GLN B 30 ? 0.7626 0.9318 0.4904 0.2078 -0.0208 0.0179 30 GLN B CB 2763 C CG . GLN B 30 ? 0.7407 0.9679 0.4879 0.2070 -0.0145 0.0165 30 GLN B CG 2764 C CD . GLN B 30 ? 0.7130 0.9841 0.4953 0.1818 -0.0056 0.0151 30 GLN B CD 2765 O OE1 . GLN B 30 ? 0.6973 0.9523 0.4968 0.1565 -0.0028 0.0172 30 GLN B OE1 2766 N NE2 . GLN B 30 ? 0.7064 1.0336 0.4960 0.1887 -0.0017 0.0115 30 GLN B NE2 2767 N N . GLY B 31 ? 0.8234 0.8381 0.4879 0.2001 -0.0399 0.0264 31 GLY B N 2768 C CA . GLY B 31 ? 0.8425 0.8051 0.4760 0.2057 -0.0477 0.0269 31 GLY B CA 2769 C C . GLY B 31 ? 0.8069 0.7747 0.4654 0.1849 -0.0432 0.0267 31 GLY B C 2770 O O . GLY B 31 ? 0.7659 0.7655 0.4614 0.1629 -0.0353 0.0272 31 GLY B O 2771 N N . SER B 32 ? 0.8246 0.7590 0.4599 0.1934 -0.0487 0.0255 32 SER B N 2772 C CA . SER B 32 ? 0.7929 0.7259 0.4470 0.1748 -0.0457 0.0256 32 SER B CA 2773 C C . SER B 32 ? 0.7972 0.7312 0.4412 0.1935 -0.0470 0.0207 32 SER B C 2774 O O . SER B 32 ? 0.8275 0.7557 0.4433 0.2229 -0.0520 0.0174 32 SER B O 2775 C CB . SER B 32 ? 0.8181 0.7004 0.4552 0.1529 -0.0517 0.0319 32 SER B CB 2776 O OG . SER B 32 ? 0.8672 0.6903 0.4525 0.1663 -0.0634 0.0337 32 SER B OG 2777 N N . GLY B 33 ? 0.7650 0.7075 0.4308 0.1780 -0.0428 0.0201 33 GLY B N 2778 C CA . GLY B 33 ? 0.7630 0.7063 0.4211 0.1927 -0.0439 0.0159 33 GLY B CA 2779 C C . GLY B 33 ? 0.7226 0.6863 0.4127 0.1727 -0.0373 0.0152 33 GLY B C 2780 O O . GLY B 33 ? 0.6904 0.6724 0.4097 0.1498 -0.0312 0.0174 33 GLY B O 2781 N N . TYR B 34 ? 0.7251 0.6840 0.4068 0.1834 -0.0389 0.0121 34 TYR B N 2782 C CA . TYR B 34 ? 0.6929 0.6685 0.4004 0.1675 -0.0335 0.0112 34 TYR B CA 2783 C C . TYR B 34 ? 0.6689 0.7013 0.3986 0.1739 -0.0267 0.0066 34 TYR B C 2784 O O . TYR B 34 ? 0.6832 0.7395 0.4017 0.1967 -0.0278 0.0033 34 TYR B O 2785 C CB . TYR B 34 ? 0.7145 0.6489 0.3985 0.1724 -0.0397 0.0110 34 TYR B CB 2786 C CG . TYR B 34 ? 0.7424 0.6202 0.4010 0.1605 -0.0471 0.0162 34 TYR B CG 2787 C CD1 . TYR B 34 ? 0.7146 0.5859 0.3906 0.1330 -0.0447 0.0203 34 TYR B CD1 2788 C CD2 . TYR B 34 ? 0.8070 0.6377 0.4204 0.1766 -0.0572 0.0172 34 TYR B CD2 2789 C CE1 . TYR B 34 ? 0.7374 0.5637 0.3894 0.1186 -0.0517 0.0258 34 TYR B CE1 2790 C CE2 . TYR B 34 ? 0.8291 0.6059 0.4143 0.1611 -0.0650 0.0229 34 TYR B CE2 2791 C CZ . TYR B 34 ? 0.8007 0.5790 0.4069 0.1306 -0.0619 0.0274 34 TYR B CZ 2792 O OH . TYR B 34 ? 0.8084 0.5408 0.3867 0.1119 -0.0697 0.0336 34 TYR B OH 2793 N N . ALA B 35 ? 0.6386 0.6930 0.3966 0.1536 -0.0201 0.0067 35 ALA B N 2794 C CA . ALA B 35 ? 0.6190 0.7215 0.3936 0.1542 -0.0147 0.0031 35 ALA B CA 2795 C C . ALA B 35 ? 0.6023 0.7014 0.3940 0.1343 -0.0112 0.0036 35 ALA B C 2796 O O . ALA B 35 ? 0.5876 0.6703 0.3909 0.1152 -0.0093 0.0064 35 ALA B O 2797 C CB . ALA B 35 ? 0.5950 0.7437 0.3858 0.1483 -0.0093 0.0027 35 ALA B CB 2798 N N . ALA B 36 ? 0.6109 0.7271 0.4027 0.1403 -0.0107 0.0008 36 ALA B N 2799 C CA . ALA B 36 ? 0.6002 0.7147 0.4060 0.1231 -0.0075 0.0011 36 ALA B CA 2800 C C . ALA B 36 ? 0.5854 0.7313 0.4110 0.1026 -0.0013 0.0014 36 ALA B C 2801 O O . ALA B 36 ? 0.5827 0.7653 0.4112 0.1038 0.0009 0.0005 36 ALA B O 2802 C CB . ALA B 36 ? 0.6117 0.7381 0.4106 0.1355 -0.0090 -0.0019 36 ALA B CB 2803 N N . ASP B 37 ? 0.5782 0.7085 0.4138 0.0842 0.0009 0.0028 37 ASP B N 2804 C CA . ASP B 37 ? 0.5748 0.7270 0.4209 0.0653 0.0055 0.0027 37 ASP B CA 2805 C C . ASP B 37 ? 0.5807 0.7546 0.4262 0.0631 0.0064 0.0010 37 ASP B C 2806 O O . ASP B 37 ? 0.5664 0.7203 0.4109 0.0631 0.0053 0.0008 37 ASP B O 2807 C CB . ASP B 37 ? 0.5730 0.6966 0.4246 0.0500 0.0068 0.0044 37 ASP B CB 2808 C CG . ASP B 37 ? 0.5831 0.7193 0.4373 0.0315 0.0102 0.0042 37 ASP B CG 2809 O OD1 . ASP B 37 ? 0.5921 0.7440 0.4472 0.0265 0.0117 0.0044 37 ASP B OD1 2810 O OD2 . ASP B 37 ? 0.5772 0.7049 0.4295 0.0216 0.0108 0.0038 37 ASP B OD2 2811 N N . LYS B 38 ? 0.5859 0.8041 0.4315 0.0608 0.0082 0.0000 38 LYS B N 2812 C CA . LYS B 38 ? 0.5998 0.8479 0.4436 0.0597 0.0086 -0.0015 38 LYS B CA 2813 C C . LYS B 38 ? 0.5917 0.8284 0.4371 0.0361 0.0103 -0.0003 38 LYS B C 2814 O O . LYS B 38 ? 0.5987 0.8322 0.4428 0.0367 0.0095 -0.0009 38 LYS B O 2815 C CB . LYS B 38 ? 0.6085 0.9159 0.4508 0.0626 0.0098 -0.0025 38 LYS B CB 2816 C CG . LYS B 38 ? 0.6556 0.9790 0.4911 0.0927 0.0072 -0.0047 38 LYS B CG 2817 C CD . LYS B 38 ? 0.7113 1.0466 0.5382 0.1150 0.0042 -0.0077 38 LYS B CD 2818 C CE . LYS B 38 ? 0.7468 1.0811 0.5585 0.1491 0.0000 -0.0102 38 LYS B CE 2819 N NZ . LYS B 38 ? 0.7574 1.1242 0.5691 0.1538 0.0011 -0.0101 38 LYS B NZ 2820 N N . GLU B 39 ? 0.5862 0.8135 0.4314 0.0166 0.0121 0.0012 39 GLU B N 2821 C CA . GLU B 39 ? 0.5968 0.8063 0.4360 -0.0050 0.0127 0.0022 39 GLU B CA 2822 C C . GLU B 39 ? 0.5816 0.7471 0.4215 -0.0013 0.0115 0.0021 39 GLU B C 2823 O O . GLU B 39 ? 0.5807 0.7416 0.4161 -0.0086 0.0110 0.0021 39 GLU B O 2824 C CB . GLU B 39 ? 0.6092 0.8103 0.4419 -0.0235 0.0137 0.0034 39 GLU B CB 2825 C CG . GLU B 39 ? 0.6778 0.8589 0.4951 -0.0467 0.0130 0.0043 39 GLU B CG 2826 C CD . GLU B 39 ? 0.7564 0.9458 0.5595 -0.0691 0.0132 0.0055 39 GLU B CD 2827 O OE1 . GLU B 39 ? 0.7710 0.9564 0.5770 -0.0662 0.0140 0.0053 39 GLU B OE1 2828 O OE2 . GLU B 39 ? 0.8166 1.0159 0.6036 -0.0913 0.0122 0.0069 39 GLU B OE2 2829 N N . SER B 40 ? 0.5582 0.6945 0.4027 0.0083 0.0108 0.0024 40 SER B N 2830 C CA . SER B 40 ? 0.5455 0.6471 0.3910 0.0120 0.0096 0.0026 40 SER B CA 2831 C C . SER B 40 ? 0.5335 0.6375 0.3806 0.0242 0.0080 0.0019 40 SER B C 2832 O O . SER B 40 ? 0.5289 0.6163 0.3748 0.0216 0.0075 0.0018 40 SER B O 2833 C CB . SER B 40 ? 0.5409 0.6195 0.3905 0.0186 0.0090 0.0036 40 SER B CB 2834 O OG . SER B 40 ? 0.5431 0.6300 0.3954 0.0319 0.0076 0.0040 40 SER B OG 2835 N N . THR B 41 ? 0.5284 0.6517 0.3758 0.0389 0.0067 0.0010 41 THR B N 2836 C CA . THR B 41 ? 0.5331 0.6566 0.3773 0.0536 0.0043 -0.0003 41 THR B CA 2837 C C . THR B 41 ? 0.5345 0.6827 0.3780 0.0468 0.0054 -0.0014 41 THR B C 2838 O O . THR B 41 ? 0.5266 0.6620 0.3691 0.0490 0.0043 -0.0019 41 THR B O 2839 C CB . THR B 41 ? 0.5382 0.6745 0.3762 0.0740 0.0018 -0.0016 41 THR B CB 2840 O OG1 . THR B 41 ? 0.5509 0.6599 0.3868 0.0776 0.0001 0.0000 41 THR B OG1 2841 C CG2 . THR B 41 ? 0.5491 0.6809 0.3778 0.0919 -0.0016 -0.0036 41 THR B CG2 2842 N N . GLN B 42 ? 0.5371 0.7220 0.3800 0.0365 0.0074 -0.0014 42 GLN B N 2843 C CA . GLN B 42 ? 0.5476 0.7619 0.3877 0.0255 0.0081 -0.0016 42 GLN B CA 2844 C C . GLN B 42 ? 0.5415 0.7256 0.3784 0.0078 0.0084 -0.0002 42 GLN B C 2845 O O . GLN B 42 ? 0.5419 0.7281 0.3775 0.0075 0.0077 -0.0006 42 GLN B O 2846 C CB . GLN B 42 ? 0.5554 0.8163 0.3930 0.0127 0.0098 -0.0010 42 GLN B CB 2847 C CG . GLN B 42 ? 0.5804 0.8842 0.4135 0.0005 0.0101 -0.0007 42 GLN B CG 2848 C CD . GLN B 42 ? 0.6292 0.9587 0.4644 0.0237 0.0086 -0.0034 42 GLN B CD 2849 O OE1 . GLN B 42 ? 0.6678 1.0109 0.5036 0.0488 0.0074 -0.0058 42 GLN B OE1 2850 N NE2 . GLN B 42 ? 0.6271 0.9607 0.4602 0.0165 0.0081 -0.0033 42 GLN B NE2 2851 N N . LYS B 43 ? 0.5447 0.7000 0.3784 -0.0046 0.0091 0.0011 43 LYS B N 2852 C CA . LYS B 43 ? 0.5537 0.6746 0.3795 -0.0172 0.0086 0.0020 43 LYS B CA 2853 C C . LYS B 43 ? 0.5364 0.6326 0.3677 -0.0040 0.0075 0.0013 43 LYS B C 2854 O O . LYS B 43 ? 0.5366 0.6241 0.3632 -0.0099 0.0070 0.0015 43 LYS B O 2855 C CB . LYS B 43 ? 0.5666 0.6590 0.3848 -0.0265 0.0088 0.0028 43 LYS B CB 2856 C CG . LYS B 43 ? 0.6233 0.6831 0.4242 -0.0406 0.0074 0.0034 43 LYS B CG 2857 C CD . LYS B 43 ? 0.7026 0.7334 0.4910 -0.0464 0.0068 0.0033 43 LYS B CD 2858 C CE . LYS B 43 ? 0.7348 0.7255 0.4983 -0.0567 0.0042 0.0034 43 LYS B CE 2859 N NZ . LYS B 43 ? 0.7766 0.7358 0.5264 -0.0549 0.0030 0.0023 43 LYS B NZ 2860 N N . ALA B 44 ? 0.5142 0.5995 0.3535 0.0120 0.0069 0.0009 44 ALA B N 2861 C CA . ALA B 44 ? 0.5023 0.5658 0.3449 0.0226 0.0054 0.0007 44 ALA B CA 2862 C C . ALA B 44 ? 0.5014 0.5819 0.3438 0.0300 0.0043 -0.0006 44 ALA B C 2863 O O . ALA B 44 ? 0.4977 0.5646 0.3396 0.0301 0.0037 -0.0007 44 ALA B O 2864 C CB . ALA B 44 ? 0.4996 0.5493 0.3456 0.0345 0.0040 0.0013 44 ALA B CB 2865 N N . PHE B 45 ? 0.4982 0.6110 0.3400 0.0376 0.0041 -0.0018 45 PHE B N 2866 C CA . PHE B 45 ? 0.5057 0.6404 0.3455 0.0482 0.0028 -0.0038 45 PHE B CA 2867 C C . PHE B 45 ? 0.4940 0.6425 0.3326 0.0324 0.0040 -0.0033 45 PHE B C 2868 O O . PHE B 45 ? 0.4984 0.6433 0.3366 0.0370 0.0030 -0.0041 45 PHE B O 2869 C CB . PHE B 45 ? 0.5125 0.6847 0.3496 0.0624 0.0021 -0.0057 45 PHE B CB 2870 C CG . PHE B 45 ? 0.5286 0.7264 0.3610 0.0785 0.0001 -0.0085 45 PHE B CG 2871 C CD1 . PHE B 45 ? 0.5612 0.7340 0.3857 0.0997 -0.0036 -0.0106 45 PHE B CD1 2872 C CD2 . PHE B 45 ? 0.5477 0.7955 0.3807 0.0717 0.0016 -0.0091 45 PHE B CD2 2873 C CE1 . PHE B 45 ? 0.5711 0.7659 0.3880 0.1175 -0.0059 -0.0138 45 PHE B CE1 2874 C CE2 . PHE B 45 ? 0.5404 0.8177 0.3689 0.0885 -0.0001 -0.0121 45 PHE B CE2 2875 C CZ . PHE B 45 ? 0.5580 0.8073 0.3784 0.1131 -0.0039 -0.0148 45 PHE B CZ 2876 N N . ASP B 46 ? 0.4982 0.6592 0.3332 0.0123 0.0057 -0.0016 46 ASP B N 2877 C CA . ASP B 46 ? 0.5025 0.6715 0.3302 -0.0070 0.0059 -0.0002 46 ASP B CA 2878 C C . ASP B 46 ? 0.4998 0.6253 0.3246 -0.0110 0.0053 0.0004 46 ASP B C 2879 O O . ASP B 46 ? 0.5022 0.6303 0.3249 -0.0137 0.0046 0.0004 46 ASP B O 2880 C CB . ASP B 46 ? 0.5134 0.6983 0.3309 -0.0306 0.0067 0.0018 46 ASP B CB 2881 C CG . ASP B 46 ? 0.5266 0.7663 0.3471 -0.0281 0.0075 0.0013 46 ASP B CG 2882 O OD1 . ASP B 46 ? 0.5204 0.7934 0.3471 -0.0103 0.0071 -0.0008 46 ASP B OD1 2883 O OD2 . ASP B 46 ? 0.5382 0.7877 0.3530 -0.0422 0.0082 0.0028 46 ASP B OD2 2884 N N . GLY B 47 ? 0.4838 0.5733 0.3083 -0.0099 0.0054 0.0009 47 GLY B N 2885 C CA . GLY B 47 ? 0.4844 0.5364 0.3070 -0.0082 0.0047 0.0012 47 GLY B CA 2886 C C . GLY B 47 ? 0.4738 0.5229 0.3046 0.0060 0.0039 0.0001 47 GLY B C 2887 O O . GLY B 47 ? 0.4650 0.5043 0.2928 0.0029 0.0035 0.0003 47 GLY B O 2888 N N . ILE B 48 ? 0.4746 0.5300 0.3127 0.0215 0.0032 -0.0009 48 ILE B N 2889 C CA . ILE B 48 ? 0.4663 0.5131 0.3070 0.0345 0.0014 -0.0019 48 ILE B CA 2890 C C . ILE B 48 ? 0.4764 0.5475 0.3156 0.0361 0.0010 -0.0034 48 ILE B C 2891 O O . ILE B 48 ? 0.4707 0.5308 0.3099 0.0382 0.0002 -0.0037 48 ILE B O 2892 C CB . ILE B 48 ? 0.4693 0.5095 0.3098 0.0498 -0.0006 -0.0025 48 ILE B CB 2893 C CG1 . ILE B 48 ? 0.4633 0.4810 0.3056 0.0463 -0.0004 -0.0005 48 ILE B CG1 2894 C CG2 . ILE B 48 ? 0.4731 0.4998 0.3094 0.0618 -0.0037 -0.0036 48 ILE B CG2 2895 C CD1 . ILE B 48 ? 0.4723 0.4670 0.3160 0.0415 -0.0003 0.0008 48 ILE B CD1 2896 N N . THR B 49 ? 0.4858 0.5937 0.3237 0.0347 0.0016 -0.0041 49 THR B N 2897 C CA . THR B 49 ? 0.4982 0.6393 0.3345 0.0349 0.0013 -0.0053 49 THR B CA 2898 C C . THR B 49 ? 0.5088 0.6407 0.3418 0.0169 0.0019 -0.0035 49 THR B C 2899 O O . THR B 49 ? 0.5094 0.6439 0.3429 0.0210 0.0011 -0.0044 49 THR B O 2900 C CB . THR B 49 ? 0.4981 0.6886 0.3328 0.0326 0.0020 -0.0058 49 THR B CB 2901 O OG1 . THR B 49 ? 0.5056 0.7044 0.3406 0.0537 0.0008 -0.0081 49 THR B OG1 2902 C CG2 . THR B 49 ? 0.4977 0.7303 0.3305 0.0305 0.0017 -0.0067 49 THR B CG2 2903 N N . ASN B 50 ? 0.5252 0.6431 0.3518 -0.0020 0.0029 -0.0010 50 ASN B N 2904 C CA . ASN B 50 ? 0.5497 0.6479 0.3666 -0.0183 0.0024 0.0008 50 ASN B CA 2905 C C . ASN B 50 ? 0.5496 0.6133 0.3699 -0.0088 0.0019 0.0003 50 ASN B C 2906 O O . ASN B 50 ? 0.5586 0.6193 0.3754 -0.0132 0.0013 0.0007 50 ASN B O 2907 C CB . ASN B 50 ? 0.5689 0.6467 0.3711 -0.0372 0.0023 0.0030 50 ASN B CB 2908 C CG . ASN B 50 ? 0.6213 0.6809 0.4044 -0.0565 0.0005 0.0052 50 ASN B CG 2909 O OD1 . ASN B 50 ? 0.6683 0.6862 0.4416 -0.0565 -0.0005 0.0056 50 ASN B OD1 2910 N ND2 . ASN B 50 ? 0.6067 0.6991 0.3824 -0.0726 -0.0002 0.0068 50 ASN B ND2 2911 N N . LYS B 51 ? 0.5427 0.5837 0.3693 0.0030 0.0021 -0.0002 51 LYS B N 2912 C CA . LYS B 51 ? 0.5510 0.5651 0.3804 0.0105 0.0015 -0.0003 51 LYS B CA 2913 C C . LYS B 51 ? 0.5528 0.5766 0.3872 0.0198 0.0006 -0.0017 51 LYS B C 2914 O O . LYS B 51 ? 0.5589 0.5703 0.3917 0.0179 0.0003 -0.0013 51 LYS B O 2915 C CB . LYS B 51 ? 0.5409 0.5378 0.3755 0.0197 0.0015 -0.0002 51 LYS B CB 2916 C CG . LYS B 51 ? 0.5373 0.5161 0.3754 0.0270 0.0006 0.0000 51 LYS B CG 2917 C CD . LYS B 51 ? 0.5122 0.4795 0.3538 0.0326 0.0000 0.0008 51 LYS B CD 2918 C CE . LYS B 51 ? 0.4838 0.4441 0.3225 0.0278 0.0013 0.0017 51 LYS B CE 2919 N NZ . LYS B 51 ? 0.4372 0.3864 0.2778 0.0315 0.0009 0.0029 51 LYS B NZ 2920 N N . VAL B 52 ? 0.5689 0.6132 0.4067 0.0314 -0.0003 -0.0035 52 VAL B N 2921 C CA . VAL B 52 ? 0.5844 0.6336 0.4229 0.0435 -0.0020 -0.0055 52 VAL B CA 2922 C C . VAL B 52 ? 0.5951 0.6673 0.4322 0.0360 -0.0016 -0.0057 52 VAL B C 2923 O O . VAL B 52 ? 0.5937 0.6587 0.4312 0.0391 -0.0024 -0.0063 52 VAL B O 2924 C CB . VAL B 52 ? 0.5916 0.6514 0.4271 0.0620 -0.0044 -0.0081 52 VAL B CB 2925 C CG1 . VAL B 52 ? 0.5924 0.6289 0.4266 0.0661 -0.0053 -0.0072 52 VAL B CG1 2926 C CG2 . VAL B 52 ? 0.6134 0.7160 0.4479 0.0642 -0.0039 -0.0096 52 VAL B CG2 2927 N N . ASN B 53 ? 0.6089 0.7099 0.4432 0.0243 -0.0005 -0.0049 53 ASN B N 2928 C CA . ASN B 53 ? 0.6226 0.7466 0.4526 0.0107 -0.0003 -0.0039 53 ASN B CA 2929 C C . ASN B 53 ? 0.6459 0.7376 0.4700 -0.0023 -0.0003 -0.0016 53 ASN B C 2930 O O . ASN B 53 ? 0.6537 0.7499 0.4769 -0.0040 -0.0009 -0.0016 53 ASN B O 2931 C CB . ASN B 53 ? 0.6196 0.7782 0.4439 -0.0047 0.0002 -0.0023 53 ASN B CB 2932 C CG . ASN B 53 ? 0.6223 0.8251 0.4512 0.0102 0.0001 -0.0050 53 ASN B CG 2933 O OD1 . ASN B 53 ? 0.6444 0.8550 0.4770 0.0320 -0.0011 -0.0083 53 ASN B OD1 2934 N ND2 . ASN B 53 ? 0.6112 0.8419 0.4371 -0.0002 0.0009 -0.0037 53 ASN B ND2 2935 N N . SER B 54 ? 0.6669 0.7262 0.4854 -0.0093 0.0000 0.0000 54 SER B N 2936 C CA . SER B 54 ? 0.6968 0.7222 0.5053 -0.0176 -0.0006 0.0017 54 SER B CA 2937 C C . SER B 54 ? 0.7088 0.7177 0.5249 -0.0047 -0.0007 0.0007 54 SER B C 2938 O O . SER B 54 ? 0.7198 0.7173 0.5293 -0.0102 -0.0013 0.0016 54 SER B O 2939 C CB . SER B 54 ? 0.7061 0.7010 0.5047 -0.0221 -0.0006 0.0028 54 SER B CB 2940 O OG . SER B 54 ? 0.7175 0.7214 0.5034 -0.0383 -0.0012 0.0043 54 SER B OG 2941 N N . VAL B 55 ? 0.7184 0.7242 0.5458 0.0106 -0.0005 -0.0008 55 VAL B N 2942 C CA . VAL B 55 ? 0.7379 0.7288 0.5703 0.0198 -0.0010 -0.0014 55 VAL B CA 2943 C C . VAL B 55 ? 0.7465 0.7559 0.5807 0.0221 -0.0018 -0.0027 55 VAL B C 2944 O O . VAL B 55 ? 0.7506 0.7512 0.5828 0.0192 -0.0019 -0.0021 55 VAL B O 2945 C CB . VAL B 55 ? 0.7340 0.7146 0.5727 0.0320 -0.0017 -0.0021 55 VAL B CB 2946 C CG1 . VAL B 55 ? 0.7393 0.7115 0.5775 0.0301 -0.0010 -0.0010 55 VAL B CG1 2947 C CG2 . VAL B 55 ? 0.7437 0.7383 0.5839 0.0433 -0.0036 -0.0044 55 VAL B CG2 2948 N N . ILE B 56 ? 0.7589 0.7958 0.5953 0.0283 -0.0024 -0.0046 56 ILE B N 2949 C CA . ILE B 56 ? 0.7715 0.8337 0.6085 0.0333 -0.0033 -0.0065 56 ILE B CA 2950 C C . ILE B 56 ? 0.7895 0.8638 0.6218 0.0167 -0.0027 -0.0045 56 ILE B C 2951 O O . ILE B 56 ? 0.7900 0.8638 0.6228 0.0176 -0.0033 -0.0048 56 ILE B O 2952 C CB . ILE B 56 ? 0.7687 0.8647 0.6056 0.0447 -0.0042 -0.0091 56 ILE B CB 2953 C CG1 . ILE B 56 ? 0.7701 0.8474 0.6053 0.0640 -0.0065 -0.0115 56 ILE B CG1 2954 C CG2 . ILE B 56 ? 0.7664 0.9010 0.6023 0.0475 -0.0050 -0.0109 56 ILE B CG2 2955 C CD1 . ILE B 56 ? 0.7728 0.8766 0.6032 0.0799 -0.0082 -0.0146 56 ILE B CD1 2956 N N . GLU B 57 ? 0.8125 0.8955 0.6375 0.0000 -0.0021 -0.0021 57 GLU B N 2957 C CA . GLU B 57 ? 0.8405 0.9334 0.6545 -0.0198 -0.0027 0.0004 57 GLU B CA 2958 C C . GLU B 57 ? 0.8604 0.9145 0.6658 -0.0265 -0.0033 0.0023 57 GLU B C 2959 O O . GLU B 57 ? 0.8703 0.9295 0.6675 -0.0380 -0.0044 0.0040 57 GLU B O 2960 C CB . GLU B 57 ? 0.8507 0.9601 0.6534 -0.0391 -0.0029 0.0029 57 GLU B CB 2961 C CG . GLU B 57 ? 0.8570 1.0238 0.6653 -0.0372 -0.0026 0.0016 57 GLU B CG 2962 C CD . GLU B 57 ? 0.8908 1.0762 0.6916 -0.0518 -0.0024 0.0034 57 GLU B CD 2963 O OE1 . GLU B 57 ? 0.9049 1.0547 0.6944 -0.0642 -0.0027 0.0057 57 GLU B OE1 2964 O OE2 . GLU B 57 ? 0.8952 1.1329 0.7001 -0.0497 -0.0022 0.0024 57 GLU B OE2 2965 N N . LYS B 58 ? 0.8711 0.8897 0.6776 -0.0182 -0.0029 0.0021 58 LYS B N 2966 C CA . LYS B 58 ? 0.8944 0.8788 0.6922 -0.0194 -0.0035 0.0033 58 LYS B CA 2967 C C . LYS B 58 ? 0.9009 0.8875 0.7088 -0.0089 -0.0034 0.0020 58 LYS B C 2968 O O . LYS B 58 ? 0.9089 0.8751 0.7092 -0.0110 -0.0040 0.0032 58 LYS B O 2969 C CB . LYS B 58 ? 0.8952 0.8490 0.6897 -0.0128 -0.0032 0.0034 58 LYS B CB 2970 C CG . LYS B 58 ? 0.9041 0.8395 0.6781 -0.0255 -0.0045 0.0051 58 LYS B CG 2971 C CD . LYS B 58 ? 0.9185 0.8301 0.6667 -0.0395 -0.0073 0.0074 58 LYS B CD 2972 C CE . LYS B 58 ? 0.9260 0.8154 0.6466 -0.0552 -0.0099 0.0093 58 LYS B CE 2973 N NZ . LYS B 58 ? 0.9005 0.8186 0.6156 -0.0761 -0.0106 0.0113 58 LYS B NZ 2974 N N . MET B 59 ? 0.9052 0.9144 0.7272 0.0029 -0.0030 -0.0004 59 MET B N 2975 C CA . MET B 59 ? 0.9151 0.9262 0.7444 0.0127 -0.0034 -0.0020 59 MET B CA 2976 C C . MET B 59 ? 0.9202 0.9659 0.7519 0.0136 -0.0041 -0.0036 59 MET B C 2977 O O . MET B 59 ? 0.9204 0.9723 0.7578 0.0266 -0.0049 -0.0062 59 MET B O 2978 C CB . MET B 59 ? 0.9089 0.9074 0.7460 0.0274 -0.0037 -0.0038 59 MET B CB 2979 C CG . MET B 59 ? 0.9276 0.8986 0.7635 0.0272 -0.0030 -0.0020 59 MET B CG 2980 S SD . MET B 59 ? 0.9715 0.9305 0.8122 0.0360 -0.0034 -0.0023 59 MET B SD 2981 C CE . MET B 59 ? 0.9555 0.9277 0.7958 0.0360 -0.0034 -0.0031 59 MET B CE 2982 N N . ASN B 60 ? 0.9342 1.0029 0.7589 -0.0009 -0.0042 -0.0019 60 ASN B N 2983 C CA . ASN B 60 ? 0.9379 1.0486 0.7638 -0.0023 -0.0049 -0.0029 60 ASN B CA 2984 C C . ASN B 60 ? 0.9398 1.0484 0.7627 -0.0092 -0.0055 -0.0017 60 ASN B C 2985 O O . ASN B 60 ? 0.9340 1.0721 0.7617 -0.0023 -0.0061 -0.0038 60 ASN B O 2986 C CB . ASN B 60 ? 0.9467 1.0910 0.7656 -0.0181 -0.0050 -0.0010 60 ASN B CB 2987 C CG . ASN B 60 ? 0.9559 1.1169 0.7803 -0.0066 -0.0044 -0.0033 60 ASN B CG 2988 O OD1 . ASN B 60 ? 0.9684 1.1201 0.8003 0.0147 -0.0046 -0.0067 60 ASN B OD1 2989 N ND2 . ASN B 60 ? 0.9642 1.1482 0.7819 -0.0220 -0.0042 -0.0011 60 ASN B ND2 2990 N N . THR B 61 ? 0.9492 1.0231 0.7619 -0.0212 -0.0057 0.0014 61 THR B N 2991 C CA . THR B 61 ? 0.9500 1.0118 0.7607 -0.0225 -0.0063 0.0022 61 THR B CA 2992 C C . THR B 61 ? 0.9442 0.9692 0.7595 -0.0097 -0.0055 0.0013 61 THR B C 2993 O O . THR B 61 ? 0.9570 0.9502 0.7625 -0.0133 -0.0056 0.0032 61 THR B O 2994 C CB . THR B 61 ? 0.9689 1.0220 0.7594 -0.0458 -0.0081 0.0066 61 THR B CB 2995 O OG1 . THR B 61 ? 0.9811 1.0676 0.7637 -0.0630 -0.0091 0.0085 61 THR B OG1 2996 C CG2 . THR B 61 ? 0.9640 1.0224 0.7557 -0.0460 -0.0087 0.0068 61 THR B CG2 2997 N N . GLN B 62 ? 0.9248 0.9565 0.7528 0.0059 -0.0053 -0.0017 62 GLN B N 2998 C CA . GLN B 62 ? 0.9126 0.9187 0.7447 0.0153 -0.0049 -0.0021 62 GLN B CA 2999 C C . GLN B 62 ? 0.8985 0.9134 0.7335 0.0175 -0.0054 -0.0030 62 GLN B C 3000 O O . GLN B 62 ? 0.9021 0.9413 0.7351 0.0109 -0.0060 -0.0029 62 GLN B O 3001 C CB . GLN B 62 ? 0.9066 0.9076 0.7462 0.0286 -0.0050 -0.0045 62 GLN B CB 3002 C CG . GLN B 62 ? 0.9104 0.9251 0.7540 0.0413 -0.0067 -0.0080 62 GLN B CG 3003 C CD . GLN B 62 ? 0.9212 0.9164 0.7648 0.0514 -0.0081 -0.0093 62 GLN B CD 3004 O OE1 . GLN B 62 ? 0.9039 0.8889 0.7470 0.0510 -0.0078 -0.0084 62 GLN B OE1 3005 N NE2 . GLN B 62 ? 0.9226 0.9115 0.7642 0.0591 -0.0102 -0.0113 62 GLN B NE2 3006 N N . PHE B 63 ? 0.8812 0.8799 0.7204 0.0253 -0.0054 -0.0036 63 PHE B N 3007 C CA . PHE B 63 ? 0.8603 0.8660 0.7021 0.0278 -0.0059 -0.0045 63 PHE B CA 3008 C C . PHE B 63 ? 0.8461 0.8725 0.6923 0.0388 -0.0074 -0.0085 63 PHE B C 3009 O O . PHE B 63 ? 0.8488 0.8733 0.6951 0.0485 -0.0085 -0.0108 63 PHE B O 3010 C CB . PHE B 63 ? 0.8593 0.8441 0.7029 0.0320 -0.0055 -0.0038 63 PHE B CB 3011 C CG . PHE B 63 ? 0.8619 0.8515 0.7072 0.0327 -0.0058 -0.0042 63 PHE B CG 3012 C CD1 . PHE B 63 ? 0.8736 0.8637 0.7127 0.0237 -0.0056 -0.0019 63 PHE B CD1 3013 C CD2 . PHE B 63 ? 0.8556 0.8457 0.7054 0.0414 -0.0069 -0.0067 63 PHE B CD2 3014 C CE1 . PHE B 63 ? 0.8609 0.8562 0.7020 0.0244 -0.0058 -0.0021 63 PHE B CE1 3015 C CE2 . PHE B 63 ? 0.8498 0.8444 0.7011 0.0420 -0.0072 -0.0071 63 PHE B CE2 3016 C CZ . PHE B 63 ? 0.8450 0.8442 0.6938 0.0340 -0.0063 -0.0049 63 PHE B CZ 3017 N N . GLU B 64 ? 0.8266 0.8715 0.6734 0.0383 -0.0080 -0.0093 64 GLU B N 3018 C CA . GLU B 64 ? 0.8097 0.8722 0.6573 0.0522 -0.0100 -0.0137 64 GLU B CA 3019 C C . GLU B 64 ? 0.7915 0.8470 0.6405 0.0545 -0.0105 -0.0144 64 GLU B C 3020 O O . GLU B 64 ? 0.7878 0.8476 0.6380 0.0440 -0.0093 -0.0117 64 GLU B O 3021 C CB . GLU B 64 ? 0.8118 0.9157 0.6586 0.0510 -0.0104 -0.0149 64 GLU B CB 3022 C CG . GLU B 64 ? 0.8322 0.9483 0.6774 0.0473 -0.0099 -0.0141 64 GLU B CG 3023 C CD . GLU B 64 ? 0.8638 1.0192 0.7068 0.0328 -0.0094 -0.0119 64 GLU B CD 3024 O OE1 . GLU B 64 ? 0.8615 1.0437 0.7048 0.0304 -0.0100 -0.0123 64 GLU B OE1 3025 O OE2 . GLU B 64 ? 0.8799 1.0407 0.7198 0.0222 -0.0087 -0.0097 64 GLU B OE2 3026 N N . ALA B 65 ? 0.7731 0.8146 0.6187 0.0674 -0.0128 -0.0176 65 ALA B N 3027 C CA . ALA B 65 ? 0.7534 0.7887 0.5984 0.0707 -0.0139 -0.0188 65 ALA B CA 3028 C C . ALA B 65 ? 0.7402 0.8064 0.5845 0.0774 -0.0152 -0.0220 65 ALA B C 3029 O O . ALA B 65 ? 0.7475 0.8312 0.5858 0.0909 -0.0175 -0.0260 65 ALA B O 3030 C CB . ALA B 65 ? 0.7624 0.7692 0.5980 0.0796 -0.0171 -0.0210 65 ALA B CB 3031 N N . VAL B 66 ? 0.7118 0.7868 0.5611 0.0692 -0.0138 -0.0201 66 VAL B N 3032 C CA . VAL B 66 ? 0.6841 0.7906 0.5337 0.0738 -0.0148 -0.0226 66 VAL B CA 3033 C C . VAL B 66 ? 0.6673 0.7587 0.5137 0.0831 -0.0168 -0.0254 66 VAL B C 3034 O O . VAL B 66 ? 0.6760 0.7455 0.5256 0.0751 -0.0155 -0.0226 66 VAL B O 3035 C CB . VAL B 66 ? 0.6849 0.8125 0.5392 0.0551 -0.0126 -0.0179 66 VAL B CB 3036 C CG1 . VAL B 66 ? 0.6776 0.8322 0.5334 0.0569 -0.0134 -0.0194 66 VAL B CG1 3037 C CG2 . VAL B 66 ? 0.6809 0.8324 0.5336 0.0455 -0.0119 -0.0159 66 VAL B CG2 3038 N N . GLY B 67 ? 0.6359 0.7394 0.4739 0.1008 -0.0203 -0.0310 67 GLY B N 3039 C CA . GLY B 67 ? 0.5997 0.6885 0.4308 0.1096 -0.0229 -0.0342 67 GLY B CA 3040 C C . GLY B 67 ? 0.5573 0.6645 0.3984 0.0998 -0.0207 -0.0320 67 GLY B C 3041 O O . GLY B 67 ? 0.5628 0.7083 0.4086 0.0983 -0.0200 -0.0321 67 GLY B O 3042 N N . LYS B 68 ? 0.5143 0.5969 0.3579 0.0921 -0.0198 -0.0297 68 LYS B N 3043 C CA . LYS B 68 ? 0.4696 0.5641 0.3204 0.0845 -0.0182 -0.0278 68 LYS B CA 3044 C C . LYS B 68 ? 0.4442 0.5145 0.2881 0.0904 -0.0204 -0.0302 68 LYS B C 3045 O O . LYS B 68 ? 0.4500 0.4906 0.2848 0.0930 -0.0224 -0.0309 68 LYS B O 3046 C CB . LYS B 68 ? 0.4705 0.5570 0.3299 0.0664 -0.0143 -0.0213 68 LYS B CB 3047 C CG . LYS B 68 ? 0.4754 0.5795 0.3371 0.0552 -0.0126 -0.0178 68 LYS B CG 3048 C CD . LYS B 68 ? 0.4719 0.5589 0.3343 0.0408 -0.0102 -0.0121 68 LYS B CD 3049 C CE . LYS B 68 ? 0.4755 0.5739 0.3334 0.0273 -0.0097 -0.0084 68 LYS B CE 3050 N NZ . LYS B 68 ? 0.4692 0.5675 0.3258 0.0296 -0.0099 -0.0093 68 LYS B NZ 3051 N N . GLU B 69 ? 0.3990 0.4821 0.2460 0.0904 -0.0204 -0.0309 69 GLU B N 3052 C CA . GLU B 69 ? 0.4038 0.4659 0.2437 0.0937 -0.0225 -0.0328 69 GLU B CA 3053 C C . GLU B 69 ? 0.3750 0.4398 0.2263 0.0806 -0.0192 -0.0284 69 GLU B C 3054 O O . GLU B 69 ? 0.3480 0.4327 0.2094 0.0718 -0.0161 -0.0248 69 GLU B O 3055 C CB . GLU B 69 ? 0.4249 0.4959 0.2520 0.1118 -0.0271 -0.0397 69 GLU B CB 3056 C CG . GLU B 69 ? 0.4723 0.5343 0.2823 0.1285 -0.0313 -0.0445 69 GLU B CG 3057 C CD . GLU B 69 ? 0.5576 0.6205 0.3475 0.1511 -0.0370 -0.0522 69 GLU B CD 3058 O OE1 . GLU B 69 ? 0.5938 0.6441 0.3764 0.1528 -0.0391 -0.0540 69 GLU B OE1 3059 O OE2 . GLU B 69 ? 0.6641 0.7408 0.4436 0.1685 -0.0397 -0.0565 69 GLU B OE2 3060 N N . PHE B 70 ? 0.3696 0.4133 0.2160 0.0788 -0.0202 -0.0284 70 PHE B N 3061 C CA . PHE B 70 ? 0.3586 0.4031 0.2142 0.0680 -0.0171 -0.0241 70 PHE B CA 3062 C C . PHE B 70 ? 0.3873 0.4233 0.2355 0.0705 -0.0197 -0.0267 70 PHE B C 3063 O O . PHE B 70 ? 0.4201 0.4343 0.2520 0.0758 -0.0240 -0.0302 70 PHE B O 3064 C CB . PHE B 70 ? 0.3523 0.3815 0.2104 0.0591 -0.0149 -0.0195 70 PHE B CB 3065 C CG . PHE B 70 ? 0.3330 0.3655 0.1950 0.0570 -0.0130 -0.0173 70 PHE B CG 3066 C CD1 . PHE B 70 ? 0.3320 0.3750 0.2005 0.0506 -0.0101 -0.0134 70 PHE B CD1 3067 C CD2 . PHE B 70 ? 0.3413 0.3632 0.1969 0.0610 -0.0148 -0.0190 70 PHE B CD2 3068 C CE1 . PHE B 70 ? 0.2811 0.3233 0.1492 0.0471 -0.0090 -0.0113 70 PHE B CE1 3069 C CE2 . PHE B 70 ? 0.3472 0.3733 0.2061 0.0587 -0.0131 -0.0172 70 PHE B CE2 3070 C CZ . PHE B 70 ? 0.3163 0.3524 0.1813 0.0511 -0.0102 -0.0133 70 PHE B CZ 3071 N N . SER B 71 ? 0.3681 0.4185 0.2249 0.0665 -0.0176 -0.0251 71 SER B N 3072 C CA . SER B 71 ? 0.4036 0.4477 0.2543 0.0674 -0.0197 -0.0272 71 SER B CA 3073 C C . SER B 71 ? 0.4169 0.4432 0.2638 0.0573 -0.0194 -0.0241 71 SER B C 3074 O O . SER B 71 ? 0.3836 0.4067 0.2349 0.0510 -0.0171 -0.0201 71 SER B O 3075 C CB . SER B 71 ? 0.3798 0.4472 0.2417 0.0655 -0.0173 -0.0259 71 SER B CB 3076 O OG . SER B 71 ? 0.4122 0.4817 0.2836 0.0555 -0.0134 -0.0202 71 SER B OG 3077 N N . ASN B 72 ? 0.4380 0.4567 0.2762 0.0554 -0.0218 -0.0257 72 ASN B N 3078 C CA . ASN B 72 ? 0.4622 0.4707 0.2950 0.0433 -0.0220 -0.0225 72 ASN B CA 3079 C C . ASN B 72 ? 0.4384 0.4692 0.2886 0.0367 -0.0166 -0.0172 72 ASN B C 3080 O O . ASN B 72 ? 0.4323 0.4650 0.2810 0.0273 -0.0158 -0.0138 72 ASN B O 3081 C CB . ASN B 72 ? 0.5015 0.4895 0.3129 0.0408 -0.0276 -0.0258 72 ASN B CB 3082 C CG . ASN B 72 ? 0.5549 0.5571 0.3716 0.0436 -0.0269 -0.0275 72 ASN B CG 3083 O OD1 . ASN B 72 ? 0.5973 0.6254 0.4339 0.0464 -0.0223 -0.0257 72 ASN B OD1 3084 N ND2 . ASN B 72 ? 0.6302 0.6125 0.4258 0.0417 -0.0322 -0.0307 72 ASN B ND2 3085 N N . LEU B 73 ? 0.4063 0.4547 0.2699 0.0416 -0.0133 -0.0163 73 LEU B N 3086 C CA . LEU B 73 ? 0.3843 0.4475 0.2587 0.0386 -0.0090 -0.0113 73 LEU B CA 3087 C C . LEU B 73 ? 0.3560 0.4181 0.2342 0.0405 -0.0068 -0.0087 73 LEU B C 3088 O O . LEU B 73 ? 0.3452 0.4134 0.2268 0.0412 -0.0042 -0.0051 73 LEU B O 3089 C CB . LEU B 73 ? 0.4002 0.4778 0.2810 0.0404 -0.0077 -0.0111 73 LEU B CB 3090 C CG . LEU B 73 ? 0.4578 0.5420 0.3376 0.0382 -0.0086 -0.0124 73 LEU B CG 3091 C CD1 . LEU B 73 ? 0.5291 0.6009 0.3975 0.0403 -0.0132 -0.0180 73 LEU B CD1 3092 C CD2 . LEU B 73 ? 0.4559 0.5554 0.3436 0.0404 -0.0066 -0.0111 73 LEU B CD2 3093 N N . GLU B 74 ? 0.3298 0.3808 0.2037 0.0417 -0.0084 -0.0104 74 GLU B N 3094 C CA . GLU B 74 ? 0.3027 0.3507 0.1783 0.0425 -0.0068 -0.0081 74 GLU B CA 3095 C C . GLU B 74 ? 0.2941 0.3316 0.1655 0.0405 -0.0074 -0.0076 74 GLU B C 3096 O O . GLU B 74 ? 0.2797 0.3104 0.1498 0.0421 -0.0076 -0.0079 74 GLU B O 3097 C CB . GLU B 74 ? 0.2996 0.3507 0.1754 0.0453 -0.0077 -0.0103 74 GLU B CB 3098 C CG . GLU B 74 ? 0.3333 0.3985 0.2124 0.0444 -0.0071 -0.0097 74 GLU B CG 3099 C CD . GLU B 74 ? 0.3714 0.4481 0.2500 0.0450 -0.0083 -0.0113 74 GLU B CD 3100 O OE1 . GLU B 74 ? 0.3555 0.4331 0.2315 0.0512 -0.0105 -0.0155 74 GLU B OE1 3101 O OE2 . GLU B 74 ? 0.3468 0.4312 0.2247 0.0388 -0.0074 -0.0082 74 GLU B OE2 3102 N N . ARG B 75 ? 0.2848 0.3232 0.1532 0.0355 -0.0078 -0.0064 75 ARG B N 3103 C CA . ARG B 75 ? 0.2843 0.3156 0.1469 0.0306 -0.0089 -0.0052 75 ARG B CA 3104 C C . ARG B 75 ? 0.2588 0.2953 0.1258 0.0332 -0.0060 -0.0021 75 ARG B C 3105 O O . ARG B 75 ? 0.2535 0.2821 0.1173 0.0318 -0.0068 -0.0019 75 ARG B O 3106 C CB . ARG B 75 ? 0.3010 0.3384 0.1575 0.0207 -0.0102 -0.0037 75 ARG B CB 3107 C CG . ARG B 75 ? 0.3765 0.4005 0.2217 0.0172 -0.0145 -0.0073 75 ARG B CG 3108 C CD . ARG B 75 ? 0.5570 0.5536 0.3854 0.0159 -0.0194 -0.0100 75 ARG B CD 3109 N NE . ARG B 75 ? 0.6806 0.6587 0.4965 0.0226 -0.0238 -0.0153 75 ARG B NE 3110 C CZ . ARG B 75 ? 0.7434 0.7160 0.5595 0.0355 -0.0247 -0.0192 75 ARG B CZ 3111 N NH1 . ARG B 75 ? 0.7039 0.6863 0.5325 0.0406 -0.0214 -0.0181 75 ARG B NH1 3112 N NH2 . ARG B 75 ? 0.7975 0.7565 0.5992 0.0441 -0.0292 -0.0245 75 ARG B NH2 3113 N N . ARG B 76 ? 0.2520 0.2995 0.1234 0.0381 -0.0031 0.0002 76 ARG B N 3114 C CA . ARG B 76 ? 0.2586 0.3065 0.1286 0.0435 -0.0012 0.0027 76 ARG B CA 3115 C C . ARG B 76 ? 0.2668 0.2986 0.1351 0.0452 -0.0017 0.0016 76 ARG B C 3116 O O . ARG B 76 ? 0.2703 0.2963 0.1364 0.0461 -0.0016 0.0022 76 ARG B O 3117 C CB . ARG B 76 ? 0.2593 0.3151 0.1273 0.0514 0.0007 0.0050 76 ARG B CB 3118 C CG . ARG B 76 ? 0.2817 0.3617 0.1507 0.0527 0.0019 0.0068 76 ARG B CG 3119 C CD . ARG B 76 ? 0.2614 0.3473 0.1262 0.0627 0.0032 0.0083 76 ARG B CD 3120 N NE . ARG B 76 ? 0.2579 0.3336 0.1244 0.0598 0.0025 0.0072 76 ARG B NE 3121 C CZ . ARG B 76 ? 0.2453 0.3094 0.1034 0.0661 0.0024 0.0083 76 ARG B CZ 3122 N NH1 . ARG B 76 ? 0.2725 0.3297 0.1173 0.0777 0.0025 0.0102 76 ARG B NH1 3123 N NH2 . ARG B 76 ? 0.2580 0.3169 0.1178 0.0614 0.0016 0.0077 76 ARG B NH2 3124 N N . LEU B 77 ? 0.2693 0.2975 0.1383 0.0449 -0.0023 0.0003 77 LEU B N 3125 C CA . LEU B 77 ? 0.2842 0.3037 0.1508 0.0441 -0.0029 -0.0004 77 LEU B CA 3126 C C . LEU B 77 ? 0.2772 0.2927 0.1449 0.0432 -0.0046 -0.0031 77 LEU B C 3127 O O . LEU B 77 ? 0.2814 0.2906 0.1471 0.0432 -0.0046 -0.0029 77 LEU B O 3128 C CB . LEU B 77 ? 0.2743 0.2992 0.1410 0.0419 -0.0035 -0.0010 77 LEU B CB 3129 C CG . LEU B 77 ? 0.3307 0.3558 0.1944 0.0380 -0.0045 -0.0013 77 LEU B CG 3130 C CD1 . LEU B 77 ? 0.3442 0.3543 0.1974 0.0354 -0.0042 0.0019 77 LEU B CD1 3131 C CD2 . LEU B 77 ? 0.2992 0.3383 0.1635 0.0341 -0.0053 -0.0016 77 LEU B CD2 3132 N N . GLU B 78 ? 0.2983 0.3144 0.1659 0.0427 -0.0066 -0.0058 78 GLU B N 3133 C CA . GLU B 78 ? 0.3057 0.3114 0.1677 0.0434 -0.0093 -0.0085 78 GLU B CA 3134 C C . GLU B 78 ? 0.3077 0.3071 0.1677 0.0402 -0.0088 -0.0061 78 GLU B C 3135 O O . GLU B 78 ? 0.2975 0.2890 0.1549 0.0414 -0.0097 -0.0069 78 GLU B O 3136 C CB . GLU B 78 ? 0.3381 0.3371 0.1922 0.0431 -0.0129 -0.0115 78 GLU B CB 3137 C CG . GLU B 78 ? 0.4110 0.3919 0.2519 0.0466 -0.0171 -0.0149 78 GLU B CG 3138 C CD . GLU B 78 ? 0.5556 0.5183 0.3788 0.0460 -0.0223 -0.0179 78 GLU B CD 3139 O OE1 . GLU B 78 ? 0.6072 0.5738 0.4303 0.0412 -0.0223 -0.0172 78 GLU B OE1 3140 O OE2 . GLU B 78 ? 0.6270 0.5683 0.4330 0.0505 -0.0269 -0.0208 78 GLU B OE2 3141 N N . ASN B 79 ? 0.3183 0.3253 0.1797 0.0367 -0.0074 -0.0032 79 ASN B N 3142 C CA . ASN B 79 ? 0.3252 0.3327 0.1843 0.0332 -0.0071 -0.0009 79 ASN B CA 3143 C C . ASN B 79 ? 0.3213 0.3278 0.1832 0.0388 -0.0048 0.0003 79 ASN B C 3144 O O . ASN B 79 ? 0.3135 0.3147 0.1734 0.0379 -0.0052 0.0007 79 ASN B O 3145 C CB . ASN B 79 ? 0.3358 0.3609 0.1954 0.0287 -0.0061 0.0019 79 ASN B CB 3146 C CG . ASN B 79 ? 0.3989 0.4325 0.2557 0.0236 -0.0062 0.0045 79 ASN B CG 3147 O OD1 . ASN B 79 ? 0.4122 0.4609 0.2721 0.0295 -0.0036 0.0066 79 ASN B OD1 3148 N ND2 . ASN B 79 ? 0.4458 0.4678 0.2933 0.0135 -0.0097 0.0042 79 ASN B ND2 3149 N N . LEU B 80 ? 0.3317 0.3399 0.1949 0.0436 -0.0030 0.0010 80 LEU B N 3150 C CA . LEU B 80 ? 0.3428 0.3428 0.2020 0.0475 -0.0020 0.0022 80 LEU B CA 3151 C C . LEU B 80 ? 0.3449 0.3362 0.2041 0.0450 -0.0031 0.0004 80 LEU B C 3152 O O . LEU B 80 ? 0.3446 0.3295 0.2012 0.0456 -0.0029 0.0010 80 LEU B O 3153 C CB . LEU B 80 ? 0.3514 0.3478 0.2050 0.0505 -0.0013 0.0035 80 LEU B CB 3154 C CG . LEU B 80 ? 0.4204 0.4017 0.2609 0.0549 -0.0013 0.0054 80 LEU B CG 3155 C CD1 . LEU B 80 ? 0.4785 0.4512 0.3069 0.0581 -0.0018 0.0071 80 LEU B CD1 3156 C CD2 . LEU B 80 ? 0.4609 0.4315 0.2985 0.0490 -0.0023 0.0048 80 LEU B CD2 3157 N N . ASN B 81 ? 0.3498 0.3436 0.2112 0.0435 -0.0044 -0.0020 81 ASN B N 3158 C CA . ASN B 81 ? 0.3702 0.3627 0.2310 0.0434 -0.0057 -0.0041 81 ASN B CA 3159 C C . ASN B 81 ? 0.3738 0.3588 0.2329 0.0443 -0.0071 -0.0052 81 ASN B C 3160 O O . ASN B 81 ? 0.3763 0.3578 0.2342 0.0446 -0.0070 -0.0053 81 ASN B O 3161 C CB . ASN B 81 ? 0.3611 0.3632 0.2233 0.0451 -0.0073 -0.0072 81 ASN B CB 3162 C CG . ASN B 81 ? 0.4056 0.4151 0.2664 0.0471 -0.0085 -0.0095 81 ASN B CG 3163 O OD1 . ASN B 81 ? 0.4333 0.4426 0.2910 0.0537 -0.0110 -0.0131 81 ASN B OD1 3164 N ND2 . ASN B 81 ? 0.4098 0.4255 0.2697 0.0415 -0.0074 -0.0074 81 ASN B ND2 3165 N N . LYS B 82 ? 0.3922 0.3737 0.2488 0.0431 -0.0087 -0.0057 82 LYS B N 3166 C CA . LYS B 82 ? 0.4172 0.3876 0.2670 0.0409 -0.0111 -0.0061 82 LYS B CA 3167 C C . LYS B 82 ? 0.4195 0.3915 0.2716 0.0384 -0.0091 -0.0030 82 LYS B C 3168 O O . LYS B 82 ? 0.4240 0.3885 0.2733 0.0389 -0.0100 -0.0034 82 LYS B O 3169 C CB . LYS B 82 ? 0.4408 0.4058 0.2828 0.0354 -0.0138 -0.0061 82 LYS B CB 3170 C CG . LYS B 82 ? 0.4999 0.4506 0.3293 0.0282 -0.0172 -0.0050 82 LYS B CG 3171 C CD . LYS B 82 ? 0.5777 0.5243 0.3959 0.0178 -0.0202 -0.0039 82 LYS B CD 3172 C CE . LYS B 82 ? 0.6442 0.5654 0.4397 0.0091 -0.0262 -0.0038 82 LYS B CE 3173 N NZ . LYS B 82 ? 0.6767 0.6022 0.4733 0.0027 -0.0254 -0.0004 82 LYS B NZ 3174 N N . LYS B 83 ? 0.4176 0.4005 0.2734 0.0378 -0.0067 -0.0002 83 LYS B N 3175 C CA . LYS B 83 ? 0.4352 0.4232 0.2914 0.0389 -0.0049 0.0022 83 LYS B CA 3176 C C . LYS B 83 ? 0.4325 0.4119 0.2883 0.0430 -0.0039 0.0017 83 LYS B C 3177 O O . LYS B 83 ? 0.4371 0.4146 0.2915 0.0435 -0.0036 0.0026 83 LYS B O 3178 C CB . LYS B 83 ? 0.4236 0.4259 0.2807 0.0432 -0.0027 0.0044 83 LYS B CB 3179 C CG . LYS B 83 ? 0.4926 0.5105 0.3507 0.0385 -0.0031 0.0054 83 LYS B CG 3180 C CD . LYS B 83 ? 0.5446 0.5733 0.3998 0.0292 -0.0046 0.0073 83 LYS B CD 3181 C CE . LYS B 83 ? 0.6004 0.6459 0.4560 0.0341 -0.0028 0.0095 83 LYS B CE 3182 N NZ . LYS B 83 ? 0.6147 0.6743 0.4666 0.0212 -0.0047 0.0119 83 LYS B NZ 3183 N N . MET B 84 ? 0.4342 0.4099 0.2897 0.0446 -0.0036 0.0008 84 MET B N 3184 C CA . MET B 84 ? 0.4624 0.4303 0.3140 0.0448 -0.0032 0.0009 84 MET B CA 3185 C C . MET B 84 ? 0.4705 0.4367 0.3237 0.0432 -0.0044 -0.0009 84 MET B C 3186 O O . MET B 84 ? 0.4664 0.4277 0.3175 0.0430 -0.0040 -0.0004 84 MET B O 3187 C CB . MET B 84 ? 0.4514 0.4181 0.2991 0.0427 -0.0032 0.0011 84 MET B CB 3188 C CG . MET B 84 ? 0.5334 0.4915 0.3731 0.0390 -0.0034 0.0019 84 MET B CG 3189 S SD . MET B 84 ? 0.6020 0.5624 0.4342 0.0302 -0.0045 0.0027 84 MET B SD 3190 C CE . MET B 84 ? 0.5903 0.5747 0.4355 0.0308 -0.0051 -0.0007 84 MET B CE 3191 N N . GLU B 85 ? 0.4896 0.4595 0.3446 0.0438 -0.0062 -0.0035 85 GLU B N 3192 C CA . GLU B 85 ? 0.5287 0.4974 0.3819 0.0460 -0.0079 -0.0060 85 GLU B CA 3193 C C . GLU B 85 ? 0.5448 0.5031 0.3947 0.0456 -0.0091 -0.0054 85 GLU B C 3194 O O . GLU B 85 ? 0.5719 0.5275 0.4208 0.0463 -0.0091 -0.0055 85 GLU B O 3195 C CB . GLU B 85 ? 0.5302 0.5053 0.3814 0.0509 -0.0102 -0.0095 85 GLU B CB 3196 C CG . GLU B 85 ? 0.5526 0.5444 0.4073 0.0490 -0.0089 -0.0095 85 GLU B CG 3197 C CD . GLU B 85 ? 0.5948 0.6026 0.4479 0.0558 -0.0111 -0.0134 85 GLU B CD 3198 O OE1 . GLU B 85 ? 0.6263 0.6270 0.4737 0.0639 -0.0139 -0.0166 85 GLU B OE1 3199 O OE2 . GLU B 85 ? 0.5599 0.5880 0.4146 0.0528 -0.0104 -0.0132 85 GLU B OE2 3200 N N . ASP B 86 ? 0.5636 0.5180 0.4111 0.0425 -0.0102 -0.0043 86 ASP B N 3201 C CA . ASP B 86 ? 0.5774 0.5260 0.4206 0.0378 -0.0112 -0.0024 86 ASP B CA 3202 C C . ASP B 86 ? 0.5716 0.5264 0.4197 0.0379 -0.0084 0.0000 86 ASP B C 3203 O O . ASP B 86 ? 0.5785 0.5290 0.4240 0.0361 -0.0091 0.0006 86 ASP B O 3204 C CB . ASP B 86 ? 0.5895 0.5417 0.4295 0.0309 -0.0122 -0.0004 86 ASP B CB 3205 C CG . ASP B 86 ? 0.6423 0.5800 0.4698 0.0282 -0.0168 -0.0024 86 ASP B CG 3206 O OD1 . ASP B 86 ? 0.6885 0.6138 0.5095 0.0352 -0.0192 -0.0059 86 ASP B OD1 3207 O OD2 . ASP B 86 ? 0.6617 0.6015 0.4838 0.0195 -0.0182 -0.0005 86 ASP B OD2 3208 N N . GLY B 87 ? 0.5542 0.5166 0.4061 0.0406 -0.0056 0.0011 87 GLY B N 3209 C CA . GLY B 87 ? 0.5401 0.5046 0.3913 0.0437 -0.0037 0.0029 87 GLY B CA 3210 C C . GLY B 87 ? 0.5344 0.4901 0.3840 0.0443 -0.0036 0.0021 87 GLY B C 3211 O O . GLY B 87 ? 0.5385 0.4937 0.3871 0.0447 -0.0033 0.0029 87 GLY B O 3212 N N . PHE B 88 ? 0.5208 0.4732 0.3700 0.0435 -0.0039 0.0005 88 PHE B N 3213 C CA . PHE B 88 ? 0.5205 0.4694 0.3675 0.0422 -0.0038 0.0000 88 PHE B CA 3214 C C . PHE B 88 ? 0.5280 0.4768 0.3769 0.0428 -0.0053 -0.0014 88 PHE B C 3215 O O . PHE B 88 ? 0.5238 0.4698 0.3716 0.0424 -0.0050 -0.0011 88 PHE B O 3216 C CB . PHE B 88 ? 0.5188 0.4720 0.3638 0.0390 -0.0040 -0.0008 88 PHE B CB 3217 C CG . PHE B 88 ? 0.5058 0.4508 0.3416 0.0361 -0.0035 0.0012 88 PHE B CG 3218 C CD1 . PHE B 88 ? 0.5065 0.4370 0.3313 0.0359 -0.0033 0.0027 88 PHE B CD1 3219 C CD2 . PHE B 88 ? 0.4965 0.4448 0.3311 0.0343 -0.0037 0.0014 88 PHE B CD2 3220 C CE1 . PHE B 88 ? 0.5038 0.4181 0.3121 0.0348 -0.0042 0.0045 88 PHE B CE1 3221 C CE2 . PHE B 88 ? 0.4887 0.4237 0.3096 0.0317 -0.0041 0.0036 88 PHE B CE2 3222 C CZ . PHE B 88 ? 0.5120 0.4275 0.3177 0.0322 -0.0047 0.0051 88 PHE B CZ 3223 N N . LEU B 89 ? 0.5350 0.4833 0.3834 0.0441 -0.0075 -0.0030 89 LEU B N 3224 C CA . LEU B 89 ? 0.5576 0.4979 0.4007 0.0456 -0.0103 -0.0042 89 LEU B CA 3225 C C . LEU B 89 ? 0.5588 0.4947 0.4008 0.0414 -0.0101 -0.0016 89 LEU B C 3226 O O . LEU B 89 ? 0.5651 0.4965 0.4048 0.0420 -0.0109 -0.0017 89 LEU B O 3227 C CB . LEU B 89 ? 0.5749 0.5076 0.4104 0.0474 -0.0137 -0.0061 89 LEU B CB 3228 C CG . LEU B 89 ? 0.6342 0.5480 0.4550 0.0478 -0.0184 -0.0069 89 LEU B CG 3229 C CD1 . LEU B 89 ? 0.6546 0.5664 0.4715 0.0558 -0.0195 -0.0092 89 LEU B CD1 3230 C CD2 . LEU B 89 ? 0.6860 0.5866 0.4936 0.0496 -0.0226 -0.0090 89 LEU B CD2 3231 N N . ASP B 90 ? 0.5494 0.4908 0.3932 0.0375 -0.0092 0.0007 90 ASP B N 3232 C CA . ASP B 90 ? 0.5575 0.5033 0.4006 0.0334 -0.0090 0.0034 90 ASP B CA 3233 C C . ASP B 90 ? 0.5488 0.4980 0.3954 0.0374 -0.0064 0.0039 90 ASP B C 3234 O O . ASP B 90 ? 0.5441 0.4937 0.3895 0.0354 -0.0068 0.0050 90 ASP B O 3235 C CB . ASP B 90 ? 0.5553 0.5148 0.3990 0.0292 -0.0086 0.0058 90 ASP B CB 3236 C CG . ASP B 90 ? 0.6059 0.5593 0.4420 0.0217 -0.0120 0.0060 90 ASP B CG 3237 O OD1 . ASP B 90 ? 0.6270 0.5621 0.4520 0.0179 -0.0159 0.0051 90 ASP B OD1 3238 O OD2 . ASP B 90 ? 0.6379 0.6023 0.4760 0.0202 -0.0112 0.0068 90 ASP B OD2 3239 N N . VAL B 91 ? 0.5385 0.4876 0.3864 0.0420 -0.0043 0.0032 91 VAL B N 3240 C CA . VAL B 91 ? 0.5403 0.4854 0.3854 0.0450 -0.0029 0.0034 91 VAL B CA 3241 C C . VAL B 91 ? 0.5471 0.4870 0.3925 0.0430 -0.0035 0.0022 91 VAL B C 3242 O O . VAL B 91 ? 0.5441 0.4828 0.3885 0.0433 -0.0031 0.0029 91 VAL B O 3243 C CB . VAL B 91 ? 0.5516 0.4900 0.3904 0.0476 -0.0020 0.0032 91 VAL B CB 3244 C CG1 . VAL B 91 ? 0.5397 0.4664 0.3699 0.0469 -0.0018 0.0030 91 VAL B CG1 3245 C CG2 . VAL B 91 ? 0.5373 0.4800 0.3720 0.0541 -0.0013 0.0043 91 VAL B CG2 3246 N N . TRP B 92 ? 0.5522 0.4919 0.3986 0.0421 -0.0045 0.0004 92 TRP B N 3247 C CA . TRP B 92 ? 0.5724 0.5124 0.4183 0.0422 -0.0052 -0.0009 92 TRP B CA 3248 C C . TRP B 92 ? 0.5672 0.5021 0.4113 0.0432 -0.0073 -0.0009 92 TRP B C 3249 O O . TRP B 92 ? 0.5760 0.5102 0.4194 0.0437 -0.0073 -0.0010 92 TRP B O 3250 C CB . TRP B 92 ? 0.5771 0.5256 0.4229 0.0431 -0.0058 -0.0030 92 TRP B CB 3251 C CG . TRP B 92 ? 0.6154 0.5668 0.4587 0.0378 -0.0043 -0.0020 92 TRP B CG 3252 C CD1 . TRP B 92 ? 0.6383 0.5907 0.4804 0.0361 -0.0041 -0.0016 92 TRP B CD1 3253 C CD2 . TRP B 92 ? 0.6425 0.5920 0.4798 0.0319 -0.0035 -0.0008 92 TRP B CD2 3254 N NE1 . TRP B 92 ? 0.6520 0.6008 0.4856 0.0290 -0.0036 0.0000 92 TRP B NE1 3255 C CE2 . TRP B 92 ? 0.6582 0.6039 0.4873 0.0256 -0.0035 0.0004 92 TRP B CE2 3256 C CE3 . TRP B 92 ? 0.6574 0.6058 0.4927 0.0302 -0.0032 -0.0006 92 TRP B CE3 3257 C CZ2 . TRP B 92 ? 0.6853 0.6225 0.5008 0.0162 -0.0039 0.0021 92 TRP B CZ2 3258 C CZ3 . TRP B 92 ? 0.6729 0.6160 0.4975 0.0216 -0.0030 0.0007 92 TRP B CZ3 3259 C CH2 . TRP B 92 ? 0.6946 0.6302 0.5076 0.0140 -0.0037 0.0022 92 TRP B CH2 3260 N N . THR B 93 ? 0.5726 0.5024 0.4134 0.0417 -0.0094 -0.0003 93 THR B N 3261 C CA . THR B 93 ? 0.5803 0.4999 0.4133 0.0392 -0.0126 0.0004 93 THR B CA 3262 C C . THR B 93 ? 0.5775 0.5029 0.4140 0.0352 -0.0109 0.0031 93 THR B C 3263 O O . THR B 93 ? 0.5716 0.4924 0.4054 0.0351 -0.0118 0.0033 93 THR B O 3264 C CB . THR B 93 ? 0.5999 0.5100 0.4232 0.0343 -0.0162 0.0012 93 THR B CB 3265 O OG1 . THR B 93 ? 0.6006 0.5037 0.4183 0.0405 -0.0182 -0.0019 93 THR B OG1 3266 C CG2 . THR B 93 ? 0.6207 0.5145 0.4290 0.0279 -0.0206 0.0029 93 THR B CG2 3267 N N . TYR B 94 ? 0.5681 0.5050 0.4096 0.0339 -0.0086 0.0049 94 TYR B N 3268 C CA . TYR B 94 ? 0.5639 0.5107 0.4077 0.0338 -0.0069 0.0068 94 TYR B CA 3269 C C . TYR B 94 ? 0.5589 0.5015 0.4041 0.0382 -0.0052 0.0055 94 TYR B C 3270 O O . TYR B 94 ? 0.5544 0.4982 0.3992 0.0370 -0.0053 0.0064 94 TYR B O 3271 C CB . TYR B 94 ? 0.5696 0.5303 0.4155 0.0370 -0.0049 0.0078 94 TYR B CB 3272 C CG . TYR B 94 ? 0.5781 0.5502 0.4236 0.0425 -0.0032 0.0087 94 TYR B CG 3273 C CD1 . TYR B 94 ? 0.6013 0.5939 0.4470 0.0393 -0.0037 0.0112 94 TYR B CD1 3274 C CD2 . TYR B 94 ? 0.6025 0.5651 0.4441 0.0506 -0.0017 0.0071 94 TYR B CD2 3275 C CE1 . TYR B 94 ? 0.6104 0.6176 0.4547 0.0473 -0.0023 0.0115 94 TYR B CE1 3276 C CE2 . TYR B 94 ? 0.6308 0.5999 0.4674 0.0585 -0.0009 0.0072 94 TYR B CE2 3277 C CZ . TYR B 94 ? 0.6293 0.6225 0.4684 0.0586 -0.0010 0.0091 94 TYR B CZ 3278 O OH . TYR B 94 ? 0.6417 0.6448 0.4749 0.0694 -0.0004 0.0087 94 TYR B OH 3279 N N . ASN B 95 ? 0.5505 0.4885 0.3955 0.0413 -0.0039 0.0038 95 ASN B N 3280 C CA . ASN B 95 ? 0.5472 0.4808 0.3901 0.0420 -0.0028 0.0030 95 ASN B CA 3281 C C . ASN B 95 ? 0.5414 0.4745 0.3856 0.0407 -0.0039 0.0022 95 ASN B C 3282 O O . ASN B 95 ? 0.5405 0.4730 0.3840 0.0404 -0.0033 0.0025 95 ASN B O 3283 C CB . ASN B 95 ? 0.5518 0.4815 0.3907 0.0408 -0.0022 0.0019 95 ASN B CB 3284 C CG . ASN B 95 ? 0.5734 0.4957 0.4039 0.0434 -0.0016 0.0027 95 ASN B CG 3285 O OD1 . ASN B 95 ? 0.5681 0.4915 0.3964 0.0491 -0.0012 0.0035 95 ASN B OD1 3286 N ND2 . ASN B 95 ? 0.5850 0.5009 0.4084 0.0399 -0.0019 0.0024 95 ASN B ND2 3287 N N . ALA B 96 ? 0.5321 0.4645 0.3760 0.0416 -0.0058 0.0009 96 ALA B N 3288 C CA . ALA B 96 ? 0.5351 0.4657 0.3762 0.0439 -0.0076 -0.0002 96 ALA B CA 3289 C C . ALA B 96 ? 0.5380 0.4615 0.3758 0.0414 -0.0093 0.0017 96 ALA B C 3290 O O . ALA B 96 ? 0.5335 0.4571 0.3710 0.0418 -0.0092 0.0019 96 ALA B O 3291 C CB . ALA B 96 ? 0.5372 0.4665 0.3735 0.0493 -0.0102 -0.0027 96 ALA B CB 3292 N N . GLU B 97 ? 0.5344 0.4542 0.3690 0.0371 -0.0110 0.0035 97 GLU B N 3293 C CA . GLU B 97 ? 0.5436 0.4588 0.3721 0.0309 -0.0133 0.0062 97 GLU B CA 3294 C C . GLU B 97 ? 0.5348 0.4627 0.3700 0.0291 -0.0107 0.0081 97 GLU B C 3295 O O . GLU B 97 ? 0.5319 0.4575 0.3640 0.0264 -0.0119 0.0094 97 GLU B O 3296 C CB . GLU B 97 ? 0.5453 0.4567 0.3660 0.0231 -0.0162 0.0083 97 GLU B CB 3297 C CG . GLU B 97 ? 0.5756 0.4656 0.3817 0.0250 -0.0208 0.0064 97 GLU B CG 3298 C CD . GLU B 97 ? 0.6172 0.4995 0.4117 0.0151 -0.0243 0.0086 97 GLU B CD 3299 O OE1 . GLU B 97 ? 0.6385 0.5373 0.4374 0.0052 -0.0231 0.0120 97 GLU B OE1 3300 O OE2 . GLU B 97 ? 0.6349 0.4961 0.4139 0.0176 -0.0286 0.0067 97 GLU B OE2 3301 N N . LEU B 98 ? 0.5260 0.4655 0.3678 0.0322 -0.0075 0.0080 98 LEU B N 3302 C CA . LEU B 98 ? 0.5252 0.4751 0.3697 0.0345 -0.0053 0.0088 98 LEU B CA 3303 C C . LEU B 98 ? 0.5328 0.4760 0.3776 0.0374 -0.0042 0.0073 98 LEU B C 3304 O O . LEU B 98 ? 0.5288 0.4758 0.3737 0.0365 -0.0042 0.0083 98 LEU B O 3305 C CB . LEU B 98 ? 0.5200 0.4782 0.3648 0.0409 -0.0032 0.0084 98 LEU B CB 3306 C CG . LEU B 98 ? 0.5359 0.5050 0.3786 0.0469 -0.0020 0.0088 98 LEU B CG 3307 C CD1 . LEU B 98 ? 0.5111 0.5005 0.3561 0.0411 -0.0031 0.0118 98 LEU B CD1 3308 C CD2 . LEU B 98 ? 0.5722 0.5442 0.4087 0.0577 -0.0008 0.0077 98 LEU B CD2 3309 N N . LEU B 99 ? 0.5338 0.4701 0.3781 0.0395 -0.0034 0.0051 99 LEU B N 3310 C CA . LEU B 99 ? 0.5484 0.4817 0.3914 0.0397 -0.0024 0.0039 99 LEU B CA 3311 C C . LEU B 99 ? 0.5425 0.4763 0.3866 0.0387 -0.0038 0.0042 99 LEU B C 3312 O O . LEU B 99 ? 0.5461 0.4811 0.3903 0.0384 -0.0030 0.0043 99 LEU B O 3313 C CB . LEU B 99 ? 0.5543 0.4866 0.3956 0.0385 -0.0021 0.0022 99 LEU B CB 3314 C CG . LEU B 99 ? 0.5802 0.5155 0.4188 0.0353 -0.0014 0.0013 99 LEU B CG 3315 C CD1 . LEU B 99 ? 0.6004 0.5288 0.4330 0.0335 -0.0005 0.0019 99 LEU B CD1 3316 C CD2 . LEU B 99 ? 0.5880 0.5268 0.4227 0.0311 -0.0013 0.0006 99 LEU B CD2 3317 N N . VAL B 100 ? 0.5364 0.4660 0.3781 0.0385 -0.0065 0.0044 100 VAL B N 3318 C CA . VAL B 100 ? 0.5325 0.4560 0.3691 0.0391 -0.0091 0.0046 100 VAL B CA 3319 C C . VAL B 100 ? 0.5276 0.4513 0.3628 0.0336 -0.0100 0.0076 100 VAL B C 3320 O O . VAL B 100 ? 0.5177 0.4404 0.3517 0.0339 -0.0103 0.0079 100 VAL B O 3321 C CB . VAL B 100 ? 0.5470 0.4588 0.3738 0.0425 -0.0130 0.0033 100 VAL B CB 3322 C CG1 . VAL B 100 ? 0.5446 0.4421 0.3586 0.0441 -0.0171 0.0038 100 VAL B CG1 3323 C CG2 . VAL B 100 ? 0.5341 0.4538 0.3631 0.0496 -0.0119 0.0001 100 VAL B CG2 3324 N N . LEU B 101 ? 0.5152 0.4437 0.3502 0.0282 -0.0105 0.0099 101 LEU B N 3325 C CA . LEU B 101 ? 0.5070 0.4444 0.3410 0.0216 -0.0112 0.0131 101 LEU B CA 3326 C C . LEU B 101 ? 0.4874 0.4366 0.3288 0.0263 -0.0078 0.0124 101 LEU B C 3327 O O . LEU B 101 ? 0.4729 0.4253 0.3135 0.0237 -0.0084 0.0139 101 LEU B O 3328 C CB . LEU B 101 ? 0.5129 0.4636 0.3460 0.0148 -0.0119 0.0158 101 LEU B CB 3329 C CG . LEU B 101 ? 0.5338 0.4743 0.3561 0.0060 -0.0160 0.0176 101 LEU B CG 3330 C CD1 . LEU B 101 ? 0.5427 0.5077 0.3666 -0.0016 -0.0157 0.0207 101 LEU B CD1 3331 C CD2 . LEU B 101 ? 0.5455 0.4635 0.3505 -0.0022 -0.0215 0.0195 101 LEU B CD2 3332 N N . MET B 102 ? 0.4689 0.4213 0.3140 0.0330 -0.0049 0.0103 102 MET B N 3333 C CA . MET B 102 ? 0.4742 0.4311 0.3197 0.0385 -0.0026 0.0093 102 MET B CA 3334 C C . MET B 102 ? 0.4689 0.4176 0.3142 0.0383 -0.0021 0.0080 102 MET B C 3335 O O . MET B 102 ? 0.4622 0.4149 0.3075 0.0389 -0.0016 0.0083 102 MET B O 3336 C CB . MET B 102 ? 0.4736 0.4265 0.3149 0.0454 -0.0010 0.0074 102 MET B CB 3337 C CG . MET B 102 ? 0.5111 0.4785 0.3511 0.0504 -0.0009 0.0083 102 MET B CG 3338 S SD . MET B 102 ? 0.6111 0.5647 0.4397 0.0607 -0.0001 0.0057 102 MET B SD 3339 C CE . MET B 102 ? 0.6169 0.5936 0.4408 0.0731 -0.0001 0.0060 102 MET B CE 3340 N N . GLU B 103 ? 0.4663 0.4073 0.3113 0.0375 -0.0024 0.0065 103 GLU B N 3341 C CA . GLU B 103 ? 0.4687 0.4086 0.3135 0.0372 -0.0019 0.0054 103 GLU B CA 3342 C C . GLU B 103 ? 0.4534 0.3935 0.2983 0.0363 -0.0038 0.0066 103 GLU B C 3343 O O . GLU B 103 ? 0.4520 0.3947 0.2975 0.0363 -0.0031 0.0064 103 GLU B O 3344 C CB . GLU B 103 ? 0.4787 0.4184 0.3222 0.0369 -0.0015 0.0034 103 GLU B CB 3345 C CG . GLU B 103 ? 0.5258 0.4605 0.3635 0.0347 0.0000 0.0027 103 GLU B CG 3346 C CD . GLU B 103 ? 0.6031 0.5318 0.4337 0.0336 0.0007 0.0027 103 GLU B CD 3347 O OE1 . GLU B 103 ? 0.6183 0.5518 0.4510 0.0322 0.0010 0.0027 103 GLU B OE1 3348 O OE2 . GLU B 103 ? 0.6228 0.5398 0.4430 0.0355 0.0007 0.0024 103 GLU B OE2 3349 N N . ASN B 104 ? 0.4438 0.3784 0.2850 0.0347 -0.0068 0.0081 104 ASN B N 3350 C CA . ASN B 104 ? 0.4457 0.3739 0.2806 0.0323 -0.0099 0.0099 104 ASN B CA 3351 C C . ASN B 104 ? 0.4396 0.3778 0.2781 0.0281 -0.0088 0.0122 104 ASN B C 3352 O O . ASN B 104 ? 0.4374 0.3753 0.2751 0.0283 -0.0091 0.0125 104 ASN B O 3353 C CB . ASN B 104 ? 0.4556 0.3699 0.2788 0.0282 -0.0144 0.0117 104 ASN B CB 3354 C CG . ASN B 104 ? 0.4811 0.3822 0.2958 0.0359 -0.0168 0.0089 104 ASN B CG 3355 O OD1 . ASN B 104 ? 0.4625 0.3709 0.2818 0.0438 -0.0148 0.0059 104 ASN B OD1 3356 N ND2 . ASN B 104 ? 0.4704 0.3540 0.2707 0.0334 -0.0213 0.0098 104 ASN B ND2 3357 N N . GLU B 105 ? 0.4245 0.3745 0.2664 0.0257 -0.0076 0.0135 105 GLU B N 3358 C CA . GLU B 105 ? 0.4297 0.3952 0.2747 0.0245 -0.0065 0.0151 105 GLU B CA 3359 C C . GLU B 105 ? 0.4212 0.3859 0.2691 0.0305 -0.0039 0.0126 105 GLU B C 3360 O O . GLU B 105 ? 0.4025 0.3713 0.2510 0.0289 -0.0041 0.0136 105 GLU B O 3361 C CB . GLU B 105 ? 0.4346 0.4177 0.2816 0.0263 -0.0054 0.0157 105 GLU B CB 3362 C CG . GLU B 105 ? 0.4583 0.4659 0.3065 0.0253 -0.0052 0.0179 105 GLU B CG 3363 C CD . GLU B 105 ? 0.5026 0.5208 0.3466 0.0106 -0.0088 0.0228 105 GLU B CD 3364 O OE1 . GLU B 105 ? 0.4959 0.5117 0.3350 0.0024 -0.0111 0.0249 105 GLU B OE1 3365 O OE2 . GLU B 105 ? 0.4901 0.5179 0.3334 0.0056 -0.0097 0.0250 105 GLU B OE2 3366 N N . HIS B 106 ? 0.4130 0.3713 0.2605 0.0356 -0.0018 0.0097 106 HIS B N 3367 C CA . HIS B 106 ? 0.4286 0.3833 0.2741 0.0380 -0.0001 0.0077 106 HIS B CA 3368 C C . HIS B 106 ? 0.4266 0.3797 0.2737 0.0353 -0.0004 0.0075 106 HIS B C 3369 O O . HIS B 106 ? 0.4295 0.3851 0.2764 0.0351 0.0004 0.0073 106 HIS B O 3370 C CB . HIS B 106 ? 0.4417 0.3861 0.2804 0.0401 0.0009 0.0054 106 HIS B CB 3371 C CG . HIS B 106 ? 0.4861 0.4295 0.3186 0.0466 0.0010 0.0049 106 HIS B CG 3372 N ND1 . HIS B 106 ? 0.5348 0.4885 0.3655 0.0529 0.0010 0.0052 106 HIS B ND1 3373 C CD2 . HIS B 106 ? 0.5431 0.4783 0.3691 0.0496 0.0009 0.0039 106 HIS B CD2 3374 C CE1 . HIS B 106 ? 0.5694 0.5220 0.3919 0.0615 0.0008 0.0041 106 HIS B CE1 3375 N NE2 . HIS B 106 ? 0.5969 0.5363 0.4162 0.0592 0.0007 0.0035 106 HIS B NE2 3376 N N . THR B 107 ? 0.4216 0.3714 0.2688 0.0349 -0.0018 0.0074 107 THR B N 3377 C CA . THR B 107 ? 0.4285 0.3794 0.2748 0.0362 -0.0027 0.0069 107 THR B CA 3378 C C . THR B 107 ? 0.4253 0.3759 0.2706 0.0349 -0.0042 0.0091 107 THR B C 3379 O O . THR B 107 ? 0.4222 0.3775 0.2685 0.0356 -0.0034 0.0086 107 THR B O 3380 C CB . THR B 107 ? 0.4322 0.3788 0.2742 0.0403 -0.0050 0.0059 107 THR B CB 3381 O OG1 . THR B 107 ? 0.4452 0.3976 0.2889 0.0406 -0.0033 0.0039 107 THR B OG1 3382 C CG2 . THR B 107 ? 0.4433 0.3909 0.2803 0.0459 -0.0069 0.0052 107 THR B CG2 3383 N N . LEU B 108 ? 0.4254 0.3716 0.2674 0.0312 -0.0067 0.0118 108 LEU B N 3384 C CA . LEU B 108 ? 0.4360 0.3812 0.2738 0.0268 -0.0091 0.0147 108 LEU B CA 3385 C C . LEU B 108 ? 0.4256 0.3852 0.2706 0.0259 -0.0063 0.0150 108 LEU B C 3386 O O . LEU B 108 ? 0.4335 0.3946 0.2780 0.0253 -0.0067 0.0158 108 LEU B O 3387 C CB . LEU B 108 ? 0.4434 0.3823 0.2724 0.0184 -0.0131 0.0184 108 LEU B CB 3388 C CG . LEU B 108 ? 0.4572 0.3744 0.2726 0.0196 -0.0173 0.0181 108 LEU B CG 3389 C CD1 . LEU B 108 ? 0.4706 0.3758 0.2704 0.0075 -0.0226 0.0225 108 LEU B CD1 3390 C CD2 . LEU B 108 ? 0.4729 0.3764 0.2791 0.0287 -0.0193 0.0161 108 LEU B CD2 3391 N N . ASP B 109 ? 0.4198 0.3886 0.2693 0.0278 -0.0039 0.0140 109 ASP B N 3392 C CA . ASP B 109 ? 0.4078 0.3868 0.2596 0.0308 -0.0017 0.0130 109 ASP B CA 3393 C C . ASP B 109 ? 0.4026 0.3755 0.2537 0.0334 0.0002 0.0102 109 ASP B C 3394 O O . ASP B 109 ? 0.3856 0.3633 0.2367 0.0342 0.0011 0.0099 109 ASP B O 3395 C CB . ASP B 109 ? 0.4061 0.3931 0.2568 0.0359 -0.0006 0.0121 109 ASP B CB 3396 C CG . ASP B 109 ? 0.4254 0.4295 0.2773 0.0316 -0.0024 0.0155 109 ASP B CG 3397 O OD1 . ASP B 109 ? 0.4670 0.4784 0.3190 0.0234 -0.0044 0.0188 109 ASP B OD1 3398 O OD2 . ASP B 109 ? 0.4322 0.4434 0.2831 0.0350 -0.0021 0.0151 109 ASP B OD2 3399 N N . PHE B 110 ? 0.3975 0.3625 0.2471 0.0335 0.0007 0.0084 110 PHE B N 3400 C CA . PHE B 110 ? 0.4057 0.3696 0.2529 0.0321 0.0022 0.0065 110 PHE B CA 3401 C C . PHE B 110 ? 0.4004 0.3710 0.2508 0.0316 0.0017 0.0074 110 PHE B C 3402 O O . PHE B 110 ? 0.3983 0.3726 0.2479 0.0301 0.0030 0.0067 110 PHE B O 3403 C CB . PHE B 110 ? 0.4026 0.3640 0.2475 0.0307 0.0024 0.0050 110 PHE B CB 3404 C CG . PHE B 110 ? 0.4134 0.3807 0.2548 0.0259 0.0035 0.0037 110 PHE B CG 3405 C CD1 . PHE B 110 ? 0.4245 0.3857 0.2569 0.0206 0.0044 0.0029 110 PHE B CD1 3406 C CD2 . PHE B 110 ? 0.4112 0.3911 0.2550 0.0268 0.0032 0.0032 110 PHE B CD2 3407 C CE1 . PHE B 110 ? 0.4451 0.4140 0.2717 0.0122 0.0050 0.0023 110 PHE B CE1 3408 C CE2 . PHE B 110 ? 0.4278 0.4220 0.2684 0.0210 0.0042 0.0023 110 PHE B CE2 3409 C CZ . PHE B 110 ? 0.4187 0.4079 0.2509 0.0115 0.0052 0.0022 110 PHE B CZ 3410 N N . HIS B 111 ? 0.4079 0.3771 0.2584 0.0334 -0.0005 0.0088 111 HIS B N 3411 C CA . HIS B 111 ? 0.4183 0.3895 0.2673 0.0350 -0.0019 0.0097 111 HIS B CA 3412 C C . HIS B 111 ? 0.4182 0.3927 0.2693 0.0317 -0.0018 0.0118 111 HIS B C 3413 O O . HIS B 111 ? 0.4158 0.3961 0.2680 0.0319 -0.0011 0.0117 111 HIS B O 3414 C CB . HIS B 111 ? 0.4354 0.3949 0.2761 0.0386 -0.0060 0.0109 111 HIS B CB 3415 C CG . HIS B 111 ? 0.4485 0.4087 0.2858 0.0455 -0.0065 0.0083 111 HIS B CG 3416 N ND1 . HIS B 111 ? 0.4852 0.4590 0.3222 0.0514 -0.0056 0.0062 111 HIS B ND1 3417 C CD2 . HIS B 111 ? 0.4731 0.4262 0.3068 0.0478 -0.0079 0.0075 111 HIS B CD2 3418 C CE1 . HIS B 111 ? 0.4757 0.4533 0.3090 0.0578 -0.0064 0.0041 111 HIS B CE1 3419 N NE2 . HIS B 111 ? 0.4770 0.4401 0.3082 0.0559 -0.0078 0.0048 111 HIS B NE2 3420 N N . ASP B 112 ? 0.4092 0.3843 0.2610 0.0288 -0.0025 0.0136 112 ASP B N 3421 C CA . ASP B 112 ? 0.4099 0.3948 0.2635 0.0257 -0.0026 0.0157 112 ASP B CA 3422 C C . ASP B 112 ? 0.4019 0.3935 0.2582 0.0290 0.0004 0.0131 112 ASP B C 3423 O O . ASP B 112 ? 0.3875 0.3856 0.2453 0.0281 0.0006 0.0137 112 ASP B O 3424 C CB . ASP B 112 ? 0.4129 0.4049 0.2660 0.0223 -0.0039 0.0180 112 ASP B CB 3425 C CG . ASP B 112 ? 0.4340 0.4426 0.2877 0.0170 -0.0052 0.0213 112 ASP B CG 3426 O OD1 . ASP B 112 ? 0.4261 0.4364 0.2794 0.0145 -0.0058 0.0226 112 ASP B OD1 3427 O OD2 . ASP B 112 ? 0.4341 0.4578 0.2882 0.0149 -0.0056 0.0228 112 ASP B OD2 3428 N N . SER B 113 ? 0.3948 0.3816 0.2484 0.0322 0.0021 0.0103 113 SER B N 3429 C CA . SER B 113 ? 0.4072 0.3904 0.2551 0.0343 0.0038 0.0075 113 SER B CA 3430 C C . SER B 113 ? 0.3948 0.3786 0.2432 0.0302 0.0047 0.0069 113 SER B C 3431 O O . SER B 113 ? 0.4053 0.3909 0.2511 0.0299 0.0054 0.0061 113 SER B O 3432 C CB . SER B 113 ? 0.4074 0.3769 0.2456 0.0362 0.0042 0.0050 113 SER B CB 3433 O OG . SER B 113 ? 0.4439 0.4018 0.2699 0.0344 0.0047 0.0026 113 SER B OG 3434 N N . ASN B 114 ? 0.4058 0.3905 0.2564 0.0282 0.0045 0.0071 114 ASN B N 3435 C CA . ASN B 114 ? 0.4091 0.4017 0.2597 0.0255 0.0053 0.0064 114 ASN B CA 3436 C C . ASN B 114 ? 0.4097 0.4098 0.2646 0.0270 0.0049 0.0080 114 ASN B C 3437 O O . ASN B 114 ? 0.4193 0.4267 0.2737 0.0246 0.0061 0.0073 114 ASN B O 3438 C CB . ASN B 114 ? 0.4068 0.4050 0.2580 0.0268 0.0048 0.0060 114 ASN B CB 3439 C CG . ASN B 114 ? 0.4070 0.4017 0.2532 0.0226 0.0055 0.0044 114 ASN B CG 3440 O OD1 . ASN B 114 ? 0.4059 0.3912 0.2441 0.0172 0.0062 0.0035 114 ASN B OD1 3441 N ND2 . ASN B 114 ? 0.4084 0.4076 0.2558 0.0255 0.0047 0.0041 114 ASN B ND2 3442 N N . VAL B 115 ? 0.4153 0.4129 0.2723 0.0292 0.0026 0.0105 115 VAL B N 3443 C CA . VAL B 115 ? 0.4032 0.4046 0.2611 0.0291 0.0013 0.0128 115 VAL B CA 3444 C C . VAL B 115 ? 0.4053 0.4136 0.2659 0.0270 0.0028 0.0129 115 VAL B C 3445 O O . VAL B 115 ? 0.4048 0.4197 0.2666 0.0264 0.0036 0.0128 115 VAL B O 3446 C CB . VAL B 115 ? 0.4130 0.4053 0.2660 0.0281 -0.0026 0.0163 115 VAL B CB 3447 C CG1 . VAL B 115 ? 0.3953 0.3896 0.2459 0.0250 -0.0046 0.0195 115 VAL B CG1 3448 C CG2 . VAL B 115 ? 0.4167 0.3977 0.2618 0.0333 -0.0051 0.0158 115 VAL B CG2 3449 N N . LYS B 116 ? 0.4116 0.4202 0.2719 0.0276 0.0029 0.0128 116 LYS B N 3450 C CA . LYS B 116 ? 0.4190 0.4356 0.2788 0.0297 0.0039 0.0119 116 LYS B CA 3451 C C . LYS B 116 ? 0.4177 0.4283 0.2718 0.0304 0.0059 0.0084 116 LYS B C 3452 O O . LYS B 116 ? 0.4135 0.4299 0.2673 0.0307 0.0064 0.0080 116 LYS B O 3453 C CB . LYS B 116 ? 0.4194 0.4395 0.2766 0.0343 0.0036 0.0113 116 LYS B CB 3454 C CG . LYS B 116 ? 0.4658 0.4936 0.3179 0.0415 0.0042 0.0091 116 LYS B CG 3455 C CD . LYS B 116 ? 0.5414 0.5766 0.3881 0.0504 0.0036 0.0079 116 LYS B CD 3456 C CE . LYS B 116 ? 0.5627 0.6111 0.4030 0.0608 0.0035 0.0057 116 LYS B CE 3457 N NZ . LYS B 116 ? 0.5921 0.6641 0.4429 0.0547 0.0033 0.0092 116 LYS B NZ 3458 N N . ASN B 117 ? 0.4243 0.4232 0.2720 0.0288 0.0065 0.0063 117 ASN B N 3459 C CA . ASN B 117 ? 0.4423 0.4329 0.2793 0.0248 0.0074 0.0037 117 ASN B CA 3460 C C . ASN B 117 ? 0.4322 0.4345 0.2738 0.0196 0.0085 0.0044 117 ASN B C 3461 O O . ASN B 117 ? 0.4418 0.4420 0.2763 0.0169 0.0089 0.0030 117 ASN B O 3462 C CB . ASN B 117 ? 0.4498 0.4273 0.2767 0.0203 0.0073 0.0022 117 ASN B CB 3463 C CG . ASN B 117 ? 0.4779 0.4374 0.2919 0.0262 0.0060 0.0005 117 ASN B CG 3464 O OD1 . ASN B 117 ? 0.4860 0.4453 0.2972 0.0351 0.0054 -0.0002 117 ASN B OD1 3465 N ND2 . ASN B 117 ? 0.4952 0.4419 0.3001 0.0223 0.0054 -0.0001 117 ASN B ND2 3466 N N . LEU B 118 ? 0.4292 0.4426 0.2800 0.0198 0.0083 0.0062 118 LEU B N 3467 C CA . LEU B 118 ? 0.4248 0.4526 0.2797 0.0183 0.0090 0.0069 118 LEU B CA 3468 C C . LEU B 118 ? 0.4203 0.4525 0.2794 0.0203 0.0087 0.0083 118 LEU B C 3469 O O . LEU B 118 ? 0.4198 0.4593 0.2781 0.0174 0.0099 0.0077 118 LEU B O 3470 C CB . LEU B 118 ? 0.4256 0.4608 0.2842 0.0230 0.0078 0.0080 118 LEU B CB 3471 C CG . LEU B 118 ? 0.4494 0.5006 0.3096 0.0261 0.0078 0.0085 118 LEU B CG 3472 C CD1 . LEU B 118 ? 0.4699 0.5382 0.3277 0.0189 0.0102 0.0067 118 LEU B CD1 3473 C CD2 . LEU B 118 ? 0.4643 0.5162 0.3222 0.0357 0.0053 0.0091 118 LEU B CD2 3474 N N . TYR B 119 ? 0.4125 0.4422 0.2751 0.0236 0.0071 0.0105 119 TYR B N 3475 C CA . TYR B 119 ? 0.4129 0.4497 0.2787 0.0239 0.0066 0.0122 119 TYR B CA 3476 C C . TYR B 119 ? 0.4225 0.4600 0.2840 0.0245 0.0081 0.0095 119 TYR B C 3477 O O . TYR B 119 ? 0.4090 0.4543 0.2720 0.0236 0.0087 0.0096 119 TYR B O 3478 C CB . TYR B 119 ? 0.4046 0.4423 0.2720 0.0240 0.0043 0.0152 119 TYR B CB 3479 C CG . TYR B 119 ? 0.4111 0.4616 0.2811 0.0221 0.0033 0.0178 119 TYR B CG 3480 C CD1 . TYR B 119 ? 0.4353 0.4872 0.3050 0.0182 0.0011 0.0214 119 TYR B CD1 3481 C CD2 . TYR B 119 ? 0.4200 0.4815 0.2901 0.0253 0.0041 0.0164 119 TYR B CD2 3482 C CE1 . TYR B 119 ? 0.4175 0.4831 0.2888 0.0142 0.0000 0.0243 119 TYR B CE1 3483 C CE2 . TYR B 119 ? 0.4389 0.5185 0.3118 0.0236 0.0033 0.0188 119 TYR B CE2 3484 C CZ . TYR B 119 ? 0.4181 0.5002 0.2925 0.0164 0.0013 0.0230 119 TYR B CZ 3485 O OH . TYR B 119 ? 0.4407 0.5422 0.3172 0.0128 0.0003 0.0257 119 TYR B OH 3486 N N . ASP B 120 ? 0.4351 0.4617 0.2883 0.0271 0.0082 0.0069 120 ASP B N 3487 C CA . ASP B 120 ? 0.4686 0.4879 0.3099 0.0307 0.0084 0.0037 120 ASP B CA 3488 C C . ASP B 120 ? 0.4859 0.4975 0.3183 0.0236 0.0093 0.0018 120 ASP B C 3489 O O . ASP B 120 ? 0.5010 0.5121 0.3271 0.0244 0.0094 0.0003 120 ASP B O 3490 C CB . ASP B 120 ? 0.4827 0.4865 0.3110 0.0371 0.0073 0.0011 120 ASP B CB 3491 C CG . ASP B 120 ? 0.5058 0.5236 0.3393 0.0459 0.0064 0.0022 120 ASP B CG 3492 O OD1 . ASP B 120 ? 0.5483 0.5864 0.3903 0.0471 0.0063 0.0041 120 ASP B OD1 3493 O OD2 . ASP B 120 ? 0.5139 0.5253 0.3423 0.0508 0.0057 0.0014 120 ASP B OD2 3494 N N . LYS B 121 ? 0.4943 0.5034 0.3255 0.0160 0.0099 0.0020 121 LYS B N 3495 C CA . LYS B 121 ? 0.5222 0.5321 0.3454 0.0058 0.0107 0.0010 121 LYS B CA 3496 C C . LYS B 121 ? 0.5151 0.5439 0.3486 0.0053 0.0118 0.0023 121 LYS B C 3497 O O . LYS B 121 ? 0.5330 0.5594 0.3573 0.0003 0.0121 0.0009 121 LYS B O 3498 C CB . LYS B 121 ? 0.5172 0.5342 0.3416 -0.0014 0.0111 0.0018 121 LYS B CB 3499 C CG . LYS B 121 ? 0.5772 0.5923 0.3854 -0.0161 0.0112 0.0007 121 LYS B CG 3500 C CD . LYS B 121 ? 0.6100 0.6433 0.4212 -0.0234 0.0118 0.0018 121 LYS B CD 3501 C CE . LYS B 121 ? 0.6610 0.6969 0.4531 -0.0428 0.0113 0.0015 121 LYS B CE 3502 N NZ . LYS B 121 ? 0.6861 0.7254 0.4715 -0.0498 0.0116 0.0012 121 LYS B NZ 3503 N N . VAL B 122 ? 0.5025 0.5467 0.3518 0.0103 0.0120 0.0051 122 VAL B N 3504 C CA . VAL B 122 ? 0.4938 0.5538 0.3512 0.0110 0.0126 0.0067 122 VAL B CA 3505 C C . VAL B 122 ? 0.4921 0.5509 0.3489 0.0138 0.0124 0.0064 122 VAL B C 3506 O O . VAL B 122 ? 0.4873 0.5516 0.3418 0.0108 0.0133 0.0055 122 VAL B O 3507 C CB . VAL B 122 ? 0.4910 0.5592 0.3578 0.0164 0.0113 0.0098 122 VAL B CB 3508 C CG1 . VAL B 122 ? 0.4769 0.5557 0.3487 0.0184 0.0109 0.0120 122 VAL B CG1 3509 C CG2 . VAL B 122 ? 0.4828 0.5585 0.3484 0.0165 0.0116 0.0093 122 VAL B CG2 3510 N N . ARG B 123 ? 0.4906 0.5455 0.3489 0.0197 0.0111 0.0070 123 ARG B N 3511 C CA . ARG B 123 ? 0.4967 0.5565 0.3537 0.0247 0.0106 0.0063 123 ARG B CA 3512 C C . ARG B 123 ? 0.5238 0.5709 0.3648 0.0255 0.0109 0.0020 123 ARG B C 3513 O O . ARG B 123 ? 0.5186 0.5729 0.3590 0.0263 0.0112 0.0014 123 ARG B O 3514 C CB . ARG B 123 ? 0.4930 0.5551 0.3510 0.0311 0.0092 0.0071 123 ARG B CB 3515 C CG . ARG B 123 ? 0.4951 0.5695 0.3504 0.0389 0.0085 0.0060 123 ARG B CG 3516 C CD . ARG B 123 ? 0.5062 0.5917 0.3624 0.0451 0.0071 0.0069 123 ARG B CD 3517 N NE . ARG B 123 ? 0.5397 0.6066 0.3846 0.0511 0.0068 0.0037 123 ARG B NE 3518 C CZ . ARG B 123 ? 0.5811 0.6343 0.4077 0.0625 0.0060 -0.0011 123 ARG B CZ 3519 N NH1 . ARG B 123 ? 0.5695 0.6256 0.3869 0.0702 0.0055 -0.0039 123 ARG B NH1 3520 N NH2 . ARG B 123 ? 0.5673 0.6009 0.3818 0.0671 0.0051 -0.0033 123 ARG B NH2 3521 N N . MET B 124 ? 0.5525 0.5778 0.3774 0.0250 0.0102 -0.0007 124 MET B N 3522 C CA . MET B 124 ? 0.6020 0.6042 0.4022 0.0257 0.0088 -0.0050 124 MET B CA 3523 C C . MET B 124 ? 0.6136 0.6149 0.4077 0.0132 0.0096 -0.0052 124 MET B C 3524 O O . MET B 124 ? 0.6449 0.6281 0.4176 0.0122 0.0080 -0.0083 124 MET B O 3525 C CB . MET B 124 ? 0.6252 0.5991 0.4046 0.0270 0.0067 -0.0074 124 MET B CB 3526 C CG . MET B 124 ? 0.6627 0.6364 0.4413 0.0427 0.0054 -0.0084 124 MET B CG 3527 S SD . MET B 124 ? 0.7712 0.7092 0.5226 0.0471 0.0025 -0.0113 124 MET B SD 3528 C CE . MET B 124 ? 0.7755 0.6739 0.4845 0.0523 -0.0014 -0.0167 124 MET B CE 3529 N N . GLN B 125 ? 0.6059 0.6275 0.4167 0.0048 0.0116 -0.0022 125 GLN B N 3530 C CA . GLN B 125 ? 0.6075 0.6399 0.4170 -0.0063 0.0129 -0.0018 125 GLN B CA 3531 C C . GLN B 125 ? 0.5846 0.6377 0.4086 -0.0022 0.0142 -0.0005 125 GLN B C 3532 O O . GLN B 125 ? 0.5948 0.6474 0.4101 -0.0074 0.0143 -0.0018 125 GLN B O 3533 C CB . GLN B 125 ? 0.6065 0.6547 0.4233 -0.0151 0.0142 0.0001 125 GLN B CB 3534 C CG . GLN B 125 ? 0.6543 0.7189 0.4665 -0.0284 0.0154 0.0003 125 GLN B CG 3535 C CD . GLN B 125 ? 0.6730 0.7537 0.4837 -0.0390 0.0160 0.0014 125 GLN B CD 3536 O OE1 . GLN B 125 ? 0.6540 0.7611 0.4812 -0.0332 0.0173 0.0032 125 GLN B OE1 3537 N NE2 . GLN B 125 ? 0.7015 0.7662 0.4887 -0.0548 0.0144 0.0003 125 GLN B NE2 3538 N N . LEU B 126 ? 0.5491 0.6181 0.3922 0.0054 0.0145 0.0024 126 LEU B N 3539 C CA . LEU B 126 ? 0.5254 0.6123 0.3804 0.0083 0.0151 0.0045 126 LEU B CA 3540 C C . LEU B 126 ? 0.5339 0.6180 0.3834 0.0144 0.0143 0.0026 126 LEU B C 3541 O O . LEU B 126 ? 0.5217 0.6186 0.3760 0.0142 0.0148 0.0032 126 LEU B O 3542 C CB . LEU B 126 ? 0.5025 0.6006 0.3722 0.0126 0.0143 0.0087 126 LEU B CB 3543 C CG . LEU B 126 ? 0.4899 0.5913 0.3630 0.0114 0.0143 0.0103 126 LEU B CG 3544 C CD1 . LEU B 126 ? 0.4608 0.5627 0.3401 0.0161 0.0120 0.0143 126 LEU B CD1 3545 C CD2 . LEU B 126 ? 0.4675 0.5841 0.3408 0.0073 0.0160 0.0100 126 LEU B CD2 3546 N N . ARG B 127 ? 0.5548 0.6241 0.3935 0.0214 0.0128 0.0001 127 ARG B N 3547 C CA . ARG B 127 ? 0.5768 0.6458 0.4070 0.0320 0.0114 -0.0025 127 ARG B CA 3548 C C . ARG B 127 ? 0.5610 0.6589 0.4086 0.0345 0.0118 0.0007 127 ARG B C 3549 O O . ARG B 127 ? 0.5427 0.6552 0.4056 0.0315 0.0118 0.0054 127 ARG B O 3550 C CB . ARG B 127 ? 0.6047 0.6510 0.4103 0.0312 0.0104 -0.0073 127 ARG B CB 3551 C CG . ARG B 127 ? 0.6408 0.6530 0.4217 0.0281 0.0086 -0.0103 127 ARG B CG 3552 C CD . ARG B 127 ? 0.6909 0.6761 0.4429 0.0196 0.0068 -0.0137 127 ARG B CD 3553 N NE . ARG B 127 ? 0.7476 0.7254 0.4844 0.0314 0.0049 -0.0174 127 ARG B NE 3554 C CZ . ARG B 127 ? 0.7973 0.7439 0.5011 0.0278 0.0020 -0.0213 127 ARG B CZ 3555 N NH1 . ARG B 127 ? 0.7973 0.7179 0.4791 0.0094 0.0005 -0.0214 127 ARG B NH1 3556 N NH2 . ARG B 127 ? 0.8372 0.7789 0.5275 0.0418 0.0000 -0.0250 127 ARG B NH2 3557 N N . ASP B 128 ? 0.5706 0.6748 0.4131 0.0387 0.0117 -0.0012 128 ASP B N 3558 C CA . ASP B 128 ? 0.5535 0.6871 0.4112 0.0397 0.0118 0.0021 128 ASP B CA 3559 C C . ASP B 128 ? 0.5402 0.6841 0.4102 0.0293 0.0132 0.0057 128 ASP B C 3560 O O . ASP B 128 ? 0.5463 0.7105 0.4247 0.0289 0.0131 0.0081 128 ASP B O 3561 C CB . ASP B 128 ? 0.5681 0.7104 0.4156 0.0521 0.0106 -0.0017 128 ASP B CB 3562 C CG . ASP B 128 ? 0.5866 0.7103 0.4175 0.0523 0.0108 -0.0063 128 ASP B CG 3563 O OD1 . ASP B 128 ? 0.6053 0.7082 0.4297 0.0419 0.0116 -0.0069 128 ASP B OD1 3564 O OD2 . ASP B 128 ? 0.6178 0.7495 0.4407 0.0622 0.0098 -0.0093 128 ASP B OD2 3565 N N . ASN B 129 ? 0.5339 0.6666 0.4038 0.0218 0.0144 0.0061 129 ASN B N 3566 C CA . ASN B 129 ? 0.5147 0.6597 0.3950 0.0155 0.0154 0.0096 129 ASN B CA 3567 C C . ASN B 129 ? 0.4965 0.6481 0.3867 0.0146 0.0137 0.0151 129 ASN B C 3568 O O . ASN B 129 ? 0.4927 0.6507 0.3876 0.0122 0.0135 0.0183 129 ASN B O 3569 C CB . ASN B 129 ? 0.5298 0.6681 0.4049 0.0089 0.0171 0.0080 129 ASN B CB 3570 C CG . ASN B 129 ? 0.5586 0.6911 0.4208 0.0046 0.0180 0.0039 129 ASN B CG 3571 O OD1 . ASN B 129 ? 0.5751 0.7065 0.4320 0.0091 0.0174 0.0019 129 ASN B OD1 3572 N ND2 . ASN B 129 ? 0.5870 0.7168 0.4416 -0.0047 0.0191 0.0028 129 ASN B ND2 3573 N N . VAL B 130 ? 0.4850 0.6329 0.3748 0.0169 0.0121 0.0161 130 VAL B N 3574 C CA . VAL B 130 ? 0.4669 0.6151 0.3601 0.0138 0.0094 0.0214 130 VAL B CA 3575 C C . VAL B 130 ? 0.4640 0.6244 0.3582 0.0135 0.0074 0.0236 130 VAL B C 3576 O O . VAL B 130 ? 0.4605 0.6277 0.3526 0.0197 0.0083 0.0200 130 VAL B O 3577 C CB . VAL B 130 ? 0.4674 0.5985 0.3573 0.0143 0.0091 0.0210 130 VAL B CB 3578 C CG1 . VAL B 130 ? 0.4565 0.5845 0.3454 0.0146 0.0108 0.0195 130 VAL B CG1 3579 C CG2 . VAL B 130 ? 0.4579 0.5808 0.3438 0.0177 0.0099 0.0173 130 VAL B CG2 3580 N N . LYS B 131 ? 0.4741 0.6373 0.3679 0.0061 0.0041 0.0295 131 LYS B N 3581 C CA . LYS B 131 ? 0.4892 0.6665 0.3821 0.0014 0.0015 0.0330 131 LYS B CA 3582 C C . LYS B 131 ? 0.4841 0.6438 0.3727 0.0010 0.0004 0.0331 131 LYS B C 3583 O O . LYS B 131 ? 0.4864 0.6245 0.3701 -0.0006 -0.0008 0.0344 131 LYS B O 3584 C CB . LYS B 131 ? 0.5020 0.6858 0.3907 -0.0113 -0.0027 0.0404 131 LYS B CB 3585 C CG . LYS B 131 ? 0.5326 0.7489 0.4253 -0.0155 -0.0032 0.0426 131 LYS B CG 3586 C CD . LYS B 131 ? 0.5890 0.8048 0.4728 -0.0316 -0.0082 0.0508 131 LYS B CD 3587 C CE . LYS B 131 ? 0.6246 0.8339 0.5087 -0.0304 -0.0078 0.0513 131 LYS B CE 3588 N NZ . LYS B 131 ? 0.6393 0.8824 0.5313 -0.0317 -0.0066 0.0516 131 LYS B NZ 3589 N N . GLU B 132 ? 0.4876 0.6578 0.3767 0.0043 0.0007 0.0315 132 GLU B N 3590 C CA . GLU B 132 ? 0.4936 0.6511 0.3789 0.0027 -0.0005 0.0322 132 GLU B CA 3591 C C . GLU B 132 ? 0.4991 0.6657 0.3790 -0.0114 -0.0052 0.0395 132 GLU B C 3592 O O . GLU B 132 ? 0.4971 0.6934 0.3786 -0.0149 -0.0061 0.0413 132 GLU B O 3593 C CB . GLU B 132 ? 0.4982 0.6653 0.3842 0.0131 0.0013 0.0275 132 GLU B CB 3594 C CG . GLU B 132 ? 0.5147 0.6570 0.3975 0.0207 0.0034 0.0226 132 GLU B CG 3595 C CD . GLU B 132 ? 0.5469 0.6951 0.4262 0.0286 0.0035 0.0200 132 GLU B CD 3596 O OE1 . GLU B 132 ? 0.5232 0.6591 0.4010 0.0268 0.0029 0.0206 132 GLU B OE1 3597 O OE2 . GLU B 132 ? 0.5771 0.7428 0.4536 0.0384 0.0039 0.0171 132 GLU B OE2 3598 N N . LEU B 133 ? 0.5108 0.6522 0.3808 -0.0197 -0.0087 0.0436 133 LEU B N 3599 C CA . LEU B 133 ? 0.5314 0.6736 0.3887 -0.0370 -0.0146 0.0512 133 LEU B CA 3600 C C . LEU B 133 ? 0.5334 0.6837 0.3868 -0.0441 -0.0165 0.0532 133 LEU B C 3601 O O . LEU B 133 ? 0.5503 0.7156 0.3946 -0.0611 -0.0209 0.0596 133 LEU B O 3602 C CB . LEU B 133 ? 0.5507 0.6568 0.3904 -0.0427 -0.0194 0.0550 133 LEU B CB 3603 C CG . LEU B 133 ? 0.5642 0.6671 0.4050 -0.0381 -0.0186 0.0546 133 LEU B CG 3604 C CD1 . LEU B 133 ? 0.6051 0.6689 0.4241 -0.0385 -0.0238 0.0574 133 LEU B CD1 3605 C CD2 . LEU B 133 ? 0.5775 0.7093 0.4210 -0.0488 -0.0196 0.0587 133 LEU B CD2 3606 N N . GLY B 134 ? 0.5269 0.6694 0.3860 -0.0330 -0.0135 0.0482 134 GLY B N 3607 C CA . GLY B 134 ? 0.5207 0.6745 0.3780 -0.0375 -0.0146 0.0494 134 GLY B CA 3608 C C . GLY B 134 ? 0.5396 0.6602 0.3837 -0.0439 -0.0182 0.0515 134 GLY B C 3609 O O . GLY B 134 ? 0.5498 0.6777 0.3919 -0.0482 -0.0191 0.0525 134 GLY B O 3610 N N . ASN B 135 ? 0.5488 0.6342 0.3823 -0.0429 -0.0204 0.0520 135 ASN B N 3611 C CA . ASN B 135 ? 0.5639 0.6123 0.3790 -0.0467 -0.0251 0.0538 135 ASN B CA 3612 C C . ASN B 135 ? 0.5493 0.5765 0.3691 -0.0290 -0.0218 0.0476 135 ASN B C 3613 O O . ASN B 135 ? 0.5596 0.5551 0.3630 -0.0266 -0.0256 0.0480 135 ASN B O 3614 C CB . ASN B 135 ? 0.5934 0.6158 0.3834 -0.0593 -0.0323 0.0601 135 ASN B CB 3615 C CG . ASN B 135 ? 0.6093 0.6266 0.4021 -0.0497 -0.0308 0.0584 135 ASN B CG 3616 O OD1 . ASN B 135 ? 0.5835 0.6234 0.3981 -0.0380 -0.0244 0.0534 135 ASN B OD1 3617 N ND2 . ASN B 135 ? 0.6701 0.6553 0.4372 -0.0547 -0.0374 0.0625 135 ASN B ND2 3618 N N . GLY B 136 ? 0.5231 0.5681 0.3619 -0.0168 -0.0155 0.0420 136 GLY B N 3619 C CA . GLY B 136 ? 0.5139 0.5461 0.3571 -0.0034 -0.0124 0.0367 136 GLY B CA 3620 C C . GLY B 136 ? 0.5156 0.5477 0.3602 0.0024 -0.0111 0.0354 136 GLY B C 3621 O O . GLY B 136 ? 0.5064 0.5366 0.3552 0.0119 -0.0082 0.0312 136 GLY B O 3622 N N . CYS B 137 ? 0.5271 0.5640 0.3675 -0.0043 -0.0134 0.0393 137 CYS B N 3623 C CA . CYS B 137 ? 0.5347 0.5724 0.3754 0.0009 -0.0126 0.0386 137 CYS B CA 3624 C C . CYS B 137 ? 0.5062 0.5703 0.3619 0.0005 -0.0083 0.0370 137 CYS B C 3625 O O . CYS B 137 ? 0.5027 0.5846 0.3637 -0.0054 -0.0080 0.0383 137 CYS B O 3626 C CB . CYS B 137 ? 0.5685 0.5864 0.3886 -0.0052 -0.0192 0.0443 137 CYS B CB 3627 S SG . CYS B 137 ? 0.6627 0.6389 0.4545 -0.0024 -0.0262 0.0461 137 CYS B SG 3628 N N . PHE B 138 ? 0.4975 0.5659 0.3581 0.0076 -0.0055 0.0340 138 PHE B N 3629 C CA . PHE B 138 ? 0.4848 0.5735 0.3559 0.0077 -0.0020 0.0323 138 PHE B CA 3630 C C . PHE B 138 ? 0.4952 0.5839 0.3619 0.0071 -0.0037 0.0350 138 PHE B C 3631 O O . PHE B 138 ? 0.4984 0.5752 0.3575 0.0133 -0.0050 0.0348 138 PHE B O 3632 C CB . PHE B 138 ? 0.4675 0.5611 0.3457 0.0140 0.0027 0.0263 138 PHE B CB 3633 C CG . PHE B 138 ? 0.4477 0.5364 0.3267 0.0156 0.0041 0.0234 138 PHE B CG 3634 C CD1 . PHE B 138 ? 0.4424 0.5398 0.3239 0.0163 0.0054 0.0215 138 PHE B CD1 3635 C CD2 . PHE B 138 ? 0.4565 0.5326 0.3319 0.0183 0.0038 0.0223 138 PHE B CD2 3636 C CE1 . PHE B 138 ? 0.4177 0.5082 0.2968 0.0194 0.0061 0.0188 138 PHE B CE1 3637 C CE2 . PHE B 138 ? 0.4062 0.4771 0.2816 0.0192 0.0049 0.0198 138 PHE B CE2 3638 C CZ . PHE B 138 ? 0.4085 0.4851 0.2851 0.0198 0.0060 0.0181 138 PHE B CZ 3639 N N . GLU B 139 ? 0.5112 0.6152 0.3815 0.0013 -0.0039 0.0373 139 GLU B N 3640 C CA . GLU B 139 ? 0.5267 0.6314 0.3928 0.0004 -0.0055 0.0400 139 GLU B CA 3641 C C . GLU B 139 ? 0.5181 0.6420 0.3967 0.0049 -0.0004 0.0358 139 GLU B C 3642 O O . GLU B 139 ? 0.5110 0.6512 0.3979 0.0036 0.0019 0.0338 139 GLU B O 3643 C CB . GLU B 139 ? 0.5397 0.6481 0.3984 -0.0119 -0.0100 0.0464 139 GLU B CB 3644 C CG . GLU B 139 ? 0.5877 0.6893 0.4359 -0.0147 -0.0134 0.0505 139 GLU B CG 3645 C CD . GLU B 139 ? 0.6418 0.7549 0.4846 -0.0302 -0.0173 0.0569 139 GLU B CD 3646 O OE1 . GLU B 139 ? 0.6755 0.7794 0.5052 -0.0422 -0.0221 0.0616 139 GLU B OE1 3647 O OE2 . GLU B 139 ? 0.6834 0.8171 0.5343 -0.0318 -0.0156 0.0573 139 GLU B OE2 3648 N N . PHE B 140 ? 0.5296 0.6521 0.4071 0.0109 0.0007 0.0342 140 PHE B N 3649 C CA . PHE B 140 ? 0.5242 0.6637 0.4109 0.0132 0.0053 0.0302 140 PHE B CA 3650 C C . PHE B 140 ? 0.5269 0.6809 0.4176 0.0093 0.0054 0.0321 140 PHE B C 3651 O O . PHE B 140 ? 0.5252 0.6756 0.4097 0.0065 0.0017 0.0371 140 PHE B O 3652 C CB . PHE B 140 ? 0.5302 0.6709 0.4139 0.0200 0.0064 0.0285 140 PHE B CB 3653 C CG . PHE B 140 ? 0.5268 0.6637 0.4097 0.0231 0.0080 0.0250 140 PHE B CG 3654 C CD1 . PHE B 140 ? 0.5082 0.6560 0.3956 0.0200 0.0120 0.0207 140 PHE B CD1 3655 C CD2 . PHE B 140 ? 0.5618 0.6824 0.4363 0.0278 0.0049 0.0263 140 PHE B CD2 3656 C CE1 . PHE B 140 ? 0.5292 0.6746 0.4141 0.0204 0.0131 0.0181 140 PHE B CE1 3657 C CE2 . PHE B 140 ? 0.5587 0.6786 0.4331 0.0306 0.0063 0.0232 140 PHE B CE2 3658 C CZ . PHE B 140 ? 0.5445 0.6783 0.4248 0.0263 0.0106 0.0193 140 PHE B CZ 3659 N N . TYR B 141 ? 0.5332 0.7009 0.4311 0.0091 0.0089 0.0283 141 TYR B N 3660 C CA . TYR B 141 ? 0.5429 0.7268 0.4451 0.0069 0.0096 0.0291 141 TYR B CA 3661 C C . TYR B 141 ? 0.5494 0.7400 0.4528 0.0087 0.0117 0.0279 141 TYR B C 3662 O O . TYR B 141 ? 0.5435 0.7468 0.4501 0.0071 0.0122 0.0288 141 TYR B O 3663 C CB . TYR B 141 ? 0.5341 0.7278 0.4391 0.0080 0.0115 0.0251 141 TYR B CB 3664 C CG . TYR B 141 ? 0.5407 0.7417 0.4460 0.0072 0.0093 0.0271 141 TYR B CG 3665 C CD1 . TYR B 141 ? 0.5423 0.7573 0.4489 0.0007 0.0063 0.0329 141 TYR B CD1 3666 C CD2 . TYR B 141 ? 0.5391 0.7354 0.4415 0.0121 0.0099 0.0235 141 TYR B CD2 3667 C CE1 . TYR B 141 ? 0.5525 0.7821 0.4589 -0.0022 0.0041 0.0352 141 TYR B CE1 3668 C CE2 . TYR B 141 ? 0.5428 0.7525 0.4454 0.0123 0.0079 0.0252 141 TYR B CE2 3669 C CZ . TYR B 141 ? 0.5551 0.7843 0.4605 0.0045 0.0052 0.0312 141 TYR B CZ 3670 O OH . TYR B 141 ? 0.5285 0.7787 0.4338 0.0025 0.0032 0.0334 141 TYR B OH 3671 N N . HIS B 142 ? 0.5685 0.7543 0.4691 0.0119 0.0129 0.0258 142 HIS B N 3672 C CA . HIS B 142 ? 0.5819 0.7803 0.4827 0.0141 0.0148 0.0249 142 HIS B CA 3673 C C . HIS B 142 ? 0.6015 0.7943 0.4953 0.0220 0.0126 0.0267 142 HIS B C 3674 O O . HIS B 142 ? 0.6065 0.7853 0.4960 0.0242 0.0110 0.0266 142 HIS B O 3675 C CB . HIS B 142 ? 0.5815 0.7874 0.4825 0.0095 0.0186 0.0199 142 HIS B CB 3676 C CG . HIS B 142 ? 0.5793 0.7754 0.4760 0.0091 0.0189 0.0177 142 HIS B CG 3677 N ND1 . HIS B 142 ? 0.5628 0.7668 0.4571 0.0124 0.0192 0.0175 142 HIS B ND1 3678 C CD2 . HIS B 142 ? 0.5780 0.7588 0.4715 0.0068 0.0187 0.0156 142 HIS B CD2 3679 C CE1 . HIS B 142 ? 0.5555 0.7497 0.4463 0.0102 0.0193 0.0156 142 HIS B CE1 3680 N NE2 . HIS B 142 ? 0.5575 0.7356 0.4473 0.0066 0.0190 0.0145 142 HIS B NE2 3681 N N . LYS B 143 ? 0.6183 0.8218 0.5089 0.0282 0.0121 0.0279 143 LYS B N 3682 C CA . LYS B 143 ? 0.6368 0.8357 0.5164 0.0405 0.0095 0.0287 143 LYS B CA 3683 C C . LYS B 143 ? 0.6330 0.8428 0.5143 0.0420 0.0121 0.0247 143 LYS B C 3684 O O . LYS B 143 ? 0.6259 0.8572 0.5142 0.0347 0.0163 0.0217 143 LYS B O 3685 C CB . LYS B 143 ? 0.6499 0.8621 0.5238 0.0499 0.0086 0.0300 143 LYS B CB 3686 C CG . LYS B 143 ? 0.6730 0.8648 0.5368 0.0506 0.0036 0.0351 143 LYS B CG 3687 C CD . LYS B 143 ? 0.7226 0.9079 0.5675 0.0673 -0.0006 0.0367 143 LYS B CD 3688 C CE . LYS B 143 ? 0.7467 0.9115 0.5788 0.0647 -0.0057 0.0423 143 LYS B CE 3689 N NZ . LYS B 143 ? 0.7659 0.8944 0.5840 0.0563 -0.0115 0.0466 143 LYS B NZ 3690 N N . CYS B 144 ? 0.6463 0.8401 0.5190 0.0495 0.0092 0.0250 144 CYS B N 3691 C CA . CYS B 144 ? 0.6383 0.8424 0.5123 0.0502 0.0114 0.0216 144 CYS B CA 3692 C C . CYS B 144 ? 0.6553 0.8641 0.5166 0.0681 0.0085 0.0212 144 CYS B C 3693 O O . CYS B 144 ? 0.6702 0.8524 0.5190 0.0771 0.0040 0.0225 144 CYS B O 3694 C CB . CYS B 144 ? 0.6388 0.8210 0.5150 0.0424 0.0110 0.0212 144 CYS B CB 3695 S SG . CYS B 144 ? 0.6319 0.8236 0.5087 0.0403 0.0134 0.0174 144 CYS B SG 3696 N N . ASP B 145 ? 0.6511 0.8952 0.5134 0.0739 0.0109 0.0193 145 ASP B N 3697 C CA . ASP B 145 ? 0.6667 0.9241 0.5156 0.0952 0.0083 0.0182 145 ASP B CA 3698 C C . ASP B 145 ? 0.6658 0.9325 0.5136 0.0981 0.0089 0.0156 145 ASP B C 3699 O O . ASP B 145 ? 0.6588 0.9186 0.5158 0.0822 0.0112 0.0149 145 ASP B O 3700 C CB . ASP B 145 ? 0.6598 0.9601 0.5105 0.1013 0.0108 0.0172 145 ASP B CB 3701 C CG . ASP B 145 ? 0.6400 0.9829 0.5041 0.0845 0.0167 0.0148 145 ASP B CG 3702 O OD1 . ASP B 145 ? 0.6227 0.9658 0.4906 0.0735 0.0183 0.0134 145 ASP B OD1 3703 O OD2 . ASP B 145 ? 0.6242 0.9998 0.4927 0.0809 0.0194 0.0147 145 ASP B OD2 3704 N N . ASP B 146 ? 0.6787 0.9620 0.5135 0.1196 0.0065 0.0138 146 ASP B N 3705 C CA . ASP B 146 ? 0.6801 0.9735 0.5120 0.1251 0.0064 0.0113 146 ASP B CA 3706 C C . ASP B 146 ? 0.6603 0.9872 0.5080 0.1040 0.0120 0.0097 146 ASP B C 3707 O O . ASP B 146 ? 0.6530 0.9671 0.5030 0.0962 0.0122 0.0090 146 ASP B O 3708 C CB . ASP B 146 ? 0.7009 1.0152 0.5145 0.1549 0.0029 0.0090 146 ASP B CB 3709 C CG . ASP B 146 ? 0.7290 0.9912 0.5169 0.1757 -0.0048 0.0101 146 ASP B CG 3710 O OD1 . ASP B 146 ? 0.7278 0.9427 0.5144 0.1635 -0.0071 0.0131 146 ASP B OD1 3711 O OD2 . ASP B 146 ? 0.7632 1.0316 0.5292 0.2042 -0.0091 0.0079 146 ASP B OD2 3712 N N . GLU B 147 ? 0.6505 1.0172 0.5062 0.0932 0.0160 0.0094 147 GLU B N 3713 C CA . GLU B 147 ? 0.6473 1.0421 0.5114 0.0692 0.0203 0.0084 147 GLU B CA 3714 C C . GLU B 147 ? 0.6325 0.9882 0.5023 0.0468 0.0214 0.0093 147 GLU B C 3715 O O . GLU B 147 ? 0.6269 0.9826 0.4967 0.0311 0.0227 0.0085 147 GLU B O 3716 C CB . GLU B 147 ? 0.6493 1.0948 0.5164 0.0609 0.0235 0.0083 147 GLU B CB 3717 C CG . GLU B 147 ? 0.6934 1.1921 0.5541 0.0830 0.0229 0.0069 147 GLU B CG 3718 C CD . GLU B 147 ? 0.7480 1.2770 0.6047 0.0875 0.0227 0.0050 147 GLU B CD 3719 O OE1 . GLU B 147 ? 0.7728 1.2893 0.6324 0.0673 0.0238 0.0051 147 GLU B OE1 3720 O OE2 . GLU B 147 ? 0.7818 1.3481 0.6305 0.1130 0.0211 0.0031 147 GLU B OE2 3721 N N . CYS B 148 ? 0.6269 0.9508 0.4995 0.0464 0.0205 0.0109 148 CYS B N 3722 C CA . CYS B 148 ? 0.6177 0.9052 0.4939 0.0313 0.0209 0.0114 148 CYS B CA 3723 C C . CYS B 148 ? 0.6140 0.8721 0.4878 0.0358 0.0186 0.0113 148 CYS B C 3724 O O . CYS B 148 ? 0.6080 0.8524 0.4821 0.0229 0.0196 0.0104 148 CYS B O 3725 C CB . CYS B 148 ? 0.6181 0.8859 0.4976 0.0329 0.0200 0.0133 148 CYS B CB 3726 S SG . CYS B 148 ? 0.6535 0.8788 0.5359 0.0237 0.0191 0.0141 148 CYS B SG 3727 N N . MET B 149 ? 0.6114 0.8580 0.4796 0.0544 0.0150 0.0122 149 MET B N 3728 C CA . MET B 149 ? 0.6063 0.8256 0.4701 0.0593 0.0124 0.0123 149 MET B CA 3729 C C . MET B 149 ? 0.5963 0.8340 0.4608 0.0538 0.0143 0.0100 149 MET B C 3730 O O . MET B 149 ? 0.5898 0.8073 0.4555 0.0456 0.0143 0.0097 149 MET B O 3731 C CB . MET B 149 ? 0.6273 0.8307 0.4777 0.0806 0.0073 0.0133 149 MET B CB 3732 C CG . MET B 149 ? 0.6405 0.8150 0.4846 0.0835 0.0037 0.0167 149 MET B CG 3733 S SD . MET B 149 ? 0.6686 0.8089 0.5189 0.0668 0.0031 0.0194 149 MET B SD 3734 C CE . MET B 149 ? 0.6704 0.7846 0.5067 0.0716 -0.0024 0.0241 149 MET B CE 3735 N N . ASN B 150 ? 0.5830 0.8624 0.4459 0.0577 0.0157 0.0085 150 ASN B N 3736 C CA . ASN B 150 ? 0.5752 0.8788 0.4374 0.0506 0.0172 0.0068 150 ASN B CA 3737 C C . ASN B 150 ? 0.5607 0.8591 0.4251 0.0240 0.0198 0.0068 150 ASN B C 3738 O O . ASN B 150 ? 0.5562 0.8502 0.4180 0.0158 0.0199 0.0062 150 ASN B O 3739 C CB . ASN B 150 ? 0.5809 0.9393 0.4400 0.0604 0.0180 0.0055 150 ASN B CB 3740 C CG . ASN B 150 ? 0.5994 0.9578 0.4489 0.0917 0.0141 0.0045 150 ASN B CG 3741 O OD1 . ASN B 150 ? 0.6059 0.9225 0.4487 0.1033 0.0104 0.0049 150 ASN B OD1 3742 N ND2 . ASN B 150 ? 0.6107 1.0150 0.4560 0.1056 0.0144 0.0034 150 ASN B ND2 3743 N N . SER B 151 ? 0.5497 0.8449 0.4156 0.0113 0.0215 0.0075 151 SER B N 3744 C CA . SER B 151 ? 0.5474 0.8255 0.4079 -0.0117 0.0226 0.0072 151 SER B CA 3745 C C . SER B 151 ? 0.5411 0.7734 0.4011 -0.0105 0.0210 0.0070 151 SER B C 3746 O O . SER B 151 ? 0.5506 0.7675 0.4023 -0.0233 0.0208 0.0063 151 SER B O 3747 C CB . SER B 151 ? 0.5502 0.8314 0.4090 -0.0231 0.0240 0.0074 151 SER B CB 3748 O OG . SER B 151 ? 0.5433 0.8001 0.4088 -0.0125 0.0233 0.0081 151 SER B OG 3749 N N . VAL B 152 ? 0.5313 0.7426 0.3977 0.0038 0.0195 0.0080 152 VAL B N 3750 C CA . VAL B 152 ? 0.5342 0.7095 0.4008 0.0057 0.0179 0.0082 152 VAL B CA 3751 C C . VAL B 152 ? 0.5427 0.7160 0.4069 0.0085 0.0170 0.0076 152 VAL B C 3752 O O . VAL B 152 ? 0.5477 0.7037 0.4071 0.0000 0.0170 0.0067 152 VAL B O 3753 C CB . VAL B 152 ? 0.5271 0.6856 0.3988 0.0177 0.0159 0.0102 152 VAL B CB 3754 C CG1 . VAL B 152 ? 0.5233 0.6528 0.3950 0.0175 0.0143 0.0106 152 VAL B CG1 3755 C CG2 . VAL B 152 ? 0.5194 0.6824 0.3941 0.0152 0.0167 0.0110 152 VAL B CG2 3756 N N . LYS B 153 ? 0.5491 0.7400 0.4144 0.0218 0.0160 0.0077 153 LYS B N 3757 C CA . LYS B 153 ? 0.5719 0.7627 0.4346 0.0279 0.0147 0.0069 153 LYS B CA 3758 C C . LYS B 153 ? 0.5833 0.7925 0.4421 0.0137 0.0164 0.0057 153 LYS B C 3759 O O . LYS B 153 ? 0.5782 0.7796 0.4351 0.0144 0.0156 0.0051 153 LYS B O 3760 C CB . LYS B 153 ? 0.5726 0.7787 0.4318 0.0483 0.0125 0.0067 153 LYS B CB 3761 C CG . LYS B 153 ? 0.5879 0.7681 0.4434 0.0619 0.0090 0.0085 153 LYS B CG 3762 C CD . LYS B 153 ? 0.6092 0.7939 0.4529 0.0838 0.0054 0.0076 153 LYS B CD 3763 C CE . LYS B 153 ? 0.6378 0.8185 0.4723 0.0979 0.0025 0.0088 153 LYS B CE 3764 N NZ . LYS B 153 ? 0.6499 0.8293 0.4660 0.1226 -0.0020 0.0071 153 LYS B NZ 3765 N N . ASN B 154 ? 0.6059 0.8398 0.4616 -0.0007 0.0184 0.0056 154 ASN B N 3766 C CA . ASN B 154 ? 0.6405 0.8883 0.4875 -0.0197 0.0192 0.0053 154 ASN B CA 3767 C C . ASN B 154 ? 0.6511 0.8695 0.4860 -0.0408 0.0191 0.0054 154 ASN B C 3768 O O . ASN B 154 ? 0.6671 0.8911 0.4883 -0.0605 0.0188 0.0056 154 ASN B O 3769 C CB . ASN B 154 ? 0.6500 0.9540 0.4955 -0.0233 0.0203 0.0053 154 ASN B CB 3770 C CG . ASN B 154 ? 0.7166 1.0446 0.5607 -0.0326 0.0219 0.0059 154 ASN B CG 3771 O OD1 . ASN B 154 ? 0.7342 1.0352 0.5784 -0.0360 0.0221 0.0062 154 ASN B OD1 3772 N ND2 . ASN B 154 ? 0.8121 1.1964 0.6547 -0.0367 0.0230 0.0062 154 ASN B ND2 3773 N N . GLY B 155 ? 0.6458 0.8316 0.4824 -0.0362 0.0187 0.0051 155 GLY B N 3774 C CA . GLY B 155 ? 0.6578 0.8076 0.4793 -0.0491 0.0176 0.0043 155 GLY B CA 3775 C C . GLY B 155 ? 0.6710 0.8252 0.4787 -0.0662 0.0178 0.0042 155 GLY B C 3776 O O . GLY B 155 ? 0.6915 0.8170 0.4769 -0.0812 0.0159 0.0034 155 GLY B O 3777 N N . THR B 156 ? 0.6570 0.8441 0.4746 -0.0638 0.0196 0.0049 156 THR B N 3778 C CA . THR B 156 ? 0.6743 0.8703 0.4794 -0.0811 0.0199 0.0050 156 THR B CA 3779 C C . THR B 156 ? 0.6614 0.8589 0.4781 -0.0697 0.0211 0.0049 156 THR B C 3780 O O . THR B 156 ? 0.6651 0.8879 0.4808 -0.0775 0.0223 0.0054 156 THR B O 3781 C CB . THR B 156 ? 0.6738 0.9203 0.4760 -0.0955 0.0210 0.0065 156 THR B CB 3782 O OG1 . THR B 156 ? 0.6540 0.9414 0.4768 -0.0764 0.0231 0.0069 156 THR B OG1 3783 C CG2 . THR B 156 ? 0.6916 0.9423 0.4829 -0.1079 0.0197 0.0071 156 THR B CG2 3784 N N . TYR B 157 ? 0.6505 0.8239 0.4776 -0.0524 0.0206 0.0045 157 TYR B N 3785 C CA . TYR B 157 ? 0.6397 0.8105 0.4754 -0.0435 0.0212 0.0046 157 TYR B CA 3786 C C . TYR B 157 ? 0.6653 0.8160 0.4830 -0.0569 0.0204 0.0029 157 TYR B C 3787 O O . TYR B 157 ? 0.6862 0.8042 0.4843 -0.0644 0.0183 0.0012 157 TYR B O 3788 C CB . TYR B 157 ? 0.6236 0.7742 0.4706 -0.0265 0.0202 0.0051 157 TYR B CB 3789 C CG . TYR B 157 ? 0.6005 0.7481 0.4546 -0.0195 0.0203 0.0057 157 TYR B CG 3790 C CD1 . TYR B 157 ? 0.5563 0.7249 0.4228 -0.0109 0.0208 0.0078 157 TYR B CD1 3791 C CD2 . TYR B 157 ? 0.5932 0.7171 0.4389 -0.0203 0.0193 0.0039 157 TYR B CD2 3792 C CE1 . TYR B 157 ? 0.5350 0.7018 0.4072 -0.0063 0.0206 0.0088 157 TYR B CE1 3793 C CE2 . TYR B 157 ? 0.5806 0.7072 0.4333 -0.0139 0.0194 0.0044 157 TYR B CE2 3794 C CZ . TYR B 157 ? 0.5446 0.6931 0.4114 -0.0086 0.0201 0.0072 157 TYR B CZ 3795 O OH . TYR B 157 ? 0.5027 0.6548 0.3756 -0.0042 0.0200 0.0083 157 TYR B OH 3796 N N . ASP B 158 ? 0.6648 0.8329 0.4864 -0.0587 0.0217 0.0033 158 ASP B N 3797 C CA . ASP B 158 ? 0.6967 0.8498 0.4992 -0.0723 0.0208 0.0017 158 ASP B CA 3798 C C . ASP B 158 ? 0.6901 0.8244 0.4979 -0.0586 0.0203 0.0005 158 ASP B C 3799 O O . ASP B 158 ? 0.6707 0.8259 0.4946 -0.0511 0.0220 0.0017 158 ASP B O 3800 C CB . ASP B 158 ? 0.6961 0.8880 0.4999 -0.0845 0.0227 0.0030 158 ASP B CB 3801 C CG . ASP B 158 ? 0.7339 0.9108 0.5112 -0.1054 0.0211 0.0017 158 ASP B CG 3802 O OD1 . ASP B 158 ? 0.7502 0.8864 0.5111 -0.1039 0.0187 -0.0007 158 ASP B OD1 3803 O OD2 . ASP B 158 ? 0.7476 0.9553 0.5185 -0.1231 0.0219 0.0031 158 ASP B OD2 3804 N N . TYR B 159 ? 0.7091 0.8064 0.5026 -0.0540 0.0179 -0.0018 159 TYR B N 3805 C CA . TYR B 159 ? 0.7130 0.7981 0.5104 -0.0395 0.0172 -0.0032 159 TYR B CA 3806 C C . TYR B 159 ? 0.7249 0.8116 0.5136 -0.0446 0.0173 -0.0046 159 TYR B C 3807 O O . TYR B 159 ? 0.7073 0.8121 0.5137 -0.0354 0.0187 -0.0035 159 TYR B O 3808 C CB . TYR B 159 ? 0.7284 0.7781 0.5093 -0.0308 0.0143 -0.0060 159 TYR B CB 3809 C CG . TYR B 159 ? 0.7246 0.7679 0.5059 -0.0155 0.0133 -0.0080 159 TYR B CG 3810 C CD1 . TYR B 159 ? 0.7022 0.7650 0.5075 -0.0022 0.0144 -0.0058 159 TYR B CD1 3811 C CD2 . TYR B 159 ? 0.7644 0.7828 0.5188 -0.0149 0.0108 -0.0121 159 TYR B CD2 3812 C CE1 . TYR B 159 ? 0.7189 0.7844 0.5250 0.0105 0.0134 -0.0072 159 TYR B CE1 3813 C CE2 . TYR B 159 ? 0.7662 0.7846 0.5206 0.0015 0.0097 -0.0143 159 TYR B CE2 3814 C CZ . TYR B 159 ? 0.7418 0.7878 0.5239 0.0138 0.0114 -0.0117 159 TYR B CZ 3815 O OH . TYR B 159 ? 0.7304 0.7846 0.5133 0.0288 0.0104 -0.0134 159 TYR B OH 3816 N N . PRO B 160 ? 0.7584 0.8246 0.5175 -0.0607 0.0152 -0.0068 160 PRO B N 3817 C CA . PRO B 160 ? 0.7721 0.8371 0.5194 -0.0672 0.0148 -0.0083 160 PRO B CA 3818 C C . PRO B 160 ? 0.7437 0.8538 0.5175 -0.0690 0.0187 -0.0052 160 PRO B C 3819 O O . PRO B 160 ? 0.7407 0.8574 0.5204 -0.0631 0.0193 -0.0058 160 PRO B O 3820 C CB . PRO B 160 ? 0.8093 0.8486 0.5192 -0.0904 0.0117 -0.0096 160 PRO B CB 3821 C CG . PRO B 160 ? 0.8234 0.8294 0.5161 -0.0879 0.0087 -0.0108 160 PRO B CG 3822 C CD . PRO B 160 ? 0.7955 0.8320 0.5251 -0.0745 0.0122 -0.0080 160 PRO B CD 3823 N N . LYS B 161 ? 0.7332 0.8744 0.5211 -0.0752 0.0209 -0.0022 161 LYS B N 3824 C CA . LYS B 161 ? 0.7107 0.8964 0.5213 -0.0734 0.0241 0.0006 161 LYS B CA 3825 C C . LYS B 161 ? 0.6868 0.8821 0.5209 -0.0540 0.0252 0.0020 161 LYS B C 3826 O O . LYS B 161 ? 0.6776 0.8958 0.5214 -0.0528 0.0268 0.0032 161 LYS B O 3827 C CB . LYS B 161 ? 0.7012 0.9147 0.5209 -0.0755 0.0254 0.0028 161 LYS B CB 3828 C CG . LYS B 161 ? 0.6971 0.9594 0.5335 -0.0724 0.0281 0.0053 161 LYS B CG 3829 C CD . LYS B 161 ? 0.7208 1.0105 0.5574 -0.0767 0.0286 0.0064 161 LYS B CD 3830 C CE . LYS B 161 ? 0.7242 1.0683 0.5710 -0.0738 0.0308 0.0080 161 LYS B CE 3831 N NZ . LYS B 161 ? 0.7246 1.0780 0.5886 -0.0520 0.0315 0.0092 161 LYS B NZ 3832 N N . TYR B 162 ? 0.6809 0.8593 0.5223 -0.0406 0.0240 0.0022 162 TYR B N 3833 C CA . TYR B 162 ? 0.6618 0.8488 0.5221 -0.0260 0.0242 0.0046 162 TYR B CA 3834 C C . TYR B 162 ? 0.6626 0.8316 0.5192 -0.0191 0.0227 0.0028 162 TYR B C 3835 O O . TYR B 162 ? 0.6495 0.8273 0.5195 -0.0100 0.0223 0.0051 162 TYR B O 3836 C CB . TYR B 162 ? 0.6510 0.8399 0.5224 -0.0170 0.0235 0.0072 162 TYR B CB 3837 C CG . TYR B 162 ? 0.6533 0.8656 0.5290 -0.0178 0.0246 0.0088 162 TYR B CG 3838 C CD1 . TYR B 162 ? 0.6405 0.8764 0.5258 -0.0107 0.0252 0.0113 162 TYR B CD1 3839 C CD2 . TYR B 162 ? 0.6667 0.8793 0.5349 -0.0243 0.0248 0.0077 162 TYR B CD2 3840 C CE1 . TYR B 162 ? 0.6499 0.9103 0.5364 -0.0070 0.0258 0.0121 162 TYR B CE1 3841 C CE2 . TYR B 162 ? 0.6776 0.9187 0.5494 -0.0228 0.0257 0.0088 162 TYR B CE2 3842 C CZ . TYR B 162 ? 0.6573 0.9229 0.5378 -0.0127 0.0262 0.0107 162 TYR B CZ 3843 O OH . TYR B 162 ? 0.6709 0.9673 0.5522 -0.0072 0.0267 0.0112 162 TYR B OH 3844 N N . GLU B 163 ? 0.6875 0.8317 0.5225 -0.0234 0.0212 -0.0012 163 GLU B N 3845 C CA . GLU B 163 ? 0.7004 0.8272 0.5269 -0.0127 0.0192 -0.0041 163 GLU B CA 3846 C C . GLU B 163 ? 0.6871 0.8324 0.5245 -0.0070 0.0198 -0.0033 163 GLU B C 3847 O O . GLU B 163 ? 0.6754 0.8284 0.5223 0.0041 0.0191 -0.0024 163 GLU B O 3848 C CB . GLU B 163 ? 0.7350 0.8264 0.5279 -0.0173 0.0164 -0.0091 163 GLU B CB 3849 C CG . GLU B 163 ? 0.7686 0.8423 0.5473 -0.0018 0.0137 -0.0132 163 GLU B CG 3850 C CD . GLU B 163 ? 0.8280 0.8565 0.5676 -0.0010 0.0096 -0.0184 163 GLU B CD 3851 O OE1 . GLU B 163 ? 0.8513 0.8602 0.5724 -0.0175 0.0086 -0.0184 163 GLU B OE1 3852 O OE2 . GLU B 163 ? 0.8451 0.8581 0.5698 0.0163 0.0068 -0.0223 163 GLU B OE2 3853 N N . GLU B 164 ? 0.6986 0.8546 0.5344 -0.0160 0.0212 -0.0033 164 GLU B N 3854 C CA . GLU B 164 ? 0.6963 0.8680 0.5390 -0.0123 0.0218 -0.0032 164 GLU B CA 3855 C C . GLU B 164 ? 0.6644 0.8638 0.5334 -0.0065 0.0229 0.0021 164 GLU B C 3856 O O . GLU B 164 ? 0.6574 0.8657 0.5334 0.0014 0.0220 0.0029 164 GLU B O 3857 C CB . GLU B 164 ? 0.7135 0.8891 0.5458 -0.0255 0.0229 -0.0045 164 GLU B CB 3858 C CG . GLU B 164 ? 0.7738 0.9143 0.5715 -0.0351 0.0203 -0.0094 164 GLU B CG 3859 C CD . GLU B 164 ? 0.8167 0.9620 0.6009 -0.0536 0.0210 -0.0099 164 GLU B CD 3860 O OE1 . GLU B 164 ? 0.8319 0.9815 0.6127 -0.0534 0.0210 -0.0113 164 GLU B OE1 3861 O OE2 . GLU B 164 ? 0.8317 0.9784 0.6072 -0.0693 0.0212 -0.0087 164 GLU B OE2 3862 N N . GLU B 165 ? 0.6482 0.8602 0.5279 -0.0102 0.0241 0.0057 165 GLU B N 3863 C CA . GLU B 165 ? 0.6291 0.8575 0.5255 -0.0049 0.0238 0.0109 165 GLU B CA 3864 C C . GLU B 165 ? 0.6293 0.8505 0.5298 0.0017 0.0215 0.0129 165 GLU B C 3865 O O . GLU B 165 ? 0.6258 0.8581 0.5338 0.0041 0.0202 0.0163 165 GLU B O 3866 C CB . GLU B 165 ? 0.6237 0.8611 0.5237 -0.0061 0.0246 0.0132 165 GLU B CB 3867 C CG . GLU B 165 ? 0.6213 0.8661 0.5300 0.0010 0.0228 0.0184 165 GLU B CG 3868 C CD . GLU B 165 ? 0.6507 0.9009 0.5582 0.0054 0.0226 0.0199 165 GLU B CD 3869 O OE1 . GLU B 165 ? 0.6388 0.8960 0.5424 0.0016 0.0245 0.0173 165 GLU B OE1 3870 O OE2 . GLU B 165 ? 0.6568 0.9040 0.5642 0.0128 0.0199 0.0239 165 GLU B OE2 3871 N N . SER B 166 ? 0.6319 0.8366 0.5263 0.0031 0.0207 0.0112 166 SER B N 3872 C CA . SER B 166 ? 0.6287 0.8298 0.5267 0.0081 0.0185 0.0135 166 SER B CA 3873 C C . SER B 166 ? 0.6324 0.8424 0.5301 0.0132 0.0174 0.0125 166 SER B C 3874 O O . SER B 166 ? 0.6141 0.8383 0.5194 0.0135 0.0157 0.0168 166 SER B O 3875 C CB . SER B 166 ? 0.6373 0.8198 0.5280 0.0091 0.0182 0.0113 166 SER B CB 3876 O OG . SER B 166 ? 0.6262 0.8057 0.5173 0.0053 0.0190 0.0121 166 SER B OG 3877 N N . LYS B 167 ? 0.6508 0.8520 0.5361 0.0168 0.0179 0.0068 167 LYS B N 3878 C CA . LYS B 167 ? 0.6663 0.8761 0.5465 0.0259 0.0167 0.0041 167 LYS B CA 3879 C C . LYS B 167 ? 0.6585 0.8958 0.5510 0.0245 0.0168 0.0076 167 LYS B C 3880 O O . LYS B 167 ? 0.6520 0.9102 0.5490 0.0295 0.0153 0.0091 167 LYS B O 3881 C CB . LYS B 167 ? 0.6917 0.8787 0.5495 0.0297 0.0165 -0.0028 167 LYS B CB 3882 C CG . LYS B 167 ? 0.7158 0.9076 0.5617 0.0435 0.0146 -0.0073 167 LYS B CG 3883 C CD . LYS B 167 ? 0.7599 0.9209 0.5774 0.0450 0.0134 -0.0139 167 LYS B CD 3884 C CE . LYS B 167 ? 0.7944 0.9171 0.5879 0.0455 0.0115 -0.0175 167 LYS B CE 3885 N NZ . LYS B 167 ? 0.8384 0.9266 0.6039 0.0351 0.0103 -0.0213 167 LYS B NZ 3886 N N . LEU B 168 ? 0.6623 0.9031 0.5596 0.0173 0.0184 0.0090 168 LEU B N 3887 C CA . LEU B 168 ? 0.6599 0.9245 0.5680 0.0149 0.0184 0.0128 168 LEU B CA 3888 C C . LEU B 168 ? 0.6568 0.9329 0.5749 0.0107 0.0162 0.0201 168 LEU B C 3889 O O . LEU B 168 ? 0.6557 0.9533 0.5783 0.0102 0.0144 0.0232 168 LEU B O 3890 C CB . LEU B 168 ? 0.6607 0.9264 0.5705 0.0087 0.0205 0.0130 168 LEU B CB 3891 C CG . LEU B 168 ? 0.6765 0.9326 0.5733 0.0081 0.0220 0.0068 168 LEU B CG 3892 C CD1 . LEU B 168 ? 0.6731 0.9309 0.5706 -0.0011 0.0242 0.0075 168 LEU B CD1 3893 C CD2 . LEU B 168 ? 0.6746 0.9444 0.5698 0.0134 0.0215 0.0047 168 LEU B CD2 3894 N N . ASN B 169 ? 0.6585 0.9199 0.5768 0.0070 0.0157 0.0228 169 ASN B N 3895 C CA . ASN B 169 ? 0.6638 0.9255 0.5843 0.0019 0.0125 0.0297 169 ASN B CA 3896 C C . ASN B 169 ? 0.6712 0.9406 0.5909 0.0013 0.0102 0.0313 169 ASN B C 3897 O O . ASN B 169 ? 0.6716 0.9509 0.5912 -0.0063 0.0068 0.0375 169 ASN B O 3898 C CB . ASN B 169 ? 0.6644 0.9053 0.5809 0.0017 0.0121 0.0308 169 ASN B CB 3899 C CG . ASN B 169 ? 0.6657 0.9068 0.5823 0.0028 0.0139 0.0302 169 ASN B CG 3900 O OD1 . ASN B 169 ? 0.6406 0.8747 0.5551 0.0049 0.0159 0.0271 169 ASN B OD1 3901 N ND2 . ASN B 169 ? 0.6587 0.9110 0.5773 0.0008 0.0131 0.0336 169 ASN B ND2 3902 N N . ARG B 170 ? 0.6832 0.9478 0.5996 0.0088 0.0115 0.0258 170 ARG B N 3903 C CA . ARG B 170 ? 0.7025 0.9775 0.6177 0.0107 0.0096 0.0266 170 ARG B CA 3904 C C . ARG B 170 ? 0.7109 1.0202 0.6292 0.0122 0.0085 0.0275 170 ARG B C 3905 O O . ARG B 170 ? 0.7160 1.0467 0.6350 0.0092 0.0062 0.0309 170 ARG B O 3906 C CB . ARG B 170 ? 0.7027 0.9614 0.6103 0.0209 0.0110 0.0200 170 ARG B CB 3907 C CG . ARG B 170 ? 0.7010 0.9703 0.6068 0.0246 0.0092 0.0205 170 ARG B CG 3908 C CD . ARG B 170 ? 0.6741 0.9212 0.5697 0.0347 0.0100 0.0144 170 ARG B CD 3909 N NE . ARG B 170 ? 0.6856 0.9240 0.5687 0.0467 0.0109 0.0072 170 ARG B NE 3910 C CZ . ARG B 170 ? 0.6814 0.8906 0.5542 0.0461 0.0123 0.0031 170 ARG B CZ 3911 N NH1 . ARG B 170 ? 0.6716 0.8645 0.5484 0.0356 0.0135 0.0053 170 ARG B NH1 3912 N NH2 . ARG B 170 ? 0.6898 0.8868 0.5451 0.0559 0.0118 -0.0031 170 ARG B NH2 3913 N N . ASN B 171 ? 0.7291 1.0470 0.6486 0.0158 0.0101 0.0249 171 ASN B N 3914 C CA . ASN B 171 ? 0.7433 1.0954 0.6642 0.0214 0.0095 0.0238 171 ASN B CA 3915 C C . ASN B 171 ? 0.7466 1.1254 0.6751 0.0099 0.0079 0.0306 171 ASN B C 3916 O O . ASN B 171 ? 0.7478 1.1634 0.6784 0.0101 0.0062 0.0323 171 ASN B O 3917 C CB . ASN B 171 ? 0.7511 1.0948 0.6635 0.0355 0.0115 0.0153 171 ASN B CB 3918 C CG . ASN B 171 ? 0.7737 1.0944 0.6717 0.0485 0.0116 0.0085 171 ASN B CG 3919 O OD1 . ASN B 171 ? 0.7780 1.1021 0.6753 0.0509 0.0104 0.0095 171 ASN B OD1 3920 N ND2 . ASN B 171 ? 0.7998 1.0948 0.6833 0.0559 0.0126 0.0017 171 ASN B ND2 3921 N N . GLU B 172 ? 0.7582 1.1213 0.6892 0.0006 0.0080 0.0343 172 GLU B N 3922 C CA . GLU B 172 ? 0.7656 1.1488 0.7006 -0.0091 0.0064 0.0401 172 GLU B CA 3923 C C . GLU B 172 ? 0.7710 1.1737 0.7039 -0.0244 0.0017 0.0489 172 GLU B C 3924 O O . GLU B 172 ? 0.7778 1.1793 0.7066 -0.0283 -0.0002 0.0510 172 GLU B O 3925 C CB . GLU B 172 ? 0.7711 1.1313 0.7060 -0.0129 0.0073 0.0416 172 GLU B CB 3926 C CG . GLU B 172 ? 0.7994 1.1277 0.7280 -0.0169 0.0058 0.0445 172 GLU B CG 3927 C CD . GLU B 172 ? 0.8366 1.1480 0.7637 -0.0158 0.0070 0.0449 172 GLU B CD 3928 O OE1 . GLU B 172 ? 0.8355 1.1580 0.7679 -0.0123 0.0098 0.0418 172 GLU B OE1 3929 O OE2 . GLU B 172 ? 0.8666 1.1549 0.7857 -0.0172 0.0048 0.0479 172 GLU B OE2 3972 C C1 . EDO F . ? 0.3868 0.4151 0.5108 -0.0080 0.0232 -0.0034 1 EDO A C1 3973 O O1 . EDO F . ? 0.3865 0.4190 0.5145 -0.0099 0.0244 -0.0028 1 EDO A O1 3974 C C2 . EDO F . ? 0.3818 0.4126 0.5043 -0.0049 0.0238 -0.0034 1 EDO A C2 3975 O O2 . EDO F . ? 0.3484 0.3866 0.4761 -0.0051 0.0237 -0.0040 1 EDO A O2 3997 O O . HOH I . ? 0.2708 0.2554 0.3384 0.0074 0.0091 -0.0166 2 HOH A O 3998 O O . HOH I . ? 0.2332 0.2511 0.3538 0.0143 0.0132 -0.0075 3 HOH A O 3999 O O . HOH I . ? 0.2134 0.2358 0.3282 -0.0021 0.0189 -0.0065 4 HOH A O 4000 O O . HOH I . ? 0.2441 0.2889 0.3499 0.0274 0.0044 -0.0226 5 HOH A O 4001 O O . HOH I . ? 0.2063 0.2356 0.3338 0.0016 0.0083 -0.0066 6 HOH A O 4002 O O . HOH I . ? 0.2721 0.2616 0.3580 -0.0136 0.0104 -0.0010 8 HOH A O 4003 O O . HOH I . ? 0.2401 0.2328 0.3093 0.0184 0.0154 -0.0132 333 HOH A O 4004 O O . HOH I . ? 0.5527 0.5406 0.6609 -0.0136 0.0201 0.0048 334 HOH A O 4005 O O . HOH I . ? 0.2377 0.2756 0.3493 0.0163 0.0100 -0.0172 335 HOH A O 4006 O O . HOH I . ? 0.6580 0.6027 0.6620 0.0480 0.0154 -0.0227 336 HOH A O 4007 O O . HOH I . ? 0.5248 0.6261 0.6680 0.0112 -0.0054 -0.0237 337 HOH A O 4008 O O . HOH I . ? 0.6569 0.6564 0.7804 -0.0516 0.0125 -0.0174 338 HOH A O 4009 O O . HOH I . ? 0.5168 0.5200 0.6071 -0.0093 0.0058 -0.0100 339 HOH A O 4010 O O . HOH I . ? 0.3255 0.2782 0.3588 -0.0035 0.0104 -0.0129 340 HOH A O 4011 O O . HOH I . ? 0.2823 0.3027 0.4031 -0.0119 0.0056 -0.0026 341 HOH A O 4012 O O . HOH I . ? 0.3596 0.4149 0.5094 -0.0400 0.0036 -0.0205 342 HOH A O 4013 O O . HOH I . ? 0.7907 0.6894 0.7685 -0.0188 0.0088 -0.0042 343 HOH A O 4014 O O . HOH I . ? 0.5272 0.5376 0.6361 0.0062 -0.0006 -0.0306 344 HOH A O 4015 O O . HOH I . ? 0.4275 0.2798 0.3221 0.1161 0.0360 -0.0340 345 HOH A O 4016 O O . HOH I . ? 0.3320 0.3182 0.3956 0.0195 0.0097 -0.0197 346 HOH A O 4017 O O . HOH I . ? 0.5216 0.5373 0.5887 0.0448 0.0209 -0.0115 347 HOH A O 4018 O O . HOH I . ? 0.6738 0.6005 0.6727 0.0224 0.0210 -0.0109 348 HOH A O 4019 O O . HOH I . ? 0.7544 0.7461 0.8195 0.0315 0.0212 -0.0145 349 HOH A O 4020 O O . HOH I . ? 0.6641 0.5895 0.6650 0.0134 0.0160 -0.0140 350 HOH A O 4021 O O . HOH I . ? 0.2789 0.2874 0.3772 -0.0041 0.0062 -0.0123 351 HOH A O 4022 O O . HOH I . ? 0.6343 0.5985 0.6638 0.0443 0.0253 -0.0177 352 HOH A O 4023 O O . HOH I . ? 0.6775 0.6235 0.6832 0.0538 0.0195 -0.0247 353 HOH A O 4024 O O . HOH I . ? 0.6191 0.6274 0.7280 0.0113 0.0045 -0.0251 354 HOH A O 4025 O O . HOH I . ? 0.2424 0.3006 0.3696 0.0132 0.0049 -0.0205 355 HOH A O 4026 O O . HOH I . ? 0.2922 0.2691 0.3553 0.0027 0.0179 -0.0054 356 HOH A O 4027 O O . HOH I . ? 0.3044 0.3035 0.3840 -0.0293 -0.0001 -0.0015 357 HOH A O 4028 O O . HOH I . ? 0.2847 0.3115 0.3888 0.0147 0.0122 -0.0153 358 HOH A O 4029 O O . HOH I . ? 0.4401 0.4510 0.5639 0.0012 0.0124 -0.0004 359 HOH A O 4030 O O . HOH I . ? 0.2296 0.2523 0.3580 -0.0055 0.0074 -0.0074 360 HOH A O 4031 O O . HOH I . ? 0.7003 0.7023 0.7135 0.0935 0.0124 -0.0197 361 HOH A O 4032 O O . HOH I . ? 0.5586 0.5741 0.6679 0.0112 0.0052 -0.0223 362 HOH A O 4033 O O . HOH I . ? 0.3399 0.3099 0.3722 0.0426 0.0114 -0.0236 363 HOH A O 4034 O O . HOH I . ? 0.7513 0.7616 0.8450 -0.0070 0.0078 -0.0085 364 HOH A O 4035 O O . HOH I . ? 0.2438 0.2654 0.3627 0.0058 0.0079 -0.0141 365 HOH A O 4036 O O . HOH I . ? 0.2760 0.3256 0.3807 0.0312 0.0020 -0.0242 366 HOH A O 4037 O O . HOH I . ? 0.2870 0.3065 0.3677 0.0350 0.0086 -0.0211 367 HOH A O 4038 O O . HOH I . ? 0.3498 0.2989 0.3818 -0.0085 0.0091 -0.0105 368 HOH A O 4039 O O . HOH I . ? 0.7890 0.7408 0.8158 -0.0322 -0.0039 0.0107 369 HOH A O 4040 O O . HOH I . ? 0.7641 0.6798 0.7514 0.0226 0.0262 -0.0058 370 HOH A O 4041 O O . HOH I . ? 0.7003 0.6895 0.7749 -0.0125 0.0057 -0.0096 371 HOH A O 4042 O O . HOH I . ? 0.3058 0.3317 0.4128 -0.0254 -0.0016 0.0039 372 HOH A O 4043 O O . HOH I . ? 0.2937 0.3255 0.3906 -0.0409 -0.0072 0.0098 373 HOH A O 4044 O O . HOH I . ? 0.6424 0.6552 0.7328 0.0257 0.0202 -0.0095 374 HOH A O 4045 O O . HOH I . ? 0.5255 0.5913 0.6840 -0.0503 0.0152 -0.0104 375 HOH A O 4046 O O . HOH I . ? 0.5233 0.6230 0.6545 0.0276 -0.0034 -0.0224 376 HOH A O 4047 O O . HOH I . ? 0.7642 0.6249 0.7004 -0.0246 0.0081 -0.0042 377 HOH A O 4048 O O . HOH I . ? 0.7048 0.7451 0.7793 0.0467 -0.0129 -0.0363 378 HOH A O 4049 O O . HOH I . ? 0.5728 0.6629 0.7037 0.0114 -0.0139 -0.0308 379 HOH A O 4050 O O . HOH I . ? 0.4768 0.5364 0.5732 0.0472 0.0103 -0.0167 380 HOH A O 4051 O O . HOH I . ? 0.7820 0.7179 0.7450 0.1123 0.0778 0.0080 381 HOH A O 4052 O O . HOH I . ? 0.7043 0.6335 0.7167 -0.0115 0.0120 -0.0022 382 HOH A O 4053 O O . HOH I . ? 0.6012 0.5383 0.6164 -0.0045 0.0123 -0.0126 383 HOH A O 4054 O O . HOH I . ? 0.6010 0.6242 0.7236 -0.0111 0.0258 -0.0010 384 HOH A O 4055 O O . HOH I . ? 0.2963 0.3643 0.4537 -0.0302 0.0156 -0.0103 385 HOH A O 4056 O O . HOH I . ? 0.5724 0.6070 0.6942 -0.0106 0.0022 0.0117 386 HOH A O 4057 O O . HOH I . ? 0.5586 0.6089 0.7023 -0.0161 0.0209 -0.0064 387 HOH A O 4058 O O . HOH I . ? 0.6719 0.6464 0.6990 0.0573 0.0053 -0.0317 388 HOH A O 4059 O O . HOH I . ? 0.5831 0.6715 0.6956 0.0409 -0.0062 -0.0254 389 HOH A O 4060 O O . HOH I . ? 0.4123 0.4307 0.5051 -0.0343 -0.0033 0.0041 390 HOH A O 4061 O O . HOH I . ? 0.3625 0.3731 0.4508 0.0166 0.0128 -0.0150 391 HOH A O 4062 O O . HOH I . ? 0.6469 0.5800 0.6619 -0.0239 0.0047 -0.0023 392 HOH A O 4063 O O . HOH I . ? 0.7913 0.7534 0.8189 -0.0413 -0.0119 0.0135 393 HOH A O 4064 O O . HOH I . ? 0.3386 0.3188 0.4477 -0.0027 0.0175 -0.0043 394 HOH A O 4065 O O . HOH I . ? 0.7377 0.7690 0.8621 -0.0054 0.0054 0.0105 395 HOH A O 4066 O O . HOH I . ? 0.5095 0.3560 0.3850 0.1215 0.0310 -0.0367 396 HOH A O 4067 O O . HOH I . ? 0.3304 0.4093 0.4488 0.0319 -0.0017 -0.0238 397 HOH A O 4068 O O . HOH I . ? 0.5793 0.5898 0.6876 0.0016 -0.0033 -0.0330 398 HOH A O 4069 O O . HOH I . ? 0.6676 0.6793 0.7343 0.0428 0.0136 -0.0177 399 HOH A O 4070 O O . HOH I . ? 0.6011 0.5579 0.6135 -0.0715 -0.0178 0.0084 400 HOH A O 4071 O O . HOH I . ? 0.7683 0.6709 0.7459 0.0106 0.0173 -0.0132 401 HOH A O 4072 O O . HOH I . ? 0.5694 0.5223 0.6021 -0.0254 0.0048 -0.0071 402 HOH A O 4073 O O . HOH I . ? 0.6265 0.6699 0.7520 -0.0113 0.0045 0.0026 403 HOH A O 4074 O O . HOH I . ? 0.5313 0.5313 0.6499 -0.0181 0.0216 -0.0001 404 HOH A O 4075 O O . HOH I . ? 0.7374 0.7592 0.8300 0.0289 0.0255 -0.0030 405 HOH A O 4076 O O . HOH I . ? 0.3480 0.3229 0.4001 0.0179 0.0108 -0.0190 406 HOH A O 4077 O O . HOH I . ? 0.6782 0.7053 0.7809 0.0162 -0.0069 -0.0346 407 HOH A O 4078 O O . HOH I . ? 0.7091 0.6080 0.6759 -0.0590 -0.0075 0.0000 408 HOH A O 4079 O O . HOH I . ? 0.2911 0.2955 0.4179 -0.0202 0.0100 -0.0173 409 HOH A O 4080 O O . HOH I . ? 0.3676 0.3695 0.4259 0.0440 0.0104 -0.0214 410 HOH A O 4081 O O . HOH I . ? 0.4721 0.5685 0.6404 -0.0475 0.0045 -0.0154 411 HOH A O 4082 O O . HOH I . ? 0.6833 0.7970 0.8533 -0.0216 0.0044 -0.0148 412 HOH A O 4083 O O . HOH I . ? 0.5458 0.5421 0.6429 -0.0117 0.0094 0.0118 413 HOH A O 4084 O O . HOH I . ? 0.6419 0.6443 0.7225 0.0130 0.0301 -0.0001 414 HOH A O 4085 O O . HOH I . ? 0.7143 0.7102 0.7667 0.0446 0.0132 -0.0193 415 HOH A O 4086 O O . HOH I . ? 0.4172 0.3605 0.4426 -0.0026 0.0117 -0.0103 416 HOH A O 4087 O O . HOH I . ? 0.6818 0.6060 0.6580 0.0767 0.0273 -0.0264 417 HOH A O 4088 O O . HOH I . ? 0.8978 0.8271 0.8783 -0.0732 -0.0227 0.0100 418 HOH A O 4089 O O . HOH I . ? 0.8207 0.8324 0.9284 -0.0095 0.0061 0.0128 419 HOH A O 4090 O O . HOH I . ? 0.7874 0.7787 0.8156 0.0662 -0.0023 -0.0349 420 HOH A O 4091 O O . HOH I . ? 0.6647 0.6591 0.7874 -0.0370 0.0152 -0.0144 421 HOH A O 4092 O O . HOH I . ? 0.3833 0.3651 0.4463 -0.0284 0.0012 -0.0040 422 HOH A O 4093 O O . HOH I . ? 0.3257 0.3375 0.4582 -0.0410 0.0146 -0.0143 423 HOH A O 4094 O O . HOH I . ? 0.3315 0.3442 0.4489 0.0034 0.0033 -0.0250 424 HOH A O 4095 O O . HOH I . ? 0.5750 0.5447 0.6215 -0.0178 0.0095 -0.0075 425 HOH A O 4096 O O . HOH I . ? 0.2919 0.3868 0.4271 0.0212 -0.0015 -0.0219 426 HOH A O 4097 O O . HOH I . ? 0.6124 0.6901 0.7444 0.0186 0.0200 -0.0075 427 HOH A O 4098 O O . HOH I . ? 0.5475 0.6055 0.6877 -0.0173 -0.0056 -0.0285 428 HOH A O 4099 O O . HOH I . ? 0.2896 0.2953 0.3810 0.0136 0.0087 -0.0189 429 HOH A O 4100 O O . HOH I . ? 0.7463 0.6904 0.7637 0.0214 0.0148 -0.0173 430 HOH A O 4101 O O . HOH I . ? 0.4303 0.3804 0.4573 0.0144 0.0144 -0.0145 431 HOH A O 4102 O O . HOH I . ? 0.3329 0.3341 0.4230 -0.0104 0.0053 -0.0098 432 HOH A O 4103 O O . HOH I . ? 0.6300 0.6297 0.7493 -0.0385 0.0041 -0.0250 433 HOH A O 4104 O O . HOH I . ? 0.3685 0.3744 0.4958 -0.0142 0.0107 -0.0146 434 HOH A O 4105 O O . HOH I . ? 0.3571 0.3250 0.4047 -0.0088 0.0098 -0.0110 435 HOH A O 4106 O O . HOH I . ? 0.3187 0.4058 0.4521 0.0222 0.0052 -0.0179 436 HOH A O 4107 O O . HOH I . ? 0.3493 0.3600 0.4763 -0.0065 0.0084 -0.0158 437 HOH A O 4108 O O . HOH I . ? 0.7922 0.7732 0.8306 0.0406 -0.0135 -0.0461 438 HOH A O 4109 O O . HOH I . ? 0.6770 0.6416 0.7281 -0.0209 0.0049 0.0112 439 HOH A O 4110 O O . HOH I . ? 0.6935 0.6941 0.7290 -0.0890 -0.0259 0.0178 440 HOH A O 4111 O O . HOH I . ? 0.7212 0.7744 0.8058 0.0395 -0.0173 -0.0375 441 HOH A O 4112 O O . HOH I . ? 0.6210 0.5992 0.6764 0.0186 0.0116 -0.0194 442 HOH A O 4113 O O . HOH I . ? 0.7681 0.7725 0.8103 0.0639 0.0105 -0.0217 443 HOH A O 4114 O O . HOH I . ? 0.7433 0.7181 0.7895 0.0188 0.0199 -0.0135 444 HOH A O 4115 O O . HOH I . ? 0.7812 0.7030 0.7839 0.0033 0.0257 0.0038 445 HOH A O 4116 O O . HOH I . ? 0.5204 0.5045 0.5535 -0.0746 -0.0203 0.0123 446 HOH A O 4117 O O . HOH I . ? 0.6764 0.6415 0.7042 0.0625 0.0350 -0.0138 447 HOH A O 4118 O O . HOH I . ? 0.6529 0.6554 0.7763 -0.0137 0.0082 -0.0192 448 HOH A O 4119 O O . HOH I . ? 0.2707 0.3266 0.4225 -0.0278 0.0184 -0.0086 449 HOH A O 4120 O O . HOH I . ? 0.7803 0.7654 0.8926 -0.0316 0.0077 -0.0228 450 HOH A O 4121 O O . HOH I . ? 0.8685 0.7703 0.8055 0.1009 0.0610 -0.0081 451 HOH A O 4122 O O . HOH I . ? 0.8377 0.8485 0.9642 -0.0818 0.0144 -0.0144 452 HOH A O 4123 O O . HOH I . ? 0.7414 0.6225 0.6373 0.1015 -0.0098 -0.0545 453 HOH A O 4124 O O . HOH I . ? 0.6699 0.7115 0.8031 0.0052 0.0098 0.0046 454 HOH A O 4125 O O . HOH I . ? 0.5529 0.5644 0.6323 0.0229 0.0336 0.0005 455 HOH A O 4126 O O . HOH I . ? 0.3143 0.3441 0.4435 0.0037 0.0094 -0.0041 456 HOH A O 4127 O O . HOH I . ? 0.4555 0.4673 0.5817 -0.0308 0.0031 -0.0249 457 HOH A O 4128 O O . HOH I . ? 0.7203 0.6995 0.7459 0.0590 -0.0059 -0.0407 458 HOH A O 4129 O O . HOH I . ? 0.8606 0.8170 0.8595 -0.0929 -0.0237 0.0121 459 HOH A O 4130 O O . HOH I . ? 0.6840 0.6593 0.7356 -0.0113 0.0115 -0.0084 460 HOH A O 4131 O O . HOH I . ? 0.7736 0.7222 0.7946 0.0238 0.0155 -0.0165 461 HOH A O 4132 O O . HOH I . ? 0.6678 0.6406 0.6910 -0.0800 -0.0150 0.0100 462 HOH A O 4133 O O . HOH I . ? 0.7449 0.7094 0.7485 0.0716 0.0136 -0.0231 463 HOH A O 4134 O O . HOH I . ? 0.4413 0.3360 0.3965 0.0851 0.0199 -0.0380 464 HOH A O 4135 O O . HOH I . ? 0.7309 0.7881 0.8004 0.0714 0.0019 -0.0222 465 HOH A O 4136 O O . HOH I . ? 0.7377 0.6275 0.7028 0.0079 0.0184 -0.0107 466 HOH A O 4137 O O . HOH I . ? 0.6605 0.7263 0.7841 0.0210 0.0177 -0.0101 467 HOH A O 4138 O O . HOH I . ? 0.3714 0.3969 0.5114 -0.0373 0.0191 -0.0093 468 HOH A O 4139 O O . HOH I . ? 0.7984 0.6984 0.7127 0.1030 -0.0056 -0.0493 469 HOH A O 4140 O O . HOH I . ? 0.6932 0.6781 0.7350 -0.0669 -0.0104 0.0080 470 HOH A O 4141 O O . HOH I . ? 0.5677 0.5966 0.6389 0.0522 0.0109 -0.0190 471 HOH A O 4142 O O . HOH I . ? 0.6610 0.6017 0.6558 0.0550 0.0177 -0.0206 472 HOH A O 4143 O O . HOH I . ? 0.3403 0.3770 0.4634 -0.0149 0.0021 0.0030 473 HOH A O 4144 O O . HOH I . ? 0.4093 0.4367 0.5233 -0.0159 0.0028 -0.0016 474 HOH A O 4145 O O . HOH I . ? 0.5284 0.6087 0.6319 0.0493 -0.0005 -0.0222 475 HOH A O 4146 O O . HOH I . ? 0.8988 0.8950 1.0208 -0.0598 0.0168 -0.0141 476 HOH A O 4147 O O . HOH I . ? 0.3582 0.4004 0.4651 0.0202 0.0275 -0.0034 477 HOH A O 4148 O O . HOH I . ? 0.5052 0.4976 0.6195 0.0034 0.0153 -0.0050 478 HOH A O 4149 O O . HOH I . ? 0.7375 0.7010 0.7706 0.0318 0.0127 -0.0218 479 HOH A O 4150 O O . HOH I . ? 0.6076 0.6516 0.7276 -0.0167 -0.0024 0.0152 480 HOH A O 4151 O O . HOH I . ? 0.3580 0.3603 0.4553 -0.0041 0.0265 0.0013 481 HOH A O 4152 O O . HOH I . ? 0.6661 0.6803 0.7949 -0.0214 0.0224 -0.0032 482 HOH A O 4153 O O . HOH I . ? 0.5181 0.5768 0.6391 0.0138 -0.0072 -0.0306 483 HOH A O 4154 O O . HOH I . ? 0.7764 0.7113 0.7868 0.0167 0.0302 0.0006 484 HOH A O 4155 O O . HOH I . ? 0.3751 0.3862 0.4584 0.0206 0.0217 -0.0082 485 HOH A O 4156 O O . HOH I . ? 0.8177 0.6239 0.6905 0.0244 0.0312 -0.0062 486 HOH A O 4157 O O . HOH I . ? 0.5277 0.4285 0.4909 0.0409 0.0295 -0.0086 487 HOH A O 4158 O O . HOH I . ? 0.6901 0.6922 0.7421 0.0492 0.0249 -0.0094 488 HOH A O 4159 O O . HOH I . ? 0.6200 0.7205 0.7746 0.0030 0.0108 -0.0122 489 HOH A O 4160 O O . HOH I . ? 0.2967 0.3513 0.4191 0.0162 0.0084 -0.0179 490 HOH A O 4161 O O . HOH I . ? 0.6921 0.7016 0.8090 -0.0155 0.0276 0.0019 491 HOH A O 4162 O O . HOH I . ? 0.6306 0.6127 0.6794 0.0405 -0.0057 -0.0411 492 HOH A O 4163 O O . HOH I . ? 0.6940 0.6959 0.8155 -0.0091 0.0076 -0.0197 493 HOH A O 4164 O O . HOH I . ? 0.6794 0.6716 0.7468 0.0228 0.0180 -0.0146 494 HOH A O 4165 O O . HOH I . ? 0.4339 0.4257 0.5082 0.0319 0.0057 -0.0300 495 HOH A O 4166 O O . HOH I . ? 0.4478 0.4751 0.5535 -0.0256 -0.0001 0.0024 496 HOH A O 4167 O O . HOH I . ? 0.3372 0.4069 0.4688 0.0149 0.0090 -0.0164 497 HOH A O 4168 O O . HOH I . ? 0.4069 0.4100 0.5291 -0.0141 0.0156 -0.0027 498 HOH A O 4169 O O . HOH I . ? 0.3571 0.3911 0.4652 0.0160 -0.0056 -0.0326 499 HOH A O 4170 O O . HOH I . ? 0.5464 0.4967 0.5591 0.0610 0.0211 -0.0264 500 HOH A O 4171 O O . HOH I . ? 0.5725 0.5586 0.6380 0.0118 0.0119 -0.0165 501 HOH A O 4172 O O . HOH I . ? 0.5912 0.6380 0.7277 -0.0123 0.0284 -0.0006 502 HOH A O 4173 O O . HOH I . ? 0.7322 0.7210 0.7600 0.0662 0.0032 -0.0302 503 HOH A O 4174 O O . HOH I . ? 0.4396 0.4474 0.5641 -0.0184 0.0199 -0.0030 504 HOH A O 4175 O O . HOH I . ? 0.4340 0.4220 0.5057 0.0077 0.0193 -0.0067 505 HOH A O 4176 O O . HOH I . ? 0.8091 0.6429 0.7161 -0.0019 0.0195 -0.0055 506 HOH A O 4177 O O . HOH I . ? 0.6197 0.6336 0.7223 0.0146 -0.0013 -0.0315 507 HOH A O 4178 O O . HOH I . ? 0.7259 0.6883 0.7360 0.0612 0.0155 -0.0211 508 HOH A O 4179 O O . HOH I . ? 0.5864 0.5525 0.6305 0.0146 0.0211 -0.0071 509 HOH A O 4180 O O . HOH I . ? 0.4443 0.3938 0.4744 0.0077 0.0195 -0.0060 510 HOH A O 4181 O O . HOH I . ? 0.3427 0.3517 0.4324 0.0112 0.0200 -0.0077 511 HOH A O 4182 O O . HOH I . ? 0.3801 0.3398 0.4136 -0.0443 -0.0063 0.0020 512 HOH A O 4183 O O . HOH I . ? 0.3661 0.4024 0.4817 -0.0231 -0.0018 0.0071 513 HOH A O 4184 O O . HOH I . ? 0.7293 0.6895 0.7638 0.0202 0.0137 -0.0188 514 HOH A O 4185 O O . HOH I . ? 0.7341 0.7211 0.7947 0.0175 0.0183 -0.0130 515 HOH A O 4186 O O . HOH I . ? 0.6335 0.6337 0.7164 0.0125 0.0106 -0.0169 516 HOH A O 4187 O O . HOH I . ? 0.6468 0.6584 0.7459 0.0105 0.0093 -0.0162 517 HOH A O 4188 O O . HOH I . ? 0.6044 0.6364 0.7258 -0.0144 0.0019 0.0063 518 HOH A O 4189 O O . HOH I . ? 0.6358 0.6779 0.7123 0.0555 0.0047 -0.0226 519 HOH A O 4190 O O . HOH I . ? 0.6515 0.6900 0.7828 -0.0034 0.0066 0.0017 520 HOH A O 4191 O O . HOH I . ? 0.4519 0.4126 0.4994 -0.0020 0.0177 -0.0024 521 HOH A O 4192 O O . HOH I . ? 0.6662 0.6024 0.6546 0.0751 0.0412 -0.0150 522 HOH A O 4193 O O . HOH I . ? 0.7199 0.7542 0.8288 0.0090 -0.0100 -0.0358 523 HOH A O 4194 O O . HOH I . ? 0.6665 0.6662 0.7129 0.0553 0.0124 -0.0204 524 HOH A O 4195 O O . HOH I . ? 0.7641 0.7604 0.8304 -0.0435 -0.0028 0.0025 525 HOH A O 4196 O O . HOH I . ? 0.4593 0.3664 0.4449 -0.0282 0.0041 -0.0036 526 HOH A O 4197 O O . HOH I . ? 0.4980 0.4480 0.5149 0.0351 0.0147 -0.0207 527 HOH A O 4198 O O . HOH I . ? 0.4823 0.4323 0.5014 -0.0537 -0.0041 0.0004 528 HOH A O 4199 O O . HOH I . ? 0.5069 0.4412 0.5064 -0.0634 -0.0080 0.0018 529 HOH A O 4200 O O . HOH I . ? 0.3826 0.4348 0.4900 0.0221 -0.0106 -0.0339 530 HOH A O 4201 O O . HOH I . ? 0.6440 0.7474 0.8082 -0.0304 -0.0037 -0.0212 531 HOH A O 4202 O O . HOH I . ? 0.4125 0.3936 0.4514 0.0516 0.0034 -0.0330 532 HOH A O 4203 O O . HOH I . ? 0.7826 0.7568 0.8227 -0.0548 -0.0049 0.0031 533 HOH A O 4204 O O . HOH I . ? 0.6068 0.6841 0.7435 0.0132 0.0158 -0.0106 534 HOH A O 4205 O O . HOH I . ? 0.3559 0.3899 0.4817 -0.0059 0.0059 -0.0029 535 HOH A O 4206 O O . HOH I . ? 0.3785 0.3715 0.4940 0.0006 0.0154 -0.0033 536 HOH A O 4207 O O . HOH I . ? 0.4343 0.4329 0.5545 -0.0105 0.0152 -0.0019 537 HOH A O 4208 O O . HOH I . ? 0.4488 0.4020 0.4815 -0.0093 0.0101 -0.0114 538 HOH A O 4209 O O . HOH I . ? 0.5006 0.3809 0.4514 0.0223 0.0242 -0.0098 539 HOH A O 4210 O O . HOH I . ? 0.4580 0.4485 0.5002 0.0538 0.0016 -0.0323 540 HOH A O 4211 O O . HOH I . ? 0.3719 0.3873 0.4371 0.0446 -0.0079 -0.0368 541 HOH A O 4212 O O . HOH I . ? 0.7818 0.7390 0.7966 0.0605 0.0092 -0.0334 542 HOH A O 4213 O O . HOH I . ? 0.8080 0.7519 0.8315 0.0109 0.0298 0.0026 543 HOH A O 4214 O O . HOH I . ? 0.3327 0.3956 0.4550 0.0212 0.0130 -0.0139 544 HOH A O 4215 O O . HOH I . ? 0.3459 0.3834 0.4759 -0.0039 0.0065 -0.0002 545 HOH A O 4216 O O . HOH I . ? 0.5236 0.3747 0.4158 0.1228 0.0462 -0.0280 546 HOH A O 4217 O O . HOH I . ? 0.2843 0.3205 0.3773 0.0348 0.0077 -0.0206 547 HOH A O 4218 O O . HOH I . ? 0.3936 0.4452 0.4905 0.0407 0.0045 -0.0220 548 HOH A O 4219 O O . HOH I . ? 0.3260 0.4089 0.4859 -0.0197 0.0128 -0.0117 549 HOH A O 4220 O O . HOH I . ? 0.3230 0.3978 0.4313 0.0419 0.0013 -0.0218 550 HOH A O 4221 O O . HOH I . ? 0.3239 0.3606 0.4526 0.0009 0.0084 -0.0025 551 HOH A O 4222 O O . HOH I . ? 0.4271 0.4554 0.5245 0.0204 0.0232 -0.0069 552 HOH A O 4223 O O . HOH I . ? 0.4447 0.3762 0.4563 -0.0297 0.0020 -0.0027 553 HOH A O 4224 O O . HOH I . ? 0.5325 0.4982 0.5709 0.0250 0.0127 -0.0190 554 HOH A O 4225 O O . HOH I . ? 0.6011 0.5237 0.6017 0.0044 0.0142 -0.0129 555 HOH A O 4226 O O . HOH I . ? 0.4322 0.3987 0.4828 -0.0160 0.0058 -0.0088 556 HOH A O 4227 O O . HOH I . ? 0.4913 0.4689 0.5042 0.0731 0.0130 -0.0222 557 HOH A O 4228 O O . HOH I . ? 0.3745 0.4244 0.5125 -0.0099 0.0246 -0.0036 558 HOH A O 4229 O O . HOH I . ? 0.3755 0.4111 0.5111 -0.0161 0.0230 -0.0042 559 HOH A O 4230 O O . HOH I . ? 0.4256 0.4931 0.5845 -0.0401 0.0170 -0.0091 560 HOH A O 4231 O O . HOH I . ? 0.5158 0.4740 0.5333 0.0573 0.0119 -0.0306 561 HOH A O 4232 O O . HOH I . ? 0.4393 0.3942 0.5341 -0.0157 0.0181 -0.0124 562 HOH A O 4233 O O . HOH I . ? 0.5533 0.5033 0.5683 -0.0588 -0.0119 0.0045 563 HOH A O 4234 O O . HOH I . ? 0.4800 0.4938 0.6028 0.0020 0.0068 -0.0184 564 HOH A O 4235 O O . HOH I . ? 0.4468 0.4648 0.5756 -0.0056 0.0089 -0.0072 565 HOH A O 4236 O O . HOH I . ? 0.5478 0.5510 0.6063 0.0436 -0.0074 -0.0386 566 HOH A O 4237 O O . HOH I . ? 0.6690 0.6359 0.7280 -0.0029 0.0266 0.0056 567 HOH A O 4238 O O . HOH I . ? 0.4833 0.4959 0.6073 0.0012 0.0083 -0.0153 568 HOH A O 4239 O O . HOH I . ? 0.3653 0.3686 0.4310 0.0364 0.0120 -0.0191 569 HOH A O 4240 O O . HOH I . ? 0.3919 0.3247 0.3831 0.0777 0.0333 -0.0223 570 HOH A O 4241 O O . HOH I . ? 0.6958 0.5487 0.5746 0.1200 0.0377 -0.0301 571 HOH A O 4242 O O . HOH I . ? 0.6245 0.4884 0.5629 0.0048 0.0195 -0.0090 572 HOH A O 4243 O O . HOH I . ? 0.5499 0.5487 0.6455 -0.0149 0.0065 0.0103 573 HOH A O 4244 O O . HOH I . ? 0.5705 0.5092 0.5568 0.0737 0.0052 -0.0396 574 HOH A O 4245 O O . HOH I . ? 0.4444 0.4854 0.5487 0.0246 0.0184 -0.0109 575 HOH A O 4246 O O . HOH I . ? 0.3849 0.4733 0.5336 0.0043 0.0166 -0.0089 576 HOH A O 4247 O O . HOH I . ? 0.5146 0.5460 0.6054 0.0260 -0.0115 -0.0375 577 HOH A O 4248 O O . HOH I . ? 0.3930 0.4331 0.5401 -0.0440 0.0193 -0.0089 578 HOH A O 4249 O O . HOH I . ? 0.4432 0.4627 0.5649 -0.0115 0.0063 -0.0006 579 HOH A O 4250 O O . HOH I . ? 0.4211 0.4144 0.4999 -0.0182 0.0038 -0.0070 580 HOH A O 4251 O O . HOH I . ? 0.3846 0.4133 0.5004 0.0100 0.0010 -0.0262 581 HOH A O 4252 O O . HOH I . ? 0.4732 0.4794 0.5650 0.0179 0.0071 -0.0224 582 HOH A O 4253 O O . HOH I . ? 0.4932 0.5720 0.6148 0.0317 0.0085 -0.0162 583 HOH A O 4254 O O . HOH I . ? 0.5828 0.5243 0.6090 -0.0148 0.0094 -0.0028 584 HOH A O 4255 O O . HOH I . ? 0.5204 0.5710 0.6337 0.0167 -0.0086 -0.0327 585 HOH A O 4256 O O . HOH I . ? 0.5073 0.5408 0.5928 0.0398 0.0167 -0.0136 586 HOH A O 4257 O O . HOH I . ? 0.5857 0.6413 0.6710 -0.0690 -0.0246 0.0252 587 HOH A O 4258 O O . HOH I . ? 0.5032 0.4473 0.5065 0.0632 0.0252 -0.0239 588 HOH A O 4259 O O . HOH I . ? 0.4560 0.4771 0.5332 0.0401 0.0073 -0.0224 589 HOH A O 4260 O O . HOH I . ? 0.5276 0.4384 0.5149 -0.0378 0.0007 -0.0039 590 HOH A O 4261 O O . HOH I . ? 0.4026 0.4047 0.5299 -0.0304 0.0209 -0.0068 591 HOH A O 4262 O O . HOH I . ? 0.4555 0.4223 0.4884 0.0338 0.0190 -0.0140 592 HOH A O 4263 O O . HOH I . ? 0.5527 0.5268 0.5807 0.0515 0.0142 -0.0207 593 HOH A O 4264 O O . HOH I . ? 0.6000 0.5475 0.6196 0.0244 0.0146 -0.0184 594 HOH A O 4265 O O . HOH I . ? 0.6817 0.4827 0.5513 0.0176 0.0282 -0.0079 595 HOH A O 4266 O O . HOH I . ? 0.6659 0.6824 0.7643 0.0167 -0.0046 -0.0343 596 HOH A O 4267 O O . HOH I . ? 0.5221 0.5960 0.6586 0.0067 0.0320 0.0016 597 HOH A O 4268 O O . HOH I . ? 0.4935 0.4532 0.5242 0.0281 0.0152 -0.0203 598 HOH A O 4269 O O . HOH I . ? 0.3687 0.4732 0.5081 0.0232 0.0015 -0.0185 599 HOH A O 4270 O O . HOH I . ? 0.6419 0.6751 0.7719 -0.0047 0.0065 0.0020 600 HOH A O 4271 O O . HOH I . ? 0.4581 0.4843 0.5215 0.0577 0.0039 -0.0249 601 HOH A O 4272 O O . HOH I . ? 0.4858 0.4933 0.5414 0.0512 -0.0029 -0.0338 602 HOH A O 4273 O O . HOH I . ? 0.4475 0.4636 0.5292 0.0275 0.0221 -0.0089 603 HOH A O 4274 O O . HOH I . ? 0.7036 0.4665 0.4750 0.1567 0.0333 -0.0453 604 HOH A O 4275 O O . HOH I . ? 0.5853 0.5682 0.6460 0.0152 0.0247 -0.0044 605 HOH A O 4276 O O . HOH I . ? 0.5186 0.5265 0.6361 0.0017 0.0049 -0.0233 606 HOH A O 4277 O O . HOH I . ? 0.4470 0.4151 0.4921 0.0124 0.0130 -0.0168 607 HOH A O 4278 O O . HOH I . ? 0.4924 0.5739 0.6296 0.0146 0.0058 -0.0179 608 HOH A O 4279 O O . HOH I . ? 0.4358 0.4233 0.4827 0.0397 0.0252 -0.0088 609 HOH A O 4280 O O . HOH I . ? 0.5905 0.4936 0.5258 0.0958 0.0087 -0.0416 610 HOH A O 4281 O O . HOH I . ? 0.5560 0.5662 0.6459 -0.0263 -0.0042 0.0114 611 HOH A O 4282 O O . HOH I . ? 0.4064 0.4664 0.5410 -0.0150 -0.0108 -0.0321 612 HOH A O 4283 O O . HOH I . ? 0.6598 0.6923 0.7907 -0.0013 0.0078 0.0000 613 HOH A O 4284 O O . HOH I . ? 0.5549 0.5544 0.6176 0.0383 -0.0065 -0.0388 614 HOH A O 4285 O O . HOH I . ? 0.4876 0.5212 0.6305 -0.0312 0.0197 -0.0081 615 HOH A O 4286 O O . HOH I . ? 0.4676 0.5018 0.5640 -0.0345 -0.0117 0.0177 616 HOH A O 4287 O O . HOH I . ? 0.5552 0.5836 0.6808 -0.0097 0.0051 0.0022 617 HOH A O 4288 O O . HOH I . ? 0.4304 0.4299 0.5397 0.0073 0.0062 -0.0237 618 HOH A O 4289 O O . HOH I . ? 0.4260 0.4627 0.5065 0.0479 0.0064 -0.0219 619 HOH A O 4290 O O . HOH I . ? 0.6927 0.6367 0.6986 0.0717 0.0320 -0.0209 620 HOH A O 4291 O O . HOH I . ? 0.3701 0.4597 0.4833 0.0461 0.0035 -0.0184 621 HOH A O 4292 O O . HOH I . ? 0.6068 0.5201 0.5586 0.0884 0.0084 -0.0408 622 HOH A O 4293 O O . HOH I . ? 0.5622 0.4610 0.5331 0.0199 0.0211 -0.0116 623 HOH A O 4294 O O . HOH I . ? 0.5285 0.4999 0.5461 -0.0857 -0.0192 0.0116 624 HOH A O 4295 O O . HOH I . ? 0.5388 0.5395 0.6013 0.0346 0.0245 -0.0082 625 HOH A O 4296 O O . HOH I . ? 0.5139 0.4360 0.5158 -0.0077 0.0112 -0.0110 626 HOH A O 4297 O O . HOH I . ? 0.5522 0.5025 0.5825 -0.0330 -0.0008 -0.0004 627 HOH A O 4298 O O . HOH I . ? 0.6545 0.5273 0.5919 0.0353 0.0325 -0.0053 628 HOH A O 4299 O O . HOH I . ? 0.5804 0.5294 0.5874 0.0584 0.0162 -0.0278 629 HOH A O 4300 O O . HOH I . ? 0.4899 0.4742 0.5557 0.0105 0.0190 -0.0077 630 HOH A O 4301 O O . HOH I . ? 0.4662 0.4500 0.5301 0.0028 0.0112 -0.0137 631 HOH A O 4302 O O . HOH I . ? 0.6178 0.6302 0.7408 -0.0106 0.0022 -0.0259 632 HOH A O 4303 O O . HOH I . ? 0.5197 0.4518 0.5140 0.0404 0.0278 -0.0087 633 HOH A O 4304 O O . HOH I . ? 0.4969 0.4663 0.5353 0.0395 0.0183 -0.0215 634 HOH A O 4305 O O . HOH I . ? 0.5308 0.4865 0.5491 0.0469 0.0151 -0.0251 635 HOH A O 4306 O O . HOH I . ? 0.5858 0.5305 0.6082 -0.0009 0.0128 -0.0133 636 HOH A O 4307 O O . HOH I . ? 0.4874 0.5280 0.6164 -0.0095 0.0036 0.0059 637 HOH A O 4308 O O . HOH I . ? 0.4201 0.4254 0.5096 -0.0217 0.0021 -0.0040 638 HOH A O 4309 O O . HOH I . ? 0.5353 0.5848 0.6287 0.0436 0.0124 -0.0160 639 HOH A O 4310 O O . HOH I . ? 0.5032 0.5218 0.6176 0.0080 0.0045 -0.0220 640 HOH A O 4311 O O . HOH I . ? 0.4257 0.3986 0.4776 0.0134 0.0298 0.0005 641 HOH A O 4312 O O . HOH I . ? 0.6093 0.6037 0.7291 -0.0379 0.0095 -0.0203 642 HOH A O 4313 O O . HOH I . ? 0.6616 0.6673 0.7406 -0.0315 -0.0078 0.0134 643 HOH A O 4314 O O . HOH I . ? 0.5926 0.6149 0.7151 -0.0070 -0.0019 -0.0296 644 HOH A O 4315 O O . HOH I . ? 0.5619 0.5918 0.6895 -0.0055 0.0065 0.0051 645 HOH A O 4316 O O . HOH I . ? 0.6455 0.6452 0.7621 0.0054 0.0155 0.0012 646 HOH A O 4317 O O . HOH I . ? 0.5416 0.5616 0.5895 0.0669 -0.0018 -0.0300 647 HOH A O 4318 O O . HOH I . ? 0.6591 0.5577 0.6252 0.0302 0.0289 -0.0063 648 HOH A O 4319 O O . HOH I . ? 0.4956 0.4480 0.5165 0.0304 0.0205 -0.0125 649 HOH A O 4320 O O . HOH I . ? 0.4694 0.5751 0.6290 -0.0031 0.0065 -0.0147 650 HOH A O 4321 O O . HOH I . ? 0.7547 0.7029 0.7747 0.0239 0.0255 -0.0061 651 HOH A O 4322 O O . HOH I . ? 0.6131 0.6594 0.7044 0.0435 0.0079 -0.0198 652 HOH A O 4323 O O . HOH I . ? 0.5348 0.5445 0.6619 -0.0063 0.0097 -0.0127 653 HOH A O 4324 O O . HOH I . ? 0.5015 0.4771 0.5551 -0.0334 0.0006 -0.0031 654 HOH A O 4325 O O . HOH I . ? 0.7758 0.6738 0.7101 0.0948 0.0227 -0.0322 655 HOH A O 4326 O O . HOH I . ? 0.4263 0.4670 0.5579 0.0014 0.0086 0.0006 656 HOH A O 4327 O O . HOH I . ? 0.6490 0.6545 0.7588 0.0070 0.0031 -0.0269 657 HOH A O 4328 O O . HOH I . ? 0.5340 0.5529 0.5964 -0.0585 -0.0237 0.0206 658 HOH A O 4329 O O . HOH I . ? 0.7496 0.5602 0.6324 0.0020 0.0219 -0.0087 659 HOH A O 4330 O O . HOH I . ? 0.4892 0.5472 0.6170 -0.0182 -0.0024 0.0154 660 HOH A O 4331 O O . HOH I . ? 0.6040 0.7118 0.7555 0.0090 0.0023 -0.0176 661 HOH A O 4332 O O . HOH I . ? 0.6614 0.5516 0.5894 0.1049 0.0530 -0.0159 662 HOH A O 4333 O O . HOH I . ? 0.6426 0.5606 0.6342 0.0180 0.0182 -0.0133 663 HOH A O 4334 O O . HOH I . ? 0.6403 0.6839 0.7495 0.0178 0.0303 -0.0011 664 HOH A O 4335 O O . HOH I . ? 0.5294 0.4862 0.5450 0.0444 0.0260 -0.0100 665 HOH A O 4336 O O . HOH I . ? 0.5024 0.5425 0.6265 -0.0140 0.0028 0.0029 666 HOH A O 4337 O O . HOH I . ? 0.7318 0.7048 0.7781 0.0267 0.0116 -0.0216 667 HOH A O 4338 O O . HOH I . ? 0.6530 0.6728 0.7611 -0.0134 0.0018 0.0136 668 HOH A O 4339 O O . HOH I . ? 0.5131 0.5271 0.6409 -0.0036 0.0097 -0.0093 669 HOH A O 4340 O O . HOH I . ? 0.6276 0.5954 0.6711 0.0392 -0.0022 -0.0409 670 HOH A O 4341 O O . HOH I . ? 0.5123 0.6008 0.6655 -0.0182 -0.0060 -0.0251 671 HOH A O 4342 O O . HOH I . ? 0.6201 0.5520 0.6328 -0.0229 0.0057 -0.0073 672 HOH A O 4343 O O . HOH I . ? 0.5079 0.4436 0.4994 0.0729 0.0336 -0.0206 673 HOH A O 4344 O O . HOH I . ? 1.0411 0.7217 0.6541 0.1793 -0.0267 -0.0766 674 HOH A O 4345 O O . HOH I . ? 0.5832 0.5331 0.5839 0.0673 0.0026 -0.0398 675 HOH A O 4346 O O . HOH I . ? 0.6793 0.6857 0.7895 -0.0112 0.0246 0.0009 676 HOH A O 4347 O O . HOH I . ? 0.6587 0.6537 0.7268 0.0210 0.0232 -0.0071 677 HOH A O 4348 O O . HOH I . ? 0.6452 0.7631 0.7963 0.0147 0.0009 -0.0173 678 HOH A O 4349 O O . HOH I . ? 0.6058 0.6974 0.7265 0.0403 0.0082 -0.0150 679 HOH A O 4350 O O . HOH I . ? 0.6977 0.6610 0.7540 -0.0149 0.0131 0.0077 680 HOH A O 4351 O O . HOH I . ? 0.5227 0.4611 0.5462 -0.0070 0.0165 0.0005 681 HOH A O 4352 O O . HOH I . ? 0.4387 0.5334 0.5854 0.0026 -0.0046 -0.0240 682 HOH A O 4353 O O . HOH I . ? 0.5220 0.5659 0.5846 0.0680 -0.0020 -0.0269 683 HOH A O 4354 O O . HOH I . ? 0.5582 0.5605 0.6053 0.0558 0.0216 -0.0125 684 HOH A O 4355 O O . HOH I . ? 0.5567 0.5713 0.6808 -0.0297 -0.0006 -0.0283 685 HOH A O 4356 O O . HOH I . ? 0.5527 0.5894 0.6404 0.0405 0.0109 -0.0181 686 HOH A O 4357 O O . HOH I . ? 0.5291 0.5258 0.6062 0.0000 0.0110 -0.0113 687 HOH A O 4358 O O . HOH I . ? 0.6501 0.5763 0.6549 0.0055 0.0156 -0.0105 688 HOH A O 4359 O O . HOH I . ? 0.7370 0.7250 0.8538 -0.0438 0.0122 -0.0184 689 HOH A O 4360 O O . HOH I . ? 0.6753 0.6822 0.7571 0.0276 0.0217 -0.0100 690 HOH A O 4361 O O . HOH I . ? 0.5487 0.5259 0.5981 0.0297 0.0181 -0.0182 691 HOH A O 4362 O O . HOH I . ? 0.7212 0.6535 0.7215 0.0313 0.0170 -0.0188 692 HOH A O 4363 O O . HOH I . ? 0.6077 0.7153 0.7363 0.0371 -0.0001 -0.0190 693 HOH A O 4364 O O . HOH I . ? 0.3963 0.4936 0.5587 -0.0149 0.0073 -0.0147 694 HOH A O 4365 O O . HOH I . ? 0.8044 0.7768 0.8421 0.0362 0.0145 -0.0186 695 HOH A O 4366 O O . HOH I . ? 0.5598 0.5944 0.6803 -0.0100 0.0051 -0.0017 696 HOH A O 4367 O O . HOH I . ? 0.6725 0.6641 0.7450 0.0107 0.0311 0.0014 697 HOH A O 4368 O O . HOH I . ? 0.4186 0.5044 0.5306 0.0463 0.0073 -0.0162 698 HOH A O 4369 O O . HOH I . ? 0.6245 0.5880 0.6348 0.0579 -0.0107 -0.0465 699 HOH A O 4370 O O . HOH I . ? 0.7568 0.7530 0.8756 -0.0726 0.0132 -0.0169 700 HOH A O 4371 O O . HOH I . ? 0.5001 0.5181 0.6288 -0.0033 0.0084 -0.0107 701 HOH A O 4372 O O . HOH I . ? 0.6010 0.6419 0.7246 -0.0158 0.0002 0.0091 702 HOH A O 4373 O O . HOH I . ? 0.4800 0.5698 0.6006 0.0328 -0.0059 -0.0253 703 HOH A O 4374 O O . HOH I . ? 0.4989 0.5918 0.6427 0.0134 0.0216 -0.0051 704 HOH A O 4375 O O . HOH I . ? 0.5771 0.5876 0.6767 0.0157 0.0064 -0.0224 705 HOH A O 4376 O O . HOH I . ? 0.6198 0.6431 0.6826 0.0503 -0.0096 -0.0365 706 HOH A O 4377 O O . HOH I . ? 0.6639 0.6937 0.7735 0.0017 -0.0110 -0.0369 707 HOH A O 4378 O O . HOH I . ? 0.5568 0.5733 0.6611 -0.0162 0.0032 -0.0046 708 HOH A O 4379 O O . HOH I . ? 0.4938 0.5123 0.6086 0.0070 0.0066 -0.0178 709 HOH A O 4380 O O . HOH J . ? 0.7522 0.7730 0.5644 0.0451 -0.0295 -0.0331 177 HOH B O 4381 O O . HOH J . ? 0.5104 0.5082 0.3506 0.0193 -0.0149 -0.0051 178 HOH B O 4382 O O . HOH J . ? 0.6005 0.4918 0.5435 0.1218 0.0612 -0.0107 179 HOH B O 4383 O O . HOH J . ? 0.5427 0.5580 0.6569 0.0098 0.0064 -0.0203 181 HOH B O 4384 O O . HOH J . ? 0.3735 0.4371 0.2492 0.0460 -0.0008 0.0018 182 HOH B O 4385 O O . HOH J . ? 0.6223 0.6170 0.7041 0.0308 0.0120 -0.0232 183 HOH B O 4386 O O . HOH J . ? 0.4081 0.5079 0.2739 -0.0085 -0.0074 0.0374 184 HOH B O 4387 O O . HOH J . ? 0.3789 0.4779 0.2447 0.0308 0.0104 0.0079 185 HOH B O 4388 O O . HOH J . ? 0.5774 0.3789 0.3944 0.1406 0.0277 -0.0439 187 HOH B O 4389 O O . HOH J . ? 0.4339 0.4806 0.2780 -0.0101 -0.0124 0.0332 188 HOH B O 4390 O O . HOH J . ? 0.3830 0.4422 0.2482 0.0300 -0.0052 0.0010 189 HOH B O 4391 O O . HOH J . ? 0.5236 0.4698 0.2772 -0.0539 -0.0399 0.0581 190 HOH B O 4392 O O . HOH J . ? 0.3460 0.3835 0.2078 0.0418 -0.0024 0.0036 191 HOH B O 4393 O O . HOH J . ? 0.4894 0.3856 0.4295 0.1143 0.0582 -0.0129 192 HOH B O 4394 O O . HOH J . ? 0.4798 0.4879 0.3040 -0.0028 0.0071 0.0023 193 HOH B O 4395 O O . HOH J . ? 0.7035 0.6919 0.4819 -0.0189 0.0096 -0.0032 194 HOH B O 4396 O O . HOH J . ? 0.5348 0.4833 0.5468 0.0730 0.0352 -0.0179 195 HOH B O 4397 O O . HOH J . ? 0.8200 0.5585 0.5403 0.1668 0.0114 -0.0570 196 HOH B O 4398 O O . HOH J . ? 0.5328 0.6290 0.4121 0.0275 -0.0052 -0.0049 197 HOH B O 4399 O O . HOH J . ? 0.5986 0.5791 0.4451 0.0516 -0.0015 0.0065 198 HOH B O 4400 O O . HOH J . ? 0.5965 0.5717 0.4240 0.0132 -0.0177 -0.0030 199 HOH B O 4401 O O . HOH J . ? 0.6734 0.6278 0.4140 0.0461 0.0029 -0.0153 200 HOH B O 4402 O O . HOH J . ? 0.6663 0.5330 0.3769 -0.0351 -0.0484 0.0545 201 HOH B O 4403 O O . HOH J . ? 0.5862 0.5810 0.4384 0.0339 -0.0052 0.0059 202 HOH B O 4404 O O . HOH J . ? 0.5723 0.7858 0.4339 -0.0315 0.0263 0.0034 203 HOH B O 4405 O O . HOH J . ? 0.5340 0.5054 0.3496 0.0535 0.0039 0.0004 204 HOH B O 4406 O O . HOH J . ? 0.6083 0.5911 0.4167 0.0897 -0.0294 -0.0339 205 HOH B O 4407 O O . HOH J . ? 0.5182 0.5346 0.3608 0.0116 0.0085 0.0041 206 HOH B O 4408 O O . HOH J . ? 0.5691 0.5486 0.4139 0.0542 -0.0155 -0.0150 208 HOH B O 4409 O O . HOH J . ? 0.6304 0.5158 0.3708 0.0087 -0.0380 0.0421 209 HOH B O 4410 O O . HOH J . ? 0.5171 0.6738 0.3685 -0.0287 -0.0139 0.0431 210 HOH B O 4411 O O . HOH J . ? 0.6738 0.6297 0.4662 0.0174 0.0064 -0.0026 211 HOH B O 4412 O O . HOH J . ? 0.5247 0.4719 0.3570 0.0415 0.0023 0.0044 212 HOH B O 4413 O O . HOH J . ? 0.4265 0.4795 0.5610 -0.0005 0.0080 0.0061 213 HOH B O 4414 O O . HOH J . ? 0.4707 0.4217 0.2887 0.0187 0.0052 0.0017 214 HOH B O 4415 O O . HOH J . ? 0.5611 0.5246 0.3622 0.0449 0.0049 -0.0027 215 HOH B O 4416 O O . HOH J . ? 0.5066 0.7633 0.3883 -0.0267 0.0283 0.0091 216 HOH B O 4417 O O . HOH J . ? 0.9148 0.6357 0.6294 0.1824 0.0467 -0.0417 219 HOH B O 4418 O O . HOH J . ? 0.6835 0.7647 0.4756 -0.0905 -0.0343 0.0661 221 HOH B O 4419 O O . HOH J . ? 0.6023 0.6783 0.4660 0.0243 -0.0057 0.0034 224 HOH B O 4420 O O . HOH J . ? 0.6833 0.9223 0.5030 0.1306 0.0012 0.0078 227 HOH B O 4421 O O . HOH J . ? 0.5570 0.6581 0.4018 -0.0134 0.0163 0.0047 235 HOH B O 4422 O O . HOH J . ? 0.6090 0.6933 0.3945 0.1293 -0.0132 0.0121 237 HOH B O 4423 O O . HOH J . ? 0.9158 0.6283 0.5513 0.1709 -0.0392 -0.0779 239 HOH B O 4424 O O . HOH J . ? 0.5689 0.5634 0.6489 0.0348 0.0165 -0.0195 246 HOH B O 4425 O O . HOH J . ? 0.8253 1.0422 0.6369 0.1343 -0.0036 -0.0077 248 HOH B O 4426 O O . HOH J . ? 0.6984 0.8102 0.4288 0.1876 -0.0229 0.0169 249 HOH B O 4427 O O . HOH J . ? 0.9016 0.7937 0.4955 0.2420 -0.0574 0.0075 256 HOH B O 4428 O O . HOH J . ? 0.7309 0.8252 0.5025 -0.0013 0.0142 -0.0169 257 HOH B O 4429 O O . HOH J . ? 0.5899 0.8101 0.4805 0.0249 0.0033 0.0239 266 HOH B O 4430 O O . HOH J . ? 0.5371 0.6233 0.4219 0.0404 -0.0040 -0.0041 268 HOH B O 4431 O O . HOH J . ? 0.6078 0.4541 0.4902 0.1309 0.0551 -0.0231 271 HOH B O 4432 O O . HOH J . ? 0.7122 0.6894 0.5104 0.0735 0.0023 -0.0032 272 HOH B O 4433 O O . HOH J . ? 0.7664 0.7695 0.5252 -0.0284 0.0105 -0.0073 273 HOH B O 4434 O O . HOH J . ? 0.6804 0.8988 0.5212 0.0882 0.0061 0.0027 275 HOH B O 4435 O O . HOH J . ? 0.6392 0.4813 0.5240 0.1285 0.0506 -0.0266 276 HOH B O 4436 O O . HOH J . ? 0.7542 0.7700 0.5311 0.0677 0.0047 -0.0128 277 HOH B O 4437 O O . HOH J . ? 0.8969 0.5839 0.4414 0.1286 -0.0768 0.0277 278 HOH B O 4438 O O . HOH J . ? 0.5565 0.5306 0.3751 0.0062 0.0071 0.0018 279 HOH B O 4439 O O . HOH J . ? 0.6214 0.7436 0.4820 0.0471 0.0083 0.0061 280 HOH B O 4440 O O . HOH J . ? 0.6419 0.5986 0.4494 0.0865 -0.0006 0.0043 283 HOH B O 4441 O O . HOH J . ? 0.9243 1.0526 0.7406 0.0477 0.0118 -0.0115 284 HOH B O 4442 O O . HOH J . ? 0.6794 0.6751 0.5287 0.0312 -0.0056 0.0081 287 HOH B O 4443 O O . HOH J . ? 0.8180 0.9927 0.6645 0.0711 -0.0141 -0.0224 294 HOH B O 4444 O O . HOH J . ? 0.7110 0.7366 0.5320 0.0009 -0.0218 -0.0124 299 HOH B O 4445 O O . HOH J . ? 0.5603 0.5262 0.3873 0.0575 0.0017 0.0044 300 HOH B O 4446 O O . HOH J . ? 0.5271 0.5639 0.3805 0.0303 -0.0076 -0.0058 301 HOH B O 4447 O O . HOH J . ? 0.7019 0.9640 0.5299 0.1191 0.0039 0.0015 309 HOH B O 4448 O O . HOH J . ? 0.6160 0.6543 0.4549 0.0066 0.0082 0.0029 310 HOH B O 4449 O O . HOH J . ? 0.6168 0.6231 0.6888 0.0486 0.0344 -0.0030 312 HOH B O 4450 O O . HOH J . ? 0.6438 0.6489 0.7384 0.0211 0.0063 -0.0253 314 HOH B O 4451 O O . HOH J . ? 0.5298 0.5733 0.6495 -0.0152 0.0048 0.0034 318 HOH B O 4452 O O . HOH J . ? 0.7402 0.7826 0.4966 -0.0638 0.0131 -0.0040 320 HOH B O 4453 O O . HOH J . ? 1.0589 0.9200 0.5994 0.2520 -0.0679 0.0228 322 HOH B O 4454 O O . HOH J . ? 0.7468 0.7017 0.5825 0.0195 -0.0114 0.0093 328 HOH B O 4455 O O . HOH J . ? 0.7219 0.8586 0.5670 0.0228 0.0157 -0.0029 332 HOH B O 4456 O O . HOH J . ? 0.9281 0.5611 0.5162 0.1890 -0.0018 -0.0727 333 HOH B O 4457 O O . HOH J . ? 0.7013 0.6677 0.4313 -0.0969 -0.0488 0.0718 335 HOH B O 4458 O O . HOH J . ? 1.0244 0.7775 0.6292 -0.0150 -0.0715 0.0628 340 HOH B O 4459 O O . HOH J . ? 0.7575 0.9141 0.5700 -0.0484 0.0225 -0.0038 341 HOH B O 4460 O O . HOH J . ? 0.6396 0.8741 0.5447 -0.0109 0.0029 0.0455 342 HOH B O 4461 O O . HOH J . ? 0.6860 0.5589 0.6059 0.1180 0.0517 -0.0211 345 HOH B O 4462 O O . HOH J . ? 0.4970 0.5549 0.6307 -0.0082 0.0050 0.0088 346 HOH B O 4463 O O . HOH J . ? 0.8200 0.8389 0.6624 0.0765 -0.0176 -0.0228 351 HOH B O 4464 O O . HOH J . ? 0.9215 0.6918 0.5422 0.0551 -0.0633 0.0460 355 HOH B O 4465 O O . HOH J . ? 0.8199 0.6825 0.7218 0.1360 0.0673 -0.0127 356 HOH B O 4466 O O . HOH J . ? 0.6548 0.7946 0.5199 0.0500 0.0037 0.0129 357 HOH B O 4467 O O . HOH J . ? 0.7841 0.7737 0.6242 0.0148 -0.0112 0.0061 358 HOH B O 4468 O O . HOH J . ? 0.9406 0.8878 0.7376 0.0653 -0.0308 -0.0285 360 HOH B O 4469 O O . HOH J . ? 0.8573 0.9500 0.6865 0.0696 0.0064 -0.0026 363 HOH B O 4470 O O . HOH J . ? 0.6164 0.6398 0.7294 -0.0041 0.0067 -0.0085 365 HOH B O 4471 O O . HOH J . ? 0.4935 0.7815 0.3872 -0.0083 0.0271 0.0036 366 HOH B O 4472 O O . HOH J . ? 0.8245 0.7443 0.5275 -0.1094 -0.0543 0.0681 367 HOH B O 4473 O O . HOH J . ? 0.7719 0.7839 0.8687 0.0219 0.0151 -0.0137 368 HOH B O 4474 O O . HOH J . ? 0.7695 1.0223 0.5520 0.1825 -0.0066 0.0043 372 HOH B O 4475 O O . HOH J . ? 0.7309 0.6438 0.5462 0.0549 -0.0010 0.0033 373 HOH B O 4476 O O . HOH J . ? 0.7909 0.6398 0.5481 -0.0030 -0.0345 0.0105 385 HOH B O 4477 O O . HOH J . ? 0.6641 0.6498 0.7365 0.0337 0.0087 -0.0286 390 HOH B O 4478 O O . HOH J . ? 0.7026 0.7179 0.8096 0.0087 0.0074 -0.0175 391 HOH B O 4479 O O . HOH J . ? 0.7032 0.9756 0.6009 0.0146 0.0235 0.0179 394 HOH B O 4480 O O . HOH J . ? 0.5947 0.9252 0.5159 0.0203 0.0153 0.0174 396 HOH B O 4481 O O . HOH J . ? 0.6874 0.7039 0.4341 -0.1143 -0.0451 0.0695 397 HOH B O 4482 O O . HOH J . ? 0.5580 0.5188 0.5787 0.0707 0.0402 -0.0114 406 HOH B O 4483 O O . HOH J . ? 0.6121 0.5472 0.4385 0.0281 0.0023 0.0025 409 HOH B O 4484 O O . HOH J . ? 0.9069 1.0122 0.7446 -0.0164 0.0144 0.0041 410 HOH B O 4485 O O . HOH J . ? 0.7039 0.5651 0.5706 0.1242 0.0046 -0.0472 416 HOH B O 4486 O O . HOH J . ? 0.6566 0.6071 0.4326 0.0177 0.0059 -0.0054 422 HOH B O 4487 O O . HOH J . ? 0.6412 0.7359 0.4849 -0.0104 0.0149 0.0046 426 HOH B O 4488 O O . HOH J . ? 0.8016 0.8057 0.6002 -0.0270 0.0049 0.0026 429 HOH B O 4489 O O . HOH J . ? 0.6029 0.8563 0.4709 -0.0395 0.0292 0.0042 431 HOH B O 4490 O O . HOH J . ? 0.9103 1.0999 0.7556 0.0264 -0.0107 -0.0119 432 HOH B O 4491 O O . HOH J . ? 0.8876 0.9080 0.6393 0.0690 0.0040 -0.0198 434 HOH B O 4492 O O . HOH J . ? 0.4511 0.3164 0.3617 0.1303 0.0620 -0.0154 435 HOH B O 4493 O O . HOH J . ? 0.6511 0.6150 0.4479 0.0865 0.0002 -0.0007 436 HOH B O 4494 O O . HOH J . ? 0.5481 0.5669 0.6516 0.0221 0.0167 -0.0100 437 HOH B O 4495 O O . HOH J . ? 0.9555 1.0369 0.6691 0.2065 -0.0275 0.0064 446 HOH B O 4496 O O . HOH J . ? 0.7574 0.9558 0.5645 -0.0465 0.0041 0.0029 449 HOH B O 4497 O O . HOH J . ? 0.9226 0.6833 0.4512 0.2612 -0.0753 -0.0105 457 HOH B O 4498 O O . HOH J . ? 0.7626 0.6264 0.6593 0.1293 0.0638 -0.0147 464 HOH B O 4499 O O . HOH J . ? 0.8674 0.8821 0.6134 -0.0834 -0.0095 0.0118 468 HOH B O 4500 O O . HOH J . ? 0.6430 0.9817 0.4993 0.0412 0.0176 0.0038 473 HOH B O 4501 O O . HOH J . ? 1.1146 1.0717 0.8278 -0.1015 -0.0535 0.0783 474 HOH B O 4502 O O . HOH J . ? 0.5210 0.5103 0.3623 0.0511 0.0004 0.0089 477 HOH B O 4503 O O . HOH J . ? 0.8317 1.0329 0.6768 -0.0058 0.0151 0.0037 481 HOH B O 4504 O O . HOH J . ? 0.6632 0.9148 0.4868 0.1022 -0.0042 -0.0156 483 HOH B O 4505 O O . HOH J . ? 0.6439 0.6047 0.3846 -0.0697 -0.0049 0.0079 487 HOH B O 4506 O O . HOH J . ? 0.7234 1.1550 0.5594 0.1419 0.0130 0.0088 490 HOH B O 4507 O O . HOH J . ? 0.9750 0.7166 0.7097 0.1752 0.0415 -0.0415 495 HOH B O 4508 O O . HOH J . ? 0.5924 0.7502 0.4077 -0.0895 -0.0289 0.0643 496 HOH B O 4509 O O . HOH J . ? 0.7839 0.9315 0.6075 -0.0710 -0.0277 0.0741 497 HOH B O 4510 O O . HOH J . ? 0.7189 0.9069 0.5507 0.0851 0.0076 -0.0088 498 HOH B O 4511 O O . HOH J . ? 0.9884 0.9834 0.7023 0.0622 0.0018 -0.0265 499 HOH B O 4512 O O . HOH J . ? 0.6899 0.6353 0.4647 -0.0137 0.0056 -0.0010 500 HOH B O 4513 O O . HOH J . ? 0.7645 0.6862 0.5851 0.0547 -0.0004 0.0036 504 HOH B O 4514 O O . HOH J . ? 0.5964 0.7656 0.4236 -0.0737 -0.0244 0.0581 505 HOH B O 4515 O O . HOH J . ? 0.8517 0.8005 0.5698 -0.0874 -0.0085 0.0108 511 HOH B O 4516 O O . HOH J . ? 1.1656 0.7699 0.7254 0.2050 0.0125 -0.0688 513 HOH B O 4517 O O . HOH J . ? 0.8202 1.0205 0.6551 -0.0192 0.0235 -0.0070 521 HOH B O 4518 O O . HOH J . ? 0.8301 0.9855 0.6878 0.0583 0.0080 0.0035 527 HOH B O 4519 O O . HOH J . ? 0.8381 1.0946 0.6678 0.0934 0.0015 -0.0089 528 HOH B O 4520 O O . HOH J . ? 0.8485 0.8721 0.5607 -0.0509 0.0103 -0.0163 529 HOH B O 4521 O O . HOH J . ? 0.8203 0.9110 0.6771 0.0508 0.0040 0.0102 530 HOH B O 4522 O O . HOH J . ? 0.6913 0.9278 0.5441 0.0434 0.0125 0.0027 532 HOH B O 4523 O O . HOH J . ? 0.8921 0.9114 0.6933 0.0825 0.0029 -0.0049 535 HOH B O 4524 O O . HOH J . ? 0.7416 0.7709 0.5755 -0.0011 0.0104 0.0033 536 HOH B O 4525 O O . HOH J . ? 0.6793 0.8387 0.5159 0.1077 -0.0201 -0.0325 538 HOH B O 4526 O O . HOH J . ? 0.7585 0.6318 0.6706 0.1285 0.0642 -0.0130 539 HOH B O 4527 O O . HOH J . ? 0.6833 0.9289 0.5387 -0.0375 0.0250 0.0071 540 HOH B O 4528 O O . HOH J . ? 0.6818 0.7750 0.5208 -0.0091 0.0127 0.0038 544 HOH B O 4529 O O . HOH J . ? 0.4207 0.3453 0.2156 0.0770 -0.0005 0.0008 545 HOH B O 4530 O O . HOH J . ? 0.7200 0.7073 0.5594 0.0542 -0.0004 0.0092 546 HOH B O 4531 O O . HOH J . ? 0.7489 0.6529 0.5473 0.0584 -0.0003 0.0013 547 HOH B O 4532 O O . HOH J . ? 0.7221 0.7490 0.5272 0.0934 0.0013 -0.0021 549 HOH B O 4533 O O . HOH J . ? 0.7397 0.7165 0.5342 -0.0210 0.0052 0.0020 550 HOH B O 4534 O O . HOH J . ? 0.5150 0.6080 0.3171 0.1071 0.0020 -0.0079 551 HOH B O 4535 O O . HOH J . ? 0.7296 0.6508 0.5410 0.0330 0.0023 0.0015 552 HOH B O 4536 O O . HOH J . ? 0.6195 0.6325 0.7142 0.0262 0.0185 -0.0111 604 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 PRO 1 9 9 PRO PRO A . n A 1 2 GLY 2 10 10 GLY GLY A . n A 1 3 ASP 3 11 11 ASP ASP A . n A 1 4 GLN 4 12 12 GLN GLN A . n A 1 5 ILE 5 13 13 ILE ILE A . n A 1 6 CYS 6 14 14 CYS CYS A . n A 1 7 ILE 7 15 15 ILE ILE A . n A 1 8 GLY 8 16 16 GLY GLY A . n A 1 9 TYR 9 17 17 TYR TYR A . n A 1 10 HIS 10 18 18 HIS HIS A . n A 1 11 ALA 11 19 19 ALA ALA A . n A 1 12 ASN 12 20 20 ASN ASN A . n A 1 13 ASN 13 21 21 ASN ASN A . n A 1 14 SER 14 22 22 SER SER A . n A 1 15 THR 15 23 23 THR THR A . n A 1 16 GLU 16 24 24 GLU GLU A . n A 1 17 LYS 17 25 25 LYS LYS A . n A 1 18 VAL 18 26 26 VAL VAL A . n A 1 19 ASP 19 27 27 ASP ASP A . n A 1 20 THR 20 28 28 THR THR A . n A 1 21 ILE 21 29 29 ILE ILE A . n A 1 22 LEU 22 30 30 LEU LEU A . n A 1 23 GLU 23 31 31 GLU GLU A . n A 1 24 ARG 24 32 32 ARG ARG A . n A 1 25 ASN 25 33 33 ASN ASN A . n A 1 26 VAL 26 34 34 VAL VAL A . n A 1 27 THR 27 35 35 THR THR A . n A 1 28 VAL 28 36 36 VAL VAL A . n A 1 29 THR 29 37 37 THR THR A . n A 1 30 HIS 30 38 38 HIS HIS A . n A 1 31 ALA 31 39 39 ALA ALA A . n A 1 32 LYS 32 40 40 LYS LYS A . n A 1 33 ASP 33 41 41 ASP ASP A . n A 1 34 ILE 34 42 42 ILE ILE A . n A 1 35 LEU 35 43 43 LEU LEU A . n A 1 36 GLU 36 44 44 GLU GLU A . n A 1 37 LYS 37 45 45 LYS LYS A . n A 1 38 THR 38 46 46 THR THR A . n A 1 39 HIS 39 47 47 HIS HIS A . n A 1 40 ASN 40 48 48 ASN ASN A . n A 1 41 GLY 41 49 49 GLY GLY A . n A 1 42 LYS 42 50 50 LYS LYS A . n A 1 43 LEU 43 51 51 LEU LEU A . n A 1 44 CYS 44 52 52 CYS CYS A . n A 1 45 LYS 45 53 53 LYS LYS A . n A 1 46 LEU 46 53 53 LEU LEU A A n A 1 47 ASN 47 54 54 ASN ASN A . n A 1 48 GLY 48 55 55 GLY GLY A . n A 1 49 ILE 49 56 56 ILE ILE A . n A 1 50 PRO 50 57 57 PRO PRO A . n A 1 51 PRO 51 58 58 PRO PRO A . n A 1 52 LEU 52 59 59 LEU LEU A . n A 1 53 GLU 53 60 60 GLU GLU A . n A 1 54 LEU 54 61 61 LEU LEU A . n A 1 55 GLY 55 62 62 GLY GLY A . n A 1 56 ASP 56 63 63 ASP ASP A . n A 1 57 CYS 57 64 64 CYS CYS A . n A 1 58 SER 58 65 65 SER SER A . n A 1 59 ILE 59 66 66 ILE ILE A . n A 1 60 ALA 60 67 67 ALA ALA A . n A 1 61 GLY 61 68 68 GLY GLY A . n A 1 62 TRP 62 69 69 TRP TRP A . n A 1 63 LEU 63 70 70 LEU LEU A . n A 1 64 LEU 64 71 71 LEU LEU A . n A 1 65 GLY 65 72 72 GLY GLY A . n A 1 66 ASN 66 73 73 ASN ASN A . n A 1 67 PRO 67 74 74 PRO PRO A . n A 1 68 GLU 68 75 75 GLU GLU A . n A 1 69 CYS 69 76 76 CYS CYS A . n A 1 70 ASP 70 77 77 ASP ASP A . n A 1 71 ARG 71 78 78 ARG ARG A . n A 1 72 LEU 72 79 79 LEU LEU A . n A 1 73 LEU 73 80 80 LEU LEU A . n A 1 74 SER 74 81 81 SER SER A . n A 1 75 VAL 75 81 81 VAL VAL A A n A 1 76 PRO 76 82 82 PRO PRO A . n A 1 77 GLU 77 83 83 GLU GLU A . n A 1 78 TRP 78 84 84 TRP TRP A . n A 1 79 SER 79 85 85 SER SER A . n A 1 80 TYR 80 86 86 TYR TYR A . n A 1 81 ILE 81 87 87 ILE ILE A . n A 1 82 MET 82 88 88 MET MET A . n A 1 83 GLU 83 89 89 GLU GLU A . n A 1 84 LYS 84 90 90 LYS LYS A . n A 1 85 GLU 85 91 91 GLU GLU A . n A 1 86 ASN 86 92 92 ASN ASN A . n A 1 87 PRO 87 93 93 PRO PRO A . n A 1 88 ARG 88 94 94 ARG ARG A . n A 1 89 ASP 89 95 95 ASP ASP A . n A 1 90 GLY 90 95 95 GLY GLY A A n A 1 91 LEU 91 96 96 LEU LEU A . n A 1 92 CYS 92 97 97 CYS CYS A . n A 1 93 TYR 93 98 98 TYR TYR A . n A 1 94 PRO 94 99 99 PRO PRO A . n A 1 95 GLY 95 100 100 GLY GLY A . n A 1 96 SER 96 101 101 SER SER A . n A 1 97 PHE 97 102 102 PHE PHE A . n A 1 98 ASN 98 103 103 ASN ASN A . n A 1 99 ASP 99 104 104 ASP ASP A . n A 1 100 TYR 100 105 105 TYR TYR A . n A 1 101 GLU 101 106 106 GLU GLU A . n A 1 102 GLU 102 107 107 GLU GLU A . n A 1 103 LEU 103 108 108 LEU LEU A . n A 1 104 LYS 104 109 109 LYS LYS A . n A 1 105 HIS 105 110 110 HIS HIS A . n A 1 106 LEU 106 111 111 LEU LEU A . n A 1 107 LEU 107 112 112 LEU LEU A . n A 1 108 SER 108 113 113 SER SER A . n A 1 109 SER 109 114 114 SER SER A . n A 1 110 VAL 110 115 115 VAL VAL A . n A 1 111 LYS 111 116 116 LYS LYS A . n A 1 112 HIS 112 116 116 HIS HIS A A n A 1 113 PHE 113 116 116 PHE PHE A B n A 1 114 GLU 114 116 116 GLU GLU A C n A 1 115 LYS 115 117 117 LYS LYS A . n A 1 116 VAL 116 118 118 VAL VAL A . n A 1 117 LYS 117 119 119 LYS LYS A . n A 1 118 ILE 118 120 120 ILE ILE A . n A 1 119 LEU 119 121 121 LEU LEU A . n A 1 120 PRO 120 122 122 PRO PRO A . n A 1 121 LYS 121 123 123 LYS LYS A . n A 1 122 ASP 122 125 125 ASP ASP A . n A 1 123 ARG 123 126 126 ARG ARG A . n A 1 124 TRP 124 127 127 TRP TRP A . n A 1 125 THR 125 128 128 THR THR A . n A 1 126 GLN 126 129 129 GLN GLN A . n A 1 127 HIS 127 130 130 HIS HIS A . n A 1 128 THR 128 131 131 THR THR A . n A 1 129 THR 129 132 132 THR THR A . n A 1 130 THR 130 133 133 THR THR A . n A 1 131 GLY 131 134 134 GLY GLY A . n A 1 132 GLY 132 135 135 GLY GLY A . n A 1 133 SER 133 136 136 SER SER A . n A 1 134 ARG 134 137 137 ARG ARG A . n A 1 135 ALA 135 138 138 ALA ALA A . n A 1 136 CYS 136 139 139 CYS CYS A . n A 1 137 ALA 137 140 140 ALA ALA A . n A 1 138 VAL 138 141 141 VAL VAL A . n A 1 139 SER 139 142 142 SER SER A . n A 1 140 GLY 140 143 143 GLY GLY A . n A 1 141 ASN 141 144 144 ASN ASN A . n A 1 142 PRO 142 145 145 PRO PRO A . n A 1 143 SER 143 146 146 SER SER A . n A 1 144 PHE 144 147 147 PHE PHE A . n A 1 145 PHE 145 148 148 PHE PHE A . n A 1 146 ARG 146 149 149 ARG ARG A . n A 1 147 ASN 147 150 150 ASN ASN A . n A 1 148 MET 148 151 151 MET MET A . n A 1 149 VAL 149 152 152 VAL VAL A . n A 1 150 TRP 150 153 153 TRP TRP A . n A 1 151 LEU 151 154 154 LEU LEU A . n A 1 152 THR 152 155 155 THR THR A . n A 1 153 GLU 153 156 156 GLU GLU A . n A 1 154 LYS 154 157 157 LYS LYS A . n A 1 155 GLY 155 158 158 GLY GLY A . n A 1 156 SER 156 159 159 SER SER A . n A 1 157 ASN 157 160 160 ASN ASN A . n A 1 158 TYR 158 161 161 TYR TYR A . n A 1 159 PRO 159 162 162 PRO PRO A . n A 1 160 VAL 160 163 163 VAL VAL A . n A 1 161 ALA 161 164 164 ALA ALA A . n A 1 162 LYS 162 165 165 LYS LYS A . n A 1 163 GLY 163 166 166 GLY GLY A . n A 1 164 SER 164 167 167 SER SER A . n A 1 165 TYR 165 168 168 TYR TYR A . n A 1 166 ASN 166 169 169 ASN ASN A . n A 1 167 ASN 167 170 170 ASN ASN A . n A 1 168 THR 168 171 171 THR THR A . n A 1 169 SER 169 172 172 SER SER A . n A 1 170 GLY 170 173 173 GLY GLY A . n A 1 171 GLU 171 174 174 GLU GLU A . n A 1 172 GLN 172 175 175 GLN GLN A . n A 1 173 MET 173 176 176 MET MET A . n A 1 174 LEU 174 177 177 LEU LEU A . n A 1 175 ILE 175 178 178 ILE ILE A . n A 1 176 ILE 176 179 179 ILE ILE A . n A 1 177 TRP 177 180 180 TRP TRP A . n A 1 178 GLY 178 181 181 GLY GLY A . n A 1 179 VAL 179 182 182 VAL VAL A . n A 1 180 HIS 180 183 183 HIS HIS A . n A 1 181 HIS 181 184 184 HIS HIS A . n A 1 182 PRO 182 185 185 PRO PRO A . n A 1 183 ASN 183 186 186 ASN ASN A . n A 1 184 ASP 184 187 187 ASP ASP A . n A 1 185 GLU 185 188 188 GLU GLU A . n A 1 186 THR 186 189 189 THR THR A . n A 1 187 GLU 187 190 190 GLU GLU A . n A 1 188 GLN 188 191 191 GLN GLN A . n A 1 189 ARG 189 192 192 ARG ARG A . n A 1 190 THR 190 193 193 THR THR A . n A 1 191 LEU 191 194 194 LEU LEU A . n A 1 192 TYR 192 195 195 TYR TYR A . n A 1 193 GLN 193 196 196 GLN GLN A . n A 1 194 ASN 194 197 197 ASN ASN A . n A 1 195 VAL 195 198 198 VAL VAL A . n A 1 196 GLY 196 199 199 GLY GLY A . n A 1 197 THR 197 200 200 THR THR A . n A 1 198 TYR 198 201 201 TYR TYR A . n A 1 199 VAL 199 202 202 VAL VAL A . n A 1 200 SER 200 203 203 SER SER A . n A 1 201 VAL 201 204 204 VAL VAL A . n A 1 202 GLY 202 205 205 GLY GLY A . n A 1 203 THR 203 206 206 THR THR A . n A 1 204 SER 204 207 207 SER SER A . n A 1 205 THR 205 208 208 THR THR A . n A 1 206 LEU 206 209 209 LEU LEU A . n A 1 207 ASN 207 210 210 ASN ASN A . n A 1 208 LYS 208 211 211 LYS LYS A . n A 1 209 ARG 209 212 212 ARG ARG A . n A 1 210 SER 210 213 213 SER SER A . n A 1 211 THR 211 214 214 THR THR A . n A 1 212 PRO 212 215 215 PRO PRO A . n A 1 213 GLU 213 216 216 GLU GLU A . n A 1 214 ILE 214 217 217 ILE ILE A . n A 1 215 ALA 215 218 218 ALA ALA A . n A 1 216 THR 216 219 219 THR THR A . n A 1 217 ARG 217 220 220 ARG ARG A . n A 1 218 PRO 218 221 221 PRO PRO A . n A 1 219 LYS 219 222 222 LYS LYS A . n A 1 220 VAL 220 223 223 VAL VAL A . n A 1 221 ASN 221 224 224 ASN ASN A . n A 1 222 GLY 222 225 225 GLY GLY A . n A 1 223 GLN 223 226 226 GLN GLN A . n A 1 224 GLY 224 227 227 GLY GLY A . n A 1 225 GLY 225 228 228 GLY GLY A . n A 1 226 ARG 226 229 229 ARG ARG A . n A 1 227 MET 227 230 230 MET MET A . n A 1 228 GLU 228 231 231 GLU GLU A . n A 1 229 PHE 229 232 232 PHE PHE A . n A 1 230 SER 230 233 233 SER SER A . n A 1 231 TRP 231 234 234 TRP TRP A . n A 1 232 THR 232 235 235 THR THR A . n A 1 233 LEU 233 236 236 LEU LEU A . n A 1 234 LEU 234 237 237 LEU LEU A . n A 1 235 ASP 235 238 238 ASP ASP A . n A 1 236 MET 236 239 239 MET MET A . n A 1 237 TRP 237 240 240 TRP TRP A . n A 1 238 ASP 238 241 241 ASP ASP A . n A 1 239 THR 239 242 242 THR THR A . n A 1 240 ILE 240 243 243 ILE ILE A . n A 1 241 ASN 241 244 244 ASN ASN A . n A 1 242 PHE 242 245 245 PHE PHE A . n A 1 243 GLU 243 246 246 GLU GLU A . n A 1 244 SER 244 247 247 SER SER A . n A 1 245 THR 245 248 248 THR THR A . n A 1 246 GLY 246 249 249 GLY GLY A . n A 1 247 ASN 247 250 250 ASN ASN A . n A 1 248 LEU 248 251 251 LEU LEU A . n A 1 249 ILE 249 252 252 ILE ILE A . n A 1 250 ALA 250 253 253 ALA ALA A . n A 1 251 PRO 251 254 254 PRO PRO A . n A 1 252 GLU 252 255 255 GLU GLU A . n A 1 253 TYR 253 256 256 TYR TYR A . n A 1 254 GLY 254 257 257 GLY GLY A . n A 1 255 PHE 255 258 258 PHE PHE A . n A 1 256 LYS 256 259 259 LYS LYS A . n A 1 257 ILE 257 260 260 ILE ILE A . n A 1 258 SER 258 261 261 SER SER A . n A 1 259 LYS 259 262 262 LYS LYS A . n A 1 260 ARG 260 263 263 ARG ARG A . n A 1 261 GLY 261 263 263 GLY GLY A A n A 1 262 SER 262 264 264 SER SER A . n A 1 263 SER 263 265 265 SER SER A . n A 1 264 GLY 264 266 266 GLY GLY A . n A 1 265 ILE 265 267 267 ILE ILE A . n A 1 266 MET 266 268 268 MET MET A . n A 1 267 LYS 267 269 269 LYS LYS A . n A 1 268 THR 268 270 270 THR THR A . n A 1 269 GLU 269 271 271 GLU GLU A . n A 1 270 GLY 270 272 272 GLY GLY A . n A 1 271 THR 271 273 273 THR THR A . n A 1 272 LEU 272 274 274 LEU LEU A . n A 1 273 GLU 273 275 275 GLU GLU A . n A 1 274 ASN 274 276 276 ASN ASN A . n A 1 275 CYS 275 277 277 CYS CYS A . n A 1 276 GLU 276 278 278 GLU GLU A . n A 1 277 THR 277 279 279 THR THR A . n A 1 278 LYS 278 280 280 LYS LYS A . n A 1 279 CYS 279 281 281 CYS CYS A . n A 1 280 GLN 280 282 282 GLN GLN A . n A 1 281 THR 281 283 283 THR THR A . n A 1 282 PRO 282 284 284 PRO PRO A . n A 1 283 LEU 283 285 285 LEU LEU A . n A 1 284 GLY 284 286 286 GLY GLY A . n A 1 285 ALA 285 287 287 ALA ALA A . n A 1 286 ILE 286 288 288 ILE ILE A . n A 1 287 ASN 287 289 289 ASN ASN A . n A 1 288 THR 288 290 290 THR THR A . n A 1 289 THR 289 291 291 THR THR A . n A 1 290 LEU 290 292 292 LEU LEU A . n A 1 291 PRO 291 293 293 PRO PRO A . n A 1 292 PHE 292 294 294 PHE PHE A . n A 1 293 HIS 293 295 295 HIS HIS A . n A 1 294 ASN 294 296 296 ASN ASN A . n A 1 295 VAL 295 297 297 VAL VAL A . n A 1 296 HIS 296 298 298 HIS HIS A . n A 1 297 PRO 297 299 299 PRO PRO A . n A 1 298 LEU 298 300 300 LEU LEU A . n A 1 299 THR 299 301 301 THR THR A . n A 1 300 ILE 300 302 302 ILE ILE A . n A 1 301 GLY 301 303 303 GLY GLY A . n A 1 302 GLU 302 304 304 GLU GLU A . n A 1 303 CYS 303 305 305 CYS CYS A . n A 1 304 PRO 304 306 306 PRO PRO A . n A 1 305 LYS 305 307 307 LYS LYS A . n A 1 306 TYR 306 308 308 TYR TYR A . n A 1 307 VAL 307 309 309 VAL VAL A . n A 1 308 LYS 308 310 310 LYS LYS A . n A 1 309 SER 309 311 311 SER SER A . n A 1 310 GLU 310 312 312 GLU GLU A . n A 1 311 LYS 311 313 313 LYS LYS A . n A 1 312 LEU 312 314 314 LEU LEU A . n A 1 313 VAL 313 315 315 VAL VAL A . n A 1 314 LEU 314 316 316 LEU LEU A . n A 1 315 ALA 315 317 317 ALA ALA A . n A 1 316 THR 316 318 318 THR THR A . n A 1 317 GLY 317 319 319 GLY GLY A . n A 1 318 LEU 318 320 320 LEU LEU A . n A 1 319 ARG 319 321 321 ARG ARG A . n A 1 320 ASN 320 322 322 ASN ASN A . n A 1 321 VAL 321 323 323 VAL VAL A . n A 1 322 PRO 322 324 324 PRO PRO A . n A 1 323 GLN 323 325 325 GLN GLN A . n A 1 324 ILE 324 326 326 ILE ILE A . n A 1 325 GLU 325 327 ? ? ? A . n A 1 326 SER 326 328 ? ? ? A . n A 1 327 ARG 327 329 ? ? ? A . n B 2 1 GLY 1 1 1 GLY GLY B . n B 2 2 LEU 2 2 2 LEU LEU B . n B 2 3 PHE 3 3 3 PHE PHE B . n B 2 4 GLY 4 4 4 GLY GLY B . n B 2 5 ALA 5 5 5 ALA ALA B . n B 2 6 ILE 6 6 6 ILE ILE B . n B 2 7 ALA 7 7 7 ALA ALA B . n B 2 8 GLY 8 8 8 GLY GLY B . n B 2 9 PHE 9 9 9 PHE PHE B . n B 2 10 ILE 10 10 10 ILE ILE B . n B 2 11 GLU 11 11 11 GLU GLU B . n B 2 12 GLY 12 12 12 GLY GLY B . n B 2 13 GLY 13 13 13 GLY GLY B . n B 2 14 TRP 14 14 14 TRP TRP B . n B 2 15 GLN 15 15 15 GLN GLN B . n B 2 16 GLY 16 16 16 GLY GLY B . n B 2 17 MET 17 17 17 MET MET B . n B 2 18 VAL 18 18 18 VAL VAL B . n B 2 19 ASP 19 19 19 ASP ASP B . n B 2 20 GLY 20 20 20 GLY GLY B . n B 2 21 TRP 21 21 21 TRP TRP B . n B 2 22 TYR 22 22 22 TYR TYR B . n B 2 23 GLY 23 23 23 GLY GLY B . n B 2 24 TYR 24 24 24 TYR TYR B . n B 2 25 HIS 25 25 25 HIS HIS B . n B 2 26 HIS 26 26 26 HIS HIS B . n B 2 27 SER 27 27 27 SER SER B . n B 2 28 ASN 28 28 28 ASN ASN B . n B 2 29 ASP 29 29 29 ASP ASP B . n B 2 30 GLN 30 30 30 GLN GLN B . n B 2 31 GLY 31 31 31 GLY GLY B . n B 2 32 SER 32 32 32 SER SER B . n B 2 33 GLY 33 33 33 GLY GLY B . n B 2 34 TYR 34 34 34 TYR TYR B . n B 2 35 ALA 35 35 35 ALA ALA B . n B 2 36 ALA 36 36 36 ALA ALA B . n B 2 37 ASP 37 37 37 ASP ASP B . n B 2 38 LYS 38 38 38 LYS LYS B . n B 2 39 GLU 39 39 39 GLU GLU B . n B 2 40 SER 40 40 40 SER SER B . n B 2 41 THR 41 41 41 THR THR B . n B 2 42 GLN 42 42 42 GLN GLN B . n B 2 43 LYS 43 43 43 LYS LYS B . n B 2 44 ALA 44 44 44 ALA ALA B . n B 2 45 PHE 45 45 45 PHE PHE B . n B 2 46 ASP 46 46 46 ASP ASP B . n B 2 47 GLY 47 47 47 GLY GLY B . n B 2 48 ILE 48 48 48 ILE ILE B . n B 2 49 THR 49 49 49 THR THR B . n B 2 50 ASN 50 50 50 ASN ASN B . n B 2 51 LYS 51 51 51 LYS LYS B . n B 2 52 VAL 52 52 52 VAL VAL B . n B 2 53 ASN 53 53 53 ASN ASN B . n B 2 54 SER 54 54 54 SER SER B . n B 2 55 VAL 55 55 55 VAL VAL B . n B 2 56 ILE 56 56 56 ILE ILE B . n B 2 57 GLU 57 57 57 GLU GLU B . n B 2 58 LYS 58 58 58 LYS LYS B . n B 2 59 MET 59 59 59 MET MET B . n B 2 60 ASN 60 60 60 ASN ASN B . n B 2 61 THR 61 61 61 THR THR B . n B 2 62 GLN 62 62 62 GLN GLN B . n B 2 63 PHE 63 63 63 PHE PHE B . n B 2 64 GLU 64 64 64 GLU GLU B . n B 2 65 ALA 65 65 65 ALA ALA B . n B 2 66 VAL 66 66 66 VAL VAL B . n B 2 67 GLY 67 67 67 GLY GLY B . n B 2 68 LYS 68 68 68 LYS LYS B . n B 2 69 GLU 69 69 69 GLU GLU B . n B 2 70 PHE 70 70 70 PHE PHE B . n B 2 71 SER 71 71 71 SER SER B . n B 2 72 ASN 72 72 72 ASN ASN B . n B 2 73 LEU 73 73 73 LEU LEU B . n B 2 74 GLU 74 74 74 GLU GLU B . n B 2 75 ARG 75 75 75 ARG ARG B . n B 2 76 ARG 76 76 76 ARG ARG B . n B 2 77 LEU 77 77 77 LEU LEU B . n B 2 78 GLU 78 78 78 GLU GLU B . n B 2 79 ASN 79 79 79 ASN ASN B . n B 2 80 LEU 80 80 80 LEU LEU B . n B 2 81 ASN 81 81 81 ASN ASN B . n B 2 82 LYS 82 82 82 LYS LYS B . n B 2 83 LYS 83 83 83 LYS LYS B . n B 2 84 MET 84 84 84 MET MET B . n B 2 85 GLU 85 85 85 GLU GLU B . n B 2 86 ASP 86 86 86 ASP ASP B . n B 2 87 GLY 87 87 87 GLY GLY B . n B 2 88 PHE 88 88 88 PHE PHE B . n B 2 89 LEU 89 89 89 LEU LEU B . n B 2 90 ASP 90 90 90 ASP ASP B . n B 2 91 VAL 91 91 91 VAL VAL B . n B 2 92 TRP 92 92 92 TRP TRP B . n B 2 93 THR 93 93 93 THR THR B . n B 2 94 TYR 94 94 94 TYR TYR B . n B 2 95 ASN 95 95 95 ASN ASN B . n B 2 96 ALA 96 96 96 ALA ALA B . n B 2 97 GLU 97 97 97 GLU GLU B . n B 2 98 LEU 98 98 98 LEU LEU B . n B 2 99 LEU 99 99 99 LEU LEU B . n B 2 100 VAL 100 100 100 VAL VAL B . n B 2 101 LEU 101 101 101 LEU LEU B . n B 2 102 MET 102 102 102 MET MET B . n B 2 103 GLU 103 103 103 GLU GLU B . n B 2 104 ASN 104 104 104 ASN ASN B . n B 2 105 GLU 105 105 105 GLU GLU B . n B 2 106 HIS 106 106 106 HIS HIS B . n B 2 107 THR 107 107 107 THR THR B . n B 2 108 LEU 108 108 108 LEU LEU B . n B 2 109 ASP 109 109 109 ASP ASP B . n B 2 110 PHE 110 110 110 PHE PHE B . n B 2 111 HIS 111 111 111 HIS HIS B . n B 2 112 ASP 112 112 112 ASP ASP B . n B 2 113 SER 113 113 113 SER SER B . n B 2 114 ASN 114 114 114 ASN ASN B . n B 2 115 VAL 115 115 115 VAL VAL B . n B 2 116 LYS 116 116 116 LYS LYS B . n B 2 117 ASN 117 117 117 ASN ASN B . n B 2 118 LEU 118 118 118 LEU LEU B . n B 2 119 TYR 119 119 119 TYR TYR B . n B 2 120 ASP 120 120 120 ASP ASP B . n B 2 121 LYS 121 121 121 LYS LYS B . n B 2 122 VAL 122 122 122 VAL VAL B . n B 2 123 ARG 123 123 123 ARG ARG B . n B 2 124 MET 124 124 124 MET MET B . n B 2 125 GLN 125 125 125 GLN GLN B . n B 2 126 LEU 126 126 126 LEU LEU B . n B 2 127 ARG 127 127 127 ARG ARG B . n B 2 128 ASP 128 128 128 ASP ASP B . n B 2 129 ASN 129 129 129 ASN ASN B . n B 2 130 VAL 130 130 130 VAL VAL B . n B 2 131 LYS 131 131 131 LYS LYS B . n B 2 132 GLU 132 132 132 GLU GLU B . n B 2 133 LEU 133 133 133 LEU LEU B . n B 2 134 GLY 134 134 134 GLY GLY B . n B 2 135 ASN 135 135 135 ASN ASN B . n B 2 136 GLY 136 136 136 GLY GLY B . n B 2 137 CYS 137 137 137 CYS CYS B . n B 2 138 PHE 138 138 138 PHE PHE B . n B 2 139 GLU 139 139 139 GLU GLU B . n B 2 140 PHE 140 140 140 PHE PHE B . n B 2 141 TYR 141 141 141 TYR TYR B . n B 2 142 HIS 142 142 142 HIS HIS B . n B 2 143 LYS 143 143 143 LYS LYS B . n B 2 144 CYS 144 144 144 CYS CYS B . n B 2 145 ASP 145 145 145 ASP ASP B . n B 2 146 ASP 146 146 146 ASP ASP B . n B 2 147 GLU 147 147 147 GLU GLU B . n B 2 148 CYS 148 148 148 CYS CYS B . n B 2 149 MET 149 149 149 MET MET B . n B 2 150 ASN 150 150 150 ASN ASN B . n B 2 151 SER 151 151 151 SER SER B . n B 2 152 VAL 152 152 152 VAL VAL B . n B 2 153 LYS 153 153 153 LYS LYS B . n B 2 154 ASN 154 154 154 ASN ASN B . n B 2 155 GLY 155 155 155 GLY GLY B . n B 2 156 THR 156 156 156 THR THR B . n B 2 157 TYR 157 157 157 TYR TYR B . n B 2 158 ASP 158 158 158 ASP ASP B . n B 2 159 TYR 159 159 159 TYR TYR B . n B 2 160 PRO 160 160 160 PRO PRO B . n B 2 161 LYS 161 161 161 LYS LYS B . n B 2 162 TYR 162 162 162 TYR TYR B . n B 2 163 GLU 163 163 163 GLU GLU B . n B 2 164 GLU 164 164 164 GLU GLU B . n B 2 165 GLU 165 165 165 GLU GLU B . n B 2 166 SER 166 166 166 SER SER B . n B 2 167 LYS 167 167 167 LYS LYS B . n B 2 168 LEU 168 168 168 LEU LEU B . n B 2 169 ASN 169 169 169 ASN ASN B . n B 2 170 ARG 170 170 170 ARG ARG B . n B 2 171 ASN 171 171 171 ASN ASN B . n B 2 172 GLU 172 172 172 GLU GLU B . n B 2 173 ILE 173 173 ? ? ? B . n B 2 174 LYS 174 174 ? ? ? 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 3 NAG 1 330 330 NAG NAG A . D 3 NAG 2 331 331 NAG NAG A . E 3 NAG 1 332 332 NAG NAG A . F 4 EDO 1 1 1 EDO EDO A . G 3 NAG 1 175 175 NAG NAG B . H 5 PEG 1 176 176 PEG PEG B . I 6 HOH 1 2 2 HOH HOH A . I 6 HOH 2 3 3 HOH HOH A . I 6 HOH 3 4 4 HOH HOH A . I 6 HOH 4 5 5 HOH HOH A . I 6 HOH 5 6 6 HOH HOH A . I 6 HOH 6 8 8 HOH HOH A . I 6 HOH 7 333 333 HOH HOH A . I 6 HOH 8 334 334 HOH HOH A . I 6 HOH 9 335 335 HOH HOH A . I 6 HOH 10 336 336 HOH HOH A . I 6 HOH 11 337 337 HOH HOH A . I 6 HOH 12 338 338 HOH HOH A . I 6 HOH 13 339 339 HOH HOH A . I 6 HOH 14 340 340 HOH HOH A . I 6 HOH 15 341 341 HOH HOH A . I 6 HOH 16 342 342 HOH HOH A . I 6 HOH 17 343 343 HOH HOH A . I 6 HOH 18 344 344 HOH HOH A . I 6 HOH 19 345 345 HOH HOH A . I 6 HOH 20 346 346 HOH HOH A . I 6 HOH 21 347 347 HOH HOH A . I 6 HOH 22 348 348 HOH HOH A . I 6 HOH 23 349 349 HOH HOH A . I 6 HOH 24 350 350 HOH HOH A . I 6 HOH 25 351 351 HOH HOH A . I 6 HOH 26 352 352 HOH HOH A . I 6 HOH 27 353 353 HOH HOH A . I 6 HOH 28 354 354 HOH HOH A . I 6 HOH 29 355 355 HOH HOH A . I 6 HOH 30 356 356 HOH HOH A . I 6 HOH 31 357 357 HOH HOH A . I 6 HOH 32 358 358 HOH HOH A . I 6 HOH 33 359 359 HOH HOH A . I 6 HOH 34 360 360 HOH HOH A . I 6 HOH 35 361 361 HOH HOH A . I 6 HOH 36 362 362 HOH HOH A . I 6 HOH 37 363 363 HOH HOH A . I 6 HOH 38 364 364 HOH HOH A . I 6 HOH 39 365 180 HOH HOH A . I 6 HOH 40 366 366 HOH HOH A . I 6 HOH 41 367 367 HOH HOH A . I 6 HOH 42 368 368 HOH HOH A . I 6 HOH 43 369 369 HOH HOH A . I 6 HOH 44 370 370 HOH HOH A . I 6 HOH 45 371 371 HOH HOH A . I 6 HOH 46 372 372 HOH HOH A . I 6 HOH 47 373 373 HOH HOH A . I 6 HOH 48 374 374 HOH HOH A . I 6 HOH 49 375 375 HOH HOH A . I 6 HOH 50 376 376 HOH HOH A . I 6 HOH 51 377 377 HOH HOH A . I 6 HOH 52 378 378 HOH HOH A . I 6 HOH 53 379 379 HOH HOH A . I 6 HOH 54 380 380 HOH HOH A . I 6 HOH 55 381 381 HOH HOH A . I 6 HOH 56 382 382 HOH HOH A . I 6 HOH 57 383 383 HOH HOH A . I 6 HOH 58 384 384 HOH HOH A . I 6 HOH 59 385 385 HOH HOH A . I 6 HOH 60 386 386 HOH HOH A . I 6 HOH 61 387 387 HOH HOH A . I 6 HOH 62 388 388 HOH HOH A . I 6 HOH 63 389 389 HOH HOH A . I 6 HOH 64 390 390 HOH HOH A . I 6 HOH 65 391 391 HOH HOH A . I 6 HOH 66 392 392 HOH HOH A . I 6 HOH 67 393 393 HOH HOH A . I 6 HOH 68 394 394 HOH HOH A . I 6 HOH 69 395 395 HOH HOH A . I 6 HOH 70 396 396 HOH HOH A . I 6 HOH 71 397 397 HOH HOH A . I 6 HOH 72 398 398 HOH HOH A . I 6 HOH 73 399 399 HOH HOH A . I 6 HOH 74 400 400 HOH HOH A . I 6 HOH 75 401 401 HOH HOH A . I 6 HOH 76 402 402 HOH HOH A . I 6 HOH 77 403 403 HOH HOH A . I 6 HOH 78 404 404 HOH HOH A . I 6 HOH 79 405 405 HOH HOH A . I 6 HOH 80 406 406 HOH HOH A . I 6 HOH 81 407 407 HOH HOH A . I 6 HOH 82 408 408 HOH HOH A . I 6 HOH 83 409 409 HOH HOH A . I 6 HOH 84 410 410 HOH HOH A . I 6 HOH 85 411 411 HOH HOH A . I 6 HOH 86 412 412 HOH HOH A . I 6 HOH 87 413 413 HOH HOH A . I 6 HOH 88 414 414 HOH HOH A . I 6 HOH 89 415 415 HOH HOH A . I 6 HOH 90 416 416 HOH HOH A . I 6 HOH 91 417 417 HOH HOH A . I 6 HOH 92 418 418 HOH HOH A . I 6 HOH 93 419 419 HOH HOH A . I 6 HOH 94 420 420 HOH HOH A . I 6 HOH 95 421 421 HOH HOH A . I 6 HOH 96 422 422 HOH HOH A . I 6 HOH 97 423 423 HOH HOH A . I 6 HOH 98 424 424 HOH HOH A . I 6 HOH 99 425 425 HOH HOH A . I 6 HOH 100 426 426 HOH HOH A . I 6 HOH 101 427 427 HOH HOH A . I 6 HOH 102 428 428 HOH HOH A . I 6 HOH 103 429 429 HOH HOH A . I 6 HOH 104 430 430 HOH HOH A . I 6 HOH 105 431 431 HOH HOH A . I 6 HOH 106 432 432 HOH HOH A . I 6 HOH 107 433 433 HOH HOH A . I 6 HOH 108 434 434 HOH HOH A . I 6 HOH 109 435 435 HOH HOH A . I 6 HOH 110 436 436 HOH HOH A . I 6 HOH 111 437 437 HOH HOH A . I 6 HOH 112 438 438 HOH HOH A . I 6 HOH 113 439 439 HOH HOH A . I 6 HOH 114 440 440 HOH HOH A . I 6 HOH 115 441 441 HOH HOH A . I 6 HOH 116 442 442 HOH HOH A . I 6 HOH 117 443 443 HOH HOH A . I 6 HOH 118 444 444 HOH HOH A . I 6 HOH 119 445 445 HOH HOH A . I 6 HOH 120 446 446 HOH HOH A . I 6 HOH 121 447 447 HOH HOH A . I 6 HOH 122 448 448 HOH HOH A . I 6 HOH 123 449 449 HOH HOH A . I 6 HOH 124 450 450 HOH HOH A . I 6 HOH 125 451 451 HOH HOH A . I 6 HOH 126 452 452 HOH HOH A . I 6 HOH 127 453 453 HOH HOH A . I 6 HOH 128 454 454 HOH HOH A . I 6 HOH 129 455 455 HOH HOH A . I 6 HOH 130 456 456 HOH HOH A . I 6 HOH 131 457 457 HOH HOH A . I 6 HOH 132 458 458 HOH HOH A . I 6 HOH 133 459 459 HOH HOH A . I 6 HOH 134 460 460 HOH HOH A . I 6 HOH 135 461 461 HOH HOH A . I 6 HOH 136 462 462 HOH HOH A . I 6 HOH 137 463 463 HOH HOH A . I 6 HOH 138 464 464 HOH HOH A . I 6 HOH 139 465 465 HOH HOH A . I 6 HOH 140 466 466 HOH HOH A . I 6 HOH 141 467 467 HOH HOH A . I 6 HOH 142 468 468 HOH HOH A . I 6 HOH 143 469 469 HOH HOH A . I 6 HOH 144 470 470 HOH HOH A . I 6 HOH 145 471 471 HOH HOH A . I 6 HOH 146 472 472 HOH HOH A . I 6 HOH 147 473 473 HOH HOH A . I 6 HOH 148 474 474 HOH HOH A . I 6 HOH 149 475 475 HOH HOH A . I 6 HOH 150 476 476 HOH HOH A . I 6 HOH 151 477 477 HOH HOH A . I 6 HOH 152 478 478 HOH HOH A . I 6 HOH 153 479 479 HOH HOH A . I 6 HOH 154 480 480 HOH HOH A . I 6 HOH 155 481 481 HOH HOH A . I 6 HOH 156 482 482 HOH HOH A . I 6 HOH 157 483 483 HOH HOH A . I 6 HOH 158 484 484 HOH HOH A . I 6 HOH 159 485 485 HOH HOH A . I 6 HOH 160 486 486 HOH HOH A . I 6 HOH 161 487 487 HOH HOH A . I 6 HOH 162 488 488 HOH HOH A . I 6 HOH 163 489 489 HOH HOH A . I 6 HOH 164 490 490 HOH HOH A . I 6 HOH 165 491 491 HOH HOH A . I 6 HOH 166 492 492 HOH HOH A . I 6 HOH 167 493 493 HOH HOH A . I 6 HOH 168 494 494 HOH HOH A . I 6 HOH 169 495 495 HOH HOH A . I 6 HOH 170 496 496 HOH HOH A . I 6 HOH 171 497 497 HOH HOH A . I 6 HOH 172 498 498 HOH HOH A . I 6 HOH 173 499 499 HOH HOH A . I 6 HOH 174 500 500 HOH HOH A . I 6 HOH 175 501 501 HOH HOH A . I 6 HOH 176 502 502 HOH HOH A . I 6 HOH 177 503 503 HOH HOH A . I 6 HOH 178 504 504 HOH HOH A . I 6 HOH 179 505 505 HOH HOH A . I 6 HOH 180 506 506 HOH HOH A . I 6 HOH 181 507 507 HOH HOH A . I 6 HOH 182 508 508 HOH HOH A . I 6 HOH 183 509 509 HOH HOH A . I 6 HOH 184 510 510 HOH HOH A . I 6 HOH 185 511 511 HOH HOH A . I 6 HOH 186 512 512 HOH HOH A . I 6 HOH 187 513 513 HOH HOH A . I 6 HOH 188 514 514 HOH HOH A . I 6 HOH 189 515 515 HOH HOH A . I 6 HOH 190 516 516 HOH HOH A . I 6 HOH 191 517 517 HOH HOH A . I 6 HOH 192 518 518 HOH HOH A . I 6 HOH 193 519 519 HOH HOH A . I 6 HOH 194 520 520 HOH HOH A . I 6 HOH 195 521 521 HOH HOH A . I 6 HOH 196 522 522 HOH HOH A . I 6 HOH 197 523 523 HOH HOH A . I 6 HOH 198 524 524 HOH HOH A . I 6 HOH 199 525 525 HOH HOH A . I 6 HOH 200 526 526 HOH HOH A . I 6 HOH 201 527 527 HOH HOH A . I 6 HOH 202 528 528 HOH HOH A . I 6 HOH 203 529 529 HOH HOH A . I 6 HOH 204 530 530 HOH HOH A . I 6 HOH 205 531 531 HOH HOH A . I 6 HOH 206 532 532 HOH HOH A . I 6 HOH 207 533 533 HOH HOH A . I 6 HOH 208 534 534 HOH HOH A . I 6 HOH 209 535 535 HOH HOH A . I 6 HOH 210 536 536 HOH HOH A . I 6 HOH 211 537 537 HOH HOH A . I 6 HOH 212 538 538 HOH HOH A . I 6 HOH 213 539 539 HOH HOH A . I 6 HOH 214 540 540 HOH HOH A . I 6 HOH 215 541 541 HOH HOH A . I 6 HOH 216 542 542 HOH HOH A . I 6 HOH 217 543 543 HOH HOH A . I 6 HOH 218 544 544 HOH HOH A . I 6 HOH 219 545 545 HOH HOH A . I 6 HOH 220 546 546 HOH HOH A . I 6 HOH 221 547 547 HOH HOH A . I 6 HOH 222 548 548 HOH HOH A . I 6 HOH 223 549 549 HOH HOH A . I 6 HOH 224 550 550 HOH HOH A . I 6 HOH 225 551 551 HOH HOH A . I 6 HOH 226 552 552 HOH HOH A . I 6 HOH 227 553 553 HOH HOH A . I 6 HOH 228 554 554 HOH HOH A . I 6 HOH 229 555 555 HOH HOH A . I 6 HOH 230 556 556 HOH HOH A . I 6 HOH 231 557 557 HOH HOH A . I 6 HOH 232 558 558 HOH HOH A . I 6 HOH 233 559 559 HOH HOH A . I 6 HOH 234 560 560 HOH HOH A . I 6 HOH 235 561 561 HOH HOH A . I 6 HOH 236 562 562 HOH HOH A . I 6 HOH 237 563 563 HOH HOH A . I 6 HOH 238 564 564 HOH HOH A . I 6 HOH 239 565 565 HOH HOH A . I 6 HOH 240 566 566 HOH HOH A . I 6 HOH 241 567 567 HOH HOH A . I 6 HOH 242 568 568 HOH HOH A . I 6 HOH 243 569 569 HOH HOH A . I 6 HOH 244 570 570 HOH HOH A . I 6 HOH 245 571 571 HOH HOH A . I 6 HOH 246 572 572 HOH HOH A . I 6 HOH 247 573 573 HOH HOH A . I 6 HOH 248 574 574 HOH HOH A . I 6 HOH 249 575 575 HOH HOH A . I 6 HOH 250 576 576 HOH HOH A . I 6 HOH 251 577 577 HOH HOH A . I 6 HOH 252 578 578 HOH HOH A . I 6 HOH 253 579 579 HOH HOH A . I 6 HOH 254 580 580 HOH HOH A . I 6 HOH 255 581 581 HOH HOH A . I 6 HOH 256 582 582 HOH HOH A . I 6 HOH 257 583 583 HOH HOH A . I 6 HOH 258 584 584 HOH HOH A . I 6 HOH 259 585 585 HOH HOH A . I 6 HOH 260 586 586 HOH HOH A . I 6 HOH 261 587 587 HOH HOH A . I 6 HOH 262 588 588 HOH HOH A . I 6 HOH 263 589 589 HOH HOH A . I 6 HOH 264 590 590 HOH HOH A . I 6 HOH 265 591 591 HOH HOH A . I 6 HOH 266 592 592 HOH HOH A . I 6 HOH 267 593 593 HOH HOH A . I 6 HOH 268 594 594 HOH HOH A . I 6 HOH 269 595 595 HOH HOH A . I 6 HOH 270 596 596 HOH HOH A . I 6 HOH 271 597 597 HOH HOH A . I 6 HOH 272 598 598 HOH HOH A . I 6 HOH 273 599 599 HOH HOH A . I 6 HOH 274 600 600 HOH HOH A . I 6 HOH 275 601 601 HOH HOH A . I 6 HOH 276 602 602 HOH HOH A . I 6 HOH 277 603 603 HOH HOH A . I 6 HOH 278 604 186 HOH HOH A . I 6 HOH 279 605 605 HOH HOH A . I 6 HOH 280 606 606 HOH HOH A . I 6 HOH 281 607 607 HOH HOH A . I 6 HOH 282 608 608 HOH HOH A . I 6 HOH 283 609 609 HOH HOH A . I 6 HOH 284 610 610 HOH HOH A . I 6 HOH 285 611 611 HOH HOH A . I 6 HOH 286 612 612 HOH HOH A . I 6 HOH 287 613 613 HOH HOH A . I 6 HOH 288 614 614 HOH HOH A . I 6 HOH 289 615 615 HOH HOH A . I 6 HOH 290 616 616 HOH HOH A . I 6 HOH 291 617 617 HOH HOH A . I 6 HOH 292 618 618 HOH HOH A . I 6 HOH 293 619 619 HOH HOH A . I 6 HOH 294 620 620 HOH HOH A . I 6 HOH 295 621 621 HOH HOH A . I 6 HOH 296 622 622 HOH HOH A . I 6 HOH 297 623 623 HOH HOH A . I 6 HOH 298 624 624 HOH HOH A . I 6 HOH 299 625 625 HOH HOH A . I 6 HOH 300 626 626 HOH HOH A . I 6 HOH 301 627 627 HOH HOH A . I 6 HOH 302 628 628 HOH HOH A . I 6 HOH 303 629 629 HOH HOH A . I 6 HOH 304 630 630 HOH HOH A . I 6 HOH 305 631 631 HOH HOH A . I 6 HOH 306 632 632 HOH HOH A . I 6 HOH 307 633 633 HOH HOH A . I 6 HOH 308 634 634 HOH HOH A . I 6 HOH 309 635 635 HOH HOH A . I 6 HOH 310 636 636 HOH HOH A . I 6 HOH 311 637 637 HOH HOH A . I 6 HOH 312 638 638 HOH HOH A . I 6 HOH 313 639 639 HOH HOH A . I 6 HOH 314 640 640 HOH HOH A . I 6 HOH 315 641 641 HOH HOH A . I 6 HOH 316 642 642 HOH HOH A . I 6 HOH 317 643 643 HOH HOH A . I 6 HOH 318 644 644 HOH HOH A . I 6 HOH 319 645 645 HOH HOH A . I 6 HOH 320 646 646 HOH HOH A . I 6 HOH 321 647 647 HOH HOH A . I 6 HOH 322 648 648 HOH HOH A . I 6 HOH 323 649 649 HOH HOH A . I 6 HOH 324 650 650 HOH HOH A . I 6 HOH 325 651 651 HOH HOH A . I 6 HOH 326 652 652 HOH HOH A . I 6 HOH 327 653 653 HOH HOH A . I 6 HOH 328 654 654 HOH HOH A . I 6 HOH 329 655 655 HOH HOH A . I 6 HOH 330 656 656 HOH HOH A . I 6 HOH 331 657 657 HOH HOH A . I 6 HOH 332 658 658 HOH HOH A . I 6 HOH 333 659 659 HOH HOH A . I 6 HOH 334 660 660 HOH HOH A . I 6 HOH 335 661 661 HOH HOH A . I 6 HOH 336 662 662 HOH HOH A . I 6 HOH 337 663 663 HOH HOH A . I 6 HOH 338 664 664 HOH HOH A . I 6 HOH 339 665 665 HOH HOH A . I 6 HOH 340 666 666 HOH HOH A . I 6 HOH 341 667 667 HOH HOH A . I 6 HOH 342 668 668 HOH HOH A . I 6 HOH 343 669 669 HOH HOH A . I 6 HOH 344 670 670 HOH HOH A . I 6 HOH 345 671 671 HOH HOH A . I 6 HOH 346 672 672 HOH HOH A . I 6 HOH 347 673 673 HOH HOH A . I 6 HOH 348 674 674 HOH HOH A . I 6 HOH 349 675 675 HOH HOH A . I 6 HOH 350 676 676 HOH HOH A . I 6 HOH 351 677 677 HOH HOH A . I 6 HOH 352 678 678 HOH HOH A . I 6 HOH 353 679 679 HOH HOH A . I 6 HOH 354 680 680 HOH HOH A . I 6 HOH 355 681 681 HOH HOH A . I 6 HOH 356 682 682 HOH HOH A . I 6 HOH 357 683 683 HOH HOH A . I 6 HOH 358 684 684 HOH HOH A . I 6 HOH 359 685 685 HOH HOH A . I 6 HOH 360 686 686 HOH HOH A . I 6 HOH 361 687 687 HOH HOH A . I 6 HOH 362 688 688 HOH HOH A . I 6 HOH 363 689 689 HOH HOH A . I 6 HOH 364 690 690 HOH HOH A . I 6 HOH 365 691 691 HOH HOH A . I 6 HOH 366 692 692 HOH HOH A . I 6 HOH 367 693 693 HOH HOH A . I 6 HOH 368 694 694 HOH HOH A . I 6 HOH 369 695 695 HOH HOH A . I 6 HOH 370 696 696 HOH HOH A . I 6 HOH 371 697 697 HOH HOH A . I 6 HOH 372 698 698 HOH HOH A . I 6 HOH 373 699 699 HOH HOH A . I 6 HOH 374 700 700 HOH HOH A . I 6 HOH 375 701 701 HOH HOH A . I 6 HOH 376 702 702 HOH HOH A . I 6 HOH 377 703 703 HOH HOH A . I 6 HOH 378 704 704 HOH HOH A . I 6 HOH 379 705 705 HOH HOH A . I 6 HOH 380 706 706 HOH HOH A . I 6 HOH 381 707 707 HOH HOH A . I 6 HOH 382 708 708 HOH HOH A . I 6 HOH 383 709 207 HOH HOH A . J 6 HOH 1 177 177 HOH HOH B . J 6 HOH 2 178 178 HOH HOH B . J 6 HOH 3 179 179 HOH HOH B . J 6 HOH 4 181 181 HOH HOH B . J 6 HOH 5 182 182 HOH HOH B . J 6 HOH 6 183 183 HOH HOH B . J 6 HOH 7 184 184 HOH HOH B . J 6 HOH 8 185 185 HOH HOH B . J 6 HOH 9 187 187 HOH HOH B . J 6 HOH 10 188 188 HOH HOH B . J 6 HOH 11 189 189 HOH HOH B . J 6 HOH 12 190 190 HOH HOH B . J 6 HOH 13 191 191 HOH HOH B . J 6 HOH 14 192 192 HOH HOH B . J 6 HOH 15 193 193 HOH HOH B . J 6 HOH 16 194 194 HOH HOH B . J 6 HOH 17 195 195 HOH HOH B . J 6 HOH 18 196 196 HOH HOH B . J 6 HOH 19 197 197 HOH HOH B . J 6 HOH 20 198 198 HOH HOH B . J 6 HOH 21 199 199 HOH HOH B . J 6 HOH 22 200 200 HOH HOH B . J 6 HOH 23 201 201 HOH HOH B . J 6 HOH 24 202 202 HOH HOH B . J 6 HOH 25 203 203 HOH HOH B . J 6 HOH 26 204 204 HOH HOH B . J 6 HOH 27 205 205 HOH HOH B . J 6 HOH 28 206 206 HOH HOH B . J 6 HOH 29 208 208 HOH HOH B . J 6 HOH 30 209 209 HOH HOH B . J 6 HOH 31 210 210 HOH HOH B . J 6 HOH 32 211 211 HOH HOH B . J 6 HOH 33 212 212 HOH HOH B . J 6 HOH 34 213 213 HOH HOH B . J 6 HOH 35 214 214 HOH HOH B . J 6 HOH 36 215 215 HOH HOH B . J 6 HOH 37 216 216 HOH HOH B . J 6 HOH 38 219 219 HOH HOH B . J 6 HOH 39 221 221 HOH HOH B . J 6 HOH 40 224 224 HOH HOH B . J 6 HOH 41 227 227 HOH HOH B . J 6 HOH 42 235 235 HOH HOH B . J 6 HOH 43 237 237 HOH HOH B . J 6 HOH 44 239 239 HOH HOH B . J 6 HOH 45 246 246 HOH HOH B . J 6 HOH 46 248 248 HOH HOH B . J 6 HOH 47 249 249 HOH HOH B . J 6 HOH 48 256 256 HOH HOH B . J 6 HOH 49 257 257 HOH HOH B . J 6 HOH 50 266 266 HOH HOH B . J 6 HOH 51 268 268 HOH HOH B . J 6 HOH 52 271 271 HOH HOH B . J 6 HOH 53 272 272 HOH HOH B . J 6 HOH 54 273 273 HOH HOH B . J 6 HOH 55 275 275 HOH HOH B . J 6 HOH 56 276 276 HOH HOH B . J 6 HOH 57 277 277 HOH HOH B . J 6 HOH 58 278 278 HOH HOH B . J 6 HOH 59 279 279 HOH HOH B . J 6 HOH 60 280 280 HOH HOH B . J 6 HOH 61 283 283 HOH HOH B . J 6 HOH 62 284 284 HOH HOH B . J 6 HOH 63 287 287 HOH HOH B . J 6 HOH 64 294 294 HOH HOH B . J 6 HOH 65 299 299 HOH HOH B . J 6 HOH 66 300 300 HOH HOH B . J 6 HOH 67 301 301 HOH HOH B . J 6 HOH 68 309 309 HOH HOH B . J 6 HOH 69 310 310 HOH HOH B . J 6 HOH 70 312 312 HOH HOH B . J 6 HOH 71 314 314 HOH HOH B . J 6 HOH 72 318 318 HOH HOH B . J 6 HOH 73 320 320 HOH HOH B . J 6 HOH 74 322 322 HOH HOH B . J 6 HOH 75 328 328 HOH HOH B . J 6 HOH 76 332 332 HOH HOH B . J 6 HOH 77 333 333 HOH HOH B . J 6 HOH 78 335 335 HOH HOH B . J 6 HOH 79 340 340 HOH HOH B . J 6 HOH 80 341 341 HOH HOH B . J 6 HOH 81 342 342 HOH HOH B . J 6 HOH 82 345 345 HOH HOH B . J 6 HOH 83 346 346 HOH HOH B . J 6 HOH 84 351 351 HOH HOH B . J 6 HOH 85 355 355 HOH HOH B . J 6 HOH 86 356 356 HOH HOH B . J 6 HOH 87 357 357 HOH HOH B . J 6 HOH 88 358 358 HOH HOH B . J 6 HOH 89 360 360 HOH HOH B . J 6 HOH 90 363 363 HOH HOH B . J 6 HOH 91 365 365 HOH HOH B . J 6 HOH 92 366 366 HOH HOH B . J 6 HOH 93 367 367 HOH HOH B . J 6 HOH 94 368 368 HOH HOH B . J 6 HOH 95 372 372 HOH HOH B . J 6 HOH 96 373 373 HOH HOH B . J 6 HOH 97 385 385 HOH HOH B . J 6 HOH 98 390 390 HOH HOH B . J 6 HOH 99 391 391 HOH HOH B . J 6 HOH 100 394 394 HOH HOH B . J 6 HOH 101 396 396 HOH HOH B . J 6 HOH 102 397 397 HOH HOH B . J 6 HOH 103 406 406 HOH HOH B . J 6 HOH 104 409 409 HOH HOH B . J 6 HOH 105 410 410 HOH HOH B . J 6 HOH 106 416 416 HOH HOH B . J 6 HOH 107 422 422 HOH HOH B . J 6 HOH 108 426 426 HOH HOH B . J 6 HOH 109 429 429 HOH HOH B . J 6 HOH 110 431 431 HOH HOH B . J 6 HOH 111 432 432 HOH HOH B . J 6 HOH 112 434 434 HOH HOH B . J 6 HOH 113 435 435 HOH HOH B . J 6 HOH 114 436 436 HOH HOH B . J 6 HOH 115 437 437 HOH HOH B . J 6 HOH 116 446 446 HOH HOH B . J 6 HOH 117 449 449 HOH HOH B . J 6 HOH 118 457 457 HOH HOH B . J 6 HOH 119 464 464 HOH HOH B . J 6 HOH 120 468 468 HOH HOH B . J 6 HOH 121 473 473 HOH HOH B . J 6 HOH 122 474 474 HOH HOH B . J 6 HOH 123 477 477 HOH HOH B . J 6 HOH 124 481 481 HOH HOH B . J 6 HOH 125 483 483 HOH HOH B . J 6 HOH 126 487 487 HOH HOH B . J 6 HOH 127 490 490 HOH HOH B . J 6 HOH 128 495 495 HOH HOH B . J 6 HOH 129 496 496 HOH HOH B . J 6 HOH 130 497 497 HOH HOH B . J 6 HOH 131 498 498 HOH HOH B . J 6 HOH 132 499 499 HOH HOH B . J 6 HOH 133 500 500 HOH HOH B . J 6 HOH 134 504 504 HOH HOH B . J 6 HOH 135 505 505 HOH HOH B . J 6 HOH 136 511 511 HOH HOH B . J 6 HOH 137 513 513 HOH HOH B . J 6 HOH 138 521 521 HOH HOH B . J 6 HOH 139 527 527 HOH HOH B . J 6 HOH 140 528 528 HOH HOH B . J 6 HOH 141 529 529 HOH HOH B . J 6 HOH 142 530 530 HOH HOH B . J 6 HOH 143 532 532 HOH HOH B . J 6 HOH 144 535 535 HOH HOH B . J 6 HOH 145 536 536 HOH HOH B . J 6 HOH 146 538 538 HOH HOH B . J 6 HOH 147 539 539 HOH HOH B . J 6 HOH 148 540 540 HOH HOH B . J 6 HOH 149 544 544 HOH HOH B . J 6 HOH 150 545 545 HOH HOH B . J 6 HOH 151 546 546 HOH HOH B . J 6 HOH 152 547 547 HOH HOH B . J 6 HOH 153 549 549 HOH HOH B . J 6 HOH 154 550 550 HOH HOH B . J 6 HOH 155 551 551 HOH HOH B . J 6 HOH 156 552 552 HOH HOH B . J 6 HOH 157 604 604 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 166 A ASN 169 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 25 A ASN 33 ? ASN 'GLYCOSYLATION SITE' 3 B ASN 154 B ASN 154 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details hexameric _pdbx_struct_assembly.oligomeric_count 6 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1,2,3 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 32010 ? 1 MORE -127 ? 1 'SSA (A^2)' 62610 ? # loop_ _pdbx_struct_oper_list.id _pdbx_struct_oper_list.type _pdbx_struct_oper_list.name _pdbx_struct_oper_list.symmetry_operation _pdbx_struct_oper_list.matrix[1][1] _pdbx_struct_oper_list.matrix[1][2] _pdbx_struct_oper_list.matrix[1][3] _pdbx_struct_oper_list.vector[1] _pdbx_struct_oper_list.matrix[2][1] _pdbx_struct_oper_list.matrix[2][2] _pdbx_struct_oper_list.matrix[2][3] _pdbx_struct_oper_list.vector[2] _pdbx_struct_oper_list.matrix[3][1] _pdbx_struct_oper_list.matrix[3][2] _pdbx_struct_oper_list.matrix[3][3] _pdbx_struct_oper_list.vector[3] 1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 2 'crystal symmetry operation' 2_545 -y,x-y-1,z -0.5000000000 -0.8660254038 0.0000000000 35.1440000000 0.8660254038 -0.5000000000 0.0000000000 -60.8711935812 0.0000000000 0.0000000000 1.0000000000 0.0000000000 3 'crystal symmetry operation' 3_655 -x+y+1,-x,z -0.5000000000 0.8660254038 0.0000000000 70.2880000000 -0.8660254038 -0.5000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 # loop_ _pdbx_struct_special_symmetry.id _pdbx_struct_special_symmetry.PDB_model_num _pdbx_struct_special_symmetry.auth_asym_id _pdbx_struct_special_symmetry.auth_comp_id _pdbx_struct_special_symmetry.auth_seq_id _pdbx_struct_special_symmetry.PDB_ins_code _pdbx_struct_special_symmetry.label_asym_id _pdbx_struct_special_symmetry.label_comp_id _pdbx_struct_special_symmetry.label_seq_id 1 1 B HOH 436 ? J HOH . 2 1 B HOH 545 ? J HOH . 3 1 B HOH 549 ? J HOH . # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2011-03-09 2 'Structure model' 1 1 2011-07-13 3 'Structure model' 1 2 2017-11-08 # _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' 'Refinement description' # _pdbx_audit_revision_category.ordinal 1 _pdbx_audit_revision_category.revision_ordinal 3 _pdbx_audit_revision_category.data_content_type 'Structure model' _pdbx_audit_revision_category.category software # _diffrn_reflns.diffrn_id 1 _diffrn_reflns.pdbx_d_res_high 1.970 _diffrn_reflns.pdbx_d_res_low 35.000 _diffrn_reflns.pdbx_number_obs 46401 _diffrn_reflns.pdbx_Rmerge_I_obs 0.065 _diffrn_reflns.pdbx_Rsym_value ? _diffrn_reflns.pdbx_chi_squared 1.01 _diffrn_reflns.av_sigmaI_over_netI 24.71 _diffrn_reflns.pdbx_redundancy 8.10 _diffrn_reflns.pdbx_percent_possible_obs 99.70 _diffrn_reflns.number 374387 _diffrn_reflns.pdbx_observed_criterion ? _diffrn_reflns.limit_h_max ? _diffrn_reflns.limit_h_min ? _diffrn_reflns.limit_k_max ? _diffrn_reflns.limit_k_min ? _diffrn_reflns.limit_l_max ? _diffrn_reflns.limit_l_min ? # loop_ _pdbx_diffrn_reflns_shell.diffrn_id _pdbx_diffrn_reflns_shell.d_res_high _pdbx_diffrn_reflns_shell.d_res_low _pdbx_diffrn_reflns_shell.number_obs _pdbx_diffrn_reflns_shell.rejects _pdbx_diffrn_reflns_shell.Rmerge_I_obs _pdbx_diffrn_reflns_shell.Rsym_value _pdbx_diffrn_reflns_shell.chi_squared _pdbx_diffrn_reflns_shell.redundancy _pdbx_diffrn_reflns_shell.percent_possible_obs 1 4.24 35.00 ? ? 0.038 ? 0.984 8.20 98.60 1 3.37 4.24 ? ? 0.047 ? 0.969 8.40 99.80 1 2.94 3.37 ? ? 0.063 ? 1.012 8.50 99.90 1 2.67 2.94 ? ? 0.080 ? 1.035 8.50 100.00 1 2.48 2.67 ? ? 0.115 ? 1.052 8.60 100.00 1 2.34 2.48 ? ? 0.151 ? 1.087 8.60 100.00 1 2.22 2.34 ? ? 0.206 ? 0.993 8.50 99.90 1 2.12 2.22 ? ? 0.262 ? 0.980 8.30 99.90 1 2.04 2.12 ? ? 0.345 ? 0.892 7.50 99.90 1 1.97 2.04 ? ? 0.432 ? 1.075 5.70 99.20 # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] 'X-RAY DIFFRACTION' 1 ? refined 20.1630 -6.7360 35.6430 0.0474 0.0651 0.1570 0.0063 0.0054 -0.0197 0.0525 0.2307 0.6598 -0.0450 -0.0655 -0.1543 0.0261 0.0131 -0.0375 -0.0147 -0.0365 0.0098 -0.0529 -0.0320 0.0105 'X-RAY DIFFRACTION' 2 ? refined 25.7410 -12.8510 -16.5750 0.1510 0.1314 0.0000 0.0371 -0.0001 0.0068 0.3619 -0.0847 4.5355 0.0103 0.7269 -0.0684 -0.0587 0.0476 0.0384 0.0289 -0.0077 -0.0192 -0.1007 -0.2329 0.0664 # loop_ _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection _pdbx_refine_tls_group.selection_details 'X-RAY DIFFRACTION' 1 1 A 1 ? ? A 326 ? ? ? ? 'X-RAY DIFFRACTION' 2 2 B 1 ? ? B 172 ? ? ? ? # _pdbx_phasing_MR.entry_id 3QQB _pdbx_phasing_MR.method_rotation ? _pdbx_phasing_MR.method_translation ? _pdbx_phasing_MR.model_details 'Phaser MODE: MR_AUTO' _pdbx_phasing_MR.R_factor ? _pdbx_phasing_MR.R_rigid_body ? _pdbx_phasing_MR.correlation_coeff_Fo_to_Fc ? _pdbx_phasing_MR.correlation_coeff_Io_to_Ic ? _pdbx_phasing_MR.d_res_high_rotation 2.500 _pdbx_phasing_MR.d_res_low_rotation 30.190 _pdbx_phasing_MR.d_res_high_translation 2.500 _pdbx_phasing_MR.d_res_low_translation 30.190 _pdbx_phasing_MR.packing ? _pdbx_phasing_MR.reflns_percent_rotation ? _pdbx_phasing_MR.reflns_percent_translation ? _pdbx_phasing_MR.sigma_F_rotation ? _pdbx_phasing_MR.sigma_F_translation ? _pdbx_phasing_MR.sigma_I_rotation ? _pdbx_phasing_MR.sigma_I_translation ? # _phasing.method mr # loop_ _software.pdbx_ordinal _software.name _software.version _software.date _software.type _software.contact_author _software.contact_author_email _software.classification _software.location _software.language _software.citation_id 1 DENZO . ? package 'Zbyszek Otwinowski' hkl@hkl-xray.com 'data reduction' http://www.hkl-xray.com/ ? ? 2 SCALEPACK . ? package 'Zbyszek Otwinowski' hkl@hkl-xray.com 'data scaling' http://www.hkl-xray.com/ ? ? 3 PHASER 1.3.3 'Fri Oct 20 12:51:01 2006' program 'Randy J. Read' cimr-phaser@lists.cam.ac.uk phasing http://www-structmed.cimr.cam.ac.uk/phaser/ ? ? 4 REFMAC 5.2.0019 ? program 'Garib N. Murshudov' garib@ysbl.york.ac.uk refinement http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 5 PDB_EXTRACT 3.10 'June 10, 2010' package PDB deposit@deposit.rcsb.org 'data extraction' http://sw-tools.pdb.org/apps/PDB_EXTRACT/ C++ ? 6 HKL-2000 . ? ? ? ? 'data collection' ? ? ? 7 HKL-2000 . ? ? ? ? 'data reduction' ? ? ? 8 HKL-2000 . ? ? ? ? 'data scaling' ? ? ? # _pdbx_validate_symm_contact.id 1 _pdbx_validate_symm_contact.PDB_model_num 1 _pdbx_validate_symm_contact.auth_atom_id_1 O _pdbx_validate_symm_contact.auth_asym_id_1 A _pdbx_validate_symm_contact.auth_comp_id_1 HOH _pdbx_validate_symm_contact.auth_seq_id_1 440 _pdbx_validate_symm_contact.PDB_ins_code_1 ? _pdbx_validate_symm_contact.label_alt_id_1 ? _pdbx_validate_symm_contact.site_symmetry_1 1_555 _pdbx_validate_symm_contact.auth_atom_id_2 O _pdbx_validate_symm_contact.auth_asym_id_2 A _pdbx_validate_symm_contact.auth_comp_id_2 HOH _pdbx_validate_symm_contact.auth_seq_id_2 591 _pdbx_validate_symm_contact.PDB_ins_code_2 ? _pdbx_validate_symm_contact.label_alt_id_2 ? _pdbx_validate_symm_contact.site_symmetry_2 3_655 _pdbx_validate_symm_contact.dist 2.15 # 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 SER A 146 ? ? -143.36 -158.26 2 1 GLN A 196 ? ? 55.59 -47.47 3 1 THR A 206 ? ? -120.31 -163.96 4 1 TRP A 240 ? ? 72.12 -0.73 5 1 SER A 265 ? ? -147.09 -148.45 6 1 ALA B 5 ? ? -93.24 -60.14 7 1 ARG B 127 ? ? 44.87 -133.81 # 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 327 ? A GLU 325 2 1 Y 1 A SER 328 ? A SER 326 3 1 Y 1 A ARG 329 ? A ARG 327 4 1 Y 1 B ILE 173 ? B ILE 173 5 1 Y 1 B LYS 174 ? B LYS 174 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 3 N-ACETYL-D-GLUCOSAMINE NAG 4 1,2-ETHANEDIOL EDO 5 'DI(HYDROXYETHYL)ETHER' PEG 6 water HOH #