data_4BH0 # _entry.id 4BH0 # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.279 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 4BH0 PDBE EBI-56331 WWPDB D_1290056331 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 4BGW unspecified 'STRUCTURE OF H5 (VN1194) INFLUENZA HAEMAGGLUTININ' PDB 4BGX unspecified ;H5 (VN1194) INFLUENZA VIRUS HAEMAGGLUTININ IN COMPLEX WITH HUMAN RECEPTOR ANALOGUE 6'-SLN ; PDB 4BGY unspecified ;H5 (VN1194) INFLUENZA VIRUS HAEMAGGLUTININ IN COMPLEX WITH AVIAN RECEPTOR ANALOGUE 3'-SLN ; PDB 4BGZ unspecified 'CRYSTAL STRUCTURE OF H5 (TYTY) INFLUENZA VIRUS HAEMAGGLUTININ' PDB 4BH1 unspecified ;H5 (TYTY) INFLUENZA VIRUS HAEMAGGLUTININ IN COMPLEX WITH AVIAN RECEPTOR ANALOGUE 3'-SLN ; PDB 4BH2 unspecified 'CRYSTAL STRUCTURE OF THE HAEMAGGLUTININ FROM A TRANSMISSIBLE MUTANT H5 INFLUENZA VIRUS' PDB 4BH3 unspecified ;HAEMAGGLUTININ FROM A TRANSMISSIBLE MUTANT H5 INFLUENZA VIRUS IN COMPLEX WITH HUMAN RECEPTOR ANALOGUE 6'-SLN ; PDB 4BH4 unspecified ;HAEMAGGLUTININ FROM A TRANSMISSIBLE MUTANT H5 INFLUENZA VIRUS IN COMPLEX WITH AVIAN RECEPTOR ANALOGUE 3'-SLN ; # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4BH0 _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2013-03-29 _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Xiong, X.' 1 'Coombs, P.J.' 2 'Martin, S.R.' 3 'Liu, J.' 4 'Xiao, H.' 5 'McCauley, J.W.' 6 'Locher, K.' 7 'Walker, P.A.' 8 'Collins, P.J.' 9 'Kawaoka, Y.' 10 'Skehel, J.J.' 11 'Gamblin, S.J.' 12 # _citation.id primary _citation.title 'Receptor Binding by a Ferret-Transmissible H5 Avian Influenza Virus' _citation.journal_abbrev Nature _citation.journal_volume 497 _citation.page_first 392 _citation.page_last ? _citation.year 2013 _citation.journal_id_ASTM NATUAS _citation.country UK _citation.journal_id_ISSN 0028-0836 _citation.journal_id_CSD 0006 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 23615615 _citation.pdbx_database_id_DOI 10.1038/NATURE12144 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Xiong, X.' 1 primary 'Coombs, P.J.' 2 primary 'R Martin, S.' 3 primary 'Liu, J.' 4 primary 'Xiao, H.' 5 primary 'Mccauley, J.W.' 6 primary 'Locher, K.' 7 primary 'Walker, P.A.' 8 primary 'Collins, P.J.' 9 primary 'Kawaoka, Y.' 10 primary 'Skehel, J.J.' 11 primary 'Gamblin, S.J.' 12 # _cell.entry_id 4BH0 _cell.length_a 70.346 _cell.length_b 228.296 _cell.length_c 71.267 _cell.angle_alpha 90.00 _cell.angle_beta 114.01 _cell.angle_gamma 90.00 _cell.Z_PDB 6 _cell.pdbx_unique_axis ? # _symmetry.entry_id 4BH0 _symmetry.space_group_name_H-M 'P 1 21 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 4 # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man HEMAGGLUTININ 36978.715 3 ? ? 'HA1 OF TRYPSIN RELEASED ECTODOMAIN, RESIDUES 17-338' ? 2 polymer man HEMAGGLUTININ 19126.004 3 ? ? 'HA2 OF TRYPSIN RELEASED ECTODOMAIN, RESIDUES 347-512' ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 5 ? ? ? ? 4 non-polymer man 'O-SIALIC ACID' 309.270 3 ? ? ? ? 5 non-polymer man BETA-D-GALACTOSE 180.156 3 ? ? ? ? 6 non-polymer syn 'PHOSPHATE ION' 94.971 5 ? ? ? ? 7 water nat water 18.015 712 ? ? ? ? # loop_ _entity_name_com.entity_id _entity_name_com.name 1 'HAEMAGGLUTININ HA1' 2 'HAEMAGGLUTININ HA2' # 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 ;PDQICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGKLCDLDGVKPLILRDCSVAGWLLGNPMCDEFLNVPEWSYI VEKINPANDLCYPGNFNDYEELKHLLSRINHFEKIQIIPKSSWSDHEASAGVSSACPYQGRSSFFRNVVWLIKKDNAYPT IKRSYNNTNQEDLLVLWGIHHPNDAAEQTRLYQNPTTYISVGTSTLNQRLVPKIATRSKVNGQSGRMEFFWTILKPNDAI NFESNGNFIAPENAYKIVKKGDSTIMKSELEYGNCNTKCQTPIGAINSSMPFHNIHPLTIGECPKYVKSSRLVLATGLRN SPQRETR ; ;PDQICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGKLCDLDGVKPLILRDCSVAGWLLGNPMCDEFLNVPEWSYI VEKINPANDLCYPGNFNDYEELKHLLSRINHFEKIQIIPKSSWSDHEASAGVSSACPYQGRSSFFRNVVWLIKKDNAYPT IKRSYNNTNQEDLLVLWGIHHPNDAAEQTRLYQNPTTYISVGTSTLNQRLVPKIATRSKVNGQSGRMEFFWTILKPNDAI NFESNGNFIAPENAYKIVKKGDSTIMKSELEYGNCNTKCQTPIGAINSSMPFHNIHPLTIGECPKYVKSSRLVLATGLRN SPQRETR ; A,C,E ? 2 'polypeptide(L)' no no ;GLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENL NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHRCDNECMESVRNGTYDYP QYSEEA ; ;GLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENL NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHRCDNECMESVRNGTYDYP QYSEEA ; B,D,F ? # 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 ASP n 1 3 GLN n 1 4 ILE n 1 5 CYS n 1 6 ILE n 1 7 GLY n 1 8 TYR n 1 9 HIS n 1 10 ALA n 1 11 ASN n 1 12 ASN n 1 13 SER n 1 14 THR n 1 15 GLU n 1 16 GLN n 1 17 VAL n 1 18 ASP n 1 19 THR n 1 20 ILE n 1 21 MET n 1 22 GLU n 1 23 LYS n 1 24 ASN n 1 25 VAL n 1 26 THR n 1 27 VAL n 1 28 THR n 1 29 HIS n 1 30 ALA n 1 31 GLN n 1 32 ASP n 1 33 ILE n 1 34 LEU n 1 35 GLU n 1 36 LYS n 1 37 THR n 1 38 HIS n 1 39 ASN n 1 40 GLY n 1 41 LYS n 1 42 LEU n 1 43 CYS n 1 44 ASP n 1 45 LEU n 1 46 ASP n 1 47 GLY n 1 48 VAL n 1 49 LYS n 1 50 PRO n 1 51 LEU n 1 52 ILE n 1 53 LEU n 1 54 ARG n 1 55 ASP n 1 56 CYS n 1 57 SER n 1 58 VAL n 1 59 ALA n 1 60 GLY n 1 61 TRP n 1 62 LEU n 1 63 LEU n 1 64 GLY n 1 65 ASN n 1 66 PRO n 1 67 MET n 1 68 CYS n 1 69 ASP n 1 70 GLU n 1 71 PHE n 1 72 LEU n 1 73 ASN n 1 74 VAL n 1 75 PRO n 1 76 GLU n 1 77 TRP n 1 78 SER n 1 79 TYR n 1 80 ILE n 1 81 VAL n 1 82 GLU n 1 83 LYS n 1 84 ILE n 1 85 ASN n 1 86 PRO n 1 87 ALA n 1 88 ASN n 1 89 ASP n 1 90 LEU n 1 91 CYS n 1 92 TYR n 1 93 PRO n 1 94 GLY n 1 95 ASN n 1 96 PHE n 1 97 ASN n 1 98 ASP n 1 99 TYR n 1 100 GLU n 1 101 GLU n 1 102 LEU n 1 103 LYS n 1 104 HIS n 1 105 LEU n 1 106 LEU n 1 107 SER n 1 108 ARG n 1 109 ILE n 1 110 ASN n 1 111 HIS n 1 112 PHE n 1 113 GLU n 1 114 LYS n 1 115 ILE n 1 116 GLN n 1 117 ILE n 1 118 ILE n 1 119 PRO n 1 120 LYS n 1 121 SER n 1 122 SER n 1 123 TRP n 1 124 SER n 1 125 ASP n 1 126 HIS n 1 127 GLU n 1 128 ALA n 1 129 SER n 1 130 ALA n 1 131 GLY n 1 132 VAL n 1 133 SER n 1 134 SER n 1 135 ALA n 1 136 CYS n 1 137 PRO n 1 138 TYR n 1 139 GLN n 1 140 GLY n 1 141 ARG n 1 142 SER n 1 143 SER n 1 144 PHE n 1 145 PHE n 1 146 ARG n 1 147 ASN n 1 148 VAL n 1 149 VAL n 1 150 TRP n 1 151 LEU n 1 152 ILE n 1 153 LYS n 1 154 LYS n 1 155 ASP n 1 156 ASN n 1 157 ALA n 1 158 TYR n 1 159 PRO n 1 160 THR n 1 161 ILE n 1 162 LYS n 1 163 ARG n 1 164 SER n 1 165 TYR n 1 166 ASN n 1 167 ASN n 1 168 THR n 1 169 ASN n 1 170 GLN n 1 171 GLU n 1 172 ASP n 1 173 LEU n 1 174 LEU n 1 175 VAL n 1 176 LEU n 1 177 TRP n 1 178 GLY n 1 179 ILE n 1 180 HIS n 1 181 HIS n 1 182 PRO n 1 183 ASN n 1 184 ASP n 1 185 ALA n 1 186 ALA n 1 187 GLU n 1 188 GLN n 1 189 THR n 1 190 ARG n 1 191 LEU n 1 192 TYR n 1 193 GLN n 1 194 ASN n 1 195 PRO n 1 196 THR n 1 197 THR n 1 198 TYR n 1 199 ILE 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 GLN n 1 209 ARG n 1 210 LEU n 1 211 VAL n 1 212 PRO n 1 213 LYS n 1 214 ILE n 1 215 ALA n 1 216 THR n 1 217 ARG n 1 218 SER n 1 219 LYS n 1 220 VAL n 1 221 ASN n 1 222 GLY n 1 223 GLN n 1 224 SER n 1 225 GLY n 1 226 ARG n 1 227 MET n 1 228 GLU n 1 229 PHE n 1 230 PHE n 1 231 TRP n 1 232 THR n 1 233 ILE n 1 234 LEU n 1 235 LYS n 1 236 PRO n 1 237 ASN n 1 238 ASP n 1 239 ALA n 1 240 ILE n 1 241 ASN n 1 242 PHE n 1 243 GLU n 1 244 SER n 1 245 ASN n 1 246 GLY n 1 247 ASN n 1 248 PHE n 1 249 ILE n 1 250 ALA n 1 251 PRO n 1 252 GLU n 1 253 ASN n 1 254 ALA n 1 255 TYR n 1 256 LYS n 1 257 ILE n 1 258 VAL n 1 259 LYS n 1 260 LYS n 1 261 GLY n 1 262 ASP n 1 263 SER n 1 264 THR n 1 265 ILE n 1 266 MET n 1 267 LYS n 1 268 SER n 1 269 GLU n 1 270 LEU n 1 271 GLU n 1 272 TYR n 1 273 GLY n 1 274 ASN n 1 275 CYS n 1 276 ASN 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 ILE n 1 284 GLY n 1 285 ALA n 1 286 ILE n 1 287 ASN n 1 288 SER n 1 289 SER n 1 290 MET n 1 291 PRO n 1 292 PHE n 1 293 HIS n 1 294 ASN n 1 295 ILE 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 SER n 1 311 ARG 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 SER n 1 322 PRO n 1 323 GLN n 1 324 ARG n 1 325 GLU n 1 326 THR 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 GLU 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 ILE n 2 46 ASP n 2 47 GLY n 2 48 VAL 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 ILE n 2 56 ILE n 2 57 ASP 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 ARG n 2 69 GLU n 2 70 PHE n 2 71 ASN n 2 72 ASN n 2 73 LEU n 2 74 GLU n 2 75 ARG n 2 76 ARG n 2 77 ILE 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 ARG 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 LEU n 2 125 GLN n 2 126 LEU n 2 127 ARG n 2 128 ASP n 2 129 ASN n 2 130 ALA 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 ARG n 2 144 CYS n 2 145 ASP n 2 146 ASN n 2 147 GLU n 2 148 CYS n 2 149 MET n 2 150 GLU n 2 151 SER n 2 152 VAL n 2 153 ARG 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 GLN n 2 162 TYR n 2 163 SER n 2 164 GLU n 2 165 GLU n 2 166 ALA 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 ? ? ? ? ? ? ? 'A/TURKEY/TURKEY/1/2005(H5N1)' ? ? ? ? 'INFLUENZA VIRUS' 375457 ? ? ? ? ? ? ? ? 'SPODOPTERA FRUGIPERDA' 7108 ? ? ? ? ? ? ? ? SF9 ? ? ? ? ? BACULOVIRUS ? ? ? PACGP67A ? ? 2 1 sample ? ? ? ? ? ? ? 'A/TURKEY/TURKEY/1/2005 (H5N1)' ? ? ? ? 'INFLUENZA VIRUS' 375457 ? ? ? ? ? ? ? ? 'SPODOPTERA FRUGIPERDA' 7108 ? ? ? ? ? ? ? ? SF9 ? ? ? ? ? BACULOVIRUS ? ? ? PACGP67A ? ? # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_db_accession _struct_ref.pdbx_db_isoform 1 UNP Q207Z6_9INFA 1 ? ? Q207Z6 ? 2 UNP Q207Z6_9INFA 2 ? ? Q207Z6 ? # 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 4BH0 A 2 ? 323 ? Q207Z6 17 ? 338 ? 1 322 2 2 4BH0 B 1 ? 166 ? Q207Z6 347 ? 512 ? 1 166 3 1 4BH0 C 2 ? 323 ? Q207Z6 17 ? 338 ? 1 322 4 2 4BH0 D 1 ? 166 ? Q207Z6 347 ? 512 ? 1 166 5 1 4BH0 E 2 ? 323 ? Q207Z6 17 ? 338 ? 1 322 6 2 4BH0 F 1 ? 166 ? Q207Z6 347 ? 512 ? 1 166 # 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 4BH0 PRO A 1 ? UNP Q207Z6 ? ? 'expression tag' 0 1 1 4BH0 ARG A 324 ? UNP Q207Z6 ? ? 'expression tag' 323 2 1 4BH0 GLU A 325 ? UNP Q207Z6 ? ? 'expression tag' 324 3 1 4BH0 THR A 326 ? UNP Q207Z6 ? ? 'expression tag' 325 4 1 4BH0 ARG A 327 ? UNP Q207Z6 ? ? 'expression tag' 326 5 3 4BH0 PRO C 1 ? UNP Q207Z6 ? ? 'expression tag' 0 6 3 4BH0 ARG C 324 ? UNP Q207Z6 ? ? 'expression tag' 323 7 3 4BH0 GLU C 325 ? UNP Q207Z6 ? ? 'expression tag' 324 8 3 4BH0 THR C 326 ? UNP Q207Z6 ? ? 'expression tag' 325 9 3 4BH0 ARG C 327 ? UNP Q207Z6 ? ? 'expression tag' 326 10 5 4BH0 PRO E 1 ? UNP Q207Z6 ? ? 'expression tag' 0 11 5 4BH0 ARG E 324 ? UNP Q207Z6 ? ? 'expression tag' 323 12 5 4BH0 GLU E 325 ? UNP Q207Z6 ? ? 'expression tag' 324 13 5 4BH0 THR E 326 ? UNP Q207Z6 ? ? 'expression tag' 325 14 5 4BH0 ARG E 327 ? UNP Q207Z6 ? ? 'expression tag' 326 15 # 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 GAL D-saccharide . BETA-D-GALACTOSE ? 'C6 H12 O6' 180.156 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PO4 non-polymer . 'PHOSPHATE ION' ? 'O4 P -3' 94.971 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 SIA non-polymer . 'O-SIALIC ACID' ? 'C11 H19 N O9' 309.270 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 4BH0 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.11 _exptl_crystal.density_percent_sol 60.46 _exptl_crystal.description NONE # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH ? _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details 'BIS-TRIS PROPANE PH 7.5, 0.05 - 0.15 M K/NAPO4 (PH 7.0), 15-18% PEG 3350' # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector PIXEL _diffrn_detector.type 'DECTRIS PILATUS 6M' _diffrn_detector.pdbx_collection_date 2012-03-10 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.9763 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'DIAMOND BEAMLINE I03' _diffrn_source.pdbx_synchrotron_site Diamond _diffrn_source.pdbx_synchrotron_beamline I03 _diffrn_source.pdbx_wavelength 0.9763 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4BH0 _reflns.observed_criterion_sigma_I 2.0 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 56.55 _reflns.d_resolution_high 2.36 _reflns.number_obs 81446 _reflns.number_all ? _reflns.percent_possible_obs 97.1 _reflns.pdbx_Rmerge_I_obs 0.09 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 7.90 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 3.1 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.36 _reflns_shell.d_res_low 2.49 _reflns_shell.percent_possible_all 92.6 _reflns_shell.Rmerge_I_obs 0.60 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 2.00 _reflns_shell.pdbx_redundancy 2.6 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4BH0 _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 77352 _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 56.61 _refine.ls_d_res_high 2.36 _refine.ls_percent_reflns_obs 97.00 _refine.ls_R_factor_obs 0.21371 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.21127 _refine.ls_R_factor_R_free 0.25839 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.0 _refine.ls_number_reflns_R_free 4094 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.931 _refine.correlation_coeff_Fo_to_Fc_free 0.896 _refine.B_iso_mean 61.609 _refine.aniso_B[1][1] -0.25 _refine.aniso_B[2][2] 4.18 _refine.aniso_B[3][3] -2.55 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] -0.83 _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. U VALUES WITH TLS ADDED' _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 0.325 _refine.pdbx_overall_ESU_R_Free 0.246 _refine.overall_SU_ML 0.196 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 14.973 _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 11019 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 191 _refine_hist.number_atoms_solvent 712 _refine_hist.number_atoms_total 11922 _refine_hist.d_res_high 2.36 _refine_hist.d_res_low 56.61 # 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 0.006 0.019 ? 11476 'X-RAY DIFFRACTION' ? r_bond_other_d 0.001 0.020 ? 10452 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.154 1.951 ? 15598 'X-RAY DIFFRACTION' ? r_angle_other_deg 0.683 3.003 ? 23983 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.593 5.000 ? 1394 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 36.368 25.132 ? 567 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 14.266 15.000 ? 1871 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 15.784 15.000 ? 52 'X-RAY DIFFRACTION' ? r_chiral_restr 0.060 0.200 ? 1702 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.004 0.020 ? 13165 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.001 0.020 ? 2704 'X-RAY DIFFRACTION' ? r_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it 0.503 1.997 ? 5594 'X-RAY DIFFRACTION' ? r_mcbond_other 0.503 1.997 ? 5593 'X-RAY DIFFRACTION' ? r_mcangle_it 0.854 2.994 ? 6982 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it 0.726 2.135 ? 5882 'X-RAY DIFFRACTION' ? r_scbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # loop_ _refine_ls_restr_ncs.dom_id _refine_ls_restr_ncs.pdbx_auth_asym_id _refine_ls_restr_ncs.pdbx_number _refine_ls_restr_ncs.rms_dev_position _refine_ls_restr_ncs.weight_position _refine_ls_restr_ncs.pdbx_type _refine_ls_restr_ncs.pdbx_ens_id _refine_ls_restr_ncs.pdbx_ordinal _refine_ls_restr_ncs.pdbx_refine_id _refine_ls_restr_ncs.ncs_model_details _refine_ls_restr_ncs.rms_dev_B_iso _refine_ls_restr_ncs.weight_B_iso 1 B 2097 0.25 0.50 'medium positional' 4 1 'X-RAY DIFFRACTION' ? ? ? 1 B 2105 0.26 0.50 'medium positional' 5 2 'X-RAY DIFFRACTION' ? ? ? 1 D 2162 0.26 0.50 'medium positional' 6 3 'X-RAY DIFFRACTION' ? ? ? 1 A 4940 0.40 5.00 'loose positional' 1 4 'X-RAY DIFFRACTION' ? ? ? 1 A 4912 0.39 5.00 'loose positional' 2 5 'X-RAY DIFFRACTION' ? ? ? 1 C 4912 0.33 5.00 'loose positional' 3 6 'X-RAY DIFFRACTION' ? ? ? 1 B 2097 2.92 2.00 'medium thermal' 4 7 'X-RAY DIFFRACTION' ? ? ? 1 B 2105 1.86 2.00 'medium thermal' 5 8 'X-RAY DIFFRACTION' ? ? ? 1 D 2162 2.46 2.00 'medium thermal' 6 9 'X-RAY DIFFRACTION' ? ? ? 1 A 4940 2.08 10.00 'loose thermal' 1 10 'X-RAY DIFFRACTION' ? ? ? 1 A 4912 2.65 10.00 'loose thermal' 2 11 'X-RAY DIFFRACTION' ? ? ? 1 C 4912 2.01 10.00 'loose thermal' 3 12 '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 2.360 _refine_ls_shell.d_res_low 2.421 _refine_ls_shell.number_reflns_R_work 5393 _refine_ls_shell.R_factor_R_work 0.284 _refine_ls_shell.percent_reflns_obs 90.54 _refine_ls_shell.R_factor_R_free 0.342 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 255 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # loop_ _struct_ncs_oper.id _struct_ncs_oper.code _struct_ncs_oper.details _struct_ncs_oper.matrix[1][1] _struct_ncs_oper.matrix[1][2] _struct_ncs_oper.matrix[1][3] _struct_ncs_oper.matrix[2][1] _struct_ncs_oper.matrix[2][2] _struct_ncs_oper.matrix[2][3] _struct_ncs_oper.matrix[3][1] _struct_ncs_oper.matrix[3][2] _struct_ncs_oper.matrix[3][3] _struct_ncs_oper.vector[1] _struct_ncs_oper.vector[2] _struct_ncs_oper.vector[3] 1 given ? 1.000000 0.000000 0.000000 0.000000 1.000000 0.000000 0.000000 0.000000 1.000000 0.00000 0.00000 0.00000 2 given ? -0.392666 -0.008014 0.919646 0.716377 0.624409 0.311316 -0.576730 0.781057 -0.239443 18.89738 -32.09268 54.58283 3 given ? 1.000000 0.000000 0.000000 0.000000 1.000000 0.000000 0.000000 0.000000 1.000000 0.00000 0.00000 0.00000 4 given ? -0.376872 0.715992 -0.587642 -0.011058 0.630898 0.775787 0.926199 0.298870 -0.229851 62.13623 -21.84333 5.12184 5 given ? 1.000000 0.000000 0.000000 0.000000 1.000000 0.000000 0.000000 0.000000 1.000000 0.00000 0.00000 0.00000 6 given ? -0.394129 -0.001629 0.919054 0.719583 0.621524 0.309690 -0.571719 0.783393 -0.243789 18.89107 -32.58561 54.79147 7 given ? 1.000000 0.000000 0.000000 0.000000 1.000000 0.000000 0.000000 0.000000 1.000000 0.00000 0.00000 0.00000 8 given ? -0.366657 -0.015503 0.930227 0.728046 0.617725 0.297261 -0.579233 0.786241 -0.215207 17.44633 -32.48622 54.28785 9 given ? 1.000000 0.000000 0.000000 0.000000 1.000000 0.000000 0.000000 0.000000 1.000000 0.00000 0.00000 0.00000 10 given ? -0.386056 0.721455 -0.574859 -0.020664 0.616251 0.787279 0.922244 0.315813 -0.222999 61.89149 -22.39217 5.54304 11 given ? 1.000000 0.000000 0.000000 0.000000 1.000000 0.000000 0.000000 0.000000 1.000000 0.00000 0.00000 0.00000 12 given ? -0.406836 0.001015 0.913501 0.718425 0.618007 0.319270 -0.564225 0.786172 -0.252157 19.24937 -32.75516 54.81853 # loop_ _struct_ncs_dom.id _struct_ncs_dom.details _struct_ncs_dom.pdbx_ens_id 1 A 1 2 C 1 1 A 2 2 E 2 1 C 3 2 E 3 1 B 4 2 D 4 1 B 5 2 F 5 1 D 6 2 F 6 # loop_ _struct_ncs_dom_lim.dom_id _struct_ncs_dom_lim.beg_auth_asym_id _struct_ncs_dom_lim.beg_auth_seq_id _struct_ncs_dom_lim.end_auth_asym_id _struct_ncs_dom_lim.end_auth_seq_id _struct_ncs_dom_lim.pdbx_component_id _struct_ncs_dom_lim.pdbx_refine_code _struct_ncs_dom_lim.beg_label_asym_id _struct_ncs_dom_lim.beg_label_comp_id _struct_ncs_dom_lim.beg_label_seq_id _struct_ncs_dom_lim.beg_label_alt_id _struct_ncs_dom_lim.end_label_asym_id _struct_ncs_dom_lim.end_label_comp_id _struct_ncs_dom_lim.end_label_seq_id _struct_ncs_dom_lim.end_label_alt_id _struct_ncs_dom_lim.pdbx_ens_id _struct_ncs_dom_lim.selection_details 1 A 1 A 319 1 6 ? ? ? ? ? ? ? ? 1 ? 2 C 1 C 319 1 6 ? ? ? ? ? ? ? ? 1 ? 1 A 1 A 318 1 6 ? ? ? ? ? ? ? ? 2 ? 2 E 1 E 318 1 6 ? ? ? ? ? ? ? ? 2 ? 1 C 1 C 318 1 6 ? ? ? ? ? ? ? ? 3 ? 2 E 1 E 318 1 6 ? ? ? ? ? ? ? ? 3 ? 1 B 10 B 154 1 4 ? ? ? ? ? ? ? ? 4 ? 2 D 10 D 154 1 4 ? ? ? ? ? ? ? ? 4 ? 1 B 10 B 154 1 4 ? ? ? ? ? ? ? ? 5 ? 2 F 10 F 154 1 4 ? ? ? ? ? ? ? ? 5 ? 1 D 10 D 157 1 4 ? ? ? ? ? ? ? ? 6 ? 2 F 10 F 157 1 4 ? ? ? ? ? ? ? ? 6 ? # loop_ _struct_ncs_ens.id _struct_ncs_ens.details 1 ? 2 ? 3 ? 4 ? 5 ? 6 ? # _struct.entry_id 4BH0 _struct.title ;H5 (tyTy) Influenza Virus Haemagglutinin in Complex with Human Receptor Analogue 6'-SLN ; _struct.pdbx_descriptor HEMAGGLUTININ _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4BH0 _struct_keywords.pdbx_keywords 'VIRAL PROTEIN' _struct_keywords.text 'VIRAL PROTEIN, N-GLYCOSYLATION, VIRUS RECEPTOR, BIRD FLU' # 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 1 ? D N N 2 ? E N N 1 ? F N N 2 ? G N N 3 ? H N N 4 ? I N N 5 ? J N N 6 ? K N N 6 ? L N N 6 ? M N N 3 ? N N N 4 ? O N N 5 ? P N N 3 ? Q N N 6 ? R N N 3 ? S N N 4 ? T N N 5 ? U N N 3 ? V N N 6 ? W N N 7 ? X N N 7 ? Y N N 7 ? Z N N 7 ? AA N N 7 ? BA N N 7 ? # _struct_biol.id 1 # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 SER A 57 ? GLY A 64 ? SER A 56 GLY A 63 1 ? 8 HELX_P HELX_P2 2 ASN A 65 ? LEU A 72 ? ASN A 64 LEU A 71 5 ? 8 HELX_P HELX_P3 3 ASP A 98 ? SER A 107 ? ASP A 97 SER A 106 1 ? 10 HELX_P HELX_P4 4 PRO A 119 ? TRP A 123 ? PRO A 118 TRP A 122 5 ? 5 HELX_P HELX_P5 5 ASP A 184 ? GLN A 193 ? ASP A 183 GLN A 192 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 ASN B 60 ? GLN B 62 ? ASN B 60 GLN B 62 5 ? 3 HELX_P HELX_P8 8 GLU B 74 ? LEU B 126 ? GLU B 74 LEU B 126 1 ? 53 HELX_P HELX_P9 9 ASP B 145 ? GLY B 155 ? ASP B 145 GLY B 155 1 ? 11 HELX_P HELX_P10 10 SER C 57 ? GLY C 64 ? SER C 56 GLY C 63 1 ? 8 HELX_P HELX_P11 11 ASN C 65 ? LEU C 72 ? ASN C 64 LEU C 71 5 ? 8 HELX_P HELX_P12 12 ASP C 98 ? SER C 107 ? ASP C 97 SER C 106 1 ? 10 HELX_P HELX_P13 13 PRO C 119 ? TRP C 123 ? PRO C 118 TRP C 122 5 ? 5 HELX_P HELX_P14 14 ASP C 184 ? GLN C 193 ? ASP C 183 GLN C 192 1 ? 10 HELX_P HELX_P15 15 ASP D 37 ? MET D 59 ? ASP D 37 MET D 59 1 ? 23 HELX_P HELX_P16 16 GLU D 74 ? LEU D 126 ? GLU D 74 LEU D 126 1 ? 53 HELX_P HELX_P17 17 ASP D 145 ? GLY D 155 ? ASP D 145 GLY D 155 1 ? 11 HELX_P HELX_P18 18 SER E 57 ? GLY E 64 ? SER E 56 GLY E 63 1 ? 8 HELX_P HELX_P19 19 ASN E 65 ? LEU E 72 ? ASN E 64 LEU E 71 5 ? 8 HELX_P HELX_P20 20 ASP E 98 ? SER E 107 ? ASP E 97 SER E 106 1 ? 10 HELX_P HELX_P21 21 PRO E 119 ? TRP E 123 ? PRO E 118 TRP E 122 5 ? 5 HELX_P HELX_P22 22 ASP E 184 ? GLN E 193 ? ASP E 183 GLN E 192 1 ? 10 HELX_P HELX_P23 23 ASP F 37 ? ASN F 60 ? ASP F 37 ASN F 60 1 ? 24 HELX_P HELX_P24 24 GLU F 74 ? LEU F 126 ? GLU F 74 LEU F 126 1 ? 53 HELX_P HELX_P25 25 ASP F 145 ? GLY F 155 ? ASP F 145 GLY F 155 1 ? 11 # _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 5 SG ? ? ? 1_555 B CYS 137 SG ? ? A CYS 4 B CYS 137 1_555 ? ? ? ? ? ? ? 2.033 ? disulf2 disulf ? ? A CYS 43 SG ? ? ? 1_555 A CYS 275 SG ? ? A CYS 42 A CYS 274 1_555 ? ? ? ? ? ? ? 2.050 ? disulf3 disulf ? ? A CYS 56 SG ? ? ? 1_555 A CYS 68 SG ? ? A CYS 55 A CYS 67 1_555 ? ? ? ? ? ? ? 2.053 ? disulf4 disulf ? ? A CYS 91 SG ? ? ? 1_555 A CYS 136 SG ? ? A CYS 90 A CYS 135 1_555 ? ? ? ? ? ? ? 2.076 ? disulf5 disulf ? ? A CYS 279 SG ? ? ? 1_555 A CYS 303 SG ? ? A CYS 278 A CYS 302 1_555 ? ? ? ? ? ? ? 2.039 ? disulf6 disulf ? ? B CYS 144 SG ? ? ? 1_555 B CYS 148 SG ? ? B CYS 144 B CYS 148 1_555 ? ? ? ? ? ? ? 2.038 ? disulf7 disulf ? ? C CYS 5 SG ? ? ? 1_555 D CYS 137 SG ? ? C CYS 4 D CYS 137 1_555 ? ? ? ? ? ? ? 2.036 ? disulf8 disulf ? ? C CYS 43 SG ? ? ? 1_555 C CYS 275 SG ? ? C CYS 42 C CYS 274 1_555 ? ? ? ? ? ? ? 2.047 ? disulf9 disulf ? ? C CYS 56 SG ? ? ? 1_555 C CYS 68 SG ? ? C CYS 55 C CYS 67 1_555 ? ? ? ? ? ? ? 2.069 ? disulf10 disulf ? ? C CYS 91 SG ? ? ? 1_555 C CYS 136 SG ? ? C CYS 90 C CYS 135 1_555 ? ? ? ? ? ? ? 2.099 ? disulf11 disulf ? ? C CYS 279 SG ? ? ? 1_555 C CYS 303 SG ? ? C CYS 278 C CYS 302 1_555 ? ? ? ? ? ? ? 2.041 ? disulf12 disulf ? ? D CYS 144 SG ? ? ? 1_555 D CYS 148 SG ? ? D CYS 144 D CYS 148 1_555 ? ? ? ? ? ? ? 2.032 ? disulf13 disulf ? ? E CYS 5 SG ? ? ? 1_555 F CYS 137 SG ? ? E CYS 4 F CYS 137 1_555 ? ? ? ? ? ? ? 2.035 ? disulf14 disulf ? ? E CYS 43 SG ? ? ? 1_555 E CYS 275 SG ? ? E CYS 42 E CYS 274 1_555 ? ? ? ? ? ? ? 2.040 ? disulf15 disulf ? ? E CYS 56 SG ? ? ? 1_555 E CYS 68 SG ? ? E CYS 55 E CYS 67 1_555 ? ? ? ? ? ? ? 2.070 ? disulf16 disulf ? ? E CYS 91 SG ? ? ? 1_555 E CYS 136 SG ? ? E CYS 90 E CYS 135 1_555 ? ? ? ? ? ? ? 2.101 ? disulf17 disulf ? ? E CYS 279 SG ? ? ? 1_555 E CYS 303 SG ? ? E CYS 278 E CYS 302 1_555 ? ? ? ? ? ? ? 2.050 ? disulf18 disulf ? ? F CYS 144 SG ? ? ? 1_555 F CYS 148 SG ? ? F CYS 144 F CYS 148 1_555 ? ? ? ? ? ? ? 2.050 ? covale1 covale ? ? A ASN 166 ND2 ? ? ? 1_555 G NAG . C1 ? ? A ASN 165 A NAG 1320 1_555 ? ? ? ? ? ? ? 1.442 ? covale2 covale ? ? I GAL . O6 ? ? ? 1_555 H SIA . C2 ? ? A GAL 1322 A SIA 1321 1_555 ? ? ? ? ? ? ? 1.436 ? covale3 covale ? ? C ASN 166 ND2 ? ? ? 1_555 M NAG . C1 ? ? C ASN 165 C NAG 1320 1_555 ? ? ? ? ? ? ? 1.450 ? covale4 covale ? ? O GAL . C1 ? ? ? 1_555 P NAG . O4 ? ? C GAL 1322 C NAG 1323 1_555 ? ? ? ? ? ? ? 1.431 ? covale5 covale ? ? O GAL . O6 ? ? ? 1_555 N SIA . C2 ? ? C GAL 1322 C SIA 1321 1_555 ? ? ? ? ? ? ? 1.434 ? covale6 covale ? ? E ASN 166 ND2 ? ? ? 1_555 R NAG . C1 ? ? E ASN 165 E NAG 1320 1_555 ? ? ? ? ? ? ? 1.456 ? covale7 covale ? ? T GAL . O6 ? ? ? 1_555 S SIA . C2 ? ? E GAL 1322 E SIA 1321 1_555 ? ? ? ? ? ? ? 1.419 ? covale8 covale ? ? T GAL . C1 ? ? ? 1_555 U NAG . O4 ? ? E GAL 1322 E NAG 1323 1_555 ? ? ? ? ? ? ? 1.434 ? # 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 BA ? 5 ? AA ? 2 ? AB ? 2 ? AC ? 3 ? AD ? 2 ? AE ? 3 ? AF ? 5 ? AG ? 5 ? AH ? 2 ? AI ? 4 ? AJ ? 3 ? DA ? 5 ? CA ? 2 ? CB ? 2 ? CC ? 3 ? CD ? 2 ? CE ? 3 ? CF ? 5 ? CG ? 5 ? CH ? 2 ? CI ? 4 ? CJ ? 3 ? FA ? 5 ? EA ? 2 ? EB ? 2 ? EC ? 3 ? ED ? 2 ? EE ? 3 ? EF ? 5 ? EG ? 5 ? EH ? 2 ? EI ? 4 ? EJ ? 2 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense BA 1 2 ? anti-parallel BA 2 3 ? anti-parallel BA 3 4 ? anti-parallel BA 4 5 ? anti-parallel AA 1 2 ? anti-parallel AB 1 2 ? anti-parallel AC 1 2 ? parallel AC 2 3 ? parallel AD 1 2 ? parallel AE 1 2 ? parallel AE 2 3 ? parallel AF 1 2 ? parallel AF 2 3 ? anti-parallel AF 3 4 ? anti-parallel AF 4 5 ? anti-parallel AG 1 2 ? parallel AG 2 3 ? anti-parallel AG 3 4 ? anti-parallel AG 4 5 ? anti-parallel AH 1 2 ? anti-parallel AI 1 2 ? anti-parallel AI 2 3 ? anti-parallel AI 3 4 ? anti-parallel AJ 1 2 ? anti-parallel AJ 2 3 ? anti-parallel DA 1 2 ? anti-parallel DA 2 3 ? anti-parallel DA 3 4 ? anti-parallel DA 4 5 ? anti-parallel CA 1 2 ? anti-parallel CB 1 2 ? anti-parallel CC 1 2 ? parallel CC 2 3 ? parallel CD 1 2 ? parallel CE 1 2 ? parallel CE 2 3 ? parallel CF 1 2 ? parallel CF 2 3 ? anti-parallel CF 3 4 ? anti-parallel CF 4 5 ? anti-parallel CG 1 2 ? parallel CG 2 3 ? anti-parallel CG 3 4 ? anti-parallel CG 4 5 ? anti-parallel CH 1 2 ? anti-parallel CI 1 2 ? anti-parallel CI 2 3 ? anti-parallel CI 3 4 ? anti-parallel CJ 1 2 ? anti-parallel CJ 2 3 ? anti-parallel FA 1 2 ? anti-parallel FA 2 3 ? anti-parallel FA 3 4 ? anti-parallel FA 4 5 ? anti-parallel EA 1 2 ? anti-parallel EB 1 2 ? anti-parallel EC 1 2 ? parallel EC 2 3 ? parallel ED 1 2 ? parallel EE 1 2 ? parallel EE 2 3 ? parallel EF 1 2 ? parallel EF 2 3 ? anti-parallel EF 3 4 ? anti-parallel EF 4 5 ? anti-parallel EG 1 2 ? parallel EG 2 3 ? anti-parallel EG 3 4 ? anti-parallel EG 4 5 ? anti-parallel EH 1 2 ? anti-parallel EI 1 2 ? anti-parallel EI 2 3 ? anti-parallel EI 3 4 ? anti-parallel EJ 1 2 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id BA 1 SER B 32 ? ALA B 36 ? SER B 32 ALA B 36 BA 2 TYR B 22 ? SER B 27 ? TYR B 22 SER B 27 BA 3 GLN A 3 ? TYR A 8 ? GLN A 2 TYR A 7 BA 4 CYS B 137 ? PHE B 140 ? CYS B 137 PHE B 140 BA 5 ALA B 130 ? GLU B 132 ? ALA B 130 GLU B 132 AA 1 GLN A 16 ? VAL A 17 ? GLN A 15 VAL A 16 AA 2 VAL A 25 ? THR A 26 ? VAL A 24 THR A 25 AB 1 ALA A 30 ? ASP A 32 ? ALA A 29 ASP A 31 AB 2 VAL A 313 ? ALA A 315 ? VAL A 312 ALA A 314 AC 1 LEU A 34 ? GLU A 35 ? LEU A 33 GLU A 34 AC 2 PHE A 292 ? HIS A 293 ? PHE A 291 HIS A 292 AC 3 LYS A 305 ? TYR A 306 ? LYS A 304 TYR A 305 AD 1 LEU A 42 ? LEU A 45 ? LEU A 41 LEU A 44 AD 2 TYR A 272 ? THR A 277 ? TYR A 271 THR A 276 AE 1 LEU A 51 ? ILE A 52 ? LEU A 50 ILE A 51 AE 2 ILE A 80 ? GLU A 82 ? ILE A 79 GLU A 81 AE 3 ILE A 265 ? LYS A 267 ? ILE A 264 LYS A 266 AF 1 GLY A 94 ? PHE A 96 ? GLY A 93 PHE A 95 AF 2 ARG A 226 ? LEU A 234 ? ARG A 225 LEU A 233 AF 3 LEU A 173 ? HIS A 181 ? LEU A 172 HIS A 180 AF 4 PHE A 248 ? PRO A 251 ? PHE A 247 PRO A 250 AF 5 VAL A 148 ? TRP A 150 ? VAL A 147 TRP A 149 AG 1 GLY A 94 ? PHE A 96 ? GLY A 93 PHE A 95 AG 2 ARG A 226 ? LEU A 234 ? ARG A 225 LEU A 233 AG 3 LEU A 173 ? HIS A 181 ? LEU A 172 HIS A 180 AG 4 ASN A 253 ? LYS A 260 ? ASN A 252 LYS A 259 AG 5 ILE A 109 ? GLN A 116 ? ILE A 108 GLN A 115 AH 1 SER A 133 ? TYR A 138 ? SER A 132 TYR A 137 AH 2 ARG A 141 ? SER A 143 ? ARG A 140 SER A 142 AI 1 ILE A 161 ? ASN A 166 ? ILE A 160 ASN A 165 AI 2 ALA A 239 ? SER A 244 ? ALA A 238 SER A 243 AI 3 ILE A 199 ? GLY A 202 ? ILE A 198 GLY A 201 AI 4 ASN A 207 ? LEU A 210 ? ASN A 206 LEU A 209 AJ 1 GLY A 284 ? ALA A 285 ? GLY A 283 ALA A 284 AJ 2 CYS A 279 ? THR A 281 ? CYS A 278 THR A 280 AJ 3 ILE A 300 ? GLY A 301 ? ILE A 299 GLY A 300 DA 1 SER D 32 ? ALA D 36 ? SER D 32 ALA D 36 DA 2 TYR D 22 ? SER D 27 ? TYR D 22 SER D 27 DA 3 GLN C 3 ? TYR C 8 ? GLN C 2 TYR C 7 DA 4 CYS D 137 ? PHE D 140 ? CYS D 137 PHE D 140 DA 5 ALA D 130 ? GLU D 132 ? ALA D 130 GLU D 132 CA 1 GLU C 15 ? VAL C 17 ? GLU C 14 VAL C 16 CA 2 VAL C 25 ? VAL C 27 ? VAL C 24 VAL C 26 CB 1 ALA C 30 ? ASP C 32 ? ALA C 29 ASP C 31 CB 2 VAL C 313 ? ALA C 315 ? VAL C 312 ALA C 314 CC 1 LEU C 34 ? GLU C 35 ? LEU C 33 GLU C 34 CC 2 PHE C 292 ? HIS C 293 ? PHE C 291 HIS C 292 CC 3 LYS C 305 ? TYR C 306 ? LYS C 304 TYR C 305 CD 1 LEU C 42 ? LEU C 45 ? LEU C 41 LEU C 44 CD 2 TYR C 272 ? THR C 277 ? TYR C 271 THR C 276 CE 1 LEU C 51 ? ILE C 52 ? LEU C 50 ILE C 51 CE 2 ILE C 80 ? GLU C 82 ? ILE C 79 GLU C 81 CE 3 ILE C 265 ? LYS C 267 ? ILE C 264 LYS C 266 CF 1 GLY C 94 ? PHE C 96 ? GLY C 93 PHE C 95 CF 2 ARG C 226 ? LEU C 234 ? ARG C 225 LEU C 233 CF 3 LEU C 173 ? HIS C 181 ? LEU C 172 HIS C 180 CF 4 PHE C 248 ? PRO C 251 ? PHE C 247 PRO C 250 CF 5 VAL C 148 ? TRP C 150 ? VAL C 147 TRP C 149 CG 1 GLY C 94 ? PHE C 96 ? GLY C 93 PHE C 95 CG 2 ARG C 226 ? LEU C 234 ? ARG C 225 LEU C 233 CG 3 LEU C 173 ? HIS C 181 ? LEU C 172 HIS C 180 CG 4 ASN C 253 ? LYS C 260 ? ASN C 252 LYS C 259 CG 5 ILE C 109 ? GLN C 116 ? ILE C 108 GLN C 115 CH 1 SER C 133 ? TYR C 138 ? SER C 132 TYR C 137 CH 2 ARG C 141 ? SER C 143 ? ARG C 140 SER C 142 CI 1 ILE C 161 ? ASN C 166 ? ILE C 160 ASN C 165 CI 2 ALA C 239 ? SER C 244 ? ALA C 238 SER C 243 CI 3 ILE C 199 ? GLY C 202 ? ILE C 198 GLY C 201 CI 4 ASN C 207 ? LEU C 210 ? ASN C 206 LEU C 209 CJ 1 ALA C 285 ? ILE C 286 ? ALA C 284 ILE C 285 CJ 2 CYS C 279 ? GLN C 280 ? CYS C 278 GLN C 279 CJ 3 ILE C 300 ? GLY C 301 ? ILE C 299 GLY C 300 FA 1 SER F 32 ? ALA F 36 ? SER F 32 ALA F 36 FA 2 TYR F 22 ? SER F 27 ? TYR F 22 SER F 27 FA 3 GLN E 3 ? TYR E 8 ? GLN E 2 TYR E 7 FA 4 CYS F 137 ? PHE F 140 ? CYS F 137 PHE F 140 FA 5 ALA F 130 ? GLU F 132 ? ALA F 130 GLU F 132 EA 1 GLN E 16 ? VAL E 17 ? GLN E 15 VAL E 16 EA 2 VAL E 25 ? THR E 26 ? VAL E 24 THR E 25 EB 1 ALA E 30 ? ASP E 32 ? ALA E 29 ASP E 31 EB 2 VAL E 313 ? ALA E 315 ? VAL E 312 ALA E 314 EC 1 LEU E 34 ? GLU E 35 ? LEU E 33 GLU E 34 EC 2 PHE E 292 ? HIS E 293 ? PHE E 291 HIS E 292 EC 3 LYS E 305 ? TYR E 306 ? LYS E 304 TYR E 305 ED 1 LEU E 42 ? LEU E 45 ? LEU E 41 LEU E 44 ED 2 TYR E 272 ? THR E 277 ? TYR E 271 THR E 276 EE 1 LEU E 51 ? ILE E 52 ? LEU E 50 ILE E 51 EE 2 ILE E 80 ? GLU E 82 ? ILE E 79 GLU E 81 EE 3 ILE E 265 ? LYS E 267 ? ILE E 264 LYS E 266 EF 1 GLY E 94 ? PHE E 96 ? GLY E 93 PHE E 95 EF 2 ARG E 226 ? LEU E 234 ? ARG E 225 LEU E 233 EF 3 LEU E 173 ? HIS E 181 ? LEU E 172 HIS E 180 EF 4 PHE E 248 ? PRO E 251 ? PHE E 247 PRO E 250 EF 5 VAL E 148 ? TRP E 150 ? VAL E 147 TRP E 149 EG 1 GLY E 94 ? PHE E 96 ? GLY E 93 PHE E 95 EG 2 ARG E 226 ? LEU E 234 ? ARG E 225 LEU E 233 EG 3 LEU E 173 ? HIS E 181 ? LEU E 172 HIS E 180 EG 4 ASN E 253 ? LYS E 260 ? ASN E 252 LYS E 259 EG 5 ILE E 109 ? GLN E 116 ? ILE E 108 GLN E 115 EH 1 SER E 133 ? TYR E 138 ? SER E 132 TYR E 137 EH 2 ARG E 141 ? SER E 143 ? ARG E 140 SER E 142 EI 1 ILE E 161 ? ASN E 166 ? ILE E 160 ASN E 165 EI 2 ALA E 239 ? SER E 244 ? ALA E 238 SER E 243 EI 3 ILE E 199 ? GLY E 202 ? ILE E 198 GLY E 201 EI 4 ASN E 207 ? LEU E 210 ? ASN E 206 LEU E 209 EJ 1 CYS E 279 ? GLN E 280 ? CYS E 278 GLN E 279 EJ 2 ILE E 300 ? GLY E 301 ? ILE E 299 GLY E 300 # 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 BA 1 2 N ALA B 35 ? N ALA B 35 O TYR B 24 ? O TYR B 24 BA 2 3 N SER B 27 ? N SER B 27 O GLN A 3 ? O GLN A 2 BA 3 4 N ILE A 4 ? N ILE A 3 O PHE B 138 ? O PHE B 138 BA 4 5 N GLU B 139 ? N GLU B 139 O LYS B 131 ? O LYS B 131 AA 1 2 N VAL A 17 ? N VAL A 16 O VAL A 25 ? O VAL A 24 AB 1 2 N GLN A 31 ? N GLN A 30 O LEU A 314 ? O LEU A 313 AC 1 2 N GLU A 35 ? N GLU A 34 O PHE A 292 ? O PHE A 291 AC 2 3 N HIS A 293 ? N HIS A 292 O LYS A 305 ? O LYS A 304 AD 1 2 O LEU A 42 ? O LEU A 41 N GLY A 273 ? N GLY A 272 AE 1 2 O LEU A 51 ? O LEU A 50 N VAL A 81 ? N VAL A 80 AE 2 3 N GLU A 82 ? N GLU A 81 O MET A 266 ? O MET A 265 AF 1 2 N ASN A 95 ? N ASN A 94 O MET A 227 ? O MET A 226 AF 2 3 N LEU A 234 ? N LEU A 233 O LEU A 173 ? O LEU A 172 AF 3 4 N GLY A 178 ? N GLY A 177 O ILE A 249 ? O ILE A 248 AF 4 5 N ALA A 250 ? N ALA A 249 O VAL A 149 ? O VAL A 148 AG 1 2 N ASN A 95 ? N ASN A 94 O MET A 227 ? O MET A 226 AG 2 3 N LEU A 234 ? N LEU A 233 O LEU A 173 ? O LEU A 172 AG 3 4 N LEU A 174 ? N LEU A 173 O TYR A 255 ? O TYR A 254 AG 4 5 O LYS A 259 ? O LYS A 258 N ASN A 110 ? N ASN A 109 AH 1 2 N TYR A 138 ? N TYR A 137 O ARG A 141 ? O ARG A 140 AI 1 2 N TYR A 165 ? N TYR A 164 O ILE A 240 ? O ILE A 239 AI 2 3 N GLU A 243 ? N GLU A 242 O SER A 200 ? O SER A 199 AI 3 4 N VAL A 201 ? N VAL A 200 O GLN A 208 ? O GLN A 207 AJ 1 2 N GLY A 284 ? N GLY A 283 O THR A 281 ? O THR A 280 AJ 2 3 N GLN A 280 ? N GLN A 279 O ILE A 300 ? O ILE A 299 DA 1 2 N ALA D 35 ? N ALA D 35 O TYR D 24 ? O TYR D 24 DA 2 3 N SER D 27 ? N SER D 27 O GLN C 3 ? O GLN C 2 DA 3 4 N ILE C 4 ? N ILE C 3 O PHE D 138 ? O PHE D 138 DA 4 5 N GLU D 139 ? N GLU D 139 O LYS D 131 ? O LYS D 131 CA 1 2 N VAL C 17 ? N VAL C 16 O VAL C 25 ? O VAL C 24 CB 1 2 N GLN C 31 ? N GLN C 30 O LEU C 314 ? O LEU C 313 CC 1 2 N GLU C 35 ? N GLU C 34 O PHE C 292 ? O PHE C 291 CC 2 3 N HIS C 293 ? N HIS C 292 O LYS C 305 ? O LYS C 304 CD 1 2 O LEU C 42 ? O LEU C 41 N GLY C 273 ? N GLY C 272 CE 1 2 O LEU C 51 ? O LEU C 50 N VAL C 81 ? N VAL C 80 CE 2 3 N GLU C 82 ? N GLU C 81 O MET C 266 ? O MET C 265 CF 1 2 N ASN C 95 ? N ASN C 94 O MET C 227 ? O MET C 226 CF 2 3 N LEU C 234 ? N LEU C 233 O LEU C 173 ? O LEU C 172 CF 3 4 N GLY C 178 ? N GLY C 177 O ILE C 249 ? O ILE C 248 CF 4 5 N ALA C 250 ? N ALA C 249 O VAL C 149 ? O VAL C 148 CG 1 2 N ASN C 95 ? N ASN C 94 O MET C 227 ? O MET C 226 CG 2 3 N LEU C 234 ? N LEU C 233 O LEU C 173 ? O LEU C 172 CG 3 4 N LEU C 174 ? N LEU C 173 O TYR C 255 ? O TYR C 254 CG 4 5 O LYS C 259 ? O LYS C 258 N ASN C 110 ? N ASN C 109 CH 1 2 N TYR C 138 ? N TYR C 137 O ARG C 141 ? O ARG C 140 CI 1 2 N TYR C 165 ? N TYR C 164 O ILE C 240 ? O ILE C 239 CI 2 3 N GLU C 243 ? N GLU C 242 O SER C 200 ? O SER C 199 CI 3 4 N VAL C 201 ? N VAL C 200 O GLN C 208 ? O GLN C 207 CJ 1 2 N ILE C 286 ? N ILE C 285 O CYS C 279 ? O CYS C 278 CJ 2 3 N GLN C 280 ? N GLN C 279 O ILE C 300 ? O ILE C 299 FA 1 2 N ALA F 35 ? N ALA F 35 O TYR F 24 ? O TYR F 24 FA 2 3 N SER F 27 ? N SER F 27 O GLN E 3 ? O GLN E 2 FA 3 4 N ILE E 4 ? N ILE E 3 O PHE F 138 ? O PHE F 138 FA 4 5 N GLU F 139 ? N GLU F 139 O LYS F 131 ? O LYS F 131 EA 1 2 N VAL E 17 ? N VAL E 16 O VAL E 25 ? O VAL E 24 EB 1 2 N GLN E 31 ? N GLN E 30 O LEU E 314 ? O LEU E 313 EC 1 2 N GLU E 35 ? N GLU E 34 O PHE E 292 ? O PHE E 291 EC 2 3 N HIS E 293 ? N HIS E 292 O LYS E 305 ? O LYS E 304 ED 1 2 O LEU E 42 ? O LEU E 41 N GLY E 273 ? N GLY E 272 EE 1 2 O LEU E 51 ? O LEU E 50 N VAL E 81 ? N VAL E 80 EE 2 3 N GLU E 82 ? N GLU E 81 O MET E 266 ? O MET E 265 EF 1 2 N ASN E 95 ? N ASN E 94 O MET E 227 ? O MET E 226 EF 2 3 N LEU E 234 ? N LEU E 233 O LEU E 173 ? O LEU E 172 EF 3 4 N GLY E 178 ? N GLY E 177 O ILE E 249 ? O ILE E 248 EF 4 5 N ALA E 250 ? N ALA E 249 O VAL E 149 ? O VAL E 148 EG 1 2 N ASN E 95 ? N ASN E 94 O MET E 227 ? O MET E 226 EG 2 3 N LEU E 234 ? N LEU E 233 O LEU E 173 ? O LEU E 172 EG 3 4 N LEU E 174 ? N LEU E 173 O TYR E 255 ? O TYR E 254 EG 4 5 O LYS E 259 ? O LYS E 258 N ASN E 110 ? N ASN E 109 EH 1 2 N TYR E 138 ? N TYR E 137 O ARG E 141 ? O ARG E 140 EI 1 2 N TYR E 165 ? N TYR E 164 O ILE E 240 ? O ILE E 239 EI 2 3 N GLU E 243 ? N GLU E 242 O SER E 200 ? O SER E 199 EI 3 4 N VAL E 201 ? N VAL E 200 O GLN E 208 ? O GLN E 207 EJ 1 2 N GLN E 280 ? N GLN E 279 O ILE E 300 ? O ILE E 299 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE PO4 A 1323' AC2 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE PO4 A 1324' AC3 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE PO4 E 1324' AC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE PO4 C 1324' AC5 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE PO4 A 1325' AC6 Software ? ? ? ? 5 'Binding site for Mono-Saccharide NAG A1320 bound to ASN A 165' AC7 Software ? ? ? ? 5 'Binding site for Mono-Saccharide NAG C1320 bound to ASN C 165' AC8 Software ? ? ? ? 4 'Binding site for Mono-Saccharide NAG E1320 bound to ASN E 165' AC9 Software ? ? ? ? 14 'Binding site for Poly-Saccharide residues SIA A1321 through GAL A1322' BC1 Software ? ? ? ? 17 'Binding site for Poly-Saccharide residues SIA C1321 through NAG C1323' BC2 Software ? ? ? ? 31 'Binding site for Poly-Saccharide residues SIA E1321 through NAG E1323' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 6 ILE A 179 ? ILE A 178 . ? 1_555 ? 2 AC1 6 HIS A 181 ? HIS A 180 . ? 1_555 ? 3 AC1 6 LEU A 210 ? LEU A 209 . ? 1_555 ? 4 AC1 6 VAL A 211 ? VAL A 210 . ? 1_555 ? 5 AC1 6 LYS A 213 ? LYS A 212 . ? 1_555 ? 6 AC1 6 GLU A 228 ? GLU A 227 . ? 1_555 ? 7 AC2 7 SER A 122 ? SER A 121 . ? 1_555 ? 8 AC2 7 TRP A 123 ? TRP A 122 . ? 1_555 ? 9 AC2 7 SER A 124 ? SER A 123 . ? 1_555 ? 10 AC2 7 ASP A 125 ? ASP A 124 . ? 1_555 ? 11 AC2 7 HIS A 126 ? HIS A 125 . ? 1_555 ? 12 AC2 7 ARG A 163 ? ARG A 162 . ? 1_555 ? 13 AC2 7 HOH W . ? HOH A 2091 . ? 1_555 ? 14 AC3 7 SER E 122 ? SER E 121 . ? 1_555 ? 15 AC3 7 TRP E 123 ? TRP E 122 . ? 1_555 ? 16 AC3 7 SER E 124 ? SER E 123 . ? 1_555 ? 17 AC3 7 ASP E 125 ? ASP E 124 . ? 1_555 ? 18 AC3 7 HIS E 126 ? HIS E 125 . ? 1_555 ? 19 AC3 7 ARG E 163 ? ARG E 162 . ? 1_555 ? 20 AC3 7 HOH AA . ? HOH E 2109 . ? 1_555 ? 21 AC4 5 SER C 122 ? SER C 121 . ? 1_555 ? 22 AC4 5 TRP C 123 ? TRP C 122 . ? 1_555 ? 23 AC4 5 SER C 124 ? SER C 123 . ? 1_555 ? 24 AC4 5 ASP C 125 ? ASP C 124 . ? 1_555 ? 25 AC4 5 HIS C 126 ? HIS C 125 . ? 1_555 ? 26 AC5 9 LYS A 103 ? LYS A 102 . ? 1_555 ? 27 AC5 9 HIS A 104 ? HIS A 103 . ? 1_555 ? 28 AC5 9 SER A 107 ? SER A 106 . ? 1_555 ? 29 AC5 9 ILE A 265 ? ILE A 264 . ? 1_555 ? 30 AC5 9 HOH W . ? HOH A 2145 . ? 1_555 ? 31 AC5 9 HOH W . ? HOH A 2180 . ? 1_555 ? 32 AC5 9 GLY B 67 ? GLY B 67 . ? 1_555 ? 33 AC5 9 ARG B 68 ? ARG B 68 . ? 1_555 ? 34 AC5 9 GLU B 69 ? GLU B 69 . ? 1_555 ? 35 AC6 5 ASN A 166 ? ASN A 165 . ? 1_555 ? 36 AC6 5 ASN A 237 ? ASN A 236 . ? 1_555 ? 37 AC6 5 ALA A 239 ? ALA A 238 . ? 1_555 ? 38 AC6 5 HOH W . ? HOH A 2100 . ? 1_555 ? 39 AC6 5 HOH W . ? HOH A 2176 . ? 1_555 ? 40 AC7 5 SER A 218 ? SER A 217 . ? 1_555 ? 41 AC7 5 ASN C 166 ? ASN C 165 . ? 1_555 ? 42 AC7 5 ASN C 237 ? ASN C 236 . ? 1_555 ? 43 AC7 5 HOH Y . ? HOH C 2131 . ? 1_555 ? 44 AC7 5 HOH Y . ? HOH C 2132 . ? 1_555 ? 45 AC8 4 SER C 218 ? SER C 217 . ? 1_555 ? 46 AC8 4 ASN E 166 ? ASN E 165 . ? 1_555 ? 47 AC8 4 ASN E 237 ? ASN E 236 . ? 1_555 ? 48 AC8 4 ALA E 239 ? ALA E 238 . ? 1_555 ? 49 AC9 14 TYR A 92 ? TYR A 91 . ? 1_555 ? 50 AC9 14 ALA A 130 ? ALA A 129 . ? 1_555 ? 51 AC9 14 VAL A 132 ? VAL A 131 . ? 1_555 ? 52 AC9 14 SER A 133 ? SER A 132 . ? 1_555 ? 53 AC9 14 SER A 134 ? SER A 133 . ? 1_555 ? 54 AC9 14 TRP A 150 ? TRP A 149 . ? 1_555 ? 55 AC9 14 HIS A 180 ? HIS A 179 . ? 1_555 ? 56 AC9 14 GLU A 187 ? GLU A 186 . ? 1_555 ? 57 AC9 14 ARG A 190 ? ARG A 189 . ? 1_555 ? 58 AC9 14 LYS A 219 ? LYS A 218 . ? 1_555 ? 59 AC9 14 GLY A 222 ? GLY A 221 . ? 1_555 ? 60 AC9 14 GLN A 223 ? GLN A 222 . ? 1_555 ? 61 AC9 14 HOH W . ? HOH A 2060 . ? 1_555 ? 62 AC9 14 HOH W . ? HOH A 2179 . ? 1_555 ? 63 BC1 17 TYR C 92 ? TYR C 91 . ? 1_555 ? 64 BC1 17 ALA C 130 ? ALA C 129 . ? 1_555 ? 65 BC1 17 VAL C 132 ? VAL C 131 . ? 1_555 ? 66 BC1 17 SER C 133 ? SER C 132 . ? 1_555 ? 67 BC1 17 SER C 134 ? SER C 133 . ? 1_555 ? 68 BC1 17 HIS C 180 ? HIS C 179 . ? 1_555 ? 69 BC1 17 ASN C 183 ? ASN C 182 . ? 1_555 ? 70 BC1 17 GLU C 187 ? GLU C 186 . ? 1_555 ? 71 BC1 17 LEU C 191 ? LEU C 190 . ? 1_555 ? 72 BC1 17 LYS C 219 ? LYS C 218 . ? 1_555 ? 73 BC1 17 GLY C 222 ? GLY C 221 . ? 1_555 ? 74 BC1 17 GLN C 223 ? GLN C 222 . ? 1_555 ? 75 BC1 17 HOH Y . ? HOH C 2070 . ? 1_555 ? 76 BC1 17 HOH Y . ? HOH C 2104 . ? 1_555 ? 77 BC1 17 HOH Y . ? HOH C 2206 . ? 1_555 ? 78 BC1 17 HOH Y . ? HOH C 2207 . ? 1_555 ? 79 BC1 17 HOH Y . ? HOH C 2208 . ? 1_555 ? 80 BC2 31 TYR C 92 ? TYR C 91 . ? 1_555 ? 81 BC2 31 ALA C 130 ? ALA C 129 . ? 1_555 ? 82 BC2 31 VAL C 132 ? VAL C 131 . ? 1_555 ? 83 BC2 31 SER C 133 ? SER C 132 . ? 1_555 ? 84 BC2 31 SER C 134 ? SER C 133 . ? 1_555 ? 85 BC2 31 HIS C 180 ? HIS C 179 . ? 1_555 ? 86 BC2 31 ASN C 183 ? ASN C 182 . ? 1_555 ? 87 BC2 31 GLU C 187 ? GLU C 186 . ? 1_555 ? 88 BC2 31 LEU C 191 ? LEU C 190 . ? 1_555 ? 89 BC2 31 LYS C 219 ? LYS C 218 . ? 1_555 ? 90 BC2 31 GLY C 222 ? GLY C 221 . ? 1_555 ? 91 BC2 31 GLN C 223 ? GLN C 222 . ? 1_555 ? 92 BC2 31 HOH Y . ? HOH C 2070 . ? 1_555 ? 93 BC2 31 HOH Y . ? HOH C 2104 . ? 1_555 ? 94 BC2 31 HOH Y . ? HOH C 2206 . ? 1_555 ? 95 BC2 31 HOH Y . ? HOH C 2207 . ? 1_555 ? 96 BC2 31 HOH Y . ? HOH C 2208 . ? 1_555 ? 97 BC2 31 TYR E 92 ? TYR E 91 . ? 1_555 ? 98 BC2 31 ALA E 130 ? ALA E 129 . ? 1_555 ? 99 BC2 31 VAL E 132 ? VAL E 131 . ? 1_555 ? 100 BC2 31 SER E 133 ? SER E 132 . ? 1_555 ? 101 BC2 31 SER E 134 ? SER E 133 . ? 1_555 ? 102 BC2 31 TRP E 150 ? TRP E 149 . ? 1_555 ? 103 BC2 31 HIS E 180 ? HIS E 179 . ? 1_555 ? 104 BC2 31 GLU E 187 ? GLU E 186 . ? 1_555 ? 105 BC2 31 LEU E 191 ? LEU E 190 . ? 1_555 ? 106 BC2 31 GLY E 222 ? GLY E 221 . ? 1_555 ? 107 BC2 31 GLN E 223 ? GLN E 222 . ? 1_555 ? 108 BC2 31 HOH AA . ? HOH E 2055 . ? 1_555 ? 109 BC2 31 HOH AA . ? HOH E 2096 . ? 1_555 ? 110 BC2 31 HOH AA . ? HOH E 2176 . ? 1_555 ? # _database_PDB_matrix.entry_id 4BH0 _database_PDB_matrix.origx[1][1] 1.000000 _database_PDB_matrix.origx[1][2] 0.000000 _database_PDB_matrix.origx[1][3] 0.000000 _database_PDB_matrix.origx[2][1] 0.000000 _database_PDB_matrix.origx[2][2] 1.000000 _database_PDB_matrix.origx[2][3] 0.000000 _database_PDB_matrix.origx[3][1] 0.000000 _database_PDB_matrix.origx[3][2] 0.000000 _database_PDB_matrix.origx[3][3] 1.000000 _database_PDB_matrix.origx_vector[1] 0.00000 _database_PDB_matrix.origx_vector[2] 0.00000 _database_PDB_matrix.origx_vector[3] 0.00000 # _atom_sites.entry_id 4BH0 _atom_sites.fract_transf_matrix[1][1] 0.014215 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.006332 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.004380 _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] 0.015361 _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 P 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 . ASP A 1 2 ? -4.584 -61.968 -17.505 1.00 181.64 ? 1 ASP A N 1 ATOM 2 C CA . ASP A 1 2 ? -3.348 -62.324 -18.266 1.00 176.62 ? 1 ASP A CA 1 ATOM 3 C C . ASP A 1 2 ? -2.090 -62.002 -17.469 1.00 168.57 ? 1 ASP A C 1 ATOM 4 O O . ASP A 1 2 ? -1.312 -62.894 -17.130 1.00 163.30 ? 1 ASP A O 1 ATOM 5 C CB . ASP A 1 2 ? -3.301 -61.572 -19.600 1.00 180.67 ? 1 ASP A CB 1 ATOM 6 C CG . ASP A 1 2 ? -4.440 -61.943 -20.521 1.00 189.34 ? 1 ASP A CG 1 ATOM 7 O OD1 . ASP A 1 2 ? -4.609 -63.148 -20.804 1.00 189.98 ? 1 ASP A OD1 1 ATOM 8 O OD2 . ASP A 1 2 ? -5.162 -61.029 -20.971 1.00 195.79 ? 1 ASP A OD2 1 ATOM 9 N N . GLN A 1 3 ? -1.902 -60.718 -17.175 1.00 168.15 ? 2 GLN A N 1 ATOM 10 C CA . GLN A 1 3 ? -0.665 -60.231 -16.574 1.00 161.53 ? 2 GLN A CA 1 ATOM 11 C C . GLN A 1 3 ? -0.910 -58.931 -15.805 1.00 161.97 ? 2 GLN A C 1 ATOM 12 O O . GLN A 1 3 ? -1.900 -58.235 -16.040 1.00 167.94 ? 2 GLN A O 1 ATOM 13 C CB . GLN A 1 3 ? 0.387 -60.011 -17.671 1.00 159.78 ? 2 GLN A CB 1 ATOM 14 C CG . GLN A 1 3 ? 1.825 -59.955 -17.172 1.00 152.73 ? 2 GLN A CG 1 ATOM 15 C CD . GLN A 1 3 ? 2.822 -59.641 -18.272 1.00 152.07 ? 2 GLN A CD 1 ATOM 16 O OE1 . GLN A 1 3 ? 3.639 -58.727 -18.139 1.00 149.43 ? 2 GLN A OE1 1 ATOM 17 N NE2 . GLN A 1 3 ? 2.760 -60.395 -19.365 1.00 154.76 ? 2 GLN A NE2 1 ATOM 18 N N . ILE A 1 4 ? -0.006 -58.621 -14.880 1.00 156.19 ? 3 ILE A N 1 ATOM 19 C CA . ILE A 1 4 ? -0.080 -57.394 -14.091 1.00 155.88 ? 3 ILE A CA 1 ATOM 20 C C . ILE A 1 4 ? 1.327 -56.909 -13.725 1.00 149.26 ? 3 ILE A C 1 ATOM 21 O O . ILE A 1 4 ? 2.243 -57.717 -13.560 1.00 144.99 ? 3 ILE A O 1 ATOM 22 C CB . ILE A 1 4 ? -0.932 -57.607 -12.820 1.00 157.91 ? 3 ILE A CB 1 ATOM 23 C CG1 . ILE A 1 4 ? -1.162 -56.279 -12.096 1.00 158.83 ? 3 ILE A CG1 1 ATOM 24 C CG2 . ILE A 1 4 ? -0.286 -58.632 -11.891 1.00 153.28 ? 3 ILE A CG2 1 ATOM 25 C CD1 . ILE A 1 4 ? -2.172 -56.366 -10.979 1.00 162.91 ? 3 ILE A CD1 1 ATOM 26 N N . CYS A 1 5 ? 1.489 -55.589 -13.613 1.00 148.88 ? 4 CYS A N 1 ATOM 27 C CA . CYS A 1 5 ? 2.786 -54.979 -13.302 1.00 143.20 ? 4 CYS A CA 1 ATOM 28 C C . CYS A 1 5 ? 2.648 -53.799 -12.338 1.00 141.74 ? 4 CYS A C 1 ATOM 29 O O . CYS A 1 5 ? 1.680 -53.040 -12.411 1.00 145.75 ? 4 CYS A O 1 ATOM 30 C CB . CYS A 1 5 ? 3.471 -54.512 -14.590 1.00 143.96 ? 4 CYS A CB 1 ATOM 31 S SG . CYS A 1 5 ? 3.805 -55.832 -15.786 1.00 145.54 ? 4 CYS A SG 1 ATOM 32 N N . ILE A 1 6 ? 3.628 -53.656 -11.445 1.00 136.07 ? 5 ILE A N 1 ATOM 33 C CA . ILE A 1 6 ? 3.679 -52.548 -10.482 1.00 134.36 ? 5 ILE A CA 1 ATOM 34 C C . ILE A 1 6 ? 4.573 -51.437 -11.040 1.00 131.59 ? 5 ILE A C 1 ATOM 35 O O . ILE A 1 6 ? 5.489 -51.708 -11.823 1.00 129.91 ? 5 ILE A O 1 ATOM 36 C CB . ILE A 1 6 ? 4.238 -53.005 -9.109 1.00 130.91 ? 5 ILE A CB 1 ATOM 37 C CG1 . ILE A 1 6 ? 3.518 -54.265 -8.604 1.00 133.00 ? 5 ILE A CG1 1 ATOM 38 C CG2 . ILE A 1 6 ? 4.136 -51.888 -8.073 1.00 130.74 ? 5 ILE A CG2 1 ATOM 39 C CD1 . ILE A 1 6 ? 2.051 -54.069 -8.289 1.00 138.61 ? 5 ILE A CD1 1 ATOM 40 N N . GLY A 1 7 ? 4.301 -50.193 -10.647 1.00 131.50 ? 6 GLY A N 1 ATOM 41 C CA . GLY A 1 7 ? 5.093 -49.052 -11.111 1.00 128.93 ? 6 GLY A CA 1 ATOM 42 C C . GLY A 1 7 ? 4.857 -47.769 -10.335 1.00 128.35 ? 6 GLY A C 1 ATOM 43 O O . GLY A 1 7 ? 4.187 -47.770 -9.299 1.00 129.25 ? 6 GLY A O 1 ATOM 44 N N . TYR A 1 8 ? 5.410 -46.673 -10.853 1.00 126.98 ? 7 TYR A N 1 ATOM 45 C CA . TYR A 1 8 ? 5.371 -45.376 -10.172 1.00 126.10 ? 7 TYR A CA 1 ATOM 46 C C . TYR A 1 8 ? 5.335 -44.196 -11.146 1.00 127.95 ? 7 TYR A C 1 ATOM 47 O O . TYR A 1 8 ? 5.829 -44.291 -12.268 1.00 128.50 ? 7 TYR A O 1 ATOM 48 C CB . TYR A 1 8 ? 6.577 -45.237 -9.242 1.00 120.72 ? 7 TYR A CB 1 ATOM 49 C CG . TYR A 1 8 ? 7.925 -45.421 -9.917 1.00 117.51 ? 7 TYR A CG 1 ATOM 50 C CD1 . TYR A 1 8 ? 8.532 -44.374 -10.610 1.00 117.25 ? 7 TYR A CD1 1 ATOM 51 C CD2 . TYR A 1 8 ? 8.603 -46.636 -9.846 1.00 115.29 ? 7 TYR A CD2 1 ATOM 52 C CE1 . TYR A 1 8 ? 9.767 -44.535 -11.219 1.00 115.16 ? 7 TYR A CE1 1 ATOM 53 C CE2 . TYR A 1 8 ? 9.838 -46.806 -10.452 1.00 113.15 ? 7 TYR A CE2 1 ATOM 54 C CZ . TYR A 1 8 ? 10.415 -45.754 -11.138 1.00 113.24 ? 7 TYR A CZ 1 ATOM 55 O OH . TYR A 1 8 ? 11.641 -45.915 -11.741 1.00 111.85 ? 7 TYR A OH 1 ATOM 56 N N . HIS A 1 9 ? 4.769 -43.081 -10.691 1.00 129.32 ? 8 HIS A N 1 ATOM 57 C CA . HIS A 1 9 ? 4.554 -41.902 -11.533 1.00 132.20 ? 8 HIS A CA 1 ATOM 58 C C . HIS A 1 9 ? 5.860 -41.309 -12.066 1.00 128.73 ? 8 HIS A C 1 ATOM 59 O O . HIS A 1 9 ? 6.872 -41.289 -11.367 1.00 123.81 ? 8 HIS A O 1 ATOM 60 C CB . HIS A 1 9 ? 3.770 -40.845 -10.744 1.00 134.39 ? 8 HIS A CB 1 ATOM 61 C CG . HIS A 1 9 ? 3.665 -39.516 -11.430 1.00 137.04 ? 8 HIS A CG 1 ATOM 62 N ND1 . HIS A 1 9 ? 3.981 -38.330 -10.803 1.00 134.94 ? 8 HIS A ND1 1 ATOM 63 C CD2 . HIS A 1 9 ? 3.281 -39.187 -12.687 1.00 141.85 ? 8 HIS A CD2 1 ATOM 64 C CE1 . HIS A 1 9 ? 3.793 -37.327 -11.643 1.00 138.23 ? 8 HIS A CE1 1 ATOM 65 N NE2 . HIS A 1 9 ? 3.373 -37.820 -12.794 1.00 142.75 ? 8 HIS A NE2 1 ATOM 66 N N . ALA A 1 10 ? 5.824 -40.847 -13.316 1.00 132.15 ? 9 ALA A N 1 ATOM 67 C CA . ALA A 1 10 ? 6.948 -40.143 -13.937 1.00 130.42 ? 9 ALA A CA 1 ATOM 68 C C . ALA A 1 10 ? 6.439 -39.011 -14.828 1.00 135.58 ? 9 ALA A C 1 ATOM 69 O O . ALA A 1 10 ? 5.271 -39.001 -15.221 1.00 141.10 ? 9 ALA A O 1 ATOM 70 C CB . ALA A 1 10 ? 7.796 -41.112 -14.747 1.00 129.54 ? 9 ALA A CB 1 ATOM 71 N N . ASN A 1 11 ? 7.321 -38.061 -15.137 1.00 134.22 ? 10 ASN A N 1 ATOM 72 C CA . ASN A 1 11 ? 6.980 -36.922 -15.995 1.00 139.23 ? 10 ASN A CA 1 ATOM 73 C C . ASN A 1 11 ? 8.237 -36.230 -16.547 1.00 137.92 ? 10 ASN A C 1 ATOM 74 O O . ASN A 1 11 ? 9.348 -36.732 -16.372 1.00 133.74 ? 10 ASN A O 1 ATOM 75 C CB . ASN A 1 11 ? 6.091 -35.929 -15.230 1.00 140.44 ? 10 ASN A CB 1 ATOM 76 C CG . ASN A 1 11 ? 6.798 -35.298 -14.042 1.00 134.58 ? 10 ASN A CG 1 ATOM 77 O OD1 . ASN A 1 11 ? 7.845 -35.771 -13.599 1.00 129.36 ? 10 ASN A OD1 1 ATOM 78 N ND2 . ASN A 1 11 ? 6.222 -34.223 -13.518 1.00 135.83 ? 10 ASN A ND2 1 ATOM 79 N N . ASN A 1 12 ? 8.053 -35.091 -17.219 1.00 142.24 ? 11 ASN A N 1 ATOM 80 C CA . ASN A 1 12 ? 9.161 -34.314 -17.789 1.00 142.03 ? 11 ASN A CA 1 ATOM 81 C C . ASN A 1 12 ? 9.515 -33.119 -16.900 1.00 138.38 ? 11 ASN A C 1 ATOM 82 O O . ASN A 1 12 ? 9.583 -31.984 -17.373 1.00 141.22 ? 11 ASN A O 1 ATOM 83 C CB . ASN A 1 12 ? 8.791 -33.823 -19.198 1.00 149.91 ? 11 ASN A CB 1 ATOM 84 C CG . ASN A 1 12 ? 8.370 -34.952 -20.124 1.00 154.44 ? 11 ASN A CG 1 ATOM 85 O OD1 . ASN A 1 12 ? 9.013 -36.000 -20.179 1.00 151.66 ? 11 ASN A OD1 1 ATOM 86 N ND2 . ASN A 1 12 ? 7.288 -34.738 -20.865 1.00 161.92 ? 11 ASN A ND2 1 ATOM 87 N N . SER A 1 13 ? 9.755 -33.387 -15.617 1.00 132.58 ? 12 SER A N 1 ATOM 88 C CA . SER A 1 13 ? 9.889 -32.329 -14.604 1.00 129.42 ? 12 SER A CA 1 ATOM 89 C C . SER A 1 13 ? 11.169 -31.495 -14.718 1.00 127.21 ? 12 SER A C 1 ATOM 90 O O . SER A 1 13 ? 11.134 -30.277 -14.522 1.00 127.57 ? 12 SER A O 1 ATOM 91 C CB . SER A 1 13 ? 9.798 -32.929 -13.193 1.00 124.60 ? 12 SER A CB 1 ATOM 92 O OG . SER A 1 13 ? 9.894 -31.925 -12.187 1.00 121.90 ? 12 SER A OG 1 ATOM 93 N N . THR A 1 14 ? 12.295 -32.155 -14.991 1.00 125.17 ? 13 THR A N 1 ATOM 94 C CA . THR A 1 14 ? 13.616 -31.501 -15.113 1.00 123.44 ? 13 THR A CA 1 ATOM 95 C C . THR A 1 14 ? 14.178 -30.885 -13.813 1.00 118.09 ? 13 THR A C 1 ATOM 96 O O . THR A 1 14 ? 15.399 -30.776 -13.671 1.00 115.97 ? 13 THR A O 1 ATOM 97 C CB . THR A 1 14 ? 13.657 -30.424 -16.235 1.00 128.49 ? 13 THR A CB 1 ATOM 98 O OG1 . THR A 1 14 ? 13.104 -29.187 -15.763 1.00 128.41 ? 13 THR A OG1 1 ATOM 99 C CG2 . THR A 1 14 ? 12.903 -30.890 -17.483 1.00 134.89 ? 13 THR A CG2 1 ATOM 100 N N . GLU A 1 15 ? 13.307 -30.480 -12.883 1.00 116.48 ? 14 GLU A N 1 ATOM 101 C CA . GLU A 1 15 ? 13.737 -29.844 -11.629 1.00 111.95 ? 14 GLU A CA 1 ATOM 102 C C . GLU A 1 15 ? 14.539 -30.793 -10.741 1.00 107.40 ? 14 GLU A C 1 ATOM 103 O O . GLU A 1 15 ? 14.224 -31.981 -10.648 1.00 107.05 ? 14 GLU A O 1 ATOM 104 C CB . GLU A 1 15 ? 12.539 -29.291 -10.842 1.00 112.46 ? 14 GLU A CB 1 ATOM 105 C CG . GLU A 1 15 ? 12.007 -27.965 -11.367 1.00 115.86 ? 14 GLU A CG 1 ATOM 106 C CD . GLU A 1 15 ? 11.310 -27.150 -10.294 1.00 115.09 ? 14 GLU A CD 1 ATOM 107 O OE1 . GLU A 1 15 ? 10.297 -27.636 -9.746 1.00 116.19 ? 14 GLU A OE1 1 ATOM 108 O OE2 . GLU A 1 15 ? 11.775 -26.025 -10.000 1.00 113.46 ? 14 GLU A OE2 1 ATOM 109 N N . GLN A 1 16 ? 15.556 -30.244 -10.076 1.00 104.00 ? 15 GLN A N 1 ATOM 110 C CA . GLN A 1 16 ? 16.541 -31.035 -9.343 1.00 100.55 ? 15 GLN A CA 1 ATOM 111 C C . GLN A 1 16 ? 16.541 -30.744 -7.850 1.00 97.38 ? 15 GLN A C 1 ATOM 112 O O . GLN A 1 16 ? 16.173 -29.649 -7.411 1.00 97.23 ? 15 GLN A O 1 ATOM 113 C CB . GLN A 1 16 ? 17.939 -30.749 -9.887 1.00 100.62 ? 15 GLN A CB 1 ATOM 114 C CG . GLN A 1 16 ? 18.193 -31.282 -11.286 1.00 103.84 ? 15 GLN A CG 1 ATOM 115 C CD . GLN A 1 16 ? 19.444 -30.697 -11.918 1.00 105.29 ? 15 GLN A CD 1 ATOM 116 O OE1 . GLN A 1 16 ? 19.864 -29.586 -11.588 1.00 104.18 ? 15 GLN A OE1 1 ATOM 117 N NE2 . GLN A 1 16 ? 20.040 -31.442 -12.845 1.00 108.12 ? 15 GLN A NE2 1 ATOM 118 N N . VAL A 1 17 ? 16.974 -31.738 -7.080 1.00 95.28 ? 16 VAL A N 1 ATOM 119 C CA . VAL A 1 17 ? 17.216 -31.577 -5.650 1.00 92.84 ? 16 VAL A CA 1 ATOM 120 C C . VAL A 1 17 ? 18.591 -32.134 -5.303 1.00 91.40 ? 16 VAL A C 1 ATOM 121 O O . VAL A 1 17 ? 19.239 -32.769 -6.132 1.00 92.20 ? 16 VAL A O 1 ATOM 122 C CB . VAL A 1 17 ? 16.143 -32.290 -4.799 1.00 93.13 ? 16 VAL A CB 1 ATOM 123 C CG1 . VAL A 1 17 ? 14.748 -31.884 -5.256 1.00 95.39 ? 16 VAL A CG1 1 ATOM 124 C CG2 . VAL A 1 17 ? 16.310 -33.806 -4.852 1.00 93.25 ? 16 VAL A CG2 1 ATOM 125 N N . ASP A 1 18 ? 19.029 -31.890 -4.074 1.00 89.87 ? 17 ASP A N 1 ATOM 126 C CA . ASP A 1 18 ? 20.301 -32.413 -3.600 1.00 89.49 ? 17 ASP A CA 1 ATOM 127 C C . ASP A 1 18 ? 20.087 -33.334 -2.412 1.00 89.42 ? 17 ASP A C 1 ATOM 128 O O . ASP A 1 18 ? 19.071 -33.256 -1.718 1.00 89.06 ? 17 ASP A O 1 ATOM 129 C CB . ASP A 1 18 ? 21.247 -31.275 -3.220 1.00 88.93 ? 17 ASP A CB 1 ATOM 130 C CG . ASP A 1 18 ? 21.812 -30.550 -4.427 1.00 89.74 ? 17 ASP A CG 1 ATOM 131 O OD1 . ASP A 1 18 ? 21.668 -31.042 -5.569 1.00 91.07 ? 17 ASP A OD1 1 ATOM 132 O OD2 . ASP A 1 18 ? 22.411 -29.474 -4.228 1.00 89.54 ? 17 ASP A OD2 1 ATOM 133 N N . THR A 1 19 ? 21.056 -34.217 -2.200 1.00 90.29 ? 18 THR A N 1 ATOM 134 C CA . THR A 1 19 ? 21.007 -35.187 -1.115 1.00 91.11 ? 18 THR A CA 1 ATOM 135 C C . THR A 1 19 ? 22.430 -35.295 -0.540 1.00 92.31 ? 18 THR A C 1 ATOM 136 O O . THR A 1 19 ? 23.333 -34.591 -0.996 1.00 92.51 ? 18 THR A O 1 ATOM 137 C CB . THR A 1 19 ? 20.404 -36.536 -1.616 1.00 91.55 ? 18 THR A CB 1 ATOM 138 O OG1 . THR A 1 19 ? 19.630 -37.148 -0.579 1.00 92.42 ? 18 THR A OG1 1 ATOM 139 C CG2 . THR A 1 19 ? 21.456 -37.504 -2.084 1.00 92.43 ? 18 THR A CG2 1 ATOM 140 N N . ILE A 1 20 ? 22.629 -36.159 0.452 1.00 93.84 ? 19 ILE A N 1 ATOM 141 C CA . ILE A 1 20 ? 23.923 -36.250 1.142 1.00 96.00 ? 19 ILE A CA 1 ATOM 142 C C . ILE A 1 20 ? 25.052 -36.745 0.219 1.00 97.34 ? 19 ILE A C 1 ATOM 143 O O . ILE A 1 20 ? 26.207 -36.339 0.375 1.00 99.11 ? 19 ILE A O 1 ATOM 144 C CB . ILE A 1 20 ? 23.861 -37.164 2.393 1.00 98.36 ? 19 ILE A CB 1 ATOM 145 C CG1 . ILE A 1 20 ? 22.681 -36.790 3.305 1.00 98.17 ? 19 ILE A CG1 1 ATOM 146 C CG2 . ILE A 1 20 ? 25.167 -37.069 3.178 1.00 101.20 ? 19 ILE A CG2 1 ATOM 147 C CD1 . ILE A 1 20 ? 22.490 -37.722 4.486 1.00 101.06 ? 19 ILE A CD1 1 ATOM 148 N N . MET A 1 21 ? 24.713 -37.612 -0.734 1.00 97.01 ? 20 MET A N 1 ATOM 149 C CA . MET A 1 21 ? 25.703 -38.219 -1.632 1.00 98.89 ? 20 MET A CA 1 ATOM 150 C C . MET A 1 21 ? 25.370 -38.073 -3.124 1.00 98.03 ? 20 MET A C 1 ATOM 151 O O . MET A 1 21 ? 25.976 -38.745 -3.957 1.00 99.80 ? 20 MET A O 1 ATOM 152 C CB . MET A 1 21 ? 25.891 -39.701 -1.276 1.00 100.64 ? 20 MET A CB 1 ATOM 153 C CG . MET A 1 21 ? 24.630 -40.548 -1.342 1.00 99.11 ? 20 MET A CG 1 ATOM 154 S SD . MET A 1 21 ? 24.867 -42.175 -0.599 1.00 101.45 ? 20 MET A SD 1 ATOM 155 C CE . MET A 1 21 ? 25.769 -43.009 -1.896 1.00 103.27 ? 20 MET A CE 1 ATOM 156 N N . GLU A 1 22 ? 24.444 -37.173 -3.457 1.00 96.03 ? 21 GLU A N 1 ATOM 157 C CA . GLU A 1 22 ? 24.014 -36.950 -4.846 1.00 95.89 ? 21 GLU A CA 1 ATOM 158 C C . GLU A 1 22 ? 23.583 -35.497 -5.080 1.00 94.62 ? 21 GLU A C 1 ATOM 159 O O . GLU A 1 22 ? 22.615 -35.026 -4.479 1.00 93.13 ? 21 GLU A O 1 ATOM 160 C CB . GLU A 1 22 ? 22.850 -37.875 -5.228 1.00 95.33 ? 21 GLU A CB 1 ATOM 161 C CG . GLU A 1 22 ? 23.073 -39.354 -4.943 1.00 96.30 ? 21 GLU A CG 1 ATOM 162 C CD . GLU A 1 22 ? 22.074 -40.251 -5.652 1.00 96.23 ? 21 GLU A CD 1 ATOM 163 O OE1 . GLU A 1 22 ? 21.861 -40.067 -6.872 1.00 96.88 ? 21 GLU A OE1 1 ATOM 164 O OE2 . GLU A 1 22 ? 21.508 -41.150 -4.992 1.00 95.84 ? 21 GLU A OE2 1 ATOM 165 N N . LYS A 1 23 ? 24.308 -34.798 -5.950 1.00 95.86 ? 22 LYS A N 1 ATOM 166 C CA . LYS A 1 23 ? 23.927 -33.457 -6.391 1.00 95.14 ? 22 LYS A CA 1 ATOM 167 C C . LYS A 1 23 ? 23.101 -33.556 -7.672 1.00 96.13 ? 22 LYS A C 1 ATOM 168 O O . LYS A 1 23 ? 23.253 -34.510 -8.440 1.00 97.93 ? 22 LYS A O 1 ATOM 169 C CB . LYS A 1 23 ? 25.173 -32.605 -6.641 1.00 96.77 ? 22 LYS A CB 1 ATOM 170 N N . ASN A 1 24 ? 22.227 -32.573 -7.893 1.00 95.36 ? 23 ASN A N 1 ATOM 171 C CA . ASN A 1 24 ? 21.413 -32.497 -9.114 1.00 97.18 ? 23 ASN A CA 1 ATOM 172 C C . ASN A 1 24 ? 20.671 -33.804 -9.426 1.00 97.40 ? 23 ASN A C 1 ATOM 173 O O . ASN A 1 24 ? 21.004 -34.511 -10.379 1.00 99.37 ? 23 ASN A O 1 ATOM 174 C CB . ASN A 1 24 ? 22.276 -32.075 -10.318 1.00 100.50 ? 23 ASN A CB 1 ATOM 175 C CG . ASN A 1 24 ? 22.628 -30.596 -10.306 1.00 100.74 ? 23 ASN A CG 1 ATOM 176 O OD1 . ASN A 1 24 ? 22.791 -29.979 -11.360 1.00 103.77 ? 23 ASN A OD1 1 ATOM 177 N ND2 . ASN A 1 24 ? 22.749 -30.021 -9.115 1.00 97.87 ? 23 ASN A ND2 1 ATOM 178 N N . VAL A 1 25 ? 19.669 -34.115 -8.609 1.00 95.38 ? 24 VAL A N 1 ATOM 179 C CA . VAL A 1 25 ? 18.872 -35.325 -8.780 1.00 95.71 ? 24 VAL A CA 1 ATOM 180 C C . VAL A 1 25 ? 17.447 -34.943 -9.171 1.00 96.85 ? 24 VAL A C 1 ATOM 181 O O . VAL A 1 25 ? 16.717 -34.343 -8.385 1.00 95.84 ? 24 VAL A O 1 ATOM 182 C CB . VAL A 1 25 ? 18.864 -36.179 -7.499 1.00 93.69 ? 24 VAL A CB 1 ATOM 183 C CG1 . VAL A 1 25 ? 18.089 -37.472 -7.720 1.00 94.36 ? 24 VAL A CG1 1 ATOM 184 C CG2 . VAL A 1 25 ? 20.293 -36.475 -7.062 1.00 93.30 ? 24 VAL A CG2 1 ATOM 185 N N . THR A 1 26 ? 17.066 -35.310 -10.392 1.00 99.59 ? 25 THR A N 1 ATOM 186 C CA . THR A 1 26 ? 15.794 -34.901 -10.983 1.00 101.92 ? 25 THR A CA 1 ATOM 187 C C . THR A 1 26 ? 14.603 -35.631 -10.365 1.00 101.68 ? 25 THR A C 1 ATOM 188 O O . THR A 1 26 ? 14.572 -36.863 -10.329 1.00 101.43 ? 25 THR A O 1 ATOM 189 C CB . THR A 1 26 ? 15.795 -35.149 -12.504 1.00 105.76 ? 25 THR A CB 1 ATOM 190 O OG1 . THR A 1 26 ? 16.331 -36.450 -12.773 1.00 105.71 ? 25 THR A OG1 1 ATOM 191 C CG2 . THR A 1 26 ? 16.641 -34.101 -13.219 1.00 107.36 ? 25 THR A CG2 1 ATOM 192 N N . VAL A 1 27 ? 13.625 -34.858 -9.894 1.00 102.18 ? 26 VAL A N 1 ATOM 193 C CA . VAL A 1 27 ? 12.427 -35.407 -9.257 1.00 102.92 ? 26 VAL A CA 1 ATOM 194 C C . VAL A 1 27 ? 11.158 -34.874 -9.915 1.00 107.08 ? 26 VAL A C 1 ATOM 195 O O . VAL A 1 27 ? 11.164 -33.801 -10.521 1.00 108.72 ? 26 VAL A O 1 ATOM 196 C CB . VAL A 1 27 ? 12.386 -35.100 -7.737 1.00 100.58 ? 26 VAL A CB 1 ATOM 197 C CG1 . VAL A 1 27 ? 13.646 -35.611 -7.052 1.00 97.27 ? 26 VAL A CG1 1 ATOM 198 C CG2 . VAL A 1 27 ? 12.194 -33.609 -7.469 1.00 100.75 ? 26 VAL A CG2 1 ATOM 199 N N . THR A 1 28 ? 10.072 -35.632 -9.780 1.00 109.31 ? 27 THR A N 1 ATOM 200 C CA . THR A 1 28 ? 8.785 -35.272 -10.387 1.00 114.40 ? 27 THR A CA 1 ATOM 201 C C . THR A 1 28 ? 8.059 -34.151 -9.643 1.00 115.50 ? 27 THR A C 1 ATOM 202 O O . THR A 1 28 ? 7.301 -33.395 -10.253 1.00 119.80 ? 27 THR A O 1 ATOM 203 C CB . THR A 1 28 ? 7.837 -36.489 -10.508 1.00 117.24 ? 27 THR A CB 1 ATOM 204 O OG1 . THR A 1 28 ? 6.538 -36.046 -10.918 1.00 123.01 ? 27 THR A OG1 1 ATOM 205 C CG2 . THR A 1 28 ? 7.708 -37.246 -9.192 1.00 114.79 ? 27 THR A CG2 1 ATOM 206 N N . HIS A 1 29 ? 8.279 -34.061 -8.333 1.00 112.20 ? 28 HIS A N 1 ATOM 207 C CA . HIS A 1 29 ? 7.686 -33.007 -7.513 1.00 113.10 ? 28 HIS A CA 1 ATOM 208 C C . HIS A 1 29 ? 8.723 -32.441 -6.547 1.00 108.20 ? 28 HIS A C 1 ATOM 209 O O . HIS A 1 29 ? 9.153 -33.123 -5.617 1.00 105.47 ? 28 HIS A O 1 ATOM 210 C CB . HIS A 1 29 ? 6.481 -33.539 -6.736 1.00 116.31 ? 28 HIS A CB 1 ATOM 211 C CG . HIS A 1 29 ? 5.269 -33.775 -7.581 1.00 122.20 ? 28 HIS A CG 1 ATOM 212 N ND1 . HIS A 1 29 ? 5.023 -34.975 -8.213 1.00 123.69 ? 28 HIS A ND1 1 ATOM 213 C CD2 . HIS A 1 29 ? 4.229 -32.966 -7.892 1.00 127.55 ? 28 HIS A CD2 1 ATOM 214 C CE1 . HIS A 1 29 ? 3.884 -34.895 -8.878 1.00 129.71 ? 28 HIS A CE1 1 ATOM 215 N NE2 . HIS A 1 29 ? 3.384 -33.685 -8.701 1.00 132.42 ? 28 HIS A NE2 1 ATOM 216 N N . ALA A 1 30 ? 9.121 -31.195 -6.787 1.00 107.34 ? 29 ALA A N 1 ATOM 217 C CA . ALA A 1 30 ? 10.080 -30.502 -5.936 1.00 103.41 ? 29 ALA A CA 1 ATOM 218 C C . ALA A 1 30 ? 9.357 -29.482 -5.073 1.00 104.54 ? 29 ALA A C 1 ATOM 219 O O . ALA A 1 30 ? 8.265 -29.025 -5.415 1.00 109.03 ? 29 ALA A O 1 ATOM 220 C CB . ALA A 1 30 ? 11.139 -29.813 -6.784 1.00 101.89 ? 29 ALA A CB 1 ATOM 221 N N . GLN A 1 31 ? 9.977 -29.132 -3.951 1.00 101.21 ? 30 GLN A N 1 ATOM 222 C CA . GLN A 1 31 ? 9.427 -28.132 -3.046 1.00 102.07 ? 30 GLN A CA 1 ATOM 223 C C . GLN A 1 31 ? 10.526 -27.182 -2.568 1.00 98.10 ? 30 GLN A C 1 ATOM 224 O O . GLN A 1 31 ? 11.223 -27.453 -1.587 1.00 95.68 ? 30 GLN A O 1 ATOM 225 C CB . GLN A 1 31 ? 8.727 -28.809 -1.860 1.00 103.86 ? 30 GLN A CB 1 ATOM 226 C CG . GLN A 1 31 ? 7.927 -27.865 -0.964 1.00 106.70 ? 30 GLN A CG 1 ATOM 227 C CD . GLN A 1 31 ? 6.828 -27.121 -1.706 1.00 111.20 ? 30 GLN A CD 1 ATOM 228 O OE1 . GLN A 1 31 ? 6.659 -25.914 -1.532 1.00 112.04 ? 30 GLN A OE1 1 ATOM 229 N NE2 . GLN A 1 31 ? 6.081 -27.836 -2.544 1.00 114.47 ? 30 GLN A NE2 1 ATOM 230 N N . ASP A 1 32 ? 10.681 -26.080 -3.297 1.00 97.74 ? 31 ASP A N 1 ATOM 231 C CA . ASP A 1 32 ? 11.539 -24.975 -2.887 1.00 94.75 ? 31 ASP A CA 1 ATOM 232 C C . ASP A 1 32 ? 10.945 -24.319 -1.639 1.00 95.34 ? 31 ASP A C 1 ATOM 233 O O . ASP A 1 32 ? 9.749 -24.030 -1.592 1.00 98.99 ? 31 ASP A O 1 ATOM 234 C CB . ASP A 1 32 ? 11.669 -23.966 -4.037 1.00 95.69 ? 31 ASP A CB 1 ATOM 235 C CG . ASP A 1 32 ? 12.275 -22.636 -3.607 1.00 94.01 ? 31 ASP A CG 1 ATOM 236 O OD1 . ASP A 1 32 ? 12.972 -22.565 -2.565 1.00 91.37 ? 31 ASP A OD1 1 ATOM 237 O OD2 . ASP A 1 32 ? 12.050 -21.649 -4.337 1.00 95.81 ? 31 ASP A OD2 1 ATOM 238 N N . ILE A 1 33 ? 11.793 -24.087 -0.637 1.00 92.16 ? 32 ILE A N 1 ATOM 239 C CA . ILE A 1 33 ? 11.367 -23.520 0.642 1.00 92.84 ? 32 ILE A CA 1 ATOM 240 C C . ILE A 1 33 ? 12.221 -22.313 1.028 1.00 90.03 ? 32 ILE A C 1 ATOM 241 O O . ILE A 1 33 ? 12.467 -22.073 2.210 1.00 89.66 ? 32 ILE A O 1 ATOM 242 C CB . ILE A 1 33 ? 11.415 -24.580 1.769 1.00 93.16 ? 32 ILE A CB 1 ATOM 243 C CG1 . ILE A 1 33 ? 12.812 -25.206 1.884 1.00 89.68 ? 32 ILE A CG1 1 ATOM 244 C CG2 . ILE A 1 33 ? 10.377 -25.664 1.518 1.00 96.23 ? 32 ILE A CG2 1 ATOM 245 C CD1 . ILE A 1 33 ? 13.001 -26.064 3.115 1.00 90.36 ? 32 ILE A CD1 1 ATOM 246 N N . LEU A 1 34 ? 12.649 -21.542 0.030 1.00 88.44 ? 33 LEU A N 1 ATOM 247 C CA . LEU A 1 34 ? 13.553 -20.409 0.255 1.00 85.78 ? 33 LEU A CA 1 ATOM 248 C C . LEU A 1 34 ? 13.201 -19.221 -0.631 1.00 86.56 ? 33 LEU A C 1 ATOM 249 O O . LEU A 1 34 ? 13.232 -19.328 -1.853 1.00 87.30 ? 33 LEU A O 1 ATOM 250 C CB . LEU A 1 34 ? 14.999 -20.836 -0.019 1.00 82.79 ? 33 LEU A CB 1 ATOM 251 C CG . LEU A 1 34 ? 16.103 -19.786 0.121 1.00 80.72 ? 33 LEU A CG 1 ATOM 252 C CD1 . LEU A 1 34 ? 16.227 -19.329 1.569 1.00 80.27 ? 33 LEU A CD1 1 ATOM 253 C CD2 . LEU A 1 34 ? 17.432 -20.331 -0.385 1.00 79.00 ? 33 LEU A CD2 1 ATOM 254 N N . GLU A 1 35 ? 12.882 -18.089 -0.009 1.00 86.76 ? 34 GLU A N 1 ATOM 255 C CA . GLU A 1 35 ? 12.592 -16.859 -0.738 1.00 87.76 ? 34 GLU A CA 1 ATOM 256 C C . GLU A 1 35 ? 13.886 -16.125 -1.079 1.00 84.52 ? 34 GLU A C 1 ATOM 257 O O . GLU A 1 35 ? 14.694 -15.842 -0.192 1.00 81.94 ? 34 GLU A O 1 ATOM 258 C CB . GLU A 1 35 ? 11.688 -15.947 0.097 1.00 90.02 ? 34 GLU A CB 1 ATOM 259 C CG . GLU A 1 35 ? 11.126 -14.755 -0.662 1.00 92.53 ? 34 GLU A CG 1 ATOM 260 C CD . GLU A 1 35 ? 10.280 -15.157 -1.859 1.00 96.35 ? 34 GLU A CD 1 ATOM 261 O OE1 . GLU A 1 35 ? 9.566 -16.180 -1.783 1.00 98.41 ? 34 GLU A OE1 1 ATOM 262 O OE2 . GLU A 1 35 ? 10.337 -14.451 -2.883 1.00 97.65 ? 34 GLU A OE2 1 ATOM 263 N N . LYS A 1 36 ? 14.068 -15.816 -2.361 1.00 85.20 ? 35 LYS A N 1 ATOM 264 C CA . LYS A 1 36 ? 15.249 -15.096 -2.844 1.00 83.17 ? 35 LYS A CA 1 ATOM 265 C C . LYS A 1 36 ? 14.921 -13.693 -3.368 1.00 84.86 ? 35 LYS A C 1 ATOM 266 O O . LYS A 1 36 ? 15.821 -12.969 -3.793 1.00 83.81 ? 35 LYS A O 1 ATOM 267 C CB . LYS A 1 36 ? 15.942 -15.893 -3.957 1.00 83.36 ? 35 LYS A CB 1 ATOM 268 C CG . LYS A 1 36 ? 16.858 -17.008 -3.478 1.00 80.83 ? 35 LYS A CG 1 ATOM 269 C CD . LYS A 1 36 ? 16.124 -18.317 -3.263 1.00 81.52 ? 35 LYS A CD 1 ATOM 270 C CE . LYS A 1 36 ? 15.914 -19.072 -4.564 1.00 83.64 ? 35 LYS A CE 1 ATOM 271 N NZ . LYS A 1 36 ? 15.078 -20.286 -4.355 1.00 84.55 ? 35 LYS A NZ 1 ATOM 272 N N . THR A 1 37 ? 13.650 -13.301 -3.337 1.00 87.92 ? 36 THR A N 1 ATOM 273 C CA . THR A 1 37 ? 13.234 -12.057 -3.981 1.00 90.61 ? 36 THR A CA 1 ATOM 274 C C . THR A 1 37 ? 12.683 -11.053 -2.981 1.00 90.90 ? 36 THR A C 1 ATOM 275 O O . THR A 1 37 ? 12.061 -11.422 -1.991 1.00 91.08 ? 36 THR A O 1 ATOM 276 C CB . THR A 1 37 ? 12.185 -12.316 -5.085 1.00 95.71 ? 36 THR A CB 1 ATOM 277 O OG1 . THR A 1 37 ? 10.983 -12.838 -4.507 1.00 98.11 ? 36 THR A OG1 1 ATOM 278 C CG2 . THR A 1 37 ? 12.720 -13.303 -6.115 1.00 95.84 ? 36 THR A CG2 1 ATOM 279 N N . HIS A 1 38 ? 12.928 -9.779 -3.256 1.00 91.32 ? 37 HIS A N 1 ATOM 280 C CA . HIS A 1 38 ? 12.394 -8.699 -2.447 1.00 92.33 ? 37 HIS A CA 1 ATOM 281 C C . HIS A 1 38 ? 12.048 -7.525 -3.349 1.00 96.01 ? 37 HIS A C 1 ATOM 282 O O . HIS A 1 38 ? 12.570 -7.421 -4.459 1.00 96.71 ? 37 HIS A O 1 ATOM 283 C CB . HIS A 1 38 ? 13.394 -8.290 -1.350 1.00 87.73 ? 37 HIS A CB 1 ATOM 284 C CG . HIS A 1 38 ? 14.724 -7.834 -1.864 1.00 84.84 ? 37 HIS A CG 1 ATOM 285 N ND1 . HIS A 1 38 ? 14.982 -6.522 -2.188 1.00 85.17 ? 37 HIS A ND1 1 ATOM 286 C CD2 . HIS A 1 38 ? 15.876 -8.507 -2.084 1.00 82.18 ? 37 HIS A CD2 1 ATOM 287 C CE1 . HIS A 1 38 ? 16.232 -6.404 -2.596 1.00 82.94 ? 37 HIS A CE1 1 ATOM 288 N NE2 . HIS A 1 38 ? 16.797 -7.595 -2.543 1.00 81.27 ? 37 HIS A NE2 1 ATOM 289 N N . ASN A 1 39 ? 11.163 -6.653 -2.872 1.00 99.15 ? 38 ASN A N 1 ATOM 290 C CA . ASN A 1 39 ? 10.680 -5.525 -3.672 1.00 103.71 ? 38 ASN A CA 1 ATOM 291 C C . ASN A 1 39 ? 11.685 -4.377 -3.810 1.00 101.59 ? 38 ASN A C 1 ATOM 292 O O . ASN A 1 39 ? 11.554 -3.537 -4.697 1.00 104.86 ? 38 ASN A O 1 ATOM 293 C CB . ASN A 1 39 ? 9.333 -5.013 -3.141 1.00 108.39 ? 38 ASN A CB 1 ATOM 294 C CG . ASN A 1 39 ? 9.430 -4.366 -1.766 1.00 105.94 ? 38 ASN A CG 1 ATOM 295 O OD1 . ASN A 1 39 ? 10.509 -4.251 -1.173 1.00 100.65 ? 38 ASN A OD1 1 ATOM 296 N ND2 . ASN A 1 39 ? 8.284 -3.937 -1.252 1.00 110.47 ? 38 ASN A ND2 1 ATOM 297 N N . GLY A 1 40 ? 12.668 -4.332 -2.919 1.00 97.03 ? 39 GLY A N 1 ATOM 298 C CA . GLY A 1 40 ? 13.773 -3.386 -3.033 1.00 94.90 ? 39 GLY A CA 1 ATOM 299 C C . GLY A 1 40 ? 13.428 -1.998 -2.541 1.00 96.47 ? 39 GLY A C 1 ATOM 300 O O . GLY A 1 40 ? 14.019 -1.017 -2.990 1.00 96.02 ? 39 GLY A O 1 ATOM 301 N N . LYS A 1 41 ? 12.468 -1.913 -1.621 1.00 45.49 ? 40 LYS A N 1 ATOM 302 C CA . LYS A 1 41 ? 12.051 -0.626 -1.041 1.00 45.19 ? 40 LYS A CA 1 ATOM 303 C C . LYS A 1 41 ? 11.676 -0.718 0.437 1.00 43.02 ? 40 LYS A C 1 ATOM 304 O O . LYS A 1 41 ? 11.460 -1.810 0.969 1.00 42.51 ? 40 LYS A O 1 ATOM 305 C CB . LYS A 1 41 ? 10.909 0.023 -1.853 1.00 47.03 ? 40 LYS A CB 1 ATOM 306 C CG . LYS A 1 41 ? 10.287 -0.813 -2.953 1.00 49.64 ? 40 LYS A CG 1 ATOM 307 C CD . LYS A 1 41 ? 9.247 -0.004 -3.724 1.00 51.52 ? 40 LYS A CD 1 ATOM 308 C CE . LYS A 1 41 ? 8.350 -0.878 -4.590 1.00 53.81 ? 40 LYS A CE 1 ATOM 309 N NZ . LYS A 1 41 ? 8.802 -0.995 -6.019 1.00 56.69 ? 40 LYS A NZ 1 ATOM 310 N N . LEU A 1 42 ? 11.614 0.445 1.083 1.00 42.26 ? 41 LEU A N 1 ATOM 311 C CA . LEU A 1 42 ? 11.232 0.559 2.488 1.00 40.55 ? 41 LEU A CA 1 ATOM 312 C C . LEU A 1 42 ? 9.741 0.894 2.621 1.00 41.55 ? 41 LEU A C 1 ATOM 313 O O . LEU A 1 42 ? 9.287 1.948 2.168 1.00 42.02 ? 41 LEU A O 1 ATOM 314 C CB . LEU A 1 42 ? 12.066 1.640 3.162 1.00 39.34 ? 41 LEU A CB 1 ATOM 315 C CG . LEU A 1 42 ? 13.584 1.395 3.264 1.00 39.17 ? 41 LEU A CG 1 ATOM 316 C CD1 . LEU A 1 42 ? 14.281 2.621 3.835 1.00 37.88 ? 41 LEU A CD1 1 ATOM 317 C CD2 . LEU A 1 42 ? 13.930 0.159 4.091 1.00 38.15 ? 41 LEU A CD2 1 ATOM 318 N N . CYS A 1 43 ? 9.004 0.009 3.286 1.00 41.72 ? 42 CYS A N 1 ATOM 319 C CA . CYS A 1 43 ? 7.546 0.028 3.304 1.00 43.39 ? 42 CYS A CA 1 ATOM 320 C C . CYS A 1 43 ? 6.992 0.183 4.723 1.00 41.85 ? 42 CYS A C 1 ATOM 321 O O . CYS A 1 43 ? 7.710 0.006 5.710 1.00 40.36 ? 42 CYS A O 1 ATOM 322 C CB . CYS A 1 43 ? 7.007 -1.278 2.719 1.00 45.21 ? 42 CYS A CB 1 ATOM 323 S SG . CYS A 1 43 ? 7.500 -1.678 1.027 1.00 48.11 ? 42 CYS A SG 1 ATOM 324 N N . ASP A 1 44 ? 5.705 0.505 4.817 1.00 42.84 ? 43 ASP A N 1 ATOM 325 C CA . ASP A 1 44 ? 5.008 0.539 6.110 1.00 42.14 ? 43 ASP A CA 1 ATOM 326 C C . ASP A 1 44 ? 5.046 -0.855 6.734 1.00 41.20 ? 43 ASP A C 1 ATOM 327 O O . ASP A 1 44 ? 5.032 -1.871 6.031 1.00 42.14 ? 43 ASP A O 1 ATOM 328 C CB . ASP A 1 44 ? 3.537 0.962 5.950 1.00 44.01 ? 43 ASP A CB 1 ATOM 329 C CG . ASP A 1 44 ? 3.381 2.365 5.417 1.00 45.33 ? 43 ASP A CG 1 ATOM 330 O OD1 . ASP A 1 44 ? 4.396 2.944 4.979 1.00 45.74 ? 43 ASP A OD1 1 ATOM 331 O OD2 . ASP A 1 44 ? 2.245 2.886 5.431 1.00 46.81 ? 43 ASP A OD2 1 ATOM 332 N N . LEU A 1 45 ? 5.099 -0.906 8.051 1.00 39.68 ? 44 LEU A N 1 ATOM 333 C CA . LEU A 1 45 ? 5.100 -2.180 8.730 1.00 39.70 ? 44 LEU A CA 1 ATOM 334 C C . LEU A 1 45 ? 3.708 -2.351 9.313 1.00 40.55 ? 44 LEU A C 1 ATOM 335 O O . LEU A 1 45 ? 3.290 -1.588 10.169 1.00 39.86 ? 44 LEU A O 1 ATOM 336 C CB . LEU A 1 45 ? 6.197 -2.238 9.799 1.00 37.56 ? 44 LEU A CB 1 ATOM 337 C CG . LEU A 1 45 ? 6.401 -3.631 10.413 1.00 37.64 ? 44 LEU A CG 1 ATOM 338 C CD1 . LEU A 1 45 ? 6.911 -4.650 9.408 1.00 38.44 ? 44 LEU A CD1 1 ATOM 339 C CD2 . LEU A 1 45 ? 7.345 -3.551 11.596 1.00 36.49 ? 44 LEU A CD2 1 ATOM 340 N N . ASP A 1 46 ? 2.988 -3.338 8.799 1.00 42.86 ? 45 ASP A N 1 ATOM 341 C CA . ASP A 1 46 ? 1.567 -3.547 9.113 1.00 44.72 ? 45 ASP A CA 1 ATOM 342 C C . ASP A 1 46 ? 0.748 -2.248 9.236 1.00 44.34 ? 45 ASP A C 1 ATOM 343 O O . ASP A 1 46 ? -0.039 -2.084 10.171 1.00 43.88 ? 45 ASP A O 1 ATOM 344 C CB . ASP A 1 46 ? 1.418 -4.403 10.372 1.00 45.31 ? 45 ASP A CB 1 ATOM 345 C CG . ASP A 1 46 ? 0.269 -5.360 10.268 1.00 48.64 ? 45 ASP A CG 1 ATOM 346 O OD1 . ASP A 1 46 ? 0.351 -6.229 9.385 1.00 51.15 ? 45 ASP A OD1 1 ATOM 347 O OD2 . ASP A 1 46 ? -0.727 -5.244 11.023 1.00 50.35 ? 45 ASP A OD2 1 ATOM 348 N N . GLY A 1 47 ? 0.938 -1.336 8.281 1.00 44.10 ? 46 GLY A N 1 ATOM 349 C CA . GLY A 1 47 ? 0.167 -0.101 8.214 1.00 44.48 ? 46 GLY A CA 1 ATOM 350 C C . GLY A 1 47 ? 0.713 1.074 9.000 1.00 43.11 ? 46 GLY A C 1 ATOM 351 O O . GLY A 1 47 ? 0.099 2.139 9.003 1.00 44.86 ? 46 GLY A O 1 ATOM 352 N N . VAL A 1 48 ? 1.851 0.897 9.669 1.00 40.80 ? 47 VAL A N 1 ATOM 353 C CA . VAL A 1 48 ? 2.548 1.997 10.337 1.00 38.96 ? 47 VAL A CA 1 ATOM 354 C C . VAL A 1 48 ? 3.824 2.346 9.555 1.00 38.05 ? 47 VAL A C 1 ATOM 355 O O . VAL A 1 48 ? 4.660 1.488 9.272 1.00 36.54 ? 47 VAL A O 1 ATOM 356 C CB . VAL A 1 48 ? 2.903 1.641 11.804 1.00 37.68 ? 47 VAL A CB 1 ATOM 357 C CG1 . VAL A 1 48 ? 3.723 2.750 12.464 1.00 36.04 ? 47 VAL A CG1 1 ATOM 358 C CG2 . VAL A 1 48 ? 1.636 1.368 12.603 1.00 38.51 ? 47 VAL A CG2 1 ATOM 359 N N . LYS A 1 49 ? 3.955 3.617 9.206 1.00 38.27 ? 48 LYS A N 1 ATOM 360 C CA . LYS A 1 49 ? 5.054 4.083 8.382 1.00 38.30 ? 48 LYS A CA 1 ATOM 361 C C . LYS A 1 49 ? 6.326 4.200 9.236 1.00 36.20 ? 48 LYS A C 1 ATOM 362 O O . LYS A 1 49 ? 6.254 4.539 10.426 1.00 34.10 ? 48 LYS A O 1 ATOM 363 C CB . LYS A 1 49 ? 4.683 5.445 7.784 1.00 40.29 ? 48 LYS A CB 1 ATOM 364 C CG . LYS A 1 49 ? 5.691 6.025 6.805 1.00 41.61 ? 48 LYS A CG 1 ATOM 365 C CD . LYS A 1 49 ? 5.203 7.335 6.192 1.00 44.00 ? 48 LYS A CD 1 ATOM 366 C CE . LYS A 1 49 ? 6.255 7.974 5.287 1.00 45.24 ? 48 LYS A CE 1 ATOM 367 N NZ . LYS A 1 49 ? 5.642 8.925 4.303 1.00 48.35 ? 48 LYS A NZ 1 ATOM 368 N N . PRO A 1 50 ? 7.495 3.914 8.639 1.00 35.39 ? 49 PRO A N 1 ATOM 369 C CA . PRO A 1 50 ? 8.719 4.120 9.413 1.00 33.87 ? 49 PRO A CA 1 ATOM 370 C C . PRO A 1 50 ? 9.084 5.593 9.480 1.00 33.72 ? 49 PRO A C 1 ATOM 371 O O . PRO A 1 50 ? 8.594 6.396 8.688 1.00 35.67 ? 49 PRO A O 1 ATOM 372 C CB . PRO A 1 50 ? 9.773 3.359 8.612 1.00 33.99 ? 49 PRO A CB 1 ATOM 373 C CG . PRO A 1 50 ? 9.276 3.426 7.200 1.00 35.86 ? 49 PRO A CG 1 ATOM 374 C CD . PRO A 1 50 ? 7.771 3.382 7.293 1.00 36.50 ? 49 PRO A CD 1 ATOM 375 N N . LEU A 1 51 ? 9.921 5.943 10.438 1.00 32.14 ? 50 LEU A N 1 ATOM 376 C CA . LEU A 1 51 ? 10.540 7.260 10.456 1.00 32.08 ? 50 LEU A CA 1 ATOM 377 C C . LEU A 1 51 ? 11.781 7.169 9.564 1.00 32.27 ? 50 LEU A C 1 ATOM 378 O O . LEU A 1 51 ? 12.757 6.554 9.953 1.00 30.76 ? 50 LEU A O 1 ATOM 379 C CB . LEU A 1 51 ? 10.924 7.650 11.887 1.00 30.35 ? 50 LEU A CB 1 ATOM 380 C CG . LEU A 1 51 ? 11.703 8.945 12.065 1.00 30.25 ? 50 LEU A CG 1 ATOM 381 C CD1 . LEU A 1 51 ? 10.942 10.144 11.501 1.00 31.90 ? 50 LEU A CD1 1 ATOM 382 C CD2 . LEU A 1 51 ? 11.998 9.137 13.536 1.00 28.87 ? 50 LEU A CD2 1 ATOM 383 N N . ILE A 1 52 ? 11.695 7.736 8.358 1.00 34.16 ? 51 ILE A N 1 ATOM 384 C CA . ILE A 1 52 ? 12.812 7.823 7.408 1.00 34.86 ? 51 ILE A CA 1 ATOM 385 C C . ILE A 1 52 ? 13.557 9.144 7.602 1.00 35.65 ? 51 ILE A C 1 ATOM 386 O O . ILE A 1 52 ? 13.086 10.193 7.166 1.00 36.73 ? 51 ILE A O 1 ATOM 387 C CB . ILE A 1 52 ? 12.317 7.787 5.945 1.00 36.50 ? 51 ILE A CB 1 ATOM 388 C CG1 . ILE A 1 52 ? 11.428 6.570 5.689 1.00 36.76 ? 51 ILE A CG1 1 ATOM 389 C CG2 . ILE A 1 52 ? 13.489 7.805 4.968 1.00 37.33 ? 51 ILE A CG2 1 ATOM 390 C CD1 . ILE A 1 52 ? 12.050 5.251 6.071 1.00 35.76 ? 51 ILE A CD1 1 ATOM 391 N N . LEU A 1 53 ? 14.734 9.090 8.220 1.00 35.58 ? 52 LEU A N 1 ATOM 392 C CA . LEU A 1 53 ? 15.468 10.306 8.566 1.00 36.14 ? 52 LEU A CA 1 ATOM 393 C C . LEU A 1 53 ? 16.204 10.961 7.398 1.00 39.20 ? 52 LEU A C 1 ATOM 394 O O . LEU A 1 53 ? 16.813 12.015 7.573 1.00 40.33 ? 52 LEU A O 1 ATOM 395 C CB . LEU A 1 53 ? 16.423 10.042 9.734 1.00 34.35 ? 52 LEU A CB 1 ATOM 396 C CG . LEU A 1 53 ? 15.698 9.857 11.070 1.00 32.40 ? 52 LEU A CG 1 ATOM 397 C CD1 . LEU A 1 53 ? 16.475 8.980 12.021 1.00 31.19 ? 52 LEU A CD1 1 ATOM 398 C CD2 . LEU A 1 53 ? 15.405 11.201 11.703 1.00 32.29 ? 52 LEU A CD2 1 ATOM 399 N N . ARG A 1 54 ? 16.136 10.361 6.213 1.00 41.91 ? 53 ARG A N 1 ATOM 400 C CA . ARG A 1 54 ? 16.691 10.963 4.999 1.00 45.44 ? 53 ARG A CA 1 ATOM 401 C C . ARG A 1 54 ? 18.185 11.267 5.119 1.00 45.55 ? 53 ARG A C 1 ATOM 402 O O . ARG A 1 54 ? 18.986 10.343 5.200 1.00 45.24 ? 53 ARG A O 1 ATOM 403 C CB . ARG A 1 54 ? 15.893 12.215 4.605 1.00 48.20 ? 53 ARG A CB 1 ATOM 404 C CG . ARG A 1 54 ? 14.442 11.934 4.261 1.00 49.51 ? 53 ARG A CG 1 ATOM 405 C CD . ARG A 1 54 ? 13.755 13.206 3.820 1.00 51.90 ? 53 ARG A CD 1 ATOM 406 N NE . ARG A 1 54 ? 14.014 13.534 2.422 1.00 54.29 ? 53 ARG A NE 1 ATOM 407 C CZ . ARG A 1 54 ? 13.511 14.598 1.803 1.00 56.71 ? 53 ARG A CZ 1 ATOM 408 N NH1 . ARG A 1 54 ? 12.739 15.455 2.464 1.00 57.18 ? 53 ARG A NH1 1 ATOM 409 N NH2 . ARG A 1 54 ? 13.791 14.819 0.524 1.00 59.23 ? 53 ARG A NH2 1 ATOM 410 N N . ASP A 1 55 ? 18.555 12.549 5.121 1.00 46.52 ? 54 ASP A N 1 ATOM 411 C CA . ASP A 1 55 ? 19.951 12.958 5.281 1.00 47.14 ? 54 ASP A CA 1 ATOM 412 C C . ASP A 1 55 ? 20.276 13.375 6.722 1.00 44.81 ? 54 ASP A C 1 ATOM 413 O O . ASP A 1 55 ? 21.277 14.040 6.955 1.00 43.73 ? 54 ASP A O 1 ATOM 414 C CB . ASP A 1 55 ? 20.272 14.109 4.329 1.00 49.81 ? 54 ASP A CB 1 ATOM 415 C CG . ASP A 1 55 ? 20.244 13.685 2.884 1.00 52.80 ? 54 ASP A CG 1 ATOM 416 O OD1 . ASP A 1 55 ? 20.738 12.571 2.600 1.00 53.69 ? 54 ASP A OD1 1 ATOM 417 O OD2 . ASP A 1 55 ? 19.737 14.459 2.035 1.00 54.51 ? 54 ASP A OD2 1 ATOM 418 N N . CYS A 1 56 ? 19.431 12.986 7.677 1.00 43.17 ? 55 CYS A N 1 ATOM 419 C CA . CYS A 1 56 ? 19.623 13.367 9.069 1.00 41.63 ? 55 CYS A CA 1 ATOM 420 C C . CYS A 1 56 ? 19.974 12.169 9.926 1.00 38.87 ? 55 CYS A C 1 ATOM 421 O O . CYS A 1 56 ? 19.466 11.063 9.720 1.00 38.49 ? 55 CYS A O 1 ATOM 422 C CB . CYS A 1 56 ? 18.374 14.052 9.620 1.00 42.73 ? 55 CYS A CB 1 ATOM 423 S SG . CYS A 1 56 ? 18.125 15.736 8.980 1.00 47.36 ? 55 CYS A SG 1 ATOM 424 N N . SER A 1 57 ? 20.863 12.397 10.884 1.00 36.89 ? 56 SER A N 1 ATOM 425 C CA . SER A 1 57 ? 21.159 11.412 11.905 1.00 34.81 ? 56 SER A CA 1 ATOM 426 C C . SER A 1 57 ? 20.135 11.503 13.017 1.00 33.32 ? 56 SER A C 1 ATOM 427 O O . SER A 1 57 ? 19.360 12.467 13.106 1.00 33.71 ? 56 SER A O 1 ATOM 428 C CB . SER A 1 57 ? 22.530 11.663 12.513 1.00 34.15 ? 56 SER A CB 1 ATOM 429 O OG . SER A 1 57 ? 22.476 12.837 13.294 1.00 34.02 ? 56 SER A OG 1 ATOM 430 N N . VAL A 1 58 ? 20.183 10.505 13.892 1.00 31.21 ? 57 VAL A N 1 ATOM 431 C CA . VAL A 1 58 ? 19.372 10.471 15.094 1.00 29.23 ? 57 VAL A CA 1 ATOM 432 C C . VAL A 1 58 ? 19.645 11.695 15.969 1.00 29.12 ? 57 VAL A C 1 ATOM 433 O O . VAL A 1 58 ? 18.720 12.306 16.479 1.00 30.19 ? 57 VAL A O 1 ATOM 434 C CB . VAL A 1 58 ? 19.628 9.165 15.876 1.00 27.86 ? 57 VAL A CB 1 ATOM 435 C CG1 . VAL A 1 58 ? 18.978 9.207 17.246 1.00 26.87 ? 57 VAL A CG1 1 ATOM 436 C CG2 . VAL A 1 58 ? 19.114 7.964 15.083 1.00 28.32 ? 57 VAL A CG2 1 ATOM 437 N N . ALA A 1 59 ? 20.914 12.048 16.140 1.00 29.09 ? 58 ALA A N 1 ATOM 438 C CA . ALA A 1 59 ? 21.303 13.185 16.972 1.00 28.39 ? 58 ALA A CA 1 ATOM 439 C C . ALA A 1 59 ? 20.801 14.513 16.414 1.00 28.83 ? 58 ALA A C 1 ATOM 440 O O . ALA A 1 59 ? 20.343 15.378 17.169 1.00 28.01 ? 58 ALA A O 1 ATOM 441 C CB . ALA A 1 59 ? 22.822 13.233 17.129 1.00 28.74 ? 58 ALA A CB 1 ATOM 442 N N . GLY A 1 60 ? 20.912 14.674 15.099 1.00 30.18 ? 59 GLY A N 1 ATOM 443 C CA . GLY A 1 60 ? 20.430 15.882 14.416 1.00 31.60 ? 59 GLY A CA 1 ATOM 444 C C . GLY A 1 60 ? 18.932 16.047 14.560 1.00 31.41 ? 59 GLY A C 1 ATOM 445 O O . GLY A 1 60 ? 18.421 17.157 14.752 1.00 32.10 ? 59 GLY A O 1 ATOM 446 N N . TRP A 1 61 ? 18.232 14.925 14.461 1.00 31.17 ? 60 TRP A N 1 ATOM 447 C CA . TRP A 1 61 ? 16.788 14.874 14.690 1.00 31.29 ? 60 TRP A CA 1 ATOM 448 C C . TRP A 1 61 ? 16.453 15.313 16.117 1.00 30.87 ? 60 TRP A C 1 ATOM 449 O O . TRP A 1 61 ? 15.668 16.240 16.303 1.00 31.37 ? 60 TRP A O 1 ATOM 450 C CB . TRP A 1 61 ? 16.265 13.455 14.407 1.00 30.78 ? 60 TRP A CB 1 ATOM 451 C CG . TRP A 1 61 ? 14.915 13.140 14.982 1.00 30.93 ? 60 TRP A CG 1 ATOM 452 C CD1 . TRP A 1 61 ? 13.815 13.960 15.017 1.00 31.72 ? 60 TRP A CD1 1 ATOM 453 C CD2 . TRP A 1 61 ? 14.505 11.898 15.569 1.00 29.99 ? 60 TRP A CD2 1 ATOM 454 N NE1 . TRP A 1 61 ? 12.757 13.309 15.611 1.00 31.15 ? 60 TRP A NE1 1 ATOM 455 C CE2 . TRP A 1 61 ? 13.150 12.042 15.954 1.00 30.29 ? 60 TRP A CE2 1 ATOM 456 C CE3 . TRP A 1 61 ? 15.151 10.679 15.810 1.00 29.19 ? 60 TRP A CE3 1 ATOM 457 C CZ2 . TRP A 1 61 ? 12.431 11.012 16.562 1.00 29.73 ? 60 TRP A CZ2 1 ATOM 458 C CZ3 . TRP A 1 61 ? 14.441 9.660 16.419 1.00 28.97 ? 60 TRP A CZ3 1 ATOM 459 C CH2 . TRP A 1 61 ? 13.089 9.837 16.794 1.00 29.50 ? 60 TRP A CH2 1 ATOM 460 N N . LEU A 1 62 ? 17.072 14.674 17.115 1.00 29.34 ? 61 LEU A N 1 ATOM 461 C CA . LEU A 1 62 ? 16.716 14.935 18.513 1.00 28.80 ? 61 LEU A CA 1 ATOM 462 C C . LEU A 1 62 ? 17.115 16.322 19.016 1.00 29.19 ? 61 LEU A C 1 ATOM 463 O O . LEU A 1 62 ? 16.342 16.978 19.716 1.00 30.96 ? 61 LEU A O 1 ATOM 464 C CB . LEU A 1 62 ? 17.295 13.856 19.432 1.00 27.59 ? 61 LEU A CB 1 ATOM 465 C CG . LEU A 1 62 ? 16.749 12.442 19.173 1.00 27.64 ? 61 LEU A CG 1 ATOM 466 C CD1 . LEU A 1 62 ? 17.419 11.445 20.101 1.00 26.90 ? 61 LEU A CD1 1 ATOM 467 C CD2 . LEU A 1 62 ? 15.236 12.364 19.325 1.00 27.65 ? 61 LEU A CD2 1 ATOM 468 N N . LEU A 1 63 ? 18.307 16.778 18.671 1.00 28.84 ? 62 LEU A N 1 ATOM 469 C CA . LEU A 1 63 ? 18.755 18.095 19.093 1.00 28.95 ? 62 LEU A CA 1 ATOM 470 C C . LEU A 1 63 ? 18.042 19.190 18.309 1.00 30.86 ? 62 LEU A C 1 ATOM 471 O O . LEU A 1 63 ? 17.855 20.299 18.799 1.00 31.24 ? 62 LEU A O 1 ATOM 472 C CB . LEU A 1 63 ? 20.274 18.203 18.950 1.00 29.21 ? 62 LEU A CB 1 ATOM 473 C CG . LEU A 1 63 ? 21.037 17.217 19.862 1.00 27.56 ? 62 LEU A CG 1 ATOM 474 C CD1 . LEU A 1 63 ? 22.492 17.048 19.464 1.00 27.73 ? 62 LEU A CD1 1 ATOM 475 C CD2 . LEU A 1 63 ? 20.940 17.650 21.311 1.00 27.07 ? 62 LEU A CD2 1 ATOM 476 N N . GLY A 1 64 ? 17.611 18.872 17.096 1.00 32.22 ? 63 GLY A N 1 ATOM 477 C CA . GLY A 1 64 ? 16.912 19.837 16.281 1.00 34.21 ? 63 GLY A CA 1 ATOM 478 C C . GLY A 1 64 ? 17.841 20.644 15.400 1.00 36.10 ? 63 GLY A C 1 ATOM 479 O O . GLY A 1 64 ? 17.776 21.873 15.380 1.00 38.06 ? 63 GLY A O 1 ATOM 480 N N . ASN A 1 65 ? 18.698 19.941 14.670 1.00 36.11 ? 64 ASN A N 1 ATOM 481 C CA . ASN A 1 65 ? 19.511 20.526 13.602 1.00 38.10 ? 64 ASN A CA 1 ATOM 482 C C . ASN A 1 65 ? 18.600 21.199 12.580 1.00 40.40 ? 64 ASN A C 1 ATOM 483 O O . ASN A 1 65 ? 17.684 20.556 12.088 1.00 40.94 ? 64 ASN A O 1 ATOM 484 C CB . ASN A 1 65 ? 20.311 19.393 12.925 1.00 37.52 ? 64 ASN A CB 1 ATOM 485 C CG . ASN A 1 65 ? 21.299 19.890 11.871 1.00 38.87 ? 64 ASN A CG 1 ATOM 486 O OD1 . ASN A 1 65 ? 21.081 20.903 11.197 1.00 39.94 ? 64 ASN A OD1 1 ATOM 487 N ND2 . ASN A 1 65 ? 22.389 19.151 11.713 1.00 38.25 ? 64 ASN A ND2 1 ATOM 488 N N . PRO A 1 66 ? 18.840 22.489 12.257 1.00 43.04 ? 65 PRO A N 1 ATOM 489 C CA . PRO A 1 66 ? 17.974 23.238 11.334 1.00 45.47 ? 65 PRO A CA 1 ATOM 490 C C . PRO A 1 66 ? 17.698 22.556 9.994 1.00 47.29 ? 65 PRO A C 1 ATOM 491 O O . PRO A 1 66 ? 16.609 22.727 9.436 1.00 49.57 ? 65 PRO A O 1 ATOM 492 C CB . PRO A 1 66 ? 18.749 24.532 11.096 1.00 47.52 ? 65 PRO A CB 1 ATOM 493 C CG . PRO A 1 66 ? 19.569 24.720 12.320 1.00 45.85 ? 65 PRO A CG 1 ATOM 494 C CD . PRO A 1 66 ? 19.890 23.350 12.839 1.00 43.44 ? 65 PRO A CD 1 ATOM 495 N N . MET A 1 67 ? 18.663 21.788 9.489 1.00 47.46 ? 66 MET A N 1 ATOM 496 C CA . MET A 1 67 ? 18.484 21.004 8.255 1.00 48.96 ? 66 MET A CA 1 ATOM 497 C C . MET A 1 67 ? 17.518 19.822 8.425 1.00 47.99 ? 66 MET A C 1 ATOM 498 O O . MET A 1 67 ? 17.127 19.205 7.439 1.00 49.07 ? 66 MET A O 1 ATOM 499 C CB . MET A 1 67 ? 19.833 20.463 7.758 1.00 49.27 ? 66 MET A CB 1 ATOM 500 C CG . MET A 1 67 ? 20.936 21.506 7.619 1.00 50.92 ? 66 MET A CG 1 ATOM 501 S SD . MET A 1 67 ? 20.402 23.002 6.766 1.00 55.09 ? 66 MET A SD 1 ATOM 502 C CE . MET A 1 67 ? 20.099 22.368 5.114 1.00 56.32 ? 66 MET A CE 1 ATOM 503 N N . CYS A 1 68 ? 17.139 19.518 9.667 1.00 46.14 ? 67 CYS A N 1 ATOM 504 C CA . CYS A 1 68 ? 16.280 18.377 9.991 1.00 45.29 ? 67 CYS A CA 1 ATOM 505 C C . CYS A 1 68 ? 14.858 18.787 10.421 1.00 45.53 ? 67 CYS A C 1 ATOM 506 O O . CYS A 1 68 ? 14.159 18.023 11.095 1.00 44.07 ? 67 CYS A O 1 ATOM 507 C CB . CYS A 1 68 ? 16.960 17.533 11.091 1.00 43.31 ? 67 CYS A CB 1 ATOM 508 S SG . CYS A 1 68 ? 18.587 16.894 10.611 1.00 42.97 ? 67 CYS A SG 1 ATOM 509 N N . ASP A 1 69 ? 14.424 19.974 9.999 1.00 47.51 ? 68 ASP A N 1 ATOM 510 C CA . ASP A 1 69 ? 13.110 20.514 10.386 1.00 48.17 ? 68 ASP A CA 1 ATOM 511 C C . ASP A 1 69 ? 11.911 19.695 9.886 1.00 48.69 ? 68 ASP A C 1 ATOM 512 O O . ASP A 1 69 ? 10.793 19.874 10.376 1.00 48.37 ? 68 ASP A O 1 ATOM 513 C CB . ASP A 1 69 ? 12.959 21.981 9.930 1.00 50.54 ? 68 ASP A CB 1 ATOM 514 C CG . ASP A 1 69 ? 13.628 22.972 10.888 1.00 49.95 ? 68 ASP A CG 1 ATOM 515 O OD1 . ASP A 1 69 ? 14.030 22.567 12.001 1.00 47.69 ? 68 ASP A OD1 1 ATOM 516 O OD2 . ASP A 1 69 ? 13.742 24.160 10.529 1.00 51.13 ? 68 ASP A OD2 1 ATOM 517 N N . GLU A 1 70 ? 12.137 18.813 8.914 1.00 49.02 ? 69 GLU A N 1 ATOM 518 C CA . GLU A 1 70 ? 11.138 17.818 8.537 1.00 49.21 ? 69 GLU A CA 1 ATOM 519 C C . GLU A 1 70 ? 10.677 16.991 9.747 1.00 46.48 ? 69 GLU A C 1 ATOM 520 O O . GLU A 1 70 ? 9.510 16.610 9.823 1.00 46.93 ? 69 GLU A O 1 ATOM 521 C CB . GLU A 1 70 ? 11.691 16.892 7.444 1.00 50.37 ? 69 GLU A CB 1 ATOM 522 C CG . GLU A 1 70 ? 10.763 15.738 7.074 1.00 51.86 ? 69 GLU A CG 1 ATOM 523 C CD . GLU A 1 70 ? 11.185 14.987 5.819 1.00 54.43 ? 69 GLU A CD 1 ATOM 524 O OE1 . GLU A 1 70 ? 12.188 15.385 5.177 1.00 56.06 ? 69 GLU A OE1 1 ATOM 525 O OE2 . GLU A 1 70 ? 10.500 13.994 5.465 1.00 55.42 ? 69 GLU A OE2 1 ATOM 526 N N . PHE A 1 71 ? 11.586 16.739 10.693 1.00 43.87 ? 70 PHE A N 1 ATOM 527 C CA . PHE A 1 71 ? 11.328 15.825 11.818 1.00 41.64 ? 70 PHE A CA 1 ATOM 528 C C . PHE A 1 71 ? 11.069 16.484 13.172 1.00 40.55 ? 70 PHE A C 1 ATOM 529 O O . PHE A 1 71 ? 11.143 15.808 14.187 1.00 38.30 ? 70 PHE A O 1 ATOM 530 C CB . PHE A 1 71 ? 12.503 14.848 11.963 1.00 39.78 ? 70 PHE A CB 1 ATOM 531 C CG . PHE A 1 71 ? 12.915 14.235 10.673 1.00 40.35 ? 70 PHE A CG 1 ATOM 532 C CD1 . PHE A 1 71 ? 12.126 13.264 10.082 1.00 40.81 ? 70 PHE A CD1 1 ATOM 533 C CD2 . PHE A 1 71 ? 14.046 14.678 10.011 1.00 40.91 ? 70 PHE A CD2 1 ATOM 534 C CE1 . PHE A 1 71 ? 12.475 12.715 8.867 1.00 41.94 ? 70 PHE A CE1 1 ATOM 535 C CE2 . PHE A 1 71 ? 14.406 14.133 8.794 1.00 41.92 ? 70 PHE A CE2 1 ATOM 536 C CZ . PHE A 1 71 ? 13.618 13.151 8.218 1.00 42.46 ? 70 PHE A CZ 1 ATOM 537 N N . LEU A 1 72 ? 10.745 17.779 13.196 1.00 41.89 ? 71 LEU A N 1 ATOM 538 C CA . LEU A 1 72 ? 10.491 18.476 14.461 1.00 41.28 ? 71 LEU A CA 1 ATOM 539 C C . LEU A 1 72 ? 9.506 17.724 15.375 1.00 40.58 ? 71 LEU A C 1 ATOM 540 O O . LEU A 1 72 ? 9.808 17.490 16.561 1.00 39.21 ? 71 LEU A O 1 ATOM 541 C CB . LEU A 1 72 ? 9.998 19.911 14.212 1.00 43.37 ? 71 LEU A CB 1 ATOM 542 C CG . LEU A 1 72 ? 11.067 20.951 13.857 1.00 44.03 ? 71 LEU A CG 1 ATOM 543 C CD1 . LEU A 1 72 ? 10.429 22.281 13.502 1.00 46.47 ? 71 LEU A CD1 1 ATOM 544 C CD2 . LEU A 1 72 ? 12.073 21.155 14.979 1.00 42.75 ? 71 LEU A CD2 1 ATOM 545 N N . ASN A 1 73 ? 8.349 17.349 14.820 1.00 40.97 ? 72 ASN A N 1 ATOM 546 C CA . ASN A 1 73 ? 7.307 16.624 15.558 1.00 40.75 ? 72 ASN A CA 1 ATOM 547 C C . ASN A 1 73 ? 6.760 15.423 14.793 1.00 39.81 ? 72 ASN A C 1 ATOM 548 O O . ASN A 1 73 ? 5.701 15.503 14.183 1.00 41.89 ? 72 ASN A O 1 ATOM 549 C CB . ASN A 1 73 ? 6.148 17.559 15.881 1.00 43.10 ? 72 ASN A CB 1 ATOM 550 C CG . ASN A 1 73 ? 6.547 18.650 16.830 1.00 43.73 ? 72 ASN A CG 1 ATOM 551 O OD1 . ASN A 1 73 ? 6.665 18.420 18.041 1.00 44.00 ? 72 ASN A OD1 1 ATOM 552 N ND2 . ASN A 1 73 ? 6.763 19.852 16.293 1.00 44.97 ? 72 ASN A ND2 1 ATOM 553 N N . VAL A 1 74 ? 7.464 14.305 14.868 1.00 36.91 ? 73 VAL A N 1 ATOM 554 C CA . VAL A 1 74 ? 7.146 13.147 14.038 1.00 36.43 ? 73 VAL A CA 1 ATOM 555 C C . VAL A 1 74 ? 6.025 12.287 14.625 1.00 35.89 ? 73 VAL A C 1 ATOM 556 O O . VAL A 1 74 ? 5.909 12.149 15.848 1.00 34.90 ? 73 VAL A O 1 ATOM 557 C CB . VAL A 1 74 ? 8.396 12.281 13.764 1.00 34.81 ? 73 VAL A CB 1 ATOM 558 C CG1 . VAL A 1 74 ? 9.472 13.134 13.126 1.00 35.24 ? 73 VAL A CG1 1 ATOM 559 C CG2 . VAL A 1 74 ? 8.933 11.636 15.037 1.00 33.14 ? 73 VAL A CG2 1 ATOM 560 N N . PRO A 1 75 ? 5.198 11.696 13.747 1.00 36.30 ? 74 PRO A N 1 ATOM 561 C CA . PRO A 1 75 ? 4.185 10.764 14.199 1.00 36.30 ? 74 PRO A CA 1 ATOM 562 C C . PRO A 1 75 ? 4.776 9.417 14.574 1.00 34.64 ? 74 PRO A C 1 ATOM 563 O O . PRO A 1 75 ? 5.931 9.120 14.283 1.00 33.28 ? 74 PRO A O 1 ATOM 564 C CB . PRO A 1 75 ? 3.290 10.609 12.975 1.00 38.37 ? 74 PRO A CB 1 ATOM 565 C CG . PRO A 1 75 ? 4.218 10.795 11.829 1.00 38.39 ? 74 PRO A CG 1 ATOM 566 C CD . PRO A 1 75 ? 5.198 11.836 12.280 1.00 37.43 ? 74 PRO A CD 1 ATOM 567 N N . GLU A 1 76 ? 3.964 8.608 15.224 1.00 34.94 ? 75 GLU A N 1 ATOM 568 C CA . GLU A 1 76 ? 4.345 7.263 15.581 1.00 34.27 ? 75 GLU A CA 1 ATOM 569 C C . GLU A 1 76 ? 4.998 6.538 14.402 1.00 33.73 ? 75 GLU A C 1 ATOM 570 O O . GLU A 1 76 ? 4.533 6.631 13.271 1.00 35.71 ? 75 GLU A O 1 ATOM 571 C CB . GLU A 1 76 ? 3.102 6.528 16.062 1.00 36.22 ? 75 GLU A CB 1 ATOM 572 C CG . GLU A 1 76 ? 3.281 5.053 16.351 1.00 36.99 ? 75 GLU A CG 1 ATOM 573 C CD . GLU A 1 76 ? 2.058 4.446 16.995 1.00 39.12 ? 75 GLU A CD 1 ATOM 574 O OE1 . GLU A 1 76 ? 1.039 5.160 17.164 1.00 41.86 ? 75 GLU A OE1 1 ATOM 575 O OE2 . GLU A 1 76 ? 2.118 3.248 17.335 1.00 40.12 ? 75 GLU A OE2 1 ATOM 576 N N . TRP A 1 77 ? 6.080 5.823 14.672 1.00 31.69 ? 76 TRP A N 1 ATOM 577 C CA . TRP A 1 77 ? 6.764 5.040 13.646 1.00 31.27 ? 76 TRP A CA 1 ATOM 578 C C . TRP A 1 77 ? 6.784 3.550 13.982 1.00 30.22 ? 76 TRP A C 1 ATOM 579 O O . TRP A 1 77 ? 6.392 3.135 15.055 1.00 29.63 ? 76 TRP A O 1 ATOM 580 C CB . TRP A 1 77 ? 8.180 5.563 13.438 1.00 30.66 ? 76 TRP A CB 1 ATOM 581 C CG . TRP A 1 77 ? 9.080 5.433 14.654 1.00 29.83 ? 76 TRP A CG 1 ATOM 582 C CD1 . TRP A 1 77 ? 9.859 4.362 14.990 1.00 29.18 ? 76 TRP A CD1 1 ATOM 583 C CD2 . TRP A 1 77 ? 9.280 6.410 15.681 1.00 29.16 ? 76 TRP A CD2 1 ATOM 584 N NE1 . TRP A 1 77 ? 10.532 4.616 16.164 1.00 28.53 ? 76 TRP A NE1 1 ATOM 585 C CE2 . TRP A 1 77 ? 10.198 5.867 16.604 1.00 28.16 ? 76 TRP A CE2 1 ATOM 586 C CE3 . TRP A 1 77 ? 8.789 7.698 15.900 1.00 29.80 ? 76 TRP A CE3 1 ATOM 587 C CZ2 . TRP A 1 77 ? 10.624 6.562 17.730 1.00 27.52 ? 76 TRP A CZ2 1 ATOM 588 C CZ3 . TRP A 1 77 ? 9.215 8.392 17.031 1.00 28.88 ? 76 TRP A CZ3 1 ATOM 589 C CH2 . TRP A 1 77 ? 10.119 7.824 17.926 1.00 27.73 ? 76 TRP A CH2 1 ATOM 590 N N . SER A 1 78 ? 7.211 2.741 13.034 1.00 30.56 ? 77 SER A N 1 ATOM 591 C CA . SER A 1 78 ? 7.278 1.288 13.230 1.00 30.61 ? 77 SER A CA 1 ATOM 592 C C . SER A 1 78 ? 8.714 0.873 13.282 1.00 29.61 ? 77 SER A C 1 ATOM 593 O O . SER A 1 78 ? 9.051 -0.039 14.004 1.00 29.73 ? 77 SER A O 1 ATOM 594 C CB . SER A 1 78 ? 6.573 0.525 12.106 1.00 31.96 ? 77 SER A CB 1 ATOM 595 O OG . SER A 1 78 ? 7.008 0.950 10.824 1.00 32.27 ? 77 SER A OG 1 ATOM 596 N N . TYR A 1 79 ? 9.544 1.524 12.483 1.00 29.87 ? 78 TYR A N 1 ATOM 597 C CA . TYR A 1 79 ? 10.993 1.417 12.614 1.00 29.51 ? 78 TYR A CA 1 ATOM 598 C C . TYR A 1 79 ? 11.677 2.711 12.147 1.00 30.03 ? 78 TYR A C 1 ATOM 599 O O . TYR A 1 79 ? 11.053 3.578 11.529 1.00 30.86 ? 78 TYR A O 1 ATOM 600 C CB . TYR A 1 79 ? 11.531 0.192 11.879 1.00 29.50 ? 78 TYR A CB 1 ATOM 601 C CG . TYR A 1 79 ? 11.252 0.192 10.406 1.00 31.18 ? 78 TYR A CG 1 ATOM 602 C CD1 . TYR A 1 79 ? 10.008 -0.195 9.922 1.00 31.62 ? 78 TYR A CD1 1 ATOM 603 C CD2 . TYR A 1 79 ? 12.231 0.576 9.486 1.00 31.54 ? 78 TYR A CD2 1 ATOM 604 C CE1 . TYR A 1 79 ? 9.739 -0.195 8.583 1.00 32.95 ? 78 TYR A CE1 1 ATOM 605 C CE2 . TYR A 1 79 ? 11.963 0.573 8.128 1.00 32.88 ? 78 TYR A CE2 1 ATOM 606 C CZ . TYR A 1 79 ? 10.703 0.192 7.684 1.00 33.51 ? 78 TYR A CZ 1 ATOM 607 O OH . TYR A 1 79 ? 10.395 0.183 6.337 1.00 34.85 ? 78 TYR A OH 1 ATOM 608 N N . ILE A 1 80 ? 12.944 2.859 12.508 1.00 30.39 ? 79 ILE A N 1 ATOM 609 C CA . ILE A 1 80 ? 13.716 4.024 12.119 1.00 31.19 ? 79 ILE A CA 1 ATOM 610 C C . ILE A 1 80 ? 14.716 3.627 11.053 1.00 32.50 ? 79 ILE A C 1 ATOM 611 O O . ILE A 1 80 ? 15.235 2.507 11.061 1.00 33.18 ? 79 ILE A O 1 ATOM 612 C CB . ILE A 1 80 ? 14.409 4.659 13.336 1.00 30.24 ? 79 ILE A CB 1 ATOM 613 C CG1 . ILE A 1 80 ? 13.343 5.168 14.300 1.00 29.56 ? 79 ILE A CG1 1 ATOM 614 C CG2 . ILE A 1 80 ? 15.322 5.808 12.900 1.00 30.67 ? 79 ILE A CG2 1 ATOM 615 C CD1 . ILE A 1 80 ? 13.859 5.480 15.677 1.00 29.06 ? 79 ILE A CD1 1 ATOM 616 N N . VAL A 1 81 ? 14.940 4.539 10.110 1.00 33.63 ? 80 VAL A N 1 ATOM 617 C CA . VAL A 1 81 ? 15.888 4.335 9.036 1.00 34.33 ? 80 VAL A CA 1 ATOM 618 C C . VAL A 1 81 ? 16.878 5.498 8.996 1.00 34.53 ? 80 VAL A C 1 ATOM 619 O O . VAL A 1 81 ? 16.483 6.657 8.848 1.00 34.32 ? 80 VAL A O 1 ATOM 620 C CB . VAL A 1 81 ? 15.183 4.222 7.683 1.00 36.19 ? 80 VAL A CB 1 ATOM 621 C CG1 . VAL A 1 81 ? 16.214 4.054 6.572 1.00 37.26 ? 80 VAL A CG1 1 ATOM 622 C CG2 . VAL A 1 81 ? 14.208 3.057 7.700 1.00 36.58 ? 80 VAL A CG2 1 ATOM 623 N N . GLU A 1 82 ? 18.158 5.162 9.156 1.00 35.03 ? 81 GLU A N 1 ATOM 624 C CA . GLU A 1 82 ? 19.257 6.117 9.121 1.00 35.73 ? 81 GLU A CA 1 ATOM 625 C C . GLU A 1 82 ? 20.191 5.721 7.964 1.00 37.45 ? 81 GLU A C 1 ATOM 626 O O . GLU A 1 82 ? 20.374 4.535 7.683 1.00 36.93 ? 81 GLU A O 1 ATOM 627 C CB . GLU A 1 82 ? 19.984 6.091 10.469 1.00 35.36 ? 81 GLU A CB 1 ATOM 628 C CG . GLU A 1 82 ? 20.851 7.303 10.766 1.00 36.21 ? 81 GLU A CG 1 ATOM 629 C CD . GLU A 1 82 ? 21.520 7.248 12.142 1.00 35.85 ? 81 GLU A CD 1 ATOM 630 O OE1 . GLU A 1 82 ? 21.888 6.145 12.610 1.00 36.70 ? 81 GLU A OE1 1 ATOM 631 O OE2 . GLU A 1 82 ? 21.693 8.320 12.766 1.00 35.72 ? 81 GLU A OE2 1 ATOM 632 N N . LYS A 1 83 ? 20.748 6.702 7.260 1.00 39.03 ? 82 LYS A N 1 ATOM 633 C CA . LYS A 1 83 ? 21.754 6.408 6.231 1.00 41.42 ? 82 LYS A CA 1 ATOM 634 C C . LYS A 1 83 ? 23.067 6.028 6.911 1.00 41.34 ? 82 LYS A C 1 ATOM 635 O O . LYS A 1 83 ? 23.238 6.260 8.104 1.00 39.16 ? 82 LYS A O 1 ATOM 636 C CB . LYS A 1 83 ? 21.941 7.597 5.282 1.00 42.97 ? 82 LYS A CB 1 ATOM 637 C CG . LYS A 1 83 ? 20.842 7.691 4.235 1.00 44.75 ? 82 LYS A CG 1 ATOM 638 C CD . LYS A 1 83 ? 21.005 8.901 3.340 1.00 47.11 ? 82 LYS A CD 1 ATOM 639 C CE . LYS A 1 83 ? 20.453 8.653 1.948 1.00 49.71 ? 82 LYS A CE 1 ATOM 640 N NZ . LYS A 1 83 ? 18.984 8.415 1.927 1.00 49.83 ? 82 LYS A NZ 1 ATOM 641 N N . ILE A 1 84 ? 23.988 5.429 6.163 1.00 44.24 ? 83 ILE A N 1 ATOM 642 C CA . ILE A 1 84 ? 25.284 5.027 6.734 1.00 44.65 ? 83 ILE A CA 1 ATOM 643 C C . ILE A 1 84 ? 26.042 6.259 7.233 1.00 44.26 ? 83 ILE A C 1 ATOM 644 O O . ILE A 1 84 ? 26.562 6.239 8.339 1.00 43.89 ? 83 ILE A O 1 ATOM 645 C CB . ILE A 1 84 ? 26.165 4.208 5.757 1.00 47.35 ? 83 ILE A CB 1 ATOM 646 C CG1 . ILE A 1 84 ? 25.654 2.761 5.583 1.00 48.29 ? 83 ILE A CG1 1 ATOM 647 C CG2 . ILE A 1 84 ? 27.588 4.109 6.293 1.00 47.93 ? 83 ILE A CG2 1 ATOM 648 C CD1 . ILE A 1 84 ? 24.205 2.593 5.126 1.00 48.81 ? 83 ILE A CD1 1 ATOM 649 N N . ASN A 1 85 ? 26.081 7.334 6.446 1.00 45.44 ? 84 ASN A N 1 ATOM 650 C CA . ASN A 1 85 ? 26.792 8.559 6.861 1.00 45.76 ? 84 ASN A CA 1 ATOM 651 C C . ASN A 1 85 ? 25.975 9.845 6.650 1.00 45.17 ? 84 ASN A C 1 ATOM 652 O O . ASN A 1 85 ? 26.189 10.580 5.684 1.00 46.38 ? 84 ASN A O 1 ATOM 653 C CB . ASN A 1 85 ? 28.137 8.654 6.132 1.00 48.49 ? 84 ASN A CB 1 ATOM 654 C CG . ASN A 1 85 ? 29.091 9.612 6.813 1.00 49.30 ? 84 ASN A CG 1 ATOM 655 O OD1 . ASN A 1 85 ? 29.538 9.353 7.930 1.00 49.28 ? 84 ASN A OD1 1 ATOM 656 N ND2 . ASN A 1 85 ? 29.402 10.725 6.154 1.00 50.92 ? 84 ASN A ND2 1 ATOM 657 N N . PRO A 1 86 ? 25.035 10.127 7.564 1.00 43.26 ? 85 PRO A N 1 ATOM 658 C CA . PRO A 1 86 ? 24.120 11.238 7.311 1.00 43.11 ? 85 PRO A CA 1 ATOM 659 C C . PRO A 1 86 ? 24.842 12.574 7.324 1.00 44.05 ? 85 PRO A C 1 ATOM 660 O O . PRO A 1 86 ? 25.644 12.839 8.224 1.00 42.98 ? 85 PRO A O 1 ATOM 661 C CB . PRO A 1 86 ? 23.111 11.160 8.468 1.00 41.13 ? 85 PRO A CB 1 ATOM 662 C CG . PRO A 1 86 ? 23.307 9.826 9.102 1.00 40.34 ? 85 PRO A CG 1 ATOM 663 C CD . PRO A 1 86 ? 24.732 9.431 8.827 1.00 41.40 ? 85 PRO A CD 1 ATOM 664 N N . ALA A 1 87 ? 24.548 13.404 6.331 1.00 45.76 ? 86 ALA A N 1 ATOM 665 C CA . ALA A 1 87 ? 25.210 14.687 6.186 1.00 47.45 ? 86 ALA A CA 1 ATOM 666 C C . ALA A 1 87 ? 24.931 15.607 7.367 1.00 46.17 ? 86 ALA A C 1 ATOM 667 O O . ALA A 1 87 ? 25.831 16.296 7.837 1.00 47.41 ? 86 ALA A O 1 ATOM 668 C CB . ALA A 1 87 ? 24.774 15.351 4.897 1.00 49.98 ? 86 ALA A CB 1 ATOM 669 N N . ASN A 1 88 ? 23.692 15.595 7.848 1.00 44.58 ? 87 ASN A N 1 ATOM 670 C CA . ASN A 1 88 ? 23.235 16.516 8.896 1.00 44.00 ? 87 ASN A CA 1 ATOM 671 C C . ASN A 1 88 ? 23.215 15.876 10.281 1.00 41.98 ? 87 ASN A C 1 ATOM 672 O O . ASN A 1 88 ? 22.175 15.381 10.733 1.00 40.53 ? 87 ASN A O 1 ATOM 673 C CB . ASN A 1 88 ? 21.835 17.046 8.559 1.00 44.42 ? 87 ASN A CB 1 ATOM 674 C CG . ASN A 1 88 ? 21.779 17.703 7.198 1.00 46.70 ? 87 ASN A CG 1 ATOM 675 O OD1 . ASN A 1 88 ? 22.495 18.666 6.942 1.00 48.68 ? 87 ASN A OD1 1 ATOM 676 N ND2 . ASN A 1 88 ? 20.939 17.181 6.317 1.00 46.78 ? 87 ASN A ND2 1 ATOM 677 N N . ASP A 1 89 ? 24.369 15.903 10.946 1.00 42.12 ? 88 ASP A N 1 ATOM 678 C CA . ASP A 1 89 ? 24.535 15.314 12.268 1.00 40.04 ? 88 ASP A CA 1 ATOM 679 C C . ASP A 1 89 ? 24.629 16.468 13.277 1.00 39.94 ? 88 ASP A C 1 ATOM 680 O O . ASP A 1 89 ? 23.646 17.189 13.478 1.00 38.88 ? 88 ASP A O 1 ATOM 681 C CB . ASP A 1 89 ? 25.757 14.377 12.265 1.00 40.84 ? 88 ASP A CB 1 ATOM 682 C CG . ASP A 1 89 ? 25.985 13.686 13.611 1.00 40.24 ? 88 ASP A CG 1 ATOM 683 O OD1 . ASP A 1 89 ? 25.075 12.977 14.095 1.00 38.50 ? 88 ASP A OD1 1 ATOM 684 O OD2 . ASP A 1 89 ? 27.083 13.869 14.192 1.00 41.97 ? 88 ASP A OD2 1 ATOM 685 N N . LEU A 1 90 ? 25.792 16.659 13.903 1.00 40.45 ? 89 LEU A N 1 ATOM 686 C CA . LEU A 1 90 ? 26.026 17.807 14.763 1.00 40.00 ? 89 LEU A CA 1 ATOM 687 C C . LEU A 1 90 ? 26.565 18.935 13.882 1.00 41.32 ? 89 LEU A C 1 ATOM 688 O O . LEU A 1 90 ? 27.718 18.895 13.432 1.00 42.94 ? 89 LEU A O 1 ATOM 689 C CB . LEU A 1 90 ? 27.023 17.469 15.872 1.00 39.81 ? 89 LEU A CB 1 ATOM 690 C CG . LEU A 1 90 ? 26.653 16.424 16.934 1.00 39.16 ? 89 LEU A CG 1 ATOM 691 C CD1 . LEU A 1 90 ? 27.850 16.177 17.858 1.00 38.54 ? 89 LEU A CD1 1 ATOM 692 C CD2 . LEU A 1 90 ? 25.426 16.837 17.736 1.00 37.68 ? 89 LEU A CD2 1 ATOM 693 N N . CYS A 1 91 ? 25.725 19.929 13.618 1.00 40.90 ? 90 CYS A N 1 ATOM 694 C CA . CYS A 1 91 ? 26.105 21.030 12.739 1.00 42.32 ? 90 CYS A CA 1 ATOM 695 C C . CYS A 1 91 ? 27.229 21.831 13.399 1.00 41.22 ? 90 CYS A C 1 ATOM 696 O O . CYS A 1 91 ? 28.252 22.103 12.781 1.00 42.19 ? 90 CYS A O 1 ATOM 697 C CB . CYS A 1 91 ? 24.882 21.907 12.374 1.00 43.68 ? 90 CYS A CB 1 ATOM 698 S SG . CYS A 1 91 ? 23.882 22.546 13.753 1.00 43.06 ? 90 CYS A SG 1 ATOM 699 N N . TYR A 1 92 ? 27.040 22.189 14.662 1.00 39.24 ? 91 TYR A N 1 ATOM 700 C CA . TYR A 1 92 ? 28.140 22.666 15.490 1.00 39.00 ? 91 TYR A CA 1 ATOM 701 C C . TYR A 1 92 ? 28.891 21.430 15.989 1.00 37.45 ? 91 TYR A C 1 ATOM 702 O O . TYR A 1 92 ? 28.283 20.539 16.562 1.00 35.75 ? 91 TYR A O 1 ATOM 703 C CB . TYR A 1 92 ? 27.630 23.501 16.657 1.00 38.28 ? 91 TYR A CB 1 ATOM 704 C CG . TYR A 1 92 ? 28.692 24.393 17.240 1.00 39.13 ? 91 TYR A CG 1 ATOM 705 C CD1 . TYR A 1 92 ? 29.634 23.884 18.115 1.00 38.26 ? 91 TYR A CD1 1 ATOM 706 C CD2 . TYR A 1 92 ? 28.772 25.736 16.897 1.00 41.09 ? 91 TYR A CD2 1 ATOM 707 C CE1 . TYR A 1 92 ? 30.614 24.684 18.655 1.00 39.21 ? 91 TYR A CE1 1 ATOM 708 C CE2 . TYR A 1 92 ? 29.760 26.554 17.430 1.00 42.00 ? 91 TYR A CE2 1 ATOM 709 C CZ . TYR A 1 92 ? 30.677 26.017 18.312 1.00 41.07 ? 91 TYR A CZ 1 ATOM 710 O OH . TYR A 1 92 ? 31.673 26.786 18.862 1.00 42.46 ? 91 TYR A OH 1 ATOM 711 N N . PRO A 1 93 ? 30.208 21.355 15.743 1.00 38.03 ? 92 PRO A N 1 ATOM 712 C CA . PRO A 1 93 ? 30.892 20.093 16.014 1.00 37.27 ? 92 PRO A CA 1 ATOM 713 C C . PRO A 1 93 ? 30.962 19.764 17.497 1.00 35.89 ? 92 PRO A C 1 ATOM 714 O O . PRO A 1 93 ? 30.940 20.659 18.333 1.00 34.99 ? 92 PRO A O 1 ATOM 715 C CB . PRO A 1 93 ? 32.295 20.323 15.455 1.00 38.89 ? 92 PRO A CB 1 ATOM 716 C CG . PRO A 1 93 ? 32.484 21.801 15.499 1.00 40.27 ? 92 PRO A CG 1 ATOM 717 C CD . PRO A 1 93 ? 31.130 22.403 15.273 1.00 40.05 ? 92 PRO A CD 1 ATOM 718 N N . GLY A 1 94 ? 31.048 18.479 17.808 1.00 35.39 ? 93 GLY A N 1 ATOM 719 C CA . GLY A 1 94 ? 31.138 18.040 19.179 1.00 34.79 ? 93 GLY A CA 1 ATOM 720 C C . GLY A 1 94 ? 30.881 16.557 19.329 1.00 35.04 ? 93 GLY A C 1 ATOM 721 O O . GLY A 1 94 ? 31.266 15.758 18.471 1.00 34.31 ? 93 GLY A O 1 ATOM 722 N N . ASN A 1 95 ? 30.248 16.198 20.441 1.00 35.19 ? 94 ASN A N 1 ATOM 723 C CA . ASN A 1 95 ? 29.825 14.828 20.675 1.00 36.32 ? 94 ASN A CA 1 ATOM 724 C C . ASN A 1 95 ? 28.530 14.718 21.475 1.00 34.98 ? 94 ASN A C 1 ATOM 725 O O . ASN A 1 95 ? 28.060 15.673 22.102 1.00 34.66 ? 94 ASN A O 1 ATOM 726 C CB . ASN A 1 95 ? 30.938 13.990 21.323 1.00 37.98 ? 94 ASN A CB 1 ATOM 727 C CG . ASN A 1 95 ? 31.445 14.573 22.635 1.00 39.63 ? 94 ASN A CG 1 ATOM 728 O OD1 . ASN A 1 95 ? 31.721 15.774 22.742 1.00 40.88 ? 94 ASN A OD1 1 ATOM 729 N ND2 . ASN A 1 95 ? 31.601 13.708 23.639 1.00 39.90 ? 94 ASN A ND2 1 ATOM 730 N N . PHE A 1 96 ? 27.940 13.541 21.372 1.00 34.42 ? 95 PHE A N 1 ATOM 731 C CA . PHE A 1 96 ? 26.769 13.171 22.118 1.00 33.32 ? 95 PHE A CA 1 ATOM 732 C C . PHE A 1 96 ? 27.271 12.102 23.083 1.00 32.30 ? 95 PHE A C 1 ATOM 733 O O . PHE A 1 96 ? 27.764 11.050 22.663 1.00 32.36 ? 95 PHE A O 1 ATOM 734 C CB . PHE A 1 96 ? 25.714 12.616 21.164 1.00 34.61 ? 95 PHE A CB 1 ATOM 735 C CG . PHE A 1 96 ? 24.291 12.973 21.527 1.00 35.52 ? 95 PHE A CG 1 ATOM 736 C CD1 . PHE A 1 96 ? 23.820 12.829 22.821 1.00 36.75 ? 95 PHE A CD1 1 ATOM 737 C CD2 . PHE A 1 96 ? 23.416 13.415 20.554 1.00 37.67 ? 95 PHE A CD2 1 ATOM 738 C CE1 . PHE A 1 96 ? 22.503 13.143 23.138 1.00 37.29 ? 95 PHE A CE1 1 ATOM 739 C CE2 . PHE A 1 96 ? 22.101 13.733 20.862 1.00 38.76 ? 95 PHE A CE2 1 ATOM 740 C CZ . PHE A 1 96 ? 21.644 13.594 22.161 1.00 37.88 ? 95 PHE A CZ 1 ATOM 741 N N . ASN A 1 97 ? 27.206 12.409 24.372 1.00 30.21 ? 96 ASN A N 1 ATOM 742 C CA . ASN A 1 97 ? 27.609 11.490 25.411 1.00 30.08 ? 96 ASN A CA 1 ATOM 743 C C . ASN A 1 97 ? 26.704 10.258 25.425 1.00 27.96 ? 96 ASN A C 1 ATOM 744 O O . ASN A 1 97 ? 25.503 10.369 25.304 1.00 27.58 ? 96 ASN A O 1 ATOM 745 C CB . ASN A 1 97 ? 27.537 12.218 26.750 1.00 32.33 ? 96 ASN A CB 1 ATOM 746 C CG . ASN A 1 97 ? 28.382 11.572 27.826 1.00 34.82 ? 96 ASN A CG 1 ATOM 747 O OD1 . ASN A 1 97 ? 29.612 11.567 27.733 1.00 37.64 ? 96 ASN A OD1 1 ATOM 748 N ND2 . ASN A 1 97 ? 27.728 11.061 28.883 1.00 34.86 ? 96 ASN A ND2 1 ATOM 749 N N . ASP A 1 98 ? 27.288 9.077 25.545 1.00 28.01 ? 97 ASP A N 1 ATOM 750 C CA . ASP A 1 98 ? 26.522 7.834 25.587 1.00 26.89 ? 97 ASP A CA 1 ATOM 751 C C . ASP A 1 98 ? 25.510 7.780 24.425 1.00 25.49 ? 97 ASP A C 1 ATOM 752 O O . ASP A 1 98 ? 24.328 7.482 24.592 1.00 24.40 ? 97 ASP A O 1 ATOM 753 C CB . ASP A 1 98 ? 25.834 7.675 26.950 1.00 27.15 ? 97 ASP A CB 1 ATOM 754 C CG . ASP A 1 98 ? 26.822 7.502 28.088 1.00 28.12 ? 97 ASP A CG 1 ATOM 755 O OD1 . ASP A 1 98 ? 27.738 6.687 27.946 1.00 28.83 ? 97 ASP A OD1 1 ATOM 756 O OD2 . ASP A 1 98 ? 26.684 8.178 29.132 1.00 29.09 ? 97 ASP A OD2 1 ATOM 757 N N . TYR A 1 99 ? 26.009 8.080 23.239 1.00 25.19 ? 98 TYR A N 1 ATOM 758 C CA . TYR A 1 99 ? 25.182 8.148 22.055 1.00 24.82 ? 98 TYR A CA 1 ATOM 759 C C . TYR A 1 99 ? 24.677 6.774 21.650 1.00 24.78 ? 98 TYR A C 1 ATOM 760 O O . TYR A 1 99 ? 23.527 6.623 21.222 1.00 24.22 ? 98 TYR A O 1 ATOM 761 C CB . TYR A 1 99 ? 25.975 8.778 20.920 1.00 25.28 ? 98 TYR A CB 1 ATOM 762 C CG . TYR A 1 99 ? 25.174 9.068 19.689 1.00 25.35 ? 98 TYR A CG 1 ATOM 763 C CD1 . TYR A 1 99 ? 23.915 9.668 19.764 1.00 24.68 ? 98 TYR A CD1 1 ATOM 764 C CD2 . TYR A 1 99 ? 25.678 8.752 18.439 1.00 26.51 ? 98 TYR A CD2 1 ATOM 765 C CE1 . TYR A 1 99 ? 23.174 9.922 18.620 1.00 25.02 ? 98 TYR A CE1 1 ATOM 766 C CE2 . TYR A 1 99 ? 24.964 9.025 17.292 1.00 27.09 ? 98 TYR A CE2 1 ATOM 767 C CZ . TYR A 1 99 ? 23.705 9.602 17.381 1.00 26.07 ? 98 TYR A CZ 1 ATOM 768 O OH . TYR A 1 99 ? 23.002 9.845 16.217 1.00 25.95 ? 98 TYR A OH 1 ATOM 769 N N . GLU A 1 100 ? 25.514 5.760 21.795 1.00 24.95 ? 99 GLU A N 1 ATOM 770 C CA . GLU A 1 100 ? 25.089 4.428 21.369 1.00 25.68 ? 99 GLU A CA 1 ATOM 771 C C . GLU A 1 100 ? 23.991 3.866 22.287 1.00 24.62 ? 99 GLU A C 1 ATOM 772 O O . GLU A 1 100 ? 23.076 3.204 21.825 1.00 23.84 ? 99 GLU A O 1 ATOM 773 C CB . GLU A 1 100 ? 26.282 3.489 21.252 1.00 26.98 ? 99 GLU A CB 1 ATOM 774 C CG . GLU A 1 100 ? 27.233 3.871 20.117 1.00 28.46 ? 99 GLU A CG 1 ATOM 775 C CD . GLU A 1 100 ? 28.008 5.175 20.353 1.00 28.98 ? 99 GLU A CD 1 ATOM 776 O OE1 . GLU A 1 100 ? 28.483 5.445 21.500 1.00 28.29 ? 99 GLU A OE1 1 ATOM 777 O OE2 . GLU A 1 100 ? 28.164 5.931 19.364 1.00 29.77 ? 99 GLU A OE2 1 ATOM 778 N N . GLU A 1 101 ? 24.072 4.158 23.581 1.00 24.26 ? 100 GLU A N 1 ATOM 779 C CA . GLU A 1 101 ? 23.056 3.701 24.546 1.00 23.78 ? 100 GLU A CA 1 ATOM 780 C C . GLU A 1 101 ? 21.684 4.380 24.366 1.00 24.12 ? 100 GLU A C 1 ATOM 781 O O . GLU A 1 101 ? 20.636 3.770 24.626 1.00 24.26 ? 100 GLU A O 1 ATOM 782 C CB . GLU A 1 101 ? 23.566 3.886 25.976 1.00 22.60 ? 100 GLU A CB 1 ATOM 783 C CG . GLU A 1 101 ? 24.625 2.871 26.335 1.00 23.04 ? 100 GLU A CG 1 ATOM 784 C CD . GLU A 1 101 ? 24.055 1.493 26.592 1.00 23.47 ? 100 GLU A CD 1 ATOM 785 O OE1 . GLU A 1 101 ? 23.122 1.373 27.407 1.00 23.18 ? 100 GLU A OE1 1 ATOM 786 O OE2 . GLU A 1 101 ? 24.552 0.517 25.997 1.00 24.06 ? 100 GLU A OE2 1 ATOM 787 N N . LEU A 1 102 ? 21.700 5.631 23.923 1.00 24.12 ? 101 LEU A N 1 ATOM 788 C CA . LEU A 1 102 ? 20.483 6.351 23.635 1.00 24.77 ? 101 LEU A CA 1 ATOM 789 C C . LEU A 1 102 ? 19.795 5.751 22.414 1.00 25.63 ? 101 LEU A C 1 ATOM 790 O O . LEU A 1 102 ? 18.564 5.603 22.383 1.00 25.92 ? 101 LEU A O 1 ATOM 791 C CB . LEU A 1 102 ? 20.785 7.822 23.355 1.00 24.92 ? 101 LEU A CB 1 ATOM 792 C CG . LEU A 1 102 ? 19.544 8.650 22.970 1.00 25.48 ? 101 LEU A CG 1 ATOM 793 C CD1 . LEU A 1 102 ? 18.455 8.589 24.038 1.00 24.77 ? 101 LEU A CD1 1 ATOM 794 C CD2 . LEU A 1 102 ? 19.953 10.088 22.699 1.00 25.92 ? 101 LEU A CD2 1 ATOM 795 N N . LYS A 1 103 ? 20.602 5.423 21.410 1.00 25.98 ? 102 LYS A N 1 ATOM 796 C CA . LYS A 1 103 ? 20.110 4.830 20.183 1.00 26.62 ? 102 LYS A CA 1 ATOM 797 C C . LYS A 1 103 ? 19.479 3.478 20.468 1.00 26.71 ? 102 LYS A C 1 ATOM 798 O O . LYS A 1 103 ? 18.494 3.087 19.813 1.00 26.16 ? 102 LYS A O 1 ATOM 799 C CB . LYS A 1 103 ? 21.229 4.738 19.135 1.00 27.56 ? 102 LYS A CB 1 ATOM 800 C CG . LYS A 1 103 ? 21.595 6.117 18.585 1.00 28.44 ? 102 LYS A CG 1 ATOM 801 C CD . LYS A 1 103 ? 22.738 6.097 17.581 1.00 29.70 ? 102 LYS A CD 1 ATOM 802 C CE . LYS A 1 103 ? 22.238 6.051 16.146 1.00 31.37 ? 102 LYS A CE 1 ATOM 803 N NZ . LYS A 1 103 ? 23.346 5.878 15.152 1.00 33.31 ? 102 LYS A NZ 1 ATOM 804 N N . HIS A 1 104 ? 20.012 2.785 21.469 1.00 26.01 ? 103 HIS A N 1 ATOM 805 C CA . HIS A 1 104 ? 19.436 1.518 21.887 1.00 27.28 ? 103 HIS A CA 1 ATOM 806 C C . HIS A 1 104 ? 18.036 1.707 22.493 1.00 28.14 ? 103 HIS A C 1 ATOM 807 O O . HIS A 1 104 ? 17.105 0.956 22.186 1.00 27.98 ? 103 HIS A O 1 ATOM 808 C CB . HIS A 1 104 ? 20.355 0.839 22.878 1.00 27.38 ? 103 HIS A CB 1 ATOM 809 C CG . HIS A 1 104 ? 19.824 -0.445 23.406 1.00 27.70 ? 103 HIS A CG 1 ATOM 810 N ND1 . HIS A 1 104 ? 20.005 -1.644 22.757 1.00 28.80 ? 103 HIS A ND1 1 ATOM 811 C CD2 . HIS A 1 104 ? 19.141 -0.725 24.538 1.00 27.94 ? 103 HIS A CD2 1 ATOM 812 C CE1 . HIS A 1 104 ? 19.448 -2.609 23.462 1.00 29.41 ? 103 HIS A CE1 1 ATOM 813 N NE2 . HIS A 1 104 ? 18.912 -2.077 24.546 1.00 29.21 ? 103 HIS A NE2 1 ATOM 814 N N . LEU A 1 105 ? 17.906 2.711 23.351 1.00 28.73 ? 104 LEU A N 1 ATOM 815 C CA . LEU A 1 105 ? 16.642 3.030 23.975 1.00 30.62 ? 104 LEU A CA 1 ATOM 816 C C . LEU A 1 105 ? 15.634 3.445 22.917 1.00 31.17 ? 104 LEU A C 1 ATOM 817 O O . LEU A 1 105 ? 14.487 3.009 22.911 1.00 31.17 ? 104 LEU A O 1 ATOM 818 C CB . LEU A 1 105 ? 16.830 4.160 24.980 1.00 32.21 ? 104 LEU A CB 1 ATOM 819 C CG . LEU A 1 105 ? 15.549 4.753 25.559 1.00 34.84 ? 104 LEU A CG 1 ATOM 820 C CD1 . LEU A 1 105 ? 14.695 3.728 26.311 1.00 35.50 ? 104 LEU A CD1 1 ATOM 821 C CD2 . LEU A 1 105 ? 15.938 5.900 26.468 1.00 36.05 ? 104 LEU A CD2 1 ATOM 822 N N . LEU A 1 106 ? 16.090 4.279 22.002 1.00 30.94 ? 105 LEU A N 1 ATOM 823 C CA . LEU A 1 106 ? 15.278 4.700 20.881 1.00 31.38 ? 105 LEU A CA 1 ATOM 824 C C . LEU A 1 106 ? 14.736 3.529 20.040 1.00 31.34 ? 105 LEU A C 1 ATOM 825 O O . LEU A 1 106 ? 13.648 3.630 19.468 1.00 31.40 ? 105 LEU A O 1 ATOM 826 C CB . LEU A 1 106 ? 16.113 5.631 20.024 1.00 32.23 ? 105 LEU A CB 1 ATOM 827 C CG . LEU A 1 106 ? 15.399 6.355 18.902 1.00 34.47 ? 105 LEU A CG 1 ATOM 828 C CD1 . LEU A 1 106 ? 14.170 7.091 19.425 1.00 34.70 ? 105 LEU A CD1 1 ATOM 829 C CD2 . LEU A 1 106 ? 16.414 7.297 18.253 1.00 34.56 ? 105 LEU A CD2 1 ATOM 830 N N . SER A 1 107 ? 15.478 2.421 19.992 1.00 30.97 ? 106 SER A N 1 ATOM 831 C CA . SER A 1 107 ? 15.039 1.205 19.292 1.00 31.98 ? 106 SER A CA 1 ATOM 832 C C . SER A 1 107 ? 13.958 0.440 20.049 1.00 32.00 ? 106 SER A C 1 ATOM 833 O O . SER A 1 107 ? 13.407 -0.522 19.531 1.00 31.58 ? 106 SER A O 1 ATOM 834 C CB . SER A 1 107 ? 16.236 0.267 19.036 1.00 33.35 ? 106 SER A CB 1 ATOM 835 O OG . SER A 1 107 ? 16.601 -0.466 20.202 1.00 33.15 ? 106 SER A OG 1 ATOM 836 N N . ARG A 1 108 ? 13.695 0.858 21.287 1.00 33.35 ? 107 ARG A N 1 ATOM 837 C CA . ARG A 1 108 ? 12.643 0.298 22.131 1.00 35.29 ? 107 ARG A CA 1 ATOM 838 C C . ARG A 1 108 ? 11.391 1.195 22.179 1.00 33.57 ? 107 ARG A C 1 ATOM 839 O O . ARG A 1 108 ? 10.442 0.883 22.890 1.00 32.64 ? 107 ARG A O 1 ATOM 840 C CB . ARG A 1 108 ? 13.171 0.134 23.561 1.00 37.66 ? 107 ARG A CB 1 ATOM 841 C CG . ARG A 1 108 ? 14.490 -0.593 23.673 1.00 40.91 ? 107 ARG A CG 1 ATOM 842 C CD . ARG A 1 108 ? 14.299 -2.095 23.674 1.00 46.08 ? 107 ARG A CD 1 ATOM 843 N NE . ARG A 1 108 ? 15.375 -2.779 22.959 1.00 51.32 ? 107 ARG A NE 1 ATOM 844 C CZ . ARG A 1 108 ? 15.770 -4.035 23.191 1.00 57.28 ? 107 ARG A CZ 1 ATOM 845 N NH1 . ARG A 1 108 ? 15.194 -4.782 24.142 1.00 57.99 ? 107 ARG A NH1 1 ATOM 846 N NH2 . ARG A 1 108 ? 16.766 -4.550 22.464 1.00 58.79 ? 107 ARG A NH2 1 ATOM 847 N N . ILE A 1 109 ? 11.415 2.297 21.427 1.00 32.00 ? 108 ILE A N 1 ATOM 848 C CA . ILE A 1 109 ? 10.372 3.316 21.429 1.00 31.38 ? 108 ILE A CA 1 ATOM 849 C C . ILE A 1 109 ? 9.721 3.455 20.055 1.00 31.00 ? 108 ILE A C 1 ATOM 850 O O . ILE A 1 109 ? 10.400 3.438 19.044 1.00 31.32 ? 108 ILE A O 1 ATOM 851 C CB . ILE A 1 109 ? 10.978 4.678 21.821 1.00 30.87 ? 108 ILE A CB 1 ATOM 852 C CG1 . ILE A 1 109 ? 11.495 4.623 23.262 1.00 30.08 ? 108 ILE A CG1 1 ATOM 853 C CG2 . ILE A 1 109 ? 9.963 5.805 21.642 1.00 30.93 ? 108 ILE A CG2 1 ATOM 854 C CD1 . ILE A 1 109 ? 12.456 5.742 23.612 1.00 29.40 ? 108 ILE A CD1 1 ATOM 855 N N . ASN A 1 110 ? 8.396 3.587 20.029 1.00 32.03 ? 109 ASN A N 1 ATOM 856 C CA . ASN A 1 110 ? 7.638 3.785 18.795 1.00 31.74 ? 109 ASN A CA 1 ATOM 857 C C . ASN A 1 110 ? 7.055 5.191 18.659 1.00 31.87 ? 109 ASN A C 1 ATOM 858 O O . ASN A 1 110 ? 6.663 5.579 17.562 1.00 32.52 ? 109 ASN A O 1 ATOM 859 C CB . ASN A 1 110 ? 6.509 2.775 18.700 1.00 33.16 ? 109 ASN A CB 1 ATOM 860 C CG . ASN A 1 110 ? 7.000 1.350 18.533 1.00 33.94 ? 109 ASN A CG 1 ATOM 861 O OD1 . ASN A 1 110 ? 6.799 0.514 19.417 1.00 35.76 ? 109 ASN A OD1 1 ATOM 862 N ND2 . ASN A 1 110 ? 7.625 1.053 17.394 1.00 33.45 ? 109 ASN A ND2 1 ATOM 863 N N . HIS A 1 111 ? 6.971 5.956 19.748 1.00 31.46 ? 110 HIS A N 1 ATOM 864 C CA . HIS A 1 111 ? 6.433 7.310 19.653 1.00 32.29 ? 110 HIS A CA 1 ATOM 865 C C . HIS A 1 111 ? 6.908 8.260 20.745 1.00 31.71 ? 110 HIS A C 1 ATOM 866 O O . HIS A 1 111 ? 7.026 7.876 21.916 1.00 30.58 ? 110 HIS A O 1 ATOM 867 C CB . HIS A 1 111 ? 4.898 7.279 19.604 1.00 33.89 ? 110 HIS A CB 1 ATOM 868 C CG . HIS A 1 111 ? 4.281 8.556 19.121 1.00 35.71 ? 110 HIS A CG 1 ATOM 869 N ND1 . HIS A 1 111 ? 3.006 8.949 19.470 1.00 37.96 ? 110 HIS A ND1 1 ATOM 870 C CD2 . HIS A 1 111 ? 4.766 9.536 18.318 1.00 36.43 ? 110 HIS A CD2 1 ATOM 871 C CE1 . HIS A 1 111 ? 2.733 10.114 18.906 1.00 38.98 ? 110 HIS A CE1 1 ATOM 872 N NE2 . HIS A 1 111 ? 3.786 10.493 18.204 1.00 37.87 ? 110 HIS A NE2 1 ATOM 873 N N . PHE A 1 112 ? 7.189 9.498 20.323 1.00 32.99 ? 111 PHE A N 1 ATOM 874 C CA . PHE A 1 112 ? 7.456 10.641 21.203 1.00 33.80 ? 111 PHE A CA 1 ATOM 875 C C . PHE A 1 112 ? 6.355 11.670 21.071 1.00 35.27 ? 111 PHE A C 1 ATOM 876 O O . PHE A 1 112 ? 5.681 11.709 20.058 1.00 37.46 ? 111 PHE A O 1 ATOM 877 C CB . PHE A 1 112 ? 8.730 11.379 20.776 1.00 33.41 ? 111 PHE A CB 1 ATOM 878 C CG . PHE A 1 112 ? 10.003 10.720 21.192 1.00 32.84 ? 111 PHE A CG 1 ATOM 879 C CD1 . PHE A 1 112 ? 10.218 10.353 22.517 1.00 32.08 ? 111 PHE A CD1 1 ATOM 880 C CD2 . PHE A 1 112 ? 11.023 10.516 20.263 1.00 32.38 ? 111 PHE A CD2 1 ATOM 881 C CE1 . PHE A 1 112 ? 11.409 9.769 22.898 1.00 30.93 ? 111 PHE A CE1 1 ATOM 882 C CE2 . PHE A 1 112 ? 12.216 9.929 20.644 1.00 31.23 ? 111 PHE A CE2 1 ATOM 883 C CZ . PHE A 1 112 ? 12.407 9.556 21.963 1.00 30.90 ? 111 PHE A CZ 1 ATOM 884 N N . GLU A 1 113 ? 6.206 12.522 22.083 1.00 35.65 ? 112 GLU A N 1 ATOM 885 C CA . GLU A 1 113 ? 5.460 13.768 21.950 1.00 37.54 ? 112 GLU A CA 1 ATOM 886 C C . GLU A 1 113 ? 6.357 14.854 22.509 1.00 36.68 ? 112 GLU A C 1 ATOM 887 O O . GLU A 1 113 ? 6.609 14.893 23.711 1.00 36.53 ? 112 GLU A O 1 ATOM 888 C CB . GLU A 1 113 ? 4.114 13.717 22.703 1.00 39.88 ? 112 GLU A CB 1 ATOM 889 C CG . GLU A 1 113 ? 3.310 15.023 22.683 1.00 42.45 ? 112 GLU A CG 1 ATOM 890 C CD . GLU A 1 113 ? 2.048 14.975 23.546 1.00 45.21 ? 112 GLU A CD 1 ATOM 891 O OE1 . GLU A 1 113 ? 1.618 13.848 23.901 1.00 46.46 ? 112 GLU A OE1 1 ATOM 892 O OE2 . GLU A 1 113 ? 1.476 16.059 23.863 1.00 45.82 ? 112 GLU A OE2 1 ATOM 893 N N . LYS A 1 114 ? 6.855 15.723 21.634 1.00 36.74 ? 113 LYS A N 1 ATOM 894 C CA . LYS A 1 114 ? 7.779 16.772 22.041 1.00 35.70 ? 113 LYS A CA 1 ATOM 895 C C . LYS A 1 114 ? 7.021 17.873 22.748 1.00 36.48 ? 113 LYS A C 1 ATOM 896 O O . LYS A 1 114 ? 5.972 18.290 22.275 1.00 38.63 ? 113 LYS A O 1 ATOM 897 C CB . LYS A 1 114 ? 8.513 17.355 20.831 1.00 35.92 ? 113 LYS A CB 1 ATOM 898 C CG . LYS A 1 114 ? 9.658 18.285 21.214 1.00 35.23 ? 113 LYS A CG 1 ATOM 899 C CD . LYS A 1 114 ? 10.591 18.573 20.045 1.00 35.61 ? 113 LYS A CD 1 ATOM 900 C CE . LYS A 1 114 ? 10.061 19.698 19.169 1.00 37.58 ? 113 LYS A CE 1 ATOM 901 N NZ . LYS A 1 114 ? 10.791 19.804 17.874 1.00 38.26 ? 113 LYS A NZ 1 ATOM 902 N N . ILE A 1 115 ? 7.552 18.333 23.876 1.00 35.52 ? 114 ILE A N 1 ATOM 903 C CA . ILE A 1 115 ? 6.989 19.469 24.597 1.00 37.01 ? 114 ILE A CA 1 ATOM 904 C C . ILE A 1 115 ? 8.066 20.487 24.930 1.00 36.34 ? 114 ILE A C 1 ATOM 905 O O . ILE A 1 115 ? 9.236 20.156 25.062 1.00 33.78 ? 114 ILE A O 1 ATOM 906 C CB . ILE A 1 115 ? 6.292 19.079 25.927 1.00 37.51 ? 114 ILE A CB 1 ATOM 907 C CG1 . ILE A 1 115 ? 7.192 18.194 26.799 1.00 35.93 ? 114 ILE A CG1 1 ATOM 908 C CG2 . ILE A 1 115 ? 4.959 18.403 25.652 1.00 39.07 ? 114 ILE A CG2 1 ATOM 909 C CD1 . ILE A 1 115 ? 6.817 18.223 28.269 1.00 36.23 ? 114 ILE A CD1 1 ATOM 910 N N . GLN A 1 116 ? 7.636 21.730 25.067 1.00 38.35 ? 115 GLN A N 1 ATOM 911 C CA . GLN A 1 116 ? 8.480 22.791 25.570 1.00 38.78 ? 115 GLN A CA 1 ATOM 912 C C . GLN A 1 116 ? 8.497 22.700 27.092 1.00 38.76 ? 115 GLN A C 1 ATOM 913 O O . GLN A 1 116 ? 7.445 22.739 27.730 1.00 40.27 ? 115 GLN A O 1 ATOM 914 C CB . GLN A 1 116 ? 7.933 24.144 25.133 1.00 40.70 ? 115 GLN A CB 1 ATOM 915 C CG . GLN A 1 116 ? 8.570 25.318 25.842 1.00 41.50 ? 115 GLN A CG 1 ATOM 916 C CD . GLN A 1 116 ? 8.006 26.634 25.378 1.00 43.87 ? 115 GLN A CD 1 ATOM 917 O OE1 . GLN A 1 116 ? 8.257 27.052 24.252 1.00 44.81 ? 115 GLN A OE1 1 ATOM 918 N NE2 . GLN A 1 116 ? 7.242 27.300 26.241 1.00 45.28 ? 115 GLN A NE2 1 ATOM 919 N N . ILE A 1 117 ? 9.687 22.579 27.670 1.00 37.04 ? 116 ILE A N 1 ATOM 920 C CA . ILE A 1 117 ? 9.818 22.561 29.121 1.00 36.70 ? 116 ILE A CA 1 ATOM 921 C C . ILE A 1 117 ? 10.485 23.811 29.678 1.00 37.57 ? 116 ILE A C 1 ATOM 922 O O . ILE A 1 117 ? 10.298 24.120 30.841 1.00 38.53 ? 116 ILE A O 1 ATOM 923 C CB . ILE A 1 117 ? 10.548 21.295 29.618 1.00 34.71 ? 116 ILE A CB 1 ATOM 924 C CG1 . ILE A 1 117 ? 11.987 21.223 29.098 1.00 33.08 ? 116 ILE A CG1 1 ATOM 925 C CG2 . ILE A 1 117 ? 9.784 20.048 29.195 1.00 34.16 ? 116 ILE A CG2 1 ATOM 926 C CD1 . ILE A 1 117 ? 12.785 20.116 29.752 1.00 31.55 ? 116 ILE A CD1 1 ATOM 927 N N . ILE A 1 118 ? 11.264 24.523 28.864 1.00 38.16 ? 117 ILE A N 1 ATOM 928 C CA . ILE A 1 118 ? 11.842 25.806 29.272 1.00 39.34 ? 117 ILE A CA 1 ATOM 929 C C . ILE A 1 118 ? 11.794 26.812 28.118 1.00 40.49 ? 117 ILE A C 1 ATOM 930 O O . ILE A 1 118 ? 12.687 26.817 27.270 1.00 39.40 ? 117 ILE A O 1 ATOM 931 C CB . ILE A 1 118 ? 13.306 25.675 29.751 1.00 38.40 ? 117 ILE A CB 1 ATOM 932 C CG1 . ILE A 1 118 ? 13.433 24.648 30.874 1.00 37.15 ? 117 ILE A CG1 1 ATOM 933 C CG2 . ILE A 1 118 ? 13.828 27.033 30.225 1.00 39.69 ? 117 ILE A CG2 1 ATOM 934 C CD1 . ILE A 1 118 ? 14.867 24.354 31.267 1.00 36.30 ? 117 ILE A CD1 1 ATOM 935 N N . PRO A 1 119 ? 10.760 27.678 28.095 1.00 42.80 ? 118 PRO A N 1 ATOM 936 C CA . PRO A 1 119 ? 10.595 28.657 27.007 1.00 44.57 ? 118 PRO A CA 1 ATOM 937 C C . PRO A 1 119 ? 11.806 29.567 26.848 1.00 45.11 ? 118 PRO A C 1 ATOM 938 O O . PRO A 1 119 ? 12.491 29.863 27.824 1.00 44.30 ? 118 PRO A O 1 ATOM 939 C CB . PRO A 1 119 ? 9.370 29.486 27.415 1.00 46.78 ? 118 PRO A CB 1 ATOM 940 C CG . PRO A 1 119 ? 8.828 28.893 28.662 1.00 46.36 ? 118 PRO A CG 1 ATOM 941 C CD . PRO A 1 119 ? 9.741 27.814 29.153 1.00 43.91 ? 118 PRO A CD 1 ATOM 942 N N . LYS A 1 120 ? 12.049 30.015 25.622 1.00 46.66 ? 119 LYS A N 1 ATOM 943 C CA . LYS A 1 120 ? 13.188 30.883 25.326 1.00 47.40 ? 119 LYS A CA 1 ATOM 944 C C . LYS A 1 120 ? 13.012 32.244 25.987 1.00 49.02 ? 119 LYS A C 1 ATOM 945 O O . LYS A 1 120 ? 13.982 32.895 26.363 1.00 48.80 ? 119 LYS A O 1 ATOM 946 C CB . LYS A 1 120 ? 13.349 31.046 23.812 1.00 49.04 ? 119 LYS A CB 1 ATOM 947 C CG . LYS A 1 120 ? 14.787 30.949 23.328 1.00 48.61 ? 119 LYS A CG 1 ATOM 948 C CD . LYS A 1 120 ? 14.857 30.941 21.808 1.00 50.18 ? 119 LYS A CD 1 ATOM 949 C CE . LYS A 1 120 ? 16.173 31.523 21.321 1.00 51.22 ? 119 LYS A CE 1 ATOM 950 N NZ . LYS A 1 120 ? 16.240 31.680 19.844 1.00 52.84 ? 119 LYS A NZ 1 ATOM 951 N N . SER A 1 121 ? 11.755 32.648 26.140 1.00 50.91 ? 120 SER A N 1 ATOM 952 C CA . SER A 1 121 ? 11.393 33.944 26.709 1.00 52.98 ? 120 SER A CA 1 ATOM 953 C C . SER A 1 121 ? 11.508 34.005 28.229 1.00 51.90 ? 120 SER A C 1 ATOM 954 O O . SER A 1 121 ? 11.309 35.061 28.817 1.00 53.17 ? 120 SER A O 1 ATOM 955 C CB . SER A 1 121 ? 9.951 34.277 26.315 1.00 55.59 ? 120 SER A CB 1 ATOM 956 O OG . SER A 1 121 ? 9.071 33.259 26.760 1.00 55.02 ? 120 SER A OG 1 ATOM 957 N N . SER A 1 122 ? 11.818 32.879 28.866 1.00 49.34 ? 121 SER A N 1 ATOM 958 C CA . SER A 1 122 ? 11.814 32.805 30.325 1.00 48.59 ? 121 SER A CA 1 ATOM 959 C C . SER A 1 122 ? 13.168 33.181 30.915 1.00 47.65 ? 121 SER A C 1 ATOM 960 O O . SER A 1 122 ? 13.319 33.243 32.131 1.00 47.78 ? 121 SER A O 1 ATOM 961 C CB . SER A 1 122 ? 11.403 31.397 30.777 1.00 46.80 ? 121 SER A CB 1 ATOM 962 O OG . SER A 1 122 ? 12.486 30.482 30.690 1.00 43.86 ? 121 SER A OG 1 ATOM 963 N N . TRP A 1 123 ? 14.150 33.423 30.053 1.00 47.12 ? 122 TRP A N 1 ATOM 964 C CA . TRP A 1 123 ? 15.494 33.784 30.478 1.00 46.01 ? 122 TRP A CA 1 ATOM 965 C C . TRP A 1 123 ? 15.636 35.298 30.579 1.00 48.65 ? 122 TRP A C 1 ATOM 966 O O . TRP A 1 123 ? 16.039 35.948 29.619 1.00 50.10 ? 122 TRP A O 1 ATOM 967 C CB . TRP A 1 123 ? 16.513 33.225 29.482 1.00 44.17 ? 122 TRP A CB 1 ATOM 968 C CG . TRP A 1 123 ? 16.481 31.726 29.362 1.00 41.36 ? 122 TRP A CG 1 ATOM 969 C CD1 . TRP A 1 123 ? 15.990 31.003 28.320 1.00 40.84 ? 122 TRP A CD1 1 ATOM 970 C CD2 . TRP A 1 123 ? 16.963 30.777 30.315 1.00 38.63 ? 122 TRP A CD2 1 ATOM 971 N NE1 . TRP A 1 123 ? 16.133 29.663 28.562 1.00 38.35 ? 122 TRP A NE1 1 ATOM 972 C CE2 . TRP A 1 123 ? 16.729 29.496 29.782 1.00 37.34 ? 122 TRP A CE2 1 ATOM 973 C CE3 . TRP A 1 123 ? 17.562 30.884 31.570 1.00 38.21 ? 122 TRP A CE3 1 ATOM 974 C CZ2 . TRP A 1 123 ? 17.083 28.326 30.456 1.00 35.57 ? 122 TRP A CZ2 1 ATOM 975 C CZ3 . TRP A 1 123 ? 17.913 29.722 32.243 1.00 36.70 ? 122 TRP A CZ3 1 ATOM 976 C CH2 . TRP A 1 123 ? 17.674 28.458 31.684 1.00 35.07 ? 122 TRP A CH2 1 ATOM 977 N N . SER A 1 124 ? 15.324 35.853 31.748 1.00 50.04 ? 123 SER A N 1 ATOM 978 C CA . SER A 1 124 ? 15.243 37.319 31.930 1.00 53.32 ? 123 SER A CA 1 ATOM 979 C C . SER A 1 124 ? 16.585 38.038 32.110 1.00 53.54 ? 123 SER A C 1 ATOM 980 O O . SER A 1 124 ? 16.680 39.230 31.845 1.00 56.06 ? 123 SER A O 1 ATOM 981 C CB . SER A 1 124 ? 14.355 37.656 33.131 1.00 54.75 ? 123 SER A CB 1 ATOM 982 O OG . SER A 1 124 ? 13.239 36.785 33.182 1.00 55.14 ? 123 SER A OG 1 ATOM 983 N N . ASP A 1 125 ? 17.608 37.326 32.575 1.00 51.73 ? 124 ASP A N 1 ATOM 984 C CA . ASP A 1 125 ? 18.917 37.934 32.839 1.00 51.74 ? 124 ASP A CA 1 ATOM 985 C C . ASP A 1 125 ? 20.012 37.336 31.964 1.00 49.37 ? 124 ASP A C 1 ATOM 986 O O . ASP A 1 125 ? 21.186 37.419 32.294 1.00 48.00 ? 124 ASP A O 1 ATOM 987 C CB . ASP A 1 125 ? 19.280 37.766 34.319 1.00 51.69 ? 124 ASP A CB 1 ATOM 988 C CG . ASP A 1 125 ? 18.205 38.307 35.243 1.00 53.58 ? 124 ASP A CG 1 ATOM 989 O OD1 . ASP A 1 125 ? 17.875 39.507 35.122 1.00 56.03 ? 124 ASP A OD1 1 ATOM 990 O OD2 . ASP A 1 125 ? 17.685 37.534 36.077 1.00 52.97 ? 124 ASP A OD2 1 ATOM 991 N N . HIS A 1 126 ? 19.622 36.728 30.850 1.00 48.62 ? 125 HIS A N 1 ATOM 992 C CA . HIS A 1 126 ? 20.576 36.148 29.917 1.00 47.39 ? 125 HIS A CA 1 ATOM 993 C C . HIS A 1 126 ? 20.079 36.323 28.492 1.00 49.16 ? 125 HIS A C 1 ATOM 994 O O . HIS A 1 126 ? 18.872 36.389 28.253 1.00 50.22 ? 125 HIS A O 1 ATOM 995 C CB . HIS A 1 126 ? 20.770 34.659 30.202 1.00 44.10 ? 125 HIS A CB 1 ATOM 996 C CG . HIS A 1 126 ? 21.383 34.372 31.534 1.00 42.76 ? 125 HIS A CG 1 ATOM 997 N ND1 . HIS A 1 126 ? 20.646 34.329 32.695 1.00 42.66 ? 125 HIS A ND1 1 ATOM 998 C CD2 . HIS A 1 126 ? 22.660 34.098 31.889 1.00 41.71 ? 125 HIS A CD2 1 ATOM 999 C CE1 . HIS A 1 126 ? 21.444 34.059 33.711 1.00 41.45 ? 125 HIS A CE1 1 ATOM 1000 N NE2 . HIS A 1 126 ? 22.670 33.905 33.248 1.00 40.93 ? 125 HIS A NE2 1 ATOM 1001 N N . GLU A 1 127 ? 21.021 36.402 27.557 1.00 50.12 ? 126 GLU A N 1 ATOM 1002 C CA . GLU A 1 127 ? 20.707 36.432 26.131 1.00 51.35 ? 126 GLU A CA 1 ATOM 1003 C C . GLU A 1 127 ? 20.453 35.018 25.622 1.00 49.45 ? 126 GLU A C 1 ATOM 1004 O O . GLU A 1 127 ? 21.330 34.159 25.721 1.00 47.96 ? 126 GLU A O 1 ATOM 1005 C CB . GLU A 1 127 ? 21.853 37.066 25.342 1.00 52.58 ? 126 GLU A CB 1 ATOM 1006 C CG . GLU A 1 127 ? 21.649 38.543 25.062 1.00 55.84 ? 126 GLU A CG 1 ATOM 1007 C CD . GLU A 1 127 ? 20.595 38.800 24.003 1.00 57.42 ? 126 GLU A CD 1 ATOM 1008 O OE1 . GLU A 1 127 ? 20.026 37.815 23.470 1.00 55.43 ? 126 GLU A OE1 1 ATOM 1009 O OE2 . GLU A 1 127 ? 20.348 39.993 23.700 1.00 60.21 ? 126 GLU A OE2 1 ATOM 1010 N N . ALA A 1 128 ? 19.253 34.794 25.090 1.00 49.99 ? 127 ALA A N 1 ATOM 1011 C CA . ALA A 1 128 ? 18.834 33.487 24.594 1.00 49.06 ? 127 ALA A CA 1 ATOM 1012 C C . ALA A 1 128 ? 18.753 33.426 23.069 1.00 50.82 ? 127 ALA A C 1 ATOM 1013 O O . ALA A 1 128 ? 18.935 32.350 22.491 1.00 51.01 ? 127 ALA A O 1 ATOM 1014 C CB . ALA A 1 128 ? 17.493 33.101 25.204 1.00 48.83 ? 127 ALA A CB 1 ATOM 1015 N N . SER A 1 129 ? 18.499 34.568 22.429 1.00 53.32 ? 128 SER A N 1 ATOM 1016 C CA . SER A 1 129 ? 18.334 34.646 20.969 1.00 55.30 ? 128 SER A CA 1 ATOM 1017 C C . SER A 1 129 ? 19.600 35.109 20.227 1.00 55.78 ? 128 SER A C 1 ATOM 1018 O O . SER A 1 129 ? 19.516 35.618 19.110 1.00 57.88 ? 128 SER A O 1 ATOM 1019 C CB . SER A 1 129 ? 17.154 35.575 20.611 1.00 58.43 ? 128 SER A CB 1 ATOM 1020 O OG . SER A 1 129 ? 15.906 34.903 20.733 1.00 58.24 ? 128 SER A OG 1 ATOM 1021 N N . ALA A 1 130 ? 20.767 34.944 20.845 1.00 53.68 ? 129 ALA A N 1 ATOM 1022 C CA . ALA A 1 130 ? 22.035 35.167 20.151 1.00 53.52 ? 129 ALA A CA 1 ATOM 1023 C C . ALA A 1 130 ? 22.833 33.869 19.998 1.00 50.91 ? 129 ALA A C 1 ATOM 1024 O O . ALA A 1 130 ? 23.913 33.878 19.424 1.00 52.14 ? 129 ALA A O 1 ATOM 1025 C CB . ALA A 1 130 ? 22.859 36.205 20.887 1.00 54.33 ? 129 ALA A CB 1 ATOM 1026 N N . GLY A 1 131 ? 22.308 32.755 20.505 1.00 47.97 ? 130 GLY A N 1 ATOM 1027 C CA . GLY A 1 131 ? 23.018 31.484 20.447 1.00 45.22 ? 130 GLY A CA 1 ATOM 1028 C C . GLY A 1 131 ? 22.985 30.849 19.074 1.00 44.78 ? 130 GLY A C 1 ATOM 1029 O O . GLY A 1 131 ? 22.368 29.804 18.890 1.00 43.74 ? 130 GLY A O 1 ATOM 1030 N N . VAL A 1 132 ? 23.666 31.474 18.120 1.00 46.32 ? 131 VAL A N 1 ATOM 1031 C CA . VAL A 1 132 ? 23.644 31.046 16.725 1.00 46.94 ? 131 VAL A CA 1 ATOM 1032 C C . VAL A 1 132 ? 25.052 30.947 16.158 1.00 47.50 ? 131 VAL A C 1 ATOM 1033 O O . VAL A 1 132 ? 25.986 31.539 16.694 1.00 47.78 ? 131 VAL A O 1 ATOM 1034 C CB . VAL A 1 132 ? 22.804 31.999 15.858 1.00 49.67 ? 131 VAL A CB 1 ATOM 1035 C CG1 . VAL A 1 132 ? 21.326 31.834 16.180 1.00 49.00 ? 131 VAL A CG1 1 ATOM 1036 C CG2 . VAL A 1 132 ? 23.245 33.450 16.054 1.00 52.14 ? 131 VAL A CG2 1 ATOM 1037 N N . SER A 1 133 ? 25.189 30.205 15.063 1.00 47.84 ? 132 SER A N 1 ATOM 1038 C CA . SER A 1 133 ? 26.495 29.857 14.520 1.00 48.52 ? 132 SER A CA 1 ATOM 1039 C C . SER A 1 133 ? 26.423 29.683 13.011 1.00 50.35 ? 132 SER A C 1 ATOM 1040 O O . SER A 1 133 ? 25.419 29.204 12.487 1.00 50.56 ? 132 SER A O 1 ATOM 1041 C CB . SER A 1 133 ? 26.974 28.549 15.164 1.00 46.41 ? 132 SER A CB 1 ATOM 1042 O OG . SER A 1 133 ? 28.305 28.234 14.794 1.00 47.75 ? 132 SER A OG 1 ATOM 1043 N N . SER A 1 134 ? 27.489 30.060 12.311 1.00 52.26 ? 133 SER A N 1 ATOM 1044 C CA . SER A 1 134 ? 27.573 29.838 10.865 1.00 54.13 ? 133 SER A CA 1 ATOM 1045 C C . SER A 1 134 ? 27.694 28.347 10.540 1.00 52.77 ? 133 SER A C 1 ATOM 1046 O O . SER A 1 134 ? 27.438 27.934 9.412 1.00 53.59 ? 133 SER A O 1 ATOM 1047 C CB . SER A 1 134 ? 28.754 30.603 10.260 1.00 56.41 ? 133 SER A CB 1 ATOM 1048 O OG . SER A 1 134 ? 29.987 30.042 10.672 1.00 55.36 ? 133 SER A OG 1 ATOM 1049 N N . ALA A 1 135 ? 28.091 27.549 11.529 1.00 51.15 ? 134 ALA A N 1 ATOM 1050 C CA . ALA A 1 135 ? 28.152 26.098 11.378 1.00 50.19 ? 134 ALA A CA 1 ATOM 1051 C C . ALA A 1 135 ? 26.763 25.472 11.267 1.00 49.86 ? 134 ALA A C 1 ATOM 1052 O O . ALA A 1 135 ? 26.633 24.357 10.750 1.00 50.02 ? 134 ALA A O 1 ATOM 1053 C CB . ALA A 1 135 ? 28.912 25.474 12.539 1.00 48.02 ? 134 ALA A CB 1 ATOM 1054 N N . CYS A 1 136 ? 25.736 26.179 11.750 1.00 50.11 ? 135 CYS A N 1 ATOM 1055 C CA . CYS A 1 136 ? 24.353 25.706 11.661 1.00 49.73 ? 135 CYS A CA 1 ATOM 1056 C C . CYS A 1 136 ? 23.487 26.639 10.812 1.00 52.12 ? 135 CYS A C 1 ATOM 1057 O O . CYS A 1 136 ? 22.599 27.312 11.332 1.00 51.54 ? 135 CYS A O 1 ATOM 1058 C CB . CYS A 1 136 ? 23.758 25.552 13.060 1.00 47.61 ? 135 CYS A CB 1 ATOM 1059 S SG . CYS A 1 136 ? 24.695 24.424 14.103 1.00 45.66 ? 135 CYS A SG 1 ATOM 1060 N N . PRO A 1 137 ? 23.736 26.670 9.492 1.00 55.15 ? 136 PRO A N 1 ATOM 1061 C CA . PRO A 1 137 ? 22.973 27.567 8.630 1.00 58.45 ? 136 PRO A CA 1 ATOM 1062 C C . PRO A 1 137 ? 21.525 27.124 8.421 1.00 59.47 ? 136 PRO A C 1 ATOM 1063 O O . PRO A 1 137 ? 21.170 25.962 8.664 1.00 57.74 ? 136 PRO A O 1 ATOM 1064 C CB . PRO A 1 137 ? 23.739 27.516 7.310 1.00 60.32 ? 136 PRO A CB 1 ATOM 1065 C CG . PRO A 1 137 ? 24.352 26.161 7.291 1.00 58.46 ? 136 PRO A CG 1 ATOM 1066 C CD . PRO A 1 137 ? 24.688 25.848 8.722 1.00 55.52 ? 136 PRO A CD 1 ATOM 1067 N N . TYR A 1 138 ? 20.711 28.072 7.975 1.00 62.93 ? 137 TYR A N 1 ATOM 1068 C CA . TYR A 1 138 ? 19.310 27.839 7.674 1.00 64.11 ? 137 TYR A CA 1 ATOM 1069 C C . TYR A 1 138 ? 18.782 29.027 6.884 1.00 67.24 ? 137 TYR A C 1 ATOM 1070 O O . TYR A 1 138 ? 18.736 30.147 7.397 1.00 67.31 ? 137 TYR A O 1 ATOM 1071 C CB . TYR A 1 138 ? 18.496 27.668 8.954 1.00 62.73 ? 137 TYR A CB 1 ATOM 1072 C CG . TYR A 1 138 ? 17.007 27.619 8.699 1.00 64.34 ? 137 TYR A CG 1 ATOM 1073 C CD1 . TYR A 1 138 ? 16.412 26.487 8.140 1.00 63.99 ? 137 TYR A CD1 1 ATOM 1074 C CD2 . TYR A 1 138 ? 16.197 28.708 8.999 1.00 66.73 ? 137 TYR A CD2 1 ATOM 1075 C CE1 . TYR A 1 138 ? 15.047 26.443 7.895 1.00 65.42 ? 137 TYR A CE1 1 ATOM 1076 C CE2 . TYR A 1 138 ? 14.832 28.676 8.756 1.00 68.19 ? 137 TYR A CE2 1 ATOM 1077 C CZ . TYR A 1 138 ? 14.260 27.543 8.207 1.00 67.15 ? 137 TYR A CZ 1 ATOM 1078 O OH . TYR A 1 138 ? 12.905 27.521 7.971 1.00 68.19 ? 137 TYR A OH 1 ATOM 1079 N N . GLN A 1 139 ? 18.390 28.768 5.637 1.00 70.34 ? 138 GLN A N 1 ATOM 1080 C CA . GLN A 1 139 ? 17.924 29.807 4.707 1.00 74.26 ? 138 GLN A CA 1 ATOM 1081 C C . GLN A 1 139 ? 18.947 30.940 4.542 1.00 76.32 ? 138 GLN A C 1 ATOM 1082 O O . GLN A 1 139 ? 18.584 32.114 4.445 1.00 78.64 ? 138 GLN A O 1 ATOM 1083 C CB . GLN A 1 139 ? 16.560 30.354 5.147 1.00 75.51 ? 138 GLN A CB 1 ATOM 1084 C CG . GLN A 1 139 ? 15.448 29.313 5.144 1.00 74.95 ? 138 GLN A CG 1 ATOM 1085 C CD . GLN A 1 139 ? 14.127 29.839 5.694 1.00 76.58 ? 138 GLN A CD 1 ATOM 1086 O OE1 . GLN A 1 139 ? 14.046 30.957 6.217 1.00 77.93 ? 138 GLN A OE1 1 ATOM 1087 N NE2 . GLN A 1 139 ? 13.081 29.021 5.590 1.00 76.03 ? 138 GLN A NE2 1 ATOM 1088 N N . GLY A 1 140 ? 20.227 30.572 4.514 1.00 75.77 ? 139 GLY A N 1 ATOM 1089 C CA . GLY A 1 140 ? 21.313 31.521 4.262 1.00 78.11 ? 139 GLY A CA 1 ATOM 1090 C C . GLY A 1 140 ? 21.718 32.401 5.434 1.00 77.97 ? 139 GLY A C 1 ATOM 1091 O O . GLY A 1 140 ? 22.428 33.395 5.245 1.00 80.01 ? 139 GLY A O 1 ATOM 1092 N N . ARG A 1 141 ? 21.280 32.049 6.642 1.00 75.39 ? 140 ARG A N 1 ATOM 1093 C CA . ARG A 1 141 ? 21.637 32.816 7.838 1.00 74.97 ? 140 ARG A CA 1 ATOM 1094 C C . ARG A 1 141 ? 21.955 31.899 9.020 1.00 69.50 ? 140 ARG A C 1 ATOM 1095 O O . ARG A 1 141 ? 21.508 30.750 9.063 1.00 67.75 ? 140 ARG A O 1 ATOM 1096 C CB . ARG A 1 141 ? 20.536 33.833 8.189 1.00 78.58 ? 140 ARG A CB 1 ATOM 1097 C CG . ARG A 1 141 ? 19.117 33.281 8.243 1.00 79.95 ? 140 ARG A CG 1 ATOM 1098 C CD . ARG A 1 141 ? 18.068 34.396 8.267 1.00 84.27 ? 140 ARG A CD 1 ATOM 1099 N NE . ARG A 1 141 ? 16.816 33.939 8.883 1.00 84.62 ? 140 ARG A NE 1 ATOM 1100 C CZ . ARG A 1 141 ? 15.841 33.270 8.259 1.00 85.23 ? 140 ARG A CZ 1 ATOM 1101 N NH1 . ARG A 1 141 ? 15.929 32.970 6.964 1.00 87.37 ? 140 ARG A NH1 1 ATOM 1102 N NH2 . ARG A 1 141 ? 14.757 32.903 8.939 1.00 83.65 ? 140 ARG A NH2 1 ATOM 1103 N N . SER A 1 142 ? 22.740 32.411 9.966 1.00 66.12 ? 141 SER A N 1 ATOM 1104 C CA . SER A 1 142 ? 23.219 31.610 11.089 1.00 61.00 ? 141 SER A CA 1 ATOM 1105 C C . SER A 1 142 ? 22.079 31.185 12.008 1.00 57.74 ? 141 SER A C 1 ATOM 1106 O O . SER A 1 142 ? 21.164 31.965 12.279 1.00 58.70 ? 141 SER A O 1 ATOM 1107 C CB . SER A 1 142 ? 24.280 32.369 11.890 1.00 61.05 ? 141 SER A CB 1 ATOM 1108 O OG . SER A 1 142 ? 25.526 32.352 11.222 1.00 61.93 ? 141 SER A OG 1 ATOM 1109 N N . SER A 1 143 ? 22.152 29.944 12.482 1.00 53.28 ? 142 SER A N 1 ATOM 1110 C CA . SER A 1 143 ? 21.112 29.371 13.328 1.00 50.44 ? 142 SER A CA 1 ATOM 1111 C C . SER A 1 143 ? 21.728 28.405 14.350 1.00 46.74 ? 142 SER A C 1 ATOM 1112 O O . SER A 1 143 ? 22.913 28.502 14.675 1.00 45.77 ? 142 SER A O 1 ATOM 1113 C CB . SER A 1 143 ? 20.068 28.666 12.450 1.00 50.49 ? 142 SER A CB 1 ATOM 1114 O OG . SER A 1 143 ? 18.917 28.307 13.187 1.00 48.91 ? 142 SER A OG 1 ATOM 1115 N N . PHE A 1 144 ? 20.920 27.479 14.850 1.00 44.34 ? 143 PHE A N 1 ATOM 1116 C CA . PHE A 1 144 ? 21.345 26.552 15.889 1.00 41.97 ? 143 PHE A CA 1 ATOM 1117 C C . PHE A 1 144 ? 20.271 25.500 16.088 1.00 40.33 ? 143 PHE A C 1 ATOM 1118 O O . PHE A 1 144 ? 19.176 25.606 15.536 1.00 41.64 ? 143 PHE A O 1 ATOM 1119 C CB . PHE A 1 144 ? 21.571 27.307 17.210 1.00 41.66 ? 143 PHE A CB 1 ATOM 1120 C CG . PHE A 1 144 ? 22.462 26.592 18.192 1.00 39.50 ? 143 PHE A CG 1 ATOM 1121 C CD1 . PHE A 1 144 ? 23.797 26.368 17.899 1.00 39.76 ? 143 PHE A CD1 1 ATOM 1122 C CD2 . PHE A 1 144 ? 21.969 26.177 19.428 1.00 37.82 ? 143 PHE A CD2 1 ATOM 1123 C CE1 . PHE A 1 144 ? 24.627 25.728 18.807 1.00 38.33 ? 143 PHE A CE1 1 ATOM 1124 C CE2 . PHE A 1 144 ? 22.793 25.540 20.342 1.00 36.50 ? 143 PHE A CE2 1 ATOM 1125 C CZ . PHE A 1 144 ? 24.125 25.316 20.031 1.00 36.77 ? 143 PHE A CZ 1 ATOM 1126 N N . PHE A 1 145 ? 20.608 24.484 16.873 1.00 38.02 ? 144 PHE A N 1 ATOM 1127 C CA . PHE A 1 145 ? 19.662 23.467 17.308 1.00 36.55 ? 144 PHE A CA 1 ATOM 1128 C C . PHE A 1 145 ? 18.404 24.111 17.903 1.00 36.90 ? 144 PHE A C 1 ATOM 1129 O O . PHE A 1 145 ? 18.488 25.093 18.640 1.00 37.29 ? 144 PHE A O 1 ATOM 1130 C CB . PHE A 1 145 ? 20.318 22.543 18.344 1.00 34.24 ? 144 PHE A CB 1 ATOM 1131 C CG . PHE A 1 145 ? 21.578 21.879 17.856 1.00 34.00 ? 144 PHE A CG 1 ATOM 1132 C CD1 . PHE A 1 145 ? 21.516 20.789 16.990 1.00 33.69 ? 144 PHE A CD1 1 ATOM 1133 C CD2 . PHE A 1 145 ? 22.828 22.340 18.259 1.00 33.78 ? 144 PHE A CD2 1 ATOM 1134 C CE1 . PHE A 1 145 ? 22.674 20.171 16.537 1.00 33.61 ? 144 PHE A CE1 1 ATOM 1135 C CE2 . PHE A 1 145 ? 23.987 21.725 17.806 1.00 34.05 ? 144 PHE A CE2 1 ATOM 1136 C CZ . PHE A 1 145 ? 23.912 20.636 16.948 1.00 33.74 ? 144 PHE A CZ 1 ATOM 1137 N N . ARG A 1 146 ? 17.246 23.548 17.577 1.00 36.81 ? 145 ARG A N 1 ATOM 1138 C CA . ARG A 1 146 ? 15.958 24.156 17.924 1.00 37.63 ? 145 ARG A CA 1 ATOM 1139 C C . ARG A 1 146 ? 15.562 23.812 19.352 1.00 36.01 ? 145 ARG A C 1 ATOM 1140 O O . ARG A 1 146 ? 15.044 24.645 20.080 1.00 37.37 ? 145 ARG A O 1 ATOM 1141 C CB . ARG A 1 146 ? 14.861 23.641 16.995 1.00 38.41 ? 145 ARG A CB 1 ATOM 1142 C CG . ARG A 1 146 ? 15.170 23.709 15.512 1.00 40.07 ? 145 ARG A CG 1 ATOM 1143 C CD . ARG A 1 146 ? 15.097 25.120 14.981 1.00 42.55 ? 145 ARG A CD 1 ATOM 1144 N NE . ARG A 1 146 ? 15.124 25.157 13.521 1.00 44.45 ? 145 ARG A NE 1 ATOM 1145 C CZ . ARG A 1 146 ? 15.198 26.277 12.804 1.00 47.31 ? 145 ARG A CZ 1 ATOM 1146 N NH1 . ARG A 1 146 ? 15.255 27.460 13.414 1.00 48.49 ? 145 ARG A NH1 1 ATOM 1147 N NH2 . ARG A 1 146 ? 15.222 26.222 11.473 1.00 49.03 ? 145 ARG A NH2 1 ATOM 1148 N N . ASN A 1 147 ? 15.831 22.574 19.743 1.00 33.81 ? 146 ASN A N 1 ATOM 1149 C CA . ASN A 1 147 ? 15.329 22.021 20.985 1.00 32.55 ? 146 ASN A CA 1 ATOM 1150 C C . ASN A 1 147 ? 16.162 22.372 22.213 1.00 31.92 ? 146 ASN A C 1 ATOM 1151 O O . ASN A 1 147 ? 15.727 22.136 23.347 1.00 31.73 ? 146 ASN A O 1 ATOM 1152 C CB . ASN A 1 147 ? 15.193 20.501 20.840 1.00 31.00 ? 146 ASN A CB 1 ATOM 1153 C CG . ASN A 1 147 ? 14.263 20.122 19.703 1.00 31.55 ? 146 ASN A CG 1 ATOM 1154 O OD1 . ASN A 1 147 ? 13.235 20.768 19.506 1.00 32.26 ? 146 ASN A OD1 1 ATOM 1155 N ND2 . ASN A 1 147 ? 14.615 19.076 18.951 1.00 30.71 ? 146 ASN A ND2 1 ATOM 1156 N N . VAL A 1 148 ? 17.345 22.942 21.992 1.00 31.72 ? 147 VAL A N 1 ATOM 1157 C CA . VAL A 1 148 ? 18.184 23.433 23.084 1.00 31.09 ? 147 VAL A CA 1 ATOM 1158 C C . VAL A 1 148 ? 18.564 24.876 22.797 1.00 33.00 ? 147 VAL A C 1 ATOM 1159 O O . VAL A 1 148 ? 18.399 25.343 21.681 1.00 34.16 ? 147 VAL A O 1 ATOM 1160 C CB . VAL A 1 148 ? 19.454 22.575 23.268 1.00 29.75 ? 147 VAL A CB 1 ATOM 1161 C CG1 . VAL A 1 148 ? 19.089 21.203 23.825 1.00 28.08 ? 147 VAL A CG1 1 ATOM 1162 C CG2 . VAL A 1 148 ? 20.256 22.461 21.959 1.00 29.84 ? 147 VAL A CG2 1 ATOM 1163 N N . VAL A 1 149 ? 19.076 25.571 23.811 1.00 33.80 ? 148 VAL A N 1 ATOM 1164 C CA . VAL A 1 149 ? 19.340 27.006 23.734 1.00 35.23 ? 148 VAL A CA 1 ATOM 1165 C C . VAL A 1 149 ? 20.741 27.356 24.229 1.00 35.23 ? 148 VAL A C 1 ATOM 1166 O O . VAL A 1 149 ? 21.109 27.047 25.368 1.00 33.99 ? 148 VAL A O 1 ATOM 1167 C CB . VAL A 1 149 ? 18.320 27.781 24.565 1.00 36.39 ? 148 VAL A CB 1 ATOM 1168 C CG1 . VAL A 1 149 ? 18.653 29.267 24.609 1.00 38.10 ? 148 VAL A CG1 1 ATOM 1169 C CG2 . VAL A 1 149 ? 16.933 27.561 23.985 1.00 37.59 ? 148 VAL A CG2 1 ATOM 1170 N N . TRP A 1 150 ? 21.498 28.029 23.364 1.00 35.99 ? 149 TRP A N 1 ATOM 1171 C CA . TRP A 1 150 ? 22.858 28.445 23.658 1.00 36.13 ? 149 TRP A CA 1 ATOM 1172 C C . TRP A 1 150 ? 22.844 29.860 24.239 1.00 37.38 ? 149 TRP A C 1 ATOM 1173 O O . TRP A 1 150 ? 22.877 30.843 23.507 1.00 38.61 ? 149 TRP A O 1 ATOM 1174 C CB . TRP A 1 150 ? 23.692 28.364 22.372 1.00 37.06 ? 149 TRP A CB 1 ATOM 1175 C CG . TRP A 1 150 ? 25.115 28.811 22.463 1.00 37.18 ? 149 TRP A CG 1 ATOM 1176 C CD1 . TRP A 1 150 ? 25.836 29.083 23.591 1.00 36.82 ? 149 TRP A CD1 1 ATOM 1177 C CD2 . TRP A 1 150 ? 26.009 28.985 21.365 1.00 38.48 ? 149 TRP A CD2 1 ATOM 1178 N NE1 . TRP A 1 150 ? 27.123 29.440 23.256 1.00 37.66 ? 149 TRP A NE1 1 ATOM 1179 C CE2 . TRP A 1 150 ? 27.255 29.382 21.895 1.00 38.73 ? 149 TRP A CE2 1 ATOM 1180 C CE3 . TRP A 1 150 ? 25.878 28.842 19.977 1.00 39.51 ? 149 TRP A CE3 1 ATOM 1181 C CZ2 . TRP A 1 150 ? 28.361 29.640 21.085 1.00 40.11 ? 149 TRP A CZ2 1 ATOM 1182 C CZ3 . TRP A 1 150 ? 26.973 29.106 19.177 1.00 40.81 ? 149 TRP A CZ3 1 ATOM 1183 C CH2 . TRP A 1 150 ? 28.201 29.503 19.734 1.00 41.15 ? 149 TRP A CH2 1 ATOM 1184 N N . LEU A 1 151 ? 22.817 29.932 25.568 1.00 36.56 ? 150 LEU A N 1 ATOM 1185 C CA . LEU A 1 151 ? 22.755 31.196 26.290 1.00 37.97 ? 150 LEU A CA 1 ATOM 1186 C C . LEU A 1 151 ? 24.104 31.896 26.320 1.00 38.61 ? 150 LEU A C 1 ATOM 1187 O O . LEU A 1 151 ? 25.135 31.249 26.393 1.00 37.70 ? 150 LEU A O 1 ATOM 1188 C CB . LEU A 1 151 ? 22.306 30.957 27.735 1.00 37.14 ? 150 LEU A CB 1 ATOM 1189 C CG . LEU A 1 151 ? 20.951 30.270 27.913 1.00 36.50 ? 150 LEU A CG 1 ATOM 1190 C CD1 . LEU A 1 151 ? 20.756 29.811 29.346 1.00 35.27 ? 150 LEU A CD1 1 ATOM 1191 C CD2 . LEU A 1 151 ? 19.823 31.187 27.479 1.00 38.44 ? 150 LEU A CD2 1 ATOM 1192 N N . ILE A 1 152 ? 24.090 33.223 26.272 1.00 40.64 ? 151 ILE A N 1 ATOM 1193 C CA . ILE A 1 152 ? 25.309 33.998 26.450 1.00 41.80 ? 151 ILE A CA 1 ATOM 1194 C C . ILE A 1 152 ? 25.072 35.128 27.445 1.00 43.11 ? 151 ILE A C 1 ATOM 1195 O O . ILE A 1 152 ? 23.957 35.320 27.931 1.00 43.62 ? 151 ILE A O 1 ATOM 1196 C CB . ILE A 1 152 ? 25.834 34.539 25.111 1.00 43.87 ? 151 ILE A CB 1 ATOM 1197 C CG1 . ILE A 1 152 ? 24.867 35.567 24.516 1.00 46.23 ? 151 ILE A CG1 1 ATOM 1198 C CG2 . ILE A 1 152 ? 26.063 33.395 24.136 1.00 42.81 ? 151 ILE A CG2 1 ATOM 1199 C CD1 . ILE A 1 152 ? 25.361 36.176 23.224 1.00 48.42 ? 151 ILE A CD1 1 ATOM 1200 N N . LYS A 1 153 ? 26.124 35.873 27.750 1.00 44.14 ? 152 LYS A N 1 ATOM 1201 C CA . LYS A 1 153 ? 26.025 36.959 28.712 1.00 45.35 ? 152 LYS A CA 1 ATOM 1202 C C . LYS A 1 153 ? 25.106 38.080 28.228 1.00 47.89 ? 152 LYS A C 1 ATOM 1203 O O . LYS A 1 153 ? 24.922 38.282 27.027 1.00 48.99 ? 152 LYS A O 1 ATOM 1204 C CB . LYS A 1 153 ? 27.411 37.515 29.023 1.00 46.02 ? 152 LYS A CB 1 ATOM 1205 C CG . LYS A 1 153 ? 27.981 38.424 27.951 1.00 48.27 ? 152 LYS A CG 1 ATOM 1206 C CD . LYS A 1 153 ? 29.484 38.555 28.106 1.00 48.63 ? 152 LYS A CD 1 ATOM 1207 C CE . LYS A 1 153 ? 30.042 39.709 27.292 1.00 50.99 ? 152 LYS A CE 1 ATOM 1208 N NZ . LYS A 1 153 ? 31.501 39.850 27.541 1.00 51.41 ? 152 LYS A NZ 1 ATOM 1209 N N . LYS A 1 154 ? 24.540 38.807 29.185 1.00 49.20 ? 153 LYS A N 1 ATOM 1210 C CA . LYS A 1 154 ? 23.674 39.939 28.905 1.00 51.83 ? 153 LYS A CA 1 ATOM 1211 C C . LYS A 1 154 ? 24.184 41.134 29.699 1.00 53.95 ? 153 LYS A C 1 ATOM 1212 O O . LYS A 1 154 ? 24.396 41.032 30.902 1.00 52.95 ? 153 LYS A O 1 ATOM 1213 C CB . LYS A 1 154 ? 22.241 39.607 29.312 1.00 51.48 ? 153 LYS A CB 1 ATOM 1214 C CG . LYS A 1 154 ? 21.231 40.692 28.985 1.00 54.46 ? 153 LYS A CG 1 ATOM 1215 C CD . LYS A 1 154 ? 19.865 40.354 29.547 1.00 54.16 ? 153 LYS A CD 1 ATOM 1216 C CE . LYS A 1 154 ? 18.850 41.420 29.173 1.00 57.10 ? 153 LYS A CE 1 ATOM 1217 N NZ . LYS A 1 154 ? 17.490 41.068 29.669 1.00 57.18 ? 153 LYS A NZ 1 ATOM 1218 N N . ASP A 1 155 ? 24.384 42.262 29.025 1.00 57.23 ? 154 ASP A N 1 ATOM 1219 C CA . ASP A 1 155 ? 24.905 43.469 29.667 1.00 59.71 ? 154 ASP A CA 1 ATOM 1220 C C . ASP A 1 155 ? 26.227 43.201 30.415 1.00 57.94 ? 154 ASP A C 1 ATOM 1221 O O . ASP A 1 155 ? 26.396 43.599 31.570 1.00 57.73 ? 154 ASP A O 1 ATOM 1222 C CB . ASP A 1 155 ? 23.846 44.070 30.608 1.00 61.79 ? 154 ASP A CB 1 ATOM 1223 C CG . ASP A 1 155 ? 22.587 44.538 29.871 1.00 64.94 ? 154 ASP A CG 1 ATOM 1224 O OD1 . ASP A 1 155 ? 22.596 44.625 28.617 1.00 66.77 ? 154 ASP A OD1 1 ATOM 1225 O OD2 . ASP A 1 155 ? 21.580 44.837 30.556 1.00 66.43 ? 154 ASP A OD2 1 ATOM 1226 N N . ASN A 1 156 ? 27.157 42.529 29.738 1.00 56.48 ? 155 ASN A N 1 ATOM 1227 C CA . ASN A 1 156 ? 28.441 42.109 30.331 1.00 55.38 ? 155 ASN A CA 1 ATOM 1228 C C . ASN A 1 156 ? 28.313 41.356 31.656 1.00 52.88 ? 155 ASN A C 1 ATOM 1229 O O . ASN A 1 156 ? 29.197 41.429 32.519 1.00 52.53 ? 155 ASN A O 1 ATOM 1230 C CB . ASN A 1 156 ? 29.387 43.310 30.497 1.00 57.94 ? 155 ASN A CB 1 ATOM 1231 C CG . ASN A 1 156 ? 30.063 43.695 29.202 1.00 59.91 ? 155 ASN A CG 1 ATOM 1232 O OD1 . ASN A 1 156 ? 30.535 42.833 28.452 1.00 58.74 ? 155 ASN A OD1 1 ATOM 1233 N ND2 . ASN A 1 156 ? 30.118 44.996 28.927 1.00 62.76 ? 155 ASN A ND2 1 ATOM 1234 N N . ALA A 1 157 ? 27.216 40.626 31.810 1.00 51.11 ? 156 ALA A N 1 ATOM 1235 C CA . ALA A 1 157 ? 26.983 39.852 33.018 1.00 49.23 ? 156 ALA A CA 1 ATOM 1236 C C . ALA A 1 157 ? 26.278 38.546 32.678 1.00 46.76 ? 156 ALA A C 1 ATOM 1237 O O . ALA A 1 157 ? 25.439 38.503 31.779 1.00 46.09 ? 156 ALA A O 1 ATOM 1238 C CB . ALA A 1 157 ? 26.166 40.661 34.012 1.00 50.50 ? 156 ALA A CB 1 ATOM 1239 N N . TYR A 1 158 ? 26.654 37.487 33.396 1.00 45.47 ? 157 TYR A N 1 ATOM 1240 C CA . TYR A 1 158 ? 26.021 36.169 33.290 1.00 43.56 ? 157 TYR A CA 1 ATOM 1241 C C . TYR A 1 158 ? 25.818 35.688 34.719 1.00 43.16 ? 157 TYR A C 1 ATOM 1242 O O . TYR A 1 158 ? 26.702 35.063 35.302 1.00 42.26 ? 157 TYR A O 1 ATOM 1243 C CB . TYR A 1 158 ? 26.909 35.199 32.502 1.00 42.04 ? 157 TYR A CB 1 ATOM 1244 C CG . TYR A 1 158 ? 26.280 33.859 32.092 1.00 39.54 ? 157 TYR A CG 1 ATOM 1245 C CD1 . TYR A 1 158 ? 25.806 32.952 33.036 1.00 38.24 ? 157 TYR A CD1 1 ATOM 1246 C CD2 . TYR A 1 158 ? 26.197 33.495 30.749 1.00 39.34 ? 157 TYR A CD2 1 ATOM 1247 C CE1 . TYR A 1 158 ? 25.260 31.723 32.659 1.00 36.49 ? 157 TYR A CE1 1 ATOM 1248 C CE2 . TYR A 1 158 ? 25.660 32.271 30.360 1.00 37.82 ? 157 TYR A CE2 1 ATOM 1249 C CZ . TYR A 1 158 ? 25.190 31.385 31.320 1.00 36.22 ? 157 TYR A CZ 1 ATOM 1250 O OH . TYR A 1 158 ? 24.644 30.181 30.927 1.00 34.29 ? 157 TYR A OH 1 ATOM 1251 N N . PRO A 1 159 ? 24.658 36.015 35.308 1.00 44.16 ? 158 PRO A N 1 ATOM 1252 C CA . PRO A 1 159 ? 24.362 35.562 36.663 1.00 43.61 ? 158 PRO A CA 1 ATOM 1253 C C . PRO A 1 159 ? 24.306 34.043 36.772 1.00 41.70 ? 158 PRO A C 1 ATOM 1254 O O . PRO A 1 159 ? 24.079 33.350 35.774 1.00 41.09 ? 158 PRO A O 1 ATOM 1255 C CB . PRO A 1 159 ? 22.984 36.168 36.938 1.00 44.87 ? 158 PRO A CB 1 ATOM 1256 C CG . PRO A 1 159 ? 22.924 37.368 36.061 1.00 46.77 ? 158 PRO A CG 1 ATOM 1257 C CD . PRO A 1 159 ? 23.640 36.953 34.808 1.00 45.67 ? 158 PRO A CD 1 ATOM 1258 N N . THR A 1 160 ? 24.524 33.532 37.975 1.00 41.22 ? 159 THR A N 1 ATOM 1259 C CA . THR A 1 160 ? 24.417 32.104 38.216 1.00 39.89 ? 159 THR A CA 1 ATOM 1260 C C . THR A 1 160 ? 22.997 31.674 37.918 1.00 39.26 ? 159 THR A C 1 ATOM 1261 O O . THR A 1 160 ? 22.051 32.257 38.424 1.00 40.60 ? 159 THR A O 1 ATOM 1262 C CB . THR A 1 160 ? 24.755 31.754 39.669 1.00 40.29 ? 159 THR A CB 1 ATOM 1263 O OG1 . THR A 1 160 ? 25.998 32.366 40.011 1.00 40.99 ? 159 THR A OG1 1 ATOM 1264 C CG2 . THR A 1 160 ? 24.864 30.238 39.846 1.00 38.91 ? 159 THR A CG2 1 ATOM 1265 N N . ILE A 1 161 ? 22.849 30.674 37.069 1.00 38.19 ? 160 ILE A N 1 ATOM 1266 C CA . ILE A 1 161 ? 21.534 30.210 36.702 1.00 38.62 ? 160 ILE A CA 1 ATOM 1267 C C . ILE A 1 161 ? 21.121 29.151 37.697 1.00 38.84 ? 160 ILE A C 1 ATOM 1268 O O . ILE A 1 161 ? 21.947 28.339 38.112 1.00 37.16 ? 160 ILE A O 1 ATOM 1269 C CB . ILE A 1 161 ? 21.517 29.653 35.269 1.00 37.95 ? 160 ILE A CB 1 ATOM 1270 C CG1 . ILE A 1 161 ? 21.639 30.810 34.282 1.00 39.34 ? 160 ILE A CG1 1 ATOM 1271 C CG2 . ILE A 1 161 ? 20.239 28.867 35.004 1.00 37.27 ? 160 ILE A CG2 1 ATOM 1272 C CD1 . ILE A 1 161 ? 21.919 30.380 32.866 1.00 39.50 ? 160 ILE A CD1 1 ATOM 1273 N N . LYS A 1 162 ? 19.853 29.203 38.102 1.00 40.32 ? 161 LYS A N 1 ATOM 1274 C CA . LYS A 1 162 ? 19.222 28.128 38.860 1.00 40.25 ? 161 LYS A CA 1 ATOM 1275 C C . LYS A 1 162 ? 17.839 27.857 38.289 1.00 40.58 ? 161 LYS A C 1 ATOM 1276 O O . LYS A 1 162 ? 16.916 28.618 38.535 1.00 44.01 ? 161 LYS A O 1 ATOM 1277 C CB . LYS A 1 162 ? 19.123 28.490 40.341 1.00 40.83 ? 161 LYS A CB 1 ATOM 1278 C CG . LYS A 1 162 ? 20.483 28.571 41.002 1.00 41.12 ? 161 LYS A CG 1 ATOM 1279 C CD . LYS A 1 162 ? 20.415 28.869 42.489 1.00 42.20 ? 161 LYS A CD 1 ATOM 1280 C CE . LYS A 1 162 ? 21.820 29.109 43.029 1.00 42.48 ? 161 LYS A CE 1 ATOM 1281 N NZ . LYS A 1 162 ? 21.885 29.198 44.514 1.00 43.84 ? 161 LYS A NZ 1 ATOM 1282 N N . ARG A 1 163 ? 17.700 26.789 37.514 1.00 39.24 ? 162 ARG A N 1 ATOM 1283 C CA . ARG A 1 163 ? 16.402 26.418 36.967 1.00 40.11 ? 162 ARG A CA 1 ATOM 1284 C C . ARG A 1 163 ? 16.106 24.973 37.265 1.00 37.70 ? 162 ARG A C 1 ATOM 1285 O O . ARG A 1 163 ? 16.917 24.100 37.004 1.00 36.74 ? 162 ARG A O 1 ATOM 1286 C CB . ARG A 1 163 ? 16.344 26.620 35.451 1.00 40.98 ? 162 ARG A CB 1 ATOM 1287 C CG . ARG A 1 163 ? 16.485 28.055 34.981 1.00 44.13 ? 162 ARG A CG 1 ATOM 1288 C CD . ARG A 1 163 ? 15.473 28.997 35.622 1.00 47.87 ? 162 ARG A CD 1 ATOM 1289 N NE . ARG A 1 163 ? 15.008 29.980 34.652 1.00 51.05 ? 162 ARG A NE 1 ATOM 1290 C CZ . ARG A 1 163 ? 14.110 29.732 33.698 1.00 51.81 ? 162 ARG A CZ 1 ATOM 1291 N NH1 . ARG A 1 163 ? 13.549 28.532 33.579 1.00 50.93 ? 162 ARG A NH1 1 ATOM 1292 N NH2 . ARG A 1 163 ? 13.767 30.696 32.858 1.00 53.76 ? 162 ARG A NH2 1 ATOM 1293 N N . SER A 1 164 ? 14.927 24.735 37.811 1.00 37.98 ? 163 SER A N 1 ATOM 1294 C CA . SER A 1 164 ? 14.416 23.396 38.000 1.00 37.29 ? 163 SER A CA 1 ATOM 1295 C C . SER A 1 164 ? 13.266 23.183 37.026 1.00 37.14 ? 163 SER A C 1 ATOM 1296 O O . SER A 1 164 ? 12.535 24.120 36.694 1.00 38.24 ? 163 SER A O 1 ATOM 1297 C CB . SER A 1 164 ? 13.931 23.210 39.435 1.00 37.93 ? 163 SER A CB 1 ATOM 1298 O OG . SER A 1 164 ? 15.015 23.301 40.343 1.00 37.47 ? 163 SER A OG 1 ATOM 1299 N N . TYR A 1 165 ? 13.134 21.956 36.542 1.00 35.17 ? 164 TYR A N 1 ATOM 1300 C CA . TYR A 1 165 ? 11.911 21.536 35.882 1.00 35.36 ? 164 TYR A CA 1 ATOM 1301 C C . TYR A 1 165 ? 11.411 20.234 36.497 1.00 35.38 ? 164 TYR A C 1 ATOM 1302 O O . TYR A 1 165 ? 12.162 19.269 36.629 1.00 34.01 ? 164 TYR A O 1 ATOM 1303 C CB . TYR A 1 165 ? 12.113 21.362 34.382 1.00 33.70 ? 164 TYR A CB 1 ATOM 1304 C CG . TYR A 1 165 ? 10.942 20.683 33.744 1.00 33.74 ? 164 TYR A CG 1 ATOM 1305 C CD1 . TYR A 1 165 ? 9.814 21.403 33.350 1.00 35.39 ? 164 TYR A CD1 1 ATOM 1306 C CD2 . TYR A 1 165 ? 10.940 19.311 33.568 1.00 32.60 ? 164 TYR A CD2 1 ATOM 1307 C CE1 . TYR A 1 165 ? 8.722 20.763 32.769 1.00 35.94 ? 164 TYR A CE1 1 ATOM 1308 C CE2 . TYR A 1 165 ? 9.863 18.667 32.996 1.00 33.09 ? 164 TYR A CE2 1 ATOM 1309 C CZ . TYR A 1 165 ? 8.756 19.388 32.601 1.00 34.79 ? 164 TYR A CZ 1 ATOM 1310 O OH . TYR A 1 165 ? 7.700 18.710 32.040 1.00 35.48 ? 164 TYR A OH 1 ATOM 1311 N N . ASN A 1 166 ? 10.130 20.218 36.845 1.00 37.20 ? 165 ASN A N 1 ATOM 1312 C CA . ASN A 1 166 ? 9.490 19.061 37.458 1.00 38.15 ? 165 ASN A CA 1 ATOM 1313 C C . ASN A 1 166 ? 8.655 18.326 36.408 1.00 37.05 ? 165 ASN A C 1 ATOM 1314 O O . ASN A 1 166 ? 7.754 18.914 35.810 1.00 38.10 ? 165 ASN A O 1 ATOM 1315 C CB . ASN A 1 166 ? 8.622 19.559 38.610 1.00 41.64 ? 165 ASN A CB 1 ATOM 1316 C CG . ASN A 1 166 ? 8.007 18.445 39.431 1.00 44.42 ? 165 ASN A CG 1 ATOM 1317 O OD1 . ASN A 1 166 ? 7.477 17.469 38.904 1.00 44.98 ? 165 ASN A OD1 1 ATOM 1318 N ND2 . ASN A 1 166 ? 8.060 18.599 40.743 1.00 48.22 ? 165 ASN A ND2 1 ATOM 1319 N N . ASN A 1 167 ? 8.959 17.052 36.167 1.00 34.94 ? 166 ASN A N 1 ATOM 1320 C CA . ASN A 1 167 ? 8.145 16.252 35.256 1.00 34.32 ? 166 ASN A CA 1 ATOM 1321 C C . ASN A 1 167 ? 6.815 15.881 35.903 1.00 36.10 ? 166 ASN A C 1 ATOM 1322 O O . ASN A 1 167 ? 6.696 14.842 36.534 1.00 36.54 ? 166 ASN A O 1 ATOM 1323 C CB . ASN A 1 167 ? 8.876 14.979 34.795 1.00 31.94 ? 166 ASN A CB 1 ATOM 1324 C CG . ASN A 1 167 ? 8.098 14.218 33.728 1.00 31.21 ? 166 ASN A CG 1 ATOM 1325 O OD1 . ASN A 1 167 ? 7.198 14.772 33.106 1.00 32.00 ? 166 ASN A OD1 1 ATOM 1326 N ND2 . ASN A 1 167 ? 8.432 12.944 33.525 1.00 29.81 ? 166 ASN A ND2 1 ATOM 1327 N N . THR A 1 168 ? 5.817 16.733 35.723 1.00 38.09 ? 167 THR A N 1 ATOM 1328 C CA . THR A 1 168 ? 4.474 16.476 36.241 1.00 41.09 ? 167 THR A CA 1 ATOM 1329 C C . THR A 1 168 ? 3.656 15.517 35.377 1.00 41.54 ? 167 THR A C 1 ATOM 1330 O O . THR A 1 168 ? 2.557 15.147 35.766 1.00 44.04 ? 167 THR A O 1 ATOM 1331 C CB . THR A 1 168 ? 3.671 17.785 36.368 1.00 43.32 ? 167 THR A CB 1 ATOM 1332 O OG1 . THR A 1 168 ? 3.885 18.577 35.192 1.00 43.70 ? 167 THR A OG1 1 ATOM 1333 C CG2 . THR A 1 168 ? 4.104 18.568 37.592 1.00 43.71 ? 167 THR A CG2 1 ATOM 1334 N N . ASN A 1 169 ? 4.189 15.125 34.220 1.00 40.47 ? 168 ASN A N 1 ATOM 1335 C CA . ASN A 1 169 ? 3.514 14.206 33.299 1.00 40.59 ? 168 ASN A CA 1 ATOM 1336 C C . ASN A 1 169 ? 3.686 12.751 33.719 1.00 40.26 ? 168 ASN A C 1 ATOM 1337 O O . ASN A 1 169 ? 4.581 12.417 34.492 1.00 40.12 ? 168 ASN A O 1 ATOM 1338 C CB . ASN A 1 169 ? 4.082 14.343 31.881 1.00 39.36 ? 168 ASN A CB 1 ATOM 1339 C CG . ASN A 1 169 ? 4.174 15.785 31.411 1.00 39.72 ? 168 ASN A CG 1 ATOM 1340 O OD1 . ASN A 1 169 ? 3.196 16.350 30.925 1.00 40.82 ? 168 ASN A OD1 1 ATOM 1341 N ND2 . ASN A 1 169 ? 5.364 16.379 31.529 1.00 38.51 ? 168 ASN A ND2 1 ATOM 1342 N N . GLN A 1 170 ? 2.852 11.885 33.162 1.00 40.78 ? 169 GLN A N 1 ATOM 1343 C CA . GLN A 1 170 ? 2.896 10.450 33.449 1.00 40.14 ? 169 GLN A CA 1 ATOM 1344 C C . GLN A 1 170 ? 3.949 9.731 32.644 1.00 37.83 ? 169 GLN A C 1 ATOM 1345 O O . GLN A 1 170 ? 4.315 8.594 32.968 1.00 37.41 ? 169 GLN A O 1 ATOM 1346 C CB . GLN A 1 170 ? 1.544 9.810 33.134 1.00 42.06 ? 169 GLN A CB 1 ATOM 1347 C CG . GLN A 1 170 ? 0.440 10.221 34.077 1.00 44.53 ? 169 GLN A CG 1 ATOM 1348 C CD . GLN A 1 170 ? 0.772 9.932 35.528 1.00 45.25 ? 169 GLN A CD 1 ATOM 1349 O OE1 . GLN A 1 170 ? 0.529 10.769 36.397 1.00 47.30 ? 169 GLN A OE1 1 ATOM 1350 N NE2 . GLN A 1 170 ? 1.339 8.751 35.799 1.00 44.04 ? 169 GLN A NE2 1 ATOM 1351 N N . GLU A 1 171 ? 4.399 10.371 31.567 1.00 36.66 ? 170 GLU A N 1 ATOM 1352 C CA . GLU A 1 171 ? 5.414 9.801 30.692 1.00 34.51 ? 170 GLU A CA 1 ATOM 1353 C C . GLU A 1 171 ? 6.800 10.064 31.254 1.00 32.61 ? 170 GLU A C 1 ATOM 1354 O O . GLU A 1 171 ? 7.029 11.111 31.858 1.00 33.03 ? 170 GLU A O 1 ATOM 1355 C CB . GLU A 1 171 ? 5.335 10.437 29.309 1.00 34.81 ? 170 GLU A CB 1 ATOM 1356 C CG . GLU A 1 171 ? 4.099 10.083 28.505 1.00 36.83 ? 170 GLU A CG 1 ATOM 1357 C CD . GLU A 1 171 ? 2.902 10.967 28.807 1.00 39.15 ? 170 GLU A CD 1 ATOM 1358 O OE1 . GLU A 1 171 ? 3.060 12.074 29.375 1.00 39.44 ? 170 GLU A OE1 1 ATOM 1359 O OE2 . GLU A 1 171 ? 1.788 10.541 28.463 1.00 41.11 ? 170 GLU A OE2 1 ATOM 1360 N N . ASP A 1 172 ? 7.712 9.113 31.057 1.00 31.24 ? 171 ASP A N 1 ATOM 1361 C CA . ASP A 1 172 ? 9.150 9.375 31.182 1.00 29.54 ? 171 ASP A CA 1 ATOM 1362 C C . ASP A 1 172 ? 9.492 10.461 30.168 1.00 28.27 ? 171 ASP A C 1 ATOM 1363 O O . ASP A 1 172 ? 8.928 10.502 29.066 1.00 27.55 ? 171 ASP A O 1 ATOM 1364 C CB . ASP A 1 172 ? 10.007 8.148 30.830 1.00 29.06 ? 171 ASP A CB 1 ATOM 1365 C CG . ASP A 1 172 ? 9.834 6.988 31.784 1.00 30.23 ? 171 ASP A CG 1 ATOM 1366 O OD1 . ASP A 1 172 ? 9.483 7.196 32.960 1.00 32.30 ? 171 ASP A OD1 1 ATOM 1367 O OD2 . ASP A 1 172 ? 10.087 5.846 31.356 1.00 31.10 ? 171 ASP A OD2 1 ATOM 1368 N N . LEU A 1 173 ? 10.437 11.314 30.536 1.00 27.10 ? 172 LEU A N 1 ATOM 1369 C CA . LEU A 1 173 ? 10.789 12.468 29.728 1.00 26.74 ? 172 LEU A CA 1 ATOM 1370 C C . LEU A 1 173 ? 12.255 12.354 29.327 1.00 24.78 ? 172 LEU A C 1 ATOM 1371 O O . LEU A 1 173 ? 13.102 12.241 30.193 1.00 23.65 ? 172 LEU A O 1 ATOM 1372 C CB . LEU A 1 173 ? 10.546 13.731 30.565 1.00 27.77 ? 172 LEU A CB 1 ATOM 1373 C CG . LEU A 1 173 ? 10.681 15.103 29.910 1.00 28.22 ? 172 LEU A CG 1 ATOM 1374 C CD1 . LEU A 1 173 ? 9.735 15.247 28.734 1.00 29.32 ? 172 LEU A CD1 1 ATOM 1375 C CD2 . LEU A 1 173 ? 10.389 16.183 30.933 1.00 29.31 ? 172 LEU A CD2 1 ATOM 1376 N N . LEU A 1 174 ? 12.552 12.347 28.024 1.00 24.32 ? 173 LEU A N 1 ATOM 1377 C CA . LEU A 1 174 ? 13.948 12.386 27.550 1.00 23.03 ? 173 LEU A CA 1 ATOM 1378 C C . LEU A 1 174 ? 14.415 13.846 27.510 1.00 23.12 ? 173 LEU A C 1 ATOM 1379 O O . LEU A 1 174 ? 13.907 14.644 26.733 1.00 23.13 ? 173 LEU A O 1 ATOM 1380 C CB . LEU A 1 174 ? 14.076 11.749 26.173 1.00 23.25 ? 173 LEU A CB 1 ATOM 1381 C CG . LEU A 1 174 ? 15.377 11.876 25.378 1.00 23.34 ? 173 LEU A CG 1 ATOM 1382 C CD1 . LEU A 1 174 ? 16.559 11.288 26.144 1.00 22.86 ? 173 LEU A CD1 1 ATOM 1383 C CD2 . LEU A 1 174 ? 15.238 11.185 24.037 1.00 23.82 ? 173 LEU A CD2 1 ATOM 1384 N N . VAL A 1 175 ? 15.372 14.191 28.366 1.00 22.78 ? 174 VAL A N 1 ATOM 1385 C CA . VAL A 1 175 ? 15.851 15.566 28.464 1.00 23.06 ? 174 VAL A CA 1 ATOM 1386 C C . VAL A 1 175 ? 17.245 15.647 27.882 1.00 22.57 ? 174 VAL A C 1 ATOM 1387 O O . VAL A 1 175 ? 18.024 14.716 28.020 1.00 23.21 ? 174 VAL A O 1 ATOM 1388 C CB . VAL A 1 175 ? 15.848 16.068 29.916 1.00 23.04 ? 174 VAL A CB 1 ATOM 1389 C CG1 . VAL A 1 175 ? 16.283 17.536 29.980 1.00 23.38 ? 174 VAL A CG1 1 ATOM 1390 C CG2 . VAL A 1 175 ? 14.461 15.889 30.509 1.00 24.02 ? 174 VAL A CG2 1 ATOM 1391 N N . LEU A 1 176 ? 17.528 16.754 27.213 1.00 22.67 ? 175 LEU A N 1 ATOM 1392 C CA . LEU A 1 176 ? 18.786 16.968 26.529 1.00 23.03 ? 175 LEU A CA 1 ATOM 1393 C C . LEU A 1 176 ? 19.340 18.352 26.848 1.00 23.24 ? 175 LEU A C 1 ATOM 1394 O O . LEU A 1 176 ? 18.620 19.348 26.783 1.00 22.65 ? 175 LEU A O 1 ATOM 1395 C CB . LEU A 1 176 ? 18.600 16.879 25.019 1.00 24.18 ? 175 LEU A CB 1 ATOM 1396 C CG . LEU A 1 176 ? 17.910 15.650 24.437 1.00 24.43 ? 175 LEU A CG 1 ATOM 1397 C CD1 . LEU A 1 176 ? 17.890 15.775 22.933 1.00 25.85 ? 175 LEU A CD1 1 ATOM 1398 C CD2 . LEU A 1 176 ? 18.630 14.388 24.817 1.00 24.18 ? 175 LEU A CD2 1 ATOM 1399 N N . TRP A 1 177 ? 20.625 18.388 27.197 1.00 23.48 ? 176 TRP A N 1 ATOM 1400 C CA . TRP A 1 177 ? 21.361 19.644 27.388 1.00 24.39 ? 176 TRP A CA 1 ATOM 1401 C C . TRP A 1 177 ? 22.789 19.463 26.914 1.00 24.23 ? 176 TRP A C 1 ATOM 1402 O O . TRP A 1 177 ? 23.217 18.344 26.593 1.00 23.06 ? 176 TRP A O 1 ATOM 1403 C CB . TRP A 1 177 ? 21.338 20.081 28.857 1.00 24.55 ? 176 TRP A CB 1 ATOM 1404 C CG . TRP A 1 177 ? 22.071 19.179 29.751 1.00 24.07 ? 176 TRP A CG 1 ATOM 1405 C CD1 . TRP A 1 177 ? 23.309 19.376 30.269 1.00 24.48 ? 176 TRP A CD1 1 ATOM 1406 C CD2 . TRP A 1 177 ? 21.616 17.923 30.257 1.00 24.18 ? 176 TRP A CD2 1 ATOM 1407 N NE1 . TRP A 1 177 ? 23.660 18.330 31.078 1.00 24.12 ? 176 TRP A NE1 1 ATOM 1408 C CE2 . TRP A 1 177 ? 22.647 17.411 31.079 1.00 23.98 ? 176 TRP A CE2 1 ATOM 1409 C CE3 . TRP A 1 177 ? 20.437 17.182 30.102 1.00 23.92 ? 176 TRP A CE3 1 ATOM 1410 C CZ2 . TRP A 1 177 ? 22.546 16.184 31.733 1.00 24.05 ? 176 TRP A CZ2 1 ATOM 1411 C CZ3 . TRP A 1 177 ? 20.332 15.951 30.754 1.00 24.07 ? 176 TRP A CZ3 1 ATOM 1412 C CH2 . TRP A 1 177 ? 21.371 15.476 31.575 1.00 23.95 ? 176 TRP A CH2 1 ATOM 1413 N N . GLY A 1 178 ? 23.529 20.562 26.885 1.00 24.84 ? 177 GLY A N 1 ATOM 1414 C CA . GLY A 1 178 ? 24.901 20.514 26.436 1.00 25.40 ? 177 GLY A CA 1 ATOM 1415 C C . GLY A 1 178 ? 25.787 21.524 27.110 1.00 25.94 ? 177 GLY A C 1 ATOM 1416 O O . GLY A 1 178 ? 25.335 22.309 27.931 1.00 27.03 ? 177 GLY A O 1 ATOM 1417 N N . ILE A 1 179 ? 27.062 21.479 26.761 1.00 26.30 ? 178 ILE A N 1 ATOM 1418 C CA . ILE A 1 179 ? 28.057 22.384 27.317 1.00 27.24 ? 178 ILE A CA 1 ATOM 1419 C C . ILE A 1 179 ? 28.978 22.841 26.213 1.00 27.99 ? 178 ILE A C 1 ATOM 1420 O O . ILE A 1 179 ? 29.357 22.053 25.369 1.00 27.99 ? 178 ILE A O 1 ATOM 1421 C CB . ILE A 1 179 ? 28.889 21.738 28.429 1.00 27.23 ? 178 ILE A CB 1 ATOM 1422 C CG1 . ILE A 1 179 ? 29.924 22.734 28.953 1.00 28.70 ? 178 ILE A CG1 1 ATOM 1423 C CG2 . ILE A 1 179 ? 29.564 20.447 27.949 1.00 26.99 ? 178 ILE A CG2 1 ATOM 1424 C CD1 . ILE A 1 179 ? 30.645 22.294 30.215 1.00 28.91 ? 178 ILE A CD1 1 ATOM 1425 N N . HIS A 1 180 ? 29.312 24.124 26.215 1.00 29.26 ? 179 HIS A N 1 ATOM 1426 C CA . HIS A 1 180 ? 30.178 24.697 25.190 1.00 30.62 ? 179 HIS A CA 1 ATOM 1427 C C . HIS A 1 180 ? 31.638 24.699 25.625 1.00 30.93 ? 179 HIS A C 1 ATOM 1428 O O . HIS A 1 180 ? 31.972 25.275 26.656 1.00 30.71 ? 179 HIS A O 1 ATOM 1429 C CB . HIS A 1 180 ? 29.742 26.126 24.864 1.00 31.98 ? 179 HIS A CB 1 ATOM 1430 C CG . HIS A 1 180 ? 30.588 26.788 23.826 1.00 33.84 ? 179 HIS A CG 1 ATOM 1431 N ND1 . HIS A 1 180 ? 31.084 28.065 23.975 1.00 35.60 ? 179 HIS A ND1 1 ATOM 1432 C CD2 . HIS A 1 180 ? 31.039 26.345 22.630 1.00 34.43 ? 179 HIS A CD2 1 ATOM 1433 C CE1 . HIS A 1 180 ? 31.790 28.386 22.909 1.00 37.24 ? 179 HIS A CE1 1 ATOM 1434 N NE2 . HIS A 1 180 ? 31.777 27.362 22.076 1.00 36.81 ? 179 HIS A NE2 1 ATOM 1435 N N . HIS A 1 181 ? 32.489 24.055 24.824 1.00 31.49 ? 180 HIS A N 1 ATOM 1436 C CA . HIS A 1 181 ? 33.934 24.001 25.051 1.00 32.36 ? 180 HIS A CA 1 ATOM 1437 C C . HIS A 1 181 ? 34.646 25.037 24.175 1.00 34.83 ? 180 HIS A C 1 ATOM 1438 O O . HIS A 1 181 ? 34.992 24.735 23.037 1.00 35.32 ? 180 HIS A O 1 ATOM 1439 C CB . HIS A 1 181 ? 34.462 22.625 24.663 1.00 31.97 ? 180 HIS A CB 1 ATOM 1440 C CG . HIS A 1 181 ? 33.873 21.490 25.441 1.00 30.42 ? 180 HIS A CG 1 ATOM 1441 N ND1 . HIS A 1 181 ? 33.862 21.458 26.819 1.00 30.14 ? 180 HIS A ND1 1 ATOM 1442 C CD2 . HIS A 1 181 ? 33.334 20.316 25.038 1.00 29.19 ? 180 HIS A CD2 1 ATOM 1443 C CE1 . HIS A 1 181 ? 33.319 20.327 27.231 1.00 28.34 ? 180 HIS A CE1 1 ATOM 1444 N NE2 . HIS A 1 181 ? 32.988 19.618 26.172 1.00 28.02 ? 180 HIS A NE2 1 ATOM 1445 N N . PRO A 1 182 ? 34.903 26.254 24.697 1.00 37.04 ? 181 PRO A N 1 ATOM 1446 C CA . PRO A 1 182 ? 35.429 27.312 23.820 1.00 39.74 ? 181 PRO A CA 1 ATOM 1447 C C . PRO A 1 182 ? 36.906 27.161 23.409 1.00 42.27 ? 181 PRO A C 1 ATOM 1448 O O . PRO A 1 182 ? 37.614 26.287 23.912 1.00 41.08 ? 181 PRO A O 1 ATOM 1449 C CB . PRO A 1 182 ? 35.227 28.591 24.644 1.00 40.17 ? 181 PRO A CB 1 ATOM 1450 C CG . PRO A 1 182 ? 34.986 28.157 26.048 1.00 38.68 ? 181 PRO A CG 1 ATOM 1451 C CD . PRO A 1 182 ? 34.964 26.655 26.111 1.00 36.95 ? 181 PRO A CD 1 ATOM 1452 N N . ASN A 1 183 ? 37.349 28.037 22.504 1.00 45.97 ? 182 ASN A N 1 ATOM 1453 C CA . ASN A 1 183 ? 38.702 27.987 21.933 1.00 48.98 ? 182 ASN A CA 1 ATOM 1454 C C . ASN A 1 183 ? 39.791 28.580 22.806 1.00 50.19 ? 182 ASN A C 1 ATOM 1455 O O . ASN A 1 183 ? 40.932 28.131 22.765 1.00 51.02 ? 182 ASN A O 1 ATOM 1456 C CB . ASN A 1 183 ? 38.736 28.724 20.591 1.00 51.97 ? 182 ASN A CB 1 ATOM 1457 C CG . ASN A 1 183 ? 37.887 28.056 19.550 1.00 52.07 ? 182 ASN A CG 1 ATOM 1458 O OD1 . ASN A 1 183 ? 37.616 26.862 19.639 1.00 51.45 ? 182 ASN A OD1 1 ATOM 1459 N ND2 . ASN A 1 183 ? 37.450 28.820 18.559 1.00 54.42 ? 182 ASN A ND2 1 ATOM 1460 N N . ASP A 1 184 ? 39.452 29.618 23.557 1.00 51.22 ? 183 ASP A N 1 ATOM 1461 C CA . ASP A 1 184 ? 40.446 30.311 24.366 1.00 53.56 ? 183 ASP A CA 1 ATOM 1462 C C . ASP A 1 184 ? 39.793 31.136 25.461 1.00 52.56 ? 183 ASP A C 1 ATOM 1463 O O . ASP A 1 184 ? 38.567 31.277 25.506 1.00 51.49 ? 183 ASP A O 1 ATOM 1464 C CB . ASP A 1 184 ? 41.327 31.196 23.477 1.00 57.33 ? 183 ASP A CB 1 ATOM 1465 C CG . ASP A 1 184 ? 40.518 32.096 22.568 1.00 59.10 ? 183 ASP A CG 1 ATOM 1466 O OD1 . ASP A 1 184 ? 39.963 33.103 23.057 1.00 60.35 ? 183 ASP A OD1 1 ATOM 1467 O OD2 . ASP A 1 184 ? 40.438 31.794 21.359 1.00 60.97 ? 183 ASP A OD2 1 ATOM 1468 N N . ALA A 1 185 ? 40.631 31.654 26.351 1.00 53.17 ? 184 ALA A N 1 ATOM 1469 C CA . ALA A 1 185 ? 40.191 32.525 27.436 1.00 53.13 ? 184 ALA A CA 1 ATOM 1470 C C . ALA A 1 185 ? 39.396 33.735 26.928 1.00 53.80 ? 184 ALA A C 1 ATOM 1471 O O . ALA A 1 185 ? 38.367 34.096 27.509 1.00 53.69 ? 184 ALA A O 1 ATOM 1472 C CB . ALA A 1 185 ? 41.393 32.990 28.259 1.00 54.24 ? 184 ALA A CB 1 ATOM 1473 N N . ALA A 1 186 ? 39.867 34.353 25.850 1.00 54.90 ? 185 ALA A N 1 ATOM 1474 C CA . ALA A 1 186 ? 39.244 35.582 25.346 1.00 56.31 ? 185 ALA A CA 1 ATOM 1475 C C . ALA A 1 186 ? 37.805 35.320 24.919 1.00 54.40 ? 185 ALA A C 1 ATOM 1476 O O . ALA A 1 186 ? 36.907 36.114 25.208 1.00 54.19 ? 185 ALA A O 1 ATOM 1477 C CB . ALA A 1 186 ? 40.046 36.165 24.185 1.00 58.50 ? 185 ALA A CB 1 ATOM 1478 N N . GLU A 1 187 ? 37.601 34.200 24.231 1.00 52.79 ? 186 GLU A N 1 ATOM 1479 C CA . GLU A 1 187 ? 36.278 33.816 23.764 1.00 51.52 ? 186 GLU A CA 1 ATOM 1480 C C . GLU A 1 187 ? 35.375 33.458 24.946 1.00 49.00 ? 186 GLU A C 1 ATOM 1481 O O . GLU A 1 187 ? 34.184 33.776 24.943 1.00 47.98 ? 186 GLU A O 1 ATOM 1482 C CB . GLU A 1 187 ? 36.386 32.648 22.782 1.00 51.14 ? 186 GLU A CB 1 ATOM 1483 C CG . GLU A 1 187 ? 35.058 32.043 22.374 1.00 50.10 ? 186 GLU A CG 1 ATOM 1484 C CD . GLU A 1 187 ? 35.222 30.900 21.398 1.00 50.11 ? 186 GLU A CD 1 ATOM 1485 O OE1 . GLU A 1 187 ? 35.739 31.144 20.281 1.00 52.96 ? 186 GLU A OE1 1 ATOM 1486 O OE2 . GLU A 1 187 ? 34.838 29.763 21.747 1.00 47.55 ? 186 GLU A OE2 1 ATOM 1487 N N . GLN A 1 188 ? 35.955 32.806 25.954 1.00 47.80 ? 187 GLN A N 1 ATOM 1488 C CA . GLN A 1 188 ? 35.235 32.452 27.176 1.00 45.68 ? 187 GLN A CA 1 ATOM 1489 C C . GLN A 1 188 ? 34.581 33.689 27.784 1.00 46.63 ? 187 GLN A C 1 ATOM 1490 O O . GLN A 1 188 ? 33.382 33.685 28.040 1.00 45.61 ? 187 GLN A O 1 ATOM 1491 C CB . GLN A 1 188 ? 36.196 31.809 28.176 1.00 44.84 ? 187 GLN A CB 1 ATOM 1492 C CG . GLN A 1 188 ? 35.637 31.558 29.567 1.00 43.41 ? 187 GLN A CG 1 ATOM 1493 C CD . GLN A 1 188 ? 34.578 30.477 29.593 1.00 41.13 ? 187 GLN A CD 1 ATOM 1494 O OE1 . GLN A 1 188 ? 34.488 29.664 28.681 1.00 40.95 ? 187 GLN A OE1 1 ATOM 1495 N NE2 . GLN A 1 188 ? 33.776 30.457 30.649 1.00 39.73 ? 187 GLN A NE2 1 ATOM 1496 N N . THR A 1 189 ? 35.369 34.744 28.001 1.00 48.37 ? 188 THR A N 1 ATOM 1497 C CA . THR A 1 189 ? 34.861 35.967 28.634 1.00 49.73 ? 188 THR A CA 1 ATOM 1498 C C . THR A 1 189 ? 33.964 36.777 27.698 1.00 51.09 ? 188 THR A C 1 ATOM 1499 O O . THR A 1 189 ? 32.995 37.396 28.139 1.00 51.32 ? 188 THR A O 1 ATOM 1500 C CB . THR A 1 189 ? 35.998 36.875 29.163 1.00 51.87 ? 188 THR A CB 1 ATOM 1501 O OG1 . THR A 1 189 ? 36.989 37.061 28.151 1.00 52.94 ? 188 THR A OG1 1 ATOM 1502 C CG2 . THR A 1 189 ? 36.651 36.252 30.391 1.00 51.34 ? 188 THR A CG2 1 ATOM 1503 N N . ARG A 1 190 ? 34.284 36.772 26.409 1.00 51.97 ? 189 ARG A N 1 ATOM 1504 C CA . ARG A 1 190 ? 33.435 37.422 25.419 1.00 53.28 ? 189 ARG A CA 1 ATOM 1505 C C . ARG A 1 190 ? 32.028 36.812 25.384 1.00 50.93 ? 189 ARG A C 1 ATOM 1506 O O . ARG A 1 190 ? 31.044 37.532 25.197 1.00 51.83 ? 189 ARG A O 1 ATOM 1507 C CB . ARG A 1 190 ? 34.077 37.345 24.035 1.00 55.30 ? 189 ARG A CB 1 ATOM 1508 C CG . ARG A 1 190 ? 33.375 38.192 22.992 1.00 58.02 ? 189 ARG A CG 1 ATOM 1509 C CD . ARG A 1 190 ? 34.195 38.313 21.717 1.00 60.76 ? 189 ARG A CD 1 ATOM 1510 N NE . ARG A 1 190 ? 34.691 37.025 21.233 1.00 60.20 ? 189 ARG A NE 1 ATOM 1511 C CZ . ARG A 1 190 ? 33.957 36.117 20.587 1.00 59.54 ? 189 ARG A CZ 1 ATOM 1512 N NH1 . ARG A 1 190 ? 32.664 36.327 20.334 1.00 59.16 ? 189 ARG A NH1 1 ATOM 1513 N NH2 . ARG A 1 190 ? 34.523 34.977 20.195 1.00 59.18 ? 189 ARG A NH2 1 ATOM 1514 N N . LEU A 1 191 ? 31.928 35.495 25.565 1.00 47.71 ? 190 LEU A N 1 ATOM 1515 C CA . LEU A 1 191 ? 30.629 34.828 25.526 1.00 45.32 ? 190 LEU A CA 1 ATOM 1516 C C . LEU A 1 191 ? 29.919 34.825 26.878 1.00 43.91 ? 190 LEU A C 1 ATOM 1517 O O . LEU A 1 191 ? 28.709 35.042 26.946 1.00 43.82 ? 190 LEU A O 1 ATOM 1518 C CB . LEU A 1 191 ? 30.772 33.386 25.044 1.00 43.75 ? 190 LEU A CB 1 ATOM 1519 C CG . LEU A 1 191 ? 31.270 33.109 23.627 1.00 44.48 ? 190 LEU A CG 1 ATOM 1520 C CD1 . LEU A 1 191 ? 30.840 31.710 23.208 1.00 42.41 ? 190 LEU A CD1 1 ATOM 1521 C CD2 . LEU A 1 191 ? 30.751 34.132 22.642 1.00 46.74 ? 190 LEU A CD2 1 ATOM 1522 N N . TYR A 1 192 ? 30.664 34.572 27.951 1.00 42.87 ? 191 TYR A N 1 ATOM 1523 C CA . TYR A 1 192 ? 30.054 34.289 29.255 1.00 41.40 ? 191 TYR A CA 1 ATOM 1524 C C . TYR A 1 192 ? 30.496 35.194 30.408 1.00 42.27 ? 191 TYR A C 1 ATOM 1525 O O . TYR A 1 192 ? 29.897 35.161 31.482 1.00 41.44 ? 191 TYR A O 1 ATOM 1526 C CB . TYR A 1 192 ? 30.311 32.823 29.620 1.00 39.21 ? 191 TYR A CB 1 ATOM 1527 C CG . TYR A 1 192 ? 30.042 31.860 28.485 1.00 38.27 ? 191 TYR A CG 1 ATOM 1528 C CD1 . TYR A 1 192 ? 28.750 31.664 28.008 1.00 37.87 ? 191 TYR A CD1 1 ATOM 1529 C CD2 . TYR A 1 192 ? 31.082 31.153 27.876 1.00 38.34 ? 191 TYR A CD2 1 ATOM 1530 C CE1 . TYR A 1 192 ? 28.490 30.778 26.973 1.00 36.93 ? 191 TYR A CE1 1 ATOM 1531 C CE2 . TYR A 1 192 ? 30.833 30.259 26.842 1.00 37.33 ? 191 TYR A CE2 1 ATOM 1532 C CZ . TYR A 1 192 ? 29.529 30.081 26.392 1.00 36.64 ? 191 TYR A CZ 1 ATOM 1533 O OH . TYR A 1 192 ? 29.256 29.219 25.358 1.00 35.43 ? 191 TYR A OH 1 ATOM 1534 N N . GLN A 1 193 ? 31.532 35.998 30.189 1.00 44.45 ? 192 GLN A N 1 ATOM 1535 C CA . GLN A 1 193 ? 32.048 36.936 31.194 1.00 45.92 ? 192 GLN A CA 1 ATOM 1536 C C . GLN A 1 193 ? 32.863 36.239 32.288 1.00 44.99 ? 192 GLN A C 1 ATOM 1537 O O . GLN A 1 193 ? 33.967 36.668 32.611 1.00 46.68 ? 192 GLN A O 1 ATOM 1538 C CB . GLN A 1 193 ? 30.919 37.760 31.827 1.00 46.51 ? 192 GLN A CB 1 ATOM 1539 C CG . GLN A 1 193 ? 31.401 39.041 32.472 1.00 48.78 ? 192 GLN A CG 1 ATOM 1540 C CD . GLN A 1 193 ? 31.886 40.037 31.440 1.00 51.18 ? 192 GLN A CD 1 ATOM 1541 O OE1 . GLN A 1 193 ? 31.137 40.430 30.547 1.00 52.28 ? 192 GLN A OE1 1 ATOM 1542 N NE2 . GLN A 1 193 ? 33.147 40.434 31.539 1.00 52.51 ? 192 GLN A NE2 1 ATOM 1543 N N . ASN A 1 194 ? 32.320 35.174 32.854 1.00 42.94 ? 193 ASN A N 1 ATOM 1544 C CA . ASN A 1 194 ? 32.996 34.443 33.913 1.00 42.29 ? 193 ASN A CA 1 ATOM 1545 C C . ASN A 1 194 ? 34.090 33.517 33.348 1.00 41.76 ? 193 ASN A C 1 ATOM 1546 O O . ASN A 1 194 ? 33.815 32.675 32.497 1.00 39.94 ? 193 ASN A O 1 ATOM 1547 C CB . ASN A 1 194 ? 31.975 33.640 34.713 1.00 41.01 ? 193 ASN A CB 1 ATOM 1548 C CG . ASN A 1 194 ? 30.785 34.479 35.148 1.00 42.05 ? 193 ASN A CG 1 ATOM 1549 O OD1 . ASN A 1 194 ? 30.924 35.664 35.457 1.00 44.30 ? 193 ASN A OD1 1 ATOM 1550 N ND2 . ASN A 1 194 ? 29.606 33.869 35.168 1.00 40.90 ? 193 ASN A ND2 1 ATOM 1551 N N . PRO A 1 195 ? 35.338 33.675 33.817 1.00 43.26 ? 194 PRO A N 1 ATOM 1552 C CA . PRO A 1 195 ? 36.427 32.883 33.229 1.00 43.93 ? 194 PRO A CA 1 ATOM 1553 C C . PRO A 1 195 ? 36.468 31.426 33.691 1.00 42.62 ? 194 PRO A C 1 ATOM 1554 O O . PRO A 1 195 ? 37.049 30.590 33.004 1.00 42.14 ? 194 PRO A O 1 ATOM 1555 C CB . PRO A 1 195 ? 37.692 33.635 33.675 1.00 45.72 ? 194 PRO A CB 1 ATOM 1556 C CG . PRO A 1 195 ? 37.296 34.362 34.915 1.00 46.02 ? 194 PRO A CG 1 ATOM 1557 C CD . PRO A 1 195 ? 35.828 34.663 34.799 1.00 45.05 ? 194 PRO A CD 1 ATOM 1558 N N . THR A 1 196 ? 35.845 31.142 34.837 1.00 42.16 ? 195 THR A N 1 ATOM 1559 C CA . THR A 1 196 ? 35.870 29.823 35.461 1.00 40.86 ? 195 THR A CA 1 ATOM 1560 C C . THR A 1 196 ? 34.440 29.345 35.714 1.00 39.28 ? 195 THR A C 1 ATOM 1561 O O . THR A 1 196 ? 33.765 29.830 36.619 1.00 39.52 ? 195 THR A O 1 ATOM 1562 C CB . THR A 1 196 ? 36.635 29.882 36.795 1.00 41.81 ? 195 THR A CB 1 ATOM 1563 O OG1 . THR A 1 196 ? 37.832 30.649 36.617 1.00 43.82 ? 195 THR A OG1 1 ATOM 1564 C CG2 . THR A 1 196 ? 36.990 28.482 37.284 1.00 41.16 ? 195 THR A CG2 1 ATOM 1565 N N . THR A 1 197 ? 33.980 28.390 34.918 1.00 37.23 ? 196 THR A N 1 ATOM 1566 C CA . THR A 1 197 ? 32.575 28.063 34.910 1.00 35.78 ? 196 THR A CA 1 ATOM 1567 C C . THR A 1 197 ? 32.335 26.593 35.173 1.00 34.16 ? 196 THR A C 1 ATOM 1568 O O . THR A 1 197 ? 33.277 25.793 35.184 1.00 34.46 ? 196 THR A O 1 ATOM 1569 C CB . THR A 1 197 ? 31.909 28.491 33.589 1.00 36.14 ? 196 THR A CB 1 ATOM 1570 O OG1 . THR A 1 197 ? 32.653 27.975 32.484 1.00 36.13 ? 196 THR A OG1 1 ATOM 1571 C CG2 . THR A 1 197 ? 31.865 30.006 33.486 1.00 37.82 ? 196 THR A CG2 1 ATOM 1572 N N . TYR A 1 198 ? 31.064 26.275 35.427 1.00 32.39 ? 197 TYR A N 1 ATOM 1573 C CA . TYR A 1 198 ? 30.608 24.931 35.760 1.00 31.05 ? 197 TYR A CA 1 ATOM 1574 C C . TYR A 1 198 ? 29.134 24.789 35.363 1.00 29.60 ? 197 TYR A C 1 ATOM 1575 O O . TYR A 1 198 ? 28.411 25.788 35.293 1.00 29.57 ? 197 TYR A O 1 ATOM 1576 C CB . TYR A 1 198 ? 30.743 24.673 37.278 1.00 31.27 ? 197 TYR A CB 1 ATOM 1577 C CG . TYR A 1 198 ? 29.805 25.523 38.103 1.00 32.32 ? 197 TYR A CG 1 ATOM 1578 C CD1 . TYR A 1 198 ? 30.165 26.811 38.493 1.00 34.72 ? 197 TYR A CD1 1 ATOM 1579 C CD2 . TYR A 1 198 ? 28.541 25.067 38.452 1.00 32.26 ? 197 TYR A CD2 1 ATOM 1580 C CE1 . TYR A 1 198 ? 29.300 27.610 39.216 1.00 35.41 ? 197 TYR A CE1 1 ATOM 1581 C CE2 . TYR A 1 198 ? 27.674 25.853 39.184 1.00 33.14 ? 197 TYR A CE2 1 ATOM 1582 C CZ . TYR A 1 198 ? 28.058 27.126 39.562 1.00 35.05 ? 197 TYR A CZ 1 ATOM 1583 O OH . TYR A 1 198 ? 27.210 27.931 40.291 1.00 36.42 ? 197 TYR A OH 1 ATOM 1584 N N . ILE A 1 199 ? 28.699 23.552 35.133 1.00 28.12 ? 198 ILE A N 1 ATOM 1585 C CA . ILE A 1 199 ? 27.274 23.216 35.008 1.00 28.10 ? 198 ILE A CA 1 ATOM 1586 C C . ILE A 1 199 ? 26.976 22.047 35.921 1.00 27.62 ? 198 ILE A C 1 ATOM 1587 O O . ILE A 1 199 ? 27.549 20.967 35.762 1.00 27.47 ? 198 ILE A O 1 ATOM 1588 C CB . ILE A 1 199 ? 26.867 22.776 33.581 1.00 27.73 ? 198 ILE A CB 1 ATOM 1589 C CG1 . ILE A 1 199 ? 26.978 23.929 32.593 1.00 28.42 ? 198 ILE A CG1 1 ATOM 1590 C CG2 . ILE A 1 199 ? 25.439 22.252 33.561 1.00 27.17 ? 198 ILE A CG2 1 ATOM 1591 C CD1 . ILE A 1 199 ? 27.347 23.444 31.214 1.00 28.48 ? 198 ILE A CD1 1 ATOM 1592 N N . SER A 1 200 ? 26.081 22.269 36.872 1.00 28.31 ? 199 SER A N 1 ATOM 1593 C CA . SER A 1 200 ? 25.634 21.229 37.782 1.00 28.10 ? 199 SER A CA 1 ATOM 1594 C C . SER A 1 200 ? 24.287 20.801 37.296 1.00 26.64 ? 199 SER A C 1 ATOM 1595 O O . SER A 1 200 ? 23.474 21.647 36.930 1.00 25.96 ? 199 SER A O 1 ATOM 1596 C CB . SER A 1 200 ? 25.474 21.749 39.208 1.00 30.02 ? 199 SER A CB 1 ATOM 1597 O OG . SER A 1 200 ? 26.697 21.643 39.890 1.00 33.08 ? 199 SER A OG 1 ATOM 1598 N N . VAL A 1 201 ? 24.069 19.492 37.301 1.00 25.12 ? 200 VAL A N 1 ATOM 1599 C CA . VAL A 1 201 ? 22.797 18.923 36.953 1.00 25.06 ? 200 VAL A CA 1 ATOM 1600 C C . VAL A 1 201 ? 22.492 17.757 37.867 1.00 24.77 ? 200 VAL A C 1 ATOM 1601 O O . VAL A 1 201 ? 23.304 16.818 37.986 1.00 24.39 ? 200 VAL A O 1 ATOM 1602 C CB . VAL A 1 201 ? 22.774 18.417 35.506 1.00 24.65 ? 200 VAL A CB 1 ATOM 1603 C CG1 . VAL A 1 201 ? 21.335 18.183 35.071 1.00 24.72 ? 200 VAL A CG1 1 ATOM 1604 C CG2 . VAL A 1 201 ? 23.448 19.424 34.581 1.00 24.92 ? 200 VAL A CG2 1 ATOM 1605 N N . GLY A 1 202 ? 21.314 17.818 38.488 1.00 24.60 ? 201 GLY A N 1 ATOM 1606 C CA . GLY A 1 202 ? 20.865 16.784 39.397 1.00 24.89 ? 201 GLY A CA 1 ATOM 1607 C C . GLY A 1 202 ? 19.413 16.372 39.196 1.00 25.24 ? 201 GLY A C 1 ATOM 1608 O O . GLY A 1 202 ? 18.550 17.219 38.914 1.00 25.00 ? 201 GLY A O 1 ATOM 1609 N N . THR A 1 203 ? 19.172 15.064 39.324 1.00 24.67 ? 202 THR A N 1 ATOM 1610 C CA . THR A 1 203 ? 17.848 14.502 39.482 1.00 25.57 ? 202 THR A CA 1 ATOM 1611 C C . THR A 1 203 ? 17.841 13.589 40.727 1.00 26.66 ? 202 THR A C 1 ATOM 1612 O O . THR A 1 203 ? 18.650 13.752 41.645 1.00 27.42 ? 202 THR A O 1 ATOM 1613 C CB . THR A 1 203 ? 17.411 13.724 38.216 1.00 24.89 ? 202 THR A CB 1 ATOM 1614 O OG1 . THR A 1 203 ? 18.103 12.462 38.116 1.00 24.28 ? 202 THR A OG1 1 ATOM 1615 C CG2 . THR A 1 203 ? 17.661 14.545 36.979 1.00 23.87 ? 202 THR A CG2 1 ATOM 1616 N N . SER A 1 204 ? 16.926 12.636 40.783 1.00 27.21 ? 203 SER A N 1 ATOM 1617 C CA . SER A 1 204 ? 16.995 11.628 41.835 1.00 28.65 ? 203 SER A CA 1 ATOM 1618 C C . SER A 1 204 ? 18.174 10.676 41.602 1.00 28.13 ? 203 SER A C 1 ATOM 1619 O O . SER A 1 204 ? 18.735 10.157 42.554 1.00 28.82 ? 203 SER A O 1 ATOM 1620 C CB . SER A 1 204 ? 15.696 10.840 41.912 1.00 29.33 ? 203 SER A CB 1 ATOM 1621 O OG . SER A 1 204 ? 15.467 10.219 40.675 1.00 28.80 ? 203 SER A OG 1 ATOM 1622 N N . THR A 1 205 ? 18.546 10.480 40.336 1.00 28.11 ? 204 THR A N 1 ATOM 1623 C CA . THR A 1 205 ? 19.641 9.574 39.928 1.00 28.42 ? 204 THR A CA 1 ATOM 1624 C C . THR A 1 205 ? 20.880 10.301 39.365 1.00 28.22 ? 204 THR A C 1 ATOM 1625 O O . THR A 1 205 ? 22.002 9.850 39.533 1.00 29.35 ? 204 THR A O 1 ATOM 1626 C CB . THR A 1 205 ? 19.157 8.561 38.863 1.00 27.83 ? 204 THR A CB 1 ATOM 1627 O OG1 . THR A 1 205 ? 18.547 9.260 37.772 1.00 26.75 ? 204 THR A OG1 1 ATOM 1628 C CG2 . THR A 1 205 ? 18.149 7.578 39.454 1.00 28.67 ? 204 THR A CG2 1 ATOM 1629 N N . LEU A 1 206 ? 20.681 11.430 38.705 1.00 27.95 ? 205 LEU A N 1 ATOM 1630 C CA . LEU A 1 206 ? 21.772 12.110 38.044 1.00 26.90 ? 205 LEU A CA 1 ATOM 1631 C C . LEU A 1 206 ? 22.499 12.996 39.017 1.00 27.33 ? 205 LEU A C 1 ATOM 1632 O O . LEU A 1 206 ? 21.880 13.609 39.874 1.00 28.62 ? 205 LEU A O 1 ATOM 1633 C CB . LEU A 1 206 ? 21.222 12.946 36.899 1.00 26.62 ? 205 LEU A CB 1 ATOM 1634 C CG . LEU A 1 206 ? 22.210 13.662 35.983 1.00 26.40 ? 205 LEU A CG 1 ATOM 1635 C CD1 . LEU A 1 206 ? 23.076 12.670 35.224 1.00 26.82 ? 205 LEU A CD1 1 ATOM 1636 C CD2 . LEU A 1 206 ? 21.427 14.523 35.015 1.00 25.96 ? 205 LEU A CD2 1 ATOM 1637 N N . ASN A 1 207 ? 23.817 13.079 38.863 1.00 27.11 ? 206 ASN A N 1 ATOM 1638 C CA . ASN A 1 207 ? 24.664 13.901 39.713 1.00 27.25 ? 206 ASN A CA 1 ATOM 1639 C C . ASN A 1 207 ? 25.916 14.331 38.932 1.00 27.43 ? 206 ASN A C 1 ATOM 1640 O O . ASN A 1 207 ? 26.958 13.673 38.989 1.00 27.60 ? 206 ASN A O 1 ATOM 1641 C CB . ASN A 1 207 ? 25.024 13.098 40.959 1.00 28.28 ? 206 ASN A CB 1 ATOM 1642 C CG . ASN A 1 207 ? 25.959 13.830 41.884 1.00 29.28 ? 206 ASN A CG 1 ATOM 1643 O OD1 . ASN A 1 207 ? 25.918 15.049 42.008 1.00 28.34 ? 206 ASN A OD1 1 ATOM 1644 N ND2 . ASN A 1 207 ? 26.811 13.074 42.553 1.00 31.57 ? 206 ASN A ND2 1 ATOM 1645 N N . GLN A 1 208 ? 25.798 15.436 38.202 1.00 27.55 ? 207 GLN A N 1 ATOM 1646 C CA . GLN A 1 208 ? 26.795 15.828 37.219 1.00 27.89 ? 207 GLN A CA 1 ATOM 1647 C C . GLN A 1 208 ? 27.358 17.223 37.494 1.00 29.42 ? 207 GLN A C 1 ATOM 1648 O O . GLN A 1 208 ? 26.603 18.142 37.785 1.00 28.75 ? 207 GLN A O 1 ATOM 1649 C CB . GLN A 1 208 ? 26.152 15.776 35.839 1.00 27.43 ? 207 GLN A CB 1 ATOM 1650 C CG . GLN A 1 208 ? 26.894 16.541 34.773 1.00 28.39 ? 207 GLN A CG 1 ATOM 1651 C CD . GLN A 1 208 ? 26.219 16.467 33.422 1.00 28.35 ? 207 GLN A CD 1 ATOM 1652 O OE1 . GLN A 1 208 ? 25.779 17.477 32.896 1.00 28.58 ? 207 GLN A OE1 1 ATOM 1653 N NE2 . GLN A 1 208 ? 26.147 15.272 32.852 1.00 28.41 ? 207 GLN A NE2 1 ATOM 1654 N N . ARG A 1 209 ? 28.686 17.362 37.410 1.00 31.54 ? 208 ARG A N 1 ATOM 1655 C CA . ARG A 1 209 ? 29.342 18.674 37.402 1.00 33.66 ? 208 ARG A CA 1 ATOM 1656 C C . ARG A 1 209 ? 30.363 18.768 36.273 1.00 34.93 ? 208 ARG A C 1 ATOM 1657 O O . ARG A 1 209 ? 31.367 18.066 36.266 1.00 37.48 ? 208 ARG A O 1 ATOM 1658 C CB . ARG A 1 209 ? 30.013 18.986 38.731 1.00 35.38 ? 208 ARG A CB 1 ATOM 1659 C CG . ARG A 1 209 ? 30.105 20.486 38.995 1.00 36.21 ? 208 ARG A CG 1 ATOM 1660 C CD . ARG A 1 209 ? 30.711 20.776 40.357 1.00 37.41 ? 208 ARG A CD 1 ATOM 1661 N NE . ARG A 1 209 ? 30.889 22.212 40.587 1.00 38.39 ? 208 ARG A NE 1 ATOM 1662 C CZ . ARG A 1 209 ? 30.058 22.999 41.272 1.00 38.42 ? 208 ARG A CZ 1 ATOM 1663 N NH1 . ARG A 1 209 ? 28.945 22.522 41.831 1.00 38.40 ? 208 ARG A NH1 1 ATOM 1664 N NH2 . ARG A 1 209 ? 30.347 24.285 41.402 1.00 38.80 ? 208 ARG A NH2 1 ATOM 1665 N N . LEU A 1 210 ? 30.091 19.647 35.314 1.00 35.10 ? 209 LEU A N 1 ATOM 1666 C CA . LEU A 1 210 ? 30.918 19.775 34.132 1.00 34.23 ? 209 LEU A CA 1 ATOM 1667 C C . LEU A 1 210 ? 31.689 21.079 34.221 1.00 34.43 ? 209 LEU A C 1 ATOM 1668 O O . LEU A 1 210 ? 31.166 22.083 34.709 1.00 33.81 ? 209 LEU A O 1 ATOM 1669 C CB . LEU A 1 210 ? 30.048 19.758 32.873 1.00 33.88 ? 209 LEU A CB 1 ATOM 1670 C CG . LEU A 1 210 ? 29.014 18.630 32.750 1.00 33.53 ? 209 LEU A CG 1 ATOM 1671 C CD1 . LEU A 1 210 ? 28.049 18.946 31.627 1.00 33.86 ? 209 LEU A CD1 1 ATOM 1672 C CD2 . LEU A 1 210 ? 29.670 17.282 32.507 1.00 33.89 ? 209 LEU A CD2 1 ATOM 1673 N N . VAL A 1 211 ? 32.942 21.039 33.773 1.00 34.64 ? 210 VAL A N 1 ATOM 1674 C CA . VAL A 1 211 ? 33.786 22.222 33.638 1.00 35.33 ? 210 VAL A CA 1 ATOM 1675 C C . VAL A 1 211 ? 34.237 22.277 32.170 1.00 35.16 ? 210 VAL A C 1 ATOM 1676 O O . VAL A 1 211 ? 34.691 21.271 31.618 1.00 35.00 ? 210 VAL A O 1 ATOM 1677 C CB . VAL A 1 211 ? 34.987 22.158 34.603 1.00 36.17 ? 210 VAL A CB 1 ATOM 1678 C CG1 . VAL A 1 211 ? 35.955 23.310 34.366 1.00 38.15 ? 210 VAL A CG1 1 ATOM 1679 C CG2 . VAL A 1 211 ? 34.498 22.190 36.039 1.00 36.14 ? 210 VAL A CG2 1 ATOM 1680 N N . PRO A 1 212 ? 34.078 23.436 31.516 1.00 35.56 ? 211 PRO A N 1 ATOM 1681 C CA . PRO A 1 212 ? 34.445 23.491 30.101 1.00 35.79 ? 211 PRO A CA 1 ATOM 1682 C C . PRO A 1 212 ? 35.923 23.275 29.883 1.00 36.47 ? 211 PRO A C 1 ATOM 1683 O O . PRO A 1 212 ? 36.734 23.703 30.706 1.00 37.62 ? 211 PRO A O 1 ATOM 1684 C CB . PRO A 1 212 ? 34.083 24.923 29.689 1.00 36.42 ? 211 PRO A CB 1 ATOM 1685 C CG . PRO A 1 212 ? 33.105 25.377 30.708 1.00 36.25 ? 211 PRO A CG 1 ATOM 1686 C CD . PRO A 1 212 ? 33.519 24.716 31.984 1.00 35.93 ? 211 PRO A CD 1 ATOM 1687 N N . LYS A 1 213 ? 36.256 22.602 28.788 1.00 36.10 ? 212 LYS A N 1 ATOM 1688 C CA . LYS A 1 213 ? 37.632 22.475 28.327 1.00 36.96 ? 212 LYS A CA 1 ATOM 1689 C C . LYS A 1 213 ? 37.942 23.584 27.318 1.00 38.58 ? 212 LYS A C 1 ATOM 1690 O O . LYS A 1 213 ? 37.395 23.601 26.208 1.00 38.54 ? 212 LYS A O 1 ATOM 1691 C CB . LYS A 1 213 ? 37.837 21.098 27.714 1.00 36.24 ? 212 LYS A CB 1 ATOM 1692 C CG . LYS A 1 213 ? 37.743 19.991 28.749 1.00 35.79 ? 212 LYS A CG 1 ATOM 1693 C CD . LYS A 1 213 ? 37.854 18.599 28.147 1.00 36.17 ? 212 LYS A CD 1 ATOM 1694 C CE . LYS A 1 213 ? 36.499 17.973 27.895 1.00 35.61 ? 212 LYS A CE 1 ATOM 1695 N NZ . LYS A 1 213 ? 36.571 16.509 27.585 1.00 36.09 ? 212 LYS A NZ 1 ATOM 1696 N N . ILE A 1 214 ? 38.801 24.516 27.713 1.00 39.96 ? 213 ILE A N 1 ATOM 1697 C CA . ILE A 1 214 ? 39.195 25.628 26.855 1.00 42.36 ? 213 ILE A CA 1 ATOM 1698 C C . ILE A 1 214 ? 40.545 25.308 26.228 1.00 44.61 ? 213 ILE A C 1 ATOM 1699 O O . ILE A 1 214 ? 41.570 25.386 26.904 1.00 46.16 ? 213 ILE A O 1 ATOM 1700 C CB . ILE A 1 214 ? 39.319 26.941 27.656 1.00 43.55 ? 213 ILE A CB 1 ATOM 1701 C CG1 . ILE A 1 214 ? 38.065 27.192 28.494 1.00 42.61 ? 213 ILE A CG1 1 ATOM 1702 C CG2 . ILE A 1 214 ? 39.548 28.120 26.727 1.00 45.49 ? 213 ILE A CG2 1 ATOM 1703 C CD1 . ILE A 1 214 ? 38.207 28.339 29.471 1.00 43.64 ? 213 ILE A CD1 1 ATOM 1704 N N . ALA A 1 215 ? 40.551 24.963 24.941 1.00 45.85 ? 214 ALA A N 1 ATOM 1705 C CA . ALA A 1 215 ? 41.780 24.531 24.263 1.00 48.49 ? 214 ALA A CA 1 ATOM 1706 C C . ALA A 1 215 ? 41.754 24.728 22.736 1.00 50.32 ? 214 ALA A C 1 ATOM 1707 O O . ALA A 1 215 ? 40.703 24.963 22.135 1.00 50.26 ? 214 ALA A O 1 ATOM 1708 C CB . ALA A 1 215 ? 42.071 23.072 24.600 1.00 47.56 ? 214 ALA A CB 1 ATOM 1709 N N . THR A 1 216 ? 42.930 24.622 22.125 1.00 52.30 ? 215 THR A N 1 ATOM 1710 C CA . THR A 1 216 ? 43.091 24.797 20.686 1.00 53.59 ? 215 THR A CA 1 ATOM 1711 C C . THR A 1 216 ? 42.776 23.493 19.950 1.00 52.56 ? 215 THR A C 1 ATOM 1712 O O . THR A 1 216 ? 43.429 22.481 20.182 1.00 52.74 ? 215 THR A O 1 ATOM 1713 C CB . THR A 1 216 ? 44.532 25.239 20.371 1.00 56.49 ? 215 THR A CB 1 ATOM 1714 O OG1 . THR A 1 216 ? 44.837 26.419 21.120 1.00 56.91 ? 215 THR A OG1 1 ATOM 1715 C CG2 . THR A 1 216 ? 44.717 25.529 18.887 1.00 58.79 ? 215 THR A CG2 1 ATOM 1716 N N . ARG A 1 217 ? 41.771 23.524 19.074 1.00 51.41 ? 216 ARG A N 1 ATOM 1717 C CA . ARG A 1 217 ? 41.347 22.338 18.309 1.00 50.49 ? 216 ARG A CA 1 ATOM 1718 C C . ARG A 1 217 ? 41.276 22.643 16.817 1.00 51.72 ? 216 ARG A C 1 ATOM 1719 O O . ARG A 1 217 ? 41.304 23.800 16.399 1.00 52.99 ? 216 ARG A O 1 ATOM 1720 C CB . ARG A 1 217 ? 39.968 21.827 18.789 1.00 47.99 ? 216 ARG A CB 1 ATOM 1721 C CG . ARG A 1 217 ? 39.980 21.102 20.134 1.00 46.50 ? 216 ARG A CG 1 ATOM 1722 C CD . ARG A 1 217 ? 38.613 21.058 20.812 1.00 43.84 ? 216 ARG A CD 1 ATOM 1723 N NE . ARG A 1 217 ? 38.179 22.388 21.246 1.00 44.12 ? 216 ARG A NE 1 ATOM 1724 C CZ . ARG A 1 217 ? 38.022 22.797 22.508 1.00 42.95 ? 216 ARG A CZ 1 ATOM 1725 N NH1 . ARG A 1 217 ? 38.229 21.996 23.540 1.00 41.32 ? 216 ARG A NH1 1 ATOM 1726 N NH2 . ARG A 1 217 ? 37.631 24.043 22.735 1.00 43.71 ? 216 ARG A NH2 1 ATOM 1727 N N . SER A 1 218 ? 41.174 21.587 16.021 1.00 51.33 ? 217 SER A N 1 ATOM 1728 C CA . SER A 1 218 ? 41.046 21.722 14.575 1.00 52.83 ? 217 SER A CA 1 ATOM 1729 C C . SER A 1 218 ? 39.622 22.136 14.211 1.00 51.21 ? 217 SER A C 1 ATOM 1730 O O . SER A 1 218 ? 38.670 21.754 14.884 1.00 48.84 ? 217 SER A O 1 ATOM 1731 C CB . SER A 1 218 ? 41.403 20.398 13.888 1.00 52.97 ? 217 SER A CB 1 ATOM 1732 O OG . SER A 1 218 ? 42.748 20.046 14.148 1.00 54.24 ? 217 SER A OG 1 ATOM 1733 N N . LYS A 1 219 ? 39.485 22.923 13.148 1.00 53.33 ? 218 LYS A N 1 ATOM 1734 C CA . LYS A 1 219 ? 38.168 23.347 12.665 1.00 52.73 ? 218 LYS A CA 1 ATOM 1735 C C . LYS A 1 219 ? 37.395 22.195 12.027 1.00 51.46 ? 218 LYS A C 1 ATOM 1736 O O . LYS A 1 219 ? 37.915 21.461 11.190 1.00 52.74 ? 218 LYS A O 1 ATOM 1737 C CB . LYS A 1 219 ? 38.282 24.505 11.667 1.00 55.70 ? 218 LYS A CB 1 ATOM 1738 C CG . LYS A 1 219 ? 38.437 25.861 12.334 1.00 56.66 ? 218 LYS A CG 1 ATOM 1739 C CD . LYS A 1 219 ? 38.578 26.978 11.313 1.00 59.81 ? 218 LYS A CD 1 ATOM 1740 C CE . LYS A 1 219 ? 38.332 28.336 11.950 1.00 60.35 ? 218 LYS A CE 1 ATOM 1741 N NZ . LYS A 1 219 ? 38.469 29.445 10.963 1.00 64.07 ? 218 LYS A NZ 1 ATOM 1742 N N . VAL A 1 220 ? 36.157 22.039 12.469 1.00 49.13 ? 219 VAL A N 1 ATOM 1743 C CA . VAL A 1 220 ? 35.195 21.162 11.846 1.00 48.21 ? 219 VAL A CA 1 ATOM 1744 C C . VAL A 1 220 ? 33.996 22.044 11.551 1.00 48.23 ? 219 VAL A C 1 ATOM 1745 O O . VAL A 1 220 ? 33.469 22.675 12.460 1.00 46.29 ? 219 VAL A O 1 ATOM 1746 C CB . VAL A 1 220 ? 34.794 20.016 12.793 1.00 45.38 ? 219 VAL A CB 1 ATOM 1747 C CG1 . VAL A 1 220 ? 33.711 19.155 12.170 1.00 44.16 ? 219 VAL A CG1 1 ATOM 1748 C CG2 . VAL A 1 220 ? 36.016 19.174 13.139 1.00 46.03 ? 219 VAL A CG2 1 ATOM 1749 N N . ASN A 1 221 ? 33.586 22.099 10.283 1.00 50.19 ? 220 ASN A N 1 ATOM 1750 C CA . ASN A 1 221 ? 32.546 23.030 9.836 1.00 50.94 ? 220 ASN A CA 1 ATOM 1751 C C . ASN A 1 221 ? 32.898 24.455 10.236 1.00 52.07 ? 220 ASN A C 1 ATOM 1752 O O . ASN A 1 221 ? 32.035 25.214 10.671 1.00 51.82 ? 220 ASN A O 1 ATOM 1753 C CB . ASN A 1 221 ? 31.176 22.660 10.419 1.00 48.86 ? 220 ASN A CB 1 ATOM 1754 C CG . ASN A 1 221 ? 30.698 21.290 9.980 1.00 48.21 ? 220 ASN A CG 1 ATOM 1755 O OD1 . ASN A 1 221 ? 31.434 20.516 9.368 1.00 49.84 ? 220 ASN A OD1 1 ATOM 1756 N ND2 . ASN A 1 221 ? 29.449 20.990 10.282 1.00 46.69 ? 220 ASN A ND2 1 ATOM 1757 N N . GLY A 1 222 ? 34.178 24.794 10.118 1.00 53.76 ? 221 GLY A N 1 ATOM 1758 C CA . GLY A 1 222 ? 34.668 26.126 10.450 1.00 55.18 ? 221 GLY A CA 1 ATOM 1759 C C . GLY A 1 222 ? 34.700 26.487 11.929 1.00 53.39 ? 221 GLY A C 1 ATOM 1760 O O . GLY A 1 222 ? 34.852 27.659 12.253 1.00 54.92 ? 221 GLY A O 1 ATOM 1761 N N . GLN A 1 223 ? 34.558 25.514 12.835 1.00 50.24 ? 222 GLN A N 1 ATOM 1762 C CA . GLN A 1 223 ? 34.600 25.816 14.279 1.00 48.37 ? 222 GLN A CA 1 ATOM 1763 C C . GLN A 1 223 ? 35.654 25.007 15.049 1.00 47.03 ? 222 GLN A C 1 ATOM 1764 O O . GLN A 1 223 ? 35.650 23.774 15.025 1.00 45.47 ? 222 GLN A O 1 ATOM 1765 C CB . GLN A 1 223 ? 33.228 25.581 14.923 1.00 46.39 ? 222 GLN A CB 1 ATOM 1766 C CG . GLN A 1 223 ? 32.068 26.282 14.242 1.00 47.34 ? 222 GLN A CG 1 ATOM 1767 C CD . GLN A 1 223 ? 32.191 27.791 14.266 1.00 49.65 ? 222 GLN A CD 1 ATOM 1768 O OE1 . GLN A 1 223 ? 32.477 28.393 15.304 1.00 49.12 ? 222 GLN A OE1 1 ATOM 1769 N NE2 . GLN A 1 223 ? 31.961 28.413 13.121 1.00 52.18 ? 222 GLN A NE2 1 ATOM 1770 N N . SER A 1 224 ? 36.546 25.712 15.736 1.00 47.84 ? 223 SER A N 1 ATOM 1771 C CA . SER A 1 224 ? 37.482 25.085 16.677 1.00 47.28 ? 223 SER A CA 1 ATOM 1772 C C . SER A 1 224 ? 36.813 24.840 18.037 1.00 44.56 ? 223 SER A C 1 ATOM 1773 O O . SER A 1 224 ? 37.316 24.052 18.851 1.00 43.45 ? 223 SER A O 1 ATOM 1774 C CB . SER A 1 224 ? 38.740 25.946 16.859 1.00 49.60 ? 223 SER A CB 1 ATOM 1775 O OG . SER A 1 224 ? 39.585 25.858 15.722 1.00 52.58 ? 223 SER A OG 1 ATOM 1776 N N . GLY A 1 225 ? 35.699 25.535 18.288 1.00 43.05 ? 224 GLY A N 1 ATOM 1777 C CA . GLY A 1 225 ? 34.870 25.286 19.462 1.00 40.14 ? 224 GLY A CA 1 ATOM 1778 C C . GLY A 1 225 ? 34.203 23.930 19.377 1.00 37.84 ? 224 GLY A C 1 ATOM 1779 O O . GLY A 1 225 ? 34.222 23.300 18.335 1.00 38.70 ? 224 GLY A O 1 ATOM 1780 N N . ARG A 1 226 ? 33.628 23.468 20.481 1.00 35.65 ? 225 ARG A N 1 ATOM 1781 C CA . ARG A 1 226 ? 32.905 22.210 20.500 1.00 34.30 ? 225 ARG A CA 1 ATOM 1782 C C . ARG A 1 226 ? 31.709 22.312 21.416 1.00 33.35 ? 225 ARG A C 1 ATOM 1783 O O . ARG A 1 226 ? 31.713 23.097 22.354 1.00 34.01 ? 225 ARG A O 1 ATOM 1784 C CB . ARG A 1 226 ? 33.799 21.045 20.966 1.00 33.80 ? 225 ARG A CB 1 ATOM 1785 C CG . ARG A 1 226 ? 34.977 20.713 20.054 1.00 35.22 ? 225 ARG A CG 1 ATOM 1786 C CD . ARG A 1 226 ? 34.509 20.107 18.753 1.00 35.54 ? 225 ARG A CD 1 ATOM 1787 N NE . ARG A 1 226 ? 35.621 19.683 17.912 1.00 37.48 ? 225 ARG A NE 1 ATOM 1788 C CZ . ARG A 1 226 ? 36.252 20.446 17.025 1.00 39.83 ? 225 ARG A CZ 1 ATOM 1789 N NH1 . ARG A 1 226 ? 35.912 21.723 16.839 1.00 40.75 ? 225 ARG A NH1 1 ATOM 1790 N NH2 . ARG A 1 226 ? 37.247 19.924 16.320 1.00 41.37 ? 225 ARG A NH2 1 ATOM 1791 N N . MET A 1 227 ? 30.690 21.511 21.127 1.00 33.01 ? 226 MET A N 1 ATOM 1792 C CA . MET A 1 227 ? 29.531 21.353 21.990 1.00 32.78 ? 226 MET A CA 1 ATOM 1793 C C . MET A 1 227 ? 29.467 19.893 22.387 1.00 31.14 ? 226 MET A C 1 ATOM 1794 O O . MET A 1 227 ? 29.601 19.017 21.549 1.00 30.98 ? 226 MET A O 1 ATOM 1795 C CB . MET A 1 227 ? 28.240 21.700 21.249 1.00 34.21 ? 226 MET A CB 1 ATOM 1796 C CG . MET A 1 227 ? 28.180 23.118 20.718 1.00 37.50 ? 226 MET A CG 1 ATOM 1797 S SD . MET A 1 227 ? 27.399 24.281 21.831 1.00 39.93 ? 226 MET A SD 1 ATOM 1798 C CE . MET A 1 227 ? 27.707 25.839 21.007 1.00 41.95 ? 226 MET A CE 1 ATOM 1799 N N . GLU A 1 228 ? 29.243 19.634 23.661 1.00 30.23 ? 227 GLU A N 1 ATOM 1800 C CA . GLU A 1 228 ? 29.123 18.269 24.140 1.00 29.76 ? 227 GLU A CA 1 ATOM 1801 C C . GLU A 1 228 ? 27.741 18.113 24.743 1.00 27.53 ? 227 GLU A C 1 ATOM 1802 O O . GLU A 1 228 ? 27.351 18.887 25.623 1.00 27.94 ? 227 GLU A O 1 ATOM 1803 C CB . GLU A 1 228 ? 30.201 18.006 25.176 1.00 30.53 ? 227 GLU A CB 1 ATOM 1804 C CG . GLU A 1 228 ? 30.240 16.595 25.728 1.00 30.60 ? 227 GLU A CG 1 ATOM 1805 C CD . GLU A 1 228 ? 31.473 16.364 26.577 1.00 31.63 ? 227 GLU A CD 1 ATOM 1806 O OE1 . GLU A 1 228 ? 32.116 17.369 26.961 1.00 31.81 ? 227 GLU A OE1 1 ATOM 1807 O OE2 . GLU A 1 228 ? 31.804 15.185 26.851 1.00 33.02 ? 227 GLU A OE2 1 ATOM 1808 N N . PHE A 1 229 ? 26.993 17.137 24.254 1.00 25.15 ? 228 PHE A N 1 ATOM 1809 C CA . PHE A 1 229 ? 25.610 17.007 24.648 1.00 23.72 ? 228 PHE A CA 1 ATOM 1810 C C . PHE A 1 229 ? 25.448 15.790 25.523 1.00 22.91 ? 228 PHE A C 1 ATOM 1811 O O . PHE A 1 229 ? 26.204 14.828 25.427 1.00 22.57 ? 228 PHE A O 1 ATOM 1812 C CB . PHE A 1 229 ? 24.674 16.967 23.422 1.00 23.63 ? 228 PHE A CB 1 ATOM 1813 C CG . PHE A 1 229 ? 24.639 18.267 22.654 1.00 24.25 ? 228 PHE A CG 1 ATOM 1814 C CD1 . PHE A 1 229 ? 23.890 19.332 23.108 1.00 24.34 ? 228 PHE A CD1 1 ATOM 1815 C CD2 . PHE A 1 229 ? 25.414 18.444 21.517 1.00 25.20 ? 228 PHE A CD2 1 ATOM 1816 C CE1 . PHE A 1 229 ? 23.873 20.535 22.421 1.00 25.46 ? 228 PHE A CE1 1 ATOM 1817 C CE2 . PHE A 1 229 ? 25.399 19.640 20.823 1.00 25.98 ? 228 PHE A CE2 1 ATOM 1818 C CZ . PHE A 1 229 ? 24.627 20.687 21.278 1.00 26.30 ? 228 PHE A CZ 1 ATOM 1819 N N . PHE A 1 230 ? 24.449 15.871 26.391 1.00 22.78 ? 229 PHE A N 1 ATOM 1820 C CA . PHE A 1 230 ? 24.136 14.833 27.351 1.00 22.08 ? 229 PHE A CA 1 ATOM 1821 C C . PHE A 1 230 ? 22.643 14.656 27.366 1.00 21.71 ? 229 PHE A C 1 ATOM 1822 O O . PHE A 1 230 ? 21.897 15.545 26.980 1.00 22.15 ? 229 PHE A O 1 ATOM 1823 C CB . PHE A 1 230 ? 24.583 15.233 28.749 1.00 22.04 ? 229 PHE A CB 1 ATOM 1824 C CG . PHE A 1 230 ? 26.032 15.576 28.849 1.00 22.44 ? 229 PHE A CG 1 ATOM 1825 C CD1 . PHE A 1 230 ? 26.976 14.592 29.143 1.00 22.03 ? 229 PHE A CD1 1 ATOM 1826 C CD2 . PHE A 1 230 ? 26.459 16.886 28.664 1.00 22.81 ? 229 PHE A CD2 1 ATOM 1827 C CE1 . PHE A 1 230 ? 28.311 14.910 29.245 1.00 22.41 ? 229 PHE A CE1 1 ATOM 1828 C CE2 . PHE A 1 230 ? 27.805 17.208 28.763 1.00 23.24 ? 229 PHE A CE2 1 ATOM 1829 C CZ . PHE A 1 230 ? 28.726 16.221 29.057 1.00 23.18 ? 229 PHE A CZ 1 ATOM 1830 N N . TRP A 1 231 ? 22.213 13.509 27.846 1.00 21.70 ? 230 TRP A N 1 ATOM 1831 C CA . TRP A 1 231 ? 20.803 13.239 27.978 1.00 22.42 ? 230 TRP A CA 1 ATOM 1832 C C . TRP A 1 231 ? 20.504 12.490 29.268 1.00 22.29 ? 230 TRP A C 1 ATOM 1833 O O . TRP A 1 231 ? 21.369 11.819 29.825 1.00 22.68 ? 230 TRP A O 1 ATOM 1834 C CB . TRP A 1 231 ? 20.341 12.433 26.784 1.00 22.63 ? 230 TRP A CB 1 ATOM 1835 C CG . TRP A 1 231 ? 21.048 11.136 26.639 1.00 22.73 ? 230 TRP A CG 1 ATOM 1836 C CD1 . TRP A 1 231 ? 22.222 10.924 26.010 1.00 22.94 ? 230 TRP A CD1 1 ATOM 1837 C CD2 . TRP A 1 231 ? 20.612 9.862 27.123 1.00 22.51 ? 230 TRP A CD2 1 ATOM 1838 N NE1 . TRP A 1 231 ? 22.563 9.593 26.079 1.00 23.24 ? 230 TRP A NE1 1 ATOM 1839 C CE2 . TRP A 1 231 ? 21.580 8.919 26.748 1.00 22.83 ? 230 TRP A CE2 1 ATOM 1840 C CE3 . TRP A 1 231 ? 19.487 9.426 27.821 1.00 22.54 ? 230 TRP A CE3 1 ATOM 1841 C CZ2 . TRP A 1 231 ? 21.466 7.560 27.056 1.00 22.77 ? 230 TRP A CZ2 1 ATOM 1842 C CZ3 . TRP A 1 231 ? 19.382 8.079 28.128 1.00 22.69 ? 230 TRP A CZ3 1 ATOM 1843 C CH2 . TRP A 1 231 ? 20.368 7.164 27.747 1.00 22.27 ? 230 TRP A CH2 1 ATOM 1844 N N . THR A 1 232 ? 19.284 12.641 29.756 1.00 22.39 ? 231 THR A N 1 ATOM 1845 C CA . THR A 1 232 ? 18.774 11.762 30.792 1.00 22.35 ? 231 THR A CA 1 ATOM 1846 C C . THR A 1 232 ? 17.268 11.504 30.587 1.00 22.94 ? 231 THR A C 1 ATOM 1847 O O . THR A 1 232 ? 16.595 12.198 29.817 1.00 22.16 ? 231 THR A O 1 ATOM 1848 C CB . THR A 1 232 ? 19.083 12.308 32.195 1.00 22.18 ? 231 THR A CB 1 ATOM 1849 O OG1 . THR A 1 232 ? 18.898 11.266 33.153 1.00 22.00 ? 231 THR A OG1 1 ATOM 1850 C CG2 . THR A 1 232 ? 18.195 13.487 32.543 1.00 22.74 ? 231 THR A CG2 1 ATOM 1851 N N . ILE A 1 233 ? 16.791 10.453 31.238 1.00 23.59 ? 232 ILE A N 1 ATOM 1852 C CA . ILE A 1 233 ? 15.390 10.114 31.286 1.00 25.06 ? 232 ILE A CA 1 ATOM 1853 C C . ILE A 1 233 ? 14.856 10.565 32.643 1.00 25.76 ? 232 ILE A C 1 ATOM 1854 O O . ILE A 1 233 ? 15.208 9.988 33.673 1.00 25.81 ? 232 ILE A O 1 ATOM 1855 C CB . ILE A 1 233 ? 15.175 8.592 31.175 1.00 25.69 ? 232 ILE A CB 1 ATOM 1856 C CG1 . ILE A 1 233 ? 15.704 8.080 29.840 1.00 25.49 ? 232 ILE A CG1 1 ATOM 1857 C CG2 . ILE A 1 233 ? 13.699 8.242 31.388 1.00 26.17 ? 232 ILE A CG2 1 ATOM 1858 C CD1 . ILE A 1 233 ? 15.230 8.872 28.633 1.00 25.75 ? 232 ILE A CD1 1 ATOM 1859 N N . LEU A 1 234 ? 14.010 11.588 32.634 1.00 26.02 ? 233 LEU A N 1 ATOM 1860 C CA . LEU A 1 234 ? 13.451 12.146 33.859 1.00 27.42 ? 233 LEU A CA 1 ATOM 1861 C C . LEU A 1 234 ? 12.142 11.435 34.189 1.00 29.17 ? 233 LEU A C 1 ATOM 1862 O O . LEU A 1 234 ? 11.163 11.580 33.469 1.00 29.83 ? 233 LEU A O 1 ATOM 1863 C CB . LEU A 1 234 ? 13.225 13.649 33.670 1.00 27.43 ? 233 LEU A CB 1 ATOM 1864 C CG . LEU A 1 234 ? 12.795 14.459 34.881 1.00 28.07 ? 233 LEU A CG 1 ATOM 1865 C CD1 . LEU A 1 234 ? 13.767 14.218 36.021 1.00 28.55 ? 233 LEU A CD1 1 ATOM 1866 C CD2 . LEU A 1 234 ? 12.735 15.937 34.535 1.00 28.12 ? 233 LEU A CD2 1 ATOM 1867 N N . LYS A 1 235 ? 12.118 10.657 35.264 1.00 31.01 ? 234 LYS A N 1 ATOM 1868 C CA . LYS A 1 235 ? 10.917 9.890 35.592 1.00 32.99 ? 234 LYS A CA 1 ATOM 1869 C C . LYS A 1 235 ? 9.754 10.792 35.994 1.00 33.22 ? 234 LYS A C 1 ATOM 1870 O O . LYS A 1 235 ? 9.965 11.908 36.458 1.00 32.83 ? 234 LYS A O 1 ATOM 1871 C CB . LYS A 1 235 ? 11.184 8.879 36.716 1.00 34.60 ? 234 LYS A CB 1 ATOM 1872 C CG . LYS A 1 235 ? 12.153 7.766 36.351 1.00 35.05 ? 234 LYS A CG 1 ATOM 1873 C CD . LYS A 1 235 ? 11.644 6.854 35.241 1.00 36.28 ? 234 LYS A CD 1 ATOM 1874 C CE . LYS A 1 235 ? 10.473 5.997 35.719 1.00 39.28 ? 234 LYS A CE 1 ATOM 1875 N NZ . LYS A 1 235 ? 9.896 5.103 34.671 1.00 39.66 ? 234 LYS A NZ 1 ATOM 1876 N N . PRO A 1 236 ? 8.518 10.309 35.806 1.00 33.75 ? 235 PRO A N 1 ATOM 1877 C CA . PRO A 1 236 ? 7.346 11.031 36.296 1.00 35.29 ? 235 PRO A CA 1 ATOM 1878 C C . PRO A 1 236 ? 7.513 11.471 37.744 1.00 36.29 ? 235 PRO A C 1 ATOM 1879 O O . PRO A 1 236 ? 7.915 10.670 38.589 1.00 36.94 ? 235 PRO A O 1 ATOM 1880 C CB . PRO A 1 236 ? 6.220 9.994 36.193 1.00 36.43 ? 235 PRO A CB 1 ATOM 1881 C CG . PRO A 1 236 ? 6.849 8.724 35.715 1.00 35.10 ? 235 PRO A CG 1 ATOM 1882 C CD . PRO A 1 236 ? 8.138 9.088 35.082 1.00 33.24 ? 235 PRO A CD 1 ATOM 1883 N N . ASN A 1 237 ? 7.216 12.738 38.016 1.00 37.41 ? 236 ASN A N 1 ATOM 1884 C CA . ASN A 1 237 ? 7.315 13.330 39.366 1.00 38.50 ? 236 ASN A CA 1 ATOM 1885 C C . ASN A 1 237 ? 8.708 13.607 39.920 1.00 36.60 ? 236 ASN A C 1 ATOM 1886 O O . ASN A 1 237 ? 8.840 14.078 41.043 1.00 38.17 ? 236 ASN A O 1 ATOM 1887 C CB . ASN A 1 237 ? 6.519 12.527 40.396 1.00 41.30 ? 236 ASN A CB 1 ATOM 1888 C CG . ASN A 1 237 ? 5.324 13.290 40.899 1.00 44.88 ? 236 ASN A CG 1 ATOM 1889 O OD1 . ASN A 1 237 ? 4.422 13.605 40.124 1.00 46.89 ? 236 ASN A OD1 1 ATOM 1890 N ND2 . ASN A 1 237 ? 5.310 13.609 42.194 1.00 46.76 ? 236 ASN A ND2 1 ATOM 1891 N N . ASP A 1 238 ? 9.739 13.328 39.143 1.00 33.80 ? 237 ASP A N 1 ATOM 1892 C CA . ASP A 1 238 ? 11.076 13.717 39.514 1.00 32.07 ? 237 ASP A CA 1 ATOM 1893 C C . ASP A 1 238 ? 11.335 15.086 38.913 1.00 31.88 ? 237 ASP A C 1 ATOM 1894 O O . ASP A 1 238 ? 10.634 15.500 37.992 1.00 31.56 ? 237 ASP A O 1 ATOM 1895 C CB . ASP A 1 238 ? 12.087 12.708 38.977 1.00 30.17 ? 237 ASP A CB 1 ATOM 1896 C CG . ASP A 1 238 ? 13.456 12.892 39.563 1.00 28.68 ? 237 ASP A CG 1 ATOM 1897 O OD1 . ASP A 1 238 ? 13.563 13.359 40.714 1.00 28.67 ? 237 ASP A OD1 1 ATOM 1898 O OD2 . ASP A 1 238 ? 14.425 12.563 38.873 1.00 26.97 ? 237 ASP A OD2 1 ATOM 1899 N N . ALA A 1 239 ? 12.331 15.788 39.445 1.00 31.55 ? 238 ALA A N 1 ATOM 1900 C CA . ALA A 1 239 ? 12.722 17.082 38.906 1.00 31.60 ? 238 ALA A CA 1 ATOM 1901 C C . ALA A 1 239 ? 14.162 17.027 38.477 1.00 29.89 ? 238 ALA A C 1 ATOM 1902 O O . ALA A 1 239 ? 14.897 16.143 38.889 1.00 29.73 ? 238 ALA A O 1 ATOM 1903 C CB . ALA A 1 239 ? 12.507 18.192 39.940 1.00 33.15 ? 238 ALA A CB 1 ATOM 1904 N N . ILE A 1 240 ? 14.537 17.965 37.615 1.00 29.54 ? 239 ILE A N 1 ATOM 1905 C CA . ILE A 1 240 ? 15.904 18.125 37.153 1.00 28.55 ? 239 ILE A CA 1 ATOM 1906 C C . ILE A 1 240 ? 16.309 19.565 37.469 1.00 29.01 ? 239 ILE A C 1 ATOM 1907 O O . ILE A 1 240 ? 15.598 20.497 37.106 1.00 30.32 ? 239 ILE A O 1 ATOM 1908 C CB . ILE A 1 240 ? 16.059 17.814 35.643 1.00 27.76 ? 239 ILE A CB 1 ATOM 1909 C CG1 . ILE A 1 240 ? 17.537 17.789 35.250 1.00 27.09 ? 239 ILE A CG1 1 ATOM 1910 C CG2 . ILE A 1 240 ? 15.316 18.839 34.787 1.00 28.55 ? 239 ILE A CG2 1 ATOM 1911 C CD1 . ILE A 1 240 ? 17.817 17.273 33.843 1.00 26.60 ? 239 ILE A CD1 1 ATOM 1912 N N . ASN A 1 241 ? 17.438 19.733 38.152 1.00 28.03 ? 240 ASN A N 1 ATOM 1913 C CA . ASN A 1 241 ? 17.881 21.042 38.600 1.00 28.70 ? 240 ASN A CA 1 ATOM 1914 C C . ASN A 1 241 ? 19.220 21.396 37.973 1.00 27.51 ? 240 ASN A C 1 ATOM 1915 O O . ASN A 1 241 ? 20.184 20.639 38.077 1.00 26.52 ? 240 ASN A O 1 ATOM 1916 C CB . ASN A 1 241 ? 17.971 21.081 40.139 1.00 29.45 ? 240 ASN A CB 1 ATOM 1917 C CG . ASN A 1 241 ? 16.776 20.416 40.814 1.00 30.15 ? 240 ASN A CG 1 ATOM 1918 O OD1 . ASN A 1 241 ? 15.643 20.920 40.761 1.00 30.75 ? 240 ASN A OD1 1 ATOM 1919 N ND2 . ASN A 1 241 ? 17.021 19.275 41.453 1.00 30.02 ? 240 ASN A ND2 1 ATOM 1920 N N . PHE A 1 242 ? 19.262 22.544 37.313 1.00 27.84 ? 241 PHE A N 1 ATOM 1921 C CA . PHE A 1 242 ? 20.444 23.001 36.615 1.00 27.85 ? 241 PHE A CA 1 ATOM 1922 C C . PHE A 1 242 ? 20.986 24.209 37.333 1.00 28.90 ? 241 PHE A C 1 ATOM 1923 O O . PHE A 1 242 ? 20.230 25.126 37.668 1.00 30.30 ? 241 PHE A O 1 ATOM 1924 C CB . PHE A 1 242 ? 20.101 23.434 35.192 1.00 28.51 ? 241 PHE A CB 1 ATOM 1925 C CG . PHE A 1 242 ? 19.646 22.318 34.289 1.00 27.53 ? 241 PHE A CG 1 ATOM 1926 C CD1 . PHE A 1 242 ? 20.568 21.540 33.614 1.00 26.76 ? 241 PHE A CD1 1 ATOM 1927 C CD2 . PHE A 1 242 ? 18.299 22.078 34.088 1.00 27.93 ? 241 PHE A CD2 1 ATOM 1928 C CE1 . PHE A 1 242 ? 20.156 20.522 32.775 1.00 26.39 ? 241 PHE A CE1 1 ATOM 1929 C CE2 . PHE A 1 242 ? 17.875 21.069 33.239 1.00 27.53 ? 241 PHE A CE2 1 ATOM 1930 C CZ . PHE A 1 242 ? 18.804 20.289 32.582 1.00 26.76 ? 241 PHE A CZ 1 ATOM 1931 N N . GLU A 1 243 ? 22.292 24.212 37.572 1.00 28.75 ? 242 GLU A N 1 ATOM 1932 C CA . GLU A 1 243 ? 22.987 25.403 38.043 1.00 29.31 ? 242 GLU A CA 1 ATOM 1933 C C . GLU A 1 243 ? 24.170 25.646 37.122 1.00 28.44 ? 242 GLU A C 1 ATOM 1934 O O . GLU A 1 243 ? 24.879 24.699 36.780 1.00 26.93 ? 242 GLU A O 1 ATOM 1935 C CB . GLU A 1 243 ? 23.442 25.235 39.497 1.00 30.46 ? 242 GLU A CB 1 ATOM 1936 C CG . GLU A 1 243 ? 24.139 26.457 40.081 1.00 32.66 ? 242 GLU A CG 1 ATOM 1937 C CD . GLU A 1 243 ? 24.399 26.349 41.583 1.00 34.52 ? 242 GLU A CD 1 ATOM 1938 O OE1 . GLU A 1 243 ? 23.455 26.022 42.349 1.00 35.28 ? 242 GLU A OE1 1 ATOM 1939 O OE2 . GLU A 1 243 ? 25.550 26.626 42.005 1.00 35.64 ? 242 GLU A OE2 1 ATOM 1940 N N . SER A 1 244 ? 24.374 26.902 36.711 1.00 28.72 ? 243 SER A N 1 ATOM 1941 C CA . SER A 1 244 ? 25.500 27.243 35.840 1.00 28.63 ? 243 SER A CA 1 ATOM 1942 C C . SER A 1 244 ? 25.862 28.710 35.898 1.00 30.03 ? 243 SER A C 1 ATOM 1943 O O . SER A 1 244 ? 24.987 29.549 36.039 1.00 31.26 ? 243 SER A O 1 ATOM 1944 C CB . SER A 1 244 ? 25.189 26.886 34.388 1.00 28.30 ? 243 SER A CB 1 ATOM 1945 O OG . SER A 1 244 ? 26.337 27.052 33.561 1.00 28.71 ? 243 SER A OG 1 ATOM 1946 N N . ASN A 1 245 ? 27.155 29.014 35.783 1.00 30.29 ? 244 ASN A N 1 ATOM 1947 C CA . ASN A 1 245 ? 27.593 30.382 35.543 1.00 32.25 ? 244 ASN A CA 1 ATOM 1948 C C . ASN A 1 245 ? 28.244 30.545 34.166 1.00 32.31 ? 244 ASN A C 1 ATOM 1949 O O . ASN A 1 245 ? 29.061 31.434 33.968 1.00 33.71 ? 244 ASN A O 1 ATOM 1950 C CB . ASN A 1 245 ? 28.521 30.871 36.661 1.00 33.49 ? 244 ASN A CB 1 ATOM 1951 C CG . ASN A 1 245 ? 29.800 30.065 36.760 1.00 33.13 ? 244 ASN A CG 1 ATOM 1952 O OD1 . ASN A 1 245 ? 29.888 28.937 36.265 1.00 32.65 ? 244 ASN A OD1 1 ATOM 1953 N ND2 . ASN A 1 245 ? 30.798 30.638 37.405 1.00 34.00 ? 244 ASN A ND2 1 ATOM 1954 N N . GLY A 1 246 ? 27.878 29.689 33.217 1.00 31.27 ? 245 GLY A N 1 ATOM 1955 C CA . GLY A 1 246 ? 28.365 29.820 31.845 1.00 31.54 ? 245 GLY A CA 1 ATOM 1956 C C . GLY A 1 246 ? 28.476 28.498 31.119 1.00 30.24 ? 245 GLY A C 1 ATOM 1957 O O . GLY A 1 246 ? 28.501 27.447 31.745 1.00 29.33 ? 245 GLY A O 1 ATOM 1958 N N . ASN A 1 247 ? 28.528 28.591 29.789 1.00 30.66 ? 246 ASN A N 1 ATOM 1959 C CA . ASN A 1 247 ? 28.800 27.486 28.865 1.00 29.65 ? 246 ASN A CA 1 ATOM 1960 C C . ASN A 1 247 ? 27.667 26.465 28.784 1.00 28.74 ? 246 ASN A C 1 ATOM 1961 O O . ASN A 1 247 ? 27.851 25.351 28.279 1.00 27.27 ? 246 ASN A O 1 ATOM 1962 C CB . ASN A 1 247 ? 30.136 26.805 29.191 1.00 29.30 ? 246 ASN A CB 1 ATOM 1963 C CG . ASN A 1 247 ? 31.295 27.782 29.243 1.00 30.34 ? 246 ASN A CG 1 ATOM 1964 O OD1 . ASN A 1 247 ? 31.437 28.546 30.193 1.00 30.74 ? 246 ASN A OD1 1 ATOM 1965 N ND2 . ASN A 1 247 ? 32.139 27.745 28.230 1.00 31.00 ? 246 ASN A ND2 1 ATOM 1966 N N . PHE A 1 248 ? 26.489 26.880 29.242 1.00 29.03 ? 247 PHE A N 1 ATOM 1967 C CA . PHE A 1 248 ? 25.342 26.007 29.384 1.00 28.43 ? 247 PHE A CA 1 ATOM 1968 C C . PHE A 1 248 ? 24.502 26.061 28.121 1.00 29.01 ? 247 PHE A C 1 ATOM 1969 O O . PHE A 1 248 ? 24.089 27.132 27.702 1.00 30.03 ? 247 PHE A O 1 ATOM 1970 C CB . PHE A 1 248 ? 24.513 26.450 30.602 1.00 28.92 ? 247 PHE A CB 1 ATOM 1971 C CG . PHE A 1 248 ? 23.294 25.594 30.881 1.00 28.34 ? 247 PHE A CG 1 ATOM 1972 C CD1 . PHE A 1 248 ? 23.304 24.228 30.672 1.00 27.21 ? 247 PHE A CD1 1 ATOM 1973 C CD2 . PHE A 1 248 ? 22.131 26.178 31.376 1.00 29.10 ? 247 PHE A CD2 1 ATOM 1974 C CE1 . PHE A 1 248 ? 22.174 23.462 30.937 1.00 26.86 ? 247 PHE A CE1 1 ATOM 1975 C CE2 . PHE A 1 248 ? 21.010 25.420 31.649 1.00 28.45 ? 247 PHE A CE2 1 ATOM 1976 C CZ . PHE A 1 248 ? 21.033 24.060 31.434 1.00 27.36 ? 247 PHE A CZ 1 ATOM 1977 N N . ILE A 1 249 ? 24.262 24.907 27.503 1.00 28.15 ? 248 ILE A N 1 ATOM 1978 C CA . ILE A 1 249 ? 23.301 24.845 26.426 1.00 28.74 ? 248 ILE A CA 1 ATOM 1979 C C . ILE A 1 249 ? 22.048 24.237 27.034 1.00 27.65 ? 248 ILE A C 1 ATOM 1980 O O . ILE A 1 249 ? 21.969 23.027 27.260 1.00 26.25 ? 248 ILE A O 1 ATOM 1981 C CB . ILE A 1 249 ? 23.806 24.035 25.221 1.00 29.05 ? 248 ILE A CB 1 ATOM 1982 C CG1 . ILE A 1 249 ? 25.258 24.397 24.886 1.00 29.95 ? 248 ILE A CG1 1 ATOM 1983 C CG2 . ILE A 1 249 ? 22.924 24.306 24.020 1.00 29.94 ? 248 ILE A CG2 1 ATOM 1984 C CD1 . ILE A 1 249 ? 25.501 25.862 24.595 1.00 31.53 ? 248 ILE A CD1 1 ATOM 1985 N N . ALA A 1 250 ? 21.082 25.103 27.331 1.00 28.19 ? 249 ALA A N 1 ATOM 1986 C CA . ALA A 1 250 ? 19.933 24.726 28.141 1.00 27.58 ? 249 ALA A CA 1 ATOM 1987 C C . ALA A 1 250 ? 18.873 24.013 27.330 1.00 27.28 ? 249 ALA A C 1 ATOM 1988 O O . ALA A 1 250 ? 18.739 24.258 26.133 1.00 27.16 ? 249 ALA A O 1 ATOM 1989 C CB . ALA A 1 250 ? 19.338 25.948 28.808 1.00 29.20 ? 249 ALA A CB 1 ATOM 1990 N N . PRO A 1 251 ? 18.116 23.109 27.984 1.00 26.97 ? 250 PRO A N 1 ATOM 1991 C CA . PRO A 1 251 ? 16.935 22.537 27.347 1.00 27.29 ? 250 PRO A CA 1 ATOM 1992 C C . PRO A 1 251 ? 15.968 23.633 26.938 1.00 29.75 ? 250 PRO A C 1 ATOM 1993 O O . PRO A 1 251 ? 15.856 24.651 27.635 1.00 30.06 ? 250 PRO A O 1 ATOM 1994 C CB . PRO A 1 251 ? 16.289 21.704 28.463 1.00 26.49 ? 250 PRO A CB 1 ATOM 1995 C CG . PRO A 1 251 ? 17.379 21.446 29.433 1.00 25.65 ? 250 PRO A CG 1 ATOM 1996 C CD . PRO A 1 251 ? 18.267 22.648 29.374 1.00 26.01 ? 250 PRO A CD 1 ATOM 1997 N N . GLU A 1 252 ? 15.309 23.440 25.802 1.00 31.20 ? 251 GLU A N 1 ATOM 1998 C CA . GLU A 1 252 ? 14.068 24.136 25.529 1.00 34.11 ? 251 GLU A CA 1 ATOM 1999 C C . GLU A 1 252 ? 12.969 23.085 25.461 1.00 32.90 ? 251 GLU A C 1 ATOM 2000 O O . GLU A 1 252 ? 12.034 23.123 26.250 1.00 33.37 ? 251 GLU A O 1 ATOM 2001 C CB . GLU A 1 252 ? 14.157 24.942 24.245 1.00 36.88 ? 251 GLU A CB 1 ATOM 2002 C CG . GLU A 1 252 ? 12.964 25.847 24.017 1.00 40.38 ? 251 GLU A CG 1 ATOM 2003 C CD . GLU A 1 252 ? 13.177 26.793 22.852 1.00 43.74 ? 251 GLU A CD 1 ATOM 2004 O OE1 . GLU A 1 252 ? 14.243 27.446 22.790 1.00 45.29 ? 251 GLU A OE1 1 ATOM 2005 O OE2 . GLU A 1 252 ? 12.277 26.885 21.994 1.00 46.62 ? 251 GLU A OE2 1 ATOM 2006 N N . ASN A 1 253 ? 13.117 22.131 24.544 1.00 31.28 ? 252 ASN A N 1 ATOM 2007 C CA . ASN A 1 253 ? 12.158 21.051 24.382 1.00 30.46 ? 252 ASN A CA 1 ATOM 2008 C C . ASN A 1 253 ? 12.718 19.719 24.835 1.00 28.58 ? 252 ASN A C 1 ATOM 2009 O O . ASN A 1 253 ? 13.896 19.434 24.625 1.00 27.74 ? 252 ASN A O 1 ATOM 2010 C CB . ASN A 1 253 ? 11.726 20.936 22.924 1.00 30.73 ? 252 ASN A CB 1 ATOM 2011 C CG . ASN A 1 253 ? 11.302 22.262 22.351 1.00 32.60 ? 252 ASN A CG 1 ATOM 2012 O OD1 . ASN A 1 253 ? 10.577 23.016 22.994 1.00 33.61 ? 252 ASN A OD1 1 ATOM 2013 N ND2 . ASN A 1 253 ? 11.771 22.568 21.147 1.00 33.19 ? 252 ASN A ND2 1 ATOM 2014 N N . ALA A 1 254 ? 11.845 18.914 25.435 1.00 28.12 ? 253 ALA A N 1 ATOM 2015 C CA . ALA A 1 254 ? 12.117 17.524 25.790 1.00 26.60 ? 253 ALA A CA 1 ATOM 2016 C C . ALA A 1 254 ? 11.083 16.614 25.116 1.00 26.47 ? 253 ALA A C 1 ATOM 2017 O O . ALA A 1 254 ? 10.113 17.092 24.536 1.00 26.74 ? 253 ALA A O 1 ATOM 2018 C CB . ALA A 1 254 ? 12.061 17.362 27.306 1.00 26.54 ? 253 ALA A CB 1 ATOM 2019 N N . TYR A 1 255 ? 11.290 15.303 25.214 1.00 25.67 ? 254 TYR A N 1 ATOM 2020 C CA . TYR A 1 255 ? 10.437 14.327 24.533 1.00 26.11 ? 254 TYR A CA 1 ATOM 2021 C C . TYR A 1 255 ? 9.735 13.406 25.519 1.00 26.36 ? 254 TYR A C 1 ATOM 2022 O O . TYR A 1 255 ? 10.380 12.729 26.316 1.00 27.30 ? 254 TYR A O 1 ATOM 2023 C CB . TYR A 1 255 ? 11.272 13.483 23.579 1.00 25.58 ? 254 TYR A CB 1 ATOM 2024 C CG . TYR A 1 255 ? 11.925 14.253 22.446 1.00 25.99 ? 254 TYR A CG 1 ATOM 2025 C CD1 . TYR A 1 255 ? 13.178 14.845 22.600 1.00 24.90 ? 254 TYR A CD1 1 ATOM 2026 C CD2 . TYR A 1 255 ? 11.289 14.379 21.214 1.00 27.35 ? 254 TYR A CD2 1 ATOM 2027 C CE1 . TYR A 1 255 ? 13.773 15.531 21.560 1.00 25.64 ? 254 TYR A CE1 1 ATOM 2028 C CE2 . TYR A 1 255 ? 11.876 15.075 20.164 1.00 27.73 ? 254 TYR A CE2 1 ATOM 2029 C CZ . TYR A 1 255 ? 13.116 15.648 20.344 1.00 27.07 ? 254 TYR A CZ 1 ATOM 2030 O OH . TYR A 1 255 ? 13.683 16.329 19.301 1.00 27.92 ? 254 TYR A OH 1 ATOM 2031 N N . LYS A 1 256 ? 8.413 13.377 25.460 1.00 27.53 ? 255 LYS A N 1 ATOM 2032 C CA . LYS A 1 256 ? 7.615 12.456 26.264 1.00 27.60 ? 255 LYS A CA 1 ATOM 2033 C C . LYS A 1 256 ? 7.587 11.100 25.577 1.00 26.34 ? 255 LYS A C 1 ATOM 2034 O O . LYS A 1 256 ? 7.160 11.005 24.428 1.00 26.91 ? 255 LYS A O 1 ATOM 2035 C CB . LYS A 1 256 ? 6.179 12.975 26.415 1.00 29.70 ? 255 LYS A CB 1 ATOM 2036 C CG . LYS A 1 256 ? 6.057 14.320 27.118 1.00 31.02 ? 255 LYS A CG 1 ATOM 2037 C CD . LYS A 1 256 ? 4.683 14.527 27.756 1.00 32.93 ? 255 LYS A CD 1 ATOM 2038 C CE . LYS A 1 256 ? 3.568 14.489 26.725 1.00 34.72 ? 255 LYS A CE 1 ATOM 2039 N NZ . LYS A 1 256 ? 2.267 15.007 27.262 1.00 37.61 ? 255 LYS A NZ 1 ATOM 2040 N N . ILE A 1 257 ? 8.045 10.059 26.267 1.00 31.36 ? 256 ILE A N 1 ATOM 2041 C CA . ILE A 1 257 ? 7.994 8.708 25.720 1.00 31.10 ? 256 ILE A CA 1 ATOM 2042 C C . ILE A 1 257 ? 6.563 8.223 25.847 1.00 32.22 ? 256 ILE A C 1 ATOM 2043 O O . ILE A 1 257 ? 6.102 7.846 26.925 1.00 33.63 ? 256 ILE A O 1 ATOM 2044 C CB . ILE A 1 257 ? 8.965 7.742 26.413 1.00 32.01 ? 256 ILE A CB 1 ATOM 2045 C CG1 . ILE A 1 257 ? 10.418 8.145 26.098 1.00 31.42 ? 256 ILE A CG1 1 ATOM 2046 C CG2 . ILE A 1 257 ? 8.702 6.303 25.979 1.00 32.59 ? 256 ILE A CG2 1 ATOM 2047 C CD1 . ILE A 1 257 ? 11.420 7.665 27.126 1.00 32.84 ? 256 ILE A CD1 1 ATOM 2048 N N . VAL A 1 258 ? 5.862 8.229 24.725 1.00 31.72 ? 257 VAL A N 1 ATOM 2049 C CA . VAL A 1 258 ? 4.445 7.972 24.738 1.00 33.21 ? 257 VAL A CA 1 ATOM 2050 C C . VAL A 1 258 ? 4.145 6.483 24.526 1.00 34.62 ? 257 VAL A C 1 ATOM 2051 O O . VAL A 1 258 ? 3.237 5.952 25.145 1.00 36.09 ? 257 VAL A O 1 ATOM 2052 C CB . VAL A 1 258 ? 3.756 8.886 23.708 1.00 32.63 ? 257 VAL A CB 1 ATOM 2053 C CG1 . VAL A 1 258 ? 2.389 8.350 23.321 1.00 34.40 ? 257 VAL A CG1 1 ATOM 2054 C CG2 . VAL A 1 258 ? 3.663 10.295 24.286 1.00 32.07 ? 257 VAL A CG2 1 ATOM 2055 N N . LYS A 1 259 ? 4.920 5.818 23.674 1.00 34.16 ? 258 LYS A N 1 ATOM 2056 C CA . LYS A 1 259 ? 4.746 4.394 23.401 1.00 35.70 ? 258 LYS A CA 1 ATOM 2057 C C . LYS A 1 259 ? 6.079 3.645 23.262 1.00 35.88 ? 258 LYS A C 1 ATOM 2058 O O . LYS A 1 259 ? 7.033 4.156 22.670 1.00 33.85 ? 258 LYS A O 1 ATOM 2059 C CB . LYS A 1 259 ? 3.959 4.217 22.111 1.00 35.51 ? 258 LYS A CB 1 ATOM 2060 C CG . LYS A 1 259 ? 3.740 2.763 21.740 1.00 36.91 ? 258 LYS A CG 1 ATOM 2061 C CD . LYS A 1 259 ? 2.832 2.615 20.537 1.00 37.34 ? 258 LYS A CD 1 ATOM 2062 C CE . LYS A 1 259 ? 2.430 1.160 20.358 1.00 39.25 ? 258 LYS A CE 1 ATOM 2063 N NZ . LYS A 1 259 ? 2.214 0.863 18.927 1.00 39.01 ? 258 LYS A NZ 1 ATOM 2064 N N . LYS A 1 260 ? 6.118 2.416 23.764 1.00 38.50 ? 259 LYS A N 1 ATOM 2065 C CA . LYS A 1 260 ? 7.268 1.546 23.576 1.00 39.76 ? 259 LYS A CA 1 ATOM 2066 C C . LYS A 1 260 ? 6.858 0.205 23.001 1.00 42.53 ? 259 LYS A C 1 ATOM 2067 O O . LYS A 1 260 ? 5.762 -0.300 23.280 1.00 44.41 ? 259 LYS A O 1 ATOM 2068 C CB . LYS A 1 260 ? 7.997 1.342 24.895 1.00 41.45 ? 259 LYS A CB 1 ATOM 2069 C CG . LYS A 1 260 ? 8.702 2.598 25.390 1.00 40.35 ? 259 LYS A CG 1 ATOM 2070 C CD . LYS A 1 260 ? 8.920 2.546 26.885 1.00 42.74 ? 259 LYS A CD 1 ATOM 2071 C CE . LYS A 1 260 ? 10.154 1.735 27.238 1.00 44.81 ? 259 LYS A CE 1 ATOM 2072 N NZ . LYS A 1 260 ? 11.399 2.530 27.010 1.00 43.99 ? 259 LYS A NZ 1 ATOM 2073 N N . GLY A 1 261 ? 7.744 -0.362 22.186 1.00 43.40 ? 260 GLY A N 1 ATOM 2074 C CA . GLY A 1 261 ? 7.533 -1.677 21.596 1.00 46.14 ? 260 GLY A CA 1 ATOM 2075 C C . GLY A 1 261 ? 8.742 -2.147 20.813 1.00 46.92 ? 260 GLY A C 1 ATOM 2076 O O . GLY A 1 261 ? 9.851 -1.626 20.980 1.00 46.37 ? 260 GLY A O 1 ATOM 2077 N N . ASP A 1 262 ? 8.533 -3.150 19.967 1.00 49.52 ? 261 ASP A N 1 ATOM 2078 C CA . ASP A 1 262 ? 9.584 -3.602 19.067 1.00 49.28 ? 261 ASP A CA 1 ATOM 2079 C C . ASP A 1 262 ? 9.709 -2.603 17.927 1.00 45.87 ? 261 ASP A C 1 ATOM 2080 O O . ASP A 1 262 ? 8.736 -2.226 17.260 1.00 46.42 ? 261 ASP A O 1 ATOM 2081 C CB . ASP A 1 262 ? 9.350 -5.029 18.552 1.00 51.95 ? 261 ASP A CB 1 ATOM 2082 C CG . ASP A 1 262 ? 9.987 -6.098 19.458 1.00 55.51 ? 261 ASP A CG 1 ATOM 2083 O OD1 . ASP A 1 262 ? 11.190 -5.966 19.804 1.00 55.50 ? 261 ASP A OD1 1 ATOM 2084 O OD2 . ASP A 1 262 ? 9.284 -7.075 19.818 1.00 59.10 ? 261 ASP A OD2 1 ATOM 2085 N N . SER A 1 263 ? 10.930 -2.141 17.765 1.00 42.83 ? 262 SER A N 1 ATOM 2086 C CA . SER A 1 263 ? 11.287 -1.221 16.730 1.00 39.67 ? 262 SER A CA 1 ATOM 2087 C C . SER A 1 263 ? 12.744 -1.518 16.469 1.00 38.73 ? 262 SER A C 1 ATOM 2088 O O . SER A 1 263 ? 13.341 -2.388 17.115 1.00 39.52 ? 262 SER A O 1 ATOM 2089 C CB . SER A 1 263 ? 11.095 0.214 17.215 1.00 38.56 ? 262 SER A CB 1 ATOM 2090 O OG . SER A 1 263 ? 11.696 1.143 16.342 1.00 37.52 ? 262 SER A OG 1 ATOM 2091 N N . THR A 1 264 ? 13.321 -0.811 15.516 1.00 36.71 ? 263 THR A N 1 ATOM 2092 C CA . THR A 1 264 ? 14.734 -0.944 15.257 1.00 35.78 ? 263 THR A CA 1 ATOM 2093 C C . THR A 1 264 ? 15.226 0.319 14.582 1.00 34.10 ? 263 THR A C 1 ATOM 2094 O O . THR A 1 264 ? 14.424 1.078 14.035 1.00 33.14 ? 263 THR A O 1 ATOM 2095 C CB . THR A 1 264 ? 15.023 -2.198 14.396 1.00 35.82 ? 263 THR A CB 1 ATOM 2096 O OG1 . THR A 1 264 ? 16.420 -2.501 14.452 1.00 36.29 ? 263 THR A OG1 1 ATOM 2097 C CG2 . THR A 1 264 ? 14.587 -2.007 12.952 1.00 34.67 ? 263 THR A CG2 1 ATOM 2098 N N . ILE A 1 265 ? 16.534 0.553 14.660 1.00 33.90 ? 264 ILE A N 1 ATOM 2099 C CA . ILE A 1 265 ? 17.180 1.547 13.826 1.00 33.03 ? 264 ILE A CA 1 ATOM 2100 C C . ILE A 1 265 ? 17.905 0.790 12.730 1.00 33.25 ? 264 ILE A C 1 ATOM 2101 O O . ILE A 1 265 ? 18.929 0.155 12.976 1.00 34.00 ? 264 ILE A O 1 ATOM 2102 C CB . ILE A 1 265 ? 18.183 2.428 14.579 1.00 33.24 ? 264 ILE A CB 1 ATOM 2103 C CG1 . ILE A 1 265 ? 17.479 3.200 15.687 1.00 33.01 ? 264 ILE A CG1 1 ATOM 2104 C CG2 . ILE A 1 265 ? 18.843 3.411 13.612 1.00 33.12 ? 264 ILE A CG2 1 ATOM 2105 C CD1 . ILE A 1 265 ? 18.417 4.020 16.547 1.00 33.71 ? 264 ILE A CD1 1 ATOM 2106 N N . MET A 1 266 ? 17.349 0.878 11.531 1.00 32.67 ? 265 MET A N 1 ATOM 2107 C CA . MET A 1 266 ? 17.936 0.319 10.329 1.00 33.50 ? 265 MET A CA 1 ATOM 2108 C C . MET A 1 266 ? 18.904 1.291 9.686 1.00 33.90 ? 265 MET A C 1 ATOM 2109 O O . MET A 1 266 ? 18.668 2.497 9.656 1.00 33.47 ? 265 MET A O 1 ATOM 2110 C CB . MET A 1 266 ? 16.852 0.042 9.293 1.00 33.13 ? 265 MET A CB 1 ATOM 2111 C CG . MET A 1 266 ? 16.353 -1.371 9.281 1.00 33.79 ? 265 MET A CG 1 ATOM 2112 S SD . MET A 1 266 ? 15.295 -1.586 7.849 1.00 33.75 ? 265 MET A SD 1 ATOM 2113 C CE . MET A 1 266 ? 14.623 -3.167 8.328 1.00 34.59 ? 265 MET A CE 1 ATOM 2114 N N . LYS A 1 267 ? 19.974 0.747 9.132 1.00 35.17 ? 266 LYS A N 1 ATOM 2115 C CA . LYS A 1 267 ? 20.867 1.528 8.293 1.00 35.95 ? 266 LYS A CA 1 ATOM 2116 C C . LYS A 1 267 ? 20.566 1.159 6.852 1.00 35.18 ? 266 LYS A C 1 ATOM 2117 O O . LYS A 1 267 ? 20.612 -0.018 6.484 1.00 34.63 ? 266 LYS A O 1 ATOM 2118 C CB . LYS A 1 267 ? 22.324 1.248 8.651 1.00 37.67 ? 266 LYS A CB 1 ATOM 2119 C CG . LYS A 1 267 ? 22.626 1.405 10.121 1.00 38.52 ? 266 LYS A CG 1 ATOM 2120 C CD . LYS A 1 267 ? 22.487 2.849 10.581 1.00 39.54 ? 266 LYS A CD 1 ATOM 2121 C CE . LYS A 1 267 ? 23.699 3.684 10.177 1.00 42.02 ? 266 LYS A CE 1 ATOM 2122 N NZ . LYS A 1 267 ? 23.769 5.007 10.873 1.00 42.54 ? 266 LYS A NZ 1 ATOM 2123 N N . SER A 1 268 ? 20.217 2.158 6.049 1.00 34.97 ? 267 SER A N 1 ATOM 2124 C CA . SER A 1 268 ? 19.921 1.921 4.643 1.00 35.41 ? 267 SER A CA 1 ATOM 2125 C C . SER A 1 268 ? 20.015 3.200 3.840 1.00 36.39 ? 267 SER A C 1 ATOM 2126 O O . SER A 1 268 ? 19.839 4.289 4.373 1.00 36.16 ? 267 SER A O 1 ATOM 2127 C CB . SER A 1 268 ? 18.520 1.322 4.487 1.00 34.82 ? 267 SER A CB 1 ATOM 2128 O OG . SER A 1 268 ? 18.221 1.142 3.125 1.00 35.62 ? 267 SER A OG 1 ATOM 2129 N N . GLU A 1 269 ? 20.304 3.056 2.549 1.00 38.03 ? 268 GLU A N 1 ATOM 2130 C CA . GLU A 1 269 ? 20.342 4.195 1.626 1.00 39.68 ? 268 GLU A CA 1 ATOM 2131 C C . GLU A 1 269 ? 18.980 4.457 0.978 1.00 39.31 ? 268 GLU A C 1 ATOM 2132 O O . GLU A 1 269 ? 18.722 5.558 0.500 1.00 40.60 ? 268 GLU A O 1 ATOM 2133 C CB . GLU A 1 269 ? 21.428 3.978 0.568 1.00 41.38 ? 268 GLU A CB 1 ATOM 2134 C CG . GLU A 1 269 ? 22.834 3.938 1.162 1.00 42.38 ? 268 GLU A CG 1 ATOM 2135 C CD . GLU A 1 269 ? 23.198 5.219 1.906 1.00 43.15 ? 268 GLU A CD 1 ATOM 2136 O OE1 . GLU A 1 269 ? 23.342 6.267 1.239 1.00 45.12 ? 268 GLU A OE1 1 ATOM 2137 O OE2 . GLU A 1 269 ? 23.325 5.182 3.152 1.00 41.51 ? 268 GLU A OE2 1 ATOM 2138 N N . LEU A 1 270 ? 18.101 3.460 1.027 1.00 38.29 ? 269 LEU A N 1 ATOM 2139 C CA . LEU A 1 270 ? 16.792 3.517 0.374 1.00 38.98 ? 269 LEU A CA 1 ATOM 2140 C C . LEU A 1 270 ? 15.876 4.641 0.889 1.00 39.95 ? 269 LEU A C 1 ATOM 2141 O O . LEU A 1 270 ? 15.937 5.032 2.061 1.00 39.57 ? 269 LEU A O 1 ATOM 2142 C CB . LEU A 1 270 ? 16.074 2.161 0.502 1.00 37.58 ? 269 LEU A CB 1 ATOM 2143 C CG . LEU A 1 270 ? 16.811 0.920 -0.034 1.00 37.68 ? 269 LEU A CG 1 ATOM 2144 C CD1 . LEU A 1 270 ? 15.991 -0.350 0.170 1.00 37.15 ? 269 LEU A CD1 1 ATOM 2145 C CD2 . LEU A 1 270 ? 17.178 1.082 -1.497 1.00 38.95 ? 269 LEU A CD2 1 ATOM 2146 N N . GLU A 1 271 ? 15.041 5.149 -0.020 1.00 42.10 ? 270 GLU A N 1 ATOM 2147 C CA . GLU A 1 271 ? 14.017 6.157 0.273 1.00 42.91 ? 270 GLU A CA 1 ATOM 2148 C C . GLU A 1 271 ? 12.704 5.419 0.612 1.00 41.35 ? 270 GLU A C 1 ATOM 2149 O O . GLU A 1 271 ? 12.671 4.187 0.606 1.00 39.86 ? 270 GLU A O 1 ATOM 2150 C CB . GLU A 1 271 ? 13.849 7.089 -0.948 1.00 46.71 ? 270 GLU A CB 1 ATOM 2151 C CG . GLU A 1 271 ? 15.084 7.939 -1.288 1.00 49.36 ? 270 GLU A CG 1 ATOM 2152 C CD . GLU A 1 271 ? 15.213 8.320 -2.773 1.00 53.99 ? 270 GLU A CD 1 ATOM 2153 O OE1 . GLU A 1 271 ? 14.899 7.480 -3.652 1.00 55.70 ? 270 GLU A OE1 1 ATOM 2154 O OE2 . GLU A 1 271 ? 15.664 9.458 -3.079 1.00 56.38 ? 270 GLU A OE2 1 ATOM 2155 N N . TYR A 1 272 ? 11.635 6.158 0.920 1.00 41.12 ? 271 TYR A N 1 ATOM 2156 C CA . TYR A 1 272 ? 10.323 5.552 1.230 1.00 40.24 ? 271 TYR A CA 1 ATOM 2157 C C . TYR A 1 272 ? 9.636 4.933 0.004 1.00 40.91 ? 271 TYR A C 1 ATOM 2158 O O . TYR A 1 272 ? 9.520 5.570 -1.029 1.00 41.84 ? 271 TYR A O 1 ATOM 2159 C CB . TYR A 1 272 ? 9.387 6.584 1.868 1.00 41.01 ? 271 TYR A CB 1 ATOM 2160 C CG . TYR A 1 272 ? 8.025 6.025 2.244 1.00 41.40 ? 271 TYR A CG 1 ATOM 2161 C CD1 . TYR A 1 272 ? 7.912 4.857 2.998 1.00 40.19 ? 271 TYR A CD1 1 ATOM 2162 C CD2 . TYR A 1 272 ? 6.853 6.664 1.851 1.00 43.29 ? 271 TYR A CD2 1 ATOM 2163 C CE1 . TYR A 1 272 ? 6.671 4.338 3.339 1.00 40.99 ? 271 TYR A CE1 1 ATOM 2164 C CE2 . TYR A 1 272 ? 5.606 6.153 2.187 1.00 44.20 ? 271 TYR A CE2 1 ATOM 2165 C CZ . TYR A 1 272 ? 5.520 4.991 2.937 1.00 43.16 ? 271 TYR A CZ 1 ATOM 2166 O OH . TYR A 1 272 ? 4.282 4.478 3.275 1.00 44.28 ? 271 TYR A OH 1 ATOM 2167 N N . GLY A 1 273 ? 9.162 3.699 0.150 1.00 40.09 ? 272 GLY A N 1 ATOM 2168 C CA . GLY A 1 273 ? 8.621 2.919 -0.968 1.00 41.19 ? 272 GLY A CA 1 ATOM 2169 C C . GLY A 1 273 ? 7.120 2.984 -1.266 1.00 43.01 ? 272 GLY A C 1 ATOM 2170 O O . GLY A 1 273 ? 6.662 2.360 -2.224 1.00 44.46 ? 272 GLY A O 1 ATOM 2171 N N . ASN A 1 274 ? 6.345 3.711 -0.464 1.00 43.11 ? 273 ASN A N 1 ATOM 2172 C CA . ASN A 1 274 ? 4.889 3.830 -0.690 1.00 45.29 ? 273 ASN A CA 1 ATOM 2173 C C . ASN A 1 274 ? 4.245 2.456 -0.887 1.00 45.87 ? 273 ASN A C 1 ATOM 2174 O O . ASN A 1 274 ? 3.690 2.147 -1.936 1.00 47.30 ? 273 ASN A O 1 ATOM 2175 C CB . ASN A 1 274 ? 4.596 4.740 -1.885 1.00 47.78 ? 273 ASN A CB 1 ATOM 2176 C CG . ASN A 1 274 ? 5.163 6.141 -1.712 1.00 48.07 ? 273 ASN A CG 1 ATOM 2177 O OD1 . ASN A 1 274 ? 6.133 6.514 -2.370 1.00 48.99 ? 273 ASN A OD1 1 ATOM 2178 N ND2 . ASN A 1 274 ? 4.574 6.915 -0.815 1.00 47.89 ? 273 ASN A ND2 1 ATOM 2179 N N . CYS A 1 275 ? 4.358 1.634 0.148 1.00 44.68 ? 274 CYS A N 1 ATOM 2180 C CA . CYS A 1 275 ? 3.997 0.221 0.101 1.00 45.45 ? 274 CYS A CA 1 ATOM 2181 C C . CYS A 1 275 ? 3.832 -0.256 1.535 1.00 43.68 ? 274 CYS A C 1 ATOM 2182 O O . CYS A 1 275 ? 4.168 0.466 2.479 1.00 42.67 ? 274 CYS A O 1 ATOM 2183 C CB . CYS A 1 275 ? 5.091 -0.598 -0.612 1.00 45.18 ? 274 CYS A CB 1 ATOM 2184 S SG . CYS A 1 275 ? 6.785 -0.148 -0.135 1.00 44.22 ? 274 CYS A SG 1 ATOM 2185 N N . ASN A 1 276 ? 3.324 -1.469 1.697 1.00 44.00 ? 275 ASN A N 1 ATOM 2186 C CA . ASN A 1 276 ? 3.115 -2.042 3.011 1.00 43.52 ? 275 ASN A CA 1 ATOM 2187 C C . ASN A 1 276 ? 3.594 -3.484 3.054 1.00 43.53 ? 275 ASN A C 1 ATOM 2188 O O . ASN A 1 276 ? 3.442 -4.223 2.081 1.00 44.94 ? 275 ASN A O 1 ATOM 2189 C CB . ASN A 1 276 ? 1.637 -1.976 3.388 1.00 45.52 ? 275 ASN A CB 1 ATOM 2190 C CG . ASN A 1 276 ? 1.388 -2.387 4.832 1.00 45.38 ? 275 ASN A CG 1 ATOM 2191 O OD1 . ASN A 1 276 ? 1.873 -1.751 5.769 1.00 42.47 ? 275 ASN A OD1 1 ATOM 2192 N ND2 . ASN A 1 276 ? 0.616 -3.451 5.017 1.00 47.95 ? 275 ASN A ND2 1 ATOM 2193 N N . THR A 1 277 ? 4.165 -3.877 4.188 1.00 42.34 ? 276 THR A N 1 ATOM 2194 C CA . THR A 1 277 ? 4.735 -5.203 4.352 1.00 42.72 ? 276 THR A CA 1 ATOM 2195 C C . THR A 1 277 ? 4.554 -5.730 5.778 1.00 43.68 ? 276 THR A C 1 ATOM 2196 O O . THR A 1 277 ? 4.341 -4.957 6.714 1.00 42.97 ? 276 THR A O 1 ATOM 2197 C CB . THR A 1 277 ? 6.240 -5.191 4.006 1.00 40.44 ? 276 THR A CB 1 ATOM 2198 O OG1 . THR A 1 277 ? 6.774 -6.512 4.118 1.00 40.82 ? 276 THR A OG1 1 ATOM 2199 C CG2 . THR A 1 277 ? 7.009 -4.279 4.943 1.00 38.98 ? 276 THR A CG2 1 ATOM 2200 N N . LYS A 1 278 ? 4.644 -7.053 5.918 1.00 45.62 ? 277 LYS A N 1 ATOM 2201 C CA . LYS A 1 278 ? 4.739 -7.712 7.221 1.00 47.11 ? 277 LYS A CA 1 ATOM 2202 C C . LYS A 1 278 ? 6.190 -8.023 7.614 1.00 46.06 ? 277 LYS A C 1 ATOM 2203 O O . LYS A 1 278 ? 6.446 -8.435 8.745 1.00 46.80 ? 277 LYS A O 1 ATOM 2204 C CB . LYS A 1 278 ? 3.952 -9.019 7.211 1.00 50.42 ? 277 LYS A CB 1 ATOM 2205 C CG . LYS A 1 278 ? 2.459 -8.858 6.974 1.00 53.09 ? 277 LYS A CG 1 ATOM 2206 C CD . LYS A 1 278 ? 1.734 -8.312 8.195 1.00 53.84 ? 277 LYS A CD 1 ATOM 2207 C CE . LYS A 1 278 ? 1.623 -9.325 9.330 1.00 56.04 ? 277 LYS A CE 1 ATOM 2208 N NZ . LYS A 1 278 ? 0.991 -10.610 8.917 1.00 59.36 ? 277 LYS A NZ 1 ATOM 2209 N N . CYS A 1 279 ? 7.130 -7.836 6.689 1.00 44.84 ? 278 CYS A N 1 ATOM 2210 C CA . CYS A 1 279 ? 8.533 -8.185 6.932 1.00 44.04 ? 278 CYS A CA 1 ATOM 2211 C C . CYS A 1 279 ? 9.453 -7.293 6.124 1.00 41.33 ? 278 CYS A C 1 ATOM 2212 O O . CYS A 1 279 ? 9.377 -7.274 4.901 1.00 41.41 ? 278 CYS A O 1 ATOM 2213 C CB . CYS A 1 279 ? 8.784 -9.650 6.561 1.00 45.91 ? 278 CYS A CB 1 ATOM 2214 S SG . CYS A 1 279 ? 10.504 -10.165 6.753 1.00 46.00 ? 278 CYS A SG 1 ATOM 2215 N N . GLN A 1 280 ? 10.328 -6.564 6.806 1.00 39.72 ? 279 GLN A N 1 ATOM 2216 C CA . GLN A 1 280 ? 11.161 -5.556 6.153 1.00 38.12 ? 279 GLN A CA 1 ATOM 2217 C C . GLN A 1 280 ? 12.659 -5.752 6.469 1.00 37.11 ? 279 GLN A C 1 ATOM 2218 O O . GLN A 1 280 ? 13.034 -5.986 7.612 1.00 36.74 ? 279 GLN A O 1 ATOM 2219 C CB . GLN A 1 280 ? 10.683 -4.166 6.582 1.00 37.69 ? 279 GLN A CB 1 ATOM 2220 C CG . GLN A 1 280 ? 11.497 -2.990 6.049 1.00 36.66 ? 279 GLN A CG 1 ATOM 2221 C CD . GLN A 1 280 ? 11.397 -2.842 4.547 1.00 37.04 ? 279 GLN A CD 1 ATOM 2222 O OE1 . GLN A 1 280 ? 12.397 -2.895 3.841 1.00 36.77 ? 279 GLN A OE1 1 ATOM 2223 N NE2 . GLN A 1 280 ? 10.186 -2.660 4.052 1.00 38.03 ? 279 GLN A NE2 1 ATOM 2224 N N . THR A 1 281 ? 13.503 -5.677 5.439 1.00 36.46 ? 280 THR A N 1 ATOM 2225 C CA . THR A 1 281 ? 14.952 -5.654 5.629 1.00 35.75 ? 280 THR A CA 1 ATOM 2226 C C . THR A 1 281 ? 15.497 -4.299 5.188 1.00 35.11 ? 280 THR A C 1 ATOM 2227 O O . THR A 1 281 ? 14.776 -3.503 4.600 1.00 34.29 ? 280 THR A O 1 ATOM 2228 C CB . THR A 1 281 ? 15.665 -6.752 4.818 1.00 36.16 ? 280 THR A CB 1 ATOM 2229 O OG1 . THR A 1 281 ? 15.906 -6.284 3.491 1.00 35.79 ? 280 THR A OG1 1 ATOM 2230 C CG2 . THR A 1 281 ? 14.852 -8.038 4.780 1.00 37.25 ? 280 THR A CG2 1 ATOM 2231 N N . PRO A 1 282 ? 16.786 -4.034 5.458 1.00 35.68 ? 281 PRO A N 1 ATOM 2232 C CA . PRO A 1 282 ? 17.379 -2.777 4.996 1.00 35.73 ? 281 PRO A CA 1 ATOM 2233 C C . PRO A 1 282 ? 17.436 -2.594 3.478 1.00 36.64 ? 281 PRO A C 1 ATOM 2234 O O . PRO A 1 282 ? 17.534 -1.461 3.015 1.00 37.39 ? 281 PRO A O 1 ATOM 2235 C CB . PRO A 1 282 ? 18.798 -2.827 5.568 1.00 36.16 ? 281 PRO A CB 1 ATOM 2236 C CG . PRO A 1 282 ? 18.719 -3.742 6.731 1.00 36.28 ? 281 PRO A CG 1 ATOM 2237 C CD . PRO A 1 282 ? 17.683 -4.762 6.372 1.00 35.98 ? 281 PRO A CD 1 ATOM 2238 N N . ILE A 1 283 ? 17.374 -3.685 2.718 1.00 37.41 ? 282 ILE A N 1 ATOM 2239 C CA . ILE A 1 283 ? 17.508 -3.620 1.263 1.00 38.69 ? 282 ILE A CA 1 ATOM 2240 C C . ILE A 1 283 ? 16.192 -3.861 0.502 1.00 39.24 ? 282 ILE A C 1 ATOM 2241 O O . ILE A 1 283 ? 16.167 -3.773 -0.728 1.00 39.78 ? 282 ILE A O 1 ATOM 2242 C CB . ILE A 1 283 ? 18.605 -4.591 0.758 1.00 40.32 ? 282 ILE A CB 1 ATOM 2243 C CG1 . ILE A 1 283 ? 18.196 -6.059 0.978 1.00 41.64 ? 282 ILE A CG1 1 ATOM 2244 C CG2 . ILE A 1 283 ? 19.931 -4.290 1.451 1.00 40.11 ? 282 ILE A CG2 1 ATOM 2245 C CD1 . ILE A 1 283 ? 19.274 -7.064 0.610 1.00 43.04 ? 282 ILE A CD1 1 ATOM 2246 N N . GLY A 1 284 ? 15.109 -4.149 1.227 1.00 38.70 ? 283 GLY A N 1 ATOM 2247 C CA . GLY A 1 284 ? 13.813 -4.393 0.612 1.00 38.74 ? 283 GLY A CA 1 ATOM 2248 C C . GLY A 1 284 ? 12.897 -5.257 1.457 1.00 39.06 ? 283 GLY A C 1 ATOM 2249 O O . GLY A 1 284 ? 13.365 -6.022 2.305 1.00 38.79 ? 283 GLY A O 1 ATOM 2250 N N . ALA A 1 285 ? 11.593 -5.135 1.202 1.00 39.29 ? 284 ALA A N 1 ATOM 2251 C CA . ALA A 1 285 ? 10.563 -5.846 1.949 1.00 40.03 ? 284 ALA A CA 1 ATOM 2252 C C . ALA A 1 285 ? 10.362 -7.265 1.406 1.00 41.22 ? 284 ALA A C 1 ATOM 2253 O O . ALA A 1 285 ? 10.832 -7.581 0.326 1.00 41.69 ? 284 ALA A O 1 ATOM 2254 C CB . ALA A 1 285 ? 9.249 -5.073 1.895 1.00 40.50 ? 284 ALA A CB 1 ATOM 2255 N N . ILE A 1 286 ? 9.653 -8.103 2.158 1.00 41.85 ? 285 ILE A N 1 ATOM 2256 C CA . ILE A 1 286 ? 9.442 -9.500 1.796 1.00 43.25 ? 285 ILE A CA 1 ATOM 2257 C C . ILE A 1 286 ? 8.007 -9.915 2.091 1.00 45.19 ? 285 ILE A C 1 ATOM 2258 O O . ILE A 1 286 ? 7.582 -9.897 3.241 1.00 44.89 ? 285 ILE A O 1 ATOM 2259 C CB . ILE A 1 286 ? 10.360 -10.451 2.592 1.00 43.44 ? 285 ILE A CB 1 ATOM 2260 C CG1 . ILE A 1 286 ? 11.835 -10.194 2.286 1.00 42.57 ? 285 ILE A CG1 1 ATOM 2261 C CG2 . ILE A 1 286 ? 10.025 -11.904 2.283 1.00 45.50 ? 285 ILE A CG2 1 ATOM 2262 C CD1 . ILE A 1 286 ? 12.771 -10.753 3.345 1.00 42.68 ? 285 ILE A CD1 1 ATOM 2263 N N . ASN A 1 287 ? 7.270 -10.295 1.048 1.00 47.25 ? 286 ASN A N 1 ATOM 2264 C CA . ASN A 1 287 ? 5.971 -10.937 1.211 1.00 50.26 ? 286 ASN A CA 1 ATOM 2265 C C . ASN A 1 287 ? 6.072 -12.367 0.680 1.00 51.86 ? 286 ASN A C 1 ATOM 2266 O O . ASN A 1 287 ? 5.975 -12.597 -0.522 1.00 52.60 ? 286 ASN A O 1 ATOM 2267 C CB . ASN A 1 287 ? 4.876 -10.139 0.490 1.00 51.70 ? 286 ASN A CB 1 ATOM 2268 C CG . ASN A 1 287 ? 3.479 -10.724 0.696 1.00 55.10 ? 286 ASN A CG 1 ATOM 2269 O OD1 . ASN A 1 287 ? 3.199 -11.372 1.706 1.00 56.23 ? 286 ASN A OD1 1 ATOM 2270 N ND2 . ASN A 1 287 ? 2.595 -10.493 -0.271 1.00 56.92 ? 286 ASN A ND2 1 ATOM 2271 N N . SER A 1 288 ? 6.292 -13.315 1.590 1.00 52.85 ? 287 SER A N 1 ATOM 2272 C CA . SER A 1 288 ? 6.456 -14.724 1.240 1.00 54.77 ? 287 SER A CA 1 ATOM 2273 C C . SER A 1 288 ? 5.838 -15.660 2.274 1.00 57.69 ? 287 SER A C 1 ATOM 2274 O O . SER A 1 288 ? 5.653 -15.297 3.434 1.00 57.64 ? 287 SER A O 1 ATOM 2275 C CB . SER A 1 288 ? 7.939 -15.054 1.105 1.00 53.28 ? 287 SER A CB 1 ATOM 2276 O OG . SER A 1 288 ? 8.149 -16.453 1.067 1.00 55.13 ? 287 SER A OG 1 ATOM 2277 N N . SER A 1 289 ? 5.538 -16.876 1.832 1.00 60.70 ? 288 SER A N 1 ATOM 2278 C CA . SER A 1 289 ? 5.014 -17.924 2.700 1.00 64.27 ? 288 SER A CA 1 ATOM 2279 C C . SER A 1 289 ? 6.066 -19.008 2.956 1.00 64.94 ? 288 SER A C 1 ATOM 2280 O O . SER A 1 289 ? 5.772 -20.023 3.588 1.00 68.62 ? 288 SER A O 1 ATOM 2281 C CB . SER A 1 289 ? 3.773 -18.551 2.057 1.00 67.65 ? 288 SER A CB 1 ATOM 2282 O OG . SER A 1 289 ? 4.096 -19.133 0.802 1.00 67.63 ? 288 SER A OG 1 ATOM 2283 N N . MET A 1 290 ? 7.285 -18.793 2.460 1.00 62.28 ? 289 MET A N 1 ATOM 2284 C CA . MET A 1 290 ? 8.390 -19.735 2.657 1.00 62.22 ? 289 MET A CA 1 ATOM 2285 C C . MET A 1 290 ? 8.822 -19.766 4.127 1.00 61.52 ? 289 MET A C 1 ATOM 2286 O O . MET A 1 290 ? 8.724 -18.754 4.831 1.00 60.13 ? 289 MET A O 1 ATOM 2287 C CB . MET A 1 290 ? 9.603 -19.333 1.807 1.00 60.15 ? 289 MET A CB 1 ATOM 2288 C CG . MET A 1 290 ? 9.367 -19.245 0.308 1.00 60.46 ? 289 MET A CG 1 ATOM 2289 S SD . MET A 1 290 ? 8.997 -20.828 -0.469 1.00 65.34 ? 289 MET A SD 1 ATOM 2290 C CE . MET A 1 290 ? 9.256 -20.416 -2.196 1.00 63.76 ? 289 MET A CE 1 ATOM 2291 N N . PRO A 1 291 ? 9.309 -20.924 4.602 1.00 62.73 ? 290 PRO A N 1 ATOM 2292 C CA . PRO A 1 291 ? 9.884 -20.944 5.955 1.00 62.47 ? 290 PRO A CA 1 ATOM 2293 C C . PRO A 1 291 ? 11.219 -20.200 6.077 1.00 58.60 ? 290 PRO A C 1 ATOM 2294 O O . PRO A 1 291 ? 11.543 -19.706 7.160 1.00 58.21 ? 290 PRO A O 1 ATOM 2295 C CB . PRO A 1 291 ? 10.071 -22.436 6.243 1.00 66.12 ? 290 PRO A CB 1 ATOM 2296 C CG . PRO A 1 291 ? 10.103 -23.095 4.907 1.00 66.51 ? 290 PRO A CG 1 ATOM 2297 C CD . PRO A 1 291 ? 9.223 -22.274 4.013 1.00 65.09 ? 290 PRO A CD 1 ATOM 2298 N N . PHE A 1 292 ? 11.973 -20.119 4.980 1.00 55.80 ? 291 PHE A N 1 ATOM 2299 C CA . PHE A 1 292 ? 13.282 -19.462 4.974 1.00 52.65 ? 291 PHE A CA 1 ATOM 2300 C C . PHE A 1 292 ? 13.405 -18.367 3.919 1.00 49.35 ? 291 PHE A C 1 ATOM 2301 O O . PHE A 1 292 ? 12.613 -18.292 2.987 1.00 48.80 ? 291 PHE A O 1 ATOM 2302 C CB . PHE A 1 292 ? 14.385 -20.488 4.730 1.00 53.40 ? 291 PHE A CB 1 ATOM 2303 C CG . PHE A 1 292 ? 14.403 -21.603 5.720 1.00 56.47 ? 291 PHE A CG 1 ATOM 2304 C CD1 . PHE A 1 292 ? 14.990 -21.433 6.961 1.00 57.14 ? 291 PHE A CD1 1 ATOM 2305 C CD2 . PHE A 1 292 ? 13.835 -22.828 5.412 1.00 59.39 ? 291 PHE A CD2 1 ATOM 2306 C CE1 . PHE A 1 292 ? 15.015 -22.462 7.880 1.00 60.70 ? 291 PHE A CE1 1 ATOM 2307 C CE2 . PHE A 1 292 ? 13.856 -23.866 6.325 1.00 62.87 ? 291 PHE A CE2 1 ATOM 2308 C CZ . PHE A 1 292 ? 14.448 -23.682 7.560 1.00 63.67 ? 291 PHE A CZ 1 ATOM 2309 N N . HIS A 1 293 ? 14.418 -17.520 4.092 1.00 47.41 ? 292 HIS A N 1 ATOM 2310 C CA . HIS A 1 293 ? 14.775 -16.484 3.121 1.00 44.70 ? 292 HIS A CA 1 ATOM 2311 C C . HIS A 1 293 ? 16.272 -16.181 3.279 1.00 43.74 ? 292 HIS A C 1 ATOM 2312 O O . HIS A 1 293 ? 16.860 -16.531 4.303 1.00 44.73 ? 292 HIS A O 1 ATOM 2313 C CB . HIS A 1 293 ? 13.935 -15.225 3.345 1.00 43.31 ? 292 HIS A CB 1 ATOM 2314 C CG . HIS A 1 293 ? 14.393 -14.398 4.507 1.00 42.57 ? 292 HIS A CG 1 ATOM 2315 N ND1 . HIS A 1 293 ? 15.207 -13.297 4.357 1.00 40.61 ? 292 HIS A ND1 1 ATOM 2316 C CD2 . HIS A 1 293 ? 14.177 -14.526 5.835 1.00 43.50 ? 292 HIS A CD2 1 ATOM 2317 C CE1 . HIS A 1 293 ? 15.463 -12.776 5.541 1.00 40.63 ? 292 HIS A CE1 1 ATOM 2318 N NE2 . HIS A 1 293 ? 14.851 -13.504 6.457 1.00 42.54 ? 292 HIS A NE2 1 ATOM 2319 N N . ASN A 1 294 ? 16.887 -15.565 2.270 1.00 42.20 ? 293 ASN A N 1 ATOM 2320 C CA . ASN A 1 294 ? 18.321 -15.244 2.314 1.00 41.90 ? 293 ASN A CA 1 ATOM 2321 C C . ASN A 1 294 ? 18.623 -13.816 1.879 1.00 40.08 ? 293 ASN A C 1 ATOM 2322 O O . ASN A 1 294 ? 19.720 -13.517 1.428 1.00 39.52 ? 293 ASN A O 1 ATOM 2323 C CB . ASN A 1 294 ? 19.142 -16.251 1.486 1.00 42.92 ? 293 ASN A CB 1 ATOM 2324 C CG . ASN A 1 294 ? 18.980 -16.078 -0.026 1.00 42.74 ? 293 ASN A CG 1 ATOM 2325 O OD1 . ASN A 1 294 ? 18.147 -15.297 -0.521 1.00 41.34 ? 293 ASN A OD1 1 ATOM 2326 N ND2 . ASN A 1 294 ? 19.786 -16.829 -0.774 1.00 43.74 ? 293 ASN A ND2 1 ATOM 2327 N N . ILE A 1 295 ? 17.635 -12.943 2.025 1.00 39.55 ? 294 ILE A N 1 ATOM 2328 C CA . ILE A 1 295 ? 17.773 -11.545 1.642 1.00 38.54 ? 294 ILE A CA 1 ATOM 2329 C C . ILE A 1 295 ? 18.792 -10.849 2.532 1.00 38.18 ? 294 ILE A C 1 ATOM 2330 O O . ILE A 1 295 ? 19.772 -10.295 2.042 1.00 38.72 ? 294 ILE A O 1 ATOM 2331 C CB . ILE A 1 295 ? 16.424 -10.779 1.744 1.00 38.30 ? 294 ILE A CB 1 ATOM 2332 C CG1 . ILE A 1 295 ? 15.289 -11.525 1.012 1.00 39.28 ? 294 ILE A CG1 1 ATOM 2333 C CG2 . ILE A 1 295 ? 16.565 -9.354 1.208 1.00 37.23 ? 294 ILE A CG2 1 ATOM 2334 C CD1 . ILE A 1 295 ? 15.599 -11.939 -0.412 1.00 39.54 ? 294 ILE A CD1 1 ATOM 2335 N N . HIS A 1 296 ? 18.557 -10.883 3.841 1.00 38.37 ? 295 HIS A N 1 ATOM 2336 C CA . HIS A 1 296 ? 19.280 -10.031 4.783 1.00 37.97 ? 295 HIS A CA 1 ATOM 2337 C C . HIS A 1 296 ? 18.963 -10.499 6.208 1.00 39.04 ? 295 HIS A C 1 ATOM 2338 O O . HIS A 1 296 ? 17.824 -10.874 6.474 1.00 39.08 ? 295 HIS A O 1 ATOM 2339 C CB . HIS A 1 296 ? 18.837 -8.578 4.606 1.00 36.43 ? 295 HIS A CB 1 ATOM 2340 C CG . HIS A 1 296 ? 19.855 -7.576 5.048 1.00 36.62 ? 295 HIS A CG 1 ATOM 2341 N ND1 . HIS A 1 296 ? 20.258 -7.451 6.358 1.00 37.19 ? 295 HIS A ND1 1 ATOM 2342 C CD2 . HIS A 1 296 ? 20.548 -6.643 4.354 1.00 36.62 ? 295 HIS A CD2 1 ATOM 2343 C CE1 . HIS A 1 296 ? 21.172 -6.502 6.450 1.00 37.45 ? 295 HIS A CE1 1 ATOM 2344 N NE2 . HIS A 1 296 ? 21.358 -5.988 5.248 1.00 36.89 ? 295 HIS A NE2 1 ATOM 2345 N N . PRO A 1 297 ? 19.964 -10.499 7.119 1.00 39.93 ? 296 PRO A N 1 ATOM 2346 C CA . PRO A 1 297 ? 19.758 -10.937 8.516 1.00 41.24 ? 296 PRO A CA 1 ATOM 2347 C C . PRO A 1 297 ? 19.116 -9.921 9.483 1.00 40.49 ? 296 PRO A C 1 ATOM 2348 O O . PRO A 1 297 ? 18.592 -10.325 10.518 1.00 41.87 ? 296 PRO A O 1 ATOM 2349 C CB . PRO A 1 297 ? 21.172 -11.296 8.976 1.00 42.84 ? 296 PRO A CB 1 ATOM 2350 C CG . PRO A 1 297 ? 22.063 -10.448 8.138 1.00 41.93 ? 296 PRO A CG 1 ATOM 2351 C CD . PRO A 1 297 ? 21.397 -10.388 6.796 1.00 40.50 ? 296 PRO A CD 1 ATOM 2352 N N . LEU A 1 298 ? 19.170 -8.628 9.163 1.00 38.85 ? 297 LEU A N 1 ATOM 2353 C CA . LEU A 1 298 ? 18.487 -7.580 9.944 1.00 37.74 ? 297 LEU A CA 1 ATOM 2354 C C . LEU A 1 298 ? 17.033 -7.355 9.476 1.00 36.80 ? 297 LEU A C 1 ATOM 2355 O O . LEU A 1 298 ? 16.739 -6.548 8.592 1.00 35.71 ? 297 LEU A O 1 ATOM 2356 C CB . LEU A 1 298 ? 19.306 -6.282 9.916 1.00 36.94 ? 297 LEU A CB 1 ATOM 2357 C CG . LEU A 1 298 ? 20.783 -6.484 10.317 1.00 38.78 ? 297 LEU A CG 1 ATOM 2358 C CD1 . LEU A 1 298 ? 21.472 -5.149 10.560 1.00 38.82 ? 297 LEU A CD1 1 ATOM 2359 C CD2 . LEU A 1 298 ? 20.956 -7.380 11.540 1.00 40.33 ? 297 LEU A CD2 1 ATOM 2360 N N . THR A 1 299 ? 16.118 -8.090 10.094 1.00 37.33 ? 298 THR A N 1 ATOM 2361 C CA . THR A 1 299 ? 14.723 -8.034 9.728 1.00 36.35 ? 298 THR A CA 1 ATOM 2362 C C . THR A 1 299 ? 13.877 -7.509 10.874 1.00 36.03 ? 298 THR A C 1 ATOM 2363 O O . THR A 1 299 ? 14.227 -7.655 12.026 1.00 36.75 ? 298 THR A O 1 ATOM 2364 C CB . THR A 1 299 ? 14.220 -9.432 9.323 1.00 37.77 ? 298 THR A CB 1 ATOM 2365 O OG1 . THR A 1 299 ? 14.256 -10.314 10.447 1.00 39.22 ? 298 THR A OG1 1 ATOM 2366 C CG2 . THR A 1 299 ? 15.079 -9.996 8.217 1.00 37.83 ? 298 THR A CG2 1 ATOM 2367 N N . ILE A 1 300 ? 12.761 -6.884 10.535 1.00 35.53 ? 299 ILE A N 1 ATOM 2368 C CA . ILE A 1 300 ? 11.724 -6.557 11.507 1.00 36.22 ? 299 ILE A CA 1 ATOM 2369 C C . ILE A 1 300 ? 10.366 -6.945 10.924 1.00 37.14 ? 299 ILE A C 1 ATOM 2370 O O . ILE A 1 300 ? 10.115 -6.733 9.745 1.00 36.07 ? 299 ILE A O 1 ATOM 2371 C CB . ILE A 1 300 ? 11.769 -5.063 11.929 1.00 34.66 ? 299 ILE A CB 1 ATOM 2372 C CG1 . ILE A 1 300 ? 10.805 -4.807 13.098 1.00 35.77 ? 299 ILE A CG1 1 ATOM 2373 C CG2 . ILE A 1 300 ? 11.487 -4.136 10.759 1.00 33.21 ? 299 ILE A CG2 1 ATOM 2374 C CD1 . ILE A 1 300 ? 10.913 -3.418 13.708 1.00 34.72 ? 299 ILE A CD1 1 ATOM 2375 N N . GLY A 1 301 ? 9.510 -7.527 11.761 1.00 39.76 ? 300 GLY A N 1 ATOM 2376 C CA . GLY A 1 301 ? 8.167 -7.943 11.361 1.00 41.82 ? 300 GLY A CA 1 ATOM 2377 C C . GLY A 1 301 ? 7.978 -9.447 11.439 1.00 44.97 ? 300 GLY A C 1 ATOM 2378 O O . GLY A 1 301 ? 8.739 -10.129 12.117 1.00 46.14 ? 300 GLY A O 1 ATOM 2379 N N . GLU A 1 302 ? 6.950 -9.960 10.761 1.00 47.51 ? 301 GLU A N 1 ATOM 2380 C CA . GLU A 1 302 ? 6.718 -11.405 10.671 1.00 50.98 ? 301 GLU A CA 1 ATOM 2381 C C . GLU A 1 302 ? 7.436 -11.944 9.447 1.00 50.83 ? 301 GLU A C 1 ATOM 2382 O O . GLU A 1 302 ? 6.947 -11.821 8.321 1.00 50.54 ? 301 GLU A O 1 ATOM 2383 C CB . GLU A 1 302 ? 5.229 -11.740 10.581 1.00 53.89 ? 301 GLU A CB 1 ATOM 2384 C CG . GLU A 1 302 ? 4.480 -11.601 11.897 1.00 56.29 ? 301 GLU A CG 1 ATOM 2385 C CD . GLU A 1 302 ? 3.413 -12.672 12.099 1.00 60.94 ? 301 GLU A CD 1 ATOM 2386 O OE1 . GLU A 1 302 ? 3.368 -13.653 11.316 1.00 62.09 ? 301 GLU A OE1 1 ATOM 2387 O OE2 . GLU A 1 302 ? 2.624 -12.534 13.065 1.00 63.52 ? 301 GLU A OE2 1 ATOM 2388 N N . CYS A 1 303 ? 8.589 -12.555 9.683 1.00 51.46 ? 302 CYS A N 1 ATOM 2389 C CA . CYS A 1 303 ? 9.486 -12.954 8.612 1.00 50.59 ? 302 CYS A CA 1 ATOM 2390 C C . CYS A 1 303 ? 9.713 -14.450 8.585 1.00 52.52 ? 302 CYS A C 1 ATOM 2391 O O . CYS A 1 303 ? 9.471 -15.132 9.578 1.00 54.87 ? 302 CYS A O 1 ATOM 2392 C CB . CYS A 1 303 ? 10.829 -12.279 8.818 1.00 48.99 ? 302 CYS A CB 1 ATOM 2393 S SG . CYS A 1 303 ? 10.711 -10.487 8.756 1.00 47.28 ? 302 CYS A SG 1 ATOM 2394 N N . PRO A 1 304 ? 10.201 -14.962 7.444 1.00 51.82 ? 303 PRO A N 1 ATOM 2395 C CA . PRO A 1 304 ? 10.789 -16.294 7.429 1.00 53.10 ? 303 PRO A CA 1 ATOM 2396 C C . PRO A 1 304 ? 12.091 -16.285 8.215 1.00 52.43 ? 303 PRO A C 1 ATOM 2397 O O . PRO A 1 304 ? 12.551 -15.223 8.638 1.00 49.86 ? 303 PRO A O 1 ATOM 2398 C CB . PRO A 1 304 ? 11.065 -16.559 5.943 1.00 52.36 ? 303 PRO A CB 1 ATOM 2399 C CG . PRO A 1 304 ? 10.386 -15.467 5.184 1.00 50.83 ? 303 PRO A CG 1 ATOM 2400 C CD . PRO A 1 304 ? 10.252 -14.314 6.121 1.00 49.84 ? 303 PRO A CD 1 ATOM 2401 N N . LYS A 1 305 ? 12.684 -17.458 8.397 1.00 54.49 ? 304 LYS A N 1 ATOM 2402 C CA . LYS A 1 305 ? 13.952 -17.569 9.102 1.00 54.63 ? 304 LYS A CA 1 ATOM 2403 C C . LYS A 1 305 ? 15.084 -17.377 8.100 1.00 52.09 ? 304 LYS A C 1 ATOM 2404 O O . LYS A 1 305 ? 15.138 -18.064 7.089 1.00 51.93 ? 304 LYS A O 1 ATOM 2405 C CB . LYS A 1 305 ? 14.068 -18.929 9.781 1.00 58.95 ? 304 LYS A CB 1 ATOM 2406 C CG . LYS A 1 305 ? 12.906 -19.284 10.701 1.00 62.21 ? 304 LYS A CG 1 ATOM 2407 C CD . LYS A 1 305 ? 12.696 -18.220 11.768 1.00 62.01 ? 304 LYS A CD 1 ATOM 2408 C CE . LYS A 1 305 ? 11.970 -18.765 12.987 1.00 65.94 ? 304 LYS A CE 1 ATOM 2409 N NZ . LYS A 1 305 ? 11.974 -17.793 14.122 1.00 65.57 ? 304 LYS A NZ 1 ATOM 2410 N N . TYR A 1 306 ? 15.971 -16.426 8.383 1.00 49.83 ? 305 TYR A N 1 ATOM 2411 C CA . TYR A 1 306 ? 17.108 -16.129 7.517 1.00 48.10 ? 305 TYR A CA 1 ATOM 2412 C C . TYR A 1 306 ? 18.149 -17.255 7.502 1.00 49.65 ? 305 TYR A C 1 ATOM 2413 O O . TYR A 1 306 ? 18.514 -17.801 8.546 1.00 51.74 ? 305 TYR A O 1 ATOM 2414 C CB . TYR A 1 306 ? 17.790 -14.830 7.957 1.00 46.62 ? 305 TYR A CB 1 ATOM 2415 C CG . TYR A 1 306 ? 19.047 -14.508 7.184 1.00 45.99 ? 305 TYR A CG 1 ATOM 2416 C CD1 . TYR A 1 306 ? 18.977 -13.885 5.946 1.00 44.38 ? 305 TYR A CD1 1 ATOM 2417 C CD2 . TYR A 1 306 ? 20.311 -14.828 7.689 1.00 47.60 ? 305 TYR A CD2 1 ATOM 2418 C CE1 . TYR A 1 306 ? 20.121 -13.587 5.226 1.00 44.07 ? 305 TYR A CE1 1 ATOM 2419 C CE2 . TYR A 1 306 ? 21.463 -14.536 6.973 1.00 47.20 ? 305 TYR A CE2 1 ATOM 2420 C CZ . TYR A 1 306 ? 21.358 -13.915 5.739 1.00 45.54 ? 305 TYR A CZ 1 ATOM 2421 O OH . TYR A 1 306 ? 22.480 -13.610 5.006 1.00 45.79 ? 305 TYR A OH 1 ATOM 2422 N N . VAL A 1 307 ? 18.622 -17.579 6.305 1.00 56.68 ? 306 VAL A N 1 ATOM 2423 C CA . VAL A 1 307 ? 19.795 -18.422 6.117 1.00 57.35 ? 306 VAL A CA 1 ATOM 2424 C C . VAL A 1 307 ? 20.664 -17.793 5.040 1.00 57.34 ? 306 VAL A C 1 ATOM 2425 O O . VAL A 1 307 ? 20.201 -16.959 4.276 1.00 56.33 ? 306 VAL A O 1 ATOM 2426 C CB . VAL A 1 307 ? 19.426 -19.866 5.722 1.00 58.09 ? 306 VAL A CB 1 ATOM 2427 C CG1 . VAL A 1 307 ? 18.786 -20.584 6.899 1.00 59.12 ? 306 VAL A CG1 1 ATOM 2428 C CG2 . VAL A 1 307 ? 18.510 -19.897 4.504 1.00 57.34 ? 306 VAL A CG2 1 ATOM 2429 N N . LYS A 1 308 ? 21.929 -18.181 5.000 1.00 59.55 ? 307 LYS A N 1 ATOM 2430 C CA . LYS A 1 308 ? 22.857 -17.676 3.992 1.00 61.33 ? 307 LYS A CA 1 ATOM 2431 C C . LYS A 1 308 ? 22.749 -18.488 2.703 1.00 62.66 ? 307 LYS A C 1 ATOM 2432 O O . LYS A 1 308 ? 23.310 -18.105 1.678 1.00 64.90 ? 307 LYS A O 1 ATOM 2433 C CB . LYS A 1 308 ? 24.301 -17.740 4.504 1.00 64.18 ? 307 LYS A CB 1 ATOM 2434 C CG . LYS A 1 308 ? 24.514 -17.091 5.854 1.00 63.93 ? 307 LYS A CG 1 ATOM 2435 C CD . LYS A 1 308 ? 25.990 -16.938 6.143 1.00 67.81 ? 307 LYS A CD 1 ATOM 2436 C CE . LYS A 1 308 ? 26.218 -16.474 7.561 1.00 68.37 ? 307 LYS A CE 1 ATOM 2437 N NZ . LYS A 1 308 ? 27.653 -16.156 7.799 1.00 72.90 ? 307 LYS A NZ 1 ATOM 2438 N N . SER A 1 309 ? 22.027 -19.604 2.765 1.00 62.13 ? 308 SER A N 1 ATOM 2439 C CA . SER A 1 309 ? 21.950 -20.555 1.663 1.00 63.43 ? 308 SER A CA 1 ATOM 2440 C C . SER A 1 309 ? 21.486 -19.917 0.361 1.00 63.69 ? 308 SER A C 1 ATOM 2441 O O . SER A 1 309 ? 20.604 -19.052 0.352 1.00 62.05 ? 308 SER A O 1 ATOM 2442 C CB . SER A 1 309 ? 20.999 -21.692 2.031 1.00 62.59 ? 308 SER A CB 1 ATOM 2443 O OG . SER A 1 309 ? 21.271 -22.163 3.340 1.00 62.98 ? 308 SER A OG 1 ATOM 2444 N N . SER A 1 310 ? 22.101 -20.351 -0.733 1.00 66.62 ? 309 SER A N 1 ATOM 2445 C CA . SER A 1 310 ? 21.696 -19.934 -2.067 1.00 68.43 ? 309 SER A CA 1 ATOM 2446 C C . SER A 1 310 ? 20.518 -20.773 -2.569 1.00 67.95 ? 309 SER A C 1 ATOM 2447 O O . SER A 1 310 ? 19.743 -20.304 -3.393 1.00 68.71 ? 309 SER A O 1 ATOM 2448 C CB . SER A 1 310 ? 22.877 -20.047 -3.027 1.00 72.72 ? 309 SER A CB 1 ATOM 2449 O OG . SER A 1 310 ? 23.444 -21.343 -2.967 1.00 74.21 ? 309 SER A OG 1 ATOM 2450 N N . ARG A 1 311 ? 20.385 -22.001 -2.066 1.00 67.53 ? 310 ARG A N 1 ATOM 2451 C CA . ARG A 1 311 ? 19.335 -22.919 -2.511 1.00 68.23 ? 310 ARG A CA 1 ATOM 2452 C C . ARG A 1 311 ? 18.850 -23.842 -1.395 1.00 66.60 ? 310 ARG A C 1 ATOM 2453 O O . ARG A 1 311 ? 19.656 -24.410 -0.660 1.00 66.69 ? 310 ARG A O 1 ATOM 2454 C CB . ARG A 1 311 ? 19.847 -23.801 -3.659 1.00 71.94 ? 310 ARG A CB 1 ATOM 2455 C CG . ARG A 1 311 ? 20.380 -23.050 -4.870 1.00 75.86 ? 310 ARG A CG 1 ATOM 2456 C CD . ARG A 1 311 ? 20.879 -24.011 -5.933 1.00 80.07 ? 310 ARG A CD 1 ATOM 2457 N NE . ARG A 1 311 ? 21.395 -23.322 -7.115 1.00 85.01 ? 310 ARG A NE 1 ATOM 2458 C CZ . ARG A 1 311 ? 21.888 -23.934 -8.193 1.00 89.59 ? 310 ARG A CZ 1 ATOM 2459 N NH1 . ARG A 1 311 ? 21.940 -25.262 -8.257 1.00 89.65 ? 310 ARG A NH1 1 ATOM 2460 N NH2 . ARG A 1 311 ? 22.338 -23.212 -9.215 1.00 94.61 ? 310 ARG A NH2 1 ATOM 2461 N N . LEU A 1 312 ? 17.531 -24.004 -1.294 1.00 66.33 ? 311 LEU A N 1 ATOM 2462 C CA . LEU A 1 312 ? 16.918 -25.005 -0.416 1.00 65.99 ? 311 LEU A CA 1 ATOM 2463 C C . LEU A 1 312 ? 15.710 -25.627 -1.103 1.00 67.21 ? 311 LEU A C 1 ATOM 2464 O O . LEU A 1 312 ? 14.653 -24.998 -1.211 1.00 67.44 ? 311 LEU A O 1 ATOM 2465 C CB . LEU A 1 312 ? 16.486 -24.391 0.917 1.00 64.94 ? 311 LEU A CB 1 ATOM 2466 C CG . LEU A 1 312 ? 17.582 -24.059 1.937 1.00 64.78 ? 311 LEU A CG 1 ATOM 2467 C CD1 . LEU A 1 312 ? 16.963 -23.379 3.152 1.00 64.24 ? 311 LEU A CD1 1 ATOM 2468 C CD2 . LEU A 1 312 ? 18.366 -25.296 2.354 1.00 66.06 ? 311 LEU A CD2 1 ATOM 2469 N N . VAL A 1 313 ? 15.876 -26.868 -1.559 1.00 68.77 ? 312 VAL A N 1 ATOM 2470 C CA . VAL A 1 313 ? 14.844 -27.572 -2.311 1.00 69.90 ? 312 VAL A CA 1 ATOM 2471 C C . VAL A 1 313 ? 14.518 -28.917 -1.660 1.00 70.16 ? 312 VAL A C 1 ATOM 2472 O O . VAL A 1 313 ? 15.323 -29.848 -1.698 1.00 70.45 ? 312 VAL A O 1 ATOM 2473 C CB . VAL A 1 313 ? 15.296 -27.812 -3.764 1.00 72.04 ? 312 VAL A CB 1 ATOM 2474 C CG1 . VAL A 1 313 ? 14.134 -28.322 -4.605 1.00 73.90 ? 312 VAL A CG1 1 ATOM 2475 C CG2 . VAL A 1 313 ? 15.876 -26.533 -4.357 1.00 72.73 ? 312 VAL A CG2 1 ATOM 2476 N N . LEU A 1 314 ? 13.334 -29.010 -1.061 1.00 70.58 ? 313 LEU A N 1 ATOM 2477 C CA . LEU A 1 314 ? 12.871 -30.266 -0.480 1.00 71.74 ? 313 LEU A CA 1 ATOM 2478 C C . LEU A 1 314 ? 12.283 -31.138 -1.570 1.00 73.31 ? 313 LEU A C 1 ATOM 2479 O O . LEU A 1 314 ? 11.503 -30.662 -2.389 1.00 74.55 ? 313 LEU A O 1 ATOM 2480 C CB . LEU A 1 314 ? 11.822 -30.027 0.615 1.00 72.64 ? 313 LEU A CB 1 ATOM 2481 C CG . LEU A 1 314 ? 12.350 -29.934 2.050 1.00 72.51 ? 313 LEU A CG 1 ATOM 2482 C CD1 . LEU A 1 314 ? 11.254 -29.465 2.994 1.00 74.28 ? 313 LEU A CD1 1 ATOM 2483 C CD2 . LEU A 1 314 ? 12.916 -31.268 2.515 1.00 73.82 ? 313 LEU A CD2 1 ATOM 2484 N N . ALA A 1 315 ? 12.668 -32.412 -1.581 1.00 74.45 ? 314 ALA A N 1 ATOM 2485 C CA . ALA A 1 315 ? 12.077 -33.390 -2.491 1.00 76.15 ? 314 ALA A CA 1 ATOM 2486 C C . ALA A 1 315 ? 10.775 -33.883 -1.887 1.00 78.17 ? 314 ALA A C 1 ATOM 2487 O O . ALA A 1 315 ? 10.709 -34.155 -0.683 1.00 78.44 ? 314 ALA A O 1 ATOM 2488 C CB . ALA A 1 315 ? 13.021 -34.557 -2.718 1.00 76.61 ? 314 ALA A CB 1 ATOM 2489 N N . THR A 1 316 ? 9.742 -33.972 -2.721 1.00 80.36 ? 315 THR A N 1 ATOM 2490 C CA . THR A 1 316 ? 8.432 -34.463 -2.299 1.00 83.34 ? 315 THR A CA 1 ATOM 2491 C C . THR A 1 316 ? 8.023 -35.710 -3.084 1.00 85.53 ? 315 THR A C 1 ATOM 2492 O O . THR A 1 316 ? 7.535 -36.679 -2.497 1.00 87.50 ? 315 THR A O 1 ATOM 2493 C CB . THR A 1 316 ? 7.355 -33.376 -2.455 1.00 85.46 ? 315 THR A CB 1 ATOM 2494 O OG1 . THR A 1 316 ? 7.405 -32.827 -3.778 1.00 85.90 ? 315 THR A OG1 1 ATOM 2495 C CG2 . THR A 1 316 ? 7.577 -32.262 -1.444 1.00 84.35 ? 315 THR A CG2 1 ATOM 2496 N N . GLY A 1 317 ? 8.221 -35.679 -4.403 1.00 85.75 ? 316 GLY A N 1 ATOM 2497 C CA . GLY A 1 317 ? 7.900 -36.812 -5.273 1.00 87.48 ? 316 GLY A CA 1 ATOM 2498 C C . GLY A 1 317 ? 9.054 -37.779 -5.459 1.00 86.20 ? 316 GLY A C 1 ATOM 2499 O O . GLY A 1 317 ? 9.997 -37.792 -4.672 1.00 84.56 ? 316 GLY A O 1 ATOM 2500 N N . LEU A 1 318 ? 8.967 -38.592 -6.508 1.00 88.05 ? 317 LEU A N 1 ATOM 2501 C CA . LEU A 1 318 ? 9.972 -39.613 -6.816 1.00 88.03 ? 317 LEU A CA 1 ATOM 2502 C C . LEU A 1 318 ? 11.013 -39.104 -7.814 1.00 88.06 ? 317 LEU A C 1 ATOM 2503 O O . LEU A 1 318 ? 10.952 -37.961 -8.259 1.00 87.72 ? 317 LEU A O 1 ATOM 2504 C CB . LEU A 1 318 ? 9.292 -40.863 -7.386 1.00 90.39 ? 317 LEU A CB 1 ATOM 2505 C CG . LEU A 1 318 ? 8.302 -41.584 -6.469 1.00 91.72 ? 317 LEU A CG 1 ATOM 2506 C CD1 . LEU A 1 318 ? 6.933 -40.912 -6.465 1.00 93.73 ? 317 LEU A CD1 1 ATOM 2507 C CD2 . LEU A 1 318 ? 8.188 -43.046 -6.884 1.00 93.46 ? 317 LEU A CD2 1 ATOM 2508 N N . ARG A 1 319 ? 11.960 -39.973 -8.164 1.00 89.18 ? 318 ARG A N 1 ATOM 2509 C CA . ARG A 1 319 ? 13.014 -39.657 -9.129 1.00 90.70 ? 318 ARG A CA 1 ATOM 2510 C C . ARG A 1 319 ? 12.489 -39.563 -10.563 1.00 93.81 ? 318 ARG A C 1 ATOM 2511 O O . ARG A 1 319 ? 11.325 -39.865 -10.829 1.00 95.04 ? 318 ARG A O 1 ATOM 2512 C CB . ARG A 1 319 ? 14.095 -40.740 -9.084 1.00 91.72 ? 318 ARG A CB 1 ATOM 2513 C CG . ARG A 1 319 ? 14.804 -40.872 -7.751 1.00 90.27 ? 318 ARG A CG 1 ATOM 2514 C CD . ARG A 1 319 ? 15.536 -42.197 -7.663 1.00 92.48 ? 318 ARG A CD 1 ATOM 2515 N NE . ARG A 1 319 ? 16.560 -42.174 -6.625 1.00 93.00 ? 318 ARG A NE 1 ATOM 2516 C CZ . ARG A 1 319 ? 17.765 -41.616 -6.752 1.00 94.43 ? 318 ARG A CZ 1 ATOM 2517 N NH1 . ARG A 1 319 ? 18.129 -41.016 -7.885 1.00 95.38 ? 318 ARG A NH1 1 ATOM 2518 N NH2 . ARG A 1 319 ? 18.617 -41.658 -5.730 1.00 95.41 ? 318 ARG A NH2 1 ATOM 2519 N N . ASN A 1 320 ? 13.366 -39.138 -11.474 1.00 96.27 ? 319 ASN A N 1 ATOM 2520 C CA . ASN A 1 320 ? 13.101 -39.154 -12.916 1.00 100.31 ? 319 ASN A CA 1 ATOM 2521 C C . ASN A 1 320 ? 14.338 -39.565 -13.706 1.00 103.65 ? 319 ASN A C 1 ATOM 2522 O O . ASN A 1 320 ? 14.228 -40.145 -14.787 1.00 107.35 ? 319 ASN A O 1 ATOM 2523 C CB . ASN A 1 320 ? 12.619 -37.780 -13.400 1.00 101.52 ? 319 ASN A CB 1 ATOM 2524 C CG . ASN A 1 320 ? 11.106 -37.665 -13.444 1.00 102.03 ? 319 ASN A CG 1 ATOM 2525 O OD1 . ASN A 1 320 ? 10.389 -38.667 -13.459 1.00 102.54 ? 319 ASN A OD1 1 ATOM 2526 N ND2 . ASN A 1 320 ? 10.613 -36.435 -13.483 1.00 102.66 ? 319 ASN A ND2 1 ATOM 2527 N N . ILE B 2 10 ? 12.942 -52.823 -11.495 1.00 152.34 ? 10 ILE B N 1 ATOM 2528 C CA . ILE B 2 10 ? 12.127 -52.004 -12.442 1.00 151.98 ? 10 ILE B CA 1 ATOM 2529 C C . ILE B 2 10 ? 13.037 -51.143 -13.316 1.00 150.99 ? 10 ILE B C 1 ATOM 2530 O O . ILE B 2 10 ? 14.034 -50.598 -12.839 1.00 150.38 ? 10 ILE B O 1 ATOM 2531 C CB . ILE B 2 10 ? 11.117 -51.101 -11.694 1.00 151.91 ? 10 ILE B CB 1 ATOM 2532 C CG1 . ILE B 2 10 ? 10.294 -51.943 -10.709 1.00 153.01 ? 10 ILE B CG1 1 ATOM 2533 C CG2 . ILE B 2 10 ? 10.216 -50.363 -12.683 1.00 151.64 ? 10 ILE B CG2 1 ATOM 2534 C CD1 . ILE B 2 10 ? 9.104 -51.233 -10.098 1.00 153.22 ? 10 ILE B CD1 1 ATOM 2535 N N . GLU B 2 11 ? 12.685 -51.028 -14.596 1.00 150.90 ? 11 GLU B N 1 ATOM 2536 C CA . GLU B 2 11 ? 13.443 -50.209 -15.537 1.00 150.10 ? 11 GLU B CA 1 ATOM 2537 C C . GLU B 2 11 ? 13.294 -48.730 -15.189 1.00 149.33 ? 11 GLU B C 1 ATOM 2538 O O . GLU B 2 11 ? 14.279 -48.052 -14.890 1.00 148.61 ? 11 GLU B O 1 ATOM 2539 C CB . GLU B 2 11 ? 12.971 -50.462 -16.973 1.00 150.32 ? 11 GLU B CB 1 ATOM 2540 N N . GLY B 2 12 ? 12.055 -48.243 -15.217 1.00 149.46 ? 12 GLY B N 1 ATOM 2541 C CA . GLY B 2 12 ? 11.768 -46.838 -14.932 1.00 148.85 ? 12 GLY B CA 1 ATOM 2542 C C . GLY B 2 12 ? 10.310 -46.581 -14.598 1.00 149.24 ? 12 GLY B C 1 ATOM 2543 O O . GLY B 2 12 ? 9.536 -47.517 -14.383 1.00 149.89 ? 12 GLY B O 1 ATOM 2544 N N . GLY B 2 13 ? 9.942 -45.303 -14.554 1.00 148.86 ? 13 GLY B N 1 ATOM 2545 C CA . GLY B 2 13 ? 8.580 -44.891 -14.223 1.00 149.29 ? 13 GLY B CA 1 ATOM 2546 C C . GLY B 2 13 ? 7.669 -44.841 -15.434 1.00 149.45 ? 13 GLY B C 1 ATOM 2547 O O . GLY B 2 13 ? 8.120 -45.013 -16.568 1.00 149.29 ? 13 GLY B O 1 ATOM 2548 N N . TRP B 2 14 ? 6.384 -44.600 -15.189 1.00 149.88 ? 14 TRP B N 1 ATOM 2549 C CA . TRP B 2 14 ? 5.385 -44.536 -16.252 1.00 150.09 ? 14 TRP B CA 1 ATOM 2550 C C . TRP B 2 14 ? 4.789 -43.136 -16.374 1.00 149.90 ? 14 TRP B C 1 ATOM 2551 O O . TRP B 2 14 ? 4.175 -42.633 -15.431 1.00 150.17 ? 14 TRP B O 1 ATOM 2552 C CB . TRP B 2 14 ? 4.260 -45.542 -15.990 1.00 150.94 ? 14 TRP B CB 1 ATOM 2553 C CG . TRP B 2 14 ? 4.721 -46.963 -15.848 1.00 151.37 ? 14 TRP B CG 1 ATOM 2554 C CD1 . TRP B 2 14 ? 5.819 -47.536 -16.426 1.00 151.09 ? 14 TRP B CD1 1 ATOM 2555 C CD2 . TRP B 2 14 ? 4.077 -47.998 -15.099 1.00 152.27 ? 14 TRP B CD2 1 ATOM 2556 N NE1 . TRP B 2 14 ? 5.906 -48.859 -16.069 1.00 151.80 ? 14 TRP B NE1 1 ATOM 2557 C CE2 . TRP B 2 14 ? 4.848 -49.170 -15.257 1.00 152.55 ? 14 TRP B CE2 1 ATOM 2558 C CE3 . TRP B 2 14 ? 2.926 -48.048 -14.303 1.00 153.00 ? 14 TRP B CE3 1 ATOM 2559 C CZ2 . TRP B 2 14 ? 4.505 -50.379 -14.651 1.00 153.58 ? 14 TRP B CZ2 1 ATOM 2560 C CZ3 . TRP B 2 14 ? 2.586 -49.250 -13.701 1.00 154.06 ? 14 TRP B CZ3 1 ATOM 2561 C CH2 . TRP B 2 14 ? 3.373 -50.399 -13.881 1.00 154.36 ? 14 TRP B CH2 1 ATOM 2562 N N . GLN B 2 15 ? 4.968 -42.517 -17.538 1.00 149.57 ? 15 GLN B N 1 ATOM 2563 C CA . GLN B 2 15 ? 4.327 -41.235 -17.839 1.00 149.46 ? 15 GLN B CA 1 ATOM 2564 C C . GLN B 2 15 ? 2.825 -41.394 -18.048 1.00 150.18 ? 15 GLN B C 1 ATOM 2565 O O . GLN B 2 15 ? 2.065 -40.443 -17.858 1.00 150.08 ? 15 GLN B O 1 ATOM 2566 C CB . GLN B 2 15 ? 4.945 -40.597 -19.082 1.00 148.88 ? 15 GLN B CB 1 ATOM 2567 C CG . GLN B 2 15 ? 6.368 -40.109 -18.877 1.00 148.35 ? 15 GLN B CG 1 ATOM 2568 C CD . GLN B 2 15 ? 6.801 -39.116 -19.939 1.00 147.89 ? 15 GLN B CD 1 ATOM 2569 O OE1 . GLN B 2 15 ? 6.293 -39.126 -21.061 1.00 147.84 ? 15 GLN B OE1 1 ATOM 2570 N NE2 . GLN B 2 15 ? 7.746 -38.251 -19.589 1.00 147.51 ? 15 GLN B NE2 1 ATOM 2571 N N . GLY B 2 16 ? 2.410 -42.594 -18.451 1.00 150.92 ? 16 GLY B N 1 ATOM 2572 C CA . GLY B 2 16 ? 1.000 -42.907 -18.651 1.00 151.81 ? 16 GLY B CA 1 ATOM 2573 C C . GLY B 2 16 ? 0.160 -42.730 -17.401 1.00 152.63 ? 16 GLY B C 1 ATOM 2574 O O . GLY B 2 16 ? -0.965 -42.237 -17.474 1.00 153.03 ? 16 GLY B O 1 ATOM 2575 N N . MET B 2 17 ? 0.704 -43.129 -16.253 1.00 153.12 ? 17 MET B N 1 ATOM 2576 C CA . MET B 2 17 ? -0.002 -42.995 -14.980 1.00 154.01 ? 17 MET B CA 1 ATOM 2577 C C . MET B 2 17 ? 0.154 -41.582 -14.418 1.00 153.65 ? 17 MET B C 1 ATOM 2578 O O . MET B 2 17 ? 1.185 -41.248 -13.836 1.00 153.34 ? 17 MET B O 1 ATOM 2579 C CB . MET B 2 17 ? 0.506 -44.026 -13.965 1.00 154.61 ? 17 MET B CB 1 ATOM 2580 C CG . MET B 2 17 ? -0.252 -44.010 -12.643 1.00 155.53 ? 17 MET B CG 1 ATOM 2581 S SD . MET B 2 17 ? 0.078 -45.444 -11.601 1.00 156.44 ? 17 MET B SD 1 ATOM 2582 C CE . MET B 2 17 ? 1.857 -45.343 -11.420 1.00 155.52 ? 17 MET B CE 1 ATOM 2583 N N . VAL B 2 18 ? -0.878 -40.761 -14.601 1.00 153.89 ? 18 VAL B N 1 ATOM 2584 C CA . VAL B 2 18 ? -0.927 -39.415 -14.031 1.00 153.78 ? 18 VAL B CA 1 ATOM 2585 C C . VAL B 2 18 ? -1.922 -39.330 -12.869 1.00 154.76 ? 18 VAL B C 1 ATOM 2586 O O . VAL B 2 18 ? -2.173 -38.244 -12.344 1.00 154.81 ? 18 VAL B O 1 ATOM 2587 C CB . VAL B 2 18 ? -1.326 -38.381 -15.100 1.00 153.35 ? 18 VAL B CB 1 ATOM 2588 N N . ASP B 2 19 ? -2.476 -40.475 -12.466 1.00 155.59 ? 19 ASP B N 1 ATOM 2589 C CA . ASP B 2 19 ? -3.497 -40.525 -11.416 1.00 156.62 ? 19 ASP B CA 1 ATOM 2590 C C . ASP B 2 19 ? -2.891 -40.238 -10.041 1.00 156.83 ? 19 ASP B C 1 ATOM 2591 O O . ASP B 2 19 ? -3.277 -39.273 -9.378 1.00 157.19 ? 19 ASP B O 1 ATOM 2592 C CB . ASP B 2 19 ? -4.203 -41.892 -11.406 1.00 157.39 ? 19 ASP B CB 1 ATOM 2593 C CG . ASP B 2 19 ? -5.035 -42.144 -12.661 1.00 157.32 ? 19 ASP B CG 1 ATOM 2594 O OD1 . ASP B 2 19 ? -5.630 -41.188 -13.202 1.00 157.01 ? 19 ASP B OD1 1 ATOM 2595 O OD2 . ASP B 2 19 ? -5.107 -43.313 -13.098 1.00 157.45 ? 19 ASP B OD2 1 ATOM 2596 N N . GLY B 2 20 ? -1.945 -41.078 -9.625 1.00 156.72 ? 20 GLY B N 1 ATOM 2597 C CA . GLY B 2 20 ? -1.269 -40.926 -8.332 1.00 156.85 ? 20 GLY B CA 1 ATOM 2598 C C . GLY B 2 20 ? 0.230 -41.116 -8.458 1.00 155.92 ? 20 GLY B C 1 ATOM 2599 O O . GLY B 2 20 ? 0.784 -40.989 -9.549 1.00 155.06 ? 20 GLY B O 1 ATOM 2600 N N . TRP B 2 21 ? 0.885 -41.418 -7.339 1.00 156.21 ? 21 TRP B N 1 ATOM 2601 C CA . TRP B 2 21 ? 2.331 -41.658 -7.331 1.00 155.49 ? 21 TRP B CA 1 ATOM 2602 C C . TRP B 2 21 ? 2.649 -43.123 -7.627 1.00 155.73 ? 21 TRP B C 1 ATOM 2603 O O . TRP B 2 21 ? 3.453 -43.414 -8.512 1.00 155.01 ? 21 TRP B O 1 ATOM 2604 C CB . TRP B 2 21 ? 2.964 -41.228 -5.998 1.00 155.54 ? 21 TRP B CB 1 ATOM 2605 C CG . TRP B 2 21 ? 3.234 -39.740 -5.881 1.00 155.02 ? 21 TRP B CG 1 ATOM 2606 C CD1 . TRP B 2 21 ? 3.663 -38.899 -6.871 1.00 154.13 ? 21 TRP B CD1 1 ATOM 2607 C CD2 . TRP B 2 21 ? 3.126 -38.936 -4.696 1.00 155.37 ? 21 TRP B CD2 1 ATOM 2608 N NE1 . TRP B 2 21 ? 3.809 -37.624 -6.382 1.00 153.94 ? 21 TRP B NE1 1 ATOM 2609 C CE2 . TRP B 2 21 ? 3.487 -37.619 -5.050 1.00 154.71 ? 21 TRP B CE2 1 ATOM 2610 C CE3 . TRP B 2 21 ? 2.751 -39.201 -3.373 1.00 156.31 ? 21 TRP B CE3 1 ATOM 2611 C CZ2 . TRP B 2 21 ? 3.485 -36.568 -4.130 1.00 155.07 ? 21 TRP B CZ2 1 ATOM 2612 C CZ3 . TRP B 2 21 ? 2.750 -38.155 -2.457 1.00 156.62 ? 21 TRP B CZ3 1 ATOM 2613 C CH2 . TRP B 2 21 ? 3.114 -36.855 -2.842 1.00 155.99 ? 21 TRP B CH2 1 ATOM 2614 N N . TYR B 2 22 ? 2.018 -44.035 -6.888 1.00 156.82 ? 22 TYR B N 1 ATOM 2615 C CA . TYR B 2 22 ? 2.197 -45.478 -7.103 1.00 157.25 ? 22 TYR B CA 1 ATOM 2616 C C . TYR B 2 22 ? 0.917 -46.087 -7.660 1.00 158.03 ? 22 TYR B C 1 ATOM 2617 O O . TYR B 2 22 ? -0.168 -45.524 -7.502 1.00 158.44 ? 22 TYR B O 1 ATOM 2618 C CB . TYR B 2 22 ? 2.562 -46.198 -5.800 1.00 157.91 ? 22 TYR B CB 1 ATOM 2619 C CG . TYR B 2 22 ? 3.319 -45.357 -4.799 1.00 157.44 ? 22 TYR B CG 1 ATOM 2620 C CD1 . TYR B 2 22 ? 4.665 -45.057 -4.985 1.00 156.38 ? 22 TYR B CD1 1 ATOM 2621 C CD2 . TYR B 2 22 ? 2.687 -44.872 -3.659 1.00 158.16 ? 22 TYR B CD2 1 ATOM 2622 C CE1 . TYR B 2 22 ? 5.358 -44.289 -4.064 1.00 156.03 ? 22 TYR B CE1 1 ATOM 2623 C CE2 . TYR B 2 22 ? 3.370 -44.106 -2.734 1.00 157.86 ? 22 TYR B CE2 1 ATOM 2624 C CZ . TYR B 2 22 ? 4.704 -43.817 -2.939 1.00 156.80 ? 22 TYR B CZ 1 ATOM 2625 O OH . TYR B 2 22 ? 5.384 -43.053 -2.018 1.00 156.56 ? 22 TYR B OH 1 ATOM 2626 N N . GLY B 2 23 ? 1.044 -47.246 -8.298 1.00 158.30 ? 23 GLY B N 1 ATOM 2627 C CA . GLY B 2 23 ? -0.118 -47.936 -8.844 1.00 159.20 ? 23 GLY B CA 1 ATOM 2628 C C . GLY B 2 23 ? 0.197 -49.162 -9.678 1.00 159.43 ? 23 GLY B C 1 ATOM 2629 O O . GLY B 2 23 ? 1.305 -49.701 -9.623 1.00 159.06 ? 23 GLY B O 1 ATOM 2630 N N . TYR B 2 24 ? -0.796 -49.589 -10.456 1.00 160.07 ? 24 TYR B N 1 ATOM 2631 C CA . TYR B 2 24 ? -0.709 -50.799 -11.266 1.00 160.54 ? 24 TYR B CA 1 ATOM 2632 C C . TYR B 2 24 ? -1.027 -50.494 -12.728 1.00 160.13 ? 24 TYR B C 1 ATOM 2633 O O . TYR B 2 24 ? -1.810 -49.589 -13.023 1.00 159.88 ? 24 TYR B O 1 ATOM 2634 C CB . TYR B 2 24 ? -1.712 -51.846 -10.769 1.00 162.00 ? 24 TYR B CB 1 ATOM 2635 C CG . TYR B 2 24 ? -1.757 -52.058 -9.268 1.00 162.72 ? 24 TYR B CG 1 ATOM 2636 C CD1 . TYR B 2 24 ? -2.424 -51.166 -8.437 1.00 162.91 ? 24 TYR B CD1 1 ATOM 2637 C CD2 . TYR B 2 24 ? -1.163 -53.171 -8.685 1.00 163.36 ? 24 TYR B CD2 1 ATOM 2638 C CE1 . TYR B 2 24 ? -2.481 -51.365 -7.067 1.00 163.70 ? 24 TYR B CE1 1 ATOM 2639 C CE2 . TYR B 2 24 ? -1.214 -53.378 -7.316 1.00 164.12 ? 24 TYR B CE2 1 ATOM 2640 C CZ . TYR B 2 24 ? -1.873 -52.474 -6.512 1.00 164.28 ? 24 TYR B CZ 1 ATOM 2641 O OH . TYR B 2 24 ? -1.924 -52.681 -5.153 1.00 165.08 ? 24 TYR B OH 1 ATOM 2642 N N . HIS B 2 25 ? -0.413 -51.252 -13.635 1.00 160.14 ? 25 HIS B N 1 ATOM 2643 C CA . HIS B 2 25 ? -0.854 -51.314 -15.029 1.00 160.13 ? 25 HIS B CA 1 ATOM 2644 C C . HIS B 2 25 ? -1.224 -52.756 -15.360 1.00 161.31 ? 25 HIS B C 1 ATOM 2645 O O . HIS B 2 25 ? -0.352 -53.622 -15.446 1.00 161.45 ? 25 HIS B O 1 ATOM 2646 C CB . HIS B 2 25 ? 0.230 -50.827 -15.995 1.00 158.98 ? 25 HIS B CB 1 ATOM 2647 C CG . HIS B 2 25 ? -0.105 -51.063 -17.439 1.00 158.89 ? 25 HIS B CG 1 ATOM 2648 N ND1 . HIS B 2 25 ? -0.986 -50.266 -18.140 1.00 158.53 ? 25 HIS B ND1 1 ATOM 2649 C CD2 . HIS B 2 25 ? 0.310 -52.017 -18.306 1.00 159.10 ? 25 HIS B CD2 1 ATOM 2650 C CE1 . HIS B 2 25 ? -1.092 -50.714 -19.378 1.00 158.52 ? 25 HIS B CE1 1 ATOM 2651 N NE2 . HIS B 2 25 ? -0.316 -51.776 -19.505 1.00 158.90 ? 25 HIS B NE2 1 ATOM 2652 N N . HIS B 2 26 ? -2.516 -53.007 -15.543 1.00 162.31 ? 26 HIS B N 1 ATOM 2653 C CA . HIS B 2 26 ? -2.994 -54.340 -15.898 1.00 163.59 ? 26 HIS B CA 1 ATOM 2654 C C . HIS B 2 26 ? -3.053 -54.519 -17.413 1.00 163.29 ? 26 HIS B C 1 ATOM 2655 O O . HIS B 2 26 ? -3.246 -53.556 -18.159 1.00 162.50 ? 26 HIS B O 1 ATOM 2656 C CB . HIS B 2 26 ? -4.370 -54.613 -15.276 1.00 164.89 ? 26 HIS B CB 1 ATOM 2657 C CG . HIS B 2 26 ? -5.484 -53.807 -15.872 1.00 164.70 ? 26 HIS B CG 1 ATOM 2658 N ND1 . HIS B 2 26 ? -6.286 -54.282 -16.888 1.00 165.12 ? 26 HIS B ND1 1 ATOM 2659 C CD2 . HIS B 2 26 ? -5.933 -52.561 -15.590 1.00 164.09 ? 26 HIS B CD2 1 ATOM 2660 C CE1 . HIS B 2 26 ? -7.178 -53.361 -17.209 1.00 164.80 ? 26 HIS B CE1 1 ATOM 2661 N NE2 . HIS B 2 26 ? -6.984 -52.307 -16.437 1.00 164.22 ? 26 HIS B NE2 1 ATOM 2662 N N . SER B 2 27 ? -2.861 -55.759 -17.851 1.00 164.05 ? 27 SER B N 1 ATOM 2663 C CA . SER B 2 27 ? -3.101 -56.158 -19.232 1.00 164.02 ? 27 SER B CA 1 ATOM 2664 C C . SER B 2 27 ? -4.110 -57.300 -19.192 1.00 165.40 ? 27 SER B C 1 ATOM 2665 O O . SER B 2 27 ? -3.956 -58.236 -18.404 1.00 166.43 ? 27 SER B O 1 ATOM 2666 C CB . SER B 2 27 ? -1.800 -56.611 -19.896 1.00 163.68 ? 27 SER B CB 1 ATOM 2667 O OG . SER B 2 27 ? -2.000 -56.894 -21.269 1.00 163.81 ? 27 SER B OG 1 ATOM 2668 N N . ASN B 2 28 ? -5.143 -57.217 -20.029 1.00 165.45 ? 28 ASN B N 1 ATOM 2669 C CA . ASN B 2 28 ? -6.285 -58.124 -19.924 1.00 166.70 ? 28 ASN B CA 1 ATOM 2670 C C . ASN B 2 28 ? -6.993 -58.349 -21.255 1.00 166.85 ? 28 ASN B C 1 ATOM 2671 O O . ASN B 2 28 ? -6.885 -57.536 -22.173 1.00 165.78 ? 28 ASN B O 1 ATOM 2672 C CB . ASN B 2 28 ? -7.283 -57.561 -18.905 1.00 166.96 ? 28 ASN B CB 1 ATOM 2673 C CG . ASN B 2 28 ? -8.056 -58.641 -18.176 1.00 168.61 ? 28 ASN B CG 1 ATOM 2674 O OD1 . ASN B 2 28 ? -7.569 -59.754 -17.981 1.00 169.45 ? 28 ASN B OD1 1 ATOM 2675 N ND2 . ASN B 2 28 ? -9.265 -58.306 -17.748 1.00 169.19 ? 28 ASN B ND2 1 ATOM 2676 N N . GLU B 2 29 ? -7.720 -59.462 -21.343 1.00 168.25 ? 29 GLU B N 1 ATOM 2677 C CA . GLU B 2 29 ? -8.538 -59.787 -22.520 1.00 168.65 ? 29 GLU B CA 1 ATOM 2678 C C . GLU B 2 29 ? -9.608 -58.726 -22.814 1.00 168.02 ? 29 GLU B C 1 ATOM 2679 O O . GLU B 2 29 ? -9.982 -58.517 -23.970 1.00 167.63 ? 29 GLU B O 1 ATOM 2680 C CB . GLU B 2 29 ? -9.187 -61.178 -22.377 1.00 170.46 ? 29 GLU B CB 1 ATOM 2681 C CG . GLU B 2 29 ? -10.244 -61.326 -21.279 1.00 171.54 ? 29 GLU B CG 1 ATOM 2682 C CD . GLU B 2 29 ? -9.671 -61.398 -19.870 1.00 171.70 ? 29 GLU B CD 1 ATOM 2683 O OE1 . GLU B 2 29 ? -8.544 -61.911 -19.697 1.00 171.64 ? 29 GLU B OE1 1 ATOM 2684 O OE2 . GLU B 2 29 ? -10.354 -60.945 -18.927 1.00 171.86 ? 29 GLU B OE2 1 ATOM 2685 N N . GLN B 2 30 ? -10.095 -58.067 -21.764 1.00 167.91 ? 30 GLN B N 1 ATOM 2686 C CA . GLN B 2 30 ? -11.069 -56.984 -21.897 1.00 167.30 ? 30 GLN B CA 1 ATOM 2687 C C . GLN B 2 30 ? -10.395 -55.705 -22.394 1.00 165.51 ? 30 GLN B C 1 ATOM 2688 O O . GLN B 2 30 ? -10.796 -55.138 -23.411 1.00 164.98 ? 30 GLN B O 1 ATOM 2689 C CB . GLN B 2 30 ? -11.766 -56.729 -20.556 1.00 167.91 ? 30 GLN B CB 1 ATOM 2690 C CG . GLN B 2 30 ? -12.708 -57.848 -20.132 1.00 169.67 ? 30 GLN B CG 1 ATOM 2691 C CD . GLN B 2 30 ? -12.914 -57.911 -18.628 1.00 170.47 ? 30 GLN B CD 1 ATOM 2692 O OE1 . GLN B 2 30 ? -11.989 -58.224 -17.881 1.00 170.51 ? 30 GLN B OE1 1 ATOM 2693 N NE2 . GLN B 2 30 ? -14.132 -57.629 -18.179 1.00 171.19 ? 30 GLN B NE2 1 ATOM 2694 N N . GLY B 2 31 ? -9.372 -55.259 -21.671 1.00 164.61 ? 31 GLY B N 1 ATOM 2695 C CA . GLY B 2 31 ? -8.616 -54.064 -22.052 1.00 163.04 ? 31 GLY B CA 1 ATOM 2696 C C . GLY B 2 31 ? -7.313 -53.934 -21.284 1.00 162.45 ? 31 GLY B C 1 ATOM 2697 O O . GLY B 2 31 ? -6.836 -54.905 -20.694 1.00 163.32 ? 31 GLY B O 1 ATOM 2698 N N . SER B 2 32 ? -6.734 -52.733 -21.300 1.00 161.10 ? 32 SER B N 1 ATOM 2699 C CA . SER B 2 32 ? -5.506 -52.447 -20.551 1.00 160.28 ? 32 SER B CA 1 ATOM 2700 C C . SER B 2 32 ? -5.414 -50.967 -20.188 1.00 159.23 ? 32 SER B C 1 ATOM 2701 O O . SER B 2 32 ? -5.642 -50.099 -21.030 1.00 158.36 ? 32 SER B O 1 ATOM 2702 C CB . SER B 2 32 ? -4.270 -52.855 -21.357 1.00 159.74 ? 32 SER B CB 1 ATOM 2703 O OG . SER B 2 32 ? -4.040 -51.963 -22.434 1.00 158.68 ? 32 SER B OG 1 ATOM 2704 N N . GLY B 2 33 ? -5.072 -50.691 -18.932 1.00 159.35 ? 33 GLY B N 1 ATOM 2705 C CA . GLY B 2 33 ? -4.941 -49.319 -18.450 1.00 158.60 ? 33 GLY B CA 1 ATOM 2706 C C . GLY B 2 33 ? -4.246 -49.229 -17.103 1.00 158.64 ? 33 GLY B C 1 ATOM 2707 O O . GLY B 2 33 ? -3.900 -50.247 -16.501 1.00 159.32 ? 33 GLY B O 1 ATOM 2708 N N . TYR B 2 34 ? -4.051 -47.999 -16.632 1.00 157.96 ? 34 TYR B N 1 ATOM 2709 C CA . TYR B 2 34 ? -3.354 -47.737 -15.371 1.00 157.82 ? 34 TYR B CA 1 ATOM 2710 C C . TYR B 2 34 ? -4.345 -47.529 -14.227 1.00 158.77 ? 34 TYR B C 1 ATOM 2711 O O . TYR B 2 34 ? -5.501 -47.169 -14.455 1.00 159.23 ? 34 TYR B O 1 ATOM 2712 C CB . TYR B 2 34 ? -2.455 -46.507 -15.515 1.00 156.52 ? 34 TYR B CB 1 ATOM 2713 C CG . TYR B 2 34 ? -1.482 -46.612 -16.666 1.00 155.65 ? 34 TYR B CG 1 ATOM 2714 C CD1 . TYR B 2 34 ? -0.230 -47.192 -16.493 1.00 155.38 ? 34 TYR B CD1 1 ATOM 2715 C CD2 . TYR B 2 34 ? -1.818 -46.142 -17.934 1.00 155.15 ? 34 TYR B CD2 1 ATOM 2716 C CE1 . TYR B 2 34 ? 0.663 -47.298 -17.546 1.00 154.74 ? 34 TYR B CE1 1 ATOM 2717 C CE2 . TYR B 2 34 ? -0.932 -46.243 -18.994 1.00 154.50 ? 34 TYR B CE2 1 ATOM 2718 C CZ . TYR B 2 34 ? 0.308 -46.822 -18.795 1.00 154.33 ? 34 TYR B CZ 1 ATOM 2719 O OH . TYR B 2 34 ? 1.191 -46.923 -19.844 1.00 153.81 ? 34 TYR B OH 1 ATOM 2720 N N . ALA B 2 35 ? -3.886 -47.758 -12.999 1.00 159.15 ? 35 ALA B N 1 ATOM 2721 C CA . ALA B 2 35 ? -4.732 -47.612 -11.815 1.00 160.09 ? 35 ALA B CA 1 ATOM 2722 C C . ALA B 2 35 ? -3.890 -47.317 -10.577 1.00 160.00 ? 35 ALA B C 1 ATOM 2723 O O . ALA B 2 35 ? -3.104 -48.159 -10.142 1.00 160.05 ? 35 ALA B O 1 ATOM 2724 C CB . ALA B 2 35 ? -5.560 -48.870 -11.603 1.00 161.43 ? 35 ALA B CB 1 ATOM 2725 N N . ALA B 2 36 ? -4.067 -46.122 -10.014 1.00 159.87 ? 36 ALA B N 1 ATOM 2726 C CA . ALA B 2 36 ? -3.295 -45.686 -8.848 1.00 159.81 ? 36 ALA B CA 1 ATOM 2727 C C . ALA B 2 36 ? -3.822 -46.313 -7.558 1.00 161.18 ? 36 ALA B C 1 ATOM 2728 O O . ALA B 2 36 ? -5.033 -46.410 -7.358 1.00 162.18 ? 36 ALA B O 1 ATOM 2729 C CB . ALA B 2 36 ? -3.312 -44.167 -8.738 1.00 159.17 ? 36 ALA B CB 1 ATOM 2730 N N . ASP B 2 37 ? -2.903 -46.731 -6.687 1.00 161.29 ? 37 ASP B N 1 ATOM 2731 C CA . ASP B 2 37 ? -3.261 -47.283 -5.382 1.00 162.53 ? 37 ASP B CA 1 ATOM 2732 C C . ASP B 2 37 ? -3.506 -46.131 -4.409 1.00 162.81 ? 37 ASP B C 1 ATOM 2733 O O . ASP B 2 37 ? -2.568 -45.446 -4.001 1.00 162.04 ? 37 ASP B O 1 ATOM 2734 C CB . ASP B 2 37 ? -2.145 -48.200 -4.865 1.00 162.44 ? 37 ASP B CB 1 ATOM 2735 C CG . ASP B 2 37 ? -2.500 -48.889 -3.551 1.00 163.79 ? 37 ASP B CG 1 ATOM 2736 O OD1 . ASP B 2 37 ? -3.691 -48.910 -3.169 1.00 164.85 ? 37 ASP B OD1 1 ATOM 2737 O OD2 . ASP B 2 37 ? -1.578 -49.420 -2.898 1.00 163.81 ? 37 ASP B OD2 1 ATOM 2738 N N . LYS B 2 38 ? -4.771 -45.924 -4.047 1.00 134.00 ? 38 LYS B N 1 ATOM 2739 C CA . LYS B 2 38 ? -5.154 -44.829 -3.151 1.00 131.75 ? 38 LYS B CA 1 ATOM 2740 C C . LYS B 2 38 ? -4.829 -45.119 -1.684 1.00 125.94 ? 38 LYS B C 1 ATOM 2741 O O . LYS B 2 38 ? -4.737 -44.193 -0.878 1.00 124.44 ? 38 LYS B O 1 ATOM 2742 C CB . LYS B 2 38 ? -6.645 -44.511 -3.297 1.00 135.15 ? 38 LYS B CB 1 ATOM 2743 C CG . LYS B 2 38 ? -7.032 -44.000 -4.675 1.00 143.08 ? 38 LYS B CG 1 ATOM 2744 N N . GLU B 2 39 ? -4.665 -46.396 -1.339 1.00 124.22 ? 39 GLU B N 1 ATOM 2745 C CA . GLU B 2 39 ? -4.287 -46.787 0.020 1.00 121.00 ? 39 GLU B CA 1 ATOM 2746 C C . GLU B 2 39 ? -2.846 -46.381 0.333 1.00 119.77 ? 39 GLU B C 1 ATOM 2747 O O . GLU B 2 39 ? -2.566 -45.869 1.417 1.00 117.91 ? 39 GLU B O 1 ATOM 2748 C CB . GLU B 2 39 ? -4.457 -48.295 0.216 1.00 121.49 ? 39 GLU B CB 1 ATOM 2749 N N . SER B 2 40 ? -1.943 -46.606 -0.622 1.00 122.14 ? 40 SER B N 1 ATOM 2750 C CA . SER B 2 40 ? -0.520 -46.283 -0.452 1.00 122.15 ? 40 SER B CA 1 ATOM 2751 C C . SER B 2 40 ? -0.187 -44.824 -0.800 1.00 122.16 ? 40 SER B C 1 ATOM 2752 O O . SER B 2 40 ? 0.756 -44.256 -0.248 1.00 120.54 ? 40 SER B O 1 ATOM 2753 C CB . SER B 2 40 ? 0.343 -47.234 -1.289 1.00 126.86 ? 40 SER B CB 1 ATOM 2754 O OG . SER B 2 40 ? 0.135 -47.036 -2.675 1.00 131.26 ? 40 SER B OG 1 ATOM 2755 N N . THR B 2 41 ? -0.951 -44.229 -1.717 1.00 125.07 ? 41 THR B N 1 ATOM 2756 C CA . THR B 2 41 ? -0.775 -42.819 -2.089 1.00 127.00 ? 41 THR B CA 1 ATOM 2757 C C . THR B 2 41 ? -1.263 -41.885 -0.979 1.00 123.80 ? 41 THR B C 1 ATOM 2758 O O . THR B 2 41 ? -0.665 -40.836 -0.739 1.00 123.40 ? 41 THR B O 1 ATOM 2759 C CB . THR B 2 41 ? -1.515 -42.475 -3.401 1.00 133.49 ? 41 THR B CB 1 ATOM 2760 O OG1 . THR B 2 41 ? -0.998 -43.278 -4.470 1.00 138.57 ? 41 THR B OG1 1 ATOM 2761 C CG2 . THR B 2 41 ? -1.350 -40.997 -3.760 1.00 137.13 ? 41 THR B CG2 1 ATOM 2762 N N . GLN B 2 42 ? -2.354 -42.266 -0.315 1.00 122.76 ? 42 GLN B N 1 ATOM 2763 C CA . GLN B 2 42 ? -2.865 -41.516 0.834 1.00 121.58 ? 42 GLN B CA 1 ATOM 2764 C C . GLN B 2 42 ? -1.865 -41.524 1.989 1.00 117.95 ? 42 GLN B C 1 ATOM 2765 O O . GLN B 2 42 ? -1.765 -40.545 2.727 1.00 117.58 ? 42 GLN B O 1 ATOM 2766 C CB . GLN B 2 42 ? -4.204 -42.090 1.307 1.00 122.73 ? 42 GLN B CB 1 ATOM 2767 N N . LYS B 2 43 ? -1.132 -42.628 2.137 1.00 116.64 ? 43 LYS B N 1 ATOM 2768 C CA . LYS B 2 43 ? -0.094 -42.748 3.164 1.00 115.01 ? 43 LYS B CA 1 ATOM 2769 C C . LYS B 2 43 ? 1.152 -41.914 2.832 1.00 114.64 ? 43 LYS B C 1 ATOM 2770 O O . LYS B 2 43 ? 1.796 -41.375 3.734 1.00 113.29 ? 43 LYS B O 1 ATOM 2771 C CB . LYS B 2 43 ? 0.300 -44.218 3.355 1.00 115.91 ? 43 LYS B CB 1 ATOM 2772 C CG . LYS B 2 43 ? 1.169 -44.475 4.576 1.00 116.16 ? 43 LYS B CG 1 ATOM 2773 N N . ALA B 2 44 ? 1.484 -41.811 1.545 1.00 117.02 ? 44 ALA B N 1 ATOM 2774 C CA . ALA B 2 44 ? 2.671 -41.066 1.101 1.00 118.06 ? 44 ALA B CA 1 ATOM 2775 C C . ALA B 2 44 ? 2.470 -39.546 1.128 1.00 118.02 ? 44 ALA B C 1 ATOM 2776 O O . ALA B 2 44 ? 3.395 -38.806 1.464 1.00 117.01 ? 44 ALA B O 1 ATOM 2777 C CB . ALA B 2 44 ? 3.093 -41.517 -0.289 1.00 122.85 ? 44 ALA B CB 1 ATOM 2778 N N . ILE B 2 45 ? 1.273 -39.086 0.767 1.00 120.18 ? 45 ILE B N 1 ATOM 2779 C CA . ILE B 2 45 ? 0.941 -37.655 0.819 1.00 122.25 ? 45 ILE B CA 1 ATOM 2780 C C . ILE B 2 45 ? 0.984 -37.136 2.262 1.00 119.13 ? 45 ILE B C 1 ATOM 2781 O O . ILE B 2 45 ? 1.460 -36.026 2.513 1.00 119.33 ? 45 ILE B O 1 ATOM 2782 C CB . ILE B 2 45 ? -0.446 -37.364 0.189 1.00 127.26 ? 45 ILE B CB 1 ATOM 2783 C CG1 . ILE B 2 45 ? -0.402 -37.603 -1.324 1.00 132.65 ? 45 ILE B CG1 1 ATOM 2784 C CG2 . ILE B 2 45 ? -0.889 -35.929 0.468 1.00 130.77 ? 45 ILE B CG2 1 ATOM 2785 C CD1 . ILE B 2 45 ? -1.764 -37.702 -1.979 1.00 138.08 ? 45 ILE B CD1 1 ATOM 2786 N N . ASP B 2 46 ? 0.492 -37.948 3.198 1.00 117.32 ? 46 ASP B N 1 ATOM 2787 C CA . ASP B 2 46 ? 0.484 -37.588 4.618 1.00 116.28 ? 46 ASP B CA 1 ATOM 2788 C C . ASP B 2 46 ? 1.894 -37.569 5.205 1.00 113.14 ? 46 ASP B C 1 ATOM 2789 O O . ASP B 2 46 ? 2.243 -36.656 5.954 1.00 113.01 ? 46 ASP B O 1 ATOM 2790 C CB . ASP B 2 46 ? -0.391 -38.558 5.423 1.00 117.26 ? 46 ASP B CB 1 ATOM 2791 C CG . ASP B 2 46 ? -1.862 -38.481 5.043 1.00 121.32 ? 46 ASP B CG 1 ATOM 2792 O OD1 . ASP B 2 46 ? -2.183 -37.934 3.964 1.00 123.53 ? 46 ASP B OD1 1 ATOM 2793 O OD2 . ASP B 2 46 ? -2.699 -38.978 5.826 1.00 123.73 ? 46 ASP B OD2 1 ATOM 2794 N N . GLY B 2 47 ? 2.691 -38.580 4.868 1.00 111.66 ? 47 GLY B N 1 ATOM 2795 C CA . GLY B 2 47 ? 4.077 -38.667 5.329 1.00 110.32 ? 47 GLY B CA 1 ATOM 2796 C C . GLY B 2 47 ? 4.946 -37.518 4.840 1.00 109.70 ? 47 GLY B C 1 ATOM 2797 O O . GLY B 2 47 ? 5.807 -37.030 5.575 1.00 108.57 ? 47 GLY B O 1 ATOM 2798 N N . VAL B 2 48 ? 4.716 -37.090 3.598 1.00 111.32 ? 48 VAL B N 1 ATOM 2799 C CA . VAL B 2 48 ? 5.448 -35.967 3.001 1.00 112.33 ? 48 VAL B CA 1 ATOM 2800 C C . VAL B 2 48 ? 4.988 -34.630 3.596 1.00 111.78 ? 48 VAL B C 1 ATOM 2801 O O . VAL B 2 48 ? 5.817 -33.771 3.906 1.00 110.94 ? 48 VAL B O 1 ATOM 2802 C CB . VAL B 2 48 ? 5.308 -35.958 1.454 1.00 117.10 ? 48 VAL B CB 1 ATOM 2803 C CG1 . VAL B 2 48 ? 5.847 -34.665 0.850 1.00 120.39 ? 48 VAL B CG1 1 ATOM 2804 C CG2 . VAL B 2 48 ? 6.028 -37.158 0.849 1.00 119.01 ? 48 VAL B CG2 1 ATOM 2805 N N . THR B 2 49 ? 3.676 -34.459 3.755 1.00 113.11 ? 49 THR B N 1 ATOM 2806 C CA . THR B 2 49 ? 3.121 -33.240 4.353 1.00 114.95 ? 49 THR B CA 1 ATOM 2807 C C . THR B 2 49 ? 3.547 -33.091 5.819 1.00 112.34 ? 49 THR B C 1 ATOM 2808 O O . THR B 2 49 ? 3.784 -31.978 6.286 1.00 113.26 ? 49 THR B O 1 ATOM 2809 C CB . THR B 2 49 ? 1.579 -33.208 4.268 1.00 119.15 ? 49 THR B CB 1 ATOM 2810 O OG1 . THR B 2 49 ? 1.163 -33.463 2.922 1.00 122.35 ? 49 THR B OG1 1 ATOM 2811 C CG2 . THR B 2 49 ? 1.039 -31.852 4.708 1.00 123.97 ? 49 THR B CG2 1 ATOM 2812 N N . ASN B 2 50 ? 3.639 -34.214 6.533 1.00 110.26 ? 50 ASN B N 1 ATOM 2813 C CA . ASN B 2 50 ? 4.105 -34.222 7.928 1.00 109.58 ? 50 ASN B CA 1 ATOM 2814 C C . ASN B 2 50 ? 5.585 -33.859 8.062 1.00 106.98 ? 50 ASN B C 1 ATOM 2815 O O . ASN B 2 50 ? 5.983 -33.231 9.044 1.00 107.20 ? 50 ASN B O 1 ATOM 2816 C CB . ASN B 2 50 ? 3.858 -35.591 8.591 1.00 110.14 ? 50 ASN B CB 1 ATOM 2817 C CG . ASN B 2 50 ? 2.436 -35.751 9.114 1.00 114.11 ? 50 ASN B CG 1 ATOM 2818 O OD1 . ASN B 2 50 ? 2.220 -36.334 10.177 1.00 116.67 ? 50 ASN B OD1 1 ATOM 2819 N ND2 . ASN B 2 50 ? 1.463 -35.240 8.368 1.00 116.09 ? 50 ASN B ND2 1 ATOM 2820 N N . LYS B 2 51 ? 6.389 -34.262 7.078 1.00 105.52 ? 51 LYS B N 1 ATOM 2821 C CA . LYS B 2 51 ? 7.836 -34.030 7.107 1.00 104.26 ? 51 LYS B CA 1 ATOM 2822 C C . LYS B 2 51 ? 8.193 -32.582 6.774 1.00 104.19 ? 51 LYS B C 1 ATOM 2823 O O . LYS B 2 51 ? 9.078 -32.001 7.404 1.00 103.03 ? 51 LYS B O 1 ATOM 2824 C CB . LYS B 2 51 ? 8.550 -34.974 6.135 1.00 105.29 ? 51 LYS B CB 1 ATOM 2825 C CG . LYS B 2 51 ? 10.042 -35.120 6.393 1.00 105.94 ? 51 LYS B CG 1 ATOM 2826 C CD . LYS B 2 51 ? 10.717 -35.932 5.298 1.00 109.34 ? 51 LYS B CD 1 ATOM 2827 C CE . LYS B 2 51 ? 12.051 -36.498 5.757 1.00 112.17 ? 51 LYS B CE 1 ATOM 2828 N NZ . LYS B 2 51 ? 11.893 -37.723 6.593 1.00 113.94 ? 51 LYS B NZ 1 ATOM 2829 N N . VAL B 2 52 ? 7.516 -32.010 5.779 1.00 106.37 ? 52 VAL B N 1 ATOM 2830 C CA . VAL B 2 52 ? 7.745 -30.613 5.392 1.00 108.30 ? 52 VAL B CA 1 ATOM 2831 C C . VAL B 2 52 ? 7.290 -29.634 6.485 1.00 108.72 ? 52 VAL B C 1 ATOM 2832 O O . VAL B 2 52 ? 7.965 -28.638 6.741 1.00 108.66 ? 52 VAL B O 1 ATOM 2833 C CB . VAL B 2 52 ? 7.085 -30.266 4.030 1.00 113.15 ? 52 VAL B CB 1 ATOM 2834 C CG1 . VAL B 2 52 ? 5.562 -30.304 4.109 1.00 115.78 ? 52 VAL B CG1 1 ATOM 2835 C CG2 . VAL B 2 52 ? 7.563 -28.908 3.530 1.00 116.73 ? 52 VAL B CG2 1 ATOM 2836 N N . ASN B 2 53 ? 6.162 -29.931 7.129 1.00 110.16 ? 53 ASN B N 1 ATOM 2837 C CA . ASN B 2 53 ? 5.638 -29.093 8.214 1.00 112.91 ? 53 ASN B CA 1 ATOM 2838 C C . ASN B 2 53 ? 6.437 -29.242 9.509 1.00 110.96 ? 53 ASN B C 1 ATOM 2839 O O . ASN B 2 53 ? 6.543 -28.295 10.289 1.00 112.91 ? 53 ASN B O 1 ATOM 2840 C CB . ASN B 2 53 ? 4.162 -29.408 8.473 1.00 117.03 ? 53 ASN B CB 1 ATOM 2841 C CG . ASN B 2 53 ? 3.280 -29.119 7.269 1.00 121.08 ? 53 ASN B CG 1 ATOM 2842 O OD1 . ASN B 2 53 ? 3.658 -28.366 6.372 1.00 122.51 ? 53 ASN B OD1 1 ATOM 2843 N ND2 . ASN B 2 53 ? 2.097 -29.725 7.244 1.00 123.99 ? 53 ASN B ND2 1 ATOM 2844 N N . SER B 2 54 ? 6.991 -30.433 9.731 1.00 108.56 ? 54 SER B N 1 ATOM 2845 C CA . SER B 2 54 ? 7.864 -30.693 10.880 1.00 108.28 ? 54 SER B CA 1 ATOM 2846 C C . SER B 2 54 ? 9.179 -29.916 10.774 1.00 106.34 ? 54 SER B C 1 ATOM 2847 O O . SER B 2 54 ? 9.692 -29.412 11.775 1.00 107.36 ? 54 SER B O 1 ATOM 2848 C CB . SER B 2 54 ? 8.153 -32.194 11.003 1.00 107.68 ? 54 SER B CB 1 ATOM 2849 O OG . SER B 2 54 ? 9.057 -32.467 12.060 1.00 108.95 ? 54 SER B OG 1 ATOM 2850 N N . ILE B 2 55 ? 9.720 -29.835 9.559 1.00 104.87 ? 55 ILE B N 1 ATOM 2851 C CA . ILE B 2 55 ? 10.931 -29.055 9.287 1.00 103.86 ? 55 ILE B CA 1 ATOM 2852 C C . ILE B 2 55 ? 10.690 -27.563 9.532 1.00 105.47 ? 55 ILE B C 1 ATOM 2853 O O . ILE B 2 55 ? 11.544 -26.878 10.095 1.00 104.97 ? 55 ILE B O 1 ATOM 2854 C CB . ILE B 2 55 ? 11.428 -29.285 7.840 1.00 104.10 ? 55 ILE B CB 1 ATOM 2855 C CG1 . ILE B 2 55 ? 12.009 -30.698 7.709 1.00 104.14 ? 55 ILE B CG1 1 ATOM 2856 C CG2 . ILE B 2 55 ? 12.472 -28.246 7.437 1.00 104.43 ? 55 ILE B CG2 1 ATOM 2857 C CD1 . ILE B 2 55 ? 12.057 -31.215 6.286 1.00 106.50 ? 55 ILE B CD1 1 ATOM 2858 N N . ILE B 2 56 ? 9.525 -27.072 9.118 1.00 108.57 ? 56 ILE B N 1 ATOM 2859 C CA . ILE B 2 56 ? 9.177 -25.658 9.280 1.00 112.15 ? 56 ILE B CA 1 ATOM 2860 C C . ILE B 2 56 ? 9.019 -25.280 10.764 1.00 113.92 ? 56 ILE B C 1 ATOM 2861 O O . ILE B 2 56 ? 9.472 -24.214 11.189 1.00 115.12 ? 56 ILE B O 1 ATOM 2862 C CB . ILE B 2 56 ? 7.894 -25.304 8.488 1.00 117.28 ? 56 ILE B CB 1 ATOM 2863 C CG1 . ILE B 2 56 ? 8.120 -25.521 6.984 1.00 117.55 ? 56 ILE B CG1 1 ATOM 2864 C CG2 . ILE B 2 56 ? 7.476 -23.859 8.749 1.00 123.16 ? 56 ILE B CG2 1 ATOM 2865 C CD1 . ILE B 2 56 ? 6.850 -25.712 6.182 1.00 122.52 ? 56 ILE B CD1 1 ATOM 2866 N N . ASP B 2 57 ? 8.391 -26.158 11.545 1.00 115.07 ? 57 ASP B N 1 ATOM 2867 C CA . ASP B 2 57 ? 8.167 -25.906 12.975 1.00 119.07 ? 57 ASP B CA 1 ATOM 2868 C C . ASP B 2 57 ? 9.434 -26.077 13.817 1.00 116.57 ? 57 ASP B C 1 ATOM 2869 O O . ASP B 2 57 ? 9.651 -25.326 14.768 1.00 119.69 ? 57 ASP B O 1 ATOM 2870 C CB . ASP B 2 57 ? 7.061 -26.819 13.518 1.00 123.00 ? 57 ASP B CB 1 ATOM 2871 C CG . ASP B 2 57 ? 5.691 -26.467 12.970 1.00 128.01 ? 57 ASP B CG 1 ATOM 2872 O OD1 . ASP B 2 57 ? 5.318 -25.274 12.995 1.00 133.03 ? 57 ASP B OD1 1 ATOM 2873 O OD2 . ASP B 2 57 ? 4.979 -27.389 12.523 1.00 127.89 ? 57 ASP B OD2 1 ATOM 2874 N N . LYS B 2 58 ? 10.258 -27.065 13.472 1.00 112.28 ? 58 LYS B N 1 ATOM 2875 C CA . LYS B 2 58 ? 11.506 -27.326 14.198 1.00 111.43 ? 58 LYS B CA 1 ATOM 2876 C C . LYS B 2 58 ? 12.489 -26.156 14.107 1.00 109.69 ? 58 LYS B C 1 ATOM 2877 O O . LYS B 2 58 ? 13.229 -25.886 15.056 1.00 111.05 ? 58 LYS B O 1 ATOM 2878 C CB . LYS B 2 58 ? 12.171 -28.602 13.677 1.00 108.99 ? 58 LYS B CB 1 ATOM 2879 N N . MET B 2 59 ? 12.479 -25.462 12.970 1.00 107.70 ? 59 MET B N 1 ATOM 2880 C CA . MET B 2 59 ? 13.366 -24.319 12.734 1.00 106.59 ? 59 MET B CA 1 ATOM 2881 C C . MET B 2 59 ? 12.730 -22.990 13.174 1.00 110.93 ? 59 MET B C 1 ATOM 2882 O O . MET B 2 59 ? 13.324 -21.927 12.995 1.00 110.71 ? 59 MET B O 1 ATOM 2883 C CB . MET B 2 59 ? 13.747 -24.252 11.247 1.00 104.28 ? 59 MET B CB 1 ATOM 2884 C CG . MET B 2 59 ? 14.370 -25.533 10.694 1.00 102.06 ? 59 MET B CG 1 ATOM 2885 S SD . MET B 2 59 ? 16.108 -25.800 11.096 1.00 100.56 ? 59 MET B SD 1 ATOM 2886 C CE . MET B 2 59 ? 16.884 -24.330 10.435 1.00 100.42 ? 59 MET B CE 1 ATOM 2887 N N . ASN B 2 60 ? 11.535 -23.059 13.763 1.00 94.39 ? 60 ASN B N 1 ATOM 2888 C CA . ASN B 2 60 ? 10.792 -21.875 14.214 1.00 93.08 ? 60 ASN B CA 1 ATOM 2889 C C . ASN B 2 60 ? 11.455 -21.141 15.388 1.00 89.01 ? 60 ASN B C 1 ATOM 2890 O O . ASN B 2 60 ? 11.100 -20.001 15.686 1.00 87.53 ? 60 ASN B O 1 ATOM 2891 C CB . ASN B 2 60 ? 9.357 -22.289 14.586 1.00 99.98 ? 60 ASN B CB 1 ATOM 2892 C CG . ASN B 2 60 ? 8.413 -21.107 14.723 1.00 100.32 ? 60 ASN B CG 1 ATOM 2893 O OD1 . ASN B 2 60 ? 8.609 -20.229 15.567 1.00 98.59 ? 60 ASN B OD1 1 ATOM 2894 N ND2 . ASN B 2 60 ? 7.367 -21.093 13.908 1.00 103.38 ? 60 ASN B ND2 1 ATOM 2895 N N . THR B 2 61 ? 12.425 -21.786 16.033 1.00 87.98 ? 61 THR B N 1 ATOM 2896 C CA . THR B 2 61 ? 13.123 -21.211 17.190 1.00 84.56 ? 61 THR B CA 1 ATOM 2897 C C . THR B 2 61 ? 14.573 -20.898 16.809 1.00 78.32 ? 61 THR B C 1 ATOM 2898 O O . THR B 2 61 ? 15.521 -21.284 17.492 1.00 77.67 ? 61 THR B O 1 ATOM 2899 C CB . THR B 2 61 ? 13.025 -22.126 18.441 1.00 90.03 ? 61 THR B CB 1 ATOM 2900 O OG1 . THR B 2 61 ? 14.185 -21.965 19.264 1.00 87.98 ? 61 THR B OG1 1 ATOM 2901 C CG2 . THR B 2 61 ? 12.891 -23.595 18.067 1.00 95.85 ? 61 THR B CG2 1 ATOM 2902 N N . GLN B 2 62 ? 14.718 -20.165 15.712 1.00 73.92 ? 62 GLN B N 1 ATOM 2903 C CA . GLN B 2 62 ? 16.015 -19.867 15.120 1.00 69.04 ? 62 GLN B CA 1 ATOM 2904 C C . GLN B 2 62 ? 16.538 -18.524 15.640 1.00 63.57 ? 62 GLN B C 1 ATOM 2905 O O . GLN B 2 62 ? 15.769 -17.707 16.141 1.00 64.78 ? 62 GLN B O 1 ATOM 2906 C CB . GLN B 2 62 ? 15.868 -19.859 13.594 1.00 69.32 ? 62 GLN B CB 1 ATOM 2907 C CG . GLN B 2 62 ? 17.147 -19.614 12.813 1.00 66.30 ? 62 GLN B CG 1 ATOM 2908 C CD . GLN B 2 62 ? 17.068 -20.083 11.367 1.00 68.77 ? 62 GLN B CD 1 ATOM 2909 O OE1 . GLN B 2 62 ? 16.416 -21.084 11.047 1.00 73.11 ? 62 GLN B OE1 1 ATOM 2910 N NE2 . GLN B 2 62 ? 17.748 -19.362 10.481 1.00 66.62 ? 62 GLN B NE2 1 ATOM 2911 N N . PHE B 2 63 ? 17.845 -18.308 15.535 1.00 58.90 ? 63 PHE B N 1 ATOM 2912 C CA . PHE B 2 63 ? 18.468 -17.063 15.991 1.00 53.87 ? 63 PHE B CA 1 ATOM 2913 C C . PHE B 2 63 ? 17.984 -15.862 15.179 1.00 52.72 ? 63 PHE B C 1 ATOM 2914 O O . PHE B 2 63 ? 17.717 -15.978 13.985 1.00 54.77 ? 63 PHE B O 1 ATOM 2915 C CB . PHE B 2 63 ? 19.997 -17.165 15.902 1.00 50.53 ? 63 PHE B CB 1 ATOM 2916 C CG . PHE B 2 63 ? 20.714 -15.947 16.415 1.00 46.06 ? 63 PHE B CG 1 ATOM 2917 C CD1 . PHE B 2 63 ? 20.876 -15.740 17.778 1.00 45.16 ? 63 PHE B CD1 1 ATOM 2918 C CD2 . PHE B 2 63 ? 21.201 -14.992 15.532 1.00 43.11 ? 63 PHE B CD2 1 ATOM 2919 C CE1 . PHE B 2 63 ? 21.517 -14.604 18.251 1.00 42.06 ? 63 PHE B CE1 1 ATOM 2920 C CE2 . PHE B 2 63 ? 21.839 -13.858 15.997 1.00 40.25 ? 63 PHE B CE2 1 ATOM 2921 C CZ . PHE B 2 63 ? 22.001 -13.664 17.357 1.00 39.33 ? 63 PHE B CZ 1 ATOM 2922 N N . GLU B 2 64 ? 17.865 -14.710 15.831 1.00 51.14 ? 64 GLU B N 1 ATOM 2923 C CA . GLU B 2 64 ? 17.460 -13.480 15.155 1.00 50.77 ? 64 GLU B CA 1 ATOM 2924 C C . GLU B 2 64 ? 18.472 -12.396 15.428 1.00 47.19 ? 64 GLU B C 1 ATOM 2925 O O . GLU B 2 64 ? 18.624 -11.947 16.563 1.00 48.05 ? 64 GLU B O 1 ATOM 2926 C CB . GLU B 2 64 ? 16.093 -13.024 15.635 1.00 54.44 ? 64 GLU B CB 1 ATOM 2927 C CG . GLU B 2 64 ? 14.971 -13.982 15.266 1.00 58.85 ? 64 GLU B CG 1 ATOM 2928 C CD . GLU B 2 64 ? 13.816 -13.918 16.239 1.00 63.12 ? 64 GLU B CD 1 ATOM 2929 O OE1 . GLU B 2 64 ? 14.034 -13.500 17.399 1.00 62.78 ? 64 GLU B OE1 1 ATOM 2930 O OE2 . GLU B 2 64 ? 12.691 -14.286 15.842 1.00 67.65 ? 64 GLU B OE2 1 ATOM 2931 N N . ALA B 2 65 ? 19.183 -12.000 14.382 1.00 45.04 ? 65 ALA B N 1 ATOM 2932 C CA . ALA B 2 65 ? 20.170 -10.948 14.478 1.00 41.79 ? 65 ALA B CA 1 ATOM 2933 C C . ALA B 2 65 ? 19.459 -9.646 14.793 1.00 42.56 ? 65 ALA B C 1 ATOM 2934 O O . ALA B 2 65 ? 18.325 -9.434 14.368 1.00 45.12 ? 65 ALA B O 1 ATOM 2935 C CB . ALA B 2 65 ? 20.950 -10.837 13.173 1.00 41.34 ? 65 ALA B CB 1 ATOM 2936 N N . VAL B 2 66 ? 20.124 -8.795 15.565 1.00 41.46 ? 66 VAL B N 1 ATOM 2937 C CA . VAL B 2 66 ? 19.592 -7.489 15.945 1.00 43.36 ? 66 VAL B CA 1 ATOM 2938 C C . VAL B 2 66 ? 20.657 -6.437 15.705 1.00 41.59 ? 66 VAL B C 1 ATOM 2939 O O . VAL B 2 66 ? 21.822 -6.675 15.984 1.00 39.13 ? 66 VAL B O 1 ATOM 2940 C CB . VAL B 2 66 ? 19.185 -7.475 17.429 1.00 44.51 ? 66 VAL B CB 1 ATOM 2941 C CG1 . VAL B 2 66 ? 18.921 -6.051 17.915 1.00 46.65 ? 66 VAL B CG1 1 ATOM 2942 C CG2 . VAL B 2 66 ? 17.960 -8.357 17.637 1.00 47.56 ? 66 VAL B CG2 1 ATOM 2943 N N . GLY B 2 67 ? 20.257 -5.279 15.190 1.00 44.40 ? 67 GLY B N 1 ATOM 2944 C CA . GLY B 2 67 ? 21.198 -4.191 14.940 1.00 43.94 ? 67 GLY B CA 1 ATOM 2945 C C . GLY B 2 67 ? 21.701 -3.625 16.253 1.00 42.55 ? 67 GLY B C 1 ATOM 2946 O O . GLY B 2 67 ? 20.905 -3.366 17.157 1.00 44.34 ? 67 GLY B O 1 ATOM 2947 N N . ARG B 2 68 ? 23.024 -3.479 16.371 1.00 39.96 ? 68 ARG B N 1 ATOM 2948 C CA . ARG B 2 68 ? 23.654 -2.831 17.530 1.00 38.23 ? 68 ARG B CA 1 ATOM 2949 C C . ARG B 2 68 ? 24.777 -1.912 17.078 1.00 37.49 ? 68 ARG B C 1 ATOM 2950 O O . ARG B 2 68 ? 25.621 -2.294 16.273 1.00 36.21 ? 68 ARG B O 1 ATOM 2951 C CB . ARG B 2 68 ? 24.209 -3.863 18.507 1.00 34.93 ? 68 ARG B CB 1 ATOM 2952 C CG . ARG B 2 68 ? 23.172 -4.844 19.012 1.00 35.93 ? 68 ARG B CG 1 ATOM 2953 C CD . ARG B 2 68 ? 23.603 -5.546 20.288 1.00 34.67 ? 68 ARG B CD 1 ATOM 2954 N NE . ARG B 2 68 ? 22.576 -6.494 20.728 1.00 36.60 ? 68 ARG B NE 1 ATOM 2955 C CZ . ARG B 2 68 ? 22.434 -7.727 20.242 1.00 36.61 ? 68 ARG B CZ 1 ATOM 2956 N NH1 . ARG B 2 68 ? 23.251 -8.188 19.290 1.00 34.15 ? 68 ARG B NH1 1 ATOM 2957 N NH2 . ARG B 2 68 ? 21.463 -8.503 20.699 1.00 39.26 ? 68 ARG B NH2 1 ATOM 2958 N N . GLU B 2 69 ? 24.785 -0.702 17.620 1.00 39.03 ? 69 GLU B N 1 ATOM 2959 C CA . GLU B 2 69 ? 25.735 0.323 17.241 1.00 39.25 ? 69 GLU B CA 1 ATOM 2960 C C . GLU B 2 69 ? 26.841 0.420 18.315 1.00 35.56 ? 69 GLU B C 1 ATOM 2961 O O . GLU B 2 69 ? 26.552 0.342 19.516 1.00 33.87 ? 69 GLU B O 1 ATOM 2962 C CB . GLU B 2 69 ? 24.984 1.647 17.101 1.00 45.42 ? 69 GLU B CB 1 ATOM 2963 C CG . GLU B 2 69 ? 25.518 2.581 16.029 1.00 49.98 ? 69 GLU B CG 1 ATOM 2964 C CD . GLU B 2 69 ? 24.605 2.719 14.819 1.00 55.16 ? 69 GLU B CD 1 ATOM 2965 O OE1 . GLU B 2 69 ? 23.372 2.897 14.988 1.00 59.12 ? 69 GLU B OE1 1 ATOM 2966 O OE2 . GLU B 2 69 ? 25.136 2.681 13.687 1.00 57.32 ? 69 GLU B OE2 1 ATOM 2967 N N . PHE B 2 70 ? 28.099 0.567 17.878 1.00 33.83 ? 70 PHE B N 1 ATOM 2968 C CA . PHE B 2 70 ? 29.256 0.709 18.780 1.00 31.70 ? 70 PHE B CA 1 ATOM 2969 C C . PHE B 2 70 ? 30.166 1.840 18.329 1.00 33.18 ? 70 PHE B C 1 ATOM 2970 O O . PHE B 2 70 ? 30.279 2.104 17.139 1.00 35.36 ? 70 PHE B O 1 ATOM 2971 C CB . PHE B 2 70 ? 30.064 -0.575 18.845 1.00 28.94 ? 70 PHE B CB 1 ATOM 2972 C CG . PHE B 2 70 ? 29.269 -1.772 19.275 1.00 28.32 ? 70 PHE B CG 1 ATOM 2973 C CD1 . PHE B 2 70 ? 29.141 -2.093 20.623 1.00 27.75 ? 70 PHE B CD1 1 ATOM 2974 C CD2 . PHE B 2 70 ? 28.649 -2.583 18.332 1.00 28.67 ? 70 PHE B CD2 1 ATOM 2975 C CE1 . PHE B 2 70 ? 28.408 -3.199 21.018 1.00 27.80 ? 70 PHE B CE1 1 ATOM 2976 C CE2 . PHE B 2 70 ? 27.919 -3.695 18.728 1.00 28.36 ? 70 PHE B CE2 1 ATOM 2977 C CZ . PHE B 2 70 ? 27.787 -3.997 20.071 1.00 27.73 ? 70 PHE B CZ 1 ATOM 2978 N N . ASN B 2 71 ? 30.803 2.525 19.276 1.00 33.05 ? 71 ASN B N 1 ATOM 2979 C CA . ASN B 2 71 ? 31.622 3.699 18.929 1.00 35.66 ? 71 ASN B CA 1 ATOM 2980 C C . ASN B 2 71 ? 33.041 3.288 18.563 1.00 33.98 ? 71 ASN B C 1 ATOM 2981 O O . ASN B 2 71 ? 33.373 2.107 18.575 1.00 30.60 ? 71 ASN B O 1 ATOM 2982 C CB . ASN B 2 71 ? 31.563 4.810 20.016 1.00 37.72 ? 71 ASN B CB 1 ATOM 2983 C CG . ASN B 2 71 ? 32.384 4.503 21.269 1.00 34.52 ? 71 ASN B CG 1 ATOM 2984 O OD1 . ASN B 2 71 ? 33.366 3.786 21.246 1.00 31.50 ? 71 ASN B OD1 1 ATOM 2985 N ND2 . ASN B 2 71 ? 31.974 5.081 22.369 1.00 36.20 ? 71 ASN B ND2 1 ATOM 2986 N N . ASN B 2 72 ? 33.866 4.264 18.220 1.00 37.88 ? 72 ASN B N 1 ATOM 2987 C CA . ASN B 2 72 ? 35.205 3.993 17.709 1.00 38.34 ? 72 ASN B CA 1 ATOM 2988 C C . ASN B 2 72 ? 36.098 3.302 18.720 1.00 34.29 ? 72 ASN B C 1 ATOM 2989 O O . ASN B 2 72 ? 36.940 2.501 18.332 1.00 33.03 ? 72 ASN B O 1 ATOM 2990 C CB . ASN B 2 72 ? 35.880 5.268 17.182 1.00 44.06 ? 72 ASN B CB 1 ATOM 2991 C CG . ASN B 2 72 ? 35.994 6.353 18.238 1.00 47.38 ? 72 ASN B CG 1 ATOM 2992 O OD1 . ASN B 2 72 ? 35.310 6.314 19.270 1.00 47.38 ? 72 ASN B OD1 1 ATOM 2993 N ND2 . ASN B 2 72 ? 36.855 7.340 17.985 1.00 52.03 ? 72 ASN B ND2 1 ATOM 2994 N N . LEU B 2 73 ? 35.915 3.608 20.004 1.00 33.04 ? 73 LEU B N 1 ATOM 2995 C CA . LEU B 2 73 ? 36.669 2.938 21.074 1.00 30.20 ? 73 LEU B CA 1 ATOM 2996 C C . LEU B 2 73 ? 35.943 1.724 21.664 1.00 27.37 ? 73 LEU B C 1 ATOM 2997 O O . LEU B 2 73 ? 36.233 1.315 22.793 1.00 26.57 ? 73 LEU B O 1 ATOM 2998 C CB . LEU B 2 73 ? 37.057 3.943 22.182 1.00 31.13 ? 73 LEU B CB 1 ATOM 2999 C CG . LEU B 2 73 ? 38.279 4.816 21.840 1.00 33.80 ? 73 LEU B CG 1 ATOM 3000 C CD1 . LEU B 2 73 ? 38.473 5.949 22.845 1.00 35.39 ? 73 LEU B CD1 1 ATOM 3001 C CD2 . LEU B 2 73 ? 39.551 3.969 21.713 1.00 31.94 ? 73 LEU B CD2 1 ATOM 3002 N N . GLU B 2 74 ? 35.007 1.145 20.909 1.00 27.53 ? 74 GLU B N 1 ATOM 3003 C CA . GLU B 2 74 ? 34.329 -0.094 21.326 1.00 25.99 ? 74 GLU B CA 1 ATOM 3004 C C . GLU B 2 74 ? 34.448 -1.156 20.242 1.00 25.67 ? 74 GLU B C 1 ATOM 3005 O O . GLU B 2 74 ? 33.511 -1.930 20.013 1.00 27.16 ? 74 GLU B O 1 ATOM 3006 C CB . GLU B 2 74 ? 32.840 0.149 21.635 1.00 26.20 ? 74 GLU B CB 1 ATOM 3007 C CG . GLU B 2 74 ? 32.541 0.929 22.906 1.00 27.16 ? 74 GLU B CG 1 ATOM 3008 C CD . GLU B 2 74 ? 31.057 1.261 23.058 1.00 29.15 ? 74 GLU B CD 1 ATOM 3009 O OE1 . GLU B 2 74 ? 30.348 1.424 22.028 1.00 29.34 ? 74 GLU B OE1 1 ATOM 3010 O OE2 . GLU B 2 74 ? 30.596 1.348 24.216 1.00 29.85 ? 74 GLU B OE2 1 ATOM 3011 N N . ARG B 2 75 ? 35.606 -1.218 19.598 1.00 26.41 ? 75 ARG B N 1 ATOM 3012 C CA . ARG B 2 75 ? 35.812 -2.134 18.472 1.00 26.50 ? 75 ARG B CA 1 ATOM 3013 C C . ARG B 2 75 ? 35.821 -3.592 18.900 1.00 24.16 ? 75 ARG B C 1 ATOM 3014 O O . ARG B 2 75 ? 35.423 -4.463 18.128 1.00 24.03 ? 75 ARG B O 1 ATOM 3015 C CB . ARG B 2 75 ? 37.129 -1.838 17.758 1.00 29.96 ? 75 ARG B CB 1 ATOM 3016 C CG . ARG B 2 75 ? 37.283 -0.421 17.230 1.00 33.89 ? 75 ARG B CG 1 ATOM 3017 C CD . ARG B 2 75 ? 36.531 -0.216 15.946 1.00 37.97 ? 75 ARG B CD 1 ATOM 3018 N NE . ARG B 2 75 ? 36.679 1.153 15.440 1.00 43.88 ? 75 ARG B NE 1 ATOM 3019 C CZ . ARG B 2 75 ? 37.678 1.594 14.675 1.00 48.17 ? 75 ARG B CZ 1 ATOM 3020 N NH1 . ARG B 2 75 ? 38.662 0.787 14.290 1.00 49.68 ? 75 ARG B NH1 1 ATOM 3021 N NH2 . ARG B 2 75 ? 37.689 2.864 14.288 1.00 52.42 ? 75 ARG B NH2 1 ATOM 3022 N N . ARG B 2 76 ? 36.306 -3.861 20.112 1.00 23.00 ? 76 ARG B N 1 ATOM 3023 C CA . ARG B 2 76 ? 36.422 -5.234 20.609 1.00 22.42 ? 76 ARG B CA 1 ATOM 3024 C C . ARG B 2 76 ? 35.055 -5.879 20.776 1.00 21.64 ? 76 ARG B C 1 ATOM 3025 O O . ARG B 2 76 ? 34.815 -6.962 20.266 1.00 22.75 ? 76 ARG B O 1 ATOM 3026 C CB . ARG B 2 76 ? 37.187 -5.290 21.941 1.00 21.68 ? 76 ARG B CB 1 ATOM 3027 C CG . ARG B 2 76 ? 38.672 -5.003 21.828 1.00 22.81 ? 76 ARG B CG 1 ATOM 3028 C CD . ARG B 2 76 ? 39.319 -4.937 23.194 1.00 22.31 ? 76 ARG B CD 1 ATOM 3029 N NE . ARG B 2 76 ? 38.777 -3.841 23.987 1.00 21.55 ? 76 ARG B NE 1 ATOM 3030 C CZ . ARG B 2 76 ? 38.570 -3.870 25.307 1.00 20.98 ? 76 ARG B CZ 1 ATOM 3031 N NH1 . ARG B 2 76 ? 38.847 -4.953 26.023 1.00 21.87 ? 76 ARG B NH1 1 ATOM 3032 N NH2 . ARG B 2 76 ? 38.065 -2.804 25.906 1.00 20.54 ? 76 ARG B NH2 1 ATOM 3033 N N . ILE B 2 77 ? 34.179 -5.227 21.522 1.00 21.86 ? 77 ILE B N 1 ATOM 3034 C CA . ILE B 2 77 ? 32.807 -5.703 21.687 1.00 23.11 ? 77 ILE B CA 1 ATOM 3035 C C . ILE B 2 77 ? 32.050 -5.645 20.361 1.00 23.53 ? 77 ILE B C 1 ATOM 3036 O O . ILE B 2 77 ? 31.211 -6.504 20.099 1.00 23.91 ? 77 ILE B O 1 ATOM 3037 C CB . ILE B 2 77 ? 32.040 -4.964 22.809 1.00 24.31 ? 77 ILE B CB 1 ATOM 3038 C CG1 . ILE B 2 77 ? 32.071 -3.449 22.623 1.00 26.56 ? 77 ILE B CG1 1 ATOM 3039 C CG2 . ILE B 2 77 ? 32.652 -5.294 24.151 1.00 25.07 ? 77 ILE B CG2 1 ATOM 3040 C CD1 . ILE B 2 77 ? 31.302 -2.695 23.690 1.00 29.45 ? 77 ILE B CD1 1 ATOM 3041 N N . GLU B 2 78 ? 32.370 -4.674 19.505 1.00 23.81 ? 78 GLU B N 1 ATOM 3042 C CA . GLU B 2 78 ? 31.751 -4.634 18.176 1.00 25.08 ? 78 GLU B CA 1 ATOM 3043 C C . GLU B 2 78 ? 32.067 -5.903 17.396 1.00 24.61 ? 78 GLU B C 1 ATOM 3044 O O . GLU B 2 78 ? 31.210 -6.425 16.675 1.00 26.13 ? 78 GLU B O 1 ATOM 3045 C CB . GLU B 2 78 ? 32.200 -3.415 17.381 1.00 27.09 ? 78 GLU B CB 1 ATOM 3046 C CG . GLU B 2 78 ? 31.640 -3.350 15.966 1.00 29.95 ? 78 GLU B CG 1 ATOM 3047 C CD . GLU B 2 78 ? 32.044 -2.071 15.257 1.00 34.48 ? 78 GLU B CD 1 ATOM 3048 O OE1 . GLU B 2 78 ? 33.276 -1.849 15.075 1.00 35.52 ? 78 GLU B OE1 1 ATOM 3049 O OE2 . GLU B 2 78 ? 31.132 -1.278 14.892 1.00 38.09 ? 78 GLU B OE2 1 ATOM 3050 N N . ASN B 2 79 ? 33.300 -6.373 17.540 1.00 23.30 ? 79 ASN B N 1 ATOM 3051 C CA . ASN B 2 79 ? 33.796 -7.548 16.845 1.00 23.94 ? 79 ASN B CA 1 ATOM 3052 C C . ASN B 2 79 ? 33.223 -8.805 17.463 1.00 23.82 ? 79 ASN B C 1 ATOM 3053 O O . ASN B 2 79 ? 32.943 -9.770 16.770 1.00 25.38 ? 79 ASN B O 1 ATOM 3054 C CB . ASN B 2 79 ? 35.333 -7.603 16.926 1.00 24.53 ? 79 ASN B CB 1 ATOM 3055 C CG . ASN B 2 79 ? 35.912 -8.858 16.281 1.00 26.66 ? 79 ASN B CG 1 ATOM 3056 O OD1 . ASN B 2 79 ? 36.122 -9.880 16.951 1.00 26.77 ? 79 ASN B OD1 1 ATOM 3057 N ND2 . ASN B 2 79 ? 36.135 -8.803 14.975 1.00 28.56 ? 79 ASN B ND2 1 ATOM 3058 N N . LEU B 2 80 ? 33.091 -8.784 18.782 1.00 23.27 ? 80 LEU B N 1 ATOM 3059 C CA . LEU B 2 80 ? 32.464 -9.862 19.540 1.00 24.51 ? 80 LEU B CA 1 ATOM 3060 C C . LEU B 2 80 ? 31.026 -10.049 19.066 1.00 24.59 ? 80 LEU B C 1 ATOM 3061 O O . LEU B 2 80 ? 30.607 -11.161 18.769 1.00 25.94 ? 80 LEU B O 1 ATOM 3062 C CB . LEU B 2 80 ? 32.484 -9.520 21.034 1.00 24.35 ? 80 LEU B CB 1 ATOM 3063 C CG . LEU B 2 80 ? 32.333 -10.648 22.051 1.00 26.05 ? 80 LEU B CG 1 ATOM 3064 C CD1 . LEU B 2 80 ? 32.988 -10.240 23.369 1.00 26.55 ? 80 LEU B CD1 1 ATOM 3065 C CD2 . LEU B 2 80 ? 30.878 -11.005 22.285 1.00 27.40 ? 80 LEU B CD2 1 ATOM 3066 N N . ASN B 2 81 ? 30.296 -8.945 18.976 1.00 23.05 ? 81 ASN B N 1 ATOM 3067 C CA . ASN B 2 81 ? 28.910 -8.959 18.544 1.00 24.30 ? 81 ASN B CA 1 ATOM 3068 C C . ASN B 2 81 ? 28.733 -9.515 17.118 1.00 25.80 ? 81 ASN B C 1 ATOM 3069 O O . ASN B 2 81 ? 27.833 -10.324 16.844 1.00 27.08 ? 81 ASN B O 1 ATOM 3070 C CB . ASN B 2 81 ? 28.348 -7.528 18.622 1.00 24.04 ? 81 ASN B CB 1 ATOM 3071 C CG . ASN B 2 81 ? 26.889 -7.446 18.218 1.00 25.48 ? 81 ASN B CG 1 ATOM 3072 O OD1 . ASN B 2 81 ? 25.993 -7.782 18.999 1.00 26.12 ? 81 ASN B OD1 1 ATOM 3073 N ND2 . ASN B 2 81 ? 26.641 -7.001 16.991 1.00 26.19 ? 81 ASN B ND2 1 ATOM 3074 N N . LYS B 2 82 ? 29.587 -9.036 16.223 1.00 25.58 ? 82 LYS B N 1 ATOM 3075 C CA . LYS B 2 82 ? 29.595 -9.432 14.844 1.00 27.57 ? 82 LYS B CA 1 ATOM 3076 C C . LYS B 2 82 ? 29.813 -10.938 14.713 1.00 28.73 ? 82 LYS B C 1 ATOM 3077 O O . LYS B 2 82 ? 29.059 -11.607 14.007 1.00 30.29 ? 82 LYS B O 1 ATOM 3078 C CB . LYS B 2 82 ? 30.714 -8.681 14.118 1.00 29.28 ? 82 LYS B CB 1 ATOM 3079 C CG . LYS B 2 82 ? 30.835 -9.002 12.637 1.00 33.13 ? 82 LYS B CG 1 ATOM 3080 C CD . LYS B 2 82 ? 31.753 -7.996 11.954 1.00 35.88 ? 82 LYS B CD 1 ATOM 3081 C CE . LYS B 2 82 ? 31.771 -8.174 10.444 1.00 40.31 ? 82 LYS B CE 1 ATOM 3082 N NZ . LYS B 2 82 ? 32.790 -9.173 10.014 1.00 43.16 ? 82 LYS B NZ 1 ATOM 3083 N N . LYS B 2 83 ? 30.829 -11.460 15.403 1.00 47.31 ? 83 LYS B N 1 ATOM 3084 C CA . LYS B 2 83 ? 31.165 -12.891 15.340 1.00 47.38 ? 83 LYS B CA 1 ATOM 3085 C C . LYS B 2 83 ? 30.117 -13.778 16.015 1.00 45.79 ? 83 LYS B C 1 ATOM 3086 O O . LYS B 2 83 ? 29.894 -14.920 15.603 1.00 46.30 ? 83 LYS B O 1 ATOM 3087 C CB . LYS B 2 83 ? 32.531 -13.160 15.987 1.00 47.96 ? 83 LYS B CB 1 ATOM 3088 C CG . LYS B 2 83 ? 33.722 -12.550 15.265 1.00 49.91 ? 83 LYS B CG 1 ATOM 3089 C CD . LYS B 2 83 ? 33.919 -13.153 13.900 1.00 52.93 ? 83 LYS B CD 1 ATOM 3090 C CE . LYS B 2 83 ? 35.347 -12.991 13.415 1.00 56.35 ? 83 LYS B CE 1 ATOM 3091 N NZ . LYS B 2 83 ? 35.667 -14.053 12.427 1.00 59.88 ? 83 LYS B NZ 1 ATOM 3092 N N . MET B 2 84 ? 29.492 -13.264 17.063 1.00 44.18 ? 84 MET B N 1 ATOM 3093 C CA . MET B 2 84 ? 28.453 -14.013 17.744 1.00 44.52 ? 84 MET B CA 1 ATOM 3094 C C . MET B 2 84 ? 27.247 -14.202 16.825 1.00 44.80 ? 84 MET B C 1 ATOM 3095 O O . MET B 2 84 ? 26.749 -15.314 16.684 1.00 44.80 ? 84 MET B O 1 ATOM 3096 C CB . MET B 2 84 ? 28.027 -13.301 19.022 1.00 44.94 ? 84 MET B CB 1 ATOM 3097 C CG . MET B 2 84 ? 27.124 -14.135 19.905 1.00 46.56 ? 84 MET B CG 1 ATOM 3098 S SD . MET B 2 84 ? 25.685 -13.217 20.426 1.00 49.65 ? 84 MET B SD 1 ATOM 3099 C CE . MET B 2 84 ? 24.827 -12.982 18.884 1.00 49.72 ? 84 MET B CE 1 ATOM 3100 N N . GLU B 2 85 ? 26.797 -13.115 16.198 1.00 45.02 ? 85 GLU B N 1 ATOM 3101 C CA . GLU B 2 85 ? 25.638 -13.160 15.294 1.00 46.53 ? 85 GLU B CA 1 ATOM 3102 C C . GLU B 2 85 ? 25.900 -14.011 14.067 1.00 46.71 ? 85 GLU B C 1 ATOM 3103 O O . GLU B 2 85 ? 25.093 -14.865 13.726 1.00 46.97 ? 85 GLU B O 1 ATOM 3104 C CB . GLU B 2 85 ? 25.239 -11.760 14.849 1.00 48.22 ? 85 GLU B CB 1 ATOM 3105 C CG . GLU B 2 85 ? 24.600 -10.973 15.972 1.00 49.33 ? 85 GLU B CG 1 ATOM 3106 C CD . GLU B 2 85 ? 24.027 -9.649 15.524 1.00 52.04 ? 85 GLU B CD 1 ATOM 3107 O OE1 . GLU B 2 85 ? 24.760 -8.914 14.828 1.00 52.02 ? 85 GLU B OE1 1 ATOM 3108 O OE2 . GLU B 2 85 ? 22.862 -9.348 15.890 1.00 54.31 ? 85 GLU B OE2 1 ATOM 3109 N N . ASP B 2 86 ? 27.027 -13.757 13.412 1.00 46.68 ? 86 ASP B N 1 ATOM 3110 C CA . ASP B 2 86 ? 27.461 -14.556 12.273 1.00 48.00 ? 86 ASP B CA 1 ATOM 3111 C C . ASP B 2 86 ? 27.714 -16.002 12.672 1.00 46.92 ? 86 ASP B C 1 ATOM 3112 O O . ASP B 2 86 ? 27.485 -16.908 11.878 1.00 47.92 ? 86 ASP B O 1 ATOM 3113 C CB . ASP B 2 86 ? 28.720 -13.971 11.617 1.00 49.62 ? 86 ASP B CB 1 ATOM 3114 C CG . ASP B 2 86 ? 28.412 -13.236 10.325 1.00 52.99 ? 86 ASP B CG 1 ATOM 3115 O OD1 . ASP B 2 86 ? 28.012 -13.914 9.334 1.00 55.29 ? 86 ASP B OD1 1 ATOM 3116 O OD2 . ASP B 2 86 ? 28.575 -11.993 10.297 1.00 54.01 ? 86 ASP B OD2 1 ATOM 3117 N N . GLY B 2 87 ? 28.196 -16.206 13.896 1.00 45.18 ? 87 GLY B N 1 ATOM 3118 C CA . GLY B 2 87 ? 28.346 -17.547 14.448 1.00 45.02 ? 87 GLY B CA 1 ATOM 3119 C C . GLY B 2 87 ? 27.024 -18.291 14.508 1.00 44.75 ? 87 GLY B C 1 ATOM 3120 O O . GLY B 2 87 ? 26.936 -19.436 14.077 1.00 45.53 ? 87 GLY B O 1 ATOM 3121 N N . PHE B 2 88 ? 25.991 -17.649 15.043 1.00 43.84 ? 88 PHE B N 1 ATOM 3122 C CA . PHE B 2 88 ? 24.669 -18.283 15.093 1.00 44.67 ? 88 PHE B CA 1 ATOM 3123 C C . PHE B 2 88 ? 24.043 -18.476 13.713 1.00 45.33 ? 88 PHE B C 1 ATOM 3124 O O . PHE B 2 88 ? 23.379 -19.478 13.472 1.00 46.28 ? 88 PHE B O 1 ATOM 3125 C CB . PHE B 2 88 ? 23.706 -17.509 15.994 1.00 45.08 ? 88 PHE B CB 1 ATOM 3126 C CG . PHE B 2 88 ? 23.936 -17.742 17.456 1.00 45.30 ? 88 PHE B CG 1 ATOM 3127 C CD1 . PHE B 2 88 ? 23.776 -19.007 17.999 1.00 46.66 ? 88 PHE B CD1 1 ATOM 3128 C CD2 . PHE B 2 88 ? 24.323 -16.707 18.288 1.00 44.71 ? 88 PHE B CD2 1 ATOM 3129 C CE1 . PHE B 2 88 ? 23.985 -19.234 19.344 1.00 47.91 ? 88 PHE B CE1 1 ATOM 3130 C CE2 . PHE B 2 88 ? 24.533 -16.926 19.635 1.00 45.72 ? 88 PHE B CE2 1 ATOM 3131 C CZ . PHE B 2 88 ? 24.365 -18.195 20.161 1.00 47.55 ? 88 PHE B CZ 1 ATOM 3132 N N . LEU B 2 89 ? 24.259 -17.519 12.817 1.00 45.37 ? 89 LEU B N 1 ATOM 3133 C CA . LEU B 2 89 ? 23.697 -17.580 11.480 1.00 46.77 ? 89 LEU B CA 1 ATOM 3134 C C . LEU B 2 89 ? 24.337 -18.719 10.668 1.00 47.13 ? 89 LEU B C 1 ATOM 3135 O O . LEU B 2 89 ? 23.660 -19.376 9.882 1.00 48.21 ? 89 LEU B O 1 ATOM 3136 C CB . LEU B 2 89 ? 23.837 -16.223 10.774 1.00 47.97 ? 89 LEU B CB 1 ATOM 3137 C CG . LEU B 2 89 ? 23.026 -15.063 11.381 1.00 48.71 ? 89 LEU B CG 1 ATOM 3138 C CD1 . LEU B 2 89 ? 23.236 -13.774 10.596 1.00 50.80 ? 89 LEU B CD1 1 ATOM 3139 C CD2 . LEU B 2 89 ? 21.543 -15.383 11.480 1.00 50.39 ? 89 LEU B CD2 1 ATOM 3140 N N . ASP B 2 90 ? 25.631 -18.960 10.878 1.00 46.60 ? 90 ASP B N 1 ATOM 3141 C CA . ASP B 2 90 ? 26.315 -20.124 10.292 1.00 47.74 ? 90 ASP B CA 1 ATOM 3142 C C . ASP B 2 90 ? 25.745 -21.448 10.825 1.00 47.46 ? 90 ASP B C 1 ATOM 3143 O O . ASP B 2 90 ? 25.510 -22.378 10.062 1.00 48.67 ? 90 ASP B O 1 ATOM 3144 C CB . ASP B 2 90 ? 27.821 -20.081 10.586 1.00 48.25 ? 90 ASP B CB 1 ATOM 3145 C CG . ASP B 2 90 ? 28.558 -19.013 9.788 1.00 49.66 ? 90 ASP B CG 1 ATOM 3146 O OD1 . ASP B 2 90 ? 28.150 -18.711 8.653 1.00 51.31 ? 90 ASP B OD1 1 ATOM 3147 O OD2 . ASP B 2 90 ? 29.571 -18.487 10.301 1.00 49.68 ? 90 ASP B OD2 1 ATOM 3148 N N . VAL B 2 91 ? 25.532 -21.513 12.137 1.00 46.28 ? 91 VAL B N 1 ATOM 3149 C CA . VAL B 2 91 ? 24.995 -22.709 12.803 1.00 46.97 ? 91 VAL B CA 1 ATOM 3150 C C . VAL B 2 91 ? 23.595 -23.080 12.315 1.00 47.44 ? 91 VAL B C 1 ATOM 3151 O O . VAL B 2 91 ? 23.314 -24.248 12.071 1.00 48.59 ? 91 VAL B O 1 ATOM 3152 C CB . VAL B 2 91 ? 24.964 -22.533 14.345 1.00 46.68 ? 91 VAL B CB 1 ATOM 3153 C CG1 . VAL B 2 91 ? 24.032 -23.549 15.009 1.00 48.28 ? 91 VAL B CG1 1 ATOM 3154 C CG2 . VAL B 2 91 ? 26.374 -22.637 14.916 1.00 47.11 ? 91 VAL B CG2 1 ATOM 3155 N N . TRP B 2 92 ? 22.720 -22.089 12.198 1.00 47.07 ? 92 TRP B N 1 ATOM 3156 C CA . TRP B 2 92 ? 21.349 -22.333 11.744 1.00 48.36 ? 92 TRP B CA 1 ATOM 3157 C C . TRP B 2 92 ? 21.244 -22.567 10.234 1.00 49.12 ? 92 TRP B C 1 ATOM 3158 O O . TRP B 2 92 ? 20.358 -23.281 9.785 1.00 50.26 ? 92 TRP B O 1 ATOM 3159 C CB . TRP B 2 92 ? 20.440 -21.194 12.185 1.00 49.01 ? 92 TRP B CB 1 ATOM 3160 C CG . TRP B 2 92 ? 20.134 -21.287 13.627 1.00 49.66 ? 92 TRP B CG 1 ATOM 3161 C CD1 . TRP B 2 92 ? 20.611 -20.493 14.625 1.00 48.99 ? 92 TRP B CD1 1 ATOM 3162 C CD2 . TRP B 2 92 ? 19.291 -22.256 14.254 1.00 51.73 ? 92 TRP B CD2 1 ATOM 3163 N NE1 . TRP B 2 92 ? 20.105 -20.898 15.833 1.00 50.72 ? 92 TRP B NE1 1 ATOM 3164 C CE2 . TRP B 2 92 ? 19.293 -21.981 15.635 1.00 52.57 ? 92 TRP B CE2 1 ATOM 3165 C CE3 . TRP B 2 92 ? 18.521 -23.323 13.778 1.00 53.27 ? 92 TRP B CE3 1 ATOM 3166 C CZ2 . TRP B 2 92 ? 18.561 -22.734 16.546 1.00 55.52 ? 92 TRP B CZ2 1 ATOM 3167 C CZ3 . TRP B 2 92 ? 17.793 -24.072 14.684 1.00 55.85 ? 92 TRP B CZ3 1 ATOM 3168 C CH2 . TRP B 2 92 ? 17.818 -23.773 16.054 1.00 57.22 ? 92 TRP B CH2 1 ATOM 3169 N N . THR B 2 93 ? 22.149 -21.957 9.469 1.00 49.05 ? 93 THR B N 1 ATOM 3170 C CA . THR B 2 93 ? 22.291 -22.217 8.037 1.00 50.65 ? 93 THR B CA 1 ATOM 3171 C C . THR B 2 93 ? 22.697 -23.671 7.827 1.00 51.38 ? 93 THR B C 1 ATOM 3172 O O . THR B 2 93 ? 22.078 -24.392 7.042 1.00 52.79 ? 93 THR B O 1 ATOM 3173 C CB . THR B 2 93 ? 23.337 -21.276 7.405 1.00 51.17 ? 93 THR B CB 1 ATOM 3174 O OG1 . THR B 2 93 ? 22.816 -19.945 7.371 1.00 51.45 ? 93 THR B OG1 1 ATOM 3175 C CG2 . THR B 2 93 ? 23.683 -21.692 5.996 1.00 53.81 ? 93 THR B CG2 1 ATOM 3176 N N . TYR B 2 94 ? 23.731 -24.092 8.546 1.00 51.11 ? 94 TYR B N 1 ATOM 3177 C CA . TYR B 2 94 ? 24.173 -25.486 8.548 1.00 52.65 ? 94 TYR B CA 1 ATOM 3178 C C . TYR B 2 94 ? 23.026 -26.414 8.921 1.00 53.03 ? 94 TYR B C 1 ATOM 3179 O O . TYR B 2 94 ? 22.757 -27.379 8.211 1.00 54.47 ? 94 TYR B O 1 ATOM 3180 C CB . TYR B 2 94 ? 25.350 -25.667 9.514 1.00 52.80 ? 94 TYR B CB 1 ATOM 3181 C CG . TYR B 2 94 ? 25.783 -27.099 9.749 1.00 55.06 ? 94 TYR B CG 1 ATOM 3182 C CD1 . TYR B 2 94 ? 26.738 -27.701 8.935 1.00 57.85 ? 94 TYR B CD1 1 ATOM 3183 C CD2 . TYR B 2 94 ? 25.247 -27.848 10.792 1.00 55.32 ? 94 TYR B CD2 1 ATOM 3184 C CE1 . TYR B 2 94 ? 27.138 -29.008 9.149 1.00 60.79 ? 94 TYR B CE1 1 ATOM 3185 C CE2 . TYR B 2 94 ? 25.644 -29.155 11.013 1.00 58.21 ? 94 TYR B CE2 1 ATOM 3186 C CZ . TYR B 2 94 ? 26.590 -29.730 10.190 1.00 60.89 ? 94 TYR B CZ 1 ATOM 3187 O OH . TYR B 2 94 ? 26.991 -31.030 10.407 1.00 64.69 ? 94 TYR B OH 1 ATOM 3188 N N . ASN B 2 95 ? 22.345 -26.104 10.023 1.00 52.47 ? 95 ASN B N 1 ATOM 3189 C CA . ASN B 2 95 ? 21.206 -26.904 10.484 1.00 53.82 ? 95 ASN B CA 1 ATOM 3190 C C . ASN B 2 95 ? 20.128 -27.066 9.414 1.00 55.04 ? 95 ASN B C 1 ATOM 3191 O O . ASN B 2 95 ? 19.590 -28.159 9.241 1.00 56.50 ? 95 ASN B O 1 ATOM 3192 C CB . ASN B 2 95 ? 20.574 -26.302 11.750 1.00 53.57 ? 95 ASN B CB 1 ATOM 3193 C CG . ASN B 2 95 ? 21.367 -26.602 13.019 1.00 53.92 ? 95 ASN B CG 1 ATOM 3194 O OD1 . ASN B 2 95 ? 22.313 -27.376 13.012 1.00 54.76 ? 95 ASN B OD1 1 ATOM 3195 N ND2 . ASN B 2 95 ? 20.965 -25.988 14.119 1.00 54.05 ? 95 ASN B ND2 1 ATOM 3196 N N . ALA B 2 96 ? 19.823 -25.982 8.702 1.00 55.25 ? 96 ALA B N 1 ATOM 3197 C CA . ALA B 2 96 ? 18.747 -25.983 7.710 1.00 57.16 ? 96 ALA B CA 1 ATOM 3198 C C . ALA B 2 96 ? 19.119 -26.801 6.470 1.00 58.73 ? 96 ALA B C 1 ATOM 3199 O O . ALA B 2 96 ? 18.312 -27.585 5.979 1.00 59.99 ? 96 ALA B O 1 ATOM 3200 C CB . ALA B 2 96 ? 18.387 -24.558 7.311 1.00 57.61 ? 96 ALA B CB 1 ATOM 3201 N N . GLU B 2 97 ? 20.337 -26.605 5.969 1.00 59.35 ? 97 GLU B N 1 ATOM 3202 C CA . GLU B 2 97 ? 20.793 -27.270 4.748 1.00 61.80 ? 97 GLU B CA 1 ATOM 3203 C C . GLU B 2 97 ? 20.999 -28.765 4.949 1.00 62.90 ? 97 GLU B C 1 ATOM 3204 O O . GLU B 2 97 ? 20.583 -29.574 4.115 1.00 64.56 ? 97 GLU B O 1 ATOM 3205 C CB . GLU B 2 97 ? 22.095 -26.645 4.246 1.00 62.80 ? 97 GLU B CB 1 ATOM 3206 C CG . GLU B 2 97 ? 21.910 -25.276 3.621 1.00 63.80 ? 97 GLU B CG 1 ATOM 3207 C CD . GLU B 2 97 ? 23.218 -24.615 3.256 1.00 65.38 ? 97 GLU B CD 1 ATOM 3208 O OE1 . GLU B 2 97 ? 24.280 -25.065 3.737 1.00 65.36 ? 97 GLU B OE1 1 ATOM 3209 O OE2 . GLU B 2 97 ? 23.183 -23.633 2.488 1.00 67.55 ? 97 GLU B OE2 1 ATOM 3210 N N . LEU B 2 98 ? 21.647 -29.122 6.053 1.00 62.67 ? 98 LEU B N 1 ATOM 3211 C CA . LEU B 2 98 ? 21.914 -30.521 6.369 1.00 64.64 ? 98 LEU B CA 1 ATOM 3212 C C . LEU B 2 98 ? 20.619 -31.306 6.582 1.00 65.15 ? 98 LEU B C 1 ATOM 3213 O O . LEU B 2 98 ? 20.529 -32.470 6.200 1.00 67.17 ? 98 LEU B O 1 ATOM 3214 C CB . LEU B 2 98 ? 22.816 -30.629 7.604 1.00 64.69 ? 98 LEU B CB 1 ATOM 3215 C CG . LEU B 2 98 ? 23.208 -32.037 8.065 1.00 67.39 ? 98 LEU B CG 1 ATOM 3216 C CD1 . LEU B 2 98 ? 23.824 -32.846 6.941 1.00 70.28 ? 98 LEU B CD1 1 ATOM 3217 C CD2 . LEU B 2 98 ? 24.194 -31.972 9.212 1.00 68.19 ? 98 LEU B CD2 1 ATOM 3218 N N . LEU B 2 99 ? 19.622 -30.664 7.180 1.00 64.14 ? 99 LEU B N 1 ATOM 3219 C CA . LEU B 2 99 ? 18.329 -31.302 7.411 1.00 65.49 ? 99 LEU B CA 1 ATOM 3220 C C . LEU B 2 99 ? 17.540 -31.530 6.119 1.00 66.74 ? 99 LEU B C 1 ATOM 3221 O O . LEU B 2 99 ? 16.780 -32.497 6.017 1.00 68.21 ? 99 LEU B O 1 ATOM 3222 C CB . LEU B 2 99 ? 17.490 -30.471 8.379 1.00 64.93 ? 99 LEU B CB 1 ATOM 3223 C CG . LEU B 2 99 ? 16.174 -31.107 8.827 1.00 67.06 ? 99 LEU B CG 1 ATOM 3224 C CD1 . LEU B 2 99 ? 16.427 -32.445 9.513 1.00 68.81 ? 99 LEU B CD1 1 ATOM 3225 C CD2 . LEU B 2 99 ? 15.418 -30.155 9.744 1.00 67.67 ? 99 LEU B CD2 1 ATOM 3226 N N . VAL B 2 100 ? 17.702 -30.634 5.148 1.00 66.71 ? 100 VAL B N 1 ATOM 3227 C CA . VAL B 2 100 ? 17.070 -30.807 3.843 1.00 68.70 ? 100 VAL B CA 1 ATOM 3228 C C . VAL B 2 100 ? 17.714 -31.977 3.095 1.00 70.50 ? 100 VAL B C 1 ATOM 3229 O O . VAL B 2 100 ? 17.012 -32.866 2.614 1.00 72.03 ? 100 VAL B O 1 ATOM 3230 C CB . VAL B 2 100 ? 17.135 -29.510 3.012 1.00 69.20 ? 100 VAL B CB 1 ATOM 3231 C CG1 . VAL B 2 100 ? 16.842 -29.771 1.538 1.00 71.79 ? 100 VAL B CG1 1 ATOM 3232 C CG2 . VAL B 2 100 ? 16.151 -28.497 3.571 1.00 69.03 ? 100 VAL B CG2 1 ATOM 3233 N N . LEU B 2 101 ? 19.044 -31.970 3.014 1.00 71.12 ? 101 LEU B N 1 ATOM 3234 C CA . LEU B 2 101 ? 19.800 -33.051 2.381 1.00 73.84 ? 101 LEU B CA 1 ATOM 3235 C C . LEU B 2 101 ? 19.487 -34.423 2.987 1.00 74.99 ? 101 LEU B C 1 ATOM 3236 O O . LEU B 2 101 ? 19.298 -35.394 2.258 1.00 77.00 ? 101 LEU B O 1 ATOM 3237 C CB . LEU B 2 101 ? 21.309 -32.783 2.457 1.00 74.84 ? 101 LEU B CB 1 ATOM 3238 C CG . LEU B 2 101 ? 21.910 -32.016 1.275 1.00 77.00 ? 101 LEU B CG 1 ATOM 3239 C CD1 . LEU B 2 101 ? 21.486 -30.560 1.239 1.00 75.61 ? 101 LEU B CD1 1 ATOM 3240 C CD2 . LEU B 2 101 ? 23.423 -32.106 1.318 1.00 79.45 ? 101 LEU B CD2 1 ATOM 3241 N N . MET B 2 102 ? 19.434 -34.492 4.314 1.00 74.41 ? 102 MET B N 1 ATOM 3242 C CA . MET B 2 102 ? 19.115 -35.740 5.015 1.00 76.39 ? 102 MET B CA 1 ATOM 3243 C C . MET B 2 102 ? 17.654 -36.165 4.837 1.00 76.39 ? 102 MET B C 1 ATOM 3244 O O . MET B 2 102 ? 17.362 -37.357 4.746 1.00 78.32 ? 102 MET B O 1 ATOM 3245 C CB . MET B 2 102 ? 19.447 -35.621 6.509 1.00 76.69 ? 102 MET B CB 1 ATOM 3246 C CG . MET B 2 102 ? 20.897 -35.945 6.838 1.00 79.00 ? 102 MET B CG 1 ATOM 3247 S SD . MET B 2 102 ? 21.470 -35.339 8.442 1.00 79.67 ? 102 MET B SD 1 ATOM 3248 C CE . MET B 2 102 ? 20.005 -35.531 9.461 1.00 79.65 ? 102 MET B CE 1 ATOM 3249 N N . GLU B 2 103 ? 16.745 -35.192 4.804 1.00 74.57 ? 103 GLU B N 1 ATOM 3250 C CA . GLU B 2 103 ? 15.325 -35.467 4.574 1.00 75.09 ? 103 GLU B CA 1 ATOM 3251 C C . GLU B 2 103 ? 15.066 -35.904 3.133 1.00 75.89 ? 103 GLU B C 1 ATOM 3252 O O . GLU B 2 103 ? 14.247 -36.786 2.889 1.00 77.27 ? 103 GLU B O 1 ATOM 3253 C CB . GLU B 2 103 ? 14.476 -34.235 4.898 1.00 74.18 ? 103 GLU B CB 1 ATOM 3254 N N . ASN B 2 104 ? 15.756 -35.271 2.186 1.00 75.37 ? 104 ASN B N 1 ATOM 3255 C CA . ASN B 2 104 ? 15.651 -35.642 0.774 1.00 76.97 ? 104 ASN B CA 1 ATOM 3256 C C . ASN B 2 104 ? 16.073 -37.092 0.546 1.00 79.11 ? 104 ASN B C 1 ATOM 3257 O O . ASN B 2 104 ? 15.399 -37.834 -0.165 1.00 80.55 ? 104 ASN B O 1 ATOM 3258 C CB . ASN B 2 104 ? 16.495 -34.703 -0.100 1.00 76.95 ? 104 ASN B CB 1 ATOM 3259 C CG . ASN B 2 104 ? 15.889 -33.317 -0.231 1.00 75.93 ? 104 ASN B CG 1 ATOM 3260 O OD1 . ASN B 2 104 ? 14.758 -33.078 0.177 1.00 75.19 ? 104 ASN B OD1 1 ATOM 3261 N ND2 . ASN B 2 104 ? 16.643 -32.398 -0.815 1.00 76.52 ? 104 ASN B ND2 1 ATOM 3262 N N . GLU B 2 105 ? 17.183 -37.487 1.165 1.00 80.01 ? 105 GLU B N 1 ATOM 3263 C CA . GLU B 2 105 ? 17.664 -38.868 1.098 1.00 83.19 ? 105 GLU B CA 1 ATOM 3264 C C . GLU B 2 105 ? 16.618 -39.851 1.623 1.00 84.30 ? 105 GLU B C 1 ATOM 3265 O O . GLU B 2 105 ? 16.373 -40.895 1.011 1.00 86.25 ? 105 GLU B O 1 ATOM 3266 C CB . GLU B 2 105 ? 18.971 -39.035 1.886 1.00 84.15 ? 105 GLU B CB 1 ATOM 3267 C CG . GLU B 2 105 ? 19.700 -40.334 1.566 1.00 88.47 ? 105 GLU B CG 1 ATOM 3268 C CD . GLU B 2 105 ? 21.157 -40.317 1.983 1.00 90.73 ? 105 GLU B CD 1 ATOM 3269 O OE1 . GLU B 2 105 ? 21.427 -40.408 3.199 1.00 90.90 ? 105 GLU B OE1 1 ATOM 3270 O OE2 . GLU B 2 105 ? 22.028 -40.223 1.089 1.00 93.10 ? 105 GLU B OE2 1 ATOM 3271 N N . ARG B 2 106 ? 16.010 -39.513 2.759 1.00 83.54 ? 106 ARG B N 1 ATOM 3272 C CA . ARG B 2 106 ? 14.935 -40.326 3.326 1.00 85.36 ? 106 ARG B CA 1 ATOM 3273 C C . ARG B 2 106 ? 13.726 -40.353 2.405 1.00 85.51 ? 106 ARG B C 1 ATOM 3274 O O . ARG B 2 106 ? 13.147 -41.412 2.171 1.00 87.84 ? 106 ARG B O 1 ATOM 3275 C CB . ARG B 2 106 ? 14.504 -39.805 4.699 1.00 85.25 ? 106 ARG B CB 1 ATOM 3276 C CG . ARG B 2 106 ? 15.420 -40.216 5.839 1.00 87.13 ? 106 ARG B CG 1 ATOM 3277 C CD . ARG B 2 106 ? 14.706 -40.103 7.177 1.00 88.64 ? 106 ARG B CD 1 ATOM 3278 N NE . ARG B 2 106 ? 15.549 -40.546 8.285 1.00 91.26 ? 106 ARG B NE 1 ATOM 3279 C CZ . ARG B 2 106 ? 16.539 -39.833 8.818 1.00 90.34 ? 106 ARG B CZ 1 ATOM 3280 N NH1 . ARG B 2 106 ? 16.840 -38.623 8.352 1.00 86.84 ? 106 ARG B NH1 1 ATOM 3281 N NH2 . ARG B 2 106 ? 17.244 -40.336 9.825 1.00 93.58 ? 106 ARG B NH2 1 ATOM 3282 N N . THR B 2 107 ? 13.357 -39.188 1.882 1.00 83.68 ? 107 THR B N 1 ATOM 3283 C CA . THR B 2 107 ? 12.175 -39.066 1.034 1.00 84.49 ? 107 THR B CA 1 ATOM 3284 C C . THR B 2 107 ? 12.260 -39.928 -0.236 1.00 86.34 ? 107 THR B C 1 ATOM 3285 O O . THR B 2 107 ? 11.280 -40.574 -0.604 1.00 87.96 ? 107 THR B O 1 ATOM 3286 C CB . THR B 2 107 ? 11.904 -37.593 0.674 1.00 83.26 ? 107 THR B CB 1 ATOM 3287 O OG1 . THR B 2 107 ? 11.754 -36.839 1.881 1.00 82.19 ? 107 THR B OG1 1 ATOM 3288 C CG2 . THR B 2 107 ? 10.637 -37.453 -0.150 1.00 85.31 ? 107 THR B CG2 1 ATOM 3289 N N . LEU B 2 108 ? 13.425 -39.947 -0.886 1.00 86.66 ? 108 LEU B N 1 ATOM 3290 C CA . LEU B 2 108 ? 13.620 -40.736 -2.111 1.00 89.02 ? 108 LEU B CA 1 ATOM 3291 C C . LEU B 2 108 ? 13.647 -42.237 -1.830 1.00 91.05 ? 108 LEU B C 1 ATOM 3292 O O . LEU B 2 108 ? 13.030 -43.022 -2.556 1.00 92.52 ? 108 LEU B O 1 ATOM 3293 C CB . LEU B 2 108 ? 14.909 -40.320 -2.824 1.00 89.85 ? 108 LEU B CB 1 ATOM 3294 C CG . LEU B 2 108 ? 14.923 -38.886 -3.361 1.00 89.34 ? 108 LEU B CG 1 ATOM 3295 C CD1 . LEU B 2 108 ? 16.296 -38.536 -3.916 1.00 91.01 ? 108 LEU B CD1 1 ATOM 3296 C CD2 . LEU B 2 108 ? 13.848 -38.684 -4.418 1.00 91.05 ? 108 LEU B CD2 1 ATOM 3297 N N . ASP B 2 109 ? 14.364 -42.627 -0.779 1.00 91.41 ? 109 ASP B N 1 ATOM 3298 C CA . ASP B 2 109 ? 14.406 -44.027 -0.346 1.00 94.16 ? 109 ASP B CA 1 ATOM 3299 C C . ASP B 2 109 ? 13.055 -44.488 0.212 1.00 94.61 ? 109 ASP B C 1 ATOM 3300 O O . ASP B 2 109 ? 12.704 -45.664 0.097 1.00 97.26 ? 109 ASP B O 1 ATOM 3301 C CB . ASP B 2 109 ? 15.504 -44.236 0.705 1.00 95.11 ? 109 ASP B CB 1 ATOM 3302 C CG . ASP B 2 109 ? 16.902 -44.014 0.150 1.00 96.42 ? 109 ASP B CG 1 ATOM 3303 O OD1 . ASP B 2 109 ? 17.108 -44.198 -1.071 1.00 98.17 ? 109 ASP B OD1 1 ATOM 3304 O OD2 . ASP B 2 109 ? 17.802 -43.658 0.942 1.00 96.51 ? 109 ASP B OD2 1 ATOM 3305 N N . PHE B 2 110 ? 12.309 -43.561 0.818 1.00 92.67 ? 110 PHE B N 1 ATOM 3306 C CA . PHE B 2 110 ? 10.954 -43.839 1.302 1.00 93.76 ? 110 PHE B CA 1 ATOM 3307 C C . PHE B 2 110 ? 10.029 -44.200 0.142 1.00 94.82 ? 110 PHE B C 1 ATOM 3308 O O . PHE B 2 110 ? 9.182 -45.086 0.270 1.00 96.90 ? 110 PHE B O 1 ATOM 3309 C CB . PHE B 2 110 ? 10.398 -42.635 2.078 1.00 92.32 ? 110 PHE B CB 1 ATOM 3310 C CG . PHE B 2 110 ? 8.946 -42.768 2.471 1.00 94.35 ? 110 PHE B CG 1 ATOM 3311 C CD1 . PHE B 2 110 ? 8.520 -43.820 3.274 1.00 97.27 ? 110 PHE B CD1 1 ATOM 3312 C CD2 . PHE B 2 110 ? 8.008 -41.826 2.053 1.00 94.21 ? 110 PHE B CD2 1 ATOM 3313 C CE1 . PHE B 2 110 ? 7.189 -43.938 3.641 1.00 99.95 ? 110 PHE B CE1 1 ATOM 3314 C CE2 . PHE B 2 110 ? 6.675 -41.939 2.418 1.00 96.93 ? 110 PHE B CE2 1 ATOM 3315 C CZ . PHE B 2 110 ? 6.266 -42.996 3.214 1.00 99.83 ? 110 PHE B CZ 1 ATOM 3316 N N . HIS B 2 111 ? 10.193 -43.517 -0.987 1.00 93.78 ? 111 HIS B N 1 ATOM 3317 C CA . HIS B 2 111 ? 9.429 -43.850 -2.183 1.00 95.48 ? 111 HIS B CA 1 ATOM 3318 C C . HIS B 2 111 ? 9.834 -45.218 -2.735 1.00 97.58 ? 111 HIS B C 1 ATOM 3319 O O . HIS B 2 111 ? 8.974 -45.995 -3.155 1.00 99.40 ? 111 HIS B O 1 ATOM 3320 C CB . HIS B 2 111 ? 9.572 -42.762 -3.246 1.00 95.09 ? 111 HIS B CB 1 ATOM 3321 C CG . HIS B 2 111 ? 8.841 -41.500 -2.907 1.00 94.40 ? 111 HIS B CG 1 ATOM 3322 N ND1 . HIS B 2 111 ? 7.493 -41.476 -2.624 1.00 96.00 ? 111 HIS B ND1 1 ATOM 3323 C CD2 . HIS B 2 111 ? 9.267 -40.218 -2.813 1.00 93.05 ? 111 HIS B CD2 1 ATOM 3324 C CE1 . HIS B 2 111 ? 7.120 -40.236 -2.362 1.00 95.65 ? 111 HIS B CE1 1 ATOM 3325 N NE2 . HIS B 2 111 ? 8.178 -39.453 -2.471 1.00 93.67 ? 111 HIS B NE2 1 ATOM 3326 N N . ASP B 2 112 ? 11.134 -45.514 -2.718 1.00 97.70 ? 112 ASP B N 1 ATOM 3327 C CA . ASP B 2 112 ? 11.618 -46.846 -3.100 1.00 100.63 ? 112 ASP B CA 1 ATOM 3328 C C . ASP B 2 112 ? 11.082 -47.926 -2.161 1.00 102.37 ? 112 ASP B C 1 ATOM 3329 O O . ASP B 2 112 ? 10.698 -49.006 -2.612 1.00 104.67 ? 112 ASP B O 1 ATOM 3330 C CB . ASP B 2 112 ? 13.152 -46.897 -3.123 1.00 101.62 ? 112 ASP B CB 1 ATOM 3331 C CG . ASP B 2 112 ? 13.734 -46.523 -4.474 1.00 102.77 ? 112 ASP B CG 1 ATOM 3332 O OD1 . ASP B 2 112 ? 13.129 -46.873 -5.512 1.00 104.11 ? 112 ASP B OD1 1 ATOM 3333 O OD2 . ASP B 2 112 ? 14.806 -45.884 -4.497 1.00 102.62 ? 112 ASP B OD2 1 ATOM 3334 N N . SER B 2 113 ? 11.061 -47.625 -0.863 1.00 101.58 ? 113 SER B N 1 ATOM 3335 C CA . SER B 2 113 ? 10.541 -48.551 0.150 1.00 104.18 ? 113 SER B CA 1 ATOM 3336 C C . SER B 2 113 ? 9.087 -48.938 -0.111 1.00 105.23 ? 113 SER B C 1 ATOM 3337 O O . SER B 2 113 ? 8.721 -50.104 0.025 1.00 108.48 ? 113 SER B O 1 ATOM 3338 C CB . SER B 2 113 ? 10.662 -47.944 1.553 1.00 103.56 ? 113 SER B CB 1 ATOM 3339 O OG . SER B 2 113 ? 9.984 -48.733 2.520 1.00 106.87 ? 113 SER B OG 1 ATOM 3340 N N . ASN B 2 114 ? 8.272 -47.957 -0.487 1.00 103.17 ? 114 ASN B N 1 ATOM 3341 C CA . ASN B 2 114 ? 6.846 -48.183 -0.737 1.00 104.73 ? 114 ASN B CA 1 ATOM 3342 C C . ASN B 2 114 ? 6.583 -48.977 -2.021 1.00 106.05 ? 114 ASN B C 1 ATOM 3343 O O . ASN B 2 114 ? 5.565 -49.663 -2.131 1.00 108.26 ? 114 ASN B O 1 ATOM 3344 C CB . ASN B 2 114 ? 6.093 -46.849 -0.778 1.00 103.18 ? 114 ASN B CB 1 ATOM 3345 C CG . ASN B 2 114 ? 6.276 -46.036 0.494 1.00 102.37 ? 114 ASN B CG 1 ATOM 3346 O OD1 . ASN B 2 114 ? 6.377 -46.587 1.593 1.00 103.90 ? 114 ASN B OD1 1 ATOM 3347 N ND2 . ASN B 2 114 ? 6.333 -44.715 0.347 1.00 100.24 ? 114 ASN B ND2 1 ATOM 3348 N N . VAL B 2 115 ? 7.501 -48.884 -2.982 1.00 105.05 ? 115 VAL B N 1 ATOM 3349 C CA . VAL B 2 115 ? 7.421 -49.671 -4.214 1.00 106.86 ? 115 VAL B CA 1 ATOM 3350 C C . VAL B 2 115 ? 7.739 -51.145 -3.923 1.00 109.87 ? 115 VAL B C 1 ATOM 3351 O O . VAL B 2 115 ? 7.051 -52.045 -4.414 1.00 112.08 ? 115 VAL B O 1 ATOM 3352 C CB . VAL B 2 115 ? 8.375 -49.122 -5.303 1.00 106.11 ? 115 VAL B CB 1 ATOM 3353 C CG1 . VAL B 2 115 ? 8.403 -50.041 -6.522 1.00 108.86 ? 115 VAL B CG1 1 ATOM 3354 C CG2 . VAL B 2 115 ? 7.963 -47.714 -5.717 1.00 104.19 ? 115 VAL B CG2 1 ATOM 3355 N N . LYS B 2 116 ? 8.779 -51.379 -3.123 1.00 110.52 ? 116 LYS B N 1 ATOM 3356 C CA . LYS B 2 116 ? 9.181 -52.735 -2.729 1.00 114.32 ? 116 LYS B CA 1 ATOM 3357 C C . LYS B 2 116 ? 8.102 -53.423 -1.891 1.00 116.55 ? 116 LYS B C 1 ATOM 3358 O O . LYS B 2 116 ? 7.825 -54.610 -2.078 1.00 120.00 ? 116 LYS B O 1 ATOM 3359 C CB . LYS B 2 116 ? 10.498 -52.703 -1.945 1.00 115.05 ? 116 LYS B CB 1 ATOM 3360 N N . ASN B 2 117 ? 7.503 -52.670 -0.972 1.00 115.21 ? 117 ASN B N 1 ATOM 3361 C CA . ASN B 2 117 ? 6.431 -53.182 -0.115 1.00 118.14 ? 117 ASN B CA 1 ATOM 3362 C C . ASN B 2 117 ? 5.137 -53.450 -0.890 1.00 119.18 ? 117 ASN B C 1 ATOM 3363 O O . ASN B 2 117 ? 4.420 -54.403 -0.588 1.00 122.85 ? 117 ASN B O 1 ATOM 3364 C CB . ASN B 2 117 ? 6.151 -52.207 1.036 1.00 116.86 ? 117 ASN B CB 1 ATOM 3365 C CG . ASN B 2 117 ? 7.346 -52.019 1.956 1.00 116.52 ? 117 ASN B CG 1 ATOM 3366 O OD1 . ASN B 2 117 ? 8.259 -52.844 1.997 1.00 118.41 ? 117 ASN B OD1 1 ATOM 3367 N ND2 . ASN B 2 117 ? 7.343 -50.921 2.702 1.00 114.42 ? 117 ASN B ND2 1 ATOM 3368 N N . LEU B 2 118 ? 4.844 -52.603 -1.877 1.00 116.69 ? 118 LEU B N 1 ATOM 3369 C CA . LEU B 2 118 ? 3.681 -52.785 -2.754 1.00 117.94 ? 118 LEU B CA 1 ATOM 3370 C C . LEU B 2 118 ? 3.885 -53.963 -3.708 1.00 120.18 ? 118 LEU B C 1 ATOM 3371 O O . LEU B 2 118 ? 2.922 -54.633 -4.097 1.00 122.60 ? 118 LEU B O 1 ATOM 3372 C CB . LEU B 2 118 ? 3.408 -51.504 -3.557 1.00 115.16 ? 118 LEU B CB 1 ATOM 3373 C CG . LEU B 2 118 ? 2.197 -51.493 -4.500 1.00 116.61 ? 118 LEU B CG 1 ATOM 3374 C CD1 . LEU B 2 118 ? 0.910 -51.780 -3.740 1.00 119.73 ? 118 LEU B CD1 1 ATOM 3375 C CD2 . LEU B 2 118 ? 2.104 -50.161 -5.232 1.00 114.75 ? 118 LEU B CD2 1 ATOM 3376 N N . TYR B 2 119 ? 5.140 -54.202 -4.086 1.00 119.90 ? 119 TYR B N 1 ATOM 3377 C CA . TYR B 2 119 ? 5.494 -55.326 -4.948 1.00 122.52 ? 119 TYR B CA 1 ATOM 3378 C C . TYR B 2 119 ? 5.338 -56.656 -4.215 1.00 126.78 ? 119 TYR B C 1 ATOM 3379 O O . TYR B 2 119 ? 4.796 -57.614 -4.766 1.00 129.38 ? 119 TYR B O 1 ATOM 3380 C CB . TYR B 2 119 ? 6.931 -55.175 -5.447 1.00 122.05 ? 119 TYR B CB 1 ATOM 3381 C CG . TYR B 2 119 ? 7.356 -56.248 -6.423 1.00 125.32 ? 119 TYR B CG 1 ATOM 3382 C CD1 . TYR B 2 119 ? 6.805 -56.307 -7.698 1.00 125.70 ? 119 TYR B CD1 1 ATOM 3383 C CD2 . TYR B 2 119 ? 8.311 -57.202 -6.074 1.00 128.74 ? 119 TYR B CD2 1 ATOM 3384 C CE1 . TYR B 2 119 ? 7.187 -57.285 -8.597 1.00 129.03 ? 119 TYR B CE1 1 ATOM 3385 C CE2 . TYR B 2 119 ? 8.702 -58.182 -6.969 1.00 132.39 ? 119 TYR B CE2 1 ATOM 3386 C CZ . TYR B 2 119 ? 8.136 -58.217 -8.229 1.00 132.41 ? 119 TYR B CZ 1 ATOM 3387 O OH . TYR B 2 119 ? 8.511 -59.181 -9.134 1.00 136.58 ? 119 TYR B OH 1 ATOM 3388 N N . ASP B 2 120 ? 5.818 -56.703 -2.973 1.00 128.02 ? 120 ASP B N 1 ATOM 3389 C CA . ASP B 2 120 ? 5.717 -57.906 -2.141 1.00 133.11 ? 120 ASP B CA 1 ATOM 3390 C C . ASP B 2 120 ? 4.272 -58.227 -1.740 1.00 135.42 ? 120 ASP B C 1 ATOM 3391 O O . ASP B 2 120 ? 3.938 -59.389 -1.504 1.00 139.87 ? 120 ASP B O 1 ATOM 3392 C CB . ASP B 2 120 ? 6.584 -57.766 -0.881 1.00 134.42 ? 120 ASP B CB 1 ATOM 3393 C CG . ASP B 2 120 ? 8.077 -57.751 -1.187 1.00 134.30 ? 120 ASP B CG 1 ATOM 3394 O OD1 . ASP B 2 120 ? 8.450 -57.634 -2.375 1.00 132.73 ? 120 ASP B OD1 1 ATOM 3395 O OD2 . ASP B 2 120 ? 8.881 -57.855 -0.234 1.00 136.39 ? 120 ASP B OD2 1 ATOM 3396 N N . LYS B 2 121 ? 3.425 -57.200 -1.661 1.00 133.07 ? 121 LYS B N 1 ATOM 3397 C CA . LYS B 2 121 ? 2.013 -57.381 -1.305 1.00 136.07 ? 121 LYS B CA 1 ATOM 3398 C C . LYS B 2 121 ? 1.257 -58.169 -2.375 1.00 137.65 ? 121 LYS B C 1 ATOM 3399 O O . LYS B 2 121 ? 0.389 -58.982 -2.055 1.00 141.94 ? 121 LYS B O 1 ATOM 3400 C CB . LYS B 2 121 ? 1.332 -56.025 -1.069 1.00 133.71 ? 121 LYS B CB 1 ATOM 3401 C CG . LYS B 2 121 ? -0.088 -56.131 -0.524 1.00 137.84 ? 121 LYS B CG 1 ATOM 3402 C CD . LYS B 2 121 ? -0.597 -54.794 -0.007 1.00 136.70 ? 121 LYS B CD 1 ATOM 3403 C CE . LYS B 2 121 ? -1.972 -54.921 0.631 1.00 142.03 ? 121 LYS B CE 1 ATOM 3404 N NZ . LYS B 2 121 ? -3.011 -55.376 -0.334 1.00 143.78 ? 121 LYS B NZ 1 ATOM 3405 N N . VAL B 2 122 ? 1.593 -57.923 -3.640 1.00 134.74 ? 122 VAL B N 1 ATOM 3406 C CA . VAL B 2 122 ? 0.981 -58.639 -4.760 1.00 136.04 ? 122 VAL B CA 1 ATOM 3407 C C . VAL B 2 122 ? 1.584 -60.039 -4.899 1.00 139.34 ? 122 VAL B C 1 ATOM 3408 O O . VAL B 2 122 ? 0.881 -60.992 -5.241 1.00 142.54 ? 122 VAL B O 1 ATOM 3409 C CB . VAL B 2 122 ? 1.142 -57.857 -6.082 1.00 132.71 ? 122 VAL B CB 1 ATOM 3410 C CG1 . VAL B 2 122 ? 0.498 -58.613 -7.240 1.00 134.72 ? 122 VAL B CG1 1 ATOM 3411 C CG2 . VAL B 2 122 ? 0.539 -56.465 -5.943 1.00 130.26 ? 122 VAL B CG2 1 ATOM 3412 N N . ARG B 2 123 ? 2.886 -60.154 -4.639 1.00 139.23 ? 123 ARG B N 1 ATOM 3413 C CA . ARG B 2 123 ? 3.561 -61.451 -4.608 1.00 143.64 ? 123 ARG B CA 1 ATOM 3414 C C . ARG B 2 123 ? 3.008 -62.328 -3.484 1.00 148.83 ? 123 ARG B C 1 ATOM 3415 O O . ARG B 2 123 ? 2.845 -63.538 -3.657 1.00 153.29 ? 123 ARG B O 1 ATOM 3416 C CB . ARG B 2 123 ? 5.070 -61.266 -4.424 1.00 143.28 ? 123 ARG B CB 1 ATOM 3417 N N . LEU B 2 124 ? 2.721 -61.708 -2.339 1.00 148.92 ? 124 LEU B N 1 ATOM 3418 C CA . LEU B 2 124 ? 2.132 -62.402 -1.190 1.00 154.66 ? 124 LEU B CA 1 ATOM 3419 C C . LEU B 2 124 ? 0.656 -62.739 -1.417 1.00 156.89 ? 124 LEU B C 1 ATOM 3420 O O . LEU B 2 124 ? 0.202 -63.829 -1.058 1.00 162.63 ? 124 LEU B O 1 ATOM 3421 C CB . LEU B 2 124 ? 2.278 -61.555 0.078 1.00 154.31 ? 124 LEU B CB 1 ATOM 3422 N N . GLN B 2 125 ? -0.086 -61.800 -2.005 1.00 153.06 ? 125 GLN B N 1 ATOM 3423 C CA . GLN B 2 125 ? -1.509 -61.995 -2.304 1.00 155.22 ? 125 GLN B CA 1 ATOM 3424 C C . GLN B 2 125 ? -1.728 -63.058 -3.387 1.00 156.86 ? 125 GLN B C 1 ATOM 3425 O O . GLN B 2 125 ? -2.697 -63.820 -3.325 1.00 161.18 ? 125 GLN B O 1 ATOM 3426 C CB . GLN B 2 125 ? -2.152 -60.665 -2.720 1.00 151.25 ? 125 GLN B CB 1 ATOM 3427 C CG . GLN B 2 125 ? -3.642 -60.749 -3.033 1.00 154.03 ? 125 GLN B CG 1 ATOM 3428 C CD . GLN B 2 125 ? -4.318 -59.390 -3.136 1.00 152.05 ? 125 GLN B CD 1 ATOM 3429 O OE1 . GLN B 2 125 ? -5.545 -59.296 -3.068 1.00 155.47 ? 125 GLN B OE1 1 ATOM 3430 N NE2 . GLN B 2 125 ? -3.525 -58.332 -3.304 1.00 147.02 ? 125 GLN B NE2 1 ATOM 3431 N N . LEU B 2 126 ? -0.833 -63.098 -4.373 1.00 153.90 ? 126 LEU B N 1 ATOM 3432 C CA . LEU B 2 126 ? -0.862 -64.120 -5.421 1.00 155.72 ? 126 LEU B CA 1 ATOM 3433 C C . LEU B 2 126 ? 0.434 -64.927 -5.388 1.00 157.84 ? 126 LEU B C 1 ATOM 3434 O O . LEU B 2 126 ? 1.393 -64.605 -6.093 1.00 155.30 ? 126 LEU B O 1 ATOM 3435 C CB . LEU B 2 126 ? -1.048 -63.471 -6.795 1.00 151.69 ? 126 LEU B CB 1 ATOM 3436 N N . ARG B 2 127 ? 0.451 -65.974 -4.563 1.00 163.45 ? 127 ARG B N 1 ATOM 3437 C CA . ARG B 2 127 ? 1.651 -66.782 -4.349 1.00 166.85 ? 127 ARG B CA 1 ATOM 3438 C C . ARG B 2 127 ? 1.682 -67.998 -5.271 1.00 170.29 ? 127 ARG B C 1 ATOM 3439 O O . ARG B 2 127 ? 2.475 -68.046 -6.211 1.00 169.02 ? 127 ARG B O 1 ATOM 3440 C CB . ARG B 2 127 ? 1.741 -67.228 -2.886 1.00 172.18 ? 127 ARG B CB 1 ATOM 3441 N N . ASP B 2 128 ? 0.812 -68.970 -5.002 1.00 175.32 ? 128 ASP B N 1 ATOM 3442 C CA . ASP B 2 128 ? 0.804 -70.241 -5.735 1.00 179.51 ? 128 ASP B CA 1 ATOM 3443 C C . ASP B 2 128 ? 0.156 -70.133 -7.116 1.00 176.15 ? 128 ASP B C 1 ATOM 3444 O O . ASP B 2 128 ? 0.496 -70.896 -8.021 1.00 178.03 ? 128 ASP B O 1 ATOM 3445 C CB . ASP B 2 128 ? 0.087 -71.320 -4.919 1.00 186.51 ? 128 ASP B CB 1 ATOM 3446 N N . ASN B 2 129 ? -0.769 -69.189 -7.272 1.00 171.95 ? 129 ASN B N 1 ATOM 3447 C CA . ASN B 2 129 ? -1.498 -69.011 -8.530 1.00 169.58 ? 129 ASN B CA 1 ATOM 3448 C C . ASN B 2 129 ? -0.901 -67.929 -9.442 1.00 164.39 ? 129 ASN B C 1 ATOM 3449 O O . ASN B 2 129 ? -1.608 -67.373 -10.286 1.00 162.11 ? 129 ASN B O 1 ATOM 3450 C CB . ASN B 2 129 ? -2.971 -68.694 -8.241 1.00 169.62 ? 129 ASN B CB 1 ATOM 3451 N N . ALA B 2 130 ? 0.391 -67.640 -9.279 1.00 163.48 ? 130 ALA B N 1 ATOM 3452 C CA . ALA B 2 130 ? 1.078 -66.646 -10.114 1.00 159.35 ? 130 ALA B CA 1 ATOM 3453 C C . ALA B 2 130 ? 2.605 -66.799 -10.062 1.00 160.63 ? 130 ALA B C 1 ATOM 3454 O O . ALA B 2 130 ? 3.159 -67.201 -9.038 1.00 163.21 ? 130 ALA B O 1 ATOM 3455 C CB . ALA B 2 130 ? 0.676 -65.237 -9.696 1.00 154.62 ? 130 ALA B CB 1 ATOM 3456 N N . LYS B 2 131 ? 3.268 -66.475 -11.174 1.00 159.63 ? 131 LYS B N 1 ATOM 3457 C CA . LYS B 2 131 ? 4.732 -66.515 -11.270 1.00 161.39 ? 131 LYS B CA 1 ATOM 3458 C C . LYS B 2 131 ? 5.313 -65.106 -11.315 1.00 157.04 ? 131 LYS B C 1 ATOM 3459 O O . LYS B 2 131 ? 4.772 -64.224 -11.984 1.00 153.62 ? 131 LYS B O 1 ATOM 3460 C CB . LYS B 2 131 ? 5.176 -67.283 -12.520 1.00 165.31 ? 131 LYS B CB 1 ATOM 3461 C CG . LYS B 2 131 ? 6.638 -67.069 -12.901 1.00 167.35 ? 131 LYS B CG 1 ATOM 3462 C CD . LYS B 2 131 ? 7.065 -67.947 -14.064 1.00 172.70 ? 131 LYS B CD 1 ATOM 3463 C CE . LYS B 2 131 ? 8.455 -67.564 -14.548 1.00 175.26 ? 131 LYS B CE 1 ATOM 3464 N NZ . LYS B 2 131 ? 9.047 -68.597 -15.443 1.00 182.50 ? 131 LYS B NZ 1 ATOM 3465 N N . GLU B 2 132 ? 6.429 -64.914 -10.615 1.00 157.88 ? 132 GLU B N 1 ATOM 3466 C CA . GLU B 2 132 ? 7.157 -63.647 -10.626 1.00 154.33 ? 132 GLU B CA 1 ATOM 3467 C C . GLU B 2 132 ? 8.105 -63.619 -11.830 1.00 156.93 ? 132 GLU B C 1 ATOM 3468 O O . GLU B 2 132 ? 8.756 -64.624 -12.135 1.00 162.82 ? 132 GLU B O 1 ATOM 3469 C CB . GLU B 2 132 ? 7.930 -63.475 -9.313 1.00 154.43 ? 132 GLU B CB 1 ATOM 3470 C CG . GLU B 2 132 ? 8.267 -62.032 -8.978 1.00 149.39 ? 132 GLU B CG 1 ATOM 3471 C CD . GLU B 2 132 ? 8.603 -61.821 -7.512 1.00 148.94 ? 132 GLU B CD 1 ATOM 3472 O OE1 . GLU B 2 132 ? 7.745 -62.106 -6.650 1.00 149.06 ? 132 GLU B OE1 1 ATOM 3473 O OE2 . GLU B 2 132 ? 9.728 -61.365 -7.220 1.00 148.99 ? 132 GLU B OE2 1 ATOM 3474 N N . LEU B 2 133 ? 8.171 -62.477 -12.516 1.00 153.56 ? 133 LEU B N 1 ATOM 3475 C CA . LEU B 2 133 ? 8.971 -62.348 -13.741 1.00 156.42 ? 133 LEU B CA 1 ATOM 3476 C C . LEU B 2 133 ? 10.375 -61.824 -13.458 1.00 157.64 ? 133 LEU B C 1 ATOM 3477 O O . LEU B 2 133 ? 11.359 -62.522 -13.709 1.00 163.35 ? 133 LEU B O 1 ATOM 3478 C CB . LEU B 2 133 ? 8.267 -61.447 -14.765 1.00 153.78 ? 133 LEU B CB 1 ATOM 3479 C CG . LEU B 2 133 ? 7.126 -62.093 -15.556 1.00 154.91 ? 133 LEU B CG 1 ATOM 3480 C CD1 . LEU B 2 133 ? 6.434 -61.053 -16.425 1.00 152.76 ? 133 LEU B CD1 1 ATOM 3481 C CD2 . LEU B 2 133 ? 7.635 -63.258 -16.399 1.00 161.12 ? 133 LEU B CD2 1 ATOM 3482 N N . GLY B 2 134 ? 10.462 -60.597 -12.944 1.00 152.85 ? 134 GLY B N 1 ATOM 3483 C CA . GLY B 2 134 ? 11.752 -59.981 -12.625 1.00 153.59 ? 134 GLY B CA 1 ATOM 3484 C C . GLY B 2 134 ? 11.824 -58.476 -12.832 1.00 149.42 ? 134 GLY B C 1 ATOM 3485 O O . GLY B 2 134 ? 12.576 -57.791 -12.138 1.00 147.79 ? 134 GLY B O 1 ATOM 3486 N N . ASN B 2 135 ? 11.050 -57.962 -13.787 1.00 148.16 ? 135 ASN B N 1 ATOM 3487 C CA . ASN B 2 135 ? 11.032 -56.527 -14.091 1.00 145.15 ? 135 ASN B CA 1 ATOM 3488 C C . ASN B 2 135 ? 9.836 -55.803 -13.462 1.00 139.61 ? 135 ASN B C 1 ATOM 3489 O O . ASN B 2 135 ? 9.335 -54.820 -14.010 1.00 138.12 ? 135 ASN B O 1 ATOM 3490 C CB . ASN B 2 135 ? 11.048 -56.309 -15.611 1.00 148.89 ? 135 ASN B CB 1 ATOM 3491 C CG . ASN B 2 135 ? 9.786 -56.810 -16.291 1.00 149.26 ? 135 ASN B CG 1 ATOM 3492 O OD1 . ASN B 2 135 ? 9.186 -57.796 -15.863 1.00 149.25 ? 135 ASN B OD1 1 ATOM 3493 N ND2 . ASN B 2 135 ? 9.380 -56.132 -17.360 1.00 150.47 ? 135 ASN B ND2 1 ATOM 3494 N N . GLY B 2 136 ? 9.390 -56.288 -12.306 1.00 137.73 ? 136 GLY B N 1 ATOM 3495 C CA . GLY B 2 136 ? 8.253 -55.700 -11.603 1.00 133.82 ? 136 GLY B CA 1 ATOM 3496 C C . GLY B 2 136 ? 6.905 -56.138 -12.153 1.00 134.64 ? 136 GLY B C 1 ATOM 3497 O O . GLY B 2 136 ? 5.964 -55.343 -12.199 1.00 132.81 ? 136 GLY B O 1 ATOM 3498 N N . CYS B 2 137 ? 6.805 -57.403 -12.560 1.00 138.06 ? 137 CYS B N 1 ATOM 3499 C CA . CYS B 2 137 ? 5.568 -57.942 -13.136 1.00 139.32 ? 137 CYS B CA 1 ATOM 3500 C C . CYS B 2 137 ? 5.266 -59.350 -12.628 1.00 141.45 ? 137 CYS B C 1 ATOM 3501 O O . CYS B 2 137 ? 6.169 -60.067 -12.192 1.00 143.71 ? 137 CYS B O 1 ATOM 3502 C CB . CYS B 2 137 ? 5.652 -57.956 -14.666 1.00 142.26 ? 137 CYS B CB 1 ATOM 3503 S SG . CYS B 2 137 ? 5.747 -56.318 -15.431 1.00 141.31 ? 137 CYS B SG 1 ATOM 3504 N N . PHE B 2 138 ? 3.988 -59.726 -12.689 1.00 141.57 ? 138 PHE B N 1 ATOM 3505 C CA . PHE B 2 138 ? 3.527 -61.062 -12.299 1.00 144.14 ? 138 PHE B CA 1 ATOM 3506 C C . PHE B 2 138 ? 2.714 -61.691 -13.430 1.00 146.33 ? 138 PHE B C 1 ATOM 3507 O O . PHE B 2 138 ? 2.012 -60.986 -14.156 1.00 145.27 ? 138 PHE B O 1 ATOM 3508 C CB . PHE B 2 138 ? 2.666 -60.990 -11.033 1.00 142.88 ? 138 PHE B CB 1 ATOM 3509 C CG . PHE B 2 138 ? 3.420 -60.562 -9.802 1.00 141.53 ? 138 PHE B CG 1 ATOM 3510 C CD1 . PHE B 2 138 ? 4.036 -61.503 -8.986 1.00 144.43 ? 138 PHE B CD1 1 ATOM 3511 C CD2 . PHE B 2 138 ? 3.505 -59.220 -9.453 1.00 137.62 ? 138 PHE B CD2 1 ATOM 3512 C CE1 . PHE B 2 138 ? 4.728 -61.115 -7.851 1.00 143.40 ? 138 PHE B CE1 1 ATOM 3513 C CE2 . PHE B 2 138 ? 4.195 -58.826 -8.319 1.00 136.42 ? 138 PHE B CE2 1 ATOM 3514 C CZ . PHE B 2 138 ? 4.807 -59.775 -7.517 1.00 139.29 ? 138 PHE B CZ 1 ATOM 3515 N N . GLU B 2 139 ? 2.810 -63.014 -13.565 1.00 149.80 ? 139 GLU B N 1 ATOM 3516 C CA . GLU B 2 139 ? 2.081 -63.766 -14.590 1.00 152.26 ? 139 GLU B CA 1 ATOM 3517 C C . GLU B 2 139 ? 1.078 -64.723 -13.954 1.00 154.02 ? 139 GLU B C 1 ATOM 3518 O O . GLU B 2 139 ? 1.471 -65.659 -13.258 1.00 156.80 ? 139 GLU B O 1 ATOM 3519 C CB . GLU B 2 139 ? 3.053 -64.575 -15.451 1.00 156.02 ? 139 GLU B CB 1 ATOM 3520 C CG . GLU B 2 139 ? 3.619 -63.827 -16.643 1.00 156.31 ? 139 GLU B CG 1 ATOM 3521 C CD . GLU B 2 139 ? 4.446 -64.728 -17.541 1.00 161.47 ? 139 GLU B CD 1 ATOM 3522 O OE1 . GLU B 2 139 ? 5.329 -65.443 -17.018 1.00 164.00 ? 139 GLU B OE1 1 ATOM 3523 O OE2 . GLU B 2 139 ? 4.214 -64.726 -18.768 1.00 163.58 ? 139 GLU B OE2 1 ATOM 3524 N N . PHE B 2 140 ? -0.209 -64.500 -14.208 1.00 153.46 ? 140 PHE B N 1 ATOM 3525 C CA . PHE B 2 140 ? -1.259 -65.362 -13.667 1.00 155.61 ? 140 PHE B CA 1 ATOM 3526 C C . PHE B 2 140 ? -1.297 -66.717 -14.375 1.00 159.85 ? 140 PHE B C 1 ATOM 3527 O O . PHE B 2 140 ? -1.272 -66.785 -15.607 1.00 161.11 ? 140 PHE B O 1 ATOM 3528 C CB . PHE B 2 140 ? -2.629 -64.691 -13.792 1.00 154.66 ? 140 PHE B CB 1 ATOM 3529 C CG . PHE B 2 140 ? -2.814 -63.505 -12.889 1.00 151.84 ? 140 PHE B CG 1 ATOM 3530 C CD1 . PHE B 2 140 ? -3.297 -63.670 -11.596 1.00 152.64 ? 140 PHE B CD1 1 ATOM 3531 C CD2 . PHE B 2 140 ? -2.520 -62.223 -13.334 1.00 148.99 ? 140 PHE B CD2 1 ATOM 3532 C CE1 . PHE B 2 140 ? -3.476 -62.580 -10.762 1.00 150.67 ? 140 PHE B CE1 1 ATOM 3533 C CE2 . PHE B 2 140 ? -2.697 -61.128 -12.504 1.00 146.77 ? 140 PHE B CE2 1 ATOM 3534 C CZ . PHE B 2 140 ? -3.175 -61.307 -11.216 1.00 147.52 ? 140 PHE B CZ 1 ATOM 3535 N N . TYR B 2 141 ? -1.371 -67.789 -13.589 1.00 162.75 ? 141 TYR B N 1 ATOM 3536 C CA . TYR B 2 141 ? -1.580 -69.137 -14.125 1.00 166.87 ? 141 TYR B CA 1 ATOM 3537 C C . TYR B 2 141 ? -3.063 -69.399 -14.431 1.00 167.92 ? 141 TYR B C 1 ATOM 3538 O O . TYR B 2 141 ? -3.407 -70.446 -14.985 1.00 171.13 ? 141 TYR B O 1 ATOM 3539 C CB . TYR B 2 141 ? -1.044 -70.195 -13.151 1.00 170.62 ? 141 TYR B CB 1 ATOM 3540 C CG . TYR B 2 141 ? 0.467 -70.302 -13.132 1.00 171.60 ? 141 TYR B CG 1 ATOM 3541 C CD1 . TYR B 2 141 ? 1.140 -71.067 -14.081 1.00 174.99 ? 141 TYR B CD1 1 ATOM 3542 C CD2 . TYR B 2 141 ? 1.222 -69.640 -12.166 1.00 169.70 ? 141 TYR B CD2 1 ATOM 3543 C CE1 . TYR B 2 141 ? 2.521 -71.170 -14.071 1.00 177.12 ? 141 TYR B CE1 1 ATOM 3544 C CE2 . TYR B 2 141 ? 2.604 -69.738 -12.147 1.00 171.34 ? 141 TYR B CE2 1 ATOM 3545 C CZ . TYR B 2 141 ? 3.248 -70.505 -13.103 1.00 175.42 ? 141 TYR B CZ 1 ATOM 3546 O OH . TYR B 2 141 ? 4.619 -70.606 -13.091 1.00 178.20 ? 141 TYR B OH 1 ATOM 3547 N N . HIS B 2 142 ? -3.927 -68.449 -14.063 1.00 165.62 ? 142 HIS B N 1 ATOM 3548 C CA . HIS B 2 142 ? -5.367 -68.537 -14.318 1.00 167.24 ? 142 HIS B CA 1 ATOM 3549 C C . HIS B 2 142 ? -5.888 -67.253 -14.978 1.00 164.76 ? 142 HIS B C 1 ATOM 3550 O O . HIS B 2 142 ? -5.125 -66.317 -15.223 1.00 161.52 ? 142 HIS B O 1 ATOM 3551 C CB . HIS B 2 142 ? -6.121 -68.829 -13.009 1.00 169.41 ? 142 HIS B CB 1 ATOM 3552 C CG . HIS B 2 142 ? -6.016 -67.741 -11.983 1.00 166.95 ? 142 HIS B CG 1 ATOM 3553 N ND1 . HIS B 2 142 ? -4.957 -67.642 -11.104 1.00 165.80 ? 142 HIS B ND1 1 ATOM 3554 C CD2 . HIS B 2 142 ? -6.846 -66.712 -11.688 1.00 165.83 ? 142 HIS B CD2 1 ATOM 3555 C CE1 . HIS B 2 142 ? -5.137 -66.596 -10.317 1.00 163.62 ? 142 HIS B CE1 1 ATOM 3556 N NE2 . HIS B 2 142 ? -6.275 -66.014 -10.651 1.00 163.72 ? 142 HIS B NE2 1 ATOM 3557 N N . ARG B 2 143 ? -7.187 -67.226 -15.273 1.00 167.03 ? 143 ARG B N 1 ATOM 3558 C CA . ARG B 2 143 ? -7.825 -66.077 -15.919 1.00 166.36 ? 143 ARG B CA 1 ATOM 3559 C C . ARG B 2 143 ? -8.297 -65.066 -14.874 1.00 165.61 ? 143 ARG B C 1 ATOM 3560 O O . ARG B 2 143 ? -9.172 -65.372 -14.062 1.00 168.15 ? 143 ARG B O 1 ATOM 3561 C CB . ARG B 2 143 ? -9.018 -66.538 -16.772 1.00 169.93 ? 143 ARG B CB 1 ATOM 3562 C CG . ARG B 2 143 ? -8.710 -67.647 -17.775 1.00 171.72 ? 143 ARG B CG 1 ATOM 3563 C CD . ARG B 2 143 ? -7.536 -67.295 -18.677 1.00 170.06 ? 143 ARG B CD 1 ATOM 3564 N NE . ARG B 2 143 ? -7.742 -66.021 -19.366 1.00 169.20 ? 143 ARG B NE 1 ATOM 3565 C CZ . ARG B 2 143 ? -6.778 -65.266 -19.893 1.00 167.50 ? 143 ARG B CZ 1 ATOM 3566 N NH1 . ARG B 2 143 ? -5.498 -65.627 -19.824 1.00 166.31 ? 143 ARG B NH1 1 ATOM 3567 N NH2 . ARG B 2 143 ? -7.099 -64.126 -20.495 1.00 167.69 ? 143 ARG B NH2 1 ATOM 3568 N N . CYS B 2 144 ? -7.717 -63.867 -14.900 1.00 163.06 ? 144 CYS B N 1 ATOM 3569 C CA . CYS B 2 144 ? -8.064 -62.801 -13.953 1.00 162.51 ? 144 CYS B CA 1 ATOM 3570 C C . CYS B 2 144 ? -8.704 -61.609 -14.673 1.00 162.88 ? 144 CYS B C 1 ATOM 3571 O O . CYS B 2 144 ? -8.005 -60.768 -15.245 1.00 160.34 ? 144 CYS B O 1 ATOM 3572 C CB . CYS B 2 144 ? -6.819 -62.354 -13.175 1.00 159.23 ? 144 CYS B CB 1 ATOM 3573 S SG . CYS B 2 144 ? -7.115 -61.114 -11.885 1.00 158.60 ? 144 CYS B SG 1 ATOM 3574 N N . ASP B 2 145 ? -10.036 -61.550 -14.638 1.00 166.66 ? 145 ASP B N 1 ATOM 3575 C CA . ASP B 2 145 ? -10.798 -60.468 -15.279 1.00 168.47 ? 145 ASP B CA 1 ATOM 3576 C C . ASP B 2 145 ? -10.647 -59.140 -14.516 1.00 167.06 ? 145 ASP B C 1 ATOM 3577 O O . ASP B 2 145 ? -9.876 -59.054 -13.559 1.00 163.77 ? 145 ASP B O 1 ATOM 3578 C CB . ASP B 2 145 ? -12.279 -60.865 -15.423 1.00 173.71 ? 145 ASP B CB 1 ATOM 3579 C CG . ASP B 2 145 ? -13.000 -60.964 -14.087 1.00 175.95 ? 145 ASP B CG 1 ATOM 3580 O OD1 . ASP B 2 145 ? -12.450 -61.584 -13.153 1.00 173.93 ? 145 ASP B OD1 1 ATOM 3581 O OD2 . ASP B 2 145 ? -14.123 -60.429 -13.977 1.00 180.32 ? 145 ASP B OD2 1 ATOM 3582 N N . ASN B 2 146 ? -11.372 -58.108 -14.947 1.00 170.01 ? 146 ASN B N 1 ATOM 3583 C CA . ASN B 2 146 ? -11.270 -56.777 -14.330 1.00 169.23 ? 146 ASN B CA 1 ATOM 3584 C C . ASN B 2 146 ? -11.700 -56.742 -12.861 1.00 170.36 ? 146 ASN B C 1 ATOM 3585 O O . ASN B 2 146 ? -11.081 -56.048 -12.057 1.00 167.69 ? 146 ASN B O 1 ATOM 3586 C CB . ASN B 2 146 ? -12.069 -55.740 -15.133 1.00 173.65 ? 146 ASN B CB 1 ATOM 3587 C CG . ASN B 2 146 ? -11.449 -55.439 -16.489 1.00 172.86 ? 146 ASN B CG 1 ATOM 3588 O OD1 . ASN B 2 146 ? -10.258 -55.666 -16.708 1.00 168.34 ? 146 ASN B OD1 1 ATOM 3589 N ND2 . ASN B 2 146 ? -12.259 -54.922 -17.407 1.00 178.17 ? 146 ASN B ND2 1 ATOM 3590 N N . GLU B 2 147 ? -12.750 -57.485 -12.515 1.00 175.09 ? 147 GLU B N 1 ATOM 3591 C CA . GLU B 2 147 ? -13.191 -57.595 -11.118 1.00 177.43 ? 147 GLU B CA 1 ATOM 3592 C C . GLU B 2 147 ? -12.196 -58.391 -10.269 1.00 173.77 ? 147 GLU B C 1 ATOM 3593 O O . GLU B 2 147 ? -12.037 -58.120 -9.079 1.00 173.74 ? 147 GLU B O 1 ATOM 3594 C CB . GLU B 2 147 ? -14.583 -58.224 -11.027 1.00 184.37 ? 147 GLU B CB 1 ATOM 3595 C CG . GLU B 2 147 ? -15.707 -57.289 -11.444 1.00 190.01 ? 147 GLU B CG 1 ATOM 3596 C CD . GLU B 2 147 ? -17.080 -57.879 -11.190 1.00 197.64 ? 147 GLU B CD 1 ATOM 3597 O OE1 . GLU B 2 147 ? -17.306 -59.046 -11.571 1.00 198.59 ? 147 GLU B OE1 1 ATOM 3598 O OE2 . GLU B 2 147 ? -17.931 -57.178 -10.603 1.00 203.22 ? 147 GLU B OE2 1 ATOM 3599 N N . CYS B 2 148 ? -11.541 -59.375 -10.883 1.00 171.50 ? 148 CYS B N 1 ATOM 3600 C CA . CYS B 2 148 ? -10.433 -60.089 -10.241 1.00 168.42 ? 148 CYS B CA 1 ATOM 3601 C C . CYS B 2 148 ? -9.221 -59.173 -10.064 1.00 163.09 ? 148 CYS B C 1 ATOM 3602 O O . CYS B 2 148 ? -8.527 -59.243 -9.049 1.00 161.64 ? 148 CYS B O 1 ATOM 3603 C CB . CYS B 2 148 ? -10.033 -61.324 -11.057 1.00 168.01 ? 148 CYS B CB 1 ATOM 3604 S SG . CYS B 2 148 ? -8.423 -62.032 -10.620 1.00 164.47 ? 148 CYS B SG 1 ATOM 3605 N N . MET B 2 149 ? -8.966 -58.326 -11.059 1.00 161.04 ? 149 MET B N 1 ATOM 3606 C CA . MET B 2 149 ? -7.835 -57.396 -11.016 1.00 156.36 ? 149 MET B CA 1 ATOM 3607 C C . MET B 2 149 ? -8.092 -56.301 -9.978 1.00 156.07 ? 149 MET B C 1 ATOM 3608 O O . MET B 2 149 ? -7.167 -55.844 -9.308 1.00 152.63 ? 149 MET B O 1 ATOM 3609 C CB . MET B 2 149 ? -7.578 -56.782 -12.400 1.00 155.84 ? 149 MET B CB 1 ATOM 3610 C CG . MET B 2 149 ? -6.109 -56.526 -12.706 1.00 151.79 ? 149 MET B CG 1 ATOM 3611 S SD . MET B 2 149 ? -5.172 -58.021 -13.101 1.00 151.24 ? 149 MET B SD 1 ATOM 3612 C CE . MET B 2 149 ? -5.788 -58.415 -14.738 1.00 154.27 ? 149 MET B CE 1 ATOM 3613 N N . GLU B 2 150 ? -9.352 -55.888 -9.853 1.00 160.09 ? 150 GLU B N 1 ATOM 3614 C CA . GLU B 2 150 ? -9.775 -55.006 -8.766 1.00 161.42 ? 150 GLU B CA 1 ATOM 3615 C C . GLU B 2 150 ? -9.466 -55.635 -7.410 1.00 160.84 ? 150 GLU B C 1 ATOM 3616 O O . GLU B 2 150 ? -8.976 -54.957 -6.512 1.00 158.93 ? 150 GLU B O 1 ATOM 3617 C CB . GLU B 2 150 ? -11.275 -54.715 -8.857 1.00 168.24 ? 150 GLU B CB 1 ATOM 3618 C CG . GLU B 2 150 ? -11.662 -53.762 -9.974 1.00 169.89 ? 150 GLU B CG 1 ATOM 3619 C CD . GLU B 2 150 ? -13.135 -53.849 -10.339 1.00 177.31 ? 150 GLU B CD 1 ATOM 3620 O OE1 . GLU B 2 150 ? -13.959 -54.155 -9.451 1.00 181.81 ? 150 GLU B OE1 1 ATOM 3621 O OE2 . GLU B 2 150 ? -13.471 -53.617 -11.520 1.00 179.29 ? 150 GLU B OE2 1 ATOM 3622 N N . SER B 2 151 ? -9.751 -56.929 -7.276 1.00 162.75 ? 151 SER B N 1 ATOM 3623 C CA . SER B 2 151 ? -9.511 -57.671 -6.034 1.00 163.97 ? 151 SER B CA 1 ATOM 3624 C C . SER B 2 151 ? -8.055 -57.589 -5.580 1.00 158.72 ? 151 SER B C 1 ATOM 3625 O O . SER B 2 151 ? -7.780 -57.424 -4.390 1.00 159.46 ? 151 SER B O 1 ATOM 3626 C CB . SER B 2 151 ? -9.898 -59.144 -6.205 1.00 167.31 ? 151 SER B CB 1 ATOM 3627 O OG . SER B 2 151 ? -11.162 -59.281 -6.828 1.00 171.80 ? 151 SER B OG 1 ATOM 3628 N N . VAL B 2 152 ? -7.133 -57.709 -6.533 1.00 154.11 ? 152 VAL B N 1 ATOM 3629 C CA . VAL B 2 152 ? -5.696 -57.636 -6.250 1.00 149.36 ? 152 VAL B CA 1 ATOM 3630 C C . VAL B 2 152 ? -5.297 -56.211 -5.845 1.00 146.28 ? 152 VAL B C 1 ATOM 3631 O O . VAL B 2 152 ? -4.466 -56.022 -4.953 1.00 144.27 ? 152 VAL B O 1 ATOM 3632 C CB . VAL B 2 152 ? -4.862 -58.122 -7.459 1.00 146.63 ? 152 VAL B CB 1 ATOM 3633 C CG1 . VAL B 2 152 ? -3.371 -57.899 -7.228 1.00 142.73 ? 152 VAL B CG1 1 ATOM 3634 C CG2 . VAL B 2 152 ? -5.142 -59.593 -7.738 1.00 149.51 ? 152 VAL B CG2 1 ATOM 3635 N N . ARG B 2 153 ? -5.892 -55.219 -6.506 1.00 146.23 ? 153 ARG B N 1 ATOM 3636 C CA . ARG B 2 153 ? -5.754 -53.811 -6.109 1.00 144.24 ? 153 ARG B CA 1 ATOM 3637 C C . ARG B 2 153 ? -6.448 -53.545 -4.771 1.00 147.60 ? 153 ARG B C 1 ATOM 3638 O O . ARG B 2 153 ? -5.947 -52.783 -3.945 1.00 145.74 ? 153 ARG B O 1 ATOM 3639 C CB . ARG B 2 153 ? -6.341 -52.888 -7.190 1.00 145.13 ? 153 ARG B CB 1 ATOM 3640 C CG . ARG B 2 153 ? -5.362 -52.506 -8.290 1.00 141.31 ? 153 ARG B CG 1 ATOM 3641 C CD . ARG B 2 153 ? -5.939 -52.681 -9.688 1.00 143.80 ? 153 ARG B CD 1 ATOM 3642 N NE . ARG B 2 153 ? -7.203 -51.977 -9.889 1.00 148.25 ? 153 ARG B NE 1 ATOM 3643 C CZ . ARG B 2 153 ? -7.972 -52.104 -10.970 1.00 151.67 ? 153 ARG B CZ 1 ATOM 3644 N NH1 . ARG B 2 153 ? -7.618 -52.911 -11.968 1.00 150.77 ? 153 ARG B NH1 1 ATOM 3645 N NH2 . ARG B 2 153 ? -9.105 -51.419 -11.057 1.00 156.69 ? 153 ARG B NH2 1 ATOM 3646 N N . ASN B 2 154 ? -7.602 -54.181 -4.574 1.00 153.03 ? 154 ASN B N 1 ATOM 3647 C CA . ASN B 2 154 ? -8.408 -54.016 -3.362 1.00 157.95 ? 154 ASN B CA 1 ATOM 3648 C C . ASN B 2 154 ? -7.721 -54.598 -2.123 1.00 157.70 ? 154 ASN B C 1 ATOM 3649 O O . ASN B 2 154 ? -7.705 -53.969 -1.064 1.00 158.84 ? 154 ASN B O 1 ATOM 3650 C CB . ASN B 2 154 ? -9.785 -54.672 -3.560 1.00 164.53 ? 154 ASN B CB 1 ATOM 3651 C CG . ASN B 2 154 ? -10.762 -54.351 -2.443 1.00 171.34 ? 154 ASN B CG 1 ATOM 3652 O OD1 . ASN B 2 154 ? -10.694 -53.289 -1.822 1.00 171.58 ? 154 ASN B OD1 1 ATOM 3653 N ND2 . ASN B 2 154 ? -11.692 -55.267 -2.192 1.00 177.54 ? 154 ASN B ND2 1 ATOM 3654 N N . GLY B 2 155 ? -7.161 -55.799 -2.266 1.00 156.67 ? 155 GLY B N 1 ATOM 3655 C CA . GLY B 2 155 ? -6.468 -56.478 -1.170 1.00 157.36 ? 155 GLY B CA 1 ATOM 3656 C C . GLY B 2 155 ? -7.395 -57.376 -0.372 1.00 164.64 ? 155 GLY B C 1 ATOM 3657 O O . GLY B 2 155 ? -8.289 -58.012 -0.928 1.00 167.60 ? 155 GLY B O 1 ATOM 3658 N N . ASP C 1 2 ? 29.777 -75.426 -11.767 1.00 171.16 ? 1 ASP C N 1 ATOM 3659 C CA . ASP C 1 2 ? 28.409 -75.706 -11.234 1.00 171.24 ? 1 ASP C CA 1 ATOM 3660 C C . ASP C 1 2 ? 27.795 -74.521 -10.466 1.00 166.54 ? 1 ASP C C 1 ATOM 3661 O O . ASP C 1 2 ? 26.571 -74.372 -10.447 1.00 165.87 ? 1 ASP C O 1 ATOM 3662 C CB . ASP C 1 2 ? 28.424 -76.958 -10.337 1.00 174.27 ? 1 ASP C CB 1 ATOM 3663 C CG . ASP C 1 2 ? 28.533 -78.262 -11.128 1.00 179.39 ? 1 ASP C CG 1 ATOM 3664 O OD1 . ASP C 1 2 ? 27.974 -78.360 -12.243 1.00 180.81 ? 1 ASP C OD1 1 ATOM 3665 O OD2 . ASP C 1 2 ? 29.170 -79.206 -10.614 1.00 182.03 ? 1 ASP C OD2 1 ATOM 3666 N N . GLN C 1 3 ? 28.625 -73.680 -9.846 1.00 163.32 ? 2 GLN C N 1 ATOM 3667 C CA . GLN C 1 3 ? 28.115 -72.632 -8.952 1.00 159.29 ? 2 GLN C CA 1 ATOM 3668 C C . GLN C 1 3 ? 28.785 -71.266 -9.126 1.00 155.24 ? 2 GLN C C 1 ATOM 3669 O O . GLN C 1 3 ? 29.979 -71.177 -9.409 1.00 155.39 ? 2 GLN C O 1 ATOM 3670 C CB . GLN C 1 3 ? 28.253 -73.089 -7.496 1.00 159.51 ? 2 GLN C CB 1 ATOM 3671 C CG . GLN C 1 3 ? 27.446 -72.259 -6.503 1.00 156.40 ? 2 GLN C CG 1 ATOM 3672 C CD . GLN C 1 3 ? 27.337 -72.897 -5.125 1.00 157.51 ? 2 GLN C CD 1 ATOM 3673 O OE1 . GLN C 1 3 ? 27.398 -72.205 -4.106 1.00 154.51 ? 2 GLN C OE1 1 ATOM 3674 N NE2 . GLN C 1 3 ? 27.167 -74.217 -5.087 1.00 161.65 ? 2 GLN C NE2 1 ATOM 3675 N N . ILE C 1 4 ? 27.990 -70.210 -8.947 1.00 151.94 ? 3 ILE C N 1 ATOM 3676 C CA . ILE C 1 4 ? 28.476 -68.824 -8.889 1.00 147.64 ? 3 ILE C CA 1 ATOM 3677 C C . ILE C 1 4 ? 27.859 -68.147 -7.660 1.00 144.26 ? 3 ILE C C 1 ATOM 3678 O O . ILE C 1 4 ? 26.743 -68.489 -7.263 1.00 145.11 ? 3 ILE C O 1 ATOM 3679 C CB . ILE C 1 4 ? 28.136 -68.023 -10.173 1.00 147.06 ? 3 ILE C CB 1 ATOM 3680 C CG1 . ILE C 1 4 ? 28.659 -66.582 -10.066 1.00 143.00 ? 3 ILE C CG1 1 ATOM 3681 C CG2 . ILE C 1 4 ? 26.635 -68.014 -10.444 1.00 147.68 ? 3 ILE C CG2 1 ATOM 3682 C CD1 . ILE C 1 4 ? 28.624 -65.810 -11.367 1.00 142.82 ? 3 ILE C CD1 1 ATOM 3683 N N . CYS C 1 5 ? 28.583 -67.199 -7.062 1.00 140.33 ? 4 CYS C N 1 ATOM 3684 C CA . CYS C 1 5 ? 28.141 -66.552 -5.823 1.00 137.24 ? 4 CYS C CA 1 ATOM 3685 C C . CYS C 1 5 ? 28.463 -65.053 -5.792 1.00 132.88 ? 4 CYS C C 1 ATOM 3686 O O . CYS C 1 5 ? 29.334 -64.584 -6.524 1.00 131.80 ? 4 CYS C O 1 ATOM 3687 C CB . CYS C 1 5 ? 28.791 -67.242 -4.618 1.00 138.03 ? 4 CYS C CB 1 ATOM 3688 S SG . CYS C 1 5 ? 28.511 -69.030 -4.518 1.00 143.22 ? 4 CYS C SG 1 ATOM 3689 N N . ILE C 1 6 ? 27.744 -64.314 -4.946 1.00 130.30 ? 5 ILE C N 1 ATOM 3690 C CA . ILE C 1 6 ? 28.039 -62.898 -4.676 1.00 126.45 ? 5 ILE C CA 1 ATOM 3691 C C . ILE C 1 6 ? 28.865 -62.795 -3.392 1.00 124.75 ? 5 ILE C C 1 ATOM 3692 O O . ILE C 1 6 ? 28.628 -63.539 -2.436 1.00 126.27 ? 5 ILE C O 1 ATOM 3693 C CB . ILE C 1 6 ? 26.750 -62.052 -4.515 1.00 124.62 ? 5 ILE C CB 1 ATOM 3694 C CG1 . ILE C 1 6 ? 25.865 -62.143 -5.767 1.00 126.50 ? 5 ILE C CG1 1 ATOM 3695 C CG2 . ILE C 1 6 ? 27.087 -60.593 -4.212 1.00 120.58 ? 5 ILE C CG2 1 ATOM 3696 C CD1 . ILE C 1 6 ? 26.454 -61.503 -7.009 1.00 125.94 ? 5 ILE C CD1 1 ATOM 3697 N N . GLY C 1 7 ? 29.835 -61.881 -3.379 1.00 122.02 ? 6 GLY C N 1 ATOM 3698 C CA . GLY C 1 7 ? 30.672 -61.646 -2.197 1.00 120.44 ? 6 GLY C CA 1 ATOM 3699 C C . GLY C 1 7 ? 31.294 -60.264 -2.192 1.00 116.90 ? 6 GLY C C 1 ATOM 3700 O O . GLY C 1 7 ? 31.021 -59.452 -3.078 1.00 115.25 ? 6 GLY C O 1 ATOM 3701 N N . TYR C 1 8 ? 32.136 -60.004 -1.193 1.00 116.21 ? 7 TYR C N 1 ATOM 3702 C CA . TYR C 1 8 ? 32.712 -58.672 -0.987 1.00 112.89 ? 7 TYR C CA 1 ATOM 3703 C C . TYR C 1 8 ? 34.163 -58.712 -0.497 1.00 113.53 ? 7 TYR C C 1 ATOM 3704 O O . TYR C 1 8 ? 34.658 -59.754 -0.063 1.00 116.38 ? 7 TYR C O 1 ATOM 3705 C CB . TYR C 1 8 ? 31.841 -57.856 -0.020 1.00 110.19 ? 7 TYR C CB 1 ATOM 3706 C CG . TYR C 1 8 ? 31.709 -58.440 1.377 1.00 110.64 ? 7 TYR C CG 1 ATOM 3707 C CD1 . TYR C 1 8 ? 30.895 -59.545 1.616 1.00 113.04 ? 7 TYR C CD1 1 ATOM 3708 C CD2 . TYR C 1 8 ? 32.387 -57.876 2.462 1.00 108.32 ? 7 TYR C CD2 1 ATOM 3709 C CE1 . TYR C 1 8 ? 30.764 -60.081 2.888 1.00 113.85 ? 7 TYR C CE1 1 ATOM 3710 C CE2 . TYR C 1 8 ? 32.263 -58.407 3.739 1.00 109.09 ? 7 TYR C CE2 1 ATOM 3711 C CZ . TYR C 1 8 ? 31.447 -59.512 3.946 1.00 111.88 ? 7 TYR C CZ 1 ATOM 3712 O OH . TYR C 1 8 ? 31.312 -60.055 5.205 1.00 112.72 ? 7 TYR C OH 1 ATOM 3713 N N . HIS C 1 9 ? 34.822 -57.557 -0.568 1.00 111.39 ? 8 HIS C N 1 ATOM 3714 C CA . HIS C 1 9 ? 36.259 -57.428 -0.305 1.00 112.22 ? 8 HIS C CA 1 ATOM 3715 C C . HIS C 1 9 ? 36.624 -57.545 1.180 1.00 112.73 ? 8 HIS C C 1 ATOM 3716 O O . HIS C 1 9 ? 35.836 -57.181 2.059 1.00 111.78 ? 8 HIS C O 1 ATOM 3717 C CB . HIS C 1 9 ? 36.756 -56.081 -0.858 1.00 109.54 ? 8 HIS C CB 1 ATOM 3718 C CG . HIS C 1 9 ? 38.209 -55.811 -0.608 1.00 109.39 ? 8 HIS C CG 1 ATOM 3719 N ND1 . HIS C 1 9 ? 39.196 -56.166 -1.502 1.00 111.46 ? 8 HIS C ND1 1 ATOM 3720 C CD2 . HIS C 1 9 ? 38.839 -55.208 0.428 1.00 107.68 ? 8 HIS C CD2 1 ATOM 3721 C CE1 . HIS C 1 9 ? 40.372 -55.801 -1.023 1.00 111.00 ? 8 HIS C CE1 1 ATOM 3722 N NE2 . HIS C 1 9 ? 40.184 -55.219 0.148 1.00 108.52 ? 8 HIS C NE2 1 ATOM 3723 N N . ALA C 1 10 ? 37.833 -58.043 1.439 1.00 114.98 ? 9 ALA C N 1 ATOM 3724 C CA . ALA C 1 10 ? 38.377 -58.147 2.795 1.00 115.54 ? 9 ALA C CA 1 ATOM 3725 C C . ALA C 1 10 ? 39.907 -58.084 2.756 1.00 116.55 ? 9 ALA C C 1 ATOM 3726 O O . ALA C 1 10 ? 40.523 -58.621 1.832 1.00 118.88 ? 9 ALA C O 1 ATOM 3727 C CB . ALA C 1 10 ? 37.919 -59.446 3.442 1.00 118.78 ? 9 ALA C CB 1 ATOM 3728 N N . ASN C 1 11 ? 40.512 -57.431 3.750 1.00 114.97 ? 10 ASN C N 1 ATOM 3729 C CA . ASN C 1 11 ? 41.979 -57.391 3.884 1.00 116.06 ? 10 ASN C CA 1 ATOM 3730 C C . ASN C 1 11 ? 42.446 -57.325 5.342 1.00 116.14 ? 10 ASN C C 1 ATOM 3731 O O . ASN C 1 11 ? 41.652 -57.040 6.239 1.00 115.40 ? 10 ASN C O 1 ATOM 3732 C CB . ASN C 1 11 ? 42.575 -56.228 3.074 1.00 113.50 ? 10 ASN C CB 1 ATOM 3733 C CG . ASN C 1 11 ? 42.025 -54.868 3.481 1.00 109.34 ? 10 ASN C CG 1 ATOM 3734 O OD1 . ASN C 1 11 ? 41.077 -54.768 4.259 1.00 108.21 ? 10 ASN C OD1 1 ATOM 3735 N ND2 . ASN C 1 11 ? 42.620 -53.809 2.942 1.00 107.08 ? 10 ASN C ND2 1 ATOM 3736 N N . ASN C 1 12 ? 43.731 -57.593 5.572 1.00 117.87 ? 11 ASN C N 1 ATOM 3737 C CA . ASN C 1 12 ? 44.307 -57.527 6.919 1.00 118.30 ? 11 ASN C CA 1 ATOM 3738 C C . ASN C 1 12 ? 44.451 -56.068 7.362 1.00 114.27 ? 11 ASN C C 1 ATOM 3739 O O . ASN C 1 12 ? 45.555 -55.521 7.388 1.00 113.78 ? 11 ASN C O 1 ATOM 3740 C CB . ASN C 1 12 ? 45.663 -58.242 6.971 1.00 121.98 ? 11 ASN C CB 1 ATOM 3741 C CG . ASN C 1 12 ? 45.551 -59.734 6.698 1.00 126.90 ? 11 ASN C CG 1 ATOM 3742 O OD1 . ASN C 1 12 ? 44.482 -60.237 6.347 1.00 127.51 ? 11 ASN C OD1 1 ATOM 3743 N ND2 . ASN C 1 12 ? 46.663 -60.451 6.856 1.00 130.47 ? 11 ASN C ND2 1 ATOM 3744 N N . SER C 1 13 ? 43.321 -55.461 7.724 1.00 111.30 ? 12 SER C N 1 ATOM 3745 C CA . SER C 1 13 ? 43.226 -54.016 7.930 1.00 107.03 ? 12 SER C CA 1 ATOM 3746 C C . SER C 1 13 ? 43.237 -53.617 9.407 1.00 106.10 ? 12 SER C C 1 ATOM 3747 O O . SER C 1 13 ? 44.068 -52.807 9.829 1.00 104.77 ? 12 SER C O 1 ATOM 3748 C CB . SER C 1 13 ? 41.954 -53.490 7.263 1.00 104.53 ? 12 SER C CB 1 ATOM 3749 O OG . SER C 1 13 ? 41.970 -52.079 7.168 1.00 100.66 ? 12 SER C OG 1 ATOM 3750 N N . THR C 1 14 ? 42.294 -54.160 10.176 1.00 106.71 ? 13 THR C N 1 ATOM 3751 C CA . THR C 1 14 ? 42.163 -53.867 11.614 1.00 106.30 ? 13 THR C CA 1 ATOM 3752 C C . THR C 1 14 ? 41.882 -52.390 11.978 1.00 102.24 ? 13 THR C C 1 ATOM 3753 O O . THR C 1 14 ? 41.832 -52.050 13.166 1.00 102.01 ? 13 THR C O 1 ATOM 3754 C CB . THR C 1 14 ? 43.396 -54.351 12.419 1.00 108.86 ? 13 THR C CB 1 ATOM 3755 O OG1 . THR C 1 14 ? 44.489 -53.438 12.246 1.00 107.04 ? 13 THR C OG1 1 ATOM 3756 C CG2 . THR C 1 14 ? 43.811 -55.758 11.991 1.00 113.14 ? 13 THR C CG2 1 ATOM 3757 N N . GLU C 1 15 ? 41.690 -51.522 10.981 1.00 99.15 ? 14 GLU C N 1 ATOM 3758 C CA . GLU C 1 15 ? 41.377 -50.112 11.240 1.00 94.76 ? 14 GLU C CA 1 ATOM 3759 C C . GLU C 1 15 ? 39.929 -49.986 11.694 1.00 93.28 ? 14 GLU C C 1 ATOM 3760 O O . GLU C 1 15 ? 39.038 -50.601 11.106 1.00 94.00 ? 14 GLU C O 1 ATOM 3761 C CB . GLU C 1 15 ? 41.614 -49.251 9.998 1.00 92.75 ? 14 GLU C CB 1 ATOM 3762 C CG . GLU C 1 15 ? 43.084 -49.040 9.666 1.00 93.52 ? 14 GLU C CG 1 ATOM 3763 C CD . GLU C 1 15 ? 43.346 -47.739 8.921 1.00 90.82 ? 14 GLU C CD 1 ATOM 3764 O OE1 . GLU C 1 15 ? 42.945 -46.660 9.420 1.00 88.76 ? 14 GLU C OE1 1 ATOM 3765 O OE2 . GLU C 1 15 ? 43.956 -47.793 7.833 1.00 91.34 ? 14 GLU C OE2 1 ATOM 3766 N N . GLN C 1 16 ? 39.698 -49.180 12.730 1.00 90.82 ? 15 GLN C N 1 ATOM 3767 C CA . GLN C 1 16 ? 38.402 -49.151 13.409 1.00 90.02 ? 15 GLN C CA 1 ATOM 3768 C C . GLN C 1 16 ? 37.691 -47.802 13.334 1.00 86.03 ? 15 GLN C C 1 ATOM 3769 O O . GLN C 1 16 ? 38.332 -46.755 13.259 1.00 83.53 ? 15 GLN C O 1 ATOM 3770 C CB . GLN C 1 16 ? 38.576 -49.570 14.868 1.00 91.75 ? 15 GLN C CB 1 ATOM 3771 C CG . GLN C 1 16 ? 38.905 -51.048 15.031 1.00 96.08 ? 15 GLN C CG 1 ATOM 3772 C CD . GLN C 1 16 ? 38.842 -51.505 16.474 1.00 98.26 ? 15 GLN C CD 1 ATOM 3773 O OE1 . GLN C 1 16 ? 38.837 -50.687 17.398 1.00 96.83 ? 15 GLN C OE1 1 ATOM 3774 N NE2 . GLN C 1 16 ? 38.793 -52.818 16.678 1.00 101.65 ? 15 GLN C NE2 1 ATOM 3775 N N . VAL C 1 17 ? 36.360 -47.847 13.361 1.00 85.54 ? 16 VAL C N 1 ATOM 3776 C CA . VAL C 1 17 ? 35.525 -46.644 13.345 1.00 82.48 ? 16 VAL C CA 1 ATOM 3777 C C . VAL C 1 17 ? 34.318 -46.796 14.264 1.00 82.75 ? 16 VAL C C 1 ATOM 3778 O O . VAL C 1 17 ? 34.023 -47.891 14.744 1.00 84.75 ? 16 VAL C O 1 ATOM 3779 C CB . VAL C 1 17 ? 35.016 -46.312 11.926 1.00 81.55 ? 16 VAL C CB 1 ATOM 3780 C CG1 . VAL C 1 17 ? 36.183 -46.113 10.973 1.00 81.16 ? 16 VAL C CG1 1 ATOM 3781 C CG2 . VAL C 1 17 ? 34.066 -47.391 11.416 1.00 83.65 ? 16 VAL C CG2 1 ATOM 3782 N N . ASP C 1 18 ? 33.628 -45.680 14.492 1.00 80.21 ? 17 ASP C N 1 ATOM 3783 C CA . ASP C 1 18 ? 32.443 -45.645 15.342 1.00 80.72 ? 17 ASP C CA 1 ATOM 3784 C C . ASP C 1 18 ? 31.198 -45.255 14.552 1.00 79.90 ? 17 ASP C C 1 ATOM 3785 O O . ASP C 1 18 ? 31.277 -44.631 13.495 1.00 77.63 ? 17 ASP C O 1 ATOM 3786 C CB . ASP C 1 18 ? 32.641 -44.653 16.493 1.00 79.37 ? 17 ASP C CB 1 ATOM 3787 C CG . ASP C 1 18 ? 33.737 -45.075 17.453 1.00 80.70 ? 17 ASP C CG 1 ATOM 3788 O OD1 . ASP C 1 18 ? 33.874 -46.290 17.722 1.00 83.98 ? 17 ASP C OD1 1 ATOM 3789 O OD2 . ASP C 1 18 ? 34.457 -44.185 17.951 1.00 79.06 ? 17 ASP C OD2 1 ATOM 3790 N N . THR C 1 19 ? 30.047 -45.642 15.087 1.00 82.12 ? 18 THR C N 1 ATOM 3791 C CA . THR C 1 19 ? 28.747 -45.287 14.529 1.00 82.36 ? 18 THR C CA 1 ATOM 3792 C C . THR C 1 19 ? 27.835 -44.928 15.694 1.00 83.47 ? 18 THR C C 1 ATOM 3793 O O . THR C 1 19 ? 28.264 -44.958 16.851 1.00 83.65 ? 18 THR C O 1 ATOM 3794 C CB . THR C 1 19 ? 28.122 -46.458 13.738 1.00 84.66 ? 18 THR C CB 1 ATOM 3795 O OG1 . THR C 1 19 ? 27.778 -47.518 14.637 1.00 87.49 ? 18 THR C OG1 1 ATOM 3796 C CG2 . THR C 1 19 ? 29.085 -46.978 12.683 1.00 84.69 ? 18 THR C CG2 1 ATOM 3797 N N . ILE C 1 20 ? 26.581 -44.596 15.395 1.00 84.51 ? 19 ILE C N 1 ATOM 3798 C CA . ILE C 1 20 ? 25.621 -44.267 16.444 1.00 86.01 ? 19 ILE C CA 1 ATOM 3799 C C . ILE C 1 20 ? 25.420 -45.448 17.394 1.00 89.19 ? 19 ILE C C 1 ATOM 3800 O O . ILE C 1 20 ? 25.603 -45.304 18.601 1.00 90.35 ? 19 ILE C O 1 ATOM 3801 C CB . ILE C 1 20 ? 24.272 -43.753 15.872 1.00 86.24 ? 19 ILE C CB 1 ATOM 3802 C CG1 . ILE C 1 20 ? 24.378 -42.247 15.582 1.00 83.66 ? 19 ILE C CG1 1 ATOM 3803 C CG2 . ILE C 1 20 ? 23.123 -44.024 16.838 1.00 88.40 ? 19 ILE C CG2 1 ATOM 3804 C CD1 . ILE C 1 20 ? 23.069 -41.573 15.221 1.00 83.91 ? 19 ILE C CD1 1 ATOM 3805 N N . MET C 1 21 ? 25.072 -46.614 16.861 1.00 91.70 ? 20 MET C N 1 ATOM 3806 C CA . MET C 1 21 ? 24.766 -47.758 17.726 1.00 95.18 ? 20 MET C CA 1 ATOM 3807 C C . MET C 1 21 ? 25.888 -48.792 17.839 1.00 95.59 ? 20 MET C C 1 ATOM 3808 O O . MET C 1 21 ? 25.816 -49.672 18.696 1.00 98.22 ? 20 MET C O 1 ATOM 3809 C CB . MET C 1 21 ? 23.439 -48.416 17.332 1.00 98.32 ? 20 MET C CB 1 ATOM 3810 C CG . MET C 1 21 ? 23.356 -48.961 15.920 1.00 99.51 ? 20 MET C CG 1 ATOM 3811 S SD . MET C 1 21 ? 21.706 -49.635 15.643 1.00 103.66 ? 20 MET C SD 1 ATOM 3812 C CE . MET C 1 21 ? 22.014 -50.747 14.267 1.00 104.93 ? 20 MET C CE 1 ATOM 3813 N N . GLU C 1 22 ? 26.922 -48.684 17.006 1.00 93.17 ? 21 GLU C N 1 ATOM 3814 C CA . GLU C 1 22 ? 28.117 -49.519 17.154 1.00 94.15 ? 21 GLU C CA 1 ATOM 3815 C C . GLU C 1 22 ? 29.387 -48.678 17.271 1.00 91.33 ? 21 GLU C C 1 ATOM 3816 O O . GLU C 1 22 ? 29.570 -47.712 16.531 1.00 88.28 ? 21 GLU C O 1 ATOM 3817 C CB . GLU C 1 22 ? 28.268 -50.484 15.976 1.00 95.59 ? 21 GLU C CB 1 ATOM 3818 C CG . GLU C 1 22 ? 27.219 -51.581 15.913 1.00 98.89 ? 21 GLU C CG 1 ATOM 3819 C CD . GLU C 1 22 ? 27.677 -52.787 15.107 1.00 101.45 ? 21 GLU C CD 1 ATOM 3820 O OE1 . GLU C 1 22 ? 28.648 -52.663 14.330 1.00 100.30 ? 21 GLU C OE1 1 ATOM 3821 O OE2 . GLU C 1 22 ? 27.065 -53.870 15.252 1.00 104.94 ? 21 GLU C OE2 1 ATOM 3822 N N . LYS C 1 23 ? 30.257 -49.058 18.205 1.00 92.29 ? 22 LYS C N 1 ATOM 3823 C CA . LYS C 1 23 ? 31.594 -48.474 18.322 1.00 90.52 ? 22 LYS C CA 1 ATOM 3824 C C . LYS C 1 23 ? 32.633 -49.592 18.250 1.00 92.85 ? 22 LYS C C 1 ATOM 3825 O O . LYS C 1 23 ? 32.301 -50.763 18.441 1.00 95.96 ? 22 LYS C O 1 ATOM 3826 C CB . LYS C 1 23 ? 31.735 -47.690 19.630 1.00 89.59 ? 22 LYS C CB 1 ATOM 3827 N N . ASN C 1 24 ? 33.884 -49.227 17.964 1.00 91.43 ? 23 ASN C N 1 ATOM 3828 C CA . ASN C 1 24 ? 34.973 -50.198 17.802 1.00 93.35 ? 23 ASN C CA 1 ATOM 3829 C C . ASN C 1 24 ? 34.658 -51.224 16.707 1.00 94.69 ? 23 ASN C C 1 ATOM 3830 O O . ASN C 1 24 ? 34.688 -52.434 16.945 1.00 97.98 ? 23 ASN C O 1 ATOM 3831 C CB . ASN C 1 24 ? 35.282 -50.908 19.134 1.00 96.47 ? 23 ASN C CB 1 ATOM 3832 C CG . ASN C 1 24 ? 35.563 -49.937 20.271 1.00 94.88 ? 23 ASN C CG 1 ATOM 3833 O OD1 . ASN C 1 24 ? 34.992 -50.049 21.357 1.00 96.18 ? 23 ASN C OD1 1 ATOM 3834 N ND2 . ASN C 1 24 ? 36.448 -48.980 20.025 1.00 92.22 ? 23 ASN C ND2 1 ATOM 3835 N N . VAL C 1 25 ? 34.353 -50.722 15.510 1.00 92.13 ? 24 VAL C N 1 ATOM 3836 C CA . VAL C 1 25 ? 33.973 -51.555 14.368 1.00 93.32 ? 24 VAL C CA 1 ATOM 3837 C C . VAL C 1 25 ? 35.077 -51.544 13.313 1.00 92.67 ? 24 VAL C C 1 ATOM 3838 O O . VAL C 1 25 ? 35.416 -50.486 12.781 1.00 89.83 ? 24 VAL C O 1 ATOM 3839 C CB . VAL C 1 25 ? 32.671 -51.044 13.717 1.00 91.76 ? 24 VAL C CB 1 ATOM 3840 C CG1 . VAL C 1 25 ? 32.276 -51.926 12.535 1.00 93.67 ? 24 VAL C CG1 1 ATOM 3841 C CG2 . VAL C 1 25 ? 31.550 -50.988 14.743 1.00 92.28 ? 24 VAL C CG2 1 ATOM 3842 N N . THR C 1 26 ? 35.612 -52.724 12.996 1.00 95.31 ? 25 THR C N 1 ATOM 3843 C CA . THR C 1 26 ? 36.724 -52.848 12.050 1.00 95.26 ? 25 THR C CA 1 ATOM 3844 C C . THR C 1 26 ? 36.240 -52.757 10.605 1.00 94.75 ? 25 THR C C 1 ATOM 3845 O O . THR C 1 26 ? 35.244 -53.384 10.244 1.00 96.20 ? 25 THR C O 1 ATOM 3846 C CB . THR C 1 26 ? 37.473 -54.184 12.227 1.00 98.65 ? 25 THR C CB 1 ATOM 3847 O OG1 . THR C 1 26 ? 37.876 -54.337 13.592 1.00 99.42 ? 25 THR C OG1 1 ATOM 3848 C CG2 . THR C 1 26 ? 38.702 -54.237 11.334 1.00 98.85 ? 25 THR C CG2 1 ATOM 3849 N N . VAL C 1 27 ? 36.959 -51.992 9.783 1.00 93.08 ? 26 VAL C N 1 ATOM 3850 C CA . VAL C 1 27 ? 36.612 -51.834 8.365 1.00 92.81 ? 26 VAL C CA 1 ATOM 3851 C C . VAL C 1 27 ? 37.793 -52.098 7.424 1.00 93.98 ? 26 VAL C C 1 ATOM 3852 O O . VAL C 1 27 ? 38.947 -52.132 7.853 1.00 94.66 ? 26 VAL C O 1 ATOM 3853 C CB . VAL C 1 27 ? 36.021 -50.438 8.060 1.00 89.33 ? 26 VAL C CB 1 ATOM 3854 C CG1 . VAL C 1 27 ? 34.698 -50.255 8.789 1.00 88.89 ? 26 VAL C CG1 1 ATOM 3855 C CG2 . VAL C 1 27 ? 37.002 -49.327 8.419 1.00 86.76 ? 26 VAL C CG2 1 ATOM 3856 N N . THR C 1 28 ? 37.485 -52.275 6.138 1.00 94.48 ? 27 THR C N 1 ATOM 3857 C CA . THR C 1 28 ? 38.499 -52.538 5.111 1.00 95.38 ? 27 THR C CA 1 ATOM 3858 C C . THR C 1 28 ? 39.221 -51.256 4.683 1.00 92.91 ? 27 THR C C 1 ATOM 3859 O O . THR C 1 28 ? 40.418 -51.285 4.384 1.00 93.60 ? 27 THR C O 1 ATOM 3860 C CB . THR C 1 28 ? 37.880 -53.188 3.862 1.00 96.80 ? 27 THR C CB 1 ATOM 3861 O OG1 . THR C 1 28 ? 36.992 -52.263 3.222 1.00 94.11 ? 27 THR C OG1 1 ATOM 3862 C CG2 . THR C 1 28 ? 37.118 -54.452 4.231 1.00 99.68 ? 27 THR C CG2 1 ATOM 3863 N N . HIS C 1 29 ? 38.481 -50.146 4.637 1.00 90.05 ? 28 HIS C N 1 ATOM 3864 C CA . HIS C 1 29 ? 39.047 -48.822 4.335 1.00 87.35 ? 28 HIS C CA 1 ATOM 3865 C C . HIS C 1 29 ? 38.389 -47.734 5.183 1.00 84.19 ? 28 HIS C C 1 ATOM 3866 O O . HIS C 1 29 ? 37.237 -47.866 5.600 1.00 83.80 ? 28 HIS C O 1 ATOM 3867 C CB . HIS C 1 29 ? 38.883 -48.477 2.850 1.00 87.26 ? 28 HIS C CB 1 ATOM 3868 C CG . HIS C 1 29 ? 39.690 -49.346 1.935 1.00 90.19 ? 28 HIS C CG 1 ATOM 3869 N ND1 . HIS C 1 29 ? 39.155 -50.434 1.278 1.00 92.62 ? 28 HIS C ND1 1 ATOM 3870 C CD2 . HIS C 1 29 ? 40.993 -49.291 1.571 1.00 90.95 ? 28 HIS C CD2 1 ATOM 3871 C CE1 . HIS C 1 29 ? 40.092 -51.008 0.546 1.00 94.81 ? 28 HIS C CE1 1 ATOM 3872 N NE2 . HIS C 1 29 ? 41.217 -50.336 0.707 1.00 93.66 ? 28 HIS C NE2 1 ATOM 3873 N N . ALA C 1 30 ? 39.128 -46.655 5.416 1.00 81.94 ? 29 ALA C N 1 ATOM 3874 C CA . ALA C 1 30 ? 38.648 -45.538 6.226 1.00 79.10 ? 29 ALA C CA 1 ATOM 3875 C C . ALA C 1 30 ? 39.562 -44.333 6.054 1.00 76.84 ? 29 ALA C C 1 ATOM 3876 O O . ALA C 1 30 ? 40.763 -44.489 5.831 1.00 78.00 ? 29 ALA C O 1 ATOM 3877 C CB . ALA C 1 30 ? 38.581 -45.940 7.693 1.00 79.60 ? 29 ALA C CB 1 ATOM 3878 N N . GLN C 1 31 ? 38.992 -43.135 6.166 1.00 74.08 ? 30 GLN C N 1 ATOM 3879 C CA . GLN C 1 31 ? 39.759 -41.900 6.028 1.00 71.61 ? 30 GLN C CA 1 ATOM 3880 C C . GLN C 1 31 ? 39.785 -41.129 7.347 1.00 69.24 ? 30 GLN C C 1 ATOM 3881 O O . GLN C 1 31 ? 38.744 -40.685 7.844 1.00 67.82 ? 30 GLN C O 1 ATOM 3882 C CB . GLN C 1 31 ? 39.171 -41.022 4.912 1.00 70.65 ? 30 GLN C CB 1 ATOM 3883 C CG . GLN C 1 31 ? 40.014 -39.806 4.532 1.00 69.00 ? 30 GLN C CG 1 ATOM 3884 C CD . GLN C 1 31 ? 41.450 -40.165 4.176 1.00 70.88 ? 30 GLN C CD 1 ATOM 3885 O OE1 . GLN C 1 31 ? 42.397 -39.543 4.661 1.00 70.64 ? 30 GLN C OE1 1 ATOM 3886 N NE2 . GLN C 1 31 ? 41.620 -41.181 3.338 1.00 73.53 ? 30 GLN C NE2 1 ATOM 3887 N N . ASP C 1 32 ? 40.977 -40.990 7.918 1.00 68.42 ? 31 ASP C N 1 ATOM 3888 C CA . ASP C 1 32 ? 41.187 -40.061 9.021 1.00 65.93 ? 31 ASP C CA 1 ATOM 3889 C C . ASP C 1 32 ? 40.988 -38.651 8.459 1.00 62.94 ? 31 ASP C C 1 ATOM 3890 O O . ASP C 1 32 ? 41.448 -38.349 7.354 1.00 62.51 ? 31 ASP C O 1 ATOM 3891 C CB . ASP C 1 32 ? 42.595 -40.223 9.606 1.00 66.55 ? 31 ASP C CB 1 ATOM 3892 C CG . ASP C 1 32 ? 42.751 -39.561 10.967 1.00 65.25 ? 31 ASP C CG 1 ATOM 3893 O OD1 . ASP C 1 32 ? 42.412 -38.368 11.111 1.00 62.86 ? 31 ASP C OD1 1 ATOM 3894 O OD2 . ASP C 1 32 ? 43.219 -40.242 11.901 1.00 66.92 ? 31 ASP C OD2 1 ATOM 3895 N N . ILE C 1 33 ? 40.276 -37.803 9.197 1.00 60.64 ? 32 ILE C N 1 ATOM 3896 C CA . ILE C 1 33 ? 40.067 -36.421 8.761 1.00 58.13 ? 32 ILE C CA 1 ATOM 3897 C C . ILE C 1 33 ? 40.458 -35.421 9.840 1.00 55.82 ? 32 ILE C C 1 ATOM 3898 O O . ILE C 1 33 ? 40.067 -34.255 9.774 1.00 54.54 ? 32 ILE C O 1 ATOM 3899 C CB . ILE C 1 33 ? 38.609 -36.191 8.307 1.00 57.83 ? 32 ILE C CB 1 ATOM 3900 C CG1 . ILE C 1 33 ? 37.627 -36.357 9.472 1.00 57.75 ? 32 ILE C CG1 1 ATOM 3901 C CG2 . ILE C 1 33 ? 38.250 -37.152 7.179 1.00 59.89 ? 32 ILE C CG2 1 ATOM 3902 C CD1 . ILE C 1 33 ? 36.248 -35.826 9.161 1.00 57.05 ? 32 ILE C CD1 1 ATOM 3903 N N . LEU C 1 34 ? 41.247 -35.872 10.814 1.00 56.15 ? 33 LEU C N 1 ATOM 3904 C CA . LEU C 1 34 ? 41.607 -35.051 11.972 1.00 54.64 ? 33 LEU C CA 1 ATOM 3905 C C . LEU C 1 34 ? 43.118 -34.979 12.126 1.00 54.69 ? 33 LEU C C 1 ATOM 3906 O O . LEU C 1 34 ? 43.775 -35.995 12.323 1.00 56.77 ? 33 LEU C O 1 ATOM 3907 C CB . LEU C 1 34 ? 40.981 -35.623 13.253 1.00 55.38 ? 33 LEU C CB 1 ATOM 3908 C CG . LEU C 1 34 ? 41.175 -34.838 14.559 1.00 54.29 ? 33 LEU C CG 1 ATOM 3909 C CD1 . LEU C 1 34 ? 40.571 -33.439 14.475 1.00 51.73 ? 33 LEU C CD1 1 ATOM 3910 C CD2 . LEU C 1 34 ? 40.592 -35.602 15.739 1.00 55.54 ? 33 LEU C CD2 1 ATOM 3911 N N . GLU C 1 35 ? 43.661 -33.769 12.023 1.00 52.76 ? 34 GLU C N 1 ATOM 3912 C CA . GLU C 1 35 ? 45.077 -33.536 12.252 1.00 52.88 ? 34 GLU C CA 1 ATOM 3913 C C . GLU C 1 35 ? 45.330 -33.418 13.752 1.00 53.24 ? 34 GLU C C 1 ATOM 3914 O O . GLU C 1 35 ? 44.633 -32.667 14.449 1.00 51.72 ? 34 GLU C O 1 ATOM 3915 C CB . GLU C 1 35 ? 45.516 -32.253 11.543 1.00 51.07 ? 34 GLU C CB 1 ATOM 3916 C CG . GLU C 1 35 ? 47.012 -31.984 11.602 1.00 51.34 ? 34 GLU C CG 1 ATOM 3917 C CD . GLU C 1 35 ? 47.815 -33.159 11.091 1.00 53.82 ? 34 GLU C CD 1 ATOM 3918 O OE1 . GLU C 1 35 ? 47.627 -33.545 9.917 1.00 54.26 ? 34 GLU C OE1 1 ATOM 3919 O OE2 . GLU C 1 35 ? 48.611 -33.707 11.873 1.00 55.24 ? 34 GLU C OE2 1 ATOM 3920 N N . LYS C 1 36 ? 46.323 -34.155 14.246 1.00 55.33 ? 35 LYS C N 1 ATOM 3921 C CA . LYS C 1 36 ? 46.675 -34.139 15.672 1.00 56.15 ? 35 LYS C CA 1 ATOM 3922 C C . LYS C 1 36 ? 48.122 -33.745 15.951 1.00 56.60 ? 35 LYS C C 1 ATOM 3923 O O . LYS C 1 36 ? 48.560 -33.793 17.105 1.00 57.66 ? 35 LYS C O 1 ATOM 3924 C CB . LYS C 1 36 ? 46.415 -35.514 16.298 1.00 58.83 ? 35 LYS C CB 1 ATOM 3925 C CG . LYS C 1 36 ? 44.953 -35.804 16.583 1.00 58.80 ? 35 LYS C CG 1 ATOM 3926 C CD . LYS C 1 36 ? 44.275 -36.481 15.410 1.00 59.58 ? 35 LYS C CD 1 ATOM 3927 C CE . LYS C 1 36 ? 44.589 -37.968 15.342 1.00 62.43 ? 35 LYS C CE 1 ATOM 3928 N NZ . LYS C 1 36 ? 43.901 -38.580 14.172 1.00 63.19 ? 35 LYS C NZ 1 ATOM 3929 N N . THR C 1 37 ? 48.862 -33.352 14.917 1.00 56.24 ? 36 THR C N 1 ATOM 3930 C CA . THR C 1 37 ? 50.283 -33.068 15.078 1.00 57.09 ? 36 THR C CA 1 ATOM 3931 C C . THR C 1 37 ? 50.653 -31.644 14.663 1.00 54.83 ? 36 THR C C 1 ATOM 3932 O O . THR C 1 37 ? 50.051 -31.059 13.762 1.00 52.93 ? 36 THR C O 1 ATOM 3933 C CB . THR C 1 37 ? 51.145 -34.077 14.298 1.00 59.65 ? 36 THR C CB 1 ATOM 3934 O OG1 . THR C 1 37 ? 50.877 -33.959 12.899 1.00 59.15 ? 36 THR C OG1 1 ATOM 3935 C CG2 . THR C 1 37 ? 50.841 -35.498 14.752 1.00 62.13 ? 36 THR C CG2 1 ATOM 3936 N N . HIS C 1 38 ? 51.645 -31.097 15.356 1.00 54.95 ? 37 HIS C N 1 ATOM 3937 C CA . HIS C 1 38 ? 52.211 -29.793 15.033 1.00 53.09 ? 37 HIS C CA 1 ATOM 3938 C C . HIS C 1 38 ? 53.726 -29.880 15.155 1.00 54.52 ? 37 HIS C C 1 ATOM 3939 O O . HIS C 1 38 ? 54.250 -30.795 15.800 1.00 56.92 ? 37 HIS C O 1 ATOM 3940 C CB . HIS C 1 38 ? 51.649 -28.700 15.955 1.00 51.04 ? 37 HIS C CB 1 ATOM 3941 C CG . HIS C 1 38 ? 51.746 -29.023 17.415 1.00 52.27 ? 37 HIS C CG 1 ATOM 3942 N ND1 . HIS C 1 38 ? 52.720 -28.494 18.233 1.00 52.92 ? 37 HIS C ND1 1 ATOM 3943 C CD2 . HIS C 1 38 ? 50.982 -29.812 18.207 1.00 53.33 ? 37 HIS C CD2 1 ATOM 3944 C CE1 . HIS C 1 38 ? 52.559 -28.946 19.463 1.00 53.96 ? 37 HIS C CE1 1 ATOM 3945 N NE2 . HIS C 1 38 ? 51.510 -29.748 19.474 1.00 54.32 ? 37 HIS C NE2 1 ATOM 3946 N N . ASN C 1 39 ? 54.424 -28.937 14.524 1.00 53.03 ? 38 ASN C N 1 ATOM 3947 C CA . ASN C 1 39 ? 55.883 -28.948 14.513 1.00 54.32 ? 38 ASN C CA 1 ATOM 3948 C C . ASN C 1 39 ? 56.469 -28.377 15.803 1.00 54.43 ? 38 ASN C C 1 ATOM 3949 O O . ASN C 1 39 ? 57.676 -28.426 16.018 1.00 56.06 ? 38 ASN C O 1 ATOM 3950 C CB . ASN C 1 39 ? 56.438 -28.230 13.272 1.00 53.37 ? 38 ASN C CB 1 ATOM 3951 C CG . ASN C 1 39 ? 56.371 -26.713 13.373 1.00 50.68 ? 38 ASN C CG 1 ATOM 3952 O OD1 . ASN C 1 39 ? 56.043 -26.148 14.416 1.00 48.85 ? 38 ASN C OD1 1 ATOM 3953 N ND2 . ASN C 1 39 ? 56.699 -26.047 12.276 1.00 50.07 ? 38 ASN C ND2 1 ATOM 3954 N N . GLY C 1 40 ? 55.610 -27.822 16.649 1.00 52.76 ? 39 GLY C N 1 ATOM 3955 C CA . GLY C 1 40 ? 56.021 -27.362 17.972 1.00 53.24 ? 39 GLY C CA 1 ATOM 3956 C C . GLY C 1 40 ? 56.834 -26.083 17.983 1.00 52.57 ? 39 GLY C C 1 ATOM 3957 O O . GLY C 1 40 ? 57.548 -25.824 18.950 1.00 54.17 ? 39 GLY C O 1 ATOM 3958 N N . LYS C 1 41 ? 56.737 -25.279 16.924 1.00 50.95 ? 40 LYS C N 1 ATOM 3959 C CA . LYS C 1 41 ? 57.480 -24.023 16.866 1.00 50.19 ? 40 LYS C CA 1 ATOM 3960 C C . LYS C 1 41 ? 56.770 -22.906 16.113 1.00 47.45 ? 40 LYS C C 1 ATOM 3961 O O . LYS C 1 41 ? 55.814 -23.144 15.374 1.00 46.13 ? 40 LYS C O 1 ATOM 3962 C CB . LYS C 1 41 ? 58.894 -24.237 16.297 1.00 53.18 ? 40 LYS C CB 1 ATOM 3963 C CG . LYS C 1 41 ? 59.082 -25.367 15.290 1.00 55.54 ? 40 LYS C CG 1 ATOM 3964 C CD . LYS C 1 41 ? 60.572 -25.696 15.153 1.00 58.38 ? 40 LYS C CD 1 ATOM 3965 C CE . LYS C 1 41 ? 60.941 -26.357 13.832 1.00 60.26 ? 40 LYS C CE 1 ATOM 3966 N NZ . LYS C 1 41 ? 61.075 -27.840 13.917 1.00 62.98 ? 40 LYS C NZ 1 ATOM 3967 N N . LEU C 1 42 ? 57.256 -21.684 16.336 1.00 46.28 ? 41 LEU C N 1 ATOM 3968 C CA . LEU C 1 42 ? 56.775 -20.486 15.653 1.00 44.23 ? 41 LEU C CA 1 ATOM 3969 C C . LEU C 1 42 ? 57.539 -20.252 14.360 1.00 45.13 ? 41 LEU C C 1 ATOM 3970 O O . LEU C 1 42 ? 58.759 -20.080 14.370 1.00 46.26 ? 41 LEU C O 1 ATOM 3971 C CB . LEU C 1 42 ? 56.936 -19.253 16.545 1.00 42.93 ? 41 LEU C CB 1 ATOM 3972 C CG . LEU C 1 42 ? 56.303 -19.333 17.929 1.00 42.38 ? 41 LEU C CG 1 ATOM 3973 C CD1 . LEU C 1 42 ? 56.354 -17.970 18.596 1.00 41.47 ? 41 LEU C CD1 1 ATOM 3974 C CD2 . LEU C 1 42 ? 54.866 -19.817 17.866 1.00 41.23 ? 41 LEU C CD2 1 ATOM 3975 N N . CYS C 1 43 ? 56.798 -20.221 13.260 1.00 45.13 ? 42 CYS C N 1 ATOM 3976 C CA . CYS C 1 43 ? 57.349 -20.116 11.915 1.00 46.79 ? 42 CYS C CA 1 ATOM 3977 C C . CYS C 1 43 ? 56.950 -18.815 11.212 1.00 44.93 ? 42 CYS C C 1 ATOM 3978 O O . CYS C 1 43 ? 56.069 -18.081 11.680 1.00 42.37 ? 42 CYS C O 1 ATOM 3979 C CB . CYS C 1 43 ? 56.826 -21.285 11.095 1.00 48.66 ? 42 CYS C CB 1 ATOM 3980 S SG . CYS C 1 43 ? 57.312 -22.886 11.758 1.00 52.26 ? 42 CYS C SG 1 ATOM 3981 N N . ASP C 1 44 ? 57.614 -18.547 10.090 1.00 45.96 ? 43 ASP C N 1 ATOM 3982 C CA . ASP C 1 44 ? 57.148 -17.563 9.118 1.00 45.51 ? 43 ASP C CA 1 ATOM 3983 C C . ASP C 1 44 ? 55.793 -18.020 8.592 1.00 44.26 ? 43 ASP C C 1 ATOM 3984 O O . ASP C 1 44 ? 55.546 -19.214 8.455 1.00 44.81 ? 43 ASP C O 1 ATOM 3985 C CB . ASP C 1 44 ? 58.123 -17.437 7.937 1.00 47.84 ? 43 ASP C CB 1 ATOM 3986 C CG . ASP C 1 44 ? 59.467 -16.849 8.335 1.00 49.45 ? 43 ASP C CG 1 ATOM 3987 O OD1 . ASP C 1 44 ? 59.666 -16.551 9.528 1.00 49.32 ? 43 ASP C OD1 1 ATOM 3988 O OD2 . ASP C 1 44 ? 60.337 -16.691 7.450 1.00 51.69 ? 43 ASP C OD2 1 ATOM 3989 N N . LEU C 1 45 ? 54.920 -17.069 8.298 1.00 42.70 ? 44 LEU C N 1 ATOM 3990 C CA . LEU C 1 45 ? 53.615 -17.393 7.746 1.00 42.61 ? 44 LEU C CA 1 ATOM 3991 C C . LEU C 1 45 ? 53.617 -17.049 6.264 1.00 43.87 ? 44 LEU C C 1 ATOM 3992 O O . LEU C 1 45 ? 53.655 -15.878 5.893 1.00 42.77 ? 44 LEU C O 1 ATOM 3993 C CB . LEU C 1 45 ? 52.522 -16.629 8.493 1.00 40.56 ? 44 LEU C CB 1 ATOM 3994 C CG . LEU C 1 45 ? 51.077 -16.977 8.142 1.00 40.13 ? 44 LEU C CG 1 ATOM 3995 C CD1 . LEU C 1 45 ? 50.758 -18.426 8.485 1.00 41.01 ? 44 LEU C CD1 1 ATOM 3996 C CD2 . LEU C 1 45 ? 50.147 -16.029 8.869 1.00 38.23 ? 44 LEU C CD2 1 ATOM 3997 N N . ASP C 1 46 ? 53.607 -18.082 5.422 1.00 46.60 ? 45 ASP C N 1 ATOM 3998 C CA . ASP C 1 46 ? 53.655 -17.910 3.969 1.00 48.88 ? 45 ASP C CA 1 ATOM 3999 C C . ASP C 1 46 ? 54.784 -16.948 3.562 1.00 49.18 ? 45 ASP C C 1 ATOM 4000 O O . ASP C 1 46 ? 54.570 -15.993 2.814 1.00 48.61 ? 45 ASP C O 1 ATOM 4001 C CB . ASP C 1 46 ? 52.292 -17.419 3.455 1.00 49.43 ? 45 ASP C CB 1 ATOM 4002 C CG . ASP C 1 46 ? 52.161 -17.520 1.946 1.00 53.31 ? 45 ASP C CG 1 ATOM 4003 O OD1 . ASP C 1 46 ? 52.508 -18.580 1.371 1.00 55.69 ? 45 ASP C OD1 1 ATOM 4004 O OD2 . ASP C 1 46 ? 51.721 -16.525 1.328 1.00 55.75 ? 45 ASP C OD2 1 ATOM 4005 N N . GLY C 1 47 ? 55.981 -17.201 4.090 1.00 49.48 ? 46 GLY C N 1 ATOM 4006 C CA . GLY C 1 47 ? 57.167 -16.438 3.733 1.00 50.57 ? 46 GLY C CA 1 ATOM 4007 C C . GLY C 1 47 ? 57.374 -15.119 4.465 1.00 48.96 ? 46 GLY C C 1 ATOM 4008 O O . GLY C 1 47 ? 58.359 -14.428 4.211 1.00 50.32 ? 46 GLY C O 1 ATOM 4009 N N . VAL C 1 48 ? 56.468 -14.761 5.372 1.00 46.74 ? 47 VAL C N 1 ATOM 4010 C CA . VAL C 1 48 ? 56.578 -13.502 6.124 1.00 45.15 ? 47 VAL C CA 1 ATOM 4011 C C . VAL C 1 48 ? 56.787 -13.768 7.623 1.00 43.98 ? 47 VAL C C 1 ATOM 4012 O O . VAL C 1 48 ? 55.954 -14.395 8.274 1.00 42.61 ? 47 VAL C O 1 ATOM 4013 C CB . VAL C 1 48 ? 55.343 -12.614 5.885 1.00 43.57 ? 47 VAL C CB 1 ATOM 4014 C CG1 . VAL C 1 48 ? 55.405 -11.357 6.737 1.00 42.36 ? 47 VAL C CG1 1 ATOM 4015 C CG2 . VAL C 1 48 ? 55.259 -12.248 4.411 1.00 45.02 ? 47 VAL C CG2 1 ATOM 4016 N N . LYS C 1 49 ? 57.908 -13.279 8.152 1.00 44.63 ? 48 LYS C N 1 ATOM 4017 C CA . LYS C 1 49 ? 58.325 -13.557 9.524 1.00 44.73 ? 48 LYS C CA 1 ATOM 4018 C C . LYS C 1 49 ? 57.499 -12.780 10.535 1.00 42.17 ? 48 LYS C C 1 ATOM 4019 O O . LYS C 1 49 ? 57.239 -11.598 10.330 1.00 42.62 ? 48 LYS C O 1 ATOM 4020 C CB . LYS C 1 49 ? 59.802 -13.193 9.717 1.00 47.17 ? 48 LYS C CB 1 ATOM 4021 C CG . LYS C 1 49 ? 60.353 -13.660 11.058 1.00 48.57 ? 48 LYS C CG 1 ATOM 4022 C CD . LYS C 1 49 ? 61.750 -13.159 11.385 1.00 50.35 ? 48 LYS C CD 1 ATOM 4023 C CE . LYS C 1 49 ? 61.985 -13.267 12.888 1.00 50.54 ? 48 LYS C CE 1 ATOM 4024 N NZ . LYS C 1 49 ? 63.389 -12.957 13.281 1.00 53.52 ? 48 LYS C NZ 1 ATOM 4025 N N . PRO C 1 50 ? 57.101 -13.428 11.645 1.00 40.56 ? 49 PRO C N 1 ATOM 4026 C CA . PRO C 1 50 ? 56.351 -12.710 12.677 1.00 38.00 ? 49 PRO C CA 1 ATOM 4027 C C . PRO C 1 50 ? 57.204 -11.746 13.494 1.00 37.47 ? 49 PRO C C 1 ATOM 4028 O O . PRO C 1 50 ? 58.430 -11.902 13.567 1.00 38.02 ? 49 PRO C O 1 ATOM 4029 C CB . PRO C 1 50 ? 55.845 -13.832 13.582 1.00 37.83 ? 49 PRO C CB 1 ATOM 4030 C CG . PRO C 1 50 ? 56.880 -14.891 13.446 1.00 39.95 ? 49 PRO C CG 1 ATOM 4031 C CD . PRO C 1 50 ? 57.294 -14.844 12.005 1.00 41.23 ? 49 PRO C CD 1 ATOM 4032 N N . LEU C 1 51 ? 56.543 -10.759 14.102 1.00 35.60 ? 50 LEU C N 1 ATOM 4033 C CA . LEU C 1 51 ? 57.186 -9.889 15.081 1.00 35.51 ? 50 LEU C CA 1 ATOM 4034 C C . LEU C 1 51 ? 57.183 -10.576 16.447 1.00 35.73 ? 50 LEU C C 1 ATOM 4035 O O . LEU C 1 51 ? 56.131 -10.664 17.086 1.00 34.05 ? 50 LEU C O 1 ATOM 4036 C CB . LEU C 1 51 ? 56.454 -8.549 15.188 1.00 33.74 ? 50 LEU C CB 1 ATOM 4037 C CG . LEU C 1 51 ? 56.889 -7.680 16.367 1.00 32.98 ? 50 LEU C CG 1 ATOM 4038 C CD1 . LEU C 1 51 ? 58.403 -7.546 16.385 1.00 34.58 ? 50 LEU C CD1 1 ATOM 4039 C CD2 . LEU C 1 51 ? 56.232 -6.309 16.276 1.00 32.38 ? 50 LEU C CD2 1 ATOM 4040 N N . ILE C 1 52 ? 58.357 -11.023 16.888 1.00 37.64 ? 51 ILE C N 1 ATOM 4041 C CA . ILE C 1 52 ? 58.528 -11.742 18.165 1.00 38.86 ? 51 ILE C CA 1 ATOM 4042 C C . ILE C 1 52 ? 59.062 -10.789 19.249 1.00 39.05 ? 51 ILE C C 1 ATOM 4043 O O . ILE C 1 52 ? 60.268 -10.502 19.302 1.00 40.45 ? 51 ILE C O 1 ATOM 4044 C CB . ILE C 1 52 ? 59.527 -12.919 18.031 1.00 41.33 ? 51 ILE C CB 1 ATOM 4045 C CG1 . ILE C 1 52 ? 59.238 -13.770 16.789 1.00 42.31 ? 51 ILE C CG1 1 ATOM 4046 C CG2 . ILE C 1 52 ? 59.508 -13.790 19.281 1.00 42.05 ? 51 ILE C CG2 1 ATOM 4047 C CD1 . ILE C 1 52 ? 57.968 -14.583 16.874 1.00 42.03 ? 51 ILE C CD1 1 ATOM 4048 N N . LEU C 1 53 ? 58.181 -10.330 20.138 1.00 37.68 ? 52 LEU C N 1 ATOM 4049 C CA . LEU C 1 53 ? 58.551 -9.305 21.123 1.00 37.34 ? 52 LEU C CA 1 ATOM 4050 C C . LEU C 1 53 ? 59.433 -9.829 22.248 1.00 38.83 ? 52 LEU C C 1 ATOM 4051 O O . LEU C 1 53 ? 59.881 -9.058 23.103 1.00 38.33 ? 52 LEU C O 1 ATOM 4052 C CB . LEU C 1 53 ? 57.303 -8.636 21.698 1.00 36.14 ? 52 LEU C CB 1 ATOM 4053 C CG . LEU C 1 53 ? 56.412 -7.959 20.649 1.00 34.98 ? 52 LEU C CG 1 ATOM 4054 C CD1 . LEU C 1 53 ? 55.178 -7.345 21.289 1.00 33.97 ? 52 LEU C CD1 1 ATOM 4055 C CD2 . LEU C 1 53 ? 57.204 -6.903 19.891 1.00 35.43 ? 52 LEU C CD2 1 ATOM 4056 N N . ARG C 1 54 ? 59.679 -11.136 22.250 1.00 40.30 ? 53 ARG C N 1 ATOM 4057 C CA . ARG C 1 54 ? 60.617 -11.747 23.178 1.00 43.30 ? 53 ARG C CA 1 ATOM 4058 C C . ARG C 1 54 ? 60.166 -11.527 24.628 1.00 42.40 ? 53 ARG C C 1 ATOM 4059 O O . ARG C 1 54 ? 59.242 -12.197 25.084 1.00 41.81 ? 53 ARG C O 1 ATOM 4060 C CB . ARG C 1 54 ? 62.056 -11.251 22.904 1.00 45.67 ? 53 ARG C CB 1 ATOM 4061 C CG . ARG C 1 54 ? 63.132 -12.085 23.582 1.00 49.54 ? 53 ARG C CG 1 ATOM 4062 C CD . ARG C 1 54 ? 64.540 -11.702 23.134 1.00 52.19 ? 53 ARG C CD 1 ATOM 4063 N NE . ARG C 1 54 ? 64.775 -11.987 21.717 1.00 53.41 ? 53 ARG C NE 1 ATOM 4064 C CZ . ARG C 1 54 ? 65.974 -12.031 21.132 1.00 55.55 ? 53 ARG C CZ 1 ATOM 4065 N NH1 . ARG C 1 54 ? 67.083 -11.824 21.831 1.00 57.83 ? 53 ARG C NH1 1 ATOM 4066 N NH2 . ARG C 1 54 ? 66.068 -12.298 19.830 1.00 55.61 ? 53 ARG C NH2 1 ATOM 4067 N N . ASP C 1 55 ? 60.800 -10.600 25.345 1.00 42.75 ? 54 ASP C N 1 ATOM 4068 C CA . ASP C 1 55 ? 60.404 -10.278 26.716 1.00 42.11 ? 54 ASP C CA 1 ATOM 4069 C C . ASP C 1 55 ? 59.739 -8.895 26.802 1.00 39.60 ? 54 ASP C C 1 ATOM 4070 O O . ASP C 1 55 ? 59.587 -8.338 27.887 1.00 38.66 ? 54 ASP C O 1 ATOM 4071 C CB . ASP C 1 55 ? 61.623 -10.406 27.643 1.00 44.47 ? 54 ASP C CB 1 ATOM 4072 C CG . ASP C 1 55 ? 62.146 -11.839 27.709 1.00 47.25 ? 54 ASP C CG 1 ATOM 4073 O OD1 . ASP C 1 55 ? 61.345 -12.749 27.997 1.00 47.51 ? 54 ASP C OD1 1 ATOM 4074 O OD2 . ASP C 1 55 ? 63.350 -12.074 27.461 1.00 49.70 ? 54 ASP C OD2 1 ATOM 4075 N N . CYS C 1 56 ? 59.307 -8.362 25.659 1.00 38.22 ? 55 CYS C N 1 ATOM 4076 C CA . CYS C 1 56 ? 58.651 -7.054 25.623 1.00 36.89 ? 55 CYS C CA 1 ATOM 4077 C C . CYS C 1 56 ? 57.134 -7.187 25.446 1.00 33.85 ? 55 CYS C C 1 ATOM 4078 O O . CYS C 1 56 ? 56.649 -8.119 24.823 1.00 32.31 ? 55 CYS C O 1 ATOM 4079 C CB . CYS C 1 56 ? 59.247 -6.178 24.517 1.00 37.96 ? 55 CYS C CB 1 ATOM 4080 S SG . CYS C 1 56 ? 60.966 -5.689 24.810 1.00 44.31 ? 55 CYS C SG 1 ATOM 4081 N N . SER C 1 57 ? 56.395 -6.249 26.028 1.00 32.23 ? 56 SER C N 1 ATOM 4082 C CA . SER C 1 57 ? 54.958 -6.150 25.813 1.00 30.59 ? 56 SER C CA 1 ATOM 4083 C C . SER C 1 57 ? 54.740 -5.236 24.614 1.00 28.83 ? 56 SER C C 1 ATOM 4084 O O . SER C 1 57 ? 55.691 -4.617 24.139 1.00 29.69 ? 56 SER C O 1 ATOM 4085 C CB . SER C 1 57 ? 54.271 -5.582 27.046 1.00 30.18 ? 56 SER C CB 1 ATOM 4086 O OG . SER C 1 57 ? 54.658 -4.233 27.262 1.00 30.12 ? 56 SER C OG 1 ATOM 4087 N N . VAL C 1 58 ? 53.508 -5.154 24.121 1.00 26.61 ? 57 VAL C N 1 ATOM 4088 C CA . VAL C 1 58 ? 53.175 -4.182 23.081 1.00 25.68 ? 57 VAL C CA 1 ATOM 4089 C C . VAL C 1 58 ? 53.463 -2.751 23.541 1.00 25.23 ? 57 VAL C C 1 ATOM 4090 O O . VAL C 1 58 ? 53.994 -1.936 22.779 1.00 25.01 ? 57 VAL C O 1 ATOM 4091 C CB . VAL C 1 58 ? 51.696 -4.282 22.652 1.00 25.10 ? 57 VAL C CB 1 ATOM 4092 C CG1 . VAL C 1 58 ? 51.306 -3.112 21.775 1.00 24.00 ? 57 VAL C CG1 1 ATOM 4093 C CG2 . VAL C 1 58 ? 51.441 -5.586 21.905 1.00 25.71 ? 57 VAL C CG2 1 ATOM 4094 N N . ALA C 1 59 ? 53.101 -2.447 24.783 1.00 25.12 ? 58 ALA C N 1 ATOM 4095 C CA . ALA C 1 59 ? 53.320 -1.112 25.333 1.00 25.05 ? 58 ALA C CA 1 ATOM 4096 C C . ALA C 1 59 ? 54.826 -0.799 25.404 1.00 25.49 ? 58 ALA C C 1 ATOM 4097 O O . ALA C 1 59 ? 55.266 0.303 25.036 1.00 24.42 ? 58 ALA C O 1 ATOM 4098 C CB . ALA C 1 59 ? 52.691 -1.003 26.712 1.00 25.49 ? 58 ALA C CB 1 ATOM 4099 N N . GLY C 1 60 ? 55.597 -1.782 25.864 1.00 25.89 ? 59 GLY C N 1 ATOM 4100 C CA . GLY C 1 60 ? 57.041 -1.637 25.973 1.00 27.55 ? 59 GLY C CA 1 ATOM 4101 C C . GLY C 1 60 ? 57.652 -1.330 24.621 1.00 27.50 ? 59 GLY C C 1 ATOM 4102 O O . GLY C 1 60 ? 58.567 -0.522 24.506 1.00 28.42 ? 59 GLY C O 1 ATOM 4103 N N . TRP C 1 61 ? 57.122 -1.981 23.597 1.00 27.20 ? 60 TRP C N 1 ATOM 4104 C CA . TRP C 1 61 ? 57.571 -1.787 22.230 1.00 27.10 ? 60 TRP C CA 1 ATOM 4105 C C . TRP C 1 61 ? 57.188 -0.396 21.696 1.00 26.25 ? 60 TRP C C 1 ATOM 4106 O O . TRP C 1 61 ? 58.045 0.322 21.193 1.00 26.90 ? 60 TRP C O 1 ATOM 4107 C CB . TRP C 1 61 ? 56.996 -2.898 21.359 1.00 26.61 ? 60 TRP C CB 1 ATOM 4108 C CG . TRP C 1 61 ? 57.008 -2.640 19.878 1.00 26.44 ? 60 TRP C CG 1 ATOM 4109 C CD1 . TRP C 1 61 ? 58.020 -2.109 19.142 1.00 27.34 ? 60 TRP C CD1 1 ATOM 4110 C CD2 . TRP C 1 61 ? 55.969 -2.962 18.952 1.00 25.54 ? 60 TRP C CD2 1 ATOM 4111 N NE1 . TRP C 1 61 ? 57.668 -2.059 17.815 1.00 27.06 ? 60 TRP C NE1 1 ATOM 4112 C CE2 . TRP C 1 61 ? 56.414 -2.585 17.673 1.00 25.90 ? 60 TRP C CE2 1 ATOM 4113 C CE3 . TRP C 1 61 ? 54.701 -3.540 19.079 1.00 24.84 ? 60 TRP C CE3 1 ATOM 4114 C CZ2 . TRP C 1 61 ? 55.642 -2.762 16.537 1.00 25.45 ? 60 TRP C CZ2 1 ATOM 4115 C CZ3 . TRP C 1 61 ? 53.927 -3.699 17.944 1.00 24.03 ? 60 TRP C CZ3 1 ATOM 4116 C CH2 . TRP C 1 61 ? 54.403 -3.320 16.694 1.00 24.71 ? 60 TRP C CH2 1 ATOM 4117 N N . LEU C 1 62 ? 55.919 -0.015 21.813 1.00 24.77 ? 61 LEU C N 1 ATOM 4118 C CA . LEU C 1 62 ? 55.451 1.208 21.175 1.00 24.27 ? 61 LEU C CA 1 ATOM 4119 C C . LEU C 1 62 ? 55.950 2.462 21.877 1.00 24.42 ? 61 LEU C C 1 ATOM 4120 O O . LEU C 1 62 ? 56.292 3.431 21.226 1.00 25.09 ? 61 LEU C O 1 ATOM 4121 C CB . LEU C 1 62 ? 53.922 1.230 21.058 1.00 23.52 ? 61 LEU C CB 1 ATOM 4122 C CG . LEU C 1 62 ? 53.270 0.062 20.294 1.00 23.56 ? 61 LEU C CG 1 ATOM 4123 C CD1 . LEU C 1 62 ? 51.741 0.105 20.382 1.00 23.09 ? 61 LEU C CD1 1 ATOM 4124 C CD2 . LEU C 1 62 ? 53.723 0.022 18.849 1.00 24.11 ? 61 LEU C CD2 1 ATOM 4125 N N . LEU C 1 63 ? 56.005 2.442 23.200 1.00 24.99 ? 62 LEU C N 1 ATOM 4126 C CA . LEU C 1 63 ? 56.534 3.574 23.962 1.00 25.56 ? 62 LEU C CA 1 ATOM 4127 C C . LEU C 1 63 ? 58.049 3.695 23.882 1.00 27.03 ? 62 LEU C C 1 ATOM 4128 O O . LEU C 1 63 ? 58.593 4.802 23.957 1.00 27.39 ? 62 LEU C O 1 ATOM 4129 C CB . LEU C 1 63 ? 56.108 3.476 25.419 1.00 25.77 ? 62 LEU C CB 1 ATOM 4130 C CG . LEU C 1 63 ? 54.636 3.805 25.653 1.00 25.06 ? 62 LEU C CG 1 ATOM 4131 C CD1 . LEU C 1 63 ? 54.123 3.183 26.935 1.00 25.50 ? 62 LEU C CD1 1 ATOM 4132 C CD2 . LEU C 1 63 ? 54.449 5.318 25.674 1.00 25.31 ? 62 LEU C CD2 1 ATOM 4133 N N . GLY C 1 64 ? 58.733 2.559 23.739 1.00 27.54 ? 63 GLY C N 1 ATOM 4134 C CA . GLY C 1 64 ? 60.167 2.564 23.558 1.00 29.12 ? 63 GLY C CA 1 ATOM 4135 C C . GLY C 1 64 ? 60.948 2.323 24.837 1.00 30.52 ? 63 GLY C C 1 ATOM 4136 O O . GLY C 1 64 ? 61.938 2.987 25.096 1.00 30.22 ? 63 GLY C O 1 ATOM 4137 N N . ASN C 1 65 ? 60.473 1.371 25.631 1.00 31.55 ? 64 ASN C N 1 ATOM 4138 C CA . ASN C 1 65 ? 61.186 0.867 26.782 1.00 33.88 ? 64 ASN C CA 1 ATOM 4139 C C . ASN C 1 65 ? 62.630 0.573 26.337 1.00 36.70 ? 64 ASN C C 1 ATOM 4140 O O . ASN C 1 65 ? 62.819 -0.100 25.317 1.00 36.88 ? 64 ASN C O 1 ATOM 4141 C CB . ASN C 1 65 ? 60.463 -0.390 27.278 1.00 33.89 ? 64 ASN C CB 1 ATOM 4142 C CG . ASN C 1 65 ? 61.055 -0.965 28.552 1.00 35.48 ? 64 ASN C CG 1 ATOM 4143 O OD1 . ASN C 1 65 ? 62.266 -0.938 28.761 1.00 36.99 ? 64 ASN C OD1 1 ATOM 4144 N ND2 . ASN C 1 65 ? 60.195 -1.529 29.394 1.00 35.40 ? 64 ASN C ND2 1 ATOM 4145 N N . PRO C 1 66 ? 63.643 1.116 27.062 1.00 38.83 ? 65 PRO C N 1 ATOM 4146 C CA . PRO C 1 66 ? 65.064 0.941 26.721 1.00 41.76 ? 65 PRO C CA 1 ATOM 4147 C C . PRO C 1 66 ? 65.524 -0.510 26.570 1.00 44.96 ? 65 PRO C C 1 ATOM 4148 O O . PRO C 1 66 ? 66.466 -0.770 25.816 1.00 46.70 ? 65 PRO C O 1 ATOM 4149 C CB . PRO C 1 66 ? 65.806 1.587 27.900 1.00 42.75 ? 65 PRO C CB 1 ATOM 4150 C CG . PRO C 1 66 ? 64.843 2.530 28.519 1.00 40.95 ? 65 PRO C CG 1 ATOM 4151 C CD . PRO C 1 66 ? 63.455 2.063 28.179 1.00 38.84 ? 65 PRO C CD 1 ATOM 4152 N N . MET C 1 67 ? 64.875 -1.438 27.279 1.00 47.02 ? 66 MET C N 1 ATOM 4153 C CA . MET C 1 67 ? 65.176 -2.873 27.152 1.00 49.59 ? 66 MET C CA 1 ATOM 4154 C C . MET C 1 67 ? 64.628 -3.468 25.854 1.00 48.38 ? 66 MET C C 1 ATOM 4155 O O . MET C 1 67 ? 64.900 -4.630 25.543 1.00 49.36 ? 66 MET C O 1 ATOM 4156 C CB . MET C 1 67 ? 64.558 -3.664 28.306 1.00 51.95 ? 66 MET C CB 1 ATOM 4157 C CG . MET C 1 67 ? 64.874 -3.154 29.697 1.00 54.31 ? 66 MET C CG 1 ATOM 4158 S SD . MET C 1 67 ? 66.628 -2.861 29.920 1.00 61.30 ? 66 MET C SD 1 ATOM 4159 C CE . MET C 1 67 ? 67.318 -4.462 29.493 1.00 63.21 ? 66 MET C CE 1 ATOM 4160 N N . CYS C 1 68 ? 63.836 -2.686 25.122 1.00 45.65 ? 67 CYS C N 1 ATOM 4161 C CA . CYS C 1 68 ? 63.152 -3.160 23.927 1.00 44.26 ? 67 CYS C CA 1 ATOM 4162 C C . CYS C 1 68 ? 63.735 -2.527 22.654 1.00 43.66 ? 67 CYS C C 1 ATOM 4163 O O . CYS C 1 68 ? 63.048 -2.437 21.628 1.00 41.88 ? 67 CYS C O 1 ATOM 4164 C CB . CYS C 1 68 ? 61.652 -2.850 24.047 1.00 42.11 ? 67 CYS C CB 1 ATOM 4165 S SG . CYS C 1 68 ? 60.820 -3.712 25.401 1.00 42.71 ? 67 CYS C SG 1 ATOM 4166 N N . ASP C 1 69 ? 64.999 -2.106 22.716 1.00 44.41 ? 68 ASP C N 1 ATOM 4167 C CA . ASP C 1 69 ? 65.645 -1.418 21.585 1.00 44.89 ? 68 ASP C CA 1 ATOM 4168 C C . ASP C 1 69 ? 65.698 -2.273 20.322 1.00 44.52 ? 68 ASP C C 1 ATOM 4169 O O . ASP C 1 69 ? 65.650 -1.748 19.210 1.00 44.67 ? 68 ASP C O 1 ATOM 4170 C CB . ASP C 1 69 ? 67.051 -0.923 21.961 1.00 47.72 ? 68 ASP C CB 1 ATOM 4171 C CG . ASP C 1 69 ? 67.032 0.454 22.638 1.00 48.28 ? 68 ASP C CG 1 ATOM 4172 O OD1 . ASP C 1 69 ? 65.953 0.929 23.071 1.00 46.52 ? 68 ASP C OD1 1 ATOM 4173 O OD2 . ASP C 1 69 ? 68.113 1.070 22.739 1.00 51.39 ? 68 ASP C OD2 1 ATOM 4174 N N . GLU C 1 70 ? 65.767 -3.587 20.499 1.00 44.62 ? 69 GLU C N 1 ATOM 4175 C CA . GLU C 1 70 ? 65.621 -4.544 19.401 1.00 44.97 ? 69 GLU C CA 1 ATOM 4176 C C . GLU C 1 70 ? 64.484 -4.201 18.430 1.00 42.54 ? 69 GLU C C 1 ATOM 4177 O O . GLU C 1 70 ? 64.577 -4.520 17.253 1.00 44.50 ? 69 GLU C O 1 ATOM 4178 C CB . GLU C 1 70 ? 65.378 -5.938 19.986 1.00 46.20 ? 69 GLU C CB 1 ATOM 4179 C CG . GLU C 1 70 ? 65.305 -7.074 18.987 1.00 47.96 ? 69 GLU C CG 1 ATOM 4180 C CD . GLU C 1 70 ? 65.122 -8.427 19.659 1.00 50.09 ? 69 GLU C CD 1 ATOM 4181 O OE1 . GLU C 1 70 ? 65.054 -8.478 20.910 1.00 51.47 ? 69 GLU C OE1 1 ATOM 4182 O OE2 . GLU C 1 70 ? 65.042 -9.447 18.937 1.00 50.97 ? 69 GLU C OE2 1 ATOM 4183 N N . PHE C 1 71 ? 63.422 -3.554 18.918 1.00 39.55 ? 70 PHE C N 1 ATOM 4184 C CA . PHE C 1 71 ? 62.219 -3.299 18.124 1.00 37.07 ? 70 PHE C CA 1 ATOM 4185 C C . PHE C 1 71 ? 61.954 -1.828 17.830 1.00 36.25 ? 70 PHE C C 1 ATOM 4186 O O . PHE C 1 71 ? 60.807 -1.434 17.694 1.00 34.21 ? 70 PHE C O 1 ATOM 4187 C CB . PHE C 1 71 ? 61.000 -3.849 18.867 1.00 35.15 ? 70 PHE C CB 1 ATOM 4188 C CG . PHE C 1 71 ? 61.195 -5.229 19.406 1.00 35.57 ? 70 PHE C CG 1 ATOM 4189 C CD1 . PHE C 1 71 ? 61.285 -6.312 18.549 1.00 36.70 ? 70 PHE C CD1 1 ATOM 4190 C CD2 . PHE C 1 71 ? 61.295 -5.448 20.760 1.00 35.50 ? 70 PHE C CD2 1 ATOM 4191 C CE1 . PHE C 1 71 ? 61.469 -7.597 19.041 1.00 37.84 ? 70 PHE C CE1 1 ATOM 4192 C CE2 . PHE C 1 71 ? 61.481 -6.728 21.259 1.00 36.84 ? 70 PHE C CE2 1 ATOM 4193 C CZ . PHE C 1 71 ? 61.568 -7.806 20.400 1.00 37.57 ? 70 PHE C CZ 1 ATOM 4194 N N . LEU C 1 72 ? 62.989 -1.005 17.736 1.00 38.02 ? 71 LEU C N 1 ATOM 4195 C CA . LEU C 1 72 ? 62.767 0.432 17.507 1.00 37.51 ? 71 LEU C CA 1 ATOM 4196 C C . LEU C 1 72 ? 62.181 0.741 16.127 1.00 37.28 ? 71 LEU C C 1 ATOM 4197 O O . LEU C 1 72 ? 61.420 1.700 15.980 1.00 35.92 ? 71 LEU C O 1 ATOM 4198 C CB . LEU C 1 72 ? 64.063 1.219 17.701 1.00 39.07 ? 71 LEU C CB 1 ATOM 4199 C CG . LEU C 1 72 ? 64.482 1.392 19.158 1.00 39.26 ? 71 LEU C CG 1 ATOM 4200 C CD1 . LEU C 1 72 ? 65.933 1.848 19.240 1.00 40.70 ? 71 LEU C CD1 1 ATOM 4201 C CD2 . LEU C 1 72 ? 63.547 2.363 19.880 1.00 37.84 ? 71 LEU C CD2 1 ATOM 4202 N N . ASN C 1 73 ? 62.562 -0.062 15.131 1.00 38.40 ? 72 ASN C N 1 ATOM 4203 C CA . ASN C 1 73 ? 62.122 0.091 13.740 1.00 38.67 ? 72 ASN C CA 1 ATOM 4204 C C . ASN C 1 73 ? 62.041 -1.281 13.084 1.00 39.14 ? 72 ASN C C 1 ATOM 4205 O O . ASN C 1 73 ? 62.967 -1.693 12.383 1.00 40.03 ? 72 ASN C O 1 ATOM 4206 C CB . ASN C 1 73 ? 63.107 0.963 12.940 1.00 40.69 ? 72 ASN C CB 1 ATOM 4207 C CG . ASN C 1 73 ? 63.139 2.410 13.416 1.00 40.40 ? 72 ASN C CG 1 ATOM 4208 O OD1 . ASN C 1 73 ? 62.147 3.116 13.328 1.00 39.40 ? 72 ASN C OD1 1 ATOM 4209 N ND2 . ASN C 1 73 ? 64.286 2.853 13.916 1.00 41.95 ? 72 ASN C ND2 1 ATOM 4210 N N . VAL C 1 74 ? 60.934 -1.986 13.311 1.00 37.48 ? 73 VAL C N 1 ATOM 4211 C CA . VAL C 1 74 ? 60.789 -3.364 12.813 1.00 37.50 ? 73 VAL C CA 1 ATOM 4212 C C . VAL C 1 74 ? 60.260 -3.435 11.375 1.00 37.03 ? 73 VAL C C 1 ATOM 4213 O O . VAL C 1 74 ? 59.626 -2.508 10.891 1.00 36.30 ? 73 VAL C O 1 ATOM 4214 C CB . VAL C 1 74 ? 59.885 -4.226 13.733 1.00 36.36 ? 73 VAL C CB 1 ATOM 4215 C CG1 . VAL C 1 74 ? 60.476 -4.292 15.134 1.00 36.31 ? 73 VAL C CG1 1 ATOM 4216 C CG2 . VAL C 1 74 ? 58.446 -3.713 13.763 1.00 34.43 ? 73 VAL C CG2 1 ATOM 4217 N N . PRO C 1 75 ? 60.539 -4.543 10.683 1.00 37.42 ? 74 PRO C N 1 ATOM 4218 C CA . PRO C 1 75 ? 59.986 -4.722 9.348 1.00 37.70 ? 74 PRO C CA 1 ATOM 4219 C C . PRO C 1 75 ? 58.561 -5.279 9.382 1.00 35.82 ? 74 PRO C C 1 ATOM 4220 O O . PRO C 1 75 ? 58.057 -5.627 10.451 1.00 34.35 ? 74 PRO C O 1 ATOM 4221 C CB . PRO C 1 75 ? 60.949 -5.726 8.709 1.00 39.93 ? 74 PRO C CB 1 ATOM 4222 C CG . PRO C 1 75 ? 61.475 -6.523 9.859 1.00 40.00 ? 74 PRO C CG 1 ATOM 4223 C CD . PRO C 1 75 ? 61.492 -5.610 11.047 1.00 38.60 ? 74 PRO C CD 1 ATOM 4224 N N . GLU C 1 76 ? 57.931 -5.342 8.210 1.00 36.15 ? 75 GLU C N 1 ATOM 4225 C CA . GLU C 1 76 ? 56.604 -5.931 8.035 1.00 34.77 ? 75 GLU C CA 1 ATOM 4226 C C . GLU C 1 76 ? 56.518 -7.291 8.693 1.00 34.31 ? 75 GLU C C 1 ATOM 4227 O O . GLU C 1 76 ? 57.429 -8.103 8.556 1.00 35.19 ? 75 GLU C O 1 ATOM 4228 C CB . GLU C 1 76 ? 56.285 -6.112 6.546 1.00 36.27 ? 75 GLU C CB 1 ATOM 4229 C CG . GLU C 1 76 ? 54.831 -6.489 6.308 1.00 35.81 ? 75 GLU C CG 1 ATOM 4230 C CD . GLU C 1 76 ? 54.513 -6.912 4.896 1.00 37.36 ? 75 GLU C CD 1 ATOM 4231 O OE1 . GLU C 1 76 ? 55.139 -6.408 3.934 1.00 39.45 ? 75 GLU C OE1 1 ATOM 4232 O OE2 . GLU C 1 76 ? 53.604 -7.755 4.764 1.00 37.46 ? 75 GLU C OE2 1 ATOM 4233 N N . TRP C 1 77 ? 55.414 -7.540 9.389 1.00 33.17 ? 76 TRP C N 1 ATOM 4234 C CA . TRP C 1 77 ? 55.208 -8.819 10.058 1.00 33.71 ? 76 TRP C CA 1 ATOM 4235 C C . TRP C 1 77 ? 53.919 -9.521 9.607 1.00 33.61 ? 76 TRP C C 1 ATOM 4236 O O . TRP C 1 77 ? 53.013 -8.895 9.064 1.00 31.83 ? 76 TRP C O 1 ATOM 4237 C CB . TRP C 1 77 ? 55.218 -8.633 11.573 1.00 32.66 ? 76 TRP C CB 1 ATOM 4238 C CG . TRP C 1 77 ? 54.097 -7.770 12.056 1.00 31.43 ? 76 TRP C CG 1 ATOM 4239 C CD1 . TRP C 1 77 ? 52.819 -8.161 12.300 1.00 30.14 ? 76 TRP C CD1 1 ATOM 4240 C CD2 . TRP C 1 77 ? 54.153 -6.367 12.342 1.00 30.79 ? 76 TRP C CD2 1 ATOM 4241 N NE1 . TRP C 1 77 ? 52.072 -7.088 12.694 1.00 29.52 ? 76 TRP C NE1 1 ATOM 4242 C CE2 . TRP C 1 77 ? 52.870 -5.977 12.746 1.00 29.33 ? 76 TRP C CE2 1 ATOM 4243 C CE3 . TRP C 1 77 ? 55.161 -5.399 12.278 1.00 31.62 ? 76 TRP C CE3 1 ATOM 4244 C CZ2 . TRP C 1 77 ? 52.563 -4.666 13.092 1.00 28.80 ? 76 TRP C CZ2 1 ATOM 4245 C CZ3 . TRP C 1 77 ? 54.853 -4.087 12.633 1.00 30.61 ? 76 TRP C CZ3 1 ATOM 4246 C CH2 . TRP C 1 77 ? 53.571 -3.739 13.035 1.00 29.28 ? 76 TRP C CH2 1 ATOM 4247 N N . SER C 1 78 ? 53.884 -10.838 9.833 1.00 34.87 ? 77 SER C N 1 ATOM 4248 C CA . SER C 1 78 ? 52.718 -11.688 9.554 1.00 34.77 ? 77 SER C CA 1 ATOM 4249 C C . SER C 1 78 ? 51.845 -11.836 10.785 1.00 33.57 ? 77 SER C C 1 ATOM 4250 O O . SER C 1 78 ? 50.622 -11.971 10.681 1.00 34.52 ? 77 SER C O 1 ATOM 4251 C CB . SER C 1 78 ? 53.171 -13.079 9.135 1.00 36.37 ? 77 SER C CB 1 ATOM 4252 O OG . SER C 1 78 ? 54.166 -13.560 10.023 1.00 37.04 ? 77 SER C OG 1 ATOM 4253 N N . TYR C 1 79 ? 52.480 -11.870 11.952 1.00 32.37 ? 78 TYR C N 1 ATOM 4254 C CA . TYR C 1 79 ? 51.759 -11.849 13.209 1.00 30.65 ? 78 TYR C CA 1 ATOM 4255 C C . TYR C 1 79 ? 52.692 -11.440 14.333 1.00 30.69 ? 78 TYR C C 1 ATOM 4256 O O . TYR C 1 79 ? 53.909 -11.389 14.164 1.00 32.12 ? 78 TYR C O 1 ATOM 4257 C CB . TYR C 1 79 ? 51.093 -13.192 13.509 1.00 30.76 ? 78 TYR C CB 1 ATOM 4258 C CG . TYR C 1 79 ? 52.029 -14.373 13.590 1.00 31.81 ? 78 TYR C CG 1 ATOM 4259 C CD1 . TYR C 1 79 ? 52.498 -14.999 12.438 1.00 33.26 ? 78 TYR C CD1 1 ATOM 4260 C CD2 . TYR C 1 79 ? 52.422 -14.881 14.815 1.00 31.76 ? 78 TYR C CD2 1 ATOM 4261 C CE1 . TYR C 1 79 ? 53.356 -16.091 12.510 1.00 34.65 ? 78 TYR C CE1 1 ATOM 4262 C CE2 . TYR C 1 79 ? 53.266 -15.965 14.900 1.00 33.53 ? 78 TYR C CE2 1 ATOM 4263 C CZ . TYR C 1 79 ? 53.736 -16.567 13.750 1.00 34.93 ? 78 TYR C CZ 1 ATOM 4264 O OH . TYR C 1 79 ? 54.591 -17.642 13.859 1.00 37.26 ? 78 TYR C OH 1 ATOM 4265 N N . ILE C 1 80 ? 52.098 -11.122 15.469 1.00 29.34 ? 79 ILE C N 1 ATOM 4266 C CA . ILE C 1 80 ? 52.819 -10.638 16.615 1.00 29.41 ? 79 ILE C CA 1 ATOM 4267 C C . ILE C 1 80 ? 52.761 -11.710 17.694 1.00 30.14 ? 79 ILE C C 1 ATOM 4268 O O . ILE C 1 80 ? 51.720 -12.342 17.889 1.00 29.09 ? 79 ILE C O 1 ATOM 4269 C CB . ILE C 1 80 ? 52.225 -9.305 17.110 1.00 27.88 ? 79 ILE C CB 1 ATOM 4270 C CG1 . ILE C 1 80 ? 52.314 -8.262 15.989 1.00 27.99 ? 79 ILE C CG1 1 ATOM 4271 C CG2 . ILE C 1 80 ? 52.959 -8.825 18.344 1.00 27.60 ? 79 ILE C CG2 1 ATOM 4272 C CD1 . ILE C 1 80 ? 51.852 -6.876 16.379 1.00 27.35 ? 79 ILE C CD1 1 ATOM 4273 N N . VAL C 1 81 ? 53.902 -11.926 18.353 1.00 31.54 ? 80 VAL C N 1 ATOM 4274 C CA . VAL C 1 81 ? 54.021 -12.896 19.424 1.00 33.08 ? 80 VAL C CA 1 ATOM 4275 C C . VAL C 1 81 ? 54.474 -12.195 20.690 1.00 33.77 ? 80 VAL C C 1 ATOM 4276 O O . VAL C 1 81 ? 55.499 -11.524 20.701 1.00 34.70 ? 80 VAL C O 1 ATOM 4277 C CB . VAL C 1 81 ? 55.023 -14.025 19.091 1.00 34.93 ? 80 VAL C CB 1 ATOM 4278 C CG1 . VAL C 1 81 ? 55.194 -14.945 20.288 1.00 36.20 ? 80 VAL C CG1 1 ATOM 4279 C CG2 . VAL C 1 81 ? 54.551 -14.826 17.887 1.00 35.09 ? 80 VAL C CG2 1 ATOM 4280 N N . GLU C 1 82 ? 53.702 -12.399 21.750 1.00 34.57 ? 81 GLU C N 1 ATOM 4281 C CA . GLU C 1 82 ? 53.893 -11.769 23.036 1.00 36.05 ? 81 GLU C CA 1 ATOM 4282 C C . GLU C 1 82 ? 53.800 -12.875 24.081 1.00 38.05 ? 81 GLU C C 1 ATOM 4283 O O . GLU C 1 82 ? 53.003 -13.798 23.927 1.00 37.82 ? 81 GLU C O 1 ATOM 4284 C CB . GLU C 1 82 ? 52.784 -10.749 23.247 1.00 35.81 ? 81 GLU C CB 1 ATOM 4285 C CG . GLU C 1 82 ? 52.987 -9.772 24.382 1.00 37.49 ? 81 GLU C CG 1 ATOM 4286 C CD . GLU C 1 82 ? 51.812 -8.806 24.524 1.00 37.94 ? 81 GLU C CD 1 ATOM 4287 O OE1 . GLU C 1 82 ? 50.644 -9.262 24.485 1.00 37.74 ? 81 GLU C OE1 1 ATOM 4288 O OE2 . GLU C 1 82 ? 52.058 -7.583 24.648 1.00 39.06 ? 81 GLU C OE2 1 ATOM 4289 N N . LYS C 1 83 ? 54.633 -12.800 25.122 1.00 39.78 ? 82 LYS C N 1 ATOM 4290 C CA . LYS C 1 83 ? 54.529 -13.727 26.241 1.00 41.40 ? 82 LYS C CA 1 ATOM 4291 C C . LYS C 1 83 ? 53.337 -13.377 27.124 1.00 40.59 ? 82 LYS C C 1 ATOM 4292 O O . LYS C 1 83 ? 52.876 -12.238 27.147 1.00 38.35 ? 82 LYS C O 1 ATOM 4293 C CB . LYS C 1 83 ? 55.802 -13.724 27.079 1.00 43.45 ? 82 LYS C CB 1 ATOM 4294 C CG . LYS C 1 83 ? 56.988 -14.372 26.402 1.00 45.27 ? 82 LYS C CG 1 ATOM 4295 C CD . LYS C 1 83 ? 58.216 -14.317 27.289 1.00 47.56 ? 82 LYS C CD 1 ATOM 4296 C CE . LYS C 1 83 ? 59.347 -15.168 26.730 1.00 50.01 ? 82 LYS C CE 1 ATOM 4297 N NZ . LYS C 1 83 ? 59.656 -14.831 25.314 1.00 49.16 ? 82 LYS C NZ 1 ATOM 4298 N N . ILE C 1 84 ? 52.860 -14.375 27.859 1.00 42.49 ? 83 ILE C N 1 ATOM 4299 C CA . ILE C 1 84 ? 51.754 -14.209 28.795 1.00 43.05 ? 83 ILE C CA 1 ATOM 4300 C C . ILE C 1 84 ? 52.011 -13.054 29.761 1.00 42.84 ? 83 ILE C C 1 ATOM 4301 O O . ILE C 1 84 ? 51.154 -12.196 29.918 1.00 41.22 ? 83 ILE C O 1 ATOM 4302 C CB . ILE C 1 84 ? 51.489 -15.523 29.573 1.00 46.34 ? 83 ILE C CB 1 ATOM 4303 C CG1 . ILE C 1 84 ? 50.657 -16.494 28.715 1.00 46.78 ? 83 ILE C CG1 1 ATOM 4304 C CG2 . ILE C 1 84 ? 50.780 -15.255 30.893 1.00 47.36 ? 83 ILE C CG2 1 ATOM 4305 C CD1 . ILE C 1 84 ? 51.465 -17.345 27.744 1.00 47.35 ? 83 ILE C CD1 1 ATOM 4306 N N . ASN C 1 85 ? 53.188 -13.037 30.392 1.00 44.91 ? 84 ASN C N 1 ATOM 4307 C CA . ASN C 1 85 ? 53.584 -11.956 31.297 1.00 45.97 ? 84 ASN C CA 1 ATOM 4308 C C . ASN C 1 85 ? 54.958 -11.372 30.949 1.00 45.73 ? 84 ASN C C 1 ATOM 4309 O O . ASN C 1 85 ? 55.976 -11.770 31.517 1.00 47.54 ? 84 ASN C O 1 ATOM 4310 C CB . ASN C 1 85 ? 53.574 -12.444 32.751 1.00 50.08 ? 84 ASN C CB 1 ATOM 4311 C CG . ASN C 1 85 ? 53.751 -11.311 33.757 1.00 51.77 ? 84 ASN C CG 1 ATOM 4312 O OD1 . ASN C 1 85 ? 53.521 -10.131 33.452 1.00 51.91 ? 84 ASN C OD1 1 ATOM 4313 N ND2 . ASN C 1 85 ? 54.153 -11.667 34.969 1.00 54.37 ? 84 ASN C ND2 1 ATOM 4314 N N . PRO C 1 86 ? 54.991 -10.409 30.019 1.00 43.21 ? 85 PRO C N 1 ATOM 4315 C CA . PRO C 1 86 ? 56.276 -9.868 29.574 1.00 42.77 ? 85 PRO C CA 1 ATOM 4316 C C . PRO C 1 86 ? 57.005 -9.057 30.639 1.00 43.32 ? 85 PRO C C 1 ATOM 4317 O O . PRO C 1 86 ? 56.428 -8.137 31.218 1.00 43.41 ? 85 PRO C O 1 ATOM 4318 C CB . PRO C 1 86 ? 55.899 -8.971 28.394 1.00 40.65 ? 85 PRO C CB 1 ATOM 4319 C CG . PRO C 1 86 ? 54.503 -9.358 28.014 1.00 39.59 ? 85 PRO C CG 1 ATOM 4320 C CD . PRO C 1 86 ? 53.860 -9.841 29.268 1.00 40.75 ? 85 PRO C CD 1 ATOM 4321 N N . ALA C 1 87 ? 58.277 -9.383 30.862 1.00 43.59 ? 86 ALA C N 1 ATOM 4322 C CA . ALA C 1 87 ? 59.092 -8.692 31.853 1.00 44.48 ? 86 ALA C CA 1 ATOM 4323 C C . ALA C 1 87 ? 59.345 -7.208 31.554 1.00 42.23 ? 86 ALA C C 1 ATOM 4324 O O . ALA C 1 87 ? 59.568 -6.425 32.475 1.00 43.45 ? 86 ALA C O 1 ATOM 4325 C CB . ALA C 1 87 ? 60.421 -9.413 32.020 1.00 47.64 ? 86 ALA C CB 1 ATOM 4326 N N . ASN C 1 88 ? 59.345 -6.825 30.285 1.00 39.09 ? 87 ASN C N 1 ATOM 4327 C CA . ASN C 1 88 ? 59.631 -5.450 29.904 1.00 37.27 ? 87 ASN C CA 1 ATOM 4328 C C . ASN C 1 88 ? 58.359 -4.810 29.381 1.00 35.12 ? 87 ASN C C 1 ATOM 4329 O O . ASN C 1 88 ? 58.040 -4.893 28.200 1.00 32.72 ? 87 ASN C O 1 ATOM 4330 C CB . ASN C 1 88 ? 60.742 -5.391 28.853 1.00 37.34 ? 87 ASN C CB 1 ATOM 4331 C CG . ASN C 1 88 ? 62.072 -5.906 29.375 1.00 39.54 ? 87 ASN C CG 1 ATOM 4332 O OD1 . ASN C 1 88 ? 62.802 -6.604 28.664 1.00 40.87 ? 87 ASN C OD1 1 ATOM 4333 N ND2 . ASN C 1 88 ? 62.400 -5.557 30.615 1.00 40.07 ? 87 ASN C ND2 1 ATOM 4334 N N . ASP C 1 89 ? 57.621 -4.204 30.303 1.00 35.10 ? 88 ASP C N 1 ATOM 4335 C CA . ASP C 1 89 ? 56.362 -3.586 30.014 1.00 33.09 ? 88 ASP C CA 1 ATOM 4336 C C . ASP C 1 89 ? 56.547 -2.078 30.234 1.00 32.73 ? 88 ASP C C 1 ATOM 4337 O O . ASP C 1 89 ? 57.247 -1.446 29.457 1.00 33.28 ? 88 ASP C O 1 ATOM 4338 C CB . ASP C 1 89 ? 55.284 -4.219 30.900 1.00 33.61 ? 88 ASP C CB 1 ATOM 4339 C CG . ASP C 1 89 ? 53.917 -3.606 30.687 1.00 31.94 ? 88 ASP C CG 1 ATOM 4340 O OD1 . ASP C 1 89 ? 53.446 -3.578 29.527 1.00 30.77 ? 88 ASP C OD1 1 ATOM 4341 O OD2 . ASP C 1 89 ? 53.341 -3.121 31.686 1.00 33.06 ? 88 ASP C OD2 1 ATOM 4342 N N . LEU C 1 90 ? 55.952 -1.491 31.271 1.00 32.81 ? 89 LEU C N 1 ATOM 4343 C CA . LEU C 1 90 ? 56.144 -0.073 31.539 1.00 32.62 ? 89 LEU C CA 1 ATOM 4344 C C . LEU C 1 90 ? 57.195 0.001 32.618 1.00 34.17 ? 89 LEU C C 1 ATOM 4345 O O . LEU C 1 90 ? 56.925 -0.362 33.752 1.00 36.04 ? 89 LEU C O 1 ATOM 4346 C CB . LEU C 1 90 ? 54.855 0.589 32.013 1.00 32.07 ? 89 LEU C CB 1 ATOM 4347 C CG . LEU C 1 90 ? 53.645 0.458 31.095 1.00 30.68 ? 89 LEU C CG 1 ATOM 4348 C CD1 . LEU C 1 90 ? 52.380 0.956 31.790 1.00 31.17 ? 89 LEU C CD1 1 ATOM 4349 C CD2 . LEU C 1 90 ? 53.871 1.221 29.806 1.00 29.85 ? 89 LEU C CD2 1 ATOM 4350 N N . CYS C 1 91 ? 58.396 0.446 32.257 1.00 33.99 ? 90 CYS C N 1 ATOM 4351 C CA . CYS C 1 91 ? 59.523 0.473 33.193 1.00 35.48 ? 90 CYS C CA 1 ATOM 4352 C C . CYS C 1 91 ? 59.250 1.470 34.315 1.00 34.30 ? 90 CYS C C 1 ATOM 4353 O O . CYS C 1 91 ? 59.411 1.149 35.492 1.00 35.24 ? 90 CYS C O 1 ATOM 4354 C CB . CYS C 1 91 ? 60.861 0.763 32.462 1.00 36.75 ? 90 CYS C CB 1 ATOM 4355 S SG . CYS C 1 91 ? 60.953 2.230 31.381 1.00 36.56 ? 90 CYS C SG 1 ATOM 4356 N N . TYR C 1 92 ? 58.842 2.678 33.944 1.00 32.17 ? 91 TYR C N 1 ATOM 4357 C CA . TYR C 1 92 ? 58.291 3.616 34.909 1.00 31.94 ? 91 TYR C CA 1 ATOM 4358 C C . TYR C 1 92 ? 56.815 3.234 35.063 1.00 31.10 ? 91 TYR C C 1 ATOM 4359 O O . TYR C 1 92 ? 56.101 3.152 34.068 1.00 29.27 ? 91 TYR C O 1 ATOM 4360 C CB . TYR C 1 92 ? 58.444 5.066 34.447 1.00 30.59 ? 91 TYR C CB 1 ATOM 4361 C CG . TYR C 1 92 ? 58.240 6.060 35.564 1.00 31.07 ? 91 TYR C CG 1 ATOM 4362 C CD1 . TYR C 1 92 ? 56.957 6.375 36.019 1.00 30.43 ? 91 TYR C CD1 1 ATOM 4363 C CD2 . TYR C 1 92 ? 59.322 6.651 36.207 1.00 32.42 ? 91 TYR C CD2 1 ATOM 4364 C CE1 . TYR C 1 92 ? 56.762 7.275 37.046 1.00 31.06 ? 91 TYR C CE1 1 ATOM 4365 C CE2 . TYR C 1 92 ? 59.136 7.559 37.235 1.00 32.95 ? 91 TYR C CE2 1 ATOM 4366 C CZ . TYR C 1 92 ? 57.851 7.862 37.651 1.00 32.32 ? 91 TYR C CZ 1 ATOM 4367 O OH . TYR C 1 92 ? 57.651 8.759 38.661 1.00 33.22 ? 91 TYR C OH 1 ATOM 4368 N N . PRO C 1 93 ? 56.364 2.979 36.304 1.00 32.50 ? 92 PRO C N 1 ATOM 4369 C CA . PRO C 1 93 ? 55.049 2.357 36.476 1.00 32.72 ? 92 PRO C CA 1 ATOM 4370 C C . PRO C 1 93 ? 53.880 3.297 36.148 1.00 31.93 ? 92 PRO C C 1 ATOM 4371 O O . PRO C 1 93 ? 54.016 4.522 36.223 1.00 31.81 ? 92 PRO C O 1 ATOM 4372 C CB . PRO C 1 93 ? 55.041 1.972 37.957 1.00 34.61 ? 92 PRO C CB 1 ATOM 4373 C CG . PRO C 1 93 ? 55.916 2.987 38.603 1.00 35.34 ? 92 PRO C CG 1 ATOM 4374 C CD . PRO C 1 93 ? 56.985 3.316 37.598 1.00 34.40 ? 92 PRO C CD 1 ATOM 4375 N N . GLY C 1 94 ? 52.753 2.718 35.760 1.00 32.04 ? 93 GLY C N 1 ATOM 4376 C CA . GLY C 1 94 ? 51.557 3.504 35.473 1.00 32.51 ? 93 GLY C CA 1 ATOM 4377 C C . GLY C 1 94 ? 50.571 2.736 34.626 1.00 32.66 ? 93 GLY C C 1 ATOM 4378 O O . GLY C 1 94 ? 50.335 1.545 34.853 1.00 33.63 ? 93 GLY C O 1 ATOM 4379 N N . ASN C 1 95 ? 49.985 3.398 33.644 1.00 32.87 ? 94 ASN C N 1 ATOM 4380 C CA . ASN C 1 95 ? 49.050 2.697 32.780 1.00 34.48 ? 94 ASN C CA 1 ATOM 4381 C C . ASN C 1 95 ? 48.963 3.274 31.393 1.00 32.27 ? 94 ASN C C 1 ATOM 4382 O O . ASN C 1 95 ? 49.325 4.430 31.147 1.00 31.43 ? 94 ASN C O 1 ATOM 4383 C CB . ASN C 1 95 ? 47.652 2.643 33.410 1.00 37.14 ? 94 ASN C CB 1 ATOM 4384 C CG . ASN C 1 95 ? 47.147 4.011 33.818 1.00 40.36 ? 94 ASN C CG 1 ATOM 4385 O OD1 . ASN C 1 95 ? 47.838 5.023 33.655 1.00 42.85 ? 94 ASN C OD1 1 ATOM 4386 N ND2 . ASN C 1 95 ? 45.939 4.051 34.366 1.00 43.45 ? 94 ASN C ND2 1 ATOM 4387 N N . PHE C 1 96 ? 48.474 2.426 30.504 1.00 31.03 ? 95 PHE C N 1 ATOM 4388 C CA . PHE C 1 96 ? 48.255 2.760 29.121 1.00 30.42 ? 95 PHE C CA 1 ATOM 4389 C C . PHE C 1 96 ? 46.736 2.807 28.913 1.00 29.53 ? 95 PHE C C 1 ATOM 4390 O O . PHE C 1 96 ? 46.041 1.804 29.047 1.00 28.02 ? 95 PHE C O 1 ATOM 4391 C CB . PHE C 1 96 ? 48.904 1.682 28.255 1.00 31.57 ? 95 PHE C CB 1 ATOM 4392 C CG . PHE C 1 96 ? 49.413 2.177 26.927 1.00 32.57 ? 95 PHE C CG 1 ATOM 4393 C CD1 . PHE C 1 96 ? 48.655 3.018 26.131 1.00 33.57 ? 95 PHE C CD1 1 ATOM 4394 C CD2 . PHE C 1 96 ? 50.649 1.783 26.471 1.00 33.29 ? 95 PHE C CD2 1 ATOM 4395 C CE1 . PHE C 1 96 ? 49.140 3.457 24.917 1.00 33.81 ? 95 PHE C CE1 1 ATOM 4396 C CE2 . PHE C 1 96 ? 51.130 2.209 25.254 1.00 32.92 ? 95 PHE C CE2 1 ATOM 4397 C CZ . PHE C 1 96 ? 50.377 3.046 24.476 1.00 32.75 ? 95 PHE C CZ 1 ATOM 4398 N N . ASN C 1 97 ? 46.232 3.999 28.618 1.00 29.12 ? 96 ASN C N 1 ATOM 4399 C CA . ASN C 1 97 ? 44.808 4.216 28.391 1.00 28.94 ? 96 ASN C CA 1 ATOM 4400 C C . ASN C 1 97 ? 44.257 3.516 27.134 1.00 27.64 ? 96 ASN C C 1 ATOM 4401 O O . ASN C 1 97 ? 44.804 3.643 26.028 1.00 25.41 ? 96 ASN C O 1 ATOM 4402 C CB . ASN C 1 97 ? 44.554 5.710 28.273 1.00 30.42 ? 96 ASN C CB 1 ATOM 4403 C CG . ASN C 1 97 ? 43.111 6.060 28.445 1.00 32.55 ? 96 ASN C CG 1 ATOM 4404 O OD1 . ASN C 1 97 ? 42.410 6.389 27.473 1.00 34.12 ? 96 ASN C OD1 1 ATOM 4405 N ND2 . ASN C 1 97 ? 42.641 6.005 29.690 1.00 34.39 ? 96 ASN C ND2 1 ATOM 4406 N N . ASP C 1 98 ? 43.149 2.800 27.309 1.00 27.43 ? 97 ASP C N 1 ATOM 4407 C CA . ASP C 1 98 ? 42.534 2.029 26.235 1.00 26.70 ? 97 ASP C CA 1 ATOM 4408 C C . ASP C 1 98 ? 43.528 1.104 25.548 1.00 25.28 ? 97 ASP C C 1 ATOM 4409 O O . ASP C 1 98 ? 43.502 0.924 24.344 1.00 25.57 ? 97 ASP C O 1 ATOM 4410 C CB . ASP C 1 98 ? 41.843 2.966 25.242 1.00 27.23 ? 97 ASP C CB 1 ATOM 4411 C CG . ASP C 1 98 ? 40.583 3.572 25.819 1.00 28.71 ? 97 ASP C CG 1 ATOM 4412 O OD1 . ASP C 1 98 ? 39.726 2.818 26.316 1.00 28.83 ? 97 ASP C OD1 1 ATOM 4413 O OD2 . ASP C 1 98 ? 40.455 4.802 25.795 1.00 30.35 ? 97 ASP C OD2 1 ATOM 4414 N N . TYR C 1 99 ? 44.405 0.519 26.345 1.00 24.85 ? 98 TYR C N 1 ATOM 4415 C CA . TYR C 1 99 ? 45.433 -0.406 25.859 1.00 24.61 ? 98 TYR C CA 1 ATOM 4416 C C . TYR C 1 99 ? 44.868 -1.581 25.056 1.00 23.53 ? 98 TYR C C 1 ATOM 4417 O O . TYR C 1 99 ? 45.489 -2.019 24.093 1.00 22.57 ? 98 TYR C O 1 ATOM 4418 C CB . TYR C 1 99 ? 46.226 -0.937 27.067 1.00 24.65 ? 98 TYR C CB 1 ATOM 4419 C CG . TYR C 1 99 ? 47.415 -1.820 26.770 1.00 25.20 ? 98 TYR C CG 1 ATOM 4420 C CD1 . TYR C 1 99 ? 48.445 -1.394 25.938 1.00 25.78 ? 98 TYR C CD1 1 ATOM 4421 C CD2 . TYR C 1 99 ? 47.546 -3.061 27.388 1.00 26.28 ? 98 TYR C CD2 1 ATOM 4422 C CE1 . TYR C 1 99 ? 49.557 -2.200 25.691 1.00 26.00 ? 98 TYR C CE1 1 ATOM 4423 C CE2 . TYR C 1 99 ? 48.652 -3.865 27.170 1.00 27.39 ? 98 TYR C CE2 1 ATOM 4424 C CZ . TYR C 1 99 ? 49.656 -3.439 26.318 1.00 27.10 ? 98 TYR C CZ 1 ATOM 4425 O OH . TYR C 1 99 ? 50.743 -4.260 26.108 1.00 27.71 ? 98 TYR C OH 1 ATOM 4426 N N . GLU C 1 100 ? 43.720 -2.103 25.466 1.00 23.79 ? 99 GLU C N 1 ATOM 4427 C CA . GLU C 1 100 ? 43.182 -3.317 24.832 1.00 24.72 ? 99 GLU C CA 1 ATOM 4428 C C . GLU C 1 100 ? 42.578 -2.971 23.471 1.00 24.09 ? 99 GLU C C 1 ATOM 4429 O O . GLU C 1 100 ? 42.582 -3.802 22.543 1.00 23.70 ? 99 GLU C O 1 ATOM 4430 C CB . GLU C 1 100 ? 42.152 -4.019 25.727 1.00 26.30 ? 99 GLU C CB 1 ATOM 4431 C CG . GLU C 1 100 ? 42.720 -4.601 27.032 1.00 27.86 ? 99 GLU C CG 1 ATOM 4432 C CD . GLU C 1 100 ? 42.970 -3.548 28.112 1.00 29.78 ? 99 GLU C CD 1 ATOM 4433 O OE1 . GLU C 1 100 ? 42.160 -2.588 28.195 1.00 30.56 ? 99 GLU C OE1 1 ATOM 4434 O OE2 . GLU C 1 100 ? 43.975 -3.669 28.884 1.00 31.18 ? 99 GLU C OE2 1 ATOM 4435 N N . GLU C 1 101 ? 42.081 -1.737 23.352 1.00 23.19 ? 100 GLU C N 1 ATOM 4436 C CA . GLU C 1 101 ? 41.538 -1.259 22.095 1.00 23.30 ? 100 GLU C CA 1 ATOM 4437 C C . GLU C 1 101 ? 42.673 -1.045 21.104 1.00 23.22 ? 100 GLU C C 1 ATOM 4438 O O . GLU C 1 101 ? 42.565 -1.405 19.933 1.00 23.08 ? 100 GLU C O 1 ATOM 4439 C CB . GLU C 1 101 ? 40.753 0.039 22.291 1.00 23.55 ? 100 GLU C CB 1 ATOM 4440 C CG . GLU C 1 101 ? 39.359 -0.147 22.860 1.00 23.93 ? 100 GLU C CG 1 ATOM 4441 C CD . GLU C 1 101 ? 38.423 -0.864 21.921 1.00 24.11 ? 100 GLU C CD 1 ATOM 4442 O OE1 . GLU C 1 101 ? 38.251 -0.406 20.755 1.00 23.74 ? 100 GLU C OE1 1 ATOM 4443 O OE2 . GLU C 1 101 ? 37.863 -1.893 22.362 1.00 23.96 ? 100 GLU C OE2 1 ATOM 4444 N N . LEU C 1 102 ? 43.781 -0.486 21.582 1.00 22.86 ? 101 LEU C N 1 ATOM 4445 C CA . LEU C 1 102 ? 44.944 -0.294 20.727 1.00 22.29 ? 101 LEU C CA 1 ATOM 4446 C C . LEU C 1 102 ? 45.500 -1.616 20.250 1.00 21.84 ? 101 LEU C C 1 ATOM 4447 O O . LEU C 1 102 ? 45.971 -1.731 19.130 1.00 20.99 ? 101 LEU C O 1 ATOM 4448 C CB . LEU C 1 102 ? 46.026 0.477 21.458 1.00 22.89 ? 101 LEU C CB 1 ATOM 4449 C CG . LEU C 1 102 ? 47.305 0.672 20.638 1.00 23.40 ? 101 LEU C CG 1 ATOM 4450 C CD1 . LEU C 1 102 ? 46.960 1.336 19.314 1.00 24.29 ? 101 LEU C CD1 1 ATOM 4451 C CD2 . LEU C 1 102 ? 48.308 1.472 21.421 1.00 23.51 ? 101 LEU C CD2 1 ATOM 4452 N N . LYS C 1 103 ? 45.458 -2.624 21.108 1.00 22.82 ? 102 LYS C N 1 ATOM 4453 C CA . LYS C 1 103 ? 45.925 -3.942 20.712 1.00 23.25 ? 102 LYS C CA 1 ATOM 4454 C C . LYS C 1 103 ? 45.001 -4.501 19.660 1.00 23.32 ? 102 LYS C C 1 ATOM 4455 O O . LYS C 1 103 ? 45.448 -5.193 18.759 1.00 23.95 ? 102 LYS C O 1 ATOM 4456 C CB . LYS C 1 103 ? 46.048 -4.871 21.920 1.00 24.52 ? 102 LYS C CB 1 ATOM 4457 C CG . LYS C 1 103 ? 47.191 -4.461 22.845 1.00 25.30 ? 102 LYS C CG 1 ATOM 4458 C CD . LYS C 1 103 ? 47.283 -5.328 24.088 1.00 26.52 ? 102 LYS C CD 1 ATOM 4459 C CE . LYS C 1 103 ? 48.087 -6.584 23.804 1.00 27.68 ? 102 LYS C CE 1 ATOM 4460 N NZ . LYS C 1 103 ? 48.278 -7.395 25.035 1.00 29.10 ? 102 LYS C NZ 1 ATOM 4461 N N . HIS C 1 104 ? 43.711 -4.184 19.754 1.00 23.33 ? 103 HIS C N 1 ATOM 4462 C CA . HIS C 1 104 ? 42.765 -4.624 18.750 1.00 23.59 ? 103 HIS C CA 1 ATOM 4463 C C . HIS C 1 104 ? 43.077 -4.051 17.366 1.00 23.65 ? 103 HIS C C 1 ATOM 4464 O O . HIS C 1 104 ? 43.131 -4.804 16.397 1.00 22.92 ? 103 HIS C O 1 ATOM 4465 C CB . HIS C 1 104 ? 41.330 -4.275 19.148 1.00 23.99 ? 103 HIS C CB 1 ATOM 4466 C CG . HIS C 1 104 ? 40.334 -4.612 18.092 1.00 24.92 ? 103 HIS C CG 1 ATOM 4467 N ND1 . HIS C 1 104 ? 39.672 -5.820 18.058 1.00 25.83 ? 103 HIS C ND1 1 ATOM 4468 C CD2 . HIS C 1 104 ? 39.927 -3.926 17.000 1.00 25.34 ? 103 HIS C CD2 1 ATOM 4469 C CE1 . HIS C 1 104 ? 38.884 -5.853 17.000 1.00 26.45 ? 103 HIS C CE1 1 ATOM 4470 N NE2 . HIS C 1 104 ? 39.025 -4.718 16.338 1.00 26.50 ? 103 HIS C NE2 1 ATOM 4471 N N . LEU C 1 105 ? 43.233 -2.724 17.281 1.00 24.49 ? 104 LEU C N 1 ATOM 4472 C CA . LEU C 1 105 ? 43.639 -2.043 16.036 1.00 26.36 ? 104 LEU C CA 1 ATOM 4473 C C . LEU C 1 105 ? 44.885 -2.680 15.438 1.00 27.46 ? 104 LEU C C 1 ATOM 4474 O O . LEU C 1 105 ? 44.983 -2.907 14.231 1.00 28.38 ? 104 LEU C O 1 ATOM 4475 C CB . LEU C 1 105 ? 44.001 -0.572 16.297 1.00 26.66 ? 104 LEU C CB 1 ATOM 4476 C CG . LEU C 1 105 ? 42.944 0.399 16.798 1.00 27.73 ? 104 LEU C CG 1 ATOM 4477 C CD1 . LEU C 1 105 ? 43.487 1.819 16.787 1.00 28.35 ? 104 LEU C CD1 1 ATOM 4478 C CD2 . LEU C 1 105 ? 41.696 0.311 15.930 1.00 29.15 ? 104 LEU C CD2 1 ATOM 4479 N N . LEU C 1 106 ? 45.843 -2.919 16.316 1.00 33.21 ? 105 LEU C N 1 ATOM 4480 C CA . LEU C 1 106 ? 47.132 -3.505 15.973 1.00 35.26 ? 105 LEU C CA 1 ATOM 4481 C C . LEU C 1 106 ? 47.038 -4.918 15.361 1.00 35.87 ? 105 LEU C C 1 ATOM 4482 O O . LEU C 1 106 ? 47.937 -5.332 14.635 1.00 36.42 ? 105 LEU C O 1 ATOM 4483 C CB . LEU C 1 106 ? 47.995 -3.534 17.239 1.00 35.54 ? 105 LEU C CB 1 ATOM 4484 C CG . LEU C 1 106 ? 49.473 -3.833 17.105 1.00 37.30 ? 105 LEU C CG 1 ATOM 4485 C CD1 . LEU C 1 106 ? 50.124 -2.767 16.234 1.00 37.66 ? 105 LEU C CD1 1 ATOM 4486 C CD2 . LEU C 1 106 ? 50.123 -3.889 18.487 1.00 36.92 ? 105 LEU C CD2 1 ATOM 4487 N N . SER C 1 107 ? 45.956 -5.642 15.639 1.00 35.75 ? 106 SER C N 1 ATOM 4488 C CA . SER C 1 107 ? 45.729 -6.953 15.018 1.00 36.94 ? 106 SER C CA 1 ATOM 4489 C C . SER C 1 107 ? 45.253 -6.830 13.570 1.00 37.57 ? 106 SER C C 1 ATOM 4490 O O . SER C 1 107 ? 45.149 -7.833 12.856 1.00 37.98 ? 106 SER C O 1 ATOM 4491 C CB . SER C 1 107 ? 44.706 -7.760 15.815 1.00 37.72 ? 106 SER C CB 1 ATOM 4492 O OG . SER C 1 107 ? 43.401 -7.284 15.584 1.00 37.75 ? 106 SER C OG 1 ATOM 4493 N N . ARG C 1 108 ? 44.930 -5.604 13.157 1.00 36.32 ? 107 ARG C N 1 ATOM 4494 C CA . ARG C 1 108 ? 44.615 -5.311 11.771 1.00 37.21 ? 107 ARG C CA 1 ATOM 4495 C C . ARG C 1 108 ? 45.776 -4.583 11.040 1.00 35.07 ? 107 ARG C C 1 ATOM 4496 O O . ARG C 1 108 ? 45.613 -4.119 9.912 1.00 34.59 ? 107 ARG C O 1 ATOM 4497 C CB . ARG C 1 108 ? 43.317 -4.489 11.686 1.00 39.46 ? 107 ARG C CB 1 ATOM 4498 C CG . ARG C 1 108 ? 42.025 -5.300 11.607 1.00 43.56 ? 107 ARG C CG 1 ATOM 4499 C CD . ARG C 1 108 ? 41.184 -5.248 12.888 1.00 45.85 ? 107 ARG C CD 1 ATOM 4500 N NE . ARG C 1 108 ? 39.755 -5.535 12.639 1.00 49.53 ? 107 ARG C NE 1 ATOM 4501 C CZ . ARG C 1 108 ? 39.155 -6.728 12.769 1.00 52.90 ? 107 ARG C CZ 1 ATOM 4502 N NH1 . ARG C 1 108 ? 39.828 -7.812 13.151 1.00 54.04 ? 107 ARG C NH1 1 ATOM 4503 N NH2 . ARG C 1 108 ? 37.852 -6.845 12.518 1.00 54.93 ? 107 ARG C NH2 1 ATOM 4504 N N . ILE C 1 109 ? 46.951 -4.520 11.664 1.00 33.11 ? 108 ILE C N 1 ATOM 4505 C CA . ILE C 1 109 ? 48.100 -3.810 11.087 1.00 31.72 ? 108 ILE C CA 1 ATOM 4506 C C . ILE C 1 109 ? 49.277 -4.741 10.860 1.00 31.63 ? 108 ILE C C 1 ATOM 4507 O O . ILE C 1 109 ? 49.603 -5.554 11.712 1.00 31.95 ? 108 ILE C O 1 ATOM 4508 C CB . ILE C 1 109 ? 48.530 -2.626 11.969 1.00 29.88 ? 108 ILE C CB 1 ATOM 4509 C CG1 . ILE C 1 109 ? 47.448 -1.537 11.942 1.00 29.38 ? 108 ILE C CG1 1 ATOM 4510 C CG2 . ILE C 1 109 ? 49.843 -2.039 11.474 1.00 29.80 ? 108 ILE C CG2 1 ATOM 4511 C CD1 . ILE C 1 109 ? 47.587 -0.473 13.011 1.00 27.93 ? 108 ILE C CD1 1 ATOM 4512 N N . ASN C 1 110 ? 49.909 -4.617 9.700 1.00 32.54 ? 109 ASN C N 1 ATOM 4513 C CA . ASN C 1 110 ? 51.065 -5.461 9.342 1.00 34.05 ? 109 ASN C CA 1 ATOM 4514 C C . ASN C 1 110 ? 52.420 -4.732 9.386 1.00 33.86 ? 109 ASN C C 1 ATOM 4515 O O . ASN C 1 110 ? 53.473 -5.390 9.450 1.00 33.75 ? 109 ASN C O 1 ATOM 4516 C CB . ASN C 1 110 ? 50.863 -6.076 7.956 1.00 35.48 ? 109 ASN C CB 1 ATOM 4517 C CG . ASN C 1 110 ? 49.861 -7.209 7.957 1.00 36.40 ? 109 ASN C CG 1 ATOM 4518 O OD1 . ASN C 1 110 ? 48.836 -7.137 7.294 1.00 37.49 ? 109 ASN C OD1 1 ATOM 4519 N ND2 . ASN C 1 110 ? 50.153 -8.260 8.696 1.00 37.04 ? 109 ASN C ND2 1 ATOM 4520 N N . HIS C 1 111 ? 52.393 -3.396 9.347 1.00 33.01 ? 110 HIS C N 1 ATOM 4521 C CA . HIS C 1 111 ? 53.619 -2.619 9.294 1.00 34.40 ? 110 HIS C CA 1 ATOM 4522 C C . HIS C 1 111 ? 53.423 -1.151 9.690 1.00 33.51 ? 110 HIS C C 1 ATOM 4523 O O . HIS C 1 111 ? 52.521 -0.482 9.186 1.00 31.61 ? 110 HIS C O 1 ATOM 4524 C CB . HIS C 1 111 ? 54.188 -2.712 7.879 1.00 37.20 ? 110 HIS C CB 1 ATOM 4525 C CG . HIS C 1 111 ? 55.594 -2.215 7.738 1.00 39.23 ? 110 HIS C CG 1 ATOM 4526 N ND1 . HIS C 1 111 ? 56.597 -2.532 8.629 1.00 39.76 ? 110 HIS C ND1 1 ATOM 4527 C CD2 . HIS C 1 111 ? 56.177 -1.475 6.764 1.00 40.40 ? 110 HIS C CD2 1 ATOM 4528 C CE1 . HIS C 1 111 ? 57.729 -1.980 8.226 1.00 40.66 ? 110 HIS C CE1 1 ATOM 4529 N NE2 . HIS C 1 111 ? 57.500 -1.332 7.099 1.00 40.85 ? 110 HIS C NE2 1 ATOM 4530 N N . PHE C 1 112 ? 54.270 -0.682 10.615 1.00 33.88 ? 111 PHE C N 1 ATOM 4531 C CA . PHE C 1 112 ? 54.450 0.747 10.897 1.00 33.73 ? 111 PHE C CA 1 ATOM 4532 C C . PHE C 1 112 ? 55.750 1.250 10.267 1.00 35.58 ? 111 PHE C C 1 ATOM 4533 O O . PHE C 1 112 ? 56.660 0.470 9.975 1.00 36.08 ? 111 PHE C O 1 ATOM 4534 C CB . PHE C 1 112 ? 54.593 1.015 12.391 1.00 33.09 ? 111 PHE C CB 1 ATOM 4535 C CG . PHE C 1 112 ? 53.379 0.708 13.207 1.00 32.91 ? 111 PHE C CG 1 ATOM 4536 C CD1 . PHE C 1 112 ? 52.205 1.451 13.056 1.00 32.64 ? 111 PHE C CD1 1 ATOM 4537 C CD2 . PHE C 1 112 ? 53.427 -0.280 14.184 1.00 33.12 ? 111 PHE C CD2 1 ATOM 4538 C CE1 . PHE C 1 112 ? 51.092 1.182 13.836 1.00 32.11 ? 111 PHE C CE1 1 ATOM 4539 C CE2 . PHE C 1 112 ? 52.324 -0.545 14.972 1.00 32.87 ? 111 PHE C CE2 1 ATOM 4540 C CZ . PHE C 1 112 ? 51.146 0.178 14.786 1.00 32.50 ? 111 PHE C CZ 1 ATOM 4541 N N . GLU C 1 113 ? 55.823 2.566 10.077 1.00 36.30 ? 112 GLU C N 1 ATOM 4542 C CA . GLU C 1 113 ? 57.070 3.262 9.838 1.00 37.30 ? 112 GLU C CA 1 ATOM 4543 C C . GLU C 1 113 ? 57.198 4.354 10.899 1.00 36.58 ? 112 GLU C C 1 ATOM 4544 O O . GLU C 1 113 ? 56.494 5.376 10.864 1.00 35.92 ? 112 GLU C O 1 ATOM 4545 C CB . GLU C 1 113 ? 57.107 3.879 8.443 1.00 39.70 ? 112 GLU C CB 1 ATOM 4546 C CG . GLU C 1 113 ? 58.462 4.488 8.089 1.00 42.42 ? 112 GLU C CG 1 ATOM 4547 C CD . GLU C 1 113 ? 58.481 5.185 6.739 1.00 45.30 ? 112 GLU C CD 1 ATOM 4548 O OE1 . GLU C 1 113 ? 57.913 4.637 5.767 1.00 47.76 ? 112 GLU C OE1 1 ATOM 4549 O OE2 . GLU C 1 113 ? 59.078 6.283 6.646 1.00 47.21 ? 112 GLU C OE2 1 ATOM 4550 N N . LYS C 1 114 ? 58.097 4.142 11.850 1.00 35.73 ? 113 LYS C N 1 ATOM 4551 C CA . LYS C 1 114 ? 58.291 5.120 12.893 1.00 35.13 ? 113 LYS C CA 1 ATOM 4552 C C . LYS C 1 114 ? 58.940 6.366 12.298 1.00 35.78 ? 113 LYS C C 1 ATOM 4553 O O . LYS C 1 114 ? 59.871 6.270 11.490 1.00 38.36 ? 113 LYS C O 1 ATOM 4554 C CB . LYS C 1 114 ? 59.138 4.550 14.022 1.00 35.11 ? 113 LYS C CB 1 ATOM 4555 C CG . LYS C 1 114 ? 58.860 5.209 15.360 1.00 34.39 ? 113 LYS C CG 1 ATOM 4556 C CD . LYS C 1 114 ? 59.561 4.476 16.482 1.00 34.97 ? 113 LYS C CD 1 ATOM 4557 C CE . LYS C 1 114 ? 61.064 4.694 16.432 1.00 36.42 ? 113 LYS C CE 1 ATOM 4558 N NZ . LYS C 1 114 ? 61.688 4.073 17.629 1.00 36.97 ? 113 LYS C NZ 1 ATOM 4559 N N . ILE C 1 115 ? 58.412 7.526 12.662 1.00 34.54 ? 114 ILE C N 1 ATOM 4560 C CA . ILE C 1 115 ? 58.977 8.791 12.234 1.00 35.66 ? 114 ILE C CA 1 ATOM 4561 C C . ILE C 1 115 ? 59.140 9.716 13.427 1.00 35.45 ? 114 ILE C C 1 ATOM 4562 O O . ILE C 1 115 ? 58.383 9.661 14.399 1.00 35.73 ? 114 ILE C O 1 ATOM 4563 C CB . ILE C 1 115 ? 58.109 9.490 11.167 1.00 36.06 ? 114 ILE C CB 1 ATOM 4564 C CG1 . ILE C 1 115 ? 56.710 9.814 11.700 1.00 35.05 ? 114 ILE C CG1 1 ATOM 4565 C CG2 . ILE C 1 115 ? 58.001 8.626 9.918 1.00 36.73 ? 114 ILE C CG2 1 ATOM 4566 C CD1 . ILE C 1 115 ? 55.975 10.832 10.852 1.00 35.80 ? 114 ILE C CD1 1 ATOM 4567 N N . GLN C 1 116 ? 60.149 10.558 13.363 1.00 36.74 ? 115 GLN C N 1 ATOM 4568 C CA . GLN C 1 116 ? 60.257 11.654 14.300 1.00 36.66 ? 115 GLN C CA 1 ATOM 4569 C C . GLN C 1 116 ? 59.183 12.681 13.968 1.00 36.11 ? 115 GLN C C 1 ATOM 4570 O O . GLN C 1 116 ? 58.934 12.955 12.805 1.00 36.07 ? 115 GLN C O 1 ATOM 4571 C CB . GLN C 1 116 ? 61.615 12.284 14.167 1.00 38.15 ? 115 GLN C CB 1 ATOM 4572 C CG . GLN C 1 116 ? 61.868 13.365 15.178 1.00 39.12 ? 115 GLN C CG 1 ATOM 4573 C CD . GLN C 1 116 ? 63.298 13.798 15.130 1.00 40.45 ? 115 GLN C CD 1 ATOM 4574 O OE1 . GLN C 1 116 ? 64.110 13.322 15.911 1.00 41.27 ? 115 GLN C OE1 1 ATOM 4575 N NE2 . GLN C 1 116 ? 63.626 14.657 14.180 1.00 41.76 ? 115 GLN C NE2 1 ATOM 4576 N N . ILE C 1 117 ? 58.513 13.218 14.978 1.00 35.94 ? 116 ILE C N 1 ATOM 4577 C CA . ILE C 1 117 ? 57.594 14.323 14.721 1.00 36.01 ? 116 ILE C CA 1 ATOM 4578 C C . ILE C 1 117 ? 57.877 15.540 15.575 1.00 36.53 ? 116 ILE C C 1 ATOM 4579 O O . ILE C 1 117 ? 57.629 16.655 15.138 1.00 37.70 ? 116 ILE C O 1 ATOM 4580 C CB . ILE C 1 117 ? 56.108 13.908 14.801 1.00 34.50 ? 116 ILE C CB 1 ATOM 4581 C CG1 . ILE C 1 117 ? 55.725 13.398 16.185 1.00 33.31 ? 116 ILE C CG1 1 ATOM 4582 C CG2 . ILE C 1 117 ? 55.808 12.858 13.743 1.00 34.28 ? 116 ILE C CG2 1 ATOM 4583 C CD1 . ILE C 1 117 ? 54.226 13.292 16.376 1.00 32.45 ? 116 ILE C CD1 1 ATOM 4584 N N . ILE C 1 118 ? 58.392 15.339 16.779 1.00 36.51 ? 117 ILE C N 1 ATOM 4585 C CA . ILE C 1 118 ? 58.845 16.463 17.599 1.00 37.54 ? 117 ILE C CA 1 ATOM 4586 C C . ILE C 1 118 ? 60.251 16.161 18.113 1.00 38.89 ? 117 ILE C C 1 ATOM 4587 O O . ILE C 1 118 ? 60.433 15.351 19.031 1.00 38.11 ? 117 ILE C O 1 ATOM 4588 C CB . ILE C 1 118 ? 57.908 16.742 18.784 1.00 36.65 ? 117 ILE C CB 1 ATOM 4589 C CG1 . ILE C 1 118 ? 56.484 17.022 18.292 1.00 36.09 ? 117 ILE C CG1 1 ATOM 4590 C CG2 . ILE C 1 118 ? 58.439 17.910 19.615 1.00 37.90 ? 117 ILE C CG2 1 ATOM 4591 C CD1 . ILE C 1 118 ? 55.467 17.090 19.410 1.00 34.98 ? 117 ILE C CD1 1 ATOM 4592 N N . PRO C 1 119 ? 61.259 16.804 17.510 1.00 41.29 ? 118 PRO C N 1 ATOM 4593 C CA . PRO C 1 119 ? 62.615 16.621 17.992 1.00 42.21 ? 118 PRO C CA 1 ATOM 4594 C C . PRO C 1 119 ? 62.790 17.102 19.430 1.00 42.13 ? 118 PRO C C 1 ATOM 4595 O O . PRO C 1 119 ? 62.222 18.118 19.827 1.00 41.22 ? 118 PRO C O 1 ATOM 4596 C CB . PRO C 1 119 ? 63.453 17.474 17.028 1.00 44.77 ? 118 PRO C CB 1 ATOM 4597 C CG . PRO C 1 119 ? 62.639 17.570 15.787 1.00 44.44 ? 118 PRO C CG 1 ATOM 4598 C CD . PRO C 1 119 ? 61.211 17.578 16.254 1.00 42.87 ? 118 PRO C CD 1 ATOM 4599 N N . LYS C 1 120 ? 63.569 16.340 20.190 1.00 42.63 ? 119 LYS C N 1 ATOM 4600 C CA . LYS C 1 120 ? 64.041 16.725 21.528 1.00 43.63 ? 119 LYS C CA 1 ATOM 4601 C C . LYS C 1 120 ? 64.657 18.126 21.547 1.00 44.35 ? 119 LYS C C 1 ATOM 4602 O O . LYS C 1 120 ? 64.493 18.862 22.506 1.00 44.69 ? 119 LYS C O 1 ATOM 4603 C CB . LYS C 1 120 ? 65.105 15.726 21.999 1.00 44.79 ? 119 LYS C CB 1 ATOM 4604 C CG . LYS C 1 120 ? 64.946 15.241 23.423 1.00 44.89 ? 119 LYS C CG 1 ATOM 4605 C CD . LYS C 1 120 ? 65.511 13.839 23.546 1.00 45.85 ? 119 LYS C CD 1 ATOM 4606 C CE . LYS C 1 120 ? 65.451 13.341 24.977 1.00 47.01 ? 119 LYS C CE 1 ATOM 4607 N NZ . LYS C 1 120 ? 65.655 11.868 25.067 1.00 47.67 ? 119 LYS C NZ 1 ATOM 4608 N N . SER C 1 121 ? 65.366 18.477 20.480 1.00 45.03 ? 120 SER C N 1 ATOM 4609 C CA . SER C 1 121 ? 66.041 19.775 20.360 1.00 46.57 ? 120 SER C CA 1 ATOM 4610 C C . SER C 1 121 ? 65.122 20.957 20.060 1.00 46.28 ? 120 SER C C 1 ATOM 4611 O O . SER C 1 121 ? 65.584 22.094 20.052 1.00 47.97 ? 120 SER C O 1 ATOM 4612 C CB . SER C 1 121 ? 67.085 19.712 19.241 1.00 48.23 ? 120 SER C CB 1 ATOM 4613 O OG . SER C 1 121 ? 66.457 19.782 17.974 1.00 47.97 ? 120 SER C OG 1 ATOM 4614 N N . SER C 1 122 ? 63.843 20.699 19.784 1.00 44.30 ? 121 SER C N 1 ATOM 4615 C CA . SER C 1 122 ? 62.900 21.766 19.441 1.00 44.11 ? 121 SER C CA 1 ATOM 4616 C C . SER C 1 122 ? 62.352 22.461 20.675 1.00 43.63 ? 121 SER C C 1 ATOM 4617 O O . SER C 1 122 ? 61.693 23.488 20.555 1.00 44.45 ? 121 SER C O 1 ATOM 4618 C CB . SER C 1 122 ? 61.735 21.216 18.623 1.00 42.59 ? 121 SER C CB 1 ATOM 4619 O OG . SER C 1 122 ? 60.985 20.290 19.384 1.00 40.95 ? 121 SER C OG 1 ATOM 4620 N N . TRP C 1 123 ? 62.625 21.895 21.851 1.00 42.53 ? 122 TRP C N 1 ATOM 4621 C CA . TRP C 1 123 ? 62.182 22.454 23.124 1.00 42.32 ? 122 TRP C CA 1 ATOM 4622 C C . TRP C 1 123 ? 63.164 23.485 23.665 1.00 44.81 ? 122 TRP C C 1 ATOM 4623 O O . TRP C 1 123 ? 64.077 23.136 24.413 1.00 44.94 ? 122 TRP C O 1 ATOM 4624 C CB . TRP C 1 123 ? 62.026 21.327 24.150 1.00 40.76 ? 122 TRP C CB 1 ATOM 4625 C CG . TRP C 1 123 ? 61.021 20.300 23.757 1.00 38.40 ? 122 TRP C CG 1 ATOM 4626 C CD1 . TRP C 1 123 ? 61.264 19.012 23.394 1.00 37.00 ? 122 TRP C CD1 1 ATOM 4627 C CD2 . TRP C 1 123 ? 59.609 20.480 23.684 1.00 37.34 ? 122 TRP C CD2 1 ATOM 4628 N NE1 . TRP C 1 123 ? 60.092 18.372 23.104 1.00 35.31 ? 122 TRP C NE1 1 ATOM 4629 C CE2 . TRP C 1 123 ? 59.055 19.252 23.273 1.00 35.52 ? 122 TRP C CE2 1 ATOM 4630 C CE3 . TRP C 1 123 ? 58.753 21.562 23.935 1.00 37.89 ? 122 TRP C CE3 1 ATOM 4631 C CZ2 . TRP C 1 123 ? 57.679 19.070 23.100 1.00 34.17 ? 122 TRP C CZ2 1 ATOM 4632 C CZ3 . TRP C 1 123 ? 57.385 21.383 23.758 1.00 36.66 ? 122 TRP C CZ3 1 ATOM 4633 C CH2 . TRP C 1 123 ? 56.866 20.143 23.345 1.00 34.86 ? 122 TRP C CH2 1 ATOM 4634 N N . SER C 1 124 ? 62.959 24.752 23.309 1.00 46.94 ? 123 SER C N 1 ATOM 4635 C CA . SER C 1 124 ? 63.868 25.837 23.717 1.00 50.04 ? 123 SER C CA 1 ATOM 4636 C C . SER C 1 124 ? 63.777 26.197 25.196 1.00 50.80 ? 123 SER C C 1 ATOM 4637 O O . SER C 1 124 ? 64.798 26.415 25.851 1.00 52.70 ? 123 SER C O 1 ATOM 4638 C CB . SER C 1 124 ? 63.587 27.104 22.906 1.00 51.93 ? 123 SER C CB 1 ATOM 4639 O OG . SER C 1 124 ? 63.617 26.838 21.520 1.00 52.39 ? 123 SER C OG 1 ATOM 4640 N N . ASP C 1 125 ? 62.551 26.265 25.708 1.00 49.83 ? 124 ASP C N 1 ATOM 4641 C CA . ASP C 1 125 ? 62.279 26.812 27.032 1.00 50.54 ? 124 ASP C CA 1 ATOM 4642 C C . ASP C 1 125 ? 61.973 25.745 28.071 1.00 48.74 ? 124 ASP C C 1 ATOM 4643 O O . ASP C 1 125 ? 61.528 26.052 29.177 1.00 49.10 ? 124 ASP C O 1 ATOM 4644 C CB . ASP C 1 125 ? 61.134 27.822 26.936 1.00 51.51 ? 124 ASP C CB 1 ATOM 4645 C CG . ASP C 1 125 ? 61.509 29.040 26.105 1.00 54.07 ? 124 ASP C CG 1 ATOM 4646 O OD1 . ASP C 1 125 ? 62.460 29.745 26.490 1.00 56.33 ? 124 ASP C OD1 1 ATOM 4647 O OD2 . ASP C 1 125 ? 60.870 29.288 25.062 1.00 54.53 ? 124 ASP C OD2 1 ATOM 4648 N N . HIS C 1 126 ? 62.230 24.490 27.725 1.00 47.42 ? 125 HIS C N 1 ATOM 4649 C CA . HIS C 1 126 ? 62.076 23.393 28.667 1.00 46.10 ? 125 HIS C CA 1 ATOM 4650 C C . HIS C 1 126 ? 63.270 22.447 28.585 1.00 46.30 ? 125 HIS C C 1 ATOM 4651 O O . HIS C 1 126 ? 63.912 22.331 27.539 1.00 46.91 ? 125 HIS C O 1 ATOM 4652 C CB . HIS C 1 126 ? 60.779 22.664 28.387 1.00 44.17 ? 125 HIS C CB 1 ATOM 4653 C CG . HIS C 1 126 ? 59.580 23.559 28.417 1.00 44.96 ? 125 HIS C CG 1 ATOM 4654 N ND1 . HIS C 1 126 ? 59.148 24.261 27.312 1.00 45.43 ? 125 HIS C ND1 1 ATOM 4655 C CD2 . HIS C 1 126 ? 58.733 23.882 29.423 1.00 44.81 ? 125 HIS C CD2 1 ATOM 4656 C CE1 . HIS C 1 126 ? 58.081 24.969 27.630 1.00 45.76 ? 125 HIS C CE1 1 ATOM 4657 N NE2 . HIS C 1 126 ? 57.806 24.755 28.905 1.00 45.75 ? 125 HIS C NE2 1 ATOM 4658 N N . GLU C 1 127 ? 63.592 21.808 29.706 1.00 46.18 ? 126 GLU C N 1 ATOM 4659 C CA . GLU C 1 127 ? 64.651 20.804 29.737 1.00 45.92 ? 126 GLU C CA 1 ATOM 4660 C C . GLU C 1 127 ? 64.094 19.493 29.192 1.00 43.32 ? 126 GLU C C 1 ATOM 4661 O O . GLU C 1 127 ? 63.125 18.950 29.738 1.00 42.49 ? 126 GLU C O 1 ATOM 4662 C CB . GLU C 1 127 ? 65.198 20.615 31.158 1.00 46.55 ? 126 GLU C CB 1 ATOM 4663 C CG . GLU C 1 127 ? 66.381 19.655 31.253 1.00 47.14 ? 126 GLU C CG 1 ATOM 4664 C CD . GLU C 1 127 ? 67.544 20.038 30.338 1.00 48.64 ? 126 GLU C CD 1 ATOM 4665 O OE1 . GLU C 1 127 ? 68.079 21.168 30.482 1.00 50.16 ? 126 GLU C OE1 1 ATOM 4666 O OE2 . GLU C 1 127 ? 67.904 19.209 29.463 1.00 47.33 ? 126 GLU C OE2 1 ATOM 4667 N N . ALA C 1 128 ? 64.706 19.010 28.110 1.00 42.30 ? 127 ALA C N 1 ATOM 4668 C CA . ALA C 1 128 ? 64.256 17.814 27.411 1.00 40.13 ? 127 ALA C CA 1 ATOM 4669 C C . ALA C 1 128 ? 65.197 16.633 27.593 1.00 39.93 ? 127 ALA C C 1 ATOM 4670 O O . ALA C 1 128 ? 64.897 15.541 27.116 1.00 38.54 ? 127 ALA C O 1 ATOM 4671 C CB . ALA C 1 128 ? 64.100 18.118 25.936 1.00 40.05 ? 127 ALA C CB 1 ATOM 4672 N N . SER C 1 129 ? 66.311 16.847 28.297 1.00 41.24 ? 128 SER C N 1 ATOM 4673 C CA . SER C 1 129 ? 67.377 15.846 28.425 1.00 41.64 ? 128 SER C CA 1 ATOM 4674 C C . SER C 1 129 ? 67.609 15.260 29.833 1.00 40.97 ? 128 SER C C 1 ATOM 4675 O O . SER C 1 129 ? 68.476 14.407 29.999 1.00 40.94 ? 128 SER C O 1 ATOM 4676 C CB . SER C 1 129 ? 68.680 16.427 27.895 1.00 44.05 ? 128 SER C CB 1 ATOM 4677 O OG . SER C 1 129 ? 68.493 16.853 26.554 1.00 45.23 ? 128 SER C OG 1 ATOM 4678 N N . ALA C 1 130 ? 66.820 15.678 30.819 1.00 40.05 ? 129 ALA C N 1 ATOM 4679 C CA . ALA C 1 130 ? 66.904 15.121 32.169 1.00 39.82 ? 129 ALA C CA 1 ATOM 4680 C C . ALA C 1 130 ? 65.686 14.267 32.554 1.00 37.76 ? 129 ALA C C 1 ATOM 4681 O O . ALA C 1 130 ? 65.523 13.887 33.718 1.00 37.68 ? 129 ALA C O 1 ATOM 4682 C CB . ALA C 1 130 ? 67.096 16.249 33.177 1.00 41.29 ? 129 ALA C CB 1 ATOM 4683 N N . GLY C 1 131 ? 64.829 13.959 31.592 1.00 36.42 ? 130 GLY C N 1 ATOM 4684 C CA . GLY C 1 131 ? 63.626 13.197 31.880 1.00 34.72 ? 130 GLY C CA 1 ATOM 4685 C C . GLY C 1 131 ? 63.900 11.714 32.004 1.00 34.47 ? 130 GLY C C 1 ATOM 4686 O O . GLY C 1 131 ? 63.568 10.958 31.110 1.00 34.49 ? 130 GLY C O 1 ATOM 4687 N N . VAL C 1 132 ? 64.481 11.292 33.121 1.00 35.25 ? 131 VAL C N 1 ATOM 4688 C CA . VAL C 1 132 ? 64.947 9.918 33.281 1.00 35.36 ? 131 VAL C CA 1 ATOM 4689 C C . VAL C 1 132 ? 64.636 9.383 34.671 1.00 35.16 ? 131 VAL C C 1 ATOM 4690 O O . VAL C 1 132 ? 64.237 10.136 35.546 1.00 35.65 ? 131 VAL C O 1 ATOM 4691 C CB . VAL C 1 132 ? 66.471 9.798 33.023 1.00 37.58 ? 131 VAL C CB 1 ATOM 4692 C CG1 . VAL C 1 132 ? 66.780 9.926 31.535 1.00 37.94 ? 131 VAL C CG1 1 ATOM 4693 C CG2 . VAL C 1 132 ? 67.246 10.839 33.814 1.00 38.90 ? 131 VAL C CG2 1 ATOM 4694 N N . SER C 1 133 ? 64.835 8.084 34.870 1.00 34.60 ? 132 SER C N 1 ATOM 4695 C CA . SER C 1 133 ? 64.457 7.432 36.111 1.00 34.97 ? 132 SER C CA 1 ATOM 4696 C C . SER C 1 133 ? 65.243 6.145 36.304 1.00 35.61 ? 132 SER C C 1 ATOM 4697 O O . SER C 1 133 ? 65.532 5.445 35.342 1.00 35.29 ? 132 SER C O 1 ATOM 4698 C CB . SER C 1 133 ? 62.954 7.104 36.085 1.00 34.16 ? 132 SER C CB 1 ATOM 4699 O OG . SER C 1 133 ? 62.533 6.400 37.250 1.00 34.52 ? 132 SER C OG 1 ATOM 4700 N N . SER C 1 134 ? 65.558 5.817 37.551 1.00 36.61 ? 133 SER C N 1 ATOM 4701 C CA . SER C 1 134 ? 66.159 4.521 37.881 1.00 37.66 ? 133 SER C CA 1 ATOM 4702 C C . SER C 1 134 ? 65.253 3.339 37.507 1.00 36.54 ? 133 SER C C 1 ATOM 4703 O O . SER C 1 134 ? 65.694 2.196 37.484 1.00 36.86 ? 133 SER C O 1 ATOM 4704 C CB . SER C 1 134 ? 66.446 4.466 39.375 1.00 38.91 ? 133 SER C CB 1 ATOM 4705 O OG . SER C 1 134 ? 65.270 4.819 40.089 1.00 39.03 ? 133 SER C OG 1 ATOM 4706 N N . ALA C 1 135 ? 63.980 3.619 37.249 1.00 35.93 ? 134 ALA C N 1 ATOM 4707 C CA . ALA C 1 135 ? 63.003 2.592 36.874 1.00 35.30 ? 134 ALA C CA 1 ATOM 4708 C C . ALA C 1 135 ? 63.218 2.103 35.454 1.00 35.04 ? 134 ALA C C 1 ATOM 4709 O O . ALA C 1 135 ? 62.763 1.019 35.107 1.00 35.17 ? 134 ALA C O 1 ATOM 4710 C CB . ALA C 1 135 ? 61.592 3.132 37.023 1.00 34.43 ? 134 ALA C CB 1 ATOM 4711 N N . CYS C 1 136 ? 63.925 2.902 34.652 1.00 35.57 ? 135 CYS C N 1 ATOM 4712 C CA . CYS C 1 136 ? 64.147 2.629 33.231 1.00 35.07 ? 135 CYS C CA 1 ATOM 4713 C C . CYS C 1 136 ? 65.644 2.584 32.927 1.00 35.50 ? 135 CYS C C 1 ATOM 4714 O O . CYS C 1 136 ? 66.182 3.469 32.265 1.00 35.00 ? 135 CYS C O 1 ATOM 4715 C CB . CYS C 1 136 ? 63.448 3.697 32.392 1.00 34.48 ? 135 CYS C CB 1 ATOM 4716 S SG . CYS C 1 136 ? 61.657 3.729 32.671 1.00 35.06 ? 135 CYS C SG 1 ATOM 4717 N N . PRO C 1 137 ? 66.326 1.543 33.425 1.00 36.20 ? 136 PRO C N 1 ATOM 4718 C CA . PRO C 1 137 ? 67.770 1.476 33.242 1.00 37.40 ? 136 PRO C CA 1 ATOM 4719 C C . PRO C 1 137 ? 68.154 1.231 31.782 1.00 37.15 ? 136 PRO C C 1 ATOM 4720 O O . PRO C 1 137 ? 67.364 0.695 31.008 1.00 36.79 ? 136 PRO C O 1 ATOM 4721 C CB . PRO C 1 137 ? 68.192 0.301 34.136 1.00 38.49 ? 136 PRO C CB 1 ATOM 4722 C CG . PRO C 1 137 ? 66.968 -0.525 34.319 1.00 37.50 ? 136 PRO C CG 1 ATOM 4723 C CD . PRO C 1 137 ? 65.807 0.420 34.232 1.00 36.23 ? 136 PRO C CD 1 ATOM 4724 N N . TYR C 1 138 ? 69.354 1.663 31.422 1.00 37.91 ? 137 TYR C N 1 ATOM 4725 C CA . TYR C 1 138 ? 69.915 1.450 30.095 1.00 37.52 ? 137 TYR C CA 1 ATOM 4726 C C . TYR C 1 138 ? 71.401 1.619 30.213 1.00 38.68 ? 137 TYR C C 1 ATOM 4727 O O . TYR C 1 138 ? 71.888 2.701 30.547 1.00 39.04 ? 137 TYR C O 1 ATOM 4728 C CB . TYR C 1 138 ? 69.373 2.458 29.083 1.00 36.96 ? 137 TYR C CB 1 ATOM 4729 C CG . TYR C 1 138 ? 69.937 2.273 27.697 1.00 37.59 ? 137 TYR C CG 1 ATOM 4730 C CD1 . TYR C 1 138 ? 69.558 1.190 26.911 1.00 37.33 ? 137 TYR C CD1 1 ATOM 4731 C CD2 . TYR C 1 138 ? 70.860 3.170 27.172 1.00 39.66 ? 137 TYR C CD2 1 ATOM 4732 C CE1 . TYR C 1 138 ? 70.078 1.005 25.637 1.00 38.35 ? 137 TYR C CE1 1 ATOM 4733 C CE2 . TYR C 1 138 ? 71.401 2.988 25.898 1.00 40.47 ? 137 TYR C CE2 1 ATOM 4734 C CZ . TYR C 1 138 ? 70.999 1.910 25.134 1.00 39.60 ? 137 TYR C CZ 1 ATOM 4735 O OH . TYR C 1 138 ? 71.510 1.734 23.874 1.00 40.90 ? 137 TYR C OH 1 ATOM 4736 N N . GLN C 1 139 ? 72.117 0.524 29.976 1.00 39.11 ? 138 GLN C N 1 ATOM 4737 C CA . GLN C 1 139 ? 73.555 0.538 29.879 1.00 40.44 ? 138 GLN C CA 1 ATOM 4738 C C . GLN C 1 139 ? 74.196 1.218 31.092 1.00 41.84 ? 138 GLN C C 1 ATOM 4739 O O . GLN C 1 139 ? 75.103 2.043 30.976 1.00 43.82 ? 138 GLN C O 1 ATOM 4740 C CB . GLN C 1 139 ? 73.961 1.184 28.552 1.00 40.40 ? 138 GLN C CB 1 ATOM 4741 C CG . GLN C 1 139 ? 73.469 0.396 27.341 1.00 39.19 ? 138 GLN C CG 1 ATOM 4742 C CD . GLN C 1 139 ? 74.217 0.716 26.051 1.00 40.05 ? 138 GLN C CD 1 ATOM 4743 O OE1 . GLN C 1 139 ? 74.743 1.814 25.868 1.00 40.62 ? 138 GLN C OE1 1 ATOM 4744 N NE2 . GLN C 1 139 ? 74.251 -0.242 25.146 1.00 40.12 ? 138 GLN C NE2 1 ATOM 4745 N N . GLY C 1 140 ? 73.708 0.846 32.266 1.00 41.53 ? 139 GLY C N 1 ATOM 4746 C CA . GLY C 1 140 ? 74.252 1.328 33.529 1.00 42.59 ? 139 GLY C CA 1 ATOM 4747 C C . GLY C 1 140 ? 73.669 2.625 34.060 1.00 41.53 ? 139 GLY C C 1 ATOM 4748 O O . GLY C 1 140 ? 74.069 3.077 35.124 1.00 42.95 ? 139 GLY C O 1 ATOM 4749 N N . ARG C 1 141 ? 72.727 3.241 33.352 1.00 39.55 ? 140 ARG C N 1 ATOM 4750 C CA . ARG C 1 141 ? 72.234 4.545 33.792 1.00 38.56 ? 140 ARG C CA 1 ATOM 4751 C C . ARG C 1 141 ? 70.723 4.633 33.740 1.00 36.55 ? 140 ARG C C 1 ATOM 4752 O O . ARG C 1 141 ? 70.049 3.752 33.230 1.00 35.38 ? 140 ARG C O 1 ATOM 4753 C CB . ARG C 1 141 ? 72.872 5.688 32.988 1.00 38.92 ? 140 ARG C CB 1 ATOM 4754 C CG . ARG C 1 141 ? 72.421 5.777 31.534 1.00 37.54 ? 140 ARG C CG 1 ATOM 4755 C CD . ARG C 1 141 ? 72.890 7.069 30.889 1.00 38.22 ? 140 ARG C CD 1 ATOM 4756 N NE . ARG C 1 141 ? 72.363 7.202 29.541 1.00 37.10 ? 140 ARG C NE 1 ATOM 4757 C CZ . ARG C 1 141 ? 72.891 6.648 28.449 1.00 37.58 ? 140 ARG C CZ 1 ATOM 4758 N NH1 . ARG C 1 141 ? 73.988 5.903 28.519 1.00 39.03 ? 140 ARG C NH1 1 ATOM 4759 N NH2 . ARG C 1 141 ? 72.300 6.833 27.273 1.00 36.52 ? 140 ARG C NH2 1 ATOM 4760 N N . SER C 1 142 ? 70.209 5.716 34.305 1.00 36.46 ? 141 SER C N 1 ATOM 4761 C CA . SER C 1 142 ? 68.813 6.010 34.269 1.00 34.83 ? 141 SER C CA 1 ATOM 4762 C C . SER C 1 142 ? 68.471 6.549 32.885 1.00 34.90 ? 141 SER C C 1 ATOM 4763 O O . SER C 1 142 ? 69.200 7.362 32.311 1.00 35.84 ? 141 SER C O 1 ATOM 4764 C CB . SER C 1 142 ? 68.440 7.013 35.364 1.00 35.08 ? 141 SER C CB 1 ATOM 4765 O OG . SER C 1 142 ? 68.547 6.420 36.652 1.00 35.28 ? 141 SER C OG 1 ATOM 4766 N N . SER C 1 143 ? 67.350 6.070 32.357 1.00 34.06 ? 142 SER C N 1 ATOM 4767 C CA . SER C 1 143 ? 66.877 6.434 31.034 1.00 33.94 ? 142 SER C CA 1 ATOM 4768 C C . SER C 1 143 ? 65.353 6.522 31.092 1.00 32.84 ? 142 SER C C 1 ATOM 4769 O O . SER C 1 143 ? 64.781 6.793 32.150 1.00 32.02 ? 142 SER C O 1 ATOM 4770 C CB . SER C 1 143 ? 67.356 5.403 30.002 1.00 34.23 ? 142 SER C CB 1 ATOM 4771 O OG . SER C 1 143 ? 66.813 5.661 28.719 1.00 33.78 ? 142 SER C OG 1 ATOM 4772 N N . PHE C 1 144 ? 64.705 6.298 29.960 1.00 32.48 ? 143 PHE C N 1 ATOM 4773 C CA . PHE C 1 144 ? 63.281 6.531 29.833 1.00 32.29 ? 143 PHE C CA 1 ATOM 4774 C C . PHE C 1 144 ? 62.778 5.979 28.501 1.00 31.79 ? 143 PHE C C 1 ATOM 4775 O O . PHE C 1 144 ? 63.567 5.557 27.660 1.00 32.66 ? 143 PHE C O 1 ATOM 4776 C CB . PHE C 1 144 ? 62.998 8.038 29.936 1.00 32.62 ? 143 PHE C CB 1 ATOM 4777 C CG . PHE C 1 144 ? 61.545 8.375 30.070 1.00 31.90 ? 143 PHE C CG 1 ATOM 4778 C CD1 . PHE C 1 144 ? 60.834 7.979 31.191 1.00 32.05 ? 143 PHE C CD1 1 ATOM 4779 C CD2 . PHE C 1 144 ? 60.888 9.085 29.078 1.00 31.72 ? 143 PHE C CD2 1 ATOM 4780 C CE1 . PHE C 1 144 ? 59.485 8.281 31.325 1.00 31.32 ? 143 PHE C CE1 1 ATOM 4781 C CE2 . PHE C 1 144 ? 59.544 9.394 29.206 1.00 31.55 ? 143 PHE C CE2 1 ATOM 4782 C CZ . PHE C 1 144 ? 58.840 8.990 30.333 1.00 30.94 ? 143 PHE C CZ 1 ATOM 4783 N N . PHE C 1 145 ? 61.462 5.968 28.329 1.00 31.74 ? 144 PHE C N 1 ATOM 4784 C CA . PHE C 1 145 ? 60.835 5.616 27.049 1.00 30.93 ? 144 PHE C CA 1 ATOM 4785 C C . PHE C 1 145 ? 61.397 6.476 25.930 1.00 32.15 ? 144 PHE C C 1 ATOM 4786 O O . PHE C 1 145 ? 61.431 7.699 26.047 1.00 33.67 ? 144 PHE C O 1 ATOM 4787 C CB . PHE C 1 145 ? 59.324 5.830 27.124 1.00 29.37 ? 144 PHE C CB 1 ATOM 4788 C CG . PHE C 1 145 ? 58.653 5.007 28.169 1.00 28.65 ? 144 PHE C CG 1 ATOM 4789 C CD1 . PHE C 1 145 ? 58.539 3.637 28.019 1.00 28.38 ? 144 PHE C CD1 1 ATOM 4790 C CD2 . PHE C 1 145 ? 58.152 5.602 29.328 1.00 29.25 ? 144 PHE C CD2 1 ATOM 4791 C CE1 . PHE C 1 145 ? 57.922 2.872 28.996 1.00 28.25 ? 144 PHE C CE1 1 ATOM 4792 C CE2 . PHE C 1 145 ? 57.537 4.848 30.312 1.00 28.77 ? 144 PHE C CE2 1 ATOM 4793 C CZ . PHE C 1 145 ? 57.430 3.474 30.146 1.00 28.72 ? 144 PHE C CZ 1 ATOM 4794 N N . ARG C 1 146 ? 61.823 5.834 24.844 1.00 32.60 ? 145 ARG C N 1 ATOM 4795 C CA . ARG C 1 146 ? 62.466 6.526 23.721 1.00 33.40 ? 145 ARG C CA 1 ATOM 4796 C C . ARG C 1 146 ? 61.522 7.373 22.861 1.00 31.26 ? 145 ARG C C 1 ATOM 4797 O O . ARG C 1 146 ? 61.940 8.364 22.276 1.00 31.51 ? 145 ARG C O 1 ATOM 4798 C CB . ARG C 1 146 ? 63.145 5.504 22.813 1.00 35.32 ? 145 ARG C CB 1 ATOM 4799 C CG . ARG C 1 146 ? 64.245 4.708 23.492 1.00 38.01 ? 145 ARG C CG 1 ATOM 4800 C CD . ARG C 1 146 ? 65.613 5.052 22.949 1.00 41.50 ? 145 ARG C CD 1 ATOM 4801 N NE . ARG C 1 146 ? 66.584 4.073 23.425 1.00 44.83 ? 145 ARG C NE 1 ATOM 4802 C CZ . ARG C 1 146 ? 67.535 4.296 24.333 1.00 45.80 ? 145 ARG C CZ 1 ATOM 4803 N NH1 . ARG C 1 146 ? 67.725 5.489 24.892 1.00 46.26 ? 145 ARG C NH1 1 ATOM 4804 N NH2 . ARG C 1 146 ? 68.320 3.301 24.681 1.00 47.22 ? 145 ARG C NH2 1 ATOM 4805 N N . ASN C 1 147 ? 60.260 6.978 22.762 1.00 29.30 ? 146 ASN C N 1 ATOM 4806 C CA . ASN C 1 147 ? 59.363 7.597 21.785 1.00 28.61 ? 146 ASN C CA 1 ATOM 4807 C C . ASN C 1 147 ? 58.611 8.811 22.306 1.00 27.92 ? 146 ASN C C 1 ATOM 4808 O O . ASN C 1 147 ? 58.004 9.545 21.531 1.00 28.24 ? 146 ASN C O 1 ATOM 4809 C CB . ASN C 1 147 ? 58.441 6.541 21.185 1.00 27.73 ? 146 ASN C CB 1 ATOM 4810 C CG . ASN C 1 147 ? 59.224 5.451 20.464 1.00 28.07 ? 146 ASN C CG 1 ATOM 4811 O OD1 . ASN C 1 147 ? 60.073 5.740 19.633 1.00 29.28 ? 146 ASN C OD1 1 ATOM 4812 N ND2 . ASN C 1 147 ? 58.965 4.203 20.800 1.00 28.00 ? 146 ASN C ND2 1 ATOM 4813 N N . VAL C 1 148 ? 58.692 9.031 23.615 1.00 27.77 ? 147 VAL C N 1 ATOM 4814 C CA . VAL C 1 148 ? 58.139 10.211 24.254 1.00 28.12 ? 147 VAL C CA 1 ATOM 4815 C C . VAL C 1 148 ? 59.227 10.895 25.069 1.00 29.71 ? 147 VAL C C 1 ATOM 4816 O O . VAL C 1 148 ? 60.227 10.260 25.408 1.00 30.82 ? 147 VAL C O 1 ATOM 4817 C CB . VAL C 1 148 ? 56.940 9.858 25.157 1.00 27.30 ? 147 VAL C CB 1 ATOM 4818 C CG1 . VAL C 1 148 ? 55.735 9.479 24.315 1.00 26.75 ? 147 VAL C CG1 1 ATOM 4819 C CG2 . VAL C 1 148 ? 57.281 8.713 26.104 1.00 27.36 ? 147 VAL C CG2 1 ATOM 4820 N N . VAL C 1 149 ? 59.030 12.180 25.374 1.00 30.62 ? 148 VAL C N 1 ATOM 4821 C CA . VAL C 1 149 ? 60.002 12.990 26.136 1.00 31.97 ? 148 VAL C CA 1 ATOM 4822 C C . VAL C 1 149 ? 59.419 13.518 27.461 1.00 31.72 ? 148 VAL C C 1 ATOM 4823 O O . VAL C 1 149 ? 58.385 14.188 27.477 1.00 31.62 ? 148 VAL C O 1 ATOM 4824 C CB . VAL C 1 149 ? 60.482 14.192 25.305 1.00 33.41 ? 148 VAL C CB 1 ATOM 4825 C CG1 . VAL C 1 149 ? 61.522 14.988 26.066 1.00 35.42 ? 148 VAL C CG1 1 ATOM 4826 C CG2 . VAL C 1 149 ? 61.069 13.720 23.996 1.00 34.21 ? 148 VAL C CG2 1 ATOM 4827 N N . TRP C 1 150 ? 60.094 13.226 28.569 1.00 31.39 ? 149 TRP C N 1 ATOM 4828 C CA . TRP C 1 150 ? 59.672 13.713 29.882 1.00 31.09 ? 149 TRP C CA 1 ATOM 4829 C C . TRP C 1 150 ? 60.279 15.094 30.124 1.00 32.30 ? 149 TRP C C 1 ATOM 4830 O O . TRP C 1 150 ? 61.443 15.219 30.539 1.00 33.07 ? 149 TRP C O 1 ATOM 4831 C CB . TRP C 1 150 ? 60.113 12.726 30.951 1.00 31.15 ? 149 TRP C CB 1 ATOM 4832 C CG . TRP C 1 150 ? 59.704 13.036 32.336 1.00 31.77 ? 149 TRP C CG 1 ATOM 4833 C CD1 . TRP C 1 150 ? 59.053 14.147 32.781 1.00 32.70 ? 149 TRP C CD1 1 ATOM 4834 C CD2 . TRP C 1 150 ? 59.948 12.224 33.486 1.00 32.50 ? 149 TRP C CD2 1 ATOM 4835 N NE1 . TRP C 1 150 ? 58.851 14.064 34.138 1.00 33.52 ? 149 TRP C NE1 1 ATOM 4836 C CE2 . TRP C 1 150 ? 59.395 12.896 34.598 1.00 33.39 ? 149 TRP C CE2 1 ATOM 4837 C CE3 . TRP C 1 150 ? 60.578 10.990 33.686 1.00 32.71 ? 149 TRP C CE3 1 ATOM 4838 C CZ2 . TRP C 1 150 ? 59.461 12.379 35.907 1.00 34.26 ? 149 TRP C CZ2 1 ATOM 4839 C CZ3 . TRP C 1 150 ? 60.643 10.468 34.988 1.00 33.65 ? 149 TRP C CZ3 1 ATOM 4840 C CH2 . TRP C 1 150 ? 60.080 11.168 36.081 1.00 34.32 ? 149 TRP C CH2 1 ATOM 4841 N N . LEU C 1 151 ? 59.487 16.125 29.848 1.00 31.77 ? 150 LEU C N 1 ATOM 4842 C CA . LEU C 1 151 ? 59.931 17.497 29.984 1.00 33.74 ? 150 LEU C CA 1 ATOM 4843 C C . LEU C 1 151 ? 59.826 17.960 31.432 1.00 35.13 ? 150 LEU C C 1 ATOM 4844 O O . LEU C 1 151 ? 58.834 17.691 32.098 1.00 34.96 ? 150 LEU C O 1 ATOM 4845 C CB . LEU C 1 151 ? 59.097 18.422 29.095 1.00 33.77 ? 150 LEU C CB 1 ATOM 4846 C CG . LEU C 1 151 ? 59.188 18.280 27.570 1.00 33.12 ? 150 LEU C CG 1 ATOM 4847 C CD1 . LEU C 1 151 ? 58.297 19.321 26.925 1.00 33.57 ? 150 LEU C CD1 1 ATOM 4848 C CD2 . LEU C 1 151 ? 60.608 18.444 27.053 1.00 34.29 ? 150 LEU C CD2 1 ATOM 4849 N N . ILE C 1 152 ? 60.865 18.639 31.913 1.00 37.04 ? 151 ILE C N 1 ATOM 4850 C CA . ILE C 1 152 ? 60.858 19.263 33.239 1.00 38.66 ? 151 ILE C CA 1 ATOM 4851 C C . ILE C 1 152 ? 61.272 20.729 33.123 1.00 40.83 ? 151 ILE C C 1 ATOM 4852 O O . ILE C 1 152 ? 61.620 21.191 32.040 1.00 41.25 ? 151 ILE C O 1 ATOM 4853 C CB . ILE C 1 152 ? 61.764 18.518 34.238 1.00 38.91 ? 151 ILE C CB 1 ATOM 4854 C CG1 . ILE C 1 152 ? 63.227 18.600 33.812 1.00 40.05 ? 151 ILE C CG1 1 ATOM 4855 C CG2 . ILE C 1 152 ? 61.302 17.076 34.389 1.00 37.02 ? 151 ILE C CG2 1 ATOM 4856 C CD1 . ILE C 1 152 ? 64.187 18.146 34.884 1.00 41.37 ? 151 ILE C CD1 1 ATOM 4857 N N . LYS C 1 153 ? 61.232 21.457 34.231 1.00 43.02 ? 152 LYS C N 1 ATOM 4858 C CA . LYS C 1 153 ? 61.423 22.906 34.181 1.00 45.73 ? 152 LYS C CA 1 ATOM 4859 C C . LYS C 1 153 ? 62.858 23.311 33.856 1.00 48.31 ? 152 LYS C C 1 ATOM 4860 O O . LYS C 1 153 ? 63.802 22.550 34.061 1.00 49.12 ? 152 LYS C O 1 ATOM 4861 C CB . LYS C 1 153 ? 60.966 23.556 35.484 1.00 47.11 ? 152 LYS C CB 1 ATOM 4862 C CG . LYS C 1 153 ? 61.806 23.218 36.693 1.00 48.24 ? 152 LYS C CG 1 ATOM 4863 C CD . LYS C 1 153 ? 61.366 24.044 37.886 1.00 49.96 ? 152 LYS C CD 1 ATOM 4864 C CE . LYS C 1 153 ? 62.333 23.889 39.039 1.00 51.09 ? 152 LYS C CE 1 ATOM 4865 N NZ . LYS C 1 153 ? 61.641 24.183 40.318 1.00 52.09 ? 152 LYS C NZ 1 ATOM 4866 N N . LYS C 1 154 ? 63.006 24.526 33.348 1.00 50.86 ? 153 LYS C N 1 ATOM 4867 C CA . LYS C 1 154 ? 64.291 25.033 32.907 1.00 53.11 ? 153 LYS C CA 1 ATOM 4868 C C . LYS C 1 154 ? 64.444 26.415 33.498 1.00 56.80 ? 153 LYS C C 1 ATOM 4869 O O . LYS C 1 154 ? 63.600 27.283 33.263 1.00 57.68 ? 153 LYS C O 1 ATOM 4870 C CB . LYS C 1 154 ? 64.343 25.084 31.376 1.00 53.16 ? 153 LYS C CB 1 ATOM 4871 C CG . LYS C 1 154 ? 65.568 25.778 30.810 1.00 55.80 ? 153 LYS C CG 1 ATOM 4872 C CD . LYS C 1 154 ? 65.959 25.253 29.437 1.00 55.52 ? 153 LYS C CD 1 ATOM 4873 C CE . LYS C 1 154 ? 67.181 25.999 28.916 1.00 58.33 ? 153 LYS C CE 1 ATOM 4874 N NZ . LYS C 1 154 ? 67.543 25.628 27.522 1.00 58.14 ? 153 LYS C NZ 1 ATOM 4875 N N . ASP C 1 155 ? 65.505 26.593 34.291 1.00 59.04 ? 154 ASP C N 1 ATOM 4876 C CA . ASP C 1 155 ? 65.799 27.844 34.979 1.00 61.96 ? 154 ASP C CA 1 ATOM 4877 C C . ASP C 1 155 ? 64.649 28.277 35.888 1.00 61.01 ? 154 ASP C C 1 ATOM 4878 O O . ASP C 1 155 ? 64.263 29.446 35.911 1.00 62.18 ? 154 ASP C O 1 ATOM 4879 C CB . ASP C 1 155 ? 66.161 28.940 33.965 1.00 65.00 ? 154 ASP C CB 1 ATOM 4880 C CG . ASP C 1 155 ? 67.221 28.483 32.961 1.00 65.82 ? 154 ASP C CG 1 ATOM 4881 O OD1 . ASP C 1 155 ? 68.306 28.037 33.402 1.00 67.39 ? 154 ASP C OD1 1 ATOM 4882 O OD2 . ASP C 1 155 ? 66.970 28.573 31.734 1.00 65.25 ? 154 ASP C OD2 1 ATOM 4883 N N . ASN C 1 156 ? 64.122 27.315 36.641 1.00 58.92 ? 155 ASN C N 1 ATOM 4884 C CA . ASN C 1 156 ? 63.027 27.542 37.598 1.00 59.00 ? 155 ASN C CA 1 ATOM 4885 C C . ASN C 1 156 ? 61.755 28.124 36.967 1.00 58.03 ? 155 ASN C C 1 ATOM 4886 O O . ASN C 1 156 ? 61.020 28.885 37.603 1.00 59.95 ? 155 ASN C O 1 ATOM 4887 C CB . ASN C 1 156 ? 63.505 28.409 38.771 1.00 62.09 ? 155 ASN C CB 1 ATOM 4888 C CG . ASN C 1 156 ? 64.566 27.717 39.611 1.00 63.13 ? 155 ASN C CG 1 ATOM 4889 O OD1 . ASN C 1 156 ? 64.494 26.512 39.854 1.00 61.79 ? 155 ASN C OD1 1 ATOM 4890 N ND2 . ASN C 1 156 ? 65.556 28.476 40.061 1.00 66.03 ? 155 ASN C ND2 1 ATOM 4891 N N . ALA C 1 157 ? 61.505 27.754 35.716 1.00 55.46 ? 156 ALA C N 1 ATOM 4892 C CA . ALA C 1 157 ? 60.298 28.161 35.012 1.00 54.30 ? 156 ALA C CA 1 ATOM 4893 C C . ALA C 1 157 ? 59.848 27.056 34.062 1.00 51.03 ? 156 ALA C C 1 ATOM 4894 O O . ALA C 1 157 ? 60.674 26.356 33.475 1.00 49.68 ? 156 ALA C O 1 ATOM 4895 C CB . ALA C 1 157 ? 60.541 29.450 34.245 1.00 56.13 ? 156 ALA C CB 1 ATOM 4896 N N . TYR C 1 158 ? 58.532 26.903 33.939 1.00 49.64 ? 157 TYR C N 1 ATOM 4897 C CA . TYR C 1 158 ? 57.925 25.995 32.977 1.00 47.31 ? 157 TYR C CA 1 ATOM 4898 C C . TYR C 1 158 ? 56.823 26.772 32.244 1.00 47.83 ? 157 TYR C C 1 ATOM 4899 O O . TYR C 1 158 ? 55.658 26.724 32.637 1.00 47.70 ? 157 TYR C O 1 ATOM 4900 C CB . TYR C 1 158 ? 57.379 24.750 33.702 1.00 45.16 ? 157 TYR C CB 1 ATOM 4901 C CG . TYR C 1 158 ? 56.974 23.569 32.822 1.00 41.97 ? 157 TYR C CG 1 ATOM 4902 C CD1 . TYR C 1 158 ? 55.938 23.668 31.907 1.00 41.06 ? 157 TYR C CD1 1 ATOM 4903 C CD2 . TYR C 1 158 ? 57.616 22.340 32.937 1.00 40.85 ? 157 TYR C CD2 1 ATOM 4904 C CE1 . TYR C 1 158 ? 55.565 22.585 31.122 1.00 38.91 ? 157 TYR C CE1 1 ATOM 4905 C CE2 . TYR C 1 158 ? 57.248 21.248 32.155 1.00 38.38 ? 157 TYR C CE2 1 ATOM 4906 C CZ . TYR C 1 158 ? 56.220 21.374 31.252 1.00 37.59 ? 157 TYR C CZ 1 ATOM 4907 O OH . TYR C 1 158 ? 55.841 20.296 30.470 1.00 35.43 ? 157 TYR C OH 1 ATOM 4908 N N . PRO C 1 159 ? 57.199 27.526 31.192 1.00 49.09 ? 158 PRO C N 1 ATOM 4909 C CA . PRO C 1 159 ? 56.235 28.245 30.357 1.00 49.26 ? 158 PRO C CA 1 ATOM 4910 C C . PRO C 1 159 ? 55.153 27.343 29.818 1.00 46.64 ? 158 PRO C C 1 ATOM 4911 O O . PRO C 1 159 ? 55.337 26.130 29.754 1.00 44.58 ? 158 PRO C O 1 ATOM 4912 C CB . PRO C 1 159 ? 57.087 28.752 29.199 1.00 50.17 ? 158 PRO C CB 1 ATOM 4913 C CG . PRO C 1 159 ? 58.406 28.980 29.820 1.00 52.06 ? 158 PRO C CG 1 ATOM 4914 C CD . PRO C 1 159 ? 58.582 27.876 30.828 1.00 50.55 ? 158 PRO C CD 1 ATOM 4915 N N . THR C 1 160 ? 54.031 27.932 29.434 1.00 47.01 ? 159 THR C N 1 ATOM 4916 C CA . THR C 1 160 ? 52.953 27.151 28.879 1.00 45.45 ? 159 THR C CA 1 ATOM 4917 C C . THR C 1 160 ? 53.360 26.701 27.482 1.00 44.48 ? 159 THR C C 1 ATOM 4918 O O . THR C 1 160 ? 53.737 27.512 26.632 1.00 45.31 ? 159 THR C O 1 ATOM 4919 C CB . THR C 1 160 ? 51.635 27.933 28.842 1.00 46.41 ? 159 THR C CB 1 ATOM 4920 O OG1 . THR C 1 160 ? 51.318 28.370 30.166 1.00 47.48 ? 159 THR C OG1 1 ATOM 4921 C CG2 . THR C 1 160 ? 50.500 27.049 28.308 1.00 44.60 ? 159 THR C CG2 1 ATOM 4922 N N . ILE C 1 161 ? 53.315 25.394 27.274 1.00 42.69 ? 160 ILE C N 1 ATOM 4923 C CA . ILE C 1 161 ? 53.610 24.823 25.990 1.00 42.28 ? 160 ILE C CA 1 ATOM 4924 C C . ILE C 1 161 ? 52.383 25.001 25.123 1.00 43.33 ? 160 ILE C C 1 ATOM 4925 O O . ILE C 1 161 ? 51.266 24.781 25.575 1.00 43.10 ? 160 ILE C O 1 ATOM 4926 C CB . ILE C 1 161 ? 53.964 23.326 26.118 1.00 40.36 ? 160 ILE C CB 1 ATOM 4927 C CG1 . ILE C 1 161 ? 55.375 23.178 26.705 1.00 40.41 ? 160 ILE C CG1 1 ATOM 4928 C CG2 . ILE C 1 161 ? 53.857 22.623 24.769 1.00 38.99 ? 160 ILE C CG2 1 ATOM 4929 C CD1 . ILE C 1 161 ? 55.701 21.776 27.186 1.00 38.80 ? 160 ILE C CD1 1 ATOM 4930 N N . LYS C 1 162 ? 52.603 25.429 23.884 1.00 45.47 ? 161 LYS C N 1 ATOM 4931 C CA . LYS C 1 162 ? 51.567 25.440 22.861 1.00 46.33 ? 161 LYS C CA 1 ATOM 4932 C C . LYS C 1 162 ? 52.206 24.939 21.573 1.00 47.11 ? 161 LYS C C 1 ATOM 4933 O O . LYS C 1 162 ? 52.887 25.703 20.879 1.00 48.53 ? 161 LYS C O 1 ATOM 4934 C CB . LYS C 1 162 ? 51.004 26.849 22.672 1.00 48.14 ? 161 LYS C CB 1 ATOM 4935 C CG . LYS C 1 162 ? 50.095 27.302 23.804 1.00 49.06 ? 161 LYS C CG 1 ATOM 4936 C CD . LYS C 1 162 ? 49.766 28.784 23.714 1.00 51.38 ? 161 LYS C CD 1 ATOM 4937 C CE . LYS C 1 162 ? 48.643 29.155 24.670 1.00 52.36 ? 161 LYS C CE 1 ATOM 4938 N NZ . LYS C 1 162 ? 48.542 30.630 24.892 1.00 55.04 ? 161 LYS C NZ 1 ATOM 4939 N N . ARG C 1 163 ? 52.000 23.654 21.273 1.00 46.32 ? 162 ARG C N 1 ATOM 4940 C CA . ARG C 1 163 ? 52.655 23.000 20.138 1.00 47.00 ? 162 ARG C CA 1 ATOM 4941 C C . ARG C 1 163 ? 51.662 22.212 19.301 1.00 44.66 ? 162 ARG C C 1 ATOM 4942 O O . ARG C 1 163 ? 50.853 21.463 19.838 1.00 43.24 ? 162 ARG C O 1 ATOM 4943 C CB . ARG C 1 163 ? 53.765 22.061 20.617 1.00 47.96 ? 162 ARG C CB 1 ATOM 4944 C CG . ARG C 1 163 ? 54.848 22.759 21.427 1.00 51.37 ? 162 ARG C CG 1 ATOM 4945 C CD . ARG C 1 163 ? 55.832 23.533 20.561 1.00 54.42 ? 162 ARG C CD 1 ATOM 4946 N NE . ARG C 1 163 ? 57.059 22.767 20.322 1.00 54.75 ? 162 ARG C NE 1 ATOM 4947 C CZ . ARG C 1 163 ? 57.337 22.067 19.225 1.00 53.86 ? 162 ARG C CZ 1 ATOM 4948 N NH1 . ARG C 1 163 ? 56.487 22.015 18.201 1.00 54.40 ? 162 ARG C NH1 1 ATOM 4949 N NH2 . ARG C 1 163 ? 58.490 21.415 19.152 1.00 53.40 ? 162 ARG C NH2 1 ATOM 4950 N N . SER C 1 164 ? 51.732 22.406 17.986 1.00 43.79 ? 163 SER C N 1 ATOM 4951 C CA . SER C 1 164 ? 50.931 21.661 17.023 1.00 41.42 ? 163 SER C CA 1 ATOM 4952 C C . SER C 1 164 ? 51.833 20.735 16.239 1.00 39.45 ? 163 SER C C 1 ATOM 4953 O O . SER C 1 164 ? 53.004 21.044 16.000 1.00 39.29 ? 163 SER C O 1 ATOM 4954 C CB . SER C 1 164 ? 50.265 22.591 16.011 1.00 42.10 ? 163 SER C CB 1 ATOM 4955 O OG . SER C 1 164 ? 49.410 23.510 16.631 1.00 43.78 ? 163 SER C OG 1 ATOM 4956 N N . TYR C 1 165 ? 51.264 19.603 15.846 1.00 37.34 ? 164 TYR C N 1 ATOM 4957 C CA . TYR C 1 165 ? 51.818 18.771 14.800 1.00 36.44 ? 164 TYR C CA 1 ATOM 4958 C C . TYR C 1 165 ? 50.707 18.453 13.792 1.00 36.14 ? 164 TYR C C 1 ATOM 4959 O O . TYR C 1 165 ? 49.675 17.894 14.146 1.00 34.32 ? 164 TYR C O 1 ATOM 4960 C CB . TYR C 1 165 ? 52.420 17.479 15.356 1.00 34.71 ? 164 TYR C CB 1 ATOM 4961 C CG . TYR C 1 165 ? 52.870 16.563 14.249 1.00 34.59 ? 164 TYR C CG 1 ATOM 4962 C CD1 . TYR C 1 165 ? 54.056 16.808 13.552 1.00 35.84 ? 164 TYR C CD1 1 ATOM 4963 C CD2 . TYR C 1 165 ? 52.090 15.482 13.855 1.00 33.33 ? 164 TYR C CD2 1 ATOM 4964 C CE1 . TYR C 1 165 ? 54.459 15.983 12.511 1.00 35.82 ? 164 TYR C CE1 1 ATOM 4965 C CE2 . TYR C 1 165 ? 52.489 14.657 12.827 1.00 33.46 ? 164 TYR C CE2 1 ATOM 4966 C CZ . TYR C 1 165 ? 53.664 14.911 12.153 1.00 35.11 ? 164 TYR C CZ 1 ATOM 4967 O OH . TYR C 1 165 ? 54.045 14.079 11.121 1.00 36.49 ? 164 TYR C OH 1 ATOM 4968 N N . ASN C 1 166 ? 50.940 18.823 12.539 1.00 37.59 ? 165 ASN C N 1 ATOM 4969 C CA . ASN C 1 166 ? 50.034 18.525 11.446 1.00 38.67 ? 165 ASN C CA 1 ATOM 4970 C C . ASN C 1 166 ? 50.547 17.328 10.656 1.00 36.89 ? 165 ASN C C 1 ATOM 4971 O O . ASN C 1 166 ? 51.599 17.395 10.036 1.00 37.33 ? 165 ASN C O 1 ATOM 4972 C CB . ASN C 1 166 ? 49.909 19.750 10.548 1.00 42.20 ? 165 ASN C CB 1 ATOM 4973 C CG . ASN C 1 166 ? 48.926 19.554 9.414 1.00 45.56 ? 165 ASN C CG 1 ATOM 4974 O OD1 . ASN C 1 166 ? 48.680 18.431 8.958 1.00 44.46 ? 165 ASN C OD1 1 ATOM 4975 N ND2 . ASN C 1 166 ? 48.356 20.669 8.945 1.00 50.49 ? 165 ASN C ND2 1 ATOM 4976 N N . ASN C 1 167 ? 49.802 16.228 10.692 1.00 35.19 ? 166 ASN C N 1 ATOM 4977 C CA . ASN C 1 167 ? 50.156 15.041 9.927 1.00 34.40 ? 166 ASN C CA 1 ATOM 4978 C C . ASN C 1 167 ? 50.082 15.297 8.419 1.00 35.90 ? 166 ASN C C 1 ATOM 4979 O O . ASN C 1 167 ? 49.022 15.141 7.797 1.00 36.08 ? 166 ASN C O 1 ATOM 4980 C CB . ASN C 1 167 ? 49.244 13.876 10.300 1.00 33.25 ? 166 ASN C CB 1 ATOM 4981 C CG . ASN C 1 167 ? 49.553 12.615 9.506 1.00 33.20 ? 166 ASN C CG 1 ATOM 4982 O OD1 . ASN C 1 167 ? 50.681 12.419 9.035 1.00 33.05 ? 166 ASN C OD1 1 ATOM 4983 N ND2 . ASN C 1 167 ? 48.551 11.757 9.349 1.00 32.62 ? 166 ASN C ND2 1 ATOM 4984 N N . THR C 1 168 ? 51.219 15.685 7.842 1.00 37.08 ? 167 THR C N 1 ATOM 4985 C CA . THR C 1 168 ? 51.326 15.983 6.408 1.00 38.75 ? 167 THR C CA 1 ATOM 4986 C C . THR C 1 168 ? 51.606 14.716 5.598 1.00 38.65 ? 167 THR C C 1 ATOM 4987 O O . THR C 1 168 ? 51.960 14.785 4.426 1.00 40.46 ? 167 THR C O 1 ATOM 4988 C CB . THR C 1 168 ? 52.428 17.035 6.141 1.00 40.60 ? 167 THR C CB 1 ATOM 4989 O OG1 . THR C 1 168 ? 53.596 16.718 6.908 1.00 41.38 ? 167 THR C OG1 1 ATOM 4990 C CG2 . THR C 1 168 ? 51.956 18.417 6.554 1.00 41.32 ? 167 THR C CG2 1 ATOM 4991 N N . ASN C 1 169 ? 51.419 13.558 6.223 1.00 37.63 ? 168 ASN C N 1 ATOM 4992 C CA . ASN C 1 169 ? 51.677 12.276 5.585 1.00 37.39 ? 168 ASN C CA 1 ATOM 4993 C C . ASN C 1 169 ? 50.398 11.701 5.010 1.00 37.18 ? 168 ASN C C 1 ATOM 4994 O O . ASN C 1 169 ? 49.297 12.037 5.448 1.00 36.86 ? 168 ASN C O 1 ATOM 4995 C CB . ASN C 1 169 ? 52.270 11.287 6.585 1.00 36.57 ? 168 ASN C CB 1 ATOM 4996 C CG . ASN C 1 169 ? 53.471 11.851 7.328 1.00 36.83 ? 168 ASN C CG 1 ATOM 4997 O OD1 . ASN C 1 169 ? 54.614 11.577 6.974 1.00 38.27 ? 168 ASN C OD1 1 ATOM 4998 N ND2 . ASN C 1 169 ? 53.217 12.658 8.345 1.00 36.25 ? 168 ASN C ND2 1 ATOM 4999 N N . GLN C 1 170 ? 50.570 10.832 4.021 1.00 37.66 ? 169 GLN C N 1 ATOM 5000 C CA . GLN C 1 170 ? 49.482 10.115 3.386 1.00 37.76 ? 169 GLN C CA 1 ATOM 5001 C C . GLN C 1 170 ? 48.870 9.060 4.315 1.00 35.82 ? 169 GLN C C 1 ATOM 5002 O O . GLN C 1 170 ? 47.726 8.650 4.121 1.00 34.79 ? 169 GLN C O 1 ATOM 5003 C CB . GLN C 1 170 ? 49.997 9.414 2.120 1.00 39.84 ? 169 GLN C CB 1 ATOM 5004 C CG . GLN C 1 170 ? 50.678 10.323 1.109 1.00 41.84 ? 169 GLN C CG 1 ATOM 5005 C CD . GLN C 1 170 ? 49.833 11.527 0.735 1.00 43.02 ? 169 GLN C CD 1 ATOM 5006 O OE1 . GLN C 1 170 ? 50.294 12.673 0.779 1.00 43.67 ? 169 GLN C OE1 1 ATOM 5007 N NE2 . GLN C 1 170 ? 48.583 11.274 0.386 1.00 43.09 ? 169 GLN C NE2 1 ATOM 5008 N N . GLU C 1 171 ? 49.633 8.647 5.328 1.00 35.04 ? 170 GLU C N 1 ATOM 5009 C CA . GLU C 1 171 ? 49.251 7.548 6.223 1.00 34.22 ? 170 GLU C CA 1 ATOM 5010 C C . GLU C 1 171 ? 48.570 8.040 7.501 1.00 33.38 ? 170 GLU C C 1 ATOM 5011 O O . GLU C 1 171 ? 48.827 9.161 7.962 1.00 33.41 ? 170 GLU C O 1 ATOM 5012 C CB . GLU C 1 171 ? 50.497 6.714 6.591 1.00 33.87 ? 170 GLU C CB 1 ATOM 5013 C CG . GLU C 1 171 ? 51.269 6.129 5.398 1.00 35.16 ? 170 GLU C CG 1 ATOM 5014 C CD . GLU C 1 171 ? 52.404 7.014 4.875 1.00 36.35 ? 170 GLU C CD 1 ATOM 5015 O OE1 . GLU C 1 171 ? 52.388 8.256 5.084 1.00 36.66 ? 170 GLU C OE1 1 ATOM 5016 O OE2 . GLU C 1 171 ? 53.328 6.468 4.238 1.00 36.89 ? 170 GLU C OE2 1 ATOM 5017 N N . ASP C 1 172 ? 47.704 7.196 8.069 1.00 33.14 ? 171 ASP C N 1 ATOM 5018 C CA . ASP C 1 172 ? 47.249 7.360 9.461 1.00 32.45 ? 171 ASP C CA 1 ATOM 5019 C C . ASP C 1 172 ? 48.430 7.275 10.427 1.00 31.53 ? 171 ASP C C 1 ATOM 5020 O O . ASP C 1 172 ? 49.337 6.458 10.247 1.00 31.44 ? 171 ASP C O 1 ATOM 5021 C CB . ASP C 1 172 ? 46.238 6.277 9.856 1.00 33.36 ? 171 ASP C CB 1 ATOM 5022 C CG . ASP C 1 172 ? 44.845 6.537 9.325 1.00 34.66 ? 171 ASP C CG 1 ATOM 5023 O OD1 . ASP C 1 172 ? 44.502 7.700 9.037 1.00 36.43 ? 171 ASP C OD1 1 ATOM 5024 O OD2 . ASP C 1 172 ? 44.077 5.560 9.210 1.00 36.69 ? 171 ASP C OD2 1 ATOM 5025 N N . LEU C 1 173 ? 48.394 8.103 11.464 1.00 30.55 ? 172 LEU C N 1 ATOM 5026 C CA . LEU C 1 173 ? 49.510 8.247 12.373 1.00 29.69 ? 172 LEU C CA 1 ATOM 5027 C C . LEU C 1 173 ? 49.083 7.930 13.791 1.00 28.75 ? 172 LEU C C 1 ATOM 5028 O O . LEU C 1 173 ? 48.146 8.554 14.313 1.00 28.63 ? 172 LEU C O 1 ATOM 5029 C CB . LEU C 1 173 ? 50.038 9.677 12.311 1.00 30.93 ? 172 LEU C CB 1 ATOM 5030 C CG . LEU C 1 173 ? 51.306 9.973 13.116 1.00 31.34 ? 172 LEU C CG 1 ATOM 5031 C CD1 . LEU C 1 173 ? 52.465 9.101 12.651 1.00 31.85 ? 172 LEU C CD1 1 ATOM 5032 C CD2 . LEU C 1 173 ? 51.666 11.445 13.002 1.00 32.22 ? 172 LEU C CD2 1 ATOM 5033 N N . LEU C 1 174 ? 49.771 6.965 14.405 1.00 27.43 ? 173 LEU C N 1 ATOM 5034 C CA . LEU C 1 174 ? 49.577 6.639 15.813 1.00 26.96 ? 173 LEU C CA 1 ATOM 5035 C C . LEU C 1 174 ? 50.472 7.504 16.721 1.00 26.14 ? 173 LEU C C 1 ATOM 5036 O O . LEU C 1 174 ? 51.674 7.266 16.840 1.00 25.85 ? 173 LEU C O 1 ATOM 5037 C CB . LEU C 1 174 ? 49.873 5.158 16.054 1.00 26.94 ? 173 LEU C CB 1 ATOM 5038 C CG . LEU C 1 174 ? 49.686 4.739 17.505 1.00 26.88 ? 173 LEU C CG 1 ATOM 5039 C CD1 . LEU C 1 174 ? 48.200 4.690 17.847 1.00 27.11 ? 173 LEU C CD1 1 ATOM 5040 C CD2 . LEU C 1 174 ? 50.362 3.399 17.743 1.00 27.35 ? 173 LEU C CD2 1 ATOM 5041 N N . VAL C 1 175 ? 49.875 8.505 17.352 1.00 25.66 ? 174 VAL C N 1 ATOM 5042 C CA . VAL C 1 175 ? 50.593 9.414 18.246 1.00 25.38 ? 174 VAL C CA 1 ATOM 5043 C C . VAL C 1 175 ? 50.417 8.955 19.699 1.00 24.76 ? 174 VAL C C 1 ATOM 5044 O O . VAL C 1 175 ? 49.339 8.541 20.092 1.00 24.11 ? 174 VAL C O 1 ATOM 5045 C CB . VAL C 1 175 ? 50.067 10.845 18.062 1.00 25.79 ? 174 VAL C CB 1 ATOM 5046 C CG1 . VAL C 1 175 ? 50.820 11.837 18.921 1.00 26.27 ? 174 VAL C CG1 1 ATOM 5047 C CG2 . VAL C 1 175 ? 50.145 11.232 16.600 1.00 26.50 ? 174 VAL C CG2 1 ATOM 5048 N N . LEU C 1 176 ? 51.492 9.034 20.478 1.00 24.90 ? 175 LEU C N 1 ATOM 5049 C CA . LEU C 1 176 ? 51.509 8.608 21.877 1.00 24.83 ? 175 LEU C CA 1 ATOM 5050 C C . LEU C 1 176 ? 51.984 9.759 22.754 1.00 25.11 ? 175 LEU C C 1 ATOM 5051 O O . LEU C 1 176 ? 52.928 10.468 22.408 1.00 25.69 ? 175 LEU C O 1 ATOM 5052 C CB . LEU C 1 176 ? 52.460 7.416 22.068 1.00 24.99 ? 175 LEU C CB 1 ATOM 5053 C CG . LEU C 1 176 ? 52.147 6.201 21.167 1.00 25.38 ? 175 LEU C CG 1 ATOM 5054 C CD1 . LEU C 1 176 ? 53.242 5.160 21.215 1.00 25.80 ? 175 LEU C CD1 1 ATOM 5055 C CD2 . LEU C 1 176 ? 50.819 5.581 21.547 1.00 25.15 ? 175 LEU C CD2 1 ATOM 5056 N N . TRP C 1 177 ? 51.349 9.914 23.907 1.00 24.98 ? 176 TRP C N 1 ATOM 5057 C CA . TRP C 1 177 ? 51.766 10.903 24.879 1.00 25.59 ? 176 TRP C CA 1 ATOM 5058 C C . TRP C 1 177 ? 51.369 10.461 26.280 1.00 25.86 ? 176 TRP C C 1 ATOM 5059 O O . TRP C 1 177 ? 50.660 9.479 26.451 1.00 25.75 ? 176 TRP C O 1 ATOM 5060 C CB . TRP C 1 177 ? 51.181 12.282 24.551 1.00 25.72 ? 176 TRP C CB 1 ATOM 5061 C CG . TRP C 1 177 ? 49.697 12.394 24.673 1.00 25.72 ? 176 TRP C CG 1 ATOM 5062 C CD1 . TRP C 1 177 ? 49.001 12.898 25.723 1.00 26.28 ? 176 TRP C CD1 1 ATOM 5063 C CD2 . TRP C 1 177 ? 48.724 12.035 23.684 1.00 25.95 ? 176 TRP C CD2 1 ATOM 5064 N NE1 . TRP C 1 177 ? 47.647 12.864 25.466 1.00 26.57 ? 176 TRP C NE1 1 ATOM 5065 C CE2 . TRP C 1 177 ? 47.450 12.332 24.223 1.00 26.34 ? 176 TRP C CE2 1 ATOM 5066 C CE3 . TRP C 1 177 ? 48.802 11.482 22.404 1.00 25.46 ? 176 TRP C CE3 1 ATOM 5067 C CZ2 . TRP C 1 177 ? 46.277 12.093 23.531 1.00 26.70 ? 176 TRP C CZ2 1 ATOM 5068 C CZ3 . TRP C 1 177 ? 47.626 11.238 21.713 1.00 26.19 ? 176 TRP C CZ3 1 ATOM 5069 C CH2 . TRP C 1 177 ? 46.378 11.547 22.280 1.00 26.52 ? 176 TRP C CH2 1 ATOM 5070 N N . GLY C 1 178 ? 51.855 11.170 27.284 1.00 26.33 ? 177 GLY C N 1 ATOM 5071 C CA . GLY C 1 178 ? 51.513 10.822 28.636 1.00 26.86 ? 177 GLY C CA 1 ATOM 5072 C C . GLY C 1 178 ? 51.405 12.012 29.541 1.00 27.75 ? 177 GLY C C 1 ATOM 5073 O O . GLY C 1 178 ? 51.549 13.156 29.130 1.00 27.84 ? 177 GLY C O 1 ATOM 5074 N N . ILE C 1 179 ? 51.135 11.698 30.797 1.00 28.91 ? 178 ILE C N 1 ATOM 5075 C CA . ILE C 1 179 ? 51.103 12.666 31.878 1.00 29.51 ? 178 ILE C CA 1 ATOM 5076 C C . ILE C 1 179 ? 51.817 12.024 33.049 1.00 29.36 ? 178 ILE C C 1 ATOM 5077 O O . ILE C 1 179 ? 51.661 10.820 33.286 1.00 28.85 ? 178 ILE C O 1 ATOM 5078 C CB . ILE C 1 179 ? 49.660 13.037 32.279 1.00 30.43 ? 178 ILE C CB 1 ATOM 5079 C CG1 . ILE C 1 179 ? 49.663 14.077 33.400 1.00 31.92 ? 178 ILE C CG1 1 ATOM 5080 C CG2 . ILE C 1 179 ? 48.872 11.813 32.732 1.00 30.28 ? 178 ILE C CG2 1 ATOM 5081 C CD1 . ILE C 1 179 ? 48.277 14.559 33.778 1.00 32.81 ? 178 ILE C CD1 1 ATOM 5082 N N . HIS C 1 180 ? 52.598 12.825 33.770 1.00 29.95 ? 179 HIS C N 1 ATOM 5083 C CA . HIS C 1 180 ? 53.241 12.377 35.004 1.00 30.14 ? 179 HIS C CA 1 ATOM 5084 C C . HIS C 1 180 ? 52.403 12.701 36.242 1.00 31.25 ? 179 HIS C C 1 ATOM 5085 O O . HIS C 1 180 ? 52.032 13.855 36.471 1.00 31.98 ? 179 HIS C O 1 ATOM 5086 C CB . HIS C 1 180 ? 54.613 13.022 35.143 1.00 30.82 ? 179 HIS C CB 1 ATOM 5087 C CG . HIS C 1 180 ? 55.338 12.614 36.383 1.00 31.67 ? 179 HIS C CG 1 ATOM 5088 N ND1 . HIS C 1 180 ? 55.879 13.524 37.262 1.00 32.87 ? 179 HIS C ND1 1 ATOM 5089 C CD2 . HIS C 1 180 ? 55.586 11.390 36.905 1.00 31.31 ? 179 HIS C CD2 1 ATOM 5090 C CE1 . HIS C 1 180 ? 56.441 12.878 38.267 1.00 33.61 ? 179 HIS C CE1 1 ATOM 5091 N NE2 . HIS C 1 180 ? 56.275 11.581 38.074 1.00 32.76 ? 179 HIS C NE2 1 ATOM 5092 N N . HIS C 1 181 ? 52.123 11.671 37.036 1.00 31.54 ? 180 HIS C N 1 ATOM 5093 C CA . HIS C 1 181 ? 51.454 11.808 38.323 1.00 32.66 ? 180 HIS C CA 1 ATOM 5094 C C . HIS C 1 181 ? 52.477 11.814 39.487 1.00 33.63 ? 180 HIS C C 1 ATOM 5095 O O . HIS C 1 181 ? 52.933 10.753 39.912 1.00 33.31 ? 180 HIS C O 1 ATOM 5096 C CB . HIS C 1 181 ? 50.468 10.650 38.511 1.00 32.48 ? 180 HIS C CB 1 ATOM 5097 C CG . HIS C 1 181 ? 49.372 10.600 37.484 1.00 31.82 ? 180 HIS C CG 1 ATOM 5098 N ND1 . HIS C 1 181 ? 48.490 11.639 37.284 1.00 32.07 ? 180 HIS C ND1 1 ATOM 5099 C CD2 . HIS C 1 181 ? 48.994 9.621 36.627 1.00 30.61 ? 180 HIS C CD2 1 ATOM 5100 C CE1 . HIS C 1 181 ? 47.630 11.313 36.339 1.00 31.28 ? 180 HIS C CE1 1 ATOM 5101 N NE2 . HIS C 1 181 ? 47.916 10.094 35.922 1.00 30.53 ? 180 HIS C NE2 1 ATOM 5102 N N . PRO C 1 182 ? 52.830 13.001 40.023 1.00 34.97 ? 181 PRO C N 1 ATOM 5103 C CA . PRO C 1 182 ? 53.842 13.034 41.102 1.00 36.59 ? 181 PRO C CA 1 ATOM 5104 C C . PRO C 1 182 ? 53.382 12.504 42.461 1.00 38.02 ? 181 PRO C C 1 ATOM 5105 O O . PRO C 1 182 ? 52.208 12.178 42.651 1.00 38.31 ? 181 PRO C O 1 ATOM 5106 C CB . PRO C 1 182 ? 54.206 14.522 41.220 1.00 37.49 ? 181 PRO C CB 1 ATOM 5107 C CG . PRO C 1 182 ? 53.495 15.214 40.106 1.00 36.84 ? 181 PRO C CG 1 ATOM 5108 C CD . PRO C 1 182 ? 52.347 14.350 39.702 1.00 35.66 ? 181 PRO C CD 1 ATOM 5109 N N . ASN C 1 183 ? 54.329 12.434 43.389 1.00 39.59 ? 182 ASN C N 1 ATOM 5110 C CA . ASN C 1 183 ? 54.113 11.870 44.718 1.00 41.49 ? 182 ASN C CA 1 ATOM 5111 C C . ASN C 1 183 ? 53.578 12.859 45.745 1.00 43.46 ? 182 ASN C C 1 ATOM 5112 O O . ASN C 1 183 ? 52.931 12.456 46.704 1.00 43.98 ? 182 ASN C O 1 ATOM 5113 C CB . ASN C 1 183 ? 55.431 11.323 45.246 1.00 42.47 ? 182 ASN C CB 1 ATOM 5114 C CG . ASN C 1 183 ? 55.968 10.212 44.395 1.00 41.66 ? 182 ASN C CG 1 ATOM 5115 O OD1 . ASN C 1 183 ? 55.343 9.163 44.274 1.00 41.51 ? 182 ASN C OD1 1 ATOM 5116 N ND2 . ASN C 1 183 ? 57.138 10.429 43.797 1.00 42.09 ? 182 ASN C ND2 1 ATOM 5117 N N . ASP C 1 184 ? 53.884 14.139 45.551 1.00 44.74 ? 183 ASP C N 1 ATOM 5118 C CA . ASP C 1 184 ? 53.503 15.195 46.483 1.00 47.50 ? 183 ASP C CA 1 ATOM 5119 C C . ASP C 1 184 ? 53.727 16.570 45.867 1.00 47.64 ? 183 ASP C C 1 ATOM 5120 O O . ASP C 1 184 ? 54.341 16.692 44.805 1.00 46.68 ? 183 ASP C O 1 ATOM 5121 C CB . ASP C 1 184 ? 54.283 15.073 47.805 1.00 50.04 ? 183 ASP C CB 1 ATOM 5122 C CG . ASP C 1 184 ? 55.794 14.976 47.607 1.00 50.45 ? 183 ASP C CG 1 ATOM 5123 O OD1 . ASP C 1 184 ? 56.366 15.760 46.822 1.00 50.96 ? 183 ASP C OD1 1 ATOM 5124 O OD2 . ASP C 1 184 ? 56.418 14.124 48.269 1.00 51.65 ? 183 ASP C OD2 1 ATOM 5125 N N . ALA C 1 185 ? 53.223 17.600 46.537 1.00 49.27 ? 184 ALA C N 1 ATOM 5126 C CA . ALA C 1 185 ? 53.352 18.981 46.066 1.00 50.15 ? 184 ALA C CA 1 ATOM 5127 C C . ALA C 1 185 ? 54.807 19.416 45.897 1.00 50.30 ? 184 ALA C C 1 ATOM 5128 O O . ALA C 1 185 ? 55.149 20.096 44.932 1.00 49.85 ? 184 ALA C O 1 ATOM 5129 C CB . ALA C 1 185 ? 52.646 19.922 47.031 1.00 53.01 ? 184 ALA C CB 1 ATOM 5130 N N . ALA C 1 186 ? 55.655 19.038 46.851 1.00 51.00 ? 185 ALA C N 1 ATOM 5131 C CA . ALA C 1 186 ? 57.079 19.364 46.796 1.00 51.69 ? 185 ALA C CA 1 ATOM 5132 C C . ALA C 1 186 ? 57.706 18.839 45.503 1.00 49.77 ? 185 ALA C C 1 ATOM 5133 O O . ALA C 1 186 ? 58.494 19.531 44.857 1.00 50.07 ? 185 ALA C O 1 ATOM 5134 C CB . ALA C 1 186 ? 57.805 18.789 48.004 1.00 52.69 ? 185 ALA C CB 1 ATOM 5135 N N . GLU C 1 187 ? 57.341 17.615 45.136 1.00 47.65 ? 186 GLU C N 1 ATOM 5136 C CA . GLU C 1 187 ? 57.822 17.005 43.914 1.00 45.74 ? 186 GLU C CA 1 ATOM 5137 C C . GLU C 1 187 ? 57.314 17.774 42.697 1.00 44.55 ? 186 GLU C C 1 ATOM 5138 O O . GLU C 1 187 ? 58.061 18.005 41.749 1.00 43.97 ? 186 GLU C O 1 ATOM 5139 C CB . GLU C 1 187 ? 57.389 15.544 43.862 1.00 44.57 ? 186 GLU C CB 1 ATOM 5140 C CG . GLU C 1 187 ? 57.915 14.784 42.663 1.00 43.39 ? 186 GLU C CG 1 ATOM 5141 C CD . GLU C 1 187 ? 57.798 13.288 42.842 1.00 42.89 ? 186 GLU C CD 1 ATOM 5142 O OE1 . GLU C 1 187 ? 58.455 12.739 43.757 1.00 44.01 ? 186 GLU C OE1 1 ATOM 5143 O OE2 . GLU C 1 187 ? 57.038 12.667 42.069 1.00 42.42 ? 186 GLU C OE2 1 ATOM 5144 N N . GLN C 1 188 ? 56.050 18.184 42.747 1.00 44.49 ? 187 GLN C N 1 ATOM 5145 C CA . GLN C 1 188 ? 55.421 18.950 41.665 1.00 43.76 ? 187 GLN C CA 1 ATOM 5146 C C . GLN C 1 188 ? 56.179 20.236 41.351 1.00 44.57 ? 187 GLN C C 1 ATOM 5147 O O . GLN C 1 188 ? 56.537 20.488 40.215 1.00 43.30 ? 187 GLN C O 1 ATOM 5148 C CB . GLN C 1 188 ? 53.967 19.285 42.042 1.00 44.54 ? 187 GLN C CB 1 ATOM 5149 C CG . GLN C 1 188 ? 53.189 20.113 41.027 1.00 44.48 ? 187 GLN C CG 1 ATOM 5150 C CD . GLN C 1 188 ? 53.043 19.433 39.680 1.00 42.68 ? 187 GLN C CD 1 ATOM 5151 O OE1 . GLN C 1 188 ? 53.128 18.208 39.571 1.00 41.69 ? 187 GLN C OE1 1 ATOM 5152 N NE2 . GLN C 1 188 ? 52.807 20.225 38.644 1.00 42.75 ? 187 GLN C NE2 1 ATOM 5153 N N . THR C 1 189 ? 56.409 21.053 42.370 1.00 47.04 ? 188 THR C N 1 ATOM 5154 C CA . THR C 1 189 ? 57.154 22.295 42.191 1.00 48.41 ? 188 THR C CA 1 ATOM 5155 C C . THR C 1 189 ? 58.616 22.010 41.843 1.00 47.93 ? 188 THR C C 1 ATOM 5156 O O . THR C 1 189 ? 59.248 22.786 41.135 1.00 47.86 ? 188 THR C O 1 ATOM 5157 C CB . THR C 1 189 ? 57.073 23.194 43.445 1.00 51.06 ? 188 THR C CB 1 ATOM 5158 O OG1 . THR C 1 189 ? 57.229 22.397 44.624 1.00 51.27 ? 188 THR C OG1 1 ATOM 5159 C CG2 . THR C 1 189 ? 55.729 23.921 43.508 1.00 51.93 ? 188 THR C CG2 1 ATOM 5160 N N . ARG C 1 190 ? 59.151 20.892 42.317 1.00 47.52 ? 189 ARG C N 1 ATOM 5161 C CA . ARG C 1 190 ? 60.555 20.593 42.061 1.00 48.40 ? 189 ARG C CA 1 ATOM 5162 C C . ARG C 1 190 ? 60.808 20.319 40.581 1.00 46.75 ? 189 ARG C C 1 ATOM 5163 O O . ARG C 1 190 ? 61.825 20.777 40.045 1.00 47.59 ? 189 ARG C O 1 ATOM 5164 C CB . ARG C 1 190 ? 61.059 19.431 42.927 1.00 49.37 ? 189 ARG C CB 1 ATOM 5165 C CG . ARG C 1 190 ? 62.573 19.268 42.900 1.00 51.42 ? 189 ARG C CG 1 ATOM 5166 C CD . ARG C 1 190 ? 63.104 18.429 44.061 1.00 53.25 ? 189 ARG C CD 1 ATOM 5167 N NE . ARG C 1 190 ? 62.647 17.033 44.003 1.00 52.55 ? 189 ARG C NE 1 ATOM 5168 C CZ . ARG C 1 190 ? 61.677 16.498 44.749 1.00 52.82 ? 189 ARG C CZ 1 ATOM 5169 N NH1 . ARG C 1 190 ? 61.005 17.220 45.652 1.00 54.29 ? 189 ARG C NH1 1 ATOM 5170 N NH2 . ARG C 1 190 ? 61.373 15.215 44.587 1.00 51.73 ? 189 ARG C NH2 1 ATOM 5171 N N . LEU C 1 191 ? 59.887 19.601 39.925 1.00 44.06 ? 190 LEU C N 1 ATOM 5172 C CA . LEU C 1 191 ? 60.047 19.238 38.511 1.00 42.22 ? 190 LEU C CA 1 ATOM 5173 C C . LEU C 1 191 ? 59.445 20.259 37.540 1.00 41.94 ? 190 LEU C C 1 ATOM 5174 O O . LEU C 1 191 ? 59.965 20.437 36.429 1.00 41.85 ? 190 LEU C O 1 ATOM 5175 C CB . LEU C 1 191 ? 59.429 17.863 38.202 1.00 40.30 ? 190 LEU C CB 1 ATOM 5176 C CG . LEU C 1 191 ? 59.558 16.675 39.168 1.00 40.34 ? 190 LEU C CG 1 ATOM 5177 C CD1 . LEU C 1 191 ? 59.198 15.393 38.441 1.00 38.46 ? 190 LEU C CD1 1 ATOM 5178 C CD2 . LEU C 1 191 ? 60.944 16.538 39.775 1.00 41.81 ? 190 LEU C CD2 1 ATOM 5179 N N . TYR C 1 192 ? 58.342 20.899 37.932 1.00 41.53 ? 191 TYR C N 1 ATOM 5180 C CA . TYR C 1 192 ? 57.537 21.699 36.989 1.00 40.90 ? 191 TYR C CA 1 ATOM 5181 C C . TYR C 1 192 ? 57.292 23.144 37.419 1.00 43.41 ? 191 TYR C C 1 ATOM 5182 O O . TYR C 1 192 ? 56.639 23.898 36.697 1.00 43.59 ? 191 TYR C O 1 ATOM 5183 C CB . TYR C 1 192 ? 56.185 21.013 36.726 1.00 38.31 ? 191 TYR C CB 1 ATOM 5184 C CG . TYR C 1 192 ? 56.308 19.538 36.439 1.00 35.76 ? 191 TYR C CG 1 ATOM 5185 C CD1 . TYR C 1 192 ? 56.886 19.088 35.263 1.00 34.41 ? 191 TYR C CD1 1 ATOM 5186 C CD2 . TYR C 1 192 ? 55.870 18.593 37.349 1.00 34.95 ? 191 TYR C CD2 1 ATOM 5187 C CE1 . TYR C 1 192 ? 57.017 17.731 34.997 1.00 32.70 ? 191 TYR C CE1 1 ATOM 5188 C CE2 . TYR C 1 192 ? 55.986 17.235 37.088 1.00 33.19 ? 191 TYR C CE2 1 ATOM 5189 C CZ . TYR C 1 192 ? 56.565 16.807 35.915 1.00 32.06 ? 191 TYR C CZ 1 ATOM 5190 O OH . TYR C 1 192 ? 56.702 15.458 35.654 1.00 30.50 ? 191 TYR C OH 1 ATOM 5191 N N . GLN C 1 193 ? 57.804 23.519 38.589 1.00 45.60 ? 192 GLN C N 1 ATOM 5192 C CA . GLN C 1 193 ? 57.620 24.849 39.176 1.00 48.34 ? 192 GLN C CA 1 ATOM 5193 C C . GLN C 1 193 ? 56.182 25.105 39.582 1.00 48.89 ? 192 GLN C C 1 ATOM 5194 O O . GLN C 1 193 ? 55.908 25.393 40.744 1.00 50.21 ? 192 GLN C O 1 ATOM 5195 C CB . GLN C 1 193 ? 58.093 25.967 38.232 1.00 49.68 ? 192 GLN C CB 1 ATOM 5196 C CG . GLN C 1 193 ? 58.278 27.318 38.924 1.00 52.55 ? 192 GLN C CG 1 ATOM 5197 C CD . GLN C 1 193 ? 59.431 27.332 39.913 1.00 54.04 ? 192 GLN C CD 1 ATOM 5198 O OE1 . GLN C 1 193 ? 60.198 26.378 40.012 1.00 53.07 ? 192 GLN C OE1 1 ATOM 5199 N NE2 . GLN C 1 193 ? 59.561 28.425 40.645 1.00 56.94 ? 192 GLN C NE2 1 ATOM 5200 N N . ASN C 1 194 ? 55.274 24.998 38.615 1.00 47.79 ? 193 ASN C N 1 ATOM 5201 C CA . ASN C 1 194 ? 53.876 25.360 38.810 1.00 48.53 ? 193 ASN C CA 1 ATOM 5202 C C . ASN C 1 194 ? 53.108 24.312 39.634 1.00 48.13 ? 193 ASN C C 1 ATOM 5203 O O . ASN C 1 194 ? 53.198 23.110 39.355 1.00 45.66 ? 193 ASN C O 1 ATOM 5204 C CB . ASN C 1 194 ? 53.204 25.568 37.449 1.00 47.32 ? 193 ASN C CB 1 ATOM 5205 C CG . ASN C 1 194 ? 54.042 26.418 36.513 1.00 47.68 ? 193 ASN C CG 1 ATOM 5206 O OD1 . ASN C 1 194 ? 54.693 27.374 36.940 1.00 49.82 ? 193 ASN C OD1 1 ATOM 5207 N ND2 . ASN C 1 194 ? 54.054 26.059 35.237 1.00 46.15 ? 193 ASN C ND2 1 ATOM 5208 N N . PRO C 1 195 ? 52.342 24.766 40.644 1.00 50.09 ? 194 PRO C N 1 ATOM 5209 C CA . PRO C 1 195 ? 51.641 23.808 41.492 1.00 50.12 ? 194 PRO C CA 1 ATOM 5210 C C . PRO C 1 195 ? 50.362 23.234 40.869 1.00 49.41 ? 194 PRO C C 1 ATOM 5211 O O . PRO C 1 195 ? 49.973 22.123 41.225 1.00 48.69 ? 194 PRO C O 1 ATOM 5212 C CB . PRO C 1 195 ? 51.323 24.628 42.752 1.00 52.52 ? 194 PRO C CB 1 ATOM 5213 C CG . PRO C 1 195 ? 51.217 26.040 42.280 1.00 53.97 ? 194 PRO C CG 1 ATOM 5214 C CD . PRO C 1 195 ? 52.030 26.163 41.014 1.00 52.74 ? 194 PRO C CD 1 ATOM 5215 N N . THR C 1 196 ? 49.728 23.963 39.946 1.00 50.13 ? 195 THR C N 1 ATOM 5216 C CA . THR C 1 196 ? 48.432 23.555 39.388 1.00 49.53 ? 195 THR C CA 1 ATOM 5217 C C . THR C 1 196 ? 48.495 23.430 37.870 1.00 48.11 ? 195 THR C C 1 ATOM 5218 O O . THR C 1 196 ? 48.524 24.440 37.155 1.00 49.08 ? 195 THR C O 1 ATOM 5219 C CB . THR C 1 196 ? 47.332 24.566 39.758 1.00 51.88 ? 195 THR C CB 1 ATOM 5220 O OG1 . THR C 1 196 ? 47.498 24.972 41.118 1.00 54.56 ? 195 THR C OG1 1 ATOM 5221 C CG2 . THR C 1 196 ? 45.950 23.953 39.579 1.00 51.49 ? 195 THR C CG2 1 ATOM 5222 N N . THR C 1 197 ? 48.473 22.196 37.368 1.00 45.87 ? 196 THR C N 1 ATOM 5223 C CA . THR C 1 197 ? 48.807 21.972 35.970 1.00 44.28 ? 196 THR C CA 1 ATOM 5224 C C . THR C 1 197 ? 47.768 21.182 35.194 1.00 43.41 ? 196 THR C C 1 ATOM 5225 O O . THR C 1 197 ? 46.870 20.568 35.771 1.00 44.31 ? 196 THR C O 1 ATOM 5226 C CB . THR C 1 197 ? 50.170 21.277 35.846 1.00 42.92 ? 196 THR C CB 1 ATOM 5227 O OG1 . THR C 1 197 ? 50.067 19.935 36.331 1.00 41.65 ? 196 THR C OG1 1 ATOM 5228 C CG2 . THR C 1 197 ? 51.232 22.048 36.638 1.00 44.12 ? 196 THR C CG2 1 ATOM 5229 N N . TYR C 1 198 ? 47.921 21.201 33.870 1.00 42.42 ? 197 TYR C N 1 ATOM 5230 C CA . TYR C 1 198 ? 46.976 20.568 32.940 1.00 41.19 ? 197 TYR C CA 1 ATOM 5231 C C . TYR C 1 198 ? 47.660 20.178 31.648 1.00 39.01 ? 197 TYR C C 1 ATOM 5232 O O . TYR C 1 198 ? 48.717 20.701 31.310 1.00 39.33 ? 197 TYR C O 1 ATOM 5233 C CB . TYR C 1 198 ? 45.836 21.527 32.596 1.00 42.32 ? 197 TYR C CB 1 ATOM 5234 C CG . TYR C 1 198 ? 46.288 22.759 31.851 1.00 43.34 ? 197 TYR C CG 1 ATOM 5235 C CD1 . TYR C 1 198 ? 46.869 23.834 32.527 1.00 45.36 ? 197 TYR C CD1 1 ATOM 5236 C CD2 . TYR C 1 198 ? 46.137 22.857 30.474 1.00 42.92 ? 197 TYR C CD2 1 ATOM 5237 C CE1 . TYR C 1 198 ? 47.292 24.961 31.844 1.00 46.35 ? 197 TYR C CE1 1 ATOM 5238 C CE2 . TYR C 1 198 ? 46.540 23.988 29.786 1.00 43.78 ? 197 TYR C CE2 1 ATOM 5239 C CZ . TYR C 1 198 ? 47.124 25.026 30.474 1.00 45.49 ? 197 TYR C CZ 1 ATOM 5240 O OH . TYR C 1 198 ? 47.536 26.131 29.786 1.00 46.73 ? 197 TYR C OH 1 ATOM 5241 N N . ILE C 1 199 ? 47.034 19.255 30.932 1.00 36.97 ? 198 ILE C N 1 ATOM 5242 C CA . ILE C 1 199 ? 47.421 18.930 29.573 1.00 35.07 ? 198 ILE C CA 1 ATOM 5243 C C . ILE C 1 199 ? 46.160 18.916 28.704 1.00 34.54 ? 198 ILE C C 1 ATOM 5244 O O . ILE C 1 199 ? 45.355 18.007 28.807 1.00 33.87 ? 198 ILE C O 1 ATOM 5245 C CB . ILE C 1 199 ? 48.136 17.558 29.491 1.00 33.13 ? 198 ILE C CB 1 ATOM 5246 C CG1 . ILE C 1 199 ? 49.335 17.510 30.443 1.00 33.40 ? 198 ILE C CG1 1 ATOM 5247 C CG2 . ILE C 1 199 ? 48.618 17.272 28.076 1.00 31.65 ? 198 ILE C CG2 1 ATOM 5248 C CD1 . ILE C 1 199 ? 49.932 16.123 30.562 1.00 31.98 ? 198 ILE C CD1 1 ATOM 5249 N N . SER C 1 200 ? 46.000 19.928 27.857 1.00 35.04 ? 199 SER C N 1 ATOM 5250 C CA . SER C 1 200 ? 44.958 19.921 26.829 1.00 35.10 ? 199 SER C CA 1 ATOM 5251 C C . SER C 1 200 ? 45.442 19.248 25.548 1.00 33.39 ? 199 SER C C 1 ATOM 5252 O O . SER C 1 200 ? 46.533 19.551 25.053 1.00 32.47 ? 199 SER C O 1 ATOM 5253 C CB . SER C 1 200 ? 44.520 21.337 26.491 1.00 37.05 ? 199 SER C CB 1 ATOM 5254 O OG . SER C 1 200 ? 43.932 21.947 27.619 1.00 40.22 ? 199 SER C OG 1 ATOM 5255 N N . VAL C 1 201 ? 44.626 18.338 25.013 1.00 32.03 ? 200 VAL C N 1 ATOM 5256 C CA . VAL C 1 201 ? 44.904 17.742 23.724 1.00 31.05 ? 200 VAL C CA 1 ATOM 5257 C C . VAL C 1 201 ? 43.664 17.832 22.855 1.00 31.53 ? 200 VAL C C 1 ATOM 5258 O O . VAL C 1 201 ? 42.559 17.560 23.310 1.00 31.68 ? 200 VAL C O 1 ATOM 5259 C CB . VAL C 1 201 ? 45.355 16.279 23.836 1.00 29.69 ? 200 VAL C CB 1 ATOM 5260 C CG1 . VAL C 1 201 ? 45.832 15.764 22.476 1.00 29.11 ? 200 VAL C CG1 1 ATOM 5261 C CG2 . VAL C 1 201 ? 46.469 16.153 24.862 1.00 29.68 ? 200 VAL C CG2 1 ATOM 5262 N N . GLY C 1 202 ? 43.866 18.206 21.597 1.00 31.44 ? 201 GLY C N 1 ATOM 5263 C CA . GLY C 1 202 ? 42.778 18.328 20.654 1.00 32.21 ? 201 GLY C CA 1 ATOM 5264 C C . GLY C 1 202 ? 43.173 17.876 19.265 1.00 31.80 ? 201 GLY C C 1 ATOM 5265 O O . GLY C 1 202 ? 44.283 18.146 18.811 1.00 32.08 ? 201 GLY C O 1 ATOM 5266 N N . THR C 1 203 ? 42.266 17.165 18.607 1.00 31.39 ? 202 THR C N 1 ATOM 5267 C CA . THR C 1 203 ? 42.334 16.939 17.174 1.00 31.26 ? 202 THR C CA 1 ATOM 5268 C C . THR C 1 203 ? 40.975 17.348 16.644 1.00 32.57 ? 202 THR C C 1 ATOM 5269 O O . THR C 1 203 ? 40.256 18.073 17.321 1.00 34.07 ? 202 THR C O 1 ATOM 5270 C CB . THR C 1 203 ? 42.654 15.460 16.832 1.00 30.21 ? 202 THR C CB 1 ATOM 5271 O OG1 . THR C 1 203 ? 41.547 14.619 17.170 1.00 30.02 ? 202 THR C OG1 1 ATOM 5272 C CG2 . THR C 1 203 ? 43.881 14.995 17.582 1.00 29.36 ? 202 THR C CG2 1 ATOM 5273 N N . SER C 1 204 ? 40.619 16.914 15.442 1.00 33.27 ? 203 SER C N 1 ATOM 5274 C CA . SER C 1 204 ? 39.260 17.133 14.935 1.00 34.81 ? 203 SER C CA 1 ATOM 5275 C C . SER C 1 204 ? 38.206 16.317 15.703 1.00 35.01 ? 203 SER C C 1 ATOM 5276 O O . SER C 1 204 ? 37.056 16.730 15.768 1.00 36.67 ? 203 SER C O 1 ATOM 5277 C CB . SER C 1 204 ? 39.185 16.849 13.435 1.00 34.94 ? 203 SER C CB 1 ATOM 5278 O OG . SER C 1 204 ? 39.508 15.504 13.188 1.00 34.89 ? 203 SER C OG 1 ATOM 5279 N N . THR C 1 205 ? 38.600 15.183 16.285 1.00 34.31 ? 204 THR C N 1 ATOM 5280 C CA . THR C 1 205 ? 37.693 14.341 17.086 1.00 34.93 ? 204 THR C CA 1 ATOM 5281 C C . THR C 1 205 ? 38.021 14.353 18.576 1.00 35.22 ? 204 THR C C 1 ATOM 5282 O O . THR C 1 205 ? 37.121 14.293 19.407 1.00 36.73 ? 204 THR C O 1 ATOM 5283 C CB . THR C 1 205 ? 37.740 12.865 16.649 1.00 34.19 ? 204 THR C CB 1 ATOM 5284 O OG1 . THR C 1 205 ? 39.070 12.368 16.794 1.00 32.77 ? 204 THR C OG1 1 ATOM 5285 C CG2 . THR C 1 205 ? 37.304 12.705 15.201 1.00 35.03 ? 204 THR C CG2 1 ATOM 5286 N N . LEU C 1 206 ? 39.310 14.404 18.908 1.00 34.13 ? 205 LEU C N 1 ATOM 5287 C CA . LEU C 1 206 ? 39.759 14.359 20.284 1.00 33.54 ? 205 LEU C CA 1 ATOM 5288 C C . LEU C 1 206 ? 39.652 15.737 20.943 1.00 34.64 ? 205 LEU C C 1 ATOM 5289 O O . LEU C 1 206 ? 39.923 16.765 20.312 1.00 34.72 ? 205 LEU C O 1 ATOM 5290 C CB . LEU C 1 206 ? 41.201 13.876 20.309 1.00 32.89 ? 205 LEU C CB 1 ATOM 5291 C CG . LEU C 1 206 ? 41.801 13.512 21.663 1.00 32.77 ? 205 LEU C CG 1 ATOM 5292 C CD1 . LEU C 1 206 ? 41.000 12.405 22.347 1.00 33.03 ? 205 LEU C CD1 1 ATOM 5293 C CD2 . LEU C 1 206 ? 43.252 13.107 21.464 1.00 31.71 ? 205 LEU C CD2 1 ATOM 5294 N N . ASN C 1 207 ? 39.240 15.744 22.210 1.00 35.19 ? 206 ASN C N 1 ATOM 5295 C CA . ASN C 1 207 ? 39.088 16.969 23.000 1.00 35.97 ? 206 ASN C CA 1 ATOM 5296 C C . ASN C 1 207 ? 39.318 16.645 24.462 1.00 36.87 ? 206 ASN C C 1 ATOM 5297 O O . ASN C 1 207 ? 38.378 16.483 25.235 1.00 37.71 ? 206 ASN C O 1 ATOM 5298 C CB . ASN C 1 207 ? 37.697 17.564 22.813 1.00 37.37 ? 206 ASN C CB 1 ATOM 5299 C CG . ASN C 1 207 ? 37.488 18.814 23.647 1.00 38.34 ? 206 ASN C CG 1 ATOM 5300 O OD1 . ASN C 1 207 ? 38.448 19.441 24.094 1.00 37.29 ? 206 ASN C OD1 1 ATOM 5301 N ND2 . ASN C 1 207 ? 36.237 19.168 23.879 1.00 39.84 ? 206 ASN C ND2 1 ATOM 5302 N N . GLN C 1 208 ? 40.584 16.568 24.839 1.00 37.72 ? 207 GLN C N 1 ATOM 5303 C CA . GLN C 1 208 ? 40.982 15.934 26.080 1.00 39.17 ? 207 GLN C CA 1 ATOM 5304 C C . GLN C 1 208 ? 41.612 16.950 27.019 1.00 41.03 ? 207 GLN C C 1 ATOM 5305 O O . GLN C 1 208 ? 42.272 17.868 26.562 1.00 41.26 ? 207 GLN C O 1 ATOM 5306 C CB . GLN C 1 208 ? 41.961 14.819 25.743 1.00 37.78 ? 207 GLN C CB 1 ATOM 5307 C CG . GLN C 1 208 ? 42.581 14.124 26.935 1.00 38.35 ? 207 GLN C CG 1 ATOM 5308 C CD . GLN C 1 208 ? 43.684 13.183 26.507 1.00 37.55 ? 207 GLN C CD 1 ATOM 5309 O OE1 . GLN C 1 208 ? 44.880 13.443 26.751 1.00 36.38 ? 207 GLN C OE1 1 ATOM 5310 N NE2 . GLN C 1 208 ? 43.297 12.097 25.836 1.00 36.57 ? 207 GLN C NE2 1 ATOM 5311 N N . ARG C 1 209 ? 41.384 16.792 28.325 1.00 43.29 ? 208 ARG C N 1 ATOM 5312 C CA . ARG C 1 209 ? 42.049 17.611 29.344 1.00 44.90 ? 208 ARG C CA 1 ATOM 5313 C C . ARG C 1 209 ? 42.427 16.764 30.564 1.00 45.50 ? 208 ARG C C 1 ATOM 5314 O O . ARG C 1 209 ? 41.560 16.356 31.334 1.00 48.45 ? 208 ARG C O 1 ATOM 5315 C CB . ARG C 1 209 ? 41.177 18.795 29.750 1.00 47.85 ? 208 ARG C CB 1 ATOM 5316 C CG . ARG C 1 209 ? 41.778 19.677 30.841 1.00 50.27 ? 208 ARG C CG 1 ATOM 5317 C CD . ARG C 1 209 ? 41.700 21.162 30.489 1.00 52.91 ? 208 ARG C CD 1 ATOM 5318 N NE . ARG C 1 209 ? 42.001 22.032 31.634 1.00 55.55 ? 208 ARG C NE 1 ATOM 5319 C CZ . ARG C 1 209 ? 42.269 23.341 31.568 1.00 56.95 ? 208 ARG C CZ 1 ATOM 5320 N NH1 . ARG C 1 209 ? 42.295 23.987 30.404 1.00 57.34 ? 208 ARG C NH1 1 ATOM 5321 N NH2 . ARG C 1 209 ? 42.516 24.015 32.684 1.00 58.41 ? 208 ARG C NH2 1 ATOM 5322 N N . LEU C 1 210 ? 43.727 16.508 30.725 1.00 43.57 ? 209 LEU C N 1 ATOM 5323 C CA . LEU C 1 210 ? 44.242 15.670 31.799 1.00 42.17 ? 209 LEU C CA 1 ATOM 5324 C C . LEU C 1 210 ? 44.805 16.530 32.921 1.00 42.98 ? 209 LEU C C 1 ATOM 5325 O O . LEU C 1 210 ? 45.454 17.547 32.671 1.00 43.31 ? 209 LEU C O 1 ATOM 5326 C CB . LEU C 1 210 ? 45.354 14.777 31.279 1.00 40.73 ? 209 LEU C CB 1 ATOM 5327 C CG . LEU C 1 210 ? 45.076 13.937 30.042 1.00 39.87 ? 209 LEU C CG 1 ATOM 5328 C CD1 . LEU C 1 210 ? 46.383 13.316 29.572 1.00 38.37 ? 209 LEU C CD1 1 ATOM 5329 C CD2 . LEU C 1 210 ? 44.028 12.871 30.335 1.00 40.10 ? 209 LEU C CD2 1 ATOM 5330 N N . VAL C 1 211 ? 44.556 16.114 34.159 1.00 43.28 ? 210 VAL C N 1 ATOM 5331 C CA . VAL C 1 211 ? 45.085 16.814 35.324 1.00 44.33 ? 210 VAL C CA 1 ATOM 5332 C C . VAL C 1 211 ? 45.833 15.805 36.196 1.00 43.72 ? 210 VAL C C 1 ATOM 5333 O O . VAL C 1 211 ? 45.358 14.676 36.398 1.00 42.94 ? 210 VAL C O 1 ATOM 5334 C CB . VAL C 1 211 ? 43.983 17.528 36.130 1.00 46.52 ? 210 VAL C CB 1 ATOM 5335 C CG1 . VAL C 1 211 ? 44.590 18.322 37.284 1.00 48.11 ? 210 VAL C CG1 1 ATOM 5336 C CG2 . VAL C 1 211 ? 43.173 18.453 35.229 1.00 46.87 ? 210 VAL C CG2 1 ATOM 5337 N N . PRO C 1 212 ? 47.023 16.190 36.688 1.00 43.58 ? 211 PRO C N 1 ATOM 5338 C CA . PRO C 1 212 ? 47.807 15.217 37.429 1.00 42.99 ? 211 PRO C CA 1 ATOM 5339 C C . PRO C 1 212 ? 47.193 14.942 38.791 1.00 43.70 ? 211 PRO C C 1 ATOM 5340 O O . PRO C 1 212 ? 46.597 15.829 39.391 1.00 45.16 ? 211 PRO C O 1 ATOM 5341 C CB . PRO C 1 212 ? 49.178 15.889 37.575 1.00 43.63 ? 211 PRO C CB 1 ATOM 5342 C CG . PRO C 1 212 ? 49.163 17.044 36.637 1.00 43.82 ? 211 PRO C CG 1 ATOM 5343 C CD . PRO C 1 212 ? 47.736 17.471 36.560 1.00 44.42 ? 211 PRO C CD 1 ATOM 5344 N N . LYS C 1 213 ? 47.372 13.710 39.254 1.00 42.81 ? 212 LYS C N 1 ATOM 5345 C CA . LYS C 1 213 ? 46.678 13.147 40.383 1.00 43.67 ? 212 LYS C CA 1 ATOM 5346 C C . LYS C 1 213 ? 47.721 12.834 41.428 1.00 44.57 ? 212 LYS C C 1 ATOM 5347 O O . LYS C 1 213 ? 48.421 11.825 41.327 1.00 44.19 ? 212 LYS C O 1 ATOM 5348 C CB . LYS C 1 213 ? 45.970 11.851 39.984 1.00 43.27 ? 212 LYS C CB 1 ATOM 5349 C CG . LYS C 1 213 ? 44.622 12.047 39.294 1.00 43.96 ? 212 LYS C CG 1 ATOM 5350 C CD . LYS C 1 213 ? 43.824 10.757 39.233 1.00 44.00 ? 212 LYS C CD 1 ATOM 5351 C CE . LYS C 1 213 ? 44.556 9.684 38.451 1.00 43.21 ? 212 LYS C CE 1 ATOM 5352 N NZ . LYS C 1 213 ? 43.618 8.707 37.833 1.00 44.03 ? 212 LYS C NZ 1 ATOM 5353 N N . ILE C 1 214 ? 47.844 13.703 42.423 1.00 45.18 ? 213 ILE C N 1 ATOM 5354 C CA . ILE C 1 214 ? 48.759 13.440 43.512 1.00 45.53 ? 213 ILE C CA 1 ATOM 5355 C C . ILE C 1 214 ? 48.130 12.477 44.527 1.00 46.08 ? 213 ILE C C 1 ATOM 5356 O O . ILE C 1 214 ? 47.031 12.691 45.034 1.00 47.43 ? 213 ILE C O 1 ATOM 5357 C CB . ILE C 1 214 ? 49.230 14.739 44.174 1.00 46.77 ? 213 ILE C CB 1 ATOM 5358 C CG1 . ILE C 1 214 ? 50.164 15.484 43.211 1.00 45.71 ? 213 ILE C CG1 1 ATOM 5359 C CG2 . ILE C 1 214 ? 49.939 14.439 45.478 1.00 48.19 ? 213 ILE C CG2 1 ATOM 5360 C CD1 . ILE C 1 214 ? 50.247 16.976 43.444 1.00 47.28 ? 213 ILE C CD1 1 ATOM 5361 N N . ALA C 1 215 ? 48.855 11.397 44.783 1.00 45.02 ? 214 ALA C N 1 ATOM 5362 C CA . ALA C 1 215 ? 48.505 10.425 45.787 1.00 45.13 ? 214 ALA C CA 1 ATOM 5363 C C . ALA C 1 215 ? 49.786 9.783 46.331 1.00 44.85 ? 214 ALA C C 1 ATOM 5364 O O . ALA C 1 215 ? 50.888 9.920 45.761 1.00 43.14 ? 214 ALA C O 1 ATOM 5365 C CB . ALA C 1 215 ? 47.574 9.373 45.204 1.00 44.25 ? 214 ALA C CB 1 ATOM 5366 N N . THR C 1 216 ? 49.636 9.109 47.462 1.00 45.62 ? 215 THR C N 1 ATOM 5367 C CA . THR C 1 216 ? 50.727 8.375 48.057 1.00 45.26 ? 215 THR C CA 1 ATOM 5368 C C . THR C 1 216 ? 50.526 6.959 47.579 1.00 43.85 ? 215 THR C C 1 ATOM 5369 O O . THR C 1 216 ? 49.475 6.367 47.823 1.00 43.67 ? 215 THR C O 1 ATOM 5370 C CB . THR C 1 216 ? 50.685 8.436 49.592 1.00 47.60 ? 215 THR C CB 1 ATOM 5371 O OG1 . THR C 1 216 ? 50.359 9.763 50.005 1.00 48.67 ? 215 THR C OG1 1 ATOM 5372 C CG2 . THR C 1 216 ? 52.032 8.034 50.185 1.00 48.22 ? 215 THR C CG2 1 ATOM 5373 N N . ARG C 1 217 ? 51.522 6.422 46.878 1.00 42.05 ? 216 ARG C N 1 ATOM 5374 C CA . ARG C 1 217 ? 51.388 5.098 46.292 1.00 40.76 ? 216 ARG C CA 1 ATOM 5375 C C . ARG C 1 217 ? 52.522 4.196 46.691 1.00 40.46 ? 216 ARG C C 1 ATOM 5376 O O . ARG C 1 217 ? 53.590 4.657 47.049 1.00 40.91 ? 216 ARG C O 1 ATOM 5377 C CB . ARG C 1 217 ? 51.340 5.207 44.778 1.00 38.57 ? 216 ARG C CB 1 ATOM 5378 C CG . ARG C 1 217 ? 50.364 6.265 44.310 1.00 38.38 ? 216 ARG C CG 1 ATOM 5379 C CD . ARG C 1 217 ? 50.508 6.564 42.835 1.00 36.18 ? 216 ARG C CD 1 ATOM 5380 N NE . ARG C 1 217 ? 49.927 7.864 42.541 1.00 36.10 ? 216 ARG C NE 1 ATOM 5381 C CZ . ARG C 1 217 ? 50.613 8.977 42.290 1.00 36.08 ? 216 ARG C CZ 1 ATOM 5382 N NH1 . ARG C 1 217 ? 51.941 8.999 42.276 1.00 35.44 ? 216 ARG C NH1 1 ATOM 5383 N NH2 . ARG C 1 217 ? 49.950 10.094 42.039 1.00 36.86 ? 216 ARG C NH2 1 ATOM 5384 N N . SER C 1 218 ? 52.273 2.898 46.609 1.00 40.30 ? 217 SER C N 1 ATOM 5385 C CA . SER C 1 218 ? 53.312 1.908 46.782 1.00 40.40 ? 217 SER C CA 1 ATOM 5386 C C . SER C 1 218 ? 54.370 2.070 45.687 1.00 39.41 ? 217 SER C C 1 ATOM 5387 O O . SER C 1 218 ? 54.066 2.425 44.550 1.00 37.21 ? 217 SER C O 1 ATOM 5388 C CB . SER C 1 218 ? 52.722 0.501 46.717 1.00 40.57 ? 217 SER C CB 1 ATOM 5389 O OG . SER C 1 218 ? 51.550 0.402 47.500 1.00 41.97 ? 217 SER C OG 1 ATOM 5390 N N . LYS C 1 219 ? 55.620 1.817 46.058 1.00 40.58 ? 218 LYS C N 1 ATOM 5391 C CA . LYS C 1 219 ? 56.717 1.802 45.110 1.00 39.78 ? 218 LYS C CA 1 ATOM 5392 C C . LYS C 1 219 ? 56.546 0.628 44.154 1.00 38.40 ? 218 LYS C C 1 ATOM 5393 O O . LYS C 1 219 ? 56.420 -0.510 44.596 1.00 38.91 ? 218 LYS C O 1 ATOM 5394 C CB . LYS C 1 219 ? 58.055 1.656 45.842 1.00 41.47 ? 218 LYS C CB 1 ATOM 5395 C CG . LYS C 1 219 ? 58.556 2.909 46.535 1.00 42.84 ? 218 LYS C CG 1 ATOM 5396 C CD . LYS C 1 219 ? 60.042 2.763 46.842 1.00 44.59 ? 218 LYS C CD 1 ATOM 5397 C CE . LYS C 1 219 ? 60.580 3.934 47.652 1.00 46.91 ? 218 LYS C CE 1 ATOM 5398 N NZ . LYS C 1 219 ? 61.971 3.691 48.158 1.00 48.56 ? 218 LYS C NZ 1 ATOM 5399 N N . VAL C 1 220 ? 56.510 0.918 42.857 1.00 36.60 ? 219 VAL C N 1 ATOM 5400 C CA . VAL C 1 220 ? 56.618 -0.096 41.820 1.00 35.77 ? 219 VAL C CA 1 ATOM 5401 C C . VAL C 1 220 ? 57.868 0.243 41.016 1.00 35.30 ? 219 VAL C C 1 ATOM 5402 O O . VAL C 1 220 ? 58.111 1.411 40.685 1.00 33.93 ? 219 VAL C O 1 ATOM 5403 C CB . VAL C 1 220 ? 55.374 -0.129 40.910 1.00 35.28 ? 219 VAL C CB 1 ATOM 5404 C CG1 . VAL C 1 220 ? 55.535 -1.157 39.795 1.00 34.58 ? 219 VAL C CG1 1 ATOM 5405 C CG2 . VAL C 1 220 ? 54.126 -0.443 41.728 1.00 36.23 ? 219 VAL C CG2 1 ATOM 5406 N N . ASN C 1 221 ? 58.669 -0.779 40.730 1.00 36.31 ? 220 ASN C N 1 ATOM 5407 C CA . ASN C 1 221 ? 60.024 -0.592 40.188 1.00 37.04 ? 220 ASN C CA 1 ATOM 5408 C C . ASN C 1 221 ? 60.787 0.516 40.907 1.00 37.72 ? 220 ASN C C 1 ATOM 5409 O O . ASN C 1 221 ? 61.500 1.291 40.272 1.00 37.15 ? 220 ASN C O 1 ATOM 5410 C CB . ASN C 1 221 ? 59.949 -0.279 38.689 1.00 36.31 ? 220 ASN C CB 1 ATOM 5411 C CG . ASN C 1 221 ? 59.429 -1.440 37.875 1.00 36.08 ? 220 ASN C CG 1 ATOM 5412 O OD1 . ASN C 1 221 ? 59.416 -2.586 38.329 1.00 37.75 ? 220 ASN C OD1 1 ATOM 5413 N ND2 . ASN C 1 221 ? 59.015 -1.152 36.652 1.00 35.42 ? 220 ASN C ND2 1 ATOM 5414 N N . GLY C 1 222 ? 60.602 0.605 42.225 1.00 39.22 ? 221 GLY C N 1 ATOM 5415 C CA . GLY C 1 222 ? 61.228 1.640 43.048 1.00 40.65 ? 221 GLY C CA 1 ATOM 5416 C C . GLY C 1 222 ? 60.620 3.036 42.996 1.00 40.60 ? 221 GLY C C 1 ATOM 5417 O O . GLY C 1 222 ? 61.080 3.925 43.714 1.00 41.51 ? 221 GLY C O 1 ATOM 5418 N N . GLN C 1 223 ? 59.601 3.239 42.161 1.00 39.79 ? 222 GLN C N 1 ATOM 5419 C CA . GLN C 1 223 ? 58.950 4.547 42.024 1.00 39.94 ? 222 GLN C CA 1 ATOM 5420 C C . GLN C 1 223 ? 57.580 4.543 42.649 1.00 39.49 ? 222 GLN C C 1 ATOM 5421 O O . GLN C 1 223 ? 56.800 3.625 42.425 1.00 38.76 ? 222 GLN C O 1 ATOM 5422 C CB . GLN C 1 223 ? 58.767 4.926 40.553 1.00 39.30 ? 222 GLN C CB 1 ATOM 5423 C CG . GLN C 1 223 ? 60.035 4.904 39.742 1.00 40.25 ? 222 GLN C CG 1 ATOM 5424 C CD . GLN C 1 223 ? 61.098 5.780 40.351 1.00 43.23 ? 222 GLN C CD 1 ATOM 5425 O OE1 . GLN C 1 223 ? 60.856 6.951 40.655 1.00 44.47 ? 222 GLN C OE1 1 ATOM 5426 N NE2 . GLN C 1 223 ? 62.285 5.213 40.550 1.00 45.03 ? 222 GLN C NE2 1 ATOM 5427 N N . SER C 1 224 ? 57.275 5.586 43.407 1.00 40.08 ? 223 SER C N 1 ATOM 5428 C CA . SER C 1 224 ? 55.911 5.796 43.870 1.00 40.29 ? 223 SER C CA 1 ATOM 5429 C C . SER C 1 224 ? 55.130 6.692 42.915 1.00 38.52 ? 223 SER C C 1 ATOM 5430 O O . SER C 1 224 ? 53.930 6.828 43.066 1.00 39.10 ? 223 SER C O 1 ATOM 5431 C CB . SER C 1 224 ? 55.899 6.369 45.284 1.00 42.27 ? 223 SER C CB 1 ATOM 5432 O OG . SER C 1 224 ? 55.869 5.313 46.228 1.00 43.72 ? 223 SER C OG 1 ATOM 5433 N N . GLY C 1 225 ? 55.819 7.299 41.946 1.00 36.67 ? 224 GLY C N 1 ATOM 5434 C CA . GLY C 1 225 ? 55.198 8.139 40.941 1.00 34.85 ? 224 GLY C CA 1 ATOM 5435 C C . GLY C 1 225 ? 54.586 7.278 39.865 1.00 33.26 ? 224 GLY C C 1 ATOM 5436 O O . GLY C 1 225 ? 54.812 6.059 39.842 1.00 32.99 ? 224 GLY C O 1 ATOM 5437 N N . ARG C 1 226 ? 53.809 7.903 38.978 1.00 31.96 ? 225 ARG C N 1 ATOM 5438 C CA . ARG C 1 226 ? 53.085 7.184 37.919 1.00 30.66 ? 225 ARG C CA 1 ATOM 5439 C C . ARG C 1 226 ? 53.068 7.932 36.591 1.00 29.90 ? 225 ARG C C 1 ATOM 5440 O O . ARG C 1 226 ? 52.902 9.144 36.546 1.00 29.60 ? 225 ARG C O 1 ATOM 5441 C CB . ARG C 1 226 ? 51.636 6.900 38.344 1.00 31.07 ? 225 ARG C CB 1 ATOM 5442 C CG . ARG C 1 226 ? 51.483 5.972 39.539 1.00 31.70 ? 225 ARG C CG 1 ATOM 5443 C CD . ARG C 1 226 ? 51.942 4.580 39.201 1.00 31.16 ? 225 ARG C CD 1 ATOM 5444 N NE . ARG C 1 226 ? 51.673 3.643 40.281 1.00 32.91 ? 225 ARG C NE 1 ATOM 5445 C CZ . ARG C 1 226 ? 52.524 3.304 41.252 1.00 33.57 ? 225 ARG C CZ 1 ATOM 5446 N NH1 . ARG C 1 226 ? 53.745 3.830 41.329 1.00 33.23 ? 225 ARG C NH1 1 ATOM 5447 N NH2 . ARG C 1 226 ? 52.132 2.421 42.163 1.00 34.56 ? 225 ARG C NH2 1 ATOM 5448 N N . MET C 1 227 ? 53.264 7.197 35.505 1.00 30.22 ? 226 MET C N 1 ATOM 5449 C CA . MET C 1 227 ? 53.091 7.751 34.167 1.00 30.56 ? 226 MET C CA 1 ATOM 5450 C C . MET C 1 227 ? 51.806 7.167 33.602 1.00 29.14 ? 226 MET C C 1 ATOM 5451 O O . MET C 1 227 ? 51.591 5.958 33.658 1.00 28.94 ? 226 MET C O 1 ATOM 5452 C CB . MET C 1 227 ? 54.269 7.400 33.271 1.00 31.29 ? 226 MET C CB 1 ATOM 5453 C CG . MET C 1 227 ? 55.591 8.047 33.667 1.00 33.71 ? 226 MET C CG 1 ATOM 5454 S SD . MET C 1 227 ? 55.767 9.796 33.242 1.00 36.61 ? 226 MET C SD 1 ATOM 5455 C CE . MET C 1 227 ? 57.342 10.204 34.000 1.00 37.16 ? 226 MET C CE 1 ATOM 5456 N N . GLU C 1 228 ? 50.944 8.024 33.082 1.00 28.28 ? 227 GLU C N 1 ATOM 5457 C CA . GLU C 1 228 ? 49.739 7.559 32.419 1.00 28.18 ? 227 GLU C CA 1 ATOM 5458 C C . GLU C 1 228 ? 49.782 7.926 30.940 1.00 26.64 ? 227 GLU C C 1 ATOM 5459 O O . GLU C 1 228 ? 49.835 9.106 30.585 1.00 26.65 ? 227 GLU C O 1 ATOM 5460 C CB . GLU C 1 228 ? 48.493 8.143 33.090 1.00 29.92 ? 227 GLU C CB 1 ATOM 5461 C CG . GLU C 1 228 ? 47.193 7.703 32.431 1.00 30.55 ? 227 GLU C CG 1 ATOM 5462 C CD . GLU C 1 228 ? 45.969 7.954 33.284 1.00 31.86 ? 227 GLU C CD 1 ATOM 5463 O OE1 . GLU C 1 228 ? 45.837 9.056 33.857 1.00 32.48 ? 227 GLU C OE1 1 ATOM 5464 O OE2 . GLU C 1 228 ? 45.124 7.046 33.351 1.00 33.17 ? 227 GLU C OE2 1 ATOM 5465 N N . PHE C 1 229 ? 49.748 6.913 30.084 1.00 25.44 ? 228 PHE C N 1 ATOM 5466 C CA . PHE C 1 229 ? 49.829 7.137 28.647 1.00 24.96 ? 228 PHE C CA 1 ATOM 5467 C C . PHE C 1 229 ? 48.502 7.094 27.887 1.00 24.35 ? 228 PHE C C 1 ATOM 5468 O O . PHE C 1 229 ? 47.554 6.385 28.245 1.00 24.45 ? 228 PHE C O 1 ATOM 5469 C CB . PHE C 1 229 ? 50.877 6.212 28.019 1.00 24.77 ? 228 PHE C CB 1 ATOM 5470 C CG . PHE C 1 229 ? 52.253 6.459 28.553 1.00 25.35 ? 228 PHE C CG 1 ATOM 5471 C CD1 . PHE C 1 229 ? 53.006 7.526 28.088 1.00 25.59 ? 228 PHE C CD1 1 ATOM 5472 C CD2 . PHE C 1 229 ? 52.769 5.679 29.577 1.00 25.61 ? 228 PHE C CD2 1 ATOM 5473 C CE1 . PHE C 1 229 ? 54.265 7.774 28.612 1.00 26.03 ? 228 PHE C CE1 1 ATOM 5474 C CE2 . PHE C 1 229 ? 54.027 5.933 30.100 1.00 25.84 ? 228 PHE C CE2 1 ATOM 5475 C CZ . PHE C 1 229 ? 54.770 6.982 29.619 1.00 25.85 ? 228 PHE C CZ 1 ATOM 5476 N N . PHE C 1 230 ? 48.468 7.881 26.822 1.00 23.81 ? 229 PHE C N 1 ATOM 5477 C CA . PHE C 1 230 ? 47.318 7.984 25.947 1.00 23.79 ? 229 PHE C CA 1 ATOM 5478 C C . PHE C 1 230 ? 47.787 7.910 24.517 1.00 22.98 ? 229 PHE C C 1 ATOM 5479 O O . PHE C 1 230 ? 48.984 8.006 24.231 1.00 22.33 ? 229 PHE C O 1 ATOM 5480 C CB . PHE C 1 230 ? 46.594 9.305 26.175 1.00 24.59 ? 229 PHE C CB 1 ATOM 5481 C CG . PHE C 1 230 ? 46.106 9.481 27.574 1.00 25.32 ? 229 PHE C CG 1 ATOM 5482 C CD1 . PHE C 1 230 ? 46.986 9.881 28.582 1.00 25.60 ? 229 PHE C CD1 1 ATOM 5483 C CD2 . PHE C 1 230 ? 44.782 9.236 27.896 1.00 25.85 ? 229 PHE C CD2 1 ATOM 5484 C CE1 . PHE C 1 230 ? 46.544 10.045 29.886 1.00 26.13 ? 229 PHE C CE1 1 ATOM 5485 C CE2 . PHE C 1 230 ? 44.339 9.383 29.202 1.00 26.87 ? 229 PHE C CE2 1 ATOM 5486 C CZ . PHE C 1 230 ? 45.220 9.796 30.191 1.00 27.09 ? 229 PHE C CZ 1 ATOM 5487 N N . TRP C 1 231 ? 46.822 7.761 23.623 1.00 22.99 ? 230 TRP C N 1 ATOM 5488 C CA . TRP C 1 231 ? 47.105 7.597 22.230 1.00 22.39 ? 230 TRP C CA 1 ATOM 5489 C C . TRP C 1 231 ? 45.956 8.043 21.360 1.00 23.02 ? 230 TRP C C 1 ATOM 5490 O O . TRP C 1 231 ? 44.814 8.156 21.805 1.00 23.02 ? 230 TRP C O 1 ATOM 5491 C CB . TRP C 1 231 ? 47.427 6.127 21.938 1.00 22.18 ? 230 TRP C CB 1 ATOM 5492 C CG . TRP C 1 231 ? 46.322 5.154 22.193 1.00 22.51 ? 230 TRP C CG 1 ATOM 5493 C CD1 . TRP C 1 231 ? 46.071 4.481 23.358 1.00 22.97 ? 230 TRP C CD1 1 ATOM 5494 C CD2 . TRP C 1 231 ? 45.354 4.690 21.251 1.00 22.81 ? 230 TRP C CD2 1 ATOM 5495 N NE1 . TRP C 1 231 ? 44.995 3.639 23.201 1.00 23.21 ? 230 TRP C NE1 1 ATOM 5496 C CE2 . TRP C 1 231 ? 44.541 3.743 21.915 1.00 23.26 ? 230 TRP C CE2 1 ATOM 5497 C CE3 . TRP C 1 231 ? 45.080 4.993 19.911 1.00 22.98 ? 230 TRP C CE3 1 ATOM 5498 C CZ2 . TRP C 1 231 ? 43.469 3.112 21.291 1.00 24.03 ? 230 TRP C CZ2 1 ATOM 5499 C CZ3 . TRP C 1 231 ? 44.031 4.348 19.286 1.00 23.42 ? 230 TRP C CZ3 1 ATOM 5500 C CH2 . TRP C 1 231 ? 43.230 3.424 19.980 1.00 24.13 ? 230 TRP C CH2 1 ATOM 5501 N N . THR C 1 232 ? 46.276 8.283 20.095 1.00 23.31 ? 231 THR C N 1 ATOM 5502 C CA . THR C 1 232 ? 45.256 8.529 19.115 1.00 23.81 ? 231 THR C CA 1 ATOM 5503 C C . THR C 1 232 ? 45.764 8.234 17.724 1.00 23.89 ? 231 THR C C 1 ATOM 5504 O O . THR C 1 232 ? 46.967 8.125 17.495 1.00 23.41 ? 231 THR C O 1 ATOM 5505 C CB . THR C 1 232 ? 44.722 9.964 19.197 1.00 24.43 ? 231 THR C CB 1 ATOM 5506 O OG1 . THR C 1 232 ? 43.444 10.003 18.582 1.00 25.52 ? 231 THR C OG1 1 ATOM 5507 C CG2 . THR C 1 232 ? 45.632 10.951 18.493 1.00 24.91 ? 231 THR C CG2 1 ATOM 5508 N N . ILE C 1 233 ? 44.809 8.073 16.817 1.00 24.64 ? 232 ILE C N 1 ATOM 5509 C CA . ILE C 1 233 ? 45.061 7.954 15.394 1.00 24.85 ? 232 ILE C CA 1 ATOM 5510 C C . ILE C 1 233 ? 44.858 9.336 14.766 1.00 25.76 ? 232 ILE C C 1 ATOM 5511 O O . ILE C 1 233 ? 43.725 9.796 14.618 1.00 25.67 ? 232 ILE C O 1 ATOM 5512 C CB . ILE C 1 233 ? 44.080 6.966 14.754 1.00 25.15 ? 232 ILE C CB 1 ATOM 5513 C CG1 . ILE C 1 233 ? 44.247 5.559 15.355 1.00 25.09 ? 232 ILE C CG1 1 ATOM 5514 C CG2 . ILE C 1 233 ? 44.248 6.935 13.251 1.00 25.74 ? 232 ILE C CG2 1 ATOM 5515 C CD1 . ILE C 1 233 ? 45.614 4.934 15.168 1.00 24.82 ? 232 ILE C CD1 1 ATOM 5516 N N . LEU C 1 234 ? 45.955 9.991 14.390 1.00 26.27 ? 233 LEU C N 1 ATOM 5517 C CA . LEU C 1 234 ? 45.862 11.299 13.724 1.00 27.63 ? 233 LEU C CA 1 ATOM 5518 C C . LEU C 1 234 ? 45.692 11.088 12.209 1.00 29.07 ? 233 LEU C C 1 ATOM 5519 O O . LEU C 1 234 ? 46.571 10.511 11.553 1.00 29.71 ? 233 LEU C O 1 ATOM 5520 C CB . LEU C 1 234 ? 47.093 12.135 14.052 1.00 27.33 ? 233 LEU C CB 1 ATOM 5521 C CG . LEU C 1 234 ? 47.123 13.605 13.628 1.00 28.28 ? 233 LEU C CG 1 ATOM 5522 C CD1 . LEU C 1 234 ? 45.998 14.406 14.259 1.00 28.49 ? 233 LEU C CD1 1 ATOM 5523 C CD2 . LEU C 1 234 ? 48.474 14.194 14.006 1.00 28.34 ? 233 LEU C CD2 1 ATOM 5524 N N . LYS C 1 235 ? 44.553 11.514 11.663 1.00 30.39 ? 234 LYS C N 1 ATOM 5525 C CA . LYS C 1 235 ? 44.263 11.324 10.227 1.00 32.14 ? 234 LYS C CA 1 ATOM 5526 C C . LYS C 1 235 ? 45.112 12.263 9.362 1.00 32.00 ? 234 LYS C C 1 ATOM 5527 O O . LYS C 1 235 ? 45.524 13.331 9.821 1.00 32.03 ? 234 LYS C O 1 ATOM 5528 C CB . LYS C 1 235 ? 42.774 11.588 9.924 1.00 34.16 ? 234 LYS C CB 1 ATOM 5529 C CG . LYS C 1 235 ? 41.785 10.658 10.617 1.00 34.68 ? 234 LYS C CG 1 ATOM 5530 C CD . LYS C 1 235 ? 41.488 9.434 9.778 1.00 36.50 ? 234 LYS C CD 1 ATOM 5531 C CE . LYS C 1 235 ? 41.596 8.159 10.597 1.00 36.76 ? 234 LYS C CE 1 ATOM 5532 N NZ . LYS C 1 235 ? 41.157 6.984 9.802 1.00 38.39 ? 234 LYS C NZ 1 ATOM 5533 N N . PRO C 1 236 ? 45.358 11.878 8.096 1.00 32.84 ? 235 PRO C N 1 ATOM 5534 C CA . PRO C 1 236 ? 46.023 12.774 7.152 1.00 33.54 ? 235 PRO C CA 1 ATOM 5535 C C . PRO C 1 236 ? 45.346 14.126 7.086 1.00 34.83 ? 235 PRO C C 1 ATOM 5536 O O . PRO C 1 236 ? 44.119 14.194 6.961 1.00 35.56 ? 235 PRO C O 1 ATOM 5537 C CB . PRO C 1 236 ? 45.873 12.046 5.825 1.00 34.08 ? 235 PRO C CB 1 ATOM 5538 C CG . PRO C 1 236 ? 45.841 10.607 6.189 1.00 33.40 ? 235 PRO C CG 1 ATOM 5539 C CD . PRO C 1 236 ? 45.164 10.531 7.523 1.00 32.79 ? 235 PRO C CD 1 ATOM 5540 N N . ASN C 1 237 ? 46.139 15.191 7.185 1.00 35.89 ? 236 ASN C N 1 ATOM 5541 C CA . ASN C 1 237 ? 45.638 16.571 7.141 1.00 37.44 ? 236 ASN C CA 1 ATOM 5542 C C . ASN C 1 237 ? 44.939 17.056 8.404 1.00 36.86 ? 236 ASN C C 1 ATOM 5543 O O . ASN C 1 237 ? 44.427 18.178 8.438 1.00 37.78 ? 236 ASN C O 1 ATOM 5544 C CB . ASN C 1 237 ? 44.734 16.792 5.931 1.00 39.47 ? 236 ASN C CB 1 ATOM 5545 C CG . ASN C 1 237 ? 45.506 17.266 4.738 1.00 41.73 ? 236 ASN C CG 1 ATOM 5546 O OD1 . ASN C 1 237 ? 45.807 18.454 4.615 1.00 43.02 ? 236 ASN C OD1 1 ATOM 5547 N ND2 . ASN C 1 237 ? 45.839 16.340 3.847 1.00 42.67 ? 236 ASN C ND2 1 ATOM 5548 N N . ASP C 1 238 ? 44.907 16.215 9.433 1.00 35.61 ? 237 ASP C N 1 ATOM 5549 C CA . ASP C 1 238 ? 44.491 16.660 10.742 1.00 35.21 ? 237 ASP C CA 1 ATOM 5550 C C . ASP C 1 238 ? 45.733 17.093 11.526 1.00 34.06 ? 237 ASP C C 1 ATOM 5551 O O . ASP C 1 238 ? 46.863 16.769 11.157 1.00 33.79 ? 237 ASP C O 1 ATOM 5552 C CB . ASP C 1 238 ? 43.718 15.557 11.470 1.00 34.64 ? 237 ASP C CB 1 ATOM 5553 C CG . ASP C 1 238 ? 42.859 16.100 12.611 1.00 35.21 ? 237 ASP C CG 1 ATOM 5554 O OD1 . ASP C 1 238 ? 42.672 17.339 12.682 1.00 34.82 ? 237 ASP C OD1 1 ATOM 5555 O OD2 . ASP C 1 238 ? 42.386 15.282 13.442 1.00 35.04 ? 237 ASP C OD2 1 ATOM 5556 N N . ALA C 1 239 ? 45.511 17.864 12.580 1.00 33.79 ? 238 ALA C N 1 ATOM 5557 C CA . ALA C 1 239 ? 46.580 18.355 13.448 1.00 32.70 ? 238 ALA C CA 1 ATOM 5558 C C . ALA C 1 239 ? 46.239 18.019 14.876 1.00 31.13 ? 238 ALA C C 1 ATOM 5559 O O . ALA C 1 239 ? 45.080 17.885 15.216 1.00 31.04 ? 238 ALA C O 1 ATOM 5560 C CB . ALA C 1 239 ? 46.752 19.856 13.291 1.00 34.12 ? 238 ALA C CB 1 ATOM 5561 N N . ILE C 1 240 ? 47.265 17.855 15.695 1.00 30.58 ? 239 ILE C N 1 ATOM 5562 C CA . ILE C 1 240 ? 47.105 17.639 17.125 1.00 30.12 ? 239 ILE C CA 1 ATOM 5563 C C . ILE C 1 240 ? 47.712 18.838 17.855 1.00 30.66 ? 239 ILE C C 1 ATOM 5564 O O . ILE C 1 240 ? 48.817 19.231 17.555 1.00 30.37 ? 239 ILE C O 1 ATOM 5565 C CB . ILE C 1 240 ? 47.737 16.299 17.566 1.00 28.91 ? 239 ILE C CB 1 ATOM 5566 C CG1 . ILE C 1 240 ? 47.450 16.024 19.039 1.00 28.58 ? 239 ILE C CG1 1 ATOM 5567 C CG2 . ILE C 1 240 ? 49.241 16.264 17.320 1.00 28.90 ? 239 ILE C CG2 1 ATOM 5568 C CD1 . ILE C 1 240 ? 47.600 14.561 19.408 1.00 27.62 ? 239 ILE C CD1 1 ATOM 5569 N N . ASN C 1 241 ? 46.962 19.437 18.774 1.00 31.90 ? 240 ASN C N 1 ATOM 5570 C CA . ASN C 1 241 ? 47.451 20.575 19.553 1.00 33.66 ? 240 ASN C CA 1 ATOM 5571 C C . ASN C 1 241 ? 47.586 20.208 21.019 1.00 33.16 ? 240 ASN C C 1 ATOM 5572 O O . ASN C 1 241 ? 46.612 19.801 21.648 1.00 33.34 ? 240 ASN C O 1 ATOM 5573 C CB . ASN C 1 241 ? 46.516 21.780 19.432 1.00 35.65 ? 240 ASN C CB 1 ATOM 5574 C CG . ASN C 1 241 ? 46.164 22.100 18.001 1.00 36.85 ? 240 ASN C CG 1 ATOM 5575 O OD1 . ASN C 1 241 ? 44.998 22.167 17.647 1.00 38.39 ? 240 ASN C OD1 1 ATOM 5576 N ND2 . ASN C 1 241 ? 47.173 22.278 17.165 1.00 37.43 ? 240 ASN C ND2 1 ATOM 5577 N N . PHE C 1 242 ? 48.799 20.357 21.546 1.00 32.83 ? 241 PHE C N 1 ATOM 5578 C CA . PHE C 1 242 ? 49.077 20.111 22.939 1.00 32.81 ? 241 PHE C CA 1 ATOM 5579 C C . PHE C 1 242 ? 49.239 21.454 23.643 1.00 35.03 ? 241 PHE C C 1 ATOM 5580 O O . PHE C 1 242 ? 49.959 22.323 23.163 1.00 37.02 ? 241 PHE C O 1 ATOM 5581 C CB . PHE C 1 242 ? 50.348 19.287 23.084 1.00 31.87 ? 241 PHE C CB 1 ATOM 5582 C CG . PHE C 1 242 ? 50.234 17.874 22.561 1.00 30.39 ? 241 PHE C CG 1 ATOM 5583 C CD1 . PHE C 1 242 ? 49.663 16.878 23.335 1.00 29.70 ? 241 PHE C CD1 1 ATOM 5584 C CD2 . PHE C 1 242 ? 50.715 17.538 21.295 1.00 30.27 ? 241 PHE C CD2 1 ATOM 5585 C CE1 . PHE C 1 242 ? 49.577 15.566 22.871 1.00 28.75 ? 241 PHE C CE1 1 ATOM 5586 C CE2 . PHE C 1 242 ? 50.628 16.232 20.816 1.00 29.33 ? 241 PHE C CE2 1 ATOM 5587 C CZ . PHE C 1 242 ? 50.055 15.243 21.607 1.00 28.64 ? 241 PHE C CZ 1 ATOM 5588 N N . GLU C 1 243 ? 48.530 21.644 24.750 1.00 35.56 ? 242 GLU C N 1 ATOM 5589 C CA . GLU C 1 243 ? 48.796 22.765 25.635 1.00 37.20 ? 242 GLU C CA 1 ATOM 5590 C C . GLU C 1 243 ? 49.046 22.199 27.028 1.00 37.12 ? 242 GLU C C 1 ATOM 5591 O O . GLU C 1 243 ? 48.365 21.263 27.455 1.00 36.52 ? 242 GLU C O 1 ATOM 5592 C CB . GLU C 1 243 ? 47.647 23.773 25.648 1.00 38.61 ? 242 GLU C CB 1 ATOM 5593 C CG . GLU C 1 243 ? 48.063 25.119 26.217 1.00 40.97 ? 242 GLU C CG 1 ATOM 5594 C CD . GLU C 1 243 ? 46.931 26.129 26.283 1.00 43.08 ? 242 GLU C CD 1 ATOM 5595 O OE1 . GLU C 1 243 ? 46.349 26.433 25.224 1.00 44.40 ? 242 GLU C OE1 1 ATOM 5596 O OE2 . GLU C 1 243 ? 46.630 26.631 27.388 1.00 44.20 ? 242 GLU C OE2 1 ATOM 5597 N N . SER C 1 244 ? 50.037 22.751 27.727 1.00 37.49 ? 243 SER C N 1 ATOM 5598 C CA . SER C 1 244 ? 50.380 22.267 29.057 1.00 36.82 ? 243 SER C CA 1 ATOM 5599 C C . SER C 1 244 ? 51.403 23.144 29.761 1.00 38.00 ? 243 SER C C 1 ATOM 5600 O O . SER C 1 244 ? 52.325 23.668 29.134 1.00 37.86 ? 243 SER C O 1 ATOM 5601 C CB . SER C 1 244 ? 50.922 20.844 28.974 1.00 34.95 ? 243 SER C CB 1 ATOM 5602 O OG . SER C 1 244 ? 51.640 20.532 30.138 1.00 35.19 ? 243 SER C OG 1 ATOM 5603 N N . ASN C 1 245 ? 51.225 23.271 31.075 1.00 39.01 ? 244 ASN C N 1 ATOM 5604 C CA . ASN C 1 245 ? 52.115 24.034 31.936 1.00 40.55 ? 244 ASN C CA 1 ATOM 5605 C C . ASN C 1 245 ? 52.789 23.149 32.988 1.00 39.97 ? 244 ASN C C 1 ATOM 5606 O O . ASN C 1 245 ? 53.338 23.647 33.986 1.00 41.06 ? 244 ASN C O 1 ATOM 5607 C CB . ASN C 1 245 ? 51.341 25.171 32.614 1.00 42.87 ? 244 ASN C CB 1 ATOM 5608 C CG . ASN C 1 245 ? 50.271 24.674 33.565 1.00 43.05 ? 244 ASN C CG 1 ATOM 5609 O OD1 . ASN C 1 245 ? 49.754 23.570 33.412 1.00 41.75 ? 244 ASN C OD1 1 ATOM 5610 N ND2 . ASN C 1 245 ? 49.928 25.495 34.558 1.00 45.25 ? 244 ASN C ND2 1 ATOM 5611 N N . GLY C 1 246 ? 52.751 21.840 32.760 1.00 37.85 ? 245 GLY C N 1 ATOM 5612 C CA . GLY C 1 246 ? 53.322 20.893 33.691 1.00 37.26 ? 245 GLY C CA 1 ATOM 5613 C C . GLY C 1 246 ? 52.887 19.469 33.416 1.00 35.81 ? 245 GLY C C 1 ATOM 5614 O O . GLY C 1 246 ? 51.832 19.224 32.842 1.00 35.06 ? 245 GLY C O 1 ATOM 5615 N N . ASN C 1 247 ? 53.738 18.528 33.810 1.00 35.48 ? 246 ASN C N 1 ATOM 5616 C CA . ASN C 1 247 ? 53.404 17.104 33.838 1.00 34.35 ? 246 ASN C CA 1 ATOM 5617 C C . ASN C 1 247 ? 53.223 16.442 32.484 1.00 32.55 ? 246 ASN C C 1 ATOM 5618 O O . ASN C 1 247 ? 52.812 15.291 32.425 1.00 31.27 ? 246 ASN C O 1 ATOM 5619 C CB . ASN C 1 247 ? 52.166 16.871 34.717 1.00 34.55 ? 246 ASN C CB 1 ATOM 5620 C CG . ASN C 1 247 ? 52.363 17.390 36.115 1.00 35.79 ? 246 ASN C CG 1 ATOM 5621 O OD1 . ASN C 1 247 ? 52.418 18.595 36.339 1.00 36.68 ? 246 ASN C OD1 1 ATOM 5622 N ND2 . ASN C 1 247 ? 52.497 16.483 37.062 1.00 35.97 ? 246 ASN C ND2 1 ATOM 5623 N N . PHE C 1 248 ? 53.597 17.152 31.419 1.00 32.75 ? 247 PHE C N 1 ATOM 5624 C CA . PHE C 1 248 ? 53.444 16.683 30.037 1.00 31.46 ? 247 PHE C CA 1 ATOM 5625 C C . PHE C 1 248 ? 54.572 15.747 29.603 1.00 31.02 ? 247 PHE C C 1 ATOM 5626 O O . PHE C 1 248 ? 55.757 16.114 29.641 1.00 31.23 ? 247 PHE C O 1 ATOM 5627 C CB . PHE C 1 248 ? 53.362 17.899 29.101 1.00 32.11 ? 247 PHE C CB 1 ATOM 5628 C CG . PHE C 1 248 ? 53.093 17.556 27.655 1.00 31.66 ? 247 PHE C CG 1 ATOM 5629 C CD1 . PHE C 1 248 ? 52.179 16.562 27.302 1.00 30.39 ? 247 PHE C CD1 1 ATOM 5630 C CD2 . PHE C 1 248 ? 53.728 18.263 26.642 1.00 32.08 ? 247 PHE C CD2 1 ATOM 5631 C CE1 . PHE C 1 248 ? 51.943 16.258 25.978 1.00 29.74 ? 247 PHE C CE1 1 ATOM 5632 C CE2 . PHE C 1 248 ? 53.487 17.966 25.316 1.00 31.48 ? 247 PHE C CE2 1 ATOM 5633 C CZ . PHE C 1 248 ? 52.593 16.964 24.986 1.00 30.48 ? 247 PHE C CZ 1 ATOM 5634 N N . ILE C 1 249 ? 54.212 14.520 29.228 1.00 30.12 ? 248 ILE C N 1 ATOM 5635 C CA . ILE C 1 249 ? 55.174 13.606 28.614 1.00 29.10 ? 248 ILE C CA 1 ATOM 5636 C C . ILE C 1 249 ? 54.894 13.674 27.118 1.00 28.53 ? 248 ILE C C 1 ATOM 5637 O O . ILE C 1 249 ? 53.920 13.097 26.636 1.00 28.09 ? 248 ILE C O 1 ATOM 5638 C CB . ILE C 1 249 ? 55.052 12.157 29.130 1.00 28.77 ? 248 ILE C CB 1 ATOM 5639 C CG1 . ILE C 1 249 ? 54.993 12.097 30.647 1.00 28.96 ? 248 ILE C CG1 1 ATOM 5640 C CG2 . ILE C 1 249 ? 56.222 11.306 28.629 1.00 29.07 ? 248 ILE C CG2 1 ATOM 5641 C CD1 . ILE C 1 249 ? 56.207 12.660 31.354 1.00 30.44 ? 248 ILE C CD1 1 ATOM 5642 N N . ALA C 1 250 ? 55.741 14.409 26.396 1.00 29.06 ? 249 ALA C N 1 ATOM 5643 C CA . ALA C 1 250 ? 55.451 14.820 25.028 1.00 28.69 ? 249 ALA C CA 1 ATOM 5644 C C . ALA C 1 250 ? 55.830 13.759 24.014 1.00 28.24 ? 249 ALA C C 1 ATOM 5645 O O . ALA C 1 250 ? 56.731 12.974 24.249 1.00 27.96 ? 249 ALA C O 1 ATOM 5646 C CB . ALA C 1 250 ? 56.170 16.120 24.710 1.00 29.90 ? 249 ALA C CB 1 ATOM 5647 N N . PRO C 1 251 ? 55.134 13.728 22.874 1.00 28.52 ? 250 PRO C N 1 ATOM 5648 C CA . PRO C 1 251 ? 55.547 12.884 21.760 1.00 28.54 ? 250 PRO C CA 1 ATOM 5649 C C . PRO C 1 251 ? 56.939 13.232 21.245 1.00 29.87 ? 250 PRO C C 1 ATOM 5650 O O . PRO C 1 251 ? 57.323 14.414 21.238 1.00 31.67 ? 250 PRO C O 1 ATOM 5651 C CB . PRO C 1 251 ? 54.526 13.206 20.671 1.00 28.57 ? 250 PRO C CB 1 ATOM 5652 C CG . PRO C 1 251 ? 53.360 13.785 21.381 1.00 28.79 ? 250 PRO C CG 1 ATOM 5653 C CD . PRO C 1 251 ? 53.906 14.482 22.575 1.00 29.14 ? 250 PRO C CD 1 ATOM 5654 N N . GLU C 1 252 ? 57.689 12.213 20.837 1.00 29.37 ? 251 GLU C N 1 ATOM 5655 C CA . GLU C 1 252 ? 58.884 12.424 20.035 1.00 30.68 ? 251 GLU C CA 1 ATOM 5656 C C . GLU C 1 252 ? 58.710 11.688 18.713 1.00 29.98 ? 251 GLU C C 1 ATOM 5657 O O . GLU C 1 252 ? 58.746 12.297 17.644 1.00 30.64 ? 251 GLU C O 1 ATOM 5658 C CB . GLU C 1 252 ? 60.132 11.938 20.771 1.00 32.18 ? 251 GLU C CB 1 ATOM 5659 C CG . GLU C 1 252 ? 61.447 12.261 20.068 1.00 34.40 ? 251 GLU C CG 1 ATOM 5660 C CD . GLU C 1 252 ? 62.669 11.807 20.857 1.00 36.13 ? 251 GLU C CD 1 ATOM 5661 O OE1 . GLU C 1 252 ? 62.531 11.512 22.073 1.00 36.41 ? 251 GLU C OE1 1 ATOM 5662 O OE2 . GLU C 1 252 ? 63.773 11.738 20.258 1.00 37.80 ? 251 GLU C OE2 1 ATOM 5663 N N . ASN C 1 253 ? 58.521 10.375 18.797 1.00 28.63 ? 252 ASN C N 1 ATOM 5664 C CA . ASN C 1 253 ? 58.269 9.561 17.621 1.00 28.67 ? 252 ASN C CA 1 ATOM 5665 C C . ASN C 1 253 ? 56.821 9.107 17.574 1.00 27.28 ? 252 ASN C C 1 ATOM 5666 O O . ASN C 1 253 ? 56.188 8.868 18.600 1.00 26.08 ? 252 ASN C O 1 ATOM 5667 C CB . ASN C 1 253 ? 59.189 8.345 17.603 1.00 29.19 ? 252 ASN C CB 1 ATOM 5668 C CG . ASN C 1 253 ? 60.657 8.729 17.696 1.00 30.23 ? 252 ASN C CG 1 ATOM 5669 O OD1 . ASN C 1 253 ? 61.115 9.615 16.991 1.00 30.46 ? 252 ASN C OD1 1 ATOM 5670 N ND2 . ASN C 1 253 ? 61.388 8.080 18.601 1.00 30.25 ? 252 ASN C ND2 1 ATOM 5671 N N . ALA C 1 254 ? 56.305 9.020 16.360 1.00 27.46 ? 253 ALA C N 1 ATOM 5672 C CA . ALA C 1 254 ? 54.976 8.515 16.111 1.00 26.34 ? 253 ALA C CA 1 ATOM 5673 C C . ALA C 1 254 ? 55.089 7.424 15.054 1.00 26.34 ? 253 ALA C C 1 ATOM 5674 O O . ALA C 1 254 ? 56.156 7.244 14.457 1.00 26.72 ? 253 ALA C O 1 ATOM 5675 C CB . ALA C 1 254 ? 54.088 9.644 15.636 1.00 26.51 ? 253 ALA C CB 1 ATOM 5676 N N . TYR C 1 255 ? 53.991 6.709 14.825 1.00 25.98 ? 254 TYR C N 1 ATOM 5677 C CA . TYR C 1 255 ? 53.967 5.589 13.899 1.00 26.53 ? 254 TYR C CA 1 ATOM 5678 C C . TYR C 1 255 ? 52.971 5.768 12.756 1.00 26.75 ? 254 TYR C C 1 ATOM 5679 O O . TYR C 1 255 ? 51.758 5.791 12.974 1.00 26.36 ? 254 TYR C O 1 ATOM 5680 C CB . TYR C 1 255 ? 53.617 4.317 14.644 1.00 26.13 ? 254 TYR C CB 1 ATOM 5681 C CG . TYR C 1 255 ? 54.614 3.908 15.688 1.00 26.51 ? 254 TYR C CG 1 ATOM 5682 C CD1 . TYR C 1 255 ? 54.513 4.374 16.996 1.00 26.16 ? 254 TYR C CD1 1 ATOM 5683 C CD2 . TYR C 1 255 ? 55.643 3.027 15.384 1.00 27.25 ? 254 TYR C CD2 1 ATOM 5684 C CE1 . TYR C 1 255 ? 55.414 3.981 17.964 1.00 26.15 ? 254 TYR C CE1 1 ATOM 5685 C CE2 . TYR C 1 255 ? 56.548 2.625 16.348 1.00 27.31 ? 254 TYR C CE2 1 ATOM 5686 C CZ . TYR C 1 255 ? 56.426 3.102 17.634 1.00 26.98 ? 254 TYR C CZ 1 ATOM 5687 O OH . TYR C 1 255 ? 57.323 2.709 18.594 1.00 27.52 ? 254 TYR C OH 1 ATOM 5688 N N . LYS C 1 256 ? 53.502 5.872 11.539 1.00 27.62 ? 255 LYS C N 1 ATOM 5689 C CA . LYS C 1 256 ? 52.694 5.863 10.317 1.00 27.96 ? 255 LYS C CA 1 ATOM 5690 C C . LYS C 1 256 ? 52.232 4.458 10.018 1.00 27.38 ? 255 LYS C C 1 ATOM 5691 O O . LYS C 1 256 ? 53.049 3.555 9.926 1.00 27.99 ? 255 LYS C O 1 ATOM 5692 C CB . LYS C 1 256 ? 53.506 6.364 9.123 1.00 29.27 ? 255 LYS C CB 1 ATOM 5693 C CG . LYS C 1 256 ? 54.051 7.762 9.315 1.00 30.02 ? 255 LYS C CG 1 ATOM 5694 C CD . LYS C 1 256 ? 54.349 8.462 8.001 1.00 32.02 ? 255 LYS C CD 1 ATOM 5695 C CE . LYS C 1 256 ? 55.265 7.666 7.085 1.00 33.60 ? 255 LYS C CE 1 ATOM 5696 N NZ . LYS C 1 256 ? 55.354 8.331 5.752 1.00 35.56 ? 255 LYS C NZ 1 ATOM 5697 N N . ILE C 1 257 ? 50.926 4.274 9.855 1.00 27.06 ? 256 ILE C N 1 ATOM 5698 C CA . ILE C 1 257 ? 50.374 2.954 9.503 1.00 27.17 ? 256 ILE C CA 1 ATOM 5699 C C . ILE C 1 257 ? 50.533 2.730 8.001 1.00 27.78 ? 256 ILE C C 1 ATOM 5700 O O . ILE C 1 257 ? 49.880 3.373 7.176 1.00 27.85 ? 256 ILE C O 1 ATOM 5701 C CB . ILE C 1 257 ? 48.902 2.818 9.964 1.00 27.13 ? 256 ILE C CB 1 ATOM 5702 C CG1 . ILE C 1 257 ? 48.856 2.852 11.499 1.00 26.70 ? 256 ILE C CG1 1 ATOM 5703 C CG2 . ILE C 1 257 ? 48.279 1.526 9.443 1.00 27.55 ? 256 ILE C CG2 1 ATOM 5704 C CD1 . ILE C 1 257 ? 47.498 3.166 12.086 1.00 26.99 ? 256 ILE C CD1 1 ATOM 5705 N N . VAL C 1 258 ? 51.423 1.809 7.661 1.00 28.38 ? 257 VAL C N 1 ATOM 5706 C CA . VAL C 1 258 ? 51.896 1.636 6.288 1.00 29.78 ? 257 VAL C CA 1 ATOM 5707 C C . VAL C 1 258 ? 51.205 0.484 5.574 1.00 30.54 ? 257 VAL C C 1 ATOM 5708 O O . VAL C 1 258 ? 50.964 0.553 4.360 1.00 31.48 ? 257 VAL C O 1 ATOM 5709 C CB . VAL C 1 258 ? 53.428 1.478 6.294 1.00 30.44 ? 257 VAL C CB 1 ATOM 5710 C CG1 . VAL C 1 258 ? 53.952 0.866 5.014 1.00 32.12 ? 257 VAL C CG1 1 ATOM 5711 C CG2 . VAL C 1 258 ? 54.054 2.841 6.537 1.00 30.52 ? 257 VAL C CG2 1 ATOM 5712 N N . LYS C 1 259 ? 50.880 -0.565 6.316 1.00 38.04 ? 258 LYS C N 1 ATOM 5713 C CA . LYS C 1 259 ? 50.143 -1.677 5.758 1.00 38.58 ? 258 LYS C CA 1 ATOM 5714 C C . LYS C 1 259 ? 49.147 -2.216 6.764 1.00 38.26 ? 258 LYS C C 1 ATOM 5715 O O . LYS C 1 259 ? 49.517 -2.545 7.889 1.00 36.90 ? 258 LYS C O 1 ATOM 5716 C CB . LYS C 1 259 ? 51.096 -2.783 5.333 1.00 38.95 ? 258 LYS C CB 1 ATOM 5717 C CG . LYS C 1 259 ? 50.390 -3.918 4.623 1.00 39.85 ? 258 LYS C CG 1 ATOM 5718 C CD . LYS C 1 259 ? 51.339 -4.983 4.117 1.00 40.83 ? 258 LYS C CD 1 ATOM 5719 C CE . LYS C 1 259 ? 50.539 -6.223 3.762 1.00 41.60 ? 258 LYS C CE 1 ATOM 5720 N NZ . LYS C 1 259 ? 51.338 -7.201 2.986 1.00 43.54 ? 258 LYS C NZ 1 ATOM 5721 N N . LYS C 1 260 ? 47.883 -2.285 6.346 1.00 39.99 ? 259 LYS C N 1 ATOM 5722 C CA . LYS C 1 260 ? 46.843 -2.999 7.067 1.00 40.64 ? 259 LYS C CA 1 ATOM 5723 C C . LYS C 1 260 ? 46.496 -4.282 6.315 1.00 42.06 ? 259 LYS C C 1 ATOM 5724 O O . LYS C 1 260 ? 46.612 -4.350 5.090 1.00 43.22 ? 259 LYS C O 1 ATOM 5725 C CB . LYS C 1 260 ? 45.592 -2.136 7.205 1.00 42.05 ? 259 LYS C CB 1 ATOM 5726 C CG . LYS C 1 260 ? 45.854 -0.813 7.902 1.00 42.22 ? 259 LYS C CG 1 ATOM 5727 C CD . LYS C 1 260 ? 44.672 0.130 7.814 1.00 44.28 ? 259 LYS C CD 1 ATOM 5728 C CE . LYS C 1 260 ? 43.604 -0.199 8.839 1.00 45.47 ? 259 LYS C CE 1 ATOM 5729 N NZ . LYS C 1 260 ? 43.892 0.461 10.143 1.00 45.58 ? 259 LYS C NZ 1 ATOM 5730 N N . GLY C 1 261 ? 46.053 -5.281 7.068 1.00 42.15 ? 260 GLY C N 1 ATOM 5731 C CA . GLY C 1 261 ? 45.772 -6.607 6.552 1.00 43.51 ? 260 GLY C CA 1 ATOM 5732 C C . GLY C 1 261 ? 45.558 -7.553 7.718 1.00 43.58 ? 260 GLY C C 1 ATOM 5733 O O . GLY C 1 261 ? 45.446 -7.117 8.865 1.00 43.46 ? 260 GLY C O 1 ATOM 5734 N N . ASP C 1 262 ? 45.507 -8.848 7.439 1.00 45.27 ? 261 ASP C N 1 ATOM 5735 C CA . ASP C 1 262 ? 45.181 -9.833 8.473 1.00 45.84 ? 261 ASP C CA 1 ATOM 5736 C C . ASP C 1 262 ? 46.387 -10.101 9.369 1.00 43.79 ? 261 ASP C C 1 ATOM 5737 O O . ASP C 1 262 ? 47.489 -10.405 8.895 1.00 44.88 ? 261 ASP C O 1 ATOM 5738 C CB . ASP C 1 262 ? 44.659 -11.149 7.858 1.00 48.00 ? 261 ASP C CB 1 ATOM 5739 C CG . ASP C 1 262 ? 43.135 -11.152 7.650 1.00 51.14 ? 261 ASP C CG 1 ATOM 5740 O OD1 . ASP C 1 262 ? 42.493 -10.077 7.760 1.00 52.07 ? 261 ASP C OD1 1 ATOM 5741 O OD2 . ASP C 1 262 ? 42.569 -12.248 7.387 1.00 53.52 ? 261 ASP C OD2 1 ATOM 5742 N N . SER C 1 263 ? 46.164 -9.986 10.668 1.00 41.85 ? 262 SER C N 1 ATOM 5743 C CA . SER C 1 263 ? 47.190 -10.271 11.659 1.00 40.52 ? 262 SER C CA 1 ATOM 5744 C C . SER C 1 263 ? 46.512 -10.652 12.978 1.00 39.16 ? 262 SER C C 1 ATOM 5745 O O . SER C 1 263 ? 45.299 -10.860 13.025 1.00 38.97 ? 262 SER C O 1 ATOM 5746 C CB . SER C 1 263 ? 48.107 -9.056 11.834 1.00 40.39 ? 262 SER C CB 1 ATOM 5747 O OG . SER C 1 263 ? 49.182 -9.315 12.730 1.00 40.81 ? 262 SER C OG 1 ATOM 5748 N N . THR C 1 264 ? 47.311 -10.743 14.034 1.00 37.86 ? 263 THR C N 1 ATOM 5749 C CA . THR C 1 264 ? 46.830 -11.089 15.369 1.00 37.16 ? 263 THR C CA 1 ATOM 5750 C C . THR C 1 264 ? 47.985 -10.959 16.363 1.00 36.75 ? 263 THR C C 1 ATOM 5751 O O . THR C 1 264 ? 49.151 -10.935 15.964 1.00 35.81 ? 263 THR C O 1 ATOM 5752 C CB . THR C 1 264 ? 46.261 -12.529 15.417 1.00 37.15 ? 263 THR C CB 1 ATOM 5753 O OG1 . THR C 1 264 ? 45.610 -12.744 16.666 1.00 37.64 ? 263 THR C OG1 1 ATOM 5754 C CG2 . THR C 1 264 ? 47.340 -13.572 15.246 1.00 37.20 ? 263 THR C CG2 1 ATOM 5755 N N . ILE C 1 265 ? 47.657 -10.877 17.651 1.00 37.13 ? 264 ILE C N 1 ATOM 5756 C CA . ILE C 1 265 ? 48.669 -10.916 18.704 1.00 37.25 ? 264 ILE C CA 1 ATOM 5757 C C . ILE C 1 265 ? 48.554 -12.257 19.420 1.00 37.55 ? 264 ILE C C 1 ATOM 5758 O O . ILE C 1 265 ? 47.541 -12.540 20.042 1.00 37.76 ? 264 ILE C O 1 ATOM 5759 C CB . ILE C 1 265 ? 48.519 -9.746 19.677 1.00 37.92 ? 264 ILE C CB 1 ATOM 5760 C CG1 . ILE C 1 265 ? 48.559 -8.425 18.896 1.00 37.72 ? 264 ILE C CG1 1 ATOM 5761 C CG2 . ILE C 1 265 ? 49.644 -9.768 20.705 1.00 38.76 ? 264 ILE C CG2 1 ATOM 5762 C CD1 . ILE C 1 265 ? 47.979 -7.252 19.641 1.00 38.57 ? 264 ILE C CD1 1 ATOM 5763 N N . MET C 1 266 ? 49.590 -13.083 19.283 1.00 37.56 ? 265 MET C N 1 ATOM 5764 C CA . MET C 1 266 ? 49.619 -14.426 19.850 1.00 38.52 ? 265 MET C CA 1 ATOM 5765 C C . MET C 1 266 ? 50.262 -14.427 21.213 1.00 39.35 ? 265 MET C C 1 ATOM 5766 O O . MET C 1 266 ? 51.356 -13.888 21.386 1.00 39.48 ? 265 MET C O 1 ATOM 5767 C CB . MET C 1 266 ? 50.420 -15.390 18.955 1.00 39.17 ? 265 MET C CB 1 ATOM 5768 C CG . MET C 1 266 ? 49.568 -16.259 18.065 1.00 39.43 ? 265 MET C CG 1 ATOM 5769 S SD . MET C 1 266 ? 50.478 -17.680 17.428 1.00 41.19 ? 265 MET C SD 1 ATOM 5770 C CE . MET C 1 266 ? 49.495 -17.985 15.970 1.00 40.61 ? 265 MET C CE 1 ATOM 5771 N N . LYS C 1 267 ? 49.592 -15.059 22.168 1.00 40.11 ? 266 LYS C N 1 ATOM 5772 C CA . LYS C 1 267 ? 50.183 -15.323 23.473 1.00 42.04 ? 266 LYS C CA 1 ATOM 5773 C C . LYS C 1 267 ? 50.957 -16.639 23.382 1.00 42.71 ? 266 LYS C C 1 ATOM 5774 O O . LYS C 1 267 ? 50.371 -17.708 23.167 1.00 42.47 ? 266 LYS C O 1 ATOM 5775 C CB . LYS C 1 267 ? 49.101 -15.382 24.552 1.00 43.37 ? 266 LYS C CB 1 ATOM 5776 C CG . LYS C 1 267 ? 48.146 -14.184 24.551 1.00 43.52 ? 266 LYS C CG 1 ATOM 5777 C CD . LYS C 1 267 ? 48.844 -12.860 24.847 1.00 44.35 ? 266 LYS C CD 1 ATOM 5778 C CE . LYS C 1 267 ? 48.978 -12.640 26.351 1.00 46.90 ? 266 LYS C CE 1 ATOM 5779 N NZ . LYS C 1 267 ? 49.791 -11.440 26.711 1.00 47.87 ? 266 LYS C NZ 1 ATOM 5780 N N . SER C 1 268 ? 52.280 -16.558 23.494 1.00 43.76 ? 267 SER C N 1 ATOM 5781 C CA . SER C 1 268 ? 53.125 -17.748 23.372 1.00 44.93 ? 267 SER C CA 1 ATOM 5782 C C . SER C 1 268 ? 54.453 -17.587 24.094 1.00 47.28 ? 267 SER C C 1 ATOM 5783 O O . SER C 1 268 ? 55.003 -16.491 24.173 1.00 47.59 ? 267 SER C O 1 ATOM 5784 C CB . SER C 1 268 ? 53.385 -18.076 21.899 1.00 43.96 ? 267 SER C CB 1 ATOM 5785 O OG . SER C 1 268 ? 54.049 -19.323 21.758 1.00 45.05 ? 267 SER C OG 1 ATOM 5786 N N . GLU C 1 269 ? 54.962 -18.701 24.607 1.00 49.51 ? 268 GLU C N 1 ATOM 5787 C CA . GLU C 1 269 ? 56.249 -18.734 25.289 1.00 52.61 ? 268 GLU C CA 1 ATOM 5788 C C . GLU C 1 269 ? 57.378 -19.226 24.385 1.00 53.50 ? 268 GLU C C 1 ATOM 5789 O O . GLU C 1 269 ? 58.535 -19.264 24.802 1.00 55.81 ? 268 GLU C O 1 ATOM 5790 C CB . GLU C 1 269 ? 56.141 -19.614 26.537 1.00 54.92 ? 268 GLU C CB 1 ATOM 5791 C CG . GLU C 1 269 ? 55.182 -19.046 27.573 1.00 55.23 ? 268 GLU C CG 1 ATOM 5792 C CD . GLU C 1 269 ? 55.566 -17.638 27.998 1.00 55.99 ? 268 GLU C CD 1 ATOM 5793 O OE1 . GLU C 1 269 ? 56.778 -17.388 28.169 1.00 58.04 ? 268 GLU C OE1 1 ATOM 5794 O OE2 . GLU C 1 269 ? 54.665 -16.784 28.150 1.00 55.21 ? 268 GLU C OE2 1 ATOM 5795 N N . LEU C 1 270 ? 57.042 -19.580 23.148 1.00 52.05 ? 269 LEU C N 1 ATOM 5796 C CA . LEU C 1 270 ? 58.030 -20.073 22.192 1.00 53.39 ? 269 LEU C CA 1 ATOM 5797 C C . LEU C 1 270 ? 58.876 -18.944 21.607 1.00 53.75 ? 269 LEU C C 1 ATOM 5798 O O . LEU C 1 270 ? 58.500 -17.773 21.642 1.00 52.17 ? 269 LEU C O 1 ATOM 5799 C CB . LEU C 1 270 ? 57.337 -20.821 21.059 1.00 51.93 ? 269 LEU C CB 1 ATOM 5800 C CG . LEU C 1 270 ? 56.449 -22.001 21.458 1.00 51.81 ? 269 LEU C CG 1 ATOM 5801 C CD1 . LEU C 1 270 ? 55.750 -22.565 20.225 1.00 50.29 ? 269 LEU C CD1 1 ATOM 5802 C CD2 . LEU C 1 270 ? 57.250 -23.073 22.185 1.00 54.62 ? 269 LEU C CD2 1 ATOM 5803 N N . GLU C 1 271 ? 60.030 -19.318 21.074 1.00 56.28 ? 270 GLU C N 1 ATOM 5804 C CA . GLU C 1 271 ? 60.915 -18.382 20.391 1.00 57.27 ? 270 GLU C CA 1 ATOM 5805 C C . GLU C 1 271 ? 60.793 -18.639 18.895 1.00 56.46 ? 270 GLU C C 1 ATOM 5806 O O . GLU C 1 271 ? 60.022 -19.502 18.476 1.00 55.82 ? 270 GLU C O 1 ATOM 5807 C CB . GLU C 1 271 ? 62.357 -18.578 20.864 1.00 60.88 ? 270 GLU C CB 1 ATOM 5808 N N . TYR C 1 272 ? 61.537 -17.890 18.091 1.00 57.18 ? 271 TYR C N 1 ATOM 5809 C CA . TYR C 1 272 ? 61.527 -18.089 16.649 1.00 57.31 ? 271 TYR C CA 1 ATOM 5810 C C . TYR C 1 272 ? 62.092 -19.460 16.281 1.00 60.60 ? 271 TYR C C 1 ATOM 5811 O O . TYR C 1 272 ? 63.124 -19.884 16.812 1.00 63.57 ? 271 TYR C O 1 ATOM 5812 C CB . TYR C 1 272 ? 62.339 -16.994 15.957 1.00 58.09 ? 271 TYR C CB 1 ATOM 5813 C CG . TYR C 1 272 ? 62.218 -17.010 14.450 1.00 57.57 ? 271 TYR C CG 1 ATOM 5814 C CD1 . TYR C 1 272 ? 60.966 -17.003 13.833 1.00 54.52 ? 271 TYR C CD1 1 ATOM 5815 C CD2 . TYR C 1 272 ? 63.347 -17.009 13.640 1.00 60.23 ? 271 TYR C CD2 1 ATOM 5816 C CE1 . TYR C 1 272 ? 60.845 -17.008 12.458 1.00 54.42 ? 271 TYR C CE1 1 ATOM 5817 C CE2 . TYR C 1 272 ? 63.236 -17.016 12.259 1.00 60.26 ? 271 TYR C CE2 1 ATOM 5818 C CZ . TYR C 1 272 ? 61.983 -17.012 11.674 1.00 57.24 ? 271 TYR C CZ 1 ATOM 5819 O OH . TYR C 1 272 ? 61.865 -17.020 10.305 1.00 57.12 ? 271 TYR C OH 1 ATOM 5820 N N . GLY C 1 273 ? 61.418 -20.148 15.367 1.00 60.52 ? 272 GLY C N 1 ATOM 5821 C CA . GLY C 1 273 ? 61.813 -21.503 14.987 1.00 63.42 ? 272 GLY C CA 1 ATOM 5822 C C . GLY C 1 273 ? 62.415 -21.661 13.603 1.00 65.82 ? 272 GLY C C 1 ATOM 5823 O O . GLY C 1 273 ? 62.596 -22.786 13.143 1.00 67.66 ? 272 GLY C O 1 ATOM 5824 N N . ASN C 1 274 ? 62.729 -20.550 12.938 1.00 66.43 ? 273 ASN C N 1 ATOM 5825 C CA . ASN C 1 274 ? 63.423 -20.582 11.644 1.00 69.75 ? 273 ASN C CA 1 ATOM 5826 C C . ASN C 1 274 ? 62.777 -21.558 10.658 1.00 70.27 ? 273 ASN C C 1 ATOM 5827 O O . ASN C 1 274 ? 63.413 -22.488 10.173 1.00 73.14 ? 273 ASN C O 1 ATOM 5828 C CB . ASN C 1 274 ? 64.897 -20.937 11.847 1.00 74.17 ? 273 ASN C CB 1 ATOM 5829 C CG . ASN C 1 274 ? 65.630 -19.917 12.696 1.00 75.27 ? 273 ASN C CG 1 ATOM 5830 O OD1 . ASN C 1 274 ? 65.799 -20.104 13.902 1.00 75.84 ? 273 ASN C OD1 1 ATOM 5831 N ND2 . ASN C 1 274 ? 66.060 -18.823 12.071 1.00 75.92 ? 273 ASN C ND2 1 ATOM 5832 N N . CYS C 1 275 ? 61.502 -21.328 10.375 1.00 67.61 ? 274 CYS C N 1 ATOM 5833 C CA . CYS C 1 275 ? 60.702 -22.234 9.561 1.00 67.92 ? 274 CYS C CA 1 ATOM 5834 C C . CYS C 1 275 ? 59.602 -21.443 8.852 1.00 64.98 ? 274 CYS C C 1 ATOM 5835 O O . CYS C 1 275 ? 59.321 -20.296 9.219 1.00 62.19 ? 274 CYS C O 1 ATOM 5836 C CB . CYS C 1 275 ? 60.104 -23.322 10.465 1.00 67.84 ? 274 CYS C CB 1 ATOM 5837 S SG . CYS C 1 275 ? 58.350 -23.715 10.201 1.00 66.35 ? 274 CYS C SG 1 ATOM 5838 N N . ASN C 1 276 ? 58.994 -22.049 7.835 1.00 64.59 ? 275 ASN C N 1 ATOM 5839 C CA . ASN C 1 276 ? 57.858 -21.442 7.141 1.00 61.91 ? 275 ASN C CA 1 ATOM 5840 C C . ASN C 1 276 ? 56.643 -22.364 7.188 1.00 59.86 ? 275 ASN C C 1 ATOM 5841 O O . ASN C 1 276 ? 56.778 -23.583 7.124 1.00 61.53 ? 275 ASN C O 1 ATOM 5842 C CB . ASN C 1 276 ? 58.228 -21.122 5.684 1.00 64.18 ? 275 ASN C CB 1 ATOM 5843 C CG . ASN C 1 276 ? 57.151 -20.321 4.965 1.00 62.23 ? 275 ASN C CG 1 ATOM 5844 O OD1 . ASN C 1 276 ? 56.457 -19.517 5.573 1.00 59.35 ? 275 ASN C OD1 1 ATOM 5845 N ND2 . ASN C 1 276 ? 57.013 -20.538 3.665 1.00 64.38 ? 275 ASN C ND2 1 ATOM 5846 N N . THR C 1 277 ? 55.458 -21.777 7.297 1.00 56.58 ? 276 THR C N 1 ATOM 5847 C CA . THR C 1 277 ? 54.219 -22.552 7.364 1.00 55.07 ? 276 THR C CA 1 ATOM 5848 C C . THR C 1 277 ? 53.064 -21.779 6.757 1.00 53.70 ? 276 THR C C 1 ATOM 5849 O O . THR C 1 277 ? 53.104 -20.554 6.652 1.00 52.47 ? 276 THR C O 1 ATOM 5850 C CB . THR C 1 277 ? 53.853 -22.921 8.817 1.00 52.78 ? 276 THR C CB 1 ATOM 5851 O OG1 . THR C 1 277 ? 52.726 -23.802 8.826 1.00 51.75 ? 276 THR C OG1 1 ATOM 5852 C CG2 . THR C 1 277 ? 53.512 -21.682 9.631 1.00 50.62 ? 276 THR C CG2 1 ATOM 5853 N N . LYS C 1 278 ? 52.036 -22.511 6.360 1.00 54.32 ? 277 LYS C N 1 ATOM 5854 C CA . LYS C 1 278 ? 50.800 -21.895 5.910 1.00 54.21 ? 277 LYS C CA 1 ATOM 5855 C C . LYS C 1 278 ? 49.903 -21.546 7.089 1.00 51.57 ? 277 LYS C C 1 ATOM 5856 O O . LYS C 1 278 ? 49.010 -20.721 6.946 1.00 50.57 ? 277 LYS C O 1 ATOM 5857 C CB . LYS C 1 278 ? 50.044 -22.833 4.962 1.00 56.56 ? 277 LYS C CB 1 ATOM 5858 C CG . LYS C 1 278 ? 50.575 -22.862 3.540 1.00 59.84 ? 277 LYS C CG 1 ATOM 5859 C CD . LYS C 1 278 ? 50.524 -21.483 2.885 1.00 60.42 ? 277 LYS C CD 1 ATOM 5860 C CE . LYS C 1 278 ? 50.360 -21.567 1.370 1.00 63.39 ? 277 LYS C CE 1 ATOM 5861 N NZ . LYS C 1 278 ? 51.247 -22.583 0.736 1.00 66.29 ? 277 LYS C NZ 1 ATOM 5862 N N . CYS C 1 279 ? 50.158 -22.165 8.246 1.00 51.18 ? 278 CYS C N 1 ATOM 5863 C CA . CYS C 1 279 ? 49.210 -22.175 9.367 1.00 49.65 ? 278 CYS C CA 1 ATOM 5864 C C . CYS C 1 279 ? 49.915 -22.242 10.735 1.00 48.46 ? 278 CYS C C 1 ATOM 5865 O O . CYS C 1 279 ? 50.642 -23.194 11.006 1.00 49.71 ? 278 CYS C O 1 ATOM 5866 C CB . CYS C 1 279 ? 48.278 -23.378 9.194 1.00 50.82 ? 278 CYS C CB 1 ATOM 5867 S SG . CYS C 1 279 ? 47.125 -23.682 10.553 1.00 50.79 ? 278 CYS C SG 1 ATOM 5868 N N . GLN C 1 280 ? 49.687 -21.238 11.592 1.00 46.43 ? 279 GLN C N 1 ATOM 5869 C CA . GLN C 1 280 ? 50.352 -21.139 12.902 1.00 45.05 ? 279 GLN C CA 1 ATOM 5870 C C . GLN C 1 280 ? 49.382 -21.116 14.076 1.00 43.66 ? 279 GLN C C 1 ATOM 5871 O O . GLN C 1 280 ? 48.341 -20.470 14.018 1.00 42.47 ? 279 GLN C O 1 ATOM 5872 C CB . GLN C 1 280 ? 51.187 -19.855 12.990 1.00 44.88 ? 279 GLN C CB 1 ATOM 5873 C CG . GLN C 1 280 ? 52.663 -20.020 12.687 1.00 46.77 ? 279 GLN C CG 1 ATOM 5874 C CD . GLN C 1 280 ? 53.429 -20.908 13.667 1.00 47.51 ? 279 GLN C CD 1 ATOM 5875 O OE1 . GLN C 1 280 ? 54.566 -21.258 13.398 1.00 49.27 ? 279 GLN C OE1 1 ATOM 5876 N NE2 . GLN C 1 280 ? 52.824 -21.259 14.797 1.00 46.60 ? 279 GLN C NE2 1 ATOM 5877 N N . THR C 1 281 ? 49.758 -21.794 15.155 1.00 43.66 ? 280 THR C N 1 ATOM 5878 C CA . THR C 1 281 ? 49.090 -21.648 16.445 1.00 43.06 ? 280 THR C CA 1 ATOM 5879 C C . THR C 1 281 ? 50.121 -21.150 17.458 1.00 43.20 ? 280 THR C C 1 ATOM 5880 O O . THR C 1 281 ? 51.303 -21.038 17.123 1.00 44.02 ? 280 THR C O 1 ATOM 5881 C CB . THR C 1 281 ? 48.475 -22.983 16.921 1.00 43.56 ? 280 THR C CB 1 ATOM 5882 O OG1 . THR C 1 281 ? 49.454 -23.753 17.630 1.00 44.49 ? 280 THR C OG1 1 ATOM 5883 C CG2 . THR C 1 281 ? 47.944 -23.785 15.741 1.00 43.92 ? 280 THR C CG2 1 ATOM 5884 N N . PRO C 1 282 ? 49.692 -20.854 18.702 1.00 43.24 ? 281 PRO C N 1 ATOM 5885 C CA . PRO C 1 282 ? 50.667 -20.459 19.721 1.00 44.16 ? 281 PRO C CA 1 ATOM 5886 C C . PRO C 1 282 ? 51.467 -21.639 20.280 1.00 45.57 ? 281 PRO C C 1 ATOM 5887 O O . PRO C 1 282 ? 52.395 -21.431 21.062 1.00 46.08 ? 281 PRO C O 1 ATOM 5888 C CB . PRO C 1 282 ? 49.796 -19.831 20.823 1.00 43.75 ? 281 PRO C CB 1 ATOM 5889 C CG . PRO C 1 282 ? 48.431 -19.690 20.229 1.00 42.90 ? 281 PRO C CG 1 ATOM 5890 C CD . PRO C 1 282 ? 48.329 -20.805 19.245 1.00 42.81 ? 281 PRO C CD 1 ATOM 5891 N N . ILE C 1 283 ? 51.103 -22.854 19.869 1.00 46.17 ? 282 ILE C N 1 ATOM 5892 C CA . ILE C 1 283 ? 51.693 -24.084 20.387 1.00 48.09 ? 282 ILE C CA 1 ATOM 5893 C C . ILE C 1 283 ? 52.630 -24.754 19.369 1.00 48.99 ? 282 ILE C C 1 ATOM 5894 O O . ILE C 1 283 ? 53.461 -25.590 19.738 1.00 51.44 ? 282 ILE C O 1 ATOM 5895 C CB . ILE C 1 283 ? 50.553 -25.038 20.859 1.00 48.55 ? 282 ILE C CB 1 ATOM 5896 C CG1 . ILE C 1 283 ? 50.732 -25.402 22.334 1.00 50.32 ? 282 ILE C CG1 1 ATOM 5897 C CG2 . ILE C 1 283 ? 50.406 -26.281 19.990 1.00 49.14 ? 282 ILE C CG2 1 ATOM 5898 C CD1 . ILE C 1 283 ? 50.446 -24.240 23.266 1.00 50.06 ? 282 ILE C CD1 1 ATOM 5899 N N . GLY C 1 284 ? 52.501 -24.381 18.095 1.00 47.90 ? 283 GLY C N 1 ATOM 5900 C CA . GLY C 1 284 ? 53.260 -24.999 17.009 1.00 48.42 ? 283 GLY C CA 1 ATOM 5901 C C . GLY C 1 284 ? 52.547 -24.818 15.681 1.00 47.38 ? 283 GLY C C 1 ATOM 5902 O O . GLY C 1 284 ? 51.352 -24.533 15.652 1.00 45.74 ? 283 GLY C O 1 ATOM 5903 N N . ALA C 1 285 ? 53.286 -24.977 14.585 1.00 48.65 ? 284 ALA C N 1 ATOM 5904 C CA . ALA C 1 285 ? 52.744 -24.800 13.231 1.00 48.44 ? 284 ALA C CA 1 ATOM 5905 C C . ALA C 1 285 ? 52.123 -26.089 12.720 1.00 49.13 ? 284 ALA C C 1 ATOM 5906 O O . ALA C 1 285 ? 52.432 -27.170 13.214 1.00 50.26 ? 284 ALA C O 1 ATOM 5907 C CB . ALA C 1 285 ? 53.837 -24.341 12.276 1.00 49.80 ? 284 ALA C CB 1 ATOM 5908 N N . ILE C 1 286 ? 51.259 -25.958 11.715 1.00 49.12 ? 285 ILE C N 1 ATOM 5909 C CA . ILE C 1 286 ? 50.536 -27.095 11.137 1.00 50.18 ? 285 ILE C CA 1 ATOM 5910 C C . ILE C 1 286 ? 50.711 -27.166 9.614 1.00 51.72 ? 285 ILE C C 1 ATOM 5911 O O . ILE C 1 286 ? 50.579 -26.159 8.916 1.00 51.22 ? 285 ILE C O 1 ATOM 5912 C CB . ILE C 1 286 ? 49.036 -27.018 11.456 1.00 48.94 ? 285 ILE C CB 1 ATOM 5913 C CG1 . ILE C 1 286 ? 48.821 -26.807 12.954 1.00 47.83 ? 285 ILE C CG1 1 ATOM 5914 C CG2 . ILE C 1 286 ? 48.324 -28.292 11.014 1.00 50.34 ? 285 ILE C CG2 1 ATOM 5915 C CD1 . ILE C 1 286 ? 47.375 -26.564 13.322 1.00 46.79 ? 285 ILE C CD1 1 ATOM 5916 N N . ASN C 1 287 ? 51.017 -28.368 9.125 1.00 53.69 ? 286 ASN C N 1 ATOM 5917 C CA . ASN C 1 287 ? 51.132 -28.660 7.701 1.00 55.94 ? 286 ASN C CA 1 ATOM 5918 C C . ASN C 1 287 ? 50.331 -29.928 7.427 1.00 57.18 ? 286 ASN C C 1 ATOM 5919 O O . ASN C 1 287 ? 50.781 -31.037 7.727 1.00 57.86 ? 286 ASN C O 1 ATOM 5920 C CB . ASN C 1 287 ? 52.596 -28.871 7.302 1.00 58.33 ? 286 ASN C CB 1 ATOM 5921 C CG . ASN C 1 287 ? 52.773 -29.084 5.806 1.00 61.08 ? 286 ASN C CG 1 ATOM 5922 O OD1 . ASN C 1 287 ? 52.150 -28.403 4.996 1.00 61.05 ? 286 ASN C OD1 1 ATOM 5923 N ND2 . ASN C 1 287 ? 53.639 -30.022 5.434 1.00 64.17 ? 286 ASN C ND2 1 ATOM 5924 N N . SER C 1 288 ? 49.140 -29.748 6.864 1.00 57.23 ? 287 SER C N 1 ATOM 5925 C CA . SER C 1 288 ? 48.146 -30.809 6.807 1.00 58.31 ? 287 SER C CA 1 ATOM 5926 C C . SER C 1 288 ? 47.159 -30.583 5.668 1.00 59.79 ? 287 SER C C 1 ATOM 5927 O O . SER C 1 288 ? 46.799 -29.448 5.366 1.00 59.14 ? 287 SER C O 1 ATOM 5928 C CB . SER C 1 288 ? 47.393 -30.854 8.142 1.00 56.18 ? 287 SER C CB 1 ATOM 5929 O OG . SER C 1 288 ? 46.396 -31.858 8.163 1.00 56.74 ? 287 SER C OG 1 ATOM 5930 N N . SER C 1 289 ? 46.726 -31.672 5.038 1.00 62.61 ? 288 SER C N 1 ATOM 5931 C CA . SER C 1 289 ? 45.648 -31.613 4.054 1.00 64.34 ? 288 SER C CA 1 ATOM 5932 C C . SER C 1 289 ? 44.311 -32.077 4.651 1.00 63.75 ? 288 SER C C 1 ATOM 5933 O O . SER C 1 289 ? 43.339 -32.262 3.917 1.00 66.09 ? 288 SER C O 1 ATOM 5934 C CB . SER C 1 289 ? 46.005 -32.454 2.825 1.00 67.74 ? 288 SER C CB 1 ATOM 5935 O OG . SER C 1 289 ? 46.001 -33.835 3.126 1.00 68.89 ? 288 SER C OG 1 ATOM 5936 N N . MET C 1 290 ? 44.264 -32.253 5.973 1.00 61.64 ? 289 MET C N 1 ATOM 5937 C CA . MET C 1 290 ? 43.039 -32.661 6.674 1.00 60.89 ? 289 MET C CA 1 ATOM 5938 C C . MET C 1 290 ? 42.060 -31.496 6.737 1.00 59.24 ? 289 MET C C 1 ATOM 5939 O O . MET C 1 290 ? 42.477 -30.347 6.663 1.00 57.94 ? 289 MET C O 1 ATOM 5940 C CB . MET C 1 290 ? 43.348 -33.096 8.108 1.00 59.45 ? 289 MET C CB 1 ATOM 5941 C CG . MET C 1 290 ? 44.292 -34.274 8.242 1.00 60.87 ? 289 MET C CG 1 ATOM 5942 S SD . MET C 1 290 ? 43.536 -35.835 7.769 1.00 64.08 ? 289 MET C SD 1 ATOM 5943 C CE . MET C 1 290 ? 44.452 -36.949 8.834 1.00 63.86 ? 289 MET C CE 1 ATOM 5944 N N . PRO C 1 291 ? 40.756 -31.789 6.881 1.00 59.40 ? 290 PRO C N 1 ATOM 5945 C CA . PRO C 1 291 ? 39.753 -30.734 7.055 1.00 58.78 ? 290 PRO C CA 1 ATOM 5946 C C . PRO C 1 291 ? 39.649 -30.207 8.496 1.00 56.51 ? 290 PRO C C 1 ATOM 5947 O O . PRO C 1 291 ? 39.266 -29.053 8.697 1.00 55.89 ? 290 PRO C O 1 ATOM 5948 C CB . PRO C 1 291 ? 38.452 -31.422 6.636 1.00 61.06 ? 290 PRO C CB 1 ATOM 5949 C CG . PRO C 1 291 ? 38.674 -32.855 6.970 1.00 61.56 ? 290 PRO C CG 1 ATOM 5950 C CD . PRO C 1 291 ? 40.137 -33.121 6.748 1.00 61.09 ? 290 PRO C CD 1 ATOM 5951 N N . PHE C 1 292 ? 39.987 -31.042 9.478 1.00 55.63 ? 291 PHE C N 1 ATOM 5952 C CA . PHE C 1 292 ? 39.902 -30.663 10.889 1.00 54.02 ? 291 PHE C CA 1 ATOM 5953 C C . PHE C 1 292 ? 41.245 -30.793 11.599 1.00 52.64 ? 291 PHE C C 1 ATOM 5954 O O . PHE C 1 292 ? 42.163 -31.428 11.095 1.00 53.27 ? 291 PHE C O 1 ATOM 5955 C CB . PHE C 1 292 ? 38.891 -31.548 11.623 1.00 54.69 ? 291 PHE C CB 1 ATOM 5956 C CG . PHE C 1 292 ? 37.486 -31.446 11.100 1.00 56.24 ? 291 PHE C CG 1 ATOM 5957 C CD1 . PHE C 1 292 ? 36.784 -30.251 11.186 1.00 56.12 ? 291 PHE C CD1 1 ATOM 5958 C CD2 . PHE C 1 292 ? 36.853 -32.555 10.545 1.00 58.28 ? 291 PHE C CD2 1 ATOM 5959 C CE1 . PHE C 1 292 ? 35.483 -30.159 10.718 1.00 57.98 ? 291 PHE C CE1 1 ATOM 5960 C CE2 . PHE C 1 292 ? 35.552 -32.469 10.078 1.00 60.01 ? 291 PHE C CE2 1 ATOM 5961 C CZ . PHE C 1 292 ? 34.869 -31.269 10.163 1.00 60.15 ? 291 PHE C CZ 1 ATOM 5962 N N . HIS C 1 293 ? 41.334 -30.188 12.779 1.00 51.57 ? 292 HIS C N 1 ATOM 5963 C CA . HIS C 1 293 ? 42.483 -30.348 13.675 1.00 51.25 ? 292 HIS C CA 1 ATOM 5964 C C . HIS C 1 293 ? 42.066 -30.050 15.115 1.00 50.34 ? 292 HIS C C 1 ATOM 5965 O O . HIS C 1 293 ? 41.057 -29.388 15.332 1.00 50.42 ? 292 HIS C O 1 ATOM 5966 C CB . HIS C 1 293 ? 43.628 -29.419 13.267 1.00 50.99 ? 292 HIS C CB 1 ATOM 5967 C CG . HIS C 1 293 ? 43.359 -27.967 13.532 1.00 50.17 ? 292 HIS C CG 1 ATOM 5968 N ND1 . HIS C 1 293 ? 43.950 -27.275 14.569 1.00 49.06 ? 292 HIS C ND1 1 ATOM 5969 C CD2 . HIS C 1 293 ? 42.569 -27.075 12.888 1.00 50.24 ? 292 HIS C CD2 1 ATOM 5970 C CE1 . HIS C 1 293 ? 43.535 -26.021 14.554 1.00 48.24 ? 292 HIS C CE1 1 ATOM 5971 N NE2 . HIS C 1 293 ? 42.696 -25.872 13.545 1.00 49.21 ? 292 HIS C NE2 1 ATOM 5972 N N . ASN C 1 294 ? 42.831 -30.540 16.090 1.00 50.12 ? 293 ASN C N 1 ATOM 5973 C CA . ASN C 1 294 ? 42.547 -30.257 17.501 1.00 50.20 ? 293 ASN C CA 1 ATOM 5974 C C . ASN C 1 294 ? 43.762 -29.707 18.242 1.00 49.55 ? 293 ASN C C 1 ATOM 5975 O O . ASN C 1 294 ? 43.907 -29.902 19.449 1.00 50.48 ? 293 ASN C O 1 ATOM 5976 C CB . ASN C 1 294 ? 41.993 -31.498 18.207 1.00 51.57 ? 293 ASN C CB 1 ATOM 5977 C CG . ASN C 1 294 ? 43.015 -32.615 18.334 1.00 52.93 ? 293 ASN C CG 1 ATOM 5978 O OD1 . ASN C 1 294 ? 44.114 -32.551 17.776 1.00 53.10 ? 293 ASN C OD1 1 ATOM 5979 N ND2 . ASN C 1 294 ? 42.648 -33.659 19.068 1.00 54.41 ? 293 ASN C ND2 1 ATOM 5980 N N . ILE C 1 295 ? 44.612 -28.989 17.516 1.00 48.79 ? 294 ILE C N 1 ATOM 5981 C CA . ILE C 1 295 ? 45.871 -28.488 18.056 1.00 48.30 ? 294 ILE C CA 1 ATOM 5982 C C . ILE C 1 295 ? 45.605 -27.340 19.021 1.00 47.20 ? 294 ILE C C 1 ATOM 5983 O O . ILE C 1 295 ? 45.931 -27.426 20.205 1.00 47.14 ? 294 ILE C O 1 ATOM 5984 C CB . ILE C 1 295 ? 46.817 -27.995 16.931 1.00 48.21 ? 294 ILE C CB 1 ATOM 5985 C CG1 . ILE C 1 295 ? 47.053 -29.098 15.891 1.00 49.61 ? 294 ILE C CG1 1 ATOM 5986 C CG2 . ILE C 1 295 ? 48.132 -27.482 17.511 1.00 48.37 ? 294 ILE C CG2 1 ATOM 5987 C CD1 . ILE C 1 295 ? 47.496 -30.432 16.458 1.00 51.18 ? 294 ILE C CD1 1 ATOM 5988 N N . HIS C 1 296 ? 45.010 -26.272 18.495 1.00 46.46 ? 295 HIS C N 1 ATOM 5989 C CA . HIS C 1 296 ? 44.705 -25.063 19.264 1.00 45.99 ? 295 HIS C CA 1 ATOM 5990 C C . HIS C 1 296 ? 43.548 -24.338 18.556 1.00 45.54 ? 295 HIS C C 1 ATOM 5991 O O . HIS C 1 296 ? 43.451 -24.405 17.326 1.00 44.62 ? 295 HIS C O 1 ATOM 5992 C CB . HIS C 1 296 ? 45.947 -24.167 19.321 1.00 45.69 ? 295 HIS C CB 1 ATOM 5993 C CG . HIS C 1 296 ? 46.008 -23.280 20.525 1.00 46.22 ? 295 HIS C CG 1 ATOM 5994 N ND1 . HIS C 1 296 ? 45.620 -21.957 20.494 1.00 45.75 ? 295 HIS C ND1 1 ATOM 5995 C CD2 . HIS C 1 296 ? 46.421 -23.519 21.793 1.00 47.38 ? 295 HIS C CD2 1 ATOM 5996 C CE1 . HIS C 1 296 ? 45.777 -21.422 21.692 1.00 46.20 ? 295 HIS C CE1 1 ATOM 5997 N NE2 . HIS C 1 296 ? 46.265 -22.347 22.498 1.00 47.54 ? 295 HIS C NE2 1 ATOM 5998 N N . PRO C 1 297 ? 42.655 -23.665 19.316 1.00 45.56 ? 296 PRO C N 1 ATOM 5999 C CA . PRO C 1 297 ? 41.590 -22.881 18.672 1.00 45.68 ? 296 PRO C CA 1 ATOM 6000 C C . PRO C 1 297 ? 42.081 -21.604 17.984 1.00 44.68 ? 296 PRO C C 1 ATOM 6001 O O . PRO C 1 297 ? 41.536 -21.214 16.955 1.00 45.33 ? 296 PRO C O 1 ATOM 6002 C CB . PRO C 1 297 ? 40.657 -22.522 19.835 1.00 46.74 ? 296 PRO C CB 1 ATOM 6003 C CG . PRO C 1 297 ? 41.513 -22.599 21.049 1.00 46.78 ? 296 PRO C CG 1 ATOM 6004 C CD . PRO C 1 297 ? 42.479 -23.717 20.777 1.00 46.43 ? 296 PRO C CD 1 ATOM 6005 N N . LEU C 1 298 ? 43.078 -20.946 18.564 1.00 43.86 ? 297 LEU C N 1 ATOM 6006 C CA . LEU C 1 298 ? 43.581 -19.681 18.027 1.00 42.90 ? 297 LEU C CA 1 ATOM 6007 C C . LEU C 1 298 ? 44.640 -19.934 16.965 1.00 41.69 ? 297 LEU C C 1 ATOM 6008 O O . LEU C 1 298 ? 45.771 -20.290 17.286 1.00 42.01 ? 297 LEU C O 1 ATOM 6009 C CB . LEU C 1 298 ? 44.147 -18.797 19.143 1.00 43.18 ? 297 LEU C CB 1 ATOM 6010 C CG . LEU C 1 298 ? 43.125 -18.016 19.980 1.00 44.77 ? 297 LEU C CG 1 ATOM 6011 C CD1 . LEU C 1 298 ? 42.150 -18.915 20.720 1.00 46.32 ? 297 LEU C CD1 1 ATOM 6012 C CD2 . LEU C 1 298 ? 43.847 -17.125 20.977 1.00 45.44 ? 297 LEU C CD2 1 ATOM 6013 N N . THR C 1 299 ? 44.269 -19.773 15.698 1.00 40.87 ? 298 THR C N 1 ATOM 6014 C CA . THR C 1 299 ? 45.216 -19.952 14.600 1.00 40.46 ? 298 THR C CA 1 ATOM 6015 C C . THR C 1 299 ? 45.212 -18.760 13.660 1.00 39.99 ? 298 THR C C 1 ATOM 6016 O O . THR C 1 299 ? 44.322 -17.912 13.721 1.00 40.31 ? 298 THR C O 1 ATOM 6017 C CB . THR C 1 299 ? 44.905 -21.222 13.771 1.00 40.90 ? 298 THR C CB 1 ATOM 6018 O OG1 . THR C 1 299 ? 43.635 -21.088 13.115 1.00 41.10 ? 298 THR C OG1 1 ATOM 6019 C CG2 . THR C 1 299 ? 44.886 -22.443 14.656 1.00 41.38 ? 298 THR C CG2 1 ATOM 6020 N N . ILE C 1 300 ? 46.208 -18.715 12.782 1.00 39.79 ? 299 ILE C N 1 ATOM 6021 C CA . ILE C 1 300 ? 46.195 -17.802 11.645 1.00 40.07 ? 299 ILE C CA 1 ATOM 6022 C C . ILE C 1 300 ? 46.784 -18.486 10.405 1.00 41.29 ? 299 ILE C C 1 ATOM 6023 O O . ILE C 1 300 ? 47.649 -19.355 10.519 1.00 41.60 ? 299 ILE C O 1 ATOM 6024 C CB . ILE C 1 300 ? 46.944 -16.493 11.968 1.00 39.05 ? 299 ILE C CB 1 ATOM 6025 C CG1 . ILE C 1 300 ? 46.621 -15.422 10.931 1.00 39.36 ? 299 ILE C CG1 1 ATOM 6026 C CG2 . ILE C 1 300 ? 48.446 -16.733 12.068 1.00 39.22 ? 299 ILE C CG2 1 ATOM 6027 C CD1 . ILE C 1 300 ? 47.182 -14.058 11.282 1.00 38.96 ? 299 ILE C CD1 1 ATOM 6028 N N . GLY C 1 301 ? 46.298 -18.091 9.231 1.00 42.28 ? 300 GLY C N 1 ATOM 6029 C CA . GLY C 1 301 ? 46.761 -18.640 7.966 1.00 44.47 ? 300 GLY C CA 1 ATOM 6030 C C . GLY C 1 301 ? 45.704 -19.520 7.332 1.00 46.13 ? 300 GLY C C 1 ATOM 6031 O O . GLY C 1 301 ? 44.567 -19.560 7.800 1.00 46.84 ? 300 GLY C O 1 ATOM 6032 N N . GLU C 1 302 ? 46.063 -20.212 6.257 1.00 80.22 ? 301 GLU C N 1 ATOM 6033 C CA . GLU C 1 302 ? 45.153 -21.176 5.641 1.00 81.53 ? 301 GLU C CA 1 ATOM 6034 C C . GLU C 1 302 ? 45.164 -22.448 6.476 1.00 78.12 ? 301 GLU C C 1 ATOM 6035 O O . GLU C 1 302 ? 45.942 -23.365 6.218 1.00 80.18 ? 301 GLU C O 1 ATOM 6036 C CB . GLU C 1 302 ? 45.559 -21.472 4.195 1.00 88.16 ? 301 GLU C CB 1 ATOM 6037 C CG . GLU C 1 302 ? 45.406 -20.289 3.251 1.00 93.00 ? 301 GLU C CG 1 ATOM 6038 N N . CYS C 1 303 ? 44.305 -22.487 7.491 1.00 73.76 ? 302 CYS C N 1 ATOM 6039 C CA . CYS C 1 303 ? 44.238 -23.618 8.411 1.00 70.85 ? 302 CYS C CA 1 ATOM 6040 C C . CYS C 1 303 ? 42.985 -24.459 8.175 1.00 69.73 ? 302 CYS C C 1 ATOM 6041 O O . CYS C 1 303 ? 42.019 -23.982 7.583 1.00 70.69 ? 302 CYS C O 1 ATOM 6042 C CB . CYS C 1 303 ? 44.234 -23.124 9.865 1.00 67.60 ? 302 CYS C CB 1 ATOM 6043 S SG . CYS C 1 303 ? 45.718 -22.214 10.376 1.00 69.05 ? 302 CYS C SG 1 ATOM 6044 N N . PRO C 1 304 ? 42.997 -25.718 8.646 1.00 67.66 ? 303 PRO C N 1 ATOM 6045 C CA . PRO C 1 304 ? 41.751 -26.470 8.753 1.00 66.47 ? 303 PRO C CA 1 ATOM 6046 C C . PRO C 1 304 ? 40.912 -25.954 9.923 1.00 62.98 ? 303 PRO C C 1 ATOM 6047 O O . PRO C 1 304 ? 41.390 -25.129 10.703 1.00 61.33 ? 303 PRO C O 1 ATOM 6048 C CB . PRO C 1 304 ? 42.211 -27.912 9.021 1.00 66.04 ? 303 PRO C CB 1 ATOM 6049 C CG . PRO C 1 304 ? 43.702 -27.895 9.067 1.00 67.33 ? 303 PRO C CG 1 ATOM 6050 C CD . PRO C 1 304 ? 44.152 -26.475 9.153 1.00 67.31 ? 303 PRO C CD 1 ATOM 6051 N N . LYS C 1 305 ? 39.684 -26.447 10.059 1.00 62.41 ? 304 LYS C N 1 ATOM 6052 C CA . LYS C 1 305 ? 38.793 -26.000 11.138 1.00 60.04 ? 304 LYS C CA 1 ATOM 6053 C C . LYS C 1 305 ? 39.064 -26.754 12.437 1.00 56.94 ? 304 LYS C C 1 ATOM 6054 O O . LYS C 1 305 ? 39.227 -27.967 12.432 1.00 57.21 ? 304 LYS C O 1 ATOM 6055 C CB . LYS C 1 305 ? 37.325 -26.166 10.732 1.00 61.79 ? 304 LYS C CB 1 ATOM 6056 C CG . LYS C 1 305 ? 36.927 -25.396 9.476 1.00 65.51 ? 304 LYS C CG 1 ATOM 6057 C CD . LYS C 1 305 ? 37.047 -23.890 9.666 1.00 65.64 ? 304 LYS C CD 1 ATOM 6058 C CE . LYS C 1 305 ? 36.345 -23.142 8.544 1.00 70.03 ? 304 LYS C CE 1 ATOM 6059 N NZ . LYS C 1 305 ? 36.499 -21.661 8.643 1.00 70.73 ? 304 LYS C NZ 1 ATOM 6060 N N . TYR C 1 306 ? 39.095 -26.025 13.546 1.00 54.92 ? 305 TYR C N 1 ATOM 6061 C CA . TYR C 1 306 ? 39.388 -26.606 14.856 1.00 53.24 ? 305 TYR C CA 1 ATOM 6062 C C . TYR C 1 306 ? 38.166 -27.288 15.483 1.00 53.38 ? 305 TYR C C 1 ATOM 6063 O O . TYR C 1 306 ? 37.041 -26.802 15.360 1.00 53.96 ? 305 TYR C O 1 ATOM 6064 C CB . TYR C 1 306 ? 39.918 -25.524 15.812 1.00 51.70 ? 305 TYR C CB 1 ATOM 6065 C CG . TYR C 1 306 ? 40.156 -26.013 17.228 1.00 50.66 ? 305 TYR C CG 1 ATOM 6066 C CD1 . TYR C 1 306 ? 41.309 -26.711 17.567 1.00 50.71 ? 305 TYR C CD1 1 ATOM 6067 C CD2 . TYR C 1 306 ? 39.224 -25.778 18.223 1.00 50.61 ? 305 TYR C CD2 1 ATOM 6068 C CE1 . TYR C 1 306 ? 41.521 -27.152 18.858 1.00 50.95 ? 305 TYR C CE1 1 ATOM 6069 C CE2 . TYR C 1 306 ? 39.426 -26.214 19.517 1.00 50.74 ? 305 TYR C CE2 1 ATOM 6070 C CZ . TYR C 1 306 ? 40.573 -26.903 19.834 1.00 50.99 ? 305 TYR C CZ 1 ATOM 6071 O OH . TYR C 1 306 ? 40.759 -27.340 21.130 1.00 51.82 ? 305 TYR C OH 1 ATOM 6072 N N . VAL C 1 307 ? 38.404 -28.416 16.149 1.00 53.49 ? 306 VAL C N 1 ATOM 6073 C CA . VAL C 1 307 ? 37.398 -29.070 16.992 1.00 54.12 ? 306 VAL C CA 1 ATOM 6074 C C . VAL C 1 307 ? 38.063 -29.632 18.248 1.00 54.39 ? 306 VAL C C 1 ATOM 6075 O O . VAL C 1 307 ? 39.289 -29.765 18.296 1.00 54.44 ? 306 VAL C O 1 ATOM 6076 C CB . VAL C 1 307 ? 36.666 -30.207 16.252 1.00 55.01 ? 306 VAL C CB 1 ATOM 6077 C CG1 . VAL C 1 307 ? 35.845 -29.651 15.099 1.00 56.06 ? 306 VAL C CG1 1 ATOM 6078 C CG2 . VAL C 1 307 ? 37.646 -31.266 15.762 1.00 55.16 ? 306 VAL C CG2 1 ATOM 6079 N N . LYS C 1 308 ? 37.255 -29.970 19.253 1.00 55.57 ? 307 LYS C N 1 ATOM 6080 C CA . LYS C 1 308 ? 37.776 -30.482 20.528 1.00 57.00 ? 307 LYS C CA 1 ATOM 6081 C C . LYS C 1 308 ? 37.891 -32.011 20.570 1.00 58.21 ? 307 LYS C C 1 ATOM 6082 O O . LYS C 1 308 ? 38.231 -32.579 21.611 1.00 60.30 ? 307 LYS C O 1 ATOM 6083 C CB . LYS C 1 308 ? 36.917 -29.989 21.700 1.00 58.39 ? 307 LYS C CB 1 ATOM 6084 C CG . LYS C 1 308 ? 36.908 -28.478 21.869 1.00 57.85 ? 307 LYS C CG 1 ATOM 6085 C CD . LYS C 1 308 ? 36.395 -28.077 23.241 1.00 60.13 ? 307 LYS C CD 1 ATOM 6086 C CE . LYS C 1 308 ? 36.411 -26.567 23.406 1.00 59.95 ? 307 LYS C CE 1 ATOM 6087 N NZ . LYS C 1 308 ? 36.004 -26.147 24.777 1.00 62.66 ? 307 LYS C NZ 1 ATOM 6088 N N . SER C 1 309 ? 37.630 -32.662 19.437 1.00 57.96 ? 308 SER C N 1 ATOM 6089 C CA . SER C 1 309 ? 37.620 -34.121 19.339 1.00 58.87 ? 308 SER C CA 1 ATOM 6090 C C . SER C 1 309 ? 38.996 -34.734 19.534 1.00 60.02 ? 308 SER C C 1 ATOM 6091 O O . SER C 1 309 ? 39.993 -34.226 19.024 1.00 59.74 ? 308 SER C O 1 ATOM 6092 C CB . SER C 1 309 ? 37.111 -34.552 17.968 1.00 58.43 ? 308 SER C CB 1 ATOM 6093 O OG . SER C 1 309 ? 35.937 -33.853 17.613 1.00 58.61 ? 308 SER C OG 1 ATOM 6094 N N . SER C 1 310 ? 39.041 -35.842 20.262 1.00 62.27 ? 309 SER C N 1 ATOM 6095 C CA . SER C 1 310 ? 40.258 -36.637 20.374 1.00 63.88 ? 309 SER C CA 1 ATOM 6096 C C . SER C 1 310 ? 40.498 -37.438 19.095 1.00 63.75 ? 309 SER C C 1 ATOM 6097 O O . SER C 1 310 ? 41.642 -37.700 18.738 1.00 65.12 ? 309 SER C O 1 ATOM 6098 C CB . SER C 1 310 ? 40.173 -37.569 21.582 1.00 66.69 ? 309 SER C CB 1 ATOM 6099 O OG . SER C 1 310 ? 38.865 -38.100 21.714 1.00 66.91 ? 309 SER C OG 1 ATOM 6100 N N . ARG C 1 311 ? 39.422 -37.812 18.404 1.00 62.92 ? 310 ARG C N 1 ATOM 6101 C CA . ARG C 1 311 ? 39.517 -38.673 17.225 1.00 63.52 ? 310 ARG C CA 1 ATOM 6102 C C . ARG C 1 311 ? 38.348 -38.465 16.267 1.00 62.17 ? 310 ARG C C 1 ATOM 6103 O O . ARG C 1 311 ? 37.204 -38.342 16.698 1.00 61.79 ? 310 ARG C O 1 ATOM 6104 C CB . ARG C 1 311 ? 39.578 -40.140 17.660 1.00 65.98 ? 310 ARG C CB 1 ATOM 6105 C CG . ARG C 1 311 ? 39.641 -41.148 16.516 1.00 67.08 ? 310 ARG C CG 1 ATOM 6106 C CD . ARG C 1 311 ? 40.487 -42.355 16.905 1.00 70.38 ? 310 ARG C CD 1 ATOM 6107 N NE . ARG C 1 311 ? 40.635 -43.337 15.829 1.00 71.56 ? 310 ARG C NE 1 ATOM 6108 C CZ . ARG C 1 311 ? 39.737 -44.271 15.517 1.00 71.89 ? 310 ARG C CZ 1 ATOM 6109 N NH1 . ARG C 1 311 ? 38.589 -44.366 16.182 1.00 71.00 ? 310 ARG C NH1 1 ATOM 6110 N NH2 . ARG C 1 311 ? 39.985 -45.121 14.526 1.00 73.66 ? 310 ARG C NH2 1 ATOM 6111 N N . LEU C 1 312 ? 38.648 -38.443 14.969 1.00 62.73 ? 311 LEU C N 1 ATOM 6112 C CA . LEU C 1 312 ? 37.634 -38.277 13.924 1.00 62.57 ? 311 LEU C CA 1 ATOM 6113 C C . LEU C 1 312 ? 38.046 -39.057 12.671 1.00 64.42 ? 311 LEU C C 1 ATOM 6114 O O . LEU C 1 312 ? 38.965 -38.649 11.949 1.00 65.35 ? 311 LEU C O 1 ATOM 6115 C CB . LEU C 1 312 ? 37.466 -36.793 13.601 1.00 61.93 ? 311 LEU C CB 1 ATOM 6116 C CG . LEU C 1 312 ? 36.085 -36.233 13.247 1.00 62.22 ? 311 LEU C CG 1 ATOM 6117 C CD1 . LEU C 1 312 ? 35.041 -36.566 14.307 1.00 62.10 ? 311 LEU C CD1 1 ATOM 6118 C CD2 . LEU C 1 312 ? 36.191 -34.723 13.065 1.00 61.48 ? 311 LEU C CD2 1 ATOM 6119 N N . VAL C 1 313 ? 37.380 -40.189 12.434 1.00 65.19 ? 312 VAL C N 1 ATOM 6120 C CA . VAL C 1 313 ? 37.693 -41.070 11.300 1.00 67.22 ? 312 VAL C CA 1 ATOM 6121 C C . VAL C 1 313 ? 36.416 -41.535 10.599 1.00 67.69 ? 312 VAL C C 1 ATOM 6122 O O . VAL C 1 313 ? 35.536 -42.122 11.228 1.00 66.79 ? 312 VAL C O 1 ATOM 6123 C CB . VAL C 1 313 ? 38.483 -42.317 11.754 1.00 68.65 ? 312 VAL C CB 1 ATOM 6124 C CG1 . VAL C 1 313 ? 38.754 -43.252 10.574 1.00 71.43 ? 312 VAL C CG1 1 ATOM 6125 C CG2 . VAL C 1 313 ? 39.784 -41.909 12.429 1.00 69.04 ? 312 VAL C CG2 1 ATOM 6126 N N . LEU C 1 314 ? 36.332 -41.274 9.295 1.00 69.44 ? 313 LEU C N 1 ATOM 6127 C CA . LEU C 1 314 ? 35.179 -41.675 8.488 1.00 70.90 ? 313 LEU C CA 1 ATOM 6128 C C . LEU C 1 314 ? 35.379 -43.065 7.890 1.00 73.27 ? 313 LEU C C 1 ATOM 6129 O O . LEU C 1 314 ? 36.489 -43.423 7.478 1.00 75.01 ? 313 LEU C O 1 ATOM 6130 C CB . LEU C 1 314 ? 34.936 -40.674 7.352 1.00 72.69 ? 313 LEU C CB 1 ATOM 6131 C CG . LEU C 1 314 ? 34.101 -39.433 7.671 1.00 71.89 ? 313 LEU C CG 1 ATOM 6132 C CD1 . LEU C 1 314 ? 34.242 -38.401 6.561 1.00 74.37 ? 313 LEU C CD1 1 ATOM 6133 C CD2 . LEU C 1 314 ? 32.637 -39.794 7.883 1.00 72.12 ? 313 LEU C CD2 1 ATOM 6134 N N . ALA C 1 315 ? 34.299 -43.838 7.830 1.00 73.56 ? 314 ALA C N 1 ATOM 6135 C CA . ALA C 1 315 ? 34.325 -45.131 7.163 1.00 75.81 ? 314 ALA C CA 1 ATOM 6136 C C . ALA C 1 315 ? 34.162 -44.908 5.665 1.00 79.41 ? 314 ALA C C 1 ATOM 6137 O O . ALA C 1 315 ? 33.462 -43.988 5.240 1.00 80.06 ? 314 ALA C O 1 ATOM 6138 C CB . ALA C 1 315 ? 33.220 -46.032 7.690 1.00 75.06 ? 314 ALA C CB 1 ATOM 6139 N N . THR C 1 316 ? 34.832 -45.742 4.875 1.00 82.45 ? 315 THR C N 1 ATOM 6140 C CA . THR C 1 316 ? 34.688 -45.733 3.419 1.00 86.92 ? 315 THR C CA 1 ATOM 6141 C C . THR C 1 316 ? 34.444 -47.150 2.899 1.00 89.17 ? 315 THR C C 1 ATOM 6142 O O . THR C 1 316 ? 33.508 -47.377 2.132 1.00 91.47 ? 315 THR C O 1 ATOM 6143 C CB . THR C 1 316 ? 35.924 -45.125 2.727 1.00 89.68 ? 315 THR C CB 1 ATOM 6144 O OG1 . THR C 1 316 ? 37.120 -45.615 3.347 1.00 89.18 ? 315 THR C OG1 1 ATOM 6145 C CG2 . THR C 1 316 ? 35.896 -43.611 2.825 1.00 88.61 ? 315 THR C CG2 1 ATOM 6146 N N . GLY C 1 317 ? 35.285 -48.092 3.326 1.00 89.10 ? 316 GLY C N 1 ATOM 6147 C CA . GLY C 1 317 ? 35.124 -49.506 2.994 1.00 91.03 ? 316 GLY C CA 1 ATOM 6148 C C . GLY C 1 317 ? 34.064 -50.202 3.829 1.00 88.71 ? 316 GLY C C 1 ATOM 6149 O O . GLY C 1 317 ? 33.167 -49.555 4.368 1.00 86.71 ? 316 GLY C O 1 ATOM 6150 N N . LEU C 1 318 ? 34.178 -51.524 3.940 1.00 89.88 ? 317 LEU C N 1 ATOM 6151 C CA . LEU C 1 318 ? 33.168 -52.358 4.601 1.00 88.63 ? 317 LEU C CA 1 ATOM 6152 C C . LEU C 1 318 ? 33.716 -52.992 5.876 1.00 86.67 ? 317 LEU C C 1 ATOM 6153 O O . LEU C 1 318 ? 34.877 -52.789 6.221 1.00 86.48 ? 317 LEU C O 1 ATOM 6154 C CB . LEU C 1 318 ? 32.700 -53.473 3.654 1.00 92.04 ? 317 LEU C CB 1 ATOM 6155 C CG . LEU C 1 318 ? 32.211 -53.075 2.258 1.00 95.64 ? 317 LEU C CG 1 ATOM 6156 C CD1 . LEU C 1 318 ? 33.368 -52.844 1.290 1.00 99.29 ? 317 LEU C CD1 1 ATOM 6157 C CD2 . LEU C 1 318 ? 31.277 -54.148 1.717 1.00 97.64 ? 317 LEU C CD2 1 ATOM 6158 N N . ARG C 1 319 ? 32.878 -53.779 6.554 1.00 85.56 ? 318 ARG C N 1 ATOM 6159 C CA . ARG C 1 319 ? 33.283 -54.525 7.751 1.00 84.90 ? 318 ARG C CA 1 ATOM 6160 C C . ARG C 1 319 ? 34.343 -55.594 7.450 1.00 87.66 ? 318 ARG C C 1 ATOM 6161 O O . ARG C 1 319 ? 34.575 -55.948 6.292 1.00 89.71 ? 318 ARG C O 1 ATOM 6162 C CB . ARG C 1 319 ? 32.075 -55.221 8.393 1.00 83.96 ? 318 ARG C CB 1 ATOM 6163 C CG . ARG C 1 319 ? 30.960 -54.304 8.868 1.00 81.98 ? 318 ARG C CG 1 ATOM 6164 C CD . ARG C 1 319 ? 29.834 -55.128 9.478 1.00 82.21 ? 318 ARG C CD 1 ATOM 6165 N NE . ARG C 1 319 ? 28.652 -54.328 9.794 1.00 81.36 ? 318 ARG C NE 1 ATOM 6166 C CZ . ARG C 1 319 ? 28.428 -53.701 10.950 1.00 80.48 ? 318 ARG C CZ 1 ATOM 6167 N NH1 . ARG C 1 319 ? 29.306 -53.757 11.952 1.00 79.79 ? 318 ARG C NH1 1 ATOM 6168 N NH2 . ARG C 1 319 ? 27.309 -53.002 11.105 1.00 80.56 ? 318 ARG C NH2 1 ATOM 6169 N N . ASN C 1 320 ? 34.968 -56.105 8.511 1.00 88.12 ? 319 ASN C N 1 ATOM 6170 C CA . ASN C 1 320 ? 35.941 -57.192 8.414 1.00 91.49 ? 319 ASN C CA 1 ATOM 6171 C C . ASN C 1 320 ? 35.627 -58.328 9.384 1.00 92.10 ? 319 ASN C C 1 ATOM 6172 O O . ASN C 1 320 ? 35.524 -59.490 8.979 1.00 93.98 ? 319 ASN C O 1 ATOM 6173 C CB . ASN C 1 320 ? 37.367 -56.668 8.654 1.00 93.03 ? 319 ASN C CB 1 ATOM 6174 C CG . ASN C 1 320 ? 38.281 -56.860 7.448 1.00 96.68 ? 319 ASN C CG 1 ATOM 6175 O OD1 . ASN C 1 320 ? 38.069 -57.752 6.617 1.00 99.24 ? 319 ASN C OD1 1 ATOM 6176 N ND2 . ASN C 1 320 ? 39.320 -56.037 7.363 1.00 97.52 ? 319 ASN C ND2 1 ATOM 6177 N N . ILE D 2 10 ? 25.000 -64.512 3.654 1.00 164.67 ? 10 ILE D N 1 ATOM 6178 C CA . ILE D 2 10 ? 26.471 -64.481 3.388 1.00 164.41 ? 10 ILE D CA 1 ATOM 6179 C C . ILE D 2 10 ? 27.238 -64.836 4.662 1.00 166.13 ? 10 ILE D C 1 ATOM 6180 O O . ILE D 2 10 ? 26.919 -64.339 5.741 1.00 166.14 ? 10 ILE D O 1 ATOM 6181 C CB . ILE D 2 10 ? 26.946 -63.090 2.901 1.00 161.95 ? 10 ILE D CB 1 ATOM 6182 C CG1 . ILE D 2 10 ? 26.119 -62.604 1.693 1.00 160.90 ? 10 ILE D CG1 1 ATOM 6183 C CG2 . ILE D 2 10 ? 28.441 -63.115 2.591 1.00 162.06 ? 10 ILE D CG2 1 ATOM 6184 C CD1 . ILE D 2 10 ? 26.676 -62.955 0.328 1.00 161.15 ? 10 ILE D CD1 1 ATOM 6185 N N . GLU D 2 11 ? 28.251 -65.689 4.530 1.00 168.00 ? 11 GLU D N 1 ATOM 6186 C CA . GLU D 2 11 ? 29.085 -66.081 5.664 1.00 170.49 ? 11 GLU D CA 1 ATOM 6187 C C . GLU D 2 11 ? 30.050 -64.960 6.032 1.00 169.45 ? 11 GLU D C 1 ATOM 6188 O O . GLU D 2 11 ? 30.102 -64.531 7.183 1.00 170.50 ? 11 GLU D O 1 ATOM 6189 C CB . GLU D 2 11 ? 29.870 -67.354 5.341 1.00 173.18 ? 11 GLU D CB 1 ATOM 6190 N N . GLY D 2 12 ? 30.810 -64.491 5.047 1.00 167.95 ? 12 GLY D N 1 ATOM 6191 C CA . GLY D 2 12 ? 31.773 -63.412 5.262 1.00 167.56 ? 12 GLY D CA 1 ATOM 6192 C C . GLY D 2 12 ? 32.344 -62.865 3.968 1.00 165.84 ? 12 GLY D C 1 ATOM 6193 O O . GLY D 2 12 ? 31.845 -63.166 2.884 1.00 164.57 ? 12 GLY D O 1 ATOM 6194 N N . GLY D 2 13 ? 33.392 -62.055 4.089 1.00 166.32 ? 13 GLY D N 1 ATOM 6195 C CA . GLY D 2 13 ? 34.039 -61.437 2.932 1.00 165.25 ? 13 GLY D CA 1 ATOM 6196 C C . GLY D 2 13 ? 35.156 -62.289 2.361 1.00 166.32 ? 13 GLY D C 1 ATOM 6197 O O . GLY D 2 13 ? 35.772 -63.081 3.079 1.00 168.48 ? 13 GLY D O 1 ATOM 6198 N N . TRP D 2 14 ? 35.421 -62.120 1.067 1.00 165.19 ? 14 TRP D N 1 ATOM 6199 C CA . TRP D 2 14 ? 36.479 -62.863 0.384 1.00 166.02 ? 14 TRP D CA 1 ATOM 6200 C C . TRP D 2 14 ? 37.764 -62.052 0.319 1.00 166.92 ? 14 TRP D C 1 ATOM 6201 O O . TRP D 2 14 ? 37.790 -60.973 -0.274 1.00 166.05 ? 14 TRP D O 1 ATOM 6202 C CB . TRP D 2 14 ? 36.059 -63.219 -1.043 1.00 164.68 ? 14 TRP D CB 1 ATOM 6203 C CG . TRP D 2 14 ? 34.783 -63.986 -1.140 1.00 164.52 ? 14 TRP D CG 1 ATOM 6204 C CD1 . TRP D 2 14 ? 34.273 -64.859 -0.221 1.00 165.91 ? 14 TRP D CD1 1 ATOM 6205 C CD2 . TRP D 2 14 ? 33.862 -63.972 -2.235 1.00 163.64 ? 14 TRP D CD2 1 ATOM 6206 N NE1 . TRP D 2 14 ? 33.083 -65.378 -0.671 1.00 165.84 ? 14 TRP D NE1 1 ATOM 6207 C CE2 . TRP D 2 14 ? 32.809 -64.851 -1.907 1.00 164.52 ? 14 TRP D CE2 1 ATOM 6208 C CE3 . TRP D 2 14 ? 33.823 -63.297 -3.461 1.00 162.79 ? 14 TRP D CE3 1 ATOM 6209 C CZ2 . TRP D 2 14 ? 31.727 -65.074 -2.760 1.00 164.62 ? 14 TRP D CZ2 1 ATOM 6210 C CZ3 . TRP D 2 14 ? 32.748 -63.518 -4.308 1.00 162.93 ? 14 TRP D CZ3 1 ATOM 6211 C CH2 . TRP D 2 14 ? 31.716 -64.400 -3.953 1.00 163.88 ? 14 TRP D CH2 1 ATOM 6212 N N . GLN D 2 15 ? 38.829 -62.576 0.921 1.00 169.25 ? 15 GLN D N 1 ATOM 6213 C CA . GLN D 2 15 ? 40.156 -61.980 0.774 1.00 170.77 ? 15 GLN D CA 1 ATOM 6214 C C . GLN D 2 15 ? 40.680 -62.160 -0.647 1.00 169.68 ? 15 GLN D C 1 ATOM 6215 O O . GLN D 2 15 ? 41.466 -61.343 -1.131 1.00 170.13 ? 15 GLN D O 1 ATOM 6216 C CB . GLN D 2 15 ? 41.153 -62.589 1.761 1.00 174.08 ? 15 GLN D CB 1 ATOM 6217 C CG . GLN D 2 15 ? 41.009 -62.083 3.187 1.00 176.36 ? 15 GLN D CG 1 ATOM 6218 C CD . GLN D 2 15 ? 42.260 -62.306 4.020 1.00 180.60 ? 15 GLN D CD 1 ATOM 6219 O OE1 . GLN D 2 15 ? 43.097 -63.150 3.696 1.00 181.85 ? 15 GLN D OE1 1 ATOM 6220 N NE2 . GLN D 2 15 ? 42.394 -61.546 5.102 1.00 183.28 ? 15 GLN D NE2 1 ATOM 6221 N N . GLY D 2 16 ? 40.244 -63.232 -1.306 1.00 168.72 ? 16 GLY D N 1 ATOM 6222 C CA . GLY D 2 16 ? 40.660 -63.534 -2.672 1.00 167.93 ? 16 GLY D CA 1 ATOM 6223 C C . GLY D 2 16 ? 40.426 -62.404 -3.657 1.00 166.65 ? 16 GLY D C 1 ATOM 6224 O O . GLY D 2 16 ? 41.232 -62.195 -4.565 1.00 166.86 ? 16 GLY D O 1 ATOM 6225 N N . MET D 2 17 ? 39.327 -61.672 -3.481 1.00 165.73 ? 17 MET D N 1 ATOM 6226 C CA . MET D 2 17 ? 39.008 -60.548 -4.358 1.00 165.22 ? 17 MET D CA 1 ATOM 6227 C C . MET D 2 17 ? 39.767 -59.295 -3.916 1.00 166.76 ? 17 MET D C 1 ATOM 6228 O O . MET D 2 17 ? 39.589 -58.819 -2.793 1.00 167.50 ? 17 MET D O 1 ATOM 6229 C CB . MET D 2 17 ? 37.500 -60.273 -4.365 1.00 164.10 ? 17 MET D CB 1 ATOM 6230 C CG . MET D 2 17 ? 37.023 -59.535 -5.608 1.00 163.99 ? 17 MET D CG 1 ATOM 6231 S SD . MET D 2 17 ? 35.514 -58.574 -5.379 1.00 163.68 ? 17 MET D SD 1 ATOM 6232 C CE . MET D 2 17 ? 34.530 -59.658 -4.347 1.00 162.62 ? 17 MET D CE 1 ATOM 6233 N N . VAL D 2 18 ? 40.622 -58.784 -4.800 1.00 167.72 ? 18 VAL D N 1 ATOM 6234 C CA . VAL D 2 18 ? 41.325 -57.518 -4.584 1.00 169.92 ? 18 VAL D CA 1 ATOM 6235 C C . VAL D 2 18 ? 41.142 -56.580 -5.780 1.00 170.56 ? 18 VAL D C 1 ATOM 6236 O O . VAL D 2 18 ? 41.963 -55.691 -6.010 1.00 172.90 ? 18 VAL D O 1 ATOM 6237 C CB . VAL D 2 18 ? 42.830 -57.750 -4.354 1.00 171.84 ? 18 VAL D CB 1 ATOM 6238 N N . ASP D 2 19 ? 40.057 -56.779 -6.529 1.00 169.16 ? 19 ASP D N 1 ATOM 6239 C CA . ASP D 2 19 ? 39.768 -55.997 -7.730 1.00 170.33 ? 19 ASP D CA 1 ATOM 6240 C C . ASP D 2 19 ? 38.849 -54.825 -7.402 1.00 171.41 ? 19 ASP D C 1 ATOM 6241 O O . ASP D 2 19 ? 39.187 -53.672 -7.666 1.00 173.98 ? 19 ASP D O 1 ATOM 6242 C CB . ASP D 2 19 ? 39.110 -56.880 -8.796 1.00 169.02 ? 19 ASP D CB 1 ATOM 6243 C CG . ASP D 2 19 ? 39.994 -58.035 -9.232 1.00 168.36 ? 19 ASP D CG 1 ATOM 6244 O OD1 . ASP D 2 19 ? 41.212 -57.822 -9.417 1.00 169.57 ? 19 ASP D OD1 1 ATOM 6245 O OD2 . ASP D 2 19 ? 39.468 -59.156 -9.400 1.00 166.97 ? 19 ASP D OD2 1 ATOM 6246 N N . GLY D 2 20 ? 37.687 -55.134 -6.829 1.00 169.86 ? 20 GLY D N 1 ATOM 6247 C CA . GLY D 2 20 ? 36.689 -54.122 -6.464 1.00 170.70 ? 20 GLY D CA 1 ATOM 6248 C C . GLY D 2 20 ? 35.991 -54.446 -5.153 1.00 169.20 ? 20 GLY D C 1 ATOM 6249 O O . GLY D 2 20 ? 36.368 -55.395 -4.463 1.00 168.01 ? 20 GLY D O 1 ATOM 6250 N N . TRP D 2 21 ? 34.970 -53.659 -4.812 1.00 169.67 ? 21 TRP D N 1 ATOM 6251 C CA . TRP D 2 21 ? 34.248 -53.827 -3.542 1.00 168.49 ? 21 TRP D CA 1 ATOM 6252 C C . TRP D 2 21 ? 33.204 -54.946 -3.601 1.00 166.34 ? 21 TRP D C 1 ATOM 6253 O O . TRP D 2 21 ? 33.106 -55.750 -2.672 1.00 165.16 ? 21 TRP D O 1 ATOM 6254 C CB . TRP D 2 21 ? 33.584 -52.511 -3.096 1.00 169.92 ? 21 TRP D CB 1 ATOM 6255 C CG . TRP D 2 21 ? 34.512 -51.535 -2.394 1.00 172.51 ? 21 TRP D CG 1 ATOM 6256 C CD1 . TRP D 2 21 ? 35.526 -51.838 -1.526 1.00 173.13 ? 21 TRP D CD1 1 ATOM 6257 C CD2 . TRP D 2 21 ? 34.475 -50.102 -2.477 1.00 175.54 ? 21 TRP D CD2 1 ATOM 6258 N NE1 . TRP D 2 21 ? 36.132 -50.688 -1.083 1.00 176.44 ? 21 TRP D NE1 1 ATOM 6259 C CE2 . TRP D 2 21 ? 35.506 -49.608 -1.649 1.00 177.97 ? 21 TRP D CE2 1 ATOM 6260 C CE3 . TRP D 2 21 ? 33.677 -49.190 -3.178 1.00 177.08 ? 21 TRP D CE3 1 ATOM 6261 C CZ2 . TRP D 2 21 ? 35.760 -48.242 -1.502 1.00 181.94 ? 21 TRP D CZ2 1 ATOM 6262 C CZ3 . TRP D 2 21 ? 33.931 -47.830 -3.031 1.00 180.92 ? 21 TRP D CZ3 1 ATOM 6263 C CH2 . TRP D 2 21 ? 34.964 -47.371 -2.199 1.00 183.33 ? 21 TRP D CH2 1 ATOM 6264 N N . TYR D 2 22 ? 32.427 -54.989 -4.682 1.00 166.55 ? 22 TYR D N 1 ATOM 6265 C CA . TYR D 2 22 ? 31.430 -56.047 -4.891 1.00 165.40 ? 22 TYR D CA 1 ATOM 6266 C C . TYR D 2 22 ? 31.770 -56.828 -6.154 1.00 165.89 ? 22 TYR D C 1 ATOM 6267 O O . TYR D 2 22 ? 32.296 -56.265 -7.115 1.00 167.40 ? 22 TYR D O 1 ATOM 6268 C CB . TYR D 2 22 ? 30.021 -55.461 -5.023 1.00 165.81 ? 22 TYR D CB 1 ATOM 6269 C CG . TYR D 2 22 ? 29.810 -54.165 -4.275 1.00 166.47 ? 22 TYR D CG 1 ATOM 6270 C CD1 . TYR D 2 22 ? 29.703 -54.146 -2.889 1.00 165.40 ? 22 TYR D CD1 1 ATOM 6271 C CD2 . TYR D 2 22 ? 29.715 -52.956 -4.958 1.00 168.76 ? 22 TYR D CD2 1 ATOM 6272 C CE1 . TYR D 2 22 ? 29.510 -52.958 -2.203 1.00 166.35 ? 22 TYR D CE1 1 ATOM 6273 C CE2 . TYR D 2 22 ? 29.521 -51.765 -4.283 1.00 169.90 ? 22 TYR D CE2 1 ATOM 6274 C CZ . TYR D 2 22 ? 29.418 -51.770 -2.907 1.00 168.61 ? 22 TYR D CZ 1 ATOM 6275 O OH . TYR D 2 22 ? 29.226 -50.586 -2.233 1.00 170.04 ? 22 TYR D OH 1 ATOM 6276 N N . GLY D 2 23 ? 31.463 -58.122 -6.159 1.00 165.15 ? 23 GLY D N 1 ATOM 6277 C CA . GLY D 2 23 ? 31.773 -58.963 -7.311 1.00 165.90 ? 23 GLY D CA 1 ATOM 6278 C C . GLY D 2 23 ? 31.294 -60.396 -7.197 1.00 165.74 ? 23 GLY D C 1 ATOM 6279 O O . GLY D 2 23 ? 30.586 -60.755 -6.253 1.00 165.10 ? 23 GLY D O 1 ATOM 6280 N N . TYR D 2 24 ? 31.700 -61.213 -8.168 1.00 166.72 ? 24 TYR D N 1 ATOM 6281 C CA . TYR D 2 24 ? 31.277 -62.607 -8.262 1.00 167.53 ? 24 TYR D CA 1 ATOM 6282 C C . TYR D 2 24 ? 32.473 -63.553 -8.154 1.00 167.36 ? 24 TYR D C 1 ATOM 6283 O O . TYR D 2 24 ? 33.585 -63.202 -8.549 1.00 166.98 ? 24 TYR D O 1 ATOM 6284 C CB . TYR D 2 24 ? 30.574 -62.867 -9.600 1.00 169.74 ? 24 TYR D CB 1 ATOM 6285 C CG . TYR D 2 24 ? 29.555 -61.824 -10.023 1.00 170.77 ? 24 TYR D CG 1 ATOM 6286 C CD1 . TYR D 2 24 ? 29.953 -60.625 -10.597 1.00 171.14 ? 24 TYR D CD1 1 ATOM 6287 C CD2 . TYR D 2 24 ? 28.194 -62.051 -9.876 1.00 171.99 ? 24 TYR D CD2 1 ATOM 6288 C CE1 . TYR D 2 24 ? 29.027 -59.676 -11.000 1.00 172.73 ? 24 TYR D CE1 1 ATOM 6289 C CE2 . TYR D 2 24 ? 27.261 -61.105 -10.273 1.00 173.34 ? 24 TYR D CE2 1 ATOM 6290 C CZ . TYR D 2 24 ? 27.682 -59.921 -10.835 1.00 173.74 ? 24 TYR D CZ 1 ATOM 6291 O OH . TYR D 2 24 ? 26.760 -58.981 -11.233 1.00 175.67 ? 24 TYR D OH 1 ATOM 6292 N N . HIS D 2 25 ? 32.232 -64.748 -7.619 1.00 168.09 ? 25 HIS D N 1 ATOM 6293 C CA . HIS D 2 25 ? 33.201 -65.843 -7.662 1.00 168.87 ? 25 HIS D CA 1 ATOM 6294 C C . HIS D 2 25 ? 32.577 -67.025 -8.395 1.00 171.38 ? 25 HIS D C 1 ATOM 6295 O O . HIS D 2 25 ? 31.737 -67.735 -7.836 1.00 172.79 ? 25 HIS D O 1 ATOM 6296 C CB . HIS D 2 25 ? 33.621 -66.269 -6.253 1.00 168.60 ? 25 HIS D CB 1 ATOM 6297 C CG . HIS D 2 25 ? 34.355 -67.575 -6.214 1.00 170.19 ? 25 HIS D CG 1 ATOM 6298 N ND1 . HIS D 2 25 ? 35.650 -67.714 -6.664 1.00 170.07 ? 25 HIS D ND1 1 ATOM 6299 C CD2 . HIS D 2 25 ? 33.970 -68.802 -5.792 1.00 172.35 ? 25 HIS D CD2 1 ATOM 6300 C CE1 . HIS D 2 25 ? 36.034 -68.969 -6.515 1.00 171.96 ? 25 HIS D CE1 1 ATOM 6301 N NE2 . HIS D 2 25 ? 35.033 -69.651 -5.988 1.00 173.57 ? 25 HIS D NE2 1 ATOM 6302 N N . HIS D 2 26 ? 32.985 -67.233 -9.644 1.00 172.48 ? 26 HIS D N 1 ATOM 6303 C CA . HIS D 2 26 ? 32.418 -68.303 -10.464 1.00 175.55 ? 26 HIS D CA 1 ATOM 6304 C C . HIS D 2 26 ? 33.196 -69.607 -10.304 1.00 176.85 ? 26 HIS D C 1 ATOM 6305 O O . HIS D 2 26 ? 34.416 -69.596 -10.140 1.00 175.57 ? 26 HIS D O 1 ATOM 6306 C CB . HIS D 2 26 ? 32.350 -67.891 -11.942 1.00 176.83 ? 26 HIS D CB 1 ATOM 6307 C CG . HIS D 2 26 ? 33.688 -67.724 -12.596 1.00 176.14 ? 26 HIS D CG 1 ATOM 6308 N ND1 . HIS D 2 26 ? 34.365 -68.773 -13.180 1.00 177.72 ? 26 HIS D ND1 1 ATOM 6309 C CD2 . HIS D 2 26 ? 34.463 -66.629 -12.776 1.00 174.33 ? 26 HIS D CD2 1 ATOM 6310 C CE1 . HIS D 2 26 ? 35.507 -68.333 -13.681 1.00 176.52 ? 26 HIS D CE1 1 ATOM 6311 N NE2 . HIS D 2 26 ? 35.589 -67.035 -13.450 1.00 174.58 ? 26 HIS D NE2 1 ATOM 6312 N N . SER D 2 27 ? 32.468 -70.721 -10.329 1.00 179.89 ? 27 SER D N 1 ATOM 6313 C CA . SER D 2 27 ? 33.055 -72.057 -10.360 1.00 182.25 ? 27 SER D CA 1 ATOM 6314 C C . SER D 2 27 ? 32.522 -72.749 -11.607 1.00 185.69 ? 27 SER D C 1 ATOM 6315 O O . SER D 2 27 ? 31.313 -72.755 -11.846 1.00 187.82 ? 27 SER D O 1 ATOM 6316 C CB . SER D 2 27 ? 32.679 -72.845 -9.104 1.00 183.91 ? 27 SER D CB 1 ATOM 6317 O OG . SER D 2 27 ? 33.469 -74.015 -8.978 1.00 186.25 ? 27 SER D OG 1 ATOM 6318 N N . ASN D 2 28 ? 33.418 -73.326 -12.403 1.00 186.58 ? 28 ASN D N 1 ATOM 6319 C CA . ASN D 2 28 ? 33.050 -73.812 -13.728 1.00 189.84 ? 28 ASN D CA 1 ATOM 6320 C C . ASN D 2 28 ? 33.892 -75.003 -14.175 1.00 192.22 ? 28 ASN D C 1 ATOM 6321 O O . ASN D 2 28 ? 34.982 -75.236 -13.648 1.00 190.59 ? 28 ASN D O 1 ATOM 6322 C CB . ASN D 2 28 ? 33.193 -72.664 -14.735 1.00 188.03 ? 28 ASN D CB 1 ATOM 6323 C CG . ASN D 2 28 ? 32.244 -72.786 -15.911 1.00 191.94 ? 28 ASN D CG 1 ATOM 6324 O OD1 . ASN D 2 28 ? 31.111 -73.249 -15.773 1.00 195.05 ? 28 ASN D OD1 1 ATOM 6325 N ND2 . ASN D 2 28 ? 32.701 -72.349 -17.076 1.00 192.21 ? 28 ASN D ND2 1 ATOM 6326 N N . GLU D 2 29 ? 33.373 -75.757 -15.144 1.00 196.52 ? 29 GLU D N 1 ATOM 6327 C CA . GLU D 2 29 ? 34.112 -76.870 -15.749 1.00 199.32 ? 29 GLU D CA 1 ATOM 6328 C C . GLU D 2 29 ? 35.420 -76.391 -16.388 1.00 196.16 ? 29 GLU D C 1 ATOM 6329 O O . GLU D 2 29 ? 36.415 -77.116 -16.394 1.00 196.54 ? 29 GLU D O 1 ATOM 6330 C CB . GLU D 2 29 ? 33.246 -77.631 -16.772 1.00 205.12 ? 29 GLU D CB 1 ATOM 6331 C CG . GLU D 2 29 ? 32.956 -76.914 -18.093 1.00 205.64 ? 29 GLU D CG 1 ATOM 6332 C CD . GLU D 2 29 ? 31.916 -75.812 -17.984 1.00 204.37 ? 29 GLU D CD 1 ATOM 6333 O OE1 . GLU D 2 29 ? 30.990 -75.933 -17.154 1.00 205.29 ? 29 GLU D OE1 1 ATOM 6334 O OE2 . GLU D 2 29 ? 32.020 -74.825 -18.742 1.00 202.77 ? 29 GLU D OE2 1 ATOM 6335 N N . GLN D 2 30 ? 35.401 -75.169 -16.918 1.00 193.42 ? 30 GLN D N 1 ATOM 6336 C CA . GLN D 2 30 ? 36.600 -74.521 -17.446 1.00 190.45 ? 30 GLN D CA 1 ATOM 6337 C C . GLN D 2 30 ? 37.589 -74.217 -16.326 1.00 186.66 ? 30 GLN D C 1 ATOM 6338 O O . GLN D 2 30 ? 38.721 -74.699 -16.338 1.00 186.30 ? 30 GLN D O 1 ATOM 6339 C CB . GLN D 2 30 ? 36.230 -73.225 -18.178 1.00 189.24 ? 30 GLN D CB 1 ATOM 6340 C CG . GLN D 2 30 ? 35.668 -73.453 -19.570 1.00 193.37 ? 30 GLN D CG 1 ATOM 6341 C CD . GLN D 2 30 ? 34.766 -72.331 -20.048 1.00 193.85 ? 30 GLN D CD 1 ATOM 6342 O OE1 . GLN D 2 30 ? 33.709 -72.086 -19.469 1.00 194.25 ? 30 GLN D OE1 1 ATOM 6343 N NE2 . GLN D 2 30 ? 35.168 -71.656 -21.122 1.00 194.26 ? 30 GLN D NE2 1 ATOM 6344 N N . GLY D 2 31 ? 37.150 -73.414 -15.362 1.00 184.25 ? 31 GLY D N 1 ATOM 6345 C CA . GLY D 2 31 ? 37.983 -73.050 -14.221 1.00 181.31 ? 31 GLY D CA 1 ATOM 6346 C C . GLY D 2 31 ? 37.181 -72.374 -13.128 1.00 179.85 ? 31 GLY D C 1 ATOM 6347 O O . GLY D 2 31 ? 35.972 -72.585 -13.015 1.00 181.54 ? 31 GLY D O 1 ATOM 6348 N N . SER D 2 32 ? 37.858 -71.560 -12.322 1.00 155.28 ? 32 SER D N 1 ATOM 6349 C CA . SER D 2 32 ? 37.205 -70.828 -11.238 1.00 153.28 ? 32 SER D CA 1 ATOM 6350 C C . SER D 2 32 ? 38.035 -69.624 -10.791 1.00 149.85 ? 32 SER D C 1 ATOM 6351 O O . SER D 2 32 ? 39.254 -69.723 -10.636 1.00 149.15 ? 32 SER D O 1 ATOM 6352 C CB . SER D 2 32 ? 36.944 -71.759 -10.050 1.00 154.61 ? 32 SER D CB 1 ATOM 6353 O OG . SER D 2 32 ? 38.145 -72.360 -9.596 1.00 154.86 ? 32 SER D OG 1 ATOM 6354 N N . GLY D 2 33 ? 37.368 -68.492 -10.586 1.00 147.80 ? 33 GLY D N 1 ATOM 6355 C CA . GLY D 2 33 ? 38.044 -67.263 -10.172 1.00 144.64 ? 33 GLY D CA 1 ATOM 6356 C C . GLY D 2 33 ? 37.093 -66.137 -9.806 1.00 142.74 ? 33 GLY D C 1 ATOM 6357 O O . GLY D 2 33 ? 35.875 -66.263 -9.945 1.00 143.86 ? 33 GLY D O 1 ATOM 6358 N N . TYR D 2 34 ? 37.663 -65.028 -9.341 1.00 139.98 ? 34 TYR D N 1 ATOM 6359 C CA . TYR D 2 34 ? 36.886 -63.867 -8.908 1.00 138.01 ? 34 TYR D CA 1 ATOM 6360 C C . TYR D 2 34 ? 36.716 -62.863 -10.047 1.00 137.16 ? 34 TYR D C 1 ATOM 6361 O O . TYR D 2 34 ? 37.441 -62.910 -11.043 1.00 137.61 ? 34 TYR D O 1 ATOM 6362 C CB . TYR D 2 34 ? 37.562 -63.192 -7.712 1.00 135.47 ? 34 TYR D CB 1 ATOM 6363 C CG . TYR D 2 34 ? 37.819 -64.129 -6.549 1.00 136.22 ? 34 TYR D CG 1 ATOM 6364 C CD1 . TYR D 2 34 ? 36.829 -64.387 -5.605 1.00 136.70 ? 34 TYR D CD1 1 ATOM 6365 C CD2 . TYR D 2 34 ? 39.052 -64.761 -6.398 1.00 136.47 ? 34 TYR D CD2 1 ATOM 6366 C CE1 . TYR D 2 34 ? 37.060 -65.245 -4.540 1.00 137.55 ? 34 TYR D CE1 1 ATOM 6367 C CE2 . TYR D 2 34 ? 39.291 -65.620 -5.337 1.00 137.29 ? 34 TYR D CE2 1 ATOM 6368 C CZ . TYR D 2 34 ? 38.292 -65.859 -4.412 1.00 137.84 ? 34 TYR D CZ 1 ATOM 6369 O OH . TYR D 2 34 ? 38.531 -66.710 -3.357 1.00 138.77 ? 34 TYR D OH 1 ATOM 6370 N N . ALA D 2 35 ? 35.752 -61.961 -9.892 1.00 136.12 ? 35 ALA D N 1 ATOM 6371 C CA . ALA D 2 35 ? 35.471 -60.941 -10.900 1.00 135.29 ? 35 ALA D CA 1 ATOM 6372 C C . ALA D 2 35 ? 34.632 -59.815 -10.302 1.00 133.61 ? 35 ALA D C 1 ATOM 6373 O O . ALA D 2 35 ? 33.497 -60.037 -9.878 1.00 134.49 ? 35 ALA D O 1 ATOM 6374 C CB . ALA D 2 35 ? 34.752 -61.558 -12.089 1.00 137.66 ? 35 ALA D CB 1 ATOM 6375 N N . ALA D 2 36 ? 35.194 -58.610 -10.272 1.00 131.37 ? 36 ALA D N 1 ATOM 6376 C CA . ALA D 2 36 ? 34.512 -57.455 -9.693 1.00 129.66 ? 36 ALA D CA 1 ATOM 6377 C C . ALA D 2 36 ? 33.464 -56.883 -10.647 1.00 130.14 ? 36 ALA D C 1 ATOM 6378 O O . ALA D 2 36 ? 33.682 -56.817 -11.857 1.00 130.66 ? 36 ALA D O 1 ATOM 6379 C CB . ALA D 2 36 ? 35.521 -56.379 -9.314 1.00 127.14 ? 36 ALA D CB 1 ATOM 6380 N N . ASP D 2 37 ? 32.325 -56.479 -10.088 1.00 130.10 ? 37 ASP D N 1 ATOM 6381 C CA . ASP D 2 37 ? 31.290 -55.776 -10.841 1.00 130.35 ? 37 ASP D CA 1 ATOM 6382 C C . ASP D 2 37 ? 31.627 -54.282 -10.865 1.00 128.02 ? 37 ASP D C 1 ATOM 6383 O O . ASP D 2 37 ? 31.427 -53.576 -9.875 1.00 126.55 ? 37 ASP D O 1 ATOM 6384 C CB . ASP D 2 37 ? 29.913 -56.009 -10.202 1.00 131.27 ? 37 ASP D CB 1 ATOM 6385 C CG . ASP D 2 37 ? 28.774 -55.361 -10.984 1.00 131.59 ? 37 ASP D CG 1 ATOM 6386 O OD1 . ASP D 2 37 ? 28.896 -55.193 -12.218 1.00 132.15 ? 37 ASP D OD1 1 ATOM 6387 O OD2 . ASP D 2 37 ? 27.745 -55.028 -10.361 1.00 131.36 ? 37 ASP D OD2 1 ATOM 6388 N N . LYS D 2 38 ? 32.146 -53.813 -11.997 1.00 127.83 ? 38 LYS D N 1 ATOM 6389 C CA . LYS D 2 38 ? 32.547 -52.412 -12.148 1.00 125.72 ? 38 LYS D CA 1 ATOM 6390 C C . LYS D 2 38 ? 31.347 -51.455 -12.137 1.00 125.27 ? 38 LYS D C 1 ATOM 6391 O O . LYS D 2 38 ? 31.474 -50.306 -11.706 1.00 123.44 ? 38 LYS D O 1 ATOM 6392 C CB . LYS D 2 38 ? 33.358 -52.225 -13.435 1.00 125.83 ? 38 LYS D CB 1 ATOM 6393 C CG . LYS D 2 38 ? 34.647 -53.032 -13.478 1.00 126.16 ? 38 LYS D CG 1 ATOM 6394 N N . GLU D 2 39 ? 30.190 -51.934 -12.601 1.00 127.01 ? 39 GLU D N 1 ATOM 6395 C CA . GLU D 2 39 ? 28.963 -51.125 -12.665 1.00 126.75 ? 39 GLU D CA 1 ATOM 6396 C C . GLU D 2 39 ? 28.460 -50.709 -11.278 1.00 125.64 ? 39 GLU D C 1 ATOM 6397 O O . GLU D 2 39 ? 28.086 -49.552 -11.064 1.00 124.23 ? 39 GLU D O 1 ATOM 6398 C CB . GLU D 2 39 ? 27.859 -51.886 -13.409 1.00 128.94 ? 39 GLU D CB 1 ATOM 6399 N N . SER D 2 40 ? 28.452 -51.655 -10.344 1.00 126.28 ? 40 SER D N 1 ATOM 6400 C CA . SER D 2 40 ? 28.051 -51.378 -8.967 1.00 125.37 ? 40 SER D CA 1 ATOM 6401 C C . SER D 2 40 ? 29.165 -50.675 -8.190 1.00 123.32 ? 40 SER D C 1 ATOM 6402 O O . SER D 2 40 ? 28.892 -49.813 -7.351 1.00 122.01 ? 40 SER D O 1 ATOM 6403 C CB . SER D 2 40 ? 27.655 -52.673 -8.257 1.00 126.99 ? 40 SER D CB 1 ATOM 6404 O OG . SER D 2 40 ? 28.727 -53.598 -8.249 1.00 127.46 ? 40 SER D OG 1 ATOM 6405 N N . THR D 2 41 ? 30.414 -51.049 -8.469 1.00 123.09 ? 41 THR D N 1 ATOM 6406 C CA . THR D 2 41 ? 31.579 -50.449 -7.810 1.00 121.26 ? 41 THR D CA 1 ATOM 6407 C C . THR D 2 41 ? 31.721 -48.966 -8.166 1.00 119.61 ? 41 THR D C 1 ATOM 6408 O O . THR D 2 41 ? 32.006 -48.143 -7.295 1.00 117.98 ? 41 THR D O 1 ATOM 6409 C CB . THR D 2 41 ? 32.882 -51.207 -8.164 1.00 121.51 ? 41 THR D CB 1 ATOM 6410 O OG1 . THR D 2 41 ? 32.817 -52.539 -7.640 1.00 122.98 ? 41 THR D OG1 1 ATOM 6411 C CG2 . THR D 2 41 ? 34.115 -50.510 -7.584 1.00 119.53 ? 41 THR D CG2 1 ATOM 6412 N N . GLN D 2 42 ? 31.521 -48.632 -9.440 1.00 120.10 ? 42 GLN D N 1 ATOM 6413 C CA . GLN D 2 42 ? 31.585 -47.239 -9.892 1.00 118.69 ? 42 GLN D CA 1 ATOM 6414 C C . GLN D 2 42 ? 30.557 -46.368 -9.167 1.00 117.99 ? 42 GLN D C 1 ATOM 6415 O O . GLN D 2 42 ? 30.851 -45.228 -8.802 1.00 116.31 ? 42 GLN D O 1 ATOM 6416 C CB . GLN D 2 42 ? 31.369 -47.149 -11.404 1.00 119.59 ? 42 GLN D CB 1 ATOM 6417 N N . LYS D 2 43 ? 29.360 -46.919 -8.955 1.00 119.22 ? 43 LYS D N 1 ATOM 6418 C CA . LYS D 2 43 ? 28.283 -46.219 -8.243 1.00 118.70 ? 43 LYS D CA 1 ATOM 6419 C C . LYS D 2 43 ? 28.626 -45.967 -6.773 1.00 117.46 ? 43 LYS D C 1 ATOM 6420 O O . LYS D 2 43 ? 28.228 -44.948 -6.206 1.00 116.42 ? 43 LYS D O 1 ATOM 6421 C CB . LYS D 2 43 ? 26.977 -47.015 -8.336 1.00 120.46 ? 43 LYS D CB 1 ATOM 6422 C CG . LYS D 2 43 ? 25.765 -46.292 -7.769 1.00 120.19 ? 43 LYS D CG 1 ATOM 6423 N N . ALA D 2 44 ? 29.359 -46.897 -6.165 1.00 117.61 ? 44 ALA D N 1 ATOM 6424 C CA . ALA D 2 44 ? 29.752 -46.785 -4.759 1.00 116.59 ? 44 ALA D CA 1 ATOM 6425 C C . ALA D 2 44 ? 30.894 -45.789 -4.548 1.00 114.64 ? 44 ALA D C 1 ATOM 6426 O O . ALA D 2 44 ? 30.906 -45.061 -3.554 1.00 113.48 ? 44 ALA D O 1 ATOM 6427 C CB . ALA D 2 44 ? 30.135 -48.151 -4.207 1.00 117.64 ? 44 ALA D CB 1 ATOM 6428 N N . ILE D 2 45 ? 31.853 -45.766 -5.475 1.00 114.30 ? 45 ILE D N 1 ATOM 6429 C CA . ILE D 2 45 ? 32.985 -44.834 -5.404 1.00 112.54 ? 45 ILE D CA 1 ATOM 6430 C C . ILE D 2 45 ? 32.502 -43.387 -5.572 1.00 111.54 ? 45 ILE D C 1 ATOM 6431 O O . ILE D 2 45 ? 32.950 -42.491 -4.851 1.00 110.15 ? 45 ILE D O 1 ATOM 6432 C CB . ILE D 2 45 ? 34.077 -45.171 -6.451 1.00 112.56 ? 45 ILE D CB 1 ATOM 6433 C CG1 . ILE D 2 45 ? 34.735 -46.515 -6.117 1.00 113.34 ? 45 ILE D CG1 1 ATOM 6434 C CG2 . ILE D 2 45 ? 35.141 -44.076 -6.504 1.00 110.89 ? 45 ILE D CG2 1 ATOM 6435 C CD1 . ILE D 2 45 ? 35.551 -47.105 -7.248 1.00 114.05 ? 45 ILE D CD1 1 ATOM 6436 N N . ASP D 2 46 ? 31.584 -43.171 -6.513 1.00 112.19 ? 46 ASP D N 1 ATOM 6437 C CA . ASP D 2 46 ? 30.997 -41.847 -6.737 1.00 111.36 ? 46 ASP D CA 1 ATOM 6438 C C . ASP D 2 46 ? 30.191 -41.397 -5.522 1.00 110.94 ? 46 ASP D C 1 ATOM 6439 O O . ASP D 2 46 ? 30.276 -40.240 -5.105 1.00 109.87 ? 46 ASP D O 1 ATOM 6440 C CB . ASP D 2 46 ? 30.092 -41.854 -7.974 1.00 112.50 ? 46 ASP D CB 1 ATOM 6441 C CG . ASP D 2 46 ? 30.847 -42.155 -9.262 1.00 112.93 ? 46 ASP D CG 1 ATOM 6442 O OD1 . ASP D 2 46 ? 32.094 -42.074 -9.269 1.00 112.11 ? 46 ASP D OD1 1 ATOM 6443 O OD2 . ASP D 2 46 ? 30.187 -42.480 -10.272 1.00 114.06 ? 46 ASP D OD2 1 ATOM 6444 N N . GLY D 2 47 ? 29.415 -42.319 -4.959 1.00 111.89 ? 47 GLY D N 1 ATOM 6445 C CA . GLY D 2 47 ? 28.594 -42.037 -3.787 1.00 111.69 ? 47 GLY D CA 1 ATOM 6446 C C . GLY D 2 47 ? 29.410 -41.656 -2.568 1.00 110.42 ? 47 GLY D C 1 ATOM 6447 O O . GLY D 2 47 ? 29.176 -40.612 -1.962 1.00 109.56 ? 47 GLY D O 1 ATOM 6448 N N . VAL D 2 48 ? 30.376 -42.505 -2.221 1.00 110.48 ? 48 VAL D N 1 ATOM 6449 C CA . VAL D 2 48 ? 31.248 -42.284 -1.060 1.00 109.49 ? 48 VAL D CA 1 ATOM 6450 C C . VAL D 2 48 ? 32.061 -40.992 -1.205 1.00 107.97 ? 48 VAL D C 1 ATOM 6451 O O . VAL D 2 48 ? 32.181 -40.221 -0.252 1.00 106.92 ? 48 VAL D O 1 ATOM 6452 C CB . VAL D 2 48 ? 32.196 -43.492 -0.831 1.00 109.89 ? 48 VAL D CB 1 ATOM 6453 C CG1 . VAL D 2 48 ? 33.290 -43.164 0.179 1.00 108.74 ? 48 VAL D CG1 1 ATOM 6454 C CG2 . VAL D 2 48 ? 31.408 -44.710 -0.370 1.00 111.43 ? 48 VAL D CG2 1 ATOM 6455 N N . THR D 2 49 ? 32.610 -40.759 -2.395 1.00 107.84 ? 49 THR D N 1 ATOM 6456 C CA . THR D 2 49 ? 33.394 -39.553 -2.660 1.00 106.66 ? 49 THR D CA 1 ATOM 6457 C C . THR D 2 49 ? 32.530 -38.291 -2.583 1.00 106.38 ? 49 THR D C 1 ATOM 6458 O O . THR D 2 49 ? 32.993 -37.246 -2.122 1.00 105.36 ? 49 THR D O 1 ATOM 6459 C CB . THR D 2 49 ? 34.084 -39.628 -4.034 1.00 106.79 ? 49 THR D CB 1 ATOM 6460 O OG1 . THR D 2 49 ? 34.870 -40.825 -4.105 1.00 107.29 ? 49 THR D OG1 1 ATOM 6461 C CG2 . THR D 2 49 ? 34.984 -38.415 -4.264 1.00 105.51 ? 49 THR D CG2 1 ATOM 6462 N N . ASN D 2 50 ? 31.280 -38.393 -3.030 1.00 107.32 ? 50 ASN D N 1 ATOM 6463 C CA . ASN D 2 50 ? 30.324 -37.285 -2.915 1.00 107.09 ? 50 ASN D CA 1 ATOM 6464 C C . ASN D 2 50 ? 29.914 -36.985 -1.474 1.00 106.81 ? 50 ASN D C 1 ATOM 6465 O O . ASN D 2 50 ? 29.515 -35.865 -1.164 1.00 106.21 ? 50 ASN D O 1 ATOM 6466 C CB . ASN D 2 50 ? 29.070 -37.556 -3.753 1.00 108.31 ? 50 ASN D CB 1 ATOM 6467 C CG . ASN D 2 50 ? 29.251 -37.189 -5.212 1.00 108.42 ? 50 ASN D CG 1 ATOM 6468 O OD1 . ASN D 2 50 ? 28.339 -36.659 -5.845 1.00 108.93 ? 50 ASN D OD1 1 ATOM 6469 N ND2 . ASN D 2 50 ? 30.433 -37.461 -5.753 1.00 108.02 ? 50 ASN D ND2 1 ATOM 6470 N N . LYS D 2 51 ? 30.004 -37.989 -0.604 1.00 107.25 ? 51 LYS D N 1 ATOM 6471 C CA . LYS D 2 51 ? 29.660 -37.834 0.809 1.00 107.15 ? 51 LYS D CA 1 ATOM 6472 C C . LYS D 2 51 ? 30.784 -37.128 1.571 1.00 105.92 ? 51 LYS D C 1 ATOM 6473 O O . LYS D 2 51 ? 30.546 -36.133 2.259 1.00 105.47 ? 51 LYS D O 1 ATOM 6474 C CB . LYS D 2 51 ? 29.385 -39.206 1.432 1.00 108.17 ? 51 LYS D CB 1 ATOM 6475 C CG . LYS D 2 51 ? 28.641 -39.162 2.753 1.00 108.54 ? 51 LYS D CG 1 ATOM 6476 C CD . LYS D 2 51 ? 28.465 -40.560 3.324 1.00 109.70 ? 51 LYS D CD 1 ATOM 6477 C CE . LYS D 2 51 ? 27.339 -40.617 4.344 1.00 110.66 ? 51 LYS D CE 1 ATOM 6478 N NZ . LYS D 2 51 ? 26.002 -40.776 3.707 1.00 111.79 ? 51 LYS D NZ 1 ATOM 6479 N N . VAL D 2 52 ? 32.001 -37.655 1.441 1.00 105.47 ? 52 VAL D N 1 ATOM 6480 C CA . VAL D 2 52 ? 33.178 -37.116 2.139 1.00 104.34 ? 52 VAL D CA 1 ATOM 6481 C C . VAL D 2 52 ? 33.479 -35.663 1.752 1.00 103.27 ? 52 VAL D C 1 ATOM 6482 O O . VAL D 2 52 ? 33.827 -34.851 2.611 1.00 102.55 ? 52 VAL D O 1 ATOM 6483 C CB . VAL D 2 52 ? 34.434 -38.012 1.932 1.00 104.25 ? 52 VAL D CB 1 ATOM 6484 C CG1 . VAL D 2 52 ? 34.870 -38.050 0.471 1.00 104.33 ? 52 VAL D CG1 1 ATOM 6485 C CG2 . VAL D 2 52 ? 35.585 -37.556 2.824 1.00 103.15 ? 52 VAL D CG2 1 ATOM 6486 N N . ASN D 2 53 ? 33.336 -35.337 0.470 1.00 103.19 ? 53 ASN D N 1 ATOM 6487 C CA . ASN D 2 53 ? 33.536 -33.966 0.005 1.00 102.40 ? 53 ASN D CA 1 ATOM 6488 C C . ASN D 2 53 ? 32.409 -33.057 0.489 1.00 102.63 ? 53 ASN D C 1 ATOM 6489 O O . ASN D 2 53 ? 32.656 -31.919 0.888 1.00 101.97 ? 53 ASN D O 1 ATOM 6490 C CB . ASN D 2 53 ? 33.638 -33.918 -1.523 1.00 102.55 ? 53 ASN D CB 1 ATOM 6491 C CG . ASN D 2 53 ? 34.828 -34.699 -2.058 1.00 102.29 ? 53 ASN D CG 1 ATOM 6492 O OD1 . ASN D 2 53 ? 35.637 -35.227 -1.297 1.00 101.89 ? 53 ASN D OD1 1 ATOM 6493 N ND2 . ASN D 2 53 ? 34.933 -34.783 -3.376 1.00 102.56 ? 53 ASN D ND2 1 ATOM 6494 N N . SER D 2 54 ? 31.180 -33.572 0.463 1.00 103.63 ? 54 SER D N 1 ATOM 6495 C CA . SER D 2 54 ? 30.008 -32.842 0.960 1.00 104.06 ? 54 SER D CA 1 ATOM 6496 C C . SER D 2 54 ? 30.103 -32.554 2.462 1.00 103.82 ? 54 SER D C 1 ATOM 6497 O O . SER D 2 54 ? 29.593 -31.537 2.933 1.00 103.65 ? 54 SER D O 1 ATOM 6498 C CB . SER D 2 54 ? 28.721 -33.621 0.654 1.00 105.25 ? 54 SER D CB 1 ATOM 6499 O OG . SER D 2 54 ? 27.576 -32.975 1.182 1.00 105.65 ? 54 SER D OG 1 ATOM 6500 N N . ILE D 2 55 ? 30.751 -33.452 3.203 1.00 103.77 ? 55 ILE D N 1 ATOM 6501 C CA . ILE D 2 55 ? 30.994 -33.253 4.633 1.00 103.55 ? 55 ILE D CA 1 ATOM 6502 C C . ILE D 2 55 ? 32.040 -32.161 4.875 1.00 102.44 ? 55 ILE D C 1 ATOM 6503 O O . ILE D 2 55 ? 31.845 -31.299 5.728 1.00 102.33 ? 55 ILE D O 1 ATOM 6504 C CB . ILE D 2 55 ? 31.420 -34.570 5.322 1.00 103.91 ? 55 ILE D CB 1 ATOM 6505 C CG1 . ILE D 2 55 ? 30.223 -35.523 5.406 1.00 105.23 ? 55 ILE D CG1 1 ATOM 6506 C CG2 . ILE D 2 55 ? 31.966 -34.309 6.723 1.00 103.56 ? 55 ILE D CG2 1 ATOM 6507 C CD1 . ILE D 2 55 ? 30.601 -36.976 5.599 1.00 105.82 ? 55 ILE D CD1 1 ATOM 6508 N N . ILE D 2 56 ? 33.140 -32.196 4.126 1.00 101.74 ? 56 ILE D N 1 ATOM 6509 C CA . ILE D 2 56 ? 34.195 -31.186 4.258 1.00 100.82 ? 56 ILE D CA 1 ATOM 6510 C C . ILE D 2 56 ? 33.656 -29.790 3.918 1.00 100.90 ? 56 ILE D C 1 ATOM 6511 O O . ILE D 2 56 ? 33.904 -28.826 4.645 1.00 100.51 ? 56 ILE D O 1 ATOM 6512 C CB . ILE D 2 56 ? 35.412 -31.500 3.351 1.00 100.16 ? 56 ILE D CB 1 ATOM 6513 C CG1 . ILE D 2 56 ? 36.090 -32.807 3.782 1.00 100.18 ? 56 ILE D CG1 1 ATOM 6514 C CG2 . ILE D 2 56 ? 36.427 -30.358 3.387 1.00 99.19 ? 56 ILE D CG2 1 ATOM 6515 C CD1 . ILE D 2 56 ? 36.938 -33.443 2.699 1.00 99.92 ? 56 ILE D CD1 1 ATOM 6516 N N . ASP D 2 57 ? 32.909 -29.700 2.820 1.00 101.57 ? 57 ASP D N 1 ATOM 6517 C CA . ASP D 2 57 ? 32.428 -28.417 2.302 1.00 101.74 ? 57 ASP D CA 1 ATOM 6518 C C . ASP D 2 57 ? 31.258 -27.837 3.105 1.00 102.48 ? 57 ASP D C 1 ATOM 6519 O O . ASP D 2 57 ? 31.009 -26.632 3.044 1.00 102.43 ? 57 ASP D O 1 ATOM 6520 C CB . ASP D 2 57 ? 32.041 -28.557 0.825 1.00 102.19 ? 57 ASP D CB 1 ATOM 6521 C CG . ASP D 2 57 ? 33.211 -29.006 -0.051 1.00 101.71 ? 57 ASP D CG 1 ATOM 6522 O OD1 . ASP D 2 57 ? 34.364 -28.612 0.229 1.00 100.95 ? 57 ASP D OD1 1 ATOM 6523 O OD2 . ASP D 2 57 ? 32.977 -29.759 -1.020 1.00 102.07 ? 57 ASP D OD2 1 ATOM 6524 N N . LYS D 2 58 ? 30.548 -28.687 3.847 1.00 103.24 ? 58 LYS D N 1 ATOM 6525 C CA . LYS D 2 58 ? 29.479 -28.233 4.746 1.00 103.94 ? 58 LYS D CA 1 ATOM 6526 C C . LYS D 2 58 ? 30.065 -27.614 6.017 1.00 103.80 ? 58 LYS D C 1 ATOM 6527 O O . LYS D 2 58 ? 29.498 -26.675 6.585 1.00 104.11 ? 58 LYS D O 1 ATOM 6528 C CB . LYS D 2 58 ? 28.554 -29.398 5.119 1.00 104.71 ? 58 LYS D CB 1 ATOM 6529 C CG . LYS D 2 58 ? 27.186 -28.980 5.644 1.00 105.53 ? 58 LYS D CG 1 ATOM 6530 C CD . LYS D 2 58 ? 26.103 -29.053 4.576 1.00 106.19 ? 58 LYS D CD 1 ATOM 6531 C CE . LYS D 2 58 ? 26.371 -28.113 3.412 1.00 105.75 ? 58 LYS D CE 1 ATOM 6532 N NZ . LYS D 2 58 ? 25.306 -28.193 2.375 1.00 106.51 ? 58 LYS D NZ 1 ATOM 6533 N N . MET D 2 59 ? 31.210 -28.142 6.447 1.00 103.43 ? 59 MET D N 1 ATOM 6534 C CA . MET D 2 59 ? 31.887 -27.683 7.663 1.00 103.25 ? 59 MET D CA 1 ATOM 6535 C C . MET D 2 59 ? 32.887 -26.553 7.358 1.00 102.75 ? 59 MET D C 1 ATOM 6536 O O . MET D 2 59 ? 33.687 -26.167 8.213 1.00 102.21 ? 59 MET D O 1 ATOM 6537 C CB . MET D 2 59 ? 32.589 -28.867 8.338 1.00 102.93 ? 59 MET D CB 1 ATOM 6538 C CG . MET D 2 59 ? 31.678 -30.067 8.588 1.00 103.64 ? 59 MET D CG 1 ATOM 6539 S SD . MET D 2 59 ? 30.509 -29.841 9.939 1.00 104.55 ? 59 MET D SD 1 ATOM 6540 C CE . MET D 2 59 ? 31.597 -29.950 11.355 1.00 104.23 ? 59 MET D CE 1 ATOM 6541 N N . ASN D 2 60 ? 32.835 -26.044 6.127 1.00 103.02 ? 60 ASN D N 1 ATOM 6542 C CA . ASN D 2 60 ? 33.580 -24.858 5.709 1.00 102.86 ? 60 ASN D CA 1 ATOM 6543 C C . ASN D 2 60 ? 33.037 -23.610 6.412 1.00 103.37 ? 60 ASN D C 1 ATOM 6544 O O . ASN D 2 60 ? 33.797 -22.746 6.846 1.00 102.73 ? 60 ASN D O 1 ATOM 6545 C CB . ASN D 2 60 ? 33.468 -24.714 4.182 1.00 102.97 ? 60 ASN D CB 1 ATOM 6546 C CG . ASN D 2 60 ? 34.363 -23.625 3.608 1.00 102.68 ? 60 ASN D CG 1 ATOM 6547 O OD1 . ASN D 2 60 ? 34.572 -22.574 4.218 1.00 102.72 ? 60 ASN D OD1 1 ATOM 6548 N ND2 . ASN D 2 60 ? 34.876 -23.866 2.403 1.00 102.38 ? 60 ASN D ND2 1 ATOM 6549 N N . THR D 2 61 ? 31.714 -23.527 6.516 1.00 104.54 ? 61 THR D N 1 ATOM 6550 C CA . THR D 2 61 ? 31.062 -22.439 7.243 1.00 105.33 ? 61 THR D CA 1 ATOM 6551 C C . THR D 2 61 ? 31.026 -22.789 8.730 1.00 105.90 ? 61 THR D C 1 ATOM 6552 O O . THR D 2 61 ? 29.991 -23.172 9.276 1.00 106.59 ? 61 THR D O 1 ATOM 6553 C CB . THR D 2 61 ? 29.648 -22.126 6.693 1.00 106.19 ? 61 THR D CB 1 ATOM 6554 O OG1 . THR D 2 61 ? 28.925 -21.322 7.634 1.00 106.95 ? 61 THR D OG1 1 ATOM 6555 C CG2 . THR D 2 61 ? 28.852 -23.399 6.400 1.00 106.65 ? 61 THR D CG2 1 ATOM 6556 N N . GLN D 2 62 ? 32.183 -22.650 9.370 1.00 59.67 ? 62 GLN D N 1 ATOM 6557 C CA . GLN D 2 62 ? 32.370 -23.041 10.761 1.00 56.11 ? 62 GLN D CA 1 ATOM 6558 C C . GLN D 2 62 ? 33.023 -21.888 11.536 1.00 54.20 ? 62 GLN D C 1 ATOM 6559 O O . GLN D 2 62 ? 33.724 -21.060 10.956 1.00 57.64 ? 62 GLN D O 1 ATOM 6560 C CB . GLN D 2 62 ? 33.214 -24.320 10.809 1.00 57.33 ? 62 GLN D CB 1 ATOM 6561 C CG . GLN D 2 62 ? 33.484 -24.871 12.200 1.00 55.32 ? 62 GLN D CG 1 ATOM 6562 C CD . GLN D 2 62 ? 33.781 -26.362 12.203 1.00 56.98 ? 62 GLN D CD 1 ATOM 6563 O OE1 . GLN D 2 62 ? 33.343 -27.103 11.318 1.00 58.64 ? 62 GLN D OE1 1 ATOM 6564 N NE2 . GLN D 2 62 ? 34.520 -26.813 13.212 1.00 57.24 ? 62 GLN D NE2 1 ATOM 6565 N N . PHE D 2 63 ? 32.781 -21.839 12.840 1.00 49.84 ? 63 PHE D N 1 ATOM 6566 C CA . PHE D 2 63 ? 33.194 -20.705 13.667 1.00 47.72 ? 63 PHE D CA 1 ATOM 6567 C C . PHE D 2 63 ? 34.715 -20.568 13.796 1.00 49.44 ? 63 PHE D C 1 ATOM 6568 O O . PHE D 2 63 ? 35.441 -21.562 13.887 1.00 50.01 ? 63 PHE D O 1 ATOM 6569 C CB . PHE D 2 63 ? 32.576 -20.828 15.059 1.00 43.79 ? 63 PHE D CB 1 ATOM 6570 C CG . PHE D 2 63 ? 32.940 -19.706 15.988 1.00 41.85 ? 63 PHE D CG 1 ATOM 6571 C CD1 . PHE D 2 63 ? 32.205 -18.529 15.994 1.00 40.44 ? 63 PHE D CD1 1 ATOM 6572 C CD2 . PHE D 2 63 ? 34.002 -19.834 16.872 1.00 41.17 ? 63 PHE D CD2 1 ATOM 6573 C CE1 . PHE D 2 63 ? 32.528 -17.504 16.853 1.00 39.12 ? 63 PHE D CE1 1 ATOM 6574 C CE2 . PHE D 2 63 ? 34.330 -18.803 17.730 1.00 39.69 ? 63 PHE D CE2 1 ATOM 6575 C CZ . PHE D 2 63 ? 33.593 -17.639 17.720 1.00 38.37 ? 63 PHE D CZ 1 ATOM 6576 N N . GLU D 2 64 ? 35.180 -19.321 13.819 1.00 50.19 ? 64 GLU D N 1 ATOM 6577 C CA . GLU D 2 64 ? 36.589 -19.030 13.988 1.00 52.50 ? 64 GLU D CA 1 ATOM 6578 C C . GLU D 2 64 ? 36.805 -18.251 15.274 1.00 49.56 ? 64 GLU D C 1 ATOM 6579 O O . GLU D 2 64 ? 36.200 -17.192 15.484 1.00 48.65 ? 64 GLU D O 1 ATOM 6580 C CB . GLU D 2 64 ? 37.124 -18.257 12.779 1.00 57.31 ? 64 GLU D CB 1 ATOM 6581 C CG . GLU D 2 64 ? 37.421 -19.154 11.590 1.00 62.01 ? 64 GLU D CG 1 ATOM 6582 C CD . GLU D 2 64 ? 37.725 -18.386 10.315 1.00 67.48 ? 64 GLU D CD 1 ATOM 6583 O OE1 . GLU D 2 64 ? 37.957 -17.156 10.384 1.00 68.76 ? 64 GLU D OE1 1 ATOM 6584 O OE2 . GLU D 2 64 ? 37.722 -19.022 9.239 1.00 70.84 ? 64 GLU D OE2 1 ATOM 6585 N N . ALA D 2 65 ? 37.666 -18.790 16.136 1.00 49.08 ? 65 ALA D N 1 ATOM 6586 C CA . ALA D 2 65 ? 38.019 -18.140 17.395 1.00 46.97 ? 65 ALA D CA 1 ATOM 6587 C C . ALA D 2 65 ? 39.027 -17.011 17.146 1.00 49.05 ? 65 ALA D C 1 ATOM 6588 O O . ALA D 2 65 ? 39.899 -17.122 16.292 1.00 52.17 ? 65 ALA D O 1 ATOM 6589 C CB . ALA D 2 65 ? 38.580 -19.161 18.371 1.00 47.03 ? 65 ALA D CB 1 ATOM 6590 N N . VAL D 2 66 ? 38.891 -15.922 17.893 1.00 47.36 ? 66 VAL D N 1 ATOM 6591 C CA . VAL D 2 66 ? 39.728 -14.738 17.687 1.00 50.13 ? 66 VAL D CA 1 ATOM 6592 C C . VAL D 2 66 ? 40.159 -14.180 19.031 1.00 48.10 ? 66 VAL D C 1 ATOM 6593 O O . VAL D 2 66 ? 39.322 -13.880 19.865 1.00 45.47 ? 66 VAL D O 1 ATOM 6594 C CB . VAL D 2 66 ? 38.976 -13.633 16.908 1.00 50.18 ? 66 VAL D CB 1 ATOM 6595 C CG1 . VAL D 2 66 ? 39.851 -12.390 16.757 1.00 53.35 ? 66 VAL D CG1 1 ATOM 6596 C CG2 . VAL D 2 66 ? 38.529 -14.146 15.542 1.00 52.36 ? 66 VAL D CG2 1 ATOM 6597 N N . GLY D 2 67 ? 41.461 -14.040 19.232 1.00 50.81 ? 67 GLY D N 1 ATOM 6598 C CA . GLY D 2 67 ? 41.977 -13.488 20.472 1.00 50.11 ? 67 GLY D CA 1 ATOM 6599 C C . GLY D 2 67 ? 41.498 -12.069 20.745 1.00 47.19 ? 67 GLY D C 1 ATOM 6600 O O . GLY D 2 67 ? 41.763 -11.145 19.976 1.00 49.10 ? 67 GLY D O 1 ATOM 6601 N N . ARG D 2 68 ? 40.763 -11.910 21.837 1.00 43.03 ? 68 ARG D N 1 ATOM 6602 C CA . ARG D 2 68 ? 40.388 -10.601 22.346 1.00 40.28 ? 68 ARG D CA 1 ATOM 6603 C C . ARG D 2 68 ? 40.909 -10.479 23.755 1.00 39.56 ? 68 ARG D C 1 ATOM 6604 O O . ARG D 2 68 ? 40.957 -11.462 24.479 1.00 38.81 ? 68 ARG D O 1 ATOM 6605 C CB . ARG D 2 68 ? 38.878 -10.436 22.351 1.00 36.54 ? 68 ARG D CB 1 ATOM 6606 C CG . ARG D 2 68 ? 38.263 -10.557 20.972 1.00 37.07 ? 68 ARG D CG 1 ATOM 6607 C CD . ARG D 2 68 ? 36.762 -10.321 21.001 1.00 33.91 ? 68 ARG D CD 1 ATOM 6608 N NE . ARG D 2 68 ? 36.203 -10.687 19.715 1.00 35.03 ? 68 ARG D NE 1 ATOM 6609 C CZ . ARG D 2 68 ? 35.830 -11.921 19.381 1.00 35.18 ? 68 ARG D CZ 1 ATOM 6610 N NH1 . ARG D 2 68 ? 35.912 -12.922 20.259 1.00 33.85 ? 68 ARG D NH1 1 ATOM 6611 N NH2 . ARG D 2 68 ? 35.348 -12.151 18.165 1.00 36.57 ? 68 ARG D NH2 1 ATOM 6612 N N . GLU D 2 69 ? 41.288 -9.266 24.140 1.00 39.80 ? 69 GLU D N 1 ATOM 6613 C CA . GLU D 2 69 ? 41.833 -9.026 25.463 1.00 40.50 ? 69 GLU D CA 1 ATOM 6614 C C . GLU D 2 69 ? 41.055 -8.001 26.255 1.00 36.32 ? 69 GLU D C 1 ATOM 6615 O O . GLU D 2 69 ? 40.473 -7.067 25.703 1.00 34.28 ? 69 GLU D O 1 ATOM 6616 C CB . GLU D 2 69 ? 43.286 -8.594 25.359 1.00 45.76 ? 69 GLU D CB 1 ATOM 6617 C CG . GLU D 2 69 ? 44.189 -9.753 25.030 1.00 50.79 ? 69 GLU D CG 1 ATOM 6618 C CD . GLU D 2 69 ? 45.612 -9.318 24.843 1.00 57.34 ? 69 GLU D CD 1 ATOM 6619 O OE1 . GLU D 2 69 ? 46.275 -9.038 25.865 1.00 60.69 ? 69 GLU D OE1 1 ATOM 6620 O OE2 . GLU D 2 69 ? 46.056 -9.232 23.678 1.00 61.03 ? 69 GLU D OE2 1 ATOM 6621 N N . PHE D 2 70 ? 41.075 -8.186 27.568 1.00 35.32 ? 70 PHE D N 1 ATOM 6622 C CA . PHE D 2 70 ? 40.297 -7.364 28.479 1.00 32.50 ? 70 PHE D CA 1 ATOM 6623 C C . PHE D 2 70 ? 41.128 -7.047 29.713 1.00 34.16 ? 70 PHE D C 1 ATOM 6624 O O . PHE D 2 70 ? 42.005 -7.809 30.102 1.00 36.89 ? 70 PHE D O 1 ATOM 6625 C CB . PHE D 2 70 ? 38.991 -8.077 28.855 1.00 30.01 ? 70 PHE D CB 1 ATOM 6626 C CG . PHE D 2 70 ? 38.223 -8.600 27.670 1.00 29.07 ? 70 PHE D CG 1 ATOM 6627 C CD1 . PHE D 2 70 ? 37.313 -7.802 27.010 1.00 27.32 ? 70 PHE D CD1 1 ATOM 6628 C CD2 . PHE D 2 70 ? 38.445 -9.891 27.198 1.00 30.70 ? 70 PHE D CD2 1 ATOM 6629 C CE1 . PHE D 2 70 ? 36.627 -8.274 25.907 1.00 27.47 ? 70 PHE D CE1 1 ATOM 6630 C CE2 . PHE D 2 70 ? 37.756 -10.376 26.104 1.00 29.75 ? 70 PHE D CE2 1 ATOM 6631 C CZ . PHE D 2 70 ? 36.847 -9.566 25.456 1.00 28.46 ? 70 PHE D CZ 1 ATOM 6632 N N . ASN D 2 71 ? 40.871 -5.896 30.310 1.00 33.51 ? 71 ASN D N 1 ATOM 6633 C CA . ASN D 2 71 ? 41.534 -5.542 31.549 1.00 35.67 ? 71 ASN D CA 1 ATOM 6634 C C . ASN D 2 71 ? 40.750 -6.082 32.735 1.00 35.66 ? 71 ASN D C 1 ATOM 6635 O O . ASN D 2 71 ? 39.641 -6.610 32.577 1.00 32.42 ? 71 ASN D O 1 ATOM 6636 C CB . ASN D 2 71 ? 41.764 -4.035 31.643 1.00 35.29 ? 71 ASN D CB 1 ATOM 6637 C CG . ASN D 2 71 ? 40.488 -3.238 31.750 1.00 32.05 ? 71 ASN D CG 1 ATOM 6638 O OD1 . ASN D 2 71 ? 39.532 -3.626 32.428 1.00 30.51 ? 71 ASN D OD1 1 ATOM 6639 N ND2 . ASN D 2 71 ? 40.481 -2.080 31.105 1.00 32.11 ? 71 ASN D ND2 1 ATOM 6640 N N . ASN D 2 72 ? 41.326 -5.937 33.925 1.00 39.58 ? 72 ASN D N 1 ATOM 6641 C CA . ASN D 2 72 ? 40.776 -6.591 35.110 1.00 41.64 ? 72 ASN D CA 1 ATOM 6642 C C . ASN D 2 72 ? 39.531 -5.923 35.718 1.00 37.97 ? 72 ASN D C 1 ATOM 6643 O O . ASN D 2 72 ? 39.056 -6.372 36.750 1.00 40.06 ? 72 ASN D O 1 ATOM 6644 C CB . ASN D 2 72 ? 41.872 -6.832 36.169 1.00 47.38 ? 72 ASN D CB 1 ATOM 6645 C CG . ASN D 2 72 ? 42.042 -5.681 37.122 1.00 48.89 ? 72 ASN D CG 1 ATOM 6646 O OD1 . ASN D 2 72 ? 42.121 -5.887 38.329 1.00 53.54 ? 72 ASN D OD1 1 ATOM 6647 N ND2 . ASN D 2 72 ? 42.108 -4.464 36.597 1.00 47.38 ? 72 ASN D ND2 1 ATOM 6648 N N . LEU D 2 73 ? 39.020 -4.861 35.094 1.00 33.91 ? 73 LEU D N 1 ATOM 6649 C CA . LEU D 2 73 ? 37.666 -4.357 35.404 1.00 31.10 ? 73 LEU D CA 1 ATOM 6650 C C . LEU D 2 73 ? 36.657 -4.622 34.275 1.00 28.15 ? 73 LEU D C 1 ATOM 6651 O O . LEU D 2 73 ? 35.581 -4.046 34.256 1.00 26.31 ? 73 LEU D O 1 ATOM 6652 C CB . LEU D 2 73 ? 37.713 -2.873 35.767 1.00 30.69 ? 73 LEU D CB 1 ATOM 6653 C CG . LEU D 2 73 ? 38.217 -2.566 37.186 1.00 33.41 ? 73 LEU D CG 1 ATOM 6654 C CD1 . LEU D 2 73 ? 38.395 -1.072 37.383 1.00 32.68 ? 73 LEU D CD1 1 ATOM 6655 C CD2 . LEU D 2 73 ? 37.280 -3.118 38.249 1.00 34.74 ? 73 LEU D CD2 1 ATOM 6656 N N . GLU D 2 74 ? 37.020 -5.519 33.354 1.00 28.08 ? 74 GLU D N 1 ATOM 6657 C CA . GLU D 2 74 ? 36.160 -5.990 32.281 1.00 25.74 ? 74 GLU D CA 1 ATOM 6658 C C . GLU D 2 74 ? 35.985 -7.512 32.411 1.00 26.79 ? 74 GLU D C 1 ATOM 6659 O O . GLU D 2 74 ? 35.922 -8.232 31.406 1.00 25.90 ? 74 GLU D O 1 ATOM 6660 C CB . GLU D 2 74 ? 36.814 -5.675 30.928 1.00 25.40 ? 74 GLU D CB 1 ATOM 6661 C CG . GLU D 2 74 ? 36.928 -4.197 30.572 1.00 24.52 ? 74 GLU D CG 1 ATOM 6662 C CD . GLU D 2 74 ? 37.688 -3.974 29.271 1.00 25.08 ? 74 GLU D CD 1 ATOM 6663 O OE1 . GLU D 2 74 ? 38.544 -4.806 28.910 1.00 26.41 ? 74 GLU D OE1 1 ATOM 6664 O OE2 . GLU D 2 74 ? 37.428 -2.965 28.599 1.00 24.39 ? 74 GLU D OE2 1 ATOM 6665 N N . ARG D 2 75 ? 35.918 -8.008 33.642 1.00 28.80 ? 75 ARG D N 1 ATOM 6666 C CA . ARG D 2 75 ? 35.837 -9.457 33.881 1.00 31.40 ? 75 ARG D CA 1 ATOM 6667 C C . ARG D 2 75 ? 34.530 -10.072 33.357 1.00 29.65 ? 75 ARG D C 1 ATOM 6668 O O . ARG D 2 75 ? 34.499 -11.257 32.969 1.00 29.71 ? 75 ARG D O 1 ATOM 6669 C CB . ARG D 2 75 ? 36.013 -9.769 35.366 1.00 35.99 ? 75 ARG D CB 1 ATOM 6670 C CG . ARG D 2 75 ? 37.361 -9.350 35.946 1.00 40.26 ? 75 ARG D CG 1 ATOM 6671 C CD . ARG D 2 75 ? 38.399 -10.412 35.681 1.00 46.06 ? 75 ARG D CD 1 ATOM 6672 N NE . ARG D 2 75 ? 39.768 -10.087 36.101 1.00 51.82 ? 75 ARG D NE 1 ATOM 6673 C CZ . ARG D 2 75 ? 40.197 -9.991 37.359 1.00 57.26 ? 75 ARG D CZ 1 ATOM 6674 N NH1 . ARG D 2 75 ? 39.365 -10.131 38.387 1.00 59.40 ? 75 ARG D NH1 1 ATOM 6675 N NH2 . ARG D 2 75 ? 41.477 -9.717 37.591 1.00 61.33 ? 75 ARG D NH2 1 ATOM 6676 N N . ARG D 2 76 ? 33.462 -9.269 33.325 1.00 27.16 ? 76 ARG D N 1 ATOM 6677 C CA . ARG D 2 76 ? 32.147 -9.750 32.866 1.00 26.46 ? 76 ARG D CA 1 ATOM 6678 C C . ARG D 2 76 ? 32.107 -10.057 31.367 1.00 25.30 ? 76 ARG D C 1 ATOM 6679 O O . ARG D 2 76 ? 31.627 -11.136 30.959 1.00 24.82 ? 76 ARG D O 1 ATOM 6680 C CB . ARG D 2 76 ? 31.035 -8.757 33.227 1.00 25.22 ? 76 ARG D CB 1 ATOM 6681 C CG . ARG D 2 76 ? 30.744 -8.716 34.724 1.00 26.82 ? 76 ARG D CG 1 ATOM 6682 C CD . ARG D 2 76 ? 29.825 -7.567 35.064 1.00 26.17 ? 76 ARG D CD 1 ATOM 6683 N NE . ARG D 2 76 ? 30.410 -6.290 34.640 1.00 23.25 ? 76 ARG D NE 1 ATOM 6684 C CZ . ARG D 2 76 ? 29.724 -5.242 34.193 1.00 21.97 ? 76 ARG D CZ 1 ATOM 6685 N NH1 . ARG D 2 76 ? 28.397 -5.277 34.098 1.00 23.41 ? 76 ARG D NH1 1 ATOM 6686 N NH2 . ARG D 2 76 ? 30.376 -4.146 33.839 1.00 20.18 ? 76 ARG D NH2 1 ATOM 6687 N N . ILE D 2 77 ? 32.609 -9.114 30.567 1.00 23.86 ? 77 ILE D N 1 ATOM 6688 C CA . ILE D 2 77 ? 32.645 -9.283 29.112 1.00 23.78 ? 77 ILE D CA 1 ATOM 6689 C C . ILE D 2 77 ? 33.690 -10.278 28.638 1.00 24.45 ? 77 ILE D C 1 ATOM 6690 O O . ILE D 2 77 ? 33.477 -10.964 27.632 1.00 24.33 ? 77 ILE D O 1 ATOM 6691 C CB . ILE D 2 77 ? 32.798 -7.950 28.351 1.00 23.71 ? 77 ILE D CB 1 ATOM 6692 C CG1 . ILE D 2 77 ? 34.014 -7.151 28.839 1.00 24.39 ? 77 ILE D CG1 1 ATOM 6693 C CG2 . ILE D 2 77 ? 31.530 -7.131 28.518 1.00 23.68 ? 77 ILE D CG2 1 ATOM 6694 C CD1 . ILE D 2 77 ? 34.242 -5.861 28.073 1.00 24.76 ? 77 ILE D CD1 1 ATOM 6695 N N . GLU D 2 78 ? 34.802 -10.354 29.363 1.00 25.90 ? 78 GLU D N 1 ATOM 6696 C CA . GLU D 2 78 ? 35.834 -11.353 29.117 1.00 28.08 ? 78 GLU D CA 1 ATOM 6697 C C . GLU D 2 78 ? 35.253 -12.762 29.311 1.00 28.38 ? 78 GLU D C 1 ATOM 6698 O O . GLU D 2 78 ? 35.533 -13.661 28.535 1.00 28.52 ? 78 GLU D O 1 ATOM 6699 C CB . GLU D 2 78 ? 37.034 -11.122 30.052 1.00 31.25 ? 78 GLU D CB 1 ATOM 6700 C CG . GLU D 2 78 ? 38.106 -12.204 30.023 1.00 35.62 ? 78 GLU D CG 1 ATOM 6701 C CD . GLU D 2 78 ? 39.167 -12.020 31.098 1.00 40.70 ? 78 GLU D CD 1 ATOM 6702 O OE1 . GLU D 2 78 ? 38.918 -11.304 32.099 1.00 42.64 ? 78 GLU D OE1 1 ATOM 6703 O OE2 . GLU D 2 78 ? 40.269 -12.598 30.955 1.00 45.77 ? 78 GLU D OE2 1 ATOM 6704 N N . ASN D 2 79 ? 34.443 -12.940 30.349 1.00 28.68 ? 79 ASN D N 1 ATOM 6705 C CA . ASN D 2 79 ? 33.802 -14.234 30.627 1.00 30.06 ? 79 ASN D CA 1 ATOM 6706 C C . ASN D 2 79 ? 32.737 -14.550 29.574 1.00 28.62 ? 79 ASN D C 1 ATOM 6707 O O . ASN D 2 79 ? 32.620 -15.688 29.116 1.00 28.84 ? 79 ASN D O 1 ATOM 6708 C CB . ASN D 2 79 ? 33.186 -14.235 32.029 1.00 31.80 ? 79 ASN D CB 1 ATOM 6709 C CG . ASN D 2 79 ? 32.485 -15.536 32.354 1.00 34.52 ? 79 ASN D CG 1 ATOM 6710 O OD1 . ASN D 2 79 ? 31.267 -15.599 32.360 1.00 35.29 ? 79 ASN D OD1 1 ATOM 6711 N ND2 . ASN D 2 79 ? 33.249 -16.585 32.590 1.00 37.04 ? 79 ASN D ND2 1 ATOM 6712 N N . LEU D 2 80 ? 31.970 -13.524 29.205 1.00 27.03 ? 80 LEU D N 1 ATOM 6713 C CA . LEU D 2 80 ? 30.998 -13.600 28.113 1.00 26.87 ? 80 LEU D CA 1 ATOM 6714 C C . LEU D 2 80 ? 31.699 -13.994 26.795 1.00 26.83 ? 80 LEU D C 1 ATOM 6715 O O . LEU D 2 80 ? 31.267 -14.923 26.111 1.00 27.26 ? 80 LEU D O 1 ATOM 6716 C CB . LEU D 2 80 ? 30.296 -12.243 27.956 1.00 26.15 ? 80 LEU D CB 1 ATOM 6717 C CG . LEU D 2 80 ? 29.032 -12.126 27.099 1.00 27.05 ? 80 LEU D CG 1 ATOM 6718 C CD1 . LEU D 2 80 ? 28.257 -10.869 27.479 1.00 27.79 ? 80 LEU D CD1 1 ATOM 6719 C CD2 . LEU D 2 80 ? 29.345 -12.110 25.608 1.00 26.81 ? 80 LEU D CD2 1 ATOM 6720 N N . ASN D 2 81 ? 32.778 -13.285 26.458 1.00 26.26 ? 81 ASN D N 1 ATOM 6721 C CA . ASN D 2 81 ? 33.610 -13.634 25.316 1.00 26.99 ? 81 ASN D CA 1 ATOM 6722 C C . ASN D 2 81 ? 34.089 -15.089 25.359 1.00 28.95 ? 81 ASN D C 1 ATOM 6723 O O . ASN D 2 81 ? 34.010 -15.807 24.358 1.00 28.90 ? 81 ASN D O 1 ATOM 6724 C CB . ASN D 2 81 ? 34.823 -12.712 25.254 1.00 27.48 ? 81 ASN D CB 1 ATOM 6725 C CG . ASN D 2 81 ? 35.685 -12.968 24.048 1.00 28.91 ? 81 ASN D CG 1 ATOM 6726 O OD1 . ASN D 2 81 ? 35.258 -12.758 22.918 1.00 29.92 ? 81 ASN D OD1 1 ATOM 6727 N ND2 . ASN D 2 81 ? 36.902 -13.424 24.275 1.00 30.69 ? 81 ASN D ND2 1 ATOM 6728 N N . LYS D 2 82 ? 34.587 -15.514 26.516 1.00 31.01 ? 82 LYS D N 1 ATOM 6729 C CA . LYS D 2 82 ? 35.165 -16.845 26.648 1.00 34.56 ? 82 LYS D CA 1 ATOM 6730 C C . LYS D 2 82 ? 34.102 -17.926 26.500 1.00 35.19 ? 82 LYS D C 1 ATOM 6731 O O . LYS D 2 82 ? 34.351 -18.947 25.876 1.00 36.22 ? 82 LYS D O 1 ATOM 6732 C CB . LYS D 2 82 ? 35.880 -17.025 27.992 1.00 37.26 ? 82 LYS D CB 1 ATOM 6733 C CG . LYS D 2 82 ? 36.392 -18.454 28.200 1.00 40.74 ? 82 LYS D CG 1 ATOM 6734 C CD . LYS D 2 82 ? 37.523 -18.515 29.210 1.00 44.93 ? 82 LYS D CD 1 ATOM 6735 C CE . LYS D 2 82 ? 38.303 -19.832 29.137 1.00 49.11 ? 82 LYS D CE 1 ATOM 6736 N NZ . LYS D 2 82 ? 37.973 -20.757 30.258 1.00 52.13 ? 82 LYS D NZ 1 ATOM 6737 N N . LYS D 2 83 ? 32.933 -17.687 27.100 1.00 35.19 ? 83 LYS D N 1 ATOM 6738 C CA . LYS D 2 83 ? 31.814 -18.628 27.062 1.00 35.63 ? 83 LYS D CA 1 ATOM 6739 C C . LYS D 2 83 ? 31.229 -18.714 25.670 1.00 34.60 ? 83 LYS D C 1 ATOM 6740 O O . LYS D 2 83 ? 30.865 -19.796 25.240 1.00 35.57 ? 83 LYS D O 1 ATOM 6741 C CB . LYS D 2 83 ? 30.713 -18.244 28.066 1.00 36.04 ? 83 LYS D CB 1 ATOM 6742 C CG . LYS D 2 83 ? 31.020 -18.645 29.503 1.00 38.40 ? 83 LYS D CG 1 ATOM 6743 N N . MET D 2 84 ? 31.146 -17.589 24.956 1.00 33.30 ? 84 MET D N 1 ATOM 6744 C CA . MET D 2 84 ? 30.611 -17.624 23.595 1.00 33.28 ? 84 MET D CA 1 ATOM 6745 C C . MET D 2 84 ? 31.552 -18.337 22.603 1.00 33.86 ? 84 MET D C 1 ATOM 6746 O O . MET D 2 84 ? 31.076 -18.984 21.683 1.00 33.92 ? 84 MET D O 1 ATOM 6747 C CB . MET D 2 84 ? 30.179 -16.233 23.113 1.00 33.24 ? 84 MET D CB 1 ATOM 6748 C CG . MET D 2 84 ? 31.142 -15.449 22.269 1.00 34.20 ? 84 MET D CG 1 ATOM 6749 S SD . MET D 2 84 ? 31.035 -15.740 20.497 1.00 36.55 ? 84 MET D SD 1 ATOM 6750 C CE . MET D 2 84 ? 32.294 -14.606 19.930 1.00 37.46 ? 84 MET D CE 1 ATOM 6751 N N . GLU D 2 85 ? 32.869 -18.244 22.794 1.00 34.40 ? 85 GLU D N 1 ATOM 6752 C CA . GLU D 2 85 ? 33.801 -18.882 21.866 1.00 36.07 ? 85 GLU D CA 1 ATOM 6753 C C . GLU D 2 85 ? 33.867 -20.384 22.122 1.00 37.83 ? 85 GLU D C 1 ATOM 6754 O O . GLU D 2 85 ? 33.760 -21.174 21.185 1.00 38.11 ? 85 GLU D O 1 ATOM 6755 C CB . GLU D 2 85 ? 35.185 -18.228 21.910 1.00 37.54 ? 85 GLU D CB 1 ATOM 6756 C CG . GLU D 2 85 ? 35.192 -16.850 21.245 1.00 37.76 ? 85 GLU D CG 1 ATOM 6757 C CD . GLU D 2 85 ? 36.570 -16.374 20.810 1.00 40.93 ? 85 GLU D CD 1 ATOM 6758 O OE1 . GLU D 2 85 ? 37.590 -16.801 21.411 1.00 43.51 ? 85 GLU D OE1 1 ATOM 6759 O OE2 . GLU D 2 85 ? 36.627 -15.562 19.858 1.00 41.24 ? 85 GLU D OE2 1 ATOM 6760 N N . ASP D 2 86 ? 34.014 -20.772 23.388 1.00 38.73 ? 86 ASP D N 1 ATOM 6761 C CA . ASP D 2 86 ? 33.877 -22.171 23.786 1.00 41.46 ? 86 ASP D CA 1 ATOM 6762 C C . ASP D 2 86 ? 32.510 -22.744 23.400 1.00 39.76 ? 86 ASP D C 1 ATOM 6763 O O . ASP D 2 86 ? 32.412 -23.899 22.986 1.00 40.37 ? 86 ASP D O 1 ATOM 6764 C CB . ASP D 2 86 ? 34.095 -22.334 25.296 1.00 44.17 ? 86 ASP D CB 1 ATOM 6765 C CG . ASP D 2 86 ? 35.558 -22.484 25.660 1.00 47.39 ? 86 ASP D CG 1 ATOM 6766 O OD1 . ASP D 2 86 ? 36.205 -23.442 25.161 1.00 50.83 ? 86 ASP D OD1 1 ATOM 6767 O OD2 . ASP D 2 86 ? 36.050 -21.655 26.453 1.00 47.64 ? 86 ASP D OD2 1 ATOM 6768 N N . GLY D 2 87 ? 31.469 -21.928 23.531 1.00 37.12 ? 87 GLY D N 1 ATOM 6769 C CA . GLY D 2 87 ? 30.118 -22.334 23.165 1.00 36.90 ? 87 GLY D CA 1 ATOM 6770 C C . GLY D 2 87 ? 30.018 -22.782 21.716 1.00 36.26 ? 87 GLY D C 1 ATOM 6771 O O . GLY D 2 87 ? 29.541 -23.887 21.425 1.00 36.97 ? 87 GLY D O 1 ATOM 6772 N N . PHE D 2 88 ? 30.476 -21.926 20.807 1.00 34.69 ? 88 PHE D N 1 ATOM 6773 C CA . PHE D 2 88 ? 30.482 -22.276 19.394 1.00 34.95 ? 88 PHE D CA 1 ATOM 6774 C C . PHE D 2 88 ? 31.395 -23.473 19.111 1.00 36.07 ? 88 PHE D C 1 ATOM 6775 O O . PHE D 2 88 ? 31.029 -24.345 18.334 1.00 36.96 ? 88 PHE D O 1 ATOM 6776 C CB . PHE D 2 88 ? 30.838 -21.077 18.515 1.00 34.32 ? 88 PHE D CB 1 ATOM 6777 C CG . PHE D 2 88 ? 29.699 -20.111 18.330 1.00 33.65 ? 88 PHE D CG 1 ATOM 6778 C CD1 . PHE D 2 88 ? 28.531 -20.515 17.706 1.00 34.22 ? 88 PHE D CD1 1 ATOM 6779 C CD2 . PHE D 2 88 ? 29.795 -18.795 18.787 1.00 32.55 ? 88 PHE D CD2 1 ATOM 6780 C CE1 . PHE D 2 88 ? 27.480 -19.637 17.528 1.00 34.87 ? 88 PHE D CE1 1 ATOM 6781 C CE2 . PHE D 2 88 ? 28.743 -17.912 18.617 1.00 32.82 ? 88 PHE D CE2 1 ATOM 6782 C CZ . PHE D 2 88 ? 27.582 -18.338 17.983 1.00 34.40 ? 88 PHE D CZ 1 ATOM 6783 N N . LEU D 2 89 ? 32.549 -23.538 19.764 1.00 36.39 ? 89 LEU D N 1 ATOM 6784 C CA . LEU D 2 89 ? 33.456 -24.663 19.554 1.00 38.72 ? 89 LEU D CA 1 ATOM 6785 C C . LEU D 2 89 ? 32.803 -25.986 19.954 1.00 39.84 ? 89 LEU D C 1 ATOM 6786 O O . LEU D 2 89 ? 32.863 -26.956 19.201 1.00 40.73 ? 89 LEU D O 1 ATOM 6787 C CB . LEU D 2 89 ? 34.781 -24.447 20.289 1.00 40.04 ? 89 LEU D CB 1 ATOM 6788 C CG . LEU D 2 89 ? 35.629 -23.283 19.744 1.00 40.25 ? 89 LEU D CG 1 ATOM 6789 C CD1 . LEU D 2 89 ? 36.840 -23.023 20.630 1.00 42.05 ? 89 LEU D CD1 1 ATOM 6790 C CD2 . LEU D 2 89 ? 36.061 -23.521 18.303 1.00 42.04 ? 89 LEU D CD2 1 ATOM 6791 N N . ASP D 2 90 ? 32.148 -26.012 21.113 1.00 40.25 ? 90 ASP D N 1 ATOM 6792 C CA . ASP D 2 90 ? 31.418 -27.207 21.566 1.00 42.06 ? 90 ASP D CA 1 ATOM 6793 C C . ASP D 2 90 ? 30.304 -27.595 20.590 1.00 41.56 ? 90 ASP D C 1 ATOM 6794 O O . ASP D 2 90 ? 30.125 -28.772 20.287 1.00 42.79 ? 90 ASP D O 1 ATOM 6795 C CB . ASP D 2 90 ? 30.832 -26.997 22.969 1.00 43.00 ? 90 ASP D CB 1 ATOM 6796 C CG . ASP D 2 90 ? 31.901 -26.972 24.065 1.00 45.39 ? 90 ASP D CG 1 ATOM 6797 O OD1 . ASP D 2 90 ? 33.033 -27.444 23.826 1.00 47.59 ? 90 ASP D OD1 1 ATOM 6798 O OD2 . ASP D 2 90 ? 31.607 -26.486 25.184 1.00 46.57 ? 90 ASP D OD2 1 ATOM 6799 N N . VAL D 2 91 ? 29.570 -26.598 20.096 1.00 40.05 ? 91 VAL D N 1 ATOM 6800 C CA . VAL D 2 91 ? 28.529 -26.818 19.080 1.00 40.13 ? 91 VAL D CA 1 ATOM 6801 C C . VAL D 2 91 ? 29.108 -27.472 17.822 1.00 40.84 ? 91 VAL D C 1 ATOM 6802 O O . VAL D 2 91 ? 28.578 -28.473 17.342 1.00 41.82 ? 91 VAL D O 1 ATOM 6803 C CB . VAL D 2 91 ? 27.831 -25.489 18.692 1.00 39.18 ? 91 VAL D CB 1 ATOM 6804 C CG1 . VAL D 2 91 ? 27.019 -25.631 17.406 1.00 40.32 ? 91 VAL D CG1 1 ATOM 6805 C CG2 . VAL D 2 91 ? 26.945 -24.998 19.832 1.00 39.11 ? 91 VAL D CG2 1 ATOM 6806 N N . TRP D 2 92 ? 30.188 -26.904 17.289 1.00 40.44 ? 92 TRP D N 1 ATOM 6807 C CA . TRP D 2 92 ? 30.768 -27.405 16.039 1.00 42.22 ? 92 TRP D CA 1 ATOM 6808 C C . TRP D 2 92 ? 31.494 -28.740 16.225 1.00 43.97 ? 92 TRP D C 1 ATOM 6809 O O . TRP D 2 92 ? 31.520 -29.572 15.313 1.00 45.41 ? 92 TRP D O 1 ATOM 6810 C CB . TRP D 2 92 ? 31.675 -26.354 15.387 1.00 42.03 ? 92 TRP D CB 1 ATOM 6811 C CG . TRP D 2 92 ? 30.893 -25.283 14.704 1.00 41.51 ? 92 TRP D CG 1 ATOM 6812 C CD1 . TRP D 2 92 ? 30.760 -23.982 15.101 1.00 40.22 ? 92 TRP D CD1 1 ATOM 6813 C CD2 . TRP D 2 92 ? 30.117 -25.417 13.506 1.00 42.88 ? 92 TRP D CD2 1 ATOM 6814 N NE1 . TRP D 2 92 ? 29.962 -23.298 14.219 1.00 41.21 ? 92 TRP D NE1 1 ATOM 6815 C CE2 . TRP D 2 92 ? 29.549 -24.156 13.234 1.00 42.97 ? 92 TRP D CE2 1 ATOM 6816 C CE3 . TRP D 2 92 ? 29.851 -26.479 12.634 1.00 44.61 ? 92 TRP D CE3 1 ATOM 6817 C CZ2 . TRP D 2 92 ? 28.726 -23.929 12.127 1.00 45.29 ? 92 TRP D CZ2 1 ATOM 6818 C CZ3 . TRP D 2 92 ? 29.033 -26.253 11.531 1.00 46.41 ? 92 TRP D CZ3 1 ATOM 6819 C CH2 . TRP D 2 92 ? 28.483 -24.988 11.288 1.00 47.12 ? 92 TRP D CH2 1 ATOM 6820 N N . THR D 2 93 ? 32.063 -28.938 17.413 1.00 44.40 ? 93 THR D N 1 ATOM 6821 C CA . THR D 2 93 ? 32.642 -30.221 17.799 1.00 46.37 ? 93 THR D CA 1 ATOM 6822 C C . THR D 2 93 ? 31.545 -31.285 17.808 1.00 47.39 ? 93 THR D C 1 ATOM 6823 O O . THR D 2 93 ? 31.714 -32.379 17.258 1.00 49.34 ? 93 THR D O 1 ATOM 6824 C CB . THR D 2 93 ? 33.311 -30.128 19.186 1.00 46.81 ? 93 THR D CB 1 ATOM 6825 O OG1 . THR D 2 93 ? 34.411 -29.213 19.125 1.00 46.21 ? 93 THR D OG1 1 ATOM 6826 C CG2 . THR D 2 93 ? 33.824 -31.481 19.643 1.00 50.14 ? 93 THR D CG2 1 ATOM 6827 N N . TYR D 2 94 ? 30.417 -30.945 18.423 1.00 46.50 ? 94 TYR D N 1 ATOM 6828 C CA . TYR D 2 94 ? 29.247 -31.814 18.438 1.00 47.68 ? 94 TYR D CA 1 ATOM 6829 C C . TYR D 2 94 ? 28.815 -32.153 17.016 1.00 48.01 ? 94 TYR D C 1 ATOM 6830 O O . TYR D 2 94 ? 28.579 -33.313 16.703 1.00 49.50 ? 94 TYR D O 1 ATOM 6831 C CB . TYR D 2 94 ? 28.096 -31.150 19.207 1.00 47.06 ? 94 TYR D CB 1 ATOM 6832 C CG . TYR D 2 94 ? 26.768 -31.885 19.136 1.00 49.00 ? 94 TYR D CG 1 ATOM 6833 C CD1 . TYR D 2 94 ? 26.450 -32.892 20.045 1.00 51.37 ? 94 TYR D CD1 1 ATOM 6834 C CD2 . TYR D 2 94 ? 25.820 -31.556 18.164 1.00 49.06 ? 94 TYR D CD2 1 ATOM 6835 C CE1 . TYR D 2 94 ? 25.230 -33.551 19.981 1.00 53.77 ? 94 TYR D CE1 1 ATOM 6836 C CE2 . TYR D 2 94 ? 24.602 -32.212 18.089 1.00 51.05 ? 94 TYR D CE2 1 ATOM 6837 C CZ . TYR D 2 94 ? 24.309 -33.208 18.997 1.00 53.49 ? 94 TYR D CZ 1 ATOM 6838 O OH . TYR D 2 94 ? 23.094 -33.856 18.914 1.00 56.43 ? 94 TYR D OH 1 ATOM 6839 N N . ASN D 2 95 ? 28.722 -31.140 16.160 1.00 47.38 ? 95 ASN D N 1 ATOM 6840 C CA . ASN D 2 95 ? 28.257 -31.342 14.783 1.00 48.65 ? 95 ASN D CA 1 ATOM 6841 C C . ASN D 2 95 ? 29.180 -32.237 13.955 1.00 50.70 ? 95 ASN D C 1 ATOM 6842 O O . ASN D 2 95 ? 28.712 -33.106 13.210 1.00 51.34 ? 95 ASN D O 1 ATOM 6843 C CB . ASN D 2 95 ? 28.053 -29.999 14.075 1.00 47.93 ? 95 ASN D CB 1 ATOM 6844 C CG . ASN D 2 95 ? 26.812 -29.273 14.562 1.00 47.83 ? 95 ASN D CG 1 ATOM 6845 O OD1 . ASN D 2 95 ? 25.902 -29.891 15.118 1.00 48.63 ? 95 ASN D OD1 1 ATOM 6846 N ND2 . ASN D 2 95 ? 26.769 -27.952 14.361 1.00 47.10 ? 95 ASN D ND2 1 ATOM 6847 N N . ALA D 2 96 ? 30.484 -32.020 14.096 1.00 51.04 ? 96 ALA D N 1 ATOM 6848 C CA . ALA D 2 96 ? 31.473 -32.804 13.372 1.00 53.25 ? 96 ALA D CA 1 ATOM 6849 C C . ALA D 2 96 ? 31.426 -34.271 13.790 1.00 54.96 ? 96 ALA D C 1 ATOM 6850 O O . ALA D 2 96 ? 31.350 -35.166 12.947 1.00 56.25 ? 96 ALA D O 1 ATOM 6851 C CB . ALA D 2 96 ? 32.867 -32.236 13.604 1.00 53.92 ? 96 ALA D CB 1 ATOM 6852 N N . GLU D 2 97 ? 31.480 -34.510 15.095 1.00 55.29 ? 97 GLU D N 1 ATOM 6853 C CA . GLU D 2 97 ? 31.491 -35.874 15.617 1.00 57.79 ? 97 GLU D CA 1 ATOM 6854 C C . GLU D 2 97 ? 30.191 -36.600 15.302 1.00 58.08 ? 97 GLU D C 1 ATOM 6855 O O . GLU D 2 97 ? 30.208 -37.773 14.941 1.00 59.64 ? 97 GLU D O 1 ATOM 6856 C CB . GLU D 2 97 ? 31.734 -35.880 17.131 1.00 58.31 ? 97 GLU D CB 1 ATOM 6857 C CG . GLU D 2 97 ? 33.179 -35.629 17.523 1.00 60.03 ? 97 GLU D CG 1 ATOM 6858 C CD . GLU D 2 97 ? 33.363 -35.542 19.024 1.00 61.51 ? 97 GLU D CD 1 ATOM 6859 O OE1 . GLU D 2 97 ? 32.521 -36.102 19.756 1.00 62.68 ? 97 GLU D OE1 1 ATOM 6860 O OE2 . GLU D 2 97 ? 34.343 -34.910 19.473 1.00 62.14 ? 97 GLU D OE2 1 ATOM 6861 N N . LEU D 2 98 ? 29.071 -35.896 15.448 1.00 57.10 ? 98 LEU D N 1 ATOM 6862 C CA . LEU D 2 98 ? 27.760 -36.488 15.211 1.00 58.90 ? 98 LEU D CA 1 ATOM 6863 C C . LEU D 2 98 ? 27.577 -36.864 13.751 1.00 59.95 ? 98 LEU D C 1 ATOM 6864 O O . LEU D 2 98 ? 27.103 -37.959 13.450 1.00 61.75 ? 98 LEU D O 1 ATOM 6865 C CB . LEU D 2 98 ? 26.632 -35.538 15.635 1.00 57.95 ? 98 LEU D CB 1 ATOM 6866 C CG . LEU D 2 98 ? 25.215 -36.053 15.351 1.00 59.93 ? 98 LEU D CG 1 ATOM 6867 C CD1 . LEU D 2 98 ? 24.939 -37.329 16.128 1.00 62.44 ? 98 LEU D CD1 1 ATOM 6868 C CD2 . LEU D 2 98 ? 24.157 -35.015 15.678 1.00 59.86 ? 98 LEU D CD2 1 ATOM 6869 N N . LEU D 2 99 ? 27.936 -35.949 12.851 1.00 59.40 ? 99 LEU D N 1 ATOM 6870 C CA . LEU D 2 99 ? 27.760 -36.185 11.420 1.00 61.27 ? 99 LEU D CA 1 ATOM 6871 C C . LEU D 2 99 ? 28.606 -37.369 10.943 1.00 63.21 ? 99 LEU D C 1 ATOM 6872 O O . LEU D 2 99 ? 28.197 -38.108 10.039 1.00 64.94 ? 99 LEU D O 1 ATOM 6873 C CB . LEU D 2 99 ? 28.098 -34.927 10.615 1.00 60.76 ? 99 LEU D CB 1 ATOM 6874 C CG . LEU D 2 99 ? 27.917 -35.028 9.098 1.00 63.75 ? 99 LEU D CG 1 ATOM 6875 C CD1 . LEU D 2 99 ? 26.494 -35.433 8.726 1.00 64.93 ? 99 LEU D CD1 1 ATOM 6876 C CD2 . LEU D 2 99 ? 28.302 -33.714 8.435 1.00 64.54 ? 99 LEU D CD2 1 ATOM 6877 N N . VAL D 2 100 ? 29.780 -37.538 11.552 1.00 63.34 ? 100 VAL D N 1 ATOM 6878 C CA . VAL D 2 100 ? 30.667 -38.652 11.227 1.00 66.03 ? 100 VAL D CA 1 ATOM 6879 C C . VAL D 2 100 ? 30.040 -39.983 11.642 1.00 67.36 ? 100 VAL D C 1 ATOM 6880 O O . VAL D 2 100 ? 30.044 -40.933 10.865 1.00 69.56 ? 100 VAL D O 1 ATOM 6881 C CB . VAL D 2 100 ? 32.057 -38.491 11.883 1.00 66.80 ? 100 VAL D CB 1 ATOM 6882 C CG1 . VAL D 2 100 ? 32.857 -39.790 11.807 1.00 70.42 ? 100 VAL D CG1 1 ATOM 6883 C CG2 . VAL D 2 100 ? 32.823 -37.362 11.212 1.00 66.62 ? 100 VAL D CG2 1 ATOM 6884 N N . LEU D 2 101 ? 29.509 -40.041 12.861 1.00 66.76 ? 101 LEU D N 1 ATOM 6885 C CA . LEU D 2 101 ? 28.827 -41.240 13.357 1.00 68.67 ? 101 LEU D CA 1 ATOM 6886 C C . LEU D 2 101 ? 27.607 -41.579 12.498 1.00 69.51 ? 101 LEU D C 1 ATOM 6887 O O . LEU D 2 101 ? 27.340 -42.749 12.213 1.00 70.93 ? 101 LEU D O 1 ATOM 6888 C CB . LEU D 2 101 ? 28.396 -41.050 14.813 1.00 68.19 ? 101 LEU D CB 1 ATOM 6889 C CG . LEU D 2 101 ? 29.538 -40.954 15.826 1.00 69.01 ? 101 LEU D CG 1 ATOM 6890 C CD1 . LEU D 2 101 ? 29.119 -40.155 17.043 1.00 68.13 ? 101 LEU D CD1 1 ATOM 6891 C CD2 . LEU D 2 101 ? 30.014 -42.323 16.261 1.00 72.80 ? 101 LEU D CD2 1 ATOM 6892 N N . MET D 2 102 ? 26.872 -40.546 12.091 1.00 68.65 ? 102 MET D N 1 ATOM 6893 C CA . MET D 2 102 ? 25.698 -40.729 11.244 1.00 70.40 ? 102 MET D CA 1 ATOM 6894 C C . MET D 2 102 ? 26.084 -41.190 9.844 1.00 71.20 ? 102 MET D C 1 ATOM 6895 O O . MET D 2 102 ? 25.485 -42.128 9.317 1.00 72.75 ? 102 MET D O 1 ATOM 6896 C CB . MET D 2 102 ? 24.870 -39.444 11.178 1.00 70.14 ? 102 MET D CB 1 ATOM 6897 C CG . MET D 2 102 ? 24.007 -39.238 12.414 1.00 71.29 ? 102 MET D CG 1 ATOM 6898 S SD . MET D 2 102 ? 23.408 -37.550 12.639 1.00 71.09 ? 102 MET D SD 1 ATOM 6899 C CE . MET D 2 102 ? 22.771 -37.209 11.001 1.00 72.46 ? 102 MET D CE 1 ATOM 6900 N N . GLU D 2 103 ? 27.082 -40.537 9.252 1.00 70.11 ? 103 GLU D N 1 ATOM 6901 C CA . GLU D 2 103 ? 27.552 -40.908 7.917 1.00 71.58 ? 103 GLU D CA 1 ATOM 6902 C C . GLU D 2 103 ? 28.194 -42.297 7.894 1.00 73.49 ? 103 GLU D C 1 ATOM 6903 O O . GLU D 2 103 ? 28.046 -43.030 6.919 1.00 76.00 ? 103 GLU D O 1 ATOM 6904 C CB . GLU D 2 103 ? 28.542 -39.875 7.390 1.00 71.38 ? 103 GLU D CB 1 ATOM 6905 N N . ASN D 2 104 ? 28.903 -42.661 8.960 1.00 73.27 ? 104 ASN D N 1 ATOM 6906 C CA . ASN D 2 104 ? 29.511 -43.994 9.052 1.00 76.00 ? 104 ASN D CA 1 ATOM 6907 C C . ASN D 2 104 ? 28.468 -45.110 9.039 1.00 78.23 ? 104 ASN D C 1 ATOM 6908 O O . ASN D 2 104 ? 28.626 -46.106 8.332 1.00 81.16 ? 104 ASN D O 1 ATOM 6909 C CB . ASN D 2 104 ? 30.380 -44.120 10.311 1.00 75.80 ? 104 ASN D CB 1 ATOM 6910 C CG . ASN D 2 104 ? 31.744 -43.469 10.156 1.00 75.54 ? 104 ASN D CG 1 ATOM 6911 O OD1 . ASN D 2 104 ? 32.091 -42.962 9.089 1.00 75.03 ? 104 ASN D OD1 1 ATOM 6912 N ND2 . ASN D 2 104 ? 32.531 -43.494 11.223 1.00 76.07 ? 104 ASN D ND2 1 ATOM 6913 N N . GLU D 2 105 ? 27.408 -44.931 9.822 1.00 78.14 ? 105 GLU D N 1 ATOM 6914 C CA . GLU D 2 105 ? 26.310 -45.892 9.890 1.00 80.79 ? 105 GLU D CA 1 ATOM 6915 C C . GLU D 2 105 ? 25.599 -46.013 8.544 1.00 81.35 ? 105 GLU D C 1 ATOM 6916 O O . GLU D 2 105 ? 25.333 -47.127 8.071 1.00 83.11 ? 105 GLU D O 1 ATOM 6917 C CB . GLU D 2 105 ? 25.312 -45.470 10.967 1.00 81.67 ? 105 GLU D CB 1 ATOM 6918 C CG . GLU D 2 105 ? 24.292 -46.531 11.345 1.00 85.52 ? 105 GLU D CG 1 ATOM 6919 C CD . GLU D 2 105 ? 23.642 -46.233 12.683 1.00 87.76 ? 105 GLU D CD 1 ATOM 6920 O OE1 . GLU D 2 105 ? 24.348 -46.292 13.715 1.00 88.93 ? 105 GLU D OE1 1 ATOM 6921 O OE2 . GLU D 2 105 ? 22.433 -45.914 12.704 1.00 89.51 ? 105 GLU D OE2 1 ATOM 6922 N N . ARG D 2 106 ? 25.302 -44.867 7.932 1.00 79.16 ? 106 ARG D N 1 ATOM 6923 C CA . ARG D 2 106 ? 24.693 -44.836 6.603 1.00 80.50 ? 106 ARG D CA 1 ATOM 6924 C C . ARG D 2 106 ? 25.609 -45.459 5.537 1.00 82.15 ? 106 ARG D C 1 ATOM 6925 O O . ARG D 2 106 ? 25.123 -46.104 4.609 1.00 84.59 ? 106 ARG D O 1 ATOM 6926 C CB . ARG D 2 106 ? 24.308 -43.404 6.214 1.00 79.49 ? 106 ARG D CB 1 ATOM 6927 N N . THR D 2 107 ? 26.922 -45.285 5.686 1.00 81.48 ? 107 THR D N 1 ATOM 6928 C CA . THR D 2 107 ? 27.900 -45.852 4.744 1.00 83.62 ? 107 THR D CA 1 ATOM 6929 C C . THR D 2 107 ? 28.019 -47.379 4.842 1.00 85.57 ? 107 THR D C 1 ATOM 6930 O O . THR D 2 107 ? 28.168 -48.055 3.822 1.00 88.39 ? 107 THR D O 1 ATOM 6931 C CB . THR D 2 107 ? 29.297 -45.230 4.940 1.00 83.42 ? 107 THR D CB 1 ATOM 6932 O OG1 . THR D 2 107 ? 29.208 -43.806 4.812 1.00 82.64 ? 107 THR D OG1 1 ATOM 6933 C CG2 . THR D 2 107 ? 30.284 -45.755 3.910 1.00 86.84 ? 107 THR D CG2 1 ATOM 6934 N N . LEU D 2 108 ? 27.968 -47.922 6.056 1.00 84.71 ? 108 LEU D N 1 ATOM 6935 C CA . LEU D 2 108 ? 28.014 -49.378 6.237 1.00 86.87 ? 108 LEU D CA 1 ATOM 6936 C C . LEU D 2 108 ? 26.720 -50.039 5.760 1.00 87.67 ? 108 LEU D C 1 ATOM 6937 O O . LEU D 2 108 ? 26.757 -51.119 5.166 1.00 90.11 ? 108 LEU D O 1 ATOM 6938 C CB . LEU D 2 108 ? 28.297 -49.747 7.694 1.00 87.06 ? 108 LEU D CB 1 ATOM 6939 C CG . LEU D 2 108 ? 29.687 -49.344 8.190 1.00 87.49 ? 108 LEU D CG 1 ATOM 6940 C CD1 . LEU D 2 108 ? 29.772 -49.463 9.703 1.00 88.03 ? 108 LEU D CD1 1 ATOM 6941 C CD2 . LEU D 2 108 ? 30.773 -50.175 7.523 1.00 90.84 ? 108 LEU D CD2 1 ATOM 6942 N N . ASP D 2 109 ? 25.587 -49.385 6.008 1.00 85.97 ? 109 ASP D N 1 ATOM 6943 C CA . ASP D 2 109 ? 24.295 -49.844 5.484 1.00 87.55 ? 109 ASP D CA 1 ATOM 6944 C C . ASP D 2 109 ? 24.205 -49.676 3.963 1.00 88.61 ? 109 ASP D C 1 ATOM 6945 O O . ASP D 2 109 ? 23.454 -50.393 3.300 1.00 90.97 ? 109 ASP D O 1 ATOM 6946 C CB . ASP D 2 109 ? 23.135 -49.093 6.152 1.00 86.61 ? 109 ASP D CB 1 ATOM 6947 C CG . ASP D 2 109 ? 22.995 -49.415 7.630 1.00 86.68 ? 109 ASP D CG 1 ATOM 6948 O OD1 . ASP D 2 109 ? 23.401 -50.520 8.051 1.00 88.43 ? 109 ASP D OD1 1 ATOM 6949 O OD2 . ASP D 2 109 ? 22.467 -48.559 8.372 1.00 85.69 ? 109 ASP D OD2 1 ATOM 6950 N N . PHE D 2 110 ? 24.961 -48.723 3.421 1.00 87.51 ? 110 PHE D N 1 ATOM 6951 C CA . PHE D 2 110 ? 25.015 -48.485 1.978 1.00 89.21 ? 110 PHE D CA 1 ATOM 6952 C C . PHE D 2 110 ? 25.716 -49.628 1.247 1.00 92.25 ? 110 PHE D C 1 ATOM 6953 O O . PHE D 2 110 ? 25.310 -50.011 0.146 1.00 94.90 ? 110 PHE D O 1 ATOM 6954 C CB . PHE D 2 110 ? 25.723 -47.159 1.695 1.00 87.92 ? 110 PHE D CB 1 ATOM 6955 C CG . PHE D 2 110 ? 25.920 -46.866 0.237 1.00 90.45 ? 110 PHE D CG 1 ATOM 6956 C CD1 . PHE D 2 110 ? 24.831 -46.629 -0.589 1.00 92.27 ? 110 PHE D CD1 1 ATOM 6957 C CD2 . PHE D 2 110 ? 27.198 -46.801 -0.305 1.00 91.77 ? 110 PHE D CD2 1 ATOM 6958 C CE1 . PHE D 2 110 ? 25.010 -46.346 -1.932 1.00 95.71 ? 110 PHE D CE1 1 ATOM 6959 C CE2 . PHE D 2 110 ? 27.384 -46.516 -1.645 1.00 95.22 ? 110 PHE D CE2 1 ATOM 6960 C CZ . PHE D 2 110 ? 26.288 -46.288 -2.461 1.00 97.23 ? 110 PHE D CZ 1 ATOM 6961 N N . HIS D 2 111 ? 26.765 -50.169 1.861 1.00 92.22 ? 111 HIS D N 1 ATOM 6962 C CA . HIS D 2 111 ? 27.469 -51.319 1.299 1.00 95.04 ? 111 HIS D CA 1 ATOM 6963 C C . HIS D 2 111 ? 26.658 -52.607 1.453 1.00 96.30 ? 111 HIS D C 1 ATOM 6964 O O . HIS D 2 111 ? 26.742 -53.492 0.605 1.00 99.11 ? 111 HIS D O 1 ATOM 6965 C CB . HIS D 2 111 ? 28.852 -51.478 1.932 1.00 95.54 ? 111 HIS D CB 1 ATOM 6966 C CG . HIS D 2 111 ? 29.805 -50.379 1.577 1.00 95.84 ? 111 HIS D CG 1 ATOM 6967 N ND1 . HIS D 2 111 ? 30.123 -50.063 0.274 1.00 98.33 ? 111 HIS D ND1 1 ATOM 6968 C CD2 . HIS D 2 111 ? 30.519 -49.530 2.354 1.00 94.15 ? 111 HIS D CD2 1 ATOM 6969 C CE1 . HIS D 2 111 ? 30.985 -49.061 0.263 1.00 98.36 ? 111 HIS D CE1 1 ATOM 6970 N NE2 . HIS D 2 111 ? 31.243 -48.721 1.513 1.00 95.63 ? 111 HIS D NE2 1 ATOM 6971 N N . ASP D 2 112 ? 25.880 -52.711 2.529 1.00 94.78 ? 112 ASP D N 1 ATOM 6972 C CA . ASP D 2 112 ? 24.953 -53.834 2.705 1.00 96.70 ? 112 ASP D CA 1 ATOM 6973 C C . ASP D 2 112 ? 23.833 -53.805 1.664 1.00 97.91 ? 112 ASP D C 1 ATOM 6974 O O . ASP D 2 112 ? 23.480 -54.843 1.104 1.00 100.08 ? 112 ASP D O 1 ATOM 6975 C CB . ASP D 2 112 ? 24.350 -53.848 4.121 1.00 95.91 ? 112 ASP D CB 1 ATOM 6976 C CG . ASP D 2 112 ? 25.042 -54.837 5.049 1.00 97.74 ? 112 ASP D CG 1 ATOM 6977 O OD1 . ASP D 2 112 ? 25.298 -55.985 4.620 1.00 101.08 ? 112 ASP D OD1 1 ATOM 6978 O OD2 . ASP D 2 112 ? 25.318 -54.473 6.212 1.00 96.73 ? 112 ASP D OD2 1 ATOM 6979 N N . SER D 2 113 ? 23.286 -52.616 1.413 1.00 96.67 ? 113 SER D N 1 ATOM 6980 C CA . SER D 2 113 ? 22.219 -52.432 0.420 1.00 98.77 ? 113 SER D CA 1 ATOM 6981 C C . SER D 2 113 ? 22.651 -52.859 -0.982 1.00 101.84 ? 113 SER D C 1 ATOM 6982 O O . SER D 2 113 ? 21.868 -53.453 -1.719 1.00 104.21 ? 113 SER D O 1 ATOM 6983 C CB . SER D 2 113 ? 21.762 -50.967 0.390 1.00 97.20 ? 113 SER D CB 1 ATOM 6984 O OG . SER D 2 113 ? 20.777 -50.745 -0.609 1.00 99.70 ? 113 SER D OG 1 ATOM 6985 N N . ASN D 2 114 ? 23.896 -52.551 -1.340 1.00 102.17 ? 114 ASN D N 1 ATOM 6986 C CA . ASN D 2 114 ? 24.426 -52.854 -2.669 1.00 105.73 ? 114 ASN D CA 1 ATOM 6987 C C . ASN D 2 114 ? 24.656 -54.346 -2.899 1.00 108.17 ? 114 ASN D C 1 ATOM 6988 O O . ASN D 2 114 ? 24.690 -54.797 -4.044 1.00 111.75 ? 114 ASN D O 1 ATOM 6989 C CB . ASN D 2 114 ? 25.727 -52.081 -2.915 1.00 105.84 ? 114 ASN D CB 1 ATOM 6990 C CG . ASN D 2 114 ? 25.515 -50.579 -2.979 1.00 104.98 ? 114 ASN D CG 1 ATOM 6991 O OD1 . ASN D 2 114 ? 24.438 -50.106 -3.340 1.00 106.19 ? 114 ASN D OD1 1 ATOM 6992 N ND2 . ASN D 2 114 ? 26.547 -49.820 -2.630 1.00 104.00 ? 114 ASN D ND2 1 ATOM 6993 N N . VAL D 2 115 ? 24.816 -55.104 -1.816 1.00 107.14 ? 115 VAL D N 1 ATOM 6994 C CA . VAL D 2 115 ? 24.926 -56.564 -1.895 1.00 109.66 ? 115 VAL D CA 1 ATOM 6995 C C . VAL D 2 115 ? 23.542 -57.215 -2.028 1.00 111.07 ? 115 VAL D C 1 ATOM 6996 O O . VAL D 2 115 ? 23.396 -58.208 -2.744 1.00 114.23 ? 115 VAL D O 1 ATOM 6997 C CB . VAL D 2 115 ? 25.675 -57.143 -0.673 1.00 108.87 ? 115 VAL D CB 1 ATOM 6998 C CG1 . VAL D 2 115 ? 25.705 -58.664 -0.717 1.00 111.78 ? 115 VAL D CG1 1 ATOM 6999 C CG2 . VAL D 2 115 ? 27.095 -56.592 -0.614 1.00 108.68 ? 115 VAL D CG2 1 ATOM 7000 N N . LYS D 2 116 ? 22.538 -56.663 -1.338 1.00 109.56 ? 116 LYS D N 1 ATOM 7001 C CA . LYS D 2 116 ? 21.143 -57.108 -1.498 1.00 111.46 ? 116 LYS D CA 1 ATOM 7002 C C . LYS D 2 116 ? 20.644 -56.765 -2.901 1.00 113.97 ? 116 LYS D C 1 ATOM 7003 O O . LYS D 2 116 ? 20.038 -57.603 -3.574 1.00 116.85 ? 116 LYS D O 1 ATOM 7004 C CB . LYS D 2 116 ? 20.206 -56.436 -0.488 1.00 110.18 ? 116 LYS D CB 1 ATOM 7005 C CG . LYS D 2 116 ? 20.504 -56.670 0.987 1.00 108.53 ? 116 LYS D CG 1 ATOM 7006 C CD . LYS D 2 116 ? 19.609 -55.776 1.840 1.00 107.50 ? 116 LYS D CD 1 ATOM 7007 C CE . LYS D 2 116 ? 20.090 -55.637 3.276 1.00 105.44 ? 116 LYS D CE 1 ATOM 7008 N NZ . LYS D 2 116 ? 19.688 -54.330 3.875 1.00 102.88 ? 116 LYS D NZ 1 ATOM 7009 N N . ASN D 2 117 ? 20.900 -55.524 -3.324 1.00 112.67 ? 117 ASN D N 1 ATOM 7010 C CA . ASN D 2 117 ? 20.512 -55.042 -4.657 1.00 115.82 ? 117 ASN D CA 1 ATOM 7011 C C . ASN D 2 117 ? 21.172 -55.823 -5.800 1.00 118.73 ? 117 ASN D C 1 ATOM 7012 O O . ASN D 2 117 ? 20.575 -55.994 -6.863 1.00 122.14 ? 117 ASN D O 1 ATOM 7013 C CB . ASN D 2 117 ? 20.850 -53.549 -4.816 1.00 114.73 ? 117 ASN D CB 1 ATOM 7014 C CG . ASN D 2 117 ? 20.025 -52.647 -3.905 1.00 112.74 ? 117 ASN D CG 1 ATOM 7015 O OD1 . ASN D 2 117 ? 18.971 -53.035 -3.403 1.00 113.84 ? 117 ASN D OD1 1 ATOM 7016 N ND2 . ASN D 2 117 ? 20.509 -51.430 -3.693 1.00 110.52 ? 117 ASN D ND2 1 ATOM 7017 N N . LEU D 2 118 ? 22.404 -56.279 -5.579 1.00 117.61 ? 118 LEU D N 1 ATOM 7018 C CA . LEU D 2 118 ? 23.142 -57.053 -6.579 1.00 121.04 ? 118 LEU D CA 1 ATOM 7019 C C . LEU D 2 118 ? 22.746 -58.530 -6.569 1.00 122.59 ? 118 LEU D C 1 ATOM 7020 O O . LEU D 2 118 ? 22.755 -59.181 -7.613 1.00 126.34 ? 118 LEU D O 1 ATOM 7021 C CB . LEU D 2 118 ? 24.654 -56.914 -6.353 1.00 120.21 ? 118 LEU D CB 1 ATOM 7022 C CG . LEU D 2 118 ? 25.590 -57.637 -7.331 1.00 124.06 ? 118 LEU D CG 1 ATOM 7023 C CD1 . LEU D 2 118 ? 25.299 -57.239 -8.772 1.00 128.22 ? 118 LEU D CD1 1 ATOM 7024 C CD2 . LEU D 2 118 ? 27.042 -57.351 -6.973 1.00 123.61 ? 118 LEU D CD2 1 ATOM 7025 N N . TYR D 2 119 ? 22.416 -59.057 -5.391 1.00 120.29 ? 119 TYR D N 1 ATOM 7026 C CA . TYR D 2 119 ? 21.983 -60.451 -5.261 1.00 122.17 ? 119 TYR D CA 1 ATOM 7027 C C . TYR D 2 119 ? 20.620 -60.684 -5.915 1.00 124.72 ? 119 TYR D C 1 ATOM 7028 O O . TYR D 2 119 ? 20.387 -61.731 -6.519 1.00 127.28 ? 119 TYR D O 1 ATOM 7029 C CB . TYR D 2 119 ? 21.929 -60.864 -3.787 1.00 120.08 ? 119 TYR D CB 1 ATOM 7030 C CG . TYR D 2 119 ? 21.548 -62.313 -3.581 1.00 122.51 ? 119 TYR D CG 1 ATOM 7031 C CD1 . TYR D 2 119 ? 22.483 -63.324 -3.765 1.00 124.25 ? 119 TYR D CD1 1 ATOM 7032 C CD2 . TYR D 2 119 ? 20.255 -62.672 -3.205 1.00 123.59 ? 119 TYR D CD2 1 ATOM 7033 C CE1 . TYR D 2 119 ? 22.145 -64.651 -3.580 1.00 126.85 ? 119 TYR D CE1 1 ATOM 7034 C CE2 . TYR D 2 119 ? 19.908 -63.999 -3.016 1.00 126.37 ? 119 TYR D CE2 1 ATOM 7035 C CZ . TYR D 2 119 ? 20.859 -64.985 -3.206 1.00 127.90 ? 119 TYR D CZ 1 ATOM 7036 O OH . TYR D 2 119 ? 20.536 -66.312 -3.027 1.00 130.78 ? 119 TYR D OH 1 ATOM 7037 N N . ASP D 2 120 ? 19.727 -59.705 -5.783 1.00 124.13 ? 120 ASP D N 1 ATOM 7038 C CA . ASP D 2 120 ? 18.406 -59.762 -6.413 1.00 127.63 ? 120 ASP D CA 1 ATOM 7039 C C . ASP D 2 120 ? 18.519 -59.657 -7.936 1.00 131.43 ? 120 ASP D C 1 ATOM 7040 O O . ASP D 2 120 ? 17.707 -60.231 -8.663 1.00 135.11 ? 120 ASP D O 1 ATOM 7041 C CB . ASP D 2 120 ? 17.497 -58.646 -5.877 1.00 126.69 ? 120 ASP D CB 1 ATOM 7042 C CG . ASP D 2 120 ? 17.205 -58.784 -4.385 1.00 124.07 ? 120 ASP D CG 1 ATOM 7043 O OD1 . ASP D 2 120 ? 17.026 -59.926 -3.908 1.00 124.71 ? 120 ASP D OD1 1 ATOM 7044 O OD2 . ASP D 2 120 ? 17.149 -57.744 -3.690 1.00 121.52 ? 120 ASP D OD2 1 ATOM 7045 N N . LYS D 2 121 ? 19.530 -58.927 -8.408 1.00 130.71 ? 121 LYS D N 1 ATOM 7046 C CA . LYS D 2 121 ? 19.783 -58.773 -9.843 1.00 134.89 ? 121 LYS D CA 1 ATOM 7047 C C . LYS D 2 121 ? 20.151 -60.097 -10.515 1.00 137.38 ? 121 LYS D C 1 ATOM 7048 O O . LYS D 2 121 ? 19.796 -60.322 -11.668 1.00 142.03 ? 121 LYS D O 1 ATOM 7049 C CB . LYS D 2 121 ? 20.890 -57.740 -10.086 1.00 134.03 ? 121 LYS D CB 1 ATOM 7050 C CG . LYS D 2 121 ? 21.093 -57.370 -11.549 1.00 139.36 ? 121 LYS D CG 1 ATOM 7051 C CD . LYS D 2 121 ? 21.993 -56.153 -11.691 1.00 139.02 ? 121 LYS D CD 1 ATOM 7052 C CE . LYS D 2 121 ? 22.092 -55.693 -13.137 1.00 145.30 ? 121 LYS D CE 1 ATOM 7053 N NZ . LYS D 2 121 ? 22.728 -56.718 -14.009 1.00 149.26 ? 121 LYS D NZ 1 ATOM 7054 N N . VAL D 2 122 ? 20.866 -60.961 -9.795 1.00 134.78 ? 122 VAL D N 1 ATOM 7055 C CA . VAL D 2 122 ? 21.217 -62.290 -10.305 1.00 137.14 ? 122 VAL D CA 1 ATOM 7056 C C . VAL D 2 122 ? 20.034 -63.249 -10.183 1.00 138.77 ? 122 VAL D C 1 ATOM 7057 O O . VAL D 2 122 ? 19.840 -64.104 -11.047 1.00 142.57 ? 122 VAL D O 1 ATOM 7058 C CB . VAL D 2 122 ? 22.435 -62.885 -9.567 1.00 134.81 ? 122 VAL D CB 1 ATOM 7059 C CG1 . VAL D 2 122 ? 22.776 -64.268 -10.113 1.00 137.89 ? 122 VAL D CG1 1 ATOM 7060 C CG2 . VAL D 2 122 ? 23.634 -61.953 -9.686 1.00 133.99 ? 122 VAL D CG2 1 ATOM 7061 N N . ARG D 2 123 ? 19.254 -63.111 -9.112 1.00 136.41 ? 123 ARG D N 1 ATOM 7062 C CA . ARG D 2 123 ? 18.065 -63.948 -8.904 1.00 138.68 ? 123 ARG D CA 1 ATOM 7063 C C . ARG D 2 123 ? 16.974 -63.666 -9.937 1.00 142.91 ? 123 ARG D C 1 ATOM 7064 O O . ARG D 2 123 ? 16.315 -64.592 -10.420 1.00 146.33 ? 123 ARG D O 1 ATOM 7065 C CB . ARG D 2 123 ? 17.496 -63.740 -7.497 1.00 136.09 ? 123 ARG D CB 1 ATOM 7066 C CG . ARG D 2 123 ? 16.302 -64.629 -7.172 1.00 138.99 ? 123 ARG D CG 1 ATOM 7067 C CD . ARG D 2 123 ? 16.104 -64.757 -5.671 1.00 136.87 ? 123 ARG D CD 1 ATOM 7068 N NE . ARG D 2 123 ? 16.030 -63.454 -5.005 1.00 133.94 ? 123 ARG D NE 1 ATOM 7069 C CZ . ARG D 2 123 ? 14.948 -62.675 -4.955 1.00 135.40 ? 123 ARG D CZ 1 ATOM 7070 N NH1 . ARG D 2 123 ? 13.809 -63.041 -5.539 1.00 140.18 ? 123 ARG D NH1 1 ATOM 7071 N NH2 . ARG D 2 123 ? 15.006 -61.511 -4.315 1.00 132.55 ? 123 ARG D NH2 1 ATOM 7072 N N . LEU D 2 124 ? 16.786 -62.387 -10.258 1.00 142.71 ? 124 LEU D N 1 ATOM 7073 C CA . LEU D 2 124 ? 15.788 -61.960 -11.243 1.00 147.59 ? 124 LEU D CA 1 ATOM 7074 C C . LEU D 2 124 ? 16.239 -62.263 -12.677 1.00 151.81 ? 124 LEU D C 1 ATOM 7075 O O . LEU D 2 124 ? 15.423 -62.638 -13.523 1.00 157.04 ? 124 LEU D O 1 ATOM 7076 C CB . LEU D 2 124 ? 15.490 -60.462 -11.087 1.00 146.99 ? 124 LEU D CB 1 ATOM 7077 C CG . LEU D 2 124 ? 14.544 -60.006 -9.962 1.00 145.37 ? 124 LEU D CG 1 ATOM 7078 C CD1 . LEU D 2 124 ? 14.523 -60.941 -8.757 1.00 142.43 ? 124 LEU D CD1 1 ATOM 7079 C CD2 . LEU D 2 124 ? 14.884 -58.586 -9.530 1.00 142.15 ? 124 LEU D CD2 1 ATOM 7080 N N . GLN D 2 125 ? 17.535 -62.101 -12.939 1.00 171.86 ? 125 GLN D N 1 ATOM 7081 C CA . GLN D 2 125 ? 18.116 -62.365 -14.261 1.00 171.93 ? 125 GLN D CA 1 ATOM 7082 C C . GLN D 2 125 ? 17.944 -63.827 -14.688 1.00 171.85 ? 125 GLN D C 1 ATOM 7083 O O . GLN D 2 125 ? 17.661 -64.106 -15.854 1.00 172.24 ? 125 GLN D O 1 ATOM 7084 C CB . GLN D 2 125 ? 19.598 -61.976 -14.259 1.00 171.59 ? 125 GLN D CB 1 ATOM 7085 C CG . GLN D 2 125 ? 20.333 -62.170 -15.577 1.00 171.96 ? 125 GLN D CG 1 ATOM 7086 C CD . GLN D 2 125 ? 21.673 -61.451 -15.610 1.00 171.72 ? 125 GLN D CD 1 ATOM 7087 O OE1 . GLN D 2 125 ? 22.168 -61.089 -16.676 1.00 172.10 ? 125 GLN D OE1 1 ATOM 7088 N NE2 . GLN D 2 125 ? 22.261 -61.232 -14.438 1.00 171.05 ? 125 GLN D NE2 1 ATOM 7089 N N . LEU D 2 126 ? 18.118 -64.747 -13.740 1.00 171.21 ? 126 LEU D N 1 ATOM 7090 C CA . LEU D 2 126 ? 17.872 -66.171 -13.968 1.00 171.19 ? 126 LEU D CA 1 ATOM 7091 C C . LEU D 2 126 ? 16.806 -66.671 -12.993 1.00 170.92 ? 126 LEU D C 1 ATOM 7092 O O . LEU D 2 126 ? 17.126 -67.210 -11.932 1.00 170.60 ? 126 LEU D O 1 ATOM 7093 C CB . LEU D 2 126 ? 19.164 -66.971 -13.792 1.00 170.93 ? 126 LEU D CB 1 ATOM 7094 N N . ARG D 2 127 ? 15.540 -66.486 -13.363 1.00 171.06 ? 127 ARG D N 1 ATOM 7095 C CA . ARG D 2 127 ? 14.414 -66.820 -12.487 1.00 170.81 ? 127 ARG D CA 1 ATOM 7096 C C . ARG D 2 127 ? 14.114 -68.318 -12.480 1.00 170.78 ? 127 ARG D C 1 ATOM 7097 O O . ARG D 2 127 ? 14.266 -68.978 -11.451 1.00 170.49 ? 127 ARG D O 1 ATOM 7098 C CB . ARG D 2 127 ? 13.162 -66.043 -12.905 1.00 171.19 ? 127 ARG D CB 1 ATOM 7099 N N . ASP D 2 128 ? 13.692 -68.844 -13.629 1.00 171.05 ? 128 ASP D N 1 ATOM 7100 C CA . ASP D 2 128 ? 13.311 -70.256 -13.759 1.00 171.01 ? 128 ASP D CA 1 ATOM 7101 C C . ASP D 2 128 ? 14.494 -71.166 -14.089 1.00 170.61 ? 128 ASP D C 1 ATOM 7102 O O . ASP D 2 128 ? 14.406 -72.384 -13.928 1.00 170.50 ? 128 ASP D O 1 ATOM 7103 C CB . ASP D 2 128 ? 12.240 -70.415 -14.842 1.00 171.67 ? 128 ASP D CB 1 ATOM 7104 N N . ASN D 2 129 ? 15.598 -70.571 -14.539 1.00 170.32 ? 129 ASN D N 1 ATOM 7105 C CA . ASN D 2 129 ? 16.762 -71.326 -15.006 1.00 170.20 ? 129 ASN D CA 1 ATOM 7106 C C . ASN D 2 129 ? 17.838 -71.555 -13.934 1.00 169.57 ? 129 ASN D C 1 ATOM 7107 O O . ASN D 2 129 ? 18.948 -71.985 -14.256 1.00 169.48 ? 129 ASN D O 1 ATOM 7108 C CB . ASN D 2 129 ? 17.390 -70.615 -16.215 1.00 170.47 ? 129 ASN D CB 1 ATOM 7109 C CG . ASN D 2 129 ? 16.382 -70.320 -17.316 1.00 171.00 ? 129 ASN D CG 1 ATOM 7110 O OD1 . ASN D 2 129 ? 15.204 -70.663 -17.209 1.00 171.22 ? 129 ASN D OD1 1 ATOM 7111 N ND2 . ASN D 2 129 ? 16.845 -69.676 -18.382 1.00 171.24 ? 129 ASN D ND2 1 ATOM 7112 N N . ALA D 2 130 ? 17.517 -71.278 -12.669 1.00 169.17 ? 130 ALA D N 1 ATOM 7113 C CA . ALA D 2 130 ? 18.486 -71.429 -11.577 1.00 168.61 ? 130 ALA D CA 1 ATOM 7114 C C . ALA D 2 130 ? 17.814 -71.514 -10.204 1.00 168.20 ? 130 ALA D C 1 ATOM 7115 O O . ALA D 2 130 ? 16.807 -70.849 -9.958 1.00 168.23 ? 130 ALA D O 1 ATOM 7116 C CB . ALA D 2 130 ? 19.482 -70.276 -11.599 1.00 168.32 ? 130 ALA D CB 1 ATOM 7117 N N . LYS D 2 131 ? 18.385 -72.331 -9.318 1.00 167.81 ? 131 LYS D N 1 ATOM 7118 C CA . LYS D 2 131 ? 17.912 -72.448 -7.935 1.00 167.53 ? 131 LYS D CA 1 ATOM 7119 C C . LYS D 2 131 ? 18.690 -71.514 -7.010 1.00 166.91 ? 131 LYS D C 1 ATOM 7120 O O . LYS D 2 131 ? 19.874 -71.258 -7.224 1.00 166.85 ? 131 LYS D O 1 ATOM 7121 C CB . LYS D 2 131 ? 18.041 -73.891 -7.428 1.00 167.64 ? 131 LYS D CB 1 ATOM 7122 C CG . LYS D 2 131 ? 17.875 -74.030 -5.919 1.00 167.51 ? 131 LYS D CG 1 ATOM 7123 C CD . LYS D 2 131 ? 17.782 -75.474 -5.463 1.00 167.77 ? 131 LYS D CD 1 ATOM 7124 C CE . LYS D 2 131 ? 17.807 -75.550 -3.944 1.00 167.62 ? 131 LYS D CE 1 ATOM 7125 N NZ . LYS D 2 131 ? 17.412 -76.891 -3.439 1.00 167.97 ? 131 LYS D NZ 1 ATOM 7126 N N . GLU D 2 132 ? 18.010 -71.025 -5.977 1.00 166.45 ? 132 GLU D N 1 ATOM 7127 C CA . GLU D 2 132 ? 18.628 -70.224 -4.927 1.00 165.77 ? 132 GLU D CA 1 ATOM 7128 C C . GLU D 2 132 ? 19.023 -71.152 -3.774 1.00 165.44 ? 132 GLU D C 1 ATOM 7129 O O . GLU D 2 132 ? 18.238 -72.019 -3.382 1.00 165.83 ? 132 GLU D O 1 ATOM 7130 C CB . GLU D 2 132 ? 17.630 -69.175 -4.447 1.00 165.71 ? 132 GLU D CB 1 ATOM 7131 C CG . GLU D 2 132 ? 18.243 -68.019 -3.686 1.00 165.22 ? 132 GLU D CG 1 ATOM 7132 C CD . GLU D 2 132 ? 17.196 -67.096 -3.098 1.00 165.24 ? 132 GLU D CD 1 ATOM 7133 O OE1 . GLU D 2 132 ? 16.051 -67.089 -3.600 1.00 165.54 ? 132 GLU D OE1 1 ATOM 7134 O OE2 . GLU D 2 132 ? 17.516 -66.378 -2.128 1.00 164.95 ? 132 GLU D OE2 1 ATOM 7135 N N . LEU D 2 133 ? 20.231 -70.973 -3.236 1.00 164.73 ? 133 LEU D N 1 ATOM 7136 C CA . LEU D 2 133 ? 20.736 -71.846 -2.168 1.00 164.39 ? 133 LEU D CA 1 ATOM 7137 C C . LEU D 2 133 ? 20.394 -71.312 -0.781 1.00 163.99 ? 133 LEU D C 1 ATOM 7138 O O . LEU D 2 133 ? 19.639 -71.943 -0.040 1.00 164.15 ? 133 LEU D O 1 ATOM 7139 C CB . LEU D 2 133 ? 22.253 -72.056 -2.292 1.00 164.19 ? 133 LEU D CB 1 ATOM 7140 C CG . LEU D 2 133 ? 22.717 -73.056 -3.356 1.00 164.55 ? 133 LEU D CG 1 ATOM 7141 C CD1 . LEU D 2 133 ? 24.238 -73.106 -3.405 1.00 164.39 ? 133 LEU D CD1 1 ATOM 7142 C CD2 . LEU D 2 133 ? 22.138 -74.443 -3.103 1.00 164.89 ? 133 LEU D CD2 1 ATOM 7143 N N . GLY D 2 134 ? 20.952 -70.154 -0.438 1.00 163.43 ? 134 GLY D N 1 ATOM 7144 C CA . GLY D 2 134 ? 20.740 -69.555 0.880 1.00 163.08 ? 134 GLY D CA 1 ATOM 7145 C C . GLY D 2 134 ? 21.939 -68.794 1.418 1.00 162.53 ? 134 GLY D C 1 ATOM 7146 O O . GLY D 2 134 ? 21.775 -67.798 2.122 1.00 162.25 ? 134 GLY D O 1 ATOM 7147 N N . ASN D 2 135 ? 23.143 -69.261 1.089 1.00 162.37 ? 135 ASN D N 1 ATOM 7148 C CA . ASN D 2 135 ? 24.381 -68.620 1.547 1.00 161.87 ? 135 ASN D CA 1 ATOM 7149 C C . ASN D 2 135 ? 24.944 -67.623 0.527 1.00 161.81 ? 135 ASN D C 1 ATOM 7150 O O . ASN D 2 135 ? 26.158 -67.446 0.424 1.00 161.55 ? 135 ASN D O 1 ATOM 7151 C CB . ASN D 2 135 ? 25.436 -69.680 1.903 1.00 161.82 ? 135 ASN D CB 1 ATOM 7152 C CG . ASN D 2 135 ? 25.851 -70.526 0.710 1.00 162.03 ? 135 ASN D CG 1 ATOM 7153 O OD1 . ASN D 2 135 ? 25.077 -70.723 -0.227 1.00 162.22 ? 135 ASN D OD1 1 ATOM 7154 N ND2 . ASN D 2 135 ? 27.077 -71.035 0.743 1.00 161.95 ? 135 ASN D ND2 1 ATOM 7155 N N . GLY D 2 136 ? 24.055 -66.966 -0.215 1.00 162.16 ? 136 GLY D N 1 ATOM 7156 C CA . GLY D 2 136 ? 24.454 -65.987 -1.220 1.00 162.42 ? 136 GLY D CA 1 ATOM 7157 C C . GLY D 2 136 ? 24.997 -66.623 -2.486 1.00 163.11 ? 136 GLY D C 1 ATOM 7158 O O . GLY D 2 136 ? 26.000 -66.163 -3.031 1.00 163.10 ? 136 GLY D O 1 ATOM 7159 N N . CYS D 2 137 ? 24.332 -67.679 -2.957 1.00 163.88 ? 137 CYS D N 1 ATOM 7160 C CA . CYS D 2 137 ? 24.749 -68.393 -4.167 1.00 164.49 ? 137 CYS D CA 1 ATOM 7161 C C . CYS D 2 137 ? 23.550 -68.844 -5.003 1.00 164.87 ? 137 CYS D C 1 ATOM 7162 O O . CYS D 2 137 ? 22.405 -68.794 -4.545 1.00 164.82 ? 137 CYS D O 1 ATOM 7163 C CB . CYS D 2 137 ? 25.607 -69.609 -3.801 1.00 164.84 ? 137 CYS D CB 1 ATOM 7164 S SG . CYS D 2 137 ? 27.180 -69.228 -2.990 1.00 164.83 ? 137 CYS D SG 1 ATOM 7165 N N . PHE D 2 138 ? 23.832 -69.277 -6.233 1.00 165.28 ? 138 PHE D N 1 ATOM 7166 C CA . PHE D 2 138 ? 22.813 -69.784 -7.159 1.00 165.71 ? 138 PHE D CA 1 ATOM 7167 C C . PHE D 2 138 ? 23.303 -71.043 -7.882 1.00 165.98 ? 138 PHE D C 1 ATOM 7168 O O . PHE D 2 138 ? 24.478 -71.137 -8.240 1.00 166.01 ? 138 PHE D O 1 ATOM 7169 C CB . PHE D 2 138 ? 22.455 -68.719 -8.202 1.00 165.91 ? 138 PHE D CB 1 ATOM 7170 C CG . PHE D 2 138 ? 21.844 -67.473 -7.622 1.00 165.71 ? 138 PHE D CG 1 ATOM 7171 C CD1 . PHE D 2 138 ? 20.486 -67.417 -7.337 1.00 165.85 ? 138 PHE D CD1 1 ATOM 7172 C CD2 . PHE D 2 138 ? 22.626 -66.352 -7.372 1.00 165.38 ? 138 PHE D CD2 1 ATOM 7173 C CE1 . PHE D 2 138 ? 19.920 -66.269 -6.809 1.00 165.74 ? 138 PHE D CE1 1 ATOM 7174 C CE2 . PHE D 2 138 ? 22.066 -65.202 -6.846 1.00 165.23 ? 138 PHE D CE2 1 ATOM 7175 C CZ . PHE D 2 138 ? 20.712 -65.160 -6.564 1.00 165.44 ? 138 PHE D CZ 1 ATOM 7176 N N . GLU D 2 139 ? 22.394 -71.996 -8.100 1.00 166.20 ? 139 GLU D N 1 ATOM 7177 C CA . GLU D 2 139 ? 22.698 -73.236 -8.827 1.00 166.45 ? 139 GLU D CA 1 ATOM 7178 C C . GLU D 2 139 ? 21.971 -73.280 -10.170 1.00 166.74 ? 139 GLU D C 1 ATOM 7179 O O . GLU D 2 139 ? 20.742 -73.348 -10.208 1.00 166.93 ? 139 GLU D O 1 ATOM 7180 C CB . GLU D 2 139 ? 22.298 -74.461 -7.998 1.00 166.56 ? 139 GLU D CB 1 ATOM 7181 C CG . GLU D 2 139 ? 23.384 -74.977 -7.070 1.00 166.42 ? 139 GLU D CG 1 ATOM 7182 C CD . GLU D 2 139 ? 22.996 -76.281 -6.399 1.00 166.62 ? 139 GLU D CD 1 ATOM 7183 O OE1 . GLU D 2 139 ? 21.943 -76.313 -5.725 1.00 166.68 ? 139 GLU D OE1 1 ATOM 7184 O OE2 . GLU D 2 139 ? 23.745 -77.272 -6.542 1.00 166.70 ? 139 GLU D OE2 1 ATOM 7185 N N . PHE D 2 140 ? 22.731 -73.256 -11.263 1.00 166.78 ? 140 PHE D N 1 ATOM 7186 C CA . PHE D 2 140 ? 22.157 -73.319 -12.610 1.00 167.12 ? 140 PHE D CA 1 ATOM 7187 C C . PHE D 2 140 ? 21.502 -74.675 -12.884 1.00 167.30 ? 140 PHE D C 1 ATOM 7188 O O . PHE D 2 140 ? 22.012 -75.715 -12.461 1.00 167.23 ? 140 PHE D O 1 ATOM 7189 C CB . PHE D 2 140 ? 23.233 -73.072 -13.675 1.00 167.38 ? 140 PHE D CB 1 ATOM 7190 C CG . PHE D 2 140 ? 23.716 -71.651 -13.744 1.00 167.22 ? 140 PHE D CG 1 ATOM 7191 C CD1 . PHE D 2 140 ? 23.063 -70.721 -14.545 1.00 167.44 ? 140 PHE D CD1 1 ATOM 7192 C CD2 . PHE D 2 140 ? 24.836 -71.247 -13.030 1.00 166.94 ? 140 PHE D CD2 1 ATOM 7193 C CE1 . PHE D 2 140 ? 23.509 -69.412 -14.621 1.00 167.34 ? 140 PHE D CE1 1 ATOM 7194 C CE2 . PHE D 2 140 ? 25.287 -69.939 -13.101 1.00 166.82 ? 140 PHE D CE2 1 ATOM 7195 C CZ . PHE D 2 140 ? 24.624 -69.020 -13.898 1.00 167.04 ? 140 PHE D CZ 1 ATOM 7196 N N . TYR D 2 141 ? 20.377 -74.649 -13.597 1.00 167.44 ? 141 TYR D N 1 ATOM 7197 C CA . TYR D 2 141 ? 19.711 -75.869 -14.064 1.00 167.67 ? 141 TYR D CA 1 ATOM 7198 C C . TYR D 2 141 ? 20.169 -76.257 -15.480 1.00 167.94 ? 141 TYR D C 1 ATOM 7199 O O . TYR D 2 141 ? 19.702 -77.252 -16.038 1.00 168.16 ? 141 TYR D O 1 ATOM 7200 C CB . TYR D 2 141 ? 18.186 -75.703 -14.018 1.00 167.85 ? 141 TYR D CB 1 ATOM 7201 C CG . TYR D 2 141 ? 17.596 -75.830 -12.629 1.00 167.65 ? 141 TYR D CG 1 ATOM 7202 C CD1 . TYR D 2 141 ? 17.424 -77.079 -12.039 1.00 167.82 ? 141 TYR D CD1 1 ATOM 7203 C CD2 . TYR D 2 141 ? 17.208 -74.705 -11.904 1.00 167.36 ? 141 TYR D CD2 1 ATOM 7204 C CE1 . TYR D 2 141 ? 16.884 -77.205 -10.770 1.00 167.66 ? 141 TYR D CE1 1 ATOM 7205 C CE2 . TYR D 2 141 ? 16.667 -74.821 -10.635 1.00 167.16 ? 141 TYR D CE2 1 ATOM 7206 C CZ . TYR D 2 141 ? 16.508 -76.074 -10.073 1.00 167.30 ? 141 TYR D CZ 1 ATOM 7207 O OH . TYR D 2 141 ? 15.972 -76.203 -8.814 1.00 167.16 ? 141 TYR D OH 1 ATOM 7208 N N . HIS D 2 142 ? 21.076 -75.463 -16.051 1.00 167.80 ? 142 HIS D N 1 ATOM 7209 C CA . HIS D 2 142 ? 21.705 -75.767 -17.337 1.00 168.08 ? 142 HIS D CA 1 ATOM 7210 C C . HIS D 2 142 ? 23.204 -75.468 -17.261 1.00 167.96 ? 142 HIS D C 1 ATOM 7211 O O . HIS D 2 142 ? 23.699 -74.996 -16.238 1.00 167.46 ? 142 HIS D O 1 ATOM 7212 C CB . HIS D 2 142 ? 21.054 -74.951 -18.458 1.00 168.31 ? 142 HIS D CB 1 ATOM 7213 C CG . HIS D 2 142 ? 21.303 -73.478 -18.359 1.00 168.03 ? 142 HIS D CG 1 ATOM 7214 N ND1 . HIS D 2 142 ? 20.654 -72.674 -17.448 1.00 167.65 ? 142 HIS D ND1 1 ATOM 7215 C CD2 . HIS D 2 142 ? 22.128 -72.664 -19.058 1.00 168.08 ? 142 HIS D CD2 1 ATOM 7216 C CE1 . HIS D 2 142 ? 21.070 -71.428 -17.588 1.00 167.54 ? 142 HIS D CE1 1 ATOM 7217 N NE2 . HIS D 2 142 ? 21.965 -71.395 -18.559 1.00 167.82 ? 142 HIS D NE2 1 ATOM 7218 N N . ARG D 2 143 ? 23.921 -75.746 -18.345 1.00 168.43 ? 143 ARG D N 1 ATOM 7219 C CA . ARG D 2 143 ? 25.365 -75.523 -18.388 1.00 168.42 ? 143 ARG D CA 1 ATOM 7220 C C . ARG D 2 143 ? 25.665 -74.063 -18.724 1.00 168.34 ? 143 ARG D C 1 ATOM 7221 O O . ARG D 2 143 ? 25.223 -73.556 -19.756 1.00 168.64 ? 143 ARG D O 1 ATOM 7222 C CB . ARG D 2 143 ? 26.025 -76.457 -19.412 1.00 168.93 ? 143 ARG D CB 1 ATOM 7223 C CG . ARG D 2 143 ? 25.705 -77.937 -19.221 1.00 169.07 ? 143 ARG D CG 1 ATOM 7224 C CD . ARG D 2 143 ? 26.008 -78.423 -17.809 1.00 168.74 ? 143 ARG D CD 1 ATOM 7225 N NE . ARG D 2 143 ? 27.402 -78.184 -17.435 1.00 168.76 ? 143 ARG D NE 1 ATOM 7226 C CZ . ARG D 2 143 ? 27.872 -78.164 -16.186 1.00 168.56 ? 143 ARG D CZ 1 ATOM 7227 N NH1 . ARG D 2 143 ? 27.071 -78.361 -15.140 1.00 168.24 ? 143 ARG D NH1 1 ATOM 7228 N NH2 . ARG D 2 143 ? 29.166 -77.935 -15.979 1.00 168.63 ? 143 ARG D NH2 1 ATOM 7229 N N . CYS D 2 144 ? 26.411 -73.395 -17.845 1.00 167.96 ? 144 CYS D N 1 ATOM 7230 C CA . CYS D 2 144 ? 26.772 -71.989 -18.032 1.00 167.94 ? 144 CYS D CA 1 ATOM 7231 C C . CYS D 2 144 ? 28.292 -71.815 -18.071 1.00 167.97 ? 144 CYS D C 1 ATOM 7232 O O . CYS D 2 144 ? 28.947 -71.705 -17.032 1.00 167.43 ? 144 CYS D O 1 ATOM 7233 C CB . CYS D 2 144 ? 26.162 -71.130 -16.921 1.00 167.46 ? 144 CYS D CB 1 ATOM 7234 S SG . CYS D 2 144 ? 26.487 -69.357 -17.077 1.00 167.44 ? 144 CYS D SG 1 ATOM 7235 N N . ASP D 2 145 ? 28.840 -71.791 -19.285 1.00 168.57 ? 145 ASP D N 1 ATOM 7236 C CA . ASP D 2 145 ? 30.282 -71.625 -19.501 1.00 168.76 ? 145 ASP D CA 1 ATOM 7237 C C . ASP D 2 145 ? 30.746 -70.198 -19.158 1.00 168.43 ? 145 ASP D C 1 ATOM 7238 O O . ASP D 2 145 ? 29.957 -69.388 -18.670 1.00 167.99 ? 145 ASP D O 1 ATOM 7239 C CB . ASP D 2 145 ? 30.650 -71.998 -20.948 1.00 169.52 ? 145 ASP D CB 1 ATOM 7240 C CG . ASP D 2 145 ? 29.951 -71.128 -21.977 1.00 169.96 ? 145 ASP D CG 1 ATOM 7241 O OD1 . ASP D 2 145 ? 28.734 -70.892 -21.825 1.00 169.81 ? 145 ASP D OD1 1 ATOM 7242 O OD2 . ASP D 2 145 ? 30.617 -70.692 -22.941 1.00 170.51 ? 145 ASP D OD2 1 ATOM 7243 N N . ASN D 2 146 ? 32.023 -69.902 -19.402 1.00 168.58 ? 146 ASN D N 1 ATOM 7244 C CA . ASN D 2 146 ? 32.601 -68.595 -19.061 1.00 168.36 ? 146 ASN D CA 1 ATOM 7245 C C . ASN D 2 146 ? 31.954 -67.414 -19.791 1.00 168.55 ? 146 ASN D C 1 ATOM 7246 O O . ASN D 2 146 ? 31.771 -66.350 -19.198 1.00 168.21 ? 146 ASN D O 1 ATOM 7247 C CB . ASN D 2 146 ? 34.118 -68.589 -19.305 1.00 168.61 ? 146 ASN D CB 1 ATOM 7248 C CG . ASN D 2 146 ? 34.882 -69.437 -18.300 1.00 168.28 ? 146 ASN D CG 1 ATOM 7249 O OD1 . ASN D 2 146 ? 34.302 -70.024 -17.385 1.00 167.92 ? 146 ASN D OD1 1 ATOM 7250 N ND2 . ASN D 2 146 ? 36.196 -69.511 -18.474 1.00 168.56 ? 146 ASN D ND2 1 ATOM 7251 N N . GLU D 2 147 ? 31.612 -67.598 -21.065 1.00 169.08 ? 147 GLU D N 1 ATOM 7252 C CA . GLU D 2 147 ? 30.911 -66.559 -21.828 1.00 169.34 ? 147 GLU D CA 1 ATOM 7253 C C . GLU D 2 147 ? 29.486 -66.350 -21.306 1.00 168.97 ? 147 GLU D C 1 ATOM 7254 O O . GLU D 2 147 ? 28.989 -65.224 -21.290 1.00 168.95 ? 147 GLU D O 1 ATOM 7255 C CB . GLU D 2 147 ? 30.889 -66.893 -23.323 1.00 170.17 ? 147 GLU D CB 1 ATOM 7256 C CG . GLU D 2 147 ? 32.223 -66.682 -24.025 1.00 170.63 ? 147 GLU D CG 1 ATOM 7257 C CD . GLU D 2 147 ? 32.140 -66.907 -25.523 1.00 171.41 ? 147 GLU D CD 1 ATOM 7258 O OE1 . GLU D 2 147 ? 31.527 -67.909 -25.945 1.00 171.58 ? 147 GLU D OE1 1 ATOM 7259 O OE2 . GLU D 2 147 ? 32.685 -66.077 -26.281 1.00 171.86 ? 147 GLU D OE2 1 ATOM 7260 N N . CYS D 2 148 ? 28.839 -67.436 -20.886 1.00 168.78 ? 148 CYS D N 1 ATOM 7261 C CA . CYS D 2 148 ? 27.542 -67.357 -20.204 1.00 168.47 ? 148 CYS D CA 1 ATOM 7262 C C . CYS D 2 148 ? 27.675 -66.666 -18.847 1.00 167.80 ? 148 CYS D C 1 ATOM 7263 O O . CYS D 2 148 ? 26.806 -65.888 -18.448 1.00 167.48 ? 148 CYS D O 1 ATOM 7264 C CB . CYS D 2 148 ? 26.941 -68.756 -20.014 1.00 168.51 ? 148 CYS D CB 1 ATOM 7265 S SG . CYS D 2 148 ? 25.580 -68.844 -18.822 1.00 168.02 ? 148 CYS D SG 1 ATOM 7266 N N . MET D 2 149 ? 28.765 -66.961 -18.142 1.00 167.53 ? 149 MET D N 1 ATOM 7267 C CA . MET D 2 149 ? 29.021 -66.372 -16.828 1.00 166.89 ? 149 MET D CA 1 ATOM 7268 C C . MET D 2 149 ? 29.313 -64.877 -16.964 1.00 166.72 ? 149 MET D C 1 ATOM 7269 O O . MET D 2 149 ? 28.894 -64.079 -16.124 1.00 166.18 ? 149 MET D O 1 ATOM 7270 C CB . MET D 2 149 ? 30.192 -67.080 -16.136 1.00 166.89 ? 149 MET D CB 1 ATOM 7271 C CG . MET D 2 149 ? 30.036 -67.201 -14.630 1.00 166.34 ? 149 MET D CG 1 ATOM 7272 S SD . MET D 2 149 ? 28.885 -68.507 -14.151 1.00 166.26 ? 149 MET D SD 1 ATOM 7273 C CE . MET D 2 149 ? 29.857 -69.978 -14.468 1.00 166.55 ? 149 MET D CE 1 ATOM 7274 N N . GLU D 2 150 ? 30.033 -64.510 -18.024 1.00 166.97 ? 150 GLU D N 1 ATOM 7275 C CA . GLU D 2 150 ? 30.250 -63.103 -18.371 1.00 166.90 ? 150 GLU D CA 1 ATOM 7276 C C . GLU D 2 150 ? 28.931 -62.394 -18.668 1.00 166.88 ? 150 GLU D C 1 ATOM 7277 O O . GLU D 2 150 ? 28.775 -61.226 -18.338 1.00 166.62 ? 150 GLU D O 1 ATOM 7278 C CB . GLU D 2 150 ? 31.179 -62.974 -19.583 1.00 167.51 ? 150 GLU D CB 1 ATOM 7279 C CG . GLU D 2 150 ? 32.656 -63.173 -19.271 1.00 167.40 ? 150 GLU D CG 1 ATOM 7280 C CD . GLU D 2 150 ? 33.531 -63.171 -20.515 1.00 168.07 ? 150 GLU D CD 1 ATOM 7281 O OE1 . GLU D 2 150 ? 33.068 -63.619 -21.588 1.00 168.48 ? 150 GLU D OE1 1 ATOM 7282 O OE2 . GLU D 2 150 ? 34.690 -62.716 -20.420 1.00 168.01 ? 150 GLU D OE2 1 ATOM 7283 N N . SER D 2 151 ? 27.994 -63.103 -19.295 1.00 167.12 ? 151 SER D N 1 ATOM 7284 C CA . SER D 2 151 ? 26.669 -62.554 -19.606 1.00 167.23 ? 151 SER D CA 1 ATOM 7285 C C . SER D 2 151 ? 25.841 -62.250 -18.356 1.00 166.57 ? 151 SER D C 1 ATOM 7286 O O . SER D 2 151 ? 24.999 -61.352 -18.374 1.00 166.54 ? 151 SER D O 1 ATOM 7287 C CB . SER D 2 151 ? 25.893 -63.514 -20.508 1.00 167.67 ? 151 SER D CB 1 ATOM 7288 O OG . SER D 2 151 ? 26.557 -63.687 -21.745 1.00 168.35 ? 151 SER D OG 1 ATOM 7289 N N . VAL D 2 152 ? 26.071 -63.009 -17.287 1.00 166.03 ? 152 VAL D N 1 ATOM 7290 C CA . VAL D 2 152 ? 25.444 -62.739 -15.992 1.00 165.51 ? 152 VAL D CA 1 ATOM 7291 C C . VAL D 2 152 ? 26.109 -61.518 -15.347 1.00 165.15 ? 152 VAL D C 1 ATOM 7292 O O . VAL D 2 152 ? 25.435 -60.675 -14.752 1.00 164.92 ? 152 VAL D O 1 ATOM 7293 C CB . VAL D 2 152 ? 25.534 -63.963 -15.051 1.00 165.15 ? 152 VAL D CB 1 ATOM 7294 C CG1 . VAL D 2 152 ? 25.003 -63.627 -13.660 1.00 164.61 ? 152 VAL D CG1 1 ATOM 7295 C CG2 . VAL D 2 152 ? 24.772 -65.142 -15.643 1.00 165.51 ? 152 VAL D CG2 1 ATOM 7296 N N . ARG D 2 153 ? 27.432 -61.438 -15.472 1.00 165.10 ? 153 ARG D N 1 ATOM 7297 C CA . ARG D 2 153 ? 28.205 -60.275 -15.021 1.00 164.78 ? 153 ARG D CA 1 ATOM 7298 C C . ARG D 2 153 ? 27.950 -59.033 -15.891 1.00 165.19 ? 153 ARG D C 1 ATOM 7299 O O . ARG D 2 153 ? 27.990 -57.907 -15.395 1.00 165.00 ? 153 ARG D O 1 ATOM 7300 C CB . ARG D 2 153 ? 29.706 -60.610 -15.011 1.00 164.71 ? 153 ARG D CB 1 ATOM 7301 C CG . ARG D 2 153 ? 30.178 -61.342 -13.759 1.00 164.11 ? 153 ARG D CG 1 ATOM 7302 C CD . ARG D 2 153 ? 31.085 -62.530 -14.059 1.00 164.31 ? 153 ARG D CD 1 ATOM 7303 N NE . ARG D 2 153 ? 32.259 -62.180 -14.858 1.00 164.67 ? 153 ARG D NE 1 ATOM 7304 C CZ . ARG D 2 153 ? 33.131 -63.063 -15.350 1.00 164.96 ? 153 ARG D CZ 1 ATOM 7305 N NH1 . ARG D 2 153 ? 32.978 -64.368 -15.134 1.00 164.92 ? 153 ARG D NH1 1 ATOM 7306 N NH2 . ARG D 2 153 ? 34.165 -62.638 -16.066 1.00 165.32 ? 153 ARG D NH2 1 ATOM 7307 N N . ASN D 2 154 ? 27.686 -59.252 -17.180 1.00 165.81 ? 154 ASN D N 1 ATOM 7308 C CA . ASN D 2 154 ? 27.512 -58.170 -18.156 1.00 166.30 ? 154 ASN D CA 1 ATOM 7309 C C . ASN D 2 154 ? 26.182 -57.435 -17.989 1.00 166.26 ? 154 ASN D C 1 ATOM 7310 O O . ASN D 2 154 ? 26.153 -56.207 -17.919 1.00 166.27 ? 154 ASN D O 1 ATOM 7311 C CB . ASN D 2 154 ? 27.627 -58.735 -19.584 1.00 167.06 ? 154 ASN D CB 1 ATOM 7312 C CG . ASN D 2 154 ? 27.604 -57.659 -20.658 1.00 167.70 ? 154 ASN D CG 1 ATOM 7313 O OD1 . ASN D 2 154 ? 28.118 -56.557 -20.467 1.00 167.63 ? 154 ASN D OD1 1 ATOM 7314 N ND2 . ASN D 2 154 ? 27.021 -57.987 -21.808 1.00 168.30 ? 154 ASN D ND2 1 ATOM 7315 N N . GLY D 2 155 ? 25.090 -58.194 -17.925 1.00 166.25 ? 155 GLY D N 1 ATOM 7316 C CA . GLY D 2 155 ? 23.743 -57.628 -17.833 1.00 166.39 ? 155 GLY D CA 1 ATOM 7317 C C . GLY D 2 155 ? 22.780 -58.287 -18.805 1.00 167.04 ? 155 GLY D C 1 ATOM 7318 O O . GLY D 2 155 ? 21.666 -58.654 -18.428 1.00 167.10 ? 155 GLY D O 1 ATOM 7319 N N . THR D 2 156 ? 23.212 -58.435 -20.058 1.00 167.61 ? 156 THR D N 1 ATOM 7320 C CA . THR D 2 156 ? 22.399 -59.067 -21.099 1.00 168.15 ? 156 THR D CA 1 ATOM 7321 C C . THR D 2 156 ? 22.399 -60.585 -20.932 1.00 167.95 ? 156 THR D C 1 ATOM 7322 O O . THR D 2 156 ? 23.457 -61.213 -20.962 1.00 167.83 ? 156 THR D O 1 ATOM 7323 C CB . THR D 2 156 ? 22.923 -58.724 -22.506 1.00 168.84 ? 156 THR D CB 1 ATOM 7324 N N . TYR D 2 157 ? 21.212 -61.165 -20.765 1.00 167.96 ? 157 TYR D N 1 ATOM 7325 C CA . TYR D 2 157 ? 21.073 -62.596 -20.486 1.00 167.76 ? 157 TYR D CA 1 ATOM 7326 C C . TYR D 2 157 ? 19.709 -63.114 -20.935 1.00 168.17 ? 157 TYR D C 1 ATOM 7327 O O . TYR D 2 157 ? 19.615 -63.947 -21.836 1.00 168.46 ? 157 TYR D O 1 ATOM 7328 C CB . TYR D 2 157 ? 21.271 -62.849 -18.988 1.00 167.00 ? 157 TYR D CB 1 ATOM 7329 C CG . TYR D 2 157 ? 21.027 -64.274 -18.535 1.00 166.72 ? 157 TYR D CG 1 ATOM 7330 C CD1 . TYR D 2 157 ? 22.059 -65.208 -18.520 1.00 166.52 ? 157 TYR D CD1 1 ATOM 7331 C CD2 . TYR D 2 157 ? 19.768 -64.680 -18.103 1.00 166.64 ? 157 TYR D CD2 1 ATOM 7332 C CE1 . TYR D 2 157 ? 21.841 -66.510 -18.098 1.00 166.33 ? 157 TYR D CE1 1 ATOM 7333 C CE2 . TYR D 2 157 ? 19.539 -65.978 -17.681 1.00 166.45 ? 157 TYR D CE2 1 ATOM 7334 C CZ . TYR D 2 157 ? 20.579 -66.889 -17.680 1.00 166.30 ? 157 TYR D CZ 1 ATOM 7335 O OH . TYR D 2 157 ? 20.350 -68.179 -17.261 1.00 166.14 ? 157 TYR D OH 1 ATOM 7336 N N . PRO E 1 1 ? 0.120 -80.701 10.040 1.00 102.89 ? 0 PRO E N 1 ATOM 7337 C CA . PRO E 1 1 ? 1.167 -80.089 9.230 1.00 101.29 ? 0 PRO E CA 1 ATOM 7338 C C . PRO E 1 1 ? 2.053 -79.131 10.042 1.00 99.63 ? 0 PRO E C 1 ATOM 7339 O O . PRO E 1 1 ? 1.594 -78.069 10.467 1.00 98.90 ? 0 PRO E O 1 ATOM 7340 C CB . PRO E 1 1 ? 0.370 -79.351 8.150 1.00 101.17 ? 0 PRO E CB 1 ATOM 7341 C CG . PRO E 1 1 ? -0.905 -80.129 8.015 1.00 103.03 ? 0 PRO E CG 1 ATOM 7342 C CD . PRO E 1 1 ? -1.084 -80.987 9.241 1.00 104.13 ? 0 PRO E CD 1 ATOM 7343 N N . ASP E 1 2 ? 3.314 -79.517 10.241 1.00 99.39 ? 1 ASP E N 1 ATOM 7344 C CA . ASP E 1 2 ? 4.224 -78.820 11.165 1.00 98.33 ? 1 ASP E CA 1 ATOM 7345 C C . ASP E 1 2 ? 4.684 -77.461 10.648 1.00 96.74 ? 1 ASP E C 1 ATOM 7346 O O . ASP E 1 2 ? 4.857 -77.268 9.442 1.00 96.87 ? 1 ASP E O 1 ATOM 7347 C CB . ASP E 1 2 ? 5.447 -79.690 11.471 1.00 99.04 ? 1 ASP E CB 1 ATOM 7348 C CG . ASP E 1 2 ? 5.096 -80.928 12.274 1.00 100.97 ? 1 ASP E CG 1 ATOM 7349 O OD1 . ASP E 1 2 ? 4.511 -80.783 13.368 1.00 101.51 ? 1 ASP E OD1 1 ATOM 7350 O OD2 . ASP E 1 2 ? 5.410 -82.044 11.816 1.00 102.19 ? 1 ASP E OD2 1 ATOM 7351 N N . GLN E 1 3 ? 4.907 -76.535 11.576 1.00 95.38 ? 2 GLN E N 1 ATOM 7352 C CA . GLN E 1 3 ? 5.105 -75.131 11.229 1.00 93.90 ? 2 GLN E CA 1 ATOM 7353 C C . GLN E 1 3 ? 5.943 -74.377 12.267 1.00 92.53 ? 2 GLN E C 1 ATOM 7354 O O . GLN E 1 3 ? 5.924 -74.712 13.450 1.00 92.77 ? 2 GLN E O 1 ATOM 7355 C CB . GLN E 1 3 ? 3.735 -74.465 11.090 1.00 93.94 ? 2 GLN E CB 1 ATOM 7356 C CG . GLN E 1 3 ? 3.758 -73.084 10.461 1.00 92.93 ? 2 GLN E CG 1 ATOM 7357 C CD . GLN E 1 3 ? 2.371 -72.486 10.330 1.00 93.47 ? 2 GLN E CD 1 ATOM 7358 O OE1 . GLN E 1 3 ? 2.126 -71.365 10.779 1.00 92.61 ? 2 GLN E OE1 1 ATOM 7359 N NE2 . GLN E 1 3 ? 1.453 -73.234 9.717 1.00 94.68 ? 2 GLN E NE2 1 ATOM 7360 N N . ILE E 1 4 ? 6.684 -73.370 11.805 1.00 91.47 ? 3 ILE E N 1 ATOM 7361 C CA . ILE E 1 4 ? 7.381 -72.418 12.689 1.00 90.34 ? 3 ILE E CA 1 ATOM 7362 C C . ILE E 1 4 ? 7.317 -71.016 12.065 1.00 89.42 ? 3 ILE E C 1 ATOM 7363 O O . ILE E 1 4 ? 7.493 -70.875 10.851 1.00 89.71 ? 3 ILE E O 1 ATOM 7364 C CB . ILE E 1 4 ? 8.848 -72.848 12.963 1.00 90.46 ? 3 ILE E CB 1 ATOM 7365 C CG1 . ILE E 1 4 ? 9.447 -72.034 14.118 1.00 89.55 ? 3 ILE E CG1 1 ATOM 7366 C CG2 . ILE E 1 4 ? 9.710 -72.736 11.708 1.00 90.50 ? 3 ILE E CG2 1 ATOM 7367 C CD1 . ILE E 1 4 ? 10.786 -72.552 14.603 1.00 90.28 ? 3 ILE E CD1 1 ATOM 7368 N N . CYS E 1 5 ? 7.047 -69.996 12.888 1.00 88.85 ? 4 CYS E N 1 ATOM 7369 C CA . CYS E 1 5 ? 6.870 -68.613 12.411 1.00 87.91 ? 4 CYS E CA 1 ATOM 7370 C C . CYS E 1 5 ? 7.779 -67.627 13.139 1.00 86.49 ? 4 CYS E C 1 ATOM 7371 O O . CYS E 1 5 ? 8.249 -67.897 14.244 1.00 86.08 ? 4 CYS E O 1 ATOM 7372 C CB . CYS E 1 5 ? 5.418 -68.147 12.591 1.00 88.59 ? 4 CYS E CB 1 ATOM 7373 S SG . CYS E 1 5 ? 4.143 -69.253 11.943 1.00 91.21 ? 4 CYS E SG 1 ATOM 7374 N N . ILE E 1 6 ? 8.004 -66.476 12.508 1.00 85.67 ? 5 ILE E N 1 ATOM 7375 C CA . ILE E 1 6 ? 8.754 -65.375 13.110 1.00 84.51 ? 5 ILE E CA 1 ATOM 7376 C C . ILE E 1 6 ? 7.796 -64.261 13.512 1.00 83.34 ? 5 ILE E C 1 ATOM 7377 O O . ILE E 1 6 ? 6.974 -63.814 12.708 1.00 83.56 ? 5 ILE E O 1 ATOM 7378 C CB . ILE E 1 6 ? 9.820 -64.824 12.137 1.00 84.87 ? 5 ILE E CB 1 ATOM 7379 C CG1 . ILE E 1 6 ? 10.864 -65.908 11.834 1.00 86.23 ? 5 ILE E CG1 1 ATOM 7380 C CG2 . ILE E 1 6 ? 10.485 -63.570 12.694 1.00 83.56 ? 5 ILE E CG2 1 ATOM 7381 C CD1 . ILE E 1 6 ? 11.588 -66.444 13.054 1.00 86.21 ? 5 ILE E CD1 1 ATOM 7382 N N . GLY E 1 7 ? 7.907 -63.829 14.765 1.00 82.21 ? 6 GLY E N 1 ATOM 7383 C CA . GLY E 1 7 ? 7.076 -62.754 15.300 1.00 81.68 ? 6 GLY E CA 1 ATOM 7384 C C . GLY E 1 7 ? 7.838 -61.922 16.309 1.00 80.45 ? 6 GLY E C 1 ATOM 7385 O O . GLY E 1 7 ? 9.040 -62.114 16.500 1.00 79.67 ? 6 GLY E O 1 ATOM 7386 N N . TYR E 1 8 ? 7.133 -61.000 16.960 1.00 80.29 ? 7 TYR E N 1 ATOM 7387 C CA . TYR E 1 8 ? 7.768 -60.059 17.876 1.00 79.26 ? 7 TYR E CA 1 ATOM 7388 C C . TYR E 1 8 ? 6.871 -59.670 19.054 1.00 79.70 ? 7 TYR E C 1 ATOM 7389 O O . TYR E 1 8 ? 5.675 -59.965 19.068 1.00 81.08 ? 7 TYR E O 1 ATOM 7390 C CB . TYR E 1 8 ? 8.241 -58.813 17.109 1.00 78.29 ? 7 TYR E CB 1 ATOM 7391 C CG . TYR E 1 8 ? 7.160 -58.078 16.334 1.00 78.94 ? 7 TYR E CG 1 ATOM 7392 C CD1 . TYR E 1 8 ? 6.725 -58.543 15.095 1.00 80.00 ? 7 TYR E CD1 1 ATOM 7393 C CD2 . TYR E 1 8 ? 6.593 -56.902 16.829 1.00 78.68 ? 7 TYR E CD2 1 ATOM 7394 C CE1 . TYR E 1 8 ? 5.745 -57.870 14.378 1.00 81.04 ? 7 TYR E CE1 1 ATOM 7395 C CE2 . TYR E 1 8 ? 5.614 -56.220 16.117 1.00 79.66 ? 7 TYR E CE2 1 ATOM 7396 C CZ . TYR E 1 8 ? 5.191 -56.711 14.890 1.00 81.03 ? 7 TYR E CZ 1 ATOM 7397 O OH . TYR E 1 8 ? 4.217 -56.043 14.176 1.00 82.32 ? 7 TYR E OH 1 ATOM 7398 N N . HIS E 1 9 ? 7.478 -59.013 20.039 1.00 78.93 ? 8 HIS E N 1 ATOM 7399 C CA . HIS E 1 9 ? 6.803 -58.611 21.272 1.00 79.47 ? 8 HIS E CA 1 ATOM 7400 C C . HIS E 1 9 ? 5.719 -57.557 21.015 1.00 79.85 ? 8 HIS E C 1 ATOM 7401 O O . HIS E 1 9 ? 5.941 -56.573 20.300 1.00 78.23 ? 8 HIS E O 1 ATOM 7402 C CB . HIS E 1 9 ? 7.842 -58.086 22.282 1.00 78.28 ? 8 HIS E CB 1 ATOM 7403 C CG . HIS E 1 9 ? 7.307 -57.866 23.667 1.00 79.02 ? 8 HIS E CG 1 ATOM 7404 N ND1 . HIS E 1 9 ? 6.810 -58.888 24.449 1.00 80.65 ? 8 HIS E ND1 1 ATOM 7405 C CD2 . HIS E 1 9 ? 7.227 -56.743 24.423 1.00 78.30 ? 8 HIS E CD2 1 ATOM 7406 C CE1 . HIS E 1 9 ? 6.425 -58.401 25.616 1.00 81.26 ? 8 HIS E CE1 1 ATOM 7407 N NE2 . HIS E 1 9 ? 6.667 -57.102 25.627 1.00 79.72 ? 8 HIS E NE2 1 ATOM 7408 N N . ALA E 1 10 ? 4.539 -57.805 21.583 1.00 81.72 ? 9 ALA E N 1 ATOM 7409 C CA . ALA E 1 10 ? 3.463 -56.820 21.651 1.00 82.89 ? 9 ALA E CA 1 ATOM 7410 C C . ALA E 1 10 ? 2.910 -56.803 23.077 1.00 84.52 ? 9 ALA E C 1 ATOM 7411 O O . ALA E 1 10 ? 3.101 -57.762 23.826 1.00 85.47 ? 9 ALA E O 1 ATOM 7412 C CB . ALA E 1 10 ? 2.368 -57.159 20.651 1.00 84.22 ? 9 ALA E CB 1 ATOM 7413 N N . ASN E 1 11 ? 2.245 -55.710 23.452 1.00 85.52 ? 10 ASN E N 1 ATOM 7414 C CA . ASN E 1 11 ? 1.602 -55.597 24.770 1.00 87.47 ? 10 ASN E CA 1 ATOM 7415 C C . ASN E 1 11 ? 0.539 -54.479 24.810 1.00 88.90 ? 10 ASN E C 1 ATOM 7416 O O . ASN E 1 11 ? 0.013 -54.096 23.763 1.00 89.34 ? 10 ASN E O 1 ATOM 7417 C CB . ASN E 1 11 ? 2.659 -55.443 25.879 1.00 86.40 ? 10 ASN E CB 1 ATOM 7418 C CG . ASN E 1 11 ? 3.359 -54.091 25.861 1.00 84.71 ? 10 ASN E CG 1 ATOM 7419 O OD1 . ASN E 1 11 ? 2.838 -53.101 25.343 1.00 84.98 ? 10 ASN E OD1 1 ATOM 7420 N ND2 . ASN E 1 11 ? 4.552 -54.044 26.444 1.00 83.27 ? 10 ASN E ND2 1 ATOM 7421 N N . ASN E 1 12 ? 0.210 -53.979 26.003 1.00 90.26 ? 11 ASN E N 1 ATOM 7422 C CA . ASN E 1 12 ? -0.808 -52.933 26.154 1.00 92.40 ? 11 ASN E CA 1 ATOM 7423 C C . ASN E 1 12 ? -0.220 -51.596 26.608 1.00 91.05 ? 11 ASN E C 1 ATOM 7424 O O . ASN E 1 12 ? -0.907 -50.787 27.232 1.00 92.63 ? 11 ASN E O 1 ATOM 7425 C CB . ASN E 1 12 ? -1.916 -53.399 27.112 1.00 95.81 ? 11 ASN E CB 1 ATOM 7426 C CG . ASN E 1 12 ? -2.718 -54.578 26.558 1.00 98.53 ? 11 ASN E CG 1 ATOM 7427 O OD1 . ASN E 1 12 ? -2.737 -54.824 25.348 1.00 97.91 ? 11 ASN E OD1 1 ATOM 7428 N ND2 . ASN E 1 12 ? -3.386 -55.312 27.445 1.00 101.40 ? 11 ASN E ND2 1 ATOM 7429 N N . SER E 1 13 ? 1.049 -51.363 26.283 1.00 88.63 ? 12 SER E N 1 ATOM 7430 C CA . SER E 1 13 ? 1.665 -50.068 26.520 1.00 87.72 ? 12 SER E CA 1 ATOM 7431 C C . SER E 1 13 ? 1.092 -49.076 25.521 1.00 88.98 ? 12 SER E C 1 ATOM 7432 O O . SER E 1 13 ? 1.274 -49.232 24.312 1.00 88.63 ? 12 SER E O 1 ATOM 7433 C CB . SER E 1 13 ? 3.186 -50.137 26.365 1.00 85.01 ? 12 SER E CB 1 ATOM 7434 O OG . SER E 1 13 ? 3.773 -48.848 26.480 1.00 82.85 ? 12 SER E OG 1 ATOM 7435 N N . THR E 1 14 ? 0.385 -48.070 26.031 1.00 90.98 ? 13 THR E N 1 ATOM 7436 C CA . THR E 1 14 ? -0.164 -47.002 25.199 1.00 92.18 ? 13 THR E CA 1 ATOM 7437 C C . THR E 1 14 ? 0.868 -45.902 24.948 1.00 89.93 ? 13 THR E C 1 ATOM 7438 O O . THR E 1 14 ? 0.687 -45.079 24.051 1.00 90.82 ? 13 THR E O 1 ATOM 7439 C CB . THR E 1 14 ? -1.409 -46.367 25.849 1.00 95.02 ? 13 THR E CB 1 ATOM 7440 O OG1 . THR E 1 14 ? -1.083 -45.895 27.163 1.00 94.35 ? 13 THR E OG1 1 ATOM 7441 C CG2 . THR E 1 14 ? -2.535 -47.379 25.940 1.00 98.02 ? 13 THR E CG2 1 ATOM 7442 N N . GLU E 1 15 ? 1.942 -45.901 25.738 1.00 87.56 ? 14 GLU E N 1 ATOM 7443 C CA . GLU E 1 15 ? 2.973 -44.855 25.687 1.00 85.17 ? 14 GLU E CA 1 ATOM 7444 C C . GLU E 1 15 ? 3.474 -44.525 24.277 1.00 83.98 ? 14 GLU E C 1 ATOM 7445 O O . GLU E 1 15 ? 3.785 -45.420 23.488 1.00 83.54 ? 14 GLU E O 1 ATOM 7446 C CB . GLU E 1 15 ? 4.152 -45.231 26.591 1.00 83.59 ? 14 GLU E CB 1 ATOM 7447 C CG . GLU E 1 15 ? 3.947 -44.825 28.046 1.00 84.51 ? 14 GLU E CG 1 ATOM 7448 C CD . GLU E 1 15 ? 4.983 -45.428 28.974 1.00 83.65 ? 14 GLU E CD 1 ATOM 7449 O OE1 . GLU E 1 15 ? 5.037 -46.676 29.070 1.00 84.98 ? 14 GLU E OE1 1 ATOM 7450 O OE2 . GLU E 1 15 ? 5.740 -44.659 29.606 1.00 82.08 ? 14 GLU E OE2 1 ATOM 7451 N N . GLN E 1 16 ? 3.558 -43.224 23.990 1.00 83.61 ? 15 GLN E N 1 ATOM 7452 C CA . GLN E 1 16 ? 3.832 -42.719 22.646 1.00 83.38 ? 15 GLN E CA 1 ATOM 7453 C C . GLN E 1 16 ? 5.167 -41.984 22.540 1.00 80.74 ? 15 GLN E C 1 ATOM 7454 O O . GLN E 1 16 ? 5.652 -41.401 23.510 1.00 79.49 ? 15 GLN E O 1 ATOM 7455 C CB . GLN E 1 16 ? 2.716 -41.767 22.209 1.00 85.83 ? 15 GLN E CB 1 ATOM 7456 C CG . GLN E 1 16 ? 1.368 -42.439 22.002 1.00 88.60 ? 15 GLN E CG 1 ATOM 7457 C CD . GLN E 1 16 ? 0.277 -41.460 21.610 1.00 91.42 ? 15 GLN E CD 1 ATOM 7458 O OE1 . GLN E 1 16 ? 0.390 -40.251 21.846 1.00 90.93 ? 15 GLN E OE1 1 ATOM 7459 N NE2 . GLN E 1 16 ? -0.792 -41.978 21.011 1.00 94.15 ? 15 GLN E NE2 1 ATOM 7460 N N . VAL E 1 17 ? 5.746 -42.024 21.342 1.00 80.19 ? 16 VAL E N 1 ATOM 7461 C CA . VAL E 1 17 ? 6.936 -41.246 21.002 1.00 78.32 ? 16 VAL E CA 1 ATOM 7462 C C . VAL E 1 17 ? 6.758 -40.640 19.615 1.00 79.55 ? 16 VAL E C 1 ATOM 7463 O O . VAL E 1 17 ? 5.909 -41.083 18.833 1.00 80.72 ? 16 VAL E O 1 ATOM 7464 C CB . VAL E 1 17 ? 8.228 -42.101 21.014 1.00 76.76 ? 16 VAL E CB 1 ATOM 7465 C CG1 . VAL E 1 17 ? 8.452 -42.721 22.384 1.00 75.64 ? 16 VAL E CG1 1 ATOM 7466 C CG2 . VAL E 1 17 ? 8.192 -43.178 19.933 1.00 77.84 ? 16 VAL E CG2 1 ATOM 7467 N N . ASP E 1 18 ? 7.564 -39.627 19.319 1.00 78.79 ? 17 ASP E N 1 ATOM 7468 C CA . ASP E 1 18 ? 7.554 -38.984 18.012 1.00 80.41 ? 17 ASP E CA 1 ATOM 7469 C C . ASP E 1 18 ? 8.797 -39.360 17.225 1.00 79.89 ? 17 ASP E C 1 ATOM 7470 O O . ASP E 1 18 ? 9.782 -39.857 17.774 1.00 77.54 ? 17 ASP E O 1 ATOM 7471 C CB . ASP E 1 18 ? 7.469 -37.465 18.159 1.00 80.81 ? 17 ASP E CB 1 ATOM 7472 C CG . ASP E 1 18 ? 6.159 -37.008 18.770 1.00 82.12 ? 17 ASP E CG 1 ATOM 7473 O OD1 . ASP E 1 18 ? 5.239 -37.842 18.919 1.00 82.94 ? 17 ASP E OD1 1 ATOM 7474 O OD2 . ASP E 1 18 ? 6.049 -35.807 19.101 1.00 82.35 ? 17 ASP E OD2 1 ATOM 7475 N N . THR E 1 19 ? 8.719 -39.129 15.923 1.00 82.42 ? 18 THR E N 1 ATOM 7476 C CA . THR E 1 19 ? 9.832 -39.345 15.014 1.00 83.31 ? 18 THR E CA 1 ATOM 7477 C C . THR E 1 19 ? 9.777 -38.224 13.983 1.00 86.17 ? 18 THR E C 1 ATOM 7478 O O . THR E 1 19 ? 8.951 -37.314 14.099 1.00 86.75 ? 18 THR E O 1 ATOM 7479 C CB . THR E 1 19 ? 9.760 -40.745 14.348 1.00 84.08 ? 18 THR E CB 1 ATOM 7480 O OG1 . THR E 1 19 ? 10.936 -40.977 13.570 1.00 84.82 ? 18 THR E OG1 1 ATOM 7481 C CG2 . THR E 1 19 ? 8.560 -40.880 13.445 1.00 86.55 ? 18 THR E CG2 1 ATOM 7482 N N . ILE E 1 20 ? 10.643 -38.288 12.979 1.00 88.36 ? 19 ILE E N 1 ATOM 7483 C CA . ILE E 1 20 ? 10.698 -37.249 11.952 1.00 92.11 ? 19 ILE E CA 1 ATOM 7484 C C . ILE E 1 20 ? 9.352 -37.100 11.232 1.00 94.99 ? 19 ILE E C 1 ATOM 7485 O O . ILE E 1 20 ? 8.788 -36.003 11.191 1.00 96.30 ? 19 ILE E O 1 ATOM 7486 C CB . ILE E 1 20 ? 11.815 -37.525 10.919 1.00 94.26 ? 19 ILE E CB 1 ATOM 7487 C CG1 . ILE E 1 20 ? 13.189 -37.512 11.602 1.00 92.77 ? 19 ILE E CG1 1 ATOM 7488 C CG2 . ILE E 1 20 ? 11.784 -36.488 9.799 1.00 97.87 ? 19 ILE E CG2 1 ATOM 7489 C CD1 . ILE E 1 20 ? 14.314 -38.045 10.737 1.00 94.44 ? 19 ILE E CD1 1 ATOM 7490 N N . MET E 1 21 ? 8.836 -38.206 10.691 1.00 95.92 ? 20 MET E N 1 ATOM 7491 C CA . MET E 1 21 ? 7.633 -38.165 9.847 1.00 99.06 ? 20 MET E CA 1 ATOM 7492 C C . MET E 1 21 ? 6.369 -38.745 10.500 1.00 98.33 ? 20 MET E C 1 ATOM 7493 O O . MET E 1 21 ? 5.328 -38.832 9.847 1.00 101.05 ? 20 MET E O 1 ATOM 7494 C CB . MET E 1 21 ? 7.904 -38.841 8.488 1.00 101.64 ? 20 MET E CB 1 ATOM 7495 C CG . MET E 1 21 ? 8.538 -40.224 8.553 1.00 100.09 ? 20 MET E CG 1 ATOM 7496 S SD . MET E 1 21 ? 8.508 -41.104 6.970 1.00 103.35 ? 20 MET E SD 1 ATOM 7497 C CE . MET E 1 21 ? 6.871 -41.834 6.997 1.00 104.10 ? 20 MET E CE 1 ATOM 7498 N N . GLU E 1 22 ? 6.443 -39.104 11.783 1.00 94.99 ? 21 GLU E N 1 ATOM 7499 C CA . GLU E 1 22 ? 5.300 -39.704 12.494 1.00 94.82 ? 21 GLU E CA 1 ATOM 7500 C C . GLU E 1 22 ? 5.182 -39.177 13.931 1.00 92.22 ? 21 GLU E C 1 ATOM 7501 O O . GLU E 1 22 ? 6.021 -39.483 14.774 1.00 89.30 ? 21 GLU E O 1 ATOM 7502 C CB . GLU E 1 22 ? 5.389 -41.248 12.532 1.00 94.10 ? 21 GLU E CB 1 ATOM 7503 C CG . GLU E 1 22 ? 5.964 -41.935 11.297 1.00 95.44 ? 21 GLU E CG 1 ATOM 7504 C CD . GLU E 1 22 ? 5.816 -43.455 11.346 1.00 95.26 ? 21 GLU E CD 1 ATOM 7505 O OE1 . GLU E 1 22 ? 4.676 -43.950 11.495 1.00 96.16 ? 21 GLU E OE1 1 ATOM 7506 O OE2 . GLU E 1 22 ? 6.839 -44.165 11.226 1.00 94.16 ? 21 GLU E OE2 1 ATOM 7507 N N . LYS E 1 23 ? 4.138 -38.395 14.207 1.00 93.58 ? 22 LYS E N 1 ATOM 7508 C CA . LYS E 1 23 ? 3.829 -37.970 15.580 1.00 91.66 ? 22 LYS E CA 1 ATOM 7509 C C . LYS E 1 23 ? 3.013 -39.054 16.300 1.00 91.24 ? 22 LYS E C 1 ATOM 7510 O O . LYS E 1 23 ? 2.481 -39.962 15.662 1.00 91.97 ? 22 LYS E O 1 ATOM 7511 C CB . LYS E 1 23 ? 3.065 -36.645 15.579 1.00 93.60 ? 22 LYS E CB 1 ATOM 7512 N N . ASN E 1 24 ? 2.938 -38.951 17.628 1.00 89.65 ? 23 ASN E N 1 ATOM 7513 C CA . ASN E 1 24 ? 2.137 -39.852 18.475 1.00 89.56 ? 23 ASN E CA 1 ATOM 7514 C C . ASN E 1 24 ? 2.110 -41.321 18.011 1.00 89.48 ? 23 ASN E C 1 ATOM 7515 O O . ASN E 1 24 ? 1.069 -41.836 17.593 1.00 91.83 ? 23 ASN E O 1 ATOM 7516 C CB . ASN E 1 24 ? 0.708 -39.295 18.632 1.00 92.49 ? 23 ASN E CB 1 ATOM 7517 C CG . ASN E 1 24 ? 0.660 -38.011 19.454 1.00 92.32 ? 23 ASN E CG 1 ATOM 7518 O OD1 . ASN E 1 24 ? 0.076 -37.008 19.035 1.00 94.19 ? 23 ASN E OD1 1 ATOM 7519 N ND2 . ASN E 1 24 ? 1.275 -38.038 20.631 1.00 89.77 ? 23 ASN E ND2 1 ATOM 7520 N N . VAL E 1 25 ? 3.267 -41.980 18.098 1.00 87.01 ? 24 VAL E N 1 ATOM 7521 C CA . VAL E 1 25 ? 3.431 -43.379 17.669 1.00 86.78 ? 24 VAL E CA 1 ATOM 7522 C C . VAL E 1 25 ? 3.595 -44.297 18.882 1.00 85.18 ? 24 VAL E C 1 ATOM 7523 O O . VAL E 1 25 ? 4.525 -44.130 19.670 1.00 82.96 ? 24 VAL E O 1 ATOM 7524 C CB . VAL E 1 25 ? 4.651 -43.532 16.730 1.00 85.87 ? 24 VAL E CB 1 ATOM 7525 C CG1 . VAL E 1 25 ? 5.104 -44.987 16.626 1.00 85.18 ? 24 VAL E CG1 1 ATOM 7526 C CG2 . VAL E 1 25 ? 4.328 -42.968 15.353 1.00 88.35 ? 24 VAL E CG2 1 ATOM 7527 N N . THR E 1 26 ? 2.710 -45.285 19.004 1.00 86.45 ? 25 THR E N 1 ATOM 7528 C CA . THR E 1 26 ? 2.655 -46.135 20.193 1.00 85.73 ? 25 THR E CA 1 ATOM 7529 C C . THR E 1 26 ? 3.712 -47.245 20.174 1.00 83.88 ? 25 THR E C 1 ATOM 7530 O O . THR E 1 26 ? 3.875 -47.946 19.172 1.00 84.52 ? 25 THR E O 1 ATOM 7531 C CB . THR E 1 26 ? 1.256 -46.757 20.348 1.00 88.61 ? 25 THR E CB 1 ATOM 7532 O OG1 . THR E 1 26 ? 0.271 -45.714 20.350 1.00 91.02 ? 25 THR E OG1 1 ATOM 7533 C CG2 . THR E 1 26 ? 1.154 -47.554 21.645 1.00 88.57 ? 25 THR E CG2 1 ATOM 7534 N N . VAL E 1 27 ? 4.408 -47.406 21.300 1.00 82.17 ? 26 VAL E N 1 ATOM 7535 C CA . VAL E 1 27 ? 5.505 -48.373 21.422 1.00 80.78 ? 26 VAL E CA 1 ATOM 7536 C C . VAL E 1 27 ? 5.420 -49.180 22.722 1.00 80.81 ? 26 VAL E C 1 ATOM 7537 O O . VAL E 1 27 ? 4.939 -48.684 23.746 1.00 81.50 ? 26 VAL E O 1 ATOM 7538 C CB . VAL E 1 27 ? 6.888 -47.680 21.348 1.00 78.86 ? 26 VAL E CB 1 ATOM 7539 C CG1 . VAL E 1 27 ? 7.168 -47.189 19.937 1.00 79.23 ? 26 VAL E CG1 1 ATOM 7540 C CG2 . VAL E 1 27 ? 6.982 -46.525 22.336 1.00 78.06 ? 26 VAL E CG2 1 ATOM 7541 N N . THR E 1 28 ? 5.901 -50.421 22.663 1.00 80.72 ? 27 THR E N 1 ATOM 7542 C CA . THR E 1 28 ? 5.877 -51.344 23.809 1.00 80.89 ? 27 THR E CA 1 ATOM 7543 C C . THR E 1 28 ? 6.702 -50.867 25.008 1.00 79.75 ? 27 THR E C 1 ATOM 7544 O O . THR E 1 28 ? 6.381 -51.193 26.148 1.00 80.06 ? 27 THR E O 1 ATOM 7545 C CB . THR E 1 28 ? 6.355 -52.764 23.415 1.00 81.00 ? 27 THR E CB 1 ATOM 7546 O OG1 . THR E 1 28 ? 6.297 -53.617 24.561 1.00 82.40 ? 27 THR E OG1 1 ATOM 7547 C CG2 . THR E 1 28 ? 7.784 -52.762 22.890 1.00 79.30 ? 27 THR E CG2 1 ATOM 7548 N N . HIS E 1 29 ? 7.775 -50.124 24.735 1.00 78.58 ? 28 HIS E N 1 ATOM 7549 C CA . HIS E 1 29 ? 8.594 -49.493 25.775 1.00 77.80 ? 28 HIS E CA 1 ATOM 7550 C C . HIS E 1 29 ? 9.051 -48.105 25.313 1.00 76.36 ? 28 HIS E C 1 ATOM 7551 O O . HIS E 1 29 ? 9.343 -47.900 24.135 1.00 75.34 ? 28 HIS E O 1 ATOM 7552 C CB . HIS E 1 29 ? 9.828 -50.345 26.106 1.00 77.70 ? 28 HIS E CB 1 ATOM 7553 C CG . HIS E 1 29 ? 9.508 -51.723 26.608 1.00 79.53 ? 28 HIS E CG 1 ATOM 7554 N ND1 . HIS E 1 29 ? 9.764 -52.860 25.871 1.00 80.00 ? 28 HIS E ND1 1 ATOM 7555 C CD2 . HIS E 1 29 ? 8.965 -52.146 27.775 1.00 80.85 ? 28 HIS E CD2 1 ATOM 7556 C CE1 . HIS E 1 29 ? 9.388 -53.923 26.560 1.00 81.71 ? 28 HIS E CE1 1 ATOM 7557 N NE2 . HIS E 1 29 ? 8.901 -53.517 27.719 1.00 82.40 ? 28 HIS E NE2 1 ATOM 7558 N N . ALA E 1 30 ? 9.129 -47.164 26.247 1.00 76.21 ? 29 ALA E N 1 ATOM 7559 C CA . ALA E 1 30 ? 9.577 -45.807 25.938 1.00 75.61 ? 29 ALA E CA 1 ATOM 7560 C C . ALA E 1 30 ? 10.273 -45.198 27.142 1.00 74.91 ? 29 ALA E C 1 ATOM 7561 O O . ALA E 1 30 ? 9.758 -45.268 28.259 1.00 75.79 ? 29 ALA E O 1 ATOM 7562 C CB . ALA E 1 30 ? 8.399 -44.943 25.519 1.00 76.48 ? 29 ALA E CB 1 ATOM 7563 N N . GLN E 1 31 ? 11.434 -44.591 26.906 1.00 74.13 ? 30 GLN E N 1 ATOM 7564 C CA . GLN E 1 31 ? 12.263 -44.051 27.981 1.00 73.64 ? 30 GLN E CA 1 ATOM 7565 C C . GLN E 1 31 ? 12.226 -42.522 27.996 1.00 72.39 ? 30 GLN E C 1 ATOM 7566 O O . GLN E 1 31 ? 12.776 -41.867 27.105 1.00 71.62 ? 30 GLN E O 1 ATOM 7567 C CB . GLN E 1 31 ? 13.707 -44.550 27.829 1.00 73.64 ? 30 GLN E CB 1 ATOM 7568 C CG . GLN E 1 31 ? 14.617 -44.264 29.019 1.00 73.42 ? 30 GLN E CG 1 ATOM 7569 C CD . GLN E 1 31 ? 14.149 -44.937 30.299 1.00 75.08 ? 30 GLN E CD 1 ATOM 7570 O OE1 . GLN E 1 31 ? 13.734 -46.104 30.296 1.00 76.45 ? 30 GLN E OE1 1 ATOM 7571 N NE2 . GLN E 1 31 ? 14.216 -44.203 31.407 1.00 75.12 ? 30 GLN E NE2 1 ATOM 7572 N N . ASP E 1 32 ? 11.572 -41.962 29.010 1.00 72.12 ? 31 ASP E N 1 ATOM 7573 C CA . ASP E 1 32 ? 11.566 -40.513 29.218 1.00 70.74 ? 31 ASP E CA 1 ATOM 7574 C C . ASP E 1 32 ? 12.969 -40.079 29.645 1.00 69.12 ? 31 ASP E C 1 ATOM 7575 O O . ASP E 1 32 ? 13.603 -40.742 30.472 1.00 69.77 ? 31 ASP E O 1 ATOM 7576 C CB . ASP E 1 32 ? 10.534 -40.131 30.286 1.00 71.41 ? 31 ASP E CB 1 ATOM 7577 C CG . ASP E 1 32 ? 10.243 -38.634 30.328 1.00 71.43 ? 31 ASP E CG 1 ATOM 7578 O OD1 . ASP E 1 32 ? 11.033 -37.840 29.770 1.00 70.37 ? 31 ASP E OD1 1 ATOM 7579 O OD2 . ASP E 1 32 ? 9.213 -38.253 30.930 1.00 72.30 ? 31 ASP E OD2 1 ATOM 7580 N N . ILE E 1 33 ? 13.451 -38.976 29.076 1.00 66.91 ? 32 ILE E N 1 ATOM 7581 C CA . ILE E 1 33 ? 14.796 -38.478 29.379 1.00 65.15 ? 32 ILE E CA 1 ATOM 7582 C C . ILE E 1 33 ? 14.816 -37.040 29.927 1.00 63.64 ? 32 ILE E C 1 ATOM 7583 O O . ILE E 1 33 ? 15.891 -36.468 30.136 1.00 62.04 ? 32 ILE E O 1 ATOM 7584 C CB . ILE E 1 33 ? 15.726 -38.589 28.144 1.00 65.36 ? 32 ILE E CB 1 ATOM 7585 C CG1 . ILE E 1 33 ? 15.095 -37.942 26.904 1.00 65.85 ? 32 ILE E CG1 1 ATOM 7586 C CG2 . ILE E 1 33 ? 16.049 -40.049 27.854 1.00 66.11 ? 32 ILE E CG2 1 ATOM 7587 C CD1 . ILE E 1 33 ? 16.062 -37.781 25.750 1.00 66.03 ? 32 ILE E CD1 1 ATOM 7588 N N . LEU E 1 34 ? 13.631 -36.482 30.184 1.00 63.26 ? 33 LEU E N 1 ATOM 7589 C CA . LEU E 1 34 ? 13.487 -35.104 30.650 1.00 61.97 ? 33 LEU E CA 1 ATOM 7590 C C . LEU E 1 34 ? 12.867 -35.048 32.052 1.00 61.86 ? 33 LEU E C 1 ATOM 7591 O O . LEU E 1 34 ? 11.891 -35.742 32.346 1.00 62.61 ? 33 LEU E O 1 ATOM 7592 C CB . LEU E 1 34 ? 12.624 -34.313 29.668 1.00 62.61 ? 33 LEU E CB 1 ATOM 7593 C CG . LEU E 1 34 ? 12.417 -32.826 29.946 1.00 62.26 ? 33 LEU E CG 1 ATOM 7594 C CD1 . LEU E 1 34 ? 13.727 -32.069 29.815 1.00 61.14 ? 33 LEU E CD1 1 ATOM 7595 C CD2 . LEU E 1 34 ? 11.378 -32.247 29.001 1.00 63.89 ? 33 LEU E CD2 1 ATOM 7596 N N . GLU E 1 35 ? 13.446 -34.196 32.895 1.00 60.60 ? 34 GLU E N 1 ATOM 7597 C CA . GLU E 1 35 ? 13.019 -33.999 34.276 1.00 60.69 ? 34 GLU E CA 1 ATOM 7598 C C . GLU E 1 35 ? 12.283 -32.658 34.407 1.00 60.86 ? 34 GLU E C 1 ATOM 7599 O O . GLU E 1 35 ? 12.894 -31.595 34.247 1.00 59.36 ? 34 GLU E O 1 ATOM 7600 C CB . GLU E 1 35 ? 14.253 -34.005 35.183 1.00 59.90 ? 34 GLU E CB 1 ATOM 7601 C CG . GLU E 1 35 ? 13.977 -33.703 36.649 1.00 60.32 ? 34 GLU E CG 1 ATOM 7602 C CD . GLU E 1 35 ? 13.098 -34.748 37.286 1.00 61.75 ? 34 GLU E CD 1 ATOM 7603 O OE1 . GLU E 1 35 ? 13.467 -35.942 37.228 1.00 62.58 ? 34 GLU E OE1 1 ATOM 7604 O OE2 . GLU E 1 35 ? 12.038 -34.377 37.827 1.00 62.68 ? 34 GLU E OE2 1 ATOM 7605 N N . LYS E 1 36 ? 10.987 -32.710 34.723 1.00 61.88 ? 35 LYS E N 1 ATOM 7606 C CA . LYS E 1 36 ? 10.141 -31.514 34.716 1.00 62.33 ? 35 LYS E CA 1 ATOM 7607 C C . LYS E 1 36 ? 9.734 -31.025 36.103 1.00 62.68 ? 35 LYS E C 1 ATOM 7608 O O . LYS E 1 36 ? 9.052 -30.008 36.215 1.00 63.44 ? 35 LYS E O 1 ATOM 7609 C CB . LYS E 1 36 ? 8.881 -31.766 33.888 1.00 64.36 ? 35 LYS E CB 1 ATOM 7610 C CG . LYS E 1 36 ? 9.139 -31.953 32.401 1.00 64.26 ? 35 LYS E CG 1 ATOM 7611 C CD . LYS E 1 36 ? 9.493 -33.389 32.040 1.00 64.00 ? 35 LYS E CD 1 ATOM 7612 C CE . LYS E 1 36 ? 8.270 -34.284 32.002 1.00 65.96 ? 35 LYS E CE 1 ATOM 7613 N NZ . LYS E 1 36 ? 8.661 -35.691 31.727 1.00 65.75 ? 35 LYS E NZ 1 ATOM 7614 N N . THR E 1 37 ? 10.166 -31.725 37.151 1.00 62.50 ? 36 THR E N 1 ATOM 7615 C CA . THR E 1 37 ? 9.721 -31.438 38.517 1.00 63.36 ? 36 THR E CA 1 ATOM 7616 C C . THR E 1 37 ? 10.869 -30.985 39.408 1.00 61.37 ? 36 THR E C 1 ATOM 7617 O O . THR E 1 37 ? 11.990 -31.482 39.287 1.00 59.16 ? 36 THR E O 1 ATOM 7618 C CB . THR E 1 37 ? 9.091 -32.682 39.175 1.00 65.58 ? 36 THR E CB 1 ATOM 7619 O OG1 . THR E 1 37 ? 10.126 -33.590 39.575 1.00 64.87 ? 36 THR E OG1 1 ATOM 7620 C CG2 . THR E 1 37 ? 8.127 -33.386 38.213 1.00 66.93 ? 36 THR E CG2 1 ATOM 7621 N N . HIS E 1 38 ? 10.567 -30.055 40.314 1.00 61.68 ? 37 HIS E N 1 ATOM 7622 C CA . HIS E 1 38 ? 11.533 -29.573 41.299 1.00 60.65 ? 37 HIS E CA 1 ATOM 7623 C C . HIS E 1 38 ? 10.873 -29.473 42.676 1.00 62.60 ? 37 HIS E C 1 ATOM 7624 O O . HIS E 1 38 ? 9.644 -29.437 42.773 1.00 64.89 ? 37 HIS E O 1 ATOM 7625 C CB . HIS E 1 38 ? 12.109 -28.219 40.866 1.00 59.00 ? 37 HIS E CB 1 ATOM 7626 C CG . HIS E 1 38 ? 11.072 -27.172 40.597 1.00 60.07 ? 37 HIS E CG 1 ATOM 7627 N ND1 . HIS E 1 38 ? 10.649 -26.280 41.558 1.00 60.97 ? 37 HIS E ND1 1 ATOM 7628 C CD2 . HIS E 1 38 ? 10.379 -26.869 39.474 1.00 60.83 ? 37 HIS E CD2 1 ATOM 7629 C CE1 . HIS E 1 38 ? 9.742 -25.472 41.040 1.00 62.18 ? 37 HIS E CE1 1 ATOM 7630 N NE2 . HIS E 1 38 ? 9.559 -25.809 39.776 1.00 61.97 ? 37 HIS E NE2 1 ATOM 7631 N N . ASN E 1 39 ? 11.688 -29.427 43.732 1.00 61.94 ? 38 ASN E N 1 ATOM 7632 C CA . ASN E 1 39 ? 11.178 -29.443 45.112 1.00 63.91 ? 38 ASN E CA 1 ATOM 7633 C C . ASN E 1 39 ? 10.694 -28.076 45.616 1.00 64.60 ? 38 ASN E C 1 ATOM 7634 O O . ASN E 1 39 ? 10.177 -27.962 46.727 1.00 67.24 ? 38 ASN E O 1 ATOM 7635 C CB . ASN E 1 39 ? 12.227 -30.034 46.069 1.00 63.69 ? 38 ASN E CB 1 ATOM 7636 C CG . ASN E 1 39 ? 13.284 -29.023 46.501 1.00 61.84 ? 38 ASN E CG 1 ATOM 7637 O OD1 . ASN E 1 39 ? 13.388 -27.924 45.953 1.00 59.68 ? 38 ASN E OD1 1 ATOM 7638 N ND2 . ASN E 1 39 ? 14.074 -29.399 47.497 1.00 62.35 ? 38 ASN E ND2 1 ATOM 7639 N N . GLY E 1 40 ? 10.907 -27.035 44.820 1.00 62.58 ? 39 GLY E N 1 ATOM 7640 C CA . GLY E 1 40 ? 10.277 -25.744 45.061 1.00 62.83 ? 39 GLY E CA 1 ATOM 7641 C C . GLY E 1 40 ? 10.901 -24.898 46.147 1.00 62.18 ? 39 GLY E C 1 ATOM 7642 O O . GLY E 1 40 ? 10.296 -23.922 46.572 1.00 63.14 ? 39 GLY E O 1 ATOM 7643 N N . LYS E 1 41 ? 12.108 -25.241 46.588 1.00 61.08 ? 40 LYS E N 1 ATOM 7644 C CA . LYS E 1 41 ? 12.751 -24.481 47.655 1.00 61.27 ? 40 LYS E CA 1 ATOM 7645 C C . LYS E 1 41 ? 14.270 -24.318 47.503 1.00 58.41 ? 40 LYS E C 1 ATOM 7646 O O . LYS E 1 41 ? 14.871 -24.882 46.595 1.00 57.08 ? 40 LYS E O 1 ATOM 7647 C CB . LYS E 1 41 ? 12.380 -25.067 49.022 1.00 64.87 ? 40 LYS E CB 1 ATOM 7648 C CG . LYS E 1 41 ? 12.466 -26.570 49.172 1.00 67.39 ? 40 LYS E CG 1 ATOM 7649 C CD . LYS E 1 41 ? 11.859 -26.987 50.505 1.00 71.23 ? 40 LYS E CD 1 ATOM 7650 C CE . LYS E 1 41 ? 12.212 -28.416 50.891 1.00 73.46 ? 40 LYS E CE 1 ATOM 7651 N NZ . LYS E 1 41 ? 11.216 -29.416 50.418 1.00 76.01 ? 40 LYS E NZ 1 ATOM 7652 N N . LEU E 1 42 ? 14.863 -23.507 48.382 1.00 57.33 ? 41 LEU E N 1 ATOM 7653 C CA . LEU E 1 42 ? 16.310 -23.251 48.384 1.00 55.14 ? 41 LEU E CA 1 ATOM 7654 C C . LEU E 1 42 ? 17.020 -24.110 49.434 1.00 56.28 ? 41 LEU E C 1 ATOM 7655 O O . LEU E 1 42 ? 16.693 -24.042 50.621 1.00 58.06 ? 41 LEU E O 1 ATOM 7656 C CB . LEU E 1 42 ? 16.599 -21.768 48.634 1.00 53.42 ? 41 LEU E CB 1 ATOM 7657 C CG . LEU E 1 42 ? 15.971 -20.787 47.642 1.00 52.35 ? 41 LEU E CG 1 ATOM 7658 C CD1 . LEU E 1 42 ? 16.194 -19.353 48.094 1.00 51.70 ? 41 LEU E CD1 1 ATOM 7659 C CD2 . LEU E 1 42 ? 16.534 -20.991 46.243 1.00 50.86 ? 41 LEU E CD2 1 ATOM 7660 N N . CYS E 1 43 ? 18.007 -24.888 48.982 1.00 55.38 ? 42 CYS E N 1 ATOM 7661 C CA . CYS E 1 43 ? 18.649 -25.929 49.782 1.00 56.83 ? 42 CYS E CA 1 ATOM 7662 C C . CYS E 1 43 ? 20.136 -25.710 49.988 1.00 55.56 ? 42 CYS E C 1 ATOM 7663 O O . CYS E 1 43 ? 20.777 -24.974 49.242 1.00 53.72 ? 42 CYS E O 1 ATOM 7664 C CB . CYS E 1 43 ? 18.488 -27.268 49.066 1.00 58.02 ? 42 CYS E CB 1 ATOM 7665 S SG . CYS E 1 43 ? 16.780 -27.707 48.706 1.00 59.61 ? 42 CYS E SG 1 ATOM 7666 N N . ASP E 1 44 ? 20.682 -26.378 50.998 1.00 57.19 ? 43 ASP E N 1 ATOM 7667 C CA . ASP E 1 44 ? 22.127 -26.550 51.112 1.00 57.09 ? 43 ASP E CA 1 ATOM 7668 C C . ASP E 1 44 ? 22.647 -27.231 49.845 1.00 56.09 ? 43 ASP E C 1 ATOM 7669 O O . ASP E 1 44 ? 21.974 -28.099 49.278 1.00 56.07 ? 43 ASP E O 1 ATOM 7670 C CB . ASP E 1 44 ? 22.482 -27.433 52.313 1.00 60.35 ? 43 ASP E CB 1 ATOM 7671 C CG . ASP E 1 44 ? 22.067 -26.832 53.642 1.00 62.04 ? 43 ASP E CG 1 ATOM 7672 O OD1 . ASP E 1 44 ? 21.722 -25.634 53.690 1.00 60.72 ? 43 ASP E OD1 1 ATOM 7673 O OD2 . ASP E 1 44 ? 22.094 -27.567 54.649 1.00 65.18 ? 43 ASP E OD2 1 ATOM 7674 N N . LEU E 1 45 ? 23.841 -26.844 49.404 1.00 54.84 ? 44 LEU E N 1 ATOM 7675 C CA . LEU E 1 45 ? 24.471 -27.482 48.250 1.00 54.16 ? 44 LEU E CA 1 ATOM 7676 C C . LEU E 1 45 ? 25.535 -28.476 48.712 1.00 56.01 ? 44 LEU E C 1 ATOM 7677 O O . LEU E 1 45 ? 26.655 -28.089 49.037 1.00 56.05 ? 44 LEU E O 1 ATOM 7678 C CB . LEU E 1 45 ? 25.081 -26.422 47.331 1.00 52.02 ? 44 LEU E CB 1 ATOM 7679 C CG . LEU E 1 45 ? 25.494 -26.903 45.939 1.00 51.39 ? 44 LEU E CG 1 ATOM 7680 C CD1 . LEU E 1 45 ? 24.276 -27.329 45.137 1.00 51.09 ? 44 LEU E CD1 1 ATOM 7681 C CD2 . LEU E 1 45 ? 26.261 -25.814 45.212 1.00 49.84 ? 44 LEU E CD2 1 ATOM 7682 N N . ASP E 1 46 ? 25.168 -29.756 48.746 1.00 57.95 ? 45 ASP E N 1 ATOM 7683 C CA . ASP E 1 46 ? 26.048 -30.831 49.224 1.00 60.63 ? 45 ASP E CA 1 ATOM 7684 C C . ASP E 1 46 ? 26.568 -30.547 50.641 1.00 62.23 ? 45 ASP E C 1 ATOM 7685 O O . ASP E 1 46 ? 27.767 -30.638 50.916 1.00 63.48 ? 45 ASP E O 1 ATOM 7686 C CB . ASP E 1 46 ? 27.212 -31.079 48.244 1.00 60.76 ? 45 ASP E CB 1 ATOM 7687 C CG . ASP E 1 46 ? 27.770 -32.511 48.328 1.00 64.30 ? 45 ASP E CG 1 ATOM 7688 O OD1 . ASP E 1 46 ? 27.457 -33.238 49.305 1.00 66.72 ? 45 ASP E OD1 1 ATOM 7689 O OD2 . ASP E 1 46 ? 28.516 -32.918 47.404 1.00 64.85 ? 45 ASP E OD2 1 ATOM 7690 N N . GLY E 1 47 ? 25.650 -30.196 51.534 1.00 62.38 ? 46 GLY E N 1 ATOM 7691 C CA . GLY E 1 47 ? 25.980 -29.986 52.937 1.00 64.35 ? 46 GLY E CA 1 ATOM 7692 C C . GLY E 1 47 ? 26.456 -28.593 53.322 1.00 62.73 ? 46 GLY E C 1 ATOM 7693 O O . GLY E 1 47 ? 26.784 -28.375 54.488 1.00 64.72 ? 46 GLY E O 1 ATOM 7694 N N . VAL E 1 48 ? 26.505 -27.651 52.376 1.00 59.43 ? 47 VAL E N 1 ATOM 7695 C CA . VAL E 1 48 ? 26.904 -26.258 52.702 1.00 58.08 ? 47 VAL E CA 1 ATOM 7696 C C . VAL E 1 48 ? 25.758 -25.269 52.462 1.00 56.23 ? 47 VAL E C 1 ATOM 7697 O O . VAL E 1 48 ? 25.236 -25.153 51.351 1.00 54.07 ? 47 VAL E O 1 ATOM 7698 C CB . VAL E 1 48 ? 28.148 -25.780 51.915 1.00 56.42 ? 47 VAL E CB 1 ATOM 7699 C CG1 . VAL E 1 48 ? 28.462 -24.320 52.241 1.00 54.99 ? 47 VAL E CG1 1 ATOM 7700 C CG2 . VAL E 1 48 ? 29.354 -26.645 52.231 1.00 58.86 ? 47 VAL E CG2 1 ATOM 7701 N N . LYS E 1 49 ? 25.398 -24.534 53.512 1.00 57.44 ? 48 LYS E N 1 ATOM 7702 C CA . LYS E 1 49 ? 24.261 -23.628 53.457 1.00 56.26 ? 48 LYS E CA 1 ATOM 7703 C C . LYS E 1 49 ? 24.573 -22.432 52.577 1.00 52.65 ? 48 LYS E C 1 ATOM 7704 O O . LYS E 1 49 ? 25.710 -21.980 52.535 1.00 52.20 ? 48 LYS E O 1 ATOM 7705 C CB . LYS E 1 49 ? 23.864 -23.160 54.863 1.00 58.69 ? 48 LYS E CB 1 ATOM 7706 C CG . LYS E 1 49 ? 22.489 -22.511 54.908 1.00 59.13 ? 48 LYS E CG 1 ATOM 7707 C CD . LYS E 1 49 ? 22.080 -22.080 56.306 1.00 62.00 ? 48 LYS E CD 1 ATOM 7708 C CE . LYS E 1 49 ? 21.267 -20.790 56.255 1.00 61.21 ? 48 LYS E CE 1 ATOM 7709 N NZ . LYS E 1 49 ? 20.533 -20.548 57.529 1.00 64.61 ? 48 LYS E NZ 1 ATOM 7710 N N . PRO E 1 50 ? 23.569 -21.935 51.840 1.00 50.43 ? 49 PRO E N 1 ATOM 7711 C CA . PRO E 1 50 ? 23.759 -20.703 51.087 1.00 47.62 ? 49 PRO E CA 1 ATOM 7712 C C . PRO E 1 50 ? 23.630 -19.452 51.963 1.00 46.83 ? 49 PRO E C 1 ATOM 7713 O O . PRO E 1 50 ? 23.155 -19.529 53.101 1.00 48.49 ? 49 PRO E O 1 ATOM 7714 C CB . PRO E 1 50 ? 22.622 -20.755 50.071 1.00 47.00 ? 49 PRO E CB 1 ATOM 7715 C CG . PRO E 1 50 ? 21.550 -21.500 50.775 1.00 49.04 ? 49 PRO E CG 1 ATOM 7716 C CD . PRO E 1 50 ? 22.286 -22.579 51.505 1.00 51.03 ? 49 PRO E CD 1 ATOM 7717 N N . LEU E 1 51 ? 24.077 -18.322 51.431 1.00 44.48 ? 50 LEU E N 1 ATOM 7718 C CA . LEU E 1 51 ? 23.870 -17.021 52.066 1.00 43.70 ? 50 LEU E CA 1 ATOM 7719 C C . LEU E 1 51 ? 22.597 -16.424 51.499 1.00 43.16 ? 50 LEU E C 1 ATOM 7720 O O . LEU E 1 51 ? 22.604 -15.951 50.376 1.00 41.42 ? 50 LEU E O 1 ATOM 7721 C CB . LEU E 1 51 ? 25.044 -16.093 51.774 1.00 42.01 ? 50 LEU E CB 1 ATOM 7722 C CG . LEU E 1 51 ? 24.893 -14.636 52.222 1.00 41.12 ? 50 LEU E CG 1 ATOM 7723 C CD1 . LEU E 1 51 ? 24.579 -14.554 53.707 1.00 42.69 ? 50 LEU E CD1 1 ATOM 7724 C CD2 . LEU E 1 51 ? 26.162 -13.872 51.908 1.00 39.89 ? 50 LEU E CD2 1 ATOM 7725 N N . ILE E 1 52 ? 21.499 -16.482 52.251 1.00 44.95 ? 51 ILE E N 1 ATOM 7726 C CA . ILE E 1 52 ? 20.236 -15.887 51.800 1.00 45.13 ? 51 ILE E CA 1 ATOM 7727 C C . ILE E 1 52 ? 20.217 -14.456 52.319 1.00 44.58 ? 51 ILE E C 1 ATOM 7728 O O . ILE E 1 52 ? 20.262 -14.245 53.525 1.00 45.87 ? 51 ILE E O 1 ATOM 7729 C CB . ILE E 1 52 ? 18.981 -16.625 52.325 1.00 47.52 ? 51 ILE E CB 1 ATOM 7730 C CG1 . ILE E 1 52 ? 19.128 -18.156 52.244 1.00 48.67 ? 51 ILE E CG1 1 ATOM 7731 C CG2 . ILE E 1 52 ? 17.743 -16.164 51.563 1.00 47.73 ? 51 ILE E CG2 1 ATOM 7732 C CD1 . ILE E 1 52 ? 19.528 -18.682 50.888 1.00 47.20 ? 51 ILE E CD1 1 ATOM 7733 N N . LEU E 1 53 ? 20.155 -13.481 51.421 1.00 43.25 ? 52 LEU E N 1 ATOM 7734 C CA . LEU E 1 53 ? 20.298 -12.075 51.814 1.00 42.93 ? 52 LEU E CA 1 ATOM 7735 C C . LEU E 1 53 ? 18.975 -11.429 52.177 1.00 44.40 ? 52 LEU E C 1 ATOM 7736 O O . LEU E 1 53 ? 18.933 -10.254 52.521 1.00 44.18 ? 52 LEU E O 1 ATOM 7737 C CB . LEU E 1 53 ? 21.005 -11.269 50.715 1.00 41.08 ? 52 LEU E CB 1 ATOM 7738 C CG . LEU E 1 53 ? 22.498 -11.557 50.573 1.00 40.09 ? 52 LEU E CG 1 ATOM 7739 C CD1 . LEU E 1 53 ? 23.068 -10.768 49.412 1.00 38.83 ? 52 LEU E CD1 1 ATOM 7740 C CD2 . LEU E 1 53 ? 23.256 -11.244 51.859 1.00 40.36 ? 52 LEU E CD2 1 ATOM 7741 N N . ARG E 1 54 ? 17.897 -12.202 52.103 1.00 46.80 ? 53 ARG E N 1 ATOM 7742 C CA . ARG E 1 54 ? 16.595 -11.768 52.586 1.00 49.11 ? 53 ARG E CA 1 ATOM 7743 C C . ARG E 1 54 ? 16.145 -10.481 51.885 1.00 48.07 ? 53 ARG E C 1 ATOM 7744 O O . ARG E 1 54 ? 15.835 -10.526 50.703 1.00 48.01 ? 53 ARG E O 1 ATOM 7745 C CB . ARG E 1 54 ? 16.631 -11.641 54.107 1.00 51.44 ? 53 ARG E CB 1 ATOM 7746 C CG . ARG E 1 54 ? 16.928 -12.969 54.788 1.00 53.78 ? 53 ARG E CG 1 ATOM 7747 C CD . ARG E 1 54 ? 17.170 -12.785 56.274 1.00 55.83 ? 53 ARG E CD 1 ATOM 7748 N NE . ARG E 1 54 ? 15.947 -12.396 56.970 1.00 58.56 ? 53 ARG E NE 1 ATOM 7749 C CZ . ARG E 1 54 ? 15.229 -13.185 57.756 1.00 61.80 ? 53 ARG E CZ 1 ATOM 7750 N NH1 . ARG E 1 54 ? 15.593 -14.441 58.001 1.00 62.72 ? 53 ARG E NH1 1 ATOM 7751 N NH2 . ARG E 1 54 ? 14.134 -12.698 58.316 1.00 64.99 ? 53 ARG E NH2 1 ATOM 7752 N N . ASP E 1 55 ? 16.114 -9.350 52.585 1.00 47.53 ? 54 ASP E N 1 ATOM 7753 C CA . ASP E 1 55 ? 15.761 -8.078 51.959 1.00 46.89 ? 54 ASP E CA 1 ATOM 7754 C C . ASP E 1 55 ? 16.983 -7.190 51.727 1.00 43.92 ? 54 ASP E C 1 ATOM 7755 O O . ASP E 1 55 ? 16.840 -6.038 51.324 1.00 43.24 ? 54 ASP E O 1 ATOM 7756 C CB . ASP E 1 55 ? 14.757 -7.323 52.822 1.00 49.43 ? 54 ASP E CB 1 ATOM 7757 C CG . ASP E 1 55 ? 13.472 -8.072 53.006 1.00 52.50 ? 54 ASP E CG 1 ATOM 7758 O OD1 . ASP E 1 55 ? 12.949 -8.601 52.009 1.00 53.23 ? 54 ASP E OD1 1 ATOM 7759 O OD2 . ASP E 1 55 ? 12.981 -8.122 54.154 1.00 55.00 ? 54 ASP E OD2 1 ATOM 7760 N N . CYS E 1 56 ? 18.177 -7.727 51.981 1.00 42.12 ? 55 CYS E N 1 ATOM 7761 C CA . CYS E 1 56 ? 19.412 -6.972 51.802 1.00 40.05 ? 55 CYS E CA 1 ATOM 7762 C C . CYS E 1 56 ? 20.011 -7.258 50.442 1.00 37.98 ? 55 CYS E C 1 ATOM 7763 O O . CYS E 1 56 ? 19.882 -8.353 49.924 1.00 38.13 ? 55 CYS E O 1 ATOM 7764 C CB . CYS E 1 56 ? 20.433 -7.293 52.900 1.00 40.08 ? 55 CYS E CB 1 ATOM 7765 S SG . CYS E 1 56 ? 19.990 -6.660 54.537 1.00 42.26 ? 55 CYS E SG 1 ATOM 7766 N N . SER E 1 57 ? 20.656 -6.253 49.864 1.00 36.08 ? 56 SER E N 1 ATOM 7767 C CA . SER E 1 57 ? 21.439 -6.437 48.656 1.00 34.73 ? 56 SER E CA 1 ATOM 7768 C C . SER E 1 57 ? 22.901 -6.708 49.023 1.00 33.30 ? 56 SER E C 1 ATOM 7769 O O . SER E 1 57 ? 23.298 -6.576 50.180 1.00 33.04 ? 56 SER E O 1 ATOM 7770 C CB . SER E 1 57 ? 21.354 -5.195 47.781 1.00 34.51 ? 56 SER E CB 1 ATOM 7771 O OG . SER E 1 57 ? 22.190 -4.174 48.300 1.00 33.59 ? 56 SER E OG 1 ATOM 7772 N N . VAL E 1 58 ? 23.693 -7.078 48.027 1.00 32.61 ? 57 VAL E N 1 ATOM 7773 C CA . VAL E 1 58 ? 25.131 -7.266 48.200 1.00 31.93 ? 57 VAL E CA 1 ATOM 7774 C C . VAL E 1 58 ? 25.732 -5.976 48.766 1.00 31.26 ? 57 VAL E C 1 ATOM 7775 O O . VAL E 1 58 ? 26.416 -6.004 49.796 1.00 30.71 ? 57 VAL E O 1 ATOM 7776 C CB . VAL E 1 58 ? 25.823 -7.665 46.862 1.00 31.83 ? 57 VAL E CB 1 ATOM 7777 C CG1 . VAL E 1 58 ? 27.340 -7.608 46.980 1.00 31.54 ? 57 VAL E CG1 1 ATOM 7778 C CG2 . VAL E 1 58 ? 25.394 -9.062 46.434 1.00 32.33 ? 57 VAL E CG2 1 ATOM 7779 N N . ALA E 1 59 ? 25.440 -4.851 48.112 1.00 31.14 ? 58 ALA E N 1 ATOM 7780 C CA . ALA E 1 59 ? 25.907 -3.559 48.595 1.00 30.98 ? 58 ALA E CA 1 ATOM 7781 C C . ALA E 1 59 ? 25.526 -3.342 50.054 1.00 31.05 ? 58 ALA E C 1 ATOM 7782 O O . ALA E 1 59 ? 26.373 -2.976 50.854 1.00 30.52 ? 58 ALA E O 1 ATOM 7783 C CB . ALA E 1 59 ? 25.389 -2.412 47.724 1.00 31.32 ? 58 ALA E CB 1 ATOM 7784 N N . GLY E 1 60 ? 24.266 -3.603 50.395 1.00 32.31 ? 59 GLY E N 1 ATOM 7785 C CA . GLY E 1 60 ? 23.775 -3.431 51.762 1.00 33.00 ? 59 GLY E CA 1 ATOM 7786 C C . GLY E 1 60 ? 24.465 -4.338 52.762 1.00 33.49 ? 59 GLY E C 1 ATOM 7787 O O . GLY E 1 60 ? 24.793 -3.923 53.876 1.00 33.70 ? 59 GLY E O 1 ATOM 7788 N N . TRP E 1 61 ? 24.655 -5.591 52.374 1.00 34.28 ? 60 TRP E N 1 ATOM 7789 C CA . TRP E 1 61 ? 25.490 -6.515 53.120 1.00 35.20 ? 60 TRP E CA 1 ATOM 7790 C C . TRP E 1 61 ? 26.910 -5.992 53.372 1.00 34.27 ? 60 TRP E C 1 ATOM 7791 O O . TRP E 1 61 ? 27.348 -5.865 54.509 1.00 35.02 ? 60 TRP E O 1 ATOM 7792 C CB . TRP E 1 61 ? 25.583 -7.817 52.345 1.00 36.54 ? 60 TRP E CB 1 ATOM 7793 C CG . TRP E 1 61 ? 26.592 -8.753 52.870 1.00 38.15 ? 60 TRP E CG 1 ATOM 7794 C CD1 . TRP E 1 61 ? 26.981 -8.899 54.168 1.00 39.28 ? 60 TRP E CD1 1 ATOM 7795 C CD2 . TRP E 1 61 ? 27.317 -9.726 52.117 1.00 39.20 ? 60 TRP E CD2 1 ATOM 7796 N NE1 . TRP E 1 61 ? 27.921 -9.890 54.267 1.00 40.90 ? 60 TRP E NE1 1 ATOM 7797 C CE2 . TRP E 1 61 ? 28.138 -10.425 53.024 1.00 40.33 ? 60 TRP E CE2 1 ATOM 7798 C CE3 . TRP E 1 61 ? 27.357 -10.070 50.761 1.00 39.20 ? 60 TRP E CE3 1 ATOM 7799 C CZ2 . TRP E 1 61 ? 28.997 -11.440 52.623 1.00 41.25 ? 60 TRP E CZ2 1 ATOM 7800 C CZ3 . TRP E 1 61 ? 28.205 -11.084 50.361 1.00 39.88 ? 60 TRP E CZ3 1 ATOM 7801 C CH2 . TRP E 1 61 ? 29.011 -11.763 51.292 1.00 41.31 ? 60 TRP E CH2 1 ATOM 7802 N N . LEU E 1 62 ? 27.629 -5.684 52.311 1.00 33.47 ? 61 LEU E N 1 ATOM 7803 C CA . LEU E 1 62 ? 29.064 -5.384 52.422 1.00 33.18 ? 61 LEU E CA 1 ATOM 7804 C C . LEU E 1 62 ? 29.390 -4.044 53.080 1.00 33.17 ? 61 LEU E C 1 ATOM 7805 O O . LEU E 1 62 ? 30.298 -3.974 53.914 1.00 33.41 ? 61 LEU E O 1 ATOM 7806 C CB . LEU E 1 62 ? 29.719 -5.477 51.042 1.00 32.56 ? 61 LEU E CB 1 ATOM 7807 C CG . LEU E 1 62 ? 29.672 -6.910 50.490 1.00 33.18 ? 61 LEU E CG 1 ATOM 7808 C CD1 . LEU E 1 62 ? 30.136 -6.964 49.038 1.00 33.31 ? 61 LEU E CD1 1 ATOM 7809 C CD2 . LEU E 1 62 ? 30.498 -7.840 51.361 1.00 33.95 ? 61 LEU E CD2 1 ATOM 7810 N N . LEU E 1 63 ? 28.665 -2.990 52.710 1.00 32.84 ? 62 LEU E N 1 ATOM 7811 C CA . LEU E 1 63 ? 28.893 -1.659 53.300 1.00 32.89 ? 62 LEU E CA 1 ATOM 7812 C C . LEU E 1 63 ? 28.439 -1.642 54.742 1.00 33.39 ? 62 LEU E C 1 ATOM 7813 O O . LEU E 1 63 ? 29.000 -0.937 55.561 1.00 33.12 ? 62 LEU E O 1 ATOM 7814 C CB . LEU E 1 63 ? 28.147 -0.581 52.529 1.00 32.68 ? 62 LEU E CB 1 ATOM 7815 C CG . LEU E 1 63 ? 28.725 -0.349 51.142 1.00 33.22 ? 62 LEU E CG 1 ATOM 7816 C CD1 . LEU E 1 63 ? 27.679 0.321 50.265 1.00 34.07 ? 62 LEU E CD1 1 ATOM 7817 C CD2 . LEU E 1 63 ? 30.011 0.477 51.188 1.00 32.81 ? 62 LEU E CD2 1 ATOM 7818 N N . GLY E 1 64 ? 27.417 -2.437 55.042 1.00 34.34 ? 63 GLY E N 1 ATOM 7819 C CA . GLY E 1 64 ? 26.900 -2.550 56.389 1.00 35.41 ? 63 GLY E CA 1 ATOM 7820 C C . GLY E 1 64 ? 25.664 -1.725 56.689 1.00 35.74 ? 63 GLY E C 1 ATOM 7821 O O . GLY E 1 64 ? 25.556 -1.193 57.779 1.00 36.35 ? 63 GLY E O 1 ATOM 7822 N N . ASN E 1 65 ? 24.724 -1.634 55.745 1.00 36.15 ? 64 ASN E N 1 ATOM 7823 C CA . ASN E 1 65 ? 23.417 -1.008 56.002 1.00 37.20 ? 64 ASN E CA 1 ATOM 7824 C C . ASN E 1 65 ? 22.892 -1.465 57.360 1.00 38.49 ? 64 ASN E C 1 ATOM 7825 O O . ASN E 1 65 ? 22.823 -2.666 57.597 1.00 39.24 ? 64 ASN E O 1 ATOM 7826 C CB . ASN E 1 65 ? 22.406 -1.388 54.904 1.00 37.89 ? 64 ASN E CB 1 ATOM 7827 C CG . ASN E 1 65 ? 21.050 -0.683 55.063 1.00 39.38 ? 64 ASN E CG 1 ATOM 7828 O OD1 . ASN E 1 65 ? 20.492 -0.595 56.157 1.00 40.30 ? 64 ASN E OD1 1 ATOM 7829 N ND2 . ASN E 1 65 ? 20.517 -0.186 53.954 1.00 39.67 ? 64 ASN E ND2 1 ATOM 7830 N N . PRO E 1 66 ? 22.519 -0.519 58.256 1.00 39.04 ? 65 PRO E N 1 ATOM 7831 C CA . PRO E 1 66 ? 22.039 -0.884 59.596 1.00 41.24 ? 65 PRO E CA 1 ATOM 7832 C C . PRO E 1 66 ? 20.931 -1.938 59.603 1.00 43.25 ? 65 PRO E C 1 ATOM 7833 O O . PRO E 1 66 ? 20.883 -2.751 60.512 1.00 45.57 ? 65 PRO E O 1 ATOM 7834 C CB . PRO E 1 66 ? 21.499 0.429 60.163 1.00 41.86 ? 65 PRO E CB 1 ATOM 7835 C CG . PRO E 1 66 ? 22.107 1.501 59.381 1.00 39.76 ? 65 PRO E CG 1 ATOM 7836 C CD . PRO E 1 66 ? 22.593 0.937 58.078 1.00 38.44 ? 65 PRO E CD 1 ATOM 7837 N N . MET E 1 67 ? 20.066 -1.933 58.594 1.00 43.46 ? 66 MET E N 1 ATOM 7838 C CA . MET E 1 67 ? 19.018 -2.954 58.464 1.00 45.83 ? 66 MET E CA 1 ATOM 7839 C C . MET E 1 67 ? 19.555 -4.354 58.152 1.00 45.60 ? 66 MET E C 1 ATOM 7840 O O . MET E 1 67 ? 18.809 -5.313 58.165 1.00 46.79 ? 66 MET E O 1 ATOM 7841 C CB . MET E 1 67 ? 18.021 -2.556 57.366 1.00 46.27 ? 66 MET E CB 1 ATOM 7842 C CG . MET E 1 67 ? 17.311 -1.221 57.593 1.00 47.37 ? 66 MET E CG 1 ATOM 7843 S SD . MET E 1 67 ? 16.408 -1.123 59.145 1.00 50.99 ? 66 MET E SD 1 ATOM 7844 C CE . MET E 1 67 ? 15.430 -2.623 59.092 1.00 53.28 ? 66 MET E CE 1 ATOM 7845 N N . CYS E 1 68 ? 20.849 -4.464 57.868 1.00 44.55 ? 67 CYS E N 1 ATOM 7846 C CA . CYS E 1 68 ? 21.436 -5.707 57.380 1.00 44.31 ? 67 CYS E CA 1 ATOM 7847 C C . CYS E 1 68 ? 22.320 -6.420 58.421 1.00 45.69 ? 67 CYS E C 1 ATOM 7848 O O . CYS E 1 68 ? 23.176 -7.244 58.061 1.00 46.23 ? 67 CYS E O 1 ATOM 7849 C CB . CYS E 1 68 ? 22.233 -5.405 56.109 1.00 41.48 ? 67 CYS E CB 1 ATOM 7850 S SG . CYS E 1 68 ? 21.169 -4.968 54.715 1.00 41.22 ? 67 CYS E SG 1 ATOM 7851 N N . ASP E 1 69 ? 22.082 -6.138 59.699 1.00 46.97 ? 68 ASP E N 1 ATOM 7852 C CA . ASP E 1 69 ? 22.968 -6.609 60.774 1.00 48.29 ? 68 ASP E CA 1 ATOM 7853 C C . ASP E 1 69 ? 23.075 -8.120 60.905 1.00 50.31 ? 68 ASP E C 1 ATOM 7854 O O . ASP E 1 69 ? 24.037 -8.621 61.479 1.00 52.14 ? 68 ASP E O 1 ATOM 7855 C CB . ASP E 1 69 ? 22.568 -5.999 62.128 1.00 49.58 ? 68 ASP E CB 1 ATOM 7856 C CG . ASP E 1 69 ? 23.135 -4.606 62.327 1.00 47.82 ? 68 ASP E CG 1 ATOM 7857 O OD1 . ASP E 1 69 ? 23.937 -4.154 61.477 1.00 44.90 ? 68 ASP E OD1 1 ATOM 7858 O OD2 . ASP E 1 69 ? 22.784 -3.962 63.341 1.00 48.88 ? 68 ASP E OD2 1 ATOM 7859 N N . GLU E 1 70 ? 22.102 -8.848 60.374 1.00 51.17 ? 69 GLU E N 1 ATOM 7860 C CA . GLU E 1 70 ? 22.165 -10.302 60.365 1.00 52.50 ? 69 GLU E CA 1 ATOM 7861 C C . GLU E 1 70 ? 23.430 -10.794 59.652 1.00 50.20 ? 69 GLU E C 1 ATOM 7862 O O . GLU E 1 70 ? 23.946 -11.873 59.961 1.00 51.68 ? 69 GLU E O 1 ATOM 7863 C CB . GLU E 1 70 ? 20.920 -10.861 59.682 1.00 53.66 ? 69 GLU E CB 1 ATOM 7864 C CG . GLU E 1 70 ? 20.864 -12.379 59.621 1.00 56.14 ? 69 GLU E CG 1 ATOM 7865 C CD . GLU E 1 70 ? 19.685 -12.869 58.815 1.00 57.23 ? 69 GLU E CD 1 ATOM 7866 O OE1 . GLU E 1 70 ? 18.695 -12.110 58.733 1.00 58.41 ? 69 GLU E OE1 1 ATOM 7867 O OE2 . GLU E 1 70 ? 19.750 -13.999 58.267 1.00 57.61 ? 69 GLU E OE2 1 ATOM 7868 N N . PHE E 1 71 ? 23.936 -9.988 58.724 1.00 46.77 ? 70 PHE E N 1 ATOM 7869 C CA . PHE E 1 71 ? 25.016 -10.406 57.828 1.00 44.92 ? 70 PHE E CA 1 ATOM 7870 C C . PHE E 1 71 ? 26.382 -9.783 58.120 1.00 44.07 ? 70 PHE E C 1 ATOM 7871 O O . PHE E 1 71 ? 27.214 -9.676 57.231 1.00 42.90 ? 70 PHE E O 1 ATOM 7872 C CB . PHE E 1 71 ? 24.602 -10.113 56.390 1.00 42.62 ? 70 PHE E CB 1 ATOM 7873 C CG . PHE E 1 71 ? 23.248 -10.657 56.042 1.00 43.17 ? 70 PHE E CG 1 ATOM 7874 C CD1 . PHE E 1 71 ? 23.047 -12.024 55.957 1.00 44.08 ? 70 PHE E CD1 1 ATOM 7875 C CD2 . PHE E 1 71 ? 22.170 -9.805 55.836 1.00 42.84 ? 70 PHE E CD2 1 ATOM 7876 C CE1 . PHE E 1 71 ? 21.799 -12.538 55.656 1.00 45.17 ? 70 PHE E CE1 1 ATOM 7877 C CE2 . PHE E 1 71 ? 20.922 -10.307 55.527 1.00 43.97 ? 70 PHE E CE2 1 ATOM 7878 C CZ . PHE E 1 71 ? 20.733 -11.679 55.438 1.00 45.25 ? 70 PHE E CZ 1 ATOM 7879 N N . LEU E 1 72 ? 26.631 -9.416 59.371 1.00 45.67 ? 71 LEU E N 1 ATOM 7880 C CA . LEU E 1 72 ? 27.862 -8.694 59.727 1.00 45.34 ? 71 LEU E CA 1 ATOM 7881 C C . LEU E 1 72 ? 29.125 -9.542 59.577 1.00 45.99 ? 71 LEU E C 1 ATOM 7882 O O . LEU E 1 72 ? 30.150 -9.048 59.096 1.00 44.78 ? 71 LEU E O 1 ATOM 7883 C CB . LEU E 1 72 ? 27.762 -8.140 61.158 1.00 46.64 ? 71 LEU E CB 1 ATOM 7884 C CG . LEU E 1 72 ? 26.866 -6.901 61.257 1.00 45.74 ? 71 LEU E CG 1 ATOM 7885 C CD1 . LEU E 1 72 ? 26.344 -6.691 62.663 1.00 48.26 ? 71 LEU E CD1 1 ATOM 7886 C CD2 . LEU E 1 72 ? 27.596 -5.656 60.780 1.00 43.57 ? 71 LEU E CD2 1 ATOM 7887 N N . ASN E 1 73 ? 29.036 -10.801 60.005 1.00 47.83 ? 72 ASN E N 1 ATOM 7888 C CA . ASN E 1 73 ? 30.133 -11.763 59.919 1.00 49.27 ? 72 ASN E CA 1 ATOM 7889 C C . ASN E 1 73 ? 29.573 -13.133 59.539 1.00 50.32 ? 72 ASN E C 1 ATOM 7890 O O . ASN E 1 73 ? 29.476 -14.008 60.379 1.00 52.46 ? 72 ASN E O 1 ATOM 7891 C CB . ASN E 1 73 ? 30.848 -11.909 61.279 1.00 51.75 ? 72 ASN E CB 1 ATOM 7892 C CG . ASN E 1 73 ? 31.446 -10.610 61.798 1.00 50.68 ? 72 ASN E CG 1 ATOM 7893 O OD1 . ASN E 1 73 ? 32.372 -10.057 61.214 1.00 49.24 ? 72 ASN E OD1 1 ATOM 7894 N ND2 . ASN E 1 73 ? 30.945 -10.144 62.934 1.00 51.93 ? 72 ASN E ND2 1 ATOM 7895 N N . VAL E 1 74 ? 29.207 -13.315 58.279 1.00 49.00 ? 73 VAL E N 1 ATOM 7896 C CA . VAL E 1 74 ? 28.494 -14.521 57.854 1.00 50.15 ? 73 VAL E CA 1 ATOM 7897 C C . VAL E 1 74 ? 29.424 -15.721 57.687 1.00 52.02 ? 73 VAL E C 1 ATOM 7898 O O . VAL E 1 74 ? 30.604 -15.552 57.403 1.00 52.63 ? 73 VAL E O 1 ATOM 7899 C CB . VAL E 1 74 ? 27.728 -14.301 56.533 1.00 48.14 ? 73 VAL E CB 1 ATOM 7900 C CG1 . VAL E 1 74 ? 26.694 -13.206 56.704 1.00 47.22 ? 73 VAL E CG1 1 ATOM 7901 C CG2 . VAL E 1 74 ? 28.672 -13.967 55.380 1.00 46.61 ? 73 VAL E CG2 1 ATOM 7902 N N . PRO E 1 75 ? 28.894 -16.940 57.855 1.00 53.51 ? 74 PRO E N 1 ATOM 7903 C CA . PRO E 1 75 ? 29.714 -18.127 57.625 1.00 55.35 ? 74 PRO E CA 1 ATOM 7904 C C . PRO E 1 75 ? 29.944 -18.418 56.131 1.00 53.45 ? 74 PRO E C 1 ATOM 7905 O O . PRO E 1 75 ? 29.473 -17.675 55.270 1.00 51.19 ? 74 PRO E O 1 ATOM 7906 C CB . PRO E 1 75 ? 28.911 -19.255 58.298 1.00 57.88 ? 74 PRO E CB 1 ATOM 7907 C CG . PRO E 1 75 ? 27.500 -18.783 58.294 1.00 56.83 ? 74 PRO E CG 1 ATOM 7908 C CD . PRO E 1 75 ? 27.523 -17.278 58.282 1.00 54.64 ? 74 PRO E CD 1 ATOM 7909 N N . GLU E 1 76 ? 30.697 -19.477 55.850 1.00 54.41 ? 75 GLU E N 1 ATOM 7910 C CA . GLU E 1 76 ? 30.995 -19.898 54.488 1.00 53.15 ? 75 GLU E CA 1 ATOM 7911 C C . GLU E 1 76 ? 29.716 -20.341 53.793 1.00 51.69 ? 75 GLU E C 1 ATOM 7912 O O . GLU E 1 76 ? 28.832 -20.920 54.422 1.00 52.82 ? 75 GLU E O 1 ATOM 7913 C CB . GLU E 1 76 ? 31.996 -21.058 54.522 1.00 56.06 ? 75 GLU E CB 1 ATOM 7914 C CG . GLU E 1 76 ? 32.263 -21.749 53.192 1.00 55.80 ? 75 GLU E CG 1 ATOM 7915 C CD . GLU E 1 76 ? 33.181 -22.946 53.337 1.00 58.72 ? 75 GLU E CD 1 ATOM 7916 O OE1 . GLU E 1 76 ? 33.871 -23.039 54.368 1.00 60.99 ? 75 GLU E OE1 1 ATOM 7917 O OE2 . GLU E 1 76 ? 33.210 -23.792 52.420 1.00 59.11 ? 75 GLU E OE2 1 ATOM 7918 N N . TRP E 1 77 ? 29.630 -20.073 52.491 1.00 49.34 ? 76 TRP E N 1 ATOM 7919 C CA . TRP E 1 77 ? 28.431 -20.374 51.711 1.00 47.83 ? 76 TRP E CA 1 ATOM 7920 C C . TRP E 1 77 ? 28.768 -21.099 50.421 1.00 47.70 ? 76 TRP E C 1 ATOM 7921 O O . TRP E 1 77 ? 29.884 -21.025 49.921 1.00 47.76 ? 76 TRP E O 1 ATOM 7922 C CB . TRP E 1 77 ? 27.670 -19.085 51.376 1.00 45.21 ? 76 TRP E CB 1 ATOM 7923 C CG . TRP E 1 77 ? 28.429 -18.186 50.482 1.00 43.38 ? 76 TRP E CG 1 ATOM 7924 C CD1 . TRP E 1 77 ? 28.487 -18.237 49.120 1.00 42.25 ? 76 TRP E CD1 1 ATOM 7925 C CD2 . TRP E 1 77 ? 29.258 -17.095 50.879 1.00 42.79 ? 76 TRP E CD2 1 ATOM 7926 N NE1 . TRP E 1 77 ? 29.300 -17.238 48.642 1.00 41.40 ? 76 TRP E NE1 1 ATOM 7927 C CE2 . TRP E 1 77 ? 29.787 -16.522 49.703 1.00 41.53 ? 76 TRP E CE2 1 ATOM 7928 C CE3 . TRP E 1 77 ? 29.606 -16.545 52.111 1.00 43.28 ? 76 TRP E CE3 1 ATOM 7929 C CZ2 . TRP E 1 77 ? 30.644 -15.441 49.729 1.00 40.87 ? 76 TRP E CZ2 1 ATOM 7930 C CZ3 . TRP E 1 77 ? 30.457 -15.468 52.135 1.00 42.63 ? 76 TRP E CZ3 1 ATOM 7931 C CH2 . TRP E 1 77 ? 30.969 -14.926 50.950 1.00 41.50 ? 76 TRP E CH2 1 ATOM 7932 N N . SER E 1 78 ? 27.772 -21.785 49.881 1.00 48.02 ? 77 SER E N 1 ATOM 7933 C CA . SER E 1 78 ? 27.900 -22.470 48.605 1.00 47.93 ? 77 SER E CA 1 ATOM 7934 C C . SER E 1 78 ? 27.518 -21.501 47.514 1.00 45.72 ? 77 SER E C 1 ATOM 7935 O O . SER E 1 78 ? 28.309 -21.226 46.619 1.00 45.70 ? 77 SER E O 1 ATOM 7936 C CB . SER E 1 78 ? 26.983 -23.687 48.564 1.00 48.98 ? 77 SER E CB 1 ATOM 7937 O OG . SER E 1 78 ? 25.713 -23.379 49.111 1.00 48.83 ? 77 SER E OG 1 ATOM 7938 N N . TYR E 1 79 ? 26.302 -20.978 47.599 1.00 44.53 ? 78 TYR E N 1 ATOM 7939 C CA . TYR E 1 79 ? 25.859 -19.924 46.689 1.00 42.84 ? 78 TYR E CA 1 ATOM 7940 C C . TYR E 1 79 ? 25.249 -18.767 47.474 1.00 42.04 ? 78 TYR E C 1 ATOM 7941 O O . TYR E 1 79 ? 24.967 -18.891 48.662 1.00 42.41 ? 78 TYR E O 1 ATOM 7942 C CB . TYR E 1 79 ? 24.879 -20.472 45.644 1.00 42.36 ? 78 TYR E CB 1 ATOM 7943 C CG . TYR E 1 79 ? 23.644 -21.135 46.207 1.00 43.18 ? 78 TYR E CG 1 ATOM 7944 C CD1 . TYR E 1 79 ? 23.696 -22.421 46.740 1.00 44.64 ? 78 TYR E CD1 1 ATOM 7945 C CD2 . TYR E 1 79 ? 22.417 -20.484 46.197 1.00 42.87 ? 78 TYR E CD2 1 ATOM 7946 C CE1 . TYR E 1 79 ? 22.563 -23.036 47.244 1.00 45.51 ? 78 TYR E CE1 1 ATOM 7947 C CE2 . TYR E 1 79 ? 21.279 -21.091 46.704 1.00 43.92 ? 78 TYR E CE2 1 ATOM 7948 C CZ . TYR E 1 79 ? 21.358 -22.362 47.229 1.00 45.14 ? 78 TYR E CZ 1 ATOM 7949 O OH . TYR E 1 79 ? 20.225 -22.952 47.730 1.00 46.31 ? 78 TYR E OH 1 ATOM 7950 N N . ILE E 1 80 ? 25.081 -17.637 46.801 1.00 41.16 ? 79 ILE E N 1 ATOM 7951 C CA . ILE E 1 80 ? 24.439 -16.466 47.387 1.00 40.91 ? 79 ILE E CA 1 ATOM 7952 C C . ILE E 1 80 ? 23.089 -16.265 46.700 1.00 41.57 ? 79 ILE E C 1 ATOM 7953 O O . ILE E 1 80 ? 22.996 -16.343 45.474 1.00 41.40 ? 79 ILE E O 1 ATOM 7954 C CB . ILE E 1 80 ? 25.284 -15.188 47.193 1.00 39.69 ? 79 ILE E CB 1 ATOM 7955 C CG1 . ILE E 1 80 ? 26.688 -15.367 47.780 1.00 39.91 ? 79 ILE E CG1 1 ATOM 7956 C CG2 . ILE E 1 80 ? 24.581 -13.987 47.817 1.00 39.02 ? 79 ILE E CG2 1 ATOM 7957 C CD1 . ILE E 1 80 ? 27.610 -14.188 47.543 1.00 39.21 ? 79 ILE E CD1 1 ATOM 7958 N N . VAL E 1 81 ? 22.060 -15.989 47.499 1.00 42.61 ? 80 VAL E N 1 ATOM 7959 C CA . VAL E 1 81 ? 20.719 -15.701 47.009 1.00 43.41 ? 80 VAL E CA 1 ATOM 7960 C C . VAL E 1 81 ? 20.327 -14.262 47.318 1.00 43.24 ? 80 VAL E C 1 ATOM 7961 O O . VAL E 1 81 ? 20.379 -13.831 48.464 1.00 43.08 ? 80 VAL E O 1 ATOM 7962 C CB . VAL E 1 81 ? 19.678 -16.607 47.686 1.00 45.29 ? 80 VAL E CB 1 ATOM 7963 C CG1 . VAL E 1 81 ? 18.264 -16.196 47.279 1.00 46.28 ? 80 VAL E CG1 1 ATOM 7964 C CG2 . VAL E 1 81 ? 19.952 -18.069 47.352 1.00 45.88 ? 80 VAL E CG2 1 ATOM 7965 N N . GLU E 1 82 ? 19.891 -13.543 46.295 1.00 43.61 ? 81 GLU E N 1 ATOM 7966 C CA . GLU E 1 82 ? 19.461 -12.163 46.446 1.00 44.24 ? 81 GLU E CA 1 ATOM 7967 C C . GLU E 1 82 ? 18.113 -11.977 45.766 1.00 45.39 ? 81 GLU E C 1 ATOM 7968 O O . GLU E 1 82 ? 17.825 -12.625 44.782 1.00 45.65 ? 81 GLU E O 1 ATOM 7969 C CB . GLU E 1 82 ? 20.497 -11.246 45.812 1.00 43.87 ? 81 GLU E CB 1 ATOM 7970 C CG . GLU E 1 82 ? 20.298 -9.764 46.064 1.00 44.10 ? 81 GLU E CG 1 ATOM 7971 C CD . GLU E 1 82 ? 21.382 -8.942 45.400 1.00 44.12 ? 81 GLU E CD 1 ATOM 7972 O OE1 . GLU E 1 82 ? 21.566 -9.087 44.172 1.00 44.79 ? 81 GLU E OE1 1 ATOM 7973 O OE2 . GLU E 1 82 ? 22.058 -8.157 46.100 1.00 44.05 ? 81 GLU E OE2 1 ATOM 7974 N N . LYS E 1 83 ? 17.286 -11.089 46.298 1.00 46.67 ? 82 LYS E N 1 ATOM 7975 C CA . LYS E 1 83 ? 16.014 -10.770 45.661 1.00 48.26 ? 82 LYS E CA 1 ATOM 7976 C C . LYS E 1 83 ? 16.212 -9.866 44.440 1.00 47.64 ? 82 LYS E C 1 ATOM 7977 O O . LYS E 1 83 ? 17.251 -9.218 44.299 1.00 46.08 ? 82 LYS E O 1 ATOM 7978 C CB . LYS E 1 83 ? 15.057 -10.147 46.675 1.00 50.04 ? 82 LYS E CB 1 ATOM 7979 C CG . LYS E 1 83 ? 14.605 -11.140 47.730 1.00 51.45 ? 82 LYS E CG 1 ATOM 7980 C CD . LYS E 1 83 ? 13.505 -10.586 48.622 1.00 54.13 ? 82 LYS E CD 1 ATOM 7981 C CE . LYS E 1 83 ? 12.729 -11.716 49.286 1.00 56.61 ? 82 LYS E CE 1 ATOM 7982 N NZ . LYS E 1 83 ? 13.594 -12.617 50.094 1.00 55.93 ? 82 LYS E NZ 1 ATOM 7983 N N . ILE E 1 84 ? 15.206 -9.827 43.571 1.00 49.09 ? 83 ILE E N 1 ATOM 7984 C CA . ILE E 1 84 ? 15.282 -9.068 42.323 1.00 49.41 ? 83 ILE E CA 1 ATOM 7985 C C . ILE E 1 84 ? 15.343 -7.575 42.586 1.00 49.37 ? 83 ILE E C 1 ATOM 7986 O O . ILE E 1 84 ? 16.081 -6.855 41.913 1.00 48.96 ? 83 ILE E O 1 ATOM 7987 C CB . ILE E 1 84 ? 14.086 -9.365 41.389 1.00 51.88 ? 83 ILE E CB 1 ATOM 7988 C CG1 . ILE E 1 84 ? 14.180 -10.797 40.830 1.00 51.93 ? 83 ILE E CG1 1 ATOM 7989 C CG2 . ILE E 1 84 ? 14.037 -8.365 40.241 1.00 52.87 ? 83 ILE E CG2 1 ATOM 7990 C CD1 . ILE E 1 84 ? 13.522 -11.853 41.702 1.00 52.97 ? 83 ILE E CD1 1 ATOM 7991 N N . ASN E 1 85 ? 14.553 -7.109 43.545 1.00 50.02 ? 84 ASN E N 1 ATOM 7992 C CA . ASN E 1 85 ? 14.605 -5.711 43.953 1.00 50.19 ? 84 ASN E CA 1 ATOM 7993 C C . ASN E 1 85 ? 14.588 -5.603 45.484 1.00 49.30 ? 84 ASN E C 1 ATOM 7994 O O . ASN E 1 85 ? 13.530 -5.415 46.078 1.00 51.27 ? 84 ASN E O 1 ATOM 7995 C CB . ASN E 1 85 ? 13.450 -4.928 43.319 1.00 53.06 ? 84 ASN E CB 1 ATOM 7996 C CG . ASN E 1 85 ? 13.522 -3.435 43.614 1.00 53.80 ? 84 ASN E CG 1 ATOM 7997 O OD1 . ASN E 1 85 ? 14.602 -2.852 43.696 1.00 51.95 ? 84 ASN E OD1 1 ATOM 7998 N ND2 . ASN E 1 85 ? 12.361 -2.810 43.772 1.00 56.85 ? 84 ASN E ND2 1 ATOM 7999 N N . PRO E 1 86 ? 15.765 -5.740 46.125 1.00 46.63 ? 85 PRO E N 1 ATOM 8000 C CA . PRO E 1 86 ? 15.833 -5.756 47.598 1.00 46.35 ? 85 PRO E CA 1 ATOM 8001 C C . PRO E 1 86 ? 15.594 -4.399 48.250 1.00 46.85 ? 85 PRO E C 1 ATOM 8002 O O . PRO E 1 86 ? 16.028 -3.381 47.727 1.00 45.68 ? 85 PRO E O 1 ATOM 8003 C CB . PRO E 1 86 ? 17.257 -6.252 47.905 1.00 44.02 ? 85 PRO E CB 1 ATOM 8004 C CG . PRO E 1 86 ? 17.961 -6.401 46.598 1.00 43.07 ? 85 PRO E CG 1 ATOM 8005 C CD . PRO E 1 86 ? 17.084 -5.903 45.492 1.00 44.61 ? 85 PRO E CD 1 ATOM 8006 N N . ALA E 1 87 ? 14.925 -4.406 49.400 1.00 38.88 ? 86 ALA E N 1 ATOM 8007 C CA . ALA E 1 87 ? 14.597 -3.177 50.129 1.00 39.33 ? 86 ALA E CA 1 ATOM 8008 C C . ALA E 1 87 ? 15.818 -2.497 50.742 1.00 38.05 ? 86 ALA E C 1 ATOM 8009 O O . ALA E 1 87 ? 15.933 -1.273 50.699 1.00 38.19 ? 86 ALA E O 1 ATOM 8010 C CB . ALA E 1 87 ? 13.582 -3.472 51.224 1.00 41.18 ? 86 ALA E CB 1 ATOM 8011 N N . ASN E 1 88 ? 16.714 -3.279 51.333 1.00 37.37 ? 87 ASN E N 1 ATOM 8012 C CA . ASN E 1 88 ? 17.837 -2.710 52.073 1.00 36.40 ? 87 ASN E CA 1 ATOM 8013 C C . ASN E 1 88 ? 19.098 -2.721 51.214 1.00 35.04 ? 87 ASN E C 1 ATOM 8014 O O . ASN E 1 88 ? 19.766 -3.763 51.065 1.00 34.43 ? 87 ASN E O 1 ATOM 8015 C CB . ASN E 1 88 ? 18.059 -3.471 53.375 1.00 37.38 ? 87 ASN E CB 1 ATOM 8016 C CG . ASN E 1 88 ? 16.812 -3.546 54.234 1.00 39.08 ? 87 ASN E CG 1 ATOM 8017 O OD1 . ASN E 1 88 ? 16.483 -4.605 54.763 1.00 40.25 ? 87 ASN E OD1 1 ATOM 8018 N ND2 . ASN E 1 88 ? 16.123 -2.425 54.388 1.00 39.30 ? 87 ASN E ND2 1 ATOM 8019 N N . ASP E 1 89 ? 19.390 -1.556 50.639 1.00 34.07 ? 88 ASP E N 1 ATOM 8020 C CA . ASP E 1 89 ? 20.470 -1.376 49.680 1.00 33.15 ? 88 ASP E CA 1 ATOM 8021 C C . ASP E 1 89 ? 21.330 -0.185 50.153 1.00 32.32 ? 88 ASP E C 1 ATOM 8022 O O . ASP E 1 89 ? 21.841 -0.215 51.262 1.00 32.00 ? 88 ASP E O 1 ATOM 8023 C CB . ASP E 1 89 ? 19.862 -1.173 48.276 1.00 33.24 ? 88 ASP E CB 1 ATOM 8024 C CG . ASP E 1 89 ? 20.914 -1.087 47.182 1.00 32.30 ? 88 ASP E CG 1 ATOM 8025 O OD1 . ASP E 1 89 ? 21.706 -2.036 47.038 1.00 31.85 ? 88 ASP E OD1 1 ATOM 8026 O OD2 . ASP E 1 89 ? 20.958 -0.054 46.478 1.00 32.51 ? 88 ASP E OD2 1 ATOM 8027 N N . LEU E 1 90 ? 21.479 0.858 49.341 1.00 31.89 ? 89 LEU E N 1 ATOM 8028 C CA . LEU E 1 90 ? 22.168 2.065 49.772 1.00 32.04 ? 89 LEU E CA 1 ATOM 8029 C C . LEU E 1 90 ? 21.177 2.928 50.519 1.00 33.06 ? 89 LEU E C 1 ATOM 8030 O O . LEU E 1 90 ? 20.426 3.686 49.903 1.00 34.42 ? 89 LEU E O 1 ATOM 8031 C CB . LEU E 1 90 ? 22.722 2.841 48.567 1.00 31.43 ? 89 LEU E CB 1 ATOM 8032 C CG . LEU E 1 90 ? 23.677 2.065 47.666 1.00 30.75 ? 89 LEU E CG 1 ATOM 8033 C CD1 . LEU E 1 90 ? 24.075 2.917 46.476 1.00 30.36 ? 89 LEU E CD1 1 ATOM 8034 C CD2 . LEU E 1 90 ? 24.898 1.619 48.461 1.00 30.63 ? 89 LEU E CD2 1 ATOM 8035 N N . CYS E 1 91 ? 21.176 2.820 51.843 1.00 33.91 ? 90 CYS E N 1 ATOM 8036 C CA . CYS E 1 91 ? 20.214 3.544 52.655 1.00 35.18 ? 90 CYS E CA 1 ATOM 8037 C C . CYS E 1 91 ? 20.382 5.039 52.401 1.00 33.37 ? 90 CYS E C 1 ATOM 8038 O O . CYS E 1 91 ? 19.423 5.728 52.057 1.00 33.54 ? 90 CYS E O 1 ATOM 8039 C CB . CYS E 1 91 ? 20.318 3.191 54.154 1.00 37.54 ? 90 CYS E CB 1 ATOM 8040 S SG . CYS E 1 91 ? 21.940 3.349 54.960 1.00 39.08 ? 90 CYS E SG 1 ATOM 8041 N N . TYR E 1 92 ? 21.602 5.532 52.575 1.00 31.13 ? 91 TYR E N 1 ATOM 8042 C CA . TYR E 1 92 ? 21.938 6.857 52.082 1.00 29.62 ? 91 TYR E CA 1 ATOM 8043 C C . TYR E 1 92 ? 22.097 6.714 50.568 1.00 28.26 ? 91 TYR E C 1 ATOM 8044 O O . TYR E 1 92 ? 22.829 5.833 50.105 1.00 27.30 ? 91 TYR E O 1 ATOM 8045 C CB . TYR E 1 92 ? 23.214 7.378 52.736 1.00 28.61 ? 91 TYR E CB 1 ATOM 8046 C CG . TYR E 1 92 ? 23.324 8.876 52.703 1.00 28.24 ? 91 TYR E CG 1 ATOM 8047 C CD1 . TYR E 1 92 ? 23.700 9.539 51.542 1.00 27.18 ? 91 TYR E CD1 1 ATOM 8048 C CD2 . TYR E 1 92 ? 23.053 9.638 53.829 1.00 29.06 ? 91 TYR E CD2 1 ATOM 8049 C CE1 . TYR E 1 92 ? 23.810 10.906 51.505 1.00 26.93 ? 91 TYR E CE1 1 ATOM 8050 C CE2 . TYR E 1 92 ? 23.150 11.013 53.796 1.00 28.99 ? 91 TYR E CE2 1 ATOM 8051 C CZ . TYR E 1 92 ? 23.529 11.637 52.624 1.00 27.97 ? 91 TYR E CZ 1 ATOM 8052 O OH . TYR E 1 92 ? 23.636 13.003 52.582 1.00 28.09 ? 91 TYR E OH 1 ATOM 8053 N N . PRO E 1 93 ? 21.392 7.552 49.791 1.00 28.12 ? 92 PRO E N 1 ATOM 8054 C CA . PRO E 1 93 ? 21.378 7.320 48.355 1.00 27.81 ? 92 PRO E CA 1 ATOM 8055 C C . PRO E 1 93 ? 22.728 7.618 47.689 1.00 27.56 ? 92 PRO E C 1 ATOM 8056 O O . PRO E 1 93 ? 23.598 8.246 48.285 1.00 27.49 ? 92 PRO E O 1 ATOM 8057 C CB . PRO E 1 93 ? 20.299 8.283 47.860 1.00 28.45 ? 92 PRO E CB 1 ATOM 8058 C CG . PRO E 1 93 ? 20.349 9.416 48.816 1.00 28.79 ? 92 PRO E CG 1 ATOM 8059 C CD . PRO E 1 93 ? 20.662 8.780 50.154 1.00 29.11 ? 92 PRO E CD 1 ATOM 8060 N N . GLY E 1 94 ? 22.886 7.174 46.453 1.00 28.08 ? 93 GLY E N 1 ATOM 8061 C CA . GLY E 1 94 ? 24.116 7.400 45.695 1.00 28.12 ? 93 GLY E CA 1 ATOM 8062 C C . GLY E 1 94 ? 24.396 6.183 44.843 1.00 28.35 ? 93 GLY E C 1 ATOM 8063 O O . GLY E 1 94 ? 23.467 5.564 44.338 1.00 28.52 ? 93 GLY E O 1 ATOM 8064 N N . ASN E 1 95 ? 25.669 5.831 44.691 1.00 28.56 ? 94 ASN E N 1 ATOM 8065 C CA . ASN E 1 95 ? 26.036 4.685 43.880 1.00 29.05 ? 94 ASN E CA 1 ATOM 8066 C C . ASN E 1 95 ? 27.248 3.913 44.370 1.00 28.68 ? 94 ASN E C 1 ATOM 8067 O O . ASN E 1 95 ? 28.107 4.428 45.074 1.00 27.54 ? 94 ASN E O 1 ATOM 8068 C CB . ASN E 1 95 ? 26.240 5.099 42.416 1.00 30.79 ? 94 ASN E CB 1 ATOM 8069 C CG . ASN E 1 95 ? 27.119 6.327 42.268 1.00 32.58 ? 94 ASN E CG 1 ATOM 8070 O OD1 . ASN E 1 95 ? 27.354 7.073 43.227 1.00 33.70 ? 94 ASN E OD1 1 ATOM 8071 N ND2 . ASN E 1 95 ? 27.621 6.545 41.063 1.00 34.54 ? 94 ASN E ND2 1 ATOM 8072 N N . PHE E 1 96 ? 27.279 2.645 43.975 1.00 29.22 ? 95 PHE E N 1 ATOM 8073 C CA . PHE E 1 96 ? 28.383 1.764 44.211 1.00 29.31 ? 95 PHE E CA 1 ATOM 8074 C C . PHE E 1 96 ? 29.120 1.637 42.880 1.00 29.56 ? 95 PHE E C 1 ATOM 8075 O O . PHE E 1 96 ? 28.598 1.074 41.912 1.00 31.20 ? 95 PHE E O 1 ATOM 8076 C CB . PHE E 1 96 ? 27.843 0.427 44.663 1.00 30.70 ? 95 PHE E CB 1 ATOM 8077 C CG . PHE E 1 96 ? 28.780 -0.349 45.526 1.00 31.60 ? 95 PHE E CG 1 ATOM 8078 C CD1 . PHE E 1 96 ? 29.948 -0.878 45.000 1.00 32.93 ? 95 PHE E CD1 1 ATOM 8079 C CD2 . PHE E 1 96 ? 28.491 -0.563 46.851 1.00 31.82 ? 95 PHE E CD2 1 ATOM 8080 C CE1 . PHE E 1 96 ? 30.813 -1.602 45.798 1.00 33.32 ? 95 PHE E CE1 1 ATOM 8081 C CE2 . PHE E 1 96 ? 29.346 -1.292 47.646 1.00 32.73 ? 95 PHE E CE2 1 ATOM 8082 C CZ . PHE E 1 96 ? 30.512 -1.806 47.126 1.00 32.82 ? 95 PHE E CZ 1 ATOM 8083 N N . ASN E 1 97 ? 30.323 2.192 42.824 1.00 28.27 ? 96 ASN E N 1 ATOM 8084 C CA . ASN E 1 97 ? 31.142 2.141 41.633 1.00 28.22 ? 96 ASN E CA 1 ATOM 8085 C C . ASN E 1 97 ? 31.611 0.743 41.263 1.00 28.00 ? 96 ASN E C 1 ATOM 8086 O O . ASN E 1 97 ? 32.035 -0.032 42.113 1.00 27.27 ? 96 ASN E O 1 ATOM 8087 C CB . ASN E 1 97 ? 32.366 3.018 41.835 1.00 28.76 ? 96 ASN E CB 1 ATOM 8088 C CG . ASN E 1 97 ? 32.977 3.446 40.539 1.00 30.09 ? 96 ASN E CG 1 ATOM 8089 O OD1 . ASN E 1 97 ? 33.959 2.848 40.081 1.00 32.26 ? 96 ASN E OD1 1 ATOM 8090 N ND2 . ASN E 1 97 ? 32.400 4.474 39.922 1.00 29.97 ? 96 ASN E ND2 1 ATOM 8091 N N . ASP E 1 98 ? 31.551 0.434 39.980 1.00 28.75 ? 97 ASP E N 1 ATOM 8092 C CA . ASP E 1 98 ? 31.976 -0.868 39.467 1.00 29.39 ? 97 ASP E CA 1 ATOM 8093 C C . ASP E 1 98 ? 31.297 -2.008 40.188 1.00 28.85 ? 97 ASP E C 1 ATOM 8094 O O . ASP E 1 98 ? 31.906 -3.055 40.416 1.00 29.13 ? 97 ASP E O 1 ATOM 8095 C CB . ASP E 1 98 ? 33.510 -0.994 39.503 1.00 29.80 ? 97 ASP E CB 1 ATOM 8096 C CG . ASP E 1 98 ? 34.172 -0.164 38.414 1.00 31.11 ? 97 ASP E CG 1 ATOM 8097 O OD1 . ASP E 1 98 ? 33.678 -0.212 37.278 1.00 31.43 ? 97 ASP E OD1 1 ATOM 8098 O OD2 . ASP E 1 98 ? 35.168 0.549 38.684 1.00 32.01 ? 97 ASP E OD2 1 ATOM 8099 N N . TYR E 1 99 ? 30.012 -1.808 40.490 1.00 28.21 ? 98 TYR E N 1 ATOM 8100 C CA . TYR E 1 99 ? 29.225 -2.743 41.317 1.00 27.82 ? 98 TYR E CA 1 ATOM 8101 C C . TYR E 1 99 ? 29.091 -4.138 40.735 1.00 28.15 ? 98 TYR E C 1 ATOM 8102 O O . TYR E 1 99 ? 29.190 -5.116 41.456 1.00 27.66 ? 98 TYR E O 1 ATOM 8103 C CB . TYR E 1 99 ? 27.820 -2.174 41.554 1.00 27.89 ? 98 TYR E CB 1 ATOM 8104 C CG . TYR E 1 99 ? 26.947 -2.924 42.548 1.00 28.10 ? 98 TYR E CG 1 ATOM 8105 C CD1 . TYR E 1 99 ? 27.439 -3.319 43.784 1.00 27.83 ? 98 TYR E CD1 1 ATOM 8106 C CD2 . TYR E 1 99 ? 25.596 -3.196 42.261 1.00 28.80 ? 98 TYR E CD2 1 ATOM 8107 C CE1 . TYR E 1 99 ? 26.631 -3.991 44.698 1.00 28.21 ? 98 TYR E CE1 1 ATOM 8108 C CE2 . TYR E 1 99 ? 24.781 -3.850 43.172 1.00 28.72 ? 98 TYR E CE2 1 ATOM 8109 C CZ . TYR E 1 99 ? 25.300 -4.245 44.388 1.00 28.72 ? 98 TYR E CZ 1 ATOM 8110 O OH . TYR E 1 99 ? 24.492 -4.879 45.316 1.00 29.50 ? 98 TYR E OH 1 ATOM 8111 N N . GLU E 1 100 ? 28.855 -4.223 39.435 1.00 29.30 ? 99 GLU E N 1 ATOM 8112 C CA . GLU E 1 100 ? 28.583 -5.511 38.797 1.00 30.40 ? 99 GLU E CA 1 ATOM 8113 C C . GLU E 1 100 ? 29.887 -6.288 38.640 1.00 30.68 ? 99 GLU E C 1 ATOM 8114 O O . GLU E 1 100 ? 29.895 -7.519 38.687 1.00 30.74 ? 99 GLU E O 1 ATOM 8115 C CB . GLU E 1 100 ? 27.893 -5.325 37.438 1.00 32.02 ? 99 GLU E CB 1 ATOM 8116 C CG . GLU E 1 100 ? 26.524 -4.660 37.499 1.00 32.31 ? 99 GLU E CG 1 ATOM 8117 C CD . GLU E 1 100 ? 26.605 -3.201 37.906 1.00 32.57 ? 99 GLU E CD 1 ATOM 8118 O OE1 . GLU E 1 100 ? 27.545 -2.499 37.471 1.00 33.70 ? 99 GLU E OE1 1 ATOM 8119 O OE2 . GLU E 1 100 ? 25.744 -2.746 38.688 1.00 33.32 ? 99 GLU E OE2 1 ATOM 8120 N N . GLU E 1 101 ? 30.991 -5.565 38.450 1.00 30.63 ? 100 GLU E N 1 ATOM 8121 C CA . GLU E 1 101 ? 32.324 -6.193 38.452 1.00 31.21 ? 100 GLU E CA 1 ATOM 8122 C C . GLU E 1 101 ? 32.688 -6.724 39.852 1.00 30.46 ? 100 GLU E C 1 ATOM 8123 O O . GLU E 1 101 ? 33.262 -7.812 39.989 1.00 30.79 ? 100 GLU E O 1 ATOM 8124 C CB . GLU E 1 101 ? 33.402 -5.227 37.922 1.00 30.90 ? 100 GLU E CB 1 ATOM 8125 C CG . GLU E 1 101 ? 33.305 -4.967 36.437 1.00 31.88 ? 100 GLU E CG 1 ATOM 8126 C CD . GLU E 1 101 ? 33.792 -6.139 35.585 1.00 33.02 ? 100 GLU E CD 1 ATOM 8127 O OE1 . GLU E 1 101 ? 34.805 -6.761 35.957 1.00 32.99 ? 100 GLU E OE1 1 ATOM 8128 O OE2 . GLU E 1 101 ? 33.174 -6.424 34.534 1.00 33.38 ? 100 GLU E OE2 1 ATOM 8129 N N . LEU E 1 102 ? 32.326 -5.981 40.888 1.00 29.98 ? 101 LEU E N 1 ATOM 8130 C CA . LEU E 1 102 ? 32.471 -6.499 42.270 1.00 30.19 ? 101 LEU E CA 1 ATOM 8131 C C . LEU E 1 102 ? 31.632 -7.755 42.465 1.00 31.19 ? 101 LEU E C 1 ATOM 8132 O O . LEU E 1 102 ? 32.106 -8.760 43.015 1.00 31.72 ? 101 LEU E O 1 ATOM 8133 C CB . LEU E 1 102 ? 32.061 -5.474 43.308 1.00 29.11 ? 101 LEU E CB 1 ATOM 8134 C CG . LEU E 1 102 ? 32.102 -5.930 44.779 1.00 29.37 ? 101 LEU E CG 1 ATOM 8135 C CD1 . LEU E 1 102 ? 33.388 -6.648 45.138 1.00 29.94 ? 101 LEU E CD1 1 ATOM 8136 C CD2 . LEU E 1 102 ? 31.899 -4.718 45.688 1.00 28.97 ? 101 LEU E CD2 1 ATOM 8137 N N . LYS E 1 103 ? 30.385 -7.692 42.007 1.00 31.53 ? 102 LYS E N 1 ATOM 8138 C CA . LYS E 1 103 ? 29.495 -8.838 42.086 1.00 32.69 ? 102 LYS E CA 1 ATOM 8139 C C . LYS E 1 103 ? 30.064 -10.031 41.350 1.00 33.99 ? 102 LYS E C 1 ATOM 8140 O O . LYS E 1 103 ? 29.934 -11.153 41.831 1.00 34.80 ? 102 LYS E O 1 ATOM 8141 C CB . LYS E 1 103 ? 28.106 -8.485 41.567 1.00 33.09 ? 102 LYS E CB 1 ATOM 8142 C CG . LYS E 1 103 ? 27.346 -7.598 42.536 1.00 32.76 ? 102 LYS E CG 1 ATOM 8143 C CD . LYS E 1 103 ? 26.024 -7.115 41.963 1.00 33.63 ? 102 LYS E CD 1 ATOM 8144 C CE . LYS E 1 103 ? 24.867 -7.994 42.411 1.00 34.64 ? 102 LYS E CE 1 ATOM 8145 N NZ . LYS E 1 103 ? 23.553 -7.378 42.082 1.00 35.35 ? 102 LYS E NZ 1 ATOM 8146 N N . HIS E 1 104 ? 30.713 -9.790 40.203 1.00 34.60 ? 103 HIS E N 1 ATOM 8147 C CA . HIS E 1 104 ? 31.315 -10.867 39.413 1.00 35.49 ? 103 HIS E CA 1 ATOM 8148 C C . HIS E 1 104 ? 32.429 -11.572 40.187 1.00 36.67 ? 103 HIS E C 1 ATOM 8149 O O . HIS E 1 104 ? 32.498 -12.787 40.183 1.00 37.44 ? 103 HIS E O 1 ATOM 8150 C CB . HIS E 1 104 ? 31.824 -10.347 38.060 1.00 35.78 ? 103 HIS E CB 1 ATOM 8151 C CG . HIS E 1 104 ? 32.554 -11.379 37.251 1.00 36.59 ? 103 HIS E CG 1 ATOM 8152 N ND1 . HIS E 1 104 ? 31.922 -12.201 36.346 1.00 37.70 ? 103 HIS E ND1 1 ATOM 8153 C CD2 . HIS E 1 104 ? 33.862 -11.726 37.224 1.00 36.82 ? 103 HIS E CD2 1 ATOM 8154 C CE1 . HIS E 1 104 ? 32.810 -13.010 35.797 1.00 38.97 ? 103 HIS E CE1 1 ATOM 8155 N NE2 . HIS E 1 104 ? 33.993 -12.745 36.317 1.00 38.44 ? 103 HIS E NE2 1 ATOM 8156 N N . LEU E 1 105 ? 33.291 -10.812 40.857 1.00 37.74 ? 104 LEU E N 1 ATOM 8157 C CA . LEU E 1 105 ? 34.291 -11.395 41.774 1.00 39.35 ? 104 LEU E CA 1 ATOM 8158 C C . LEU E 1 105 ? 33.638 -12.208 42.881 1.00 40.01 ? 104 LEU E C 1 ATOM 8159 O O . LEU E 1 105 ? 34.141 -13.251 43.275 1.00 41.65 ? 104 LEU E O 1 ATOM 8160 C CB . LEU E 1 105 ? 35.153 -10.308 42.431 1.00 38.80 ? 104 LEU E CB 1 ATOM 8161 C CG . LEU E 1 105 ? 36.065 -9.506 41.505 1.00 39.54 ? 104 LEU E CG 1 ATOM 8162 C CD1 . LEU E 1 105 ? 36.834 -8.463 42.299 1.00 39.22 ? 104 LEU E CD1 1 ATOM 8163 C CD2 . LEU E 1 105 ? 37.011 -10.433 40.744 1.00 41.12 ? 104 LEU E CD2 1 ATOM 8164 N N . LEU E 1 106 ? 32.511 -11.719 43.372 1.00 40.25 ? 105 LEU E N 1 ATOM 8165 C CA . LEU E 1 106 ? 31.829 -12.331 44.502 1.00 41.41 ? 105 LEU E CA 1 ATOM 8166 C C . LEU E 1 106 ? 31.281 -13.712 44.180 1.00 43.50 ? 105 LEU E C 1 ATOM 8167 O O . LEU E 1 106 ? 31.078 -14.517 45.090 1.00 45.71 ? 105 LEU E O 1 ATOM 8168 C CB . LEU E 1 106 ? 30.702 -11.416 44.975 1.00 40.57 ? 105 LEU E CB 1 ATOM 8169 C CG . LEU E 1 106 ? 30.078 -11.685 46.330 1.00 40.98 ? 105 LEU E CG 1 ATOM 8170 C CD1 . LEU E 1 106 ? 31.126 -11.604 47.425 1.00 41.64 ? 105 LEU E CD1 1 ATOM 8171 C CD2 . LEU E 1 106 ? 28.964 -10.678 46.569 1.00 40.28 ? 105 LEU E CD2 1 ATOM 8172 N N . SER E 1 107 ? 31.059 -13.992 42.897 1.00 44.37 ? 106 SER E N 1 ATOM 8173 C CA . SER E 1 107 ? 30.593 -15.308 42.459 1.00 46.42 ? 106 SER E CA 1 ATOM 8174 C C . SER E 1 107 ? 31.720 -16.341 42.361 1.00 48.19 ? 106 SER E C 1 ATOM 8175 O O . SER E 1 107 ? 31.481 -17.490 41.988 1.00 48.90 ? 106 SER E O 1 ATOM 8176 C CB . SER E 1 107 ? 29.894 -15.185 41.107 1.00 46.96 ? 106 SER E CB 1 ATOM 8177 O OG . SER E 1 107 ? 30.821 -14.843 40.091 1.00 48.10 ? 106 SER E OG 1 ATOM 8178 N N . ARG E 1 108 ? 32.943 -15.931 42.683 1.00 48.91 ? 107 ARG E N 1 ATOM 8179 C CA . ARG E 1 108 ? 34.084 -16.846 42.745 1.00 51.12 ? 107 ARG E CA 1 ATOM 8180 C C . ARG E 1 108 ? 34.585 -16.956 44.196 1.00 48.83 ? 107 ARG E C 1 ATOM 8181 O O . ARG E 1 108 ? 35.649 -17.516 44.442 1.00 48.94 ? 107 ARG E O 1 ATOM 8182 C CB . ARG E 1 108 ? 35.226 -16.344 41.845 1.00 54.16 ? 107 ARG E CB 1 ATOM 8183 C CG . ARG E 1 108 ? 34.798 -15.513 40.631 1.00 56.56 ? 107 ARG E CG 1 ATOM 8184 C CD . ARG E 1 108 ? 34.523 -16.364 39.399 1.00 61.09 ? 107 ARG E CD 1 ATOM 8185 N NE . ARG E 1 108 ? 33.321 -15.947 38.663 1.00 62.82 ? 107 ARG E NE 1 ATOM 8186 C CZ . ARG E 1 108 ? 33.036 -16.309 37.409 1.00 65.37 ? 107 ARG E CZ 1 ATOM 8187 N NH1 . ARG E 1 108 ? 33.869 -17.079 36.713 1.00 66.56 ? 107 ARG E NH1 1 ATOM 8188 N NH2 . ARG E 1 108 ? 31.912 -15.884 36.837 1.00 66.08 ? 107 ARG E NH2 1 ATOM 8189 N N . ILE E 1 109 ? 33.828 -16.393 45.144 1.00 45.77 ? 108 ILE E N 1 ATOM 8190 C CA . ILE E 1 109 ? 34.225 -16.348 46.551 1.00 44.60 ? 108 ILE E CA 1 ATOM 8191 C C . ILE E 1 109 ? 33.178 -17.060 47.426 1.00 44.83 ? 108 ILE E C 1 ATOM 8192 O O . ILE E 1 109 ? 31.968 -16.873 47.256 1.00 43.63 ? 108 ILE E O 1 ATOM 8193 C CB . ILE E 1 109 ? 34.437 -14.889 47.015 1.00 42.51 ? 108 ILE E CB 1 ATOM 8194 C CG1 . ILE E 1 109 ? 35.636 -14.269 46.285 1.00 41.79 ? 108 ILE E CG1 1 ATOM 8195 C CG2 . ILE E 1 109 ? 34.641 -14.807 48.524 1.00 42.53 ? 108 ILE E CG2 1 ATOM 8196 C CD1 . ILE E 1 109 ? 35.658 -12.754 46.288 1.00 40.12 ? 108 ILE E CD1 1 ATOM 8197 N N . ASN E 1 110 ? 33.667 -17.875 48.355 1.00 46.28 ? 109 ASN E N 1 ATOM 8198 C CA . ASN E 1 110 ? 32.823 -18.697 49.229 1.00 47.78 ? 109 ASN E CA 1 ATOM 8199 C C . ASN E 1 110 ? 32.830 -18.270 50.698 1.00 47.26 ? 109 ASN E C 1 ATOM 8200 O O . ASN E 1 110 ? 31.991 -18.729 51.472 1.00 47.70 ? 109 ASN E O 1 ATOM 8201 C CB . ASN E 1 110 ? 33.273 -20.159 49.152 1.00 50.14 ? 109 ASN E CB 1 ATOM 8202 C CG . ASN E 1 110 ? 33.085 -20.752 47.775 1.00 50.97 ? 109 ASN E CG 1 ATOM 8203 O OD1 . ASN E 1 110 ? 34.055 -21.043 47.075 1.00 52.55 ? 109 ASN E OD1 1 ATOM 8204 N ND2 . ASN E 1 110 ? 31.833 -20.931 47.372 1.00 51.00 ? 109 ASN E ND2 1 ATOM 8205 N N . HIS E 1 111 ? 33.786 -17.430 51.087 1.00 46.27 ? 110 HIS E N 1 ATOM 8206 C CA . HIS E 1 111 ? 33.871 -16.962 52.466 1.00 46.89 ? 110 HIS E CA 1 ATOM 8207 C C . HIS E 1 111 ? 34.754 -15.715 52.633 1.00 45.91 ? 110 HIS E C 1 ATOM 8208 O O . HIS E 1 111 ? 35.825 -15.607 52.017 1.00 45.80 ? 110 HIS E O 1 ATOM 8209 C CB . HIS E 1 111 ? 34.371 -18.077 53.390 1.00 48.97 ? 110 HIS E CB 1 ATOM 8210 C CG . HIS E 1 111 ? 34.121 -17.812 54.843 1.00 50.17 ? 110 HIS E CG 1 ATOM 8211 N ND1 . HIS E 1 111 ? 34.881 -18.377 55.844 1.00 52.24 ? 110 HIS E ND1 1 ATOM 8212 C CD2 . HIS E 1 111 ? 33.201 -17.035 55.464 1.00 49.45 ? 110 HIS E CD2 1 ATOM 8213 C CE1 . HIS E 1 111 ? 34.437 -17.963 57.019 1.00 52.97 ? 110 HIS E CE1 1 ATOM 8214 N NE2 . HIS E 1 111 ? 33.421 -17.144 56.816 1.00 51.14 ? 110 HIS E NE2 1 ATOM 8215 N N . PHE E 1 112 ? 34.268 -14.783 53.457 1.00 44.92 ? 111 PHE E N 1 ATOM 8216 C CA . PHE E 1 112 ? 35.036 -13.628 53.922 1.00 44.37 ? 111 PHE E CA 1 ATOM 8217 C C . PHE E 1 112 ? 35.312 -13.751 55.413 1.00 46.38 ? 111 PHE E C 1 ATOM 8218 O O . PHE E 1 112 ? 34.500 -14.300 56.167 1.00 47.64 ? 111 PHE E O 1 ATOM 8219 C CB . PHE E 1 112 ? 34.255 -12.327 53.751 1.00 42.08 ? 111 PHE E CB 1 ATOM 8220 C CG . PHE E 1 112 ? 34.132 -11.855 52.343 1.00 40.44 ? 111 PHE E CG 1 ATOM 8221 C CD1 . PHE E 1 112 ? 35.254 -11.527 51.604 1.00 40.08 ? 111 PHE E CD1 1 ATOM 8222 C CD2 . PHE E 1 112 ? 32.883 -11.684 51.770 1.00 39.74 ? 111 PHE E CD2 1 ATOM 8223 C CE1 . PHE E 1 112 ? 35.135 -11.075 50.304 1.00 39.21 ? 111 PHE E CE1 1 ATOM 8224 C CE2 . PHE E 1 112 ? 32.755 -11.226 50.474 1.00 38.63 ? 111 PHE E CE2 1 ATOM 8225 C CZ . PHE E 1 112 ? 33.882 -10.925 49.734 1.00 38.36 ? 111 PHE E CZ 1 ATOM 8226 N N . GLU E 1 113 ? 36.447 -13.209 55.839 1.00 46.79 ? 112 GLU E N 1 ATOM 8227 C CA . GLU E 1 113 ? 36.674 -12.919 57.241 1.00 48.14 ? 112 GLU E CA 1 ATOM 8228 C C . GLU E 1 113 ? 36.799 -11.407 57.331 1.00 45.70 ? 112 GLU E C 1 ATOM 8229 O O . GLU E 1 113 ? 37.745 -10.832 56.807 1.00 44.44 ? 112 GLU E O 1 ATOM 8230 C CB . GLU E 1 113 ? 37.933 -13.624 57.758 1.00 51.56 ? 112 GLU E CB 1 ATOM 8231 C CG . GLU E 1 113 ? 38.099 -13.541 59.271 1.00 54.99 ? 112 GLU E CG 1 ATOM 8232 C CD . GLU E 1 113 ? 39.326 -14.275 59.801 1.00 58.82 ? 112 GLU E CD 1 ATOM 8233 O OE1 . GLU E 1 113 ? 39.600 -15.422 59.370 1.00 60.55 ? 112 GLU E OE1 1 ATOM 8234 O OE2 . GLU E 1 113 ? 40.017 -13.705 60.676 1.00 61.46 ? 112 GLU E OE2 1 ATOM 8235 N N . LYS E 1 114 ? 35.826 -10.760 57.965 1.00 44.96 ? 113 LYS E N 1 ATOM 8236 C CA . LYS E 1 114 ? 35.821 -9.297 58.066 1.00 43.14 ? 113 LYS E CA 1 ATOM 8237 C C . LYS E 1 114 ? 36.733 -8.882 59.202 1.00 44.07 ? 113 LYS E C 1 ATOM 8238 O O . LYS E 1 114 ? 36.617 -9.410 60.296 1.00 45.89 ? 113 LYS E O 1 ATOM 8239 C CB . LYS E 1 114 ? 34.408 -8.762 58.315 1.00 42.59 ? 113 LYS E CB 1 ATOM 8240 C CG . LYS E 1 114 ? 34.330 -7.245 58.301 1.00 41.60 ? 113 LYS E CG 1 ATOM 8241 C CD . LYS E 1 114 ? 32.904 -6.727 58.310 1.00 41.22 ? 113 LYS E CD 1 ATOM 8242 C CE . LYS E 1 114 ? 32.312 -6.725 59.703 1.00 43.56 ? 113 LYS E CE 1 ATOM 8243 N NZ . LYS E 1 114 ? 30.896 -6.262 59.667 1.00 43.74 ? 113 LYS E NZ 1 ATOM 8244 N N . ILE E 1 115 ? 37.630 -7.936 58.938 1.00 42.89 ? 114 ILE E N 1 ATOM 8245 C CA . ILE E 1 115 ? 38.589 -7.471 59.929 1.00 44.11 ? 114 ILE E CA 1 ATOM 8246 C C . ILE E 1 115 ? 38.583 -5.955 60.019 1.00 43.10 ? 114 ILE E C 1 ATOM 8247 O O . ILE E 1 115 ? 38.206 -5.280 59.084 1.00 41.15 ? 114 ILE E O 1 ATOM 8248 C CB . ILE E 1 115 ? 40.021 -7.976 59.634 1.00 44.93 ? 114 ILE E CB 1 ATOM 8249 C CG1 . ILE E 1 115 ? 40.635 -7.298 58.404 1.00 43.15 ? 114 ILE E CG1 1 ATOM 8250 C CG2 . ILE E 1 115 ? 40.021 -9.485 59.433 1.00 46.08 ? 114 ILE E CG2 1 ATOM 8251 C CD1 . ILE E 1 115 ? 42.100 -7.649 58.212 1.00 44.20 ? 114 ILE E CD1 1 ATOM 8252 N N . GLN E 1 116 ? 39.001 -5.434 61.164 1.00 45.29 ? 115 GLN E N 1 ATOM 8253 C CA . GLN E 1 116 ? 39.010 -4.001 61.416 1.00 45.07 ? 115 GLN E CA 1 ATOM 8254 C C . GLN E 1 116 ? 40.366 -3.440 61.020 1.00 44.95 ? 115 GLN E C 1 ATOM 8255 O O . GLN E 1 116 ? 41.363 -3.717 61.680 1.00 47.53 ? 115 GLN E O 1 ATOM 8256 C CB . GLN E 1 116 ? 38.759 -3.735 62.898 1.00 47.45 ? 115 GLN E CB 1 ATOM 8257 C CG . GLN E 1 116 ? 38.675 -2.261 63.245 1.00 47.51 ? 115 GLN E CG 1 ATOM 8258 C CD . GLN E 1 116 ? 38.552 -2.030 64.732 1.00 50.39 ? 115 GLN E CD 1 ATOM 8259 O OE1 . GLN E 1 116 ? 37.463 -1.789 65.246 1.00 51.05 ? 115 GLN E OE1 1 ATOM 8260 N NE2 . GLN E 1 116 ? 39.673 -2.110 65.433 1.00 52.45 ? 115 GLN E NE2 1 ATOM 8261 N N . ILE E 1 117 ? 40.405 -2.649 59.958 1.00 42.67 ? 116 ILE E N 1 ATOM 8262 C CA . ILE E 1 117 ? 41.666 -2.116 59.459 1.00 42.77 ? 116 ILE E CA 1 ATOM 8263 C C . ILE E 1 117 ? 41.906 -0.673 59.906 1.00 43.29 ? 116 ILE E C 1 ATOM 8264 O O . ILE E 1 117 ? 43.038 -0.205 59.870 1.00 44.14 ? 116 ILE E O 1 ATOM 8265 C CB . ILE E 1 117 ? 41.764 -2.223 57.922 1.00 40.73 ? 116 ILE E CB 1 ATOM 8266 C CG1 . ILE E 1 117 ? 40.705 -1.367 57.236 1.00 38.51 ? 116 ILE E CG1 1 ATOM 8267 C CG2 . ILE E 1 117 ? 41.617 -3.673 57.484 1.00 40.89 ? 116 ILE E CG2 1 ATOM 8268 C CD1 . ILE E 1 117 ? 40.940 -1.194 55.756 1.00 37.19 ? 116 ILE E CD1 1 ATOM 8269 N N . ILE E 1 118 ? 40.847 0.035 60.301 1.00 43.34 ? 117 ILE E N 1 ATOM 8270 C CA . ILE E 1 118 ? 40.974 1.390 60.865 1.00 43.94 ? 117 ILE E CA 1 ATOM 8271 C C . ILE E 1 118 ? 39.991 1.586 62.023 1.00 45.53 ? 117 ILE E C 1 ATOM 8272 O O . ILE E 1 118 ? 38.793 1.701 61.794 1.00 44.73 ? 117 ILE E O 1 ATOM 8273 C CB . ILE E 1 118 ? 40.713 2.488 59.826 1.00 41.60 ? 117 ILE E CB 1 ATOM 8274 C CG1 . ILE E 1 118 ? 41.685 2.371 58.654 1.00 40.83 ? 117 ILE E CG1 1 ATOM 8275 C CG2 . ILE E 1 118 ? 40.853 3.860 60.471 1.00 42.20 ? 117 ILE E CG2 1 ATOM 8276 C CD1 . ILE E 1 118 ? 41.480 3.411 57.574 1.00 39.15 ? 117 ILE E CD1 1 ATOM 8277 N N . PRO E 1 119 ? 40.494 1.634 63.270 1.00 48.06 ? 118 PRO E N 1 ATOM 8278 C CA . PRO E 1 119 ? 39.568 1.783 64.385 1.00 49.97 ? 118 PRO E CA 1 ATOM 8279 C C . PRO E 1 119 ? 38.880 3.137 64.399 1.00 49.85 ? 118 PRO E C 1 ATOM 8280 O O . PRO E 1 119 ? 39.500 4.152 64.082 1.00 49.33 ? 118 PRO E O 1 ATOM 8281 C CB . PRO E 1 119 ? 40.465 1.639 65.618 1.00 52.67 ? 118 PRO E CB 1 ATOM 8282 C CG . PRO E 1 119 ? 41.670 0.911 65.127 1.00 52.72 ? 118 PRO E CG 1 ATOM 8283 C CD . PRO E 1 119 ? 41.872 1.417 63.735 1.00 49.78 ? 118 PRO E CD 1 ATOM 8284 N N . LYS E 1 120 ? 37.605 3.130 64.775 1.00 50.57 ? 119 LYS E N 1 ATOM 8285 C CA . LYS E 1 120 ? 36.819 4.347 64.934 1.00 50.67 ? 119 LYS E CA 1 ATOM 8286 C C . LYS E 1 120 ? 37.373 5.234 66.062 1.00 52.04 ? 119 LYS E C 1 ATOM 8287 O O . LYS E 1 120 ? 37.212 6.448 66.026 1.00 51.51 ? 119 LYS E O 1 ATOM 8288 C CB . LYS E 1 120 ? 35.360 3.973 65.213 1.00 51.91 ? 119 LYS E CB 1 ATOM 8289 C CG . LYS E 1 120 ? 34.323 5.059 64.954 1.00 51.41 ? 119 LYS E CG 1 ATOM 8290 C CD . LYS E 1 120 ? 32.934 4.435 65.064 1.00 52.31 ? 119 LYS E CD 1 ATOM 8291 C CE . LYS E 1 120 ? 31.805 5.408 64.772 1.00 52.21 ? 119 LYS E CE 1 ATOM 8292 N NZ . LYS E 1 120 ? 30.469 4.844 65.143 1.00 53.50 ? 119 LYS E NZ 1 ATOM 8293 N N . SER E 1 121 ? 38.031 4.633 67.052 1.00 53.50 ? 120 SER E N 1 ATOM 8294 C CA . SER E 1 121 ? 38.664 5.410 68.129 1.00 55.36 ? 120 SER E CA 1 ATOM 8295 C C . SER E 1 121 ? 39.926 6.162 67.676 1.00 54.52 ? 120 SER E C 1 ATOM 8296 O O . SER E 1 121 ? 40.376 7.088 68.361 1.00 55.88 ? 120 SER E O 1 ATOM 8297 C CB . SER E 1 121 ? 39.016 4.499 69.310 1.00 58.22 ? 120 SER E CB 1 ATOM 8298 O OG . SER E 1 121 ? 40.101 3.641 68.995 1.00 57.93 ? 120 SER E OG 1 ATOM 8299 N N . SER E 1 122 ? 40.480 5.775 66.522 1.00 52.17 ? 121 SER E N 1 ATOM 8300 C CA . SER E 1 122 ? 41.777 6.283 66.070 1.00 51.73 ? 121 SER E CA 1 ATOM 8301 C C . SER E 1 122 ? 41.707 7.674 65.453 1.00 50.19 ? 121 SER E C 1 ATOM 8302 O O . SER E 1 122 ? 42.739 8.276 65.170 1.00 50.32 ? 121 SER E O 1 ATOM 8303 C CB . SER E 1 122 ? 42.415 5.307 65.084 1.00 50.43 ? 121 SER E CB 1 ATOM 8304 O OG . SER E 1 122 ? 41.779 5.346 63.823 1.00 47.97 ? 121 SER E OG 1 ATOM 8305 N N . TRP E 1 123 ? 40.497 8.184 65.246 1.00 49.02 ? 122 TRP E N 1 ATOM 8306 C CA . TRP E 1 123 ? 40.304 9.511 64.665 1.00 47.70 ? 122 TRP E CA 1 ATOM 8307 C C . TRP E 1 123 ? 40.277 10.546 65.768 1.00 50.04 ? 122 TRP E C 1 ATOM 8308 O O . TRP E 1 123 ? 39.229 10.796 66.349 1.00 51.99 ? 122 TRP E O 1 ATOM 8309 C CB . TRP E 1 123 ? 38.996 9.559 63.867 1.00 45.10 ? 122 TRP E CB 1 ATOM 8310 C CG . TRP E 1 123 ? 38.937 8.542 62.791 1.00 42.55 ? 122 TRP E CG 1 ATOM 8311 C CD1 . TRP E 1 123 ? 38.240 7.368 62.807 1.00 42.19 ? 122 TRP E CD1 1 ATOM 8312 C CD2 . TRP E 1 123 ? 39.614 8.589 61.537 1.00 40.68 ? 122 TRP E CD2 1 ATOM 8313 N NE1 . TRP E 1 123 ? 38.441 6.680 61.639 1.00 40.16 ? 122 TRP E NE1 1 ATOM 8314 C CE2 . TRP E 1 123 ? 39.280 7.407 60.838 1.00 39.22 ? 122 TRP E CE2 1 ATOM 8315 C CE3 . TRP E 1 123 ? 40.479 9.510 60.933 1.00 40.02 ? 122 TRP E CE3 1 ATOM 8316 C CZ2 . TRP E 1 123 ? 39.767 7.132 59.567 1.00 37.44 ? 122 TRP E CZ2 1 ATOM 8317 C CZ3 . TRP E 1 123 ? 40.962 9.232 59.659 1.00 38.16 ? 122 TRP E CZ3 1 ATOM 8318 C CH2 . TRP E 1 123 ? 40.610 8.049 58.999 1.00 37.14 ? 122 TRP E CH2 1 ATOM 8319 N N . SER E 1 124 ? 41.424 11.157 66.048 1.00 51.27 ? 123 SER E N 1 ATOM 8320 C CA . SER E 1 124 ? 41.565 12.065 67.190 1.00 53.69 ? 123 SER E CA 1 ATOM 8321 C C . SER E 1 124 ? 41.327 13.539 66.854 1.00 53.24 ? 123 SER E C 1 ATOM 8322 O O . SER E 1 124 ? 40.908 14.307 67.718 1.00 54.68 ? 123 SER E O 1 ATOM 8323 C CB . SER E 1 124 ? 42.956 11.912 67.800 1.00 55.75 ? 123 SER E CB 1 ATOM 8324 O OG . SER E 1 124 ? 43.241 10.551 68.029 1.00 56.33 ? 123 SER E OG 1 ATOM 8325 N N . ASP E 1 125 ? 41.625 13.927 65.616 1.00 37.67 ? 124 ASP E N 1 ATOM 8326 C CA . ASP E 1 125 ? 41.426 15.300 65.139 1.00 38.15 ? 124 ASP E CA 1 ATOM 8327 C C . ASP E 1 125 ? 40.176 15.457 64.255 1.00 36.74 ? 124 ASP E C 1 ATOM 8328 O O . ASP E 1 125 ? 39.992 16.492 63.610 1.00 36.37 ? 124 ASP E O 1 ATOM 8329 C CB . ASP E 1 125 ? 42.653 15.749 64.341 1.00 39.36 ? 124 ASP E CB 1 ATOM 8330 C CG . ASP E 1 125 ? 43.847 16.077 65.221 1.00 41.96 ? 124 ASP E CG 1 ATOM 8331 O OD1 . ASP E 1 125 ? 43.826 15.787 66.436 1.00 43.41 ? 124 ASP E OD1 1 ATOM 8332 O OD2 . ASP E 1 125 ? 44.820 16.639 64.686 1.00 43.84 ? 124 ASP E OD2 1 ATOM 8333 N N . HIS E 1 126 ? 39.333 14.429 64.201 1.00 35.56 ? 125 HIS E N 1 ATOM 8334 C CA . HIS E 1 126 ? 38.082 14.519 63.471 1.00 34.94 ? 125 HIS E CA 1 ATOM 8335 C C . HIS E 1 126 ? 36.954 13.955 64.318 1.00 35.40 ? 125 HIS E C 1 ATOM 8336 O O . HIS E 1 126 ? 37.188 13.124 65.199 1.00 37.03 ? 125 HIS E O 1 ATOM 8337 C CB . HIS E 1 126 ? 38.170 13.763 62.144 1.00 33.11 ? 125 HIS E CB 1 ATOM 8338 C CG . HIS E 1 126 ? 39.201 14.311 61.213 1.00 32.79 ? 125 HIS E CG 1 ATOM 8339 N ND1 . HIS E 1 126 ? 40.544 14.071 61.375 1.00 34.26 ? 125 HIS E ND1 1 ATOM 8340 C CD2 . HIS E 1 126 ? 39.089 15.100 60.121 1.00 32.46 ? 125 HIS E CD2 1 ATOM 8341 C CE1 . HIS E 1 126 ? 41.220 14.689 60.424 1.00 34.72 ? 125 HIS E CE1 1 ATOM 8342 N NE2 . HIS E 1 126 ? 40.360 15.320 59.647 1.00 33.74 ? 125 HIS E NE2 1 ATOM 8343 N N . GLU E 1 127 ? 35.738 14.426 64.054 1.00 34.69 ? 126 GLU E N 1 ATOM 8344 C CA . GLU E 1 127 ? 34.544 13.838 64.646 1.00 34.38 ? 126 GLU E CA 1 ATOM 8345 C C . GLU E 1 127 ? 34.217 12.582 63.866 1.00 32.59 ? 126 GLU E C 1 ATOM 8346 O O . GLU E 1 127 ? 33.999 12.646 62.664 1.00 31.15 ? 126 GLU E O 1 ATOM 8347 C CB . GLU E 1 127 ? 33.382 14.828 64.592 1.00 34.78 ? 126 GLU E CB 1 ATOM 8348 C CG . GLU E 1 127 ? 32.074 14.299 65.161 1.00 35.39 ? 126 GLU E CG 1 ATOM 8349 C CD . GLU E 1 127 ? 32.158 13.911 66.624 1.00 37.41 ? 126 GLU E CD 1 ATOM 8350 O OE1 . GLU E 1 127 ? 32.148 14.823 67.482 1.00 40.11 ? 126 GLU E OE1 1 ATOM 8351 O OE2 . GLU E 1 127 ? 32.218 12.695 66.921 1.00 37.75 ? 126 GLU E OE2 1 ATOM 8352 N N . ALA E 1 128 ? 34.217 11.441 64.547 1.00 33.36 ? 127 ALA E N 1 ATOM 8353 C CA . ALA E 1 128 ? 33.919 10.147 63.927 1.00 32.41 ? 127 ALA E CA 1 ATOM 8354 C C . ALA E 1 128 ? 32.672 9.479 64.476 1.00 32.76 ? 127 ALA E C 1 ATOM 8355 O O . ALA E 1 128 ? 32.360 8.368 64.056 1.00 31.70 ? 127 ALA E O 1 ATOM 8356 C CB . ALA E 1 128 ? 35.098 9.213 64.118 1.00 33.68 ? 127 ALA E CB 1 ATOM 8357 N N . SER E 1 129 ? 31.971 10.141 65.406 1.00 34.21 ? 128 SER E N 1 ATOM 8358 C CA . SER E 1 129 ? 30.787 9.568 66.069 1.00 35.23 ? 128 SER E CA 1 ATOM 8359 C C . SER E 1 129 ? 29.457 10.275 65.757 1.00 33.84 ? 128 SER E C 1 ATOM 8360 O O . SER E 1 129 ? 28.487 10.124 66.498 1.00 35.46 ? 128 SER E O 1 ATOM 8361 C CB . SER E 1 129 ? 30.997 9.547 67.588 1.00 37.27 ? 128 SER E CB 1 ATOM 8362 O OG . SER E 1 129 ? 32.031 8.641 67.930 1.00 40.41 ? 128 SER E OG 1 ATOM 8363 N N . ALA E 1 130 ? 29.399 11.036 64.677 1.00 32.11 ? 129 ALA E N 1 ATOM 8364 C CA . ALA E 1 130 ? 28.172 11.746 64.329 1.00 32.04 ? 129 ALA E CA 1 ATOM 8365 C C . ALA E 1 130 ? 27.838 11.651 62.834 1.00 30.83 ? 129 ALA E C 1 ATOM 8366 O O . ALA E 1 130 ? 26.978 12.382 62.317 1.00 31.71 ? 129 ALA E O 1 ATOM 8367 C CB . ALA E 1 130 ? 28.252 13.197 64.812 1.00 32.38 ? 129 ALA E CB 1 ATOM 8368 N N . GLY E 1 131 ? 28.491 10.716 62.152 1.00 30.06 ? 130 GLY E N 1 ATOM 8369 C CA . GLY E 1 131 ? 28.214 10.443 60.753 1.00 28.75 ? 130 GLY E CA 1 ATOM 8370 C C . GLY E 1 131 ? 26.968 9.609 60.559 1.00 28.05 ? 130 GLY E C 1 ATOM 8371 O O . GLY E 1 131 ? 27.055 8.452 60.172 1.00 27.58 ? 130 GLY E O 1 ATOM 8372 N N . VAL E 1 132 ? 25.805 10.211 60.806 1.00 27.92 ? 131 VAL E N 1 ATOM 8373 C CA . VAL E 1 132 ? 24.531 9.486 60.812 1.00 26.88 ? 131 VAL E CA 1 ATOM 8374 C C . VAL E 1 132 ? 23.529 10.206 59.931 1.00 26.44 ? 131 VAL E C 1 ATOM 8375 O O . VAL E 1 132 ? 23.672 11.397 59.672 1.00 27.48 ? 131 VAL E O 1 ATOM 8376 C CB . VAL E 1 132 ? 23.944 9.350 62.238 1.00 27.89 ? 131 VAL E CB 1 ATOM 8377 C CG1 . VAL E 1 132 ? 24.858 8.519 63.120 1.00 28.04 ? 131 VAL E CG1 1 ATOM 8378 C CG2 . VAL E 1 132 ? 23.714 10.712 62.876 1.00 28.45 ? 131 VAL E CG2 1 ATOM 8379 N N . SER E 1 133 ? 22.523 9.482 59.461 1.00 25.86 ? 132 SER E N 1 ATOM 8380 C CA . SER E 1 133 ? 21.461 10.089 58.665 1.00 25.85 ? 132 SER E CA 1 ATOM 8381 C C . SER E 1 133 ? 20.160 9.354 58.872 1.00 26.16 ? 132 SER E C 1 ATOM 8382 O O . SER E 1 133 ? 20.138 8.118 59.040 1.00 27.00 ? 132 SER E O 1 ATOM 8383 C CB . SER E 1 133 ? 21.809 10.076 57.180 1.00 25.02 ? 132 SER E CB 1 ATOM 8384 O OG . SER E 1 133 ? 20.729 10.582 56.409 1.00 25.46 ? 132 SER E OG 1 ATOM 8385 N N . SER E 1 134 ? 19.080 10.121 58.855 1.00 26.02 ? 133 SER E N 1 ATOM 8386 C CA . SER E 1 134 ? 17.731 9.573 58.931 1.00 27.15 ? 133 SER E CA 1 ATOM 8387 C C . SER E 1 134 ? 17.416 8.695 57.721 1.00 27.14 ? 133 SER E C 1 ATOM 8388 O O . SER E 1 134 ? 16.437 7.956 57.727 1.00 29.32 ? 133 SER E O 1 ATOM 8389 C CB . SER E 1 134 ? 16.711 10.704 59.022 1.00 27.22 ? 133 SER E CB 1 ATOM 8390 O OG . SER E 1 134 ? 16.820 11.526 57.878 1.00 26.63 ? 133 SER E OG 1 ATOM 8391 N N . ALA E 1 135 ? 18.240 8.783 56.685 1.00 26.47 ? 134 ALA E N 1 ATOM 8392 C CA . ALA E 1 135 ? 18.170 7.854 55.571 1.00 26.82 ? 134 ALA E CA 1 ATOM 8393 C C . ALA E 1 135 ? 18.545 6.423 55.972 1.00 28.16 ? 134 ALA E C 1 ATOM 8394 O O . ALA E 1 135 ? 18.206 5.467 55.268 1.00 31.54 ? 134 ALA E O 1 ATOM 8395 C CB . ALA E 1 135 ? 19.065 8.332 54.442 1.00 25.93 ? 134 ALA E CB 1 ATOM 8396 N N . CYS E 1 136 ? 19.245 6.267 57.086 1.00 28.18 ? 135 CYS E N 1 ATOM 8397 C CA . CYS E 1 136 ? 19.735 4.957 57.509 1.00 28.07 ? 135 CYS E CA 1 ATOM 8398 C C . CYS E 1 136 ? 19.242 4.661 58.912 1.00 27.30 ? 135 CYS E C 1 ATOM 8399 O O . CYS E 1 136 ? 20.028 4.635 59.832 1.00 27.27 ? 135 CYS E O 1 ATOM 8400 C CB . CYS E 1 136 ? 21.265 4.944 57.510 1.00 27.73 ? 135 CYS E CB 1 ATOM 8401 S SG . CYS E 1 136 ? 21.989 5.231 55.892 1.00 28.97 ? 135 CYS E SG 1 ATOM 8402 N N . PRO E 1 137 ? 17.932 4.447 59.076 1.00 26.57 ? 136 PRO E N 1 ATOM 8403 C CA . PRO E 1 137 ? 17.436 4.239 60.416 1.00 26.64 ? 136 PRO E CA 1 ATOM 8404 C C . PRO E 1 137 ? 17.930 2.933 61.029 1.00 26.71 ? 136 PRO E C 1 ATOM 8405 O O . PRO E 1 137 ? 18.296 1.989 60.315 1.00 26.89 ? 136 PRO E O 1 ATOM 8406 C CB . PRO E 1 137 ? 15.909 4.213 60.241 1.00 27.23 ? 136 PRO E CB 1 ATOM 8407 C CG . PRO E 1 137 ? 15.671 3.914 58.810 1.00 26.83 ? 136 PRO E CG 1 ATOM 8408 C CD . PRO E 1 137 ? 16.858 4.431 58.061 1.00 26.25 ? 136 PRO E CD 1 ATOM 8409 N N . TYR E 1 138 ? 17.955 2.906 62.351 1.00 26.62 ? 137 TYR E N 1 ATOM 8410 C CA . TYR E 1 138 ? 18.220 1.697 63.083 1.00 27.56 ? 137 TYR E CA 1 ATOM 8411 C C . TYR E 1 138 ? 17.515 1.785 64.430 1.00 28.89 ? 137 TYR E C 1 ATOM 8412 O O . TYR E 1 138 ? 17.872 2.615 65.267 1.00 29.20 ? 137 TYR E O 1 ATOM 8413 C CB . TYR E 1 138 ? 19.721 1.512 63.270 1.00 26.85 ? 137 TYR E CB 1 ATOM 8414 C CG . TYR E 1 138 ? 20.039 0.326 64.125 1.00 27.85 ? 137 TYR E CG 1 ATOM 8415 C CD1 . TYR E 1 138 ? 19.951 -0.957 63.618 1.00 28.29 ? 137 TYR E CD1 1 ATOM 8416 C CD2 . TYR E 1 138 ? 20.402 0.483 65.461 1.00 28.90 ? 137 TYR E CD2 1 ATOM 8417 C CE1 . TYR E 1 138 ? 20.213 -2.055 64.412 1.00 29.40 ? 137 TYR E CE1 1 ATOM 8418 C CE2 . TYR E 1 138 ? 20.674 -0.609 66.257 1.00 30.14 ? 137 TYR E CE2 1 ATOM 8419 C CZ . TYR E 1 138 ? 20.582 -1.870 65.718 1.00 30.42 ? 137 TYR E CZ 1 ATOM 8420 O OH . TYR E 1 138 ? 20.862 -2.951 66.499 1.00 32.71 ? 137 TYR E OH 1 ATOM 8421 N N . GLN E 1 139 ? 16.508 0.935 64.626 1.00 30.12 ? 138 GLN E N 1 ATOM 8422 C CA . GLN E 1 139 ? 15.721 0.900 65.873 1.00 31.46 ? 138 GLN E CA 1 ATOM 8423 C C . GLN E 1 139 ? 15.160 2.292 66.208 1.00 31.70 ? 138 GLN E C 1 ATOM 8424 O O . GLN E 1 139 ? 15.299 2.792 67.324 1.00 32.40 ? 138 GLN E O 1 ATOM 8425 C CB . GLN E 1 139 ? 16.563 0.327 67.025 1.00 32.00 ? 138 GLN E CB 1 ATOM 8426 C CG . GLN E 1 139 ? 17.073 -1.082 66.751 1.00 32.30 ? 138 GLN E CG 1 ATOM 8427 C CD . GLN E 1 139 ? 17.592 -1.802 67.989 1.00 34.13 ? 138 GLN E CD 1 ATOM 8428 O OE1 . GLN E 1 139 ? 17.920 -1.182 68.991 1.00 34.50 ? 138 GLN E OE1 1 ATOM 8429 N NE2 . GLN E 1 139 ? 17.702 -3.122 67.902 1.00 35.38 ? 138 GLN E NE2 1 ATOM 8430 N N . GLY E 1 140 ? 14.563 2.926 65.209 1.00 31.21 ? 139 GLY E N 1 ATOM 8431 C CA . GLY E 1 140 ? 13.923 4.216 65.394 1.00 32.33 ? 139 GLY E CA 1 ATOM 8432 C C . GLY E 1 140 ? 14.809 5.452 65.390 1.00 32.07 ? 139 GLY E C 1 ATOM 8433 O O . GLY E 1 140 ? 14.315 6.551 65.645 1.00 32.67 ? 139 GLY E O 1 ATOM 8434 N N . ARG E 1 141 ? 16.106 5.299 65.114 1.00 31.88 ? 140 ARG E N 1 ATOM 8435 C CA . ARG E 1 141 ? 17.023 6.456 65.107 1.00 31.12 ? 140 ARG E CA 1 ATOM 8436 C C . ARG E 1 141 ? 17.962 6.500 63.895 1.00 28.32 ? 140 ARG E C 1 ATOM 8437 O O . ARG E 1 141 ? 18.219 5.493 63.250 1.00 27.32 ? 140 ARG E O 1 ATOM 8438 C CB . ARG E 1 141 ? 17.857 6.466 66.388 1.00 32.65 ? 140 ARG E CB 1 ATOM 8439 C CG . ARG E 1 141 ? 18.919 5.371 66.445 1.00 33.24 ? 140 ARG E CG 1 ATOM 8440 C CD . ARG E 1 141 ? 19.913 5.590 67.583 1.00 34.70 ? 140 ARG E CD 1 ATOM 8441 N NE . ARG E 1 141 ? 20.981 4.596 67.564 1.00 35.00 ? 140 ARG E NE 1 ATOM 8442 C CZ . ARG E 1 141 ? 20.928 3.397 68.145 1.00 37.23 ? 140 ARG E CZ 1 ATOM 8443 N NH1 . ARG E 1 141 ? 19.850 2.997 68.821 1.00 39.01 ? 140 ARG E NH1 1 ATOM 8444 N NH2 . ARG E 1 141 ? 21.971 2.585 68.048 1.00 37.79 ? 140 ARG E NH2 1 ATOM 8445 N N . SER E 1 142 ? 18.494 7.685 63.634 1.00 27.02 ? 141 SER E N 1 ATOM 8446 C CA . SER E 1 142 ? 19.509 7.886 62.614 1.00 25.29 ? 141 SER E CA 1 ATOM 8447 C C . SER E 1 142 ? 20.816 7.134 62.924 1.00 25.83 ? 141 SER E C 1 ATOM 8448 O O . SER E 1 142 ? 21.354 7.184 64.033 1.00 26.78 ? 141 SER E O 1 ATOM 8449 C CB . SER E 1 142 ? 19.799 9.372 62.435 1.00 24.46 ? 141 SER E CB 1 ATOM 8450 O OG . SER E 1 142 ? 18.603 10.106 62.237 1.00 23.62 ? 141 SER E OG 1 ATOM 8451 N N . SER E 1 143 ? 21.318 6.448 61.902 1.00 25.06 ? 142 SER E N 1 ATOM 8452 C CA . SER E 1 143 ? 22.493 5.623 61.996 1.00 24.81 ? 142 SER E CA 1 ATOM 8453 C C . SER E 1 143 ? 23.244 5.695 60.653 1.00 24.31 ? 142 SER E C 1 ATOM 8454 O O . SER E 1 143 ? 23.101 6.677 59.902 1.00 23.04 ? 142 SER E O 1 ATOM 8455 C CB . SER E 1 143 ? 22.064 4.190 62.328 1.00 25.46 ? 142 SER E CB 1 ATOM 8456 O OG . SER E 1 143 ? 23.179 3.375 62.605 1.00 25.88 ? 142 SER E OG 1 ATOM 8457 N N . PHE E 1 144 ? 24.037 4.662 60.345 1.00 24.32 ? 143 PHE E N 1 ATOM 8458 C CA . PHE E 1 144 ? 24.879 4.677 59.155 1.00 23.46 ? 143 PHE E CA 1 ATOM 8459 C C . PHE E 1 144 ? 25.483 3.304 58.871 1.00 23.92 ? 143 PHE E C 1 ATOM 8460 O O . PHE E 1 144 ? 25.395 2.407 59.703 1.00 24.63 ? 143 PHE E O 1 ATOM 8461 C CB . PHE E 1 144 ? 25.995 5.716 59.321 1.00 23.15 ? 143 PHE E CB 1 ATOM 8462 C CG . PHE E 1 144 ? 26.640 6.112 58.030 1.00 22.13 ? 143 PHE E CG 1 ATOM 8463 C CD1 . PHE E 1 144 ? 25.913 6.778 57.063 1.00 21.83 ? 143 PHE E CD1 1 ATOM 8464 C CD2 . PHE E 1 144 ? 27.963 5.797 57.770 1.00 22.14 ? 143 PHE E CD2 1 ATOM 8465 C CE1 . PHE E 1 144 ? 26.486 7.122 55.848 1.00 21.15 ? 143 PHE E CE1 1 ATOM 8466 C CE2 . PHE E 1 144 ? 28.547 6.151 56.568 1.00 21.39 ? 143 PHE E CE2 1 ATOM 8467 C CZ . PHE E 1 144 ? 27.807 6.811 55.608 1.00 21.09 ? 143 PHE E CZ 1 ATOM 8468 N N . PHE E 1 145 ? 26.097 3.148 57.699 1.00 23.48 ? 144 PHE E N 1 ATOM 8469 C CA . PHE E 1 145 ? 26.751 1.880 57.333 1.00 24.20 ? 144 PHE E CA 1 ATOM 8470 C C . PHE E 1 145 ? 27.794 1.517 58.380 1.00 25.49 ? 144 PHE E C 1 ATOM 8471 O O . PHE E 1 145 ? 28.569 2.362 58.792 1.00 25.70 ? 144 PHE E O 1 ATOM 8472 C CB . PHE E 1 145 ? 27.441 1.973 55.962 1.00 23.51 ? 144 PHE E CB 1 ATOM 8473 C CG . PHE E 1 145 ? 26.531 2.391 54.831 1.00 22.64 ? 144 PHE E CG 1 ATOM 8474 C CD1 . PHE E 1 145 ? 25.751 1.463 54.171 1.00 22.45 ? 144 PHE E CD1 1 ATOM 8475 C CD2 . PHE E 1 145 ? 26.477 3.716 54.423 1.00 21.71 ? 144 PHE E CD2 1 ATOM 8476 C CE1 . PHE E 1 145 ? 24.927 1.837 53.120 1.00 22.01 ? 144 PHE E CE1 1 ATOM 8477 C CE2 . PHE E 1 145 ? 25.667 4.098 53.374 1.00 21.37 ? 144 PHE E CE2 1 ATOM 8478 C CZ . PHE E 1 145 ? 24.885 3.159 52.721 1.00 21.78 ? 144 PHE E CZ 1 ATOM 8479 N N . ARG E 1 146 ? 27.808 0.253 58.789 1.00 27.14 ? 145 ARG E N 1 ATOM 8480 C CA . ARG E 1 146 ? 28.620 -0.215 59.892 1.00 28.68 ? 145 ARG E CA 1 ATOM 8481 C C . ARG E 1 146 ? 30.110 -0.354 59.559 1.00 28.59 ? 145 ARG E C 1 ATOM 8482 O O . ARG E 1 146 ? 30.950 -0.312 60.465 1.00 29.88 ? 145 ARG E O 1 ATOM 8483 C CB . ARG E 1 146 ? 28.134 -1.586 60.357 1.00 31.75 ? 145 ARG E CB 1 ATOM 8484 C CG . ARG E 1 146 ? 26.685 -1.675 60.783 1.00 33.38 ? 145 ARG E CG 1 ATOM 8485 C CD . ARG E 1 146 ? 26.448 -1.019 62.118 1.00 35.45 ? 145 ARG E CD 1 ATOM 8486 N NE . ARG E 1 146 ? 25.230 -1.533 62.736 1.00 37.39 ? 145 ARG E NE 1 ATOM 8487 C CZ . ARG E 1 146 ? 24.375 -0.804 63.448 1.00 38.87 ? 145 ARG E CZ 1 ATOM 8488 N NH1 . ARG E 1 146 ? 24.576 0.501 63.631 1.00 39.44 ? 145 ARG E NH1 1 ATOM 8489 N NH2 . ARG E 1 146 ? 23.293 -1.377 63.968 1.00 39.27 ? 145 ARG E NH2 1 ATOM 8490 N N . ASN E 1 147 ? 30.445 -0.551 58.290 1.00 26.58 ? 146 ASN E N 1 ATOM 8491 C CA . ASN E 1 147 ? 31.817 -0.881 57.927 1.00 26.66 ? 146 ASN E CA 1 ATOM 8492 C C . ASN E 1 147 ? 32.617 0.288 57.393 1.00 25.89 ? 146 ASN E C 1 ATOM 8493 O O . ASN E 1 147 ? 33.794 0.133 57.082 1.00 27.37 ? 146 ASN E O 1 ATOM 8494 C CB . ASN E 1 147 ? 31.839 -2.032 56.931 1.00 26.25 ? 146 ASN E CB 1 ATOM 8495 C CG . ASN E 1 147 ? 31.147 -3.255 57.470 1.00 27.45 ? 146 ASN E CG 1 ATOM 8496 O OD1 . ASN E 1 147 ? 31.370 -3.653 58.616 1.00 29.36 ? 146 ASN E OD1 1 ATOM 8497 N ND2 . ASN E 1 147 ? 30.296 -3.855 56.661 1.00 27.08 ? 146 ASN E ND2 1 ATOM 8498 N N . VAL E 1 148 ? 31.992 1.452 57.304 1.00 25.04 ? 147 VAL E N 1 ATOM 8499 C CA . VAL E 1 148 ? 32.698 2.681 56.953 1.00 24.45 ? 147 VAL E CA 1 ATOM 8500 C C . VAL E 1 148 ? 32.271 3.802 57.901 1.00 24.72 ? 147 VAL E C 1 ATOM 8501 O O . VAL E 1 148 ? 31.232 3.707 58.546 1.00 25.09 ? 147 VAL E O 1 ATOM 8502 C CB . VAL E 1 148 ? 32.406 3.110 55.517 1.00 23.55 ? 147 VAL E CB 1 ATOM 8503 C CG1 . VAL E 1 148 ? 32.918 2.070 54.529 1.00 24.14 ? 147 VAL E CG1 1 ATOM 8504 C CG2 . VAL E 1 148 ? 30.913 3.332 55.324 1.00 23.22 ? 147 VAL E CG2 1 ATOM 8505 N N . VAL E 1 149 ? 33.071 4.859 57.979 1.00 24.58 ? 148 VAL E N 1 ATOM 8506 C CA . VAL E 1 149 ? 32.821 5.929 58.934 1.00 25.41 ? 148 VAL E CA 1 ATOM 8507 C C . VAL E 1 149 ? 32.721 7.261 58.201 1.00 24.71 ? 148 VAL E C 1 ATOM 8508 O O . VAL E 1 149 ? 33.613 7.644 57.452 1.00 23.68 ? 148 VAL E O 1 ATOM 8509 C CB . VAL E 1 149 ? 33.899 5.994 60.052 1.00 26.47 ? 148 VAL E CB 1 ATOM 8510 C CG1 . VAL E 1 149 ? 33.540 7.036 61.100 1.00 26.80 ? 148 VAL E CG1 1 ATOM 8511 C CG2 . VAL E 1 149 ? 34.044 4.641 60.731 1.00 27.67 ? 148 VAL E CG2 1 ATOM 8512 N N . TRP E 1 150 ? 31.604 7.941 58.421 1.00 24.75 ? 149 TRP E N 1 ATOM 8513 C CA . TRP E 1 150 ? 31.377 9.261 57.871 1.00 24.86 ? 149 TRP E CA 1 ATOM 8514 C C . TRP E 1 150 ? 31.991 10.257 58.866 1.00 25.78 ? 149 TRP E C 1 ATOM 8515 O O . TRP E 1 150 ? 31.397 10.541 59.898 1.00 27.28 ? 149 TRP E O 1 ATOM 8516 C CB . TRP E 1 150 ? 29.870 9.477 57.697 1.00 24.52 ? 149 TRP E CB 1 ATOM 8517 C CG . TRP E 1 150 ? 29.476 10.769 57.053 1.00 24.65 ? 149 TRP E CG 1 ATOM 8518 C CD1 . TRP E 1 150 ? 30.294 11.771 56.661 1.00 24.97 ? 149 TRP E CD1 1 ATOM 8519 C CD2 . TRP E 1 150 ? 28.148 11.196 56.753 1.00 24.64 ? 149 TRP E CD2 1 ATOM 8520 N NE1 . TRP E 1 150 ? 29.565 12.786 56.099 1.00 25.35 ? 149 TRP E NE1 1 ATOM 8521 C CE2 . TRP E 1 150 ? 28.242 12.460 56.151 1.00 24.83 ? 149 TRP E CE2 1 ATOM 8522 C CE3 . TRP E 1 150 ? 26.882 10.621 56.917 1.00 25.68 ? 149 TRP E CE3 1 ATOM 8523 C CZ2 . TRP E 1 150 ? 27.124 13.175 55.728 1.00 25.21 ? 149 TRP E CZ2 1 ATOM 8524 C CZ3 . TRP E 1 150 ? 25.769 11.325 56.473 1.00 25.01 ? 149 TRP E CZ3 1 ATOM 8525 C CH2 . TRP E 1 150 ? 25.900 12.582 55.885 1.00 25.06 ? 149 TRP E CH2 1 ATOM 8526 N N . LEU E 1 151 ? 33.194 10.746 58.568 1.00 24.86 ? 150 LEU E N 1 ATOM 8527 C CA . LEU E 1 151 ? 33.884 11.705 59.424 1.00 26.23 ? 150 LEU E CA 1 ATOM 8528 C C . LEU E 1 151 ? 33.454 13.142 59.111 1.00 25.95 ? 150 LEU E C 1 ATOM 8529 O O . LEU E 1 151 ? 33.208 13.473 57.965 1.00 25.09 ? 150 LEU E O 1 ATOM 8530 C CB . LEU E 1 151 ? 35.413 11.591 59.235 1.00 27.17 ? 150 LEU E CB 1 ATOM 8531 C CG . LEU E 1 151 ? 36.057 10.215 59.475 1.00 27.67 ? 150 LEU E CG 1 ATOM 8532 C CD1 . LEU E 1 151 ? 37.503 10.171 59.013 1.00 28.36 ? 150 LEU E CD1 1 ATOM 8533 C CD2 . LEU E 1 151 ? 35.958 9.817 60.941 1.00 28.80 ? 150 LEU E CD2 1 ATOM 8534 N N . ILE E 1 152 ? 33.382 14.000 60.124 1.00 27.43 ? 151 ILE E N 1 ATOM 8535 C CA . ILE E 1 152 ? 33.207 15.446 59.886 1.00 28.55 ? 151 ILE E CA 1 ATOM 8536 C C . ILE E 1 152 ? 34.218 16.294 60.678 1.00 30.27 ? 151 ILE E C 1 ATOM 8537 O O . ILE E 1 152 ? 35.100 15.766 61.363 1.00 30.98 ? 151 ILE E O 1 ATOM 8538 C CB . ILE E 1 152 ? 31.755 15.921 60.123 1.00 28.37 ? 151 ILE E CB 1 ATOM 8539 C CG1 . ILE E 1 152 ? 31.282 15.594 61.529 1.00 29.30 ? 151 ILE E CG1 1 ATOM 8540 C CG2 . ILE E 1 152 ? 30.818 15.302 59.099 1.00 27.36 ? 151 ILE E CG2 1 ATOM 8541 C CD1 . ILE E 1 152 ? 30.129 16.471 61.973 1.00 29.94 ? 151 ILE E CD1 1 ATOM 8542 N N . LYS E 1 153 ? 34.118 17.611 60.534 1.00 31.24 ? 152 LYS E N 1 ATOM 8543 C CA . LYS E 1 153 ? 35.062 18.510 61.161 1.00 32.73 ? 152 LYS E CA 1 ATOM 8544 C C . LYS E 1 153 ? 34.913 18.440 62.678 1.00 34.09 ? 152 LYS E C 1 ATOM 8545 O O . LYS E 1 153 ? 33.853 18.094 63.190 1.00 32.27 ? 152 LYS E O 1 ATOM 8546 C CB . LYS E 1 153 ? 34.871 19.938 60.653 1.00 33.42 ? 152 LYS E CB 1 ATOM 8547 C CG . LYS E 1 153 ? 33.639 20.643 61.186 1.00 34.02 ? 152 LYS E CG 1 ATOM 8548 C CD . LYS E 1 153 ? 33.502 22.018 60.553 1.00 35.14 ? 152 LYS E CD 1 ATOM 8549 C CE . LYS E 1 153 ? 32.377 22.809 61.201 1.00 35.89 ? 152 LYS E CE 1 ATOM 8550 N NZ . LYS E 1 153 ? 32.009 23.997 60.392 1.00 36.48 ? 152 LYS E NZ 1 ATOM 8551 N N . LYS E 1 154 ? 36.007 18.728 63.379 1.00 36.48 ? 153 LYS E N 1 ATOM 8552 C CA . LYS E 1 154 ? 36.015 18.782 64.827 1.00 38.97 ? 153 LYS E CA 1 ATOM 8553 C C . LYS E 1 154 ? 36.573 20.141 65.207 1.00 41.84 ? 153 LYS E C 1 ATOM 8554 O O . LYS E 1 154 ? 37.605 20.559 64.671 1.00 42.29 ? 153 LYS E O 1 ATOM 8555 C CB . LYS E 1 154 ? 36.886 17.665 65.376 1.00 40.01 ? 153 LYS E CB 1 ATOM 8556 C CG . LYS E 1 154 ? 36.853 17.501 66.881 1.00 42.66 ? 153 LYS E CG 1 ATOM 8557 C CD . LYS E 1 154 ? 38.023 16.638 67.343 1.00 44.19 ? 153 LYS E CD 1 ATOM 8558 C CE . LYS E 1 154 ? 38.039 16.484 68.850 1.00 46.45 ? 153 LYS E CE 1 ATOM 8559 N NZ . LYS E 1 154 ? 39.099 15.536 69.282 1.00 48.05 ? 153 LYS E NZ 1 ATOM 8560 N N . ASP E 1 155 ? 35.892 20.830 66.118 1.00 44.36 ? 154 ASP E N 1 ATOM 8561 C CA . ASP E 1 155 ? 36.335 22.147 66.590 1.00 47.90 ? 154 ASP E CA 1 ATOM 8562 C C . ASP E 1 155 ? 36.640 23.064 65.404 1.00 47.50 ? 154 ASP E C 1 ATOM 8563 O O . ASP E 1 155 ? 37.720 23.659 65.310 1.00 47.40 ? 154 ASP E O 1 ATOM 8564 C CB . ASP E 1 155 ? 37.556 22.012 67.514 1.00 51.26 ? 154 ASP E CB 1 ATOM 8565 C CG . ASP E 1 155 ? 37.215 21.341 68.838 1.00 53.81 ? 154 ASP E CG 1 ATOM 8566 O OD1 . ASP E 1 155 ? 36.214 21.748 69.468 1.00 57.09 ? 154 ASP E OD1 1 ATOM 8567 O OD2 . ASP E 1 155 ? 37.947 20.419 69.260 1.00 55.51 ? 154 ASP E OD2 1 ATOM 8568 N N . ASN E 1 156 ? 35.668 23.135 64.493 1.00 46.00 ? 155 ASN E N 1 ATOM 8569 C CA . ASN E 1 156 ? 35.738 23.970 63.290 1.00 46.03 ? 155 ASN E CA 1 ATOM 8570 C C . ASN E 1 156 ? 37.019 23.771 62.476 1.00 45.12 ? 155 ASN E C 1 ATOM 8571 O O . ASN E 1 156 ? 37.576 24.723 61.925 1.00 46.21 ? 155 ASN E O 1 ATOM 8572 C CB . ASN E 1 156 ? 35.509 25.454 63.658 1.00 48.85 ? 155 ASN E CB 1 ATOM 8573 C CG . ASN E 1 156 ? 34.026 25.821 63.705 1.00 48.88 ? 155 ASN E CG 1 ATOM 8574 O OD1 . ASN E 1 156 ? 33.284 25.579 62.746 1.00 47.78 ? 155 ASN E OD1 1 ATOM 8575 N ND2 . ASN E 1 156 ? 33.590 26.405 64.818 1.00 50.25 ? 155 ASN E ND2 1 ATOM 8576 N N . ALA E 1 157 ? 37.476 22.525 62.396 1.00 42.68 ? 156 ALA E N 1 ATOM 8577 C CA . ALA E 1 157 ? 38.649 22.201 61.593 1.00 41.84 ? 156 ALA E CA 1 ATOM 8578 C C . ALA E 1 157 ? 38.622 20.756 61.123 1.00 39.23 ? 156 ALA E C 1 ATOM 8579 O O . ALA E 1 157 ? 38.125 19.866 61.810 1.00 37.91 ? 156 ALA E O 1 ATOM 8580 C CB . ALA E 1 157 ? 39.922 22.478 62.368 1.00 43.68 ? 156 ALA E CB 1 ATOM 8581 N N . TYR E 1 158 ? 39.145 20.554 59.922 1.00 38.19 ? 157 TYR E N 1 ATOM 8582 C CA . TYR E 1 158 ? 39.277 19.240 59.327 1.00 36.11 ? 157 TYR E CA 1 ATOM 8583 C C . TYR E 1 158 ? 40.731 19.157 58.851 1.00 37.05 ? 157 TYR E C 1 ATOM 8584 O O . TYR E 1 158 ? 41.054 19.579 57.744 1.00 37.50 ? 157 TYR E O 1 ATOM 8585 C CB . TYR E 1 158 ? 38.292 19.095 58.162 1.00 33.91 ? 157 TYR E CB 1 ATOM 8586 C CG . TYR E 1 158 ? 38.093 17.678 57.652 1.00 31.65 ? 157 TYR E CG 1 ATOM 8587 C CD1 . TYR E 1 158 ? 39.072 17.030 56.906 1.00 31.35 ? 157 TYR E CD1 1 ATOM 8588 C CD2 . TYR E 1 158 ? 36.918 16.989 57.912 1.00 30.29 ? 157 TYR E CD2 1 ATOM 8589 C CE1 . TYR E 1 158 ? 38.881 15.724 56.440 1.00 29.81 ? 157 TYR E CE1 1 ATOM 8590 C CE2 . TYR E 1 158 ? 36.719 15.694 57.452 1.00 28.85 ? 157 TYR E CE2 1 ATOM 8591 C CZ . TYR E 1 158 ? 37.701 15.062 56.716 1.00 28.54 ? 157 TYR E CZ 1 ATOM 8592 O OH . TYR E 1 158 ? 37.481 13.770 56.252 1.00 27.44 ? 157 TYR E OH 1 ATOM 8593 N N . PRO E 1 159 ? 41.626 18.658 59.704 1.00 37.83 ? 158 PRO E N 1 ATOM 8594 C CA . PRO E 1 159 ? 42.983 18.539 59.214 1.00 39.08 ? 158 PRO E CA 1 ATOM 8595 C C . PRO E 1 159 ? 43.091 17.486 58.120 1.00 37.80 ? 158 PRO E C 1 ATOM 8596 O O . PRO E 1 159 ? 42.303 16.531 58.080 1.00 36.26 ? 158 PRO E O 1 ATOM 8597 C CB . PRO E 1 159 ? 43.780 18.149 60.469 1.00 40.45 ? 158 PRO E CB 1 ATOM 8598 C CG . PRO E 1 159 ? 42.963 18.667 61.600 1.00 40.89 ? 158 PRO E CG 1 ATOM 8599 C CD . PRO E 1 159 ? 41.546 18.443 61.157 1.00 39.22 ? 158 PRO E CD 1 ATOM 8600 N N . THR E 1 160 ? 44.049 17.688 57.225 1.00 39.05 ? 159 THR E N 1 ATOM 8601 C CA . THR E 1 160 ? 44.274 16.778 56.117 1.00 38.73 ? 159 THR E CA 1 ATOM 8602 C C . THR E 1 160 ? 44.655 15.405 56.646 1.00 37.91 ? 159 THR E C 1 ATOM 8603 O O . THR E 1 160 ? 45.619 15.267 57.392 1.00 40.37 ? 159 THR E O 1 ATOM 8604 C CB . THR E 1 160 ? 45.379 17.306 55.197 1.00 40.32 ? 159 THR E CB 1 ATOM 8605 O OG1 . THR E 1 160 ? 44.984 18.588 54.700 1.00 41.42 ? 159 THR E OG1 1 ATOM 8606 C CG2 . THR E 1 160 ? 45.611 16.353 54.017 1.00 39.48 ? 159 THR E CG2 1 ATOM 8607 N N . ILE E 1 161 ? 43.870 14.406 56.283 1.00 35.61 ? 160 ILE E N 1 ATOM 8608 C CA . ILE E 1 161 ? 44.081 13.043 56.746 1.00 35.62 ? 160 ILE E CA 1 ATOM 8609 C C . ILE E 1 161 ? 45.140 12.373 55.884 1.00 37.09 ? 160 ILE E C 1 ATOM 8610 O O . ILE E 1 161 ? 45.078 12.448 54.653 1.00 36.62 ? 160 ILE E O 1 ATOM 8611 C CB . ILE E 1 161 ? 42.777 12.232 56.669 1.00 33.67 ? 160 ILE E CB 1 ATOM 8612 C CG1 . ILE E 1 161 ? 41.844 12.651 57.812 1.00 34.30 ? 160 ILE E CG1 1 ATOM 8613 C CG2 . ILE E 1 161 ? 43.053 10.737 56.722 1.00 33.45 ? 160 ILE E CG2 1 ATOM 8614 C CD1 . ILE E 1 161 ? 40.396 12.242 57.617 1.00 33.04 ? 160 ILE E CD1 1 ATOM 8615 N N . LYS E 1 162 ? 46.113 11.735 56.533 1.00 38.48 ? 161 LYS E N 1 ATOM 8616 C CA . LYS E 1 162 ? 47.031 10.814 55.862 1.00 39.88 ? 161 LYS E CA 1 ATOM 8617 C C . LYS E 1 162 ? 47.041 9.522 56.673 1.00 40.68 ? 161 LYS E C 1 ATOM 8618 O O . LYS E 1 162 ? 47.607 9.485 57.766 1.00 45.16 ? 161 LYS E O 1 ATOM 8619 C CB . LYS E 1 162 ? 48.453 11.401 55.738 1.00 41.82 ? 161 LYS E CB 1 ATOM 8620 C CG . LYS E 1 162 ? 48.486 12.903 55.483 1.00 42.58 ? 161 LYS E CG 1 ATOM 8621 C CD . LYS E 1 162 ? 49.750 13.374 54.774 1.00 44.33 ? 161 LYS E CD 1 ATOM 8622 C CE . LYS E 1 162 ? 49.759 14.899 54.691 1.00 45.89 ? 161 LYS E CE 1 ATOM 8623 N NZ . LYS E 1 162 ? 50.635 15.451 53.616 1.00 47.18 ? 161 LYS E NZ 1 ATOM 8624 N N . ARG E 1 163 ? 46.385 8.484 56.160 1.00 39.18 ? 162 ARG E N 1 ATOM 8625 C CA . ARG E 1 163 ? 46.385 7.161 56.784 1.00 39.62 ? 162 ARG E CA 1 ATOM 8626 C C . ARG E 1 163 ? 46.876 6.140 55.784 1.00 40.00 ? 162 ARG E C 1 ATOM 8627 O O . ARG E 1 163 ? 46.625 6.262 54.587 1.00 40.53 ? 162 ARG E O 1 ATOM 8628 C CB . ARG E 1 163 ? 44.979 6.747 57.228 1.00 38.51 ? 162 ARG E CB 1 ATOM 8629 C CG . ARG E 1 163 ? 44.375 7.586 58.336 1.00 39.42 ? 162 ARG E CG 1 ATOM 8630 C CD . ARG E 1 163 ? 45.265 7.706 59.573 1.00 41.31 ? 162 ARG E CD 1 ATOM 8631 N NE . ARG E 1 163 ? 44.474 8.164 60.712 1.00 41.05 ? 162 ARG E NE 1 ATOM 8632 C CZ . ARG E 1 163 ? 43.689 7.373 61.438 1.00 41.03 ? 162 ARG E CZ 1 ATOM 8633 N NH1 . ARG E 1 163 ? 43.612 6.066 61.177 1.00 40.67 ? 162 ARG E NH1 1 ATOM 8634 N NH2 . ARG E 1 163 ? 42.988 7.883 62.443 1.00 41.55 ? 162 ARG E NH2 1 ATOM 8635 N N . SER E 1 164 ? 47.554 5.117 56.276 1.00 40.99 ? 163 SER E N 1 ATOM 8636 C CA . SER E 1 164 ? 48.013 4.032 55.434 1.00 41.70 ? 163 SER E CA 1 ATOM 8637 C C . SER E 1 164 ? 47.695 2.717 56.106 1.00 41.35 ? 163 SER E C 1 ATOM 8638 O O . SER E 1 164 ? 47.539 2.654 57.311 1.00 44.33 ? 163 SER E O 1 ATOM 8639 C CB . SER E 1 164 ? 49.513 4.156 55.191 1.00 44.48 ? 163 SER E CB 1 ATOM 8640 O OG . SER E 1 164 ? 49.807 5.378 54.536 1.00 46.02 ? 163 SER E OG 1 ATOM 8641 N N . TYR E 1 165 ? 47.562 1.671 55.321 1.00 40.69 ? 164 TYR E N 1 ATOM 8642 C CA . TYR E 1 165 ? 47.357 0.348 55.865 1.00 41.87 ? 164 TYR E CA 1 ATOM 8643 C C . TYR E 1 165 ? 48.070 -0.604 54.927 1.00 42.65 ? 164 TYR E C 1 ATOM 8644 O O . TYR E 1 165 ? 47.848 -0.572 53.711 1.00 40.95 ? 164 TYR E O 1 ATOM 8645 C CB . TYR E 1 165 ? 45.865 -0.010 56.002 1.00 41.22 ? 164 TYR E CB 1 ATOM 8646 C CG . TYR E 1 165 ? 45.664 -1.471 56.346 1.00 43.16 ? 164 TYR E CG 1 ATOM 8647 C CD1 . TYR E 1 165 ? 45.870 -1.937 57.638 1.00 45.47 ? 164 TYR E CD1 1 ATOM 8648 C CD2 . TYR E 1 165 ? 45.319 -2.393 55.366 1.00 44.55 ? 164 TYR E CD2 1 ATOM 8649 C CE1 . TYR E 1 165 ? 45.731 -3.282 57.949 1.00 47.32 ? 164 TYR E CE1 1 ATOM 8650 C CE2 . TYR E 1 165 ? 45.171 -3.736 55.666 1.00 46.30 ? 164 TYR E CE2 1 ATOM 8651 C CZ . TYR E 1 165 ? 45.379 -4.178 56.954 1.00 47.96 ? 164 TYR E CZ 1 ATOM 8652 O OH . TYR E 1 165 ? 45.229 -5.516 57.242 1.00 50.42 ? 164 TYR E OH 1 ATOM 8653 N N . ASN E 1 166 ? 48.951 -1.419 55.495 1.00 44.47 ? 165 ASN E N 1 ATOM 8654 C CA . ASN E 1 166 ? 49.713 -2.383 54.737 1.00 46.19 ? 165 ASN E CA 1 ATOM 8655 C C . ASN E 1 166 ? 49.036 -3.710 54.990 1.00 45.86 ? 165 ASN E C 1 ATOM 8656 O O . ASN E 1 166 ? 48.824 -4.086 56.140 1.00 45.82 ? 165 ASN E O 1 ATOM 8657 C CB . ASN E 1 166 ? 51.172 -2.367 55.205 1.00 49.95 ? 165 ASN E CB 1 ATOM 8658 C CG . ASN E 1 166 ? 52.044 -3.412 54.521 1.00 53.40 ? 165 ASN E CG 1 ATOM 8659 O OD1 . ASN E 1 166 ? 51.632 -4.556 54.315 1.00 52.98 ? 165 ASN E OD1 1 ATOM 8660 N ND2 . ASN E 1 166 ? 53.282 -3.020 54.181 1.00 57.80 ? 165 ASN E ND2 1 ATOM 8661 N N . ASN E 1 167 ? 48.641 -4.399 53.921 1.00 45.12 ? 166 ASN E N 1 ATOM 8662 C CA . ASN E 1 167 ? 48.008 -5.699 54.092 1.00 44.83 ? 166 ASN E CA 1 ATOM 8663 C C . ASN E 1 167 ? 49.061 -6.740 54.462 1.00 46.63 ? 166 ASN E C 1 ATOM 8664 O O . ASN E 1 167 ? 49.671 -7.351 53.596 1.00 46.96 ? 166 ASN E O 1 ATOM 8665 C CB . ASN E 1 167 ? 47.216 -6.132 52.857 1.00 42.49 ? 166 ASN E CB 1 ATOM 8666 C CG . ASN E 1 167 ? 46.625 -7.521 53.015 1.00 42.65 ? 166 ASN E CG 1 ATOM 8667 O OD1 . ASN E 1 167 ? 46.650 -8.091 54.108 1.00 44.42 ? 166 ASN E OD1 1 ATOM 8668 N ND2 . ASN E 1 167 ? 46.118 -8.082 51.933 1.00 41.19 ? 166 ASN E ND2 1 ATOM 8669 N N . THR E 1 168 ? 49.254 -6.934 55.763 1.00 48.61 ? 167 THR E N 1 ATOM 8670 C CA . THR E 1 168 ? 50.217 -7.917 56.270 1.00 51.97 ? 167 THR E CA 1 ATOM 8671 C C . THR E 1 168 ? 49.604 -9.319 56.375 1.00 53.42 ? 167 THR E C 1 ATOM 8672 O O . THR E 1 168 ? 50.195 -10.199 56.994 1.00 53.84 ? 167 THR E O 1 ATOM 8673 C CB . THR E 1 168 ? 50.765 -7.499 57.654 1.00 53.34 ? 167 THR E CB 1 ATOM 8674 O OG1 . THR E 1 168 ? 49.678 -7.335 58.570 1.00 53.69 ? 167 THR E OG1 1 ATOM 8675 C CG2 . THR E 1 168 ? 51.516 -6.183 57.565 1.00 53.09 ? 167 THR E CG2 1 ATOM 8676 N N . ASN E 1 169 ? 48.419 -9.512 55.784 1.00 53.29 ? 168 ASN E N 1 ATOM 8677 C CA . ASN E 1 169 ? 47.772 -10.826 55.737 1.00 54.87 ? 168 ASN E CA 1 ATOM 8678 C C . ASN E 1 169 ? 48.161 -11.590 54.486 1.00 55.92 ? 168 ASN E C 1 ATOM 8679 O O . ASN E 1 169 ? 48.585 -11.006 53.485 1.00 56.00 ? 168 ASN E O 1 ATOM 8680 C CB . ASN E 1 169 ? 46.246 -10.706 55.768 1.00 53.78 ? 168 ASN E CB 1 ATOM 8681 C CG . ASN E 1 169 ? 45.743 -9.869 56.932 1.00 53.68 ? 168 ASN E CG 1 ATOM 8682 O OD1 . ASN E 1 169 ? 45.795 -10.300 58.087 1.00 56.36 ? 168 ASN E OD1 1 ATOM 8683 N ND2 . ASN E 1 169 ? 45.240 -8.672 56.633 1.00 51.45 ? 168 ASN E ND2 1 ATOM 8684 N N . GLN E 1 170 ? 47.962 -12.902 54.543 1.00 57.65 ? 169 GLN E N 1 ATOM 8685 C CA . GLN E 1 170 ? 48.333 -13.807 53.466 1.00 57.82 ? 169 GLN E CA 1 ATOM 8686 C C . GLN E 1 170 ? 47.281 -13.770 52.378 1.00 55.31 ? 169 GLN E C 1 ATOM 8687 O O . GLN E 1 170 ? 47.534 -14.193 51.246 1.00 56.52 ? 169 GLN E O 1 ATOM 8688 C CB . GLN E 1 170 ? 48.447 -15.242 53.987 1.00 61.44 ? 169 GLN E CB 1 ATOM 8689 C CG . GLN E 1 170 ? 49.227 -15.408 55.292 1.00 64.73 ? 169 GLN E CG 1 ATOM 8690 C CD . GLN E 1 170 ? 50.729 -15.178 55.158 1.00 66.90 ? 169 GLN E CD 1 ATOM 8691 O OE1 . GLN E 1 170 ? 51.461 -15.212 56.160 1.00 68.83 ? 169 GLN E OE1 1 ATOM 8692 N NE2 . GLN E 1 170 ? 51.202 -14.954 53.926 1.00 65.64 ? 169 GLN E NE2 1 ATOM 8693 N N . GLU E 1 171 ? 46.099 -13.260 52.724 1.00 52.67 ? 170 GLU E N 1 ATOM 8694 C CA . GLU E 1 171 ? 44.958 -13.251 51.823 1.00 49.61 ? 170 GLU E CA 1 ATOM 8695 C C . GLU E 1 171 ? 44.768 -11.900 51.150 1.00 46.06 ? 170 GLU E C 1 ATOM 8696 O O . GLU E 1 171 ? 45.299 -10.885 51.599 1.00 44.58 ? 170 GLU E O 1 ATOM 8697 C CB . GLU E 1 171 ? 43.683 -13.614 52.589 1.00 50.09 ? 170 GLU E CB 1 ATOM 8698 C CG . GLU E 1 171 ? 43.697 -14.990 53.252 1.00 53.05 ? 170 GLU E CG 1 ATOM 8699 C CD . GLU E 1 171 ? 44.341 -14.994 54.628 1.00 54.75 ? 170 GLU E CD 1 ATOM 8700 O OE1 . GLU E 1 171 ? 44.666 -13.895 55.133 1.00 54.11 ? 170 GLU E OE1 1 ATOM 8701 O OE2 . GLU E 1 171 ? 44.520 -16.095 55.206 1.00 56.66 ? 170 GLU E OE2 1 ATOM 8702 N N . ASP E 1 172 ? 44.001 -11.916 50.060 1.00 44.35 ? 171 ASP E N 1 ATOM 8703 C CA . ASP E 1 172 ? 43.535 -10.705 49.395 1.00 41.87 ? 171 ASP E CA 1 ATOM 8704 C C . ASP E 1 172 ? 42.521 -9.992 50.282 1.00 39.53 ? 171 ASP E C 1 ATOM 8705 O O . ASP E 1 172 ? 41.822 -10.619 51.075 1.00 39.95 ? 171 ASP E O 1 ATOM 8706 C CB . ASP E 1 172 ? 42.875 -11.039 48.050 1.00 41.64 ? 171 ASP E CB 1 ATOM 8707 C CG . ASP E 1 172 ? 43.878 -11.397 46.966 1.00 43.07 ? 171 ASP E CG 1 ATOM 8708 O OD1 . ASP E 1 172 ? 45.093 -11.291 47.213 1.00 45.23 ? 171 ASP E OD1 1 ATOM 8709 O OD2 . ASP E 1 172 ? 43.452 -11.789 45.857 1.00 43.23 ? 171 ASP E OD2 1 ATOM 8710 N N . LEU E 1 173 ? 42.429 -8.681 50.132 1.00 36.87 ? 172 LEU E N 1 ATOM 8711 C CA . LEU E 1 173 ? 41.590 -7.896 51.007 1.00 36.04 ? 172 LEU E CA 1 ATOM 8712 C C . LEU E 1 173 ? 40.716 -6.943 50.207 1.00 33.70 ? 172 LEU E C 1 ATOM 8713 O O . LEU E 1 173 ? 41.238 -6.083 49.501 1.00 32.63 ? 172 LEU E O 1 ATOM 8714 C CB . LEU E 1 173 ? 42.482 -7.128 51.988 1.00 36.86 ? 172 LEU E CB 1 ATOM 8715 C CG . LEU E 1 173 ? 41.884 -6.573 53.279 1.00 37.02 ? 172 LEU E CG 1 ATOM 8716 C CD1 . LEU E 1 173 ? 41.401 -7.683 54.198 1.00 38.89 ? 172 LEU E CD1 1 ATOM 8717 C CD2 . LEU E 1 173 ? 42.921 -5.736 54.006 1.00 37.56 ? 172 LEU E CD2 1 ATOM 8718 N N . LEU E 1 174 ? 39.393 -7.115 50.316 1.00 32.55 ? 173 LEU E N 1 ATOM 8719 C CA . LEU E 1 174 ? 38.428 -6.191 49.737 1.00 30.44 ? 173 LEU E CA 1 ATOM 8720 C C . LEU E 1 174 ? 38.290 -5.011 50.678 1.00 30.54 ? 173 LEU E C 1 ATOM 8721 O O . LEU E 1 174 ? 37.914 -5.170 51.836 1.00 30.76 ? 173 LEU E O 1 ATOM 8722 C CB . LEU E 1 174 ? 37.055 -6.852 49.545 1.00 30.27 ? 173 LEU E CB 1 ATOM 8723 C CG . LEU E 1 174 ? 35.887 -5.970 49.050 1.00 28.53 ? 173 LEU E CG 1 ATOM 8724 C CD1 . LEU E 1 174 ? 36.174 -5.310 47.720 1.00 27.56 ? 173 LEU E CD1 1 ATOM 8725 C CD2 . LEU E 1 174 ? 34.617 -6.780 48.919 1.00 29.01 ? 173 LEU E CD2 1 ATOM 8726 N N . VAL E 1 175 ? 38.583 -3.820 50.166 1.00 30.12 ? 174 VAL E N 1 ATOM 8727 C CA . VAL E 1 175 ? 38.598 -2.612 50.973 1.00 28.52 ? 174 VAL E CA 1 ATOM 8728 C C . VAL E 1 175 ? 37.591 -1.678 50.358 1.00 26.98 ? 174 VAL E C 1 ATOM 8729 O O . VAL E 1 175 ? 37.536 -1.551 49.141 1.00 25.85 ? 174 VAL E O 1 ATOM 8730 C CB . VAL E 1 175 ? 39.975 -1.944 50.935 1.00 28.82 ? 174 VAL E CB 1 ATOM 8731 C CG1 . VAL E 1 175 ? 39.979 -0.668 51.769 1.00 28.78 ? 174 VAL E CG1 1 ATOM 8732 C CG2 . VAL E 1 175 ? 41.034 -2.922 51.410 1.00 30.78 ? 174 VAL E CG2 1 ATOM 8733 N N . LEU E 1 176 ? 36.797 -1.038 51.206 1.00 26.56 ? 175 LEU E N 1 ATOM 8734 C CA . LEU E 1 176 ? 35.722 -0.176 50.764 1.00 25.73 ? 175 LEU E CA 1 ATOM 8735 C C . LEU E 1 176 ? 35.855 1.203 51.392 1.00 25.08 ? 175 LEU E C 1 ATOM 8736 O O . LEU E 1 176 ? 36.354 1.354 52.508 1.00 26.21 ? 175 LEU E O 1 ATOM 8737 C CB . LEU E 1 176 ? 34.391 -0.770 51.165 1.00 25.95 ? 175 LEU E CB 1 ATOM 8738 C CG . LEU E 1 176 ? 34.223 -2.261 50.906 1.00 27.02 ? 175 LEU E CG 1 ATOM 8739 C CD1 . LEU E 1 176 ? 32.922 -2.702 51.547 1.00 28.34 ? 175 LEU E CD1 1 ATOM 8740 C CD2 . LEU E 1 176 ? 34.215 -2.551 49.423 1.00 27.26 ? 175 LEU E CD2 1 ATOM 8741 N N . TRP E 1 177 ? 35.394 2.202 50.665 1.00 23.39 ? 176 TRP E N 1 ATOM 8742 C CA . TRP E 1 177 ? 35.402 3.575 51.135 1.00 22.13 ? 176 TRP E CA 1 ATOM 8743 C C . TRP E 1 177 ? 34.468 4.349 50.247 1.00 20.79 ? 176 TRP E C 1 ATOM 8744 O O . TRP E 1 177 ? 33.961 3.814 49.276 1.00 21.13 ? 176 TRP E O 1 ATOM 8745 C CB . TRP E 1 177 ? 36.811 4.167 51.066 1.00 22.24 ? 176 TRP E CB 1 ATOM 8746 C CG . TRP E 1 177 ? 37.361 4.378 49.679 1.00 21.18 ? 176 TRP E CG 1 ATOM 8747 C CD1 . TRP E 1 177 ? 37.377 5.550 48.978 1.00 20.72 ? 176 TRP E CD1 1 ATOM 8748 C CD2 . TRP E 1 177 ? 38.017 3.408 48.855 1.00 20.94 ? 176 TRP E CD2 1 ATOM 8749 N NE1 . TRP E 1 177 ? 37.976 5.358 47.756 1.00 20.84 ? 176 TRP E NE1 1 ATOM 8750 C CE2 . TRP E 1 177 ? 38.390 4.055 47.662 1.00 20.73 ? 176 TRP E CE2 1 ATOM 8751 C CE3 . TRP E 1 177 ? 38.323 2.048 49.008 1.00 21.53 ? 176 TRP E CE3 1 ATOM 8752 C CZ2 . TRP E 1 177 ? 39.045 3.388 46.616 1.00 20.93 ? 176 TRP E CZ2 1 ATOM 8753 C CZ3 . TRP E 1 177 ? 38.978 1.390 47.973 1.00 21.37 ? 176 TRP E CZ3 1 ATOM 8754 C CH2 . TRP E 1 177 ? 39.326 2.063 46.794 1.00 21.20 ? 176 TRP E CH2 1 ATOM 8755 N N . GLY E 1 178 ? 34.260 5.615 50.553 1.00 20.54 ? 177 GLY E N 1 ATOM 8756 C CA . GLY E 1 178 ? 33.355 6.416 49.757 1.00 19.56 ? 177 GLY E CA 1 ATOM 8757 C C . GLY E 1 178 ? 33.626 7.887 49.868 1.00 19.17 ? 177 GLY E C 1 ATOM 8758 O O . GLY E 1 178 ? 34.560 8.317 50.554 1.00 19.82 ? 177 GLY E O 1 ATOM 8759 N N . ILE E 1 179 ? 32.804 8.649 49.167 1.00 18.37 ? 178 ILE E N 1 ATOM 8760 C CA . ILE E 1 179 ? 32.873 10.104 49.172 1.00 18.67 ? 178 ILE E CA 1 ATOM 8761 C C . ILE E 1 179 ? 31.451 10.635 49.328 1.00 18.62 ? 178 ILE E C 1 ATOM 8762 O O . ILE E 1 179 ? 30.505 10.016 48.869 1.00 18.13 ? 178 ILE E O 1 ATOM 8763 C CB . ILE E 1 179 ? 33.507 10.651 47.872 1.00 18.75 ? 178 ILE E CB 1 ATOM 8764 C CG1 . ILE E 1 179 ? 33.547 12.181 47.890 1.00 19.51 ? 178 ILE E CG1 1 ATOM 8765 C CG2 . ILE E 1 179 ? 32.758 10.173 46.643 1.00 18.28 ? 178 ILE E CG2 1 ATOM 8766 C CD1 . ILE E 1 179 ? 34.499 12.763 46.885 1.00 20.12 ? 178 ILE E CD1 1 ATOM 8767 N N . HIS E 1 180 ? 31.307 11.781 49.974 1.00 19.68 ? 179 HIS E N 1 ATOM 8768 C CA . HIS E 1 180 ? 30.006 12.401 50.142 1.00 19.57 ? 179 HIS E CA 1 ATOM 8769 C C . HIS E 1 180 ? 29.922 13.589 49.211 1.00 20.59 ? 179 HIS E C 1 ATOM 8770 O O . HIS E 1 180 ? 30.775 14.467 49.258 1.00 21.35 ? 179 HIS E O 1 ATOM 8771 C CB . HIS E 1 180 ? 29.810 12.827 51.592 1.00 19.71 ? 179 HIS E CB 1 ATOM 8772 C CG . HIS E 1 180 ? 28.526 13.546 51.850 1.00 20.50 ? 179 HIS E CG 1 ATOM 8773 N ND1 . HIS E 1 180 ? 28.481 14.809 52.400 1.00 21.24 ? 179 HIS E ND1 1 ATOM 8774 C CD2 . HIS E 1 180 ? 27.237 13.181 51.643 1.00 20.61 ? 179 HIS E CD2 1 ATOM 8775 C CE1 . HIS E 1 180 ? 27.223 15.192 52.517 1.00 21.63 ? 179 HIS E CE1 1 ATOM 8776 N NE2 . HIS E 1 180 ? 26.447 14.221 52.071 1.00 20.95 ? 179 HIS E NE2 1 ATOM 8777 N N . HIS E 1 181 ? 28.891 13.598 48.370 1.00 20.68 ? 180 HIS E N 1 ATOM 8778 C CA . HIS E 1 181 ? 28.566 14.731 47.536 1.00 21.48 ? 180 HIS E CA 1 ATOM 8779 C C . HIS E 1 181 ? 27.521 15.577 48.269 1.00 22.37 ? 180 HIS E C 1 ATOM 8780 O O . HIS E 1 181 ? 26.356 15.197 48.352 1.00 21.08 ? 180 HIS E O 1 ATOM 8781 C CB . HIS E 1 181 ? 28.025 14.251 46.189 1.00 21.54 ? 180 HIS E CB 1 ATOM 8782 C CG . HIS E 1 181 ? 28.947 13.319 45.480 1.00 21.82 ? 180 HIS E CG 1 ATOM 8783 N ND1 . HIS E 1 181 ? 30.169 13.721 44.992 1.00 22.64 ? 180 HIS E ND1 1 ATOM 8784 C CD2 . HIS E 1 181 ? 28.848 12.000 45.202 1.00 21.26 ? 180 HIS E CD2 1 ATOM 8785 C CE1 . HIS E 1 181 ? 30.785 12.696 44.440 1.00 21.91 ? 180 HIS E CE1 1 ATOM 8786 N NE2 . HIS E 1 181 ? 30.004 11.638 44.553 1.00 21.48 ? 180 HIS E NE2 1 ATOM 8787 N N . PRO E 1 182 ? 27.938 16.724 48.830 1.00 24.05 ? 181 PRO E N 1 ATOM 8788 C CA . PRO E 1 182 ? 26.961 17.549 49.558 1.00 24.88 ? 181 PRO E CA 1 ATOM 8789 C C . PRO E 1 182 ? 25.977 18.311 48.657 1.00 25.63 ? 181 PRO E C 1 ATOM 8790 O O . PRO E 1 182 ? 26.117 18.304 47.430 1.00 25.64 ? 181 PRO E O 1 ATOM 8791 C CB . PRO E 1 182 ? 27.844 18.512 50.348 1.00 25.53 ? 181 PRO E CB 1 ATOM 8792 C CG . PRO E 1 182 ? 29.086 18.612 49.544 1.00 25.78 ? 181 PRO E CG 1 ATOM 8793 C CD . PRO E 1 182 ? 29.302 17.272 48.925 1.00 24.31 ? 181 PRO E CD 1 ATOM 8794 N N . ASN E 1 183 ? 24.983 18.940 49.274 1.00 26.11 ? 182 ASN E N 1 ATOM 8795 C CA . ASN E 1 183 ? 23.960 19.682 48.540 1.00 26.90 ? 182 ASN E CA 1 ATOM 8796 C C . ASN E 1 183 ? 24.390 21.083 48.121 1.00 27.98 ? 182 ASN E C 1 ATOM 8797 O O . ASN E 1 183 ? 23.916 21.586 47.102 1.00 28.94 ? 182 ASN E O 1 ATOM 8798 C CB . ASN E 1 183 ? 22.679 19.773 49.369 1.00 27.15 ? 182 ASN E CB 1 ATOM 8799 C CG . ASN E 1 183 ? 22.078 18.415 49.635 1.00 26.62 ? 182 ASN E CG 1 ATOM 8800 O OD1 . ASN E 1 183 ? 21.935 17.626 48.716 1.00 25.65 ? 182 ASN E OD1 1 ATOM 8801 N ND2 . ASN E 1 183 ? 21.730 18.128 50.894 1.00 26.92 ? 182 ASN E ND2 1 ATOM 8802 N N . ASP E 1 184 ? 25.261 21.721 48.896 1.00 28.65 ? 183 ASP E N 1 ATOM 8803 C CA . ASP E 1 184 ? 25.673 23.111 48.584 1.00 31.02 ? 183 ASP E CA 1 ATOM 8804 C C . ASP E 1 184 ? 26.909 23.588 49.347 1.00 31.26 ? 183 ASP E C 1 ATOM 8805 O O . ASP E 1 184 ? 27.395 22.919 50.250 1.00 31.77 ? 183 ASP E O 1 ATOM 8806 C CB . ASP E 1 184 ? 24.503 24.085 48.812 1.00 32.07 ? 183 ASP E CB 1 ATOM 8807 C CG . ASP E 1 184 ? 23.844 23.911 50.172 1.00 32.21 ? 183 ASP E CG 1 ATOM 8808 O OD1 . ASP E 1 184 ? 24.541 23.924 51.197 1.00 31.77 ? 183 ASP E OD1 1 ATOM 8809 O OD2 . ASP E 1 184 ? 22.608 23.762 50.219 1.00 34.00 ? 183 ASP E OD2 1 ATOM 8810 N N . ALA E 1 185 ? 27.405 24.758 48.972 1.00 32.91 ? 184 ALA E N 1 ATOM 8811 C CA . ALA E 1 185 ? 28.615 25.324 49.558 1.00 33.45 ? 184 ALA E CA 1 ATOM 8812 C C . ALA E 1 185 ? 28.543 25.447 51.074 1.00 33.36 ? 184 ALA E C 1 ATOM 8813 O O . ALA E 1 185 ? 29.545 25.242 51.771 1.00 33.34 ? 184 ALA E O 1 ATOM 8814 C CB . ALA E 1 185 ? 28.892 26.693 48.947 1.00 35.71 ? 184 ALA E CB 1 ATOM 8815 N N . ALA E 1 186 ? 27.370 25.823 51.575 1.00 33.25 ? 185 ALA E N 1 ATOM 8816 C CA . ALA E 1 186 ? 27.162 25.962 53.010 1.00 33.18 ? 185 ALA E CA 1 ATOM 8817 C C . ALA E 1 186 ? 27.274 24.604 53.699 1.00 31.33 ? 185 ALA E C 1 ATOM 8818 O O . ALA E 1 186 ? 27.950 24.474 54.706 1.00 31.23 ? 185 ALA E O 1 ATOM 8819 C CB . ALA E 1 186 ? 25.802 26.573 53.280 1.00 33.90 ? 185 ALA E CB 1 ATOM 8820 N N . GLU E 1 187 ? 26.597 23.595 53.165 1.00 29.77 ? 186 GLU E N 1 ATOM 8821 C CA . GLU E 1 187 ? 26.689 22.247 53.735 1.00 28.69 ? 186 GLU E CA 1 ATOM 8822 C C . GLU E 1 187 ? 28.161 21.829 53.828 1.00 28.26 ? 186 GLU E C 1 ATOM 8823 O O . GLU E 1 187 ? 28.593 21.307 54.838 1.00 27.86 ? 186 GLU E O 1 ATOM 8824 C CB . GLU E 1 187 ? 25.900 21.230 52.903 1.00 27.37 ? 186 GLU E CB 1 ATOM 8825 C CG . GLU E 1 187 ? 25.314 20.092 53.720 1.00 27.32 ? 186 GLU E CG 1 ATOM 8826 C CD . GLU E 1 187 ? 24.741 18.981 52.864 1.00 26.71 ? 186 GLU E CD 1 ATOM 8827 O OE1 . GLU E 1 187 ? 25.514 18.237 52.249 1.00 26.44 ? 186 GLU E OE1 1 ATOM 8828 O OE2 . GLU E 1 187 ? 23.509 18.840 52.794 1.00 27.86 ? 186 GLU E OE2 1 ATOM 8829 N N . GLN E 1 188 ? 28.923 22.106 52.775 1.00 28.88 ? 187 GLN E N 1 ATOM 8830 C CA . GLN E 1 188 ? 30.310 21.663 52.664 1.00 29.28 ? 187 GLN E CA 1 ATOM 8831 C C . GLN E 1 188 ? 31.172 22.168 53.817 1.00 31.15 ? 187 GLN E C 1 ATOM 8832 O O . GLN E 1 188 ? 31.922 21.386 54.419 1.00 31.59 ? 187 GLN E O 1 ATOM 8833 C CB . GLN E 1 188 ? 30.896 22.127 51.324 1.00 29.52 ? 187 GLN E CB 1 ATOM 8834 C CG . GLN E 1 188 ? 32.368 21.851 51.123 1.00 29.41 ? 187 GLN E CG 1 ATOM 8835 C CD . GLN E 1 188 ? 32.716 20.362 51.124 1.00 28.03 ? 187 GLN E CD 1 ATOM 8836 O OE1 . GLN E 1 188 ? 31.879 19.501 50.839 1.00 25.39 ? 187 GLN E OE1 1 ATOM 8837 N NE2 . GLN E 1 188 ? 33.982 20.061 51.427 1.00 27.78 ? 187 GLN E NE2 1 ATOM 8838 N N . THR E 1 189 ? 31.064 23.462 54.124 1.00 32.47 ? 188 THR E N 1 ATOM 8839 C CA . THR E 1 189 ? 31.845 24.041 55.198 1.00 34.32 ? 188 THR E CA 1 ATOM 8840 C C . THR E 1 189 ? 31.235 23.708 56.539 1.00 33.93 ? 188 THR E C 1 ATOM 8841 O O . THR E 1 189 ? 31.956 23.577 57.521 1.00 34.16 ? 188 THR E O 1 ATOM 8842 C CB . THR E 1 189 ? 32.006 25.575 55.061 1.00 36.91 ? 188 THR E CB 1 ATOM 8843 O OG1 . THR E 1 189 ? 30.721 26.206 55.036 1.00 36.91 ? 188 THR E OG1 1 ATOM 8844 C CG2 . THR E 1 189 ? 32.761 25.903 53.786 1.00 37.87 ? 188 THR E CG2 1 ATOM 8845 N N . ARG E 1 190 ? 29.916 23.568 56.594 1.00 33.43 ? 189 ARG E N 1 ATOM 8846 C CA . ARG E 1 190 ? 29.285 23.144 57.831 1.00 34.25 ? 189 ARG E CA 1 ATOM 8847 C C . ARG E 1 190 ? 29.817 21.764 58.242 1.00 33.01 ? 189 ARG E C 1 ATOM 8848 O O . ARG E 1 190 ? 30.170 21.564 59.404 1.00 34.05 ? 189 ARG E O 1 ATOM 8849 C CB . ARG E 1 190 ? 27.759 23.129 57.722 1.00 34.98 ? 189 ARG E CB 1 ATOM 8850 C CG . ARG E 1 190 ? 27.078 22.765 59.036 1.00 36.12 ? 189 ARG E CG 1 ATOM 8851 C CD . ARG E 1 190 ? 25.622 23.180 59.065 1.00 37.82 ? 189 ARG E CD 1 ATOM 8852 N NE . ARG E 1 190 ? 24.884 22.648 57.923 1.00 37.73 ? 189 ARG E NE 1 ATOM 8853 C CZ . ARG E 1 190 ? 24.397 21.408 57.836 1.00 38.08 ? 189 ARG E CZ 1 ATOM 8854 N NH1 . ARG E 1 190 ? 24.551 20.532 58.838 1.00 37.77 ? 189 ARG E NH1 1 ATOM 8855 N NH2 . ARG E 1 190 ? 23.749 21.040 56.730 1.00 36.98 ? 189 ARG E NH2 1 ATOM 8856 N N . LEU E 1 191 ? 29.902 20.832 57.297 1.00 30.59 ? 190 LEU E N 1 ATOM 8857 C CA . LEU E 1 191 ? 30.336 19.476 57.628 1.00 29.94 ? 190 LEU E CA 1 ATOM 8858 C C . LEU E 1 191 ? 31.858 19.308 57.649 1.00 30.31 ? 190 LEU E C 1 ATOM 8859 O O . LEU E 1 191 ? 32.376 18.587 58.492 1.00 29.52 ? 190 LEU E O 1 ATOM 8860 C CB . LEU E 1 191 ? 29.747 18.440 56.665 1.00 28.02 ? 190 LEU E CB 1 ATOM 8861 C CG . LEU E 1 191 ? 28.231 18.365 56.408 1.00 27.52 ? 190 LEU E CG 1 ATOM 8862 C CD1 . LEU E 1 191 ? 27.833 16.926 56.071 1.00 25.67 ? 190 LEU E CD1 1 ATOM 8863 C CD2 . LEU E 1 191 ? 27.419 18.882 57.580 1.00 28.51 ? 190 LEU E CD2 1 ATOM 8864 N N . TYR E 1 192 ? 32.564 19.956 56.722 1.00 30.77 ? 191 TYR E N 1 ATOM 8865 C CA . TYR E 1 192 ? 33.981 19.660 56.509 1.00 31.49 ? 191 TYR E CA 1 ATOM 8866 C C . TYR E 1 192 ? 34.911 20.878 56.538 1.00 34.14 ? 191 TYR E C 1 ATOM 8867 O O . TYR E 1 192 ? 36.105 20.733 56.305 1.00 34.81 ? 191 TYR E O 1 ATOM 8868 C CB . TYR E 1 192 ? 34.159 18.936 55.176 1.00 30.21 ? 191 TYR E CB 1 ATOM 8869 C CG . TYR E 1 192 ? 33.170 17.814 54.926 1.00 28.01 ? 191 TYR E CG 1 ATOM 8870 C CD1 . TYR E 1 192 ? 33.270 16.623 55.608 1.00 27.43 ? 191 TYR E CD1 1 ATOM 8871 C CD2 . TYR E 1 192 ? 32.147 17.951 53.994 1.00 27.38 ? 191 TYR E CD2 1 ATOM 8872 C CE1 . TYR E 1 192 ? 32.379 15.589 55.381 1.00 26.25 ? 191 TYR E CE1 1 ATOM 8873 C CE2 . TYR E 1 192 ? 31.247 16.926 53.760 1.00 26.34 ? 191 TYR E CE2 1 ATOM 8874 C CZ . TYR E 1 192 ? 31.375 15.744 54.464 1.00 25.87 ? 191 TYR E CZ 1 ATOM 8875 O OH . TYR E 1 192 ? 30.516 14.695 54.250 1.00 25.85 ? 191 TYR E OH 1 ATOM 8876 N N . GLN E 1 193 ? 34.354 22.061 56.793 1.00 35.85 ? 192 GLN E N 1 ATOM 8877 C CA . GLN E 1 193 ? 35.091 23.322 56.897 1.00 38.40 ? 192 GLN E CA 1 ATOM 8878 C C . GLN E 1 193 ? 35.737 23.815 55.606 1.00 38.74 ? 192 GLN E C 1 ATOM 8879 O O . GLN E 1 193 ? 35.537 24.959 55.198 1.00 40.81 ? 192 GLN E O 1 ATOM 8880 C CB . GLN E 1 193 ? 36.140 23.257 58.018 1.00 40.61 ? 192 GLN E CB 1 ATOM 8881 C CG . GLN E 1 193 ? 36.564 24.632 58.527 1.00 43.34 ? 192 GLN E CG 1 ATOM 8882 C CD . GLN E 1 193 ? 35.392 25.447 59.075 1.00 44.50 ? 192 GLN E CD 1 ATOM 8883 O OE1 . GLN E 1 193 ? 34.481 24.912 59.711 1.00 43.15 ? 192 GLN E OE1 1 ATOM 8884 N NE2 . GLN E 1 193 ? 35.416 26.749 58.828 1.00 46.74 ? 192 GLN E NE2 1 ATOM 8885 N N . ASN E 1 194 ? 36.544 22.972 54.990 1.00 37.93 ? 193 ASN E N 1 ATOM 8886 C CA . ASN E 1 194 ? 37.242 23.331 53.762 1.00 38.42 ? 193 ASN E CA 1 ATOM 8887 C C . ASN E 1 194 ? 36.287 23.309 52.576 1.00 37.31 ? 193 ASN E C 1 ATOM 8888 O O . ASN E 1 194 ? 35.537 22.357 52.417 1.00 35.90 ? 193 ASN E O 1 ATOM 8889 C CB . ASN E 1 194 ? 38.386 22.355 53.520 1.00 37.93 ? 193 ASN E CB 1 ATOM 8890 C CG . ASN E 1 194 ? 39.222 22.146 54.751 1.00 37.83 ? 193 ASN E CG 1 ATOM 8891 O OD1 . ASN E 1 194 ? 39.666 23.109 55.355 1.00 40.31 ? 193 ASN E OD1 1 ATOM 8892 N ND2 . ASN E 1 194 ? 39.419 20.894 55.147 1.00 36.30 ? 193 ASN E ND2 1 ATOM 8893 N N . PRO E 1 195 ? 36.287 24.378 51.758 1.00 39.07 ? 194 PRO E N 1 ATOM 8894 C CA . PRO E 1 195 ? 35.390 24.422 50.593 1.00 38.31 ? 194 PRO E CA 1 ATOM 8895 C C . PRO E 1 195 ? 35.812 23.536 49.409 1.00 38.00 ? 194 PRO E C 1 ATOM 8896 O O . PRO E 1 195 ? 34.949 23.049 48.684 1.00 38.66 ? 194 PRO E O 1 ATOM 8897 C CB . PRO E 1 195 ? 35.399 25.907 50.200 1.00 39.96 ? 194 PRO E CB 1 ATOM 8898 C CG . PRO E 1 195 ? 36.641 26.467 50.776 1.00 41.14 ? 194 PRO E CG 1 ATOM 8899 C CD . PRO E 1 195 ? 36.950 25.675 52.004 1.00 40.30 ? 194 PRO E CD 1 ATOM 8900 N N . THR E 1 196 ? 37.113 23.333 49.215 1.00 39.05 ? 195 THR E N 1 ATOM 8901 C CA . THR E 1 196 ? 37.635 22.554 48.085 1.00 38.98 ? 195 THR E CA 1 ATOM 8902 C C . THR E 1 196 ? 38.377 21.332 48.603 1.00 37.27 ? 195 THR E C 1 ATOM 8903 O O . THR E 1 196 ? 39.473 21.460 49.183 1.00 39.14 ? 195 THR E O 1 ATOM 8904 C CB . THR E 1 196 ? 38.638 23.375 47.242 1.00 41.84 ? 195 THR E CB 1 ATOM 8905 O OG1 . THR E 1 196 ? 38.012 24.561 46.747 1.00 43.71 ? 195 THR E OG1 1 ATOM 8906 C CG2 . THR E 1 196 ? 39.164 22.549 46.068 1.00 41.66 ? 195 THR E CG2 1 ATOM 8907 N N . THR E 1 197 ? 37.814 20.150 48.379 1.00 33.95 ? 196 THR E N 1 ATOM 8908 C CA . THR E 1 197 ? 38.352 18.953 49.003 1.00 32.50 ? 196 THR E CA 1 ATOM 8909 C C . THR E 1 197 ? 38.578 17.830 48.016 1.00 31.52 ? 196 THR E C 1 ATOM 8910 O O . THR E 1 197 ? 38.107 17.873 46.885 1.00 30.72 ? 196 THR E O 1 ATOM 8911 C CB . THR E 1 197 ? 37.446 18.437 50.148 1.00 31.05 ? 196 THR E CB 1 ATOM 8912 O OG1 . THR E 1 197 ? 36.264 17.862 49.603 1.00 29.39 ? 196 THR E OG1 1 ATOM 8913 C CG2 . THR E 1 197 ? 37.074 19.567 51.120 1.00 32.20 ? 196 THR E CG2 1 ATOM 8914 N N . TYR E 1 198 ? 39.308 16.820 48.476 1.00 30.79 ? 197 TYR E N 1 ATOM 8915 C CA . TYR E 1 198 ? 39.668 15.694 47.653 1.00 30.16 ? 197 TYR E CA 1 ATOM 8916 C C . TYR E 1 198 ? 39.866 14.462 48.514 1.00 28.86 ? 197 TYR E C 1 ATOM 8917 O O . TYR E 1 198 ? 39.952 14.542 49.731 1.00 28.92 ? 197 TYR E O 1 ATOM 8918 C CB . TYR E 1 198 ? 40.971 15.990 46.899 1.00 32.16 ? 197 TYR E CB 1 ATOM 8919 C CG . TYR E 1 198 ? 42.147 16.140 47.838 1.00 33.52 ? 197 TYR E CG 1 ATOM 8920 C CD1 . TYR E 1 198 ? 42.451 17.372 48.409 1.00 35.09 ? 197 TYR E CD1 1 ATOM 8921 C CD2 . TYR E 1 198 ? 42.924 15.044 48.192 1.00 33.29 ? 197 TYR E CD2 1 ATOM 8922 C CE1 . TYR E 1 198 ? 43.503 17.511 49.290 1.00 35.78 ? 197 TYR E CE1 1 ATOM 8923 C CE2 . TYR E 1 198 ? 43.980 15.179 49.072 1.00 34.43 ? 197 TYR E CE2 1 ATOM 8924 C CZ . TYR E 1 198 ? 44.264 16.414 49.619 1.00 35.63 ? 197 TYR E CZ 1 ATOM 8925 O OH . TYR E 1 198 ? 45.323 16.554 50.497 1.00 37.03 ? 197 TYR E OH 1 ATOM 8926 N N . ILE E 1 199 ? 39.932 13.322 47.852 1.00 28.27 ? 198 ILE E N 1 ATOM 8927 C CA . ILE E 1 199 ? 40.305 12.063 48.472 1.00 28.08 ? 198 ILE E CA 1 ATOM 8928 C C . ILE E 1 199 ? 41.275 11.416 47.491 1.00 28.58 ? 198 ILE E C 1 ATOM 8929 O O . ILE E 1 199 ? 40.893 11.127 46.356 1.00 26.22 ? 198 ILE E O 1 ATOM 8930 C CB . ILE E 1 199 ? 39.084 11.148 48.678 1.00 27.23 ? 198 ILE E CB 1 ATOM 8931 C CG1 . ILE E 1 199 ? 38.031 11.851 49.532 1.00 27.20 ? 198 ILE E CG1 1 ATOM 8932 C CG2 . ILE E 1 199 ? 39.493 9.829 49.332 1.00 27.70 ? 198 ILE E CG2 1 ATOM 8933 C CD1 . ILE E 1 199 ? 36.702 11.140 49.539 1.00 26.62 ? 198 ILE E CD1 1 ATOM 8934 N N . SER E 1 200 ? 42.535 11.269 47.905 1.00 30.25 ? 199 SER E N 1 ATOM 8935 C CA . SER E 1 200 ? 43.521 10.509 47.145 1.00 30.85 ? 199 SER E CA 1 ATOM 8936 C C . SER E 1 200 ? 43.515 9.106 47.687 1.00 29.75 ? 199 SER E C 1 ATOM 8937 O O . SER E 1 200 ? 43.531 8.925 48.888 1.00 31.63 ? 199 SER E O 1 ATOM 8938 C CB . SER E 1 200 ? 44.933 11.071 47.336 1.00 33.40 ? 199 SER E CB 1 ATOM 8939 O OG . SER E 1 200 ? 44.942 12.490 47.345 1.00 36.24 ? 199 SER E OG 1 ATOM 8940 N N . VAL E 1 201 ? 43.512 8.110 46.815 1.00 28.88 ? 200 VAL E N 1 ATOM 8941 C CA . VAL E 1 201 ? 43.762 6.724 47.228 1.00 28.10 ? 200 VAL E CA 1 ATOM 8942 C C . VAL E 1 201 ? 44.753 6.068 46.253 1.00 28.53 ? 200 VAL E C 1 ATOM 8943 O O . VAL E 1 201 ? 44.545 6.082 45.039 1.00 28.23 ? 200 VAL E O 1 ATOM 8944 C CB . VAL E 1 201 ? 42.468 5.895 47.252 1.00 26.64 ? 200 VAL E CB 1 ATOM 8945 C CG1 . VAL E 1 201 ? 42.710 4.564 47.949 1.00 26.81 ? 200 VAL E CG1 1 ATOM 8946 C CG2 . VAL E 1 201 ? 41.352 6.671 47.932 1.00 26.42 ? 200 VAL E CG2 1 ATOM 8947 N N . GLY E 1 202 ? 45.832 5.505 46.780 1.00 28.84 ? 201 GLY E N 1 ATOM 8948 C CA . GLY E 1 202 ? 46.790 4.811 45.945 1.00 29.18 ? 201 GLY E CA 1 ATOM 8949 C C . GLY E 1 202 ? 47.109 3.453 46.529 1.00 29.14 ? 201 GLY E C 1 ATOM 8950 O O . GLY E 1 202 ? 47.077 3.279 47.746 1.00 29.72 ? 201 GLY E O 1 ATOM 8951 N N . THR E 1 203 ? 47.398 2.499 45.658 1.00 28.55 ? 202 THR E N 1 ATOM 8952 C CA . THR E 1 203 ? 47.993 1.226 46.045 1.00 29.96 ? 202 THR E CA 1 ATOM 8953 C C . THR E 1 203 ? 49.151 1.002 45.068 1.00 31.52 ? 202 THR E C 1 ATOM 8954 O O . THR E 1 203 ? 49.770 1.979 44.639 1.00 31.68 ? 202 THR E O 1 ATOM 8955 C CB . THR E 1 203 ? 46.973 0.070 45.993 1.00 29.38 ? 202 THR E CB 1 ATOM 8956 O OG1 . THR E 1 203 ? 46.559 -0.148 44.638 1.00 29.35 ? 202 THR E OG1 1 ATOM 8957 C CG2 . THR E 1 203 ? 45.762 0.372 46.844 1.00 27.91 ? 202 THR E CG2 1 ATOM 8958 N N . SER E 1 204 ? 49.452 -0.246 44.700 1.00 32.44 ? 203 SER E N 1 ATOM 8959 C CA . SER E 1 204 ? 50.455 -0.483 43.658 1.00 33.94 ? 203 SER E CA 1 ATOM 8960 C C . SER E 1 204 ? 49.860 -0.343 42.252 1.00 33.65 ? 203 SER E C 1 ATOM 8961 O O . SER E 1 204 ? 50.597 -0.086 41.302 1.00 34.36 ? 203 SER E O 1 ATOM 8962 C CB . SER E 1 204 ? 51.122 -1.852 43.824 1.00 35.61 ? 203 SER E CB 1 ATOM 8963 O OG . SER E 1 204 ? 50.175 -2.898 43.785 1.00 35.38 ? 203 SER E OG 1 ATOM 8964 N N . THR E 1 205 ? 48.539 -0.502 42.140 1.00 32.77 ? 204 THR E N 1 ATOM 8965 C CA . THR E 1 205 ? 47.797 -0.406 40.862 1.00 32.91 ? 204 THR E CA 1 ATOM 8966 C C . THR E 1 205 ? 46.790 0.752 40.842 1.00 31.53 ? 204 THR E C 1 ATOM 8967 O O . THR E 1 205 ? 46.515 1.319 39.798 1.00 32.22 ? 204 THR E O 1 ATOM 8968 C CB . THR E 1 205 ? 47.019 -1.717 40.554 1.00 32.57 ? 204 THR E CB 1 ATOM 8969 O OG1 . THR E 1 205 ? 46.330 -2.164 41.730 1.00 32.43 ? 204 THR E OG1 1 ATOM 8970 C CG2 . THR E 1 205 ? 47.969 -2.819 40.117 1.00 34.39 ? 204 THR E CG2 1 ATOM 8971 N N . LEU E 1 206 ? 46.256 1.109 41.998 1.00 30.39 ? 205 LEU E N 1 ATOM 8972 C CA . LEU E 1 206 ? 45.246 2.152 42.094 1.00 28.91 ? 205 LEU E CA 1 ATOM 8973 C C . LEU E 1 206 ? 45.894 3.524 42.262 1.00 29.00 ? 205 LEU E C 1 ATOM 8974 O O . LEU E 1 206 ? 46.759 3.698 43.082 1.00 29.95 ? 205 LEU E O 1 ATOM 8975 C CB . LEU E 1 206 ? 44.331 1.850 43.282 1.00 28.15 ? 205 LEU E CB 1 ATOM 8976 C CG . LEU E 1 206 ? 43.110 2.752 43.514 1.00 27.14 ? 205 LEU E CG 1 ATOM 8977 C CD1 . LEU E 1 206 ? 42.015 2.488 42.474 1.00 26.45 ? 205 LEU E CD1 1 ATOM 8978 C CD2 . LEU E 1 206 ? 42.595 2.524 44.921 1.00 26.31 ? 205 LEU E CD2 1 ATOM 8979 N N . ASN E 1 207 ? 45.478 4.483 41.452 1.00 29.14 ? 206 ASN E N 1 ATOM 8980 C CA . ASN E 1 207 ? 45.895 5.883 41.557 1.00 29.94 ? 206 ASN E CA 1 ATOM 8981 C C . ASN E 1 207 ? 44.609 6.706 41.364 1.00 30.03 ? 206 ASN E C 1 ATOM 8982 O O . ASN E 1 207 ? 44.209 7.034 40.242 1.00 29.04 ? 206 ASN E O 1 ATOM 8983 C CB . ASN E 1 207 ? 46.945 6.197 40.477 1.00 31.09 ? 206 ASN E CB 1 ATOM 8984 C CG . ASN E 1 207 ? 47.328 7.663 40.418 1.00 31.10 ? 206 ASN E CG 1 ATOM 8985 O OD1 . ASN E 1 207 ? 47.340 8.353 41.425 1.00 31.84 ? 206 ASN E OD1 1 ATOM 8986 N ND2 . ASN E 1 207 ? 47.667 8.133 39.237 1.00 31.75 ? 206 ASN E ND2 1 ATOM 8987 N N . GLN E 1 208 ? 43.943 6.977 42.477 1.00 30.78 ? 207 GLN E N 1 ATOM 8988 C CA . GLN E 1 208 ? 42.624 7.590 42.477 1.00 30.54 ? 207 GLN E CA 1 ATOM 8989 C C . GLN E 1 208 ? 42.664 8.945 43.175 1.00 30.88 ? 207 GLN E C 1 ATOM 8990 O O . GLN E 1 208 ? 43.291 9.089 44.215 1.00 29.95 ? 207 GLN E O 1 ATOM 8991 C CB . GLN E 1 208 ? 41.653 6.672 43.193 1.00 30.04 ? 207 GLN E CB 1 ATOM 8992 C CG . GLN E 1 208 ? 40.323 7.332 43.519 1.00 31.24 ? 207 GLN E CG 1 ATOM 8993 C CD . GLN E 1 208 ? 39.318 6.355 44.077 1.00 30.78 ? 207 GLN E CD 1 ATOM 8994 O OE1 . GLN E 1 208 ? 39.010 6.381 45.274 1.00 30.25 ? 207 GLN E OE1 1 ATOM 8995 N NE2 . GLN E 1 208 ? 38.811 5.473 43.217 1.00 31.11 ? 207 GLN E NE2 1 ATOM 8996 N N . ARG E 1 209 ? 42.005 9.931 42.581 1.00 32.60 ? 208 ARG E N 1 ATOM 8997 C CA . ARG E 1 209 ? 41.778 11.224 43.223 1.00 34.72 ? 208 ARG E CA 1 ATOM 8998 C C . ARG E 1 209 ? 40.340 11.683 42.998 1.00 34.80 ? 208 ARG E C 1 ATOM 8999 O O . ARG E 1 209 ? 39.978 12.055 41.890 1.00 37.01 ? 208 ARG E O 1 ATOM 9000 C CB . ARG E 1 209 ? 42.734 12.261 42.678 1.00 37.78 ? 208 ARG E CB 1 ATOM 9001 C CG . ARG E 1 209 ? 42.515 13.655 43.243 1.00 40.04 ? 208 ARG E CG 1 ATOM 9002 C CD . ARG E 1 209 ? 43.797 14.186 43.860 1.00 42.99 ? 208 ARG E CD 1 ATOM 9003 N NE . ARG E 1 209 ? 43.663 15.579 44.266 1.00 44.64 ? 208 ARG E NE 1 ATOM 9004 C CZ . ARG E 1 209 ? 44.528 16.222 45.042 1.00 47.01 ? 208 ARG E CZ 1 ATOM 9005 N NH1 . ARG E 1 209 ? 45.602 15.599 45.518 1.00 47.46 ? 208 ARG E NH1 1 ATOM 9006 N NH2 . ARG E 1 209 ? 44.311 17.499 45.352 1.00 48.93 ? 208 ARG E NH2 1 ATOM 9007 N N . LEU E 1 210 ? 39.537 11.662 44.061 1.00 34.76 ? 209 LEU E N 1 ATOM 9008 C CA . LEU E 1 210 ? 38.109 12.013 44.001 1.00 33.99 ? 209 LEU E CA 1 ATOM 9009 C C . LEU E 1 210 ? 37.865 13.434 44.461 1.00 34.56 ? 209 LEU E C 1 ATOM 9010 O O . LEU E 1 210 ? 38.405 13.850 45.478 1.00 35.65 ? 209 LEU E O 1 ATOM 9011 C CB . LEU E 1 210 ? 37.308 11.081 44.905 1.00 32.49 ? 209 LEU E CB 1 ATOM 9012 C CG . LEU E 1 210 ? 37.440 9.593 44.596 1.00 31.85 ? 209 LEU E CG 1 ATOM 9013 C CD1 . LEU E 1 210 ? 36.772 8.779 45.682 1.00 31.23 ? 209 LEU E CD1 1 ATOM 9014 C CD2 . LEU E 1 210 ? 36.836 9.280 43.237 1.00 32.54 ? 209 LEU E CD2 1 ATOM 9015 N N . VAL E 1 211 ? 37.054 14.174 43.710 1.00 35.01 ? 210 VAL E N 1 ATOM 9016 C CA . VAL E 1 211 ? 36.589 15.495 44.126 1.00 35.39 ? 210 VAL E CA 1 ATOM 9017 C C . VAL E 1 211 ? 35.064 15.445 44.273 1.00 33.91 ? 210 VAL E C 1 ATOM 9018 O O . VAL E 1 211 ? 34.390 14.955 43.379 1.00 33.75 ? 210 VAL E O 1 ATOM 9019 C CB . VAL E 1 211 ? 36.983 16.578 43.098 1.00 36.83 ? 210 VAL E CB 1 ATOM 9020 C CG1 . VAL E 1 211 ? 36.303 17.909 43.404 1.00 37.48 ? 210 VAL E CG1 1 ATOM 9021 C CG2 . VAL E 1 211 ? 38.494 16.749 43.060 1.00 37.30 ? 210 VAL E CG2 1 ATOM 9022 N N . PRO E 1 212 ? 34.518 15.945 45.400 1.00 33.49 ? 211 PRO E N 1 ATOM 9023 C CA . PRO E 1 212 ? 33.053 15.990 45.550 1.00 33.55 ? 211 PRO E CA 1 ATOM 9024 C C . PRO E 1 212 ? 32.358 16.858 44.495 1.00 33.61 ? 211 PRO E C 1 ATOM 9025 O O . PRO E 1 212 ? 32.872 17.907 44.119 1.00 35.69 ? 211 PRO E O 1 ATOM 9026 C CB . PRO E 1 212 ? 32.846 16.596 46.949 1.00 33.14 ? 211 PRO E CB 1 ATOM 9027 C CG . PRO E 1 212 ? 34.137 16.424 47.660 1.00 32.98 ? 211 PRO E CG 1 ATOM 9028 C CD . PRO E 1 212 ? 35.209 16.415 46.614 1.00 33.73 ? 211 PRO E CD 1 ATOM 9029 N N . LYS E 1 213 ? 31.215 16.386 44.013 1.00 32.49 ? 212 LYS E N 1 ATOM 9030 C CA . LYS E 1 213 ? 30.381 17.096 43.057 1.00 32.93 ? 212 LYS E CA 1 ATOM 9031 C C . LYS E 1 213 ? 29.197 17.689 43.774 1.00 31.61 ? 212 LYS E C 1 ATOM 9032 O O . LYS E 1 213 ? 28.299 16.970 44.179 1.00 31.62 ? 212 LYS E O 1 ATOM 9033 C CB . LYS E 1 213 ? 29.866 16.140 41.978 1.00 32.56 ? 212 LYS E CB 1 ATOM 9034 C CG . LYS E 1 213 ? 30.956 15.565 41.100 1.00 33.05 ? 212 LYS E CG 1 ATOM 9035 C CD . LYS E 1 213 ? 30.391 14.729 39.960 1.00 33.03 ? 212 LYS E CD 1 ATOM 9036 C CE . LYS E 1 213 ? 29.851 13.406 40.447 1.00 32.84 ? 212 LYS E CE 1 ATOM 9037 N NZ . LYS E 1 213 ? 29.870 12.407 39.346 1.00 33.88 ? 212 LYS E NZ 1 ATOM 9038 N N . ILE E 1 214 ? 29.198 19.004 43.944 1.00 31.79 ? 213 ILE E N 1 ATOM 9039 C CA . ILE E 1 214 ? 28.015 19.688 44.431 1.00 30.60 ? 213 ILE E CA 1 ATOM 9040 C C . ILE E 1 214 ? 27.042 19.849 43.271 1.00 30.02 ? 213 ILE E C 1 ATOM 9041 O O . ILE E 1 214 ? 27.405 20.315 42.189 1.00 29.73 ? 213 ILE E O 1 ATOM 9042 C CB . ILE E 1 214 ? 28.341 21.058 45.039 1.00 32.35 ? 213 ILE E CB 1 ATOM 9043 C CG1 . ILE E 1 214 ? 28.972 20.864 46.418 1.00 32.26 ? 213 ILE E CG1 1 ATOM 9044 C CG2 . ILE E 1 214 ? 27.082 21.914 45.143 1.00 33.14 ? 213 ILE E CG2 1 ATOM 9045 C CD1 . ILE E 1 214 ? 29.730 22.080 46.907 1.00 34.08 ? 213 ILE E CD1 1 ATOM 9046 N N . ALA E 1 215 ? 25.810 19.420 43.509 1.00 28.94 ? 214 ALA E N 1 ATOM 9047 C CA . ALA E 1 215 ? 24.683 19.728 42.639 1.00 28.82 ? 214 ALA E CA 1 ATOM 9048 C C . ALA E 1 215 ? 23.408 19.732 43.485 1.00 28.07 ? 214 ALA E C 1 ATOM 9049 O O . ALA E 1 215 ? 23.434 19.341 44.670 1.00 27.12 ? 214 ALA E O 1 ATOM 9050 C CB . ALA E 1 215 ? 24.585 18.710 41.515 1.00 28.70 ? 214 ALA E CB 1 ATOM 9051 N N . THR E 1 216 ? 22.312 20.186 42.875 1.00 27.77 ? 215 THR E N 1 ATOM 9052 C CA . THR E 1 216 ? 21.007 20.286 43.520 1.00 27.34 ? 215 THR E CA 1 ATOM 9053 C C . THR E 1 216 ? 20.154 19.113 43.072 1.00 27.08 ? 215 THR E C 1 ATOM 9054 O O . THR E 1 216 ? 19.719 19.056 41.926 1.00 27.66 ? 215 THR E O 1 ATOM 9055 C CB . THR E 1 216 ? 20.319 21.595 43.122 1.00 28.77 ? 215 THR E CB 1 ATOM 9056 O OG1 . THR E 1 216 ? 21.167 22.684 43.482 1.00 29.65 ? 215 THR E OG1 1 ATOM 9057 C CG2 . THR E 1 216 ? 18.953 21.746 43.797 1.00 29.05 ? 215 THR E CG2 1 ATOM 9058 N N . ARG E 1 217 ? 19.902 18.190 43.987 1.00 26.41 ? 216 ARG E N 1 ATOM 9059 C CA . ARG E 1 217 ? 19.340 16.896 43.644 1.00 26.00 ? 216 ARG E CA 1 ATOM 9060 C C . ARG E 1 217 ? 18.014 16.654 44.378 1.00 26.26 ? 216 ARG E C 1 ATOM 9061 O O . ARG E 1 217 ? 17.726 17.276 45.403 1.00 26.91 ? 216 ARG E O 1 ATOM 9062 C CB . ARG E 1 217 ? 20.387 15.816 43.959 1.00 24.96 ? 216 ARG E CB 1 ATOM 9063 C CG . ARG E 1 217 ? 21.658 15.962 43.100 1.00 26.31 ? 216 ARG E CG 1 ATOM 9064 C CD . ARG E 1 217 ? 22.873 15.154 43.583 1.00 25.71 ? 216 ARG E CD 1 ATOM 9065 N NE . ARG E 1 217 ? 23.187 15.571 44.938 1.00 26.64 ? 216 ARG E NE 1 ATOM 9066 C CZ . ARG E 1 217 ? 24.342 16.040 45.391 1.00 26.49 ? 216 ARG E CZ 1 ATOM 9067 N NH1 . ARG E 1 217 ? 25.441 16.104 44.647 1.00 26.66 ? 216 ARG E NH1 1 ATOM 9068 N NH2 . ARG E 1 217 ? 24.386 16.419 46.655 1.00 26.80 ? 216 ARG E NH2 1 ATOM 9069 N N . SER E 1 218 ? 17.204 15.762 43.830 1.00 26.45 ? 217 SER E N 1 ATOM 9070 C CA . SER E 1 218 ? 15.931 15.391 44.421 1.00 27.21 ? 217 SER E CA 1 ATOM 9071 C C . SER E 1 218 ? 16.155 14.524 45.637 1.00 27.03 ? 217 SER E C 1 ATOM 9072 O O . SER E 1 218 ? 17.128 13.787 45.694 1.00 27.18 ? 217 SER E O 1 ATOM 9073 C CB . SER E 1 218 ? 15.101 14.616 43.406 1.00 27.66 ? 217 SER E CB 1 ATOM 9074 O OG . SER E 1 218 ? 15.132 15.279 42.160 1.00 28.99 ? 217 SER E OG 1 ATOM 9075 N N . LYS E 1 219 ? 15.244 14.597 46.599 1.00 28.36 ? 218 LYS E N 1 ATOM 9076 C CA . LYS E 1 219 ? 15.365 13.808 47.820 1.00 28.79 ? 218 LYS E CA 1 ATOM 9077 C C . LYS E 1 219 ? 15.138 12.319 47.568 1.00 28.14 ? 218 LYS E C 1 ATOM 9078 O O . LYS E 1 219 ? 14.136 11.938 47.006 1.00 29.22 ? 218 LYS E O 1 ATOM 9079 C CB . LYS E 1 219 ? 14.366 14.285 48.869 1.00 30.42 ? 218 LYS E CB 1 ATOM 9080 C CG . LYS E 1 219 ? 14.671 15.643 49.485 1.00 32.35 ? 218 LYS E CG 1 ATOM 9081 C CD . LYS E 1 219 ? 13.873 15.817 50.770 1.00 34.45 ? 218 LYS E CD 1 ATOM 9082 C CE . LYS E 1 219 ? 13.847 17.258 51.229 1.00 36.97 ? 218 LYS E CE 1 ATOM 9083 N NZ . LYS E 1 219 ? 15.226 17.805 51.381 1.00 37.62 ? 218 LYS E NZ 1 ATOM 9084 N N . VAL E 1 220 ? 16.077 11.483 47.985 1.00 27.61 ? 219 VAL E N 1 ATOM 9085 C CA . VAL E 1 220 ? 15.890 10.034 47.952 1.00 27.50 ? 219 VAL E CA 1 ATOM 9086 C C . VAL E 1 220 ? 16.079 9.590 49.388 1.00 27.17 ? 219 VAL E C 1 ATOM 9087 O O . VAL E 1 220 ? 17.053 10.000 50.025 1.00 26.74 ? 219 VAL E O 1 ATOM 9088 C CB . VAL E 1 220 ? 16.892 9.342 47.008 1.00 26.55 ? 219 VAL E CB 1 ATOM 9089 C CG1 . VAL E 1 220 ? 16.717 7.834 47.044 1.00 26.77 ? 219 VAL E CG1 1 ATOM 9090 C CG2 . VAL E 1 220 ? 16.700 9.841 45.588 1.00 27.40 ? 219 VAL E CG2 1 ATOM 9091 N N . ASN E 1 221 ? 15.142 8.793 49.905 1.00 26.63 ? 220 ASN E N 1 ATOM 9092 C CA . ASN E 1 221 ? 15.076 8.499 51.344 1.00 26.74 ? 220 ASN E CA 1 ATOM 9093 C C . ASN E 1 221 ? 15.330 9.755 52.190 1.00 25.65 ? 220 ASN E C 1 ATOM 9094 O O . ASN E 1 221 ? 16.111 9.741 53.137 1.00 25.54 ? 220 ASN E O 1 ATOM 9095 C CB . ASN E 1 221 ? 16.051 7.374 51.718 1.00 26.77 ? 220 ASN E CB 1 ATOM 9096 C CG . ASN E 1 221 ? 15.822 6.114 50.898 1.00 27.97 ? 220 ASN E CG 1 ATOM 9097 O OD1 . ASN E 1 221 ? 14.697 5.848 50.467 1.00 29.08 ? 220 ASN E OD1 1 ATOM 9098 N ND2 . ASN E 1 221 ? 16.891 5.341 50.660 1.00 27.40 ? 220 ASN E ND2 1 ATOM 9099 N N . GLY E 1 222 ? 14.656 10.838 51.826 1.00 25.95 ? 221 GLY E N 1 ATOM 9100 C CA . GLY E 1 222 ? 14.773 12.118 52.521 1.00 25.80 ? 221 GLY E CA 1 ATOM 9101 C C . GLY E 1 222 ? 16.047 12.928 52.323 1.00 25.00 ? 221 GLY E C 1 ATOM 9102 O O . GLY E 1 222 ? 16.172 13.982 52.921 1.00 27.32 ? 221 GLY E O 1 ATOM 9103 N N . GLN E 1 223 ? 16.981 12.475 51.487 1.00 23.98 ? 222 GLN E N 1 ATOM 9104 C CA . GLN E 1 223 ? 18.274 13.150 51.338 1.00 23.63 ? 222 GLN E CA 1 ATOM 9105 C C . GLN E 1 223 ? 18.573 13.593 49.921 1.00 22.64 ? 222 GLN E C 1 ATOM 9106 O O . GLN E 1 223 ? 18.459 12.815 48.990 1.00 22.37 ? 222 GLN E O 1 ATOM 9107 C CB . GLN E 1 223 ? 19.432 12.255 51.781 1.00 24.16 ? 222 GLN E CB 1 ATOM 9108 C CG . GLN E 1 223 ? 19.273 11.644 53.159 1.00 25.67 ? 222 GLN E CG 1 ATOM 9109 C CD . GLN E 1 223 ? 19.278 12.662 54.269 1.00 27.50 ? 222 GLN E CD 1 ATOM 9110 O OE1 . GLN E 1 223 ? 19.737 13.803 54.109 1.00 28.37 ? 222 GLN E OE1 1 ATOM 9111 N NE2 . GLN E 1 223 ? 18.782 12.250 55.418 1.00 28.93 ? 222 GLN E NE2 1 ATOM 9112 N N . SER E 1 224 ? 18.981 14.853 49.791 1.00 22.12 ? 223 SER E N 1 ATOM 9113 C CA . SER E 1 224 ? 19.560 15.380 48.568 1.00 21.58 ? 223 SER E CA 1 ATOM 9114 C C . SER E 1 224 ? 21.065 15.096 48.467 1.00 19.91 ? 223 SER E C 1 ATOM 9115 O O . SER E 1 224 ? 21.608 15.107 47.385 1.00 19.29 ? 223 SER E O 1 ATOM 9116 C CB . SER E 1 224 ? 19.315 16.896 48.465 1.00 22.60 ? 223 SER E CB 1 ATOM 9117 O OG . SER E 1 224 ? 17.999 17.146 48.030 1.00 24.11 ? 223 SER E OG 1 ATOM 9118 N N . GLY E 1 225 ? 21.757 14.898 49.582 1.00 19.61 ? 224 GLY E N 1 ATOM 9119 C CA . GLY E 1 225 ? 23.151 14.469 49.507 1.00 19.58 ? 224 GLY E CA 1 ATOM 9120 C C . GLY E 1 225 ? 23.266 13.118 48.802 1.00 19.10 ? 224 GLY E C 1 ATOM 9121 O O . GLY E 1 225 ? 22.263 12.443 48.599 1.00 18.62 ? 224 GLY E O 1 ATOM 9122 N N . ARG E 1 226 ? 24.478 12.738 48.412 1.00 19.69 ? 225 ARG E N 1 ATOM 9123 C CA . ARG E 1 226 ? 24.759 11.404 47.852 1.00 19.91 ? 225 ARG E CA 1 ATOM 9124 C C . ARG E 1 226 ? 26.100 10.892 48.351 1.00 21.34 ? 225 ARG E C 1 ATOM 9125 O O . ARG E 1 226 ? 27.034 11.671 48.605 1.00 21.59 ? 225 ARG E O 1 ATOM 9126 C CB . ARG E 1 226 ? 24.825 11.439 46.314 1.00 20.41 ? 225 ARG E CB 1 ATOM 9127 C CG . ARG E 1 226 ? 23.580 11.933 45.594 1.00 21.58 ? 225 ARG E CG 1 ATOM 9128 C CD . ARG E 1 226 ? 22.509 10.858 45.525 1.00 21.81 ? 225 ARG E CD 1 ATOM 9129 N NE . ARG E 1 226 ? 21.281 11.349 44.893 1.00 23.44 ? 225 ARG E NE 1 ATOM 9130 C CZ . ARG E 1 226 ? 20.292 11.992 45.516 1.00 24.26 ? 225 ARG E CZ 1 ATOM 9131 N NH1 . ARG E 1 226 ? 20.345 12.267 46.820 1.00 24.11 ? 225 ARG E NH1 1 ATOM 9132 N NH2 . ARG E 1 226 ? 19.232 12.371 44.826 1.00 25.44 ? 225 ARG E NH2 1 ATOM 9133 N N . MET E 1 227 ? 26.204 9.569 48.454 1.00 23.38 ? 226 MET E N 1 ATOM 9134 C CA . MET E 1 227 ? 27.459 8.907 48.746 1.00 23.74 ? 226 MET E CA 1 ATOM 9135 C C . MET E 1 227 ? 27.793 8.050 47.544 1.00 23.34 ? 226 MET E C 1 ATOM 9136 O O . MET E 1 227 ? 26.953 7.322 47.045 1.00 23.15 ? 226 MET E O 1 ATOM 9137 C CB . MET E 1 227 ? 27.322 7.996 49.957 1.00 25.61 ? 226 MET E CB 1 ATOM 9138 C CG . MET E 1 227 ? 26.671 8.645 51.167 1.00 28.00 ? 226 MET E CG 1 ATOM 9139 S SD . MET E 1 227 ? 27.816 9.191 52.435 1.00 29.71 ? 226 MET E SD 1 ATOM 9140 C CE . MET E 1 227 ? 26.750 10.089 53.560 1.00 29.74 ? 226 MET E CE 1 ATOM 9141 N N . GLU E 1 228 ? 29.029 8.115 47.092 1.00 22.84 ? 227 GLU E N 1 ATOM 9142 C CA . GLU E 1 228 ? 29.479 7.261 46.017 1.00 22.49 ? 227 GLU E CA 1 ATOM 9143 C C . GLU E 1 228 ? 30.536 6.377 46.627 1.00 22.49 ? 227 GLU E C 1 ATOM 9144 O O . GLU E 1 228 ? 31.480 6.882 47.217 1.00 23.77 ? 227 GLU E O 1 ATOM 9145 C CB . GLU E 1 228 ? 30.037 8.137 44.908 1.00 23.25 ? 227 GLU E CB 1 ATOM 9146 C CG . GLU E 1 228 ? 30.564 7.409 43.693 1.00 23.64 ? 227 GLU E CG 1 ATOM 9147 C CD . GLU E 1 228 ? 30.763 8.334 42.509 1.00 24.48 ? 227 GLU E CD 1 ATOM 9148 O OE1 . GLU E 1 228 ? 30.918 9.572 42.688 1.00 26.35 ? 227 GLU E OE1 1 ATOM 9149 O OE2 . GLU E 1 228 ? 30.757 7.825 41.379 1.00 25.42 ? 227 GLU E OE2 1 ATOM 9150 N N . PHE E 1 229 ? 30.370 5.062 46.529 1.00 22.74 ? 228 PHE E N 1 ATOM 9151 C CA . PHE E 1 229 ? 31.311 4.122 47.154 1.00 23.04 ? 228 PHE E CA 1 ATOM 9152 C C . PHE E 1 229 ? 32.243 3.440 46.173 1.00 22.65 ? 228 PHE E C 1 ATOM 9153 O O . PHE E 1 229 ? 31.859 3.138 45.043 1.00 22.04 ? 228 PHE E O 1 ATOM 9154 C CB . PHE E 1 229 ? 30.547 3.080 47.959 1.00 23.65 ? 228 PHE E CB 1 ATOM 9155 C CG . PHE E 1 229 ? 29.896 3.652 49.184 1.00 23.90 ? 228 PHE E CG 1 ATOM 9156 C CD1 . PHE E 1 229 ? 30.636 3.886 50.320 1.00 23.78 ? 228 PHE E CD1 1 ATOM 9157 C CD2 . PHE E 1 229 ? 28.559 4.010 49.173 1.00 23.91 ? 228 PHE E CD2 1 ATOM 9158 C CE1 . PHE E 1 229 ? 30.050 4.437 51.440 1.00 24.43 ? 228 PHE E CE1 1 ATOM 9159 C CE2 . PHE E 1 229 ? 27.967 4.557 50.283 1.00 23.62 ? 228 PHE E CE2 1 ATOM 9160 C CZ . PHE E 1 229 ? 28.711 4.771 51.420 1.00 24.45 ? 228 PHE E CZ 1 ATOM 9161 N N . PHE E 1 230 ? 33.463 3.180 46.636 1.00 22.62 ? 229 PHE E N 1 ATOM 9162 C CA . PHE E 1 230 ? 34.485 2.514 45.827 1.00 22.01 ? 229 PHE E CA 1 ATOM 9163 C C . PHE E 1 230 ? 35.076 1.325 46.531 1.00 22.09 ? 229 PHE E C 1 ATOM 9164 O O . PHE E 1 230 ? 34.863 1.122 47.732 1.00 21.75 ? 229 PHE E O 1 ATOM 9165 C CB . PHE E 1 230 ? 35.595 3.485 45.499 1.00 22.35 ? 229 PHE E CB 1 ATOM 9166 C CG . PHE E 1 230 ? 35.122 4.685 44.734 1.00 22.54 ? 229 PHE E CG 1 ATOM 9167 C CD1 . PHE E 1 230 ? 34.542 5.764 45.403 1.00 22.06 ? 229 PHE E CD1 1 ATOM 9168 C CD2 . PHE E 1 230 ? 35.228 4.729 43.350 1.00 22.20 ? 229 PHE E CD2 1 ATOM 9169 C CE1 . PHE E 1 230 ? 34.114 6.872 44.699 1.00 22.17 ? 229 PHE E CE1 1 ATOM 9170 C CE2 . PHE E 1 230 ? 34.784 5.839 42.645 1.00 22.19 ? 229 PHE E CE2 1 ATOM 9171 C CZ . PHE E 1 230 ? 34.238 6.906 43.318 1.00 21.99 ? 229 PHE E CZ 1 ATOM 9172 N N . TRP E 1 231 ? 35.841 0.553 45.767 1.00 22.19 ? 230 TRP E N 1 ATOM 9173 C CA . TRP E 1 231 ? 36.475 -0.648 46.272 1.00 22.83 ? 230 TRP E CA 1 ATOM 9174 C C . TRP E 1 231 ? 37.730 -0.993 45.498 1.00 23.12 ? 230 TRP E C 1 ATOM 9175 O O . TRP E 1 231 ? 37.961 -0.498 44.412 1.00 23.39 ? 230 TRP E O 1 ATOM 9176 C CB . TRP E 1 231 ? 35.505 -1.839 46.228 1.00 22.80 ? 230 TRP E CB 1 ATOM 9177 C CG . TRP E 1 231 ? 35.010 -2.183 44.862 1.00 22.79 ? 230 TRP E CG 1 ATOM 9178 C CD1 . TRP E 1 231 ? 33.945 -1.627 44.211 1.00 21.96 ? 230 TRP E CD1 1 ATOM 9179 C CD2 . TRP E 1 231 ? 35.546 -3.177 43.971 1.00 23.44 ? 230 TRP E CD2 1 ATOM 9180 N NE1 . TRP E 1 231 ? 33.791 -2.205 42.974 1.00 21.93 ? 230 TRP E NE1 1 ATOM 9181 C CE2 . TRP E 1 231 ? 34.757 -3.157 42.799 1.00 22.74 ? 230 TRP E CE2 1 ATOM 9182 C CE3 . TRP E 1 231 ? 36.626 -4.062 44.043 1.00 24.36 ? 230 TRP E CE3 1 ATOM 9183 C CZ2 . TRP E 1 231 ? 35.006 -3.988 41.716 1.00 23.73 ? 230 TRP E CZ2 1 ATOM 9184 C CZ3 . TRP E 1 231 ? 36.873 -4.895 42.975 1.00 25.49 ? 230 TRP E CZ3 1 ATOM 9185 C CH2 . TRP E 1 231 ? 36.062 -4.853 41.816 1.00 25.65 ? 230 TRP E CH2 1 ATOM 9186 N N . THR E 1 232 ? 38.546 -1.849 46.085 1.00 23.67 ? 231 THR E N 1 ATOM 9187 C CA . THR E 1 232 ? 39.684 -2.406 45.399 1.00 24.51 ? 231 THR E CA 1 ATOM 9188 C C . THR E 1 232 ? 40.045 -3.700 46.107 1.00 25.75 ? 231 THR E C 1 ATOM 9189 O O . THR E 1 232 ? 39.626 -3.930 47.239 1.00 26.35 ? 231 THR E O 1 ATOM 9190 C CB . THR E 1 232 ? 40.866 -1.411 45.381 1.00 24.65 ? 231 THR E CB 1 ATOM 9191 O OG1 . THR E 1 232 ? 41.872 -1.858 44.462 1.00 25.39 ? 231 THR E OG1 1 ATOM 9192 C CG2 . THR E 1 232 ? 41.474 -1.244 46.745 1.00 25.13 ? 231 THR E CG2 1 ATOM 9193 N N . ILE E 1 233 ? 40.792 -4.552 45.429 1.00 26.97 ? 232 ILE E N 1 ATOM 9194 C CA . ILE E 1 233 ? 41.400 -5.720 46.059 1.00 28.80 ? 232 ILE E CA 1 ATOM 9195 C C . ILE E 1 233 ? 42.842 -5.353 46.424 1.00 29.88 ? 232 ILE E C 1 ATOM 9196 O O . ILE E 1 233 ? 43.641 -4.972 45.557 1.00 29.75 ? 232 ILE E O 1 ATOM 9197 C CB . ILE E 1 233 ? 41.388 -6.938 45.113 1.00 29.76 ? 232 ILE E CB 1 ATOM 9198 C CG1 . ILE E 1 233 ? 39.964 -7.247 44.655 1.00 29.07 ? 232 ILE E CG1 1 ATOM 9199 C CG2 . ILE E 1 233 ? 42.005 -8.152 45.796 1.00 31.71 ? 232 ILE E CG2 1 ATOM 9200 C CD1 . ILE E 1 233 ? 39.030 -7.640 45.783 1.00 29.10 ? 232 ILE E CD1 1 ATOM 9201 N N . LEU E 1 234 ? 43.168 -5.436 47.707 1.00 30.74 ? 233 LEU E N 1 ATOM 9202 C CA . LEU E 1 234 ? 44.507 -5.103 48.158 1.00 32.17 ? 233 LEU E CA 1 ATOM 9203 C C . LEU E 1 234 ? 45.254 -6.403 48.357 1.00 33.87 ? 233 LEU E C 1 ATOM 9204 O O . LEU E 1 234 ? 44.891 -7.212 49.203 1.00 33.36 ? 233 LEU E O 1 ATOM 9205 C CB . LEU E 1 234 ? 44.479 -4.278 49.447 1.00 32.51 ? 233 LEU E CB 1 ATOM 9206 C CG . LEU E 1 234 ? 45.846 -3.764 49.916 1.00 34.27 ? 233 LEU E CG 1 ATOM 9207 C CD1 . LEU E 1 234 ? 46.457 -2.806 48.898 1.00 34.52 ? 233 LEU E CD1 1 ATOM 9208 C CD2 . LEU E 1 234 ? 45.740 -3.081 51.263 1.00 34.54 ? 233 LEU E CD2 1 ATOM 9209 N N . LYS E 1 235 ? 46.294 -6.590 47.551 1.00 35.73 ? 234 LYS E N 1 ATOM 9210 C CA . LYS E 1 235 ? 47.056 -7.832 47.525 1.00 38.49 ? 234 LYS E CA 1 ATOM 9211 C C . LYS E 1 235 ? 47.952 -7.907 48.748 1.00 38.79 ? 234 LYS E C 1 ATOM 9212 O O . LYS E 1 235 ? 48.291 -6.870 49.322 1.00 38.13 ? 234 LYS E O 1 ATOM 9213 C CB . LYS E 1 235 ? 47.920 -7.899 46.263 1.00 40.17 ? 234 LYS E CB 1 ATOM 9214 C CG . LYS E 1 235 ? 47.120 -7.943 44.971 1.00 40.55 ? 234 LYS E CG 1 ATOM 9215 C CD . LYS E 1 235 ? 46.545 -9.327 44.711 1.00 42.39 ? 234 LYS E CD 1 ATOM 9216 C CE . LYS E 1 235 ? 47.622 -10.322 44.293 1.00 45.07 ? 234 LYS E CE 1 ATOM 9217 N NZ . LYS E 1 235 ? 47.378 -11.687 44.852 1.00 47.16 ? 234 LYS E NZ 1 ATOM 9218 N N . PRO E 1 236 ? 48.321 -9.131 49.163 1.00 40.03 ? 235 PRO E N 1 ATOM 9219 C CA . PRO E 1 236 ? 49.304 -9.295 50.234 1.00 41.97 ? 235 PRO E CA 1 ATOM 9220 C C . PRO E 1 236 ? 50.530 -8.416 50.016 1.00 42.39 ? 235 PRO E C 1 ATOM 9221 O O . PRO E 1 236 ? 51.025 -8.324 48.893 1.00 43.08 ? 235 PRO E O 1 ATOM 9222 C CB . PRO E 1 236 ? 49.690 -10.775 50.123 1.00 43.64 ? 235 PRO E CB 1 ATOM 9223 C CG . PRO E 1 236 ? 48.449 -11.433 49.627 1.00 42.93 ? 235 PRO E CG 1 ATOM 9224 C CD . PRO E 1 236 ? 47.749 -10.426 48.750 1.00 40.56 ? 235 PRO E CD 1 ATOM 9225 N N . ASN E 1 237 ? 50.990 -7.758 51.074 1.00 42.63 ? 236 ASN E N 1 ATOM 9226 C CA . ASN E 1 237 ? 52.218 -6.949 51.042 1.00 43.80 ? 236 ASN E CA 1 ATOM 9227 C C . ASN E 1 237 ? 52.125 -5.624 50.298 1.00 42.09 ? 236 ASN E C 1 ATOM 9228 O O . ASN E 1 237 ? 53.109 -4.875 50.228 1.00 42.62 ? 236 ASN E O 1 ATOM 9229 C CB . ASN E 1 237 ? 53.411 -7.749 50.518 1.00 45.78 ? 236 ASN E CB 1 ATOM 9230 C CG . ASN E 1 237 ? 54.132 -8.473 51.610 1.00 48.49 ? 236 ASN E CG 1 ATOM 9231 O OD1 . ASN E 1 237 ? 55.353 -8.397 51.712 1.00 51.79 ? 236 ASN E OD1 1 ATOM 9232 N ND2 . ASN E 1 237 ? 53.387 -9.176 52.445 1.00 48.98 ? 236 ASN E ND2 1 ATOM 9233 N N . ASP E 1 238 ? 50.957 -5.332 49.748 1.00 40.00 ? 237 ASP E N 1 ATOM 9234 C CA . ASP E 1 238 ? 50.721 -4.018 49.212 1.00 39.14 ? 237 ASP E CA 1 ATOM 9235 C C . ASP E 1 238 ? 50.079 -3.205 50.303 1.00 38.56 ? 237 ASP E C 1 ATOM 9236 O O . ASP E 1 238 ? 49.618 -3.749 51.310 1.00 38.79 ? 237 ASP E O 1 ATOM 9237 C CB . ASP E 1 238 ? 49.819 -4.057 47.982 1.00 37.80 ? 237 ASP E CB 1 ATOM 9238 C CG . ASP E 1 238 ? 49.979 -2.823 47.114 1.00 37.39 ? 237 ASP E CG 1 ATOM 9239 O OD1 . ASP E 1 238 ? 50.953 -2.066 47.361 1.00 37.64 ? 237 ASP E OD1 1 ATOM 9240 O OD2 . ASP E 1 238 ? 49.147 -2.614 46.195 1.00 35.88 ? 237 ASP E OD2 1 ATOM 9241 N N . ALA E 1 239 ? 50.062 -1.893 50.107 1.00 38.36 ? 238 ALA E N 1 ATOM 9242 C CA . ALA E 1 239 ? 49.487 -0.989 51.079 1.00 37.18 ? 238 ALA E CA 1 ATOM 9243 C C . ALA E 1 239 ? 48.601 -0.006 50.369 1.00 35.05 ? 238 ALA E C 1 ATOM 9244 O O . ALA E 1 239 ? 48.909 0.406 49.261 1.00 34.99 ? 238 ALA E O 1 ATOM 9245 C CB . ALA E 1 239 ? 50.589 -0.257 51.830 1.00 38.70 ? 238 ALA E CB 1 ATOM 9246 N N . ILE E 1 240 ? 47.503 0.362 51.025 1.00 34.04 ? 239 ILE E N 1 ATOM 9247 C CA . ILE E 1 240 ? 46.591 1.381 50.534 1.00 32.43 ? 239 ILE E CA 1 ATOM 9248 C C . ILE E 1 240 ? 46.822 2.661 51.342 1.00 32.55 ? 239 ILE E C 1 ATOM 9249 O O . ILE E 1 240 ? 46.900 2.619 52.567 1.00 33.50 ? 239 ILE E O 1 ATOM 9250 C CB . ILE E 1 240 ? 45.112 0.916 50.628 1.00 31.30 ? 239 ILE E CB 1 ATOM 9251 C CG1 . ILE E 1 240 ? 44.179 1.882 49.880 1.00 29.36 ? 239 ILE E CG1 1 ATOM 9252 C CG2 . ILE E 1 240 ? 44.656 0.775 52.077 1.00 31.70 ? 239 ILE E CG2 1 ATOM 9253 C CD1 . ILE E 1 240 ? 42.813 1.307 49.593 1.00 27.77 ? 239 ILE E CD1 1 ATOM 9254 N N . ASN E 1 241 ? 46.943 3.789 50.651 1.00 31.42 ? 240 ASN E N 1 ATOM 9255 C CA . ASN E 1 241 ? 47.219 5.058 51.292 1.00 31.87 ? 240 ASN E CA 1 ATOM 9256 C C . ASN E 1 241 ? 46.143 6.060 50.980 1.00 30.77 ? 240 ASN E C 1 ATOM 9257 O O . ASN E 1 241 ? 45.964 6.444 49.832 1.00 30.62 ? 240 ASN E O 1 ATOM 9258 C CB . ASN E 1 241 ? 48.565 5.600 50.830 1.00 33.47 ? 240 ASN E CB 1 ATOM 9259 C CG . ASN E 1 241 ? 49.674 4.593 51.003 1.00 34.76 ? 240 ASN E CG 1 ATOM 9260 O OD1 . ASN E 1 241 ? 50.048 4.255 52.126 1.00 36.01 ? 240 ASN E OD1 1 ATOM 9261 N ND2 . ASN E 1 241 ? 50.185 4.086 49.897 1.00 35.19 ? 240 ASN E ND2 1 ATOM 9262 N N . PHE E 1 242 ? 45.443 6.495 52.019 1.00 30.69 ? 241 PHE E N 1 ATOM 9263 C CA . PHE E 1 242 ? 44.376 7.461 51.884 1.00 29.83 ? 241 PHE E CA 1 ATOM 9264 C C . PHE E 1 242 ? 44.831 8.864 52.261 1.00 31.16 ? 241 PHE E C 1 ATOM 9265 O O . PHE E 1 242 ? 45.512 9.051 53.257 1.00 32.26 ? 241 PHE E O 1 ATOM 9266 C CB . PHE E 1 242 ? 43.221 7.054 52.781 1.00 28.97 ? 241 PHE E CB 1 ATOM 9267 C CG . PHE E 1 242 ? 42.458 5.867 52.277 1.00 27.46 ? 241 PHE E CG 1 ATOM 9268 C CD1 . PHE E 1 242 ? 41.466 6.027 51.328 1.00 26.47 ? 241 PHE E CD1 1 ATOM 9269 C CD2 . PHE E 1 242 ? 42.718 4.597 52.771 1.00 27.63 ? 241 PHE E CD2 1 ATOM 9270 C CE1 . PHE E 1 242 ? 40.752 4.932 50.857 1.00 26.06 ? 241 PHE E CE1 1 ATOM 9271 C CE2 . PHE E 1 242 ? 42.019 3.499 52.310 1.00 26.86 ? 241 PHE E CE2 1 ATOM 9272 C CZ . PHE E 1 242 ? 41.031 3.664 51.350 1.00 26.32 ? 241 PHE E CZ 1 ATOM 9273 N N . GLU E 1 243 ? 44.430 9.857 51.479 1.00 31.18 ? 242 GLU E N 1 ATOM 9274 C CA . GLU E 1 243 ? 44.612 11.243 51.899 1.00 32.50 ? 242 GLU E CA 1 ATOM 9275 C C . GLU E 1 243 ? 43.393 12.091 51.556 1.00 31.09 ? 242 GLU E C 1 ATOM 9276 O O . GLU E 1 243 ? 42.873 12.005 50.445 1.00 31.19 ? 242 GLU E O 1 ATOM 9277 C CB . GLU E 1 243 ? 45.870 11.848 51.281 1.00 34.59 ? 242 GLU E CB 1 ATOM 9278 C CG . GLU E 1 243 ? 46.095 13.295 51.703 1.00 37.02 ? 242 GLU E CG 1 ATOM 9279 C CD . GLU E 1 243 ? 47.342 13.890 51.114 1.00 39.34 ? 242 GLU E CD 1 ATOM 9280 O OE1 . GLU E 1 243 ? 48.337 13.163 50.986 1.00 41.82 ? 242 GLU E OE1 1 ATOM 9281 O OE2 . GLU E 1 243 ? 47.327 15.088 50.781 1.00 41.48 ? 242 GLU E OE2 1 ATOM 9282 N N . SER E 1 244 ? 42.950 12.913 52.504 1.00 30.64 ? 243 SER E N 1 ATOM 9283 C CA . SER E 1 244 ? 41.769 13.754 52.295 1.00 29.95 ? 243 SER E CA 1 ATOM 9284 C C . SER E 1 244 ? 41.682 14.940 53.241 1.00 30.45 ? 243 SER E C 1 ATOM 9285 O O . SER E 1 244 ? 42.100 14.854 54.383 1.00 31.69 ? 243 SER E O 1 ATOM 9286 C CB . SER E 1 244 ? 40.500 12.925 52.468 1.00 28.55 ? 243 SER E CB 1 ATOM 9287 O OG . SER E 1 244 ? 39.356 13.713 52.232 1.00 27.90 ? 243 SER E OG 1 ATOM 9288 N N . ASN E 1 245 ? 41.112 16.034 52.756 1.00 30.08 ? 244 ASN E N 1 ATOM 9289 C CA . ASN E 1 245 ? 40.799 17.182 53.594 1.00 31.51 ? 244 ASN E CA 1 ATOM 9290 C C . ASN E 1 245 ? 39.276 17.390 53.719 1.00 30.32 ? 244 ASN E C 1 ATOM 9291 O O . ASN E 1 245 ? 38.819 18.475 54.064 1.00 30.58 ? 244 ASN E O 1 ATOM 9292 C CB . ASN E 1 245 ? 41.453 18.441 53.025 1.00 33.34 ? 244 ASN E CB 1 ATOM 9293 C CG . ASN E 1 245 ? 40.827 18.876 51.723 1.00 33.50 ? 244 ASN E CG 1 ATOM 9294 O OD1 . ASN E 1 245 ? 40.369 18.038 50.951 1.00 32.65 ? 244 ASN E OD1 1 ATOM 9295 N ND2 . ASN E 1 245 ? 40.779 20.190 51.477 1.00 35.38 ? 244 ASN E ND2 1 ATOM 9296 N N . GLY E 1 246 ? 38.503 16.344 53.450 1.00 28.58 ? 245 GLY E N 1 ATOM 9297 C CA . GLY E 1 246 ? 37.052 16.414 53.554 1.00 27.77 ? 245 GLY E CA 1 ATOM 9298 C C . GLY E 1 246 ? 36.326 15.373 52.717 1.00 25.96 ? 245 GLY E C 1 ATOM 9299 O O . GLY E 1 246 ? 36.897 14.787 51.794 1.00 25.43 ? 245 GLY E O 1 ATOM 9300 N N . ASN E 1 247 ? 35.061 15.154 53.077 1.00 25.11 ? 246 ASN E N 1 ATOM 9301 C CA . ASN E 1 247 ? 34.098 14.341 52.324 1.00 23.61 ? 246 ASN E CA 1 ATOM 9302 C C . ASN E 1 247 ? 34.441 12.864 52.272 1.00 23.20 ? 246 ASN E C 1 ATOM 9303 O O . ASN E 1 247 ? 33.888 12.134 51.485 1.00 23.33 ? 246 ASN E O 1 ATOM 9304 C CB . ASN E 1 247 ? 33.908 14.900 50.921 1.00 23.25 ? 246 ASN E CB 1 ATOM 9305 C CG . ASN E 1 247 ? 33.509 16.366 50.934 1.00 24.21 ? 246 ASN E CG 1 ATOM 9306 O OD1 . ASN E 1 247 ? 34.320 17.236 51.222 1.00 24.68 ? 246 ASN E OD1 1 ATOM 9307 N ND2 . ASN E 1 247 ? 32.251 16.641 50.624 1.00 23.55 ? 246 ASN E ND2 1 ATOM 9308 N N . PHE E 1 248 ? 35.325 12.434 53.157 1.00 23.97 ? 247 PHE E N 1 ATOM 9309 C CA . PHE E 1 248 ? 35.878 11.102 53.132 1.00 24.52 ? 247 PHE E CA 1 ATOM 9310 C C . PHE E 1 248 ? 35.035 10.193 54.029 1.00 24.21 ? 247 PHE E C 1 ATOM 9311 O O . PHE E 1 248 ? 34.824 10.487 55.212 1.00 24.29 ? 247 PHE E O 1 ATOM 9312 C CB . PHE E 1 248 ? 37.338 11.163 53.607 1.00 26.34 ? 247 PHE E CB 1 ATOM 9313 C CG . PHE E 1 248 ? 38.053 9.841 53.628 1.00 26.75 ? 247 PHE E CG 1 ATOM 9314 C CD1 . PHE E 1 248 ? 37.854 8.893 52.637 1.00 26.11 ? 247 PHE E CD1 1 ATOM 9315 C CD2 . PHE E 1 248 ? 38.965 9.571 54.625 1.00 28.44 ? 247 PHE E CD2 1 ATOM 9316 C CE1 . PHE E 1 248 ? 38.530 7.696 52.662 1.00 26.60 ? 247 PHE E CE1 1 ATOM 9317 C CE2 . PHE E 1 248 ? 39.653 8.374 54.656 1.00 29.00 ? 247 PHE E CE2 1 ATOM 9318 C CZ . PHE E 1 248 ? 39.434 7.435 53.670 1.00 28.47 ? 247 PHE E CZ 1 ATOM 9319 N N . ILE E 1 249 ? 34.513 9.119 53.444 1.00 22.29 ? 248 ILE E N 1 ATOM 9320 C CA . ILE E 1 249 ? 33.850 8.095 54.208 1.00 21.89 ? 248 ILE E CA 1 ATOM 9321 C C . ILE E 1 249 ? 34.918 7.016 54.341 1.00 22.11 ? 248 ILE E C 1 ATOM 9322 O O . ILE E 1 249 ? 35.142 6.270 53.407 1.00 21.38 ? 248 ILE E O 1 ATOM 9323 C CB . ILE E 1 249 ? 32.601 7.560 53.469 1.00 21.54 ? 248 ILE E CB 1 ATOM 9324 C CG1 . ILE E 1 249 ? 31.727 8.708 52.934 1.00 21.18 ? 248 ILE E CG1 1 ATOM 9325 C CG2 . ILE E 1 249 ? 31.784 6.664 54.385 1.00 21.73 ? 248 ILE E CG2 1 ATOM 9326 C CD1 . ILE E 1 249 ? 31.314 9.716 53.994 1.00 21.78 ? 248 ILE E CD1 1 ATOM 9327 N N . ALA E 1 250 ? 35.601 6.953 55.484 1.00 23.37 ? 249 ALA E N 1 ATOM 9328 C CA . ALA E 1 250 ? 36.794 6.111 55.604 1.00 24.55 ? 249 ALA E CA 1 ATOM 9329 C C . ALA E 1 250 ? 36.481 4.646 55.847 1.00 24.80 ? 249 ALA E C 1 ATOM 9330 O O . ALA E 1 250 ? 35.446 4.319 56.410 1.00 24.31 ? 249 ALA E O 1 ATOM 9331 C CB . ALA E 1 250 ? 37.686 6.621 56.709 1.00 26.14 ? 249 ALA E CB 1 ATOM 9332 N N . PRO E 1 251 ? 37.394 3.751 55.439 1.00 25.69 ? 250 PRO E N 1 ATOM 9333 C CA . PRO E 1 251 ? 37.216 2.362 55.857 1.00 26.56 ? 250 PRO E CA 1 ATOM 9334 C C . PRO E 1 251 ? 37.235 2.218 57.385 1.00 28.19 ? 250 PRO E C 1 ATOM 9335 O O . PRO E 1 251 ? 37.981 2.930 58.067 1.00 29.11 ? 250 PRO E O 1 ATOM 9336 C CB . PRO E 1 251 ? 38.426 1.629 55.241 1.00 26.80 ? 250 PRO E CB 1 ATOM 9337 C CG . PRO E 1 251 ? 39.035 2.566 54.265 1.00 26.20 ? 250 PRO E CG 1 ATOM 9338 C CD . PRO E 1 251 ? 38.610 3.953 54.633 1.00 26.07 ? 250 PRO E CD 1 ATOM 9339 N N . GLU E 1 252 ? 36.396 1.334 57.910 1.00 28.87 ? 251 GLU E N 1 ATOM 9340 C CA . GLU E 1 252 ? 36.564 0.845 59.267 1.00 31.41 ? 251 GLU E CA 1 ATOM 9341 C C . GLU E 1 252 ? 36.838 -0.655 59.191 1.00 31.58 ? 251 GLU E C 1 ATOM 9342 O O . GLU E 1 252 ? 37.835 -1.126 59.725 1.00 31.75 ? 251 GLU E O 1 ATOM 9343 C CB . GLU E 1 252 ? 35.340 1.133 60.150 1.00 33.07 ? 251 GLU E CB 1 ATOM 9344 C CG . GLU E 1 252 ? 35.400 0.424 61.500 1.00 36.33 ? 251 GLU E CG 1 ATOM 9345 C CD . GLU E 1 252 ? 34.211 0.708 62.404 1.00 38.60 ? 251 GLU E CD 1 ATOM 9346 O OE1 . GLU E 1 252 ? 33.431 1.655 62.131 1.00 39.47 ? 251 GLU E OE1 1 ATOM 9347 O OE2 . GLU E 1 252 ? 34.046 -0.039 63.394 1.00 40.75 ? 251 GLU E OE2 1 ATOM 9348 N N . ASN E 1 253 ? 35.949 -1.404 58.539 1.00 30.62 ? 252 ASN E N 1 ATOM 9349 C CA . ASN E 1 253 ? 36.183 -2.840 58.338 1.00 31.51 ? 252 ASN E CA 1 ATOM 9350 C C . ASN E 1 253 ? 36.424 -3.148 56.871 1.00 30.94 ? 252 ASN E C 1 ATOM 9351 O O . ASN E 1 253 ? 35.958 -2.428 55.997 1.00 29.40 ? 252 ASN E O 1 ATOM 9352 C CB . ASN E 1 253 ? 35.010 -3.686 58.827 1.00 31.61 ? 252 ASN E CB 1 ATOM 9353 C CG . ASN E 1 253 ? 34.661 -3.441 60.285 1.00 32.41 ? 252 ASN E CG 1 ATOM 9354 O OD1 . ASN E 1 253 ? 35.537 -3.402 61.159 1.00 32.86 ? 252 ASN E OD1 1 ATOM 9355 N ND2 . ASN E 1 253 ? 33.360 -3.293 60.557 1.00 31.69 ? 252 ASN E ND2 1 ATOM 9356 N N . ALA E 1 254 ? 37.156 -4.231 56.628 1.00 32.30 ? 253 ALA E N 1 ATOM 9357 C CA . ALA E 1 254 ? 37.405 -4.752 55.293 1.00 31.52 ? 253 ALA E CA 1 ATOM 9358 C C . ALA E 1 254 ? 37.329 -6.278 55.350 1.00 33.00 ? 253 ALA E C 1 ATOM 9359 O O . ALA E 1 254 ? 37.260 -6.858 56.436 1.00 33.90 ? 253 ALA E O 1 ATOM 9360 C CB . ALA E 1 254 ? 38.774 -4.298 54.814 1.00 32.04 ? 253 ALA E CB 1 ATOM 9361 N N . TYR E 1 255 ? 37.391 -6.924 54.186 1.00 32.96 ? 254 TYR E N 1 ATOM 9362 C CA . TYR E 1 255 ? 37.130 -8.364 54.071 1.00 33.75 ? 254 TYR E CA 1 ATOM 9363 C C . TYR E 1 255 ? 38.296 -9.191 53.517 1.00 35.12 ? 254 TYR E C 1 ATOM 9364 O O . TYR E 1 255 ? 38.688 -9.028 52.360 1.00 33.65 ? 254 TYR E O 1 ATOM 9365 C CB . TYR E 1 255 ? 35.927 -8.587 53.160 1.00 32.21 ? 254 TYR E CB 1 ATOM 9366 C CG . TYR E 1 255 ? 34.652 -7.996 53.671 1.00 31.21 ? 254 TYR E CG 1 ATOM 9367 C CD1 . TYR E 1 255 ? 34.290 -6.702 53.341 1.00 29.38 ? 254 TYR E CD1 1 ATOM 9368 C CD2 . TYR E 1 255 ? 33.784 -8.739 54.471 1.00 32.16 ? 254 TYR E CD2 1 ATOM 9369 C CE1 . TYR E 1 255 ? 33.109 -6.151 53.799 1.00 28.39 ? 254 TYR E CE1 1 ATOM 9370 C CE2 . TYR E 1 255 ? 32.600 -8.194 54.936 1.00 31.48 ? 254 TYR E CE2 1 ATOM 9371 C CZ . TYR E 1 255 ? 32.269 -6.897 54.591 1.00 29.49 ? 254 TYR E CZ 1 ATOM 9372 O OH . TYR E 1 255 ? 31.095 -6.339 55.034 1.00 29.17 ? 254 TYR E OH 1 ATOM 9373 N N . LYS E 1 256 ? 38.828 -10.088 54.346 1.00 37.18 ? 255 LYS E N 1 ATOM 9374 C CA . LYS E 1 256 ? 39.785 -11.088 53.884 1.00 38.97 ? 255 LYS E CA 1 ATOM 9375 C C . LYS E 1 256 ? 39.044 -12.125 53.056 1.00 39.24 ? 255 LYS E C 1 ATOM 9376 O O . LYS E 1 256 ? 38.077 -12.717 53.524 1.00 39.90 ? 255 LYS E O 1 ATOM 9377 C CB . LYS E 1 256 ? 40.492 -11.803 55.050 1.00 40.86 ? 255 LYS E CB 1 ATOM 9378 C CG . LYS E 1 256 ? 41.347 -10.899 55.926 1.00 41.29 ? 255 LYS E CG 1 ATOM 9379 C CD . LYS E 1 256 ? 42.529 -11.627 56.568 1.00 43.37 ? 255 LYS E CD 1 ATOM 9380 C CE . LYS E 1 256 ? 42.126 -12.601 57.666 1.00 45.10 ? 255 LYS E CE 1 ATOM 9381 N NZ . LYS E 1 256 ? 43.258 -13.484 58.085 1.00 47.58 ? 255 LYS E NZ 1 ATOM 9382 N N . ILE E 1 257 ? 39.518 -12.357 51.840 1.00 39.00 ? 256 ILE E N 1 ATOM 9383 C CA . ILE E 1 257 ? 38.953 -13.388 50.987 1.00 39.93 ? 256 ILE E CA 1 ATOM 9384 C C . ILE E 1 257 ? 39.603 -14.693 51.408 1.00 42.42 ? 256 ILE E C 1 ATOM 9385 O O . ILE E 1 257 ? 40.709 -15.006 50.994 1.00 44.02 ? 256 ILE E O 1 ATOM 9386 C CB . ILE E 1 257 ? 39.225 -13.109 49.493 1.00 38.77 ? 256 ILE E CB 1 ATOM 9387 C CG1 . ILE E 1 257 ? 38.694 -11.733 49.103 1.00 36.39 ? 256 ILE E CG1 1 ATOM 9388 C CG2 . ILE E 1 257 ? 38.602 -14.189 48.623 1.00 39.77 ? 256 ILE E CG2 1 ATOM 9389 C CD1 . ILE E 1 257 ? 39.264 -11.207 47.807 1.00 35.92 ? 256 ILE E CD1 1 ATOM 9390 N N . VAL E 1 258 ? 38.915 -15.447 52.247 1.00 44.18 ? 257 VAL E N 1 ATOM 9391 C CA . VAL E 1 258 ? 39.508 -16.629 52.864 1.00 47.26 ? 257 VAL E CA 1 ATOM 9392 C C . VAL E 1 258 ? 39.196 -17.912 52.094 1.00 49.23 ? 257 VAL E C 1 ATOM 9393 O O . VAL E 1 258 ? 39.953 -18.881 52.186 1.00 50.96 ? 257 VAL E O 1 ATOM 9394 C CB . VAL E 1 258 ? 39.089 -16.743 54.346 1.00 48.11 ? 257 VAL E CB 1 ATOM 9395 C CG1 . VAL E 1 258 ? 39.599 -18.037 54.965 1.00 52.16 ? 257 VAL E CG1 1 ATOM 9396 C CG2 . VAL E 1 258 ? 39.647 -15.560 55.114 1.00 46.90 ? 257 VAL E CG2 1 ATOM 9397 N N . LYS E 1 259 ? 38.097 -17.930 51.342 1.00 49.49 ? 258 LYS E N 1 ATOM 9398 C CA . LYS E 1 259 ? 37.793 -19.086 50.498 1.00 52.52 ? 258 LYS E CA 1 ATOM 9399 C C . LYS E 1 259 ? 37.307 -18.700 49.111 1.00 51.54 ? 258 LYS E C 1 ATOM 9400 O O . LYS E 1 259 ? 36.300 -18.010 48.970 1.00 49.40 ? 258 LYS E O 1 ATOM 9401 C CB . LYS E 1 259 ? 36.771 -20.011 51.161 1.00 54.86 ? 258 LYS E CB 1 ATOM 9402 C CG . LYS E 1 259 ? 36.867 -21.437 50.639 1.00 58.10 ? 258 LYS E CG 1 ATOM 9403 C CD . LYS E 1 259 ? 35.695 -22.314 51.056 1.00 60.43 ? 258 LYS E CD 1 ATOM 9404 C CE . LYS E 1 259 ? 35.675 -23.616 50.255 1.00 63.18 ? 258 LYS E CE 1 ATOM 9405 N NZ . LYS E 1 259 ? 36.811 -24.528 50.587 1.00 65.67 ? 258 LYS E NZ 1 ATOM 9406 N N . LYS E 1 260 ? 38.038 -19.162 48.095 1.00 53.71 ? 259 LYS E N 1 ATOM 9407 C CA . LYS E 1 260 ? 37.637 -19.011 46.693 1.00 54.43 ? 259 LYS E CA 1 ATOM 9408 C C . LYS E 1 260 ? 37.176 -20.357 46.155 1.00 56.86 ? 259 LYS E C 1 ATOM 9409 O O . LYS E 1 260 ? 37.559 -21.402 46.681 1.00 59.88 ? 259 LYS E O 1 ATOM 9410 C CB . LYS E 1 260 ? 38.782 -18.439 45.845 1.00 54.04 ? 259 LYS E CB 1 ATOM 9411 C CG . LYS E 1 260 ? 38.989 -16.939 46.052 1.00 52.20 ? 259 LYS E CG 1 ATOM 9412 C CD . LYS E 1 260 ? 40.028 -16.359 45.105 1.00 51.95 ? 259 LYS E CD 1 ATOM 9413 C CE . LYS E 1 260 ? 39.417 -15.915 43.785 1.00 51.14 ? 259 LYS E CE 1 ATOM 9414 N NZ . LYS E 1 260 ? 38.966 -14.491 43.837 1.00 49.64 ? 259 LYS E NZ 1 ATOM 9415 N N . GLY E 1 261 ? 36.333 -20.329 45.125 1.00 56.65 ? 260 GLY E N 1 ATOM 9416 C CA . GLY E 1 261 ? 35.791 -21.558 44.541 1.00 59.70 ? 260 GLY E CA 1 ATOM 9417 C C . GLY E 1 261 ? 34.531 -21.307 43.738 1.00 59.16 ? 260 GLY E C 1 ATOM 9418 O O . GLY E 1 261 ? 34.228 -20.171 43.399 1.00 57.23 ? 260 GLY E O 1 ATOM 9419 N N . ASP E 1 262 ? 33.805 -22.377 43.423 1.00 62.09 ? 261 ASP E N 1 ATOM 9420 C CA . ASP E 1 262 ? 32.538 -22.257 42.703 1.00 61.49 ? 261 ASP E CA 1 ATOM 9421 C C . ASP E 1 262 ? 31.468 -21.643 43.590 1.00 59.42 ? 261 ASP E C 1 ATOM 9422 O O . ASP E 1 262 ? 31.187 -22.142 44.675 1.00 61.07 ? 261 ASP E O 1 ATOM 9423 C CB . ASP E 1 262 ? 32.045 -23.621 42.192 1.00 65.09 ? 261 ASP E CB 1 ATOM 9424 C CG . ASP E 1 262 ? 32.341 -23.844 40.711 1.00 66.52 ? 261 ASP E CG 1 ATOM 9425 O OD1 . ASP E 1 262 ? 32.553 -22.847 39.976 1.00 64.55 ? 261 ASP E OD1 1 ATOM 9426 O OD2 . ASP E 1 262 ? 32.350 -25.022 40.284 1.00 68.06 ? 261 ASP E OD2 1 ATOM 9427 N N . SER E 1 263 ? 30.889 -20.549 43.114 1.00 56.26 ? 262 SER E N 1 ATOM 9428 C CA . SER E 1 263 ? 29.724 -19.947 43.737 1.00 54.22 ? 262 SER E CA 1 ATOM 9429 C C . SER E 1 263 ? 28.932 -19.215 42.659 1.00 51.79 ? 262 SER E C 1 ATOM 9430 O O . SER E 1 263 ? 29.275 -19.280 41.484 1.00 52.75 ? 262 SER E O 1 ATOM 9431 C CB . SER E 1 263 ? 30.149 -18.988 44.846 1.00 52.44 ? 262 SER E CB 1 ATOM 9432 O OG . SER E 1 263 ? 29.019 -18.465 45.522 1.00 52.15 ? 262 SER E OG 1 ATOM 9433 N N . THR E 1 264 ? 27.869 -18.536 43.058 1.00 49.68 ? 263 THR E N 1 ATOM 9434 C CA . THR E 1 264 ? 27.051 -17.777 42.126 1.00 47.96 ? 263 THR E CA 1 ATOM 9435 C C . THR E 1 264 ? 26.124 -16.857 42.915 1.00 46.30 ? 263 THR E C 1 ATOM 9436 O O . THR E 1 264 ? 25.908 -17.073 44.108 1.00 46.43 ? 263 THR E O 1 ATOM 9437 C CB . THR E 1 264 ? 26.227 -18.711 41.214 1.00 50.25 ? 263 THR E CB 1 ATOM 9438 O OG1 . THR E 1 264 ? 25.539 -17.945 40.224 1.00 49.41 ? 263 THR E OG1 1 ATOM 9439 C CG2 . THR E 1 264 ? 25.213 -19.521 42.012 1.00 52.42 ? 263 THR E CG2 1 ATOM 9440 N N . ILE E 1 265 ? 25.602 -15.826 42.254 1.00 44.06 ? 264 ILE E N 1 ATOM 9441 C CA . ILE E 1 265 ? 24.561 -14.988 42.836 1.00 42.73 ? 264 ILE E CA 1 ATOM 9442 C C . ILE E 1 265 ? 23.242 -15.236 42.127 1.00 43.71 ? 264 ILE E C 1 ATOM 9443 O O . ILE E 1 265 ? 23.026 -14.746 41.025 1.00 44.57 ? 264 ILE E O 1 ATOM 9444 C CB . ILE E 1 265 ? 24.916 -13.492 42.777 1.00 40.46 ? 264 ILE E CB 1 ATOM 9445 C CG1 . ILE E 1 265 ? 26.156 -13.238 43.638 1.00 39.42 ? 264 ILE E CG1 1 ATOM 9446 C CG2 . ILE E 1 265 ? 23.737 -12.650 43.257 1.00 39.55 ? 264 ILE E CG2 1 ATOM 9447 C CD1 . ILE E 1 265 ? 26.661 -11.818 43.593 1.00 37.71 ? 264 ILE E CD1 1 ATOM 9448 N N . MET E 1 266 ? 22.370 -16.006 42.773 1.00 44.83 ? 265 MET E N 1 ATOM 9449 C CA . MET E 1 266 ? 21.035 -16.270 42.263 1.00 45.19 ? 265 MET E CA 1 ATOM 9450 C C . MET E 1 266 ? 20.069 -15.168 42.621 1.00 43.40 ? 265 MET E C 1 ATOM 9451 O O . MET E 1 266 ? 20.090 -14.655 43.736 1.00 41.12 ? 265 MET E O 1 ATOM 9452 C CB . MET E 1 266 ? 20.466 -17.541 42.865 1.00 47.46 ? 265 MET E CB 1 ATOM 9453 C CG . MET E 1 266 ? 20.937 -18.803 42.210 1.00 49.70 ? 265 MET E CG 1 ATOM 9454 S SD . MET E 1 266 ? 19.887 -20.134 42.783 1.00 52.48 ? 265 MET E SD 1 ATOM 9455 C CE . MET E 1 266 ? 20.662 -21.470 41.887 1.00 54.60 ? 265 MET E CE 1 ATOM 9456 N N . LYS E 1 267 ? 19.189 -14.857 41.675 1.00 43.75 ? 266 LYS E N 1 ATOM 9457 C CA . LYS E 1 267 ? 18.058 -14.001 41.934 1.00 43.17 ? 266 LYS E CA 1 ATOM 9458 C C . LYS E 1 267 ? 16.879 -14.919 42.202 1.00 45.07 ? 266 LYS E C 1 ATOM 9459 O O . LYS E 1 267 ? 16.565 -15.800 41.392 1.00 46.10 ? 266 LYS E O 1 ATOM 9460 C CB . LYS E 1 267 ? 17.782 -13.082 40.745 1.00 43.20 ? 266 LYS E CB 1 ATOM 9461 C CG . LYS E 1 267 ? 18.997 -12.305 40.246 1.00 41.84 ? 266 LYS E CG 1 ATOM 9462 C CD . LYS E 1 267 ? 19.577 -11.360 41.288 1.00 40.32 ? 266 LYS E CD 1 ATOM 9463 C CE . LYS E 1 267 ? 18.944 -9.980 41.197 1.00 39.49 ? 266 LYS E CE 1 ATOM 9464 N NZ . LYS E 1 267 ? 19.390 -9.069 42.293 1.00 37.34 ? 266 LYS E NZ 1 ATOM 9465 N N . SER E 1 268 ? 16.249 -14.733 43.355 1.00 44.26 ? 267 SER E N 1 ATOM 9466 C CA . SER E 1 268 ? 15.135 -15.578 43.761 1.00 46.32 ? 267 SER E CA 1 ATOM 9467 C C . SER E 1 268 ? 14.341 -14.870 44.837 1.00 45.45 ? 267 SER E C 1 ATOM 9468 O O . SER E 1 268 ? 14.884 -14.046 45.577 1.00 43.64 ? 267 SER E O 1 ATOM 9469 C CB . SER E 1 268 ? 15.646 -16.930 44.270 1.00 48.21 ? 267 SER E CB 1 ATOM 9470 O OG . SER E 1 268 ? 14.572 -17.779 44.633 1.00 50.87 ? 267 SER E OG 1 ATOM 9471 N N . GLU E 1 269 ? 13.049 -15.161 44.894 1.00 52.31 ? 268 GLU E N 1 ATOM 9472 C CA . GLU E 1 269 ? 12.193 -14.623 45.944 1.00 54.82 ? 268 GLU E CA 1 ATOM 9473 C C . GLU E 1 269 ? 12.003 -15.639 47.072 1.00 55.75 ? 268 GLU E C 1 ATOM 9474 O O . GLU E 1 269 ? 11.498 -15.293 48.141 1.00 57.86 ? 268 GLU E O 1 ATOM 9475 C CB . GLU E 1 269 ? 10.848 -14.183 45.365 1.00 57.30 ? 268 GLU E CB 1 ATOM 9476 C CG . GLU E 1 269 ? 10.964 -13.061 44.341 1.00 57.25 ? 268 GLU E CG 1 ATOM 9477 C CD . GLU E 1 269 ? 11.443 -11.747 44.943 1.00 57.80 ? 268 GLU E CD 1 ATOM 9478 O OE1 . GLU E 1 269 ? 10.670 -11.123 45.707 1.00 60.56 ? 268 GLU E OE1 1 ATOM 9479 O OE2 . GLU E 1 269 ? 12.587 -11.328 44.644 1.00 55.68 ? 268 GLU E OE2 1 ATOM 9480 N N . LEU E 1 270 ? 12.449 -16.876 46.846 1.00 54.55 ? 269 LEU E N 1 ATOM 9481 C CA . LEU E 1 270 ? 12.301 -17.955 47.822 1.00 55.91 ? 269 LEU E CA 1 ATOM 9482 C C . LEU E 1 270 ? 13.159 -17.738 49.065 1.00 55.93 ? 269 LEU E C 1 ATOM 9483 O O . LEU E 1 270 ? 14.211 -17.110 48.995 1.00 54.02 ? 269 LEU E O 1 ATOM 9484 C CB . LEU E 1 270 ? 12.672 -19.300 47.189 1.00 54.65 ? 269 LEU E CB 1 ATOM 9485 C CG . LEU E 1 270 ? 11.879 -19.738 45.952 1.00 54.93 ? 269 LEU E CG 1 ATOM 9486 C CD1 . LEU E 1 270 ? 12.332 -21.121 45.485 1.00 53.96 ? 269 LEU E CD1 1 ATOM 9487 C CD2 . LEU E 1 270 ? 10.377 -19.709 46.213 1.00 57.82 ? 269 LEU E CD2 1 ATOM 9488 N N . GLU E 1 271 ? 12.684 -18.254 50.199 1.00 58.71 ? 270 GLU E N 1 ATOM 9489 C CA . GLU E 1 271 ? 13.445 -18.272 51.451 1.00 59.23 ? 270 GLU E CA 1 ATOM 9490 C C . GLU E 1 271 ? 14.083 -19.652 51.659 1.00 59.37 ? 270 GLU E C 1 ATOM 9491 O O . GLU E 1 271 ? 13.772 -20.603 50.936 1.00 59.50 ? 270 GLU E O 1 ATOM 9492 C CB . GLU E 1 271 ? 12.531 -17.943 52.627 1.00 62.61 ? 270 GLU E CB 1 ATOM 9493 N N . TYR E 1 272 ? 14.966 -19.757 52.653 1.00 59.41 ? 271 TYR E N 1 ATOM 9494 C CA . TYR E 1 272 ? 15.666 -21.014 52.953 1.00 59.33 ? 271 TYR E CA 1 ATOM 9495 C C . TYR E 1 272 ? 14.666 -22.136 53.208 1.00 62.44 ? 271 TYR E C 1 ATOM 9496 O O . TYR E 1 272 ? 13.604 -21.899 53.778 1.00 65.31 ? 271 TYR E O 1 ATOM 9497 C CB . TYR E 1 272 ? 16.593 -20.837 54.165 1.00 59.74 ? 271 TYR E CB 1 ATOM 9498 C CG . TYR E 1 272 ? 17.396 -22.066 54.531 1.00 60.38 ? 271 TYR E CG 1 ATOM 9499 C CD1 . TYR E 1 272 ? 18.192 -22.697 53.591 1.00 58.09 ? 271 TYR E CD1 1 ATOM 9500 C CD2 . TYR E 1 272 ? 17.368 -22.589 55.825 1.00 63.79 ? 271 TYR E CD2 1 ATOM 9501 C CE1 . TYR E 1 272 ? 18.929 -23.821 53.912 1.00 59.63 ? 271 TYR E CE1 1 ATOM 9502 C CE2 . TYR E 1 272 ? 18.106 -23.719 56.158 1.00 65.23 ? 271 TYR E CE2 1 ATOM 9503 C CZ . TYR E 1 272 ? 18.886 -24.332 55.194 1.00 63.10 ? 271 TYR E CZ 1 ATOM 9504 O OH . TYR E 1 272 ? 19.633 -25.448 55.497 1.00 64.37 ? 271 TYR E OH 1 ATOM 9505 N N . GLY E 1 273 ? 15.008 -23.350 52.785 1.00 62.38 ? 272 GLY E N 1 ATOM 9506 C CA . GLY E 1 273 ? 14.075 -24.480 52.840 1.00 65.46 ? 272 GLY E CA 1 ATOM 9507 C C . GLY E 1 273 ? 14.473 -25.657 53.716 1.00 68.46 ? 272 GLY E C 1 ATOM 9508 O O . GLY E 1 273 ? 13.765 -26.671 53.740 1.00 71.40 ? 272 GLY E O 1 ATOM 9509 N N . ASN E 1 274 ? 15.592 -25.540 54.432 1.00 68.39 ? 273 ASN E N 1 ATOM 9510 C CA . ASN E 1 274 ? 16.074 -26.610 55.326 1.00 71.93 ? 273 ASN E CA 1 ATOM 9511 C C . ASN E 1 274 ? 16.330 -27.971 54.645 1.00 72.43 ? 273 ASN E C 1 ATOM 9512 O O . ASN E 1 274 ? 16.299 -29.013 55.295 1.00 76.30 ? 273 ASN E O 1 ATOM 9513 C CB . ASN E 1 274 ? 15.120 -26.784 56.522 1.00 76.52 ? 273 ASN E CB 1 ATOM 9514 C CG . ASN E 1 274 ? 15.467 -25.872 57.680 1.00 77.74 ? 273 ASN E CG 1 ATOM 9515 O OD1 . ASN E 1 274 ? 15.243 -24.660 57.625 1.00 75.85 ? 273 ASN E OD1 1 ATOM 9516 N ND2 . ASN E 1 274 ? 16.013 -26.453 58.743 1.00 81.12 ? 273 ASN E ND2 1 ATOM 9517 N N . CYS E 1 275 ? 16.604 -27.947 53.344 1.00 68.94 ? 274 CYS E N 1 ATOM 9518 C CA . CYS E 1 275 ? 16.851 -29.157 52.563 1.00 68.98 ? 274 CYS E CA 1 ATOM 9519 C C . CYS E 1 275 ? 18.315 -29.209 52.143 1.00 66.74 ? 274 CYS E C 1 ATOM 9520 O O . CYS E 1 275 ? 19.035 -28.204 52.219 1.00 64.15 ? 274 CYS E O 1 ATOM 9521 C CB . CYS E 1 275 ? 15.976 -29.150 51.308 1.00 67.28 ? 274 CYS E CB 1 ATOM 9522 S SG . CYS E 1 275 ? 15.880 -27.511 50.526 1.00 63.98 ? 274 CYS E SG 1 ATOM 9523 N N . ASN E 1 276 ? 18.746 -30.385 51.696 1.00 67.37 ? 275 ASN E N 1 ATOM 9524 C CA . ASN E 1 276 ? 20.044 -30.544 51.054 1.00 65.77 ? 275 ASN E CA 1 ATOM 9525 C C . ASN E 1 276 ? 19.816 -30.953 49.608 1.00 63.70 ? 275 ASN E C 1 ATOM 9526 O O . ASN E 1 276 ? 18.816 -31.599 49.297 1.00 64.73 ? 275 ASN E O 1 ATOM 9527 C CB . ASN E 1 276 ? 20.889 -31.590 51.784 1.00 69.37 ? 275 ASN E CB 1 ATOM 9528 C CG . ASN E 1 276 ? 22.361 -31.518 51.415 1.00 68.78 ? 275 ASN E CG 1 ATOM 9529 O OD1 . ASN E 1 276 ? 22.917 -30.435 51.211 1.00 66.17 ? 275 ASN E OD1 1 ATOM 9530 N ND2 . ASN E 1 276 ? 23.008 -32.673 51.343 1.00 71.71 ? 275 ASN E ND2 1 ATOM 9531 N N . THR E 1 277 ? 20.728 -30.557 48.724 1.00 61.35 ? 276 THR E N 1 ATOM 9532 C CA . THR E 1 277 ? 20.609 -30.884 47.306 1.00 59.79 ? 276 THR E CA 1 ATOM 9533 C C . THR E 1 277 ? 21.970 -30.958 46.628 1.00 59.73 ? 276 THR E C 1 ATOM 9534 O O . THR E 1 277 ? 22.968 -30.471 47.157 1.00 59.58 ? 276 THR E O 1 ATOM 9535 C CB . THR E 1 277 ? 19.693 -29.886 46.556 1.00 56.71 ? 276 THR E CB 1 ATOM 9536 O OG1 . THR E 1 277 ? 19.273 -30.455 45.313 1.00 56.20 ? 276 THR E OG1 1 ATOM 9537 C CG2 . THR E 1 277 ? 20.395 -28.570 46.277 1.00 54.14 ? 276 THR E CG2 1 ATOM 9538 N N . LYS E 1 278 ? 21.988 -31.612 45.469 1.00 60.41 ? 277 LYS E N 1 ATOM 9539 C CA . LYS E 1 278 ? 23.145 -31.644 44.580 1.00 60.84 ? 277 LYS E CA 1 ATOM 9540 C C . LYS E 1 278 ? 22.992 -30.608 43.467 1.00 58.11 ? 277 LYS E C 1 ATOM 9541 O O . LYS E 1 278 ? 23.956 -30.310 42.767 1.00 58.18 ? 277 LYS E O 1 ATOM 9542 C CB . LYS E 1 278 ? 23.280 -33.030 43.946 1.00 63.48 ? 277 LYS E CB 1 ATOM 9543 C CG . LYS E 1 278 ? 23.771 -34.123 44.884 1.00 67.80 ? 277 LYS E CG 1 ATOM 9544 C CD . LYS E 1 278 ? 25.272 -34.025 45.157 1.00 69.78 ? 277 LYS E CD 1 ATOM 9545 C CE . LYS E 1 278 ? 25.978 -35.358 44.899 1.00 73.93 ? 277 LYS E CE 1 ATOM 9546 N NZ . LYS E 1 278 ? 25.507 -36.473 45.770 1.00 77.11 ? 277 LYS E NZ 1 ATOM 9547 N N . CYS E 1 279 ? 21.781 -30.066 43.308 1.00 56.59 ? 278 CYS E N 1 ATOM 9548 C CA . CYS E 1 279 ? 21.447 -29.207 42.175 1.00 54.60 ? 278 CYS E CA 1 ATOM 9549 C C . CYS E 1 279 ? 20.375 -28.167 42.521 1.00 52.46 ? 278 CYS E C 1 ATOM 9550 O O . CYS E 1 279 ? 19.210 -28.518 42.722 1.00 52.62 ? 278 CYS E O 1 ATOM 9551 C CB . CYS E 1 279 ? 20.961 -30.078 41.017 1.00 55.83 ? 278 CYS E CB 1 ATOM 9552 S SG . CYS E 1 279 ? 20.552 -29.200 39.492 1.00 54.46 ? 278 CYS E SG 1 ATOM 9553 N N . GLN E 1 280 ? 20.776 -26.894 42.575 1.00 50.29 ? 279 GLN E N 1 ATOM 9554 C CA . GLN E 1 280 ? 19.856 -25.786 42.845 1.00 48.68 ? 279 GLN E CA 1 ATOM 9555 C C . GLN E 1 280 ? 19.594 -24.945 41.610 1.00 46.93 ? 279 GLN E C 1 ATOM 9556 O O . GLN E 1 280 ? 20.530 -24.557 40.902 1.00 46.24 ? 279 GLN E O 1 ATOM 9557 C CB . GLN E 1 280 ? 20.414 -24.840 43.921 1.00 48.49 ? 279 GLN E CB 1 ATOM 9558 C CG . GLN E 1 280 ? 19.813 -24.998 45.310 1.00 49.92 ? 279 GLN E CG 1 ATOM 9559 C CD . GLN E 1 280 ? 18.314 -24.727 45.404 1.00 49.86 ? 279 GLN E CD 1 ATOM 9560 O OE1 . GLN E 1 280 ? 17.670 -25.230 46.302 1.00 52.42 ? 279 GLN E OE1 1 ATOM 9561 N NE2 . GLN E 1 280 ? 17.765 -23.942 44.494 1.00 48.28 ? 279 GLN E NE2 1 ATOM 9562 N N . THR E 1 281 ? 18.321 -24.639 41.381 1.00 46.20 ? 280 THR E N 1 ATOM 9563 C CA . THR E 1 281 ? 17.942 -23.584 40.457 1.00 45.20 ? 280 THR E CA 1 ATOM 9564 C C . THR E 1 281 ? 17.335 -22.466 41.296 1.00 45.29 ? 280 THR E C 1 ATOM 9565 O O . THR E 1 281 ? 17.012 -22.683 42.461 1.00 46.18 ? 280 THR E O 1 ATOM 9566 C CB . THR E 1 281 ? 16.924 -24.069 39.410 1.00 45.13 ? 280 THR E CB 1 ATOM 9567 O OG1 . THR E 1 281 ? 15.597 -23.929 39.926 1.00 45.44 ? 280 THR E OG1 1 ATOM 9568 C CG2 . THR E 1 281 ? 17.197 -25.515 39.017 1.00 45.80 ? 280 THR E CG2 1 ATOM 9569 N N . PRO E 1 282 ? 17.158 -21.268 40.714 1.00 44.80 ? 281 PRO E N 1 ATOM 9570 C CA . PRO E 1 282 ? 16.591 -20.185 41.525 1.00 45.22 ? 281 PRO E CA 1 ATOM 9571 C C . PRO E 1 282 ? 15.127 -20.420 41.899 1.00 46.78 ? 281 PRO E C 1 ATOM 9572 O O . PRO E 1 282 ? 14.600 -19.720 42.754 1.00 47.47 ? 281 PRO E O 1 ATOM 9573 C CB . PRO E 1 282 ? 16.714 -18.955 40.617 1.00 44.67 ? 281 PRO E CB 1 ATOM 9574 C CG . PRO E 1 282 ? 17.611 -19.356 39.498 1.00 44.21 ? 281 PRO E CG 1 ATOM 9575 C CD . PRO E 1 282 ? 17.408 -20.830 39.336 1.00 44.21 ? 281 PRO E CD 1 ATOM 9576 N N . ILE E 1 283 ? 14.488 -21.402 41.266 1.00 47.57 ? 282 ILE E N 1 ATOM 9577 C CA . ILE E 1 283 ? 13.061 -21.642 41.450 1.00 49.69 ? 282 ILE E CA 1 ATOM 9578 C C . ILE E 1 283 ? 12.783 -22.961 42.193 1.00 50.93 ? 282 ILE E C 1 ATOM 9579 O O . ILE E 1 283 ? 11.688 -23.177 42.723 1.00 52.85 ? 282 ILE E O 1 ATOM 9580 C CB . ILE E 1 283 ? 12.353 -21.545 40.070 1.00 50.36 ? 282 ILE E CB 1 ATOM 9581 C CG1 . ILE E 1 283 ? 11.031 -20.775 40.189 1.00 52.88 ? 282 ILE E CG1 1 ATOM 9582 C CG2 . ILE E 1 283 ? 12.180 -22.909 39.404 1.00 50.27 ? 282 ILE E CG2 1 ATOM 9583 C CD1 . ILE E 1 283 ? 10.737 -19.889 38.996 1.00 53.39 ? 282 ILE E CD1 1 ATOM 9584 N N . GLY E 1 284 ? 13.788 -23.828 42.248 1.00 50.52 ? 283 GLY E N 1 ATOM 9585 C CA . GLY E 1 284 ? 13.694 -25.066 43.008 1.00 52.34 ? 283 GLY E CA 1 ATOM 9586 C C . GLY E 1 284 ? 14.931 -25.926 42.879 1.00 51.78 ? 283 GLY E C 1 ATOM 9587 O O . GLY E 1 284 ? 15.715 -25.758 41.955 1.00 49.65 ? 283 GLY E O 1 ATOM 9588 N N . ALA E 1 285 ? 15.101 -26.841 43.830 1.00 54.71 ? 284 ALA E N 1 ATOM 9589 C CA . ALA E 1 285 ? 16.178 -27.831 43.792 1.00 55.69 ? 284 ALA E CA 1 ATOM 9590 C C . ALA E 1 285 ? 15.734 -29.030 42.968 1.00 56.58 ? 284 ALA E C 1 ATOM 9591 O O . ALA E 1 285 ? 14.543 -29.214 42.742 1.00 58.05 ? 284 ALA E O 1 ATOM 9592 C CB . ALA E 1 285 ? 16.549 -28.265 45.202 1.00 57.92 ? 284 ALA E CB 1 ATOM 9593 N N . ILE E 1 286 ? 16.689 -29.846 42.530 1.00 57.01 ? 285 ILE E N 1 ATOM 9594 C CA . ILE E 1 286 ? 16.407 -30.967 41.631 1.00 57.89 ? 285 ILE E CA 1 ATOM 9595 C C . ILE E 1 286 ? 17.097 -32.232 42.115 1.00 60.41 ? 285 ILE E C 1 ATOM 9596 O O . ILE E 1 286 ? 18.287 -32.214 42.418 1.00 61.07 ? 285 ILE E O 1 ATOM 9597 C CB . ILE E 1 286 ? 16.891 -30.660 40.198 1.00 56.37 ? 285 ILE E CB 1 ATOM 9598 C CG1 . ILE E 1 286 ? 16.058 -29.530 39.585 1.00 55.01 ? 285 ILE E CG1 1 ATOM 9599 C CG2 . ILE E 1 286 ? 16.821 -31.898 39.313 1.00 57.24 ? 285 ILE E CG2 1 ATOM 9600 C CD1 . ILE E 1 286 ? 16.659 -28.954 38.320 1.00 53.88 ? 285 ILE E CD1 1 ATOM 9601 N N . ASN E 1 287 ? 16.340 -33.326 42.169 1.00 62.32 ? 286 ASN E N 1 ATOM 9602 C CA . ASN E 1 287 ? 16.859 -34.629 42.559 1.00 65.39 ? 286 ASN E CA 1 ATOM 9603 C C . ASN E 1 287 ? 16.471 -35.628 41.473 1.00 66.12 ? 286 ASN E C 1 ATOM 9604 O O . ASN E 1 287 ? 15.357 -36.154 41.471 1.00 66.86 ? 286 ASN E O 1 ATOM 9605 C CB . ASN E 1 287 ? 16.289 -35.043 43.924 1.00 68.34 ? 286 ASN E CB 1 ATOM 9606 C CG . ASN E 1 287 ? 16.772 -36.413 44.378 1.00 72.39 ? 286 ASN E CG 1 ATOM 9607 O OD1 . ASN E 1 287 ? 17.970 -36.702 44.354 1.00 73.21 ? 286 ASN E OD1 1 ATOM 9608 N ND2 . ASN E 1 287 ? 15.837 -37.261 44.809 1.00 75.30 ? 286 ASN E ND2 1 ATOM 9609 N N . SER E 1 288 ? 17.392 -35.870 40.544 1.00 65.83 ? 287 SER E N 1 ATOM 9610 C CA . SER E 1 288 ? 17.094 -36.637 39.339 1.00 66.30 ? 287 SER E CA 1 ATOM 9611 C C . SER E 1 288 ? 18.328 -37.311 38.755 1.00 67.87 ? 287 SER E C 1 ATOM 9612 O O . SER E 1 288 ? 19.447 -36.831 38.927 1.00 67.46 ? 287 SER E O 1 ATOM 9613 C CB . SER E 1 288 ? 16.497 -35.709 38.279 1.00 63.64 ? 287 SER E CB 1 ATOM 9614 O OG . SER E 1 288 ? 16.245 -36.396 37.065 1.00 63.60 ? 287 SER E OG 1 ATOM 9615 N N . SER E 1 289 ? 18.106 -38.428 38.064 1.00 69.88 ? 288 SER E N 1 ATOM 9616 C CA . SER E 1 289 ? 19.153 -39.101 37.303 1.00 71.60 ? 288 SER E CA 1 ATOM 9617 C C . SER E 1 289 ? 18.922 -38.945 35.796 1.00 70.05 ? 288 SER E C 1 ATOM 9618 O O . SER E 1 289 ? 19.628 -39.551 34.992 1.00 71.07 ? 288 SER E O 1 ATOM 9619 C CB . SER E 1 289 ? 19.223 -40.582 37.690 1.00 75.91 ? 288 SER E CB 1 ATOM 9620 O OG . SER E 1 289 ? 17.971 -41.227 37.512 1.00 76.42 ? 288 SER E OG 1 ATOM 9621 N N . MET E 1 290 ? 17.946 -38.117 35.422 1.00 67.82 ? 289 MET E N 1 ATOM 9622 C CA . MET E 1 290 ? 17.662 -37.822 34.014 1.00 66.66 ? 289 MET E CA 1 ATOM 9623 C C . MET E 1 290 ? 18.793 -36.982 33.408 1.00 65.33 ? 289 MET E C 1 ATOM 9624 O O . MET E 1 290 ? 19.388 -36.160 34.106 1.00 65.11 ? 289 MET E O 1 ATOM 9625 C CB . MET E 1 290 ? 16.361 -37.025 33.886 1.00 64.99 ? 289 MET E CB 1 ATOM 9626 C CG . MET E 1 290 ? 15.116 -37.739 34.381 1.00 66.53 ? 289 MET E CG 1 ATOM 9627 S SD . MET E 1 290 ? 14.460 -38.898 33.176 1.00 68.58 ? 289 MET E SD 1 ATOM 9628 C CE . MET E 1 290 ? 12.800 -39.112 33.815 1.00 69.36 ? 289 MET E CE 1 ATOM 9629 N N . PRO E 1 291 ? 19.095 -37.188 32.109 1.00 64.89 ? 290 PRO E N 1 ATOM 9630 C CA . PRO E 1 291 ? 20.130 -36.385 31.451 1.00 63.81 ? 290 PRO E CA 1 ATOM 9631 C C . PRO E 1 291 ? 19.722 -34.925 31.176 1.00 60.57 ? 290 PRO E C 1 ATOM 9632 O O . PRO E 1 291 ? 20.589 -34.043 31.142 1.00 60.45 ? 290 PRO E O 1 ATOM 9633 C CB . PRO E 1 291 ? 20.396 -37.145 30.142 1.00 66.03 ? 290 PRO E CB 1 ATOM 9634 C CG . PRO E 1 291 ? 19.183 -37.979 29.904 1.00 66.16 ? 290 PRO E CG 1 ATOM 9635 C CD . PRO E 1 291 ? 18.597 -38.283 31.248 1.00 66.19 ? 290 PRO E CD 1 ATOM 9636 N N . PHE E 1 292 ? 18.422 -34.678 30.995 1.00 57.96 ? 291 PHE E N 1 ATOM 9637 C CA . PHE E 1 292 ? 17.904 -33.339 30.687 1.00 54.84 ? 291 PHE E CA 1 ATOM 9638 C C . PHE E 1 292 ? 16.847 -32.882 31.682 1.00 52.78 ? 291 PHE E C 1 ATOM 9639 O O . PHE E 1 292 ? 16.150 -33.702 32.274 1.00 53.03 ? 291 PHE E O 1 ATOM 9640 C CB . PHE E 1 292 ? 17.262 -33.308 29.293 1.00 55.00 ? 291 PHE E CB 1 ATOM 9641 C CG . PHE E 1 292 ? 18.190 -33.702 28.181 1.00 56.47 ? 291 PHE E CG 1 ATOM 9642 C CD1 . PHE E 1 292 ? 19.045 -32.773 27.614 1.00 56.61 ? 291 PHE E CD1 1 ATOM 9643 C CD2 . PHE E 1 292 ? 18.200 -35.003 27.696 1.00 58.18 ? 291 PHE E CD2 1 ATOM 9644 C CE1 . PHE E 1 292 ? 19.904 -33.134 26.587 1.00 58.86 ? 291 PHE E CE1 1 ATOM 9645 C CE2 . PHE E 1 292 ? 19.048 -35.371 26.663 1.00 60.15 ? 291 PHE E CE2 1 ATOM 9646 C CZ . PHE E 1 292 ? 19.904 -34.435 26.111 1.00 60.67 ? 291 PHE E CZ 1 ATOM 9647 N N . HIS E 1 293 ? 16.724 -31.565 31.837 1.00 50.53 ? 292 HIS E N 1 ATOM 9648 C CA . HIS E 1 293 ? 15.625 -30.963 32.593 1.00 49.34 ? 292 HIS E CA 1 ATOM 9649 C C . HIS E 1 293 ? 15.204 -29.674 31.901 1.00 47.79 ? 292 HIS E C 1 ATOM 9650 O O . HIS E 1 293 ? 15.911 -29.181 31.034 1.00 47.75 ? 292 HIS E O 1 ATOM 9651 C CB . HIS E 1 293 ? 16.060 -30.663 34.026 1.00 49.11 ? 292 HIS E CB 1 ATOM 9652 C CG . HIS E 1 293 ? 17.033 -29.533 34.125 1.00 48.32 ? 292 HIS E CG 1 ATOM 9653 N ND1 . HIS E 1 293 ? 16.677 -28.279 34.574 1.00 47.26 ? 292 HIS E ND1 1 ATOM 9654 C CD2 . HIS E 1 293 ? 18.343 -29.456 33.795 1.00 48.55 ? 292 HIS E CD2 1 ATOM 9655 C CE1 . HIS E 1 293 ? 17.730 -27.485 34.538 1.00 46.73 ? 292 HIS E CE1 1 ATOM 9656 N NE2 . HIS E 1 293 ? 18.754 -28.174 34.069 1.00 47.70 ? 292 HIS E NE2 1 ATOM 9657 N N . ASN E 1 294 ? 14.061 -29.125 32.288 1.00 47.03 ? 293 ASN E N 1 ATOM 9658 C CA . ASN E 1 294 ? 13.572 -27.892 31.676 1.00 46.85 ? 293 ASN E CA 1 ATOM 9659 C C . ASN E 1 294 ? 13.042 -26.900 32.710 1.00 46.13 ? 293 ASN E C 1 ATOM 9660 O O . ASN E 1 294 ? 12.100 -26.157 32.446 1.00 46.31 ? 293 ASN E O 1 ATOM 9661 C CB . ASN E 1 294 ? 12.494 -28.218 30.647 1.00 47.89 ? 293 ASN E CB 1 ATOM 9662 C CG . ASN E 1 294 ? 11.226 -28.750 31.278 1.00 48.96 ? 293 ASN E CG 1 ATOM 9663 O OD1 . ASN E 1 294 ? 11.118 -28.874 32.501 1.00 48.55 ? 293 ASN E OD1 1 ATOM 9664 N ND2 . ASN E 1 294 ? 10.254 -29.075 30.439 1.00 50.61 ? 293 ASN E ND2 1 ATOM 9665 N N . ILE E 1 295 ? 13.682 -26.888 33.874 1.00 45.31 ? 294 ILE E N 1 ATOM 9666 C CA . ILE E 1 295 ? 13.213 -26.140 35.030 1.00 45.40 ? 294 ILE E CA 1 ATOM 9667 C C . ILE E 1 295 ? 13.631 -24.675 34.905 1.00 44.70 ? 294 ILE E C 1 ATOM 9668 O O . ILE E 1 295 ? 12.782 -23.784 34.840 1.00 45.55 ? 294 ILE E O 1 ATOM 9669 C CB . ILE E 1 295 ? 13.780 -26.733 36.343 1.00 45.35 ? 294 ILE E CB 1 ATOM 9670 C CG1 . ILE E 1 295 ? 13.451 -28.238 36.456 1.00 46.61 ? 294 ILE E CG1 1 ATOM 9671 C CG2 . ILE E 1 295 ? 13.271 -25.959 37.553 1.00 45.48 ? 294 ILE E CG2 1 ATOM 9672 C CD1 . ILE E 1 295 ? 11.980 -28.574 36.355 1.00 47.97 ? 294 ILE E CD1 1 ATOM 9673 N N . HIS E 1 296 ? 14.939 -24.440 34.868 1.00 43.39 ? 295 HIS E N 1 ATOM 9674 C CA . HIS E 1 296 ? 15.479 -23.095 34.776 1.00 43.05 ? 295 HIS E CA 1 ATOM 9675 C C . HIS E 1 296 ? 16.856 -23.184 34.122 1.00 43.02 ? 295 HIS E C 1 ATOM 9676 O O . HIS E 1 296 ? 17.570 -24.167 34.333 1.00 42.88 ? 295 HIS E O 1 ATOM 9677 C CB . HIS E 1 296 ? 15.584 -22.476 36.174 1.00 42.38 ? 295 HIS E CB 1 ATOM 9678 C CG . HIS E 1 296 ? 15.503 -20.983 36.186 1.00 42.50 ? 295 HIS E CG 1 ATOM 9679 N ND1 . HIS E 1 296 ? 16.620 -20.176 36.158 1.00 42.24 ? 295 HIS E ND1 1 ATOM 9680 C CD2 . HIS E 1 296 ? 14.438 -20.147 36.229 1.00 43.48 ? 295 HIS E CD2 1 ATOM 9681 C CE1 . HIS E 1 296 ? 16.249 -18.907 36.183 1.00 42.63 ? 295 HIS E CE1 1 ATOM 9682 N NE2 . HIS E 1 296 ? 14.930 -18.862 36.223 1.00 43.69 ? 295 HIS E NE2 1 ATOM 9683 N N . PRO E 1 297 ? 17.230 -22.171 33.318 1.00 43.44 ? 296 PRO E N 1 ATOM 9684 C CA . PRO E 1 297 ? 18.566 -22.144 32.722 1.00 44.10 ? 296 PRO E CA 1 ATOM 9685 C C . PRO E 1 297 ? 19.717 -21.973 33.718 1.00 43.93 ? 296 PRO E C 1 ATOM 9686 O O . PRO E 1 297 ? 20.799 -22.497 33.493 1.00 44.95 ? 296 PRO E O 1 ATOM 9687 C CB . PRO E 1 297 ? 18.508 -20.934 31.772 1.00 45.14 ? 296 PRO E CB 1 ATOM 9688 C CG . PRO E 1 297 ? 17.368 -20.108 32.254 1.00 44.92 ? 296 PRO E CG 1 ATOM 9689 C CD . PRO E 1 297 ? 16.378 -21.092 32.792 1.00 44.31 ? 296 PRO E CD 1 ATOM 9690 N N . LEU E 1 298 ? 19.504 -21.227 34.792 1.00 43.55 ? 297 LEU E N 1 ATOM 9691 C CA . LEU E 1 298 ? 20.589 -20.926 35.736 1.00 43.61 ? 297 LEU E CA 1 ATOM 9692 C C . LEU E 1 298 ? 20.608 -21.938 36.870 1.00 43.44 ? 297 LEU E C 1 ATOM 9693 O O . LEU E 1 298 ? 19.699 -21.967 37.676 1.00 43.82 ? 297 LEU E O 1 ATOM 9694 C CB . LEU E 1 298 ? 20.446 -19.498 36.275 1.00 43.10 ? 297 LEU E CB 1 ATOM 9695 C CG . LEU E 1 298 ? 20.218 -18.438 35.186 1.00 44.16 ? 297 LEU E CG 1 ATOM 9696 C CD1 . LEU E 1 298 ? 20.170 -17.034 35.768 1.00 44.32 ? 297 LEU E CD1 1 ATOM 9697 C CD2 . LEU E 1 298 ? 21.289 -18.539 34.110 1.00 45.31 ? 297 LEU E CD2 1 ATOM 9698 N N . THR E 1 299 ? 21.629 -22.790 36.909 1.00 44.42 ? 298 THR E N 1 ATOM 9699 C CA . THR E 1 299 ? 21.756 -23.788 37.973 1.00 44.92 ? 298 THR E CA 1 ATOM 9700 C C . THR E 1 299 ? 23.181 -23.856 38.506 1.00 45.97 ? 298 THR E C 1 ATOM 9701 O O . THR E 1 299 ? 24.101 -23.302 37.905 1.00 46.65 ? 298 THR E O 1 ATOM 9702 C CB . THR E 1 299 ? 21.320 -25.197 37.503 1.00 45.43 ? 298 THR E CB 1 ATOM 9703 O OG1 . THR E 1 299 ? 22.327 -25.780 36.666 1.00 46.27 ? 298 THR E OG1 1 ATOM 9704 C CG2 . THR E 1 299 ? 20.002 -25.128 36.744 1.00 45.00 ? 298 THR E CG2 1 ATOM 9705 N N . ILE E 1 300 ? 23.344 -24.524 39.646 1.00 46.80 ? 299 ILE E N 1 ATOM 9706 C CA . ILE E 1 300 ? 24.663 -24.796 40.217 1.00 48.82 ? 299 ILE E CA 1 ATOM 9707 C C . ILE E 1 300 ? 24.696 -26.222 40.769 1.00 51.14 ? 299 ILE E C 1 ATOM 9708 O O . ILE E 1 300 ? 23.670 -26.742 41.197 1.00 51.60 ? 299 ILE E O 1 ATOM 9709 C CB . ILE E 1 300 ? 25.041 -23.756 41.306 1.00 48.05 ? 299 ILE E CB 1 ATOM 9710 C CG1 . ILE E 1 300 ? 26.489 -23.959 41.777 1.00 49.83 ? 299 ILE E CG1 1 ATOM 9711 C CG2 . ILE E 1 300 ? 24.073 -23.815 42.478 1.00 47.40 ? 299 ILE E CG2 1 ATOM 9712 C CD1 . ILE E 1 300 ? 26.990 -22.913 42.753 1.00 49.43 ? 299 ILE E CD1 1 ATOM 9713 N N . GLY E 1 301 ? 25.869 -26.851 40.736 1.00 54.21 ? 300 GLY E N 1 ATOM 9714 C CA . GLY E 1 301 ? 26.068 -28.188 41.313 1.00 57.31 ? 300 GLY E CA 1 ATOM 9715 C C . GLY E 1 301 ? 25.986 -29.293 40.275 1.00 59.44 ? 300 GLY E C 1 ATOM 9716 O O . GLY E 1 301 ? 25.979 -29.017 39.078 1.00 59.43 ? 300 GLY E O 1 ATOM 9717 N N . GLU E 1 302 ? 25.932 -30.544 40.729 1.00 62.37 ? 301 GLU E N 1 ATOM 9718 C CA . GLU E 1 302 ? 25.746 -31.690 39.824 1.00 64.29 ? 301 GLU E CA 1 ATOM 9719 C C . GLU E 1 302 ? 24.315 -31.709 39.276 1.00 61.92 ? 301 GLU E C 1 ATOM 9720 O O . GLU E 1 302 ? 23.388 -32.159 39.953 1.00 61.32 ? 301 GLU E O 1 ATOM 9721 C CB . GLU E 1 302 ? 26.063 -33.024 40.524 1.00 68.19 ? 301 GLU E CB 1 ATOM 9722 C CG . GLU E 1 302 ? 27.538 -33.404 40.531 1.00 71.80 ? 301 GLU E CG 1 ATOM 9723 N N . CYS E 1 303 ? 24.156 -31.216 38.048 1.00 60.55 ? 302 CYS E N 1 ATOM 9724 C CA . CYS E 1 303 ? 22.848 -31.037 37.424 1.00 58.35 ? 302 CYS E CA 1 ATOM 9725 C C . CYS E 1 303 ? 22.794 -31.707 36.059 1.00 58.42 ? 302 CYS E C 1 ATOM 9726 O O . CYS E 1 303 ? 23.831 -31.955 35.452 1.00 59.72 ? 302 CYS E O 1 ATOM 9727 C CB . CYS E 1 303 ? 22.558 -29.542 37.232 1.00 56.26 ? 302 CYS E CB 1 ATOM 9728 S SG . CYS E 1 303 ? 22.369 -28.596 38.761 1.00 56.67 ? 302 CYS E SG 1 ATOM 9729 N N . PRO E 1 304 ? 21.577 -31.981 35.561 1.00 57.22 ? 303 PRO E N 1 ATOM 9730 C CA . PRO E 1 304 ? 21.422 -32.371 34.164 1.00 57.57 ? 303 PRO E CA 1 ATOM 9731 C C . PRO E 1 304 ? 21.508 -31.169 33.220 1.00 56.21 ? 303 PRO E C 1 ATOM 9732 O O . PRO E 1 304 ? 21.551 -30.017 33.665 1.00 53.86 ? 303 PRO E O 1 ATOM 9733 C CB . PRO E 1 304 ? 20.012 -32.981 34.107 1.00 57.14 ? 303 PRO E CB 1 ATOM 9734 C CG . PRO E 1 304 ? 19.397 -32.782 35.454 1.00 56.52 ? 303 PRO E CG 1 ATOM 9735 C CD . PRO E 1 304 ? 20.280 -31.880 36.250 1.00 55.86 ? 303 PRO E CD 1 ATOM 9736 N N . LYS E 1 305 ? 21.507 -31.447 31.921 1.00 56.99 ? 304 LYS E N 1 ATOM 9737 C CA . LYS E 1 305 ? 21.575 -30.392 30.918 1.00 56.36 ? 304 LYS E CA 1 ATOM 9738 C C . LYS E 1 305 ? 20.198 -29.782 30.659 1.00 53.55 ? 304 LYS E C 1 ATOM 9739 O O . LYS E 1 305 ? 19.223 -30.487 30.432 1.00 53.04 ? 304 LYS E O 1 ATOM 9740 C CB . LYS E 1 305 ? 22.181 -30.934 29.625 1.00 59.20 ? 304 LYS E CB 1 ATOM 9741 C CG . LYS E 1 305 ? 23.617 -31.423 29.775 1.00 62.32 ? 304 LYS E CG 1 ATOM 9742 C CD . LYS E 1 305 ? 24.523 -30.323 30.326 1.00 63.00 ? 304 LYS E CD 1 ATOM 9743 C CE . LYS E 1 305 ? 25.997 -30.650 30.142 1.00 66.72 ? 304 LYS E CE 1 ATOM 9744 N NZ . LYS E 1 305 ? 26.878 -29.525 30.571 1.00 67.25 ? 304 LYS E NZ 1 ATOM 9745 N N . TYR E 1 306 ? 20.134 -28.459 30.703 1.00 51.68 ? 305 TYR E N 1 ATOM 9746 C CA . TYR E 1 306 ? 18.892 -27.740 30.480 1.00 50.26 ? 305 TYR E CA 1 ATOM 9747 C C . TYR E 1 306 ? 18.512 -27.688 28.997 1.00 51.52 ? 305 TYR E C 1 ATOM 9748 O O . TYR E 1 306 ? 19.358 -27.411 28.145 1.00 52.74 ? 305 TYR E O 1 ATOM 9749 C CB . TYR E 1 306 ? 19.012 -26.307 31.004 1.00 48.78 ? 305 TYR E CB 1 ATOM 9750 C CG . TYR E 1 306 ? 17.763 -25.488 30.785 1.00 47.82 ? 305 TYR E CG 1 ATOM 9751 C CD1 . TYR E 1 306 ? 16.688 -25.575 31.660 1.00 46.92 ? 305 TYR E CD1 1 ATOM 9752 C CD2 . TYR E 1 306 ? 17.649 -24.639 29.694 1.00 48.38 ? 305 TYR E CD2 1 ATOM 9753 C CE1 . TYR E 1 306 ? 15.544 -24.825 31.462 1.00 46.96 ? 305 TYR E CE1 1 ATOM 9754 C CE2 . TYR E 1 306 ? 16.511 -23.889 29.488 1.00 48.33 ? 305 TYR E CE2 1 ATOM 9755 C CZ . TYR E 1 306 ? 15.463 -23.984 30.374 1.00 47.55 ? 305 TYR E CZ 1 ATOM 9756 O OH . TYR E 1 306 ? 14.326 -23.249 30.167 1.00 48.05 ? 305 TYR E OH 1 ATOM 9757 N N . VAL E 1 307 ? 17.234 -27.930 28.710 1.00 51.07 ? 306 VAL E N 1 ATOM 9758 C CA . VAL E 1 307 ? 16.655 -27.653 27.395 1.00 52.14 ? 306 VAL E CA 1 ATOM 9759 C C . VAL E 1 307 ? 15.319 -26.940 27.587 1.00 52.24 ? 306 VAL E C 1 ATOM 9760 O O . VAL E 1 307 ? 14.763 -26.942 28.689 1.00 51.34 ? 306 VAL E O 1 ATOM 9761 C CB . VAL E 1 307 ? 16.457 -28.937 26.559 1.00 53.12 ? 306 VAL E CB 1 ATOM 9762 C CG1 . VAL E 1 307 ? 17.804 -29.524 26.167 1.00 54.20 ? 306 VAL E CG1 1 ATOM 9763 C CG2 . VAL E 1 307 ? 15.620 -29.969 27.309 1.00 52.41 ? 306 VAL E CG2 1 ATOM 9764 N N . LYS E 1 308 ? 14.816 -26.321 26.521 1.00 54.05 ? 307 LYS E N 1 ATOM 9765 C CA . LYS E 1 308 ? 13.503 -25.663 26.554 1.00 54.69 ? 307 LYS E CA 1 ATOM 9766 C C . LYS E 1 308 ? 12.379 -26.604 26.106 1.00 55.63 ? 307 LYS E C 1 ATOM 9767 O O . LYS E 1 308 ? 11.225 -26.189 25.964 1.00 56.62 ? 307 LYS E O 1 ATOM 9768 C CB . LYS E 1 308 ? 13.501 -24.419 25.668 1.00 56.05 ? 307 LYS E CB 1 ATOM 9769 C CG . LYS E 1 308 ? 14.368 -23.293 26.174 1.00 55.92 ? 307 LYS E CG 1 ATOM 9770 C CD . LYS E 1 308 ? 14.136 -22.043 25.340 1.00 58.44 ? 307 LYS E CD 1 ATOM 9771 C CE . LYS E 1 308 ? 15.068 -20.916 25.742 1.00 58.55 ? 307 LYS E CE 1 ATOM 9772 N NZ . LYS E 1 308 ? 15.002 -19.789 24.772 1.00 61.54 ? 307 LYS E NZ 1 ATOM 9773 N N . SER E 1 309 ? 12.706 -27.870 25.882 1.00 55.92 ? 308 SER E N 1 ATOM 9774 C CA . SER E 1 309 ? 11.707 -28.816 25.419 1.00 57.28 ? 308 SER E CA 1 ATOM 9775 C C . SER E 1 309 ? 10.629 -28.994 26.473 1.00 57.38 ? 308 SER E C 1 ATOM 9776 O O . SER E 1 309 ? 10.927 -29.087 27.665 1.00 55.98 ? 308 SER E O 1 ATOM 9777 C CB . SER E 1 309 ? 12.346 -30.166 25.100 1.00 57.33 ? 308 SER E CB 1 ATOM 9778 O OG . SER E 1 309 ? 13.440 -29.996 24.217 1.00 58.42 ? 308 SER E OG 1 ATOM 9779 N N . SER E 1 310 ? 9.376 -29.023 26.026 1.00 59.58 ? 309 SER E N 1 ATOM 9780 C CA . SER E 1 310 ? 8.273 -29.426 26.886 1.00 60.61 ? 309 SER E CA 1 ATOM 9781 C C . SER E 1 310 ? 8.280 -30.944 27.085 1.00 60.95 ? 309 SER E C 1 ATOM 9782 O O . SER E 1 310 ? 7.810 -31.430 28.110 1.00 61.57 ? 309 SER E O 1 ATOM 9783 C CB . SER E 1 310 ? 6.932 -28.973 26.300 1.00 62.95 ? 309 SER E CB 1 ATOM 9784 O OG . SER E 1 310 ? 6.724 -29.509 25.005 1.00 64.41 ? 309 SER E OG 1 ATOM 9785 N N . ARG E 1 311 ? 8.825 -31.685 26.116 1.00 61.36 ? 310 ARG E N 1 ATOM 9786 C CA . ARG E 1 311 ? 8.732 -33.146 26.120 1.00 62.41 ? 310 ARG E CA 1 ATOM 9787 C C . ARG E 1 311 ? 9.875 -33.828 25.364 1.00 61.58 ? 310 ARG E C 1 ATOM 9788 O O . ARG E 1 311 ? 10.239 -33.412 24.268 1.00 61.70 ? 310 ARG E O 1 ATOM 9789 C CB . ARG E 1 311 ? 7.392 -33.568 25.518 1.00 65.22 ? 310 ARG E CB 1 ATOM 9790 C CG . ARG E 1 311 ? 7.249 -35.063 25.290 1.00 66.80 ? 310 ARG E CG 1 ATOM 9791 C CD . ARG E 1 311 ? 5.843 -35.404 24.839 1.00 69.66 ? 310 ARG E CD 1 ATOM 9792 N NE . ARG E 1 311 ? 5.738 -36.796 24.407 1.00 71.44 ? 310 ARG E NE 1 ATOM 9793 C CZ . ARG E 1 311 ? 5.707 -37.844 25.227 1.00 72.89 ? 310 ARG E CZ 1 ATOM 9794 N NH1 . ARG E 1 311 ? 5.776 -37.681 26.546 1.00 73.28 ? 310 ARG E NH1 1 ATOM 9795 N NH2 . ARG E 1 311 ? 5.605 -39.071 24.725 1.00 74.48 ? 310 ARG E NH2 1 ATOM 9796 N N . LEU E 1 312 ? 10.406 -34.900 25.947 1.00 61.35 ? 311 LEU E N 1 ATOM 9797 C CA . LEU E 1 312 ? 11.574 -35.588 25.400 1.00 61.65 ? 311 LEU E CA 1 ATOM 9798 C C . LEU E 1 312 ? 11.562 -37.075 25.794 1.00 62.92 ? 311 LEU E C 1 ATOM 9799 O O . LEU E 1 312 ? 11.950 -37.433 26.913 1.00 62.99 ? 311 LEU E O 1 ATOM 9800 C CB . LEU E 1 312 ? 12.847 -34.905 25.909 1.00 60.65 ? 311 LEU E CB 1 ATOM 9801 C CG . LEU E 1 312 ? 14.000 -34.714 24.924 1.00 61.30 ? 311 LEU E CG 1 ATOM 9802 C CD1 . LEU E 1 312 ? 13.642 -33.700 23.848 1.00 61.40 ? 311 LEU E CD1 1 ATOM 9803 C CD2 . LEU E 1 312 ? 15.247 -34.273 25.674 1.00 60.59 ? 311 LEU E CD2 1 ATOM 9804 N N . VAL E 1 313 ? 11.115 -37.932 24.874 1.00 63.87 ? 312 VAL E N 1 ATOM 9805 C CA . VAL E 1 313 ? 10.977 -39.366 25.148 1.00 64.89 ? 312 VAL E CA 1 ATOM 9806 C C . VAL E 1 313 ? 11.611 -40.221 24.055 1.00 66.33 ? 312 VAL E C 1 ATOM 9807 O O . VAL E 1 313 ? 11.273 -40.088 22.875 1.00 66.16 ? 312 VAL E O 1 ATOM 9808 C CB . VAL E 1 313 ? 9.501 -39.778 25.273 1.00 65.90 ? 312 VAL E CB 1 ATOM 9809 C CG1 . VAL E 1 313 ? 9.386 -41.254 25.672 1.00 68.10 ? 312 VAL E CG1 1 ATOM 9810 C CG2 . VAL E 1 313 ? 8.779 -38.881 26.269 1.00 64.84 ? 312 VAL E CG2 1 ATOM 9811 N N . LEU E 1 314 ? 12.505 -41.117 24.474 1.00 67.49 ? 313 LEU E N 1 ATOM 9812 C CA . LEU E 1 314 ? 13.209 -42.026 23.568 1.00 69.33 ? 313 LEU E CA 1 ATOM 9813 C C . LEU E 1 314 ? 12.444 -43.323 23.374 1.00 71.23 ? 313 LEU E C 1 ATOM 9814 O O . LEU E 1 314 ? 11.969 -43.923 24.340 1.00 71.96 ? 313 LEU E O 1 ATOM 9815 C CB . LEU E 1 314 ? 14.597 -42.374 24.117 1.00 70.23 ? 313 LEU E CB 1 ATOM 9816 C CG . LEU E 1 314 ? 15.759 -41.450 23.765 1.00 69.71 ? 313 LEU E CG 1 ATOM 9817 C CD1 . LEU E 1 314 ? 16.965 -41.780 24.631 1.00 70.85 ? 313 LEU E CD1 1 ATOM 9818 C CD2 . LEU E 1 314 ? 16.109 -41.561 22.288 1.00 71.22 ? 313 LEU E CD2 1 ATOM 9819 N N . ALA E 1 315 ? 12.350 -43.760 22.122 1.00 72.59 ? 314 ALA E N 1 ATOM 9820 C CA . ALA E 1 315 ? 11.802 -45.070 21.800 1.00 74.66 ? 314 ALA E CA 1 ATOM 9821 C C . ALA E 1 315 ? 12.824 -46.129 22.195 1.00 76.95 ? 314 ALA E C 1 ATOM 9822 O O . ALA E 1 315 ? 14.014 -45.967 21.939 1.00 77.88 ? 314 ALA E O 1 ATOM 9823 C CB . ALA E 1 315 ? 11.489 -45.165 20.316 1.00 75.48 ? 314 ALA E CB 1 ATOM 9824 N N . THR E 1 316 ? 12.360 -47.200 22.831 1.00 78.63 ? 315 THR E N 1 ATOM 9825 C CA . THR E 1 316 ? 13.242 -48.273 23.287 1.00 81.46 ? 315 THR E CA 1 ATOM 9826 C C . THR E 1 316 ? 12.829 -49.625 22.711 1.00 84.26 ? 315 THR E C 1 ATOM 9827 O O . THR E 1 316 ? 13.673 -50.367 22.205 1.00 87.00 ? 315 THR E O 1 ATOM 9828 C CB . THR E 1 316 ? 13.279 -48.346 24.826 1.00 81.78 ? 315 THR E CB 1 ATOM 9829 O OG1 . THR E 1 316 ? 11.956 -48.185 25.348 1.00 80.95 ? 315 THR E OG1 1 ATOM 9830 C CG2 . THR E 1 316 ? 14.170 -47.244 25.395 1.00 79.88 ? 315 THR E CG2 1 ATOM 9831 N N . GLY E 1 317 ? 11.537 -49.941 22.792 1.00 84.00 ? 316 GLY E N 1 ATOM 9832 C CA . GLY E 1 317 ? 10.998 -51.181 22.225 1.00 86.54 ? 316 GLY E CA 1 ATOM 9833 C C . GLY E 1 317 ? 10.442 -51.006 20.820 1.00 85.58 ? 316 GLY E C 1 ATOM 9834 O O . GLY E 1 317 ? 10.625 -49.959 20.189 1.00 83.62 ? 316 GLY E O 1 ATOM 9835 N N . LEU E 1 318 ? 9.758 -52.038 20.335 1.00 87.16 ? 317 LEU E N 1 ATOM 9836 C CA . LEU E 1 318 ? 9.159 -52.031 19.002 1.00 86.83 ? 317 LEU E CA 1 ATOM 9837 C C . LEU E 1 318 ? 7.842 -51.258 18.978 1.00 84.61 ? 317 LEU E C 1 ATOM 9838 O O . LEU E 1 318 ? 7.361 -50.796 20.014 1.00 82.94 ? 317 LEU E O 1 ATOM 9839 C CB . LEU E 1 318 ? 8.919 -53.471 18.531 1.00 90.08 ? 317 LEU E CB 1 ATOM 9840 N N . ARG E 1 319 ? 7.264 -51.123 17.785 1.00 84.93 ? 318 ARG E N 1 ATOM 9841 C CA . ARG E 1 319 ? 5.931 -50.538 17.625 1.00 84.26 ? 318 ARG E CA 1 ATOM 9842 C C . ARG E 1 319 ? 4.898 -51.395 18.342 1.00 85.99 ? 318 ARG E C 1 ATOM 9843 O O . ARG E 1 319 ? 5.050 -52.613 18.432 1.00 87.97 ? 318 ARG E O 1 ATOM 9844 C CB . ARG E 1 319 ? 5.541 -50.446 16.147 1.00 85.20 ? 318 ARG E CB 1 ATOM 9845 C CG . ARG E 1 319 ? 6.323 -49.432 15.333 1.00 84.33 ? 318 ARG E CG 1 ATOM 9846 C CD . ARG E 1 319 ? 5.940 -49.514 13.864 1.00 85.92 ? 318 ARG E CD 1 ATOM 9847 N NE . ARG E 1 319 ? 6.891 -48.813 12.997 1.00 86.03 ? 318 ARG E NE 1 ATOM 9848 C CZ . ARG E 1 319 ? 6.866 -47.511 12.713 1.00 84.15 ? 318 ARG E CZ 1 ATOM 9849 N NH1 . ARG E 1 319 ? 5.931 -46.715 13.221 1.00 82.90 ? 318 ARG E NH1 1 ATOM 9850 N NH2 . ARG E 1 319 ? 7.789 -47.002 11.906 1.00 84.53 ? 318 ARG E NH2 1 ATOM 9851 N N . ASN E 1 320 ? 3.845 -50.754 18.837 1.00 85.35 ? 319 ASN E N 1 ATOM 9852 C CA . ASN E 1 320 ? 2.779 -51.457 19.533 1.00 87.36 ? 319 ASN E CA 1 ATOM 9853 C C . ASN E 1 320 ? 1.414 -50.866 19.213 1.00 87.79 ? 319 ASN E C 1 ATOM 9854 O O . ASN E 1 320 ? 0.426 -51.596 19.140 1.00 90.74 ? 319 ASN E O 1 ATOM 9855 C CB . ASN E 1 320 ? 3.022 -51.421 21.043 1.00 87.08 ? 319 ASN E CB 1 ATOM 9856 C CG . ASN E 1 320 ? 2.170 -52.426 21.794 1.00 90.09 ? 319 ASN E CG 1 ATOM 9857 O OD1 . ASN E 1 320 ? 1.965 -53.556 21.337 1.00 92.02 ? 319 ASN E OD1 1 ATOM 9858 N ND2 . ASN E 1 320 ? 1.674 -52.023 22.960 1.00 90.19 ? 319 ASN E ND2 1 ATOM 9859 N N . ILE F 2 10 ? 3.842 -59.565 7.985 1.00 104.70 ? 10 ILE F N 1 ATOM 9860 C CA . ILE F 2 10 ? 3.307 -59.901 9.339 1.00 101.59 ? 10 ILE F CA 1 ATOM 9861 C C . ILE F 2 10 ? 2.125 -58.995 9.683 1.00 101.47 ? 10 ILE F C 1 ATOM 9862 O O . ILE F 2 10 ? 2.157 -57.793 9.412 1.00 103.09 ? 10 ILE F O 1 ATOM 9863 C CB . ILE F 2 10 ? 4.393 -59.776 10.435 1.00 100.12 ? 10 ILE F CB 1 ATOM 9864 C CG1 . ILE F 2 10 ? 5.631 -60.601 10.051 1.00 100.96 ? 10 ILE F CG1 1 ATOM 9865 C CG2 . ILE F 2 10 ? 3.843 -60.221 11.788 1.00 97.59 ? 10 ILE F CG2 1 ATOM 9866 C CD1 . ILE F 2 10 ? 6.695 -60.698 11.127 1.00 99.77 ? 10 ILE F CD1 1 ATOM 9867 N N . GLU F 2 11 ? 1.087 -59.582 10.278 1.00 99.87 ? 11 GLU F N 1 ATOM 9868 C CA . GLU F 2 11 ? -0.109 -58.838 10.680 1.00 100.08 ? 11 GLU F CA 1 ATOM 9869 C C . GLU F 2 11 ? 0.207 -57.899 11.840 1.00 99.23 ? 11 GLU F C 1 ATOM 9870 O O . GLU F 2 11 ? -0.006 -56.687 11.743 1.00 100.93 ? 11 GLU F O 1 ATOM 9871 C CB . GLU F 2 11 ? -1.233 -59.798 11.077 1.00 98.73 ? 11 GLU F CB 1 ATOM 9872 N N . GLY F 2 12 ? 0.725 -58.464 12.929 1.00 96.85 ? 12 GLY F N 1 ATOM 9873 C CA . GLY F 2 12 ? 1.104 -57.679 14.108 1.00 96.18 ? 12 GLY F CA 1 ATOM 9874 C C . GLY F 2 12 ? 2.021 -58.427 15.060 1.00 94.19 ? 12 GLY F C 1 ATOM 9875 O O . GLY F 2 12 ? 2.619 -59.442 14.693 1.00 93.56 ? 12 GLY F O 1 ATOM 9876 N N . GLY F 2 13 ? 2.134 -57.917 16.286 1.00 93.55 ? 13 GLY F N 1 ATOM 9877 C CA . GLY F 2 13 ? 2.962 -58.541 17.318 1.00 92.25 ? 13 GLY F CA 1 ATOM 9878 C C . GLY F 2 13 ? 2.227 -59.648 18.055 1.00 91.08 ? 13 GLY F C 1 ATOM 9879 O O . GLY F 2 13 ? 1.023 -59.830 17.870 1.00 90.99 ? 13 GLY F O 1 ATOM 9880 N N . TRP F 2 14 ? 2.959 -60.386 18.889 1.00 90.33 ? 14 TRP F N 1 ATOM 9881 C CA . TRP F 2 14 ? 2.380 -61.422 19.745 1.00 89.73 ? 14 TRP F CA 1 ATOM 9882 C C . TRP F 2 14 ? 2.449 -61.041 21.225 1.00 90.53 ? 14 TRP F C 1 ATOM 9883 O O . TRP F 2 14 ? 3.538 -60.850 21.771 1.00 90.83 ? 14 TRP F O 1 ATOM 9884 C CB . TRP F 2 14 ? 3.108 -62.753 19.548 1.00 89.11 ? 14 TRP F CB 1 ATOM 9885 C CG . TRP F 2 14 ? 3.074 -63.280 18.149 1.00 88.83 ? 14 TRP F CG 1 ATOM 9886 C CD1 . TRP F 2 14 ? 2.117 -63.047 17.202 1.00 88.78 ? 14 TRP F CD1 1 ATOM 9887 C CD2 . TRP F 2 14 ? 4.027 -64.161 17.547 1.00 89.10 ? 14 TRP F CD2 1 ATOM 9888 N NE1 . TRP F 2 14 ? 2.426 -63.716 16.042 1.00 89.07 ? 14 TRP F NE1 1 ATOM 9889 C CE2 . TRP F 2 14 ? 3.592 -64.410 16.227 1.00 89.31 ? 14 TRP F CE2 1 ATOM 9890 C CE3 . TRP F 2 14 ? 5.210 -64.761 17.993 1.00 89.77 ? 14 TRP F CE3 1 ATOM 9891 C CZ2 . TRP F 2 14 ? 4.300 -65.233 15.346 1.00 90.21 ? 14 TRP F CZ2 1 ATOM 9892 C CZ3 . TRP F 2 14 ? 5.914 -65.584 17.117 1.00 90.73 ? 14 TRP F CZ3 1 ATOM 9893 C CH2 . TRP F 2 14 ? 5.454 -65.811 15.808 1.00 90.92 ? 14 TRP F CH2 1 ATOM 9894 N N . GLN F 2 15 ? 1.286 -60.945 21.869 1.00 91.32 ? 15 GLN F N 1 ATOM 9895 C CA . GLN F 2 15 ? 1.217 -60.728 23.317 1.00 92.82 ? 15 GLN F CA 1 ATOM 9896 C C . GLN F 2 15 ? 1.644 -61.975 24.088 1.00 93.00 ? 15 GLN F C 1 ATOM 9897 O O . GLN F 2 15 ? 2.131 -61.875 25.216 1.00 94.08 ? 15 GLN F O 1 ATOM 9898 C CB . GLN F 2 15 ? -0.194 -60.307 23.746 1.00 94.03 ? 15 GLN F CB 1 ATOM 9899 C CG . GLN F 2 15 ? -0.556 -58.880 23.361 1.00 95.32 ? 15 GLN F CG 1 ATOM 9900 C CD . GLN F 2 15 ? -1.758 -58.345 24.125 1.00 97.53 ? 15 GLN F CD 1 ATOM 9901 O OE1 . GLN F 2 15 ? -2.572 -59.107 24.646 1.00 98.20 ? 15 GLN F OE1 1 ATOM 9902 N NE2 . GLN F 2 15 ? -1.874 -57.028 24.190 1.00 99.28 ? 15 GLN F NE2 1 ATOM 9903 N N . GLY F 2 16 ? 1.472 -63.143 23.468 1.00 92.40 ? 16 GLY F N 1 ATOM 9904 C CA . GLY F 2 16 ? 1.825 -64.422 24.084 1.00 93.01 ? 16 GLY F CA 1 ATOM 9905 C C . GLY F 2 16 ? 3.312 -64.672 24.296 1.00 93.99 ? 16 GLY F C 1 ATOM 9906 O O . GLY F 2 16 ? 3.689 -65.698 24.877 1.00 94.58 ? 16 GLY F O 1 ATOM 9907 N N . MET F 2 17 ? 4.155 -63.751 23.820 1.00 94.31 ? 17 MET F N 1 ATOM 9908 C CA . MET F 2 17 ? 5.597 -63.813 24.048 1.00 95.75 ? 17 MET F CA 1 ATOM 9909 C C . MET F 2 17 ? 6.065 -62.655 24.927 1.00 97.04 ? 17 MET F C 1 ATOM 9910 O O . MET F 2 17 ? 6.295 -61.548 24.438 1.00 96.72 ? 17 MET F O 1 ATOM 9911 C CB . MET F 2 17 ? 6.349 -63.789 22.715 1.00 95.48 ? 17 MET F CB 1 ATOM 9912 C CG . MET F 2 17 ? 7.851 -64.006 22.852 1.00 97.00 ? 17 MET F CG 1 ATOM 9913 S SD . MET F 2 17 ? 8.685 -64.247 21.270 1.00 97.38 ? 17 MET F SD 1 ATOM 9914 C CE . MET F 2 17 ? 8.296 -62.694 20.460 1.00 96.41 ? 17 MET F CE 1 ATOM 9915 N N . VAL F 2 18 ? 6.205 -62.923 26.223 1.00 98.94 ? 18 VAL F N 1 ATOM 9916 C CA . VAL F 2 18 ? 6.778 -61.967 27.166 1.00 100.72 ? 18 VAL F CA 1 ATOM 9917 C C . VAL F 2 18 ? 8.189 -62.387 27.591 1.00 102.59 ? 18 VAL F C 1 ATOM 9918 O O . VAL F 2 18 ? 8.724 -61.864 28.571 1.00 104.54 ? 18 VAL F O 1 ATOM 9919 C CB . VAL F 2 18 ? 5.896 -61.829 28.421 1.00 102.28 ? 18 VAL F CB 1 ATOM 9920 N N . ASP F 2 19 ? 8.785 -63.322 26.847 1.00 102.55 ? 19 ASP F N 1 ATOM 9921 C CA . ASP F 2 19 ? 10.133 -63.827 27.130 1.00 104.82 ? 19 ASP F CA 1 ATOM 9922 C C . ASP F 2 19 ? 11.219 -62.912 26.567 1.00 104.88 ? 19 ASP F C 1 ATOM 9923 O O . ASP F 2 19 ? 12.274 -62.755 27.179 1.00 106.94 ? 19 ASP F O 1 ATOM 9924 C CB . ASP F 2 19 ? 10.323 -65.231 26.535 1.00 105.38 ? 19 ASP F CB 1 ATOM 9925 C CG . ASP F 2 19 ? 9.422 -66.272 27.175 1.00 106.01 ? 19 ASP F CG 1 ATOM 9926 O OD1 . ASP F 2 19 ? 9.388 -66.358 28.421 1.00 108.20 ? 19 ASP F OD1 1 ATOM 9927 O OD2 . ASP F 2 19 ? 8.760 -67.018 26.424 1.00 105.02 ? 19 ASP F OD2 1 ATOM 9928 N N . GLY F 2 20 ? 10.972 -62.339 25.390 1.00 103.24 ? 20 GLY F N 1 ATOM 9929 C CA . GLY F 2 20 ? 11.926 -61.432 24.743 1.00 103.44 ? 20 GLY F CA 1 ATOM 9930 C C . GLY F 2 20 ? 11.280 -60.555 23.683 1.00 101.81 ? 20 GLY F C 1 ATOM 9931 O O . GLY F 2 20 ? 10.054 -60.533 23.550 1.00 100.58 ? 20 GLY F O 1 ATOM 9932 N N . TRP F 2 21 ? 12.110 -59.834 22.928 1.00 102.25 ? 21 TRP F N 1 ATOM 9933 C CA . TRP F 2 21 ? 11.627 -58.927 21.877 1.00 101.32 ? 21 TRP F CA 1 ATOM 9934 C C . TRP F 2 21 ? 11.328 -59.653 20.557 1.00 100.40 ? 21 TRP F C 1 ATOM 9935 O O . TRP F 2 21 ? 10.349 -59.329 19.883 1.00 99.39 ? 21 TRP F O 1 ATOM 9936 C CB . TRP F 2 21 ? 12.618 -57.775 21.635 1.00 102.56 ? 21 TRP F CB 1 ATOM 9937 C CG . TRP F 2 21 ? 12.555 -56.653 22.660 1.00 103.37 ? 21 TRP F CG 1 ATOM 9938 C CD1 . TRP F 2 21 ? 11.457 -56.240 23.371 1.00 103.15 ? 21 TRP F CD1 1 ATOM 9939 C CD2 . TRP F 2 21 ? 13.628 -55.779 23.045 1.00 104.65 ? 21 TRP F CD2 1 ATOM 9940 N NE1 . TRP F 2 21 ? 11.788 -55.182 24.185 1.00 104.06 ? 21 TRP F NE1 1 ATOM 9941 C CE2 . TRP F 2 21 ? 13.112 -54.877 24.005 1.00 104.91 ? 21 TRP F CE2 1 ATOM 9942 C CE3 . TRP F 2 21 ? 14.978 -55.678 22.680 1.00 105.88 ? 21 TRP F CE3 1 ATOM 9943 C CZ2 . TRP F 2 21 ? 13.898 -53.885 24.605 1.00 106.10 ? 21 TRP F CZ2 1 ATOM 9944 C CZ3 . TRP F 2 21 ? 15.760 -54.690 23.276 1.00 107.09 ? 21 TRP F CZ3 1 ATOM 9945 C CH2 . TRP F 2 21 ? 15.215 -53.807 24.229 1.00 106.98 ? 21 TRP F CH2 1 ATOM 9946 N N . TYR F 2 22 ? 12.172 -60.617 20.188 1.00 100.98 ? 22 TYR F N 1 ATOM 9947 C CA . TYR F 2 22 ? 11.952 -61.426 18.983 1.00 100.60 ? 22 TYR F CA 1 ATOM 9948 C C . TYR F 2 22 ? 11.936 -62.903 19.351 1.00 100.69 ? 22 TYR F C 1 ATOM 9949 O O . TYR F 2 22 ? 12.566 -63.313 20.328 1.00 101.89 ? 22 TYR F O 1 ATOM 9950 C CB . TYR F 2 22 ? 13.041 -61.166 17.936 1.00 102.32 ? 22 TYR F CB 1 ATOM 9951 C CG . TYR F 2 22 ? 13.620 -59.769 17.981 1.00 102.79 ? 22 TYR F CG 1 ATOM 9952 C CD1 . TYR F 2 22 ? 12.883 -58.671 17.542 1.00 101.90 ? 22 TYR F CD1 1 ATOM 9953 C CD2 . TYR F 2 22 ? 14.906 -59.546 18.467 1.00 104.32 ? 22 TYR F CD2 1 ATOM 9954 C CE1 . TYR F 2 22 ? 13.410 -57.390 17.588 1.00 102.41 ? 22 TYR F CE1 1 ATOM 9955 C CE2 . TYR F 2 22 ? 15.443 -58.272 18.515 1.00 104.73 ? 22 TYR F CE2 1 ATOM 9956 C CZ . TYR F 2 22 ? 14.692 -57.195 18.076 1.00 103.72 ? 22 TYR F CZ 1 ATOM 9957 O OH . TYR F 2 22 ? 15.223 -55.925 18.123 1.00 104.13 ? 22 TYR F OH 1 ATOM 9958 N N . GLY F 2 23 ? 11.218 -63.702 18.567 1.00 99.69 ? 23 GLY F N 1 ATOM 9959 C CA . GLY F 2 23 ? 11.161 -65.139 18.804 1.00 99.86 ? 23 GLY F CA 1 ATOM 9960 C C . GLY F 2 23 ? 10.380 -65.936 17.776 1.00 98.97 ? 23 GLY F C 1 ATOM 9961 O O . GLY F 2 23 ? 10.195 -65.501 16.637 1.00 98.75 ? 23 GLY F O 1 ATOM 9962 N N . TYR F 2 24 ? 9.928 -67.115 18.196 1.00 98.52 ? 24 TYR F N 1 ATOM 9963 C CA . TYR F 2 24 ? 9.240 -68.062 17.323 1.00 98.11 ? 24 TYR F CA 1 ATOM 9964 C C . TYR F 2 24 ? 7.983 -68.607 17.998 1.00 96.21 ? 24 TYR F C 1 ATOM 9965 O O . TYR F 2 24 ? 7.912 -68.677 19.225 1.00 96.01 ? 24 TYR F O 1 ATOM 9966 C CB . TYR F 2 24 ? 10.148 -69.255 16.998 1.00 100.63 ? 24 TYR F CB 1 ATOM 9967 C CG . TYR F 2 24 ? 11.561 -68.920 16.562 1.00 103.06 ? 24 TYR F CG 1 ATOM 9968 C CD1 . TYR F 2 24 ? 12.512 -68.496 17.481 1.00 104.06 ? 24 TYR F CD1 1 ATOM 9969 C CD2 . TYR F 2 24 ? 11.956 -69.066 15.238 1.00 104.84 ? 24 TYR F CD2 1 ATOM 9970 C CE1 . TYR F 2 24 ? 13.808 -68.205 17.091 1.00 106.51 ? 24 TYR F CE1 1 ATOM 9971 C CE2 . TYR F 2 24 ? 13.251 -68.776 14.840 1.00 107.53 ? 24 TYR F CE2 1 ATOM 9972 C CZ . TYR F 2 24 ? 14.172 -68.346 15.772 1.00 108.26 ? 24 TYR F CZ 1 ATOM 9973 O OH . TYR F 2 24 ? 15.459 -68.056 15.391 1.00 111.14 ? 24 TYR F OH 1 ATOM 9974 N N . HIS F 2 25 ? 6.996 -68.987 17.192 1.00 95.09 ? 25 HIS F N 1 ATOM 9975 C CA . HIS F 2 25 ? 5.863 -69.775 17.674 1.00 93.90 ? 25 HIS F CA 1 ATOM 9976 C C . HIS F 2 25 ? 5.757 -71.051 16.847 1.00 94.75 ? 25 HIS F C 1 ATOM 9977 O O . HIS F 2 25 ? 5.470 -70.997 15.651 1.00 94.77 ? 25 HIS F O 1 ATOM 9978 C CB . HIS F 2 25 ? 4.554 -68.986 17.594 1.00 92.01 ? 25 HIS F CB 1 ATOM 9979 C CG . HIS F 2 25 ? 3.346 -69.791 17.969 1.00 91.02 ? 25 HIS F CG 1 ATOM 9980 N ND1 . HIS F 2 25 ? 2.913 -69.923 19.272 1.00 90.65 ? 25 HIS F ND1 1 ATOM 9981 C CD2 . HIS F 2 25 ? 2.488 -70.517 17.213 1.00 90.57 ? 25 HIS F CD2 1 ATOM 9982 C CE1 . HIS F 2 25 ? 1.835 -70.687 19.300 1.00 90.01 ? 25 HIS F CE1 1 ATOM 9983 N NE2 . HIS F 2 25 ? 1.559 -71.063 18.064 1.00 89.85 ? 25 HIS F NE2 1 ATOM 9984 N N . HIS F 2 26 ? 5.988 -72.194 17.488 1.00 95.73 ? 26 HIS F N 1 ATOM 9985 C CA . HIS F 2 26 ? 5.938 -73.482 16.799 1.00 97.06 ? 26 HIS F CA 1 ATOM 9986 C C . HIS F 2 26 ? 4.623 -74.217 17.061 1.00 95.43 ? 26 HIS F C 1 ATOM 9987 O O . HIS F 2 26 ? 4.039 -74.098 18.136 1.00 94.35 ? 26 HIS F O 1 ATOM 9988 C CB . HIS F 2 26 ? 7.137 -74.356 17.190 1.00 100.09 ? 26 HIS F CB 1 ATOM 9989 C CG . HIS F 2 26 ? 7.115 -74.830 18.610 1.00 100.60 ? 26 HIS F CG 1 ATOM 9990 N ND1 . HIS F 2 26 ? 6.596 -76.053 18.978 1.00 101.35 ? 26 HIS F ND1 1 ATOM 9991 C CD2 . HIS F 2 26 ? 7.557 -74.251 19.751 1.00 100.92 ? 26 HIS F CD2 1 ATOM 9992 C CE1 . HIS F 2 26 ? 6.712 -76.203 20.285 1.00 102.12 ? 26 HIS F CE1 1 ATOM 9993 N NE2 . HIS F 2 26 ? 7.292 -75.124 20.778 1.00 101.91 ? 26 HIS F NE2 1 ATOM 9994 N N . SER F 2 27 ? 4.161 -74.954 16.052 1.00 95.60 ? 27 SER F N 1 ATOM 9995 C CA . SER F 2 27 ? 2.986 -75.815 16.166 1.00 94.48 ? 27 SER F CA 1 ATOM 9996 C C . SER F 2 27 ? 3.415 -77.240 15.855 1.00 96.64 ? 27 SER F C 1 ATOM 9997 O O . SER F 2 27 ? 4.042 -77.497 14.821 1.00 98.58 ? 27 SER F O 1 ATOM 9998 C CB . SER F 2 27 ? 1.888 -75.375 15.200 1.00 92.96 ? 27 SER F CB 1 ATOM 9999 O OG . SER F 2 27 ? 0.856 -76.347 15.126 1.00 92.40 ? 27 SER F OG 1 ATOM 10000 N N . ASN F 2 28 ? 3.062 -78.167 16.740 1.00 96.69 ? 28 ASN F N 1 ATOM 10001 C CA . ASN F 2 28 ? 3.648 -79.502 16.718 1.00 99.17 ? 28 ASN F CA 1 ATOM 10002 C C . ASN F 2 28 ? 2.678 -80.580 17.159 1.00 98.80 ? 28 ASN F C 1 ATOM 10003 O O . ASN F 2 28 ? 1.775 -80.329 17.956 1.00 96.78 ? 28 ASN F O 1 ATOM 10004 C CB . ASN F 2 28 ? 4.854 -79.518 17.660 1.00 101.27 ? 28 ASN F CB 1 ATOM 10005 C CG . ASN F 2 28 ? 6.062 -80.181 17.061 1.00 104.68 ? 28 ASN F CG 1 ATOM 10006 O OD1 . ASN F 2 28 ? 6.117 -80.443 15.864 1.00 105.45 ? 28 ASN F OD1 1 ATOM 10007 N ND2 . ASN F 2 28 ? 7.054 -80.438 17.896 1.00 107.30 ? 28 ASN F ND2 1 ATOM 10008 N N . GLU F 2 29 ? 2.886 -81.789 16.647 1.00 101.24 ? 29 GLU F N 1 ATOM 10009 C CA . GLU F 2 29 ? 2.123 -82.960 17.082 1.00 101.53 ? 29 GLU F CA 1 ATOM 10010 C C . GLU F 2 29 ? 2.177 -83.134 18.607 1.00 102.10 ? 29 GLU F C 1 ATOM 10011 O O . GLU F 2 29 ? 1.186 -83.521 19.229 1.00 100.89 ? 29 GLU F O 1 ATOM 10012 C CB . GLU F 2 29 ? 2.604 -84.233 16.358 1.00 104.80 ? 29 GLU F CB 1 ATOM 10013 C CG . GLU F 2 29 ? 4.039 -84.689 16.642 1.00 108.90 ? 29 GLU F CG 1 ATOM 10014 C CD . GLU F 2 29 ? 5.109 -83.926 15.868 1.00 110.16 ? 29 GLU F CD 1 ATOM 10015 O OE1 . GLU F 2 29 ? 4.844 -83.472 14.733 1.00 109.05 ? 29 GLU F OE1 1 ATOM 10016 O OE2 . GLU F 2 29 ? 6.233 -83.794 16.395 1.00 112.53 ? 29 GLU F OE2 1 ATOM 10017 N N . GLN F 2 30 ? 3.330 -82.822 19.196 1.00 104.21 ? 30 GLN F N 1 ATOM 10018 C CA . GLN F 2 30 ? 3.516 -82.860 20.646 1.00 105.45 ? 30 GLN F CA 1 ATOM 10019 C C . GLN F 2 30 ? 2.770 -81.710 21.331 1.00 102.66 ? 30 GLN F C 1 ATOM 10020 O O . GLN F 2 30 ? 1.882 -81.943 22.154 1.00 102.22 ? 30 GLN F O 1 ATOM 10021 C CB . GLN F 2 30 ? 5.011 -82.798 20.985 1.00 108.76 ? 30 GLN F CB 1 ATOM 10022 C CG . GLN F 2 30 ? 5.793 -84.037 20.554 1.00 112.75 ? 30 GLN F CG 1 ATOM 10023 C CD . GLN F 2 30 ? 7.215 -83.720 20.122 1.00 115.42 ? 30 GLN F CD 1 ATOM 10024 O OE1 . GLN F 2 30 ? 7.431 -83.046 19.114 1.00 114.10 ? 30 GLN F OE1 1 ATOM 10025 N NE2 . GLN F 2 30 ? 8.194 -84.214 20.877 1.00 119.53 ? 30 GLN F NE2 1 ATOM 10026 N N . GLY F 2 31 ? 3.131 -80.476 20.989 1.00 101.23 ? 31 GLY F N 1 ATOM 10027 C CA . GLY F 2 31 ? 2.491 -79.296 21.569 1.00 98.92 ? 31 GLY F CA 1 ATOM 10028 C C . GLY F 2 31 ? 2.698 -78.037 20.750 1.00 97.05 ? 31 GLY F C 1 ATOM 10029 O O . GLY F 2 31 ? 3.054 -78.096 19.575 1.00 97.01 ? 31 GLY F O 1 ATOM 10030 N N . SER F 2 32 ? 2.463 -76.891 21.377 1.00 95.90 ? 32 SER F N 1 ATOM 10031 C CA . SER F 2 32 ? 2.665 -75.601 20.717 1.00 94.59 ? 32 SER F CA 1 ATOM 10032 C C . SER F 2 32 ? 2.802 -74.471 21.736 1.00 94.24 ? 32 SER F C 1 ATOM 10033 O O . SER F 2 32 ? 2.067 -74.417 22.720 1.00 93.78 ? 32 SER F O 1 ATOM 10034 C CB . SER F 2 32 ? 1.517 -75.308 19.742 1.00 92.55 ? 32 SER F CB 1 ATOM 10035 O OG . SER F 2 32 ? 0.266 -75.293 20.403 1.00 91.60 ? 32 SER F OG 1 ATOM 10036 N N . GLY F 2 33 ? 3.752 -73.576 21.488 1.00 94.63 ? 33 GLY F N 1 ATOM 10037 C CA . GLY F 2 33 ? 4.058 -72.493 22.415 1.00 94.98 ? 33 GLY F CA 1 ATOM 10038 C C . GLY F 2 33 ? 5.164 -71.607 21.882 1.00 95.47 ? 33 GLY F C 1 ATOM 10039 O O . GLY F 2 33 ? 5.765 -71.907 20.847 1.00 95.99 ? 33 GLY F O 1 ATOM 10040 N N . TYR F 2 34 ? 5.438 -70.521 22.600 1.00 95.64 ? 34 TYR F N 1 ATOM 10041 C CA . TYR F 2 34 ? 6.396 -69.513 22.150 1.00 95.94 ? 34 TYR F CA 1 ATOM 10042 C C . TYR F 2 34 ? 7.813 -69.792 22.631 1.00 98.36 ? 34 TYR F C 1 ATOM 10043 O O . TYR F 2 34 ? 8.037 -70.609 23.523 1.00 99.97 ? 34 TYR F O 1 ATOM 10044 C CB . TYR F 2 34 ? 5.964 -68.125 22.623 1.00 95.03 ? 34 TYR F CB 1 ATOM 10045 C CG . TYR F 2 34 ? 4.629 -67.692 22.072 1.00 93.34 ? 34 TYR F CG 1 ATOM 10046 C CD1 . TYR F 2 34 ? 3.448 -68.005 22.735 1.00 93.03 ? 34 TYR F CD1 1 ATOM 10047 C CD2 . TYR F 2 34 ? 4.546 -66.972 20.885 1.00 92.58 ? 34 TYR F CD2 1 ATOM 10048 C CE1 . TYR F 2 34 ? 2.219 -67.610 22.233 1.00 91.89 ? 34 TYR F CE1 1 ATOM 10049 C CE2 . TYR F 2 34 ? 3.323 -66.570 20.376 1.00 91.53 ? 34 TYR F CE2 1 ATOM 10050 C CZ . TYR F 2 34 ? 2.164 -66.891 21.052 1.00 91.18 ? 34 TYR F CZ 1 ATOM 10051 O OH . TYR F 2 34 ? 0.952 -66.491 20.540 1.00 90.58 ? 34 TYR F OH 1 ATOM 10052 N N . ALA F 2 35 ? 8.764 -69.093 22.022 1.00 99.01 ? 35 ALA F N 1 ATOM 10053 C CA . ALA F 2 35 ? 10.171 -69.189 22.392 1.00 101.68 ? 35 ALA F CA 1 ATOM 10054 C C . ALA F 2 35 ? 10.920 -67.964 21.867 1.00 101.61 ? 35 ALA F C 1 ATOM 10055 O O . ALA F 2 35 ? 10.928 -67.706 20.666 1.00 100.91 ? 35 ALA F O 1 ATOM 10056 C CB . ALA F 2 35 ? 10.776 -70.466 21.832 1.00 103.76 ? 35 ALA F CB 1 ATOM 10057 N N . ALA F 2 36 ? 11.538 -67.207 22.769 1.00 102.72 ? 36 ALA F N 1 ATOM 10058 C CA . ALA F 2 36 ? 12.274 -66.005 22.380 1.00 102.86 ? 36 ALA F CA 1 ATOM 10059 C C . ALA F 2 36 ? 13.654 -66.373 21.843 1.00 105.58 ? 36 ALA F C 1 ATOM 10060 O O . ALA F 2 36 ? 14.269 -67.339 22.299 1.00 107.94 ? 36 ALA F O 1 ATOM 10061 C CB . ALA F 2 36 ? 12.396 -65.046 23.557 1.00 102.94 ? 36 ALA F CB 1 ATOM 10062 N N . ASP F 2 37 ? 14.123 -65.605 20.863 1.00 105.78 ? 37 ASP F N 1 ATOM 10063 C CA . ASP F 2 37 ? 15.473 -65.753 20.332 1.00 108.81 ? 37 ASP F CA 1 ATOM 10064 C C . ASP F 2 37 ? 16.415 -64.889 21.173 1.00 110.08 ? 37 ASP F C 1 ATOM 10065 O O . ASP F 2 37 ? 16.344 -63.660 21.127 1.00 108.50 ? 37 ASP F O 1 ATOM 10066 C CB . ASP F 2 37 ? 15.515 -65.330 18.858 1.00 108.71 ? 37 ASP F CB 1 ATOM 10067 C CG . ASP F 2 37 ? 16.835 -65.673 18.175 1.00 112.20 ? 37 ASP F CG 1 ATOM 10068 O OD1 . ASP F 2 37 ? 17.660 -66.411 18.758 1.00 114.98 ? 37 ASP F OD1 1 ATOM 10069 O OD2 . ASP F 2 37 ? 17.045 -65.200 17.038 1.00 112.80 ? 37 ASP F OD2 1 ATOM 10070 N N . LYS F 2 38 ? 17.288 -65.541 21.939 1.00 113.26 ? 38 LYS F N 1 ATOM 10071 C CA . LYS F 2 38 ? 18.183 -64.848 22.873 1.00 115.03 ? 38 LYS F CA 1 ATOM 10072 C C . LYS F 2 38 ? 19.400 -64.209 22.191 1.00 117.00 ? 38 LYS F C 1 ATOM 10073 O O . LYS F 2 38 ? 19.856 -63.148 22.617 1.00 116.58 ? 38 LYS F O 1 ATOM 10074 C CB . LYS F 2 38 ? 18.645 -65.808 23.975 1.00 117.93 ? 38 LYS F CB 1 ATOM 10075 C CG . LYS F 2 38 ? 17.516 -66.312 24.862 1.00 116.64 ? 38 LYS F CG 1 ATOM 10076 N N . GLU F 2 39 ? 19.924 -64.854 21.148 1.00 119.37 ? 39 GLU F N 1 ATOM 10077 C CA . GLU F 2 39 ? 21.062 -64.311 20.393 1.00 121.73 ? 39 GLU F CA 1 ATOM 10078 C C . GLU F 2 39 ? 20.693 -63.012 19.665 1.00 119.44 ? 39 GLU F C 1 ATOM 10079 O O . GLU F 2 39 ? 21.499 -62.078 19.593 1.00 120.26 ? 39 GLU F O 1 ATOM 10080 C CB . GLU F 2 39 ? 21.582 -65.341 19.386 1.00 124.74 ? 39 GLU F CB 1 ATOM 10081 N N . SER F 2 40 ? 19.472 -62.967 19.132 1.00 116.94 ? 40 SER F N 1 ATOM 10082 C CA . SER F 2 40 ? 18.951 -61.792 18.423 1.00 115.05 ? 40 SER F CA 1 ATOM 10083 C C . SER F 2 40 ? 18.484 -60.690 19.387 1.00 112.85 ? 40 SER F C 1 ATOM 10084 O O . SER F 2 40 ? 18.638 -59.498 19.099 1.00 112.26 ? 40 SER F O 1 ATOM 10085 C CB . SER F 2 40 ? 17.804 -62.215 17.494 1.00 113.63 ? 40 SER F CB 1 ATOM 10086 O OG . SER F 2 40 ? 17.180 -61.108 16.873 1.00 112.04 ? 40 SER F OG 1 ATOM 10087 N N . THR F 2 41 ? 17.909 -61.092 20.521 1.00 111.94 ? 41 THR F N 1 ATOM 10088 C CA . THR F 2 41 ? 17.499 -60.150 21.567 1.00 110.55 ? 41 THR F CA 1 ATOM 10089 C C . THR F 2 41 ? 18.721 -59.507 22.231 1.00 112.50 ? 41 THR F C 1 ATOM 10090 O O . THR F 2 41 ? 18.716 -58.307 22.518 1.00 111.66 ? 41 THR F O 1 ATOM 10091 C CB . THR F 2 41 ? 16.627 -60.842 22.639 1.00 109.78 ? 41 THR F CB 1 ATOM 10092 O OG1 . THR F 2 41 ? 15.427 -61.343 22.037 1.00 107.86 ? 41 THR F OG1 1 ATOM 10093 C CG2 . THR F 2 41 ? 16.252 -59.872 23.757 1.00 109.00 ? 41 THR F CG2 1 ATOM 10094 N N . GLN F 2 42 ? 19.758 -60.311 22.472 1.00 115.35 ? 42 GLN F N 1 ATOM 10095 C CA . GLN F 2 42 ? 21.018 -59.816 23.029 1.00 117.73 ? 42 GLN F CA 1 ATOM 10096 C C . GLN F 2 42 ? 21.597 -58.695 22.170 1.00 117.85 ? 42 GLN F C 1 ATOM 10097 O O . GLN F 2 42 ? 21.999 -57.655 22.687 1.00 117.85 ? 42 GLN F O 1 ATOM 10098 C CB . GLN F 2 42 ? 22.040 -60.949 23.147 1.00 121.18 ? 42 GLN F CB 1 ATOM 10099 N N . LYS F 2 43 ? 21.619 -58.914 20.857 1.00 118.37 ? 43 LYS F N 1 ATOM 10100 C CA . LYS F 2 43 ? 22.143 -57.935 19.898 1.00 118.91 ? 43 LYS F CA 1 ATOM 10101 C C . LYS F 2 43 ? 21.350 -56.619 19.884 1.00 116.23 ? 43 LYS F C 1 ATOM 10102 O O . LYS F 2 43 ? 21.912 -55.554 19.617 1.00 116.51 ? 43 LYS F O 1 ATOM 10103 C CB . LYS F 2 43 ? 22.165 -58.545 18.488 1.00 120.18 ? 43 LYS F CB 1 ATOM 10104 C CG . LYS F 2 43 ? 22.858 -57.690 17.437 1.00 121.65 ? 43 LYS F CG 1 ATOM 10105 N N . ALA F 2 44 ? 20.052 -56.701 20.173 1.00 113.89 ? 44 ALA F N 1 ATOM 10106 C CA . ALA F 2 44 ? 19.174 -55.527 20.172 1.00 112.00 ? 44 ALA F CA 1 ATOM 10107 C C . ALA F 2 44 ? 19.265 -54.710 21.466 1.00 111.67 ? 44 ALA F C 1 ATOM 10108 O O . ALA F 2 44 ? 19.234 -53.480 21.425 1.00 110.89 ? 44 ALA F O 1 ATOM 10109 C CB . ALA F 2 44 ? 17.735 -55.950 19.917 1.00 110.05 ? 44 ALA F CB 1 ATOM 10110 N N . ILE F 2 45 ? 19.360 -55.395 22.606 1.00 112.38 ? 45 ILE F N 1 ATOM 10111 C CA . ILE F 2 45 ? 19.513 -54.731 23.907 1.00 112.81 ? 45 ILE F CA 1 ATOM 10112 C C . ILE F 2 45 ? 20.857 -53.997 23.973 1.00 114.79 ? 45 ILE F C 1 ATOM 10113 O O . ILE F 2 45 ? 20.957 -52.924 24.573 1.00 114.67 ? 45 ILE F O 1 ATOM 10114 C CB . ILE F 2 45 ? 19.393 -55.734 25.084 1.00 113.67 ? 45 ILE F CB 1 ATOM 10115 C CG1 . ILE F 2 45 ? 17.966 -56.292 25.164 1.00 111.81 ? 45 ILE F CG1 1 ATOM 10116 C CG2 . ILE F 2 45 ? 19.771 -55.076 26.410 1.00 114.86 ? 45 ILE F CG2 1 ATOM 10117 C CD1 . ILE F 2 45 ? 17.818 -57.495 26.070 1.00 112.94 ? 45 ILE F CD1 1 ATOM 10118 N N . ASP F 2 46 ? 21.881 -54.580 23.351 1.00 116.75 ? 46 ASP F N 1 ATOM 10119 C CA . ASP F 2 46 ? 23.208 -53.962 23.280 1.00 118.71 ? 46 ASP F CA 1 ATOM 10120 C C . ASP F 2 46 ? 23.201 -52.751 22.347 1.00 117.83 ? 46 ASP F C 1 ATOM 10121 O O . ASP F 2 46 ? 23.757 -51.706 22.683 1.00 118.37 ? 46 ASP F O 1 ATOM 10122 C CB . ASP F 2 46 ? 24.257 -54.974 22.801 1.00 121.44 ? 46 ASP F CB 1 ATOM 10123 C CG . ASP F 2 46 ? 24.391 -56.178 23.728 1.00 123.01 ? 46 ASP F CG 1 ATOM 10124 O OD1 . ASP F 2 46 ? 23.698 -56.231 24.768 1.00 122.03 ? 46 ASP F OD1 1 ATOM 10125 O OD2 . ASP F 2 46 ? 25.188 -57.083 23.403 1.00 125.55 ? 46 ASP F OD2 1 ATOM 10126 N N . GLY F 2 47 ? 22.570 -52.899 21.182 1.00 116.80 ? 47 GLY F N 1 ATOM 10127 C CA . GLY F 2 47 ? 22.473 -51.818 20.194 1.00 116.43 ? 47 GLY F CA 1 ATOM 10128 C C . GLY F 2 47 ? 21.612 -50.637 20.621 1.00 114.71 ? 47 GLY F C 1 ATOM 10129 O O . GLY F 2 47 ? 21.837 -49.508 20.178 1.00 114.89 ? 47 GLY F O 1 ATOM 10130 N N . VAL F 2 48 ? 20.619 -50.901 21.469 1.00 113.29 ? 48 VAL F N 1 ATOM 10131 C CA . VAL F 2 48 ? 19.773 -49.850 22.041 1.00 112.30 ? 48 VAL F CA 1 ATOM 10132 C C . VAL F 2 48 ? 20.477 -49.182 23.223 1.00 113.25 ? 48 VAL F C 1 ATOM 10133 O O . VAL F 2 48 ? 20.500 -47.954 23.319 1.00 113.29 ? 48 VAL F O 1 ATOM 10134 C CB . VAL F 2 48 ? 18.400 -50.408 22.487 1.00 110.91 ? 48 VAL F CB 1 ATOM 10135 C CG1 . VAL F 2 48 ? 17.645 -49.409 23.360 1.00 110.65 ? 48 VAL F CG1 1 ATOM 10136 C CG2 . VAL F 2 48 ? 17.563 -50.779 21.270 1.00 110.05 ? 48 VAL F CG2 1 ATOM 10137 N N . THR F 2 49 ? 21.045 -49.991 24.117 1.00 114.32 ? 49 THR F N 1 ATOM 10138 C CA . THR F 2 49 ? 21.772 -49.474 25.282 1.00 115.87 ? 49 THR F CA 1 ATOM 10139 C C . THR F 2 49 ? 23.027 -48.688 24.869 1.00 117.19 ? 49 THR F C 1 ATOM 10140 O O . THR F 2 49 ? 23.424 -47.750 25.558 1.00 117.78 ? 49 THR F O 1 ATOM 10141 C CB . THR F 2 49 ? 22.152 -50.606 26.263 1.00 117.25 ? 49 THR F CB 1 ATOM 10142 O OG1 . THR F 2 49 ? 20.988 -51.387 26.569 1.00 116.15 ? 49 THR F OG1 1 ATOM 10143 C CG2 . THR F 2 49 ? 22.735 -50.038 27.561 1.00 118.92 ? 49 THR F CG2 1 ATOM 10144 N N . ASN F 2 50 ? 23.642 -49.074 23.749 1.00 117.86 ? 50 ASN F N 1 ATOM 10145 C CA . ASN F 2 50 ? 24.746 -48.307 23.156 1.00 119.30 ? 50 ASN F CA 1 ATOM 10146 C C . ASN F 2 50 ? 24.278 -46.946 22.633 1.00 118.62 ? 50 ASN F C 1 ATOM 10147 O O . ASN F 2 50 ? 25.002 -45.956 22.723 1.00 119.57 ? 50 ASN F O 1 ATOM 10148 C CB . ASN F 2 50 ? 25.406 -49.083 22.003 1.00 120.57 ? 50 ASN F CB 1 ATOM 10149 C CG . ASN F 2 50 ? 26.375 -50.158 22.480 1.00 122.76 ? 50 ASN F CG 1 ATOM 10150 O OD1 . ASN F 2 50 ? 27.343 -50.479 21.789 1.00 124.91 ? 50 ASN F OD1 1 ATOM 10151 N ND2 . ASN F 2 50 ? 26.116 -50.725 23.653 1.00 122.72 ? 50 ASN F ND2 1 ATOM 10152 N N . LYS F 2 51 ? 23.064 -46.913 22.086 1.00 117.35 ? 51 LYS F N 1 ATOM 10153 C CA . LYS F 2 51 ? 22.494 -45.705 21.486 1.00 117.16 ? 51 LYS F CA 1 ATOM 10154 C C . LYS F 2 51 ? 22.087 -44.678 22.545 1.00 117.06 ? 51 LYS F C 1 ATOM 10155 O O . LYS F 2 51 ? 22.480 -43.514 22.473 1.00 117.71 ? 51 LYS F O 1 ATOM 10156 C CB . LYS F 2 51 ? 21.276 -46.077 20.630 1.00 116.04 ? 51 LYS F CB 1 ATOM 10157 C CG . LYS F 2 51 ? 20.830 -45.003 19.654 1.00 116.48 ? 51 LYS F CG 1 ATOM 10158 C CD . LYS F 2 51 ? 19.540 -45.409 18.958 1.00 115.59 ? 51 LYS F CD 1 ATOM 10159 C CE . LYS F 2 51 ? 19.391 -44.731 17.606 1.00 117.04 ? 51 LYS F CE 1 ATOM 10160 N NZ . LYS F 2 51 ? 20.136 -45.448 16.534 1.00 118.23 ? 51 LYS F NZ 1 ATOM 10161 N N . VAL F 2 52 ? 21.292 -45.123 23.517 1.00 116.64 ? 52 VAL F N 1 ATOM 10162 C CA . VAL F 2 52 ? 20.791 -44.250 24.585 1.00 117.17 ? 52 VAL F CA 1 ATOM 10163 C C . VAL F 2 52 ? 21.927 -43.610 25.390 1.00 118.92 ? 52 VAL F C 1 ATOM 10164 O O . VAL F 2 52 ? 21.854 -42.429 25.741 1.00 119.74 ? 52 VAL F O 1 ATOM 10165 C CB . VAL F 2 52 ? 19.803 -44.995 25.529 1.00 116.57 ? 52 VAL F CB 1 ATOM 10166 C CG1 . VAL F 2 52 ? 20.485 -46.133 26.283 1.00 117.03 ? 52 VAL F CG1 1 ATOM 10167 C CG2 . VAL F 2 52 ? 19.150 -44.024 26.505 1.00 117.42 ? 52 VAL F CG2 1 ATOM 10168 N N . ASN F 2 53 ? 22.976 -44.385 25.662 1.00 119.99 ? 53 ASN F N 1 ATOM 10169 C CA . ASN F 2 53 ? 24.146 -43.882 26.386 1.00 121.87 ? 53 ASN F CA 1 ATOM 10170 C C . ASN F 2 53 ? 24.952 -42.907 25.527 1.00 122.36 ? 53 ASN F C 1 ATOM 10171 O O . ASN F 2 53 ? 25.474 -41.912 26.032 1.00 123.36 ? 53 ASN F O 1 ATOM 10172 C CB . ASN F 2 53 ? 25.047 -45.039 26.843 1.00 123.36 ? 53 ASN F CB 1 ATOM 10173 C CG . ASN F 2 53 ? 24.336 -46.016 27.773 1.00 123.44 ? 53 ASN F CG 1 ATOM 10174 O OD1 . ASN F 2 53 ? 23.222 -45.763 28.236 1.00 122.82 ? 53 ASN F OD1 1 ATOM 10175 N ND2 . ASN F 2 53 ? 24.983 -47.148 28.043 1.00 124.66 ? 53 ASN F ND2 1 ATOM 10176 N N . SER F 2 54 ? 25.040 -43.204 24.230 1.00 121.94 ? 54 SER F N 1 ATOM 10177 C CA . SER F 2 54 ? 25.763 -42.365 23.267 1.00 122.82 ? 54 SER F CA 1 ATOM 10178 C C . SER F 2 54 ? 25.087 -41.005 23.054 1.00 122.52 ? 54 SER F C 1 ATOM 10179 O O . SER F 2 54 ? 25.758 -40.006 22.789 1.00 123.63 ? 54 SER F O 1 ATOM 10180 C CB . SER F 2 54 ? 25.902 -43.103 21.928 1.00 122.97 ? 54 SER F CB 1 ATOM 10181 O OG . SER F 2 54 ? 26.589 -42.320 20.970 1.00 124.46 ? 54 SER F OG 1 ATOM 10182 N N . ILE F 2 55 ? 23.761 -40.978 23.166 1.00 121.29 ? 55 ILE F N 1 ATOM 10183 C CA . ILE F 2 55 ? 22.995 -39.734 23.097 1.00 121.53 ? 55 ILE F CA 1 ATOM 10184 C C . ILE F 2 55 ? 23.262 -38.859 24.326 1.00 122.50 ? 55 ILE F C 1 ATOM 10185 O O . ILE F 2 55 ? 23.380 -37.640 24.207 1.00 123.61 ? 55 ILE F O 1 ATOM 10186 C CB . ILE F 2 55 ? 21.483 -40.026 22.967 1.00 120.52 ? 55 ILE F CB 1 ATOM 10187 C CG1 . ILE F 2 55 ? 21.192 -40.641 21.593 1.00 120.06 ? 55 ILE F CG1 1 ATOM 10188 C CG2 . ILE F 2 55 ? 20.655 -38.759 23.161 1.00 121.52 ? 55 ILE F CG2 1 ATOM 10189 C CD1 . ILE F 2 55 ? 19.904 -41.433 21.528 1.00 118.83 ? 55 ILE F CD1 1 ATOM 10190 N N . ILE F 2 56 ? 23.362 -39.488 25.495 1.00 122.42 ? 56 ILE F N 1 ATOM 10191 C CA . ILE F 2 56 ? 23.621 -38.775 26.751 1.00 123.66 ? 56 ILE F CA 1 ATOM 10192 C C . ILE F 2 56 ? 25.043 -38.197 26.789 1.00 125.07 ? 56 ILE F C 1 ATOM 10193 O O . ILE F 2 56 ? 25.243 -37.051 27.206 1.00 126.33 ? 56 ILE F O 1 ATOM 10194 C CB . ILE F 2 56 ? 23.405 -39.697 27.977 1.00 123.63 ? 56 ILE F CB 1 ATOM 10195 C CG1 . ILE F 2 56 ? 21.945 -40.164 28.051 1.00 122.57 ? 56 ILE F CG1 1 ATOM 10196 C CG2 . ILE F 2 56 ? 23.788 -38.982 29.271 1.00 125.51 ? 56 ILE F CG2 1 ATOM 10197 C CD1 . ILE F 2 56 ? 21.744 -41.439 28.842 1.00 122.28 ? 56 ILE F CD1 1 ATOM 10198 N N . ASP F 2 57 ? 26.018 -38.992 26.353 1.00 125.19 ? 57 ASP F N 1 ATOM 10199 C CA . ASP F 2 57 ? 27.429 -38.603 26.409 1.00 126.80 ? 57 ASP F CA 1 ATOM 10200 C C . ASP F 2 57 ? 27.779 -37.497 25.418 1.00 127.59 ? 57 ASP F C 1 ATOM 10201 O O . ASP F 2 57 ? 28.638 -36.663 25.702 1.00 128.65 ? 57 ASP F O 1 ATOM 10202 C CB . ASP F 2 57 ? 28.332 -39.817 26.162 1.00 127.15 ? 57 ASP F CB 1 ATOM 10203 C CG . ASP F 2 57 ? 28.216 -40.866 27.255 1.00 127.52 ? 57 ASP F CG 1 ATOM 10204 O OD1 . ASP F 2 57 ? 28.169 -40.488 28.445 1.00 128.45 ? 57 ASP F OD1 1 ATOM 10205 O OD2 . ASP F 2 57 ? 28.177 -42.071 26.926 1.00 127.07 ? 57 ASP F OD2 1 ATOM 10206 N N . LYS F 2 58 ? 27.118 -37.491 24.262 1.00 98.33 ? 58 LYS F N 1 ATOM 10207 C CA . LYS F 2 58 ? 27.359 -36.465 23.242 1.00 96.46 ? 58 LYS F CA 1 ATOM 10208 C C . LYS F 2 58 ? 26.777 -35.123 23.669 1.00 90.81 ? 58 LYS F C 1 ATOM 10209 O O . LYS F 2 58 ? 27.244 -34.067 23.229 1.00 88.67 ? 58 LYS F O 1 ATOM 10210 C CB . LYS F 2 58 ? 26.747 -36.868 21.895 1.00 98.89 ? 58 LYS F CB 1 ATOM 10211 C CG . LYS F 2 58 ? 27.373 -36.172 20.689 1.00 99.27 ? 58 LYS F CG 1 ATOM 10212 C CD . LYS F 2 58 ? 28.327 -37.079 19.919 1.00 106.21 ? 58 LYS F CD 1 ATOM 10213 C CE . LYS F 2 58 ? 29.519 -37.528 20.751 1.00 108.80 ? 58 LYS F CE 1 ATOM 10214 N NZ . LYS F 2 58 ? 30.390 -38.473 19.998 1.00 116.22 ? 58 LYS F NZ 1 ATOM 10215 N N . MET F 2 59 ? 25.754 -35.173 24.522 1.00 89.49 ? 59 MET F N 1 ATOM 10216 C CA . MET F 2 59 ? 25.043 -33.971 24.961 1.00 84.36 ? 59 MET F CA 1 ATOM 10217 C C . MET F 2 59 ? 25.589 -33.371 26.258 1.00 81.51 ? 59 MET F C 1 ATOM 10218 O O . MET F 2 59 ? 25.194 -32.269 26.636 1.00 77.86 ? 59 MET F O 1 ATOM 10219 C CB . MET F 2 59 ? 23.548 -34.276 25.110 1.00 85.03 ? 59 MET F CB 1 ATOM 10220 C CG . MET F 2 59 ? 22.859 -34.595 23.790 1.00 87.53 ? 59 MET F CG 1 ATOM 10221 S SD . MET F 2 59 ? 22.733 -33.190 22.663 1.00 85.58 ? 59 MET F SD 1 ATOM 10222 C CE . MET F 2 59 ? 21.749 -32.037 23.611 1.00 80.52 ? 59 MET F CE 1 ATOM 10223 N N . ASN F 2 60 ? 26.509 -34.064 26.927 1.00 83.65 ? 60 ASN F N 1 ATOM 10224 C CA . ASN F 2 60 ? 27.081 -33.543 28.171 1.00 82.46 ? 60 ASN F CA 1 ATOM 10225 C C . ASN F 2 60 ? 28.127 -32.433 27.968 1.00 79.78 ? 60 ASN F C 1 ATOM 10226 O O . ASN F 2 60 ? 28.688 -31.933 28.942 1.00 79.18 ? 60 ASN F O 1 ATOM 10227 C CB . ASN F 2 60 ? 27.642 -34.683 29.038 1.00 87.75 ? 60 ASN F CB 1 ATOM 10228 C CG . ASN F 2 60 ? 28.969 -35.217 28.542 1.00 92.01 ? 60 ASN F CG 1 ATOM 10229 O OD1 . ASN F 2 60 ? 29.576 -34.675 27.620 1.00 91.03 ? 60 ASN F OD1 1 ATOM 10230 N ND2 . ASN F 2 60 ? 29.427 -36.296 29.163 1.00 97.74 ? 60 ASN F ND2 1 ATOM 10231 N N . THR F 2 61 ? 28.376 -32.051 26.712 1.00 78.51 ? 61 THR F N 1 ATOM 10232 C CA . THR F 2 61 ? 29.227 -30.895 26.393 1.00 76.53 ? 61 THR F CA 1 ATOM 10233 C C . THR F 2 61 ? 28.341 -29.681 26.125 1.00 70.54 ? 61 THR F C 1 ATOM 10234 O O . THR F 2 61 ? 28.778 -28.692 25.537 1.00 69.38 ? 61 THR F O 1 ATOM 10235 C CB . THR F 2 61 ? 30.113 -31.139 25.147 1.00 80.16 ? 61 THR F CB 1 ATOM 10236 O OG1 . THR F 2 61 ? 29.461 -30.632 23.974 1.00 78.04 ? 61 THR F OG1 1 ATOM 10237 C CG2 . THR F 2 61 ? 30.433 -32.628 24.947 1.00 86.14 ? 61 THR F CG2 1 ATOM 10238 N N . GLN F 2 62 ? 27.091 -29.770 26.560 1.00 68.17 ? 62 GLN F N 1 ATOM 10239 C CA . GLN F 2 62 ? 26.078 -28.775 26.259 1.00 63.48 ? 62 GLN F CA 1 ATOM 10240 C C . GLN F 2 62 ? 26.347 -27.459 26.992 1.00 59.05 ? 62 GLN F C 1 ATOM 10241 O O . GLN F 2 62 ? 26.999 -27.441 28.033 1.00 59.76 ? 62 GLN F O 1 ATOM 10242 C CB . GLN F 2 62 ? 24.707 -29.350 26.623 1.00 64.14 ? 62 GLN F CB 1 ATOM 10243 C CG . GLN F 2 62 ? 23.520 -28.428 26.417 1.00 61.53 ? 62 GLN F CG 1 ATOM 10244 C CD . GLN F 2 62 ? 22.192 -29.173 26.433 1.00 64.01 ? 62 GLN F CD 1 ATOM 10245 O OE1 . GLN F 2 62 ? 22.143 -30.409 26.405 1.00 67.09 ? 62 GLN F OE1 1 ATOM 10246 N NE2 . GLN F 2 62 ? 21.104 -28.420 26.483 1.00 62.86 ? 62 GLN F NE2 1 ATOM 10247 N N . PHE F 2 63 ? 25.847 -26.366 26.422 1.00 54.87 ? 63 PHE F N 1 ATOM 10248 C CA . PHE F 2 63 ? 26.074 -25.021 26.946 1.00 51.11 ? 63 PHE F CA 1 ATOM 10249 C C . PHE F 2 63 ? 25.464 -24.830 28.332 1.00 50.96 ? 63 PHE F C 1 ATOM 10250 O O . PHE F 2 63 ? 24.322 -25.221 28.585 1.00 51.72 ? 63 PHE F O 1 ATOM 10251 C CB . PHE F 2 63 ? 25.485 -23.982 25.986 1.00 47.82 ? 63 PHE F CB 1 ATOM 10252 C CG . PHE F 2 63 ? 25.708 -22.558 26.410 1.00 44.12 ? 63 PHE F CG 1 ATOM 10253 C CD1 . PHE F 2 63 ? 26.869 -21.888 26.061 1.00 43.67 ? 63 PHE F CD1 1 ATOM 10254 C CD2 . PHE F 2 63 ? 24.739 -21.878 27.128 1.00 42.41 ? 63 PHE F CD2 1 ATOM 10255 C CE1 . PHE F 2 63 ? 27.068 -20.565 26.433 1.00 40.96 ? 63 PHE F CE1 1 ATOM 10256 C CE2 . PHE F 2 63 ? 24.931 -20.559 27.509 1.00 39.95 ? 63 PHE F CE2 1 ATOM 10257 C CZ . PHE F 2 63 ? 26.098 -19.903 27.163 1.00 38.74 ? 63 PHE F CZ 1 ATOM 10258 N N . GLU F 2 64 ? 26.240 -24.216 29.218 1.00 50.90 ? 64 GLU F N 1 ATOM 10259 C CA . GLU F 2 64 ? 25.781 -23.877 30.553 1.00 51.13 ? 64 GLU F CA 1 ATOM 10260 C C . GLU F 2 64 ? 25.708 -22.356 30.672 1.00 47.14 ? 64 GLU F C 1 ATOM 10261 O O . GLU F 2 64 ? 26.717 -21.672 30.526 1.00 45.00 ? 64 GLU F O 1 ATOM 10262 C CB . GLU F 2 64 ? 26.727 -24.474 31.592 1.00 55.56 ? 64 GLU F CB 1 ATOM 10263 C CG . GLU F 2 64 ? 26.872 -25.986 31.439 1.00 60.22 ? 64 GLU F CG 1 ATOM 10264 C CD . GLU F 2 64 ? 27.622 -26.646 32.578 1.00 65.76 ? 64 GLU F CD 1 ATOM 10265 O OE1 . GLU F 2 64 ? 28.240 -25.921 33.388 1.00 66.56 ? 64 GLU F OE1 1 ATOM 10266 O OE2 . GLU F 2 64 ? 27.584 -27.900 32.667 1.00 70.55 ? 64 GLU F OE2 1 ATOM 10267 N N . ALA F 2 65 ? 24.498 -21.844 30.904 1.00 45.90 ? 65 ALA F N 1 ATOM 10268 C CA . ALA F 2 65 ? 24.264 -20.406 31.092 1.00 43.36 ? 65 ALA F CA 1 ATOM 10269 C C . ALA F 2 65 ? 24.718 -19.915 32.474 1.00 44.14 ? 65 ALA F C 1 ATOM 10270 O O . ALA F 2 65 ? 24.768 -20.671 33.445 1.00 46.81 ? 65 ALA F O 1 ATOM 10271 C CB . ALA F 2 65 ? 22.793 -20.076 30.880 1.00 43.07 ? 65 ALA F CB 1 ATOM 10272 N N . VAL F 2 66 ? 25.051 -18.634 32.536 1.00 41.98 ? 66 VAL F N 1 ATOM 10273 C CA . VAL F 2 66 ? 25.610 -18.028 33.729 1.00 43.72 ? 66 VAL F CA 1 ATOM 10274 C C . VAL F 2 66 ? 24.969 -16.666 33.888 1.00 41.68 ? 66 VAL F C 1 ATOM 10275 O O . VAL F 2 66 ? 24.868 -15.912 32.925 1.00 39.43 ? 66 VAL F O 1 ATOM 10276 C CB . VAL F 2 66 ? 27.138 -17.846 33.598 1.00 44.33 ? 66 VAL F CB 1 ATOM 10277 C CG1 . VAL F 2 66 ? 27.687 -17.037 34.762 1.00 46.21 ? 66 VAL F CG1 1 ATOM 10278 C CG2 . VAL F 2 66 ? 27.830 -19.203 33.494 1.00 47.27 ? 66 VAL F CG2 1 ATOM 10279 N N . GLY F 2 67 ? 24.533 -16.357 35.099 1.00 43.79 ? 67 GLY F N 1 ATOM 10280 C CA . GLY F 2 67 ? 23.954 -15.063 35.373 1.00 43.18 ? 67 GLY F CA 1 ATOM 10281 C C . GLY F 2 67 ? 25.025 -13.997 35.271 1.00 41.53 ? 67 GLY F C 1 ATOM 10282 O O . GLY F 2 67 ? 26.087 -14.122 35.889 1.00 44.17 ? 67 GLY F O 1 ATOM 10283 N N . ARG F 2 68 ? 24.760 -12.971 34.472 1.00 37.60 ? 68 ARG F N 1 ATOM 10284 C CA . ARG F 2 68 ? 25.635 -11.814 34.396 1.00 36.29 ? 68 ARG F CA 1 ATOM 10285 C C . ARG F 2 68 ? 24.802 -10.575 34.641 1.00 35.47 ? 68 ARG F C 1 ATOM 10286 O O . ARG F 2 68 ? 23.685 -10.478 34.139 1.00 35.29 ? 68 ARG F O 1 ATOM 10287 C CB . ARG F 2 68 ? 26.308 -11.735 33.029 1.00 33.56 ? 68 ARG F CB 1 ATOM 10288 C CG . ARG F 2 68 ? 27.255 -12.887 32.781 1.00 35.19 ? 68 ARG F CG 1 ATOM 10289 C CD . ARG F 2 68 ? 28.216 -12.643 31.623 1.00 34.09 ? 68 ARG F CD 1 ATOM 10290 N NE . ARG F 2 68 ? 28.901 -13.892 31.268 1.00 35.99 ? 68 ARG F NE 1 ATOM 10291 C CZ . ARG F 2 68 ? 28.350 -14.882 30.553 1.00 35.70 ? 68 ARG F CZ 1 ATOM 10292 N NH1 . ARG F 2 68 ? 27.106 -14.790 30.086 1.00 33.59 ? 68 ARG F NH1 1 ATOM 10293 N NH2 . ARG F 2 68 ? 29.048 -15.982 30.302 1.00 38.42 ? 68 ARG F NH2 1 ATOM 10294 N N . GLU F 2 69 ? 25.340 -9.638 35.413 1.00 35.71 ? 69 GLU F N 1 ATOM 10295 C CA . GLU F 2 69 ? 24.608 -8.424 35.767 1.00 36.19 ? 69 GLU F CA 1 ATOM 10296 C C . GLU F 2 69 ? 25.179 -7.204 35.060 1.00 32.77 ? 69 GLU F C 1 ATOM 10297 O O . GLU F 2 69 ? 26.397 -7.061 34.948 1.00 31.59 ? 69 GLU F O 1 ATOM 10298 C CB . GLU F 2 69 ? 24.617 -8.222 37.281 1.00 41.01 ? 69 GLU F CB 1 ATOM 10299 C CG . GLU F 2 69 ? 23.946 -9.370 38.023 1.00 45.27 ? 69 GLU F CG 1 ATOM 10300 C CD . GLU F 2 69 ? 23.502 -8.986 39.411 1.00 51.25 ? 69 GLU F CD 1 ATOM 10301 O OE1 . GLU F 2 69 ? 23.012 -7.845 39.561 1.00 52.28 ? 69 GLU F OE1 1 ATOM 10302 O OE2 . GLU F 2 69 ? 23.640 -9.812 40.349 1.00 56.25 ? 69 GLU F OE2 1 ATOM 10303 N N . PHE F 2 70 ? 24.281 -6.338 34.593 1.00 31.72 ? 70 PHE F N 1 ATOM 10304 C CA . PHE F 2 70 ? 24.643 -5.091 33.910 1.00 29.84 ? 70 PHE F CA 1 ATOM 10305 C C . PHE F 2 70 ? 23.877 -3.927 34.508 1.00 31.54 ? 70 PHE F C 1 ATOM 10306 O O . PHE F 2 70 ? 22.810 -4.122 35.079 1.00 33.89 ? 70 PHE F O 1 ATOM 10307 C CB . PHE F 2 70 ? 24.354 -5.187 32.414 1.00 27.47 ? 70 PHE F CB 1 ATOM 10308 C CG . PHE F 2 70 ? 25.004 -6.372 31.761 1.00 27.40 ? 70 PHE F CG 1 ATOM 10309 C CD1 . PHE F 2 70 ? 26.313 -6.305 31.313 1.00 26.56 ? 70 PHE F CD1 1 ATOM 10310 C CD2 . PHE F 2 70 ? 24.314 -7.573 31.627 1.00 28.26 ? 70 PHE F CD2 1 ATOM 10311 C CE1 . PHE F 2 70 ? 26.919 -7.410 30.737 1.00 26.61 ? 70 PHE F CE1 1 ATOM 10312 C CE2 . PHE F 2 70 ? 24.913 -8.675 31.036 1.00 27.59 ? 70 PHE F CE2 1 ATOM 10313 C CZ . PHE F 2 70 ? 26.220 -8.594 30.599 1.00 26.98 ? 70 PHE F CZ 1 ATOM 10314 N N . ASN F 2 71 ? 24.439 -2.724 34.378 1.00 30.98 ? 71 ASN F N 1 ATOM 10315 C CA . ASN F 2 71 ? 23.819 -1.514 34.882 1.00 33.11 ? 71 ASN F CA 1 ATOM 10316 C C . ASN F 2 71 ? 23.039 -0.821 33.776 1.00 32.81 ? 71 ASN F C 1 ATOM 10317 O O . ASN F 2 71 ? 23.056 -1.254 32.621 1.00 29.80 ? 71 ASN F O 1 ATOM 10318 C CB . ASN F 2 71 ? 24.860 -0.571 35.510 1.00 34.37 ? 71 ASN F CB 1 ATOM 10319 C CG . ASN F 2 71 ? 25.855 -0.012 34.506 1.00 31.31 ? 71 ASN F CG 1 ATOM 10320 O OD1 . ASN F 2 71 ? 25.540 0.217 33.354 1.00 29.91 ? 71 ASN F OD1 1 ATOM 10321 N ND2 . ASN F 2 71 ? 27.066 0.196 34.948 1.00 32.36 ? 71 ASN F ND2 1 ATOM 10322 N N . ASN F 2 72 ? 22.356 0.263 34.133 1.00 36.13 ? 72 ASN F N 1 ATOM 10323 C CA . ASN F 2 72 ? 21.414 0.886 33.225 1.00 37.81 ? 72 ASN F CA 1 ATOM 10324 C C . ASN F 2 72 ? 22.066 1.622 32.056 1.00 35.10 ? 72 ASN F C 1 ATOM 10325 O O . ASN F 2 72 ? 21.355 2.086 31.176 1.00 35.81 ? 72 ASN F O 1 ATOM 10326 C CB . ASN F 2 72 ? 20.467 1.824 33.982 1.00 43.58 ? 72 ASN F CB 1 ATOM 10327 C CG . ASN F 2 72 ? 21.086 3.180 34.269 1.00 45.91 ? 72 ASN F CG 1 ATOM 10328 O OD1 . ASN F 2 72 ? 22.223 3.278 34.745 1.00 46.27 ? 72 ASN F OD1 1 ATOM 10329 N ND2 . ASN F 2 72 ? 20.334 4.241 33.984 1.00 49.47 ? 72 ASN F ND2 1 ATOM 10330 N N . LEU F 2 73 ? 23.395 1.752 32.048 1.00 32.62 ? 73 LEU F N 1 ATOM 10331 C CA . LEU F 2 73 ? 24.085 2.300 30.882 1.00 30.91 ? 73 LEU F CA 1 ATOM 10332 C C . LEU F 2 73 ? 24.907 1.243 30.136 1.00 28.48 ? 73 LEU F C 1 ATOM 10333 O O . LEU F 2 73 ? 25.775 1.586 29.327 1.00 27.80 ? 73 LEU F O 1 ATOM 10334 C CB . LEU F 2 73 ? 24.929 3.516 31.280 1.00 32.19 ? 73 LEU F CB 1 ATOM 10335 C CG . LEU F 2 73 ? 24.119 4.804 31.499 1.00 34.76 ? 73 LEU F CG 1 ATOM 10336 C CD1 . LEU F 2 73 ? 24.972 5.884 32.147 1.00 36.36 ? 73 LEU F CD1 1 ATOM 10337 C CD2 . LEU F 2 73 ? 23.504 5.322 30.202 1.00 34.73 ? 73 LEU F CD2 1 ATOM 10338 N N . GLU F 2 74 ? 24.585 -0.032 30.388 1.00 27.86 ? 74 GLU F N 1 ATOM 10339 C CA . GLU F 2 74 ? 25.201 -1.189 29.720 1.00 26.18 ? 74 GLU F CA 1 ATOM 10340 C C . GLU F 2 74 ? 24.124 -2.016 29.022 1.00 26.74 ? 74 GLU F C 1 ATOM 10341 O O . GLU F 2 74 ? 24.208 -3.251 28.939 1.00 26.40 ? 74 GLU F O 1 ATOM 10342 C CB . GLU F 2 74 ? 25.947 -2.069 30.730 1.00 25.91 ? 74 GLU F CB 1 ATOM 10343 C CG . GLU F 2 74 ? 27.218 -1.449 31.277 1.00 26.43 ? 74 GLU F CG 1 ATOM 10344 C CD . GLU F 2 74 ? 27.875 -2.290 32.364 1.00 27.79 ? 74 GLU F CD 1 ATOM 10345 O OE1 . GLU F 2 74 ? 27.165 -2.877 33.216 1.00 27.82 ? 74 GLU F OE1 1 ATOM 10346 O OE2 . GLU F 2 74 ? 29.122 -2.354 32.377 1.00 28.58 ? 74 GLU F OE2 1 ATOM 10347 N N . ARG F 2 75 ? 23.127 -1.322 28.489 1.00 27.75 ? 75 ARG F N 1 ATOM 10348 C CA . ARG F 2 75 ? 21.976 -1.977 27.895 1.00 29.40 ? 75 ARG F CA 1 ATOM 10349 C C . ARG F 2 75 ? 22.322 -2.780 26.639 1.00 27.34 ? 75 ARG F C 1 ATOM 10350 O O . ARG F 2 75 ? 21.787 -3.863 26.437 1.00 27.18 ? 75 ARG F O 1 ATOM 10351 C CB . ARG F 2 75 ? 20.867 -0.954 27.586 1.00 33.17 ? 75 ARG F CB 1 ATOM 10352 C CG . ARG F 2 75 ? 19.633 -1.017 28.467 1.00 37.81 ? 75 ARG F CG 1 ATOM 10353 C CD . ARG F 2 75 ? 19.905 -0.838 29.943 1.00 39.42 ? 75 ARG F CD 1 ATOM 10354 N NE . ARG F 2 75 ? 18.771 -1.278 30.765 1.00 44.82 ? 75 ARG F NE 1 ATOM 10355 C CZ . ARG F 2 75 ? 17.745 -0.512 31.133 1.00 50.00 ? 75 ARG F CZ 1 ATOM 10356 N NH1 . ARG F 2 75 ? 17.658 0.763 30.762 1.00 52.48 ? 75 ARG F NH1 1 ATOM 10357 N NH2 . ARG F 2 75 ? 16.791 -1.027 31.885 1.00 54.93 ? 75 ARG F NH2 1 ATOM 10358 N N . ARG F 2 76 ? 23.185 -2.246 25.783 1.00 25.81 ? 76 ARG F N 1 ATOM 10359 C CA . ARG F 2 76 ? 23.568 -2.963 24.563 1.00 25.19 ? 76 ARG F CA 1 ATOM 10360 C C . ARG F 2 76 ? 24.233 -4.315 24.894 1.00 24.61 ? 76 ARG F C 1 ATOM 10361 O O . ARG F 2 76 ? 23.859 -5.345 24.337 1.00 24.83 ? 76 ARG F O 1 ATOM 10362 C CB . ARG F 2 76 ? 24.473 -2.107 23.688 1.00 24.37 ? 76 ARG F CB 1 ATOM 10363 C CG . ARG F 2 76 ? 23.783 -0.891 23.076 1.00 26.00 ? 76 ARG F CG 1 ATOM 10364 C CD . ARG F 2 76 ? 24.774 0.127 22.538 1.00 25.63 ? 76 ARG F CD 1 ATOM 10365 N NE . ARG F 2 76 ? 25.687 0.547 23.602 1.00 23.54 ? 76 ARG F NE 1 ATOM 10366 C CZ . ARG F 2 76 ? 26.984 0.814 23.462 1.00 22.87 ? 76 ARG F CZ 1 ATOM 10367 N NH1 . ARG F 2 76 ? 27.583 0.734 22.264 1.00 25.10 ? 76 ARG F NH1 1 ATOM 10368 N NH2 . ARG F 2 76 ? 27.683 1.177 24.530 1.00 20.95 ? 76 ARG F NH2 1 ATOM 10369 N N . ILE F 2 77 ? 25.193 -4.314 25.812 1.00 24.37 ? 77 ILE F N 1 ATOM 10370 C CA . ILE F 2 77 ? 25.862 -5.556 26.185 1.00 24.79 ? 77 ILE F CA 1 ATOM 10371 C C . ILE F 2 77 ? 24.955 -6.464 26.995 1.00 25.18 ? 77 ILE F C 1 ATOM 10372 O O . ILE F 2 77 ? 25.057 -7.687 26.884 1.00 25.47 ? 77 ILE F O 1 ATOM 10373 C CB . ILE F 2 77 ? 27.198 -5.341 26.920 1.00 25.14 ? 77 ILE F CB 1 ATOM 10374 C CG1 . ILE F 2 77 ? 27.019 -4.564 28.217 1.00 26.23 ? 77 ILE F CG1 1 ATOM 10375 C CG2 . ILE F 2 77 ? 28.166 -4.599 26.024 1.00 26.39 ? 77 ILE F CG2 1 ATOM 10376 C CD1 . ILE F 2 77 ? 28.272 -4.537 29.071 1.00 27.83 ? 77 ILE F CD1 1 ATOM 10377 N N . GLU F 2 78 ? 24.059 -5.877 27.789 1.00 26.12 ? 78 GLU F N 1 ATOM 10378 C CA . GLU F 2 78 ? 23.026 -6.664 28.453 1.00 27.95 ? 78 GLU F CA 1 ATOM 10379 C C . GLU F 2 78 ? 22.192 -7.432 27.436 1.00 27.38 ? 78 GLU F C 1 ATOM 10380 O O . GLU F 2 78 ? 21.972 -8.631 27.599 1.00 27.82 ? 78 GLU F O 1 ATOM 10381 C CB . GLU F 2 78 ? 22.116 -5.793 29.321 1.00 31.31 ? 78 GLU F CB 1 ATOM 10382 C CG . GLU F 2 78 ? 21.046 -6.568 30.088 1.00 35.23 ? 78 GLU F CG 1 ATOM 10383 C CD . GLU F 2 78 ? 20.126 -5.644 30.864 1.00 40.49 ? 78 GLU F CD 1 ATOM 10384 O OE1 . GLU F 2 78 ? 19.541 -4.735 30.233 1.00 43.43 ? 78 GLU F OE1 1 ATOM 10385 O OE2 . GLU F 2 78 ? 19.996 -5.805 32.103 1.00 43.73 ? 78 GLU F OE2 1 ATOM 10386 N N . ASN F 2 79 ? 21.725 -6.745 26.399 1.00 27.17 ? 79 ASN F N 1 ATOM 10387 C CA . ASN F 2 79 ? 20.967 -7.401 25.324 1.00 28.83 ? 79 ASN F CA 1 ATOM 10388 C C . ASN F 2 79 ? 21.804 -8.446 24.605 1.00 28.28 ? 79 ASN F C 1 ATOM 10389 O O . ASN F 2 79 ? 21.342 -9.559 24.402 1.00 29.39 ? 79 ASN F O 1 ATOM 10390 C CB . ASN F 2 79 ? 20.456 -6.397 24.297 1.00 30.32 ? 79 ASN F CB 1 ATOM 10391 C CG . ASN F 2 79 ? 19.423 -7.008 23.352 1.00 33.74 ? 79 ASN F CG 1 ATOM 10392 O OD1 . ASN F 2 79 ? 19.655 -7.134 22.144 1.00 34.78 ? 79 ASN F OD1 1 ATOM 10393 N ND2 . ASN F 2 79 ? 18.293 -7.415 23.907 1.00 35.26 ? 79 ASN F ND2 1 ATOM 10394 N N . LEU F 2 80 ? 23.034 -8.076 24.242 1.00 26.99 ? 80 LEU F N 1 ATOM 10395 C CA . LEU F 2 80 ? 23.971 -8.986 23.592 1.00 27.80 ? 80 LEU F CA 1 ATOM 10396 C C . LEU F 2 80 ? 24.125 -10.270 24.412 1.00 28.12 ? 80 LEU F C 1 ATOM 10397 O O . LEU F 2 80 ? 23.995 -11.368 23.885 1.00 28.67 ? 80 LEU F O 1 ATOM 10398 C CB . LEU F 2 80 ? 25.331 -8.299 23.404 1.00 27.58 ? 80 LEU F CB 1 ATOM 10399 C CG . LEU F 2 80 ? 26.427 -8.953 22.543 1.00 29.46 ? 80 LEU F CG 1 ATOM 10400 C CD1 . LEU F 2 80 ? 27.561 -7.972 22.258 1.00 30.14 ? 80 LEU F CD1 1 ATOM 10401 C CD2 . LEU F 2 80 ? 27.006 -10.194 23.195 1.00 29.83 ? 80 LEU F CD2 1 ATOM 10402 N N . ASN F 2 81 ? 24.398 -10.111 25.707 1.00 27.88 ? 81 ASN F N 1 ATOM 10403 C CA . ASN F 2 81 ? 24.522 -11.237 26.629 1.00 27.92 ? 81 ASN F CA 1 ATOM 10404 C C . ASN F 2 81 ? 23.279 -12.119 26.583 1.00 29.22 ? 81 ASN F C 1 ATOM 10405 O O . ASN F 2 81 ? 23.378 -13.347 26.580 1.00 29.79 ? 81 ASN F O 1 ATOM 10406 C CB . ASN F 2 81 ? 24.756 -10.713 28.054 1.00 27.81 ? 81 ASN F CB 1 ATOM 10407 C CG . ASN F 2 81 ? 24.943 -11.822 29.071 1.00 28.09 ? 81 ASN F CG 1 ATOM 10408 O OD1 . ASN F 2 81 ? 25.965 -12.495 29.087 1.00 28.83 ? 81 ASN F OD1 1 ATOM 10409 N ND2 . ASN F 2 81 ? 23.961 -12.005 29.926 1.00 28.45 ? 81 ASN F ND2 1 ATOM 10410 N N . LYS F 2 82 ? 22.113 -11.479 26.531 1.00 30.19 ? 82 LYS F N 1 ATOM 10411 C CA . LYS F 2 82 ? 20.845 -12.190 26.554 1.00 32.35 ? 82 LYS F CA 1 ATOM 10412 C C . LYS F 2 82 ? 20.661 -12.999 25.285 1.00 33.51 ? 82 LYS F C 1 ATOM 10413 O O . LYS F 2 82 ? 20.384 -14.203 25.343 1.00 34.59 ? 82 LYS F O 1 ATOM 10414 C CB . LYS F 2 82 ? 19.672 -11.230 26.722 1.00 34.45 ? 82 LYS F CB 1 ATOM 10415 C CG . LYS F 2 82 ? 18.401 -11.976 27.047 1.00 39.18 ? 82 LYS F CG 1 ATOM 10416 C CD . LYS F 2 82 ? 17.189 -11.077 27.233 1.00 43.56 ? 82 LYS F CD 1 ATOM 10417 C CE . LYS F 2 82 ? 15.970 -11.936 27.548 1.00 48.85 ? 82 LYS F CE 1 ATOM 10418 N NZ . LYS F 2 82 ? 14.699 -11.355 27.037 1.00 54.83 ? 82 LYS F NZ 1 ATOM 10419 N N . LYS F 2 83 ? 20.798 -12.323 24.147 1.00 32.84 ? 83 LYS F N 1 ATOM 10420 C CA . LYS F 2 83 ? 20.756 -12.973 22.839 1.00 34.22 ? 83 LYS F CA 1 ATOM 10421 C C . LYS F 2 83 ? 21.680 -14.186 22.737 1.00 32.41 ? 83 LYS F C 1 ATOM 10422 O O . LYS F 2 83 ? 21.280 -15.243 22.236 1.00 34.06 ? 83 LYS F O 1 ATOM 10423 C CB . LYS F 2 83 ? 21.126 -11.982 21.743 1.00 35.40 ? 83 LYS F CB 1 ATOM 10424 C CG . LYS F 2 83 ? 19.954 -11.554 20.894 1.00 39.87 ? 83 LYS F CG 1 ATOM 10425 C CD . LYS F 2 83 ? 18.900 -10.811 21.689 1.00 40.87 ? 83 LYS F CD 1 ATOM 10426 C CE . LYS F 2 83 ? 17.773 -10.354 20.772 1.00 45.91 ? 83 LYS F CE 1 ATOM 10427 N NZ . LYS F 2 83 ? 17.244 -11.466 19.929 1.00 49.86 ? 83 LYS F NZ 1 ATOM 10428 N N . MET F 2 84 ? 22.911 -14.016 23.207 1.00 52.35 ? 84 MET F N 1 ATOM 10429 C CA . MET F 2 84 ? 23.923 -15.061 23.140 1.00 52.38 ? 84 MET F CA 1 ATOM 10430 C C . MET F 2 84 ? 23.525 -16.317 23.916 1.00 52.28 ? 84 MET F C 1 ATOM 10431 O O . MET F 2 84 ? 23.690 -17.435 23.425 1.00 52.50 ? 84 MET F O 1 ATOM 10432 C CB . MET F 2 84 ? 25.223 -14.539 23.712 1.00 53.61 ? 84 MET F CB 1 ATOM 10433 C CG . MET F 2 84 ? 26.409 -15.449 23.469 1.00 56.29 ? 84 MET F CG 1 ATOM 10434 S SD . MET F 2 84 ? 27.424 -15.621 24.937 1.00 59.82 ? 84 MET F SD 1 ATOM 10435 C CE . MET F 2 84 ? 26.597 -16.963 25.775 1.00 59.97 ? 84 MET F CE 1 ATOM 10436 N N . GLU F 2 85 ? 23.019 -16.134 25.131 1.00 51.78 ? 85 GLU F N 1 ATOM 10437 C CA . GLU F 2 85 ? 22.664 -17.269 25.982 1.00 52.92 ? 85 GLU F CA 1 ATOM 10438 C C . GLU F 2 85 ? 21.376 -17.953 25.541 1.00 51.81 ? 85 GLU F C 1 ATOM 10439 O O . GLU F 2 85 ? 21.305 -19.182 25.516 1.00 52.35 ? 85 GLU F O 1 ATOM 10440 C CB . GLU F 2 85 ? 22.586 -16.849 27.447 1.00 54.84 ? 85 GLU F CB 1 ATOM 10441 C CG . GLU F 2 85 ? 23.958 -16.572 28.042 1.00 56.56 ? 85 GLU F CG 1 ATOM 10442 C CD . GLU F 2 85 ? 23.958 -16.605 29.551 1.00 59.89 ? 85 GLU F CD 1 ATOM 10443 O OE1 . GLU F 2 85 ? 22.920 -16.250 30.148 1.00 60.50 ? 85 GLU F OE1 1 ATOM 10444 O OE2 . GLU F 2 85 ? 24.995 -16.989 30.132 1.00 62.75 ? 85 GLU F OE2 1 ATOM 10445 N N . ASP F 2 86 ? 20.372 -17.161 25.184 1.00 50.41 ? 86 ASP F N 1 ATOM 10446 C CA . ASP F 2 86 ? 19.171 -17.705 24.546 1.00 50.45 ? 86 ASP F CA 1 ATOM 10447 C C . ASP F 2 86 ? 19.514 -18.436 23.250 1.00 49.28 ? 86 ASP F C 1 ATOM 10448 O O . ASP F 2 86 ? 18.994 -19.528 22.988 1.00 49.72 ? 86 ASP F O 1 ATOM 10449 C CB . ASP F 2 86 ? 18.145 -16.610 24.254 1.00 50.61 ? 86 ASP F CB 1 ATOM 10450 C CG . ASP F 2 86 ? 17.055 -16.562 25.273 1.00 52.96 ? 86 ASP F CG 1 ATOM 10451 O OD1 . ASP F 2 86 ? 16.463 -17.631 25.578 1.00 55.02 ? 86 ASP F OD1 1 ATOM 10452 O OD2 . ASP F 2 86 ? 16.764 -15.460 25.751 1.00 53.56 ? 86 ASP F OD2 1 ATOM 10453 N N . GLY F 2 87 ? 20.390 -17.819 22.458 1.00 48.01 ? 87 GLY F N 1 ATOM 10454 C CA . GLY F 2 87 ? 20.865 -18.390 21.218 1.00 47.86 ? 87 GLY F CA 1 ATOM 10455 C C . GLY F 2 87 ? 21.392 -19.795 21.403 1.00 48.31 ? 87 GLY F C 1 ATOM 10456 O O . GLY F 2 87 ? 20.980 -20.713 20.699 1.00 48.56 ? 87 GLY F O 1 ATOM 10457 N N . PHE F 2 88 ? 22.299 -19.965 22.358 1.00 48.69 ? 88 PHE F N 1 ATOM 10458 C CA . PHE F 2 88 ? 22.905 -21.272 22.591 1.00 49.96 ? 88 PHE F CA 1 ATOM 10459 C C . PHE F 2 88 ? 21.899 -22.286 23.113 1.00 50.20 ? 88 PHE F C 1 ATOM 10460 O O . PHE F 2 88 ? 21.946 -23.450 22.720 1.00 50.71 ? 88 PHE F O 1 ATOM 10461 C CB . PHE F 2 88 ? 24.110 -21.183 23.537 1.00 51.62 ? 88 PHE F CB 1 ATOM 10462 C CG . PHE F 2 88 ? 25.390 -20.850 22.840 1.00 52.67 ? 88 PHE F CG 1 ATOM 10463 C CD1 . PHE F 2 88 ? 25.910 -21.705 21.882 1.00 54.00 ? 88 PHE F CD1 1 ATOM 10464 C CD2 . PHE F 2 88 ? 26.064 -19.678 23.120 1.00 52.87 ? 88 PHE F CD2 1 ATOM 10465 C CE1 . PHE F 2 88 ? 27.085 -21.400 21.223 1.00 56.08 ? 88 PHE F CE1 1 ATOM 10466 C CE2 . PHE F 2 88 ? 27.243 -19.368 22.465 1.00 54.62 ? 88 PHE F CE2 1 ATOM 10467 C CZ . PHE F 2 88 ? 27.751 -20.229 21.512 1.00 56.48 ? 88 PHE F CZ 1 ATOM 10468 N N . LEU F 2 89 ? 20.993 -21.846 23.982 1.00 50.18 ? 89 LEU F N 1 ATOM 10469 C CA . LEU F 2 89 ? 19.976 -22.739 24.533 1.00 51.31 ? 89 LEU F CA 1 ATOM 10470 C C . LEU F 2 89 ? 18.991 -23.197 23.457 1.00 50.58 ? 89 LEU F C 1 ATOM 10471 O O . LEU F 2 89 ? 18.547 -24.343 23.488 1.00 51.39 ? 89 LEU F O 1 ATOM 10472 C CB . LEU F 2 89 ? 19.229 -22.084 25.690 1.00 52.60 ? 89 LEU F CB 1 ATOM 10473 C CG . LEU F 2 89 ? 20.081 -21.702 26.903 1.00 54.28 ? 89 LEU F CG 1 ATOM 10474 C CD1 . LEU F 2 89 ? 19.284 -20.786 27.815 1.00 55.61 ? 89 LEU F CD1 1 ATOM 10475 C CD2 . LEU F 2 89 ? 20.588 -22.918 27.660 1.00 56.89 ? 89 LEU F CD2 1 ATOM 10476 N N . ASP F 2 90 ? 18.670 -22.320 22.506 1.00 49.54 ? 90 ASP F N 1 ATOM 10477 C CA . ASP F 2 90 ? 17.849 -22.710 21.350 1.00 49.71 ? 90 ASP F CA 1 ATOM 10478 C C . ASP F 2 90 ? 18.559 -23.738 20.462 1.00 49.55 ? 90 ASP F C 1 ATOM 10479 O O . ASP F 2 90 ? 17.959 -24.737 20.051 1.00 50.08 ? 90 ASP F O 1 ATOM 10480 C CB . ASP F 2 90 ? 17.457 -21.497 20.505 1.00 49.68 ? 90 ASP F CB 1 ATOM 10481 C CG . ASP F 2 90 ? 16.449 -20.600 21.194 1.00 50.59 ? 90 ASP F CG 1 ATOM 10482 O OD1 . ASP F 2 90 ? 15.740 -21.061 22.111 1.00 51.81 ? 90 ASP F OD1 1 ATOM 10483 O OD2 . ASP F 2 90 ? 16.369 -19.416 20.810 1.00 50.70 ? 90 ASP F OD2 1 ATOM 10484 N N . VAL F 2 91 ? 19.833 -23.493 20.177 1.00 49.24 ? 91 VAL F N 1 ATOM 10485 C CA . VAL F 2 91 ? 20.639 -24.439 19.400 1.00 50.01 ? 91 VAL F CA 1 ATOM 10486 C C . VAL F 2 91 ? 20.630 -25.826 20.049 1.00 50.70 ? 91 VAL F C 1 ATOM 10487 O O . VAL F 2 91 ? 20.310 -26.816 19.401 1.00 51.03 ? 91 VAL F O 1 ATOM 10488 C CB . VAL F 2 91 ? 22.095 -23.942 19.237 1.00 50.63 ? 91 VAL F CB 1 ATOM 10489 C CG1 . VAL F 2 91 ? 23.004 -25.051 18.728 1.00 52.40 ? 91 VAL F CG1 1 ATOM 10490 C CG2 . VAL F 2 91 ? 22.152 -22.729 18.312 1.00 50.59 ? 91 VAL F CG2 1 ATOM 10491 N N . TRP F 2 92 ? 20.973 -25.889 21.330 1.00 51.39 ? 92 TRP F N 1 ATOM 10492 C CA . TRP F 2 92 ? 21.111 -27.171 22.018 1.00 53.02 ? 92 TRP F CA 1 ATOM 10493 C C . TRP F 2 92 ? 19.769 -27.864 22.252 1.00 53.14 ? 92 TRP F C 1 ATOM 10494 O O . TRP F 2 92 ? 19.693 -29.088 22.252 1.00 53.83 ? 92 TRP F O 1 ATOM 10495 C CB . TRP F 2 92 ? 21.870 -27.000 23.336 1.00 54.74 ? 92 TRP F CB 1 ATOM 10496 C CG . TRP F 2 92 ? 23.344 -26.865 23.133 1.00 56.10 ? 92 TRP F CG 1 ATOM 10497 C CD1 . TRP F 2 92 ? 24.095 -25.752 23.318 1.00 56.22 ? 92 TRP F CD1 1 ATOM 10498 C CD2 . TRP F 2 92 ? 24.244 -27.892 22.690 1.00 58.16 ? 92 TRP F CD2 1 ATOM 10499 N NE1 . TRP F 2 92 ? 25.411 -26.013 23.031 1.00 58.58 ? 92 TRP F NE1 1 ATOM 10500 C CE2 . TRP F 2 92 ? 25.533 -27.319 22.640 1.00 59.92 ? 92 TRP F CE2 1 ATOM 10501 C CE3 . TRP F 2 92 ? 24.086 -29.237 22.338 1.00 58.91 ? 92 TRP F CE3 1 ATOM 10502 C CZ2 . TRP F 2 92 ? 26.662 -28.042 22.248 1.00 63.03 ? 92 TRP F CZ2 1 ATOM 10503 C CZ3 . TRP F 2 92 ? 25.207 -29.957 21.944 1.00 61.64 ? 92 TRP F CZ3 1 ATOM 10504 C CH2 . TRP F 2 92 ? 26.479 -29.356 21.904 1.00 63.96 ? 92 TRP F CH2 1 ATOM 10505 N N . THR F 2 93 ? 18.721 -27.074 22.458 1.00 52.92 ? 93 THR F N 1 ATOM 10506 C CA . THR F 2 93 ? 17.362 -27.592 22.521 1.00 53.82 ? 93 THR F CA 1 ATOM 10507 C C . THR F 2 93 ? 17.019 -28.244 21.186 1.00 53.53 ? 93 THR F C 1 ATOM 10508 O O . THR F 2 93 ? 16.487 -29.356 21.148 1.00 54.25 ? 93 THR F O 1 ATOM 10509 C CB . THR F 2 93 ? 16.364 -26.465 22.864 1.00 54.26 ? 93 THR F CB 1 ATOM 10510 O OG1 . THR F 2 93 ? 16.571 -26.052 24.222 1.00 55.40 ? 93 THR F OG1 1 ATOM 10511 C CG2 . THR F 2 93 ? 14.912 -26.919 22.690 1.00 55.79 ? 93 THR F CG2 1 ATOM 10512 N N . TYR F 2 94 ? 17.348 -27.555 20.098 1.00 53.05 ? 94 TYR F N 1 ATOM 10513 C CA . TYR F 2 94 ? 17.185 -28.101 18.751 1.00 53.76 ? 94 TYR F CA 1 ATOM 10514 C C . TYR F 2 94 ? 17.933 -29.425 18.586 1.00 54.20 ? 94 TYR F C 1 ATOM 10515 O O . TYR F 2 94 ? 17.354 -30.410 18.143 1.00 54.66 ? 94 TYR F O 1 ATOM 10516 C CB . TYR F 2 94 ? 17.658 -27.088 17.712 1.00 53.91 ? 94 TYR F CB 1 ATOM 10517 C CG . TYR F 2 94 ? 17.637 -27.577 16.286 1.00 55.48 ? 94 TYR F CG 1 ATOM 10518 C CD1 . TYR F 2 94 ? 18.710 -28.288 15.755 1.00 56.28 ? 94 TYR F CD1 1 ATOM 10519 C CD2 . TYR F 2 94 ? 16.554 -27.308 15.455 1.00 57.08 ? 94 TYR F CD2 1 ATOM 10520 C CE1 . TYR F 2 94 ? 18.702 -28.729 14.440 1.00 58.25 ? 94 TYR F CE1 1 ATOM 10521 C CE2 . TYR F 2 94 ? 16.535 -27.744 14.139 1.00 59.14 ? 94 TYR F CE2 1 ATOM 10522 C CZ . TYR F 2 94 ? 17.613 -28.456 13.635 1.00 59.59 ? 94 TYR F CZ 1 ATOM 10523 O OH . TYR F 2 94 ? 17.592 -28.890 12.328 1.00 62.22 ? 94 TYR F OH 1 ATOM 10524 N N . ASN F 2 95 ? 19.210 -29.435 18.959 1.00 54.67 ? 95 ASN F N 1 ATOM 10525 C CA . ASN F 2 95 ? 20.054 -30.629 18.852 1.00 56.08 ? 95 ASN F CA 1 ATOM 10526 C C . ASN F 2 95 ? 19.526 -31.814 19.656 1.00 56.94 ? 95 ASN F C 1 ATOM 10527 O O . ASN F 2 95 ? 19.605 -32.962 19.199 1.00 57.58 ? 95 ASN F O 1 ATOM 10528 C CB . ASN F 2 95 ? 21.500 -30.328 19.279 1.00 57.20 ? 95 ASN F CB 1 ATOM 10529 C CG . ASN F 2 95 ? 22.251 -29.476 18.265 1.00 57.73 ? 95 ASN F CG 1 ATOM 10530 O OD1 . ASN F 2 95 ? 21.988 -29.548 17.071 1.00 58.30 ? 95 ASN F OD1 1 ATOM 10531 N ND2 . ASN F 2 95 ? 23.197 -28.671 18.740 1.00 58.37 ? 95 ASN F ND2 1 ATOM 10532 N N . ALA F 2 96 ? 18.997 -31.534 20.846 1.00 57.45 ? 96 ALA F N 1 ATOM 10533 C CA . ALA F 2 96 ? 18.426 -32.573 21.701 1.00 59.22 ? 96 ALA F CA 1 ATOM 10534 C C . ALA F 2 96 ? 17.166 -33.157 21.074 1.00 59.31 ? 96 ALA F C 1 ATOM 10535 O O . ALA F 2 96 ? 17.028 -34.369 20.967 1.00 60.16 ? 96 ALA F O 1 ATOM 10536 C CB . ALA F 2 96 ? 18.121 -32.025 23.086 1.00 60.40 ? 96 ALA F CB 1 ATOM 10537 N N . GLU F 2 97 ? 16.262 -32.286 20.644 1.00 59.34 ? 97 GLU F N 1 ATOM 10538 C CA . GLU F 2 97 ? 15.012 -32.714 20.029 1.00 60.40 ? 97 GLU F CA 1 ATOM 10539 C C . GLU F 2 97 ? 15.252 -33.425 18.708 1.00 60.49 ? 97 GLU F C 1 ATOM 10540 O O . GLU F 2 97 ? 14.747 -34.525 18.489 1.00 61.15 ? 97 GLU F O 1 ATOM 10541 C CB . GLU F 2 97 ? 14.086 -31.519 19.808 1.00 60.86 ? 97 GLU F CB 1 ATOM 10542 C CG . GLU F 2 97 ? 13.450 -31.001 21.084 1.00 62.46 ? 97 GLU F CG 1 ATOM 10543 C CD . GLU F 2 97 ? 12.686 -29.708 20.875 1.00 63.65 ? 97 GLU F CD 1 ATOM 10544 O OE1 . GLU F 2 97 ? 12.756 -29.132 19.766 1.00 63.36 ? 97 GLU F OE1 1 ATOM 10545 O OE2 . GLU F 2 97 ? 12.025 -29.251 21.829 1.00 65.98 ? 97 GLU F OE2 1 ATOM 10546 N N . LEU F 2 98 ? 16.025 -32.792 17.832 1.00 60.57 ? 98 LEU F N 1 ATOM 10547 C CA . LEU F 2 98 ? 16.305 -33.357 16.518 1.00 61.67 ? 98 LEU F CA 1 ATOM 10548 C C . LEU F 2 98 ? 16.959 -34.732 16.610 1.00 62.17 ? 98 LEU F C 1 ATOM 10549 O O . LEU F 2 98 ? 16.682 -35.605 15.788 1.00 62.85 ? 98 LEU F O 1 ATOM 10550 C CB . LEU F 2 98 ? 17.199 -32.417 15.702 1.00 62.13 ? 98 LEU F CB 1 ATOM 10551 C CG . LEU F 2 98 ? 17.527 -32.905 14.282 1.00 64.03 ? 98 LEU F CG 1 ATOM 10552 C CD1 . LEU F 2 98 ? 16.264 -33.003 13.443 1.00 65.30 ? 98 LEU F CD1 1 ATOM 10553 C CD2 . LEU F 2 98 ? 18.537 -32.005 13.591 1.00 65.29 ? 98 LEU F CD2 1 ATOM 10554 N N . LEU F 2 99 ? 17.829 -34.922 17.597 1.00 62.56 ? 99 LEU F N 1 ATOM 10555 C CA . LEU F 2 99 ? 18.521 -36.199 17.755 1.00 64.18 ? 99 LEU F CA 1 ATOM 10556 C C . LEU F 2 99 ? 17.570 -37.285 18.236 1.00 64.89 ? 99 LEU F C 1 ATOM 10557 O O . LEU F 2 99 ? 17.685 -38.434 17.829 1.00 65.68 ? 99 LEU F O 1 ATOM 10558 C CB . LEU F 2 99 ? 19.703 -36.076 18.718 1.00 65.20 ? 99 LEU F CB 1 ATOM 10559 C CG . LEU F 2 99 ? 20.567 -37.332 18.881 1.00 67.35 ? 99 LEU F CG 1 ATOM 10560 C CD1 . LEU F 2 99 ? 21.185 -37.746 17.550 1.00 68.31 ? 99 LEU F CD1 1 ATOM 10561 C CD2 . LEU F 2 99 ? 21.645 -37.117 19.933 1.00 69.37 ? 99 LEU F CD2 1 ATOM 10562 N N . VAL F 2 100 ? 16.635 -36.914 19.104 1.00 65.49 ? 100 VAL F N 1 ATOM 10563 C CA . VAL F 2 100 ? 15.650 -37.858 19.624 1.00 66.71 ? 100 VAL F CA 1 ATOM 10564 C C . VAL F 2 100 ? 14.708 -38.338 18.518 1.00 67.10 ? 100 VAL F C 1 ATOM 10565 O O . VAL F 2 100 ? 14.434 -39.536 18.414 1.00 67.88 ? 100 VAL F O 1 ATOM 10566 C CB . VAL F 2 100 ? 14.865 -37.241 20.806 1.00 67.53 ? 100 VAL F CB 1 ATOM 10567 C CG1 . VAL F 2 100 ? 13.642 -38.080 21.167 1.00 69.32 ? 100 VAL F CG1 1 ATOM 10568 C CG2 . VAL F 2 100 ? 15.779 -37.094 22.014 1.00 68.45 ? 100 VAL F CG2 1 ATOM 10569 N N . LEU F 2 101 ? 14.229 -37.414 17.689 1.00 67.58 ? 101 LEU F N 1 ATOM 10570 C CA . LEU F 2 101 ? 13.327 -37.763 16.589 1.00 69.47 ? 101 LEU F CA 1 ATOM 10571 C C . LEU F 2 101 ? 14.003 -38.723 15.611 1.00 70.80 ? 101 LEU F C 1 ATOM 10572 O O . LEU F 2 101 ? 13.436 -39.761 15.245 1.00 71.07 ? 101 LEU F O 1 ATOM 10573 C CB . LEU F 2 101 ? 12.855 -36.510 15.842 1.00 69.78 ? 101 LEU F CB 1 ATOM 10574 C CG . LEU F 2 101 ? 11.978 -35.527 16.627 1.00 70.74 ? 101 LEU F CG 1 ATOM 10575 C CD1 . LEU F 2 101 ? 11.541 -34.361 15.754 1.00 71.78 ? 101 LEU F CD1 1 ATOM 10576 C CD2 . LEU F 2 101 ? 10.762 -36.215 17.224 1.00 72.60 ? 101 LEU F CD2 1 ATOM 10577 N N . MET F 2 102 ? 15.218 -38.364 15.203 1.00 71.59 ? 102 MET F N 1 ATOM 10578 C CA . MET F 2 102 ? 16.007 -39.185 14.289 1.00 73.53 ? 102 MET F CA 1 ATOM 10579 C C . MET F 2 102 ? 16.385 -40.541 14.888 1.00 73.80 ? 102 MET F C 1 ATOM 10580 O O . MET F 2 102 ? 16.394 -41.550 14.180 1.00 74.49 ? 102 MET F O 1 ATOM 10581 C CB . MET F 2 102 ? 17.267 -38.426 13.851 1.00 74.85 ? 102 MET F CB 1 ATOM 10582 C CG . MET F 2 102 ? 16.992 -37.366 12.795 1.00 76.55 ? 102 MET F CG 1 ATOM 10583 S SD . MET F 2 102 ? 18.244 -36.070 12.684 1.00 78.77 ? 102 MET F SD 1 ATOM 10584 C CE . MET F 2 102 ? 19.759 -37.026 12.832 1.00 80.07 ? 102 MET F CE 1 ATOM 10585 N N . GLU F 2 103 ? 16.701 -40.561 16.181 1.00 73.64 ? 103 GLU F N 1 ATOM 10586 C CA . GLU F 2 103 ? 17.081 -41.801 16.862 1.00 74.78 ? 103 GLU F CA 1 ATOM 10587 C C . GLU F 2 103 ? 15.888 -42.746 16.976 1.00 75.06 ? 103 GLU F C 1 ATOM 10588 O O . GLU F 2 103 ? 16.034 -43.955 16.816 1.00 75.88 ? 103 GLU F O 1 ATOM 10589 C CB . GLU F 2 103 ? 17.657 -41.510 18.251 1.00 75.05 ? 103 GLU F CB 1 ATOM 10590 N N . ASN F 2 104 ? 14.713 -42.189 17.251 1.00 75.13 ? 104 ASN F N 1 ATOM 10591 C CA . ASN F 2 104 ? 13.487 -42.981 17.302 1.00 76.18 ? 104 ASN F CA 1 ATOM 10592 C C . ASN F 2 104 ? 13.177 -43.621 15.954 1.00 77.02 ? 104 ASN F C 1 ATOM 10593 O O . ASN F 2 104 ? 12.797 -44.794 15.897 1.00 76.88 ? 104 ASN F O 1 ATOM 10594 C CB . ASN F 2 104 ? 12.299 -42.122 17.749 1.00 76.74 ? 104 ASN F CB 1 ATOM 10595 C CG . ASN F 2 104 ? 12.369 -41.736 19.218 1.00 77.38 ? 104 ASN F CG 1 ATOM 10596 O OD1 . ASN F 2 104 ? 13.166 -42.280 19.987 1.00 77.71 ? 104 ASN F OD1 1 ATOM 10597 N ND2 . ASN F 2 104 ? 11.523 -40.794 19.617 1.00 78.02 ? 104 ASN F ND2 1 ATOM 10598 N N . GLU F 2 105 ? 13.350 -42.852 14.877 1.00 77.66 ? 105 GLU F N 1 ATOM 10599 C CA . GLU F 2 105 ? 13.128 -43.360 13.520 1.00 79.98 ? 105 GLU F CA 1 ATOM 10600 C C . GLU F 2 105 ? 14.044 -44.543 13.238 1.00 80.63 ? 105 GLU F C 1 ATOM 10601 O O . GLU F 2 105 ? 13.585 -45.596 12.782 1.00 80.97 ? 105 GLU F O 1 ATOM 10602 C CB . GLU F 2 105 ? 13.361 -42.271 12.465 1.00 81.39 ? 105 GLU F CB 1 ATOM 10603 C CG . GLU F 2 105 ? 12.715 -42.560 11.112 1.00 84.38 ? 105 GLU F CG 1 ATOM 10604 C CD . GLU F 2 105 ? 12.132 -41.314 10.460 1.00 87.25 ? 105 GLU F CD 1 ATOM 10605 O OE1 . GLU F 2 105 ? 11.029 -40.891 10.875 1.00 88.10 ? 105 GLU F OE1 1 ATOM 10606 O OE2 . GLU F 2 105 ? 12.776 -40.746 9.545 1.00 89.27 ? 105 GLU F OE2 1 ATOM 10607 N N . ARG F 2 106 ? 15.334 -44.362 13.518 1.00 80.62 ? 106 ARG F N 1 ATOM 10608 C CA . ARG F 2 106 ? 16.315 -45.430 13.344 1.00 82.47 ? 106 ARG F CA 1 ATOM 10609 C C . ARG F 2 106 ? 16.002 -46.636 14.226 1.00 81.62 ? 106 ARG F C 1 ATOM 10610 O O . ARG F 2 106 ? 16.097 -47.775 13.772 1.00 82.29 ? 106 ARG F O 1 ATOM 10611 C CB . ARG F 2 106 ? 17.739 -44.933 13.627 1.00 84.54 ? 106 ARG F CB 1 ATOM 10612 C CG . ARG F 2 106 ? 18.315 -44.042 12.536 1.00 86.93 ? 106 ARG F CG 1 ATOM 10613 C CD . ARG F 2 106 ? 19.836 -44.021 12.571 1.00 90.36 ? 106 ARG F CD 1 ATOM 10614 N NE . ARG F 2 106 ? 20.390 -43.078 11.596 1.00 93.55 ? 106 ARG F NE 1 ATOM 10615 C CZ . ARG F 2 106 ? 21.671 -42.704 11.526 1.00 96.42 ? 106 ARG F CZ 1 ATOM 10616 N NH1 . ARG F 2 106 ? 22.574 -43.189 12.372 1.00 97.83 ? 106 ARG F NH1 1 ATOM 10617 N NH2 . ARG F 2 106 ? 22.055 -41.836 10.596 1.00 98.47 ? 106 ARG F NH2 1 ATOM 10618 N N . THR F 2 107 ? 15.619 -46.381 15.476 1.00 79.82 ? 107 THR F N 1 ATOM 10619 C CA . THR F 2 107 ? 15.338 -47.456 16.434 1.00 79.64 ? 107 THR F CA 1 ATOM 10620 C C . THR F 2 107 ? 14.128 -48.316 16.037 1.00 78.72 ? 107 THR F C 1 ATOM 10621 O O . THR F 2 107 ? 14.154 -49.531 16.213 1.00 79.58 ? 107 THR F O 1 ATOM 10622 C CB . THR F 2 107 ? 15.149 -46.890 17.857 1.00 79.72 ? 107 THR F CB 1 ATOM 10623 O OG1 . THR F 2 107 ? 16.318 -46.150 18.228 1.00 79.46 ? 107 THR F OG1 1 ATOM 10624 C CG2 . THR F 2 107 ? 14.926 -48.007 18.872 1.00 81.59 ? 107 THR F CG2 1 ATOM 10625 N N . LEU F 2 108 ? 13.084 -47.691 15.501 1.00 77.73 ? 108 LEU F N 1 ATOM 10626 C CA . LEU F 2 108 ? 11.905 -48.424 15.029 1.00 78.40 ? 108 LEU F CA 1 ATOM 10627 C C . LEU F 2 108 ? 12.211 -49.217 13.755 1.00 79.10 ? 108 LEU F C 1 ATOM 10628 O O . LEU F 2 108 ? 11.815 -50.378 13.629 1.00 79.09 ? 108 LEU F O 1 ATOM 10629 C CB . LEU F 2 108 ? 10.731 -47.468 14.791 1.00 78.61 ? 108 LEU F CB 1 ATOM 10630 C CG . LEU F 2 108 ? 10.177 -46.765 16.036 1.00 79.11 ? 108 LEU F CG 1 ATOM 10631 C CD1 . LEU F 2 108 ? 9.059 -45.801 15.663 1.00 80.17 ? 108 LEU F CD1 1 ATOM 10632 C CD2 . LEU F 2 108 ? 9.687 -47.776 17.064 1.00 80.86 ? 108 LEU F CD2 1 ATOM 10633 N N . ASP F 2 109 ? 12.924 -48.584 12.823 1.00 79.74 ? 109 ASP F N 1 ATOM 10634 C CA . ASP F 2 109 ? 13.384 -49.249 11.596 1.00 80.96 ? 109 ASP F CA 1 ATOM 10635 C C . ASP F 2 109 ? 14.447 -50.320 11.881 1.00 81.60 ? 109 ASP F C 1 ATOM 10636 O O . ASP F 2 109 ? 14.572 -51.292 11.128 1.00 82.52 ? 109 ASP F O 1 ATOM 10637 C CB . ASP F 2 109 ? 13.934 -48.217 10.602 1.00 81.64 ? 109 ASP F CB 1 ATOM 10638 C CG . ASP F 2 109 ? 12.855 -47.294 10.058 1.00 82.45 ? 109 ASP F CG 1 ATOM 10639 O OD1 . ASP F 2 109 ? 11.706 -47.757 9.883 1.00 83.15 ? 109 ASP F OD1 1 ATOM 10640 O OD2 . ASP F 2 109 ? 13.157 -46.107 9.799 1.00 82.41 ? 109 ASP F OD2 1 ATOM 10641 N N . PHE F 2 110 ? 15.206 -50.130 12.962 1.00 81.49 ? 110 PHE F N 1 ATOM 10642 C CA . PHE F 2 110 ? 16.201 -51.110 13.414 1.00 83.04 ? 110 PHE F CA 1 ATOM 10643 C C . PHE F 2 110 ? 15.531 -52.402 13.883 1.00 83.05 ? 110 PHE F C 1 ATOM 10644 O O . PHE F 2 110 ? 16.000 -53.490 13.562 1.00 84.66 ? 110 PHE F O 1 ATOM 10645 C CB . PHE F 2 110 ? 17.080 -50.513 14.525 1.00 83.70 ? 110 PHE F CB 1 ATOM 10646 C CG . PHE F 2 110 ? 18.015 -51.499 15.169 1.00 86.36 ? 110 PHE F CG 1 ATOM 10647 C CD1 . PHE F 2 110 ? 18.923 -52.220 14.403 1.00 89.22 ? 110 PHE F CD1 1 ATOM 10648 C CD2 . PHE F 2 110 ? 18.000 -51.694 16.545 1.00 87.37 ? 110 PHE F CD2 1 ATOM 10649 C CE1 . PHE F 2 110 ? 19.786 -53.131 14.995 1.00 92.41 ? 110 PHE F CE1 1 ATOM 10650 C CE2 . PHE F 2 110 ? 18.861 -52.599 17.144 1.00 90.76 ? 110 PHE F CE2 1 ATOM 10651 C CZ . PHE F 2 110 ? 19.757 -53.319 16.368 1.00 93.26 ? 110 PHE F CZ 1 ATOM 10652 N N . HIS F 2 111 ? 14.438 -52.281 14.635 1.00 81.85 ? 111 HIS F N 1 ATOM 10653 C CA . HIS F 2 111 ? 13.663 -53.453 15.060 1.00 81.86 ? 111 HIS F CA 1 ATOM 10654 C C . HIS F 2 111 ? 13.024 -54.164 13.872 1.00 81.50 ? 111 HIS F C 1 ATOM 10655 O O . HIS F 2 111 ? 12.944 -55.392 13.855 1.00 82.40 ? 111 HIS F O 1 ATOM 10656 C CB . HIS F 2 111 ? 12.576 -53.066 16.067 1.00 81.84 ? 111 HIS F CB 1 ATOM 10657 C CG . HIS F 2 111 ? 13.099 -52.767 17.438 1.00 82.75 ? 111 HIS F CG 1 ATOM 10658 N ND1 . HIS F 2 111 ? 13.813 -53.685 18.177 1.00 84.48 ? 111 HIS F ND1 1 ATOM 10659 C CD2 . HIS F 2 111 ? 12.993 -51.660 18.212 1.00 82.51 ? 111 HIS F CD2 1 ATOM 10660 C CE1 . HIS F 2 111 ? 14.135 -53.153 19.343 1.00 85.85 ? 111 HIS F CE1 1 ATOM 10661 N NE2 . HIS F 2 111 ? 13.649 -51.925 19.389 1.00 84.42 ? 111 HIS F NE2 1 ATOM 10662 N N . ASP F 2 112 ? 12.562 -53.391 12.891 1.00 80.70 ? 112 ASP F N 1 ATOM 10663 C CA . ASP F 2 112 ? 12.026 -53.955 11.650 1.00 81.50 ? 112 ASP F CA 1 ATOM 10664 C C . ASP F 2 112 ? 13.064 -54.817 10.948 1.00 82.35 ? 112 ASP F C 1 ATOM 10665 O O . ASP F 2 112 ? 12.810 -55.984 10.649 1.00 82.59 ? 112 ASP F O 1 ATOM 10666 C CB . ASP F 2 112 ? 11.560 -52.850 10.694 1.00 82.08 ? 112 ASP F CB 1 ATOM 10667 C CG . ASP F 2 112 ? 10.051 -52.743 10.611 1.00 83.09 ? 112 ASP F CG 1 ATOM 10668 O OD1 . ASP F 2 112 ? 9.383 -53.801 10.512 1.00 83.17 ? 112 ASP F OD1 1 ATOM 10669 O OD2 . ASP F 2 112 ? 9.541 -51.599 10.627 1.00 83.04 ? 112 ASP F OD2 1 ATOM 10670 N N . SER F 2 113 ? 14.232 -54.228 10.700 1.00 82.91 ? 113 SER F N 1 ATOM 10671 C CA . SER F 2 113 ? 15.349 -54.916 10.051 1.00 84.94 ? 113 SER F CA 1 ATOM 10672 C C . SER F 2 113 ? 15.656 -56.272 10.692 1.00 86.17 ? 113 SER F C 1 ATOM 10673 O O . SER F 2 113 ? 15.928 -57.248 9.984 1.00 87.57 ? 113 SER F O 1 ATOM 10674 C CB . SER F 2 113 ? 16.603 -54.038 10.086 1.00 85.73 ? 113 SER F CB 1 ATOM 10675 O OG . SER F 2 113 ? 17.691 -54.663 9.430 1.00 88.27 ? 113 SER F OG 1 ATOM 10676 N N . ASN F 2 114 ? 15.597 -56.333 12.022 1.00 85.45 ? 114 ASN F N 1 ATOM 10677 C CA . ASN F 2 114 ? 15.930 -57.563 12.754 1.00 86.95 ? 114 ASN F CA 1 ATOM 10678 C C . ASN F 2 114 ? 14.843 -58.646 12.654 1.00 86.40 ? 114 ASN F C 1 ATOM 10679 O O . ASN F 2 114 ? 15.112 -59.825 12.906 1.00 87.56 ? 114 ASN F O 1 ATOM 10680 C CB . ASN F 2 114 ? 16.230 -57.246 14.220 1.00 87.66 ? 114 ASN F CB 1 ATOM 10681 C CG . ASN F 2 114 ? 17.187 -56.075 14.382 1.00 88.52 ? 114 ASN F CG 1 ATOM 10682 O OD1 . ASN F 2 114 ? 17.954 -55.748 13.472 1.00 89.61 ? 114 ASN F OD1 1 ATOM 10683 N ND2 . ASN F 2 114 ? 17.129 -55.421 15.538 1.00 88.57 ? 114 ASN F ND2 1 ATOM 10684 N N . VAL F 2 115 ? 13.624 -58.241 12.292 1.00 84.77 ? 115 VAL F N 1 ATOM 10685 C CA . VAL F 2 115 ? 12.534 -59.180 12.007 1.00 84.55 ? 115 VAL F CA 1 ATOM 10686 C C . VAL F 2 115 ? 12.661 -59.748 10.586 1.00 85.15 ? 115 VAL F C 1 ATOM 10687 O O . VAL F 2 115 ? 12.411 -60.939 10.364 1.00 85.16 ? 115 VAL F O 1 ATOM 10688 C CB . VAL F 2 115 ? 11.145 -58.516 12.178 1.00 83.90 ? 115 VAL F CB 1 ATOM 10689 C CG1 . VAL F 2 115 ? 10.027 -59.479 11.779 1.00 84.67 ? 115 VAL F CG1 1 ATOM 10690 C CG2 . VAL F 2 115 ? 10.952 -58.039 13.612 1.00 83.60 ? 115 VAL F CG2 1 ATOM 10691 N N . LYS F 2 116 ? 13.038 -58.892 9.633 1.00 85.33 ? 116 LYS F N 1 ATOM 10692 C CA . LYS F 2 116 ? 13.276 -59.322 8.249 1.00 87.23 ? 116 LYS F CA 1 ATOM 10693 C C . LYS F 2 116 ? 14.442 -60.304 8.209 1.00 88.73 ? 116 LYS F C 1 ATOM 10694 O O . LYS F 2 116 ? 14.351 -61.364 7.596 1.00 90.20 ? 116 LYS F O 1 ATOM 10695 C CB . LYS F 2 116 ? 13.623 -58.137 7.334 1.00 88.65 ? 116 LYS F CB 1 ATOM 10696 C CG . LYS F 2 116 ? 12.635 -56.973 7.297 1.00 87.79 ? 116 LYS F CG 1 ATOM 10697 C CD . LYS F 2 116 ? 13.269 -55.755 6.622 1.00 88.91 ? 116 LYS F CD 1 ATOM 10698 C CE . LYS F 2 116 ? 12.489 -54.470 6.868 1.00 87.81 ? 116 LYS F CE 1 ATOM 10699 N NZ . LYS F 2 116 ? 13.294 -53.248 6.574 1.00 88.15 ? 116 LYS F NZ 1 ATOM 10700 N N . ASN F 2 117 ? 15.536 -59.933 8.872 1.00 89.10 ? 117 ASN F N 1 ATOM 10701 C CA . ASN F 2 117 ? 16.770 -60.722 8.870 1.00 91.81 ? 117 ASN F CA 1 ATOM 10702 C C . ASN F 2 117 ? 16.615 -62.065 9.582 1.00 91.70 ? 117 ASN F C 1 ATOM 10703 O O . ASN F 2 117 ? 17.258 -63.047 9.210 1.00 94.10 ? 117 ASN F O 1 ATOM 10704 C CB . ASN F 2 117 ? 17.918 -59.928 9.511 1.00 92.86 ? 117 ASN F CB 1 ATOM 10705 C CG . ASN F 2 117 ? 18.238 -58.641 8.764 1.00 93.55 ? 117 ASN F CG 1 ATOM 10706 O OD1 . ASN F 2 117 ? 17.900 -58.486 7.589 1.00 94.48 ? 117 ASN F OD1 1 ATOM 10707 N ND2 . ASN F 2 117 ? 18.887 -57.704 9.451 1.00 93.45 ? 117 ASN F ND2 1 ATOM 10708 N N . LEU F 2 118 ? 15.768 -62.096 10.609 1.00 89.55 ? 118 LEU F N 1 ATOM 10709 C CA . LEU F 2 118 ? 15.467 -63.330 11.336 1.00 89.87 ? 118 LEU F CA 1 ATOM 10710 C C . LEU F 2 118 ? 14.547 -64.241 10.523 1.00 88.98 ? 118 LEU F C 1 ATOM 10711 O O . LEU F 2 118 ? 14.677 -65.463 10.578 1.00 90.36 ? 118 LEU F O 1 ATOM 10712 C CB . LEU F 2 118 ? 14.833 -63.014 12.696 1.00 88.82 ? 118 LEU F CB 1 ATOM 10713 C CG . LEU F 2 118 ? 14.533 -64.203 13.617 1.00 90.33 ? 118 LEU F CG 1 ATOM 10714 C CD1 . LEU F 2 118 ? 15.798 -64.989 13.935 1.00 93.56 ? 118 LEU F CD1 1 ATOM 10715 C CD2 . LEU F 2 118 ? 13.862 -63.726 14.895 1.00 90.17 ? 118 LEU F CD2 1 ATOM 10716 N N . TYR F 2 119 ? 13.620 -63.640 9.778 1.00 87.30 ? 119 TYR F N 1 ATOM 10717 C CA . TYR F 2 119 ? 12.736 -64.384 8.881 1.00 87.65 ? 119 TYR F CA 1 ATOM 10718 C C . TYR F 2 119 ? 13.507 -65.028 7.723 1.00 90.18 ? 119 TYR F C 1 ATOM 10719 O O . TYR F 2 119 ? 13.210 -66.157 7.322 1.00 89.96 ? 119 TYR F O 1 ATOM 10720 C CB . TYR F 2 119 ? 11.636 -63.471 8.332 1.00 86.92 ? 119 TYR F CB 1 ATOM 10721 C CG . TYR F 2 119 ? 10.669 -64.186 7.420 1.00 87.92 ? 119 TYR F CG 1 ATOM 10722 C CD1 . TYR F 2 119 ? 9.721 -65.060 7.937 1.00 87.57 ? 119 TYR F CD1 1 ATOM 10723 C CD2 . TYR F 2 119 ? 10.712 -64.002 6.040 1.00 89.98 ? 119 TYR F CD2 1 ATOM 10724 C CE1 . TYR F 2 119 ? 8.835 -65.729 7.107 1.00 88.96 ? 119 TYR F CE1 1 ATOM 10725 C CE2 . TYR F 2 119 ? 9.831 -64.669 5.201 1.00 91.70 ? 119 TYR F CE2 1 ATOM 10726 C CZ . TYR F 2 119 ? 8.891 -65.535 5.738 1.00 90.85 ? 119 TYR F CZ 1 ATOM 10727 O OH . TYR F 2 119 ? 8.003 -66.204 4.918 1.00 92.26 ? 119 TYR F OH 1 ATOM 10728 N N . ASP F 2 120 ? 14.490 -64.300 7.196 1.00 92.09 ? 120 ASP F N 1 ATOM 10729 C CA . ASP F 2 120 ? 15.341 -64.798 6.114 1.00 95.72 ? 120 ASP F CA 1 ATOM 10730 C C . ASP F 2 120 ? 16.218 -65.962 6.578 1.00 98.03 ? 120 ASP F C 1 ATOM 10731 O O . ASP F 2 120 ? 16.436 -66.911 5.828 1.00 100.20 ? 120 ASP F O 1 ATOM 10732 C CB . ASP F 2 120 ? 16.239 -63.679 5.571 1.00 97.45 ? 120 ASP F CB 1 ATOM 10733 C CG . ASP F 2 120 ? 15.457 -62.565 4.893 1.00 96.59 ? 120 ASP F CG 1 ATOM 10734 O OD1 . ASP F 2 120 ? 14.212 -62.635 4.832 1.00 94.53 ? 120 ASP F OD1 1 ATOM 10735 O OD2 . ASP F 2 120 ? 16.101 -61.607 4.419 1.00 98.67 ? 120 ASP F OD2 1 ATOM 10736 N N . LYS F 2 121 ? 16.722 -65.872 7.808 1.00 98.18 ? 121 LYS F N 1 ATOM 10737 C CA . LYS F 2 121 ? 17.584 -66.908 8.387 1.00 101.20 ? 121 LYS F CA 1 ATOM 10738 C C . LYS F 2 121 ? 16.872 -68.261 8.470 1.00 100.80 ? 121 LYS F C 1 ATOM 10739 O O . LYS F 2 121 ? 17.481 -69.297 8.211 1.00 103.70 ? 121 LYS F O 1 ATOM 10740 C CB . LYS F 2 121 ? 18.065 -66.481 9.780 1.00 101.48 ? 121 LYS F CB 1 ATOM 10741 C CG . LYS F 2 121 ? 19.070 -67.428 10.424 1.00 105.68 ? 121 LYS F CG 1 ATOM 10742 C CD . LYS F 2 121 ? 19.578 -66.877 11.749 1.00 106.66 ? 121 LYS F CD 1 ATOM 10743 C CE . LYS F 2 121 ? 20.712 -67.718 12.316 1.00 112.11 ? 121 LYS F CE 1 ATOM 10744 N NZ . LYS F 2 121 ? 20.289 -69.105 12.659 1.00 113.14 ? 121 LYS F NZ 1 ATOM 10745 N N . VAL F 2 122 ? 15.588 -68.240 8.830 1.00 97.65 ? 122 VAL F N 1 ATOM 10746 C CA . VAL F 2 122 ? 14.762 -69.453 8.859 1.00 97.03 ? 122 VAL F CA 1 ATOM 10747 C C . VAL F 2 122 ? 14.421 -69.901 7.434 1.00 97.86 ? 122 VAL F C 1 ATOM 10748 O O . VAL F 2 122 ? 14.332 -71.100 7.160 1.00 98.57 ? 122 VAL F O 1 ATOM 10749 C CB . VAL F 2 122 ? 13.460 -69.244 9.668 1.00 94.32 ? 122 VAL F CB 1 ATOM 10750 C CG1 . VAL F 2 122 ? 12.593 -70.497 9.645 1.00 94.16 ? 122 VAL F CG1 1 ATOM 10751 C CG2 . VAL F 2 122 ? 13.784 -68.846 11.103 1.00 94.51 ? 122 VAL F CG2 1 ATOM 10752 N N . ARG F 2 123 ? 14.226 -68.940 6.532 1.00 97.62 ? 123 ARG F N 1 ATOM 10753 C CA . ARG F 2 123 ? 14.018 -69.251 5.116 1.00 99.62 ? 123 ARG F CA 1 ATOM 10754 C C . ARG F 2 123 ? 15.289 -69.860 4.504 1.00 103.59 ? 123 ARG F C 1 ATOM 10755 O O . ARG F 2 123 ? 15.213 -70.811 3.725 1.00 105.14 ? 123 ARG F O 1 ATOM 10756 C CB . ARG F 2 123 ? 13.584 -67.999 4.345 1.00 99.42 ? 123 ARG F CB 1 ATOM 10757 C CG . ARG F 2 123 ? 13.177 -68.255 2.901 1.00 102.11 ? 123 ARG F CG 1 ATOM 10758 C CD . ARG F 2 123 ? 12.335 -67.115 2.341 1.00 102.17 ? 123 ARG F CD 1 ATOM 10759 N NE . ARG F 2 123 ? 12.983 -65.806 2.484 1.00 102.28 ? 123 ARG F NE 1 ATOM 10760 C CZ . ARG F 2 123 ? 13.948 -65.329 1.692 1.00 105.91 ? 123 ARG F CZ 1 ATOM 10761 N NH1 . ARG F 2 123 ? 14.419 -66.044 0.671 1.00 110.08 ? 123 ARG F NH1 1 ATOM 10762 N NH2 . ARG F 2 123 ? 14.454 -64.119 1.925 1.00 105.67 ? 123 ARG F NH2 1 ATOM 10763 N N . LEU F 2 124 ? 16.448 -69.321 4.884 1.00 105.07 ? 124 LEU F N 1 ATOM 10764 C CA . LEU F 2 124 ? 17.742 -69.813 4.406 1.00 109.91 ? 124 LEU F CA 1 ATOM 10765 C C . LEU F 2 124 ? 18.169 -71.134 5.064 1.00 111.42 ? 124 LEU F C 1 ATOM 10766 O O . LEU F 2 124 ? 18.728 -72.002 4.395 1.00 115.16 ? 124 LEU F O 1 ATOM 10767 C CB . LEU F 2 124 ? 18.829 -68.759 4.635 1.00 111.47 ? 124 LEU F CB 1 ATOM 10768 N N . GLN F 2 125 ? 17.921 -71.268 6.367 1.00 109.21 ? 125 GLN F N 1 ATOM 10769 C CA . GLN F 2 125 ? 18.311 -72.462 7.135 1.00 111.59 ? 125 GLN F CA 1 ATOM 10770 C C . GLN F 2 125 ? 17.566 -73.715 6.659 1.00 111.56 ? 125 GLN F C 1 ATOM 10771 O O . GLN F 2 125 ? 18.104 -74.825 6.676 1.00 114.08 ? 125 GLN F O 1 ATOM 10772 C CB . GLN F 2 125 ? 18.053 -72.227 8.628 1.00 109.63 ? 125 GLN F CB 1 ATOM 10773 C CG . GLN F 2 125 ? 18.347 -73.412 9.539 1.00 112.24 ? 125 GLN F CG 1 ATOM 10774 C CD . GLN F 2 125 ? 18.381 -73.028 11.011 1.00 112.20 ? 125 GLN F CD 1 ATOM 10775 O OE1 . GLN F 2 125 ? 18.982 -73.726 11.827 1.00 115.78 ? 125 GLN F OE1 1 ATOM 10776 N NE2 . GLN F 2 125 ? 17.736 -71.912 11.356 1.00 108.60 ? 125 GLN F NE2 1 ATOM 10777 N N . LEU F 2 126 ? 16.321 -73.511 6.248 1.00 108.76 ? 126 LEU F N 1 ATOM 10778 C CA . LEU F 2 126 ? 15.516 -74.542 5.620 1.00 109.00 ? 126 LEU F CA 1 ATOM 10779 C C . LEU F 2 126 ? 14.916 -73.952 4.341 1.00 108.99 ? 126 LEU F C 1 ATOM 10780 O O . LEU F 2 126 ? 13.857 -73.318 4.370 1.00 106.40 ? 126 LEU F O 1 ATOM 10781 C CB . LEU F 2 126 ? 14.447 -75.075 6.593 1.00 106.33 ? 126 LEU F CB 1 ATOM 10782 C CG . LEU F 2 126 ? 13.881 -74.188 7.720 1.00 103.27 ? 126 LEU F CG 1 ATOM 10783 C CD1 . LEU F 2 126 ? 12.536 -73.575 7.350 1.00 100.42 ? 126 LEU F CD1 1 ATOM 10784 C CD2 . LEU F 2 126 ? 13.741 -75.000 9.000 1.00 103.67 ? 126 LEU F CD2 1 ATOM 10785 N N . ARG F 2 127 ? 15.627 -74.145 3.229 1.00 112.80 ? 127 ARG F N 1 ATOM 10786 C CA . ARG F 2 127 ? 15.257 -73.556 1.940 1.00 113.91 ? 127 ARG F CA 1 ATOM 10787 C C . ARG F 2 127 ? 14.332 -74.479 1.154 1.00 114.08 ? 127 ARG F C 1 ATOM 10788 O O . ARG F 2 127 ? 13.195 -74.113 0.848 1.00 112.41 ? 127 ARG F O 1 ATOM 10789 C CB . ARG F 2 127 ? 16.513 -73.253 1.115 1.00 119.02 ? 127 ARG F CB 1 ATOM 10790 N N . ASP F 2 128 ? 14.833 -75.674 0.841 1.00 116.33 ? 128 ASP F N 1 ATOM 10791 C CA . ASP F 2 128 ? 14.112 -76.647 0.010 1.00 117.09 ? 128 ASP F CA 1 ATOM 10792 C C . ASP F 2 128 ? 13.284 -77.661 0.818 1.00 113.70 ? 128 ASP F C 1 ATOM 10793 O O . ASP F 2 128 ? 12.498 -78.420 0.241 1.00 113.93 ? 128 ASP F O 1 ATOM 10794 C CB . ASP F 2 128 ? 15.087 -77.377 -0.935 1.00 122.65 ? 128 ASP F CB 1 ATOM 10795 C CG . ASP F 2 128 ? 16.265 -78.024 -0.207 1.00 124.32 ? 128 ASP F CG 1 ATOM 10796 O OD1 . ASP F 2 128 ? 16.398 -77.849 1.023 1.00 121.34 ? 128 ASP F OD1 1 ATOM 10797 O OD2 . ASP F 2 128 ? 17.072 -78.702 -0.876 1.00 129.16 ? 128 ASP F OD2 1 ATOM 10798 N N . ASN F 2 129 ? 13.463 -77.671 2.140 1.00 110.88 ? 129 ASN F N 1 ATOM 10799 C CA . ASN F 2 129 ? 12.684 -78.534 3.034 1.00 108.11 ? 129 ASN F CA 1 ATOM 10800 C C . ASN F 2 129 ? 11.482 -77.816 3.663 1.00 104.71 ? 129 ASN F C 1 ATOM 10801 O O . ASN F 2 129 ? 10.851 -78.355 4.576 1.00 102.60 ? 129 ASN F O 1 ATOM 10802 C CB . ASN F 2 129 ? 13.583 -79.109 4.144 1.00 108.68 ? 129 ASN F CB 1 ATOM 10803 C CG . ASN F 2 129 ? 14.556 -80.168 3.638 1.00 112.61 ? 129 ASN F CG 1 ATOM 10804 O OD1 . ASN F 2 129 ? 14.405 -80.706 2.539 1.00 113.90 ? 129 ASN F OD1 1 ATOM 10805 N ND2 . ASN F 2 129 ? 15.560 -80.477 4.452 1.00 114.64 ? 129 ASN F ND2 1 ATOM 10806 N N . ALA F 2 130 ? 11.162 -76.612 3.178 1.00 104.85 ? 130 ALA F N 1 ATOM 10807 C CA . ALA F 2 130 ? 10.028 -75.837 3.703 1.00 102.25 ? 130 ALA F CA 1 ATOM 10808 C C . ALA F 2 130 ? 9.568 -74.711 2.762 1.00 103.13 ? 130 ALA F C 1 ATOM 10809 O O . ALA F 2 130 ? 10.385 -74.054 2.114 1.00 104.66 ? 130 ALA F O 1 ATOM 10810 C CB . ALA F 2 130 ? 10.372 -75.266 5.071 1.00 100.46 ? 130 ALA F CB 1 ATOM 10811 N N . LYS F 2 131 ? 8.252 -74.499 2.714 1.00 102.87 ? 131 LYS F N 1 ATOM 10812 C CA . LYS F 2 131 ? 7.627 -73.476 1.869 1.00 104.68 ? 131 LYS F CA 1 ATOM 10813 C C . LYS F 2 131 ? 7.239 -72.271 2.715 1.00 102.74 ? 131 LYS F C 1 ATOM 10814 O O . LYS F 2 131 ? 6.660 -72.430 3.792 1.00 100.60 ? 131 LYS F O 1 ATOM 10815 C CB . LYS F 2 131 ? 6.375 -74.051 1.188 1.00 107.15 ? 131 LYS F CB 1 ATOM 10816 C CG . LYS F 2 131 ? 5.416 -73.031 0.577 1.00 109.53 ? 131 LYS F CG 1 ATOM 10817 C CD . LYS F 2 131 ? 4.047 -73.653 0.322 1.00 111.51 ? 131 LYS F CD 1 ATOM 10818 C CE . LYS F 2 131 ? 3.013 -72.617 -0.100 1.00 114.60 ? 131 LYS F CE 1 ATOM 10819 N NZ . LYS F 2 131 ? 2.494 -72.862 -1.475 1.00 119.70 ? 131 LYS F NZ 1 ATOM 10820 N N . GLU F 2 132 ? 7.546 -71.072 2.216 1.00 103.90 ? 132 GLU F N 1 ATOM 10821 C CA . GLU F 2 132 ? 7.142 -69.822 2.865 1.00 102.23 ? 132 GLU F CA 1 ATOM 10822 C C . GLU F 2 132 ? 5.683 -69.524 2.523 1.00 103.81 ? 132 GLU F C 1 ATOM 10823 O O . GLU F 2 132 ? 5.278 -69.629 1.361 1.00 107.05 ? 132 GLU F O 1 ATOM 10824 C CB . GLU F 2 132 ? 8.032 -68.661 2.414 1.00 103.08 ? 132 GLU F CB 1 ATOM 10825 N N . LEU F 2 133 ? 4.900 -69.157 3.537 1.00 102.17 ? 133 LEU F N 1 ATOM 10826 C CA . LEU F 2 133 ? 3.468 -68.898 3.356 1.00 104.07 ? 133 LEU F CA 1 ATOM 10827 C C . LEU F 2 133 ? 3.208 -67.448 2.952 1.00 104.77 ? 133 LEU F C 1 ATOM 10828 O O . LEU F 2 133 ? 2.419 -67.187 2.043 1.00 108.30 ? 133 LEU F O 1 ATOM 10829 C CB . LEU F 2 133 ? 2.683 -69.252 4.628 1.00 103.27 ? 133 LEU F CB 1 ATOM 10830 C CG . LEU F 2 133 ? 2.491 -70.754 4.894 1.00 103.31 ? 133 LEU F CG 1 ATOM 10831 C CD1 . LEU F 2 133 ? 1.874 -70.977 6.269 1.00 102.91 ? 133 LEU F CD1 1 ATOM 10832 C CD2 . LEU F 2 133 ? 1.646 -71.413 3.808 1.00 106.44 ? 133 LEU F CD2 1 ATOM 10833 N N . GLY F 2 134 ? 3.871 -66.514 3.627 1.00 101.58 ? 134 GLY F N 1 ATOM 10834 C CA . GLY F 2 134 ? 3.738 -65.093 3.308 1.00 102.40 ? 134 GLY F CA 1 ATOM 10835 C C . GLY F 2 134 ? 3.358 -64.221 4.489 1.00 100.19 ? 134 GLY F C 1 ATOM 10836 O O . GLY F 2 134 ? 3.641 -63.022 4.486 1.00 99.99 ? 134 GLY F O 1 ATOM 10837 N N . ASN F 2 135 ? 2.716 -64.816 5.496 1.00 98.74 ? 135 ASN F N 1 ATOM 10838 C CA . ASN F 2 135 ? 2.305 -64.088 6.708 1.00 97.50 ? 135 ASN F CA 1 ATOM 10839 C C . ASN F 2 135 ? 3.372 -64.087 7.814 1.00 93.43 ? 135 ASN F C 1 ATOM 10840 O O . ASN F 2 135 ? 3.087 -63.718 8.955 1.00 92.75 ? 135 ASN F O 1 ATOM 10841 C CB . ASN F 2 135 ? 0.991 -64.666 7.251 1.00 99.71 ? 135 ASN F CB 1 ATOM 10842 C CG . ASN F 2 135 ? 1.136 -66.099 7.739 1.00 98.55 ? 135 ASN F CG 1 ATOM 10843 O OD1 . ASN F 2 135 ? 2.098 -66.795 7.399 1.00 95.81 ? 135 ASN F OD1 1 ATOM 10844 N ND2 . ASN F 2 135 ? 0.175 -66.550 8.538 1.00 100.76 ? 135 ASN F ND2 1 ATOM 10845 N N . GLY F 2 136 ? 4.591 -64.497 7.464 1.00 91.34 ? 136 GLY F N 1 ATOM 10846 C CA . GLY F 2 136 ? 5.694 -64.619 8.413 1.00 88.78 ? 136 GLY F CA 1 ATOM 10847 C C . GLY F 2 136 ? 5.928 -66.039 8.915 1.00 88.49 ? 136 GLY F C 1 ATOM 10848 O O . GLY F 2 136 ? 6.564 -66.221 9.954 1.00 87.89 ? 136 GLY F O 1 ATOM 10849 N N . CYS F 2 137 ? 5.448 -67.046 8.179 1.00 91.26 ? 137 CYS F N 1 ATOM 10850 C CA . CYS F 2 137 ? 5.558 -68.449 8.614 1.00 85.92 ? 137 CYS F CA 1 ATOM 10851 C C . CYS F 2 137 ? 6.295 -69.337 7.604 1.00 84.43 ? 137 CYS F C 1 ATOM 10852 O O . CYS F 2 137 ? 6.709 -68.877 6.536 1.00 87.77 ? 137 CYS F O 1 ATOM 10853 C CB . CYS F 2 137 ? 4.166 -69.024 8.907 1.00 87.32 ? 137 CYS F CB 1 ATOM 10854 S SG . CYS F 2 137 ? 3.349 -68.284 10.339 1.00 89.11 ? 137 CYS F SG 1 ATOM 10855 N N . PHE F 2 138 ? 6.471 -70.608 7.969 1.00 80.36 ? 138 PHE F N 1 ATOM 10856 C CA . PHE F 2 138 ? 7.123 -71.592 7.114 1.00 79.19 ? 138 PHE F CA 1 ATOM 10857 C C . PHE F 2 138 ? 6.600 -73.006 7.402 1.00 76.97 ? 138 PHE F C 1 ATOM 10858 O O . PHE F 2 138 ? 6.712 -73.495 8.528 1.00 73.25 ? 138 PHE F O 1 ATOM 10859 C CB . PHE F 2 138 ? 8.636 -71.541 7.327 1.00 77.01 ? 138 PHE F CB 1 ATOM 10860 N N . GLU F 2 139 ? 6.024 -73.646 6.384 1.00 79.81 ? 139 GLU F N 1 ATOM 10861 C CA . GLU F 2 139 ? 5.523 -75.026 6.497 1.00 79.06 ? 139 GLU F CA 1 ATOM 10862 C C . GLU F 2 139 ? 6.608 -76.031 6.151 1.00 76.84 ? 139 GLU F C 1 ATOM 10863 O O . GLU F 2 139 ? 7.157 -76.008 5.052 1.00 78.94 ? 139 GLU F O 1 ATOM 10864 C CB . GLU F 2 139 ? 4.335 -75.263 5.563 1.00 84.53 ? 139 GLU F CB 1 ATOM 10865 C CG . GLU F 2 139 ? 2.989 -74.890 6.147 1.00 87.53 ? 139 GLU F CG 1 ATOM 10866 C CD . GLU F 2 139 ? 1.863 -75.173 5.180 1.00 94.46 ? 139 GLU F CD 1 ATOM 10867 O OE1 . GLU F 2 139 ? 1.855 -74.556 4.095 1.00 99.26 ? 139 GLU F OE1 1 ATOM 10868 O OE2 . GLU F 2 139 ? 0.995 -76.012 5.501 1.00 96.17 ? 139 GLU F OE2 1 ATOM 10869 N N . PHE F 2 140 ? 6.899 -76.927 7.084 1.00 73.89 ? 140 PHE F N 1 ATOM 10870 C CA . PHE F 2 140 ? 7.854 -78.001 6.835 1.00 73.13 ? 140 PHE F CA 1 ATOM 10871 C C . PHE F 2 140 ? 7.286 -79.005 5.828 1.00 76.46 ? 140 PHE F C 1 ATOM 10872 O O . PHE F 2 140 ? 6.073 -79.240 5.781 1.00 77.89 ? 140 PHE F O 1 ATOM 10873 C CB . PHE F 2 140 ? 8.210 -78.717 8.139 1.00 69.84 ? 140 PHE F CB 1 ATOM 10874 C CG . PHE F 2 140 ? 9.062 -77.899 9.072 1.00 67.90 ? 140 PHE F CG 1 ATOM 10875 C CD1 . PHE F 2 140 ? 8.494 -76.925 9.891 1.00 66.78 ? 140 PHE F CD1 1 ATOM 10876 C CD2 . PHE F 2 140 ? 10.437 -78.108 9.138 1.00 67.69 ? 140 PHE F CD2 1 ATOM 10877 C CE1 . PHE F 2 140 ? 9.283 -76.177 10.751 1.00 65.90 ? 140 PHE F CE1 1 ATOM 10878 C CE2 . PHE F 2 140 ? 11.227 -77.361 9.996 1.00 67.44 ? 140 PHE F CE2 1 ATOM 10879 C CZ . PHE F 2 140 ? 10.650 -76.390 10.801 1.00 66.11 ? 140 PHE F CZ 1 ATOM 10880 N N . TYR F 2 141 ? 8.173 -79.575 5.014 1.00 78.57 ? 141 TYR F N 1 ATOM 10881 C CA . TYR F 2 141 ? 7.816 -80.664 4.102 1.00 82.23 ? 141 TYR F CA 1 ATOM 10882 C C . TYR F 2 141 ? 8.179 -82.025 4.702 1.00 80.64 ? 141 TYR F C 1 ATOM 10883 O O . TYR F 2 141 ? 8.071 -83.053 4.036 1.00 84.06 ? 141 TYR F O 1 ATOM 10884 C CB . TYR F 2 141 ? 8.487 -80.468 2.738 1.00 86.52 ? 141 TYR F CB 1 ATOM 10885 C CG . TYR F 2 141 ? 7.758 -79.487 1.848 1.00 90.90 ? 141 TYR F CG 1 ATOM 10886 C CD1 . TYR F 2 141 ? 6.562 -79.841 1.225 1.00 95.59 ? 141 TYR F CD1 1 ATOM 10887 C CD2 . TYR F 2 141 ? 8.257 -78.206 1.630 1.00 91.99 ? 141 TYR F CD2 1 ATOM 10888 C CE1 . TYR F 2 141 ? 5.884 -78.949 0.407 1.00 100.90 ? 141 TYR F CE1 1 ATOM 10889 C CE2 . TYR F 2 141 ? 7.588 -77.304 0.815 1.00 96.88 ? 141 TYR F CE2 1 ATOM 10890 C CZ . TYR F 2 141 ? 6.398 -77.681 0.205 1.00 101.47 ? 141 TYR F CZ 1 ATOM 10891 O OH . TYR F 2 141 ? 5.721 -76.797 -0.608 1.00 107.54 ? 141 TYR F OH 1 ATOM 10892 N N . HIS F 2 142 ? 8.621 -82.012 5.958 1.00 77.07 ? 142 HIS F N 1 ATOM 10893 C CA . HIS F 2 142 ? 8.808 -83.220 6.763 1.00 76.12 ? 142 HIS F CA 1 ATOM 10894 C C . HIS F 2 142 ? 8.329 -82.923 8.190 1.00 73.12 ? 142 HIS F C 1 ATOM 10895 O O . HIS F 2 142 ? 7.953 -81.787 8.504 1.00 71.45 ? 142 HIS F O 1 ATOM 10896 C CB . HIS F 2 142 ? 10.281 -83.641 6.770 1.00 76.95 ? 142 HIS F CB 1 ATOM 10897 C CG . HIS F 2 142 ? 11.184 -82.653 7.437 1.00 75.94 ? 142 HIS F CG 1 ATOM 10898 N ND1 . HIS F 2 142 ? 11.538 -81.457 6.849 1.00 76.60 ? 142 HIS F ND1 1 ATOM 10899 C CD2 . HIS F 2 142 ? 11.788 -82.669 8.650 1.00 74.88 ? 142 HIS F CD2 1 ATOM 10900 C CE1 . HIS F 2 142 ? 12.327 -80.784 7.667 1.00 75.53 ? 142 HIS F CE1 1 ATOM 10901 N NE2 . HIS F 2 142 ? 12.494 -81.496 8.767 1.00 74.46 ? 142 HIS F NE2 1 ATOM 10902 N N . ARG F 2 143 ? 8.346 -83.939 9.050 1.00 72.83 ? 143 ARG F N 1 ATOM 10903 C CA . ARG F 2 143 ? 7.914 -83.777 10.439 1.00 71.01 ? 143 ARG F CA 1 ATOM 10904 C C . ARG F 2 143 ? 9.088 -83.262 11.258 1.00 68.82 ? 143 ARG F C 1 ATOM 10905 O O . ARG F 2 143 ? 10.168 -83.844 11.224 1.00 70.40 ? 143 ARG F O 1 ATOM 10906 C CB . ARG F 2 143 ? 7.410 -85.099 11.027 1.00 73.58 ? 143 ARG F CB 1 ATOM 10907 C CG . ARG F 2 143 ? 6.437 -85.882 10.144 1.00 77.19 ? 143 ARG F CG 1 ATOM 10908 C CD . ARG F 2 143 ? 5.141 -85.129 9.910 1.00 78.77 ? 143 ARG F CD 1 ATOM 10909 N NE . ARG F 2 143 ? 4.385 -84.979 11.150 1.00 79.28 ? 143 ARG F NE 1 ATOM 10910 C CZ . ARG F 2 143 ? 3.311 -84.207 11.298 1.00 81.38 ? 143 ARG F CZ 1 ATOM 10911 N NH1 . ARG F 2 143 ? 2.845 -83.485 10.280 1.00 83.39 ? 143 ARG F NH1 1 ATOM 10912 N NH2 . ARG F 2 143 ? 2.706 -84.145 12.479 1.00 82.22 ? 143 ARG F NH2 1 ATOM 10913 N N . CYS F 2 144 ? 8.875 -82.166 11.980 1.00 66.69 ? 144 CYS F N 1 ATOM 10914 C CA . CYS F 2 144 ? 9.913 -81.547 12.796 1.00 65.72 ? 144 CYS F CA 1 ATOM 10915 C C . CYS F 2 144 ? 9.501 -81.626 14.262 1.00 65.39 ? 144 CYS F C 1 ATOM 10916 O O . CYS F 2 144 ? 8.614 -80.891 14.701 1.00 64.41 ? 144 CYS F O 1 ATOM 10917 C CB . CYS F 2 144 ? 10.111 -80.084 12.371 1.00 65.06 ? 144 CYS F CB 1 ATOM 10918 S SG . CYS F 2 144 ? 11.399 -79.203 13.286 1.00 65.72 ? 144 CYS F SG 1 ATOM 10919 N N . ASP F 2 145 ? 10.129 -82.521 15.020 1.00 66.92 ? 145 ASP F N 1 ATOM 10920 C CA . ASP F 2 145 ? 9.794 -82.671 16.441 1.00 67.92 ? 145 ASP F CA 1 ATOM 10921 C C . ASP F 2 145 ? 10.446 -81.561 17.277 1.00 68.25 ? 145 ASP F C 1 ATOM 10922 O O . ASP F 2 145 ? 11.109 -80.682 16.730 1.00 67.98 ? 145 ASP F O 1 ATOM 10923 C CB . ASP F 2 145 ? 10.162 -84.074 16.958 1.00 70.55 ? 145 ASP F CB 1 ATOM 10924 C CG . ASP F 2 145 ? 11.640 -84.226 17.273 1.00 73.51 ? 145 ASP F CG 1 ATOM 10925 O OD1 . ASP F 2 145 ? 12.487 -83.829 16.442 1.00 73.80 ? 145 ASP F OD1 1 ATOM 10926 O OD2 . ASP F 2 145 ? 11.952 -84.761 18.355 1.00 76.83 ? 145 ASP F OD2 1 ATOM 10927 N N . ASN F 2 146 ? 10.247 -81.602 18.594 1.00 70.11 ? 146 ASN F N 1 ATOM 10928 C CA . ASN F 2 146 ? 10.705 -80.527 19.490 1.00 71.35 ? 146 ASN F CA 1 ATOM 10929 C C . ASN F 2 146 ? 12.225 -80.291 19.530 1.00 74.32 ? 146 ASN F C 1 ATOM 10930 O O . ASN F 2 146 ? 12.666 -79.161 19.742 1.00 75.29 ? 146 ASN F O 1 ATOM 10931 C CB . ASN F 2 146 ? 10.179 -80.758 20.916 1.00 73.73 ? 146 ASN F CB 1 ATOM 10932 C CG . ASN F 2 146 ? 8.710 -80.388 21.074 1.00 72.40 ? 146 ASN F CG 1 ATOM 10933 O OD1 . ASN F 2 146 ? 8.148 -79.627 20.281 1.00 70.12 ? 146 ASN F OD1 1 ATOM 10934 N ND2 . ASN F 2 146 ? 8.084 -80.914 22.117 1.00 75.09 ? 146 ASN F ND2 1 ATOM 10935 N N . GLU F 2 147 ? 13.017 -81.346 19.343 1.00 77.09 ? 147 GLU F N 1 ATOM 10936 C CA . GLU F 2 147 ? 14.476 -81.204 19.233 1.00 81.20 ? 147 GLU F CA 1 ATOM 10937 C C . GLU F 2 147 ? 14.855 -80.567 17.891 1.00 79.16 ? 147 GLU F C 1 ATOM 10938 O O . GLU F 2 147 ? 15.774 -79.744 17.815 1.00 81.36 ? 147 GLU F O 1 ATOM 10939 C CB . GLU F 2 147 ? 15.165 -82.565 19.370 1.00 85.88 ? 147 GLU F CB 1 ATOM 10940 C CG . GLU F 2 147 ? 15.022 -83.204 20.741 1.00 90.01 ? 147 GLU F CG 1 ATOM 10941 C CD . GLU F 2 147 ? 15.634 -84.594 20.810 1.00 95.51 ? 147 GLU F CD 1 ATOM 10942 O OE1 . GLU F 2 147 ? 15.437 -85.393 19.865 1.00 94.04 ? 147 GLU F OE1 1 ATOM 10943 O OE2 . GLU F 2 147 ? 16.316 -84.893 21.814 1.00 102.39 ? 147 GLU F OE2 1 ATOM 10944 N N . CYS F 2 148 ? 14.147 -80.977 16.840 1.00 75.48 ? 148 CYS F N 1 ATOM 10945 C CA . CYS F 2 148 ? 14.285 -80.394 15.509 1.00 73.64 ? 148 CYS F CA 1 ATOM 10946 C C . CYS F 2 148 ? 13.918 -78.906 15.524 1.00 71.62 ? 148 CYS F C 1 ATOM 10947 O O . CYS F 2 148 ? 14.606 -78.078 14.923 1.00 72.30 ? 148 CYS F O 1 ATOM 10948 C CB . CYS F 2 148 ? 13.388 -81.152 14.524 1.00 71.08 ? 148 CYS F CB 1 ATOM 10949 S SG . CYS F 2 148 ? 13.077 -80.331 12.946 1.00 69.95 ? 148 CYS F SG 1 ATOM 10950 N N . MET F 2 149 ? 12.834 -78.582 16.224 1.00 69.46 ? 149 MET F N 1 ATOM 10951 C CA . MET F 2 149 ? 12.314 -77.216 16.273 1.00 68.46 ? 149 MET F CA 1 ATOM 10952 C C . MET F 2 149 ? 13.274 -76.286 17.025 1.00 71.74 ? 149 MET F C 1 ATOM 10953 O O . MET F 2 149 ? 13.488 -75.142 16.618 1.00 71.62 ? 149 MET F O 1 ATOM 10954 C CB . MET F 2 149 ? 10.921 -77.204 16.920 1.00 66.70 ? 149 MET F CB 1 ATOM 10955 C CG . MET F 2 149 ? 9.982 -76.157 16.343 1.00 65.18 ? 149 MET F CG 1 ATOM 10956 S SD . MET F 2 149 ? 9.418 -76.533 14.671 1.00 62.61 ? 149 MET F SD 1 ATOM 10957 C CE . MET F 2 149 ? 8.049 -77.625 15.025 1.00 62.95 ? 149 MET F CE 1 ATOM 10958 N N . GLU F 2 150 ? 13.847 -76.798 18.114 1.00 75.42 ? 150 GLU F N 1 ATOM 10959 C CA . GLU F 2 150 ? 14.933 -76.125 18.832 1.00 80.40 ? 150 GLU F CA 1 ATOM 10960 C C . GLU F 2 150 ? 16.164 -75.923 17.948 1.00 83.17 ? 150 GLU F C 1 ATOM 10961 O O . GLU F 2 150 ? 16.827 -74.894 18.039 1.00 86.12 ? 150 GLU F O 1 ATOM 10962 C CB . GLU F 2 150 ? 15.329 -76.929 20.074 1.00 84.84 ? 150 GLU F CB 1 ATOM 10963 C CG . GLU F 2 150 ? 14.312 -76.846 21.203 1.00 84.63 ? 150 GLU F CG 1 ATOM 10964 C CD . GLU F 2 150 ? 14.484 -77.928 22.256 1.00 88.65 ? 150 GLU F CD 1 ATOM 10965 O OE1 . GLU F 2 150 ? 15.212 -78.916 22.012 1.00 91.24 ? 150 GLU F OE1 1 ATOM 10966 O OE2 . GLU F 2 150 ? 13.878 -77.790 23.338 1.00 90.23 ? 150 GLU F OE2 1 ATOM 10967 N N . SER F 2 151 ? 16.461 -76.909 17.103 1.00 82.97 ? 151 SER F N 1 ATOM 10968 C CA . SER F 2 151 ? 17.574 -76.826 16.151 1.00 86.36 ? 151 SER F CA 1 ATOM 10969 C C . SER F 2 151 ? 17.423 -75.632 15.198 1.00 84.76 ? 151 SER F C 1 ATOM 10970 O O . SER F 2 151 ? 18.405 -74.964 14.862 1.00 88.65 ? 151 SER F O 1 ATOM 10971 C CB . SER F 2 151 ? 17.676 -78.122 15.338 1.00 86.16 ? 151 SER F CB 1 ATOM 10972 O OG . SER F 2 151 ? 19.019 -78.410 15.022 1.00 92.67 ? 151 SER F OG 1 ATOM 10973 N N . VAL F 2 152 ? 16.187 -75.378 14.771 1.00 79.75 ? 152 VAL F N 1 ATOM 10974 C CA . VAL F 2 152 ? 15.860 -74.227 13.928 1.00 78.80 ? 152 VAL F CA 1 ATOM 10975 C C . VAL F 2 152 ? 16.038 -72.922 14.719 1.00 80.98 ? 152 VAL F C 1 ATOM 10976 O O . VAL F 2 152 ? 16.500 -71.909 14.180 1.00 82.79 ? 152 VAL F O 1 ATOM 10977 C CB . VAL F 2 152 ? 14.418 -74.342 13.379 1.00 74.21 ? 152 VAL F CB 1 ATOM 10978 C CG1 . VAL F 2 152 ? 14.021 -73.097 12.597 1.00 74.27 ? 152 VAL F CG1 1 ATOM 10979 C CG2 . VAL F 2 152 ? 14.287 -75.582 12.503 1.00 73.37 ? 152 VAL F CG2 1 ATOM 10980 N N . ARG F 2 153 ? 15.674 -72.968 16.000 1.00 81.15 ? 153 ARG F N 1 ATOM 10981 C CA . ARG F 2 153 ? 15.888 -71.854 16.934 1.00 84.20 ? 153 ARG F CA 1 ATOM 10982 C C . ARG F 2 153 ? 17.355 -71.712 17.373 1.00 90.98 ? 153 ARG F C 1 ATOM 10983 O O . ARG F 2 153 ? 17.818 -70.610 17.676 1.00 94.34 ? 153 ARG F O 1 ATOM 10984 C CB . ARG F 2 153 ? 14.985 -72.033 18.164 1.00 82.58 ? 153 ARG F CB 1 ATOM 10985 C CG . ARG F 2 153 ? 13.559 -71.547 17.949 1.00 78.77 ? 153 ARG F CG 1 ATOM 10986 C CD . ARG F 2 153 ? 12.512 -72.472 18.544 1.00 76.50 ? 153 ARG F CD 1 ATOM 10987 N NE . ARG F 2 153 ? 12.701 -72.708 19.975 1.00 79.51 ? 153 ARG F NE 1 ATOM 10988 C CZ . ARG F 2 153 ? 12.014 -73.597 20.694 1.00 79.10 ? 153 ARG F CZ 1 ATOM 10989 N NH1 . ARG F 2 153 ? 11.076 -74.356 20.128 1.00 75.74 ? 153 ARG F NH1 1 ATOM 10990 N NH2 . ARG F 2 153 ? 12.269 -73.734 21.992 1.00 82.66 ? 153 ARG F NH2 1 ATOM 10991 N N . ASN F 2 154 ? 18.074 -72.833 17.407 1.00 93.93 ? 154 ASN F N 1 ATOM 10992 C CA . ASN F 2 154 ? 19.473 -72.870 17.835 1.00 101.75 ? 154 ASN F CA 1 ATOM 10993 C C . ASN F 2 154 ? 20.419 -72.309 16.775 1.00 105.78 ? 154 ASN F C 1 ATOM 10994 O O . ASN F 2 154 ? 21.377 -71.612 17.105 1.00 112.31 ? 154 ASN F O 1 ATOM 10995 C CB . ASN F 2 154 ? 19.872 -74.311 18.181 1.00 104.08 ? 154 ASN F CB 1 ATOM 10996 C CG . ASN F 2 154 ? 21.293 -74.422 18.700 1.00 113.73 ? 154 ASN F CG 1 ATOM 10997 O OD1 . ASN F 2 154 ? 21.772 -73.552 19.429 1.00 118.45 ? 154 ASN F OD1 1 ATOM 10998 N ND2 . ASN F 2 154 ? 21.974 -75.507 18.334 1.00 117.54 ? 154 ASN F ND2 1 ATOM 10999 N N . GLY F 2 155 ? 20.147 -72.623 15.508 1.00 102.87 ? 155 GLY F N 1 ATOM 11000 C CA . GLY F 2 155 ? 20.983 -72.177 14.391 1.00 107.39 ? 155 GLY F CA 1 ATOM 11001 C C . GLY F 2 155 ? 21.653 -73.331 13.666 1.00 110.78 ? 155 GLY F C 1 ATOM 11002 O O . GLY F 2 155 ? 21.853 -73.271 12.451 1.00 111.44 ? 155 GLY F O 1 ATOM 11003 N N . THR F 2 156 ? 22.016 -74.373 14.414 1.00 114.01 ? 156 THR F N 1 ATOM 11004 C CA . THR F 2 156 ? 22.563 -75.596 13.833 1.00 117.62 ? 156 THR F CA 1 ATOM 11005 C C . THR F 2 156 ? 21.418 -76.444 13.294 1.00 110.65 ? 156 THR F C 1 ATOM 11006 O O . THR F 2 156 ? 20.513 -76.806 14.043 1.00 105.90 ? 156 THR F O 1 ATOM 11007 C CB . THR F 2 156 ? 23.343 -76.420 14.875 1.00 124.05 ? 156 THR F CB 1 ATOM 11008 N N . TYR F 2 157 ? 21.462 -76.751 11.997 1.00 111.25 ? 157 TYR F N 1 ATOM 11009 C CA . TYR F 2 157 ? 20.392 -77.494 11.329 1.00 105.67 ? 157 TYR F CA 1 ATOM 11010 C C . TYR F 2 157 ? 20.905 -78.136 10.039 1.00 109.39 ? 157 TYR F C 1 ATOM 11011 O O . TYR F 2 157 ? 20.716 -79.333 9.805 1.00 109.32 ? 157 TYR F O 1 ATOM 11012 C CB . TYR F 2 157 ? 19.218 -76.554 11.029 1.00 99.73 ? 157 TYR F CB 1 ATOM 11013 C CG . TYR F 2 157 ? 18.025 -77.222 10.387 1.00 94.93 ? 157 TYR F CG 1 ATOM 11014 C CD1 . TYR F 2 157 ? 17.919 -77.324 9.002 1.00 95.83 ? 157 TYR F CD1 1 ATOM 11015 C CD2 . TYR F 2 157 ? 16.998 -77.749 11.166 1.00 90.73 ? 157 TYR F CD2 1 ATOM 11016 C CE1 . TYR F 2 157 ? 16.829 -77.942 8.410 1.00 92.69 ? 157 TYR F CE1 1 ATOM 11017 C CE2 . TYR F 2 157 ? 15.903 -78.369 10.584 1.00 87.38 ? 157 TYR F CE2 1 ATOM 11018 C CZ . TYR F 2 157 ? 15.822 -78.465 9.207 1.00 88.37 ? 157 TYR F CZ 1 ATOM 11019 O OH . TYR F 2 157 ? 14.736 -79.083 8.629 1.00 85.11 ? 157 TYR F OH 1 HETATM 11020 C C1 . NAG G 3 . ? 7.451 17.610 41.597 1.00 33.59 ? 1320 NAG A C1 1 HETATM 11021 C C2 . NAG G 3 . ? 8.057 17.200 42.949 1.00 35.36 ? 1320 NAG A C2 1 HETATM 11022 C C3 . NAG G 3 . ? 7.089 16.387 43.816 1.00 37.69 ? 1320 NAG A C3 1 HETATM 11023 C C4 . NAG G 3 . ? 5.701 17.028 43.862 1.00 38.49 ? 1320 NAG A C4 1 HETATM 11024 C C5 . NAG G 3 . ? 5.193 17.225 42.436 1.00 39.63 ? 1320 NAG A C5 1 HETATM 11025 C C6 . NAG G 3 . ? 3.812 17.881 42.423 1.00 41.05 ? 1320 NAG A C6 1 HETATM 11026 C C7 . NAG G 3 . ? 10.472 16.759 43.154 1.00 32.52 ? 1320 NAG A C7 1 HETATM 11027 C C8 . NAG G 3 . ? 11.550 15.724 43.014 1.00 32.37 ? 1320 NAG A C8 1 HETATM 11028 N N2 . NAG G 3 . ? 9.239 16.367 42.835 1.00 33.25 ? 1320 NAG A N2 1 HETATM 11029 O O3 . NAG G 3 . ? 7.656 16.194 45.105 1.00 38.22 ? 1320 NAG A O3 1 HETATM 11030 O O4 . NAG G 3 . ? 4.808 16.201 44.573 1.00 41.66 ? 1320 NAG A O4 1 HETATM 11031 O O5 . NAG G 3 . ? 6.094 18.043 41.709 1.00 34.26 ? 1320 NAG A O5 1 HETATM 11032 O O6 . NAG G 3 . ? 3.933 19.218 42.872 1.00 43.09 ? 1320 NAG A O6 1 HETATM 11033 O O7 . NAG G 3 . ? 10.774 17.886 43.530 1.00 31.22 ? 1320 NAG A O7 1 HETATM 11034 C C1 . SIA H 4 . ? 30.094 31.438 14.555 1.00 63.64 ? 1321 SIA A C1 1 HETATM 11035 C C2 . SIA H 4 . ? 30.831 32.608 15.204 1.00 62.65 ? 1321 SIA A C2 1 HETATM 11036 C C3 . SIA H 4 . ? 29.874 33.796 15.342 1.00 59.38 ? 1321 SIA A C3 1 HETATM 11037 C C4 . SIA H 4 . ? 28.785 33.568 16.384 1.00 59.25 ? 1321 SIA A C4 1 HETATM 11038 C C5 . SIA H 4 . ? 29.397 33.123 17.713 1.00 59.11 ? 1321 SIA A C5 1 HETATM 11039 C C6 . SIA H 4 . ? 30.428 31.998 17.539 1.00 58.88 ? 1321 SIA A C6 1 HETATM 11040 C C7 . SIA H 4 . ? 31.189 31.743 18.842 1.00 56.14 ? 1321 SIA A C7 1 HETATM 11041 C C8 . SIA H 4 . ? 32.150 30.554 18.727 1.00 53.33 ? 1321 SIA A C8 1 HETATM 11042 C C9 . SIA H 4 . ? 32.213 29.802 20.048 1.00 52.02 ? 1321 SIA A C9 1 HETATM 11043 C C10 . SIA H 4 . ? 27.648 33.225 19.435 1.00 58.33 ? 1321 SIA A C10 1 HETATM 11044 C C11 . SIA H 4 . ? 26.598 32.464 20.182 1.00 56.28 ? 1321 SIA A C11 1 HETATM 11045 N N5 . SIA H 4 . ? 28.328 32.536 18.524 1.00 57.63 ? 1321 SIA A N5 1 HETATM 11046 O O1A . SIA H 4 . ? 29.526 31.644 13.457 1.00 62.85 ? 1321 SIA A O1A 1 HETATM 11047 O O1B . SIA H 4 . ? 30.058 30.310 15.115 1.00 59.00 ? 1321 SIA A O1B 1 HETATM 11048 O O4 . SIA H 4 . ? 28.032 34.779 16.559 1.00 57.96 ? 1321 SIA A O4 1 HETATM 11049 O O6 . SIA H 4 . ? 31.379 32.272 16.494 1.00 60.64 ? 1321 SIA A O6 1 HETATM 11050 O O7 . SIA H 4 . ? 31.908 32.928 19.220 1.00 56.95 ? 1321 SIA A O7 1 HETATM 11051 O O8 . SIA H 4 . ? 31.737 29.642 17.702 1.00 51.72 ? 1321 SIA A O8 1 HETATM 11052 O O9 . SIA H 4 . ? 33.120 28.689 19.981 1.00 52.26 ? 1321 SIA A O9 1 HETATM 11053 O O10 . SIA H 4 . ? 27.853 34.404 19.663 1.00 63.71 ? 1321 SIA A O10 1 HETATM 11054 C C1 . GAL I 5 . ? 32.435 32.606 10.373 1.00 78.65 ? 1322 GAL A C1 1 HETATM 11055 C C2 . GAL I 5 . ? 33.432 31.606 9.754 1.00 77.63 ? 1322 GAL A C2 1 HETATM 11056 C C3 . GAL I 5 . ? 33.861 30.496 10.715 1.00 75.98 ? 1322 GAL A C3 1 HETATM 11057 C C4 . GAL I 5 . ? 34.154 31.077 12.090 1.00 74.49 ? 1322 GAL A C4 1 HETATM 11058 C C5 . GAL I 5 . ? 32.918 31.832 12.569 1.00 74.17 ? 1322 GAL A C5 1 HETATM 11059 C C6 . GAL I 5 . ? 32.979 32.215 14.052 1.00 70.78 ? 1322 GAL A C6 1 HETATM 11060 O O1 . GAL I 5 . ? 32.377 33.784 9.567 1.00 77.90 ? 1322 GAL A O1 1 HETATM 11061 O O2 . GAL I 5 . ? 32.850 30.977 8.605 1.00 75.77 ? 1322 GAL A O2 1 HETATM 11062 O O3 . GAL I 5 . ? 35.013 29.821 10.192 1.00 73.42 ? 1322 GAL A O3 1 HETATM 11063 O O4 . GAL I 5 . ? 35.271 31.969 11.988 1.00 75.85 ? 1322 GAL A O4 1 HETATM 11064 O O5 . GAL I 5 . ? 32.784 32.977 11.719 1.00 75.25 ? 1322 GAL A O5 1 HETATM 11065 O O6 . GAL I 5 . ? 31.888 33.093 14.362 1.00 66.83 ? 1322 GAL A O6 1 HETATM 11066 P P . PO4 J 6 . ? 33.086 18.347 30.831 1.00 76.94 ? 1323 PO4 A P 1 HETATM 11067 O O1 . PO4 J 6 . ? 34.577 18.578 30.774 1.00 75.27 ? 1323 PO4 A O1 1 HETATM 11068 O O2 . PO4 J 6 . ? 32.695 17.226 29.891 1.00 71.76 ? 1323 PO4 A O2 1 HETATM 11069 O O3 . PO4 J 6 . ? 32.404 19.632 30.428 1.00 74.56 ? 1323 PO4 A O3 1 HETATM 11070 O O4 . PO4 J 6 . ? 32.684 17.972 32.239 1.00 73.81 ? 1323 PO4 A O4 1 HETATM 11071 P P . PO4 K 6 . ? 17.314 33.869 34.216 1.00 65.87 ? 1324 PO4 A P 1 HETATM 11072 O O1 . PO4 K 6 . ? 17.755 34.003 32.770 1.00 61.13 ? 1324 PO4 A O1 1 HETATM 11073 O O2 . PO4 K 6 . ? 17.547 32.463 34.733 1.00 68.18 ? 1324 PO4 A O2 1 HETATM 11074 O O3 . PO4 K 6 . ? 15.842 34.199 34.373 1.00 60.68 ? 1324 PO4 A O3 1 HETATM 11075 O O4 . PO4 K 6 . ? 18.156 34.832 35.016 1.00 66.86 ? 1324 PO4 A O4 1 HETATM 11076 P P . PO4 L 6 . ? 21.006 0.770 17.793 1.00 70.27 ? 1325 PO4 A P 1 HETATM 11077 O O1 . PO4 L 6 . ? 22.135 1.044 18.762 1.00 70.40 ? 1325 PO4 A O1 1 HETATM 11078 O O2 . PO4 L 6 . ? 21.082 -0.633 17.237 1.00 68.15 ? 1325 PO4 A O2 1 HETATM 11079 O O3 . PO4 L 6 . ? 21.124 1.753 16.647 1.00 65.48 ? 1325 PO4 A O3 1 HETATM 11080 O O4 . PO4 L 6 . ? 19.701 0.912 18.544 1.00 67.85 ? 1325 PO4 A O4 1 HETATM 11081 C C1 . NAG M 3 . ? 47.414 20.712 7.844 1.00 38.11 ? 1320 NAG C C1 1 HETATM 11082 C C2 . NAG M 3 . ? 46.130 21.533 7.985 1.00 40.80 ? 1320 NAG C C2 1 HETATM 11083 C C3 . NAG M 3 . ? 45.371 21.671 6.666 1.00 42.55 ? 1320 NAG C C3 1 HETATM 11084 C C4 . NAG M 3 . ? 46.296 22.150 5.547 1.00 44.32 ? 1320 NAG C C4 1 HETATM 11085 C C5 . NAG M 3 . ? 47.462 21.158 5.470 1.00 43.84 ? 1320 NAG C C5 1 HETATM 11086 C C6 . NAG M 3 . ? 48.463 21.500 4.377 1.00 44.91 ? 1320 NAG C C6 1 HETATM 11087 C C7 . NAG M 3 . ? 44.811 21.534 10.078 1.00 38.88 ? 1320 NAG C C7 1 HETATM 11088 C C8 . NAG M 3 . ? 43.868 20.753 10.952 1.00 37.54 ? 1320 NAG C C8 1 HETATM 11089 N N2 . NAG M 3 . ? 45.229 20.929 8.955 1.00 40.10 ? 1320 NAG C N2 1 HETATM 11090 O O3 . NAG M 3 . ? 44.280 22.539 6.863 1.00 44.95 ? 1320 NAG C O3 1 HETATM 11091 O O4 . NAG M 3 . ? 45.613 22.254 4.308 1.00 42.47 ? 1320 NAG C O4 1 HETATM 11092 O O5 . NAG M 3 . ? 48.155 21.130 6.705 1.00 41.43 ? 1320 NAG C O5 1 HETATM 11093 O O6 . NAG M 3 . ? 49.139 22.683 4.736 1.00 48.01 ? 1320 NAG C O6 1 HETATM 11094 O O7 . NAG M 3 . ? 45.162 22.665 10.427 1.00 38.15 ? 1320 NAG C O7 1 HETATM 11095 C C1 . SIA N 4 . ? 64.132 8.421 39.630 1.00 42.39 ? 1321 SIA C C1 1 HETATM 11096 C C2 . SIA N 4 . ? 64.333 9.667 40.469 1.00 40.92 ? 1321 SIA C C2 1 HETATM 11097 C C3 . SIA N 4 . ? 65.538 10.483 39.986 1.00 38.42 ? 1321 SIA C C3 1 HETATM 11098 C C4 . SIA N 4 . ? 65.269 11.204 38.671 1.00 38.45 ? 1321 SIA C C4 1 HETATM 11099 C C5 . SIA N 4 . ? 63.959 11.990 38.765 1.00 37.19 ? 1321 SIA C C5 1 HETATM 11100 C C6 . SIA N 4 . ? 62.808 11.115 39.228 1.00 36.95 ? 1321 SIA C C6 1 HETATM 11101 C C7 . SIA N 4 . ? 61.521 11.904 39.465 1.00 37.31 ? 1321 SIA C C7 1 HETATM 11102 C C8 . SIA N 4 . ? 60.471 11.013 40.136 1.00 35.85 ? 1321 SIA C C8 1 HETATM 11103 C C9 . SIA N 4 . ? 59.066 11.569 39.965 1.00 36.12 ? 1321 SIA C C9 1 HETATM 11104 C C10 . SIA N 4 . ? 63.176 13.639 37.190 1.00 36.76 ? 1321 SIA C C10 1 HETATM 11105 C C11 . SIA N 4 . ? 62.828 13.945 35.764 1.00 37.22 ? 1321 SIA C C11 1 HETATM 11106 N N5 . SIA N 4 . ? 63.596 12.407 37.423 1.00 34.91 ? 1321 SIA C N5 1 HETATM 11107 O O1A . SIA N 4 . ? 65.121 7.694 39.375 1.00 44.71 ? 1321 SIA C O1A 1 HETATM 11108 O O1B . SIA N 4 . ? 62.977 8.135 39.235 1.00 41.14 ? 1321 SIA C O1B 1 HETATM 11109 O O4 . SIA N 4 . ? 66.340 12.108 38.351 1.00 36.69 ? 1321 SIA C O4 1 HETATM 11110 O O6 . SIA N 4 . ? 63.145 10.474 40.456 1.00 38.80 ? 1321 SIA C O6 1 HETATM 11111 O O7 . SIA N 4 . ? 61.789 13.079 40.252 1.00 35.87 ? 1321 SIA C O7 1 HETATM 11112 O O8 . SIA N 4 . ? 60.482 9.701 39.559 1.00 34.78 ? 1321 SIA C O8 1 HETATM 11113 O O9 . SIA N 4 . ? 58.108 10.687 40.569 1.00 36.16 ? 1321 SIA C O9 1 HETATM 11114 O O10 . SIA N 4 . ? 63.078 14.471 38.075 1.00 36.90 ? 1321 SIA C O10 1 HETATM 11115 C C1 . GAL O 5 . ? 66.194 6.060 43.295 1.00 62.52 ? 1322 GAL C C1 1 HETATM 11116 C C2 . GAL O 5 . ? 65.528 4.971 44.142 1.00 60.36 ? 1322 GAL C C2 1 HETATM 11117 C C3 . GAL O 5 . ? 63.994 4.932 44.019 1.00 58.30 ? 1322 GAL C C3 1 HETATM 11118 C C4 . GAL O 5 . ? 63.360 6.325 43.852 1.00 56.15 ? 1322 GAL C C4 1 HETATM 11119 C C5 . GAL O 5 . ? 64.129 7.095 42.787 1.00 54.85 ? 1322 GAL C C5 1 HETATM 11120 C C6 . GAL O 5 . ? 63.558 8.470 42.441 1.00 51.36 ? 1322 GAL C C6 1 HETATM 11121 O O2 . GAL O 5 . ? 66.037 3.703 43.712 1.00 58.65 ? 1322 GAL C O2 1 HETATM 11122 O O3 . GAL O 5 . ? 63.431 4.245 45.157 1.00 57.64 ? 1322 GAL C O3 1 HETATM 11123 O O4 . GAL O 5 . ? 63.365 7.073 45.078 1.00 51.63 ? 1322 GAL C O4 1 HETATM 11124 O O5 . GAL O 5 . ? 65.428 7.258 43.320 1.00 61.04 ? 1322 GAL C O5 1 HETATM 11125 O O6 . GAL O 5 . ? 64.580 9.272 41.825 1.00 44.70 ? 1322 GAL C O6 1 HETATM 11126 C C1 . NAG P 3 . ? 70.129 9.362 42.220 1.00 76.08 ? 1323 NAG C C1 1 HETATM 11127 C C2 . NAG P 3 . ? 68.695 9.793 42.566 1.00 75.95 ? 1323 NAG C C2 1 HETATM 11128 C C3 . NAG P 3 . ? 68.075 8.806 43.563 1.00 76.00 ? 1323 NAG C C3 1 HETATM 11129 C C4 . NAG P 3 . ? 68.123 7.408 42.933 1.00 74.35 ? 1323 NAG C C4 1 HETATM 11130 C C5 . NAG P 3 . ? 69.587 7.066 42.637 1.00 75.29 ? 1323 NAG C C5 1 HETATM 11131 C C6 . NAG P 3 . ? 69.776 5.651 42.081 1.00 74.57 ? 1323 NAG C C6 1 HETATM 11132 C C7 . NAG P 3 . ? 69.259 11.793 44.124 1.00 76.33 ? 1323 NAG C C7 1 HETATM 11133 C C8 . NAG P 3 . ? 70.295 11.093 44.965 1.00 75.73 ? 1323 NAG C C8 1 HETATM 11134 N N2 . NAG P 3 . ? 68.626 11.165 43.113 1.00 76.80 ? 1323 NAG C N2 1 HETATM 11135 O O1 . NAG P 3 . ? 70.693 10.230 41.239 1.00 76.53 ? 1323 NAG C O1 1 HETATM 11136 O O3 . NAG P 3 . ? 66.740 9.223 43.896 1.00 75.57 ? 1323 NAG C O3 1 HETATM 11137 O O4 . NAG P 3 . ? 67.501 6.406 43.765 1.00 68.71 ? 1323 NAG C O4 1 HETATM 11138 O O5 . NAG P 3 . ? 70.099 8.028 41.703 1.00 75.28 ? 1323 NAG C O5 1 HETATM 11139 O O6 . NAG P 3 . ? 70.648 4.903 42.938 1.00 71.87 ? 1323 NAG C O6 1 HETATM 11140 O O7 . NAG P 3 . ? 68.989 12.964 44.363 1.00 72.57 ? 1323 NAG C O7 1 HETATM 11141 P P . PO4 Q 6 . ? 59.474 25.545 23.783 1.00 69.02 ? 1324 PO4 C P 1 HETATM 11142 O O1 . PO4 Q 6 . ? 60.398 25.479 22.582 1.00 66.60 ? 1324 PO4 C O1 1 HETATM 11143 O O2 . PO4 Q 6 . ? 58.109 25.012 23.404 1.00 72.82 ? 1324 PO4 C O2 1 HETATM 11144 O O3 . PO4 Q 6 . ? 59.346 26.979 24.246 1.00 67.42 ? 1324 PO4 C O3 1 HETATM 11145 O O4 . PO4 Q 6 . ? 60.039 24.714 24.915 1.00 65.02 ? 1324 PO4 C O4 1 HETATM 11146 C C1 . NAG R 3 . ? 54.226 -3.924 53.539 1.00 39.77 ? 1320 NAG E C1 1 HETATM 11147 C C2 . NAG R 3 . ? 55.127 -3.158 52.583 1.00 42.10 ? 1320 NAG E C2 1 HETATM 11148 C C3 . NAG R 3 . ? 56.266 -4.002 52.024 1.00 45.47 ? 1320 NAG E C3 1 HETATM 11149 C C4 . NAG R 3 . ? 56.983 -4.770 53.127 1.00 48.52 ? 1320 NAG E C4 1 HETATM 11150 C C5 . NAG R 3 . ? 55.967 -5.543 53.974 1.00 47.32 ? 1320 NAG E C5 1 HETATM 11151 C C6 . NAG R 3 . ? 56.658 -6.204 55.155 1.00 48.67 ? 1320 NAG E C6 1 HETATM 11152 C C7 . NAG R 3 . ? 54.330 -1.398 51.089 1.00 41.17 ? 1320 NAG E C7 1 HETATM 11153 C C8 . NAG R 3 . ? 53.574 -1.071 49.837 1.00 40.16 ? 1320 NAG E C8 1 HETATM 11154 N N2 . NAG R 3 . ? 54.398 -2.687 51.420 1.00 42.32 ? 1320 NAG E N2 1 HETATM 11155 O O3 . NAG R 3 . ? 57.143 -3.121 51.361 1.00 45.74 ? 1320 NAG E O3 1 HETATM 11156 O O4 . NAG R 3 . ? 57.929 -5.663 52.570 1.00 52.86 ? 1320 NAG E O4 1 HETATM 11157 O O5 . NAG R 3 . ? 54.977 -4.673 54.485 1.00 41.75 ? 1320 NAG E O5 1 HETATM 11158 O O6 . NAG R 3 . ? 57.366 -5.213 55.877 1.00 51.97 ? 1320 NAG E O6 1 HETATM 11159 O O7 . NAG R 3 . ? 54.841 -0.497 51.754 1.00 40.27 ? 1320 NAG E O7 1 HETATM 11160 C C1 . SIA S 4 . ? 20.397 13.664 57.939 1.00 32.14 ? 1321 SIA E C1 1 HETATM 11161 C C2 . SIA S 4 . ? 20.752 15.100 58.340 1.00 31.74 ? 1321 SIA E C2 1 HETATM 11162 C C3 . SIA S 4 . ? 21.112 15.156 59.827 1.00 30.24 ? 1321 SIA E C3 1 HETATM 11163 C C4 . SIA S 4 . ? 22.480 14.558 60.123 1.00 30.10 ? 1321 SIA E C4 1 HETATM 11164 C C5 . SIA S 4 . ? 23.543 15.132 59.183 1.00 28.70 ? 1321 SIA E C5 1 HETATM 11165 C C6 . SIA S 4 . ? 23.098 15.004 57.731 1.00 29.44 ? 1321 SIA E C6 1 HETATM 11166 C C7 . SIA S 4 . ? 24.062 15.612 56.729 1.00 28.75 ? 1321 SIA E C7 1 HETATM 11167 C C8 . SIA S 4 . ? 23.478 15.563 55.318 1.00 28.01 ? 1321 SIA E C8 1 HETATM 11168 C C9 . SIA S 4 . ? 24.537 15.905 54.294 1.00 26.70 ? 1321 SIA E C9 1 HETATM 11169 C C10 . SIA S 4 . ? 25.957 14.792 59.262 1.00 28.03 ? 1321 SIA E C10 1 HETATM 11170 C C11 . SIA S 4 . ? 27.078 13.811 59.431 1.00 28.39 ? 1321 SIA E C11 1 HETATM 11171 N N5 . SIA S 4 . ? 24.719 14.295 59.331 1.00 27.12 ? 1321 SIA E N5 1 HETATM 11172 O O1A . SIA S 4 . ? 19.642 12.978 58.670 1.00 31.18 ? 1321 SIA E O1A 1 HETATM 11173 O O1B . SIA S 4 . ? 20.865 13.190 56.879 1.00 29.27 ? 1321 SIA E O1B 1 HETATM 11174 O O4 . SIA S 4 . ? 22.847 14.814 61.495 1.00 31.04 ? 1321 SIA E O4 1 HETATM 11175 O O6 . SIA S 4 . ? 21.820 15.636 57.545 1.00 30.46 ? 1321 SIA E O6 1 HETATM 11176 O O7 . SIA S 4 . ? 24.325 16.959 57.136 1.00 30.79 ? 1321 SIA E O7 1 HETATM 11177 O O8 . SIA S 4 . ? 22.973 14.254 55.004 1.00 28.71 ? 1321 SIA E O8 1 HETATM 11178 O O9 . SIA S 4 . ? 23.957 15.835 52.982 1.00 24.18 ? 1321 SIA E O9 1 HETATM 11179 O O10 . SIA S 4 . ? 26.189 15.963 59.054 1.00 27.52 ? 1321 SIA E O10 1 HETATM 11180 C C1 . GAL T 5 . ? 15.909 15.360 58.393 1.00 55.29 ? 1322 GAL E C1 1 HETATM 11181 C C2 . GAL T 5 . ? 14.909 15.314 57.238 1.00 53.67 ? 1322 GAL E C2 1 HETATM 11182 C C3 . GAL T 5 . ? 15.589 14.853 55.936 1.00 49.70 ? 1322 GAL E C3 1 HETATM 11183 C C4 . GAL T 5 . ? 16.907 15.595 55.685 1.00 48.65 ? 1322 GAL E C4 1 HETATM 11184 C C5 . GAL T 5 . ? 17.736 15.521 56.956 1.00 46.88 ? 1322 GAL E C5 1 HETATM 11185 C C6 . GAL T 5 . ? 19.125 16.126 56.856 1.00 40.87 ? 1322 GAL E C6 1 HETATM 11186 O O2 . GAL T 5 . ? 13.842 14.438 57.624 1.00 52.05 ? 1322 GAL E O2 1 HETATM 11187 O O3 . GAL T 5 . ? 14.728 15.032 54.813 1.00 43.96 ? 1322 GAL E O3 1 HETATM 11188 O O4 . GAL T 5 . ? 16.694 16.967 55.323 1.00 49.39 ? 1322 GAL E O4 1 HETATM 11189 O O5 . GAL T 5 . ? 17.007 16.178 57.985 1.00 51.05 ? 1322 GAL E O5 1 HETATM 11190 O O6 . GAL T 5 . ? 19.671 16.003 58.166 1.00 33.83 ? 1322 GAL E O6 1 HETATM 11191 C C1 . NAG U 3 . ? 16.341 15.633 63.666 1.00 68.57 ? 1323 NAG E C1 1 HETATM 11192 C C2 . NAG U 3 . ? 17.469 15.654 62.627 1.00 67.99 ? 1323 NAG E C2 1 HETATM 11193 C C3 . NAG U 3 . ? 16.971 16.259 61.316 1.00 66.68 ? 1323 NAG E C3 1 HETATM 11194 C C4 . NAG U 3 . ? 15.818 15.395 60.807 1.00 65.67 ? 1323 NAG E C4 1 HETATM 11195 C C5 . NAG U 3 . ? 14.695 15.344 61.850 1.00 63.69 ? 1323 NAG E C5 1 HETATM 11196 C C6 . NAG U 3 . ? 13.614 14.344 61.433 1.00 61.73 ? 1323 NAG E C6 1 HETATM 11197 C C7 . NAG U 3 . ? 18.635 17.739 63.448 1.00 70.53 ? 1323 NAG E C7 1 HETATM 11198 C C8 . NAG U 3 . ? 19.979 18.246 63.882 1.00 69.91 ? 1323 NAG E C8 1 HETATM 11199 N N2 . NAG U 3 . ? 18.617 16.443 63.103 1.00 69.08 ? 1323 NAG E N2 1 HETATM 11200 O O1 . NAG U 3 . ? 16.791 14.907 64.805 1.00 67.35 ? 1323 NAG E O1 1 HETATM 11201 O O3 . NAG U 3 . ? 18.046 16.325 60.373 1.00 65.18 ? 1323 NAG E O3 1 HETATM 11202 O O4 . NAG U 3 . ? 15.298 15.908 59.569 1.00 62.41 ? 1323 NAG E O4 1 HETATM 11203 O O5 . NAG U 3 . ? 15.171 14.971 63.156 1.00 69.28 ? 1323 NAG E O5 1 HETATM 11204 O O6 . NAG U 3 . ? 14.124 13.003 61.420 1.00 55.27 ? 1323 NAG E O6 1 HETATM 11205 O O7 . NAG U 3 . ? 17.659 18.477 63.432 1.00 69.04 ? 1323 NAG E O7 1 HETATM 11206 P P . PO4 V 6 . ? 43.727 11.975 63.027 1.00 72.53 ? 1324 PO4 E P 1 HETATM 11207 O O1 . PO4 V 6 . ? 43.698 10.463 62.920 1.00 73.28 ? 1324 PO4 E O1 1 HETATM 11208 O O2 . PO4 V 6 . ? 44.108 12.601 61.700 1.00 70.68 ? 1324 PO4 E O2 1 HETATM 11209 O O3 . PO4 V 6 . ? 44.758 12.357 64.064 1.00 72.97 ? 1324 PO4 E O3 1 HETATM 11210 O O4 . PO4 V 6 . ? 42.353 12.476 63.436 1.00 67.95 ? 1324 PO4 E O4 1 HETATM 11211 O O . HOH W 7 . ? 6.796 -53.211 -14.116 1.00 84.86 ? 2001 HOH A O 1 HETATM 11212 O O . HOH W 7 . ? 17.831 -29.879 -2.568 1.00 48.21 ? 2002 HOH A O 1 HETATM 11213 O O . HOH W 7 . ? 20.632 -26.714 -4.650 1.00 45.76 ? 2003 HOH A O 1 HETATM 11214 O O . HOH W 7 . ? 24.233 9.722 2.481 1.00 48.33 ? 2004 HOH A O 1 HETATM 11215 O O . HOH W 7 . ? 24.063 -31.539 -13.998 1.00 52.15 ? 2005 HOH A O 1 HETATM 11216 O O . HOH W 7 . ? 25.825 -29.024 -10.275 1.00 46.62 ? 2006 HOH A O 1 HETATM 11217 O O . HOH W 7 . ? 19.067 -36.566 -12.857 1.00 47.01 ? 2007 HOH A O 1 HETATM 11218 O O . HOH W 7 . ? 5.962 -30.770 -10.765 1.00 50.50 ? 2008 HOH A O 1 HETATM 11219 O O . HOH W 7 . ? 5.949 -29.539 -7.298 1.00 63.35 ? 2009 HOH A O 1 HETATM 11220 O O . HOH W 7 . ? 5.942 -30.167 -3.942 1.00 63.16 ? 2010 HOH A O 1 HETATM 11221 O O . HOH W 7 . ? 7.936 -24.560 -4.184 1.00 53.82 ? 2011 HOH A O 1 HETATM 11222 O O . HOH W 7 . ? 15.814 -22.670 -2.750 1.00 57.84 ? 2012 HOH A O 1 HETATM 11223 O O . HOH W 7 . ? 10.879 -22.038 -7.208 1.00 49.48 ? 2013 HOH A O 1 HETATM 11224 O O . HOH W 7 . ? 32.599 4.835 28.712 1.00 41.98 ? 2014 HOH A O 1 HETATM 11225 O O . HOH W 7 . ? 29.259 -0.812 27.540 1.00 26.09 ? 2015 HOH A O 1 HETATM 11226 O O . HOH W 7 . ? 8.850 -11.720 -1.181 1.00 43.50 ? 2016 HOH A O 1 HETATM 11227 O O . HOH W 7 . ? 18.039 -10.368 -3.878 1.00 55.29 ? 2017 HOH A O 1 HETATM 11228 O O . HOH W 7 . ? 10.134 -4.121 23.894 1.00 37.70 ? 2018 HOH A O 1 HETATM 11229 O O . HOH W 7 . ? 15.710 -16.108 -7.156 1.00 46.00 ? 2019 HOH A O 1 HETATM 11230 O O . HOH W 7 . ? 14.797 -9.399 -5.843 1.00 48.13 ? 2020 HOH A O 1 HETATM 11231 O O . HOH W 7 . ? 13.552 -4.862 -6.524 1.00 41.87 ? 2021 HOH A O 1 HETATM 11232 O O . HOH W 7 . ? 19.320 -5.473 -3.587 1.00 43.09 ? 2022 HOH A O 1 HETATM 11233 O O . HOH W 7 . ? 11.826 2.445 -0.505 1.00 37.65 ? 2023 HOH A O 1 HETATM 11234 O O . HOH W 7 . ? 3.635 -2.126 12.916 1.00 40.53 ? 2024 HOH A O 1 HETATM 11235 O O . HOH W 7 . ? 1.688 5.536 9.741 1.00 37.14 ? 2025 HOH A O 1 HETATM 11236 O O . HOH W 7 . ? 5.686 7.348 10.842 1.00 20.01 ? 2026 HOH A O 1 HETATM 11237 O O . HOH W 7 . ? 8.916 9.202 7.962 1.00 35.99 ? 2027 HOH A O 1 HETATM 11238 O O . HOH W 7 . ? 16.776 7.549 6.068 1.00 40.62 ? 2028 HOH A O 1 HETATM 11239 O O . HOH W 7 . ? 19.939 9.279 7.558 1.00 29.71 ? 2029 HOH A O 1 HETATM 11240 O O . HOH W 7 . ? 17.174 15.123 5.058 1.00 51.00 ? 2030 HOH A O 1 HETATM 11241 O O . HOH W 7 . ? 18.427 11.728 0.547 1.00 49.73 ? 2031 HOH A O 1 HETATM 11242 O O . HOH W 7 . ? 23.289 11.993 3.865 1.00 51.11 ? 2032 HOH A O 1 HETATM 11243 O O . HOH W 7 . ? 8.801 30.111 35.921 1.00 48.75 ? 2033 HOH A O 1 HETATM 11244 O O . HOH W 7 . ? 5.889 22.315 31.138 1.00 43.29 ? 2034 HOH A O 1 HETATM 11245 O O . HOH W 7 . ? 12.987 17.974 16.792 1.00 33.66 ? 2035 HOH A O 1 HETATM 11246 O O . HOH W 7 . ? 14.327 17.917 14.552 1.00 36.40 ? 2036 HOH A O 1 HETATM 11247 O O . HOH W 7 . ? 10.207 14.678 16.551 1.00 33.19 ? 2037 HOH A O 1 HETATM 11248 O O . HOH W 7 . ? 15.134 20.333 13.532 1.00 43.06 ? 2038 HOH A O 1 HETATM 11249 O O . HOH W 7 . ? 45.372 30.415 22.657 1.00 44.59 ? 2039 HOH A O 1 HETATM 11250 O O . HOH W 7 . ? 24.354 19.694 9.182 1.00 44.72 ? 2040 HOH A O 1 HETATM 11251 O O . HOH W 7 . ? 14.400 18.316 6.807 1.00 44.10 ? 2041 HOH A O 1 HETATM 11252 O O . HOH W 7 . ? 16.033 19.006 4.179 1.00 40.30 ? 2042 HOH A O 1 HETATM 11253 O O . HOH W 7 . ? 7.562 17.420 12.155 1.00 36.02 ? 2043 HOH A O 1 HETATM 11254 O O . HOH W 7 . ? 17.203 6.033 43.160 1.00 31.18 ? 2044 HOH A O 1 HETATM 11255 O O . HOH W 7 . ? 8.166 13.247 9.005 1.00 39.08 ? 2045 HOH A O 1 HETATM 11256 O O . HOH W 7 . ? 31.140 13.984 32.974 1.00 64.82 ? 2046 HOH A O 1 HETATM 11257 O O . HOH W 7 . ? 6.121 15.710 19.038 1.00 30.25 ? 2047 HOH A O 1 HETATM 11258 O O . HOH W 7 . ? 2.792 18.447 15.689 1.00 45.01 ? 2048 HOH A O 1 HETATM 11259 O O . HOH W 7 . ? 37.925 15.168 31.433 1.00 41.21 ? 2049 HOH A O 1 HETATM 11260 O O . HOH W 7 . ? 1.198 9.066 15.666 1.00 39.08 ? 2050 HOH A O 1 HETATM 11261 O O . HOH W 7 . ? 1.911 7.078 12.212 1.00 41.96 ? 2051 HOH A O 1 HETATM 11262 O O . HOH W 7 . ? 18.329 5.681 31.118 1.00 52.04 ? 2052 HOH A O 1 HETATM 11263 O O . HOH W 7 . ? 24.091 8.257 14.366 1.00 32.44 ? 2053 HOH A O 1 HETATM 11264 O O . HOH W 7 . ? 25.155 7.381 3.271 1.00 46.84 ? 2054 HOH A O 1 HETATM 11265 O O . HOH W 7 . ? 27.331 11.216 10.528 1.00 44.92 ? 2055 HOH A O 1 HETATM 11266 O O . HOH W 7 . ? 26.636 19.061 7.446 1.00 45.28 ? 2056 HOH A O 1 HETATM 11267 O O . HOH W 7 . ? 26.575 11.709 16.654 1.00 41.64 ? 2057 HOH A O 1 HETATM 11268 O O . HOH W 7 . ? 25.963 9.951 12.891 1.00 38.40 ? 2058 HOH A O 1 HETATM 11269 O O . HOH W 7 . ? 30.248 17.358 13.264 1.00 51.34 ? 2059 HOH A O 1 HETATM 11270 O O . HOH W 7 . ? 34.094 27.977 17.461 1.00 32.21 ? 2060 HOH A O 1 HETATM 11271 O O . HOH W 7 . ? 31.949 16.589 15.612 1.00 35.56 ? 2061 HOH A O 1 HETATM 11272 O O . HOH W 7 . ? 34.548 15.183 18.345 1.00 44.99 ? 2062 HOH A O 1 HETATM 11273 O O . HOH W 7 . ? 33.940 17.531 22.722 1.00 31.93 ? 2063 HOH A O 1 HETATM 11274 O O . HOH W 7 . ? 28.805 8.222 22.756 1.00 26.18 ? 2064 HOH A O 1 HETATM 11275 O O . HOH W 7 . ? 24.462 11.711 28.372 1.00 22.99 ? 2065 HOH A O 1 HETATM 11276 O O . HOH W 7 . ? 30.094 8.097 25.605 1.00 38.82 ? 2066 HOH A O 1 HETATM 11277 O O . HOH W 7 . ? 26.821 4.909 24.411 1.00 19.63 ? 2067 HOH A O 1 HETATM 11278 O O . HOH W 7 . ? 30.242 7.817 28.597 1.00 45.75 ? 2068 HOH A O 1 HETATM 11279 O O . HOH W 7 . ? 24.210 9.388 29.911 1.00 26.37 ? 2069 HOH A O 1 HETATM 11280 O O . HOH W 7 . ? -1.832 -11.189 -1.601 1.00 43.33 ? 2070 HOH A O 1 HETATM 11281 O O . HOH W 7 . ? 27.612 5.411 16.986 1.00 36.00 ? 2071 HOH A O 1 HETATM 11282 O O . HOH W 7 . ? 20.274 2.428 27.103 1.00 21.56 ? 2072 HOH A O 1 HETATM 11283 O O . HOH W 7 . ? 26.391 -1.527 26.605 1.00 29.21 ? 2073 HOH A O 1 HETATM 11284 O O . HOH W 7 . ? 25.983 5.637 14.934 1.00 50.34 ? 2074 HOH A O 1 HETATM 11285 O O . HOH W 7 . ? 20.179 -2.072 19.873 1.00 45.05 ? 2075 HOH A O 1 HETATM 11286 O O . HOH W 7 . ? 17.196 -2.837 26.917 1.00 34.18 ? 2076 HOH A O 1 HETATM 11287 O O . HOH W 7 . ? 10.323 -1.705 24.273 1.00 33.21 ? 2077 HOH A O 1 HETATM 11288 O O . HOH W 7 . ? 5.237 -1.904 18.311 1.00 40.32 ? 2078 HOH A O 1 HETATM 11289 O O . HOH W 7 . ? 6.785 22.168 21.486 1.00 49.66 ? 2079 HOH A O 1 HETATM 11290 O O . HOH W 7 . ? 4.661 22.716 26.555 1.00 41.61 ? 2080 HOH A O 1 HETATM 11291 O O . HOH W 7 . ? 10.993 28.386 23.653 1.00 53.23 ? 2081 HOH A O 1 HETATM 11292 O O . HOH W 7 . ? 15.383 27.420 27.087 1.00 36.74 ? 2082 HOH A O 1 HETATM 11293 O O . HOH W 7 . ? 15.212 37.292 18.267 1.00 50.57 ? 2083 HOH A O 1 HETATM 11294 O O . HOH W 7 . ? 20.324 29.322 20.832 1.00 47.85 ? 2084 HOH A O 1 HETATM 11295 O O . HOH W 7 . ? 11.593 25.302 4.294 1.00 45.65 ? 2085 HOH A O 1 HETATM 11296 O O . HOH W 7 . ? 15.098 27.652 20.318 1.00 53.92 ? 2086 HOH A O 1 HETATM 11297 O O . HOH W 7 . ? 11.286 26.299 14.312 1.00 41.14 ? 2087 HOH A O 1 HETATM 11298 O O . HOH W 7 . ? 25.429 29.422 28.600 1.00 28.90 ? 2088 HOH A O 1 HETATM 11299 O O . HOH W 7 . ? 28.858 37.885 35.037 1.00 44.49 ? 2089 HOH A O 1 HETATM 11300 O O . HOH W 7 . ? 24.890 35.113 40.354 1.00 49.14 ? 2090 HOH A O 1 HETATM 11301 O O . HOH W 7 . ? 20.139 33.614 36.906 1.00 43.39 ? 2091 HOH A O 1 HETATM 11302 O O . HOH W 7 . ? 28.152 30.380 40.777 1.00 39.68 ? 2092 HOH A O 1 HETATM 11303 O O . HOH W 7 . ? 18.349 31.644 37.629 1.00 38.52 ? 2093 HOH A O 1 HETATM 11304 O O . HOH W 7 . ? 11.703 26.732 33.548 1.00 49.26 ? 2094 HOH A O 1 HETATM 11305 O O . HOH W 7 . ? 13.120 27.308 38.072 1.00 36.35 ? 2095 HOH A O 1 HETATM 11306 O O . HOH W 7 . ? 10.474 25.694 35.529 1.00 46.06 ? 2096 HOH A O 1 HETATM 11307 O O . HOH W 7 . ? 5.472 19.740 31.442 1.00 35.42 ? 2097 HOH A O 1 HETATM 11308 O O . HOH W 7 . ? 8.793 22.932 37.043 1.00 49.07 ? 2098 HOH A O 1 HETATM 11309 O O . HOH W 7 . ? 6.731 21.418 35.455 1.00 45.93 ? 2099 HOH A O 1 HETATM 11310 O O . HOH W 7 . ? 9.654 20.358 42.716 1.00 41.53 ? 2100 HOH A O 1 HETATM 11311 O O . HOH W 7 . ? 2.986 18.725 32.610 1.00 50.15 ? 2101 HOH A O 1 HETATM 11312 O O . HOH W 7 . ? -0.393 10.950 29.849 1.00 24.11 ? 2102 HOH A O 1 HETATM 11313 O O . HOH W 7 . ? 0.379 9.174 26.726 1.00 29.65 ? 2103 HOH A O 1 HETATM 11314 O O . HOH W 7 . ? 6.742 6.956 29.275 1.00 22.80 ? 2104 HOH A O 1 HETATM 11315 O O . HOH W 7 . ? 15.760 18.866 26.409 1.00 25.75 ? 2105 HOH A O 1 HETATM 11316 O O . HOH W 7 . ? 43.526 28.743 24.340 1.00 55.37 ? 2106 HOH A O 1 HETATM 11317 O O . HOH W 7 . ? 43.590 30.350 26.630 1.00 38.06 ? 2107 HOH A O 1 HETATM 11318 O O . HOH W 7 . ? 38.357 33.517 30.343 1.00 51.07 ? 2108 HOH A O 1 HETATM 11319 O O . HOH W 7 . ? 35.670 28.102 32.515 1.00 37.48 ? 2109 HOH A O 1 HETATM 11320 O O . HOH W 7 . ? 33.520 28.061 39.661 1.00 42.31 ? 2110 HOH A O 1 HETATM 11321 O O . HOH W 7 . ? 22.196 21.359 40.177 1.00 31.45 ? 2111 HOH A O 1 HETATM 11322 O O . HOH W 7 . ? 24.924 23.293 42.306 1.00 38.61 ? 2112 HOH A O 1 HETATM 11323 O O . HOH W 7 . ? 21.324 12.380 42.218 1.00 31.95 ? 2113 HOH A O 1 HETATM 11324 O O . HOH W 7 . ? 17.479 11.577 35.848 1.00 26.63 ? 2114 HOH A O 1 HETATM 11325 O O . HOH W 7 . ? 19.224 7.718 43.716 1.00 40.06 ? 2115 HOH A O 1 HETATM 11326 O O . HOH W 7 . ? 23.150 10.001 42.285 1.00 26.20 ? 2116 HOH A O 1 HETATM 11327 O O . HOH W 7 . ? 16.000 8.538 37.252 1.00 30.85 ? 2117 HOH A O 1 HETATM 11328 O O . HOH W 7 . ? 25.365 10.818 37.387 1.00 42.66 ? 2118 HOH A O 1 HETATM 11329 O O . HOH W 7 . ? 28.453 10.681 41.582 1.00 54.95 ? 2119 HOH A O 1 HETATM 11330 O O . HOH W 7 . ? 28.588 12.911 33.572 1.00 49.56 ? 2120 HOH A O 1 HETATM 11331 O O . HOH W 7 . ? 29.847 14.675 36.025 1.00 38.80 ? 2121 HOH A O 1 HETATM 11332 O O . HOH W 7 . ? 31.451 20.273 43.266 1.00 38.76 ? 2122 HOH A O 1 HETATM 11333 O O . HOH W 7 . ? 33.276 22.843 39.541 1.00 38.65 ? 2123 HOH A O 1 HETATM 11334 O O . HOH W 7 . ? 35.039 18.906 37.226 1.00 59.51 ? 2124 HOH A O 1 HETATM 11335 O O . HOH W 7 . ? 37.727 20.143 32.368 1.00 35.87 ? 2125 HOH A O 1 HETATM 11336 O O . HOH W 7 . ? 37.177 25.908 32.463 1.00 54.43 ? 2126 HOH A O 1 HETATM 11337 O O . HOH W 7 . ? 39.689 24.612 30.278 1.00 37.84 ? 2127 HOH A O 1 HETATM 11338 O O . HOH W 7 . ? 39.318 14.607 29.024 1.00 40.52 ? 2128 HOH A O 1 HETATM 11339 O O . HOH W 7 . ? 40.652 32.036 11.606 1.00 59.17 ? 2129 HOH A O 1 HETATM 11340 O O . HOH W 7 . ? 23.915 12.291 31.164 1.00 45.81 ? 2130 HOH A O 1 HETATM 11341 O O . HOH W 7 . ? 18.512 8.042 32.613 1.00 37.01 ? 2131 HOH A O 1 HETATM 11342 O O . HOH W 7 . ? 21.017 9.433 33.265 1.00 31.07 ? 2132 HOH A O 1 HETATM 11343 O O . HOH W 7 . ? 14.548 10.803 37.121 1.00 24.96 ? 2133 HOH A O 1 HETATM 11344 O O . HOH W 7 . ? 16.422 7.617 34.399 1.00 23.44 ? 2134 HOH A O 1 HETATM 11345 O O . HOH W 7 . ? 7.495 3.539 33.754 1.00 48.99 ? 2135 HOH A O 1 HETATM 11346 O O . HOH W 7 . ? 8.082 7.484 39.148 1.00 48.60 ? 2136 HOH A O 1 HETATM 11347 O O . HOH W 7 . ? 9.933 10.587 40.726 1.00 45.99 ? 2137 HOH A O 1 HETATM 11348 O O . HOH W 7 . ? 11.951 12.169 42.941 1.00 36.07 ? 2138 HOH A O 1 HETATM 11349 O O . HOH W 7 . ? 14.931 17.858 42.469 1.00 23.04 ? 2139 HOH A O 1 HETATM 11350 O O . HOH W 7 . ? 19.228 24.479 40.324 1.00 30.44 ? 2140 HOH A O 1 HETATM 11351 O O . HOH W 7 . ? 20.886 24.907 42.488 1.00 36.88 ? 2141 HOH A O 1 HETATM 11352 O O . HOH W 7 . ? 23.976 25.019 44.875 1.00 33.30 ? 2142 HOH A O 1 HETATM 11353 O O . HOH W 7 . ? 12.906 4.636 28.561 1.00 42.92 ? 2143 HOH A O 1 HETATM 11354 O O . HOH W 7 . ? 17.679 -4.804 13.377 1.00 30.59 ? 2144 HOH A O 1 HETATM 11355 O O . HOH W 7 . ? 18.184 -0.647 16.350 1.00 37.33 ? 2145 HOH A O 1 HETATM 11356 O O . HOH W 7 . ? 21.930 0.828 13.389 1.00 42.50 ? 2146 HOH A O 1 HETATM 11357 O O . HOH W 7 . ? 20.295 -2.363 10.039 1.00 28.07 ? 2147 HOH A O 1 HETATM 11358 O O . HOH W 7 . ? 21.253 0.460 1.703 1.00 37.75 ? 2148 HOH A O 1 HETATM 11359 O O . HOH W 7 . ? 21.883 6.919 -1.505 1.00 52.90 ? 2149 HOH A O 1 HETATM 11360 O O . HOH W 7 . ? 16.361 12.264 -4.392 1.00 57.22 ? 2150 HOH A O 1 HETATM 11361 O O . HOH W 7 . ? 17.918 3.611 -4.251 1.00 49.15 ? 2151 HOH A O 1 HETATM 11362 O O . HOH W 7 . ? 3.601 2.368 -4.747 1.00 38.63 ? 2152 HOH A O 1 HETATM 11363 O O . HOH W 7 . ? 2.111 -2.508 -1.037 1.00 50.25 ? 2153 HOH A O 1 HETATM 11364 O O . HOH W 7 . ? 5.571 -5.914 0.258 1.00 43.54 ? 2154 HOH A O 1 HETATM 11365 O O . HOH W 7 . ? -2.242 -3.356 7.169 1.00 40.78 ? 2155 HOH A O 1 HETATM 11366 O O . HOH W 7 . ? 6.727 -12.696 4.588 1.00 38.43 ? 2156 HOH A O 1 HETATM 11367 O O . HOH W 7 . ? 0.605 -10.851 -1.169 1.00 49.65 ? 2157 HOH A O 1 HETATM 11368 O O . HOH W 7 . ? 1.030 -22.808 1.934 1.00 56.84 ? 2158 HOH A O 1 HETATM 11369 O O . HOH W 7 . ? 7.012 -16.748 6.892 1.00 50.29 ? 2159 HOH A O 1 HETATM 11370 O O . HOH W 7 . ? 14.432 -12.786 9.509 1.00 39.79 ? 2160 HOH A O 1 HETATM 11371 O O . HOH W 7 . ? 20.618 -10.316 -0.735 1.00 31.67 ? 2161 HOH A O 1 HETATM 11372 O O . HOH W 7 . ? 18.588 -12.830 11.438 1.00 41.23 ? 2162 HOH A O 1 HETATM 11373 O O . HOH W 7 . ? 17.287 -7.166 13.240 1.00 27.95 ? 2163 HOH A O 1 HETATM 11374 O O . HOH W 7 . ? 13.505 -10.113 12.874 1.00 46.54 ? 2164 HOH A O 1 HETATM 11375 O O . HOH W 7 . ? 10.042 -7.555 14.538 1.00 35.88 ? 2165 HOH A O 1 HETATM 11376 O O . HOH W 7 . ? 8.283 -12.135 15.220 1.00 49.13 ? 2166 HOH A O 1 HETATM 11377 O O . HOH W 7 . ? 0.119 -13.848 12.061 1.00 56.68 ? 2167 HOH A O 1 HETATM 11378 O O . HOH W 7 . ? 4.858 -6.399 13.553 1.00 46.23 ? 2168 HOH A O 1 HETATM 11379 O O . HOH W 7 . ? 10.150 -16.617 16.282 1.00 50.94 ? 2169 HOH A O 1 HETATM 11380 O O . HOH W 7 . ? 24.920 -12.646 5.929 1.00 54.04 ? 2170 HOH A O 1 HETATM 11381 O O . HOH W 7 . ? 30.158 -15.743 8.833 1.00 42.81 ? 2171 HOH A O 1 HETATM 11382 O O . HOH W 7 . ? 26.851 -20.508 3.757 1.00 51.95 ? 2172 HOH A O 1 HETATM 11383 O O . HOH W 7 . ? 23.798 -22.863 -5.876 1.00 49.96 ? 2173 HOH A O 1 HETATM 11384 O O . HOH W 7 . ? 19.109 -27.870 -1.160 1.00 51.96 ? 2174 HOH A O 1 HETATM 11385 O O . HOH W 7 . ? 10.891 -41.703 -13.101 1.00 66.54 ? 2175 HOH A O 1 HETATM 11386 O O . HOH W 7 . ? 7.742 18.563 46.214 1.00 46.98 ? 2176 HOH A O 1 HETATM 11387 O O . HOH W 7 . ? 2.152 20.243 46.016 1.00 46.53 ? 2177 HOH A O 1 HETATM 11388 O O . HOH W 7 . ? 26.375 35.759 14.127 1.00 52.28 ? 2178 HOH A O 1 HETATM 11389 O O . HOH W 7 . ? 34.255 35.474 11.052 1.00 51.96 ? 2179 HOH A O 1 HETATM 11390 O O . HOH W 7 . ? 23.063 -0.565 19.819 1.00 32.38 ? 2180 HOH A O 1 HETATM 11391 O O . HOH X 7 . ? 17.870 -47.600 -13.608 1.00 55.92 ? 2001 HOH B O 1 HETATM 11392 O O . HOH X 7 . ? 15.624 -48.391 -10.843 1.00 50.04 ? 2002 HOH B O 1 HETATM 11393 O O . HOH X 7 . ? 2.684 -36.596 -17.872 1.00 56.40 ? 2003 HOH B O 1 HETATM 11394 O O . HOH X 7 . ? 1.238 -36.895 -8.288 1.00 69.93 ? 2004 HOH B O 1 HETATM 11395 O O . HOH X 7 . ? 40.568 4.582 16.512 1.00 42.07 ? 2005 HOH B O 1 HETATM 11396 O O . HOH X 7 . ? 34.177 -1.991 26.110 1.00 24.70 ? 2006 HOH B O 1 HETATM 11397 O O . HOH X 7 . ? 33.004 -5.310 13.342 1.00 52.89 ? 2007 HOH B O 1 HETATM 11398 O O . HOH X 7 . ? -4.635 -46.545 -20.560 1.00 63.32 ? 2008 HOH B O 1 HETATM 11399 O O . HOH X 7 . ? 9.332 -69.390 -19.507 1.00 50.78 ? 2009 HOH B O 1 HETATM 11400 O O . HOH X 7 . ? -1.012 -35.117 6.368 1.00 62.04 ? 2010 HOH B O 1 HETATM 11401 O O . HOH X 7 . ? 4.074 -31.429 0.788 1.00 65.26 ? 2011 HOH B O 1 HETATM 11402 O O . HOH X 7 . ? -4.071 -54.053 -11.859 1.00 74.12 ? 2012 HOH B O 1 HETATM 11403 O O . HOH X 7 . ? 9.587 -27.302 16.862 1.00 51.96 ? 2013 HOH B O 1 HETATM 11404 O O . HOH X 7 . ? 13.273 -26.584 18.052 1.00 55.94 ? 2014 HOH B O 1 HETATM 11405 O O . HOH X 7 . ? 6.651 -17.200 13.764 1.00 52.82 ? 2015 HOH B O 1 HETATM 11406 O O . HOH X 7 . ? 14.361 -23.471 22.031 1.00 44.35 ? 2016 HOH B O 1 HETATM 11407 O O . HOH X 7 . ? 15.439 -24.436 19.505 1.00 44.23 ? 2017 HOH B O 1 HETATM 11408 O O . HOH X 7 . ? 17.489 -18.263 18.982 1.00 44.55 ? 2018 HOH B O 1 HETATM 11409 O O . HOH X 7 . ? 11.984 -11.702 14.755 1.00 59.26 ? 2019 HOH B O 1 HETATM 11410 O O . HOH X 7 . ? 24.130 -6.717 15.551 1.00 39.06 ? 2020 HOH B O 1 HETATM 11411 O O . HOH X 7 . ? 23.958 -10.223 18.613 1.00 48.76 ? 2021 HOH B O 1 HETATM 11412 O O . HOH X 7 . ? 28.481 0.328 15.063 1.00 28.63 ? 2022 HOH B O 1 HETATM 11413 O O . HOH X 7 . ? 33.842 4.400 24.769 1.00 40.53 ? 2023 HOH B O 1 HETATM 11414 O O . HOH X 7 . ? 33.015 6.802 17.685 1.00 37.02 ? 2024 HOH B O 1 HETATM 11415 O O . HOH X 7 . ? 40.003 2.337 18.185 1.00 35.10 ? 2025 HOH B O 1 HETATM 11416 O O . HOH X 7 . ? 36.633 -0.317 25.196 1.00 21.78 ? 2026 HOH B O 1 HETATM 11417 O O . HOH X 7 . ? 31.502 -0.215 26.225 1.00 23.96 ? 2027 HOH B O 1 HETATM 11418 O O . HOH X 7 . ? 34.941 -4.172 15.451 1.00 37.09 ? 2028 HOH B O 1 HETATM 11419 O O . HOH X 7 . ? 33.569 0.846 15.025 1.00 49.05 ? 2029 HOH B O 1 HETATM 11420 O O . HOH X 7 . ? 39.864 0.096 11.961 1.00 50.79 ? 2030 HOH B O 1 HETATM 11421 O O . HOH X 7 . ? 35.358 -2.857 23.234 1.00 22.54 ? 2031 HOH B O 1 HETATM 11422 O O . HOH X 7 . ? 40.940 -0.732 25.998 1.00 20.18 ? 2032 HOH B O 1 HETATM 11423 O O . HOH X 7 . ? 28.833 -6.278 15.402 1.00 31.70 ? 2033 HOH B O 1 HETATM 11424 O O . HOH X 7 . ? 37.726 -10.499 13.470 1.00 43.45 ? 2034 HOH B O 1 HETATM 11425 O O . HOH X 7 . ? 32.301 -7.462 6.788 1.00 54.33 ? 2035 HOH B O 1 HETATM 11426 O O . HOH X 7 . ? 31.854 -15.803 13.482 1.00 41.83 ? 2036 HOH B O 1 HETATM 11427 O O . HOH X 7 . ? 29.493 -20.727 14.013 1.00 27.32 ? 2037 HOH B O 1 HETATM 11428 O O . HOH X 7 . ? 20.259 -19.536 18.178 1.00 41.76 ? 2038 HOH B O 1 HETATM 11429 O O . HOH X 7 . ? 25.780 -32.508 12.563 1.00 56.32 ? 2039 HOH B O 1 HETATM 11430 O O . HOH X 7 . ? 21.568 -30.480 12.536 1.00 52.30 ? 2040 HOH B O 1 HETATM 11431 O O . HOH X 7 . ? 24.066 -27.813 15.763 1.00 45.62 ? 2041 HOH B O 1 HETATM 11432 O O . HOH X 7 . ? 15.981 -48.572 -3.337 1.00 55.25 ? 2042 HOH B O 1 HETATM 11433 O O . HOH X 7 . ? 9.162 -49.237 4.968 1.00 62.44 ? 2043 HOH B O 1 HETATM 11434 O O . HOH X 7 . ? 1.120 -52.273 -0.112 1.00 50.55 ? 2044 HOH B O 1 HETATM 11435 O O . HOH X 7 . ? 9.419 -54.607 5.223 1.00 64.33 ? 2045 HOH B O 1 HETATM 11436 O O . HOH X 7 . ? 11.154 -68.742 -17.287 1.00 69.89 ? 2046 HOH B O 1 HETATM 11437 O O . HOH X 7 . ? 2.755 -68.070 -15.098 1.00 64.88 ? 2047 HOH B O 1 HETATM 11438 O O . HOH X 7 . ? 4.176 -68.799 -20.873 1.00 57.33 ? 2048 HOH B O 1 HETATM 11439 O O . HOH X 7 . ? -0.864 -73.384 -15.805 1.00 58.18 ? 2049 HOH B O 1 HETATM 11440 O O . HOH X 7 . ? -4.405 -55.605 -9.310 1.00 61.56 ? 2050 HOH B O 1 HETATM 11441 O O . HOH X 7 . ? -10.261 -58.978 -2.913 1.00 58.00 ? 2051 HOH B O 1 HETATM 11442 O O . HOH X 7 . ? -11.435 -50.711 -10.213 1.00 63.27 ? 2052 HOH B O 1 HETATM 11443 O O . HOH X 7 . ? -13.981 -51.060 -0.340 1.00 59.76 ? 2053 HOH B O 1 HETATM 11444 O O . HOH Y 7 . ? 26.101 -75.450 -13.823 1.00 52.10 ? 2001 HOH C O 1 HETATM 11445 O O . HOH Y 7 . ? 29.936 -78.095 -6.270 1.00 47.16 ? 2002 HOH C O 1 HETATM 11446 O O . HOH Y 7 . ? 45.576 -55.406 -2.021 1.00 54.27 ? 2003 HOH C O 1 HETATM 11447 O O . HOH Y 7 . ? 32.681 -61.228 7.709 1.00 53.08 ? 2004 HOH C O 1 HETATM 11448 O O . HOH Y 7 . ? 44.325 -55.390 0.555 1.00 62.52 ? 2005 HOH C O 1 HETATM 11449 O O . HOH Y 7 . ? 42.265 -47.960 13.871 1.00 51.41 ? 2006 HOH C O 1 HETATM 11450 O O . HOH Y 7 . ? 34.778 -43.368 13.515 1.00 46.40 ? 2007 HOH C O 1 HETATM 11451 O O . HOH Y 7 . ? 37.088 -42.977 18.568 1.00 68.81 ? 2008 HOH C O 1 HETATM 11452 O O . HOH Y 7 . ? 18.637 -48.367 16.203 1.00 92.45 ? 2009 HOH C O 1 HETATM 11453 O O . HOH Y 7 . ? 26.522 -56.494 14.050 1.00 59.81 ? 2010 HOH C O 1 HETATM 11454 O O . HOH Y 7 . ? 63.657 -2.342 33.171 1.00 28.96 ? 2011 HOH C O 1 HETATM 11455 O O . HOH Y 7 . ? 38.510 -49.562 21.868 1.00 50.13 ? 2012 HOH C O 1 HETATM 11456 O O . HOH Y 7 . ? 60.110 -4.551 1.432 1.00 40.70 ? 2013 HOH C O 1 HETATM 11457 O O . HOH Y 7 . ? 41.198 -45.903 3.288 1.00 57.30 ? 2014 HOH C O 1 HETATM 11458 O O . HOH Y 7 . ? 42.913 -41.836 6.556 1.00 49.97 ? 2015 HOH C O 1 HETATM 11459 O O . HOH Y 7 . ? 42.429 -40.657 15.146 1.00 47.09 ? 2016 HOH C O 1 HETATM 11460 O O . HOH Y 7 . ? 47.236 -36.513 11.637 1.00 57.33 ? 2017 HOH C O 1 HETATM 11461 O O . HOH Y 7 . ? 50.433 -30.730 11.127 1.00 44.18 ? 2018 HOH C O 1 HETATM 11462 O O . HOH Y 7 . ? 38.962 -8.843 7.972 1.00 56.30 ? 2019 HOH C O 1 HETATM 11463 O O . HOH Y 7 . ? 52.452 -32.602 17.352 1.00 56.00 ? 2020 HOH C O 1 HETATM 11464 O O . HOH Y 7 . ? 59.863 -29.124 18.739 1.00 46.01 ? 2021 HOH C O 1 HETATM 11465 O O . HOH Y 7 . ? 57.528 -26.933 21.649 1.00 49.23 ? 2022 HOH C O 1 HETATM 11466 O O . HOH Y 7 . ? 60.134 -24.229 19.532 1.00 43.72 ? 2023 HOH C O 1 HETATM 11467 O O . HOH Y 7 . ? 58.964 -30.279 11.872 1.00 55.66 ? 2024 HOH C O 1 HETATM 11468 O O . HOH Y 7 . ? 60.311 -21.954 17.663 1.00 48.49 ? 2025 HOH C O 1 HETATM 11469 O O . HOH Y 7 . ? 59.473 -22.792 13.468 1.00 55.01 ? 2026 HOH C O 1 HETATM 11470 O O . HOH Y 7 . ? 51.636 -14.229 5.386 1.00 57.79 ? 2027 HOH C O 1 HETATM 11471 O O . HOH Y 7 . ? 68.881 -2.499 40.111 1.00 41.41 ? 2028 HOH C O 1 HETATM 11472 O O . HOH Y 7 . ? 60.778 -12.996 4.844 1.00 50.83 ? 2029 HOH C O 1 HETATM 11473 O O . HOH Y 7 . ? 59.482 -10.825 6.450 1.00 35.29 ? 2030 HOH C O 1 HETATM 11474 O O . HOH Y 7 . ? 58.802 -9.505 10.996 1.00 37.40 ? 2031 HOH C O 1 HETATM 11475 O O . HOH Y 7 . ? 60.816 -10.415 15.380 1.00 37.09 ? 2032 HOH C O 1 HETATM 11476 O O . HOH Y 7 . ? 62.615 -10.962 17.734 1.00 53.19 ? 2033 HOH C O 1 HETATM 11477 O O . HOH Y 7 . ? 57.840 -13.403 22.252 1.00 59.66 ? 2034 HOH C O 1 HETATM 11478 O O . HOH Y 7 . ? 56.944 -10.637 25.011 1.00 26.47 ? 2035 HOH C O 1 HETATM 11479 O O . HOH Y 7 . ? 59.412 -11.891 29.868 1.00 36.65 ? 2036 HOH C O 1 HETATM 11480 O O . HOH Y 7 . ? 60.859 -0.067 20.979 1.00 30.42 ? 2037 HOH C O 1 HETATM 11481 O O . HOH Y 7 . ? 59.991 2.252 19.034 1.00 41.12 ? 2038 HOH C O 1 HETATM 11482 O O . HOH Y 7 . ? 58.950 -0.749 15.727 1.00 29.00 ? 2039 HOH C O 1 HETATM 11483 O O . HOH Y 7 . ? 63.278 0.727 22.788 1.00 29.50 ? 2040 HOH C O 1 HETATM 11484 O O . HOH Y 7 . ? 64.459 -0.162 31.123 1.00 58.49 ? 2041 HOH C O 1 HETATM 11485 O O . HOH Y 7 . ? 61.686 -3.283 31.626 1.00 38.21 ? 2042 HOH C O 1 HETATM 11486 O O . HOH Y 7 . ? 65.484 -5.157 22.890 1.00 34.53 ? 2043 HOH C O 1 HETATM 11487 O O . HOH Y 7 . ? 69.216 -1.719 31.626 1.00 37.30 ? 2044 HOH C O 1 HETATM 11488 O O . HOH Y 7 . ? 70.168 -0.359 22.265 1.00 38.63 ? 2045 HOH C O 1 HETATM 11489 O O . HOH Y 7 . ? 68.964 -4.775 21.552 1.00 42.60 ? 2046 HOH C O 1 HETATM 11490 O O . HOH Y 7 . ? 63.818 -2.922 14.896 1.00 40.15 ? 2047 HOH C O 1 HETATM 11491 O O . HOH Y 7 . ? 62.370 -6.960 15.017 1.00 42.73 ? 2048 HOH C O 1 HETATM 11492 O O . HOH Y 7 . ? 68.347 -10.468 16.655 1.00 58.35 ? 2049 HOH C O 1 HETATM 11493 O O . HOH Y 7 . ? 60.190 -0.109 10.759 1.00 50.88 ? 2050 HOH C O 1 HETATM 11494 O O . HOH Y 7 . ? 59.967 2.146 11.864 1.00 31.88 ? 2051 HOH C O 1 HETATM 11495 O O . HOH Y 7 . ? 62.838 5.686 13.778 1.00 46.26 ? 2052 HOH C O 1 HETATM 11496 O O . HOH Y 7 . ? 66.200 0.498 14.034 1.00 48.81 ? 2053 HOH C O 1 HETATM 11497 O O . HOH Y 7 . ? 64.274 4.739 16.692 1.00 44.20 ? 2054 HOH C O 1 HETATM 11498 O O . HOH Y 7 . ? 41.491 19.327 38.933 1.00 37.33 ? 2055 HOH C O 1 HETATM 11499 O O . HOH Y 7 . ? 58.561 0.298 13.157 1.00 46.95 ? 2056 HOH C O 1 HETATM 11500 O O . HOH Y 7 . ? 57.004 -1.589 11.710 1.00 44.73 ? 2057 HOH C O 1 HETATM 11501 O O . HOH Y 7 . ? 58.557 -7.318 12.347 1.00 35.30 ? 2058 HOH C O 1 HETATM 11502 O O . HOH Y 7 . ? 59.385 -8.153 6.382 1.00 41.56 ? 2059 HOH C O 1 HETATM 11503 O O . HOH Y 7 . ? 59.373 -4.618 5.815 1.00 45.08 ? 2060 HOH C O 1 HETATM 11504 O O . HOH Y 7 . ? 55.211 -3.227 4.073 1.00 39.92 ? 2061 HOH C O 1 HETATM 11505 O O . HOH Y 7 . ? 50.303 -6.551 26.886 1.00 26.67 ? 2062 HOH C O 1 HETATM 11506 O O . HOH Y 7 . ? 57.561 -15.900 23.210 1.00 46.01 ? 2063 HOH C O 1 HETATM 11507 O O . HOH Y 7 . ? 55.357 -14.554 30.530 1.00 46.34 ? 2064 HOH C O 1 HETATM 11508 O O . HOH Y 7 . ? 58.471 -14.272 30.680 1.00 33.01 ? 2065 HOH C O 1 HETATM 11509 O O . HOH Y 7 . ? 65.294 -8.229 29.482 1.00 38.40 ? 2066 HOH C O 1 HETATM 11510 O O . HOH Y 7 . ? 57.072 -3.913 34.216 1.00 56.61 ? 2067 HOH C O 1 HETATM 11511 O O . HOH Y 7 . ? 46.309 -12.214 3.841 1.00 37.53 ? 2068 HOH C O 1 HETATM 11512 O O . HOH Y 7 . ? 53.630 3.744 32.671 1.00 36.25 ? 2069 HOH C O 1 HETATM 11513 O O . HOH Y 7 . ? 58.543 8.395 41.554 1.00 31.01 ? 2070 HOH C O 1 HETATM 11514 O O . HOH Y 7 . ? 52.459 0.213 35.994 1.00 28.19 ? 2071 HOH C O 1 HETATM 11515 O O . HOH Y 7 . ? 50.046 0.589 37.337 1.00 34.73 ? 2072 HOH C O 1 HETATM 11516 O O . HOH Y 7 . ? 48.226 5.461 36.793 1.00 28.45 ? 2073 HOH C O 1 HETATM 11517 O O . HOH Y 7 . ? 45.178 6.414 36.585 1.00 50.04 ? 2074 HOH C O 1 HETATM 11518 O O . HOH Y 7 . ? 43.833 -0.569 30.566 1.00 47.51 ? 2075 HOH C O 1 HETATM 11519 O O . HOH Y 7 . ? 44.681 2.096 31.515 1.00 36.23 ? 2076 HOH C O 1 HETATM 11520 O O . HOH Y 7 . ? 44.306 6.551 25.006 1.00 31.92 ? 2077 HOH C O 1 HETATM 11521 O O . HOH Y 7 . ? 41.337 1.397 29.887 1.00 44.50 ? 2078 HOH C O 1 HETATM 11522 O O . HOH Y 7 . ? 38.654 0.845 26.572 1.00 42.20 ? 2079 HOH C O 1 HETATM 11523 O O . HOH Y 7 . ? 41.657 6.434 23.838 1.00 33.56 ? 2080 HOH C O 1 HETATM 11524 O O . HOH Y 7 . ? 42.337 -6.705 22.323 1.00 24.25 ? 2081 HOH C O 1 HETATM 11525 O O . HOH Y 7 . ? 45.632 -6.724 28.676 1.00 39.34 ? 2082 HOH C O 1 HETATM 11526 O O . HOH Y 7 . ? 45.528 -2.996 31.418 1.00 45.33 ? 2083 HOH C O 1 HETATM 11527 O O . HOH Y 7 . ? 40.223 -0.327 18.608 1.00 26.78 ? 2084 HOH C O 1 HETATM 11528 O O . HOH Y 7 . ? 37.763 -3.936 13.674 1.00 50.41 ? 2085 HOH C O 1 HETATM 11529 O O . HOH Y 7 . ? 44.152 -0.265 12.922 1.00 41.60 ? 2086 HOH C O 1 HETATM 11530 O O . HOH Y 7 . ? 40.368 -7.076 9.705 1.00 53.11 ? 2087 HOH C O 1 HETATM 11531 O O . HOH Y 7 . ? 60.051 0.981 8.296 1.00 54.81 ? 2088 HOH C O 1 HETATM 11532 O O . HOH Y 7 . ? 61.881 10.656 10.788 1.00 42.43 ? 2089 HOH C O 1 HETATM 11533 O O . HOH Y 7 . ? 62.570 8.038 14.387 1.00 37.25 ? 2090 HOH C O 1 HETATM 11534 O O . HOH Y 7 . ? 63.777 11.015 17.752 1.00 42.53 ? 2091 HOH C O 1 HETATM 11535 O O . HOH Y 7 . ? 64.521 13.882 19.072 1.00 36.25 ? 2092 HOH C O 1 HETATM 11536 O O . HOH Y 7 . ? 58.058 17.421 12.416 1.00 40.13 ? 2093 HOH C O 1 HETATM 11537 O O . HOH Y 7 . ? 58.114 19.784 16.143 1.00 62.37 ? 2094 HOH C O 1 HETATM 11538 O O . HOH Y 7 . ? 59.861 15.645 21.898 1.00 38.28 ? 2095 HOH C O 1 HETATM 11539 O O . HOH Y 7 . ? 66.720 15.799 18.547 1.00 52.01 ? 2096 HOH C O 1 HETATM 11540 O O . HOH Y 7 . ? 62.824 10.255 26.294 1.00 38.06 ? 2097 HOH C O 1 HETATM 11541 O O . HOH Y 7 . ? 71.057 20.492 18.264 1.00 46.87 ? 2098 HOH C O 1 HETATM 11542 O O . HOH Y 7 . ? 60.772 24.418 16.982 1.00 48.80 ? 2099 HOH C O 1 HETATM 11543 O O . HOH Y 7 . ? 64.683 29.663 28.141 1.00 40.76 ? 2100 HOH C O 1 HETATM 11544 O O . HOH Y 7 . ? 61.057 29.961 30.510 1.00 49.76 ? 2101 HOH C O 1 HETATM 11545 O O . HOH Y 7 . ? 66.615 20.344 26.698 1.00 42.50 ? 2102 HOH C O 1 HETATM 11546 O O . HOH Y 7 . ? 64.137 16.521 30.899 1.00 26.79 ? 2103 HOH C O 1 HETATM 11547 O O . HOH Y 7 . ? 66.754 13.910 35.984 1.00 43.72 ? 2104 HOH C O 1 HETATM 11548 O O . HOH Y 7 . ? 62.554 11.703 28.661 1.00 31.45 ? 2105 HOH C O 1 HETATM 11549 O O . HOH Y 7 . ? 68.042 0.934 37.965 1.00 42.19 ? 2106 HOH C O 1 HETATM 11550 O O . HOH Y 7 . ? 63.888 2.473 40.392 1.00 31.51 ? 2107 HOH C O 1 HETATM 11551 O O . HOH Y 7 . ? 64.690 -2.337 37.981 1.00 49.03 ? 2108 HOH C O 1 HETATM 11552 O O . HOH Y 7 . ? 70.567 -1.779 29.172 1.00 33.48 ? 2109 HOH C O 1 HETATM 11553 O O . HOH Y 7 . ? 72.565 -2.851 25.136 1.00 35.53 ? 2110 HOH C O 1 HETATM 11554 O O . HOH Y 7 . ? 76.484 -0.916 32.888 1.00 44.82 ? 2111 HOH C O 1 HETATM 11555 O O . HOH Y 7 . ? 71.298 1.491 36.209 1.00 48.60 ? 2112 HOH C O 1 HETATM 11556 O O . HOH Y 7 . ? 69.978 8.405 29.914 1.00 23.58 ? 2113 HOH C O 1 HETATM 11557 O O . HOH Y 7 . ? 68.014 8.492 38.394 1.00 38.68 ? 2114 HOH C O 1 HETATM 11558 O O . HOH Y 7 . ? 65.311 7.485 26.434 1.00 42.39 ? 2115 HOH C O 1 HETATM 11559 O O . HOH Y 7 . ? 64.527 8.537 21.611 1.00 46.76 ? 2116 HOH C O 1 HETATM 11560 O O . HOH Y 7 . ? 56.330 18.058 31.441 1.00 23.17 ? 2117 HOH C O 1 HETATM 11561 O O . HOH Y 7 . ? 67.901 24.567 34.393 1.00 45.81 ? 2118 HOH C O 1 HETATM 11562 O O . HOH Y 7 . ? 63.424 31.885 34.401 1.00 63.45 ? 2119 HOH C O 1 HETATM 11563 O O . HOH Y 7 . ? 71.534 27.876 33.822 1.00 47.18 ? 2120 HOH C O 1 HETATM 11564 O O . HOH Y 7 . ? 66.551 24.873 38.505 1.00 53.09 ? 2121 HOH C O 1 HETATM 11565 O O . HOH Y 7 . ? 56.725 28.910 35.369 1.00 36.72 ? 2122 HOH C O 1 HETATM 11566 O O . HOH Y 7 . ? 53.575 28.496 33.017 1.00 36.75 ? 2123 HOH C O 1 HETATM 11567 O O . HOH Y 7 . ? 53.799 30.894 29.663 1.00 55.51 ? 2124 HOH C O 1 HETATM 11568 O O . HOH Y 7 . ? 51.000 31.665 29.111 1.00 43.58 ? 2125 HOH C O 1 HETATM 11569 O O . HOH Y 7 . ? 53.756 29.472 22.848 1.00 51.56 ? 2126 HOH C O 1 HETATM 11570 O O . HOH Y 7 . ? 53.483 24.067 16.802 1.00 38.11 ? 2127 HOH C O 1 HETATM 11571 O O . HOH Y 7 . ? 49.644 26.371 18.625 1.00 46.48 ? 2128 HOH C O 1 HETATM 11572 O O . HOH Y 7 . ? 53.619 20.226 12.119 1.00 37.59 ? 2129 HOH C O 1 HETATM 11573 O O . HOH Y 7 . ? 53.854 18.679 9.589 1.00 41.33 ? 2130 HOH C O 1 HETATM 11574 O O . HOH Y 7 . ? 48.766 18.373 6.099 1.00 45.04 ? 2131 HOH C O 1 HETATM 11575 O O . HOH Y 7 . ? 48.074 23.273 10.662 1.00 37.90 ? 2132 HOH C O 1 HETATM 11576 O O . HOH Y 7 . ? 50.912 22.436 7.740 1.00 44.61 ? 2133 HOH C O 1 HETATM 11577 O O . HOH Y 7 . ? 53.546 9.862 3.424 1.00 45.66 ? 2134 HOH C O 1 HETATM 11578 O O . HOH Y 7 . ? 45.798 6.757 5.611 1.00 35.33 ? 2135 HOH C O 1 HETATM 11579 O O . HOH Y 7 . ? 46.108 10.340 2.604 1.00 41.40 ? 2136 HOH C O 1 HETATM 11580 O O . HOH Y 7 . ? 47.095 9.830 0.267 1.00 26.53 ? 2137 HOH C O 1 HETATM 11581 O O . HOH Y 7 . ? 53.816 4.112 2.624 1.00 29.25 ? 2138 HOH C O 1 HETATM 11582 O O . HOH Y 7 . ? 47.499 4.613 7.109 1.00 20.58 ? 2139 HOH C O 1 HETATM 11583 O O . HOH Y 7 . ? 44.125 2.933 10.583 1.00 34.94 ? 2140 HOH C O 1 HETATM 11584 O O . HOH Y 7 . ? 53.914 9.816 19.530 1.00 33.14 ? 2141 HOH C O 1 HETATM 11585 O O . HOH Y 7 . ? 50.830 11.474 48.456 1.00 39.64 ? 2142 HOH C O 1 HETATM 11586 O O . HOH Y 7 . ? 51.141 14.125 49.137 1.00 28.05 ? 2143 HOH C O 1 HETATM 11587 O O . HOH Y 7 . ? 59.416 16.021 47.530 1.00 44.74 ? 2144 HOH C O 1 HETATM 11588 O O . HOH Y 7 . ? 51.178 16.574 48.928 1.00 33.08 ? 2145 HOH C O 1 HETATM 11589 O O . HOH Y 7 . ? 53.533 21.998 44.391 1.00 36.28 ? 2146 HOH C O 1 HETATM 11590 O O . HOH Y 7 . ? 59.733 13.919 46.030 1.00 47.92 ? 2147 HOH C O 1 HETATM 11591 O O . HOH Y 7 . ? 63.870 19.895 38.211 1.00 36.62 ? 2148 HOH C O 1 HETATM 11592 O O . HOH Y 7 . ? 63.768 16.545 41.517 1.00 40.11 ? 2149 HOH C O 1 HETATM 11593 O O . HOH Y 7 . ? 61.583 22.836 44.986 1.00 40.03 ? 2150 HOH C O 1 HETATM 11594 O O . HOH Y 7 . ? 45.889 26.045 35.700 1.00 53.99 ? 2151 HOH C O 1 HETATM 11595 O O . HOH Y 7 . ? 45.463 21.864 23.195 1.00 33.40 ? 2152 HOH C O 1 HETATM 11596 O O . HOH Y 7 . ? 42.576 12.291 16.425 1.00 31.74 ? 2153 HOH C O 1 HETATM 11597 O O . HOH Y 7 . ? 40.324 11.867 14.495 1.00 32.64 ? 2154 HOH C O 1 HETATM 11598 O O . HOH Y 7 . ? 39.691 11.135 19.112 1.00 41.34 ? 2155 HOH C O 1 HETATM 11599 O O . HOH Y 7 . ? 38.789 13.231 26.660 1.00 36.59 ? 2156 HOH C O 1 HETATM 11600 O O . HOH Y 7 . ? 41.001 20.042 26.296 1.00 48.02 ? 2157 HOH C O 1 HETATM 11601 O O . HOH Y 7 . ? 43.568 9.370 24.208 1.00 28.56 ? 2158 HOH C O 1 HETATM 11602 O O . HOH Y 7 . ? 40.742 11.141 26.149 1.00 51.73 ? 2159 HOH C O 1 HETATM 11603 O O . HOH Y 7 . ? 43.523 15.173 39.266 1.00 43.27 ? 2160 HOH C O 1 HETATM 11604 O O . HOH Y 7 . ? 46.298 15.987 42.453 1.00 35.48 ? 2161 HOH C O 1 HETATM 11605 O O . HOH Y 7 . ? 47.760 18.979 39.814 1.00 39.86 ? 2162 HOH C O 1 HETATM 11606 O O . HOH Y 7 . ? 47.584 12.948 48.068 1.00 25.05 ? 2163 HOH C O 1 HETATM 11607 O O . HOH Y 7 . ? 47.238 8.788 48.887 1.00 38.15 ? 2164 HOH C O 1 HETATM 11608 O O . HOH Y 7 . ? 48.400 8.614 52.820 1.00 38.71 ? 2165 HOH C O 1 HETATM 11609 O O . HOH Y 7 . ? 49.143 10.929 52.010 1.00 38.38 ? 2166 HOH C O 1 HETATM 11610 O O . HOH Y 7 . ? 56.135 1.767 48.768 1.00 46.06 ? 2167 HOH C O 1 HETATM 11611 O O . HOH Y 7 . ? 64.068 3.762 49.745 1.00 47.83 ? 2168 HOH C O 1 HETATM 11612 O O . HOH Y 7 . ? 58.990 -3.094 41.891 1.00 47.15 ? 2169 HOH C O 1 HETATM 11613 O O . HOH Y 7 . ? 60.054 -1.175 43.916 1.00 43.43 ? 2170 HOH C O 1 HETATM 11614 O O . HOH Y 7 . ? 59.832 6.929 44.745 1.00 29.13 ? 2171 HOH C O 1 HETATM 11615 O O . HOH Y 7 . ? 49.098 2.792 41.483 1.00 44.24 ? 2172 HOH C O 1 HETATM 11616 O O . HOH Y 7 . ? 49.067 2.850 38.606 1.00 34.87 ? 2173 HOH C O 1 HETATM 11617 O O . HOH Y 7 . ? 44.010 11.437 34.833 1.00 36.91 ? 2174 HOH C O 1 HETATM 11618 O O . HOH Y 7 . ? 42.177 6.430 20.910 1.00 40.69 ? 2175 HOH C O 1 HETATM 11619 O O . HOH Y 7 . ? 41.687 7.184 17.593 1.00 44.42 ? 2176 HOH C O 1 HETATM 11620 O O . HOH Y 7 . ? 41.306 8.698 19.990 1.00 28.30 ? 2177 HOH C O 1 HETATM 11621 O O . HOH Y 7 . ? 42.803 12.531 13.205 1.00 34.96 ? 2178 HOH C O 1 HETATM 11622 O O . HOH Y 7 . ? 41.022 9.016 14.950 1.00 37.02 ? 2179 HOH C O 1 HETATM 11623 O O . HOH Y 7 . ? 48.471 24.661 21.275 1.00 44.17 ? 2180 HOH C O 1 HETATM 11624 O O . HOH Y 7 . ? 64.438 8.289 18.741 1.00 42.36 ? 2181 HOH C O 1 HETATM 11625 O O . HOH Y 7 . ? 49.873 -9.480 2.962 1.00 42.82 ? 2182 HOH C O 1 HETATM 11626 O O . HOH Y 7 . ? 47.381 -6.920 2.929 1.00 34.59 ? 2183 HOH C O 1 HETATM 11627 O O . HOH Y 7 . ? 45.685 -9.422 4.274 1.00 43.04 ? 2184 HOH C O 1 HETATM 11628 O O . HOH Y 7 . ? 42.758 -12.234 10.800 1.00 43.00 ? 2185 HOH C O 1 HETATM 11629 O O . HOH Y 7 . ? 39.041 -13.555 4.826 1.00 45.09 ? 2186 HOH C O 1 HETATM 11630 O O . HOH Y 7 . ? 46.864 -16.413 21.488 1.00 38.61 ? 2187 HOH C O 1 HETATM 11631 O O . HOH Y 7 . ? 56.713 -26.261 8.458 1.00 55.92 ? 2188 HOH C O 1 HETATM 11632 O O . HOH Y 7 . ? 60.056 -25.592 8.104 1.00 64.60 ? 2189 HOH C O 1 HETATM 11633 O O . HOH Y 7 . ? 53.827 -26.188 8.652 1.00 47.18 ? 2190 HOH C O 1 HETATM 11634 O O . HOH Y 7 . ? 49.023 -18.756 4.633 1.00 54.12 ? 2191 HOH C O 1 HETATM 11635 O O . HOH Y 7 . ? 54.846 -32.383 5.661 1.00 54.32 ? 2192 HOH C O 1 HETATM 11636 O O . HOH Y 7 . ? 55.878 -30.333 2.873 1.00 60.85 ? 2193 HOH C O 1 HETATM 11637 O O . HOH Y 7 . ? 41.423 -34.455 3.123 1.00 53.92 ? 2194 HOH C O 1 HETATM 11638 O O . HOH Y 7 . ? 43.167 -28.292 5.716 1.00 35.88 ? 2195 HOH C O 1 HETATM 11639 O O . HOH Y 7 . ? 41.960 -23.264 13.245 1.00 53.43 ? 2196 HOH C O 1 HETATM 11640 O O . HOH Y 7 . ? 46.582 -30.120 21.454 1.00 43.13 ? 2197 HOH C O 1 HETATM 11641 O O . HOH Y 7 . ? 38.617 -21.629 16.205 1.00 33.23 ? 2198 HOH C O 1 HETATM 11642 O O . HOH Y 7 . ? 41.956 -18.577 12.187 1.00 48.88 ? 2199 HOH C O 1 HETATM 11643 O O . HOH Y 7 . ? 43.157 -19.964 10.185 1.00 41.28 ? 2200 HOH C O 1 HETATM 11644 O O . HOH Y 7 . ? 43.161 -16.963 9.925 1.00 53.43 ? 2201 HOH C O 1 HETATM 11645 O O . HOH Y 7 . ? 41.677 -20.890 7.620 1.00 39.33 ? 2202 HOH C O 1 HETATM 11646 O O . HOH Y 7 . ? 42.160 -18.057 7.189 1.00 47.99 ? 2203 HOH C O 1 HETATM 11647 O O . HOH Y 7 . ? 34.997 -40.521 13.849 1.00 43.15 ? 2204 HOH C O 1 HETATM 11648 O O . HOH Y 7 . ? 35.452 -58.719 5.425 1.00 62.08 ? 2205 HOH C O 1 HETATM 11649 O O . HOH Y 7 . ? 64.061 17.098 38.658 1.00 45.44 ? 2206 HOH C O 1 HETATM 11650 O O . HOH Y 7 . ? 64.494 9.450 45.220 1.00 56.78 ? 2207 HOH C O 1 HETATM 11651 O O . HOH Y 7 . ? 62.082 7.879 47.104 1.00 56.20 ? 2208 HOH C O 1 HETATM 11652 O O . HOH Z 7 . ? 40.247 -6.793 41.374 1.00 47.59 ? 2001 HOH D O 1 HETATM 11653 O O . HOH Z 7 . ? 32.685 -3.647 30.645 1.00 23.06 ? 2002 HOH D O 1 HETATM 11654 O O . HOH Z 7 . ? 33.087 -68.189 -15.531 1.00 71.09 ? 2003 HOH D O 1 HETATM 11655 O O . HOH Z 7 . ? 35.293 -72.936 -24.670 1.00 45.93 ? 2004 HOH D O 1 HETATM 11656 O O . HOH Z 7 . ? 37.092 -38.493 -1.610 1.00 60.85 ? 2005 HOH D O 1 HETATM 11657 O O . HOH Z 7 . ? 33.371 -25.373 -1.899 1.00 47.03 ? 2006 HOH D O 1 HETATM 11658 O O . HOH Z 7 . ? 22.268 -27.628 0.501 1.00 53.46 ? 2007 HOH D O 1 HETATM 11659 O O . HOH Z 7 . ? 35.013 -14.907 17.704 1.00 30.93 ? 2008 HOH D O 1 HETATM 11660 O O . HOH Z 7 . ? 39.053 -14.771 22.679 1.00 39.81 ? 2009 HOH D O 1 HETATM 11661 O O . HOH Z 7 . ? 40.708 -13.030 27.466 1.00 40.98 ? 2010 HOH D O 1 HETATM 11662 O O . HOH Z 7 . ? 44.103 -13.549 22.922 1.00 33.34 ? 2011 HOH D O 1 HETATM 11663 O O . HOH Z 7 . ? 42.439 -10.860 28.531 1.00 39.58 ? 2012 HOH D O 1 HETATM 11664 O O . HOH Z 7 . ? 43.604 -8.277 32.757 1.00 48.00 ? 2013 HOH D O 1 HETATM 11665 O O . HOH Z 7 . ? 44.101 -5.032 33.543 1.00 33.29 ? 2014 HOH D O 1 HETATM 11666 O O . HOH Z 7 . ? 38.277 -7.276 39.497 1.00 27.91 ? 2015 HOH D O 1 HETATM 11667 O O . HOH Z 7 . ? 41.393 -1.894 35.582 1.00 37.39 ? 2016 HOH D O 1 HETATM 11668 O O . HOH Z 7 . ? 33.033 -3.361 33.307 1.00 21.08 ? 2017 HOH D O 1 HETATM 11669 O O . HOH Z 7 . ? 34.601 -2.366 28.346 1.00 39.69 ? 2018 HOH D O 1 HETATM 11670 O O . HOH Z 7 . ? 36.821 -13.159 32.965 1.00 18.06 ? 2019 HOH D O 1 HETATM 11671 O O . HOH Z 7 . ? 41.936 -9.712 34.588 1.00 32.22 ? 2020 HOH D O 1 HETATM 11672 O O . HOH Z 7 . ? 37.536 -13.343 38.553 1.00 44.79 ? 2021 HOH D O 1 HETATM 11673 O O . HOH Z 7 . ? 32.741 -6.254 31.744 1.00 17.74 ? 2022 HOH D O 1 HETATM 11674 O O . HOH Z 7 . ? 30.537 -2.746 37.127 1.00 18.76 ? 2023 HOH D O 1 HETATM 11675 O O . HOH Z 7 . ? 37.937 -14.060 26.852 1.00 29.23 ? 2024 HOH D O 1 HETATM 11676 O O . HOH Z 7 . ? 38.811 -15.367 30.443 1.00 59.76 ? 2025 HOH D O 1 HETATM 11677 O O . HOH Z 7 . ? 36.581 -15.970 32.174 1.00 28.79 ? 2026 HOH D O 1 HETATM 11678 O O . HOH Z 7 . ? 30.441 -22.141 26.829 1.00 29.69 ? 2027 HOH D O 1 HETATM 11679 O O . HOH Z 7 . ? 38.242 -20.400 23.099 1.00 45.77 ? 2028 HOH D O 1 HETATM 11680 O O . HOH Z 7 . ? 39.930 -24.578 24.330 1.00 42.08 ? 2029 HOH D O 1 HETATM 11681 O O . HOH Z 7 . ? 27.709 -24.742 23.471 1.00 30.98 ? 2030 HOH D O 1 HETATM 11682 O O . HOH Z 7 . ? 31.339 -30.697 22.181 1.00 61.83 ? 2031 HOH D O 1 HETATM 11683 O O . HOH Z 7 . ? 29.480 -24.939 25.771 1.00 38.33 ? 2032 HOH D O 1 HETATM 11684 O O . HOH Z 7 . ? 22.341 -50.096 -5.304 1.00 56.97 ? 2033 HOH D O 1 HETATM 11685 O O . HOH Z 7 . ? 23.069 -58.513 1.470 1.00 62.86 ? 2034 HOH D O 1 HETATM 11686 O O . HOH Z 7 . ? 19.379 -51.311 3.387 1.00 61.34 ? 2035 HOH D O 1 HETATM 11687 O O . HOH Z 7 . ? 21.316 -57.088 5.619 1.00 58.79 ? 2036 HOH D O 1 HETATM 11688 O O . HOH Z 7 . ? 16.653 -58.369 0.076 1.00 56.23 ? 2037 HOH D O 1 HETATM 11689 O O . HOH Z 7 . ? 15.361 -72.790 -19.394 1.00 57.45 ? 2038 HOH D O 1 HETATM 11690 O O . HOH Z 7 . ? 19.938 -77.792 -10.163 1.00 55.51 ? 2039 HOH D O 1 HETATM 11691 O O . HOH Z 7 . ? 15.625 -79.585 -16.724 1.00 54.19 ? 2040 HOH D O 1 HETATM 11692 O O . HOH Z 7 . ? 28.318 -68.914 -23.716 1.00 50.36 ? 2041 HOH D O 1 HETATM 11693 O O . HOH Z 7 . ? 37.822 -65.702 -20.776 1.00 51.95 ? 2042 HOH D O 1 HETATM 11694 O O . HOH Z 7 . ? 38.040 -63.431 -22.591 1.00 63.24 ? 2043 HOH D O 1 HETATM 11695 O O . HOH Z 7 . ? 18.044 -60.890 -22.193 1.00 46.43 ? 2044 HOH D O 1 HETATM 11696 O O . HOH AA 7 . ? 4.818 -56.370 27.791 1.00 52.15 ? 2001 HOH E O 1 HETATM 11697 O O . HOH AA 7 . ? 9.656 -57.600 26.956 1.00 55.40 ? 2002 HOH E O 1 HETATM 11698 O O . HOH AA 7 . ? 2.310 -54.552 28.946 1.00 51.99 ? 2003 HOH E O 1 HETATM 11699 O O . HOH AA 7 . ? 1.573 -47.307 28.351 1.00 58.22 ? 2004 HOH E O 1 HETATM 11700 O O . HOH AA 7 . ? 24.354 -17.270 56.277 1.00 44.97 ? 2005 HOH E O 1 HETATM 11701 O O . HOH AA 7 . ? 12.030 -15.019 60.377 1.00 38.66 ? 2006 HOH E O 1 HETATM 11702 O O . HOH AA 7 . ? 9.403 -35.793 28.389 1.00 42.78 ? 2007 HOH E O 1 HETATM 11703 O O . HOH AA 7 . ? 6.776 -36.742 28.788 1.00 52.44 ? 2008 HOH E O 1 HETATM 11704 O O . HOH AA 7 . ? 24.000 0.127 43.910 1.00 37.19 ? 2009 HOH E O 1 HETATM 11705 O O . HOH AA 7 . ? 10.788 -36.985 36.572 1.00 48.74 ? 2010 HOH E O 1 HETATM 11706 O O . HOH AA 7 . ? 7.495 -29.142 39.883 1.00 49.70 ? 2011 HOH E O 1 HETATM 11707 O O . HOH AA 7 . ? 7.177 -27.756 43.688 1.00 56.89 ? 2012 HOH E O 1 HETATM 11708 O O . HOH AA 7 . ? 9.712 -30.695 48.585 1.00 74.18 ? 2013 HOH E O 1 HETATM 11709 O O . HOH AA 7 . ? 28.292 1.145 63.538 1.00 39.46 ? 2014 HOH E O 1 HETATM 11710 O O . HOH AA 7 . ? 22.438 -30.340 55.105 1.00 48.64 ? 2015 HOH E O 1 HETATM 11711 O O . HOH AA 7 . ? 25.690 -20.257 54.565 1.00 36.48 ? 2016 HOH E O 1 HETATM 11712 O O . HOH AA 7 . ? 30.522 -3.199 62.947 1.00 36.45 ? 2017 HOH E O 1 HETATM 11713 O O . HOH AA 7 . ? 21.704 -17.655 54.826 1.00 40.46 ? 2018 HOH E O 1 HETATM 11714 O O . HOH AA 7 . ? 19.616 -15.402 55.829 1.00 31.15 ? 2019 HOH E O 1 HETATM 11715 O O . HOH AA 7 . ? 17.774 -13.586 49.734 1.00 33.83 ? 2020 HOH E O 1 HETATM 11716 O O . HOH AA 7 . ? 17.858 -10.008 48.813 1.00 29.07 ? 2021 HOH E O 1 HETATM 11717 O O . HOH AA 7 . ? 11.866 -12.250 60.774 1.00 41.98 ? 2022 HOH E O 1 HETATM 11718 O O . HOH AA 7 . ? 16.853 -14.478 61.610 1.00 55.93 ? 2023 HOH E O 1 HETATM 11719 O O . HOH AA 7 . ? 27.669 29.493 66.112 1.00 51.41 ? 2024 HOH E O 1 HETATM 11720 O O . HOH AA 7 . ? 16.900 -8.498 55.135 1.00 28.73 ? 2025 HOH E O 1 HETATM 11721 O O . HOH AA 7 . ? 13.567 -6.852 49.789 1.00 30.00 ? 2026 HOH E O 1 HETATM 11722 O O . HOH AA 7 . ? 10.342 -9.193 50.863 1.00 46.07 ? 2027 HOH E O 1 HETATM 11723 O O . HOH AA 7 . ? 11.313 -5.133 53.621 1.00 57.33 ? 2028 HOH E O 1 HETATM 11724 O O . HOH AA 7 . ? 26.688 -6.338 57.111 1.00 42.72 ? 2029 HOH E O 1 HETATM 11725 O O . HOH AA 7 . ? 29.173 -6.301 57.310 1.00 32.21 ? 2030 HOH E O 1 HETATM 11726 O O . HOH AA 7 . ? 30.165 -10.910 56.605 1.00 36.50 ? 2031 HOH E O 1 HETATM 11727 O O . HOH AA 7 . ? 25.019 -4.392 58.878 1.00 26.91 ? 2032 HOH E O 1 HETATM 11728 O O . HOH AA 7 . ? 20.032 20.810 47.192 1.00 40.72 ? 2033 HOH E O 1 HETATM 11729 O O . HOH AA 7 . ? 19.248 1.647 57.504 1.00 48.65 ? 2034 HOH E O 1 HETATM 11730 O O . HOH AA 7 . ? 17.308 0.117 53.912 1.00 27.08 ? 2035 HOH E O 1 HETATM 11731 O O . HOH AA 7 . ? 19.724 -7.930 59.216 1.00 26.25 ? 2036 HOH E O 1 HETATM 11732 O O . HOH AA 7 . ? 16.803 -2.412 62.422 1.00 43.20 ? 2037 HOH E O 1 HETATM 11733 O O . HOH AA 7 . ? 26.609 -12.278 61.174 1.00 48.00 ? 2038 HOH E O 1 HETATM 11734 O O . HOH AA 7 . ? 22.455 -15.566 58.641 1.00 38.57 ? 2039 HOH E O 1 HETATM 11735 O O . HOH AA 7 . ? 33.388 -11.889 59.180 1.00 29.20 ? 2040 HOH E O 1 HETATM 11736 O O . HOH AA 7 . ? 31.958 -14.051 55.572 1.00 42.45 ? 2041 HOH E O 1 HETATM 11737 O O . HOH AA 7 . ? 33.131 -14.455 59.406 1.00 46.07 ? 2042 HOH E O 1 HETATM 11738 O O . HOH AA 7 . ? 26.605 -17.702 54.681 1.00 35.38 ? 2043 HOH E O 1 HETATM 11739 O O . HOH AA 7 . ? 32.396 -21.080 57.829 1.00 46.99 ? 2044 HOH E O 1 HETATM 11740 O O . HOH AA 7 . ? 32.341 -23.730 49.548 1.00 49.97 ? 2045 HOH E O 1 HETATM 11741 O O . HOH AA 7 . ? 29.317 -23.767 46.085 1.00 41.53 ? 2046 HOH E O 1 HETATM 11742 O O . HOH AA 7 . ? 22.203 -5.902 44.218 1.00 33.00 ? 2047 HOH E O 1 HETATM 11743 O O . HOH AA 7 . ? 14.800 -14.365 48.189 1.00 32.56 ? 2048 HOH E O 1 HETATM 11744 O O . HOH AA 7 . ? 12.757 -8.315 44.949 1.00 34.29 ? 2049 HOH E O 1 HETATM 11745 O O . HOH AA 7 . ? 11.869 -7.371 47.821 1.00 44.09 ? 2050 HOH E O 1 HETATM 11746 O O . HOH AA 7 . ? 14.529 0.825 51.224 1.00 48.07 ? 2051 HOH E O 1 HETATM 11747 O O . HOH AA 7 . ? 18.173 0.844 51.246 1.00 25.72 ? 2052 HOH E O 1 HETATM 11748 O O . HOH AA 7 . ? 13.507 -1.803 55.817 1.00 44.04 ? 2053 HOH E O 1 HETATM 11749 O O . HOH AA 7 . ? 18.995 4.003 46.799 1.00 54.55 ? 2054 HOH E O 1 HETATM 11750 O O . HOH AA 7 . ? 21.442 15.254 52.280 1.00 21.89 ? 2055 HOH E O 1 HETATM 11751 O O . HOH AA 7 . ? 20.603 5.653 45.687 1.00 23.02 ? 2056 HOH E O 1 HETATM 11752 O O . HOH AA 7 . ? 23.110 2.955 43.304 1.00 50.41 ? 2057 HOH E O 1 HETATM 11753 O O . HOH AA 7 . ? 21.744 7.582 42.732 1.00 34.34 ? 2058 HOH E O 1 HETATM 11754 O O . HOH AA 7 . ? 26.167 9.548 43.394 1.00 22.49 ? 2059 HOH E O 1 HETATM 11755 O O . HOH AA 7 . ? 28.412 0.092 38.686 1.00 37.36 ? 2060 HOH E O 1 HETATM 11756 O O . HOH AA 7 . ? 35.577 1.198 42.795 1.00 27.88 ? 2061 HOH E O 1 HETATM 11757 O O . HOH AA 7 . ? 33.457 3.092 37.214 1.00 49.02 ? 2062 HOH E O 1 HETATM 11758 O O . HOH AA 7 . ? 32.755 8.039 39.580 1.00 32.26 ? 2063 HOH E O 1 HETATM 11759 O O . HOH AA 7 . ? 29.975 2.403 37.661 1.00 35.03 ? 2064 HOH E O 1 HETATM 11760 O O . HOH AA 7 . ? 32.313 -1.273 35.540 1.00 27.62 ? 2065 HOH E O 1 HETATM 11761 O O . HOH AA 7 . ? 36.752 0.087 40.593 1.00 30.04 ? 2066 HOH E O 1 HETATM 11762 O O . HOH AA 7 . ? 35.375 0.825 33.883 1.00 32.73 ? 2067 HOH E O 1 HETATM 11763 O O . HOH AA 7 . ? 23.279 -4.996 39.382 1.00 39.60 ? 2068 HOH E O 1 HETATM 11764 O O . HOH AA 7 . ? 25.547 -0.121 39.559 1.00 39.57 ? 2069 HOH E O 1 HETATM 11765 O O . HOH AA 7 . ? 35.753 -8.037 38.404 1.00 23.12 ? 2070 HOH E O 1 HETATM 11766 O O . HOH AA 7 . ? 28.915 -13.386 36.526 1.00 57.23 ? 2071 HOH E O 1 HETATM 11767 O O . HOH AA 7 . ? 32.810 -17.265 60.264 1.00 53.21 ? 2072 HOH E O 1 HETATM 11768 O O . HOH AA 7 . ? 32.801 -11.451 56.775 1.00 40.03 ? 2073 HOH E O 1 HETATM 11769 O O . HOH AA 7 . ? 37.407 -11.892 61.727 1.00 55.82 ? 2074 HOH E O 1 HETATM 11770 O O . HOH AA 7 . ? 36.150 -7.830 63.324 1.00 46.00 ? 2075 HOH E O 1 HETATM 11771 O O . HOH AA 7 . ? 36.409 0.746 64.772 1.00 38.48 ? 2076 HOH E O 1 HETATM 11772 O O . HOH AA 7 . ? 35.461 -2.517 63.726 1.00 33.29 ? 2077 HOH E O 1 HETATM 11773 O O . HOH AA 7 . ? 37.716 4.372 60.537 1.00 31.76 ? 2078 HOH E O 1 HETATM 11774 O O . HOH AA 7 . ? 37.299 2.150 67.618 1.00 45.16 ? 2079 HOH E O 1 HETATM 11775 O O . HOH AA 7 . ? 37.582 8.710 67.114 1.00 40.37 ? 2080 HOH E O 1 HETATM 11776 O O . HOH AA 7 . ? 30.892 2.812 62.948 1.00 44.38 ? 2081 HOH E O 1 HETATM 11777 O O . HOH AA 7 . ? 28.480 6.817 64.593 1.00 43.25 ? 2082 HOH E O 1 HETATM 11778 O O . HOH AA 7 . ? 36.279 10.980 67.501 1.00 42.61 ? 2083 HOH E O 1 HETATM 11779 O O . HOH AA 7 . ? 41.250 13.894 70.642 1.00 41.73 ? 2084 HOH E O 1 HETATM 11780 O O . HOH AA 7 . ? 36.085 13.745 68.536 1.00 56.94 ? 2085 HOH E O 1 HETATM 11781 O O . HOH AA 7 . ? 31.410 11.870 62.501 1.00 29.57 ? 2086 HOH E O 1 HETATM 11782 O O . HOH AA 7 . ? 29.965 8.353 62.804 1.00 25.38 ? 2087 HOH E O 1 HETATM 11783 O O . HOH AA 7 . ? 27.308 7.802 67.137 1.00 36.93 ? 2088 HOH E O 1 HETATM 11784 O O . HOH AA 7 . ? 29.312 13.976 62.685 1.00 46.21 ? 2089 HOH E O 1 HETATM 11785 O O . HOH AA 7 . ? 29.389 7.108 60.372 1.00 19.66 ? 2090 HOH E O 1 HETATM 11786 O O . HOH AA 7 . ? 15.037 7.442 60.354 1.00 45.54 ? 2091 HOH E O 1 HETATM 11787 O O . HOH AA 7 . ? 13.262 5.416 55.801 1.00 43.43 ? 2092 HOH E O 1 HETATM 11788 O O . HOH AA 7 . ? 17.566 1.445 69.974 1.00 56.17 ? 2093 HOH E O 1 HETATM 11789 O O . HOH AA 7 . ? 16.990 -4.292 65.150 1.00 38.23 ? 2094 HOH E O 1 HETATM 11790 O O . HOH AA 7 . ? 23.924 0.573 66.420 1.00 40.35 ? 2095 HOH E O 1 HETATM 11791 O O . HOH AA 7 . ? 19.237 12.555 61.648 1.00 36.74 ? 2096 HOH E O 1 HETATM 11792 O O . HOH AA 7 . ? 16.034 10.676 63.543 1.00 40.24 ? 2097 HOH E O 1 HETATM 11793 O O . HOH AA 7 . ? 24.266 3.557 64.863 1.00 33.96 ? 2098 HOH E O 1 HETATM 11794 O O . HOH AA 7 . ? 27.055 2.935 61.792 1.00 29.11 ? 2099 HOH E O 1 HETATM 11795 O O . HOH AA 7 . ? 29.383 4.382 60.653 1.00 21.46 ? 2100 HOH E O 1 HETATM 11796 O O . HOH AA 7 . ? 30.751 -0.364 63.172 1.00 46.38 ? 2101 HOH E O 1 HETATM 11797 O O . HOH AA 7 . ? 26.506 -3.709 65.165 1.00 43.90 ? 2102 HOH E O 1 HETATM 11798 O O . HOH AA 7 . ? 34.847 13.263 55.880 1.00 14.11 ? 2103 HOH E O 1 HETATM 11799 O O . HOH AA 7 . ? 30.767 19.907 63.937 1.00 49.82 ? 2104 HOH E O 1 HETATM 11800 O O . HOH AA 7 . ? 29.844 24.805 61.643 1.00 43.69 ? 2105 HOH E O 1 HETATM 11801 O O . HOH AA 7 . ? 32.442 29.019 64.736 1.00 47.85 ? 2106 HOH E O 1 HETATM 11802 O O . HOH AA 7 . ? 43.097 20.284 56.156 1.00 30.89 ? 2107 HOH E O 1 HETATM 11803 O O . HOH AA 7 . ? 46.041 20.030 57.328 1.00 42.23 ? 2108 HOH E O 1 HETATM 11804 O O . HOH AA 7 . ? 45.933 11.318 59.698 1.00 39.31 ? 2109 HOH E O 1 HETATM 11805 O O . HOH AA 7 . ? 48.782 5.729 59.011 1.00 39.25 ? 2110 HOH E O 1 HETATM 11806 O O . HOH AA 7 . ? 50.369 7.872 55.207 1.00 28.68 ? 2111 HOH E O 1 HETATM 11807 O O . HOH AA 7 . ? 53.864 0.194 54.897 1.00 41.87 ? 2112 HOH E O 1 HETATM 11808 O O . HOH AA 7 . ? 43.146 -14.306 49.050 1.00 34.23 ? 2113 HOH E O 1 HETATM 11809 O O . HOH AA 7 . ? 37.047 -1.367 54.114 1.00 35.53 ? 2114 HOH E O 1 HETATM 11810 O O . HOH AA 7 . ? 23.616 22.298 44.586 1.00 27.01 ? 2115 HOH E O 1 HETATM 11811 O O . HOH AA 7 . ? 21.367 18.562 46.355 1.00 38.19 ? 2116 HOH E O 1 HETATM 11812 O O . HOH AA 7 . ? 25.032 27.191 49.617 1.00 33.40 ? 2117 HOH E O 1 HETATM 11813 O O . HOH AA 7 . ? 31.960 25.301 50.757 1.00 43.34 ? 2118 HOH E O 1 HETATM 11814 O O . HOH AA 7 . ? 23.924 23.519 55.893 1.00 32.22 ? 2119 HOH E O 1 HETATM 11815 O O . HOH AA 7 . ? 42.467 21.793 53.708 1.00 39.19 ? 2120 HOH E O 1 HETATM 11816 O O . HOH AA 7 . ? 39.739 23.950 50.628 1.00 39.49 ? 2121 HOH E O 1 HETATM 11817 O O . HOH AA 7 . ? 32.164 24.410 47.954 1.00 42.86 ? 2122 HOH E O 1 HETATM 11818 O O . HOH AA 7 . ? 32.852 21.577 47.116 1.00 39.96 ? 2123 HOH E O 1 HETATM 11819 O O . HOH AA 7 . ? 35.065 20.273 47.377 1.00 54.32 ? 2124 HOH E O 1 HETATM 11820 O O . HOH AA 7 . ? 42.167 21.357 47.723 1.00 42.62 ? 2125 HOH E O 1 HETATM 11821 O O . HOH AA 7 . ? 44.825 -2.133 44.769 1.00 33.51 ? 2126 HOH E O 1 HETATM 11822 O O . HOH AA 7 . ? 51.052 -4.521 39.131 1.00 54.54 ? 2127 HOH E O 1 HETATM 11823 O O . HOH AA 7 . ? 47.114 -4.917 43.095 1.00 31.80 ? 2128 HOH E O 1 HETATM 11824 O O . HOH AA 7 . ? 43.426 4.301 39.585 1.00 35.90 ? 2129 HOH E O 1 HETATM 11825 O O . HOH AA 7 . ? 37.888 6.753 40.212 1.00 37.55 ? 2130 HOH E O 1 HETATM 11826 O O . HOH AA 7 . ? 38.098 1.948 43.189 1.00 38.99 ? 2131 HOH E O 1 HETATM 11827 O O . HOH AA 7 . ? 40.242 9.045 39.962 1.00 39.88 ? 2132 HOH E O 1 HETATM 11828 O O . HOH AA 7 . ? 41.906 17.369 43.546 1.00 40.25 ? 2133 HOH E O 1 HETATM 11829 O O . HOH AA 7 . ? 35.706 12.053 41.414 1.00 26.47 ? 2134 HOH E O 1 HETATM 11830 O O . HOH AA 7 . ? 33.521 11.952 42.298 1.00 27.65 ? 2135 HOH E O 1 HETATM 11831 O O . HOH AA 7 . ? 33.842 17.588 40.865 1.00 50.10 ? 2136 HOH E O 1 HETATM 11832 O O . HOH AA 7 . ? 32.327 12.762 37.220 1.00 40.45 ? 2137 HOH E O 1 HETATM 11833 O O . HOH AA 7 . ? 17.000 19.806 46.414 1.00 42.29 ? 2138 HOH E O 1 HETATM 11834 O O . HOH AA 7 . ? 13.274 16.504 46.530 1.00 24.86 ? 2139 HOH E O 1 HETATM 11835 O O . HOH AA 7 . ? 12.681 10.994 49.436 1.00 31.76 ? 2140 HOH E O 1 HETATM 11836 O O . HOH AA 7 . ? 14.756 20.076 53.807 1.00 57.31 ? 2141 HOH E O 1 HETATM 11837 O O . HOH AA 7 . ? 12.744 8.083 48.313 1.00 32.56 ? 2142 HOH E O 1 HETATM 11838 O O . HOH AA 7 . ? 37.941 -1.882 41.808 1.00 41.75 ? 2143 HOH E O 1 HETATM 11839 O O . HOH AA 7 . ? 40.843 -1.444 42.272 1.00 30.96 ? 2144 HOH E O 1 HETATM 11840 O O . HOH AA 7 . ? 41.108 -4.235 42.585 1.00 35.35 ? 2145 HOH E O 1 HETATM 11841 O O . HOH AA 7 . ? 47.197 -4.780 45.850 1.00 27.93 ? 2146 HOH E O 1 HETATM 11842 O O . HOH AA 7 . ? 55.504 -11.125 53.703 1.00 48.31 ? 2147 HOH E O 1 HETATM 11843 O O . HOH AA 7 . ? 40.986 -20.571 48.909 1.00 36.40 ? 2148 HOH E O 1 HETATM 11844 O O . HOH AA 7 . ? 39.894 -12.054 44.224 1.00 45.10 ? 2149 HOH E O 1 HETATM 11845 O O . HOH AA 7 . ? 36.524 -20.555 41.345 1.00 49.89 ? 2150 HOH E O 1 HETATM 11846 O O . HOH AA 7 . ? 23.855 -18.071 37.464 1.00 44.84 ? 2151 HOH E O 1 HETATM 11847 O O . HOH AA 7 . ? 24.598 -12.963 38.589 1.00 43.76 ? 2152 HOH E O 1 HETATM 11848 O O . HOH AA 7 . ? 19.431 -16.274 38.876 1.00 44.78 ? 2153 HOH E O 1 HETATM 11849 O O . HOH AA 7 . ? 11.510 -22.572 49.989 1.00 42.96 ? 2154 HOH E O 1 HETATM 11850 O O . HOH AA 7 . ? 16.699 -17.753 54.832 1.00 43.49 ? 2155 HOH E O 1 HETATM 11851 O O . HOH AA 7 . ? 13.836 -21.502 56.749 1.00 54.16 ? 2156 HOH E O 1 HETATM 11852 O O . HOH AA 7 . ? 11.870 -26.262 59.175 1.00 49.66 ? 2157 HOH E O 1 HETATM 11853 O O . HOH AA 7 . ? 16.357 -32.136 45.667 1.00 40.45 ? 2158 HOH E O 1 HETATM 11854 O O . HOH AA 7 . ? 9.256 -21.551 43.097 1.00 52.37 ? 2159 HOH E O 1 HETATM 11855 O O . HOH AA 7 . ? 20.053 -34.162 41.108 1.00 50.84 ? 2160 HOH E O 1 HETATM 11856 O O . HOH AA 7 . ? 16.532 -39.926 44.380 1.00 69.84 ? 2161 HOH E O 1 HETATM 11857 O O . HOH AA 7 . ? 15.540 -39.245 38.028 1.00 44.47 ? 2162 HOH E O 1 HETATM 11858 O O . HOH AA 7 . ? 20.892 -27.353 33.789 1.00 43.64 ? 2163 HOH E O 1 HETATM 11859 O O . HOH AA 7 . ? 12.398 -23.630 31.868 1.00 42.88 ? 2164 HOH E O 1 HETATM 11860 O O . HOH AA 7 . ? 10.248 -24.425 35.130 1.00 48.85 ? 2165 HOH E O 1 HETATM 11861 O O . HOH AA 7 . ? 23.481 -23.033 34.460 1.00 44.73 ? 2166 HOH E O 1 HETATM 11862 O O . HOH AA 7 . ? 28.057 -25.592 38.957 1.00 38.81 ? 2167 HOH E O 1 HETATM 11863 O O . HOH AA 7 . ? 14.537 -20.809 29.394 1.00 36.86 ? 2168 HOH E O 1 HETATM 11864 O O . HOH AA 7 . ? 4.554 -32.271 24.827 1.00 54.74 ? 2169 HOH E O 1 HETATM 11865 O O . HOH AA 7 . ? 10.163 -36.473 21.961 1.00 40.63 ? 2170 HOH E O 1 HETATM 11866 O O . HOH AA 7 . ? 11.096 -54.911 20.646 1.00 53.02 ? 2171 HOH E O 1 HETATM 11867 O O . HOH AA 7 . ? 8.885 -50.367 13.139 1.00 58.36 ? 2172 HOH E O 1 HETATM 11868 O O . HOH AA 7 . ? 58.824 -2.963 58.211 1.00 50.10 ? 2173 HOH E O 1 HETATM 11869 O O . HOH AA 7 . ? 26.300 16.537 62.490 1.00 49.60 ? 2174 HOH E O 1 HETATM 11870 O O . HOH AA 7 . ? 22.884 17.833 62.699 1.00 48.52 ? 2175 HOH E O 1 HETATM 11871 O O . HOH AA 7 . ? 19.049 15.454 66.244 1.00 41.25 ? 2176 HOH E O 1 HETATM 11872 O O . HOH BA 7 . ? 1.175 -54.778 16.989 1.00 59.45 ? 2001 HOH F O 1 HETATM 11873 O O . HOH BA 7 . ? -0.152 -56.575 18.623 1.00 59.25 ? 2002 HOH F O 1 HETATM 11874 O O . HOH BA 7 . ? 12.245 -67.199 28.703 1.00 61.96 ? 2003 HOH F O 1 HETATM 11875 O O . HOH BA 7 . ? 0.394 -68.310 15.949 1.00 62.13 ? 2004 HOH F O 1 HETATM 11876 O O . HOH BA 7 . ? 9.943 -71.279 26.194 1.00 44.52 ? 2005 HOH F O 1 HETATM 11877 O O . HOH BA 7 . ? 20.491 -84.458 8.568 1.00 46.52 ? 2006 HOH F O 1 HETATM 11878 O O . HOH BA 7 . ? 32.704 -39.353 17.914 1.00 38.07 ? 2007 HOH F O 1 HETATM 11879 O O . HOH BA 7 . ? 21.419 -9.155 32.781 1.00 43.10 ? 2008 HOH F O 1 HETATM 11880 O O . HOH BA 7 . ? 28.014 -10.583 36.578 1.00 41.81 ? 2009 HOH F O 1 HETATM 11881 O O . HOH BA 7 . ? 20.867 -6.863 35.223 1.00 47.23 ? 2010 HOH F O 1 HETATM 11882 O O . HOH BA 7 . ? 19.821 3.420 29.499 1.00 41.60 ? 2011 HOH F O 1 HETATM 11883 O O . HOH BA 7 . ? 28.026 1.596 27.369 1.00 27.87 ? 2012 HOH F O 1 HETATM 11884 O O . HOH BA 7 . ? 28.877 2.505 30.804 1.00 40.54 ? 2013 HOH F O 1 HETATM 11885 O O . HOH BA 7 . ? 30.421 -2.222 30.185 1.00 36.03 ? 2014 HOH F O 1 HETATM 11886 O O . HOH BA 7 . ? 19.149 -4.751 27.464 1.00 32.84 ? 2015 HOH F O 1 HETATM 11887 O O . HOH BA 7 . ? 17.340 -3.547 29.852 1.00 48.53 ? 2016 HOH F O 1 HETATM 11888 O O . HOH BA 7 . ? 21.614 -10.391 29.869 1.00 19.77 ? 2017 HOH F O 1 HETATM 11889 O O . HOH BA 7 . ? 18.585 -15.235 21.012 1.00 33.80 ? 2018 HOH F O 1 HETATM 11890 O O . HOH BA 7 . ? 11.079 -44.861 7.887 1.00 51.76 ? 2019 HOH F O 1 HETATM 11891 O O . HOH BA 7 . ? 18.092 -79.145 3.076 1.00 51.09 ? 2020 HOH F O 1 HETATM 11892 O O . HOH BA 7 . ? 16.659 -84.336 6.124 1.00 42.56 ? 2021 HOH F O 1 HETATM 11893 O O . HOH BA 7 . ? 4.374 -82.717 6.579 1.00 54.88 ? 2022 HOH F O 1 HETATM 11894 O O . HOH BA 7 . ? 11.913 -84.742 13.694 1.00 49.72 ? 2023 HOH F O 1 HETATM 11895 O O . HOH BA 7 . ? 14.996 -88.405 18.823 1.00 41.92 ? 2024 HOH F O 1 HETATM 11896 O O . HOH BA 7 . ? 20.235 -81.658 7.913 1.00 53.19 ? 2025 HOH F O 1 HETATM 11897 O O . HOH BA 7 . ? 14.810 -15.523 63.534 1.00 41.60 ? 2026 HOH F O 1 HETATM 11898 O O . HOH BA 7 . ? 59.669 35.719 40.643 1.00 52.15 ? 2027 HOH F O 1 HETATM 11899 O O . HOH BA 7 . ? 11.075 32.246 15.260 1.00 44.77 ? 2028 HOH F O 1 HETATM 11900 O O . HOH BA 7 . ? 67.368 -7.324 35.179 1.00 46.26 ? 2029 HOH F O 1 HETATM 11901 O O . HOH BA 7 . ? 73.295 -0.346 42.379 1.00 45.97 ? 2030 HOH F O 1 HETATM 11902 O O . HOH BA 7 . ? 10.158 -6.994 62.071 1.00 40.62 ? 2031 HOH F O 1 HETATM 11903 O O . HOH BA 7 . ? -15.759 -46.530 -19.254 1.00 54.84 ? 2032 HOH F O 1 HETATM 11904 O O . HOH BA 7 . ? -7.735 -54.194 20.219 1.00 55.40 ? 2033 HOH F O 1 HETATM 11905 O O . HOH BA 7 . ? 8.844 20.390 66.581 1.00 48.28 ? 2034 HOH F O 1 HETATM 11906 O O . HOH BA 7 . ? -1.838 -67.445 -23.476 1.00 50.48 ? 2035 HOH F O 1 HETATM 11907 O O . HOH BA 7 . ? 44.936 -57.958 -13.610 1.00 59.75 ? 2036 HOH F O 1 HETATM 11908 O O . HOH BA 7 . ? 12.663 23.223 57.648 1.00 54.47 ? 2037 HOH F O 1 HETATM 11909 O O . HOH BA 7 . ? 25.028 -84.540 9.328 1.00 40.60 ? 2038 HOH F O 1 HETATM 11910 O O . HOH BA 7 . ? 61.707 26.403 46.357 1.00 49.00 ? 2039 HOH F O 1 HETATM 11911 O O . HOH BA 7 . ? 27.279 -24.943 -13.951 1.00 63.59 ? 2040 HOH F O 1 HETATM 11912 O O . HOH BA 7 . ? 30.353 -3.272 5.716 1.00 49.06 ? 2041 HOH F O 1 HETATM 11913 O O . HOH BA 7 . ? 31.090 4.222 5.959 1.00 42.86 ? 2042 HOH F O 1 HETATM 11914 O O . HOH BA 7 . ? 5.792 -45.275 -22.731 1.00 54.70 ? 2043 HOH F O 1 HETATM 11915 O O . HOH BA 7 . ? 46.891 -18.254 30.293 1.00 50.27 ? 2044 HOH F O 1 HETATM 11916 O O . HOH BA 7 . ? 3.455 -80.740 -5.975 1.00 50.15 ? 2045 HOH F O 1 HETATM 11917 O O . HOH BA 7 . ? 3.162 -8.630 41.874 1.00 44.46 ? 2046 HOH F O 1 HETATM 11918 O O . HOH BA 7 . ? 5.510 -12.708 40.234 1.00 48.80 ? 2047 HOH F O 1 HETATM 11919 O O . HOH BA 7 . ? 4.045 -12.017 45.024 1.00 48.15 ? 2048 HOH F O 1 HETATM 11920 O O . HOH BA 7 . ? 38.481 -30.854 51.020 1.00 54.49 ? 2049 HOH F O 1 HETATM 11921 O O . HOH BA 7 . ? 34.623 -1.887 5.584 1.00 47.94 ? 2050 HOH F O 1 HETATM 11922 O O . HOH BA 7 . ? 6.098 -74.444 -21.378 1.00 55.34 ? 2051 HOH F 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 . ASP A 2 ? 2.4360 1.6558 2.8094 -0.5170 -0.7868 -0.8861 1 ASP A N 2 C CA . ASP A 2 ? 2.5146 1.6263 2.5695 -0.5151 -0.7830 -0.8261 1 ASP A CA 3 C C . ASP A 2 ? 2.4345 1.6092 2.3610 -0.5173 -0.6588 -0.7927 1 ASP A C 4 O O . ASP A 2 ? 2.4003 1.5946 2.2097 -0.5273 -0.5688 -0.7677 1 ASP A O 5 C CB . ASP A 2 ? 2.6681 1.6155 2.5808 -0.5012 -0.9240 -0.8083 1 ASP A CB 6 C CG . ASP A 2 ? 2.7814 1.6308 2.7816 -0.4978 -1.0691 -0.8357 1 ASP A CG 7 O OD1 . ASP A 2 ? 2.8094 1.6312 2.7774 -0.5078 -1.0665 -0.8339 1 ASP A OD1 8 O OD2 . ASP A 2 ? 2.8477 1.6411 2.9501 -0.4846 -1.1929 -0.8597 1 ASP A OD2 9 N N . GLN A 3 ? 2.4095 1.6120 2.3672 -0.5071 -0.6616 -0.7942 2 GLN A N 10 C CA . GLN A 3 ? 2.3559 1.5976 2.1837 -0.5057 -0.5670 -0.7616 2 GLN A CA 11 C C . GLN A 3 ? 2.2866 1.6102 2.2572 -0.4988 -0.5525 -0.7832 2 GLN A C 12 O O . GLN A 3 ? 2.3093 1.6296 2.4419 -0.4913 -0.6365 -0.8173 2 GLN A O 13 C CB . GLN A 3 ? 2.4662 1.5735 2.0311 -0.4994 -0.6031 -0.7169 2 GLN A CB 14 C CG . GLN A 3 ? 2.4157 1.5530 1.8342 -0.5007 -0.4959 -0.6821 2 GLN A CG 15 C CD . GLN A 3 ? 2.5328 1.5313 1.7136 -0.4987 -0.5200 -0.6473 2 GLN A CD 16 O OE1 . GLN A 3 ? 2.5219 1.5208 1.6346 -0.4930 -0.4882 -0.6320 2 GLN A OE1 17 N NE2 . GLN A 3 ? 2.6536 1.5232 1.7030 -0.5064 -0.5710 -0.6370 2 GLN A NE2 18 N N . ILE A 4 ? 2.2086 1.6009 2.1248 -0.5012 -0.4501 -0.7652 3 ILE A N 19 C CA . ILE A 4 ? 2.1446 1.6101 2.1678 -0.4962 -0.4238 -0.7810 3 ILE A CA 20 C C . ILE A 4 ? 2.1146 1.5862 1.9703 -0.4911 -0.3566 -0.7411 3 ILE A C 21 O O . ILE A 4 ? 2.1080 1.5715 1.8294 -0.4967 -0.2945 -0.7129 3 ILE A O 22 C CB . ILE A 4 ? 2.0615 1.6380 2.3003 -0.5136 -0.3466 -0.8258 3 ILE A CB 23 C CG1 . ILE A 4 ? 2.0099 1.6504 2.3745 -0.5101 -0.3273 -0.8486 3 ILE A CG1 24 C CG2 . ILE A 4 ? 2.0191 1.6321 2.1728 -0.5318 -0.2299 -0.8100 3 ILE A CG2 25 C CD1 . ILE A 4 ? 1.9565 1.6836 2.5497 -0.5318 -0.2549 -0.9032 3 ILE A CD1 26 N N . CYS A 5 ? 2.0987 1.5831 1.9750 -0.4797 -0.3741 -0.7415 4 CYS A N 27 C CA . CYS A 5 ? 2.0707 1.5602 1.8098 -0.4733 -0.3195 -0.7080 4 CYS A CA 28 C C . CYS A 5 ? 1.9868 1.5577 1.8408 -0.4700 -0.2874 -0.7252 4 CYS A C 29 O O . CYS A 5 ? 1.9822 1.5696 1.9858 -0.4656 -0.3421 -0.7567 4 CYS A O 30 C CB . CYS A 5 ? 2.1797 1.5496 1.7403 -0.4624 -0.3841 -0.6783 4 CYS A CB 31 S SG . CYS A 5 ? 2.2986 1.5468 1.6843 -0.4702 -0.4107 -0.6556 4 CYS A SG 32 N N . ILE A 6 ? 1.9226 1.5376 1.7098 -0.4721 -0.2034 -0.7060 5 ILE A N 33 C CA . ILE A 6 ? 1.8535 1.5348 1.7165 -0.4704 -0.1649 -0.7170 5 ILE A CA 34 C C . ILE A 6 ? 1.8672 1.5096 1.6227 -0.4525 -0.1968 -0.6903 5 ILE A C 35 O O . ILE A 6 ? 1.9214 1.4947 1.5197 -0.4469 -0.2073 -0.6595 5 ILE A O 36 C CB . ILE A 6 ? 1.8006 1.5332 1.6399 -0.4849 -0.0614 -0.7121 5 ILE A CB 37 C CG1 . ILE A 6 ? 1.8021 1.5485 1.7025 -0.5072 -0.0192 -0.7340 5 ILE A CG1 38 C CG2 . ILE A 6 ? 1.7533 1.5418 1.6724 -0.4876 -0.0212 -0.7282 5 ILE A CG2 39 C CD1 . ILE A 6 ? 1.7906 1.5779 1.8978 -0.5210 -0.0208 -0.7855 5 ILE A CD1 40 N N . GLY A 7 ? 1.8240 1.5054 1.6667 -0.4460 -0.2061 -0.7050 6 GLY A N 41 C CA . GLY A 7 ? 1.8345 1.4801 1.5840 -0.4306 -0.2329 -0.6827 6 GLY A CA 42 C C . GLY A 7 ? 1.7702 1.4799 1.6263 -0.4258 -0.2204 -0.6996 6 GLY A C 43 O O . GLY A 7 ? 1.7111 1.4942 1.7054 -0.4372 -0.1744 -0.7286 6 GLY A O 44 N N . TYR A 8 ? 1.7893 1.4611 1.5741 -0.4118 -0.2560 -0.6833 7 TYR A N 45 C CA . TYR A 8 ? 1.7335 1.4606 1.5970 -0.4054 -0.2438 -0.6941 7 TYR A CA 46 C C . TYR A 8 ? 1.7912 1.4514 1.6187 -0.3905 -0.3283 -0.6895 7 TYR A C 47 O O . TYR A 8 ? 1.8833 1.4392 1.5599 -0.3869 -0.3726 -0.6665 7 TYR A O 48 C CB . TYR A 8 ? 1.6780 1.4456 1.4630 -0.4062 -0.1592 -0.6713 7 TYR A CB 49 C CG . TYR A 8 ? 1.7175 1.4213 1.3258 -0.3994 -0.1514 -0.6346 7 TYR A CG 50 C CD1 . TYR A 8 ? 1.7580 1.4104 1.2865 -0.3882 -0.1814 -0.6199 7 TYR A CD1 51 C CD2 . TYR A 8 ? 1.7207 1.4108 1.2490 -0.4063 -0.1082 -0.6183 7 TYR A CD2 52 C CE1 . TYR A 8 ? 1.8020 1.3905 1.1830 -0.3867 -0.1590 -0.5937 7 TYR A CE1 53 C CE2 . TYR A 8 ? 1.7574 1.3906 1.1510 -0.4020 -0.0925 -0.5922 7 TYR A CE2 54 C CZ . TYR A 8 ? 1.7987 1.3810 1.1226 -0.3935 -0.1129 -0.5818 7 TYR A CZ 55 O OH . TYR A 8 ? 1.8422 1.3622 1.0452 -0.3938 -0.0832 -0.5629 7 TYR A OH 56 N N . HIS A 9 ? 1.7495 1.4583 1.7056 -0.3845 -0.3454 -0.7125 8 HIS A N 57 C CA . HIS A 9 ? 1.8119 1.4553 1.7556 -0.3705 -0.4360 -0.7135 8 HIS A CA 58 C C . HIS A 9 ? 1.8584 1.4311 1.6015 -0.3644 -0.4264 -0.6751 8 HIS A C 59 O O . HIS A 9 ? 1.7980 1.4198 1.4861 -0.3659 -0.3424 -0.6569 8 HIS A O 60 C CB . HIS A 9 ? 1.7470 1.4734 1.8857 -0.3662 -0.4392 -0.7481 8 HIS A CB 61 C CG . HIS A 9 ? 1.8045 1.4714 1.9307 -0.3508 -0.5261 -0.7478 8 HIS A CG 62 N ND1 . HIS A 9 ? 1.7492 1.4680 1.9097 -0.3441 -0.4971 -0.7487 8 HIS A ND1 63 C CD2 . HIS A 9 ? 1.9248 1.4702 1.9946 -0.3419 -0.6458 -0.7463 8 HIS A CD2 64 C CE1 . HIS A 9 ? 1.8265 1.4659 1.9594 -0.3312 -0.5926 -0.7480 8 HIS A CE1 65 N NE2 . HIS A 9 ? 1.9426 1.4683 2.0128 -0.3303 -0.6864 -0.7462 8 HIS A NE2 66 N N . ALA A 10 ? 1.9817 1.4252 1.6142 -0.3595 -0.5145 -0.6656 9 ALA A N 67 C CA . ALA A 10 ? 2.0529 1.4061 1.4961 -0.3582 -0.5064 -0.6361 9 ALA A CA 68 C C . ALA A 10 ? 2.1671 1.4096 1.5743 -0.3509 -0.6153 -0.6416 9 ALA A C 69 O O . ALA A 10 ? 2.2168 1.4247 1.7193 -0.3465 -0.7136 -0.6648 9 ALA A O 70 C CB . ALA A 10 ? 2.1397 1.3914 1.3906 -0.3705 -0.4778 -0.6108 9 ALA A CB 71 N N . ASN A 11 ? 2.2147 1.3955 1.4893 -0.3500 -0.6009 -0.6224 10 ASN A N 72 C CA . ASN A 11 ? 2.3443 1.3973 1.5482 -0.3453 -0.7018 -0.6238 10 ASN A CA 73 C C . ASN A 11 ? 2.4354 1.3813 1.4233 -0.3539 -0.6597 -0.5971 10 ASN A C 74 O O . ASN A 11 ? 2.4038 1.3699 1.3079 -0.3633 -0.5571 -0.5802 10 ASN A O 75 C CB . ASN A 11 ? 2.2505 1.4117 1.6737 -0.3289 -0.7434 -0.6520 10 ASN A CB 76 C CG . ASN A 11 ? 2.1049 1.4084 1.6001 -0.3238 -0.6408 -0.6486 10 ASN A CG 77 O OD1 . ASN A 11 ? 2.0469 1.3961 1.4720 -0.3303 -0.5399 -0.6292 10 ASN A OD1 78 N ND2 . ASN A 11 ? 2.0503 1.4187 1.6919 -0.3119 -0.6716 -0.6694 10 ASN A ND2 79 N N . ASN A 12 ? 2.5579 1.3833 1.4631 -0.3517 -0.7393 -0.5964 11 ASN A N 80 C CA . ASN A 12 ? 2.6645 1.3699 1.3621 -0.3635 -0.7001 -0.5756 11 ASN A CA 81 C C . ASN A 12 ? 2.5432 1.3685 1.3460 -0.3495 -0.6595 -0.5786 11 ASN A C 82 O O . ASN A 12 ? 2.6416 1.3672 1.3567 -0.3495 -0.7064 -0.5755 11 ASN A O 83 C CB . ASN A 12 ? 2.9179 1.3710 1.4070 -0.3755 -0.8161 -0.5706 11 ASN A CB 84 C CG . ASN A 12 ? 3.0617 1.3735 1.4326 -0.3902 -0.8706 -0.5680 11 ASN A CG 85 O OD1 . ASN A 12 ? 3.0463 1.3655 1.3505 -0.4041 -0.7838 -0.5581 11 ASN A OD1 86 N ND2 . ASN A 12 ? 3.2098 1.3852 1.5573 -0.3868 -1.0213 -0.5781 11 ASN A ND2 87 N N . SER A 13 ? 2.3458 1.3706 1.3207 -0.3396 -0.5736 -0.5841 12 SER A N 88 C CA . SER A 13 ? 2.2191 1.3733 1.3248 -0.3254 -0.5422 -0.5908 12 SER A CA 89 C C . SER A 13 ? 2.2480 1.3603 1.2251 -0.3303 -0.4780 -0.5731 12 SER A C 90 O O . SER A 13 ? 2.2392 1.3628 1.2451 -0.3214 -0.5001 -0.5763 12 SER A O 91 C CB . SER A 13 ? 2.0303 1.3789 1.3248 -0.3186 -0.4681 -0.6014 12 SER A CB 92 O OG . SER A 13 ? 1.9208 1.3809 1.3299 -0.3076 -0.4374 -0.6087 12 SER A OG 93 N N . THR A 14 ? 2.2768 1.3474 1.1316 -0.3445 -0.3947 -0.5581 13 THR A N 94 C CA . THR A 14 ? 2.3029 1.3339 1.0533 -0.3524 -0.3179 -0.5471 13 THR A CA 95 C C . THR A 14 ? 2.1307 1.3296 1.0264 -0.3367 -0.2554 -0.5491 13 THR A C 96 O O . THR A 14 ? 2.1146 1.3202 0.9716 -0.3418 -0.1738 -0.5430 13 THR A O 97 C CB . THR A 14 ? 2.4897 1.3320 1.0602 -0.3641 -0.3699 -0.5427 13 THR A CB 98 O OG1 . THR A 14 ? 2.4369 1.3367 1.1053 -0.3466 -0.4255 -0.5496 13 THR A OG1 99 C CG2 . THR A 14 ? 2.6850 1.3373 1.1027 -0.3788 -0.4599 -0.5415 13 THR A CG2 100 N N . GLU A 15 ? 2.0128 1.3363 1.0764 -0.3198 -0.2921 -0.5605 14 GLU A N 101 C CA . GLU A 15 ? 1.8680 1.3319 1.0534 -0.3073 -0.2406 -0.5627 14 GLU A CA 102 C C . GLU A 15 ? 1.7620 1.3208 0.9976 -0.3078 -0.1578 -0.5580 14 GLU A C 103 O O . GLU A 15 ? 1.7441 1.3213 1.0017 -0.3125 -0.1523 -0.5597 14 GLU A O 104 C CB . GLU A 15 ? 1.7872 1.3479 1.1379 -0.2944 -0.2904 -0.5809 14 GLU A CB 105 C CG . GLU A 15 ? 1.8553 1.3530 1.1937 -0.2879 -0.3654 -0.5872 14 GLU A CG 106 C CD . GLU A 15 ? 1.7445 1.3653 1.2628 -0.2749 -0.3753 -0.6061 14 GLU A CD 107 O OE1 . GLU A 15 ? 1.6856 1.3800 1.3491 -0.2735 -0.3913 -0.6273 14 GLU A OE1 108 O OE2 . GLU A 15 ? 1.7185 1.3577 1.2345 -0.2683 -0.3612 -0.6023 14 GLU A OE2 109 N N . GLN A 16 ? 1.6938 1.3068 0.9507 -0.3024 -0.1013 -0.5530 15 GLN A N 110 C CA . GLN A 16 ? 1.6191 1.2933 0.9078 -0.3021 -0.0333 -0.5482 15 GLN A CA 111 C C . GLN A 16 ? 1.4988 1.2943 0.9069 -0.2913 -0.0154 -0.5515 15 GLN A C 112 O O . GLN A 16 ? 1.4680 1.3008 0.9251 -0.2839 -0.0342 -0.5563 15 GLN A O 113 C CB . GLN A 16 ? 1.6671 1.2788 0.8770 -0.3075 0.0199 -0.5432 15 GLN A CB 114 C CG . GLN A 16 ? 1.8011 1.2733 0.8708 -0.3259 0.0296 -0.5418 15 GLN A CG 115 C CD . GLN A 16 ? 1.8736 1.2634 0.8634 -0.3370 0.0896 -0.5443 15 GLN A CD 116 O OE1 . GLN A 16 ? 1.8417 1.2571 0.8595 -0.3302 0.1005 -0.5459 15 GLN A OE1 117 N NE2 . GLN A 16 ? 1.9776 1.2617 0.8686 -0.3567 0.1348 -0.5478 15 GLN A NE2 118 N N . VAL A 17 ? 1.4451 1.2873 0.8877 -0.2921 0.0195 -0.5492 16 VAL A N 119 C CA . VAL A 17 ? 1.3627 1.2851 0.8796 -0.2861 0.0403 -0.5500 16 VAL A CA 120 C C . VAL A 17 ? 1.3472 1.2687 0.8568 -0.2829 0.0779 -0.5429 16 VAL A C 121 O O . VAL A 17 ? 1.3889 1.2598 0.8543 -0.2868 0.0962 -0.5409 16 VAL A O 122 C CB . VAL A 17 ? 1.3329 1.3000 0.9055 -0.2934 0.0344 -0.5588 16 VAL A CB 123 C CG1 . VAL A 17 ? 1.3483 1.3151 0.9609 -0.2965 -0.0062 -0.5732 16 VAL A CG1 124 C CG2 . VAL A 17 ? 1.3495 1.2983 0.8951 -0.3011 0.0495 -0.5548 16 VAL A CG2 125 N N . ASP A 18 ? 1.2969 1.2648 0.8526 -0.2768 0.0870 -0.5417 17 ASP A N 126 C CA . ASP A 18 ? 1.2883 1.2529 0.8587 -0.2712 0.1058 -0.5381 17 ASP A CA 127 C C . ASP A 18 ? 1.2801 1.2582 0.8592 -0.2756 0.0993 -0.5359 17 ASP A C 128 O O . ASP A 18 ? 1.2694 1.2659 0.8486 -0.2842 0.0932 -0.5391 17 ASP A O 129 C CB . ASP A 18 ? 1.2647 1.2446 0.8693 -0.2596 0.1114 -0.5385 17 ASP A CB 130 C CG . ASP A 18 ? 1.2938 1.2377 0.8782 -0.2589 0.1316 -0.5425 17 ASP A CG 131 O OD1 . ASP A 18 ? 1.3462 1.2372 0.8766 -0.2686 0.1437 -0.5443 17 ASP A OD1 132 O OD2 . ASP A 18 ? 1.2778 1.2344 0.8899 -0.2511 0.1376 -0.5447 17 ASP A OD2 133 N N . THR A 19 ? 1.2955 1.2531 0.8818 -0.2720 0.1029 -0.5336 18 THR A N 134 C CA . THR A 19 ? 1.3153 1.2587 0.8876 -0.2775 0.0903 -0.5302 18 THR A CA 135 C C . THR A 19 ? 1.3245 1.2488 0.9338 -0.2644 0.0745 -0.5294 18 THR A C 136 O O . THR A 19 ? 1.3067 1.2410 0.9673 -0.2525 0.0821 -0.5346 18 THR A O 137 C CB . THR A 19 ? 1.3373 1.2620 0.8789 -0.2889 0.0967 -0.5302 18 THR A CB 138 O OG1 . THR A 19 ? 1.3638 1.2760 0.8716 -0.3029 0.0922 -0.5298 18 THR A OG1 139 C CG2 . THR A 19 ? 1.3527 1.2499 0.9091 -0.2830 0.1004 -0.5303 18 THR A CG2 140 N N . ILE A 20 ? 1.3641 1.2514 0.9499 -0.2675 0.0499 -0.5254 19 ILE A N 141 C CA . ILE A 20 ? 1.3880 1.2440 1.0155 -0.2537 0.0146 -0.5264 19 ILE A CA 142 C C . ILE A 20 ? 1.3748 1.2340 1.0896 -0.2413 0.0239 -0.5374 19 ILE A C 143 O O . ILE A 20 ? 1.3695 1.2268 1.1691 -0.2262 0.0076 -0.5468 19 ILE A O 144 C CB . ILE A 20 ? 1.4640 1.2498 1.0232 -0.2624 -0.0250 -0.5193 19 ILE A CB 145 C CG1 . ILE A 20 ? 1.5011 1.2651 0.9637 -0.2832 -0.0150 -0.5142 19 ILE A CG1 146 C CG2 . ILE A 20 ? 1.5008 1.2405 1.1037 -0.2460 -0.0815 -0.5210 19 ILE A CG2 147 C CD1 . ILE A 20 ? 1.6049 1.2716 0.9633 -0.3006 -0.0412 -0.5085 19 ILE A CD1 148 N N . MET A 21 ? 1.3750 1.2346 1.0761 -0.2493 0.0531 -0.5396 20 MET A N 149 C CA . MET A 21 ? 1.3769 1.2272 1.1530 -0.2434 0.0750 -0.5539 20 MET A CA 150 C C . MET A 21 ? 1.3725 1.2271 1.1251 -0.2537 0.1313 -0.5595 20 MET A C 151 O O . MET A 21 ? 1.3910 1.2225 1.1784 -0.2566 0.1628 -0.5723 20 MET A O 152 C CB . MET A 21 ? 1.4116 1.2255 1.1865 -0.2446 0.0492 -0.5532 20 MET A CB 153 C CG . MET A 21 ? 1.4292 1.2335 1.1027 -0.2615 0.0554 -0.5408 20 MET A CG 154 S SD . MET A 21 ? 1.4836 1.2322 1.1388 -0.2633 0.0143 -0.5375 20 MET A SD 155 C CE . MET A 21 ? 1.4759 1.2259 1.2219 -0.2581 0.0491 -0.5552 20 MET A CE 156 N N . GLU A 22 ? 1.3620 1.2331 1.0534 -0.2605 0.1416 -0.5520 21 GLU A N 157 C CA . GLU A 22 ? 1.3855 1.2337 1.0241 -0.2720 0.1790 -0.5551 21 GLU A CA 158 C C . GLU A 22 ? 1.3744 1.2346 0.9861 -0.2718 0.1805 -0.5526 21 GLU A C 159 O O . GLU A 22 ? 1.3532 1.2438 0.9414 -0.2716 0.1522 -0.5437 21 GLU A O 160 C CB . GLU A 22 ? 1.4080 1.2414 0.9726 -0.2847 0.1714 -0.5469 21 GLU A CB 161 C CG . GLU A 22 ? 1.4204 1.2413 0.9971 -0.2863 0.1658 -0.5469 21 GLU A CG 162 C CD . GLU A 22 ? 1.4504 1.2478 0.9578 -0.3002 0.1689 -0.5424 21 GLU A CD 163 O OE1 . GLU A 22 ? 1.4886 1.2464 0.9456 -0.3093 0.1903 -0.5455 21 GLU A OE1 164 O OE2 . GLU A 22 ? 1.4471 1.2528 0.9415 -0.3039 0.1486 -0.5366 21 GLU A OE2 165 N N . LYS A 23 ? 1.3987 1.2276 1.0158 -0.2742 0.2179 -0.5634 22 LYS A N 166 C CA . LYS A 23 ? 1.4072 1.2271 0.9806 -0.2765 0.2204 -0.5615 22 LYS A CA 167 C C . LYS A 23 ? 1.4800 1.2305 0.9419 -0.2931 0.2265 -0.5589 22 LYS A C 168 O O . LYS A 23 ? 1.5343 1.2302 0.9561 -0.3049 0.2510 -0.5633 22 LYS A O 169 C CB . LYS A 23 ? 1.4149 1.2201 1.0415 -0.2737 0.2602 -0.5765 22 LYS A CB 170 N N . ASN A 24 ? 1.4893 1.2331 0.9008 -0.2940 0.1982 -0.5526 23 ASN A N 171 C CA . ASN A 24 ? 1.5790 1.2366 0.8766 -0.3086 0.1843 -0.5503 23 ASN A CA 172 C C . ASN A 24 ? 1.6001 1.2377 0.8628 -0.3163 0.1660 -0.5467 23 ASN A C 173 O O . ASN A 24 ? 1.6762 1.2313 0.8681 -0.3308 0.1947 -0.5504 23 ASN A O 174 C CB . ASN A 24 ? 1.6862 1.2330 0.8992 -0.3249 0.2358 -0.5598 23 ASN A CB 175 C CG . ASN A 24 ? 1.6920 1.2323 0.9032 -0.3217 0.2429 -0.5626 23 ASN A CG 176 O OD1 . ASN A 24 ? 1.8048 1.2327 0.9053 -0.3387 0.2644 -0.5670 23 ASN A OD1 177 N ND2 . ASN A 24 ? 1.5841 1.2308 0.9035 -0.3024 0.2255 -0.5601 23 ASN A ND2 178 N N . VAL A 25 ? 1.5345 1.2420 0.8473 -0.3092 0.1245 -0.5420 24 VAL A N 179 C CA . VAL A 25 ? 1.5472 1.2462 0.8430 -0.3161 0.1055 -0.5404 24 VAL A CA 180 C C . VAL A 25 ? 1.5740 1.2562 0.8494 -0.3188 0.0487 -0.5418 24 VAL A C 181 O O . VAL A 25 ? 1.5153 1.2637 0.8625 -0.3115 0.0229 -0.5458 24 VAL A O 182 C CB . VAL A 25 ? 1.4687 1.2476 0.8435 -0.3103 0.1096 -0.5391 24 VAL A CB 183 C CG1 . VAL A 25 ? 1.4880 1.2535 0.8436 -0.3194 0.0967 -0.5389 24 VAL A CG1 184 C CG2 . VAL A 25 ? 1.4476 1.2371 0.8603 -0.3042 0.1471 -0.5402 24 VAL A CG2 185 N N . THR A 26 ? 1.6730 1.2571 0.8537 -0.3304 0.0281 -0.5414 25 THR A N 186 C CA . THR A 26 ? 1.7254 1.2652 0.8819 -0.3323 -0.0414 -0.5451 25 THR A CA 187 C C . THR A 26 ? 1.6669 1.2771 0.9193 -0.3300 -0.0745 -0.5532 25 THR A C 188 O O . THR A 26 ? 1.6628 1.2775 0.9134 -0.3361 -0.0584 -0.5521 25 THR A O 189 C CB . THR A 26 ? 1.8775 1.2614 0.8793 -0.3483 -0.0604 -0.5418 25 THR A CB 190 O OG1 . THR A 26 ? 1.8987 1.2565 0.8611 -0.3585 -0.0165 -0.5392 25 THR A OG1 191 C CG2 . THR A 26 ? 1.9662 1.2528 0.8602 -0.3559 -0.0365 -0.5392 25 THR A CG2 192 N N . VAL A 27 ? 1.6264 1.2874 0.9684 -0.3229 -0.1162 -0.5646 26 VAL A N 193 C CA . VAL A 27 ? 1.5753 1.3029 1.0321 -0.3242 -0.1372 -0.5808 26 VAL A CA 194 C C . VAL A 27 ? 1.6270 1.3155 1.1258 -0.3222 -0.2197 -0.5970 26 VAL A C 195 O O . VAL A 27 ? 1.6812 1.3124 1.1370 -0.3168 -0.2622 -0.5952 26 VAL A O 196 C CB . VAL A 27 ? 1.4720 1.3103 1.0391 -0.3213 -0.0949 -0.5891 26 VAL A CB 197 C CG1 . VAL A 27 ? 1.4358 1.2972 0.9627 -0.3215 -0.0326 -0.5738 26 VAL A CG1 198 C CG2 . VAL A 27 ? 1.4488 1.3132 1.0659 -0.3124 -0.1137 -0.5963 26 VAL A CG2 199 N N . THR A 28 ? 1.6163 1.3310 1.2059 -0.3269 -0.2450 -0.6149 27 THR A N 200 C CA . THR A 28 ? 1.6681 1.3467 1.3318 -0.3238 -0.3344 -0.6366 27 THR A CA 201 C C . THR A 28 ? 1.6046 1.3592 1.4244 -0.3163 -0.3496 -0.6612 27 THR A C 202 O O . THR A 28 ? 1.6590 1.3681 1.5246 -0.3088 -0.4337 -0.6759 27 THR A O 203 C CB . THR A 28 ? 1.6792 1.3620 1.4133 -0.3319 -0.3565 -0.6535 27 THR A CB 204 O OG1 . THR A 28 ? 1.7188 1.3821 1.5729 -0.3268 -0.4474 -0.6821 27 THR A OG1 205 C CG2 . THR A 28 ? 1.5764 1.3704 1.4146 -0.3411 -0.2749 -0.6655 27 THR A CG2 206 N N . HIS A 29 ? 1.5027 1.3602 1.3999 -0.3195 -0.2721 -0.6671 28 HIS A N 207 C CA . HIS A 29 ? 1.4434 1.3720 1.4819 -0.3162 -0.2674 -0.6918 28 HIS A CA 208 C C . HIS A 29 ? 1.3801 1.3574 1.3735 -0.3152 -0.1944 -0.6752 28 HIS A C 209 O O . HIS A 29 ? 1.3367 1.3539 1.3166 -0.3253 -0.1238 -0.6702 28 HIS A O 210 C CB . HIS A 29 ? 1.4017 1.3981 1.6192 -0.3289 -0.2450 -0.7308 28 HIS A CB 211 C CG . HIS A 29 ? 1.4529 1.4144 1.7756 -0.3265 -0.3312 -0.7581 28 HIS A CG 212 N ND1 . HIS A 29 ? 1.4987 1.4157 1.7851 -0.3322 -0.3554 -0.7552 28 HIS A ND1 213 C CD2 . HIS A 29 ? 1.4708 1.4312 1.9440 -0.3182 -0.4065 -0.7911 28 HIS A CD2 214 C CE1 . HIS A 29 ? 1.5448 1.4315 1.9518 -0.3274 -0.4451 -0.7846 28 HIS A CE1 215 N NE2 . HIS A 29 ? 1.5307 1.4423 2.0583 -0.3183 -0.4806 -0.8078 28 HIS A NE2 216 N N . ALA A 30 ? 1.3843 1.3460 1.3479 -0.3034 -0.2186 -0.6671 29 ALA A N 217 C CA . ALA A 30 ? 1.3319 1.3349 1.2623 -0.3003 -0.1618 -0.6532 29 ALA A CA 218 C C . ALA A 30 ? 1.2791 1.3470 1.3459 -0.3000 -0.1547 -0.6796 29 ALA A C 219 O O . ALA A 30 ? 1.2975 1.3669 1.4779 -0.2971 -0.2086 -0.7064 29 ALA A O 220 C CB . ALA A 30 ? 1.3787 1.3160 1.1767 -0.2899 -0.1808 -0.6269 29 ALA A CB 221 N N . GLN A 31 ? 1.2242 1.3379 1.2831 -0.3036 -0.0912 -0.6739 30 GLN A N 222 C CA . GLN A 31 ? 1.1806 1.3475 1.3500 -0.3065 -0.0705 -0.6980 30 GLN A CA 223 C C . GLN A 31 ? 1.1517 1.3270 1.2485 -0.2978 -0.0462 -0.6763 30 GLN A C 224 O O . GLN A 31 ? 1.1336 1.3213 1.1802 -0.3055 0.0100 -0.6655 30 GLN A O 225 C CB . GLN A 31 ? 1.1629 1.3678 1.4154 -0.3301 -0.0031 -0.7252 30 GLN A CB 226 C CG . GLN A 31 ? 1.1395 1.3889 1.5258 -0.3399 0.0285 -0.7607 30 GLN A CG 227 C CD . GLN A 31 ? 1.1398 1.4044 1.6808 -0.3294 -0.0389 -0.7922 30 GLN A CD 228 O OE1 . GLN A 31 ? 1.1208 1.4081 1.7281 -0.3218 -0.0515 -0.8043 30 GLN A OE1 229 N NE2 . GLN A 31 ? 1.1673 1.4132 1.7687 -0.3281 -0.0902 -0.8062 30 GLN A NE2 230 N N . ASP A 32 ? 1.1572 1.3135 1.2430 -0.2821 -0.0959 -0.6704 31 ASP A N 231 C CA . ASP A 32 ? 1.1282 1.2976 1.1742 -0.2732 -0.0790 -0.6563 31 ASP A CA 232 C C . ASP A 32 ? 1.0804 1.3087 1.2332 -0.2819 -0.0398 -0.6811 31 ASP A C 233 O O . ASP A 32 ? 1.0749 1.3273 1.3589 -0.2865 -0.0560 -0.7140 31 ASP A O 234 C CB . ASP A 32 ? 1.1693 1.2899 1.1766 -0.2580 -0.1433 -0.6483 31 ASP A CB 235 C CG . ASP A 32 ? 1.1435 1.2851 1.1433 -0.2490 -0.1313 -0.6416 31 ASP A CG 236 O OD1 . ASP A 32 ? 1.1008 1.2819 1.0888 -0.2519 -0.0752 -0.6341 31 ASP A OD1 237 O OD2 . ASP A 32 ? 1.1781 1.2855 1.1767 -0.2392 -0.1851 -0.6439 31 ASP A OD2 238 N N . ILE A 33 ? 1.0532 1.2955 1.1528 -0.2853 0.0108 -0.6681 32 ILE A N 239 C CA . ILE A 33 ? 1.0293 1.3046 1.1936 -0.2989 0.0594 -0.6893 32 ILE A CA 240 C C . ILE A 33 ? 1.0045 1.2878 1.1282 -0.2874 0.0622 -0.6741 32 ILE A C 241 O O . ILE A 33 ? 1.0058 1.2909 1.1100 -0.2991 0.1092 -0.6764 32 ILE A O 242 C CB . ILE A 33 ? 1.0533 1.3116 1.1747 -0.3231 0.1242 -0.6925 32 ILE A CB 243 C CG1 . ILE A 33 ? 1.0669 1.2896 1.0506 -0.3165 0.1266 -0.6562 32 ILE A CG1 244 C CG2 . ILE A 33 ? 1.0708 1.3277 1.2577 -0.3383 0.1314 -0.7157 32 ILE A CG2 245 C CD1 . ILE A 33 ? 1.1116 1.2945 1.0272 -0.3396 0.1778 -0.6559 32 ILE A CD1 246 N N . LEU A 34 ? 0.9947 1.2694 1.0962 -0.2669 0.0117 -0.6598 33 LEU A N 247 C CA . LEU A 34 ? 0.9730 1.2526 1.0336 -0.2548 0.0125 -0.6442 33 LEU A CA 248 C C . LEU A 34 ? 0.9710 1.2475 1.0700 -0.2403 -0.0407 -0.6497 33 LEU A C 249 O O . LEU A 34 ? 1.0097 1.2408 1.0663 -0.2322 -0.0883 -0.6412 33 LEU A O 250 C CB . LEU A 34 ? 0.9829 1.2313 0.9314 -0.2466 0.0181 -0.6134 33 LEU A CB 251 C CG . LEU A 34 ? 0.9692 1.2181 0.8797 -0.2339 0.0200 -0.5979 33 LEU A CG 252 C CD1 . LEU A 34 ? 0.9499 1.2232 0.8768 -0.2405 0.0533 -0.6025 33 LEU A CD1 253 C CD2 . LEU A 34 ? 0.9843 1.1992 0.8179 -0.2271 0.0256 -0.5767 33 LEU A CD2 254 N N . GLU A 35 ? 0.9400 1.2504 1.1060 -0.2388 -0.0338 -0.6640 34 GLU A N 255 C CA . GLU A 35 ? 0.9434 1.2465 1.1443 -0.2244 -0.0878 -0.6692 34 GLU A CA 256 C C . GLU A 35 ? 0.9471 1.2233 1.0410 -0.2119 -0.0913 -0.6406 34 GLU A C 257 O O . GLU A 35 ? 0.9155 1.2154 0.9823 -0.2124 -0.0487 -0.6304 34 GLU A O 258 C CB . GLU A 35 ? 0.9114 1.2646 1.2443 -0.2290 -0.0742 -0.7005 34 GLU A CB 259 C CG . GLU A 35 ? 0.9241 1.2685 1.3228 -0.2141 -0.1427 -0.7130 34 GLU A CG 260 C CD . GLU A 35 ? 0.9748 1.2746 1.4114 -0.2087 -0.2204 -0.7246 34 GLU A CD 261 O OE1 . GLU A 35 ? 0.9755 1.2860 1.4775 -0.2195 -0.2120 -0.7427 34 GLU A OE1 262 O OE2 . GLU A 35 ? 1.0259 1.2671 1.4172 -0.1950 -0.2933 -0.7158 34 GLU A OE2 263 N N . LYS A 36 ? 0.9979 1.2117 1.0275 -0.2030 -0.1424 -0.6301 35 LYS A N 264 C CA . LYS A 36 ? 1.0198 1.1923 0.9478 -0.1953 -0.1392 -0.6083 35 LYS A CA 265 C C . LYS A 36 ? 1.0482 1.1923 0.9837 -0.1860 -0.1888 -0.6137 35 LYS A C 266 O O . LYS A 36 ? 1.0768 1.1789 0.9285 -0.1820 -0.1841 -0.5989 35 LYS A O 267 C CB . LYS A 36 ? 1.0895 1.1804 0.8972 -0.1995 -0.1415 -0.5913 35 LYS A CB 268 C CG . LYS A 36 ? 1.0605 1.1713 0.8392 -0.2050 -0.0852 -0.5799 35 LYS A CG 269 C CD . LYS A 36 ? 1.0512 1.1800 0.8659 -0.2134 -0.0839 -0.5875 35 LYS A CD 270 C CE . LYS A 36 ? 1.1295 1.1775 0.8707 -0.2186 -0.1150 -0.5836 35 LYS A CE 271 N NZ . LYS A 36 ? 1.1174 1.1874 0.9074 -0.2263 -0.1183 -0.5935 35 LYS A NZ 272 N N . THR A 37 ? 1.0447 1.2075 1.0881 -0.1834 -0.2356 -0.6377 36 THR A N 273 C CA . THR A 37 ? 1.0911 1.2097 1.1418 -0.1736 -0.3015 -0.6444 36 THR A CA 274 C C . THR A 37 ? 1.0219 1.2220 1.2097 -0.1686 -0.2920 -0.6659 36 THR A C 275 O O . THR A 37 ? 0.9595 1.2347 1.2661 -0.1759 -0.2533 -0.6874 36 THR A O 276 C CB . THR A 37 ? 1.1782 1.2185 1.2398 -0.1722 -0.3923 -0.6575 36 THR A CB 277 O OG1 . THR A 37 ? 1.1284 1.2382 1.3611 -0.1747 -0.3992 -0.6889 36 THR A OG1 278 C CG2 . THR A 37 ? 1.2642 1.2062 1.1710 -0.1805 -0.3990 -0.6364 36 THR A CG2 279 N N . HIS A 38 ? 1.0447 1.2187 1.2063 -0.1590 -0.3216 -0.6615 37 HIS A N 280 C CA . HIS A 38 ? 0.9932 1.2333 1.2814 -0.1534 -0.3198 -0.6829 37 HIS A CA 281 C C . HIS A 38 ? 1.0665 1.2381 1.3434 -0.1412 -0.4057 -0.6866 37 HIS A C 282 O O . HIS A 38 ? 1.1608 1.2253 1.2881 -0.1400 -0.4466 -0.6653 37 HIS A O 283 C CB . HIS A 38 ? 0.9245 1.2235 1.1851 -0.1555 -0.2407 -0.6692 37 HIS A CB 284 C CG . HIS A 38 ? 0.9534 1.2008 1.0692 -0.1504 -0.2322 -0.6388 37 HIS A CG 285 N ND1 . HIS A 38 ? 0.9763 1.1957 1.0641 -0.1414 -0.2599 -0.6347 37 HIS A ND1 286 C CD2 . HIS A 38 ? 0.9666 1.1847 0.9711 -0.1547 -0.1933 -0.6154 37 HIS A CD2 287 C CE1 . HIS A 38 ? 1.0051 1.1778 0.9681 -0.1422 -0.2330 -0.6110 37 HIS A CE1 288 N NE2 . HIS A 38 ? 0.9982 1.1715 0.9179 -0.1500 -0.1920 -0.6007 37 HIS A NE2 289 N N . ASN A 39 ? 1.0387 1.2596 1.4686 -0.1348 -0.4310 -0.7158 38 ASN A N 290 C CA . ASN A 39 ? 1.1151 1.2684 1.5571 -0.1217 -0.5269 -0.7242 38 ASN A CA 291 C C . ASN A 39 ? 1.1410 1.2586 1.4601 -0.1161 -0.5181 -0.6994 38 ASN A C 292 O O . ASN A 39 ? 1.2342 1.2569 1.4928 -0.1083 -0.5985 -0.6964 38 ASN A O 293 C CB . ASN A 39 ? 1.0734 1.2930 1.7517 -0.1163 -0.5601 -0.7707 38 ASN A CB 294 C CG . ASN A 39 ? 0.9719 1.3005 1.7526 -0.1205 -0.4737 -0.7851 38 ASN A CG 295 O OD1 . ASN A 39 ? 0.9321 1.2861 1.6058 -0.1252 -0.3993 -0.7583 38 ASN A OD1 296 N ND2 . ASN A 39 ? 0.9384 1.3242 1.9345 -0.1200 -0.4845 -0.8310 38 ASN A ND2 297 N N . GLY A 40 ? 1.0732 1.2575 1.3557 -0.1208 -0.4252 -0.6835 39 GLY A N 298 C CA . GLY A 40 ? 1.0954 1.2489 1.2614 -0.1172 -0.4052 -0.6598 39 GLY A CA 299 C C . GLY A 40 ? 1.0716 1.2649 1.3287 -0.1072 -0.4231 -0.6746 39 GLY A C 300 O O . GLY A 40 ? 1.1149 1.2526 1.2807 -0.1022 -0.4418 -0.6602 39 GLY A O 301 N N . LYS A 41 ? 0.4394 0.9656 0.3232 -0.0528 -0.0655 -0.1986 40 LYS A N 302 C CA . LYS A 41 ? 0.4397 0.9548 0.3225 -0.0458 -0.0733 -0.1695 40 LYS A CA 303 C C . LYS A 41 ? 0.4059 0.9026 0.3258 -0.0355 -0.0736 -0.1634 40 LYS A C 304 O O . LYS A 41 ? 0.3926 0.8850 0.3373 -0.0350 -0.0716 -0.1797 40 LYS A O 305 C CB . LYS A 41 ? 0.4662 0.9939 0.3268 -0.0474 -0.0923 -0.1565 40 LYS A CB 306 C CG . LYS A 41 ? 0.4964 1.0459 0.3435 -0.0560 -0.1006 -0.1751 40 LYS A CG 307 C CD . LYS A 41 ? 0.5244 1.0850 0.3478 -0.0561 -0.1218 -0.1590 40 LYS A CD 308 C CE . LYS A 41 ? 0.5475 1.1307 0.3663 -0.0630 -0.1340 -0.1775 40 LYS A CE 309 N NZ . LYS A 41 ? 0.5941 1.1917 0.3679 -0.0764 -0.1333 -0.1863 40 LYS A NZ 310 N N . LEU A 42 ? 0.4000 0.8842 0.3212 -0.0286 -0.0762 -0.1400 41 LEU A N 311 C CA . LEU A 42 ? 0.3737 0.8412 0.3257 -0.0197 -0.0762 -0.1321 41 LEU A CA 312 C C . LEU A 42 ? 0.3801 0.8557 0.3428 -0.0151 -0.0920 -0.1240 41 LEU A C 313 O O . LEU A 42 ? 0.3897 0.8698 0.3369 -0.0116 -0.1031 -0.1075 41 LEU A O 314 C CB . LEU A 42 ? 0.3653 0.8149 0.3144 -0.0146 -0.0691 -0.1138 41 LEU A CB 315 C CG . LEU A 42 ? 0.3663 0.8091 0.3127 -0.0178 -0.0530 -0.1218 41 LEU A CG 316 C CD1 . LEU A 42 ? 0.3569 0.7843 0.2981 -0.0144 -0.0481 -0.1019 41 LEU A CD1 317 C CD2 . LEU A 42 ? 0.3471 0.7807 0.3214 -0.0157 -0.0460 -0.1400 41 LEU A CD2 318 N N . CYS A 43 ? 0.3727 0.8493 0.3629 -0.0153 -0.0930 -0.1357 42 CYS A N 319 C CA . CYS A 43 ? 0.3836 0.8759 0.3889 -0.0137 -0.1067 -0.1356 42 CYS A CA 320 C C . CYS A 43 ? 0.3574 0.8391 0.3934 -0.0082 -0.1040 -0.1301 42 CYS A C 321 O O . CYS A 43 ? 0.3428 0.8030 0.3876 -0.0074 -0.0918 -0.1290 42 CYS A O 322 C CB . CYS A 43 ? 0.3998 0.9077 0.4100 -0.0232 -0.1099 -0.1582 42 CYS A CB 323 S SG . CYS A 43 ? 0.4428 0.9672 0.4178 -0.0321 -0.1126 -0.1707 42 CYS A SG 324 N N . ASP A 44 ? 0.3590 0.8575 0.4113 -0.0047 -0.1156 -0.1277 43 ASP A N 325 C CA . ASP A 44 ? 0.3410 0.8358 0.4241 -0.0021 -0.1121 -0.1267 43 ASP A CA 326 C C . ASP A 44 ? 0.3273 0.8135 0.4245 -0.0133 -0.1017 -0.1436 43 ASP A C 327 O O . ASP A 44 ? 0.3388 0.8319 0.4304 -0.0223 -0.1031 -0.1591 43 ASP A O 328 C CB . ASP A 44 ? 0.3491 0.8713 0.4515 0.0023 -0.1268 -0.1270 43 ASP A CB 329 C CG . ASP A 44 ? 0.3684 0.8950 0.4586 0.0152 -0.1404 -0.1094 43 ASP A CG 330 O OD1 . ASP A 44 ? 0.3887 0.8986 0.4504 0.0175 -0.1384 -0.0973 43 ASP A OD1 331 O OD2 . ASP A 44 ? 0.3739 0.9206 0.4838 0.0228 -0.1535 -0.1082 43 ASP A OD2 332 N N . LEU A 45 ? 0.3086 0.7770 0.4218 -0.0135 -0.0919 -0.1405 44 LEU A N 333 C CA . LEU A 45 ? 0.3101 0.7646 0.4335 -0.0250 -0.0836 -0.1537 44 LEU A CA 334 C C . LEU A 45 ? 0.3066 0.7783 0.4556 -0.0310 -0.0855 -0.1593 44 LEU A C 335 O O . LEU A 45 ? 0.2929 0.7659 0.4555 -0.0260 -0.0829 -0.1505 44 LEU A O 336 C CB . LEU A 45 ? 0.2956 0.7161 0.4151 -0.0235 -0.0717 -0.1471 44 LEU A CB 337 C CG . LEU A 45 ? 0.3028 0.7008 0.4265 -0.0350 -0.0654 -0.1596 44 LEU A CG 338 C CD1 . LEU A 45 ? 0.3167 0.7139 0.4297 -0.0395 -0.0678 -0.1752 44 LEU A CD1 339 C CD2 . LEU A 45 ? 0.3002 0.6651 0.4210 -0.0322 -0.0567 -0.1507 44 LEU A CD2 340 N N . ASP A 46 ? 0.3284 0.8156 0.4844 -0.0424 -0.0899 -0.1755 45 ASP A N 341 C CA . ASP A 46 ? 0.3348 0.8472 0.5170 -0.0503 -0.0928 -0.1841 45 ASP A CA 342 C C . ASP A 46 ? 0.3157 0.8541 0.5148 -0.0380 -0.0999 -0.1747 45 ASP A C 343 O O . ASP A 46 ? 0.2989 0.8464 0.5218 -0.0410 -0.0947 -0.1765 45 ASP A O 344 C CB . ASP A 46 ? 0.3457 0.8371 0.5386 -0.0646 -0.0800 -0.1895 45 ASP A CB 345 C CG . ASP A 46 ? 0.3754 0.8867 0.5859 -0.0817 -0.0817 -0.2068 45 ASP A CG 346 O OD1 . ASP A 46 ? 0.4096 0.9222 0.6114 -0.0887 -0.0871 -0.2191 45 ASP A OD1 347 O OD2 . ASP A 46 ? 0.3840 0.9116 0.6175 -0.0888 -0.0774 -0.2098 45 ASP A OD2 348 N N . GLY A 47 ? 0.3134 0.8627 0.4994 -0.0245 -0.1120 -0.1655 46 GLY A N 349 C CA . GLY A 47 ? 0.3059 0.8776 0.5065 -0.0105 -0.1231 -0.1569 46 GLY A CA 350 C C . GLY A 47 ? 0.2961 0.8477 0.4942 0.0025 -0.1178 -0.1395 46 GLY A C 351 O O . GLY A 47 ? 0.3090 0.8753 0.5201 0.0156 -0.1274 -0.1326 46 GLY A O 352 N N . VAL A 48 ? 0.2831 0.8011 0.4658 -0.0003 -0.1037 -0.1332 47 VAL A N 353 C CA . VAL A 48 ? 0.2694 0.7656 0.4453 0.0109 -0.0987 -0.1168 47 VAL A CA 354 C C . VAL A 48 ? 0.2748 0.7523 0.4183 0.0152 -0.1003 -0.1058 47 VAL A C 355 O O . VAL A 48 ? 0.2652 0.7301 0.3931 0.0070 -0.0940 -0.1116 47 VAL A O 356 C CB . VAL A 48 ? 0.2585 0.7312 0.4418 0.0040 -0.0818 -0.1174 47 VAL A CB 357 C CG1 . VAL A 48 ? 0.2487 0.6979 0.4229 0.0147 -0.0768 -0.1013 47 VAL A CG1 358 C CG2 . VAL A 48 ? 0.2523 0.7450 0.4657 -0.0027 -0.0780 -0.1283 47 VAL A CG2 359 N N . LYS A 49 ? 0.2815 0.7572 0.4154 0.0278 -0.1086 -0.0909 48 LYS A N 360 C CA . LYS A 49 ? 0.2974 0.7587 0.3991 0.0300 -0.1104 -0.0798 48 LYS A CA 361 C C . LYS A 49 ? 0.2836 0.7149 0.3768 0.0288 -0.0952 -0.0731 48 LYS A C 362 O O . LYS A 49 ? 0.2559 0.6754 0.3644 0.0320 -0.0881 -0.0696 48 LYS A O 363 C CB . LYS A 49 ? 0.3240 0.7896 0.4172 0.0426 -0.1260 -0.0645 48 LYS A CB 364 C CG . LYS A 49 ? 0.3577 0.8097 0.4134 0.0423 -0.1292 -0.0515 48 LYS A CG 365 C CD . LYS A 49 ? 0.3917 0.8438 0.4362 0.0539 -0.1476 -0.0352 48 LYS A CD 366 C CE . LYS A 49 ? 0.4273 0.8617 0.4298 0.0503 -0.1491 -0.0202 48 LYS A CE 367 N NZ . LYS A 49 ? 0.4722 0.9090 0.4557 0.0579 -0.1718 -0.0064 48 LYS A NZ 368 N N . PRO A 50 ? 0.2847 0.7056 0.3543 0.0238 -0.0900 -0.0728 49 PRO A N 369 C CA . PRO A 50 ? 0.2757 0.6713 0.3396 0.0238 -0.0775 -0.0667 49 PRO A CA 370 C C . PRO A 50 ? 0.2818 0.6651 0.3343 0.0322 -0.0801 -0.0480 49 PRO A C 371 O O . PRO A 50 ? 0.3072 0.6989 0.3492 0.0373 -0.0922 -0.0389 49 PRO A O 372 C CB . PRO A 50 ? 0.2836 0.6784 0.3292 0.0163 -0.0722 -0.0752 49 PRO A CB 373 C CG . PRO A 50 ? 0.3056 0.7217 0.3349 0.0144 -0.0834 -0.0768 49 PRO A CG 374 C CD . PRO A 50 ? 0.3016 0.7350 0.3502 0.0175 -0.0945 -0.0798 49 PRO A CD 375 N N . LEU A 51 ? 0.2684 0.6303 0.3225 0.0334 -0.0701 -0.0420 50 LEU A N 376 C CA . LEU A 51 ? 0.2775 0.6239 0.3173 0.0385 -0.0706 -0.0253 50 LEU A CA 377 C C . LEU A 51 ? 0.2890 0.6333 0.3037 0.0311 -0.0656 -0.0245 50 LEU A C 378 O O . LEU A 51 ? 0.2714 0.6088 0.2882 0.0262 -0.0547 -0.0318 50 LEU A O 379 C CB . LEU A 51 ? 0.2583 0.5841 0.3107 0.0415 -0.0617 -0.0212 50 LEU A CB 380 C CG . LEU A 51 ? 0.2680 0.5742 0.3070 0.0451 -0.0603 -0.0055 50 LEU A CG 381 C CD1 . LEU A 51 ? 0.2912 0.5977 0.3232 0.0535 -0.0736 0.0073 50 LEU A CD1 382 C CD2 . LEU A 51 ? 0.2518 0.5401 0.3048 0.0470 -0.0517 -0.0049 50 LEU A CD2 383 N N . ILE A 52 ? 0.3183 0.6698 0.3096 0.0298 -0.0742 -0.0166 51 ILE A N 384 C CA . ILE A 52 ? 0.3363 0.6882 0.2998 0.0207 -0.0687 -0.0149 51 ILE A CA 385 C C . ILE A 52 ? 0.3584 0.6895 0.3064 0.0209 -0.0663 0.0031 51 ILE A C 386 O O . ILE A 52 ? 0.3799 0.7032 0.3122 0.0245 -0.0776 0.0188 51 ILE A O 387 C CB . ILE A 52 ? 0.3595 0.7283 0.2988 0.0163 -0.0797 -0.0145 51 ILE A CB 388 C CG1 . ILE A 52 ? 0.3506 0.7407 0.3052 0.0157 -0.0844 -0.0322 51 ILE A CG1 389 C CG2 . ILE A 52 ? 0.3792 0.7509 0.2881 0.0040 -0.0712 -0.0151 51 ILE A CG2 390 C CD1 . ILE A 52 ? 0.3319 0.7253 0.3012 0.0102 -0.0713 -0.0518 51 ILE A CD1 391 N N . LEU A 53 ? 0.3595 0.6807 0.3114 0.0168 -0.0528 0.0006 52 LEU A N 392 C CA . LEU A 53 ? 0.3772 0.6778 0.3180 0.0158 -0.0493 0.0162 52 LEU A CA 393 C C . LEU A 53 ? 0.4277 0.7280 0.3336 0.0044 -0.0478 0.0256 52 LEU A C 394 O O . LEU A 53 ? 0.4523 0.7342 0.3456 0.0010 -0.0453 0.0395 52 LEU A O 395 C CB . LEU A 53 ? 0.3514 0.6426 0.3111 0.0154 -0.0368 0.0098 52 LEU A CB 396 C CG . LEU A 53 ? 0.3208 0.6027 0.3075 0.0253 -0.0388 0.0074 52 LEU A CG 397 C CD1 . LEU A 53 ? 0.3007 0.5793 0.3051 0.0239 -0.0290 -0.0047 52 LEU A CD1 398 C CD2 . LEU A 53 ? 0.3265 0.5879 0.3123 0.0318 -0.0433 0.0234 52 LEU A CD2 399 N N . ARG A 54 ? 0.4614 0.7810 0.3498 -0.0030 -0.0492 0.0182 53 ARG A N 400 C CA . ARG A 54 ? 0.5189 0.8393 0.3683 -0.0162 -0.0483 0.0274 53 ARG A CA 401 C C . ARG A 54 ? 0.5237 0.8406 0.3661 -0.0282 -0.0313 0.0267 53 ARG A C 402 O O . ARG A 54 ? 0.5094 0.8433 0.3661 -0.0325 -0.0183 0.0078 53 ARG A O 403 C CB . ARG A 54 ? 0.5680 0.8692 0.3941 -0.0123 -0.0654 0.0508 53 ARG A CB 404 C CG . ARG A 54 ? 0.5795 0.8902 0.4113 -0.0015 -0.0838 0.0500 53 ARG A CG 405 C CD . ARG A 54 ? 0.6245 0.9146 0.4328 0.0035 -0.1028 0.0730 53 ARG A CD 406 N NE . ARG A 54 ? 0.6706 0.9603 0.4319 -0.0102 -0.1082 0.0829 53 ARG A NE 407 C CZ . ARG A 54 ? 0.7181 0.9871 0.4492 -0.0084 -0.1269 0.1044 53 ARG A CZ 408 N NH1 . ARG A 54 ? 0.7257 0.9738 0.4729 0.0082 -0.1419 0.1167 53 ARG A NH1 409 N NH2 . ARG A 54 ? 0.7662 1.0341 0.4499 -0.0237 -0.1310 0.1134 53 ARG A NH2 410 N N . ASP A 55 ? 0.5503 0.8452 0.3720 -0.0334 -0.0322 0.0463 54 ASP A N 411 C CA . ASP A 55 ? 0.5610 0.8527 0.3773 -0.0463 -0.0162 0.0463 54 ASP A CA 412 C C . ASP A 55 ? 0.5282 0.8017 0.3725 -0.0378 -0.0130 0.0492 54 ASP A C 413 O O . ASP A 55 ? 0.5193 0.7840 0.3580 -0.0475 -0.0036 0.0543 54 ASP A O 414 C CB . ASP A 55 ? 0.6146 0.8919 0.3860 -0.0620 -0.0176 0.0660 54 ASP A CB 415 C CG . ASP A 55 ? 0.6568 0.9540 0.3953 -0.0751 -0.0170 0.0616 54 ASP A CG 416 O OD1 . ASP A 55 ? 0.6541 0.9809 0.4047 -0.0795 -0.0049 0.0386 54 ASP A OD1 417 O OD2 . ASP A 55 ? 0.6965 0.9784 0.3961 -0.0810 -0.0293 0.0805 54 ASP A OD2 418 N N . CYS A 56 ? 0.4993 0.7683 0.3724 -0.0214 -0.0205 0.0453 55 CYS A N 419 C CA . CYS A 56 ? 0.4779 0.7291 0.3747 -0.0136 -0.0184 0.0477 55 CYS A CA 420 C C . CYS A 56 ? 0.4280 0.6921 0.3568 -0.0085 -0.0110 0.0281 55 CYS A C 421 O O . CYS A 56 ? 0.4142 0.6945 0.3537 -0.0044 -0.0130 0.0148 55 CYS A O 422 C CB . CYS A 56 ? 0.4964 0.7281 0.3990 0.0003 -0.0327 0.0601 55 CYS A CB 423 S SG . CYS A 56 ? 0.5761 0.7792 0.4442 -0.0026 -0.0440 0.0863 55 CYS A SG 424 N N . SER A 57 ? 0.4013 0.6562 0.3439 -0.0094 -0.0035 0.0265 56 SER A N 425 C CA . SER A 57 ? 0.3640 0.6230 0.3355 -0.0030 0.0001 0.0115 56 SER A CA 426 C C . SER A 57 ? 0.3458 0.5881 0.3318 0.0088 -0.0076 0.0161 56 SER A C 427 O O . SER A 57 ? 0.3584 0.5861 0.3363 0.0131 -0.0146 0.0300 56 SER A O 428 C CB . SER A 57 ? 0.3535 0.6100 0.3337 -0.0087 0.0093 0.0080 56 SER A CB 429 O OG . SER A 57 ? 0.3611 0.5934 0.3381 -0.0074 0.0069 0.0228 56 SER A OG 430 N N . VAL A 58 ? 0.3116 0.5551 0.3189 0.0137 -0.0063 0.0038 57 VAL A N 431 C CA . VAL A 58 ? 0.2870 0.5157 0.3079 0.0220 -0.0106 0.0057 57 VAL A CA 432 C C . VAL A 58 ? 0.2932 0.5008 0.3124 0.0230 -0.0098 0.0174 57 VAL A C 433 O O . VAL A 58 ? 0.3101 0.5060 0.3309 0.0293 -0.0144 0.0247 57 VAL A O 434 C CB . VAL A 58 ? 0.2634 0.4930 0.3020 0.0238 -0.0089 -0.0086 57 VAL A CB 435 C CG1 . VAL A 58 ? 0.2535 0.4656 0.3018 0.0288 -0.0112 -0.0059 57 VAL A CG1 436 C CG2 . VAL A 58 ? 0.2628 0.5093 0.3038 0.0235 -0.0111 -0.0205 57 VAL A CG2 437 N N . ALA A 59 ? 0.2945 0.4987 0.3120 0.0168 -0.0037 0.0176 58 ALA A N 438 C CA . ALA A 59 ? 0.2931 0.4768 0.3086 0.0160 -0.0026 0.0273 58 ALA A CA 439 C C . ALA A 59 ? 0.3088 0.4799 0.3065 0.0154 -0.0066 0.0431 58 ALA A C 440 O O . ALA A 59 ? 0.3047 0.4558 0.3035 0.0206 -0.0099 0.0508 58 ALA A O 441 C CB . ALA A 59 ? 0.2952 0.4825 0.3140 0.0077 0.0043 0.0224 58 ALA A CB 442 N N . GLY A 60 ? 0.3284 0.5096 0.3085 0.0089 -0.0068 0.0475 59 GLY A N 443 C CA . GLY A 60 ? 0.3586 0.5248 0.3169 0.0079 -0.0132 0.0642 59 GLY A CA 444 C C . GLY A 60 ? 0.3566 0.5167 0.3201 0.0214 -0.0246 0.0684 59 GLY A C 445 O O . GLY A 60 ? 0.3744 0.5131 0.3321 0.0270 -0.0317 0.0802 59 GLY A O 446 N N . TRP A 61 ? 0.3427 0.5224 0.3190 0.0267 -0.0265 0.0572 60 TRP A N 447 C CA . TRP A 61 ? 0.3398 0.5211 0.3277 0.0389 -0.0357 0.0567 60 TRP A CA 448 C C . TRP A 61 ? 0.3341 0.4995 0.3393 0.0465 -0.0345 0.0557 60 TRP A C 449 O O . TRP A 61 ? 0.3439 0.4970 0.3509 0.0553 -0.0419 0.0629 60 TRP A O 450 C CB . TRP A 61 ? 0.3213 0.5273 0.3207 0.0395 -0.0356 0.0426 60 TRP A CB 451 C CG . TRP A 61 ? 0.3148 0.5267 0.3338 0.0493 -0.0410 0.0369 60 TRP A CG 452 C CD1 . TRP A 61 ? 0.3244 0.5322 0.3483 0.0595 -0.0507 0.0432 60 TRP A CD1 453 C CD2 . TRP A 61 ? 0.2928 0.5169 0.3297 0.0490 -0.0371 0.0227 60 TRP A CD2 454 N NE1 . TRP A 61 ? 0.3054 0.5264 0.3516 0.0648 -0.0513 0.0323 60 TRP A NE1 455 C CE2 . TRP A 61 ? 0.2896 0.5193 0.3419 0.0573 -0.0428 0.0206 60 TRP A CE2 456 C CE3 . TRP A 61 ? 0.2791 0.5089 0.3208 0.0425 -0.0301 0.0112 60 TRP A CE3 457 C CZ2 . TRP A 61 ? 0.2728 0.5140 0.3427 0.0563 -0.0399 0.0080 60 TRP A CZ2 458 C CZ3 . TRP A 61 ? 0.2691 0.5052 0.3262 0.0427 -0.0291 0.0003 60 TRP A CZ3 459 C CH2 . TRP A 61 ? 0.2696 0.5115 0.3395 0.0481 -0.0331 -0.0008 60 TRP A CH2 460 N N . LEU A 62 ? 0.3110 0.4758 0.3279 0.0432 -0.0258 0.0465 61 LEU A N 461 C CA . LEU A 62 ? 0.3039 0.4555 0.3347 0.0485 -0.0237 0.0437 61 LEU A CA 462 C C . LEU A 62 ? 0.3193 0.4463 0.3435 0.0494 -0.0237 0.0535 61 LEU A C 463 O O . LEU A 62 ? 0.3425 0.4586 0.3749 0.0576 -0.0263 0.0541 61 LEU A O 464 C CB . LEU A 62 ? 0.2845 0.4388 0.3249 0.0439 -0.0165 0.0326 61 LEU A CB 465 C CG . LEU A 62 ? 0.2761 0.4492 0.3249 0.0433 -0.0169 0.0217 61 LEU A CG 466 C CD1 . LEU A 62 ? 0.2662 0.4346 0.3210 0.0388 -0.0123 0.0128 61 LEU A CD1 467 C CD2 . LEU A 62 ? 0.2699 0.4509 0.3294 0.0498 -0.0208 0.0188 61 LEU A CD2 468 N N . LEU A 63 ? 0.3220 0.4409 0.3327 0.0405 -0.0204 0.0596 62 LEU A N 469 C CA . LEU A 63 ? 0.3345 0.4280 0.3373 0.0391 -0.0205 0.0689 62 LEU A CA 470 C C . LEU A 63 ? 0.3675 0.4472 0.3578 0.0447 -0.0304 0.0819 62 LEU A C 471 O O . LEU A 63 ? 0.3808 0.4364 0.3697 0.0494 -0.0339 0.0881 62 LEU A O 472 C CB . LEU A 63 ? 0.3415 0.4333 0.3350 0.0256 -0.0134 0.0703 62 LEU A CB 473 C CG . LEU A 63 ? 0.3125 0.4142 0.3204 0.0223 -0.0067 0.0574 62 LEU A CG 474 C CD1 . LEU A 63 ? 0.3126 0.4239 0.3170 0.0101 -0.0004 0.0548 62 LEU A CD1 475 C CD2 . LEU A 63 ? 0.3098 0.3931 0.3257 0.0261 -0.0060 0.0553 62 LEU A CD2 476 N N . GLY A 64 ? 0.3834 0.4767 0.3641 0.0450 -0.0364 0.0856 63 GLY A N 477 C CA . GLY A 64 ? 0.4180 0.4972 0.3845 0.0509 -0.0490 0.0989 63 GLY A CA 478 C C . GLY A 64 ? 0.4575 0.5197 0.3943 0.0379 -0.0493 0.1135 63 GLY A C 479 O O . GLY A 64 ? 0.4964 0.5288 0.4206 0.0396 -0.0564 0.1263 63 GLY A O 480 N N . ASN A 65 ? 0.4553 0.5361 0.3807 0.0241 -0.0413 0.1108 64 ASN A N 481 C CA . ASN A 65 ? 0.4938 0.5658 0.3877 0.0084 -0.0400 0.1232 64 ASN A CA 482 C C . ASN A 65 ? 0.5354 0.5932 0.4064 0.0133 -0.0561 0.1386 64 ASN A C 483 O O . ASN A 65 ? 0.5344 0.6105 0.4103 0.0222 -0.0640 0.1345 64 ASN A O 484 C CB . ASN A 65 ? 0.4767 0.5809 0.3679 -0.0041 -0.0287 0.1122 64 ASN A CB 485 C CG . ASN A 65 ? 0.5054 0.6067 0.3649 -0.0242 -0.0228 0.1216 64 ASN A CG 486 O OD1 . ASN A 65 ? 0.5366 0.6137 0.3672 -0.0290 -0.0312 0.1394 64 ASN A OD1 487 N ND2 . ASN A 65 ? 0.4874 0.6137 0.3520 -0.0367 -0.0085 0.1089 64 ASN A ND2 488 N N . PRO A 66 ? 0.5887 0.6123 0.4339 0.0074 -0.0624 0.1566 65 PRO A N 489 C CA . PRO A 66 ? 0.6346 0.6374 0.4554 0.0134 -0.0814 0.1735 65 PRO A CA 490 C C . PRO A 66 ? 0.6572 0.6824 0.4570 0.0077 -0.0863 0.1753 65 PRO A C 491 O O . PRO A 66 ? 0.6895 0.7105 0.4834 0.0200 -0.1045 0.1822 65 PRO A O 492 C CB . PRO A 66 ? 0.6842 0.6475 0.4735 -0.0008 -0.0822 0.1919 65 PRO A CB 493 C CG . PRO A 66 ? 0.6581 0.6158 0.4679 -0.0047 -0.0682 0.1833 65 PRO A CG 494 C CD . PRO A 66 ? 0.6041 0.6033 0.4428 -0.0043 -0.0538 0.1619 65 PRO A CD 495 N N . MET A 67 ? 0.6544 0.7043 0.4445 -0.0101 -0.0707 0.1677 66 MET A N 496 C CA . MET A 67 ? 0.6713 0.7466 0.4424 -0.0170 -0.0724 0.1652 66 MET A CA 497 C C . MET A 67 ? 0.6384 0.7453 0.4395 -0.0013 -0.0764 0.1484 66 MET A C 498 O O . MET A 67 ? 0.6501 0.7765 0.4378 -0.0037 -0.0815 0.1459 66 MET A O 499 C CB . MET A 67 ? 0.6725 0.7691 0.4302 -0.0400 -0.0523 0.1572 66 MET A CB 500 C CG . MET A 67 ? 0.7106 0.7825 0.4413 -0.0602 -0.0440 0.1705 66 MET A CG 501 S SD . MET A 67 ? 0.7958 0.8194 0.4776 -0.0646 -0.0642 0.2016 66 MET A SD 502 C CE . MET A 67 ? 0.8167 0.8622 0.4608 -0.0755 -0.0691 0.2041 66 MET A CE 503 N N . CYS A 68 ? 0.6008 0.7118 0.4402 0.0129 -0.0740 0.1368 67 CYS A N 504 C CA . CYS A 68 ? 0.5707 0.7100 0.4400 0.0252 -0.0754 0.1200 67 CYS A CA 505 C C . CYS A 68 ? 0.5697 0.7018 0.4582 0.0455 -0.0918 0.1222 67 CYS A C 506 O O . CYS A 68 ? 0.5346 0.6858 0.4542 0.0556 -0.0905 0.1076 67 CYS A O 507 C CB . CYS A 68 ? 0.5317 0.6845 0.4294 0.0234 -0.0586 0.1029 67 CYS A CB 508 S SG . CYS A 68 ? 0.5260 0.6954 0.4113 0.0028 -0.0402 0.0948 67 CYS A SG 509 N N . ASP A 69 ? 0.6100 0.7150 0.4799 0.0511 -0.1076 0.1397 68 ASP A N 510 C CA . ASP A 69 ? 0.6141 0.7115 0.5046 0.0723 -0.1247 0.1410 68 ASP A CA 511 C C . ASP A 69 ? 0.6053 0.7337 0.5110 0.0825 -0.1360 0.1313 68 ASP A C 512 O O . ASP A 69 ? 0.5901 0.7235 0.5239 0.1001 -0.1466 0.1257 68 ASP A O 513 C CB . ASP A 69 ? 0.6660 0.7235 0.5307 0.0767 -0.1422 0.1627 68 ASP A CB 514 C CG . ASP A 69 ? 0.6691 0.6930 0.5356 0.0755 -0.1351 0.1683 68 ASP A CG 515 O OD1 . ASP A 69 ? 0.6289 0.6623 0.5206 0.0746 -0.1188 0.1546 68 ASP A OD1 516 O OD2 . ASP A 69 ? 0.7051 0.6912 0.5464 0.0750 -0.1469 0.1866 68 ASP A OD2 517 N N . GLU A 70 ? 0.6077 0.7585 0.4963 0.0709 -0.1336 0.1279 69 GLU A N 518 C CA . GLU A 70 ? 0.5931 0.7774 0.4989 0.0773 -0.1406 0.1148 69 GLU A CA 519 C C . GLU A 70 ? 0.5373 0.7422 0.4865 0.0845 -0.1298 0.0949 69 GLU A C 520 O O . GLU A 70 ? 0.5278 0.7534 0.5016 0.0955 -0.1389 0.0854 69 GLU A O 521 C CB . GLU A 70 ? 0.6095 0.8140 0.4903 0.0609 -0.1346 0.1107 69 GLU A CB 522 C CG . GLU A 70 ? 0.6108 0.8504 0.5092 0.0647 -0.1398 0.0947 69 GLU A CG 523 C CD . GLU A 70 ? 0.6473 0.9042 0.5164 0.0497 -0.1379 0.0915 69 GLU A CD 524 O OE1 . GLU A 70 ? 0.6844 0.9278 0.5179 0.0356 -0.1321 0.1020 69 GLU A OE1 525 O OE2 . GLU A 70 ? 0.6464 0.9314 0.5278 0.0509 -0.1416 0.0774 69 GLU A OE2 526 N N . PHE A 71 ? 0.5033 0.7023 0.4611 0.0774 -0.1111 0.0889 70 PHE A N 527 C CA . PHE A 71 ? 0.4583 0.6739 0.4496 0.0797 -0.0993 0.0710 70 PHE A CA 528 C C . PHE A 71 ? 0.4421 0.6425 0.4561 0.0894 -0.0958 0.0694 70 PHE A C 529 O O . PHE A 71 ? 0.4046 0.6124 0.4382 0.0873 -0.0835 0.0571 70 PHE A O 530 C CB . PHE A 71 ? 0.4344 0.6567 0.4204 0.0651 -0.0819 0.0626 70 PHE A CB 531 C CG . PHE A 71 ? 0.4444 0.6813 0.4075 0.0545 -0.0825 0.0618 70 PHE A CG 532 C CD1 . PHE A 71 ? 0.4393 0.7019 0.4093 0.0553 -0.0879 0.0510 70 PHE A CD1 533 C CD2 . PHE A 71 ? 0.4649 0.6907 0.3987 0.0427 -0.0775 0.0713 70 PHE A CD2 534 C CE1 . PHE A 71 ? 0.4565 0.7329 0.4039 0.0452 -0.0885 0.0488 70 PHE A CE1 535 C CE2 . PHE A 71 ? 0.4802 0.7214 0.3912 0.0318 -0.0768 0.0690 70 PHE A CE2 536 C CZ . PHE A 71 ? 0.4765 0.7427 0.3938 0.0335 -0.0825 0.0576 70 PHE A CZ 537 N N . LEU A 72 ? 0.4677 0.6457 0.4779 0.0997 -0.1071 0.0813 71 LEU A N 538 C CA . LEU A 72 ? 0.4578 0.6210 0.4893 0.1093 -0.1037 0.0780 71 LEU A CA 539 C C . LEU A 72 ? 0.4285 0.6173 0.4959 0.1157 -0.0983 0.0592 71 LEU A C 540 O O . LEU A 72 ? 0.4082 0.5937 0.4879 0.1121 -0.0841 0.0507 71 LEU A O 541 C CB . LEU A 72 ? 0.4944 0.6323 0.5209 0.1230 -0.1208 0.0910 71 LEU A CB 542 C CG . LEU A 72 ? 0.5263 0.6269 0.5195 0.1153 -0.1222 0.1098 71 LEU A CG 543 C CD1 . LEU A 72 ? 0.5685 0.6415 0.5556 0.1300 -0.1429 0.1229 71 LEU A CD1 544 C CD2 . LEU A 72 ? 0.5149 0.5990 0.5103 0.1071 -0.1050 0.1070 71 LEU A CD2 545 N N . ASN A 73 ? 0.4201 0.6341 0.5024 0.1236 -0.1095 0.0528 72 ASN A N 546 C CA . ASN A 73 ? 0.3965 0.6387 0.5131 0.1276 -0.1046 0.0342 72 ASN A CA 547 C C . ASN A 73 ? 0.3723 0.6465 0.4935 0.1219 -0.1076 0.0254 72 ASN A C 548 O O . ASN A 73 ? 0.3877 0.6816 0.5222 0.1315 -0.1223 0.0222 72 ASN A O 549 C CB . ASN A 73 ? 0.4164 0.6617 0.5593 0.1464 -0.1162 0.0303 72 ASN A CB 550 C CG . ASN A 73 ? 0.4339 0.6497 0.5779 0.1522 -0.1114 0.0342 72 ASN A CG 551 O OD1 . ASN A 73 ? 0.4327 0.6490 0.5899 0.1478 -0.0954 0.0234 72 ASN A OD1 552 N ND2 . ASN A 73 ? 0.4645 0.6518 0.5922 0.1612 -0.1257 0.0497 72 ASN A ND2 553 N N . VAL A 74 ? 0.3369 0.6162 0.4491 0.1070 -0.0946 0.0201 73 VAL A N 554 C CA . VAL A 74 ? 0.3228 0.6274 0.4339 0.0996 -0.0971 0.0122 73 VAL A CA 555 C C . VAL A 74 ? 0.2961 0.6285 0.4387 0.0990 -0.0933 -0.0056 73 VAL A C 556 O O . VAL A 74 ? 0.2791 0.6089 0.4378 0.0969 -0.0810 -0.0135 73 VAL A O 557 C CB . VAL A 74 ? 0.3121 0.6098 0.4008 0.0847 -0.0861 0.0126 73 VAL A CB 558 C CG1 . VAL A 74 ? 0.3351 0.6101 0.3936 0.0828 -0.0885 0.0288 73 VAL A CG1 559 C CG2 . VAL A 74 ? 0.2906 0.5800 0.3885 0.0770 -0.0693 0.0044 73 VAL A CG2 560 N N . PRO A 75 ? 0.2900 0.6494 0.4396 0.0990 -0.1035 -0.0125 74 PRO A N 561 C CA . PRO A 75 ? 0.2711 0.6587 0.4491 0.0945 -0.0989 -0.0304 74 PRO A CA 562 C C . PRO A 75 ? 0.2532 0.6383 0.4244 0.0773 -0.0838 -0.0386 74 PRO A C 563 O O . PRO A 75 ? 0.2503 0.6173 0.3968 0.0705 -0.0791 -0.0322 74 PRO A O 564 C CB . PRO A 75 ? 0.2868 0.7014 0.4696 0.0992 -0.1169 -0.0335 74 PRO A CB 565 C CG . PRO A 75 ? 0.3046 0.7033 0.4506 0.0969 -0.1243 -0.0194 74 PRO A CG 566 C CD . PRO A 75 ? 0.3095 0.6742 0.4384 0.1009 -0.1195 -0.0043 74 PRO A CD 567 N N . GLU A 76 ? 0.2433 0.6468 0.4373 0.0702 -0.0766 -0.0535 75 GLU A N 568 C CA . GLU A 76 ? 0.2381 0.6374 0.4266 0.0538 -0.0648 -0.0619 75 GLU A CA 569 C C . GLU A 76 ? 0.2387 0.6371 0.4056 0.0481 -0.0700 -0.0608 75 GLU A C 570 O O . GLU A 76 ? 0.2582 0.6751 0.4234 0.0522 -0.0830 -0.0610 75 GLU A O 571 C CB . GLU A 76 ? 0.2449 0.6704 0.4606 0.0460 -0.0607 -0.0784 75 GLU A CB 572 C CG . GLU A 76 ? 0.2580 0.6788 0.4684 0.0276 -0.0510 -0.0878 75 GLU A CG 573 C CD . GLU A 76 ? 0.2687 0.7127 0.5047 0.0170 -0.0445 -0.1031 75 GLU A CD 574 O OE1 . GLU A 76 ? 0.2865 0.7559 0.5480 0.0251 -0.0474 -0.1085 75 GLU A OE1 575 O OE2 . GLU A 76 ? 0.2857 0.7222 0.5165 0.0003 -0.0364 -0.1104 75 GLU A OE2 576 N N . TRP A 77 ? 0.2252 0.6027 0.3760 0.0390 -0.0605 -0.0605 76 TRP A N 577 C CA . TRP A 77 ? 0.2260 0.6032 0.3587 0.0331 -0.0630 -0.0631 76 TRP A CA 578 C C . TRP A 77 ? 0.2123 0.5868 0.3488 0.0198 -0.0559 -0.0766 76 TRP A C 579 O O . TRP A 77 ? 0.2028 0.5715 0.3513 0.0134 -0.0483 -0.0815 76 TRP A O 580 C CB . TRP A 77 ? 0.2330 0.5885 0.3431 0.0357 -0.0601 -0.0518 76 TRP A CB 581 C CG . TRP A 77 ? 0.2316 0.5613 0.3403 0.0326 -0.0485 -0.0498 76 TRP A CG 582 C CD1 . TRP A 77 ? 0.2293 0.5456 0.3336 0.0245 -0.0418 -0.0568 76 TRP A CD1 583 C CD2 . TRP A 77 ? 0.2276 0.5412 0.3392 0.0380 -0.0440 -0.0407 76 TRP A CD2 584 N NE1 . TRP A 77 ? 0.2291 0.5225 0.3325 0.0246 -0.0345 -0.0516 76 TRP A NE1 585 C CE2 . TRP A 77 ? 0.2236 0.5155 0.3307 0.0320 -0.0350 -0.0420 76 TRP A CE2 586 C CE3 . TRP A 77 ? 0.2335 0.5476 0.3509 0.0479 -0.0480 -0.0321 76 TRP A CE3 587 C CZ2 . TRP A 77 ? 0.2220 0.4946 0.3287 0.0342 -0.0292 -0.0352 76 TRP A CZ2 588 C CZ3 . TRP A 77 ? 0.2283 0.5223 0.3465 0.0503 -0.0411 -0.0263 76 TRP A CZ3 589 C CH2 . TRP A 77 ? 0.2223 0.4968 0.3344 0.0428 -0.0316 -0.0278 76 TRP A CH2 590 N N . SER A 78 ? 0.2194 0.5973 0.3442 0.0147 -0.0586 -0.0831 77 SER A N 591 C CA . SER A 78 ? 0.2215 0.5930 0.3484 0.0028 -0.0539 -0.0966 77 SER A CA 592 C C . SER A 78 ? 0.2219 0.5696 0.3336 0.0020 -0.0486 -0.0959 77 SER A C 593 O O . SER A 78 ? 0.2293 0.5577 0.3424 -0.0046 -0.0434 -0.1018 77 SER A O 594 C CB . SER A 78 ? 0.2299 0.6252 0.3589 -0.0027 -0.0617 -0.1091 77 SER A CB 595 O OG . SER A 78 ? 0.2360 0.6418 0.3482 0.0027 -0.0690 -0.1059 77 SER A OG 596 N N . TYR A 79 ? 0.2294 0.5789 0.3264 0.0084 -0.0506 -0.0894 78 TYR A N 597 C CA . TYR A 79 ? 0.2346 0.5654 0.3209 0.0094 -0.0447 -0.0881 78 TYR A CA 598 C C . TYR A 79 ? 0.2453 0.5775 0.3180 0.0162 -0.0450 -0.0747 78 TYR A C 599 O O . TYR A 79 ? 0.2529 0.5987 0.3208 0.0201 -0.0517 -0.0667 78 TYR A O 600 C CB . TYR A 79 ? 0.2356 0.5679 0.3174 0.0041 -0.0444 -0.1036 78 TYR A CB 601 C CG . TYR A 79 ? 0.2521 0.6090 0.3234 0.0028 -0.0501 -0.1091 78 TYR A CG 602 C CD1 . TYR A 79 ? 0.2496 0.6251 0.3267 -0.0012 -0.0572 -0.1159 78 TYR A CD1 603 C CD2 . TYR A 79 ? 0.2603 0.6233 0.3147 0.0042 -0.0481 -0.1082 78 TYR A CD2 604 C CE1 . TYR A 79 ? 0.2630 0.6606 0.3282 -0.0028 -0.0639 -0.1208 78 TYR A CE1 605 C CE2 . TYR A 79 ? 0.2748 0.6596 0.3148 0.0012 -0.0533 -0.1130 78 TYR A CE2 606 C CZ . TYR A 79 ? 0.2757 0.6770 0.3205 -0.0018 -0.0622 -0.1188 78 TYR A CZ 607 O OH . TYR A 79 ? 0.2910 0.7138 0.3194 -0.0052 -0.0691 -0.1236 78 TYR A OH 608 N N . ILE A 80 ? 0.2569 0.5734 0.3242 0.0173 -0.0387 -0.0719 79 ILE A N 609 C CA . ILE A 80 ? 0.2720 0.5876 0.3256 0.0206 -0.0372 -0.0599 79 ILE A CA 610 C C . ILE A 80 ? 0.2894 0.6147 0.3304 0.0165 -0.0340 -0.0682 79 ILE A C 611 O O . ILE A 80 ? 0.2963 0.6205 0.3438 0.0140 -0.0307 -0.0830 79 ILE A O 612 C CB . ILE A 80 ? 0.2657 0.5598 0.3234 0.0238 -0.0318 -0.0508 79 ILE A CB 613 C CG1 . ILE A 80 ? 0.2555 0.5434 0.3240 0.0273 -0.0340 -0.0439 79 ILE A CG1 614 C CG2 . ILE A 80 ? 0.2766 0.5687 0.3197 0.0247 -0.0294 -0.0396 79 ILE A CG2 615 C CD1 . ILE A 80 ? 0.2550 0.5208 0.3284 0.0285 -0.0285 -0.0388 79 ILE A CD1 616 N N . VAL A 81 ? 0.3069 0.6414 0.3293 0.0155 -0.0353 -0.0594 80 VAL A N 617 C CA . VAL A 81 ? 0.3168 0.6635 0.3238 0.0094 -0.0303 -0.0668 80 VAL A CA 618 C C . VAL A 81 ? 0.3261 0.6661 0.3195 0.0074 -0.0246 -0.0539 80 VAL A C 619 O O . VAL A 81 ? 0.3298 0.6640 0.3099 0.0086 -0.0296 -0.0367 80 VAL A O 620 C CB . VAL A 81 ? 0.3395 0.7062 0.3293 0.0051 -0.0371 -0.0696 80 VAL A CB 621 C CG1 . VAL A 81 ? 0.3548 0.7353 0.3256 -0.0032 -0.0297 -0.0783 80 VAL A CG1 622 C CG2 . VAL A 81 ? 0.3369 0.7115 0.3412 0.0053 -0.0426 -0.0838 80 VAL A CG2 623 N N . GLU A 82 ? 0.3307 0.6709 0.3293 0.0046 -0.0148 -0.0631 81 GLU A N 624 C CA . GLU A 82 ? 0.3439 0.6810 0.3325 0.0001 -0.0073 -0.0546 81 GLU A CA 625 C C . GLU A 82 ? 0.3622 0.7213 0.3393 -0.0092 0.0014 -0.0684 81 GLU A C 626 O O . GLU A 82 ? 0.3478 0.7193 0.3359 -0.0087 0.0037 -0.0885 81 GLU A O 627 C CB . GLU A 82 ? 0.3376 0.6586 0.3471 0.0050 -0.0034 -0.0553 81 GLU A CB 628 C CG . GLU A 82 ? 0.3536 0.6660 0.3559 0.0013 0.0019 -0.0426 81 GLU A CG 629 C CD . GLU A 82 ? 0.3473 0.6443 0.3702 0.0063 0.0038 -0.0440 81 GLU A CD 630 O OE1 . GLU A 82 ? 0.3516 0.6496 0.3930 0.0104 0.0039 -0.0590 81 GLU A OE1 631 O OE2 . GLU A 82 ? 0.3519 0.6338 0.3712 0.0061 0.0041 -0.0300 81 GLU A OE2 632 N N . LYS A 83 ? 0.3885 0.7522 0.3422 -0.0187 0.0067 -0.0585 82 LYS A N 633 C CA . LYS A 83 ? 0.4147 0.8016 0.3573 -0.0301 0.0183 -0.0727 82 LYS A CA 634 C C . LYS A 83 ? 0.4035 0.7951 0.3719 -0.0288 0.0287 -0.0871 82 LYS A C 635 O O . LYS A 83 ? 0.3756 0.7495 0.3624 -0.0213 0.0263 -0.0807 82 LYS A O 636 C CB . LYS A 83 ? 0.4461 0.8346 0.3519 -0.0437 0.0211 -0.0565 82 LYS A CB 637 C CG . LYS A 83 ? 0.4770 0.8690 0.3543 -0.0467 0.0106 -0.0490 82 LYS A CG 638 C CD . LYS A 83 ? 0.5223 0.9092 0.3585 -0.0606 0.0109 -0.0300 82 LYS A CD 639 C CE . LYS A 83 ? 0.5610 0.9630 0.3645 -0.0693 0.0059 -0.0322 82 LYS A CE 640 N NZ . LYS A 83 ? 0.5635 0.9602 0.3694 -0.0575 -0.0127 -0.0269 82 LYS A NZ 641 N N . ILE A 84 ? 0.4311 0.8479 0.4017 -0.0357 0.0398 -0.1077 83 ILE A N 642 C CA . ILE A 84 ? 0.4237 0.8496 0.4230 -0.0332 0.0486 -0.1244 83 ILE A CA 643 C C . ILE A 84 ? 0.4224 0.8409 0.4184 -0.0397 0.0542 -0.1092 83 ILE A C 644 O O . ILE A 84 ? 0.4128 0.8210 0.4336 -0.0319 0.0526 -0.1103 83 ILE A O 645 C CB . ILE A 84 ? 0.4450 0.9042 0.4498 -0.0395 0.0607 -0.1525 83 ILE A CB 646 C CG1 . ILE A 84 ? 0.4507 0.9136 0.4703 -0.0297 0.0545 -0.1733 83 ILE A CG1 647 C CG2 . ILE A 84 ? 0.4383 0.9103 0.4725 -0.0380 0.0699 -0.1676 83 ILE A CG2 648 C CD1 . ILE A 84 ? 0.4676 0.9210 0.4660 -0.0295 0.0438 -0.1638 83 ILE A CD1 649 N N . ASN A 85 ? 0.4473 0.8681 0.4109 -0.0544 0.0595 -0.0943 84 ASN A N 650 C CA . ASN A 85 ? 0.4566 0.8678 0.4142 -0.0631 0.0651 -0.0793 84 ASN A CA 651 C C . ASN A 85 ? 0.4691 0.8551 0.3920 -0.0689 0.0578 -0.0498 84 ASN A C 652 O O . ASN A 85 ? 0.4939 0.8842 0.3840 -0.0855 0.0638 -0.0408 84 ASN A O 653 C CB . ASN A 85 ? 0.4815 0.9233 0.4376 -0.0795 0.0830 -0.0945 84 ASN A CB 654 C CG . ASN A 85 ? 0.4910 0.9270 0.4549 -0.0868 0.0894 -0.0865 84 ASN A CG 655 O OD1 . ASN A 85 ? 0.4813 0.9125 0.4783 -0.0754 0.0862 -0.0929 84 ASN A OD1 656 N ND2 . ASN A 85 ? 0.5227 0.9574 0.4545 -0.1066 0.0977 -0.0721 84 ASN A ND2 657 N N . PRO A 86 ? 0.4519 0.8103 0.3814 -0.0555 0.0444 -0.0350 85 PRO A N 658 C CA . PRO A 86 ? 0.4675 0.8025 0.3676 -0.0574 0.0346 -0.0097 85 PRO A CA 659 C C . PRO A 86 ? 0.4904 0.8113 0.3720 -0.0706 0.0404 0.0063 85 PRO A C 660 O O . PRO A 86 ? 0.4718 0.7880 0.3731 -0.0705 0.0460 0.0041 85 PRO A O 661 C CB . PRO A 86 ? 0.4429 0.7563 0.3632 -0.0393 0.0218 -0.0031 85 PRO A CB 662 C CG . PRO A 86 ? 0.4181 0.7436 0.3710 -0.0298 0.0236 -0.0242 85 PRO A CG 663 C CD . PRO A 86 ? 0.4209 0.7686 0.3834 -0.0386 0.0372 -0.0415 85 PRO A CD 664 N N . ALA A 87 ? 0.5279 0.8403 0.3703 -0.0826 0.0379 0.0228 86 ALA A N 665 C CA . ALA A 87 ? 0.5630 0.8587 0.3812 -0.0986 0.0433 0.0395 86 ALA A CA 666 C C . ALA A 87 ? 0.5544 0.8164 0.3834 -0.0888 0.0347 0.0554 86 ALA A C 667 O O . ALA A 87 ? 0.5720 0.8257 0.4037 -0.0981 0.0427 0.0588 86 ALA A O 668 C CB . ALA A 87 ? 0.6143 0.9010 0.3838 -0.1123 0.0385 0.0565 86 ALA A CB 669 N N . ASN A 88 ? 0.5374 0.7822 0.3740 -0.0705 0.0192 0.0629 87 ASN A N 670 C CA . ASN A 88 ? 0.5383 0.7506 0.3828 -0.0601 0.0100 0.0775 87 ASN A CA 671 C C . ASN A 88 ? 0.4985 0.7132 0.3831 -0.0453 0.0107 0.0646 87 ASN A C 672 O O . ASN A 88 ? 0.4756 0.6887 0.3756 -0.0297 0.0014 0.0618 87 ASN A O 673 C CB . ASN A 88 ? 0.5560 0.7479 0.3837 -0.0493 -0.0080 0.0939 87 ASN A CB 674 C CG . ASN A 88 ? 0.6023 0.7865 0.3854 -0.0635 -0.0123 0.1094 87 ASN A CG 675 O OD1 . ASN A 88 ? 0.6415 0.8079 0.4001 -0.0790 -0.0076 0.1222 87 ASN A OD1 676 N ND2 . ASN A 88 ? 0.6033 0.8001 0.3738 -0.0598 -0.0216 0.1084 87 ASN A ND2 677 N N . ASP A 89 ? 0.4937 0.7124 0.3940 -0.0514 0.0214 0.0567 88 ASP A N 678 C CA . ASP A 89 ? 0.4559 0.6751 0.3901 -0.0399 0.0217 0.0451 88 ASP A CA 679 C C . ASP A 89 ? 0.4642 0.6537 0.3993 -0.0386 0.0190 0.0576 88 ASP A C 680 O O . ASP A 89 ? 0.4617 0.6273 0.3879 -0.0307 0.0090 0.0713 88 ASP A O 681 C CB . ASP A 89 ? 0.4501 0.6979 0.4037 -0.0457 0.0331 0.0244 88 ASP A CB 682 C CG . ASP A 89 ? 0.4322 0.6785 0.4182 -0.0338 0.0310 0.0128 88 ASP A CG 683 O OD1 . ASP A 89 ? 0.4082 0.6496 0.4048 -0.0206 0.0232 0.0097 88 ASP A OD1 684 O OD2 . ASP A 89 ? 0.4485 0.6981 0.4480 -0.0388 0.0366 0.0070 88 ASP A OD2 685 N N . LEU A 90 ? 0.4660 0.6575 0.4133 -0.0460 0.0270 0.0518 89 LEU A N 686 C CA . LEU A 90 ? 0.4700 0.6341 0.4156 -0.0481 0.0256 0.0626 89 LEU A CA 687 C C . LEU A 90 ? 0.4998 0.6536 0.4164 -0.0667 0.0304 0.0762 89 LEU A C 688 O O . LEU A 90 ? 0.5144 0.6873 0.4296 -0.0829 0.0421 0.0692 89 LEU A O 689 C CB . LEU A 90 ? 0.4564 0.6278 0.4284 -0.0480 0.0304 0.0495 89 LEU A CB 690 C CG . LEU A 90 ? 0.4385 0.6135 0.4359 -0.0322 0.0251 0.0377 89 LEU A CG 691 C CD1 . LEU A 90 ? 0.4210 0.6034 0.4400 -0.0348 0.0285 0.0259 89 LEU A CD1 692 C CD2 . LEU A 90 ? 0.4293 0.5776 0.4246 -0.0197 0.0160 0.0471 89 LEU A CD2 693 N N . CYS A 91 ? 0.5123 0.6360 0.4055 -0.0647 0.0212 0.0949 90 CYS A N 694 C CA . CYS A 91 ? 0.5473 0.6537 0.4067 -0.0828 0.0232 0.1111 90 CYS A CA 695 C C . CYS A 91 ? 0.5360 0.6308 0.3993 -0.0965 0.0314 0.1118 90 CYS A C 696 O O . CYS A 91 ? 0.5491 0.6543 0.3993 -0.1181 0.0428 0.1115 90 CYS A O 697 C CB . CYS A 91 ? 0.5842 0.6562 0.4192 -0.0744 0.0075 0.1314 90 CYS A CB 698 S SG . CYS A 91 ? 0.5809 0.6200 0.4351 -0.0520 -0.0054 0.1360 90 CYS A SG 699 N N . TYR A 92 ? 0.5113 0.5866 0.3929 -0.0853 0.0263 0.1113 91 TYR A N 700 C CA . TYR A 92 ? 0.5054 0.5770 0.3992 -0.0958 0.0337 0.1063 91 TYR A CA 701 C C . TYR A 92 ? 0.4622 0.5719 0.3886 -0.0926 0.0409 0.0840 91 TYR A C 702 O O . TYR A 92 ? 0.4317 0.5495 0.3771 -0.0749 0.0353 0.0752 91 TYR A O 703 C CB . TYR A 92 ? 0.5065 0.5423 0.4056 -0.0849 0.0249 0.1128 91 TYR A CB 704 C CG . TYR A 92 ? 0.5218 0.5437 0.4213 -0.1004 0.0308 0.1135 91 TYR A CG 705 C CD1 . TYR A 92 ? 0.4944 0.5380 0.4211 -0.1026 0.0370 0.0971 91 TYR A CD1 706 C CD2 . TYR A 92 ? 0.5676 0.5537 0.4399 -0.1135 0.0289 0.1306 91 TYR A CD2 707 C CE1 . TYR A 92 ? 0.5091 0.5427 0.4380 -0.1175 0.0417 0.0964 91 TYR A CE1 708 C CE2 . TYR A 92 ? 0.5832 0.5563 0.4561 -0.1297 0.0347 0.1304 91 TYR A CE2 709 C CZ . TYR A 92 ? 0.5530 0.5520 0.4553 -0.1317 0.0414 0.1126 91 TYR A CZ 710 O OH . TYR A 92 ? 0.5726 0.5624 0.4781 -0.1481 0.0465 0.1106 91 TYR A OH 711 N N . PRO A 93 ? 0.4594 0.5929 0.3924 -0.1101 0.0529 0.0743 92 PRO A N 712 C CA . PRO A 93 ? 0.4264 0.5984 0.3910 -0.1052 0.0579 0.0520 92 PRO A CA 713 C C . PRO A 93 ? 0.4018 0.5679 0.3939 -0.0910 0.0510 0.0434 92 PRO A C 714 O O . PRO A 93 ? 0.4004 0.5393 0.3896 -0.0917 0.0471 0.0513 92 PRO A O 715 C CB . PRO A 93 ? 0.4377 0.6353 0.4043 -0.1282 0.0722 0.0437 92 PRO A CB 716 C CG . PRO A 93 ? 0.4739 0.6393 0.4168 -0.1445 0.0735 0.0611 92 PRO A CG 717 C CD . PRO A 93 ? 0.4936 0.6200 0.4081 -0.1350 0.0621 0.0819 92 PRO A CD 718 N N . GLY A 94 ? 0.3794 0.5692 0.3959 -0.0788 0.0489 0.0272 93 GLY A N 719 C CA . GLY A 94 ? 0.3662 0.5502 0.4051 -0.0663 0.0413 0.0193 93 GLY A CA 720 C C . GLY A 94 ? 0.3573 0.5590 0.4148 -0.0514 0.0364 0.0056 93 GLY A C 721 O O . GLY A 94 ? 0.3360 0.5663 0.4012 -0.0532 0.0415 -0.0059 93 GLY A O 722 N N . ASN A 95 ? 0.3634 0.5467 0.4269 -0.0378 0.0268 0.0062 94 ASN A N 723 C CA . ASN A 95 ? 0.3708 0.5622 0.4471 -0.0243 0.0207 -0.0037 94 ASN A CA 724 C C . ASN A 95 ? 0.3651 0.5306 0.4333 -0.0130 0.0130 0.0041 94 ASN A C 725 O O . ASN A 95 ? 0.3725 0.5143 0.4300 -0.0134 0.0115 0.0148 94 ASN A O 726 C CB . ASN A 95 ? 0.3777 0.5850 0.4800 -0.0210 0.0168 -0.0203 94 ASN A CB 727 C CG . ASN A 95 ? 0.4026 0.5931 0.5099 -0.0220 0.0112 -0.0184 94 ASN A CG 728 O OD1 . ASN A 95 ? 0.4247 0.6054 0.5229 -0.0323 0.0155 -0.0103 94 ASN A OD1 729 N ND2 . ASN A 95 ? 0.4034 0.5888 0.5235 -0.0121 0.0007 -0.0261 94 ASN A ND2 730 N N . PHE A 96 ? 0.3540 0.5259 0.4277 -0.0039 0.0091 -0.0023 95 PHE A N 731 C CA . PHE A 96 ? 0.3477 0.5011 0.4171 0.0051 0.0030 0.0015 95 PHE A CA 732 C C . PHE A 96 ? 0.3308 0.4823 0.4141 0.0105 -0.0040 -0.0090 95 PHE A C 733 O O . PHE A 96 ? 0.3218 0.4898 0.4178 0.0133 -0.0058 -0.0207 95 PHE A O 734 C CB . PHE A 96 ? 0.3632 0.5251 0.4265 0.0090 0.0035 0.0022 95 PHE A CB 735 C CG . PHE A 96 ? 0.3836 0.5286 0.4373 0.0143 0.0009 0.0114 95 PHE A CG 736 C CD1 . PHE A 96 ? 0.4044 0.5318 0.4600 0.0185 -0.0027 0.0114 95 PHE A CD1 737 C CD2 . PHE A 96 ? 0.4130 0.5619 0.4562 0.0149 0.0016 0.0188 95 PHE A CD2 738 C CE1 . PHE A 96 ? 0.4165 0.5335 0.4667 0.0229 -0.0034 0.0168 95 PHE A CE1 739 C CE2 . PHE A 96 ? 0.4318 0.5694 0.4712 0.0212 -0.0015 0.0247 95 PHE A CE2 740 C CZ . PHE A 96 ? 0.4238 0.5471 0.4684 0.0251 -0.0030 0.0227 95 PHE A CZ 741 N N . ASN A 97 ? 0.3123 0.4427 0.3926 0.0116 -0.0086 -0.0055 96 ASN A N 742 C CA . ASN A 97 ? 0.3111 0.4331 0.3987 0.0159 -0.0177 -0.0125 96 ASN A CA 743 C C . ASN A 97 ? 0.2864 0.4036 0.3720 0.0219 -0.0219 -0.0154 96 ASN A C 744 O O . ASN A 97 ? 0.2872 0.3982 0.3626 0.0225 -0.0185 -0.0095 96 ASN A O 745 C CB . ASN A 97 ? 0.3506 0.4489 0.4286 0.0137 -0.0207 -0.0064 96 ASN A CB 746 C CG . ASN A 97 ? 0.3830 0.4730 0.4668 0.0156 -0.0317 -0.0128 96 ASN A CG 747 O OD1 . ASN A 97 ? 0.4092 0.5129 0.5080 0.0146 -0.0350 -0.0200 96 ASN A OD1 748 N ND2 . ASN A 97 ? 0.3951 0.4627 0.4664 0.0174 -0.0377 -0.0102 96 ASN A ND2 749 N N . ASP A 98 ? 0.2824 0.4027 0.3791 0.0265 -0.0297 -0.0255 97 ASP A N 750 C CA . ASP A 98 ? 0.2718 0.3837 0.3659 0.0307 -0.0347 -0.0287 97 ASP A CA 751 C C . ASP A 98 ? 0.2507 0.3763 0.3412 0.0301 -0.0267 -0.0275 97 ASP A C 752 O O . ASP A 98 ? 0.2433 0.3593 0.3245 0.0298 -0.0261 -0.0235 97 ASP A O 753 C CB . ASP A 98 ? 0.2900 0.3728 0.3685 0.0292 -0.0400 -0.0219 97 ASP A CB 754 C CG . ASP A 98 ? 0.3073 0.3746 0.3864 0.0301 -0.0511 -0.0236 97 ASP A CG 755 O OD1 . ASP A 98 ? 0.3098 0.3824 0.4032 0.0356 -0.0603 -0.0328 97 ASP A OD1 756 O OD2 . ASP A 98 ? 0.3298 0.3800 0.3955 0.0257 -0.0516 -0.0167 97 ASP A OD2 757 N N . TYR A 99 ? 0.2365 0.3861 0.3343 0.0289 -0.0207 -0.0315 98 TYR A N 758 C CA . TYR A 99 ? 0.2290 0.3927 0.3211 0.0276 -0.0144 -0.0299 98 TYR A CA 759 C C . TYR A 99 ? 0.2260 0.3931 0.3223 0.0314 -0.0181 -0.0393 98 TYR A C 760 O O . TYR A 99 ? 0.2210 0.3892 0.3097 0.0308 -0.0165 -0.0362 98 TYR A O 761 C CB . TYR A 99 ? 0.2263 0.4133 0.3209 0.0228 -0.0069 -0.0321 98 TYR A CB 762 C CG . TYR A 99 ? 0.2268 0.4262 0.3100 0.0200 -0.0015 -0.0277 98 TYR A CG 763 C CD1 . TYR A 99 ? 0.2266 0.4143 0.2967 0.0208 -0.0020 -0.0157 98 TYR A CD1 764 C CD2 . TYR A 99 ? 0.2326 0.4567 0.3180 0.0165 0.0036 -0.0367 98 TYR A CD2 765 C CE1 . TYR A 99 ? 0.2307 0.4295 0.2903 0.0192 0.0000 -0.0114 98 TYR A CE1 766 C CE2 . TYR A 99 ? 0.2413 0.4757 0.3123 0.0130 0.0071 -0.0320 98 TYR A CE2 767 C CZ . TYR A 99 ? 0.2372 0.4581 0.2951 0.0148 0.0040 -0.0187 98 TYR A CZ 768 O OH . TYR A 99 ? 0.2369 0.4682 0.2806 0.0123 0.0048 -0.0141 98 TYR A OH 769 N N . GLU A 100 ? 0.2234 0.3915 0.3328 0.0356 -0.0243 -0.0515 99 GLU A N 770 C CA . GLU A 100 ? 0.2312 0.3997 0.3448 0.0391 -0.0285 -0.0616 99 GLU A CA 771 C C . GLU A 100 ? 0.2303 0.3723 0.3329 0.0382 -0.0340 -0.0554 99 GLU A C 772 O O . GLU A 100 ? 0.2212 0.3642 0.3204 0.0369 -0.0336 -0.0581 99 GLU A O 773 C CB . GLU A 100 ? 0.2390 0.4142 0.3717 0.0454 -0.0348 -0.0779 99 GLU A CB 774 C CG . GLU A 100 ? 0.2426 0.4512 0.3875 0.0442 -0.0263 -0.0882 99 GLU A CG 775 C CD . GLU A 100 ? 0.2463 0.4629 0.3916 0.0390 -0.0207 -0.0810 99 GLU A CD 776 O OE1 . GLU A 100 ? 0.2420 0.4425 0.3903 0.0407 -0.0274 -0.0766 99 GLU A OE1 777 O OE2 . GLU A 100 ? 0.2505 0.4890 0.3913 0.0319 -0.0097 -0.0800 99 GLU A OE2 778 N N . GLU A 101 ? 0.2355 0.3548 0.3312 0.0372 -0.0384 -0.0475 100 GLU A N 779 C CA . GLU A 101 ? 0.2424 0.3367 0.3245 0.0332 -0.0417 -0.0414 100 GLU A CA 780 C C . GLU A 101 ? 0.2477 0.3480 0.3206 0.0282 -0.0326 -0.0336 100 GLU A C 781 O O . GLU A 101 ? 0.2545 0.3461 0.3209 0.0239 -0.0326 -0.0333 100 GLU A O 782 C CB . GLU A 101 ? 0.2384 0.3077 0.3124 0.0321 -0.0485 -0.0356 100 GLU A CB 783 C CG . GLU A 101 ? 0.2457 0.3020 0.3274 0.0378 -0.0621 -0.0435 100 GLU A CG 784 C CD . GLU A 101 ? 0.2614 0.2949 0.3355 0.0365 -0.0702 -0.0463 100 GLU A CD 785 O OE1 . GLU A 101 ? 0.2711 0.2834 0.3260 0.0281 -0.0693 -0.0379 100 GLU A OE1 786 O OE2 . GLU A 101 ? 0.2636 0.2996 0.3507 0.0431 -0.0772 -0.0576 100 GLU A OE2 787 N N . LEU A 102 ? 0.2427 0.3576 0.3160 0.0286 -0.0258 -0.0278 101 LEU A N 788 C CA . LEU A 102 ? 0.2500 0.3725 0.3184 0.0269 -0.0195 -0.0215 101 LEU A CA 789 C C . LEU A 102 ? 0.2534 0.3946 0.3258 0.0273 -0.0186 -0.0272 101 LEU A C 790 O O . LEU A 102 ? 0.2566 0.4007 0.3274 0.0252 -0.0171 -0.0265 101 LEU A O 791 C CB . LEU A 102 ? 0.2501 0.3796 0.3170 0.0280 -0.0149 -0.0137 101 LEU A CB 792 C CG . LEU A 102 ? 0.2559 0.3925 0.3196 0.0290 -0.0110 -0.0074 101 LEU A CG 793 C CD1 . LEU A 102 ? 0.2515 0.3764 0.3129 0.0273 -0.0096 -0.0065 101 LEU A CD1 794 C CD2 . LEU A 102 ? 0.2626 0.3996 0.3226 0.0300 -0.0084 0.0010 101 LEU A CD2 795 N N . LYS A 103 ? 0.2508 0.4070 0.3290 0.0294 -0.0192 -0.0341 102 LYS A N 796 C CA . LYS A 103 ? 0.2520 0.4268 0.3323 0.0293 -0.0187 -0.0412 102 LYS A CA 797 C C . LYS A 103 ? 0.2558 0.4209 0.3381 0.0274 -0.0231 -0.0490 102 LYS A C 798 O O . LYS A 103 ? 0.2452 0.4213 0.3272 0.0252 -0.0226 -0.0524 102 LYS A O 799 C CB . LYS A 103 ? 0.2563 0.4494 0.3415 0.0305 -0.0169 -0.0493 102 LYS A CB 800 C CG . LYS A 103 ? 0.2658 0.4702 0.3443 0.0286 -0.0113 -0.0402 102 LYS A CG 801 C CD . LYS A 103 ? 0.2740 0.4987 0.3557 0.0265 -0.0069 -0.0487 102 LYS A CD 802 C CE . LYS A 103 ? 0.2913 0.5367 0.3637 0.0233 -0.0040 -0.0512 102 LYS A CE 803 N NZ . LYS A 103 ? 0.3076 0.5754 0.3824 0.0194 0.0021 -0.0627 102 LYS A NZ 804 N N . HIS A 104 ? 0.2542 0.3969 0.3372 0.0275 -0.0283 -0.0514 103 HIS A N 805 C CA . HIS A 104 ? 0.2765 0.4023 0.3574 0.0238 -0.0333 -0.0567 103 HIS A CA 806 C C . HIS A 104 ? 0.2919 0.4121 0.3649 0.0163 -0.0295 -0.0499 103 HIS A C 807 O O . HIS A 104 ? 0.2888 0.4119 0.3620 0.0111 -0.0294 -0.0549 103 HIS A O 808 C CB . HIS A 104 ? 0.2872 0.3860 0.3671 0.0256 -0.0420 -0.0584 103 HIS A CB 809 C CG . HIS A 104 ? 0.3018 0.3755 0.3749 0.0202 -0.0486 -0.0616 103 HIS A CG 810 N ND1 . HIS A 104 ? 0.3144 0.3854 0.3943 0.0225 -0.0545 -0.0739 103 HIS A ND1 811 C CD2 . HIS A 104 ? 0.3183 0.3664 0.3767 0.0113 -0.0499 -0.0544 103 HIS A CD2 812 C CE1 . HIS A 104 ? 0.3353 0.3775 0.4045 0.0151 -0.0603 -0.0730 103 HIS A CE1 813 N NE2 . HIS A 104 ? 0.3420 0.3705 0.3970 0.0073 -0.0570 -0.0608 103 HIS A NE2 814 N N . LEU A 105 ? 0.3034 0.4173 0.3708 0.0154 -0.0258 -0.0402 104 LEU A N 815 C CA . LEU A 105 ? 0.3293 0.4420 0.3922 0.0089 -0.0204 -0.0358 104 LEU A CA 816 C C . LEU A 105 ? 0.3241 0.4648 0.3953 0.0106 -0.0167 -0.0376 104 LEU A C 817 O O . LEU A 105 ? 0.3210 0.4685 0.3948 0.0047 -0.0147 -0.0413 104 LEU A O 818 C CB . LEU A 105 ? 0.3546 0.4577 0.4115 0.0095 -0.0169 -0.0272 104 LEU A CB 819 C CG . LEU A 105 ? 0.3866 0.4944 0.4425 0.0047 -0.0094 -0.0249 104 LEU A CG 820 C CD1 . LEU A 105 ? 0.4014 0.4973 0.4501 -0.0073 -0.0076 -0.0286 104 LEU A CD1 821 C CD2 . LEU A 105 ? 0.4074 0.5048 0.4576 0.0066 -0.0064 -0.0183 104 LEU A CD2 822 N N . LEU A 106 ? 0.3146 0.4716 0.3893 0.0178 -0.0165 -0.0350 105 LEU A N 823 C CA . LEU A 106 ? 0.3103 0.4920 0.3899 0.0204 -0.0160 -0.0354 105 LEU A CA 824 C C . LEU A 106 ? 0.3045 0.4983 0.3879 0.0168 -0.0188 -0.0457 105 LEU A C 825 O O . LEU A 106 ? 0.2974 0.5097 0.3859 0.0162 -0.0193 -0.0475 105 LEU A O 826 C CB . LEU A 106 ? 0.3189 0.5100 0.3955 0.0262 -0.0163 -0.0302 105 LEU A CB 827 C CG . LEU A 106 ? 0.3405 0.5522 0.4167 0.0295 -0.0178 -0.0266 105 LEU A CG 828 C CD1 . LEU A 106 ? 0.3410 0.5546 0.4227 0.0320 -0.0176 -0.0220 105 LEU A CD1 829 C CD2 . LEU A 106 ? 0.3439 0.5574 0.4116 0.0319 -0.0171 -0.0195 105 LEU A CD2 830 N N . SER A 107 ? 0.3036 0.4868 0.3861 0.0148 -0.0217 -0.0535 106 SER A N 831 C CA . SER A 107 ? 0.3133 0.5029 0.3988 0.0106 -0.0247 -0.0650 106 SER A CA 832 C C . SER A 107 ? 0.3169 0.4959 0.4027 0.0010 -0.0243 -0.0676 106 SER A C 833 O O . SER A 107 ? 0.3091 0.4930 0.3977 -0.0044 -0.0265 -0.0770 106 SER A O 834 C CB . SER A 107 ? 0.3339 0.5129 0.4201 0.0131 -0.0287 -0.0742 106 SER A CB 835 O OG . SER A 107 ? 0.3427 0.4911 0.4258 0.0103 -0.0324 -0.0741 106 SER A OG 836 N N . ARG A 108 ? 0.3404 0.5045 0.4221 -0.0025 -0.0207 -0.0601 107 ARG A N 837 C CA . ARG A 108 ? 0.3685 0.5238 0.4483 -0.0145 -0.0175 -0.0617 107 ARG A CA 838 C C . ARG A 108 ? 0.3357 0.5151 0.4248 -0.0154 -0.0115 -0.0601 107 ARG A C 839 O O . ARG A 108 ? 0.3238 0.5023 0.4139 -0.0263 -0.0064 -0.0628 107 ARG A O 840 C CB . ARG A 108 ? 0.4141 0.5362 0.4803 -0.0197 -0.0171 -0.0555 107 ARG A CB 841 C CG . ARG A 108 ? 0.4659 0.5629 0.5253 -0.0158 -0.0255 -0.0564 107 ARG A CG 842 C CD . ARG A 108 ? 0.5396 0.6170 0.5941 -0.0245 -0.0311 -0.0637 107 ARG A CD 843 N NE . ARG A 108 ? 0.6063 0.6777 0.6657 -0.0155 -0.0398 -0.0713 107 ARG A NE 844 C CZ . ARG A 108 ? 0.6934 0.7357 0.7473 -0.0183 -0.0487 -0.0765 107 ARG A CZ 845 N NH1 . ARG A 108 ? 0.7174 0.7296 0.7561 -0.0319 -0.0506 -0.0729 107 ARG A NH1 846 N NH2 . ARG A 108 ? 0.7094 0.7517 0.7725 -0.0076 -0.0560 -0.0861 107 ARG A NH2 847 N N . ILE A 109 ? 0.3065 0.5067 0.4024 -0.0044 -0.0124 -0.0563 108 ILE A N 848 C CA . ILE A 109 ? 0.2879 0.5095 0.3949 -0.0007 -0.0094 -0.0546 108 ILE A CA 849 C C . ILE A 109 ? 0.2699 0.5211 0.3869 0.0045 -0.0152 -0.0585 108 ILE A C 850 O O . ILE A 109 ? 0.2745 0.5295 0.3858 0.0096 -0.0203 -0.0575 108 ILE A O 851 C CB . ILE A 109 ? 0.2849 0.4993 0.3885 0.0088 -0.0080 -0.0444 108 ILE A CB 852 C CG1 . ILE A 109 ? 0.2874 0.4746 0.3806 0.0029 -0.0029 -0.0411 108 ILE A CG1 853 C CG2 . ILE A 109 ? 0.2742 0.5097 0.3911 0.0162 -0.0077 -0.0432 108 ILE A CG2 854 C CD1 . ILE A 109 ? 0.2850 0.4598 0.3720 0.0108 -0.0028 -0.0320 108 ILE A CD1 855 N N . ASN A 110 ? 0.2705 0.5440 0.4024 0.0026 -0.0144 -0.0640 109 ASN A N 856 C CA . ASN A 110 ? 0.2534 0.5565 0.3958 0.0081 -0.0221 -0.0677 109 ASN A CA 857 C C . ASN A 110 ? 0.2463 0.5649 0.3996 0.0208 -0.0258 -0.0621 109 ASN A C 858 O O . ASN A 110 ? 0.2468 0.5847 0.4039 0.0283 -0.0354 -0.0614 109 ASN A O 859 C CB . ASN A 110 ? 0.2612 0.5824 0.4164 -0.0030 -0.0215 -0.0806 109 ASN A CB 860 C CG . ASN A 110 ? 0.2797 0.5855 0.4242 -0.0144 -0.0214 -0.0871 109 ASN A CG 861 O OD1 . ASN A 110 ? 0.3084 0.5991 0.4509 -0.0274 -0.0153 -0.0914 109 ASN A OD1 862 N ND2 . ASN A 110 ? 0.2753 0.5837 0.4117 -0.0101 -0.0282 -0.0883 109 ASN A ND2 863 N N . HIS A 111 ? 0.2428 0.5519 0.4003 0.0233 -0.0193 -0.0587 110 HIS A N 864 C CA . HIS A 111 ? 0.2457 0.5661 0.4150 0.0369 -0.0237 -0.0546 110 HIS A CA 865 C C . HIS A 111 ? 0.2466 0.5461 0.4121 0.0411 -0.0171 -0.0483 110 HIS A C 866 O O . HIS A 111 ? 0.2377 0.5241 0.4001 0.0316 -0.0066 -0.0517 110 HIS A O 867 C CB . HIS A 111 ? 0.2462 0.5992 0.4423 0.0377 -0.0254 -0.0665 110 HIS A CB 868 C CG . HIS A 111 ? 0.2593 0.6273 0.4700 0.0550 -0.0357 -0.0635 110 HIS A CG 869 N ND1 . HIS A 111 ? 0.2693 0.6637 0.5094 0.0601 -0.0359 -0.0744 110 HIS A ND1 870 C CD2 . HIS A 111 ? 0.2750 0.6340 0.4749 0.0681 -0.0471 -0.0509 110 HIS A CD2 871 C CE1 . HIS A 111 ? 0.2778 0.6772 0.5258 0.0780 -0.0487 -0.0687 110 HIS A CE1 872 N NE2 . HIS A 111 ? 0.2805 0.6564 0.5020 0.0823 -0.0558 -0.0533 110 HIS A NE2 873 N N . PHE A 112 ? 0.2653 0.5596 0.4283 0.0545 -0.0240 -0.0387 111 PHE A N 874 C CA . PHE A 112 ? 0.2815 0.5586 0.4441 0.0611 -0.0201 -0.0336 111 PHE A CA 875 C C . PHE A 112 ? 0.2872 0.5812 0.4716 0.0749 -0.0264 -0.0369 111 PHE A C 876 O O . PHE A 112 ? 0.3051 0.6193 0.4989 0.0818 -0.0377 -0.0379 111 PHE A O 877 C CB . PHE A 112 ? 0.2913 0.5448 0.4333 0.0658 -0.0244 -0.0193 111 PHE A CB 878 C CG . PHE A 112 ? 0.2968 0.5301 0.4207 0.0555 -0.0178 -0.0164 111 PHE A CG 879 C CD1 . PHE A 112 ? 0.2924 0.5120 0.4144 0.0475 -0.0081 -0.0206 111 PHE A CD1 880 C CD2 . PHE A 112 ? 0.2978 0.5259 0.4063 0.0541 -0.0219 -0.0098 111 PHE A CD2 881 C CE1 . PHE A 112 ? 0.2894 0.4896 0.3960 0.0400 -0.0051 -0.0178 111 PHE A CE1 882 C CE2 . PHE A 112 ? 0.2926 0.5048 0.3892 0.0466 -0.0171 -0.0091 111 PHE A CE2 883 C CZ . PHE A 112 ? 0.2933 0.4910 0.3897 0.0405 -0.0100 -0.0127 111 PHE A CZ 884 N N . GLU A 113 ? 0.2926 0.5774 0.4846 0.0798 -0.0205 -0.0390 112 GLU A N 885 C CA . GLU A 113 ? 0.3081 0.5998 0.5184 0.0968 -0.0286 -0.0401 112 GLU A CA 886 C C . GLU A 113 ? 0.3127 0.5721 0.5089 0.1017 -0.0267 -0.0306 112 GLU A C 887 O O . GLU A 113 ? 0.3154 0.5632 0.5094 0.0953 -0.0143 -0.0355 112 GLU A O 888 C CB . GLU A 113 ? 0.3177 0.6375 0.5598 0.0982 -0.0218 -0.0586 112 GLU A CB 889 C CG . GLU A 113 ? 0.3394 0.6672 0.6060 0.1183 -0.0304 -0.0631 112 GLU A CG 890 C CD . GLU A 113 ? 0.3526 0.7116 0.6535 0.1187 -0.0206 -0.0849 112 GLU A CD 891 O OE1 . GLU A 113 ? 0.3598 0.7393 0.6661 0.1023 -0.0093 -0.0957 112 GLU A OE1 892 O OE2 . GLU A 113 ? 0.3516 0.7148 0.6747 0.1348 -0.0240 -0.0923 112 GLU A OE2 893 N N . LYS A 114 ? 0.3228 0.5662 0.5068 0.1114 -0.0392 -0.0167 113 LYS A N 894 C CA . LYS A 114 ? 0.3256 0.5363 0.4942 0.1143 -0.0384 -0.0066 113 LYS A CA 895 C C . LYS A 114 ? 0.3296 0.5376 0.5186 0.1278 -0.0392 -0.0141 113 LYS A C 896 O O . LYS A 114 ? 0.3442 0.5690 0.5545 0.1416 -0.0498 -0.0190 113 LYS A O 897 C CB . LYS A 114 ? 0.3413 0.5350 0.4883 0.1178 -0.0510 0.0109 113 LYS A CB 898 C CG . LYS A 114 ? 0.3505 0.5097 0.4782 0.1158 -0.0485 0.0218 113 LYS A CG 899 C CD . LYS A 114 ? 0.3691 0.5135 0.4704 0.1119 -0.0564 0.0385 113 LYS A CD 900 C CE . LYS A 114 ? 0.3985 0.5321 0.4970 0.1253 -0.0735 0.0490 113 LYS A CE 901 N NZ . LYS A 114 ? 0.4199 0.5442 0.4895 0.1187 -0.0813 0.0649 113 LYS A NZ 902 N N . ILE A 115 ? 0.3262 0.5137 0.5096 0.1242 -0.0287 -0.0163 114 ILE A N 903 C CA . ILE A 115 ? 0.3417 0.5221 0.5423 0.1368 -0.0285 -0.0244 114 ILE A CA 904 C C . ILE A 115 ? 0.3528 0.4946 0.5332 0.1371 -0.0289 -0.0136 114 ILE A C 905 O O . ILE A 115 ? 0.3339 0.4590 0.4904 0.1240 -0.0235 -0.0046 114 ILE A O 906 C CB . ILE A 115 ? 0.3361 0.5344 0.5547 0.1311 -0.0121 -0.0445 114 ILE A CB 907 C CG1 . ILE A 115 ? 0.3273 0.5147 0.5231 0.1108 0.0024 -0.0436 114 ILE A CG1 908 C CG2 . ILE A 115 ? 0.3327 0.5718 0.5798 0.1338 -0.0124 -0.0587 114 ILE A CG2 909 C CD1 . ILE A 115 ? 0.3279 0.5182 0.5301 0.1041 0.0183 -0.0595 114 ILE A CD1 910 N N . GLN A 116 ? 0.3786 0.5071 0.5711 0.1526 -0.0360 -0.0159 115 GLN A N 911 C CA . GLN A 116 ? 0.4014 0.4930 0.5790 0.1531 -0.0353 -0.0095 115 GLN A CA 912 C C . GLN A 116 ? 0.3993 0.4913 0.5818 0.1457 -0.0180 -0.0252 115 GLN A C 913 O O . GLN A 116 ? 0.4032 0.5157 0.6109 0.1524 -0.0121 -0.0435 115 GLN A O 914 C CB . GLN A 116 ? 0.4277 0.5019 0.6167 0.1734 -0.0510 -0.0069 115 GLN A CB 915 C CG . GLN A 116 ? 0.4536 0.4899 0.6330 0.1753 -0.0493 -0.0053 115 GLN A CG 916 C CD . GLN A 116 ? 0.4871 0.5018 0.6776 0.1963 -0.0669 -0.0025 115 GLN A CD 917 O OE1 . GLN A 116 ? 0.5106 0.5066 0.6853 0.2002 -0.0832 0.0159 115 GLN A OE1 918 N NE2 . GLN A 116 ? 0.4960 0.5118 0.7126 0.2099 -0.0643 -0.0212 115 GLN A NE2 919 N N . ILE A 117 ? 0.3926 0.4636 0.5509 0.1312 -0.0100 -0.0191 116 ILE A N 920 C CA . ILE A 117 ? 0.3904 0.4571 0.5470 0.1229 0.0047 -0.0322 116 ILE A CA 921 C C . ILE A 117 ? 0.4162 0.4482 0.5630 0.1255 0.0039 -0.0303 116 ILE A C 922 O O . ILE A 117 ? 0.4282 0.4568 0.5788 0.1238 0.0140 -0.0445 116 ILE A O 923 C CB . ILE A 117 ? 0.3697 0.4416 0.5075 0.1031 0.0147 -0.0304 116 ILE A CB 924 C CG1 . ILE A 117 ? 0.3641 0.4151 0.4776 0.0946 0.0094 -0.0130 116 ILE A CG1 925 C CG2 . ILE A 117 ? 0.3484 0.4526 0.4967 0.0994 0.0166 -0.0349 116 ILE A CG2 926 C CD1 . ILE A 117 ? 0.3501 0.4016 0.4469 0.0778 0.0172 -0.0130 116 ILE A CD1 927 N N . ILE A 118 ? 0.4369 0.4431 0.5697 0.1280 -0.0074 -0.0135 117 ILE A N 928 C CA . ILE A 118 ? 0.4667 0.4371 0.5909 0.1307 -0.0099 -0.0112 117 ILE A CA 929 C C . ILE A 118 ? 0.4891 0.4375 0.6118 0.1431 -0.0269 0.0030 117 ILE A C 930 O O . ILE A 118 ? 0.4867 0.4216 0.5885 0.1349 -0.0330 0.0209 117 ILE A O 931 C CB . ILE A 118 ? 0.4697 0.4211 0.5681 0.1125 -0.0039 -0.0035 117 ILE A CB 932 C CG1 . ILE A 118 ? 0.4495 0.4177 0.5443 0.0995 0.0098 -0.0149 117 ILE A CG1 933 C CG2 . ILE A 118 ? 0.5006 0.4155 0.5918 0.1142 -0.0062 -0.0031 117 ILE A CG2 934 C CD1 . ILE A 118 ? 0.4511 0.4051 0.5230 0.0829 0.0127 -0.0074 117 ILE A CD1 935 N N . PRO A 119 ? 0.5127 0.4567 0.6568 0.1626 -0.0350 -0.0054 118 PRO A N 936 C CA . PRO A 119 ? 0.5443 0.4634 0.6858 0.1762 -0.0544 0.0087 118 PRO A CA 937 C C . PRO A 119 ? 0.5754 0.4499 0.6887 0.1669 -0.0586 0.0248 118 PRO A C 938 O O . PRO A 119 ? 0.5729 0.4317 0.6786 0.1573 -0.0482 0.0188 118 PRO A O 939 C CB . PRO A 119 ? 0.5619 0.4809 0.7345 0.1991 -0.0604 -0.0085 118 PRO A CB 940 C CG . PRO A 119 ? 0.5397 0.4893 0.7323 0.1962 -0.0419 -0.0330 118 PRO A CG 941 C CD . PRO A 119 ? 0.5122 0.4728 0.6832 0.1723 -0.0262 -0.0297 118 PRO A CD 942 N N . LYS A 120 ? 0.6072 0.4614 0.7039 0.1685 -0.0739 0.0450 119 LYS A N 943 C CA . LYS A 120 ? 0.6405 0.4522 0.7083 0.1570 -0.0780 0.0620 119 LYS A CA 944 C C . LYS A 120 ? 0.6721 0.4448 0.7457 0.1679 -0.0833 0.0556 119 LYS A C 945 O O . LYS A 120 ? 0.6858 0.4269 0.7414 0.1555 -0.0796 0.0605 119 LYS A O 946 C CB . LYS A 120 ? 0.6727 0.4718 0.7189 0.1554 -0.0934 0.0850 119 LYS A CB 947 C CG . LYS A 120 ? 0.6825 0.4684 0.6959 0.1309 -0.0877 0.1018 119 LYS A CG 948 C CD . LYS A 120 ? 0.7120 0.4924 0.7023 0.1273 -0.1006 0.1227 119 LYS A CD 949 C CE . LYS A 120 ? 0.7470 0.4960 0.7029 0.1055 -0.0990 0.1406 119 LYS A CE 950 N NZ . LYS A 120 ? 0.7808 0.5183 0.7083 0.1000 -0.1117 0.1620 119 LYS A NZ 951 N N . SER A 121 ? 0.6851 0.4623 0.7866 0.1914 -0.0919 0.0426 120 SER A N 952 C CA . SER A 121 ? 0.7196 0.4611 0.8322 0.2065 -0.0990 0.0333 120 SER A CA 953 C C . SER A 121 ? 0.7002 0.4468 0.8250 0.2026 -0.0809 0.0101 120 SER A C 954 O O . SER A 121 ? 0.7232 0.4403 0.8566 0.2132 -0.0842 -0.0003 120 SER A O 955 C CB . SER A 121 ? 0.7393 0.4899 0.8827 0.2352 -0.1153 0.0246 120 SER A CB 956 O OG . SER A 121 ? 0.7042 0.5090 0.8773 0.2405 -0.1041 0.0046 120 SER A OG 957 N N . SER A 122 ? 0.6561 0.4382 0.7802 0.1873 -0.0625 0.0018 121 SER A N 958 C CA . SER A 122 ? 0.6405 0.4318 0.7739 0.1827 -0.0453 -0.0207 121 SER A CA 959 C C . SER A 122 ? 0.6474 0.4092 0.7540 0.1629 -0.0383 -0.0152 121 SER A C 960 O O . SER A 122 ? 0.6482 0.4108 0.7563 0.1570 -0.0257 -0.0322 121 SER A O 961 C CB . SER A 122 ? 0.5976 0.4391 0.7415 0.1755 -0.0305 -0.0324 121 SER A CB 962 O OG . SER A 122 ? 0.5659 0.4151 0.6854 0.1536 -0.0232 -0.0197 121 SER A OG 963 N N . TRP A 123 ? 0.6571 0.3945 0.7387 0.1513 -0.0463 0.0077 122 TRP A N 964 C CA . TRP A 123 ? 0.6594 0.3713 0.7172 0.1312 -0.0409 0.0138 122 TRP A CA 965 C C . TRP A 123 ? 0.7117 0.3725 0.7642 0.1367 -0.0503 0.0149 122 TRP A C 966 O O . TRP A 123 ? 0.7462 0.3754 0.7819 0.1341 -0.0627 0.0346 122 TRP A O 967 C CB . TRP A 123 ? 0.6421 0.3585 0.6774 0.1136 -0.0427 0.0360 122 TRP A CB 968 C CG . TRP A 123 ? 0.5899 0.3524 0.6292 0.1075 -0.0343 0.0347 122 TRP A CG 969 C CD1 . TRP A 123 ? 0.5742 0.3605 0.6170 0.1127 -0.0398 0.0436 122 TRP A CD1 970 C CD2 . TRP A 123 ? 0.5472 0.3343 0.5860 0.0950 -0.0205 0.0241 122 TRP A CD2 971 N NE1 . TRP A 123 ? 0.5293 0.3527 0.5751 0.1042 -0.0295 0.0384 122 TRP A NE1 972 C CE2 . TRP A 123 ? 0.5175 0.3408 0.5603 0.0936 -0.0183 0.0272 122 TRP A CE2 973 C CE3 . TRP A 123 ? 0.5459 0.3262 0.5797 0.0847 -0.0112 0.0123 122 TRP A CE3 974 C CZ2 . TRP A 123 ? 0.4867 0.3364 0.5284 0.0827 -0.0077 0.0199 122 TRP A CZ2 975 C CZ3 . TRP A 123 ? 0.5183 0.3262 0.5498 0.0738 -0.0013 0.0058 122 TRP A CZ3 976 C CH2 . TRP A 123 ? 0.4855 0.3261 0.5209 0.0732 0.0000 0.0100 122 TRP A CH2 977 N N . SER A 124 ? 0.7286 0.3796 0.7930 0.1430 -0.0440 -0.0063 123 SER A N 978 C CA . SER A 124 ? 0.7866 0.3880 0.8512 0.1525 -0.0536 -0.0099 123 SER A CA 979 C C . SER A 124 ? 0.8115 0.3733 0.8491 0.1315 -0.0532 -0.0001 123 SER A C 980 O O . SER A 124 ? 0.8618 0.3757 0.8923 0.1358 -0.0649 0.0057 123 SER A O 981 C CB . SER A 124 ? 0.7941 0.4021 0.8838 0.1677 -0.0461 -0.0402 123 SER A CB 982 O OG . SER A 124 ? 0.7751 0.4299 0.8901 0.1809 -0.0410 -0.0528 123 SER A OG 983 N N . ASP A 125 ? 0.7869 0.3678 0.8105 0.1089 -0.0408 0.0008 124 ASP A N 984 C CA . ASP A 125 ? 0.8046 0.3550 0.8062 0.0873 -0.0391 0.0071 124 ASP A CA 985 C C . ASP A 125 ? 0.7772 0.3389 0.7595 0.0664 -0.0387 0.0287 124 ASP A C 986 O O . ASP A 125 ? 0.7666 0.3221 0.7350 0.0453 -0.0334 0.0309 124 ASP A O 987 C CB . ASP A 125 ? 0.8000 0.3610 0.8029 0.0782 -0.0258 -0.0143 124 ASP A CB 988 C CG . ASP A 125 ? 0.8197 0.3742 0.8415 0.0972 -0.0232 -0.0392 124 ASP A CG 989 O OD1 . ASP A 125 ? 0.8633 0.3767 0.8889 0.1088 -0.0328 -0.0417 124 ASP A OD1 990 O OD2 . ASP A 125 ? 0.7966 0.3865 0.8293 0.1002 -0.0117 -0.0567 124 ASP A OD2 991 N N . HIS A 126 ? 0.7611 0.3419 0.7442 0.0721 -0.0440 0.0430 125 HIS A N 992 C CA . HIS A 126 ? 0.7467 0.3409 0.7128 0.0535 -0.0430 0.0619 125 HIS A CA 993 C C . HIS A 126 ? 0.7751 0.3591 0.7336 0.0614 -0.0557 0.0813 125 HIS A C 994 O O . HIS A 126 ? 0.7832 0.3688 0.7560 0.0837 -0.0641 0.0782 125 HIS A O 995 C CB . HIS A 126 ? 0.6851 0.3312 0.6591 0.0480 -0.0319 0.0554 125 HIS A CB 996 C CG . HIS A 126 ? 0.6640 0.3205 0.6402 0.0376 -0.0213 0.0394 125 HIS A CG 997 N ND1 . HIS A 126 ? 0.6565 0.3189 0.6455 0.0485 -0.0161 0.0193 125 HIS A ND1 998 C CD2 . HIS A 126 ? 0.6515 0.3151 0.6182 0.0171 -0.0156 0.0399 125 HIS A CD2 999 C CE1 . HIS A 126 ? 0.6407 0.3099 0.6241 0.0345 -0.0084 0.0096 125 HIS A CE1 1000 N NE2 . HIS A 126 ? 0.6376 0.3082 0.6091 0.0163 -0.0089 0.0218 125 HIS A NE2 1001 N N . GLU A 127 ? 0.7979 0.3728 0.7336 0.0422 -0.0571 0.1004 126 GLU A N 1002 C CA . GLU A 127 ? 0.8204 0.3887 0.7420 0.0447 -0.0681 0.1208 126 GLU A CA 1003 C C . GLU A 127 ? 0.7761 0.3966 0.7060 0.0470 -0.0630 0.1206 126 GLU A C 1004 O O . GLU A 127 ? 0.7475 0.3988 0.6760 0.0308 -0.0513 0.1184 126 GLU A O 1005 C CB . GLU A 127 ? 0.8560 0.3950 0.7468 0.0196 -0.0693 0.1404 126 GLU A CB 1006 C CG . GLU A 127 ? 0.9239 0.4000 0.7977 0.0225 -0.0838 0.1518 126 GLU A CG 1007 C CD . GLU A 127 ? 0.9520 0.4108 0.8189 0.0408 -0.1020 0.1663 126 GLU A CD 1008 O OE1 . GLU A 127 ? 0.9104 0.4093 0.7862 0.0503 -0.1023 0.1668 126 GLU A OE1 1009 O OE2 . GLU A 127 ? 1.0107 0.4143 0.8627 0.0456 -0.1172 0.1773 126 GLU A OE2 1010 N N . ALA A 128 ? 0.7764 0.4062 0.7166 0.0677 -0.0729 0.1219 127 ALA A N 1011 C CA . ALA A 128 ? 0.7457 0.4228 0.6952 0.0718 -0.0697 0.1205 127 ALA A CA 1012 C C . ALA A 128 ? 0.7758 0.4502 0.7049 0.0689 -0.0803 0.1410 127 ALA A C 1013 O O . ALA A 128 ? 0.7666 0.4774 0.6939 0.0621 -0.0748 0.1430 127 ALA A O 1014 C CB . ALA A 128 ? 0.7255 0.4246 0.7050 0.0957 -0.0712 0.1030 127 ALA A CB 1015 N N . SER A 129 ? 0.8281 0.4577 0.7399 0.0734 -0.0959 0.1561 128 SER A N 1016 C CA . SER A 129 ? 0.8647 0.4848 0.7516 0.0709 -0.1088 0.1773 128 SER A CA 1017 C C . SER A 129 ? 0.8916 0.4868 0.7408 0.0421 -0.1055 0.1966 128 SER A C 1018 O O . SER A 129 ? 0.9369 0.5051 0.7571 0.0378 -0.1186 0.2170 128 SER A O 1019 C CB . SER A 129 ? 0.9153 0.5001 0.8044 0.0952 -0.1318 0.1837 128 SER A CB 1020 O OG . SER A 129 ? 0.8909 0.5108 0.8110 0.1194 -0.1367 0.1701 128 SER A OG 1021 N N . ALA A 130 ? 0.8621 0.4666 0.7109 0.0216 -0.0886 0.1898 129 ALA A N 1022 C CA . ALA A 130 ? 0.8736 0.4682 0.6917 -0.0084 -0.0814 0.2042 129 ALA A CA 1023 C C . ALA A 130 ? 0.8201 0.4692 0.6448 -0.0233 -0.0643 0.1962 129 ALA A C 1024 O O . ALA A 130 ? 0.8414 0.4937 0.6460 -0.0486 -0.0556 0.2041 129 ALA A O 1025 C CB . ALA A 130 ? 0.8986 0.4555 0.7100 -0.0226 -0.0774 0.2034 129 ALA A CB 1026 N N . GLY A 131 ? 0.7592 0.4507 0.6124 -0.0083 -0.0596 0.1799 130 GLY A N 1027 C CA . GLY A 131 ? 0.7051 0.4455 0.5674 -0.0194 -0.0453 0.1706 130 GLY A CA 1028 C C . GLY A 131 ? 0.6981 0.4598 0.5435 -0.0257 -0.0464 0.1809 130 GLY A C 1029 O O . GLY A 131 ? 0.6688 0.4645 0.5284 -0.0139 -0.0465 0.1734 130 GLY A O 1030 N N . VAL A 132 ? 0.7349 0.4763 0.5484 -0.0462 -0.0465 0.1973 131 VAL A N 1031 C CA . VAL A 132 ? 0.7460 0.5018 0.5358 -0.0549 -0.0481 0.2088 131 VAL A CA 1032 C C . VAL A 132 ? 0.7545 0.5240 0.5262 -0.0858 -0.0328 0.2115 131 VAL A C 1033 O O . VAL A 132 ? 0.7628 0.5186 0.5339 -0.1017 -0.0248 0.2099 131 VAL A O 1034 C CB . VAL A 132 ? 0.8047 0.5173 0.5652 -0.0483 -0.0675 0.2300 131 VAL A CB 1035 C CG1 . VAL A 132 ? 0.7884 0.5019 0.5715 -0.0163 -0.0826 0.2245 131 VAL A CG1 1036 C CG2 . VAL A 132 ? 0.8618 0.5184 0.6008 -0.0598 -0.0724 0.2432 131 VAL A CG2 1037 N N . SER A 133 ? 0.7538 0.5521 0.5116 -0.0947 -0.0286 0.2141 132 SER A N 1038 C CA . SER A 133 ? 0.7569 0.5818 0.5045 -0.1226 -0.0113 0.2108 132 SER A CA 1039 C C . SER A 133 ? 0.7897 0.6209 0.5022 -0.1354 -0.0122 0.2236 132 SER A C 1040 O O . SER A 133 ? 0.7910 0.6294 0.5004 -0.1191 -0.0231 0.2264 132 SER A O 1041 C CB . SER A 133 ? 0.7001 0.5774 0.4858 -0.1176 0.0014 0.1867 132 SER A CB 1042 O OG . SER A 133 ? 0.7080 0.6140 0.4921 -0.1425 0.0183 0.1793 132 SER A OG 1043 N N . SER A 134 ? 0.8233 0.6536 0.5088 -0.1661 -0.0003 0.2304 133 SER A N 1044 C CA . SER A 134 ? 0.8557 0.6963 0.5044 -0.1831 0.0022 0.2405 133 SER A CA 1045 C C . SER A 134 ? 0.8112 0.7120 0.4818 -0.1787 0.0130 0.2204 133 SER A C 1046 O O . SER A 134 ? 0.8252 0.7395 0.4711 -0.1845 0.0123 0.2253 133 SER A O 1047 C CB . SER A 134 ? 0.9003 0.7277 0.5150 -0.2206 0.0154 0.2506 133 SER A CB 1048 O OG . SER A 134 ? 0.8631 0.7343 0.5058 -0.2358 0.0369 0.2295 133 SER A OG 1049 N N . ALA A 135 ? 0.7645 0.6991 0.4798 -0.1686 0.0221 0.1979 134 ALA A N 1050 C CA . ALA A 135 ? 0.7264 0.7135 0.4670 -0.1607 0.0301 0.1775 134 ALA A CA 1051 C C . ALA A 135 ? 0.7193 0.7086 0.4663 -0.1340 0.0151 0.1779 134 ALA A C 1052 O O . ALA A 135 ? 0.7065 0.7325 0.4614 -0.1302 0.0191 0.1660 134 ALA A O 1053 C CB . ALA A 135 ? 0.6748 0.6901 0.4596 -0.1558 0.0402 0.1553 134 ALA A CB 1054 N N . CYS A 136 ? 0.7355 0.6872 0.4812 -0.1159 -0.0017 0.1899 135 CYS A N 1055 C CA . CYS A 136 ? 0.7274 0.6811 0.4811 -0.0910 -0.0169 0.1903 135 CYS A CA 1056 C C . CYS A 136 ? 0.7826 0.6979 0.4997 -0.0885 -0.0352 0.2136 135 CYS A C 1057 O O . CYS A 136 ? 0.7835 0.6677 0.5068 -0.0701 -0.0507 0.2209 135 CYS A O 1058 C CB . CYS A 136 ? 0.6887 0.6394 0.4806 -0.0677 -0.0217 0.1793 135 CYS A CB 1059 S SG . CYS A 136 ? 0.6374 0.6281 0.4692 -0.0686 -0.0047 0.1539 135 CYS A SG 1060 N N . PRO A 137 ? 0.8331 0.7505 0.5115 -0.1069 -0.0343 0.2245 136 PRO A N 1061 C CA . PRO A 137 ? 0.9017 0.7790 0.5400 -0.1061 -0.0540 0.2487 136 PRO A CA 1062 C C . PRO A 137 ? 0.9091 0.7925 0.5578 -0.0791 -0.0734 0.2484 136 PRO A C 1063 O O . PRO A 137 ? 0.8632 0.7874 0.5431 -0.0665 -0.0689 0.2296 136 PRO A O 1064 C CB . PRO A 137 ? 0.9372 0.8232 0.5313 -0.1360 -0.0443 0.2571 136 PRO A CB 1065 C CG . PRO A 137 ? 0.8856 0.8298 0.5055 -0.1409 -0.0245 0.2322 136 PRO A CG 1066 C CD . PRO A 137 ? 0.8275 0.7850 0.4970 -0.1285 -0.0159 0.2140 136 PRO A CD 1067 N N . TYR A 138 ? 0.9755 0.8170 0.5983 -0.0710 -0.0959 0.2691 137 TYR A N 1068 C CA . TYR A 138 ? 0.9873 0.8312 0.6174 -0.0460 -0.1178 0.2709 137 TYR A CA 1069 C C . TYR A 138 ? 1.0584 0.8504 0.6457 -0.0457 -0.1423 0.2983 137 TYR A C 1070 O O . TYR A 138 ? 1.0756 0.8219 0.6597 -0.0407 -0.1516 0.3095 137 TYR A O 1071 C CB . TYR A 138 ? 0.9501 0.8011 0.6321 -0.0173 -0.1223 0.2555 137 TYR A CB 1072 C CG . TYR A 138 ? 0.9668 0.8180 0.6597 0.0088 -0.1462 0.2572 137 TYR A CG 1073 C CD1 . TYR A 138 ? 0.9455 0.8384 0.6473 0.0146 -0.1480 0.2467 137 TYR A CD1 1074 C CD2 . TYR A 138 ? 1.0098 0.8201 0.7054 0.0278 -0.1676 0.2681 137 TYR A CD2 1075 C CE1 . TYR A 138 ? 0.9583 0.8548 0.6725 0.0378 -0.1704 0.2471 137 TYR A CE1 1076 C CE2 . TYR A 138 ? 1.0223 0.8365 0.7321 0.0528 -0.1906 0.2679 137 TYR A CE2 1077 C CZ . TYR A 138 ? 0.9911 0.8497 0.7106 0.0573 -0.1918 0.2574 137 TYR A CZ 1078 O OH . TYR A 138 ? 0.9964 0.8617 0.7325 0.0815 -0.2151 0.2559 137 TYR A OH 1079 N N . GLN A 139 ? 1.1073 0.9049 0.6604 -0.0510 -0.1537 0.3086 138 GLN A N 1080 C CA . GLN A 139 ? 1.1900 0.9376 0.6939 -0.0531 -0.1793 0.3368 138 GLN A CA 1081 C C . GLN A 139 ? 1.2465 0.9456 0.7077 -0.0802 -0.1736 0.3570 138 GLN A C 1082 O O . GLN A 139 ? 1.3030 0.9449 0.7399 -0.0751 -0.1951 0.3784 138 GLN A O 1083 C CB . GLN A 139 ? 1.2056 0.9290 0.7343 -0.0180 -0.2083 0.3403 138 GLN A CB 1084 C CG . GLN A 139 ? 1.1708 0.9404 0.7363 0.0061 -0.2166 0.3227 138 GLN A CG 1085 C CD . GLN A 139 ? 1.1860 0.9387 0.7847 0.0412 -0.2425 0.3216 138 GLN A CD 1086 O OE1 . GLN A 139 ? 1.2181 0.9248 0.8177 0.0501 -0.2532 0.3314 138 GLN A OE1 1087 N NE2 . GLN A 139 ? 1.1561 0.9478 0.7846 0.0611 -0.2523 0.3078 138 GLN A NE2 1088 N N . GLY A 140 ? 1.2343 0.9565 0.6881 -0.1089 -0.1449 0.3490 139 GLY A N 1089 C CA . GLY A 140 ? 1.2904 0.9749 0.7025 -0.1407 -0.1352 0.3658 139 GLY A CA 1090 C C . GLY A 140 ? 1.2922 0.9436 0.7265 -0.1379 -0.1315 0.3654 139 GLY A C 1091 O O . GLY A 140 ? 1.3445 0.9529 0.7424 -0.1618 -0.1292 0.3829 139 GLY A O 1092 N N . ARG A 141 ? 1.2342 0.9045 0.7258 -0.1107 -0.1303 0.3455 140 ARG A N 1093 C CA . ARG A 141 ? 1.2302 0.8727 0.7455 -0.1069 -0.1262 0.3419 140 ARG A CA 1094 C C . ARG A 141 ? 1.1258 0.8171 0.6978 -0.0971 -0.1062 0.3126 140 ARG A C 1095 O O . ARG A 141 ? 1.0785 0.8171 0.6783 -0.0832 -0.1026 0.2959 140 ARG A O 1096 C CB . ARG A 141 ? 1.2924 0.8824 0.8108 -0.0798 -0.1548 0.3542 140 ARG A CB 1097 C CG . ARG A 141 ? 1.2926 0.9034 0.8414 -0.0445 -0.1737 0.3456 140 ARG A CG 1098 C CD . ARG A 141 ? 1.3677 0.9231 0.9107 -0.0204 -0.2053 0.3609 140 ARG A CD 1099 N NE . ARG A 141 ? 1.3468 0.9280 0.9401 0.0161 -0.2172 0.3434 140 ARG A NE 1100 C CZ . ARG A 141 ? 1.3430 0.9524 0.9428 0.0324 -0.2314 0.3409 140 ARG A CZ 1101 N NH1 . ARG A 141 ? 1.3828 0.9971 0.9397 0.0168 -0.2374 0.3555 140 ARG A NH1 1102 N NH2 . ARG A 141 ? 1.2981 0.9324 0.9476 0.0635 -0.2396 0.3227 140 ARG A NH2 1103 N N . SER A 142 ? 1.0826 0.7603 0.6692 -0.1056 -0.0942 0.3069 141 SER A N 1104 C CA . SER A 142 ? 0.9880 0.7077 0.6220 -0.1005 -0.0756 0.2811 141 SER A CA 1105 C C . SER A 142 ? 0.9280 0.6601 0.6055 -0.0658 -0.0855 0.2667 141 SER A C 1106 O O . SER A 142 ? 0.9515 0.6472 0.6313 -0.0461 -0.1044 0.2743 141 SER A O 1107 C CB . SER A 142 ? 0.9947 0.6930 0.6318 -0.1178 -0.0634 0.2795 141 SER A CB 1108 O OG . SER A 142 ? 1.0106 0.7206 0.6217 -0.1521 -0.0460 0.2830 141 SER A OG 1109 N N . SER A 143 ? 0.8430 0.6263 0.5549 -0.0592 -0.0726 0.2450 142 SER A N 1110 C CA . SER A 143 ? 0.7876 0.5891 0.5395 -0.0304 -0.0787 0.2297 142 SER A CA 1111 C C . SER A 143 ? 0.7159 0.5563 0.5034 -0.0313 -0.0600 0.2069 142 SER A C 1112 O O . SER A 143 ? 0.7032 0.5464 0.4894 -0.0500 -0.0457 0.2032 142 SER A O 1113 C CB . SER A 143 ? 0.7820 0.6051 0.5313 -0.0170 -0.0906 0.2310 142 SER A CB 1114 O OG . SER A 143 ? 0.7458 0.5812 0.5312 0.0102 -0.0989 0.2184 142 SER A OG 1115 N N . PHE A 144 ? 0.6655 0.5351 0.4839 -0.0118 -0.0612 0.1919 143 PHE A N 1116 C CA . PHE A 144 ? 0.6145 0.5152 0.4649 -0.0102 -0.0472 0.1716 143 PHE A CA 1117 C C . PHE A 144 ? 0.5755 0.5059 0.4509 0.0088 -0.0510 0.1591 143 PHE A C 1118 O O . PHE A 144 ? 0.5943 0.5210 0.4665 0.0222 -0.0647 0.1649 143 PHE A O 1119 C CB . PHE A 144 ? 0.6138 0.4900 0.4790 -0.0066 -0.0450 0.1668 143 PHE A CB 1120 C CG . PHE A 144 ? 0.5712 0.4715 0.4579 -0.0134 -0.0302 0.1503 143 PHE A CG 1121 C CD1 . PHE A 144 ? 0.5724 0.4868 0.4514 -0.0347 -0.0181 0.1488 143 PHE A CD1 1122 C CD2 . PHE A 144 ? 0.5380 0.4464 0.4523 0.0011 -0.0290 0.1358 143 PHE A CD2 1123 C CE1 . PHE A 144 ? 0.5399 0.4759 0.4404 -0.0391 -0.0075 0.1334 143 PHE A CE1 1124 C CE2 . PHE A 144 ? 0.5098 0.4363 0.4404 -0.0050 -0.0181 0.1222 143 PHE A CE2 1125 C CZ . PHE A 144 ? 0.5108 0.4507 0.4355 -0.0240 -0.0086 0.1211 143 PHE A CZ 1126 N N . PHE A 145 ? 0.5285 0.4875 0.4283 0.0093 -0.0396 0.1420 144 PHE A N 1127 C CA . PHE A 145 ? 0.4930 0.4775 0.4180 0.0248 -0.0410 0.1286 144 PHE A CA 1128 C C . PHE A 145 ? 0.4988 0.4657 0.4372 0.0443 -0.0520 0.1285 144 PHE A C 1129 O O . PHE A 145 ? 0.5128 0.4515 0.4525 0.0470 -0.0533 0.1308 144 PHE A O 1130 C CB . PHE A 145 ? 0.4501 0.4548 0.3961 0.0214 -0.0284 0.1123 144 PHE A CB 1131 C CG . PHE A 145 ? 0.4423 0.4673 0.3822 0.0048 -0.0180 0.1086 144 PHE A CG 1132 C CD1 . PHE A 145 ? 0.4287 0.4831 0.3681 0.0030 -0.0162 0.1033 144 PHE A CD1 1133 C CD2 . PHE A 145 ? 0.4433 0.4600 0.3800 -0.0088 -0.0100 0.1086 144 PHE A CD2 1134 C CE1 . PHE A 145 ? 0.4215 0.4969 0.3585 -0.0110 -0.0062 0.0969 144 PHE A CE1 1135 C CE2 . PHE A 145 ? 0.4392 0.4793 0.3751 -0.0233 -0.0003 0.1025 144 PHE A CE2 1136 C CZ . PHE A 145 ? 0.4251 0.4948 0.3618 -0.0237 0.0018 0.0960 144 PHE A CZ 1137 N N . ARG A 146 ? 0.4878 0.4731 0.4377 0.0577 -0.0597 0.1242 145 ARG A N 1138 C CA . ARG A 146 ? 0.4968 0.4711 0.4617 0.0773 -0.0716 0.1230 145 ARG A CA 1139 C C . ARG A 146 ? 0.4634 0.4473 0.4573 0.0852 -0.0633 0.1058 145 ARG A C 1140 O O . ARG A 146 ? 0.4831 0.4484 0.4881 0.0962 -0.0671 0.1029 145 ARG A O 1141 C CB . ARG A 146 ? 0.4985 0.4939 0.4670 0.0875 -0.0833 0.1234 145 ARG A CB 1142 C CG . ARG A 146 ? 0.5308 0.5235 0.4680 0.0781 -0.0911 0.1386 145 ARG A CG 1143 C CD . ARG A 146 ? 0.5835 0.5357 0.4973 0.0808 -0.1060 0.1574 145 ARG A CD 1144 N NE . ARG A 146 ? 0.6191 0.5691 0.5005 0.0732 -0.1165 0.1725 145 ARG A NE 1145 C CZ . ARG A 146 ? 0.6782 0.5907 0.5286 0.0705 -0.1303 0.1926 145 ARG A CZ 1146 N NH1 . ARG A 146 ? 0.7065 0.5795 0.5565 0.0759 -0.1355 0.1993 145 ARG A NH1 1147 N NH2 . ARG A 146 ? 0.7112 0.6231 0.5283 0.0616 -0.1393 0.2062 145 ARG A NH2 1148 N N . ASN A 147 ? 0.4229 0.4344 0.4270 0.0788 -0.0522 0.0941 146 ASN A N 1149 C CA . ASN A 147 ? 0.3950 0.4191 0.4226 0.0843 -0.0446 0.0782 146 ASN A CA 1150 C C . ASN A 147 ? 0.3926 0.3998 0.4203 0.0775 -0.0350 0.0737 146 ASN A C 1151 O O . ASN A 147 ? 0.3837 0.3952 0.4266 0.0814 -0.0292 0.0614 146 ASN A O 1152 C CB . ASN A 147 ? 0.3617 0.4185 0.3973 0.0799 -0.0390 0.0688 146 ASN A CB 1153 C CG . ASN A 147 ? 0.3618 0.4376 0.3993 0.0867 -0.0489 0.0707 146 ASN A CG 1154 O OD1 . ASN A 147 ? 0.3690 0.4418 0.4150 0.0999 -0.0593 0.0722 146 ASN A OD1 1155 N ND2 . ASN A 147 ? 0.3466 0.4426 0.3773 0.0783 -0.0465 0.0696 146 ASN A ND2 1156 N N . VAL A 148 ? 0.4022 0.3908 0.4121 0.0661 -0.0333 0.0831 147 VAL A N 1157 C CA . VAL A 148 ? 0.4007 0.3712 0.4094 0.0592 -0.0263 0.0797 147 VAL A CA 1158 C C . VAL A 148 ? 0.4412 0.3775 0.4349 0.0570 -0.0319 0.0919 147 VAL A C 1159 O O . VAL A 148 ? 0.4635 0.3909 0.4435 0.0577 -0.0404 0.1046 147 VAL A O 1160 C CB . VAL A 148 ? 0.3804 0.3646 0.3854 0.0444 -0.0174 0.0762 147 VAL A CB 1161 C CG1 . VAL A 148 ? 0.3461 0.3555 0.3651 0.0467 -0.0128 0.0637 147 VAL A CG1 1162 C CG2 . VAL A 148 ? 0.3842 0.3755 0.3738 0.0336 -0.0179 0.0860 147 VAL A CG2 1163 N N . VAL A 149 ? 0.4583 0.3735 0.4522 0.0534 -0.0278 0.0882 148 VAL A N 1164 C CA . VAL A 149 ? 0.4931 0.3707 0.4744 0.0519 -0.0333 0.0978 148 VAL A CA 1165 C C . VAL A 149 ? 0.5006 0.3656 0.4721 0.0343 -0.0259 0.0984 148 VAL A C 1166 O O . VAL A 149 ? 0.4799 0.3506 0.4608 0.0314 -0.0188 0.0865 148 VAL A O 1167 C CB . VAL A 149 ? 0.5093 0.3687 0.5044 0.0683 -0.0378 0.0898 148 VAL A CB 1168 C CG1 . VAL A 149 ? 0.5499 0.3654 0.5322 0.0667 -0.0439 0.0981 148 VAL A CG1 1169 C CG2 . VAL A 149 ? 0.5159 0.3888 0.5234 0.0862 -0.0470 0.0889 148 VAL A CG2 1170 N N . TRP A 150 ? 0.5228 0.3703 0.4742 0.0216 -0.0280 0.1123 149 TRP A N 1171 C CA . TRP A 150 ? 0.5309 0.3682 0.4734 0.0025 -0.0212 0.1135 149 TRP A CA 1172 C C . TRP A 150 ? 0.5633 0.3576 0.4994 0.0030 -0.0256 0.1163 149 TRP A C 1173 O O . TRP A 150 ? 0.5953 0.3588 0.5128 -0.0013 -0.0324 0.1306 149 TRP A O 1174 C CB . TRP A 150 ? 0.5465 0.3912 0.4702 -0.0144 -0.0191 0.1257 149 TRP A CB 1175 C CG . TRP A 150 ? 0.5530 0.3916 0.4681 -0.0366 -0.0114 0.1272 149 TRP A CG 1176 C CD1 . TRP A 150 ? 0.5473 0.3799 0.4716 -0.0431 -0.0066 0.1176 149 TRP A CD1 1177 C CD2 . TRP A 150 ? 0.5747 0.4165 0.4706 -0.0569 -0.0070 0.1376 149 TRP A CD2 1178 N NE1 . TRP A 150 ? 0.5610 0.3937 0.4758 -0.0657 -0.0002 0.1210 149 TRP A NE1 1179 C CE2 . TRP A 150 ? 0.5783 0.4173 0.4757 -0.0752 0.0007 0.1330 149 TRP A CE2 1180 C CE3 . TRP A 150 ? 0.5923 0.4402 0.4686 -0.0627 -0.0086 0.1496 149 TRP A CE3 1181 C CZ2 . TRP A 150 ? 0.5990 0.4434 0.4816 -0.0995 0.0083 0.1392 149 TRP A CZ2 1182 C CZ3 . TRP A 150 ? 0.6138 0.4648 0.4717 -0.0873 -0.0007 0.1565 149 TRP A CZ3 1183 C CH2 . TRP A 150 ? 0.6170 0.4672 0.4793 -0.1058 0.0083 0.1509 149 TRP A CH2 1184 N N . LEU A 151 ? 0.5494 0.3404 0.4990 0.0072 -0.0219 0.1024 150 LEU A N 1185 C CA . LEU A 151 ? 0.5813 0.3333 0.5280 0.0090 -0.0251 0.1006 150 LEU A CA 1186 C C . LEU A 151 ? 0.6005 0.3334 0.5328 -0.0130 -0.0215 0.1059 150 LEU A C 1187 O O . LEU A 151 ? 0.5802 0.3379 0.5143 -0.0278 -0.0138 0.1025 150 LEU A O 1188 C CB . LEU A 151 ? 0.5628 0.3213 0.5267 0.0188 -0.0207 0.0818 150 LEU A CB 1189 C CG . LEU A 151 ? 0.5420 0.3218 0.5228 0.0386 -0.0219 0.0731 150 LEU A CG 1190 C CD1 . LEU A 151 ? 0.5184 0.3105 0.5112 0.0412 -0.0141 0.0546 150 LEU A CD1 1191 C CD2 . LEU A 151 ? 0.5737 0.3292 0.5574 0.0561 -0.0325 0.0771 150 LEU A CD2 1192 N N . ILE A 152 ? 0.6451 0.3340 0.5649 -0.0151 -0.0276 0.1132 151 ILE A N 1193 C CA . ILE A 152 ? 0.6711 0.3384 0.5784 -0.0372 -0.0239 0.1163 151 ILE A CA 1194 C C . ILE A 152 ? 0.7008 0.3279 0.6093 -0.0320 -0.0277 0.1087 151 ILE A C 1195 O O . ILE A 152 ? 0.7069 0.3241 0.6263 -0.0108 -0.0329 0.1009 151 ILE A O 1196 C CB . ILE A 152 ? 0.7117 0.3611 0.5940 -0.0540 -0.0265 0.1365 151 ILE A CB 1197 C CG1 . ILE A 152 ? 0.7618 0.3656 0.6292 -0.0415 -0.0406 0.1502 151 ILE A CG1 1198 C CG2 . ILE A 152 ? 0.6845 0.3761 0.5657 -0.0592 -0.0215 0.1411 151 ILE A CG2 1199 C CD1 . ILE A 152 ? 0.8082 0.3872 0.6441 -0.0601 -0.0444 0.1722 151 ILE A CD1 1200 N N . LYS A 153 ? 0.7242 0.3299 0.6229 -0.0520 -0.0247 0.1093 152 LYS A N 1201 C CA . LYS A 153 ? 0.7526 0.3190 0.6513 -0.0497 -0.0278 0.1006 152 LYS A CA 1202 C C . LYS A 153 ? 0.8046 0.3218 0.6931 -0.0361 -0.0404 0.1106 152 LYS A C 1203 O O . LYS A 153 ? 0.8282 0.3321 0.7009 -0.0375 -0.0474 0.1292 152 LYS A O 1204 C CB . LYS A 153 ? 0.7682 0.3226 0.6577 -0.0767 -0.0225 0.0999 152 LYS A CB 1205 C CG . LYS A 153 ? 0.8161 0.3365 0.6812 -0.0961 -0.0257 0.1195 152 LYS A CG 1206 C CD . LYS A 153 ? 0.8189 0.3485 0.6800 -0.1265 -0.0168 0.1173 152 LYS A CD 1207 C CE . LYS A 153 ? 0.8725 0.3580 0.7068 -0.1491 -0.0192 0.1346 152 LYS A CE 1208 N NZ . LYS A 153 ? 0.8734 0.3718 0.7081 -0.1797 -0.0095 0.1293 152 LYS A NZ 1209 N N . LYS A 154 ? 0.8275 0.3173 0.7246 -0.0229 -0.0440 0.0973 153 LYS A N 1210 C CA . LYS A 154 ? 0.8791 0.3190 0.7710 -0.0073 -0.0575 0.1028 153 LYS A CA 1211 C C . LYS A 154 ? 0.9234 0.3176 0.8086 -0.0169 -0.0584 0.0953 153 LYS A C 1212 O O . LYS A 154 ? 0.9029 0.3087 0.8001 -0.0180 -0.0504 0.0754 153 LYS A O 1213 C CB . LYS A 154 ? 0.8617 0.3167 0.7774 0.0237 -0.0613 0.0890 153 LYS A CB 1214 C CG . LYS A 154 ? 0.9147 0.3232 0.8313 0.0449 -0.0776 0.0926 153 LYS A CG 1215 C CD . LYS A 154 ? 0.8935 0.3242 0.8399 0.0746 -0.0790 0.0734 153 LYS A CD 1216 C CE . LYS A 154 ? 0.9436 0.3304 0.8953 0.0984 -0.0974 0.0756 153 LYS A CE 1217 N NZ . LYS A 154 ? 0.9240 0.3390 0.9093 0.1275 -0.0980 0.0548 153 LYS A NZ 1218 N N . ASP A 155 ? 0.9900 0.3307 0.8537 -0.0250 -0.0687 0.1115 154 ASP A N 1219 C CA . ASP A 155 ? 1.0409 0.3320 0.8956 -0.0363 -0.0706 0.1060 154 ASP A CA 1220 C C . ASP A 155 ? 1.0111 0.3249 0.8654 -0.0635 -0.0565 0.0960 154 ASP A C 1221 O O . ASP A 155 ? 1.0090 0.3128 0.8714 -0.0643 -0.0530 0.0771 154 ASP A O 1222 C CB . ASP A 155 ? 1.0689 0.3364 0.9423 -0.0091 -0.0767 0.0857 154 ASP A CB 1223 C CG . ASP A 155 ? 1.1175 0.3561 0.9937 0.0183 -0.0940 0.0945 154 ASP A CG 1224 O OD1 . ASP A 155 ? 1.1524 0.3756 1.0088 0.0139 -0.1037 0.1193 154 ASP A OD1 1225 O OD2 . ASP A 155 ? 1.1314 0.3628 1.0296 0.0446 -0.0983 0.0757 154 ASP A OD2 1226 N N . ASN A 156 ? 0.9849 0.3306 0.8304 -0.0855 -0.0489 0.1078 155 ASN A N 1227 C CA . ASN A 156 ? 0.9592 0.3360 0.8088 -0.1101 -0.0367 0.0984 155 ASN A CA 1228 C C . ASN A 156 ? 0.9075 0.3216 0.7798 -0.0992 -0.0301 0.0742 155 ASN A C 1229 O O . ASN A 156 ? 0.8998 0.3211 0.7751 -0.1151 -0.0246 0.0617 155 ASN A O 1230 C CB . ASN A 156 ? 1.0122 0.3440 0.8452 -0.1359 -0.0373 0.1007 155 ASN A CB 1231 C CG . ASN A 156 ? 1.0514 0.3653 0.8594 -0.1606 -0.0377 0.1245 155 ASN A CG 1232 O OD1 . ASN A 156 ? 1.0228 0.3788 0.8301 -0.1713 -0.0305 0.1328 155 ASN A OD1 1233 N ND2 . ASN A 156 ? 1.1161 0.3661 0.9021 -0.1707 -0.0458 0.1353 155 ASN A ND2 1234 N N . ALA A 157 ? 0.8724 0.3103 0.7591 -0.0735 -0.0311 0.0680 156 ALA A N 1235 C CA . ALA A 157 ? 0.8316 0.3034 0.7355 -0.0638 -0.0247 0.0468 156 ALA A CA 1236 C C . ALA A 157 ? 0.7809 0.2985 0.6970 -0.0480 -0.0222 0.0480 156 ALA A C 1237 O O . ALA A 157 ? 0.7737 0.2873 0.6898 -0.0337 -0.0278 0.0592 156 ALA A O 1238 C CB . ALA A 157 ? 0.8563 0.2964 0.7657 -0.0477 -0.0276 0.0297 156 ALA A CB 1239 N N . TYR A 158 ? 0.7477 0.3069 0.6730 -0.0515 -0.0150 0.0368 157 TYR A N 1240 C CA . TYR A 158 ? 0.7054 0.3073 0.6422 -0.0382 -0.0120 0.0350 157 TYR A CA 1241 C C . TYR A 158 ? 0.6926 0.3106 0.6367 -0.0336 -0.0069 0.0147 157 TYR A C 1242 O O . TYR A 158 ? 0.6739 0.3141 0.6174 -0.0464 -0.0038 0.0092 157 TYR A O 1243 C CB . TYR A 158 ? 0.6745 0.3119 0.6108 -0.0517 -0.0091 0.0456 157 TYR A CB 1244 C CG . TYR A 158 ? 0.6262 0.3035 0.5724 -0.0390 -0.0073 0.0471 157 TYR A CG 1245 C CD1 . TYR A 158 ? 0.5984 0.3002 0.5543 -0.0295 -0.0039 0.0333 157 TYR A CD1 1246 C CD2 . TYR A 158 ? 0.6208 0.3098 0.5640 -0.0388 -0.0089 0.0623 157 TYR A CD2 1247 C CE1 . TYR A 158 ? 0.5623 0.2978 0.5262 -0.0201 -0.0024 0.0347 157 TYR A CE1 1248 C CE2 . TYR A 158 ? 0.5868 0.3113 0.5388 -0.0286 -0.0075 0.0627 157 TYR A CE2 1249 C CZ . TYR A 158 ? 0.5553 0.3023 0.5185 -0.0192 -0.0044 0.0489 157 TYR A CZ 1250 O OH . TYR A 158 ? 0.5175 0.2966 0.4887 -0.0104 -0.0032 0.0493 157 TYR A OH 1251 N N . PRO A 159 ? 0.7071 0.3132 0.6575 -0.0156 -0.0067 0.0027 158 PRO A N 1252 C CA . PRO A 159 ? 0.6940 0.3151 0.6476 -0.0126 -0.0005 -0.0168 158 PRO A CA 1253 C C . PRO A 159 ? 0.6537 0.3191 0.6114 -0.0122 0.0037 -0.0170 158 PRO A C 1254 O O . PRO A 159 ? 0.6375 0.3228 0.6006 -0.0073 0.0022 -0.0047 158 PRO A O 1255 C CB . PRO A 159 ? 0.7123 0.3169 0.6755 0.0083 -0.0002 -0.0283 158 PRO A CB 1256 C CG . PRO A 159 ? 0.7505 0.3150 0.7116 0.0122 -0.0091 -0.0171 158 PRO A CG 1257 C CD . PRO A 159 ? 0.7356 0.3101 0.6896 0.0013 -0.0128 0.0054 158 PRO A CD 1258 N N . THR A 160 ? 0.6449 0.3231 0.5979 -0.0180 0.0080 -0.0306 159 THR A N 1259 C CA . THR A 160 ? 0.6159 0.3298 0.5698 -0.0178 0.0108 -0.0313 159 THR A CA 1260 C C . THR A 160 ? 0.6000 0.3272 0.5646 -0.0002 0.0146 -0.0335 159 THR A C 1261 O O . THR A 160 ? 0.6192 0.3350 0.5883 0.0101 0.0185 -0.0460 159 THR A O 1262 C CB . THR A 160 ? 0.6235 0.3417 0.5656 -0.0269 0.0136 -0.0459 159 THR A CB 1263 O OG1 . THR A 160 ? 0.6399 0.3432 0.5741 -0.0424 0.0090 -0.0466 159 THR A OG1 1264 C CG2 . THR A 160 ? 0.5962 0.3462 0.5357 -0.0293 0.0136 -0.0432 159 THR A CG2 1265 N N . ILE A 161 ? 0.5758 0.3285 0.5465 0.0030 0.0136 -0.0227 160 ILE A N 1266 C CA . ILE A 161 ? 0.5721 0.3406 0.5545 0.0184 0.0164 -0.0245 160 ILE A CA 1267 C C . ILE A 161 ? 0.5687 0.3593 0.5475 0.0161 0.0233 -0.0358 160 ILE A C 1268 O O . ILE A 161 ? 0.5475 0.3485 0.5157 0.0042 0.0223 -0.0338 160 ILE A O 1269 C CB . ILE A 161 ? 0.5561 0.3405 0.5453 0.0222 0.0116 -0.0080 160 ILE A CB 1270 C CG1 . ILE A 161 ? 0.5824 0.3405 0.5717 0.0254 0.0049 0.0032 160 ILE A CG1 1271 C CG2 . ILE A 161 ? 0.5354 0.3438 0.5368 0.0354 0.0145 -0.0112 160 ILE A CG2 1272 C CD1 . ILE A 161 ? 0.5805 0.3507 0.5695 0.0239 0.0001 0.0206 160 ILE A CD1 1273 N N . LYS A 162 ? 0.5826 0.3792 0.5700 0.0271 0.0299 -0.0483 161 LYS A N 1274 C CA . LYS A 162 ? 0.5752 0.3950 0.5592 0.0245 0.0380 -0.0578 161 LYS A CA 1275 C C . LYS A 162 ? 0.5662 0.4056 0.5700 0.0391 0.0416 -0.0612 161 LYS A C 1276 O O . LYS A 162 ? 0.6068 0.4418 0.6233 0.0502 0.0458 -0.0743 161 LYS A O 1277 C CB . LYS A 162 ? 0.5901 0.3999 0.5611 0.0176 0.0458 -0.0758 161 LYS A CB 1278 C CG . LYS A 162 ? 0.6056 0.4004 0.5561 0.0018 0.0410 -0.0733 161 LYS A CG 1279 C CD . LYS A 162 ? 0.6285 0.4134 0.5615 -0.0068 0.0480 -0.0911 161 LYS A CD 1280 C CE . LYS A 162 ? 0.6435 0.4121 0.5585 -0.0214 0.0402 -0.0882 161 LYS A CE 1281 N NZ . LYS A 162 ? 0.6711 0.4316 0.5630 -0.0327 0.0451 -0.1040 161 LYS A NZ 1282 N N . ARG A 163 ? 0.5403 0.4019 0.5485 0.0396 0.0394 -0.0509 162 ARG A N 1283 C CA . ARG A 163 ? 0.5375 0.4215 0.5650 0.0519 0.0422 -0.0546 162 ARG A CA 1284 C C . ARG A 163 ? 0.5003 0.4094 0.5225 0.0434 0.0480 -0.0561 162 ARG A C 1285 O O . ARG A 163 ? 0.4908 0.4035 0.5017 0.0344 0.0435 -0.0448 162 ARG A O 1286 C CB . ARG A 163 ? 0.5440 0.4291 0.5838 0.0625 0.0319 -0.0397 162 ARG A CB 1287 C CG . ARG A 163 ? 0.5919 0.4487 0.6360 0.0717 0.0243 -0.0357 162 ARG A CG 1288 C CD . ARG A 163 ? 0.6371 0.4856 0.6958 0.0846 0.0281 -0.0537 162 ARG A CD 1289 N NE . ARG A 163 ? 0.6783 0.5106 0.7507 0.1012 0.0170 -0.0476 162 ARG A NE 1290 C CZ . ARG A 163 ? 0.6764 0.5260 0.7658 0.1148 0.0107 -0.0435 162 ARG A CZ 1291 N NH1 . ARG A 163 ? 0.6509 0.5362 0.7478 0.1132 0.0160 -0.0460 162 ARG A NH1 1292 N NH2 . ARG A 163 ? 0.7051 0.5345 0.8031 0.1296 -0.0020 -0.0366 162 ARG A NH2 1293 N N . SER A 164 ? 0.4951 0.4213 0.5264 0.0462 0.0581 -0.0710 163 SER A N 1294 C CA . SER A 164 ? 0.4796 0.4295 0.5077 0.0380 0.0643 -0.0728 163 SER A CA 1295 C C . SER A 164 ? 0.4605 0.4352 0.5152 0.0510 0.0637 -0.0742 163 SER A C 1296 O O . SER A 164 ? 0.4667 0.4430 0.5430 0.0663 0.0626 -0.0816 163 SER A O 1297 C CB . SER A 164 ? 0.4908 0.4439 0.5062 0.0268 0.0780 -0.0900 163 SER A CB 1298 O OG . SER A 164 ? 0.5018 0.4324 0.4895 0.0138 0.0765 -0.0880 163 SER A OG 1299 N N . TYR A 165 ? 0.4298 0.4227 0.4835 0.0455 0.0628 -0.0673 164 TYR A N 1300 C CA . TYR A 165 ? 0.4149 0.4363 0.4922 0.0537 0.0647 -0.0725 164 TYR A CA 1301 C C . TYR A 165 ? 0.4118 0.4515 0.4808 0.0387 0.0750 -0.0789 164 TYR A C 1302 O O . TYR A 165 ? 0.4041 0.4363 0.4517 0.0258 0.0726 -0.0690 164 TYR A O 1303 C CB . TYR A 165 ? 0.3890 0.4154 0.4757 0.0629 0.0518 -0.0571 164 TYR A CB 1304 C CG . TYR A 165 ? 0.3723 0.4298 0.4798 0.0680 0.0528 -0.0621 164 TYR A CG 1305 C CD1 . TYR A 165 ? 0.3786 0.4513 0.5145 0.0844 0.0512 -0.0719 164 TYR A CD1 1306 C CD2 . TYR A 165 ? 0.3556 0.4272 0.4558 0.0566 0.0546 -0.0583 164 TYR A CD2 1307 C CE1 . TYR A 165 ? 0.3677 0.4725 0.5251 0.0887 0.0513 -0.0779 164 TYR A CE1 1308 C CE2 . TYR A 165 ? 0.3456 0.4465 0.4651 0.0595 0.0557 -0.0638 164 TYR A CE2 1309 C CZ . TYR A 165 ? 0.3515 0.4706 0.4998 0.0751 0.0542 -0.0738 164 TYR A CZ 1310 O OH . TYR A 165 ? 0.3426 0.4937 0.5116 0.0771 0.0546 -0.0803 164 TYR A OH 1311 N N . ASN A 166 ? 0.4209 0.4846 0.5078 0.0403 0.0859 -0.0958 165 ASN A N 1312 C CA . ASN A 166 ? 0.4292 0.5113 0.5088 0.0239 0.0978 -0.1037 165 ASN A CA 1313 C C . ASN A 166 ? 0.3981 0.5089 0.5005 0.0288 0.0947 -0.1026 165 ASN A C 1314 O O . ASN A 166 ? 0.3941 0.5256 0.5280 0.0445 0.0931 -0.1112 165 ASN A O 1315 C CB . ASN A 166 ? 0.4680 0.5612 0.5528 0.0196 0.1145 -0.1262 165 ASN A CB 1316 C CG . ASN A 166 ? 0.5027 0.6115 0.5734 -0.0021 0.1294 -0.1350 165 ASN A CG 1317 O OD1 . ASN A 166 ? 0.5008 0.6291 0.5792 -0.0073 0.1298 -0.1326 165 ASN A OD1 1318 N ND2 . ASN A 166 ? 0.5615 0.6610 0.6095 -0.0165 0.1421 -0.1457 165 ASN A ND2 1319 N N . ASN A 167 ? 0.3763 0.4875 0.4635 0.0161 0.0924 -0.0925 166 ASN A N 1320 C CA . ASN A 167 ? 0.3529 0.4914 0.4594 0.0177 0.0905 -0.0931 166 ASN A CA 1321 C C . ASN A 167 ? 0.3613 0.5289 0.4813 0.0081 0.1065 -0.1125 166 ASN A C 1322 O O . ASN A 167 ? 0.3732 0.5408 0.4740 -0.0123 0.1153 -0.1138 166 ASN A O 1323 C CB . ASN A 167 ? 0.3328 0.4611 0.4195 0.0071 0.0830 -0.0781 166 ASN A CB 1324 C CG . ASN A 167 ? 0.3079 0.4629 0.4148 0.0097 0.0794 -0.0788 166 ASN A CG 1325 O OD1 . ASN A 167 ? 0.3000 0.4795 0.4364 0.0231 0.0780 -0.0867 166 ASN A OD1 1326 N ND2 . ASN A 167 ? 0.2972 0.4469 0.3886 -0.0025 0.0766 -0.0713 166 ASN A ND2 1327 N N . THR A 168 ? 0.3671 0.5595 0.5207 0.0226 0.1097 -0.1277 167 THR A N 1328 C CA . THR A 168 ? 0.3862 0.6141 0.5607 0.0152 0.1257 -0.1495 167 THR A CA 1329 C C . THR A 168 ? 0.3750 0.6339 0.5694 0.0124 0.1235 -0.1509 167 THR A C 1330 O O . THR A 168 ? 0.3901 0.6812 0.6019 0.0028 0.1372 -0.1689 167 THR A O 1331 C CB . THR A 168 ? 0.3968 0.6430 0.6061 0.0345 0.1289 -0.1687 167 THR A CB 1332 O OG1 . THR A 168 ? 0.3975 0.6373 0.6256 0.0594 0.1095 -0.1585 167 THR A OG1 1333 C CG2 . THR A 168 ? 0.4149 0.6395 0.6061 0.0302 0.1390 -0.1768 167 THR A CG2 1334 N N . ASN A 169 ? 0.3650 0.6156 0.5569 0.0196 0.1071 -0.1335 168 ASN A N 1335 C CA . ASN A 169 ? 0.3521 0.6293 0.5606 0.0174 0.1027 -0.1338 168 ASN A CA 1336 C C . ASN A 169 ? 0.3593 0.6292 0.5409 -0.0086 0.1103 -0.1295 168 ASN A C 1337 O O . ASN A 169 ? 0.3798 0.6179 0.5264 -0.0219 0.1132 -0.1205 168 ASN A O 1338 C CB . ASN A 169 ? 0.3381 0.6071 0.5500 0.0340 0.0824 -0.1170 168 ASN A CB 1339 C CG . ASN A 169 ? 0.3391 0.6024 0.5674 0.0585 0.0714 -0.1152 168 ASN A CG 1340 O OD1 . ASN A 169 ? 0.3332 0.6228 0.5949 0.0740 0.0668 -0.1259 168 ASN A OD1 1341 N ND2 . ASN A 169 ? 0.3435 0.5710 0.5484 0.0620 0.0658 -0.1014 168 ASN A ND2 1342 N N . GLN A 170 ? 0.3512 0.6488 0.5491 -0.0154 0.1112 -0.1354 169 GLN A N 1343 C CA . GLN A 170 ? 0.3535 0.6434 0.5279 -0.0405 0.1171 -0.1318 169 GLN A CA 1344 C C . GLN A 170 ? 0.3401 0.6032 0.4938 -0.0392 0.1016 -0.1123 169 GLN A C 1345 O O . GLN A 170 ? 0.3503 0.5937 0.4775 -0.0580 0.1032 -0.1059 169 GLN A O 1346 C CB . GLN A 170 ? 0.3545 0.6863 0.5570 -0.0495 0.1244 -0.1475 169 GLN A CB 1347 C CG . GLN A 170 ? 0.3691 0.7318 0.5911 -0.0577 0.1439 -0.1703 169 GLN A CG 1348 C CD . GLN A 170 ? 0.3988 0.7370 0.5834 -0.0818 0.1605 -0.1710 169 GLN A CD 1349 O OE1 . GLN A 170 ? 0.4212 0.7658 0.6099 -0.0806 0.1725 -0.1836 169 GLN A OE1 1350 N NE2 . GLN A 170 ? 0.4061 0.7144 0.5528 -0.1035 0.1601 -0.1577 169 GLN A NE2 1351 N N . GLU A 171 ? 0.3215 0.5839 0.4872 -0.0175 0.0864 -0.1037 170 GLU A N 1352 C CA . GLU A 171 ? 0.3065 0.5484 0.4562 -0.0144 0.0724 -0.0876 170 GLU A CA 1353 C C . GLU A 171 ? 0.3052 0.5084 0.4255 -0.0147 0.0692 -0.0747 170 GLU A C 1354 O O . GLU A 171 ? 0.3137 0.5083 0.4327 -0.0079 0.0724 -0.0758 170 GLU A O 1355 C CB . GLU A 171 ? 0.2978 0.5553 0.4693 0.0067 0.0584 -0.0837 170 GLU A CB 1356 C CG . GLU A 171 ? 0.3009 0.5967 0.5015 0.0089 0.0563 -0.0945 170 GLU A CG 1357 C CD . GLU A 171 ? 0.3091 0.6360 0.5421 0.0179 0.0621 -0.1107 170 GLU A CD 1358 O OE1 . GLU A 171 ? 0.3149 0.6328 0.5505 0.0281 0.0647 -0.1122 170 GLU A OE1 1359 O OE2 . GLU A 171 ? 0.3140 0.6758 0.5722 0.0150 0.0638 -0.1234 170 GLU A OE2 1360 N N . ASP A 172 ? 0.3026 0.4833 0.4011 -0.0220 0.0624 -0.0640 171 ASP A N 1361 C CA . ASP A 172 ? 0.2982 0.4480 0.3760 -0.0175 0.0544 -0.0514 171 ASP A CA 1362 C C . ASP A 172 ? 0.2746 0.4316 0.3678 0.0024 0.0455 -0.0462 171 ASP A C 1363 O O . ASP A 172 ? 0.2518 0.4310 0.3639 0.0113 0.0401 -0.0477 171 ASP A O 1364 C CB . ASP A 172 ? 0.3039 0.4353 0.3648 -0.0243 0.0458 -0.0432 171 ASP A CB 1365 C CG . ASP A 172 ? 0.3313 0.4462 0.3709 -0.0448 0.0512 -0.0448 171 ASP A CG 1366 O OD1 . ASP A 172 ? 0.3639 0.4720 0.3914 -0.0558 0.0614 -0.0489 171 ASP A OD1 1367 O OD2 . ASP A 172 ? 0.3476 0.4536 0.3802 -0.0506 0.0447 -0.0419 171 ASP A OD2 1368 N N . LEU A 173 ? 0.2701 0.4066 0.3527 0.0081 0.0430 -0.0396 172 LEU A N 1369 C CA . LEU A 173 ? 0.2618 0.3995 0.3545 0.0243 0.0357 -0.0338 172 LEU A CA 1370 C C . LEU A 173 ? 0.2487 0.3667 0.3258 0.0249 0.0273 -0.0220 172 LEU A C 1371 O O . LEU A 173 ? 0.2471 0.3440 0.3072 0.0179 0.0284 -0.0194 172 LEU A O 1372 C CB . LEU A 173 ? 0.2755 0.4073 0.3721 0.0296 0.0415 -0.0388 172 LEU A CB 1373 C CG . LEU A 173 ? 0.2785 0.4076 0.3860 0.0462 0.0344 -0.0342 172 LEU A CG 1374 C CD1 . LEU A 173 ? 0.2768 0.4305 0.4065 0.0580 0.0277 -0.0359 172 LEU A CD1 1375 C CD2 . LEU A 173 ? 0.2940 0.4149 0.4047 0.0496 0.0415 -0.0424 172 LEU A CD2 1376 N N . LEU A 174 ? 0.2382 0.3647 0.3210 0.0324 0.0190 -0.0160 173 LEU A N 1377 C CA . LEU A 174 ? 0.2301 0.3430 0.3017 0.0332 0.0127 -0.0069 173 LEU A CA 1378 C C . LEU A 174 ? 0.2351 0.3372 0.3060 0.0409 0.0110 -0.0009 173 LEU A C 1379 O O . LEU A 174 ? 0.2295 0.3396 0.3095 0.0503 0.0075 0.0016 173 LEU A O 1380 C CB . LEU A 174 ? 0.2267 0.3543 0.3023 0.0356 0.0064 -0.0045 173 LEU A CB 1381 C CG . LEU A 174 ? 0.2319 0.3544 0.3002 0.0371 0.0011 0.0026 173 LEU A CG 1382 C CD1 . LEU A 174 ? 0.2347 0.3405 0.2930 0.0302 0.0010 0.0023 173 LEU A CD1 1383 C CD2 . LEU A 174 ? 0.2307 0.3714 0.3027 0.0384 -0.0032 0.0017 173 LEU A CD2 1384 N N . VAL A 175 ? 0.2414 0.3234 0.3006 0.0365 0.0124 0.0013 174 VAL A N 1385 C CA . VAL A 175 ? 0.2503 0.3184 0.3074 0.0414 0.0114 0.0061 174 VAL A CA 1386 C C . VAL A 175 ? 0.2490 0.3102 0.2984 0.0389 0.0065 0.0141 174 VAL A C 1387 O O . VAL A 175 ? 0.2588 0.3197 0.3031 0.0327 0.0051 0.0132 174 VAL A O 1388 C CB . VAL A 175 ? 0.2575 0.3095 0.3081 0.0374 0.0173 0.0008 174 VAL A CB 1389 C CG1 . VAL A 175 ? 0.2676 0.3035 0.3170 0.0426 0.0159 0.0047 174 VAL A CG1 1390 C CG2 . VAL A 175 ? 0.2633 0.3268 0.3225 0.0377 0.0246 -0.0096 174 VAL A CG2 1391 N N . LEU A 176 ? 0.2522 0.3079 0.3013 0.0435 0.0037 0.0212 175 LEU A N 1392 C CA . LEU A 176 ? 0.2600 0.3124 0.3025 0.0393 0.0008 0.0282 175 LEU A CA 1393 C C . LEU A 176 ? 0.2714 0.3034 0.3080 0.0385 0.0008 0.0333 175 LEU A C 1394 O O . LEU A 176 ? 0.2664 0.2892 0.3049 0.0454 -0.0003 0.0357 175 LEU A O 1395 C CB . LEU A 176 ? 0.2694 0.3365 0.3128 0.0422 -0.0029 0.0338 175 LEU A CB 1396 C CG . LEU A 176 ? 0.2634 0.3516 0.3130 0.0438 -0.0039 0.0288 175 LEU A CG 1397 C CD1 . LEU A 176 ? 0.2786 0.3787 0.3247 0.0454 -0.0082 0.0350 175 LEU A CD1 1398 C CD2 . LEU A 176 ? 0.2588 0.3514 0.3083 0.0372 -0.0025 0.0225 175 LEU A CD2 1399 N N . TRP A 177 ? 0.2787 0.3036 0.3098 0.0304 0.0012 0.0340 176 TRP A N 1400 C CA . TRP A 177 ? 0.2985 0.3047 0.3235 0.0265 0.0012 0.0388 176 TRP A CA 1401 C C . TRP A 177 ? 0.2950 0.3076 0.3179 0.0169 0.0009 0.0410 176 TRP A C 1402 O O . TRP A 177 ? 0.2725 0.3032 0.3002 0.0151 0.0004 0.0371 176 TRP A O 1403 C CB . TRP A 177 ? 0.3071 0.2960 0.3296 0.0252 0.0033 0.0326 176 TRP A CB 1404 C CG . TRP A 177 ? 0.3009 0.2924 0.3213 0.0186 0.0031 0.0265 176 TRP A CG 1405 C CD1 . TRP A 177 ? 0.3096 0.2940 0.3265 0.0107 0.0011 0.0256 176 TRP A CD1 1406 C CD2 . TRP A 177 ? 0.2992 0.2994 0.3200 0.0190 0.0032 0.0206 176 TRP A CD2 1407 N NE1 . TRP A 177 ? 0.3046 0.2920 0.3196 0.0078 -0.0016 0.0199 176 TRP A NE1 1408 C CE2 . TRP A 177 ? 0.3001 0.2950 0.3157 0.0121 -0.0003 0.0175 176 TRP A CE2 1409 C CE3 . TRP A 177 ? 0.2910 0.3021 0.3157 0.0235 0.0053 0.0177 176 TRP A CE3 1410 C CZ2 . TRP A 177 ? 0.3021 0.2981 0.3134 0.0100 -0.0028 0.0132 176 TRP A CZ2 1411 C CZ3 . TRP A 177 ? 0.2934 0.3069 0.3141 0.0194 0.0047 0.0128 176 TRP A CZ3 1412 C CH2 . TRP A 177 ? 0.2979 0.3014 0.3103 0.0129 0.0002 0.0113 176 TRP A CH2 1413 N N . GLY A 178 ? 0.3094 0.3076 0.3266 0.0106 0.0013 0.0460 177 GLY A N 1414 C CA . GLY A 178 ? 0.3135 0.3207 0.3309 -0.0001 0.0025 0.0466 177 GLY A CA 1415 C C . GLY A 178 ? 0.3273 0.3171 0.3411 -0.0089 0.0032 0.0469 177 GLY A C 1416 O O . GLY A 178 ? 0.3499 0.3178 0.3593 -0.0063 0.0025 0.0468 177 GLY A O 1417 N N . ILE A 179 ? 0.3267 0.3284 0.3440 -0.0200 0.0048 0.0455 178 ILE A N 1418 C CA . ILE A 179 ? 0.3431 0.3326 0.3590 -0.0311 0.0055 0.0447 178 ILE A CA 1419 C C . ILE A 179 ? 0.3502 0.3494 0.3639 -0.0446 0.0102 0.0494 178 ILE A C 1420 O O . ILE A 179 ? 0.3394 0.3648 0.3593 -0.0466 0.0128 0.0468 178 ILE A O 1421 C CB . ILE A 179 ? 0.3368 0.3347 0.3631 -0.0330 0.0020 0.0335 178 ILE A CB 1422 C CG1 . ILE A 179 ? 0.3591 0.3463 0.3850 -0.0456 0.0022 0.0319 178 ILE A CG1 1423 C CG2 . ILE A 179 ? 0.3185 0.3476 0.3592 -0.0325 0.0008 0.0263 178 ILE A CG2 1424 C CD1 . ILE A 179 ? 0.3583 0.3484 0.3916 -0.0469 -0.0040 0.0214 178 ILE A CD1 1425 N N . HIS A 180 ? 0.3771 0.3541 0.3806 -0.0548 0.0118 0.0559 179 HIS A N 1426 C CA . HIS A 180 ? 0.3947 0.3771 0.3917 -0.0716 0.0176 0.0617 179 HIS A CA 1427 C C . HIS A 180 ? 0.3886 0.3875 0.3991 -0.0860 0.0205 0.0517 179 HIS A C 1428 O O . HIS A 180 ? 0.3905 0.3733 0.4028 -0.0892 0.0177 0.0479 179 HIS A O 1429 C CB . HIS A 180 ? 0.4311 0.3765 0.4073 -0.0767 0.0169 0.0756 179 HIS A CB 1430 C CG . HIS A 180 ? 0.4588 0.4043 0.4225 -0.0972 0.0231 0.0837 179 HIS A CG 1431 N ND1 . HIS A 180 ? 0.4947 0.4114 0.4462 -0.1121 0.0242 0.0900 179 HIS A ND1 1432 C CD2 . HIS A 180 ? 0.4592 0.4299 0.4190 -0.1073 0.0295 0.0856 179 HIS A CD2 1433 C CE1 . HIS A 180 ? 0.5174 0.4407 0.4567 -0.1316 0.0311 0.0968 179 HIS A CE1 1434 N NE2 . HIS A 180 ? 0.4991 0.4564 0.4430 -0.1291 0.0349 0.0939 179 HIS A NE2 1435 N N . HIS A 181 ? 0.3809 0.4136 0.4017 -0.0944 0.0260 0.0459 180 HIS A N 1436 C CA . HIS A 181 ? 0.3781 0.4347 0.4167 -0.1084 0.0293 0.0342 180 HIS A CA 1437 C C . HIS A 181 ? 0.4140 0.4683 0.4410 -0.1315 0.0389 0.0409 180 HIS A C 1438 O O . HIS A 181 ? 0.4127 0.4909 0.4384 -0.1405 0.0471 0.0406 180 HIS A O 1439 C CB . HIS A 181 ? 0.3518 0.4505 0.4125 -0.1033 0.0303 0.0207 180 HIS A CB 1440 C CG . HIS A 181 ? 0.3280 0.4288 0.3989 -0.0831 0.0206 0.0142 180 HIS A CG 1441 N ND1 . HIS A 181 ? 0.3281 0.4139 0.4032 -0.0764 0.0115 0.0101 180 HIS A ND1 1442 C CD2 . HIS A 181 ? 0.3057 0.4215 0.3818 -0.0702 0.0187 0.0107 180 HIS A CD2 1443 C CE1 . HIS A 181 ? 0.3021 0.3918 0.3826 -0.0610 0.0045 0.0057 180 HIS A CE1 1444 N NE2 . HIS A 181 ? 0.2916 0.3990 0.3739 -0.0568 0.0086 0.0058 180 HIS A NE2 1445 N N . PRO A 182 ? 0.4550 0.4803 0.4720 -0.1431 0.0385 0.0462 181 PRO A N 1446 C CA . PRO A 182 ? 0.4984 0.5133 0.4980 -0.1669 0.0473 0.0557 181 PRO A CA 1447 C C . PRO A 182 ? 0.5115 0.5658 0.5286 -0.1886 0.0575 0.0436 181 PRO A C 1448 O O . PRO A 182 ? 0.4746 0.5646 0.5215 -0.1837 0.0559 0.0261 181 PRO A O 1449 C CB . PRO A 182 ? 0.5236 0.4929 0.5096 -0.1711 0.0424 0.0629 181 PRO A CB 1450 C CG . PRO A 182 ? 0.5001 0.4674 0.5021 -0.1540 0.0332 0.0521 181 PRO A CG 1451 C CD . PRO A 182 ? 0.4587 0.4639 0.4814 -0.1389 0.0309 0.0409 181 PRO A CD 1452 N N . ASN A 183 ? 0.5672 0.6140 0.5653 -0.2130 0.0675 0.0527 182 ASN A N 1453 C CA . ASN A 183 ? 0.5874 0.6739 0.5996 -0.2376 0.0805 0.0413 182 ASN A CA 1454 C C . ASN A 183 ? 0.5950 0.6864 0.6255 -0.2532 0.0810 0.0304 182 ASN A C 1455 O O . ASN A 183 ? 0.5806 0.7179 0.6400 -0.2641 0.0875 0.0125 182 ASN A O 1456 C CB . ASN A 183 ? 0.6401 0.7148 0.6195 -0.2615 0.0921 0.0566 182 ASN A CB 1457 C CG . ASN A 183 ? 0.6450 0.7255 0.6078 -0.2505 0.0931 0.0644 182 ASN A CG 1458 O OD1 . ASN A 183 ? 0.6205 0.7299 0.6042 -0.2301 0.0896 0.0530 182 ASN A OD1 1459 N ND2 . ASN A 183 ? 0.6975 0.7486 0.6213 -0.2642 0.0964 0.0842 182 ASN A ND2 1460 N N . ASP A 184 ? 0.6287 0.6739 0.6435 -0.2549 0.0741 0.0400 183 ASP A N 1461 C CA . ASP A 184 ? 0.6539 0.6989 0.6822 -0.2721 0.0742 0.0306 183 ASP A CA 1462 C C . ASP A 184 ? 0.6627 0.6566 0.6774 -0.2630 0.0627 0.0377 183 ASP A C 1463 O O . ASP A 184 ? 0.6681 0.6258 0.6623 -0.2449 0.0560 0.0505 183 ASP A O 1464 C CB . ASP A 184 ? 0.7048 0.7527 0.7207 -0.3078 0.0889 0.0349 183 ASP A CB 1465 C CG . ASP A 184 ? 0.7585 0.7577 0.7293 -0.3168 0.0917 0.0598 183 ASP A CG 1466 O OD1 . ASP A 184 ? 0.7995 0.7447 0.7487 -0.3158 0.0839 0.0724 183 ASP A OD1 1467 O OD2 . ASP A 184 ? 0.7819 0.7962 0.7383 -0.3244 0.1009 0.0663 183 ASP A OD2 1468 N N . ALA A 185 ? 0.6659 0.6600 0.6943 -0.2754 0.0605 0.0270 184 ALA A N 1469 C CA . ALA A 185 ? 0.6849 0.6325 0.7013 -0.2707 0.0509 0.0302 184 ALA A CA 1470 C C . ALA A 185 ? 0.7252 0.6146 0.7042 -0.2774 0.0522 0.0510 184 ALA A C 1471 O O . ALA A 185 ? 0.7418 0.5910 0.7071 -0.2593 0.0432 0.0573 184 ALA A O 1472 C CB . ALA A 185 ? 0.6885 0.6485 0.7239 -0.2897 0.0501 0.0153 184 ALA A CB 1473 N N . ALA A 186 ? 0.7462 0.6309 0.7087 -0.3032 0.0628 0.0610 185 ALA A N 1474 C CA . ALA A 186 ? 0.7967 0.6213 0.7214 -0.3124 0.0620 0.0819 185 ALA A CA 1475 C C . ALA A 186 ? 0.7868 0.5871 0.6930 -0.2857 0.0546 0.0963 185 ALA A C 1476 O O . ALA A 186 ? 0.8078 0.5561 0.6948 -0.2749 0.0456 0.1068 185 ALA A O 1477 C CB . ALA A 186 ? 0.8297 0.6564 0.7365 -0.3475 0.0752 0.0910 185 ALA A CB 1478 N N . GLU A 187 ? 0.7505 0.5901 0.6649 -0.2750 0.0581 0.0949 186 GLU A N 1479 C CA . GLU A 187 ? 0.7440 0.5690 0.6444 -0.2505 0.0513 0.1066 186 GLU A CA 1480 C C . GLU A 187 ? 0.7106 0.5258 0.6251 -0.2203 0.0400 0.0988 186 GLU A C 1481 O O . GLU A 187 ? 0.7140 0.4948 0.6140 -0.2022 0.0317 0.1089 186 GLU A O 1482 C CB . GLU A 187 ? 0.7208 0.5938 0.6285 -0.2485 0.0586 0.1040 186 GLU A CB 1483 C CG . GLU A 187 ? 0.7124 0.5796 0.6115 -0.2221 0.0511 0.1123 186 GLU A CG 1484 C CD . GLU A 187 ? 0.6947 0.6088 0.6004 -0.2219 0.0586 0.1081 186 GLU A CD 1485 O OE1 . GLU A 187 ? 0.7343 0.6558 0.6219 -0.2444 0.0683 0.1154 186 GLU A OE1 1486 O OE2 . GLU A 187 ? 0.6457 0.5879 0.5729 -0.2004 0.0551 0.0972 186 GLU A OE2 1487 N N . GLN A 188 ? 0.6759 0.5220 0.6184 -0.2158 0.0393 0.0804 187 GLN A N 1488 C CA . GLN A 188 ? 0.6479 0.4864 0.6013 -0.1917 0.0300 0.0716 187 GLN A CA 1489 C C . GLN A 188 ? 0.6841 0.4674 0.6202 -0.1885 0.0237 0.0777 187 GLN A C 1490 O O . GLN A 188 ? 0.6801 0.4423 0.6105 -0.1667 0.0174 0.0811 187 GLN A O 1491 C CB . GLN A 188 ? 0.6167 0.4898 0.5971 -0.1941 0.0290 0.0525 187 GLN A CB 1492 C CG . GLN A 188 ? 0.6000 0.4625 0.5869 -0.1751 0.0197 0.0430 187 GLN A CG 1493 C CD . GLN A 188 ? 0.5662 0.4404 0.5562 -0.1501 0.0160 0.0433 187 GLN A CD 1494 O OE1 . GLN A 188 ? 0.5537 0.4540 0.5480 -0.1462 0.0194 0.0466 187 GLN A OE1 1495 N NE2 . GLN A 188 ? 0.5555 0.4110 0.5428 -0.1344 0.0099 0.0388 187 GLN A NE2 1496 N N . THR A 189 ? 0.7158 0.4767 0.6451 -0.2104 0.0257 0.0776 188 THR A N 1497 C CA . THR A 189 ? 0.7563 0.4625 0.6706 -0.2085 0.0195 0.0809 188 THR A CA 1498 C C . THR A 189 ? 0.7975 0.4588 0.6848 -0.2050 0.0160 0.1008 188 THR A C 1499 O O . THR A 189 ? 0.8163 0.4377 0.6958 -0.1885 0.0080 0.1029 188 THR A O 1500 C CB . THR A 189 ? 0.7876 0.4808 0.7023 -0.2346 0.0219 0.0741 188 THR A CB 1501 O OG1 . THR A 189 ? 0.7978 0.5059 0.7074 -0.2625 0.0311 0.0808 188 THR A OG1 1502 C CG2 . THR A 189 ? 0.7616 0.4879 0.7011 -0.2325 0.0201 0.0534 188 THR A CG2 1503 N N . ARG A 190 ? 0.8111 0.4791 0.6842 -0.2203 0.0215 0.1145 189 ARG A N 1504 C CA . ARG A 190 ? 0.8509 0.4779 0.6955 -0.2167 0.0160 0.1352 189 ARG A CA 1505 C C . ARG A 190 ? 0.8191 0.4479 0.6681 -0.1836 0.0076 0.1370 189 ARG A C 1506 O O . ARG A 190 ? 0.8501 0.4353 0.6839 -0.1702 -0.0024 0.1478 189 ARG A O 1507 C CB . ARG A 190 ? 0.8777 0.5190 0.7044 -0.2408 0.0245 0.1484 189 ARG A CB 1508 C CG . ARG A 190 ? 0.9409 0.5323 0.7310 -0.2430 0.0172 0.1724 189 ARG A CG 1509 C CD . ARG A 190 ? 0.9809 0.5807 0.7467 -0.2747 0.0274 0.1854 189 ARG A CD 1510 N NE . ARG A 190 ? 0.9459 0.6120 0.7294 -0.2776 0.0390 0.1755 189 ARG A NE 1511 C CZ . ARG A 190 ? 0.9295 0.6194 0.7131 -0.2594 0.0368 0.1786 189 ARG A CZ 1512 N NH1 . ARG A 190 ? 0.9409 0.5973 0.7093 -0.2364 0.0229 0.1915 189 ARG A NH1 1513 N NH2 . ARG A 190 ? 0.8993 0.6484 0.7006 -0.2637 0.0479 0.1671 189 ARG A NH2 1514 N N . LEU A 191 ? 0.7544 0.4331 0.6253 -0.1704 0.0110 0.1259 190 LEU A N 1515 C CA . LEU A 191 ? 0.7199 0.4053 0.5967 -0.1416 0.0045 0.1263 190 LEU A CA 1516 C C . LEU A 191 ? 0.6998 0.3760 0.5923 -0.1208 -0.0006 0.1123 190 LEU A C 1517 O O . LEU A 191 ? 0.7061 0.3615 0.5970 -0.0997 -0.0081 0.1148 190 LEU A O 1518 C CB . LEU A 191 ? 0.6772 0.4170 0.5679 -0.1377 0.0102 0.1212 190 LEU A CB 1519 C CG . LEU A 191 ? 0.6848 0.4436 0.5616 -0.1542 0.0165 0.1321 190 LEU A CG 1520 C CD1 . LEU A 191 ? 0.6396 0.4419 0.5297 -0.1394 0.0180 0.1269 190 LEU A CD1 1521 C CD2 . LEU A 191 ? 0.7389 0.4534 0.5834 -0.1594 0.0105 0.1534 190 LEU A CD2 1522 N N . TYR A 192 ? 0.6758 0.3691 0.5836 -0.1269 0.0033 0.0966 191 TYR A N 1523 C CA . TYR A 192 ? 0.6523 0.3468 0.5738 -0.1089 0.0004 0.0816 191 TYR A CA 1524 C C . TYR A 192 ? 0.6726 0.3401 0.5934 -0.1169 -0.0006 0.0712 191 TYR A C 1525 O O . TYR A 192 ? 0.6619 0.3232 0.5891 -0.1030 -0.0028 0.0590 191 TYR A O 1526 C CB . TYR A 192 ? 0.6019 0.3461 0.5417 -0.1037 0.0037 0.0706 191 TYR A CB 1527 C CG . TYR A 192 ? 0.5795 0.3534 0.5211 -0.0985 0.0056 0.0785 191 TYR A CG 1528 C CD1 . TYR A 192 ? 0.5776 0.3454 0.5156 -0.0795 0.0016 0.0850 191 TYR A CD1 1529 C CD2 . TYR A 192 ? 0.5662 0.3760 0.5145 -0.1126 0.0113 0.0776 191 TYR A CD2 1530 C CE1 . TYR A 192 ? 0.5564 0.3513 0.4952 -0.0754 0.0028 0.0912 191 TYR A CE1 1531 C CE2 . TYR A 192 ? 0.5439 0.3809 0.4934 -0.1079 0.0135 0.0828 191 TYR A CE2 1532 C CZ . TYR A 192 ? 0.5401 0.3684 0.4834 -0.0898 0.0091 0.0901 191 TYR A CZ 1533 O OH . TYR A 192 ? 0.5163 0.3704 0.4593 -0.0858 0.0106 0.0947 191 TYR A OH 1534 N N . GLN A 193 ? 0.7082 0.3602 0.6206 -0.1406 0.0015 0.0750 192 GLN A N 1535 C CA . GLN A 193 ? 0.7366 0.3610 0.6470 -0.1515 0.0002 0.0653 192 GLN A CA 1536 C C . GLN A 193 ? 0.7078 0.3667 0.6349 -0.1568 0.0021 0.0476 192 GLN A C 1537 O O . GLN A 193 ? 0.7282 0.3878 0.6573 -0.1777 0.0036 0.0420 192 GLN A O 1538 C CB . GLN A 193 ? 0.7607 0.3414 0.6650 -0.1334 -0.0059 0.0617 192 GLN A CB 1539 C CG . GLN A 193 ? 0.8064 0.3450 0.7020 -0.1474 -0.0079 0.0563 192 GLN A CG 1540 C CD . GLN A 193 ? 0.8546 0.3585 0.7314 -0.1673 -0.0087 0.0735 192 GLN A CD 1541 O OE1 . GLN A 193 ? 0.8820 0.3586 0.7456 -0.1586 -0.0137 0.0889 192 GLN A OE1 1542 N NE2 . GLN A 193 ? 0.8717 0.3768 0.7463 -0.1951 -0.0044 0.0712 192 GLN A NE2 1543 N N . ASN A 194 ? 0.6690 0.3552 0.6072 -0.1387 0.0009 0.0391 193 ASN A N 1544 C CA . ASN A 194 ? 0.6470 0.3623 0.5976 -0.1415 -0.0001 0.0239 193 ASN A CA 1545 C C . ASN A 194 ? 0.6202 0.3810 0.5852 -0.1530 0.0021 0.0240 193 ASN A C 1546 O O . ASN A 194 ? 0.5877 0.3725 0.5573 -0.1453 0.0044 0.0307 193 ASN A O 1547 C CB . ASN A 194 ? 0.6271 0.3509 0.5803 -0.1196 -0.0023 0.0161 193 ASN A CB 1548 C CG . ASN A 194 ? 0.6563 0.3416 0.5996 -0.1060 -0.0031 0.0139 193 ASN A CG 1549 O OD1 . ASN A 194 ? 0.6993 0.3493 0.6346 -0.1135 -0.0042 0.0115 193 ASN A OD1 1550 N ND2 . ASN A 194 ? 0.6384 0.3312 0.5842 -0.0860 -0.0025 0.0135 193 ASN A ND2 1551 N N . PRO A 195 ? 0.6319 0.4060 0.6057 -0.1712 0.0013 0.0148 194 PRO A N 1552 C CA . PRO A 195 ? 0.6193 0.4386 0.6111 -0.1821 0.0037 0.0124 194 PRO A CA 1553 C C . PRO A 195 ? 0.5846 0.4421 0.5924 -0.1675 -0.0015 0.0036 194 PRO A C 1554 O O . PRO A 195 ? 0.5608 0.4558 0.5844 -0.1696 0.0005 0.0026 194 PRO A O 1555 C CB . PRO A 195 ? 0.6398 0.4594 0.6379 -0.2061 0.0034 0.0036 194 PRO A CB 1556 C CG . PRO A 195 ? 0.6593 0.4432 0.6458 -0.2025 -0.0024 -0.0035 194 PRO A CG 1557 C CD . PRO A 195 ? 0.6647 0.4133 0.6336 -0.1836 -0.0016 0.0054 194 PRO A CD 1558 N N . THR A 196 ? 0.5844 0.4306 0.5867 -0.1536 -0.0080 -0.0030 195 THR A N 1559 C CA . THR A 196 ? 0.5555 0.4293 0.5676 -0.1412 -0.0152 -0.0107 195 THR A CA 1560 C C . THR A 196 ? 0.5443 0.4041 0.5439 -0.1211 -0.0150 -0.0068 195 THR A C 1561 O O . THR A 196 ? 0.5608 0.3939 0.5466 -0.1163 -0.0161 -0.0106 195 THR A O 1562 C CB . THR A 196 ? 0.5663 0.4414 0.5807 -0.1479 -0.0247 -0.0241 195 THR A CB 1563 O OG1 . THR A 196 ? 0.5862 0.4676 0.6109 -0.1688 -0.0238 -0.0285 195 THR A OG1 1564 C CG2 . THR A 196 ? 0.5438 0.4500 0.5701 -0.1385 -0.0348 -0.0310 195 THR A CG2 1565 N N . THR A 197 ? 0.5098 0.3895 0.5152 -0.1102 -0.0129 -0.0008 196 THR A N 1566 C CA . THR A 197 ? 0.4987 0.3664 0.4941 -0.0933 -0.0108 0.0038 196 THR A CA 1567 C C . THR A 197 ? 0.4685 0.3597 0.4695 -0.0820 -0.0153 0.0006 196 THR A C 1568 O O . THR A 197 ? 0.4593 0.3764 0.4735 -0.0852 -0.0208 -0.0041 196 THR A O 1569 C CB . THR A 197 ? 0.5069 0.3669 0.4990 -0.0902 -0.0040 0.0164 196 THR A CB 1570 O OG1 . THR A 197 ? 0.4936 0.3821 0.4969 -0.0970 -0.0015 0.0205 196 THR A OG1 1571 C CG2 . THR A 197 ? 0.5437 0.3685 0.5246 -0.0989 -0.0015 0.0208 196 THR A CG2 1572 N N . TYR A 198 ? 0.4526 0.3335 0.4442 -0.0688 -0.0134 0.0022 197 TYR A N 1573 C CA . TYR A 198 ? 0.4306 0.3264 0.4225 -0.0588 -0.0169 0.0000 197 TYR A CA 1574 C C . TYR A 198 ? 0.4162 0.3056 0.4028 -0.0464 -0.0107 0.0049 197 TYR A C 1575 O O . TYR A 198 ? 0.4246 0.2935 0.4054 -0.0438 -0.0058 0.0067 197 TYR A O 1576 C CB . TYR A 198 ? 0.4403 0.3269 0.4207 -0.0608 -0.0237 -0.0089 197 TYR A CB 1577 C CG . TYR A 198 ? 0.4681 0.3274 0.4322 -0.0592 -0.0186 -0.0129 197 TYR A CG 1578 C CD1 . TYR A 198 ? 0.5070 0.3457 0.4663 -0.0676 -0.0173 -0.0169 197 TYR A CD1 1579 C CD2 . TYR A 198 ? 0.4718 0.3268 0.4269 -0.0498 -0.0140 -0.0140 197 TYR A CD2 1580 C CE1 . TYR A 198 ? 0.5281 0.3422 0.4748 -0.0649 -0.0122 -0.0229 197 TYR A CE1 1581 C CE2 . TYR A 198 ? 0.4938 0.3278 0.4373 -0.0479 -0.0079 -0.0206 197 TYR A CE2 1582 C CZ . TYR A 198 ? 0.5263 0.3395 0.4660 -0.0546 -0.0072 -0.0254 197 TYR A CZ 1583 O OH . TYR A 198 ? 0.5537 0.3461 0.4838 -0.0517 -0.0011 -0.0344 197 TYR A OH 1584 N N . ILE A 199 ? 0.3906 0.2972 0.3807 -0.0386 -0.0119 0.0059 198 ILE A N 1585 C CA . ILE A 199 ? 0.3923 0.2966 0.3784 -0.0277 -0.0070 0.0076 198 ILE A CA 1586 C C . ILE A 199 ? 0.3873 0.2961 0.3661 -0.0256 -0.0105 0.0025 198 ILE A C 1587 O O . ILE A 199 ? 0.3784 0.3026 0.3624 -0.0258 -0.0167 0.0029 198 ILE A O 1588 C CB . ILE A 199 ? 0.3788 0.2999 0.3747 -0.0213 -0.0044 0.0154 198 ILE A CB 1589 C CG1 . ILE A 199 ? 0.3898 0.3024 0.3873 -0.0238 -0.0013 0.0229 198 ILE A CG1 1590 C CG2 . ILE A 199 ? 0.3716 0.2948 0.3659 -0.0107 -0.0009 0.0151 198 ILE A CG2 1591 C CD1 . ILE A 199 ? 0.3810 0.3147 0.3863 -0.0249 -0.0007 0.0296 198 ILE A CD1 1592 N N . SER A 200 ? 0.4049 0.2995 0.3712 -0.0242 -0.0065 -0.0027 199 SER A N 1593 C CA . SER A 200 ? 0.4062 0.3011 0.3600 -0.0249 -0.0080 -0.0067 199 SER A CA 1594 C C . SER A 200 ? 0.3838 0.2868 0.3415 -0.0168 -0.0004 -0.0056 199 SER A C 1595 O O . SER A 200 ? 0.3743 0.2739 0.3380 -0.0109 0.0065 -0.0066 199 SER A O 1596 C CB . SER A 200 ? 0.4433 0.3193 0.3780 -0.0313 -0.0064 -0.0151 199 SER A CB 1597 O OG . SER A 200 ? 0.4861 0.3573 0.4133 -0.0397 -0.0168 -0.0167 199 SER A OG 1598 N N . VAL A 201 ? 0.3622 0.2749 0.3171 -0.0165 -0.0032 -0.0042 200 VAL A N 1599 C CA . VAL A 201 ? 0.3573 0.2795 0.3153 -0.0113 0.0035 -0.0046 200 VAL A CA 1600 C C . VAL A 201 ? 0.3605 0.2790 0.3015 -0.0177 0.0020 -0.0070 200 VAL A C 1601 O O . VAL A 201 ? 0.3578 0.2752 0.2936 -0.0209 -0.0081 -0.0036 200 VAL A O 1602 C CB . VAL A 201 ? 0.3402 0.2809 0.3154 -0.0043 0.0018 0.0018 200 VAL A CB 1603 C CG1 . VAL A 201 ? 0.3355 0.2865 0.3170 0.0018 0.0094 0.0003 200 VAL A CG1 1604 C CG2 . VAL A 201 ? 0.3394 0.2815 0.3258 -0.0020 0.0008 0.0066 200 VAL A CG2 1605 N N . GLY A 202 ? 0.3618 0.2783 0.2945 -0.0197 0.0120 -0.0133 201 GLY A N 1606 C CA . GLY A 202 ? 0.3741 0.2850 0.2863 -0.0291 0.0131 -0.0154 201 GLY A CA 1607 C C . GLY A 202 ? 0.3724 0.2967 0.2899 -0.0284 0.0246 -0.0198 201 GLY A C 1608 O O . GLY A 202 ? 0.3612 0.2952 0.2934 -0.0217 0.0342 -0.0261 201 GLY A O 1609 N N . THR A 203 ? 0.3688 0.2931 0.2754 -0.0352 0.0223 -0.0168 202 THR A N 1610 C CA . THR A 203 ? 0.3775 0.3117 0.2820 -0.0406 0.0335 -0.0223 202 THR A CA 1611 C C . THR A 203 ? 0.4091 0.3244 0.2791 -0.0579 0.0329 -0.0218 202 THR A C 1612 O O . THR A 203 ? 0.4330 0.3281 0.2804 -0.0645 0.0261 -0.0202 202 THR A O 1613 C CB . THR A 203 ? 0.3560 0.3086 0.2810 -0.0337 0.0318 -0.0184 202 THR A CB 1614 O OG1 . THR A 203 ? 0.3553 0.2977 0.2693 -0.0381 0.0201 -0.0106 202 THR A OG1 1615 C CG2 . THR A 203 ? 0.3296 0.2958 0.2813 -0.0185 0.0291 -0.0158 202 THR A CG2 1616 N N . SER A 204 ? 0.4164 0.3369 0.2802 -0.0665 0.0392 -0.0231 203 SER A N 1617 C CA . SER A 204 ? 0.4545 0.3523 0.2816 -0.0845 0.0361 -0.0194 203 SER A CA 1618 C C . SER A 204 ? 0.4571 0.3359 0.2755 -0.0823 0.0156 -0.0072 203 SER A C 1619 O O . SER A 204 ? 0.4853 0.3377 0.2718 -0.0931 0.0059 -0.0020 203 SER A O 1620 C CB . SER A 204 ? 0.4612 0.3690 0.2839 -0.0965 0.0490 -0.0240 203 SER A CB 1621 O OG . SER A 204 ? 0.4410 0.3643 0.2889 -0.0874 0.0452 -0.0207 203 SER A OG 1622 N N . THR A 205 ? 0.4427 0.3354 0.2897 -0.0681 0.0085 -0.0037 204 THR A N 1623 C CA . THR A 205 ? 0.4506 0.3312 0.2979 -0.0630 -0.0102 0.0044 204 THR A CA 1624 C C . THR A 205 ? 0.4391 0.3265 0.3067 -0.0493 -0.0199 0.0057 204 THR A C 1625 O O . THR A 205 ? 0.4593 0.3337 0.3221 -0.0472 -0.0361 0.0098 204 THR A O 1626 C CB . THR A 205 ? 0.4339 0.3260 0.2973 -0.0593 -0.0108 0.0056 204 THR A CB 1627 O OG1 . THR A 205 ? 0.3999 0.3221 0.2942 -0.0487 -0.0002 0.0007 204 THR A OG1 1628 C CG2 . THR A 205 ? 0.4562 0.3365 0.2966 -0.0757 -0.0047 0.0058 204 THR A CG2 1629 N N . LEU A 206 ? 0.4213 0.3287 0.3117 -0.0406 -0.0107 0.0017 205 LEU A N 1630 C CA . LEU A 206 ? 0.3990 0.3143 0.3086 -0.0304 -0.0176 0.0031 205 LEU A CA 1631 C C . LEU A 206 ? 0.4133 0.3149 0.3100 -0.0344 -0.0209 0.0017 205 LEU A C 1632 O O . LEU A 206 ? 0.4371 0.3313 0.3189 -0.0413 -0.0116 -0.0026 205 LEU A O 1633 C CB . LEU A 206 ? 0.3794 0.3173 0.3145 -0.0209 -0.0076 0.0011 205 LEU A CB 1634 C CG . LEU A 206 ? 0.3667 0.3150 0.3213 -0.0124 -0.0120 0.0033 205 LEU A CG 1635 C CD1 . LEU A 206 ? 0.3661 0.3217 0.3312 -0.0084 -0.0228 0.0057 205 LEU A CD1 1636 C CD2 . LEU A 206 ? 0.3502 0.3142 0.3218 -0.0052 -0.0023 0.0029 205 LEU A CD2 1637 N N . ASN A 207 ? 0.4083 0.3089 0.3127 -0.0305 -0.0335 0.0036 206 ASN A N 1638 C CA . ASN A 207 ? 0.4171 0.3064 0.3118 -0.0345 -0.0388 0.0018 206 ASN A CA 1639 C C . ASN A 207 ? 0.4068 0.3094 0.3259 -0.0275 -0.0466 0.0019 206 ASN A C 1640 O O . ASN A 207 ? 0.4079 0.3099 0.3307 -0.0258 -0.0615 0.0026 206 ASN A O 1641 C CB . ASN A 207 ? 0.4478 0.3136 0.3127 -0.0435 -0.0514 0.0038 206 ASN A CB 1642 C CG . ASN A 207 ? 0.4683 0.3225 0.3215 -0.0483 -0.0597 0.0015 206 ASN A CG 1643 O OD1 . ASN A 207 ? 0.4540 0.3114 0.3112 -0.0494 -0.0509 -0.0032 206 ASN A OD1 1644 N ND2 . ASN A 207 ? 0.5072 0.3465 0.3456 -0.0510 -0.0784 0.0046 206 ASN A ND2 1645 N N . GLN A 208 ? 0.3988 0.3135 0.3345 -0.0238 -0.0366 0.0007 207 GLN A N 1646 C CA . GLN A 208 ? 0.3900 0.3207 0.3490 -0.0193 -0.0399 0.0012 207 GLN A CA 1647 C C . GLN A 208 ? 0.4105 0.3364 0.3709 -0.0236 -0.0374 -0.0009 207 GLN A C 1648 O O . GLN A 208 ? 0.4076 0.3240 0.3605 -0.0250 -0.0277 -0.0022 207 GLN A O 1649 C CB . GLN A 208 ? 0.3726 0.3210 0.3485 -0.0124 -0.0311 0.0038 207 GLN A CB 1650 C CG . GLN A 208 ? 0.3735 0.3367 0.3682 -0.0107 -0.0290 0.0050 207 GLN A CG 1651 C CD . GLN A 208 ? 0.3641 0.3429 0.3702 -0.0049 -0.0216 0.0084 207 GLN A CD 1652 O OE1 . GLN A 208 ? 0.3666 0.3447 0.3746 -0.0039 -0.0142 0.0116 207 GLN A OE1 1653 N NE2 . GLN A 208 ? 0.3585 0.3495 0.3712 -0.0008 -0.0249 0.0077 207 GLN A NE2 1654 N N . ARG A 209 ? 0.4312 0.3642 0.4028 -0.0256 -0.0465 -0.0028 208 ARG A N 1655 C CA . ARG A 209 ? 0.4567 0.3884 0.4339 -0.0311 -0.0438 -0.0048 208 ARG A CA 1656 C C . ARG A 209 ? 0.4571 0.4112 0.4587 -0.0309 -0.0450 -0.0048 208 ARG A C 1657 O O . ARG A 209 ? 0.4809 0.4485 0.4946 -0.0304 -0.0556 -0.0086 208 ARG A O 1658 C CB . ARG A 209 ? 0.4880 0.4050 0.4511 -0.0387 -0.0529 -0.0097 208 ARG A CB 1659 C CG . ARG A 209 ? 0.5034 0.4090 0.4632 -0.0454 -0.0460 -0.0124 208 ARG A CG 1660 C CD . ARG A 209 ? 0.5290 0.4199 0.4725 -0.0538 -0.0552 -0.0185 208 ARG A CD 1661 N NE . ARG A 209 ? 0.5459 0.4250 0.4876 -0.0609 -0.0493 -0.0226 208 ARG A NE 1662 C CZ . ARG A 209 ? 0.5588 0.4176 0.4833 -0.0630 -0.0410 -0.0264 208 ARG A CZ 1663 N NH1 . ARG A 209 ? 0.5672 0.4175 0.4742 -0.0599 -0.0358 -0.0274 208 ARG A NH1 1664 N NH2 . ARG A 209 ? 0.5674 0.4142 0.4926 -0.0691 -0.0373 -0.0307 208 ARG A NH2 1665 N N . LEU A 210 ? 0.4556 0.4137 0.4641 -0.0316 -0.0343 -0.0010 209 LEU A N 1666 C CA . LEU A 210 ? 0.4311 0.4107 0.4587 -0.0340 -0.0322 -0.0004 209 LEU A CA 1667 C C . LEU A 210 ? 0.4350 0.4088 0.4643 -0.0450 -0.0298 -0.0014 209 LEU A C 1668 O O . LEU A 210 ? 0.4392 0.3902 0.4552 -0.0478 -0.0256 0.0004 209 LEU A O 1669 C CB . LEU A 210 ? 0.4235 0.4102 0.4534 -0.0288 -0.0228 0.0062 209 LEU A CB 1670 C CG . LEU A 210 ? 0.4193 0.4088 0.4458 -0.0190 -0.0231 0.0074 209 LEU A CG 1671 C CD1 . LEU A 210 ? 0.4224 0.4153 0.4487 -0.0148 -0.0143 0.0140 209 LEU A CD1 1672 C CD2 . LEU A 210 ? 0.4134 0.4218 0.4523 -0.0154 -0.0309 0.0025 209 LEU A CD2 1673 N N . VAL A 211 ? 0.4245 0.4197 0.4717 -0.0516 -0.0325 -0.0059 210 VAL A N 1674 C CA . VAL A 211 ? 0.4321 0.4265 0.4837 -0.0650 -0.0289 -0.0071 210 VAL A CA 1675 C C . VAL A 211 ? 0.4175 0.4354 0.4829 -0.0703 -0.0205 -0.0047 210 VAL A C 1676 O O . VAL A 211 ? 0.4008 0.4464 0.4827 -0.0662 -0.0225 -0.0098 210 VAL A O 1677 C CB . VAL A 211 ? 0.4371 0.4389 0.4981 -0.0714 -0.0401 -0.0173 210 VAL A CB 1678 C CG1 . VAL A 211 ? 0.4581 0.4639 0.5272 -0.0877 -0.0358 -0.0199 210 VAL A CG1 1679 C CG2 . VAL A 211 ? 0.4520 0.4279 0.4931 -0.0686 -0.0477 -0.0188 210 VAL A CG2 1680 N N . PRO A 212 ? 0.4297 0.4349 0.4864 -0.0795 -0.0111 0.0029 211 PRO A N 1681 C CA . PRO A 212 ? 0.4236 0.4490 0.4872 -0.0868 -0.0024 0.0064 211 PRO A CA 1682 C C . PRO A 212 ? 0.4136 0.4718 0.5001 -0.0983 -0.0025 -0.0045 211 PRO A C 1683 O O . PRO A 212 ? 0.4262 0.4835 0.5196 -0.1065 -0.0074 -0.0117 211 PRO A O 1684 C CB . PRO A 212 ? 0.4471 0.4441 0.4925 -0.0968 0.0046 0.0176 211 PRO A CB 1685 C CG . PRO A 212 ? 0.4610 0.4244 0.4917 -0.0876 0.0004 0.0200 211 PRO A CG 1686 C CD . PRO A 212 ? 0.4522 0.4222 0.4907 -0.0836 -0.0085 0.0087 211 PRO A CD 1687 N N . LYS A 213 ? 0.3946 0.4833 0.4937 -0.0989 0.0029 -0.0075 212 LYS A N 1688 C CA . LYS A 213 ? 0.3851 0.5106 0.5084 -0.1114 0.0065 -0.0195 212 LYS A CA 1689 C C . LYS A 213 ? 0.4095 0.5338 0.5225 -0.1322 0.0205 -0.0122 212 LYS A C 1690 O O . LYS A 213 ? 0.4137 0.5376 0.5131 -0.1336 0.0290 -0.0032 212 LYS A O 1691 C CB . LYS A 213 ? 0.3577 0.5181 0.5011 -0.1006 0.0054 -0.0294 212 LYS A CB 1692 C CG . LYS A 213 ? 0.3485 0.5085 0.5026 -0.0826 -0.0102 -0.0371 212 LYS A CG 1693 C CD . LYS A 213 ? 0.3375 0.5260 0.5104 -0.0703 -0.0127 -0.0468 212 LYS A CD 1694 C CE . LYS A 213 ? 0.3429 0.5128 0.4971 -0.0570 -0.0128 -0.0371 212 LYS A CE 1695 N NZ . LYS A 213 ? 0.3363 0.5269 0.5079 -0.0433 -0.0189 -0.0476 212 LYS A NZ 1696 N N . ILE A 214 ? 0.4266 0.5481 0.5434 -0.1494 0.0220 -0.0155 213 ILE A N 1697 C CA . ILE A 214 ? 0.4627 0.5792 0.5674 -0.1729 0.0348 -0.0083 213 ILE A CA 1698 C C . ILE A 214 ? 0.4657 0.6314 0.5978 -0.1886 0.0431 -0.0235 213 ILE A C 1699 O O . ILE A 214 ? 0.4711 0.6561 0.6267 -0.1960 0.0390 -0.0373 213 ILE A O 1700 C CB . ILE A 214 ? 0.4941 0.5750 0.5855 -0.1853 0.0326 -0.0033 213 ILE A CB 1701 C CG1 . ILE A 214 ? 0.5038 0.5408 0.5743 -0.1680 0.0238 0.0062 213 ILE A CG1 1702 C CG2 . ILE A 214 ? 0.5303 0.5957 0.6023 -0.2097 0.0449 0.0077 213 ILE A CG2 1703 C CD1 . ILE A 214 ? 0.5311 0.5349 0.5919 -0.1771 0.0198 0.0067 213 ILE A CD1 1704 N N . ALA A 215 ? 0.4748 0.6628 0.6046 -0.1941 0.0547 -0.0223 214 ALA A N 1705 C CA . ALA A 215 ? 0.4809 0.7219 0.6393 -0.2078 0.0647 -0.0399 214 ALA A CA 1706 C C . ALA A 215 ? 0.5060 0.7591 0.6468 -0.2248 0.0822 -0.0335 214 ALA A C 1707 O O . ALA A 215 ? 0.5263 0.7490 0.6343 -0.2212 0.0840 -0.0153 214 ALA A O 1708 C CB . ALA A 215 ? 0.4456 0.7229 0.6384 -0.1862 0.0551 -0.0584 214 ALA A CB 1709 N N . THR A 216 ? 0.5080 0.8075 0.6715 -0.2436 0.0948 -0.0496 215 THR A N 1710 C CA . THR A 216 ? 0.5239 0.8409 0.6710 -0.2642 0.1134 -0.0465 215 THR A CA 1711 C C . THR A 216 ? 0.4972 0.8451 0.6548 -0.2471 0.1153 -0.0561 215 THR A C 1712 O O . THR A 216 ? 0.4717 0.8625 0.6695 -0.2354 0.1122 -0.0791 215 THR A O 1713 C CB . THR A 216 ? 0.5396 0.8978 0.7086 -0.2944 0.1284 -0.0627 215 THR A CB 1714 O OG1 . THR A 216 ? 0.5577 0.8861 0.7183 -0.3104 0.1254 -0.0550 215 THR A OG1 1715 C CG2 . THR A 216 ? 0.5715 0.9452 0.7171 -0.3208 0.1497 -0.0585 215 THR A CG2 1716 N N . ARG A 217 ? 0.5021 0.8271 0.6239 -0.2452 0.1190 -0.0390 216 ARG A N 1717 C CA . ARG A 217 ? 0.4808 0.8304 0.6072 -0.2301 0.1208 -0.0467 216 ARG A CA 1718 C C . ARG A 217 ? 0.5040 0.8614 0.5995 -0.2518 0.1380 -0.0392 216 ARG A C 1719 O O . ARG A 217 ? 0.5392 0.8717 0.6022 -0.2760 0.1459 -0.0226 216 ARG A O 1720 C CB . ARG A 217 ? 0.4654 0.7794 0.5786 -0.2009 0.1044 -0.0341 216 ARG A CB 1721 C CG . ARG A 217 ? 0.4365 0.7501 0.5800 -0.1767 0.0876 -0.0448 216 ARG A CG 1722 C CD . ARG A 217 ? 0.4248 0.6930 0.5479 -0.1556 0.0734 -0.0282 216 ARG A CD 1723 N NE . ARG A 217 ? 0.4521 0.6758 0.5482 -0.1645 0.0715 -0.0092 216 ARG A NE 1724 C CZ . ARG A 217 ? 0.4456 0.6422 0.5438 -0.1572 0.0605 -0.0062 216 ARG A CZ 1725 N NH1 . ARG A 217 ? 0.4135 0.6199 0.5364 -0.1412 0.0491 -0.0187 216 ARG A NH1 1726 N NH2 . ARG A 217 ? 0.4770 0.6336 0.5499 -0.1664 0.0603 0.0096 216 ARG A NH2 1727 N N . SER A 218 ? 0.4856 0.8755 0.5891 -0.2436 0.1432 -0.0516 217 SER A N 1728 C CA . SER A 218 ? 0.5118 0.9114 0.5838 -0.2628 0.1589 -0.0460 217 SER A CA 1729 C C . SER A 218 ? 0.5243 0.8723 0.5489 -0.2555 0.1500 -0.0174 217 SER A C 1730 O O . SER A 218 ? 0.5020 0.8245 0.5290 -0.2289 0.1336 -0.0106 217 SER A O 1731 C CB . SER A 218 ? 0.4872 0.9398 0.5856 -0.2547 0.1666 -0.0717 217 SER A CB 1732 O OG . SER A 218 ? 0.4706 0.9742 0.6157 -0.2612 0.1746 -0.1000 217 SER A OG 1733 N N . LYS A 219 ? 0.5704 0.9037 0.5520 -0.2799 0.1605 -0.0011 218 LYS A N 1734 C CA . LYS A 219 ? 0.5936 0.8801 0.5296 -0.2738 0.1509 0.0257 218 LYS A CA 1735 C C . LYS A 219 ? 0.5721 0.8756 0.5072 -0.2548 0.1474 0.0197 218 LYS A C 1736 O O . LYS A 219 ? 0.5714 0.9184 0.5141 -0.2630 0.1605 0.0021 218 LYS A O 1737 C CB . LYS A 219 ? 0.6555 0.9185 0.5420 -0.3064 0.1611 0.0459 218 LYS A CB 1738 C CG . LYS A 219 ? 0.6874 0.9057 0.5595 -0.3194 0.1567 0.0632 218 LYS A CG 1739 C CD . LYS A 219 ? 0.7537 0.9450 0.5738 -0.3535 0.1660 0.0842 218 LYS A CD 1740 C CE . LYS A 219 ? 0.7879 0.9186 0.5862 -0.3596 0.1557 0.1065 218 LYS A CE 1741 N NZ . LYS A 219 ? 0.8643 0.9617 0.6081 -0.3939 0.1629 0.1290 218 LYS A NZ 1742 N N . VAL A 220 ? 0.5563 0.8263 0.4841 -0.2297 0.1300 0.0327 219 VAL A N 1743 C CA . VAL A 220 ? 0.5459 0.8210 0.4646 -0.2133 0.1242 0.0327 219 VAL A CA 1744 C C . VAL A 220 ? 0.5773 0.8018 0.4533 -0.2112 0.1123 0.0617 219 VAL A C 1745 O O . VAL A 220 ? 0.5649 0.7522 0.4414 -0.1998 0.1001 0.0742 219 VAL A O 1746 C CB . VAL A 220 ? 0.4938 0.7791 0.4510 -0.1827 0.1126 0.0180 219 VAL A CB 1747 C CG1 . VAL A 220 ? 0.4813 0.7684 0.4279 -0.1668 0.1060 0.0190 219 VAL A CG1 1748 C CG2 . VAL A 220 ? 0.4719 0.8038 0.4731 -0.1826 0.1209 -0.0105 219 VAL A CG2 1749 N N . ASN A 221 ? 0.6147 0.8383 0.4539 -0.2221 0.1154 0.0715 220 ASN A N 1750 C CA . ASN A 221 ? 0.6549 0.8303 0.4499 -0.2227 0.1030 0.1001 220 ASN A CA 1751 C C . ASN A 221 ? 0.6887 0.8241 0.4655 -0.2388 0.1022 0.1177 220 ASN A C 1752 O O . ASN A 221 ? 0.7055 0.7948 0.4685 -0.2270 0.0866 0.1364 220 ASN A O 1753 C CB . ASN A 221 ? 0.6324 0.7868 0.4372 -0.1907 0.0836 0.1057 220 ASN A CB 1754 C CG . ASN A 221 ? 0.6083 0.7963 0.4269 -0.1758 0.0827 0.0904 220 ASN A CG 1755 O OD1 . ASN A 221 ? 0.6126 0.8414 0.4396 -0.1859 0.0963 0.0723 220 ASN A OD1 1756 N ND2 . ASN A 221 ? 0.5934 0.7649 0.4155 -0.1521 0.0670 0.0962 220 ASN A ND2 1757 N N . GLY A 222 ? 0.7027 0.8574 0.4825 -0.2654 0.1191 0.1096 221 GLY A N 1758 C CA . GLY A 222 ? 0.7382 0.8574 0.5008 -0.2854 0.1207 0.1243 221 GLY A CA 1759 C C . GLY A 222 ? 0.7117 0.8111 0.5055 -0.2701 0.1116 0.1215 221 GLY A C 1760 O O . GLY A 222 ? 0.7500 0.8102 0.5266 -0.2827 0.1090 0.1361 221 GLY A O 1761 N N . GLN A 223 ? 0.6496 0.7728 0.4862 -0.2444 0.1065 0.1033 222 GLN A N 1762 C CA . GLN A 223 ? 0.6229 0.7283 0.4864 -0.2308 0.0980 0.0998 222 GLN A CA 1763 C C . GLN A 223 ? 0.5754 0.7257 0.4858 -0.2284 0.1050 0.0732 222 GLN A C 1764 O O . GLN A 223 ? 0.5352 0.7216 0.4709 -0.2136 0.1055 0.0562 222 GLN A O 1765 C CB . GLN A 223 ? 0.6055 0.6840 0.4728 -0.1993 0.0801 0.1068 222 GLN A CB 1766 C CG . GLN A 223 ? 0.6446 0.6812 0.4726 -0.1955 0.0691 0.1308 222 GLN A CG 1767 C CD . GLN A 223 ? 0.6998 0.6880 0.4986 -0.2121 0.0663 0.1503 222 GLN A CD 1768 O OE1 . GLN A 223 ? 0.6949 0.6637 0.5074 -0.2112 0.0639 0.1485 222 GLN A OE1 1769 N NE2 . GLN A 223 ? 0.7535 0.7193 0.5096 -0.2276 0.0655 0.1693 222 GLN A NE2 1770 N N . SER A 224 ? 0.5832 0.7292 0.5051 -0.2426 0.1089 0.0696 223 SER A N 1771 C CA . SER A 224 ? 0.5491 0.7307 0.5164 -0.2375 0.1106 0.0460 223 SER A CA 1772 C C . SER A 224 ? 0.5159 0.6759 0.5013 -0.2098 0.0941 0.0451 223 SER A C 1773 O O . SER A 224 ? 0.4811 0.6676 0.5021 -0.1982 0.0906 0.0267 223 SER A O 1774 C CB . SER A 224 ? 0.5740 0.7630 0.5474 -0.2657 0.1212 0.0411 223 SER A CB 1775 O OG . SER A 224 ? 0.6011 0.8268 0.5696 -0.2915 0.1395 0.0334 223 SER A OG 1776 N N . GLY A 225 ? 0.5213 0.6328 0.4814 -0.1999 0.0835 0.0645 224 GLY A N 1777 C CA . GLY A 225 ? 0.4873 0.5781 0.4594 -0.1741 0.0694 0.0641 224 GLY A CA 1778 C C . GLY A 225 ? 0.4461 0.5594 0.4323 -0.1517 0.0647 0.0557 224 GLY A C 1779 O O . GLY A 225 ? 0.4497 0.5883 0.4322 -0.1548 0.0709 0.0525 224 GLY A O 1780 N N . ARG A 226 ? 0.4164 0.5202 0.4176 -0.1308 0.0540 0.0513 225 ARG A N 1781 C CA . ARG A 226 ? 0.3906 0.5096 0.4030 -0.1105 0.0486 0.0445 225 ARG A CA 1782 C C . ARG A 226 ? 0.3904 0.4782 0.3983 -0.0919 0.0376 0.0514 225 ARG A C 1783 O O . ARG A 226 ? 0.4078 0.4703 0.4140 -0.0923 0.0338 0.0546 225 ARG A O 1784 C CB . ARG A 226 ? 0.3608 0.5168 0.4064 -0.1055 0.0487 0.0234 225 ARG A CB 1785 C CG . ARG A 226 ? 0.3611 0.5579 0.4192 -0.1210 0.0604 0.0107 225 ARG A CG 1786 C CD . ARG A 226 ? 0.3635 0.5769 0.4098 -0.1205 0.0661 0.0114 225 ARG A CD 1787 N NE . ARG A 226 ? 0.3691 0.6255 0.4295 -0.1345 0.0787 -0.0043 225 ARG A NE 1788 C CZ . ARG A 226 ? 0.4010 0.6664 0.4459 -0.1589 0.0919 -0.0008 225 ARG A CZ 1789 N NH1 . ARG A 226 ? 0.4354 0.6650 0.4478 -0.1723 0.0930 0.0200 225 ARG A NH1 1790 N NH2 . ARG A 226 ? 0.3998 0.7101 0.4619 -0.1705 0.1044 -0.0191 225 ARG A NH2 1791 N N . MET A 227 ? 0.3853 0.4769 0.3918 -0.0767 0.0334 0.0522 226 MET A N 1792 C CA . MET A 227 ? 0.3891 0.4601 0.3962 -0.0589 0.0245 0.0547 226 MET A CA 1793 C C . MET A 227 ? 0.3543 0.4480 0.3808 -0.0470 0.0215 0.0412 226 MET A C 1794 O O . MET A 227 ? 0.3421 0.4611 0.3739 -0.0466 0.0243 0.0352 226 MET A O 1795 C CB . MET A 227 ? 0.4190 0.4736 0.4071 -0.0517 0.0211 0.0678 226 MET A CB 1796 C CG . MET A 227 ? 0.4779 0.5043 0.4426 -0.0620 0.0212 0.0835 226 MET A CG 1797 S SD . MET A 227 ? 0.5246 0.5078 0.4846 -0.0528 0.0135 0.0906 226 MET A SD 1798 C CE . MET A 227 ? 0.5704 0.5212 0.5022 -0.0693 0.0138 0.1083 226 MET A CE 1799 N N . GLU A 228 ? 0.3435 0.4261 0.3787 -0.0380 0.0155 0.0365 227 GLU A N 1800 C CA . GLU A 228 ? 0.3282 0.4247 0.3778 -0.0274 0.0108 0.0257 227 GLU A CA 1801 C C . GLU A 228 ? 0.3086 0.3862 0.3510 -0.0155 0.0062 0.0300 227 GLU A C 1802 O O . GLU A 228 ? 0.3238 0.3782 0.3596 -0.0142 0.0045 0.0341 227 GLU A O 1803 C CB . GLU A 228 ? 0.3315 0.4325 0.3960 -0.0297 0.0067 0.0155 227 GLU A CB 1804 C CG . GLU A 228 ? 0.3246 0.4354 0.4024 -0.0194 -0.0006 0.0049 227 GLU A CG 1805 C CD . GLU A 228 ? 0.3300 0.4480 0.4237 -0.0218 -0.0068 -0.0051 227 GLU A CD 1806 O OE1 . GLU A 228 ? 0.3346 0.4464 0.4273 -0.0312 -0.0053 -0.0036 227 GLU A OE1 1807 O OE2 . GLU A 228 ? 0.3396 0.4683 0.4467 -0.0142 -0.0144 -0.0149 227 GLU A OE2 1808 N N . PHE A 229 ? 0.2741 0.3630 0.3184 -0.0076 0.0050 0.0278 228 PHE A N 1809 C CA . PHE A 229 ? 0.2620 0.3381 0.3010 0.0018 0.0023 0.0311 228 PHE A CA 1810 C C . PHE A 229 ? 0.2485 0.3266 0.2952 0.0073 -0.0019 0.0224 228 PHE A C 1811 O O . PHE A 229 ? 0.2362 0.3284 0.2927 0.0069 -0.0042 0.0143 228 PHE A O 1812 C CB . PHE A 229 ? 0.2603 0.3445 0.2929 0.0054 0.0032 0.0368 228 PHE A CB 1813 C CG . PHE A 229 ? 0.2760 0.3498 0.2953 0.0004 0.0049 0.0485 228 PHE A CG 1814 C CD1 . PHE A 229 ? 0.2876 0.3371 0.2998 0.0047 0.0024 0.0561 228 PHE A CD1 1815 C CD2 . PHE A 229 ? 0.2861 0.3725 0.2988 -0.0095 0.0089 0.0512 228 PHE A CD2 1816 C CE1 . PHE A 229 ? 0.3117 0.3457 0.3098 0.0005 0.0016 0.0679 228 PHE A CE1 1817 C CE2 . PHE A 229 ? 0.3065 0.3784 0.3020 -0.0163 0.0095 0.0639 228 PHE A CE2 1818 C CZ . PHE A 229 ? 0.3225 0.3661 0.3104 -0.0107 0.0048 0.0730 228 PHE A CZ 1819 N N . PHE A 230 ? 0.2538 0.3163 0.2953 0.0121 -0.0031 0.0238 229 PHE A N 1820 C CA . PHE A 230 ? 0.2461 0.3041 0.2886 0.0147 -0.0067 0.0177 229 PHE A CA 1821 C C . PHE A 230 ? 0.2430 0.2992 0.2824 0.0198 -0.0045 0.0188 229 PHE A C 1822 O O . PHE A 230 ? 0.2500 0.3039 0.2874 0.0228 -0.0017 0.0238 229 PHE A O 1823 C CB . PHE A 230 ? 0.2536 0.2931 0.2906 0.0113 -0.0090 0.0163 229 PHE A CB 1824 C CG . PHE A 230 ? 0.2561 0.2981 0.2983 0.0058 -0.0118 0.0143 229 PHE A CG 1825 C CD1 . PHE A 230 ? 0.2457 0.2950 0.2961 0.0057 -0.0190 0.0073 229 PHE A CD1 1826 C CD2 . PHE A 230 ? 0.2633 0.2999 0.3033 0.0007 -0.0081 0.0188 229 PHE A CD2 1827 C CE1 . PHE A 230 ? 0.2453 0.3013 0.3046 0.0010 -0.0220 0.0034 229 PHE A CE1 1828 C CE2 . PHE A 230 ? 0.2649 0.3066 0.3114 -0.0063 -0.0098 0.0157 229 PHE A CE2 1829 C CZ . PHE A 230 ? 0.2563 0.3101 0.3141 -0.0059 -0.0166 0.0073 229 PHE A CZ 1830 N N . TRP A 231 ? 0.2429 0.2991 0.2822 0.0204 -0.0066 0.0138 230 TRP A N 1831 C CA . TRP A 231 ? 0.2521 0.3093 0.2902 0.0229 -0.0037 0.0128 230 TRP A CA 1832 C C . TRP A 231 ? 0.2576 0.3015 0.2876 0.0185 -0.0043 0.0087 230 TRP A C 1833 O O . TRP A 231 ? 0.2669 0.3020 0.2925 0.0151 -0.0101 0.0069 230 TRP A O 1834 C CB . TRP A 231 ? 0.2462 0.3222 0.2911 0.0257 -0.0044 0.0112 230 TRP A CB 1835 C CG . TRP A 231 ? 0.2452 0.3253 0.2928 0.0239 -0.0091 0.0057 230 TRP A CG 1836 C CD1 . TRP A 231 ? 0.2431 0.3320 0.2965 0.0239 -0.0118 0.0035 230 TRP A CD1 1837 C CD2 . TRP A 231 ? 0.2449 0.3198 0.2904 0.0218 -0.0118 0.0008 230 TRP A CD2 1838 N NE1 . TRP A 231 ? 0.2453 0.3348 0.3026 0.0243 -0.0172 -0.0035 230 TRP A NE1 1839 C CE2 . TRP A 231 ? 0.2460 0.3244 0.2968 0.0227 -0.0179 -0.0042 230 TRP A CE2 1840 C CE3 . TRP A 231 ? 0.2495 0.3173 0.2893 0.0184 -0.0094 -0.0005 230 TRP A CE3 1841 C CZ2 . TRP A 231 ? 0.2487 0.3187 0.2978 0.0213 -0.0235 -0.0093 230 TRP A CZ2 1842 C CZ3 . TRP A 231 ? 0.2553 0.3154 0.2910 0.0143 -0.0135 -0.0047 230 TRP A CZ3 1843 C CH2 . TRP A 231 ? 0.2491 0.3080 0.2888 0.0163 -0.0214 -0.0083 230 TRP A CH2 1844 N N . THR A 232 ? 0.2602 0.3025 0.2879 0.0180 0.0010 0.0068 231 THR A N 1845 C CA . THR A 232 ? 0.2662 0.2989 0.2838 0.0111 0.0022 0.0028 231 THR A CA 1846 C C . THR A 232 ? 0.2673 0.3133 0.2910 0.0110 0.0089 -0.0013 231 THR A C 1847 O O . THR A 232 ? 0.2482 0.3092 0.2844 0.0181 0.0115 -0.0013 231 THR A O 1848 C CB . THR A 232 ? 0.2756 0.2883 0.2787 0.0054 0.0036 0.0023 231 THR A CB 1849 O OG1 . THR A 232 ? 0.2829 0.2824 0.2703 -0.0037 0.0023 0.0004 231 THR A OG1 1850 C CG2 . THR A 232 ? 0.2813 0.2954 0.2871 0.0076 0.0124 -0.0003 231 THR A CG2 1851 N N . ILE A 233 ? 0.2804 0.3206 0.2950 0.0022 0.0103 -0.0047 232 ILE A N 1852 C CA . ILE A 233 ? 0.2932 0.3461 0.3127 -0.0016 0.0178 -0.0106 232 ILE A CA 1853 C C . ILE A 233 ? 0.3090 0.3523 0.3172 -0.0095 0.0266 -0.0149 232 ILE A C 1854 O O . ILE A 233 ? 0.3234 0.3465 0.3106 -0.0205 0.0259 -0.0140 232 ILE A O 1855 C CB . ILE A 233 ? 0.3037 0.3544 0.3177 -0.0099 0.0150 -0.0122 232 ILE A CB 1856 C CG1 . ILE A 233 ? 0.2940 0.3552 0.3191 -0.0024 0.0070 -0.0107 232 ILE A CG1 1857 C CG2 . ILE A 233 ? 0.3037 0.3682 0.3221 -0.0177 0.0245 -0.0195 232 ILE A CG2 1858 C CD1 . ILE A 233 ? 0.2830 0.3690 0.3263 0.0078 0.0084 -0.0109 232 ILE A CD1 1859 N N . LEU A 234 ? 0.3034 0.3604 0.3247 -0.0038 0.0342 -0.0202 233 LEU A N 1860 C CA . LEU A 234 ? 0.3253 0.3774 0.3391 -0.0102 0.0444 -0.0275 233 LEU A CA 1861 C C . LEU A 234 ? 0.3412 0.4088 0.3581 -0.0204 0.0546 -0.0369 233 LEU A C 1862 O O . LEU A 234 ? 0.3334 0.4266 0.3733 -0.0139 0.0576 -0.0429 233 LEU A O 1863 C CB . LEU A 234 ? 0.3180 0.3765 0.3474 0.0026 0.0468 -0.0306 233 LEU A CB 1864 C CG . LEU A 234 ? 0.3298 0.3827 0.3539 -0.0010 0.0570 -0.0401 233 LEU A CG 1865 C CD1 . LEU A 234 ? 0.3546 0.3808 0.3494 -0.0132 0.0559 -0.0366 233 LEU A CD1 1866 C CD2 . LEU A 234 ? 0.3245 0.3786 0.3650 0.0140 0.0559 -0.0420 233 LEU A CD2 1867 N N . LYS A 235 ? 0.3777 0.4300 0.3705 -0.0375 0.0592 -0.0380 234 LYS A N 1868 C CA . LYS A 235 ? 0.3980 0.4642 0.3910 -0.0513 0.0701 -0.0467 234 LYS A CA 1869 C C . LYS A 235 ? 0.3871 0.4774 0.3977 -0.0499 0.0846 -0.0613 234 LYS A C 1870 O O . LYS A 235 ? 0.3831 0.4691 0.3949 -0.0428 0.0873 -0.0646 234 LYS A O 1871 C CB . LYS A 235 ? 0.4393 0.4785 0.3966 -0.0725 0.0715 -0.0431 234 LYS A CB 1872 C CG . LYS A 235 ? 0.4578 0.4736 0.4003 -0.0743 0.0564 -0.0312 234 LYS A CG 1873 C CD . LYS A 235 ? 0.4624 0.4941 0.4219 -0.0730 0.0534 -0.0321 234 LYS A CD 1874 C CE . LYS A 235 ? 0.5011 0.5384 0.4526 -0.0931 0.0648 -0.0389 234 LYS A CE 1875 N NZ . LYS A 235 ? 0.4948 0.5485 0.4634 -0.0937 0.0623 -0.0415 234 LYS A NZ 1876 N N . PRO A 236 ? 0.3797 0.4966 0.4061 -0.0566 0.0937 -0.0716 235 PRO A N 1877 C CA . PRO A 236 ? 0.3839 0.5276 0.4293 -0.0570 0.1089 -0.0889 235 PRO A CA 1878 C C . PRO A 236 ? 0.4102 0.5374 0.4311 -0.0690 0.1201 -0.0945 235 PRO A C 1879 O O . PRO A 236 ? 0.4382 0.5413 0.4238 -0.0886 0.1221 -0.0888 235 PRO A O 1880 C CB . PRO A 236 ? 0.3875 0.5551 0.4414 -0.0723 0.1179 -0.0977 235 PRO A CB 1881 C CG . PRO A 236 ? 0.3838 0.5310 0.4188 -0.0804 0.1068 -0.0839 235 PRO A CG 1882 C CD . PRO A 236 ? 0.3687 0.4947 0.3994 -0.0635 0.0903 -0.0696 235 PRO A CD 1883 N N . ASN A 237 ? 0.4151 0.5532 0.4530 -0.0570 0.1260 -0.1055 236 ASN A N 1884 C CA . ASN A 237 ? 0.4400 0.5656 0.4573 -0.0667 0.1376 -0.1142 236 ASN A CA 1885 C C . ASN A 237 ? 0.4397 0.5262 0.4246 -0.0678 0.1281 -0.1012 236 ASN A C 1886 O O . ASN A 237 ? 0.4702 0.5448 0.4350 -0.0766 0.1366 -0.1081 236 ASN A O 1887 C CB . ASN A 237 ? 0.4792 0.6127 0.4773 -0.0936 0.1556 -0.1248 236 ASN A CB 1888 C CG . ASN A 237 ? 0.5049 0.6721 0.5278 -0.0933 0.1745 -0.1496 236 ASN A CG 1889 O OD1 . ASN A 237 ? 0.5048 0.7069 0.5697 -0.0793 0.1760 -0.1607 236 ASN A OD1 1890 N ND2 . ASN A 237 ? 0.5401 0.6983 0.5381 -0.1082 0.1885 -0.1595 236 ASN A ND2 1891 N N . ASP A 238 ? 0.4115 0.4804 0.3923 -0.0592 0.1109 -0.0840 237 ASP A N 1892 C CA . ASP A 238 ? 0.4072 0.4451 0.3660 -0.0570 0.1004 -0.0733 237 ASP A CA 1893 C C . ASP A 238 ? 0.3955 0.4371 0.3785 -0.0358 0.0955 -0.0746 237 ASP A C 1894 O O . ASP A 238 ? 0.3734 0.4376 0.3879 -0.0215 0.0954 -0.0790 237 ASP A O 1895 C CB . ASP A 238 ? 0.3939 0.4134 0.3389 -0.0587 0.0846 -0.0563 237 ASP A CB 1896 C CG . ASP A 238 ? 0.3935 0.3824 0.3134 -0.0605 0.0740 -0.0469 237 ASP A CG 1897 O OD1 . ASP A 238 ? 0.4048 0.3807 0.3038 -0.0695 0.0799 -0.0522 237 ASP A OD1 1898 O OD2 . ASP A 238 ? 0.3743 0.3541 0.2962 -0.0533 0.0597 -0.0355 237 ASP A OD2 1899 N N . ALA A 239 ? 0.4045 0.4224 0.3717 -0.0346 0.0904 -0.0708 238 ALA A N 1900 C CA . ALA A 239 ? 0.4001 0.4147 0.3856 -0.0170 0.0846 -0.0700 238 ALA A CA 1901 C C . ALA A 239 ? 0.3889 0.3830 0.3636 -0.0145 0.0696 -0.0542 238 ALA A C 1902 O O . ALA A 239 ? 0.3991 0.3792 0.3510 -0.0258 0.0640 -0.0467 238 ALA A O 1903 C CB . ALA A 239 ? 0.4234 0.4311 0.4048 -0.0176 0.0943 -0.0840 238 ALA A CB 1904 N N . ILE A 240 ? 0.3790 0.3720 0.3712 0.0000 0.0626 -0.0497 239 ILE A N 1905 C CA . ILE A 240 ? 0.3738 0.3511 0.3598 0.0021 0.0503 -0.0370 239 ILE A CA 1906 C C . ILE A 240 ? 0.3844 0.3461 0.3715 0.0075 0.0502 -0.0402 239 ILE A C 1907 O O . ILE A 240 ? 0.3934 0.3600 0.3985 0.0188 0.0533 -0.0458 239 ILE A O 1908 C CB . ILE A 240 ? 0.3540 0.3438 0.3569 0.0116 0.0420 -0.0268 239 ILE A CB 1909 C CG1 . ILE A 240 ? 0.3520 0.3295 0.3476 0.0103 0.0313 -0.0157 239 ILE A CG1 1910 C CG2 . ILE A 240 ? 0.3532 0.3527 0.3789 0.0264 0.0424 -0.0287 239 ILE A CG2 1911 C CD1 . ILE A 240 ? 0.3375 0.3283 0.3448 0.0160 0.0244 -0.0070 239 ILE A CD1 1912 N N . ASN A 241 ? 0.3847 0.3269 0.3531 -0.0004 0.0454 -0.0371 240 ASN A N 1913 C CA . ASN A 241 ? 0.3997 0.3245 0.3660 0.0014 0.0455 -0.0414 240 ASN A CA 1914 C C . ASN A 241 ? 0.3881 0.3024 0.3548 0.0021 0.0344 -0.0299 240 ASN A C 1915 O O . ASN A 241 ? 0.3797 0.2919 0.3358 -0.0053 0.0271 -0.0234 240 ASN A O 1916 C CB . ASN A 241 ? 0.4216 0.3334 0.3638 -0.0111 0.0512 -0.0515 240 ASN A CB 1917 C CG . ASN A 241 ? 0.4282 0.3528 0.3645 -0.0174 0.0635 -0.0620 240 ASN A CG 1918 O OD1 . ASN A 241 ? 0.4258 0.3635 0.3791 -0.0102 0.0736 -0.0737 240 ASN A OD1 1919 N ND2 . ASN A 241 ? 0.4356 0.3566 0.3481 -0.0314 0.0621 -0.0584 240 ASN A ND2 1920 N N . PHE A 242 ? 0.3903 0.2977 0.3697 0.0108 0.0328 -0.0279 241 PHE A N 1921 C CA . PHE A 242 ? 0.3929 0.2916 0.3736 0.0097 0.0244 -0.0175 241 PHE A CA 1922 C C . PHE A 242 ? 0.4163 0.2920 0.3896 0.0058 0.0244 -0.0226 241 PHE A C 1923 O O . PHE A 242 ? 0.4360 0.3016 0.4133 0.0119 0.0296 -0.0313 241 PHE A O 1924 C CB . PHE A 242 ? 0.3940 0.2984 0.3907 0.0203 0.0216 -0.0090 241 PHE A CB 1925 C CG . PHE A 242 ? 0.3712 0.2987 0.3760 0.0241 0.0204 -0.0036 241 PHE A CG 1926 C CD1 . PHE A 242 ? 0.3589 0.2957 0.3622 0.0192 0.0150 0.0048 241 PHE A CD1 1927 C CD2 . PHE A 242 ? 0.3680 0.3094 0.3838 0.0326 0.0247 -0.0088 241 PHE A CD2 1928 C CE1 . PHE A 242 ? 0.3451 0.3019 0.3555 0.0225 0.0139 0.0082 241 PHE A CE1 1929 C CE2 . PHE A 242 ? 0.3534 0.3158 0.3766 0.0352 0.0232 -0.0046 241 PHE A CE2 1930 C CZ . PHE A 242 ? 0.3429 0.3115 0.3621 0.0300 0.0178 0.0040 241 PHE A CZ 1931 N N . GLU A 243 ? 0.4198 0.2881 0.3842 -0.0039 0.0181 -0.0188 242 GLU A N 1932 C CA . GLU A 243 ? 0.4360 0.2825 0.3949 -0.0092 0.0166 -0.0221 242 GLU A CA 1933 C C . GLU A 243 ? 0.4230 0.2697 0.3876 -0.0139 0.0097 -0.0112 242 GLU A C 1934 O O . GLU A 243 ? 0.3979 0.2610 0.3643 -0.0179 0.0050 -0.0059 242 GLU A O 1935 C CB . GLU A 243 ? 0.4595 0.2976 0.3999 -0.0199 0.0162 -0.0315 242 GLU A CB 1936 C CG . GLU A 243 ? 0.4971 0.3127 0.4310 -0.0265 0.0146 -0.0372 242 GLU A CG 1937 C CD . GLU A 243 ? 0.5306 0.3374 0.4434 -0.0369 0.0145 -0.0484 242 GLU A CD 1938 O OE1 . GLU A 243 ? 0.5430 0.3516 0.4456 -0.0362 0.0221 -0.0575 242 GLU A OE1 1939 O OE2 . GLU A 243 ? 0.5499 0.3486 0.4555 -0.0469 0.0070 -0.0487 242 GLU A OE2 1940 N N . SER A 244 ? 0.4318 0.2600 0.3992 -0.0138 0.0093 -0.0087 243 SER A N 1941 C CA . SER A 244 ? 0.4297 0.2574 0.4004 -0.0217 0.0048 0.0010 243 SER A CA 1942 C C . SER A 244 ? 0.4582 0.2574 0.4252 -0.0269 0.0043 0.0008 243 SER A C 1943 O O . SER A 244 ? 0.4805 0.2598 0.4471 -0.0185 0.0066 -0.0028 243 SER A O 1944 C CB . SER A 244 ? 0.4178 0.2598 0.3975 -0.0154 0.0045 0.0127 243 SER A CB 1945 O OG . SER A 244 ? 0.4209 0.2675 0.4023 -0.0258 0.0020 0.0209 243 SER A OG 1946 N N . ASN A 245 ? 0.4626 0.2600 0.4283 -0.0408 0.0012 0.0036 244 ASN A N 1947 C CA . ASN A 245 ? 0.4978 0.2677 0.4597 -0.0485 0.0006 0.0066 244 ASN A CA 1948 C C . ASN A 245 ? 0.4958 0.2710 0.4606 -0.0563 0.0000 0.0204 244 ASN A C 1949 O O . ASN A 245 ? 0.5203 0.2794 0.4811 -0.0698 -0.0005 0.0235 244 ASN A O 1950 C CB . ASN A 245 ? 0.5192 0.2779 0.4750 -0.0618 -0.0013 -0.0036 244 ASN A CB 1951 C CG . ASN A 245 ? 0.5041 0.2893 0.4651 -0.0738 -0.0053 -0.0044 244 ASN A CG 1952 O OD1 . ASN A 245 ? 0.4862 0.2992 0.4548 -0.0699 -0.0063 -0.0003 244 ASN A OD1 1953 N ND2 . ASN A 245 ? 0.5188 0.2959 0.4772 -0.0878 -0.0085 -0.0109 244 ASN A ND2 1954 N N . GLY A 246 ? 0.4733 0.2711 0.4437 -0.0493 0.0006 0.0282 245 GLY A N 1955 C CA . GLY A 246 ? 0.4749 0.2786 0.4448 -0.0568 0.0012 0.0410 245 GLY A CA 1956 C C . GLY A 246 ? 0.4434 0.2837 0.4217 -0.0541 0.0023 0.0436 245 GLY A C 1957 O O . GLY A 246 ? 0.4226 0.2838 0.4081 -0.0496 0.0014 0.0354 245 GLY A O 1958 N N . ASN A 247 ? 0.4483 0.2933 0.4233 -0.0574 0.0037 0.0551 246 ASN A N 1959 C CA . ASN A 247 ? 0.4219 0.3010 0.4036 -0.0580 0.0057 0.0575 246 ASN A CA 1960 C C . ASN A 247 ? 0.4037 0.2975 0.3905 -0.0408 0.0042 0.0559 246 ASN A C 1961 O O . ASN A 247 ? 0.3729 0.2957 0.3673 -0.0395 0.0052 0.0542 246 ASN A O 1962 C CB . ASN A 247 ? 0.4041 0.3107 0.3982 -0.0694 0.0069 0.0483 246 ASN A CB 1963 C CG . ASN A 247 ? 0.4212 0.3183 0.4132 -0.0886 0.0090 0.0483 246 ASN A CG 1964 O OD1 . ASN A 247 ? 0.4350 0.3094 0.4233 -0.0922 0.0068 0.0440 246 ASN A OD1 1965 N ND2 . ASN A 247 ? 0.4226 0.3384 0.4168 -0.1024 0.0141 0.0517 246 ASN A ND2 1966 N N . PHE A 248 ? 0.4150 0.2891 0.3987 -0.0280 0.0022 0.0555 247 PHE A N 1967 C CA . PHE A 248 ? 0.4011 0.2882 0.3909 -0.0130 0.0016 0.0516 247 PHE A CA 1968 C C . PHE A 248 ? 0.4084 0.2977 0.3959 -0.0051 -0.0003 0.0617 247 PHE A C 1969 O O . PHE A 248 ? 0.4320 0.2968 0.4119 -0.0024 -0.0036 0.0695 247 PHE A O 1970 C CB . PHE A 248 ? 0.4131 0.2821 0.4032 -0.0045 0.0018 0.0427 247 PHE A CB 1971 C CG . PHE A 248 ? 0.3988 0.2823 0.3958 0.0084 0.0030 0.0367 247 PHE A CG 1972 C CD1 . PHE A 248 ? 0.3738 0.2843 0.3757 0.0088 0.0036 0.0352 247 PHE A CD1 1973 C CD2 . PHE A 248 ? 0.4118 0.2819 0.4117 0.0196 0.0038 0.0310 247 PHE A CD2 1974 C CE1 . PHE A 248 ? 0.3635 0.2861 0.3709 0.0181 0.0053 0.0296 247 PHE A CE1 1975 C CE2 . PHE A 248 ? 0.3955 0.2819 0.4033 0.0293 0.0064 0.0239 247 PHE A CE2 1976 C CZ . PHE A 248 ? 0.3723 0.2843 0.3827 0.0274 0.0074 0.0238 247 PHE A CZ 1977 N N . ILE A 249 ? 0.3866 0.3033 0.3796 -0.0014 0.0000 0.0616 248 ILE A N 1978 C CA . ILE A 249 ? 0.3932 0.3143 0.3844 0.0076 -0.0031 0.0692 248 ILE A CA 1979 C C . ILE A 249 ? 0.3729 0.3025 0.3749 0.0218 -0.0035 0.0607 248 ILE A C 1980 O O . ILE A 249 ? 0.3454 0.2976 0.3545 0.0226 -0.0013 0.0538 248 ILE A O 1981 C CB . ILE A 249 ? 0.3895 0.3356 0.3785 0.0012 -0.0018 0.0738 248 ILE A CB 1982 C CG1 . ILE A 249 ? 0.4029 0.3493 0.3854 -0.0162 0.0020 0.0769 248 ILE A CG1 1983 C CG2 . ILE A 249 ? 0.4044 0.3479 0.3853 0.0079 -0.0069 0.0843 248 ILE A CG2 1984 C CD1 . ILE A 249 ? 0.4386 0.3535 0.4059 -0.0242 0.0005 0.0879 248 ILE A CD1 1985 N N . ALA A 250 ? 0.3855 0.2962 0.3893 0.0324 -0.0064 0.0601 249 ALA A N 1986 C CA . ALA A 250 ? 0.3712 0.2895 0.3870 0.0438 -0.0045 0.0487 249 ALA A CA 1987 C C . ALA A 250 ? 0.3573 0.2974 0.3817 0.0537 -0.0074 0.0495 249 ALA A C 1988 O O . ALA A 250 ? 0.3572 0.2973 0.3772 0.0562 -0.0136 0.0601 249 ALA A O 1989 C CB . ALA A 250 ? 0.3994 0.2920 0.4178 0.0519 -0.0059 0.0442 249 ALA A CB 1990 N N . PRO A 251 ? 0.3436 0.3024 0.3788 0.0577 -0.0030 0.0383 250 PRO A N 1991 C CA . PRO A 251 ? 0.3367 0.3165 0.3835 0.0675 -0.0056 0.0365 250 PRO A CA 1992 C C . PRO A 251 ? 0.3691 0.3376 0.4236 0.0818 -0.0129 0.0384 250 PRO A C 1993 O O . PRO A 251 ? 0.3795 0.3266 0.4358 0.0862 -0.0127 0.0344 250 PRO A O 1994 C CB . PRO A 251 ? 0.3188 0.3130 0.3745 0.0670 0.0021 0.0223 250 PRO A CB 1995 C CG . PRO A 251 ? 0.3154 0.2996 0.3595 0.0548 0.0071 0.0199 250 PRO A CG 1996 C CD . PRO A 251 ? 0.3311 0.2906 0.3664 0.0522 0.0041 0.0269 250 PRO A CD 1997 N N . GLU A 252 ? 0.3817 0.3632 0.4403 0.0893 -0.0207 0.0443 251 GLU A N 1998 C CA . GLU A 252 ? 0.4142 0.3943 0.4874 0.1061 -0.0290 0.0418 251 GLU A CA 1999 C C . GLU A 252 ? 0.3810 0.3959 0.4727 0.1115 -0.0272 0.0313 251 GLU A C 2000 O O . GLU A 252 ? 0.3773 0.4025 0.4881 0.1190 -0.0229 0.0168 251 GLU A O 2001 C CB . GLU A 252 ? 0.4592 0.4218 0.5202 0.1108 -0.0428 0.0584 251 GLU A CB 2002 C CG . GLU A 252 ? 0.5014 0.4554 0.5773 0.1305 -0.0552 0.0567 251 GLU A CG 2003 C CD . GLU A 252 ? 0.5595 0.4856 0.6166 0.1337 -0.0707 0.0757 251 GLU A CD 2004 O OE1 . GLU A 252 ? 0.5963 0.4931 0.6313 0.1223 -0.0698 0.0869 251 GLU A OE1 2005 O OE2 . GLU A 252 ? 0.5917 0.5248 0.6549 0.1465 -0.0846 0.0797 251 GLU A OE2 2006 N N . ASN A 253 ? 0.3562 0.3900 0.4422 0.1059 -0.0293 0.0370 252 ASN A N 2007 C CA . ASN A 253 ? 0.3297 0.3960 0.4313 0.1083 -0.0279 0.0276 252 ASN A CA 2008 C C . ASN A 253 ? 0.3033 0.3830 0.3994 0.0939 -0.0174 0.0226 252 ASN A C 2009 O O . ASN A 253 ? 0.3010 0.3722 0.3805 0.0837 -0.0157 0.0301 252 ASN A O 2010 C CB . ASN A 253 ? 0.3297 0.4079 0.4299 0.1142 -0.0406 0.0363 252 ASN A CB 2011 C CG . ASN A 253 ? 0.3599 0.4186 0.4602 0.1282 -0.0547 0.0449 252 ASN A CG 2012 O OD1 . ASN A 253 ? 0.3689 0.4215 0.4866 0.1405 -0.0565 0.0366 252 ASN A OD1 2013 N ND2 . ASN A 253 ? 0.3780 0.4254 0.4577 0.1261 -0.0650 0.0610 252 ASN A ND2 2014 N N . ALA A 254 ? 0.2855 0.3862 0.3965 0.0932 -0.0110 0.0095 253 ALA A N 2015 C CA . ALA A 254 ? 0.2637 0.3766 0.3701 0.0805 -0.0034 0.0046 253 ALA A CA 2016 C C . ALA A 254 ? 0.2479 0.3898 0.3680 0.0822 -0.0058 -0.0012 253 ALA A C 2017 O O . ALA A 254 ? 0.2419 0.3968 0.3773 0.0937 -0.0129 -0.0032 253 ALA A O 2018 C CB . ALA A 254 ? 0.2651 0.3719 0.3714 0.0735 0.0078 -0.0057 253 ALA A CB 2019 N N . TYR A 255 ? 0.2363 0.3874 0.3515 0.0710 -0.0011 -0.0047 254 TYR A N 2020 C CA . TYR A 255 ? 0.2296 0.4066 0.3555 0.0698 -0.0034 -0.0104 254 TYR A CA 2021 C C . TYR A 255 ? 0.2268 0.4146 0.3601 0.0601 0.0067 -0.0230 254 TYR A C 2022 O O . TYR A 255 ? 0.2479 0.4219 0.3673 0.0485 0.0131 -0.0235 254 TYR A O 2023 C CB . TYR A 255 ? 0.2270 0.4049 0.3397 0.0640 -0.0077 -0.0040 254 TYR A CB 2024 C CG . TYR A 255 ? 0.2380 0.4091 0.3403 0.0699 -0.0165 0.0080 254 TYR A CG 2025 C CD1 . TYR A 255 ? 0.2366 0.3858 0.3237 0.0671 -0.0153 0.0166 254 TYR A CD1 2026 C CD2 . TYR A 255 ? 0.2488 0.4356 0.3548 0.0767 -0.0263 0.0109 254 TYR A CD2 2027 C CE1 . TYR A 255 ? 0.2521 0.3949 0.3271 0.0691 -0.0218 0.0278 254 TYR A CE1 2028 C CE2 . TYR A 255 ? 0.2613 0.4397 0.3525 0.0796 -0.0342 0.0231 254 TYR A CE2 2029 C CZ . TYR A 255 ? 0.2656 0.4218 0.3409 0.0749 -0.0310 0.0316 254 TYR A CZ 2030 O OH . TYR A 255 ? 0.2849 0.4326 0.3431 0.0747 -0.0375 0.0438 254 TYR A OH 2031 N N . LYS A 256 ? 0.2262 0.4388 0.3810 0.0640 0.0075 -0.0334 255 LYS A N 2032 C CA . LYS A 256 ? 0.2197 0.4468 0.3821 0.0520 0.0181 -0.0463 255 LYS A CA 2033 C C . LYS A 256 ? 0.2015 0.4389 0.3600 0.0425 0.0156 -0.0466 255 LYS A C 2034 O O . LYS A 256 ? 0.1992 0.4551 0.3679 0.0491 0.0065 -0.0462 255 LYS A O 2035 C CB . LYS A 256 ? 0.2272 0.4822 0.4189 0.0597 0.0205 -0.0599 255 LYS A CB 2036 C CG . LYS A 256 ? 0.2443 0.4905 0.4439 0.0706 0.0232 -0.0632 255 LYS A CG 2037 C CD . LYS A 256 ? 0.2493 0.5241 0.4777 0.0725 0.0320 -0.0826 255 LYS A CD 2038 C CE . LYS A 256 ? 0.2506 0.5599 0.5085 0.0835 0.0219 -0.0893 255 LYS A CE 2039 N NZ . LYS A 256 ? 0.2654 0.6049 0.5584 0.0907 0.0281 -0.1097 255 LYS A NZ 2040 N N . ILE A 257 ? 0.3088 0.5524 0.3301 -0.0691 -0.0256 -0.0218 256 ILE A N 2041 C CA . ILE A 257 ? 0.3236 0.5386 0.3192 -0.0749 -0.0233 -0.0149 256 ILE A CA 2042 C C . ILE A 257 ? 0.3420 0.5528 0.3294 -0.0967 -0.0049 -0.0154 256 ILE A C 2043 O O . ILE A 257 ? 0.3797 0.5654 0.3325 -0.1044 0.0074 -0.0148 256 ILE A O 2044 C CB . ILE A 257 ? 0.3656 0.5380 0.3123 -0.0605 -0.0319 -0.0114 256 ILE A CB 2045 C CG1 . ILE A 257 ? 0.3464 0.5340 0.3133 -0.0396 -0.0509 -0.0191 256 ILE A CG1 2046 C CG2 . ILE A 257 ? 0.3975 0.5309 0.3098 -0.0692 -0.0251 -0.0035 256 ILE A CG2 2047 C CD1 . ILE A 257 ? 0.3873 0.5476 0.3129 -0.0162 -0.0654 -0.0248 256 ILE A CD1 2048 N N . VAL A 258 ? 0.3169 0.5523 0.3356 -0.1060 -0.0018 -0.0196 257 VAL A N 2049 C CA . VAL A 258 ? 0.3284 0.5769 0.3565 -0.1266 0.0148 -0.0296 257 VAL A CA 2050 C C . VAL A 258 ? 0.3665 0.5812 0.3677 -0.1426 0.0276 -0.0290 257 VAL A C 2051 O O . VAL A 258 ? 0.3945 0.5958 0.3809 -0.1636 0.0493 -0.0364 257 VAL A O 2052 C CB . VAL A 258 ? 0.2885 0.5862 0.3650 -0.1231 0.0088 -0.0406 257 VAL A CB 2053 C CG1 . VAL A 258 ? 0.2976 0.6169 0.3924 -0.1415 0.0214 -0.0584 257 VAL A CG1 2054 C CG2 . VAL A 258 ? 0.2674 0.5893 0.3616 -0.1139 0.0049 -0.0440 257 VAL A CG2 2055 N N . LYS A 259 ? 0.3682 0.5670 0.3626 -0.1341 0.0169 -0.0217 258 LYS A N 2056 C CA . LYS A 259 ? 0.4086 0.5711 0.3765 -0.1475 0.0279 -0.0209 258 LYS A CA 2057 C C . LYS A 259 ? 0.4368 0.5577 0.3687 -0.1301 0.0140 -0.0073 258 LYS A C 2058 O O . LYS A 259 ? 0.3984 0.5382 0.3492 -0.1109 -0.0057 -0.0040 258 LYS A O 2059 C CB . LYS A 259 ? 0.3798 0.5794 0.3900 -0.1570 0.0287 -0.0348 258 LYS A CB 2060 C CG . LYS A 259 ? 0.4152 0.5815 0.4055 -0.1730 0.0414 -0.0377 258 LYS A CG 2061 C CD . LYS A 259 ? 0.3901 0.6012 0.4274 -0.1821 0.0420 -0.0582 258 LYS A CD 2062 C CE . LYS A 259 ? 0.4307 0.6089 0.4517 -0.2048 0.0612 -0.0666 258 LYS A CE 2063 N NZ . LYS A 259 ? 0.4035 0.6168 0.4617 -0.2008 0.0497 -0.0802 258 LYS A NZ 2064 N N . LYS A 260 ? 0.5071 0.5695 0.3862 -0.1373 0.0262 -0.0018 259 LYS A N 2065 C CA . LYS A 260 ? 0.5496 0.5699 0.3912 -0.1192 0.0122 0.0077 259 LYS A CA 2066 C C . LYS A 260 ? 0.6029 0.5879 0.4252 -0.1355 0.0260 0.0068 259 LYS A C 2067 O O . LYS A 260 ? 0.6357 0.6030 0.4485 -0.1625 0.0535 0.0001 259 LYS A O 2068 C CB . LYS A 260 ? 0.6098 0.5774 0.3875 -0.1006 0.0083 0.0163 259 LYS A CB 2069 C CG . LYS A 260 ? 0.5761 0.5807 0.3761 -0.0796 -0.0104 0.0136 259 LYS A CG 2070 C CD . LYS A 260 ? 0.6415 0.6015 0.3808 -0.0661 -0.0082 0.0174 259 LYS A CD 2071 C CE . LYS A 260 ? 0.7037 0.6134 0.3851 -0.0343 -0.0278 0.0206 259 LYS A CE 2072 N NZ . LYS A 260 ? 0.6641 0.6213 0.3857 -0.0075 -0.0575 0.0090 259 LYS A NZ 2073 N N . GLY A 261 ? 0.6174 0.5940 0.4373 -0.1205 0.0087 0.0104 260 GLY A N 2074 C CA . GLY A 261 ? 0.6710 0.6110 0.4709 -0.1323 0.0187 0.0095 260 GLY A CA 2075 C C . GLY A 261 ? 0.6842 0.6181 0.4802 -0.1089 -0.0057 0.0137 260 GLY A C 2076 O O . GLY A 261 ? 0.6739 0.6186 0.4694 -0.0828 -0.0280 0.0166 260 GLY A O 2077 N N . ASP A 262 ? 0.7222 0.6410 0.5182 -0.1191 -0.0005 0.0103 261 ASP A N 2078 C CA . ASP A 262 ? 0.7172 0.6379 0.5172 -0.0991 -0.0228 0.0115 261 ASP A CA 2079 C C . ASP A 262 ? 0.6264 0.6222 0.4943 -0.0946 -0.0367 0.0049 261 ASP A C 2080 O O . ASP A 262 ? 0.6057 0.6426 0.5154 -0.1107 -0.0280 -0.0036 261 ASP A O 2081 C CB . ASP A 262 ? 0.7745 0.6504 0.5489 -0.1104 -0.0126 0.0097 261 ASP A CB 2082 C CG . ASP A 262 ? 0.8777 0.6637 0.5675 -0.0959 -0.0115 0.0200 261 ASP A CG 2083 O OD1 . ASP A 262 ? 0.8894 0.6646 0.5546 -0.0632 -0.0364 0.0244 261 ASP A OD1 2084 O OD2 . ASP A 262 ? 0.9585 0.6825 0.6044 -0.1162 0.0149 0.0212 261 ASP A OD2 2085 N N . SER A 263 ? 0.5805 0.5913 0.4554 -0.0706 -0.0576 0.0065 262 SER A N 2086 C CA . SER A 263 ? 0.5051 0.5714 0.4308 -0.0640 -0.0676 0.0019 262 SER A CA 2087 C C . SER A 263 ? 0.4978 0.5576 0.4160 -0.0415 -0.0863 -0.0004 262 SER A C 2088 O O . SER A 263 ? 0.5370 0.5529 0.4116 -0.0290 -0.0940 0.0005 262 SER A O 2089 C CB . SER A 263 ? 0.4712 0.5716 0.4221 -0.0638 -0.0651 0.0015 262 SER A CB 2090 O OG . SER A 263 ? 0.4329 0.5719 0.4205 -0.0543 -0.0724 -0.0017 262 SER A OG 2091 N N . THR A 264 ? 0.4457 0.5461 0.4028 -0.0350 -0.0927 -0.0056 263 THR A N 2092 C CA . THR A 264 ? 0.4313 0.5362 0.3919 -0.0160 -0.1077 -0.0140 263 THR A CA 2093 C C . THR A 264 ? 0.3806 0.5297 0.3850 -0.0148 -0.1046 -0.0204 263 THR A C 2094 O O . THR A 264 ? 0.3555 0.5241 0.3796 -0.0257 -0.0932 -0.0153 263 THR A O 2095 C CB . THR A 264 ? 0.4420 0.5286 0.3901 -0.0121 -0.1148 -0.0157 263 THR A CB 2096 O OG1 . THR A 264 ? 0.4498 0.5352 0.3936 0.0094 -0.1318 -0.0276 263 THR A OG1 2097 C CG2 . THR A 264 ? 0.4067 0.5233 0.3870 -0.0215 -0.1086 -0.0157 263 THR A CG2 2098 N N . ILE A 265 ? 0.3695 0.5317 0.3866 -0.0007 -0.1137 -0.0344 264 ILE A N 2099 C CA . ILE A 265 ? 0.3344 0.5303 0.3903 -0.0023 -0.1056 -0.0437 264 ILE A CA 2100 C C . ILE A 265 ? 0.3343 0.5332 0.3956 0.0033 -0.1109 -0.0513 264 ILE A C 2101 O O . ILE A 265 ? 0.3451 0.5430 0.4035 0.0175 -0.1252 -0.0666 264 ILE A O 2102 C CB . ILE A 265 ? 0.3225 0.5396 0.4007 0.0049 -0.1068 -0.0620 264 ILE A CB 2103 C CG1 . ILE A 265 ? 0.3221 0.5371 0.3949 0.0003 -0.1022 -0.0551 264 ILE A CG1 2104 C CG2 . ILE A 265 ? 0.2994 0.5434 0.4156 -0.0019 -0.0904 -0.0732 264 ILE A CG2 2105 C CD1 . ILE A 265 ? 0.3161 0.5533 0.4114 0.0086 -0.1052 -0.0763 264 ILE A CD1 2106 N N . MET A 266 ? 0.3235 0.5268 0.3909 -0.0050 -0.1007 -0.0426 265 MET A N 2107 C CA . MET A 266 ? 0.3302 0.5386 0.4038 -0.0011 -0.1021 -0.0487 265 MET A CA 2108 C C . MET A 266 ? 0.3186 0.5492 0.4202 -0.0023 -0.0879 -0.0618 265 MET A C 2109 O O . MET A 266 ? 0.3080 0.5440 0.4195 -0.0097 -0.0709 -0.0582 265 MET A O 2110 C CB . MET A 266 ? 0.3303 0.5336 0.3948 -0.0070 -0.0972 -0.0357 265 MET A CB 2111 C CG . MET A 266 ? 0.3521 0.5356 0.3961 -0.0067 -0.1091 -0.0324 265 MET A CG 2112 S SD . MET A 266 ? 0.3483 0.5398 0.3939 -0.0106 -0.1044 -0.0272 265 MET A SD 2113 C CE . MET A 266 ? 0.3750 0.5392 0.3999 -0.0171 -0.1133 -0.0270 265 MET A CE 2114 N N . LYS A 267 ? 0.3277 0.5680 0.4405 0.0040 -0.0923 -0.0782 266 LYS A N 2115 C CA . LYS A 267 ? 0.3232 0.5811 0.4614 -0.0012 -0.0725 -0.0928 266 LYS A CA 2116 C C . LYS A 267 ? 0.3208 0.5698 0.4458 -0.0019 -0.0655 -0.0830 266 LYS A C 2117 O O . LYS A 267 ? 0.3181 0.5637 0.4336 0.0054 -0.0815 -0.0839 266 LYS A O 2118 C CB . LYS A 267 ? 0.3274 0.6100 0.4936 0.0062 -0.0805 -0.1250 266 LYS A CB 2119 C CG . LYS A 267 ? 0.3328 0.6245 0.5063 0.0146 -0.0949 -0.1380 266 LYS A CG 2120 C CD . LYS A 267 ? 0.3363 0.6370 0.5289 0.0018 -0.0741 -0.1391 266 LYS A CD 2121 C CE . LYS A 267 ? 0.3431 0.6731 0.5800 -0.0076 -0.0518 -0.1710 266 LYS A CE 2122 N NZ . LYS A 267 ? 0.3387 0.6788 0.5986 -0.0184 -0.0340 -0.1803 266 LYS A NZ 2123 N N . SER A 268 ? 0.3232 0.5636 0.4418 -0.0086 -0.0420 -0.0735 267 SER A N 2124 C CA . SER A 268 ? 0.3393 0.5681 0.4380 -0.0050 -0.0348 -0.0649 267 SER A CA 2125 C C . SER A 268 ? 0.3613 0.5730 0.4482 -0.0097 -0.0032 -0.0609 267 SER A C 2126 O O . SER A 268 ? 0.3607 0.5645 0.4487 -0.0157 0.0109 -0.0575 267 SER A O 2127 C CB . SER A 268 ? 0.3429 0.5621 0.4180 0.0014 -0.0512 -0.0466 267 SER A CB 2128 O OG . SER A 268 ? 0.3622 0.5733 0.4179 0.0088 -0.0466 -0.0415 267 SER A OG 2129 N N . GLU A 269 ? 0.3913 0.5920 0.4617 -0.0061 0.0090 -0.0613 268 GLU A N 2130 C CA . GLU A 269 ? 0.4323 0.6011 0.4741 -0.0074 0.0423 -0.0545 268 GLU A CA 2131 C C . GLU A 269 ? 0.4517 0.5944 0.4475 0.0094 0.0370 -0.0316 268 GLU A C 2132 O O . GLU A 269 ? 0.4916 0.5986 0.4525 0.0138 0.0604 -0.0216 268 GLU A O 2133 C CB . GLU A 269 ? 0.4550 0.6204 0.4968 -0.0116 0.0628 -0.0691 268 GLU A CB 2134 C CG . GLU A 269 ? 0.4406 0.6366 0.5330 -0.0277 0.0722 -0.1001 268 GLU A CG 2135 C CD . GLU A 269 ? 0.4461 0.6370 0.5563 -0.0434 0.0983 -0.1092 268 GLU A CD 2136 O OE1 . GLU A 269 ? 0.4917 0.6456 0.5770 -0.0523 0.1374 -0.1056 268 GLU A OE1 2137 O OE2 . GLU A 269 ? 0.4045 0.6236 0.5488 -0.0460 0.0809 -0.1200 268 GLU A OE2 2138 N N . LEU A 270 ? 0.4331 0.5928 0.4289 0.0196 0.0064 -0.0263 269 LEU A N 2139 C CA . LEU A 270 ? 0.4571 0.6052 0.4186 0.0384 -0.0041 -0.0136 269 LEU A CA 2140 C C . LEU A 270 ? 0.4793 0.6135 0.4251 0.0434 0.0000 -0.0032 269 LEU A C 2141 O O . LEU A 270 ? 0.4629 0.6070 0.4334 0.0303 0.0007 -0.0043 269 LEU A O 2142 C CB . LEU A 270 ? 0.4248 0.6005 0.4022 0.0422 -0.0352 -0.0174 269 LEU A CB 2143 C CG . LEU A 270 ? 0.4180 0.6059 0.4076 0.0409 -0.0442 -0.0276 269 LEU A CG 2144 C CD1 . LEU A 270 ? 0.4008 0.6076 0.4029 0.0423 -0.0710 -0.0314 269 LEU A CD1 2145 C CD2 . LEU A 270 ? 0.4503 0.6205 0.4090 0.0535 -0.0303 -0.0274 269 LEU A CD2 2146 N N . GLU A 271 ? 0.5289 0.6399 0.4306 0.0659 0.0011 0.0049 270 GLU A N 2147 C CA . GLU A 271 ? 0.5512 0.6484 0.4308 0.0788 0.0002 0.0125 270 GLU A CA 2148 C C . GLU A 271 ? 0.5123 0.6477 0.4111 0.0869 -0.0317 0.0060 270 GLU A C 2149 O O . GLU A 271 ? 0.4752 0.6391 0.4002 0.0801 -0.0482 -0.0024 270 GLU A O 2150 C CB . GLU A 271 ? 0.6389 0.6843 0.4514 0.1050 0.0175 0.0218 270 GLU A CB 2151 C CG . GLU A 271 ? 0.6963 0.6943 0.4846 0.0930 0.0584 0.0268 270 GLU A CG 2152 C CD . GLU A 271 ? 0.7979 0.7396 0.5136 0.1166 0.0780 0.0347 270 GLU A CD 2153 O OE1 . GLU A 271 ? 0.8208 0.7739 0.5216 0.1352 0.0595 0.0318 270 GLU A OE1 2154 O OE2 . GLU A 271 ? 0.8637 0.7449 0.5334 0.1165 0.1145 0.0431 270 GLU A OE2 2155 N N . TYR A 272 ? 0.5130 0.6486 0.4005 0.1000 -0.0384 0.0070 271 TYR A N 2156 C CA . TYR A 272 ? 0.4808 0.6568 0.3912 0.1057 -0.0647 -0.0055 271 TYR A CA 2157 C C . TYR A 272 ? 0.4916 0.6790 0.3837 0.1317 -0.0824 -0.0171 271 TYR A C 2158 O O . TYR A 272 ? 0.5299 0.6878 0.3720 0.1614 -0.0796 -0.0135 271 TYR A O 2159 C CB . TYR A 272 ? 0.4916 0.6691 0.3974 0.1146 -0.0671 -0.0060 271 TYR A CB 2160 C CG . TYR A 272 ? 0.4708 0.6951 0.4069 0.1172 -0.0901 -0.0251 271 TYR A CG 2161 C CD1 . TYR A 272 ? 0.4294 0.6866 0.4109 0.0902 -0.0968 -0.0342 271 TYR A CD1 2162 C CD2 . TYR A 272 ? 0.4980 0.7312 0.4154 0.1471 -0.1035 -0.0369 271 TYR A CD2 2163 C CE1 . TYR A 272 ? 0.4161 0.7138 0.4273 0.0873 -0.1111 -0.0554 271 TYR A CE1 2164 C CE2 . TYR A 272 ? 0.4807 0.7644 0.4342 0.1471 -0.1224 -0.0618 271 TYR A CE2 2165 C CZ . TYR A 272 ? 0.4404 0.7564 0.4430 0.1141 -0.1235 -0.0713 271 TYR A CZ 2166 O OH . TYR A 272 ? 0.4259 0.7899 0.4664 0.1090 -0.1356 -0.0996 271 TYR A OH 2167 N N . GLY A 273 ? 0.4554 0.6827 0.3851 0.1214 -0.0999 -0.0324 272 GLY A N 2168 C CA . GLY A 273 ? 0.4652 0.7110 0.3886 0.1417 -0.1172 -0.0483 272 GLY A CA 2169 C C . GLY A 273 ? 0.4752 0.7555 0.4033 0.1659 -0.1389 -0.0723 272 GLY A C 2170 O O . GLY A 273 ? 0.4879 0.7880 0.4131 0.1856 -0.1549 -0.0903 272 GLY A O 2171 N N . ASN A 274 ? 0.4687 0.7613 0.4078 0.1659 -0.1407 -0.0770 273 ASN A N 2172 C CA . ASN A 274 ? 0.4791 0.8125 0.4292 0.1902 -0.1623 -0.1067 273 ASN A CA 2173 C C . ASN A 274 ? 0.4536 0.8378 0.4512 0.1789 -0.1766 -0.1371 273 ASN A C 2174 O O . ASN A 274 ? 0.4669 0.8730 0.4571 0.2080 -0.1949 -0.1599 273 ASN A O 2175 C CB . ASN A 274 ? 0.5400 0.8480 0.4274 0.2418 -0.1727 -0.1079 273 ASN A CB 2176 C CG . ASN A 274 ? 0.5810 0.8295 0.4158 0.2522 -0.1540 -0.0794 273 ASN A CG 2177 O OD1 . ASN A 274 ? 0.6274 0.8215 0.4121 0.2601 -0.1369 -0.0569 273 ASN A OD1 2178 N ND2 . ASN A 274 ? 0.5717 0.8289 0.4188 0.2498 -0.1542 -0.0821 273 ASN A ND2 2179 N N . CYS A 275 ? 0.4190 0.8170 0.4616 0.1370 -0.1666 -0.1378 274 CYS A N 2180 C CA . CYS A 275 ? 0.4041 0.8342 0.4885 0.1163 -0.1710 -0.1613 274 CYS A CA 2181 C C . CYS A 275 ? 0.3678 0.8026 0.4890 0.0738 -0.1559 -0.1614 274 CYS A C 2182 O O . CYS A 275 ? 0.3651 0.7785 0.4775 0.0629 -0.1444 -0.1407 274 CYS A O 2183 C CB . CYS A 275 ? 0.4145 0.8191 0.4827 0.1136 -0.1688 -0.1471 274 CYS A CB 2184 S SG . CYS A 275 ? 0.4320 0.7794 0.4686 0.0996 -0.1487 -0.1040 274 CYS A SG 2185 N N . ASN A 276 ? 0.3517 0.8098 0.5101 0.0502 -0.1540 -0.1852 275 ASN A N 2186 C CA . ASN A 276 ? 0.3393 0.7915 0.5228 0.0099 -0.1358 -0.1864 275 ASN A CA 2187 C C . ASN A 276 ? 0.3443 0.7753 0.5340 -0.0152 -0.1273 -0.1861 275 ASN A C 2188 O O . ASN A 276 ? 0.3529 0.8012 0.5534 -0.0071 -0.1368 -0.2051 275 ASN A O 2189 C CB . ASN A 276 ? 0.3339 0.8360 0.5595 0.0014 -0.1348 -0.2252 275 ASN A CB 2190 C CG . ASN A 276 ? 0.3313 0.8193 0.5737 -0.0404 -0.1106 -0.2242 275 ASN A CG 2191 O OD1 . ASN A 276 ? 0.3111 0.7697 0.5328 -0.0475 -0.1014 -0.1968 275 ASN A OD1 2192 N ND2 . ASN A 276 ? 0.3457 0.8524 0.6237 -0.0686 -0.0980 -0.2561 275 ASN A ND2 2193 N N . THR A 277 ? 0.3462 0.7371 0.5252 -0.0427 -0.1105 -0.1657 276 THR A N 2194 C CA . THR A 277 ? 0.3649 0.7212 0.5369 -0.0632 -0.1022 -0.1611 276 THR A CA 2195 C C . THR A 277 ? 0.3900 0.7122 0.5574 -0.0971 -0.0798 -0.1569 276 THR A C 2196 O O . THR A 277 ? 0.3831 0.7029 0.5467 -0.1030 -0.0719 -0.1484 276 THR A O 2197 C CB . THR A 277 ? 0.3591 0.6801 0.4972 -0.0480 -0.1099 -0.1309 276 THR A CB 2198 O OG1 . THR A 277 ? 0.3782 0.6655 0.5071 -0.0631 -0.1053 -0.1290 276 THR A OG1 2199 C CG2 . THR A 277 ? 0.3567 0.6520 0.4722 -0.0470 -0.1047 -0.1032 276 THR A CG2 2200 N N . LYS A 278 ? 0.4268 0.7175 0.5891 -0.1179 -0.0688 -0.1627 277 LYS A N 2201 C CA . LYS A 278 ? 0.4728 0.7077 0.6093 -0.1458 -0.0460 -0.1523 277 LYS A CA 2202 C C . LYS A 278 ? 0.4948 0.6719 0.5833 -0.1355 -0.0519 -0.1195 277 LYS A C 2203 O O . LYS A 278 ? 0.5339 0.6569 0.5872 -0.1491 -0.0375 -0.1062 277 LYS A O 2204 C CB . LYS A 278 ? 0.5143 0.7362 0.6650 -0.1754 -0.0257 -0.1797 277 LYS A CB 2205 C CG . LYS A 278 ? 0.5096 0.7921 0.7152 -0.1907 -0.0161 -0.2220 277 LYS A CG 2206 C CD . LYS A 278 ? 0.5187 0.7996 0.7274 -0.2122 0.0058 -0.2255 277 LYS A CD 2207 C CE . LYS A 278 ? 0.5811 0.7905 0.7574 -0.2498 0.0419 -0.2219 277 LYS A CE 2208 N NZ . LYS A 278 ? 0.6186 0.8204 0.8163 -0.2778 0.0628 -0.2552 277 LYS A NZ 2209 N N . CYS A 279 ? 0.4770 0.6648 0.5618 -0.1099 -0.0727 -0.1092 278 CYS A N 2210 C CA . CYS A 279 ? 0.4938 0.6376 0.5420 -0.0980 -0.0807 -0.0867 278 CYS A CA 2211 C C . CYS A 279 ? 0.4487 0.6198 0.5018 -0.0712 -0.0985 -0.0763 278 CYS A C 2212 O O . CYS A 279 ? 0.4338 0.6356 0.5039 -0.0590 -0.1080 -0.0860 278 CYS A O 2213 C CB . CYS A 279 ? 0.5335 0.6428 0.5678 -0.1040 -0.0800 -0.0937 278 CYS A CB 2214 S SG . CYS A 279 ? 0.5650 0.6262 0.5565 -0.0834 -0.0949 -0.0733 278 CYS A SG 2215 N N . GLN A 280 ? 0.4383 0.5962 0.4747 -0.0623 -0.1009 -0.0588 279 GLN A N 2216 C CA . GLN A 280 ? 0.4082 0.5894 0.4507 -0.0422 -0.1099 -0.0512 279 GLN A CA 2217 C C . GLN A 280 ? 0.4095 0.5666 0.4337 -0.0317 -0.1170 -0.0421 279 GLN A C 2218 O O . GLN A 280 ? 0.4216 0.5486 0.4257 -0.0347 -0.1161 -0.0363 279 GLN A O 2219 C CB . GLN A 280 ? 0.3927 0.5948 0.4445 -0.0414 -0.1039 -0.0464 279 GLN A CB 2220 C CG . GLN A 280 ? 0.3750 0.5904 0.4275 -0.0244 -0.1060 -0.0381 279 GLN A CG 2221 C CD . GLN A 280 ? 0.3720 0.6072 0.4281 -0.0092 -0.1108 -0.0439 279 GLN A CD 2222 O OE1 . GLN A 280 ? 0.3723 0.6027 0.4218 0.0007 -0.1127 -0.0412 279 GLN A OE1 2223 N NE2 . GLN A 280 ? 0.3736 0.6319 0.4392 -0.0057 -0.1128 -0.0549 279 GLN A NE2 2224 N N . THR A 281 ? 0.3947 0.5657 0.4248 -0.0176 -0.1241 -0.0441 280 THR A N 2225 C CA . THR A 281 ? 0.3907 0.5530 0.4144 -0.0066 -0.1302 -0.0427 280 THR A CA 2226 C C . THR A 281 ? 0.3697 0.5568 0.4075 0.0002 -0.1232 -0.0408 280 THR A C 2227 O O . THR A 281 ? 0.3521 0.5553 0.3954 0.0006 -0.1158 -0.0378 280 THR A O 2228 C CB . THR A 281 ? 0.3993 0.5551 0.4193 0.0019 -0.1408 -0.0509 280 THR A CB 2229 O OG1 . THR A 281 ? 0.3808 0.5641 0.4147 0.0099 -0.1388 -0.0546 280 THR A OG1 2230 C CG2 . THR A 281 ? 0.4243 0.5576 0.4332 -0.0070 -0.1430 -0.0549 280 THR A CG2 2231 N N . PRO A 282 ? 0.3751 0.5634 0.4170 0.0069 -0.1245 -0.0454 281 PRO A N 2232 C CA . PRO A 282 ? 0.3652 0.5716 0.4206 0.0092 -0.1113 -0.0467 281 PRO A CA 2233 C C . PRO A 282 ? 0.3739 0.5895 0.4286 0.0148 -0.1037 -0.0479 281 PRO A C 2234 O O . PRO A 282 ? 0.3828 0.6013 0.4365 0.0156 -0.0873 -0.0446 281 PRO A O 2235 C CB . PRO A 282 ? 0.3655 0.5762 0.4320 0.0142 -0.1154 -0.0605 281 PRO A CB 2236 C CG . PRO A 282 ? 0.3794 0.5691 0.4298 0.0174 -0.1317 -0.0606 281 PRO A CG 2237 C CD . PRO A 282 ? 0.3879 0.5588 0.4204 0.0131 -0.1366 -0.0522 281 PRO A CD 2238 N N . ILE A 283 ? 0.3855 0.6002 0.4356 0.0197 -0.1140 -0.0524 282 ILE A N 2239 C CA . ILE A 283 ? 0.4012 0.6229 0.4460 0.0280 -0.1084 -0.0549 282 ILE A CA 2240 C C . ILE A 283 ? 0.4105 0.6357 0.4447 0.0334 -0.1138 -0.0517 282 ILE A C 2241 O O . ILE A 283 ? 0.4199 0.6488 0.4426 0.0449 -0.1110 -0.0537 282 ILE A O 2242 C CB . ILE A 283 ? 0.4185 0.6436 0.4696 0.0330 -0.1161 -0.0680 282 ILE A CB 2243 C CG1 . ILE A 283 ? 0.4395 0.6554 0.4870 0.0336 -0.1358 -0.0713 282 ILE A CG1 2244 C CG2 . ILE A 283 ? 0.4085 0.6395 0.4759 0.0311 -0.1123 -0.0795 282 ILE A CG2 2245 C CD1 . ILE A 283 ? 0.4558 0.6721 0.5071 0.0414 -0.1467 -0.0852 282 ILE A CD1 2246 N N . GLY A 284 ? 0.4024 0.6276 0.4403 0.0260 -0.1206 -0.0501 283 GLY A N 2247 C CA . GLY A 284 ? 0.3988 0.6367 0.4364 0.0303 -0.1265 -0.0556 283 GLY A CA 2248 C C . GLY A 284 ? 0.3997 0.6357 0.4484 0.0151 -0.1321 -0.0617 283 GLY A C 2249 O O . GLY A 284 ? 0.4039 0.6192 0.4507 0.0046 -0.1338 -0.0602 283 GLY A O 2250 N N . ALA A 285 ? 0.3932 0.6488 0.4507 0.0156 -0.1338 -0.0713 284 ALA A N 2251 C CA . ALA A 285 ? 0.3971 0.6542 0.4694 -0.0029 -0.1326 -0.0822 284 ALA A CA 2252 C C . ALA A 285 ? 0.4100 0.6656 0.4904 -0.0085 -0.1383 -0.0980 284 ALA A C 2253 O O . ALA A 285 ? 0.4145 0.6774 0.4919 0.0057 -0.1467 -0.1020 284 ALA A O 2254 C CB . ALA A 285 ? 0.3885 0.6757 0.4746 0.0000 -0.1317 -0.0934 284 ALA A CB 2255 N N . ILE A 286 ? 0.4193 0.6624 0.5081 -0.0306 -0.1310 -0.1079 285 ILE A N 2256 C CA . ILE A 286 ? 0.4385 0.6712 0.5336 -0.0408 -0.1317 -0.1240 285 ILE A CA 2257 C C . ILE A 286 ? 0.4493 0.6971 0.5703 -0.0626 -0.1201 -0.1486 285 ILE A C 2258 O O . ILE A 286 ? 0.4541 0.6807 0.5706 -0.0833 -0.1044 -0.1456 285 ILE A O 2259 C CB . ILE A 286 ? 0.4689 0.6460 0.5355 -0.0500 -0.1281 -0.1111 285 ILE A CB 2260 C CG1 . ILE A 286 ? 0.4665 0.6353 0.5157 -0.0292 -0.1402 -0.0955 285 ILE A CG1 2261 C CG2 . ILE A 286 ? 0.5008 0.6581 0.5698 -0.0628 -0.1251 -0.1282 285 ILE A CG2 2262 C CD1 . ILE A 286 ? 0.4949 0.6135 0.5130 -0.0308 -0.1404 -0.0833 285 ILE A CD1 2263 N N . ASN A 287 ? 0.4531 0.7396 0.6023 -0.0579 -0.1269 -0.1763 286 ASN A N 2264 C CA . ASN A 287 ? 0.4738 0.7790 0.6566 -0.0817 -0.1144 -0.2096 286 ASN A CA 2265 C C . ASN A 287 ? 0.4979 0.7861 0.6862 -0.0921 -0.1127 -0.2260 286 ASN A C 2266 O O . ASN A 287 ? 0.4892 0.8132 0.6959 -0.0748 -0.1282 -0.2446 286 ASN A O 2267 C CB . ASN A 287 ? 0.4573 0.8309 0.6759 -0.0659 -0.1250 -0.2381 286 ASN A CB 2268 C CG . ASN A 287 ? 0.4744 0.8798 0.7392 -0.0920 -0.1109 -0.2816 286 ASN A CG 2269 O OD1 . ASN A 287 ? 0.5001 0.8706 0.7655 -0.1275 -0.0854 -0.2842 286 ASN A OD1 2270 N ND2 . ASN A 287 ? 0.4634 0.9340 0.7653 -0.0736 -0.1262 -0.3189 286 ASN A ND2 2271 N N . SER A 288 ? 0.5380 0.7658 0.7041 -0.1181 -0.0936 -0.2183 287 SER A N 2272 C CA . SER A 288 ? 0.5743 0.7701 0.7366 -0.1298 -0.0886 -0.2309 287 SER A CA 2273 C C . SER A 288 ? 0.6327 0.7740 0.7850 -0.1688 -0.0558 -0.2410 287 SER A C 2274 O O . SER A 288 ? 0.6495 0.7597 0.7807 -0.1839 -0.0381 -0.2272 287 SER A O 2275 C CB . SER A 288 ? 0.5839 0.7366 0.7038 -0.1096 -0.1034 -0.2016 287 SER A CB 2276 O OG . SER A 288 ? 0.6288 0.7328 0.7330 -0.1222 -0.0957 -0.2092 287 SER A OG 2277 N N . SER A 289 ? 0.6723 0.7977 0.8361 -0.1852 -0.0457 -0.2654 288 SER A N 2278 C CA . SER A 289 ? 0.7455 0.8046 0.8919 -0.2244 -0.0090 -0.2763 288 SER A CA 2279 C C . SER A 289 ? 0.8047 0.7733 0.8892 -0.2206 -0.0073 -0.2528 288 SER A C 2280 O O . SER A 289 ? 0.8857 0.7808 0.9406 -0.2495 0.0238 -0.2588 288 SER A O 2281 C CB . SER A 289 ? 0.7523 0.8570 0.9609 -0.2505 0.0071 -0.3292 288 SER A CB 2282 O OG . SER A 289 ? 0.7360 0.8685 0.9649 -0.2324 -0.0148 -0.3445 288 SER A OG 2283 N N . MET A 290 ? 0.7775 0.7487 0.8401 -0.1845 -0.0393 -0.2283 289 MET A N 2284 C CA . MET A 290 ? 0.8219 0.7152 0.8267 -0.1726 -0.0449 -0.2082 289 MET A CA 2285 C C . MET A 290 ? 0.8649 0.6722 0.8002 -0.1758 -0.0302 -0.1789 289 MET A C 2286 O O . MET A 290 ? 0.8428 0.6660 0.7758 -0.1741 -0.0288 -0.1647 289 MET A O 2287 C CB . MET A 290 ? 0.7838 0.7125 0.7891 -0.1329 -0.0823 -0.1933 289 MET A CB 2288 C CG . MET A 290 ? 0.7434 0.7503 0.8033 -0.1211 -0.1005 -0.2173 289 MET A CG 2289 S SD . MET A 290 ? 0.8071 0.7940 0.8813 -0.1365 -0.0927 -0.2491 289 MET A SD 2290 C CE . MET A 290 ? 0.7412 0.8196 0.8615 -0.1046 -0.1261 -0.2646 289 MET A CE 2291 N N . PRO A 291 ? 0.9327 0.6447 0.8059 -0.1773 -0.0201 -0.1702 290 PRO A N 2292 C CA . PRO A 291 ? 0.9844 0.6099 0.7790 -0.1689 -0.0128 -0.1411 290 PRO A CA 2293 C C . PRO A 291 ? 0.9361 0.5792 0.7112 -0.1264 -0.0497 -0.1168 290 PRO A C 2294 O O . PRO A 291 ? 0.9566 0.5655 0.6893 -0.1172 -0.0485 -0.0970 290 PRO A O 2295 C CB . PRO A 291 ? 1.0891 0.6053 0.8178 -0.1756 0.0047 -0.1413 290 PRO A CB 2296 C CG . PRO A 291 ? 1.0656 0.6217 0.8396 -0.1742 -0.0081 -0.1642 290 PRO A CG 2297 C CD . PRO A 291 ? 0.9780 0.6500 0.8450 -0.1880 -0.0112 -0.1888 290 PRO A CD 2298 N N . PHE A 292 ? 0.8716 0.5692 0.6791 -0.1019 -0.0801 -0.1216 291 PHE A N 2299 C CA . PHE A 292 ? 0.8271 0.5478 0.6253 -0.0647 -0.1120 -0.1062 291 PHE A CA 2300 C C . PHE A 292 ? 0.7288 0.5522 0.5938 -0.0550 -0.1298 -0.1123 291 PHE A C 2301 O O . PHE A 292 ? 0.6882 0.5639 0.6020 -0.0684 -0.1253 -0.1293 291 PHE A O 2302 C CB . PHE A 292 ? 0.8659 0.5388 0.6240 -0.0383 -0.1317 -0.1059 291 PHE A CB 2303 C CG . PHE A 292 ? 0.9703 0.5280 0.6471 -0.0398 -0.1166 -0.0982 291 PHE A CG 2304 C CD1 . PHE A 292 ? 1.0205 0.5186 0.6320 -0.0197 -0.1209 -0.0801 291 PHE A CD1 2305 C CD2 . PHE A 292 ? 1.0306 0.5345 0.6914 -0.0598 -0.0970 -0.1104 291 PHE A CD2 2306 C CE1 . PHE A 292 ? 1.1350 0.5143 0.6568 -0.0162 -0.1063 -0.0713 291 PHE A CE1 2307 C CE2 . PHE A 292 ? 1.1439 0.5269 0.7180 -0.0608 -0.0788 -0.1017 291 PHE A CE2 2308 C CZ . PHE A 292 ? 1.2008 0.5178 0.7005 -0.0373 -0.0837 -0.0807 291 PHE A CZ 2309 N N . HIS A 293 ? 0.6969 0.5447 0.5595 -0.0300 -0.1491 -0.1002 292 HIS A N 2310 C CA . HIS A 293 ? 0.6192 0.5482 0.5307 -0.0176 -0.1633 -0.1033 292 HIS A CA 2311 C C . HIS A 293 ? 0.6112 0.5424 0.5082 0.0115 -0.1843 -0.0972 292 HIS A C 2312 O O . HIS A 293 ? 0.6562 0.5347 0.5086 0.0232 -0.1893 -0.0903 292 HIS A O 2313 C CB . HIS A 293 ? 0.5774 0.5501 0.5180 -0.0309 -0.1515 -0.0992 292 HIS A CB 2314 C CG . HIS A 293 ? 0.5799 0.5383 0.4989 -0.0245 -0.1511 -0.0831 292 HIS A CG 2315 N ND1 . HIS A 293 ? 0.5358 0.5355 0.4718 -0.0078 -0.1622 -0.0778 292 HIS A ND1 2316 C CD2 . HIS A 293 ? 0.6225 0.5276 0.5024 -0.0321 -0.1399 -0.0730 292 HIS A CD2 2317 C CE1 . HIS A 293 ? 0.5502 0.5290 0.4646 -0.0051 -0.1600 -0.0672 292 HIS A CE1 2318 N NE2 . HIS A 293 ? 0.6060 0.5269 0.4835 -0.0179 -0.1478 -0.0630 292 HIS A NE2 2319 N N . ASN A 294 ? 0.5605 0.5503 0.4925 0.0242 -0.1955 -0.1030 293 ASN A N 2320 C CA . ASN A 294 ? 0.5530 0.5559 0.4830 0.0485 -0.2120 -0.1052 293 ASN A CA 2321 C C . ASN A 294 ? 0.4982 0.5607 0.4637 0.0501 -0.2082 -0.1038 293 ASN A C 2322 O O . ASN A 294 ? 0.4774 0.5671 0.4569 0.0648 -0.2164 -0.1126 293 ASN A O 2323 C CB . ASN A 294 ? 0.5678 0.5674 0.4956 0.0650 -0.2282 -0.1191 293 ASN A CB 2324 C CG . ASN A 294 ? 0.5351 0.5876 0.5010 0.0626 -0.2272 -0.1282 293 ASN A CG 2325 O OD1 . ASN A 294 ? 0.4980 0.5851 0.4875 0.0504 -0.2153 -0.1247 293 ASN A OD1 2326 N ND2 . ASN A 294 ? 0.5458 0.6025 0.5135 0.0777 -0.2410 -0.1414 293 ASN A ND2 2327 N N . ILE A 295 ? 0.4815 0.5611 0.4599 0.0344 -0.1935 -0.0949 294 ILE A N 2328 C CA . ILE A 295 ? 0.4456 0.5698 0.4489 0.0354 -0.1862 -0.0915 294 ILE A CA 2329 C C . ILE A 295 ? 0.4418 0.5662 0.4423 0.0440 -0.1885 -0.0902 294 ILE A C 2330 O O . ILE A 295 ? 0.4333 0.5863 0.4514 0.0530 -0.1890 -0.0984 294 ILE A O 2331 C CB . ILE A 295 ? 0.4348 0.5724 0.4477 0.0201 -0.1724 -0.0837 294 ILE A CB 2332 C CG1 . ILE A 295 ? 0.4431 0.5852 0.4641 0.0112 -0.1710 -0.0926 294 ILE A CG1 2333 C CG2 . ILE A 295 ? 0.4036 0.5780 0.4330 0.0249 -0.1645 -0.0796 294 ILE A CG2 2334 C CD1 . ILE A 295 ? 0.4349 0.6002 0.4670 0.0230 -0.1792 -0.1037 294 ILE A CD1 2335 N N . HIS A 296 ? 0.4622 0.5548 0.4408 0.0407 -0.1883 -0.0827 295 HIS A N 2336 C CA . HIS A 296 ? 0.4549 0.5535 0.4343 0.0479 -0.1895 -0.0827 295 HIS A CA 2337 C C . HIS A 296 ? 0.4982 0.5467 0.4382 0.0486 -0.1924 -0.0749 295 HIS A C 2338 O O . HIS A 296 ? 0.5133 0.5344 0.4370 0.0326 -0.1817 -0.0649 295 HIS A O 2339 C CB . HIS A 296 ? 0.4151 0.5488 0.4201 0.0366 -0.1732 -0.0757 295 HIS A CB 2340 C CG . HIS A 296 ? 0.4045 0.5606 0.4260 0.0434 -0.1716 -0.0832 295 HIS A CG 2341 N ND1 . HIS A 296 ? 0.4208 0.5621 0.4298 0.0505 -0.1787 -0.0856 295 HIS A ND1 2342 C CD2 . HIS A 296 ? 0.3837 0.5746 0.4328 0.0435 -0.1612 -0.0917 295 HIS A CD2 2343 C CE1 . HIS A 296 ? 0.4046 0.5778 0.4403 0.0545 -0.1749 -0.0986 295 HIS A CE1 2344 N NE2 . HIS A 296 ? 0.3800 0.5813 0.4403 0.0480 -0.1617 -0.1021 295 HIS A NE2 2345 N N . PRO A 297 ? 0.5195 0.5550 0.4425 0.0682 -0.2061 -0.0825 296 PRO A N 2346 C CA . PRO A 297 ? 0.5717 0.5507 0.4444 0.0751 -0.2098 -0.0747 296 PRO A CA 2347 C C . PRO A 297 ? 0.5615 0.5430 0.4339 0.0629 -0.1965 -0.0631 296 PRO A C 2348 O O . PRO A 297 ? 0.6117 0.5408 0.4384 0.0616 -0.1923 -0.0529 296 PRO A O 2349 C CB . PRO A 297 ? 0.5996 0.5719 0.4560 0.1084 -0.2347 -0.0932 296 PRO A CB 2350 C CG . PRO A 297 ? 0.5450 0.5878 0.4601 0.1105 -0.2365 -0.1114 296 PRO A CG 2351 C CD . PRO A 297 ? 0.5092 0.5763 0.4532 0.0889 -0.2211 -0.1038 296 PRO A CD 2352 N N . LEU A 298 ? 0.5074 0.5434 0.4251 0.0546 -0.1883 -0.0650 297 LEU A N 2353 C CA . LEU A 298 ? 0.4890 0.5328 0.4121 0.0418 -0.1749 -0.0546 297 LEU A CA 2354 C C . LEU A 298 ? 0.4711 0.5211 0.4059 0.0163 -0.1560 -0.0421 297 LEU A C 2355 O O . LEU A 298 ? 0.4320 0.5230 0.4018 0.0083 -0.1478 -0.0422 297 LEU A O 2356 C CB . LEU A 298 ? 0.4493 0.5425 0.4117 0.0468 -0.1744 -0.0654 297 LEU A CB 2357 C CG . LEU A 298 ? 0.4700 0.5706 0.4328 0.0726 -0.1942 -0.0879 297 LEU A CG 2358 C CD1 . LEU A 298 ? 0.4417 0.5883 0.4449 0.0727 -0.1887 -0.1024 297 LEU A CD1 2359 C CD2 . LEU A 298 ? 0.5258 0.5733 0.4330 0.0936 -0.2115 -0.0879 297 LEU A CD2 2360 N N . THR A 299 ? 0.5034 0.5096 0.4054 0.0051 -0.1481 -0.0340 298 THR A N 2361 C CA . THR A 299 ? 0.4833 0.4982 0.3998 -0.0187 -0.1309 -0.0303 298 THR A CA 2362 C C . THR A 299 ? 0.4879 0.4891 0.3920 -0.0323 -0.1166 -0.0226 298 THR A C 2363 O O . THR A 299 ? 0.5224 0.4849 0.3890 -0.0248 -0.1182 -0.0174 298 THR A O 2364 C CB . THR A 299 ? 0.5195 0.4986 0.4169 -0.0277 -0.1270 -0.0340 298 THR A CB 2365 O OG1 . THR A 299 ? 0.5798 0.4891 0.4212 -0.0268 -0.1231 -0.0283 298 THR A OG1 2366 C CG2 . THR A 299 ? 0.5123 0.5044 0.4204 -0.0128 -0.1424 -0.0423 298 THR A CG2 2367 N N . ILE A 300 ? 0.4604 0.4946 0.3949 -0.0496 -0.1037 -0.0241 299 ILE A N 2368 C CA . ILE A 300 ? 0.4751 0.4988 0.4022 -0.0673 -0.0869 -0.0211 299 ILE A CA 2369 C C . ILE A 300 ? 0.4740 0.5130 0.4239 -0.0896 -0.0723 -0.0330 299 ILE A C 2370 O O . ILE A 300 ? 0.4346 0.5166 0.4192 -0.0866 -0.0783 -0.0422 299 ILE A O 2371 C CB . ILE A 300 ? 0.4363 0.4959 0.3845 -0.0628 -0.0873 -0.0167 299 ILE A CB 2372 C CG1 . ILE A 300 ? 0.4600 0.5038 0.3950 -0.0795 -0.0706 -0.0141 299 ILE A CG1 2373 C CG2 . ILE A 300 ? 0.3854 0.4999 0.3765 -0.0601 -0.0897 -0.0217 299 ILE A CG2 2374 C CD1 . ILE A 300 ? 0.4329 0.5039 0.3823 -0.0740 -0.0716 -0.0096 299 ILE A CD1 2375 N N . GLY A 301 ? 0.5264 0.5290 0.4550 -0.1111 -0.0522 -0.0355 300 GLY A N 2376 C CA . GLY A 301 ? 0.5379 0.5574 0.4935 -0.1365 -0.0343 -0.0545 300 GLY A CA 2377 C C . GLY A 301 ? 0.6072 0.5689 0.5323 -0.1527 -0.0192 -0.0606 300 GLY A C 2378 O O . GLY A 301 ? 0.6628 0.5578 0.5323 -0.1449 -0.0192 -0.0464 300 GLY A O 2379 N N . GLU A 302 ? 0.6200 0.6053 0.5798 -0.1738 -0.0062 -0.0844 301 GLU A N 2380 C CA . GLU A 302 ? 0.6889 0.6215 0.6265 -0.1924 0.0111 -0.0946 301 GLU A CA 2381 C C . GLU A 302 ? 0.6786 0.6252 0.6274 -0.1734 -0.0116 -0.0973 301 GLU A C 2382 O O . GLU A 302 ? 0.6375 0.6451 0.6375 -0.1730 -0.0198 -0.1175 301 GLU A O 2383 C CB . GLU A 302 ? 0.7055 0.6602 0.6819 -0.2284 0.0401 -0.1264 301 GLU A CB 2384 C CG . GLU A 302 ? 0.7546 0.6748 0.7090 -0.2554 0.0728 -0.1269 301 GLU A CG 2385 C CD . GLU A 302 ? 0.8240 0.7103 0.7811 -0.2975 0.1140 -0.1545 301 GLU A CD 2386 O OE1 . GLU A 302 ? 0.8383 0.7151 0.8056 -0.3051 0.1169 -0.1704 301 GLU A OE1 2387 O OE2 . GLU A 302 ? 0.8659 0.7330 0.8144 -0.3249 0.1462 -0.1619 301 GLU A OE2 2388 N N . CYS A 303 ? 0.7222 0.6120 0.6208 -0.1552 -0.0229 -0.0791 302 CYS A N 2389 C CA . CYS A 303 ? 0.7041 0.6078 0.6101 -0.1328 -0.0473 -0.0794 302 CYS A CA 2390 C C . CYS A 303 ? 0.7651 0.5993 0.6310 -0.1381 -0.0397 -0.0824 302 CYS A C 2391 O O . CYS A 303 ? 0.8375 0.5955 0.6517 -0.1527 -0.0172 -0.0769 302 CYS A O 2392 C CB . CYS A 303 ? 0.6887 0.5959 0.5767 -0.1010 -0.0720 -0.0602 302 CYS A CB 2393 S SG . CYS A 303 ? 0.6278 0.6092 0.5592 -0.0933 -0.0797 -0.0560 302 CYS A SG 2394 N N . PRO A 304 ? 0.7432 0.5979 0.6275 -0.1250 -0.0574 -0.0906 303 PRO A N 2395 C CA . PRO A 304 ? 0.7981 0.5831 0.6363 -0.1194 -0.0584 -0.0891 303 PRO A CA 2396 C C . PRO A 304 ? 0.8253 0.5610 0.6056 -0.0888 -0.0764 -0.0678 303 PRO A C 2397 O O . PRO A 304 ? 0.7806 0.5467 0.5670 -0.0740 -0.0883 -0.0572 303 PRO A O 2398 C CB . PRO A 304 ? 0.7567 0.5944 0.6382 -0.1081 -0.0779 -0.1038 303 PRO A CB 2399 C CG . PRO A 304 ? 0.6859 0.6138 0.6316 -0.1114 -0.0821 -0.1153 303 PRO A CG 2400 C CD . PRO A 304 ? 0.6712 0.6094 0.6128 -0.1120 -0.0772 -0.1012 303 PRO A CD 2401 N N . LYS A 305 ? 0.8948 0.5558 0.6196 -0.0774 -0.0794 -0.0648 304 LYS A N 2402 C CA . LYS A 305 ? 0.9313 0.5456 0.5985 -0.0417 -0.1012 -0.0510 304 LYS A CA 2403 C C . LYS A 305 ? 0.8681 0.5405 0.5705 -0.0129 -0.1347 -0.0580 304 LYS A C 2404 O O . LYS A 305 ? 0.8557 0.5396 0.5778 -0.0138 -0.1400 -0.0695 304 LYS A O 2405 C CB . LYS A 305 ? 1.0533 0.5518 0.6344 -0.0376 -0.0899 -0.0457 304 LYS A CB 2406 C CG . LYS A 305 ? 1.1317 0.5599 0.6717 -0.0716 -0.0480 -0.0411 304 LYS A CG 2407 C CD . LYS A 305 ? 1.1292 0.5668 0.6599 -0.0728 -0.0414 -0.0287 304 LYS A CD 2408 C CE . LYS A 305 ? 1.2393 0.5731 0.6929 -0.0934 -0.0030 -0.0193 304 LYS A CE 2409 N NZ . LYS A 305 ? 1.2419 0.5759 0.6735 -0.0860 -0.0016 -0.0057 304 LYS A NZ 2410 N N . TYR A 306 ? 0.8233 0.5338 0.5361 0.0106 -0.1547 -0.0538 305 TYR A N 2411 C CA . TYR A 306 ? 0.7708 0.5380 0.5187 0.0354 -0.1816 -0.0636 305 TYR A CA 2412 C C . TYR A 306 ? 0.8217 0.5394 0.5252 0.0650 -0.2027 -0.0704 305 TYR A C 2413 O O . TYR A 306 ? 0.8952 0.5394 0.5310 0.0839 -0.2078 -0.0647 305 TYR A O 2414 C CB . TYR A 306 ? 0.7287 0.5440 0.4986 0.0497 -0.1925 -0.0619 305 TYR A CB 2415 C CG . TYR A 306 ? 0.6911 0.5606 0.4957 0.0728 -0.2149 -0.0761 305 TYR A CG 2416 C CD1 . TYR A 306 ? 0.6286 0.5665 0.4912 0.0628 -0.2116 -0.0821 305 TYR A CD1 2417 C CD2 . TYR A 306 ? 0.7267 0.5780 0.5038 0.1062 -0.2386 -0.0866 305 TYR A CD2 2418 C CE1 . TYR A 306 ? 0.5994 0.5829 0.4919 0.0800 -0.2259 -0.0966 305 TYR A CE1 2419 C CE2 . TYR A 306 ? 0.6901 0.5969 0.5061 0.1242 -0.2559 -0.1057 305 TYR A CE2 2420 C CZ . TYR A 306 ? 0.6283 0.5996 0.5022 0.1082 -0.2467 -0.1098 305 TYR A CZ 2421 O OH . TYR A 306 ? 0.6020 0.6247 0.5129 0.1219 -0.2574 -0.1298 305 TYR A OH 2422 N N . VAL A 307 ? 0.6892 0.6179 0.8465 0.1498 -0.1776 -0.2419 306 VAL A N 2423 C CA . VAL A 307 ? 0.6925 0.6140 0.8725 0.1583 -0.2021 -0.2668 306 VAL A CA 2424 C C . VAL A 307 ? 0.6635 0.6284 0.8865 0.1565 -0.1840 -0.2901 306 VAL A C 2425 O O . VAL A 307 ? 0.6510 0.6328 0.8565 0.1458 -0.1599 -0.2794 306 VAL A O 2426 C CB . VAL A 307 ? 0.7069 0.6170 0.8831 0.1545 -0.2150 -0.2709 306 VAL A CB 2427 C CG1 . VAL A 307 ? 0.7641 0.6043 0.8777 0.1474 -0.2290 -0.2558 306 VAL A CG1 2428 C CG2 . VAL A 307 ? 0.6824 0.6315 0.8647 0.1424 -0.1935 -0.2632 306 VAL A CG2 2429 N N . LYS A 308 ? 0.6711 0.6421 0.9492 0.1639 -0.1969 -0.3278 307 LYS A N 2430 C CA . LYS A 308 ? 0.6666 0.6722 0.9913 0.1505 -0.1633 -0.3655 307 LYS A CA 2431 C C . LYS A 308 ? 0.6801 0.6946 1.0060 0.1322 -0.1416 -0.3830 307 LYS A C 2432 O O . LYS A 308 ? 0.7043 0.7261 1.0354 0.1063 -0.0988 -0.4138 307 LYS A O 2433 C CB . LYS A 308 ? 0.6674 0.6851 1.0861 0.1642 -0.1822 -0.4155 307 LYS A CB 2434 C CG . LYS A 308 ? 0.6762 0.6674 1.0851 0.1825 -0.2169 -0.4007 307 LYS A CG 2435 C CD . LYS A 308 ? 0.6815 0.6924 1.2024 0.1944 -0.2373 -0.4593 307 LYS A CD 2436 C CE . LYS A 308 ? 0.7123 0.6755 1.2099 0.2143 -0.2898 -0.4439 307 LYS A CE 2437 N NZ . LYS A 308 ? 0.7187 0.7080 1.3431 0.2266 -0.3145 -0.5066 307 LYS A NZ 2438 N N . SER A 309 ? 0.6838 0.6851 0.9917 0.1392 -0.1660 -0.3657 308 SER A N 2439 C CA . SER A 309 ? 0.6987 0.7027 1.0085 0.1239 -0.1524 -0.3834 308 SER A CA 2440 C C . SER A 309 ? 0.7286 0.7205 0.9706 0.0922 -0.1148 -0.3751 308 SER A C 2441 O O . SER A 309 ? 0.7325 0.7098 0.9153 0.0901 -0.1194 -0.3377 308 SER A O 2442 C CB . SER A 309 ? 0.7036 0.6884 0.9861 0.1339 -0.1845 -0.3565 308 SER A CB 2443 O OG . SER A 309 ? 0.7133 0.6697 1.0097 0.1568 -0.2258 -0.3548 308 SER A OG 2444 N N . SER A 310 ? 0.7667 0.7510 1.0136 0.0654 -0.0807 -0.4146 309 SER A N 2445 C CA . SER A 310 ? 0.8399 0.7746 0.9852 0.0261 -0.0504 -0.4088 309 SER A CA 2446 C C . SER A 310 ? 0.8588 0.7720 0.9510 0.0257 -0.0805 -0.3775 309 SER A C 2447 O O . SER A 310 ? 0.9186 0.7784 0.9135 0.0059 -0.0886 -0.3529 309 SER A O 2448 C CB . SER A 310 ? 0.8961 0.8135 1.0533 -0.0151 0.0127 -0.4726 309 SER A CB 2449 O OG . SER A 310 ? 0.8697 0.8235 1.1264 -0.0049 0.0129 -0.5142 309 SER A OG 2450 N N . ARG A 311 ? 0.8233 0.7669 0.9754 0.0472 -0.1040 -0.3802 310 ARG A N 2451 C CA . ARG A 311 ? 0.8492 0.7782 0.9649 0.0444 -0.1280 -0.3581 310 ARG A CA 2452 C C . ARG A 311 ? 0.8033 0.7582 0.9687 0.0738 -0.1623 -0.3425 310 ARG A C 2453 O O . ARG A 311 ? 0.7815 0.7471 1.0050 0.0913 -0.1698 -0.3647 310 ARG A O 2454 C CB . ARG A 311 ? 0.9105 0.8140 1.0088 0.0146 -0.0986 -0.3947 310 ARG A CB 2455 C CG . ARG A 311 ? 1.0072 0.8522 1.0229 -0.0320 -0.0503 -0.4190 310 ARG A CG 2456 C CD . ARG A 311 ? 1.0777 0.8900 1.0746 -0.0684 -0.0101 -0.4624 310 ARG A CD 2457 N NE . ARG A 311 ? 1.2049 0.9327 1.0921 -0.1282 0.0492 -0.4913 310 ARG A NE 2458 C CZ . ARG A 311 ? 1.2969 0.9700 1.1369 -0.1778 0.1040 -0.5370 310 ARG A CZ 2459 N NH1 . ARG A 311 ? 1.2630 0.9704 1.1729 -0.1677 0.1016 -0.5583 310 ARG A NH1 2460 N NH2 . ARG A 311 ? 1.4381 1.0084 1.1482 -0.2434 0.1662 -0.5644 310 ARG A NH2 2461 N N . LEU A 312 ? 0.8094 0.7618 0.9490 0.0758 -0.1854 -0.3099 311 LEU A N 2462 C CA . LEU A 312 ? 0.7973 0.7528 0.9571 0.0874 -0.2047 -0.2997 311 LEU A CA 2463 C C . LEU A 312 ? 0.8204 0.7725 0.9605 0.0736 -0.2163 -0.2881 311 LEU A C 2464 O O . LEU A 312 ? 0.8196 0.7812 0.9613 0.0716 -0.2283 -0.2713 311 LEU A O 2465 C CB . LEU A 312 ? 0.7799 0.7383 0.9490 0.1003 -0.2098 -0.2806 311 LEU A CB 2466 C CG . LEU A 312 ? 0.7775 0.7234 0.9604 0.1165 -0.2132 -0.2899 311 LEU A CG 2467 C CD1 . LEU A 312 ? 0.7807 0.7131 0.9470 0.1192 -0.2116 -0.2688 311 LEU A CD1 2468 C CD2 . LEU A 312 ? 0.8012 0.7142 0.9946 0.1265 -0.2363 -0.3105 311 LEU A CD2 2469 N N . VAL A 313 ? 0.8463 0.7855 0.9809 0.0657 -0.2174 -0.3022 312 VAL A N 2470 C CA . VAL A 313 ? 0.8690 0.8019 0.9850 0.0502 -0.2300 -0.2960 312 VAL A CA 2471 C C . VAL A 313 ? 0.8718 0.7956 0.9983 0.0505 -0.2343 -0.2988 312 VAL A C 2472 O O . VAL A 313 ? 0.8830 0.7865 1.0073 0.0532 -0.2330 -0.3165 312 VAL A O 2473 C CB . VAL A 313 ? 0.9212 0.8253 0.9903 0.0288 -0.2221 -0.3117 312 VAL A CB 2474 C CG1 . VAL A 313 ? 0.9607 0.8477 0.9995 0.0126 -0.2478 -0.3016 312 VAL A CG1 2475 C CG2 . VAL A 313 ? 0.9508 0.8334 0.9791 0.0186 -0.2079 -0.3147 312 VAL A CG2 2476 N N . LEU A 314 ? 0.8694 0.8016 1.0105 0.0448 -0.2374 -0.2875 313 LEU A N 2477 C CA . LEU A 314 ? 0.8971 0.8024 1.0261 0.0333 -0.2339 -0.2915 313 LEU A CA 2478 C C . LEU A 314 ? 0.9165 0.8258 1.0430 0.0176 -0.2433 -0.2980 313 LEU A C 2479 O O . LEU A 314 ? 0.9167 0.8517 1.0642 0.0112 -0.2575 -0.2958 313 LEU A O 2480 C CB . LEU A 314 ? 0.9035 0.8081 1.0481 0.0203 -0.2155 -0.2885 313 LEU A CB 2481 C CG . LEU A 314 ? 0.9358 0.7850 1.0342 0.0218 -0.2036 -0.2841 313 LEU A CG 2482 C CD1 . LEU A 314 ? 0.9544 0.8011 1.0664 -0.0016 -0.1686 -0.2885 313 LEU A CD1 2483 C CD2 . LEU A 314 ? 1.0032 0.7706 1.0308 0.0173 -0.2169 -0.2875 313 LEU A CD2 2484 N N . ALA A 315 ? 0.9527 0.8260 1.0501 0.0127 -0.2437 -0.3070 314 ALA A N 2485 C CA . ALA A 315 ? 0.9784 0.8480 1.0667 -0.0052 -0.2499 -0.3138 314 ALA A CA 2486 C C . ALA A 315 ? 0.9984 0.8688 1.1028 -0.0260 -0.2407 -0.3150 314 ALA A C 2487 O O . ALA A 315 ? 1.0220 0.8552 1.1030 -0.0330 -0.2228 -0.3149 314 ALA A O 2488 C CB . ALA A 315 ? 1.0076 0.8368 1.0664 -0.0020 -0.2517 -0.3281 314 ALA A CB 2489 N N . THR A 316 ? 1.0041 0.9053 1.1437 -0.0405 -0.2531 -0.3209 315 THR A N 2490 C CA . THR A 316 ? 1.0222 0.9371 1.2070 -0.0656 -0.2389 -0.3363 315 THR A CA 2491 C C . THR A 316 ? 1.0603 0.9603 1.2291 -0.0849 -0.2488 -0.3461 315 THR A C 2492 O O . THR A 316 ? 1.0986 0.9713 1.2547 -0.1100 -0.2229 -0.3585 315 THR A O 2493 C CB . THR A 316 ? 0.9952 0.9718 1.2799 -0.0638 -0.2528 -0.3475 315 THR A CB 2494 O OG1 . THR A 316 ? 0.9979 0.9837 1.2820 -0.0493 -0.3042 -0.3391 315 THR A OG1 2495 C CG2 . THR A 316 ? 0.9705 0.9589 1.2753 -0.0518 -0.2307 -0.3428 315 THR A CG2 2496 N N . GLY A 317 ? 1.0675 0.9702 1.2203 -0.0790 -0.2830 -0.3417 316 GLY A N 2497 C CA . GLY A 317 ? 1.1048 0.9867 1.2322 -0.0979 -0.2957 -0.3501 316 GLY A CA 2498 C C . GLY A 317 ? 1.1315 0.9618 1.1817 -0.0960 -0.2817 -0.3480 316 GLY A C 2499 O O . GLY A 317 ? 1.1254 0.9334 1.1540 -0.0803 -0.2648 -0.3447 316 GLY A O 2500 N N . LEU A 318 ? 1.1741 0.9814 1.1901 -0.1114 -0.2943 -0.3546 317 LEU A N 2501 C CA . LEU A 318 ? 1.2075 0.9683 1.1686 -0.1118 -0.2802 -0.3628 317 LEU A CA 2502 C C . LEU A 318 ? 1.2258 0.9694 1.1505 -0.1082 -0.2767 -0.3686 317 LEU A C 2503 O O . LEU A 318 ? 1.2208 0.9738 1.1383 -0.1077 -0.2883 -0.3602 317 LEU A O 2504 C CB . LEU A 318 ? 1.2522 0.9902 1.1917 -0.1373 -0.2854 -0.3722 317 LEU A CB 2505 C CG . LEU A 318 ? 1.2609 0.9998 1.2243 -0.1541 -0.2740 -0.3767 317 LEU A CG 2506 C CD1 . LEU A 318 ? 1.2414 1.0368 1.2828 -0.1671 -0.2870 -0.3826 317 LEU A CD1 2507 C CD2 . LEU A 318 ? 1.3124 1.0068 1.2318 -0.1747 -0.2702 -0.3875 317 LEU A CD2 2508 N N . ARG A 319 ? 1.2594 0.9688 1.1600 -0.1099 -0.2576 -0.3888 318 ARG A N 2509 C CA . ARG A 319 ? 1.2965 0.9820 1.1675 -0.1187 -0.2339 -0.4103 318 ARG A CA 2510 C C . ARG A 319 ? 1.3781 1.0197 1.1666 -0.1559 -0.2416 -0.4089 318 ARG A C 2511 O O . ARG A 319 ? 1.4004 1.0381 1.1725 -0.1683 -0.2759 -0.3933 318 ARG A O 2512 C CB . ARG A 319 ? 1.3086 0.9723 1.2037 -0.1113 -0.2101 -0.4453 318 ARG A CB 2513 C CG . ARG A 319 ? 1.2641 0.9401 1.2253 -0.0728 -0.2198 -0.4518 318 ARG A CG 2514 C CD . ARG A 319 ? 1.2953 0.9351 1.2832 -0.0615 -0.2216 -0.4852 318 ARG A CD 2515 N NE . ARG A 319 ? 1.2812 0.9152 1.3369 -0.0219 -0.2423 -0.5042 318 ARG A NE 2516 C CZ . ARG A 319 ? 1.2648 0.9239 1.3989 -0.0066 -0.2258 -0.5438 318 ARG A CZ 2517 N NH1 . ARG A 319 ? 1.2679 0.9508 1.4053 -0.0352 -0.1745 -0.5691 318 ARG A NH1 2518 N NH2 . ARG A 319 ? 1.2580 0.9056 1.4613 0.0335 -0.2623 -0.5623 318 ARG A NH2 2519 N N . ASN A 320 ? 1.4429 1.0399 1.1751 -0.1781 -0.2094 -0.4303 319 ASN A N 2520 C CA . ASN A 320 ? 1.5624 1.0752 1.1735 -0.2244 -0.2104 -0.4346 319 ASN A CA 2521 C C . ASN A 320 ? 1.6358 1.0958 1.2063 -0.2564 -0.1423 -0.4821 319 ASN A C 2522 O O . ASN A 320 ? 1.7406 1.1236 1.2145 -0.2988 -0.1292 -0.4959 319 ASN A O 2523 C CB . ASN A 320 ? 1.6181 1.0877 1.1514 -0.2371 -0.2449 -0.4099 319 ASN A CB 2524 C CG . ASN A 320 ? 1.6224 1.0967 1.1573 -0.2300 -0.3233 -0.3782 319 ASN A CG 2525 O OD1 . ASN A 320 ? 1.6149 1.1045 1.1764 -0.2319 -0.3440 -0.3781 319 ASN A OD1 2526 N ND2 . ASN A 320 ? 1.6415 1.1011 1.1578 -0.2223 -0.3692 -0.3573 319 ASN A ND2 2527 N N . ILE B 10 ? 1.9276 1.9610 1.8995 -0.3955 -0.5962 -0.6329 10 ILE B N 2528 C CA . ILE B 10 ? 1.9245 1.9641 1.8859 -0.3885 -0.5883 -0.6395 10 ILE B CA 2529 C C . ILE B 10 ? 1.9205 1.9488 1.8675 -0.3766 -0.5785 -0.6559 10 ILE B C 2530 O O . ILE B 10 ? 1.9164 1.9415 1.8556 -0.3735 -0.5712 -0.6588 10 ILE B O 2531 C CB . ILE B 10 ? 1.9182 1.9819 1.8717 -0.3901 -0.5782 -0.6294 10 ILE B CB 2532 C CG1 . ILE B 10 ? 1.9221 2.0016 1.8900 -0.4029 -0.5875 -0.6113 10 ILE B CG1 2533 C CG2 . ILE B 10 ? 1.9160 1.9852 1.8602 -0.3834 -0.5720 -0.6359 10 ILE B CG2 2534 C CD1 . ILE B 10 ? 1.9172 2.0247 1.8796 -0.4044 -0.5799 -0.6012 10 ILE B CD1 2535 N N . GLU B 11 ? 1.9220 1.9455 1.8659 -0.3705 -0.5789 -0.6658 11 GLU B N 2536 C CA . GLU B 11 ? 1.9188 1.9348 1.8495 -0.3599 -0.5702 -0.6802 11 GLU B CA 2537 C C . GLU B 11 ? 1.9111 1.9376 1.8249 -0.3558 -0.5552 -0.6792 11 GLU B C 2538 O O . GLU B 11 ? 1.9062 1.9292 1.8108 -0.3521 -0.5478 -0.6828 11 GLU B O 2539 C CB . GLU B 11 ? 1.9228 1.9339 1.8547 -0.3549 -0.5748 -0.6899 11 GLU B CB 2540 N N . GLY B 12 ? 1.9096 1.9492 1.8198 -0.3563 -0.5517 -0.6742 12 GLY B N 2541 C CA . GLY B 12 ? 1.9039 1.9534 1.7983 -0.3513 -0.5393 -0.6740 12 GLY B CA 2542 C C . GLY B 12 ? 1.9028 1.9704 1.7971 -0.3537 -0.5380 -0.6655 12 GLY B C 2543 O O . GLY B 12 ? 1.9044 1.9791 1.8116 -0.3610 -0.5464 -0.6571 12 GLY B O 2544 N N . GLY B 13 ? 1.9003 1.9758 1.7800 -0.3474 -0.5283 -0.6677 13 GLY B N 2545 C CA . GLY B 13 ? 1.8999 1.9950 1.7772 -0.3475 -0.5261 -0.6611 13 GLY B CA 2546 C C . GLY B 13 ? 1.9022 1.9974 1.7786 -0.3446 -0.5272 -0.6660 13 GLY B C 2547 O O . GLY B 13 ? 1.9053 1.9856 1.7814 -0.3416 -0.5290 -0.6753 13 GLY B O 2548 N N . TRP B 14 ? 1.9017 2.0155 1.7775 -0.3452 -0.5262 -0.6598 14 TRP B N 2549 C CA . TRP B 14 ? 1.9038 2.0201 1.7789 -0.3428 -0.5273 -0.6634 14 TRP B CA 2550 C C . TRP B 14 ? 1.9037 2.0288 1.7627 -0.3340 -0.5184 -0.6677 14 TRP B C 2551 O O . TRP B 14 ? 1.9023 2.0460 1.7573 -0.3330 -0.5151 -0.6616 14 TRP B O 2552 C CB . TRP B 14 ? 1.9047 2.0361 1.7941 -0.3515 -0.5354 -0.6520 14 TRP B CB 2553 C CG . TRP B 14 ? 1.9074 2.0297 1.8139 -0.3609 -0.5467 -0.6466 14 TRP B CG 2554 C CD1 . TRP B 14 ? 1.9099 2.0100 1.8206 -0.3603 -0.5514 -0.6545 14 TRP B CD1 2555 C CD2 . TRP B 14 ? 1.9093 2.0449 1.8311 -0.3721 -0.5560 -0.6321 14 TRP B CD2 2556 N NE1 . TRP B 14 ? 1.9144 2.0112 1.8420 -0.3698 -0.5637 -0.6467 14 TRP B NE1 2557 C CE2 . TRP B 14 ? 1.9145 2.0322 1.8495 -0.3779 -0.5670 -0.6321 14 TRP B CE2 2558 C CE3 . TRP B 14 ? 1.9082 2.0707 1.8342 -0.3778 -0.5567 -0.6186 14 TRP B CE3 2559 C CZ2 . TRP B 14 ? 1.9199 2.0432 1.8722 -0.3900 -0.5795 -0.6186 14 TRP B CZ2 2560 C CZ3 . TRP B 14 ? 1.9132 2.0839 1.8564 -0.3905 -0.5682 -0.6042 14 TRP B CZ3 2561 C CH2 . TRP B 14 ? 1.9196 2.0694 1.8759 -0.3968 -0.5800 -0.6041 14 TRP B CH2 2562 N N . GLN B 15 ? 1.9069 2.0193 1.7568 -0.3272 -0.5154 -0.6784 15 GLN B N 2563 C CA . GLN B 15 ? 1.9083 2.0266 1.7438 -0.3190 -0.5090 -0.6831 15 GLN B CA 2564 C C . GLN B 15 ? 1.9105 2.0458 1.7495 -0.3197 -0.5108 -0.6788 15 GLN B C 2565 O O . GLN B 15 ? 1.9087 2.0561 1.7376 -0.3137 -0.5065 -0.6796 15 GLN B O 2566 C CB . GLN B 15 ? 1.9099 2.0106 1.7360 -0.3130 -0.5063 -0.6944 15 GLN B CB 2567 C CG . GLN B 15 ? 1.9102 1.9970 1.7294 -0.3109 -0.5033 -0.6986 15 GLN B CG 2568 C CD . GLN B 15 ? 1.9124 1.9876 1.7191 -0.3045 -0.4997 -0.7077 15 GLN B CD 2569 O OE1 . GLN B 15 ? 1.9124 1.9861 1.7186 -0.3027 -0.5006 -0.7122 15 GLN B OE1 2570 N NE2 . GLN B 15 ? 1.9135 1.9808 1.7103 -0.3016 -0.4963 -0.7098 15 GLN B NE2 2571 N N . GLY B 16 ? 1.9149 2.0509 1.7682 -0.3269 -0.5181 -0.6747 16 GLY B N 2572 C CA . GLY B 16 ? 1.9189 2.0714 1.7776 -0.3293 -0.5210 -0.6691 16 GLY B CA 2573 C C . GLY B 16 ? 1.9202 2.0995 1.7795 -0.3314 -0.5196 -0.6584 16 GLY B C 2574 O O . GLY B 16 ? 1.9211 2.1173 1.7758 -0.3279 -0.5173 -0.6572 16 GLY B O 2575 N N . MET B 17 ? 1.9227 2.1075 1.7875 -0.3366 -0.5209 -0.6507 17 MET B N 2576 C CA . MET B 17 ? 1.9241 2.1377 1.7899 -0.3386 -0.5196 -0.6400 17 MET B CA 2577 C C . MET B 17 ? 1.9232 2.1429 1.7719 -0.3275 -0.5110 -0.6462 17 MET B C 2578 O O . MET B 17 ? 1.9238 2.1343 1.7678 -0.3255 -0.5083 -0.6486 17 MET B O 2579 C CB . MET B 17 ? 1.9256 2.1439 1.8049 -0.3493 -0.5253 -0.6284 17 MET B CB 2580 C CG . MET B 17 ? 1.9250 2.1772 1.8070 -0.3526 -0.5247 -0.6156 17 MET B CG 2581 S SD . MET B 17 ? 1.9273 2.1878 1.8287 -0.3683 -0.5340 -0.5987 17 MET B SD 2582 C CE . MET B 17 ? 1.9270 2.1576 1.8244 -0.3658 -0.5319 -0.6072 17 MET B CE 2583 N N . VAL B 18 ? 1.9241 2.1590 1.7638 -0.3200 -0.5076 -0.6491 18 VAL B N 2584 C CA . VAL B 18 ? 1.9253 2.1685 1.7492 -0.3085 -0.5015 -0.6551 18 VAL B CA 2585 C C . VAL B 18 ? 1.9248 2.2052 1.7499 -0.3077 -0.5009 -0.6462 18 VAL B C 2586 O O . VAL B 18 ? 1.9257 2.2180 1.7381 -0.2969 -0.4971 -0.6514 18 VAL B O 2587 C CB . VAL B 18 ? 1.9276 2.1605 1.7385 -0.2983 -0.4986 -0.6668 18 VAL B CB 2588 N N . ASP B 19 ? 1.9239 2.2234 1.7643 -0.3190 -0.5057 -0.6328 19 ASP B N 2589 C CA . ASP B 19 ? 1.9225 2.2624 1.7658 -0.3199 -0.5058 -0.6222 19 ASP B CA 2590 C C . ASP B 19 ? 1.9219 2.2748 1.7621 -0.3179 -0.5034 -0.6190 19 ASP B C 2591 O O . ASP B 19 ? 1.9234 2.2967 1.7524 -0.3070 -0.4994 -0.6230 19 ASP B O 2592 C CB . ASP B 19 ? 1.9208 2.2767 1.7826 -0.3346 -0.5131 -0.6068 19 ASP B CB 2593 C CG . ASP B 19 ? 1.9209 2.2706 1.7857 -0.3359 -0.5158 -0.6091 19 ASP B CG 2594 O OD1 . ASP B 19 ? 1.9201 2.2724 1.7728 -0.3249 -0.5113 -0.6187 19 ASP B OD1 2595 O OD2 . ASP B 19 ? 1.9201 2.2623 1.7999 -0.3478 -0.5234 -0.6013 19 ASP B OD2 2596 N N . GLY B 20 ? 1.9211 2.2620 1.7713 -0.3278 -0.5065 -0.6125 20 GLY B N 2597 C CA . GLY B 20 ? 1.9198 2.2710 1.7685 -0.3273 -0.5046 -0.6088 20 GLY B CA 2598 C C . GLY B 20 ? 1.9195 2.2360 1.7686 -0.3298 -0.5048 -0.6137 20 GLY B C 2599 O O . GLY B 20 ? 1.9201 2.2054 1.7659 -0.3278 -0.5046 -0.6234 20 GLY B O 2600 N N . TRP B 21 ? 1.9193 2.2431 1.7726 -0.3342 -0.5052 -0.6068 21 TRP B N 2601 C CA . TRP B 21 ? 1.9199 2.2135 1.7744 -0.3371 -0.5056 -0.6104 21 TRP B CA 2602 C C . TRP B 21 ? 1.9208 2.2027 1.7934 -0.3517 -0.5135 -0.6012 21 TRP B C 2603 O O . TRP B 21 ? 1.9216 2.1722 1.7956 -0.3529 -0.5154 -0.6084 21 TRP B O 2604 C CB . TRP B 21 ? 1.9185 2.2231 1.7682 -0.3339 -0.5025 -0.6085 21 TRP B CB 2605 C CG . TRP B 21 ? 1.9200 2.2192 1.7507 -0.3185 -0.4963 -0.6219 21 TRP B CG 2606 C CD1 . TRP B 21 ? 1.9221 2.1931 1.7410 -0.3101 -0.4939 -0.6355 21 TRP B CD1 2607 C CD2 . TRP B 21 ? 1.9198 2.2419 1.7415 -0.3098 -0.4931 -0.6226 21 TRP B CD2 2608 N NE1 . TRP B 21 ? 1.9240 2.1973 1.7277 -0.2974 -0.4904 -0.6442 21 TRP B NE1 2609 C CE2 . TRP B 21 ? 1.9231 2.2271 1.7279 -0.2961 -0.4899 -0.6373 21 TRP B CE2 2610 C CE3 . TRP B 21 ? 1.9184 2.2758 1.7448 -0.3120 -0.4934 -0.6121 21 TRP B CE3 2611 C CZ2 . TRP B 21 ? 1.9272 2.2449 1.7197 -0.2840 -0.4878 -0.6429 21 TRP B CZ2 2612 C CZ3 . TRP B 21 ? 1.9210 2.2948 1.7349 -0.2994 -0.4901 -0.6180 21 TRP B CZ3 2613 C CH2 . TRP B 21 ? 1.9256 2.2784 1.7227 -0.2852 -0.4878 -0.6338 21 TRP B CH2 2614 N N . TYR B 22 ? 1.9214 2.2292 1.8076 -0.3625 -0.5190 -0.5855 22 TYR B N 2615 C CA . TYR B 22 ? 1.9240 2.2219 1.8286 -0.3770 -0.5291 -0.5754 22 TYR B CA 2616 C C . TYR B 22 ? 1.9258 2.2388 1.8398 -0.3835 -0.5352 -0.5674 22 TYR B C 2617 O O . TYR B 22 ? 1.9235 2.2643 1.8321 -0.3789 -0.5314 -0.5653 22 TYR B O 2618 C CB . TYR B 22 ? 1.9237 2.2372 1.8390 -0.3872 -0.5333 -0.5610 22 TYR B CB 2619 C CG . TYR B 22 ? 1.9198 2.2381 1.8240 -0.3796 -0.5256 -0.5650 22 TYR B CG 2620 C CD1 . TYR B 22 ? 1.9190 2.2057 1.8168 -0.3750 -0.5228 -0.5759 22 TYR B CD1 2621 C CD2 . TYR B 22 ? 1.9176 2.2738 1.8179 -0.3768 -0.5217 -0.5579 22 TYR B CD2 2622 C CE1 . TYR B 22 ? 1.9167 2.2070 1.8046 -0.3683 -0.5165 -0.5794 22 TYR B CE1 2623 C CE2 . TYR B 22 ? 1.9158 2.2763 1.8059 -0.3691 -0.5155 -0.5623 22 TYR B CE2 2624 C CZ . TYR B 22 ? 1.9157 2.2421 1.7998 -0.3651 -0.5131 -0.5729 22 TYR B CZ 2625 O OH . TYR B 22 ? 1.9148 2.2447 1.7890 -0.3577 -0.5077 -0.5770 22 TYR B OH 2626 N N . GLY B 23 ? 1.9303 2.2254 1.8587 -0.3938 -0.5453 -0.5631 23 GLY B N 2627 C CA . GLY B 23 ? 1.9343 2.2411 1.8733 -0.4014 -0.5529 -0.5547 23 GLY B CA 2628 C C . GLY B 23 ? 1.9414 2.2211 1.8951 -0.4106 -0.5654 -0.5536 23 GLY B C 2629 O O . GLY B 23 ? 1.9428 2.1989 1.9017 -0.4137 -0.5699 -0.5559 23 GLY B O 2630 N N . TYR B 24 ? 1.9460 2.2297 1.9062 -0.4144 -0.5714 -0.5505 24 TYR B N 2631 C CA . TYR B 24 ? 1.9545 2.2154 1.9298 -0.4231 -0.5854 -0.5488 24 TYR B CA 2632 C C . TYR B 24 ? 1.9573 2.2004 1.9264 -0.4148 -0.5839 -0.5630 24 TYR B C 2633 O O . TYR B 24 ? 1.9530 2.2107 1.9108 -0.4069 -0.5750 -0.5674 24 TYR B O 2634 C CB . TYR B 24 ? 1.9592 2.2436 1.9522 -0.4389 -0.5981 -0.5278 24 TYR B CB 2635 C CG . TYR B 24 ? 1.9566 2.2702 1.9556 -0.4480 -0.5990 -0.5103 24 TYR B CG 2636 C CD1 . TYR B 24 ? 1.9498 2.3008 1.9392 -0.4435 -0.5881 -0.5053 24 TYR B CD1 2637 C CD2 . TYR B 24 ? 1.9624 2.2676 1.9770 -0.4609 -0.6116 -0.4987 24 TYR B CD2 2638 C CE1 . TYR B 24 ? 1.9480 2.3290 1.9429 -0.4515 -0.5889 -0.4893 24 TYR B CE1 2639 C CE2 . TYR B 24 ? 1.9605 2.2941 1.9810 -0.4699 -0.6127 -0.4818 24 TYR B CE2 2640 C CZ . TYR B 24 ? 1.9528 2.3254 1.9634 -0.4652 -0.6010 -0.4771 24 TYR B CZ 2641 O OH . TYR B 24 ? 1.9508 2.3544 1.9671 -0.4737 -0.6020 -0.4604 24 TYR B OH 2642 N N . HIS B 25 ? 1.9653 2.1775 1.9417 -0.4160 -0.5930 -0.5705 25 HIS B N 2643 C CA . HIS B 25 ? 1.9703 2.1679 1.9457 -0.4114 -0.5957 -0.5807 25 HIS B CA 2644 C C . HIS B 25 ? 1.9814 2.1708 1.9767 -0.4235 -0.6142 -0.5716 25 HIS B C 2645 O O . HIS B 25 ? 1.9875 2.1543 1.9925 -0.4272 -0.6248 -0.5735 25 HIS B O 2646 C CB . HIS B 25 ? 1.9691 2.1374 1.9338 -0.3994 -0.5900 -0.6007 25 HIS B CB 2647 C CG . HIS B 25 ? 1.9728 2.1254 1.9386 -0.3953 -0.5946 -0.6111 25 HIS B CG 2648 N ND1 . HIS B 25 ? 1.9686 2.1303 1.9244 -0.3884 -0.5870 -0.6163 25 HIS B ND1 2649 C CD2 . HIS B 25 ? 1.9800 2.1092 1.9558 -0.3965 -0.6067 -0.6174 25 HIS B CD2 2650 C CE1 . HIS B 25 ? 1.9728 2.1177 1.9324 -0.3861 -0.5936 -0.6251 25 HIS B CE1 2651 N NE2 . HIS B 25 ? 1.9801 2.1055 1.9517 -0.3905 -0.6057 -0.6263 25 HIS B NE2 2652 N N . HIS B 26 ? 1.9859 2.1936 1.9874 -0.4294 -0.6191 -0.5619 26 HIS B N 2653 C CA . HIS B 26 ? 1.9983 2.1985 2.0188 -0.4413 -0.6381 -0.5524 26 HIS B CA 2654 C C . HIS B 26 ? 2.0028 2.1785 2.0226 -0.4342 -0.6426 -0.5675 26 HIS B C 2655 O O . HIS B 26 ? 1.9978 2.1732 2.0031 -0.4225 -0.6303 -0.5804 26 HIS B O 2656 C CB . HIS B 26 ? 2.0004 2.2349 2.0297 -0.4531 -0.6427 -0.5319 26 HIS B CB 2657 C CG . HIS B 26 ? 1.9954 2.2475 2.0147 -0.4463 -0.6334 -0.5356 26 HIS B CG 2658 N ND1 . HIS B 26 ? 2.0007 2.2464 2.0266 -0.4485 -0.6422 -0.5364 26 HIS B ND1 2659 C CD2 . HIS B 26 ? 1.9852 2.2606 1.9885 -0.4371 -0.6168 -0.5390 26 HIS B CD2 2660 C CE1 . HIS B 26 ? 1.9942 2.2589 2.0085 -0.4412 -0.6307 -0.5398 26 HIS B CE1 2661 N NE2 . HIS B 26 ? 1.9854 2.2681 1.9859 -0.4339 -0.6157 -0.5417 26 HIS B NE2 2662 N N . SER B 27 ? 2.0142 2.1690 2.0498 -0.4412 -0.6611 -0.5661 27 SER B N 2663 C CA . SER B 27 ? 2.0194 2.1543 2.0581 -0.4365 -0.6693 -0.5778 27 SER B CA 2664 C C . SER B 27 ? 2.0287 2.1693 2.0864 -0.4511 -0.6886 -0.5613 27 SER B C 2665 O O . SER B 27 ? 2.0369 2.1771 2.1095 -0.4638 -0.7027 -0.5469 27 SER B O 2666 C CB . SER B 27 ? 2.0259 2.1274 2.0657 -0.4291 -0.6757 -0.5944 27 SER B CB 2667 O OG . SER B 27 ? 2.0329 2.1173 2.0739 -0.4225 -0.6823 -0.6076 27 SER B OG 2668 N N . ASN B 28 ? 2.0276 2.1736 2.0849 -0.4498 -0.6897 -0.5625 28 ASN B N 2669 C CA . ASN B 28 ? 2.0340 2.1917 2.1079 -0.4643 -0.7060 -0.5446 28 ASN B CA 2670 C C . ASN B 28 ? 2.0391 2.1855 2.1149 -0.4603 -0.7127 -0.5532 28 ASN B C 2671 O O . ASN B 28 ? 2.0326 2.1721 2.0940 -0.4462 -0.7002 -0.5709 28 ASN B O 2672 C CB . ASN B 28 ? 2.0246 2.2233 2.0957 -0.4718 -0.6964 -0.5262 28 ASN B CB 2673 C CG . ASN B 28 ? 2.0332 2.2485 2.1244 -0.4915 -0.7145 -0.5011 28 ASN B CG 2674 O OD1 . ASN B 28 ? 2.0449 2.2415 2.1517 -0.5011 -0.7332 -0.4946 28 ASN B OD1 2675 N ND2 . ASN B 28 ? 2.0286 2.2802 2.1195 -0.4977 -0.7097 -0.4862 28 ASN B ND2 2676 N N . GLU B 29 ? 2.0513 2.1961 2.1452 -0.4734 -0.7333 -0.5398 29 GLU B N 2677 C CA . GLU B 29 ? 2.0578 2.1941 2.1558 -0.4718 -0.7421 -0.5450 29 GLU B CA 2678 C C . GLU B 29 ? 2.0454 2.2081 2.1303 -0.4666 -0.7250 -0.5452 29 GLU B C 2679 O O . GLU B 29 ? 2.0453 2.1985 2.1252 -0.4581 -0.7235 -0.5579 29 GLU B O 2680 C CB . GLU B 29 ? 2.0743 2.2069 2.1954 -0.4891 -0.7688 -0.5270 29 GLU B CB 2681 C CG . GLU B 29 ? 2.0729 2.2419 2.2028 -0.5065 -0.7713 -0.4991 29 GLU B CG 2682 C CD . GLU B 29 ? 2.0693 2.2520 2.2024 -0.5152 -0.7696 -0.4851 29 GLU B CD 2683 O OE1 . GLU B 29 ? 2.0754 2.2328 2.2131 -0.5143 -0.7777 -0.4911 29 GLU B OE1 2684 O OE2 . GLU B 29 ? 2.0595 2.2798 2.1906 -0.5226 -0.7604 -0.4681 29 GLU B OE2 2685 N N . GLN B 30 ? 2.0346 2.2311 2.1140 -0.4711 -0.7126 -0.5314 30 GLN B N 2686 C CA . GLN B 30 ? 2.0221 2.2462 2.0882 -0.4651 -0.6959 -0.5318 30 GLN B CA 2687 C C . GLN B 30 ? 2.0095 2.2250 2.0540 -0.4465 -0.6753 -0.5535 30 GLN B C 2688 O O . GLN B 30 ? 2.0073 2.2186 2.0423 -0.4366 -0.6685 -0.5660 30 GLN B O 2689 C CB . GLN B 30 ? 2.0157 2.2808 2.0833 -0.4752 -0.6907 -0.5105 30 GLN B CB 2690 C CG . GLN B 30 ? 2.0256 2.3073 2.1138 -0.4947 -0.7098 -0.4863 30 GLN B CG 2691 C CD . GLN B 30 ? 2.0223 2.3390 2.1158 -0.5068 -0.7089 -0.4643 30 GLN B CD 2692 O OE1 . GLN B 30 ? 2.0242 2.3328 2.1216 -0.5105 -0.7120 -0.4611 30 GLN B OE1 2693 N NE2 . GLN B 30 ? 2.0175 2.3751 2.1115 -0.5130 -0.7050 -0.4489 30 GLN B NE2 2694 N N . GLY B 31 ? 2.0014 2.2144 2.0384 -0.4422 -0.6663 -0.5573 31 GLY B N 2695 C CA . GLY B 31 ? 1.9912 2.1951 2.0084 -0.4259 -0.6483 -0.5764 31 GLY B CA 2696 C C . GLY B 31 ? 1.9881 2.1823 2.0019 -0.4239 -0.6440 -0.5795 31 GLY B C 2697 O O . GLY B 31 ? 1.9970 2.1838 2.0245 -0.4338 -0.6567 -0.5704 31 GLY B O 2698 N N . SER B 32 ? 1.9772 2.1709 1.9729 -0.4113 -0.6268 -0.5921 32 SER B N 2699 C CA . SER B 32 ? 1.9711 2.1574 1.9615 -0.4084 -0.6208 -0.5954 32 SER B CA 2700 C C . SER B 32 ? 1.9596 2.1599 1.9304 -0.3977 -0.6017 -0.6016 32 SER B C 2701 O O . SER B 32 ? 1.9538 2.1511 1.9118 -0.3871 -0.5926 -0.6137 32 SER B O 2702 C CB . SER B 32 ? 1.9751 2.1275 1.9664 -0.4025 -0.6259 -0.6109 32 SER B CB 2703 O OG . SER B 32 ? 1.9701 2.1121 1.9467 -0.3890 -0.6153 -0.6285 32 SER B OG 2704 N N . GLY B 33 ? 1.9569 2.1718 1.9257 -0.4003 -0.5967 -0.5934 33 GLY B N 2705 C CA . GLY B 33 ? 1.9490 2.1769 1.8999 -0.3901 -0.5805 -0.5990 33 GLY B CA 2706 C C . GLY B 33 ? 1.9465 2.1836 1.8972 -0.3931 -0.5775 -0.5917 33 GLY B C 2707 O O . GLY B 33 ? 1.9512 2.1862 1.9160 -0.4041 -0.5878 -0.5811 33 GLY B O 2708 N N . TYR B 34 ? 1.9400 2.1868 1.8747 -0.3833 -0.5642 -0.5975 34 TYR B N 2709 C CA . TYR B 34 ? 1.9362 2.1918 1.8682 -0.3840 -0.5599 -0.5927 34 TYR B CA 2710 C C . TYR B 34 ? 1.9347 2.2300 1.8676 -0.3877 -0.5576 -0.5784 34 TYR B C 2711 O O . TYR B 34 ? 1.9347 2.2508 1.8646 -0.3855 -0.5554 -0.5762 34 TYR B O 2712 C CB . TYR B 34 ? 1.9306 2.1718 1.8445 -0.3706 -0.5480 -0.6081 34 TYR B CB 2713 C CG . TYR B 34 ? 1.9318 2.1384 1.8435 -0.3661 -0.5492 -0.6222 34 TYR B CG 2714 C CD1 . TYR B 34 ? 1.9333 2.1198 1.8505 -0.3692 -0.5533 -0.6241 34 TYR B CD1 2715 C CD2 . TYR B 34 ? 1.9316 2.1276 1.8358 -0.3587 -0.5465 -0.6335 34 TYR B CD2 2716 C CE1 . TYR B 34 ? 1.9352 2.0939 1.8503 -0.3645 -0.5545 -0.6372 34 TYR B CE1 2717 C CE2 . TYR B 34 ? 1.9331 2.1016 1.8354 -0.3544 -0.5476 -0.6460 34 TYR B CE2 2718 C CZ . TYR B 34 ? 1.9350 2.0859 1.8428 -0.3571 -0.5516 -0.6480 34 TYR B CZ 2719 O OH . TYR B 34 ? 1.9370 2.0642 1.8427 -0.3522 -0.5527 -0.6607 34 TYR B OH 2720 N N . ALA B 35 ? 1.9340 2.2416 1.8711 -0.3932 -0.5582 -0.5687 35 ALA B N 2721 C CA . ALA B 35 ? 1.9316 2.2807 1.8702 -0.3970 -0.5564 -0.5544 35 ALA B CA 2722 C C . ALA B 35 ? 1.9292 2.2857 1.8641 -0.3960 -0.5518 -0.5518 35 ALA B C 2723 O O . ALA B 35 ? 1.9302 2.2751 1.8759 -0.4052 -0.5587 -0.5451 35 ALA B O 2724 C CB . ALA B 35 ? 1.9361 2.3030 1.8942 -0.4134 -0.5692 -0.5352 35 ALA B CB 2725 N N . ALA B 36 ? 1.9263 2.3018 1.8460 -0.3843 -0.5411 -0.5574 36 ALA B N 2726 C CA . ALA B 36 ? 1.9248 2.3081 1.8390 -0.3810 -0.5360 -0.5568 36 ALA B CA 2727 C C . ALA B 36 ? 1.9254 2.3478 1.8509 -0.3920 -0.5403 -0.5370 36 ALA B C 2728 O O . ALA B 36 ? 1.9253 2.3821 1.8547 -0.3951 -0.5418 -0.5270 36 ALA B O 2729 C CB . ALA B 36 ? 1.9217 2.3104 1.8156 -0.3637 -0.5247 -0.5709 36 ALA B CB 2730 N N . ASP B 37 ? 1.9262 2.3448 1.8571 -0.3979 -0.5424 -0.5311 37 ASP B N 2731 C CA . ASP B 37 ? 1.9260 2.3822 1.8672 -0.4084 -0.5462 -0.5119 37 ASP B CA 2732 C C . ASP B 37 ? 1.9233 2.4122 1.8502 -0.3959 -0.5358 -0.5154 37 ASP B C 2733 O O . ASP B 37 ? 1.9216 2.3972 1.8378 -0.3869 -0.5295 -0.5256 37 ASP B O 2734 C CB . ASP B 37 ? 1.9272 2.3646 1.8800 -0.4195 -0.5532 -0.5046 37 ASP B CB 2735 C CG . ASP B 37 ? 1.9273 2.4030 1.8927 -0.4326 -0.5588 -0.4828 37 ASP B CG 2736 O OD1 . ASP B 37 ? 1.9259 2.4429 1.8946 -0.4361 -0.5595 -0.4707 37 ASP B OD1 2737 O OD2 . ASP B 37 ? 1.9287 2.3944 1.9009 -0.4396 -0.5626 -0.4772 37 ASP B OD2 2738 N N . LYS B 38 ? 1.6066 1.9182 1.5666 -0.0162 -0.2641 -0.4042 38 LYS B N 2739 C CA . LYS B 38 ? 1.5695 1.8448 1.5915 0.0196 -0.2871 -0.3579 38 LYS B CA 2740 C C . LYS B 38 ? 1.4542 1.7596 1.5714 0.0611 -0.2257 -0.3751 38 LYS B C 2741 O O . LYS B 38 ? 1.4308 1.7218 1.5755 0.0715 -0.2149 -0.3561 38 LYS B O 2742 C CB . LYS B 38 ? 1.5930 1.8330 1.7090 0.0382 -0.3666 -0.3353 38 LYS B CB 2743 C CG . LYS B 38 ? 1.7486 1.9241 1.7635 -0.0212 -0.4696 -0.2888 38 LYS B CG 2744 N N . GLU B 39 ? 1.4050 1.7441 1.5706 0.0708 -0.1968 -0.4085 39 GLU B N 2745 C CA . GLU B 39 ? 1.3434 1.6879 1.5661 0.0779 -0.1660 -0.4065 39 GLU B CA 2746 C C . GLU B 39 ? 1.3414 1.6816 1.5276 0.0677 -0.1397 -0.4002 39 GLU B C 2747 O O . GLU B 39 ? 1.3242 1.6470 1.5088 0.0603 -0.1246 -0.3746 39 GLU B O 2748 C CB . GLU B 39 ? 1.3210 1.6806 1.6144 0.0787 -0.1764 -0.4292 39 GLU B CB 2749 N N . SER B 40 ? 1.3724 1.7346 1.5334 0.0553 -0.1278 -0.4358 40 SER B N 2750 C CA . SER B 40 ? 1.3708 1.7407 1.5296 0.0436 -0.0983 -0.4506 40 SER B CA 2751 C C . SER B 40 ? 1.4169 1.7687 1.4559 0.0231 -0.0843 -0.4213 40 SER B C 2752 O O . SER B 40 ? 1.4004 1.7454 1.4340 0.0215 -0.0629 -0.4110 40 SER B O 2753 C CB . SER B 40 ? 1.3883 1.8102 1.6216 0.0259 -0.0756 -0.5378 40 SER B CB 2754 O OG . SER B 40 ? 1.4700 1.9198 1.5974 -0.0205 -0.0542 -0.5769 40 SER B OG 2755 N N . THR B 41 ? 1.4901 1.8233 1.4385 0.0008 -0.1129 -0.4007 41 THR B N 2756 C CA . THR B 41 ? 1.5639 1.8573 1.4039 -0.0299 -0.1327 -0.3554 41 THR B CA 2757 C C . THR B 41 ? 1.5135 1.7732 1.4170 0.0111 -0.1502 -0.3095 41 THR B C 2758 O O . THR B 41 ? 1.5291 1.7666 1.3928 0.0024 -0.1454 -0.2831 41 THR B O 2759 C CB . THR B 41 ? 1.6949 1.9516 1.4254 -0.0860 -0.1973 -0.3294 41 THR B CB 2760 O OG1 . THR B 41 ? 1.7733 2.0727 1.4187 -0.1538 -0.1616 -0.3911 41 THR B OG1 2761 C CG2 . THR B 41 ? 1.7979 1.9889 1.4232 -0.1313 -0.2512 -0.2639 41 THR B CG2 2762 N N . GLN B 42 ? 1.4635 1.7276 1.4729 0.0452 -0.1619 -0.3144 42 GLN B N 2763 C CA . GLN B 42 ? 1.4215 1.6790 1.5187 0.0645 -0.1517 -0.3098 42 GLN B CA 2764 C C . GLN B 42 ? 1.3777 1.6465 1.4571 0.0563 -0.0950 -0.3106 42 GLN B C 2765 O O . GLN B 42 ? 1.3697 1.6303 1.4672 0.0521 -0.0765 -0.3054 42 GLN B O 2766 C CB . GLN B 42 ? 1.3900 1.6686 1.6045 0.0775 -0.1542 -0.3420 42 GLN B CB 2767 N N . LYS B 43 ? 1.3616 1.6442 1.4258 0.0492 -0.0796 -0.3194 43 LYS B N 2768 C CA . LYS B 43 ? 1.3463 1.6200 1.4036 0.0319 -0.0583 -0.3072 43 LYS B CA 2769 C C . LYS B 43 ? 1.3608 1.6286 1.3665 0.0319 -0.0433 -0.2989 43 LYS B C 2770 O O . LYS B 43 ? 1.3540 1.6050 1.3454 0.0194 -0.0282 -0.2787 43 LYS B O 2771 C CB . LYS B 43 ? 1.3389 1.6138 1.4511 0.0241 -0.0814 -0.3173 43 LYS B CB 2772 C CG . LYS B 43 ? 1.3504 1.5894 1.4738 -0.0104 -0.0997 -0.2860 43 LYS B CG 2773 N N . ALA B 44 ? 1.4004 1.6824 1.3631 0.0287 -0.0445 -0.3181 44 ALA B N 2774 C CA . ALA B 44 ? 1.4338 1.7182 1.3335 0.0076 -0.0208 -0.3227 44 ALA B CA 2775 C C . ALA B 44 ? 1.4691 1.7164 1.2984 0.0014 -0.0339 -0.2755 44 ALA B C 2776 O O . ALA B 44 ? 1.4693 1.7083 1.2680 -0.0068 -0.0125 -0.2637 44 ALA B O 2777 C CB . ALA B 44 ? 1.4972 1.8176 1.3527 -0.0316 -0.0044 -0.3766 44 ALA B CB 2778 N N . ILE B 45 ? 1.5041 1.7254 1.3366 0.0059 -0.0803 -0.2519 45 ILE B N 2779 C CA . ILE B 45 ? 1.5449 1.7221 1.3778 0.0048 -0.1196 -0.2121 45 ILE B CA 2780 C C . ILE B 45 ? 1.4747 1.6602 1.3913 0.0294 -0.0810 -0.2203 45 ILE B C 2781 O O . ILE B 45 ? 1.4882 1.6518 1.3937 0.0250 -0.0816 -0.2006 45 ILE B O 2782 C CB . ILE B 45 ? 1.6003 1.7420 1.4929 0.0079 -0.2027 -0.1942 45 ILE B CB 2783 C CG1 . ILE B 45 ? 1.7240 1.8372 1.4787 -0.0512 -0.2562 -0.1693 45 ILE B CG1 2784 C CG2 . ILE B 45 ? 1.6285 1.7239 1.6163 0.0181 -0.2599 -0.1686 45 ILE B CG2 2785 C CD1 . ILE B 45 ? 1.7863 1.8607 1.5993 -0.0536 -0.3512 -0.1495 45 ILE B CD1 2786 N N . ASP B 46 ? 1.4194 1.6346 1.4034 0.0375 -0.0475 -0.2510 46 ASP B N 2787 C CA . ASP B 46 ? 1.3881 1.6152 1.4146 0.0223 -0.0009 -0.2691 46 ASP B CA 2788 C C . ASP B 46 ? 1.3783 1.5952 1.3252 0.0037 0.0265 -0.2454 46 ASP B C 2789 O O . ASP B 46 ? 1.3802 1.5905 1.3230 -0.0112 0.0518 -0.2435 46 ASP B O 2790 C CB . ASP B 46 ? 1.3754 1.6300 1.4496 -0.0025 0.0241 -0.3041 46 ASP B CB 2791 C CG . ASP B 46 ? 1.3795 1.6538 1.5760 0.0146 0.0056 -0.3460 46 ASP B CG 2792 O OD1 . ASP B 46 ? 1.4023 1.6536 1.6377 0.0489 -0.0541 -0.3300 46 ASP B OD1 2793 O OD2 . ASP B 46 ? 1.3799 1.6879 1.6333 -0.0200 0.0434 -0.3946 46 ASP B OD2 2794 N N . GLY B 47 ? 1.3701 1.5877 1.2844 0.0037 0.0172 -0.2375 47 GLY B N 2795 C CA . GLY B 47 ? 1.3652 1.5704 1.2558 -0.0097 0.0243 -0.2229 47 GLY B CA 2796 C C . GLY B 47 ? 1.3748 1.5750 1.2180 -0.0029 0.0390 -0.2137 47 GLY B C 2797 O O . GLY B 47 ? 1.3706 1.5559 1.1986 -0.0153 0.0523 -0.1980 47 GLY B O 2798 N N . VAL B 48 ? 1.4071 1.6113 1.2112 0.0015 0.0279 -0.2172 48 VAL B N 2799 C CA . VAL B 48 ? 1.4499 1.6388 1.1793 -0.0160 0.0308 -0.1999 48 VAL B CA 2800 C C . VAL B 48 ? 1.4481 1.6046 1.1941 -0.0070 0.0159 -0.1689 48 VAL B C 2801 O O . VAL B 48 ? 1.4524 1.5956 1.1672 -0.0149 0.0311 -0.1528 48 VAL B O 2802 C CB . VAL B 48 ? 1.5396 1.7272 1.1824 -0.0539 0.0076 -0.2037 48 VAL B CB 2803 C CG1 . VAL B 48 ? 1.6296 1.7809 1.1637 -0.0997 -0.0096 -0.1674 48 VAL B CG1 2804 C CG2 . VAL B 48 ? 1.5437 1.7843 1.1937 -0.0766 0.0475 -0.2685 48 VAL B CG2 2805 N N . THR B 49 ? 1.4404 1.5906 1.2664 0.0089 -0.0122 -0.1743 49 THR B N 2806 C CA . THR B 49 ? 1.4384 1.5727 1.3563 0.0181 -0.0240 -0.1781 49 THR B CA 2807 C C . THR B 49 ? 1.3912 1.5494 1.3276 0.0052 0.0433 -0.2041 49 THR B C 2808 O O . THR B 49 ? 1.3947 1.5435 1.3650 0.0021 0.0529 -0.2076 49 THR B O 2809 C CB . THR B 49 ? 1.4407 1.5793 1.5071 0.0353 -0.0631 -0.2103 49 THR B CB 2810 O OG1 . THR B 49 ? 1.5052 1.6094 1.5338 0.0328 -0.1408 -0.1750 49 THR B OG1 2811 C CG2 . THR B 49 ? 1.4508 1.5778 1.6816 0.0455 -0.0869 -0.2375 49 THR B CG2 2812 N N . ASN B 50 ? 1.3671 1.5472 1.2751 -0.0156 0.0782 -0.2178 50 ASN B N 2813 C CA . ASN B 50 ? 1.3675 1.5516 1.2441 -0.0628 0.1238 -0.2257 50 ASN B CA 2814 C C . ASN B 50 ? 1.3679 1.5264 1.1702 -0.0655 0.1237 -0.1862 50 ASN B C 2815 O O . ASN B 50 ? 1.3805 1.5323 1.1602 -0.1007 0.1523 -0.1874 50 ASN B O 2816 C CB . ASN B 50 ? 1.3839 1.5712 1.2294 -0.1082 0.1262 -0.2272 50 ASN B CB 2817 C CG . ASN B 50 ? 1.4015 1.6248 1.3092 -0.1458 0.1599 -0.2862 50 ASN B CG 2818 O OD1 . ASN B 50 ? 1.4515 1.6768 1.3044 -0.2310 0.1856 -0.2980 50 ASN B OD1 2819 N ND2 . ASN B 50 ? 1.3792 1.6265 1.4051 -0.0977 0.1519 -0.3253 50 ASN B ND2 2820 N N . LYS B 51 ? 1.3614 1.5131 1.1347 -0.0387 0.0987 -0.1652 51 LYS B N 2821 C CA . LYS B 51 ? 1.3614 1.5005 1.0993 -0.0423 0.1029 -0.1471 51 LYS B CA 2822 C C . LYS B 51 ? 1.3748 1.5030 1.0808 -0.0349 0.1129 -0.1340 51 LYS B C 2823 O O . LYS B 51 ? 1.3712 1.4868 1.0565 -0.0467 0.1288 -0.1210 51 LYS B O 2824 C CB . LYS B 51 ? 1.3616 1.5191 1.1195 -0.0315 0.0913 -0.1665 51 LYS B CB 2825 C CG . LYS B 51 ? 1.3587 1.5140 1.1524 -0.0395 0.0928 -0.1736 51 LYS B CG 2826 C CD . LYS B 51 ? 1.3638 1.5625 1.2278 -0.0369 0.1019 -0.2348 51 LYS B CD 2827 C CE . LYS B 51 ? 1.3538 1.5538 1.3542 -0.0391 0.0829 -0.2640 51 LYS B CE 2828 N NZ . LYS B 51 ? 1.3509 1.5151 1.4632 -0.0391 0.0095 -0.2457 51 LYS B NZ 2829 N N . VAL B 52 ? 1.4057 1.5273 1.1084 -0.0233 0.0875 -0.1293 52 VAL B N 2830 C CA . VAL B 52 ? 1.4482 1.5394 1.1271 -0.0278 0.0671 -0.1027 52 VAL B CA 2831 C C . VAL B 52 ? 1.4261 1.5123 1.1923 -0.0202 0.0788 -0.1162 52 VAL B C 2832 O O . VAL B 52 ? 1.4359 1.5043 1.1880 -0.0256 0.0845 -0.1008 52 VAL B O 2833 C CB . VAL B 52 ? 1.5301 1.5891 1.1797 -0.0412 -0.0002 -0.0761 52 VAL B CB 2834 C CG1 . VAL B 52 ? 1.5239 1.5771 1.2979 -0.0164 -0.0441 -0.0906 52 VAL B CG1 2835 C CG2 . VAL B 52 ? 1.6107 1.6184 1.2059 -0.0700 -0.0438 -0.0298 52 VAL B CG2 2836 N N . ASN B 53 ? 1.4034 1.5142 1.2678 -0.0177 0.0922 -0.1600 53 ASN B N 2837 C CA . ASN B 53 ? 1.3945 1.5253 1.3700 -0.0315 0.1280 -0.2131 53 ASN B CA 2838 C C . ASN B 53 ? 1.3920 1.5364 1.2875 -0.0798 0.1928 -0.2220 53 ASN B C 2839 O O . ASN B 53 ? 1.3991 1.5534 1.3373 -0.1032 0.2281 -0.2555 53 ASN B O 2840 C CB . ASN B 53 ? 1.3858 1.5550 1.5055 -0.0351 0.1382 -0.2842 53 ASN B CB 2841 C CG . ASN B 53 ? 1.4084 1.5501 1.6417 0.0074 0.0496 -0.2724 53 ASN B CG 2842 O OD1 . ASN B 53 ? 1.4518 1.5378 1.6649 0.0232 -0.0255 -0.2131 53 ASN B OD1 2843 N ND2 . ASN B 53 ? 1.3984 1.5705 1.7421 0.0115 0.0475 -0.3233 53 ASN B ND2 2844 N N . SER B 54 ? 1.3979 1.5357 1.1909 -0.1025 0.1951 -0.1920 54 SER B N 2845 C CA . SER B 54 ? 1.4291 1.5512 1.1337 -0.1624 0.2167 -0.1740 54 SER B CA 2846 C C . SER B 54 ? 1.4264 1.5223 1.0917 -0.1440 0.2090 -0.1363 54 SER B C 2847 O O . SER B 54 ? 1.4565 1.5413 1.0811 -0.1912 0.2327 -0.1352 54 SER B O 2848 C CB . SER B 54 ? 1.4459 1.5472 1.0980 -0.1871 0.1804 -0.1404 54 SER B CB 2849 O OG . SER B 54 ? 1.5011 1.5611 1.0771 -0.2547 0.1623 -0.1029 54 SER B OG 2850 N N . ILE B 55 ? 1.4102 1.4988 1.0755 -0.0920 0.1803 -0.1115 55 ILE B N 2851 C CA . ILE B 55 ? 1.4145 1.4863 1.0452 -0.0816 0.1801 -0.0862 55 ILE B CA 2852 C C . ILE B 55 ? 1.4274 1.4922 1.0875 -0.0790 0.1925 -0.0932 55 ILE B C 2853 O O . ILE B 55 ? 1.4343 1.4866 1.0673 -0.0929 0.2092 -0.0818 55 ILE B O 2854 C CB . ILE B 55 ? 1.4239 1.5009 1.0306 -0.0602 0.1619 -0.0785 55 ILE B CB 2855 C CG1 . ILE B 55 ? 1.4103 1.5044 1.0419 -0.0628 0.1567 -0.0955 55 ILE B CG1 2856 C CG2 . ILE B 55 ? 1.4475 1.5117 1.0086 -0.0673 0.1696 -0.0613 55 ILE B CG2 2857 C CD1 . ILE B 55 ? 1.4331 1.5560 1.0572 -0.0613 0.1579 -0.1238 55 ILE B CD1 2858 N N . ILE B 56 ? 1.4368 1.5068 1.1815 -0.0607 0.1739 -0.1162 56 ILE B N 2859 C CA . ILE B 56 ? 1.4524 1.5128 1.2960 -0.0530 0.1643 -0.1353 56 ILE B CA 2860 C C . ILE B 56 ? 1.4463 1.5408 1.3413 -0.0936 0.2327 -0.1990 56 ILE B C 2861 O O . ILE B 56 ? 1.4534 1.5414 1.3791 -0.0999 0.2465 -0.2087 56 ILE B O 2862 C CB . ILE B 56 ? 1.4743 1.5239 1.4576 -0.0259 0.1010 -0.1514 56 ILE B CB 2863 C CG1 . ILE B 56 ? 1.5264 1.5290 1.4109 -0.0205 0.0258 -0.0793 56 ILE B CG1 2864 C CG2 . ILE B 56 ? 1.4932 1.5305 1.6556 -0.0157 0.0725 -0.1862 56 ILE B CG2 2865 C CD1 . ILE B 56 ? 1.5639 1.5478 1.5434 -0.0080 -0.0492 -0.0803 56 ILE B CD1 2866 N N . ASP B 57 ? 1.4511 1.5813 1.3396 -0.1386 0.2776 -0.2452 57 ASP B N 2867 C CA . ASP B 57 ? 1.4868 1.6548 1.3823 -0.2211 0.3547 -0.3182 57 ASP B CA 2868 C C . ASP B 57 ? 1.5225 1.6581 1.2485 -0.2791 0.3676 -0.2664 57 ASP B C 2869 O O . ASP B 57 ? 1.5602 1.7099 1.2773 -0.3395 0.4176 -0.3080 57 ASP B O 2870 C CB . ASP B 57 ? 1.5167 1.7291 1.4276 -0.2837 0.3976 -0.3839 57 ASP B CB 2871 C CG . ASP B 57 ? 1.4903 1.7474 1.6259 -0.2405 0.3958 -0.4678 57 ASP B CG 2872 O OD1 . ASP B 57 ? 1.4817 1.7628 1.8098 -0.2192 0.4037 -0.5385 57 ASP B OD1 2873 O OD2 . ASP B 57 ? 1.4828 1.7476 1.6288 -0.2278 0.3762 -0.4662 57 ASP B OD2 2874 N N . LYS B 58 ? 1.5184 1.6114 1.1363 -0.2658 0.3168 -0.1851 58 LYS B N 2875 C CA . LYS B 58 ? 1.5617 1.6094 1.0624 -0.3155 0.2966 -0.1286 58 LYS B CA 2876 C C . LYS B 58 ? 1.5418 1.5760 1.0497 -0.2828 0.3009 -0.1114 58 LYS B C 2877 O O . LYS B 58 ? 1.5920 1.6012 1.0262 -0.3444 0.3073 -0.0948 58 LYS B O 2878 C CB . LYS B 58 ? 1.5519 1.5629 1.0263 -0.2906 0.2272 -0.0664 58 LYS B CB 2879 N N . MET B 59 ? 1.4892 1.5313 1.0715 -0.2009 0.2884 -0.1091 59 MET B N 2880 C CA . MET B 59 ? 1.4796 1.5048 1.0655 -0.1737 0.2858 -0.0882 59 MET B CA 2881 C C . MET B 59 ? 1.4948 1.5406 1.1791 -0.1805 0.3186 -0.1454 59 MET B C 2882 O O . MET B 59 ? 1.4909 1.5190 1.1965 -0.1592 0.3096 -0.1300 59 MET B O 2883 C CB . MET B 59 ? 1.4544 1.4666 1.0410 -0.1160 0.2454 -0.0509 59 MET B CB 2884 C CG . MET B 59 ? 1.4400 1.4533 0.9844 -0.1102 0.2271 -0.0306 59 MET B CG 2885 S SD . MET B 59 ? 1.4340 1.4307 0.9560 -0.1255 0.2222 -0.0092 59 MET B SD 2886 C CE . MET B 59 ? 1.4426 1.4341 0.9385 -0.1127 0.2386 0.0022 59 MET B CE 2887 N N . ASN B 60 ? 0.9735 1.3282 1.2846 -0.5773 -0.3404 -0.1847 60 ASN B N 2888 C CA . ASN B 60 ? 0.9023 1.3990 1.2351 -0.5669 -0.3009 -0.1894 60 ASN B CA 2889 C C . ASN B 60 ? 0.8587 1.3593 1.1640 -0.5609 -0.2642 -0.1540 60 ASN B C 2890 O O . ASN B 60 ? 0.7993 1.4025 1.1239 -0.5316 -0.2324 -0.1676 60 ASN B O 2891 C CB . ASN B 60 ? 0.9351 1.5444 1.3192 -0.6447 -0.3000 -0.1978 60 ASN B CB 2892 C CG . ASN B 60 ? 0.8675 1.6431 1.3011 -0.6209 -0.2690 -0.2289 60 ASN B CG 2893 O OD1 . ASN B 60 ? 0.8288 1.6568 1.2603 -0.6062 -0.2330 -0.2197 60 ASN B OD1 2894 N ND2 . ASN B 60 ? 0.8598 1.7219 1.3462 -0.6163 -0.2869 -0.2711 60 ASN B ND2 2895 N N . THR B 61 ? 0.8966 1.2838 1.1622 -0.5856 -0.2741 -0.1128 61 THR B N 2896 C CA . THR B 61 ? 0.8653 1.2488 1.0985 -0.5872 -0.2448 -0.0765 61 THR B CA 2897 C C . THR B 61 ? 0.8335 1.1101 1.0323 -0.5136 -0.2500 -0.0733 61 THR B C 2898 O O . THR B 61 ? 0.8649 1.0527 1.0333 -0.5264 -0.2594 -0.0368 61 THR B O 2899 C CB . THR B 61 ? 0.9508 1.3074 1.1623 -0.6870 -0.2535 -0.0225 61 THR B CB 2900 O OG1 . THR B 61 ? 0.9651 1.2470 1.1305 -0.6778 -0.2496 0.0178 61 THR B OG1 2901 C CG2 . THR B 61 ? 1.0563 1.3108 1.2747 -0.7404 -0.3068 -0.0082 61 THR B CG2 2902 N N . GLN B 62 ? 0.7700 1.0641 0.9743 -0.4399 -0.2454 -0.1111 62 GLN B N 2903 C CA . GLN B 62 ? 0.7454 0.9581 0.9198 -0.3742 -0.2481 -0.1173 62 GLN B CA 2904 C C . GLN B 62 ? 0.6694 0.9186 0.8273 -0.3324 -0.2116 -0.1059 62 GLN B C 2905 O O . GLN B 62 ? 0.6453 0.9917 0.8241 -0.3379 -0.1877 -0.1089 62 GLN B O 2906 C CB . GLN B 62 ? 0.7462 0.9632 0.9242 -0.3309 -0.2654 -0.1614 62 GLN B CB 2907 C CG . GLN B 62 ? 0.7399 0.8937 0.8853 -0.2718 -0.2656 -0.1769 62 GLN B CG 2908 C CD . GLN B 62 ? 0.7746 0.9218 0.9163 -0.2517 -0.2898 -0.2234 62 GLN B CD 2909 O OE1 . GLN B 62 ? 0.8247 0.9621 0.9911 -0.2862 -0.3184 -0.2440 62 GLN B OE1 2910 N NE2 . GLN B 62 ? 0.7561 0.9119 0.8633 -0.2013 -0.2790 -0.2407 62 GLN B NE2 2911 N N . PHE B 63 ? 0.6446 0.8200 0.7733 -0.2915 -0.2090 -0.0988 63 PHE B N 2912 C CA . PHE B 63 ? 0.5791 0.7755 0.6921 -0.2534 -0.1782 -0.0880 63 PHE B CA 2913 C C . PHE B 63 ? 0.5388 0.8032 0.6610 -0.2060 -0.1675 -0.1112 63 PHE B C 2914 O O . PHE B 63 ? 0.5645 0.8318 0.6848 -0.1862 -0.1856 -0.1338 63 PHE B O 2915 C CB . PHE B 63 ? 0.5758 0.6823 0.6615 -0.2215 -0.1811 -0.0803 63 PHE B CB 2916 C CG . PHE B 63 ? 0.5197 0.6405 0.5898 -0.1889 -0.1519 -0.0675 63 PHE B CG 2917 C CD1 . PHE B 63 ? 0.5065 0.6369 0.5722 -0.2160 -0.1372 -0.0400 63 PHE B CD1 2918 C CD2 . PHE B 63 ? 0.4848 0.6123 0.5410 -0.1375 -0.1412 -0.0821 63 PHE B CD2 2919 C CE1 . PHE B 63 ? 0.4659 0.6105 0.5215 -0.1864 -0.1121 -0.0344 63 PHE B CE1 2920 C CE2 . PHE B 63 ? 0.4496 0.5840 0.4956 -0.1118 -0.1183 -0.0697 63 PHE B CE2 2921 C CZ . PHE B 63 ? 0.4341 0.5762 0.4838 -0.1333 -0.1037 -0.0495 63 PHE B CZ 2922 N N . GLU B 64 ? 0.4974 0.8147 0.6308 -0.1894 -0.1436 -0.1064 64 GLU B N 2923 C CA . GLU B 64 ? 0.4711 0.8375 0.6205 -0.1418 -0.1440 -0.1229 64 GLU B CA 2924 C C . GLU B 64 ? 0.4429 0.7777 0.5721 -0.1040 -0.1271 -0.1090 64 GLU B C 2925 O O . GLU B 64 ? 0.4430 0.7984 0.5841 -0.1124 -0.1054 -0.1031 64 GLU B O 2926 C CB . GLU B 64 ? 0.4615 0.9366 0.6703 -0.1541 -0.1396 -0.1443 64 GLU B CB 2927 C CG . GLU B 64 ? 0.4924 1.0145 0.7291 -0.1930 -0.1576 -0.1614 64 GLU B CG 2928 C CD . GLU B 64 ? 0.4888 1.1261 0.7832 -0.2328 -0.1407 -0.1805 64 GLU B CD 2929 O OE1 . GLU B 64 ? 0.4731 1.1410 0.7711 -0.2468 -0.1117 -0.1759 64 GLU B OE1 2930 O OE2 . GLU B 64 ? 0.5085 1.2162 0.8456 -0.2528 -0.1555 -0.2046 64 GLU B OE2 2931 N N . ALA B 65 ? 0.4422 0.7315 0.5373 -0.0685 -0.1367 -0.1049 65 ALA B N 2932 C CA . ALA B 65 ? 0.4191 0.6755 0.4930 -0.0372 -0.1239 -0.0895 65 ALA B CA 2933 C C . ALA B 65 ? 0.3979 0.7054 0.5136 -0.0125 -0.1262 -0.0955 65 ALA B C 2934 O O . ALA B 65 ? 0.4002 0.7615 0.5525 -0.0046 -0.1469 -0.1121 65 ALA B O 2935 C CB . ALA B 65 ? 0.4438 0.6579 0.4688 -0.0164 -0.1342 -0.0845 65 ALA B CB 2936 N N . VAL B 66 ? 0.3880 0.6801 0.5069 0.0011 -0.1086 -0.0873 66 VAL B N 2937 C CA . VAL B 66 ? 0.3826 0.7132 0.5517 0.0300 -0.1139 -0.1011 66 VAL B CA 2938 C C . VAL B 66 ? 0.3902 0.6571 0.5326 0.0577 -0.1158 -0.0788 66 VAL B C 2939 O O . VAL B 66 ? 0.3883 0.6083 0.4900 0.0468 -0.0953 -0.0619 66 VAL B O 2940 C CB . VAL B 66 ? 0.3609 0.7562 0.5738 0.0090 -0.0872 -0.1254 66 VAL B CB 2941 C CG1 . VAL B 66 ? 0.3581 0.7859 0.6285 0.0451 -0.0902 -0.1509 66 VAL B CG1 2942 C CG2 . VAL B 66 ? 0.3618 0.8372 0.6081 -0.0253 -0.0868 -0.1478 66 VAL B CG2 2943 N N . GLY B 67 ? 0.4178 0.6815 0.5874 0.0917 -0.1455 -0.0779 67 GLY B N 2944 C CA . GLY B 67 ? 0.4418 0.6398 0.5878 0.1111 -0.1537 -0.0513 67 GLY B CA 2945 C C . GLY B 67 ? 0.4135 0.6129 0.5902 0.1141 -0.1278 -0.0667 67 GLY B C 2946 O O . GLY B 67 ? 0.3935 0.6551 0.6361 0.1213 -0.1228 -0.1054 67 GLY B O 2947 N N . ARG B 68 ? 0.4148 0.5582 0.5453 0.1052 -0.1094 -0.0425 68 ARG B N 2948 C CA . ARG B 68 ? 0.3876 0.5245 0.5403 0.1077 -0.0891 -0.0544 68 ARG B CA 2949 C C . ARG B 68 ? 0.4127 0.4767 0.5348 0.1148 -0.0970 -0.0228 68 ARG B C 2950 O O . ARG B 68 ? 0.4284 0.4571 0.4902 0.0991 -0.0918 0.0075 68 ARG B O 2951 C CB . ARG B 68 ? 0.3469 0.5034 0.4769 0.0762 -0.0528 -0.0598 68 ARG B CB 2952 C CG . ARG B 68 ? 0.3299 0.5552 0.4801 0.0540 -0.0447 -0.0821 68 ARG B CG 2953 C CD . ARG B 68 ? 0.3119 0.5582 0.4470 0.0189 -0.0172 -0.0846 68 ARG B CD 2954 N NE . ARG B 68 ? 0.3104 0.6222 0.4578 -0.0146 -0.0119 -0.0979 68 ARG B NE 2955 C CZ . ARG B 68 ? 0.3254 0.6200 0.4454 -0.0392 -0.0199 -0.0802 68 ARG B CZ 2956 N NH1 . ARG B 68 ? 0.3306 0.5535 0.4134 -0.0292 -0.0314 -0.0572 68 ARG B NH1 2957 N NH2 . ARG B 68 ? 0.3341 0.6895 0.4679 -0.0769 -0.0165 -0.0902 68 ARG B NH2 2958 N N . GLU B 69 ? 0.4221 0.4702 0.5906 0.1354 -0.1093 -0.0355 69 GLU B N 2959 C CA . GLU B 69 ? 0.4558 0.4308 0.6045 0.1377 -0.1236 -0.0041 69 GLU B CA 2960 C C . GLU B 69 ? 0.4123 0.3814 0.5573 0.1239 -0.0893 -0.0142 69 GLU B C 2961 O O . GLU B 69 ? 0.3615 0.3787 0.5466 0.1267 -0.0710 -0.0546 69 GLU B O 2962 C CB . GLU B 69 ? 0.5215 0.4689 0.7350 0.1718 -0.1724 -0.0126 69 GLU B CB 2963 C CG . GLU B 69 ? 0.6206 0.4797 0.7984 0.1679 -0.2126 0.0426 69 GLU B CG 2964 C CD . GLU B 69 ? 0.6938 0.5377 0.8641 0.1792 -0.2648 0.0702 69 GLU B CD 2965 O OE1 . GLU B 69 ? 0.7073 0.5863 0.9527 0.2138 -0.2953 0.0348 69 GLU B OE1 2966 O OE2 . GLU B 69 ? 0.7613 0.5653 0.8512 0.1512 -0.2770 0.1255 69 GLU B OE2 2967 N N . PHE B 70 ? 0.4229 0.3443 0.5182 0.1047 -0.0803 0.0202 70 PHE B N 2968 C CA . PHE B 70 ? 0.3991 0.3132 0.4920 0.0911 -0.0532 0.0135 70 PHE B CA 2969 C C . PHE B 70 ? 0.4430 0.2933 0.5243 0.0827 -0.0674 0.0437 70 PHE B C 2970 O O . PHE B 70 ? 0.4950 0.3104 0.5379 0.0716 -0.0867 0.0831 70 PHE B O 2971 C CB . PHE B 70 ? 0.3709 0.3082 0.4205 0.0686 -0.0216 0.0186 70 PHE B CB 2972 C CG . PHE B 70 ? 0.3450 0.3315 0.3993 0.0665 -0.0125 -0.0014 70 PHE B CG 2973 C CD1 . PHE B 70 ? 0.3180 0.3423 0.3938 0.0592 0.0025 -0.0266 70 PHE B CD1 2974 C CD2 . PHE B 70 ? 0.3531 0.3502 0.3860 0.0649 -0.0210 0.0064 70 PHE B CD2 2975 C CE1 . PHE B 70 ? 0.3052 0.3724 0.3787 0.0455 0.0081 -0.0366 70 PHE B CE1 2976 C CE2 . PHE B 70 ? 0.3338 0.3706 0.3730 0.0564 -0.0157 -0.0093 70 PHE B CE2 2977 C CZ . PHE B 70 ? 0.3082 0.3781 0.3670 0.0443 -0.0017 -0.0276 70 PHE B CZ 2978 N N . ASN B 71 ? 0.4359 0.2731 0.5466 0.0819 -0.0598 0.0267 71 ASN B N 2979 C CA . ASN B 71 ? 0.4919 0.2631 0.5998 0.0691 -0.0776 0.0549 71 ASN B CA 2980 C C . ASN B 71 ? 0.4874 0.2613 0.5422 0.0330 -0.0479 0.0814 71 ASN B C 2981 O O . ASN B 71 ? 0.4375 0.2589 0.4661 0.0258 -0.0187 0.0733 71 ASN B O 2982 C CB . ASN B 71 ? 0.5022 0.2522 0.6785 0.0868 -0.0921 0.0183 71 ASN B CB 2983 C CG . ASN B 71 ? 0.4458 0.2366 0.6290 0.0759 -0.0558 -0.0145 71 ASN B CG 2984 O OD1 . ASN B 71 ? 0.4156 0.2247 0.5566 0.0518 -0.0276 0.0016 71 ASN B OD1 2985 N ND2 . ASN B 71 ? 0.4416 0.2510 0.6829 0.0948 -0.0604 -0.0654 71 ASN B ND2 2986 N N . ASN B 72 ? 0.5564 0.2807 0.6022 0.0094 -0.0589 0.1104 72 ASN B N 2987 C CA . ASN B 72 ? 0.5722 0.3121 0.5723 -0.0300 -0.0309 0.1334 72 ASN B CA 2988 C C . ASN B 72 ? 0.4984 0.2881 0.5164 -0.0304 0.0050 0.0983 72 ASN B C 2989 O O . ASN B 72 ? 0.4770 0.3092 0.4686 -0.0482 0.0317 0.0988 72 ASN B O 2990 C CB . ASN B 72 ? 0.6693 0.3477 0.6570 -0.0654 -0.0520 0.1754 72 ASN B CB 2991 C CG . ASN B 72 ? 0.7067 0.3371 0.7563 -0.0542 -0.0711 0.1550 72 ASN B CG 2992 O OD1 . ASN B 72 ? 0.6850 0.3279 0.7872 -0.0156 -0.0748 0.1082 72 ASN B OD1 2993 N ND2 . ASN B 72 ? 0.7842 0.3648 0.8279 -0.0926 -0.0834 0.1868 72 ASN B ND2 2994 N N . LEU B 73 ? 0.4668 0.2562 0.5320 -0.0110 0.0024 0.0642 73 LEU B N 2995 C CA . LEU B 73 ? 0.4113 0.2466 0.4894 -0.0123 0.0276 0.0347 73 LEU B CA 2996 C C . LEU B 73 ? 0.3608 0.2413 0.4375 0.0063 0.0358 0.0119 73 LEU B C 2997 O O . LEU B 73 ? 0.3365 0.2472 0.4258 0.0064 0.0445 -0.0109 73 LEU B O 2998 C CB . LEU B 73 ? 0.4149 0.2332 0.5345 -0.0130 0.0211 0.0107 73 LEU B CB 2999 C CG . LEU B 73 ? 0.4588 0.2462 0.5791 -0.0449 0.0212 0.0315 73 LEU B CG 3000 C CD1 . LEU B 73 ? 0.4730 0.2307 0.6406 -0.0438 0.0063 0.0046 73 LEU B CD1 3001 C CD2 . LEU B 73 ? 0.4237 0.2631 0.5265 -0.0663 0.0501 0.0337 73 LEU B CD2 3002 N N . GLU B 74 ? 0.3675 0.2528 0.4257 0.0164 0.0298 0.0216 74 GLU B N 3003 C CA . GLU B 74 ? 0.3366 0.2609 0.3899 0.0249 0.0356 0.0065 74 GLU B CA 3004 C C . GLU B 74 ? 0.3404 0.2735 0.3612 0.0202 0.0405 0.0212 74 GLU B C 3005 O O . GLU B 74 ? 0.3570 0.3042 0.3707 0.0275 0.0349 0.0179 74 GLU B O 3006 C CB . GLU B 74 ? 0.3274 0.2640 0.4040 0.0426 0.0222 -0.0109 74 GLU B CB 3007 C CG . GLU B 74 ? 0.3201 0.2745 0.4374 0.0495 0.0211 -0.0461 74 GLU B CG 3008 C CD . GLU B 74 ? 0.3235 0.3050 0.4788 0.0701 0.0082 -0.0749 74 GLU B CD 3009 O OE1 . GLU B 74 ? 0.3317 0.2919 0.4910 0.0846 -0.0114 -0.0601 74 GLU B OE1 3010 O OE2 . GLU B 74 ? 0.3057 0.3399 0.4883 0.0698 0.0171 -0.1157 74 GLU B OE2 3011 N N . ARG B 75 ? 0.3545 0.2884 0.3604 0.0061 0.0520 0.0305 75 ARG B N 3012 C CA . ARG B 75 ? 0.3577 0.3117 0.3373 0.0012 0.0589 0.0320 75 ARG B CA 3013 C C . ARG B 75 ? 0.3171 0.2919 0.3089 0.0107 0.0587 0.0109 75 ARG B C 3014 O O . ARG B 75 ? 0.3164 0.3016 0.2948 0.0142 0.0556 0.0044 75 ARG B O 3015 C CB . ARG B 75 ? 0.3993 0.3711 0.3679 -0.0206 0.0763 0.0356 75 ARG B CB 3016 C CG . ARG B 75 ? 0.4652 0.4083 0.4142 -0.0431 0.0722 0.0669 75 ARG B CG 3017 C CD . ARG B 75 ? 0.5358 0.4683 0.4386 -0.0532 0.0595 0.0938 75 ARG B CD 3018 N NE . ARG B 75 ? 0.6321 0.5227 0.5125 -0.0806 0.0443 0.1347 75 ARG B NE 3019 C CZ . ARG B 75 ? 0.6919 0.5997 0.5384 -0.1242 0.0585 0.1560 75 ARG B CZ 3020 N NH1 . ARG B 75 ? 0.6892 0.6704 0.5279 -0.1410 0.0933 0.1294 75 ARG B NH1 3021 N NH2 . ARG B 75 ? 0.7711 0.6247 0.5958 -0.1538 0.0349 0.2023 75 ARG B NH2 3022 N N . ARG B 76 ? 0.2936 0.2705 0.3099 0.0123 0.0566 0.0015 76 ARG B N 3023 C CA . ARG B 76 ? 0.2803 0.2623 0.3093 0.0169 0.0447 -0.0095 76 ARG B CA 3024 C C . ARG B 76 ? 0.2764 0.2521 0.2935 0.0169 0.0318 -0.0042 76 ARG B C 3025 O O . ARG B 76 ? 0.2919 0.2641 0.3081 0.0195 0.0216 -0.0104 76 ARG B O 3026 C CB . ARG B 76 ? 0.2638 0.2466 0.3132 0.0127 0.0368 -0.0115 76 ARG B CB 3027 C CG . ARG B 76 ? 0.2645 0.2631 0.3390 0.0129 0.0450 -0.0236 76 ARG B CG 3028 C CD . ARG B 76 ? 0.2517 0.2520 0.3438 0.0080 0.0320 -0.0236 76 ARG B CD 3029 N NE . ARG B 76 ? 0.2480 0.2449 0.3257 -0.0022 0.0384 -0.0169 76 ARG B NE 3030 C CZ . ARG B 76 ? 0.2409 0.2441 0.3120 -0.0124 0.0265 -0.0154 76 ARG B CZ 3031 N NH1 . ARG B 76 ? 0.2529 0.2555 0.3224 -0.0181 0.0016 -0.0071 76 ARG B NH1 3032 N NH2 . ARG B 76 ? 0.2342 0.2453 0.3006 -0.0189 0.0357 -0.0236 76 ARG B NH2 3033 N N . ILE B 77 ? 0.2784 0.2590 0.2930 0.0125 0.0320 0.0008 77 ILE B N 3034 C CA . ILE B 77 ? 0.2921 0.2850 0.3010 0.0073 0.0243 0.0014 77 ILE B CA 3035 C C . ILE B 77 ? 0.3008 0.2923 0.3008 0.0177 0.0225 0.0018 77 ILE B C 3036 O O . ILE B 77 ? 0.3044 0.3033 0.3005 0.0132 0.0132 0.0000 77 ILE B O 3037 C CB . ILE B 77 ? 0.2945 0.3162 0.3129 0.0000 0.0289 -0.0070 77 ILE B CB 3038 C CG1 . ILE B 77 ? 0.3188 0.3353 0.3548 0.0159 0.0351 -0.0163 77 ILE B CG1 3039 C CG2 . ILE B 77 ? 0.3025 0.3344 0.3155 -0.0198 0.0267 -0.0048 77 ILE B CG2 3040 C CD1 . ILE B 77 ? 0.3348 0.3886 0.3952 0.0149 0.0387 -0.0418 77 ILE B CD1 3041 N N . GLU B 78 ? 0.3102 0.2911 0.3032 0.0263 0.0275 0.0075 78 GLU B N 3042 C CA . GLU B 78 ? 0.3332 0.3132 0.3064 0.0310 0.0202 0.0138 78 GLU B CA 3043 C C . GLU B 78 ? 0.3297 0.3173 0.2881 0.0272 0.0205 0.0034 78 GLU B C 3044 O O . GLU B 78 ? 0.3499 0.3459 0.2970 0.0281 0.0102 -0.0003 78 GLU B O 3045 C CB . GLU B 78 ? 0.3702 0.3322 0.3268 0.0295 0.0202 0.0320 78 GLU B CB 3046 C CG . GLU B 78 ? 0.4175 0.3800 0.3402 0.0270 0.0074 0.0463 78 GLU B CG 3047 C CD . GLU B 78 ? 0.4919 0.4279 0.3900 0.0153 -0.0007 0.0769 78 GLU B CD 3048 O OE1 . GLU B 78 ? 0.5095 0.4484 0.3916 -0.0041 0.0178 0.0827 78 GLU B OE1 3049 O OE2 . GLU B 78 ? 0.5453 0.4575 0.4441 0.0233 -0.0296 0.0961 78 GLU B OE2 3050 N N . ASN B 79 ? 0.3102 0.2982 0.2767 0.0251 0.0295 -0.0075 79 ASN B N 3051 C CA . ASN B 79 ? 0.3138 0.3122 0.2836 0.0273 0.0277 -0.0316 79 ASN B CA 3052 C C . ASN B 79 ? 0.3114 0.2925 0.3009 0.0278 0.0066 -0.0386 79 ASN B C 3053 O O . ASN B 79 ? 0.3304 0.3117 0.3222 0.0300 -0.0043 -0.0577 79 ASN B O 3054 C CB . ASN B 79 ? 0.3095 0.3217 0.3008 0.0291 0.0399 -0.0491 79 ASN B CB 3055 C CG . ASN B 79 ? 0.3224 0.3527 0.3376 0.0385 0.0346 -0.0897 79 ASN B CG 3056 O OD1 . ASN B 79 ? 0.3188 0.3262 0.3719 0.0489 0.0119 -0.1029 79 ASN B OD1 3057 N ND2 . ASN B 79 ? 0.3398 0.4115 0.3337 0.0332 0.0510 -0.1111 79 ASN B ND2 3058 N N . LEU B 80 ? 0.3053 0.2723 0.3066 0.0206 -0.0007 -0.0231 80 LEU B N 3059 C CA . LEU B 80 ? 0.3242 0.2732 0.3336 0.0069 -0.0236 -0.0163 80 LEU B CA 3060 C C . LEU B 80 ? 0.3249 0.2872 0.3221 -0.0013 -0.0273 -0.0149 80 LEU B C 3061 O O . LEU B 80 ? 0.3450 0.2924 0.3481 -0.0089 -0.0464 -0.0216 80 LEU B O 3062 C CB . LEU B 80 ? 0.3223 0.2725 0.3304 -0.0096 -0.0251 0.0036 80 LEU B CB 3063 C CG . LEU B 80 ? 0.3515 0.2783 0.3597 -0.0352 -0.0538 0.0216 80 LEU B CG 3064 C CD1 . LEU B 80 ? 0.3583 0.2895 0.3607 -0.0483 -0.0557 0.0371 80 LEU B CD1 3065 C CD2 . LEU B 80 ? 0.3675 0.3128 0.3607 -0.0632 -0.0571 0.0323 80 LEU B CD2 3066 N N . ASN B 81 ? 0.2994 0.2884 0.2877 0.0018 -0.0137 -0.0094 81 ASN B N 3067 C CA . ASN B 81 ? 0.3078 0.3205 0.2948 -0.0019 -0.0195 -0.0118 81 ASN B CA 3068 C C . ASN B 81 ? 0.3320 0.3416 0.3065 0.0055 -0.0284 -0.0246 81 ASN B C 3069 O O . ASN B 81 ? 0.3443 0.3613 0.3232 -0.0049 -0.0426 -0.0317 81 ASN B O 3070 C CB . ASN B 81 ? 0.2940 0.3313 0.2881 0.0103 -0.0110 -0.0098 81 ASN B CB 3071 C CG . ASN B 81 ? 0.2966 0.3677 0.3039 0.0119 -0.0218 -0.0176 81 ASN B CG 3072 O OD1 . ASN B 81 ? 0.2858 0.3936 0.3130 -0.0049 -0.0218 -0.0257 81 ASN B OD1 3073 N ND2 . ASN B 81 ? 0.3109 0.3776 0.3062 0.0277 -0.0327 -0.0149 81 ASN B ND2 3074 N N . LYS B 82 ? 0.3360 0.3428 0.2929 0.0183 -0.0191 -0.0288 82 LYS B N 3075 C CA . LYS B 82 ? 0.3646 0.3828 0.3000 0.0210 -0.0227 -0.0454 82 LYS B CA 3076 C C . LYS B 82 ? 0.3774 0.3829 0.3314 0.0182 -0.0355 -0.0741 82 LYS B C 3077 O O . LYS B 82 ? 0.3957 0.4095 0.3455 0.0140 -0.0493 -0.0899 82 LYS B O 3078 C CB . LYS B 82 ? 0.3912 0.4197 0.3014 0.0236 -0.0049 -0.0449 82 LYS B CB 3079 C CG . LYS B 82 ? 0.4413 0.5001 0.3173 0.0183 -0.0033 -0.0654 82 LYS B CG 3080 C CD . LYS B 82 ? 0.4815 0.5614 0.3203 0.0068 0.0157 -0.0527 82 LYS B CD 3081 C CE . LYS B 82 ? 0.5393 0.6646 0.3276 -0.0091 0.0187 -0.0686 82 LYS B CE 3082 N NZ . LYS B 82 ? 0.5556 0.7233 0.3608 -0.0090 0.0370 -0.1255 82 LYS B NZ 3083 N N . LYS B 83 ? 0.4700 0.8751 0.4523 0.0012 0.0915 -0.1966 83 LYS B N 3084 C CA . LYS B 83 ? 0.4574 0.8796 0.4631 0.0125 0.1085 -0.2188 83 LYS B CA 3085 C C . LYS B 83 ? 0.4344 0.8374 0.4679 0.0364 0.1056 -0.2057 83 LYS B C 3086 O O . LYS B 83 ? 0.4391 0.8385 0.4813 0.0367 0.1079 -0.2155 83 LYS B O 3087 C CB . LYS B 83 ? 0.4477 0.8972 0.4772 0.0301 0.1206 -0.2459 83 LYS B CB 3088 C CG . LYS B 83 ? 0.4653 0.9509 0.4800 -0.0012 0.1357 -0.2779 83 LYS B CG 3089 C CD . LYS B 83 ? 0.5008 1.0072 0.5030 -0.0400 0.1522 -0.3121 83 LYS B CD 3090 C CE . LYS B 83 ? 0.5210 1.0838 0.5360 -0.0711 0.1810 -0.3712 83 LYS B CE 3091 N NZ . LYS B 83 ? 0.5446 1.1439 0.5866 -0.0944 0.2035 -0.4265 83 LYS B NZ 3092 N N . MET B 84 ? 0.4141 0.8056 0.4588 0.0498 0.1040 -0.1893 84 MET B N 3093 C CA . MET B 84 ? 0.4184 0.7940 0.4792 0.0557 0.1103 -0.1842 84 MET B CA 3094 C C . MET B 84 ? 0.4151 0.7905 0.4963 0.0436 0.1014 -0.1839 84 MET B C 3095 O O . MET B 84 ? 0.4169 0.7832 0.5019 0.0410 0.1068 -0.1870 84 MET B O 3096 C CB . MET B 84 ? 0.4218 0.7948 0.4907 0.0592 0.1200 -0.1799 84 MET B CB 3097 C CG . MET B 84 ? 0.4492 0.8041 0.5157 0.0481 0.1379 -0.1829 84 MET B CG 3098 S SD . MET B 84 ? 0.4591 0.8437 0.5837 0.0359 0.1544 -0.2035 84 MET B SD 3099 C CE . MET B 84 ? 0.4344 0.8373 0.6174 0.0414 0.1241 -0.2098 84 MET B CE 3100 N N . GLU B 85 ? 0.4139 0.7902 0.5064 0.0356 0.0790 -0.1801 85 GLU B N 3101 C CA . GLU B 85 ? 0.4283 0.7938 0.5457 0.0254 0.0538 -0.1809 85 GLU B CA 3102 C C . GLU B 85 ? 0.4478 0.8011 0.5259 0.0065 0.0497 -0.1796 85 GLU B C 3103 O O . GLU B 85 ? 0.4457 0.7955 0.5431 0.0046 0.0488 -0.1833 85 GLU B O 3104 C CB . GLU B 85 ? 0.4517 0.7982 0.5820 0.0201 0.0094 -0.1762 85 GLU B CB 3105 C CG . GLU B 85 ? 0.4355 0.8024 0.6363 0.0401 0.0104 -0.1919 85 GLU B CG 3106 C CD . GLU B 85 ? 0.4662 0.8068 0.7042 0.0420 -0.0499 -0.1951 85 GLU B CD 3107 O OE1 . GLU B 85 ? 0.5026 0.8018 0.6722 0.0246 -0.0827 -0.1729 85 GLU B OE1 3108 O OE2 . GLU B 85 ? 0.4555 0.8150 0.7931 0.0570 -0.0664 -0.2254 85 GLU B OE2 3109 N N . ASP B 86 ? 0.4662 0.8170 0.4905 -0.0128 0.0513 -0.1807 86 ASP B N 3110 C CA . ASP B 86 ? 0.4961 0.8455 0.4820 -0.0396 0.0588 -0.1930 86 ASP B CA 3111 C C . ASP B 86 ? 0.4655 0.8355 0.4814 -0.0183 0.0855 -0.2106 86 ASP B C 3112 O O . ASP B 86 ? 0.4812 0.8478 0.4917 -0.0307 0.0875 -0.2211 86 ASP B O 3113 C CB . ASP B 86 ? 0.5341 0.8899 0.4613 -0.0756 0.0684 -0.2067 86 ASP B CB 3114 C CG . ASP B 86 ? 0.6194 0.9258 0.4682 -0.1306 0.0357 -0.1936 86 ASP B CG 3115 O OD1 . ASP B 86 ? 0.6642 0.9526 0.4839 -0.1584 0.0305 -0.1984 86 ASP B OD1 3116 O OD2 . ASP B 86 ? 0.6568 0.9318 0.4635 -0.1503 0.0097 -0.1772 86 ASP B OD2 3117 N N . GLY B 87 ? 0.4321 0.8120 0.4726 0.0106 0.0983 -0.2132 87 GLY B N 3118 C CA . GLY B 87 ? 0.4261 0.7985 0.4857 0.0302 0.1048 -0.2235 87 GLY B CA 3119 C C . GLY B 87 ? 0.4269 0.7777 0.4956 0.0283 0.1021 -0.2110 87 GLY B C 3120 O O . GLY B 87 ? 0.4395 0.7800 0.5105 0.0274 0.1008 -0.2210 87 GLY B O 3121 N N . PHE B 88 ? 0.4113 0.7599 0.4943 0.0263 0.1021 -0.1970 88 PHE B N 3122 C CA . PHE B 88 ? 0.4172 0.7578 0.5221 0.0182 0.1049 -0.1964 88 PHE B CA 3123 C C . PHE B 88 ? 0.4223 0.7639 0.5361 0.0056 0.0876 -0.1985 88 PHE B C 3124 O O . PHE B 88 ? 0.4348 0.7673 0.5563 -0.0003 0.0903 -0.2020 88 PHE B O 3125 C CB . PHE B 88 ? 0.4054 0.7598 0.5473 0.0151 0.1141 -0.2004 88 PHE B CB 3126 C CG . PHE B 88 ? 0.4221 0.7615 0.5376 0.0104 0.1380 -0.1999 88 PHE B CG 3127 C CD1 . PHE B 88 ? 0.4649 0.7667 0.5411 -0.0053 0.1482 -0.1971 88 PHE B CD1 3128 C CD2 . PHE B 88 ? 0.4112 0.7607 0.5269 0.0153 0.1448 -0.2003 88 PHE B CD2 3129 C CE1 . PHE B 88 ? 0.5109 0.7748 0.5345 -0.0233 0.1613 -0.1921 88 PHE B CE1 3130 C CE2 . PHE B 88 ? 0.4467 0.7704 0.5200 0.0013 0.1642 -0.1985 88 PHE B CE2 3131 C CZ . PHE B 88 ? 0.5039 0.7790 0.5236 -0.0215 0.1706 -0.1930 88 PHE B CZ 3132 N N . LEU B 89 ? 0.4272 0.7689 0.5275 -0.0047 0.0658 -0.1946 89 LEU B N 3133 C CA . LEU B 89 ? 0.4557 0.7790 0.5423 -0.0267 0.0389 -0.1925 89 LEU B CA 3134 C C . LEU B 89 ? 0.4731 0.7949 0.5227 -0.0408 0.0542 -0.2042 89 LEU B C 3135 O O . LEU B 89 ? 0.4919 0.8002 0.5393 -0.0540 0.0439 -0.2054 89 LEU B O 3136 C CB . LEU B 89 ? 0.4902 0.7888 0.5435 -0.0469 0.0015 -0.1814 89 LEU B CB 3137 C CG . LEU B 89 ? 0.4819 0.7767 0.5919 -0.0302 -0.0297 -0.1781 89 LEU B CG 3138 C CD1 . LEU B 89 ? 0.5412 0.7871 0.6017 -0.0545 -0.0829 -0.1628 89 LEU B CD1 3139 C CD2 . LEU B 89 ? 0.4730 0.7755 0.6658 -0.0183 -0.0470 -0.1920 89 LEU B CD2 3140 N N . ASP B 90 ? 0.4658 0.8055 0.4992 -0.0365 0.0770 -0.2202 90 ASP B N 3141 C CA . ASP B 90 ? 0.4782 0.8284 0.5071 -0.0423 0.0928 -0.2486 90 ASP B CA 3142 C C . ASP B 90 ? 0.4692 0.8048 0.5291 -0.0200 0.0933 -0.2482 90 ASP B C 3143 O O . ASP B 90 ? 0.4867 0.8166 0.5457 -0.0300 0.0930 -0.2611 90 ASP B O 3144 C CB . ASP B 90 ? 0.4717 0.8521 0.5094 -0.0347 0.1108 -0.2798 90 ASP B CB 3145 C CG . ASP B 90 ? 0.4988 0.8963 0.4915 -0.0747 0.1199 -0.2929 90 ASP B CG 3146 O OD1 . ASP B 90 ? 0.5449 0.9226 0.4821 -0.1195 0.1126 -0.2877 90 ASP B OD1 3147 O OD2 . ASP B 90 ? 0.4869 0.9100 0.4906 -0.0674 0.1316 -0.3088 90 ASP B OD2 3148 N N . VAL B 91 ? 0.4535 0.7758 0.5289 0.0022 0.0938 -0.2337 91 VAL B N 3149 C CA . VAL B 91 ? 0.4718 0.7616 0.5510 0.0098 0.0916 -0.2290 91 VAL B CA 3150 C C . VAL B 91 ? 0.4769 0.7609 0.5645 -0.0069 0.0912 -0.2205 91 VAL B C 3151 O O . VAL B 91 ? 0.4999 0.7621 0.5838 -0.0104 0.0878 -0.2255 91 VAL B O 3152 C CB . VAL B 91 ? 0.4809 0.7454 0.5470 0.0169 0.0943 -0.2135 91 VAL B CB 3153 C CG1 . VAL B 91 ? 0.5229 0.7436 0.5679 0.0010 0.0958 -0.2038 91 VAL B CG1 3154 C CG2 . VAL B 91 ? 0.4931 0.7439 0.5529 0.0376 0.0810 -0.2239 91 VAL B CG2 3155 N N . TRP B 92 ? 0.4596 0.7612 0.5674 -0.0155 0.0888 -0.2121 92 TRP B N 3156 C CA . TRP B 92 ? 0.4657 0.7684 0.6033 -0.0287 0.0816 -0.2129 92 TRP B CA 3157 C C . TRP B 92 ? 0.4826 0.7779 0.6056 -0.0425 0.0610 -0.2150 92 TRP B C 3158 O O . TRP B 92 ? 0.4947 0.7822 0.6327 -0.0518 0.0549 -0.2177 92 TRP B O 3159 C CB . TRP B 92 ? 0.4489 0.7744 0.6386 -0.0287 0.0757 -0.2166 92 TRP B CB 3160 C CG . TRP B 92 ? 0.4499 0.7838 0.6529 -0.0320 0.1065 -0.2246 92 TRP B CG 3161 C CD1 . TRP B 92 ? 0.4401 0.7826 0.6386 -0.0262 0.1197 -0.2243 92 TRP B CD1 3162 C CD2 . TRP B 92 ? 0.4773 0.8045 0.6837 -0.0540 0.1309 -0.2357 92 TRP B CD2 3163 N NE1 . TRP B 92 ? 0.4650 0.8043 0.6578 -0.0475 0.1519 -0.2355 92 TRP B NE1 3164 C CE2 . TRP B 92 ? 0.4919 0.8204 0.6851 -0.0686 0.1605 -0.2430 92 TRP B CE2 3165 C CE3 . TRP B 92 ? 0.4985 0.8154 0.7097 -0.0698 0.1319 -0.2413 92 TRP B CE3 3166 C CZ2 . TRP B 92 ? 0.5410 0.8558 0.7127 -0.1084 0.1934 -0.2569 92 TRP B CZ2 3167 C CZ3 . TRP B 92 ? 0.5384 0.8455 0.7378 -0.1031 0.1630 -0.2541 92 TRP B CZ3 3168 C CH2 . TRP B 92 ? 0.5654 0.8694 0.7392 -0.1267 0.1946 -0.2623 92 TRP B CH2 3169 N N . THR B 93 ? 0.4942 0.7895 0.5797 -0.0521 0.0526 -0.2159 93 THR B N 3170 C CA . THR B 93 ? 0.5333 0.8142 0.5767 -0.0811 0.0406 -0.2226 93 THR B CA 3171 C C . THR B 93 ? 0.5416 0.8258 0.5844 -0.0780 0.0610 -0.2435 93 THR B C 3172 O O . THR B 93 ? 0.5662 0.8364 0.6029 -0.0930 0.0532 -0.2466 93 THR B O 3173 C CB . THR B 93 ? 0.5591 0.8391 0.5458 -0.1077 0.0391 -0.2274 93 THR B CB 3174 O OG1 . THR B 93 ? 0.5735 0.8296 0.5514 -0.1158 0.0029 -0.2048 93 THR B OG1 3175 C CG2 . THR B 93 ? 0.6176 0.8841 0.5428 -0.1534 0.0412 -0.2451 93 THR B CG2 3176 N N . TYR B 94 ? 0.5298 0.8274 0.5847 -0.0566 0.0793 -0.2601 94 TYR B N 3177 C CA . TYR B 94 ? 0.5458 0.8373 0.6173 -0.0443 0.0845 -0.2851 94 TYR B CA 3178 C C . TYR B 94 ? 0.5581 0.8178 0.6389 -0.0396 0.0758 -0.2673 94 TYR B C 3179 O O . TYR B 94 ? 0.5800 0.8288 0.6607 -0.0480 0.0723 -0.2798 94 TYR B O 3180 C CB . TYR B 94 ? 0.5386 0.8337 0.6335 -0.0152 0.0853 -0.3028 94 TYR B CB 3181 C CG . TYR B 94 ? 0.5665 0.8358 0.6894 0.0057 0.0696 -0.3284 94 TYR B CG 3182 C CD1 . TYR B 94 ? 0.5799 0.8780 0.7400 0.0069 0.0727 -0.3843 94 TYR B CD1 3183 C CD2 . TYR B 94 ? 0.5933 0.8042 0.7041 0.0182 0.0485 -0.3028 94 TYR B CD2 3184 C CE1 . TYR B 94 ? 0.6127 0.8817 0.8151 0.0321 0.0453 -0.4146 94 TYR B CE1 3185 C CE2 . TYR B 94 ? 0.6401 0.8050 0.7665 0.0352 0.0177 -0.3224 94 TYR B CE2 3186 C CZ . TYR B 94 ? 0.6461 0.8400 0.8273 0.0483 0.0111 -0.3787 94 TYR B CZ 3187 O OH . TYR B 94 ? 0.7004 0.8436 0.9137 0.0712 -0.0319 -0.4051 94 TYR B OH 3188 N N . ASN B 95 ? 0.5532 0.8006 0.6398 -0.0333 0.0765 -0.2434 95 ASN B N 3189 C CA . ASN B 95 ? 0.5779 0.7993 0.6676 -0.0427 0.0772 -0.2325 95 ASN B CA 3190 C C . ASN B 95 ? 0.5850 0.8158 0.6904 -0.0606 0.0709 -0.2336 95 ASN B C 3191 O O . ASN B 95 ? 0.6118 0.8205 0.7144 -0.0690 0.0693 -0.2361 95 ASN B O 3192 C CB . ASN B 95 ? 0.5726 0.7949 0.6678 -0.0491 0.0909 -0.2199 95 ASN B CB 3193 C CG . ASN B 95 ? 0.6032 0.7857 0.6596 -0.0432 0.0910 -0.2130 95 ASN B CG 3194 O OD1 . ASN B 95 ? 0.6318 0.7795 0.6692 -0.0283 0.0709 -0.2184 95 ASN B OD1 3195 N ND2 . ASN B 95 ? 0.6072 0.7909 0.6554 -0.0572 0.1085 -0.2063 95 ASN B ND2 3196 N N . ALA B 96 ? 0.5765 0.8291 0.6934 -0.0681 0.0590 -0.2305 96 ALA B N 3197 C CA . ALA B 96 ? 0.5965 0.8458 0.7292 -0.0854 0.0374 -0.2298 96 ALA B CA 3198 C C . ALA B 96 ? 0.6355 0.8677 0.7281 -0.1015 0.0319 -0.2387 96 ALA B C 3199 O O . ALA B 96 ? 0.6529 0.8725 0.7539 -0.1117 0.0240 -0.2406 96 ALA B O 3200 C CB . ALA B 96 ? 0.5959 0.8497 0.7433 -0.0906 0.0066 -0.2226 96 ALA B CB 3201 N N . GLU B 97 ? 0.6550 0.8920 0.7080 -0.1084 0.0401 -0.2514 97 GLU B N 3202 C CA . GLU B 97 ? 0.7004 0.9315 0.7160 -0.1341 0.0441 -0.2741 97 GLU B CA 3203 C C . GLU B 97 ? 0.7073 0.9353 0.7471 -0.1172 0.0569 -0.2955 97 GLU B C 3204 O O . GLU B 97 ? 0.7359 0.9510 0.7658 -0.1339 0.0527 -0.3057 97 GLU B O 3205 C CB . GLU B 97 ? 0.7203 0.9700 0.6956 -0.1556 0.0604 -0.2979 97 GLU B CB 3206 C CG . GLU B 97 ? 0.7597 0.9875 0.6769 -0.1923 0.0372 -0.2767 97 GLU B CG 3207 C CD . GLU B 97 ? 0.7903 1.0362 0.6575 -0.2240 0.0605 -0.3018 97 GLU B CD 3208 O OE1 . GLU B 97 ? 0.7622 1.0523 0.6687 -0.2034 0.0946 -0.3385 97 GLU B OE1 3209 O OE2 . GLU B 97 ? 0.8563 1.0663 0.6438 -0.2735 0.0394 -0.2877 97 GLU B OE2 3210 N N . LEU B 98 ? 0.6951 0.9241 0.7617 -0.0859 0.0640 -0.3017 98 LEU B N 3211 C CA . LEU B 98 ? 0.7215 0.9263 0.8080 -0.0677 0.0583 -0.3204 98 LEU B CA 3212 C C . LEU B 98 ? 0.7412 0.9103 0.8236 -0.0746 0.0484 -0.2963 98 LEU B C 3213 O O . LEU B 98 ? 0.7740 0.9192 0.8589 -0.0754 0.0397 -0.3112 98 LEU B O 3214 C CB . LEU B 98 ? 0.7213 0.9111 0.8254 -0.0365 0.0497 -0.3249 98 LEU B CB 3215 C CG . LEU B 98 ? 0.7667 0.9061 0.8875 -0.0153 0.0215 -0.3428 98 LEU B CG 3216 C CD1 . LEU B 98 ? 0.7834 0.9447 0.9423 -0.0137 0.0205 -0.3976 98 LEU B CD1 3217 C CD2 . LEU B 98 ? 0.7818 0.8945 0.9145 0.0130 -0.0018 -0.3473 98 LEU B CD2 3218 N N . LEU B 99 ? 0.7276 0.8979 0.8113 -0.0821 0.0512 -0.2669 99 LEU B N 3219 C CA . LEU B 99 ? 0.7496 0.8998 0.8388 -0.0975 0.0501 -0.2544 99 LEU B CA 3220 C C . LEU B 99 ? 0.7603 0.9183 0.8570 -0.1156 0.0405 -0.2593 99 LEU B C 3221 O O . LEU B 99 ? 0.7853 0.9222 0.8842 -0.1270 0.0378 -0.2594 99 LEU B O 3222 C CB . LEU B 99 ? 0.7297 0.8973 0.8400 -0.1056 0.0625 -0.2410 99 LEU B CB 3223 C CG . LEU B 99 ? 0.7553 0.9136 0.8789 -0.1316 0.0731 -0.2416 99 LEU B CG 3224 C CD1 . LEU B 99 ? 0.8176 0.9112 0.8856 -0.1431 0.0723 -0.2355 99 LEU B CD1 3225 C CD2 . LEU B 99 ? 0.7372 0.9326 0.9013 -0.1439 0.0936 -0.2481 99 LEU B CD2 3226 N N . VAL B 100 ? 0.7558 0.9338 0.8451 -0.1247 0.0310 -0.2614 100 VAL B N 3227 C CA . VAL B 100 ? 0.7887 0.9569 0.8645 -0.1493 0.0123 -0.2639 100 VAL B CA 3228 C C . VAL B 100 ? 0.8248 0.9802 0.8736 -0.1567 0.0211 -0.2885 100 VAL B C 3229 O O . VAL B 100 ? 0.8496 0.9872 0.9000 -0.1673 0.0135 -0.2907 100 VAL B O 3230 C CB . VAL B 100 ? 0.8052 0.9721 0.8520 -0.1699 -0.0113 -0.2559 100 VAL B CB 3231 C CG1 . VAL B 100 ? 0.8646 1.0014 0.8614 -0.2077 -0.0340 -0.2598 100 VAL B CG1 3232 C CG2 . VAL B 100 ? 0.7828 0.9578 0.8820 -0.1601 -0.0357 -0.2402 100 VAL B CG2 3233 N N . LEU B 101 ? 0.8319 1.0021 0.8681 -0.1510 0.0373 -0.3146 101 LEU B N 3234 C CA . LEU B 101 ? 0.8657 1.0371 0.9026 -0.1541 0.0475 -0.3571 101 LEU B CA 3235 C C . LEU B 101 ? 0.8815 1.0200 0.9477 -0.1304 0.0362 -0.3586 101 LEU B C 3236 O O . LEU B 101 ? 0.9115 1.0368 0.9773 -0.1406 0.0325 -0.3789 101 LEU B O 3237 C CB . LEU B 101 ? 0.8622 1.0680 0.9132 -0.1457 0.0669 -0.3992 101 LEU B CB 3238 C CG . LEU B 101 ? 0.8960 1.1307 0.8990 -0.1941 0.0882 -0.4278 101 LEU B CG 3239 C CD1 . LEU B 101 ? 0.8994 1.1230 0.8502 -0.2167 0.0768 -0.3840 101 LEU B CD1 3240 C CD2 . LEU B 101 ? 0.8977 1.1807 0.9402 -0.1880 0.1156 -0.4925 101 LEU B CD2 3241 N N . MET B 102 ? 0.8774 0.9933 0.9565 -0.1060 0.0284 -0.3366 102 MET B N 3242 C CA . MET B 102 ? 0.9209 0.9811 1.0002 -0.0961 0.0094 -0.3302 102 MET B CA 3243 C C . MET B 102 ? 0.9315 0.9736 0.9971 -0.1215 0.0092 -0.3059 102 MET B C 3244 O O . MET B 102 ? 0.9727 0.9725 1.0304 -0.1258 -0.0050 -0.3109 102 MET B O 3245 C CB . MET B 102 ? 0.9404 0.9647 1.0086 -0.0801 -0.0015 -0.3102 102 MET B CB 3246 C CG . MET B 102 ? 0.9666 0.9754 1.0597 -0.0475 -0.0245 -0.3426 102 MET B CG 3247 S SD . MET B 102 ? 0.9939 0.9678 1.0654 -0.0323 -0.0394 -0.3178 102 MET B SD 3248 C CE . MET B 102 ? 1.0361 0.9528 1.0373 -0.0726 -0.0327 -0.2659 102 MET B CE 3249 N N . GLU B 103 ? 0.8959 0.9692 0.9680 -0.1372 0.0201 -0.2851 103 GLU B N 3250 C CA . GLU B 103 ? 0.8992 0.9707 0.9829 -0.1607 0.0186 -0.2742 103 GLU B CA 3251 C C . GLU B 103 ? 0.9110 0.9829 0.9895 -0.1741 0.0067 -0.2869 103 GLU B C 3252 O O . GLU B 103 ? 0.9345 0.9860 1.0153 -0.1882 0.0009 -0.2866 103 GLU B O 3253 C CB . GLU B 103 ? 0.8623 0.9734 0.9827 -0.1679 0.0237 -0.2636 103 GLU B CB 3254 N N . ASN B 104 ? 0.9038 0.9949 0.9650 -0.1781 0.0046 -0.2991 104 ASN B N 3255 C CA . ASN B 104 ? 0.9356 1.0192 0.9694 -0.2036 -0.0039 -0.3146 104 ASN B CA 3256 C C . ASN B 104 ? 0.9695 1.0326 1.0036 -0.1981 0.0011 -0.3427 104 ASN B C 3257 O O . ASN B 104 ? 0.9966 1.0414 1.0225 -0.2156 -0.0079 -0.3460 104 ASN B O 3258 C CB . ASN B 104 ? 0.9446 1.0437 0.9354 -0.2255 0.0000 -0.3281 104 ASN B CB 3259 C CG . ASN B 104 ? 0.9369 1.0330 0.9150 -0.2396 -0.0253 -0.2984 104 ASN B CG 3260 O OD1 . ASN B 104 ? 0.9142 1.0074 0.9350 -0.2308 -0.0469 -0.2772 104 ASN B OD1 3261 N ND2 . ASN B 104 ? 0.9628 1.0581 0.8862 -0.2655 -0.0255 -0.3034 104 ASN B ND2 3262 N N . GLU B 105 ? 0.9755 1.0379 1.0266 -0.1716 0.0080 -0.3659 105 GLU B N 3263 C CA . GLU B 105 ? 1.0189 1.0532 1.0885 -0.1574 -0.0017 -0.3994 105 GLU B CA 3264 C C . GLU B 105 ? 1.0533 1.0339 1.1155 -0.1596 -0.0207 -0.3717 105 GLU B C 3265 O O . GLU B 105 ? 1.0862 1.0425 1.1483 -0.1669 -0.0310 -0.3889 105 GLU B O 3266 C CB . GLU B 105 ? 1.0203 1.0518 1.1252 -0.1218 -0.0095 -0.4285 105 GLU B CB 3267 C CG . GLU B 105 ? 1.0676 1.0784 1.2155 -0.1032 -0.0294 -0.4840 105 GLU B CG 3268 C CD . GLU B 105 ? 1.0695 1.0985 1.2792 -0.0686 -0.0401 -0.5360 105 GLU B CD 3269 O OE1 . GLU B 105 ? 1.0866 1.0661 1.3008 -0.0400 -0.0742 -0.5139 105 GLU B OE1 3270 O OE2 . GLU B 105 ? 1.0642 1.1557 1.3174 -0.0756 -0.0151 -0.6044 105 GLU B OE2 3271 N N . ARG B 106 ? 1.0530 1.0158 1.1051 -0.1602 -0.0215 -0.3338 106 ARG B N 3272 C CA . ARG B 106 ? 1.0983 1.0137 1.1312 -0.1796 -0.0297 -0.3107 106 ARG B CA 3273 C C . ARG B 106 ? 1.0892 1.0280 1.1317 -0.2061 -0.0236 -0.3065 106 ARG B C 3274 O O . ARG B 106 ? 1.1342 1.0373 1.1660 -0.2208 -0.0336 -0.3079 106 ARG B O 3275 C CB . ARG B 106 ? 1.1061 1.0106 1.1224 -0.1911 -0.0189 -0.2823 106 ARG B CB 3276 C CG . ARG B 106 ? 1.1636 1.0027 1.1442 -0.1777 -0.0404 -0.2767 106 ARG B CG 3277 C CD . ARG B 106 ? 1.2109 1.0137 1.1431 -0.2142 -0.0281 -0.2489 106 ARG B CD 3278 N NE . ARG B 106 ? 1.2937 1.0072 1.1667 -0.2112 -0.0616 -0.2369 106 ARG B NE 3279 C CZ . ARG B 106 ? 1.2778 0.9978 1.1568 -0.1838 -0.0692 -0.2371 106 ARG B CZ 3280 N NH1 . ARG B 106 ? 1.1828 0.9967 1.1197 -0.1593 -0.0403 -0.2482 106 ARG B NH1 3281 N NH2 . ARG B 106 ? 1.3716 0.9924 1.1916 -0.1840 -0.1136 -0.2249 106 ARG B NH2 3282 N N . THR B 107 ? 1.0424 1.0325 1.1043 -0.2125 -0.0160 -0.3014 107 THR B N 3283 C CA . THR B 107 ? 1.0420 1.0470 1.1210 -0.2356 -0.0255 -0.2978 107 THR B CA 3284 C C . THR B 107 ? 1.0804 1.0648 1.1350 -0.2475 -0.0372 -0.3149 107 THR B C 3285 O O . THR B 107 ? 1.1032 1.0736 1.1652 -0.2652 -0.0470 -0.3125 107 THR B O 3286 C CB . THR B 107 ? 1.0067 1.0497 1.1072 -0.2380 -0.0357 -0.2902 107 THR B CB 3287 O OG1 . THR B 107 ? 0.9735 1.0413 1.1077 -0.2273 -0.0219 -0.2818 107 THR B OG1 3288 C CG2 . THR B 107 ? 1.0220 1.0681 1.1511 -0.2586 -0.0639 -0.2888 107 THR B CG2 3289 N N . LEU B 108 ? 1.0916 1.0794 1.1216 -0.2422 -0.0322 -0.3392 108 LEU B N 3290 C CA . LEU B 108 ? 1.1336 1.1089 1.1398 -0.2606 -0.0350 -0.3678 108 LEU B CA 3291 C C . LEU B 108 ? 1.1677 1.1050 1.1868 -0.2480 -0.0412 -0.3832 108 LEU B C 3292 O O . LEU B 108 ? 1.1961 1.1136 1.2056 -0.2663 -0.0501 -0.3892 108 LEU B O 3293 C CB . LEU B 108 ? 1.1431 1.1443 1.1265 -0.2689 -0.0171 -0.4061 108 LEU B CB 3294 C CG . LEU B 108 ? 1.1453 1.1631 1.0860 -0.2974 -0.0182 -0.3908 108 LEU B CG 3295 C CD1 . LEU B 108 ? 1.1667 1.2128 1.0784 -0.3164 0.0104 -0.4364 108 LEU B CD1 3296 C CD2 . LEU B 108 ? 1.1912 1.1798 1.0883 -0.3382 -0.0469 -0.3706 108 LEU B CD2 3297 N N . ASP B 109 ? 1.1737 1.0900 1.2094 -0.2185 -0.0450 -0.3884 109 ASP B N 3298 C CA . ASP B 109 ? 1.2281 1.0829 1.2665 -0.2071 -0.0685 -0.3973 109 ASP B CA 3299 C C . ASP B 109 ? 1.2547 1.0702 1.2696 -0.2313 -0.0753 -0.3580 109 ASP B C 3300 O O . ASP B 109 ? 1.3099 1.0736 1.3117 -0.2401 -0.0941 -0.3620 109 ASP B O 3301 C CB . ASP B 109 ? 1.2463 1.0679 1.2994 -0.1731 -0.0883 -0.4085 109 ASP B CB 3302 C CG . ASP B 109 ? 1.2324 1.0990 1.3320 -0.1491 -0.0818 -0.4669 109 ASP B CG 3303 O OD1 . ASP B 109 ? 1.2373 1.1417 1.3508 -0.1633 -0.0646 -0.5100 109 ASP B OD1 3304 O OD2 . ASP B 109 ? 1.2264 1.0920 1.3484 -0.1216 -0.0917 -0.4753 109 ASP B OD2 3305 N N . PHE B 110 ? 1.2205 1.0641 1.2364 -0.2453 -0.0585 -0.3278 110 PHE B N 3306 C CA . PHE B 110 ? 1.2402 1.0709 1.2510 -0.2782 -0.0526 -0.3064 110 PHE B CA 3307 C C . PHE B 110 ? 1.2433 1.0891 1.2701 -0.2976 -0.0577 -0.3139 110 PHE B C 3308 O O . PHE B 110 ? 1.2835 1.0975 1.3004 -0.3229 -0.0610 -0.3099 110 PHE B O 3309 C CB . PHE B 110 ? 1.1973 1.0766 1.2338 -0.2877 -0.0297 -0.2923 110 PHE B CB 3310 C CG . PHE B 110 ? 1.2107 1.1044 1.2696 -0.3273 -0.0141 -0.2907 110 PHE B CG 3311 C CD1 . PHE B 110 ? 1.2837 1.1179 1.2942 -0.3633 -0.0084 -0.2848 110 PHE B CD1 3312 C CD2 . PHE B 110 ? 1.1618 1.1249 1.2928 -0.3331 -0.0095 -0.3011 110 PHE B CD2 3313 C CE1 . PHE B 110 ? 1.3014 1.1600 1.3362 -0.4106 0.0162 -0.2952 110 PHE B CE1 3314 C CE2 . PHE B 110 ? 1.1705 1.1628 1.3496 -0.3690 0.0068 -0.3169 110 PHE B CE2 3315 C CZ . PHE B 110 ? 1.2378 1.1855 1.3695 -0.4110 0.0273 -0.3169 110 PHE B CZ 3316 N N . HIS B 111 ? 1.2126 1.0979 1.2527 -0.2929 -0.0613 -0.3242 111 HIS B N 3317 C CA . HIS B 111 ? 1.2337 1.1194 1.2747 -0.3143 -0.0753 -0.3306 111 HIS B CA 3318 C C . HIS B 111 ? 1.2840 1.1256 1.2979 -0.3150 -0.0828 -0.3514 111 HIS B C 3319 O O . HIS B 111 ? 1.3146 1.1352 1.3269 -0.3350 -0.0928 -0.3506 111 HIS B O 3320 C CB . HIS B 111 ? 1.2221 1.1361 1.2546 -0.3218 -0.0866 -0.3330 111 HIS B CB 3321 C CG . HIS B 111 ? 1.1884 1.1357 1.2625 -0.3226 -0.0979 -0.3157 111 HIS B CG 3322 N ND1 . HIS B 111 ? 1.1833 1.1466 1.3173 -0.3334 -0.1091 -0.3127 111 HIS B ND1 3323 C CD2 . HIS B 111 ? 1.1634 1.1328 1.2391 -0.3141 -0.1027 -0.3084 111 HIS B CD2 3324 C CE1 . HIS B 111 ? 1.1511 1.1482 1.3347 -0.3268 -0.1234 -0.3096 111 HIS B CE1 3325 N NE2 . HIS B 111 ? 1.1406 1.1357 1.2828 -0.3148 -0.1224 -0.3020 111 HIS B NE2 3326 N N . ASP B 112 ? 1.2921 1.1227 1.2970 -0.2920 -0.0804 -0.3767 112 ASP B N 3327 C CA . ASP B 112 ? 1.3444 1.1331 1.3458 -0.2850 -0.0939 -0.4087 112 ASP B CA 3328 C C . ASP B 112 ? 1.3938 1.1132 1.3825 -0.2872 -0.1150 -0.3887 112 ASP B C 3329 O O . ASP B 112 ? 1.4394 1.1189 1.4187 -0.2985 -0.1309 -0.3985 112 ASP B O 3330 C CB . ASP B 112 ? 1.3458 1.1451 1.3701 -0.2551 -0.0920 -0.4546 112 ASP B CB 3331 C CG . ASP B 112 ? 1.3444 1.1945 1.3658 -0.2734 -0.0688 -0.5000 112 ASP B CG 3332 O OD1 . ASP B 112 ? 1.3712 1.2177 1.3668 -0.3049 -0.0675 -0.5067 112 ASP B OD1 3333 O OD2 . ASP B 112 ? 1.3236 1.2141 1.3612 -0.2637 -0.0506 -0.5316 112 ASP B OD2 3334 N N . SER B 113 ? 1.3953 1.0931 1.3712 -0.2844 -0.1153 -0.3610 113 SER B N 3335 C CA . SER B 113 ? 1.4698 1.0857 1.4026 -0.3058 -0.1344 -0.3376 113 SER B CA 3336 C C . SER B 113 ? 1.4854 1.1034 1.4091 -0.3492 -0.1226 -0.3235 113 SER B C 3337 O O . SER B 113 ? 1.5632 1.1090 1.4495 -0.3706 -0.1437 -0.3197 113 SER B O 3338 C CB . SER B 113 ? 1.4771 1.0758 1.3816 -0.3127 -0.1272 -0.3108 113 SER B CB 3339 O OG . SER B 113 ? 1.5692 1.0846 1.4065 -0.3569 -0.1380 -0.2864 113 SER B OG 3340 N N . ASN B 114 ? 1.4200 1.1167 1.3833 -0.3620 -0.0956 -0.3195 114 ASN B N 3341 C CA . ASN B 114 ? 1.4275 1.1425 1.4092 -0.4003 -0.0864 -0.3167 114 ASN B CA 3342 C C . ASN B 114 ? 1.4481 1.1499 1.4312 -0.4029 -0.1054 -0.3307 114 ASN B C 3343 O O . ASN B 114 ? 1.4812 1.1677 1.4641 -0.4351 -0.1066 -0.3298 114 ASN B O 3344 C CB . ASN B 114 ? 1.3575 1.1582 1.4046 -0.4053 -0.0678 -0.3184 114 ASN B CB 3345 C CG . ASN B 114 ? 1.3387 1.1602 1.3906 -0.4068 -0.0436 -0.3110 114 ASN B CG 3346 O OD1 . ASN B 114 ? 1.3931 1.1626 1.3919 -0.4304 -0.0331 -0.3013 114 ASN B OD1 3347 N ND2 . ASN B 114 ? 1.2725 1.1590 1.3770 -0.3867 -0.0395 -0.3145 114 ASN B ND2 3348 N N . VAL B 115 ? 1.4329 1.1431 1.4152 -0.3757 -0.1158 -0.3489 115 VAL B N 3349 C CA . VAL B 115 ? 1.4643 1.1581 1.4375 -0.3825 -0.1303 -0.3692 115 VAL B CA 3350 C C . VAL B 115 ? 1.5376 1.1531 1.4837 -0.3795 -0.1508 -0.3794 115 VAL B C 3351 O O . VAL B 115 ? 1.5792 1.1645 1.5145 -0.4006 -0.1623 -0.3823 115 VAL B O 3352 C CB . VAL B 115 ? 1.4450 1.1719 1.4147 -0.3697 -0.1264 -0.3968 115 VAL B CB 3353 C CG1 . VAL B 115 ? 1.4927 1.1989 1.4446 -0.3842 -0.1354 -0.4272 115 VAL B CG1 3354 C CG2 . VAL B 115 ? 1.4012 1.1791 1.3782 -0.3817 -0.1228 -0.3810 115 VAL B CG2 3355 N N . LYS B 116 ? 1.5624 1.1375 1.4991 -0.3527 -0.1640 -0.3855 116 LYS B N 3356 C CA . LYS B 116 ? 1.6508 1.1300 1.5628 -0.3454 -0.2039 -0.3953 116 LYS B CA 3357 C C . LYS B 116 ? 1.7211 1.1300 1.5770 -0.3900 -0.2137 -0.3583 116 LYS B C 3358 O O . LYS B 116 ? 1.7981 1.1349 1.6262 -0.4046 -0.2431 -0.3621 116 LYS B O 3359 C CB . LYS B 116 ? 1.6696 1.1121 1.5896 -0.3066 -0.2304 -0.4091 116 LYS B CB 3360 N N . ASN B 117 ? 1.7025 1.1338 1.5409 -0.4178 -0.1860 -0.3286 117 ASN B N 3361 C CA . ASN B 117 ? 1.7761 1.1555 1.5571 -0.4781 -0.1791 -0.3033 117 ASN B CA 3362 C C . ASN B 117 ? 1.7657 1.1880 1.5745 -0.5122 -0.1593 -0.3101 117 ASN B C 3363 O O . ASN B 117 ? 1.8505 1.2087 1.6086 -0.5598 -0.1664 -0.3018 117 ASN B O 3364 C CB . ASN B 117 ? 1.7532 1.1649 1.5219 -0.5045 -0.1435 -0.2858 117 ASN B CB 3365 C CG . ASN B 117 ? 1.7830 1.1351 1.5089 -0.4800 -0.1686 -0.2738 117 ASN B CG 3366 O OD1 . ASN B 117 ? 1.8483 1.1081 1.5424 -0.4538 -0.2229 -0.2765 117 ASN B OD1 3367 N ND2 . ASN B 117 ? 1.7360 1.1403 1.4709 -0.4863 -0.1346 -0.2656 117 ASN B ND2 3368 N N . LEU B 118 ? 1.6767 1.1977 1.5592 -0.4924 -0.1407 -0.3249 118 LEU B N 3369 C CA . LEU B 118 ? 1.6667 1.2272 1.5870 -0.5172 -0.1351 -0.3346 118 LEU B CA 3370 C C . LEU B 118 ? 1.7222 1.2268 1.6171 -0.5105 -0.1653 -0.3459 118 LEU B C 3371 O O . LEU B 118 ? 1.7564 1.2501 1.6515 -0.5430 -0.1682 -0.3483 118 LEU B O 3372 C CB . LEU B 118 ? 1.5753 1.2315 1.5684 -0.4984 -0.1269 -0.3440 118 LEU B CB 3373 C CG . LEU B 118 ? 1.5638 1.2591 1.6074 -0.5198 -0.1360 -0.3554 118 LEU B CG 3374 C CD1 . LEU B 118 ? 1.5864 1.2997 1.6629 -0.5676 -0.1145 -0.3630 118 LEU B CD1 3375 C CD2 . LEU B 118 ? 1.5007 1.2603 1.5989 -0.5004 -0.1492 -0.3596 118 LEU B CD2 3376 N N . TYR B 119 ? 1.7318 1.2080 1.6158 -0.4695 -0.1860 -0.3611 119 TYR B N 3377 C CA . TYR B 119 ? 1.7852 1.2122 1.6577 -0.4595 -0.2138 -0.3855 119 TYR B CA 3378 C C . TYR B 119 ? 1.8948 1.2101 1.7119 -0.4803 -0.2468 -0.3740 119 TYR B C 3379 O O . TYR B 119 ? 1.9452 1.2224 1.7483 -0.4999 -0.2626 -0.3805 119 TYR B O 3380 C CB . TYR B 119 ? 1.7670 1.2069 1.6631 -0.4134 -0.2219 -0.4226 119 TYR B CB 3381 C CG . TYR B 119 ? 1.8162 1.2243 1.7210 -0.4032 -0.2439 -0.4661 119 TYR B CG 3382 C CD1 . TYR B 119 ? 1.8081 1.2529 1.7151 -0.4250 -0.2307 -0.4815 119 TYR B CD1 3383 C CD2 . TYR B 119 ? 1.8800 1.2163 1.7950 -0.3726 -0.2845 -0.4967 119 TYR B CD2 3384 C CE1 . TYR B 119 ? 1.8557 1.2760 1.7707 -0.4210 -0.2450 -0.5280 119 TYR B CE1 3385 C CE2 . TYR B 119 ? 1.9243 1.2393 1.8663 -0.3613 -0.3048 -0.5491 119 TYR B CE2 3386 C CZ . TYR B 119 ? 1.9097 1.2716 1.8495 -0.3877 -0.2787 -0.5656 119 TYR B CZ 3387 O OH . TYR B 119 ? 1.9594 1.3050 1.9250 -0.3820 -0.2927 -0.6237 119 TYR B OH 3388 N N . ASP B 120 ? 1.9458 1.1975 1.7206 -0.4809 -0.2630 -0.3549 120 ASP B N 3389 C CA . ASP B 120 ? 2.0827 1.1987 1.7759 -0.5120 -0.3074 -0.3361 120 ASP B CA 3390 C C . ASP B 120 ? 2.1343 1.2348 1.7759 -0.5876 -0.2819 -0.3108 120 ASP B C 3391 O O . ASP B 120 ? 2.2506 1.2428 1.8211 -0.6253 -0.3161 -0.3001 120 ASP B O 3392 C CB . ASP B 120 ? 2.1418 1.1802 1.7852 -0.5033 -0.3383 -0.3181 120 ASP B CB 3393 C CG . ASP B 120 ? 2.1223 1.1557 1.8246 -0.4300 -0.3782 -0.3548 120 ASP B CG 3394 O OD1 . ASP B 120 ? 2.0494 1.1622 1.8314 -0.3922 -0.3635 -0.3979 120 ASP B OD1 3395 O OD2 . ASP B 120 ? 2.1884 1.1369 1.8566 -0.4159 -0.4248 -0.3457 120 ASP B OD2 3396 N N . LYS B 121 ? 2.0548 1.2626 1.7386 -0.6116 -0.2248 -0.3079 121 LYS B N 3397 C CA . LYS B 121 ? 2.0935 1.3163 1.7599 -0.6853 -0.1903 -0.3028 121 LYS B CA 3398 C C . LYS B 121 ? 2.1039 1.3316 1.7945 -0.6967 -0.1995 -0.3168 121 LYS B C 3399 O O . LYS B 121 ? 2.1921 1.3691 1.8317 -0.7602 -0.1958 -0.3120 121 LYS B O 3400 C CB . LYS B 121 ? 1.9942 1.3468 1.7392 -0.6964 -0.1341 -0.3142 121 LYS B CB 3401 C CG . LYS B 121 ? 2.0342 1.4192 1.7835 -0.7777 -0.0904 -0.3275 121 LYS B CG 3402 C CD . LYS B 121 ? 1.9516 1.4559 1.7862 -0.7877 -0.0397 -0.3500 121 LYS B CD 3403 C CE . LYS B 121 ? 1.9981 1.5464 1.8521 -0.8766 0.0120 -0.3824 121 LYS B CE 3404 N NZ . LYS B 121 ? 1.9802 1.5741 1.9087 -0.8886 0.0080 -0.4086 121 LYS B NZ 3405 N N . VAL B 122 ? 2.0257 1.3102 1.7835 -0.6436 -0.2098 -0.3355 122 VAL B N 3406 C CA . VAL B 122 ? 2.0353 1.3213 1.8120 -0.6512 -0.2226 -0.3497 122 VAL B CA 3407 C C . VAL B 122 ? 2.1383 1.3040 1.8517 -0.6441 -0.2709 -0.3514 122 VAL B C 3408 O O . VAL B 122 ? 2.2018 1.3235 1.8905 -0.6775 -0.2838 -0.3525 122 VAL B O 3409 C CB . VAL B 122 ? 1.9399 1.3143 1.7879 -0.6104 -0.2195 -0.3693 122 VAL B CB 3410 C CG1 . VAL B 122 ? 1.9656 1.3322 1.8208 -0.6247 -0.2357 -0.3830 122 VAL B CG1 3411 C CG2 . VAL B 122 ? 1.8524 1.3290 1.7675 -0.6139 -0.1903 -0.3681 122 VAL B CG2 3412 N N . ARG B 123 ? 2.1594 1.2730 1.8578 -0.5988 -0.3027 -0.3571 123 ARG B N 3413 C CA . ARG B 123 ? 2.2712 1.2602 1.9262 -0.5849 -0.3640 -0.3667 123 ARG B CA 3414 C C . ARG B 123 ? 2.4164 1.2752 1.9632 -0.6484 -0.3921 -0.3311 123 ARG B C 3415 O O . ARG B 123 ? 2.5222 1.2793 2.0228 -0.6665 -0.4373 -0.3319 123 ARG B O 3416 C CB . ARG B 123 ? 2.2638 1.2321 1.9477 -0.5219 -0.3969 -0.3900 123 ARG B CB 3417 N N . LEU B 124 ? 2.4343 1.2916 1.9323 -0.6896 -0.3649 -0.3022 124 LEU B N 3418 C CA . LEU B 124 ? 2.5911 1.3246 1.9604 -0.7739 -0.3795 -0.2689 124 LEU B CA 3419 C C . LEU B 124 ? 2.6112 1.3803 1.9692 -0.8482 -0.3352 -0.2702 124 LEU B C 3420 O O . LEU B 124 ? 2.7589 1.4062 2.0140 -0.9121 -0.3644 -0.2543 124 LEU B O 3421 C CB . LEU B 124 ? 2.6039 1.3364 1.9225 -0.8052 -0.3528 -0.2467 124 LEU B CB 3422 N N . GLN B 125 ? 2.4735 1.4031 1.9388 -0.8416 -0.2717 -0.2918 125 GLN B N 3423 C CA . GLN B 125 ? 2.4727 1.4606 1.9643 -0.9033 -0.2306 -0.3061 125 GLN B CA 3424 C C . GLN B 125 ? 2.5057 1.4522 2.0018 -0.8918 -0.2673 -0.3143 125 GLN B C 3425 O O . GLN B 125 ? 2.5856 1.4974 2.0408 -0.9597 -0.2594 -0.3151 125 GLN B O 3426 C CB . GLN B 125 ? 2.3192 1.4819 1.9455 -0.8853 -0.1747 -0.3331 125 GLN B CB 3427 C CG . GLN B 125 ? 2.3081 1.5479 1.9963 -0.9421 -0.1376 -0.3612 125 GLN B CG 3428 C CD . GLN B 125 ? 2.1840 1.5819 2.0112 -0.9316 -0.0940 -0.3944 125 GLN B CD 3429 O OE1 . GLN B 125 ? 2.1789 1.6519 2.0761 -0.9842 -0.0589 -0.4300 125 GLN B OE1 3430 N NE2 . GLN B 125 ? 2.0871 1.5356 1.9632 -0.8646 -0.1004 -0.3889 125 GLN B NE2 3431 N N . LEU B 126 ? 2.4491 1.4037 1.9947 -0.8124 -0.3022 -0.3264 126 LEU B N 3432 C CA . LEU B 126 ? 2.4854 1.3964 2.0345 -0.7968 -0.3389 -0.3407 126 LEU B CA 3433 C C . LEU B 126 ? 2.5651 1.3576 2.0743 -0.7497 -0.4065 -0.3449 126 LEU B C 3434 O O . LEU B 126 ? 2.4963 1.3325 2.0716 -0.6812 -0.4170 -0.3736 126 LEU B O 3435 C CB . LEU B 126 ? 2.3589 1.3934 2.0111 -0.7554 -0.3178 -0.3675 126 LEU B CB 3436 N N . ARG B 127 ? 2.7232 1.3617 2.1253 -0.7920 -0.4560 -0.3221 127 ARG B N 3437 C CA . ARG B 127 ? 2.8223 1.3255 2.1916 -0.7485 -0.5405 -0.3287 127 ARG B CA 3438 C C . ARG B 127 ? 2.8829 1.3220 2.2651 -0.7315 -0.5905 -0.3555 127 ARG B C 3439 O O . ARG B 127 ? 2.8205 1.3060 2.2953 -0.6621 -0.6050 -0.4030 127 ARG B O 3440 C CB . ARG B 127 ? 2.9912 1.3311 2.2197 -0.8067 -0.5877 -0.2854 127 ARG B CB 3441 N N . ASP B 128 ? 3.0125 1.3481 2.3004 -0.8019 -0.6122 -0.3305 128 ASP B N 3442 C CA . ASP B 128 ? 3.0957 1.3450 2.3799 -0.7930 -0.6696 -0.3516 128 ASP B CA 3443 C C . ASP B 128 ? 2.9794 1.3611 2.3523 -0.7808 -0.6166 -0.3830 128 ASP B C 3444 O O . ASP B 128 ? 2.9974 1.3549 2.4119 -0.7446 -0.6529 -0.4206 128 ASP B O 3445 C CB . ASP B 128 ? 3.2925 1.3691 2.4250 -0.8834 -0.7152 -0.3094 128 ASP B CB 3446 N N . ASN B 129 ? 2.8710 1.3870 2.2753 -0.8121 -0.5373 -0.3721 129 ASN B N 3447 C CA . ASN B 129 ? 2.7792 1.4079 2.2561 -0.8094 -0.4971 -0.3953 129 ASN B CA 3448 C C . ASN B 129 ? 2.6358 1.3984 2.2116 -0.7472 -0.4640 -0.4265 129 ASN B C 3449 O O . ASN B 129 ? 2.5571 1.4210 2.1814 -0.7559 -0.4268 -0.4342 129 ASN B O 3450 C CB . ASN B 129 ? 2.7638 1.4518 2.2291 -0.8844 -0.4445 -0.3741 129 ASN B CB 3451 N N . ALA B 130 ? 2.6186 1.3733 2.2194 -0.6901 -0.4831 -0.4462 130 ALA B N 3452 C CA . ALA B 130 ? 2.5023 1.3726 2.1797 -0.6418 -0.4504 -0.4801 130 ALA B CA 3453 C C . ALA B 130 ? 2.5162 1.3569 2.2298 -0.5808 -0.4832 -0.5233 130 ALA B C 3454 O O . ALA B 130 ? 2.5905 1.3352 2.2751 -0.5688 -0.5296 -0.5117 130 ALA B O 3455 C CB . ALA B 130 ? 2.4032 1.3727 2.0990 -0.6527 -0.3999 -0.4519 130 ALA B CB 3456 N N . LYS B 131 ? 2.4566 1.3766 2.2320 -0.5491 -0.4615 -0.5781 131 LYS B N 3457 C CA . LYS B 131 ? 2.4562 1.3808 2.2947 -0.4937 -0.4797 -0.6407 131 LYS B CA 3458 C C . LYS B 131 ? 2.3545 1.3874 2.2248 -0.4769 -0.4295 -0.6474 131 LYS B C 3459 O O . LYS B 131 ? 2.2867 1.4047 2.1451 -0.5034 -0.3810 -0.6330 131 LYS B O 3460 C CB . LYS B 131 ? 2.4852 1.4224 2.3732 -0.4810 -0.4849 -0.7188 131 LYS B CB 3461 C CG . LYS B 131 ? 2.4624 1.4551 2.4409 -0.4341 -0.4778 -0.8072 131 LYS B CG 3462 C CD . LYS B 131 ? 2.5074 1.5118 2.5425 -0.4288 -0.4805 -0.8994 131 LYS B CD 3463 C CE . LYS B 131 ? 2.4776 1.5697 2.6118 -0.3973 -0.4517 -1.0029 131 LYS B CE 3464 N NZ . LYS B 131 ? 2.5404 1.6355 2.7580 -0.3850 -0.4643 -1.1144 131 LYS B NZ 3465 N N . GLU B 132 ? 2.3563 1.3761 2.2663 -0.4336 -0.4504 -0.6705 132 GLU B N 3466 C CA . GLU B 132 ? 2.2675 1.3842 2.2121 -0.4147 -0.4066 -0.6853 132 GLU B CA 3467 C C . GLU B 132 ? 2.2526 1.4453 2.2645 -0.4000 -0.3785 -0.7788 132 GLU B C 3468 O O . GLU B 132 ? 2.3189 1.4766 2.3905 -0.3743 -0.4125 -0.8494 132 GLU B O 3469 C CB . GLU B 132 ? 2.2810 1.3478 2.2386 -0.3784 -0.4433 -0.6717 132 GLU B CB 3470 C CG . GLU B 132 ? 2.1858 1.3402 2.1501 -0.3719 -0.3965 -0.6529 132 GLU B CG 3471 C CD . GLU B 132 ? 2.2084 1.2988 2.1517 -0.3542 -0.4312 -0.6123 132 GLU B CD 3472 O OE1 . GLU B 132 ? 2.2611 1.2739 2.1283 -0.3878 -0.4508 -0.5485 132 GLU B OE1 3473 O OE2 . GLU B 132 ? 2.1818 1.2990 2.1799 -0.3135 -0.4369 -0.6476 132 GLU B OE2 3474 N N . LEU B 133 ? 2.1810 1.4727 2.1806 -0.4228 -0.3185 -0.7844 133 LEU B N 3475 C CA . LEU B 133 ? 2.1809 1.5474 2.2150 -0.4349 -0.2773 -0.8738 133 LEU B CA 3476 C C . LEU B 133 ? 2.1521 1.5753 2.2619 -0.3997 -0.2611 -0.9389 133 LEU B C 3477 O O . LEU B 133 ? 2.1902 1.6239 2.3921 -0.3718 -0.2721 -1.0364 133 LEU B O 3478 C CB . LEU B 133 ? 2.1558 1.5771 2.1098 -0.4958 -0.2294 -0.8466 133 LEU B CB 3479 C CG . LEU B 133 ? 2.2008 1.5848 2.1002 -0.5368 -0.2399 -0.8236 133 LEU B CG 3480 C CD1 . LEU B 133 ? 2.1890 1.6090 2.0060 -0.5942 -0.2125 -0.7873 133 LEU B CD1 3481 C CD2 . LEU B 133 ? 2.2703 1.6436 2.2077 -0.5392 -0.2415 -0.9134 133 LEU B CD2 3482 N N . GLY B 134 ? 2.0868 1.5507 2.1700 -0.4007 -0.2366 -0.8926 134 GLY B N 3483 C CA . GLY B 134 ? 2.0542 1.5762 2.2051 -0.3707 -0.2185 -0.9484 134 GLY B CA 3484 C C . GLY B 134 ? 1.9946 1.5903 2.0920 -0.4031 -0.1646 -0.9205 134 GLY B C 3485 O O . GLY B 134 ? 1.9519 1.5779 2.0855 -0.3748 -0.1589 -0.9250 134 GLY B O 3486 N N . ASN B 135 ? 2.0022 1.6166 2.0104 -0.4636 -0.1336 -0.8913 135 ASN B N 3487 C CA . ASN B 135 ? 1.9706 1.6332 1.9110 -0.5028 -0.0967 -0.8604 135 ASN B CA 3488 C C . ASN B 135 ? 1.9281 1.5602 1.8161 -0.5041 -0.1211 -0.7515 135 ASN B C 3489 O O . ASN B 135 ? 1.9287 1.5735 1.7454 -0.5475 -0.1111 -0.7153 135 ASN B O 3490 C CB . ASN B 135 ? 2.0348 1.7241 1.8981 -0.5796 -0.0568 -0.9053 135 ASN B CB 3491 C CG . ASN B 135 ? 2.0800 1.7153 1.8756 -0.6158 -0.0812 -0.8618 135 ASN B CG 3492 O OD1 . ASN B 135 ? 2.0825 1.6719 1.9164 -0.5829 -0.1171 -0.8404 135 ASN B OD1 3493 N ND2 . ASN B 135 ? 2.1333 1.7639 1.8198 -0.6890 -0.0674 -0.8480 135 ASN B ND2 3494 N N . GLY B 136 ? 1.9073 1.4947 1.8311 -0.4617 -0.1567 -0.7059 136 GLY B N 3495 C CA . GLY B 136 ? 1.8727 1.4433 1.7685 -0.4657 -0.1725 -0.6206 136 GLY B CA 3496 C C . GLY B 136 ? 1.9050 1.4447 1.7657 -0.5000 -0.1902 -0.5870 136 GLY B C 3497 O O . GLY B 136 ? 1.8848 1.4372 1.7240 -0.5217 -0.1958 -0.5393 136 GLY B O 3498 N N . CYS B 137 ? 1.9601 1.4593 1.8262 -0.5027 -0.2044 -0.6169 137 CYS B N 3499 C CA . CYS B 137 ? 1.9963 1.4648 1.8322 -0.5361 -0.2220 -0.5917 137 CYS B CA 3500 C C . CYS B 137 ? 2.0393 1.4414 1.8935 -0.5217 -0.2503 -0.5927 137 CYS B C 3501 O O . CYS B 137 ? 2.0675 1.4383 1.9545 -0.4881 -0.2638 -0.6296 137 CYS B O 3502 C CB . CYS B 137 ? 2.0449 1.5260 1.8341 -0.5796 -0.2090 -0.6313 137 CYS B CB 3503 S SG . CYS B 137 ? 2.0408 1.5635 1.7645 -0.6221 -0.1925 -0.6172 137 CYS B SG 3504 N N . PHE B 138 ? 2.0561 1.4317 1.8912 -0.5491 -0.2659 -0.5549 138 PHE B N 3505 C CA . PHE B 138 ? 2.1139 1.4166 1.9461 -0.5509 -0.2940 -0.5500 138 PHE B CA 3506 C C . PHE B 138 ? 2.1530 1.4433 1.9633 -0.5857 -0.3017 -0.5594 138 PHE B C 3507 O O . PHE B 138 ? 2.1317 1.4609 1.9267 -0.6149 -0.2946 -0.5435 138 PHE B O 3508 C CB . PHE B 138 ? 2.1082 1.3866 1.9338 -0.5623 -0.3003 -0.4952 138 PHE B CB 3509 C CG . PHE B 138 ? 2.0927 1.3610 1.9239 -0.5347 -0.2992 -0.4825 138 PHE B CG 3510 C CD1 . PHE B 138 ? 2.1648 1.3431 1.9798 -0.5169 -0.3345 -0.4879 138 PHE B CD1 3511 C CD2 . PHE B 138 ? 2.0144 1.3514 1.8631 -0.5279 -0.2723 -0.4644 138 PHE B CD2 3512 C CE1 . PHE B 138 ? 2.1606 1.3165 1.9713 -0.4951 -0.3427 -0.4739 138 PHE B CE1 3513 C CE2 . PHE B 138 ? 2.0027 1.3283 1.8524 -0.5047 -0.2714 -0.4525 138 PHE B CE2 3514 C CZ . PHE B 138 ? 2.0768 1.3110 1.9045 -0.4895 -0.3064 -0.4563 138 PHE B CZ 3515 N N . GLU B 139 ? 2.2189 1.4457 2.0271 -0.5824 -0.3254 -0.5851 139 GLU B N 3516 C CA . GLU B 139 ? 2.2641 1.4704 2.0505 -0.6145 -0.3351 -0.5969 139 GLU B CA 3517 C C . GLU B 139 ? 2.3138 1.4523 2.0857 -0.6326 -0.3623 -0.5616 139 GLU B C 3518 O O . GLU B 139 ? 2.3757 1.4382 2.1437 -0.6160 -0.3911 -0.5677 139 GLU B O 3519 C CB . GLU B 139 ? 2.3122 1.5042 2.1116 -0.6022 -0.3369 -0.6712 139 GLU B CB 3520 C CG . GLU B 139 ? 2.2992 1.5573 2.0824 -0.6234 -0.3004 -0.7159 139 GLU B CG 3521 C CD . GLU B 139 ? 2.3594 1.6130 2.1626 -0.6243 -0.2929 -0.8044 139 GLU B CD 3522 O OE1 . GLU B 139 ? 2.3770 1.6079 2.2462 -0.5799 -0.3101 -0.8528 139 GLU B OE1 3523 O OE2 . GLU B 139 ? 2.3969 1.6658 2.1525 -0.6716 -0.2743 -0.8306 139 GLU B OE2 3524 N N . PHE B 140 ? 2.3027 1.4622 2.0660 -0.6706 -0.3591 -0.5289 140 PHE B N 3525 C CA . PHE B 140 ? 2.3522 1.4592 2.1010 -0.7015 -0.3755 -0.5021 140 PHE B CA 3526 C C . PHE B 140 ? 2.4362 1.4754 2.1617 -0.7104 -0.4021 -0.5288 140 PHE B C 3527 O O . PHE B 140 ? 2.4454 1.5063 2.1695 -0.7165 -0.4004 -0.5579 140 PHE B O 3528 C CB . PHE B 140 ? 2.3121 1.4778 2.0862 -0.7381 -0.3643 -0.4755 140 PHE B CB 3529 C CG . PHE B 140 ? 2.2441 1.4707 2.0541 -0.7345 -0.3418 -0.4528 140 PHE B CG 3530 C CD1 . PHE B 140 ? 2.2603 1.4709 2.0683 -0.7583 -0.3286 -0.4326 140 PHE B CD1 3531 C CD2 . PHE B 140 ? 2.1767 1.4706 2.0136 -0.7158 -0.3341 -0.4543 140 PHE B CD2 3532 C CE1 . PHE B 140 ? 2.2017 1.4747 2.0482 -0.7589 -0.3028 -0.4207 140 PHE B CE1 3533 C CE2 . PHE B 140 ? 2.1160 1.4658 1.9945 -0.7098 -0.3168 -0.4377 140 PHE B CE2 3534 C CZ . PHE B 140 ? 2.1229 1.4686 2.0135 -0.7291 -0.2984 -0.4240 140 PHE B CZ 3535 N N . TYR B 141 ? 2.5132 1.4607 2.2099 -0.7178 -0.4300 -0.5184 141 TYR B N 3536 C CA . TYR B 141 ? 2.5986 1.4695 2.2721 -0.7307 -0.4625 -0.5382 141 TYR B CA 3537 C C . TYR B 141 ? 2.6138 1.4933 2.2730 -0.7848 -0.4566 -0.5131 141 TYR B C 3538 O O . TYR B 141 ? 2.6795 1.5043 2.3181 -0.8020 -0.4800 -0.5264 141 TYR B O 3539 C CB . TYR B 141 ? 2.6997 1.4457 2.3373 -0.7206 -0.5110 -0.5352 141 TYR B CB 3540 C CG . TYR B 141 ? 2.7064 1.4306 2.3829 -0.6599 -0.5366 -0.5828 141 TYR B CG 3541 C CD1 . TYR B 141 ? 2.7411 1.4497 2.4578 -0.6317 -0.5585 -0.6490 141 TYR B CD1 3542 C CD2 . TYR B 141 ? 2.6792 1.4046 2.3637 -0.6320 -0.5383 -0.5710 141 TYR B CD2 3543 C CE1 . TYR B 141 ? 2.7488 1.4521 2.5287 -0.5762 -0.5807 -0.7109 141 TYR B CE1 3544 C CE2 . TYR B 141 ? 2.6864 1.3984 2.4252 -0.5747 -0.5656 -0.6239 141 TYR B CE2 3545 C CZ . TYR B 141 ? 2.7216 1.4271 2.5162 -0.5463 -0.5864 -0.6982 141 TYR B CZ 3546 O OH . TYR B 141 ? 2.7297 1.4362 2.6047 -0.4894 -0.6120 -0.7683 141 TYR B OH 3547 N N . HIS B 142 ? 2.5529 1.5045 2.2352 -0.8100 -0.4276 -0.4843 142 HIS B N 3548 C CA . HIS B 142 ? 2.5580 1.5391 2.2571 -0.8592 -0.4214 -0.4725 142 HIS B CA 3549 C C . HIS B 142 ? 2.4707 1.5576 2.2318 -0.8566 -0.4074 -0.4738 142 HIS B C 3550 O O . HIS B 142 ? 2.4119 1.5403 2.1847 -0.8230 -0.4000 -0.4785 142 HIS B O 3551 C CB . HIS B 142 ? 2.6022 1.5544 2.2799 -0.9080 -0.4084 -0.4478 142 HIS B CB 3552 C CG . HIS B 142 ? 2.5440 1.5528 2.2465 -0.9059 -0.3765 -0.4338 142 HIS B CG 3553 N ND1 . HIS B 142 ? 2.5598 1.5196 2.2201 -0.8807 -0.3803 -0.4219 142 HIS B ND1 3554 C CD2 . HIS B 142 ? 2.4726 1.5823 2.2459 -0.9255 -0.3443 -0.4354 142 HIS B CD2 3555 C CE1 . HIS B 142 ? 2.4991 1.5268 2.1909 -0.8882 -0.3459 -0.4122 142 HIS B CE1 3556 N NE2 . HIS B 142 ? 2.4442 1.5663 2.2099 -0.9143 -0.3226 -0.4233 142 HIS B NE2 3557 N N . ARG B 143 ? 2.4738 1.5968 2.2756 -0.8942 -0.4111 -0.4727 143 ARG B N 3558 C CA . ARG B 143 ? 2.4154 1.6206 2.2850 -0.8932 -0.4201 -0.4762 143 ARG B CA 3559 C C . ARG B 143 ? 2.3557 1.6363 2.3002 -0.8971 -0.3959 -0.4718 143 ARG B C 3560 O O . ARG B 143 ? 2.3697 1.6690 2.3499 -0.9361 -0.3751 -0.4778 143 ARG B O 3561 C CB . ARG B 143 ? 2.4501 1.6581 2.3482 -0.9278 -0.4477 -0.4866 143 ARG B CB 3562 C CG . ARG B 143 ? 2.5220 1.6551 2.3474 -0.9332 -0.4687 -0.4953 143 ARG B CG 3563 C CD . ARG B 143 ? 2.5247 1.6414 2.2951 -0.9041 -0.4751 -0.5055 143 ARG B CD 3564 N NE . ARG B 143 ? 2.4916 1.6551 2.2820 -0.9040 -0.4961 -0.5004 143 ARG B NE 3565 C CZ . ARG B 143 ? 2.4845 1.6506 2.2289 -0.8892 -0.4938 -0.5051 143 ARG B CZ 3566 N NH1 . ARG B 143 ? 2.4928 1.6366 2.1896 -0.8680 -0.4645 -0.5250 143 ARG B NH1 3567 N NH2 . ARG B 143 ? 2.4782 1.6660 2.2271 -0.8992 -0.5261 -0.4943 143 ARG B NH2 3568 N N . CYS B 144 ? 2.3015 1.6261 2.2676 -0.8631 -0.3955 -0.4670 144 CYS B N 3569 C CA . CYS B 144 ? 2.2431 1.6435 2.2880 -0.8607 -0.3742 -0.4686 144 CYS B CA 3570 C C . CYS B 144 ? 2.1975 1.6619 2.3294 -0.8505 -0.4123 -0.4788 144 CYS B C 3571 O O . CYS B 144 ? 2.1752 1.6361 2.2808 -0.8221 -0.4342 -0.4678 144 CYS B O 3572 C CB . CYS B 144 ? 2.2196 1.6098 2.2204 -0.8279 -0.3479 -0.4535 144 CYS B CB 3573 S SG . CYS B 144 ? 2.1549 1.6317 2.2394 -0.8275 -0.3142 -0.4572 144 CYS B SG 3574 N N . ASP B 145 ? 2.1929 1.7099 2.4293 -0.8779 -0.4256 -0.5040 145 ASP B N 3575 C CA . ASP B 145 ? 2.1632 1.7321 2.5056 -0.8673 -0.4817 -0.5212 145 ASP B CA 3576 C C . ASP B 145 ? 2.0954 1.7334 2.5184 -0.8412 -0.4727 -0.5296 145 ASP B C 3577 O O . ASP B 145 ? 2.0656 1.7091 2.4477 -0.8321 -0.4195 -0.5177 145 ASP B O 3578 C CB . ASP B 145 ? 2.1769 1.7894 2.6338 -0.9015 -0.5019 -0.5597 145 ASP B CB 3579 C CG . ASP B 145 ? 2.1444 1.8396 2.7011 -0.9338 -0.4405 -0.5995 145 ASP B CG 3580 O OD1 . ASP B 145 ? 2.1558 1.8244 2.6281 -0.9538 -0.3776 -0.5848 145 ASP B OD1 3581 O OD2 . ASP B 145 ? 2.1162 1.8990 2.8358 -0.9446 -0.4583 -0.6511 145 ASP B OD2 3582 N N . ASN B 146 ? 2.0797 1.7621 2.6178 -0.8284 -0.5333 -0.5512 146 ASN B N 3583 C CA . ASN B 146 ? 2.0197 1.7642 2.6459 -0.8001 -0.5377 -0.5637 146 ASN B CA 3584 C C . ASN B 146 ? 1.9692 1.8072 2.6964 -0.8172 -0.4638 -0.6039 146 ASN B C 3585 O O . ASN B 146 ? 1.9266 1.7926 2.6523 -0.7991 -0.4294 -0.5983 146 ASN B O 3586 C CB . ASN B 146 ? 2.0324 1.7913 2.7742 -0.7836 -0.6376 -0.5851 146 ASN B CB 3587 C CG . ASN B 146 ? 2.1027 1.7539 2.7112 -0.7767 -0.7129 -0.5388 146 ASN B CG 3588 O OD1 . ASN B 146 ? 2.1182 1.7093 2.5687 -0.7758 -0.6800 -0.4988 146 ASN B OD1 3589 N ND2 . ASN B 146 ? 2.1583 1.7813 2.8299 -0.7779 -0.8175 -0.5500 146 ASN B ND2 3590 N N . GLU B 147 ? 1.9872 1.8715 2.7939 -0.8601 -0.4366 -0.6473 147 GLU B N 3591 C CA . GLU B 147 ? 1.9663 1.9323 2.8428 -0.9005 -0.3544 -0.6920 147 GLU B CA 3592 C C . GLU B 147 ? 1.9997 1.8979 2.7048 -0.9232 -0.2835 -0.6479 147 GLU B C 3593 O O . GLU B 147 ? 1.9849 1.9217 2.6946 -0.9450 -0.2230 -0.6624 147 GLU B O 3594 C CB . GLU B 147 ? 1.9919 2.0235 2.9895 -0.9543 -0.3402 -0.7571 147 GLU B CB 3595 C CG . GLU B 147 ? 1.9547 2.0848 3.1800 -0.9349 -0.4033 -0.8280 147 GLU B CG 3596 C CD . GLU B 147 ? 1.9735 2.1918 3.3441 -0.9932 -0.3756 -0.9105 147 GLU B CD 3597 O OE1 . GLU B 147 ? 2.0320 2.1955 3.3178 -1.0300 -0.3667 -0.8926 147 GLU B OE1 3598 O OE2 . GLU B 147 ? 1.9323 2.2797 3.5094 -1.0045 -0.3605 -1.0005 147 GLU B OE2 3599 N N . CYS B 148 ? 2.0553 1.8477 2.6128 -0.9200 -0.2974 -0.5991 148 CYS B N 3600 C CA . CYS B 148 ? 2.0977 1.8047 2.4965 -0.9259 -0.2577 -0.5557 148 CYS B CA 3601 C C . CYS B 148 ? 2.0476 1.7446 2.4046 -0.8728 -0.2607 -0.5256 148 CYS B C 3602 O O . CYS B 148 ? 2.0598 1.7321 2.3494 -0.8791 -0.2200 -0.5096 148 CYS B O 3603 C CB . CYS B 148 ? 2.1668 1.7695 2.4470 -0.9271 -0.2830 -0.5246 148 CYS B CB 3604 S SG . CYS B 148 ? 2.2169 1.7041 2.3280 -0.9061 -0.2697 -0.4777 148 CYS B SG 3605 N N . MET B 149 ? 2.0087 1.7150 2.3951 -0.8268 -0.3131 -0.5173 149 MET B N 3606 C CA . MET B 149 ? 1.9654 1.6640 2.3115 -0.7815 -0.3179 -0.4918 149 MET B CA 3607 C C . MET B 149 ? 1.8999 1.6838 2.3460 -0.7772 -0.2910 -0.5152 149 MET B C 3608 O O . MET B 149 ? 1.8738 1.6519 2.2733 -0.7569 -0.2641 -0.4963 149 MET B O 3609 C CB . MET B 149 ? 1.9726 1.6455 2.3029 -0.7527 -0.3833 -0.4782 149 MET B CB 3610 C CG . MET B 149 ? 1.9760 1.5980 2.1930 -0.7230 -0.3797 -0.4477 149 MET B CG 3611 S SD . MET B 149 ? 2.0428 1.5766 2.1270 -0.7288 -0.3596 -0.4358 149 MET B SD 3612 C CE . MET B 149 ? 2.1023 1.5970 2.1619 -0.7513 -0.4151 -0.4411 149 MET B CE 3613 N N . GLU B 150 ? 1.8736 1.7408 2.4680 -0.7964 -0.2994 -0.5641 150 GLU B N 3614 C CA . GLU B 150 ? 1.8194 1.7824 2.5313 -0.8041 -0.2627 -0.6064 150 GLU B CA 3615 C C . GLU B 150 ? 1.8419 1.7944 2.4749 -0.8500 -0.1799 -0.6039 150 GLU B C 3616 O O . GLU B 150 ? 1.8093 1.7885 2.4406 -0.8435 -0.1455 -0.6039 150 GLU B O 3617 C CB . GLU B 150 ? 1.8091 1.8702 2.7131 -0.8258 -0.2811 -0.6794 150 GLU B CB 3618 C CG . GLU B 150 ? 1.7910 1.8636 2.8001 -0.7793 -0.3799 -0.6898 150 GLU B CG 3619 C CD . GLU B 150 ? 1.8024 1.9446 2.9900 -0.7991 -0.4179 -0.7597 150 GLU B CD 3620 O OE1 . GLU B 150 ? 1.7935 2.0270 3.0874 -0.8458 -0.3539 -0.8259 150 GLU B OE1 3621 O OE2 . GLU B 150 ? 1.8303 1.9329 3.0490 -0.7744 -0.5130 -0.7524 150 GLU B OE2 3622 N N . SER B 151 ? 1.9088 1.8099 2.4651 -0.9010 -0.1546 -0.5996 151 SER B N 3623 C CA . SER B 151 ? 1.9746 1.8317 2.4235 -0.9605 -0.0902 -0.5913 151 SER B CA 3624 C C . SER B 151 ? 1.9801 1.7553 2.2951 -0.9264 -0.0886 -0.5358 151 SER B C 3625 O O . SER B 151 ? 2.0058 1.7768 2.2758 -0.9584 -0.0434 -0.5357 151 SER B O 3626 C CB . SER B 151 ? 2.0722 1.8523 2.4324 -1.0144 -0.0865 -0.5823 151 SER B CB 3627 O OG . SER B 151 ? 2.0646 1.9143 2.5486 -1.0375 -0.0983 -0.6312 151 SER B OG 3628 N N . VAL B 152 ? 1.9632 1.6749 2.2171 -0.8671 -0.1374 -0.4952 152 VAL B N 3629 C CA . VAL B 152 ? 1.9606 1.6035 2.1107 -0.8274 -0.1424 -0.4540 152 VAL B CA 3630 C C . VAL B 152 ? 1.8774 1.5908 2.0895 -0.7913 -0.1318 -0.4585 152 VAL B C 3631 O O . VAL B 152 ? 1.8825 1.5667 2.0324 -0.7859 -0.1103 -0.4396 152 VAL B O 3632 C CB . VAL B 152 ? 1.9688 1.5446 2.0577 -0.7811 -0.1891 -0.4294 152 VAL B CB 3633 C CG1 . VAL B 152 ? 1.9587 1.4878 1.9765 -0.7356 -0.1937 -0.4046 152 VAL B CG1 3634 C CG2 . VAL B 152 ? 2.0548 1.5502 2.0757 -0.8147 -0.2005 -0.4251 152 VAL B CG2 3635 N N . ARG B 153 ? 1.8089 1.6051 2.1419 -0.7670 -0.1561 -0.4831 153 ARG B N 3636 C CA . ARG B 153 ? 1.7323 1.6016 2.1463 -0.7381 -0.1520 -0.4959 153 ARG B CA 3637 C C . ARG B 153 ? 1.7295 1.6688 2.2096 -0.7863 -0.0927 -0.5370 153 ARG B C 3638 O O . ARG B 153 ? 1.6973 1.6616 2.1782 -0.7764 -0.0661 -0.5359 153 ARG B O 3639 C CB . ARG B 153 ? 1.6888 1.6091 2.2161 -0.7062 -0.2116 -0.5150 153 ARG B CB 3640 C CG . ARG B 153 ? 1.6852 1.5474 2.1362 -0.6613 -0.2624 -0.4753 153 ARG B CG 3641 C CD . ARG B 153 ? 1.7209 1.5569 2.1858 -0.6622 -0.3266 -0.4769 153 ARG B CD 3642 N NE . ARG B 153 ? 1.7037 1.6054 2.3237 -0.6649 -0.3704 -0.5181 153 ARG B NE 3643 C CZ . ARG B 153 ? 1.7407 1.6234 2.3988 -0.6711 -0.4360 -0.5277 153 ARG B CZ 3644 N NH1 . ARG B 153 ? 1.7952 1.5971 2.3360 -0.6809 -0.4571 -0.4973 153 ARG B NH1 3645 N NH2 . ARG B 153 ? 1.7288 1.6733 2.5512 -0.6678 -0.4852 -0.5742 153 ARG B NH2 3646 N N . ASN B 154 ? 1.7694 1.7423 2.3026 -0.8450 -0.0681 -0.5786 154 ASN B N 3647 C CA . ASN B 154 ? 1.7837 1.8337 2.3836 -0.9115 -0.0005 -0.6354 154 ASN B CA 3648 C C . ASN B 154 ? 1.8607 1.8322 2.2988 -0.9632 0.0527 -0.6050 154 ASN B C 3649 O O . ASN B 154 ? 1.8542 1.8718 2.3089 -0.9920 0.1015 -0.6297 154 ASN B O 3650 C CB . ASN B 154 ? 1.8203 1.9220 2.5091 -0.9707 0.0140 -0.6929 154 ASN B CB 3651 C CG . ASN B 154 ? 1.8333 2.0462 2.6305 -1.0459 0.0892 -0.7772 154 ASN B CG 3652 O OD1 . ASN B 154 ? 1.7825 2.0723 2.6643 -1.0333 0.1124 -0.8108 154 ASN B OD1 3653 N ND2 . ASN B 154 ? 1.9071 2.1332 2.7053 -1.1302 0.1310 -0.8190 154 ASN B ND2 3654 N N . GLY B 155 ? 1.9421 1.7870 2.2235 -0.9767 0.0358 -0.5536 155 GLY B N 3655 C CA . GLY B 155 ? 2.0449 1.7791 2.1546 -1.0258 0.0606 -0.5173 155 GLY B CA 3656 C C . GLY B 155 ? 2.1660 1.8751 2.2143 -1.1413 0.1108 -0.5456 155 GLY B C 3657 O O . GLY B 155 ? 2.1832 1.9110 2.2737 -1.1726 0.1098 -0.5714 155 GLY B O 3658 N N . ASP C 2 ? 2.5433 1.1335 2.8264 -0.6259 0.8890 -1.3151 1 ASP C N 3659 C CA . ASP C 2 ? 2.5526 1.1317 2.8217 -0.6538 0.8861 -1.3087 1 ASP C CA 3660 C C . ASP C 2 ? 2.4862 1.1121 2.7291 -0.6482 0.8519 -1.2642 1 ASP C C 3661 O O . ASP C 2 ? 2.4745 1.1274 2.7002 -0.6779 0.8449 -1.2700 1 ASP C O 3662 C CB . ASP C 2 ? 2.6132 1.0976 2.9103 -0.6482 0.9071 -1.2993 1 ASP C CB 3663 C CG . ASP C 2 ? 2.6855 1.1238 3.0067 -0.6679 0.9435 -1.3513 1 ASP C CG 3664 O OD1 . ASP C 2 ? 2.6945 1.1725 3.0026 -0.7026 0.9540 -1.3977 1 ASP C OD1 3665 O OD2 . ASP C 2 ? 2.7344 1.0940 3.0876 -0.6487 0.9606 -1.3456 1 ASP C OD2 3666 N N . GLN C 3 ? 2.4418 1.0791 2.6844 -0.6109 0.8310 -1.2223 2 GLN C N 3667 C CA . GLN C 3 ? 2.3865 1.0574 2.6082 -0.6025 0.8008 -1.1772 2 GLN C CA 3668 C C . GLN C 3 ? 2.3192 1.0533 2.5258 -0.5782 0.7739 -1.1549 2 GLN C C 3669 O O . GLN C 3 ? 2.3179 1.0478 2.5381 -0.5528 0.7775 -1.1556 2 GLN C O 3670 C CB . GLN C 3 ? 2.4089 1.0087 2.6429 -0.5819 0.8015 -1.1348 2 GLN C CB 3671 C CG . GLN C 3 ? 2.3689 0.9925 2.5809 -0.5838 0.7781 -1.0950 2 GLN C CG 3672 C CD . GLN C 3 ? 2.4078 0.9532 2.6233 -0.5755 0.7841 -1.0600 2 GLN C CD 3673 O OE1 . GLN C 3 ? 2.3738 0.9205 2.5762 -0.5574 0.7643 -1.0155 2 GLN C OE1 3674 N NE2 . GLN C 3 ? 2.4792 0.9536 2.7091 -0.5904 0.8116 -1.0800 2 GLN C NE2 3675 N N . ILE C 4 ? 2.2665 1.0587 2.4476 -0.5869 0.7476 -1.1364 3 ILE C N 3676 C CA . ILE C 4 ? 2.1988 1.0477 2.3630 -0.5641 0.7189 -1.1073 3 ILE C CA 3677 C C . ILE C 4 ? 2.1563 1.0127 2.3120 -0.5562 0.6968 -1.0623 3 ILE C C 3678 O O . ILE C 4 ? 2.1708 1.0177 2.3249 -0.5802 0.7001 -1.0652 3 ILE C O 3679 C CB . ILE C 4 ? 2.1756 1.0998 2.3120 -0.5852 0.7059 -1.1356 3 ILE C CB 3680 C CG1 . ILE C 4 ? 2.1127 1.0900 2.2305 -0.5612 0.6766 -1.1032 3 ILE C CG1 3681 C CG2 . ILE C 4 ? 2.1777 1.1331 2.3001 -0.6228 0.6985 -1.1546 3 ILE C CG2 3682 C CD1 . ILE C 4 ? 2.0997 1.1402 2.1864 -0.5773 0.6647 -1.1283 3 ILE C CD1 3683 N N . CYS C 5 ? 2.1024 0.9757 2.2537 -0.5241 0.6760 -1.0230 4 CYS C N 3684 C CA . CYS C 5 ? 2.0651 0.9411 2.2083 -0.5139 0.6566 -0.9789 4 CYS C CA 3685 C C . CYS C 5 ? 1.9941 0.9339 2.1207 -0.4949 0.6266 -0.9524 4 CYS C C 3686 O O . CYS C 5 ? 1.9722 0.9398 2.0958 -0.4811 0.6221 -0.9599 4 CYS C O 3687 C CB . CYS C 5 ? 2.0957 0.8941 2.2545 -0.4893 0.6656 -0.9474 4 CYS C CB 3688 S SG . CYS C 5 ? 2.1844 0.8947 2.3623 -0.5083 0.7006 -0.9727 4 CYS C SG 3689 N N . ILE C 6 ? 1.9577 0.9193 2.0737 -0.4958 0.6079 -0.9230 5 ILE C N 3690 C CA . ILE C 6 ? 1.8961 0.9098 1.9984 -0.4753 0.5793 -0.8919 5 ILE C CA 3691 C C . ILE C 6 ? 1.8866 0.8586 1.9947 -0.4422 0.5747 -0.8474 5 ILE C C 3692 O O . ILE C 6 ? 1.9231 0.8375 2.0368 -0.4436 0.5858 -0.8327 5 ILE C O 3693 C CB . ILE C 6 ? 1.8591 0.9264 1.9494 -0.4952 0.5597 -0.8874 5 ILE C CB 3694 C CG1 . ILE C 6 ? 1.8706 0.9801 1.9554 -0.5284 0.5595 -0.9311 5 ILE C CG1 3695 C CG2 . ILE C 6 ? 1.7956 0.9126 1.8732 -0.4729 0.5307 -0.8549 5 ILE C CG2 3696 C CD1 . ILE C 6 ? 1.8541 1.0093 1.9218 -0.5249 0.5479 -0.9481 5 ILE C CD1 3697 N N . GLY C 7 ? 1.8441 0.8433 1.9488 -0.4140 0.5580 -0.8263 6 GLY C N 3698 C CA . GLY C 7 ? 1.8331 0.8005 1.9426 -0.3813 0.5489 -0.7836 6 GLY C CA 3699 C C . GLY C 7 ? 1.7734 0.7947 1.8734 -0.3590 0.5245 -0.7608 6 GLY C C 3700 O O . GLY C 7 ? 1.7367 0.8186 1.8235 -0.3695 0.5138 -0.7759 6 GLY C O 3701 N N . TYR C 8 ? 1.7711 0.7680 1.8761 -0.3287 0.5147 -0.7240 7 TYR C N 3702 C CA . TYR C 8 ? 1.7163 0.7601 1.8128 -0.3069 0.4913 -0.6980 7 TYR C CA 3703 C C . TYR C 8 ? 1.7279 0.7432 1.8425 -0.2705 0.4878 -0.6768 7 TYR C C 3704 O O . TYR C 8 ? 1.7784 0.7315 1.9117 -0.2596 0.4997 -0.6746 7 TYR C O 3705 C CB . TYR C 8 ? 1.6817 0.7452 1.7597 -0.3122 0.4739 -0.6682 7 TYR C CB 3706 C CG . TYR C 8 ? 1.7085 0.7101 1.7850 -0.3068 0.4775 -0.6389 7 TYR C CG 3707 C CD1 . TYR C 8 ? 1.7548 0.7085 1.8315 -0.3302 0.4967 -0.6515 7 TYR C CD1 3708 C CD2 . TYR C 8 ? 1.6851 0.6743 1.7562 -0.2803 0.4615 -0.5985 7 TYR C CD2 3709 C CE1 . TYR C 8 ? 1.7885 0.6805 1.8567 -0.3281 0.5006 -0.6239 7 TYR C CE1 3710 C CE2 . TYR C 8 ? 1.7180 0.6466 1.7800 -0.2776 0.4636 -0.5708 7 TYR C CE2 3711 C CZ . TYR C 8 ? 1.7712 0.6497 1.8298 -0.3020 0.4836 -0.5831 7 TYR C CZ 3712 O OH . TYR C 8 ? 1.8090 0.6219 1.8520 -0.3022 0.4867 -0.5551 7 TYR C OH 3713 N N . HIS C 9 ? 1.6868 0.7481 1.7972 -0.2521 0.4702 -0.6615 8 HIS C N 3714 C CA . HIS C 9 ? 1.6941 0.7436 1.8260 -0.2182 0.4654 -0.6470 8 HIS C CA 3715 C C . HIS C 9 ? 1.7146 0.7180 1.8503 -0.1950 0.4531 -0.6056 8 HIS C C 3716 O O . HIS C 9 ? 1.7110 0.7120 1.8240 -0.2029 0.4424 -0.5804 8 HIS C O 3717 C CB . HIS C 9 ? 1.6411 0.7570 1.7637 -0.2097 0.4509 -0.6444 8 HIS C CB 3718 C CG . HIS C 9 ? 1.6322 0.7452 1.7789 -0.1764 0.4454 -0.6312 8 HIS C CG 3719 N ND1 . HIS C 9 ? 1.6492 0.7643 1.8215 -0.1685 0.4608 -0.6597 8 HIS C ND1 3720 C CD2 . HIS C 9 ? 1.6098 0.7201 1.7611 -0.1499 0.4265 -0.5945 8 HIS C CD2 3721 C CE1 . HIS C 9 ? 1.6355 0.7507 1.8311 -0.1379 0.4514 -0.6416 8 HIS C CE1 3722 N NE2 . HIS C 9 ? 1.6096 0.7216 1.7920 -0.1258 0.4295 -0.6014 8 HIS C NE2 3723 N N . ALA C 10 ? 1.7455 0.7129 1.9104 -0.1669 0.4541 -0.5998 9 ALA C N 3724 C CA . ALA C 10 ? 1.7663 0.6883 1.9351 -0.1414 0.4385 -0.5601 9 ALA C CA 3725 C C . ALA C 10 ? 1.7674 0.6877 1.9731 -0.1064 0.4318 -0.5574 9 ALA C C 3726 O O . ALA C 10 ? 1.7865 0.7068 2.0233 -0.1029 0.4481 -0.5901 9 ALA C O 3727 C CB . ALA C 10 ? 1.8339 0.6778 2.0013 -0.1493 0.4492 -0.5554 9 ALA C CB 3728 N N . ASN C 11 ? 1.7481 0.6682 1.9521 -0.0818 0.4085 -0.5207 10 ASN C N 3729 C CA . ASN C 11 ? 1.7500 0.6659 1.9938 -0.0465 0.3988 -0.5154 10 ASN C CA 3730 C C . ASN C 11 ? 1.7657 0.6410 2.0057 -0.0214 0.3733 -0.4706 10 ASN C C 3731 O O . ASN C 11 ? 1.7741 0.6360 1.9743 -0.0324 0.3628 -0.4419 10 ASN C O 3732 C CB . ASN C 11 ? 1.6897 0.6808 1.9416 -0.0413 0.3965 -0.5286 10 ASN C CB 3733 C CG . ASN C 11 ? 1.6337 0.6737 1.8468 -0.0487 0.3785 -0.5030 10 ASN C CG 3734 O OD1 . ASN C 11 ? 1.6355 0.6602 1.8157 -0.0615 0.3707 -0.4803 10 ASN C OD1 3735 N ND2 . ASN C 11 ? 1.5839 0.6826 1.8018 -0.0416 0.3734 -0.5083 10 ASN C ND2 3736 N N . ASN C 12 ? 1.7801 0.6360 2.0622 0.0114 0.3633 -0.4663 11 ASN C N 3737 C CA . ASN C 12 ? 1.7990 0.6165 2.0793 0.0377 0.3351 -0.4243 11 ASN C CA 3738 C C . ASN C 12 ? 1.7361 0.6105 1.9950 0.0437 0.3148 -0.3999 11 ASN C C 3739 O O . ASN C 12 ? 1.7102 0.6126 2.0003 0.0697 0.3013 -0.3964 11 ASN C O 3740 C CB . ASN C 12 ? 1.8373 0.6209 2.1764 0.0725 0.3280 -0.4300 11 ASN C CB 3741 C CG . ASN C 12 ? 1.9143 0.6314 2.2757 0.0694 0.3455 -0.4502 11 ASN C CG 3742 O OD1 . ASN C 12 ? 1.9367 0.6373 2.2706 0.0392 0.3659 -0.4640 11 ASN C OD1 3743 N ND2 . ASN C 12 ? 1.9546 0.6332 2.3695 0.1008 0.3372 -0.4531 11 ASN C ND2 3744 N N . SER C 13 ? 1.7098 0.6006 1.9184 0.0193 0.3134 -0.3844 12 SER C N 3745 C CA . SER C 13 ? 1.6426 0.5950 1.8288 0.0182 0.2995 -0.3681 12 SER C CA 3746 C C . SER C 13 ? 1.6494 0.5754 1.8064 0.0284 0.2744 -0.3233 12 SER C C 3747 O O . SER C 13 ? 1.6209 0.5727 1.7871 0.0502 0.2544 -0.3057 12 SER C O 3748 C CB . SER C 13 ? 1.6068 0.6031 1.7614 -0.0158 0.3140 -0.3843 12 SER C CB 3749 O OG . SER C 13 ? 1.5404 0.6021 1.6819 -0.0156 0.3027 -0.3763 12 SER C OG 3750 N N . THR C 14 ? 1.6865 0.5620 1.8060 0.0103 0.2766 -0.3063 13 THR C N 3751 C CA . THR C 14 ? 1.7048 0.5473 1.7865 0.0138 0.2560 -0.2644 13 THR C CA 3752 C C . THR C 14 ? 1.6418 0.5446 1.6980 0.0088 0.2442 -0.2481 13 THR C C 3753 O O . THR C 14 ? 1.6571 0.5373 1.6813 0.0113 0.2274 -0.2146 13 THR C O 3754 C CB . THR C 14 ? 1.7480 0.5391 1.8489 0.0479 0.2323 -0.2405 13 THR C CB 3755 O OG1 . THR C 14 ? 1.6966 0.5409 1.8292 0.0739 0.2158 -0.2396 13 THR C OG1 3756 C CG2 . THR C 14 ? 1.8094 0.5440 1.9454 0.0575 0.2423 -0.2588 13 THR C CG2 3757 N N . GLU C 15 ? 1.5747 0.5503 1.6421 0.0007 0.2526 -0.2711 14 GLU C N 3758 C CA . GLU C 15 ? 1.5072 0.5401 1.5531 -0.0046 0.2423 -0.2580 14 GLU C CA 3759 C C . GLU C 15 ? 1.5036 0.5314 1.5091 -0.0358 0.2509 -0.2519 14 GLU C C 3760 O O . GLU C 15 ? 1.5160 0.5364 1.5192 -0.0589 0.2704 -0.2743 14 GLU C O 3761 C CB . GLU C 15 ? 1.4498 0.5564 1.5176 -0.0044 0.2478 -0.2841 14 GLU C CB 3762 C CG . GLU C 15 ? 1.4407 0.5651 1.5474 0.0253 0.2386 -0.2883 14 GLU C CG 3763 C CD . GLU C 15 ? 1.3800 0.5786 1.4921 0.0258 0.2368 -0.2988 14 GLU C CD 3764 O OE1 . GLU C 15 ? 1.3520 0.5816 1.4387 0.0205 0.2253 -0.2801 14 GLU C OE1 3765 O OE2 . GLU C 15 ? 1.3685 0.5928 1.5092 0.0303 0.2477 -0.3264 14 GLU C OE2 3766 N N . GLN C 16 ? 1.4802 0.5140 1.4564 -0.0374 0.2374 -0.2238 15 GLN C N 3767 C CA . GLN C 16 ? 1.4876 0.5064 1.4263 -0.0661 0.2460 -0.2153 15 GLN C CA 3768 C C . GLN C 16 ? 1.4181 0.5038 1.3466 -0.0793 0.2439 -0.2169 15 GLN C C 3769 O O . GLN C 16 ? 1.3683 0.4995 1.3059 -0.0627 0.2292 -0.2098 15 GLN C O 3770 C CB . GLN C 16 ? 1.5430 0.4946 1.4483 -0.0624 0.2353 -0.1805 15 GLN C CB 3771 C CG . GLN C 16 ? 1.6234 0.4962 1.5309 -0.0573 0.2397 -0.1786 15 GLN C CG 3772 C CD . GLN C 16 ? 1.6905 0.4896 1.5533 -0.0608 0.2305 -0.1437 15 GLN C CD 3773 O OE1 . GLN C 16 ? 1.6793 0.4868 1.5127 -0.0611 0.2171 -0.1189 15 GLN C OE1 3774 N NE2 . GLN C 16 ? 1.7614 0.4848 1.6160 -0.0649 0.2378 -0.1415 15 GLN C NE2 3775 N N . VAL C 17 ? 1.4158 0.5061 1.3282 -0.1092 0.2588 -0.2272 16 VAL C N 3776 C CA . VAL C 17 ? 1.3592 0.5089 1.2655 -0.1236 0.2572 -0.2303 16 VAL C CA 3777 C C . VAL C 17 ? 1.3802 0.5053 1.2583 -0.1517 0.2690 -0.2237 16 VAL C C 3778 O O . VAL C 17 ? 1.4316 0.4949 1.2933 -0.1640 0.2814 -0.2204 16 VAL C O 3779 C CB . VAL C 17 ? 1.3201 0.5277 1.2506 -0.1334 0.2638 -0.2634 16 VAL C CB 3780 C CG1 . VAL C 17 ? 1.2987 0.5317 1.2533 -0.1096 0.2557 -0.2725 16 VAL C CG1 3781 C CG2 . VAL C 17 ? 1.3535 0.5372 1.2872 -0.1582 0.2845 -0.2886 16 VAL C CG2 3782 N N . ASP C 18 ? 1.3333 0.5069 1.2073 -0.1625 0.2661 -0.2229 17 ASP C N 3783 C CA . ASP C 18 ? 1.3510 0.5123 1.2036 -0.1907 0.2791 -0.2205 17 ASP C CA 3784 C C . ASP C 18 ? 1.3151 0.5305 1.1902 -0.2132 0.2892 -0.2508 17 ASP C C 3785 O O . ASP C 18 ? 1.2595 0.5303 1.1598 -0.2050 0.2802 -0.2671 17 ASP C O 3786 C CB . ASP C 18 ? 1.3391 0.5077 1.1686 -0.1856 0.2675 -0.1934 17 ASP C CB 3787 C CG . ASP C 18 ? 1.3850 0.4944 1.1868 -0.1671 0.2557 -0.1615 17 ASP C CG 3788 O OD1 . ASP C 18 ? 1.4536 0.4969 1.2403 -0.1705 0.2631 -0.1563 17 ASP C OD1 3789 O OD2 . ASP C 18 ? 1.3601 0.4882 1.1555 -0.1493 0.2378 -0.1417 17 ASP C OD2 3790 N N . THR C 19 ? 1.3528 0.5495 1.2176 -0.2427 0.3077 -0.2586 18 THR C N 3791 C CA . THR C 19 ? 1.3314 0.5774 1.2203 -0.2663 0.3169 -0.2874 18 THR C CA 3792 C C . THR C 19 ? 1.3526 0.5931 1.2257 -0.2894 0.3289 -0.2810 18 THR C C 3793 O O . THR C 19 ? 1.3806 0.5781 1.2193 -0.2871 0.3294 -0.2537 18 THR C O 3794 C CB . THR C 19 ? 1.3623 0.5895 1.2648 -0.2851 0.3343 -0.3158 18 THR C CB 3795 O OG1 . THR C 19 ? 1.4300 0.5877 1.3063 -0.3046 0.3548 -0.3087 18 THR C OG1 3796 C CG2 . THR C 19 ? 1.3607 0.5822 1.2747 -0.2644 0.3267 -0.3227 18 THR C CG2 3797 N N . ILE C 20 ? 1.3430 0.6264 1.2415 -0.3124 0.3383 -0.3070 19 ILE C N 3798 C CA . ILE C 20 ? 1.3650 0.6475 1.2553 -0.3375 0.3537 -0.3071 19 ILE C CA 3799 C C . ILE C 20 ? 1.4441 0.6476 1.2970 -0.3595 0.3778 -0.2981 19 ILE C C 3800 O O . ILE C 20 ? 1.4830 0.6506 1.2991 -0.3643 0.3824 -0.2743 19 ILE C O 3801 C CB . ILE C 20 ? 1.3321 0.6781 1.2663 -0.3580 0.3590 -0.3413 19 ILE C CB 3802 C CG1 . ILE C 20 ? 1.2683 0.6838 1.2263 -0.3397 0.3356 -0.3393 19 ILE C CG1 3803 C CG2 . ILE C 20 ? 1.3673 0.6947 1.2966 -0.3933 0.3866 -0.3516 19 ILE C CG2 3804 C CD1 . ILE C 20 ? 1.2360 0.7136 1.2387 -0.3572 0.3367 -0.3691 19 ILE C CD1 3805 N N . MET C 21 ? 1.4842 0.6570 1.3426 -0.3736 0.3927 -0.3162 20 MET C N 3806 C CA . MET C 21 ? 1.5664 0.6613 1.3887 -0.3981 0.4175 -0.3095 20 MET C CA 3807 C C . MET C 21 ? 1.6069 0.6273 1.3975 -0.3806 0.4125 -0.2864 20 MET C C 3808 O O . MET C 21 ? 1.6781 0.6243 1.4293 -0.3971 0.4284 -0.2727 20 MET C O 3809 C CB . MET C 21 ? 1.5960 0.6972 1.4425 -0.4332 0.4432 -0.3454 20 MET C CB 3810 C CG . MET C 21 ? 1.5911 0.7158 1.4737 -0.4288 0.4397 -0.3733 20 MET C CG 3811 S SD . MET C 21 ? 1.6305 0.7656 1.5422 -0.4734 0.4700 -0.4159 20 MET C SD 3812 C CE . MET C 21 ? 1.6454 0.7667 1.5747 -0.4672 0.4688 -0.4372 20 MET C CE 3813 N N . GLU C 22 ? 1.5648 0.6028 1.3722 -0.3478 0.3906 -0.2822 21 GLU C N 3814 C CA . GLU C 22 ? 1.6062 0.5796 1.3912 -0.3257 0.3818 -0.2595 21 GLU C CA 3815 C C . GLU C 22 ? 1.5646 0.5578 1.3475 -0.2891 0.3534 -0.2342 21 GLU C C 3816 O O . GLU C 22 ? 1.4929 0.5554 1.3057 -0.2740 0.3391 -0.2439 21 GLU C O 3817 C CB . GLU C 22 ? 1.6186 0.5832 1.4300 -0.3217 0.3869 -0.2829 21 GLU C CB 3818 C CG . GLU C 22 ? 1.6735 0.6009 1.4830 -0.3561 0.4152 -0.3052 21 GLU C CG 3819 C CD . GLU C 22 ? 1.7151 0.6029 1.5363 -0.3491 0.4203 -0.3178 21 GLU C CD 3820 O OE1 . GLU C 22 ? 1.6872 0.5950 1.5287 -0.3198 0.4033 -0.3184 21 GLU C OE1 3821 O OE2 . GLU C 22 ? 1.7804 0.6159 1.5910 -0.3741 0.4431 -0.3285 21 GLU C OE2 3822 N N . LYS C 23 ? 1.6098 0.5400 1.3565 -0.2759 0.3444 -0.2017 22 LYS C N 3823 C CA . LYS C 23 ? 1.5843 0.5237 1.3312 -0.2398 0.3168 -0.1780 22 LYS C CA 3824 C C . LYS C 23 ? 1.6367 0.5115 1.3795 -0.2191 0.3090 -0.1659 22 LYS C C 3825 O O . LYS C 23 ? 1.7030 0.5137 1.4292 -0.2347 0.3243 -0.1677 22 LYS C O 3826 C CB . LYS C 23 ? 1.5882 0.5185 1.2973 -0.2405 0.3075 -0.1485 22 LYS C CB 3827 N N . ASN C 24 ? 1.6070 0.4989 1.3679 -0.1842 0.2857 -0.1551 23 ASN C N 3828 C CA . ASN C 24 ? 1.6460 0.4856 1.4153 -0.1599 0.2756 -0.1468 23 ASN C CA 3829 C C . ASN C 24 ? 1.6568 0.4862 1.4547 -0.1678 0.2939 -0.1778 23 ASN C C 3830 O O . ASN C 24 ? 1.7266 0.4841 1.5120 -0.1727 0.3021 -0.1741 23 ASN C O 3831 C CB . ASN C 24 ? 1.7311 0.4816 1.4525 -0.1606 0.2688 -0.1127 23 ASN C CB 3832 C CG . ASN C 24 ? 1.7205 0.4768 1.4077 -0.1559 0.2512 -0.0824 23 ASN C CG 3833 O OD1 . ASN C 24 ? 1.7683 0.4802 1.4058 -0.1786 0.2581 -0.0645 23 ASN C OD1 3834 N ND2 . ASN C 24 ? 1.6605 0.4706 1.3725 -0.1282 0.2298 -0.0777 23 ASN C ND2 3835 N N . VAL C 25 ? 1.5890 0.4886 1.4227 -0.1699 0.2996 -0.2080 24 VAL C N 3836 C CA . VAL C 25 ? 1.5947 0.4957 1.4553 -0.1803 0.3172 -0.2416 24 VAL C CA 3837 C C . VAL C 25 ? 1.5647 0.4928 1.4633 -0.1520 0.3075 -0.2550 24 VAL C C 3838 O O . VAL C 25 ? 1.5014 0.4949 1.4168 -0.1399 0.2962 -0.2599 24 VAL C O 3839 C CB . VAL C 25 ? 1.5517 0.5119 1.4226 -0.2086 0.3316 -0.2699 24 VAL C CB 3840 C CG1 . VAL C 25 ? 1.5674 0.5281 1.4633 -0.2210 0.3486 -0.3053 24 VAL C CG1 3841 C CG2 . VAL C 25 ? 1.5755 0.5157 1.4150 -0.2383 0.3441 -0.2610 24 VAL C CG2 3842 N N . THR C 26 ? 1.6106 0.4876 1.5232 -0.1432 0.3134 -0.2624 25 THR C N 3843 C CA . THR C 26 ? 1.5908 0.4863 1.5422 -0.1169 0.3074 -0.2772 25 THR C CA 3844 C C . THR C 26 ? 1.5581 0.5077 1.5340 -0.1308 0.3224 -0.3170 25 THR C C 3845 O O . THR C 26 ? 1.5816 0.5198 1.5535 -0.1574 0.3413 -0.3377 25 THR C O 3846 C CB . THR C 26 ? 1.6556 0.4747 1.6179 -0.1018 0.3088 -0.2732 25 THR C CB 3847 O OG1 . THR C 26 ? 1.6943 0.4555 1.6277 -0.0905 0.2923 -0.2346 25 THR C OG1 3848 C CG2 . THR C 26 ? 1.6356 0.4768 1.6432 -0.0731 0.3029 -0.2892 25 THR C CG2 3849 N N . VAL C 27 ? 1.5101 0.5165 1.5097 -0.1138 0.3137 -0.3279 26 VAL C N 3850 C CA . VAL C 27 ? 1.4840 0.5413 1.5011 -0.1264 0.3252 -0.3644 26 VAL C CA 3851 C C . VAL C 27 ? 1.4850 0.5508 1.5350 -0.1056 0.3269 -0.3831 26 VAL C C 3852 O O . VAL C 27 ? 1.4948 0.5419 1.5599 -0.0778 0.3156 -0.3670 26 VAL C O 3853 C CB . VAL C 27 ? 1.4187 0.5494 1.4260 -0.1361 0.3161 -0.3660 26 VAL C CB 3854 C CG1 . VAL C 27 ? 1.4218 0.5502 1.4051 -0.1613 0.3195 -0.3577 26 VAL C CG1 3855 C CG2 . VAL C 27 ? 1.3750 0.5370 1.3844 -0.1103 0.2957 -0.3434 26 VAL C CG2 3856 N N . THR C 28 ? 1.4778 0.5727 1.5391 -0.1203 0.3412 -0.4186 27 THR C N 3857 C CA . THR C 28 ? 1.4757 0.5817 1.5667 -0.1065 0.3483 -0.4429 27 THR C CA 3858 C C . THR C 28 ? 1.4226 0.5898 1.5178 -0.0923 0.3354 -0.4402 27 THR C C 3859 O O . THR C 28 ? 1.4215 0.5913 1.5434 -0.0707 0.3351 -0.4456 27 THR C O 3860 C CB . THR C 28 ? 1.4896 0.6033 1.5851 -0.1310 0.3695 -0.4835 27 THR C CB 3861 O OG1 . THR C 28 ? 1.4427 0.6151 1.5177 -0.1522 0.3658 -0.4943 27 THR C OG1 3862 C CG2 . THR C 28 ? 1.5471 0.6012 1.6389 -0.1477 0.3843 -0.4887 27 THR C CG2 3863 N N . HIS C 29 ? 1.3780 0.5938 1.4494 -0.1054 0.3257 -0.4335 28 HIS C N 3864 C CA . HIS C 29 ? 1.3259 0.5975 1.3952 -0.0942 0.3121 -0.4270 28 HIS C CA 3865 C C . HIS C 29 ? 1.2854 0.5821 1.3310 -0.0976 0.2947 -0.3994 28 HIS C C 3866 O O . HIS C 29 ? 1.2887 0.5770 1.3180 -0.1168 0.2963 -0.3958 28 HIS C O 3867 C CB . HIS C 29 ? 1.3110 0.6276 1.3768 -0.1099 0.3205 -0.4594 28 HIS C CB 3868 C CG . HIS C 29 ? 1.3454 0.6461 1.4351 -0.1061 0.3389 -0.4891 28 HIS C CG 3869 N ND1 . HIS C 29 ? 1.3833 0.6594 1.4763 -0.1249 0.3577 -0.5178 28 HIS C ND1 3870 C CD2 . HIS C 29 ? 1.3448 0.6515 1.4593 -0.0865 0.3428 -0.4969 28 HIS C CD2 3871 C CE1 . HIS C 29 ? 1.4059 0.6727 1.5235 -0.1169 0.3729 -0.5420 28 HIS C CE1 3872 N NE2 . HIS C 29 ? 1.3802 0.6658 1.5127 -0.0937 0.3646 -0.5304 28 HIS C NE2 3873 N N . ALA C 30 ? 1.2461 0.5749 1.2924 -0.0800 0.2797 -0.3823 29 ALA C N 3874 C CA . ALA C 30 ? 1.2081 0.5623 1.2349 -0.0808 0.2632 -0.3565 29 ALA C CA 3875 C C . ALA C 30 ? 1.1639 0.5610 1.1945 -0.0635 0.2502 -0.3473 29 ALA C C 3876 O O . ALA C 30 ? 1.1730 0.5660 1.2245 -0.0445 0.2515 -0.3507 29 ALA C O 3877 C CB . ALA C 30 ? 1.2326 0.5400 1.2517 -0.0739 0.2578 -0.3277 29 ALA C CB 3878 N N . GLN C 31 ? 1.1210 0.5590 1.1344 -0.0704 0.2381 -0.3369 30 GLN C N 3879 C CA . GLN C 31 ? 1.0761 0.5548 1.0897 -0.0566 0.2257 -0.3273 30 GLN C CA 3880 C C . GLN C 31 ? 1.0484 0.5285 1.0537 -0.0461 0.2100 -0.2949 30 GLN C C 3881 O O . GLN C 31 ? 1.0327 0.5218 1.0222 -0.0594 0.2049 -0.2858 30 GLN C O 3882 C CB . GLN C 31 ? 1.0528 0.5797 1.0519 -0.0729 0.2231 -0.3434 30 GLN C CB 3883 C CG . GLN C 31 ? 1.0196 0.5856 1.0163 -0.0616 0.2136 -0.3379 30 GLN C CG 3884 C CD . GLN C 31 ? 1.0391 0.5969 1.0569 -0.0444 0.2226 -0.3465 30 GLN C CD 3885 O OE1 . GLN C 31 ? 1.0293 0.5973 1.0573 -0.0258 0.2147 -0.3311 30 GLN C OE1 3886 N NE2 . GLN C 31 ? 1.0752 0.6152 1.1031 -0.0509 0.2397 -0.3731 30 GLN C NE2 3887 N N . ASP C 32 ? 1.0367 0.5080 1.0548 -0.0227 0.2026 -0.2792 31 ASP C N 3888 C CA . ASP C 32 ? 1.0049 0.4860 1.0141 -0.0120 0.1863 -0.2504 31 ASP C CA 3889 C C . ASP C 32 ? 0.9515 0.4882 0.9517 -0.0172 0.1789 -0.2524 31 ASP C C 3890 O O . ASP C 32 ? 0.9350 0.4984 0.9416 -0.0171 0.1831 -0.2700 31 ASP C O 3891 C CB . ASP C 32 ? 1.0122 0.4755 1.0409 0.0147 0.1782 -0.2368 31 ASP C CB 3892 C CG . ASP C 32 ? 1.0015 0.4602 1.0172 0.0243 0.1611 -0.2053 31 ASP C CG 3893 O OD1 . ASP C 32 ? 0.9633 0.4594 0.9656 0.0192 0.1536 -0.1969 31 ASP C OD1 3894 O OD2 . ASP C 32 ? 1.0364 0.4518 1.0541 0.0367 0.1545 -0.1888 31 ASP C OD2 3895 N N . ILE C 33 ? 0.9226 0.4745 0.9068 -0.0234 0.1689 -0.2354 32 ILE C N 3896 C CA . ILE C 33 ? 0.8770 0.4780 0.8537 -0.0270 0.1597 -0.2347 32 ILE C CA 3897 C C . ILE C 33 ? 0.8453 0.4577 0.8177 -0.0149 0.1459 -0.2089 32 ILE C C 3898 O O . ILE C 33 ? 0.8199 0.4674 0.7846 -0.0194 0.1374 -0.2043 32 ILE C O 3899 C CB . ILE C 33 ? 0.8706 0.4901 0.8363 -0.0500 0.1604 -0.2465 32 ILE C CB 3900 C CG1 . ILE C 33 ? 0.8780 0.4791 0.8368 -0.0597 0.1604 -0.2338 32 ILE C CG1 3901 C CG2 . ILE C 33 ? 0.8989 0.5092 0.8673 -0.0631 0.1731 -0.2738 32 ILE C CG2 3902 C CD1 . ILE C 33 ? 0.8606 0.4902 0.8166 -0.0794 0.1577 -0.2442 32 ILE C CD1 3903 N N . LEU C 34 ? 0.8580 0.4398 0.8355 0.0004 0.1426 -0.1923 33 LEU C N 3904 C CA . LEU C 34 ? 0.8397 0.4262 0.8101 0.0107 0.1292 -0.1672 33 LEU C CA 3905 C C . LEU C 34 ? 0.8346 0.4203 0.8228 0.0343 0.1217 -0.1601 33 LEU C C 3906 O O . LEU C 34 ? 0.8683 0.4193 0.8695 0.0458 0.1231 -0.1600 33 LEU C O 3907 C CB . LEU C 34 ? 0.8684 0.4144 0.8213 0.0038 0.1290 -0.1504 33 LEU C CB 3908 C CG . LEU C 34 ? 0.8595 0.4054 0.7976 0.0094 0.1164 -0.1248 33 LEU C CG 3909 C CD1 . LEU C 34 ? 0.8130 0.4060 0.7463 0.0009 0.1123 -0.1246 33 LEU C CD1 3910 C CD2 . LEU C 34 ? 0.8995 0.3964 0.8143 -0.0004 0.1193 -0.1103 33 LEU C CD2 3911 N N . GLU C 35 ? 0.7964 0.4205 0.7877 0.0415 0.1134 -0.1552 34 GLU C N 3912 C CA . GLU C 35 ? 0.7894 0.4192 0.8005 0.0630 0.1054 -0.1489 34 GLU C CA 3913 C C . GLU C 35 ? 0.8040 0.4127 0.8060 0.0726 0.0905 -0.1221 34 GLU C C 3914 O O . GLU C 35 ? 0.7891 0.4067 0.7691 0.0632 0.0852 -0.1085 34 GLU C O 3915 C CB . GLU C 35 ? 0.7489 0.4271 0.7642 0.0640 0.1039 -0.1549 34 GLU C CB 3916 C CG . GLU C 35 ? 0.7397 0.4300 0.7810 0.0842 0.0987 -0.1539 34 GLU C CG 3917 C CD . GLU C 35 ? 0.7683 0.4377 0.8387 0.0949 0.1075 -0.1706 34 GLU C CD 3918 O OE1 . GLU C 35 ? 0.7712 0.4456 0.8446 0.0850 0.1230 -0.1938 34 GLU C OE1 3919 O OE2 . GLU C 35 ? 0.7875 0.4338 0.8775 0.1129 0.0981 -0.1608 34 GLU C OE2 3920 N N . LYS C 36 ? 0.8342 0.4145 0.8532 0.0910 0.0832 -0.1154 35 LYS C N 3921 C CA . LYS C 36 ? 0.8572 0.4119 0.8643 0.1009 0.0658 -0.0891 35 LYS C CA 3922 C C . LYS C 36 ? 0.8491 0.4183 0.8830 0.1244 0.0507 -0.0833 35 LYS C C 3923 O O . LYS C 36 ? 0.8727 0.4193 0.8985 0.1348 0.0330 -0.0619 35 LYS C O 3924 C CB . LYS C 36 ? 0.9149 0.4089 0.9112 0.1008 0.0651 -0.0807 35 LYS C CB 3925 C CG . LYS C 36 ? 0.9331 0.4058 0.8952 0.0760 0.0762 -0.0783 35 LYS C CG 3926 C CD . LYS C 36 ? 0.9395 0.4128 0.9111 0.0632 0.0955 -0.1034 35 LYS C CD 3927 C CE . LYS C 36 ? 0.9888 0.4111 0.9718 0.0702 0.0995 -0.1080 35 LYS C CE 3928 N NZ . LYS C 36 ? 0.9947 0.4202 0.9858 0.0556 0.1193 -0.1346 35 LYS C NZ 3929 N N . THR C 37 ? 0.8219 0.4282 0.8864 0.1315 0.0575 -0.1026 36 THR C N 3930 C CA . THR C 37 ? 0.8160 0.4385 0.9146 0.1534 0.0457 -0.1022 36 THR C CA 3931 C C . THR C 37 ? 0.7680 0.4440 0.8713 0.1513 0.0472 -0.1071 36 THR C C 3932 O O . THR C 37 ? 0.7391 0.4415 0.8301 0.1355 0.0612 -0.1195 36 THR C O 3933 C CB . THR C 37 ? 0.8375 0.4498 0.9791 0.1672 0.0534 -0.1237 36 THR C CB 3934 O OG1 . THR C 37 ? 0.8206 0.4592 0.9676 0.1541 0.0759 -0.1502 36 THR C OG1 3935 C CG2 . THR C 37 ? 0.8891 0.4438 1.0274 0.1709 0.0504 -0.1177 36 THR C CG2 3936 N N . HIS C 38 ? 0.7596 0.4488 0.8794 0.1669 0.0312 -0.0965 37 HIS C N 3937 C CA . HIS C 38 ? 0.7167 0.4540 0.8462 0.1671 0.0320 -0.1014 37 HIS C CA 3938 C C . HIS C 38 ? 0.7153 0.4644 0.8917 0.1894 0.0226 -0.1076 37 HIS C C 3939 O O . HIS C 38 ? 0.7496 0.4679 0.9451 0.2061 0.0084 -0.1008 37 HIS C O 3940 C CB . HIS C 38 ? 0.6985 0.4464 0.7941 0.1585 0.0212 -0.0799 37 HIS C CB 3941 C CG . HIS C 38 ? 0.7293 0.4453 0.8113 0.1670 0.0003 -0.0556 37 HIS C CG 3942 N ND1 . HIS C 38 ? 0.7295 0.4566 0.8245 0.1812 -0.0184 -0.0443 37 HIS C ND1 3943 C CD2 . HIS C 38 ? 0.7673 0.4386 0.8201 0.1614 -0.0047 -0.0404 37 HIS C CD2 3944 C CE1 . HIS C 38 ? 0.7630 0.4525 0.8346 0.1842 -0.0358 -0.0223 37 HIS C CE1 3945 N NE2 . HIS C 38 ? 0.7885 0.4423 0.8328 0.1718 -0.0269 -0.0192 37 HIS C NE2 3946 N N . ASN C 39 ? 0.6754 0.4679 0.8715 0.1894 0.0301 -0.1212 38 ASN C N 3947 C CA . ASN C 39 ? 0.6682 0.4794 0.9160 0.2088 0.0244 -0.1325 38 ASN C CA 3948 C C . ASN C 39 ? 0.6668 0.4829 0.9183 0.2217 -0.0015 -0.1112 38 ASN C C 3949 O O . ASN C 39 ? 0.6679 0.4973 0.9647 0.2399 -0.0121 -0.1177 38 ASN C O 3950 C CB . ASN C 39 ? 0.6355 0.4892 0.9029 0.2009 0.0462 -0.1584 38 ASN C CB 3951 C CG . ASN C 39 ? 0.5974 0.4854 0.8426 0.1902 0.0454 -0.1502 38 ASN C CG 3952 O OD1 . ASN C 39 ? 0.5829 0.4678 0.8050 0.1908 0.0281 -0.1269 38 ASN C OD1 3953 N ND2 . ASN C 39 ? 0.5776 0.4964 0.8281 0.1793 0.0652 -0.1701 38 ASN C ND2 3954 N N . GLY C 40 ? 0.6642 0.4707 0.8695 0.2113 -0.0113 -0.0877 39 GLY C N 3955 C CA . GLY C 40 ? 0.6731 0.4773 0.8722 0.2206 -0.0366 -0.0659 39 GLY C CA 3956 C C . GLY C 40 ? 0.6431 0.4937 0.8604 0.2226 -0.0391 -0.0703 39 GLY C C 3957 O O . GLY C 40 ? 0.6588 0.5123 0.8871 0.2349 -0.0612 -0.0585 39 GLY C O 3958 N N . LYS C 41 ? 0.6108 0.4956 0.8292 0.2098 -0.0174 -0.0870 40 LYS C N 3959 C CA . LYS C 41 ? 0.5821 0.5092 0.8156 0.2091 -0.0168 -0.0921 40 LYS C CA 3960 C C . LYS C 41 ? 0.5498 0.5001 0.7528 0.1879 0.0015 -0.0962 40 LYS C C 3961 O O . LYS C 41 ? 0.5452 0.4843 0.7230 0.1744 0.0159 -0.1006 40 LYS C O 3962 C CB . LYS C 41 ? 0.5916 0.5431 0.8856 0.2235 -0.0124 -0.1157 40 LYS C CB 3963 C CG . LYS C 41 ? 0.6159 0.5558 0.9385 0.2275 0.0039 -0.1382 40 LYS C CG 3964 C CD . LYS C 41 ? 0.6223 0.5823 1.0136 0.2469 0.0011 -0.1587 40 LYS C CD 3965 C CE . LYS C 41 ? 0.6327 0.5991 1.0576 0.2448 0.0277 -0.1908 40 LYS C CE 3966 N NZ . LYS C 41 ? 0.6688 0.6010 1.1231 0.2613 0.0212 -0.1959 40 LYS C NZ 3967 N N . LEU C 42 ? 0.5237 0.5049 0.7297 0.1854 -0.0010 -0.0944 41 LEU C N 3968 C CA . LEU C 42 ? 0.4985 0.5022 0.6796 0.1673 0.0137 -0.0978 41 LEU C CA 3969 C C . LEU C 42 ? 0.4935 0.5220 0.6990 0.1628 0.0347 -0.1230 41 LEU C C 3970 O O . LEU C 42 ? 0.4870 0.5379 0.7326 0.1722 0.0349 -0.1350 41 LEU C O 3971 C CB . LEU C 42 ? 0.4791 0.5014 0.6504 0.1655 0.0019 -0.0839 41 LEU C CB 3972 C CG . LEU C 42 ? 0.4882 0.4884 0.6335 0.1675 -0.0177 -0.0601 41 LEU C CG 3973 C CD1 . LEU C 42 ? 0.4738 0.4953 0.6063 0.1613 -0.0239 -0.0505 41 LEU C CD1 3974 C CD2 . LEU C 42 ? 0.4955 0.4673 0.6034 0.1561 -0.0129 -0.0519 41 LEU C CD2 3975 N N . CYS C 43 ? 0.5035 0.5279 0.6832 0.1470 0.0522 -0.1316 42 CYS C N 3976 C CA . CYS C 43 ? 0.5154 0.5557 0.7064 0.1380 0.0751 -0.1561 42 CYS C CA 3977 C C . CYS C 43 ? 0.4988 0.5537 0.6544 0.1183 0.0855 -0.1555 42 CYS C C 3978 O O . CYS C 43 ? 0.4783 0.5295 0.6018 0.1120 0.0752 -0.1368 42 CYS C O 3979 C CB . CYS C 43 ? 0.5485 0.5661 0.7339 0.1342 0.0867 -0.1682 42 CYS C CB 3980 S SG . CYS C 43 ? 0.5878 0.5823 0.8154 0.1570 0.0761 -0.1709 42 CYS C SG 3981 N N . ASP C 44 ? 0.5047 0.5744 0.6670 0.1082 0.1063 -0.1767 43 ASP C N 3982 C CA . ASP C 44 ? 0.5116 0.5850 0.6324 0.0866 0.1185 -0.1783 43 ASP C CA 3983 C C . ASP C 44 ? 0.5172 0.5663 0.5982 0.0766 0.1172 -0.1729 43 ASP C C 3984 O O . ASP C 44 ? 0.5264 0.5593 0.6166 0.0815 0.1191 -0.1799 43 ASP C O 3985 C CB . ASP C 44 ? 0.5328 0.6203 0.6646 0.0752 0.1442 -0.2049 43 ASP C CB 3986 C CG . ASP C 44 ? 0.5299 0.6458 0.7028 0.0818 0.1482 -0.2138 43 ASP C CG 3987 O OD1 . ASP C 44 ? 0.5190 0.6435 0.7111 0.0960 0.1290 -0.1987 43 ASP C OD1 3988 O OD2 . ASP C 44 ? 0.5494 0.6792 0.7354 0.0713 0.1714 -0.2373 43 ASP C OD2 3989 N N . LEU C 45 ? 0.5121 0.5585 0.5516 0.0627 0.1130 -0.1611 44 LEU C N 3990 C CA . LEU C 45 ? 0.5295 0.5562 0.5333 0.0523 0.1098 -0.1572 44 LEU C CA 3991 C C . LEU C 45 ? 0.5569 0.5813 0.5285 0.0322 0.1255 -0.1714 44 LEU C C 3992 O O . LEU C 45 ? 0.5492 0.5798 0.4960 0.0209 0.1261 -0.1664 44 LEU C O 3993 C CB . LEU C 45 ? 0.5115 0.5351 0.4942 0.0518 0.0909 -0.1346 44 LEU C CB 3994 C CG . LEU C 45 ? 0.5212 0.5275 0.4760 0.0434 0.0837 -0.1300 44 LEU C CG 3995 C CD1 . LEU C 45 ? 0.5323 0.5224 0.5031 0.0515 0.0836 -0.1342 44 LEU C CD1 3996 C CD2 . LEU C 45 ? 0.5007 0.5093 0.4423 0.0427 0.0673 -0.1110 44 LEU C CD2 3997 N N . ASP C 46 ? 0.5957 0.6089 0.5659 0.0267 0.1385 -0.1894 45 ASP C N 3998 C CA . ASP C 46 ? 0.6380 0.6457 0.5735 0.0053 0.1552 -0.2054 45 ASP C CA 3999 C C . ASP C 46 ? 0.6366 0.6601 0.5718 -0.0033 0.1705 -0.2138 45 ASP C C 4000 O O . ASP C 46 ? 0.6453 0.6641 0.5372 -0.0214 0.1728 -0.2104 45 ASP C O 4001 C CB . ASP C 46 ? 0.6666 0.6597 0.5516 -0.0085 0.1415 -0.1927 45 ASP C CB 4002 C CG . ASP C 46 ? 0.7340 0.7144 0.5768 -0.0312 0.1551 -0.2088 45 ASP C CG 4003 O OD1 . ASP C 46 ? 0.7629 0.7377 0.6154 -0.0345 0.1721 -0.2302 45 ASP C OD1 4004 O OD2 . ASP C 46 ? 0.7820 0.7560 0.5802 -0.0463 0.1486 -0.2003 45 ASP C OD2 4005 N N . GLY C 47 ? 0.6180 0.6591 0.6026 0.0095 0.1796 -0.2245 46 GLY C N 4006 C CA . GLY C 47 ? 0.6225 0.6817 0.6171 0.0012 0.1976 -0.2375 46 GLY C CA 4007 C C . GLY C 47 ? 0.5979 0.6709 0.5914 0.0038 0.1863 -0.2195 46 GLY C C 4008 O O . GLY C 47 ? 0.6071 0.6954 0.6093 -0.0040 0.2016 -0.2302 46 GLY C O 4009 N N . VAL C 48 ? 0.5746 0.6426 0.5587 0.0134 0.1616 -0.1943 47 VAL C N 4010 C CA . VAL C 48 ? 0.5509 0.6308 0.5337 0.0157 0.1505 -0.1773 47 VAL C CA 4011 C C . VAL C 48 ? 0.5178 0.6097 0.5433 0.0386 0.1335 -0.1663 47 VAL C C 4012 O O . VAL C 48 ? 0.5043 0.5844 0.5303 0.0489 0.1179 -0.1542 47 VAL C O 4013 C CB . VAL C 48 ? 0.5530 0.6169 0.4854 0.0045 0.1365 -0.1578 47 VAL C CB 4014 C CG1 . VAL C 48 ? 0.5333 0.6079 0.4680 0.0080 0.1249 -0.1410 47 VAL C CG1 4015 C CG2 . VAL C 48 ? 0.5920 0.6414 0.4772 -0.0191 0.1508 -0.1672 47 VAL C CG2 4016 N N . LYS C 49 ? 0.5075 0.6217 0.5664 0.0447 0.1368 -0.1712 48 LYS C N 4017 C CA . LYS C 49 ? 0.4911 0.6173 0.5910 0.0656 0.1206 -0.1633 48 LYS C CA 4018 C C . LYS C 49 ? 0.4664 0.5889 0.5470 0.0687 0.1000 -0.1383 48 LYS C C 4019 O O . LYS C 49 ? 0.4801 0.6047 0.5343 0.0567 0.1010 -0.1309 48 LYS C O 4020 C CB . LYS C 49 ? 0.4983 0.6523 0.6414 0.0697 0.1298 -0.1785 48 LYS C CB 4021 C CG . LYS C 49 ? 0.4971 0.6625 0.6856 0.0924 0.1108 -0.1730 48 LYS C CG 4022 C CD . LYS C 49 ? 0.4941 0.6907 0.7281 0.0971 0.1149 -0.1865 48 LYS C CD 4023 C CE . LYS C 49 ? 0.4853 0.6888 0.7461 0.1168 0.0881 -0.1720 48 LYS C CE 4024 N NZ . LYS C 49 ? 0.4946 0.7303 0.8083 0.1245 0.0879 -0.1869 48 LYS C NZ 4025 N N . PRO C 50 ? 0.4443 0.5594 0.5373 0.0838 0.0821 -0.1257 49 PRO C N 4026 C CA . PRO C 50 ? 0.4182 0.5307 0.4947 0.0853 0.0650 -0.1045 49 PRO C CA 4027 C C . PRO C 50 ? 0.3979 0.5324 0.4934 0.0890 0.0598 -0.1013 49 PRO C C 4028 O O . PRO C 50 ? 0.3870 0.5394 0.5182 0.0959 0.0642 -0.1140 49 PRO C O 4029 C CB . PRO C 50 ? 0.4192 0.5151 0.5029 0.0983 0.0508 -0.0952 49 PRO C CB 4030 C CG . PRO C 50 ? 0.4325 0.5316 0.5536 0.1103 0.0552 -0.1101 49 PRO C CG 4031 C CD . PRO C 50 ? 0.4467 0.5525 0.5670 0.0989 0.0772 -0.1304 49 PRO C CD 4032 N N . LEU C 51 ? 0.3814 0.5153 0.4559 0.0841 0.0507 -0.0860 50 LEU C N 4033 C CA . LEU C 51 ? 0.3691 0.5211 0.4589 0.0876 0.0431 -0.0810 50 LEU C CA 4034 C C . LEU C 51 ? 0.3688 0.5164 0.4722 0.1020 0.0247 -0.0708 50 LEU C C 4035 O O . LEU C 51 ? 0.3603 0.4917 0.4415 0.1011 0.0152 -0.0568 50 LEU C O 4036 C CB . LEU C 51 ? 0.3563 0.5072 0.4183 0.0760 0.0415 -0.0699 50 LEU C CB 4037 C CG . LEU C 51 ? 0.3377 0.5040 0.4113 0.0788 0.0322 -0.0632 50 LEU C CG 4038 C CD1 . LEU C 51 ? 0.3384 0.5290 0.4465 0.0827 0.0375 -0.0768 50 LEU C CD1 4039 C CD2 . LEU C 51 ? 0.3388 0.5032 0.3883 0.0665 0.0340 -0.0556 50 LEU C CD2 4040 N N . ILE C 52 ? 0.3763 0.5377 0.5159 0.1141 0.0195 -0.0784 51 ILE C N 4041 C CA . ILE C 52 ? 0.3903 0.5444 0.5419 0.1284 -0.0008 -0.0684 51 ILE C CA 4042 C C . ILE C 52 ? 0.3844 0.5563 0.5427 0.1293 -0.0129 -0.0621 51 ILE C C 4043 O O . ILE C 52 ? 0.3826 0.5790 0.5750 0.1343 -0.0136 -0.0734 51 ILE C O 4044 C CB . ILE C 52 ? 0.4073 0.5637 0.5991 0.1440 -0.0041 -0.0806 51 ILE C CB 4045 C CG1 . ILE C 52 ? 0.4240 0.5681 0.6153 0.1415 0.0123 -0.0928 51 ILE C CG1 4046 C CG2 . ILE C 52 ? 0.4216 0.5598 0.6162 0.1583 -0.0280 -0.0667 51 ILE C CG2 4047 C CD1 . ILE C 52 ? 0.4417 0.5536 0.6016 0.1401 0.0083 -0.0807 51 ILE C CD1 4048 N N . LEU C 53 ? 0.3810 0.5414 0.5092 0.1238 -0.0219 -0.0461 52 LEU C N 4049 C CA . LEU C 53 ? 0.3714 0.5473 0.4998 0.1210 -0.0309 -0.0409 52 LEU C CA 4050 C C . LEU C 53 ? 0.3823 0.5619 0.5308 0.1343 -0.0523 -0.0376 52 LEU C C 4051 O O . LEU C 53 ? 0.3704 0.5644 0.5214 0.1326 -0.0619 -0.0349 52 LEU C O 4052 C CB . LEU C 53 ? 0.3731 0.5355 0.4644 0.1095 -0.0316 -0.0276 52 LEU C CB 4053 C CG . LEU C 53 ? 0.3654 0.5248 0.4388 0.0971 -0.0151 -0.0299 52 LEU C CG 4054 C CD1 . LEU C 53 ? 0.3656 0.5135 0.4114 0.0877 -0.0170 -0.0190 52 LEU C CD1 4055 C CD2 . LEU C 53 ? 0.3589 0.5408 0.4463 0.0909 -0.0032 -0.0410 52 LEU C CD2 4056 N N . ARG C 54 ? 0.4013 0.5663 0.5635 0.1476 -0.0612 -0.0377 53 ARG C N 4057 C CA . ARG C 54 ? 0.4310 0.5972 0.6168 0.1629 -0.0847 -0.0352 53 ARG C CA 4058 C C . ARG C 54 ? 0.4364 0.5866 0.5879 0.1594 -0.1038 -0.0163 53 ARG C C 4059 O O . ARG C 54 ? 0.4511 0.5685 0.5688 0.1572 -0.1087 -0.0024 53 ARG C O 4060 C CB . ARG C 54 ? 0.4318 0.6359 0.6674 0.1690 -0.0843 -0.0533 53 ARG C CB 4061 C CG . ARG C 54 ? 0.4670 0.6747 0.7405 0.1887 -0.1095 -0.0553 53 ARG C CG 4062 C CD . ARG C 54 ? 0.4673 0.7158 0.7998 0.1948 -0.1058 -0.0783 53 ARG C CD 4063 N NE . ARG C 54 ? 0.4707 0.7292 0.8295 0.1933 -0.0796 -0.0986 53 ARG C NE 4064 C CZ . ARG C 54 ? 0.4684 0.7577 0.8846 0.1996 -0.0720 -0.1229 53 ARG C CZ 4065 N NH1 . ARG C 54 ? 0.4740 0.7899 0.9332 0.2099 -0.0907 -0.1304 53 ARG C NH1 4066 N NH2 . ARG C 54 ? 0.4624 0.7565 0.8938 0.1946 -0.0451 -0.1414 53 ARG C NH2 4067 N N . ASP C 55 ? 0.4312 0.6033 0.5895 0.1569 -0.1132 -0.0170 54 ASP C N 4068 C CA . ASP C 55 ? 0.4397 0.5979 0.5621 0.1504 -0.1293 -0.0012 54 ASP C CA 4069 C C . ASP C 55 ? 0.4119 0.5815 0.5110 0.1319 -0.1138 -0.0013 54 ASP C C 4070 O O . ASP C 55 ? 0.4088 0.5758 0.4843 0.1240 -0.1234 0.0065 54 ASP C O 4071 C CB . ASP C 55 ? 0.4580 0.6281 0.6033 0.1623 -0.1571 -0.0007 54 ASP C CB 4072 C CG . ASP C 55 ? 0.4929 0.6441 0.6583 0.1818 -0.1768 0.0023 54 ASP C CG 4073 O OD1 . ASP C 55 ? 0.5201 0.6325 0.6523 0.1821 -0.1815 0.0166 54 ASP C OD1 4074 O OD2 . ASP C 55 ? 0.4990 0.6735 0.7159 0.1968 -0.1870 -0.0105 54 ASP C OD2 4075 N N . CYS C 56 ? 0.3897 0.5689 0.4934 0.1244 -0.0903 -0.0102 55 CYS C N 4076 C CA . CYS C 56 ? 0.3763 0.5636 0.4617 0.1085 -0.0761 -0.0107 55 CYS C CA 4077 C C . CYS C 56 ? 0.3572 0.5195 0.4091 0.0991 -0.0655 -0.0026 55 CYS C C 4078 O O . CYS C 56 ? 0.3445 0.4899 0.3931 0.1032 -0.0614 -0.0016 55 CYS C O 4079 C CB . CYS C 56 ? 0.3722 0.5862 0.4837 0.1049 -0.0593 -0.0255 55 CYS C CB 4080 S SG . CYS C 56 ? 0.4262 0.6763 0.5808 0.1110 -0.0679 -0.0388 55 CYS C SG 4081 N N . SER C 57 ? 0.3444 0.5054 0.3745 0.0862 -0.0611 0.0012 56 SER C N 4082 C CA . SER C 57 ? 0.3371 0.4809 0.3441 0.0764 -0.0497 0.0050 56 SER C CA 4083 C C . SER C 57 ? 0.3068 0.4638 0.3248 0.0715 -0.0342 -0.0031 56 SER C C 4084 O O . SER C 57 ? 0.3041 0.4816 0.3421 0.0730 -0.0310 -0.0108 56 SER C O 4085 C CB . SER C 57 ? 0.3429 0.4789 0.3248 0.0645 -0.0515 0.0107 56 SER C CB 4086 O OG . SER C 57 ? 0.3322 0.4896 0.3226 0.0578 -0.0479 0.0050 56 SER C OG 4087 N N . VAL C 58 ? 0.2871 0.4315 0.2922 0.0650 -0.0253 -0.0018 57 VAL C N 4088 C CA . VAL C 58 ? 0.2713 0.4233 0.2809 0.0593 -0.0143 -0.0071 57 VAL C CA 4089 C C . VAL C 58 ? 0.2593 0.4261 0.2730 0.0519 -0.0119 -0.0094 57 VAL C C 4090 O O . VAL C 58 ? 0.2496 0.4277 0.2729 0.0497 -0.0054 -0.0147 57 VAL C O 4091 C CB . VAL C 58 ? 0.2735 0.4096 0.2705 0.0539 -0.0095 -0.0051 57 VAL C CB 4092 C CG1 . VAL C 58 ? 0.2573 0.3981 0.2565 0.0478 -0.0028 -0.0083 57 VAL C CG1 4093 C CG2 . VAL C 58 ? 0.2866 0.4092 0.2810 0.0597 -0.0093 -0.0052 57 VAL C CG2 4094 N N . ALA C 59 ? 0.2618 0.4266 0.2659 0.0465 -0.0159 -0.0061 58 ALA C N 4095 C CA . ALA C 59 ? 0.2555 0.4331 0.2632 0.0385 -0.0132 -0.0095 58 ALA C CA 4096 C C . ALA C 59 ? 0.2487 0.4469 0.2729 0.0421 -0.0170 -0.0143 58 ALA C C 4097 O O . ALA C 59 ? 0.2274 0.4384 0.2621 0.0371 -0.0100 -0.0201 58 ALA C O 4098 C CB . ALA C 59 ? 0.2687 0.4392 0.2606 0.0306 -0.0158 -0.0069 58 ALA C CB 4099 N N . GLY C 60 ? 0.2518 0.4519 0.2797 0.0508 -0.0284 -0.0125 59 GLY C N 4100 C CA . GLY C 60 ? 0.2581 0.4801 0.3084 0.0558 -0.0345 -0.0189 59 GLY C CA 4101 C C . GLY C 60 ? 0.2464 0.4809 0.3174 0.0572 -0.0226 -0.0281 59 GLY C C 4102 O O . GLY C 60 ? 0.2454 0.5000 0.3342 0.0538 -0.0185 -0.0367 59 GLY C O 4103 N N . TRP C 61 ? 0.2488 0.4698 0.3149 0.0603 -0.0160 -0.0270 60 TRP C N 4104 C CA . TRP C 61 ? 0.2417 0.4688 0.3188 0.0589 -0.0030 -0.0354 60 TRP C CA 4105 C C . TRP C 61 ? 0.2346 0.4606 0.3019 0.0464 0.0087 -0.0364 60 TRP C C 4106 O O . TRP C 61 ? 0.2346 0.4739 0.3136 0.0410 0.0177 -0.0448 60 TRP C O 4107 C CB . TRP C 61 ? 0.2440 0.4539 0.3131 0.0641 -0.0004 -0.0336 60 TRP C CB 4108 C CG . TRP C 61 ? 0.2439 0.4510 0.3097 0.0582 0.0141 -0.0400 60 TRP C CG 4109 C CD1 . TRP C 61 ? 0.2460 0.4675 0.3252 0.0533 0.0256 -0.0510 60 TRP C CD1 4110 C CD2 . TRP C 61 ? 0.2460 0.4330 0.2911 0.0552 0.0185 -0.0363 60 TRP C CD2 4111 N NE1 . TRP C 61 ? 0.2522 0.4608 0.3148 0.0461 0.0375 -0.0534 60 TRP C NE1 4112 C CE2 . TRP C 61 ? 0.2515 0.4393 0.2934 0.0479 0.0317 -0.0442 60 TRP C CE2 4113 C CE3 . TRP C 61 ? 0.2490 0.4173 0.2775 0.0567 0.0127 -0.0282 60 TRP C CE3 4114 C CZ2 . TRP C 61 ? 0.2593 0.4287 0.2790 0.0426 0.0367 -0.0428 60 TRP C CZ2 4115 C CZ3 . TRP C 61 ? 0.2491 0.4025 0.2614 0.0524 0.0176 -0.0281 60 TRP C CZ3 4116 C CH2 . TRP C 61 ? 0.2595 0.4130 0.2661 0.0458 0.0282 -0.0347 60 TRP C CH2 4117 N N . LEU C 62 ? 0.2280 0.4374 0.2757 0.0415 0.0085 -0.0286 61 LEU C N 4118 C CA . LEU C 62 ? 0.2267 0.4296 0.2656 0.0318 0.0170 -0.0283 61 LEU C CA 4119 C C . LEU C 62 ? 0.2217 0.4374 0.2686 0.0245 0.0193 -0.0317 61 LEU C C 4120 O O . LEU C 62 ? 0.2301 0.4461 0.2771 0.0167 0.0283 -0.0351 61 LEU C O 4121 C CB . LEU C 62 ? 0.2291 0.4122 0.2522 0.0303 0.0143 -0.0209 61 LEU C CB 4122 C CG . LEU C 62 ? 0.2374 0.4064 0.2513 0.0356 0.0124 -0.0183 61 LEU C CG 4123 C CD1 . LEU C 62 ? 0.2395 0.3933 0.2442 0.0339 0.0084 -0.0132 61 LEU C CD1 4124 C CD2 . LEU C 62 ? 0.2476 0.4125 0.2557 0.0333 0.0199 -0.0219 61 LEU C CD2 4125 N N . LEU C 63 ? 0.2250 0.4489 0.2757 0.0255 0.0114 -0.0311 62 LEU C N 4126 C CA . LEU C 63 ? 0.2250 0.4625 0.2836 0.0178 0.0132 -0.0361 62 LEU C CA 4127 C C . LEU C 63 ? 0.2290 0.4895 0.3083 0.0181 0.0148 -0.0456 62 LEU C C 4128 O O . LEU C 63 ? 0.2274 0.4983 0.3149 0.0093 0.0216 -0.0521 62 LEU C O 4129 C CB . LEU C 63 ? 0.2298 0.4676 0.2814 0.0166 0.0043 -0.0334 62 LEU C CB 4130 C CG . LEU C 63 ? 0.2314 0.4513 0.2693 0.0118 0.0073 -0.0291 62 LEU C CG 4131 C CD1 . LEU C 63 ? 0.2429 0.4579 0.2679 0.0107 0.0002 -0.0261 62 LEU C CD1 4132 C CD2 . LEU C 63 ? 0.2324 0.4533 0.2757 0.0020 0.0158 -0.0338 62 LEU C CD2 4133 N N . GLY C 64 ? 0.2288 0.4975 0.3199 0.0280 0.0087 -0.0479 63 GLY C N 4134 C CA . GLY C 64 ? 0.2315 0.5245 0.3501 0.0295 0.0106 -0.0598 63 GLY C CA 4135 C C . GLY C 64 ? 0.2376 0.5497 0.3720 0.0345 -0.0054 -0.0628 63 GLY C C 4136 O O . GLY C 64 ? 0.2193 0.5540 0.3748 0.0300 -0.0043 -0.0734 63 GLY C O 4137 N N . ASN C 65 ? 0.2585 0.5595 0.3805 0.0429 -0.0210 -0.0533 64 ASN C N 4138 C CA . ASN C 65 ? 0.2812 0.5938 0.4124 0.0496 -0.0409 -0.0533 64 ASN C CA 4139 C C . ASN C 65 ? 0.2941 0.6335 0.4666 0.0575 -0.0434 -0.0670 64 ASN C C 4140 O O . ASN C 65 ? 0.2922 0.6304 0.4785 0.0642 -0.0358 -0.0712 64 ASN C O 4141 C CB . ASN C 65 ? 0.2964 0.5853 0.4059 0.0583 -0.0545 -0.0402 64 ASN C CB 4142 C CG . ASN C 65 ? 0.3157 0.6077 0.4244 0.0646 -0.0789 -0.0362 64 ASN C CG 4143 O OD1 . ASN C 65 ? 0.3172 0.6328 0.4553 0.0703 -0.0897 -0.0449 64 ASN C OD1 4144 N ND2 . ASN C 65 ? 0.3348 0.6012 0.4090 0.0631 -0.0883 -0.0232 64 ASN C ND2 4145 N N . PRO C 66 ? 0.3053 0.6704 0.4996 0.0555 -0.0525 -0.0761 65 PRO C N 4146 C CA . PRO C 66 ? 0.3164 0.7123 0.5580 0.0621 -0.0549 -0.0927 65 PRO C CA 4147 C C . PRO C 66 ? 0.3493 0.7452 0.6134 0.0806 -0.0695 -0.0931 65 PRO C C 4148 O O . PRO C 66 ? 0.3507 0.7676 0.6559 0.0859 -0.0626 -0.1090 65 PRO C O 4149 C CB . PRO C 66 ? 0.3175 0.7357 0.5709 0.0581 -0.0706 -0.0983 65 PRO C CB 4150 C CG . PRO C 66 ? 0.3133 0.7153 0.5272 0.0437 -0.0651 -0.0893 65 PRO C CG 4151 C CD . PRO C 66 ? 0.3102 0.6779 0.4874 0.0444 -0.0581 -0.0740 65 PRO C CD 4152 N N . MET C 67 ? 0.3922 0.7636 0.6305 0.0895 -0.0882 -0.0769 66 MET C N 4153 C CA . MET C 67 ? 0.4216 0.7855 0.6771 0.1076 -0.1029 -0.0748 66 MET C CA 4154 C C . MET C 67 ? 0.4121 0.7607 0.6652 0.1097 -0.0830 -0.0758 66 MET C C 4155 O O . MET C 67 ? 0.4201 0.7631 0.6921 0.1239 -0.0902 -0.0774 66 MET C O 4156 C CB . MET C 67 ? 0.4726 0.8080 0.6930 0.1135 -0.1276 -0.0554 66 MET C CB 4157 C CG . MET C 67 ? 0.5047 0.8464 0.7122 0.1088 -0.1490 -0.0509 66 MET C CG 4158 S SD . MET C 67 ? 0.5582 0.9448 0.8261 0.1170 -0.1654 -0.0703 66 MET C SD 4159 C CE . MET C 67 ? 0.5695 0.9537 0.8783 0.1422 -0.1830 -0.0728 66 MET C CE 4160 N N . CYS C 68 ? 0.3885 0.7283 0.6175 0.0956 -0.0597 -0.0748 67 CYS C N 4161 C CA . CYS C 68 ? 0.3809 0.7027 0.5980 0.0949 -0.0423 -0.0740 67 CYS C CA 4162 C C . CYS C 68 ? 0.3611 0.6997 0.5981 0.0860 -0.0178 -0.0908 67 CYS C C 4163 O O . CYS C 68 ? 0.3510 0.6734 0.5668 0.0786 -0.0005 -0.0893 67 CYS C O 4164 C CB . CYS C 68 ? 0.3787 0.6723 0.5489 0.0857 -0.0375 -0.0583 67 CYS C CB 4165 S SG . CYS C 68 ? 0.4051 0.6727 0.5449 0.0919 -0.0600 -0.0398 67 CYS C SG 4166 N N . ASP C 69 ? 0.3470 0.7169 0.6233 0.0857 -0.0166 -0.1071 68 ASP C N 4167 C CA . ASP C 69 ? 0.3419 0.7278 0.6357 0.0737 0.0090 -0.1249 68 ASP C CA 4168 C C . ASP C 69 ? 0.3372 0.7158 0.6386 0.0761 0.0246 -0.1339 68 ASP C C 4169 O O . ASP C 69 ? 0.3446 0.7188 0.6338 0.0618 0.0487 -0.1413 68 ASP C O 4170 C CB . ASP C 69 ? 0.3492 0.7731 0.6906 0.0730 0.0071 -0.1438 68 ASP C CB 4171 C CG . ASP C 69 ? 0.3581 0.7898 0.6864 0.0595 0.0074 -0.1412 68 ASP C CG 4172 O OD1 . ASP C 69 ? 0.3576 0.7661 0.6435 0.0538 0.0042 -0.1238 68 ASP C OD1 4173 O OD2 . ASP C 69 ? 0.3755 0.8376 0.7392 0.0539 0.0120 -0.1585 68 ASP C OD2 4174 N N . GLU C 70 ? 0.3344 0.7084 0.6524 0.0931 0.0107 -0.1329 69 GLU C N 4175 C CA . GLU C 70 ? 0.3420 0.7039 0.6624 0.0964 0.0238 -0.1397 69 GLU C CA 4176 C C . GLU C 70 ? 0.3370 0.6712 0.6078 0.0820 0.0417 -0.1309 69 GLU C C 4177 O O . GLU C 70 ? 0.3636 0.6932 0.6338 0.0761 0.0609 -0.1421 69 GLU C O 4178 C CB . GLU C 70 ? 0.3600 0.7077 0.6876 0.1162 0.0017 -0.1307 69 GLU C CB 4179 C CG . GLU C 70 ? 0.3832 0.7190 0.7198 0.1219 0.0126 -0.1394 69 GLU C CG 4180 C CD . GLU C 70 ? 0.4128 0.7321 0.7581 0.1418 -0.0106 -0.1299 69 GLU C CD 4181 O OE1 . GLU C 70 ? 0.4333 0.7486 0.7735 0.1502 -0.0360 -0.1155 69 GLU C OE1 4182 O OE2 . GLU C 70 ? 0.4248 0.7325 0.7793 0.1478 -0.0034 -0.1369 69 GLU C OE2 4183 N N . PHE C 71 ? 0.3187 0.6346 0.5491 0.0760 0.0350 -0.1120 70 PHE C N 4184 C CA . PHE C 71 ? 0.3114 0.5996 0.4972 0.0654 0.0454 -0.1017 70 PHE C CA 4185 C C . PHE C 71 ? 0.3101 0.5952 0.4720 0.0482 0.0568 -0.0987 70 PHE C C 4186 O O . PHE C 71 ? 0.3035 0.5661 0.4300 0.0426 0.0555 -0.0852 70 PHE C O 4187 C CB . PHE C 71 ? 0.3033 0.5687 0.4633 0.0730 0.0282 -0.0827 70 PHE C CB 4188 C CG . PHE C 71 ? 0.3034 0.5662 0.4818 0.0898 0.0133 -0.0816 70 PHE C CG 4189 C CD1 . PHE C 71 ? 0.3171 0.5724 0.5048 0.0955 0.0201 -0.0896 70 PHE C CD1 4190 C CD2 . PHE C 71 ? 0.3000 0.5649 0.4840 0.0991 -0.0078 -0.0727 70 PHE C CD2 4191 C CE1 . PHE C 71 ? 0.3274 0.5768 0.5333 0.1116 0.0057 -0.0882 70 PHE C CE1 4192 C CE2 . PHE C 71 ? 0.3151 0.5721 0.5125 0.1145 -0.0236 -0.0697 70 PHE C CE2 4193 C CZ . PHE C 71 ? 0.3227 0.5716 0.5328 0.1215 -0.0171 -0.0773 70 PHE C CZ 4194 N N . LEU C 72 ? 0.3183 0.6250 0.5011 0.0398 0.0676 -0.1118 71 LEU C N 4195 C CA . LEU C 72 ? 0.3218 0.6220 0.4812 0.0231 0.0781 -0.1083 71 LEU C CA 4196 C C . LEU C 72 ? 0.3399 0.6142 0.4623 0.0092 0.0947 -0.1060 71 LEU C C 4197 O O . LEU C 72 ? 0.3396 0.5946 0.4306 -0.0003 0.0953 -0.0945 71 LEU C O 4198 C CB . LEU C 72 ? 0.3215 0.6504 0.5126 0.0155 0.0875 -0.1246 71 LEU C CB 4199 C CG . LEU C 72 ? 0.3078 0.6588 0.5248 0.0244 0.0686 -0.1237 71 LEU C CG 4200 C CD1 . LEU C 72 ? 0.3005 0.6856 0.5603 0.0193 0.0771 -0.1448 71 LEU C CD1 4201 C CD2 . LEU C 72 ? 0.3050 0.6408 0.4918 0.0187 0.0610 -0.1077 71 LEU C CD2 4202 N N . ASN C 73 ? 0.3530 0.6264 0.4796 0.0079 0.1073 -0.1176 72 ASN C N 4203 C CA . ASN C 73 ? 0.3777 0.6256 0.4658 -0.0067 0.1231 -0.1174 72 ASN C CA 4204 C C . ASN C 73 ? 0.3841 0.6272 0.4755 0.0000 0.1262 -0.1245 72 ASN C C 4205 O O . ASN C 73 ? 0.3853 0.6401 0.4954 -0.0051 0.1440 -0.1440 72 ASN C O 4206 C CB . ASN C 73 ? 0.4016 0.6553 0.4888 -0.0266 0.1477 -0.1325 72 ASN C CB 4207 C CG . ASN C 73 ? 0.4012 0.6539 0.4796 -0.0365 0.1475 -0.1256 72 ASN C CG 4208 O OD1 . ASN C 73 ? 0.4097 0.6359 0.4512 -0.0414 0.1405 -0.1085 72 ASN C OD1 4209 N ND2 . ASN C 73 ? 0.3988 0.6807 0.5142 -0.0394 0.1549 -0.1404 72 ASN C ND2 4210 N N . VAL C 74 ? 0.3743 0.6002 0.4494 0.0106 0.1103 -0.1104 73 VAL C N 4211 C CA . VAL C 74 ? 0.3748 0.5950 0.4547 0.0184 0.1114 -0.1166 73 VAL C CA 4212 C C . VAL C 74 ? 0.3909 0.5861 0.4297 0.0036 0.1249 -0.1183 73 VAL C C 4213 O O . VAL C 74 ? 0.4014 0.5768 0.4011 -0.0092 0.1255 -0.1078 73 VAL C O 4214 C CB . VAL C 74 ? 0.3621 0.5746 0.4445 0.0356 0.0893 -0.1025 73 VAL C CB 4215 C CG1 . VAL C 74 ? 0.3425 0.5764 0.4606 0.0493 0.0748 -0.1012 73 VAL C CG1 4216 C CG2 . VAL C 74 ? 0.3588 0.5473 0.4018 0.0312 0.0790 -0.0837 73 VAL C CG2 4217 N N . PRO C 75 ? 0.3933 0.5878 0.4407 0.0051 0.1348 -0.1321 74 PRO C N 4218 C CA . PRO C 75 ? 0.4194 0.5888 0.4241 -0.0094 0.1460 -0.1340 74 PRO C CA 4219 C C . PRO C 75 ? 0.4117 0.5587 0.3903 -0.0026 0.1279 -0.1178 74 PRO C C 4220 O O . PRO C 75 ? 0.3860 0.5372 0.3818 0.0132 0.1097 -0.1069 74 PRO C O 4221 C CB . PRO C 75 ? 0.4344 0.6161 0.4664 -0.0102 0.1654 -0.1589 74 PRO C CB 4222 C CG . PRO C 75 ? 0.4088 0.6142 0.4968 0.0127 0.1531 -0.1628 74 PRO C CG 4223 C CD . PRO C 75 ? 0.3836 0.6009 0.4820 0.0192 0.1371 -0.1488 74 PRO C CD 4224 N N . GLU C 76 ? 0.4383 0.5611 0.3740 -0.0162 0.1335 -0.1173 75 GLU C N 4225 C CA . GLU C 76 ? 0.4355 0.5380 0.3474 -0.0122 0.1183 -0.1061 75 GLU C CA 4226 C C . GLU C 76 ? 0.4156 0.5266 0.3613 0.0056 0.1117 -0.1101 75 GLU C C 4227 O O . GLU C 76 ? 0.4132 0.5364 0.3875 0.0097 0.1242 -0.1271 75 GLU C O 4228 C CB . GLU C 76 ? 0.4772 0.5563 0.3444 -0.0300 0.1287 -0.1123 75 GLU C CB 4229 C CG . GLU C 76 ? 0.4874 0.5457 0.3273 -0.0281 0.1104 -0.0999 75 GLU C CG 4230 C CD . GLU C 76 ? 0.5285 0.5648 0.3262 -0.0444 0.1183 -0.1078 75 GLU C CD 4231 O OE1 . GLU C 76 ? 0.5679 0.5948 0.3360 -0.0633 0.1351 -0.1158 75 GLU C OE1 4232 O OE2 . GLU C 76 ? 0.5346 0.5618 0.3269 -0.0395 0.1077 -0.1061 75 GLU C OE2 4233 N N . TRP C 77 ? 0.4047 0.5077 0.3476 0.0155 0.0925 -0.0952 76 TRP C N 4234 C CA . TRP C 77 ? 0.4025 0.5073 0.3708 0.0308 0.0852 -0.0963 76 TRP C CA 4235 C C . TRP C 77 ? 0.4163 0.5002 0.3605 0.0289 0.0776 -0.0917 76 TRP C C 4236 O O . TRP C 77 ? 0.4089 0.4796 0.3208 0.0191 0.0715 -0.0837 76 TRP C O 4237 C CB . TRP C 77 ? 0.3771 0.4934 0.3703 0.0445 0.0707 -0.0849 76 TRP C CB 4238 C CG . TRP C 77 ? 0.3710 0.4792 0.3437 0.0418 0.0572 -0.0683 76 TRP C CG 4239 C CD1 . TRP C 77 ? 0.3633 0.4577 0.3242 0.0439 0.0458 -0.0593 76 TRP C CD1 4240 C CD2 . TRP C 77 ? 0.3633 0.4773 0.3291 0.0359 0.0549 -0.0609 76 TRP C CD2 4241 N NE1 . TRP C 77 ? 0.3596 0.4523 0.3094 0.0402 0.0367 -0.0480 76 TRP C NE1 4242 C CE2 . TRP C 77 ? 0.3530 0.4564 0.3050 0.0358 0.0416 -0.0481 76 TRP C CE2 4243 C CE3 . TRP C 77 ? 0.3674 0.4945 0.3393 0.0299 0.0640 -0.0654 76 TRP C CE3 4244 C CZ2 . TRP C 77 ? 0.3482 0.4526 0.2935 0.0313 0.0364 -0.0395 76 TRP C CZ2 4245 C CZ3 . TRP C 77 ? 0.3582 0.4847 0.3198 0.0246 0.0587 -0.0555 76 TRP C CZ3 4246 C CH2 . TRP C 77 ? 0.3495 0.4644 0.2986 0.0259 0.0448 -0.0427 76 TRP C CH2 4247 N N . SER C 78 ? 0.4271 0.5079 0.3898 0.0388 0.0773 -0.0975 77 SER C N 4248 C CA . SER C 78 ? 0.4370 0.4998 0.3842 0.0381 0.0708 -0.0952 77 SER C CA 4249 C C . SER C 78 ? 0.4201 0.4798 0.3756 0.0478 0.0546 -0.0807 77 SER C C 4250 O O . SER C 78 ? 0.4416 0.4893 0.3805 0.0440 0.0463 -0.0750 77 SER C O 4251 C CB . SER C 78 ? 0.4534 0.5117 0.4166 0.0424 0.0814 -0.1108 77 SER C CB 4252 O OG . SER C 78 ? 0.4447 0.5149 0.4474 0.0573 0.0817 -0.1140 77 SER C OG 4253 N N . TYR C 79 ? 0.3926 0.4629 0.3741 0.0594 0.0502 -0.0761 78 TYR C N 4254 C CA . TYR C 79 ? 0.3711 0.4377 0.3556 0.0656 0.0367 -0.0623 78 TYR C CA 4255 C C . TYR C 79 ? 0.3597 0.4409 0.3654 0.0744 0.0320 -0.0576 78 TYR C C 4256 O O . TYR C 79 ? 0.3669 0.4616 0.3918 0.0782 0.0383 -0.0664 78 TYR C O 4257 C CB . TYR C 79 ? 0.3776 0.4268 0.3641 0.0706 0.0332 -0.0618 78 TYR C CB 4258 C CG . TYR C 79 ? 0.3844 0.4302 0.3938 0.0813 0.0373 -0.0702 78 TYR C CG 4259 C CD1 . TYR C 79 ? 0.4021 0.4461 0.4156 0.0790 0.0500 -0.0860 78 TYR C CD1 4260 C CD2 . TYR C 79 ? 0.3794 0.4215 0.4055 0.0933 0.0280 -0.0627 78 TYR C CD2 4261 C CE1 . TYR C 79 ? 0.4115 0.4525 0.4523 0.0901 0.0538 -0.0957 78 TYR C CE1 4262 C CE2 . TYR C 79 ? 0.3958 0.4324 0.4458 0.1051 0.0285 -0.0697 78 TYR C CE2 4263 C CZ . TYR C 79 ? 0.4098 0.4469 0.4706 0.1043 0.0417 -0.0869 78 TYR C CZ 4264 O OH . TYR C 79 ? 0.4309 0.4629 0.5220 0.1173 0.0421 -0.0955 78 TYR C OH 4265 N N . ILE C 80 ? 0.3443 0.4234 0.3469 0.0762 0.0214 -0.0453 79 ILE C N 4266 C CA . ILE C 80 ? 0.3366 0.4278 0.3530 0.0823 0.0146 -0.0396 79 ILE C CA 4267 C C . ILE C 80 ? 0.3484 0.4263 0.3703 0.0916 0.0049 -0.0330 79 ILE C C 4268 O O . ILE C 80 ? 0.3460 0.4053 0.3538 0.0890 0.0029 -0.0282 79 ILE C O 4269 C CB . ILE C 80 ? 0.3190 0.4166 0.3234 0.0746 0.0109 -0.0313 79 ILE C CB 4270 C CG1 . ILE C 80 ? 0.3210 0.4258 0.3166 0.0653 0.0190 -0.0362 79 ILE C CG1 4271 C CG2 . ILE C 80 ? 0.3075 0.4172 0.3238 0.0793 0.0039 -0.0264 79 ILE C CG2 4272 C CD1 . ILE C 80 ? 0.3137 0.4237 0.3015 0.0587 0.0155 -0.0293 79 ILE C CD1 4273 N N . VAL C 81 ? 0.3565 0.4427 0.3990 0.1019 -0.0014 -0.0335 80 VAL C N 4274 C CA . VAL C 81 ? 0.3804 0.4507 0.4257 0.1115 -0.0140 -0.0254 80 VAL C CA 4275 C C . VAL C 81 ? 0.3860 0.4656 0.4315 0.1131 -0.0261 -0.0165 80 VAL C C 4276 O O . VAL C 81 ? 0.3835 0.4860 0.4487 0.1163 -0.0272 -0.0221 80 VAL C O 4277 C CB . VAL C 81 ? 0.3955 0.4632 0.4683 0.1250 -0.0155 -0.0342 80 VAL C CB 4278 C CG1 . VAL C 81 ? 0.4184 0.4654 0.4914 0.1356 -0.0328 -0.0229 80 VAL C CG1 4279 C CG2 . VAL C 81 ? 0.4023 0.4581 0.4728 0.1222 -0.0027 -0.0442 80 VAL C CG2 4280 N N . GLU C 82 ? 0.4100 0.4708 0.4325 0.1095 -0.0341 -0.0041 81 GLU C N 4281 C CA . GLU C 82 ? 0.4308 0.4952 0.4438 0.1073 -0.0450 0.0049 81 GLU C CA 4282 C C . GLU C 82 ? 0.4711 0.5062 0.4683 0.1120 -0.0588 0.0165 81 GLU C C 4283 O O . GLU C 82 ? 0.4811 0.4912 0.4644 0.1099 -0.0551 0.0194 81 GLU C O 4284 C CB . GLU C 82 ? 0.4338 0.5006 0.4262 0.0925 -0.0371 0.0076 81 GLU C CB 4285 C CG . GLU C 82 ? 0.4546 0.5311 0.4388 0.0870 -0.0434 0.0127 81 GLU C CG 4286 C CD . GLU C 82 ? 0.4646 0.5427 0.4340 0.0727 -0.0337 0.0126 81 GLU C CD 4287 O OE1 . GLU C 82 ? 0.4725 0.5334 0.4279 0.0661 -0.0280 0.0141 81 GLU C OE1 4288 O OE2 . GLU C 82 ? 0.4704 0.5677 0.4458 0.0681 -0.0314 0.0096 81 GLU C OE2 4289 N N . LYS C 83 ? 0.4922 0.5287 0.4904 0.1178 -0.0754 0.0232 82 LYS C N 4290 C CA . LYS C 83 ? 0.5316 0.5354 0.5057 0.1200 -0.0912 0.0372 82 LYS C CA 4291 C C . LYS C 83 ? 0.5410 0.5271 0.4739 0.1020 -0.0861 0.0461 82 LYS C C 4292 O O . LYS C 83 ? 0.5078 0.5126 0.4367 0.0907 -0.0758 0.0418 82 LYS C O 4293 C CB . LYS C 83 ? 0.5514 0.5617 0.5377 0.1313 -0.1140 0.0417 82 LYS C CB 4294 C CG . LYS C 83 ? 0.5558 0.5776 0.5864 0.1507 -0.1218 0.0326 82 LYS C CG 4295 C CD . LYS C 83 ? 0.5765 0.6071 0.6233 0.1624 -0.1474 0.0362 82 LYS C CD 4296 C CE . LYS C 83 ? 0.5888 0.6266 0.6845 0.1834 -0.1575 0.0265 82 LYS C CE 4297 N NZ . LYS C 83 ? 0.5549 0.6240 0.6890 0.1845 -0.1345 0.0057 82 LYS C NZ 4298 N N . ILE C 84 ? 0.5876 0.5360 0.4906 0.0989 -0.0928 0.0576 83 ILE C N 4299 C CA . ILE C 84 ? 0.6155 0.5427 0.4772 0.0799 -0.0864 0.0649 83 ILE C CA 4300 C C . ILE C 84 ? 0.6121 0.5548 0.4606 0.0710 -0.0913 0.0670 83 ILE C C 4301 O O . ILE C 84 ? 0.5917 0.5439 0.4303 0.0558 -0.0764 0.0619 83 ILE C O 4302 C CB . ILE C 84 ? 0.6847 0.5639 0.5119 0.0779 -0.0960 0.0789 83 ILE C CB 4303 C CG1 . ILE C 84 ? 0.6952 0.5561 0.5261 0.0771 -0.0822 0.0745 83 ILE C CG1 4304 C CG2 . ILE C 84 ? 0.7212 0.5779 0.5002 0.0574 -0.0945 0.0879 83 ILE C CG2 4305 C CD1 . ILE C 84 ? 0.6904 0.5527 0.5557 0.0973 -0.0887 0.0701 83 ILE C CD1 4306 N N . ASN C 85 ? 0.6363 0.5824 0.4877 0.0808 -0.1127 0.0730 84 ASN C N 4307 C CA . ASN C 85 ? 0.6477 0.6103 0.4884 0.0730 -0.1194 0.0738 84 ASN C CA 4308 C C . ASN C 85 ? 0.6191 0.6177 0.5005 0.0879 -0.1313 0.0665 84 ASN C C 4309 O O . ASN C 85 ? 0.6422 0.6367 0.5273 0.0989 -0.1551 0.0728 84 ASN C O 4310 C CB . ASN C 85 ? 0.7281 0.6546 0.5200 0.0643 -0.1361 0.0893 84 ASN C CB 4311 C CG . ASN C 85 ? 0.7515 0.6916 0.5237 0.0510 -0.1395 0.0888 84 ASN C CG 4312 O OD1 . ASN C 85 ? 0.7369 0.7085 0.5267 0.0440 -0.1237 0.0767 84 ASN C OD1 4313 N ND2 . ASN C 85 ? 0.8061 0.7199 0.5397 0.0468 -0.1609 0.1021 84 ASN C ND2 4314 N N . PRO C 86 ? 0.5654 0.5985 0.4777 0.0876 -0.1152 0.0529 85 PRO C N 4315 C CA . PRO C 86 ? 0.5348 0.6023 0.4877 0.0995 -0.1221 0.0435 85 PRO C CA 4316 C C . PRO C 86 ? 0.5388 0.6208 0.4862 0.0956 -0.1367 0.0449 85 PRO C C 4317 O O . PRO C 86 ? 0.5465 0.6314 0.4712 0.0797 -0.1282 0.0447 85 PRO C O 4318 C CB . PRO C 86 ? 0.4926 0.5850 0.4666 0.0947 -0.0988 0.0306 85 PRO C CB 4319 C CG . PRO C 86 ? 0.4935 0.5641 0.4464 0.0860 -0.0837 0.0331 85 PRO C CG 4320 C CD . PRO C 86 ? 0.5319 0.5718 0.4444 0.0766 -0.0909 0.0453 85 PRO C CD 4321 N N . ALA C 87 ? 0.5306 0.6231 0.5023 0.1102 -0.1584 0.0445 86 ALA C N 4322 C CA . ALA C 87 ? 0.5372 0.6453 0.5073 0.1078 -0.1761 0.0448 86 ALA C CA 4323 C C . ALA C 87 ? 0.4892 0.6354 0.4800 0.0990 -0.1610 0.0308 86 ALA C C 4324 O O . ALA C 87 ? 0.5067 0.6613 0.4828 0.0893 -0.1684 0.0310 86 ALA C O 4325 C CB . ALA C 87 ? 0.5647 0.6790 0.5662 0.1278 -0.2042 0.0450 86 ALA C CB 4326 N N . ASN C 88 ? 0.4320 0.5988 0.4543 0.1014 -0.1405 0.0186 87 ASN C N 4327 C CA . ASN C 88 ? 0.3919 0.5905 0.4335 0.0931 -0.1259 0.0059 87 ASN C CA 4328 C C . ASN C 88 ? 0.3737 0.5644 0.3963 0.0796 -0.1015 0.0055 87 ASN C C 4329 O O . ASN C 88 ? 0.3383 0.5306 0.3741 0.0819 -0.0862 0.0005 87 ASN C O 4330 C CB . ASN C 88 ? 0.3662 0.5943 0.4582 0.1042 -0.1217 -0.0086 87 ASN C CB 4331 C CG . ASN C 88 ? 0.3794 0.6216 0.5012 0.1185 -0.1470 -0.0117 87 ASN C CG 4332 O OD1 . ASN C 88 ? 0.3804 0.6322 0.5401 0.1328 -0.1494 -0.0200 87 ASN C OD1 4333 N ND2 . ASN C 88 ? 0.3905 0.6345 0.4972 0.1145 -0.1665 -0.0065 87 ASN C ND2 4334 N N . ASP C 89 ? 0.3871 0.5682 0.3783 0.0652 -0.0992 0.0101 88 ASP C N 4335 C CA . ASP C 89 ? 0.3693 0.5426 0.3453 0.0527 -0.0791 0.0090 88 ASP C CA 4336 C C . ASP C 89 ? 0.3550 0.5500 0.3385 0.0418 -0.0707 0.0001 88 ASP C C 4337 O O . ASP C 89 ? 0.3450 0.5623 0.3571 0.0451 -0.0649 -0.0085 88 ASP C O 4338 C CB . ASP C 89 ? 0.3995 0.5415 0.3358 0.0440 -0.0806 0.0190 88 ASP C CB 4339 C CG . ASP C 89 ? 0.3839 0.5195 0.3101 0.0310 -0.0603 0.0154 88 ASP C CG 4340 O OD1 . ASP C 89 ? 0.3624 0.5010 0.3055 0.0349 -0.0488 0.0116 88 ASP C OD1 4341 O OD2 . ASP C 89 ? 0.4083 0.5366 0.3110 0.0166 -0.0565 0.0152 88 ASP C OD2 4342 N N . LEU C 90 ? 0.3667 0.5546 0.3251 0.0277 -0.0685 0.0011 89 LEU C N 4343 C CA . LEU C 90 ? 0.3553 0.5623 0.3218 0.0171 -0.0605 -0.0081 89 LEU C CA 4344 C C . LEU C 90 ? 0.3731 0.5905 0.3344 0.0158 -0.0787 -0.0084 89 LEU C C 4345 O O . LEU C 90 ? 0.4135 0.6139 0.3416 0.0083 -0.0883 -0.0019 89 LEU C O 4346 C CB . LEU C 90 ? 0.3589 0.5538 0.3056 0.0016 -0.0455 -0.0103 89 LEU C CB 4347 C CG . LEU C 90 ? 0.3439 0.5267 0.2948 0.0022 -0.0309 -0.0100 89 LEU C CG 4348 C CD1 . LEU C 90 ? 0.3596 0.5306 0.2941 -0.0129 -0.0182 -0.0140 89 LEU C CD1 4349 C CD2 . LEU C 90 ? 0.3188 0.5164 0.2988 0.0075 -0.0219 -0.0158 89 LEU C CD2 4350 N N . CYS C 91 ? 0.3514 0.5957 0.3443 0.0221 -0.0837 -0.0163 90 CYS C N 4351 C CA . CYS C 91 ? 0.3646 0.6232 0.3602 0.0231 -0.1046 -0.0181 90 CYS C CA 4352 C C . CYS C 91 ? 0.3574 0.6168 0.3288 0.0048 -0.1021 -0.0220 90 CYS C C 4353 O O . CYS C 91 ? 0.3823 0.6317 0.3248 -0.0004 -0.1195 -0.0165 90 CYS C O 4354 C CB . CYS C 91 ? 0.3541 0.6453 0.3967 0.0330 -0.1076 -0.0296 90 CYS C CB 4355 S SG . CYS C 91 ? 0.3349 0.6481 0.4060 0.0245 -0.0802 -0.0442 90 CYS C SG 4356 N N . TYR C 92 ? 0.3237 0.5929 0.3054 -0.0053 -0.0810 -0.0316 91 TYR C N 4357 C CA . TYR C 92 ? 0.3297 0.5951 0.2885 -0.0238 -0.0728 -0.0368 91 TYR C CA 4358 C C . TYR C 92 ? 0.3381 0.5749 0.2683 -0.0306 -0.0607 -0.0305 91 TYR C C 4359 O O . TYR C 92 ? 0.3127 0.5434 0.2559 -0.0253 -0.0473 -0.0295 91 TYR C O 4360 C CB . TYR C 92 ? 0.2975 0.5824 0.2822 -0.0314 -0.0552 -0.0502 91 TYR C CB 4361 C CG . TYR C 92 ? 0.3089 0.5955 0.2761 -0.0500 -0.0502 -0.0588 91 TYR C CG 4362 C CD1 . TYR C 92 ? 0.3146 0.5820 0.2593 -0.0627 -0.0350 -0.0601 91 TYR C CD1 4363 C CD2 . TYR C 92 ? 0.3163 0.6246 0.2909 -0.0558 -0.0604 -0.0675 91 TYR C CD2 4364 C CE1 . TYR C 92 ? 0.3272 0.5960 0.2567 -0.0811 -0.0280 -0.0704 91 TYR C CE1 4365 C CE2 . TYR C 92 ? 0.3285 0.6379 0.2854 -0.0743 -0.0549 -0.0769 91 TYR C CE2 4366 C CZ . TYR C 92 ? 0.3352 0.6240 0.2688 -0.0871 -0.0380 -0.0784 91 TYR C CZ 4367 O OH . TYR C 92 ? 0.3518 0.6414 0.2690 -0.1066 -0.0301 -0.0900 91 TYR C OH 4368 N N . PRO C 93 ? 0.3751 0.5940 0.2655 -0.0435 -0.0654 -0.0271 92 PRO C N 4369 C CA . PRO C 93 ? 0.3962 0.5870 0.2596 -0.0499 -0.0550 -0.0215 92 PRO C CA 4370 C C . PRO C 93 ? 0.3823 0.5731 0.2575 -0.0600 -0.0289 -0.0322 92 PRO C C 4371 O O . PRO C 93 ? 0.3701 0.5769 0.2615 -0.0675 -0.0192 -0.0438 92 PRO C O 4372 C CB . PRO C 93 ? 0.4428 0.6148 0.2574 -0.0645 -0.0663 -0.0168 92 PRO C CB 4373 C CG . PRO C 93 ? 0.4436 0.6370 0.2620 -0.0727 -0.0723 -0.0264 92 PRO C CG 4374 C CD . PRO C 93 ? 0.4059 0.6287 0.2723 -0.0557 -0.0786 -0.0300 92 PRO C CD 4375 N N . GLY C 94 ? 0.3912 0.5643 0.2619 -0.0594 -0.0184 -0.0290 93 GLY C N 4376 C CA . GLY C 94 ? 0.3923 0.5646 0.2781 -0.0675 0.0035 -0.0396 93 GLY C CA 4377 C C . GLY C 94 ? 0.3960 0.5551 0.2895 -0.0600 0.0096 -0.0352 93 GLY C C 4378 O O . GLY C 94 ? 0.4223 0.5630 0.2922 -0.0590 0.0037 -0.0261 93 GLY C O 4379 N N . ASN C 95 ? 0.3855 0.5522 0.3110 -0.0551 0.0202 -0.0412 94 ASN C N 4380 C CA . ASN C 95 ? 0.4065 0.5625 0.3411 -0.0479 0.0240 -0.0380 94 ASN C CA 4381 C C . ASN C 95 ? 0.3643 0.5297 0.3319 -0.0363 0.0256 -0.0392 94 ASN C C 4382 O O . ASN C 95 ? 0.3437 0.5211 0.3292 -0.0367 0.0286 -0.0447 94 ASN C O 4383 C CB . ASN C 95 ? 0.4466 0.5902 0.3744 -0.0622 0.0392 -0.0468 94 ASN C CB 4384 C CG . ASN C 95 ? 0.4779 0.6312 0.4241 -0.0734 0.0535 -0.0624 94 ASN C CG 4385 O OD1 . ASN C 95 ? 0.4998 0.6669 0.4611 -0.0711 0.0517 -0.0655 94 ASN C OD1 4386 N ND2 . ASN C 95 ? 0.5193 0.6650 0.4664 -0.0866 0.0690 -0.0739 94 ASN C ND2 4387 N N . PHE C 96 ? 0.3500 0.5069 0.3218 -0.0272 0.0233 -0.0336 95 PHE C N 4388 C CA . PHE C 96 ? 0.3335 0.4936 0.3286 -0.0173 0.0230 -0.0330 95 PHE C CA 4389 C C . PHE C 96 ? 0.3205 0.4727 0.3285 -0.0210 0.0310 -0.0396 95 PHE C C 4390 O O . PHE C 96 ? 0.3079 0.4497 0.3068 -0.0225 0.0323 -0.0386 95 PHE C O 4391 C CB . PHE C 96 ? 0.3508 0.5080 0.3405 -0.0049 0.0134 -0.0233 95 PHE C CB 4392 C CG . PHE C 96 ? 0.3561 0.5199 0.3613 0.0034 0.0115 -0.0219 95 PHE C CG 4393 C CD1 . PHE C 96 ? 0.3646 0.5258 0.3848 0.0031 0.0153 -0.0252 95 PHE C CD1 4394 C CD2 . PHE C 96 ? 0.3631 0.5341 0.3675 0.0109 0.0055 -0.0179 95 PHE C CD2 4395 C CE1 . PHE C 96 ? 0.3655 0.5275 0.3916 0.0084 0.0134 -0.0225 95 PHE C CE1 4396 C CE2 . PHE C 96 ? 0.3538 0.5288 0.3681 0.0154 0.0067 -0.0179 95 PHE C CE2 4397 C CZ . PHE C 96 ? 0.3515 0.5201 0.3726 0.0133 0.0107 -0.0193 95 PHE C CZ 4398 N N . ASN C 97 ? 0.3058 0.4630 0.3375 -0.0226 0.0359 -0.0474 96 ASN C N 4399 C CA . ASN C 97 ? 0.2975 0.4507 0.3512 -0.0246 0.0415 -0.0561 96 ASN C CA 4400 C C . ASN C 97 ? 0.2808 0.4274 0.3417 -0.0142 0.0336 -0.0506 96 ASN C C 4401 O O . ASN C 97 ? 0.2529 0.3986 0.3139 -0.0048 0.0248 -0.0427 96 ASN C O 4402 C CB . ASN C 97 ? 0.3056 0.4640 0.3859 -0.0259 0.0451 -0.0645 96 ASN C CB 4403 C CG . ASN C 97 ? 0.3234 0.4809 0.4324 -0.0301 0.0523 -0.0781 96 ASN C CG 4404 O OD1 . ASN C 97 ? 0.3360 0.4906 0.4697 -0.0218 0.0453 -0.0788 96 ASN C OD1 4405 N ND2 . ASN C 97 ? 0.3467 0.5065 0.4533 -0.0439 0.0661 -0.0902 96 ASN C ND2 4406 N N . ASP C 98 ? 0.2781 0.4197 0.3442 -0.0179 0.0378 -0.0564 97 ASP C N 4407 C CA . ASP C 98 ? 0.2687 0.4046 0.3409 -0.0101 0.0305 -0.0532 97 ASP C CA 4408 C C . ASP C 98 ? 0.2604 0.3911 0.3089 -0.0017 0.0221 -0.0400 97 ASP C C 4409 O O . ASP C 98 ? 0.2640 0.3917 0.3156 0.0063 0.0138 -0.0355 97 ASP C O 4410 C CB . ASP C 98 ? 0.2649 0.4026 0.3670 -0.0036 0.0233 -0.0570 97 ASP C CB 4411 C CG . ASP C 98 ? 0.2710 0.4139 0.4059 -0.0102 0.0310 -0.0732 97 ASP C CG 4412 O OD1 . ASP C 98 ? 0.2708 0.4138 0.4108 -0.0172 0.0391 -0.0820 97 ASP C OD1 4413 O OD2 . ASP C 98 ? 0.2831 0.4294 0.4403 -0.0091 0.0302 -0.0783 97 ASP C OD2 4414 N N . TYR C 99 ? 0.2632 0.3924 0.2883 -0.0044 0.0238 -0.0349 98 TYR C N 4415 C CA . TYR C 99 ? 0.2674 0.3928 0.2749 0.0039 0.0163 -0.0245 98 TYR C CA 4416 C C . TYR C 99 ? 0.2578 0.3730 0.2629 0.0086 0.0135 -0.0224 98 TYR C C 4417 O O . TYR C 99 ? 0.2473 0.3613 0.2486 0.0171 0.0075 -0.0171 98 TYR C O 4418 C CB . TYR C 99 ? 0.2762 0.3989 0.2613 -0.0002 0.0164 -0.0204 98 TYR C CB 4419 C CG . TYR C 99 ? 0.2879 0.4086 0.2609 0.0094 0.0073 -0.0114 98 TYR C CG 4420 C CD1 . TYR C 99 ? 0.2883 0.4203 0.2708 0.0177 0.0028 -0.0095 98 TYR C CD1 4421 C CD2 . TYR C 99 ? 0.3131 0.4194 0.2658 0.0092 0.0038 -0.0055 98 TYR C CD2 4422 C CE1 . TYR C 99 ? 0.2922 0.4251 0.2706 0.0266 -0.0041 -0.0046 98 TYR C CE1 4423 C CE2 . TYR C 99 ? 0.3296 0.4340 0.2769 0.0196 -0.0058 0.0014 98 TYR C CE2 4424 C CZ . TYR C 99 ? 0.3154 0.4353 0.2787 0.0287 -0.0095 0.0007 98 TYR C CZ 4425 O OH . TYR C 99 ? 0.3226 0.4428 0.2872 0.0391 -0.0180 0.0046 98 TYR C OH 4426 N N . GLU C 100 ? 0.2627 0.3708 0.2701 0.0017 0.0192 -0.0282 99 GLU C N 4427 C CA . GLU C 100 ? 0.2793 0.3767 0.2831 0.0043 0.0175 -0.0273 99 GLU C CA 4428 C C . GLU C 100 ? 0.2636 0.3651 0.2866 0.0102 0.0112 -0.0304 99 GLU C C 4429 O O . GLU C 100 ? 0.2625 0.3577 0.2802 0.0155 0.0064 -0.0278 99 GLU C O 4430 C CB . GLU C 100 ? 0.3041 0.3915 0.3035 -0.0072 0.0274 -0.0337 99 GLU C CB 4431 C CG . GLU C 100 ? 0.3380 0.4130 0.3075 -0.0147 0.0316 -0.0280 99 GLU C CG 4432 C CD . GLU C 100 ? 0.3607 0.4436 0.3272 -0.0233 0.0368 -0.0314 99 GLU C CD 4433 O OE1 . GLU C 100 ? 0.3591 0.4529 0.3489 -0.0292 0.0442 -0.0431 99 GLU C OE1 4434 O OE2 . GLU C 100 ? 0.3880 0.4662 0.3305 -0.0241 0.0326 -0.0234 99 GLU C OE2 4435 N N . GLU C 101 ? 0.2422 0.3526 0.2861 0.0092 0.0102 -0.0361 100 GLU C N 4436 C CA . GLU C 101 ? 0.2381 0.3495 0.2976 0.0149 0.0003 -0.0373 100 GLU C CA 4437 C C . GLU C 101 ? 0.2432 0.3522 0.2866 0.0220 -0.0067 -0.0275 100 GLU C C 4438 O O . GLU C 101 ? 0.2455 0.3484 0.2831 0.0260 -0.0143 -0.0251 100 GLU C O 4439 C CB . GLU C 101 ? 0.2293 0.3479 0.3173 0.0128 -0.0005 -0.0455 100 GLU C CB 4440 C CG . GLU C 101 ? 0.2241 0.3469 0.3381 0.0061 0.0055 -0.0595 100 GLU C CG 4441 C CD . GLU C 101 ? 0.2235 0.3437 0.3488 0.0091 -0.0030 -0.0633 100 GLU C CD 4442 O OE1 . GLU C 101 ? 0.2170 0.3353 0.3496 0.0168 -0.0185 -0.0599 100 GLU C OE1 4443 O OE2 . GLU C 101 ? 0.2226 0.3409 0.3468 0.0025 0.0054 -0.0696 100 GLU C OE2 4444 N N . LEU C 102 ? 0.2398 0.3537 0.2748 0.0220 -0.0032 -0.0233 101 LEU C N 4445 C CA . LEU C 102 ? 0.2373 0.3505 0.2589 0.0265 -0.0063 -0.0166 101 LEU C CA 4446 C C . LEU C 102 ? 0.2382 0.3467 0.2446 0.0305 -0.0062 -0.0136 101 LEU C C 4447 O O . LEU C 102 ? 0.2319 0.3365 0.2290 0.0331 -0.0088 -0.0114 101 LEU C O 4448 C CB . LEU C 102 ? 0.2425 0.3647 0.2624 0.0247 -0.0016 -0.0152 101 LEU C CB 4449 C CG . LEU C 102 ? 0.2519 0.3759 0.2614 0.0275 -0.0017 -0.0110 101 LEU C CG 4450 C CD1 . LEU C 102 ? 0.2676 0.3816 0.2735 0.0273 -0.0069 -0.0088 101 LEU C CD1 4451 C CD2 . LEU C 102 ? 0.2485 0.3838 0.2610 0.0247 0.0027 -0.0118 101 LEU C CD2 4452 N N . LYS C 103 ? 0.2526 0.3591 0.2550 0.0299 -0.0026 -0.0141 102 LYS C N 4453 C CA . LYS C 103 ? 0.2642 0.3636 0.2555 0.0345 -0.0029 -0.0119 102 LYS C CA 4454 C C . LYS C 103 ? 0.2677 0.3588 0.2593 0.0346 -0.0060 -0.0149 102 LYS C C 4455 O O . LYS C 103 ? 0.2803 0.3664 0.2633 0.0382 -0.0067 -0.0146 102 LYS C O 4456 C CB . LYS C 103 ? 0.2847 0.3783 0.2686 0.0334 -0.0004 -0.0100 102 LYS C CB 4457 C CG . LYS C 103 ? 0.2930 0.3946 0.2735 0.0345 -0.0010 -0.0064 102 LYS C CG 4458 C CD . LYS C 103 ? 0.3165 0.4077 0.2834 0.0323 -0.0017 -0.0025 102 LYS C CD 4459 C CE . LYS C 103 ? 0.3360 0.4183 0.2973 0.0415 -0.0068 0.0017 102 LYS C CE 4460 N NZ . LYS C 103 ? 0.3647 0.4319 0.3089 0.0400 -0.0109 0.0081 102 LYS C NZ 4461 N N . HIS C 104 ? 0.2641 0.3546 0.2676 0.0302 -0.0077 -0.0196 103 HIS C N 4462 C CA . HIS C 104 ? 0.2682 0.3529 0.2749 0.0300 -0.0134 -0.0236 103 HIS C CA 4463 C C . HIS C 104 ? 0.2727 0.3550 0.2709 0.0325 -0.0215 -0.0208 103 HIS C C 4464 O O . HIS C 104 ? 0.2699 0.3449 0.2559 0.0332 -0.0237 -0.0216 103 HIS C O 4465 C CB . HIS C 104 ? 0.2649 0.3531 0.2935 0.0251 -0.0148 -0.0315 103 HIS C CB 4466 C CG . HIS C 104 ? 0.2752 0.3601 0.3112 0.0252 -0.0239 -0.0366 103 HIS C CG 4467 N ND1 . HIS C 104 ? 0.2882 0.3680 0.3251 0.0220 -0.0209 -0.0425 103 HIS C ND1 4468 C CD2 . HIS C 104 ? 0.2795 0.3635 0.3196 0.0277 -0.0374 -0.0364 103 HIS C CD2 4469 C CE1 . HIS C 104 ? 0.2938 0.3730 0.3379 0.0225 -0.0322 -0.0471 103 HIS C CE1 4470 N NE2 . HIS C 104 ? 0.2938 0.3746 0.3384 0.0261 -0.0436 -0.0427 103 HIS C NE2 4471 N N . LEU C 105 ? 0.2806 0.3665 0.2831 0.0323 -0.0253 -0.0180 104 LEU C N 4472 C CA . LEU C 105 ? 0.3117 0.3904 0.2993 0.0324 -0.0322 -0.0135 104 LEU C CA 4473 C C . LEU C 105 ? 0.3336 0.4096 0.2999 0.0326 -0.0251 -0.0117 104 LEU C C 4474 O O . LEU C 105 ? 0.3547 0.4209 0.3027 0.0305 -0.0282 -0.0115 104 LEU C O 4475 C CB . LEU C 105 ? 0.3132 0.3942 0.3056 0.0314 -0.0330 -0.0097 104 LEU C CB 4476 C CG . LEU C 105 ? 0.3177 0.4010 0.3347 0.0315 -0.0397 -0.0125 104 LEU C CG 4477 C CD1 . LEU C 105 ? 0.3266 0.4073 0.3430 0.0304 -0.0405 -0.0079 104 LEU C CD1 4478 C CD2 . LEU C 105 ? 0.3359 0.4113 0.3601 0.0329 -0.0548 -0.0147 104 LEU C CD2 4479 N N . LEU C 106 ? 0.4565 0.4076 0.3976 -0.0446 -0.0811 0.0382 105 LEU C N 4480 C CA . LEU C 106 ? 0.4968 0.4257 0.4172 -0.0362 -0.0741 0.0302 105 LEU C CA 4481 C C . LEU C 106 ? 0.5243 0.4144 0.4239 -0.0379 -0.0885 0.0322 105 LEU C C 4482 O O . LEU C 106 ? 0.5491 0.4111 0.4232 -0.0290 -0.0851 0.0235 105 LEU C O 4483 C CB . LEU C 106 ? 0.4841 0.4436 0.4225 -0.0308 -0.0616 0.0304 105 LEU C CB 4484 C CG . LEU C 106 ? 0.5134 0.4648 0.4391 -0.0197 -0.0504 0.0214 105 LEU C CG 4485 C CD1 . LEU C 106 ? 0.5240 0.4703 0.4366 -0.0153 -0.0387 0.0108 105 LEU C CD1 4486 C CD2 . LEU C 106 ? 0.4902 0.4751 0.4372 -0.0159 -0.0420 0.0235 105 LEU C CD2 4487 N N . SER C 107 ? 0.5201 0.4083 0.4298 -0.0492 -0.1047 0.0436 106 SER C N 4488 C CA . SER C 107 ? 0.5565 0.4023 0.4446 -0.0533 -0.1220 0.0459 106 SER C CA 4489 C C . SER C 107 ? 0.5856 0.3949 0.4470 -0.0551 -0.1338 0.0402 106 SER C C 4490 O O . SER C 107 ? 0.6133 0.3802 0.4494 -0.0568 -0.1488 0.0390 106 SER C O 4491 C CB . SER C 107 ? 0.5558 0.4123 0.4649 -0.0680 -0.1363 0.0618 106 SER C CB 4492 O OG . SER C 107 ? 0.5464 0.4167 0.4709 -0.0801 -0.1468 0.0689 106 SER C OG 4493 N N . ARG C 108 ? 0.5638 0.3872 0.4290 -0.0547 -0.1284 0.0369 107 ARG C N 4494 C CA . ARG C 108 ? 0.5958 0.3855 0.4325 -0.0542 -0.1373 0.0306 107 ARG C CA 4495 C C . ARG C 108 ? 0.5813 0.3588 0.3924 -0.0409 -0.1197 0.0176 107 ARG C C 4496 O O . ARG C 108 ? 0.5919 0.3445 0.3776 -0.0393 -0.1233 0.0123 107 ARG C O 4497 C CB . ARG C 108 ? 0.6113 0.4207 0.4670 -0.0634 -0.1470 0.0373 107 ARG C CB 4498 C CG . ARG C 108 ? 0.6622 0.4649 0.5278 -0.0781 -0.1713 0.0482 107 ARG C CG 4499 C CD . ARG C 108 ? 0.6599 0.5119 0.5702 -0.0878 -0.1718 0.0619 107 ARG C CD 4500 N NE . ARG C 108 ? 0.6999 0.5563 0.6255 -0.1026 -0.1938 0.0725 107 ARG C NE 4501 C CZ . ARG C 108 ? 0.7445 0.5897 0.6757 -0.1172 -0.2116 0.0828 107 ARG C CZ 4502 N NH1 . ARG C 108 ? 0.7697 0.5939 0.6895 -0.1182 -0.2113 0.0841 107 ARG C NH1 4503 N NH2 . ARG C 108 ? 0.7611 0.6161 0.7099 -0.1314 -0.2313 0.0926 107 ARG C NH2 4504 N N . ILE C 109 ? 0.5485 0.3435 0.3659 -0.0319 -0.1012 0.0132 108 ILE C N 4505 C CA . ILE C 109 ? 0.5381 0.3296 0.3374 -0.0213 -0.0827 0.0026 108 ILE C CA 4506 C C . ILE C 109 ? 0.5498 0.3226 0.3290 -0.0094 -0.0756 -0.0047 108 ILE C C 4507 O O . ILE C 109 ? 0.5462 0.3286 0.3390 -0.0069 -0.0761 -0.0019 108 ILE C O 4508 C CB . ILE C 109 ? 0.4914 0.3258 0.3181 -0.0209 -0.0655 0.0027 108 ILE C CB 4509 C CG1 . ILE C 109 ? 0.4770 0.3236 0.3156 -0.0286 -0.0713 0.0071 108 ILE C CG1 4510 C CG2 . ILE C 109 ? 0.4957 0.3292 0.3070 -0.0122 -0.0461 -0.0067 108 ILE C CG2 4511 C CD1 . ILE C 109 ? 0.4354 0.3227 0.3029 -0.0290 -0.0593 0.0084 108 ILE C CD1 4512 N N . ASN C 110 ? 0.5815 0.3277 0.3272 -0.0009 -0.0688 -0.0138 109 ASN C N 4513 C CA . ASN C 110 ? 0.6139 0.3424 0.3374 0.0137 -0.0605 -0.0224 109 ASN C CA 4514 C C . ASN C 110 ? 0.6008 0.3565 0.3292 0.0229 -0.0349 -0.0289 109 ASN C C 4515 O O . ASN C 110 ? 0.6008 0.3577 0.3239 0.0363 -0.0256 -0.0347 109 ASN C O 4516 C CB . ASN C 110 ? 0.6648 0.3411 0.3422 0.0190 -0.0714 -0.0288 109 ASN C CB 4517 C CG . ASN C 110 ? 0.6896 0.3339 0.3594 0.0123 -0.0975 -0.0240 109 ASN C CG 4518 O OD1 . ASN C 110 ? 0.7159 0.3365 0.3718 0.0030 -0.1145 -0.0216 109 ASN C OD1 4519 N ND2 . ASN C 110 ? 0.6954 0.3380 0.3738 0.0163 -0.1020 -0.0222 109 ASN C ND2 4520 N N . HIS C 111 ? 0.5795 0.3565 0.3182 0.0160 -0.0247 -0.0276 110 HIS C N 4521 C CA . HIS C 111 ? 0.5876 0.3889 0.3305 0.0210 -0.0018 -0.0326 110 HIS C CA 4522 C C . HIS C 111 ? 0.5604 0.3886 0.3241 0.0098 0.0051 -0.0288 110 HIS C C 4523 O O . HIS C 111 ? 0.5449 0.3577 0.2984 0.0021 -0.0030 -0.0258 110 HIS C O 4524 C CB . HIS C 111 ? 0.6468 0.4181 0.3485 0.0299 0.0063 -0.0401 110 HIS C CB 4525 C CG . HIS C 111 ? 0.6631 0.4597 0.3676 0.0366 0.0309 -0.0450 110 HIS C CG 4526 N ND1 . HIS C 111 ? 0.6492 0.4805 0.3810 0.0437 0.0418 -0.0468 110 HIS C ND1 4527 C CD2 . HIS C 111 ? 0.6867 0.4791 0.3693 0.0372 0.0465 -0.0478 110 HIS C CD2 4528 C CE1 . HIS C 111 ? 0.6545 0.5054 0.3846 0.0476 0.0630 -0.0506 110 HIS C CE1 4529 N NE2 . HIS C 111 ? 0.6745 0.5025 0.3748 0.0431 0.0669 -0.0508 110 HIS C NE2 4530 N N . PHE C 112 ? 0.5428 0.4096 0.3349 0.0098 0.0187 -0.0292 111 PHE C N 4531 C CA . PHE C 112 ? 0.5283 0.4179 0.3353 0.0009 0.0286 -0.0280 111 PHE C CA 4532 C C . PHE C 112 ? 0.5524 0.4498 0.3495 0.0035 0.0488 -0.0328 111 PHE C C 4533 O O . PHE C 112 ? 0.5607 0.4599 0.3503 0.0142 0.0576 -0.0375 111 PHE C O 4534 C CB . PHE C 112 ? 0.4945 0.4230 0.3396 -0.0021 0.0299 -0.0255 111 PHE C CB 4535 C CG . PHE C 112 ? 0.4860 0.4175 0.3467 -0.0060 0.0136 -0.0193 111 PHE C CG 4536 C CD1 . PHE C 112 ? 0.4859 0.4088 0.3452 -0.0135 0.0039 -0.0153 111 PHE C CD1 4537 C CD2 . PHE C 112 ? 0.4780 0.4241 0.3562 -0.0019 0.0086 -0.0166 111 PHE C CD2 4538 C CE1 . PHE C 112 ? 0.4702 0.4025 0.3472 -0.0168 -0.0092 -0.0088 111 PHE C CE1 4539 C CE2 . PHE C 112 ? 0.4675 0.4203 0.3611 -0.0068 -0.0044 -0.0093 111 PHE C CE2 4540 C CZ . PHE C 112 ? 0.4643 0.4120 0.3583 -0.0144 -0.0129 -0.0053 111 PHE C CZ 4541 N N . GLU C 113 ? 0.5598 0.4622 0.3570 -0.0063 0.0560 -0.0313 112 GLU C N 4542 C CA . GLU C 113 ? 0.5653 0.4868 0.3649 -0.0090 0.0757 -0.0335 112 GLU C CA 4543 C C . GLU C 113 ? 0.5363 0.4869 0.3664 -0.0197 0.0777 -0.0314 112 GLU C C 4544 O O . GLU C 113 ? 0.5333 0.4721 0.3594 -0.0289 0.0718 -0.0285 112 GLU C O 4545 C CB . GLU C 113 ? 0.6172 0.5101 0.3809 -0.0126 0.0828 -0.0328 112 GLU C CB 4546 C CG . GLU C 113 ? 0.6442 0.5582 0.4091 -0.0164 0.1051 -0.0335 112 GLU C CG 4547 C CD . GLU C 113 ? 0.7027 0.5882 0.4300 -0.0218 0.1130 -0.0310 112 GLU C CD 4548 O OE1 . GLU C 113 ? 0.7575 0.6072 0.4496 -0.0146 0.1064 -0.0321 112 GLU C OE1 4549 O OE2 . GLU C 113 ? 0.7215 0.6189 0.4530 -0.0341 0.1251 -0.0274 112 GLU C OE2 4550 N N . LYS C 114 ? 0.5038 0.4906 0.3629 -0.0176 0.0846 -0.0335 113 LYS C N 4551 C CA . LYS C 114 ? 0.4785 0.4917 0.3645 -0.0272 0.0853 -0.0328 113 LYS C CA 4552 C C . LYS C 114 ? 0.4893 0.5022 0.3680 -0.0394 0.0975 -0.0320 113 LYS C C 4553 O O . LYS C 114 ? 0.5240 0.5407 0.3928 -0.0389 0.1121 -0.0327 113 LYS C O 4554 C CB . LYS C 114 ? 0.4553 0.5066 0.3721 -0.0217 0.0884 -0.0353 113 LYS C CB 4555 C CG . LYS C 114 ? 0.4309 0.5029 0.3728 -0.0280 0.0811 -0.0348 113 LYS C CG 4556 C CD . LYS C 114 ? 0.4181 0.5238 0.3866 -0.0208 0.0810 -0.0367 113 LYS C CD 4557 C CE . LYS C 114 ? 0.4215 0.5570 0.4050 -0.0226 0.0952 -0.0399 113 LYS C CE 4558 N NZ . LYS C 114 ? 0.4083 0.5774 0.4188 -0.0153 0.0925 -0.0416 113 LYS C NZ 4559 N N . ILE C 115 ? 0.4748 0.4813 0.3563 -0.0500 0.0915 -0.0302 114 ILE C N 4560 C CA . ILE C 115 ? 0.4923 0.4953 0.3673 -0.0639 0.1006 -0.0285 114 ILE C CA 4561 C C . ILE C 115 ? 0.4748 0.4975 0.3747 -0.0729 0.0964 -0.0299 114 ILE C C 4562 O O . ILE C 115 ? 0.4726 0.4996 0.3851 -0.0683 0.0841 -0.0316 114 ILE C O 4563 C CB . ILE C 115 ? 0.5231 0.4832 0.3638 -0.0685 0.0956 -0.0246 114 ILE C CB 4564 C CG1 . ILE C 115 ? 0.5157 0.4593 0.3567 -0.0659 0.0773 -0.0242 114 ILE C CG1 4565 C CG2 . ILE C 115 ? 0.5488 0.4864 0.3600 -0.0601 0.0993 -0.0238 114 ILE C CG2 4566 C CD1 . ILE C 115 ? 0.5475 0.4528 0.3597 -0.0718 0.0714 -0.0205 114 ILE C CD1 4567 N N . GLN C 116 ? 0.4846 0.5199 0.3913 -0.0860 0.1068 -0.0293 115 GLN C N 4568 C CA . GLN C 116 ? 0.4759 0.5190 0.3980 -0.0971 0.1011 -0.0309 115 GLN C CA 4569 C C . GLN C 116 ? 0.4904 0.4930 0.3883 -0.1017 0.0907 -0.0289 115 GLN C C 4570 O O . GLN C 116 ? 0.5093 0.4820 0.3792 -0.1048 0.0939 -0.0244 115 GLN C O 4571 C CB . GLN C 116 ? 0.4839 0.5479 0.4177 -0.1125 0.1140 -0.0295 115 GLN C CB 4572 C CG . GLN C 116 ? 0.4880 0.5600 0.4382 -0.1252 0.1068 -0.0321 115 GLN C CG 4573 C CD . GLN C 116 ? 0.4893 0.5899 0.4576 -0.1413 0.1189 -0.0303 115 GLN C CD 4574 O OE1 . GLN C 116 ? 0.4763 0.6172 0.4746 -0.1394 0.1209 -0.0336 115 GLN C OE1 4575 N NE2 . GLN C 116 ? 0.5182 0.5994 0.4687 -0.1574 0.1270 -0.0240 115 GLN C NE2 4576 N N . ILE C 117 ? 0.4860 0.4868 0.3926 -0.1000 0.0780 -0.0323 116 ILE C N 4577 C CA . ILE C 117 ? 0.5066 0.4701 0.3915 -0.1032 0.0680 -0.0312 116 ILE C CA 4578 C C . ILE C 117 ? 0.5109 0.4735 0.4034 -0.1133 0.0626 -0.0349 116 ILE C C 4579 O O . ILE C 117 ? 0.5437 0.4731 0.4154 -0.1215 0.0585 -0.0331 116 ILE C O 4580 C CB . ILE C 117 ? 0.4947 0.4438 0.3721 -0.0882 0.0551 -0.0313 116 ILE C CB 4581 C CG1 . ILE C 117 ? 0.4615 0.4394 0.3646 -0.0782 0.0480 -0.0358 116 ILE C CG1 4582 C CG2 . ILE C 117 ? 0.5001 0.4394 0.3629 -0.0813 0.0580 -0.0274 116 ILE C CG2 4583 C CD1 . ILE C 117 ? 0.4559 0.4224 0.3544 -0.0660 0.0352 -0.0352 116 ILE C CD1 4584 N N . ILE C 118 ? 0.4908 0.4864 0.4100 -0.1125 0.0615 -0.0402 117 ILE C N 4585 C CA . ILE C 118 ? 0.5017 0.4969 0.4275 -0.1235 0.0561 -0.0447 117 ILE C CA 4586 C C . ILE C 118 ? 0.4965 0.5315 0.4496 -0.1330 0.0643 -0.0462 117 ILE C C 4587 O O . ILE C 118 ? 0.4683 0.5362 0.4435 -0.1236 0.0629 -0.0500 117 ILE C O 4588 C CB . ILE C 118 ? 0.4899 0.4834 0.4191 -0.1115 0.0421 -0.0516 117 ILE C CB 4589 C CG1 . ILE C 118 ? 0.5017 0.4615 0.4080 -0.1004 0.0336 -0.0499 117 ILE C CG1 4590 C CG2 . ILE C 118 ? 0.5064 0.4952 0.4383 -0.1226 0.0353 -0.0577 117 ILE C CG2 4591 C CD1 . ILE C 118 ? 0.4838 0.4494 0.3958 -0.0849 0.0224 -0.0558 117 ILE C CD1 4592 N N . PRO C 119 ? 0.5278 0.5612 0.4797 -0.1520 0.0726 -0.0424 118 PRO C N 4593 C CA . PRO C 119 ? 0.5160 0.5907 0.4970 -0.1623 0.0796 -0.0434 118 PRO C CA 4594 C C . PRO C 119 ? 0.5048 0.5929 0.5027 -0.1644 0.0668 -0.0516 118 PRO C C 4595 O O . PRO C 119 ? 0.5087 0.5662 0.4913 -0.1678 0.0547 -0.0554 118 PRO C O 4596 C CB . PRO C 119 ? 0.5548 0.6185 0.5274 -0.1851 0.0894 -0.0363 118 PRO C CB 4597 C CG . PRO C 119 ? 0.5754 0.5989 0.5139 -0.1815 0.0928 -0.0302 118 PRO C CG 4598 C CD . PRO C 119 ? 0.5692 0.5661 0.4934 -0.1643 0.0776 -0.0352 118 PRO C CD 4599 N N . LYS C 120 ? 0.4867 0.6191 0.5139 -0.1607 0.0689 -0.0545 119 LYS C N 4600 C CA . LYS C 120 ? 0.4866 0.6386 0.5323 -0.1649 0.0578 -0.0620 119 LYS C CA 4601 C C . LYS C 120 ? 0.5022 0.6379 0.5447 -0.1891 0.0525 -0.0627 119 LYS C C 4602 O O . LYS C 120 ? 0.5114 0.6355 0.5508 -0.1917 0.0381 -0.0701 119 LYS C O 4603 C CB . LYS C 120 ? 0.4728 0.6774 0.5516 -0.1615 0.0636 -0.0625 119 LYS C CB 4604 C CG . LYS C 120 ? 0.4625 0.6883 0.5546 -0.1480 0.0521 -0.0696 119 LYS C CG 4605 C CD . LYS C 120 ? 0.4536 0.7201 0.5683 -0.1349 0.0594 -0.0677 119 LYS C CD 4606 C CE . LYS C 120 ? 0.4571 0.7453 0.5838 -0.1226 0.0478 -0.0735 119 LYS C CE 4607 N NZ . LYS C 120 ? 0.4515 0.7677 0.5920 -0.1054 0.0530 -0.0707 119 LYS C NZ 4608 N N . SER C 121 ? 0.5118 0.6456 0.5534 -0.2070 0.0641 -0.0546 120 SER C N 4609 C CA . SER C 121 ? 0.5373 0.6554 0.5765 -0.2341 0.0604 -0.0526 120 SER C CA 4610 C C . SER C 121 ? 0.5663 0.6233 0.5687 -0.2391 0.0500 -0.0528 120 SER C C 4611 O O . SER C 121 ? 0.5968 0.6327 0.5930 -0.2615 0.0437 -0.0516 120 SER C O 4612 C CB . SER C 121 ? 0.5479 0.6866 0.5977 -0.2518 0.0787 -0.0417 120 SER C CB 4613 O OG . SER C 121 ? 0.5665 0.6702 0.5857 -0.2499 0.0880 -0.0340 120 SER C OG 4614 N N . SER C 122 ? 0.5589 0.5870 0.5372 -0.2190 0.0476 -0.0537 121 SER C N 4615 C CA . SER C 122 ? 0.5875 0.5579 0.5304 -0.2199 0.0374 -0.0539 121 SER C CA 4616 C C . SER C 122 ? 0.5898 0.5417 0.5260 -0.2126 0.0185 -0.0655 121 SER C C 4617 O O . SER C 122 ? 0.6258 0.5292 0.5337 -0.2136 0.0078 -0.0675 121 SER C O 4618 C CB . SER C 122 ? 0.5823 0.5321 0.5039 -0.2007 0.0414 -0.0501 121 SER C CB 4619 O OG . SER C 122 ? 0.5511 0.5216 0.4831 -0.1768 0.0375 -0.0564 121 SER C OG 4620 N N . TRP C 123 ? 0.5555 0.5446 0.5155 -0.2040 0.0143 -0.0734 122 TRP C N 4621 C CA . TRP C 123 ? 0.5591 0.5360 0.5126 -0.1953 -0.0026 -0.0855 122 TRP C CA 4622 C C . TRP C 123 ? 0.5918 0.5613 0.5492 -0.2186 -0.0132 -0.0900 122 TRP C C 4623 O O . TRP C 123 ? 0.5715 0.5802 0.5556 -0.2251 -0.0145 -0.0933 122 TRP C O 4624 C CB . TRP C 123 ? 0.5180 0.5380 0.4925 -0.1755 -0.0024 -0.0910 122 TRP C CB 4625 C CG . TRP C 123 ? 0.4869 0.5136 0.4585 -0.1537 0.0053 -0.0868 122 TRP C CG 4626 C CD1 . TRP C 123 ? 0.4514 0.5127 0.4415 -0.1475 0.0176 -0.0806 122 TRP C CD1 4627 C CD2 . TRP C 123 ? 0.4908 0.4881 0.4396 -0.1358 0.0001 -0.0885 122 TRP C CD2 4628 N NE1 . TRP C 123 ? 0.4361 0.4895 0.4159 -0.1287 0.0194 -0.0781 122 TRP C NE1 4629 C CE2 . TRP C 123 ? 0.4586 0.4758 0.4150 -0.1214 0.0092 -0.0824 122 TRP C CE2 4630 C CE3 . TRP C 123 ? 0.5200 0.4763 0.4431 -0.1295 -0.0120 -0.0948 122 TRP C CE3 4631 C CZ2 . TRP C 123 ? 0.4517 0.4528 0.3939 -0.1033 0.0063 -0.0816 122 TRP C CZ2 4632 C CZ3 . TRP C 123 ? 0.5138 0.4561 0.4231 -0.1089 -0.0137 -0.0944 122 TRP C CZ3 4633 C CH2 . TRP C 123 ? 0.4791 0.4456 0.3996 -0.0972 -0.0045 -0.0874 122 TRP C CH2 4634 N N . SER C 124 ? 0.6453 0.5628 0.5751 -0.2310 -0.0224 -0.0902 123 SER C N 4635 C CA . SER C 124 ? 0.6900 0.5916 0.6196 -0.2569 -0.0345 -0.0935 123 SER C CA 4636 C C . SER C 124 ? 0.7010 0.6005 0.6286 -0.2483 -0.0529 -0.1089 123 SER C C 4637 O O . SER C 124 ? 0.7123 0.6318 0.6582 -0.2656 -0.0603 -0.1126 123 SER C O 4638 C CB . SER C 124 ? 0.7464 0.5848 0.6416 -0.2716 -0.0408 -0.0889 123 SER C CB 4639 O OG . SER C 124 ? 0.7544 0.5902 0.6457 -0.2790 -0.0244 -0.0744 123 SER C OG 4640 N N . ASP C 125 ? 0.7041 0.5803 0.6090 -0.2213 -0.0603 -0.1178 124 ASP C N 4641 C CA . ASP C 125 ? 0.7223 0.5839 0.6141 -0.2105 -0.0784 -0.1333 124 ASP C CA 4642 C C . ASP C 125 ? 0.6788 0.5858 0.5871 -0.1866 -0.0760 -0.1397 124 ASP C C 4643 O O . ASP C 125 ? 0.6913 0.5887 0.5853 -0.1712 -0.0885 -0.1526 124 ASP C O 4644 C CB . ASP C 125 ? 0.7688 0.5684 0.6196 -0.1966 -0.0896 -0.1397 124 ASP C CB 4645 C CG . ASP C 125 ? 0.8263 0.5725 0.6556 -0.2221 -0.0966 -0.1346 124 ASP C CG 4646 O OD1 . ASP C 125 ? 0.8579 0.5935 0.6889 -0.2462 -0.1080 -0.1380 124 ASP C OD1 4647 O OD2 . ASP C 125 ? 0.8490 0.5635 0.6592 -0.2192 -0.0916 -0.1265 124 ASP C OD2 4648 N N . HIS C 126 ? 0.6367 0.5918 0.5732 -0.1832 -0.0600 -0.1306 125 HIS C N 4649 C CA . HIS C 126 ? 0.5994 0.5989 0.5532 -0.1636 -0.0574 -0.1343 125 HIS C CA 4650 C C . HIS C 126 ? 0.5722 0.6242 0.5628 -0.1757 -0.0481 -0.1274 125 HIS C C 4651 O O . HIS C 126 ? 0.5730 0.6327 0.5766 -0.1925 -0.0372 -0.1173 125 HIS C O 4652 C CB . HIS C 126 ? 0.5772 0.5779 0.5230 -0.1381 -0.0485 -0.1305 125 HIS C CB 4653 C CG . HIS C 126 ? 0.6137 0.5678 0.5264 -0.1238 -0.0569 -0.1369 125 HIS C CG 4654 N ND1 . HIS C 126 ? 0.6401 0.5525 0.5334 -0.1294 -0.0561 -0.1318 125 HIS C ND1 4655 C CD2 . HIS C 126 ? 0.6215 0.5647 0.5164 -0.1028 -0.0663 -0.1479 125 HIS C CD2 4656 C CE1 . HIS C 126 ? 0.6648 0.5427 0.5312 -0.1116 -0.0655 -0.1398 125 HIS C CE1 4657 N NE2 . HIS C 126 ? 0.6580 0.5549 0.5251 -0.0948 -0.0710 -0.1498 125 HIS C NE2 4658 N N . GLU C 127 ? 0.5536 0.6414 0.5596 -0.1665 -0.0526 -0.1330 126 GLU C N 4659 C CA . GLU C 127 ? 0.5210 0.6613 0.5624 -0.1725 -0.0449 -0.1272 126 GLU C CA 4660 C C . GLU C 127 ? 0.4779 0.6401 0.5278 -0.1548 -0.0290 -0.1182 126 GLU C C 4661 O O . GLU C 127 ? 0.4705 0.6334 0.5103 -0.1327 -0.0295 -0.1203 126 GLU C O 4662 C CB . GLU C 127 ? 0.5163 0.6839 0.5683 -0.1685 -0.0578 -0.1364 126 GLU C CB 4663 C CG . GLU C 127 ? 0.4930 0.7153 0.5828 -0.1744 -0.0525 -0.1311 126 GLU C CG 4664 C CD . GLU C 127 ? 0.5005 0.7347 0.6127 -0.2019 -0.0469 -0.1243 126 GLU C CD 4665 O OE1 . GLU C 127 ? 0.5273 0.7427 0.6358 -0.2236 -0.0589 -0.1288 126 GLU C OE1 4666 O OE2 . GLU C 127 ? 0.4681 0.7297 0.6005 -0.2018 -0.0304 -0.1142 126 GLU C OE2 4667 N N . ALA C 128 ? 0.4535 0.6327 0.5208 -0.1649 -0.0152 -0.1082 127 ALA C N 4668 C CA . ALA C 128 ? 0.4194 0.6131 0.4920 -0.1504 -0.0007 -0.0998 127 ALA C CA 4669 C C . ALA C 128 ? 0.3898 0.6337 0.4935 -0.1473 0.0060 -0.0962 127 ALA C C 4670 O O . ALA C 128 ? 0.3669 0.6228 0.4747 -0.1341 0.0163 -0.0901 127 ALA C O 4671 C CB . ALA C 128 ? 0.4303 0.5992 0.4919 -0.1602 0.0103 -0.0916 127 ALA C CB 4672 N N . SER C 129 ? 0.3903 0.6617 0.5150 -0.1585 -0.0013 -0.1004 128 SER C N 4673 C CA . SER C 129 ? 0.3677 0.6892 0.5250 -0.1568 0.0041 -0.0971 128 SER C CA 4674 C C . SER C 129 ? 0.3460 0.6959 0.5145 -0.1440 -0.0076 -0.1031 128 SER C C 4675 O O . SER C 129 ? 0.3231 0.7140 0.5182 -0.1402 -0.0048 -0.1006 128 SER C O 4676 C CB . SER C 129 ? 0.3841 0.7253 0.5643 -0.1816 0.0075 -0.0944 128 SER C CB 4677 O OG . SER C 129 ? 0.4112 0.7278 0.5794 -0.1925 0.0202 -0.0872 128 SER C OG 4678 N N . ALA C 130 ? 0.3488 0.6770 0.4956 -0.1356 -0.0202 -0.1105 129 ALA C N 4679 C CA . ALA C 130 ? 0.3372 0.6879 0.4879 -0.1219 -0.0310 -0.1155 129 ALA C CA 4680 C C . ALA C 130 ? 0.3195 0.6624 0.4526 -0.0980 -0.0280 -0.1129 129 ALA C C 4681 O O . ALA C 130 ? 0.3161 0.6707 0.4446 -0.0856 -0.0367 -0.1164 129 ALA C O 4682 C CB . ALA C 130 ? 0.3641 0.7011 0.5034 -0.1310 -0.0491 -0.1268 129 ALA C CB 4683 N N . GLY C 131 ? 0.3125 0.6361 0.4351 -0.0924 -0.0162 -0.1062 130 GLY C N 4684 C CA . GLY C 131 ? 0.2982 0.6147 0.4061 -0.0728 -0.0135 -0.1025 130 GLY C CA 4685 C C . GLY C 131 ? 0.2800 0.6260 0.4037 -0.0608 -0.0086 -0.0951 130 GLY C C 4686 O O . GLY C 131 ? 0.2809 0.6232 0.4060 -0.0561 0.0015 -0.0875 130 GLY C O 4687 N N . VAL C 132 ? 0.2781 0.6502 0.4110 -0.0551 -0.0172 -0.0977 131 VAL C N 4688 C CA . VAL C 132 ? 0.2650 0.6648 0.4138 -0.0440 -0.0147 -0.0910 131 VAL C CA 4689 C C . VAL C 132 ? 0.2617 0.6724 0.4018 -0.0302 -0.0242 -0.0912 131 VAL C C 4690 O O . VAL C 132 ? 0.2763 0.6776 0.4003 -0.0298 -0.0327 -0.0979 131 VAL C O 4691 C CB . VAL C 132 ? 0.2728 0.7040 0.4508 -0.0527 -0.0146 -0.0921 131 VAL C CB 4692 C CG1 . VAL C 132 ? 0.2762 0.7021 0.4632 -0.0628 -0.0010 -0.0884 131 VAL C CG1 4693 C CG2 . VAL C 132 ? 0.2840 0.7255 0.4686 -0.0655 -0.0276 -0.1015 131 VAL C CG2 4694 N N . SER C 133 ? 0.2458 0.6744 0.3944 -0.0182 -0.0229 -0.0838 132 SER C N 4695 C CA . SER C 133 ? 0.2515 0.6880 0.3890 -0.0047 -0.0305 -0.0810 132 SER C CA 4696 C C . SER C 133 ? 0.2464 0.7069 0.3996 0.0051 -0.0324 -0.0746 132 SER C C 4697 O O . SER C 133 ? 0.2377 0.7000 0.4031 0.0068 -0.0242 -0.0695 132 SER C O 4698 C CB . SER C 133 ? 0.2556 0.6704 0.3718 0.0033 -0.0247 -0.0740 132 SER C CB 4699 O OG . SER C 133 ? 0.2613 0.6845 0.3657 0.0156 -0.0300 -0.0688 132 SER C OG 4700 N N . SER C 134 ? 0.2547 0.7314 0.4047 0.0131 -0.0436 -0.0751 133 SER C N 4701 C CA . SER C 134 ? 0.2584 0.7538 0.4184 0.0257 -0.0474 -0.0680 133 SER C CA 4702 C C . SER C 134 ? 0.2538 0.7320 0.4022 0.0359 -0.0399 -0.0556 133 SER C C 4703 O O . SER C 134 ? 0.2530 0.7390 0.4084 0.0463 -0.0415 -0.0489 133 SER C O 4704 C CB . SER C 134 ? 0.2723 0.7823 0.4235 0.0327 -0.0619 -0.0700 133 SER C CB 4705 O OG . SER C 134 ? 0.2893 0.7813 0.4121 0.0351 -0.0622 -0.0692 133 SER C OG 4706 N N . ALA C 135 ? 0.2600 0.7145 0.3906 0.0331 -0.0332 -0.0525 134 ALA C N 4707 C CA . ALA C 135 ? 0.2614 0.6985 0.3813 0.0395 -0.0272 -0.0403 134 ALA C CA 4708 C C . ALA C 135 ? 0.2578 0.6847 0.3888 0.0378 -0.0187 -0.0381 134 ALA C C 4709 O O . ALA C 135 ? 0.2656 0.6795 0.3909 0.0443 -0.0167 -0.0285 134 ALA C O 4710 C CB . ALA C 135 ? 0.2622 0.6823 0.3634 0.0365 -0.0230 -0.0382 134 ALA C CB 4711 N N . CYS C 136 ? 0.2582 0.6901 0.4031 0.0289 -0.0142 -0.0467 135 CYS C N 4712 C CA . CYS C 136 ? 0.2524 0.6748 0.4050 0.0267 -0.0044 -0.0460 135 CYS C CA 4713 C C . CYS C 136 ? 0.2411 0.6899 0.4176 0.0271 -0.0037 -0.0513 135 CYS C C 4714 O O . CYS C 136 ? 0.2289 0.6841 0.4166 0.0157 0.0018 -0.0576 135 CYS C O 4715 C CB . CYS C 136 ? 0.2544 0.6564 0.3991 0.0144 0.0028 -0.0495 135 CYS C CB 4716 S SG . CYS C 136 ? 0.2782 0.6547 0.3992 0.0156 0.0025 -0.0430 135 CYS C SG 4717 N N . PRO C 137 ? 0.2416 0.7072 0.4265 0.0404 -0.0095 -0.0481 136 PRO C N 4718 C CA . PRO C 137 ? 0.2374 0.7348 0.4485 0.0429 -0.0096 -0.0531 136 PRO C CA 4719 C C . PRO C 137 ? 0.2325 0.7270 0.4520 0.0433 0.0037 -0.0536 136 PRO C C 4720 O O . PRO C 137 ? 0.2433 0.7086 0.4458 0.0469 0.0100 -0.0488 136 PRO C O 4721 C CB . PRO C 137 ? 0.2465 0.7564 0.4593 0.0604 -0.0202 -0.0483 136 PRO C CB 4722 C CG . PRO C 137 ? 0.2535 0.7311 0.4401 0.0671 -0.0214 -0.0386 136 PRO C CG 4723 C CD . PRO C 137 ? 0.2495 0.7066 0.4203 0.0534 -0.0171 -0.0391 136 PRO C CD 4724 N N . TYR C 138 ? 0.2232 0.7489 0.4683 0.0388 0.0077 -0.0592 137 TYR C N 4725 C CA . TYR C 138 ? 0.2133 0.7441 0.4682 0.0405 0.0218 -0.0600 137 TYR C CA 4726 C C . TYR C 138 ? 0.2006 0.7793 0.4897 0.0407 0.0219 -0.0645 137 TYR C C 4727 O O . TYR C 138 ? 0.1928 0.7924 0.4978 0.0241 0.0189 -0.0689 137 TYR C O 4728 C CB . TYR C 138 ? 0.2167 0.7261 0.4613 0.0231 0.0330 -0.0613 137 TYR C CB 4729 C CG . TYR C 138 ? 0.2210 0.7351 0.4720 0.0245 0.0486 -0.0616 137 TYR C CG 4730 C CD1 . TYR C 138 ? 0.2309 0.7220 0.4654 0.0398 0.0545 -0.0584 137 TYR C CD1 4731 C CD2 . TYR C 138 ? 0.2312 0.7723 0.5032 0.0103 0.0575 -0.0649 137 TYR C CD2 4732 C CE1 . TYR C 138 ? 0.2421 0.7365 0.4784 0.0432 0.0695 -0.0595 137 TYR C CE1 4733 C CE2 . TYR C 138 ? 0.2375 0.7859 0.5141 0.0124 0.0738 -0.0645 137 TYR C CE2 4734 C CZ . TYR C 138 ? 0.2408 0.7654 0.4983 0.0299 0.0800 -0.0624 137 TYR C CZ 4735 O OH . TYR C 138 ? 0.2554 0.7855 0.5131 0.0336 0.0966 -0.0628 137 TYR C OH 4736 N N . GLN C 139 ? 0.1964 0.7923 0.4970 0.0601 0.0239 -0.0635 138 GLN C N 4737 C CA . GLN C 139 ? 0.1847 0.8306 0.5210 0.0636 0.0266 -0.0672 138 GLN C CA 4738 C C . GLN C 139 ? 0.1839 0.8636 0.5422 0.0541 0.0119 -0.0705 138 GLN C C 4739 O O . GLN C 139 ? 0.1874 0.9034 0.5742 0.0399 0.0143 -0.0742 138 GLN C O 4740 C CB . GLN C 139 ? 0.1776 0.8332 0.5241 0.0514 0.0454 -0.0689 138 GLN C CB 4741 C CG . GLN C 139 ? 0.1802 0.8048 0.5040 0.0642 0.0589 -0.0666 138 GLN C CG 4742 C CD . GLN C 139 ? 0.1794 0.8251 0.5169 0.0599 0.0785 -0.0681 138 GLN C CD 4743 O OE1 . GLN C 139 ? 0.1719 0.8426 0.5286 0.0391 0.0844 -0.0691 138 GLN C OE1 4744 N NE2 . GLN C 139 ? 0.1884 0.8222 0.5136 0.0792 0.0888 -0.0681 138 GLN C NE2 4745 N N . GLY C 140 ? 0.1893 0.8559 0.5326 0.0616 -0.0037 -0.0687 139 GLY C N 4746 C CA . GLY C 140 ? 0.1887 0.8827 0.5466 0.0563 -0.0205 -0.0721 139 GLY C CA 4747 C C . GLY C 140 ? 0.1846 0.8632 0.5302 0.0341 -0.0265 -0.0758 139 GLY C C 4748 O O . GLY C 140 ? 0.1939 0.8907 0.5471 0.0293 -0.0416 -0.0797 139 GLY C O 4749 N N . ARG C 141 ? 0.1779 0.8218 0.5028 0.0217 -0.0161 -0.0752 140 ARG C N 4750 C CA . ARG C 141 ? 0.1743 0.8028 0.4877 0.0020 -0.0217 -0.0799 140 ARG C CA 4751 C C . ARG C 141 ? 0.1766 0.7582 0.4537 0.0023 -0.0187 -0.0769 140 ARG C C 4752 O O . ARG C 141 ? 0.1738 0.7342 0.4363 0.0140 -0.0113 -0.0708 140 ARG C O 4753 C CB . ARG C 141 ? 0.1680 0.8100 0.5007 -0.0202 -0.0139 -0.0839 140 ARG C CB 4754 C CG . ARG C 141 ? 0.1612 0.7805 0.4847 -0.0251 0.0050 -0.0803 140 ARG C CG 4755 C CD . ARG C 141 ? 0.1637 0.7890 0.4994 -0.0502 0.0110 -0.0830 140 ARG C CD 4756 N NE . ARG C 141 ? 0.1632 0.7620 0.4842 -0.0548 0.0282 -0.0792 140 ARG C NE 4757 C CZ . ARG C 141 ? 0.1604 0.7742 0.4930 -0.0493 0.0440 -0.0756 140 ARG C CZ 4758 N NH1 . ARG C 141 ? 0.1542 0.8123 0.5161 -0.0378 0.0457 -0.0755 140 ARG C NH1 4759 N NH2 . ARG C 141 ? 0.1634 0.7476 0.4766 -0.0537 0.0579 -0.0724 140 ARG C NH2 4760 N N . SER C 142 ? 0.1853 0.7514 0.4484 -0.0104 -0.0255 -0.0818 141 SER C N 4761 C CA . SER C 142 ? 0.1881 0.7149 0.4204 -0.0113 -0.0226 -0.0801 141 SER C CA 4762 C C . SER C 142 ? 0.1969 0.7031 0.4259 -0.0226 -0.0084 -0.0793 141 SER C C 4763 O O . SER C 142 ? 0.2001 0.7169 0.4447 -0.0378 -0.0046 -0.0830 141 SER C O 4764 C CB . SER C 142 ? 0.1991 0.7171 0.4163 -0.0183 -0.0351 -0.0869 141 SER C CB 4765 O OG . SER C 142 ? 0.1988 0.7303 0.4113 -0.0058 -0.0477 -0.0863 141 SER C OG 4766 N N . SER C 143 ? 0.2029 0.6796 0.4113 -0.0156 -0.0011 -0.0736 142 SER C N 4767 C CA . SER C 143 ? 0.2121 0.6650 0.4123 -0.0234 0.0112 -0.0718 142 SER C CA 4768 C C . SER C 143 ? 0.2189 0.6372 0.3917 -0.0202 0.0109 -0.0689 142 SER C C 4769 O O . SER C 143 ? 0.2135 0.6279 0.3750 -0.0175 0.0020 -0.0706 142 SER C O 4770 C CB . SER C 143 ? 0.2101 0.6704 0.4199 -0.0148 0.0221 -0.0670 142 SER C CB 4771 O OG . SER C 143 ? 0.2174 0.6515 0.4144 -0.0207 0.0336 -0.0649 142 SER C OG 4772 N N . PHE C 144 ? 0.2257 0.6205 0.3877 -0.0201 0.0204 -0.0644 143 PHE C N 4773 C CA . PHE C 144 ? 0.2409 0.6052 0.3805 -0.0193 0.0203 -0.0617 143 PHE C CA 4774 C C . PHE C 144 ? 0.2447 0.5875 0.3756 -0.0175 0.0295 -0.0561 143 PHE C C 4775 O O . PHE C 144 ? 0.2505 0.6002 0.3901 -0.0172 0.0370 -0.0556 143 PHE C O 4776 C CB . PHE C 144 ? 0.2524 0.6031 0.3837 -0.0318 0.0176 -0.0685 143 PHE C CB 4777 C CG . PHE C 144 ? 0.2588 0.5840 0.3690 -0.0282 0.0157 -0.0670 143 PHE C CG 4778 C CD1 . PHE C 144 ? 0.2613 0.5920 0.3644 -0.0177 0.0095 -0.0650 143 PHE C CD1 4779 C CD2 . PHE C 144 ? 0.2699 0.5675 0.3676 -0.0348 0.0202 -0.0670 143 PHE C CD2 4780 C CE1 . PHE C 144 ? 0.2633 0.5765 0.3501 -0.0135 0.0088 -0.0632 143 PHE C CE1 4781 C CE2 . PHE C 144 ? 0.2798 0.5579 0.3610 -0.0298 0.0178 -0.0658 143 PHE C CE2 4782 C CZ . PHE C 144 ? 0.2701 0.5581 0.3473 -0.0190 0.0127 -0.0639 143 PHE C CZ 4783 N N . PHE C 145 ? 0.2581 0.5762 0.3715 -0.0154 0.0287 -0.0522 144 PHE C N 4784 C CA . PHE C 145 ? 0.2601 0.5531 0.3617 -0.0153 0.0349 -0.0476 144 PHE C CA 4785 C C . PHE C 145 ? 0.2788 0.5630 0.3795 -0.0265 0.0430 -0.0514 144 PHE C C 4786 O O . PHE C 145 ? 0.3002 0.5800 0.3991 -0.0368 0.0417 -0.0561 144 PHE C O 4787 C CB . PHE C 145 ? 0.2528 0.5244 0.3387 -0.0142 0.0310 -0.0440 144 PHE C CB 4788 C CG . PHE C 145 ? 0.2408 0.5212 0.3264 -0.0051 0.0247 -0.0381 144 PHE C CG 4789 C CD1 . PHE C 145 ? 0.2382 0.5165 0.3236 0.0021 0.0238 -0.0305 144 PHE C CD1 4790 C CD2 . PHE C 145 ? 0.2460 0.5356 0.3295 -0.0037 0.0195 -0.0401 144 PHE C CD2 4791 C CE1 . PHE C 145 ? 0.2346 0.5199 0.3188 0.0085 0.0180 -0.0232 144 PHE C CE1 4792 C CE2 . PHE C 145 ? 0.2371 0.5368 0.3191 0.0040 0.0151 -0.0333 144 PHE C CE2 4793 C CZ . PHE C 145 ? 0.2368 0.5347 0.3197 0.0091 0.0144 -0.0240 144 PHE C CZ 4794 N N . ARG C 146 ? 0.2864 0.5661 0.3860 -0.0242 0.0511 -0.0492 145 ARG C N 4795 C CA . ARG C 146 ? 0.2987 0.5733 0.3968 -0.0346 0.0610 -0.0512 145 ARG C CA 4796 C C . ARG C 146 ? 0.2903 0.5304 0.3669 -0.0426 0.0621 -0.0500 145 ARG C C 4797 O O . ARG C 146 ? 0.2966 0.5305 0.3702 -0.0550 0.0673 -0.0518 145 ARG C O 4798 C CB . ARG C 146 ? 0.3208 0.6005 0.4205 -0.0265 0.0702 -0.0494 145 ARG C CB 4799 C CG . ARG C 146 ? 0.3357 0.6506 0.4578 -0.0172 0.0700 -0.0509 145 ARG C CG 4800 C CD . ARG C 146 ? 0.3653 0.7069 0.5045 -0.0230 0.0812 -0.0537 145 ARG C CD 4801 N NE . ARG C 146 ? 0.3899 0.7639 0.5494 -0.0095 0.0810 -0.0548 145 ARG C NE 4802 C CZ . ARG C 146 ? 0.3811 0.7923 0.5667 -0.0115 0.0770 -0.0577 145 ARG C CZ 4803 N NH1 . ARG C 146 ? 0.3804 0.8015 0.5755 -0.0280 0.0726 -0.0604 145 ARG C NH1 4804 N NH2 . ARG C 146 ? 0.3850 0.8225 0.5866 0.0036 0.0760 -0.0582 145 ARG C NH2 4805 N N . ASN C 147 ? 0.2778 0.4958 0.3395 -0.0361 0.0566 -0.0463 146 ASN C N 4806 C CA . ASN C 147 ? 0.2870 0.4721 0.3278 -0.0411 0.0570 -0.0446 146 ASN C CA 4807 C C . ASN C 147 ? 0.2839 0.4577 0.3190 -0.0465 0.0500 -0.0471 146 ASN C C 4808 O O . ASN C 147 ? 0.3025 0.4494 0.3209 -0.0512 0.0496 -0.0464 146 ASN C O 4809 C CB . ASN C 147 ? 0.2865 0.4526 0.3144 -0.0322 0.0543 -0.0392 146 ASN C CB 4810 C CG . ASN C 147 ? 0.2901 0.4591 0.3172 -0.0260 0.0614 -0.0383 146 ASN C CG 4811 O OD1 . ASN C 147 ? 0.3062 0.4756 0.3304 -0.0304 0.0715 -0.0402 146 ASN C OD1 4812 N ND2 . ASN C 147 ? 0.2878 0.4590 0.3169 -0.0155 0.0564 -0.0351 146 ASN C ND2 4813 N N . VAL C 148 ? 0.2715 0.4649 0.3185 -0.0445 0.0441 -0.0505 147 VAL C N 4814 C CA . VAL C 148 ? 0.2809 0.4654 0.3218 -0.0474 0.0373 -0.0550 147 VAL C CA 4815 C C . VAL C 148 ? 0.2909 0.4939 0.3439 -0.0550 0.0358 -0.0616 147 VAL C C 4816 O O . VAL C 148 ? 0.2905 0.5201 0.3603 -0.0547 0.0383 -0.0618 147 VAL C O 4817 C CB . VAL C 148 ? 0.2698 0.4583 0.3092 -0.0359 0.0301 -0.0530 147 VAL C CB 4818 C CG1 . VAL C 148 ? 0.2735 0.4415 0.3013 -0.0315 0.0292 -0.0467 147 VAL C CG1 4819 C CG2 . VAL C 148 ? 0.2564 0.4730 0.3100 -0.0282 0.0290 -0.0504 147 VAL C CG2 4820 N N . VAL C 149 ? 0.3105 0.4983 0.3545 -0.0612 0.0302 -0.0673 148 VAL C N 4821 C CA . VAL C 149 ? 0.3209 0.5204 0.3733 -0.0708 0.0259 -0.0745 148 VAL C CA 4822 C C . VAL C 149 ? 0.3199 0.5193 0.3660 -0.0633 0.0152 -0.0813 148 VAL C C 4823 O O . VAL C 149 ? 0.3323 0.5078 0.3611 -0.0582 0.0109 -0.0834 148 VAL C O 4824 C CB . VAL C 149 ? 0.3497 0.5259 0.3936 -0.0879 0.0276 -0.0761 148 VAL C CB 4825 C CG1 . VAL C 149 ? 0.3678 0.5559 0.4220 -0.1004 0.0215 -0.0829 148 VAL C CG1 4826 C CG2 . VAL C 149 ? 0.3582 0.5357 0.4056 -0.0948 0.0398 -0.0693 148 VAL C CG2 4827 N N . TRP C 150 ? 0.3022 0.5289 0.3613 -0.0613 0.0106 -0.0850 149 TRP C N 4828 C CA . TRP C 150 ? 0.3009 0.5290 0.3514 -0.0537 0.0007 -0.0923 149 TRP C CA 4829 C C . TRP C 150 ? 0.3236 0.5359 0.3675 -0.0667 -0.0073 -0.1019 149 TRP C C 4830 O O . TRP C 150 ? 0.3228 0.5532 0.3806 -0.0769 -0.0113 -0.1056 149 TRP C O 4831 C CB . TRP C 150 ? 0.2859 0.5478 0.3498 -0.0453 -0.0016 -0.0913 149 TRP C CB 4832 C CG . TRP C 150 ? 0.2956 0.5624 0.3490 -0.0357 -0.0106 -0.0977 149 TRP C CG 4833 C CD1 . TRP C 150 ? 0.3213 0.5662 0.3548 -0.0328 -0.0170 -0.1061 149 TRP C CD1 4834 C CD2 . TRP C 150 ? 0.2937 0.5881 0.3530 -0.0263 -0.0144 -0.0967 149 TRP C CD2 4835 N NE1 . TRP C 150 ? 0.3296 0.5881 0.3556 -0.0215 -0.0235 -0.1107 149 TRP C NE1 4836 C CE2 . TRP C 150 ? 0.3127 0.6016 0.3540 -0.0182 -0.0221 -0.1045 149 TRP C CE2 4837 C CE3 . TRP C 150 ? 0.2818 0.6033 0.3578 -0.0228 -0.0124 -0.0900 149 TRP C CE3 4838 C CZ2 . TRP C 150 ? 0.3176 0.6282 0.3559 -0.0078 -0.0273 -0.1052 149 TRP C CZ2 4839 C CZ3 . TRP C 150 ? 0.2875 0.6292 0.3615 -0.0127 -0.0187 -0.0901 149 TRP C CZ3 4840 C CH2 . TRP C 150 ? 0.3043 0.6406 0.3590 -0.0059 -0.0258 -0.0974 149 TRP C CH2 4841 N N . LEU C 151 ? 0.3355 0.5134 0.3582 -0.0665 -0.0109 -0.1058 150 LEU C N 4842 C CA . LEU C 151 ? 0.3725 0.5256 0.3837 -0.0792 -0.0200 -0.1147 150 LEU C CA 4843 C C . LEU C 151 ? 0.3928 0.5479 0.3938 -0.0707 -0.0322 -0.1257 150 LEU C C 4844 O O . LEU C 151 ? 0.3932 0.5513 0.3838 -0.0520 -0.0329 -0.1272 150 LEU C O 4845 C CB . LEU C 151 ? 0.3946 0.5050 0.3835 -0.0803 -0.0203 -0.1145 150 LEU C CB 4846 C CG . LEU C 151 ? 0.3901 0.4877 0.3805 -0.0906 -0.0102 -0.1047 150 LEU C CG 4847 C CD1 . LEU C 151 ? 0.4197 0.4719 0.3839 -0.0894 -0.0143 -0.1060 150 LEU C CD1 4848 C CD2 . LEU C 151 ? 0.3966 0.5039 0.4020 -0.1130 -0.0063 -0.1021 150 LEU C CD2 4849 N N . ILE C 152 ? 0.4161 0.5711 0.4202 -0.0849 -0.0418 -0.1332 151 ILE C N 4850 C CA . ILE C 152 ? 0.4434 0.5928 0.4325 -0.0788 -0.0559 -0.1457 151 ILE C CA 4851 C C . ILE C 152 ? 0.4890 0.6001 0.4622 -0.0952 -0.0680 -0.1547 151 ILE C C 4852 O O . ILE C 152 ? 0.4993 0.5923 0.4755 -0.1124 -0.0644 -0.1496 151 ILE C O 4853 C CB . ILE C 152 ? 0.4271 0.6167 0.4347 -0.0786 -0.0602 -0.1471 151 ILE C CB 4854 C CG1 . ILE C 152 ? 0.4275 0.6336 0.4603 -0.1021 -0.0618 -0.1450 151 ILE C CG1 4855 C CG2 . ILE C 152 ? 0.3885 0.6101 0.4079 -0.0622 -0.0497 -0.1375 151 ILE C CG2 4856 C CD1 . ILE C 152 ? 0.4270 0.6685 0.4760 -0.1029 -0.0709 -0.1489 151 ILE C CD1 4857 N N . LYS C 153 ? 0.5281 0.6245 0.4819 -0.0901 -0.0826 -0.1679 152 LYS C N 4858 C CA . LYS C 153 ? 0.5851 0.6355 0.5167 -0.1030 -0.0965 -0.1776 152 LYS C CA 4859 C C . LYS C 153 ? 0.6100 0.6647 0.5606 -0.1337 -0.1027 -0.1762 152 LYS C C 4860 O O . LYS C 153 ? 0.5962 0.6939 0.5761 -0.1419 -0.1002 -0.1718 152 LYS C O 4861 C CB . LYS C 153 ? 0.6188 0.6499 0.5209 -0.0870 -0.1114 -0.1935 152 LYS C CB 4862 C CG . LYS C 153 ? 0.6206 0.6813 0.5310 -0.0885 -0.1215 -0.2002 152 LYS C CG 4863 C CD . LYS C 153 ? 0.6637 0.6962 0.5380 -0.0737 -0.1374 -0.2175 152 LYS C CD 4864 C CE . LYS C 153 ? 0.6690 0.7240 0.5479 -0.0791 -0.1513 -0.2253 152 LYS C CE 4865 N NZ . LYS C 153 ? 0.6978 0.7400 0.5414 -0.0545 -0.1605 -0.2395 152 LYS C NZ 4866 N N . LYS C 154 ? 0.6629 0.6729 0.5966 -0.1505 -0.1112 -0.1794 153 LYS C N 4867 C CA . LYS C 154 ? 0.6854 0.6960 0.6364 -0.1830 -0.1164 -0.1760 153 LYS C CA 4868 C C . LYS C 154 ? 0.7575 0.7201 0.6803 -0.1934 -0.1385 -0.1895 153 LYS C C 4869 O O . LYS C 154 ? 0.7972 0.7078 0.6865 -0.1861 -0.1437 -0.1944 153 LYS C O 4870 C CB . LYS C 154 ? 0.6869 0.6874 0.6454 -0.1978 -0.1018 -0.1619 153 LYS C CB 4871 C CG . LYS C 154 ? 0.7171 0.7130 0.6898 -0.2333 -0.1058 -0.1568 153 LYS C CG 4872 C CD . LYS C 154 ? 0.6993 0.7160 0.6939 -0.2462 -0.0856 -0.1402 153 LYS C CD 4873 C CE . LYS C 154 ? 0.7307 0.7457 0.7398 -0.2830 -0.0887 -0.1341 153 LYS C CE 4874 N NZ . LYS C 154 ? 0.7178 0.7485 0.7427 -0.2959 -0.0680 -0.1179 153 LYS C NZ 4875 N N . ASP C 155 ? 0.7759 0.7556 0.7116 -0.2092 -0.1528 -0.1959 154 ASP C N 4876 C CA . ASP C 155 ? 0.8361 0.7719 0.7459 -0.2212 -0.1772 -0.2099 154 ASP C CA 4877 C C . ASP C 155 ? 0.8509 0.7494 0.7176 -0.1910 -0.1872 -0.2256 154 ASP C C 4878 O O . ASP C 155 ? 0.8974 0.7366 0.7286 -0.1922 -0.2011 -0.2351 154 ASP C O 4879 C CB . ASP C 155 ? 0.8921 0.7834 0.7942 -0.2507 -0.1815 -0.2043 154 ASP C CB 4880 C CG . ASP C 155 ? 0.8749 0.8067 0.8192 -0.2790 -0.1674 -0.1871 154 ASP C CG 4881 O OD1 . ASP C 155 ? 0.8677 0.8471 0.8457 -0.2929 -0.1707 -0.1860 154 ASP C OD1 4882 O OD2 . ASP C 155 ? 0.8728 0.7899 0.8162 -0.2861 -0.1531 -0.1748 154 ASP C OD2 4883 N N . ASN C 156 ? 0.8117 0.7458 0.6811 -0.1635 -0.1799 -0.2279 155 ASN C N 4884 C CA . ASN C 156 ? 0.8326 0.7443 0.6648 -0.1318 -0.1858 -0.2417 155 ASN C CA 4885 C C . ASN C 156 ? 0.8450 0.7118 0.6480 -0.1147 -0.1801 -0.2425 155 ASN C C 4886 O O . ASN C 156 ? 0.8951 0.7228 0.6599 -0.0955 -0.1911 -0.2570 155 ASN C O 4887 C CB . ASN C 156 ? 0.8894 0.7740 0.6956 -0.1355 -0.2115 -0.2601 155 ASN C CB 4888 C CG . ASN C 156 ? 0.8778 0.8112 0.7097 -0.1445 -0.2182 -0.2609 155 ASN C CG 4889 O OD1 . ASN C 156 ? 0.8365 0.8209 0.6903 -0.1310 -0.2047 -0.2531 155 ASN C OD1 4890 N ND2 . ASN C 156 ? 0.9210 0.8378 0.7499 -0.1677 -0.2406 -0.2699 155 ASN C ND2 4891 N N . ALA C 157 ? 0.8044 0.6777 0.6249 -0.1203 -0.1633 -0.2273 156 ALA C N 4892 C CA . ALA C 157 ? 0.8092 0.6467 0.6071 -0.1038 -0.1570 -0.2256 156 ALA C CA 4893 C C . ALA C 157 ? 0.7471 0.6206 0.5712 -0.0982 -0.1345 -0.2087 156 ALA C C 4894 O O . ALA C 157 ? 0.7081 0.6152 0.5644 -0.1171 -0.1249 -0.1966 156 ALA C O 4895 C CB . ALA C 157 ? 0.8592 0.6367 0.6368 -0.1245 -0.1685 -0.2268 156 ALA C CB 4896 N N . TYR C 158 ? 0.7364 0.6032 0.5464 -0.0715 -0.1269 -0.2084 157 TYR C N 4897 C CA . TYR C 158 ? 0.6926 0.5833 0.5215 -0.0652 -0.1086 -0.1935 157 TYR C CA 4898 C C . TYR C 158 ? 0.7230 0.5682 0.5260 -0.0529 -0.1098 -0.1940 157 TYR C C 4899 O O . TYR C 158 ? 0.7256 0.5711 0.5156 -0.0251 -0.1080 -0.1986 157 TYR C O 4900 C CB . TYR C 158 ? 0.6433 0.5848 0.4875 -0.0434 -0.0978 -0.1907 157 TYR C CB 4901 C CG . TYR C 158 ? 0.5839 0.5577 0.4529 -0.0407 -0.0801 -0.1746 157 TYR C CG 4902 C CD1 . TYR C 158 ? 0.5811 0.5365 0.4423 -0.0310 -0.0740 -0.1686 157 TYR C CD1 4903 C CD2 . TYR C 158 ? 0.5441 0.5652 0.4426 -0.0468 -0.0710 -0.1659 157 TYR C CD2 4904 C CE1 . TYR C 158 ? 0.5381 0.5203 0.4198 -0.0291 -0.0599 -0.1547 157 TYR C CE1 4905 C CE2 . TYR C 158 ? 0.4981 0.5441 0.4160 -0.0438 -0.0565 -0.1522 157 TYR C CE2 4906 C CZ . TYR C 158 ? 0.4978 0.5238 0.4068 -0.0356 -0.0513 -0.1468 157 TYR C CZ 4907 O OH . TYR C 158 ? 0.4575 0.5049 0.3835 -0.0334 -0.0389 -0.1339 157 TYR C OH 4908 N N . PRO C 159 ? 0.7545 0.5608 0.5497 -0.0735 -0.1132 -0.1890 158 PRO C N 4909 C CA . PRO C 159 ? 0.7799 0.5410 0.5508 -0.0635 -0.1151 -0.1876 158 PRO C CA 4910 C C . PRO C 159 ? 0.7338 0.5216 0.5165 -0.0436 -0.1007 -0.1780 158 PRO C C 4911 O O . PRO C 159 ? 0.6817 0.5185 0.4933 -0.0452 -0.0875 -0.1689 158 PRO C O 4912 C CB . PRO C 159 ? 0.8005 0.5335 0.5719 -0.0951 -0.1157 -0.1777 158 PRO C CB 4913 C CG . PRO C 159 ? 0.8186 0.5595 0.5998 -0.1191 -0.1239 -0.1823 158 PRO C CG 4914 C CD . PRO C 159 ? 0.7715 0.5714 0.5776 -0.1077 -0.1177 -0.1852 158 PRO C CD 4915 N N . THR C 160 ? 0.7571 0.5118 0.5173 -0.0248 -0.1043 -0.1802 159 THR C N 4916 C CA . THR C 160 ? 0.7256 0.5040 0.4973 -0.0071 -0.0929 -0.1710 159 THR C CA 4917 C C . THR C 160 ? 0.7087 0.4876 0.4937 -0.0279 -0.0837 -0.1551 159 THR C C 4918 O O . THR C 160 ? 0.7390 0.4749 0.5076 -0.0445 -0.0890 -0.1519 159 THR C O 4919 C CB . THR C 160 ? 0.7572 0.5029 0.5032 0.0199 -0.1005 -0.1777 159 THR C CB 4920 O OG1 . THR C 160 ? 0.7760 0.5211 0.5068 0.0405 -0.1081 -0.1936 159 THR C OG1 4921 C CG2 . THR C 160 ? 0.7181 0.4954 0.4808 0.0373 -0.0894 -0.1675 159 THR C CG2 4922 N N . ILE C 161 ? 0.6607 0.4874 0.4737 -0.0273 -0.0700 -0.1451 160 ILE C N 4923 C CA . ILE C 161 ? 0.6504 0.4812 0.4747 -0.0428 -0.0602 -0.1310 160 ILE C CA 4924 C C . ILE C 161 ? 0.6758 0.4841 0.4864 -0.0278 -0.0613 -0.1262 160 ILE C C 4925 O O . ILE C 161 ? 0.6678 0.4900 0.4795 -0.0037 -0.0623 -0.1292 160 ILE C O 4926 C CB . ILE C 161 ? 0.5968 0.4833 0.4532 -0.0450 -0.0470 -0.1232 160 ILE C CB 4927 C CG1 . ILE C 161 ? 0.5856 0.4925 0.4570 -0.0638 -0.0462 -0.1258 160 ILE C CG1 4928 C CG2 . ILE C 161 ? 0.5760 0.4657 0.4397 -0.0520 -0.0370 -0.1096 160 ILE C CG2 4929 C CD1 . ILE C 161 ? 0.5377 0.4985 0.4378 -0.0609 -0.0364 -0.1213 160 ILE C CD1 4930 N N . LYS C 162 ? 0.7186 0.4928 0.5159 -0.0424 -0.0613 -0.1182 161 LYS C N 4931 C CA . LYS C 162 ? 0.7396 0.4948 0.5256 -0.0314 -0.0620 -0.1112 161 LYS C CA 4932 C C . LYS C 162 ? 0.7487 0.5025 0.5385 -0.0522 -0.0522 -0.0979 161 LYS C C 4933 O O . LYS C 162 ? 0.7847 0.5022 0.5568 -0.0713 -0.0542 -0.0943 161 LYS C O 4934 C CB . LYS C 162 ? 0.7930 0.4907 0.5453 -0.0231 -0.0765 -0.1173 161 LYS C CB 4935 C CG . LYS C 162 ? 0.8066 0.5051 0.5521 0.0046 -0.0855 -0.1307 161 LYS C CG 4936 C CD . LYS C 162 ? 0.8691 0.5050 0.5781 0.0118 -0.1014 -0.1388 161 LYS C CD 4937 C CE . LYS C 162 ? 0.8830 0.5220 0.5844 0.0456 -0.1088 -0.1516 161 LYS C CE 4938 N NZ . LYS C 162 ? 0.9502 0.5270 0.6141 0.0533 -0.1258 -0.1634 161 LYS C NZ 4939 N N . ARG C 163 ? 0.7187 0.5114 0.5299 -0.0486 -0.0418 -0.0904 162 ARG C N 4940 C CA . ARG C 163 ? 0.7243 0.5216 0.5397 -0.0657 -0.0310 -0.0791 162 ARG C CA 4941 C C . ARG C 163 ? 0.6926 0.4955 0.5085 -0.0537 -0.0289 -0.0714 162 ARG C C 4942 O O . ARG C 163 ? 0.6592 0.4921 0.4913 -0.0371 -0.0292 -0.0725 162 ARG C O 4943 C CB . ARG C 163 ? 0.7126 0.5541 0.5555 -0.0772 -0.0199 -0.0782 162 ARG C CB 4944 C CG . ARG C 163 ? 0.7550 0.5958 0.6010 -0.0916 -0.0229 -0.0853 162 ARG C CG 4945 C CD . ARG C 163 ? 0.8079 0.6192 0.6406 -0.1168 -0.0208 -0.0799 162 ARG C CD 4946 N NE . ARG C 163 ? 0.7927 0.6394 0.6482 -0.1339 -0.0075 -0.0741 162 ARG C NE 4947 C CZ . ARG C 163 ? 0.7776 0.6331 0.6356 -0.1400 0.0049 -0.0640 162 ARG C CZ 4948 N NH1 . ARG C 163 ? 0.7998 0.6295 0.6375 -0.1326 0.0053 -0.0579 162 ARG C NH1 4949 N NH2 . ARG C 163 ? 0.7526 0.6434 0.6328 -0.1528 0.0167 -0.0605 162 ARG C NH2 4950 N N . SER C 164 ? 0.6980 0.4710 0.4948 -0.0632 -0.0273 -0.0631 163 SER C N 4951 C CA . SER C 164 ? 0.6689 0.4425 0.4624 -0.0552 -0.0263 -0.0553 163 SER C CA 4952 C C . SER C 164 ? 0.6369 0.4256 0.4363 -0.0701 -0.0128 -0.0476 163 SER C C 4953 O O . SER C 164 ? 0.6378 0.4213 0.4338 -0.0886 -0.0050 -0.0457 163 SER C O 4954 C CB . SER C 164 ? 0.7050 0.4283 0.4662 -0.0525 -0.0361 -0.0515 163 SER C CB 4955 O OG . SER C 164 ? 0.7352 0.4403 0.4879 -0.0363 -0.0493 -0.0589 163 SER C OG 4956 N N . TYR C 165 ? 0.6009 0.4088 0.4091 -0.0615 -0.0106 -0.0432 164 TYR C N 4957 C CA . TYR C 165 ? 0.5902 0.4004 0.3938 -0.0708 -0.0004 -0.0359 164 TYR C CA 4958 C C . TYR C 165 ? 0.5986 0.3889 0.3855 -0.0610 -0.0079 -0.0305 164 TYR C C 4959 O O . TYR C 165 ? 0.5659 0.3724 0.3656 -0.0468 -0.0155 -0.0313 164 TYR C O 4960 C CB . TYR C 165 ? 0.5440 0.3990 0.3756 -0.0709 0.0094 -0.0367 164 TYR C CB 4961 C CG . TYR C 165 ? 0.5450 0.4001 0.3691 -0.0762 0.0189 -0.0304 164 TYR C CG 4962 C CD1 . TYR C 165 ? 0.5668 0.4143 0.3805 -0.0916 0.0309 -0.0272 164 TYR C CD1 4963 C CD2 . TYR C 165 ? 0.5266 0.3877 0.3520 -0.0659 0.0155 -0.0275 164 TYR C CD2 4964 C CE1 . TYR C 165 ? 0.5702 0.4172 0.3736 -0.0940 0.0406 -0.0222 164 TYR C CE1 4965 C CE2 . TYR C 165 ? 0.5337 0.3900 0.3476 -0.0690 0.0230 -0.0231 164 TYR C CE2 4966 C CZ . TYR C 165 ? 0.5610 0.4102 0.3628 -0.0817 0.0361 -0.0210 164 TYR C CZ 4967 O OH . TYR C 165 ? 0.5846 0.4293 0.3723 -0.0823 0.0445 -0.0175 164 TYR C OH 4968 N N . ASN C 166 ? 0.6382 0.3939 0.3961 -0.0698 -0.0060 -0.0244 165 ASN C N 4969 C CA . ASN C 166 ? 0.6662 0.3994 0.4037 -0.0625 -0.0136 -0.0190 165 ASN C CA 4970 C C . ASN C 166 ? 0.6409 0.3848 0.3759 -0.0674 -0.0031 -0.0147 165 ASN C C 4971 O O . ASN C 166 ? 0.6534 0.3896 0.3751 -0.0803 0.0094 -0.0115 165 ASN C O 4972 C CB . ASN C 166 ? 0.7398 0.4226 0.4409 -0.0675 -0.0197 -0.0148 165 ASN C CB 4973 C CG . ASN C 166 ? 0.7992 0.4554 0.4762 -0.0591 -0.0301 -0.0093 165 ASN C CG 4974 O OD1 . ASN C 166 ? 0.7793 0.4496 0.4601 -0.0555 -0.0290 -0.0072 165 ASN C OD1 4975 N ND2 . ASN C 166 ? 0.8845 0.4991 0.5346 -0.0558 -0.0420 -0.0071 165 ASN C ND2 4976 N N . ASN C 167 ? 0.6091 0.3713 0.3566 -0.0568 -0.0085 -0.0146 166 ASN C N 4977 C CA . ASN C 167 ? 0.5996 0.3664 0.3411 -0.0587 -0.0015 -0.0117 166 ASN C CA 4978 C C . ASN C 167 ? 0.6457 0.3713 0.3469 -0.0622 -0.0028 -0.0062 166 ASN C C 4979 O O . ASN C 167 ? 0.6592 0.3655 0.3460 -0.0543 -0.0167 -0.0038 166 ASN C O 4980 C CB . ASN C 167 ? 0.5709 0.3602 0.3323 -0.0477 -0.0105 -0.0123 166 ASN C CB 4981 C CG . ASN C 167 ? 0.5739 0.3619 0.3255 -0.0484 -0.0060 -0.0103 166 ASN C CG 4982 O OD1 . ASN C 167 ? 0.5764 0.3622 0.3169 -0.0552 0.0082 -0.0104 166 ASN C OD1 4983 N ND2 . ASN C 167 ? 0.5648 0.3543 0.3202 -0.0410 -0.0186 -0.0087 166 ASN C ND2 4984 N N . THR C 168 ? 0.6704 0.3843 0.3539 -0.0746 0.0116 -0.0037 167 THR C N 4985 C CA . THR C 168 ? 0.7187 0.3935 0.3601 -0.0796 0.0136 0.0025 167 THR C CA 4986 C C . THR C 168 ? 0.7202 0.3986 0.3497 -0.0765 0.0207 0.0030 167 THR C C 4987 O O . THR C 168 ? 0.7637 0.4157 0.3579 -0.0808 0.0273 0.0075 167 THR C O 4988 C CB . THR C 168 ? 0.7517 0.4127 0.3781 -0.0960 0.0271 0.0066 167 THR C CB 4989 O OG1 . THR C 168 ? 0.7386 0.4387 0.3946 -0.1037 0.0428 0.0034 167 THR C OG1 4990 C CG2 . THR C 168 ? 0.7704 0.4074 0.3920 -0.0982 0.0154 0.0071 167 THR C CG2 4991 N N . ASN C 169 ? 0.6882 0.3967 0.3445 -0.0684 0.0188 -0.0015 168 ASN C N 4992 C CA . ASN C 169 ? 0.6880 0.3986 0.3341 -0.0636 0.0237 -0.0025 168 ASN C CA 4993 C C . ASN C 169 ? 0.6976 0.3865 0.3286 -0.0544 0.0043 -0.0018 168 ASN C C 4994 O O . ASN C 169 ? 0.6895 0.3779 0.3329 -0.0499 -0.0121 -0.0012 168 ASN C O 4995 C CB . ASN C 169 ? 0.6517 0.4041 0.3337 -0.0606 0.0315 -0.0074 168 ASN C CB 4996 C CG . ASN C 169 ? 0.6387 0.4184 0.3422 -0.0696 0.0476 -0.0087 168 ASN C CG 4997 O OD1 . ASN C 169 ? 0.6546 0.4450 0.3544 -0.0737 0.0645 -0.0088 168 ASN C OD1 4998 N ND2 . ASN C 169 ? 0.6201 0.4114 0.3457 -0.0724 0.0419 -0.0099 168 ASN C ND2 4999 N N . GLN C 170 ? 0.7181 0.3902 0.3223 -0.0512 0.0064 -0.0021 169 GLN C N 5000 C CA . GLN C 170 ? 0.7322 0.3825 0.3198 -0.0438 -0.0124 -0.0020 169 GLN C CA 5001 C C . GLN C 170 ? 0.6867 0.3645 0.3098 -0.0383 -0.0231 -0.0047 169 GLN C C 5002 O O . GLN C 170 ? 0.6774 0.3450 0.2994 -0.0343 -0.0428 -0.0034 169 GLN C O 5003 C CB . GLN C 170 ? 0.7811 0.4050 0.3274 -0.0414 -0.0058 -0.0030 169 GLN C CB 5004 C CG . GLN C 170 ? 0.8284 0.4257 0.3355 -0.0474 0.0073 0.0011 169 GLN C CG 5005 C CD . GLN C 170 ? 0.8590 0.4272 0.3482 -0.0505 -0.0064 0.0069 169 GLN C CD 5006 O OE1 . GLN C 170 ? 0.8704 0.4336 0.3550 -0.0589 0.0025 0.0112 169 GLN C OE1 5007 N NE2 . GLN C 170 ? 0.8694 0.4182 0.3493 -0.0438 -0.0297 0.0072 169 GLN C NE2 5008 N N . GLU C 171 ? 0.6545 0.3676 0.3090 -0.0390 -0.0108 -0.0077 170 GLU C N 5009 C CA . GLU C 171 ? 0.6253 0.3641 0.3108 -0.0347 -0.0180 -0.0093 170 GLU C CA 5010 C C . GLU C 171 ? 0.5922 0.3602 0.3158 -0.0351 -0.0250 -0.0077 170 GLU C C 5011 O O . GLU C 171 ? 0.5871 0.3631 0.3189 -0.0382 -0.0186 -0.0079 170 GLU C O 5012 C CB . GLU C 171 ? 0.6105 0.3701 0.3060 -0.0331 -0.0013 -0.0133 170 GLU C CB 5013 C CG . GLU C 171 ? 0.6472 0.3827 0.3061 -0.0297 0.0082 -0.0161 170 GLU C CG 5014 C CD . GLU C 171 ? 0.6683 0.4022 0.3106 -0.0347 0.0288 -0.0158 170 GLU C CD 5015 O OE1 . GLU C 171 ? 0.6700 0.4057 0.3172 -0.0427 0.0313 -0.0125 170 GLU C OE1 5016 O OE2 . GLU C 171 ? 0.6824 0.4129 0.3060 -0.0307 0.0427 -0.0187 170 GLU C OE2 5017 N N . ASP C 172 ? 0.5770 0.3599 0.3222 -0.0321 -0.0380 -0.0061 171 ASP C N 5018 C CA . ASP C 172 ? 0.5430 0.3624 0.3275 -0.0313 -0.0404 -0.0049 171 ASP C CA 5019 C C . ASP C 172 ? 0.5153 0.3629 0.3196 -0.0324 -0.0234 -0.0082 171 ASP C C 5020 O O . ASP C 172 ? 0.5158 0.3639 0.3146 -0.0321 -0.0143 -0.0105 171 ASP C O 5021 C CB . ASP C 172 ? 0.5439 0.3760 0.3474 -0.0299 -0.0553 -0.0008 171 ASP C CB 5022 C CG . ASP C 172 ? 0.5660 0.3855 0.3653 -0.0289 -0.0747 0.0033 171 ASP C CG 5023 O OD1 . ASP C 172 ? 0.5946 0.4041 0.3853 -0.0268 -0.0772 0.0032 171 ASP C OD1 5024 O OD2 . ASP C 172 ? 0.5897 0.4093 0.3950 -0.0305 -0.0886 0.0071 171 ASP C OD2 5025 N N . LEU C 173 ? 0.4876 0.3586 0.3144 -0.0325 -0.0204 -0.0090 172 LEU C N 5026 C CA . LEU C 173 ? 0.4626 0.3588 0.3065 -0.0344 -0.0061 -0.0127 172 LEU C CA 5027 C C . LEU C 173 ? 0.4282 0.3592 0.3048 -0.0311 -0.0094 -0.0118 172 LEU C C 5028 O O . LEU C 173 ? 0.4203 0.3596 0.3079 -0.0281 -0.0173 -0.0106 172 LEU C O 5029 C CB . LEU C 173 ? 0.4840 0.3718 0.3194 -0.0391 0.0011 -0.0153 172 LEU C CB 5030 C CG . LEU C 173 ? 0.4761 0.3874 0.3270 -0.0436 0.0151 -0.0192 172 LEU C CG 5031 C CD1 . LEU C 173 ? 0.4826 0.3985 0.3288 -0.0453 0.0274 -0.0202 172 LEU C CD1 5032 C CD2 . LEU C 173 ? 0.4955 0.3927 0.3359 -0.0505 0.0187 -0.0208 172 LEU C CD2 5033 N N . LEU C 174 ? 0.3999 0.3513 0.2907 -0.0303 -0.0033 -0.0123 173 LEU C N 5034 C CA . LEU C 174 ? 0.3733 0.3584 0.2926 -0.0277 -0.0042 -0.0110 173 LEU C CA 5035 C C . LEU C 174 ? 0.3523 0.3572 0.2833 -0.0288 0.0058 -0.0163 173 LEU C C 5036 O O . LEU C 174 ? 0.3450 0.3585 0.2785 -0.0307 0.0158 -0.0194 173 LEU C O 5037 C CB . LEU C 174 ? 0.3679 0.3616 0.2942 -0.0260 -0.0045 -0.0083 173 LEU C CB 5038 C CG . LEU C 174 ? 0.3471 0.3742 0.2999 -0.0238 -0.0054 -0.0053 173 LEU C CG 5039 C CD1 . LEU C 174 ? 0.3436 0.3788 0.3074 -0.0234 -0.0171 0.0013 173 LEU C CD1 5040 C CD2 . LEU C 174 ? 0.3502 0.3822 0.3065 -0.0218 -0.0035 -0.0037 173 LEU C CD2 5041 N N . VAL C 175 ? 0.3415 0.3537 0.2796 -0.0270 0.0022 -0.0177 174 VAL C N 5042 C CA . VAL C 175 ? 0.3304 0.3570 0.2769 -0.0283 0.0086 -0.0235 174 VAL C CA 5043 C C . VAL C 175 ? 0.3035 0.3642 0.2731 -0.0231 0.0078 -0.0230 174 VAL C C 5044 O O . VAL C 175 ? 0.2885 0.3602 0.2672 -0.0179 0.0009 -0.0182 174 VAL C O 5045 C CB . VAL C 175 ? 0.3455 0.3537 0.2805 -0.0278 0.0042 -0.0266 174 VAL C CB 5046 C CG1 . VAL C 175 ? 0.3473 0.3638 0.2871 -0.0303 0.0087 -0.0334 174 VAL C CG1 5047 C CG2 . VAL C 175 ? 0.3750 0.3474 0.2842 -0.0330 0.0040 -0.0252 174 VAL C CG2 5048 N N . LEU C 176 ? 0.2962 0.3746 0.2751 -0.0250 0.0147 -0.0274 175 LEU C N 5049 C CA . LEU C 176 ? 0.2788 0.3883 0.2761 -0.0201 0.0145 -0.0272 175 LEU C CA 5050 C C . LEU C 176 ? 0.2788 0.3966 0.2785 -0.0204 0.0160 -0.0351 175 LEU C C 5051 O O . LEU C 176 ? 0.2917 0.3991 0.2853 -0.0277 0.0201 -0.0404 175 LEU C O 5052 C CB . LEU C 176 ? 0.2734 0.3968 0.2791 -0.0208 0.0191 -0.0252 175 LEU C CB 5053 C CG . LEU C 176 ? 0.2850 0.3947 0.2845 -0.0203 0.0167 -0.0187 175 LEU C CG 5054 C CD1 . LEU C 176 ? 0.2862 0.4040 0.2900 -0.0190 0.0217 -0.0187 175 LEU C CD1 5055 C CD2 . LEU C 176 ? 0.2779 0.3937 0.2838 -0.0170 0.0081 -0.0108 175 LEU C CD2 5056 N N . TRP C 177 ? 0.2681 0.4049 0.2760 -0.0130 0.0126 -0.0358 176 TRP C N 5057 C CA . TRP C 177 ? 0.2732 0.4175 0.2812 -0.0116 0.0124 -0.0442 176 TRP C CA 5058 C C . TRP C 177 ? 0.2630 0.4372 0.2821 -0.0027 0.0113 -0.0430 176 TRP C C 5059 O O . TRP C 177 ? 0.2543 0.4426 0.2814 0.0011 0.0107 -0.0344 176 TRP C O 5060 C CB . TRP C 177 ? 0.2879 0.4079 0.2813 -0.0097 0.0081 -0.0498 176 TRP C CB 5061 C CG . TRP C 177 ? 0.2871 0.4096 0.2804 0.0015 0.0029 -0.0467 176 TRP C CG 5062 C CD1 . TRP C 177 ? 0.2887 0.4257 0.2839 0.0131 0.0004 -0.0505 176 TRP C CD1 5063 C CD2 . TRP C 177 ? 0.2944 0.4058 0.2856 0.0030 -0.0005 -0.0394 176 TRP C CD2 5064 N NE1 . TRP C 177 ? 0.2906 0.4305 0.2882 0.0220 -0.0033 -0.0455 176 TRP C NE1 5065 C CE2 . TRP C 177 ? 0.2934 0.4178 0.2895 0.0152 -0.0050 -0.0385 176 TRP C CE2 5066 C CE3 . TRP C 177 ? 0.2966 0.3892 0.2815 -0.0042 -0.0007 -0.0339 176 TRP C CE3 5067 C CZ2 . TRP C 177 ? 0.2981 0.4197 0.2965 0.0191 -0.0105 -0.0317 176 TRP C CZ2 5068 C CZ3 . TRP C 177 ? 0.3085 0.3941 0.2922 -0.0005 -0.0073 -0.0277 176 TRP C CZ3 5069 C CH2 . TRP C 177 ? 0.3046 0.4059 0.2968 0.0104 -0.0126 -0.0263 176 TRP C CH2 5070 N N . GLY C 178 ? 0.2665 0.4494 0.2845 -0.0006 0.0106 -0.0511 177 GLY C N 5071 C CA . GLY C 178 ? 0.2620 0.4722 0.2862 0.0083 0.0100 -0.0503 177 GLY C CA 5072 C C . GLY C 178 ? 0.2769 0.4860 0.2912 0.0151 0.0067 -0.0609 177 GLY C C 5073 O O . GLY C 178 ? 0.2902 0.4746 0.2927 0.0126 0.0037 -0.0690 177 GLY C O 5074 N N . ILE C 179 ? 0.2823 0.5167 0.2992 0.0242 0.0070 -0.0604 178 ILE C N 5075 C CA . ILE C 179 ? 0.2931 0.5297 0.2983 0.0330 0.0038 -0.0712 178 ILE C CA 5076 C C . ILE C 179 ? 0.2816 0.5430 0.2908 0.0339 0.0040 -0.0709 178 ILE C C 5077 O O . ILE C 179 ? 0.2645 0.5471 0.2844 0.0345 0.0075 -0.0598 178 ILE C O 5078 C CB . ILE C 179 ? 0.3040 0.5481 0.3039 0.0485 0.0045 -0.0707 178 ILE C CB 5079 C CG1 . ILE C 179 ? 0.3289 0.5717 0.3120 0.0601 0.0011 -0.0839 178 ILE C CG1 5080 C CG2 . ILE C 179 ? 0.2868 0.5634 0.3001 0.0533 0.0098 -0.0571 178 ILE C CG2 5081 C CD1 . ILE C 179 ? 0.3395 0.5906 0.3165 0.0784 0.0027 -0.0851 178 ILE C CD1 5082 N N . HIS C 180 ? 0.2940 0.5507 0.2933 0.0337 -0.0010 -0.0828 179 HIS C N 5083 C CA . HIS C 180 ? 0.2888 0.5680 0.2882 0.0365 -0.0030 -0.0843 179 HIS C CA 5084 C C . HIS C 180 ? 0.3035 0.5956 0.2882 0.0529 -0.0031 -0.0880 179 HIS C C 5085 O O . HIS C 180 ? 0.3237 0.5995 0.2919 0.0604 -0.0067 -0.0994 179 HIS C O 5086 C CB . HIS C 180 ? 0.3014 0.5707 0.2989 0.0262 -0.0102 -0.0952 179 HIS C CB 5087 C CG . HIS C 180 ? 0.3049 0.5963 0.3020 0.0290 -0.0146 -0.0974 179 HIS C CG 5088 N ND1 . HIS C 180 ? 0.3268 0.6123 0.3097 0.0301 -0.0238 -0.1108 179 HIS C ND1 5089 C CD2 . HIS C 180 ? 0.2886 0.6055 0.2953 0.0315 -0.0126 -0.0879 179 HIS C CD2 5090 C CE1 . HIS C 180 ? 0.3280 0.6364 0.3124 0.0333 -0.0272 -0.1095 179 HIS C CE1 5091 N NE2 . HIS C 180 ? 0.3062 0.6337 0.3048 0.0345 -0.0202 -0.0953 179 HIS C NE2 5092 N N . HIS C 181 ? 0.2964 0.6165 0.2853 0.0588 0.0008 -0.0782 180 HIS C N 5093 C CA . HIS C 181 ? 0.3095 0.6476 0.2838 0.0741 0.0025 -0.0800 180 HIS C CA 5094 C C . HIS C 181 ? 0.3228 0.6688 0.2861 0.0751 -0.0040 -0.0871 180 HIS C C 5095 O O . HIS C 181 ? 0.3101 0.6747 0.2808 0.0723 -0.0035 -0.0777 180 HIS C O 5096 C CB . HIS C 181 ? 0.2948 0.6599 0.2793 0.0785 0.0112 -0.0625 180 HIS C CB 5097 C CG . HIS C 181 ? 0.2838 0.6454 0.2798 0.0780 0.0160 -0.0550 180 HIS C CG 5098 N ND1 . HIS C 181 ? 0.2923 0.6453 0.2806 0.0883 0.0168 -0.0626 180 HIS C ND1 5099 C CD2 . HIS C 181 ? 0.2614 0.6265 0.2749 0.0693 0.0190 -0.0407 180 HIS C CD2 5100 C CE1 . HIS C 181 ? 0.2773 0.6311 0.2799 0.0856 0.0198 -0.0530 180 HIS C CE1 5101 N NE2 . HIS C 181 ? 0.2608 0.6210 0.2782 0.0734 0.0209 -0.0398 180 HIS C NE2 5102 N N . PRO C 182 ? 0.3515 0.6815 0.2956 0.0796 -0.0118 -0.1039 181 PRO C N 5103 C CA . PRO C 182 ? 0.3736 0.7098 0.3067 0.0795 -0.0205 -0.1115 181 PRO C CA 5104 C C . PRO C 182 ? 0.3883 0.7498 0.3062 0.0941 -0.0174 -0.1071 181 PRO C C 5105 O O . PRO C 182 ? 0.3877 0.7645 0.3032 0.1049 -0.0072 -0.0984 181 PRO C O 5106 C CB . PRO C 182 ? 0.4012 0.7079 0.3154 0.0797 -0.0310 -0.1309 181 PRO C CB 5107 C CG . PRO C 182 ? 0.3999 0.6833 0.3164 0.0787 -0.0274 -0.1324 181 PRO C CG 5108 C CD . PRO C 182 ? 0.3742 0.6772 0.3035 0.0852 -0.0147 -0.1169 181 PRO C CD 5109 N N . ASN C 183 ? 0.4098 0.7768 0.3177 0.0937 -0.0266 -0.1129 182 ASN C N 5110 C CA . ASN C 183 ? 0.4320 0.8216 0.3226 0.1060 -0.0252 -0.1083 182 ASN C CA 5111 C C . ASN C 183 ? 0.4701 0.8540 0.3270 0.1233 -0.0271 -0.1223 182 ASN C C 5112 O O . ASN C 183 ? 0.4753 0.8797 0.3159 0.1370 -0.0202 -0.1164 182 ASN C O 5113 C CB . ASN C 183 ? 0.4408 0.8381 0.3346 0.0987 -0.0362 -0.1082 182 ASN C CB 5114 C CG . ASN C 183 ? 0.4177 0.8235 0.3415 0.0859 -0.0339 -0.0941 182 ASN C CG 5115 O OD1 . ASN C 183 ? 0.4083 0.8283 0.3403 0.0877 -0.0246 -0.0775 182 ASN C OD1 5116 N ND2 . ASN C 183 ? 0.4206 0.8177 0.3608 0.0727 -0.0426 -0.1006 182 ASN C ND2 5117 N N . ASP C 184 ? 0.5001 0.8548 0.3449 0.1225 -0.0366 -0.1407 183 ASP C N 5118 C CA . ASP C 184 ? 0.5514 0.8928 0.3605 0.1397 -0.0413 -0.1576 183 ASP C CA 5119 C C . ASP C 184 ? 0.5690 0.8707 0.3702 0.1353 -0.0514 -0.1752 183 ASP C C 5120 O O . ASP C 184 ? 0.5544 0.8413 0.3778 0.1169 -0.0554 -0.1740 183 ASP C O 5121 C CB . ASP C 184 ? 0.5889 0.9373 0.3750 0.1440 -0.0521 -0.1642 183 ASP C CB 5122 C CG . ASP C 184 ? 0.5914 0.9327 0.3927 0.1243 -0.0677 -0.1677 183 ASP C CG 5123 O OD1 . ASP C 184 ? 0.6029 0.9192 0.4140 0.1107 -0.0763 -0.1772 183 ASP C OD1 5124 O OD2 . ASP C 184 ? 0.5990 0.9610 0.4022 0.1226 -0.0717 -0.1606 183 ASP C OD2 5125 N N . ALA C 185 ? 0.6070 0.8903 0.3746 0.1529 -0.0553 -0.1913 184 ALA C N 5126 C CA . ALA C 185 ? 0.6375 0.8771 0.3909 0.1511 -0.0666 -0.2089 184 ALA C CA 5127 C C . ALA C 185 ? 0.6456 0.8622 0.4031 0.1287 -0.0850 -0.2179 184 ALA C C 5128 O O . ALA C 185 ? 0.6464 0.8342 0.4132 0.1141 -0.0909 -0.2220 184 ALA C O 5129 C CB . ALA C 185 ? 0.6931 0.9167 0.4042 0.1768 -0.0693 -0.2260 184 ALA C CB 5130 N N . ALA C 186 ? 0.6524 0.8826 0.4027 0.1258 -0.0943 -0.2205 185 ALA C N 5131 C CA . ALA C 186 ? 0.6631 0.8796 0.4212 0.1041 -0.1125 -0.2280 185 ALA C CA 5132 C C . ALA C 186 ? 0.6215 0.8468 0.4225 0.0806 -0.1081 -0.2146 185 ALA C C 5133 O O . ALA C 186 ? 0.6299 0.8323 0.4402 0.0614 -0.1184 -0.2208 185 ALA C O 5134 C CB . ALA C 186 ? 0.6715 0.9103 0.4200 0.1065 -0.1217 -0.2291 185 ALA C CB 5135 N N . GLU C 187 ? 0.5759 0.8335 0.4011 0.0820 -0.0925 -0.1961 186 GLU C N 5136 C CA . GLU C 187 ? 0.5361 0.8029 0.3986 0.0636 -0.0864 -0.1832 186 GLU C CA 5137 C C . GLU C 187 ? 0.5294 0.7673 0.3959 0.0578 -0.0818 -0.1847 186 GLU C C 5138 O O . GLU C 187 ? 0.5194 0.7462 0.4049 0.0383 -0.0848 -0.1835 186 GLU C O 5139 C CB . GLU C 187 ? 0.5036 0.8054 0.3844 0.0693 -0.0720 -0.1641 186 GLU C CB 5140 C CG . GLU C 187 ? 0.4736 0.7850 0.3899 0.0530 -0.0659 -0.1513 186 GLU C CG 5141 C CD . GLU C 187 ? 0.4519 0.7949 0.3828 0.0574 -0.0572 -0.1343 186 GLU C CD 5142 O OE1 . GLU C 187 ? 0.4607 0.8220 0.3892 0.0598 -0.0641 -0.1333 186 GLU C OE1 5143 O OE2 . GLU C 187 ? 0.4402 0.7875 0.3837 0.0584 -0.0448 -0.1219 186 GLU C OE2 5144 N N . GLN C 188 ? 0.5386 0.7653 0.3863 0.0756 -0.0746 -0.1871 187 GLN C N 5145 C CA . GLN C 188 ? 0.5393 0.7369 0.3865 0.0740 -0.0713 -0.1887 187 GLN C CA 5146 C C . GLN C 188 ? 0.5672 0.7234 0.4027 0.0600 -0.0866 -0.2031 187 GLN C C 5147 O O . GLN C 188 ? 0.5515 0.6913 0.4023 0.0428 -0.0863 -0.1991 187 GLN C O 5148 C CB . GLN C 188 ? 0.5572 0.7522 0.3829 0.0995 -0.0638 -0.1918 187 GLN C CB 5149 C CG . GLN C 188 ? 0.5678 0.7324 0.3897 0.1026 -0.0618 -0.1943 187 GLN C CG 5150 C CD . GLN C 188 ? 0.5321 0.7049 0.3846 0.0895 -0.0520 -0.1781 187 GLN C CD 5151 O OE1 . GLN C 188 ? 0.5008 0.7067 0.3764 0.0845 -0.0431 -0.1635 187 GLN C OE1 5152 N NE2 . GLN C 188 ? 0.5448 0.6845 0.3950 0.0845 -0.0544 -0.1805 187 GLN C NE2 5153 N N . THR C 189 ? 0.6145 0.7520 0.4205 0.0669 -0.1004 -0.2196 188 THR C N 5154 C CA . THR C 189 ? 0.6507 0.7456 0.4427 0.0521 -0.1177 -0.2337 188 THR C CA 5155 C C . THR C 189 ? 0.6315 0.7380 0.4514 0.0236 -0.1250 -0.2292 188 THR C C 5156 O O . THR C 189 ? 0.6385 0.7171 0.4625 0.0032 -0.1334 -0.2325 188 THR C O 5157 C CB . THR C 189 ? 0.7063 0.7766 0.4569 0.0671 -0.1328 -0.2538 188 THR C CB 5158 O OG1 . THR C 189 ? 0.6987 0.8043 0.4450 0.0779 -0.1322 -0.2530 188 THR C OG1 5159 C CG2 . THR C 189 ? 0.7359 0.7806 0.4565 0.0931 -0.1284 -0.2620 188 THR C CG2 5160 N N . ARG C 190 ? 0.6056 0.7543 0.4454 0.0221 -0.1216 -0.2207 189 ARG C N 5161 C CA . ARG C 190 ? 0.6018 0.7672 0.4700 -0.0020 -0.1286 -0.2168 189 ARG C CA 5162 C C . ARG C 190 ? 0.5694 0.7378 0.4688 -0.0196 -0.1174 -0.2039 189 ARG C C 5163 O O . ARG C 190 ? 0.5775 0.7386 0.4921 -0.0429 -0.1247 -0.2050 189 ARG C O 5164 C CB . ARG C 190 ? 0.5952 0.8042 0.4762 0.0032 -0.1285 -0.2108 189 ARG C CB 5165 C CG . ARG C 190 ? 0.6062 0.8337 0.5138 -0.0187 -0.1398 -0.2103 189 ARG C CG 5166 C CD . ARG C 190 ? 0.6175 0.8788 0.5266 -0.0106 -0.1468 -0.2096 189 ARG C CD 5167 N NE . ARG C 190 ? 0.5929 0.8871 0.5164 0.0021 -0.1306 -0.1935 189 ARG C NE 5168 C CZ . ARG C 190 ? 0.6008 0.9029 0.5032 0.0239 -0.1233 -0.1901 189 ARG C CZ 5169 N NH1 . ARG C 190 ? 0.6386 0.9209 0.5032 0.0388 -0.1288 -0.2022 189 ARG C NH1 5170 N NH2 . ARG C 190 ? 0.5724 0.9021 0.4909 0.0309 -0.1100 -0.1739 189 ARG C NH2 5171 N N . LEU C 191 ? 0.5290 0.7081 0.4369 -0.0090 -0.1001 -0.1917 190 LEU C N 5172 C CA . LEU C 191 ? 0.4962 0.6780 0.4299 -0.0230 -0.0887 -0.1792 190 LEU C CA 5173 C C . LEU C 191 ? 0.5112 0.6511 0.4312 -0.0270 -0.0875 -0.1817 190 LEU C C 5174 O O . LEU C 191 ? 0.5081 0.6388 0.4431 -0.0456 -0.0844 -0.1759 190 LEU C O 5175 C CB . LEU C 191 ? 0.4560 0.6686 0.4065 -0.0118 -0.0725 -0.1639 190 LEU C CB 5176 C CG . LEU C 191 ? 0.4413 0.6921 0.3992 -0.0009 -0.0707 -0.1582 190 LEU C CG 5177 C CD1 . LEU C 191 ? 0.4032 0.6757 0.3822 0.0016 -0.0560 -0.1417 190 LEU C CD1 5178 C CD2 . LEU C 191 ? 0.4495 0.7190 0.4198 -0.0120 -0.0823 -0.1623 190 LEU C CD2 5179 N N . TYR C 192 ? 0.5237 0.6393 0.4148 -0.0084 -0.0894 -0.1896 191 TYR C N 5180 C CA . TYR C 192 ? 0.5325 0.6108 0.4104 -0.0065 -0.0870 -0.1900 191 TYR C CA 5181 C C . TYR C 192 ? 0.5916 0.6231 0.4344 -0.0013 -0.1018 -0.2067 191 TYR C C 5182 O O . TYR C 192 ? 0.6106 0.6065 0.4390 0.0017 -0.1020 -0.2081 191 TYR C O 5183 C CB . TYR C 192 ? 0.4942 0.5874 0.3739 0.0139 -0.0729 -0.1810 191 TYR C CB 5184 C CG . TYR C 192 ? 0.4380 0.5734 0.3471 0.0114 -0.0601 -0.1653 191 TYR C CG 5185 C CD1 . TYR C 192 ? 0.4121 0.5512 0.3438 -0.0062 -0.0537 -0.1548 191 TYR C CD1 5186 C CD2 . TYR C 192 ? 0.4152 0.5850 0.3274 0.0268 -0.0546 -0.1610 191 TYR C CD2 5187 C CE1 . TYR C 192 ? 0.3711 0.5444 0.3268 -0.0070 -0.0433 -0.1417 191 TYR C CE1 5188 C CE2 . TYR C 192 ? 0.3738 0.5768 0.3104 0.0242 -0.0447 -0.1465 191 TYR C CE2 5189 C CZ . TYR C 192 ? 0.3522 0.5557 0.3102 0.0079 -0.0396 -0.1376 191 TYR C CZ 5190 O OH . TYR C 192 ? 0.3157 0.5480 0.2950 0.0068 -0.0310 -0.1245 191 TYR C OH 5191 N N . GLN C 193 ? 0.6255 0.6545 0.4527 0.0006 -0.1151 -0.2196 192 GLN C N 5192 C CA . GLN C 193 ? 0.6882 0.6708 0.4777 0.0076 -0.1314 -0.2377 192 GLN C CA 5193 C C . GLN C 193 ? 0.7076 0.6797 0.4704 0.0397 -0.1265 -0.2439 192 GLN C C 5194 O O . GLN C 193 ? 0.7341 0.7030 0.4705 0.0582 -0.1334 -0.2569 192 GLN C O 5195 C CB . GLN C 193 ? 0.7235 0.6575 0.5062 -0.0143 -0.1414 -0.2404 192 GLN C CB 5196 C CG . GLN C 193 ? 0.7896 0.6726 0.5344 -0.0139 -0.1631 -0.2598 192 GLN C CG 5197 C CD . GLN C 193 ? 0.8041 0.6988 0.5503 -0.0274 -0.1783 -0.2683 192 GLN C CD 5198 O OE1 . GLN C 193 ? 0.7658 0.7067 0.5439 -0.0391 -0.1729 -0.2591 192 GLN C OE1 5199 N NE2 . GLN C 193 ? 0.8674 0.7182 0.5777 -0.0252 -0.1987 -0.2865 192 GLN C NE2 5200 N N . ASN C 194 ? 0.6926 0.6609 0.4623 0.0468 -0.1148 -0.2346 193 ASN C N 5201 C CA . ASN C 194 ? 0.7128 0.6705 0.4607 0.0766 -0.1104 -0.2398 193 ASN C CA 5202 C C . ASN C 194 ? 0.6882 0.6966 0.4437 0.0988 -0.0967 -0.2342 193 ASN C C 5203 O O . ASN C 194 ? 0.6331 0.6827 0.4191 0.0915 -0.0844 -0.2184 193 ASN C O 5204 C CB . ASN C 194 ? 0.7013 0.6401 0.4566 0.0751 -0.1039 -0.2306 193 ASN C CB 5205 C CG . ASN C 194 ? 0.7220 0.6159 0.4737 0.0488 -0.1147 -0.2314 193 ASN C CG 5206 O OD1 . ASN C 194 ? 0.7686 0.6260 0.4981 0.0402 -0.1309 -0.2445 193 ASN C OD1 5207 N ND2 . ASN C 194 ? 0.6950 0.5909 0.4674 0.0346 -0.1060 -0.2168 193 ASN C ND2 5208 N N . PRO C 195 ? 0.7243 0.7285 0.4504 0.1262 -0.0987 -0.2468 194 PRO C N 5209 C CA . PRO C 195 ? 0.7064 0.7598 0.4379 0.1460 -0.0851 -0.2405 194 PRO C CA 5210 C C . PRO C 195 ? 0.6825 0.7622 0.4325 0.1597 -0.0683 -0.2268 194 PRO C C 5211 O O . PRO C 195 ? 0.6518 0.7783 0.4197 0.1649 -0.0552 -0.2141 194 PRO C O 5212 C CB . PRO C 195 ? 0.7564 0.7926 0.4464 0.1705 -0.0934 -0.2602 194 PRO C CB 5213 C CG . PRO C 195 ? 0.8034 0.7798 0.4672 0.1733 -0.1072 -0.2750 194 PRO C CG 5214 C CD . PRO C 195 ? 0.7882 0.7418 0.4738 0.1415 -0.1126 -0.2667 194 PRO C CD 5215 N N . THR C 196 ? 0.7029 0.7526 0.4490 0.1645 -0.0699 -0.2284 195 THR C N 5216 C CA . THR C 196 ? 0.6821 0.7555 0.4442 0.1797 -0.0567 -0.2172 195 THR C CA 5217 C C . THR C 196 ? 0.6617 0.7205 0.4456 0.1609 -0.0558 -0.2053 195 THR C C 5218 O O . THR C 196 ? 0.6944 0.7068 0.4635 0.1582 -0.0656 -0.2122 195 THR C O 5219 C CB . THR C 196 ? 0.7274 0.7822 0.4614 0.2113 -0.0588 -0.2308 195 THR C CB 5220 O OG1 . THR C 196 ? 0.7723 0.8248 0.4759 0.2274 -0.0636 -0.2465 195 THR C OG1 5221 C CG2 . THR C 196 ? 0.7016 0.7990 0.4555 0.2305 -0.0434 -0.2188 195 THR C CG2 5222 N N . THR C 197 ? 0.6103 0.7060 0.4265 0.1488 -0.0447 -0.1872 196 THR C N 5223 C CA . THR C 197 ? 0.5886 0.6701 0.4234 0.1276 -0.0445 -0.1764 196 THR C CA 5224 C C . THR C 197 ? 0.5613 0.6688 0.4193 0.1324 -0.0339 -0.1610 196 THR C C 5225 O O . THR C 197 ? 0.5568 0.7028 0.4239 0.1483 -0.0250 -0.1553 196 THR C O 5226 C CB . THR C 197 ? 0.5630 0.6535 0.4140 0.1012 -0.0448 -0.1704 196 THR C CB 5227 O OG1 . THR C 197 ? 0.5239 0.6625 0.3958 0.1022 -0.0342 -0.1585 196 THR C OG1 5228 C CG2 . THR C 197 ? 0.5926 0.6603 0.4234 0.0944 -0.0572 -0.1854 196 THR C CG2 5229 N N . TYR C 198 ? 0.5529 0.6390 0.4197 0.1173 -0.0354 -0.1537 197 TYR C N 5230 C CA . TYR C 198 ? 0.5255 0.6275 0.4117 0.1196 -0.0289 -0.1400 197 TYR C CA 5231 C C . TYR C 198 ? 0.4995 0.5855 0.3971 0.0957 -0.0290 -0.1304 197 TYR C C 5232 O O . TYR C 198 ? 0.5168 0.5728 0.4047 0.0794 -0.0345 -0.1353 197 TYR C O 5233 C CB . TYR C 198 ? 0.5515 0.6326 0.4240 0.1400 -0.0336 -0.1457 197 TYR C CB 5234 C CG . TYR C 198 ? 0.5915 0.6145 0.4404 0.1334 -0.0455 -0.1547 197 TYR C CG 5235 C CD1 . TYR C 198 ? 0.6376 0.6268 0.4588 0.1363 -0.0551 -0.1708 197 TYR C CD1 5236 C CD2 . TYR C 198 ? 0.5932 0.5923 0.4451 0.1234 -0.0480 -0.1466 197 TYR C CD2 5237 C CE1 . TYR C 198 ? 0.6765 0.6094 0.4752 0.1279 -0.0669 -0.1776 197 TYR C CE1 5238 C CE2 . TYR C 198 ? 0.6304 0.5744 0.4585 0.1163 -0.0587 -0.1531 197 TYR C CE2 5239 C CZ . TYR C 198 ? 0.6716 0.5827 0.4740 0.1177 -0.0680 -0.1680 197 TYR C CZ 5240 O OH . TYR C 198 ? 0.7145 0.5684 0.4926 0.1082 -0.0793 -0.1730 197 TYR C OH 5241 N N . ILE C 199 ? 0.4601 0.5669 0.3777 0.0938 -0.0228 -0.1166 198 ILE C N 5242 C CA . ILE C 199 ? 0.4396 0.5287 0.3639 0.0758 -0.0228 -0.1078 198 ILE C CA 5243 C C . ILE C 199 ? 0.4324 0.5191 0.3608 0.0855 -0.0240 -0.1008 198 ILE C C 5244 O O . ILE C 199 ? 0.4061 0.5274 0.3534 0.0914 -0.0190 -0.0912 198 ILE C O 5245 C CB . ILE C 199 ? 0.3989 0.5155 0.3441 0.0602 -0.0154 -0.0970 198 ILE C CB 5246 C CG1 . ILE C 199 ? 0.4001 0.5250 0.3440 0.0528 -0.0152 -0.1035 198 ILE C CG1 5247 C CG2 . ILE C 199 ? 0.3861 0.4821 0.3342 0.0431 -0.0148 -0.0896 198 ILE C CG2 5248 C CD1 . ILE C 199 ? 0.3651 0.5207 0.3292 0.0428 -0.0085 -0.0935 198 ILE C CD1 5249 N N . SER C 200 ? 0.4583 0.5038 0.3690 0.0864 -0.0317 -0.1050 199 SER C N 5250 C CA . SER C 200 ? 0.4605 0.4988 0.3740 0.0928 -0.0349 -0.0978 199 SER C CA 5251 C C . SER C 200 ? 0.4412 0.4676 0.3598 0.0726 -0.0334 -0.0871 199 SER C C 5252 O O . SER C 200 ? 0.4428 0.4413 0.3496 0.0558 -0.0336 -0.0888 199 SER C O 5253 C CB . SER C 200 ? 0.5077 0.5035 0.3963 0.1051 -0.0453 -0.1070 199 SER C CB 5254 O OG . SER C 200 ? 0.5466 0.5530 0.4286 0.1278 -0.0469 -0.1176 199 SER C OG 5255 N N . VAL C 201 ? 0.4111 0.4591 0.3465 0.0743 -0.0320 -0.0760 200 VAL C N 5256 C CA . VAL C 201 ? 0.4037 0.4366 0.3394 0.0588 -0.0321 -0.0669 200 VAL C CA 5257 C C . VAL C 201 ? 0.4119 0.4381 0.3478 0.0682 -0.0398 -0.0612 200 VAL C C 5258 O O . VAL C 201 ? 0.3981 0.4552 0.3504 0.0824 -0.0410 -0.0584 200 VAL C O 5259 C CB . VAL C 201 ? 0.3697 0.4331 0.3252 0.0472 -0.0242 -0.0581 200 VAL C CB 5260 C CG1 . VAL C 201 ? 0.3718 0.4129 0.3212 0.0319 -0.0241 -0.0512 200 VAL C CG1 5261 C CG2 . VAL C 201 ? 0.3641 0.4410 0.3225 0.0413 -0.0179 -0.0636 200 VAL C CG2 5262 N N . GLY C 202 ? 0.4298 0.4171 0.3477 0.0599 -0.0449 -0.0591 201 GLY C N 5263 C CA . GLY C 202 ? 0.4444 0.4203 0.3591 0.0677 -0.0543 -0.0537 201 GLY C CA 5264 C C . GLY C 202 ? 0.4518 0.4014 0.3547 0.0520 -0.0558 -0.0463 201 GLY C C 5265 O O . GLY C 202 ? 0.4705 0.3923 0.3559 0.0379 -0.0515 -0.0478 201 GLY C O 5266 N N . THR C 203 ? 0.4398 0.4002 0.3526 0.0543 -0.0617 -0.0379 202 THR C N 5267 C CA . THR C 203 ? 0.4544 0.3836 0.3496 0.0445 -0.0669 -0.0319 202 THR C CA 5268 C C . THR C 203 ? 0.4729 0.3969 0.3675 0.0588 -0.0811 -0.0292 202 THR C C 5269 O O . THR C 203 ? 0.4858 0.4213 0.3874 0.0758 -0.0853 -0.0339 202 THR C O 5270 C CB . THR C 203 ? 0.4314 0.3777 0.3384 0.0315 -0.0621 -0.0243 202 THR C CB 5271 O OG1 . THR C 203 ? 0.4081 0.3909 0.3415 0.0380 -0.0673 -0.0182 202 THR C OG1 5272 C CG2 . THR C 203 ? 0.4133 0.3745 0.3274 0.0216 -0.0486 -0.0272 202 THR C CG2 5273 N N . SER C 204 ? 0.4907 0.3974 0.3758 0.0536 -0.0893 -0.0222 203 SER C N 5274 C CA . SER C 204 ? 0.5083 0.4165 0.3976 0.0668 -0.1047 -0.0186 203 SER C CA 5275 C C . SER C 204 ? 0.4793 0.4430 0.4079 0.0746 -0.1067 -0.0140 203 SER C C 5276 O O . SER C 204 ? 0.4911 0.4700 0.4319 0.0904 -0.1168 -0.0132 203 SER C O 5277 C CB . SER C 204 ? 0.5291 0.4028 0.3955 0.0583 -0.1143 -0.0124 203 SER C CB 5278 O OG . SER C 204 ? 0.5208 0.4085 0.3963 0.0443 -0.1100 -0.0069 203 SER C OG 5279 N N . THR C 205 ? 0.4537 0.4478 0.4020 0.0637 -0.0970 -0.0104 204 THR C N 5280 C CA . THR C 205 ? 0.4314 0.4789 0.4167 0.0676 -0.0971 -0.0041 204 THR C CA 5281 C C . THR C 205 ? 0.4182 0.4999 0.4200 0.0725 -0.0835 -0.0081 204 THR C C 5282 O O . THR C 205 ? 0.4148 0.5386 0.4422 0.0838 -0.0830 -0.0058 204 THR C O 5283 C CB . THR C 205 ? 0.4156 0.4723 0.4110 0.0510 -0.0988 0.0053 204 THR C CB 5284 O OG1 . THR C 205 ? 0.4060 0.4494 0.3895 0.0382 -0.0867 0.0028 204 THR C OG1 5285 C CG2 . THR C 205 ? 0.4420 0.4678 0.4212 0.0463 -0.1140 0.0096 204 THR C CG2 5286 N N . LEU C 206 ? 0.4145 0.4801 0.4020 0.0638 -0.0726 -0.0137 205 LEU C N 5287 C CA . LEU C 206 ? 0.3936 0.4876 0.3930 0.0668 -0.0608 -0.0179 205 LEU C CA 5288 C C . LEU C 206 ? 0.4131 0.5004 0.4024 0.0838 -0.0603 -0.0288 205 LEU C C 5289 O O . LEU C 206 ? 0.4364 0.4821 0.4004 0.0864 -0.0657 -0.0351 205 LEU C O 5290 C CB . LEU C 206 ? 0.3939 0.4731 0.3824 0.0510 -0.0514 -0.0197 205 LEU C CB 5291 C CG . LEU C 206 ? 0.3783 0.4874 0.3794 0.0506 -0.0403 -0.0221 205 LEU C CG 5292 C CD1 . LEU C 206 ? 0.3569 0.5116 0.3863 0.0516 -0.0388 -0.0121 205 LEU C CD1 5293 C CD2 . LEU C 206 ? 0.3745 0.4657 0.3644 0.0356 -0.0332 -0.0240 205 LEU C CD2 5294 N N . ASN C 207 ? 0.4013 0.5276 0.4080 0.0957 -0.0542 -0.0308 206 ASN C N 5295 C CA . ASN C 207 ? 0.4157 0.5387 0.4123 0.1145 -0.0535 -0.0425 206 ASN C CA 5296 C C . ASN C 207 ? 0.4104 0.5709 0.4193 0.1188 -0.0422 -0.0449 206 ASN C C 5297 O O . ASN C 207 ? 0.4005 0.6031 0.4289 0.1327 -0.0391 -0.0423 206 ASN C O 5298 C CB . ASN C 207 ? 0.4268 0.5614 0.4314 0.1353 -0.0624 -0.0422 206 ASN C CB 5299 C CG . ASN C 207 ? 0.4450 0.5746 0.4369 0.1582 -0.0620 -0.0554 206 ASN C CG 5300 O OD1 . ASN C 207 ? 0.4481 0.5506 0.4182 0.1562 -0.0588 -0.0656 206 ASN C OD1 5301 N ND2 . ASN C 207 ? 0.4502 0.6071 0.4563 0.1805 -0.0659 -0.0554 206 ASN C ND2 5302 N N . GLN C 208 ? 0.4299 0.5761 0.4271 0.1068 -0.0360 -0.0498 207 GLN C N 5303 C CA . GLN C 208 ? 0.4331 0.6135 0.4416 0.1054 -0.0259 -0.0493 207 GLN C CA 5304 C C . GLN C 208 ? 0.4674 0.6346 0.4568 0.1145 -0.0238 -0.0637 207 GLN C C 5305 O O . GLN C 208 ? 0.4921 0.6167 0.4590 0.1112 -0.0289 -0.0724 207 GLN C O 5306 C CB . GLN C 208 ? 0.4149 0.5928 0.4278 0.0836 -0.0220 -0.0420 207 GLN C CB 5307 C CG . GLN C 208 ? 0.4098 0.6162 0.4310 0.0801 -0.0130 -0.0411 207 GLN C CG 5308 C CD . GLN C 208 ? 0.4027 0.5993 0.4245 0.0609 -0.0105 -0.0363 207 GLN C CD 5309 O OE1 . GLN C 208 ? 0.3965 0.5784 0.4073 0.0543 -0.0079 -0.0435 207 GLN C OE1 5310 N NE2 . GLN C 208 ? 0.3835 0.5877 0.4181 0.0522 -0.0122 -0.0244 207 GLN C NE2 5311 N N . ARG C 209 ? 0.4817 0.6844 0.4787 0.1256 -0.0168 -0.0658 208 ARG C N 5312 C CA . ARG C 209 ? 0.5121 0.7041 0.4896 0.1334 -0.0153 -0.0798 208 ARG C CA 5313 C C . ARG C 209 ? 0.5041 0.7334 0.4912 0.1310 -0.0061 -0.0767 208 ARG C C 5314 O O . ARG C 209 ? 0.5233 0.7938 0.5238 0.1433 0.0001 -0.0715 208 ARG C O 5315 C CB . ARG C 209 ? 0.5555 0.7422 0.5203 0.1592 -0.0192 -0.0908 208 ARG C CB 5316 C CG . ARG C 209 ? 0.5989 0.7713 0.5398 0.1693 -0.0195 -0.1068 208 ARG C CG 5317 C CD . ARG C 209 ? 0.6579 0.7812 0.5710 0.1818 -0.0304 -0.1208 208 ARG C CD 5318 N NE . ARG C 209 ? 0.7033 0.8148 0.5922 0.1964 -0.0320 -0.1372 208 ARG C NE 5319 C CZ . ARG C 209 ? 0.7481 0.8092 0.6065 0.2039 -0.0429 -0.1519 208 ARG C CZ 5320 N NH1 . ARG C 209 ? 0.7715 0.7881 0.6188 0.1979 -0.0526 -0.1516 208 ARG C NH1 5321 N NH2 . ARG C 209 ? 0.7769 0.8293 0.6129 0.2175 -0.0449 -0.1669 208 ARG C NH2 5322 N N . LEU C 210 ? 0.4863 0.7022 0.4667 0.1153 -0.0053 -0.0792 209 LEU C N 5323 C CA . LEU C 210 ? 0.4562 0.7024 0.4435 0.1115 0.0015 -0.0759 209 LEU C CA 5324 C C . LEU C 210 ? 0.4761 0.7144 0.4423 0.1211 0.0002 -0.0909 209 LEU C C 5325 O O . LEU C 210 ? 0.4995 0.6995 0.4466 0.1187 -0.0069 -0.1031 209 LEU C O 5326 C CB . LEU C 210 ? 0.4381 0.6768 0.4325 0.0895 0.0021 -0.0692 209 LEU C CB 5327 C CG . LEU C 210 ? 0.4234 0.6589 0.4324 0.0775 0.0014 -0.0565 209 LEU C CG 5328 C CD1 . LEU C 210 ? 0.4088 0.6305 0.4183 0.0591 0.0020 -0.0545 209 LEU C CD1 5329 C CD2 . LEU C 210 ? 0.4064 0.6808 0.4361 0.0808 0.0058 -0.0424 209 LEU C CD2 5330 N N . VAL C 211 ? 0.4677 0.7409 0.4358 0.1311 0.0067 -0.0896 210 VAL C N 5331 C CA . VAL C 211 ? 0.4902 0.7580 0.4361 0.1408 0.0050 -0.1039 210 VAL C CA 5332 C C . VAL C 211 ? 0.4721 0.7655 0.4235 0.1320 0.0095 -0.0978 210 VAL C C 5333 O O . VAL C 211 ? 0.4446 0.7729 0.4140 0.1299 0.0172 -0.0828 210 VAL C O 5334 C CB . VAL C 211 ? 0.5169 0.7993 0.4511 0.1680 0.0080 -0.1115 210 VAL C CB 5335 C CG1 . VAL C 211 ? 0.5511 0.8201 0.4565 0.1784 0.0041 -0.1285 210 VAL C CG1 5336 C CG2 . VAL C 211 ? 0.5306 0.7891 0.4612 0.1788 0.0026 -0.1164 210 VAL C CG2 5337 N N . PRO C 212 ? 0.4815 0.7565 0.4176 0.1256 0.0035 -0.1086 211 PRO C N 5338 C CA . PRO C 212 ? 0.4647 0.7621 0.4065 0.1170 0.0059 -0.1026 211 PRO C CA 5339 C C . PRO C 212 ? 0.4653 0.7961 0.3987 0.1339 0.0125 -0.1011 211 PRO C C 5340 O O . PRO C 212 ? 0.4907 0.8193 0.4056 0.1527 0.0126 -0.1121 211 PRO C O 5341 C CB . PRO C 212 ? 0.4869 0.7558 0.4148 0.1069 -0.0041 -0.1161 211 PRO C CB 5342 C CG . PRO C 212 ? 0.5056 0.7347 0.4244 0.1045 -0.0109 -0.1255 211 PRO C CG 5343 C CD . PRO C 212 ? 0.5134 0.7463 0.4278 0.1240 -0.0070 -0.1257 211 PRO C CD 5344 N N . LYS C 213 ? 0.4405 0.8003 0.3858 0.1274 0.0179 -0.0875 212 LYS C N 5345 C CA . LYS C 213 ? 0.4401 0.8370 0.3821 0.1398 0.0268 -0.0796 212 LYS C CA 5346 C C . LYS C 213 ? 0.4548 0.8556 0.3828 0.1373 0.0230 -0.0830 212 LYS C C 5347 O O . LYS C 213 ? 0.4439 0.8508 0.3842 0.1232 0.0218 -0.0726 212 LYS C O 5348 C CB . LYS C 213 ? 0.4171 0.8422 0.3847 0.1317 0.0350 -0.0576 212 LYS C CB 5349 C CG . LYS C 213 ? 0.4174 0.8532 0.3994 0.1384 0.0401 -0.0518 212 LYS C CG 5350 C CD . LYS C 213 ? 0.3988 0.8690 0.4040 0.1313 0.0480 -0.0295 212 LYS C CD 5351 C CE . LYS C 213 ? 0.3884 0.8454 0.4080 0.1096 0.0432 -0.0187 212 LYS C CE 5352 N NZ . LYS C 213 ? 0.3846 0.8601 0.4282 0.1007 0.0465 0.0002 212 LYS C NZ 5353 N N . ILE C 214 ? 0.4735 0.8688 0.3743 0.1518 0.0198 -0.0982 213 ILE C N 5354 C CA . ILE C 214 ? 0.4816 0.8820 0.3662 0.1513 0.0149 -0.1018 213 ILE C CA 5355 C C . ILE C 214 ? 0.4764 0.9162 0.3582 0.1598 0.0260 -0.0871 213 ILE C C 5356 O O . ILE C 214 ? 0.4894 0.9498 0.3628 0.1765 0.0360 -0.0855 213 ILE C O 5357 C CB . ILE C 214 ? 0.5163 0.8909 0.3697 0.1619 0.0047 -0.1247 213 ILE C CB 5358 C CG1 . ILE C 214 ? 0.5141 0.8498 0.3725 0.1464 -0.0078 -0.1358 213 ILE C CG1 5359 C CG2 . ILE C 214 ? 0.5374 0.9229 0.3707 0.1653 0.0001 -0.1278 213 ILE C CG2 5360 C CD1 . ILE C 214 ? 0.5550 0.8559 0.3852 0.1563 -0.0179 -0.1577 213 ILE C CD1 5361 N N . ALA C 215 ? 0.4570 0.9072 0.3463 0.1478 0.0241 -0.0755 214 ALA C N 5362 C CA . ALA C 215 ? 0.4497 0.9318 0.3330 0.1525 0.0322 -0.0605 214 ALA C CA 5363 C C . ALA C 215 ? 0.4495 0.9278 0.3268 0.1438 0.0224 -0.0591 214 ALA C C 5364 O O . ALA C 215 ? 0.4321 0.8887 0.3182 0.1320 0.0111 -0.0667 214 ALA C O 5365 C CB . ALA C 215 ? 0.4224 0.9271 0.3318 0.1450 0.0430 -0.0381 214 ALA C CB 5366 N N . THR C 216 ? 0.4567 0.9580 0.3185 0.1504 0.0269 -0.0491 215 THR C N 5367 C CA . THR C 216 ? 0.4543 0.9554 0.3097 0.1443 0.0178 -0.0450 215 THR C CA 5368 C C . THR C 216 ? 0.4247 0.9380 0.3033 0.1318 0.0230 -0.0213 215 THR C C 5369 O O . THR C 216 ? 0.4143 0.9500 0.2948 0.1342 0.0352 -0.0048 215 THR C O 5370 C CB . THR C 216 ? 0.4908 1.0064 0.3111 0.1592 0.0185 -0.0469 215 THR C CB 5371 O OG1 . THR C 216 ? 0.5153 1.0220 0.3116 0.1748 0.0182 -0.0672 215 THR C OG1 5372 C CG2 . THR C 216 ? 0.5046 1.0126 0.3149 0.1544 0.0036 -0.0496 215 THR C CG2 5373 N N . ARG C 217 ? 0.4007 0.8994 0.2973 0.1185 0.0137 -0.0196 216 ARG C N 5374 C CA . ARG C 217 ? 0.3762 0.8790 0.2935 0.1070 0.0166 0.0007 216 ARG C CA 5375 C C . ARG C 217 ? 0.3740 0.8738 0.2892 0.1029 0.0065 0.0064 216 ARG C C 5376 O O . ARG C 217 ? 0.3850 0.8773 0.2921 0.1052 -0.0044 -0.0073 216 ARG C O 5377 C CB . ARG C 217 ? 0.3451 0.8312 0.2889 0.0961 0.0166 -0.0011 216 ARG C CB 5378 C CG . ARG C 217 ? 0.3427 0.8274 0.2881 0.1014 0.0235 -0.0098 216 ARG C CG 5379 C CD . ARG C 217 ? 0.3151 0.7783 0.2813 0.0913 0.0210 -0.0149 216 ARG C CD 5380 N NE . ARG C 217 ? 0.3185 0.7735 0.2796 0.0987 0.0231 -0.0289 216 ARG C NE 5381 C CZ . ARG C 217 ? 0.3280 0.7607 0.2820 0.0992 0.0156 -0.0476 216 ARG C CZ 5382 N NH1 . ARG C 217 ? 0.3239 0.7443 0.2782 0.0915 0.0059 -0.0551 216 ARG C NH1 5383 N NH2 . ARG C 217 ? 0.3435 0.7663 0.2906 0.1072 0.0173 -0.0586 216 ARG C NH2 5384 N N . SER C 218 ? 0.3678 0.8727 0.2906 0.0966 0.0091 0.0271 217 SER C N 5385 C CA . SER C 218 ? 0.3709 0.8693 0.2947 0.0931 -0.0010 0.0341 217 SER C CA 5386 C C . SER C 218 ? 0.3571 0.8377 0.3024 0.0862 -0.0095 0.0224 217 SER C C 5387 O O . SER C 218 ? 0.3267 0.7973 0.2895 0.0798 -0.0055 0.0182 217 SER C O 5388 C CB . SER C 218 ? 0.3707 0.8716 0.2990 0.0864 0.0031 0.0589 217 SER C CB 5389 O OG . SER C 218 ? 0.3865 0.9073 0.3008 0.0897 0.0144 0.0717 217 SER C OG 5390 N N . LYS C 219 ? 0.3732 0.8518 0.3167 0.0882 -0.0214 0.0176 218 LYS C N 5391 C CA . LYS C 219 ? 0.3596 0.8271 0.3246 0.0824 -0.0287 0.0090 218 LYS C CA 5392 C C . LYS C 219 ? 0.3402 0.7971 0.3214 0.0761 -0.0259 0.0237 218 LYS C C 5393 O O . LYS C 219 ? 0.3490 0.8061 0.3231 0.0777 -0.0277 0.0398 218 LYS C O 5394 C CB . LYS C 219 ? 0.3803 0.8539 0.3412 0.0873 -0.0426 0.0029 218 LYS C CB 5395 C CG . LYS C 219 ? 0.3999 0.8788 0.3490 0.0909 -0.0497 -0.0158 218 LYS C CG 5396 C CD . LYS C 219 ? 0.4174 0.9026 0.3741 0.0920 -0.0651 -0.0229 218 LYS C CD 5397 C CE . LYS C 219 ? 0.4500 0.9393 0.3927 0.0944 -0.0754 -0.0409 218 LYS C CE 5398 N NZ . LYS C 219 ? 0.4652 0.9655 0.4141 0.0961 -0.0923 -0.0458 218 LYS C NZ 5399 N N . VAL C 220 ? 0.3152 0.7601 0.3150 0.0689 -0.0222 0.0181 219 VAL C N 5400 C CA . VAL C 220 ? 0.3047 0.7354 0.3190 0.0637 -0.0220 0.0274 219 VAL C CA 5401 C C . VAL C 220 ? 0.2947 0.7208 0.3257 0.0621 -0.0266 0.0137 219 VAL C C 5402 O O . VAL C 220 ? 0.2752 0.7023 0.3115 0.0588 -0.0252 -0.0008 219 VAL C O 5403 C CB . VAL C 220 ? 0.2998 0.7206 0.3199 0.0564 -0.0128 0.0344 219 VAL C CB 5404 C CG1 . VAL C 220 ? 0.2936 0.6952 0.3251 0.0514 -0.0144 0.0421 219 VAL C CG1 5405 C CG2 . VAL C 220 ? 0.3123 0.7443 0.3197 0.0571 -0.0071 0.0490 219 VAL C CG2 5406 N N . ASN C 221 ? 0.3065 0.7279 0.3451 0.0648 -0.0321 0.0189 220 ASN C N 5407 C CA . ASN C 221 ? 0.3088 0.7341 0.3643 0.0657 -0.0367 0.0072 220 ASN C CA 5408 C C . ASN C 221 ? 0.3112 0.7541 0.3676 0.0663 -0.0425 -0.0072 220 ASN C C 5409 O O . ASN C 221 ? 0.2979 0.7441 0.3693 0.0609 -0.0422 -0.0196 220 ASN C O 5410 C CB . ASN C 221 ? 0.2994 0.7111 0.3690 0.0582 -0.0291 0.0019 220 ASN C CB 5411 C CG . ASN C 221 ? 0.3033 0.6950 0.3724 0.0581 -0.0264 0.0142 220 ASN C CG 5412 O OD1 . ASN C 221 ? 0.3284 0.7154 0.3903 0.0638 -0.0317 0.0260 220 ASN C OD1 5413 N ND2 . ASN C 221 ? 0.2980 0.6749 0.3728 0.0513 -0.0195 0.0114 220 ASN C ND2 5414 N N . GLY C 222 ? 0.3329 0.7857 0.3714 0.0718 -0.0478 -0.0052 221 GLY C N 5415 C CA . GLY C 222 ? 0.3481 0.8144 0.3819 0.0728 -0.0555 -0.0192 221 GLY C CA 5416 C C . GLY C 222 ? 0.3516 0.8129 0.3780 0.0673 -0.0507 -0.0310 221 GLY C C 5417 O O . GLY C 222 ? 0.3635 0.8314 0.3820 0.0679 -0.0585 -0.0432 221 GLY C O 5418 N N . GLN C 223 ? 0.3453 0.7934 0.3730 0.0626 -0.0396 -0.0279 222 GLN C N 5419 C CA . GLN C 223 ? 0.3524 0.7926 0.3723 0.0593 -0.0352 -0.0387 222 GLN C CA 5420 C C . GLN C 223 ? 0.3528 0.7942 0.3534 0.0658 -0.0281 -0.0313 222 GLN C C 5421 O O . GLN C 223 ? 0.3432 0.7843 0.3452 0.0661 -0.0215 -0.0162 222 GLN C O 5422 C CB . GLN C 223 ? 0.3442 0.7691 0.3798 0.0501 -0.0280 -0.0415 222 GLN C CB 5423 C CG . GLN C 223 ? 0.3489 0.7746 0.4055 0.0430 -0.0313 -0.0472 222 GLN C CG 5424 C CD . GLN C 223 ? 0.3829 0.8184 0.4412 0.0402 -0.0416 -0.0610 222 GLN C CD 5425 O OE1 . GLN C 223 ? 0.4050 0.8329 0.4517 0.0376 -0.0439 -0.0718 222 GLN C OE1 5426 N NE2 . GLN C 223 ? 0.3954 0.8474 0.4679 0.0412 -0.0490 -0.0609 222 GLN C NE2 5427 N N . SER C 224 ? 0.3659 0.8085 0.3485 0.0708 -0.0296 -0.0421 223 SER C N 5428 C CA . SER C 224 ? 0.3729 0.8189 0.3388 0.0781 -0.0206 -0.0373 223 SER C CA 5429 C C . SER C 224 ? 0.3531 0.7856 0.3247 0.0750 -0.0136 -0.0437 223 SER C C 5430 O O . SER C 224 ? 0.3613 0.7987 0.3253 0.0810 -0.0051 -0.0388 223 SER C O 5431 C CB . SER C 224 ? 0.4042 0.8588 0.3428 0.0890 -0.0251 -0.0452 223 SER C CB 5432 O OG . SER C 224 ? 0.4212 0.8909 0.3487 0.0947 -0.0256 -0.0312 223 SER C OG 5433 N N . GLY C 225 ? 0.3304 0.7474 0.3155 0.0659 -0.0173 -0.0539 224 GLY C N 5434 C CA . GLY C 225 ? 0.3115 0.7115 0.3008 0.0622 -0.0123 -0.0595 224 GLY C CA 5435 C C . GLY C 225 ? 0.2869 0.6841 0.2925 0.0568 -0.0046 -0.0456 224 GLY C C 5436 O O . GLY C 225 ? 0.2780 0.6831 0.2920 0.0548 -0.0042 -0.0331 224 GLY C O 5437 N N . ARG C 226 ? 0.2741 0.6576 0.2823 0.0550 0.0000 -0.0479 225 ARG C N 5438 C CA . ARG C 226 ? 0.2549 0.6337 0.2762 0.0500 0.0060 -0.0356 225 ARG C CA 5439 C C . ARG C 226 ? 0.2510 0.6066 0.2781 0.0429 0.0065 -0.0424 225 ARG C C 5440 O O . ARG C 226 ? 0.2543 0.5979 0.2723 0.0453 0.0050 -0.0541 225 ARG C O 5441 C CB . ARG C 226 ? 0.2564 0.6500 0.2740 0.0574 0.0126 -0.0249 225 ARG C CB 5442 C CG . ARG C 226 ? 0.2588 0.6753 0.2703 0.0625 0.0141 -0.0134 225 ARG C CG 5443 C CD . ARG C 226 ? 0.2488 0.6641 0.2711 0.0546 0.0121 0.0000 225 ARG C CD 5444 N NE . ARG C 226 ? 0.2672 0.7010 0.2822 0.0583 0.0133 0.0138 225 ARG C NE 5445 C CZ . ARG C 226 ? 0.2765 0.7175 0.2813 0.0624 0.0081 0.0134 225 ARG C CZ 5446 N NH1 . ARG C 226 ? 0.2748 0.7094 0.2783 0.0631 0.0007 -0.0007 225 ARG C NH1 5447 N NH2 . ARG C 226 ? 0.2871 0.7427 0.2832 0.0650 0.0099 0.0284 225 ARG C NH2 5448 N N . MET C 227 ? 0.2541 0.6005 0.2936 0.0348 0.0079 -0.0352 226 MET C N 5449 C CA . MET C 227 ? 0.2648 0.5887 0.3074 0.0283 0.0093 -0.0387 226 MET C CA 5450 C C . MET C 227 ? 0.2456 0.5689 0.2923 0.0292 0.0127 -0.0268 226 MET C C 5451 O O . MET C 227 ? 0.2382 0.5701 0.2912 0.0278 0.0134 -0.0144 226 MET C O 5452 C CB . MET C 227 ? 0.2745 0.5882 0.3260 0.0189 0.0087 -0.0400 226 MET C CB 5453 C CG . MET C 227 ? 0.3040 0.6206 0.3562 0.0152 0.0047 -0.0514 226 MET C CG 5454 S SD . MET C 227 ? 0.3511 0.6455 0.3942 0.0091 0.0024 -0.0659 226 MET C SD 5455 C CE . MET C 227 ? 0.3525 0.6588 0.4004 0.0032 -0.0044 -0.0760 226 MET C CE 5456 N N . GLU C 228 ? 0.2397 0.5521 0.2826 0.0313 0.0135 -0.0304 227 GLU C N 5457 C CA . GLU C 228 ? 0.2364 0.5485 0.2856 0.0310 0.0150 -0.0199 227 GLU C CA 5458 C C . GLU C 228 ? 0.2264 0.5105 0.2750 0.0240 0.0134 -0.0228 227 GLU C C 5459 O O . GLU C 228 ? 0.2349 0.5024 0.2751 0.0252 0.0121 -0.0330 227 GLU C O 5460 C CB . GLU C 228 ? 0.2538 0.5822 0.3005 0.0420 0.0172 -0.0195 227 GLU C CB 5461 C CG . GLU C 228 ? 0.2567 0.5901 0.3138 0.0412 0.0178 -0.0081 227 GLU C CG 5462 C CD . GLU C 228 ? 0.2629 0.6247 0.3228 0.0526 0.0219 -0.0041 227 GLU C CD 5463 O OE1 . GLU C 228 ? 0.2736 0.6375 0.3229 0.0644 0.0231 -0.0155 227 GLU C OE1 5464 O OE2 . GLU C 228 ? 0.2685 0.6504 0.3412 0.0496 0.0237 0.0106 227 GLU C OE2 5465 N N . PHE C 229 ? 0.2118 0.4881 0.2665 0.0171 0.0128 -0.0136 228 PHE C N 5466 C CA . PHE C 229 ? 0.2161 0.4651 0.2671 0.0107 0.0114 -0.0156 228 PHE C CA 5467 C C . PHE C 229 ? 0.2101 0.4522 0.2627 0.0111 0.0084 -0.0089 228 PHE C C 5468 O O . PHE C 229 ? 0.2026 0.4621 0.2642 0.0126 0.0071 0.0015 228 PHE C O 5469 C CB . PHE C 229 ? 0.2167 0.4556 0.2689 0.0039 0.0122 -0.0135 228 PHE C CB 5470 C CG . PHE C 229 ? 0.2216 0.4671 0.2744 0.0031 0.0144 -0.0215 228 PHE C CG 5471 C CD1 . PHE C 229 ? 0.2308 0.4630 0.2782 -0.0012 0.0159 -0.0318 228 PHE C CD1 5472 C CD2 . PHE C 229 ? 0.2161 0.4821 0.2749 0.0063 0.0141 -0.0182 228 PHE C CD2 5473 C CE1 . PHE C 229 ? 0.2318 0.4739 0.2830 -0.0035 0.0168 -0.0388 228 PHE C CE1 5474 C CE2 . PHE C 229 ? 0.2153 0.4901 0.2764 0.0059 0.0145 -0.0258 228 PHE C CE2 5475 C CZ . PHE C 229 ? 0.2196 0.4841 0.2785 0.0004 0.0157 -0.0362 228 PHE C CZ 5476 N N . PHE C 230 ? 0.2146 0.4314 0.2583 0.0089 0.0066 -0.0145 229 PHE C N 5477 C CA . PHE C 230 ? 0.2181 0.4243 0.2614 0.0093 0.0018 -0.0098 229 PHE C CA 5478 C C . PHE C 230 ? 0.2221 0.3965 0.2544 0.0016 0.0001 -0.0110 229 PHE C C 5479 O O . PHE C 230 ? 0.2202 0.3825 0.2454 -0.0032 0.0042 -0.0165 229 PHE C O 5480 C CB . PHE C 230 ? 0.2298 0.4357 0.2687 0.0186 0.0003 -0.0166 229 PHE C CB 5481 C CG . PHE C 230 ? 0.2260 0.4633 0.2724 0.0288 0.0031 -0.0168 229 PHE C CG 5482 C CD1 . PHE C 230 ? 0.2290 0.4733 0.2700 0.0316 0.0068 -0.0251 229 PHE C CD1 5483 C CD2 . PHE C 230 ? 0.2207 0.4822 0.2792 0.0355 0.0022 -0.0087 229 PHE C CD2 5484 C CE1 . PHE C 230 ? 0.2259 0.4976 0.2693 0.0422 0.0096 -0.0259 229 PHE C CE1 5485 C CE2 . PHE C 230 ? 0.2214 0.5143 0.2852 0.0458 0.0068 -0.0085 229 PHE C CE2 5486 C CZ . PHE C 230 ? 0.2263 0.5225 0.2804 0.0498 0.0106 -0.0175 229 PHE C CZ 5487 N N . TRP C 231 ? 0.2267 0.3892 0.2573 0.0007 -0.0060 -0.0056 230 TRP C N 5488 C CA . TRP C 231 ? 0.2341 0.3655 0.2510 -0.0056 -0.0085 -0.0057 230 TRP C CA 5489 C C . TRP C 231 ? 0.2487 0.3654 0.2603 -0.0037 -0.0169 -0.0032 230 TRP C C 5490 O O . TRP C 231 ? 0.2382 0.3741 0.2623 0.0019 -0.0215 0.0009 230 TRP C O 5491 C CB . TRP C 231 ? 0.2313 0.3609 0.2504 -0.0112 -0.0094 0.0012 230 TRP C CB 5492 C CG . TRP C 231 ? 0.2263 0.3705 0.2583 -0.0122 -0.0165 0.0123 230 TRP C CG 5493 C CD1 . TRP C 231 ? 0.2172 0.3903 0.2649 -0.0113 -0.0153 0.0193 230 TRP C CD1 5494 C CD2 . TRP C 231 ? 0.2355 0.3656 0.2654 -0.0161 -0.0266 0.0190 230 TRP C CD2 5495 N NE1 . TRP C 231 ? 0.2153 0.3942 0.2723 -0.0157 -0.0234 0.0307 230 TRP C NE1 5496 C CE2 . TRP C 231 ? 0.2278 0.3808 0.2750 -0.0189 -0.0313 0.0303 230 TRP C CE2 5497 C CE3 . TRP C 231 ? 0.2531 0.3529 0.2670 -0.0182 -0.0330 0.0170 230 TRP C CE3 5498 C CZ2 . TRP C 231 ? 0.2376 0.3858 0.2895 -0.0248 -0.0428 0.0393 230 TRP C CZ2 5499 C CZ3 . TRP C 231 ? 0.2599 0.3534 0.2763 -0.0224 -0.0451 0.0250 230 TRP C CZ3 5500 C CH2 . TRP C 231 ? 0.2539 0.3722 0.2906 -0.0262 -0.0503 0.0360 230 TRP C CH2 5501 N N . THR C 232 ? 0.2695 0.3535 0.2624 -0.0081 -0.0188 -0.0056 231 THR C N 5502 C CA . THR C 232 ? 0.2845 0.3506 0.2696 -0.0071 -0.0287 -0.0025 231 THR C CA 5503 C C . THR C 232 ? 0.3047 0.3356 0.2672 -0.0137 -0.0300 -0.0028 231 THR C C 5504 O O . THR C 232 ? 0.3056 0.3261 0.2578 -0.0181 -0.0213 -0.0068 231 THR C O 5505 C CB . THR C 232 ? 0.2957 0.3564 0.2759 0.0009 -0.0313 -0.0078 231 THR C CB 5506 O OG1 . THR C 232 ? 0.3100 0.3672 0.2921 0.0047 -0.0429 -0.0026 231 THR C OG1 5507 C CG2 . THR C 232 ? 0.3209 0.3483 0.2772 -0.0025 -0.0275 -0.0150 231 THR C CG2 5508 N N . ILE C 233 ? 0.3218 0.3372 0.2773 -0.0138 -0.0414 0.0016 232 ILE C N 5509 C CA . ILE C 233 ? 0.3457 0.3239 0.2746 -0.0182 -0.0448 0.0011 232 ILE C CA 5510 C C . ILE C 233 ? 0.3712 0.3258 0.2819 -0.0151 -0.0474 -0.0025 232 ILE C C 5511 O O . ILE C 233 ? 0.3688 0.3235 0.2829 -0.0095 -0.0585 -0.0002 232 ILE C O 5512 C CB . ILE C 233 ? 0.3514 0.3233 0.2808 -0.0207 -0.0588 0.0083 232 ILE C CB 5513 C CG1 . ILE C 233 ? 0.3396 0.3292 0.2843 -0.0248 -0.0582 0.0131 232 ILE C CG1 5514 C CG2 . ILE C 233 ? 0.3835 0.3139 0.2806 -0.0235 -0.0639 0.0070 232 ILE C CG2 5515 C CD1 . ILE C 233 ? 0.3449 0.3217 0.2761 -0.0271 -0.0476 0.0089 232 ILE C CD1 5516 N N . LEU C 234 ? 0.3905 0.3252 0.2822 -0.0188 -0.0375 -0.0078 233 LEU C N 5517 C CA . LEU C 234 ? 0.4247 0.3304 0.2945 -0.0177 -0.0401 -0.0102 233 LEU C CA 5518 C C . LEU C 234 ? 0.4648 0.3342 0.3052 -0.0208 -0.0465 -0.0071 233 LEU C C 5519 O O . LEU C 234 ? 0.4827 0.3387 0.3072 -0.0269 -0.0387 -0.0074 233 LEU C O 5520 C CB . LEU C 234 ? 0.4245 0.3258 0.2880 -0.0228 -0.0273 -0.0158 233 LEU C CB 5521 C CG . LEU C 234 ? 0.4537 0.3249 0.2958 -0.0232 -0.0293 -0.0183 233 LEU C CG 5522 C CD1 . LEU C 234 ? 0.4513 0.3283 0.3027 -0.0116 -0.0400 -0.0200 233 LEU C CD1 5523 C CD2 . LEU C 234 ? 0.4552 0.3264 0.2951 -0.0323 -0.0164 -0.0227 233 LEU C CD2 5524 N N . LYS C 235 ? 0.4890 0.3439 0.3217 -0.0154 -0.0610 -0.0044 234 LYS C N 5525 C CA . LYS C 235 ? 0.5331 0.3523 0.3357 -0.0174 -0.0699 -0.0013 234 LYS C CA 5526 C C . LYS C 235 ? 0.5552 0.3376 0.3229 -0.0220 -0.0623 -0.0030 234 LYS C C 5527 O O . LYS C 235 ? 0.5562 0.3367 0.3239 -0.0224 -0.0560 -0.0058 234 LYS C O 5528 C CB . LYS C 235 ? 0.5585 0.3748 0.3646 -0.0096 -0.0895 0.0023 234 LYS C CB 5529 C CG . LYS C 235 ? 0.5413 0.3944 0.3818 -0.0070 -0.0987 0.0064 234 LYS C CG 5530 C CD . LYS C 235 ? 0.5715 0.4123 0.4029 -0.0129 -0.1088 0.0105 234 LYS C CD 5531 C CE . LYS C 235 ? 0.5559 0.4270 0.4138 -0.0178 -0.1053 0.0130 234 LYS C CE 5532 N NZ . LYS C 235 ? 0.5847 0.4405 0.4334 -0.0235 -0.1189 0.0169 234 LYS C NZ 5533 N N . PRO C 236 ? 0.5868 0.3381 0.3226 -0.0260 -0.0632 -0.0010 235 PRO C N 5534 C CA . PRO C 236 ? 0.6201 0.3347 0.3193 -0.0310 -0.0567 -0.0004 235 PRO C CA 5535 C C . PRO C 236 ? 0.6461 0.3412 0.3358 -0.0264 -0.0669 0.0007 235 PRO C C 5536 O O . PRO C 236 ? 0.6548 0.3478 0.3486 -0.0177 -0.0845 0.0026 235 PRO C O 5537 C CB . PRO C 236 ? 0.6473 0.3330 0.3144 -0.0316 -0.0627 0.0020 235 PRO C CB 5538 C CG . PRO C 236 ? 0.6240 0.3335 0.3112 -0.0307 -0.0633 0.0006 235 PRO C CG 5539 C CD . PRO C 236 ? 0.5890 0.3372 0.3194 -0.0268 -0.0688 0.0004 235 PRO C CD 5540 N N . ASN C 237 ? 0.6680 0.3494 0.3461 -0.0322 -0.0568 -0.0001 236 ASN C N 5541 C CA . ASN C 237 ? 0.7005 0.3565 0.3652 -0.0279 -0.0661 0.0005 236 ASN C CA 5542 C C . ASN C 237 ? 0.6741 0.3559 0.3703 -0.0174 -0.0731 -0.0039 236 ASN C C 5543 O O . ASN C 237 ? 0.6963 0.3571 0.3821 -0.0104 -0.0825 -0.0045 236 ASN C O 5544 C CB . ASN C 237 ? 0.7491 0.3683 0.3822 -0.0223 -0.0826 0.0054 236 ASN C CB 5545 C CG . ASN C 237 ? 0.8069 0.3833 0.3950 -0.0324 -0.0755 0.0101 236 ASN C CG 5546 O OD1 . ASN C 237 ? 0.8390 0.3879 0.4077 -0.0363 -0.0742 0.0120 236 ASN C OD1 5547 N ND2 . ASN C 237 ? 0.8276 0.3965 0.3969 -0.0367 -0.0708 0.0122 236 ASN C ND2 5548 N N . ASP C 238 ? 0.6317 0.3572 0.3639 -0.0150 -0.0686 -0.0069 237 ASP C N 5549 C CA . ASP C 238 ? 0.6079 0.3612 0.3685 -0.0061 -0.0705 -0.0117 237 ASP C CA 5550 C C . ASP C 238 ? 0.5892 0.3498 0.3550 -0.0149 -0.0555 -0.0165 237 ASP C C 5551 O O . ASP C 238 ? 0.5902 0.3464 0.3472 -0.0277 -0.0429 -0.0155 237 ASP C O 5552 C CB . ASP C 238 ? 0.5745 0.3715 0.3701 0.0007 -0.0743 -0.0109 237 ASP C CB 5553 C CG . ASP C 238 ? 0.5645 0.3880 0.3850 0.0146 -0.0800 -0.0144 237 ASP C CG 5554 O OD1 . ASP C 238 ? 0.5710 0.3733 0.3784 0.0219 -0.0847 -0.0180 237 ASP C OD1 5555 O OD2 . ASP C 238 ? 0.5384 0.4030 0.3900 0.0185 -0.0795 -0.0134 237 ASP C OD2 5556 N N . ALA C 239 ? 0.5777 0.3492 0.3569 -0.0073 -0.0577 -0.0221 238 ALA C N 5557 C CA . ALA C 239 ? 0.5594 0.3381 0.3447 -0.0149 -0.0470 -0.0278 238 ALA C CA 5558 C C . ALA C 239 ? 0.5147 0.3358 0.3322 -0.0051 -0.0463 -0.0330 238 ALA C C 5559 O O . ALA C 239 ? 0.5037 0.3411 0.3344 0.0091 -0.0551 -0.0328 238 ALA C O 5560 C CB . ALA C 239 ? 0.5993 0.3376 0.3593 -0.0163 -0.0518 -0.0304 238 ALA C CB 5561 N N . ILE C 240 ? 0.4968 0.3377 0.3272 -0.0131 -0.0355 -0.0369 239 ILE C N 5562 C CA . ILE C 240 ? 0.4699 0.3482 0.3262 -0.0048 -0.0339 -0.0423 239 ILE C CA 5563 C C . ILE C 240 ? 0.4840 0.3486 0.3322 -0.0065 -0.0337 -0.0507 239 ILE C C 5564 O O . ILE C 240 ? 0.4900 0.3370 0.3269 -0.0215 -0.0281 -0.0512 239 ILE C O 5565 C CB . ILE C 240 ? 0.4350 0.3497 0.3135 -0.0111 -0.0239 -0.0399 239 ILE C CB 5566 C CG1 . ILE C 240 ? 0.4099 0.3630 0.3128 -0.0016 -0.0230 -0.0438 239 ILE C CG1 5567 C CG2 . ILE C 240 ? 0.4387 0.3476 0.3117 -0.0272 -0.0129 -0.0406 239 ILE C CG2 5568 C CD1 . ILE C 240 ? 0.3790 0.3668 0.3036 -0.0038 -0.0173 -0.0388 239 ILE C CD1 5569 N N . ASN C 241 ? 0.4958 0.3675 0.3488 0.0089 -0.0405 -0.0571 240 ASN C N 5570 C CA . ASN C 241 ? 0.5268 0.3825 0.3695 0.0093 -0.0427 -0.0667 240 ASN C CA 5571 C C . ASN C 241 ? 0.5002 0.3953 0.3642 0.0160 -0.0386 -0.0730 240 ASN C C 5572 O O . ASN C 241 ? 0.4879 0.4118 0.3669 0.0322 -0.0401 -0.0732 240 ASN C O 5573 C CB . ASN C 241 ? 0.5697 0.3923 0.3924 0.0248 -0.0553 -0.0713 240 ASN C CB 5574 C CG . ASN C 241 ? 0.6051 0.3894 0.4055 0.0216 -0.0616 -0.0640 240 ASN C CG 5575 O OD1 . ASN C 241 ? 0.6260 0.4076 0.4249 0.0372 -0.0704 -0.0619 240 ASN C OD1 5576 N ND2 . ASN C 241 ? 0.6272 0.3841 0.4106 0.0015 -0.0569 -0.0596 240 ASN C ND2 5577 N N . PHE C 242 ? 0.4949 0.3921 0.3601 0.0029 -0.0335 -0.0775 241 PHE C N 5578 C CA . PHE C 242 ? 0.4787 0.4083 0.3593 0.0079 -0.0308 -0.0841 241 PHE C CA 5579 C C . PHE C 242 ? 0.5217 0.4250 0.3841 0.0123 -0.0389 -0.0960 241 PHE C C 5580 O O . PHE C 242 ? 0.5653 0.4318 0.4096 -0.0013 -0.0424 -0.0981 241 PHE C O 5581 C CB . PHE C 242 ? 0.4542 0.4065 0.3500 -0.0088 -0.0215 -0.0813 241 PHE C CB 5582 C CG . PHE C 242 ? 0.4214 0.3994 0.3339 -0.0110 -0.0142 -0.0712 241 PHE C CG 5583 C CD1 . PHE C 242 ? 0.3935 0.4092 0.3255 -0.0004 -0.0120 -0.0686 241 PHE C CD1 5584 C CD2 . PHE C 242 ? 0.4270 0.3894 0.3334 -0.0237 -0.0097 -0.0641 241 PHE C CD2 5585 C CE1 . PHE C 242 ? 0.3707 0.4053 0.3161 -0.0034 -0.0071 -0.0593 241 PHE C CE1 5586 C CE2 . PHE C 242 ? 0.4049 0.3864 0.3231 -0.0246 -0.0043 -0.0562 241 PHE C CE2 5587 C CZ . PHE C 242 ? 0.3781 0.3941 0.3159 -0.0148 -0.0040 -0.0539 241 PHE C CZ 5588 N N . GLU C 243 ? 0.5220 0.4419 0.3870 0.0316 -0.0422 -0.1036 242 GLU C N 5589 C CA . GLU C 243 ? 0.5558 0.4544 0.4032 0.0368 -0.0498 -0.1168 242 GLU C CA 5590 C C . GLU C 243 ? 0.5362 0.4754 0.3985 0.0427 -0.0455 -0.1220 242 GLU C C 5591 O O . GLU C 243 ? 0.5092 0.4886 0.3898 0.0542 -0.0392 -0.1171 242 GLU C O 5592 C CB . GLU C 243 ? 0.5892 0.4607 0.4169 0.0590 -0.0597 -0.1235 242 GLU C CB 5593 C CG . GLU C 243 ? 0.6418 0.4723 0.4423 0.0608 -0.0704 -0.1373 242 GLU C CG 5594 C CD . GLU C 243 ? 0.6854 0.4871 0.4642 0.0864 -0.0808 -0.1454 242 GLU C CD 5595 O OE1 . GLU C 243 ? 0.7137 0.4898 0.4834 0.0893 -0.0853 -0.1394 242 GLU C OE1 5596 O OE2 . GLU C 243 ? 0.7022 0.5057 0.4712 0.1049 -0.0850 -0.1581 242 GLU C OE2 5597 N N . SER C 244 ? 0.5474 0.4758 0.4011 0.0336 -0.0494 -0.1312 243 SER C N 5598 C CA . SER C 244 ? 0.5238 0.4872 0.3878 0.0383 -0.0468 -0.1366 243 SER C CA 5599 C C . SER C 244 ? 0.5511 0.4927 0.4001 0.0287 -0.0556 -0.1487 243 SER C C 5600 O O . SER C 244 ? 0.5606 0.4742 0.4037 0.0076 -0.0594 -0.1483 243 SER C O 5601 C CB . SER C 244 ? 0.4771 0.4819 0.3687 0.0270 -0.0361 -0.1255 243 SER C CB 5602 O OG . SER C 244 ? 0.4697 0.4992 0.3678 0.0254 -0.0359 -0.1307 243 SER C OG 5603 N N . ASN C 245 ? 0.5612 0.5170 0.4037 0.0438 -0.0588 -0.1590 244 ASN C N 5604 C CA . ASN C 245 ? 0.5919 0.5298 0.4190 0.0371 -0.0691 -0.1721 244 ASN C CA 5605 C C . ASN C 245 ? 0.5648 0.5458 0.4081 0.0344 -0.0653 -0.1724 244 ASN C C 5606 O O . ASN C 245 ? 0.5852 0.5597 0.4152 0.0346 -0.0744 -0.1844 244 ASN C O 5607 C CB . ASN C 245 ? 0.6420 0.5487 0.4379 0.0597 -0.0795 -0.1872 244 ASN C CB 5608 C CG . ASN C 245 ? 0.6317 0.5747 0.4294 0.0883 -0.0730 -0.1896 244 ASN C CG 5609 O OD1 . ASN C 245 ? 0.5933 0.5778 0.4149 0.0925 -0.0609 -0.1773 244 ASN C OD1 5610 N ND2 . ASN C 245 ? 0.6738 0.6004 0.4449 0.1079 -0.0811 -0.2053 244 ASN C ND2 5611 N N . GLY C 246 ? 0.5154 0.5375 0.3853 0.0319 -0.0533 -0.1593 245 GLY C N 5612 C CA . GLY C 246 ? 0.4892 0.5518 0.3745 0.0307 -0.0496 -0.1574 245 GLY C CA 5613 C C . GLY C 246 ? 0.4497 0.5516 0.3593 0.0339 -0.0369 -0.1424 245 GLY C C 5614 O O . GLY C 246 ? 0.4385 0.5423 0.3511 0.0435 -0.0314 -0.1354 245 GLY C O 5615 N N . ASN C 247 ? 0.4297 0.5615 0.3568 0.0251 -0.0338 -0.1375 246 ASN C N 5616 C CA . ASN C 247 ? 0.3964 0.5651 0.3435 0.0292 -0.0238 -0.1242 246 ASN C CA 5617 C C . ASN C 247 ? 0.3692 0.5362 0.3313 0.0206 -0.0166 -0.1118 246 ASN C C 5618 O O . ASN C 247 ? 0.3401 0.5318 0.3162 0.0242 -0.0098 -0.1008 246 ASN C O 5619 C CB . ASN C 247 ? 0.3948 0.5828 0.3351 0.0510 -0.0204 -0.1234 246 ASN C CB 5620 C CG . ASN C 247 ? 0.4151 0.6070 0.3376 0.0613 -0.0266 -0.1356 246 ASN C CG 5621 O OD1 . ASN C 247 ? 0.4431 0.6060 0.3444 0.0649 -0.0352 -0.1492 246 ASN C OD1 5622 N ND2 . ASN C 247 ? 0.4044 0.6293 0.3327 0.0660 -0.0232 -0.1308 246 ASN C ND2 5623 N N . PHE C 248 ? 0.3836 0.5199 0.3408 0.0082 -0.0187 -0.1134 247 PHE C N 5624 C CA . PHE C 248 ? 0.3672 0.4955 0.3326 0.0003 -0.0127 -0.1030 247 PHE C CA 5625 C C . PHE C 248 ? 0.3498 0.4952 0.3336 -0.0139 -0.0070 -0.0963 247 PHE C C 5626 O O . PHE C 248 ? 0.3521 0.4953 0.3390 -0.0272 -0.0091 -0.1008 247 PHE C O 5627 C CB . PHE C 248 ? 0.3952 0.4811 0.3434 -0.0061 -0.0173 -0.1072 247 PHE C CB 5628 C CG . PHE C 248 ? 0.3932 0.4659 0.3436 -0.0126 -0.0121 -0.0973 247 PHE C CG 5629 C CD1 . PHE C 248 ? 0.3685 0.4577 0.3283 -0.0038 -0.0073 -0.0878 247 PHE C CD1 5630 C CD2 . PHE C 248 ? 0.4119 0.4539 0.3528 -0.0281 -0.0129 -0.0972 247 PHE C CD2 5631 C CE1 . PHE C 248 ? 0.3656 0.4399 0.3242 -0.0095 -0.0044 -0.0798 247 PHE C CE1 5632 C CE2 . PHE C 248 ? 0.4097 0.4379 0.3484 -0.0331 -0.0082 -0.0884 247 PHE C CE2 5633 C CZ . PHE C 248 ? 0.3892 0.4327 0.3360 -0.0232 -0.0046 -0.0804 247 PHE C CZ 5634 N N . ILE C 249 ? 0.3281 0.4917 0.3244 -0.0107 -0.0005 -0.0856 248 ILE C N 5635 C CA . ILE C 249 ? 0.3064 0.4816 0.3174 -0.0213 0.0052 -0.0792 248 ILE C CA 5636 C C . ILE C 249 ? 0.3093 0.4601 0.3144 -0.0274 0.0091 -0.0739 248 ILE C C 5637 O O . ILE C 249 ? 0.3049 0.4533 0.3089 -0.0206 0.0104 -0.0669 248 ILE C O 5638 C CB . ILE C 249 ? 0.2876 0.4927 0.3124 -0.0140 0.0085 -0.0712 248 ILE C CB 5639 C CG1 . ILE C 249 ? 0.2827 0.5097 0.3079 -0.0048 0.0045 -0.0750 248 ILE C CG1 5640 C CG2 . ILE C 249 ? 0.2831 0.4996 0.3216 -0.0224 0.0133 -0.0673 248 ILE C CG2 5641 C CD1 . ILE C 249 ? 0.2989 0.5320 0.3256 -0.0113 -0.0003 -0.0843 248 ILE C CD1 5642 N N . ALA C 250 ? 0.3238 0.4562 0.3241 -0.0411 0.0102 -0.0767 249 ALA C N 5643 C CA . ALA C 250 ? 0.3335 0.4357 0.3208 -0.0472 0.0125 -0.0730 249 ALA C CA 5644 C C . ALA C 250 ? 0.3235 0.4319 0.3176 -0.0513 0.0210 -0.0647 249 ALA C C 5645 O O . ALA C 250 ? 0.3066 0.4395 0.3160 -0.0538 0.0258 -0.0635 249 ALA C O 5646 C CB . ALA C 250 ? 0.3607 0.4382 0.3370 -0.0612 0.0101 -0.0783 249 ALA C CB 5647 N N . PRO C 251 ? 0.3392 0.4240 0.3202 -0.0507 0.0221 -0.0596 250 PRO C N 5648 C CA . PRO C 251 ? 0.3402 0.4232 0.3209 -0.0550 0.0299 -0.0532 250 PRO C CA 5649 C C . PRO C 251 ? 0.3560 0.4400 0.3386 -0.0693 0.0380 -0.0542 250 PRO C C 5650 O O . PRO C 251 ? 0.3862 0.4555 0.3617 -0.0797 0.0363 -0.0578 250 PRO C O 5651 C CB . PRO C 251 ? 0.3582 0.4087 0.3186 -0.0530 0.0268 -0.0494 250 PRO C CB 5652 C CG . PRO C 251 ? 0.3633 0.4095 0.3209 -0.0429 0.0173 -0.0521 250 PRO C CG 5653 C CD . PRO C 251 ? 0.3614 0.4198 0.3258 -0.0442 0.0152 -0.0599 250 PRO C CD 5654 N N . GLU C 252 ? 0.3406 0.4422 0.3329 -0.0697 0.0464 -0.0509 251 GLU C N 5655 C CA . GLU C 252 ? 0.3565 0.4598 0.3494 -0.0820 0.0568 -0.0498 251 GLU C CA 5656 C C . GLU C 252 ? 0.3573 0.4460 0.3359 -0.0788 0.0640 -0.0442 251 GLU C C 5657 O O . GLU C 252 ? 0.3802 0.4440 0.3399 -0.0870 0.0684 -0.0415 251 GLU C O 5658 C CB . GLU C 252 ? 0.3538 0.4961 0.3724 -0.0839 0.0613 -0.0524 251 GLU C CB 5659 C CG . GLU C 252 ? 0.3764 0.5291 0.4013 -0.0978 0.0726 -0.0511 251 GLU C CG 5660 C CD . GLU C 252 ? 0.3743 0.5700 0.4285 -0.0986 0.0754 -0.0538 251 GLU C CD 5661 O OE1 . GLU C 252 ? 0.3679 0.5807 0.4346 -0.0909 0.0664 -0.0576 251 GLU C OE1 5662 O OE2 . GLU C 252 ? 0.3856 0.5999 0.4504 -0.1065 0.0867 -0.0518 251 GLU C OE2 5663 N N . ASN C 253 ? 0.3337 0.4352 0.3187 -0.0670 0.0643 -0.0425 252 ASN C N 5664 C CA . ASN C 253 ? 0.3453 0.4298 0.3140 -0.0619 0.0686 -0.0385 252 ASN C CA 5665 C C . ASN C 253 ? 0.3376 0.4033 0.2957 -0.0529 0.0576 -0.0357 252 ASN C C 5666 O O . ASN C 253 ? 0.3141 0.3923 0.2845 -0.0469 0.0494 -0.0359 252 ASN C O 5667 C CB . ASN C 253 ? 0.3397 0.4483 0.3208 -0.0549 0.0763 -0.0387 252 ASN C CB 5668 C CG . ASN C 253 ? 0.3384 0.4740 0.3358 -0.0632 0.0874 -0.0410 252 ASN C CG 5669 O OD1 . ASN C 253 ? 0.3471 0.4740 0.3361 -0.0752 0.0948 -0.0400 252 ASN C OD1 5670 N ND2 . ASN C 253 ? 0.3194 0.4889 0.3409 -0.0574 0.0877 -0.0434 252 ASN C ND2 5671 N N . ALA C 254 ? 0.3573 0.3938 0.2922 -0.0526 0.0574 -0.0326 253 ALA C N 5672 C CA . ALA C 254 ? 0.3524 0.3710 0.2773 -0.0455 0.0464 -0.0292 253 ALA C CA 5673 C C . ALA C 254 ? 0.3626 0.3665 0.2716 -0.0409 0.0491 -0.0272 253 ALA C C 5674 O O . ALA C 254 ? 0.3685 0.3748 0.2718 -0.0424 0.0609 -0.0288 253 ALA C O 5675 C CB . ALA C 254 ? 0.3692 0.3607 0.2772 -0.0491 0.0396 -0.0282 253 ALA C CB 5676 N N . TYR C 255 ? 0.3653 0.3547 0.2672 -0.0353 0.0379 -0.0239 254 TYR C N 5677 C CA . TYR C 255 ? 0.3841 0.3551 0.2685 -0.0301 0.0369 -0.0228 254 TYR C CA 5678 C C . TYR C 255 ? 0.4079 0.3431 0.2653 -0.0311 0.0278 -0.0202 254 TYR C C 5679 O O . TYR C 255 ? 0.4034 0.3336 0.2646 -0.0306 0.0143 -0.0168 254 TYR C O 5680 C CB . TYR C 255 ? 0.3700 0.3534 0.2691 -0.0235 0.0292 -0.0206 254 TYR C CB 5681 C CG . TYR C 255 ? 0.3565 0.3721 0.2786 -0.0202 0.0364 -0.0228 254 TYR C CG 5682 C CD1 . TYR C 255 ? 0.3352 0.3778 0.2809 -0.0220 0.0346 -0.0224 254 TYR C CD1 5683 C CD2 . TYR C 255 ? 0.3658 0.3847 0.2848 -0.0137 0.0442 -0.0255 254 TYR C CD2 5684 C CE1 . TYR C 255 ? 0.3189 0.3903 0.2842 -0.0186 0.0394 -0.0242 254 TYR C CE1 5685 C CE2 . TYR C 255 ? 0.3492 0.3984 0.2900 -0.0093 0.0491 -0.0273 254 TYR C CE2 5686 C CZ . TYR C 255 ? 0.3288 0.4037 0.2925 -0.0125 0.0462 -0.0264 254 TYR C CZ 5687 O OH . TYR C 255 ? 0.3192 0.4234 0.3030 -0.0079 0.0495 -0.0280 254 TYR C OH 5688 N N . LYS C 256 ? 0.4355 0.3480 0.2657 -0.0321 0.0354 -0.0215 255 LYS C N 5689 C CA . LYS C 256 ? 0.4627 0.3378 0.2616 -0.0317 0.0265 -0.0195 255 LYS C CA 5690 C C . LYS C 256 ? 0.4624 0.3246 0.2532 -0.0247 0.0165 -0.0193 255 LYS C C 5691 O O . LYS C 256 ? 0.4699 0.3358 0.2578 -0.0189 0.0239 -0.0224 255 LYS C O 5692 C CB . LYS C 256 ? 0.4960 0.3511 0.2650 -0.0345 0.0394 -0.0207 255 LYS C CB 5693 C CG . LYS C 256 ? 0.5011 0.3643 0.2751 -0.0441 0.0492 -0.0199 255 LYS C CG 5694 C CD . LYS C 256 ? 0.5483 0.3817 0.2865 -0.0494 0.0566 -0.0176 255 LYS C CD 5695 C CE . LYS C 256 ? 0.5767 0.4057 0.2943 -0.0447 0.0704 -0.0196 255 LYS C CE 5696 N NZ . LYS C 256 ? 0.6257 0.4220 0.3032 -0.0496 0.0761 -0.0161 255 LYS C NZ 5697 N N . ILE C 257 ? 0.4649 0.3115 0.2518 -0.0253 -0.0011 -0.0156 256 ILE C N 5698 C CA . ILE C 257 ? 0.4753 0.3044 0.2524 -0.0213 -0.0140 -0.0146 256 ILE C CA 5699 C C . ILE C 257 ? 0.5105 0.2999 0.2451 -0.0184 -0.0145 -0.0176 256 ILE C C 5700 O O . ILE C 257 ? 0.5263 0.2919 0.2397 -0.0213 -0.0220 -0.0160 256 ILE C O 5701 C CB . ILE C 257 ? 0.4680 0.3009 0.2617 -0.0248 -0.0335 -0.0085 256 ILE C CB 5702 C CG1 . ILE C 257 ? 0.4361 0.3095 0.2689 -0.0259 -0.0308 -0.0057 256 ILE C CG1 5703 C CG2 . ILE C 257 ? 0.4859 0.2948 0.2661 -0.0240 -0.0494 -0.0068 256 ILE C CG2 5704 C CD1 . ILE C 257 ? 0.4279 0.3159 0.2816 -0.0291 -0.0442 0.0005 256 ILE C CD1 5705 N N . VAL C 258 ? 0.5250 0.3074 0.2458 -0.0112 -0.0064 -0.0224 257 VAL C N 5706 C CA . VAL C 258 ? 0.5679 0.3173 0.2462 -0.0060 -0.0008 -0.0268 257 VAL C CA 5707 C C . VAL C 258 ? 0.5986 0.3114 0.2503 -0.0012 -0.0187 -0.0285 257 VAL C C 5708 O O . VAL C 258 ? 0.6354 0.3125 0.2481 0.0003 -0.0234 -0.0304 257 VAL C O 5709 C CB . VAL C 258 ? 0.5703 0.3375 0.2486 0.0007 0.0220 -0.0319 257 VAL C CB 5710 C CG1 . VAL C 258 ? 0.6162 0.3523 0.2517 0.0106 0.0279 -0.0376 257 VAL C CG1 5711 C CG2 . VAL C 258 ? 0.5587 0.3500 0.2507 -0.0072 0.0381 -0.0299 257 VAL C CG2 5712 N N . LYS C 259 ? 0.3553 0.6063 0.4836 -0.1802 0.0801 -0.1170 258 LYS C N 5713 C CA . LYS C 259 ? 0.3667 0.6031 0.4958 -0.1794 0.0686 -0.1149 258 LYS C CA 5714 C C . LYS C 259 ? 0.3437 0.5888 0.5210 -0.1608 0.0651 -0.1065 258 LYS C C 5715 O O . LYS C 259 ? 0.3129 0.5785 0.5105 -0.1455 0.0807 -0.1122 258 LYS C O 5716 C CB . LYS C 259 ? 0.3767 0.6187 0.4842 -0.1799 0.0846 -0.1314 258 LYS C CB 5717 C CG . LYS C 259 ? 0.4012 0.6179 0.4948 -0.1833 0.0728 -0.1302 258 LYS C CG 5718 C CD . LYS C 259 ? 0.4234 0.6370 0.4906 -0.1843 0.0937 -0.1476 258 LYS C CD 5719 C CE . LYS C 259 ? 0.4441 0.6335 0.5030 -0.1834 0.0819 -0.1456 258 LYS C CE 5720 N NZ . LYS C 259 ? 0.4889 0.6578 0.5075 -0.1890 0.1029 -0.1621 258 LYS C NZ 5721 N N . LYS C 260 ? 0.3660 0.5919 0.5613 -0.1642 0.0434 -0.0917 259 LYS C N 5722 C CA . LYS C 260 ? 0.3565 0.5874 0.6001 -0.1496 0.0409 -0.0835 259 LYS C CA 5723 C C . LYS C 260 ? 0.3830 0.6006 0.6144 -0.1552 0.0268 -0.0844 259 LYS C C 5724 O O . LYS C 260 ? 0.4206 0.6126 0.6088 -0.1742 0.0107 -0.0845 259 LYS C O 5725 C CB . LYS C 260 ? 0.3622 0.5834 0.6520 -0.1487 0.0271 -0.0633 259 LYS C CB 5726 C CG . LYS C 260 ? 0.3612 0.5858 0.6569 -0.1443 0.0424 -0.0619 259 LYS C CG 5727 C CD . LYS C 260 ? 0.3764 0.5871 0.7188 -0.1444 0.0291 -0.0414 259 LYS C CD 5728 C CE . LYS C 260 ? 0.3675 0.5830 0.7769 -0.1266 0.0437 -0.0326 259 LYS C CE 5729 N NZ . LYS C 260 ? 0.3690 0.5829 0.7796 -0.1143 0.0782 -0.0389 259 LYS C NZ 5730 N N . GLY C 261 ? 0.3702 0.5981 0.6331 -0.1407 0.0336 -0.0850 260 GLY C N 5731 C CA . GLY C 261 ? 0.3956 0.6108 0.6466 -0.1440 0.0236 -0.0874 260 GLY C CA 5732 C C . GLY C 261 ? 0.3800 0.6115 0.6642 -0.1246 0.0395 -0.0912 260 GLY C C 5733 O O . GLY C 261 ? 0.3634 0.6092 0.6785 -0.1114 0.0557 -0.0896 260 GLY C O 5734 N N . ASP C 262 ? 0.4092 0.6314 0.6794 -0.1245 0.0361 -0.0967 261 ASP C N 5735 C CA . ASP C 262 ? 0.4041 0.6352 0.7023 -0.1085 0.0478 -0.0988 261 ASP C CA 5736 C C . ASP C 262 ? 0.3773 0.6253 0.6611 -0.0939 0.0721 -0.1149 261 ASP C C 5737 O O . ASP C 262 ? 0.4014 0.6517 0.6519 -0.0952 0.0785 -0.1280 261 ASP C O 5738 C CB . ASP C 262 ? 0.4419 0.6531 0.7288 -0.1146 0.0333 -0.0979 261 ASP C CB 5739 C CG . ASP C 262 ? 0.4699 0.6711 0.8019 -0.1230 0.0092 -0.0770 261 ASP C CG 5740 O OD1 . ASP C 262 ? 0.4658 0.6740 0.8386 -0.1250 0.0023 -0.0625 261 ASP C OD1 5741 O OD2 . ASP C 262 ? 0.5052 0.6913 0.8369 -0.1276 -0.0031 -0.0739 261 ASP C OD2 5742 N N . SER C 263 ? 0.3416 0.5970 0.6514 -0.0812 0.0856 -0.1127 262 SER C N 5743 C CA . SER C 263 ? 0.3261 0.5905 0.6229 -0.0695 0.1013 -0.1239 262 SER C CA 5744 C C . SER C 263 ? 0.3062 0.5598 0.6220 -0.0594 0.1124 -0.1197 262 SER C C 5745 O O . SER C 263 ? 0.2974 0.5413 0.6419 -0.0603 0.1114 -0.1098 262 SER C O 5746 C CB . SER C 263 ? 0.3247 0.6007 0.6092 -0.0726 0.1071 -0.1268 262 SER C CB 5747 O OG . SER C 263 ? 0.3309 0.6148 0.6049 -0.0643 0.1152 -0.1352 262 SER C OG 5748 N N . THR C 264 ? 0.2958 0.5476 0.5951 -0.0518 0.1224 -0.1262 263 THR C N 5749 C CA . THR C 264 ? 0.2942 0.5236 0.5938 -0.0454 0.1353 -0.1239 263 THR C CA 5750 C C . THR C 264 ? 0.3015 0.5243 0.5704 -0.0425 0.1375 -0.1299 263 THR C C 5751 O O . THR C 264 ? 0.2855 0.5288 0.5462 -0.0426 0.1278 -0.1361 263 THR C O 5752 C CB . THR C 264 ? 0.2952 0.5149 0.6015 -0.0400 0.1335 -0.1249 263 THR C CB 5753 O OG1 . THR C 264 ? 0.3108 0.5027 0.6164 -0.0369 0.1498 -0.1215 263 THR C OG1 5754 C CG2 . THR C 264 ? 0.3004 0.5272 0.5857 -0.0337 0.1247 -0.1355 263 THR C CG2 5755 N N . ILE C 265 ? 0.3229 0.5130 0.5748 -0.0420 0.1503 -0.1272 264 ILE C N 5756 C CA . ILE C 265 ? 0.3430 0.5146 0.5577 -0.0426 0.1458 -0.1304 264 ILE C CA 5757 C C . ILE C 265 ? 0.3595 0.5071 0.5598 -0.0365 0.1442 -0.1324 264 ILE C C 5758 O O . ILE C 265 ? 0.3747 0.4904 0.5696 -0.0371 0.1610 -0.1294 264 ILE C O 5759 C CB . ILE C 265 ? 0.3728 0.5095 0.5584 -0.0513 0.1600 -0.1261 264 ILE C CB 5760 C CG1 . ILE C 265 ? 0.3573 0.5168 0.5589 -0.0569 0.1612 -0.1235 264 ILE C CG1 5761 C CG2 . ILE C 265 ? 0.4068 0.5187 0.5469 -0.0566 0.1469 -0.1272 264 ILE C CG2 5762 C CD1 . ILE C 265 ? 0.3867 0.5087 0.5700 -0.0637 0.1828 -0.1185 264 ILE C CD1 5763 N N . MET C 266 ? 0.3550 0.5182 0.5538 -0.0305 0.1257 -0.1372 265 MET C N 5764 C CA . MET C 266 ? 0.3784 0.5203 0.5646 -0.0236 0.1196 -0.1391 265 MET C CA 5765 C C . MET C 266 ? 0.4166 0.5184 0.5598 -0.0285 0.1098 -0.1360 265 MET C C 5766 O O . MET C 266 ? 0.4166 0.5284 0.5550 -0.0322 0.0933 -0.1344 265 MET C O 5767 C CB . MET C 266 ? 0.3671 0.5426 0.5783 -0.0132 0.1053 -0.1453 265 MET C CB 5768 C CG . MET C 266 ? 0.3624 0.5447 0.5909 -0.0087 0.1116 -0.1483 265 MET C CG 5769 S SD . MET C 266 ? 0.3759 0.5727 0.6163 0.0043 0.1006 -0.1567 265 MET C SD 5770 C CE . MET C 266 ? 0.3619 0.5676 0.6132 0.0002 0.1083 -0.1594 265 MET C CE 5771 N N . LYS C 267 ? 0.4536 0.5064 0.5638 -0.0306 0.1183 -0.1343 266 LYS C N 5772 C CA . LYS C 267 ? 0.5129 0.5144 0.5699 -0.0376 0.1040 -0.1306 266 LYS C CA 5773 C C . LYS C 267 ? 0.5132 0.5261 0.5831 -0.0263 0.0782 -0.1319 266 LYS C C 5774 O O . LYS C 267 ? 0.5085 0.5180 0.5871 -0.0183 0.0843 -0.1351 266 LYS C O 5775 C CB . LYS C 267 ? 0.5692 0.5024 0.5761 -0.0474 0.1294 -0.1289 266 LYS C CB 5776 C CG . LYS C 267 ? 0.5740 0.4967 0.5829 -0.0549 0.1634 -0.1280 266 LYS C CG 5777 C CD . LYS C 267 ? 0.5964 0.5099 0.5785 -0.0657 0.1579 -0.1253 266 LYS C CD 5778 C CE . LYS C 267 ? 0.6868 0.5132 0.5817 -0.0832 0.1618 -0.1222 266 LYS C CE 5779 N NZ . LYS C 267 ? 0.7170 0.5264 0.5754 -0.0970 0.1495 -0.1185 266 LYS C NZ 5780 N N . SER C 268 ? 0.5185 0.5470 0.5969 -0.0255 0.0492 -0.1286 267 SER C N 5781 C CA . SER C 268 ? 0.5199 0.5630 0.6242 -0.0125 0.0248 -0.1285 267 SER C CA 5782 C C . SER C 268 ? 0.5538 0.5882 0.6543 -0.0176 -0.0116 -0.1190 267 SER C C 5783 O O . SER C 268 ? 0.5540 0.5994 0.6549 -0.0281 -0.0191 -0.1148 267 SER C O 5784 C CB . SER C 268 ? 0.4646 0.5723 0.6334 0.0027 0.0326 -0.1366 267 SER C CB 5785 O OG . SER C 268 ? 0.4669 0.5827 0.6619 0.0173 0.0172 -0.1378 267 SER C OG 5786 N N . GLU C 269 ? 0.5894 0.6029 0.6887 -0.0109 -0.0370 -0.1144 268 GLU C N 5787 C CA . GLU C 269 ? 0.6288 0.6339 0.7359 -0.0151 -0.0799 -0.1020 268 GLU C CA 5788 C C . GLU C 269 ? 0.5867 0.6596 0.7861 0.0043 -0.0929 -0.1025 268 GLU C C 5789 O O . GLU C 269 ? 0.6033 0.6828 0.8342 0.0034 -0.1297 -0.0905 268 GLU C O 5790 C CB . GLU C 269 ? 0.7040 0.6333 0.7493 -0.0222 -0.1047 -0.0935 268 GLU C CB 5791 C CG . GLU C 269 ? 0.7673 0.6171 0.7139 -0.0453 -0.0894 -0.0924 268 GLU C CG 5792 C CD . GLU C 269 ? 0.7922 0.6272 0.7079 -0.0658 -0.0970 -0.0861 268 GLU C CD 5793 O OE1 . GLU C 269 ? 0.8043 0.6548 0.7458 -0.0702 -0.1373 -0.0749 268 GLU C OE1 5794 O OE2 . GLU C 269 ? 0.8065 0.6142 0.6769 -0.0775 -0.0627 -0.0915 268 GLU C OE2 5795 N N . LEU C 270 ? 0.5384 0.6576 0.7816 0.0202 -0.0621 -0.1155 269 LEU C N 5796 C CA . LEU C 270 ? 0.5086 0.6849 0.8347 0.0387 -0.0623 -0.1190 269 LEU C CA 5797 C C . LEU C 270 ? 0.4802 0.7080 0.8541 0.0337 -0.0600 -0.1181 269 LEU C C 5798 O O . LEU C 270 ? 0.4714 0.6971 0.8133 0.0179 -0.0513 -0.1182 269 LEU C O 5799 C CB . LEU C 270 ? 0.4803 0.6737 0.8190 0.0529 -0.0281 -0.1339 269 LEU C CB 5800 C CG . LEU C 270 ? 0.5079 0.6554 0.8051 0.0580 -0.0263 -0.1361 269 LEU C CG 5801 C CD1 . LEU C 270 ? 0.4800 0.6441 0.7864 0.0673 0.0058 -0.1500 269 LEU C CD1 5802 C CD2 . LEU C 270 ? 0.5448 0.6713 0.8592 0.0690 -0.0580 -0.1274 269 LEU C CD2 5803 N N . GLU C 271 ? 0.4706 0.7429 0.9246 0.0475 -0.0658 -0.1171 270 GLU C N 5804 C CA . GLU C 271 ? 0.4465 0.7720 0.9574 0.0442 -0.0585 -0.1174 270 GLU C CA 5805 C C . GLU C 271 ? 0.4132 0.7749 0.9571 0.0567 -0.0149 -0.1346 270 GLU C C 5806 O O . GLU C 271 ? 0.4195 0.7625 0.9387 0.0662 0.0040 -0.1444 270 GLU C O 5807 C CB . GLU C 271 ? 0.4590 0.8079 1.0460 0.0488 -0.0940 -0.1025 270 GLU C CB 5808 N N . TYR C 272 ? 0.3909 0.7980 0.9837 0.0540 0.0011 -0.1381 271 TYR C N 5809 C CA . TYR C 272 ? 0.3770 0.8084 0.9920 0.0621 0.0440 -0.1545 271 TYR C CA 5810 C C . TYR C 272 ? 0.3986 0.8357 1.0680 0.0850 0.0550 -0.1594 271 TYR C C 5811 O O . TYR C 272 ? 0.4075 0.8618 1.1458 0.0958 0.0336 -0.1489 271 TYR C O 5812 C CB . TYR C 272 ? 0.3589 0.8329 1.0152 0.0525 0.0593 -0.1563 271 TYR C CB 5813 C CG . TYR C 272 ? 0.3489 0.8337 1.0046 0.0540 0.1059 -0.1739 271 TYR C CG 5814 C CD1 . TYR C 272 ? 0.3449 0.7990 0.9273 0.0472 0.1234 -0.1838 271 TYR C CD1 5815 C CD2 . TYR C 272 ? 0.3470 0.8676 1.0738 0.0597 0.1323 -0.1796 271 TYR C CD2 5816 C CE1 . TYR C 272 ? 0.3491 0.8011 0.9176 0.0439 0.1608 -0.1983 271 TYR C CE1 5817 C CE2 . TYR C 272 ? 0.3538 0.8707 1.0647 0.0572 0.1777 -0.1966 271 TYR C CE2 5818 C CZ . TYR C 272 ? 0.3568 0.8358 0.9823 0.0481 0.1893 -0.2056 271 TYR C CZ 5819 O OH . TYR C 272 ? 0.3697 0.8336 0.9669 0.0414 0.2293 -0.2209 271 TYR C OH 5820 N N . GLY C 273 ? 0.4135 0.8328 1.0529 0.0917 0.0870 -0.1744 272 GLY C N 5821 C CA . GLY C 273 ? 0.4397 0.8530 1.1170 0.1133 0.1023 -0.1810 272 GLY C CA 5822 C C . GLY C 273 ? 0.4517 0.8827 1.1664 0.1199 0.1498 -0.1964 272 GLY C C 5823 O O . GLY C 273 ? 0.4742 0.8899 1.2066 0.1366 0.1713 -0.2049 272 GLY C O 5824 N N . ASN C 274 ? 0.4486 0.9052 1.1700 0.1058 0.1689 -0.2004 273 ASN C N 5825 C CA . ASN C 274 ? 0.4754 0.9443 1.2303 0.1085 0.2183 -0.2151 273 ASN C CA 5826 C C . ASN C 274 ? 0.5157 0.9385 1.2156 0.1129 0.2532 -0.2321 273 ASN C C 5827 O O . ASN C 274 ? 0.5403 0.9566 1.2819 0.1298 0.2834 -0.2408 273 ASN C O 5828 C CB . ASN C 274 ? 0.4789 0.9879 1.3513 0.1266 0.2234 -0.2093 273 ASN C CB 5829 C CG . ASN C 274 ? 0.4594 1.0124 1.3879 0.1179 0.1879 -0.1915 273 ASN C CG 5830 O OD1 . ASN C 274 ? 0.4572 1.0141 1.4101 0.1226 0.1402 -0.1740 273 ASN C OD1 5831 N ND2 . ASN C 274 ? 0.4544 1.0341 1.3961 0.1025 0.2093 -0.1952 273 ASN C ND2 5832 N N . CYS C 275 ? 0.5242 0.9126 1.1321 0.0967 0.2480 -0.2357 274 CYS C N 5833 C CA . CYS C 275 ? 0.5669 0.9040 1.1096 0.0958 0.2693 -0.2483 274 CYS C CA 5834 C C . CYS C 275 ? 0.5662 0.8780 1.0245 0.0698 0.2699 -0.2515 274 CYS C C 5835 O O . CYS C 275 ? 0.5262 0.8595 0.9770 0.0565 0.2494 -0.2426 274 CYS C O 5836 C CB . CYS C 275 ? 0.5771 0.8922 1.1083 0.1092 0.2414 -0.2418 274 CYS C CB 5837 S SG . CYS C 275 ? 0.6106 0.8718 1.0386 0.0938 0.2307 -0.2440 274 CYS C SG 5838 N N . ASN C 276 ? 0.5992 0.8611 0.9936 0.0617 0.2915 -0.2630 275 ASN C N 5839 C CA . ASN C 276 ? 0.6023 0.8329 0.9168 0.0361 0.2845 -0.2631 275 ASN C CA 5840 C C . ASN C 276 ? 0.6089 0.7961 0.8691 0.0335 0.2671 -0.2612 275 ASN C C 5841 O O . ASN C 276 ? 0.6396 0.8004 0.8977 0.0465 0.2790 -0.2680 275 ASN C O 5842 C CB . ASN C 276 ? 0.6548 0.8551 0.9287 0.0191 0.3238 -0.2771 275 ASN C CB 5843 C CG . ASN C 276 ? 0.6666 0.8353 0.8623 -0.0101 0.3094 -0.2738 275 ASN C CG 5844 O OD1 . ASN C 276 ? 0.6217 0.8135 0.8197 -0.0167 0.2759 -0.2604 275 ASN C OD1 5845 N ND2 . ASN C 276 ? 0.7369 0.8473 0.8619 -0.0287 0.3346 -0.2853 275 ASN C ND2 5846 N N . THR C 277 ? 0.5829 0.7625 0.8041 0.0165 0.2397 -0.2513 276 THR C N 5847 C CA . THR C 277 ? 0.5904 0.7332 0.7685 0.0110 0.2206 -0.2469 276 THR C CA 5848 C C . THR C 277 ? 0.5956 0.7190 0.7255 -0.0151 0.2028 -0.2393 276 THR C C 5849 O O . THR C 277 ? 0.5703 0.7162 0.7068 -0.0257 0.1981 -0.2343 276 THR C O 5850 C CB . THR C 277 ? 0.5430 0.7068 0.7556 0.0264 0.1947 -0.2359 276 THR C CB 5851 O OG1 . THR C 277 ? 0.5547 0.6814 0.7299 0.0213 0.1815 -0.2329 276 THR C OG1 5852 C CG2 . THR C 277 ? 0.4971 0.6956 0.7306 0.0205 0.1736 -0.2232 276 THR C CG2 5853 N N . LYS C 278 ? 0.6330 0.7132 0.7174 -0.0262 0.1907 -0.2370 277 LYS C N 5854 C CA . LYS C 278 ? 0.6483 0.7111 0.7002 -0.0505 0.1652 -0.2251 277 LYS C CA 5855 C C . LYS C 278 ? 0.5905 0.6851 0.6838 -0.0452 0.1391 -0.2094 277 LYS C C 5856 O O . LYS C 278 ? 0.5771 0.6745 0.6699 -0.0608 0.1196 -0.1971 277 LYS C O 5857 C CB . LYS C 278 ? 0.7208 0.7200 0.7080 -0.0683 0.1590 -0.2267 277 LYS C CB 5858 C CG . LYS C 278 ? 0.8020 0.7493 0.7223 -0.0863 0.1816 -0.2395 277 LYS C CG 5859 C CD . LYS C 278 ? 0.8141 0.7647 0.7170 -0.1074 0.1746 -0.2342 277 LYS C CD 5860 C CE . LYS C 278 ? 0.9092 0.7820 0.7173 -0.1391 0.1788 -0.2396 277 LYS C CE 5861 N NZ . LYS C 278 ? 0.9773 0.8012 0.7401 -0.1353 0.2210 -0.2603 277 LYS C NZ 5862 N N . CYS C 279 ? 0.5674 0.6812 0.6957 -0.0240 0.1403 -0.2096 278 CYS C N 5863 C CA . CYS C 279 ? 0.5360 0.6613 0.6890 -0.0206 0.1217 -0.1969 278 CYS C CA 5864 C C . CYS C 279 ? 0.4996 0.6520 0.6895 0.0002 0.1247 -0.1970 278 CYS C C 5865 O O . CYS C 279 ? 0.5161 0.6621 0.7105 0.0156 0.1322 -0.2045 278 CYS C O 5866 C CB . CYS C 279 ? 0.5719 0.6593 0.6997 -0.0259 0.1124 -0.1948 278 CYS C CB 5867 S SG . CYS C 279 ? 0.5602 0.6527 0.7167 -0.0220 0.0979 -0.1814 278 CYS C SG 5868 N N . GLN C 280 ? 0.4583 0.6345 0.6714 -0.0006 0.1175 -0.1877 279 GLN C N 5869 C CA . GLN C 280 ? 0.4277 0.6200 0.6637 0.0133 0.1157 -0.1858 279 GLN C CA 5870 C C . GLN C 280 ? 0.4143 0.5941 0.6502 0.0117 0.1079 -0.1758 279 GLN C C 5871 O O . GLN C 280 ? 0.3991 0.5773 0.6373 0.0000 0.1067 -0.1678 279 GLN C O 5872 C CB . GLN C 280 ? 0.4091 0.6324 0.6634 0.0117 0.1181 -0.1851 279 GLN C CB 5873 C CG . GLN C 280 ? 0.4199 0.6622 0.6948 0.0222 0.1272 -0.1939 279 GLN C CG 5874 C CD . GLN C 280 ? 0.4223 0.6640 0.7187 0.0398 0.1202 -0.1937 279 GLN C CD 5875 O OE1 . GLN C 280 ? 0.4302 0.6864 0.7554 0.0508 0.1279 -0.1997 279 GLN C OE1 5876 N NE2 . GLN C 280 ? 0.4213 0.6436 0.7058 0.0417 0.1063 -0.1862 279 GLN C NE2 5877 N N . THR C 281 ? 0.4186 0.5867 0.6535 0.0230 0.1039 -0.1755 280 THR C N 5878 C CA . THR C 281 ? 0.4203 0.5691 0.6464 0.0203 0.1012 -0.1673 280 THR C CA 5879 C C . THR C 281 ? 0.4207 0.5735 0.6472 0.0253 0.0937 -0.1651 280 THR C C 5880 O O . THR C 281 ? 0.4171 0.5933 0.6620 0.0324 0.0891 -0.1691 280 THR C O 5881 C CB . THR C 281 ? 0.4437 0.5586 0.6526 0.0238 0.0994 -0.1671 280 THR C CB 5882 O OG1 . THR C 281 ? 0.4619 0.5645 0.6639 0.0368 0.0902 -0.1697 280 THR C OG1 5883 C CG2 . THR C 281 ? 0.4510 0.5607 0.6571 0.0209 0.1010 -0.1713 280 THR C CG2 5884 N N . PRO C 282 ? 0.4374 0.5628 0.6426 0.0198 0.0929 -0.1582 281 PRO C N 5885 C CA . PRO C 282 ? 0.4558 0.5725 0.6495 0.0205 0.0796 -0.1544 281 PRO C CA 5886 C C . PRO C 282 ? 0.4814 0.5799 0.6701 0.0317 0.0615 -0.1545 281 PRO C C 5887 O O . PRO C 282 ? 0.4917 0.5827 0.6762 0.0318 0.0425 -0.1491 281 PRO C O 5888 C CB . PRO C 282 ? 0.4754 0.5530 0.6339 0.0077 0.0893 -0.1478 281 PRO C CB 5889 C CG . PRO C 282 ? 0.4589 0.5404 0.6307 0.0026 0.1097 -0.1477 281 PRO C CG 5890 C CD . PRO C 282 ? 0.4468 0.5432 0.6367 0.0105 0.1056 -0.1530 281 PRO C CD 5891 N N . ILE C 283 ? 0.4918 0.5808 0.6816 0.0398 0.0646 -0.1592 282 ILE C N 5892 C CA . ILE C 283 ? 0.5256 0.5913 0.7100 0.0513 0.0485 -0.1588 282 ILE C CA 5893 C C . ILE C 283 ? 0.5130 0.6093 0.7389 0.0677 0.0481 -0.1662 282 ILE C C 5894 O O . ILE C 283 ? 0.5424 0.6297 0.7822 0.0805 0.0326 -0.1647 282 ILE C O 5895 C CB . ILE C 283 ? 0.5588 0.5792 0.7063 0.0474 0.0548 -0.1585 282 ILE C CB 5896 C CG1 . ILE C 283 ? 0.6125 0.5811 0.7181 0.0436 0.0379 -0.1510 282 ILE C CG1 5897 C CG2 . ILE C 283 ? 0.5627 0.5840 0.7205 0.0579 0.0590 -0.1658 282 ILE C CG2 5898 C CD1 . ILE C 283 ? 0.6280 0.5734 0.7004 0.0269 0.0418 -0.1445 282 ILE C CD1 5899 N N . GLY C 284 ? 0.4828 0.6098 0.7274 0.0664 0.0660 -0.1737 283 GLY C N 5900 C CA . GLY C 284 ? 0.4734 0.6190 0.7473 0.0790 0.0758 -0.1831 283 GLY C CA 5901 C C . GLY C 284 ? 0.4626 0.6135 0.7241 0.0698 0.0957 -0.1908 283 GLY C C 5902 O O . GLY C 284 ? 0.4543 0.5927 0.6908 0.0563 0.0971 -0.1873 283 GLY C O 5903 N N . ALA C 285 ? 0.4677 0.6331 0.7473 0.0757 0.1111 -0.2004 284 ALA C N 5904 C CA . ALA C 285 ? 0.4748 0.6345 0.7311 0.0634 0.1279 -0.2077 284 ALA C CA 5905 C C . ALA C 285 ? 0.5077 0.6277 0.7314 0.0639 0.1329 -0.2133 284 ALA C C 5906 O O . ALA C 285 ? 0.5265 0.6288 0.7543 0.0785 0.1301 -0.2150 284 ALA C O 5907 C CB . ALA C 285 ? 0.4768 0.6593 0.7559 0.0659 0.1474 -0.2165 284 ALA C CB 5908 N N . ILE C 286 ? 0.5249 0.6271 0.7143 0.0464 0.1375 -0.2151 285 ILE C N 5909 C CA . ILE C 286 ? 0.5661 0.6245 0.7158 0.0408 0.1386 -0.2188 285 ILE C CA 5910 C C . ILE C 286 ? 0.6060 0.6393 0.7198 0.0290 0.1558 -0.2292 285 ILE C C 5911 O O . ILE C 286 ? 0.5996 0.6422 0.7042 0.0133 0.1568 -0.2278 285 ILE C O 5912 C CB . ILE C 286 ? 0.5595 0.6060 0.6940 0.0244 0.1205 -0.2071 285 ILE C CB 5913 C CG1 . ILE C 286 ? 0.5319 0.5938 0.6914 0.0321 0.1102 -0.1978 285 ILE C CG1 5914 C CG2 . ILE C 286 ? 0.6051 0.6057 0.7018 0.0181 0.1175 -0.2092 285 ILE C CG2 5915 C CD1 . ILE C 286 ? 0.5218 0.5764 0.6793 0.0166 0.1004 -0.1861 285 ILE C CD1 5916 N N . ASN C 287 ? 0.6524 0.6469 0.7404 0.0358 0.1701 -0.2396 286 ASN C N 5917 C CA . ASN C 287 ? 0.7130 0.6634 0.7488 0.0224 0.1900 -0.2509 286 ASN C CA 5918 C C . ASN C 287 ? 0.7646 0.6584 0.7494 0.0148 0.1835 -0.2521 286 ASN C C 5919 O O . ASN C 287 ? 0.7791 0.6529 0.7661 0.0328 0.1947 -0.2592 286 ASN C O 5920 C CB . ASN C 287 ? 0.7355 0.6883 0.7923 0.0402 0.2257 -0.2658 286 ASN C CB 5921 C CG . ASN C 287 ? 0.8103 0.7074 0.8030 0.0238 0.2546 -0.2795 286 ASN C CG 5922 O OD1 . ASN C 287 ? 0.8327 0.7095 0.7771 -0.0032 0.2466 -0.2767 286 ASN C OD1 5923 N ND2 . ASN C 287 ? 0.8606 0.7270 0.8505 0.0393 0.2890 -0.2940 286 ASN C ND2 5924 N N . SER C 288 ? 0.7882 0.6557 0.7304 -0.0125 0.1627 -0.2437 287 SER C N 5925 C CA . SER C 288 ? 0.8301 0.6520 0.7331 -0.0238 0.1464 -0.2394 287 SER C CA 5926 C C . SER C 288 ? 0.8826 0.6614 0.7275 -0.0591 0.1278 -0.2326 287 SER C C 5927 O O . SER C 288 ? 0.8637 0.6645 0.7188 -0.0745 0.1138 -0.2234 287 SER C O 5928 C CB . SER C 288 ? 0.7765 0.6321 0.7257 -0.0164 0.1239 -0.2256 287 SER C CB 5929 O OG . SER C 288 ? 0.8069 0.6229 0.7259 -0.0282 0.1083 -0.2202 287 SER C OG 5930 N N . SER C 289 ? 0.9612 0.6743 0.7431 -0.0731 0.1247 -0.2360 288 SER C N 5931 C CA . SER C 289 ? 1.0187 0.6829 0.7428 -0.1106 0.0965 -0.2254 288 SER C CA 5932 C C . SER C 289 ? 1.0027 0.6706 0.7488 -0.1214 0.0614 -0.2076 288 SER C C 5933 O O . SER C 289 ? 1.0608 0.6850 0.7653 -0.1531 0.0322 -0.1961 288 SER C O 5934 C CB . SER C 289 ? 1.1242 0.6993 0.7500 -0.1266 0.1146 -0.2399 288 SER C CB 5935 O OG . SER C 289 ? 1.1582 0.6969 0.7624 -0.1160 0.1231 -0.2469 288 SER C OG 5936 N N . MET C 290 ? 0.9384 0.6545 0.7488 -0.0975 0.0637 -0.2042 289 MET C N 5937 C CA . MET C 290 ? 0.9168 0.6400 0.7566 -0.1060 0.0383 -0.1882 289 MET C CA 5938 C C . MET C 290 ? 0.8656 0.6284 0.7565 -0.1230 0.0126 -0.1682 289 MET C C 5939 O O . MET C 290 ? 0.8289 0.6275 0.7448 -0.1186 0.0180 -0.1680 289 MET C O 5940 C CB . MET C 290 ? 0.8722 0.6283 0.7581 -0.0769 0.0522 -0.1914 289 MET C CB 5941 C CG . MET C 290 ? 0.9126 0.6352 0.7649 -0.0559 0.0746 -0.2083 289 MET C CG 5942 S SD . MET C 290 ? 1.0005 0.6473 0.7868 -0.0737 0.0632 -0.2085 289 MET C SD 5943 C CE . MET C 290 ? 0.9967 0.6379 0.7916 -0.0379 0.0853 -0.2211 289 MET C CE 5944 N N . PRO C 291 ? 0.8627 0.6194 0.7747 -0.1421 -0.0145 -0.1505 290 PRO C N 5945 C CA . PRO C 291 ? 0.8190 0.6165 0.7978 -0.1553 -0.0367 -0.1294 290 PRO C CA 5946 C C . PRO C 291 ? 0.7450 0.6010 0.8010 -0.1328 -0.0193 -0.1258 290 PRO C C 5947 O O . PRO C 291 ? 0.7055 0.6014 0.8166 -0.1346 -0.0238 -0.1144 290 PRO C O 5948 C CB . PRO C 291 ? 0.8603 0.6238 0.8359 -0.1848 -0.0706 -0.1117 290 PRO C CB 5949 C CG . PRO C 291 ? 0.8936 0.6192 0.8259 -0.1768 -0.0578 -0.1237 290 PRO C CG 5950 C CD . PRO C 291 ? 0.9134 0.6197 0.7878 -0.1553 -0.0268 -0.1483 290 PRO C CD 5951 N N . PHE C 292 ? 0.7353 0.5890 0.7890 -0.1132 0.0003 -0.1354 291 PHE C N 5952 C CA . PHE C 292 ? 0.6842 0.5760 0.7920 -0.0955 0.0177 -0.1329 291 PHE C CA 5953 C C . PHE C 292 ? 0.6708 0.5695 0.7598 -0.0673 0.0416 -0.1501 291 PHE C C 5954 O O . PHE C 292 ? 0.7021 0.5763 0.7454 -0.0588 0.0476 -0.1640 291 PHE C O 5955 C CB . PHE C 292 ? 0.6915 0.5685 0.8179 -0.1021 0.0154 -0.1241 291 PHE C CB 5956 C CG . PHE C 292 ? 0.6984 0.5748 0.8636 -0.1297 -0.0095 -0.1035 291 PHE C CG 5957 C CD1 . PHE C 292 ? 0.6602 0.5759 0.8958 -0.1367 -0.0143 -0.0877 291 PHE C CD1 5958 C CD2 . PHE C 292 ? 0.7478 0.5828 0.8836 -0.1493 -0.0298 -0.0984 291 PHE C CD2 5959 C CE1 . PHE C 292 ? 0.6661 0.5844 0.9524 -0.1616 -0.0406 -0.0657 291 PHE C CE1 5960 C CE2 . PHE C 292 ? 0.7548 0.5903 0.9348 -0.1769 -0.0584 -0.0763 291 PHE C CE2 5961 C CZ . PHE C 292 ? 0.7151 0.5946 0.9756 -0.1825 -0.0646 -0.0592 291 PHE C CZ 5962 N N . HIS C 293 ? 0.6352 0.5631 0.7611 -0.0543 0.0551 -0.1480 292 HIS C N 5963 C CA . HIS C 293 ? 0.6341 0.5653 0.7477 -0.0305 0.0707 -0.1596 292 HIS C CA 5964 C C . HIS C 293 ? 0.6115 0.5502 0.7508 -0.0262 0.0813 -0.1532 292 HIS C C 5965 O O . HIS C 293 ? 0.5954 0.5482 0.7721 -0.0384 0.0835 -0.1414 292 HIS C O 5966 C CB . HIS C 293 ? 0.6208 0.5794 0.7368 -0.0201 0.0764 -0.1673 292 HIS C CB 5967 C CG . HIS C 293 ? 0.5852 0.5807 0.7402 -0.0245 0.0782 -0.1587 292 HIS C CG 5968 N ND1 . HIS C 293 ? 0.5596 0.5746 0.7297 -0.0119 0.0885 -0.1598 292 HIS C ND1 5969 C CD2 . HIS C 293 ? 0.5724 0.5840 0.7525 -0.0410 0.0695 -0.1481 292 HIS C CD2 5970 C CE1 . HIS C 293 ? 0.5305 0.5713 0.7308 -0.0195 0.0901 -0.1518 292 HIS C CE1 5971 N NE2 . HIS C 293 ? 0.5390 0.5805 0.7502 -0.0360 0.0786 -0.1442 292 HIS C NE2 5972 N N . ASN C 294 ? 0.6206 0.5445 0.7390 -0.0102 0.0883 -0.1601 293 ASN C N 5973 C CA . ASN C 294 ? 0.6221 0.5385 0.7464 -0.0088 0.0996 -0.1552 293 ASN C CA 5974 C C . ASN C 294 ? 0.6146 0.5386 0.7292 0.0062 0.1012 -0.1602 293 ASN C C 5975 O O . ASN C 294 ? 0.6423 0.5398 0.7357 0.0093 0.1050 -0.1591 293 ASN C O 5976 C CB . ASN C 294 ? 0.6624 0.5357 0.7612 -0.0120 0.1018 -0.1543 293 ASN C CB 5977 C CG . ASN C 294 ? 0.7022 0.5477 0.7609 0.0037 0.0930 -0.1640 293 ASN C CG 5978 O OD1 . ASN C 294 ? 0.7001 0.5603 0.7569 0.0174 0.0871 -0.1717 293 ASN C OD1 5979 N ND2 . ASN C 294 ? 0.7445 0.5479 0.7746 0.0018 0.0938 -0.1634 293 ASN C ND2 5980 N N . ILE C 295 ? 0.5898 0.5462 0.7177 0.0127 0.0972 -0.1645 294 ILE C N 5981 C CA . ILE C 295 ? 0.5800 0.5485 0.7066 0.0261 0.0944 -0.1681 294 ILE C CA 5982 C C . ILE C 295 ? 0.5627 0.5354 0.6951 0.0193 0.1020 -0.1610 294 ILE C C 5983 O O . ILE C 295 ? 0.5790 0.5248 0.6873 0.0217 0.1005 -0.1592 294 ILE C O 5984 C CB . ILE C 295 ? 0.5617 0.5644 0.7054 0.0327 0.0925 -0.1748 294 ILE C CB 5985 C CG1 . ILE C 295 ? 0.5888 0.5771 0.7187 0.0374 0.0918 -0.1833 294 ILE C CG1 5986 C CG2 . ILE C 295 ? 0.5549 0.5741 0.7087 0.0454 0.0877 -0.1764 294 ILE C CG2 5987 C CD1 . ILE C 295 ? 0.6262 0.5814 0.7367 0.0509 0.0874 -0.1872 294 ILE C CD1 5988 N N . HIS C 296 ? 0.5351 0.5352 0.6950 0.0096 0.1095 -0.1566 295 HIS C N 5989 C CA . HIS C 296 ? 0.5253 0.5286 0.6933 0.0030 0.1214 -0.1505 295 HIS C CA 5990 C C . HIS C 296 ? 0.4993 0.5241 0.7067 -0.0089 0.1297 -0.1430 295 HIS C C 5991 O O . HIS C 296 ? 0.4753 0.5212 0.6988 -0.0118 0.1189 -0.1434 295 HIS C O 5992 C CB . HIS C 296 ? 0.5144 0.5400 0.6816 0.0099 0.1144 -0.1534 295 HIS C CB 5993 C CG . HIS C 296 ? 0.5334 0.5399 0.6827 0.0048 0.1226 -0.1490 295 HIS C CG 5994 N ND1 . HIS C 296 ? 0.5167 0.5385 0.6831 -0.0028 0.1351 -0.1446 295 HIS C ND1 5995 C CD2 . HIS C 296 ? 0.5755 0.5407 0.6839 0.0044 0.1193 -0.1478 295 HIS C CD2 5996 C CE1 . HIS C 296 ? 0.5441 0.5330 0.6783 -0.0078 0.1428 -0.1421 295 HIS C CE1 5997 N NE2 . HIS C 296 ? 0.5862 0.5384 0.6815 -0.0050 0.1320 -0.1436 295 HIS C NE2 5998 N N . PRO C 297 ? 0.4980 0.5121 0.7206 -0.0170 0.1489 -0.1355 296 PRO C N 5999 C CA . PRO C 297 ? 0.4744 0.5122 0.7488 -0.0268 0.1549 -0.1258 296 PRO C CA 6000 C C . PRO C 297 ? 0.4446 0.5168 0.7361 -0.0262 0.1485 -0.1250 296 PRO C C 6001 O O . PRO C 297 ? 0.4334 0.5286 0.7600 -0.0333 0.1385 -0.1183 296 PRO C O 6002 C CB . PRO C 297 ? 0.4926 0.5040 0.7792 -0.0328 0.1848 -0.1195 296 PRO C CB 6003 C CG . PRO C 297 ? 0.5251 0.4999 0.7523 -0.0281 0.1926 -0.1269 296 PRO C CG 6004 C CD . PRO C 297 ? 0.5335 0.5049 0.7258 -0.0193 0.1676 -0.1348 296 PRO C CD 6005 N N . LEU C 298 ? 0.4431 0.5147 0.7084 -0.0201 0.1517 -0.1304 297 LEU C N 6006 C CA . LEU C 298 ? 0.4170 0.5179 0.6948 -0.0207 0.1478 -0.1298 297 LEU C CA 6007 C C . LEU C 298 ? 0.3975 0.5219 0.6644 -0.0159 0.1284 -0.1376 297 LEU C C 6008 O O . LEU C 298 ? 0.4107 0.5328 0.6527 -0.0071 0.1230 -0.1453 297 LEU C O 6009 C CB . LEU C 298 ? 0.4340 0.5194 0.6871 -0.0195 0.1602 -0.1310 297 LEU C CB 6010 C CG . LEU C 298 ? 0.4575 0.5197 0.7235 -0.0265 0.1879 -0.1236 297 LEU C CG 6011 C CD1 . LEU C 298 ? 0.4894 0.5161 0.7544 -0.0297 0.2061 -0.1211 297 LEU C CD1 6012 C CD2 . LEU C 298 ? 0.4877 0.5258 0.7128 -0.0281 0.1971 -0.1259 297 LEU C CD2 6013 N N . THR C 299 ? 0.3747 0.5173 0.6607 -0.0228 0.1182 -0.1349 298 THR C N 6014 C CA . THR C 299 ? 0.3706 0.5267 0.6399 -0.0213 0.1068 -0.1433 298 THR C CA 6015 C C . THR C 299 ? 0.3537 0.5304 0.6351 -0.0307 0.1016 -0.1396 298 THR C C 6016 O O . THR C 299 ? 0.3468 0.5284 0.6561 -0.0383 0.1024 -0.1286 298 THR C O 6017 C CB . THR C 299 ? 0.3865 0.5257 0.6418 -0.0245 0.0972 -0.1462 298 THR C CB 6018 O OG1 . THR C 299 ? 0.3833 0.5186 0.6597 -0.0397 0.0872 -0.1345 298 THR C OG1 6019 C CG2 . THR C 299 ? 0.4050 0.5207 0.6462 -0.0156 0.1012 -0.1497 298 THR C CG2 6020 N N . ILE C 300 ? 0.3547 0.5404 0.6164 -0.0305 0.0982 -0.1485 299 ILE C N 6021 C CA . ILE C 300 ? 0.3560 0.5507 0.6158 -0.0431 0.0913 -0.1460 299 ILE C CA 6022 C C . ILE C 300 ? 0.3878 0.5681 0.6128 -0.0482 0.0888 -0.1560 299 ILE C C 6023 O O . ILE C 300 ? 0.3978 0.5737 0.6088 -0.0367 0.0983 -0.1675 299 ILE C O 6024 C CB . ILE C 300 ? 0.3332 0.5506 0.5998 -0.0411 0.0984 -0.1469 299 ILE C CB 6025 C CG1 . ILE C 300 ? 0.3354 0.5572 0.6025 -0.0563 0.0897 -0.1406 299 ILE C CG1 6026 C CG2 . ILE C 300 ? 0.3357 0.5649 0.5893 -0.0308 0.1066 -0.1596 299 ILE C CG2 6027 C CD1 . ILE C 300 ? 0.3216 0.5626 0.5959 -0.0562 0.0962 -0.1397 299 ILE C CD1 6028 N N . GLY C 301 ? 0.4098 0.5770 0.6194 -0.0662 0.0764 -0.1509 300 GLY C N 6029 C CA . GLY C 301 ? 0.4629 0.6019 0.6249 -0.0765 0.0765 -0.1603 300 GLY C CA 6030 C C . GLY C 301 ? 0.5032 0.6052 0.6443 -0.0914 0.0575 -0.1532 300 GLY C C 6031 O O . GLY C 301 ? 0.4997 0.6053 0.6745 -0.0946 0.0425 -0.1390 300 GLY C O 6032 N N . GLU C 302 ? 1.6187 0.7932 0.6360 -0.4906 0.1545 -0.2047 301 GLU C N 6033 C CA . GLU C 302 ? 1.6699 0.8032 0.6245 -0.5098 0.1324 -0.1931 301 GLU C CA 6034 C C . GLU C 302 ? 1.5493 0.7751 0.6438 -0.4509 0.1517 -0.2115 301 GLU C C 6035 O O . GLU C 302 ? 1.5606 0.7987 0.6869 -0.4670 0.2179 -0.2588 301 GLU C O 6036 C CB . GLU C 302 ? 1.8436 0.8668 0.6393 -0.6036 0.1842 -0.2234 301 GLU C CB 6037 C CG . GLU C 302 ? 2.0070 0.9045 0.6220 -0.6748 0.1539 -0.1983 301 GLU C CG 6038 N N . CYS C 303 ? 1.4461 0.7303 0.6261 -0.3859 0.0958 -0.1767 302 CYS C N 6039 C CA . CYS C 303 ? 1.3450 0.7038 0.6431 -0.3302 0.1057 -0.1871 302 CYS C CA 6040 C C . CYS C 303 ? 1.3430 0.6857 0.6205 -0.3268 0.0695 -0.1646 302 CYS C C 6041 O O . CYS C 303 ? 1.3988 0.6862 0.6008 -0.3511 0.0177 -0.1331 302 CYS C O 6042 C CB . CYS C 303 ? 1.2458 0.6731 0.6494 -0.2636 0.0801 -0.1699 302 CYS C CB 6043 S SG . CYS C 303 ? 1.2359 0.6937 0.6938 -0.2548 0.1135 -0.1970 302 CYS C SG 6044 N N . PRO C 304 ? 1.2772 0.6641 0.6294 -0.2966 0.0910 -0.1811 303 PRO C N 6045 C CA . PRO C 304 ? 1.2580 0.6461 0.6213 -0.2788 0.0551 -0.1580 303 PRO C CA 6046 C C . PRO C 304 ? 1.1773 0.6043 0.6113 -0.2262 0.0114 -0.1254 303 PRO C C 6047 O O . PRO C 304 ? 1.1345 0.5896 0.6058 -0.2015 0.0115 -0.1220 303 PRO C O 6048 C CB . PRO C 304 ? 1.2192 0.6429 0.6470 -0.2616 0.0975 -0.1890 303 PRO C CB 6049 C CG . PRO C 304 ? 1.2159 0.6588 0.6836 -0.2683 0.1507 -0.2305 303 PRO C CG 6050 C CD . PRO C 304 ? 1.2264 0.6616 0.6694 -0.2757 0.1430 -0.2221 303 PRO C CD 6051 N N . LYS C 305 ? 1.1624 0.5888 0.6199 -0.2121 -0.0201 -0.1064 304 LYS C N 6052 C CA . LYS C 305 ? 1.0977 0.5542 0.6292 -0.1703 -0.0489 -0.0843 304 LYS C CA 6053 C C . LYS C 305 ? 1.0204 0.5227 0.6203 -0.1261 -0.0175 -0.0943 304 LYS C C 6054 O O . LYS C 305 ? 1.0185 0.5270 0.6281 -0.1224 0.0055 -0.1085 304 LYS C O 6055 C CB . LYS C 305 ? 1.1232 0.5550 0.6693 -0.1774 -0.0942 -0.0661 304 LYS C CB 6056 C CG . LYS C 305 ? 1.2181 0.5827 0.6882 -0.2234 -0.1475 -0.0496 304 LYS C CG 6057 C CD . LYS C 305 ? 1.2221 0.5786 0.6931 -0.2228 -0.1770 -0.0338 304 LYS C CD 6058 C CE . LYS C 305 ? 1.3254 0.6017 0.7337 -0.2649 -0.2516 -0.0103 304 LYS C CE 6059 N NZ . LYS C 305 ? 1.3408 0.6009 0.7455 -0.2682 -0.2849 0.0059 304 LYS C NZ 6060 N N . TYR C 306 ? 0.9747 0.4983 0.6135 -0.0965 -0.0203 -0.0861 305 TYR C N 6061 C CA . TYR C 306 ? 0.9350 0.4775 0.6103 -0.0616 0.0012 -0.0918 305 TYR C CA 6062 C C . TYR C 306 ? 0.9272 0.4657 0.6353 -0.0474 0.0035 -0.0845 305 TYR C C 6063 O O . TYR C 306 ? 0.9261 0.4608 0.6632 -0.0521 -0.0138 -0.0748 305 TYR C O 6064 C CB . TYR C 306 ? 0.9092 0.4610 0.5941 -0.0425 -0.0014 -0.0875 305 TYR C CB 6065 C CG . TYR C 306 ? 0.8940 0.4406 0.5902 -0.0136 0.0104 -0.0891 305 TYR C CG 6066 C CD1 . TYR C 306 ? 0.8953 0.4387 0.5926 -0.0025 0.0155 -0.1027 305 TYR C CD1 6067 C CD2 . TYR C 306 ? 0.8948 0.4281 0.5999 -0.0021 0.0150 -0.0797 305 TYR C CD2 6068 C CE1 . TYR C 306 ? 0.9102 0.4266 0.5989 0.0189 0.0117 -0.0996 305 TYR C CE1 6069 C CE2 . TYR C 306 ? 0.9136 0.4177 0.5965 0.0137 0.0259 -0.0800 305 TYR C CE2 6070 C CZ . TYR C 306 ? 0.9274 0.4174 0.5926 0.0241 0.0177 -0.0862 305 TYR C CZ 6071 O OH . TYR C 306 ? 0.9682 0.4075 0.5929 0.0353 0.0148 -0.0819 305 TYR C OH 6072 N N . VAL C 307 ? 0.9290 0.4633 0.6400 -0.0322 0.0238 -0.0919 306 VAL C N 6073 C CA . VAL C 307 ? 0.9354 0.4551 0.6655 -0.0209 0.0374 -0.0881 306 VAL C CA 6074 C C . VAL C 307 ? 0.9558 0.4504 0.6602 -0.0022 0.0506 -0.0897 306 VAL C C 6075 O O . VAL C 307 ? 0.9600 0.4552 0.6530 0.0048 0.0419 -0.0960 306 VAL C O 6076 C CB . VAL C 307 ? 0.9426 0.4604 0.6869 -0.0323 0.0408 -0.0922 306 VAL C CB 6077 C CG1 . VAL C 307 ? 0.9484 0.4708 0.7106 -0.0536 0.0135 -0.0872 306 VAL C CG1 6078 C CG2 . VAL C 307 ? 0.9508 0.4698 0.6752 -0.0354 0.0485 -0.1048 306 VAL C CG2 6079 N N . LYS C 308 ? 0.9841 0.4470 0.6802 0.0015 0.0698 -0.0864 307 LYS C N 6080 C CA . LYS C 308 ? 1.0376 0.4483 0.6798 0.0110 0.0750 -0.0834 307 LYS C CA 6081 C C . LYS C 308 ? 1.0666 0.4504 0.6945 0.0124 0.0765 -0.0851 307 LYS C C 6082 O O . LYS C 308 ? 1.1320 0.4543 0.7047 0.0161 0.0719 -0.0793 307 LYS C O 6083 C CB . LYS C 308 ? 1.0788 0.4468 0.6928 0.0042 0.1032 -0.0819 307 LYS C CB 6084 C CG . LYS C 308 ? 1.0601 0.4476 0.6904 0.0045 0.1012 -0.0822 307 LYS C CG 6085 C CD . LYS C 308 ? 1.1242 0.4528 0.7077 -0.0057 0.1350 -0.0866 307 LYS C CD 6086 C CE . LYS C 308 ? 1.1057 0.4566 0.7152 -0.0048 0.1338 -0.0898 307 LYS C CE 6087 N NZ . LYS C 308 ? 1.1805 0.4656 0.7344 -0.0206 0.1738 -0.0994 307 LYS C NZ 6088 N N . SER C 309 ? 1.0376 0.4573 0.7071 0.0066 0.0781 -0.0922 308 SER C N 6089 C CA . SER C 309 ? 1.0552 0.4566 0.7246 0.0068 0.0821 -0.0962 308 SER C CA 6090 C C . SER C 309 ? 1.0761 0.4615 0.7427 0.0192 0.0570 -0.1016 308 SER C C 6091 O O . SER C 309 ? 1.0522 0.4693 0.7482 0.0229 0.0425 -0.1121 308 SER C O 6092 C CB . SER C 309 ? 1.0209 0.4646 0.7343 -0.0054 0.0870 -0.1055 308 SER C CB 6093 O OG . SER C 309 ? 1.0093 0.4697 0.7477 -0.0160 0.0931 -0.1022 308 SER C OG 6094 N N . SER C 310 ? 1.1318 0.4630 0.7712 0.0236 0.0507 -0.0967 309 SER C N 6095 C CA . SER C 310 ? 1.1504 0.4625 0.8140 0.0362 0.0172 -0.1047 309 SER C CA 6096 C C . SER C 310 ? 1.1067 0.4711 0.8443 0.0322 0.0280 -0.1276 309 SER C C 6097 O O . SER C 310 ? 1.0981 0.4792 0.8970 0.0390 0.0112 -0.1482 309 SER C O 6098 C CB . SER C 310 ? 1.2387 0.4578 0.8373 0.0380 -0.0024 -0.0886 309 SER C CB 6099 O OG . SER C 310 ? 1.2615 0.4588 0.8220 0.0229 0.0353 -0.0813 309 SER C OG 6100 N N . ARG C 311 ? 1.0884 0.4752 0.8271 0.0184 0.0574 -0.1282 310 ARG C N 6101 C CA . ARG C 311 ? 1.0673 0.4893 0.8569 0.0085 0.0706 -0.1497 310 ARG C CA 6102 C C . ARG C 311 ? 1.0426 0.4943 0.8253 -0.0112 0.0933 -0.1488 310 ARG C C 6103 O O . ARG C 311 ? 1.0500 0.4865 0.8112 -0.0127 0.1017 -0.1331 310 ARG C O 6104 C CB . ARG C 311 ? 1.1069 0.4906 0.9092 0.0164 0.0623 -0.1510 310 ARG C CB 6105 C CG . ARG C 311 ? 1.0916 0.5075 0.9495 0.0054 0.0798 -0.1764 310 ARG C CG 6106 C CD . ARG C 311 ? 1.1258 0.5127 1.0355 0.0192 0.0573 -0.1888 310 ARG C CD 6107 N NE . ARG C 311 ? 1.1089 0.5271 1.0827 0.0073 0.0794 -0.2196 310 ARG C NE 6108 C CZ . ARG C 311 ? 1.1180 0.5312 1.0820 -0.0008 0.0963 -0.2169 310 ARG C CZ 6109 N NH1 . ARG C 311 ? 1.1388 0.5189 1.0398 0.0006 0.0979 -0.1872 310 ARG C NH1 6110 N NH2 . ARG C 311 ? 1.1124 0.5517 1.1344 -0.0138 0.1171 -0.2488 310 ARG C NH2 6111 N N . LEU C 312 ? 1.0320 0.5170 0.8344 -0.0304 0.1026 -0.1688 311 LEU C N 6112 C CA . LEU C 312 ? 1.0311 0.5284 0.8176 -0.0543 0.1089 -0.1673 311 LEU C CA 6113 C C . LEU C 312 ? 1.0488 0.5548 0.8439 -0.0790 0.1246 -0.1948 311 LEU C C 6114 O O . LEU C 312 ? 1.0598 0.5742 0.8491 -0.0980 0.1357 -0.2160 311 LEU C O 6115 C CB . LEU C 312 ? 1.0290 0.5354 0.7884 -0.0652 0.0962 -0.1569 311 LEU C CB 6116 C CG . LEU C 312 ? 1.0357 0.5384 0.7899 -0.0765 0.0804 -0.1407 311 LEU C CG 6117 C CD1 . LEU C 312 ? 1.0276 0.5200 0.8119 -0.0580 0.0877 -0.1291 311 LEU C CD1 6118 C CD2 . LEU C 312 ? 1.0317 0.5381 0.7661 -0.0839 0.0608 -0.1307 311 LEU C CD2 6119 N N . VAL C 313 ? 1.0565 0.5558 0.8644 -0.0824 0.1317 -0.1981 312 VAL C N 6120 C CA . VAL C 313 ? 1.0795 0.5809 0.8936 -0.1082 0.1513 -0.2272 312 VAL C CA 6121 C C . VAL C 313 ? 1.0964 0.5863 0.8892 -0.1265 0.1451 -0.2202 312 VAL C C 6122 O O . VAL C 313 ? 1.0780 0.5639 0.8956 -0.1085 0.1403 -0.2057 312 VAL C O 6123 C CB . VAL C 313 ? 1.0762 0.5792 0.9527 -0.0907 0.1640 -0.2476 312 VAL C CB 6124 C CG1 . VAL C 313 ? 1.1050 0.6111 0.9978 -0.1202 0.1925 -0.2838 312 VAL C CG1 6125 C CG2 . VAL C 313 ? 1.0660 0.5745 0.9826 -0.0720 0.1579 -0.2576 312 VAL C CG2 6126 N N . LEU C 314 ? 1.1406 0.6154 0.8822 -0.1665 0.1447 -0.2320 313 LEU C N 6127 C CA . LEU C 314 ? 1.1749 0.6276 0.8911 -0.1890 0.1267 -0.2266 313 LEU C CA 6128 C C . LEU C 314 ? 1.2028 0.6509 0.9301 -0.2044 0.1544 -0.2548 313 LEU C C 6129 O O . LEU C 314 ? 1.2240 0.6739 0.9518 -0.2207 0.1895 -0.2874 313 LEU C O 6130 C CB . LEU C 314 ? 1.2388 0.6530 0.8701 -0.2318 0.0990 -0.2212 313 LEU C CB 6131 C CG . LEU C 314 ? 1.2303 0.6387 0.8621 -0.2218 0.0518 -0.1890 313 LEU C CG 6132 C CD1 . LEU C 314 ? 1.3116 0.6690 0.8451 -0.2678 0.0221 -0.1846 313 LEU C CD1 6133 C CD2 . LEU C 314 ? 1.2142 0.6222 0.9036 -0.2079 0.0202 -0.1737 313 LEU C CD2 6134 N N . ALA C 315 ? 1.2016 0.6438 0.9495 -0.2007 0.1414 -0.2469 314 ALA C N 6135 C CA . ALA C 315 ? 1.2308 0.6648 0.9847 -0.2187 0.1634 -0.2724 314 ALA C CA 6136 C C . ALA C 315 ? 1.3231 0.7103 0.9838 -0.2748 0.1536 -0.2854 314 ALA C C 6137 O O . ALA C 315 ? 1.3597 0.7157 0.9664 -0.2924 0.1092 -0.2632 314 ALA C O 6138 C CB . ALA C 315 ? 1.2002 0.6415 1.0102 -0.1951 0.1539 -0.2595 314 ALA C CB 6139 N N . THR C 316 ? 1.3734 0.7463 1.0129 -0.3065 0.1934 -0.3230 315 THR C N 6140 C CA . THR C 316 ? 1.4891 0.7972 1.0160 -0.3707 0.1917 -0.3403 315 THR C CA 6141 C C . THR C 316 ? 1.5150 0.8147 1.0581 -0.3859 0.2145 -0.3667 315 THR C C 6142 O O . THR C 316 ? 1.5799 0.8328 1.0627 -0.4147 0.1799 -0.3586 315 THR C O 6143 C CB . THR C 316 ? 1.5594 0.8371 1.0109 -0.4170 0.2353 -0.3724 315 THR C CB 6144 O OG1 . THR C 316 ? 1.5012 0.8322 1.0550 -0.3917 0.2916 -0.4061 315 THR C OG1 6145 C CG2 . THR C 316 ? 1.5722 0.8308 0.9636 -0.4208 0.1990 -0.3424 315 THR C CG2 6146 N N . GLY C 317 ? 1.4707 0.8121 1.1025 -0.3660 0.2661 -0.3983 316 GLY C N 6147 C CA . GLY C 317 ? 1.4815 0.8244 1.1528 -0.3727 0.2910 -0.4250 316 GLY C CA 6148 C C . GLY C 317 ? 1.4167 0.7889 1.1650 -0.3252 0.2583 -0.3944 316 GLY C C 6149 O O . GLY C 317 ? 1.3894 0.7657 1.1392 -0.3013 0.2133 -0.3546 316 GLY C O 6150 N N . LEU C 318 ? 1.4019 0.7918 1.2210 -0.3143 0.2856 -0.4171 317 LEU C N 6151 C CA . LEU C 318 ? 1.3595 0.7657 1.2421 -0.2793 0.2644 -0.3947 317 LEU C CA 6152 C C . LEU C 318 ? 1.2894 0.7304 1.2730 -0.2305 0.2787 -0.3915 317 LEU C C 6153 O O . LEU C 318 ? 1.2714 0.7265 1.2879 -0.2211 0.2968 -0.4071 317 LEU C O 6154 C CB . LEU C 318 ? 1.4142 0.7979 1.2848 -0.3102 0.2756 -0.4197 317 LEU C CB 6155 C CG . LEU C 318 ? 1.5199 0.8440 1.2698 -0.3697 0.2560 -0.4273 317 LEU C CG 6156 C CD1 . LEU C 318 ? 1.6040 0.8938 1.2748 -0.4242 0.3031 -0.4704 317 LEU C CD1 6157 C CD2 . LEU C 318 ? 1.5497 0.8543 1.3056 -0.3830 0.2438 -0.4343 317 LEU C CD2 6158 N N . ARG C 319 ? 1.2584 0.7033 1.2890 -0.2033 0.2674 -0.3725 318 ARG C N 6159 C CA . ARG C 319 ? 1.2232 0.6759 1.3266 -0.1643 0.2727 -0.3654 318 ARG C CA 6160 C C . ARG C 319 ? 1.2338 0.6933 1.4034 -0.1685 0.3000 -0.4064 318 ARG C C 6161 O O . ARG C 319 ? 1.2626 0.7223 1.4234 -0.2044 0.3265 -0.4441 318 ARG C O 6162 C CB . ARG C 319 ? 1.2081 0.6491 1.3326 -0.1463 0.2633 -0.3413 318 ARG C CB 6163 C CG . ARG C 319 ? 1.1942 0.6295 1.2911 -0.1393 0.2437 -0.3086 318 ARG C CG 6164 C CD . ARG C 319 ? 1.1897 0.6105 1.3233 -0.1276 0.2494 -0.2964 318 ARG C CD 6165 N NE . ARG C 319 ? 1.1788 0.5968 1.3153 -0.1265 0.2387 -0.2776 318 ARG C NE 6166 C CZ . ARG C 319 ? 1.1740 0.5782 1.3054 -0.1104 0.2455 -0.2570 318 ARG C CZ 6167 N NH1 . ARG C 319 ? 1.1818 0.5643 1.2855 -0.0938 0.2542 -0.2457 318 ARG C NH1 6168 N NH2 . ARG C 319 ? 1.1655 0.5713 1.3241 -0.1134 0.2413 -0.2502 318 ARG C NH2 6169 N N . ASN C 320 ? 1.2191 0.6746 1.4543 -0.1350 0.2907 -0.4003 319 ASN C N 6170 C CA . ASN C 320 ? 1.2285 0.6880 1.5596 -0.1315 0.3051 -0.4383 319 ASN C CA 6171 C C . ASN C 320 ? 1.2299 0.6623 1.6070 -0.1023 0.2832 -0.4178 319 ASN C C 6172 O O . ASN C 320 ? 1.2361 0.6687 1.6659 -0.1087 0.2973 -0.4409 319 ASN C O 6173 C CB . ASN C 320 ? 1.2253 0.6956 1.6139 -0.1234 0.3040 -0.4606 319 ASN C CB 6174 C CG . ASN C 320 ? 1.2462 0.7385 1.6886 -0.1596 0.3527 -0.5256 319 ASN C CG 6175 O OD1 . ASN C 320 ? 1.2718 0.7656 1.7333 -0.1846 0.3843 -0.5583 319 ASN C OD1 6176 N ND2 . ASN C 320 ? 1.2437 0.7488 1.7127 -0.1660 0.3647 -0.5490 319 ASN C ND2 6177 N N . ILE D 10 ? 1.9564 1.8666 2.4337 -0.4907 0.9870 -0.6896 10 ILE D N 6178 C CA . ILE D 10 ? 1.9463 1.8870 2.4135 -0.4627 0.9588 -0.6598 10 ILE D CA 6179 C C . ILE D 10 ? 2.0087 1.8918 2.4116 -0.4053 0.9706 -0.6330 10 ILE D C 6180 O O . ILE D 10 ? 2.0219 1.8848 2.4058 -0.3855 0.9588 -0.6285 10 ILE D O 6181 C CB . ILE D 10 ? 1.8683 1.8987 2.3860 -0.4727 0.8881 -0.6458 10 ILE D CB 6182 C CG1 . ILE D 10 ? 1.8129 1.9128 2.3877 -0.5154 0.8763 -0.6637 10 ILE D CG1 6183 C CG2 . ILE D 10 ? 1.8599 1.9234 2.3741 -0.4484 0.8650 -0.6224 10 ILE D CG2 6184 C CD1 . ILE D 10 ? 1.7874 1.9488 2.3864 -0.5270 0.8755 -0.6642 10 ILE D CD1 6185 N N . GLU D 11 ? 2.0497 1.9156 2.4179 -0.3738 0.9942 -0.6155 11 GLU D N 6186 C CA . GLU D 11 ? 2.1153 1.9462 2.4162 -0.3063 1.0068 -0.5867 11 GLU D CA 6187 C C . GLU D 11 ? 2.0688 1.9842 2.3852 -0.2848 0.9332 -0.5770 11 GLU D C 6188 O O . GLU D 11 ? 2.0893 2.0095 2.3794 -0.2486 0.9169 -0.5734 11 GLU D O 6189 C CB . GLU D 11 ? 2.1765 1.9669 2.4364 -0.2758 1.0596 -0.5695 11 GLU D CB 6190 N N . GLY D 12 ? 2.0102 1.9965 2.3743 -0.3077 0.8929 -0.5775 12 GLY D N 6191 C CA . GLY D 12 ? 1.9667 2.0361 2.3637 -0.2965 0.8310 -0.5773 12 GLY D CA 6192 C C . GLY D 12 ? 1.9014 2.0359 2.3637 -0.3335 0.7987 -0.5775 12 GLY D C 6193 O O . GLY D 12 ? 1.8801 2.0081 2.3645 -0.3696 0.8156 -0.5791 12 GLY D O 6194 N N . GLY D 13 ? 1.8726 2.0775 2.3692 -0.3229 0.7553 -0.5798 13 GLY D N 6195 C CA . GLY D 13 ? 1.8168 2.0823 2.3795 -0.3531 0.7287 -0.5766 13 GLY D CA 6196 C C . GLY D 13 ? 1.8334 2.1145 2.3713 -0.3314 0.7376 -0.5629 13 GLY D C 6197 O O . GLY D 13 ? 1.8860 2.1530 2.3624 -0.2829 0.7523 -0.5574 13 GLY D O 6198 N N . TRP D 14 ? 1.7931 2.1070 2.3762 -0.3616 0.7307 -0.5545 14 TRP D N 6199 C CA . TRP D 14 ? 1.8027 2.1355 2.3699 -0.3464 0.7372 -0.5417 14 TRP D CA 6200 C C . TRP D 14 ? 1.7728 2.1806 2.3886 -0.3396 0.6994 -0.5446 14 TRP D C 6201 O O . TRP D 14 ? 1.7235 2.1720 2.4137 -0.3716 0.6787 -0.5459 14 TRP D O 6202 C CB . TRP D 14 ? 1.7776 2.1134 2.3660 -0.3807 0.7538 -0.5345 14 TRP D CB 6203 C CG . TRP D 14 ? 1.8040 2.0837 2.3633 -0.3968 0.7941 -0.5457 14 TRP D CG 6204 C CD1 . TRP D 14 ? 1.8662 2.0711 2.3662 -0.3760 0.8334 -0.5523 14 TRP D CD1 6205 C CD2 . TRP D 14 ? 1.7741 2.0765 2.3667 -0.4351 0.8045 -0.5561 14 TRP D CD2 6206 N NE1 . TRP D 14 ? 1.8749 2.0484 2.3776 -0.4068 0.8700 -0.5716 14 TRP D NE1 6207 C CE2 . TRP D 14 ? 1.8167 2.0585 2.3755 -0.4429 0.8496 -0.5780 14 TRP D CE2 6208 C CE3 . TRP D 14 ? 1.7204 2.0962 2.3685 -0.4587 0.7836 -0.5497 14 TRP D CE3 6209 C CZ2 . TRP D 14 ? 1.8018 2.0666 2.3863 -0.4783 0.8698 -0.6041 14 TRP D CZ2 6210 C CZ3 . TRP D 14 ? 1.7076 2.1112 2.3715 -0.4848 0.8013 -0.5682 14 TRP D CZ3 6211 C CH2 . TRP D 14 ? 1.7457 2.1000 2.3807 -0.4968 0.8418 -0.6003 14 TRP D CH2 6212 N N . GLN D 15 ? 1.8085 2.2371 2.3848 -0.2952 0.6962 -0.5462 15 GLN D N 6213 C CA . GLN D 15 ? 1.7847 2.2946 2.4090 -0.2890 0.6648 -0.5568 15 GLN D CA 6214 C C . GLN D 15 ? 1.7551 2.2821 2.4095 -0.3118 0.6676 -0.5376 15 GLN D C 6215 O O . GLN D 15 ? 1.7179 2.3045 2.4414 -0.3283 0.6460 -0.5439 15 GLN D O 6216 C CB . GLN D 15 ? 1.8343 2.3787 2.4012 -0.2271 0.6611 -0.5652 15 GLN D CB 6217 C CG . GLN D 15 ? 1.8562 2.4306 2.4139 -0.1986 0.6451 -0.5939 15 GLN D CG 6218 C CD . GLN D 15 ? 1.8903 2.5522 2.4192 -0.1374 0.6280 -0.6135 15 GLN D CD 6219 O OE1 . GLN D 15 ? 1.9159 2.5907 2.4025 -0.1032 0.6384 -0.5949 15 GLN D OE1 6220 N NE2 . GLN D 15 ? 1.8927 2.6252 2.4456 -0.1206 0.6020 -0.6550 15 GLN D NE2 6221 N N . GLY D 16 ? 1.7757 2.2520 2.3827 -0.3129 0.6990 -0.5180 16 GLY D N 6222 C CA . GLY D 16 ? 1.7520 2.2481 2.3802 -0.3313 0.7042 -0.5020 16 GLY D CA 6223 C C . GLY D 16 ? 1.6945 2.2325 2.4047 -0.3722 0.6870 -0.4964 16 GLY D C 6224 O O . GLY D 16 ? 1.6698 2.2525 2.4174 -0.3787 0.6786 -0.4845 16 GLY D O 6225 N N . MET D 17 ? 1.6790 2.2023 2.4156 -0.3947 0.6861 -0.5012 17 MET D N 6226 C CA . MET D 17 ? 1.6359 2.1956 2.4459 -0.4233 0.6785 -0.4883 17 MET D CA 6227 C C . MET D 17 ? 1.6203 2.2146 2.5011 -0.4273 0.6593 -0.4970 17 MET D C 6228 O O . MET D 17 ? 1.6310 2.2147 2.5185 -0.4244 0.6502 -0.5204 17 MET D O 6229 C CB . MET D 17 ? 1.6301 2.1653 2.4394 -0.4415 0.6893 -0.4894 17 MET D CB 6230 C CG . MET D 17 ? 1.5966 2.1763 2.4577 -0.4581 0.6931 -0.4662 17 MET D CG 6231 S SD . MET D 17 ? 1.5871 2.1583 2.4736 -0.4726 0.6976 -0.4652 17 MET D SD 6232 C CE . MET D 17 ? 1.6194 2.1276 2.4318 -0.4734 0.7084 -0.4980 17 MET D CE 6233 N N . VAL D 18 ? 1.5989 2.2369 2.5367 -0.4344 0.6576 -0.4823 18 VAL D N 6234 C CA . VAL D 18 ? 1.5864 2.2570 2.6126 -0.4462 0.6525 -0.4944 18 VAL D CA 6235 C C . VAL D 18 ? 1.5661 2.2521 2.6623 -0.4629 0.6725 -0.4594 18 VAL D C 6236 O O . VAL D 18 ? 1.5604 2.2725 2.7366 -0.4723 0.6817 -0.4605 18 VAL D O 6237 C CB . VAL D 18 ? 1.5915 2.3069 2.6305 -0.4326 0.6393 -0.5160 18 VAL D CB 6238 N N . ASP D 19 ? 1.5614 2.2367 2.6292 -0.4631 0.6840 -0.4301 19 ASP D N 6239 C CA . ASP D 19 ? 1.5511 2.2521 2.6686 -0.4639 0.7062 -0.3883 19 ASP D CA 6240 C C . ASP D 19 ? 1.5562 2.2371 2.7196 -0.4720 0.7220 -0.3803 19 ASP D C 6241 O O . ASP D 19 ? 1.5608 2.2455 2.8041 -0.4758 0.7465 -0.3623 19 ASP D O 6242 C CB . ASP D 19 ? 1.5442 2.2717 2.6061 -0.4527 0.7096 -0.3665 19 ASP D CB 6243 C CG . ASP D 19 ? 1.5437 2.2884 2.5647 -0.4454 0.7008 -0.3723 19 ASP D CG 6244 O OD1 . ASP D 19 ? 1.5419 2.3028 2.5982 -0.4429 0.6990 -0.3671 19 ASP D OD1 6245 O OD2 . ASP D 19 ? 1.5480 2.2899 2.5062 -0.4432 0.7001 -0.3849 19 ASP D OD2 6246 N N . GLY D 20 ? 1.5609 2.2163 2.6764 -0.4742 0.7142 -0.3938 20 GLY D N 6247 C CA . GLY D 20 ? 1.5674 2.2022 2.7161 -0.4799 0.7276 -0.3871 20 GLY D CA 6248 C C . GLY D 20 ? 1.5763 2.1691 2.6830 -0.4889 0.7102 -0.4257 20 GLY D C 6249 O O . GLY D 20 ? 1.5837 2.1615 2.6383 -0.4865 0.6916 -0.4554 20 GLY D O 6250 N N . TRP D 21 ? 1.5820 2.1555 2.7089 -0.4941 0.7202 -0.4214 21 TRP D N 6251 C CA . TRP D 21 ? 1.5921 2.1247 2.6850 -0.5019 0.7064 -0.4559 21 TRP D CA 6252 C C . TRP D 21 ? 1.5950 2.1182 2.6068 -0.4979 0.7015 -0.4621 21 TRP D C 6253 O O . TRP D 21 ? 1.6094 2.0979 2.5680 -0.4973 0.6912 -0.4916 21 TRP D O 6254 C CB . TRP D 21 ? 1.5973 2.1099 2.7490 -0.5111 0.7215 -0.4524 21 TRP D CB 6255 C CG . TRP D 21 ? 1.6052 2.1115 2.8376 -0.5247 0.7274 -0.4778 21 TRP D CG 6256 C CD1 . TRP D 21 ? 1.6088 2.1252 2.8441 -0.5286 0.7070 -0.5231 21 TRP D CD1 6257 C CD2 . TRP D 21 ? 1.6156 2.1116 2.9424 -0.5350 0.7611 -0.4660 21 TRP D CD2 6258 N NE1 . TRP D 21 ? 1.6159 2.1399 2.9478 -0.5458 0.7225 -0.5497 21 TRP D NE1 6259 C CE2 . TRP D 21 ? 1.6224 2.1247 3.0150 -0.5527 0.7599 -0.5150 21 TRP D CE2 6260 C CE3 . TRP D 21 ? 1.6260 2.1122 2.9898 -0.5271 0.7975 -0.4193 21 TRP D CE3 6261 C CZ2 . TRP D 21 ? 1.6394 2.1302 3.1430 -0.5713 0.7985 -0.5251 21 TRP D CZ2 6262 C CZ3 . TRP D 21 ? 1.6480 2.1122 3.1140 -0.5387 0.8389 -0.4175 21 TRP D CZ3 6263 C CH2 . TRP D 21 ? 1.6546 2.1169 3.1940 -0.5648 0.8413 -0.4732 21 TRP D CH2 6264 N N . TYR D 22 ? 1.5874 2.1474 2.5933 -0.4924 0.7139 -0.4368 22 TYR D N 6265 C CA . TYR D 22 ? 1.5907 2.1583 2.5353 -0.4939 0.7156 -0.4539 22 TYR D CA 6266 C C . TYR D 22 ? 1.5833 2.2077 2.5120 -0.4860 0.7208 -0.4444 22 TYR D C 6267 O O . TYR D 22 ? 1.5737 2.2465 2.5403 -0.4731 0.7257 -0.4104 22 TYR D O 6268 C CB . TYR D 22 ? 1.5870 2.1734 2.5393 -0.4937 0.7244 -0.4479 22 TYR D CB 6269 C CG . TYR D 22 ? 1.5913 2.1439 2.5898 -0.4960 0.7265 -0.4370 22 TYR D CG 6270 C CD1 . TYR D 22 ? 1.6023 2.0930 2.5888 -0.5086 0.7161 -0.4677 22 TYR D CD1 6271 C CD2 . TYR D 22 ? 1.5910 2.1745 2.6464 -0.4820 0.7448 -0.3953 22 TYR D CD2 6272 C CE1 . TYR D 22 ? 1.6068 2.0717 2.6420 -0.5136 0.7199 -0.4651 22 TYR D CE1 6273 C CE2 . TYR D 22 ? 1.6013 2.1472 2.7068 -0.4862 0.7560 -0.3879 22 TYR D CE2 6274 C CZ . TYR D 22 ? 1.6066 2.0953 2.7044 -0.5054 0.7415 -0.4268 22 TYR D CZ 6275 O OH . TYR D 22 ? 1.6170 2.0732 2.7705 -0.5124 0.7542 -0.4266 22 TYR D OH 6276 N N . GLY D 23 ? 1.5937 2.2112 2.4699 -0.4929 0.7255 -0.4753 23 GLY D N 6277 C CA . GLY D 23 ? 1.5889 2.2623 2.4521 -0.4889 0.7328 -0.4769 23 GLY D CA 6278 C C . GLY D 23 ? 1.6094 2.2636 2.4241 -0.5023 0.7501 -0.5209 23 GLY D C 6279 O O . GLY D 23 ? 1.6295 2.2256 2.4178 -0.5131 0.7603 -0.5478 23 GLY D O 6280 N N . TYR D 24 ? 1.6088 2.3095 2.4160 -0.5015 0.7593 -0.5291 24 TYR D N 6281 C CA . TYR D 24 ? 1.6338 2.3227 2.4087 -0.5174 0.7877 -0.5762 24 TYR D CA 6282 C C . TYR D 24 ? 1.6571 2.2976 2.4040 -0.5118 0.7978 -0.5745 24 TYR D C 6283 O O . TYR D 24 ? 1.6412 2.3023 2.4010 -0.4970 0.7789 -0.5416 24 TYR D O 6284 C CB . TYR D 24 ? 1.6164 2.4212 2.4117 -0.5225 0.7966 -0.6012 24 TYR D CB 6285 C CG . TYR D 24 ? 1.5921 2.4801 2.4160 -0.5132 0.7840 -0.5916 24 TYR D CG 6286 C CD1 . TYR D 24 ? 1.5698 2.5102 2.4226 -0.4853 0.7641 -0.5357 24 TYR D CD1 6287 C CD2 . TYR D 24 ? 1.5982 2.5146 2.4219 -0.5289 0.7984 -0.6377 24 TYR D CD2 6288 C CE1 . TYR D 24 ? 1.5575 2.5733 2.4319 -0.4668 0.7603 -0.5190 24 TYR D CE1 6289 C CE2 . TYR D 24 ? 1.5793 2.5817 2.4250 -0.5133 0.7874 -0.6270 24 TYR D CE2 6290 C CZ . TYR D 24 ? 1.5608 2.6118 2.4286 -0.4789 0.7691 -0.5642 24 TYR D CZ 6291 O OH . TYR D 24 ? 1.5516 2.6861 2.4367 -0.4539 0.7656 -0.5458 24 TYR D OH 6292 N N . HIS D 25 ? 1.7007 2.2749 2.4111 -0.5214 0.8336 -0.6090 25 HIS D N 6293 C CA . HIS D 25 ? 1.7343 2.2671 2.4148 -0.5130 0.8564 -0.6108 25 HIS D CA 6294 C C . HIS D 25 ? 1.7579 2.3123 2.4413 -0.5364 0.9019 -0.6623 25 HIS D C 6295 O O . HIS D 25 ? 1.7992 2.2965 2.4693 -0.5522 0.9447 -0.7003 25 HIS D O 6296 C CB . HIS D 25 ? 1.7837 2.2067 2.4155 -0.4930 0.8722 -0.6008 25 HIS D CB 6297 C CG . HIS D 25 ? 1.8347 2.2040 2.4275 -0.4792 0.9124 -0.6050 25 HIS D CG 6298 N ND1 . HIS D 25 ? 1.8272 2.2193 2.4151 -0.4602 0.8971 -0.5796 25 HIS D ND1 6299 C CD2 . HIS D 25 ? 1.8996 2.1899 2.4590 -0.4802 0.9746 -0.6304 25 HIS D CD2 6300 C CE1 . HIS D 25 ? 1.8844 2.2157 2.4334 -0.4474 0.9451 -0.5869 25 HIS D CE1 6301 N NE2 . HIS D 25 ? 1.9326 2.1974 2.4649 -0.4587 0.9965 -0.6165 25 HIS D NE2 6302 N N . HIS D 26 ? 1.7359 2.3754 2.4422 -0.5395 0.8968 -0.6677 26 HIS D N 6303 C CA . HIS D 26 ? 1.7543 2.4388 2.4767 -0.5650 0.9390 -0.7281 26 HIS D CA 6304 C C . HIS D 26 ? 1.8072 2.4111 2.5012 -0.5635 0.9856 -0.7384 26 HIS D C 6305 O O . HIS D 26 ? 1.8112 2.3796 2.4798 -0.5373 0.9696 -0.6931 26 HIS D O 6306 C CB . HIS D 26 ? 1.7067 2.5430 2.4690 -0.5650 0.9128 -0.7354 26 HIS D CB 6307 C CG . HIS D 26 ? 1.6895 2.5534 2.4495 -0.5423 0.8874 -0.6899 26 HIS D CG 6308 N ND1 . HIS D 26 ? 1.7103 2.5770 2.4652 -0.5470 0.9132 -0.7097 26 HIS D ND1 6309 C CD2 . HIS D 26 ? 1.6554 2.5451 2.4232 -0.5164 0.8438 -0.6282 26 HIS D CD2 6310 C CE1 . HIS D 26 ? 1.6855 2.5808 2.4403 -0.5235 0.8814 -0.6603 26 HIS D CE1 6311 N NE2 . HIS D 26 ? 1.6530 2.5620 2.4182 -0.5057 0.8412 -0.6116 26 HIS D NE2 6312 N N . SER D 27 ? 1.8524 2.4278 2.5547 -0.5911 1.0488 -0.8006 27 SER D N 6313 C CA . SER D 27 ? 1.9115 2.4156 2.5973 -0.5928 1.1096 -0.8188 27 SER D CA 6314 C C . SER D 27 ? 1.9037 2.5087 2.6428 -0.6297 1.1411 -0.8944 27 SER D C 6315 O O . SER D 27 ? 1.8968 2.5632 2.6760 -0.6613 1.1574 -0.9570 27 SER D O 6316 C CB . SER D 27 ? 1.9930 2.3499 2.6447 -0.5900 1.1769 -0.8270 27 SER D CB 6317 O OG . SER D 27 ? 2.0612 2.3304 2.6850 -0.5751 1.2371 -0.8213 27 SER D OG 6318 N N . ASN D 28 ? 1.9045 2.5376 2.6469 -0.6254 1.1492 -0.8943 28 ASN D N 6319 C CA . ASN D 28 ? 1.8845 2.6468 2.6816 -0.6556 1.1649 -0.9653 28 ASN D CA 6320 C C . ASN D 28 ? 1.9276 2.6517 2.7241 -0.6597 1.2159 -0.9831 28 ASN D C 6321 O O . ASN D 28 ? 1.9573 2.5787 2.7054 -0.6286 1.2200 -0.9224 28 ASN D O 6322 C CB . ASN D 28 ? 1.8026 2.7235 2.6179 -0.6381 1.0862 -0.9377 28 ASN D CB 6323 C CG . ASN D 28 ? 1.7752 2.8688 2.6488 -0.6635 1.0904 -1.0194 28 ASN D CG 6324 O OD1 . ASN D 28 ? 1.7974 2.9090 2.7046 -0.6980 1.1327 -1.0972 28 ASN D OD1 6325 N ND2 . ASN D 28 ? 1.7279 2.9597 2.6154 -0.6434 1.0475 -1.0042 28 ASN D ND2 6326 N N . GLU D 29 ? 1.9325 2.7484 2.7858 -0.6970 1.2566 -1.0714 29 GLU D N 6327 C CA . GLU D 29 ? 1.9694 2.7695 2.8343 -0.7058 1.3068 -1.0989 29 GLU D CA 6328 C C . GLU D 29 ? 1.9218 2.7726 2.7585 -0.6686 1.2430 -1.0286 29 GLU D C 6329 O O . GLU D 29 ? 1.9590 2.7363 2.7723 -0.6555 1.2727 -1.0057 29 GLU D O 6330 C CB . GLU D 29 ? 1.9749 2.8986 2.9199 -0.7564 1.3554 -1.2206 29 GLU D CB 6331 C CG . GLU D 29 ? 1.8927 3.0436 2.8771 -0.7556 1.2878 -1.2514 29 GLU D CG 6332 C CD . GLU D 29 ? 1.8419 3.0880 2.8350 -0.7507 1.2358 -1.2525 29 GLU D CD 6333 O OE1 . GLU D 29 ? 1.8732 3.0510 2.8758 -0.7741 1.2721 -1.2858 29 GLU D OE1 6334 O OE2 . GLU D 29 ? 1.7750 3.1638 2.7654 -0.7202 1.1631 -1.2176 29 GLU D OE2 6335 N N . GLN D 30 ? 1.8450 2.8187 2.6853 -0.6496 1.1615 -0.9932 30 GLN D N 6336 C CA . GLN D 30 ? 1.8006 2.8177 2.6179 -0.6126 1.1007 -0.9195 30 GLN D CA 6337 C C . GLN D 30 ? 1.8196 2.6942 2.5783 -0.5788 1.0844 -0.8338 30 GLN D C 6338 O O . GLN D 30 ? 1.8416 2.6630 2.5737 -0.5601 1.0930 -0.8013 30 GLN D O 6339 C CB . GLN D 30 ? 1.7278 2.8969 2.5655 -0.5957 1.0314 -0.8977 30 GLN D CB 6340 C CG . GLN D 30 ? 1.7017 3.0560 2.5894 -0.6089 1.0325 -0.9680 30 GLN D CG 6341 C CD . GLN D 30 ? 1.6523 3.1527 2.5603 -0.5923 0.9868 -0.9663 30 GLN D CD 6342 O OE1 . GLN D 30 ? 1.6573 3.1492 2.5740 -0.6069 0.9945 -0.9944 30 GLN D OE1 6343 N NE2 . GLN D 30 ? 1.6098 3.2471 2.5240 -0.5570 0.9435 -0.9312 30 GLN D NE2 6344 N N . GLY D 31 ? 1.8120 2.6361 2.5524 -0.5694 1.0606 -0.8021 31 GLY D N 6345 C CA . GLY D 31 ? 1.8295 2.5400 2.5194 -0.5360 1.0426 -0.7322 31 GLY D CA 6346 C C . GLY D 31 ? 1.8323 2.4902 2.5106 -0.5352 1.0321 -0.7219 31 GLY D C 6347 O O . GLY D 31 ? 1.8450 2.5081 2.5444 -0.5631 1.0619 -0.7736 31 GLY D O 6348 N N . SER D 32 ? 2.0502 1.4766 2.3731 -0.5279 0.4446 -0.6998 32 SER D N 6349 C CA . SER D 32 ? 2.0218 1.4693 2.3325 -0.5155 0.4361 -0.6588 32 SER D CA 6350 C C . SER D 32 ? 1.9875 1.4419 2.2640 -0.4862 0.4299 -0.6371 32 SER D C 6351 O O . SER D 32 ? 1.9879 1.4113 2.2677 -0.4704 0.4363 -0.6376 32 SER D O 6352 C CB . SER D 32 ? 2.0348 1.4527 2.3868 -0.5153 0.4434 -0.6326 32 SER D CB 6353 O OG . SER D 32 ? 2.0461 1.4172 2.4206 -0.5013 0.4543 -0.6292 32 SER D OG 6354 N N . GLY D 33 ? 1.9586 1.4536 2.2033 -0.4792 0.4171 -0.6183 33 GLY D N 6355 C CA . GLY D 33 ? 1.9263 1.4311 2.1380 -0.4523 0.4091 -0.5977 33 GLY D CA 6356 C C . GLY D 33 ? 1.8972 1.4460 2.0802 -0.4461 0.3948 -0.5748 33 GLY D C 6357 O O . GLY D 33 ? 1.9013 1.4768 2.0876 -0.4633 0.3910 -0.5755 33 GLY D O 6358 N N . TYR D 34 ? 1.8689 1.4251 2.0246 -0.4211 0.3867 -0.5549 34 TYR D N 6359 C CA . TYR D 34 ? 1.8400 1.4356 1.9680 -0.4108 0.3725 -0.5318 34 TYR D CA 6360 C C . TYR D 34 ? 1.8285 1.4612 1.9215 -0.4157 0.3619 -0.5496 34 TYR D C 6361 O O . TYR D 34 ? 1.8383 1.4651 1.9250 -0.4210 0.3651 -0.5755 34 TYR D O 6362 C CB . TYR D 34 ? 1.8149 1.3986 1.9338 -0.3803 0.3685 -0.4996 34 TYR D CB 6363 C CG . TYR D 34 ? 1.8246 1.3736 1.9772 -0.3733 0.3789 -0.4795 34 TYR D CG 6364 C CD1 . TYR D 34 ? 1.8220 1.3830 1.9890 -0.3744 0.3779 -0.4550 34 TYR D CD1 6365 C CD2 . TYR D 34 ? 1.8361 1.3422 2.0069 -0.3653 0.3899 -0.4840 34 TYR D CD2 6366 C CE1 . TYR D 34 ? 1.8318 1.3638 2.0307 -0.3680 0.3874 -0.4347 34 TYR D CE1 6367 C CE2 . TYR D 34 ? 1.8459 1.3215 2.0488 -0.3587 0.3995 -0.4642 34 TYR D CE2 6368 C CZ . TYR D 34 ? 1.8437 1.3328 2.0608 -0.3603 0.3982 -0.4392 34 TYR D CZ 6369 O OH . TYR D 34 ? 1.8537 1.3150 2.1038 -0.3538 0.4077 -0.4177 34 TYR D OH 6370 N N . ALA D 35 ? 1.8093 1.4819 1.8806 -0.4134 0.3494 -0.5348 35 ALA D N 6371 C CA . ALA D 35 ? 1.7964 1.5085 1.8354 -0.4175 0.3381 -0.5474 35 ALA D CA 6372 C C . ALA D 35 ? 1.7708 1.5187 1.7870 -0.4049 0.3238 -0.5211 35 ALA D C 6373 O O . ALA D 35 ? 1.7730 1.5394 1.7974 -0.4133 0.3221 -0.5101 35 ALA D O 6374 C CB . ALA D 35 ? 1.8179 1.5490 1.8632 -0.4477 0.3416 -0.5784 35 ALA D CB 6375 N N . ALA D 36 ? 1.7481 1.5062 1.7369 -0.3845 0.3132 -0.5110 36 ALA D N 6376 C CA . ALA D 36 ? 1.7233 1.5132 1.6900 -0.3695 0.2986 -0.4866 36 ALA D CA 6377 C C . ALA D 36 ? 1.7197 1.5572 1.6677 -0.3854 0.2894 -0.4976 36 ALA D C 6378 O O . ALA D 36 ? 1.7254 1.5745 1.6643 -0.3989 0.2896 -0.5219 36 ALA D O 6379 C CB . ALA D 36 ? 1.7008 1.4823 1.6475 -0.3421 0.2900 -0.4725 36 ALA D CB 6380 N N . ASP D 37 ? 1.7114 1.5779 1.6538 -0.3833 0.2814 -0.4792 37 ASP D N 6381 C CA . ASP D 37 ? 1.7051 1.6197 1.6277 -0.3944 0.2709 -0.4843 37 ASP D CA 6382 C C . ASP D 37 ? 1.6794 1.6126 1.5719 -0.3728 0.2559 -0.4721 37 ASP D C 6383 O O . ASP D 37 ? 1.6618 1.6003 1.5462 -0.3516 0.2472 -0.4470 37 ASP D O 6384 C CB . ASP D 37 ? 1.7060 1.6444 1.6371 -0.4011 0.2691 -0.4690 37 ASP D CB 6385 C CG . ASP D 37 ? 1.6993 1.6886 1.6117 -0.4140 0.2589 -0.4744 37 ASP D CG 6386 O OD1 . ASP D 37 ? 1.7048 1.7099 1.6064 -0.4281 0.2577 -0.4971 37 ASP D OD1 6387 O OD2 . ASP D 37 ? 1.6887 1.7044 1.5978 -0.4099 0.2523 -0.4553 37 ASP D OD2 6388 N N . LYS D 38 ? 1.6786 1.6224 1.5560 -0.3781 0.2526 -0.4900 38 LYS D N 6389 C CA . LYS D 38 ? 1.6550 1.6154 1.5063 -0.3594 0.2383 -0.4796 38 LYS D CA 6390 C C . LYS D 38 ? 1.6400 1.6461 1.4736 -0.3575 0.2242 -0.4665 38 LYS D C 6391 O O . LYS D 38 ? 1.6193 1.6346 1.4361 -0.3358 0.2111 -0.4484 38 LYS D O 6392 C CB . LYS D 38 ? 1.6584 1.6223 1.5001 -0.3680 0.2391 -0.5019 38 LYS D CB 6393 C CG . LYS D 38 ? 1.6722 1.5923 1.5290 -0.3669 0.2519 -0.5146 38 LYS D CG 6394 N N . GLU D 39 ? 1.6510 1.6853 1.4893 -0.3798 0.2266 -0.4758 39 GLU D N 6395 C CA . GLU D 39 ? 1.6374 1.7180 1.4605 -0.3805 0.2144 -0.4648 39 GLU D CA 6396 C C . GLU D 39 ? 1.6233 1.7043 1.4461 -0.3590 0.2079 -0.4359 39 GLU D C 6397 O O . GLU D 39 ? 1.6030 1.7095 1.4073 -0.3433 0.1937 -0.4206 39 GLU D O 6398 C CB . GLU D 39 ? 1.6531 1.7614 1.4846 -0.4104 0.2199 -0.4816 39 GLU D CB 6399 N N . SER D 40 ? 1.6332 1.6873 1.4774 -0.3580 0.2181 -0.4286 40 SER D N 6400 C CA . SER D 40 ? 1.6212 1.6751 1.4671 -0.3371 0.2135 -0.4014 40 SER D CA 6401 C C . SER D 40 ? 1.6069 1.6337 1.4450 -0.3072 0.2079 -0.3871 40 SER D C 6402 O O . SER D 40 ? 1.5899 1.6291 1.4167 -0.2850 0.1969 -0.3664 40 SER D O 6403 C CB . SER D 40 ? 1.6381 1.6750 1.5118 -0.3475 0.2266 -0.3972 40 SER D CB 6404 O OG . SER D 40 ? 1.6528 1.6450 1.5451 -0.3511 0.2396 -0.4080 40 SER D OG 6405 N N . THR D 41 ? 1.6139 1.6044 1.4583 -0.3067 0.2154 -0.3987 41 THR D N 6406 C CA . THR D 41 ? 1.6021 1.5648 1.4404 -0.2801 0.2109 -0.3870 41 THR D CA 6407 C C . THR D 41 ? 1.5824 1.5673 1.3949 -0.2652 0.1937 -0.3820 41 THR D C 6408 O O . THR D 41 ? 1.5662 1.5465 1.3699 -0.2395 0.1836 -0.3637 41 THR D O 6409 C CB . THR D 41 ? 1.6147 1.5361 1.4660 -0.2849 0.2231 -0.4023 41 THR D CB 6410 O OG1 . THR D 41 ? 1.6326 1.5292 1.5105 -0.2947 0.2383 -0.4032 41 THR D OG1 6411 C CG2 . THR D 41 ? 1.6009 1.4962 1.4445 -0.2583 0.2174 -0.3908 41 THR D CG2 6412 N N . GLN D 42 ? 1.5841 1.5936 1.3853 -0.2813 0.1900 -0.3980 42 GLN D N 6413 C CA . GLN D 42 ? 1.5657 1.5994 1.3444 -0.2697 0.1735 -0.3930 42 GLN D CA 6414 C C . GLN D 42 ? 1.5507 1.6138 1.3186 -0.2548 0.1601 -0.3729 42 GLN D C 6415 O O . GLN D 42 ? 1.5329 1.5990 1.2874 -0.2324 0.1461 -0.3596 42 GLN D O 6416 C CB . GLN D 42 ? 1.5706 1.6321 1.3412 -0.2924 0.1732 -0.4130 42 GLN D CB 6417 N N . LYS D 43 ? 1.5567 1.6414 1.3315 -0.2670 0.1643 -0.3709 43 LYS D N 6418 C CA . LYS D 43 ? 1.5429 1.6581 1.3089 -0.2539 0.1531 -0.3522 43 LYS D CA 6419 C C . LYS D 43 ? 1.5332 1.6277 1.3017 -0.2253 0.1496 -0.3315 43 LYS D C 6420 O O . LYS D 43 ? 1.5182 1.6314 1.2738 -0.2048 0.1357 -0.3163 43 LYS D O 6421 C CB . LYS D 43 ? 1.5533 1.6948 1.3288 -0.2752 0.1602 -0.3549 43 LYS D CB 6422 C CG . LYS D 43 ? 1.5403 1.7202 1.3060 -0.2642 0.1488 -0.3373 43 LYS D CG 6423 N N . ALA D 44 ? 1.5421 1.5990 1.3275 -0.2237 0.1621 -0.3313 44 ALA D N 6424 C CA . ALA D 44 ? 1.5344 1.5714 1.3239 -0.1975 0.1604 -0.3122 44 ALA D CA 6425 C C . ALA D 44 ? 1.5203 1.5375 1.2977 -0.1735 0.1496 -0.3076 44 ALA D C 6426 O O . ALA D 44 ? 1.5074 1.5265 1.2779 -0.1479 0.1393 -0.2910 44 ALA D O 6427 C CB . ALA D 44 ? 1.5503 1.5554 1.3640 -0.2050 0.1777 -0.3124 44 ALA D CB 6428 N N . ILE D 45 ? 1.5227 1.5219 1.2983 -0.1818 0.1518 -0.3224 45 ILE D N 6429 C CA . ILE D 45 ? 1.5100 1.4906 1.2754 -0.1617 0.1415 -0.3188 45 ILE D CA 6430 C C . ILE D 45 ? 1.4935 1.5051 1.2393 -0.1485 0.1216 -0.3110 45 ILE D C 6431 O O . ILE D 45 ? 1.4809 1.4847 1.2194 -0.1230 0.1093 -0.2986 45 ILE D O 6432 C CB . ILE D 45 ? 1.5165 1.4751 1.2850 -0.1754 0.1489 -0.3366 45 ILE D CB 6433 C CG1 . ILE D 45 ? 1.5317 1.4537 1.3209 -0.1828 0.1673 -0.3425 45 ILE D CG1 6434 C CG2 . ILE D 45 ? 1.5032 1.4495 1.2604 -0.1562 0.1361 -0.3318 45 ILE D CG2 6435 C CD1 . ILE D 45 ? 1.5443 1.4499 1.3390 -0.2015 0.1776 -0.3637 45 ILE D CD1 6436 N N . ASP D 46 ? 1.4925 1.5394 1.2308 -0.1657 0.1184 -0.3185 46 ASP D N 6437 C CA . ASP D 46 ? 1.4767 1.5562 1.1982 -0.1552 0.1000 -0.3109 46 ASP D CA 6438 C C . ASP D 46 ? 1.4676 1.5616 1.1858 -0.1341 0.0915 -0.2931 46 ASP D C 6439 O O . ASP D 46 ? 1.4558 1.5556 1.1632 -0.1113 0.0752 -0.2824 46 ASP D O 6440 C CB . ASP D 46 ? 1.4804 1.5974 1.1964 -0.1798 0.1002 -0.3222 46 ASP D CB 6441 C CG . ASP D 46 ? 1.4880 1.5978 1.2050 -0.1996 0.1068 -0.3404 46 ASP D CG 6442 O OD1 . ASP D 46 ? 1.4872 1.5661 1.2062 -0.1914 0.1076 -0.3425 46 ASP D OD1 6443 O OD2 . ASP D 46 ? 1.4936 1.6307 1.2093 -0.2233 0.1110 -0.3529 46 ASP D OD2 6444 N N . GLY D 47 ? 1.4741 1.5747 1.2025 -0.1416 0.1022 -0.2899 47 GLY D N 6445 C CA . GLY D 47 ? 1.4665 1.5843 1.1929 -0.1229 0.0961 -0.2730 47 GLY D CA 6446 C C . GLY D 47 ? 1.4590 1.5507 1.1858 -0.0933 0.0907 -0.2605 47 GLY D C 6447 O O . GLY D 47 ? 1.4472 1.5524 1.1629 -0.0696 0.0755 -0.2496 47 GLY D O 6448 N N . VAL D 48 ? 1.4677 1.5222 1.2075 -0.0944 0.1031 -0.2627 48 VAL D N 6449 C CA . VAL D 48 ? 1.4634 1.4912 1.2053 -0.0677 0.0999 -0.2514 48 VAL D CA 6450 C C . VAL D 48 ? 1.4516 1.4705 1.1800 -0.0487 0.0829 -0.2509 48 VAL D C 6451 O O . VAL D 48 ? 1.4405 1.4593 1.1627 -0.0219 0.0708 -0.2394 48 VAL D O 6452 C CB . VAL D 48 ? 1.4755 1.4644 1.2353 -0.0755 0.1174 -0.2551 48 VAL D CB 6453 C CG1 . VAL D 48 ? 1.4703 1.4302 1.2308 -0.0488 0.1131 -0.2452 48 VAL D CG1 6454 C CG2 . VAL D 48 ? 1.4873 1.4831 1.2634 -0.0886 0.1324 -0.2507 48 VAL D CG2 6455 N N . THR D 49 ? 1.4534 1.4659 1.1781 -0.0626 0.0817 -0.2634 49 THR D N 6456 C CA . THR D 49 ? 1.4445 1.4494 1.1588 -0.0475 0.0657 -0.2626 49 THR D CA 6457 C C . THR D 49 ? 1.4344 1.4724 1.1349 -0.0335 0.0464 -0.2549 49 THR D C 6458 O O . THR D 49 ? 1.4259 1.4572 1.1200 -0.0101 0.0307 -0.2478 49 THR D O 6459 C CB . THR D 49 ? 1.4488 1.4456 1.1629 -0.0676 0.0694 -0.2769 49 THR D CB 6460 O OG1 . THR D 49 ? 1.4609 1.4269 1.1886 -0.0801 0.0875 -0.2852 49 THR D OG1 6461 C CG2 . THR D 49 ? 1.4386 1.4257 1.1446 -0.0520 0.0530 -0.2739 49 THR D CG2 6462 N N . ASN D 50 ? 1.4356 1.5091 1.1327 -0.0476 0.0475 -0.2565 50 ASN D N 6463 C CA . ASN D 50 ? 1.4253 1.5331 1.1105 -0.0346 0.0305 -0.2486 50 ASN D CA 6464 C C . ASN D 50 ? 1.4205 1.5334 1.1042 -0.0075 0.0238 -0.2350 50 ASN D C 6465 O O . ASN D 50 ? 1.4102 1.5408 1.0843 0.0119 0.0066 -0.2282 50 ASN D O 6466 C CB . ASN D 50 ? 1.4287 1.5750 1.1114 -0.0576 0.0346 -0.2535 50 ASN D CB 6467 C CG . ASN D 50 ? 1.4283 1.5849 1.1061 -0.0762 0.0315 -0.2641 50 ASN D CG 6468 O OD1 . ASN D 50 ? 1.4253 1.6177 1.0956 -0.0833 0.0241 -0.2638 50 ASN D OD1 6469 N ND2 . ASN D 50 ? 1.4315 1.5590 1.1137 -0.0838 0.0372 -0.2727 50 ASN D ND2 6470 N N . LYS D 51 ? 1.4275 1.5262 1.1213 -0.0062 0.0373 -0.2311 51 LYS D N 6471 C CA . LYS D 51 ? 1.4242 1.5293 1.1175 0.0189 0.0329 -0.2179 51 LYS D CA 6472 C C . LYS D 51 ? 1.4187 1.4957 1.1097 0.0463 0.0220 -0.2135 51 LYS D C 6473 O O . LYS D 51 ? 1.4118 1.5011 1.0942 0.0716 0.0059 -0.2065 51 LYS D O 6474 C CB . LYS D 51 ? 1.4339 1.5351 1.1410 0.0092 0.0517 -0.2137 51 LYS D CB 6475 C CG . LYS D 51 ? 1.4316 1.5541 1.1383 0.0301 0.0490 -0.1990 51 LYS D CG 6476 C CD . LYS D 51 ? 1.4426 1.5596 1.1659 0.0189 0.0681 -0.1932 51 LYS D CD 6477 C CE . LYS D 51 ? 1.4430 1.5952 1.1661 0.0316 0.0670 -0.1786 51 LYS D CE 6478 N NZ . LYS D 51 ? 1.4453 1.6353 1.1667 0.0123 0.0688 -0.1799 51 LYS D NZ 6479 N N . VAL D 52 ? 1.4228 1.4625 1.1219 0.0411 0.0307 -0.2184 52 VAL D N 6480 C CA . VAL D 52 ? 1.4184 1.4287 1.1171 0.0646 0.0222 -0.2147 52 VAL D CA 6481 C C . VAL D 52 ? 1.4078 1.4203 1.0956 0.0785 0.0006 -0.2160 52 VAL D C 6482 O O . VAL D 52 ? 1.4021 1.4084 1.0858 0.1054 -0.0133 -0.2100 52 VAL D O 6483 C CB . VAL D 52 ? 1.4266 1.3973 1.1369 0.0536 0.0368 -0.2201 52 VAL D CB 6484 C CG1 . VAL D 52 ? 1.4303 1.3933 1.1405 0.0300 0.0400 -0.2329 52 VAL D CG1 6485 C CG2 . VAL D 52 ? 1.4219 1.3644 1.1329 0.0789 0.0290 -0.2144 52 VAL D CG2 6486 N N . ASN D 53 ? 1.4047 1.4271 1.0887 0.0602 -0.0022 -0.2237 53 ASN D N 6487 C CA . ASN D 53 ? 1.3957 1.4232 1.0716 0.0710 -0.0226 -0.2235 53 ASN D CA 6488 C C . ASN D 53 ? 1.3906 1.4512 1.0577 0.0884 -0.0380 -0.2168 53 ASN D C 6489 O O . ASN D 53 ? 1.3845 1.4425 1.0473 0.1114 -0.0569 -0.2128 53 ASN D O 6490 C CB . ASN D 53 ? 1.3958 1.4296 1.0710 0.0457 -0.0206 -0.2322 53 ASN D CB 6491 C CG . ASN D 53 ? 1.4004 1.4023 1.0838 0.0304 -0.0070 -0.2400 53 ASN D CG 6492 O OD1 . ASN D 53 ? 1.4028 1.3755 1.0929 0.0392 0.0001 -0.2382 53 ASN D OD1 6493 N ND2 . ASN D 53 ? 1.4016 1.4107 1.0845 0.0077 -0.0032 -0.2486 53 ASN D ND2 6494 N N . SER D 54 ? 1.3934 1.4849 1.0590 0.0775 -0.0301 -0.2157 54 SER D N 6495 C CA . SER D 54 ? 1.3898 1.5162 1.0474 0.0934 -0.0425 -0.2090 54 SER D CA 6496 C C . SER D 54 ? 1.3889 1.5103 1.0454 0.1247 -0.0497 -0.2011 54 SER D C 6497 O O . SER D 54 ? 1.3829 1.5228 1.0323 0.1468 -0.0666 -0.1970 54 SER D O 6498 C CB . SER D 54 ? 1.3937 1.5536 1.0515 0.0734 -0.0302 -0.2089 54 SER D CB 6499 O OG . SER D 54 ? 1.3895 1.5847 1.0398 0.0892 -0.0411 -0.2018 54 SER D OG 6500 N N . ILE D 55 ? 1.3936 1.4915 1.0577 0.1269 -0.0368 -0.1992 55 ILE D N 6501 C CA . ILE D 55 ? 1.3928 1.4849 1.0565 0.1563 -0.0424 -0.1918 55 ILE D CA 6502 C C . ILE D 55 ? 1.3879 1.4553 1.0489 0.1784 -0.0605 -0.1935 55 ILE D C 6503 O O . ILE D 55 ? 1.3852 1.4623 1.0406 0.2059 -0.0761 -0.1900 55 ILE D O 6504 C CB . ILE D 55 ? 1.3996 1.4743 1.0739 0.1511 -0.0228 -0.1879 55 ILE D CB 6505 C CG1 . ILE D 55 ? 1.4053 1.5095 1.0834 0.1359 -0.0082 -0.1833 55 ILE D CG1 6506 C CG2 . ILE D 55 ? 1.3988 1.4628 1.0730 0.1818 -0.0293 -0.1809 55 ILE D CG2 6507 C CD1 . ILE D 55 ? 1.4143 1.4997 1.1066 0.1195 0.0137 -0.1814 55 ILE D CD1 6508 N N . ILE D 56 ? 1.3878 1.4245 1.0534 0.1666 -0.0587 -0.1991 56 ILE D N 6509 C CA . ILE D 56 ? 1.3845 1.3964 1.0495 0.1847 -0.0757 -0.2002 56 ILE D CA 6510 C C . ILE D 56 ? 1.3815 1.4130 1.0393 0.1965 -0.0981 -0.2004 56 ILE D C 6511 O O . ILE D 56 ? 1.3788 1.4056 1.0343 0.2232 -0.1161 -0.1987 56 ILE D O 6512 C CB . ILE D 56 ? 1.3848 1.3642 1.0564 0.1666 -0.0688 -0.2056 56 ILE D CB 6513 C CG1 . ILE D 56 ? 1.3900 1.3456 1.0704 0.1587 -0.0482 -0.2053 56 ILE D CG1 6514 C CG2 . ILE D 56 ? 1.3798 1.3371 1.0517 0.1840 -0.0883 -0.2056 56 ILE D CG2 6515 C CD1 . ILE D 56 ? 1.3922 1.3249 1.0793 0.1336 -0.0356 -0.2122 56 ILE D CD1 6516 N N . ASP D 57 ? 1.3833 1.4372 1.0384 0.1766 -0.0970 -0.2027 57 ASP D N 6517 C CA . ASP D 57 ? 1.3810 1.4533 1.0313 0.1840 -0.1172 -0.2022 57 ASP D CA 6518 C C . ASP D 57 ? 1.3819 1.4861 1.0254 0.2053 -0.1281 -0.1981 57 ASP D C 6519 O O . ASP D 57 ? 1.3790 1.4929 1.0199 0.2208 -0.1482 -0.1972 57 ASP D O 6520 C CB . ASP D 57 ? 1.3815 1.4697 1.0315 0.1547 -0.1115 -0.2054 57 ASP D CB 6521 C CG . ASP D 57 ? 1.3827 1.4425 1.0391 0.1349 -0.1026 -0.2102 57 ASP D CG 6522 O OD1 . ASP D 57 ? 1.3819 1.4110 1.0426 0.1471 -0.1101 -0.2096 57 ASP D OD1 6523 O OD2 . ASP D 57 ? 1.3838 1.4530 1.0411 0.1074 -0.0881 -0.2149 57 ASP D OD2 6524 N N . LYS D 58 ? 1.3865 1.5077 1.0282 0.2061 -0.1151 -0.1952 58 LYS D N 6525 C CA . LYS D 58 ? 1.3871 1.5399 1.0223 0.2283 -0.1239 -0.1909 58 LYS D CA 6526 C C . LYS D 58 ? 1.3904 1.5284 1.0249 0.2620 -0.1373 -0.1900 58 LYS D C 6527 O O . LYS D 58 ? 1.3898 1.5467 1.0190 0.2863 -0.1541 -0.1893 58 LYS D O 6528 C CB . LYS D 58 ? 1.3886 1.5662 1.0236 0.2171 -0.1049 -0.1866 58 LYS D CB 6529 C CG . LYS D 58 ? 1.3871 1.6076 1.0148 0.2316 -0.1121 -0.1818 58 LYS D CG 6530 C CD . LYS D 58 ? 1.3858 1.6378 1.0109 0.2087 -0.1084 -0.1819 58 LYS D CD 6531 C CE . LYS D 58 ? 1.3826 1.6286 1.0067 0.2012 -0.1216 -0.1865 58 LYS D CE 6532 N NZ . LYS D 58 ? 1.3819 1.6616 1.0033 0.1789 -0.1179 -0.1863 58 LYS D NZ 6533 N N . MET D 59 ? 1.3950 1.4997 1.0350 0.2635 -0.1300 -0.1906 59 MET D N 6534 C CA . MET D 59 ? 1.3980 1.4870 1.0380 0.2938 -0.1410 -0.1903 59 MET D CA 6535 C C . MET D 59 ? 1.4000 1.4611 1.0428 0.3045 -0.1607 -0.1949 59 MET D C 6536 O O . MET D 59 ? 1.3992 1.4404 1.0437 0.3265 -0.1703 -0.1961 59 MET D O 6537 C CB . MET D 59 ? 1.3985 1.4681 1.0441 0.2903 -0.1226 -0.1871 59 MET D CB 6538 C CG . MET D 59 ? 1.3989 1.4933 1.0454 0.2769 -0.1022 -0.1812 59 MET D CG 6539 S SD . MET D 59 ? 1.3989 1.5355 1.0380 0.3050 -0.1079 -0.1746 59 MET D SD 6540 C CE . MET D 59 ? 1.4012 1.5156 1.0433 0.3318 -0.1096 -0.1720 59 MET D CE 6541 N N . ASN D 60 ? 1.4030 1.4641 1.0471 0.2882 -0.1668 -0.1968 60 ASN D N 6542 C CA . ASN D 60 ? 1.4063 1.4473 1.0544 0.2970 -0.1874 -0.1993 60 ASN D CA 6543 C C . ASN D 60 ? 1.4088 1.4651 1.0537 0.3276 -0.2109 -0.2003 60 ASN D C 6544 O O . ASN D 60 ? 1.4064 1.4414 1.0553 0.3477 -0.2287 -0.2029 60 ASN D O 6545 C CB . ASN D 60 ? 1.4053 1.4510 1.0558 0.2702 -0.1861 -0.1992 60 ASN D CB 6546 C CG . ASN D 60 ? 1.4067 1.4301 1.0643 0.2743 -0.2049 -0.1994 60 ASN D CG 6547 O OD1 . ASN D 60 ? 1.4090 1.4251 1.0687 0.2998 -0.2258 -0.2000 60 ASN D OD1 6548 N ND2 . ASN D 60 ? 1.4046 1.4186 1.0666 0.2489 -0.1980 -0.1991 60 ASN D ND2 6549 N N . THR D 61 ? 1.4134 1.5070 1.0515 0.3310 -0.2112 -0.1988 61 THR D N 6550 C CA . THR D 61 ? 1.4183 1.5308 1.0528 0.3610 -0.2318 -0.2006 61 THR D CA 6551 C C . THR D 61 ? 1.4252 1.5430 1.0552 0.3853 -0.2291 -0.2014 61 THR D C 6552 O O . THR D 61 ? 1.4252 1.5761 1.0484 0.3911 -0.2222 -0.1988 61 THR D O 6553 C CB . THR D 61 ? 1.4175 1.5702 1.0468 0.3556 -0.2343 -0.1982 61 THR D CB 6554 O OG1 . THR D 61 ? 1.4213 1.5960 1.0460 0.3867 -0.2501 -0.2002 61 THR D OG1 6555 C CG2 . THR D 61 ? 1.4168 1.5937 1.0415 0.3312 -0.2099 -0.1940 61 THR D CG2 6556 N N . GLN D 62 ? 1.0647 0.6683 0.5342 -0.1387 0.1221 -0.1944 62 GLN D N 6557 C CA . GLN D 62 ? 0.9437 0.6398 0.5484 -0.1087 0.1160 -0.1914 62 GLN D CA 6558 C C . GLN D 62 ? 0.9016 0.6209 0.5369 -0.1058 0.1306 -0.1845 62 GLN D C 6559 O O . GLN D 62 ? 0.9787 0.6564 0.5549 -0.1327 0.1667 -0.1955 62 GLN D O 6560 C CB . GLN D 62 ? 0.9223 0.6553 0.6006 -0.1081 0.1462 -0.2246 62 GLN D CB 6561 C CG . GLN D 62 ? 0.8369 0.6350 0.6298 -0.0766 0.1307 -0.2238 62 GLN D CG 6562 C CD . GLN D 62 ? 0.8351 0.6482 0.6816 -0.0675 0.1324 -0.2486 62 GLN D CD 6563 O OE1 . GLN D 62 ? 0.8785 0.6657 0.6838 -0.0796 0.1347 -0.2562 62 GLN D OE1 6564 N NE2 . GLN D 62 ? 0.7982 0.6443 0.7320 -0.0441 0.1245 -0.2621 62 GLN D NE2 6565 N N . PHE D 63 ? 0.8001 0.5758 0.5177 -0.0776 0.1060 -0.1682 63 PHE D N 6566 C CA . PHE D 63 ? 0.7574 0.5540 0.5016 -0.0714 0.1097 -0.1573 63 PHE D CA 6567 C C . PHE D 63 ? 0.7538 0.5741 0.5504 -0.0810 0.1546 -0.1904 63 PHE D C 6568 O O . PHE D 63 ? 0.7290 0.5777 0.5934 -0.0754 0.1682 -0.2214 63 PHE D O 6569 C CB . PHE D 63 ? 0.6713 0.5110 0.4815 -0.0431 0.0763 -0.1364 63 PHE D CB 6570 C CG . PHE D 63 ? 0.6312 0.4910 0.4677 -0.0354 0.0767 -0.1247 63 PHE D CG 6571 C CD1 . PHE D 63 ? 0.6322 0.4750 0.4290 -0.0368 0.0597 -0.1021 63 PHE D CD1 6572 C CD2 . PHE D 63 ? 0.5892 0.4812 0.4939 -0.0239 0.0869 -0.1395 63 PHE D CD2 6573 C CE1 . PHE D 63 ? 0.6014 0.4624 0.4223 -0.0304 0.0614 -0.0919 63 PHE D CE1 6574 C CE2 . PHE D 63 ? 0.5577 0.4657 0.4846 -0.0168 0.0846 -0.1300 63 PHE D CE2 6575 C CZ . PHE D 63 ? 0.5600 0.4543 0.4434 -0.0219 0.0761 -0.1048 63 PHE D CZ 6576 N N . GLU D 64 ? 0.7750 0.5832 0.5487 -0.0945 0.1749 -0.1889 64 GLU D N 6577 C CA . GLU D 64 ? 0.7728 0.6096 0.6122 -0.1060 0.2195 -0.2281 64 GLU D CA 6578 C C . GLU D 64 ? 0.7003 0.5793 0.6033 -0.0829 0.1991 -0.2144 64 GLU D C 6579 O O . GLU D 64 ? 0.7135 0.5715 0.5633 -0.0834 0.1843 -0.1812 64 GLU D O 6580 C CB . GLU D 64 ? 0.8855 0.6582 0.6336 -0.1542 0.2776 -0.2496 64 GLU D CB 6581 C CG . GLU D 64 ? 0.9704 0.7064 0.6793 -0.1839 0.3169 -0.2843 64 GLU D CG 6582 C CD . GLU D 64 ? 1.1204 0.7550 0.6883 -0.2407 0.3752 -0.2994 64 GLU D CD 6583 O OE1 . GLU D 64 ? 1.1649 0.7644 0.6832 -0.2591 0.3939 -0.2914 64 GLU D OE1 6584 O OE2 . GLU D 64 ? 1.2068 0.7844 0.7005 -0.2700 0.4035 -0.3193 64 GLU D OE2 6585 N N . ALA D 65 ? 0.6392 0.5709 0.6547 -0.0604 0.1921 -0.2426 65 ALA D N 6586 C CA . ALA D 65 ? 0.5816 0.5458 0.6570 -0.0377 0.1691 -0.2360 65 ALA D CA 6587 C C . ALA D 65 ? 0.5970 0.5709 0.6956 -0.0622 0.2153 -0.2667 65 ALA D C 6588 O O . ALA D 65 ? 0.6283 0.6028 0.7509 -0.0909 0.2675 -0.3157 65 ALA D O 6589 C CB . ALA D 65 ? 0.5408 0.5344 0.7114 -0.0025 0.1319 -0.2578 65 ALA D CB 6590 N N . VAL D 66 ? 0.5767 0.5550 0.6678 -0.0554 0.2021 -0.2419 66 VAL D N 6591 C CA . VAL D 66 ? 0.6078 0.5878 0.7090 -0.0820 0.2473 -0.2666 66 VAL D CA 6592 C C . VAL D 66 ? 0.5415 0.5637 0.7221 -0.0542 0.2170 -0.2666 66 VAL D C 6593 O O . VAL D 66 ? 0.5218 0.5368 0.6687 -0.0323 0.1747 -0.2201 66 VAL D O 6594 C CB . VAL D 66 ? 0.6774 0.5884 0.6409 -0.1126 0.2668 -0.2299 66 VAL D CB 6595 C CG1 . VAL D 66 ? 0.7221 0.6213 0.6834 -0.1444 0.3175 -0.2548 66 VAL D CG1 6596 C CG2 . VAL D 66 ? 0.7601 0.6075 0.6217 -0.1407 0.2884 -0.2295 66 VAL D CG2 6597 N N . GLY D 67 ? 0.5253 0.5898 0.8155 -0.0570 0.2399 -0.3248 67 GLY D N 6598 C CA . GLY D 67 ? 0.4789 0.5785 0.8466 -0.0303 0.2067 -0.3318 67 GLY D CA 6599 C C . GLY D 67 ? 0.4728 0.5512 0.7690 -0.0430 0.2150 -0.2908 67 GLY D C 6600 O O . GLY D 67 ? 0.5175 0.5748 0.7730 -0.0823 0.2711 -0.3021 67 GLY D O 6601 N N . ARG D 68 ? 0.4305 0.5029 0.7012 -0.0129 0.1615 -0.2446 68 ARG D N 6602 C CA . ARG D 68 ? 0.4134 0.4750 0.6418 -0.0172 0.1605 -0.2122 68 ARG D CA 6603 C C . ARG D 68 ? 0.3713 0.4593 0.6724 0.0144 0.1173 -0.2215 68 ARG D C 6604 O O . ARG D 68 ? 0.3526 0.4385 0.6832 0.0447 0.0699 -0.2250 68 ARG D O 6605 C CB . ARG D 68 ? 0.4130 0.4361 0.5392 -0.0143 0.1388 -0.1520 68 ARG D CB 6606 C CG . ARG D 68 ? 0.4614 0.4434 0.5035 -0.0401 0.1644 -0.1412 68 ARG D CG 6607 C CD . ARG D 68 ? 0.4570 0.4075 0.4237 -0.0324 0.1332 -0.0930 68 ARG D CD 6608 N NE . ARG D 68 ? 0.5112 0.4169 0.4028 -0.0497 0.1416 -0.0882 68 ARG D NE 6609 C CZ . ARG D 68 ? 0.5113 0.4195 0.4057 -0.0431 0.1299 -0.0915 68 ARG D CZ 6610 N NH1 . ARG D 68 ? 0.4598 0.4057 0.4206 -0.0199 0.1090 -0.0970 68 ARG D NH1 6611 N NH2 . ARG D 68 ? 0.5710 0.4302 0.3881 -0.0603 0.1355 -0.0885 68 ARG D NH2 6612 N N . GLU D 69 ? 0.3656 0.4646 0.6818 0.0063 0.1306 -0.2249 69 GLU D N 6613 C CA . GLU D 69 ? 0.3479 0.4644 0.7262 0.0348 0.0875 -0.2363 69 GLU D CA 6614 C C . GLU D 69 ? 0.3240 0.4188 0.6369 0.0369 0.0742 -0.1884 69 GLU D C 6615 O O . GLU D 69 ? 0.3234 0.4040 0.5748 0.0129 0.1076 -0.1622 69 GLU D O 6616 C CB . GLU D 69 ? 0.3593 0.5225 0.8567 0.0268 0.1119 -0.3048 69 GLU D CB 6617 C CG . GLU D 69 ? 0.3779 0.5712 0.9805 0.0388 0.1040 -0.3668 69 GLU D CG 6618 C CD . GLU D 69 ? 0.3943 0.6439 1.1403 0.0261 0.1368 -0.4499 69 GLU D CD 6619 O OE1 . GLU D 69 ? 0.4012 0.6731 1.2316 0.0547 0.0896 -0.4776 69 GLU D OE1 6620 O OE2 . GLU D 69 ? 0.4276 0.6928 1.1985 -0.0157 0.2118 -0.4912 69 GLU D OE2 6621 N N . PHE D 70 ? 0.3133 0.3946 0.6341 0.0658 0.0218 -0.1804 70 PHE D N 6622 C CA . PHE D 70 ? 0.3067 0.3623 0.5656 0.0678 0.0086 -0.1389 70 PHE D CA 6623 C C . PHE D 70 ? 0.3142 0.3666 0.6172 0.0899 -0.0322 -0.1598 70 PHE D C 6624 O O . PHE D 70 ? 0.3299 0.3801 0.6916 0.1141 -0.0737 -0.1968 70 PHE D O 6625 C CB . PHE D 70 ? 0.3181 0.3290 0.4931 0.0723 -0.0101 -0.0967 70 PHE D CB 6626 C CG . PHE D 70 ? 0.3159 0.3290 0.4596 0.0570 0.0161 -0.0840 70 PHE D CG 6627 C CD1 . PHE D 70 ? 0.3082 0.3208 0.4088 0.0383 0.0428 -0.0589 70 PHE D CD1 6628 C CD2 . PHE D 70 ? 0.3327 0.3423 0.4911 0.0639 0.0072 -0.1007 70 PHE D CD2 6629 C CE1 . PHE D 70 ? 0.3238 0.3283 0.3913 0.0272 0.0562 -0.0505 70 PHE D CE1 6630 C CE2 . PHE D 70 ? 0.3318 0.3400 0.4585 0.0497 0.0290 -0.0907 70 PHE D CE2 6631 C CZ . PHE D 70 ? 0.3328 0.3366 0.4118 0.0315 0.0517 -0.0657 70 PHE D CZ 6632 N N . ASN D 71 ? 0.3157 0.3640 0.5932 0.0834 -0.0259 -0.1399 71 ASN D N 6633 C CA . ASN D 71 ? 0.3401 0.3736 0.6415 0.1036 -0.0689 -0.1553 71 ASN D CA 6634 C C . ASN D 71 ? 0.3982 0.3544 0.6020 0.1166 -0.1118 -0.1208 71 ASN D C 6635 O O . ASN D 71 ? 0.3913 0.3179 0.5226 0.1057 -0.0977 -0.0877 71 ASN D O 6636 C CB . ASN D 71 ? 0.3183 0.3810 0.6416 0.0880 -0.0391 -0.1567 71 ASN D CB 6637 C CG . ASN D 71 ? 0.3130 0.3543 0.5505 0.0708 -0.0140 -0.1059 71 ASN D CG 6638 O OD1 . ASN D 71 ? 0.3321 0.3290 0.4979 0.0750 -0.0317 -0.0745 71 ASN D OD1 6639 N ND2 . ASN D 71 ? 0.3025 0.3688 0.5485 0.0491 0.0287 -0.1036 71 ASN D ND2 6640 N N . ASN D 72 ? 0.4641 0.3788 0.6609 0.1365 -0.1624 -0.1329 72 ASN D N 6641 C CA . ASN D 72 ? 0.5635 0.3736 0.6448 0.1453 -0.2066 -0.1078 72 ASN D CA 6642 C C . ASN D 72 ? 0.5624 0.3349 0.5451 0.1189 -0.1720 -0.0649 72 ASN D C 6643 O O . ASN D 72 ? 0.6585 0.3320 0.5315 0.1158 -0.1953 -0.0478 72 ASN D O 6644 C CB . ASN D 72 ? 0.6538 0.4043 0.7417 0.1788 -0.2878 -0.1396 72 ASN D CB 6645 C CG . ASN D 72 ? 0.6861 0.4186 0.7528 0.1770 -0.2981 -0.1362 72 ASN D CG 6646 O OD1 . ASN D 72 ? 0.8122 0.4379 0.7839 0.1897 -0.3551 -0.1307 72 ASN D OD1 6647 N ND2 . ASN D 72 ? 0.6124 0.4345 0.7530 0.1597 -0.2448 -0.1395 72 ASN D ND2 6648 N N . LEU D 73 ? 0.4768 0.3171 0.4943 0.0984 -0.1173 -0.0523 73 LEU D N 6649 C CA . LEU D 73 ? 0.4694 0.2904 0.4215 0.0736 -0.0795 -0.0203 73 LEU D CA 6650 C C . LEU D 73 ? 0.4149 0.2754 0.3789 0.0584 -0.0395 -0.0069 73 LEU D C 6651 O O . LEU D 73 ? 0.3935 0.2625 0.3435 0.0412 -0.0087 0.0080 73 LEU D O 6652 C CB . LEU D 73 ? 0.4479 0.2966 0.4213 0.0662 -0.0619 -0.0177 73 LEU D CB 6653 C CG . LEU D 73 ? 0.5201 0.3043 0.4449 0.0737 -0.0982 -0.0230 73 LEU D CG 6654 C CD1 . LEU D 73 ? 0.4843 0.3094 0.4478 0.0676 -0.0790 -0.0246 73 LEU D CD1 6655 C CD2 . LEU D 73 ? 0.6120 0.2944 0.4133 0.0569 -0.0980 -0.0045 73 LEU D CD2 6656 N N . GLU D 74 ? 0.3965 0.2784 0.3918 0.0666 -0.0452 -0.0177 74 GLU D N 6657 C CA . GLU D 74 ? 0.3582 0.2640 0.3555 0.0555 -0.0188 -0.0081 74 GLU D CA 6658 C C . GLU D 74 ? 0.4006 0.2593 0.3580 0.0601 -0.0378 -0.0092 74 GLU D C 6659 O O . GLU D 74 ? 0.3743 0.2563 0.3533 0.0607 -0.0311 -0.0141 74 GLU D O 6660 C CB . GLU D 74 ? 0.3145 0.2778 0.3727 0.0553 -0.0019 -0.0225 74 GLU D CB 6661 C CG . GLU D 74 ? 0.2860 0.2798 0.3656 0.0450 0.0221 -0.0203 74 GLU D CG 6662 C CD . GLU D 74 ? 0.2721 0.2950 0.3855 0.0353 0.0467 -0.0394 74 GLU D CD 6663 O OE1 . GLU D 74 ? 0.2720 0.3076 0.4236 0.0403 0.0434 -0.0666 74 GLU D OE1 6664 O OE2 . GLU D 74 ? 0.2693 0.2923 0.3650 0.0201 0.0706 -0.0305 74 GLU D OE2 6665 N N . ARG D 75 ? 0.4766 0.2554 0.3620 0.0611 -0.0617 -0.0048 75 ARG D N 6666 C CA . ARG D 75 ? 0.5530 0.2612 0.3787 0.0646 -0.0849 -0.0056 75 ARG D CA 6667 C C . ARG D 75 ? 0.5378 0.2475 0.3409 0.0415 -0.0470 0.0054 75 ARG D C 6668 O O . ARG D 75 ? 0.5520 0.2378 0.3388 0.0448 -0.0569 0.0019 75 ARG D O 6669 C CB . ARG D 75 ? 0.6865 0.2757 0.4051 0.0653 -0.1202 -0.0016 75 ARG D CB 6670 C CG . ARG D 75 ? 0.7372 0.3125 0.4798 0.0948 -0.1756 -0.0196 75 ARG D CG 6671 C CD . ARG D 75 ? 0.8064 0.3625 0.5810 0.1274 -0.2334 -0.0448 75 ARG D CD 6672 N NE . ARG D 75 ? 0.8586 0.4167 0.6935 0.1612 -0.2943 -0.0774 75 ARG D NE 6673 C CZ . ARG D 75 ? 0.9878 0.4432 0.7444 0.1755 -0.3532 -0.0801 75 ARG D CZ 6674 N NH1 . ARG D 75 ? 1.1106 0.4411 0.7053 0.1523 -0.3501 -0.0492 75 ARG D NH1 6675 N NH2 . ARG D 75 ? 1.0049 0.4786 0.8466 0.2105 -0.4139 -0.1197 75 ARG D NH2 6676 N N . ARG D 76 ? 0.4925 0.2330 0.3064 0.0199 -0.0068 0.0130 76 ARG D N 6677 C CA . ARG D 76 ? 0.4798 0.2301 0.2955 -0.0015 0.0266 0.0126 76 ARG D CA 6678 C C . ARG D 76 ? 0.4216 0.2390 0.3004 0.0087 0.0261 0.0092 76 ARG D C 6679 O O . ARG D 76 ? 0.4244 0.2276 0.2908 0.0024 0.0304 0.0055 76 ARG D O 6680 C CB . ARG D 76 ? 0.4504 0.2217 0.2860 -0.0232 0.0627 0.0092 76 ARG D CB 6681 C CG . ARG D 76 ? 0.5272 0.2124 0.2792 -0.0477 0.0802 0.0074 76 ARG D CG 6682 C CD . ARG D 76 ? 0.4935 0.2128 0.2880 -0.0666 0.1167 -0.0036 76 ARG D CD 6683 N NE . ARG D 76 ? 0.4129 0.1995 0.2710 -0.0430 0.0981 0.0039 76 ARG D NE 6684 C CZ . ARG D 76 ? 0.3504 0.2000 0.2842 -0.0428 0.1113 -0.0043 76 ARG D CZ 6685 N NH1 . ARG D 76 ? 0.3469 0.2160 0.3266 -0.0613 0.1401 -0.0271 76 ARG D NH1 6686 N NH2 . ARG D 76 ? 0.3033 0.1922 0.2710 -0.0239 0.0936 0.0050 76 ARG D NH2 6687 N N . ILE D 77 ? 0.3654 0.2427 0.2984 0.0205 0.0231 0.0095 77 ILE D N 6688 C CA . ILE D 77 ? 0.3386 0.2584 0.3065 0.0251 0.0245 0.0061 77 ILE D CA 6689 C C . ILE D 77 ? 0.3468 0.2624 0.3194 0.0370 0.0099 -0.0045 77 ILE D C 6690 O O . ILE D 77 ? 0.3393 0.2668 0.3182 0.0351 0.0141 -0.0088 77 ILE D O 6691 C CB . ILE D 77 ? 0.3160 0.2732 0.3118 0.0261 0.0308 0.0089 77 ILE D CB 6692 C CG1 . ILE D 77 ? 0.3182 0.2816 0.3268 0.0328 0.0279 0.0050 77 ILE D CG1 6693 C CG2 . ILE D 77 ? 0.3096 0.2741 0.3157 0.0186 0.0373 0.0131 77 ILE D CG2 6694 C CD1 . ILE D 77 ? 0.3121 0.2962 0.3323 0.0277 0.0403 0.0067 77 ILE D CD1 6695 N N . GLU D 78 ? 0.3703 0.2677 0.3460 0.0506 -0.0108 -0.0138 78 GLU D N 6696 C CA . GLU D 78 ? 0.3928 0.2833 0.3905 0.0666 -0.0335 -0.0345 78 GLU D CA 6697 C C . GLU D 78 ? 0.4307 0.2686 0.3789 0.0657 -0.0452 -0.0296 78 GLU D C 6698 O O . GLU D 78 ? 0.4223 0.2699 0.3912 0.0713 -0.0490 -0.0425 78 GLU D O 6699 C CB . GLU D 78 ? 0.4324 0.3046 0.4501 0.0865 -0.0681 -0.0520 78 GLU D CB 6700 C CG . GLU D 78 ? 0.4810 0.3373 0.5348 0.1104 -0.1071 -0.0831 78 GLU D CG 6701 C CD . GLU D 78 ? 0.5504 0.3737 0.6223 0.1357 -0.1590 -0.1047 78 GLU D CD 6702 O OE1 . GLU D 78 ? 0.6047 0.3906 0.6246 0.1325 -0.1678 -0.0866 78 GLU D OE1 6703 O OE2 . GLU D 78 ? 0.5876 0.4203 0.7312 0.1602 -0.1950 -0.1452 78 GLU D OE2 6704 N N . ASN D 79 ? 0.4786 0.2543 0.3566 0.0539 -0.0451 -0.0140 79 ASN D N 6705 C CA . ASN D 79 ? 0.5401 0.2483 0.3536 0.0441 -0.0471 -0.0102 79 ASN D CA 6706 C C . ASN D 79 ? 0.4979 0.2515 0.3378 0.0275 -0.0143 -0.0093 79 ASN D C 6707 O O . ASN D 79 ? 0.5103 0.2461 0.3392 0.0276 -0.0182 -0.0145 79 ASN D O 6708 C CB . ASN D 79 ? 0.6253 0.2405 0.3424 0.0242 -0.0416 0.0008 79 ASN D CB 6709 C CG . ASN D 79 ? 0.7170 0.2445 0.3501 0.0044 -0.0332 0.0023 79 ASN D CG 6710 O OD1 . ASN D 79 ? 0.7305 0.2582 0.3521 -0.0271 0.0119 0.0013 79 ASN D OD1 6711 N ND2 . ASN D 79 ? 0.7912 0.2429 0.3732 0.0227 -0.0774 -0.0008 79 ASN D ND2 6712 N N . LEU D 80 ? 0.4479 0.2550 0.3240 0.0159 0.0112 -0.0053 80 LEU D N 6713 C CA . LEU D 80 ? 0.4190 0.2709 0.3310 0.0067 0.0282 -0.0094 80 LEU D CA 6714 C C . LEU D 80 ? 0.3988 0.2832 0.3371 0.0198 0.0177 -0.0151 80 LEU D C 6715 O O . LEU D 80 ? 0.4052 0.2883 0.3421 0.0157 0.0195 -0.0208 80 LEU D O 6716 C CB . LEU D 80 ? 0.3832 0.2776 0.3328 0.0016 0.0396 -0.0080 80 LEU D CB 6717 C CG . LEU D 80 ? 0.3702 0.2975 0.3600 -0.0053 0.0444 -0.0186 80 LEU D CG 6718 C CD1 . LEU D 80 ? 0.3597 0.3092 0.3870 -0.0095 0.0502 -0.0243 80 LEU D CD1 6719 C CD2 . LEU D 80 ? 0.3574 0.3068 0.3543 0.0061 0.0273 -0.0168 80 LEU D CD2 6720 N N . ASN D 81 ? 0.3754 0.2851 0.3372 0.0309 0.0125 -0.0181 81 ASN D N 6721 C CA . ASN D 81 ? 0.3703 0.3013 0.3539 0.0355 0.0143 -0.0324 81 ASN D CA 6722 C C . ASN D 81 ? 0.4029 0.3105 0.3864 0.0447 0.0002 -0.0462 81 ASN D C 6723 O O . ASN D 81 ? 0.3981 0.3140 0.3857 0.0408 0.0072 -0.0551 81 ASN D O 6724 C CB . ASN D 81 ? 0.3580 0.3121 0.3738 0.0401 0.0194 -0.0445 81 ASN D CB 6725 C CG . ASN D 81 ? 0.3616 0.3347 0.4021 0.0345 0.0371 -0.0691 81 ASN D CG 6726 O OD1 . ASN D 81 ? 0.3849 0.3556 0.3961 0.0189 0.0553 -0.0654 81 ASN D OD1 6727 N ND2 . ASN D 81 ? 0.3628 0.3471 0.4560 0.0461 0.0302 -0.0996 81 ASN D ND2 6728 N N . LYS D 82 ? 0.4470 0.3140 0.4172 0.0576 -0.0245 -0.0486 82 LYS D N 6729 C CA . LYS D 82 ? 0.5057 0.3350 0.4724 0.0722 -0.0508 -0.0641 82 LYS D CA 6730 C C . LYS D 82 ? 0.5419 0.3349 0.4601 0.0592 -0.0434 -0.0536 82 LYS D C 6731 O O . LYS D 82 ? 0.5523 0.3418 0.4821 0.0649 -0.0498 -0.0673 82 LYS D O 6732 C CB . LYS D 82 ? 0.5698 0.3356 0.5103 0.0918 -0.0939 -0.0682 82 LYS D CB 6733 C CG . LYS D 82 ? 0.6405 0.3441 0.5633 0.1110 -0.1349 -0.0842 82 LYS D CG 6734 C CD . LYS D 82 ? 0.7107 0.3600 0.6362 0.1420 -0.1957 -0.1029 82 LYS D CD 6735 C CE . LYS D 82 ? 0.7725 0.3762 0.7169 0.1707 -0.2474 -0.1325 82 LYS D CE 6736 N NZ . LYS D 82 ? 0.9040 0.3606 0.7158 0.1763 -0.2949 -0.1141 82 LYS D NZ 6737 N N . LYS D 83 ? 0.5657 0.3331 0.4380 0.0395 -0.0263 -0.0355 83 LYS D N 6738 C CA . LYS D 83 ? 0.5950 0.3289 0.4296 0.0200 -0.0103 -0.0329 83 LYS D CA 6739 C C . LYS D 83 ? 0.5461 0.3419 0.4264 0.0139 0.0060 -0.0395 83 LYS D C 6740 O O . LYS D 83 ? 0.5675 0.3469 0.4371 0.0084 0.0082 -0.0462 83 LYS D O 6741 C CB . LYS D 83 ? 0.6268 0.3238 0.4187 -0.0061 0.0148 -0.0251 83 LYS D CB 6742 C CG . LYS D 83 ? 0.7249 0.3123 0.4217 -0.0114 0.0017 -0.0185 83 LYS D CG 6743 N N . MET D 84 ? 0.4976 0.3508 0.4165 0.0147 0.0135 -0.0377 84 MET D N 6744 C CA . MET D 84 ? 0.4794 0.3672 0.4179 0.0099 0.0184 -0.0435 84 MET D CA 6745 C C . MET D 84 ? 0.4835 0.3763 0.4264 0.0173 0.0155 -0.0557 84 MET D C 6746 O O . MET D 84 ? 0.4851 0.3802 0.4233 0.0112 0.0175 -0.0623 84 MET D O 6747 C CB . MET D 84 ? 0.4634 0.3822 0.4172 0.0081 0.0188 -0.0381 84 MET D CB 6748 C CG . MET D 84 ? 0.4735 0.4042 0.4217 0.0122 0.0200 -0.0377 84 MET D CG 6749 S SD . MET D 84 ? 0.5169 0.4375 0.4342 0.0043 0.0194 -0.0461 84 MET D SD 6750 C CE . MET D 84 ? 0.5385 0.4519 0.4326 -0.0032 0.0391 -0.0492 84 MET D CE 6751 N N . GLU D 85 ? 0.4835 0.3792 0.4442 0.0294 0.0114 -0.0653 85 GLU D N 6752 C CA . GLU D 85 ? 0.4934 0.4000 0.4771 0.0327 0.0168 -0.0889 85 GLU D CA 6753 C C . GLU D 85 ? 0.5272 0.4022 0.5080 0.0418 0.0004 -0.0986 85 GLU D C 6754 O O . GLU D 85 ? 0.5294 0.4076 0.5108 0.0362 0.0086 -0.1103 85 GLU D O 6755 C CB . GLU D 85 ? 0.4889 0.4188 0.5185 0.0399 0.0225 -0.1104 85 GLU D CB 6756 C CG . GLU D 85 ? 0.4895 0.4386 0.5067 0.0230 0.0485 -0.1053 85 GLU D CG 6757 C CD . GLU D 85 ? 0.5066 0.4785 0.5700 0.0165 0.0741 -0.1397 85 GLU D CD 6758 O OE1 . GLU D 85 ? 0.5112 0.4989 0.6431 0.0339 0.0610 -0.1691 85 GLU D OE1 6759 O OE2 . GLU D 85 ? 0.5241 0.4896 0.5532 -0.0074 0.1064 -0.1421 85 GLU D OE2 6760 N N . ASP D 86 ? 0.5591 0.3898 0.5225 0.0542 -0.0244 -0.0930 86 ASP D N 6761 C CA . ASP D 86 ? 0.6243 0.3959 0.5549 0.0599 -0.0443 -0.0961 86 ASP D CA 6762 C C . ASP D 86 ? 0.6182 0.3795 0.5129 0.0374 -0.0234 -0.0846 86 ASP D C 6763 O O . ASP D 86 ? 0.6360 0.3756 0.5220 0.0369 -0.0267 -0.0941 86 ASP D O 6764 C CB . ASP D 86 ? 0.7024 0.3950 0.5806 0.0707 -0.0765 -0.0866 86 ASP D CB 6765 C CG . ASP D 86 ? 0.7340 0.4129 0.6536 0.1033 -0.1203 -0.1118 86 ASP D CG 6766 O OD1 . ASP D 86 ? 0.7659 0.4420 0.7234 0.1196 -0.1394 -0.1384 86 ASP D OD1 6767 O OD2 . ASP D 86 ? 0.7385 0.4103 0.6614 0.1136 -0.1383 -0.1100 86 ASP D OD2 6768 N N . GLY D 87 ? 0.5814 0.3614 0.4674 0.0198 -0.0039 -0.0703 87 GLY D N 6769 C CA . GLY D 87 ? 0.5801 0.3628 0.4589 -0.0010 0.0139 -0.0709 87 GLY D CA 6770 C C . GLY D 87 ? 0.5525 0.3700 0.4549 -0.0010 0.0154 -0.0828 87 GLY D C 6771 O O . GLY D 87 ? 0.5715 0.3692 0.4636 -0.0088 0.0182 -0.0913 87 GLY D O 6772 N N . PHE D 88 ? 0.5130 0.3703 0.4345 0.0039 0.0157 -0.0843 88 PHE D N 6773 C CA . PHE D 88 ? 0.5128 0.3829 0.4320 -0.0003 0.0186 -0.0961 88 PHE D CA 6774 C C . PHE D 88 ? 0.5296 0.3856 0.4552 0.0062 0.0200 -0.1135 88 PHE D C 6775 O O . PHE D 88 ? 0.5458 0.3954 0.4628 -0.0002 0.0221 -0.1233 88 PHE D O 6776 C CB . PHE D 88 ? 0.5034 0.3893 0.4111 -0.0038 0.0236 -0.0947 88 PHE D CB 6777 C CG . PHE D 88 ? 0.4972 0.3868 0.3944 -0.0080 0.0098 -0.0837 88 PHE D CG 6778 C CD1 . PHE D 88 ? 0.5069 0.3917 0.4016 -0.0125 -0.0065 -0.0907 88 PHE D CD1 6779 C CD2 . PHE D 88 ? 0.4799 0.3777 0.3792 -0.0049 0.0080 -0.0718 88 PHE D CD2 6780 C CE1 . PHE D 88 ? 0.5110 0.3994 0.4144 -0.0106 -0.0308 -0.0905 88 PHE D CE1 6781 C CE2 . PHE D 88 ? 0.4830 0.3813 0.3824 -0.0044 -0.0124 -0.0673 88 PHE D CE2 6782 C CZ . PHE D 88 ? 0.5023 0.3962 0.4084 -0.0056 -0.0351 -0.0790 88 PHE D CZ 6783 N N . LEU D 89 ? 0.5281 0.3783 0.4762 0.0214 0.0134 -0.1218 89 LEU D N 6784 C CA . LEU D 89 ? 0.5534 0.3911 0.5265 0.0332 0.0064 -0.1471 89 LEU D CA 6785 C C . LEU D 89 ? 0.5940 0.3835 0.5361 0.0336 -0.0076 -0.1426 89 LEU D C 6786 O O . LEU D 89 ? 0.6044 0.3903 0.5526 0.0319 -0.0042 -0.1591 89 LEU D O 6787 C CB . LEU D 89 ? 0.5545 0.3929 0.5739 0.0552 -0.0114 -0.1652 89 LEU D CB 6788 C CG . LEU D 89 ? 0.5261 0.4138 0.5890 0.0494 0.0130 -0.1828 89 LEU D CG 6789 C CD1 . LEU D 89 ? 0.5264 0.4199 0.6514 0.0731 -0.0104 -0.2061 89 LEU D CD1 6790 C CD2 . LEU D 89 ? 0.5351 0.4459 0.6160 0.0317 0.0486 -0.2134 89 LEU D CD2 6791 N N . ASP D 90 ? 0.6277 0.3728 0.5285 0.0304 -0.0171 -0.1224 90 ASP D N 6792 C CA . ASP D 90 ? 0.6882 0.3694 0.5402 0.0205 -0.0202 -0.1186 90 ASP D CA 6793 C C . ASP D 90 ? 0.6706 0.3801 0.5283 -0.0005 0.0023 -0.1231 90 ASP D C 6794 O O . ASP D 90 ? 0.7005 0.3807 0.5445 -0.0044 0.0017 -0.1331 90 ASP D O 6795 C CB . ASP D 90 ? 0.7419 0.3589 0.5329 0.0084 -0.0195 -0.1001 90 ASP D CB 6796 C CG . ASP D 90 ? 0.8048 0.3567 0.5628 0.0313 -0.0565 -0.0968 90 ASP D CG 6797 O OD1 . ASP D 90 ? 0.8227 0.3714 0.6138 0.0594 -0.0889 -0.1149 90 ASP D OD1 6798 O OD2 . ASP D 90 ? 0.8562 0.3557 0.5576 0.0213 -0.0557 -0.0811 90 ASP D OD2 6799 N N . VAL D 91 ? 0.6272 0.3883 0.5060 -0.0115 0.0155 -0.1185 91 VAL D N 6800 C CA . VAL D 91 ? 0.6148 0.4029 0.5068 -0.0259 0.0229 -0.1283 91 VAL D CA 6801 C C . VAL D 91 ? 0.6200 0.4174 0.5143 -0.0208 0.0201 -0.1426 91 VAL D C 6802 O O . VAL D 91 ? 0.6379 0.4232 0.5276 -0.0292 0.0220 -0.1540 91 VAL D O 6803 C CB . VAL D 91 ? 0.5813 0.4124 0.4949 -0.0296 0.0200 -0.1244 91 VAL D CB 6804 C CG1 . VAL D 91 ? 0.5870 0.4359 0.5089 -0.0355 0.0091 -0.1386 91 VAL D CG1 6805 C CG2 . VAL D 91 ? 0.5768 0.4049 0.5041 -0.0412 0.0301 -0.1216 91 VAL D CG2 6806 N N . TRP D 92 ? 0.6061 0.4224 0.5078 -0.0114 0.0217 -0.1466 92 TRP D N 6807 C CA . TRP D 92 ? 0.6278 0.4487 0.5274 -0.0145 0.0310 -0.1669 92 TRP D CA 6808 C C . TRP D 92 ? 0.6506 0.4502 0.5697 -0.0041 0.0284 -0.1856 92 TRP D C 6809 O O . TRP D 92 ? 0.6713 0.4666 0.5873 -0.0104 0.0359 -0.2036 92 TRP D O 6810 C CB . TRP D 92 ? 0.6205 0.4586 0.5176 -0.0181 0.0469 -0.1741 92 TRP D CB 6811 C CG . TRP D 92 ? 0.6302 0.4647 0.4820 -0.0308 0.0431 -0.1602 92 TRP D CG 6812 C CD1 . TRP D 92 ? 0.6137 0.4556 0.4586 -0.0291 0.0377 -0.1432 92 TRP D CD1 6813 C CD2 . TRP D 92 ? 0.6725 0.4829 0.4739 -0.0439 0.0345 -0.1639 92 TRP D CD2 6814 N NE1 . TRP D 92 ? 0.6509 0.4705 0.4441 -0.0384 0.0226 -0.1366 92 TRP D NE1 6815 C CE2 . TRP D 92 ? 0.6912 0.4875 0.4537 -0.0468 0.0169 -0.1492 92 TRP D CE2 6816 C CE3 . TRP D 92 ? 0.7070 0.4992 0.4885 -0.0521 0.0347 -0.1796 92 TRP D CE3 6817 C CZ2 . TRP D 92 ? 0.7554 0.5105 0.4548 -0.0546 -0.0093 -0.1506 92 TRP D CZ2 6818 C CZ3 . TRP D 92 ? 0.7622 0.5195 0.4816 -0.0626 0.0142 -0.1804 92 TRP D CZ3 6819 C CH2 . TRP D 92 ? 0.7931 0.5276 0.4694 -0.0624 -0.0117 -0.1663 92 TRP D CH2 6820 N N . THR D 93 ? 0.6593 0.4356 0.5920 0.0132 0.0119 -0.1826 93 THR D N 6821 C CA . THR D 93 ? 0.6955 0.4295 0.6368 0.0288 -0.0069 -0.1987 93 THR D CA 6822 C C . THR D 93 ? 0.7361 0.4296 0.6347 0.0146 -0.0057 -0.1909 93 THR D C 6823 O O . THR D 93 ? 0.7642 0.4420 0.6682 0.0164 -0.0074 -0.2093 93 THR D O 6824 C CB . THR D 93 ? 0.7165 0.4067 0.6552 0.0514 -0.0391 -0.1932 93 THR D CB 6825 O OG1 . THR D 93 ? 0.6742 0.4096 0.6717 0.0652 -0.0401 -0.2102 93 THR D OG1 6826 C CG2 . THR D 93 ? 0.7851 0.4055 0.7145 0.0714 -0.0737 -0.2089 93 THR D CG2 6827 N N . TYR D 94 ? 0.7412 0.4202 0.6053 -0.0022 0.0015 -0.1696 94 TYR D N 6828 C CA . TYR D 94 ? 0.7760 0.4240 0.6115 -0.0238 0.0131 -0.1700 94 TYR D CA 6829 C C . TYR D 94 ? 0.7580 0.4487 0.6171 -0.0327 0.0222 -0.1861 94 TYR D C 6830 O O . TYR D 94 ? 0.7894 0.4529 0.6383 -0.0389 0.0242 -0.1983 94 TYR D O 6831 C CB . TYR D 94 ? 0.7736 0.4188 0.5954 -0.0456 0.0297 -0.1579 94 TYR D CB 6832 C CG . TYR D 94 ? 0.8047 0.4348 0.6223 -0.0748 0.0516 -0.1710 94 TYR D CG 6833 C CD1 . TYR D 94 ? 0.8838 0.4256 0.6424 -0.0941 0.0657 -0.1722 94 TYR D CD1 6834 C CD2 . TYR D 94 ? 0.7671 0.4610 0.6358 -0.0846 0.0559 -0.1865 94 TYR D CD2 6835 C CE1 . TYR D 94 ? 0.9166 0.4465 0.6799 -0.1274 0.0956 -0.1922 94 TYR D CE1 6836 C CE2 . TYR D 94 ? 0.7874 0.4772 0.6750 -0.1108 0.0744 -0.2090 94 TYR D CE2 6837 C CZ . TYR D 94 ? 0.8588 0.4730 0.7003 -0.1347 0.1002 -0.2136 94 TYR D CZ 6838 O OH . TYR D 94 ? 0.8876 0.4998 0.7564 -0.1668 0.1278 -0.2436 94 TYR D OH 6839 N N . ASN D 95 ? 0.7263 0.4701 0.6037 -0.0342 0.0247 -0.1862 95 ASN D N 6840 C CA . ASN D 95 ? 0.7363 0.5002 0.6118 -0.0439 0.0258 -0.2003 95 ASN D CA 6841 C C . ASN D 95 ? 0.7663 0.5202 0.6396 -0.0397 0.0321 -0.2200 95 ASN D C 6842 O O . ASN D 95 ? 0.7805 0.5251 0.6448 -0.0492 0.0334 -0.2338 95 ASN D O 6843 C CB . ASN D 95 ? 0.7209 0.5128 0.5872 -0.0462 0.0193 -0.1944 95 ASN D CB 6844 C CG . ASN D 95 ? 0.7080 0.5159 0.5933 -0.0511 0.0071 -0.1874 95 ASN D CG 6845 O OD1 . ASN D 95 ? 0.7113 0.5156 0.6206 -0.0610 0.0112 -0.1957 95 ASN D OD1 6846 N ND2 . ASN D 95 ? 0.6963 0.5186 0.5745 -0.0468 -0.0049 -0.1777 95 ASN D ND2 6847 N N . ALA D 96 ? 0.7628 0.5213 0.6550 -0.0262 0.0370 -0.2277 96 ALA D N 6848 C CA . ALA D 96 ? 0.7847 0.5411 0.6975 -0.0227 0.0481 -0.2581 96 ALA D CA 6849 C C . ALA D 96 ? 0.8163 0.5350 0.7367 -0.0136 0.0346 -0.2672 96 ALA D C 6850 O O . ALA D 96 ? 0.8358 0.5478 0.7537 -0.0212 0.0429 -0.2866 96 ALA D O 6851 C CB . ALA D 96 ? 0.7710 0.5474 0.7302 -0.0094 0.0555 -0.2760 96 ALA D CB 6852 N N . GLU D 97 ? 0.8348 0.5151 0.7505 0.0009 0.0127 -0.2532 97 GLU D N 6853 C CA . GLU D 97 ? 0.8937 0.5096 0.7925 0.0093 -0.0056 -0.2593 97 GLU D CA 6854 C C . GLU D 97 ? 0.9163 0.5130 0.7774 -0.0156 0.0079 -0.2533 97 GLU D C 6855 O O . GLU D 97 ? 0.9477 0.5142 0.8042 -0.0160 0.0058 -0.2693 97 GLU D O 6856 C CB . GLU D 97 ? 0.9340 0.4818 0.7995 0.0250 -0.0353 -0.2419 97 GLU D CB 6857 C CG . GLU D 97 ? 0.9389 0.4873 0.8545 0.0588 -0.0660 -0.2609 97 GLU D CG 6858 C CD . GLU D 97 ? 1.0034 0.4679 0.8657 0.0748 -0.1050 -0.2414 97 GLU D CD 6859 O OE1 . GLU D 97 ? 1.0771 0.4551 0.8491 0.0586 -0.1072 -0.2187 97 GLU D OE1 6860 O OE2 . GLU D 97 ? 0.9931 0.4700 0.8977 0.1001 -0.1313 -0.2519 97 GLU D OE2 6861 N N . LEU D 98 ? 0.9023 0.5192 0.7479 -0.0357 0.0209 -0.2361 98 LEU D N 6862 C CA . LEU D 98 ? 0.9324 0.5407 0.7647 -0.0610 0.0343 -0.2405 98 LEU D CA 6863 C C . LEU D 98 ? 0.9281 0.5721 0.7775 -0.0667 0.0376 -0.2606 98 LEU D C 6864 O O . LEU D 98 ? 0.9615 0.5811 0.8037 -0.0777 0.0422 -0.2744 98 LEU D O 6865 C CB . LEU D 98 ? 0.9087 0.5437 0.7495 -0.0788 0.0446 -0.2311 98 LEU D CB 6866 C CG . LEU D 98 ? 0.9260 0.5673 0.7835 -0.1060 0.0589 -0.2498 98 LEU D CG 6867 C CD1 . LEU D 98 ? 0.9977 0.5602 0.8145 -0.1248 0.0772 -0.2552 98 LEU D CD1 6868 C CD2 . LEU D 98 ? 0.8987 0.5806 0.7949 -0.1197 0.0653 -0.2538 98 LEU D CD2 6869 N N . LEU D 99 ? 0.9031 0.5920 0.7617 -0.0626 0.0366 -0.2628 99 LEU D N 6870 C CA . LEU D 99 ? 0.9262 0.6282 0.7734 -0.0722 0.0386 -0.2810 99 LEU D CA 6871 C C . LEU D 99 ? 0.9565 0.6374 0.8078 -0.0679 0.0482 -0.3034 99 LEU D C 6872 O O . LEU D 99 ? 0.9853 0.6585 0.8233 -0.0797 0.0510 -0.3202 99 LEU D O 6873 C CB . LEU D 99 ? 0.9204 0.6432 0.7449 -0.0739 0.0386 -0.2778 99 LEU D CB 6874 C CG . LEU D 99 ? 0.9790 0.6869 0.7560 -0.0887 0.0382 -0.2948 99 LEU D CG 6875 C CD1 . LEU D 99 ? 0.9963 0.7001 0.7704 -0.0968 0.0127 -0.3006 99 LEU D CD1 6876 C CD2 . LEU D 99 ? 1.0098 0.7078 0.7343 -0.0954 0.0403 -0.2886 99 LEU D CD2 6877 N N . VAL D 100 ? 0.9529 0.6239 0.8297 -0.0492 0.0485 -0.3085 100 VAL D N 6878 C CA . VAL D 100 ? 0.9846 0.6373 0.8867 -0.0393 0.0514 -0.3379 100 VAL D CA 6879 C C . VAL D 100 ? 1.0240 0.6263 0.9090 -0.0408 0.0399 -0.3372 100 VAL D C 6880 O O . VAL D 100 ? 1.0540 0.6472 0.9415 -0.0467 0.0469 -0.3596 100 VAL D O 6881 C CB . VAL D 100 ? 0.9770 0.6305 0.9304 -0.0127 0.0416 -0.3525 100 VAL D CB 6882 C CG1 . VAL D 100 ? 1.0186 0.6437 1.0131 0.0047 0.0304 -0.3877 100 VAL D CG1 6883 C CG2 . VAL D 100 ? 0.9504 0.6529 0.9280 -0.0194 0.0675 -0.3679 100 VAL D CG2 6884 N N . LEU D 101 ? 1.0391 0.5996 0.8977 -0.0400 0.0271 -0.3135 101 LEU D N 6885 C CA . LEU D 101 ? 1.0982 0.5910 0.9198 -0.0508 0.0245 -0.3122 101 LEU D CA 6886 C C . LEU D 101 ? 1.1013 0.6191 0.9207 -0.0790 0.0435 -0.3215 101 LEU D C 6887 O O . LEU D 101 ? 1.1346 0.6174 0.9429 -0.0875 0.0471 -0.3363 101 LEU D O 6888 C CB . LEU D 101 ? 1.1295 0.5594 0.9018 -0.0568 0.0195 -0.2869 101 LEU D CB 6889 C CG . LEU D 101 ? 1.1644 0.5379 0.9199 -0.0266 -0.0132 -0.2787 101 LEU D CG 6890 C CD1 . LEU D 101 ? 1.1813 0.5190 0.8883 -0.0366 -0.0114 -0.2512 101 LEU D CD1 6891 C CD2 . LEU D 101 ? 1.2611 0.5298 0.9748 -0.0124 -0.0417 -0.2886 101 LEU D CD2 6892 N N . MET D 102 ? 1.0671 0.6412 0.9000 -0.0911 0.0493 -0.3158 102 MET D N 6893 C CA . MET D 102 ? 1.0773 0.6774 0.9199 -0.1122 0.0532 -0.3312 102 MET D CA 6894 C C . MET D 102 ? 1.0850 0.6974 0.9229 -0.1109 0.0511 -0.3518 102 MET D C 6895 O O . MET D 102 ? 1.1091 0.7090 0.9461 -0.1240 0.0532 -0.3702 102 MET D O 6896 C CB . MET D 102 ? 1.0515 0.6994 0.9138 -0.1183 0.0452 -0.3250 102 MET D CB 6897 C CG . MET D 102 ? 1.0643 0.7018 0.9423 -0.1334 0.0582 -0.3197 102 MET D CG 6898 S SD . MET D 102 ? 1.0313 0.7244 0.9453 -0.1310 0.0464 -0.3120 102 MET D SD 6899 C CE . MET D 102 ? 1.0294 0.7627 0.9610 -0.1277 0.0116 -0.3340 102 MET D CE 6900 N N . GLU D 103 ? 1.0670 0.6982 0.8984 -0.0997 0.0523 -0.3526 103 GLU D N 6901 C CA . GLU D 103 ? 1.0922 0.7223 0.9050 -0.1059 0.0614 -0.3765 103 GLU D CA 6902 C C . GLU D 103 ? 1.1196 0.7220 0.9507 -0.1002 0.0712 -0.3984 103 GLU D C 6903 O O . GLU D 103 ? 1.1593 0.7520 0.9760 -0.1120 0.0783 -0.4206 103 GLU D O 6904 C CB . GLU D 103 ? 1.0902 0.7348 0.8871 -0.1043 0.0746 -0.3789 103 GLU D CB 6905 N N . ASN D 104 ? 1.1150 0.6957 0.9733 -0.0803 0.0654 -0.3941 104 ASN D N 6906 C CA . ASN D 104 ? 1.1564 0.6976 1.0333 -0.0686 0.0621 -0.4164 104 ASN D CA 6907 C C . ASN D 104 ? 1.2065 0.7089 1.0567 -0.0848 0.0609 -0.4171 104 ASN D C 6908 O O . ASN D 104 ? 1.2467 0.7348 1.1020 -0.0879 0.0668 -0.4424 104 ASN D O 6909 C CB . ASN D 104 ? 1.1599 0.6629 1.0572 -0.0394 0.0382 -0.4105 104 ASN D CB 6910 C CG . ASN D 104 ? 1.1240 0.6657 1.0805 -0.0191 0.0397 -0.4331 104 ASN D CG 6911 O OD1 . ASN D 104 ? 1.0957 0.6858 1.0691 -0.0328 0.0694 -0.4541 104 ASN D OD1 6912 N ND2 . ASN D 104 ? 1.1324 0.6424 1.1154 0.0110 0.0077 -0.4332 104 ASN D ND2 6913 N N . GLU D 105 ? 1.2188 0.7046 1.0454 -0.0986 0.0588 -0.3947 105 GLU D N 6914 C CA . GLU D 105 ? 1.2703 0.7210 1.0783 -0.1220 0.0669 -0.4012 105 GLU D CA 6915 C C . GLU D 105 ? 1.2588 0.7532 1.0789 -0.1392 0.0720 -0.4229 105 GLU D C 6916 O O . GLU D 105 ? 1.2906 0.7604 1.1066 -0.1494 0.0773 -0.4428 105 GLU D O 6917 C CB . GLU D 105 ? 1.2925 0.7255 1.0851 -0.1410 0.0757 -0.3835 105 GLU D CB 6918 C CG . GLU D 105 ? 1.3668 0.7444 1.1379 -0.1717 0.0955 -0.3957 105 GLU D CG 6919 C CD . GLU D 105 ? 1.4217 0.7512 1.1613 -0.1945 0.1157 -0.3823 105 GLU D CD 6920 O OE1 . GLU D 105 ? 1.4825 0.7337 1.1627 -0.1831 0.1074 -0.3604 105 GLU D OE1 6921 O OE2 . GLU D 105 ? 1.4197 0.7857 1.1955 -0.2242 0.1383 -0.3986 105 GLU D OE2 6922 N N . ARG D 106 ? 1.2115 0.7588 1.0371 -0.1414 0.0649 -0.4193 106 ARG D N 6923 C CA . ARG D 106 ? 1.2243 0.7938 1.0405 -0.1541 0.0558 -0.4391 106 ARG D CA 6924 C C . ARG D 106 ? 1.2581 0.8123 1.0506 -0.1523 0.0661 -0.4595 106 ARG D C 6925 O O . ARG D 106 ? 1.2976 0.8422 1.0741 -0.1657 0.0630 -0.4811 106 ARG D O 6926 C CB . ARG D 106 ? 1.2037 0.8069 1.0094 -0.1529 0.0355 -0.4292 106 ARG D CB 6927 N N . THR D 107 ? 1.2483 0.8007 1.0469 -0.1371 0.0798 -0.4593 107 THR D N 6928 C CA . THR D 107 ? 1.2800 0.8225 1.0746 -0.1387 0.1002 -0.4899 107 THR D CA 6929 C C . THR D 107 ? 1.3072 0.8182 1.1256 -0.1350 0.1032 -0.5105 107 THR D C 6930 O O . THR D 107 ? 1.3502 0.8514 1.1567 -0.1467 0.1170 -0.5394 107 THR D O 6931 C CB . THR D 107 ? 1.2626 0.8210 1.0859 -0.1245 0.1173 -0.4976 107 THR D CB 6932 O OG1 . THR D 107 ? 1.2568 0.8354 1.0477 -0.1310 0.1176 -0.4784 107 THR D OG1 6933 C CG2 . THR D 107 ? 1.3043 0.8577 1.1372 -0.1335 0.1497 -0.5422 107 THR D CG2 6934 N N . LEU D 108 ? 1.2994 0.7808 1.1382 -0.1208 0.0902 -0.4965 108 LEU D N 6935 C CA . LEU D 108 ? 1.3417 0.7722 1.1864 -0.1175 0.0873 -0.5127 108 LEU D CA 6936 C C . LEU D 108 ? 1.3634 0.7841 1.1836 -0.1445 0.0917 -0.5180 108 LEU D C 6937 O O . LEU D 108 ? 1.4019 0.7995 1.2221 -0.1501 0.0978 -0.5427 108 LEU D O 6938 C CB . LEU D 108 ? 1.3658 0.7353 1.2066 -0.0980 0.0670 -0.4943 108 LEU D CB 6939 C CG . LEU D 108 ? 1.3576 0.7281 1.2382 -0.0639 0.0501 -0.5002 108 LEU D CG 6940 C CD1 . LEU D 108 ? 1.4011 0.6945 1.2490 -0.0465 0.0191 -0.4740 108 LEU D CD1 6941 C CD2 . LEU D 108 ? 1.3823 0.7514 1.3176 -0.0465 0.0501 -0.5458 108 LEU D CD2 6942 N N . ASP D 109 ? 1.3377 0.7797 1.1489 -0.1608 0.0878 -0.5014 109 ASP D N 6943 C CA . ASP D 109 ? 1.3559 0.8036 1.1669 -0.1864 0.0880 -0.5172 109 ASP D CA 6944 C C . ASP D 109 ? 1.3658 0.8407 1.1603 -0.1935 0.0805 -0.5387 109 ASP D C 6945 O O . ASP D 109 ? 1.3982 0.8666 1.1914 -0.2096 0.0765 -0.5615 109 ASP D O 6946 C CB . ASP D 109 ? 1.3295 0.8013 1.1597 -0.2003 0.0839 -0.5063 109 ASP D CB 6947 C CG . ASP D 109 ? 1.3499 0.7709 1.1723 -0.2071 0.1008 -0.4904 109 ASP D CG 6948 O OD1 . ASP D 109 ? 1.4049 0.7564 1.1984 -0.2070 0.1095 -0.4919 109 ASP D OD1 6949 O OD2 . ASP D 109 ? 1.3271 0.7660 1.1627 -0.2142 0.1043 -0.4779 109 ASP D OD2 6950 N N . PHE D 110 ? 1.3534 0.8469 1.1246 -0.1848 0.0796 -0.5332 110 PHE D N 6951 C CA . PHE D 110 ? 1.3937 0.8825 1.1132 -0.1970 0.0764 -0.5520 110 PHE D CA 6952 C C . PHE D 110 ? 1.4440 0.9057 1.1550 -0.2029 0.1004 -0.5824 110 PHE D C 6953 O O . PHE D 110 ? 1.4988 0.9403 1.1665 -0.2202 0.0962 -0.6041 110 PHE D O 6954 C CB . PHE D 110 ? 1.3878 0.8841 1.0687 -0.1936 0.0803 -0.5393 110 PHE D CB 6955 C CG . PHE D 110 ? 1.4609 0.9212 1.0544 -0.2133 0.0845 -0.5581 110 PHE D CG 6956 C CD1 . PHE D 110 ? 1.5123 0.9465 1.0468 -0.2248 0.0450 -0.5622 110 PHE D CD1 6957 C CD2 . PHE D 110 ? 1.4924 0.9351 1.0590 -0.2225 0.1272 -0.5771 110 PHE D CD2 6958 C CE1 . PHE D 110 ? 1.6147 0.9861 1.0357 -0.2458 0.0438 -0.5774 110 PHE D CE1 6959 C CE2 . PHE D 110 ? 1.5899 0.9774 1.0506 -0.2505 0.1412 -0.5965 110 PHE D CE2 6960 C CZ . PHE D 110 ? 1.6598 1.0016 1.0326 -0.2624 0.0973 -0.5926 110 PHE D CZ 6961 N N . HIS D 111 ? 1.4311 0.8877 1.1850 -0.1868 0.1203 -0.5878 111 HIS D N 6962 C CA . HIS D 111 ? 1.4696 0.9036 1.2376 -0.1881 0.1413 -0.6231 111 HIS D CA 6963 C C . HIS D 111 ? 1.4918 0.8980 1.2690 -0.1937 0.1315 -0.6301 111 HIS D C 6964 O O . HIS D 111 ? 1.5367 0.9245 1.3046 -0.2047 0.1435 -0.6603 111 HIS D O 6965 C CB . HIS D 111 ? 1.4548 0.8911 1.2840 -0.1630 0.1536 -0.6358 111 HIS D CB 6966 C CG . HIS D 111 ? 1.4481 0.9129 1.2804 -0.1645 0.1769 -0.6458 111 HIS D CG 6967 N ND1 . HIS D 111 ? 1.4975 0.9576 1.2809 -0.1927 0.2114 -0.6741 111 HIS D ND1 6968 C CD2 . HIS D 111 ? 1.4059 0.8945 1.2767 -0.1457 0.1747 -0.6343 111 HIS D CD2 6969 C CE1 . HIS D 111 ? 1.4887 0.9679 1.2806 -0.1948 0.2355 -0.6810 111 HIS D CE1 6970 N NE2 . HIS D 111 ? 1.4250 0.9294 1.2791 -0.1643 0.2119 -0.6579 111 HIS D NE2 6971 N N . ASP D 112 ? 1.4710 0.8681 1.2618 -0.1910 0.1158 -0.6058 112 ASP D N 6972 C CA . ASP D 112 ? 1.5055 0.8704 1.2980 -0.2059 0.1143 -0.6146 112 ASP D CA 6973 C C . ASP D 112 ? 1.5188 0.9056 1.2956 -0.2300 0.1055 -0.6323 112 ASP D C 6974 O O . ASP D 112 ? 1.5540 0.9198 1.3284 -0.2431 0.1099 -0.6573 112 ASP D O 6975 C CB . ASP D 112 ? 1.5031 0.8403 1.3008 -0.2082 0.1116 -0.5897 112 ASP D CB 6976 C CG . ASP D 112 ? 1.5556 0.8155 1.3425 -0.1936 0.1119 -0.5856 112 ASP D CG 6977 O OD1 . ASP D 112 ? 1.6107 0.8334 1.3963 -0.1934 0.1149 -0.6089 112 ASP D OD1 6978 O OD2 . ASP D 112 ? 1.5592 0.7847 1.3313 -0.1817 0.1040 -0.5600 112 ASP D OD2 6979 N N . SER D 113 ? 1.4945 0.9176 1.2608 -0.2331 0.0865 -0.6216 113 SER D N 6980 C CA . SER D 113 ? 1.5224 0.9576 1.2727 -0.2489 0.0594 -0.6415 113 SER D CA 6981 C C . SER D 113 ? 1.5907 0.9971 1.2815 -0.2576 0.0612 -0.6662 113 SER D C 6982 O O . SER D 113 ? 1.6278 1.0222 1.3093 -0.2717 0.0441 -0.6919 113 SER D O 6983 C CB . SER D 113 ? 1.4961 0.9603 1.2367 -0.2432 0.0281 -0.6258 113 SER D CB 6984 O OG . SER D 113 ? 1.5353 0.9972 1.2556 -0.2518 -0.0146 -0.6489 113 SER D OG 6985 N N . ASN D 114 ? 1.6118 1.0050 1.2649 -0.2524 0.0854 -0.6639 114 ASN D N 6986 C CA . ASN D 114 ? 1.6921 1.0481 1.2769 -0.2685 0.1010 -0.6918 114 ASN D CA 6987 C C . ASN D 114 ? 1.7200 1.0579 1.3321 -0.2740 0.1237 -0.7212 114 ASN D C 6988 O O . ASN D 114 ? 1.7951 1.0992 1.3516 -0.2928 0.1312 -0.7494 114 ASN D O 6989 C CB . ASN D 114 ? 1.7072 1.0561 1.2578 -0.2689 0.1348 -0.6915 114 ASN D CB 6990 C CG . ASN D 114 ? 1.7158 1.0630 1.2097 -0.2696 0.1130 -0.6658 114 ASN D CG 6991 O OD1 . ASN D 114 ? 1.7506 1.0835 1.2007 -0.2735 0.0666 -0.6578 114 ASN D OD1 6992 N ND2 . ASN D 114 ? 1.6968 1.0568 1.1977 -0.2643 0.1423 -0.6572 114 ASN D ND2 6993 N N . VAL D 115 ? 1.6798 1.0265 1.3643 -0.2587 0.1325 -0.7147 115 VAL D N 6994 C CA . VAL D 115 ? 1.7122 1.0315 1.4227 -0.2613 0.1466 -0.7401 115 VAL D CA 6995 C C . VAL D 115 ? 1.7317 1.0441 1.4441 -0.2788 0.1269 -0.7483 115 VAL D C 6996 O O . VAL D 115 ? 1.7830 1.0717 1.4852 -0.2916 0.1336 -0.7772 115 VAL D O 6997 C CB . VAL D 115 ? 1.6886 0.9923 1.4556 -0.2368 0.1545 -0.7309 115 VAL D CB 6998 C CG1 . VAL D 115 ? 1.7343 0.9943 1.5185 -0.2383 0.1615 -0.7559 115 VAL D CG1 6999 C CG2 . VAL D 115 ? 1.6734 0.9916 1.4641 -0.2174 0.1705 -0.7376 115 VAL D CG2 7000 N N . LYS D 116 ? 1.6970 1.0329 1.4326 -0.2811 0.1059 -0.7296 116 LYS D N 7001 C CA . LYS D 116 ? 1.7109 1.0534 1.4706 -0.3008 0.0880 -0.7494 116 LYS D CA 7002 C C . LYS D 116 ? 1.7576 1.1017 1.4710 -0.3105 0.0549 -0.7727 116 LYS D C 7003 O O . LYS D 116 ? 1.7988 1.1283 1.5124 -0.3254 0.0459 -0.8039 116 LYS D O 7004 C CB . LYS D 116 ? 1.6673 1.0417 1.4771 -0.3039 0.0774 -0.7357 116 LYS D CB 7005 C CG . LYS D 116 ? 1.6473 0.9985 1.4776 -0.3009 0.1066 -0.7111 116 LYS D CG 7006 C CD . LYS D 116 ? 1.6088 0.9943 1.4811 -0.3089 0.1018 -0.7022 116 LYS D CD 7007 C CE . LYS D 116 ? 1.5981 0.9487 1.4593 -0.3040 0.1264 -0.6696 116 LYS D CE 7008 N NZ . LYS D 116 ? 1.5420 0.9369 1.4300 -0.3013 0.1178 -0.6535 116 LYS D NZ 7009 N N . ASN D 117 ? 1.7565 1.1054 1.4190 -0.3025 0.0336 -0.7574 117 ASN D N 7010 C CA . ASN D 117 ? 1.8338 1.1520 1.4147 -0.3110 -0.0069 -0.7746 117 ASN D CA 7011 C C . ASN D 117 ? 1.9145 1.1786 1.4181 -0.3268 0.0157 -0.7989 117 ASN D C 7012 O O . ASN D 117 ? 1.9915 1.2158 1.4334 -0.3397 -0.0187 -0.8236 117 ASN D O 7013 C CB . ASN D 117 ? 1.8446 1.1535 1.3608 -0.3021 -0.0272 -0.7492 117 ASN D CB 7014 C CG . ASN D 117 ? 1.7795 1.1381 1.3656 -0.2874 -0.0607 -0.7323 117 ASN D CG 7015 O OD1 . ASN D 117 ? 1.7510 1.1471 1.4272 -0.2890 -0.0774 -0.7498 117 ASN D OD1 7016 N ND2 . ASN D 117 ? 1.7639 1.1225 1.3129 -0.2767 -0.0651 -0.7037 117 ASN D ND2 7017 N N . LEU D 118 ? 1.8996 1.1590 1.4099 -0.3251 0.0703 -0.7970 118 LEU D N 7018 C CA . LEU D 118 ? 1.9762 1.1906 1.4319 -0.3421 0.1041 -0.8280 118 LEU D CA 7019 C C . LEU D 118 ? 1.9789 1.1916 1.4873 -0.3472 0.1112 -0.8534 118 LEU D C 7020 O O . LEU D 118 ? 2.0577 1.2299 1.5124 -0.3658 0.1176 -0.8845 118 LEU D O 7021 C CB . LEU D 118 ? 1.9603 1.1785 1.4284 -0.3369 0.1589 -0.8292 118 LEU D CB 7022 C CG . LEU D 118 ? 2.0344 1.2133 1.4657 -0.3573 0.2077 -0.8719 118 LEU D CG 7023 C CD1 . LEU D 118 ? 2.1599 1.2670 1.4449 -0.3910 0.2012 -0.8891 118 LEU D CD1 7024 C CD2 . LEU D 118 ? 2.0063 1.2051 1.4852 -0.3494 0.2587 -0.8829 118 LEU D CD2 7025 N N . TYR D 119 ? 1.9086 1.1528 1.5088 -0.3342 0.1132 -0.8409 119 TYR D N 7026 C CA . TYR D 119 ? 1.9224 1.1533 1.5661 -0.3420 0.1219 -0.8630 119 TYR D CA 7027 C C . TYR D 119 ? 1.9568 1.1877 1.5941 -0.3603 0.0848 -0.8867 119 TYR D C 7028 O O . TYR D 119 ? 1.9991 1.2054 1.6315 -0.3745 0.0901 -0.9172 119 TYR D O 7029 C CB . TYR D 119 ? 1.8703 1.1076 1.5845 -0.3302 0.1343 -0.8421 119 TYR D CB 7030 C CG . TYR D 119 ? 1.9032 1.1062 1.6452 -0.3418 0.1481 -0.8631 119 TYR D CG 7031 C CD1 . TYR D 119 ? 1.9388 1.1027 1.6794 -0.3346 0.1710 -0.8798 119 TYR D CD1 7032 C CD2 . TYR D 119 ? 1.9040 1.1117 1.6802 -0.3619 0.1402 -0.8726 119 TYR D CD2 7033 C CE1 . TYR D 119 ? 1.9809 1.1016 1.7370 -0.3451 0.1813 -0.8979 119 TYR D CE1 7034 C CE2 . TYR D 119 ? 1.9476 1.1137 1.7400 -0.3782 0.1589 -0.8933 119 TYR D CE2 7035 C CZ . TYR D 119 ? 1.9893 1.1070 1.7633 -0.3687 0.1771 -0.9022 119 TYR D CZ 7036 O OH . TYR D 119 ? 2.0414 1.1060 1.8217 -0.3843 0.1933 -0.9218 119 TYR D OH 7037 N N . ASP D 120 ? 1.9363 1.1961 1.5837 -0.3580 0.0435 -0.8776 120 ASP D N 7038 C CA . ASP D 120 ? 1.9749 1.2401 1.6344 -0.3695 -0.0063 -0.9090 120 ASP D CA 7039 C C . ASP D 120 ? 2.0792 1.2885 1.6260 -0.3779 -0.0368 -0.9295 120 ASP D C 7040 O O . ASP D 120 ? 2.1325 1.3247 1.6761 -0.3894 -0.0702 -0.9651 120 ASP D O 7041 C CB . ASP D 120 ? 1.9304 1.2408 1.6422 -0.3599 -0.0491 -0.9014 120 ASP D CB 7042 C CG . ASP D 120 ? 1.8492 1.2025 1.6625 -0.3613 -0.0144 -0.8888 120 ASP D CG 7043 O OD1 . ASP D 120 ? 1.8457 1.1899 1.7029 -0.3772 0.0223 -0.9032 120 ASP D OD1 7044 O OD2 . ASP D 120 ? 1.7988 1.1828 1.6356 -0.3496 -0.0225 -0.8650 120 ASP D OD2 7045 N N . LYS D 121 ? 2.1156 1.2873 1.5635 -0.3761 -0.0226 -0.9102 121 LYS D N 7046 C CA . LYS D 121 ? 2.2430 1.3336 1.5485 -0.3931 -0.0386 -0.9281 121 LYS D CA 7047 C C . LYS D 121 ? 2.2925 1.3495 1.5777 -0.4124 -0.0008 -0.9609 121 LYS D C 7048 O O . LYS D 121 ? 2.4050 1.3966 1.5945 -0.4298 -0.0298 -0.9877 121 LYS D O 7049 C CB . LYS D 121 ? 2.2784 1.3303 1.4837 -0.3964 -0.0102 -0.9048 121 LYS D CB 7050 C CG . LYS D 121 ? 2.4443 1.3843 1.4664 -0.4226 -0.0246 -0.9213 121 LYS D CG 7051 C CD . LYS D 121 ? 2.4889 1.3843 1.4086 -0.4309 0.0012 -0.8985 121 LYS D CD 7052 C CE . LYS D 121 ? 2.6887 1.4412 1.3905 -0.4644 -0.0147 -0.9134 121 LYS D CE 7053 N NZ . LYS D 121 ? 2.7777 1.4760 1.4175 -0.4986 0.0457 -0.9521 121 LYS D NZ 7054 N N . VAL D 122 ? 2.2203 1.3118 1.5889 -0.4081 0.0580 -0.9601 122 VAL D N 7055 C CA . VAL D 122 ? 2.2583 1.3236 1.6285 -0.4227 0.0938 -0.9935 122 VAL D CA 7056 C C . VAL D 122 ? 2.2508 1.3329 1.6885 -0.4268 0.0651 -1.0146 122 VAL D C 7057 O O . VAL D 122 ? 2.3232 1.3680 1.7256 -0.4441 0.0647 -1.0483 122 VAL D O 7058 C CB . VAL D 122 ? 2.1986 1.2846 1.6390 -0.4110 0.1559 -0.9907 122 VAL D CB 7059 C CG1 . VAL D 122 ? 2.2444 1.3012 1.6936 -0.4237 0.1881 -1.0299 122 VAL D CG1 7060 C CG2 . VAL D 122 ? 2.2050 1.2842 1.6019 -0.4096 0.1898 -0.9816 122 VAL D CG2 7061 N N . ARG D 123 ? 2.1711 1.3061 1.7057 -0.4154 0.0473 -0.9996 123 ARG D N 7062 C CA . ARG D 123 ? 2.1674 1.3220 1.7798 -0.4260 0.0291 -1.0270 123 ARG D CA 7063 C C . ARG D 123 ? 2.2358 1.3780 1.8160 -0.4343 -0.0389 -1.0599 123 ARG D C 7064 O O . ARG D 123 ? 2.2749 1.4071 1.8777 -0.4491 -0.0509 -1.0984 123 ARG D O 7065 C CB . ARG D 123 ? 2.0832 1.2885 1.7990 -0.4203 0.0365 -1.0094 123 ARG D CB 7066 C CG . ARG D 123 ? 2.0846 1.3073 1.8889 -0.4407 0.0357 -1.0453 123 ARG D CG 7067 C CD . ARG D 123 ? 2.0277 1.2670 1.9055 -0.4463 0.0752 -1.0276 123 ARG D CD 7068 N NE . ARG D 123 ? 1.9710 1.2497 1.8682 -0.4318 0.0601 -0.9992 123 ARG D NE 7069 C CZ . ARG D 123 ? 1.9510 1.2803 1.9132 -0.4345 0.0217 -1.0202 123 ARG D CZ 7070 N NH1 . ARG D 123 ? 1.9839 1.3347 2.0073 -0.4499 -0.0108 -1.0743 123 ARG D NH1 7071 N NH2 . ARG D 123 ? 1.8997 1.2603 1.8759 -0.4198 0.0121 -0.9922 123 ARG D NH2 7072 N N . LEU D 124 ? 2.2536 1.3891 1.7796 -0.4228 -0.0894 -1.0465 124 LEU D N 7073 C CA . LEU D 124 ? 2.3406 1.4454 1.8215 -0.4228 -0.1743 -1.0773 124 LEU D CA 7074 C C . LEU D 124 ? 2.4792 1.4860 1.8025 -0.4388 -0.1850 -1.0940 124 LEU D C 7075 O O . LEU D 124 ? 2.5662 1.5368 1.8636 -0.4456 -0.2423 -1.1330 124 LEU D O 7076 C CB . LEU D 124 ? 2.3376 1.4485 1.7985 -0.4026 -0.2314 -1.0561 124 LEU D CB 7077 C CG . LEU D 124 ? 2.2343 1.4355 1.8536 -0.3889 -0.2519 -1.0609 124 LEU D CG 7078 C CD1 . LEU D 124 ? 2.1327 1.3974 1.8814 -0.4012 -0.1769 -1.0611 124 LEU D CD1 7079 C CD2 . LEU D 124 ? 2.2015 1.4096 1.7899 -0.3692 -0.2682 -1.0207 124 LEU D CD2 7080 N N . GLN D 125 ? 2.5307 2.0243 1.9748 -0.6072 0.3888 -0.9727 125 GLN D N 7081 C CA . GLN D 125 ? 2.5386 2.0240 1.9699 -0.6149 0.3913 -0.9738 125 GLN D CA 7082 C C . GLN D 125 ? 2.5342 2.0239 1.9711 -0.6204 0.3995 -0.9785 125 GLN D C 7083 O O . GLN D 125 ? 2.5430 2.0301 1.9712 -0.6262 0.3984 -0.9813 125 GLN D O 7084 C CB . GLN D 125 ? 2.5394 2.0159 1.9644 -0.6167 0.3960 -0.9702 125 GLN D CB 7085 C CG . GLN D 125 ? 2.5513 2.0194 1.9628 -0.6255 0.3995 -0.9718 125 GLN D CG 7086 C CD . GLN D 125 ? 2.5539 2.0132 1.9573 -0.6270 0.4018 -0.9686 125 GLN D CD 7087 O OE1 . GLN D 125 ? 2.5667 2.0174 1.9549 -0.6337 0.4013 -0.9690 125 GLN D OE1 7088 N NE2 . GLN D 125 ? 2.5417 2.0028 1.9546 -0.6212 0.4044 -0.9656 125 GLN D NE2 7089 N N . LEU D 126 ? 2.5198 2.0151 1.9703 -0.6189 0.4072 -0.9792 126 LEU D N 7090 C CA . LEU D 126 ? 2.5159 2.0155 1.9730 -0.6233 0.4146 -0.9836 126 LEU D CA 7091 C C . LEU D 126 ? 2.5048 2.0145 1.9748 -0.6196 0.4144 -0.9854 126 LEU D C 7092 O O . LEU D 126 ? 2.4969 2.0085 1.9766 -0.6175 0.4199 -0.9844 126 LEU D O 7093 C CB . LEU D 126 ? 2.5128 2.0080 1.9736 -0.6262 0.4246 -0.9835 126 LEU D CB 7094 N N . ARG D 127 ? 2.5047 2.0205 1.9743 -0.6191 0.4078 -0.9884 127 ARG D N 7095 C CA . ARG D 127 ? 2.4940 2.0205 1.9753 -0.6160 0.4069 -0.9911 127 ARG D CA 7096 C C . ARG D 127 ? 2.4898 2.0207 1.9782 -0.6207 0.4150 -0.9952 127 ARG D C 7097 O O . ARG D 127 ? 2.4824 2.0156 1.9796 -0.6200 0.4210 -0.9948 127 ARG D O 7098 C CB . ARG D 127 ? 2.4976 2.0295 1.9770 -0.6135 0.3963 -0.9939 127 ARG D CB 7099 N N . ASP D 128 ? 2.4948 2.0259 1.9784 -0.6259 0.4149 -0.9990 128 ASP D N 7100 C CA . ASP D 128 ? 2.4909 2.0262 1.9803 -0.6307 0.4220 -1.0033 128 ASP D CA 7101 C C . ASP D 128 ? 2.4889 2.0167 1.9765 -0.6354 0.4308 -1.0026 128 ASP D C 7102 O O . ASP D 128 ? 2.4849 2.0146 1.9785 -0.6388 0.4375 -1.0053 128 ASP D O 7103 C CB . ASP D 128 ? 2.4989 2.0387 1.9848 -0.6339 0.4174 -1.0081 128 ASP D CB 7104 N N . ASN D 129 ? 2.4908 2.0101 1.9704 -0.6359 0.4308 -0.9995 129 ASN D N 7105 C CA . ASN D 129 ? 2.4921 2.0048 1.9700 -0.6406 0.4386 -1.0001 129 ASN D CA 7106 C C . ASN D 129 ? 2.4829 1.9918 1.9680 -0.6377 0.4440 -0.9973 129 ASN D C 7107 O O . ASN D 129 ? 2.4840 1.9871 1.9683 -0.6405 0.4496 -0.9979 129 ASN D O 7108 C CB . ASN D 129 ? 2.5023 2.0079 1.9668 -0.6441 0.4363 -0.9996 129 ASN D CB 7109 C CG . ASN D 129 ? 2.5115 2.0187 1.9671 -0.6471 0.4297 -1.0021 129 ASN D CG 7110 O OD1 . ASN D 129 ? 2.5101 2.0247 1.9707 -0.6462 0.4271 -1.0047 129 ASN D OD1 7111 N ND2 . ASN D 129 ? 2.5215 2.0212 1.9633 -0.6510 0.4270 -1.0015 129 ASN D ND2 7112 N N . ALA D 130 ? 2.4744 1.9865 1.9664 -0.6322 0.4423 -0.9947 130 ALA D N 7113 C CA . ALA D 130 ? 2.4667 1.9744 1.9649 -0.6291 0.4463 -0.9916 130 ALA D CA 7114 C C . ALA D 130 ? 2.4573 1.9697 1.9636 -0.6250 0.4454 -0.9901 130 ALA D C 7115 O O . ALA D 130 ? 2.4554 1.9744 1.9619 -0.6224 0.4399 -0.9901 130 ALA D O 7116 C CB . ALA D 130 ? 2.4669 1.9688 1.9595 -0.6261 0.4438 -0.9876 130 ALA D CB 7117 N N . LYS D 131 ? 2.4515 1.9601 1.9643 -0.6248 0.4507 -0.9894 131 LYS D N 7118 C CA . LYS D 131 ? 2.4450 1.9560 1.9641 -0.6219 0.4506 -0.9876 131 LYS D CA 7119 C C . LYS D 131 ? 2.4384 1.9452 1.9581 -0.6162 0.4485 -0.9824 131 LYS D C 7120 O O . LYS D 131 ? 2.4406 1.9405 1.9583 -0.6151 0.4497 -0.9805 131 LYS D O 7121 C CB . LYS D 131 ? 2.4460 1.9533 1.9702 -0.6253 0.4567 -0.9895 131 LYS D CB 7122 C CG . LYS D 131 ? 2.4432 1.9493 1.9719 -0.6231 0.4572 -0.9869 131 LYS D CG 7123 C CD . LYS D 131 ? 2.4469 1.9487 1.9787 -0.6274 0.4622 -0.9890 131 LYS D CD 7124 C CE . LYS D 131 ? 2.4456 1.9434 1.9797 -0.6256 0.4625 -0.9858 131 LYS D CE 7125 N NZ . LYS D 131 ? 2.4509 1.9450 1.9861 -0.6308 0.4664 -0.9879 131 LYS D NZ 7126 N N . GLU D 132 ? 2.4300 1.9414 1.9527 -0.6128 0.4456 -0.9807 132 GLU D N 7127 C CA . GLU D 132 ? 2.4221 1.9300 1.9461 -0.6074 0.4438 -0.9758 132 GLU D CA 7128 C C . GLU D 132 ? 2.4184 1.9204 1.9472 -0.6081 0.4484 -0.9746 132 GLU D C 7129 O O . GLU D 132 ? 2.4215 1.9262 1.9529 -0.6115 0.4508 -0.9771 132 GLU D O 7130 C CB . GLU D 132 ? 2.4183 1.9346 1.9431 -0.6037 0.4380 -0.9752 132 GLU D CB 7131 C CG . GLU D 132 ? 2.4133 1.9268 1.9376 -0.5977 0.4345 -0.9702 132 GLU D CG 7132 C CD . GLU D 132 ? 2.4096 1.9322 1.9363 -0.5941 0.4290 -0.9705 132 GLU D CD 7133 O OE1 . GLU D 132 ? 2.4104 1.9415 1.9379 -0.5956 0.4262 -0.9749 132 GLU D OE1 7134 O OE2 . GLU D 132 ? 2.4058 1.9271 1.9342 -0.5896 0.4273 -0.9668 132 GLU D OE2 7135 N N . LEU D 133 ? 2.4119 1.9055 1.9415 -0.6051 0.4494 -0.9709 133 LEU D N 7136 C CA . LEU D 133 ? 2.4091 1.8947 1.9423 -0.6054 0.4527 -0.9695 133 LEU D CA 7137 C C . LEU D 133 ? 2.4033 1.8896 1.9378 -0.6022 0.4506 -0.9659 133 LEU D C 7138 O O . LEU D 133 ? 2.4046 1.8921 1.9403 -0.6051 0.4522 -0.9670 133 LEU D O 7139 C CB . LEU D 133 ? 2.4095 1.8849 1.9438 -0.6040 0.4546 -0.9682 133 LEU D CB 7140 C CG . LEU D 133 ? 2.4148 1.8872 1.9498 -0.6083 0.4584 -0.9727 133 LEU D CG 7141 C CD1 . LEU D 133 ? 2.4148 1.8786 1.9524 -0.6063 0.4599 -0.9723 133 LEU D CD1 7142 C CD2 . LEU D 133 ? 2.4191 1.8897 1.9562 -0.6130 0.4615 -0.9755 133 LEU D CD2 7143 N N . GLY D 134 ? 2.3967 1.8821 1.9305 -0.5968 0.4473 -0.9620 134 GLY D N 7144 C CA . GLY D 134 ? 2.3917 1.8776 1.9268 -0.5934 0.4453 -0.9585 134 GLY D CA 7145 C C . GLY D 134 ? 2.3872 1.8658 1.9223 -0.5880 0.4436 -0.9535 134 GLY D C 7146 O O . GLY D 134 ? 2.3826 1.8641 1.9178 -0.5839 0.4404 -0.9505 134 GLY D O 7147 N N . ASN D 135 ? 2.3879 1.8577 1.9237 -0.5880 0.4458 -0.9533 135 ASN D N 7148 C CA . ASN D 135 ? 2.3836 1.8463 1.9202 -0.5831 0.4446 -0.9494 135 ASN D CA 7149 C C . ASN D 135 ? 2.3831 1.8482 1.9168 -0.5810 0.4428 -0.9492 135 ASN D C 7150 O O . ASN D 135 ? 2.3814 1.8403 1.9162 -0.5791 0.4436 -0.9483 135 ASN D O 7151 C CB . ASN D 135 ? 2.3856 1.8369 1.9256 -0.5838 0.4475 -0.9498 135 ASN D CB 7152 C CG . ASN D 135 ? 2.3884 1.8382 1.9295 -0.5877 0.4507 -0.9547 135 ASN D CG 7153 O OD1 . ASN D 135 ? 2.3893 1.8461 1.9282 -0.5914 0.4517 -0.9579 135 ASN D OD1 7154 N ND2 . ASN D 135 ? 2.3891 1.8301 1.9341 -0.5867 0.4523 -0.9557 135 ASN D ND2 7155 N N . GLY D 136 ? 2.3859 1.8596 1.9158 -0.5817 0.4401 -0.9504 136 GLY D N 7156 C CA . GLY D 136 ? 2.3905 1.8654 1.9153 -0.5808 0.4377 -0.9501 136 GLY D CA 7157 C C . GLY D 136 ? 2.4007 1.8732 1.9235 -0.5855 0.4412 -0.9541 136 GLY D C 7158 O O . GLY D 136 ? 2.4027 1.8712 1.9229 -0.5853 0.4418 -0.9539 136 GLY D O 7159 N N . CYS D 137 ? 2.4092 1.8842 1.9331 -0.5902 0.4439 -0.9582 137 CYS D N 7160 C CA . CYS D 137 ? 2.4180 1.8914 1.9405 -0.5952 0.4476 -0.9626 137 CYS D CA 7161 C C . CYS D 137 ? 2.4214 1.9016 1.9412 -0.5997 0.4473 -0.9663 137 CYS D C 7162 O O . CYS D 137 ? 2.4185 1.9046 1.9392 -0.5991 0.4449 -0.9660 137 CYS D O 7163 C CB . CYS D 137 ? 2.4225 1.8889 1.9517 -0.5965 0.4526 -0.9647 137 CYS D CB 7164 S SG . CYS D 137 ? 2.4238 1.8816 1.9574 -0.5916 0.4530 -0.9618 137 CYS D SG 7165 N N . PHE D 138 ? 2.4279 1.9073 1.9446 -0.6045 0.4500 -0.9702 138 PHE D N 7166 C CA . PHE D 138 ? 2.4325 1.9174 1.9463 -0.6093 0.4501 -0.9741 138 PHE D CA 7167 C C . PHE D 138 ? 2.4361 1.9180 1.9522 -0.6146 0.4560 -0.9790 138 PHE D C 7168 O O . PHE D 138 ? 2.4380 1.9147 1.9547 -0.6155 0.4591 -0.9802 138 PHE D O 7169 C CB . PHE D 138 ? 2.4372 1.9249 1.9415 -0.6102 0.4453 -0.9740 138 PHE D CB 7170 C CG . PHE D 138 ? 2.4342 1.9253 1.9363 -0.6049 0.4384 -0.9701 138 PHE D CG 7171 C CD1 . PHE D 138 ? 2.4328 1.9317 1.9368 -0.6039 0.4347 -0.9710 138 PHE D CD1 7172 C CD2 . PHE D 138 ? 2.4327 1.9197 1.9313 -0.6011 0.4357 -0.9660 138 PHE D CD2 7173 C CE1 . PHE D 138 ? 2.4304 1.9331 1.9336 -0.5989 0.4281 -0.9683 138 PHE D CE1 7174 C CE2 . PHE D 138 ? 2.4304 1.9204 1.9272 -0.5962 0.4290 -0.9627 138 PHE D CE2 7175 C CZ . PHE D 138 ? 2.4294 1.9274 1.9289 -0.5949 0.4251 -0.9640 138 PHE D CZ 7176 N N . GLU D 139 ? 2.4370 1.9227 1.9549 -0.6182 0.4576 -0.9822 139 GLU D N 7177 C CA . GLU D 139 ? 2.4402 1.9238 1.9603 -0.6235 0.4629 -0.9872 139 GLU D CA 7178 C C . GLU D 139 ? 2.4442 1.9329 1.9580 -0.6285 0.4624 -0.9907 139 GLU D C 7179 O O . GLU D 139 ? 2.4449 1.9397 1.9576 -0.6293 0.4600 -0.9914 139 GLU D O 7180 C CB . GLU D 139 ? 2.4398 1.9220 1.9666 -0.6243 0.4655 -0.9882 139 GLU D CB 7181 C CG . GLU D 139 ? 2.4388 1.9123 1.9719 -0.6218 0.4677 -0.9871 139 GLU D CG 7182 C CD . GLU D 139 ? 2.4410 1.9111 1.9785 -0.6239 0.4698 -0.9884 139 GLU D CD 7183 O OE1 . GLU D 139 ? 2.4409 1.9146 1.9775 -0.6240 0.4683 -0.9868 139 GLU D OE1 7184 O OE2 . GLU D 139 ? 2.4428 1.9064 1.9846 -0.6256 0.4730 -0.9916 139 GLU D OE2 7185 N N . PHE D 140 ? 2.4470 1.9330 1.9566 -0.6322 0.4648 -0.9935 140 PHE D N 7186 C CA . PHE D 140 ? 2.4527 1.9420 1.9550 -0.6377 0.4645 -0.9970 140 PHE D CA 7187 C C . PHE D 140 ? 2.4527 1.9447 1.9592 -0.6419 0.4681 -1.0013 140 PHE D C 7188 O O . PHE D 140 ? 2.4503 1.9390 1.9644 -0.6425 0.4727 -1.0033 140 PHE D O 7189 C CB . PHE D 140 ? 2.4593 1.9443 1.9558 -0.6418 0.4674 -0.9995 140 PHE D CB 7190 C CG . PHE D 140 ? 2.4608 1.9431 1.9494 -0.6396 0.4634 -0.9957 140 PHE D CG 7191 C CD1 . PHE D 140 ? 2.4672 1.9505 1.9440 -0.6413 0.4578 -0.9944 140 PHE D CD1 7192 C CD2 . PHE D 140 ? 2.4574 1.9355 1.9500 -0.6359 0.4647 -0.9935 140 PHE D CD2 7193 C CE1 . PHE D 140 ? 2.4701 1.9496 1.9384 -0.6396 0.4536 -0.9908 140 PHE D CE1 7194 C CE2 . PHE D 140 ? 2.4594 1.9347 1.9442 -0.6342 0.4612 -0.9900 140 PHE D CE2 7195 C CZ . PHE D 140 ? 2.4662 1.9419 1.9384 -0.6362 0.4556 -0.9886 140 PHE D CZ 7196 N N . TYR D 141 ? 2.4542 1.9517 1.9558 -0.6447 0.4655 -1.0030 141 TYR D N 7197 C CA . TYR D 141 ? 2.4553 1.9559 1.9595 -0.6495 0.4688 -1.0076 141 TYR D CA 7198 C C . TYR D 141 ? 2.4610 1.9597 1.9600 -0.6559 0.4722 -1.0121 141 TYR D C 7199 O O . TYR D 141 ? 2.4627 1.9636 1.9630 -0.6604 0.4751 -1.0163 141 TYR D O 7200 C CB . TYR D 141 ? 2.4554 1.9637 1.9583 -0.6491 0.4642 -1.0078 141 TYR D CB 7201 C CG . TYR D 141 ? 2.4495 1.9607 1.9595 -0.6451 0.4632 -1.0056 141 TYR D CG 7202 C CD1 . TYR D 141 ? 2.4497 1.9602 1.9663 -0.6470 0.4678 -1.0074 141 TYR D CD1 7203 C CD2 . TYR D 141 ? 2.4451 1.9592 1.9546 -0.6398 0.4576 -1.0018 141 TYR D CD2 7204 C CE1 . TYR D 141 ? 2.4454 1.9578 1.9670 -0.6445 0.4672 -1.0056 141 TYR D CE1 7205 C CE2 . TYR D 141 ? 2.4395 1.9565 1.9551 -0.6369 0.4573 -1.0003 141 TYR D CE2 7206 C CZ . TYR D 141 ? 2.4397 1.9557 1.9609 -0.6397 0.4623 -1.0022 141 TYR D CZ 7207 O OH . TYR D 141 ? 2.4358 1.9538 1.9615 -0.6380 0.4622 -1.0009 141 TYR D OH 7208 N N . HIS D 142 ? 2.4628 1.9575 1.9553 -0.6568 0.4720 -1.0115 142 HIS D N 7209 C CA . HIS D 142 ? 2.4689 1.9611 1.9561 -0.6635 0.4761 -1.0162 142 HIS D CA 7210 C C . HIS D 142 ? 2.4687 1.9555 1.9573 -0.6633 0.4798 -1.0166 142 HIS D C 7211 O O . HIS D 142 ? 2.4615 1.9463 1.9548 -0.6575 0.4785 -1.0129 142 HIS D O 7212 C CB . HIS D 142 ? 2.4761 1.9691 1.9496 -0.6672 0.4713 -1.0160 142 HIS D CB 7213 C CG . HIS D 142 ? 2.4764 1.9663 1.9413 -0.6642 0.4656 -1.0113 142 HIS D CG 7214 N ND1 . HIS D 142 ? 2.4705 1.9627 1.9366 -0.6575 0.4590 -1.0064 142 HIS D ND1 7215 C CD2 . HIS D 142 ? 2.4824 1.9668 1.9369 -0.6674 0.4654 -1.0110 142 HIS D CD2 7216 C CE1 . HIS D 142 ? 2.4735 1.9614 1.9305 -0.6562 0.4547 -1.0030 142 HIS D CE1 7217 N NE2 . HIS D 142 ? 2.4814 1.9642 1.9307 -0.6624 0.4585 -1.0055 142 HIS D NE2 7218 N N . ARG D 143 ? 2.4765 1.9614 1.9615 -0.6697 0.4845 -1.0217 143 ARG D N 7219 C CA . ARG D 143 ? 2.4771 1.9579 1.9642 -0.6705 0.4887 -1.0238 143 ARG D CA 7220 C C . ARG D 143 ? 2.4813 1.9591 1.9558 -0.6710 0.4850 -1.0203 143 ARG D C 7221 O O . ARG D 143 ? 2.4896 1.9667 1.9509 -0.6762 0.4826 -1.0205 143 ARG D O 7222 C CB . ARG D 143 ? 2.4829 1.9636 1.9719 -0.6780 0.4959 -1.0319 143 ARG D CB 7223 C CG . ARG D 143 ? 2.4803 1.9631 1.9805 -0.6782 0.4993 -1.0358 143 ARG D CG 7224 C CD . ARG D 143 ? 2.4723 1.9532 1.9857 -0.6710 0.4990 -1.0337 143 ARG D CD 7225 N NE . ARG D 143 ? 2.4716 1.9489 1.9914 -0.6688 0.5016 -1.0354 143 ARG D NE 7226 C CZ . ARG D 143 ? 2.4672 1.9413 1.9958 -0.6620 0.4999 -1.0324 143 ARG D CZ 7227 N NH1 . ARG D 143 ? 2.4623 1.9360 1.9937 -0.6569 0.4961 -1.0273 143 ARG D NH1 7228 N NH2 . ARG D 143 ? 2.4671 1.9383 2.0015 -0.6604 0.5023 -1.0350 143 ARG D NH2 7229 N N . CYS D 144 ? 2.4760 1.9513 1.9542 -0.6657 0.4840 -1.0169 144 CYS D N 7230 C CA . CYS D 144 ? 2.4808 1.9526 1.9476 -0.6657 0.4803 -1.0132 144 CYS D CA 7231 C C . CYS D 144 ? 2.4813 1.9498 1.9510 -0.6674 0.4858 -1.0165 144 CYS D C 7232 O O . CYS D 144 ? 2.4716 1.9392 1.9508 -0.6613 0.4862 -1.0146 144 CYS D O 7233 C CB . CYS D 144 ? 2.4743 1.9466 1.9415 -0.6574 0.4730 -1.0057 144 CYS D CB 7234 S SG . CYS D 144 ? 2.4807 1.9479 1.9334 -0.6565 0.4671 -1.0005 144 CYS D SG 7235 N N . ASP D 145 ? 2.4921 1.9590 1.9534 -0.6761 0.4901 -1.0218 145 ASP D N 7236 C CA . ASP D 145 ? 2.4946 1.9594 1.9581 -0.6794 0.4962 -1.0266 145 ASP D CA 7237 C C . ASP D 145 ? 2.4946 1.9552 1.9495 -0.6771 0.4924 -1.0214 145 ASP D C 7238 O O . ASP D 145 ? 2.4915 1.9509 1.9403 -0.6720 0.4848 -1.0139 145 ASP D O 7239 C CB . ASP D 145 ? 2.5069 1.9715 1.9626 -0.6906 0.5022 -1.0344 145 ASP D CB 7240 C CG . ASP D 145 ? 2.5208 1.9816 1.9551 -0.6970 0.4977 -1.0315 145 ASP D CG 7241 O OD1 . ASP D 145 ? 2.5207 1.9816 1.9497 -0.6936 0.4905 -1.0258 145 ASP D OD1 7242 O OD2 . ASP D 145 ? 2.5328 1.9901 1.9554 -0.7058 0.5013 -1.0354 145 ASP D OD2 7243 N N . ASN D 146 ? 2.4970 1.9558 1.9522 -0.6808 0.4976 -1.0258 146 ASN D N 7244 C CA . ASN D 146 ? 2.4981 1.9528 1.9458 -0.6790 0.4949 -1.0214 146 ASN D CA 7245 C C . ASN D 146 ? 2.5097 1.9590 1.9353 -0.6833 0.4886 -1.0163 146 ASN D C 7246 O O . ASN D 146 ? 2.5084 1.9545 1.9283 -0.6781 0.4822 -1.0093 146 ASN D O 7247 C CB . ASN D 146 ? 2.4998 1.9542 1.9522 -0.6836 0.5027 -1.0287 146 ASN D CB 7248 C CG . ASN D 146 ? 2.4870 1.9450 1.9617 -0.6768 0.5064 -1.0324 146 ASN D CG 7249 O OD1 . ASN D 146 ? 2.4783 1.9379 1.9637 -0.6690 0.5031 -1.0288 146 ASN D OD1 7250 N ND2 . ASN D 146 ? 2.4880 1.9469 1.9695 -0.6801 0.5130 -1.0399 146 ASN D ND2 7251 N N . GLU D 147 ? 2.5212 1.9688 1.9341 -0.6927 0.4900 -1.0199 147 GLU D N 7252 C CA . GLU D 147 ? 2.5342 1.9751 1.9249 -0.6972 0.4829 -1.0153 147 GLU D CA 7253 C C . GLU D 147 ? 2.5293 1.9713 1.9194 -0.6895 0.4731 -1.0081 147 GLU D C 7254 O O . GLU D 147 ? 2.5350 1.9719 1.9122 -0.6876 0.4647 -1.0021 147 GLU D O 7255 C CB . GLU D 147 ? 2.5500 1.9883 1.9271 -0.7096 0.4868 -1.0212 147 GLU D CB 7256 C CG . GLU D 147 ? 2.5589 1.9942 1.9298 -0.7195 0.4951 -1.0278 147 GLU D CG 7257 C CD . GLU D 147 ? 2.5754 2.0070 1.9301 -0.7327 0.4985 -1.0333 147 GLU D CD 7258 O OE1 . GLU D 147 ? 2.5746 2.0104 1.9342 -0.7344 0.5002 -1.0365 147 GLU D OE1 7259 O OE2 . GLU D 147 ? 2.5898 2.0139 1.9262 -0.7420 0.4994 -1.0343 147 GLU D OE2 7260 N N . CYS D 148 ? 2.5198 1.9687 1.9242 -0.6852 0.4742 -1.0094 148 CYS D N 7261 C CA . CYS D 148 ? 2.5138 1.9657 1.9215 -0.6773 0.4662 -1.0038 148 CYS D CA 7262 C C . CYS D 148 ? 2.5025 1.9550 1.9178 -0.6674 0.4622 -0.9978 148 CYS D C 7263 O O . CYS D 148 ? 2.5002 1.9523 1.9109 -0.6622 0.4536 -0.9922 148 CYS D O 7264 C CB . CYS D 148 ? 2.5073 1.9662 1.9288 -0.6758 0.4696 -1.0072 148 CYS D CB 7265 S SG . CYS D 148 ? 2.4961 1.9607 1.9273 -0.6656 0.4624 -1.0017 148 CYS D SG 7266 N N . MET D 149 ? 2.4947 1.9483 1.9222 -0.6648 0.4682 -0.9995 149 MET D N 7267 C CA . MET D 149 ? 2.4840 1.9377 1.9193 -0.6558 0.4652 -0.9942 149 MET D CA 7268 C C . MET D 149 ? 2.4886 1.9362 1.9095 -0.6560 0.4600 -0.9897 149 MET D C 7269 O O . MET D 149 ? 2.4818 1.9291 1.9029 -0.6488 0.4533 -0.9835 149 MET D O 7270 C CB . MET D 149 ? 2.4782 1.9334 1.9294 -0.6535 0.4725 -0.9979 149 MET D CB 7271 C CG . MET D 149 ? 2.4660 1.9234 1.9307 -0.6435 0.4701 -0.9934 149 MET D CG 7272 S SD . MET D 149 ? 2.4596 1.9223 1.9351 -0.6406 0.4697 -0.9940 149 MET D SD 7273 C CE . MET D 149 ? 2.4589 1.9222 1.9467 -0.6448 0.4791 -1.0026 149 MET D CE 7274 N N . GLU D 150 ? 2.4977 1.9402 1.9060 -0.6649 0.4632 -0.9930 150 GLU D N 7275 C CA . GLU D 150 ? 2.5052 1.9400 1.8960 -0.6672 0.4580 -0.9890 150 GLU D CA 7276 C C . GLU D 150 ? 2.5103 1.9421 1.8880 -0.6658 0.4472 -0.9838 150 GLU D C 7277 O O . GLU D 150 ? 2.5114 1.9385 1.8808 -0.6620 0.4397 -0.9782 150 GLU D O 7278 C CB . GLU D 150 ? 2.5191 1.9486 1.8969 -0.6790 0.4640 -0.9945 150 GLU D CB 7279 C CG . GLU D 150 ? 2.5139 1.9448 1.9017 -0.6803 0.4731 -0.9994 150 GLU D CG 7280 C CD . GLU D 150 ? 2.5274 1.9547 1.9036 -0.6931 0.4803 -1.0065 150 GLU D CD 7281 O OE1 . GLU D 150 ? 2.5360 1.9622 1.9030 -0.7011 0.4814 -1.0099 150 GLU D OE1 7282 O OE2 . GLU D 150 ? 2.5272 1.9528 1.9034 -0.6956 0.4850 -1.0090 150 GLU D OE2 7283 N N . SER D 151 ? 2.5130 1.9474 1.8894 -0.6685 0.4460 -0.9861 151 SER D N 7284 C CA . SER D 151 ? 2.5185 1.9509 1.8845 -0.6669 0.4354 -0.9824 151 SER D CA 7285 C C . SER D 151 ? 2.5046 1.9425 1.8818 -0.6555 0.4286 -0.9774 151 SER D C 7286 O O . SER D 151 ? 2.5079 1.9431 1.8765 -0.6523 0.4183 -0.9735 151 SER D O 7287 C CB . SER D 151 ? 2.5237 1.9588 1.8882 -0.6723 0.4367 -0.9869 151 SER D CB 7288 O OG . SER D 151 ? 2.5384 1.9678 1.8902 -0.6836 0.4421 -0.9915 151 SER D OG 7289 N N . VAL D 152 ? 2.4889 1.9342 1.8850 -0.6496 0.4340 -0.9780 152 VAL D N 7290 C CA . VAL D 152 ? 2.4770 1.9273 1.8841 -0.6395 0.4290 -0.9736 152 VAL D CA 7291 C C . VAL D 152 ? 2.4753 1.9210 1.8787 -0.6351 0.4255 -0.9686 152 VAL D C 7292 O O . VAL D 152 ? 2.4724 1.9186 1.8749 -0.6287 0.4173 -0.9642 152 VAL D O 7293 C CB . VAL D 152 ? 2.4635 1.9213 1.8900 -0.6357 0.4359 -0.9757 152 VAL D CB 7294 C CG1 . VAL D 152 ? 2.4518 1.9140 1.8884 -0.6262 0.4314 -0.9712 152 VAL D CG1 7295 C CG2 . VAL D 152 ? 2.4655 1.9279 1.8953 -0.6397 0.4386 -0.9804 152 VAL D CG2 7296 N N . ARG D 153 ? 2.4765 1.9180 1.8785 -0.6387 0.4321 -0.9700 153 ARG D N 7297 C CA . ARG D 153 ? 2.4759 1.9121 1.8727 -0.6360 0.4297 -0.9658 153 ARG D CA 7298 C C . ARG D 153 ? 2.4912 1.9185 1.8666 -0.6401 0.4216 -0.9630 153 ARG D C 7299 O O . ARG D 153 ? 2.4917 1.9152 1.8620 -0.6355 0.4151 -0.9580 153 ARG D O 7300 C CB . ARG D 153 ? 2.4739 1.9087 1.8756 -0.6397 0.4394 -0.9694 153 ARG D CB 7301 C CG . ARG D 153 ? 2.4577 1.8982 1.8796 -0.6327 0.4445 -0.9698 153 ARG D CG 7302 C CD . ARG D 153 ? 2.4562 1.8988 1.8879 -0.6374 0.4546 -0.9770 153 ARG D CD 7303 N NE . ARG D 153 ? 2.4650 1.9031 1.8886 -0.6450 0.4599 -0.9810 153 ARG D NE 7304 C CZ . ARG D 153 ? 2.4659 1.9057 1.8960 -0.6507 0.4687 -0.9886 153 ARG D CZ 7305 N NH1 . ARG D 153 ? 2.4589 1.9038 1.9033 -0.6493 0.4729 -0.9927 153 ARG D NH1 7306 N NH2 . ARG D 153 ? 2.4744 1.9105 1.8965 -0.6581 0.4735 -0.9927 153 ARG D NH2 7307 N N . ASN D 154 ? 2.5047 1.9280 1.8671 -0.6488 0.4215 -0.9663 154 ASN D N 7308 C CA . ASN D 154 ? 2.5222 1.9347 1.8616 -0.6545 0.4139 -0.9642 154 ASN D CA 7309 C C . ASN D 154 ? 2.5236 1.9351 1.8581 -0.6484 0.4007 -0.9598 154 ASN D C 7310 O O . ASN D 154 ? 2.5301 1.9341 1.8530 -0.6464 0.3923 -0.9553 154 ASN D O 7311 C CB . ASN D 154 ? 2.5374 1.9456 1.8644 -0.6664 0.4182 -0.9695 154 ASN D CB 7312 C CG . ASN D 154 ? 2.5588 1.9535 1.8595 -0.6741 0.4111 -0.9676 154 ASN D CG 7313 O OD1 . ASN D 154 ? 2.5637 1.9509 1.8545 -0.6737 0.4074 -0.9637 154 ASN D OD1 7314 N ND2 . ASN D 154 ? 2.5718 1.9626 1.8603 -0.6817 0.4091 -0.9703 154 ASN D ND2 7315 N N . GLY D 155 ? 2.5179 1.9371 1.8617 -0.6454 0.3988 -0.9617 155 GLY D N 7316 C CA . GLY D 155 ? 2.5203 1.9403 1.8616 -0.6398 0.3865 -0.9594 155 GLY D CA 7317 C C . GLY D 155 ? 2.5296 1.9507 1.8664 -0.6445 0.3841 -0.9633 155 GLY D C 7318 O O . GLY D 155 ? 2.5241 1.9535 1.8714 -0.6391 0.3801 -0.9644 155 GLY D O 7319 N N . THR D 156 ? 2.5448 1.9577 1.8658 -0.6550 0.3869 -0.9657 156 THR D N 7320 C CA . THR D 156 ? 2.5538 1.9664 1.8687 -0.6607 0.3851 -0.9695 156 THR D CA 7321 C C . THR D 156 ? 2.5418 1.9655 1.8739 -0.6616 0.3961 -0.9745 156 THR D C 7322 O O . THR D 156 ? 2.5384 1.9631 1.8749 -0.6660 0.4072 -0.9771 156 THR D O 7323 C CB . THR D 156 ? 2.5751 1.9742 1.8659 -0.6727 0.3849 -0.9707 156 THR D CB 7324 N N . TYR D 157 ? 2.5359 1.9679 1.8777 -0.6576 0.3927 -0.9763 157 TYR D N 7325 C CA . TYR D 157 ? 2.5242 1.9668 1.8829 -0.6576 0.4020 -0.9806 157 TYR D CA 7326 C C . TYR D 157 ? 2.5272 1.9749 1.8875 -0.6575 0.3969 -0.9835 157 TYR D C 7327 O O . TYR D 157 ? 2.5320 1.9796 1.8888 -0.6646 0.4013 -0.9876 157 TYR D O 7328 C CB . TYR D 157 ? 2.5053 1.9565 1.8835 -0.6489 0.4060 -0.9788 157 TYR D CB 7329 C CG . TYR D 157 ? 2.4926 1.9537 1.8880 -0.6481 0.4142 -0.9826 157 TYR D CG 7330 C CD1 . TYR D 157 ? 2.4877 1.9494 1.8898 -0.6519 0.4254 -0.9855 157 TYR D CD1 7331 C CD2 . TYR D 157 ? 2.4855 1.9552 1.8905 -0.6436 0.4104 -0.9838 157 TYR D CD2 7332 C CE1 . TYR D 157 ? 2.4778 1.9470 1.8947 -0.6512 0.4320 -0.9888 157 TYR D CE1 7333 C CE2 . TYR D 157 ? 2.4757 1.9534 1.8949 -0.6435 0.4177 -0.9871 157 TYR D CE2 7334 C CZ . TYR D 157 ? 2.4724 1.9491 1.8970 -0.6472 0.4282 -0.9893 157 TYR D CZ 7335 O OH . TYR D 157 ? 2.4638 1.9470 1.9017 -0.6472 0.4346 -0.9924 157 TYR D OH 7336 N N . PRO E 1 ? 1.6495 0.7577 1.5019 -0.4550 0.0053 -0.4634 0 PRO E N 7337 C CA . PRO E 1 ? 1.6259 0.7524 1.4701 -0.4322 -0.0089 -0.4592 0 PRO E CA 7338 C C . PRO E 1 ? 1.6119 0.7373 1.4362 -0.4246 -0.0049 -0.4429 0 PRO E C 7339 O O . PRO E 1 ? 1.5928 0.7384 1.4265 -0.4283 0.0026 -0.4389 0 PRO E O 7340 C CB . PRO E 1 ? 1.6028 0.7667 1.4742 -0.4281 -0.0176 -0.4719 0 PRO E CB 7341 C CG . PRO E 1 ? 1.6163 0.7805 1.5176 -0.4430 -0.0151 -0.4881 0 PRO E CG 7342 C CD . PRO E 1 ? 1.6451 0.7757 1.5354 -0.4624 0.0033 -0.4835 0 PRO E CD 7343 N N . ASP E 2 ? 1.6237 0.7264 1.4260 -0.4133 -0.0118 -0.4365 1 ASP E N 7344 C CA . ASP E 2 ? 1.6197 0.7129 1.4032 -0.4063 -0.0105 -0.4221 1 ASP E CA 7345 C C . ASP E 2 ? 1.5846 0.7165 1.3745 -0.3939 -0.0100 -0.4207 1 ASP E C 7346 O O . ASP E 2 ? 1.5764 0.7307 1.3735 -0.3865 -0.0150 -0.4315 1 ASP E O 7347 C CB . ASP E 2 ? 1.6464 0.7029 1.4135 -0.3954 -0.0242 -0.4216 1 ASP E CB 7348 C CG . ASP E 2 ? 1.6970 0.6979 1.4413 -0.4094 -0.0280 -0.4180 1 ASP E CG 7349 O OD1 . ASP E 2 ? 1.7209 0.6944 1.4414 -0.4272 -0.0171 -0.4063 1 ASP E OD1 7350 O OD2 . ASP E 2 ? 1.7186 0.6990 1.4650 -0.4045 -0.0411 -0.4279 1 ASP E OD2 7351 N N . GLN E 3 ? 1.5701 0.7033 1.3506 -0.3937 -0.0036 -0.4075 2 GLN E N 7352 C CA . GLN E 3 ? 1.5386 0.7059 1.3230 -0.3859 -0.0014 -0.4045 2 GLN E CA 7353 C C . GLN E 3 ? 1.5283 0.6891 1.2982 -0.3801 0.0021 -0.3905 2 GLN E C 7354 O O . GLN E 3 ? 1.5466 0.6764 1.3018 -0.3874 0.0050 -0.3805 2 GLN E O 7355 C CB . GLN E 3 ? 1.5250 0.7156 1.3285 -0.3960 0.0028 -0.4074 2 GLN E CB 7356 C CG . GLN E 3 ? 1.5022 0.7218 1.3069 -0.3879 -0.0022 -0.4070 2 GLN E CG 7357 C CD . GLN E 3 ? 1.4931 0.7328 1.3254 -0.3950 -0.0055 -0.4146 2 GLN E CD 7358 O OE1 . GLN E 3 ? 1.4745 0.7298 1.3141 -0.3942 -0.0037 -0.4098 2 GLN E OE1 7359 N NE2 . GLN E 3 ? 1.5014 0.7416 1.3545 -0.4011 -0.0121 -0.4295 2 GLN E NE2 7360 N N . ILE E 4 ? 1.5073 0.6920 1.2760 -0.3690 0.0017 -0.3905 3 ILE E N 7361 C CA . ILE E 4 ? 1.4955 0.6820 1.2549 -0.3631 0.0055 -0.3782 3 ILE E CA 7362 C C . ILE E 4 ? 1.4729 0.6923 1.2323 -0.3601 0.0090 -0.3774 3 ILE E C 7363 O O . ILE E 4 ? 1.4737 0.7051 1.2296 -0.3578 0.0061 -0.3884 3 ILE E O 7364 C CB . ILE E 4 ? 1.5037 0.6733 1.2601 -0.3499 -0.0020 -0.3820 3 ILE E CB 7365 C CG1 . ILE E 4 ? 1.4979 0.6603 1.2440 -0.3449 -0.0012 -0.3683 3 ILE E CG1 7366 C CG2 . ILE E 4 ? 1.4931 0.6854 1.2598 -0.3414 -0.0015 -0.4004 3 ILE E CG2 7367 C CD1 . ILE E 4 ? 1.5143 0.6527 1.2630 -0.3309 -0.0154 -0.3742 3 ILE E CD1 7368 N N . CYS E 5 ? 1.4636 0.6912 1.2211 -0.3620 0.0146 -0.3649 4 CYS E N 7369 C CA . CYS E 5 ? 1.4440 0.6968 1.1992 -0.3596 0.0144 -0.3628 4 CYS E CA 7370 C C . CYS E 5 ? 1.4278 0.6856 1.1729 -0.3527 0.0200 -0.3518 4 CYS E C 7371 O O . CYS E 5 ? 1.4287 0.6705 1.1711 -0.3513 0.0231 -0.3436 4 CYS E O 7372 C CB . CYS E 5 ? 1.4423 0.7075 1.2161 -0.3684 0.0133 -0.3630 4 CYS E CB 7373 S SG . CYS E 5 ? 1.4688 0.7310 1.2654 -0.3780 0.0070 -0.3787 4 CYS E SG 7374 N N . ILE E 6 ? 1.4155 0.6897 1.1498 -0.3495 0.0191 -0.3518 5 ILE E N 7375 C CA . ILE E 6 ? 1.4009 0.6833 1.1267 -0.3440 0.0248 -0.3421 5 ILE E CA 7376 C C . ILE E 6 ? 1.3801 0.6755 1.1108 -0.3472 0.0231 -0.3331 5 ILE E C 7377 O O . ILE E 6 ? 1.3807 0.6823 1.1115 -0.3498 0.0128 -0.3384 5 ILE E O 7378 C CB . ILE E 6 ? 1.4102 0.6978 1.1166 -0.3410 0.0282 -0.3510 5 ILE E CB 7379 C CG1 . ILE E 6 ? 1.4273 0.7074 1.1415 -0.3374 0.0320 -0.3665 5 ILE E CG1 7380 C CG2 . ILE E 6 ? 1.3931 0.6907 1.0911 -0.3368 0.0345 -0.3420 5 ILE E CG2 7381 C CD1 . ILE E 6 ? 1.4241 0.6950 1.1564 -0.3284 0.0306 -0.3630 5 ILE E CD1 7382 N N . GLY E 7 ? 1.3640 0.6604 1.0992 -0.3468 0.0306 -0.3213 6 GLY E N 7383 C CA . GLY E 7 ? 1.3486 0.6598 1.0947 -0.3500 0.0315 -0.3154 6 GLY E CA 7384 C C . GLY E 7 ? 1.3357 0.6485 1.0723 -0.3456 0.0395 -0.3023 6 GLY E C 7385 O O . GLY E 7 ? 1.3334 0.6369 1.0566 -0.3386 0.0417 -0.2993 6 GLY E O 7386 N N . TYR E 8 ? 1.3253 0.6510 1.0740 -0.3493 0.0428 -0.2977 7 TYR E N 7387 C CA . TYR E 8 ? 1.3145 0.6433 1.0536 -0.3453 0.0496 -0.2852 7 TYR E CA 7388 C C . TYR E 8 ? 1.3135 0.6462 1.0684 -0.3561 0.0604 -0.2824 7 TYR E C 7389 O O . TYR E 8 ? 1.3203 0.6595 1.1007 -0.3670 0.0634 -0.2938 7 TYR E O 7390 C CB . TYR E 8 ? 1.3011 0.6449 1.0287 -0.3366 0.0420 -0.2837 7 TYR E CB 7391 C CG . TYR E 8 ? 1.3015 0.6574 1.0403 -0.3378 0.0280 -0.2911 7 TYR E CG 7392 C CD1 . TYR E 8 ? 1.3186 0.6676 1.0533 -0.3387 0.0140 -0.3024 7 TYR E CD1 7393 C CD2 . TYR E 8 ? 1.2885 0.6590 1.0420 -0.3369 0.0248 -0.2885 7 TYR E CD2 7394 C CE1 . TYR E 8 ? 1.3281 0.6798 1.0710 -0.3379 -0.0069 -0.3106 7 TYR E CE1 7395 C CE2 . TYR E 8 ? 1.2938 0.6710 1.0617 -0.3352 0.0043 -0.2984 7 TYR E CE2 7396 C CZ . TYR E 8 ? 1.3174 0.6827 1.0787 -0.3351 -0.0136 -0.3094 7 TYR E CZ 7397 O OH . TYR E 8 ? 1.3301 0.6939 1.1038 -0.3316 -0.0417 -0.3207 7 TYR E OH 7398 N N . HIS E 9 ? 1.3096 0.6381 1.0511 -0.3542 0.0678 -0.2702 8 HIS E N 7399 C CA . HIS E 9 ? 1.3146 0.6417 1.0631 -0.3671 0.0823 -0.2677 8 HIS E CA 7400 C C . HIS E 9 ? 1.2957 0.6568 1.0811 -0.3689 0.0808 -0.2788 8 HIS E C 7401 O O . HIS E 9 ? 1.2682 0.6476 1.0566 -0.3560 0.0667 -0.2776 8 HIS E O 7402 C CB . HIS E 9 ? 1.3137 0.6257 1.0347 -0.3622 0.0865 -0.2517 8 HIS E CB 7403 C CG . HIS E 9 ? 1.3306 0.6277 1.0441 -0.3793 0.1039 -0.2480 8 HIS E CG 7404 N ND1 . HIS E 9 ? 1.3698 0.6300 1.0645 -0.4001 0.1168 -0.2503 8 HIS E ND1 7405 C CD2 . HIS E 9 ? 1.3166 0.6256 1.0327 -0.3814 0.1124 -0.2431 8 HIS E CD2 7406 C CE1 . HIS E 9 ? 1.3852 0.6337 1.0686 -0.4168 0.1348 -0.2480 8 HIS E CE1 7407 N NE2 . HIS E 9 ? 1.3496 0.6301 1.0491 -0.4046 0.1322 -0.2440 8 HIS E NE2 7408 N N . ALA E 10 ? 1.3086 0.6742 1.1220 -0.3865 0.0945 -0.2926 9 ALA E N 7409 C CA . ALA E 10 ? 1.2969 0.6951 1.1572 -0.3899 0.0949 -0.3089 9 ALA E CA 7410 C C . ALA E 10 ? 1.3171 0.7094 1.1846 -0.4130 0.1244 -0.3149 9 ALA E C 7411 O O . ALA E 10 ? 1.3523 0.7089 1.1861 -0.4297 0.1422 -0.3090 9 ALA E O 7412 C CB . ALA E 10 ? 1.2930 0.7095 1.1974 -0.3901 0.0809 -0.3323 9 ALA E CB 7413 N N . ASN E 11 ? 1.3069 0.7285 1.2137 -0.4155 0.1288 -0.3277 10 ASN E N 7414 C CA . ASN E 11 ? 1.3286 0.7477 1.2472 -0.4418 0.1615 -0.3398 10 ASN E CA 7415 C C . ASN E 11 ? 1.3074 0.7723 1.2979 -0.4426 0.1613 -0.3678 10 ASN E C 7416 O O . ASN E 11 ? 1.2879 0.7815 1.3251 -0.4259 0.1334 -0.3831 10 ASN E O 7417 C CB . ASN E 11 ? 1.3478 0.7313 1.2034 -0.4462 0.1748 -0.3133 10 ASN E CB 7418 C CG . ASN E 11 ? 1.3207 0.7237 1.1741 -0.4248 0.1602 -0.2990 10 ASN E CG 7419 O OD1 . ASN E 11 ? 1.2955 0.7371 1.1961 -0.4135 0.1468 -0.3119 10 ASN E OD1 7420 N ND2 . ASN E 11 ? 1.3309 0.7037 1.1291 -0.4191 0.1600 -0.2735 10 ASN E ND2 7421 N N . ASN E 12 ? 1.3209 0.7887 1.3199 -0.4625 0.1901 -0.3767 11 ASN E N 7422 C CA . ASN E 12 ? 1.3071 0.8204 1.3832 -0.4647 0.1921 -0.4087 11 ASN E CA 7423 C C . ASN E 12 ? 1.2903 0.8134 1.3557 -0.4513 0.1859 -0.3936 11 ASN E C 7424 O O . ASN E 12 ? 1.2848 0.8353 1.3995 -0.4612 0.2000 -0.4173 11 ASN E O 7425 C CB . ASN E 12 ? 1.3367 0.8541 1.4496 -0.5038 0.2359 -0.4439 11 ASN E CB 7426 C CG . ASN E 12 ? 1.3611 0.8788 1.5038 -0.5169 0.2406 -0.4675 11 ASN E CG 7427 O OD1 . ASN E 12 ? 1.3436 0.8723 1.5041 -0.4933 0.2056 -0.4663 11 ASN E OD1 7428 N ND2 . ASN E 12 ? 1.4026 0.9039 1.5461 -0.5573 0.2853 -0.4899 11 ASN E ND2 7429 N N . SER E 13 ? 1.2863 0.7889 1.2920 -0.4295 0.1658 -0.3573 12 SER E N 7430 C CA . SER E 13 ? 1.2748 0.7875 1.2705 -0.4137 0.1551 -0.3423 12 SER E CA 7431 C C . SER E 13 ? 1.2606 0.8080 1.3119 -0.3920 0.1200 -0.3590 12 SER E C 7432 O O . SER E 13 ? 1.2607 0.8032 1.3034 -0.3743 0.0889 -0.3536 12 SER E O 7433 C CB . SER E 13 ? 1.2750 0.7574 1.1977 -0.3975 0.1438 -0.3043 12 SER E CB 7434 O OG . SER E 13 ? 1.2462 0.7400 1.1618 -0.3820 0.1325 -0.2915 12 SER E OG 7435 N N . THR E 14 ? 1.2580 0.8352 1.3637 -0.3948 0.1234 -0.3812 13 THR E N 7436 C CA . THR E 14 ? 1.2470 0.8502 1.4049 -0.3730 0.0838 -0.3985 13 THR E CA 7437 C C . THR E 14 ? 1.2383 0.8298 1.3488 -0.3515 0.0610 -0.3686 13 THR E C 7438 O O . THR E 14 ? 1.2438 0.8382 1.3686 -0.3315 0.0208 -0.3733 13 THR E O 7439 C CB . THR E 14 ? 1.2394 0.8823 1.4883 -0.3841 0.0947 -0.4418 13 THR E CB 7440 O OG1 . THR E 14 ? 1.2360 0.8801 1.4687 -0.4000 0.1307 -0.4350 13 THR E OG1 7441 C CG2 . THR E 14 ? 1.2528 0.9111 1.5600 -0.4062 0.1157 -0.4795 13 THR E CG2 7442 N N . GLU E 15 ? 1.2342 0.8073 1.2854 -0.3568 0.0849 -0.3393 14 GLU E N 7443 C CA . GLU E 15 ? 1.2209 0.7853 1.2297 -0.3404 0.0710 -0.3130 14 GLU E CA 7444 C C . GLU E 15 ? 1.2220 0.7701 1.1988 -0.3195 0.0321 -0.3003 14 GLU E C 7445 O O . GLU E 15 ? 1.2323 0.7618 1.1797 -0.3183 0.0259 -0.2933 14 GLU E O 7446 C CB . GLU E 15 ? 1.2294 0.7702 1.1764 -0.3481 0.0987 -0.2845 14 GLU E CB 7447 C CG . GLU E 15 ? 1.2352 0.7827 1.1930 -0.3649 0.1295 -0.2894 14 GLU E CG 7448 C CD . GLU E 15 ? 1.2576 0.7699 1.1507 -0.3748 0.1525 -0.2642 14 GLU E CD 7449 O OE1 . GLU E 15 ? 1.2913 0.7779 1.1596 -0.3871 0.1641 -0.2619 14 GLU E OE1 7450 O OE2 . GLU E 15 ? 1.2484 0.7553 1.1150 -0.3698 0.1556 -0.2475 14 GLU E OE2 7451 N N . GLN E 16 ? 1.2162 0.7668 1.1938 -0.3055 0.0072 -0.2981 15 GLN E N 7452 C CA . GLN E 16 ? 1.2330 0.7589 1.1759 -0.2901 -0.0325 -0.2908 15 GLN E CA 7453 C C . GLN E 16 ? 1.2290 0.7337 1.1047 -0.2841 -0.0320 -0.2620 15 GLN E C 7454 O O . GLN E 16 ? 1.2102 0.7264 1.0836 -0.2856 -0.0127 -0.2519 15 GLN E O 7455 C CB . GLN E 16 ? 1.2438 0.7780 1.2391 -0.2791 -0.0720 -0.3163 15 GLN E CB 7456 C CG . GLN E 16 ? 1.2481 0.8018 1.3163 -0.2823 -0.0817 -0.3514 15 GLN E CG 7457 C CD . GLN E 16 ? 1.2601 0.8223 1.3910 -0.2683 -0.1268 -0.3820 15 GLN E CD 7458 O OE1 . GLN E 16 ? 1.2534 0.8154 1.3861 -0.2590 -0.1426 -0.3798 15 GLN E OE1 7459 N NE2 . GLN E 16 ? 1.2743 0.8427 1.4602 -0.2657 -0.1508 -0.4129 15 GLN E NE2 7460 N N . VAL E 17 ? 1.2515 0.7233 1.0718 -0.2797 -0.0519 -0.2513 16 VAL E N 7461 C CA . VAL E 17 ? 1.2574 0.7049 1.0134 -0.2770 -0.0536 -0.2303 16 VAL E CA 7462 C C . VAL E 17 ? 1.3009 0.7071 1.0142 -0.2726 -0.0942 -0.2324 16 VAL E C 7463 O O . VAL E 17 ? 1.3160 0.7092 1.0417 -0.2708 -0.1200 -0.2470 16 VAL E O 7464 C CB . VAL E 17 ? 1.2545 0.6942 0.9675 -0.2837 -0.0240 -0.2146 16 VAL E CB 7465 C CG1 . VAL E 17 ? 1.2223 0.6875 0.9642 -0.2881 0.0089 -0.2109 16 VAL E CG1 7466 C CG2 . VAL E 17 ? 1.2819 0.7016 0.9738 -0.2879 -0.0305 -0.2200 16 VAL E CG2 7467 N N . ASP E 18 ? 1.3186 0.6985 0.9766 -0.2724 -0.1005 -0.2183 17 ASP E N 7468 C CA . ASP E 18 ? 1.3790 0.7031 0.9729 -0.2733 -0.1376 -0.2171 17 ASP E CA 7469 C C . ASP E 18 ? 1.4096 0.7007 0.9249 -0.2873 -0.1176 -0.2049 17 ASP E C 7470 O O . ASP E 18 ? 1.3714 0.6867 0.8878 -0.2925 -0.0783 -0.1974 17 ASP E O 7471 C CB . ASP E 18 ? 1.3940 0.7015 0.9747 -0.2667 -0.1623 -0.2133 17 ASP E CB 7472 C CG . ASP E 18 ? 1.3732 0.7101 1.0366 -0.2528 -0.1880 -0.2327 17 ASP E CG 7473 O OD1 . ASP E 18 ? 1.3532 0.7179 1.0800 -0.2501 -0.1895 -0.2514 17 ASP E OD1 7474 O OD2 . ASP E 18 ? 1.3758 0.7089 1.0442 -0.2456 -0.2056 -0.2320 17 ASP E OD2 7475 N N . THR E 19 ? 1.4839 0.7159 0.9314 -0.2943 -0.1468 -0.2062 18 THR E N 7476 C CA . THR E 19 ? 1.5366 0.7279 0.9008 -0.3129 -0.1283 -0.1999 18 THR E CA 7477 C C . THR E 19 ? 1.6278 0.7428 0.9034 -0.3217 -0.1649 -0.1962 18 THR E C 7478 O O . THR E 19 ? 1.6359 0.7362 0.9239 -0.3095 -0.2051 -0.1975 18 THR E O 7479 C CB . THR E 19 ? 1.5477 0.7365 0.9104 -0.3195 -0.1195 -0.2086 18 THR E CB 7480 O OG1 . THR E 19 ? 1.5915 0.7485 0.8824 -0.3398 -0.0935 -0.2071 18 THR E OG1 7481 C CG2 . THR E 19 ? 1.5947 0.7456 0.9481 -0.3153 -0.1669 -0.2188 18 THR E CG2 7482 N N . ILE E 20 ? 1.7033 0.7656 0.8881 -0.3444 -0.1517 -0.1940 19 ILE E N 7483 C CA . ILE E 20 ? 1.8159 0.7895 0.8943 -0.3596 -0.1832 -0.1895 19 ILE E CA 7484 C C . ILE E 20 ? 1.8737 0.7965 0.9389 -0.3490 -0.2482 -0.1958 19 ILE E C 7485 O O . ILE E 20 ? 1.9093 0.7938 0.9558 -0.3403 -0.2932 -0.1934 19 ILE E O 7486 C CB . ILE E 20 ? 1.8937 0.8150 0.8726 -0.3925 -0.1515 -0.1914 19 ILE E CB 7487 C CG1 . ILE E 20 ? 1.8529 0.8218 0.8500 -0.4023 -0.0921 -0.1908 19 ILE E CG1 7488 C CG2 . ILE E 20 ? 2.0182 0.8308 0.8692 -0.4136 -0.1861 -0.1867 19 ILE E CG2 7489 C CD1 . ILE E 20 ? 1.9054 0.8458 0.8371 -0.4339 -0.0504 -0.2022 19 ILE E CD1 7490 N N . MET E 21 ? 1.8806 0.8035 0.9605 -0.3481 -0.2559 -0.2059 20 MET E N 7491 C CA . MET E 21 ? 1.9455 0.8120 1.0061 -0.3398 -0.3200 -0.2151 20 MET E CA 7492 C C . MET E 21 ? 1.8730 0.8046 1.0582 -0.3123 -0.3417 -0.2308 20 MET E C 7493 O O . MET E 21 ? 1.9190 0.8136 1.1067 -0.3028 -0.3951 -0.2437 20 MET E O 7494 C CB . MET E 21 ? 2.0343 0.8299 0.9977 -0.3634 -0.3222 -0.2175 20 MET E CB 7495 C CG . MET E 21 ? 1.9867 0.8347 0.9814 -0.3729 -0.2666 -0.2222 20 MET E CG 7496 S SD . MET E 21 ? 2.0858 0.8556 0.9853 -0.3962 -0.2783 -0.2303 20 MET E SD 7497 C CE . MET E 21 ? 2.0563 0.8518 1.0471 -0.3666 -0.3305 -0.2442 20 MET E CE 7498 N N . GLU E 22 ? 1.7671 0.7896 1.0522 -0.3013 -0.3020 -0.2320 21 GLU E N 7499 C CA . GLU E 22 ? 1.7047 0.7909 1.1072 -0.2818 -0.3110 -0.2500 21 GLU E CA 7500 C C . GLU E 22 ? 1.6208 0.7750 1.1081 -0.2697 -0.2904 -0.2510 21 GLU E C 7501 O O . GLU E 22 ? 1.5636 0.7625 1.0667 -0.2756 -0.2390 -0.2399 21 GLU E O 7502 C CB . GLU E 22 ? 1.6709 0.7963 1.1079 -0.2873 -0.2750 -0.2550 21 GLU E CB 7503 C CG . GLU E 22 ? 1.7354 0.8064 1.0844 -0.3052 -0.2710 -0.2508 21 GLU E CG 7504 C CD . GLU E 22 ? 1.7040 0.8149 1.1006 -0.3064 -0.2451 -0.2594 21 GLU E CD 7505 O OE1 . GLU E 22 ? 1.6831 0.8191 1.1513 -0.2940 -0.2669 -0.2759 21 GLU E OE1 7506 O OE2 . GLU E 22 ? 1.6984 0.8151 1.0639 -0.3203 -0.2033 -0.2524 21 GLU E OE2 7507 N N . LYS E 23 ? 1.6176 0.7773 1.1605 -0.2531 -0.3324 -0.2666 22 LYS E N 7508 C CA . LYS E 23 ? 1.5404 0.7675 1.1745 -0.2430 -0.3130 -0.2739 22 LYS E CA 7509 C C . LYS E 23 ? 1.4786 0.7720 1.2159 -0.2400 -0.2903 -0.2951 22 LYS E C 7510 O O . LYS E 23 ? 1.4871 0.7726 1.2348 -0.2408 -0.3027 -0.3075 22 LYS E O 7511 C CB . LYS E 23 ? 1.5647 0.7708 1.2209 -0.2274 -0.3666 -0.2869 22 LYS E CB 7512 N N . ASN E 24 ? 1.4152 0.7690 1.2219 -0.2392 -0.2554 -0.2995 23 ASN E N 7513 C CA . ASN E 24 ? 1.3631 0.7758 1.2639 -0.2418 -0.2285 -0.3219 23 ASN E CA 7514 C C . ASN E 24 ? 1.3645 0.7768 1.2585 -0.2508 -0.2120 -0.3233 23 ASN E C 7515 O O . ASN E 24 ? 1.3757 0.7933 1.3199 -0.2471 -0.2352 -0.3490 23 ASN E O 7516 C CB . ASN E 24 ? 1.3614 0.7960 1.3568 -0.2292 -0.2663 -0.3597 23 ASN E CB 7517 C CG . ASN E 24 ? 1.3425 0.7959 1.3691 -0.2222 -0.2696 -0.3633 23 ASN E CG 7518 O OD1 . ASN E 24 ? 1.3679 0.7994 1.4114 -0.2071 -0.3220 -0.3787 23 ASN E OD1 7519 N ND2 . ASN E 24 ? 1.2964 0.7858 1.3287 -0.2326 -0.2169 -0.3498 23 ASN E ND2 7520 N N . VAL E 25 ? 1.3541 0.7610 1.1908 -0.2617 -0.1734 -0.2982 24 VAL E N 7521 C CA . VAL E 25 ? 1.3570 0.7606 1.1796 -0.2703 -0.1558 -0.2969 24 VAL E CA 7522 C C . VAL E 25 ? 1.3098 0.7553 1.1713 -0.2804 -0.1061 -0.2958 24 VAL E C 7523 O O . VAL E 25 ? 1.2864 0.7402 1.1253 -0.2844 -0.0758 -0.2774 24 VAL E O 7524 C CB . VAL E 25 ? 1.3923 0.7511 1.1190 -0.2764 -0.1525 -0.2742 24 VAL E CB 7525 C CG1 . VAL E 25 ? 1.3842 0.7500 1.1022 -0.2858 -0.1221 -0.2708 24 VAL E CG1 7526 C CG2 . VAL E 25 ? 1.4603 0.7617 1.1346 -0.2727 -0.2029 -0.2780 24 VAL E CG2 7527 N N . THR E 26 ? 1.3016 0.7670 1.2161 -0.2856 -0.0997 -0.3158 25 THR E N 7528 C CA . THR E 26 ? 1.2713 0.7665 1.2194 -0.2991 -0.0557 -0.3185 25 THR E CA 7529 C C . THR E 26 ? 1.2710 0.7498 1.1662 -0.3066 -0.0291 -0.2974 25 THR E C 7530 O O . THR E 26 ? 1.2953 0.7535 1.1626 -0.3056 -0.0410 -0.2961 25 THR E O 7531 C CB . THR E 26 ? 1.2733 0.7939 1.2994 -0.3057 -0.0562 -0.3523 25 THR E CB 7532 O OG1 . THR E 26 ? 1.2773 0.8159 1.3649 -0.2966 -0.0846 -0.3783 25 THR E OG1 7533 C CG2 . THR E 26 ? 1.2582 0.7992 1.3076 -0.3256 -0.0078 -0.3561 25 THR E CG2 7534 N N . VAL E 27 ? 1.2512 0.7367 1.1341 -0.3140 0.0042 -0.2834 26 VAL E N 7535 C CA . VAL E 27 ? 1.2545 0.7224 1.0921 -0.3184 0.0249 -0.2654 26 VAL E CA 7536 C C . VAL E 27 ? 1.2499 0.7208 1.0994 -0.3328 0.0569 -0.2653 26 VAL E C 7537 O O . VAL E 27 ? 1.2452 0.7303 1.1209 -0.3407 0.0714 -0.2713 26 VAL E O 7538 C CB . VAL E 27 ? 1.2512 0.7064 1.0383 -0.3106 0.0260 -0.2440 26 VAL E CB 7539 C CG1 . VAL E 27 ? 1.2741 0.7100 1.0262 -0.3034 0.0000 -0.2429 26 VAL E CG1 7540 C CG2 . VAL E 27 ? 1.2331 0.7023 1.0303 -0.3087 0.0330 -0.2382 26 VAL E CG2 7541 N N . THR E 28 ? 1.2633 0.7151 1.0883 -0.3379 0.0670 -0.2593 27 THR E N 7542 C CA . THR E 28 ? 1.2723 0.7097 1.0913 -0.3539 0.0928 -0.2574 27 THR E CA 7543 C C . THR E 28 ? 1.2713 0.6967 1.0620 -0.3556 0.1074 -0.2408 27 THR E C 7544 O O . THR E 28 ? 1.2814 0.6927 1.0675 -0.3728 0.1283 -0.2422 27 THR E O 7545 C CB . THR E 28 ? 1.2909 0.7028 1.0839 -0.3558 0.0934 -0.2533 27 THR E CB 7546 O OG1 . THR E 28 ? 1.3227 0.7084 1.0994 -0.3730 0.1143 -0.2508 27 THR E OG1 7547 C CG2 . THR E 28 ? 1.2859 0.6853 1.0418 -0.3407 0.0833 -0.2382 27 THR E CG2 7548 N N . HIS E 29 ? 1.2640 0.6902 1.0314 -0.3400 0.0969 -0.2264 28 HIS E N 7549 C CA . HIS E 29 ? 1.2642 0.6824 1.0092 -0.3382 0.1058 -0.2117 28 HIS E CA 7550 C C . HIS E 29 ? 1.2391 0.6770 0.9850 -0.3239 0.0937 -0.2064 28 HIS E C 7551 O O . HIS E 29 ? 1.2271 0.6688 0.9663 -0.3146 0.0783 -0.2076 28 HIS E O 7552 C CB . HIS E 29 ? 1.2861 0.6726 0.9934 -0.3343 0.1063 -0.1993 28 HIS E CB 7553 C CG . HIS E 29 ? 1.3246 0.6789 1.0181 -0.3485 0.1143 -0.2018 28 HIS E CG 7554 N ND1 . HIS E 29 ? 1.3370 0.6778 1.0247 -0.3454 0.1058 -0.2055 28 HIS E ND1 7555 C CD2 . HIS E 29 ? 1.3554 0.6826 1.0337 -0.3685 0.1309 -0.2018 28 HIS E CD2 7556 C CE1 . HIS E 29 ? 1.3761 0.6824 1.0462 -0.3611 0.1142 -0.2064 28 HIS E CE1 7557 N NE2 . HIS E 29 ? 1.3920 0.6865 1.0521 -0.3770 0.1305 -0.2041 28 HIS E NE2 7558 N N . ALA E 30 ? 1.2345 0.6792 0.9819 -0.3248 0.1015 -0.2005 29 ALA E N 7559 C CA . ALA E 30 ? 1.2228 0.6823 0.9675 -0.3128 0.0909 -0.1946 29 ALA E CA 7560 C C . ALA E 30 ? 1.2205 0.6755 0.9501 -0.3125 0.1027 -0.1820 29 ALA E C 7561 O O . ALA E 30 ? 1.2309 0.6817 0.9670 -0.3246 0.1180 -0.1837 29 ALA E O 7562 C CB . ALA E 30 ? 1.2141 0.6960 0.9956 -0.3122 0.0785 -0.2086 29 ALA E CB 7563 N N . GLN E 31 ? 1.2182 0.6721 0.9261 -0.3009 0.0970 -0.1716 30 GLN E N 7564 C CA . GLN E 31 ? 1.2191 0.6668 0.9119 -0.2980 0.1047 -0.1599 30 GLN E CA 7565 C C . GLN E 31 ? 1.1940 0.6620 0.8944 -0.2923 0.1008 -0.1569 30 GLN E C 7566 O O . GLN E 31 ? 1.1860 0.6591 0.8759 -0.2843 0.0909 -0.1555 30 GLN E O 7567 C CB . GLN E 31 ? 1.2316 0.6637 0.9023 -0.2888 0.1014 -0.1547 30 GLN E CB 7568 C CG . GLN E 31 ? 1.2385 0.6566 0.8945 -0.2846 0.1045 -0.1448 30 GLN E CG 7569 C CD . GLN E 31 ? 1.2745 0.6625 0.9155 -0.2965 0.1115 -0.1402 30 GLN E CD 7570 O OE1 . GLN E 31 ? 1.3014 0.6678 0.9353 -0.3051 0.1123 -0.1441 30 GLN E OE1 7571 N NE2 . GLN E 31 ? 1.2809 0.6622 0.9109 -0.2997 0.1176 -0.1322 30 GLN E NE2 7572 N N . ASP E 32 ? 1.1832 0.6586 0.8983 -0.2990 0.1099 -0.1575 31 ASP E N 7573 C CA . ASP E 32 ? 1.1569 0.6499 0.8807 -0.2933 0.1062 -0.1547 31 ASP E CA 7574 C C . ASP E 32 ? 1.1489 0.6329 0.8444 -0.2849 0.1084 -0.1402 31 ASP E C 7575 O O . ASP E 32 ? 1.1698 0.6336 0.8475 -0.2869 0.1161 -0.1337 31 ASP E O 7576 C CB . ASP E 32 ? 1.1526 0.6567 0.9038 -0.3049 0.1194 -0.1632 31 ASP E CB 7577 C CG . ASP E 32 ? 1.1382 0.6648 0.9109 -0.2981 0.1112 -0.1660 31 ASP E CG 7578 O OD1 . ASP E 32 ? 1.1311 0.6576 0.8848 -0.2857 0.0979 -0.1558 31 ASP E OD1 7579 O OD2 . ASP E 32 ? 1.1312 0.6746 0.9409 -0.3070 0.1193 -0.1810 31 ASP E OD2 7580 N N . ILE E 33 ? 1.1193 0.6136 0.8091 -0.2762 0.0995 -0.1368 32 ILE E N 7581 C CA . ILE E 33 ? 1.1050 0.5953 0.7748 -0.2687 0.1025 -0.1274 32 ILE E CA 7582 C C . ILE E 33 ? 1.0807 0.5835 0.7536 -0.2654 0.1025 -0.1214 32 ILE E C 7583 O O . ILE E 33 ? 1.0652 0.5673 0.7246 -0.2595 0.1047 -0.1152 32 ILE E O 7584 C CB . ILE E 33 ? 1.1151 0.6010 0.7672 -0.2649 0.0979 -0.1311 32 ILE E CB 7585 C CG1 . ILE E 33 ? 1.1241 0.6103 0.7676 -0.2673 0.0853 -0.1357 32 ILE E CG1 7586 C CG2 . ILE E 33 ? 1.1289 0.6026 0.7801 -0.2661 0.0999 -0.1374 32 ILE E CG2 7587 C CD1 . ILE E 33 ? 1.1407 0.6150 0.7531 -0.2698 0.0859 -0.1398 32 ILE E CD1 7588 N N . LEU E 34 ? 1.0639 0.5795 0.7602 -0.2693 0.1000 -0.1265 33 LEU E N 7589 C CA . LEU E 34 ? 1.0401 0.5689 0.7453 -0.2659 0.0975 -0.1238 33 LEU E CA 7590 C C . LEU E 34 ? 1.0303 0.5652 0.7548 -0.2744 0.1131 -0.1263 33 LEU E C 7591 O O . LEU E 34 ? 1.0324 0.5688 0.7774 -0.2855 0.1214 -0.1379 33 LEU E O 7592 C CB . LEU E 34 ? 1.0410 0.5770 0.7606 -0.2626 0.0765 -0.1328 33 LEU E CB 7593 C CG . LEU E 34 ? 1.0299 0.5760 0.7597 -0.2572 0.0669 -0.1322 33 LEU E CG 7594 C CD1 . LEU E 34 ? 1.0316 0.5678 0.7233 -0.2523 0.0682 -0.1178 33 LEU E CD1 7595 C CD2 . LEU E 34 ? 1.0448 0.5898 0.7926 -0.2531 0.0380 -0.1451 33 LEU E CD2 7596 N N . GLU E 35 ? 1.0167 0.5534 0.7323 -0.2714 0.1188 -0.1173 34 GLU E N 7597 C CA . GLU E 35 ? 1.0154 0.5520 0.7385 -0.2818 0.1357 -0.1188 34 GLU E CA 7598 C C . GLU E 35 ? 0.9977 0.5603 0.7543 -0.2798 0.1316 -0.1278 34 GLU E C 7599 O O . GLU E 35 ? 0.9793 0.5478 0.7281 -0.2687 0.1216 -0.1192 34 GLU E O 7600 C CB . GLU E 35 ? 1.0246 0.5396 0.7117 -0.2788 0.1416 -0.1031 34 GLU E CB 7601 C CG . GLU E 35 ? 1.0359 0.5405 0.7153 -0.2911 0.1583 -0.1020 34 GLU E CG 7602 C CD . GLU E 35 ? 1.0632 0.5467 0.7363 -0.3129 0.1758 -0.1113 34 GLU E CD 7603 O OE1 . GLU E 35 ? 1.0933 0.5462 0.7383 -0.3159 0.1737 -0.1065 34 GLU E OE1 7604 O OE2 . GLU E 35 ? 1.0624 0.5591 0.7600 -0.3283 0.1924 -0.1261 34 GLU E OE2 7605 N N . LYS E 36 ? 0.9921 0.5700 0.7890 -0.2914 0.1398 -0.1479 35 LYS E N 7606 C CA . LYS E 36 ? 0.9730 0.5788 0.8163 -0.2878 0.1309 -0.1640 35 LYS E CA 7607 C C . LYS E 36 ? 0.9685 0.5836 0.8292 -0.3016 0.1553 -0.1733 35 LYS E C 7608 O O . LYS E 36 ? 0.9547 0.5953 0.8604 -0.2987 0.1492 -0.1900 35 LYS E O 7609 C CB . LYS E 36 ? 0.9764 0.5990 0.8701 -0.2883 0.1167 -0.1893 35 LYS E CB 7610 C CG . LYS E 36 ? 0.9850 0.5956 0.8609 -0.2745 0.0868 -0.1826 35 LYS E CG 7611 C CD . LYS E 36 ? 0.9976 0.5896 0.8444 -0.2806 0.0960 -0.1753 35 LYS E CD 7612 C CE . LYS E 36 ? 1.0048 0.6071 0.8939 -0.2927 0.1029 -0.1993 35 LYS E CE 7613 N NZ . LYS E 36 ? 1.0200 0.6011 0.8771 -0.2990 0.1121 -0.1908 35 LYS E NZ 7614 N N . THR E 37 ? 0.9877 0.5772 0.8095 -0.3170 0.1806 -0.1638 36 THR E N 7615 C CA . THR E 37 ? 0.9980 0.5855 0.8237 -0.3374 0.2091 -0.1744 36 THR E CA 7616 C C . THR E 37 ? 0.9982 0.5612 0.7724 -0.3343 0.2131 -0.1506 36 THR E C 7617 O O . THR E 37 ? 0.9951 0.5304 0.7221 -0.3248 0.2030 -0.1281 36 THR E O 7618 C CB . THR E 37 ? 1.0392 0.6020 0.8503 -0.3666 0.2384 -0.1869 36 THR E CB 7619 O OG1 . THR E 37 ? 1.0712 0.5840 0.8095 -0.3695 0.2398 -0.1615 36 THR E OG1 7620 C CG2 . THR E 37 ? 1.0348 0.6169 0.8913 -0.3686 0.2329 -0.2083 36 THR E CG2 7621 N N . HIS E 38 ? 0.9936 0.5678 0.7821 -0.3425 0.2274 -0.1590 37 HIS E N 7622 C CA . HIS E 38 ? 1.0045 0.5541 0.7458 -0.3420 0.2325 -0.1393 37 HIS E CA 7623 C C . HIS E 38 ? 1.0366 0.5720 0.7698 -0.3718 0.2665 -0.1544 37 HIS E C 7624 O O . HIS E 38 ? 1.0409 0.6010 0.8234 -0.3896 0.2858 -0.1847 37 HIS E O 7625 C CB . HIS E 38 ? 0.9682 0.5452 0.7281 -0.3174 0.2105 -0.1300 37 HIS E CB 7626 C CG . HIS E 38 ? 0.9454 0.5652 0.7715 -0.3146 0.2066 -0.1537 37 HIS E CG 7627 N ND1 . HIS E 38 ? 0.9450 0.5786 0.7927 -0.3244 0.2227 -0.1666 37 HIS E ND1 7628 C CD2 . HIS E 38 ? 0.9289 0.5770 0.8050 -0.3024 0.1845 -0.1687 37 HIS E CD2 7629 C CE1 . HIS E 38 ? 0.9249 0.5972 0.8402 -0.3167 0.2099 -0.1904 37 HIS E CE1 7630 N NE2 . HIS E 38 ? 0.9147 0.5934 0.8461 -0.3028 0.1842 -0.1916 37 HIS E NE2 7631 N N . ASN E 39 ? 1.0625 0.5564 0.7343 -0.3787 0.2737 -0.1364 38 ASN E N 7632 C CA . ASN E 39 ? 1.1076 0.5712 0.7494 -0.4126 0.3082 -0.1482 38 ASN E CA 7633 C C . ASN E 39 ? 1.0886 0.5904 0.7754 -0.4153 0.3209 -0.1651 38 ASN E C 7634 O O . ASN E 39 ? 1.1340 0.6168 0.8037 -0.4461 0.3539 -0.1805 38 ASN E O 7635 C CB . ASN E 39 ? 1.1613 0.5507 0.7078 -0.4205 0.3059 -0.1222 38 ASN E CB 7636 C CG . ASN E 39 ? 1.1448 0.5319 0.6728 -0.4006 0.2888 -0.1027 38 ASN E CG 7637 O OD1 . ASN E 39 ? 1.0821 0.5221 0.6634 -0.3781 0.2764 -0.1040 38 ASN E OD1 7638 N ND2 . ASN E 39 ? 1.2003 0.5200 0.6488 -0.4093 0.2856 -0.0851 38 ASN E ND2 7639 N N . GLY E 40 ? 1.0301 0.5795 0.7679 -0.3850 0.2949 -0.1624 39 GLY E N 7640 C CA . GLY E 40 ? 0.9991 0.5919 0.7960 -0.3839 0.3008 -0.1835 39 GLY E CA 7641 C C . GLY E 40 ? 1.0082 0.5844 0.7699 -0.3871 0.3094 -0.1716 39 GLY E C 7642 O O . GLY E 40 ? 0.9950 0.6020 0.8020 -0.3928 0.3214 -0.1929 39 GLY E O 7643 N N . LYS E 41 ? 1.0353 0.5637 0.7214 -0.3822 0.3008 -0.1404 40 LYS E N 7644 C CA . LYS E 41 ? 1.0579 0.5645 0.7055 -0.3849 0.3062 -0.1284 40 LYS E CA 7645 C C . LYS E 41 ? 1.0426 0.5283 0.6481 -0.3575 0.2755 -0.0955 40 LYS E C 7646 O O . LYS E 41 ? 1.0270 0.5120 0.6295 -0.3387 0.2527 -0.0827 40 LYS E O 7647 C CB . LYS E 41 ? 1.1422 0.5932 0.7293 -0.4252 0.3419 -0.1365 40 LYS E CB 7648 C CG . LYS E 41 ? 1.2161 0.6062 0.7380 -0.4440 0.3472 -0.1286 40 LYS E CG 7649 C CD . LYS E 41 ? 1.3041 0.6369 0.7654 -0.4914 0.3881 -0.1429 40 LYS E CD 7650 C CE . LYS E 41 ? 1.3925 0.6393 0.7592 -0.5110 0.3870 -0.1275 40 LYS E CE 7651 N NZ . LYS E 41 ? 1.4164 0.6678 0.8036 -0.5328 0.4079 -0.1488 40 LYS E NZ 7652 N N . LEU E 42 ? 1.0423 0.5142 0.6218 -0.3561 0.2762 -0.0858 41 LEU E N 7653 C CA . LEU E 42 ? 1.0315 0.4854 0.5782 -0.3317 0.2489 -0.0600 41 LEU E CA 7654 C C . LEU E 42 ? 1.0994 0.4768 0.5621 -0.3444 0.2471 -0.0453 41 LEU E C 7655 O O . LEU E 42 ? 1.1497 0.4878 0.5685 -0.3701 0.2677 -0.0491 41 LEU E O 7656 C CB . LEU E 42 ? 0.9906 0.4759 0.5630 -0.3188 0.2451 -0.0584 41 LEU E CB 7657 C CG . LEU E 42 ? 0.9307 0.4803 0.5780 -0.3044 0.2388 -0.0718 41 LEU E CG 7658 C CD1 . LEU E 42 ? 0.9094 0.4807 0.5739 -0.2960 0.2370 -0.0710 41 LEU E CD1 7659 C CD2 . LEU E 42 ? 0.9007 0.4677 0.5639 -0.2805 0.2125 -0.0621 41 LEU E CD2 7660 N N . CYS E 43 ? 1.1039 0.4566 0.5435 -0.3266 0.2203 -0.0306 42 CYS E N 7661 C CA . CYS E 43 ? 1.1749 0.4476 0.5369 -0.3353 0.2083 -0.0188 42 CYS E CA 7662 C C . CYS E 43 ? 1.1721 0.4232 0.5154 -0.3092 0.1747 -0.0036 42 CYS E C 7663 O O . CYS E 43 ? 1.1148 0.4172 0.5089 -0.2832 0.1615 -0.0024 42 CYS E O 7664 C CB . CYS E 43 ? 1.1969 0.4539 0.5537 -0.3369 0.2016 -0.0204 42 CYS E CB 7665 S SG . CYS E 43 ? 1.1985 0.4814 0.5850 -0.3662 0.2382 -0.0421 42 CYS E SG 7666 N N . ASP E 44 ? 1.2453 0.4147 0.5129 -0.3177 0.1594 0.0057 43 ASP E N 7667 C CA . ASP E 44 ? 1.2589 0.3982 0.5121 -0.2910 0.1190 0.0151 43 ASP E CA 7668 C C . ASP E 44 ? 1.2193 0.3912 0.5207 -0.2679 0.1003 0.0106 43 ASP E C 7669 O O . ASP E 44 ? 1.2178 0.3907 0.5219 -0.2783 0.1101 0.0060 43 ASP E O 7670 C CB . ASP E 44 ? 1.3686 0.3994 0.5248 -0.3056 0.0986 0.0240 43 ASP E CB 7671 C CG . ASP E 44 ? 1.4270 0.4106 0.5197 -0.3325 0.1168 0.0281 43 ASP E CG 7672 O OD1 . ASP E 44 ? 1.3778 0.4181 0.5110 -0.3334 0.1400 0.0239 43 ASP E OD1 7673 O OD2 . ASP E 44 ? 1.5321 0.4155 0.5289 -0.3543 0.1068 0.0350 43 ASP E OD2 7674 N N . LEU E 45 ? 1.1815 0.3799 0.5220 -0.2385 0.0757 0.0091 44 LEU E N 7675 C CA . LEU E 45 ? 1.1487 0.3746 0.5342 -0.2185 0.0595 0.0005 44 LEU E CA 7676 C C . LEU E 45 ? 1.2039 0.3648 0.5593 -0.2051 0.0192 -0.0009 44 LEU E C 7677 O O . LEU E 45 ? 1.2023 0.3565 0.5705 -0.1853 -0.0062 -0.0047 44 LEU E O 7678 C CB . LEU E 45 ? 1.0743 0.3742 0.5280 -0.1988 0.0630 -0.0066 44 LEU E CB 7679 C CG . LEU E 45 ? 1.0367 0.3762 0.5397 -0.1859 0.0595 -0.0190 44 LEU E CG 7680 C CD1 . LEU E 45 ? 1.0236 0.3846 0.5326 -0.2009 0.0812 -0.0191 44 LEU E CD1 7681 C CD2 . LEU E 45 ? 0.9812 0.3769 0.5352 -0.1714 0.0634 -0.0273 44 LEU E CD2 7682 N N . ASP E 46 ? 1.2579 0.3687 0.5750 -0.2158 0.0113 0.0000 45 ASP E N 7683 C CA . ASP E 46 ? 1.3293 0.3646 0.6097 -0.2045 -0.0325 -0.0019 45 ASP E CA 7684 C C . ASP E 46 ? 1.3964 0.3558 0.6121 -0.2056 -0.0587 0.0069 45 ASP E C 7685 O O . ASP E 46 ? 1.4177 0.3506 0.6436 -0.1809 -0.1009 -0.0004 45 ASP E O 7686 C CB . ASP E 46 ? 1.2918 0.3693 0.6472 -0.1731 -0.0571 -0.0206 45 ASP E CB 7687 C CG . ASP E 46 ? 1.3658 0.3775 0.6996 -0.1632 -0.0983 -0.0282 45 ASP E CG 7688 O OD1 . ASP E 46 ? 1.4557 0.3745 0.7045 -0.1781 -0.1167 -0.0162 45 ASP E OD1 7689 O OD2 . ASP E 46 ? 1.3384 0.3876 0.7377 -0.1424 -0.1121 -0.0480 45 ASP E OD2 7690 N N . GLY E 47 ? 1.4317 0.3556 0.5827 -0.2352 -0.0333 0.0197 46 GLY E N 7691 C CA . GLY E 47 ? 1.5120 0.3504 0.5825 -0.2437 -0.0543 0.0298 46 GLY E CA 7692 C C . GLY E 47 ? 1.4690 0.3462 0.5682 -0.2321 -0.0509 0.0308 46 GLY E C 7693 O O . GLY E 47 ? 1.5406 0.3457 0.5726 -0.2379 -0.0704 0.0388 46 GLY E O 7694 N N . VAL E 48 ? 1.3619 0.3440 0.5521 -0.2170 -0.0281 0.0230 47 VAL E N 7695 C CA . VAL E 48 ? 1.3222 0.3441 0.5405 -0.2075 -0.0220 0.0240 47 VAL E CA 7696 C C . VAL E 48 ? 1.2695 0.3553 0.5114 -0.2264 0.0273 0.0264 47 VAL E C 7697 O O . VAL E 48 ? 1.1999 0.3548 0.4993 -0.2251 0.0499 0.0201 47 VAL E O 7698 C CB . VAL E 48 ? 1.2525 0.3356 0.5554 -0.1727 -0.0424 0.0099 47 VAL E CB 7699 C CG1 . VAL E 48 ? 1.2126 0.3360 0.5408 -0.1662 -0.0322 0.0115 47 VAL E CG1 7700 C CG2 . VAL E 48 ? 1.3059 0.3300 0.6003 -0.1506 -0.0956 0.0005 47 VAL E CG2 7701 N N . LYS E 49 ? 1.3082 0.3678 0.5064 -0.2434 0.0408 0.0336 48 LYS E N 7702 C CA . LYS E 49 ? 1.2686 0.3804 0.4884 -0.2629 0.0848 0.0317 48 LYS E CA 7703 C C . LYS E 49 ? 1.1641 0.3676 0.4687 -0.2404 0.0913 0.0267 48 LYS E C 7704 O O . LYS E 49 ? 1.1473 0.3611 0.4748 -0.2164 0.0673 0.0266 48 LYS E O 7705 C CB . LYS E 49 ? 1.3414 0.3975 0.4911 -0.2886 0.0983 0.0374 48 LYS E CB 7706 C CG . LYS E 49 ? 1.3264 0.4254 0.4949 -0.3156 0.1466 0.0288 48 LYS E CG 7707 C CD . LYS E 49 ? 1.4048 0.4477 0.5032 -0.3457 0.1656 0.0300 48 LYS E CD 7708 C CE . LYS E 49 ? 1.3508 0.4675 0.5075 -0.3533 0.2015 0.0182 48 LYS E CE 7709 N NZ . LYS E 49 ? 1.4319 0.4983 0.5245 -0.3928 0.2333 0.0118 48 LYS E NZ 7710 N N . PRO E 50 ? 1.0994 0.3661 0.4505 -0.2486 0.1216 0.0203 49 PRO E N 7711 C CA . PRO E 50 ? 1.0176 0.3578 0.4339 -0.2316 0.1269 0.0169 49 PRO E CA 7712 C C . PRO E 50 ? 1.0072 0.3541 0.4178 -0.2369 0.1380 0.0194 49 PRO E C 7713 O O . PRO E 50 ? 1.0610 0.3616 0.4198 -0.2585 0.1493 0.0214 49 PRO E O 7714 C CB . PRO E 50 ? 0.9799 0.3684 0.4372 -0.2400 0.1484 0.0084 49 PRO E CB 7715 C CG . PRO E 50 ? 1.0327 0.3816 0.4490 -0.2689 0.1680 0.0050 49 PRO E CG 7716 C CD . PRO E 50 ? 1.1055 0.3773 0.4557 -0.2712 0.1471 0.0136 49 PRO E CD 7717 N N . LEU E 51 ? 0.9439 0.3435 0.4025 -0.2195 0.1355 0.0183 50 LEU E N 7718 C CA . LEU E 51 ? 0.9258 0.3435 0.3910 -0.2227 0.1469 0.0191 50 LEU E CA 7719 C C . LEU E 51 ? 0.8886 0.3557 0.3955 -0.2327 0.1703 0.0095 50 LEU E C 7720 O O . LEU E 51 ? 0.8360 0.3491 0.3884 -0.2197 0.1662 0.0065 50 LEU E O 7721 C CB . LEU E 51 ? 0.8855 0.3306 0.3800 -0.1991 0.1304 0.0217 50 LEU E CB 7722 C CG . LEU E 51 ? 0.8601 0.3321 0.3700 -0.1989 0.1403 0.0225 50 LEU E CG 7723 C CD1 . LEU E 51 ? 0.9121 0.3381 0.3718 -0.2160 0.1481 0.0259 50 LEU E CD1 7724 C CD2 . LEU E 51 ? 0.8294 0.3223 0.3640 -0.1773 0.1240 0.0239 50 LEU E CD2 7725 N N . ILE E 52 ? 0.9211 0.3746 0.4119 -0.2572 0.1937 0.0017 51 ILE E N 7726 C CA . ILE E 52 ? 0.8901 0.3921 0.4322 -0.2659 0.2131 -0.0143 51 ILE E CA 7727 C C . ILE E 52 ? 0.8683 0.3948 0.4307 -0.2626 0.2179 -0.0169 51 ILE E C 7728 O O . ILE E 52 ? 0.9074 0.4025 0.4326 -0.2767 0.2292 -0.0161 51 ILE E O 7729 C CB . ILE E 52 ? 0.9313 0.4143 0.4599 -0.2970 0.2411 -0.0300 51 ILE E CB 7730 C CG1 . ILE E 52 ? 0.9767 0.4125 0.4599 -0.3057 0.2373 -0.0242 51 ILE E CG1 7731 C CG2 . ILE E 52 ? 0.8910 0.4312 0.4910 -0.2996 0.2529 -0.0520 51 ILE E CG2 7732 C CD1 . ILE E 52 ? 0.9402 0.4001 0.4530 -0.2841 0.2163 -0.0192 51 ILE E CD1 7733 N N . LEU E 53 ? 0.8175 0.3934 0.4323 -0.2456 0.2081 -0.0200 52 LEU E N 7734 C CA . LEU E 53 ? 0.7997 0.3977 0.4338 -0.2386 0.2072 -0.0205 52 LEU E CA 7735 C C . LEU E 53 ? 0.7961 0.4209 0.4699 -0.2533 0.2266 -0.0428 52 LEU E C 7736 O O . LEU E 53 ? 0.7793 0.4243 0.4749 -0.2487 0.2266 -0.0469 52 LEU E O 7737 C CB . LEU E 53 ? 0.7575 0.3848 0.4183 -0.2146 0.1850 -0.0126 52 LEU E CB 7738 C CG . LEU E 53 ? 0.7613 0.3687 0.3932 -0.2005 0.1697 0.0030 52 LEU E CG 7739 C CD1 . LEU E 53 ? 0.7284 0.3629 0.3840 -0.1846 0.1555 0.0059 52 LEU E CD1 7740 C CD2 . LEU E 53 ? 0.7847 0.3648 0.3840 -0.2009 0.1697 0.0106 52 LEU E CD2 7741 N N . ARG E 54 ? 0.8211 0.4475 0.5094 -0.2713 0.2433 -0.0605 53 ARG E N 7742 C CA . ARG E 54 ? 0.8279 0.4784 0.5596 -0.2903 0.2671 -0.0900 53 ARG E CA 7743 C C . ARG E 54 ? 0.7742 0.4755 0.5766 -0.2717 0.2497 -0.1029 53 ARG E C 7744 O O . ARG E 54 ? 0.7545 0.4772 0.5923 -0.2576 0.2291 -0.1066 53 ARG E O 7745 C CB . ARG E 54 ? 0.8833 0.5005 0.5706 -0.3143 0.2940 -0.0931 53 ARG E CB 7746 C CG . ARG E 54 ? 0.9606 0.5137 0.5688 -0.3361 0.3072 -0.0824 53 ARG E CG 7747 C CD . ARG E 54 ? 1.0243 0.5283 0.5687 -0.3590 0.3268 -0.0801 53 ARG E CD 7748 N NE . ARG E 54 ? 1.0444 0.5639 0.6166 -0.3901 0.3658 -0.1135 53 ARG E NE 7749 C CZ . ARG E 54 ? 1.1132 0.5915 0.6433 -0.4307 0.4022 -0.1309 53 ARG E CZ 7750 N NH1 . ARG E 54 ? 1.1746 0.5852 0.6232 -0.4452 0.4015 -0.1148 53 ARG E NH1 7751 N NH2 . ARG E 54 ? 1.1323 0.6349 0.7021 -0.4589 0.4402 -0.1676 53 ARG E NH2 7752 N N . ASP E 55 ? 0.7576 0.4722 0.5760 -0.2717 0.2548 -0.1097 54 ASP E N 7753 C CA . ASP E 55 ? 0.7156 0.4703 0.5954 -0.2527 0.2327 -0.1209 54 ASP E CA 7754 C C . ASP E 55 ? 0.6891 0.4375 0.5419 -0.2304 0.2089 -0.0934 54 ASP E C 7755 O O . ASP E 55 ? 0.6609 0.4319 0.5502 -0.2158 0.1894 -0.0987 54 ASP E O 7756 C CB . ASP E 55 ? 0.7221 0.5025 0.6532 -0.2676 0.2539 -0.1543 54 ASP E CB 7757 C CG . ASP E 55 ? 0.7432 0.5366 0.7147 -0.2920 0.2806 -0.1900 54 ASP E CG 7758 O OD1 . ASP E 55 ? 0.7372 0.5439 0.7413 -0.2850 0.2657 -0.1987 54 ASP E OD1 7759 O OD2 . ASP E 55 ? 0.7774 0.5657 0.7466 -0.3204 0.3182 -0.2113 54 ASP E OD2 7760 N N . CYS E 56 ? 0.6978 0.4136 0.4889 -0.2284 0.2091 -0.0669 55 CYS E N 7761 C CA . CYS E 56 ? 0.6809 0.3914 0.4493 -0.2099 0.1907 -0.0448 55 CYS E CA 7762 C C . CYS E 56 ? 0.6573 0.3666 0.4189 -0.1948 0.1684 -0.0319 55 CYS E C 7763 O O . CYS E 56 ? 0.6656 0.3653 0.4179 -0.1986 0.1693 -0.0314 55 CYS E O 7764 C CB . CYS E 56 ? 0.7114 0.3872 0.4243 -0.2150 0.2002 -0.0288 55 CYS E CB 7765 S SG . CYS E 56 ? 0.7445 0.4120 0.4490 -0.2339 0.2251 -0.0404 55 CYS E SG 7766 N N . SER E 57 ? 0.6305 0.3467 0.3936 -0.1801 0.1503 -0.0227 56 SER E N 7767 C CA . SER E 57 ? 0.6224 0.3301 0.3669 -0.1706 0.1346 -0.0109 56 SER E CA 7768 C C . SER E 57 ? 0.6216 0.3126 0.3310 -0.1667 0.1386 0.0038 56 SER E C 7769 O O . SER E 57 ? 0.6248 0.3081 0.3224 -0.1684 0.1472 0.0071 56 SER E O 7770 C CB . SER E 57 ? 0.6134 0.3279 0.3699 -0.1613 0.1135 -0.0114 56 SER E CB 7771 O OG . SER E 57 ? 0.6054 0.3198 0.3509 -0.1561 0.1135 -0.0029 56 SER E OG 7772 N N . VAL E 58 ? 0.6201 0.3039 0.3148 -0.1621 0.1313 0.0095 57 VAL E N 7773 C CA . VAL E 58 ? 0.6213 0.2948 0.2970 -0.1569 0.1325 0.0163 57 VAL E CA 7774 C C . VAL E 58 ? 0.6101 0.2899 0.2874 -0.1514 0.1311 0.0199 57 VAL E C 7775 O O . VAL E 58 ? 0.6085 0.2804 0.2779 -0.1483 0.1339 0.0229 57 VAL E O 7776 C CB . VAL E 58 ? 0.6239 0.2939 0.2915 -0.1562 0.1287 0.0150 57 VAL E CB 7777 C CG1 . VAL E 58 ? 0.6227 0.2899 0.2857 -0.1510 0.1309 0.0141 57 VAL E CG1 7778 C CG2 . VAL E 58 ? 0.6336 0.2960 0.2988 -0.1605 0.1303 0.0118 57 VAL E CG2 7779 N N . ALA E 59 ? 0.6034 0.2921 0.2875 -0.1502 0.1237 0.0195 58 ALA E N 7780 C CA . ALA E 59 ? 0.5990 0.2932 0.2847 -0.1458 0.1217 0.0227 58 ALA E CA 7781 C C . ALA E 59 ? 0.5952 0.2941 0.2902 -0.1457 0.1286 0.0222 58 ALA E C 7782 O O . ALA E 59 ? 0.5921 0.2877 0.2796 -0.1417 0.1311 0.0263 58 ALA E O 7783 C CB . ALA E 59 ? 0.6027 0.2971 0.2900 -0.1457 0.1081 0.0218 58 ALA E CB 7784 N N . GLY E 60 ? 0.6039 0.3087 0.3149 -0.1520 0.1328 0.0144 59 GLY E N 7785 C CA . GLY E 60 ? 0.6107 0.3165 0.3266 -0.1583 0.1452 0.0096 59 GLY E CA 7786 C C . GLY E 60 ? 0.6369 0.3162 0.3192 -0.1628 0.1541 0.0160 59 GLY E C 7787 O O . GLY E 60 ? 0.6479 0.3165 0.3159 -0.1645 0.1589 0.0185 59 GLY E O 7788 N N . TRP E 61 ? 0.6574 0.3210 0.3241 -0.1649 0.1534 0.0180 60 TRP E N 7789 C CA . TRP E 61 ? 0.6919 0.3216 0.3236 -0.1654 0.1519 0.0243 60 TRP E CA 7790 C C . TRP E 61 ? 0.6838 0.3084 0.3096 -0.1518 0.1398 0.0304 60 TRP E C 7791 O O . TRP E 61 ? 0.7088 0.3099 0.3118 -0.1518 0.1373 0.0338 60 TRP E O 7792 C CB . TRP E 61 ? 0.7146 0.3337 0.3399 -0.1657 0.1479 0.0239 60 TRP E CB 7793 C CG . TRP E 61 ? 0.7568 0.3401 0.3525 -0.1614 0.1375 0.0283 60 TRP E CG 7794 C CD1 . TRP E 61 ? 0.7958 0.3407 0.3558 -0.1641 0.1329 0.0325 60 TRP E CD1 7795 C CD2 . TRP E 61 ? 0.7716 0.3480 0.3695 -0.1537 0.1265 0.0264 60 TRP E CD2 7796 N NE1 . TRP E 61 ? 0.8336 0.3456 0.3747 -0.1561 0.1146 0.0335 60 TRP E NE1 7797 C CE2 . TRP E 61 ? 0.8097 0.3441 0.3784 -0.1494 0.1117 0.0284 60 TRP E CE2 7798 C CE3 . TRP E 61 ? 0.7570 0.3552 0.3771 -0.1507 0.1265 0.0217 60 TRP E CE3 7799 C CZ2 . TRP E 61 ? 0.8257 0.3445 0.3969 -0.1398 0.0955 0.0232 60 TRP E CZ2 7800 C CZ3 . TRP E 61 ? 0.7700 0.3551 0.3901 -0.1440 0.1162 0.0169 60 TRP E CZ3 7801 C CH2 . TRP E 61 ? 0.8068 0.3551 0.4074 -0.1376 0.1002 0.0165 60 TRP E CH2 7802 N N . LEU E 62 ? 0.6610 0.3048 0.3058 -0.1421 0.1329 0.0294 61 LEU E N 7803 C CA . LEU E 62 ? 0.6571 0.2987 0.3049 -0.1307 0.1236 0.0287 61 LEU E CA 7804 C C . LEU E 62 ? 0.6523 0.3030 0.3049 -0.1265 0.1234 0.0312 61 LEU E C 7805 O O . LEU E 62 ? 0.6626 0.2984 0.3084 -0.1192 0.1148 0.0311 61 LEU E O 7806 C CB . LEU E 62 ? 0.6378 0.2959 0.3032 -0.1276 0.1232 0.0219 61 LEU E CB 7807 C CG . LEU E 62 ? 0.6506 0.2974 0.3126 -0.1296 0.1214 0.0176 61 LEU E CG 7808 C CD1 . LEU E 62 ? 0.6426 0.3049 0.3180 -0.1316 0.1260 0.0089 61 LEU E CD1 7809 C CD2 . LEU E 62 ? 0.6724 0.2916 0.3260 -0.1218 0.1083 0.0143 61 LEU E CD2 7810 N N . LEU E 63 ? 0.6367 0.3090 0.3019 -0.1299 0.1292 0.0323 62 LEU E N 7811 C CA . LEU E 63 ? 0.6323 0.3140 0.3032 -0.1262 0.1288 0.0345 62 LEU E CA 7812 C C . LEU E 63 ? 0.6490 0.3148 0.3045 -0.1307 0.1329 0.0366 62 LEU E C 7813 O O . LEU E 63 ? 0.6487 0.3102 0.2994 -0.1263 0.1301 0.0389 62 LEU E O 7814 C CB . LEU E 63 ? 0.6179 0.3196 0.3042 -0.1284 0.1288 0.0338 62 LEU E CB 7815 C CG . LEU E 63 ? 0.6237 0.3290 0.3094 -0.1282 0.1252 0.0326 62 LEU E CG 7816 C CD1 . LEU E 63 ? 0.6322 0.3410 0.3213 -0.1321 0.1180 0.0321 62 LEU E CD1 7817 C CD2 . LEU E 63 ? 0.6176 0.3255 0.3034 -0.1242 0.1258 0.0316 62 LEU E CD2 7818 N N . GLY E 64 ? 0.6684 0.3228 0.3132 -0.1422 0.1414 0.0343 63 GLY E N 7819 C CA . GLY E 64 ? 0.6983 0.3291 0.3180 -0.1539 0.1512 0.0334 63 GLY E CA 7820 C C . GLY E 64 ? 0.6878 0.3404 0.3297 -0.1643 0.1661 0.0238 63 GLY E C 7821 O O . GLY E 64 ? 0.7033 0.3456 0.3321 -0.1712 0.1743 0.0219 63 GLY E O 7822 N N . ASN E 65 ? 0.6720 0.3525 0.3490 -0.1657 0.1680 0.0150 64 ASN E N 7823 C CA . ASN E 65 ? 0.6665 0.3695 0.3773 -0.1754 0.1798 -0.0018 64 ASN E CA 7824 C C . ASN E 65 ? 0.6994 0.3786 0.3843 -0.1968 0.2035 -0.0104 64 ASN E C 7825 O O . ASN E 65 ? 0.7302 0.3794 0.3811 -0.2090 0.2118 -0.0088 64 ASN E O 7826 C CB . ASN E 65 ? 0.6567 0.3800 0.4027 -0.1765 0.1765 -0.0136 64 ASN E CB 7827 C CG . ASN E 65 ? 0.6489 0.4007 0.4466 -0.1831 0.1831 -0.0381 64 ASN E CG 7828 O OD1 . ASN E 65 ? 0.6593 0.4107 0.4609 -0.1988 0.2051 -0.0524 64 ASN E OD1 7829 N ND2 . ASN E 65 ? 0.6323 0.4052 0.4695 -0.1720 0.1628 -0.0458 64 ASN E ND2 7830 N N . PRO E 66 ? 0.6999 0.3875 0.3959 -0.2040 0.2153 -0.0207 65 PRO E N 7831 C CA . PRO E 66 ? 0.7493 0.4068 0.4106 -0.2302 0.2424 -0.0310 65 PRO E CA 7832 C C . PRO E 66 ? 0.7768 0.4271 0.4391 -0.2539 0.2653 -0.0489 65 PRO E C 7833 O O . PRO E 66 ? 0.8414 0.4443 0.4456 -0.2773 0.2838 -0.0489 65 PRO E O 7834 C CB . PRO E 66 ? 0.7350 0.4209 0.4342 -0.2334 0.2528 -0.0478 65 PRO E CB 7835 C CG . PRO E 66 ? 0.6875 0.4032 0.4200 -0.2061 0.2258 -0.0372 65 PRO E CG 7836 C CD . PRO E 66 ? 0.6691 0.3881 0.4033 -0.1899 0.2042 -0.0232 65 PRO E CD 7837 N N . MET E 67 ? 0.7457 0.4367 0.4688 -0.2488 0.2622 -0.0644 66 MET E N 7838 C CA . MET E 67 ? 0.7727 0.4622 0.5061 -0.2697 0.2826 -0.0839 66 MET E CA 7839 C C . MET E 67 ? 0.8008 0.4511 0.4804 -0.2715 0.2768 -0.0649 66 MET E C 7840 O O . MET E 67 ? 0.8215 0.4605 0.4956 -0.2914 0.2951 -0.0779 66 MET E O 7841 C CB . MET E 67 ? 0.7328 0.4748 0.5501 -0.2589 0.2720 -0.1060 66 MET E CB 7842 C CG . MET E 67 ? 0.7113 0.4936 0.5949 -0.2560 0.2732 -0.1318 66 MET E CG 7843 S SD . MET E 67 ? 0.7569 0.5356 0.6449 -0.2939 0.3218 -0.1664 66 MET E SD 7844 C CE . MET E 67 ? 0.7907 0.5574 0.6762 -0.3238 0.3517 -0.1885 66 MET E CE 7845 N N . CYS E 68 ? 0.8057 0.4364 0.4505 -0.2512 0.2516 -0.0374 67 CYS E N 7846 C CA . CYS E 68 ? 0.8246 0.4257 0.4330 -0.2470 0.2396 -0.0221 67 CYS E CA 7847 C C . CYS E 68 ? 0.8904 0.4260 0.4195 -0.2553 0.2371 -0.0067 67 CYS E C 7848 O O . CYS E 68 ? 0.9148 0.4247 0.4167 -0.2437 0.2170 0.0078 67 CYS E O 7849 C CB . CYS E 68 ? 0.7706 0.3987 0.4068 -0.2183 0.2114 -0.0091 67 CYS E CB 7850 S SG . CYS E 68 ? 0.7260 0.4067 0.4334 -0.2107 0.2053 -0.0248 67 CYS E SG 7851 N N . ASP E 69 ? 0.9298 0.4339 0.4207 -0.2763 0.2556 -0.0122 68 ASP E N 7852 C CA . ASP E 69 ? 0.9985 0.4300 0.4060 -0.2830 0.2461 0.0030 68 ASP E CA 7853 C C . ASP E 69 ? 1.0658 0.4351 0.4105 -0.2960 0.2415 0.0098 68 ASP E C 7854 O O . ASP E 69 ? 1.1306 0.4381 0.4124 -0.2913 0.2179 0.0249 68 ASP E O 7855 C CB . ASP E 69 ? 1.0371 0.4398 0.4068 -0.3086 0.2702 -0.0061 68 ASP E CB 7856 C CG . ASP E 69 ? 0.9938 0.4285 0.3943 -0.2893 0.2594 -0.0021 68 ASP E CG 7857 O OD1 . ASP E 69 ? 0.9308 0.4022 0.3729 -0.2576 0.2328 0.0089 68 ASP E OD1 7858 O OD2 . ASP E 69 ? 1.0186 0.4395 0.3990 -0.3082 0.2797 -0.0116 68 ASP E OD2 7859 N N . GLU E 70 ? 1.0662 0.4489 0.4289 -0.3110 0.2603 -0.0025 69 GLU E N 7860 C CA . GLU E 70 ? 1.1204 0.4467 0.4275 -0.3225 0.2551 0.0037 69 GLU E CA 7861 C C . GLU E 70 ? 1.0927 0.4130 0.4017 -0.2897 0.2140 0.0220 69 GLU E C 7862 O O . GLU E 70 ? 1.1536 0.4085 0.4014 -0.2928 0.1961 0.0316 69 GLU E O 7863 C CB . GLU E 70 ? 1.1110 0.4701 0.4578 -0.3389 0.2809 -0.0147 69 GLU E CB 7864 C CG . GLU E 70 ? 1.1792 0.4825 0.4712 -0.3531 0.2786 -0.0098 69 GLU E CG 7865 C CD . GLU E 70 ? 1.1622 0.5070 0.5053 -0.3652 0.3014 -0.0292 69 GLU E CD 7866 O OE1 . GLU E 70 ? 1.1392 0.5371 0.5429 -0.3749 0.3271 -0.0523 69 GLU E OE1 7867 O OE2 . GLU E 70 ? 1.1791 0.5036 0.5060 -0.3640 0.2917 -0.0235 69 GLU E OE2 7868 N N . PHE E 71 ? 1.0051 0.3893 0.3825 -0.2602 0.1992 0.0243 70 PHE E N 7869 C CA . PHE E 71 ? 0.9721 0.3655 0.3690 -0.2323 0.1685 0.0336 70 PHE E CA 7870 C C . PHE E 71 ? 0.9636 0.3507 0.3599 -0.2092 0.1416 0.0420 70 PHE E C 7871 O O . PHE E 71 ? 0.9245 0.3434 0.3619 -0.1862 0.1242 0.0426 70 PHE E O 7872 C CB . PHE E 71 ? 0.8957 0.3590 0.3644 -0.2203 0.1732 0.0270 70 PHE E CB 7873 C CG . PHE E 71 ? 0.8943 0.3699 0.3759 -0.2400 0.1964 0.0151 70 PHE E CG 7874 C CD1 . PHE E 71 ? 0.9290 0.3679 0.3777 -0.2510 0.1968 0.0156 70 PHE E CD1 7875 C CD2 . PHE E 71 ? 0.8586 0.3809 0.3882 -0.2474 0.2159 0.0004 70 PHE E CD2 7876 C CE1 . PHE E 71 ? 0.9339 0.3849 0.3974 -0.2704 0.2195 0.0020 70 PHE E CE1 7877 C CE2 . PHE E 71 ? 0.8609 0.3972 0.4123 -0.2648 0.2357 -0.0159 70 PHE E CE2 7878 C CZ . PHE E 71 ? 0.8997 0.4014 0.4179 -0.2772 0.2393 -0.0151 70 PHE E CZ 7879 N N . LEU E 72 ? 1.0149 0.3573 0.3628 -0.2174 0.1389 0.0462 71 LEU E N 7880 C CA . LEU E 72 ? 1.0101 0.3495 0.3630 -0.1958 0.1138 0.0514 71 LEU E CA 7881 C C . LEU E 72 ? 1.0330 0.3382 0.3763 -0.1751 0.0757 0.0539 71 LEU E C 7882 O O . LEU E 72 ? 0.9907 0.3293 0.3811 -0.1511 0.0581 0.0503 71 LEU E O 7883 C CB . LEU E 72 ? 1.0609 0.3535 0.3576 -0.2115 0.1190 0.0546 71 LEU E CB 7884 C CG . LEU E 72 ? 1.0207 0.3647 0.3525 -0.2225 0.1511 0.0473 71 LEU E CG 7885 C CD1 . LEU E 72 ? 1.0922 0.3830 0.3585 -0.2508 0.1692 0.0455 71 LEU E CD1 7886 C CD2 . LEU E 72 ? 0.9543 0.3552 0.3458 -0.1969 0.1402 0.0483 71 LEU E CD2 7887 N N . ASN E 73 ? 1.0989 0.3358 0.3825 -0.1861 0.0634 0.0570 72 ASN E N 7888 C CA . ASN E 73 ? 1.1345 0.3299 0.4077 -0.1670 0.0226 0.0559 72 ASN E CA 7889 C C . ASN E 73 ? 1.1671 0.3317 0.4130 -0.1792 0.0242 0.0562 72 ASN E C 7890 O O . ASN E 73 ? 1.2494 0.3281 0.4156 -0.1938 0.0095 0.0619 72 ASN E O 7891 C CB . ASN E 73 ? 1.2198 0.3262 0.4202 -0.1662 -0.0115 0.0615 72 ASN E CB 7892 C CG . ASN E 73 ? 1.1926 0.3200 0.4128 -0.1546 -0.0164 0.0612 72 ASN E CG 7893 O OD1 . ASN E 73 ? 1.1337 0.3133 0.4236 -0.1286 -0.0300 0.0526 72 ASN E OD1 7894 N ND2 . ASN E 73 ? 1.2452 0.3274 0.4006 -0.1762 -0.0041 0.0687 72 ASN E ND2 7895 N N . VAL E 74 ? 1.1093 0.3375 0.4148 -0.1747 0.0409 0.0503 73 VAL E N 7896 C CA . VAL E 74 ? 1.1373 0.3457 0.4225 -0.1886 0.0488 0.0501 73 VAL E CA 7897 C C . VAL E 74 ? 1.1799 0.3432 0.4532 -0.1724 0.0095 0.0472 73 VAL E C 7898 O O . VAL E 74 ? 1.1679 0.3478 0.4839 -0.1458 -0.0181 0.0393 73 VAL E O 7899 C CB . VAL E 74 ? 1.0629 0.3517 0.4144 -0.1894 0.0776 0.0439 73 VAL E CB 7900 C CG1 . VAL E 74 ? 1.0330 0.3612 0.3997 -0.2051 0.1115 0.0427 73 VAL E CG1 7901 C CG2 . VAL E 74 ? 1.0003 0.3474 0.4229 -0.1626 0.0650 0.0366 73 VAL E CG2 7902 N N . PRO E 75 ? 1.2359 0.3422 0.4550 -0.1889 0.0072 0.0506 74 PRO E N 7903 C CA . PRO E 75 ? 1.2756 0.3394 0.4880 -0.1724 -0.0325 0.0460 74 PRO E CA 7904 C C . PRO E 75 ? 1.1985 0.3369 0.4953 -0.1550 -0.0277 0.0340 74 PRO E C 7905 O O . PRO E 75 ? 1.1253 0.3418 0.4777 -0.1562 0.0040 0.0313 74 PRO E O 7906 C CB . PRO E 75 ? 1.3684 0.3439 0.4868 -0.2014 -0.0308 0.0547 74 PRO E CB 7907 C CG . PRO E 75 ? 1.3460 0.3548 0.4582 -0.2322 0.0224 0.0572 74 PRO E CG 7908 C CD . PRO E 75 ? 1.2783 0.3554 0.4421 -0.2248 0.0415 0.0554 74 PRO E CD 7909 N N . GLU E 76 ? 1.2186 0.3269 0.5216 -0.1392 -0.0622 0.0253 75 GLU E N 7910 C CA . GLU E 76 ? 1.1583 0.3267 0.5342 -0.1249 -0.0590 0.0110 75 GLU E CA 7911 C C . GLU E 76 ? 1.1342 0.3259 0.5038 -0.1461 -0.0236 0.0171 75 GLU E C 7912 O O . GLU E 76 ? 1.1888 0.3264 0.4915 -0.1691 -0.0154 0.0279 75 GLU E O 7913 C CB . GLU E 76 ? 1.2110 0.3301 0.5887 -0.1055 -0.1065 -0.0021 75 GLU E CB 7914 C CG . GLU E 76 ? 1.1694 0.3375 0.6130 -0.0945 -0.1038 -0.0194 75 GLU E CG 7915 C CD . GLU E 76 ? 1.2240 0.3374 0.6696 -0.0756 -0.1539 -0.0351 75 GLU E CD 7916 O OE1 . GLU E 76 ? 1.2857 0.3331 0.6984 -0.0642 -0.1966 -0.0366 75 GLU E OE1 7917 O OE2 . GLU E 76 ? 1.2107 0.3444 0.6908 -0.0716 -0.1533 -0.0473 75 GLU E OE2 7918 N N . TRP E 77 ? 1.0568 0.3245 0.4934 -0.1402 -0.0030 0.0084 76 TRP E N 7919 C CA . TRP E 77 ? 1.0264 0.3233 0.4674 -0.1573 0.0277 0.0117 76 TRP E CA 7920 C C . TRP E 77 ? 0.9984 0.3278 0.4859 -0.1467 0.0243 -0.0009 76 TRP E C 7921 O O . TRP E 77 ? 0.9763 0.3286 0.5095 -0.1277 0.0091 -0.0155 76 TRP E O 7922 C CB . TRP E 77 ? 0.9646 0.3206 0.4325 -0.1658 0.0604 0.0152 76 TRP E CB 7923 C CG . TRP E 77 ? 0.9017 0.3171 0.4292 -0.1494 0.0621 0.0064 76 TRP E CG 7924 C CD1 . TRP E 77 ? 0.8579 0.3189 0.4283 -0.1455 0.0715 -0.0026 76 TRP E CD1 7925 C CD2 . TRP E 77 ? 0.8836 0.3137 0.4283 -0.1380 0.0558 0.0045 76 TRP E CD2 7926 N NE1 . TRP E 77 ? 0.8216 0.3212 0.4299 -0.1352 0.0737 -0.0105 76 TRP E NE1 7927 C CE2 . TRP E 77 ? 0.8320 0.3165 0.4293 -0.1295 0.0643 -0.0065 76 TRP E CE2 7928 C CE3 . TRP E 77 ? 0.9096 0.3083 0.4263 -0.1360 0.0444 0.0106 76 TRP E CE3 7929 C CZ2 . TRP E 77 ? 0.8058 0.3159 0.4308 -0.1199 0.0633 -0.0126 76 TRP E CZ2 7930 C CZ3 . TRP E 77 ? 0.8808 0.3087 0.4302 -0.1231 0.0408 0.0052 76 TRP E CZ3 7931 C CH2 . TRP E 77 ? 0.8292 0.3136 0.4338 -0.1155 0.0511 -0.0067 76 TRP E CH2 7932 N N . SER E 78 ? 1.0046 0.3371 0.4827 -0.1611 0.0411 0.0018 77 SER E N 7933 C CA . SER E 78 ? 0.9802 0.3434 0.4972 -0.1550 0.0423 -0.0091 77 SER E CA 7934 C C . SER E 78 ? 0.9153 0.3461 0.4754 -0.1569 0.0680 -0.0119 77 SER E C 7935 O O . SER E 78 ? 0.8895 0.3556 0.4910 -0.1461 0.0675 -0.0243 77 SER E O 7936 C CB . SER E 78 ? 1.0163 0.3457 0.4988 -0.1702 0.0462 -0.0047 77 SER E CB 7937 O OG . SER E 78 ? 1.0282 0.3494 0.4776 -0.1928 0.0706 0.0055 77 SER E OG 7938 N N . TYR E 79 ? 0.8998 0.3439 0.4482 -0.1724 0.0898 -0.0031 78 TYR E N 7939 C CA . TYR E 79 ? 0.8497 0.3469 0.4312 -0.1738 0.1071 -0.0047 78 TYR E CA 7940 C C . TYR E 79 ? 0.8394 0.3442 0.4134 -0.1808 0.1183 0.0024 78 TYR E C 7941 O O . TYR E 79 ? 0.8670 0.3371 0.4073 -0.1895 0.1192 0.0080 78 TYR E O 7942 C CB . TYR E 79 ? 0.8345 0.3487 0.4263 -0.1828 0.1180 -0.0078 78 TYR E CB 7943 C CG . TYR E 79 ? 0.8604 0.3519 0.4283 -0.1997 0.1278 -0.0047 78 TYR E CG 7944 C CD1 . TYR E 79 ? 0.9056 0.3505 0.4400 -0.2054 0.1204 -0.0033 78 TYR E CD1 7945 C CD2 . TYR E 79 ? 0.8448 0.3589 0.4250 -0.2114 0.1442 -0.0064 78 TYR E CD2 7946 C CE1 . TYR E 79 ? 0.9337 0.3539 0.4415 -0.2259 0.1342 -0.0028 78 TYR E CE1 7947 C CE2 . TYR E 79 ? 0.8687 0.3656 0.4344 -0.2303 0.1582 -0.0100 78 TYR E CE2 7948 C CZ . TYR E 79 ? 0.9131 0.3624 0.4395 -0.2394 0.1558 -0.0077 78 TYR E CZ 7949 O OH . TYR E 79 ? 0.9410 0.3699 0.4485 -0.2630 0.1744 -0.0134 78 TYR E OH 7950 N N . ILE E 80 ? 0.8058 0.3508 0.4071 -0.1783 0.1261 0.0010 79 ILE E N 7951 C CA . ILE E 80 ? 0.7973 0.3558 0.4012 -0.1835 0.1355 0.0047 79 ILE E CA 7952 C C . ILE E 80 ? 0.7910 0.3737 0.4147 -0.1927 0.1456 -0.0002 79 ILE E C 7953 O O . ILE E 80 ? 0.7780 0.3777 0.4173 -0.1896 0.1418 -0.0039 79 ILE E O 7954 C CB . ILE E 80 ? 0.7686 0.3501 0.3892 -0.1724 0.1316 0.0055 79 ILE E CB 7955 C CG1 . ILE E 80 ? 0.7800 0.3427 0.3937 -0.1610 0.1189 0.0048 79 ILE E CG1 7956 C CG2 . ILE E 80 ? 0.7541 0.3489 0.3794 -0.1770 0.1394 0.0083 79 ILE E CG2 7957 C CD1 . ILE E 80 ? 0.7566 0.3429 0.3903 -0.1518 0.1177 0.0019 79 ILE E CD1 7958 N N . VAL E 81 ? 0.8044 0.3863 0.4281 -0.2050 0.1577 -0.0033 80 VAL E N 7959 C CA . VAL E 81 ? 0.7957 0.4030 0.4505 -0.2127 0.1648 -0.0145 80 VAL E CA 7960 C C . VAL E 81 ? 0.7775 0.4089 0.4566 -0.2106 0.1661 -0.0187 80 VAL E C 7961 O O . VAL E 81 ? 0.7820 0.4048 0.4500 -0.2164 0.1758 -0.0178 80 VAL E O 7962 C CB . VAL E 81 ? 0.8276 0.4184 0.4746 -0.2327 0.1822 -0.0238 80 VAL E CB 7963 C CG1 . VAL E 81 ? 0.8136 0.4369 0.5079 -0.2399 0.1892 -0.0427 80 VAL E CG1 7964 C CG2 . VAL E 81 ? 0.8524 0.4163 0.4745 -0.2353 0.1790 -0.0201 80 VAL E CG2 7965 N N . GLU E 82 ? 0.7639 0.4200 0.4729 -0.2033 0.1544 -0.0241 81 GLU E N 7966 C CA . GLU E 82 ? 0.7562 0.4329 0.4918 -0.1993 0.1495 -0.0301 81 GLU E CA 7967 C C . GLU E 82 ? 0.7499 0.4462 0.5285 -0.2008 0.1410 -0.0485 81 GLU E C 7968 O O . GLU E 82 ? 0.7533 0.4467 0.5343 -0.1997 0.1314 -0.0511 81 GLU E O 7969 C CB . GLU E 82 ? 0.7559 0.4326 0.4783 -0.1861 0.1344 -0.0181 81 GLU E CB 7970 C CG . GLU E 82 ? 0.7481 0.4387 0.4885 -0.1807 0.1270 -0.0206 81 GLU E CG 7971 C CD . GLU E 82 ? 0.7581 0.4417 0.4764 -0.1719 0.1150 -0.0090 81 GLU E CD 7972 O OE1 . GLU E 82 ? 0.7748 0.4481 0.4788 -0.1709 0.1037 -0.0072 81 GLU E OE1 7973 O OE2 . GLU E 82 ? 0.7587 0.4442 0.4709 -0.1683 0.1186 -0.0030 81 GLU E OE2 7974 N N . LYS E 83 ? 0.7469 0.4628 0.5633 -0.2028 0.1426 -0.0641 82 LYS E N 7975 C CA . LYS E 83 ? 0.7428 0.4787 0.6121 -0.2007 0.1276 -0.0873 82 LYS E CA 7976 C C . LYS E 83 ? 0.7378 0.4676 0.6046 -0.1842 0.0921 -0.0810 82 LYS E C 7977 O O . LYS E 83 ? 0.7345 0.4509 0.5653 -0.1772 0.0856 -0.0621 82 LYS E O 7978 C CB . LYS E 83 ? 0.7406 0.5009 0.6596 -0.2093 0.1418 -0.1125 82 LYS E CB 7979 C CG . LYS E 83 ? 0.7602 0.5180 0.6766 -0.2330 0.1789 -0.1246 82 LYS E CG 7980 C CD . LYS E 83 ? 0.7664 0.5507 0.7392 -0.2470 0.1984 -0.1584 82 LYS E CD 7981 C CE . LYS E 83 ? 0.7980 0.5779 0.7747 -0.2755 0.2347 -0.1792 82 LYS E CE 7982 N NZ . LYS E 83 ? 0.8312 0.5672 0.7264 -0.2910 0.2577 -0.1546 82 LYS E NZ 7983 N N . ILE E 84 ? 0.7429 0.4772 0.6450 -0.1795 0.0684 -0.0987 83 ILE E N 7984 C CA . ILE E 84 ? 0.7592 0.4720 0.6459 -0.1667 0.0295 -0.0934 83 ILE E CA 7985 C C . ILE E 84 ? 0.7551 0.4686 0.6519 -0.1576 0.0121 -0.0945 83 ILE E C 7986 O O . ILE E 84 ? 0.7747 0.4596 0.6258 -0.1519 -0.0071 -0.0774 83 ILE E O 7987 C CB . ILE E 84 ? 0.7786 0.4899 0.7026 -0.1625 0.0009 -0.1151 83 ILE E CB 7988 C CG1 . ILE E 84 ? 0.7899 0.4920 0.6909 -0.1702 0.0124 -0.1093 83 ILE E CG1 7989 C CG2 . ILE E 84 ? 0.8094 0.4868 0.7124 -0.1499 -0.0463 -0.1120 83 ILE E CG2 7990 C CD1 . ILE E 84 ? 0.7810 0.5106 0.7209 -0.1832 0.0451 -0.1262 83 ILE E CD1 7991 N N . ASN E 85 ? 0.7336 0.4778 0.6892 -0.1585 0.0202 -0.1171 84 ASN E N 7992 C CA . ASN E 85 ? 0.7291 0.4778 0.6999 -0.1500 0.0067 -0.1201 84 ASN E CA 7993 C C . ASN E 85 ? 0.6994 0.4778 0.6959 -0.1602 0.0442 -0.1285 84 ASN E C 7994 O O . ASN E 85 ? 0.6925 0.5001 0.7554 -0.1643 0.0507 -0.1603 84 ASN E O 7995 C CB . ASN E 85 ? 0.7468 0.4963 0.7728 -0.1371 -0.0371 -0.1473 84 ASN E CB 7996 C CG . ASN E 85 ? 0.7526 0.5002 0.7912 -0.1264 -0.0582 -0.1500 84 ASN E CG 7997 O OD1 . ASN E 85 ? 0.7543 0.4824 0.7370 -0.1258 -0.0542 -0.1233 84 ASN E OD1 7998 N ND2 . ASN E 85 ? 0.7578 0.5268 0.8753 -0.1179 -0.0815 -0.1856 84 ASN E ND2 7999 N N . PRO E 86 ? 0.6863 0.4549 0.6304 -0.1656 0.0690 -0.1031 85 PRO E N 8000 C CA . PRO E 86 ? 0.6753 0.4592 0.6265 -0.1779 0.1041 -0.1079 85 PRO E CA 8001 C C . PRO E 86 ? 0.6646 0.4656 0.6497 -0.1729 0.0991 -0.1200 85 PRO E C 8002 O O . PRO E 86 ? 0.6568 0.4478 0.6308 -0.1586 0.0719 -0.1092 85 PRO E O 8003 C CB . PRO E 86 ? 0.6764 0.4367 0.5594 -0.1804 0.1197 -0.0768 85 PRO E CB 8004 C CG . PRO E 86 ? 0.6829 0.4226 0.5307 -0.1704 0.0974 -0.0587 85 PRO E CG 8005 C CD . PRO E 86 ? 0.6927 0.4325 0.5696 -0.1617 0.0646 -0.0722 85 PRO E CD 8006 N N . ALA E 87 ? 0.6436 0.3122 0.5215 -0.0292 0.1568 0.0088 86 ALA E N 8007 C CA . ALA E 87 ? 0.6383 0.3234 0.5323 -0.0272 0.1647 0.0019 86 ALA E CA 8008 C C . ALA E 87 ? 0.6352 0.3256 0.4847 -0.0176 0.1657 0.0022 86 ALA E C 8009 O O . ALA E 87 ? 0.6294 0.3329 0.4887 -0.0153 0.1568 -0.0050 86 ALA E O 8010 C CB . ALA E 87 ? 0.6526 0.3399 0.5720 -0.0308 0.1936 0.0013 86 ALA E CB 8011 N N . ASN E 88 ? 0.6453 0.3248 0.4496 -0.0120 0.1751 0.0104 87 ASN E N 8012 C CA . ASN E 88 ? 0.6451 0.3283 0.4093 -0.0025 0.1763 0.0104 87 ASN E CA 8013 C C . ASN E 88 ? 0.6376 0.3172 0.3763 0.0021 0.1557 0.0125 87 ASN E C 8014 O O . ASN E 88 ? 0.6427 0.3087 0.3567 0.0043 0.1551 0.0198 87 ASN E O 8015 C CB . ASN E 88 ? 0.6727 0.3452 0.4024 0.0011 0.1982 0.0183 87 ASN E CB 8016 C CG . ASN E 88 ? 0.6860 0.3606 0.4381 -0.0048 0.2236 0.0168 87 ASN E CG 8017 O OD1 . ASN E 88 ? 0.7086 0.3696 0.4511 -0.0079 0.2410 0.0265 87 ASN E OD1 8018 N ND2 . ASN E 88 ? 0.6726 0.3636 0.4568 -0.0067 0.2269 0.0045 87 ASN E ND2 8019 N N . ASP E 89 ? 0.6181 0.3096 0.3668 0.0030 0.1399 0.0058 88 ASP E N 8020 C CA . ASP E 89 ? 0.6127 0.3027 0.3441 0.0054 0.1217 0.0066 88 ASP E CA 8021 C C . ASP E 89 ? 0.6018 0.3038 0.3223 0.0128 0.1170 0.0019 88 ASP E C 8022 O O . ASP E 89 ? 0.6052 0.3072 0.3032 0.0202 0.1268 0.0022 88 ASP E O 8023 C CB . ASP E 89 ? 0.6053 0.2948 0.3626 -0.0034 0.1047 0.0046 88 ASP E CB 8024 C CG . ASP E 89 ? 0.6021 0.2874 0.3375 -0.0031 0.0891 0.0059 88 ASP E CG 8025 O OD1 . ASP E 89 ? 0.6086 0.2834 0.3181 -0.0003 0.0924 0.0091 88 ASP E OD1 8026 O OD2 . ASP E 89 ? 0.5993 0.2912 0.3447 -0.0060 0.0745 0.0037 88 ASP E OD2 8027 N N . LEU E 90 ? 0.5883 0.2991 0.3244 0.0108 0.1011 -0.0018 89 LEU E N 8028 C CA . LEU E 90 ? 0.5865 0.3095 0.3214 0.0170 0.0961 -0.0070 89 LEU E CA 8029 C C . LEU E 90 ? 0.5855 0.3203 0.3503 0.0162 0.1027 -0.0152 89 LEU E C 8030 O O . LEU E 90 ? 0.5885 0.3302 0.3892 0.0104 0.0927 -0.0185 89 LEU E O 8031 C CB . LEU E 90 ? 0.5755 0.3017 0.3169 0.0140 0.0773 -0.0063 89 LEU E CB 8032 C CG . LEU E 90 ? 0.5794 0.2946 0.2943 0.0133 0.0725 -0.0006 89 LEU E CG 8033 C CD1 . LEU E 90 ? 0.5719 0.2894 0.2920 0.0083 0.0569 0.0006 89 LEU E CD1 8034 C CD2 . LEU E 90 ? 0.5877 0.3009 0.2751 0.0234 0.0799 -0.0001 89 LEU E CD2 8035 N N . CYS E 91 ? 0.6008 0.3368 0.3505 0.0219 0.1190 -0.0187 90 CYS E N 8036 C CA . CYS E 91 ? 0.6046 0.3513 0.3807 0.0210 0.1305 -0.0287 90 CYS E CA 8037 C C . CYS E 91 ? 0.5677 0.3291 0.3711 0.0227 0.1159 -0.0378 90 CYS E C 8038 O O . CYS E 91 ? 0.5521 0.3220 0.4001 0.0173 0.1118 -0.0436 90 CYS E O 8039 C CB . CYS E 91 ? 0.6463 0.3895 0.3905 0.0268 0.1515 -0.0312 90 CYS E CB 8040 S SG . CYS E 91 ? 0.6838 0.4236 0.3775 0.0390 0.1455 -0.0311 90 CYS E SG 8041 N N . TYR E 92 ? 0.5458 0.3097 0.3270 0.0301 0.1070 -0.0389 91 TYR E N 8042 C CA . TYR E 92 ? 0.5142 0.2895 0.3215 0.0308 0.0899 -0.0442 91 TYR E CA 8043 C C . TYR E 92 ? 0.4965 0.2660 0.3109 0.0239 0.0732 -0.0336 91 TYR E C 8044 O O . TYR E 92 ? 0.4982 0.2571 0.2819 0.0242 0.0721 -0.0251 91 TYR E O 8045 C CB . TYR E 92 ? 0.5079 0.2870 0.2921 0.0407 0.0857 -0.0488 91 TYR E CB 8046 C CG . TYR E 92 ? 0.4873 0.2804 0.3052 0.0424 0.0738 -0.0586 91 TYR E CG 8047 C CD1 . TYR E 92 ? 0.4660 0.2616 0.3049 0.0383 0.0554 -0.0528 91 TYR E CD1 8048 C CD2 . TYR E 92 ? 0.4911 0.2937 0.3192 0.0475 0.0812 -0.0739 91 TYR E CD2 8049 C CE1 . TYR E 92 ? 0.4478 0.2549 0.3205 0.0395 0.0437 -0.0602 91 TYR E CE1 8050 C CE2 . TYR E 92 ? 0.4741 0.2893 0.3379 0.0493 0.0694 -0.0840 91 TYR E CE2 8051 C CZ . TYR E 92 ? 0.4525 0.2698 0.3404 0.0453 0.0501 -0.0762 91 TYR E CZ 8052 O OH . TYR E 92 ? 0.4375 0.2661 0.3637 0.0467 0.0376 -0.0846 91 TYR E OH 8053 N N . PRO E 93 ? 0.4798 0.2548 0.3336 0.0173 0.0599 -0.0345 92 PRO E N 8054 C CA . PRO E 93 ? 0.4789 0.2447 0.3328 0.0091 0.0443 -0.0238 92 PRO E CA 8055 C C . PRO E 93 ? 0.4845 0.2477 0.3147 0.0107 0.0338 -0.0176 92 PRO E C 8056 O O . PRO E 93 ? 0.4823 0.2534 0.3085 0.0181 0.0347 -0.0221 92 PRO E O 8057 C CB . PRO E 93 ? 0.4685 0.2402 0.3720 0.0025 0.0305 -0.0263 92 PRO E CB 8058 C CG . PRO E 93 ? 0.4597 0.2464 0.3878 0.0089 0.0338 -0.0381 92 PRO E CG 8059 C CD . PRO E 93 ? 0.4728 0.2611 0.3719 0.0170 0.0565 -0.0452 92 PRO E CD 8060 N N . GLY E 94 ? 0.4997 0.2516 0.3154 0.0036 0.0246 -0.0081 93 GLY E N 8061 C CA . GLY E 94 ? 0.5087 0.2571 0.3026 0.0032 0.0180 -0.0021 93 GLY E CA 8062 C C . GLY E 94 ? 0.5275 0.2610 0.2885 -0.0013 0.0209 0.0040 93 GLY E C 8063 O O . GLY E 94 ? 0.5320 0.2567 0.2949 -0.0080 0.0179 0.0061 93 GLY E O 8064 N N . ASN E 95 ? 0.5399 0.2706 0.2745 0.0023 0.0266 0.0055 94 ASN E N 8065 C CA . ASN E 95 ? 0.5606 0.2775 0.2656 -0.0014 0.0310 0.0089 94 ASN E CA 8066 C C . ASN E 95 ? 0.5631 0.2790 0.2475 0.0070 0.0435 0.0062 94 ASN E C 8067 O O . ASN E 95 ? 0.5439 0.2691 0.2331 0.0150 0.0457 0.0033 94 ASN E O 8068 C CB . ASN E 95 ? 0.5891 0.2977 0.2830 -0.0118 0.0202 0.0154 94 ASN E CB 8069 C CG . ASN E 95 ? 0.6062 0.3231 0.3084 -0.0112 0.0158 0.0181 94 ASN E CG 8070 O OD1 . ASN E 95 ? 0.6087 0.3390 0.3328 -0.0035 0.0164 0.0139 94 ASN E OD1 8071 N ND2 . ASN E 95 ? 0.6401 0.3482 0.3238 -0.0197 0.0121 0.0246 94 ASN E ND2 8072 N N . PHE E 96 ? 0.5806 0.2844 0.2452 0.0052 0.0499 0.0066 95 PHE E N 8073 C CA . PHE E 96 ? 0.5886 0.2884 0.2365 0.0119 0.0600 0.0044 95 PHE E CA 8074 C C . PHE E 96 ? 0.5994 0.2920 0.2315 0.0052 0.0604 0.0049 95 PHE E C 8075 O O . PHE E 96 ? 0.6287 0.3094 0.2472 -0.0034 0.0586 0.0055 95 PHE E O 8076 C CB . PHE E 96 ? 0.6119 0.3020 0.2524 0.0138 0.0674 0.0042 95 PHE E CB 8077 C CG . PHE E 96 ? 0.6269 0.3150 0.2587 0.0242 0.0757 0.0029 95 PHE E CG 8078 C CD1 . PHE E 96 ? 0.6484 0.3318 0.2710 0.0263 0.0794 0.0005 95 PHE E CD1 8079 C CD2 . PHE E 96 ? 0.6288 0.3183 0.2615 0.0314 0.0798 0.0041 95 PHE E CD2 8080 C CE1 . PHE E 96 ? 0.6553 0.3357 0.2749 0.0363 0.0840 -0.0003 95 PHE E CE1 8081 C CE2 . PHE E 96 ? 0.6456 0.3302 0.2677 0.0408 0.0840 0.0047 95 PHE E CE2 8082 C CZ . PHE E 96 ? 0.6495 0.3297 0.2676 0.0436 0.0845 0.0027 95 PHE E CZ 8083 N N . ASN E 97 ? 0.5803 0.2794 0.2143 0.0087 0.0632 0.0037 96 ASN E N 8084 C CA . ASN E 97 ? 0.5864 0.2797 0.2060 0.0022 0.0680 0.0034 96 ASN E CA 8085 C C . ASN E 97 ? 0.5928 0.2749 0.1959 0.0030 0.0792 -0.0020 96 ASN E C 8086 O O . ASN E 97 ? 0.5814 0.2640 0.1904 0.0127 0.0845 -0.0055 96 ASN E O 8087 C CB . ASN E 97 ? 0.5848 0.2893 0.2186 0.0069 0.0707 0.0026 96 ASN E CB 8088 C CG . ASN E 97 ? 0.6069 0.3071 0.2292 -0.0030 0.0753 0.0050 96 ASN E CG 8089 O OD1 . ASN E 97 ? 0.6382 0.3347 0.2528 -0.0028 0.0883 0.0000 96 ASN E OD1 8090 N ND2 . ASN E 97 ? 0.6060 0.3054 0.2273 -0.0123 0.0654 0.0129 96 ASN E ND2 8091 N N . ASP E 98 ? 0.6133 0.2839 0.1948 -0.0073 0.0818 -0.0029 97 ASP E N 8092 C CA . ASP E 98 ? 0.6304 0.2895 0.1968 -0.0078 0.0929 -0.0107 97 ASP E CA 8093 C C . ASP E 98 ? 0.6237 0.2771 0.1951 -0.0024 0.0920 -0.0125 97 ASP E C 8094 O O . ASP E 98 ? 0.6280 0.2768 0.2016 0.0035 0.1010 -0.0185 97 ASP E O 8095 C CB . ASP E 98 ? 0.6310 0.2954 0.2058 -0.0018 0.1066 -0.0170 97 ASP E CB 8096 C CG . ASP E 98 ? 0.6512 0.3160 0.2148 -0.0111 0.1131 -0.0163 97 ASP E CG 8097 O OD1 . ASP E 98 ? 0.6689 0.3214 0.2038 -0.0231 0.1126 -0.0155 97 ASP E OD1 8098 O OD2 . ASP E 98 ? 0.6525 0.3285 0.2349 -0.0069 0.1181 -0.0161 97 ASP E OD2 8099 N N . TYR E 99 ? 0.6143 0.2671 0.1903 -0.0052 0.0814 -0.0073 98 TYR E N 8100 C CA . TYR E 99 ? 0.6078 0.2564 0.1927 -0.0007 0.0816 -0.0068 98 TYR E CA 8101 C C . TYR E 99 ? 0.6205 0.2538 0.1950 -0.0037 0.0865 -0.0127 98 TYR E C 8102 O O . TYR E 99 ? 0.6132 0.2424 0.1953 0.0030 0.0922 -0.0134 98 TYR E O 8103 C CB . TYR E 99 ? 0.6039 0.2552 0.2003 -0.0054 0.0709 -0.0015 98 TYR E CB 8104 C CG . TYR E 99 ? 0.6028 0.2521 0.2126 -0.0015 0.0738 0.0002 98 TYR E CG 8105 C CD1 . TYR E 99 ? 0.5970 0.2496 0.2108 0.0090 0.0822 0.0018 98 TYR E CD1 8106 C CD2 . TYR E 99 ? 0.6105 0.2536 0.2298 -0.0089 0.0674 0.0010 98 TYR E CD2 8107 C CE1 . TYR E 99 ? 0.6004 0.2492 0.2223 0.0113 0.0870 0.0053 98 TYR E CE1 8108 C CE2 . TYR E 99 ? 0.6051 0.2465 0.2397 -0.0064 0.0730 0.0033 98 TYR E CE2 8109 C CZ . TYR E 99 ? 0.6045 0.2484 0.2381 0.0032 0.0840 0.0060 98 TYR E CZ 8110 O OH . TYR E 99 ? 0.6119 0.2524 0.2566 0.0046 0.0918 0.0100 98 TYR E OH 8111 N N . GLU E 100 ? 0.6446 0.2679 0.2006 -0.0141 0.0832 -0.0169 99 GLU E N 8112 C CA . GLU E 100 ? 0.6670 0.2747 0.2133 -0.0180 0.0857 -0.0248 99 GLU E CA 8113 C C . GLU E 100 ? 0.6729 0.2775 0.2152 -0.0127 0.1002 -0.0338 99 GLU E C 8114 O O . GLU E 100 ? 0.6753 0.2702 0.2225 -0.0102 0.1051 -0.0400 99 GLU E O 8115 C CB . GLU E 100 ? 0.6990 0.2950 0.2224 -0.0313 0.0752 -0.0276 99 GLU E CB 8116 C CG . GLU E 100 ? 0.6987 0.2958 0.2328 -0.0369 0.0579 -0.0199 99 GLU E CG 8117 C CD . GLU E 100 ? 0.6940 0.3056 0.2376 -0.0357 0.0527 -0.0107 99 GLU E CD 8118 O OE1 . GLU E 100 ? 0.7120 0.3273 0.2409 -0.0369 0.0569 -0.0097 99 GLU E OE1 8119 O OE2 . GLU E 100 ? 0.6924 0.3123 0.2613 -0.0335 0.0457 -0.0051 99 GLU E OE2 8120 N N . GLU E 101 ? 0.6707 0.2838 0.2092 -0.0111 0.1072 -0.0349 100 GLU E N 8121 C CA . GLU E 101 ? 0.6757 0.2890 0.2210 -0.0046 0.1217 -0.0439 100 GLU E CA 8122 C C . GLU E 101 ? 0.6557 0.2740 0.2275 0.0089 0.1222 -0.0403 100 GLU E C 8123 O O . GLU E 101 ? 0.6585 0.2701 0.2409 0.0145 0.1291 -0.0471 100 GLU E O 8124 C CB . GLU E 101 ? 0.6707 0.2925 0.2109 -0.0069 0.1299 -0.0456 100 GLU E CB 8125 C CG . GLU E 101 ? 0.6974 0.3094 0.2045 -0.0208 0.1337 -0.0504 100 GLU E CG 8126 C CD . GLU E 101 ? 0.7204 0.3195 0.2148 -0.0238 0.1478 -0.0664 100 GLU E CD 8127 O OE1 . GLU E 101 ? 0.7111 0.3141 0.2280 -0.0152 0.1605 -0.0747 100 GLU E OE1 8128 O OE2 . GLU E 101 ? 0.7403 0.3249 0.2031 -0.0347 0.1453 -0.0716 100 GLU E OE2 8129 N N . LEU E 102 ? 0.6431 0.2714 0.2245 0.0139 0.1141 -0.0298 101 LEU E N 8130 C CA . LEU E 102 ? 0.6400 0.2693 0.2375 0.0255 0.1126 -0.0245 101 LEU E CA 8131 C C . LEU E 102 ? 0.6570 0.2725 0.2554 0.0248 0.1125 -0.0232 101 LEU E C 8132 O O . LEU E 102 ? 0.6627 0.2708 0.2715 0.0322 0.1154 -0.0235 101 LEU E O 8133 C CB . LEU E 102 ? 0.6211 0.2618 0.2229 0.0295 0.1049 -0.0151 101 LEU E CB 8134 C CG . LEU E 102 ? 0.6226 0.2619 0.2314 0.0402 0.1028 -0.0084 101 LEU E CG 8135 C CD1 . LEU E 102 ? 0.6277 0.2631 0.2466 0.0500 0.1050 -0.0116 101 LEU E CD1 8136 C CD2 . LEU E 102 ? 0.6128 0.2648 0.2229 0.0438 0.0967 -0.0030 101 LEU E CD2 8137 N N . LYS E 103 ? 0.6652 0.2764 0.2561 0.0156 0.1078 -0.0215 102 LYS E N 8138 C CA . LYS E 103 ? 0.6827 0.2808 0.2786 0.0133 0.1076 -0.0208 102 LYS E CA 8139 C C . LYS E 103 ? 0.7032 0.2887 0.2994 0.0129 0.1136 -0.0319 102 LYS E C 8140 O O . LYS E 103 ? 0.7128 0.2881 0.3214 0.0168 0.1157 -0.0306 102 LYS E O 8141 C CB . LYS E 103 ? 0.6893 0.2857 0.2823 0.0029 0.0996 -0.0192 102 LYS E CB 8142 C CG . LYS E 103 ? 0.6783 0.2855 0.2807 0.0043 0.0957 -0.0090 102 LYS E CG 8143 C CD . LYS E 103 ? 0.6879 0.2949 0.2950 -0.0058 0.0861 -0.0084 102 LYS E CD 8144 C CE . LYS E 103 ? 0.6973 0.2963 0.3223 -0.0080 0.0872 -0.0054 102 LYS E CE 8145 N NZ . LYS E 103 ? 0.7006 0.3024 0.3400 -0.0165 0.0769 -0.0045 102 LYS E NZ 8146 N N . HIS E 104 ? 0.7153 0.3008 0.2984 0.0080 0.1176 -0.0430 103 HIS E N 8147 C CA . HIS E 104 ? 0.7304 0.3045 0.3135 0.0071 0.1258 -0.0573 103 HIS E CA 8148 C C . HIS E 104 ? 0.7377 0.3119 0.3438 0.0191 0.1324 -0.0585 103 HIS E C 8149 O O . HIS E 104 ? 0.7468 0.3093 0.3663 0.0216 0.1351 -0.0643 103 HIS E O 8150 C CB . HIS E 104 ? 0.7419 0.3160 0.3015 -0.0014 0.1317 -0.0689 103 HIS E CB 8151 C CG . HIS E 104 ? 0.7556 0.3193 0.3150 -0.0022 0.1437 -0.0866 103 HIS E CG 8152 N ND1 . HIS E 104 ? 0.7793 0.3276 0.3254 -0.0101 0.1423 -0.0981 103 HIS E ND1 8153 C CD2 . HIS E 104 ? 0.7526 0.3191 0.3271 0.0041 0.1571 -0.0965 103 HIS E CD2 8154 C CE1 . HIS E 104 ? 0.7959 0.3380 0.3467 -0.0086 0.1558 -0.1150 103 HIS E CE1 8155 N NE2 . HIS E 104 ? 0.7789 0.3322 0.3491 0.0000 0.1654 -0.1142 103 HIS E NE2 8156 N N . LEU E 105 ? 0.7445 0.3312 0.3581 0.0267 0.1330 -0.0532 104 LEU E N 8157 C CA . LEU E 105 ? 0.7570 0.3433 0.3948 0.0391 0.1340 -0.0518 104 LEU E CA 8158 C C . LEU E 105 ? 0.7659 0.3424 0.4118 0.0445 0.1269 -0.0395 104 LEU E C 8159 O O . LEU E 105 ? 0.7838 0.3504 0.4482 0.0514 0.1271 -0.0402 104 LEU E O 8160 C CB . LEU E 105 ? 0.7428 0.3442 0.3870 0.0462 0.1313 -0.0467 104 LEU E CB 8161 C CG . LEU E 105 ? 0.7489 0.3605 0.3926 0.0424 0.1403 -0.0572 104 LEU E CG 8162 C CD1 . LEU E 105 ? 0.7359 0.3620 0.3921 0.0501 0.1352 -0.0514 104 LEU E CD1 8163 C CD2 . LEU E 105 ? 0.7658 0.3711 0.4252 0.0432 0.1531 -0.0736 104 LEU E CD2 8164 N N . LEU E 106 ? 0.7723 0.3509 0.4059 0.0407 0.1214 -0.0280 105 LEU E N 8165 C CA . LEU E 106 ? 0.7886 0.3585 0.4262 0.0445 0.1177 -0.0144 105 LEU E CA 8166 C C . LEU E 106 ? 0.8171 0.3700 0.4654 0.0411 0.1200 -0.0168 105 LEU E C 8167 O O . LEU E 106 ? 0.8460 0.3880 0.5028 0.0456 0.1187 -0.0059 105 LEU E O 8168 C CB . LEU E 106 ? 0.7794 0.3572 0.4048 0.0398 0.1148 -0.0047 105 LEU E CB 8169 C CG . LEU E 106 ? 0.7868 0.3591 0.4109 0.0436 0.1142 0.0104 105 LEU E CG 8170 C CD1 . LEU E 106 ? 0.7959 0.3685 0.4175 0.0554 0.1103 0.0172 105 LEU E CD1 8171 C CD2 . LEU E 106 ? 0.7769 0.3594 0.3938 0.0376 0.1141 0.0151 105 LEU E CD2 8172 N N . SER E 107 ? 0.8299 0.3793 0.4766 0.0329 0.1230 -0.0310 106 SER E N 8173 C CA . SER E 107 ? 0.8571 0.3902 0.5166 0.0295 0.1244 -0.0371 106 SER E CA 8174 C C . SER E 107 ? 0.8756 0.3999 0.5554 0.0368 0.1284 -0.0463 106 SER E C 8175 O O . SER E 107 ? 0.8842 0.3944 0.5791 0.0350 0.1296 -0.0534 106 SER E O 8176 C CB . SER E 107 ? 0.8687 0.3998 0.5154 0.0177 0.1237 -0.0504 106 SER E CB 8177 O OG . SER E 107 ? 0.8858 0.4211 0.5205 0.0160 0.1292 -0.0659 106 SER E OG 8178 N N . ARG E 108 ? 0.8802 0.4128 0.5651 0.0452 0.1298 -0.0473 107 ARG E N 8179 C CA . ARG E 108 ? 0.9016 0.4270 0.6136 0.0537 0.1321 -0.0552 107 ARG E CA 8180 C C . ARG E 108 ? 0.8696 0.3926 0.5932 0.0653 0.1231 -0.0376 107 ARG E C 8181 O O . ARG E 108 ? 0.8639 0.3825 0.6129 0.0742 0.1210 -0.0413 107 ARG E O 8182 C CB . ARG E 108 ? 0.9356 0.4717 0.6505 0.0539 0.1411 -0.0733 107 ARG E CB 8183 C CG . ARG E 108 ? 0.9731 0.5167 0.6589 0.0419 0.1479 -0.0838 107 ARG E CG 8184 C CD . ARG E 108 ? 1.0355 0.5674 0.7181 0.0338 0.1553 -0.1029 107 ARG E CD 8185 N NE . ARG E 108 ? 1.0686 0.5980 0.7201 0.0216 0.1514 -0.1032 107 ARG E NE 8186 C CZ . ARG E 108 ? 1.1093 0.6299 0.7445 0.0121 0.1559 -0.1207 107 ARG E CZ 8187 N NH1 . ARG E 108 ? 1.1230 0.6372 0.7687 0.0130 0.1678 -0.1411 107 ARG E NH1 8188 N NH2 . ARG E 108 ? 1.1283 0.6456 0.7366 0.0016 0.1477 -0.1188 107 ARG E NH2 8189 N N . ILE E 109 ? 0.8364 0.3616 0.5408 0.0650 0.1174 -0.0194 108 ILE E N 8190 C CA . ILE E 109 ? 0.8230 0.3446 0.5267 0.0749 0.1082 -0.0021 108 ILE E CA 8191 C C . ILE E 109 ? 0.8335 0.3394 0.5301 0.0730 0.1062 0.0162 108 ILE E C 8192 O O . ILE E 109 ? 0.8220 0.3291 0.5065 0.0639 0.1114 0.0194 108 ILE E O 8193 C CB . ILE E 109 ? 0.7973 0.3363 0.4814 0.0770 0.1048 0.0019 108 ILE E CB 8194 C CG1 . ILE E 109 ? 0.7794 0.3320 0.4763 0.0798 0.1071 -0.0139 108 ILE E CG1 8195 C CG2 . ILE E 109 ? 0.8028 0.3359 0.4770 0.0859 0.0942 0.0198 108 ILE E CG2 8196 C CD1 . ILE E 109 ? 0.7576 0.3289 0.4379 0.0779 0.1066 -0.0141 108 ILE E CD1 8197 N N . ASN E 110 ? 0.8537 0.3442 0.5602 0.0813 0.0985 0.0286 109 ASN E N 8198 C CA . ASN E 110 ? 0.8808 0.3527 0.5818 0.0795 0.0978 0.0481 109 ASN E CA 8199 C C . ASN E 110 ? 0.8851 0.3522 0.5584 0.0849 0.0910 0.0692 109 ASN E C 8200 O O . ASN E 110 ? 0.8997 0.3530 0.5597 0.0814 0.0942 0.0869 109 ASN E O 8201 C CB . ASN E 110 ? 0.9070 0.3586 0.6395 0.0835 0.0936 0.0486 109 ASN E CB 8202 C CG . ASN E 110 ? 0.9090 0.3613 0.6664 0.0772 0.1015 0.0275 109 ASN E CG 8203 O OD1 . ASN E 110 ? 0.9203 0.3748 0.7016 0.0815 0.1010 0.0102 109 ASN E OD1 8204 N ND2 . ASN E 110 ? 0.9115 0.3616 0.6644 0.0667 0.1089 0.0274 109 ASN E ND2 8205 N N . HIS E 111 ? 0.8720 0.3493 0.5367 0.0930 0.0820 0.0670 110 HIS E N 8206 C CA . HIS E 111 ? 0.8917 0.3639 0.5257 0.0986 0.0735 0.0844 110 HIS E CA 8207 C C . HIS E 111 ? 0.8760 0.3661 0.5024 0.1053 0.0650 0.0760 110 HIS E C 8208 O O . HIS E 111 ? 0.8628 0.3612 0.5158 0.1107 0.0595 0.0619 110 HIS E O 8209 C CB . HIS E 111 ? 0.9259 0.3721 0.5625 0.1059 0.0609 0.1018 110 HIS E CB 8210 C CG . HIS E 111 ? 0.9591 0.3933 0.5536 0.1084 0.0548 0.1232 110 HIS E CG 8211 N ND1 . HIS E 111 ? 0.9955 0.4082 0.5812 0.1175 0.0366 0.1392 110 HIS E ND1 8212 C CD2 . HIS E 111 ? 0.9607 0.4003 0.5179 0.1028 0.0646 0.1305 110 HIS E CD2 8213 C CE1 . HIS E 111 ? 1.0232 0.4274 0.5618 0.1169 0.0357 0.1558 110 HIS E CE1 8214 N NE2 . HIS E 111 ? 1.0000 0.4210 0.5219 0.1081 0.0541 0.1499 110 HIS E NE2 8215 N N . PHE E 112 ? 0.8726 0.3685 0.4653 0.1045 0.0653 0.0837 111 PHE E N 8216 C CA . PHE E 112 ? 0.8649 0.3741 0.4468 0.1117 0.0546 0.0789 111 PHE E CA 8217 C C . PHE E 112 ? 0.9064 0.3983 0.4575 0.1193 0.0405 0.0961 111 PHE E C 8218 O O . PHE E 112 ? 0.9370 0.4117 0.4612 0.1155 0.0457 0.1128 111 PHE E O 8219 C CB . PHE E 112 ? 0.8346 0.3640 0.4002 0.1050 0.0646 0.0721 111 PHE E CB 8220 C CG . PHE E 112 ? 0.8000 0.3477 0.3886 0.0981 0.0739 0.0553 111 PHE E CG 8221 C CD1 . PHE E 112 ? 0.7836 0.3423 0.3967 0.1023 0.0691 0.0414 111 PHE E CD1 8222 C CD2 . PHE E 112 ? 0.7905 0.3438 0.3756 0.0870 0.0873 0.0535 111 PHE E CD2 8223 C CE1 . PHE E 112 ? 0.7632 0.3363 0.3903 0.0949 0.0788 0.0274 111 PHE E CE1 8224 C CE2 . PHE E 112 ? 0.7668 0.3339 0.3670 0.0802 0.0932 0.0394 111 PHE E CE2 8225 C CZ . PHE E 112 ? 0.7545 0.3307 0.3722 0.0838 0.0895 0.0269 111 PHE E CZ 8226 N N . GLU E 113 ? 0.9095 0.4052 0.4631 0.1295 0.0226 0.0919 112 GLU E N 8227 C CA . GLU E 113 ? 0.9434 0.4267 0.4590 0.1362 0.0073 0.1046 112 GLU E CA 8228 C C . GLU E 113 ? 0.9080 0.4138 0.4143 0.1375 0.0060 0.0918 112 GLU E C 8229 O O . GLU E 113 ? 0.8768 0.3980 0.4135 0.1427 -0.0024 0.0775 112 GLU E O 8230 C CB . GLU E 113 ? 0.9880 0.4533 0.5174 0.1481 -0.0179 0.1109 112 GLU E CB 8231 C CG . GLU E 113 ? 1.0542 0.4992 0.5360 0.1544 -0.0366 0.1276 112 GLU E CG 8232 C CD . GLU E 113 ? 1.1045 0.5288 0.6013 0.1663 -0.0662 0.1355 112 GLU E CD 8233 O OE1 . GLU E 113 ? 1.1195 0.5312 0.6497 0.1674 -0.0685 0.1400 112 GLU E OE1 8234 O OE2 . GLU E 113 ? 1.1462 0.5660 0.6230 0.1749 -0.0891 0.1368 112 GLU E OE2 8235 N N . LYS E 114 ? 0.9106 0.4188 0.3788 0.1322 0.0159 0.0962 113 LYS E N 8236 C CA . LYS E 114 ? 0.8827 0.4122 0.3441 0.1328 0.0156 0.0833 113 LYS E CA 8237 C C . LYS E 114 ? 0.9047 0.4261 0.3436 0.1440 -0.0080 0.0852 113 LYS E C 8238 O O . LYS E 114 ? 0.9486 0.4470 0.3479 0.1465 -0.0154 0.1004 113 LYS E O 8239 C CB . LYS E 114 ? 0.8827 0.4182 0.3173 0.1231 0.0358 0.0849 113 LYS E CB 8240 C CG . LYS E 114 ? 0.8621 0.4207 0.2975 0.1230 0.0363 0.0700 113 LYS E CG 8241 C CD . LYS E 114 ? 0.8584 0.4258 0.2819 0.1127 0.0577 0.0686 113 LYS E CD 8242 C CE . LYS E 114 ? 0.9091 0.4621 0.2838 0.1127 0.0627 0.0780 113 LYS E CE 8243 N NZ . LYS E 114 ? 0.9089 0.4718 0.2811 0.1022 0.0862 0.0749 113 LYS E NZ 8244 N N . ILE E 115 ? 0.8756 0.4146 0.3392 0.1500 -0.0203 0.0702 114 ILE E N 8245 C CA . ILE E 115 ? 0.8978 0.4307 0.3475 0.1613 -0.0463 0.0689 114 ILE E CA 8246 C C . ILE E 115 ? 0.8776 0.4325 0.3272 0.1618 -0.0471 0.0534 114 ILE E C 8247 O O . ILE E 115 ? 0.8370 0.4139 0.3124 0.1551 -0.0316 0.0425 114 ILE E O 8248 C CB . ILE E 115 ? 0.8951 0.4242 0.3877 0.1712 -0.0679 0.0656 114 ILE E CB 8249 C CG1 . ILE E 115 ? 0.8450 0.4011 0.3934 0.1704 -0.0619 0.0468 114 ILE E CG1 8250 C CG2 . ILE E 115 ? 0.9136 0.4220 0.4150 0.1705 -0.0665 0.0791 114 ILE E CG2 8251 C CD1 . ILE E 115 ? 0.8431 0.3977 0.4385 0.1805 -0.0820 0.0409 114 ILE E CD1 8252 N N . GLN E 116 ? 0.9180 0.4652 0.3374 0.1696 -0.0668 0.0527 115 GLN E N 8253 C CA . GLN E 116 ? 0.9097 0.4753 0.3273 0.1710 -0.0701 0.0372 115 GLN E CA 8254 C C . GLN E 116 ? 0.8874 0.4663 0.3542 0.1796 -0.0906 0.0239 115 GLN E C 8255 O O . GLN E 116 ? 0.9246 0.4900 0.3910 0.1900 -0.1175 0.0258 115 GLN E O 8256 C CB . GLN E 116 ? 0.9660 0.5146 0.3223 0.1749 -0.0809 0.0413 115 GLN E CB 8257 C CG . GLN E 116 ? 0.9621 0.5285 0.3145 0.1763 -0.0835 0.0236 115 GLN E CG 8258 C CD . GLN E 116 ? 1.0262 0.5737 0.3146 0.1808 -0.0959 0.0251 115 GLN E CD 8259 O OE1 . GLN E 116 ? 1.0490 0.5940 0.2965 0.1740 -0.0762 0.0257 115 GLN E OE1 8260 N NE2 . GLN E 116 ? 1.0601 0.5933 0.3395 0.1921 -0.1288 0.0251 115 GLN E NE2 8261 N N . ILE E 117 ? 0.8356 0.4401 0.3456 0.1750 -0.0788 0.0111 116 ILE E N 8262 C CA . ILE E 117 ? 0.8145 0.4332 0.3774 0.1814 -0.0932 -0.0013 116 ILE E CA 8263 C C . ILE E 117 ? 0.8146 0.4481 0.3819 0.1850 -0.1045 -0.0155 116 ILE E C 8264 O O . ILE E 117 ? 0.8100 0.4512 0.4158 0.1925 -0.1227 -0.0253 116 ILE E O 8265 C CB . ILE E 117 ? 0.7670 0.4022 0.3780 0.1739 -0.0734 -0.0059 116 ILE E CB 8266 C CG1 . ILE E 117 ? 0.7341 0.3868 0.3421 0.1625 -0.0510 -0.0103 116 ILE E CG1 8267 C CG2 . ILE E 117 ? 0.7743 0.3943 0.3850 0.1712 -0.0643 0.0051 116 ILE E CG2 8268 C CD1 . ILE E 117 ? 0.6975 0.3665 0.3489 0.1553 -0.0355 -0.0164 116 ILE E CD1 8269 N N . ILE E 118 ? 0.8248 0.4631 0.3587 0.1796 -0.0931 -0.0178 117 ILE E N 8270 C CA . ILE E 118 ? 0.8283 0.4785 0.3625 0.1833 -0.1043 -0.0324 117 ILE E CA 8271 C C . ILE E 118 ? 0.8728 0.5116 0.3452 0.1823 -0.1009 -0.0310 117 ILE E C 8272 O O . ILE E 118 ? 0.8661 0.5100 0.3234 0.1728 -0.0768 -0.0289 117 ILE E O 8273 C CB . ILE E 118 ? 0.7757 0.4525 0.3523 0.1759 -0.0893 -0.0431 117 ILE E CB 8274 C CG1 . ILE E 118 ? 0.7429 0.4309 0.3773 0.1755 -0.0888 -0.0451 117 ILE E CG1 8275 C CG2 . ILE E 118 ? 0.7784 0.4663 0.3587 0.1803 -0.1023 -0.0586 117 ILE E CG2 8276 C CD1 . ILE E 118 ? 0.7013 0.4123 0.3739 0.1671 -0.0743 -0.0526 117 ILE E CD1 8277 N N . PRO E 119 ? 0.9221 0.5447 0.3590 0.1917 -0.1249 -0.0330 118 PRO E N 8278 C CA . PRO E 119 ? 0.9722 0.5821 0.3444 0.1899 -0.1186 -0.0323 118 PRO E CA 8279 C C . PRO E 119 ? 0.9614 0.5919 0.3407 0.1857 -0.1066 -0.0497 118 PRO E C 8280 O O . PRO E 119 ? 0.9343 0.5829 0.3570 0.1894 -0.1185 -0.0648 118 PRO E O 8281 C CB . PRO E 119 ? 1.0258 0.6137 0.3617 0.2016 -0.1521 -0.0326 118 PRO E CB 8282 C CG . PRO E 119 ? 1.0139 0.5971 0.3918 0.2084 -0.1723 -0.0260 118 PRO E CG 8283 C CD . PRO E 119 ? 0.9432 0.5552 0.3931 0.2039 -0.1584 -0.0346 118 PRO E CD 8284 N N . LYS E 120 ? 0.9846 0.6117 0.3250 0.1779 -0.0828 -0.0475 119 LYS E N 8285 C CA . LYS E 120 ? 0.9790 0.6232 0.3230 0.1740 -0.0700 -0.0645 119 LYS E CA 8286 C C . LYS E 120 ? 1.0055 0.6459 0.3255 0.1833 -0.0928 -0.0819 119 LYS E C 8287 O O . LYS E 120 ? 0.9842 0.6431 0.3298 0.1833 -0.0923 -0.1006 119 LYS E O 8288 C CB . LYS E 120 ? 1.0091 0.6473 0.3158 0.1640 -0.0390 -0.0580 119 LYS E CB 8289 C CG . LYS E 120 ? 0.9877 0.6475 0.3179 0.1569 -0.0186 -0.0731 119 LYS E CG 8290 C CD . LYS E 120 ? 1.0101 0.6633 0.3141 0.1465 0.0129 -0.0637 119 LYS E CD 8291 C CE . LYS E 120 ? 0.9920 0.6660 0.3256 0.1389 0.0341 -0.0780 119 LYS E CE 8292 N NZ . LYS E 120 ? 1.0204 0.6864 0.3258 0.1295 0.0648 -0.0715 119 LYS E NZ 8293 N N . SER E 121 ? 1.0484 0.6638 0.3204 0.1913 -0.1147 -0.0759 120 SER E N 8294 C CA . SER E 121 ? 1.0828 0.6915 0.3290 0.2009 -0.1415 -0.0929 120 SER E CA 8295 C C . SER E 121 ? 1.0456 0.6702 0.3556 0.2095 -0.1701 -0.1061 120 SER E C 8296 O O . SER E 121 ? 1.0633 0.6899 0.3700 0.2166 -0.1908 -0.1252 120 SER E O 8297 C CB . SER E 121 ? 1.1553 0.7291 0.3276 0.2066 -0.1600 -0.0805 120 SER E CB 8298 O OG . SER E 121 ? 1.1477 0.7108 0.3425 0.2131 -0.1843 -0.0666 120 SER E OG 8299 N N . SER E 122 ? 0.9924 0.6283 0.3614 0.2085 -0.1698 -0.0971 121 SER E N 8300 C CA . SER E 122 ? 0.9618 0.6101 0.3935 0.2162 -0.1952 -0.1065 121 SER E CA 8301 C C . SER E 122 ? 0.9140 0.5910 0.4019 0.2134 -0.1891 -0.1245 121 SER E C 8302 O O . SER E 122 ? 0.8941 0.5824 0.4352 0.2193 -0.2090 -0.1346 121 SER E O 8303 C CB . SER E 122 ? 0.9318 0.5801 0.4041 0.2155 -0.1942 -0.0911 121 SER E CB 8304 O OG . SER E 122 ? 0.8823 0.5492 0.3908 0.2047 -0.1642 -0.0864 121 SER E OG 8305 N N . TRP E 123 ? 0.8981 0.5862 0.3782 0.2043 -0.1621 -0.1283 122 TRP E N 8306 C CA . TRP E 123 ? 0.8552 0.5688 0.3880 0.2008 -0.1561 -0.1437 122 TRP E CA 8307 C C . TRP E 123 ? 0.8914 0.6049 0.4049 0.2070 -0.1708 -0.1661 122 TRP E C 8308 O O . TRP E 123 ? 0.9300 0.6409 0.4043 0.2031 -0.1546 -0.1726 122 TRP E O 8309 C CB . TRP E 123 ? 0.8162 0.5414 0.3561 0.1881 -0.1224 -0.1372 122 TRP E CB 8310 C CG . TRP E 123 ? 0.7796 0.5036 0.3335 0.1815 -0.1078 -0.1172 122 TRP E CG 8311 C CD1 . TRP E 123 ? 0.7932 0.5026 0.3072 0.1765 -0.0910 -0.1010 122 TRP E CD1 8312 C CD2 . TRP E 123 ? 0.7323 0.4693 0.3440 0.1788 -0.1078 -0.1122 122 TRP E CD2 8313 N NE1 . TRP E 123 ? 0.7563 0.4690 0.3003 0.1714 -0.0823 -0.0876 122 TRP E NE1 8314 C CE2 . TRP E 123 ? 0.7198 0.4491 0.3212 0.1725 -0.0913 -0.0943 122 TRP E CE2 8315 C CE3 . TRP E 123 ? 0.6985 0.4523 0.3697 0.1806 -0.1190 -0.1211 122 TRP E CE3 8316 C CZ2 . TRP E 123 ? 0.6802 0.4178 0.3244 0.1679 -0.0851 -0.0869 122 TRP E CZ2 8317 C CZ3 . TRP E 123 ? 0.6580 0.4199 0.3717 0.1753 -0.1110 -0.1117 122 TRP E CZ3 8318 C CH2 . TRP E 123 ? 0.6533 0.4067 0.3509 0.1692 -0.0941 -0.0956 122 TRP E CH2 8319 N N . SER E 124 ? 0.8959 0.6123 0.4397 0.2165 -0.2009 -0.1792 123 SER E N 8320 C CA . SER E 124 ? 0.9348 0.6477 0.4571 0.2241 -0.2208 -0.2024 123 SER E CA 8321 C C . SER E 124 ? 0.9028 0.6401 0.4798 0.2218 -0.2171 -0.2225 123 SER E C 8322 O O . SER E 124 ? 0.9293 0.6658 0.4824 0.2243 -0.2204 -0.2427 123 SER E O 8323 C CB . SER E 124 ? 0.9644 0.6645 0.4892 0.2366 -0.2605 -0.2073 123 SER E CB 8324 O OG . SER E 124 ? 0.9933 0.6706 0.4764 0.2389 -0.2664 -0.1872 123 SER E OG 8325 N N . ASP E 125 ? 0.3674 0.7129 0.3507 0.0021 -0.0836 -0.1902 124 ASP E N 8326 C CA . ASP E 125 ? 0.3734 0.6994 0.3765 -0.0187 -0.0786 -0.2043 124 ASP E CA 8327 C C . ASP E 125 ? 0.3712 0.6509 0.3738 -0.0225 -0.0670 -0.1893 124 ASP E C 8328 O O . ASP E 125 ? 0.3682 0.6263 0.3872 -0.0381 -0.0616 -0.1956 124 ASP E O 8329 C CB . ASP E 125 ? 0.3738 0.7170 0.4044 -0.0337 -0.0806 -0.2132 124 ASP E CB 8330 C CG . ASP E 125 ? 0.3884 0.7783 0.4273 -0.0365 -0.0919 -0.2361 124 ASP E CG 8331 O OD1 . ASP E 125 ? 0.4054 0.8182 0.4258 -0.0235 -0.0997 -0.2431 124 ASP E OD1 8332 O OD2 . ASP E 125 ? 0.3985 0.8043 0.4627 -0.0522 -0.0929 -0.2475 124 ASP E OD2 8333 N N . HIS E 126 ? 0.3673 0.6320 0.3517 -0.0085 -0.0631 -0.1694 125 HIS E N 8334 C CA . HIS E 126 ? 0.3726 0.5988 0.3558 -0.0107 -0.0533 -0.1566 125 HIS E CA 8335 C C . HIS E 126 ? 0.3890 0.6069 0.3491 0.0025 -0.0503 -0.1486 125 HIS E C 8336 O O . HIS E 126 ? 0.4088 0.6468 0.3514 0.0157 -0.0547 -0.1452 125 HIS E O 8337 C CB . HIS E 126 ? 0.3513 0.5652 0.3413 -0.0105 -0.0492 -0.1383 125 HIS E CB 8338 C CG . HIS E 126 ? 0.3374 0.5586 0.3498 -0.0239 -0.0499 -0.1440 125 HIS E CG 8339 N ND1 . HIS E 126 ? 0.3420 0.5972 0.3624 -0.0239 -0.0571 -0.1515 125 HIS E ND1 8340 C CD2 . HIS E 126 ? 0.3349 0.5351 0.3632 -0.0377 -0.0438 -0.1429 125 HIS E CD2 8341 C CE1 . HIS E 126 ? 0.3406 0.5962 0.3822 -0.0386 -0.0546 -0.1554 125 HIS E CE1 8342 N NE2 . HIS E 126 ? 0.3384 0.5595 0.3840 -0.0471 -0.0463 -0.1494 125 HIS E NE2 8343 N N . GLU E 127 ? 0.3895 0.5788 0.3496 -0.0006 -0.0425 -0.1455 126 GLU E N 8344 C CA . GLU E 127 ? 0.3951 0.5746 0.3363 0.0102 -0.0373 -0.1356 126 GLU E CA 8345 C C . GLU E 127 ? 0.3777 0.5457 0.3148 0.0164 -0.0331 -0.1135 126 GLU E C 8346 O O . GLU E 127 ? 0.3611 0.5110 0.3112 0.0098 -0.0294 -0.1062 126 GLU E O 8347 C CB . GLU E 127 ? 0.4064 0.5627 0.3523 0.0049 -0.0306 -0.1415 126 GLU E CB 8348 C CG . GLU E 127 ? 0.4222 0.5706 0.3518 0.0147 -0.0238 -0.1323 126 GLU E CG 8349 C CD . GLU E 127 ? 0.4474 0.6187 0.3553 0.0252 -0.0264 -0.1372 126 GLU E CD 8350 O OE1 . GLU E 127 ? 0.4794 0.6598 0.3846 0.0240 -0.0284 -0.1557 126 GLU E OE1 8351 O OE2 . GLU E 127 ? 0.4541 0.6334 0.3465 0.0352 -0.0260 -0.1224 126 GLU E OE2 8352 N N . ALA E 128 ? 0.3903 0.5685 0.3087 0.0293 -0.0337 -0.1030 127 ALA E N 8353 C CA . ALA E 128 ? 0.3842 0.5498 0.2973 0.0357 -0.0292 -0.0829 127 ALA E CA 8354 C C . ALA E 128 ? 0.3984 0.5513 0.2951 0.0427 -0.0211 -0.0714 127 ALA E C 8355 O O . ALA E 128 ? 0.3905 0.5313 0.2825 0.0472 -0.0165 -0.0554 127 ALA E O 8356 C CB . ALA E 128 ? 0.3960 0.5812 0.3025 0.0454 -0.0357 -0.0778 127 ALA E CB 8357 N N . SER E 129 ? 0.4183 0.5742 0.3071 0.0431 -0.0186 -0.0800 128 SER E N 8358 C CA . SER E 129 ? 0.4390 0.5874 0.3120 0.0494 -0.0098 -0.0701 128 SER E CA 8359 C C . SER E 129 ? 0.4236 0.5557 0.3063 0.0425 -0.0020 -0.0734 128 SER E C 8360 O O . SER E 129 ? 0.4480 0.5799 0.3192 0.0466 0.0051 -0.0706 128 SER E O 8361 C CB . SER E 129 ? 0.4650 0.6352 0.3157 0.0594 -0.0120 -0.0753 128 SER E CB 8362 O OG . SER E 129 ? 0.5040 0.6889 0.3422 0.0695 -0.0180 -0.0675 128 SER E OG 8363 N N . ALA E 130 ? 0.3990 0.5187 0.3021 0.0331 -0.0031 -0.0786 129 ALA E N 8364 C CA . ALA E 130 ? 0.3997 0.5050 0.3127 0.0287 0.0031 -0.0815 129 ALA E CA 8365 C C . ALA E 130 ? 0.3845 0.4723 0.3144 0.0223 0.0048 -0.0731 129 ALA E C 8366 O O . ALA E 130 ? 0.3956 0.4721 0.3368 0.0188 0.0081 -0.0760 129 ALA E O 8367 C CB . ALA E 130 ? 0.4011 0.5096 0.3194 0.0255 0.0004 -0.1011 129 ALA E CB 8368 N N . GLY E 131 ? 0.3750 0.4616 0.3054 0.0222 0.0026 -0.0627 130 GLY E N 8369 C CA . GLY E 131 ? 0.3587 0.4315 0.3019 0.0172 0.0041 -0.0545 130 GLY E CA 8370 C C . GLY E 131 ? 0.3533 0.4176 0.2949 0.0185 0.0118 -0.0439 130 GLY E C 8371 O O . GLY E 131 ? 0.3496 0.4099 0.2881 0.0197 0.0135 -0.0334 130 GLY E O 8372 N N . VAL E 132 ? 0.3512 0.4132 0.2965 0.0181 0.0166 -0.0478 131 VAL E N 8373 C CA . VAL E 132 ? 0.3391 0.3980 0.2842 0.0185 0.0248 -0.0398 131 VAL E CA 8374 C C . VAL E 132 ? 0.3299 0.3832 0.2914 0.0152 0.0262 -0.0426 131 VAL E C 8375 O O . VAL E 132 ? 0.3415 0.3918 0.3106 0.0145 0.0225 -0.0510 131 VAL E O 8376 C CB . VAL E 132 ? 0.3534 0.4215 0.2846 0.0236 0.0311 -0.0409 131 VAL E CB 8377 C CG1 . VAL E 132 ? 0.3596 0.4340 0.2718 0.0291 0.0299 -0.0355 131 VAL E CG1 8378 C CG2 . VAL E 132 ? 0.3580 0.4321 0.2908 0.0255 0.0301 -0.0553 131 VAL E CG2 8379 N N . SER E 133 ? 0.3211 0.3729 0.2883 0.0132 0.0316 -0.0356 132 SER E N 8380 C CA . SER E 133 ? 0.3160 0.3671 0.2987 0.0118 0.0326 -0.0379 132 SER E CA 8381 C C . SER E 133 ? 0.3166 0.3744 0.3029 0.0106 0.0410 -0.0339 132 SER E C 8382 O O . SER E 133 ? 0.3295 0.3861 0.3100 0.0076 0.0456 -0.0261 132 SER E O 8383 C CB . SER E 133 ? 0.3047 0.3487 0.2971 0.0082 0.0271 -0.0345 132 SER E CB 8384 O OG . SER E 133 ? 0.3052 0.3510 0.3111 0.0086 0.0275 -0.0356 132 SER E OG 8385 N N . SER E 134 ? 0.3089 0.3735 0.3059 0.0129 0.0434 -0.0394 133 SER E N 8386 C CA . SER E 134 ? 0.3168 0.3923 0.3223 0.0109 0.0513 -0.0374 133 SER E CA 8387 C C . SER E 134 ? 0.3134 0.3879 0.3297 0.0044 0.0502 -0.0318 133 SER E C 8388 O O . SER E 134 ? 0.3356 0.4189 0.3595 -0.0002 0.0570 -0.0298 133 SER E O 8389 C CB . SER E 134 ? 0.3107 0.3958 0.3277 0.0167 0.0525 -0.0458 133 SER E CB 8390 O OG . SER E 134 ? 0.3018 0.3805 0.3292 0.0190 0.0446 -0.0476 133 SER E OG 8391 N N . ALA E 135 ? 0.3077 0.3727 0.3251 0.0034 0.0421 -0.0302 134 ALA E N 8392 C CA . ALA E 135 ? 0.3105 0.3738 0.3345 -0.0025 0.0405 -0.0259 134 ALA E CA 8393 C C . ALA E 135 ? 0.3330 0.3892 0.3478 -0.0076 0.0459 -0.0195 134 ALA E C 8394 O O . ALA E 135 ? 0.3739 0.4289 0.3953 -0.0139 0.0475 -0.0174 134 ALA E O 8395 C CB . ALA E 135 ? 0.3016 0.3572 0.3262 -0.0013 0.0314 -0.0256 134 ALA E CB 8396 N N . CYS E 136 ? 0.3401 0.3911 0.3393 -0.0045 0.0484 -0.0167 135 CYS E N 8397 C CA . CYS E 136 ? 0.3457 0.3870 0.3335 -0.0066 0.0532 -0.0086 135 CYS E CA 8398 C C . CYS E 136 ? 0.3382 0.3833 0.3156 -0.0053 0.0630 -0.0049 135 CYS E C 8399 O O . CYS E 136 ? 0.3442 0.3868 0.3048 0.0004 0.0629 -0.0019 135 CYS E O 8400 C CB . CYS E 136 ? 0.3483 0.3813 0.3239 -0.0018 0.0462 -0.0067 135 CYS E CB 8401 S SG . CYS E 136 ? 0.3620 0.3913 0.3473 -0.0034 0.0363 -0.0097 135 CYS E SG 8402 N N . PRO E 137 ? 0.3227 0.3766 0.3100 -0.0105 0.0716 -0.0054 136 PRO E N 8403 C CA . PRO E 137 ? 0.3252 0.3848 0.3021 -0.0093 0.0822 -0.0017 136 PRO E CA 8404 C C . PRO E 137 ? 0.3366 0.3816 0.2967 -0.0103 0.0893 0.0107 136 PRO E C 8405 O O . PRO E 137 ? 0.3432 0.3733 0.3052 -0.0146 0.0885 0.0156 136 PRO E O 8406 C CB . PRO E 137 ? 0.3216 0.3957 0.3171 -0.0162 0.0902 -0.0052 136 PRO E CB 8407 C CG . PRO E 137 ? 0.3112 0.3834 0.3245 -0.0228 0.0848 -0.0081 136 PRO E CG 8408 C CD . PRO E 137 ? 0.3087 0.3711 0.3174 -0.0172 0.0719 -0.0101 136 PRO E CD 8409 N N . TYR E 138 ? 0.3400 0.3888 0.2826 -0.0053 0.0961 0.0155 137 TYR E N 8410 C CA . TYR E 138 ? 0.3621 0.3977 0.2871 -0.0050 0.1051 0.0295 137 TYR E CA 8411 C C . TYR E 138 ? 0.3789 0.4267 0.2918 -0.0031 0.1170 0.0333 137 TYR E C 8412 O O . TYR E 138 ? 0.3832 0.4432 0.2830 0.0060 0.1135 0.0286 137 TYR E O 8413 C CB . TYR E 138 ? 0.3627 0.3879 0.2693 0.0048 0.0963 0.0342 137 TYR E CB 8414 C CG . TYR E 138 ? 0.3872 0.3985 0.2724 0.0087 0.1052 0.0502 137 TYR E CG 8415 C CD1 . TYR E 138 ? 0.3991 0.3884 0.2871 0.0026 0.1118 0.0601 137 TYR E CD1 8416 C CD2 . TYR E 138 ? 0.4057 0.4253 0.2670 0.0189 0.1076 0.0555 137 TYR E CD2 8417 C CE1 . TYR E 138 ? 0.4256 0.3981 0.2931 0.0070 0.1211 0.0766 137 TYR E CE1 8418 C CE2 . TYR E 138 ? 0.4332 0.4393 0.2725 0.0241 0.1161 0.0725 137 TYR E CE2 8419 C CZ . TYR E 138 ? 0.4441 0.4251 0.2867 0.0183 0.1232 0.0838 137 TYR E CZ 8420 O OH . TYR E 138 ? 0.4863 0.4501 0.3064 0.0245 0.1323 0.1021 137 TYR E OH 8421 N N . GLN E 139 ? 0.3936 0.4390 0.3115 -0.0125 0.1315 0.0409 138 GLN E N 8422 C CA . GLN E 139 ? 0.4100 0.4680 0.3171 -0.0123 0.1458 0.0461 138 GLN E CA 8423 C C . GLN E 139 ? 0.4018 0.4863 0.3163 -0.0076 0.1428 0.0313 138 GLN E C 8424 O O . GLN E 139 ? 0.4129 0.5089 0.3091 0.0011 0.1452 0.0304 138 GLN E O 8425 C CB . GLN E 139 ? 0.4311 0.4792 0.3056 -0.0025 0.1497 0.0604 138 GLN E CB 8426 C CG . GLN E 139 ? 0.4472 0.4662 0.3137 -0.0052 0.1540 0.0762 138 GLN E CG 8427 C CD . GLN E 139 ? 0.4845 0.4939 0.3184 0.0043 0.1621 0.0942 138 GLN E CD 8428 O OE1 . GLN E 139 ? 0.4902 0.5160 0.3043 0.0156 0.1600 0.0933 138 GLN E OE1 8429 N NE2 . GLN E 139 ? 0.5116 0.4934 0.3390 0.0007 0.1712 0.1104 138 GLN E NE2 8430 N N . GLY E 140 ? 0.3838 0.4773 0.3244 -0.0123 0.1371 0.0192 139 GLY E N 8431 C CA . GLY E 140 ? 0.3872 0.5030 0.3379 -0.0073 0.1349 0.0052 139 GLY E CA 8432 C C . GLY E 140 ? 0.3858 0.5024 0.3303 0.0038 0.1206 -0.0056 139 GLY E C 8433 O O . GLY E 140 ? 0.3860 0.5179 0.3371 0.0092 0.1196 -0.0175 139 GLY E O 8434 N N . ARG E 141 ? 0.3925 0.4930 0.3256 0.0072 0.1103 -0.0024 140 ARG E N 8435 C CA . ARG E 141 ? 0.3842 0.4854 0.3128 0.0156 0.0974 -0.0133 140 ARG E CA 8436 C C . ARG E 141 ? 0.3508 0.4375 0.2874 0.0139 0.0848 -0.0140 140 ARG E C 8437 O O . ARG E 141 ? 0.3417 0.4162 0.2802 0.0087 0.0850 -0.0049 140 ARG E O 8438 C CB . ARG E 141 ? 0.4115 0.5158 0.3131 0.0240 0.0974 -0.0115 140 ARG E CB 8439 C CG . ARG E 141 ? 0.4292 0.5193 0.3143 0.0253 0.0952 0.0018 140 ARG E CG 8440 C CD . ARG E 141 ? 0.4538 0.5511 0.3134 0.0359 0.0909 0.0009 140 ARG E CD 8441 N NE . ARG E 141 ? 0.4664 0.5517 0.3117 0.0395 0.0873 0.0134 140 ARG E NE 8442 C CZ . ARG E 141 ? 0.5030 0.5804 0.3311 0.0415 0.0968 0.0303 140 ARG E CZ 8443 N NH1 . ARG E 141 ? 0.5261 0.6072 0.3487 0.0385 0.1117 0.0376 140 ARG E NH1 8444 N NH2 . ARG E 141 ? 0.5179 0.5834 0.3343 0.0470 0.0920 0.0405 140 ARG E NH2 8445 N N . SER E 142 ? 0.3326 0.4205 0.2732 0.0183 0.0747 -0.0251 141 SER E N 8446 C CA . SER E 142 ? 0.3128 0.3893 0.2587 0.0173 0.0633 -0.0263 141 SER E CA 8447 C C . SER E 142 ? 0.3277 0.3971 0.2565 0.0197 0.0594 -0.0191 141 SER E C 8448 O O . SER E 142 ? 0.3436 0.4193 0.2546 0.0258 0.0595 -0.0197 141 SER E O 8449 C CB . SER E 142 ? 0.2995 0.3776 0.2521 0.0208 0.0553 -0.0394 141 SER E CB 8450 O OG . SER E 142 ? 0.2818 0.3664 0.2490 0.0216 0.0588 -0.0458 141 SER E OG 8451 N N . SER E 143 ? 0.3198 0.3779 0.2543 0.0159 0.0556 -0.0130 142 SER E N 8452 C CA . SER E 143 ? 0.3233 0.3743 0.2449 0.0191 0.0521 -0.0056 142 SER E CA 8453 C C . SER E 143 ? 0.3155 0.3592 0.2490 0.0161 0.0433 -0.0074 142 SER E C 8454 O O . SER E 143 ? 0.2942 0.3398 0.2413 0.0133 0.0385 -0.0154 142 SER E O 8455 C CB . SER E 143 ? 0.3373 0.3795 0.2503 0.0177 0.0622 0.0078 142 SER E CB 8456 O OG . SER E 143 ? 0.3502 0.3851 0.2480 0.0240 0.0595 0.0161 142 SER E OG 8457 N N . PHE E 144 ? 0.3205 0.3554 0.2480 0.0176 0.0420 0.0004 143 PHE E N 8458 C CA . PHE E 144 ? 0.3081 0.3386 0.2445 0.0159 0.0343 -0.0014 143 PHE E CA 8459 C C . PHE E 144 ? 0.3199 0.3390 0.2499 0.0183 0.0355 0.0078 143 PHE E C 8460 O O . PHE E 144 ? 0.3353 0.3485 0.2520 0.0224 0.0417 0.0166 143 PHE E O 8461 C CB . PHE E 144 ? 0.3014 0.3417 0.2365 0.0191 0.0252 -0.0097 143 PHE E CB 8462 C CG . PHE E 144 ? 0.2848 0.3234 0.2325 0.0153 0.0187 -0.0133 143 PHE E CG 8463 C CD1 . PHE E 144 ? 0.2772 0.3130 0.2389 0.0095 0.0186 -0.0167 143 PHE E CD1 8464 C CD2 . PHE E 144 ? 0.2849 0.3264 0.2299 0.0183 0.0131 -0.0126 143 PHE E CD2 8465 C CE1 . PHE E 144 ? 0.2661 0.3003 0.2370 0.0063 0.0136 -0.0183 143 PHE E CE1 8466 C CE2 . PHE E 144 ? 0.2717 0.3132 0.2278 0.0143 0.0086 -0.0154 143 PHE E CE2 8467 C CZ . PHE E 144 ? 0.2653 0.3024 0.2334 0.0081 0.0091 -0.0177 143 PHE E CZ 8468 N N . PHE E 145 ? 0.3127 0.3280 0.2513 0.0165 0.0303 0.0061 144 PHE E N 8469 C CA . PHE E 145 ? 0.3273 0.3311 0.2610 0.0200 0.0311 0.0131 144 PHE E CA 8470 C C . PHE E 145 ? 0.3481 0.3553 0.2650 0.0312 0.0290 0.0182 144 PHE E C 8471 O O . PHE E 145 ? 0.3465 0.3689 0.2611 0.0349 0.0222 0.0125 144 PHE E O 8472 C CB . PHE E 145 ? 0.3148 0.3191 0.2593 0.0179 0.0248 0.0083 144 PHE E CB 8473 C CG . PHE E 145 ? 0.2988 0.3030 0.2583 0.0089 0.0250 0.0032 144 PHE E CG 8474 C CD1 . PHE E 145 ? 0.2979 0.2917 0.2630 0.0037 0.0300 0.0048 144 PHE E CD1 8475 C CD2 . PHE E 145 ? 0.2808 0.2954 0.2487 0.0059 0.0201 -0.0032 144 PHE E CD2 8476 C CE1 . PHE E 145 ? 0.2866 0.2845 0.2649 -0.0034 0.0289 -0.0005 144 PHE E CE1 8477 C CE2 . PHE E 145 ? 0.2722 0.2878 0.2519 0.0000 0.0197 -0.0065 144 PHE E CE2 8478 C CZ . PHE E 145 ? 0.2777 0.2872 0.2626 -0.0042 0.0235 -0.0054 144 PHE E CZ 8479 N N . ARG E 146 ? 0.3774 0.3704 0.2831 0.0365 0.0350 0.0289 145 ARG E N 8480 C CA . ARG E 146 ? 0.4025 0.3979 0.2893 0.0492 0.0342 0.0367 145 ARG E CA 8481 C C . ARG E 146 ? 0.3990 0.4024 0.2849 0.0586 0.0250 0.0348 145 ARG E C 8482 O O . ARG E 146 ? 0.4153 0.4315 0.2883 0.0698 0.0204 0.0370 145 ARG E O 8483 C CB . ARG E 146 ? 0.4528 0.4260 0.3275 0.0524 0.0449 0.0509 145 ARG E CB 8484 C CG . ARG E 146 ? 0.4757 0.4415 0.3508 0.0431 0.0561 0.0546 145 ARG E CG 8485 C CD . ARG E 146 ? 0.5015 0.4828 0.3627 0.0474 0.0577 0.0557 145 ARG E CD 8486 N NE . ARG E 146 ? 0.5311 0.5025 0.3871 0.0418 0.0714 0.0644 145 ARG E NE 8487 C CZ . ARG E 146 ? 0.5456 0.5308 0.4003 0.0380 0.0759 0.0609 145 ARG E CZ 8488 N NH1 . ARG E 146 ? 0.5444 0.5511 0.4027 0.0394 0.0675 0.0481 145 ARG E NH1 8489 N NH2 . ARG E 146 ? 0.5545 0.5317 0.4056 0.0323 0.0897 0.0695 145 ARG E NH2 8490 N N . ASN E 147 ? 0.3707 0.3693 0.2699 0.0549 0.0225 0.0307 146 ASN E N 8491 C CA . ASN E 147 ? 0.3693 0.3751 0.2685 0.0645 0.0156 0.0297 146 ASN E CA 8492 C C . ASN E 147 ? 0.3477 0.3765 0.2592 0.0607 0.0067 0.0178 146 ASN E C 8493 O O . ASN E 147 ? 0.3619 0.4021 0.2759 0.0676 0.0010 0.0156 146 ASN E O 8494 C CB . ASN E 147 ? 0.3694 0.3549 0.2729 0.0653 0.0196 0.0332 146 ASN E CB 8495 C CG . ASN E 147 ? 0.3973 0.3565 0.2891 0.0684 0.0295 0.0453 146 ASN E CG 8496 O OD1 . ASN E 147 ? 0.4277 0.3848 0.3026 0.0791 0.0314 0.0552 146 ASN E OD1 8497 N ND2 . ASN E 147 ? 0.3963 0.3358 0.2966 0.0589 0.0362 0.0446 146 ASN E ND2 8498 N N . VAL E 148 ? 0.3319 0.3675 0.2517 0.0500 0.0060 0.0105 147 VAL E N 8499 C CA . VAL E 148 ? 0.3145 0.3691 0.2452 0.0451 -0.0010 -0.0001 147 VAL E CA 8500 C C . VAL E 148 ? 0.3156 0.3795 0.2439 0.0415 -0.0021 -0.0060 147 VAL E C 8501 O O . VAL E 148 ? 0.3255 0.3809 0.2466 0.0408 0.0034 -0.0024 147 VAL E O 8502 C CB . VAL E 148 ? 0.2995 0.3495 0.2455 0.0348 -0.0005 -0.0043 147 VAL E CB 8503 C CG1 . VAL E 148 ? 0.3084 0.3519 0.2569 0.0385 0.0001 -0.0013 147 VAL E CG1 8504 C CG2 . VAL E 148 ? 0.2988 0.3356 0.2479 0.0269 0.0050 -0.0033 147 VAL E CG2 8505 N N . VAL E 149 ? 0.3057 0.3873 0.2409 0.0386 -0.0085 -0.0160 148 VAL E N 8506 C CA . VAL E 149 ? 0.3139 0.4047 0.2466 0.0359 -0.0101 -0.0241 148 VAL E CA 8507 C C . VAL E 149 ? 0.2998 0.3905 0.2485 0.0242 -0.0115 -0.0336 148 VAL E C 8508 O O . VAL E 149 ? 0.2806 0.3787 0.2403 0.0198 -0.0151 -0.0379 148 VAL E O 8509 C CB . VAL E 149 ? 0.3229 0.4363 0.2464 0.0443 -0.0169 -0.0291 148 VAL E CB 8510 C CG1 . VAL E 149 ? 0.3255 0.4479 0.2448 0.0418 -0.0181 -0.0392 148 VAL E CG1 8511 C CG2 . VAL E 149 ? 0.3445 0.4562 0.2503 0.0583 -0.0154 -0.0170 148 VAL E CG2 8512 N N . TRP E 150 ? 0.3030 0.3847 0.2527 0.0197 -0.0076 -0.0361 149 TRP E N 8513 C CA . TRP E 150 ? 0.3014 0.3791 0.2641 0.0106 -0.0081 -0.0441 149 TRP E CA 8514 C C . TRP E 150 ? 0.3088 0.3999 0.2707 0.0094 -0.0124 -0.0570 149 TRP E C 8515 O O . TRP E 150 ? 0.3300 0.4227 0.2836 0.0124 -0.0110 -0.0614 149 TRP E O 8516 C CB . TRP E 150 ? 0.3013 0.3646 0.2656 0.0088 -0.0022 -0.0412 149 TRP E CB 8517 C CG . TRP E 150 ? 0.3015 0.3570 0.2781 0.0020 -0.0020 -0.0468 149 TRP E CG 8518 C CD1 . TRP E 150 ? 0.3021 0.3588 0.2876 -0.0041 -0.0052 -0.0536 149 TRP E CD1 8519 C CD2 . TRP E 150 ? 0.3034 0.3482 0.2845 0.0012 0.0021 -0.0454 149 TRP E CD2 8520 N NE1 . TRP E 150 ? 0.3085 0.3521 0.3025 -0.0079 -0.0030 -0.0550 149 TRP E NE1 8521 C CE2 . TRP E 150 ? 0.3048 0.3423 0.2963 -0.0036 0.0009 -0.0504 149 TRP E CE2 8522 C CE3 . TRP E 150 ? 0.3185 0.3600 0.2970 0.0043 0.0072 -0.0404 149 TRP E CE3 8523 C CZ2 . TRP E 150 ? 0.3109 0.3379 0.3088 -0.0033 0.0037 -0.0499 149 TRP E CZ2 8524 C CZ3 . TRP E 150 ? 0.3094 0.3444 0.2964 0.0035 0.0097 -0.0414 149 TRP E CZ3 8525 C CH2 . TRP E 150 ? 0.3095 0.3372 0.3054 0.0009 0.0075 -0.0458 149 TRP E CH2 8526 N N . LEU E 151 ? 0.2903 0.3929 0.2612 0.0046 -0.0175 -0.0639 150 LEU E N 8527 C CA . LEU E 151 ? 0.3021 0.4193 0.2752 0.0012 -0.0222 -0.0788 150 LEU E CA 8528 C C . LEU E 151 ? 0.2992 0.4026 0.2842 -0.0090 -0.0199 -0.0877 150 LEU E C 8529 O O . LEU E 151 ? 0.2899 0.3785 0.2849 -0.0149 -0.0167 -0.0823 150 LEU E O 8530 C CB . LEU E 151 ? 0.3043 0.4429 0.2848 -0.0005 -0.0283 -0.0835 150 LEU E CB 8531 C CG . LEU E 151 ? 0.3092 0.4624 0.2795 0.0114 -0.0315 -0.0752 150 LEU E CG 8532 C CD1 . LEU E 151 ? 0.3069 0.4817 0.2889 0.0092 -0.0366 -0.0797 150 LEU E CD1 8533 C CD2 . LEU E 151 ? 0.3254 0.4911 0.2777 0.0224 -0.0343 -0.0769 150 LEU E CD2 8534 N N . ILE E 152 ? 0.3170 0.4249 0.3000 -0.0103 -0.0214 -0.1014 151 ILE E N 8535 C CA . ILE E 152 ? 0.3318 0.4255 0.3273 -0.0203 -0.0195 -0.1121 151 ILE E CA 8536 C C . ILE E 152 ? 0.3465 0.4561 0.3474 -0.0271 -0.0247 -0.1314 151 ILE E C 8537 O O . ILE E 152 ? 0.3487 0.4842 0.3442 -0.0236 -0.0308 -0.1364 151 ILE E O 8538 C CB . ILE E 152 ? 0.3371 0.4120 0.3288 -0.0166 -0.0140 -0.1119 151 ILE E CB 8539 C CG1 . ILE E 152 ? 0.3499 0.4370 0.3260 -0.0076 -0.0144 -0.1176 151 ILE E CG1 8540 C CG2 . ILE E 152 ? 0.3290 0.3892 0.3211 -0.0132 -0.0093 -0.0952 151 ILE E CG2 8541 C CD1 . ILE E 152 ? 0.3627 0.4362 0.3384 -0.0058 -0.0096 -0.1250 151 ILE E CD1 8542 N N . LYS E 153 ? 0.3601 0.4542 0.3726 -0.0368 -0.0223 -0.1424 152 LYS E N 8543 C CA . LYS E 153 ? 0.3721 0.4784 0.3932 -0.0464 -0.0264 -0.1626 152 LYS E CA 8544 C C . LYS E 153 ? 0.3877 0.5125 0.3947 -0.0385 -0.0308 -0.1763 152 LYS E C 8545 O O . LYS E 153 ? 0.3714 0.4903 0.3642 -0.0279 -0.0279 -0.1713 152 LYS E O 8546 C CB . LYS E 153 ? 0.3848 0.4638 0.4209 -0.0584 -0.0213 -0.1704 152 LYS E CB 8547 C CG . LYS E 153 ? 0.4014 0.4590 0.4319 -0.0531 -0.0172 -0.1764 152 LYS E CG 8548 C CD . LYS E 153 ? 0.4211 0.4473 0.4667 -0.0637 -0.0116 -0.1815 152 LYS E CD 8549 C CE . LYS E 153 ? 0.4385 0.4452 0.4798 -0.0573 -0.0080 -0.1911 152 LYS E CE 8550 N NZ . LYS E 153 ? 0.4541 0.4239 0.5078 -0.0633 -0.0013 -0.1897 152 LYS E NZ 8551 N N . LYS E 154 ? 0.4083 0.5587 0.4191 -0.0437 -0.0377 -0.1936 153 LYS E N 8552 C CA . LYS E 154 ? 0.4372 0.6091 0.4343 -0.0371 -0.0430 -0.2095 153 LYS E CA 8553 C C . LYS E 154 ? 0.4684 0.6412 0.4801 -0.0512 -0.0451 -0.2354 153 LYS E C 8554 O O . LYS E 154 ? 0.4657 0.6449 0.4960 -0.0647 -0.0471 -0.2420 153 LYS E O 8555 C CB . LYS E 154 ? 0.4419 0.6502 0.4280 -0.0277 -0.0511 -0.2060 153 LYS E CB 8556 C CG . LYS E 154 ? 0.4734 0.7073 0.4399 -0.0171 -0.0568 -0.2181 153 LYS E CG 8557 C CD . LYS E 154 ? 0.4818 0.7549 0.4420 -0.0096 -0.0667 -0.2179 153 LYS E CD 8558 C CE . LYS E 154 ? 0.5084 0.8098 0.4467 0.0021 -0.0730 -0.2294 153 LYS E CE 8559 N NZ . LYS E 154 ? 0.5188 0.8582 0.4483 0.0133 -0.0828 -0.2256 153 LYS E NZ 8560 N N . ASP E 155 ? 0.5050 0.6714 0.5091 -0.0486 -0.0438 -0.2507 154 ASP E N 8561 C CA . ASP E 155 ? 0.5460 0.7108 0.5631 -0.0618 -0.0454 -0.2784 154 ASP E CA 8562 C C . ASP E 155 ? 0.5427 0.6778 0.5842 -0.0790 -0.0396 -0.2777 154 ASP E C 8563 O O . ASP E 155 ? 0.5322 0.6774 0.5913 -0.0947 -0.0425 -0.2928 154 ASP E O 8564 C CB . ASP E 155 ? 0.5742 0.7830 0.5903 -0.0643 -0.0565 -0.2978 154 ASP E CB 8565 C CG . ASP E 155 ? 0.6062 0.8426 0.5956 -0.0470 -0.0619 -0.3015 154 ASP E CG 8566 O OD1 . ASP E 155 ? 0.6561 0.8789 0.6338 -0.0408 -0.0575 -0.3082 154 ASP E OD1 8567 O OD2 . ASP E 155 ? 0.6191 0.8913 0.5986 -0.0388 -0.0700 -0.2974 154 ASP E OD2 8568 N N . ASN E 156 ? 0.5350 0.6352 0.5773 -0.0758 -0.0311 -0.2591 155 ASN E N 8569 C CA . ASN E 156 ? 0.5403 0.6071 0.6014 -0.0888 -0.0239 -0.2532 155 ASN E CA 8570 C C . ASN E 156 ? 0.5189 0.5999 0.5954 -0.1020 -0.0256 -0.2485 155 ASN E C 8571 O O . ASN E 156 ? 0.5318 0.5967 0.6270 -0.1187 -0.0214 -0.2554 155 ASN E O 8572 C CB . ASN E 156 ? 0.5816 0.6217 0.6528 -0.0982 -0.0198 -0.2748 155 ASN E CB 8573 C CG . ASN E 156 ? 0.5953 0.6044 0.6576 -0.0857 -0.0133 -0.2694 155 ASN E CG 8574 O OD1 . ASN E 156 ? 0.5887 0.5766 0.6499 -0.0794 -0.0079 -0.2472 155 ASN E OD1 8575 N ND2 . ASN E 156 ? 0.6147 0.6236 0.6708 -0.0815 -0.0139 -0.2908 155 ASN E ND2 8576 N N . ALA E 157 ? 0.4806 0.5912 0.5495 -0.0942 -0.0309 -0.2365 156 ALA E N 8577 C CA . ALA E 157 ? 0.4598 0.5874 0.5426 -0.1040 -0.0322 -0.2307 156 ALA E CA 8578 C C . ALA E 157 ? 0.4255 0.5680 0.4968 -0.0905 -0.0342 -0.2088 156 ALA E C 8579 O O . ALA E 157 ? 0.4110 0.5655 0.4637 -0.0748 -0.0380 -0.2037 156 ALA E O 8580 C CB . ALA E 157 ? 0.4674 0.6309 0.5611 -0.1142 -0.0400 -0.2542 156 ALA E CB 8581 N N . TYR E 158 ? 0.4096 0.5493 0.4921 -0.0972 -0.0306 -0.1958 157 TYR E N 8582 C CA . TYR E 158 ? 0.3813 0.5342 0.4562 -0.0865 -0.0320 -0.1769 157 TYR E CA 8583 C C . TYR E 158 ? 0.3785 0.5588 0.4705 -0.0970 -0.0341 -0.1811 157 TYR E C 8584 O O . TYR E 158 ? 0.3837 0.5518 0.4892 -0.1087 -0.0275 -0.1745 157 TYR E O 8585 C CB . TYR E 158 ? 0.3657 0.4859 0.4367 -0.0831 -0.0240 -0.1561 157 TYR E CB 8586 C CG . TYR E 158 ? 0.3383 0.4662 0.3980 -0.0699 -0.0250 -0.1377 157 TYR E CG 8587 C CD1 . TYR E 158 ? 0.3260 0.4725 0.3926 -0.0717 -0.0258 -0.1312 157 TYR E CD1 8588 C CD2 . TYR E 158 ? 0.3304 0.4469 0.3735 -0.0562 -0.0242 -0.1276 157 TYR E CD2 8589 C CE1 . TYR E 158 ? 0.3084 0.4593 0.3648 -0.0593 -0.0263 -0.1159 157 TYR E CE1 8590 C CE2 . TYR E 158 ? 0.3139 0.4345 0.3477 -0.0457 -0.0243 -0.1122 157 TYR E CE2 8591 C CZ . TYR E 158 ? 0.3025 0.4390 0.3426 -0.0468 -0.0255 -0.1067 157 TYR E CZ 8592 O OH . TYR E 158 ? 0.2913 0.4289 0.3221 -0.0360 -0.0252 -0.0927 157 TYR E OH 8593 N N . PRO E 159 ? 0.3754 0.5948 0.4670 -0.0929 -0.0432 -0.1925 158 PRO E N 8594 C CA . PRO E 159 ? 0.3754 0.6244 0.4850 -0.1019 -0.0450 -0.1964 158 PRO E CA 8595 C C . PRO E 159 ? 0.3599 0.6096 0.4667 -0.0937 -0.0419 -0.1752 158 PRO E C 8596 O O . PRO E 159 ? 0.3501 0.5888 0.4385 -0.0775 -0.0421 -0.1602 158 PRO E O 8597 C CB . PRO E 159 ? 0.3789 0.6720 0.4858 -0.0949 -0.0568 -0.2128 158 PRO E CB 8598 C CG . PRO E 159 ? 0.3927 0.6744 0.4864 -0.0914 -0.0593 -0.2246 158 PRO E CG 8599 C CD . PRO E 159 ? 0.3905 0.6310 0.4686 -0.0827 -0.0517 -0.2057 158 PRO E CD 8600 N N . THR E 160 ? 0.3653 0.6273 0.4910 -0.1059 -0.0383 -0.1750 159 THR E N 8601 C CA . THR E 160 ? 0.3604 0.6257 0.4854 -0.0995 -0.0348 -0.1576 159 THR E CA 8602 C C . THR E 160 ? 0.3439 0.6389 0.4576 -0.0798 -0.0434 -0.1544 159 THR E C 8603 O O . THR E 160 ? 0.3601 0.6928 0.4807 -0.0782 -0.0514 -0.1677 159 THR E O 8604 C CB . THR E 160 ? 0.3677 0.6478 0.5163 -0.1170 -0.0291 -0.1606 159 THR E CB 8605 O OG1 . THR E 160 ? 0.3898 0.6370 0.5470 -0.1347 -0.0200 -0.1612 159 THR E OG1 8606 C CG2 . THR E 160 ? 0.3561 0.6410 0.5028 -0.1095 -0.0250 -0.1436 159 THR E CG2 8607 N N . ILE E 161 ? 0.3264 0.6036 0.4227 -0.0647 -0.0418 -0.1372 160 ILE E N 8608 C CA . ILE E 161 ? 0.3247 0.6210 0.4077 -0.0446 -0.0482 -0.1312 160 ILE E CA 8609 C C . ILE E 161 ? 0.3315 0.6518 0.4258 -0.0422 -0.0477 -0.1271 160 ILE E C 8610 O O . ILE E 161 ? 0.3281 0.6344 0.4288 -0.0491 -0.0399 -0.1185 160 ILE E O 8611 C CB . ILE E 161 ? 0.3177 0.5823 0.3790 -0.0313 -0.0453 -0.1150 160 ILE E CB 8612 C CG1 . ILE E 161 ? 0.3346 0.5859 0.3828 -0.0289 -0.0472 -0.1201 160 ILE E CG1 8613 C CG2 . ILE E 161 ? 0.3146 0.5914 0.3646 -0.0122 -0.0487 -0.1050 160 ILE E CG2 8614 C CD1 . ILE E 161 ? 0.3353 0.5522 0.3676 -0.0221 -0.0418 -0.1062 160 ILE E CD1 8615 N N . LYS E 162 ? 0.3358 0.6939 0.4320 -0.0313 -0.0561 -0.1336 161 LYS E N 8616 C CA . LYS E 162 ? 0.3435 0.7254 0.4464 -0.0222 -0.0565 -0.1286 161 LYS E CA 8617 C C . LYS E 162 ? 0.3563 0.7485 0.4408 0.0027 -0.0642 -0.1224 161 LYS E C 8618 O O . LYS E 162 ? 0.4036 0.8256 0.4867 0.0100 -0.0735 -0.1322 161 LYS E O 8619 C CB . LYS E 162 ? 0.3449 0.7698 0.4743 -0.0343 -0.0587 -0.1438 161 LYS E CB 8620 C CG . LYS E 162 ? 0.3512 0.7680 0.4983 -0.0607 -0.0529 -0.1545 161 LYS E CG 8621 C CD . LYS E 162 ? 0.3534 0.8026 0.5283 -0.0762 -0.0491 -0.1631 161 LYS E CD 8622 C CE . LYS E 162 ? 0.3714 0.8089 0.5632 -0.1031 -0.0430 -0.1743 161 LYS E CE 8623 N NZ . LYS E 162 ? 0.3750 0.8264 0.5912 -0.1221 -0.0334 -0.1757 161 LYS E NZ 8624 N N . ARG E 163 ? 0.3509 0.7173 0.4203 0.0156 -0.0601 -0.1063 162 ARG E N 8625 C CA . ARG E 163 ? 0.3614 0.7310 0.4129 0.0395 -0.0651 -0.0975 162 ARG E CA 8626 C C . ARG E 163 ? 0.3643 0.7363 0.4192 0.0499 -0.0618 -0.0892 162 ARG E C 8627 O O . ARG E 163 ? 0.3743 0.7295 0.4360 0.0403 -0.0538 -0.0850 162 ARG E O 8628 C CB . ARG E 163 ? 0.3681 0.6987 0.3962 0.0461 -0.0619 -0.0858 162 ARG E CB 8629 C CG . ARG E 163 ? 0.3835 0.7104 0.4039 0.0400 -0.0648 -0.0931 162 ARG E CG 8630 C CD . ARG E 163 ? 0.3946 0.7609 0.4140 0.0478 -0.0756 -0.1049 162 ARG E CD 8631 N NE . ARG E 163 ? 0.3994 0.7569 0.4034 0.0476 -0.0775 -0.1087 162 ARG E NE 8632 C CZ . ARG E 163 ? 0.4128 0.7537 0.3923 0.0626 -0.0769 -0.0968 162 ARG E CZ 8633 N NH1 . ARG E 163 ? 0.4160 0.7451 0.3839 0.0789 -0.0747 -0.0804 162 ARG E NH1 8634 N NH2 . ARG E 163 ? 0.4254 0.7612 0.3920 0.0613 -0.0778 -0.1015 162 ARG E NH2 8635 N N . SER E 164 ? 0.3719 0.7646 0.4208 0.0709 -0.0680 -0.0866 163 SER E N 8636 C CA . SER E 164 ? 0.3801 0.7736 0.4305 0.0843 -0.0652 -0.0793 163 SER E CA 8637 C C . SER E 164 ? 0.3883 0.7663 0.4162 0.1089 -0.0678 -0.0670 163 SER E C 8638 O O . SER E 164 ? 0.4292 0.8116 0.4434 0.1177 -0.0739 -0.0659 163 SER E O 8639 C CB . SER E 164 ? 0.3915 0.8342 0.4640 0.0858 -0.0695 -0.0906 163 SER E CB 8640 O OG . SER E 164 ? 0.4000 0.8545 0.4938 0.0612 -0.0652 -0.1009 163 SER E OG 8641 N N . TYR E 165 ? 0.3884 0.7461 0.4114 0.1196 -0.0624 -0.0576 164 TYR E N 8642 C CA . TYR E 165 ? 0.4159 0.7559 0.4189 0.1432 -0.0635 -0.0453 164 TYR E CA 8643 C C . TYR E 165 ? 0.4219 0.7665 0.4320 0.1563 -0.0608 -0.0436 164 TYR E C 8644 O O . TYR E 165 ? 0.4021 0.7330 0.4206 0.1459 -0.0534 -0.0448 164 TYR E O 8645 C CB . TYR E 165 ? 0.4306 0.7213 0.4141 0.1403 -0.0566 -0.0333 164 TYR E CB 8646 C CG . TYR E 165 ? 0.4695 0.7361 0.4340 0.1630 -0.0549 -0.0194 164 TYR E CG 8647 C CD1 . TYR E 165 ? 0.5019 0.7759 0.4496 0.1812 -0.0608 -0.0126 164 TYR E CD1 8648 C CD2 . TYR E 165 ? 0.4975 0.7343 0.4607 0.1666 -0.0472 -0.0134 164 TYR E CD2 8649 C CE1 . TYR E 165 ? 0.5396 0.7887 0.4694 0.2027 -0.0582 0.0018 164 TYR E CE1 8650 C CE2 . TYR E 165 ? 0.5336 0.7449 0.4806 0.1868 -0.0446 -0.0012 164 TYR E CE2 8651 C CZ . TYR E 165 ? 0.5587 0.7746 0.4889 0.2049 -0.0497 0.0074 164 TYR E CZ 8652 O OH . TYR E 165 ? 0.6053 0.7917 0.5185 0.2252 -0.0459 0.0214 164 TYR E OH 8653 N N . ASN E 166 ? 0.4391 0.8050 0.4456 0.1802 -0.0672 -0.0415 165 ASN E N 8654 C CA . ASN E 166 ? 0.4565 0.8291 0.4694 0.1967 -0.0654 -0.0407 165 ASN E CA 8655 C C . ASN E 166 ? 0.4746 0.8033 0.4645 0.2157 -0.0615 -0.0253 165 ASN E C 8656 O O . ASN E 166 ? 0.4825 0.8039 0.4543 0.2293 -0.0657 -0.0162 165 ASN E O 8657 C CB . ASN E 166 ? 0.4812 0.9092 0.5074 0.2116 -0.0753 -0.0492 165 ASN E CB 8658 C CG . ASN E 166 ? 0.5190 0.9579 0.5521 0.2329 -0.0740 -0.0488 165 ASN E CG 8659 O OD1 . ASN E 166 ? 0.5310 0.9328 0.5491 0.2490 -0.0692 -0.0379 165 ASN E OD1 8660 N ND2 . ASN E 166 ? 0.5492 1.0405 0.6063 0.2330 -0.0780 -0.0618 165 ASN E ND2 8661 N N . ASN E 167 ? 0.4756 0.7734 0.4654 0.2155 -0.0528 -0.0225 166 ASN E N 8662 C CA . ASN E 167 ? 0.4935 0.7464 0.4635 0.2318 -0.0477 -0.0091 166 ASN E CA 8663 C C . ASN E 167 ? 0.5126 0.7798 0.4793 0.2629 -0.0524 -0.0051 166 ASN E C 8664 O O . ASN E 167 ? 0.5124 0.7834 0.4885 0.2730 -0.0497 -0.0095 166 ASN E O 8665 C CB . ASN E 167 ? 0.4761 0.6911 0.4471 0.2214 -0.0373 -0.0094 166 ASN E CB 8666 C CG . ASN E 167 ? 0.4999 0.6677 0.4529 0.2372 -0.0313 0.0026 166 ASN E CG 8667 O OD1 . ASN E 167 ? 0.5307 0.6890 0.4679 0.2543 -0.0339 0.0141 166 ASN E OD1 8668 N ND2 . ASN E 167 ? 0.4905 0.6289 0.4455 0.2318 -0.0231 0.0000 166 ASN E ND2 8669 N N . THR E 168 ? 0.5397 0.8152 0.4919 0.2791 -0.0594 0.0034 167 THR E N 8670 C CA . THR E 168 ? 0.5797 0.8689 0.5258 0.3119 -0.0649 0.0096 167 THR E CA 8671 C C . THR E 168 ? 0.6240 0.8570 0.5484 0.3300 -0.0570 0.0264 167 THR E C 8672 O O . THR E 168 ? 0.6330 0.8667 0.5460 0.3593 -0.0607 0.0363 167 THR E O 8673 C CB . THR E 168 ? 0.5868 0.9143 0.5253 0.3235 -0.0770 0.0116 167 THR E CB 8674 O OG1 . THR E 168 ? 0.6084 0.9067 0.5249 0.3161 -0.0750 0.0227 167 THR E OG1 8675 C CG2 . THR E 168 ? 0.5563 0.9415 0.5190 0.3066 -0.0849 -0.0070 167 THR E CG2 8676 N N . ASN E 169 ? 0.6402 0.8250 0.5593 0.3126 -0.0461 0.0296 168 ASN E N 8677 C CA . ASN E 169 ? 0.6849 0.8130 0.5870 0.3250 -0.0367 0.0432 168 ASN E CA 8678 C C . ASN E 169 ? 0.6984 0.8138 0.6123 0.3319 -0.0311 0.0353 168 ASN E C 8679 O O . ASN E 169 ? 0.6834 0.8267 0.6176 0.3198 -0.0319 0.0197 168 ASN E O 8680 C CB . ASN E 169 ? 0.6892 0.7731 0.5809 0.3022 -0.0276 0.0493 168 ASN E CB 8681 C CG . ASN E 169 ? 0.6876 0.7836 0.5683 0.2928 -0.0318 0.0551 168 ASN E CG 8682 O OD1 . ASN E 169 ? 0.7298 0.8206 0.5907 0.3102 -0.0340 0.0693 168 ASN E OD1 8683 N ND2 . ASN E 169 ? 0.6504 0.7616 0.5426 0.2661 -0.0325 0.0445 168 ASN E ND2 8684 N N . GLN E 170 ? 0.7400 0.8104 0.6399 0.3506 -0.0244 0.0464 169 GLN E N 8685 C CA . GLN E 170 ? 0.7453 0.7980 0.6534 0.3615 -0.0186 0.0392 169 GLN E CA 8686 C C . GLN E 170 ? 0.7225 0.7426 0.6362 0.3353 -0.0088 0.0306 169 GLN E C 8687 O O . GLN E 170 ? 0.7359 0.7510 0.6604 0.3365 -0.0045 0.0188 169 GLN E O 8688 C CB . GLN E 170 ? 0.8113 0.8217 0.7012 0.3914 -0.0143 0.0547 169 GLN E CB 8689 C CG . GLN E 170 ? 0.8499 0.8829 0.7266 0.4195 -0.0234 0.0689 169 GLN E CG 8690 C CD . GLN E 170 ? 0.8518 0.9451 0.7448 0.4397 -0.0345 0.0584 169 GLN E CD 8691 O OE1 . GLN E 170 ? 0.8693 0.9915 0.7544 0.4627 -0.0440 0.0670 169 GLN E OE1 8692 N NE2 . GLN E 170 ? 0.8210 0.9362 0.7367 0.4317 -0.0331 0.0396 169 GLN E NE2 8693 N N . GLU E 171 ? 0.6980 0.6986 0.6045 0.3124 -0.0056 0.0358 170 GLU E N 8694 C CA . GLU E 171 ? 0.6685 0.6376 0.5788 0.2880 0.0031 0.0291 170 GLU E CA 8695 C C . GLU E 171 ? 0.6068 0.6106 0.5325 0.2620 -0.0002 0.0160 170 GLU E C 8696 O O . GLU E 171 ? 0.5722 0.6179 0.5037 0.2588 -0.0083 0.0142 170 GLU E O 8697 C CB . GLU E 171 ? 0.6953 0.6191 0.5887 0.2793 0.0102 0.0434 170 GLU E CB 8698 C CG . GLU E 171 ? 0.7533 0.6331 0.6291 0.3024 0.0162 0.0592 170 GLU E CG 8699 C CD . GLU E 171 ? 0.7743 0.6708 0.6349 0.3246 0.0094 0.0752 170 GLU E CD 8700 O OE1 . GLU E 171 ? 0.7500 0.6917 0.6141 0.3192 0.0000 0.0727 170 GLU E OE1 8701 O OE2 . GLU E 171 ? 0.8146 0.6786 0.6594 0.3478 0.0136 0.0901 170 GLU E OE2 8702 N N . ASP E 172 ? 0.5893 0.5744 0.5214 0.2439 0.0061 0.0067 171 ASP E N 8703 C CA . ASP E 172 ? 0.5468 0.5539 0.4899 0.2182 0.0047 -0.0028 171 ASP E CA 8704 C C . ASP E 172 ? 0.5222 0.5216 0.4579 0.2025 0.0042 0.0059 171 ASP E C 8705 O O . ASP E 172 ? 0.5432 0.5092 0.4652 0.2058 0.0084 0.0175 171 ASP E O 8706 C CB . ASP E 172 ? 0.5489 0.5356 0.4976 0.2053 0.0116 -0.0138 171 ASP E CB 8707 C CG . ASP E 172 ? 0.5574 0.5627 0.5161 0.2161 0.0119 -0.0264 171 ASP E CG 8708 O OD1 . ASP E 172 ? 0.5723 0.6098 0.5363 0.2320 0.0068 -0.0270 171 ASP E OD1 8709 O OD2 . ASP E 172 ? 0.5636 0.5535 0.5252 0.2088 0.0172 -0.0368 171 ASP E OD2 8710 N N . LEU E 173 ? 0.4758 0.5048 0.4204 0.1852 0.0000 0.0003 172 LEU E N 8711 C CA . LEU E 173 ? 0.4679 0.4948 0.4066 0.1721 -0.0011 0.0069 172 LEU E CA 8712 C C . LEU E 173 ? 0.4344 0.4639 0.3819 0.1478 0.0005 -0.0004 172 LEU E C 8713 O O . LEU E 173 ? 0.4072 0.4658 0.3668 0.1400 -0.0025 -0.0092 172 LEU E O 8714 C CB . LEU E 173 ? 0.4657 0.5298 0.4049 0.1792 -0.0099 0.0086 172 LEU E CB 8715 C CG . LEU E 173 ? 0.4717 0.5347 0.3998 0.1747 -0.0121 0.0170 172 LEU E CG 8716 C CD1 . LEU E 173 ? 0.5134 0.5420 0.4220 0.1885 -0.0074 0.0318 172 LEU E CD1 8717 C CD2 . LEU E 173 ? 0.4626 0.5693 0.3950 0.1803 -0.0218 0.0133 172 LEU E CD2 8718 N N . LEU E 174 ? 0.4320 0.4314 0.3734 0.1363 0.0060 0.0036 173 LEU E N 8719 C CA . LEU E 174 ? 0.4022 0.4039 0.3504 0.1150 0.0070 -0.0015 173 LEU E CA 8720 C C . LEU E 174 ? 0.3976 0.4177 0.3449 0.1082 0.0025 0.0018 173 LEU E C 8721 O O . LEU E 174 ? 0.4075 0.4172 0.3441 0.1122 0.0032 0.0105 173 LEU E O 8722 C CB . LEU E 174 ? 0.4132 0.3796 0.3574 0.1058 0.0144 0.0003 173 LEU E CB 8723 C CG . LEU E 174 ? 0.3883 0.3566 0.3389 0.0855 0.0153 -0.0039 173 LEU E CG 8724 C CD1 . LEU E 174 ? 0.3656 0.3546 0.3267 0.0780 0.0125 -0.0144 173 LEU E CD1 8725 C CD2 . LEU E 174 ? 0.4056 0.3423 0.3541 0.0777 0.0225 -0.0031 173 LEU E CD2 8726 N N . VAL E 175 ? 0.3799 0.4262 0.3380 0.0977 -0.0012 -0.0053 174 VAL E N 8727 C CA . VAL E 175 ? 0.3530 0.4181 0.3124 0.0909 -0.0057 -0.0050 174 VAL E CA 8728 C C . VAL E 175 ? 0.3328 0.3940 0.2982 0.0729 -0.0038 -0.0083 174 VAL E C 8729 O O . VAL E 175 ? 0.3154 0.3784 0.2881 0.0663 -0.0022 -0.0134 174 VAL E O 8730 C CB . VAL E 175 ? 0.3417 0.4426 0.3106 0.0943 -0.0118 -0.0111 174 VAL E CB 8731 C CG1 . VAL E 175 ? 0.3345 0.4532 0.3058 0.0857 -0.0163 -0.0132 174 VAL E CG1 8732 C CG2 . VAL E 175 ? 0.3653 0.4741 0.3299 0.1148 -0.0144 -0.0086 174 VAL E CG2 8733 N N . LEU E 176 ? 0.3304 0.3870 0.2917 0.0663 -0.0039 -0.0053 175 LEU E N 8734 C CA . LEU E 176 ? 0.3200 0.3713 0.2862 0.0515 -0.0021 -0.0073 175 LEU E CA 8735 C C . LEU E 176 ? 0.3050 0.3729 0.2747 0.0450 -0.0060 -0.0101 175 LEU E C 8736 O O . LEU E 176 ? 0.3176 0.3957 0.2824 0.0511 -0.0092 -0.0094 175 LEU E O 8737 C CB . LEU E 176 ? 0.3334 0.3600 0.2925 0.0491 0.0031 -0.0021 175 LEU E CB 8738 C CG . LEU E 176 ? 0.3560 0.3608 0.3099 0.0559 0.0080 0.0011 175 LEU E CG 8739 C CD1 . LEU E 176 ? 0.3819 0.3650 0.3299 0.0513 0.0140 0.0068 175 LEU E CD1 8740 C CD2 . LEU E 176 ? 0.3569 0.3601 0.3187 0.0516 0.0090 -0.0057 175 LEU E CD2 8741 N N . TRP E 177 ? 0.2802 0.3503 0.2580 0.0333 -0.0056 -0.0135 176 TRP E N 8742 C CA . TRP E 177 ? 0.2593 0.3397 0.2416 0.0257 -0.0081 -0.0170 176 TRP E CA 8743 C C . TRP E 177 ? 0.2432 0.3154 0.2311 0.0152 -0.0057 -0.0173 176 TRP E C 8744 O O . TRP E 177 ? 0.2502 0.3138 0.2385 0.0141 -0.0033 -0.0158 176 TRP E O 8745 C CB . TRP E 177 ? 0.2501 0.3544 0.2405 0.0253 -0.0120 -0.0225 176 TRP E CB 8746 C CG . TRP E 177 ? 0.2309 0.3433 0.2305 0.0202 -0.0105 -0.0244 176 TRP E CG 8747 C CD1 . TRP E 177 ? 0.2209 0.3374 0.2289 0.0087 -0.0093 -0.0264 176 TRP E CD1 8748 C CD2 . TRP E 177 ? 0.2258 0.3433 0.2262 0.0271 -0.0093 -0.0243 176 TRP E CD2 8749 N NE1 . TRP E 177 ? 0.2179 0.3430 0.2308 0.0076 -0.0070 -0.0265 176 TRP E NE1 8750 C CE2 . TRP E 177 ? 0.2172 0.3443 0.2260 0.0189 -0.0072 -0.0264 176 TRP E CE2 8751 C CE3 . TRP E 177 ? 0.2368 0.3501 0.2310 0.0401 -0.0092 -0.0225 176 TRP E CE3 8752 C CZ2 . TRP E 177 ? 0.2160 0.3519 0.2271 0.0231 -0.0051 -0.0279 176 TRP E CZ2 8753 C CZ3 . TRP E 177 ? 0.2315 0.3513 0.2291 0.0447 -0.0075 -0.0248 176 TRP E CZ3 8754 C CH2 . TRP E 177 ? 0.2223 0.3548 0.2282 0.0361 -0.0055 -0.0280 176 TRP E CH2 8755 N N . GLY E 178 ? 0.2378 0.3129 0.2298 0.0081 -0.0068 -0.0200 177 GLY E N 8756 C CA . GLY E 178 ? 0.2267 0.2933 0.2232 0.0003 -0.0048 -0.0191 177 GLY E CA 8757 C C . GLY E 178 ? 0.2181 0.2890 0.2213 -0.0069 -0.0058 -0.0225 177 GLY E C 8758 O O . GLY E 178 ? 0.2215 0.3040 0.2275 -0.0079 -0.0082 -0.0274 177 GLY E O 8759 N N . ILE E 179 ? 0.2101 0.2716 0.2163 -0.0119 -0.0040 -0.0202 178 ILE E N 8760 C CA . ILE E 179 ? 0.2128 0.2715 0.2251 -0.0189 -0.0036 -0.0222 178 ILE E CA 8761 C C . ILE E 179 ? 0.2172 0.2619 0.2283 -0.0182 -0.0024 -0.0205 178 ILE E C 8762 O O . ILE E 179 ? 0.2133 0.2537 0.2216 -0.0149 -0.0016 -0.0167 178 ILE E O 8763 C CB . ILE E 179 ? 0.2109 0.2727 0.2285 -0.0247 -0.0016 -0.0188 178 ILE E CB 8764 C CG1 . ILE E 179 ? 0.2212 0.2748 0.2450 -0.0325 0.0002 -0.0197 178 ILE E CG1 8765 C CG2 . ILE E 179 ? 0.2078 0.2650 0.2216 -0.0222 -0.0002 -0.0124 178 ILE E CG2 8766 C CD1 . ILE E 179 ? 0.2253 0.2840 0.2549 -0.0401 0.0034 -0.0166 178 ILE E CD1 8767 N N . HIS E 180 ? 0.2314 0.2703 0.2458 -0.0213 -0.0022 -0.0246 179 HIS E N 8768 C CA . HIS E 180 ? 0.2340 0.2609 0.2486 -0.0193 -0.0009 -0.0239 179 HIS E CA 8769 C C . HIS E 180 ? 0.2487 0.2651 0.2684 -0.0232 0.0007 -0.0201 179 HIS E C 8770 O O . HIS E 180 ? 0.2577 0.2715 0.2821 -0.0295 0.0016 -0.0229 179 HIS E O 8771 C CB . HIS E 180 ? 0.2365 0.2625 0.2496 -0.0180 -0.0012 -0.0319 179 HIS E CB 8772 C CG . HIS E 180 ? 0.2497 0.2649 0.2642 -0.0150 0.0006 -0.0328 179 HIS E CG 8773 N ND1 . HIS E 180 ? 0.2608 0.2671 0.2790 -0.0169 0.0013 -0.0395 179 HIS E ND1 8774 C CD2 . HIS E 180 ? 0.2520 0.2652 0.2658 -0.0101 0.0020 -0.0288 179 HIS E CD2 8775 C CE1 . HIS E 180 ? 0.2679 0.2668 0.2870 -0.0116 0.0031 -0.0391 179 HIS E CE1 8776 N NE2 . HIS E 180 ? 0.2580 0.2627 0.2751 -0.0076 0.0034 -0.0326 179 HIS E NE2 8777 N N . HIS E 181 ? 0.2519 0.2629 0.2707 -0.0193 0.0012 -0.0135 180 HIS E N 8778 C CA . HIS E 181 ? 0.2652 0.2643 0.2865 -0.0197 0.0028 -0.0077 180 HIS E CA 8779 C C . HIS E 181 ? 0.2795 0.2671 0.3033 -0.0152 0.0034 -0.0110 180 HIS E C 8780 O O . HIS E 181 ? 0.2623 0.2530 0.2856 -0.0085 0.0025 -0.0105 180 HIS E O 8781 C CB . HIS E 181 ? 0.2656 0.2691 0.2835 -0.0159 0.0020 0.0008 180 HIS E CB 8782 C CG . HIS E 181 ? 0.2661 0.2819 0.2810 -0.0189 0.0018 0.0024 180 HIS E CG 8783 N ND1 . HIS E 181 ? 0.2756 0.2930 0.2915 -0.0252 0.0042 0.0046 180 HIS E ND1 8784 C CD2 . HIS E 181 ? 0.2563 0.2832 0.2680 -0.0165 0.0002 0.0011 180 HIS E CD2 8785 C CE1 . HIS E 181 ? 0.2627 0.2936 0.2759 -0.0253 0.0037 0.0046 180 HIS E CE1 8786 N NE2 . HIS E 181 ? 0.2569 0.2920 0.2671 -0.0198 0.0012 0.0023 180 HIS E NE2 8787 N N . PRO E 182 ? 0.3036 0.2788 0.3313 -0.0190 0.0053 -0.0159 181 PRO E N 8788 C CA . PRO E 182 ? 0.3173 0.2808 0.3473 -0.0135 0.0062 -0.0206 181 PRO E CA 8789 C C . PRO E 182 ? 0.3306 0.2813 0.3618 -0.0061 0.0072 -0.0118 181 PRO E C 8790 O O . PRO E 182 ? 0.3317 0.2816 0.3606 -0.0061 0.0072 -0.0012 181 PRO E O 8791 C CB . PRO E 182 ? 0.3275 0.2809 0.3615 -0.0208 0.0079 -0.0301 181 PRO E CB 8792 C CG . PRO E 182 ? 0.3297 0.2838 0.3658 -0.0303 0.0091 -0.0255 181 PRO E CG 8793 C CD . PRO E 182 ? 0.3064 0.2792 0.3377 -0.0289 0.0068 -0.0194 181 PRO E CD 8794 N N . ASN E 183 ? 0.3384 0.2811 0.3724 0.0012 0.0080 -0.0162 182 ASN E N 8795 C CA . ASN E 183 ? 0.3515 0.2835 0.3870 0.0112 0.0083 -0.0083 182 ASN E CA 8796 C C . ASN E 183 ? 0.3736 0.2787 0.4106 0.0100 0.0118 -0.0037 182 ASN E C 8797 O O . ASN E 183 ? 0.3894 0.2854 0.4245 0.0172 0.0120 0.0081 182 ASN E O 8798 C CB . ASN E 183 ? 0.3519 0.2883 0.3912 0.0212 0.0081 -0.0153 182 ASN E CB 8799 C CG . ASN E 183 ? 0.3371 0.2984 0.3759 0.0222 0.0062 -0.0175 182 ASN E CG 8800 O OD1 . ASN E 183 ? 0.3213 0.2946 0.3585 0.0221 0.0037 -0.0104 182 ASN E OD1 8801 N ND2 . ASN E 183 ? 0.3381 0.3068 0.3777 0.0227 0.0078 -0.0276 182 ASN E ND2 8802 N N . ASP E 184 ? 0.3853 0.2776 0.4254 0.0010 0.0146 -0.0129 183 ASP E N 8803 C CA . ASP E 184 ? 0.4244 0.2867 0.4674 -0.0020 0.0195 -0.0098 183 ASP E CA 8804 C C . ASP E 184 ? 0.4283 0.2827 0.4765 -0.0167 0.0223 -0.0219 183 ASP E C 8805 O O . ASP E 184 ? 0.4283 0.3015 0.4771 -0.0223 0.0196 -0.0338 183 ASP E O 8806 C CB . ASP E 184 ? 0.4434 0.2863 0.4889 0.0114 0.0210 -0.0104 183 ASP E CB 8807 C CG . ASP E 184 ? 0.4409 0.2935 0.4894 0.0164 0.0195 -0.0265 183 ASP E CG 8808 O OD1 . ASP E 184 ? 0.4341 0.2887 0.4843 0.0074 0.0201 -0.0406 183 ASP E OD1 8809 O OD2 . ASP E 184 ? 0.4607 0.3212 0.5097 0.0299 0.0179 -0.0253 183 ASP E OD2 8810 N N . ALA E 185 ? 0.4572 0.2840 0.5092 -0.0228 0.0278 -0.0187 184 ALA E N 8811 C CA . ALA E 185 ? 0.4641 0.2829 0.5237 -0.0390 0.0311 -0.0307 184 ALA E CA 8812 C C . ALA E 185 ? 0.4602 0.2837 0.5236 -0.0397 0.0287 -0.0522 184 ALA E C 8813 O O . ALA E 185 ? 0.4538 0.2914 0.5213 -0.0516 0.0273 -0.0652 184 ALA E O 8814 C CB . ALA E 185 ? 0.5037 0.2856 0.5675 -0.0443 0.0389 -0.0236 184 ALA E CB 8815 N N . ALA E 186 ? 0.4626 0.2761 0.5246 -0.0264 0.0284 -0.0564 185 ALA E N 8816 C CA . ALA E 186 ? 0.4594 0.2781 0.5229 -0.0249 0.0269 -0.0767 185 ALA E CA 8817 C C . ALA E 186 ? 0.4257 0.2813 0.4833 -0.0245 0.0212 -0.0820 185 ALA E C 8818 O O . ALA E 186 ? 0.4200 0.2885 0.4781 -0.0316 0.0191 -0.0974 185 ALA E O 8819 C CB . ALA E 186 ? 0.4738 0.2770 0.5370 -0.0088 0.0284 -0.0784 185 ALA E CB 8820 N N . GLU E 187 ? 0.4022 0.2745 0.4541 -0.0159 0.0187 -0.0695 186 GLU E N 8821 C CA . GLU E 187 ? 0.3804 0.2833 0.4262 -0.0155 0.0145 -0.0721 186 GLU E CA 8822 C C . GLU E 187 ? 0.3704 0.2865 0.4169 -0.0285 0.0125 -0.0758 186 GLU E C 8823 O O . GLU E 187 ? 0.3603 0.2947 0.4034 -0.0304 0.0096 -0.0865 186 GLU E O 8824 C CB . GLU E 187 ? 0.3608 0.2766 0.4024 -0.0075 0.0129 -0.0574 186 GLU E CB 8825 C CG . GLU E 187 ? 0.3543 0.2932 0.3903 -0.0022 0.0110 -0.0611 186 GLU E CG 8826 C CD . GLU E 187 ? 0.3430 0.2952 0.3766 0.0018 0.0096 -0.0485 186 GLU E CD 8827 O OE1 . GLU E 187 ? 0.3376 0.2978 0.3689 -0.0038 0.0078 -0.0423 186 GLU E OE1 8828 O OE2 . GLU E 187 ? 0.3558 0.3119 0.3909 0.0107 0.0103 -0.0459 186 GLU E OE2 8829 N N . GLN E 188 ? 0.3796 0.2874 0.4304 -0.0367 0.0143 -0.0669 187 GLN E N 8830 C CA . GLN E 188 ? 0.3784 0.3021 0.4318 -0.0484 0.0128 -0.0688 187 GLN E CA 8831 C C . GLN E 188 ? 0.3985 0.3274 0.4573 -0.0576 0.0116 -0.0879 187 GLN E C 8832 O O . GLN E 188 ? 0.3962 0.3508 0.4532 -0.0602 0.0071 -0.0947 187 GLN E O 8833 C CB . GLN E 188 ? 0.3841 0.2951 0.4422 -0.0562 0.0171 -0.0563 187 GLN E CB 8834 C CG . GLN E 188 ? 0.3753 0.3029 0.4392 -0.0693 0.0171 -0.0588 187 GLN E CG 8835 C CD . GLN E 188 ? 0.3496 0.3076 0.4077 -0.0654 0.0121 -0.0563 187 GLN E CD 8836 O OE1 . GLN E 188 ? 0.3173 0.2804 0.3669 -0.0546 0.0100 -0.0479 187 GLN E OE1 8837 N NE2 . GLN E 188 ? 0.3377 0.3162 0.4014 -0.0742 0.0102 -0.0640 187 GLN E NE2 8838 N N . THR E 189 ? 0.4211 0.3260 0.4865 -0.0617 0.0152 -0.0972 188 THR E N 8839 C CA . THR E 189 ? 0.4410 0.3503 0.5126 -0.0715 0.0139 -0.1180 188 THR E CA 8840 C C . THR E 189 ? 0.4342 0.3574 0.4974 -0.0619 0.0098 -0.1313 188 THR E C 8841 O O . THR E 189 ? 0.4305 0.3737 0.4936 -0.0668 0.0056 -0.1471 188 THR E O 8842 C CB . THR E 189 ? 0.4814 0.3570 0.5639 -0.0810 0.0201 -0.1252 188 THR E CB 8843 O OG1 . THR E 189 ? 0.4914 0.3402 0.5705 -0.0687 0.0234 -0.1219 188 THR E OG1 8844 C CG2 . THR E 189 ? 0.4950 0.3587 0.5852 -0.0926 0.0255 -0.1115 188 THR E CG2 8845 N N . ARG E 190 ? 0.4329 0.3483 0.4889 -0.0480 0.0111 -0.1253 189 ARG E N 8846 C CA . ARG E 190 ? 0.4411 0.3723 0.4879 -0.0385 0.0085 -0.1358 189 ARG E CA 8847 C C . ARG E 190 ? 0.4173 0.3814 0.4552 -0.0374 0.0034 -0.1331 189 ARG E C 8848 O O . ARG E 190 ? 0.4263 0.4090 0.4583 -0.0370 0.0000 -0.1467 189 ARG E O 8849 C CB . ARG E 190 ? 0.4549 0.3763 0.4975 -0.0242 0.0116 -0.1283 189 ARG E CB 8850 C CG . ARG E 190 ? 0.4670 0.4051 0.5003 -0.0151 0.0109 -0.1393 189 ARG E CG 8851 C CD . ARG E 190 ? 0.4923 0.4184 0.5260 -0.0024 0.0152 -0.1378 189 ARG E CD 8852 N NE . ARG E 190 ? 0.4913 0.4153 0.5267 0.0034 0.0161 -0.1183 189 ARG E NE 8853 C CZ . ARG E 190 ? 0.4909 0.4355 0.5204 0.0079 0.0152 -0.1081 189 ARG E CZ 8854 N NH1 . ARG E 190 ? 0.4827 0.4496 0.5027 0.0081 0.0141 -0.1132 189 ARG E NH1 8855 N NH2 . ARG E 190 ? 0.4766 0.4191 0.5093 0.0121 0.0156 -0.0928 189 ARG E NH2 8856 N N . LEU E 191 ? 0.3850 0.3559 0.4213 -0.0363 0.0028 -0.1161 190 LEU E N 8857 C CA . LEU E 191 ? 0.3707 0.3683 0.3983 -0.0334 -0.0013 -0.1121 190 LEU E CA 8858 C C . LEU E 191 ? 0.3683 0.3829 0.4005 -0.0431 -0.0053 -0.1174 190 LEU E C 8859 O O . LEU E 191 ? 0.3529 0.3909 0.3778 -0.0402 -0.0099 -0.1228 190 LEU E O 8860 C CB . LEU E 191 ? 0.3473 0.3459 0.3712 -0.0275 -0.0001 -0.0936 190 LEU E CB 8861 C CG . LEU E 191 ? 0.3453 0.3334 0.3668 -0.0181 0.0033 -0.0859 190 LEU E CG 8862 C CD1 . LEU E 191 ? 0.3199 0.3207 0.3347 -0.0129 0.0028 -0.0738 190 LEU E CD1 8863 C CD2 . LEU E 191 ? 0.3595 0.3462 0.3774 -0.0119 0.0050 -0.0975 190 LEU E CD2 8864 N N . TYR E 192 ? 0.3735 0.3778 0.4176 -0.0538 -0.0033 -0.1153 191 TYR E N 8865 C CA . TYR E 192 ? 0.3738 0.3978 0.4246 -0.0629 -0.0063 -0.1178 191 TYR E CA 8866 C C . TYR E 192 ? 0.4043 0.4227 0.4700 -0.0784 -0.0048 -0.1312 191 TYR E C 8867 O O . TYR E 192 ? 0.4039 0.4405 0.4781 -0.0875 -0.0065 -0.1341 191 TYR E O 8868 C CB . TYR E 192 ? 0.3572 0.3819 0.4087 -0.0625 -0.0044 -0.1000 191 TYR E CB 8869 C CG . TYR E 192 ? 0.3331 0.3584 0.3727 -0.0497 -0.0047 -0.0868 191 TYR E CG 8870 C CD1 . TYR E 192 ? 0.3222 0.3676 0.3521 -0.0416 -0.0087 -0.0866 191 TYR E CD1 8871 C CD2 . TYR E 192 ? 0.3318 0.3378 0.3705 -0.0457 -0.0007 -0.0747 191 TYR E CD2 8872 C CE1 . TYR E 192 ? 0.3109 0.3547 0.3315 -0.0320 -0.0078 -0.0752 191 TYR E CE1 8873 C CE2 . TYR E 192 ? 0.3205 0.3293 0.3507 -0.0359 -0.0010 -0.0648 191 TYR E CE2 8874 C CZ . TYR E 192 ? 0.3115 0.3381 0.3333 -0.0301 -0.0040 -0.0655 191 TYR E CZ 8875 O OH . TYR E 192 ? 0.3132 0.3408 0.3279 -0.0224 -0.0032 -0.0563 191 TYR E OH 8876 N N . GLN E 193 ? 0.4331 0.4262 0.5028 -0.0814 -0.0010 -0.1395 192 GLN E N 8877 C CA . GLN E 193 ? 0.4644 0.4457 0.5487 -0.0971 0.0016 -0.1540 192 GLN E CA 8878 C C . GLN E 193 ? 0.4693 0.4363 0.5660 -0.1099 0.0080 -0.1432 192 GLN E C 8879 O O . GLN E 193 ? 0.5037 0.4389 0.6080 -0.1172 0.0148 -0.1432 192 GLN E O 8880 C CB . GLN E 193 ? 0.4807 0.4928 0.5692 -0.1040 -0.0050 -0.1752 192 GLN E CB 8881 C CG . GLN E 193 ? 0.5153 0.5138 0.6174 -0.1185 -0.0027 -0.1967 192 GLN E CG 8882 C CD . GLN E 193 ? 0.5418 0.5107 0.6382 -0.1114 0.0003 -0.2042 192 GLN E CD 8883 O OE1 . GLN E 193 ? 0.5277 0.5026 0.6092 -0.0959 -0.0022 -0.2030 192 GLN E OE1 8884 N NE2 . GLN E 193 ? 0.5769 0.5133 0.6857 -0.1226 0.0069 -0.2118 192 GLN E NE2 8885 N N . ASN E 194 ? 0.4507 0.4411 0.5492 -0.1125 0.0064 -0.1344 193 ASN E N 8886 C CA . ASN E 194 ? 0.4559 0.4386 0.5651 -0.1247 0.0131 -0.1238 193 ASN E CA 8887 C C . ASN E 194 ? 0.4532 0.4102 0.5540 -0.1164 0.0186 -0.1016 193 ASN E C 8888 O O . ASN E 194 ? 0.4372 0.4011 0.5255 -0.1020 0.0152 -0.0915 193 ASN E O 8889 C CB . ASN E 194 ? 0.4359 0.4559 0.5491 -0.1279 0.0095 -0.1225 193 ASN E CB 8890 C CG . ASN E 194 ? 0.4222 0.4745 0.5406 -0.1311 0.0016 -0.1432 193 ASN E CG 8891 O OD1 . ASN E 194 ? 0.4506 0.5001 0.5806 -0.1437 0.0022 -0.1607 193 ASN E OD1 8892 N ND2 . ASN E 194 ? 0.3958 0.4782 0.5051 -0.1191 -0.0057 -0.1416 193 ASN E ND2 8893 N N . PRO E 195 ? 0.4833 0.4103 0.5908 -0.1253 0.0272 -0.0942 194 PRO E N 8894 C CA . PRO E 195 ? 0.4843 0.3885 0.5826 -0.1161 0.0318 -0.0725 194 PRO E CA 8895 C C . PRO E 195 ? 0.4758 0.3979 0.5700 -0.1152 0.0329 -0.0559 194 PRO E C 8896 O O . PRO E 195 ? 0.4895 0.4070 0.5722 -0.1027 0.0323 -0.0411 194 PRO E O 8897 C CB . PRO E 195 ? 0.5153 0.3811 0.6216 -0.1262 0.0412 -0.0704 194 PRO E CB 8898 C CG . PRO E 195 ? 0.5222 0.3959 0.6449 -0.1459 0.0431 -0.0881 194 PRO E CG 8899 C CD . PRO E 195 ? 0.4999 0.4089 0.6225 -0.1429 0.0330 -0.1067 194 PRO E CD 8900 N N . THR E 196 ? 0.4784 0.4227 0.5826 -0.1281 0.0344 -0.0597 195 THR E N 8901 C CA . THR E 196 ? 0.4724 0.4349 0.5737 -0.1280 0.0365 -0.0459 195 THR E CA 8902 C C . THR E 196 ? 0.4369 0.4393 0.5397 -0.1252 0.0290 -0.0550 195 THR E C 8903 O O . THR E 196 ? 0.4494 0.4724 0.5653 -0.1364 0.0279 -0.0688 195 THR E O 8904 C CB . THR E 196 ? 0.5066 0.4632 0.6197 -0.1459 0.0468 -0.0406 195 THR E CB 8905 O OG1 . THR E 196 ? 0.5446 0.4604 0.6556 -0.1483 0.0548 -0.0304 195 THR E OG1 8906 C CG2 . THR E 196 ? 0.4986 0.4767 0.6075 -0.1447 0.0495 -0.0270 195 THR E CG2 8907 N N . THR E 197 ? 0.3953 0.4090 0.4854 -0.1104 0.0240 -0.0475 196 THR E N 8908 C CA . THR E 197 ? 0.3666 0.4125 0.4556 -0.1043 0.0167 -0.0553 196 THR E CA 8909 C C . THR E 197 ? 0.3508 0.4130 0.4337 -0.0975 0.0169 -0.0442 196 THR E C 8910 O O . THR E 197 ? 0.3469 0.3964 0.4236 -0.0954 0.0215 -0.0306 196 THR E O 8911 C CB . THR E 197 ? 0.3519 0.3968 0.4309 -0.0916 0.0094 -0.0617 196 THR E CB 8912 O OG1 . THR E 197 ? 0.3393 0.3717 0.4056 -0.0794 0.0093 -0.0493 196 THR E OG1 8913 C CG2 . THR E 197 ? 0.3710 0.3983 0.4540 -0.0964 0.0095 -0.0737 196 THR E CG2 8914 N N . TYR E 198 ? 0.3314 0.4225 0.4157 -0.0930 0.0115 -0.0509 197 TYR E N 8915 C CA . TYR E 198 ? 0.3192 0.4275 0.3991 -0.0861 0.0115 -0.0436 197 TYR E CA 8916 C C . TYR E 198 ? 0.2977 0.4261 0.3728 -0.0741 0.0038 -0.0500 197 TYR E C 8917 O O . TYR E 198 ? 0.2960 0.4306 0.3722 -0.0727 -0.0014 -0.0602 197 TYR E O 8918 C CB . TYR E 198 ? 0.3338 0.4611 0.4268 -0.0979 0.0173 -0.0438 197 TYR E CB 8919 C CG . TYR E 198 ? 0.3371 0.4912 0.4451 -0.1052 0.0139 -0.0592 197 TYR E CG 8920 C CD1 . TYR E 198 ? 0.3550 0.5027 0.4754 -0.1199 0.0159 -0.0690 197 TYR E CD1 8921 C CD2 . TYR E 198 ? 0.3231 0.5089 0.4327 -0.0965 0.0081 -0.0650 197 TYR E CD2 8922 C CE1 . TYR E 198 ? 0.3495 0.5253 0.4844 -0.1269 0.0117 -0.0852 197 TYR E CE1 8923 C CE2 . TYR E 198 ? 0.3233 0.5378 0.4467 -0.1016 0.0037 -0.0796 197 TYR E CE2 8924 C CZ . TYR E 198 ? 0.3354 0.5465 0.4717 -0.1174 0.0051 -0.0903 197 TYR E CZ 8925 O OH . TYR E 198 ? 0.3374 0.5810 0.4884 -0.1231 0.0000 -0.1070 197 TYR E OH 8926 N N . ILE E 199 ? 0.2891 0.4268 0.3579 -0.0648 0.0034 -0.0435 198 ILE E N 8927 C CA . ILE E 199 ? 0.2821 0.4381 0.3465 -0.0527 -0.0024 -0.0474 198 ILE E CA 8928 C C . ILE E 199 ? 0.2799 0.4566 0.3492 -0.0514 0.0002 -0.0451 198 ILE E C 8929 O O . ILE E 199 ? 0.2547 0.4229 0.3185 -0.0498 0.0045 -0.0366 198 ILE E O 8930 C CB . ILE E 199 ? 0.2822 0.4210 0.3314 -0.0401 -0.0048 -0.0415 198 ILE E CB 8931 C CG1 . ILE E 199 ? 0.2898 0.4091 0.3346 -0.0414 -0.0060 -0.0433 198 ILE E CG1 8932 C CG2 . ILE E 199 ? 0.2851 0.4386 0.3287 -0.0271 -0.0097 -0.0437 198 ILE E CG2 8933 C CD1 . ILE E 199 ? 0.2923 0.3942 0.3248 -0.0323 -0.0062 -0.0366 198 ILE E CD1 8934 N N . SER E 200 ? 0.2875 0.4936 0.3680 -0.0523 -0.0021 -0.0536 199 SER E N 8935 C CA . SER E 200 ? 0.2852 0.5157 0.3709 -0.0480 -0.0002 -0.0533 199 SER E CA 8936 C C . SER E 200 ? 0.2723 0.5091 0.3487 -0.0297 -0.0063 -0.0538 199 SER E C 8937 O O . SER E 200 ? 0.2955 0.5369 0.3694 -0.0236 -0.0128 -0.0588 199 SER E O 8938 C CB . SER E 200 ? 0.3001 0.5635 0.4053 -0.0579 0.0003 -0.0631 199 SER E CB 8939 O OG . SER E 200 ? 0.3356 0.5903 0.4508 -0.0763 0.0047 -0.0656 199 SER E OG 8940 N N . VAL E 201 ? 0.2633 0.5000 0.3338 -0.0204 -0.0040 -0.0487 200 VAL E N 8941 C CA . VAL E 201 ? 0.2533 0.4972 0.3172 -0.0026 -0.0085 -0.0496 200 VAL E CA 8942 C C . VAL E 201 ? 0.2491 0.5154 0.3196 0.0027 -0.0051 -0.0510 200 VAL E C 8943 O O . VAL E 201 ? 0.2478 0.5081 0.3165 -0.0013 0.0010 -0.0470 200 VAL E O 8944 C CB . VAL E 201 ? 0.2508 0.4635 0.2978 0.0062 -0.0088 -0.0426 200 VAL E CB 8945 C CG1 . VAL E 201 ? 0.2546 0.4697 0.2942 0.0240 -0.0131 -0.0427 200 VAL E CG1 8946 C CG2 . VAL E 201 ? 0.2573 0.4478 0.2987 -0.0008 -0.0099 -0.0405 200 VAL E CG2 8947 N N . GLY E 202 ? 0.2413 0.5355 0.3190 0.0128 -0.0093 -0.0571 201 GLY E N 8948 C CA . GLY E 202 ? 0.2355 0.5530 0.3200 0.0205 -0.0062 -0.0596 201 GLY E CA 8949 C C . GLY E 202 ? 0.2357 0.5575 0.3139 0.0427 -0.0116 -0.0605 201 GLY E C 8950 O O . GLY E 202 ? 0.2444 0.5662 0.3183 0.0503 -0.0186 -0.0611 201 GLY E O 8951 N N . THR E 203 ? 0.2282 0.5522 0.3044 0.0537 -0.0081 -0.0604 202 THR E N 8952 C CA . THR E 203 ? 0.2440 0.5766 0.3176 0.0760 -0.0119 -0.0621 202 THR E CA 8953 C C . THR E 203 ? 0.2481 0.6139 0.3353 0.0798 -0.0073 -0.0686 202 THR E C 8954 O O . THR E 203 ? 0.2364 0.6288 0.3385 0.0648 -0.0038 -0.0726 202 THR E O 8955 C CB . THR E 203 ? 0.2562 0.5489 0.3112 0.0881 -0.0111 -0.0559 202 THR E CB 8956 O OG1 . THR E 203 ? 0.2608 0.5412 0.3129 0.0834 -0.0040 -0.0562 202 THR E OG1 8957 C CG2 . THR E 203 ? 0.2517 0.5139 0.2946 0.0819 -0.0136 -0.0494 202 THR E CG2 8958 N N . SER E 204 ? 0.2618 0.6261 0.3446 0.0989 -0.0064 -0.0699 203 SER E N 8959 C CA . SER E 204 ? 0.2667 0.6615 0.3613 0.1029 -0.0008 -0.0767 203 SER E CA 8960 C C . SER E 204 ? 0.2701 0.6497 0.3586 0.0921 0.0080 -0.0755 203 SER E C 8961 O O . SER E 204 ? 0.2665 0.6739 0.3651 0.0876 0.0145 -0.0801 203 SER E O 8962 C CB . SER E 204 ? 0.2858 0.6878 0.3793 0.1298 -0.0033 -0.0800 203 SER E CB 8963 O OG . SER E 204 ? 0.3037 0.6618 0.3786 0.1409 -0.0028 -0.0753 203 SER E OG 8964 N N . THR E 205 ? 0.2782 0.6165 0.3502 0.0880 0.0083 -0.0696 204 THR E N 8965 C CA . THR E 205 ? 0.2882 0.6104 0.3517 0.0789 0.0151 -0.0684 204 THR E CA 8966 C C . THR E 205 ? 0.2783 0.5823 0.3371 0.0591 0.0156 -0.0613 204 THR E C 8967 O O . THR E 205 ? 0.2876 0.5924 0.3440 0.0479 0.0214 -0.0593 204 THR E O 8968 C CB . THR E 205 ? 0.2997 0.5894 0.3483 0.0921 0.0153 -0.0697 204 THR E CB 8969 O OG1 . THR E 205 ? 0.3100 0.5713 0.3507 0.0982 0.0094 -0.0647 204 THR E OG1 8970 C CG2 . THR E 205 ? 0.3162 0.6217 0.3685 0.1110 0.0175 -0.0779 204 THR E CG2 8971 N N . LEU E 206 ? 0.2698 0.5583 0.3264 0.0559 0.0098 -0.0571 205 LEU E N 8972 C CA . LEU E 206 ? 0.2590 0.5280 0.3112 0.0398 0.0099 -0.0509 205 LEU E CA 8973 C C . LEU E 206 ? 0.2482 0.5394 0.3141 0.0245 0.0114 -0.0510 205 LEU E C 8974 O O . LEU E 206 ? 0.2491 0.5624 0.3262 0.0261 0.0078 -0.0554 205 LEU E O 8975 C CB . LEU E 206 ? 0.2614 0.5032 0.3046 0.0442 0.0039 -0.0474 205 LEU E CB 8976 C CG . LEU E 206 ? 0.2584 0.4768 0.2959 0.0311 0.0035 -0.0416 205 LEU E CG 8977 C CD1 . LEU E 206 ? 0.2603 0.4571 0.2874 0.0284 0.0069 -0.0388 205 LEU E CD1 8978 C CD2 . LEU E 206 ? 0.2549 0.4579 0.2868 0.0363 -0.0021 -0.0397 205 LEU E CD2 8979 N N . ASN E 207 ? 0.2522 0.5376 0.3171 0.0097 0.0169 -0.0462 206 ASN E N 8980 C CA . ASN E 207 ? 0.2545 0.5517 0.3312 -0.0074 0.0199 -0.0449 206 ASN E CA 8981 C C . ASN E 207 ? 0.2696 0.5352 0.3361 -0.0175 0.0210 -0.0366 206 ASN E C 8982 O O . ASN E 207 ? 0.2615 0.5203 0.3214 -0.0229 0.0268 -0.0305 206 ASN E O 8983 C CB . ASN E 207 ? 0.2558 0.5826 0.3426 -0.0139 0.0285 -0.0461 206 ASN E CB 8984 C CG . ASN E 207 ? 0.2492 0.5840 0.3481 -0.0340 0.0341 -0.0434 206 ASN E CG 8985 O OD1 . ASN E 207 ? 0.2571 0.5887 0.3637 -0.0415 0.0300 -0.0460 206 ASN E OD1 8986 N ND2 . ASN E 207 ? 0.2537 0.5987 0.3539 -0.0430 0.0440 -0.0386 206 ASN E ND2 8987 N N . GLN E 208 ? 0.2858 0.5335 0.3500 -0.0182 0.0151 -0.0364 207 GLN E N 8988 C CA . GLN E 208 ? 0.2960 0.5136 0.3506 -0.0240 0.0149 -0.0297 207 GLN E CA 8989 C C . GLN E 208 ? 0.2987 0.5125 0.3620 -0.0373 0.0149 -0.0299 207 GLN E C 8990 O O . GLN E 208 ? 0.2796 0.5063 0.3519 -0.0380 0.0109 -0.0371 207 GLN E O 8991 C CB . GLN E 208 ? 0.3001 0.4975 0.3438 -0.0126 0.0089 -0.0299 207 GLN E CB 8992 C CG . GLN E 208 ? 0.3263 0.4971 0.3633 -0.0178 0.0076 -0.0250 207 GLN E CG 8993 C CD . GLN E 208 ? 0.3300 0.4826 0.3568 -0.0079 0.0036 -0.0247 207 GLN E CD 8994 O OE1 . GLN E 208 ? 0.3260 0.4715 0.3517 -0.0059 0.0000 -0.0261 207 GLN E OE1 8995 N NE2 . GLN E 208 ? 0.3390 0.4846 0.3582 -0.0023 0.0050 -0.0236 207 GLN E NE2 8996 N N . ARG E 209 ? 0.3274 0.5235 0.3874 -0.0470 0.0194 -0.0226 208 ARG E N 8997 C CA . ARG E 209 ? 0.3565 0.5399 0.4226 -0.0586 0.0199 -0.0225 208 ARG E CA 8998 C C . ARG E 209 ? 0.3717 0.5243 0.4262 -0.0581 0.0199 -0.0144 208 ARG E C 8999 O O . ARG E 209 ? 0.4043 0.5488 0.4529 -0.0607 0.0250 -0.0054 208 ARG E O 9000 C CB . ARG E 209 ? 0.3871 0.5825 0.4657 -0.0737 0.0277 -0.0215 208 ARG E CB 9001 C CG . ARG E 209 ? 0.4192 0.5972 0.5048 -0.0869 0.0295 -0.0220 208 ARG E CG 9002 C CD . ARG E 209 ? 0.4422 0.6438 0.5473 -0.0988 0.0306 -0.0328 208 ARG E CD 9003 N NE . ARG E 209 ? 0.4666 0.6496 0.5796 -0.1137 0.0340 -0.0344 208 ARG E NE 9004 C CZ . ARG E 209 ? 0.4861 0.6836 0.6164 -0.1259 0.0337 -0.0467 208 ARG E CZ 9005 N NH1 . ARG E 209 ? 0.4756 0.7101 0.6175 -0.1241 0.0293 -0.0579 208 ARG E NH1 9006 N NH2 . ARG E 209 ? 0.5156 0.6910 0.6524 -0.1396 0.0375 -0.0486 208 ARG E NH2 9007 N N . LEU E 210 ? 0.3772 0.5151 0.4283 -0.0539 0.0142 -0.0176 209 LEU E N 9008 C CA . LEU E 210 ? 0.3791 0.4912 0.4209 -0.0515 0.0134 -0.0115 209 LEU E CA 9009 C C . LEU E 210 ? 0.3899 0.4859 0.4371 -0.0610 0.0154 -0.0114 209 LEU E C 9010 O O . LEU E 210 ? 0.3992 0.5002 0.4550 -0.0660 0.0136 -0.0201 209 LEU E O 9011 C CB . LEU E 210 ? 0.3644 0.4705 0.3993 -0.0410 0.0073 -0.0152 209 LEU E CB 9012 C CG . LEU E 210 ? 0.3549 0.4708 0.3841 -0.0309 0.0055 -0.0161 209 LEU E CG 9013 C CD1 . LEU E 210 ? 0.3516 0.4597 0.3752 -0.0225 0.0009 -0.0190 209 LEU E CD1 9014 C CD2 . LEU E 210 ? 0.3678 0.4789 0.3896 -0.0288 0.0081 -0.0098 209 LEU E CD2 9015 N N . VAL E 211 ? 0.4038 0.4807 0.4458 -0.0625 0.0189 -0.0019 210 VAL E N 9016 C CA . VAL E 211 ? 0.4146 0.4698 0.4601 -0.0686 0.0209 -0.0010 210 VAL E CA 9017 C C . VAL E 211 ? 0.4049 0.4421 0.4412 -0.0588 0.0175 0.0026 210 VAL E C 9018 O O . VAL E 211 ? 0.4060 0.4428 0.4336 -0.0519 0.0170 0.0102 210 VAL E O 9019 C CB . VAL E 211 ? 0.4352 0.4811 0.4830 -0.0784 0.0294 0.0087 210 VAL E CB 9020 C CG1 . VAL E 211 ? 0.4527 0.4695 0.5019 -0.0820 0.0319 0.0116 210 VAL E CG1 9021 C CG2 . VAL E 211 ? 0.4305 0.4959 0.4908 -0.0906 0.0340 0.0037 210 VAL E CG2 9022 N N . PRO E 212 ? 0.4028 0.4280 0.4417 -0.0582 0.0150 -0.0040 211 PRO E N 9023 C CA . PRO E 212 ? 0.4106 0.4211 0.4430 -0.0491 0.0125 -0.0010 211 PRO E CA 9024 C C . PRO E 212 ? 0.4184 0.4116 0.4469 -0.0474 0.0161 0.0110 211 PRO E C 9025 O O . PRO E 212 ? 0.4474 0.4288 0.4795 -0.0551 0.0215 0.0155 211 PRO E O 9026 C CB . PRO E 212 ? 0.4066 0.4086 0.4438 -0.0504 0.0109 -0.0114 211 PRO E CB 9027 C CG . PRO E 212 ? 0.3969 0.4151 0.4409 -0.0577 0.0099 -0.0214 211 PRO E CG 9028 C CD . PRO E 212 ? 0.4017 0.4301 0.4496 -0.0650 0.0138 -0.0161 211 PRO E CD 9029 N N . LYS E 213 ? 0.4067 0.3995 0.4279 -0.0375 0.0132 0.0163 212 LYS E N 9030 C CA . LYS E 213 ? 0.4185 0.3984 0.4343 -0.0321 0.0148 0.0279 212 LYS E CA 9031 C C . LYS E 213 ? 0.4060 0.3714 0.4237 -0.0250 0.0128 0.0255 212 LYS E C 9032 O O . LYS E 213 ? 0.4036 0.3772 0.4205 -0.0180 0.0085 0.0210 212 LYS E O 9033 C CB . LYS E 213 ? 0.4116 0.4063 0.4189 -0.0249 0.0119 0.0336 212 LYS E CB 9034 C CG . LYS E 213 ? 0.4139 0.4237 0.4179 -0.0299 0.0144 0.0362 212 LYS E CG 9035 C CD . LYS E 213 ? 0.4124 0.4358 0.4069 -0.0225 0.0116 0.0405 212 LYS E CD 9036 C CE . LYS E 213 ? 0.4057 0.4406 0.4013 -0.0182 0.0062 0.0304 212 LYS E CE 9037 N NZ . LYS E 213 ? 0.4158 0.4671 0.4041 -0.0151 0.0047 0.0305 212 LYS E NZ 9038 N N . ILE E 214 ? 0.4145 0.3578 0.4355 -0.0272 0.0167 0.0281 213 ILE E N 9039 C CA . ILE E 214 ? 0.4039 0.3321 0.4263 -0.0181 0.0155 0.0271 213 ILE E CA 9040 C C . ILE E 214 ? 0.3997 0.3261 0.4148 -0.0068 0.0142 0.0405 213 ILE E C 9041 O O . ILE E 214 ? 0.4003 0.3199 0.4095 -0.0076 0.0176 0.0531 213 ILE E O 9042 C CB . ILE E 214 ? 0.4327 0.3350 0.4613 -0.0235 0.0204 0.0238 213 ILE E CB 9043 C CG1 . ILE E 214 ? 0.4271 0.3357 0.4628 -0.0315 0.0194 0.0069 213 ILE E CG1 9044 C CG2 . ILE E 214 ? 0.4491 0.3324 0.4775 -0.0112 0.0203 0.0269 213 ILE E CG2 9045 C CD1 . ILE E 214 ? 0.4545 0.3424 0.4980 -0.0420 0.0245 0.0008 213 ILE E CD1 9046 N N . ALA E 215 ? 0.3829 0.3181 0.3983 0.0037 0.0093 0.0375 214 ALA E N 9047 C CA . ALA E 215 ? 0.3829 0.3181 0.3939 0.0169 0.0068 0.0476 214 ALA E CA 9048 C C . ALA E 215 ? 0.3701 0.3086 0.3876 0.0265 0.0035 0.0396 214 ALA E C 9049 O O . ALA E 215 ? 0.3548 0.2973 0.3782 0.0222 0.0036 0.0271 214 ALA E O 9050 C CB . ALA E 215 ? 0.3760 0.3344 0.3797 0.0189 0.0029 0.0528 214 ALA E CB 9051 N N . THR E 216 ? 0.3668 0.3054 0.3829 0.0402 0.0009 0.0472 215 THR E N 9052 C CA . THR E 216 ? 0.3567 0.3016 0.3805 0.0512 -0.0017 0.0407 215 THR E CA 9053 C C . THR E 216 ? 0.3424 0.3188 0.3675 0.0551 -0.0077 0.0383 215 THR E C 9054 O O . THR E 216 ? 0.3478 0.3353 0.3678 0.0627 -0.0117 0.0471 215 THR E O 9055 C CB . THR E 216 ? 0.3814 0.3073 0.4043 0.0656 -0.0011 0.0503 215 THR E CB 9056 O OG1 . THR E 216 ? 0.4037 0.2967 0.4259 0.0600 0.0054 0.0521 215 THR E OG1 9057 C CG2 . THR E 216 ? 0.3788 0.3138 0.4112 0.0786 -0.0036 0.0428 215 THR E CG2 9058 N N . ARG E 217 ? 0.3268 0.3179 0.3586 0.0497 -0.0080 0.0262 216 ARG E N 9059 C CA . ARG E 217 ? 0.3118 0.3303 0.3458 0.0482 -0.0120 0.0219 216 ARG E CA 9060 C C . ARG E 217 ? 0.3061 0.3403 0.3514 0.0541 -0.0129 0.0134 216 ARG E C 9061 O O . ARG E 217 ? 0.3157 0.3402 0.3662 0.0572 -0.0096 0.0085 216 ARG E O 9062 C CB . ARG E 217 ? 0.2987 0.3199 0.3295 0.0346 -0.0101 0.0167 216 ARG E CB 9063 C CG . ARG E 217 ? 0.3220 0.3342 0.3432 0.0290 -0.0090 0.0246 216 ARG E CG 9064 C CD . ARG E 217 ? 0.3153 0.3271 0.3344 0.0172 -0.0065 0.0192 216 ARG E CD 9065 N NE . ARG E 217 ? 0.3296 0.3295 0.3528 0.0138 -0.0033 0.0126 216 ARG E NE 9066 C CZ . ARG E 217 ? 0.3323 0.3199 0.3543 0.0068 -0.0002 0.0113 216 ARG E CZ 9067 N NH1 . ARG E 217 ? 0.3365 0.3219 0.3543 0.0009 0.0010 0.0167 216 ARG E NH1 9068 N NH2 . ARG E 217 ? 0.3374 0.3176 0.3631 0.0053 0.0015 0.0033 216 ARG E NH2 9069 N N . SER E 218 ? 0.2983 0.3582 0.3482 0.0553 -0.0170 0.0107 217 SER E N 9070 C CA . SER E 218 ? 0.2970 0.3770 0.3598 0.0588 -0.0172 0.0023 217 SER E CA 9071 C C . SER E 218 ? 0.2936 0.3737 0.3596 0.0475 -0.0117 -0.0067 217 SER E C 9072 O O . SER E 218 ? 0.3001 0.3735 0.3591 0.0372 -0.0102 -0.0070 217 SER E O 9073 C CB . SER E 218 ? 0.2912 0.4004 0.3591 0.0606 -0.0233 0.0007 217 SER E CB 9074 O OG . SER E 218 ? 0.3105 0.4202 0.3707 0.0706 -0.0289 0.0108 217 SER E OG 9075 N N . LYS E 219 ? 0.3043 0.3929 0.3801 0.0505 -0.0085 -0.0135 218 LYS E N 9076 C CA . LYS E 219 ? 0.3092 0.3984 0.3862 0.0411 -0.0023 -0.0206 218 LYS E CA 9077 C C . LYS E 219 ? 0.2943 0.4001 0.3749 0.0309 -0.0019 -0.0239 218 LYS E C 9078 O O . LYS E 219 ? 0.2970 0.4248 0.3881 0.0322 -0.0044 -0.0268 218 LYS E O 9079 C CB . LYS E 219 ? 0.3242 0.4211 0.4106 0.0474 0.0020 -0.0269 218 LYS E CB 9080 C CG . LYS E 219 ? 0.3567 0.4331 0.4393 0.0557 0.0038 -0.0271 218 LYS E CG 9081 C CD . LYS E 219 ? 0.3782 0.4630 0.4676 0.0592 0.0100 -0.0358 218 LYS E CD 9082 C CE . LYS E 219 ? 0.4159 0.4835 0.5049 0.0705 0.0111 -0.0383 218 LYS E CE 9083 N NZ . LYS E 219 ? 0.4378 0.4768 0.5146 0.0654 0.0109 -0.0365 218 LYS E NZ 9084 N N . VAL E 220 ? 0.2938 0.3888 0.3662 0.0209 0.0012 -0.0241 219 VAL E N 9085 C CA . VAL E 220 ? 0.2882 0.3929 0.3636 0.0109 0.0036 -0.0276 219 VAL E CA 9086 C C . VAL E 220 ? 0.2876 0.3847 0.3597 0.0059 0.0115 -0.0295 219 VAL E C 9087 O O . VAL E 220 ? 0.2912 0.3721 0.3526 0.0068 0.0126 -0.0273 219 VAL E O 9088 C CB . VAL E 220 ? 0.2813 0.3792 0.3482 0.0056 0.0001 -0.0249 219 VAL E CB 9089 C CG1 . VAL E 220 ? 0.2813 0.3843 0.3514 -0.0045 0.0035 -0.0295 219 VAL E CG1 9090 C CG2 . VAL E 220 ? 0.2887 0.3959 0.3562 0.0115 -0.0073 -0.0222 219 VAL E CG2 9091 N N . ASN E 221 ? 0.2735 0.3838 0.3545 0.0007 0.0171 -0.0336 220 ASN E N 9092 C CA . ASN E 221 ? 0.2774 0.3837 0.3548 -0.0021 0.0258 -0.0343 220 ASN E CA 9093 C C . ASN E 221 ? 0.2680 0.3668 0.3396 0.0066 0.0263 -0.0348 220 ASN E C 9094 O O . ASN E 221 ? 0.2745 0.3613 0.3342 0.0058 0.0295 -0.0338 220 ASN E O 9095 C CB . ASN E 221 ? 0.2868 0.3779 0.3523 -0.0098 0.0294 -0.0307 220 ASN E CB 9096 C CG . ASN E 221 ? 0.2990 0.3935 0.3703 -0.0187 0.0297 -0.0318 220 ASN E CG 9097 O OD1 . ASN E 221 ? 0.3022 0.4144 0.3882 -0.0222 0.0304 -0.0367 220 ASN E OD1 9098 N ND2 . ASN E 221 ? 0.3003 0.3793 0.3612 -0.0221 0.0289 -0.0286 220 ASN E ND2 9099 N N . GLY E 222 ? 0.2665 0.3729 0.3465 0.0156 0.0229 -0.0370 221 GLY E N 9100 C CA . GLY E 222 ? 0.2685 0.3663 0.3452 0.0246 0.0234 -0.0392 221 GLY E CA 9101 C C . GLY E 222 ? 0.2695 0.3451 0.3351 0.0266 0.0189 -0.0364 221 GLY E C 9102 O O . GLY E 222 ? 0.3027 0.3690 0.3662 0.0327 0.0197 -0.0399 221 GLY E O 9103 N N . GLN E 223 ? 0.2613 0.3288 0.3208 0.0213 0.0147 -0.0312 222 GLN E N 9104 C CA . GLN E 223 ? 0.2663 0.3151 0.3165 0.0210 0.0117 -0.0288 222 GLN E CA 9105 C C . GLN E 223 ? 0.2551 0.2992 0.3058 0.0230 0.0060 -0.0225 222 GLN E C 9106 O O . GLN E 223 ? 0.2483 0.3014 0.3002 0.0203 0.0033 -0.0194 222 GLN E O 9107 C CB . GLN E 223 ? 0.2782 0.3215 0.3182 0.0130 0.0128 -0.0279 222 GLN E CB 9108 C CG . GLN E 223 ? 0.2974 0.3450 0.3328 0.0111 0.0187 -0.0316 222 GLN E CG 9109 C CD . GLN E 223 ? 0.3229 0.3665 0.3555 0.0158 0.0209 -0.0380 222 GLN E CD 9110 O OE1 . GLN E 223 ? 0.3374 0.3700 0.3703 0.0187 0.0179 -0.0403 222 GLN E OE1 9111 N NE2 . GLN E 223 ? 0.3394 0.3910 0.3688 0.0162 0.0268 -0.0412 222 GLN E NE2 9112 N N . SER E 224 ? 0.2542 0.2831 0.3031 0.0276 0.0047 -0.0209 223 SER E N 9113 C CA . SER E 224 ? 0.2515 0.2711 0.2973 0.0286 0.0010 -0.0130 223 SER E CA 9114 C C . SER E 224 ? 0.2361 0.2466 0.2738 0.0194 0.0011 -0.0112 223 SER E C 9115 O O . SER E 224 ? 0.2301 0.2385 0.2643 0.0178 -0.0010 -0.0045 223 SER E O 9116 C CB . SER E 224 ? 0.2690 0.2728 0.3168 0.0374 0.0011 -0.0109 223 SER E CB 9117 O OG . SER E 224 ? 0.2819 0.2971 0.3371 0.0483 -0.0008 -0.0093 223 SER E OG 9118 N N . GLY E 225 ? 0.2346 0.2415 0.2690 0.0142 0.0036 -0.0173 224 GLY E N 9119 C CA . GLY E 225 ? 0.2370 0.2411 0.2655 0.0064 0.0030 -0.0164 224 GLY E CA 9120 C C . GLY E 225 ? 0.2278 0.2436 0.2540 0.0035 0.0016 -0.0130 224 GLY E C 9121 O O . GLY E 225 ? 0.2174 0.2432 0.2468 0.0056 0.0015 -0.0131 224 GLY E O 9122 N N . ARG E 226 ? 0.2370 0.2521 0.2587 -0.0015 0.0008 -0.0111 225 ARG E N 9123 C CA . ARG E 226 ? 0.2379 0.2619 0.2567 -0.0039 0.0000 -0.0097 225 ARG E CA 9124 C C . ARG E 226 ? 0.2575 0.2817 0.2717 -0.0076 0.0004 -0.0117 225 ARG E C 9125 O O . ARG E 226 ? 0.2619 0.2822 0.2761 -0.0102 0.0003 -0.0128 225 ARG E O 9126 C CB . ARG E 226 ? 0.2433 0.2707 0.2613 -0.0035 -0.0022 -0.0041 225 ARG E CB 9127 C CG . ARG E 226 ? 0.2557 0.2867 0.2774 0.0020 -0.0042 -0.0011 225 ARG E CG 9128 C CD . ARG E 226 ? 0.2531 0.2968 0.2788 0.0026 -0.0050 -0.0051 225 ARG E CD 9129 N NE . ARG E 226 ? 0.2690 0.3215 0.3000 0.0089 -0.0078 -0.0036 225 ARG E NE 9130 C CZ . ARG E 226 ? 0.2768 0.3303 0.3145 0.0140 -0.0071 -0.0052 225 ARG E CZ 9131 N NH1 . ARG E 226 ? 0.2771 0.3226 0.3161 0.0132 -0.0032 -0.0090 225 ARG E NH1 9132 N NH2 . ARG E 226 ? 0.2862 0.3509 0.3292 0.0212 -0.0106 -0.0037 225 ARG E NH2 9133 N N . MET E 227 ? 0.2827 0.3117 0.2938 -0.0079 0.0009 -0.0123 226 MET E N 9134 C CA . MET E 227 ? 0.2880 0.3193 0.2946 -0.0089 0.0007 -0.0132 226 MET E CA 9135 C C . MET E 227 ? 0.2819 0.3172 0.2875 -0.0093 0.0000 -0.0113 226 MET E C 9136 O O . MET E 227 ? 0.2789 0.3150 0.2854 -0.0089 0.0004 -0.0114 226 MET E O 9137 C CB . MET E 227 ? 0.3134 0.3442 0.3152 -0.0066 0.0027 -0.0149 226 MET E CB 9138 C CG . MET E 227 ? 0.3445 0.3735 0.3459 -0.0053 0.0044 -0.0176 226 MET E CG 9139 S SD . MET E 227 ? 0.3667 0.3990 0.3629 -0.0044 0.0028 -0.0223 226 MET E SD 9140 C CE . MET E 227 ? 0.3679 0.3979 0.3641 -0.0026 0.0053 -0.0272 226 MET E CE 9141 N N . GLU E 228 ? 0.2744 0.3141 0.2791 -0.0104 -0.0007 -0.0108 227 GLU E N 9142 C CA . GLU E 228 ? 0.2689 0.3139 0.2717 -0.0098 -0.0009 -0.0103 227 GLU E CA 9143 C C . GLU E 228 ? 0.2688 0.3166 0.2689 -0.0071 -0.0006 -0.0125 227 GLU E C 9144 O O . GLU E 228 ? 0.2830 0.3358 0.2842 -0.0075 -0.0014 -0.0135 227 GLU E O 9145 C CB . GLU E 228 ? 0.2764 0.3263 0.2804 -0.0125 -0.0011 -0.0071 227 GLU E CB 9146 C CG . GLU E 228 ? 0.2796 0.3379 0.2807 -0.0117 -0.0008 -0.0071 227 GLU E CG 9147 C CD . GLU E 228 ? 0.2891 0.3518 0.2890 -0.0140 0.0000 -0.0018 227 GLU E CD 9148 O OE1 . GLU E 228 ? 0.3136 0.3715 0.3160 -0.0173 0.0011 0.0022 227 GLU E OE1 9149 O OE2 . GLU E 228 ? 0.2998 0.3701 0.2956 -0.0125 0.0000 -0.0017 227 GLU E OE2 9150 N N . PHE E 229 ? 0.2741 0.3188 0.2710 -0.0038 0.0003 -0.0137 228 PHE E N 9151 C CA . PHE E 229 ? 0.2790 0.3241 0.2722 0.0015 0.0007 -0.0145 228 PHE E CA 9152 C C . PHE E 229 ? 0.2719 0.3236 0.2649 0.0044 0.0007 -0.0164 228 PHE E C 9153 O O . PHE E 229 ? 0.2641 0.3159 0.2574 0.0028 0.0013 -0.0181 228 PHE E O 9154 C CB . PHE E 229 ? 0.2923 0.3249 0.2811 0.0043 0.0033 -0.0134 228 PHE E CB 9155 C CG . PHE E 229 ? 0.2971 0.3266 0.2844 0.0033 0.0041 -0.0116 228 PHE E CG 9156 C CD1 . PHE E 229 ? 0.2956 0.3293 0.2784 0.0074 0.0028 -0.0110 228 PHE E CD1 9157 C CD2 . PHE E 229 ? 0.2973 0.3229 0.2881 -0.0010 0.0058 -0.0117 228 PHE E CD2 9158 C CE1 . PHE E 229 ? 0.3051 0.3376 0.2853 0.0069 0.0037 -0.0107 228 PHE E CE1 9159 C CE2 . PHE E 229 ? 0.2945 0.3188 0.2840 -0.0011 0.0072 -0.0110 228 PHE E CE2 9160 C CZ . PHE E 229 ? 0.3060 0.3332 0.2895 0.0027 0.0063 -0.0107 228 PHE E CZ 9161 N N . PHE E 230 ? 0.2692 0.3287 0.2615 0.0096 -0.0001 -0.0171 229 PHE E N 9162 C CA . PHE E 230 ? 0.2582 0.3267 0.2512 0.0143 0.0002 -0.0198 229 PHE E CA 9163 C C . PHE E 230 ? 0.2619 0.3264 0.2507 0.0248 0.0004 -0.0199 229 PHE E C 9164 O O . PHE E 230 ? 0.2616 0.3187 0.2458 0.0283 0.0000 -0.0168 229 PHE E O 9165 C CB . PHE E 230 ? 0.2541 0.3417 0.2532 0.0111 -0.0006 -0.0207 229 PHE E CB 9166 C CG . PHE E 230 ? 0.2552 0.3440 0.2572 0.0017 0.0001 -0.0186 229 PHE E CG 9167 C CD1 . PHE E 230 ? 0.2504 0.3332 0.2543 -0.0037 -0.0007 -0.0165 229 PHE E CD1 9168 C CD2 . PHE E 230 ? 0.2488 0.3440 0.2505 -0.0002 0.0021 -0.0184 229 PHE E CD2 9169 C CE1 . PHE E 230 ? 0.2517 0.3326 0.2577 -0.0105 0.0004 -0.0133 229 PHE E CE1 9170 C CE2 . PHE E 230 ? 0.2486 0.3437 0.2509 -0.0072 0.0031 -0.0142 229 PHE E CE2 9171 C CZ . PHE E 230 ? 0.2480 0.3347 0.2526 -0.0120 0.0023 -0.0112 229 PHE E CZ 9172 N N . TRP E 231 ? 0.2613 0.3311 0.2505 0.0308 0.0013 -0.0232 230 TRP E N 9173 C CA . TRP E 231 ? 0.2725 0.3372 0.2577 0.0432 0.0018 -0.0232 230 TRP E CA 9174 C C . TRP E 231 ? 0.2691 0.3508 0.2582 0.0502 0.0018 -0.0279 230 TRP E C 9175 O O . TRP E 231 ? 0.2668 0.3615 0.2605 0.0445 0.0027 -0.0314 230 TRP E O 9176 C CB . TRP E 231 ? 0.2829 0.3213 0.2622 0.0452 0.0054 -0.0227 230 TRP E CB 9177 C CG . TRP E 231 ? 0.2832 0.3179 0.2646 0.0403 0.0075 -0.0291 230 TRP E CG 9178 C CD1 . TRP E 231 ? 0.2722 0.3061 0.2557 0.0295 0.0075 -0.0307 230 TRP E CD1 9179 C CD2 . TRP E 231 ? 0.2922 0.3252 0.2730 0.0472 0.0095 -0.0357 230 TRP E CD2 9180 N NE1 . TRP E 231 ? 0.2719 0.3056 0.2555 0.0288 0.0088 -0.0382 230 TRP E NE1 9181 C CE2 . TRP E 231 ? 0.2831 0.3154 0.2652 0.0391 0.0104 -0.0419 230 TRP E CE2 9182 C CE3 . TRP E 231 ? 0.3041 0.3376 0.2836 0.0606 0.0103 -0.0376 230 TRP E CE3 9183 C CZ2 . TRP E 231 ? 0.2961 0.3279 0.2774 0.0428 0.0123 -0.0511 230 TRP E CZ2 9184 C CZ3 . TRP E 231 ? 0.3192 0.3502 0.2989 0.0650 0.0128 -0.0463 230 TRP E CZ3 9185 C CH2 . TRP E 231 ? 0.3214 0.3515 0.3017 0.0555 0.0139 -0.0536 230 TRP E CH2 9186 N N . THR E 232 ? 0.2766 0.3593 0.2635 0.0636 0.0010 -0.0274 231 THR E N 9187 C CA . THR E 232 ? 0.2809 0.3785 0.2717 0.0732 0.0016 -0.0327 231 THR E CA 9188 C C . THR E 232 ? 0.3034 0.3871 0.2878 0.0902 0.0018 -0.0302 231 THR E C 9189 O O . THR E 232 ? 0.3183 0.3872 0.2955 0.0937 0.0009 -0.0233 231 THR E O 9190 C CB . THR E 232 ? 0.2678 0.3998 0.2687 0.0710 -0.0010 -0.0350 231 THR E CB 9191 O OG1 . THR E 232 ? 0.2694 0.4193 0.2757 0.0782 0.0009 -0.0411 231 THR E OG1 9192 C CG2 . THR E 232 ? 0.2701 0.4131 0.2714 0.0780 -0.0058 -0.0321 231 THR E CG2 9193 N N . ILE E 233 ? 0.3171 0.4044 0.3032 0.1014 0.0036 -0.0356 232 ILE E N 9194 C CA . ILE E 233 ? 0.3452 0.4226 0.3263 0.1208 0.0036 -0.0330 232 ILE E CA 9195 C C . ILE E 233 ? 0.3442 0.4579 0.3329 0.1312 -0.0011 -0.0343 232 ILE E C 9196 O O . ILE E 233 ? 0.3300 0.4712 0.3290 0.1296 -0.0008 -0.0418 232 ILE E O 9197 C CB . ILE E 233 ? 0.3642 0.4228 0.3435 0.1290 0.0086 -0.0396 232 ILE E CB 9198 C CG1 . ILE E 233 ? 0.3674 0.3951 0.3419 0.1163 0.0129 -0.0411 232 ILE E CG1 9199 C CG2 . ILE E 233 ? 0.3958 0.4397 0.3691 0.1509 0.0091 -0.0357 232 ILE E CG2 9200 C CD1 . ILE E 233 ? 0.3807 0.3781 0.3466 0.1151 0.0145 -0.0313 232 ILE E CD1 9201 N N . LEU E 234 ? 0.3557 0.4725 0.3397 0.1413 -0.0054 -0.0274 233 LEU E N 9202 C CA . LEU E 234 ? 0.3584 0.5131 0.3506 0.1515 -0.0112 -0.0297 233 LEU E CA 9203 C C . LEU E 234 ? 0.3829 0.5329 0.3709 0.1764 -0.0113 -0.0281 233 LEU E C 9204 O O . LEU E 234 ? 0.3898 0.5130 0.3645 0.1884 -0.0111 -0.0189 233 LEU E O 9205 C CB . LEU E 234 ? 0.3593 0.5268 0.3491 0.1478 -0.0172 -0.0250 233 LEU E CB 9206 C CG . LEU E 234 ? 0.3627 0.5756 0.3637 0.1548 -0.0242 -0.0300 233 LEU E CG 9207 C CD1 . LEU E 234 ? 0.3494 0.5934 0.3686 0.1402 -0.0229 -0.0401 233 LEU E CD1 9208 C CD2 . LEU E 234 ? 0.3644 0.5873 0.3605 0.1526 -0.0306 -0.0267 233 LEU E CD2 9209 N N . LYS E 235 ? 0.3941 0.5697 0.3934 0.1844 -0.0109 -0.0366 234 LYS E N 9210 C CA . LYS E 235 ? 0.4310 0.6030 0.4283 0.2096 -0.0104 -0.0371 234 LYS E CA 9211 C C . LYS E 235 ? 0.4272 0.6228 0.4237 0.2279 -0.0182 -0.0316 234 LYS E C 9212 O O . LYS E 235 ? 0.4058 0.6336 0.4091 0.2193 -0.0241 -0.0327 234 LYS E O 9213 C CB . LYS E 235 ? 0.4390 0.6373 0.4499 0.2122 -0.0073 -0.0494 234 LYS E CB 9214 C CG . LYS E 235 ? 0.4509 0.6289 0.4607 0.1973 0.0000 -0.0558 234 LYS E CG 9215 C CD . LYS E 235 ? 0.4928 0.6262 0.4913 0.2090 0.0051 -0.0557 234 LYS E CD 9216 C CE . LYS E 235 ? 0.5223 0.6647 0.5251 0.2330 0.0068 -0.0627 234 LYS E CE 9217 N NZ . LYS E 235 ? 0.5674 0.6666 0.5579 0.2527 0.0089 -0.0566 234 LYS E NZ 9218 N N . PRO E 236 ? 0.4513 0.6305 0.4390 0.2537 -0.0183 -0.0260 235 PRO E N 9219 C CA . PRO E 236 ? 0.4670 0.6737 0.4538 0.2756 -0.0265 -0.0211 235 PRO E CA 9220 C C . PRO E 236 ? 0.4447 0.7130 0.4526 0.2736 -0.0326 -0.0326 235 PRO E C 9221 O O . PRO E 236 ? 0.4425 0.7292 0.4648 0.2694 -0.0286 -0.0435 235 PRO E O 9222 C CB . PRO E 236 ? 0.4987 0.6811 0.4781 0.3040 -0.0234 -0.0173 235 PRO E CB 9223 C CG . PRO E 236 ? 0.5127 0.6377 0.4805 0.2946 -0.0138 -0.0139 235 PRO E CG 9224 C CD . PRO E 236 ? 0.4779 0.6085 0.4545 0.2637 -0.0107 -0.0229 235 PRO E CD 9225 N N . ASN E 237 ? 0.4364 0.7371 0.4463 0.2751 -0.0416 -0.0309 236 ASN E N 9226 C CA . ASN E 237 ? 0.4233 0.7859 0.4549 0.2735 -0.0480 -0.0425 236 ASN E CA 9227 C C . ASN E 237 ? 0.3890 0.7727 0.4373 0.2425 -0.0450 -0.0528 236 ASN E C 9228 O O . ASN E 237 ? 0.3722 0.8063 0.4405 0.2371 -0.0488 -0.0629 236 ASN E O 9229 C CB . ASN E 237 ? 0.4355 0.8248 0.4788 0.2974 -0.0483 -0.0487 236 ASN E CB 9230 C CG . ASN E 237 ? 0.4672 0.8714 0.5035 0.3286 -0.0572 -0.0420 236 ASN E CG 9231 O OD1 . ASN E 237 ? 0.4863 0.9424 0.5390 0.3421 -0.0636 -0.0499 236 ASN E OD1 9232 N ND2 . ASN E 237 ? 0.4961 0.8566 0.5080 0.3406 -0.0574 -0.0269 236 ASN E ND2 9233 N N . ASP E 238 ? 0.3776 0.7237 0.4183 0.2225 -0.0380 -0.0500 237 ASP E N 9234 C CA . ASP E 238 ? 0.3583 0.7180 0.4107 0.1941 -0.0354 -0.0564 237 ASP E CA 9235 C C . ASP E 238 ? 0.3556 0.7088 0.4006 0.1822 -0.0404 -0.0521 237 ASP E C 9236 O O . ASP E 238 ? 0.3713 0.7031 0.3994 0.1945 -0.0440 -0.0431 237 ASP E O 9237 C CB . ASP E 238 ? 0.3535 0.6807 0.4020 0.1798 -0.0258 -0.0564 237 ASP E CB 9238 C CG . ASP E 238 ? 0.3355 0.6859 0.3992 0.1557 -0.0219 -0.0636 237 ASP E CG 9239 O OD1 . ASP E 238 ? 0.3186 0.7122 0.3991 0.1510 -0.0254 -0.0701 237 ASP E OD1 9240 O OD2 . ASP E 238 ? 0.3257 0.6523 0.3850 0.1416 -0.0152 -0.0626 237 ASP E OD2 9241 N N . ALA E 239 ? 0.3430 0.7142 0.4003 0.1587 -0.0400 -0.0585 238 ALA E N 9242 C CA . ALA E 239 ? 0.3310 0.6981 0.3834 0.1459 -0.0444 -0.0572 238 ALA E CA 9243 C C . ALA E 239 ? 0.3098 0.6572 0.3645 0.1202 -0.0379 -0.0578 238 ALA E C 9244 O O . ALA E 239 ? 0.3012 0.6595 0.3685 0.1089 -0.0322 -0.0626 238 ALA E O 9245 C CB . ALA E 239 ? 0.3286 0.7455 0.3961 0.1450 -0.0527 -0.0668 238 ALA E CB 9246 N N . ILE E 240 ? 0.3106 0.6301 0.3526 0.1124 -0.0384 -0.0524 239 ILE E N 9247 C CA . ILE E 240 ? 0.2960 0.5968 0.3394 0.0899 -0.0334 -0.0524 239 ILE E CA 9248 C C . ILE E 240 ? 0.2878 0.6092 0.3397 0.0765 -0.0382 -0.0594 239 ILE E C 9249 O O . ILE E 240 ? 0.2994 0.6286 0.3446 0.0843 -0.0450 -0.0600 239 ILE E O 9250 C CB . ILE E 240 ? 0.3030 0.5581 0.3280 0.0898 -0.0298 -0.0428 239 ILE E CB 9251 C CG1 . ILE E 240 ? 0.2834 0.5210 0.3110 0.0691 -0.0245 -0.0427 239 ILE E CG1 9252 C CG2 . ILE E 240 ? 0.3157 0.5617 0.3268 0.0973 -0.0348 -0.0381 239 ILE E CG2 9253 C CD1 . ILE E 240 ? 0.2808 0.4794 0.2948 0.0689 -0.0200 -0.0352 239 ILE E CD1 9254 N N . ASN E 241 ? 0.2659 0.5957 0.3319 0.0565 -0.0342 -0.0648 240 ASN E N 9255 C CA . ASN E 241 ? 0.2622 0.6096 0.3389 0.0415 -0.0374 -0.0734 240 ASN E CA 9256 C C . ASN E 241 ? 0.2591 0.5769 0.3331 0.0234 -0.0321 -0.0708 240 ASN E C 9257 O O . ASN E 241 ? 0.2585 0.5670 0.3377 0.0124 -0.0249 -0.0681 240 ASN E O 9258 C CB . ASN E 241 ? 0.2609 0.6498 0.3609 0.0333 -0.0368 -0.0835 240 ASN E CB 9259 C CG . ASN E 241 ? 0.2647 0.6866 0.3695 0.0530 -0.0418 -0.0865 240 ASN E CG 9260 O OD1 . ASN E 241 ? 0.2759 0.7153 0.3769 0.0662 -0.0507 -0.0895 240 ASN E OD1 9261 N ND2 . ASN E 241 ? 0.2647 0.6957 0.3766 0.0568 -0.0361 -0.0855 240 ASN E ND2 9262 N N . PHE E 242 ? 0.2654 0.5700 0.3306 0.0213 -0.0358 -0.0716 241 PHE E N 9263 C CA . PHE E 242 ? 0.2647 0.5414 0.3272 0.0066 -0.0316 -0.0697 241 PHE E CA 9264 C C . PHE E 242 ? 0.2718 0.5631 0.3490 -0.0103 -0.0326 -0.0810 241 PHE E C 9265 O O . PHE E 242 ? 0.2757 0.5925 0.3576 -0.0084 -0.0395 -0.0910 241 PHE E O 9266 C CB . PHE E 242 ? 0.2686 0.5199 0.3122 0.0151 -0.0336 -0.0640 241 PHE E CB 9267 C CG . PHE E 242 ? 0.2620 0.4889 0.2923 0.0262 -0.0301 -0.0527 241 PHE E CG 9268 C CD1 . PHE E 242 ? 0.2590 0.4596 0.2869 0.0186 -0.0238 -0.0467 241 PHE E CD1 9269 C CD2 . PHE E 242 ? 0.2666 0.4964 0.2867 0.0444 -0.0331 -0.0483 241 PHE E CD2 9270 C CE1 . PHE E 242 ? 0.2644 0.4441 0.2817 0.0272 -0.0208 -0.0387 241 PHE E CE1 9271 C CE2 . PHE E 242 ? 0.2689 0.4734 0.2779 0.0531 -0.0290 -0.0391 241 PHE E CE2 9272 C CZ . PHE E 242 ? 0.2704 0.4506 0.2787 0.0435 -0.0229 -0.0353 241 PHE E CZ 9273 N N . GLU E 243 ? 0.2755 0.5498 0.3593 -0.0266 -0.0257 -0.0797 242 GLU E N 9274 C CA . GLU E 243 ? 0.2872 0.5645 0.3829 -0.0436 -0.0254 -0.0898 242 GLU E CA 9275 C C . GLU E 243 ? 0.2839 0.5234 0.3738 -0.0529 -0.0197 -0.0840 242 GLU E C 9276 O O . GLU E 243 ? 0.2926 0.5134 0.3788 -0.0543 -0.0134 -0.0733 242 GLU E O 9277 C CB . GLU E 243 ? 0.2971 0.6020 0.4148 -0.0573 -0.0220 -0.0970 242 GLU E CB 9278 C CG . GLU E 243 ? 0.3231 0.6285 0.4550 -0.0770 -0.0207 -0.1086 242 GLU E CG 9279 C CD . GLU E 243 ? 0.3353 0.6686 0.4909 -0.0928 -0.0159 -0.1159 242 GLU E CD 9280 O OE1 . GLU E 243 ? 0.3522 0.7208 0.5159 -0.0858 -0.0185 -0.1189 242 GLU E OE1 9281 O OE2 . GLU E 243 ? 0.3633 0.6827 0.5297 -0.1121 -0.0089 -0.1183 242 GLU E OE2 9282 N N . SER E 244 ? 0.2817 0.5118 0.3706 -0.0583 -0.0222 -0.0918 243 SER E N 9283 C CA . SER E 244 ? 0.2864 0.4813 0.3703 -0.0649 -0.0172 -0.0873 243 SER E CA 9284 C C . SER E 244 ? 0.2924 0.4825 0.3820 -0.0749 -0.0188 -0.1004 243 SER E C 9285 O O . SER E 244 ? 0.3015 0.5117 0.3908 -0.0716 -0.0258 -0.1123 243 SER E O 9286 C CB . SER E 244 ? 0.2820 0.4558 0.3469 -0.0508 -0.0182 -0.0773 243 SER E CB 9287 O OG . SER E 244 ? 0.2850 0.4287 0.3464 -0.0556 -0.0138 -0.0732 243 SER E OG 9288 N N . ASN E 245 ? 0.2955 0.4583 0.3891 -0.0860 -0.0123 -0.0984 244 ASN E N 9289 C CA . ASN E 245 ? 0.3166 0.4665 0.4140 -0.0943 -0.0127 -0.1106 244 ASN E CA 9290 C C . ASN E 245 ? 0.3172 0.4338 0.4009 -0.0869 -0.0106 -0.1037 244 ASN E C 9291 O O . ASN E 245 ? 0.3261 0.4228 0.4129 -0.0936 -0.0082 -0.1106 244 ASN E O 9292 C CB . ASN E 245 ? 0.3359 0.4791 0.4517 -0.1142 -0.0059 -0.1157 244 ASN E CB 9293 C CG . ASN E 245 ? 0.3489 0.4612 0.4628 -0.1178 0.0033 -0.0993 244 ASN E CG 9294 O OD1 . ASN E 245 ? 0.3426 0.4518 0.4460 -0.1075 0.0042 -0.0848 244 ASN E OD1 9295 N ND2 . ASN E 245 ? 0.3773 0.4659 0.5007 -0.1320 0.0101 -0.1016 244 ASN E ND2 9296 N N . GLY E 246 ? 0.3015 0.4132 0.3713 -0.0732 -0.0114 -0.0912 245 GLY E N 9297 C CA . GLY E 246 ? 0.3034 0.3896 0.3619 -0.0657 -0.0096 -0.0849 245 GLY E CA 9298 C C . GLY E 246 ? 0.2859 0.3655 0.3346 -0.0557 -0.0081 -0.0695 245 GLY E C 9299 O O . GLY E 246 ? 0.2754 0.3642 0.3264 -0.0560 -0.0069 -0.0624 245 GLY E O 9300 N N . ASN E 247 ? 0.2832 0.3488 0.3219 -0.0473 -0.0079 -0.0659 246 ASN E N 9301 C CA . ASN E 247 ? 0.2699 0.3261 0.3009 -0.0394 -0.0061 -0.0533 246 ASN E CA 9302 C C . ASN E 247 ? 0.2620 0.3330 0.2864 -0.0317 -0.0084 -0.0487 246 ASN E C 9303 O O . ASN E 247 ? 0.2669 0.3324 0.2872 -0.0274 -0.0068 -0.0399 246 ASN E O 9304 C CB . ASN E 247 ? 0.2682 0.3109 0.3041 -0.0445 -0.0017 -0.0443 246 ASN E CB 9305 C CG . ASN E 247 ? 0.2851 0.3079 0.3267 -0.0505 0.0014 -0.0468 246 ASN E CG 9306 O OD1 . ASN E 247 ? 0.2882 0.3110 0.3383 -0.0601 0.0024 -0.0549 246 ASN E OD1 9307 N ND2 . ASN E 247 ? 0.2838 0.2895 0.3215 -0.0448 0.0032 -0.0407 246 ASN E ND2 9308 N N . PHE E 248 ? 0.2660 0.3556 0.2890 -0.0291 -0.0125 -0.0554 247 PHE E N 9309 C CA . PHE E 248 ? 0.2701 0.3736 0.2878 -0.0208 -0.0148 -0.0513 247 PHE E CA 9310 C C . PHE E 248 ? 0.2724 0.3709 0.2765 -0.0102 -0.0154 -0.0479 247 PHE E C 9311 O O . PHE E 248 ? 0.2742 0.3756 0.2728 -0.0080 -0.0172 -0.0537 247 PHE E O 9312 C CB . PHE E 248 ? 0.2824 0.4115 0.3066 -0.0224 -0.0192 -0.0600 247 PHE E CB 9313 C CG . PHE E 248 ? 0.2838 0.4290 0.3033 -0.0116 -0.0220 -0.0564 247 PHE E CG 9314 C CD1 . PHE E 248 ? 0.2792 0.4170 0.2958 -0.0067 -0.0190 -0.0470 247 PHE E CD1 9315 C CD2 . PHE E 248 ? 0.2978 0.4665 0.3162 -0.0058 -0.0279 -0.0633 247 PHE E CD2 9316 C CE1 . PHE E 248 ? 0.2827 0.4325 0.2954 0.0041 -0.0211 -0.0444 247 PHE E CE1 9317 C CE2 . PHE E 248 ? 0.3016 0.4845 0.3156 0.0063 -0.0306 -0.0593 247 PHE E CE2 9318 C CZ . PHE E 248 ? 0.2995 0.4711 0.3108 0.0113 -0.0268 -0.0498 247 PHE E CZ 9319 N N . ILE E 249 ? 0.2527 0.3429 0.2512 -0.0046 -0.0130 -0.0388 248 ILE E N 9320 C CA . ILE E 249 ? 0.2535 0.3384 0.2398 0.0044 -0.0121 -0.0340 248 ILE E CA 9321 C C . ILE E 249 ? 0.2534 0.3509 0.2355 0.0128 -0.0148 -0.0320 248 ILE E C 9322 O O . ILE E 249 ? 0.2445 0.3394 0.2285 0.0148 -0.0134 -0.0275 248 ILE E O 9323 C CB . ILE E 249 ? 0.2555 0.3228 0.2401 0.0042 -0.0074 -0.0266 248 ILE E CB 9324 C CG1 . ILE E 249 ? 0.2516 0.3095 0.2435 -0.0031 -0.0055 -0.0281 248 ILE E CG1 9325 C CG2 . ILE E 249 ? 0.2640 0.3241 0.2374 0.0107 -0.0045 -0.0221 248 ILE E CG2 9326 C CD1 . ILE E 249 ? 0.2598 0.3167 0.2509 -0.0045 -0.0057 -0.0345 248 ILE E CD1 9327 N N . ALA E 250 ? 0.2662 0.3790 0.2427 0.0189 -0.0191 -0.0359 249 ALA E N 9328 C CA . ALA E 250 ? 0.2762 0.4057 0.2509 0.0282 -0.0230 -0.0351 249 ALA E CA 9329 C C . ALA E 250 ? 0.2877 0.4056 0.2489 0.0408 -0.0206 -0.0246 249 ALA E C 9330 O O . ALA E 250 ? 0.2902 0.3924 0.2410 0.0427 -0.0167 -0.0191 249 ALA E O 9331 C CB . ALA E 250 ? 0.2884 0.4423 0.2623 0.0308 -0.0295 -0.0440 249 ALA E CB 9332 N N . PRO E 251 ? 0.2963 0.4216 0.2582 0.0495 -0.0222 -0.0219 250 PRO E N 9333 C CA . PRO E 251 ? 0.3162 0.4286 0.2642 0.0632 -0.0199 -0.0119 250 PRO E CA 9334 C C . PRO E 251 ? 0.3397 0.4589 0.2723 0.0730 -0.0225 -0.0090 250 PRO E C 9335 O O . PRO E 251 ? 0.3425 0.4866 0.2766 0.0739 -0.0291 -0.0168 250 PRO E O 9336 C CB . PRO E 251 ? 0.3135 0.4381 0.2665 0.0725 -0.0226 -0.0121 250 PRO E CB 9337 C CG . PRO E 251 ? 0.2947 0.4358 0.2650 0.0613 -0.0243 -0.0212 250 PRO E CG 9338 C CD . PRO E 251 ? 0.2899 0.4352 0.2652 0.0480 -0.0253 -0.0277 250 PRO E CD 9339 N N . GLU E 252 ? 0.3603 0.4582 0.2782 0.0792 -0.0169 0.0017 251 GLU E N 9340 C CA . GLU E 252 ? 0.3970 0.4998 0.2963 0.0927 -0.0183 0.0084 251 GLU E CA 9341 C C . GLU E 252 ? 0.4079 0.4946 0.2971 0.1074 -0.0151 0.0209 251 GLU E C 9342 O O . GLU E 252 ? 0.4077 0.5092 0.2893 0.1230 -0.0205 0.0238 251 GLU E O 9343 C CB . GLU E 252 ? 0.4256 0.5172 0.3136 0.0882 -0.0128 0.0119 251 GLU E CB 9344 C CG . GLU E 252 ? 0.4742 0.5670 0.3391 0.1033 -0.0121 0.0223 251 GLU E CG 9345 C CD . GLU E 252 ? 0.5096 0.5943 0.3626 0.0990 -0.0055 0.0256 251 GLU E CD 9346 O OE1 . GLU E 252 ? 0.5174 0.6010 0.3812 0.0851 -0.0035 0.0170 251 GLU E OE1 9347 O OE2 . GLU E 252 ? 0.5455 0.6248 0.3777 0.1104 -0.0018 0.0377 251 GLU E OE2 9348 N N . ASN E 253 ? 0.4058 0.4623 0.2953 0.1029 -0.0065 0.0277 252 ASN E N 9349 C CA . ASN E 253 ? 0.4266 0.4622 0.3084 0.1155 -0.0023 0.0382 252 ASN E CA 9350 C C . ASN E 253 ? 0.4166 0.4451 0.3139 0.1108 -0.0014 0.0323 252 ASN E C 9351 O O . ASN E 253 ? 0.3919 0.4223 0.3029 0.0957 -0.0009 0.0240 252 ASN E O 9352 C CB . ASN E 253 ? 0.4430 0.4465 0.3115 0.1149 0.0083 0.0509 252 ASN E CB 9353 C CG . ASN E 253 ? 0.4570 0.4667 0.3077 0.1196 0.0093 0.0579 252 ASN E CG 9354 O OD1 . ASN E 253 ? 0.4600 0.4894 0.2990 0.1339 0.0027 0.0603 252 ASN E OD1 9355 N ND2 . ASN E 253 ? 0.4535 0.4487 0.3018 0.1081 0.0178 0.0609 252 ASN E ND2 9356 N N . ALA E 254 ? 0.4375 0.4581 0.3314 0.1252 -0.0011 0.0371 253 ALA E N 9357 C CA . ALA E 254 ? 0.4268 0.4384 0.3323 0.1238 0.0007 0.0318 253 ALA E CA 9358 C C . ALA E 254 ? 0.4598 0.4392 0.3546 0.1367 0.0074 0.0420 253 ALA E C 9359 O O . ALA E 254 ? 0.4808 0.4482 0.3590 0.1483 0.0097 0.0544 253 ALA E O 9360 C CB . ALA E 254 ? 0.4186 0.4631 0.3355 0.1295 -0.0075 0.0226 253 ALA E CB 9361 N N . TYR E 255 ? 0.4612 0.4264 0.3646 0.1357 0.0106 0.0368 254 TYR E N 9362 C CA . TYR E 255 ? 0.4863 0.4140 0.3820 0.1442 0.0187 0.0442 254 TYR E CA 9363 C C . TYR E 255 ? 0.5028 0.4309 0.4006 0.1622 0.0167 0.0416 254 TYR E C 9364 O O . TYR E 255 ? 0.4757 0.4158 0.3869 0.1582 0.0147 0.0294 254 TYR E O 9365 C CB . TYR E 255 ? 0.4720 0.3757 0.3759 0.1260 0.0262 0.0385 254 TYR E CB 9366 C CG . TYR E 255 ? 0.4613 0.3605 0.3638 0.1098 0.0300 0.0415 254 TYR E CG 9367 C CD1 . TYR E 255 ? 0.4265 0.3502 0.3393 0.0955 0.0254 0.0330 254 TYR E CD1 9368 C CD2 . TYR E 255 ? 0.4870 0.3566 0.3783 0.1089 0.0393 0.0533 254 TYR E CD2 9369 C CE1 . TYR E 255 ? 0.4150 0.3358 0.3276 0.0822 0.0289 0.0349 254 TYR E CE1 9370 C CE2 . TYR E 255 ? 0.4785 0.3473 0.3700 0.0941 0.0435 0.0553 254 TYR E CE2 9371 C CZ . TYR E 255 ? 0.4409 0.3362 0.3434 0.0815 0.0379 0.0455 254 TYR E CZ 9372 O OH . TYR E 255 ? 0.4362 0.3323 0.3399 0.0686 0.0419 0.0465 254 TYR E OH 9373 N N . LYS E 256 ? 0.5379 0.4529 0.4216 0.1831 0.0176 0.0537 255 LYS E N 9374 C CA . LYS E 256 ? 0.5631 0.4702 0.4473 0.2027 0.0176 0.0529 255 LYS E CA 9375 C C . LYS E 256 ? 0.5804 0.4441 0.4665 0.1968 0.0280 0.0505 255 LYS E C 9376 O O . LYS E 256 ? 0.6040 0.4315 0.4806 0.1913 0.0368 0.0602 255 LYS E O 9377 C CB . LYS E 256 ? 0.5946 0.4966 0.4612 0.2289 0.0159 0.0684 255 LYS E CB 9378 C CG . LYS E 256 ? 0.5855 0.5336 0.4497 0.2377 0.0045 0.0693 255 LYS E CG 9379 C CD . LYS E 256 ? 0.6122 0.5694 0.4662 0.2687 -0.0006 0.0782 255 LYS E CD 9380 C CE . LYS E 256 ? 0.6546 0.5751 0.4836 0.2842 0.0057 0.0996 255 LYS E CE 9381 N NZ . LYS E 256 ? 0.6885 0.6114 0.5076 0.3172 0.0016 0.1089 255 LYS E NZ 9382 N N . ILE E 257 ? 0.5717 0.4400 0.4702 0.1976 0.0274 0.0369 256 ILE E N 9383 C CA . ILE E 257 ? 0.5954 0.4249 0.4965 0.1934 0.0363 0.0313 256 ILE E CA 9384 C C . ILE E 257 ? 0.6405 0.4406 0.5305 0.2188 0.0403 0.0408 256 ILE E C 9385 O O . ILE E 257 ? 0.6548 0.4687 0.5488 0.2368 0.0364 0.0353 256 ILE E O 9386 C CB . ILE E 257 ? 0.5692 0.4175 0.4862 0.1854 0.0341 0.0119 256 ILE E CB 9387 C CG1 . ILE E 257 ? 0.5256 0.4047 0.4521 0.1633 0.0295 0.0048 256 ILE E CG1 9388 C CG2 . ILE E 257 ? 0.5941 0.4033 0.5134 0.1806 0.0429 0.0036 256 ILE E CG2 9389 C CD1 . ILE E 257 ? 0.5054 0.4143 0.4449 0.1589 0.0256 -0.0107 256 ILE E CD1 9390 N N . VAL E 258 ? 0.6809 0.4406 0.5570 0.2207 0.0486 0.0559 257 VAL E N 9391 C CA . VAL E 258 ? 0.7348 0.4638 0.5968 0.2468 0.0527 0.0697 257 VAL E CA 9392 C C . VAL E 258 ? 0.7755 0.4549 0.6398 0.2479 0.0634 0.0641 257 VAL E C 9393 O O . VAL E 258 ? 0.8069 0.4647 0.6645 0.2723 0.0656 0.0694 257 VAL E O 9394 C CB . VAL E 258 ? 0.7575 0.4708 0.5994 0.2520 0.0563 0.0924 257 VAL E CB 9395 C CG1 . VAL E 258 ? 0.8274 0.5023 0.6522 0.2795 0.0621 0.1093 257 VAL E CG1 9396 C CG2 . VAL E 258 ? 0.7260 0.4910 0.5650 0.2560 0.0443 0.0954 257 VAL E CG2 9397 N N . LYS E 259 ? 0.7814 0.4431 0.6556 0.2225 0.0699 0.0527 258 LYS E N 9398 C CA . LYS E 259 ? 0.8327 0.4508 0.7119 0.2207 0.0794 0.0427 258 LYS E CA 9399 C C . LYS E 259 ? 0.8094 0.4426 0.7063 0.1991 0.0779 0.0187 258 LYS E C 9400 O O . LYS E 259 ? 0.7765 0.4206 0.6799 0.1748 0.0780 0.0144 258 LYS E O 9401 C CB . LYS E 259 ? 0.8843 0.4464 0.7537 0.2132 0.0933 0.0564 258 LYS E CB 9402 C CG . LYS E 259 ? 0.9429 0.4523 0.8123 0.2224 0.1034 0.0515 258 LYS E CG 9403 C CD . LYS E 259 ? 0.9928 0.4454 0.8576 0.2074 0.1190 0.0606 258 LYS E CD 9404 C CE . LYS E 259 ? 1.0427 0.4446 0.9130 0.2102 0.1289 0.0483 258 LYS E CE 9405 N NZ . LYS E 259 ? 1.0875 0.4626 0.9450 0.2447 0.1305 0.0593 258 LYS E NZ 9406 N N . LYS E 260 ? 0.8339 0.4688 0.7379 0.2098 0.0766 0.0030 259 LYS E N 9407 C CA . LYS E 260 ? 0.8348 0.4800 0.7532 0.1925 0.0761 -0.0206 259 LYS E CA 9408 C C . LYS E 260 ? 0.8825 0.4752 0.8024 0.1908 0.0870 -0.0304 259 LYS E C 9409 O O . LYS E 260 ? 0.9371 0.4898 0.8479 0.2093 0.0937 -0.0206 259 LYS E O 9410 C CB . LYS E 260 ? 0.8121 0.5035 0.7378 0.2035 0.0670 -0.0336 259 LYS E CB 9411 C CG . LYS E 260 ? 0.7697 0.5146 0.6990 0.1955 0.0570 -0.0300 259 LYS E CG 9412 C CD . LYS E 260 ? 0.7485 0.5384 0.6867 0.2022 0.0500 -0.0435 259 LYS E CD 9413 C CE . LYS E 260 ? 0.7303 0.5348 0.6779 0.1816 0.0498 -0.0619 259 LYS E CE 9414 N NZ . LYS E 260 ? 0.6982 0.5379 0.6498 0.1631 0.0438 -0.0589 259 LYS E NZ 9415 N N . GLY E 261 ? 0.8764 0.4686 0.8074 0.1687 0.0889 -0.0499 260 GLY E N 9416 C CA . GLY E 261 ? 0.9298 0.4739 0.8646 0.1628 0.0991 -0.0633 260 GLY E CA 9417 C C . GLY E 261 ? 0.9172 0.4664 0.8642 0.1325 0.1002 -0.0808 260 GLY E C 9418 O O . GLY E 261 ? 0.8761 0.4696 0.8285 0.1194 0.0920 -0.0849 260 GLY E O 9419 N N . ASP E 262 ? 0.9678 0.4716 0.9194 0.1218 0.1104 -0.0916 261 ASP E N 9420 C CA . ASP E 262 ? 0.9546 0.4625 0.9192 0.0925 0.1118 -0.1095 261 ASP E CA 9421 C C . ASP E 262 ? 0.9261 0.4394 0.8921 0.0734 0.1136 -0.0940 261 ASP E C 9422 O O . ASP E 262 ? 0.9611 0.4387 0.9203 0.0743 0.1228 -0.0751 261 ASP E O 9423 C CB . ASP E 262 ? 1.0152 0.4716 0.9862 0.0847 0.1229 -0.1266 261 ASP E CB 9424 C CG . ASP E 262 ? 1.0258 0.4973 1.0041 0.0851 0.1185 -0.1572 261 ASP E CG 9425 O OD1 . ASP E 262 ? 0.9824 0.5073 0.9629 0.0833 0.1074 -0.1662 261 ASP E OD1 9426 O OD2 . ASP E 262 ? 1.0587 0.4873 1.0398 0.0872 0.1268 -0.1722 261 ASP E OD2 9427 N N . SER E 263 ? 0.8684 0.4269 0.8423 0.0572 0.1051 -0.1017 262 SER E N 9428 C CA . SER E 263 ? 0.8379 0.4056 0.8166 0.0368 0.1067 -0.0926 262 SER E CA 9429 C C . SER E 263 ? 0.7897 0.3963 0.7817 0.0173 0.0991 -0.1127 262 SER E C 9430 O O . SER E 263 ? 0.7955 0.4173 0.7911 0.0195 0.0938 -0.1326 262 SER E O 9431 C CB . SER E 263 ? 0.8113 0.4018 0.7793 0.0473 0.1019 -0.0685 262 SER E CB 9432 O OG . SER E 263 ? 0.8041 0.4011 0.7760 0.0290 0.1047 -0.0596 262 SER E OG 9433 N N . THR E 264 ? 0.7552 0.3786 0.7537 -0.0004 0.0987 -0.1075 263 THR E N 9434 C CA . THR E 264 ? 0.7163 0.3787 0.7269 -0.0172 0.0909 -0.1241 263 THR E CA 9435 C C . THR E 264 ? 0.6873 0.3699 0.7017 -0.0296 0.0902 -0.1109 263 THR E C 9436 O O . THR E 264 ? 0.6981 0.3580 0.7079 -0.0298 0.0983 -0.0928 263 THR E O 9437 C CB . THR E 264 ? 0.7465 0.3920 0.7706 -0.0344 0.0956 -0.1488 263 THR E CB 9438 O OG1 . THR E 264 ? 0.7181 0.4071 0.7521 -0.0473 0.0860 -0.1655 263 THR E OG1 9439 C CG2 . THR E 264 ? 0.7840 0.3914 0.8161 -0.0511 0.1089 -0.1438 263 THR E CG2 9440 N N . ILE E 265 ? 0.6422 0.3677 0.6639 -0.0384 0.0806 -0.1195 264 ILE E N 9441 C CA . ILE E 265 ? 0.6163 0.3625 0.6448 -0.0514 0.0800 -0.1115 264 ILE E CA 9442 C C . ILE E 265 ? 0.6195 0.3751 0.6660 -0.0732 0.0808 -0.1306 264 ILE E C 9443 O O . ILE E 265 ? 0.6178 0.4056 0.6698 -0.0767 0.0714 -0.1463 264 ILE E O 9444 C CB . ILE E 265 ? 0.5750 0.3636 0.5984 -0.0437 0.0685 -0.1039 264 ILE E CB 9445 C CG1 . ILE E 265 ? 0.5694 0.3510 0.5774 -0.0243 0.0681 -0.0853 264 ILE E CG1 9446 C CG2 . ILE E 265 ? 0.5534 0.3635 0.5856 -0.0569 0.0678 -0.0989 264 ILE E CG2 9447 C CD1 . ILE E 265 ? 0.5367 0.3558 0.5400 -0.0169 0.0578 -0.0787 264 ILE E CD1 9448 N N . MET E 266 ? 0.6398 0.3681 0.6951 -0.0877 0.0925 -0.1289 265 MET E N 9449 C CA . MET E 266 ? 0.6344 0.3728 0.7097 -0.1106 0.0945 -0.1467 265 MET E CA 9450 C C . MET E 266 ? 0.5963 0.3723 0.6802 -0.1194 0.0904 -0.1409 265 MET E C 9451 O O . MET E 266 ? 0.5702 0.3448 0.6472 -0.1146 0.0939 -0.1204 265 MET E O 9452 C CB . MET E 266 ? 0.6755 0.3689 0.7588 -0.1246 0.1106 -0.1466 265 MET E CB 9453 C CG . MET E 266 ? 0.7162 0.3726 0.7996 -0.1239 0.1156 -0.1622 265 MET E CG 9454 S SD . MET E 266 ? 0.7617 0.3712 0.8608 -0.1480 0.1350 -0.1655 265 MET E SD 9455 C CE . MET E 266 ? 0.8037 0.3704 0.9004 -0.1422 0.1385 -0.1855 265 MET E CE 9456 N N . LYS E 267 ? 0.5844 0.3942 0.6838 -0.1319 0.0832 -0.1602 266 LYS E N 9457 C CA . LYS E 267 ? 0.5612 0.4056 0.6734 -0.1425 0.0805 -0.1585 266 LYS E CA 9458 C C . LYS E 267 ? 0.5832 0.4135 0.7157 -0.1657 0.0923 -0.1682 266 LYS E C 9459 O O . LYS E 267 ? 0.5950 0.4174 0.7391 -0.1778 0.0937 -0.1898 266 LYS E O 9460 C CB . LYS E 267 ? 0.5439 0.4365 0.6607 -0.1407 0.0651 -0.1726 266 LYS E CB 9461 C CG . LYS E 267 ? 0.5291 0.4337 0.6268 -0.1201 0.0547 -0.1662 266 LYS E CG 9462 C CD . LYS E 267 ? 0.5142 0.4188 0.5989 -0.1068 0.0546 -0.1415 266 LYS E CD 9463 C CE . LYS E 267 ? 0.4886 0.4340 0.5775 -0.1060 0.0457 -0.1377 266 LYS E CE 9464 N NZ . LYS E 267 ? 0.4654 0.4096 0.5437 -0.0954 0.0465 -0.1160 266 LYS E NZ 9465 N N . SER E 268 ? 0.5726 0.3995 0.7093 -0.1724 0.1015 -0.1527 267 SER E N 9466 C CA . SER E 268 ? 0.5968 0.4098 0.7532 -0.1955 0.1152 -0.1588 267 SER E CA 9467 C C . SER E 268 ? 0.5778 0.4092 0.7395 -0.2002 0.1206 -0.1432 267 SER E C 9468 O O . SER E 268 ? 0.5591 0.3948 0.7040 -0.1841 0.1181 -0.1234 267 SER E O 9469 C CB . SER E 268 ? 0.6430 0.3964 0.7922 -0.1978 0.1305 -0.1526 267 SER E CB 9470 O OG . SER E 268 ? 0.6756 0.4125 0.8446 -0.2223 0.1454 -0.1584 267 SER E OG 9471 N N . GLU E 269 ? 0.7013 0.5425 0.7436 -0.0545 0.1972 -0.1902 268 GLU E N 9472 C CA . GLU E 269 ? 0.7148 0.5879 0.7800 -0.0498 0.2102 -0.2211 268 GLU E CA 9473 C C . GLU E 269 ? 0.7274 0.6139 0.7769 -0.0798 0.2515 -0.2232 268 GLU E C 9474 O O . GLU E 269 ? 0.7459 0.6538 0.7985 -0.0857 0.2709 -0.2466 268 GLU E O 9475 C CB . GLU E 269 ? 0.7106 0.6280 0.8384 -0.0317 0.1951 -0.2608 268 GLU E CB 9476 C CG . GLU E 269 ? 0.7199 0.6064 0.8488 -0.0033 0.1452 -0.2600 268 GLU E CG 9477 C CD . GLU E 269 ? 0.7452 0.6015 0.8492 0.0145 0.1248 -0.2603 268 GLU E CD 9478 O OE1 . GLU E 269 ? 0.7578 0.6463 0.8967 0.0297 0.1265 -0.2971 268 GLU E OE1 9479 O OE2 . GLU E 269 ? 0.7538 0.5568 0.8050 0.0122 0.1077 -0.2272 268 GLU E OE2 9480 N N . LEU E 270 ? 0.7269 0.5936 0.7519 -0.1007 0.2628 -0.1996 269 LEU E N 9481 C CA . LEU E 270 ? 0.7569 0.6169 0.7503 -0.1345 0.2949 -0.1971 269 LEU E CA 9482 C C . LEU E 270 ? 0.7907 0.6074 0.7266 -0.1434 0.3000 -0.1806 269 LEU E C 9483 O O . LEU E 270 ? 0.7833 0.5682 0.7010 -0.1248 0.2774 -0.1605 269 LEU E O 9484 C CB . LEU E 270 ? 0.7548 0.5904 0.7313 -0.1497 0.2947 -0.1747 269 LEU E CB 9485 C CG . LEU E 270 ? 0.7310 0.6012 0.7548 -0.1463 0.2904 -0.1872 269 LEU E CG 9486 C CD1 . LEU E 270 ? 0.7375 0.5763 0.7363 -0.1627 0.2912 -0.1651 269 LEU E CD1 9487 C CD2 . LEU E 270 ? 0.7324 0.6629 0.8016 -0.1582 0.3121 -0.2267 269 LEU E CD2 9488 N N . GLU E 271 ? 0.8378 0.6516 0.7413 -0.1759 0.3297 -0.1907 270 GLU E N 9489 C CA . GLU E 271 ? 0.8855 0.6452 0.7196 -0.1923 0.3339 -0.1732 270 GLU E CA 9490 C C . GLU E 271 ? 0.9277 0.6253 0.7028 -0.2180 0.3304 -0.1440 270 GLU E C 9491 O O . GLU E 271 ? 0.9228 0.6263 0.7116 -0.2271 0.3319 -0.1417 270 GLU E O 9492 C CB . GLU E 271 ? 0.9244 0.7093 0.7452 -0.2180 0.3679 -0.2048 270 GLU E CB 9493 N N . TYR E 272 ? 0.9720 0.6051 0.6799 -0.2285 0.3212 -0.1232 271 TYR E N 9494 C CA . TYR E 272 ? 1.0167 0.5754 0.6620 -0.2486 0.3061 -0.0967 271 TYR E CA 9495 C C . TYR E 272 ? 1.0697 0.6205 0.6819 -0.2941 0.3322 -0.1056 271 TYR E C 9496 O O . TYR E 272 ? 1.0953 0.6820 0.7041 -0.3228 0.3681 -0.1315 271 TYR E O 9497 C CB . TYR E 272 ? 1.0700 0.5568 0.6429 -0.2558 0.2898 -0.0786 271 TYR E CB 9498 C CG . TYR E 272 ? 1.1305 0.5276 0.6359 -0.2710 0.2616 -0.0532 271 TYR E CG 9499 C CD1 . TYR E 272 ? 1.0944 0.4812 0.6315 -0.2450 0.2307 -0.0411 271 TYR E CD1 9500 C CD2 . TYR E 272 ? 1.2335 0.5508 0.6392 -0.3121 0.2625 -0.0440 271 TYR E CD2 9501 C CE1 . TYR E 272 ? 1.1603 0.4631 0.6423 -0.2529 0.1974 -0.0234 271 TYR E CE1 9502 C CE2 . TYR E 272 ? 1.3067 0.5274 0.6441 -0.3238 0.2259 -0.0212 271 TYR E CE2 9503 C CZ . TYR E 272 ? 1.2671 0.4823 0.6480 -0.2907 0.1911 -0.0124 271 TYR E CZ 9504 O OH . TYR E 272 ? 1.3353 0.4540 0.6565 -0.2957 0.1474 0.0046 271 TYR E OH 9505 N N . GLY E 273 ? 1.0920 0.5975 0.6807 -0.3021 0.3144 -0.0877 272 GLY E N 9506 C CA . GLY E 273 ? 1.1452 0.6397 0.7021 -0.3465 0.3356 -0.0941 272 GLY E CA 9507 C C . GLY E 273 ? 1.2559 0.6414 0.7039 -0.3863 0.3198 -0.0715 272 GLY E C 9508 O O . GLY E 273 ? 1.3132 0.6767 0.7228 -0.4279 0.3335 -0.0737 272 GLY E O 9509 N N . ASN E 274 ? 1.2976 0.6090 0.6918 -0.3755 0.2871 -0.0503 273 ASN E N 9510 C CA . ASN E 274 ? 1.4216 0.6098 0.7014 -0.4099 0.2590 -0.0275 273 ASN E CA 9511 C C . ASN E 274 ? 1.4502 0.5857 0.7159 -0.4093 0.2274 -0.0145 273 ASN E C 9512 O O . ASN E 274 ? 1.5669 0.6009 0.7310 -0.4506 0.2101 -0.0004 273 ASN E O 9513 C CB . ASN E 274 ? 1.5224 0.6768 0.7082 -0.4792 0.2965 -0.0357 273 ASN E CB 9514 C CG . ASN E 274 ? 1.5625 0.6911 0.7001 -0.4860 0.3003 -0.0349 273 ASN E CG 9515 O OD1 . ASN E 274 ? 1.4879 0.7007 0.6930 -0.4619 0.3248 -0.0543 273 ASN E OD1 9516 N ND2 . ASN E 274 ? 1.6879 0.6915 0.7025 -0.5193 0.2718 -0.0124 273 ASN E ND2 9517 N N . CYS E 275 ? 1.3538 0.5511 0.7145 -0.3641 0.2174 -0.0197 274 CYS E N 9518 C CA . CYS E 275 ? 1.3660 0.5264 0.7282 -0.3569 0.1890 -0.0129 274 CYS E CA 9519 C C . CYS E 275 ? 1.3343 0.4703 0.7313 -0.3040 0.1385 -0.0059 274 CYS E C 9520 O O . CYS E 275 ? 1.2766 0.4464 0.7142 -0.2722 0.1328 -0.0080 274 CYS E O 9521 C CB . CYS E 275 ? 1.2849 0.5401 0.7313 -0.3493 0.2193 -0.0300 274 CYS E CB 9522 S SG . CYS E 275 ? 1.1633 0.5439 0.7237 -0.3057 0.2440 -0.0484 274 CYS E SG 9523 N N . ASN E 276 ? 1.3653 0.4453 0.7489 -0.2959 0.1019 -0.0015 275 ASN E N 9524 C CA . ASN E 276 ? 1.3267 0.4058 0.7664 -0.2438 0.0584 -0.0066 275 ASN E CA 9525 C C . ASN E 276 ? 1.2540 0.3970 0.7692 -0.2246 0.0687 -0.0205 275 ASN E C 9526 O O . ASN E 276 ? 1.2740 0.4158 0.7697 -0.2539 0.0887 -0.0199 275 ASN E O 9527 C CB . ASN E 276 ? 1.4402 0.3919 0.8033 -0.2432 -0.0038 0.0036 275 ASN E CB 9528 C CG . ASN E 276 ? 1.4090 0.3672 0.8370 -0.1870 -0.0505 -0.0095 275 ASN E CG 9529 O OD1 . ASN E 276 ? 1.3285 0.3613 0.8244 -0.1596 -0.0379 -0.0185 275 ASN E OD1 9530 N ND2 . ASN E 276 ? 1.4791 0.3584 0.8870 -0.1707 -0.1064 -0.0141 275 ASN E ND2 9531 N N . THR E 277 ? 1.1771 0.3776 0.7762 -0.1797 0.0574 -0.0348 276 THR E N 9532 C CA . THR E 277 ? 1.1145 0.3750 0.7820 -0.1624 0.0675 -0.0500 276 THR E CA 9533 C C . THR E 277 ? 1.0855 0.3668 0.8172 -0.1183 0.0369 -0.0691 276 THR E C 9534 O O . THR E 277 ? 1.0828 0.3562 0.8245 -0.0982 0.0147 -0.0727 276 THR E O 9535 C CB . THR E 277 ? 1.0259 0.3838 0.7450 -0.1685 0.1169 -0.0552 276 THR E CB 9536 O OG1 . THR E 277 ? 0.9950 0.3873 0.7529 -0.1652 0.1258 -0.0654 276 THR E OG1 9537 C CG2 . THR E 277 ? 0.9537 0.3749 0.7284 -0.1418 0.1241 -0.0625 276 THR E CG2 9538 N N . LYS E 278 ? 1.0705 0.3792 0.8455 -0.1058 0.0364 -0.0848 277 LYS E N 9539 C CA . LYS E 278 ? 1.0365 0.3893 0.8856 -0.0688 0.0202 -0.1124 277 LYS E CA 9540 C C . LYS E 278 ? 0.9476 0.4013 0.8588 -0.0665 0.0620 -0.1224 277 LYS E C 9541 O O . LYS E 278 ? 0.9121 0.4161 0.8823 -0.0447 0.0598 -0.1463 277 LYS E O 9542 C CB . LYS E 278 ? 1.0800 0.3974 0.9343 -0.0581 -0.0065 -0.1278 277 LYS E CB 9543 C CG . LYS E 278 ? 1.1903 0.3970 0.9886 -0.0510 -0.0646 -0.1253 277 LYS E CG 9544 C CD . LYS E 278 ? 1.2005 0.4056 1.0450 -0.0106 -0.1074 -0.1508 277 LYS E CD 9545 C CE . LYS E 278 ? 1.2672 0.4164 1.1254 0.0194 -0.1640 -0.1781 277 LYS E CE 9546 N NZ . LYS E 278 ? 1.3875 0.4003 1.1418 0.0009 -0.2088 -0.1552 277 LYS E NZ 9547 N N . CYS E 279 ? 0.9246 0.4052 0.8203 -0.0910 0.0978 -0.1072 278 CYS E N 9548 C CA . CYS E 279 ? 0.8590 0.4162 0.7992 -0.0918 0.1294 -0.1147 278 CYS E CA 9549 C C . CYS E 279 ? 0.8296 0.4102 0.7535 -0.1105 0.1570 -0.0994 278 CYS E C 9550 O O . CYS E 279 ? 0.8440 0.4127 0.7425 -0.1316 0.1700 -0.0912 278 CYS E O 9551 C CB . CYS E 279 ? 0.8657 0.4339 0.8216 -0.0954 0.1353 -0.1247 278 CYS E CB 9552 S SG . CYS E 279 ? 0.8099 0.4532 0.8060 -0.0998 0.1657 -0.1342 278 CYS E SG 9553 N N . GLN E 280 ? 0.7846 0.4002 0.7258 -0.1032 0.1648 -0.0998 279 GLN E N 9554 C CA . GLN E 280 ? 0.7585 0.3985 0.6923 -0.1141 0.1853 -0.0914 279 GLN E CA 9555 C C . GLN E 280 ? 0.7092 0.3990 0.6747 -0.1117 0.1974 -0.0992 279 GLN E C 9556 O O . GLN E 280 ? 0.6871 0.3969 0.6728 -0.1032 0.1934 -0.1077 279 GLN E O 9557 C CB . GLN E 280 ? 0.7650 0.3945 0.6826 -0.1089 0.1800 -0.0842 279 GLN E CB 9558 C CG . GLN E 280 ? 0.8131 0.4013 0.6820 -0.1252 0.1826 -0.0725 279 GLN E CG 9559 C CD . GLN E 280 ? 0.8061 0.4179 0.6701 -0.1448 0.2091 -0.0744 279 GLN E CD 9560 O OE1 . GLN E 280 ? 0.8621 0.4438 0.6858 -0.1677 0.2174 -0.0705 279 GLN E OE1 9561 N NE2 . GLN E 280 ? 0.7562 0.4194 0.6588 -0.1380 0.2202 -0.0834 279 GLN E NE2 9562 N N . THR E 281 ? 0.6935 0.4012 0.6607 -0.1217 0.2107 -0.0986 280 THR E N 9563 C CA . THR E 281 ? 0.6641 0.4041 0.6489 -0.1192 0.2137 -0.1037 280 THR E CA 9564 C C . THR E 281 ? 0.6648 0.4122 0.6438 -0.1177 0.2170 -0.1018 280 THR E C 9565 O O . THR E 281 ? 0.6856 0.4202 0.6488 -0.1239 0.2240 -0.0988 280 THR E O 9566 C CB . THR E 281 ? 0.6535 0.4084 0.6528 -0.1266 0.2178 -0.1106 280 THR E CB 9567 O OG1 . THR E 281 ? 0.6511 0.4189 0.6563 -0.1336 0.2262 -0.1143 280 THR E OG1 9568 C CG2 . THR E 281 ? 0.6674 0.4063 0.6662 -0.1308 0.2170 -0.1127 280 THR E CG2 9569 N N . PRO E 282 ? 0.6511 0.4138 0.6373 -0.1115 0.2102 -0.1054 281 PRO E N 9570 C CA . PRO E 282 ? 0.6549 0.4236 0.6395 -0.1057 0.2093 -0.1084 281 PRO E CA 9571 C C . PRO E 282 ? 0.6607 0.4518 0.6647 -0.1107 0.2206 -0.1223 281 PRO E C 9572 O O . PRO E 282 ? 0.6646 0.4669 0.6722 -0.1075 0.2251 -0.1314 281 PRO E O 9573 C CB . PRO E 282 ? 0.6488 0.4172 0.6312 -0.0985 0.1913 -0.1102 281 PRO E CB 9574 C CG . PRO E 282 ? 0.6480 0.4093 0.6221 -0.1064 0.1884 -0.1060 281 PRO E CG 9575 C CD . PRO E 282 ? 0.6413 0.4087 0.6294 -0.1121 0.2004 -0.1083 281 PRO E CD 9576 N N . ILE E 283 ? 0.6624 0.4638 0.6810 -0.1202 0.2264 -0.1275 282 ILE E N 9577 C CA . ILE E 283 ? 0.6699 0.5025 0.7155 -0.1285 0.2380 -0.1462 282 ILE E CA 9578 C C . ILE E 283 ? 0.6942 0.5179 0.7227 -0.1532 0.2593 -0.1438 282 ILE E C 9579 O O . ILE E 283 ? 0.7050 0.5556 0.7474 -0.1696 0.2773 -0.1611 282 ILE E O 9580 C CB . ILE E 283 ? 0.6624 0.5129 0.7379 -0.1220 0.2226 -0.1571 282 ILE E CB 9581 C CG1 . ILE E 283 ? 0.6669 0.5571 0.7850 -0.1134 0.2176 -0.1852 282 ILE E CG1 9582 C CG2 . ILE E 283 ? 0.6625 0.5089 0.7384 -0.1368 0.2295 -0.1536 282 ILE E CG2 9583 C CD1 . ILE E 283 ? 0.6701 0.5557 0.8027 -0.0948 0.1833 -0.1927 282 ILE E CD1 9584 N N . GLY E 284 ? 0.7131 0.4967 0.7095 -0.1577 0.2556 -0.1255 283 GLY E N 9585 C CA . GLY E 284 ? 0.7580 0.5103 0.7202 -0.1818 0.2663 -0.1192 283 GLY E CA 9586 C C . GLY E 284 ? 0.7761 0.4800 0.7110 -0.1763 0.2494 -0.1032 283 GLY E C 9587 O O . GLY E 284 ? 0.7412 0.4503 0.6948 -0.1574 0.2361 -0.1021 283 GLY E O 9588 N N . ALA E 285 ? 0.8454 0.4997 0.7334 -0.1948 0.2484 -0.0941 284 ALA E N 9589 C CA . ALA E 285 ? 0.8841 0.4846 0.7471 -0.1877 0.2246 -0.0840 284 ALA E CA 9590 C C . ALA E 285 ? 0.8979 0.4885 0.7634 -0.1975 0.2222 -0.0872 284 ALA E C 9591 O O . ALA E 285 ? 0.9055 0.5212 0.7787 -0.2179 0.2407 -0.0938 284 ALA E O 9592 C CB . ALA E 285 ? 0.9557 0.4897 0.7552 -0.2034 0.2146 -0.0719 284 ALA E CB 9593 N N . ILE E 286 ? 0.9154 0.4722 0.7785 -0.1822 0.1983 -0.0864 285 ILE E N 9594 C CA . ILE E 286 ? 0.9285 0.4743 0.7964 -0.1866 0.1925 -0.0914 285 ILE E CA 9595 C C . ILE E 286 ? 1.0013 0.4683 0.8254 -0.1866 0.1617 -0.0865 285 ILE E C 9596 O O . ILE E 286 ? 1.0175 0.4599 0.8429 -0.1632 0.1369 -0.0889 285 ILE E O 9597 C CB . ILE E 286 ? 0.8763 0.4685 0.7970 -0.1627 0.1917 -0.1044 285 ILE E CB 9598 C CG1 . ILE E 286 ? 0.8281 0.4810 0.7809 -0.1653 0.2128 -0.1085 285 ILE E CG1 9599 C CG2 . ILE E 286 ? 0.8930 0.4662 0.8155 -0.1637 0.1818 -0.1117 285 ILE E CG2 9600 C CD1 . ILE E 286 ? 0.7913 0.4784 0.7772 -0.1483 0.2109 -0.1184 285 ILE E CD1 9601 N N . ASN E 287 ? 1.0522 0.4776 0.8379 -0.2129 0.1597 -0.0820 286 ASN E N 9602 C CA . ASN E 287 ? 1.1385 0.4738 0.8720 -0.2155 0.1234 -0.0773 286 ASN E CA 9603 C C . ASN E 287 ? 1.1445 0.4772 0.8905 -0.2173 0.1190 -0.0855 286 ASN E C 9604 O O . ASN E 287 ? 1.1673 0.4891 0.8839 -0.2524 0.1339 -0.0797 286 ASN E O 9605 C CB . ASN E 287 ? 1.2297 0.4914 0.8755 -0.2576 0.1216 -0.0598 286 ASN E CB 9606 C CG . ASN E 287 ? 1.3435 0.4901 0.9169 -0.2645 0.0751 -0.0521 286 ASN E CG 9607 O OD1 . ASN E 287 ? 1.3629 0.4722 0.9463 -0.2279 0.0337 -0.0588 286 ASN E OD1 9608 N ND2 . ASN E 287 ? 1.4247 0.5124 0.9240 -0.3131 0.0791 -0.0409 286 ASN E ND2 9609 N N . SER E 288 ? 1.1209 0.4679 0.9122 -0.1817 0.1007 -0.1022 287 SER E N 9610 C CA . SER E 288 ? 1.1159 0.4739 0.9291 -0.1790 0.1005 -0.1141 287 SER E CA 9611 C C . SER E 288 ? 1.1332 0.4719 0.9735 -0.1422 0.0673 -0.1364 287 SER E C 9612 O O . SER E 288 ? 1.1120 0.4671 0.9839 -0.1137 0.0550 -0.1492 287 SER E O 9613 C CB . SER E 288 ? 1.0339 0.4822 0.9017 -0.1791 0.1363 -0.1208 287 SER E CB 9614 O OG . SER E 288 ? 1.0240 0.4820 0.9103 -0.1771 0.1358 -0.1326 287 SER E OG 9615 N N . SER E 289 ? 1.1718 0.4795 1.0038 -0.1435 0.0531 -0.1449 288 SER E N 9616 C CA . SER E 289 ? 1.1827 0.4855 1.0520 -0.1078 0.0258 -0.1750 288 SER E CA 9617 C C . SER E 289 ? 1.1230 0.4967 1.0418 -0.1047 0.0541 -0.1929 288 SER E C 9618 O O . SER E 289 ? 1.1236 0.5022 1.0743 -0.0809 0.0396 -0.2224 288 SER E O 9619 C CB . SER E 289 ? 1.2906 0.4879 1.1054 -0.1076 -0.0216 -0.1750 288 SER E CB 9620 O OG . SER E 289 ? 1.3237 0.4893 1.0904 -0.1453 -0.0107 -0.1566 288 SER E OG 9621 N N . MET E 290 ? 1.0753 0.5018 0.9997 -0.1284 0.0919 -0.1782 289 MET E N 9622 C CA . MET E 290 ? 1.0290 0.5146 0.9889 -0.1298 0.1160 -0.1915 289 MET E CA 9623 C C . MET E 290 ? 0.9762 0.5210 0.9850 -0.1077 0.1267 -0.2156 289 MET E C 9624 O O . MET E 290 ? 0.9644 0.5259 0.9836 -0.0992 0.1282 -0.2127 289 MET E O 9625 C CB . MET E 290 ? 0.9976 0.5193 0.9522 -0.1574 0.1448 -0.1716 289 MET E CB 9626 C CG . MET E 290 ? 1.0435 0.5263 0.9579 -0.1878 0.1439 -0.1536 289 MET E CG 9627 S SD . MET E 290 ? 1.0770 0.5427 0.9858 -0.1986 0.1386 -0.1622 289 MET E SD 9628 C CE . MET E 290 ? 1.1009 0.5567 0.9776 -0.2434 0.1522 -0.1421 289 MET E CE 9629 N N . PRO E 291 ? 0.9517 0.5275 0.9861 -0.1029 0.1357 -0.2408 290 PRO E N 9630 C CA . PRO E 291 ? 0.9052 0.5404 0.9789 -0.0929 0.1523 -0.2671 290 PRO E CA 9631 C C . PRO E 291 ? 0.8509 0.5301 0.9202 -0.1122 0.1799 -0.2508 290 PRO E C 9632 O O . PRO E 291 ? 0.8301 0.5472 0.9193 -0.1086 0.1907 -0.2630 290 PRO E O 9633 C CB . PRO E 291 ? 0.9241 0.5712 1.0134 -0.0905 0.1560 -0.2992 290 PRO E CB 9634 C CG . PRO E 291 ? 0.9518 0.5554 1.0064 -0.1052 0.1487 -0.2800 290 PRO E CG 9635 C CD . PRO E 291 ? 0.9800 0.5313 1.0035 -0.1084 0.1294 -0.2496 290 PRO E CD 9636 N N . PHE E 292 ? 0.8286 0.5007 0.8729 -0.1324 0.1878 -0.2263 291 PHE E N 9637 C CA . PHE E 292 ? 0.7811 0.4836 0.8187 -0.1475 0.2042 -0.2127 291 PHE E CA 9638 C C . PHE E 292 ? 0.7622 0.4553 0.7877 -0.1546 0.2026 -0.1856 291 PHE E C 9639 O O . PHE E 292 ? 0.7789 0.4433 0.7926 -0.1599 0.1952 -0.1756 291 PHE E O 9640 C CB . PHE E 292 ? 0.7848 0.4946 0.8101 -0.1647 0.2119 -0.2174 291 PHE E CB 9641 C CG . PHE E 292 ? 0.7972 0.5199 0.8282 -0.1654 0.2198 -0.2478 291 PHE E CG 9642 C CD1 . PHE E 292 ? 0.7890 0.5427 0.8192 -0.1747 0.2355 -0.2630 291 PHE E CD1 9643 C CD2 . PHE E 292 ? 0.8241 0.5277 0.8585 -0.1604 0.2129 -0.2641 291 PHE E CD2 9644 C CE1 . PHE E 292 ? 0.8091 0.5824 0.8448 -0.1817 0.2489 -0.2975 291 PHE E CE1 9645 C CE2 . PHE E 292 ? 0.8400 0.5616 0.8837 -0.1615 0.2230 -0.2988 291 PHE E CE2 9646 C CZ . PHE E 292 ? 0.8330 0.5933 0.8788 -0.1735 0.2435 -0.3173 291 PHE E CZ 9647 N N . HIS E 293 ? 0.7255 0.4426 0.7516 -0.1578 0.2100 -0.1769 292 HIS E N 9648 C CA . HIS E 293 ? 0.7103 0.4309 0.7332 -0.1646 0.2110 -0.1594 292 HIS E CA 9649 C C . HIS E 293 ? 0.6837 0.4261 0.7060 -0.1697 0.2121 -0.1580 292 HIS E C 9650 O O . HIS E 293 ? 0.6844 0.4321 0.6977 -0.1721 0.2135 -0.1660 292 HIS E O 9651 C CB . HIS E 293 ? 0.7108 0.4240 0.7310 -0.1566 0.2102 -0.1504 292 HIS E CB 9652 C CG . HIS E 293 ? 0.6927 0.4246 0.7185 -0.1471 0.2124 -0.1527 292 HIS E CG 9653 N ND1 . HIS E 293 ? 0.6749 0.4216 0.6990 -0.1478 0.2151 -0.1435 292 HIS E ND1 9654 C CD2 . HIS E 293 ? 0.6897 0.4304 0.7244 -0.1385 0.2122 -0.1667 292 HIS E CD2 9655 C CE1 . HIS E 293 ? 0.6648 0.4216 0.6891 -0.1420 0.2156 -0.1472 292 HIS E CE1 9656 N NE2 . HIS E 293 ? 0.6738 0.4315 0.7068 -0.1379 0.2158 -0.1624 292 HIS E NE2 9657 N N . ASN E 294 ? 0.6681 0.4208 0.6978 -0.1732 0.2095 -0.1510 293 ASN E N 9658 C CA . ASN E 294 ? 0.6629 0.4258 0.6910 -0.1740 0.1998 -0.1516 293 ASN E CA 9659 C C . ASN E 294 ? 0.6438 0.4228 0.6860 -0.1664 0.1977 -0.1480 293 ASN E C 9660 O O . ASN E 294 ? 0.6387 0.4278 0.6929 -0.1642 0.1844 -0.1531 293 ASN E O 9661 C CB . ASN E 294 ? 0.6757 0.4364 0.7072 -0.1828 0.1889 -0.1572 293 ASN E CB 9662 C CG . ASN E 294 ? 0.6738 0.4521 0.7340 -0.1866 0.1910 -0.1601 293 ASN E CG 9663 O OD1 . ASN E 294 ? 0.6617 0.4507 0.7321 -0.1867 0.2030 -0.1575 293 ASN E OD1 9664 N ND2 . ASN E 294 ? 0.6905 0.4714 0.7609 -0.1939 0.1800 -0.1674 293 ASN E ND2 9665 N N . ILE E 295 ? 0.6339 0.4127 0.6747 -0.1610 0.2078 -0.1421 294 ILE E N 9666 C CA . ILE E 295 ? 0.6266 0.4199 0.6781 -0.1561 0.2107 -0.1407 294 ILE E CA 9667 C C . ILE E 295 ? 0.6203 0.4141 0.6640 -0.1459 0.1993 -0.1392 294 ILE E C 9668 O O . ILE E 295 ? 0.6229 0.4278 0.6797 -0.1402 0.1867 -0.1460 294 ILE E O 9669 C CB . ILE E 295 ? 0.6344 0.4145 0.6742 -0.1579 0.2227 -0.1332 294 ILE E CB 9670 C CG1 . ILE E 295 ? 0.6589 0.4211 0.6910 -0.1718 0.2282 -0.1326 294 ILE E CG1 9671 C CG2 . ILE E 295 ? 0.6294 0.4241 0.6743 -0.1574 0.2295 -0.1339 294 ILE E CG2 9672 C CD1 . ILE E 295 ? 0.6632 0.4464 0.7128 -0.1876 0.2345 -0.1412 294 ILE E CD1 9673 N N . HIS E 296 ? 0.6147 0.3955 0.6385 -0.1441 0.2011 -0.1333 295 HIS E N 9674 C CA . HIS E 296 ? 0.6181 0.3928 0.6247 -0.1405 0.1912 -0.1302 295 HIS E CA 9675 C C . HIS E 296 ? 0.6268 0.3938 0.6137 -0.1490 0.1965 -0.1313 295 HIS E C 9676 O O . HIS E 296 ? 0.6199 0.3917 0.6174 -0.1476 0.2076 -0.1354 295 HIS E O 9677 C CB . HIS E 296 ? 0.6060 0.3862 0.6176 -0.1304 0.1946 -0.1256 295 HIS E CB 9678 C CG . HIS E 296 ? 0.6140 0.3872 0.6134 -0.1241 0.1783 -0.1248 295 HIS E CG 9679 N ND1 . HIS E 296 ? 0.6243 0.3830 0.5973 -0.1269 0.1743 -0.1184 295 HIS E ND1 9680 C CD2 . HIS E 296 ? 0.6215 0.3983 0.6321 -0.1149 0.1616 -0.1326 295 HIS E CD2 9681 C CE1 . HIS E 296 ? 0.6385 0.3833 0.5978 -0.1212 0.1547 -0.1182 295 HIS E CE1 9682 N NE2 . HIS E 296 ? 0.6402 0.3954 0.6244 -0.1110 0.1445 -0.1282 295 HIS E NE2 9683 N N . PRO E 297 ? 0.6468 0.4002 0.6035 -0.1598 0.1869 -0.1312 296 PRO E N 9684 C CA . PRO E 297 ? 0.6606 0.4158 0.5989 -0.1753 0.1977 -0.1383 296 PRO E CA 9685 C C . PRO E 297 ? 0.6487 0.4196 0.6008 -0.1680 0.2071 -0.1394 296 PRO E C 9686 O O . PRO E 297 ? 0.6517 0.4404 0.6156 -0.1733 0.2197 -0.1536 296 PRO E O 9687 C CB . PRO E 297 ? 0.7006 0.4260 0.5884 -0.1955 0.1822 -0.1350 296 PRO E CB 9688 C CG . PRO E 297 ? 0.7035 0.4118 0.5914 -0.1798 0.1578 -0.1256 296 PRO E CG 9689 C CD . PRO E 297 ? 0.6727 0.4040 0.6070 -0.1618 0.1629 -0.1284 296 PRO E CD 9690 N N . LEU E 298 ? 0.6451 0.4111 0.5984 -0.1555 0.1995 -0.1283 297 LEU E N 9691 C CA . LEU E 298 ? 0.6404 0.4153 0.6012 -0.1496 0.2038 -0.1280 297 LEU E CA 9692 C C . LEU E 298 ? 0.6277 0.4064 0.6161 -0.1318 0.2070 -0.1267 297 LEU E C 9693 O O . LEU E 298 ? 0.6354 0.4051 0.6244 -0.1236 0.2043 -0.1174 297 LEU E O 9694 C CB . LEU E 298 ? 0.6470 0.4063 0.5844 -0.1482 0.1915 -0.1168 297 LEU E CB 9695 C CG . LEU E 298 ? 0.6829 0.4175 0.5772 -0.1671 0.1779 -0.1148 297 LEU E CG 9696 C CD1 . LEU E 298 ? 0.7014 0.4126 0.5697 -0.1636 0.1603 -0.1051 297 LEU E CD1 9697 C CD2 . LEU E 298 ? 0.7026 0.4429 0.5760 -0.1957 0.1903 -0.1261 297 LEU E CD2 9698 N N . THR E 299 ? 0.6299 0.4192 0.6387 -0.1280 0.2110 -0.1394 298 THR E N 9699 C CA . THR E 299 ? 0.6361 0.4115 0.6588 -0.1125 0.2048 -0.1378 298 THR E CA 9700 C C . THR E 299 ? 0.6406 0.4236 0.6824 -0.1026 0.1975 -0.1500 298 THR E C 9701 O O . THR E 299 ? 0.6359 0.4471 0.6895 -0.1104 0.2036 -0.1652 298 THR E O 9702 C CB . THR E 299 ? 0.6423 0.4093 0.6745 -0.1112 0.2048 -0.1446 298 THR E CB 9703 O OG1 . THR E 299 ? 0.6385 0.4249 0.6945 -0.1099 0.2065 -0.1686 298 THR E OG1 9704 C CG2 . THR E 299 ? 0.6403 0.4080 0.6613 -0.1226 0.2111 -0.1381 298 THR E CG2 9705 N N . ILE E 300 ? 0.6605 0.4156 0.7021 -0.0885 0.1830 -0.1451 299 ILE E N 9706 C CA . ILE E 300 ? 0.6783 0.4336 0.7431 -0.0736 0.1664 -0.1600 299 ILE E CA 9707 C C . ILE E 300 ? 0.7216 0.4355 0.7859 -0.0592 0.1441 -0.1633 299 ILE E C 9708 O O . ILE E 300 ? 0.7515 0.4271 0.7817 -0.0658 0.1431 -0.1448 299 ILE E O 9709 C CB . ILE E 300 ? 0.6766 0.4225 0.7263 -0.0712 0.1596 -0.1471 299 ILE E CB 9710 C CG1 . ILE E 300 ? 0.6860 0.4389 0.7682 -0.0553 0.1393 -0.1674 299 ILE E CG1 9711 C CG2 . ILE E 300 ? 0.6979 0.3974 0.7056 -0.0722 0.1547 -0.1218 299 ILE E CG2 9712 C CD1 . ILE E 300 ? 0.6874 0.4335 0.7569 -0.0541 0.1315 -0.1570 299 ILE E CD1 9713 N N . GLY E 301 ? 0.7457 0.4663 0.8474 -0.0413 0.1244 -0.1900 300 GLY E N 9714 C CA . GLY E 301 ? 0.8041 0.4716 0.9016 -0.0235 0.0908 -0.1959 300 GLY E CA 9715 C C . GLY E 301 ? 0.8205 0.4959 0.9416 -0.0186 0.0902 -0.2176 300 GLY E C 9716 O O . GLY E 301 ? 0.7937 0.5231 0.9410 -0.0284 0.1170 -0.2332 300 GLY E O 9717 N N . GLU E 302 ? 0.8839 0.4978 0.9880 -0.0058 0.0574 -0.2189 301 GLU E N 9718 C CA . GLU E 302 ? 0.9049 0.5140 1.0235 -0.0006 0.0527 -0.2375 301 GLU E CA 9719 C C . GLU E 302 ? 0.8884 0.4946 0.9694 -0.0279 0.0825 -0.2122 301 GLU E C 9720 O O . GLU E 302 ? 0.9180 0.4665 0.9453 -0.0417 0.0755 -0.1853 301 GLU E O 9721 C CB . GLU E 302 ? 0.9874 0.5158 1.0878 0.0202 0.0010 -0.2443 301 GLU E CB 9722 C CG . GLU E 302 ? 1.0063 0.5503 1.1713 0.0569 -0.0354 -0.2896 301 GLU E CG 9723 N N . CYS E 303 ? 0.8420 0.5094 0.9493 -0.0386 0.1146 -0.2234 302 CYS E N 9724 C CA . CYS E 303 ? 0.8212 0.4943 0.9016 -0.0625 0.1402 -0.2033 302 CYS E CA 9725 C C . CYS E 303 ? 0.8077 0.5030 0.9088 -0.0645 0.1494 -0.2256 302 CYS E C 9726 O O . CYS E 303 ? 0.8001 0.5267 0.9422 -0.0516 0.1472 -0.2601 302 CYS E O 9727 C CB . CYS E 303 ? 0.7821 0.4964 0.8590 -0.0777 0.1663 -0.1905 302 CYS E CB 9728 S SG . CYS E 303 ? 0.8045 0.4964 0.8523 -0.0791 0.1617 -0.1634 302 CYS E SG 9729 N N . PRO E 304 ? 0.8050 0.4885 0.8806 -0.0821 0.1608 -0.2096 303 PRO E N 9730 C CA . PRO E 304 ? 0.7974 0.5042 0.8856 -0.0890 0.1735 -0.2275 303 PRO E CA 9731 C C . PRO E 304 ? 0.7620 0.5184 0.8552 -0.1053 0.1995 -0.2322 303 PRO E C 9732 O O . PRO E 304 ? 0.7302 0.5000 0.8160 -0.1106 0.2061 -0.2186 303 PRO E O 9733 C CB . PRO E 304 ? 0.8140 0.4872 0.8699 -0.1043 0.1734 -0.2057 303 PRO E CB 9734 C CG . PRO E 304 ? 0.8264 0.4677 0.8534 -0.1103 0.1671 -0.1786 303 PRO E CG 9735 C CD . PRO E 304 ? 0.8105 0.4645 0.8471 -0.0989 0.1644 -0.1781 303 PRO E CD 9736 N N . LYS E 305 ? 0.7645 0.5392 0.8615 -0.1158 0.2117 -0.2508 304 LYS E N 9737 C CA . LYS E 305 ? 0.7505 0.5563 0.8345 -0.1388 0.2328 -0.2552 304 LYS E CA 9738 C C . LYS E 305 ? 0.7331 0.5204 0.7812 -0.1553 0.2336 -0.2257 304 LYS E C 9739 O O . LYS E 305 ? 0.7366 0.5027 0.7760 -0.1571 0.2277 -0.2169 304 LYS E O 9740 C CB . LYS E 305 ? 0.7750 0.6042 0.8699 -0.1482 0.2463 -0.2907 304 LYS E CB 9741 C CG . LYS E 305 ? 0.7867 0.6495 0.9315 -0.1307 0.2462 -0.3320 304 LYS E CG 9742 C CD . LYS E 305 ? 0.7797 0.6750 0.9388 -0.1335 0.2533 -0.3366 304 LYS E CD 9743 C CE . LYS E 305 ? 0.7902 0.7377 1.0070 -0.1237 0.2594 -0.3893 304 LYS E CE 9744 N NZ . LYS E 305 ? 0.7801 0.7645 1.0103 -0.1329 0.2693 -0.3960 304 LYS E NZ 9745 N N . TYR E 306 ? 0.7131 0.5077 0.7426 -0.1665 0.2377 -0.2133 305 TYR E N 9746 C CA . TYR E 306 ? 0.7098 0.4877 0.7121 -0.1770 0.2311 -0.1914 305 TYR E CA 9747 C C . TYR E 306 ? 0.7387 0.5073 0.7114 -0.1990 0.2330 -0.1981 305 TYR E C 9748 O O . TYR E 306 ? 0.7572 0.5347 0.7120 -0.2175 0.2450 -0.2151 305 TYR E O 9749 C CB . TYR E 306 ? 0.6950 0.4749 0.6832 -0.1793 0.2279 -0.1786 305 TYR E CB 9750 C CG . TYR E 306 ? 0.6962 0.4580 0.6626 -0.1846 0.2138 -0.1625 305 TYR E CG 9751 C CD1 . TYR E 306 ? 0.6789 0.4399 0.6639 -0.1712 0.2059 -0.1512 305 TYR E CD1 9752 C CD2 . TYR E 306 ? 0.7229 0.4663 0.6489 -0.2048 0.2060 -0.1626 305 TYR E CD2 9753 C CE1 . TYR E 306 ? 0.6839 0.4373 0.6630 -0.1716 0.1899 -0.1454 305 TYR E CE1 9754 C CE2 . TYR E 306 ? 0.7354 0.4563 0.6447 -0.2044 0.1832 -0.1518 305 TYR E CE2 9755 C CZ . TYR E 306 ? 0.7105 0.4418 0.6542 -0.1847 0.1748 -0.1458 305 TYR E CZ 9756 O OH . TYR E 306 ? 0.7224 0.4400 0.6632 -0.1802 0.1494 -0.1437 305 TYR E OH 9757 N N . VAL E 307 ? 0.7414 0.4920 0.7070 -0.2004 0.2212 -0.1866 306 VAL E N 9758 C CA . VAL E 307 ? 0.7739 0.5039 0.7033 -0.2208 0.2135 -0.1875 306 VAL E CA 9759 C C . VAL E 307 ? 0.7811 0.4965 0.7073 -0.2164 0.1907 -0.1711 306 VAL E C 9760 O O . VAL E 307 ? 0.7543 0.4836 0.7126 -0.1995 0.1879 -0.1632 306 VAL E O 9761 C CB . VAL E 307 ? 0.7877 0.5117 0.7186 -0.2261 0.2178 -0.2002 306 VAL E CB 9762 C CG1 . VAL E 307 ? 0.7933 0.5356 0.7301 -0.2305 0.2383 -0.2262 306 VAL E CG1 9763 C CG2 . VAL E 307 ? 0.7675 0.4918 0.7317 -0.2093 0.2118 -0.1930 306 VAL E CG2 9764 N N . LYS E 308 ? 0.8272 0.5129 0.7134 -0.2326 0.1727 -0.1694 307 LYS E N 9765 C CA . LYS E 308 ? 0.8389 0.5100 0.7289 -0.2246 0.1426 -0.1614 307 LYS E CA 9766 C C . LYS E 308 ? 0.8436 0.5153 0.7549 -0.2229 0.1331 -0.1657 307 LYS E C 9767 O O . LYS E 308 ? 0.8544 0.5192 0.7774 -0.2165 0.1055 -0.1662 307 LYS E O 9768 C CB . LYS E 308 ? 0.8920 0.5163 0.7211 -0.2415 0.1160 -0.1573 307 LYS E CB 9769 C CG . LYS E 308 ? 0.9002 0.5187 0.7057 -0.2447 0.1184 -0.1514 307 LYS E CG 9770 C CD . LYS E 308 ? 0.9762 0.5324 0.7117 -0.2626 0.0819 -0.1451 307 LYS E CD 9771 C CE . LYS E 308 ? 0.9941 0.5365 0.6941 -0.2728 0.0841 -0.1387 307 LYS E CE 9772 N NZ . LYS E 308 ? 1.0883 0.5527 0.6973 -0.3009 0.0476 -0.1317 307 LYS E NZ 9773 N N . SER E 309 ? 0.8417 0.5219 0.7612 -0.2277 0.1528 -0.1719 308 SER E N 9774 C CA . SER E 309 ? 0.8548 0.5322 0.7892 -0.2298 0.1445 -0.1756 308 SER E CA 9775 C C . SER E 309 ? 0.8289 0.5359 0.8154 -0.2159 0.1409 -0.1740 308 SER E C 9776 O O . SER E 309 ? 0.7958 0.5252 0.8059 -0.2066 0.1574 -0.1707 308 SER E O 9777 C CB . SER E 309 ? 0.8562 0.5335 0.7886 -0.2355 0.1651 -0.1838 308 SER E CB 9778 O OG . SER E 309 ? 0.8883 0.5513 0.7800 -0.2506 0.1759 -0.1932 308 SER E OG 9779 N N . SER E 310 ? 0.8510 0.5585 0.8541 -0.2172 0.1191 -0.1794 309 SER E N 9780 C CA . SER E 310 ? 0.8337 0.5784 0.8906 -0.2122 0.1217 -0.1859 309 SER E CA 9781 C C . SER E 310 ? 0.8356 0.5825 0.8975 -0.2234 0.1423 -0.1852 309 SER E C 9782 O O . SER E 310 ? 0.8258 0.5974 0.9159 -0.2269 0.1565 -0.1868 309 SER E O 9783 C CB . SER E 310 ? 0.8527 0.6038 0.9354 -0.2094 0.0887 -0.1988 309 SER E CB 9784 O OG . SER E 310 ? 0.8917 0.6097 0.9459 -0.2213 0.0724 -0.1996 309 SER E OG 9785 N N . ARG E 311 ? 0.8622 0.5786 0.8906 -0.2318 0.1433 -0.1842 310 ARG E N 9786 C CA . ARG E 311 ? 0.8783 0.5860 0.9068 -0.2414 0.1539 -0.1855 310 ARG E CA 9787 C C . ARG E 311 ? 0.8898 0.5674 0.8826 -0.2430 0.1615 -0.1883 310 ARG E C 9788 O O . ARG E 311 ? 0.9067 0.5674 0.8700 -0.2481 0.1551 -0.1929 310 ARG E O 9789 C CB . ARG E 311 ? 0.9064 0.6187 0.9527 -0.2527 0.1378 -0.1925 310 ARG E CB 9790 C CG . ARG E 311 ? 0.9361 0.6294 0.9725 -0.2662 0.1439 -0.1934 310 ARG E CG 9791 C CD . ARG E 311 ? 0.9598 0.6659 1.0211 -0.2795 0.1286 -0.2017 310 ARG E CD 9792 N NE . ARG E 311 ? 0.9979 0.6762 1.0400 -0.2943 0.1304 -0.2018 310 ARG E NE 9793 C CZ . ARG E 311 ? 1.0202 0.6904 1.0587 -0.3066 0.1443 -0.1980 310 ARG E CZ 9794 N NH1 . ARG E 311 ? 1.0155 0.7034 1.0653 -0.3086 0.1600 -0.1934 310 ARG E NH1 9795 N NH2 . ARG E 311 ? 1.0594 0.6955 1.0748 -0.3194 0.1400 -0.1985 310 ARG E NH2 9796 N N . LEU E 312 ? 0.8901 0.5578 0.8830 -0.2406 0.1731 -0.1888 311 LEU E N 9797 C CA . LEU E 312 ? 0.9074 0.5548 0.8802 -0.2361 0.1795 -0.1999 311 LEU E CA 9798 C C . LEU E 312 ? 0.9325 0.5539 0.9040 -0.2359 0.1772 -0.2020 311 LEU E C 9799 O O . LEU E 312 ? 0.9349 0.5476 0.9107 -0.2281 0.1785 -0.1972 311 LEU E O 9800 C CB . LEU E 312 ? 0.8894 0.5502 0.8646 -0.2228 0.1905 -0.2034 311 LEU E CB 9801 C CG . LEU E 312 ? 0.9029 0.5653 0.8607 -0.2245 0.2000 -0.2223 311 LEU E CG 9802 C CD1 . LEU E 312 ? 0.9156 0.5743 0.8428 -0.2426 0.1960 -0.2204 311 LEU E CD1 9803 C CD2 . LEU E 312 ? 0.8826 0.5645 0.8551 -0.2108 0.2107 -0.2294 311 LEU E CD2 9804 N N . VAL E 313 ? 0.9560 0.5564 0.9143 -0.2459 0.1699 -0.2086 312 VAL E N 9805 C CA . VAL E 313 ? 0.9838 0.5491 0.9326 -0.2488 0.1623 -0.2100 312 VAL E CA 9806 C C . VAL E 313 ? 1.0158 0.5562 0.9479 -0.2442 0.1584 -0.2300 312 VAL E C 9807 O O . VAL E 313 ? 1.0173 0.5590 0.9373 -0.2548 0.1580 -0.2365 312 VAL E O 9808 C CB . VAL E 313 ? 0.9967 0.5592 0.9477 -0.2712 0.1558 -0.1991 312 VAL E CB 9809 C CG1 . VAL E 313 ? 1.0479 0.5630 0.9764 -0.2803 0.1464 -0.1976 312 VAL E CG1 9810 C CG2 . VAL E 313 ? 0.9632 0.5618 0.9385 -0.2777 0.1629 -0.1880 312 VAL E CG2 9811 N N . LEU E 314 ? 1.0401 0.5538 0.9701 -0.2282 0.1520 -0.2420 313 LEU E N 9812 C CA . LEU E 314 ? 1.0730 0.5656 0.9953 -0.2186 0.1470 -0.2690 313 LEU E CA 9813 C C . LEU E 314 ? 1.1209 0.5650 1.0206 -0.2291 0.1289 -0.2654 313 LEU E C 9814 O O . LEU E 314 ? 1.1454 0.5557 1.0328 -0.2354 0.1153 -0.2487 313 LEU E O 9815 C CB . LEU E 314 ? 1.0800 0.5681 1.0203 -0.1901 0.1416 -0.2915 313 LEU E CB 9816 C CG . LEU E 314 ? 1.0486 0.5865 1.0134 -0.1790 0.1616 -0.3152 313 LEU E CG 9817 C CD1 . LEU E 314 ? 1.0543 0.5900 1.0475 -0.1490 0.1497 -0.3353 313 LEU E CD1 9818 C CD2 . LEU E 314 ? 1.0649 0.6182 1.0228 -0.1875 0.1761 -0.3455 313 LEU E CD2 9819 N N . ALA E 315 ? 1.1451 0.5808 1.0320 -0.2350 0.1289 -0.2818 314 ALA E N 9820 C CA . ALA E 315 ? 1.1959 0.5813 1.0592 -0.2428 0.1100 -0.2835 314 ALA E CA 9821 C C . ALA E 315 ? 1.2388 0.5834 1.1015 -0.2166 0.0913 -0.3057 314 ALA E C 9822 O O . ALA E 315 ? 1.2354 0.6026 1.1211 -0.1929 0.0978 -0.3361 314 ALA E O 9823 C CB . ALA E 315 ? 1.2111 0.5979 1.0586 -0.2555 0.1148 -0.2969 314 ALA E CB 9824 N N . THR E 316 ? 1.2895 0.5727 1.1252 -0.2224 0.0657 -0.2932 315 THR E N 9825 C CA . THR E 316 ? 1.3475 0.5732 1.1744 -0.1961 0.0352 -0.3128 315 THR E CA 9826 C C . THR E 316 ? 1.4164 0.5767 1.2083 -0.2025 0.0099 -0.3206 315 THR E C 9827 O O . THR E 316 ? 1.4565 0.5933 1.2555 -0.1749 -0.0073 -0.3564 315 THR E O 9828 C CB . THR E 316 ? 1.3703 0.5572 1.1795 -0.1966 0.0170 -0.2896 315 THR E CB 9829 O OG1 . THR E 316 ? 1.3711 0.5520 1.1525 -0.2369 0.0257 -0.2531 315 THR E OG1 9830 C CG2 . THR E 316 ? 1.3156 0.5556 1.1635 -0.1757 0.0323 -0.2949 315 THR E CG2 9831 N N . GLY E 317 ? 1.4331 0.5672 1.1909 -0.2389 0.0074 -0.2911 316 GLY E N 9832 C CA . GLY E 317 ? 1.4993 0.5701 1.2187 -0.2518 -0.0156 -0.2943 316 GLY E CA 9833 C C . GLY E 317 ? 1.4730 0.5788 1.1997 -0.2649 0.0023 -0.3029 316 GLY E C 9834 O O . GLY E 317 ? 1.4160 0.5883 1.1729 -0.2614 0.0300 -0.3105 316 GLY E O 9835 N N . LEU E 318 ? 1.5227 0.5752 1.2136 -0.2829 -0.0165 -0.3008 317 LEU E N 9836 C CA . LEU E 318 ? 1.5135 0.5841 1.2015 -0.2977 -0.0064 -0.3080 317 LEU E CA 9837 C C . LEU E 318 ? 1.4680 0.5819 1.1647 -0.3335 0.0097 -0.2794 317 LEU E C 9838 O O . LEU E 318 ? 1.4370 0.5702 1.1439 -0.3482 0.0161 -0.2567 317 LEU E O 9839 C CB . LEU E 318 ? 1.5946 0.5873 1.2405 -0.3029 -0.0365 -0.3174 317 LEU E CB 9840 N N . ARG E 319 ? 1.4681 0.5968 1.1618 -0.3468 0.0141 -0.2844 318 ARG E N 9841 C CA . ARG E 319 ? 1.4437 0.6076 1.1501 -0.3778 0.0192 -0.2642 318 ARG E CA 9842 C C . ARG E 319 ? 1.4822 0.6130 1.1719 -0.4097 0.0049 -0.2459 318 ARG E C 9843 O O . ARG E 319 ? 1.5431 0.6057 1.1935 -0.4130 -0.0149 -0.2489 318 ARG E O 9844 C CB . ARG E 319 ? 1.4591 0.6245 1.1537 -0.3861 0.0162 -0.2749 318 ARG E CB 9845 C CG . ARG E 319 ? 1.4355 0.6339 1.1345 -0.3701 0.0331 -0.2905 318 ARG E CG 9846 C CD . ARG E 319 ? 1.4724 0.6520 1.1402 -0.3845 0.0258 -0.3009 318 ARG E CD 9847 N NE . ARG E 319 ? 1.4750 0.6678 1.1257 -0.3760 0.0434 -0.3217 318 ARG E NE 9848 C CZ . ARG E 319 ? 1.4404 0.6650 1.0917 -0.3824 0.0523 -0.3154 318 ARG E CZ 9849 N NH1 . ARG E 319 ? 1.4064 0.6583 1.0848 -0.3902 0.0425 -0.2914 318 ARG E NH1 9850 N NH2 . ARG E 319 ? 1.4538 0.6815 1.0763 -0.3830 0.0704 -0.3365 318 ARG E NH2 9851 N N . ASN E 320 ? 1.4485 0.6274 1.1670 -0.4351 0.0145 -0.2305 319 ASN E N 9852 C CA . ASN E 320 ? 1.4837 0.6454 1.1899 -0.4753 0.0085 -0.2173 319 ASN E CA 9853 C C . ASN E 320 ? 1.4541 0.6783 1.2032 -0.5023 0.0138 -0.2165 319 ASN E C 9854 O O . ASN E 320 ? 1.4989 0.7099 1.2389 -0.5378 0.0050 -0.2148 319 ASN E O 9855 C CB . ASN E 320 ? 1.4852 0.6404 1.1830 -0.4832 0.0175 -0.2045 319 ASN E CB 9856 C CG . ASN E 320 ? 1.5515 0.6622 1.2093 -0.5315 0.0101 -0.1925 319 ASN E CG 9857 O OD1 . ASN E 320 ? 1.6122 0.6580 1.2259 -0.5468 -0.0112 -0.1932 319 ASN E OD1 9858 N ND2 . ASN E 320 ? 1.5390 0.6815 1.2063 -0.5597 0.0285 -0.1829 319 ASN E ND2 9859 N N . ILE F 10 ? 1.3946 1.0063 1.5771 -0.3347 -0.0051 -0.0486 10 ILE F N 9860 C CA . ILE F 10 ? 1.3582 0.9261 1.5756 -0.2744 0.0018 -0.0612 10 ILE F CA 9861 C C . ILE F 10 ? 1.3489 0.8805 1.6258 -0.2725 -0.0205 -0.0154 10 ILE F C 9862 O O . ILE F 10 ? 1.3551 0.8928 1.6690 -0.2975 -0.0396 0.0161 10 ILE F O 9863 C CB . ILE F 10 ? 1.3344 0.9039 1.5656 -0.2346 0.0196 -0.1013 10 ILE F CB 9864 C CG1 . ILE F 10 ? 1.3437 0.9531 1.5388 -0.2374 0.0393 -0.1482 10 ILE F CG1 9865 C CG2 . ILE F 10 ? 1.3122 0.8344 1.5610 -0.1848 0.0265 -0.1146 10 ILE F CG2 9866 C CD1 . ILE F 10 ? 1.3231 0.9319 1.5356 -0.1971 0.0509 -0.1876 10 ILE F CD1 9867 N N . GLU F 11 ? 1.3358 0.8299 1.6289 -0.2442 -0.0178 -0.0140 11 GLU F N 9868 C CA . GLU F 11 ? 1.3259 0.7852 1.6912 -0.2392 -0.0332 0.0202 11 GLU F CA 9869 C C . GLU F 11 ? 1.3030 0.7459 1.7211 -0.2121 -0.0221 0.0061 11 GLU F C 9870 O O . GLU F 11 ? 1.3038 0.7448 1.7863 -0.2280 -0.0392 0.0349 11 GLU F O 9871 C CB . GLU F 11 ? 1.3197 0.7457 1.6858 -0.2165 -0.0263 0.0165 11 GLU F CB 9872 N N . GLY F 12 ? 1.2863 0.7158 1.6775 -0.1748 0.0039 -0.0374 12 GLY F N 9873 C CA . GLY F 12 ? 1.2722 0.6843 1.6978 -0.1532 0.0176 -0.0564 12 GLY F CA 9874 C C . GLY F 12 ? 1.2668 0.6724 1.6395 -0.1239 0.0374 -0.1011 12 GLY F C 9875 O O . GLY F 12 ? 1.2705 0.6942 1.5899 -0.1200 0.0386 -0.1190 12 GLY F O 9876 N N . GLY F 13 ? 1.2612 0.6399 1.6533 -0.1067 0.0512 -0.1195 13 GLY F N 9877 C CA . GLY F 13 ? 1.2655 0.6302 1.6091 -0.0841 0.0626 -0.1562 13 GLY F CA 9878 C C . GLY F 13 ? 1.2754 0.6000 1.5852 -0.0676 0.0721 -0.1709 13 GLY F C 9879 O O . GLY F 13 ? 1.2731 0.5802 1.6036 -0.0714 0.0753 -0.1562 13 GLY F O 9880 N N . TRP F 14 ? 1.2875 0.5965 1.5479 -0.0518 0.0732 -0.1981 14 TRP F N 9881 C CA . TRP F 14 ? 1.3082 0.5735 1.5274 -0.0406 0.0786 -0.2120 14 TRP F CA 9882 C C . TRP F 14 ? 1.3378 0.5617 1.5402 -0.0421 0.0908 -0.2307 14 TRP F C 9883 O O . TRP F 14 ? 1.3476 0.5733 1.5300 -0.0399 0.0829 -0.2441 14 TRP F O 9884 C CB . TRP F 14 ? 1.3133 0.5861 1.4861 -0.0267 0.0631 -0.2260 14 TRP F CB 9885 C CG . TRP F 14 ? 1.2949 0.6065 1.4737 -0.0304 0.0567 -0.2164 14 TRP F CG 9886 C CD1 . TRP F 14 ? 1.2824 0.6067 1.4839 -0.0455 0.0592 -0.1916 14 TRP F CD1 9887 C CD2 . TRP F 14 ? 1.2935 0.6349 1.4568 -0.0236 0.0469 -0.2338 14 TRP F CD2 9888 N NE1 . TRP F 14 ? 1.2790 0.6385 1.4666 -0.0531 0.0528 -0.1917 14 TRP F NE1 9889 C CE2 . TRP F 14 ? 1.2845 0.6566 1.4522 -0.0391 0.0489 -0.2212 14 TRP F CE2 9890 C CE3 . TRP F 14 ? 1.3040 0.6490 1.4576 -0.0083 0.0357 -0.2600 14 TRP F CE3 9891 C CZ2 . TRP F 14 ? 1.2869 0.6948 1.4458 -0.0418 0.0476 -0.2402 14 TRP F CZ2 9892 C CZ3 . TRP F 14 ? 1.3017 0.6833 1.4622 -0.0057 0.0320 -0.2787 14 TRP F CZ3 9893 C CH2 . TRP F 14 ? 1.2933 0.7067 1.4543 -0.0233 0.0417 -0.2718 14 TRP F CH2 9894 N N . GLN F 15 ? 1.3577 0.5443 1.5679 -0.0498 0.1109 -0.2335 15 GLN F N 9895 C CA . GLN F 15 ? 1.4013 0.5435 1.5817 -0.0609 0.1282 -0.2564 15 GLN F CA 9896 C C . GLN F 15 ? 1.4424 0.5519 1.5392 -0.0580 0.1130 -0.2690 15 GLN F C 9897 O O . GLN F 15 ? 1.4810 0.5596 1.5337 -0.0709 0.1131 -0.2846 15 GLN F O 9898 C CB . GLN F 15 ? 1.4129 0.5272 1.6326 -0.0749 0.1600 -0.2623 15 GLN F CB 9899 C CG . GLN F 15 ? 1.3903 0.5253 1.7062 -0.0819 0.1739 -0.2546 15 GLN F CG 9900 C CD . GLN F 15 ? 1.4121 0.5151 1.7785 -0.0983 0.2115 -0.2743 15 GLN F CD 9901 O OE1 . GLN F 15 ? 1.4412 0.5130 1.7770 -0.1046 0.2278 -0.2879 15 GLN F OE1 9902 N NE2 . GLN F 15 ? 1.4034 0.5148 1.8536 -0.1070 0.2267 -0.2787 15 GLN F NE2 9903 N N . GLY F 16 ? 1.4400 0.5547 1.5161 -0.0443 0.0966 -0.2605 16 GLY F N 9904 C CA . GLY F 16 ? 1.4809 0.5636 1.4894 -0.0403 0.0753 -0.2683 16 GLY F CA 9905 C C . GLY F 16 ? 1.4961 0.5887 1.4862 -0.0316 0.0445 -0.2743 16 GLY F C 9906 O O . GLY F 16 ? 1.5292 0.5916 1.4728 -0.0298 0.0188 -0.2781 16 GLY F O 9907 N N . MET F 17 ? 1.4723 0.6064 1.5046 -0.0276 0.0439 -0.2739 17 MET F N 9908 C CA . MET F 17 ? 1.4873 0.6345 1.5162 -0.0207 0.0172 -0.2818 17 MET F CA 9909 C C . MET F 17 ? 1.5088 0.6445 1.5336 -0.0375 0.0246 -0.2874 17 MET F C 9910 O O . MET F 17 ? 1.4781 0.6487 1.5481 -0.0389 0.0387 -0.2851 17 MET F O 9911 C CB . MET F 17 ? 1.4462 0.6559 1.5258 -0.0050 0.0109 -0.2815 17 MET F CB 9912 C CG . MET F 17 ? 1.4549 0.6835 1.5470 0.0047 -0.0159 -0.2945 17 MET F CG 9913 S SD . MET F 17 ? 1.4160 0.7182 1.5655 0.0171 -0.0161 -0.3051 17 MET F SD 9914 C CE . MET F 17 ? 1.3820 0.7221 1.5590 -0.0009 0.0124 -0.2894 17 MET F CE 9915 N N . VAL F 18 ? 1.5692 0.6539 1.5359 -0.0546 0.0132 -0.2939 18 VAL F N 9916 C CA . VAL F 18 ? 1.6027 0.6714 1.5526 -0.0756 0.0161 -0.3016 18 VAL F CA 9917 C C . VAL F 18 ? 1.6325 0.6992 1.5663 -0.0718 -0.0279 -0.3016 18 VAL F C 9918 O O . VAL F 18 ? 1.6766 0.7178 1.5776 -0.0943 -0.0359 -0.3057 18 VAL F O 9919 C CB . VAL F 18 ? 1.6627 0.6716 1.5517 -0.1107 0.0382 -0.3113 18 VAL F CB 9920 N N . ASP F 19 ? 1.6132 0.7068 1.5764 -0.0455 -0.0562 -0.2988 19 ASP F N 9921 C CA . ASP F 19 ? 1.6376 0.7338 1.6110 -0.0373 -0.1017 -0.3003 19 ASP F CA 9922 C C . ASP F 19 ? 1.6000 0.7515 1.6334 -0.0272 -0.0997 -0.3073 19 ASP F C 9923 O O . ASP F 19 ? 1.6273 0.7730 1.6628 -0.0324 -0.1290 -0.3087 19 ASP F O 9924 C CB . ASP F 19 ? 1.6334 0.7381 1.6323 -0.0130 -0.1294 -0.3012 19 ASP F CB 9925 C CG . ASP F 19 ? 1.6815 0.7273 1.6189 -0.0238 -0.1417 -0.2922 19 ASP F CG 9926 O OD1 . ASP F 19 ? 1.7505 0.7386 1.6220 -0.0522 -0.1619 -0.2843 19 ASP F OD1 9927 O OD2 . ASP F 19 ? 1.6610 0.7173 1.6117 -0.0081 -0.1320 -0.2929 19 ASP F OD2 9928 N N . GLY F 20 ? 1.5458 0.7499 1.6268 -0.0161 -0.0686 -0.3097 20 GLY F N 9929 C CA . GLY F 20 ? 1.5121 0.7715 1.6466 -0.0113 -0.0630 -0.3159 20 GLY F CA 9930 C C . GLY F 20 ? 1.4684 0.7672 1.6327 -0.0144 -0.0267 -0.3099 20 GLY F C 9931 O O . GLY F 20 ? 1.4639 0.7444 1.6131 -0.0199 -0.0059 -0.3002 20 GLY F O 9932 N N . TRP F 21 ? 1.4412 0.7931 1.6507 -0.0137 -0.0222 -0.3141 21 TRP F N 9933 C CA . TRP F 21 ? 1.4072 0.7968 1.6455 -0.0234 0.0036 -0.3030 21 TRP F CA 9934 C C . TRP F 21 ? 1.3781 0.8040 1.6323 -0.0196 0.0097 -0.3029 21 TRP F C 9935 O O . TRP F 21 ? 1.3627 0.7937 1.6199 -0.0301 0.0253 -0.2856 21 TRP F O 9936 C CB . TRP F 21 ? 1.3989 0.8275 1.6704 -0.0322 0.0055 -0.3053 21 TRP F CB 9937 C CG . TRP F 21 ? 1.4229 0.8203 1.6841 -0.0444 0.0113 -0.3005 21 TRP F CG 9938 C CD1 . TRP F 21 ? 1.4420 0.7938 1.6833 -0.0546 0.0277 -0.2933 21 TRP F CD1 9939 C CD2 . TRP F 21 ? 1.4295 0.8416 1.7052 -0.0506 0.0046 -0.3067 21 TRP F CD2 9940 N NE1 . TRP F 21 ? 1.4586 0.7951 1.6999 -0.0680 0.0336 -0.2973 21 TRP F NE1 9941 C CE2 . TRP F 21 ? 1.4517 0.8235 1.7107 -0.0653 0.0177 -0.3031 21 TRP F CE2 9942 C CE3 . TRP F 21 ? 1.4204 0.8767 1.7257 -0.0468 -0.0089 -0.3181 21 TRP F CE3 9943 C CZ2 . TRP F 21 ? 1.4648 0.8371 1.7293 -0.0762 0.0157 -0.3081 21 TRP F CZ2 9944 C CZ3 . TRP F 21 ? 1.4330 0.8904 1.7453 -0.0560 -0.0130 -0.3207 21 TRP F CZ3 9945 C CH2 . TRP F 21 ? 1.4537 0.8684 1.7426 -0.0706 -0.0017 -0.3144 21 TRP F CH2 9946 N N . TYR F 22 ? 1.3719 0.8228 1.6418 -0.0073 -0.0033 -0.3232 22 TYR F N 9947 C CA . TYR F 22 ? 1.3521 0.8363 1.6337 -0.0075 0.0055 -0.3307 22 TYR F CA 9948 C C . TYR F 22 ? 1.3645 0.8225 1.6388 0.0125 -0.0116 -0.3454 22 TYR F C 9949 O O . TYR F 22 ? 1.3880 0.8188 1.6644 0.0256 -0.0367 -0.3540 22 TYR F O 9950 C CB . TYR F 22 ? 1.3382 0.8889 1.6604 -0.0181 0.0141 -0.3502 22 TYR F CB 9951 C CG . TYR F 22 ? 1.3321 0.9046 1.6687 -0.0331 0.0186 -0.3422 22 TYR F CG 9952 C CD1 . TYR F 22 ? 1.3228 0.8984 1.6503 -0.0551 0.0312 -0.3140 22 TYR F CD1 9953 C CD2 . TYR F 22 ? 1.3362 0.9247 1.7024 -0.0257 0.0069 -0.3616 22 TYR F CD2 9954 C CE1 . TYR F 22 ? 1.3177 0.9110 1.6621 -0.0692 0.0332 -0.3058 22 TYR F CE1 9955 C CE2 . TYR F 22 ? 1.3310 0.9389 1.7091 -0.0399 0.0110 -0.3545 22 TYR F CE2 9956 C CZ . TYR F 22 ? 1.3218 0.9316 1.6873 -0.0616 0.0249 -0.3269 22 TYR F CZ 9957 O OH . TYR F 22 ? 1.3160 0.9431 1.6970 -0.0762 0.0270 -0.3191 22 TYR F OH 9958 N N . GLY F 23 ? 1.3524 0.8163 1.6189 0.0121 -0.0019 -0.3459 23 GLY F N 9959 C CA . GLY F 23 ? 1.3629 0.8031 1.6280 0.0305 -0.0181 -0.3600 23 GLY F CA 9960 C C . GLY F 23 ? 1.3497 0.8034 1.6071 0.0263 -0.0027 -0.3625 23 GLY F C 9961 O O . GLY F 23 ? 1.3317 0.8272 1.5929 0.0057 0.0194 -0.3604 23 GLY F O 9962 N N . TYR F 24 ? 1.3617 0.7771 1.6041 0.0417 -0.0174 -0.3652 24 TYR F N 9963 C CA . TYR F 24 ? 1.3563 0.7793 1.5919 0.0400 -0.0061 -0.3709 24 TYR F CA 9964 C C . TYR F 24 ? 1.3685 0.7320 1.5549 0.0459 -0.0141 -0.3483 24 TYR F C 9965 O O . TYR F 24 ? 1.3903 0.7044 1.5532 0.0539 -0.0341 -0.3389 24 TYR F O 9966 C CB . TYR F 24 ? 1.3643 0.8082 1.6510 0.0550 -0.0158 -0.4091 24 TYR F CB 9967 C CG . TYR F 24 ? 1.3555 0.8544 1.7057 0.0529 -0.0103 -0.4413 24 TYR F CG 9968 C CD1 . TYR F 24 ? 1.3616 0.8518 1.7402 0.0646 -0.0340 -0.4435 24 TYR F CD1 9969 C CD2 . TYR F 24 ? 1.3475 0.9071 1.7289 0.0349 0.0191 -0.4721 24 TYR F CD2 9970 C CE1 . TYR F 24 ? 1.3535 0.8955 1.7979 0.0630 -0.0288 -0.4748 24 TYR F CE1 9971 C CE2 . TYR F 24 ? 1.3433 0.9557 1.7867 0.0295 0.0289 -0.5071 24 TYR F CE2 9972 C CZ . TYR F 24 ? 1.3433 0.9474 1.8224 0.0460 0.0044 -0.5081 24 TYR F CZ 9973 O OH . TYR F 24 ? 1.3390 0.9968 1.8868 0.0410 0.0142 -0.5440 24 TYR F OH 9974 N N . HIS F 25 ? 1.3592 0.7272 1.5266 0.0368 0.0016 -0.3399 25 HIS F N 9975 C CA . HIS F 25 ? 1.3740 0.6913 1.5025 0.0432 -0.0047 -0.3254 25 HIS F CA 9976 C C . HIS F 25 ? 1.3773 0.7076 1.5149 0.0480 -0.0033 -0.3439 25 HIS F C 9977 O O . HIS F 25 ? 1.3640 0.7326 1.5042 0.0307 0.0171 -0.3459 25 HIS F O 9978 C CB . HIS F 25 ? 1.3641 0.6669 1.4650 0.0269 0.0123 -0.2944 25 HIS F CB 9979 C CG . HIS F 25 ? 1.3787 0.6354 1.4442 0.0305 0.0106 -0.2824 25 HIS F CG 9980 N ND1 . HIS F 25 ? 1.4037 0.6043 1.4364 0.0346 0.0016 -0.2758 25 HIS F ND1 9981 C CD2 . HIS F 25 ? 1.3762 0.6345 1.4304 0.0265 0.0173 -0.2770 25 HIS F CD2 9982 C CE1 . HIS F 25 ? 1.4145 0.5853 1.4199 0.0342 0.0041 -0.2674 25 HIS F CE1 9983 N NE2 . HIS F 25 ? 1.3963 0.6011 1.4164 0.0316 0.0124 -0.2671 25 HIS F NE2 9984 N N . HIS F 26 ? 1.3996 0.6962 1.5414 0.0675 -0.0272 -0.3567 26 HIS F N 9985 C CA . HIS F 26 ? 1.4076 0.7126 1.5676 0.0744 -0.0273 -0.3786 26 HIS F CA 9986 C C . HIS F 26 ? 1.4193 0.6767 1.5298 0.0754 -0.0311 -0.3582 26 HIS F C 9987 O O . HIS F 26 ? 1.4363 0.6423 1.5063 0.0771 -0.0445 -0.3354 26 HIS F O 9988 C CB . HIS F 26 ? 1.4270 0.7301 1.6457 0.0958 -0.0548 -0.4093 26 HIS F CB 9989 C CG . HIS F 26 ? 1.4620 0.6992 1.6609 0.1097 -0.0959 -0.3925 26 HIS F CG 9990 N ND1 . HIS F 26 ? 1.4916 0.6831 1.6759 0.1191 -0.1186 -0.3888 26 HIS F ND1 9991 C CD2 . HIS F 26 ? 1.4807 0.6879 1.6659 0.1097 -0.1204 -0.3772 26 HIS F CD2 9992 C CE1 . HIS F 26 ? 1.5288 0.6638 1.6874 0.1213 -0.1570 -0.3699 26 HIS F CE1 9993 N NE2 . HIS F 26 ? 1.5241 0.6673 1.6807 0.1145 -0.1581 -0.3632 26 HIS F NE2 9994 N N . SER F 27 ? 1.4149 0.6909 1.5265 0.0697 -0.0164 -0.3687 27 SER F N 9995 C CA . SER F 27 ? 1.4274 0.6630 1.4992 0.0714 -0.0202 -0.3540 27 SER F CA 9996 C C . SER F 27 ? 1.4437 0.6787 1.5492 0.0856 -0.0317 -0.3852 27 SER F C 9997 O O . SER F 27 ? 1.4378 0.7220 1.5856 0.0798 -0.0142 -0.4177 27 SER F O 9998 C CB . SER F 27 ? 1.4113 0.6667 1.4538 0.0478 0.0060 -0.3340 27 SER F CB 9999 O OG . SER F 27 ? 1.4246 0.6488 1.4374 0.0492 0.0038 -0.3258 27 SER F OG 10000 N N . ASN F 28 ? 1.4690 0.6476 1.5570 0.1003 -0.0598 -0.3770 28 ASN F N 10001 C CA . ASN F 28 ? 1.4876 0.6563 1.6241 0.1183 -0.0822 -0.4055 28 ASN F CA 10002 C C . ASN F 28 ? 1.5148 0.6276 1.6114 0.1230 -0.1006 -0.3898 28 ASN F C 10003 O O . ASN F 28 ? 1.5259 0.5937 1.5573 0.1155 -0.1069 -0.3566 28 ASN F O 10004 C CB . ASN F 28 ? 1.5033 0.6566 1.6879 0.1346 -0.1195 -0.4138 28 ASN F CB 10005 C CG . ASN F 28 ? 1.5000 0.6921 1.7850 0.1487 -0.1240 -0.4601 28 ASN F CG 10006 O OD1 . ASN F 28 ? 1.4835 0.7237 1.7993 0.1416 -0.0900 -0.4920 28 ASN F OD1 10007 N ND2 . ASN F 28 ? 1.5215 0.6931 1.8622 0.1650 -0.1661 -0.4657 28 ASN F ND2 10008 N N . GLU F 29 ? 1.5301 0.6461 1.6703 0.1336 -0.1071 -0.4174 29 GLU F N 10009 C CA . GLU F 29 ? 1.5614 0.6223 1.6740 0.1400 -0.1308 -0.4055 29 GLU F CA 10010 C C . GLU F 29 ? 1.6011 0.5939 1.6842 0.1449 -0.1788 -0.3772 29 GLU F C 10011 O O . GLU F 29 ? 1.6254 0.5660 1.6419 0.1367 -0.1903 -0.3500 29 GLU F O 10012 C CB . GLU F 29 ? 1.5732 0.6493 1.7594 0.1529 -0.1347 -0.4464 29 GLU F CB 10013 C CG . GLU F 29 ? 1.5880 0.6712 1.8785 0.1735 -0.1660 -0.4785 29 GLU F CG 10014 C CD . GLU F 29 ? 1.5582 0.7131 1.9143 0.1703 -0.1352 -0.5153 29 GLU F CD 10015 O OE1 . GLU F 29 ? 1.5327 0.7397 1.8709 0.1503 -0.0860 -0.5314 29 GLU F OE1 10016 O OE2 . GLU F 29 ? 1.5639 0.7220 1.9897 0.1842 -0.1625 -0.5274 29 GLU F OE2 10017 N N . GLN F 30 ? 1.6121 0.6059 1.7412 0.1532 -0.2063 -0.3834 30 GLN F N 10018 C CA . GLN F 30 ? 1.6600 0.5907 1.7556 0.1489 -0.2552 -0.3547 30 GLN F CA 10019 C C . GLN F 30 ? 1.6616 0.5735 1.6655 0.1258 -0.2358 -0.3235 30 GLN F C 10020 O O . GLN F 30 ? 1.7001 0.5559 1.6278 0.1091 -0.2468 -0.2973 30 GLN F O 10021 C CB . GLN F 30 ? 1.6700 0.6122 1.8500 0.1621 -0.2912 -0.3705 30 GLN F CB 10022 C CG . GLN F 30 ? 1.6816 0.6312 1.9711 0.1850 -0.3195 -0.4029 30 GLN F CG 10023 C CD . GLN F 30 ? 1.6591 0.6638 2.0625 0.2000 -0.3193 -0.4399 30 GLN F CD 10024 O OE1 . GLN F 30 ? 1.6124 0.6843 2.0385 0.1980 -0.2673 -0.4683 30 GLN F OE1 10025 N NE2 . GLN F 30 ? 1.6960 0.6716 2.1739 0.2116 -0.3798 -0.4390 30 GLN F NE2 10026 N N . GLY F 31 ? 1.6239 0.5828 1.6395 0.1223 -0.2053 -0.3292 31 GLY F N 10027 C CA . GLY F 31 ? 1.6210 0.5680 1.5692 0.1014 -0.1830 -0.3059 31 GLY F CA 10028 C C . GLY F 31 ? 1.5678 0.5778 1.5418 0.0994 -0.1422 -0.3145 31 GLY F C 10029 O O . GLY F 31 ? 1.5321 0.5964 1.5571 0.1078 -0.1226 -0.3362 31 GLY F O 10030 N N . SER F 32 ? 1.5684 0.5697 1.5056 0.0837 -0.1288 -0.2984 32 SER F N 10031 C CA . SER F 32 ? 1.5255 0.5804 1.4877 0.0792 -0.0959 -0.3017 32 SER F CA 10032 C C . SER F 32 ? 1.5370 0.5721 1.4713 0.0648 -0.0947 -0.2894 32 SER F C 10033 O O . SER F 32 ? 1.5670 0.5517 1.4445 0.0484 -0.0956 -0.2750 32 SER F O 10034 C CB . SER F 32 ? 1.4947 0.5743 1.4472 0.0704 -0.0591 -0.2930 32 SER F CB 10035 O OG . SER F 32 ? 1.5152 0.5496 1.4156 0.0577 -0.0507 -0.2732 32 SER F OG 10036 N N . GLY F 33 ? 1.5152 0.5911 1.4891 0.0673 -0.0899 -0.2982 33 GLY F N 10037 C CA . GLY F 33 ? 1.5310 0.5921 1.4855 0.0538 -0.0898 -0.2905 33 GLY F CA 10038 C C . GLY F 33 ? 1.5012 0.6167 1.5092 0.0595 -0.0840 -0.3024 33 GLY F C 10039 O O . GLY F 33 ? 1.4747 0.6383 1.5341 0.0718 -0.0809 -0.3196 33 GLY F O 10040 N N . TYR F 34 ? 1.5103 0.6182 1.5053 0.0470 -0.0801 -0.2963 34 TYR F N 10041 C CA . TYR F 34 ? 1.4822 0.6400 1.5228 0.0488 -0.0717 -0.3049 34 TYR F CA 10042 C C . TYR F 34 ? 1.5023 0.6617 1.5732 0.0585 -0.1077 -0.3176 34 TYR F C 10043 O O . TYR F 34 ? 1.5450 0.6577 1.5955 0.0595 -0.1443 -0.3140 34 TYR F O 10044 C CB . TYR F 34 ? 1.4794 0.6306 1.5005 0.0304 -0.0477 -0.2931 34 TYR F CB 10045 C CG . TYR F 34 ? 1.4579 0.6139 1.4746 0.0213 -0.0145 -0.2805 34 TYR F CG 10046 C CD1 . TYR F 34 ? 1.4843 0.5918 1.4582 0.0108 -0.0054 -0.2723 34 TYR F CD1 10047 C CD2 . TYR F 34 ? 1.4171 0.6251 1.4754 0.0192 0.0053 -0.2758 34 TYR F CD2 10048 C CE1 . TYR F 34 ? 1.4643 0.5770 1.4498 0.0033 0.0225 -0.2613 34 TYR F CE1 10049 C CE2 . TYR F 34 ? 1.4012 0.6109 1.4655 0.0089 0.0273 -0.2594 34 TYR F CE2 10050 C CZ . TYR F 34 ? 1.4222 0.5853 1.4567 0.0035 0.0359 -0.2529 34 TYR F CZ 10051 O OH . TYR F 34 ? 1.4065 0.5727 1.4623 -0.0057 0.0555 -0.2372 34 TYR F OH 10052 N N . ALA F 35 ? 1.4753 0.6883 1.5982 0.0628 -0.0996 -0.3308 35 ALA F N 10053 C CA . ALA F 35 ? 1.4906 0.7140 1.6587 0.0718 -0.1311 -0.3447 35 ALA F CA 10054 C C . ALA F 35 ? 1.4591 0.7373 1.6642 0.0671 -0.1101 -0.3533 35 ALA F C 10055 O O . ALA F 35 ? 1.4220 0.7540 1.6578 0.0659 -0.0814 -0.3647 35 ALA F O 10056 C CB . ALA F 35 ? 1.4906 0.7318 1.7198 0.0920 -0.1512 -0.3677 35 ALA F CB 10057 N N . ALA F 36 ? 1.4813 0.7439 1.6775 0.0593 -0.1254 -0.3468 36 ALA F N 10058 C CA . ALA F 36 ? 1.4564 0.7666 1.6851 0.0536 -0.1083 -0.3533 36 ALA F CA 10059 C C . ALA F 36 ? 1.4479 0.8065 1.7570 0.0678 -0.1230 -0.3810 36 ALA F C 10060 O O . ALA F 36 ? 1.4732 0.8131 1.8149 0.0813 -0.1602 -0.3903 36 ALA F O 10061 C CB . ALA F 36 ? 1.4824 0.7571 1.6714 0.0377 -0.1167 -0.3384 36 ALA F CB 10062 N N . ASP F 37 ? 1.4175 0.8381 1.7635 0.0617 -0.0944 -0.3947 37 ASP F N 10063 C CA . ASP F 37 ? 1.4110 0.8849 1.8384 0.0695 -0.0991 -0.4269 37 ASP F CA 10064 C C . ASP F 37 ? 1.4241 0.8942 1.8641 0.0667 -0.1197 -0.4219 37 ASP F C 10065 O O . ASP F 37 ? 1.4078 0.8914 1.8230 0.0512 -0.0996 -0.4097 37 ASP F O 10066 C CB . ASP F 37 ? 1.3796 0.9216 1.8292 0.0547 -0.0562 -0.4449 37 ASP F CB 10067 C CG . ASP F 37 ? 1.3740 0.9761 1.9129 0.0586 -0.0515 -0.4889 37 ASP F CG 10068 O OD1 . ASP F 37 ? 1.3924 0.9840 1.9920 0.0790 -0.0839 -0.5069 37 ASP F OD1 10069 O OD2 . ASP F 37 ? 1.3580 1.0179 1.9098 0.0374 -0.0158 -0.5062 37 ASP F OD2 10070 N N . LYS F 38 ? 1.4571 0.9067 1.9395 0.0802 -0.1632 -0.4296 38 LYS F N 10071 C CA . LYS F 38 ? 1.4809 0.9180 1.9715 0.0754 -0.1918 -0.4214 38 LYS F CA 10072 C C . LYS F 38 ? 1.4567 0.9632 2.0252 0.0758 -0.1778 -0.4488 38 LYS F C 10073 O O . LYS F 38 ? 1.4543 0.9647 2.0102 0.0645 -0.1790 -0.4391 38 LYS F O 10074 C CB . LYS F 38 ? 1.5300 0.9138 2.0368 0.0842 -0.2530 -0.4130 38 LYS F CB 10075 C CG . LYS F 38 ? 1.5698 0.8776 1.9843 0.0743 -0.2705 -0.3829 38 LYS F CG 10076 N N . GLU F 39 ? 1.4416 1.0029 2.0907 0.0857 -0.1621 -0.4859 39 GLU F N 10077 C CA . GLU F 39 ? 1.4220 1.0550 2.1479 0.0809 -0.1412 -0.5191 39 GLU F CA 10078 C C . GLU F 39 ? 1.3987 1.0670 2.0725 0.0554 -0.0955 -0.5098 39 GLU F C 10079 O O . GLU F 39 ? 1.3896 1.0922 2.0873 0.0450 -0.0886 -0.5161 39 GLU F O 10080 C CB . GLU F 39 ? 1.4114 1.0953 2.2327 0.0904 -0.1253 -0.5681 39 GLU F CB 10081 N N . SER F 40 ? 1.3926 1.0506 1.9998 0.0443 -0.0685 -0.4926 40 SER F N 10082 C CA . SER F 40 ? 1.3761 1.0592 1.9359 0.0175 -0.0331 -0.4759 40 SER F CA 10083 C C . SER F 40 ? 1.3824 1.0209 1.8841 0.0117 -0.0433 -0.4378 40 SER F C 10084 O O . SER F 40 ? 1.3695 1.0323 1.8633 -0.0070 -0.0269 -0.4283 40 SER F O 10085 C CB . SER F 40 ? 1.3703 1.0564 1.8905 0.0060 -0.0069 -0.4696 40 SER F CB 10086 O OG . SER F 40 ? 1.3600 1.0605 1.8362 -0.0219 0.0169 -0.4448 40 SER F OG 10087 N N . THR F 41 ? 1.4062 0.9791 1.8677 0.0237 -0.0690 -0.4180 41 THR F N 10088 C CA . THR F 41 ? 1.4218 0.9484 1.8302 0.0144 -0.0757 -0.3903 41 THR F CA 10089 C C . THR F 41 ? 1.4345 0.9690 1.8709 0.0128 -0.0963 -0.3962 41 THR F C 10090 O O . THR F 41 ? 1.4316 0.9639 1.8467 -0.0019 -0.0858 -0.3833 41 THR F O 10091 C CB . THR F 41 ? 1.4549 0.9089 1.8071 0.0194 -0.0959 -0.3732 41 THR F CB 10092 O OG1 . THR F 41 ? 1.4418 0.8882 1.7680 0.0200 -0.0752 -0.3661 41 THR F OG1 10093 C CG2 . THR F 41 ? 1.4788 0.8861 1.7766 0.0027 -0.0966 -0.3533 41 THR F CG2 10094 N N . GLN F 42 ? 1.4492 0.9925 1.9410 0.0278 -0.1273 -0.4159 42 GLN F N 10095 C CA . GLN F 42 ? 1.4619 1.0172 1.9941 0.0270 -0.1518 -0.4229 42 GLN F CA 10096 C C . GLN F 42 ? 1.4321 1.0509 1.9948 0.0141 -0.1198 -0.4347 42 GLN F C 10097 O O . GLN F 42 ? 1.4377 1.0526 1.9873 0.0027 -0.1234 -0.4242 42 GLN F O 10098 C CB . GLN F 42 ? 1.4745 1.0402 2.0896 0.0466 -0.1893 -0.4461 42 GLN F CB 10099 N N . LYS F 43 ? 1.4081 1.0834 2.0060 0.0112 -0.0882 -0.4565 43 LYS F N 10100 C CA . LYS F 43 ? 1.3863 1.1244 2.0072 -0.0091 -0.0568 -0.4682 43 LYS F CA 10101 C C . LYS F 43 ? 1.3783 1.1017 1.9362 -0.0303 -0.0383 -0.4350 43 LYS F C 10102 O O . LYS F 43 ? 1.3672 1.1229 1.9368 -0.0473 -0.0275 -0.4343 43 LYS F O 10103 C CB . LYS F 43 ? 1.3723 1.1670 2.0269 -0.0180 -0.0251 -0.4981 43 LYS F CB 10104 C CG . LYS F 43 ? 1.3598 1.2234 2.0389 -0.0471 0.0064 -0.5161 43 LYS F CG 10105 N N . ALA F 44 ? 1.3841 1.0591 1.8841 -0.0298 -0.0352 -0.4088 44 ALA F N 10106 C CA . ALA F 44 ? 1.3800 1.0373 1.8381 -0.0481 -0.0187 -0.3791 44 ALA F CA 10107 C C . ALA F 44 ? 1.3982 1.0112 1.8333 -0.0490 -0.0327 -0.3654 44 ALA F C 10108 O O . ALA F 44 ? 1.3867 1.0064 1.8199 -0.0653 -0.0209 -0.3528 44 ALA F O 10109 C CB . ALA F 44 ? 1.3781 1.0050 1.7981 -0.0484 -0.0074 -0.3608 44 ALA F CB 10110 N N . ILE F 45 ? 1.4295 0.9952 1.8451 -0.0360 -0.0588 -0.3676 45 ILE F N 10111 C CA . ILE F 45 ? 1.4608 0.9811 1.8442 -0.0446 -0.0732 -0.3581 45 ILE F CA 10112 C C . ILE F 45 ? 1.4611 1.0167 1.8835 -0.0494 -0.0838 -0.3680 45 ILE F C 10113 O O . ILE F 45 ? 1.4710 1.0107 1.8750 -0.0643 -0.0803 -0.3595 45 ILE F O 10114 C CB . ILE F 45 ? 1.5045 0.9647 1.8498 -0.0387 -0.1053 -0.3560 45 ILE F CB 10115 C CG1 . ILE F 45 ? 1.5103 0.9296 1.8083 -0.0388 -0.0909 -0.3454 45 ILE F CG1 10116 C CG2 . ILE F 45 ? 1.5465 0.9635 1.8538 -0.0567 -0.1232 -0.3492 45 ILE F CG2 10117 C CD1 . ILE F 45 ? 1.5546 0.9206 1.8160 -0.0349 -0.1235 -0.3429 45 ILE F CD1 10118 N N . ASP F 46 ? 1.4498 1.0545 1.9317 -0.0380 -0.0944 -0.3892 46 ASP F N 10119 C CA . ASP F 46 ? 1.4441 1.0909 1.9753 -0.0422 -0.1023 -0.4028 46 ASP F CA 10120 C C . ASP F 46 ? 1.4151 1.1078 1.9540 -0.0613 -0.0688 -0.3995 46 ASP F C 10121 O O . ASP F 46 ? 1.4189 1.1175 1.9610 -0.0733 -0.0702 -0.3951 46 ASP F O 10122 C CB . ASP F 46 ? 1.4382 1.1288 2.0471 -0.0259 -0.1180 -0.4331 46 ASP F CB 10123 C CG . ASP F 46 ? 1.4711 1.1154 2.0872 -0.0080 -0.1617 -0.4330 46 ASP F CG 10124 O OD1 . ASP F 46 ? 1.5039 1.0813 2.0514 -0.0130 -0.1796 -0.4088 46 ASP F OD1 10125 O OD2 . ASP F 46 ? 1.4671 1.1416 2.1615 0.0077 -0.1783 -0.4585 46 ASP F OD2 10126 N N . GLY F 47 ? 1.3921 1.1143 1.9313 -0.0679 -0.0421 -0.3994 47 GLY F N 10127 C CA . GLY F 47 ? 1.3733 1.1356 1.9148 -0.0933 -0.0161 -0.3902 47 GLY F CA 10128 C C . GLY F 47 ? 1.3762 1.1003 1.8820 -0.1064 -0.0097 -0.3591 47 GLY F C 10129 O O . GLY F 47 ? 1.3665 1.1155 1.8831 -0.1272 0.0000 -0.3490 47 GLY F O 10130 N N . VAL F 48 ? 1.3905 1.0545 1.8593 -0.0965 -0.0139 -0.3461 48 VAL F N 10131 C CA . VAL F 48 ? 1.3986 1.0217 1.8463 -0.1079 -0.0045 -0.3251 48 VAL F CA 10132 C C . VAL F 48 ? 1.4214 1.0201 1.8614 -0.1112 -0.0160 -0.3307 48 VAL F C 10133 O O . VAL F 48 ? 1.4185 1.0173 1.8685 -0.1266 -0.0067 -0.3220 48 VAL F O 10134 C CB . VAL F 48 ? 1.4098 0.9800 1.8241 -0.1010 0.0017 -0.3154 48 VAL F CB 10135 C CG1 . VAL F 48 ? 1.4261 0.9493 1.8285 -0.1126 0.0140 -0.3056 48 VAL F CG1 10136 C CG2 . VAL F 48 ? 1.3887 0.9810 1.8116 -0.1038 0.0138 -0.3034 48 VAL F CG2 10137 N N . THR F 49 ? 1.4483 1.0237 1.8715 -0.0996 -0.0394 -0.3435 49 THR F N 10138 C CA . THR F 49 ? 1.4819 1.0308 1.8895 -0.1079 -0.0564 -0.3473 49 THR F CA 10139 C C . THR F 49 ? 1.4666 1.0675 1.9186 -0.1137 -0.0606 -0.3542 49 THR F C 10140 O O . THR F 49 ? 1.4818 1.0682 1.9251 -0.1275 -0.0633 -0.3522 49 THR F O 10141 C CB . THR F 49 ? 1.5206 1.0322 1.9020 -0.0993 -0.0908 -0.3537 49 THR F CB 10142 O OG1 . THR F 49 ? 1.5363 1.0025 1.8743 -0.0963 -0.0860 -0.3476 49 THR F OG1 10143 C CG2 . THR F 49 ? 1.5653 1.0387 1.9143 -0.1175 -0.1106 -0.3526 49 THR F CG2 10144 N N . ASN F 50 ? 1.4395 1.1008 1.9376 -0.1068 -0.0584 -0.3653 50 ASN F N 10145 C CA . ASN F 50 ? 1.4242 1.1423 1.9662 -0.1173 -0.0551 -0.3742 50 ASN F CA 10146 C C . ASN F 50 ? 1.4135 1.1417 1.9516 -0.1395 -0.0319 -0.3558 50 ASN F C 10147 O O . ASN F 50 ? 1.4142 1.1604 1.9684 -0.1526 -0.0327 -0.3555 50 ASN F O 10148 C CB . ASN F 50 ? 1.4025 1.1845 1.9939 -0.1121 -0.0497 -0.3968 50 ASN F CB 10149 C CG . ASN F 50 ? 1.4146 1.2026 2.0470 -0.0917 -0.0781 -0.4208 50 ASN F CG 10150 O OD1 . ASN F 50 ? 1.4019 1.2475 2.0965 -0.0904 -0.0751 -0.4478 50 ASN F OD1 10151 N ND2 . ASN F 50 ? 1.4441 1.1721 2.0466 -0.0794 -0.1067 -0.4119 50 ASN F ND2 10152 N N . LYS F 51 ? 1.4071 1.1221 1.9293 -0.1442 -0.0150 -0.3388 51 LYS F N 10153 C CA . LYS F 51 ? 1.3996 1.1212 1.9305 -0.1663 0.0000 -0.3162 51 LYS F CA 10154 C C . LYS F 51 ? 1.4177 1.0899 1.9399 -0.1719 0.0024 -0.3069 51 LYS F C 10155 O O . LYS F 51 ? 1.4148 1.0996 1.9578 -0.1882 0.0045 -0.2997 51 LYS F O 10156 C CB . LYS F 51 ? 1.3888 1.1069 1.9132 -0.1701 0.0108 -0.2988 51 LYS F CB 10157 C CG . LYS F 51 ? 1.3813 1.1187 1.9256 -0.1983 0.0170 -0.2713 51 LYS F CG 10158 C CD . LYS F 51 ? 1.3762 1.1008 1.9149 -0.2027 0.0212 -0.2502 51 LYS F CD 10159 C CE . LYS F 51 ? 1.3779 1.1384 1.9307 -0.2386 0.0184 -0.2229 51 LYS F CE 10160 N NZ . LYS F 51 ? 1.3794 1.1969 1.9157 -0.2548 0.0231 -0.2383 51 LYS F NZ 10161 N N . VAL F 52 ? 1.4412 1.0574 1.9328 -0.1618 0.0043 -0.3096 52 VAL F N 10162 C CA . VAL F 52 ? 1.4684 1.0339 1.9495 -0.1720 0.0144 -0.3092 52 VAL F CA 10163 C C . VAL F 52 ? 1.4928 1.0576 1.9679 -0.1808 0.0038 -0.3207 52 VAL F C 10164 O O . VAL F 52 ? 1.5029 1.0539 1.9927 -0.1965 0.0149 -0.3186 52 VAL F O 10165 C CB . VAL F 52 ? 1.4944 1.0009 1.9337 -0.1662 0.0213 -0.3165 52 VAL F CB 10166 C CG1 . VAL F 52 ? 1.5201 1.0113 1.9150 -0.1564 -0.0022 -0.3301 52 VAL F CG1 10167 C CG2 . VAL F 52 ? 1.5224 0.9803 1.9585 -0.1838 0.0423 -0.3227 52 VAL F CG2 10168 N N . ASN F 53 ? 1.5059 1.0856 1.9676 -0.1713 -0.0192 -0.3330 53 ASN F N 10169 C CA . ASN F 53 ? 1.5297 1.1116 1.9890 -0.1800 -0.0357 -0.3419 53 ASN F CA 10170 C C . ASN F 53 ? 1.5017 1.1396 2.0077 -0.1889 -0.0320 -0.3384 53 ASN F C 10171 O O . ASN F 53 ? 1.5150 1.1476 2.0243 -0.2032 -0.0328 -0.3395 53 ASN F O 10172 C CB . ASN F 53 ? 1.5513 1.1351 2.0004 -0.1670 -0.0686 -0.3531 53 ASN F CB 10173 C CG . ASN F 53 ? 1.5904 1.1142 1.9852 -0.1644 -0.0792 -0.3532 53 ASN F CG 10174 O OD1 . ASN F 53 ? 1.6098 1.0884 1.9684 -0.1752 -0.0576 -0.3499 53 ASN F OD1 10175 N ND2 . ASN F 53 ? 1.6060 1.1291 2.0012 -0.1521 -0.1133 -0.3581 53 ASN F ND2 10176 N N . SER F 54 ? 1.4686 1.1587 2.0056 -0.1849 -0.0270 -0.3350 54 SER F N 10177 C CA . SER F 54 ? 1.4485 1.1950 2.0228 -0.2008 -0.0221 -0.3311 54 SER F CA 10178 C C . SER F 54 ? 1.4455 1.1784 2.0311 -0.2210 -0.0084 -0.3093 54 SER F C 10179 O O . SER F 54 ? 1.4434 1.2025 2.0512 -0.2382 -0.0094 -0.3048 54 SER F O 10180 C CB . SER F 54 ? 1.4258 1.2272 2.0191 -0.2009 -0.0164 -0.3356 54 SER F CB 10181 O OG . SER F 54 ? 1.4178 1.2735 2.0374 -0.2250 -0.0098 -0.3330 54 SER F OG 10182 N N . ILE F 55 ? 1.4460 1.1378 2.0245 -0.2193 0.0026 -0.2962 55 ILE F N 10183 C CA . ILE F 55 ? 1.4467 1.1169 2.0539 -0.2358 0.0129 -0.2771 55 ILE F CA 10184 C C . ILE F 55 ? 1.4721 1.1054 2.0769 -0.2421 0.0173 -0.2893 55 ILE F C 10185 O O . ILE F 55 ? 1.4734 1.1103 2.1128 -0.2588 0.0200 -0.2798 55 ILE F O 10186 C CB . ILE F 55 ? 1.4434 1.0785 2.0572 -0.2307 0.0238 -0.2644 55 ILE F CB 10187 C CG1 . ILE F 55 ? 1.4233 1.0967 2.0416 -0.2337 0.0183 -0.2466 55 ILE F CG1 10188 C CG2 . ILE F 55 ? 1.4506 1.0540 2.1124 -0.2446 0.0338 -0.2510 55 ILE F CG2 10189 C CD1 . ILE F 55 ? 1.4202 1.0636 2.0310 -0.2219 0.0249 -0.2402 55 ILE F CD1 10190 N N . ILE F 56 ? 1.4978 1.0942 2.0593 -0.2331 0.0165 -0.3097 56 ILE F N 10191 C CA . ILE F 56 ? 1.5326 1.0896 2.0763 -0.2462 0.0216 -0.3247 56 ILE F CA 10192 C C . ILE F 56 ? 1.5368 1.1277 2.0875 -0.2546 0.0054 -0.3281 56 ILE F C 10193 O O . ILE F 56 ? 1.5518 1.1308 2.1173 -0.2715 0.0127 -0.3303 56 ILE F O 10194 C CB . ILE F 56 ? 1.5699 1.0768 2.0507 -0.2440 0.0195 -0.3425 56 ILE F CB 10195 C CG1 . ILE F 56 ? 1.5710 1.0407 2.0452 -0.2397 0.0406 -0.3428 56 ILE F CG1 10196 C CG2 . ILE F 56 ? 1.6173 1.0846 2.0669 -0.2673 0.0236 -0.3592 56 ILE F CG2 10197 C CD1 . ILE F 56 ? 1.6009 1.0348 2.0103 -0.2350 0.0318 -0.3534 56 ILE F CD1 10198 N N . ASP F 57 ? 1.5251 1.1588 2.0726 -0.2431 -0.0152 -0.3311 57 ASP F N 10199 C CA . ASP F 57 ? 1.5293 1.1985 2.0897 -0.2494 -0.0320 -0.3377 57 ASP F CA 10200 C C . ASP F 57 ? 1.5095 1.2238 2.1143 -0.2644 -0.0249 -0.3253 57 ASP F C 10201 O O . ASP F 57 ? 1.5155 1.2413 2.1310 -0.2772 -0.0306 -0.3285 57 ASP F O 10202 C CB . ASP F 57 ? 1.5203 1.2255 2.0851 -0.2324 -0.0544 -0.3489 57 ASP F CB 10203 C CG . ASP F 57 ? 1.5551 1.2129 2.0770 -0.2223 -0.0732 -0.3572 57 ASP F CG 10204 O OD1 . ASP F 57 ? 1.5970 1.2045 2.0788 -0.2369 -0.0782 -0.3595 57 ASP F OD1 10205 O OD2 . ASP F 57 ? 1.5441 1.2135 2.0705 -0.2039 -0.0838 -0.3615 57 ASP F OD2 10206 N N . LYS F 58 ? 1.7262 0.5026 1.5073 0.0421 0.1568 -0.0856 58 LYS F N 10207 C CA . LYS F 58 ? 1.6783 0.5178 1.4687 0.0519 0.1870 -0.1115 58 LYS F CA 10208 C C . LYS F 58 ? 1.5622 0.5226 1.3651 0.0278 0.1571 -0.0973 58 LYS F C 10209 O O . LYS F 58 ? 1.5000 0.5314 1.3377 0.0457 0.1718 -0.1034 58 LYS F O 10210 C CB . LYS F 58 ? 1.7715 0.5293 1.4562 0.0240 0.2165 -0.1559 58 LYS F CB 10211 C CG . LYS F 58 ? 1.7808 0.5404 1.4505 0.0455 0.2656 -0.1856 58 LYS F CG 10212 C CD . LYS F 58 ? 1.9101 0.5535 1.5717 0.0825 0.3316 -0.2120 58 LYS F CD 10213 C CE . LYS F 58 ? 1.8903 0.5486 1.6951 0.1392 0.3417 -0.1856 58 LYS F CE 10214 N NZ . LYS F 58 ? 2.0196 0.5614 1.8348 0.1772 0.4134 -0.2143 58 LYS F NZ 10215 N N . MET F 59 ? 1.5496 0.5259 1.3246 -0.0138 0.1223 -0.0798 59 MET F N 10216 C CA . MET F 59 ? 1.4459 0.5264 1.2327 -0.0402 0.1009 -0.0696 59 MET F CA 10217 C C . MET F 59 ? 1.3754 0.5095 1.2118 -0.0223 0.0780 -0.0309 59 MET F C 10218 O O . MET F 59 ? 1.2972 0.5146 1.1463 -0.0365 0.0670 -0.0231 59 MET F O 10219 C CB . MET F 59 ? 1.4730 0.5426 1.2152 -0.0995 0.0871 -0.0770 59 MET F CB 10220 C CG . MET F 59 ? 1.5356 0.5632 1.2268 -0.1258 0.0903 -0.1153 59 MET F CG 10221 S SD . MET F 59 ? 1.4870 0.5899 1.1746 -0.1228 0.0849 -0.1379 59 MET F SD 10222 C CE . MET F 59 ? 1.3587 0.5875 1.1129 -0.1509 0.0580 -0.1178 59 MET F CE 10223 N N . ASN F 60 ? 1.4127 0.4909 1.2744 0.0088 0.0656 -0.0067 60 ASN F N 10224 C CA . ASN F 60 ? 1.3784 0.4841 1.2704 0.0232 0.0290 0.0320 60 ASN F CA 10225 C C . ASN F 60 ? 1.2854 0.4795 1.2661 0.0625 0.0254 0.0354 60 ASN F C 10226 O O . ASN F 60 ? 1.2611 0.4766 1.2706 0.0745 -0.0134 0.0665 60 ASN F O 10227 C CB . ASN F 60 ? 1.4840 0.4844 1.3656 0.0393 -0.0009 0.0618 60 ASN F CB 10228 C CG . ASN F 60 ? 1.5157 0.4894 1.4909 0.0978 0.0019 0.0597 60 ASN F CG 10229 O OD1 . ASN F 60 ? 1.4578 0.4933 1.5076 0.1266 0.0338 0.0371 60 ASN F OD1 10230 N ND2 . ASN F 60 ? 1.6219 0.4954 1.5963 0.1155 -0.0278 0.0837 60 ASN F ND2 10231 N N . THR F 61 ? 1.2458 0.4785 1.2586 0.0780 0.0651 0.0036 61 THR F N 10232 C CA . THR F 61 ? 1.1658 0.4845 1.2573 0.1060 0.0739 0.0024 61 THR F CA 10233 C C . THR F 61 ? 1.0793 0.4737 1.1269 0.0741 0.0772 -0.0090 61 THR F C 10234 O O . THR F 61 ? 1.0324 0.4878 1.1159 0.0876 0.0950 -0.0190 61 THR F O 10235 C CB . THR F 61 ? 1.1999 0.5003 1.3453 0.1414 0.1288 -0.0261 61 THR F CB 10236 O OG1 . THR F 61 ? 1.1948 0.5031 1.2671 0.1184 0.1662 -0.0602 61 THR F OG1 10237 C CG2 . THR F 61 ? 1.3098 0.5048 1.4580 0.1604 0.1461 -0.0334 61 THR F CG2 10238 N N . GLN F 62 ? 1.0753 0.4615 1.0530 0.0316 0.0624 -0.0075 62 GLN F N 10239 C CA . GLN F 62 ? 1.0039 0.4541 0.9538 0.0009 0.0639 -0.0209 62 GLN F CA 10240 C C . GLN F 62 ? 0.9104 0.4397 0.8933 0.0066 0.0465 -0.0012 62 GLN F C 10241 O O . GLN F 62 ? 0.9156 0.4371 0.9179 0.0195 0.0224 0.0271 62 GLN F O 10242 C CB . GLN F 62 ? 1.0395 0.4590 0.9384 -0.0454 0.0578 -0.0243 62 GLN F CB 10243 C CG . GLN F 62 ? 0.9842 0.4708 0.8826 -0.0782 0.0548 -0.0372 62 GLN F CG 10244 C CD . GLN F 62 ? 1.0329 0.4877 0.9115 -0.1241 0.0549 -0.0489 62 GLN F CD 10245 O OE1 . GLN F 62 ? 1.1088 0.4834 0.9568 -0.1336 0.0591 -0.0515 62 GLN F OE1 10246 N NE2 . GLN F 62 ? 0.9872 0.5052 0.8960 -0.1529 0.0506 -0.0564 62 GLN F NE2 10247 N N . PHE F 63 ? 0.8364 0.4301 0.8181 -0.0037 0.0529 -0.0161 63 PHE F N 10248 C CA . PHE F 63 ? 0.7560 0.4215 0.7643 0.0014 0.0410 -0.0024 63 PHE F CA 10249 C C . PHE F 63 ? 0.7631 0.4278 0.7453 -0.0231 0.0240 0.0189 63 PHE F C 10250 O O . PHE F 63 ? 0.7893 0.4355 0.7401 -0.0561 0.0322 0.0130 63 PHE F O 10251 C CB . PHE F 63 ? 0.6991 0.4171 0.7005 -0.0074 0.0496 -0.0239 63 PHE F CB 10252 C CG . PHE F 63 ? 0.6214 0.4074 0.6474 -0.0015 0.0409 -0.0127 63 PHE F CG 10253 C CD1 . PHE F 63 ? 0.5945 0.4068 0.6578 0.0260 0.0480 -0.0092 63 PHE F CD1 10254 C CD2 . PHE F 63 ? 0.5912 0.4114 0.6086 -0.0251 0.0319 -0.0078 63 PHE F CD2 10255 C CE1 . PHE F 63 ? 0.5352 0.4039 0.6171 0.0282 0.0382 0.0003 63 PHE F CE1 10256 C CE2 . PHE F 63 ? 0.5381 0.4098 0.5697 -0.0198 0.0260 0.0003 63 PHE F CE2 10257 C CZ . PHE F 63 ? 0.5060 0.4007 0.5650 0.0060 0.0251 0.0052 63 PHE F CZ 10258 N N . GLU F 64 ? 0.7545 0.4313 0.7481 -0.0098 0.0028 0.0428 64 GLU F N 10259 C CA . GLU F 64 ? 0.7820 0.4374 0.7231 -0.0342 -0.0090 0.0625 64 GLU F CA 10260 C C . GLU F 64 ? 0.7049 0.4285 0.6575 -0.0350 -0.0087 0.0606 64 GLU F C 10261 O O . GLU F 64 ? 0.6529 0.4104 0.6462 -0.0104 -0.0266 0.0676 64 GLU F O 10262 C CB . GLU F 64 ? 0.8709 0.4527 0.7874 -0.0230 -0.0473 0.0944 64 GLU F CB 10263 C CG . GLU F 64 ? 0.9567 0.4642 0.8669 -0.0172 -0.0495 0.0973 64 GLU F CG 10264 C CD . GLU F 64 ? 1.0707 0.4853 0.9424 -0.0105 -0.0975 0.1328 64 GLU F CD 10265 O OE1 . GLU F 64 ? 1.0861 0.4967 0.9462 -0.0059 -0.1380 0.1554 64 GLU F OE1 10266 O OE2 . GLU F 64 ? 1.1666 0.5013 1.0126 -0.0114 -0.1010 0.1390 64 GLU F OE2 10267 N N . ALA F 65 ? 0.6903 0.4339 0.6197 -0.0635 0.0148 0.0497 65 ALA F N 10268 C CA . ALA F 65 ? 0.6376 0.4358 0.5740 -0.0658 0.0199 0.0464 65 ALA F CA 10269 C C . ALA F 65 ? 0.6846 0.4354 0.5569 -0.0734 0.0041 0.0703 65 ALA F C 10270 O O . ALA F 65 ? 0.7706 0.4356 0.5724 -0.0891 -0.0035 0.0883 65 ALA F O 10271 C CB . ALA F 65 ? 0.6160 0.4490 0.5712 -0.0907 0.0517 0.0254 65 ALA F CB 10272 N N . VAL F 66 ? 0.6395 0.4328 0.5227 -0.0647 -0.0039 0.0708 66 VAL F N 10273 C CA . VAL F 66 ? 0.7010 0.4435 0.5164 -0.0719 -0.0287 0.0918 66 VAL F CA 10274 C C . VAL F 66 ? 0.6666 0.4450 0.4720 -0.0819 -0.0022 0.0788 66 VAL F C 10275 O O . VAL F 66 ? 0.5880 0.4467 0.4634 -0.0662 0.0054 0.0630 66 VAL F O 10276 C CB . VAL F 66 ? 0.6892 0.4443 0.5506 -0.0441 -0.0817 0.1093 66 VAL F CB 10277 C CG1 . VAL F 66 ? 0.7533 0.4568 0.5454 -0.0554 -0.1199 0.1296 66 VAL F CG1 10278 C CG2 . VAL F 66 ? 0.7308 0.4460 0.6190 -0.0290 -0.1081 0.1227 66 VAL F CG2 10279 N N . GLY F 67 ? 0.7501 0.4552 0.4582 -0.1086 0.0141 0.0853 67 GLY F N 10280 C CA . GLY F 67 ? 0.7411 0.4648 0.4347 -0.1170 0.0451 0.0721 67 GLY F CA 10281 C C . GLY F 67 ? 0.7074 0.4580 0.4122 -0.0987 0.0014 0.0807 67 GLY F C 10282 O O . GLY F 67 ? 0.7756 0.4704 0.4322 -0.0985 -0.0504 0.1037 67 GLY F O 10283 N N . ARG F 68 ? 0.6073 0.4395 0.3816 -0.0844 0.0164 0.0637 68 ARG F N 10284 C CA . ARG F 68 ? 0.5805 0.4349 0.3631 -0.0726 -0.0143 0.0693 68 ARG F CA 10285 C C . ARG F 68 ? 0.5756 0.4348 0.3371 -0.0803 0.0231 0.0531 68 ARG F C 10286 O O . ARG F 68 ? 0.5415 0.4442 0.3550 -0.0783 0.0643 0.0335 68 ARG F O 10287 C CB . ARG F 68 ? 0.4833 0.4223 0.3694 -0.0451 -0.0317 0.0657 68 ARG F CB 10288 C CG . ARG F 68 ? 0.4941 0.4265 0.4164 -0.0331 -0.0617 0.0796 68 ARG F CG 10289 C CD . ARG F 68 ? 0.4285 0.4240 0.4425 -0.0088 -0.0704 0.0772 68 ARG F CD 10290 N NE . ARG F 68 ? 0.4384 0.4273 0.5018 0.0053 -0.0812 0.0839 68 ARG F NE 10291 C CZ . ARG F 68 ? 0.4311 0.4208 0.5042 0.0097 -0.0556 0.0711 68 ARG F CZ 10292 N NH1 . ARG F 68 ? 0.4082 0.4115 0.4566 -0.0003 -0.0259 0.0522 68 ARG F NH1 10293 N NH2 . ARG F 68 ? 0.4569 0.4302 0.5727 0.0244 -0.0634 0.0768 68 ARG F NH2 10294 N N . GLU F 69 ? 0.6180 0.4286 0.3102 -0.0890 0.0049 0.0609 69 GLU F N 10295 C CA . GLU F 69 ? 0.6391 0.4362 0.2996 -0.0959 0.0444 0.0447 69 GLU F CA 10296 C C . GLU F 69 ? 0.5591 0.4140 0.2720 -0.0778 0.0211 0.0424 69 GLU F C 10297 O O . GLU F 69 ? 0.5395 0.3997 0.2609 -0.0735 -0.0296 0.0584 69 GLU F O 10298 C CB . GLU F 69 ? 0.7949 0.4613 0.3019 -0.1266 0.0531 0.0511 69 GLU F CB 10299 C CG . GLU F 69 ? 0.8989 0.4876 0.3332 -0.1501 0.0895 0.0527 69 GLU F CG 10300 C CD . GLU F 69 ? 1.0768 0.5238 0.3464 -0.1843 0.1329 0.0486 69 GLU F CD 10301 O OE1 . GLU F 69 ? 1.0938 0.5373 0.3553 -0.1844 0.1756 0.0297 69 GLU F OE1 10302 O OE2 . GLU F 69 ? 1.2246 0.5505 0.3621 -0.2117 0.1269 0.0638 69 GLU F OE2 10303 N N . PHE F 70 ? 0.5175 0.4129 0.2748 -0.0679 0.0584 0.0229 70 PHE F N 10304 C CA . PHE F 70 ? 0.4674 0.4042 0.2621 -0.0522 0.0430 0.0197 70 PHE F CA 10305 C C . PHE F 70 ? 0.5145 0.4128 0.2710 -0.0567 0.0816 0.0043 70 PHE F C 10306 O O . PHE F 70 ? 0.5578 0.4273 0.3025 -0.0651 0.1333 -0.0097 70 PHE F O 10307 C CB . PHE F 70 ? 0.3751 0.3973 0.2712 -0.0290 0.0393 0.0127 70 PHE F CB 10308 C CG . PHE F 70 ? 0.3539 0.4035 0.2837 -0.0240 0.0158 0.0225 70 PHE F CG 10309 C CD1 . PHE F 70 ? 0.3328 0.3966 0.2795 -0.0179 -0.0151 0.0355 70 PHE F CD1 10310 C CD2 . PHE F 70 ? 0.3548 0.4118 0.3069 -0.0265 0.0303 0.0173 70 PHE F CD2 10311 C CE1 . PHE F 70 ? 0.3141 0.3967 0.3001 -0.0108 -0.0261 0.0417 70 PHE F CE1 10312 C CE2 . PHE F 70 ? 0.3335 0.4042 0.3104 -0.0209 0.0126 0.0243 70 PHE F CE2 10313 C CZ . PHE F 70 ? 0.3165 0.3984 0.3101 -0.0114 -0.0130 0.0359 70 PHE F CZ 10314 N N . ASN F 71 ? 0.5136 0.4074 0.2560 -0.0521 0.0624 0.0059 71 ASN F N 10315 C CA . ASN F 71 ? 0.5671 0.4177 0.2730 -0.0532 0.0977 -0.0094 71 ASN F CA 10316 C C . ASN F 71 ? 0.5053 0.4264 0.3148 -0.0253 0.1102 -0.0222 71 ASN F C 10317 O O . ASN F 71 ? 0.4183 0.4091 0.3049 -0.0096 0.0861 -0.0179 71 ASN F O 10318 C CB . ASN F 71 ? 0.6355 0.4198 0.2505 -0.0689 0.0652 -0.0001 71 ASN F CB 10319 C CG . ASN F 71 ? 0.5572 0.4005 0.2320 -0.0574 0.0184 0.0116 71 ASN F CG 10320 O OD1 . ASN F 71 ? 0.4894 0.4005 0.2463 -0.0352 0.0233 0.0072 71 ASN F OD1 10321 N ND2 . ASN F 71 ? 0.5967 0.4049 0.2279 -0.0755 -0.0280 0.0272 71 ASN F ND2 10322 N N . ASN F 72 ? 0.5603 0.4494 0.3628 -0.0195 0.1456 -0.0380 72 ASN F N 10323 C CA . ASN F 72 ? 0.5277 0.4720 0.4368 0.0086 0.1548 -0.0502 72 ASN F CA 10324 C C . ASN F 72 ? 0.4751 0.4527 0.4055 0.0245 0.1043 -0.0387 72 ASN F C 10325 O O . ASN F 72 ? 0.4473 0.4597 0.4536 0.0477 0.0955 -0.0442 72 ASN F O 10326 C CB . ASN F 72 ? 0.6163 0.5123 0.5273 0.0137 0.2138 -0.0720 72 ASN F CB 10327 C CG . ASN F 72 ? 0.6924 0.5272 0.5248 0.0127 0.2051 -0.0715 72 ASN F CG 10328 O OD1 . ASN F 72 ? 0.7493 0.5336 0.4748 -0.0098 0.1763 -0.0584 72 ASN F OD1 10329 N ND2 . ASN F 72 ? 0.7164 0.5528 0.6104 0.0371 0.2252 -0.0855 72 ASN F ND2 10330 N N . LEU F 73 ? 0.4708 0.4307 0.3377 0.0106 0.0708 -0.0225 73 LEU F N 10331 C CA . LEU F 73 ? 0.4346 0.4206 0.3191 0.0200 0.0349 -0.0113 73 LEU F CA 10332 C C . LEU F 73 ? 0.3835 0.4105 0.2880 0.0157 0.0101 0.0020 73 LEU F C 10333 O O . LEU F 73 ? 0.3728 0.4071 0.2761 0.0150 -0.0083 0.0121 73 LEU F O 10334 C CB . LEU F 73 ? 0.4886 0.4239 0.3106 0.0081 0.0250 -0.0063 73 LEU F CB 10335 C CG . LEU F 73 ? 0.5377 0.4321 0.3506 0.0214 0.0473 -0.0203 73 LEU F CG 10336 C CD1 . LEU F 73 ? 0.6075 0.4347 0.3392 0.0022 0.0394 -0.0173 73 LEU F CD1 10337 C CD2 . LEU F 73 ? 0.5064 0.4313 0.3818 0.0489 0.0327 -0.0204 73 LEU F CD2 10338 N N . GLU F 74 ? 0.3625 0.4094 0.2866 0.0124 0.0179 0.0004 74 GLU F N 10339 C CA . GLU F 74 ? 0.3222 0.4018 0.2704 0.0113 0.0021 0.0094 74 GLU F CA 10340 C C . GLU F 74 ? 0.3025 0.4138 0.2995 0.0228 0.0073 -0.0002 74 GLU F C 10341 O O . GLU F 74 ? 0.2893 0.4145 0.2993 0.0184 0.0066 0.0015 74 GLU F O 10342 C CB . GLU F 74 ? 0.3343 0.3948 0.2551 -0.0059 -0.0042 0.0193 74 GLU F CB 10343 C CG . GLU F 74 ? 0.3605 0.3933 0.2501 -0.0203 -0.0291 0.0325 74 GLU F CG 10344 C CD . GLU F 74 ? 0.4000 0.3981 0.2576 -0.0376 -0.0523 0.0450 74 GLU F CD 10345 O OE1 . GLU F 74 ? 0.4301 0.3886 0.2380 -0.0459 -0.0376 0.0410 74 GLU F OE1 10346 O OE2 . GLU F 74 ? 0.3988 0.4031 0.2840 -0.0444 -0.0868 0.0597 74 GLU F OE2 10347 N N . ARG F 75 ? 0.3021 0.4207 0.3312 0.0372 0.0058 -0.0099 75 ARG F N 10348 C CA . ARG F 75 ? 0.2929 0.4398 0.3843 0.0458 -0.0004 -0.0197 75 ARG F CA 10349 C C . ARG F 75 ? 0.2680 0.4209 0.3498 0.0466 -0.0277 -0.0151 75 ARG F C 10350 O O . ARG F 75 ? 0.2502 0.4192 0.3632 0.0429 -0.0312 -0.0206 75 ARG F O 10351 C CB . ARG F 75 ? 0.3211 0.4719 0.4674 0.0637 -0.0087 -0.0291 75 ARG F CB 10352 C CG . ARG F 75 ? 0.3476 0.5155 0.5733 0.0658 0.0266 -0.0450 75 ARG F CG 10353 C CD . ARG F 75 ? 0.3970 0.5295 0.5712 0.0510 0.0788 -0.0490 75 ARG F CD 10354 N NE . ARG F 75 ? 0.4415 0.5805 0.6807 0.0452 0.1300 -0.0657 75 ARG F NE 10355 C CZ . ARG F 75 ? 0.4816 0.6210 0.7971 0.0576 0.1669 -0.0826 75 ARG F CZ 10356 N NH1 . ARG F 75 ? 0.5096 0.6410 0.8433 0.0795 0.1503 -0.0840 75 ARG F NH1 10357 N NH2 . ARG F 75 ? 0.5214 0.6646 0.9012 0.0477 0.2266 -0.0989 75 ARG F NH2 10358 N N . ARG F 76 ? 0.2731 0.4023 0.3053 0.0487 -0.0415 -0.0065 76 ARG F N 10359 C CA . ARG F 76 ? 0.2820 0.3935 0.2814 0.0468 -0.0545 -0.0049 76 ARG F CA 10360 C C . ARG F 76 ? 0.2683 0.3934 0.2734 0.0375 -0.0354 -0.0038 76 ARG F C 10361 O O . ARG F 76 ? 0.2718 0.3926 0.2789 0.0356 -0.0424 -0.0100 76 ARG F O 10362 C CB . ARG F 76 ? 0.3069 0.3764 0.2424 0.0459 -0.0546 0.0031 76 ARG F CB 10363 C CG . ARG F 76 ? 0.3471 0.3822 0.2586 0.0559 -0.0838 0.0043 76 ARG F CG 10364 C CD . ARG F 76 ? 0.3811 0.3685 0.2241 0.0501 -0.0727 0.0142 76 ARG F CD 10365 N NE . ARG F 76 ? 0.3367 0.3522 0.2052 0.0422 -0.0445 0.0190 76 ARG F NE 10366 C CZ . ARG F 76 ? 0.3388 0.3420 0.1881 0.0287 -0.0195 0.0266 76 ARG F CZ 10367 N NH1 . ARG F 76 ? 0.4004 0.3577 0.1956 0.0212 -0.0023 0.0290 76 ARG F NH1 10368 N NH2 . ARG F 76 ? 0.2949 0.3231 0.1778 0.0199 -0.0105 0.0312 76 ARG F NH2 10369 N N . ILE F 77 ? 0.2610 0.3953 0.2696 0.0314 -0.0182 0.0046 77 ILE F N 10370 C CA . ILE F 77 ? 0.2590 0.4007 0.2821 0.0259 -0.0086 0.0086 77 ILE F CA 10371 C C . ILE F 77 ? 0.2545 0.4051 0.2970 0.0208 -0.0069 0.0037 77 ILE F C 10372 O O . ILE F 77 ? 0.2564 0.4045 0.3066 0.0184 -0.0042 0.0030 77 ILE F O 10373 C CB . ILE F 77 ? 0.2595 0.4031 0.2926 0.0203 -0.0062 0.0220 77 ILE F CB 10374 C CG1 . ILE F 77 ? 0.2818 0.4165 0.2982 0.0121 -0.0143 0.0264 77 ILE F CG1 10375 C CG2 . ILE F 77 ? 0.2778 0.4151 0.3095 0.0213 0.0034 0.0255 77 ILE F CG2 10376 C CD1 . ILE F 77 ? 0.3028 0.4285 0.3261 0.0018 -0.0306 0.0413 77 ILE F CD1 10377 N N . GLU F 78 ? 0.2629 0.4164 0.3131 0.0181 -0.0012 -0.0010 78 GLU F N 10378 C CA . GLU F 78 ? 0.2766 0.4339 0.3514 0.0097 0.0136 -0.0088 78 GLU F CA 10379 C C . GLU F 78 ? 0.2506 0.4248 0.3648 0.0120 0.0009 -0.0192 78 GLU F C 10380 O O . GLU F 78 ? 0.2540 0.4252 0.3779 0.0025 0.0073 -0.0212 78 GLU F O 10381 C CB . GLU F 78 ? 0.3160 0.4693 0.4043 0.0074 0.0364 -0.0171 78 GLU F CB 10382 C CG . GLU F 78 ? 0.3559 0.5068 0.4757 -0.0059 0.0692 -0.0270 78 GLU F CG 10383 C CD . GLU F 78 ? 0.4171 0.5594 0.5620 -0.0066 0.1077 -0.0396 78 GLU F CD 10384 O OE1 . GLU F 78 ? 0.4243 0.5953 0.6303 0.0107 0.0967 -0.0477 78 GLU F OE1 10385 O OE2 . GLU F 78 ? 0.4900 0.5849 0.5863 -0.0245 0.1502 -0.0415 78 GLU F OE2 10386 N N . ASN F 79 ? 0.2411 0.4213 0.3697 0.0225 -0.0231 -0.0248 79 ASN F N 10387 C CA . ASN F 79 ? 0.2551 0.4344 0.4058 0.0217 -0.0519 -0.0337 79 ASN F CA 10388 C C . ASN F 79 ? 0.2764 0.4256 0.3723 0.0171 -0.0539 -0.0317 79 ASN F C 10389 O O . ASN F 79 ? 0.2875 0.4317 0.3973 0.0078 -0.0596 -0.0387 79 ASN F O 10390 C CB . ASN F 79 ? 0.2778 0.4452 0.4288 0.0330 -0.0915 -0.0358 79 ASN F CB 10391 C CG . ASN F 79 ? 0.3132 0.4727 0.4960 0.0284 -0.1372 -0.0449 79 ASN F CG 10392 O OD1 . ASN F 79 ? 0.3685 0.4753 0.4775 0.0267 -0.1716 -0.0442 79 ASN F OD1 10393 N ND2 . ASN F 79 ? 0.2833 0.4853 0.5711 0.0226 -0.1359 -0.0542 79 ASN F ND2 10394 N N . LEU F 80 ? 0.2857 0.4124 0.3274 0.0228 -0.0437 -0.0236 80 LEU F N 10395 C CA . LEU F 80 ? 0.3200 0.4148 0.3213 0.0215 -0.0300 -0.0237 80 LEU F CA 10396 C C . LEU F 80 ? 0.3104 0.4163 0.3416 0.0161 -0.0149 -0.0222 80 LEU F C 10397 O O . LEU F 80 ? 0.3302 0.4108 0.3481 0.0118 -0.0151 -0.0299 80 LEU F O 10398 C CB . LEU F 80 ? 0.3291 0.4129 0.3057 0.0271 -0.0076 -0.0148 80 LEU F CB 10399 C CG . LEU F 80 ? 0.3758 0.4212 0.3220 0.0284 0.0222 -0.0175 80 LEU F CG 10400 C CD1 . LEU F 80 ? 0.3893 0.4273 0.3284 0.0302 0.0478 -0.0105 80 LEU F CD1 10401 C CD2 . LEU F 80 ? 0.3595 0.4201 0.3536 0.0310 0.0380 -0.0149 80 LEU F CD2 10402 N N . ASN F 81 ? 0.2913 0.4198 0.3479 0.0145 -0.0049 -0.0118 81 ASN F N 10403 C CA . ASN F 81 ? 0.2904 0.4121 0.3581 0.0074 0.0033 -0.0062 81 ASN F CA 10404 C C . ASN F 81 ? 0.3024 0.4215 0.3863 -0.0049 0.0022 -0.0176 81 ASN F C 10405 O O . ASN F 81 ? 0.3184 0.4153 0.3979 -0.0100 0.0061 -0.0182 81 ASN F O 10406 C CB . ASN F 81 ? 0.2908 0.4129 0.3526 0.0015 0.0063 0.0063 81 ASN F CB 10407 C CG . ASN F 81 ? 0.3096 0.4007 0.3567 -0.0085 0.0082 0.0163 81 ASN F CG 10408 O OD1 . ASN F 81 ? 0.3224 0.3983 0.3745 -0.0016 -0.0021 0.0270 81 ASN F OD1 10409 N ND2 . ASN F 81 ? 0.3248 0.3995 0.3566 -0.0250 0.0239 0.0132 81 ASN F ND2 10410 N N . LYS F 82 ? 0.2966 0.4386 0.4118 -0.0094 -0.0039 -0.0269 82 LYS F N 10411 C CA . LYS F 82 ? 0.3054 0.4560 0.4675 -0.0243 -0.0050 -0.0385 82 LYS F CA 10412 C C . LYS F 82 ? 0.3316 0.4600 0.4814 -0.0272 -0.0321 -0.0483 82 LYS F C 10413 O O . LYS F 82 ? 0.3495 0.4602 0.5045 -0.0408 -0.0281 -0.0527 82 LYS F O 10414 C CB . LYS F 82 ? 0.2973 0.4841 0.5274 -0.0248 -0.0067 -0.0471 82 LYS F CB 10415 C CG . LYS F 82 ? 0.3250 0.5293 0.6340 -0.0441 0.0047 -0.0587 82 LYS F CG 10416 C CD . LYS F 82 ? 0.3313 0.5788 0.7448 -0.0423 0.0094 -0.0695 82 LYS F CD 10417 C CE . LYS F 82 ? 0.3570 0.6264 0.8726 -0.0656 0.0285 -0.0821 82 LYS F CE 10418 N NZ . LYS F 82 ? 0.3679 0.6885 1.0268 -0.0617 0.0008 -0.0952 82 LYS F NZ 10419 N N . LYS F 83 ? 0.3385 0.4526 0.4567 -0.0173 -0.0597 -0.0518 83 LYS F N 10420 C CA . LYS F 83 ? 0.3905 0.4533 0.4563 -0.0224 -0.0865 -0.0616 83 LYS F CA 10421 C C . LYS F 83 ? 0.3973 0.4187 0.4153 -0.0233 -0.0595 -0.0621 83 LYS F C 10422 O O . LYS F 83 ? 0.4367 0.4205 0.4368 -0.0363 -0.0712 -0.0728 83 LYS F O 10423 C CB . LYS F 83 ? 0.4407 0.4662 0.4381 -0.0126 -0.1076 -0.0612 83 LYS F CB 10424 C CG . LYS F 83 ? 0.5009 0.5090 0.5048 -0.0191 -0.1683 -0.0683 83 LYS F CG 10425 C CD . LYS F 83 ? 0.4496 0.5301 0.5731 -0.0154 -0.1823 -0.0669 83 LYS F CD 10426 C CE . LYS F 83 ? 0.5093 0.5731 0.6617 -0.0180 -0.2561 -0.0719 83 LYS F CE 10427 N NZ . LYS F 83 ? 0.5845 0.5989 0.7109 -0.0389 -0.3012 -0.0825 83 LYS F NZ 10428 N N . MET F 84 ? 0.6885 0.4484 0.8520 -0.1227 0.1888 -0.1255 84 MET F N 10429 C CA . MET F 84 ? 0.6863 0.4375 0.8664 -0.1159 0.1803 -0.1331 84 MET F CA 10430 C C . MET F 84 ? 0.7039 0.4229 0.8593 -0.1163 0.1674 -0.1278 84 MET F C 10431 O O . MET F 84 ? 0.7041 0.4192 0.8715 -0.1140 0.1649 -0.1332 84 MET F O 10432 C CB . MET F 84 ? 0.6908 0.4426 0.9033 -0.1073 0.1659 -0.1397 84 MET F CB 10433 C CG . MET F 84 ? 0.7051 0.4546 0.9790 -0.0990 0.1550 -0.1572 84 MET F CG 10434 S SD . MET F 84 ? 0.7543 0.4640 1.0543 -0.0864 0.0974 -0.1569 84 MET F SD 10435 C CE . MET F 84 ? 0.8042 0.4512 1.0232 -0.0916 0.0703 -0.1402 84 MET F CE 10436 N N . GLU F 85 ? 0.7244 0.4079 0.8349 -0.1235 0.1637 -0.1193 85 GLU F N 10437 C CA . GLU F 85 ? 0.7757 0.4011 0.8337 -0.1318 0.1551 -0.1150 85 GLU F CA 10438 C C . GLU F 85 ? 0.7593 0.3922 0.8167 -0.1413 0.1823 -0.1171 85 GLU F C 10439 O O . GLU F 85 ? 0.7793 0.3886 0.8210 -0.1423 0.1753 -0.1171 85 GLU F O 10440 C CB . GLU F 85 ? 0.8502 0.4030 0.8302 -0.1465 0.1500 -0.1083 85 GLU F CB 10441 C CG . GLU F 85 ? 0.8853 0.4044 0.8591 -0.1363 0.1009 -0.1051 85 GLU F CG 10442 C CD . GLU F 85 ? 1.0065 0.4075 0.8615 -0.1565 0.0785 -0.0956 85 GLU F CD 10443 O OE1 . GLU F 85 ? 1.0511 0.4122 0.8354 -0.1816 0.1234 -0.0954 85 GLU F OE1 10444 O OE2 . GLU F 85 ? 1.0716 0.4079 0.9046 -0.1503 0.0151 -0.0915 85 GLU F OE2 10445 N N . ASP F 86 ? 0.7215 0.3853 0.8083 -0.1476 0.2073 -0.1208 86 ASP F N 10446 C CA . ASP F 86 ? 0.7060 0.3845 0.8262 -0.1533 0.2222 -0.1269 86 ASP F CA 10447 C C . ASP F 86 ? 0.6777 0.3789 0.8157 -0.1427 0.2039 -0.1259 86 ASP F C 10448 O O . ASP F 86 ? 0.6864 0.3777 0.8247 -0.1456 0.2054 -0.1278 86 ASP F O 10449 C CB . ASP F 86 ? 0.6792 0.3860 0.8577 -0.1582 0.2348 -0.1347 86 ASP F CB 10450 C CG . ASP F 86 ? 0.7135 0.3928 0.9058 -0.1780 0.2744 -0.1487 86 ASP F CG 10451 O OD1 . ASP F 86 ? 0.7528 0.4024 0.9350 -0.1898 0.2944 -0.1560 86 ASP F OD1 10452 O OD2 . ASP F 86 ? 0.7119 0.3949 0.9282 -0.1848 0.2923 -0.1560 86 ASP F OD2 10453 N N . GLY F 87 ? 0.6519 0.3739 0.7981 -0.1348 0.1933 -0.1255 87 GLY F N 10454 C CA . GLY F 87 ? 0.6497 0.3734 0.7953 -0.1331 0.1892 -0.1296 87 GLY F CA 10455 C C . GLY F 87 ? 0.6607 0.3710 0.8037 -0.1287 0.1868 -0.1328 87 GLY F C 10456 O O . GLY F 87 ? 0.6681 0.3709 0.8060 -0.1320 0.1879 -0.1347 87 GLY F O 10457 N N . PHE F 88 ? 0.6679 0.3670 0.8148 -0.1216 0.1753 -0.1336 88 PHE F N 10458 C CA . PHE F 88 ? 0.6885 0.3662 0.8434 -0.1158 0.1596 -0.1380 88 PHE F CA 10459 C C . PHE F 88 ? 0.7163 0.3624 0.8287 -0.1232 0.1584 -0.1300 88 PHE F C 10460 O O . PHE F 88 ? 0.7232 0.3619 0.8416 -0.1213 0.1541 -0.1336 88 PHE F O 10461 C CB . PHE F 88 ? 0.7104 0.3654 0.8852 -0.1063 0.1275 -0.1411 88 PHE F CB 10462 C CG . PHE F 88 ? 0.6862 0.3716 0.9430 -0.0977 0.1312 -0.1611 88 PHE F CG 10463 C CD1 . PHE F 88 ? 0.6811 0.3785 0.9921 -0.0968 0.1472 -0.1806 88 PHE F CD1 10464 C CD2 . PHE F 88 ? 0.6754 0.3734 0.9599 -0.0940 0.1275 -0.1652 88 PHE F CD2 10465 C CE1 . PHE F 88 ? 0.6718 0.3893 1.0694 -0.0958 0.1682 -0.2086 88 PHE F CE1 10466 C CE2 . PHE F 88 ? 0.6595 0.3827 1.0330 -0.0902 0.1421 -0.1907 88 PHE F CE2 10467 C CZ . PHE F 88 ? 0.6606 0.3917 1.0935 -0.0929 0.1673 -0.2149 88 PHE F CZ 10468 N N . LEU F 89 ? 0.7367 0.3600 0.8096 -0.1348 0.1696 -0.1232 89 LEU F N 10469 C CA . LEU F 89 ? 0.7777 0.3610 0.8108 -0.1490 0.1835 -0.1220 89 LEU F CA 10470 C C . LEU F 89 ? 0.7430 0.3617 0.8169 -0.1501 0.1989 -0.1271 89 LEU F C 10471 O O . LEU F 89 ? 0.7653 0.3622 0.8249 -0.1552 0.2023 -0.1283 89 LEU F O 10472 C CB . LEU F 89 ? 0.8236 0.3638 0.8111 -0.1690 0.2096 -0.1227 89 LEU F CB 10473 C CG . LEU F 89 ? 0.8921 0.3643 0.8056 -0.1748 0.1885 -0.1155 89 LEU F CG 10474 C CD1 . LEU F 89 ? 0.9356 0.3695 0.8075 -0.1990 0.2293 -0.1206 89 LEU F CD1 10475 C CD2 . LEU F 89 ? 0.9823 0.3641 0.8150 -0.1813 0.1550 -0.1092 89 LEU F CD2 10476 N N . ASP F 90 ? 0.7013 0.3621 0.8185 -0.1466 0.2005 -0.1294 90 ASP F N 10477 C CA . ASP F 90 ? 0.6890 0.3640 0.8355 -0.1480 0.1958 -0.1326 90 ASP F CA 10478 C C . ASP F 90 ? 0.6946 0.3642 0.8238 -0.1426 0.1860 -0.1325 90 ASP F C 10479 O O . ASP F 90 ? 0.7043 0.3642 0.8343 -0.1457 0.1840 -0.1338 90 ASP F O 10480 C CB . ASP F 90 ? 0.6736 0.3656 0.8482 -0.1484 0.1832 -0.1332 90 ASP F CB 10481 C CG . ASP F 90 ? 0.6653 0.3668 0.8898 -0.1545 0.1933 -0.1398 90 ASP F CG 10482 O OD1 . ASP F 90 ? 0.6787 0.3689 0.9210 -0.1640 0.2200 -0.1486 90 ASP F OD1 10483 O OD2 . ASP F 90 ? 0.6558 0.3684 0.9020 -0.1530 0.1790 -0.1395 90 ASP F OD2 10484 N N . VAL F 91 ? 0.6909 0.3652 0.8148 -0.1365 0.1847 -0.1352 91 VAL F N 10485 C CA . VAL F 91 ? 0.7030 0.3693 0.8276 -0.1349 0.1880 -0.1438 91 VAL F CA 10486 C C . VAL F 91 ? 0.7165 0.3682 0.8414 -0.1304 0.1798 -0.1430 91 VAL F C 10487 O O . VAL F 91 ? 0.7255 0.3685 0.8448 -0.1334 0.1823 -0.1455 91 VAL F O 10488 C CB . VAL F 91 ? 0.6991 0.3735 0.8511 -0.1308 0.1973 -0.1567 91 VAL F CB 10489 C CG1 . VAL F 91 ? 0.7133 0.3796 0.8979 -0.1296 0.2077 -0.1744 91 VAL F CG1 10490 C CG2 . VAL F 91 ? 0.7069 0.3777 0.8374 -0.1419 0.2125 -0.1599 91 VAL F CG2 10491 N N . TRP F 92 ? 0.7337 0.3679 0.8510 -0.1259 0.1657 -0.1386 92 TRP F N 10492 C CA . TRP F 92 ? 0.7733 0.3695 0.8717 -0.1244 0.1477 -0.1369 92 TRP F CA 10493 C C . TRP F 92 ? 0.7945 0.3696 0.8547 -0.1369 0.1616 -0.1312 92 TRP F C 10494 O O . TRP F 92 ? 0.8152 0.3673 0.8626 -0.1374 0.1545 -0.1316 92 TRP F O 10495 C CB . TRP F 92 ? 0.8185 0.3686 0.8927 -0.1216 0.1158 -0.1325 92 TRP F CB 10496 C CG . TRP F 92 ? 0.8073 0.3716 0.9526 -0.1061 0.0904 -0.1453 92 TRP F CG 10497 C CD1 . TRP F 92 ? 0.7923 0.3723 0.9712 -0.1004 0.0835 -0.1497 92 TRP F CD1 10498 C CD2 . TRP F 92 ? 0.8103 0.3757 1.0237 -0.0955 0.0725 -0.1613 92 TRP F CD2 10499 N NE1 . TRP F 92 ? 0.7869 0.3782 1.0607 -0.0872 0.0637 -0.1702 92 TRP F NE1 10500 C CE2 . TRP F 92 ? 0.7968 0.3800 1.0999 -0.0842 0.0578 -0.1794 92 TRP F CE2 10501 C CE3 . TRP F 92 ? 0.8219 0.3753 1.0411 -0.0949 0.0693 -0.1654 92 TRP F CE3 10502 C CZ2 . TRP F 92 ? 0.7960 0.3865 1.2121 -0.0732 0.0436 -0.2065 92 TRP F CZ2 10503 C CZ3 . TRP F 92 ? 0.8216 0.3814 1.1390 -0.0833 0.0531 -0.1886 92 TRP F CZ3 10504 C CH2 . TRP F 92 ? 0.8093 0.3881 1.2326 -0.0730 0.0420 -0.2112 92 TRP F CH2 10505 N N . THR F 93 ? 0.7905 0.3732 0.8468 -0.1475 0.1832 -0.1298 93 THR F N 10506 C CA . THR F 93 ? 0.8048 0.3772 0.8626 -0.1609 0.2049 -0.1335 93 THR F CA 10507 C C . THR F 93 ? 0.7805 0.3805 0.8726 -0.1553 0.1972 -0.1360 93 THR F C 10508 O O . THR F 93 ? 0.7970 0.3805 0.8834 -0.1600 0.2012 -0.1380 93 THR F O 10509 C CB . THR F 93 ? 0.7964 0.3801 0.8851 -0.1722 0.2301 -0.1404 93 THR F CB 10510 O OG1 . THR F 93 ? 0.8461 0.3807 0.8781 -0.1855 0.2465 -0.1398 93 THR F OG1 10511 C CG2 . THR F 93 ? 0.7984 0.3839 0.9373 -0.1847 0.2528 -0.1536 93 THR F CG2 10512 N N . TYR F 94 ? 0.7588 0.3857 0.8709 -0.1490 0.1865 -0.1360 94 TYR F N 10513 C CA . TYR F 94 ? 0.7686 0.3934 0.8805 -0.1498 0.1763 -0.1377 94 TYR F CA 10514 C C . TYR F 94 ? 0.7840 0.3961 0.8792 -0.1459 0.1780 -0.1405 94 TYR F C 10515 O O . TYR F 94 ? 0.7950 0.3955 0.8860 -0.1493 0.1754 -0.1412 94 TYR F O 10516 C CB . TYR F 94 ? 0.7759 0.3986 0.8737 -0.1522 0.1695 -0.1384 94 TYR F CB 10517 C CG . TYR F 94 ? 0.8209 0.4074 0.8795 -0.1621 0.1619 -0.1410 94 TYR F CG 10518 C CD1 . TYR F 94 ? 0.8441 0.4151 0.8791 -0.1652 0.1829 -0.1506 94 TYR F CD1 10519 C CD2 . TYR F 94 ? 0.8560 0.4106 0.9022 -0.1713 0.1312 -0.1370 94 TYR F CD2 10520 C CE1 . TYR F 94 ? 0.9058 0.4237 0.8837 -0.1819 0.1861 -0.1559 94 TYR F CE1 10521 C CE2 . TYR F 94 ? 0.9249 0.4176 0.9043 -0.1862 0.1179 -0.1377 94 TYR F CE2 10522 C CZ . TYR F 94 ? 0.9531 0.4241 0.8869 -0.1939 0.1518 -0.1469 94 TYR F CZ 10523 O OH . TYR F 94 ? 1.0418 0.4326 0.8894 -0.2160 0.1484 -0.1503 94 TYR F OH 10524 N N . ASN F 95 ? 0.7878 0.4015 0.8878 -0.1380 0.1784 -0.1447 95 ASN F N 10525 C CA . ASN F 95 ? 0.8051 0.4078 0.9179 -0.1323 0.1749 -0.1530 95 ASN F CA 10526 C C . ASN F 95 ? 0.8314 0.4083 0.9236 -0.1323 0.1629 -0.1465 95 ASN F C 10527 O O . ASN F 95 ? 0.8410 0.4089 0.9376 -0.1313 0.1614 -0.1512 95 ASN F O 10528 C CB . ASN F 95 ? 0.8035 0.4107 0.9589 -0.1220 0.1668 -0.1637 95 ASN F CB 10529 C CG . ASN F 95 ? 0.7958 0.4195 0.9779 -0.1268 0.1931 -0.1793 95 ASN F CG 10530 O OD1 . ASN F 95 ? 0.8161 0.4282 0.9708 -0.1401 0.2169 -0.1854 95 ASN F OD1 10531 N ND2 . ASN F 95 ? 0.7856 0.4217 1.0104 -0.1198 0.1889 -0.1872 95 ASN F ND2 10532 N N . ALA F 96 ? 0.8563 0.4099 0.9164 -0.1378 0.1597 -0.1378 96 ALA F N 10533 C CA . ALA F 96 ? 0.9103 0.4150 0.9246 -0.1470 0.1572 -0.1334 96 ALA F CA 10534 C C . ALA F 96 ? 0.9038 0.4209 0.9286 -0.1556 0.1780 -0.1360 96 ALA F C 10535 O O . ALA F 96 ? 0.9253 0.4228 0.9373 -0.1567 0.1740 -0.1365 96 ALA F O 10536 C CB . ALA F 96 ? 0.9623 0.4149 0.9176 -0.1614 0.1631 -0.1282 96 ALA F CB 10537 N N . GLU F 97 ? 0.8831 0.4300 0.9413 -0.1607 0.1931 -0.1389 97 GLU F N 10538 C CA . GLU F 97 ? 0.8820 0.4380 0.9747 -0.1678 0.2007 -0.1446 97 GLU F CA 10539 C C . GLU F 97 ? 0.8796 0.4439 0.9746 -0.1608 0.1822 -0.1434 97 GLU F C 10540 O O . GLU F 97 ? 0.8924 0.4442 0.9867 -0.1640 0.1822 -0.1453 97 GLU F O 10541 C CB . GLU F 97 ? 0.8607 0.4407 1.0109 -0.1724 0.2046 -0.1511 97 GLU F CB 10542 C CG . GLU F 97 ? 0.8821 0.4464 1.0446 -0.1874 0.2400 -0.1610 97 GLU F CG 10543 C CD . GLU F 97 ? 0.8607 0.4544 1.1032 -0.1893 0.2411 -0.1714 97 GLU F CD 10544 O OE1 . GLU F 97 ? 0.8403 0.4572 1.1097 -0.1781 0.2034 -0.1660 97 GLU F OE1 10545 O OE2 . GLU F 97 ? 0.8842 0.4654 1.1571 -0.2055 0.2805 -0.1871 97 GLU F OE2 10546 N N . LEU F 98 ? 0.8794 0.4539 0.9678 -0.1557 0.1722 -0.1424 98 LEU F N 10547 C CA . LEU F 98 ? 0.9057 0.4646 0.9729 -0.1581 0.1655 -0.1451 98 LEU F CA 10548 C C . LEU F 98 ? 0.9176 0.4674 0.9771 -0.1538 0.1724 -0.1493 98 LEU F C 10549 O O . LEU F 98 ? 0.9371 0.4689 0.9817 -0.1589 0.1706 -0.1517 98 LEU F O 10550 C CB . LEU F 98 ? 0.9221 0.4727 0.9658 -0.1618 0.1702 -0.1490 98 LEU F CB 10551 C CG . LEU F 98 ? 0.9781 0.4834 0.9714 -0.1757 0.1767 -0.1564 98 LEU F CG 10552 C CD1 . LEU F 98 ? 1.0184 0.4830 0.9794 -0.1867 0.1444 -0.1487 98 LEU F CD1 10553 C CD2 . LEU F 98 ? 1.0136 0.4940 0.9728 -0.1874 0.1994 -0.1668 98 LEU F CD2 10554 N N . LEU F 99 ? 0.9179 0.4711 0.9877 -0.1451 0.1727 -0.1506 99 LEU F N 10555 C CA . LEU F 99 ? 0.9409 0.4793 1.0181 -0.1390 0.1669 -0.1564 99 LEU F CA 10556 C C . LEU F 99 ? 0.9654 0.4819 1.0182 -0.1436 0.1621 -0.1496 99 LEU F C 10557 O O . LEU F 99 ? 0.9786 0.4842 1.0324 -0.1424 0.1595 -0.1536 99 LEU F O 10558 C CB . LEU F 99 ? 0.9485 0.4791 1.0495 -0.1281 0.1486 -0.1601 99 LEU F CB 10559 C CG . LEU F 99 ? 0.9719 0.4817 1.1053 -0.1192 0.1279 -0.1702 99 LEU F CG 10560 C CD1 . LEU F 99 ? 0.9609 0.4898 1.1445 -0.1202 0.1545 -0.1916 99 LEU F CD1 10561 C CD2 . LEU F 99 ? 0.9953 0.4814 1.1590 -0.1079 0.0885 -0.1731 99 LEU F CD2 10562 N N . VAL F 100 ? 0.9829 0.4885 1.0169 -0.1521 0.1682 -0.1430 100 VAL F N 10563 C CA . VAL F 100 ? 1.0158 0.4916 1.0273 -0.1632 0.1774 -0.1422 100 VAL F CA 10564 C C . VAL F 100 ? 1.0042 0.4992 1.0459 -0.1662 0.1811 -0.1461 100 VAL F C 10565 O O . VAL F 100 ? 1.0235 0.5011 1.0545 -0.1686 0.1807 -0.1470 100 VAL F O 10566 C CB . VAL F 100 ? 1.0427 0.4909 1.0322 -0.1798 0.2009 -0.1434 100 VAL F CB 10567 C CG1 . VAL F 100 ? 1.0775 0.4952 1.0608 -0.1985 0.2288 -0.1514 100 VAL F CG1 10568 C CG2 . VAL F 100 ? 1.0947 0.4878 1.0182 -0.1824 0.1872 -0.1369 100 VAL F CG2 10569 N N . LEU F 101 ? 0.9912 0.5110 1.0654 -0.1667 0.1763 -0.1476 101 LEU F N 10570 C CA . LEU F 101 ? 1.0085 0.5262 1.1046 -0.1708 0.1616 -0.1502 101 LEU F CA 10571 C C . LEU F 101 ? 1.0439 0.5443 1.1019 -0.1686 0.1540 -0.1491 101 LEU F C 10572 O O . LEU F 101 ? 1.0521 0.5385 1.1096 -0.1719 0.1488 -0.1504 101 LEU F O 10573 C CB . LEU F 101 ? 1.0024 0.5250 1.1239 -0.1729 0.1397 -0.1503 101 LEU F CB 10574 C CG . LEU F 101 ? 0.9857 0.5279 1.1740 -0.1763 0.1470 -0.1576 101 LEU F CG 10575 C CD1 . LEU F 101 ? 0.9905 0.5281 1.2085 -0.1767 0.1092 -0.1575 101 LEU F CD1 10576 C CD2 . LEU F 101 ? 0.9881 0.5300 1.2402 -0.1854 0.1657 -0.1717 101 LEU F CD2 10577 N N . MET F 102 ? 1.0625 0.5614 1.0961 -0.1653 0.1596 -0.1510 102 MET F N 10578 C CA . MET F 102 ? 1.1031 0.5802 1.1104 -0.1683 0.1683 -0.1587 102 MET F CA 10579 C C . MET F 102 ? 1.1008 0.5800 1.1233 -0.1604 0.1721 -0.1619 102 MET F C 10580 O O . MET F 102 ? 1.1203 0.5804 1.1296 -0.1645 0.1757 -0.1671 102 MET F O 10581 C CB . MET F 102 ? 1.1230 0.5967 1.1239 -0.1708 0.1879 -0.1695 102 MET F CB 10582 C CG . MET F 102 ? 1.1742 0.6116 1.1224 -0.1873 0.1848 -0.1682 102 MET F CG 10583 S SD . MET F 102 ? 1.2025 0.6412 1.1493 -0.1920 0.2129 -0.1801 102 MET F SD 10584 C CE . MET F 102 ? 1.1935 0.6473 1.2015 -0.1865 0.2513 -0.2064 102 MET F CE 10585 N N . GLU F 103 ? 1.0906 0.5782 1.1290 -0.1515 0.1666 -0.1586 103 GLU F N 10586 C CA . GLU F 103 ? 1.1115 0.5794 1.1502 -0.1457 0.1560 -0.1596 103 GLU F CA 10587 C C . GLU F 103 ? 1.1287 0.5795 1.1437 -0.1538 0.1573 -0.1537 103 GLU F C 10588 O O . GLU F 103 ? 1.1459 0.5804 1.1566 -0.1521 0.1522 -0.1564 103 GLU F O 10589 C CB . GLU F 103 ? 1.1241 0.5718 1.1553 -0.1402 0.1371 -0.1550 103 GLU F CB 10590 N N . ASN F 104 ? 1.1285 0.5834 1.1425 -0.1633 0.1664 -0.1497 104 ASN F N 10591 C CA . ASN F 104 ? 1.1451 0.5872 1.1621 -0.1735 0.1745 -0.1512 104 ASN F CA 10592 C C . ASN F 104 ? 1.1507 0.5975 1.1779 -0.1728 0.1636 -0.1532 104 ASN F C 10593 O O . ASN F 104 ? 1.1565 0.5877 1.1769 -0.1756 0.1642 -0.1544 104 ASN F O 10594 C CB . ASN F 104 ? 1.1375 0.5879 1.1904 -0.1850 0.1913 -0.1565 104 ASN F CB 10595 C CG . ASN F 104 ? 1.1673 0.5867 1.1860 -0.1959 0.2148 -0.1576 104 ASN F CG 10596 O OD1 . ASN F 104 ? 1.2076 0.5834 1.1614 -0.1964 0.2080 -0.1512 104 ASN F OD1 10597 N ND2 . ASN F 104 ? 1.1587 0.5868 1.2187 -0.2074 0.2389 -0.1675 104 ASN F ND2 10598 N N . GLU F 105 ? 1.1567 0.6097 1.1840 -0.1727 0.1528 -0.1534 105 GLU F N 10599 C CA . GLU F 105 ? 1.2028 0.6298 1.2061 -0.1792 0.1391 -0.1546 105 GLU F CA 10600 C C . GLU F 105 ? 1.2234 0.6373 1.2026 -0.1769 0.1525 -0.1600 105 GLU F C 10601 O O . GLU F 105 ? 1.2377 0.6330 1.2057 -0.1809 0.1475 -0.1606 105 GLU F O 10602 C CB . GLU F 105 ? 1.2405 0.6426 1.2092 -0.1874 0.1269 -0.1542 105 GLU F CB 10603 C CG . GLU F 105 ? 1.3149 0.6565 1.2347 -0.2022 0.0977 -0.1526 105 GLU F CG 10604 C CD . GLU F 105 ? 1.3706 0.6734 1.2709 -0.2117 0.0582 -0.1476 105 GLU F CD 10605 O OE1 . GLU F 105 ? 1.3490 0.6735 1.3247 -0.2060 0.0276 -0.1466 105 GLU F OE1 10606 O OE2 . GLU F 105 ? 1.4457 0.6877 1.2584 -0.2277 0.0591 -0.1480 105 GLU F OE2 10607 N N . ARG F 106 ? 1.2175 0.6414 1.2043 -0.1702 0.1677 -0.1671 106 ARG F N 10608 C CA . ARG F 106 ? 1.2396 0.6551 1.2387 -0.1662 0.1795 -0.1795 106 ARG F CA 10609 C C . ARG F 106 ? 1.2268 0.6395 1.2349 -0.1587 0.1652 -0.1740 106 ARG F C 10610 O O . ARG F 106 ? 1.2405 0.6384 1.2474 -0.1597 0.1677 -0.1801 106 ARG F O 10611 C CB . ARG F 106 ? 1.2462 0.6758 1.2898 -0.1585 0.1913 -0.1941 106 ARG F CB 10612 C CG . ARG F 106 ? 1.2865 0.7018 1.3145 -0.1729 0.2222 -0.2086 106 ARG F CG 10613 C CD . ARG F 106 ? 1.3016 0.7270 1.4047 -0.1686 0.2475 -0.2366 106 ARG F CD 10614 N NE . ARG F 106 ? 1.3579 0.7586 1.4379 -0.1891 0.2907 -0.2547 106 ARG F NE 10615 C CZ . ARG F 106 ? 1.3663 0.7751 1.5219 -0.1910 0.3253 -0.2853 106 ARG F CZ 10616 N NH1 . ARG F 106 ? 1.3322 0.7764 1.6083 -0.1694 0.3087 -0.3012 106 ARG F NH1 10617 N NH2 . ARG F 106 ? 1.4201 0.7897 1.5315 -0.2173 0.3738 -0.3028 106 ARG F NH2 10618 N N . THR F 107 ? 1.2050 0.6183 1.2091 -0.1556 0.1540 -0.1639 107 THR F N 10619 C CA . THR F 107 ? 1.2201 0.6028 1.2028 -0.1561 0.1429 -0.1588 107 THR F CA 10620 C C . THR F 107 ? 1.2154 0.5903 1.1851 -0.1658 0.1511 -0.1568 107 THR F C 10621 O O . THR F 107 ? 1.2395 0.5895 1.1944 -0.1658 0.1449 -0.1572 107 THR F O 10622 C CB . THR F 107 ? 1.2416 0.5965 1.1907 -0.1616 0.1387 -0.1508 107 THR F CB 10623 O OG1 . THR F 107 ? 1.2322 0.5896 1.1973 -0.1511 0.1212 -0.1524 107 THR F OG1 10624 C CG2 . THR F 107 ? 1.3064 0.5956 1.1978 -0.1708 0.1281 -0.1462 107 THR F CG2 10625 N N . LEU F 108 ? 1.1922 0.5843 1.1769 -0.1736 0.1586 -0.1563 108 LEU F N 10626 C CA . LEU F 108 ? 1.1991 0.5844 1.1951 -0.1818 0.1585 -0.1581 108 LEU F CA 10627 C C . LEU F 108 ? 1.2167 0.5917 1.1969 -0.1803 0.1483 -0.1599 108 LEU F C 10628 O O . LEU F 108 ? 1.2233 0.5837 1.1979 -0.1828 0.1472 -0.1608 108 LEU F O 10629 C CB . LEU F 108 ? 1.1811 0.5814 1.2241 -0.1890 0.1551 -0.1615 108 LEU F CB 10630 C CG . LEU F 108 ? 1.1768 0.5816 1.2473 -0.1972 0.1799 -0.1673 108 LEU F CG 10631 C CD1 . LEU F 108 ? 1.1563 0.5814 1.3083 -0.2020 0.1718 -0.1771 108 LEU F CD1 10632 C CD2 . LEU F 108 ? 1.2169 0.5875 1.2677 -0.2111 0.2093 -0.1735 108 LEU F CD2 10633 N N . ASP F 109 ? 1.2313 0.6031 1.1951 -0.1806 0.1470 -0.1626 109 ASP F N 10634 C CA . ASP F 109 ? 1.2690 0.6096 1.1975 -0.1876 0.1515 -0.1694 109 ASP F CA 10635 C C . ASP F 109 ? 1.2709 0.6141 1.2152 -0.1797 0.1672 -0.1796 109 ASP F C 10636 O O . ASP F 109 ? 1.2963 0.6151 1.2239 -0.1856 0.1751 -0.1871 109 ASP F O 10637 C CB . ASP F 109 ? 1.3000 0.6132 1.1885 -0.1992 0.1591 -0.1747 109 ASP F CB 10638 C CG . ASP F 109 ? 1.3273 0.6142 1.1912 -0.2091 0.1261 -0.1648 109 ASP F CG 10639 O OD1 . ASP F 109 ? 1.3362 0.6108 1.2121 -0.2112 0.0965 -0.1593 109 ASP F OD1 10640 O OD2 . ASP F 109 ? 1.3382 0.6129 1.1800 -0.2148 0.1250 -0.1644 109 ASP F OD2 10641 N N . PHE F 110 ? 1.2510 0.6149 1.2301 -0.1670 0.1654 -0.1810 110 PHE F N 10642 C CA . PHE F 110 ? 1.2607 0.6193 1.2750 -0.1564 0.1606 -0.1914 110 PHE F CA 10643 C C . PHE F 110 ? 1.2741 0.6126 1.2685 -0.1559 0.1454 -0.1832 110 PHE F C 10644 O O . PHE F 110 ? 1.2926 0.6189 1.3051 -0.1528 0.1444 -0.1933 110 PHE F O 10645 C CB . PHE F 110 ? 1.2552 0.6208 1.3041 -0.1441 0.1425 -0.1923 110 PHE F CB 10646 C CG . PHE F 110 ? 1.2814 0.6256 1.3742 -0.1315 0.1136 -0.2015 110 PHE F CG 10647 C CD1 . PHE F 110 ? 1.2929 0.6415 1.4554 -0.1277 0.1256 -0.2267 110 PHE F CD1 10648 C CD2 . PHE F 110 ? 1.3179 0.6220 1.3796 -0.1271 0.0722 -0.1879 110 PHE F CD2 10649 C CE1 . PHE F 110 ? 1.3186 0.6457 1.5465 -0.1138 0.0876 -0.2387 110 PHE F CE1 10650 C CE2 . PHE F 110 ? 1.3629 0.6266 1.4586 -0.1161 0.0264 -0.1949 110 PHE F CE2 10651 C CZ . PHE F 110 ? 1.3559 0.6382 1.5491 -0.1064 0.0293 -0.2207 110 PHE F CZ 10652 N N . HIS F 111 ? 1.2721 0.6032 1.2346 -0.1619 0.1398 -0.1691 111 HIS F N 10653 C CA . HIS F 111 ? 1.2904 0.5936 1.2263 -0.1678 0.1358 -0.1640 111 HIS F CA 10654 C C . HIS F 111 ? 1.2834 0.5915 1.2214 -0.1731 0.1431 -0.1673 111 HIS F C 10655 O O . HIS F 111 ? 1.3045 0.5932 1.2330 -0.1732 0.1390 -0.1685 111 HIS F O 10656 C CB . HIS F 111 ? 1.3046 0.5908 1.2141 -0.1811 0.1470 -0.1573 111 HIS F CB 10657 C CG . HIS F 111 ? 1.3449 0.5877 1.2114 -0.1840 0.1377 -0.1524 111 HIS F CG 10658 N ND1 . HIS F 111 ? 1.4009 0.5842 1.2245 -0.1821 0.1086 -0.1491 111 HIS F ND1 10659 C CD2 . HIS F 111 ? 1.3503 0.5848 1.1999 -0.1912 0.1472 -0.1499 111 HIS F CD2 10660 C CE1 . HIS F 111 ? 1.4550 0.5833 1.2236 -0.1896 0.0949 -0.1432 111 HIS F CE1 10661 N NE2 . HIS F 111 ? 1.4214 0.5825 1.2035 -0.1958 0.1235 -0.1440 111 HIS F NE2 10662 N N . ASP F 112 ? 1.2681 0.5889 1.2089 -0.1791 0.1469 -0.1679 112 ASP F N 10663 C CA . ASP F 112 ? 1.2907 0.5923 1.2135 -0.1877 0.1427 -0.1699 112 ASP F CA 10664 C C . ASP F 112 ? 1.3120 0.5954 1.2213 -0.1874 0.1559 -0.1813 112 ASP F C 10665 O O . ASP F 112 ? 1.3239 0.5905 1.2235 -0.1896 0.1545 -0.1830 112 ASP F O 10666 C CB . ASP F 112 ? 1.3082 0.5965 1.2138 -0.1975 0.1303 -0.1679 112 ASP F CB 10667 C CG . ASP F 112 ? 1.3127 0.5972 1.2470 -0.2029 0.1038 -0.1635 112 ASP F CG 10668 O OD1 . ASP F 112 ? 1.3139 0.5882 1.2579 -0.2054 0.0975 -0.1645 112 ASP F OD1 10669 O OD2 . ASP F 112 ? 1.3010 0.5922 1.2617 -0.2047 0.0875 -0.1620 112 ASP F OD2 10670 N N . SER F 113 ? 1.3145 0.6009 1.2346 -0.1863 0.1737 -0.1933 113 SER F N 10671 C CA . SER F 113 ? 1.3403 0.6100 1.2769 -0.1893 0.2003 -0.2154 113 SER F CA 10672 C C . SER F 113 ? 1.3397 0.6153 1.3189 -0.1762 0.1884 -0.2195 113 SER F C 10673 O O . SER F 113 ? 1.3634 0.6181 1.3454 -0.1823 0.2049 -0.2337 113 SER F O 10674 C CB . SER F 113 ? 1.3310 0.6137 1.3125 -0.1874 0.2238 -0.2339 113 SER F CB 10675 O OG . SER F 113 ? 1.3544 0.6202 1.3792 -0.1942 0.2613 -0.2654 113 SER F OG 10676 N N . ASN F 114 ? 1.3195 0.6084 1.3184 -0.1621 0.1588 -0.2075 114 ASN F N 10677 C CA . ASN F 114 ? 1.3366 0.6085 1.3583 -0.1517 0.1342 -0.2091 114 ASN F CA 10678 C C . ASN F 114 ? 1.3518 0.6043 1.3267 -0.1589 0.1305 -0.1978 114 ASN F C 10679 O O . ASN F 114 ? 1.3698 0.6011 1.3558 -0.1537 0.1151 -0.2017 114 ASN F O 10680 C CB . ASN F 114 ? 1.3511 0.6072 1.3723 -0.1421 0.0977 -0.1987 114 ASN F CB 10681 C CG . ASN F 114 ? 1.3386 0.6157 1.4090 -0.1345 0.0967 -0.2081 114 ASN F CG 10682 O OD1 . ASN F 114 ? 1.3250 0.6260 1.4534 -0.1345 0.1248 -0.2300 114 ASN F OD1 10683 N ND2 . ASN F 114 ? 1.3557 0.6140 1.3955 -0.1325 0.0705 -0.1939 114 ASN F ND2 10684 N N . VAL F 115 ? 1.3428 0.6003 1.2777 -0.1704 0.1398 -0.1863 115 VAL F N 10685 C CA . VAL F 115 ? 1.3536 0.5962 1.2625 -0.1786 0.1384 -0.1804 115 VAL F CA 10686 C C . VAL F 115 ? 1.3698 0.5982 1.2671 -0.1857 0.1501 -0.1902 115 VAL F C 10687 O O . VAL F 115 ? 1.3782 0.5901 1.2671 -0.1873 0.1479 -0.1916 115 VAL F O 10688 C CB . VAL F 115 ? 1.3450 0.5952 1.2475 -0.1883 0.1382 -0.1711 115 VAL F CB 10689 C CG1 . VAL F 115 ? 1.3603 0.5965 1.2600 -0.1967 0.1349 -0.1704 115 VAL F CG1 10690 C CG2 . VAL F 115 ? 1.3434 0.5901 1.2428 -0.1898 0.1418 -0.1661 115 VAL F CG2 10691 N N . LYS F 116 ? 1.3800 0.6006 1.2616 -0.1945 0.1651 -0.1977 116 LYS F N 10692 C CA . LYS F 116 ? 1.4329 0.6094 1.2720 -0.2112 0.1855 -0.2105 116 LYS F CA 10693 C C . LYS F 116 ? 1.4367 0.6127 1.3218 -0.2064 0.2107 -0.2330 116 LYS F C 10694 O O . LYS F 116 ? 1.4707 0.6188 1.3376 -0.2142 0.2203 -0.2403 116 LYS F O 10695 C CB . LYS F 116 ? 1.4784 0.6206 1.2691 -0.2291 0.2041 -0.2175 116 LYS F CB 10696 C CG . LYS F 116 ? 1.4802 0.6167 1.2388 -0.2333 0.1716 -0.1990 116 LYS F CG 10697 C CD . LYS F 116 ? 1.5228 0.6222 1.2330 -0.2497 0.1911 -0.2072 116 LYS F CD 10698 C CE . LYS F 116 ? 1.5069 0.6153 1.2138 -0.2474 0.1545 -0.1904 116 LYS F CE 10699 N NZ . LYS F 116 ? 1.5279 0.6170 1.2042 -0.2579 0.1771 -0.1983 116 LYS F NZ 10700 N N . ASN F 117 ? 1.4077 0.6128 1.3648 -0.1933 0.2172 -0.2463 117 ASN F N 10701 C CA . ASN F 117 ? 1.4128 0.6200 1.4552 -0.1865 0.2348 -0.2758 117 ASN F CA 10702 C C . ASN F 117 ? 1.4017 0.6101 1.4724 -0.1713 0.1996 -0.2693 117 ASN F C 10703 O O . ASN F 117 ? 1.4176 0.6150 1.5427 -0.1708 0.2133 -0.2928 117 ASN F O 10704 C CB . ASN F 117 ? 1.3864 0.6220 1.5198 -0.1735 0.2338 -0.2922 117 ASN F CB 10705 C CG . ASN F 117 ? 1.4055 0.6339 1.5151 -0.1913 0.2773 -0.3042 117 ASN F CG 10706 O OD1 . ASN F 117 ? 1.4604 0.6432 1.4860 -0.2183 0.3154 -0.3092 117 ASN F OD1 10707 N ND2 . ASN F 117 ? 1.3744 0.6327 1.5434 -0.1792 0.2673 -0.3081 117 ASN F ND2 10708 N N . LEU F 118 ? 1.3860 0.5984 1.4179 -0.1626 0.1591 -0.2407 118 LEU F N 10709 C CA . LEU F 118 ? 1.3988 0.5912 1.4244 -0.1548 0.1263 -0.2313 118 LEU F CA 10710 C C . LEU F 118 ? 1.4086 0.5867 1.3854 -0.1669 0.1411 -0.2267 118 LEU F C 10711 O O . LEU F 118 ? 1.4271 0.5879 1.4179 -0.1629 0.1305 -0.2318 118 LEU F O 10712 C CB . LEU F 118 ? 1.4068 0.5839 1.3838 -0.1524 0.0934 -0.2069 118 LEU F CB 10713 C CG . LEU F 118 ? 1.4549 0.5826 1.3942 -0.1519 0.0601 -0.1966 118 LEU F CG 10714 C CD1 . LEU F 118 ? 1.4827 0.5843 1.4876 -0.1363 0.0203 -0.2118 118 LEU F CD1 10715 C CD2 . LEU F 118 ? 1.4913 0.5797 1.3550 -0.1619 0.0470 -0.1774 118 LEU F CD2 10716 N N . TYR F 119 ? 1.4052 0.5837 1.3279 -0.1812 0.1572 -0.2174 119 TYR F N 10717 C CA . TYR F 119 ? 1.4332 0.5877 1.3093 -0.1941 0.1624 -0.2137 119 TYR F CA 10718 C C . TYR F 119 ? 1.4748 0.6006 1.3509 -0.2046 0.1940 -0.2371 119 TYR F C 10719 O O . TYR F 119 ? 1.4845 0.5889 1.3444 -0.2089 0.1946 -0.2391 119 TYR F O 10720 C CB . TYR F 119 ? 1.4421 0.5885 1.2717 -0.2069 0.1552 -0.2007 119 TYR F CB 10721 C CG . TYR F 119 ? 1.4817 0.5915 1.2672 -0.2202 0.1445 -0.1965 119 TYR F CG 10722 C CD1 . TYR F 119 ? 1.4697 0.5871 1.2702 -0.2165 0.1277 -0.1879 119 TYR F CD1 10723 C CD2 . TYR F 119 ? 1.5496 0.6013 1.2676 -0.2405 0.1511 -0.2025 119 TYR F CD2 10724 C CE1 . TYR F 119 ? 1.5078 0.5919 1.2803 -0.2274 0.1121 -0.1854 119 TYR F CE1 10725 C CE2 . TYR F 119 ? 1.6052 0.6067 1.2723 -0.2540 0.1298 -0.1972 119 TYR F CE2 10726 C CZ . TYR F 119 ? 1.5733 0.5991 1.2794 -0.2447 0.1074 -0.1886 119 TYR F CZ 10727 O OH . TYR F 119 ? 1.6199 0.5970 1.2884 -0.2567 0.0806 -0.1847 119 TYR F OH 10728 N N . ASP F 120 ? 1.4951 0.6145 1.3891 -0.2122 0.2275 -0.2580 120 ASP F N 10729 C CA . ASP F 120 ? 1.5525 0.6325 1.4515 -0.2303 0.2780 -0.2905 120 ASP F CA 10730 C C . ASP F 120 ? 1.5395 0.6401 1.5452 -0.2140 0.2792 -0.3128 120 ASP F C 10731 O O . ASP F 120 ? 1.5771 0.6460 1.5837 -0.2265 0.3094 -0.3330 120 ASP F O 10732 C CB . ASP F 120 ? 1.5784 0.6414 1.4825 -0.2466 0.3250 -0.3144 120 ASP F CB 10733 C CG . ASP F 120 ? 1.6233 0.6403 1.4061 -0.2684 0.3212 -0.2956 120 ASP F CG 10734 O OD1 . ASP F 120 ? 1.6243 0.6276 1.3398 -0.2687 0.2771 -0.2665 120 ASP F OD1 10735 O OD2 . ASP F 120 ? 1.6658 0.6545 1.4285 -0.2864 0.3598 -0.3129 120 ASP F OD2 10736 N N . LYS F 121 ? 1.4992 0.6405 1.5906 -0.1879 0.2410 -0.3097 121 LYS F N 10737 C CA . LYS F 121 ? 1.4979 0.6466 1.7002 -0.1694 0.2184 -0.3295 121 LYS F CA 10738 C C . LYS F 121 ? 1.5125 0.6421 1.6752 -0.1670 0.1940 -0.3150 121 LYS F C 10739 O O . LYS F 121 ? 1.5287 0.6481 1.7629 -0.1640 0.2010 -0.3401 121 LYS F O 10740 C CB . LYS F 121 ? 1.4755 0.6422 1.7381 -0.1451 0.1597 -0.3200 121 LYS F CB 10741 C CG . LYS F 121 ? 1.4906 0.6470 1.8775 -0.1249 0.1146 -0.3418 121 LYS F CG 10742 C CD . LYS F 121 ? 1.4933 0.6410 1.9182 -0.1055 0.0455 -0.3313 121 LYS F CD 10743 C CE . LYS F 121 ? 1.5225 0.6457 2.0913 -0.0848 -0.0160 -0.3578 121 LYS F CE 10744 N NZ . LYS F 121 ? 1.5649 0.6424 2.0914 -0.0811 -0.0606 -0.3441 121 LYS F NZ 10745 N N . VAL F 122 ? 1.5079 0.6324 1.5700 -0.1694 0.1688 -0.2788 122 VAL F N 10746 C CA . VAL F 122 ? 1.5220 0.6262 1.5383 -0.1710 0.1521 -0.2650 122 VAL F CA 10747 C C . VAL F 122 ? 1.5549 0.6362 1.5270 -0.1915 0.1941 -0.2759 122 VAL F C 10748 O O . VAL F 122 ? 1.5690 0.6326 1.5435 -0.1927 0.1944 -0.2817 122 VAL F O 10749 C CB . VAL F 122 ? 1.5140 0.6156 1.4538 -0.1725 0.1245 -0.2315 122 VAL F CB 10750 C CG1 . VAL F 122 ? 1.5330 0.6118 1.4326 -0.1773 0.1152 -0.2217 122 VAL F CG1 10751 C CG2 . VAL F 122 ? 1.5158 0.6103 1.4647 -0.1607 0.0874 -0.2211 122 VAL F CG2 10752 N N . ARG F 123 ? 1.5750 0.6416 1.4925 -0.2105 0.2252 -0.2778 123 ARG F N 10753 C CA . ARG F 123 ? 1.6433 0.6538 1.4878 -0.2381 0.2627 -0.2895 123 ARG F CA 10754 C C . ARG F 123 ? 1.6788 0.6688 1.5882 -0.2478 0.3176 -0.3326 123 ARG F C 10755 O O . ARG F 123 ? 1.7233 0.6706 1.6007 -0.2636 0.3423 -0.3453 123 ARG F O 10756 C CB . ARG F 123 ? 1.6848 0.6562 1.4364 -0.2605 0.2728 -0.2814 123 ARG F CB 10757 C CG . ARG F 123 ? 1.7908 0.6674 1.4213 -0.2957 0.2945 -0.2865 123 ARG F CG 10758 C CD . ARG F 123 ? 1.8449 0.6683 1.3687 -0.3138 0.2659 -0.2657 123 ARG F CD 10759 N NE . ARG F 123 ? 1.8397 0.6731 1.3735 -0.3166 0.2864 -0.2731 123 ARG F NE 10760 C CZ . ARG F 123 ? 1.9219 0.6921 1.4100 -0.3459 0.3484 -0.3019 123 ARG F CZ 10761 N NH1 . ARG F 123 ? 2.0249 0.7087 1.4486 -0.3788 0.4041 -0.3294 123 ARG F NH1 10762 N NH2 . ARG F 123 ? 1.9077 0.6943 1.4128 -0.3461 0.3626 -0.3067 123 ARG F NH2 10763 N N . LEU F 124 ? 1.6529 0.6725 1.6666 -0.2390 0.3376 -0.3587 124 LEU F N 10764 C CA . LEU F 124 ? 1.6814 0.6897 1.8049 -0.2476 0.3952 -0.4107 124 LEU F CA 10765 C C . LEU F 124 ? 1.6509 0.6870 1.8952 -0.2222 0.3613 -0.4225 124 LEU F C 10766 O O . LEU F 124 ? 1.6875 0.6990 1.9888 -0.2348 0.4071 -0.4599 124 LEU F O 10767 C CB . LEU F 124 ? 1.6598 0.6929 1.8827 -0.2454 0.4229 -0.4392 124 LEU F CB 10768 N N . GLN F 125 ? 1.6006 0.6734 1.8755 -0.1905 0.2824 -0.3929 125 GLN F N 10769 C CA . GLN F 125 ? 1.5970 0.6754 1.9674 -0.1667 0.2306 -0.3989 125 GLN F CA 10770 C C . GLN F 125 ? 1.6280 0.6797 1.9310 -0.1750 0.2339 -0.3893 125 GLN F C 10771 O O . GLN F 125 ? 1.6325 0.6766 2.0254 -0.1667 0.2253 -0.4126 125 GLN F O 10772 C CB . GLN F 125 ? 1.5740 0.6603 1.9310 -0.1419 0.1455 -0.3636 125 GLN F CB 10773 C CG . GLN F 125 ? 1.5968 0.6575 2.0103 -0.1214 0.0739 -0.3618 125 GLN F CG 10774 C CD . GLN F 125 ? 1.6128 0.6475 2.0026 -0.1050 -0.0080 -0.3348 125 GLN F CD 10775 O OE1 . GLN F 125 ? 1.6514 0.6449 2.1028 -0.0885 -0.0808 -0.3396 125 GLN F OE1 10776 N NE2 . GLN F 125 ? 1.5962 0.6405 1.8896 -0.1122 -0.0006 -0.3073 125 GLN F NE2 10777 N N . LEU F 126 ? 1.6467 0.6829 1.8028 -0.1906 0.2407 -0.3564 126 LEU F N 10778 C CA . LEU F 126 ? 1.6848 0.6910 1.7656 -0.2029 0.2484 -0.3472 126 LEU F CA 10779 C C . LEU F 126 ? 1.7385 0.7024 1.7002 -0.2353 0.2957 -0.3450 126 LEU F C 10780 O O . LEU F 126 ? 1.7378 0.6976 1.6070 -0.2398 0.2705 -0.3127 126 LEU F O 10781 C CB . LEU F 126 ? 1.6677 0.6794 1.6929 -0.1886 0.1867 -0.3075 126 LEU F CB 10782 C CG . LEU F 126 ? 1.6347 0.6646 1.6242 -0.1786 0.1465 -0.2767 126 LEU F CG 10783 C CD1 . LEU F 126 ? 1.6314 0.6599 1.5241 -0.1936 0.1532 -0.2518 126 LEU F CD1 10784 C CD2 . LEU F 126 ? 1.6453 0.6575 1.6360 -0.1639 0.0917 -0.2608 126 LEU F CD2 10785 N N . ARG F 127 ? 1.8003 0.7191 1.7663 -0.2612 0.3634 -0.3832 127 ARG F N 10786 C CA . ARG F 127 ? 1.8873 0.7272 1.7134 -0.3013 0.4099 -0.3861 127 ARG F CA 10787 C C . ARG F 127 ? 1.9480 0.7257 1.6605 -0.3199 0.4031 -0.3723 127 ARG F C 10788 O O . ARG F 127 ? 1.9778 0.7205 1.5727 -0.3293 0.3644 -0.3392 127 ARG F O 10789 C CB . ARG F 127 ? 1.9546 0.7489 1.8188 -0.3312 0.5013 -0.4400 127 ARG F CB 10790 N N . ASP F 128 ? 1.9646 0.7279 1.7272 -0.3244 0.4359 -0.4002 128 ASP F N 10791 C CA . ASP F 128 ? 2.0317 0.7274 1.6896 -0.3453 0.4381 -0.3934 128 ASP F CA 10792 C C . ASP F 128 ? 1.9593 0.7095 1.6510 -0.3138 0.3702 -0.3625 128 ASP F C 10793 O O . ASP F 128 ? 2.0061 0.7092 1.6134 -0.3267 0.3582 -0.3503 128 ASP F O 10794 C CB . ASP F 128 ? 2.1173 0.7487 1.7941 -0.3768 0.5265 -0.4460 128 ASP F CB 10795 C CG . ASP F 128 ? 2.0415 0.7499 1.9321 -0.3492 0.5446 -0.4845 128 ASP F CG 10796 O OD1 . ASP F 128 ? 1.9370 0.7335 1.9397 -0.3079 0.4832 -0.4678 128 ASP F OD1 10797 O OD2 . ASP F 128 ? 2.0973 0.7656 2.0443 -0.3717 0.6184 -0.5343 128 ASP F OD2 10798 N N . ASN F 129 ? 1.8590 0.6927 1.6611 -0.2767 0.3264 -0.3512 129 ASN F N 10799 C CA . ASN F 129 ? 1.8077 0.6761 1.6237 -0.2528 0.2674 -0.3229 129 ASN F CA 10800 C C . ASN F 129 ? 1.7759 0.6661 1.5361 -0.2454 0.2194 -0.2836 129 ASN F C 10801 O O . ASN F 129 ? 1.7374 0.6513 1.5097 -0.2299 0.1806 -0.2637 129 ASN F O 10802 C CB . ASN F 129 ? 1.7567 0.6689 1.7037 -0.2238 0.2427 -0.3355 129 ASN F CB 10803 C CG . ASN F 129 ? 1.7825 0.6784 1.8176 -0.2266 0.2773 -0.3762 129 ASN F CG 10804 O OD1 . ASN F 129 ? 1.8321 0.6824 1.8129 -0.2512 0.3226 -0.3909 129 ASN F OD1 10805 N ND2 . ASN F 129 ? 1.7522 0.6759 1.9275 -0.2028 0.2516 -0.3966 129 ASN F ND2 10806 N N . ALA F 130 ? 1.8032 0.6762 1.5042 -0.2598 0.2255 -0.2763 130 ALA F N 10807 C CA . ALA F 130 ? 1.7722 0.6666 1.4460 -0.2542 0.1839 -0.2465 130 ALA F CA 10808 C C . ALA F 130 ? 1.8264 0.6731 1.4187 -0.2762 0.1820 -0.2408 130 ALA F C 10809 O O . ALA F 130 ? 1.8679 0.6794 1.4292 -0.2923 0.2181 -0.2579 130 ALA F O 10810 C CB . ALA F 130 ? 1.7071 0.6595 1.4501 -0.2318 0.1684 -0.2400 130 ALA F CB 10811 N N . LYS F 131 ? 1.8357 0.6732 1.3997 -0.2787 0.1377 -0.2195 131 LYS F N 10812 C CA . LYS F 131 ? 1.9027 0.6812 1.3934 -0.2979 0.1105 -0.2108 131 LYS F CA 10813 C C . LYS F 131 ? 1.8402 0.6746 1.3886 -0.2836 0.0881 -0.1995 131 LYS F C 10814 O O . LYS F 131 ? 1.7658 0.6636 1.3926 -0.2659 0.0758 -0.1924 131 LYS F O 10815 C CB . LYS F 131 ? 1.9672 0.6899 1.4140 -0.3094 0.0617 -0.1993 131 LYS F CB 10816 C CG . LYS F 131 ? 2.0313 0.6949 1.4352 -0.3226 0.0011 -0.1867 131 LYS F CG 10817 C CD . LYS F 131 ? 2.0567 0.6959 1.4840 -0.3232 -0.0602 -0.1779 131 LYS F CD 10818 C CE . LYS F 131 ? 2.1108 0.7006 1.5427 -0.3301 -0.1378 -0.1687 131 LYS F CE 10819 N NZ . LYS F 131 ? 2.2644 0.7101 1.5736 -0.3578 -0.2014 -0.1625 131 LYS F NZ 10820 N N . GLU F 132 ? 1.8829 0.6817 1.3829 -0.2961 0.0882 -0.2003 132 GLU F N 10821 C CA . GLU F 132 ? 1.8312 0.6732 1.3799 -0.2855 0.0647 -0.1906 132 GLU F CA 10822 C C . GLU F 132 ? 1.8591 0.6704 1.4148 -0.2907 -0.0006 -0.1785 132 GLU F C 10823 O O . GLU F 132 ? 1.9619 0.6762 1.4292 -0.3119 -0.0375 -0.1752 132 GLU F O 10824 C CB . GLU F 132 ? 1.8711 0.6802 1.3650 -0.2981 0.0874 -0.1973 132 GLU F CB 10825 N N . LEU F 133 ? 1.7789 0.6607 1.4422 -0.2742 -0.0160 -0.1754 133 LEU F N 10826 C CA . LEU F 133 ? 1.7875 0.6549 1.5118 -0.2764 -0.0761 -0.1731 133 LEU F CA 10827 C C . LEU F 133 ? 1.8095 0.6435 1.5278 -0.2822 -0.1203 -0.1691 133 LEU F C 10828 O O . LEU F 133 ? 1.8879 0.6432 1.5838 -0.2942 -0.1917 -0.1653 133 LEU F O 10829 C CB . LEU F 133 ? 1.7066 0.6549 1.5621 -0.2631 -0.0573 -0.1811 133 LEU F CB 10830 C CG . LEU F 133 ? 1.7011 0.6588 1.5653 -0.2619 -0.0353 -0.1847 133 LEU F CG 10831 C CD1 . LEU F 133 ? 1.6432 0.6597 1.6068 -0.2575 0.0005 -0.1956 133 LEU F CD1 10832 C CD2 . LEU F 133 ? 1.7655 0.6614 1.6170 -0.2719 -0.0887 -0.1842 133 LEU F CD2 10833 N N . GLY F 134 ? 1.7467 0.6304 1.4824 -0.2741 -0.0863 -0.1696 134 GLY F N 10834 C CA . GLY F 134 ? 1.7696 0.6244 1.4964 -0.2791 -0.1235 -0.1658 134 GLY F CA 10835 C C . GLY F 134 ? 1.6704 0.6124 1.5239 -0.2636 -0.1109 -0.1715 134 GLY F C 10836 O O . GLY F 134 ? 1.6719 0.6114 1.5155 -0.2639 -0.1191 -0.1688 134 GLY F O 10837 N N . ASN F 135 ? 1.5936 0.6013 1.5565 -0.2543 -0.0852 -0.1817 135 ASN F N 10838 C CA . ASN F 135 ? 1.5180 0.5936 1.5927 -0.2475 -0.0569 -0.1928 135 ASN F CA 10839 C C . ASN F 135 ? 1.4642 0.5843 1.5012 -0.2411 0.0097 -0.1899 135 ASN F C 10840 O O . ASN F 135 ? 1.4215 0.5803 1.5222 -0.2412 0.0447 -0.1994 135 ASN F O 10841 C CB . ASN F 135 ? 1.4931 0.5940 1.7014 -0.2504 -0.0534 -0.2127 135 ASN F CB 10842 C CG . ASN F 135 ? 1.4858 0.5943 1.6642 -0.2525 -0.0079 -0.2141 135 ASN F CG 10843 O OD1 . ASN F 135 ? 1.4946 0.5830 1.5626 -0.2497 0.0015 -0.1998 135 ASN F OD1 10844 N ND2 . ASN F 135 ? 1.4716 0.6028 1.7539 -0.2603 0.0238 -0.2353 135 ASN F ND2 10845 N N . GLY F 136 ? 1.4771 0.5796 1.4137 -0.2385 0.0254 -0.1801 136 GLY F N 10846 C CA . GLY F 136 ? 1.4441 0.5754 1.3535 -0.2306 0.0699 -0.1784 136 GLY F CA 10847 C C . GLY F 136 ? 1.4474 0.5754 1.3392 -0.2287 0.0917 -0.1795 136 GLY F C 10848 O O . GLY F 136 ? 1.4407 0.5780 1.3206 -0.2239 0.1150 -0.1788 136 GLY F O 10849 N N . CYS F 137 ? 1.5664 0.6012 1.2997 0.1755 0.1113 0.0174 137 CYS F N 10850 C CA . CYS F 137 ? 1.4313 0.5894 1.2436 0.1422 0.0892 0.0002 137 CYS F CA 10851 C C . CYS F 137 ? 1.4520 0.5731 1.1828 0.1058 0.0728 -0.0038 137 CYS F C 10852 O O . CYS F 137 ? 1.5769 0.5734 1.1843 0.1014 0.0808 0.0052 137 CYS F O 10853 C CB . CYS F 137 ? 1.3725 0.6436 1.3016 0.1727 0.0358 0.0194 137 CYS F CB 10854 S SG . CYS F 137 ? 1.3349 0.6658 1.3850 0.2068 0.0798 0.0132 137 CYS F SG 10855 N N . PHE F 138 ? 1.3524 0.5628 1.1381 0.0793 0.0592 -0.0187 138 PHE F N 10856 C CA . PHE F 138 ? 1.3721 0.5477 1.0887 0.0480 0.0530 -0.0247 138 PHE F CA 10857 C C . PHE F 138 ? 1.2947 0.5612 1.0682 0.0367 0.0130 -0.0248 138 PHE F C 10858 O O . PHE F 138 ? 1.1926 0.5427 1.0478 0.0303 0.0264 -0.0423 138 PHE F O 10859 C CB . PHE F 138 ? 1.3556 0.5098 1.0605 0.0162 0.1185 -0.0585 138 PHE F CB 10860 N N . GLU F 139 ? 1.3637 0.5952 1.0736 0.0294 -0.0364 -0.0056 139 GLU F N 10861 C CA . GLU F 139 ? 1.3246 0.6174 1.0617 0.0075 -0.0706 -0.0075 139 GLU F CA 10862 C C . GLU F 139 ? 1.3389 0.5769 1.0034 -0.0225 -0.0355 -0.0266 139 GLU F C 10863 O O . GLU F 139 ? 1.4423 0.5677 0.9893 -0.0363 -0.0208 -0.0245 139 GLU F O 10864 C CB . GLU F 139 ? 1.4090 0.6915 1.1112 0.0052 -0.1482 0.0200 139 GLU F CB 10865 C CG . GLU F 139 ? 1.3623 0.7614 1.2019 0.0324 -0.1919 0.0344 139 GLU F CG 10866 C CD . GLU F 139 ? 1.4518 0.8605 1.2766 0.0267 -0.2831 0.0604 139 GLU F CD 10867 O OE1 . GLU F 139 ? 1.5840 0.8892 1.2981 0.0411 -0.3229 0.0845 139 GLU F OE1 10868 O OE2 . GLU F 139 ? 1.4090 0.9208 1.3240 0.0033 -0.3167 0.0557 139 GLU F OE2 10869 N N . PHE F 140 ? 1.2592 0.5630 0.9850 -0.0303 -0.0183 -0.0445 140 PHE F N 10870 C CA . PHE F 140 ? 1.2821 0.5404 0.9558 -0.0471 0.0134 -0.0602 140 PHE F CA 10871 C C . PHE F 140 ? 1.3828 0.5706 0.9517 -0.0755 -0.0173 -0.0493 140 PHE F C 10872 O O . PHE F 140 ? 1.3850 0.6095 0.9649 -0.0879 -0.0729 -0.0352 140 PHE F O 10873 C CB . PHE F 140 ? 1.1900 0.5221 0.9412 -0.0406 0.0271 -0.0764 140 PHE F CB 10874 C CG . PHE F 140 ? 1.1235 0.5046 0.9517 -0.0233 0.0561 -0.0921 140 PHE F CG 10875 C CD1 . PHE F 140 ? 1.0727 0.5048 0.9597 -0.0141 0.0478 -0.0898 140 PHE F CD1 10876 C CD2 . PHE F 140 ? 1.1162 0.4926 0.9628 -0.0183 0.0927 -0.1112 140 PHE F CD2 10877 C CE1 . PHE F 140 ? 1.0359 0.4966 0.9713 -0.0092 0.0722 -0.1068 140 PHE F CE1 10878 C CE2 . PHE F 140 ? 1.0700 0.5004 0.9918 -0.0120 0.1081 -0.1282 140 PHE F CE2 10879 C CZ . PHE F 140 ? 1.0315 0.4958 0.9843 -0.0120 0.0962 -0.1263 140 PHE F CZ 10880 N N . TYR F 141 ? 1.4766 0.5618 0.9470 -0.0894 0.0227 -0.0586 141 TYR F N 10881 C CA . TYR F 141 ? 1.5974 0.5868 0.9400 -0.1240 0.0071 -0.0538 141 TYR F CA 10882 C C . TYR F 141 ? 1.5713 0.5682 0.9243 -0.1272 0.0345 -0.0686 141 TYR F C 10883 O O . TYR F 141 ? 1.6860 0.5854 0.9225 -0.1572 0.0395 -0.0699 141 TYR F O 10884 C CB . TYR F 141 ? 1.7548 0.5860 0.9462 -0.1410 0.0454 -0.0548 141 TYR F CB 10885 C CG . TYR F 141 ? 1.8605 0.6280 0.9649 -0.1496 -0.0068 -0.0313 141 TYR F CG 10886 C CD1 . TYR F 141 ? 1.9569 0.6945 0.9805 -0.1781 -0.0908 -0.0103 141 TYR F CD1 10887 C CD2 . TYR F 141 ? 1.8879 0.6201 0.9869 -0.1302 0.0225 -0.0295 141 TYR F CD2 10888 C CE1 . TYR F 141 ? 2.0711 0.7485 1.0142 -0.1773 -0.1548 0.0160 141 TYR F CE1 10889 C CE2 . TYR F 141 ? 2.0103 0.6610 1.0096 -0.1298 -0.0291 -0.0034 141 TYR F CE2 10890 C CZ . TYR F 141 ? 2.1021 0.7275 1.0256 -0.1483 -0.1236 0.0215 141 TYR F CZ 10891 O OH . TYR F 141 ? 2.2394 0.7829 1.0637 -0.1396 -0.1908 0.0521 141 TYR F OH 10892 N N . HIS F 142 ? 1.4536 0.5475 0.9273 -0.0968 0.0513 -0.0790 142 HIS F N 10893 C CA . HIS F 142 ? 1.4348 0.5379 0.9195 -0.0909 0.0631 -0.0875 142 HIS F CA 10894 C C . HIS F 142 ? 1.3229 0.5389 0.9164 -0.0769 0.0375 -0.0877 142 HIS F C 10895 O O . HIS F 142 ? 1.2544 0.5399 0.9202 -0.0696 0.0200 -0.0834 142 HIS F O 10896 C CB . HIS F 142 ? 1.4539 0.5207 0.9490 -0.0591 0.1227 -0.1022 142 HIS F CB 10897 C CG . HIS F 142 ? 1.3691 0.5263 0.9901 -0.0266 0.1379 -0.1124 142 HIS F CG 10898 N ND1 . HIS F 142 ? 1.3713 0.5291 1.0098 -0.0315 0.1577 -0.1164 142 HIS F ND1 10899 C CD2 . HIS F 142 ? 1.2947 0.5341 1.0163 0.0045 0.1321 -0.1203 142 HIS F CD2 10900 C CE1 . HIS F 142 ? 1.2901 0.5351 1.0445 -0.0100 0.1680 -0.1295 142 HIS F CE1 10901 N NE2 . HIS F 142 ? 1.2404 0.5403 1.0485 0.0122 0.1467 -0.1315 142 HIS F NE2 10902 N N . ARG F 143 ? 1.3230 0.5348 0.9091 -0.0733 0.0416 -0.0927 143 ARG F N 10903 C CA . ARG F 143 ? 1.2539 0.5372 0.9068 -0.0668 0.0266 -0.0949 143 ARG F CA 10904 C C . ARG F 143 ? 1.1908 0.5133 0.9107 -0.0263 0.0384 -0.1028 143 ARG F C 10905 O O . ARG F 143 ? 1.2245 0.5149 0.9352 0.0008 0.0559 -0.1077 143 ARG F O 10906 C CB . ARG F 143 ? 1.3258 0.5587 0.9111 -0.0865 0.0280 -0.0970 143 ARG F CB 10907 C CG . ARG F 143 ? 1.4166 0.5958 0.9204 -0.1378 0.0187 -0.0947 143 ARG F CG 10908 C CD . ARG F 143 ? 1.3859 0.6497 0.9572 -0.1705 -0.0168 -0.0901 143 ARG F CD 10909 N NE . ARG F 143 ? 1.3445 0.6777 0.9898 -0.1783 -0.0135 -0.0966 143 ARG F NE 10910 C CZ . ARG F 143 ? 1.3048 0.7347 1.0523 -0.1916 -0.0319 -0.0950 143 ARG F CZ 10911 N NH1 . ARG F 143 ? 1.3024 0.7755 1.0903 -0.1930 -0.0704 -0.0828 143 ARG F NH1 10912 N NH2 . ARG F 143 ? 1.2820 0.7551 1.0866 -0.2003 -0.0092 -0.1053 143 ARG F NH2 10913 N N . CYS F 144 ? 1.1169 0.5088 0.9081 -0.0228 0.0284 -0.1050 144 CYS F N 10914 C CA . CYS F 144 ? 1.0713 0.5037 0.9219 0.0022 0.0302 -0.1152 144 CYS F CA 10915 C C . CYS F 144 ? 1.0660 0.5079 0.9106 -0.0008 0.0148 -0.1178 144 CYS F C 10916 O O . CYS F 144 ? 1.0383 0.5057 0.9031 -0.0176 0.0177 -0.1179 144 CYS F O 10917 C CB . CYS F 144 ? 1.0314 0.5028 0.9375 0.0001 0.0412 -0.1191 144 CYS F CB 10918 S SG . CYS F 144 ? 0.9968 0.5221 0.9780 0.0127 0.0429 -0.1379 144 CYS F SG 10919 N N . ASP F 145 ? 1.1094 0.5166 0.9166 0.0177 0.0018 -0.1191 145 ASP F N 10920 C CA . ASP F 145 ? 1.1467 0.5263 0.9075 0.0110 -0.0121 -0.1210 145 ASP F CA 10921 C C . ASP F 145 ? 1.1214 0.5438 0.9277 0.0157 -0.0287 -0.1311 145 ASP F C 10922 O O . ASP F 145 ? 1.0726 0.5538 0.9565 0.0211 -0.0253 -0.1380 145 ASP F O 10923 C CB . ASP F 145 ? 1.2381 0.5339 0.9085 0.0306 -0.0267 -0.1146 145 ASP F CB 10924 C CG . ASP F 145 ? 1.2592 0.5703 0.9635 0.0779 -0.0608 -0.1144 145 ASP F CG 10925 O OD1 . ASP F 145 ? 1.2094 0.5857 1.0088 0.0967 -0.0544 -0.1196 145 ASP F OD1 10926 O OD2 . ASP F 145 ? 1.3432 0.5972 0.9785 0.0957 -0.0943 -0.1094 145 ASP F OD2 10927 N N . ASN F 146 ? 1.1824 0.5584 0.9228 0.0058 -0.0420 -0.1342 146 ASN F N 10928 C CA . ASN F 146 ? 1.1885 0.5815 0.9406 -0.0037 -0.0575 -0.1460 146 ASN F CA 10929 C C . ASN F 146 ? 1.1870 0.6345 1.0022 0.0191 -0.1018 -0.1529 146 ASN F C 10930 O O . ASN F 146 ? 1.1694 0.6599 1.0314 0.0018 -0.1051 -0.1671 146 ASN F O 10931 C CB . ASN F 146 ? 1.2912 0.5886 0.9215 -0.0247 -0.0606 -0.1483 146 ASN F CB 10932 C CG . ASN F 146 ? 1.2880 0.5612 0.9015 -0.0582 -0.0008 -0.1526 146 ASN F CG 10933 O OD1 . ASN F 146 ? 1.2066 0.5467 0.9108 -0.0620 0.0297 -0.1534 146 ASN F OD1 10934 N ND2 . ASN F 146 ? 1.3945 0.5664 0.8921 -0.0809 0.0176 -0.1557 146 ASN F ND2 10935 N N . GLU F 147 ? 1.2199 0.6660 1.0429 0.0569 -0.1324 -0.1446 147 GLU F N 10936 C CA . GLU F 147 ? 1.2102 0.7367 1.1382 0.0847 -0.1706 -0.1527 147 GLU F CA 10937 C C . GLU F 147 ? 1.1178 0.7247 1.1651 0.0808 -0.1244 -0.1637 147 GLU F C 10938 O O . GLU F 147 ? 1.0854 0.7724 1.2333 0.0723 -0.1308 -0.1817 147 GLU F O 10939 C CB . GLU F 147 ? 1.2840 0.7815 1.1972 0.1385 -0.2092 -0.1384 147 GLU F CB 10940 C CG . GLU F 147 ? 1.4162 0.8126 1.1910 0.1474 -0.2650 -0.1259 147 GLU F CG 10941 C CD . GLU F 147 ? 1.5138 0.8579 1.2570 0.2107 -0.3008 -0.1067 147 GLU F CD 10942 O OE1 . GLU F 147 ? 1.5032 0.8208 1.2488 0.2319 -0.2539 -0.0991 147 GLU F OE1 10943 O OE2 . GLU F 147 ? 1.6230 0.9398 1.3273 0.2405 -0.3786 -0.0981 147 GLU F OE2 10944 N N . CYS F 148 ? 1.0908 0.6638 1.1129 0.0808 -0.0780 -0.1543 148 CYS F N 10945 C CA . CYS F 148 ? 1.0363 0.6416 1.1201 0.0707 -0.0295 -0.1614 148 CYS F CA 10946 C C . CYS F 148 ? 0.9974 0.6256 1.0981 0.0343 -0.0113 -0.1716 148 CYS F C 10947 O O . CYS F 148 ? 0.9704 0.6380 1.1384 0.0230 0.0146 -0.1865 148 CYS F O 10948 C CB . CYS F 148 ? 1.0499 0.5884 1.0621 0.0690 0.0013 -0.1465 148 CYS F CB 10949 S SG . CYS F 148 ? 1.0366 0.5656 1.0554 0.0452 0.0508 -0.1481 148 CYS F SG 10950 N N . MET F 149 ? 1.0037 0.5960 1.0392 0.0159 -0.0160 -0.1650 149 MET F N 10951 C CA . MET F 149 ? 0.9897 0.5829 1.0283 -0.0099 0.0085 -0.1711 149 MET F CA 10952 C C . MET F 149 ? 1.0088 0.6339 1.0828 -0.0288 -0.0043 -0.1927 149 MET F C 10953 O O . MET F 149 ? 0.9952 0.6288 1.0969 -0.0489 0.0259 -0.2045 149 MET F O 10954 C CB . MET F 149 ? 1.0025 0.5522 0.9792 -0.0201 0.0160 -0.1611 149 MET F CB 10955 C CG . MET F 149 ? 0.9798 0.5256 0.9710 -0.0268 0.0507 -0.1555 149 MET F CG 10956 S SD . MET F 149 ? 0.9433 0.4906 0.9448 -0.0147 0.0567 -0.1366 149 MET F SD 10957 C CE . MET F 149 ? 0.9584 0.4990 0.9343 -0.0202 0.0465 -0.1246 149 MET F CE 10958 N N . GLU F 150 ? 1.0582 0.6891 1.1180 -0.0254 -0.0531 -0.1976 150 GLU F N 10959 C CA . GLU F 150 ? 1.0933 0.7672 1.1940 -0.0470 -0.0862 -0.2196 150 GLU F CA 10960 C C . GLU F 150 ? 1.0548 0.8189 1.2862 -0.0443 -0.0764 -0.2363 150 GLU F C 10961 O O . GLU F 150 ? 1.0624 0.8654 1.3442 -0.0805 -0.0690 -0.2604 150 GLU F O 10962 C CB . GLU F 150 ? 1.1725 0.8279 1.2229 -0.0354 -0.1582 -0.2157 150 GLU F CB 10963 C CG . GLU F 150 ? 1.2544 0.8022 1.1588 -0.0572 -0.1589 -0.2098 150 GLU F CG 10964 C CD . GLU F 150 ? 1.3582 0.8431 1.1666 -0.0392 -0.2227 -0.1980 150 GLU F CD 10965 O OE1 . GLU F 150 ? 1.3625 0.8850 1.2191 0.0036 -0.2656 -0.1876 150 GLU F OE1 10966 O OE2 . GLU F 150 ? 1.4585 0.8391 1.1304 -0.0663 -0.2246 -0.1988 150 GLU F OE2 10967 N N . SER F 151 ? 1.0282 0.8155 1.3088 -0.0066 -0.0671 -0.2266 151 SER F N 10968 C CA . SER F 151 ? 1.0041 0.8658 1.4114 -0.0020 -0.0363 -0.2443 151 SER F CA 10969 C C . SER F 151 ? 0.9912 0.8311 1.3980 -0.0402 0.0341 -0.2576 151 SER F C 10970 O O . SER F 151 ? 0.9900 0.8873 1.4907 -0.0666 0.0619 -0.2851 151 SER F O 10971 C CB . SER F 151 ? 1.0016 0.8495 1.4225 0.0451 -0.0194 -0.2293 151 SER F CB 10972 O OG . SER F 151 ? 1.0053 0.9431 1.5723 0.0657 -0.0141 -0.2474 151 SER F OG 10973 N N . VAL F 152 ? 0.9915 0.7456 1.2930 -0.0430 0.0617 -0.2382 152 VAL F N 10974 C CA . VAL F 152 ? 1.0080 0.7112 1.2748 -0.0699 0.1184 -0.2425 152 VAL F CA 10975 C C . VAL F 152 ? 1.0367 0.7405 1.2994 -0.1105 0.1209 -0.2624 152 VAL F C 10976 O O . VAL F 152 ? 1.0621 0.7483 1.3352 -0.1431 0.1689 -0.2814 152 VAL F O 10977 C CB . VAL F 152 ? 1.0095 0.6326 1.1772 -0.0538 0.1272 -0.2124 152 VAL F CB 10978 C CG1 . VAL F 152 ? 1.0496 0.6052 1.1669 -0.0710 0.1721 -0.2107 152 VAL F CG1 10979 C CG2 . VAL F 152 ? 1.0105 0.6154 1.1617 -0.0281 0.1283 -0.1971 152 VAL F CG2 10980 N N . ARG F 153 ? 1.0509 0.7540 1.2781 -0.1135 0.0754 -0.2597 153 ARG F N 10981 C CA . ARG F 153 ? 1.1033 0.7910 1.3049 -0.1575 0.0726 -0.2809 153 ARG F CA 10982 C C . ARG F 153 ? 1.1257 0.9049 1.4261 -0.1909 0.0404 -0.3136 153 ARG F C 10983 O O . ARG F 153 ? 1.1710 0.9436 1.4698 -0.2436 0.0568 -0.3405 153 ARG F O 10984 C CB . ARG F 153 ? 1.1319 0.7653 1.2404 -0.1536 0.0413 -0.2684 153 ARG F CB 10985 C CG . ARG F 153 ? 1.1364 0.6868 1.1695 -0.1402 0.0878 -0.2487 153 ARG F CG 10986 C CD . ARG F 153 ? 1.1328 0.6570 1.1167 -0.1146 0.0691 -0.2278 153 ARG F CD 10987 N NE . ARG F 153 ? 1.2019 0.6964 1.1226 -0.1353 0.0324 -0.2379 153 ARG F NE 10988 C CZ . ARG F 153 ? 1.2314 0.6853 1.0886 -0.1235 0.0164 -0.2256 153 ARG F CZ 10989 N NH1 . ARG F 153 ? 1.1842 0.6410 1.0525 -0.0949 0.0338 -0.2052 153 ARG F NH1 10990 N NH2 . ARG F 153 ? 1.3244 0.7231 1.0932 -0.1470 -0.0176 -0.2352 153 ARG F NH2 10991 N N . ASN F 154 ? 1.1045 0.9690 1.4952 -0.1598 -0.0060 -0.3116 154 ASN F N 10992 C CA . ASN F 154 ? 1.1210 1.1021 1.6430 -0.1791 -0.0521 -0.3398 154 ASN F CA 10993 C C . ASN F 154 ? 1.1081 1.1551 1.7559 -0.2075 0.0127 -0.3699 154 ASN F C 10994 O O . ASN F 154 ? 1.1358 1.2582 1.8732 -0.2593 0.0029 -0.4052 154 ASN F O 10995 C CB . ASN F 154 ? 1.1106 1.1525 1.6914 -0.1206 -0.1215 -0.3227 154 ASN F CB 10996 C CG . ASN F 154 ? 1.1341 1.3141 1.8729 -0.1279 -0.1880 -0.3476 154 ASN F CG 10997 O OD1 . ASN F 154 ? 1.1787 1.3911 1.9305 -0.1850 -0.2231 -0.3732 154 ASN F OD1 10998 N ND2 . ASN F 154 ? 1.1136 1.3754 1.9769 -0.0696 -0.2076 -0.3405 154 ASN F ND2 10999 N N . GLY F 155 ? 1.0849 1.0940 1.7295 -0.1808 0.0808 -0.3582 155 GLY F N 11000 C CA . GLY F 155 ? 1.1016 1.1402 1.8382 -0.2083 0.1609 -0.3863 155 GLY F CA 11001 C C . GLY F 155 ? 1.0831 1.1884 1.9375 -0.1619 0.1782 -0.3857 155 GLY F C 11002 O O . GLY F 155 ? 1.1039 1.1667 1.9633 -0.1677 0.2646 -0.3942 155 GLY F O 11003 N N . THR F 156 ? 1.0689 1.2598 2.0030 -0.1148 0.1003 -0.3754 156 THR F N 11004 C CA . THR F 156 ? 1.0658 1.3033 2.0996 -0.0559 0.1146 -0.3693 156 THR F CA 11005 C C . THR F 156 ? 1.0752 1.1803 1.9487 -0.0137 0.1310 -0.3303 156 THR F C 11006 O O . THR F 156 ? 1.0708 1.1224 1.8302 0.0041 0.0706 -0.3023 156 THR F O 11007 C CB . THR F 156 ? 1.0619 1.4242 2.2271 -0.0111 0.0159 -0.3675 156 THR F CB 11008 N N . TYR F 157 ? 1.1079 1.1529 1.9661 -0.0058 0.2161 -0.3315 157 TYR F N 11009 C CA . TYR F 157 ? 1.1347 1.0473 1.8329 0.0197 0.2340 -0.2988 157 TYR F CA 11010 C C . TYR F 157 ? 1.1913 1.0567 1.9082 0.0357 0.3211 -0.3071 157 TYR F C 11011 O O . TYR F 157 ? 1.2205 1.0373 1.8959 0.0801 0.3198 -0.2884 157 TYR F O 11012 C CB . TYR F 157 ? 1.1471 0.9540 1.6882 -0.0192 0.2467 -0.2853 157 TYR F CB 11013 C CG . TYR F 157 ? 1.1769 0.8653 1.5646 -0.0020 0.2484 -0.2527 157 TYR F CG 11014 C CD1 . TYR F 157 ? 1.2492 0.8350 1.5567 -0.0120 0.3156 -0.2510 157 TYR F CD1 11015 C CD2 . TYR F 157 ? 1.1535 0.8249 1.4687 0.0164 0.1841 -0.2262 157 TYR F CD2 11016 C CE1 . TYR F 157 ? 1.2921 0.7728 1.4568 -0.0047 0.3047 -0.2228 157 TYR F CE1 11017 C CE2 . TYR F 157 ? 1.1825 0.7619 1.3755 0.0225 0.1827 -0.2009 157 TYR F CE2 11018 C CZ . TYR F 157 ? 1.2489 0.7389 1.3698 0.0114 0.2361 -0.1987 157 TYR F CZ 11019 O OH . TYR F 157 ? 1.2781 0.6802 1.2754 0.0093 0.2225 -0.1750 157 TYR F OH # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 PRO 1 0 ? ? ? A . n A 1 2 ASP 2 1 1 ASP ASP A . n A 1 3 GLN 3 2 2 GLN GLN A . n A 1 4 ILE 4 3 3 ILE ILE A . n A 1 5 CYS 5 4 4 CYS CYS A . n A 1 6 ILE 6 5 5 ILE ILE A . n A 1 7 GLY 7 6 6 GLY GLY A . n A 1 8 TYR 8 7 7 TYR TYR A . n A 1 9 HIS 9 8 8 HIS HIS A . n A 1 10 ALA 10 9 9 ALA ALA A . n A 1 11 ASN 11 10 10 ASN ASN A . n A 1 12 ASN 12 11 11 ASN ASN A . n A 1 13 SER 13 12 12 SER SER A . n A 1 14 THR 14 13 13 THR THR A . n A 1 15 GLU 15 14 14 GLU GLU A . n A 1 16 GLN 16 15 15 GLN GLN A . n A 1 17 VAL 17 16 16 VAL VAL A . n A 1 18 ASP 18 17 17 ASP ASP A . n A 1 19 THR 19 18 18 THR THR A . n A 1 20 ILE 20 19 19 ILE ILE A . n A 1 21 MET 21 20 20 MET MET A . n A 1 22 GLU 22 21 21 GLU GLU A . n A 1 23 LYS 23 22 22 LYS LYS A . n A 1 24 ASN 24 23 23 ASN ASN A . n A 1 25 VAL 25 24 24 VAL VAL A . n A 1 26 THR 26 25 25 THR THR A . n A 1 27 VAL 27 26 26 VAL VAL A . n A 1 28 THR 28 27 27 THR THR A . n A 1 29 HIS 29 28 28 HIS HIS A . n A 1 30 ALA 30 29 29 ALA ALA A . n A 1 31 GLN 31 30 30 GLN GLN A . n A 1 32 ASP 32 31 31 ASP ASP A . n A 1 33 ILE 33 32 32 ILE ILE A . n A 1 34 LEU 34 33 33 LEU LEU A . n A 1 35 GLU 35 34 34 GLU GLU A . n A 1 36 LYS 36 35 35 LYS LYS A . n A 1 37 THR 37 36 36 THR THR A . n A 1 38 HIS 38 37 37 HIS HIS A . n A 1 39 ASN 39 38 38 ASN ASN A . n A 1 40 GLY 40 39 39 GLY GLY A . n A 1 41 LYS 41 40 40 LYS LYS A . n A 1 42 LEU 42 41 41 LEU LEU A . n A 1 43 CYS 43 42 42 CYS CYS A . n A 1 44 ASP 44 43 43 ASP ASP A . n A 1 45 LEU 45 44 44 LEU LEU A . n A 1 46 ASP 46 45 45 ASP ASP A . n A 1 47 GLY 47 46 46 GLY GLY A . n A 1 48 VAL 48 47 47 VAL VAL A . n A 1 49 LYS 49 48 48 LYS LYS A . n A 1 50 PRO 50 49 49 PRO PRO A . n A 1 51 LEU 51 50 50 LEU LEU A . n A 1 52 ILE 52 51 51 ILE ILE A . n A 1 53 LEU 53 52 52 LEU LEU A . n A 1 54 ARG 54 53 53 ARG ARG A . n A 1 55 ASP 55 54 54 ASP ASP A . n A 1 56 CYS 56 55 55 CYS CYS A . n A 1 57 SER 57 56 56 SER SER A . n A 1 58 VAL 58 57 57 VAL VAL A . n A 1 59 ALA 59 58 58 ALA ALA A . n A 1 60 GLY 60 59 59 GLY GLY A . n A 1 61 TRP 61 60 60 TRP TRP A . n A 1 62 LEU 62 61 61 LEU LEU A . n A 1 63 LEU 63 62 62 LEU LEU A . n A 1 64 GLY 64 63 63 GLY GLY A . n A 1 65 ASN 65 64 64 ASN ASN A . n A 1 66 PRO 66 65 65 PRO PRO A . n A 1 67 MET 67 66 66 MET MET A . n A 1 68 CYS 68 67 67 CYS CYS A . n A 1 69 ASP 69 68 68 ASP ASP A . n A 1 70 GLU 70 69 69 GLU GLU A . n A 1 71 PHE 71 70 70 PHE PHE A . n A 1 72 LEU 72 71 71 LEU LEU A . n A 1 73 ASN 73 72 72 ASN ASN A . n A 1 74 VAL 74 73 73 VAL VAL A . n A 1 75 PRO 75 74 74 PRO PRO A . n A 1 76 GLU 76 75 75 GLU GLU A . n A 1 77 TRP 77 76 76 TRP TRP A . n A 1 78 SER 78 77 77 SER SER A . n A 1 79 TYR 79 78 78 TYR TYR A . n A 1 80 ILE 80 79 79 ILE ILE A . n A 1 81 VAL 81 80 80 VAL VAL A . n A 1 82 GLU 82 81 81 GLU GLU A . n A 1 83 LYS 83 82 82 LYS LYS A . n A 1 84 ILE 84 83 83 ILE ILE A . n A 1 85 ASN 85 84 84 ASN ASN A . n A 1 86 PRO 86 85 85 PRO PRO A . n A 1 87 ALA 87 86 86 ALA ALA A . n A 1 88 ASN 88 87 87 ASN ASN A . n A 1 89 ASP 89 88 88 ASP ASP A . n A 1 90 LEU 90 89 89 LEU LEU A . n A 1 91 CYS 91 90 90 CYS CYS A . n A 1 92 TYR 92 91 91 TYR TYR A . n A 1 93 PRO 93 92 92 PRO PRO A . n A 1 94 GLY 94 93 93 GLY GLY A . n A 1 95 ASN 95 94 94 ASN ASN A . n A 1 96 PHE 96 95 95 PHE PHE A . n A 1 97 ASN 97 96 96 ASN ASN A . n A 1 98 ASP 98 97 97 ASP ASP A . n A 1 99 TYR 99 98 98 TYR TYR A . n A 1 100 GLU 100 99 99 GLU GLU A . n A 1 101 GLU 101 100 100 GLU GLU A . n A 1 102 LEU 102 101 101 LEU LEU A . n A 1 103 LYS 103 102 102 LYS LYS A . n A 1 104 HIS 104 103 103 HIS HIS A . n A 1 105 LEU 105 104 104 LEU LEU A . n A 1 106 LEU 106 105 105 LEU LEU A . n A 1 107 SER 107 106 106 SER SER A . n A 1 108 ARG 108 107 107 ARG ARG A . n A 1 109 ILE 109 108 108 ILE ILE A . n A 1 110 ASN 110 109 109 ASN ASN A . n A 1 111 HIS 111 110 110 HIS HIS A . n A 1 112 PHE 112 111 111 PHE PHE A . n A 1 113 GLU 113 112 112 GLU GLU A . n A 1 114 LYS 114 113 113 LYS LYS A . n A 1 115 ILE 115 114 114 ILE ILE A . n A 1 116 GLN 116 115 115 GLN GLN A . n A 1 117 ILE 117 116 116 ILE ILE A . n A 1 118 ILE 118 117 117 ILE ILE A . n A 1 119 PRO 119 118 118 PRO PRO A . n A 1 120 LYS 120 119 119 LYS LYS A . n A 1 121 SER 121 120 120 SER SER A . n A 1 122 SER 122 121 121 SER SER A . n A 1 123 TRP 123 122 122 TRP TRP A . n A 1 124 SER 124 123 123 SER SER A . n A 1 125 ASP 125 124 124 ASP ASP A . n A 1 126 HIS 126 125 125 HIS HIS A . n A 1 127 GLU 127 126 126 GLU GLU A . n A 1 128 ALA 128 127 127 ALA ALA A . n A 1 129 SER 129 128 128 SER SER A . n A 1 130 ALA 130 129 129 ALA ALA A . n A 1 131 GLY 131 130 130 GLY GLY A . n A 1 132 VAL 132 131 131 VAL VAL A . n A 1 133 SER 133 132 132 SER SER A . n A 1 134 SER 134 133 133 SER SER A . n A 1 135 ALA 135 134 134 ALA ALA A . n A 1 136 CYS 136 135 135 CYS CYS A . n A 1 137 PRO 137 136 136 PRO PRO A . n A 1 138 TYR 138 137 137 TYR TYR A . n A 1 139 GLN 139 138 138 GLN GLN A . n A 1 140 GLY 140 139 139 GLY GLY A . n A 1 141 ARG 141 140 140 ARG ARG A . n A 1 142 SER 142 141 141 SER SER A . n A 1 143 SER 143 142 142 SER SER A . n A 1 144 PHE 144 143 143 PHE PHE A . n A 1 145 PHE 145 144 144 PHE PHE A . n A 1 146 ARG 146 145 145 ARG ARG A . n A 1 147 ASN 147 146 146 ASN ASN A . n A 1 148 VAL 148 147 147 VAL VAL A . n A 1 149 VAL 149 148 148 VAL VAL A . n A 1 150 TRP 150 149 149 TRP TRP A . n A 1 151 LEU 151 150 150 LEU LEU A . n A 1 152 ILE 152 151 151 ILE ILE A . n A 1 153 LYS 153 152 152 LYS LYS A . n A 1 154 LYS 154 153 153 LYS LYS A . n A 1 155 ASP 155 154 154 ASP ASP A . n A 1 156 ASN 156 155 155 ASN ASN A . n A 1 157 ALA 157 156 156 ALA ALA A . n A 1 158 TYR 158 157 157 TYR TYR A . n A 1 159 PRO 159 158 158 PRO PRO A . n A 1 160 THR 160 159 159 THR THR A . n A 1 161 ILE 161 160 160 ILE ILE A . n A 1 162 LYS 162 161 161 LYS LYS A . n A 1 163 ARG 163 162 162 ARG ARG A . n A 1 164 SER 164 163 163 SER SER A . n A 1 165 TYR 165 164 164 TYR TYR A . n A 1 166 ASN 166 165 165 ASN ASN A . n A 1 167 ASN 167 166 166 ASN ASN A . n A 1 168 THR 168 167 167 THR THR A . n A 1 169 ASN 169 168 168 ASN ASN A . n A 1 170 GLN 170 169 169 GLN GLN A . n A 1 171 GLU 171 170 170 GLU GLU A . n A 1 172 ASP 172 171 171 ASP ASP A . n A 1 173 LEU 173 172 172 LEU LEU A . n A 1 174 LEU 174 173 173 LEU LEU A . n A 1 175 VAL 175 174 174 VAL VAL A . n A 1 176 LEU 176 175 175 LEU LEU A . n A 1 177 TRP 177 176 176 TRP TRP A . n A 1 178 GLY 178 177 177 GLY GLY A . n A 1 179 ILE 179 178 178 ILE ILE A . n A 1 180 HIS 180 179 179 HIS HIS A . n A 1 181 HIS 181 180 180 HIS HIS A . n A 1 182 PRO 182 181 181 PRO PRO A . n A 1 183 ASN 183 182 182 ASN ASN A . n A 1 184 ASP 184 183 183 ASP ASP A . n A 1 185 ALA 185 184 184 ALA ALA A . n A 1 186 ALA 186 185 185 ALA ALA A . n A 1 187 GLU 187 186 186 GLU GLU A . n A 1 188 GLN 188 187 187 GLN GLN A . n A 1 189 THR 189 188 188 THR THR A . n A 1 190 ARG 190 189 189 ARG ARG A . n A 1 191 LEU 191 190 190 LEU LEU A . n A 1 192 TYR 192 191 191 TYR TYR A . n A 1 193 GLN 193 192 192 GLN GLN A . n A 1 194 ASN 194 193 193 ASN ASN A . n A 1 195 PRO 195 194 194 PRO PRO A . n A 1 196 THR 196 195 195 THR THR A . n A 1 197 THR 197 196 196 THR THR A . n A 1 198 TYR 198 197 197 TYR TYR A . n A 1 199 ILE 199 198 198 ILE ILE A . n A 1 200 SER 200 199 199 SER SER A . n A 1 201 VAL 201 200 200 VAL VAL A . n A 1 202 GLY 202 201 201 GLY GLY A . n A 1 203 THR 203 202 202 THR THR A . n A 1 204 SER 204 203 203 SER SER A . n A 1 205 THR 205 204 204 THR THR A . n A 1 206 LEU 206 205 205 LEU LEU A . n A 1 207 ASN 207 206 206 ASN ASN A . n A 1 208 GLN 208 207 207 GLN GLN A . n A 1 209 ARG 209 208 208 ARG ARG A . n A 1 210 LEU 210 209 209 LEU LEU A . n A 1 211 VAL 211 210 210 VAL VAL A . n A 1 212 PRO 212 211 211 PRO PRO A . n A 1 213 LYS 213 212 212 LYS LYS A . n A 1 214 ILE 214 213 213 ILE ILE A . n A 1 215 ALA 215 214 214 ALA ALA A . n A 1 216 THR 216 215 215 THR THR A . n A 1 217 ARG 217 216 216 ARG ARG A . n A 1 218 SER 218 217 217 SER SER A . n A 1 219 LYS 219 218 218 LYS LYS A . n A 1 220 VAL 220 219 219 VAL VAL A . n A 1 221 ASN 221 220 220 ASN ASN A . n A 1 222 GLY 222 221 221 GLY GLY A . n A 1 223 GLN 223 222 222 GLN GLN A . n A 1 224 SER 224 223 223 SER SER A . n A 1 225 GLY 225 224 224 GLY GLY A . n A 1 226 ARG 226 225 225 ARG ARG A . n A 1 227 MET 227 226 226 MET MET A . n A 1 228 GLU 228 227 227 GLU GLU A . n A 1 229 PHE 229 228 228 PHE PHE A . n A 1 230 PHE 230 229 229 PHE PHE A . n A 1 231 TRP 231 230 230 TRP TRP A . n A 1 232 THR 232 231 231 THR THR A . n A 1 233 ILE 233 232 232 ILE ILE A . n A 1 234 LEU 234 233 233 LEU LEU A . n A 1 235 LYS 235 234 234 LYS LYS A . n A 1 236 PRO 236 235 235 PRO PRO A . n A 1 237 ASN 237 236 236 ASN ASN A . n A 1 238 ASP 238 237 237 ASP ASP A . n A 1 239 ALA 239 238 238 ALA ALA A . n A 1 240 ILE 240 239 239 ILE ILE A . n A 1 241 ASN 241 240 240 ASN ASN A . n A 1 242 PHE 242 241 241 PHE PHE A . n A 1 243 GLU 243 242 242 GLU GLU A . n A 1 244 SER 244 243 243 SER SER A . n A 1 245 ASN 245 244 244 ASN ASN A . n A 1 246 GLY 246 245 245 GLY GLY A . n A 1 247 ASN 247 246 246 ASN ASN A . n A 1 248 PHE 248 247 247 PHE PHE A . n A 1 249 ILE 249 248 248 ILE ILE A . n A 1 250 ALA 250 249 249 ALA ALA A . n A 1 251 PRO 251 250 250 PRO PRO A . n A 1 252 GLU 252 251 251 GLU GLU A . n A 1 253 ASN 253 252 252 ASN ASN A . n A 1 254 ALA 254 253 253 ALA ALA A . n A 1 255 TYR 255 254 254 TYR TYR A . n A 1 256 LYS 256 255 255 LYS LYS A . n A 1 257 ILE 257 256 256 ILE ILE A . n A 1 258 VAL 258 257 257 VAL VAL A . n A 1 259 LYS 259 258 258 LYS LYS A . n A 1 260 LYS 260 259 259 LYS LYS A . n A 1 261 GLY 261 260 260 GLY GLY A . n A 1 262 ASP 262 261 261 ASP ASP A . n A 1 263 SER 263 262 262 SER SER A . n A 1 264 THR 264 263 263 THR THR A . n A 1 265 ILE 265 264 264 ILE ILE A . n A 1 266 MET 266 265 265 MET MET A . n A 1 267 LYS 267 266 266 LYS LYS A . n A 1 268 SER 268 267 267 SER SER A . n A 1 269 GLU 269 268 268 GLU GLU A . n A 1 270 LEU 270 269 269 LEU LEU A . n A 1 271 GLU 271 270 270 GLU GLU A . n A 1 272 TYR 272 271 271 TYR TYR A . n A 1 273 GLY 273 272 272 GLY GLY A . n A 1 274 ASN 274 273 273 ASN ASN A . n A 1 275 CYS 275 274 274 CYS CYS A . n A 1 276 ASN 276 275 275 ASN ASN A . n A 1 277 THR 277 276 276 THR THR A . n A 1 278 LYS 278 277 277 LYS LYS A . n A 1 279 CYS 279 278 278 CYS CYS A . n A 1 280 GLN 280 279 279 GLN GLN A . n A 1 281 THR 281 280 280 THR THR A . n A 1 282 PRO 282 281 281 PRO PRO A . n A 1 283 ILE 283 282 282 ILE ILE A . n A 1 284 GLY 284 283 283 GLY GLY A . n A 1 285 ALA 285 284 284 ALA ALA A . n A 1 286 ILE 286 285 285 ILE ILE A . n A 1 287 ASN 287 286 286 ASN ASN A . n A 1 288 SER 288 287 287 SER SER A . n A 1 289 SER 289 288 288 SER SER A . n A 1 290 MET 290 289 289 MET MET A . n A 1 291 PRO 291 290 290 PRO PRO A . n A 1 292 PHE 292 291 291 PHE PHE A . n A 1 293 HIS 293 292 292 HIS HIS A . n A 1 294 ASN 294 293 293 ASN ASN A . n A 1 295 ILE 295 294 294 ILE ILE A . n A 1 296 HIS 296 295 295 HIS HIS A . n A 1 297 PRO 297 296 296 PRO PRO A . n A 1 298 LEU 298 297 297 LEU LEU A . n A 1 299 THR 299 298 298 THR THR A . n A 1 300 ILE 300 299 299 ILE ILE A . n A 1 301 GLY 301 300 300 GLY GLY A . n A 1 302 GLU 302 301 301 GLU GLU A . n A 1 303 CYS 303 302 302 CYS CYS A . n A 1 304 PRO 304 303 303 PRO PRO A . n A 1 305 LYS 305 304 304 LYS LYS A . n A 1 306 TYR 306 305 305 TYR TYR A . n A 1 307 VAL 307 306 306 VAL VAL A . n A 1 308 LYS 308 307 307 LYS LYS A . n A 1 309 SER 309 308 308 SER SER A . n A 1 310 SER 310 309 309 SER SER A . n A 1 311 ARG 311 310 310 ARG ARG A . n A 1 312 LEU 312 311 311 LEU LEU A . n A 1 313 VAL 313 312 312 VAL VAL A . n A 1 314 LEU 314 313 313 LEU LEU A . n A 1 315 ALA 315 314 314 ALA ALA A . n A 1 316 THR 316 315 315 THR THR A . n A 1 317 GLY 317 316 316 GLY GLY A . n A 1 318 LEU 318 317 317 LEU LEU A . n A 1 319 ARG 319 318 318 ARG ARG A . n A 1 320 ASN 320 319 319 ASN ASN A . n A 1 321 SER 321 320 ? ? ? A . n A 1 322 PRO 322 321 ? ? ? A . n A 1 323 GLN 323 322 ? ? ? A . n A 1 324 ARG 324 323 ? ? ? A . n A 1 325 GLU 325 324 ? ? ? A . n A 1 326 THR 326 325 ? ? ? A . n A 1 327 ARG 327 326 ? ? ? A . n B 2 1 GLY 1 1 ? ? ? B . n B 2 2 LEU 2 2 ? ? ? B . n B 2 3 PHE 3 3 ? ? ? B . n B 2 4 GLY 4 4 ? ? ? B . n B 2 5 ALA 5 5 ? ? ? B . n B 2 6 ILE 6 6 ? ? ? B . n B 2 7 ALA 7 7 ? ? ? B . n B 2 8 GLY 8 8 ? ? ? B . n B 2 9 PHE 9 9 ? ? ? 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 GLU 29 29 29 GLU GLU 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 ILE 45 45 45 ILE ILE 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 VAL 48 48 48 VAL VAL 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 ILE 55 55 55 ILE ILE B . n B 2 56 ILE 56 56 56 ILE ILE B . n B 2 57 ASP 57 57 57 ASP ASP 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 ARG 68 68 68 ARG ARG 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 ASN 71 71 71 ASN ASN 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 ILE 77 77 77 ILE ILE 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 ARG 106 106 106 ARG ARG 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 LEU 124 124 124 LEU LEU 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 ALA 130 130 130 ALA ALA 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 ARG 143 143 143 ARG ARG 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 ASN 146 146 146 ASN ASN 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 GLU 150 150 150 GLU GLU 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 ARG 153 153 153 ARG ARG 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 ? ? ? B . n B 2 157 TYR 157 157 ? ? ? B . n B 2 158 ASP 158 158 ? ? ? B . n B 2 159 TYR 159 159 ? ? ? B . n B 2 160 PRO 160 160 ? ? ? B . n B 2 161 GLN 161 161 ? ? ? B . n B 2 162 TYR 162 162 ? ? ? B . n B 2 163 SER 163 163 ? ? ? B . n B 2 164 GLU 164 164 ? ? ? B . n B 2 165 GLU 165 165 ? ? ? B . n B 2 166 ALA 166 166 ? ? ? B . n C 1 1 PRO 1 0 ? ? ? C . n C 1 2 ASP 2 1 1 ASP ASP C . n C 1 3 GLN 3 2 2 GLN GLN C . n C 1 4 ILE 4 3 3 ILE ILE C . n C 1 5 CYS 5 4 4 CYS CYS C . n C 1 6 ILE 6 5 5 ILE ILE C . n C 1 7 GLY 7 6 6 GLY GLY C . n C 1 8 TYR 8 7 7 TYR TYR C . n C 1 9 HIS 9 8 8 HIS HIS C . n C 1 10 ALA 10 9 9 ALA ALA C . n C 1 11 ASN 11 10 10 ASN ASN C . n C 1 12 ASN 12 11 11 ASN ASN C . n C 1 13 SER 13 12 12 SER SER C . n C 1 14 THR 14 13 13 THR THR C . n C 1 15 GLU 15 14 14 GLU GLU C . n C 1 16 GLN 16 15 15 GLN GLN C . n C 1 17 VAL 17 16 16 VAL VAL C . n C 1 18 ASP 18 17 17 ASP ASP C . n C 1 19 THR 19 18 18 THR THR C . n C 1 20 ILE 20 19 19 ILE ILE C . n C 1 21 MET 21 20 20 MET MET C . n C 1 22 GLU 22 21 21 GLU GLU C . n C 1 23 LYS 23 22 22 LYS LYS C . n C 1 24 ASN 24 23 23 ASN ASN C . n C 1 25 VAL 25 24 24 VAL VAL C . n C 1 26 THR 26 25 25 THR THR C . n C 1 27 VAL 27 26 26 VAL VAL C . n C 1 28 THR 28 27 27 THR THR C . n C 1 29 HIS 29 28 28 HIS HIS C . n C 1 30 ALA 30 29 29 ALA ALA C . n C 1 31 GLN 31 30 30 GLN GLN C . n C 1 32 ASP 32 31 31 ASP ASP C . n C 1 33 ILE 33 32 32 ILE ILE C . n C 1 34 LEU 34 33 33 LEU LEU C . n C 1 35 GLU 35 34 34 GLU GLU C . n C 1 36 LYS 36 35 35 LYS LYS C . n C 1 37 THR 37 36 36 THR THR C . n C 1 38 HIS 38 37 37 HIS HIS C . n C 1 39 ASN 39 38 38 ASN ASN C . n C 1 40 GLY 40 39 39 GLY GLY C . n C 1 41 LYS 41 40 40 LYS LYS C . n C 1 42 LEU 42 41 41 LEU LEU C . n C 1 43 CYS 43 42 42 CYS CYS C . n C 1 44 ASP 44 43 43 ASP ASP C . n C 1 45 LEU 45 44 44 LEU LEU C . n C 1 46 ASP 46 45 45 ASP ASP C . n C 1 47 GLY 47 46 46 GLY GLY C . n C 1 48 VAL 48 47 47 VAL VAL C . n C 1 49 LYS 49 48 48 LYS LYS C . n C 1 50 PRO 50 49 49 PRO PRO C . n C 1 51 LEU 51 50 50 LEU LEU C . n C 1 52 ILE 52 51 51 ILE ILE C . n C 1 53 LEU 53 52 52 LEU LEU C . n C 1 54 ARG 54 53 53 ARG ARG C . n C 1 55 ASP 55 54 54 ASP ASP C . n C 1 56 CYS 56 55 55 CYS CYS C . n C 1 57 SER 57 56 56 SER SER C . n C 1 58 VAL 58 57 57 VAL VAL C . n C 1 59 ALA 59 58 58 ALA ALA C . n C 1 60 GLY 60 59 59 GLY GLY C . n C 1 61 TRP 61 60 60 TRP TRP C . n C 1 62 LEU 62 61 61 LEU LEU C . n C 1 63 LEU 63 62 62 LEU LEU C . n C 1 64 GLY 64 63 63 GLY GLY C . n C 1 65 ASN 65 64 64 ASN ASN C . n C 1 66 PRO 66 65 65 PRO PRO C . n C 1 67 MET 67 66 66 MET MET C . n C 1 68 CYS 68 67 67 CYS CYS C . n C 1 69 ASP 69 68 68 ASP ASP C . n C 1 70 GLU 70 69 69 GLU GLU C . n C 1 71 PHE 71 70 70 PHE PHE C . n C 1 72 LEU 72 71 71 LEU LEU C . n C 1 73 ASN 73 72 72 ASN ASN C . n C 1 74 VAL 74 73 73 VAL VAL C . n C 1 75 PRO 75 74 74 PRO PRO C . n C 1 76 GLU 76 75 75 GLU GLU C . n C 1 77 TRP 77 76 76 TRP TRP C . n C 1 78 SER 78 77 77 SER SER C . n C 1 79 TYR 79 78 78 TYR TYR C . n C 1 80 ILE 80 79 79 ILE ILE C . n C 1 81 VAL 81 80 80 VAL VAL C . n C 1 82 GLU 82 81 81 GLU GLU C . n C 1 83 LYS 83 82 82 LYS LYS C . n C 1 84 ILE 84 83 83 ILE ILE C . n C 1 85 ASN 85 84 84 ASN ASN C . n C 1 86 PRO 86 85 85 PRO PRO C . n C 1 87 ALA 87 86 86 ALA ALA C . n C 1 88 ASN 88 87 87 ASN ASN C . n C 1 89 ASP 89 88 88 ASP ASP C . n C 1 90 LEU 90 89 89 LEU LEU C . n C 1 91 CYS 91 90 90 CYS CYS C . n C 1 92 TYR 92 91 91 TYR TYR C . n C 1 93 PRO 93 92 92 PRO PRO C . n C 1 94 GLY 94 93 93 GLY GLY C . n C 1 95 ASN 95 94 94 ASN ASN C . n C 1 96 PHE 96 95 95 PHE PHE C . n C 1 97 ASN 97 96 96 ASN ASN C . n C 1 98 ASP 98 97 97 ASP ASP C . n C 1 99 TYR 99 98 98 TYR TYR C . n C 1 100 GLU 100 99 99 GLU GLU C . n C 1 101 GLU 101 100 100 GLU GLU C . n C 1 102 LEU 102 101 101 LEU LEU C . n C 1 103 LYS 103 102 102 LYS LYS C . n C 1 104 HIS 104 103 103 HIS HIS C . n C 1 105 LEU 105 104 104 LEU LEU C . n C 1 106 LEU 106 105 105 LEU LEU C . n C 1 107 SER 107 106 106 SER SER C . n C 1 108 ARG 108 107 107 ARG ARG C . n C 1 109 ILE 109 108 108 ILE ILE C . n C 1 110 ASN 110 109 109 ASN ASN C . n C 1 111 HIS 111 110 110 HIS HIS C . n C 1 112 PHE 112 111 111 PHE PHE C . n C 1 113 GLU 113 112 112 GLU GLU C . n C 1 114 LYS 114 113 113 LYS LYS C . n C 1 115 ILE 115 114 114 ILE ILE C . n C 1 116 GLN 116 115 115 GLN GLN C . n C 1 117 ILE 117 116 116 ILE ILE C . n C 1 118 ILE 118 117 117 ILE ILE C . n C 1 119 PRO 119 118 118 PRO PRO C . n C 1 120 LYS 120 119 119 LYS LYS C . n C 1 121 SER 121 120 120 SER SER C . n C 1 122 SER 122 121 121 SER SER C . n C 1 123 TRP 123 122 122 TRP TRP C . n C 1 124 SER 124 123 123 SER SER C . n C 1 125 ASP 125 124 124 ASP ASP C . n C 1 126 HIS 126 125 125 HIS HIS C . n C 1 127 GLU 127 126 126 GLU GLU C . n C 1 128 ALA 128 127 127 ALA ALA C . n C 1 129 SER 129 128 128 SER SER C . n C 1 130 ALA 130 129 129 ALA ALA C . n C 1 131 GLY 131 130 130 GLY GLY C . n C 1 132 VAL 132 131 131 VAL VAL C . n C 1 133 SER 133 132 132 SER SER C . n C 1 134 SER 134 133 133 SER SER C . n C 1 135 ALA 135 134 134 ALA ALA C . n C 1 136 CYS 136 135 135 CYS CYS C . n C 1 137 PRO 137 136 136 PRO PRO C . n C 1 138 TYR 138 137 137 TYR TYR C . n C 1 139 GLN 139 138 138 GLN GLN C . n C 1 140 GLY 140 139 139 GLY GLY C . n C 1 141 ARG 141 140 140 ARG ARG C . n C 1 142 SER 142 141 141 SER SER C . n C 1 143 SER 143 142 142 SER SER C . n C 1 144 PHE 144 143 143 PHE PHE C . n C 1 145 PHE 145 144 144 PHE PHE C . n C 1 146 ARG 146 145 145 ARG ARG C . n C 1 147 ASN 147 146 146 ASN ASN C . n C 1 148 VAL 148 147 147 VAL VAL C . n C 1 149 VAL 149 148 148 VAL VAL C . n C 1 150 TRP 150 149 149 TRP TRP C . n C 1 151 LEU 151 150 150 LEU LEU C . n C 1 152 ILE 152 151 151 ILE ILE C . n C 1 153 LYS 153 152 152 LYS LYS C . n C 1 154 LYS 154 153 153 LYS LYS C . n C 1 155 ASP 155 154 154 ASP ASP C . n C 1 156 ASN 156 155 155 ASN ASN C . n C 1 157 ALA 157 156 156 ALA ALA C . n C 1 158 TYR 158 157 157 TYR TYR C . n C 1 159 PRO 159 158 158 PRO PRO C . n C 1 160 THR 160 159 159 THR THR C . n C 1 161 ILE 161 160 160 ILE ILE C . n C 1 162 LYS 162 161 161 LYS LYS C . n C 1 163 ARG 163 162 162 ARG ARG C . n C 1 164 SER 164 163 163 SER SER C . n C 1 165 TYR 165 164 164 TYR TYR C . n C 1 166 ASN 166 165 165 ASN ASN C . n C 1 167 ASN 167 166 166 ASN ASN C . n C 1 168 THR 168 167 167 THR THR C . n C 1 169 ASN 169 168 168 ASN ASN C . n C 1 170 GLN 170 169 169 GLN GLN C . n C 1 171 GLU 171 170 170 GLU GLU C . n C 1 172 ASP 172 171 171 ASP ASP C . n C 1 173 LEU 173 172 172 LEU LEU C . n C 1 174 LEU 174 173 173 LEU LEU C . n C 1 175 VAL 175 174 174 VAL VAL C . n C 1 176 LEU 176 175 175 LEU LEU C . n C 1 177 TRP 177 176 176 TRP TRP C . n C 1 178 GLY 178 177 177 GLY GLY C . n C 1 179 ILE 179 178 178 ILE ILE C . n C 1 180 HIS 180 179 179 HIS HIS C . n C 1 181 HIS 181 180 180 HIS HIS C . n C 1 182 PRO 182 181 181 PRO PRO C . n C 1 183 ASN 183 182 182 ASN ASN C . n C 1 184 ASP 184 183 183 ASP ASP C . n C 1 185 ALA 185 184 184 ALA ALA C . n C 1 186 ALA 186 185 185 ALA ALA C . n C 1 187 GLU 187 186 186 GLU GLU C . n C 1 188 GLN 188 187 187 GLN GLN C . n C 1 189 THR 189 188 188 THR THR C . n C 1 190 ARG 190 189 189 ARG ARG C . n C 1 191 LEU 191 190 190 LEU LEU C . n C 1 192 TYR 192 191 191 TYR TYR C . n C 1 193 GLN 193 192 192 GLN GLN C . n C 1 194 ASN 194 193 193 ASN ASN C . n C 1 195 PRO 195 194 194 PRO PRO C . n C 1 196 THR 196 195 195 THR THR C . n C 1 197 THR 197 196 196 THR THR C . n C 1 198 TYR 198 197 197 TYR TYR C . n C 1 199 ILE 199 198 198 ILE ILE C . n C 1 200 SER 200 199 199 SER SER C . n C 1 201 VAL 201 200 200 VAL VAL C . n C 1 202 GLY 202 201 201 GLY GLY C . n C 1 203 THR 203 202 202 THR THR C . n C 1 204 SER 204 203 203 SER SER C . n C 1 205 THR 205 204 204 THR THR C . n C 1 206 LEU 206 205 205 LEU LEU C . n C 1 207 ASN 207 206 206 ASN ASN C . n C 1 208 GLN 208 207 207 GLN GLN C . n C 1 209 ARG 209 208 208 ARG ARG C . n C 1 210 LEU 210 209 209 LEU LEU C . n C 1 211 VAL 211 210 210 VAL VAL C . n C 1 212 PRO 212 211 211 PRO PRO C . n C 1 213 LYS 213 212 212 LYS LYS C . n C 1 214 ILE 214 213 213 ILE ILE C . n C 1 215 ALA 215 214 214 ALA ALA C . n C 1 216 THR 216 215 215 THR THR C . n C 1 217 ARG 217 216 216 ARG ARG C . n C 1 218 SER 218 217 217 SER SER C . n C 1 219 LYS 219 218 218 LYS LYS C . n C 1 220 VAL 220 219 219 VAL VAL C . n C 1 221 ASN 221 220 220 ASN ASN C . n C 1 222 GLY 222 221 221 GLY GLY C . n C 1 223 GLN 223 222 222 GLN GLN C . n C 1 224 SER 224 223 223 SER SER C . n C 1 225 GLY 225 224 224 GLY GLY C . n C 1 226 ARG 226 225 225 ARG ARG C . n C 1 227 MET 227 226 226 MET MET C . n C 1 228 GLU 228 227 227 GLU GLU C . n C 1 229 PHE 229 228 228 PHE PHE C . n C 1 230 PHE 230 229 229 PHE PHE C . n C 1 231 TRP 231 230 230 TRP TRP C . n C 1 232 THR 232 231 231 THR THR C . n C 1 233 ILE 233 232 232 ILE ILE C . n C 1 234 LEU 234 233 233 LEU LEU C . n C 1 235 LYS 235 234 234 LYS LYS C . n C 1 236 PRO 236 235 235 PRO PRO C . n C 1 237 ASN 237 236 236 ASN ASN C . n C 1 238 ASP 238 237 237 ASP ASP C . n C 1 239 ALA 239 238 238 ALA ALA C . n C 1 240 ILE 240 239 239 ILE ILE C . n C 1 241 ASN 241 240 240 ASN ASN C . n C 1 242 PHE 242 241 241 PHE PHE C . n C 1 243 GLU 243 242 242 GLU GLU C . n C 1 244 SER 244 243 243 SER SER C . n C 1 245 ASN 245 244 244 ASN ASN C . n C 1 246 GLY 246 245 245 GLY GLY C . n C 1 247 ASN 247 246 246 ASN ASN C . n C 1 248 PHE 248 247 247 PHE PHE C . n C 1 249 ILE 249 248 248 ILE ILE C . n C 1 250 ALA 250 249 249 ALA ALA C . n C 1 251 PRO 251 250 250 PRO PRO C . n C 1 252 GLU 252 251 251 GLU GLU C . n C 1 253 ASN 253 252 252 ASN ASN C . n C 1 254 ALA 254 253 253 ALA ALA C . n C 1 255 TYR 255 254 254 TYR TYR C . n C 1 256 LYS 256 255 255 LYS LYS C . n C 1 257 ILE 257 256 256 ILE ILE C . n C 1 258 VAL 258 257 257 VAL VAL C . n C 1 259 LYS 259 258 258 LYS LYS C . n C 1 260 LYS 260 259 259 LYS LYS C . n C 1 261 GLY 261 260 260 GLY GLY C . n C 1 262 ASP 262 261 261 ASP ASP C . n C 1 263 SER 263 262 262 SER SER C . n C 1 264 THR 264 263 263 THR THR C . n C 1 265 ILE 265 264 264 ILE ILE C . n C 1 266 MET 266 265 265 MET MET C . n C 1 267 LYS 267 266 266 LYS LYS C . n C 1 268 SER 268 267 267 SER SER C . n C 1 269 GLU 269 268 268 GLU GLU C . n C 1 270 LEU 270 269 269 LEU LEU C . n C 1 271 GLU 271 270 270 GLU GLU C . n C 1 272 TYR 272 271 271 TYR TYR C . n C 1 273 GLY 273 272 272 GLY GLY C . n C 1 274 ASN 274 273 273 ASN ASN C . n C 1 275 CYS 275 274 274 CYS CYS C . n C 1 276 ASN 276 275 275 ASN ASN C . n C 1 277 THR 277 276 276 THR THR C . n C 1 278 LYS 278 277 277 LYS LYS C . n C 1 279 CYS 279 278 278 CYS CYS C . n C 1 280 GLN 280 279 279 GLN GLN C . n C 1 281 THR 281 280 280 THR THR C . n C 1 282 PRO 282 281 281 PRO PRO C . n C 1 283 ILE 283 282 282 ILE ILE C . n C 1 284 GLY 284 283 283 GLY GLY C . n C 1 285 ALA 285 284 284 ALA ALA C . n C 1 286 ILE 286 285 285 ILE ILE C . n C 1 287 ASN 287 286 286 ASN ASN C . n C 1 288 SER 288 287 287 SER SER C . n C 1 289 SER 289 288 288 SER SER C . n C 1 290 MET 290 289 289 MET MET C . n C 1 291 PRO 291 290 290 PRO PRO C . n C 1 292 PHE 292 291 291 PHE PHE C . n C 1 293 HIS 293 292 292 HIS HIS C . n C 1 294 ASN 294 293 293 ASN ASN C . n C 1 295 ILE 295 294 294 ILE ILE C . n C 1 296 HIS 296 295 295 HIS HIS C . n C 1 297 PRO 297 296 296 PRO PRO C . n C 1 298 LEU 298 297 297 LEU LEU C . n C 1 299 THR 299 298 298 THR THR C . n C 1 300 ILE 300 299 299 ILE ILE C . n C 1 301 GLY 301 300 300 GLY GLY C . n C 1 302 GLU 302 301 301 GLU GLU C . n C 1 303 CYS 303 302 302 CYS CYS C . n C 1 304 PRO 304 303 303 PRO PRO C . n C 1 305 LYS 305 304 304 LYS LYS C . n C 1 306 TYR 306 305 305 TYR TYR C . n C 1 307 VAL 307 306 306 VAL VAL C . n C 1 308 LYS 308 307 307 LYS LYS C . n C 1 309 SER 309 308 308 SER SER C . n C 1 310 SER 310 309 309 SER SER C . n C 1 311 ARG 311 310 310 ARG ARG C . n C 1 312 LEU 312 311 311 LEU LEU C . n C 1 313 VAL 313 312 312 VAL VAL C . n C 1 314 LEU 314 313 313 LEU LEU C . n C 1 315 ALA 315 314 314 ALA ALA C . n C 1 316 THR 316 315 315 THR THR C . n C 1 317 GLY 317 316 316 GLY GLY C . n C 1 318 LEU 318 317 317 LEU LEU C . n C 1 319 ARG 319 318 318 ARG ARG C . n C 1 320 ASN 320 319 319 ASN ASN C . n C 1 321 SER 321 320 ? ? ? C . n C 1 322 PRO 322 321 ? ? ? C . n C 1 323 GLN 323 322 ? ? ? C . n C 1 324 ARG 324 323 ? ? ? C . n C 1 325 GLU 325 324 ? ? ? C . n C 1 326 THR 326 325 ? ? ? C . n C 1 327 ARG 327 326 ? ? ? C . n D 2 1 GLY 1 1 ? ? ? D . n D 2 2 LEU 2 2 ? ? ? D . n D 2 3 PHE 3 3 ? ? ? D . n D 2 4 GLY 4 4 ? ? ? D . n D 2 5 ALA 5 5 ? ? ? D . n D 2 6 ILE 6 6 ? ? ? D . n D 2 7 ALA 7 7 ? ? ? D . n D 2 8 GLY 8 8 ? ? ? D . n D 2 9 PHE 9 9 ? ? ? D . n D 2 10 ILE 10 10 10 ILE ILE D . n D 2 11 GLU 11 11 11 GLU GLU D . n D 2 12 GLY 12 12 12 GLY GLY D . n D 2 13 GLY 13 13 13 GLY GLY D . n D 2 14 TRP 14 14 14 TRP TRP D . n D 2 15 GLN 15 15 15 GLN GLN D . n D 2 16 GLY 16 16 16 GLY GLY D . n D 2 17 MET 17 17 17 MET MET D . n D 2 18 VAL 18 18 18 VAL VAL D . n D 2 19 ASP 19 19 19 ASP ASP D . n D 2 20 GLY 20 20 20 GLY GLY D . n D 2 21 TRP 21 21 21 TRP TRP D . n D 2 22 TYR 22 22 22 TYR TYR D . n D 2 23 GLY 23 23 23 GLY GLY D . n D 2 24 TYR 24 24 24 TYR TYR D . n D 2 25 HIS 25 25 25 HIS HIS D . n D 2 26 HIS 26 26 26 HIS HIS D . n D 2 27 SER 27 27 27 SER SER D . n D 2 28 ASN 28 28 28 ASN ASN D . n D 2 29 GLU 29 29 29 GLU GLU D . n D 2 30 GLN 30 30 30 GLN GLN D . n D 2 31 GLY 31 31 31 GLY GLY D . n D 2 32 SER 32 32 32 SER SER D . n D 2 33 GLY 33 33 33 GLY GLY D . n D 2 34 TYR 34 34 34 TYR TYR D . n D 2 35 ALA 35 35 35 ALA ALA D . n D 2 36 ALA 36 36 36 ALA ALA D . n D 2 37 ASP 37 37 37 ASP ASP D . n D 2 38 LYS 38 38 38 LYS LYS D . n D 2 39 GLU 39 39 39 GLU GLU D . n D 2 40 SER 40 40 40 SER SER D . n D 2 41 THR 41 41 41 THR THR D . n D 2 42 GLN 42 42 42 GLN GLN D . n D 2 43 LYS 43 43 43 LYS LYS D . n D 2 44 ALA 44 44 44 ALA ALA D . n D 2 45 ILE 45 45 45 ILE ILE D . n D 2 46 ASP 46 46 46 ASP ASP D . n D 2 47 GLY 47 47 47 GLY GLY D . n D 2 48 VAL 48 48 48 VAL VAL D . n D 2 49 THR 49 49 49 THR THR D . n D 2 50 ASN 50 50 50 ASN ASN D . n D 2 51 LYS 51 51 51 LYS LYS D . n D 2 52 VAL 52 52 52 VAL VAL D . n D 2 53 ASN 53 53 53 ASN ASN D . n D 2 54 SER 54 54 54 SER SER D . n D 2 55 ILE 55 55 55 ILE ILE D . n D 2 56 ILE 56 56 56 ILE ILE D . n D 2 57 ASP 57 57 57 ASP ASP D . n D 2 58 LYS 58 58 58 LYS LYS D . n D 2 59 MET 59 59 59 MET MET D . n D 2 60 ASN 60 60 60 ASN ASN D . n D 2 61 THR 61 61 61 THR THR D . n D 2 62 GLN 62 62 62 GLN GLN D . n D 2 63 PHE 63 63 63 PHE PHE D . n D 2 64 GLU 64 64 64 GLU GLU D . n D 2 65 ALA 65 65 65 ALA ALA D . n D 2 66 VAL 66 66 66 VAL VAL D . n D 2 67 GLY 67 67 67 GLY GLY D . n D 2 68 ARG 68 68 68 ARG ARG D . n D 2 69 GLU 69 69 69 GLU GLU D . n D 2 70 PHE 70 70 70 PHE PHE D . n D 2 71 ASN 71 71 71 ASN ASN D . n D 2 72 ASN 72 72 72 ASN ASN D . n D 2 73 LEU 73 73 73 LEU LEU D . n D 2 74 GLU 74 74 74 GLU GLU D . n D 2 75 ARG 75 75 75 ARG ARG D . n D 2 76 ARG 76 76 76 ARG ARG D . n D 2 77 ILE 77 77 77 ILE ILE D . n D 2 78 GLU 78 78 78 GLU GLU D . n D 2 79 ASN 79 79 79 ASN ASN D . n D 2 80 LEU 80 80 80 LEU LEU D . n D 2 81 ASN 81 81 81 ASN ASN D . n D 2 82 LYS 82 82 82 LYS LYS D . n D 2 83 LYS 83 83 83 LYS LYS D . n D 2 84 MET 84 84 84 MET MET D . n D 2 85 GLU 85 85 85 GLU GLU D . n D 2 86 ASP 86 86 86 ASP ASP D . n D 2 87 GLY 87 87 87 GLY GLY D . n D 2 88 PHE 88 88 88 PHE PHE D . n D 2 89 LEU 89 89 89 LEU LEU D . n D 2 90 ASP 90 90 90 ASP ASP D . n D 2 91 VAL 91 91 91 VAL VAL D . n D 2 92 TRP 92 92 92 TRP TRP D . n D 2 93 THR 93 93 93 THR THR D . n D 2 94 TYR 94 94 94 TYR TYR D . n D 2 95 ASN 95 95 95 ASN ASN D . n D 2 96 ALA 96 96 96 ALA ALA D . n D 2 97 GLU 97 97 97 GLU GLU D . n D 2 98 LEU 98 98 98 LEU LEU D . n D 2 99 LEU 99 99 99 LEU LEU D . n D 2 100 VAL 100 100 100 VAL VAL D . n D 2 101 LEU 101 101 101 LEU LEU D . n D 2 102 MET 102 102 102 MET MET D . n D 2 103 GLU 103 103 103 GLU GLU D . n D 2 104 ASN 104 104 104 ASN ASN D . n D 2 105 GLU 105 105 105 GLU GLU D . n D 2 106 ARG 106 106 106 ARG ARG D . n D 2 107 THR 107 107 107 THR THR D . n D 2 108 LEU 108 108 108 LEU LEU D . n D 2 109 ASP 109 109 109 ASP ASP D . n D 2 110 PHE 110 110 110 PHE PHE D . n D 2 111 HIS 111 111 111 HIS HIS D . n D 2 112 ASP 112 112 112 ASP ASP D . n D 2 113 SER 113 113 113 SER SER D . n D 2 114 ASN 114 114 114 ASN ASN D . n D 2 115 VAL 115 115 115 VAL VAL D . n D 2 116 LYS 116 116 116 LYS LYS D . n D 2 117 ASN 117 117 117 ASN ASN D . n D 2 118 LEU 118 118 118 LEU LEU D . n D 2 119 TYR 119 119 119 TYR TYR D . n D 2 120 ASP 120 120 120 ASP ASP D . n D 2 121 LYS 121 121 121 LYS LYS D . n D 2 122 VAL 122 122 122 VAL VAL D . n D 2 123 ARG 123 123 123 ARG ARG D . n D 2 124 LEU 124 124 124 LEU LEU D . n D 2 125 GLN 125 125 125 GLN GLN D . n D 2 126 LEU 126 126 126 LEU LEU D . n D 2 127 ARG 127 127 127 ARG ARG D . n D 2 128 ASP 128 128 128 ASP ASP D . n D 2 129 ASN 129 129 129 ASN ASN D . n D 2 130 ALA 130 130 130 ALA ALA D . n D 2 131 LYS 131 131 131 LYS LYS D . n D 2 132 GLU 132 132 132 GLU GLU D . n D 2 133 LEU 133 133 133 LEU LEU D . n D 2 134 GLY 134 134 134 GLY GLY D . n D 2 135 ASN 135 135 135 ASN ASN D . n D 2 136 GLY 136 136 136 GLY GLY D . n D 2 137 CYS 137 137 137 CYS CYS D . n D 2 138 PHE 138 138 138 PHE PHE D . n D 2 139 GLU 139 139 139 GLU GLU D . n D 2 140 PHE 140 140 140 PHE PHE D . n D 2 141 TYR 141 141 141 TYR TYR D . n D 2 142 HIS 142 142 142 HIS HIS D . n D 2 143 ARG 143 143 143 ARG ARG D . n D 2 144 CYS 144 144 144 CYS CYS D . n D 2 145 ASP 145 145 145 ASP ASP D . n D 2 146 ASN 146 146 146 ASN ASN D . n D 2 147 GLU 147 147 147 GLU GLU D . n D 2 148 CYS 148 148 148 CYS CYS D . n D 2 149 MET 149 149 149 MET MET D . n D 2 150 GLU 150 150 150 GLU GLU D . n D 2 151 SER 151 151 151 SER SER D . n D 2 152 VAL 152 152 152 VAL VAL D . n D 2 153 ARG 153 153 153 ARG ARG D . n D 2 154 ASN 154 154 154 ASN ASN D . n D 2 155 GLY 155 155 155 GLY GLY D . n D 2 156 THR 156 156 156 THR THR D . n D 2 157 TYR 157 157 157 TYR TYR D . n D 2 158 ASP 158 158 ? ? ? D . n D 2 159 TYR 159 159 ? ? ? D . n D 2 160 PRO 160 160 ? ? ? D . n D 2 161 GLN 161 161 ? ? ? D . n D 2 162 TYR 162 162 ? ? ? D . n D 2 163 SER 163 163 ? ? ? D . n D 2 164 GLU 164 164 ? ? ? D . n D 2 165 GLU 165 165 ? ? ? D . n D 2 166 ALA 166 166 ? ? ? D . n E 1 1 PRO 1 0 0 PRO PRO E . n E 1 2 ASP 2 1 1 ASP ASP E . n E 1 3 GLN 3 2 2 GLN GLN E . n E 1 4 ILE 4 3 3 ILE ILE E . n E 1 5 CYS 5 4 4 CYS CYS E . n E 1 6 ILE 6 5 5 ILE ILE E . n E 1 7 GLY 7 6 6 GLY GLY E . n E 1 8 TYR 8 7 7 TYR TYR E . n E 1 9 HIS 9 8 8 HIS HIS E . n E 1 10 ALA 10 9 9 ALA ALA E . n E 1 11 ASN 11 10 10 ASN ASN E . n E 1 12 ASN 12 11 11 ASN ASN E . n E 1 13 SER 13 12 12 SER SER E . n E 1 14 THR 14 13 13 THR THR E . n E 1 15 GLU 15 14 14 GLU GLU E . n E 1 16 GLN 16 15 15 GLN GLN E . n E 1 17 VAL 17 16 16 VAL VAL E . n E 1 18 ASP 18 17 17 ASP ASP E . n E 1 19 THR 19 18 18 THR THR E . n E 1 20 ILE 20 19 19 ILE ILE E . n E 1 21 MET 21 20 20 MET MET E . n E 1 22 GLU 22 21 21 GLU GLU E . n E 1 23 LYS 23 22 22 LYS LYS E . n E 1 24 ASN 24 23 23 ASN ASN E . n E 1 25 VAL 25 24 24 VAL VAL E . n E 1 26 THR 26 25 25 THR THR E . n E 1 27 VAL 27 26 26 VAL VAL E . n E 1 28 THR 28 27 27 THR THR E . n E 1 29 HIS 29 28 28 HIS HIS E . n E 1 30 ALA 30 29 29 ALA ALA E . n E 1 31 GLN 31 30 30 GLN GLN E . n E 1 32 ASP 32 31 31 ASP ASP E . n E 1 33 ILE 33 32 32 ILE ILE E . n E 1 34 LEU 34 33 33 LEU LEU E . n E 1 35 GLU 35 34 34 GLU GLU E . n E 1 36 LYS 36 35 35 LYS LYS E . n E 1 37 THR 37 36 36 THR THR E . n E 1 38 HIS 38 37 37 HIS HIS E . n E 1 39 ASN 39 38 38 ASN ASN E . n E 1 40 GLY 40 39 39 GLY GLY E . n E 1 41 LYS 41 40 40 LYS LYS E . n E 1 42 LEU 42 41 41 LEU LEU E . n E 1 43 CYS 43 42 42 CYS CYS E . n E 1 44 ASP 44 43 43 ASP ASP E . n E 1 45 LEU 45 44 44 LEU LEU E . n E 1 46 ASP 46 45 45 ASP ASP E . n E 1 47 GLY 47 46 46 GLY GLY E . n E 1 48 VAL 48 47 47 VAL VAL E . n E 1 49 LYS 49 48 48 LYS LYS E . n E 1 50 PRO 50 49 49 PRO PRO E . n E 1 51 LEU 51 50 50 LEU LEU E . n E 1 52 ILE 52 51 51 ILE ILE E . n E 1 53 LEU 53 52 52 LEU LEU E . n E 1 54 ARG 54 53 53 ARG ARG E . n E 1 55 ASP 55 54 54 ASP ASP E . n E 1 56 CYS 56 55 55 CYS CYS E . n E 1 57 SER 57 56 56 SER SER E . n E 1 58 VAL 58 57 57 VAL VAL E . n E 1 59 ALA 59 58 58 ALA ALA E . n E 1 60 GLY 60 59 59 GLY GLY E . n E 1 61 TRP 61 60 60 TRP TRP E . n E 1 62 LEU 62 61 61 LEU LEU E . n E 1 63 LEU 63 62 62 LEU LEU E . n E 1 64 GLY 64 63 63 GLY GLY E . n E 1 65 ASN 65 64 64 ASN ASN E . n E 1 66 PRO 66 65 65 PRO PRO E . n E 1 67 MET 67 66 66 MET MET E . n E 1 68 CYS 68 67 67 CYS CYS E . n E 1 69 ASP 69 68 68 ASP ASP E . n E 1 70 GLU 70 69 69 GLU GLU E . n E 1 71 PHE 71 70 70 PHE PHE E . n E 1 72 LEU 72 71 71 LEU LEU E . n E 1 73 ASN 73 72 72 ASN ASN E . n E 1 74 VAL 74 73 73 VAL VAL E . n E 1 75 PRO 75 74 74 PRO PRO E . n E 1 76 GLU 76 75 75 GLU GLU E . n E 1 77 TRP 77 76 76 TRP TRP E . n E 1 78 SER 78 77 77 SER SER E . n E 1 79 TYR 79 78 78 TYR TYR E . n E 1 80 ILE 80 79 79 ILE ILE E . n E 1 81 VAL 81 80 80 VAL VAL E . n E 1 82 GLU 82 81 81 GLU GLU E . n E 1 83 LYS 83 82 82 LYS LYS E . n E 1 84 ILE 84 83 83 ILE ILE E . n E 1 85 ASN 85 84 84 ASN ASN E . n E 1 86 PRO 86 85 85 PRO PRO E . n E 1 87 ALA 87 86 86 ALA ALA E . n E 1 88 ASN 88 87 87 ASN ASN E . n E 1 89 ASP 89 88 88 ASP ASP E . n E 1 90 LEU 90 89 89 LEU LEU E . n E 1 91 CYS 91 90 90 CYS CYS E . n E 1 92 TYR 92 91 91 TYR TYR E . n E 1 93 PRO 93 92 92 PRO PRO E . n E 1 94 GLY 94 93 93 GLY GLY E . n E 1 95 ASN 95 94 94 ASN ASN E . n E 1 96 PHE 96 95 95 PHE PHE E . n E 1 97 ASN 97 96 96 ASN ASN E . n E 1 98 ASP 98 97 97 ASP ASP E . n E 1 99 TYR 99 98 98 TYR TYR E . n E 1 100 GLU 100 99 99 GLU GLU E . n E 1 101 GLU 101 100 100 GLU GLU E . n E 1 102 LEU 102 101 101 LEU LEU E . n E 1 103 LYS 103 102 102 LYS LYS E . n E 1 104 HIS 104 103 103 HIS HIS E . n E 1 105 LEU 105 104 104 LEU LEU E . n E 1 106 LEU 106 105 105 LEU LEU E . n E 1 107 SER 107 106 106 SER SER E . n E 1 108 ARG 108 107 107 ARG ARG E . n E 1 109 ILE 109 108 108 ILE ILE E . n E 1 110 ASN 110 109 109 ASN ASN E . n E 1 111 HIS 111 110 110 HIS HIS E . n E 1 112 PHE 112 111 111 PHE PHE E . n E 1 113 GLU 113 112 112 GLU GLU E . n E 1 114 LYS 114 113 113 LYS LYS E . n E 1 115 ILE 115 114 114 ILE ILE E . n E 1 116 GLN 116 115 115 GLN GLN E . n E 1 117 ILE 117 116 116 ILE ILE E . n E 1 118 ILE 118 117 117 ILE ILE E . n E 1 119 PRO 119 118 118 PRO PRO E . n E 1 120 LYS 120 119 119 LYS LYS E . n E 1 121 SER 121 120 120 SER SER E . n E 1 122 SER 122 121 121 SER SER E . n E 1 123 TRP 123 122 122 TRP TRP E . n E 1 124 SER 124 123 123 SER SER E . n E 1 125 ASP 125 124 124 ASP ASP E . n E 1 126 HIS 126 125 125 HIS HIS E . n E 1 127 GLU 127 126 126 GLU GLU E . n E 1 128 ALA 128 127 127 ALA ALA E . n E 1 129 SER 129 128 128 SER SER E . n E 1 130 ALA 130 129 129 ALA ALA E . n E 1 131 GLY 131 130 130 GLY GLY E . n E 1 132 VAL 132 131 131 VAL VAL E . n E 1 133 SER 133 132 132 SER SER E . n E 1 134 SER 134 133 133 SER SER E . n E 1 135 ALA 135 134 134 ALA ALA E . n E 1 136 CYS 136 135 135 CYS CYS E . n E 1 137 PRO 137 136 136 PRO PRO E . n E 1 138 TYR 138 137 137 TYR TYR E . n E 1 139 GLN 139 138 138 GLN GLN E . n E 1 140 GLY 140 139 139 GLY GLY E . n E 1 141 ARG 141 140 140 ARG ARG E . n E 1 142 SER 142 141 141 SER SER E . n E 1 143 SER 143 142 142 SER SER E . n E 1 144 PHE 144 143 143 PHE PHE E . n E 1 145 PHE 145 144 144 PHE PHE E . n E 1 146 ARG 146 145 145 ARG ARG E . n E 1 147 ASN 147 146 146 ASN ASN E . n E 1 148 VAL 148 147 147 VAL VAL E . n E 1 149 VAL 149 148 148 VAL VAL E . n E 1 150 TRP 150 149 149 TRP TRP E . n E 1 151 LEU 151 150 150 LEU LEU E . n E 1 152 ILE 152 151 151 ILE ILE E . n E 1 153 LYS 153 152 152 LYS LYS E . n E 1 154 LYS 154 153 153 LYS LYS E . n E 1 155 ASP 155 154 154 ASP ASP E . n E 1 156 ASN 156 155 155 ASN ASN E . n E 1 157 ALA 157 156 156 ALA ALA E . n E 1 158 TYR 158 157 157 TYR TYR E . n E 1 159 PRO 159 158 158 PRO PRO E . n E 1 160 THR 160 159 159 THR THR E . n E 1 161 ILE 161 160 160 ILE ILE E . n E 1 162 LYS 162 161 161 LYS LYS E . n E 1 163 ARG 163 162 162 ARG ARG E . n E 1 164 SER 164 163 163 SER SER E . n E 1 165 TYR 165 164 164 TYR TYR E . n E 1 166 ASN 166 165 165 ASN ASN E . n E 1 167 ASN 167 166 166 ASN ASN E . n E 1 168 THR 168 167 167 THR THR E . n E 1 169 ASN 169 168 168 ASN ASN E . n E 1 170 GLN 170 169 169 GLN GLN E . n E 1 171 GLU 171 170 170 GLU GLU E . n E 1 172 ASP 172 171 171 ASP ASP E . n E 1 173 LEU 173 172 172 LEU LEU E . n E 1 174 LEU 174 173 173 LEU LEU E . n E 1 175 VAL 175 174 174 VAL VAL E . n E 1 176 LEU 176 175 175 LEU LEU E . n E 1 177 TRP 177 176 176 TRP TRP E . n E 1 178 GLY 178 177 177 GLY GLY E . n E 1 179 ILE 179 178 178 ILE ILE E . n E 1 180 HIS 180 179 179 HIS HIS E . n E 1 181 HIS 181 180 180 HIS HIS E . n E 1 182 PRO 182 181 181 PRO PRO E . n E 1 183 ASN 183 182 182 ASN ASN E . n E 1 184 ASP 184 183 183 ASP ASP E . n E 1 185 ALA 185 184 184 ALA ALA E . n E 1 186 ALA 186 185 185 ALA ALA E . n E 1 187 GLU 187 186 186 GLU GLU E . n E 1 188 GLN 188 187 187 GLN GLN E . n E 1 189 THR 189 188 188 THR THR E . n E 1 190 ARG 190 189 189 ARG ARG E . n E 1 191 LEU 191 190 190 LEU LEU E . n E 1 192 TYR 192 191 191 TYR TYR E . n E 1 193 GLN 193 192 192 GLN GLN E . n E 1 194 ASN 194 193 193 ASN ASN E . n E 1 195 PRO 195 194 194 PRO PRO E . n E 1 196 THR 196 195 195 THR THR E . n E 1 197 THR 197 196 196 THR THR E . n E 1 198 TYR 198 197 197 TYR TYR E . n E 1 199 ILE 199 198 198 ILE ILE E . n E 1 200 SER 200 199 199 SER SER E . n E 1 201 VAL 201 200 200 VAL VAL E . n E 1 202 GLY 202 201 201 GLY GLY E . n E 1 203 THR 203 202 202 THR THR E . n E 1 204 SER 204 203 203 SER SER E . n E 1 205 THR 205 204 204 THR THR E . n E 1 206 LEU 206 205 205 LEU LEU E . n E 1 207 ASN 207 206 206 ASN ASN E . n E 1 208 GLN 208 207 207 GLN GLN E . n E 1 209 ARG 209 208 208 ARG ARG E . n E 1 210 LEU 210 209 209 LEU LEU E . n E 1 211 VAL 211 210 210 VAL VAL E . n E 1 212 PRO 212 211 211 PRO PRO E . n E 1 213 LYS 213 212 212 LYS LYS E . n E 1 214 ILE 214 213 213 ILE ILE E . n E 1 215 ALA 215 214 214 ALA ALA E . n E 1 216 THR 216 215 215 THR THR E . n E 1 217 ARG 217 216 216 ARG ARG E . n E 1 218 SER 218 217 217 SER SER E . n E 1 219 LYS 219 218 218 LYS LYS E . n E 1 220 VAL 220 219 219 VAL VAL E . n E 1 221 ASN 221 220 220 ASN ASN E . n E 1 222 GLY 222 221 221 GLY GLY E . n E 1 223 GLN 223 222 222 GLN GLN E . n E 1 224 SER 224 223 223 SER SER E . n E 1 225 GLY 225 224 224 GLY GLY E . n E 1 226 ARG 226 225 225 ARG ARG E . n E 1 227 MET 227 226 226 MET MET E . n E 1 228 GLU 228 227 227 GLU GLU E . n E 1 229 PHE 229 228 228 PHE PHE E . n E 1 230 PHE 230 229 229 PHE PHE E . n E 1 231 TRP 231 230 230 TRP TRP E . n E 1 232 THR 232 231 231 THR THR E . n E 1 233 ILE 233 232 232 ILE ILE E . n E 1 234 LEU 234 233 233 LEU LEU E . n E 1 235 LYS 235 234 234 LYS LYS E . n E 1 236 PRO 236 235 235 PRO PRO E . n E 1 237 ASN 237 236 236 ASN ASN E . n E 1 238 ASP 238 237 237 ASP ASP E . n E 1 239 ALA 239 238 238 ALA ALA E . n E 1 240 ILE 240 239 239 ILE ILE E . n E 1 241 ASN 241 240 240 ASN ASN E . n E 1 242 PHE 242 241 241 PHE PHE E . n E 1 243 GLU 243 242 242 GLU GLU E . n E 1 244 SER 244 243 243 SER SER E . n E 1 245 ASN 245 244 244 ASN ASN E . n E 1 246 GLY 246 245 245 GLY GLY E . n E 1 247 ASN 247 246 246 ASN ASN E . n E 1 248 PHE 248 247 247 PHE PHE E . n E 1 249 ILE 249 248 248 ILE ILE E . n E 1 250 ALA 250 249 249 ALA ALA E . n E 1 251 PRO 251 250 250 PRO PRO E . n E 1 252 GLU 252 251 251 GLU GLU E . n E 1 253 ASN 253 252 252 ASN ASN E . n E 1 254 ALA 254 253 253 ALA ALA E . n E 1 255 TYR 255 254 254 TYR TYR E . n E 1 256 LYS 256 255 255 LYS LYS E . n E 1 257 ILE 257 256 256 ILE ILE E . n E 1 258 VAL 258 257 257 VAL VAL E . n E 1 259 LYS 259 258 258 LYS LYS E . n E 1 260 LYS 260 259 259 LYS LYS E . n E 1 261 GLY 261 260 260 GLY GLY E . n E 1 262 ASP 262 261 261 ASP ASP E . n E 1 263 SER 263 262 262 SER SER E . n E 1 264 THR 264 263 263 THR THR E . n E 1 265 ILE 265 264 264 ILE ILE E . n E 1 266 MET 266 265 265 MET MET E . n E 1 267 LYS 267 266 266 LYS LYS E . n E 1 268 SER 268 267 267 SER SER E . n E 1 269 GLU 269 268 268 GLU GLU E . n E 1 270 LEU 270 269 269 LEU LEU E . n E 1 271 GLU 271 270 270 GLU GLU E . n E 1 272 TYR 272 271 271 TYR TYR E . n E 1 273 GLY 273 272 272 GLY GLY E . n E 1 274 ASN 274 273 273 ASN ASN E . n E 1 275 CYS 275 274 274 CYS CYS E . n E 1 276 ASN 276 275 275 ASN ASN E . n E 1 277 THR 277 276 276 THR THR E . n E 1 278 LYS 278 277 277 LYS LYS E . n E 1 279 CYS 279 278 278 CYS CYS E . n E 1 280 GLN 280 279 279 GLN GLN E . n E 1 281 THR 281 280 280 THR THR E . n E 1 282 PRO 282 281 281 PRO PRO E . n E 1 283 ILE 283 282 282 ILE ILE E . n E 1 284 GLY 284 283 283 GLY GLY E . n E 1 285 ALA 285 284 284 ALA ALA E . n E 1 286 ILE 286 285 285 ILE ILE E . n E 1 287 ASN 287 286 286 ASN ASN E . n E 1 288 SER 288 287 287 SER SER E . n E 1 289 SER 289 288 288 SER SER E . n E 1 290 MET 290 289 289 MET MET E . n E 1 291 PRO 291 290 290 PRO PRO E . n E 1 292 PHE 292 291 291 PHE PHE E . n E 1 293 HIS 293 292 292 HIS HIS E . n E 1 294 ASN 294 293 293 ASN ASN E . n E 1 295 ILE 295 294 294 ILE ILE E . n E 1 296 HIS 296 295 295 HIS HIS E . n E 1 297 PRO 297 296 296 PRO PRO E . n E 1 298 LEU 298 297 297 LEU LEU E . n E 1 299 THR 299 298 298 THR THR E . n E 1 300 ILE 300 299 299 ILE ILE E . n E 1 301 GLY 301 300 300 GLY GLY E . n E 1 302 GLU 302 301 301 GLU GLU E . n E 1 303 CYS 303 302 302 CYS CYS E . n E 1 304 PRO 304 303 303 PRO PRO E . n E 1 305 LYS 305 304 304 LYS LYS E . n E 1 306 TYR 306 305 305 TYR TYR E . n E 1 307 VAL 307 306 306 VAL VAL E . n E 1 308 LYS 308 307 307 LYS LYS E . n E 1 309 SER 309 308 308 SER SER E . n E 1 310 SER 310 309 309 SER SER E . n E 1 311 ARG 311 310 310 ARG ARG E . n E 1 312 LEU 312 311 311 LEU LEU E . n E 1 313 VAL 313 312 312 VAL VAL E . n E 1 314 LEU 314 313 313 LEU LEU E . n E 1 315 ALA 315 314 314 ALA ALA E . n E 1 316 THR 316 315 315 THR THR E . n E 1 317 GLY 317 316 316 GLY GLY E . n E 1 318 LEU 318 317 317 LEU LEU E . n E 1 319 ARG 319 318 318 ARG ARG E . n E 1 320 ASN 320 319 319 ASN ASN E . n E 1 321 SER 321 320 ? ? ? E . n E 1 322 PRO 322 321 ? ? ? E . n E 1 323 GLN 323 322 ? ? ? E . n E 1 324 ARG 324 323 ? ? ? E . n E 1 325 GLU 325 324 ? ? ? E . n E 1 326 THR 326 325 ? ? ? E . n E 1 327 ARG 327 326 ? ? ? E . n F 2 1 GLY 1 1 ? ? ? F . n F 2 2 LEU 2 2 ? ? ? F . n F 2 3 PHE 3 3 ? ? ? F . n F 2 4 GLY 4 4 ? ? ? F . n F 2 5 ALA 5 5 ? ? ? F . n F 2 6 ILE 6 6 ? ? ? F . n F 2 7 ALA 7 7 ? ? ? F . n F 2 8 GLY 8 8 ? ? ? F . n F 2 9 PHE 9 9 ? ? ? F . n F 2 10 ILE 10 10 10 ILE ILE F . n F 2 11 GLU 11 11 11 GLU GLU F . n F 2 12 GLY 12 12 12 GLY GLY F . n F 2 13 GLY 13 13 13 GLY GLY F . n F 2 14 TRP 14 14 14 TRP TRP F . n F 2 15 GLN 15 15 15 GLN GLN F . n F 2 16 GLY 16 16 16 GLY GLY F . n F 2 17 MET 17 17 17 MET MET F . n F 2 18 VAL 18 18 18 VAL VAL F . n F 2 19 ASP 19 19 19 ASP ASP F . n F 2 20 GLY 20 20 20 GLY GLY F . n F 2 21 TRP 21 21 21 TRP TRP F . n F 2 22 TYR 22 22 22 TYR TYR F . n F 2 23 GLY 23 23 23 GLY GLY F . n F 2 24 TYR 24 24 24 TYR TYR F . n F 2 25 HIS 25 25 25 HIS HIS F . n F 2 26 HIS 26 26 26 HIS HIS F . n F 2 27 SER 27 27 27 SER SER F . n F 2 28 ASN 28 28 28 ASN ASN F . n F 2 29 GLU 29 29 29 GLU GLU F . n F 2 30 GLN 30 30 30 GLN GLN F . n F 2 31 GLY 31 31 31 GLY GLY F . n F 2 32 SER 32 32 32 SER SER F . n F 2 33 GLY 33 33 33 GLY GLY F . n F 2 34 TYR 34 34 34 TYR TYR F . n F 2 35 ALA 35 35 35 ALA ALA F . n F 2 36 ALA 36 36 36 ALA ALA F . n F 2 37 ASP 37 37 37 ASP ASP F . n F 2 38 LYS 38 38 38 LYS LYS F . n F 2 39 GLU 39 39 39 GLU GLU F . n F 2 40 SER 40 40 40 SER SER F . n F 2 41 THR 41 41 41 THR THR F . n F 2 42 GLN 42 42 42 GLN GLN F . n F 2 43 LYS 43 43 43 LYS LYS F . n F 2 44 ALA 44 44 44 ALA ALA F . n F 2 45 ILE 45 45 45 ILE ILE F . n F 2 46 ASP 46 46 46 ASP ASP F . n F 2 47 GLY 47 47 47 GLY GLY F . n F 2 48 VAL 48 48 48 VAL VAL F . n F 2 49 THR 49 49 49 THR THR F . n F 2 50 ASN 50 50 50 ASN ASN F . n F 2 51 LYS 51 51 51 LYS LYS F . n F 2 52 VAL 52 52 52 VAL VAL F . n F 2 53 ASN 53 53 53 ASN ASN F . n F 2 54 SER 54 54 54 SER SER F . n F 2 55 ILE 55 55 55 ILE ILE F . n F 2 56 ILE 56 56 56 ILE ILE F . n F 2 57 ASP 57 57 57 ASP ASP F . n F 2 58 LYS 58 58 58 LYS LYS F . n F 2 59 MET 59 59 59 MET MET F . n F 2 60 ASN 60 60 60 ASN ASN F . n F 2 61 THR 61 61 61 THR THR F . n F 2 62 GLN 62 62 62 GLN GLN F . n F 2 63 PHE 63 63 63 PHE PHE F . n F 2 64 GLU 64 64 64 GLU GLU F . n F 2 65 ALA 65 65 65 ALA ALA F . n F 2 66 VAL 66 66 66 VAL VAL F . n F 2 67 GLY 67 67 67 GLY GLY F . n F 2 68 ARG 68 68 68 ARG ARG F . n F 2 69 GLU 69 69 69 GLU GLU F . n F 2 70 PHE 70 70 70 PHE PHE F . n F 2 71 ASN 71 71 71 ASN ASN F . n F 2 72 ASN 72 72 72 ASN ASN F . n F 2 73 LEU 73 73 73 LEU LEU F . n F 2 74 GLU 74 74 74 GLU GLU F . n F 2 75 ARG 75 75 75 ARG ARG F . n F 2 76 ARG 76 76 76 ARG ARG F . n F 2 77 ILE 77 77 77 ILE ILE F . n F 2 78 GLU 78 78 78 GLU GLU F . n F 2 79 ASN 79 79 79 ASN ASN F . n F 2 80 LEU 80 80 80 LEU LEU F . n F 2 81 ASN 81 81 81 ASN ASN F . n F 2 82 LYS 82 82 82 LYS LYS F . n F 2 83 LYS 83 83 83 LYS LYS F . n F 2 84 MET 84 84 84 MET MET F . n F 2 85 GLU 85 85 85 GLU GLU F . n F 2 86 ASP 86 86 86 ASP ASP F . n F 2 87 GLY 87 87 87 GLY GLY F . n F 2 88 PHE 88 88 88 PHE PHE F . n F 2 89 LEU 89 89 89 LEU LEU F . n F 2 90 ASP 90 90 90 ASP ASP F . n F 2 91 VAL 91 91 91 VAL VAL F . n F 2 92 TRP 92 92 92 TRP TRP F . n F 2 93 THR 93 93 93 THR THR F . n F 2 94 TYR 94 94 94 TYR TYR F . n F 2 95 ASN 95 95 95 ASN ASN F . n F 2 96 ALA 96 96 96 ALA ALA F . n F 2 97 GLU 97 97 97 GLU GLU F . n F 2 98 LEU 98 98 98 LEU LEU F . n F 2 99 LEU 99 99 99 LEU LEU F . n F 2 100 VAL 100 100 100 VAL VAL F . n F 2 101 LEU 101 101 101 LEU LEU F . n F 2 102 MET 102 102 102 MET MET F . n F 2 103 GLU 103 103 103 GLU GLU F . n F 2 104 ASN 104 104 104 ASN ASN F . n F 2 105 GLU 105 105 105 GLU GLU F . n F 2 106 ARG 106 106 106 ARG ARG F . n F 2 107 THR 107 107 107 THR THR F . n F 2 108 LEU 108 108 108 LEU LEU F . n F 2 109 ASP 109 109 109 ASP ASP F . n F 2 110 PHE 110 110 110 PHE PHE F . n F 2 111 HIS 111 111 111 HIS HIS F . n F 2 112 ASP 112 112 112 ASP ASP F . n F 2 113 SER 113 113 113 SER SER F . n F 2 114 ASN 114 114 114 ASN ASN F . n F 2 115 VAL 115 115 115 VAL VAL F . n F 2 116 LYS 116 116 116 LYS LYS F . n F 2 117 ASN 117 117 117 ASN ASN F . n F 2 118 LEU 118 118 118 LEU LEU F . n F 2 119 TYR 119 119 119 TYR TYR F . n F 2 120 ASP 120 120 120 ASP ASP F . n F 2 121 LYS 121 121 121 LYS LYS F . n F 2 122 VAL 122 122 122 VAL VAL F . n F 2 123 ARG 123 123 123 ARG ARG F . n F 2 124 LEU 124 124 124 LEU LEU F . n F 2 125 GLN 125 125 125 GLN GLN F . n F 2 126 LEU 126 126 126 LEU LEU F . n F 2 127 ARG 127 127 127 ARG ARG F . n F 2 128 ASP 128 128 128 ASP ASP F . n F 2 129 ASN 129 129 129 ASN ASN F . n F 2 130 ALA 130 130 130 ALA ALA F . n F 2 131 LYS 131 131 131 LYS LYS F . n F 2 132 GLU 132 132 132 GLU GLU F . n F 2 133 LEU 133 133 133 LEU LEU F . n F 2 134 GLY 134 134 134 GLY GLY F . n F 2 135 ASN 135 135 135 ASN ASN F . n F 2 136 GLY 136 136 136 GLY GLY F . n F 2 137 CYS 137 137 137 CYS CYS F . n F 2 138 PHE 138 138 138 PHE PHE F . n F 2 139 GLU 139 139 139 GLU GLU F . n F 2 140 PHE 140 140 140 PHE PHE F . n F 2 141 TYR 141 141 141 TYR TYR F . n F 2 142 HIS 142 142 142 HIS HIS F . n F 2 143 ARG 143 143 143 ARG ARG F . n F 2 144 CYS 144 144 144 CYS CYS F . n F 2 145 ASP 145 145 145 ASP ASP F . n F 2 146 ASN 146 146 146 ASN ASN F . n F 2 147 GLU 147 147 147 GLU GLU F . n F 2 148 CYS 148 148 148 CYS CYS F . n F 2 149 MET 149 149 149 MET MET F . n F 2 150 GLU 150 150 150 GLU GLU F . n F 2 151 SER 151 151 151 SER SER F . n F 2 152 VAL 152 152 152 VAL VAL F . n F 2 153 ARG 153 153 153 ARG ARG F . n F 2 154 ASN 154 154 154 ASN ASN F . n F 2 155 GLY 155 155 155 GLY GLY F . n F 2 156 THR 156 156 156 THR THR F . n F 2 157 TYR 157 157 157 TYR TYR F . n F 2 158 ASP 158 158 ? ? ? F . n F 2 159 TYR 159 159 ? ? ? F . n F 2 160 PRO 160 160 ? ? ? F . n F 2 161 GLN 161 161 ? ? ? F . n F 2 162 TYR 162 162 ? ? ? F . n F 2 163 SER 163 163 ? ? ? F . n F 2 164 GLU 164 164 ? ? ? F . n F 2 165 GLU 165 165 ? ? ? F . n F 2 166 ALA 166 166 ? ? ? F . 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 G 3 NAG 1 1320 1320 NAG NAG A . H 4 SIA 1 1321 1321 SIA SIA A . I 5 GAL 2 1322 1322 GAL GAL A . J 6 PO4 1 1323 1323 PO4 PO4 A . K 6 PO4 1 1324 1324 PO4 PO4 A . L 6 PO4 1 1325 1325 PO4 PO4 A . M 3 NAG 1 1320 1320 NAG NAG C . N 4 SIA 1 1321 1321 SIA SIA C . O 5 GAL 2 1322 1322 GAL GAL C . P 3 NAG 3 1323 1323 NAG NAG C . Q 6 PO4 1 1324 1324 PO4 PO4 C . R 3 NAG 1 1320 1320 NAG NAG E . S 4 SIA 1 1321 1321 SIA SIA E . T 5 GAL 2 1322 1322 GAL GAL E . U 3 NAG 3 1323 1323 NAG NAG E . V 6 PO4 1 1324 1324 PO4 PO4 E . W 7 HOH 1 2001 2001 HOH HOH A . W 7 HOH 2 2002 2002 HOH HOH A . W 7 HOH 3 2003 2003 HOH HOH A . W 7 HOH 4 2004 2004 HOH HOH A . W 7 HOH 5 2005 2005 HOH HOH A . W 7 HOH 6 2006 2006 HOH HOH A . W 7 HOH 7 2007 2007 HOH HOH A . W 7 HOH 8 2008 2008 HOH HOH A . W 7 HOH 9 2009 2009 HOH HOH A . W 7 HOH 10 2010 2010 HOH HOH A . W 7 HOH 11 2011 2011 HOH HOH A . W 7 HOH 12 2012 2012 HOH HOH A . W 7 HOH 13 2013 2013 HOH HOH A . W 7 HOH 14 2014 2014 HOH HOH A . W 7 HOH 15 2015 2015 HOH HOH A . W 7 HOH 16 2016 2016 HOH HOH A . W 7 HOH 17 2017 2017 HOH HOH A . W 7 HOH 18 2018 2018 HOH HOH A . W 7 HOH 19 2019 2019 HOH HOH A . W 7 HOH 20 2020 2020 HOH HOH A . W 7 HOH 21 2021 2021 HOH HOH A . W 7 HOH 22 2022 2022 HOH HOH A . W 7 HOH 23 2023 2023 HOH HOH A . W 7 HOH 24 2024 2024 HOH HOH A . W 7 HOH 25 2025 2025 HOH HOH A . W 7 HOH 26 2026 2026 HOH HOH A . W 7 HOH 27 2027 2027 HOH HOH A . W 7 HOH 28 2028 2028 HOH HOH A . W 7 HOH 29 2029 2029 HOH HOH A . W 7 HOH 30 2030 2030 HOH HOH A . W 7 HOH 31 2031 2031 HOH HOH A . W 7 HOH 32 2032 2032 HOH HOH A . W 7 HOH 33 2033 2033 HOH HOH A . W 7 HOH 34 2034 2034 HOH HOH A . W 7 HOH 35 2035 2035 HOH HOH A . W 7 HOH 36 2036 2036 HOH HOH A . W 7 HOH 37 2037 2037 HOH HOH A . W 7 HOH 38 2038 2038 HOH HOH A . W 7 HOH 39 2039 2039 HOH HOH A . W 7 HOH 40 2040 2040 HOH HOH A . W 7 HOH 41 2041 2041 HOH HOH A . W 7 HOH 42 2042 2042 HOH HOH A . W 7 HOH 43 2043 2043 HOH HOH A . W 7 HOH 44 2044 2044 HOH HOH A . W 7 HOH 45 2045 2045 HOH HOH A . W 7 HOH 46 2046 2046 HOH HOH A . W 7 HOH 47 2047 2047 HOH HOH A . W 7 HOH 48 2048 2048 HOH HOH A . W 7 HOH 49 2049 2049 HOH HOH A . W 7 HOH 50 2050 2050 HOH HOH A . W 7 HOH 51 2051 2051 HOH HOH A . W 7 HOH 52 2052 2052 HOH HOH A . W 7 HOH 53 2053 2053 HOH HOH A . W 7 HOH 54 2054 2054 HOH HOH A . W 7 HOH 55 2055 2055 HOH HOH A . W 7 HOH 56 2056 2056 HOH HOH A . W 7 HOH 57 2057 2057 HOH HOH A . W 7 HOH 58 2058 2058 HOH HOH A . W 7 HOH 59 2059 2059 HOH HOH A . W 7 HOH 60 2060 2060 HOH HOH A . W 7 HOH 61 2061 2061 HOH HOH A . W 7 HOH 62 2062 2062 HOH HOH A . W 7 HOH 63 2063 2063 HOH HOH A . W 7 HOH 64 2064 2064 HOH HOH A . W 7 HOH 65 2065 2065 HOH HOH A . W 7 HOH 66 2066 2066 HOH HOH A . W 7 HOH 67 2067 2067 HOH HOH A . W 7 HOH 68 2068 2068 HOH HOH A . W 7 HOH 69 2069 2069 HOH HOH A . W 7 HOH 70 2070 2070 HOH HOH A . W 7 HOH 71 2071 2071 HOH HOH A . W 7 HOH 72 2072 2072 HOH HOH A . W 7 HOH 73 2073 2073 HOH HOH A . W 7 HOH 74 2074 2074 HOH HOH A . W 7 HOH 75 2075 2075 HOH HOH A . W 7 HOH 76 2076 2076 HOH HOH A . W 7 HOH 77 2077 2077 HOH HOH A . W 7 HOH 78 2078 2078 HOH HOH A . W 7 HOH 79 2079 2079 HOH HOH A . W 7 HOH 80 2080 2080 HOH HOH A . W 7 HOH 81 2081 2081 HOH HOH A . W 7 HOH 82 2082 2082 HOH HOH A . W 7 HOH 83 2083 2083 HOH HOH A . W 7 HOH 84 2084 2084 HOH HOH A . W 7 HOH 85 2085 2085 HOH HOH A . W 7 HOH 86 2086 2086 HOH HOH A . W 7 HOH 87 2087 2087 HOH HOH A . W 7 HOH 88 2088 2088 HOH HOH A . W 7 HOH 89 2089 2089 HOH HOH A . W 7 HOH 90 2090 2090 HOH HOH A . W 7 HOH 91 2091 2091 HOH HOH A . W 7 HOH 92 2092 2092 HOH HOH A . W 7 HOH 93 2093 2093 HOH HOH A . W 7 HOH 94 2094 2094 HOH HOH A . W 7 HOH 95 2095 2095 HOH HOH A . W 7 HOH 96 2096 2096 HOH HOH A . W 7 HOH 97 2097 2097 HOH HOH A . W 7 HOH 98 2098 2098 HOH HOH A . W 7 HOH 99 2099 2099 HOH HOH A . W 7 HOH 100 2100 2100 HOH HOH A . W 7 HOH 101 2101 2101 HOH HOH A . W 7 HOH 102 2102 2102 HOH HOH A . W 7 HOH 103 2103 2103 HOH HOH A . W 7 HOH 104 2104 2104 HOH HOH A . W 7 HOH 105 2105 2105 HOH HOH A . W 7 HOH 106 2106 2106 HOH HOH A . W 7 HOH 107 2107 2107 HOH HOH A . W 7 HOH 108 2108 2108 HOH HOH A . W 7 HOH 109 2109 2109 HOH HOH A . W 7 HOH 110 2110 2110 HOH HOH A . W 7 HOH 111 2111 2111 HOH HOH A . W 7 HOH 112 2112 2112 HOH HOH A . W 7 HOH 113 2113 2113 HOH HOH A . W 7 HOH 114 2114 2114 HOH HOH A . W 7 HOH 115 2115 2115 HOH HOH A . W 7 HOH 116 2116 2116 HOH HOH A . W 7 HOH 117 2117 2117 HOH HOH A . W 7 HOH 118 2118 2118 HOH HOH A . W 7 HOH 119 2119 2119 HOH HOH A . W 7 HOH 120 2120 2120 HOH HOH A . W 7 HOH 121 2121 2121 HOH HOH A . W 7 HOH 122 2122 2122 HOH HOH A . W 7 HOH 123 2123 2123 HOH HOH A . W 7 HOH 124 2124 2124 HOH HOH A . W 7 HOH 125 2125 2125 HOH HOH A . W 7 HOH 126 2126 2126 HOH HOH A . W 7 HOH 127 2127 2127 HOH HOH A . W 7 HOH 128 2128 2128 HOH HOH A . W 7 HOH 129 2129 2129 HOH HOH A . W 7 HOH 130 2130 2130 HOH HOH A . W 7 HOH 131 2131 2131 HOH HOH A . W 7 HOH 132 2132 2132 HOH HOH A . W 7 HOH 133 2133 2133 HOH HOH A . W 7 HOH 134 2134 2134 HOH HOH A . W 7 HOH 135 2135 2135 HOH HOH A . W 7 HOH 136 2136 2136 HOH HOH A . W 7 HOH 137 2137 2137 HOH HOH A . W 7 HOH 138 2138 2138 HOH HOH A . W 7 HOH 139 2139 2139 HOH HOH A . W 7 HOH 140 2140 2140 HOH HOH A . W 7 HOH 141 2141 2141 HOH HOH A . W 7 HOH 142 2142 2142 HOH HOH A . W 7 HOH 143 2143 2143 HOH HOH A . W 7 HOH 144 2144 2144 HOH HOH A . W 7 HOH 145 2145 2145 HOH HOH A . W 7 HOH 146 2146 2146 HOH HOH A . W 7 HOH 147 2147 2147 HOH HOH A . W 7 HOH 148 2148 2148 HOH HOH A . W 7 HOH 149 2149 2149 HOH HOH A . W 7 HOH 150 2150 2150 HOH HOH A . W 7 HOH 151 2151 2151 HOH HOH A . W 7 HOH 152 2152 2152 HOH HOH A . W 7 HOH 153 2153 2153 HOH HOH A . W 7 HOH 154 2154 2154 HOH HOH A . W 7 HOH 155 2155 2155 HOH HOH A . W 7 HOH 156 2156 2156 HOH HOH A . W 7 HOH 157 2157 2157 HOH HOH A . W 7 HOH 158 2158 2158 HOH HOH A . W 7 HOH 159 2159 2159 HOH HOH A . W 7 HOH 160 2160 2160 HOH HOH A . W 7 HOH 161 2161 2161 HOH HOH A . W 7 HOH 162 2162 2162 HOH HOH A . W 7 HOH 163 2163 2163 HOH HOH A . W 7 HOH 164 2164 2164 HOH HOH A . W 7 HOH 165 2165 2165 HOH HOH A . W 7 HOH 166 2166 2166 HOH HOH A . W 7 HOH 167 2167 2167 HOH HOH A . W 7 HOH 168 2168 2168 HOH HOH A . W 7 HOH 169 2169 2169 HOH HOH A . W 7 HOH 170 2170 2170 HOH HOH A . W 7 HOH 171 2171 2171 HOH HOH A . W 7 HOH 172 2172 2172 HOH HOH A . W 7 HOH 173 2173 2173 HOH HOH A . W 7 HOH 174 2174 2174 HOH HOH A . W 7 HOH 175 2175 2175 HOH HOH A . W 7 HOH 176 2176 2176 HOH HOH A . W 7 HOH 177 2177 2177 HOH HOH A . W 7 HOH 178 2178 2178 HOH HOH A . W 7 HOH 179 2179 2179 HOH HOH A . W 7 HOH 180 2180 2180 HOH HOH A . X 7 HOH 1 2001 2001 HOH HOH B . X 7 HOH 2 2002 2002 HOH HOH B . X 7 HOH 3 2003 2003 HOH HOH B . X 7 HOH 4 2004 2004 HOH HOH B . X 7 HOH 5 2005 2005 HOH HOH B . X 7 HOH 6 2006 2006 HOH HOH B . X 7 HOH 7 2007 2007 HOH HOH B . X 7 HOH 8 2008 2008 HOH HOH B . X 7 HOH 9 2009 2009 HOH HOH B . X 7 HOH 10 2010 2010 HOH HOH B . X 7 HOH 11 2011 2011 HOH HOH B . X 7 HOH 12 2012 2012 HOH HOH B . X 7 HOH 13 2013 2013 HOH HOH B . X 7 HOH 14 2014 2014 HOH HOH B . X 7 HOH 15 2015 2015 HOH HOH B . X 7 HOH 16 2016 2016 HOH HOH B . X 7 HOH 17 2017 2017 HOH HOH B . X 7 HOH 18 2018 2018 HOH HOH B . X 7 HOH 19 2019 2019 HOH HOH B . X 7 HOH 20 2020 2020 HOH HOH B . X 7 HOH 21 2021 2021 HOH HOH B . X 7 HOH 22 2022 2022 HOH HOH B . X 7 HOH 23 2023 2023 HOH HOH B . X 7 HOH 24 2024 2024 HOH HOH B . X 7 HOH 25 2025 2025 HOH HOH B . X 7 HOH 26 2026 2026 HOH HOH B . X 7 HOH 27 2027 2027 HOH HOH B . X 7 HOH 28 2028 2028 HOH HOH B . X 7 HOH 29 2029 2029 HOH HOH B . X 7 HOH 30 2030 2030 HOH HOH B . X 7 HOH 31 2031 2031 HOH HOH B . X 7 HOH 32 2032 2032 HOH HOH B . X 7 HOH 33 2033 2033 HOH HOH B . X 7 HOH 34 2034 2034 HOH HOH B . X 7 HOH 35 2035 2035 HOH HOH B . X 7 HOH 36 2036 2036 HOH HOH B . X 7 HOH 37 2037 2037 HOH HOH B . X 7 HOH 38 2038 2038 HOH HOH B . X 7 HOH 39 2039 2039 HOH HOH B . X 7 HOH 40 2040 2040 HOH HOH B . X 7 HOH 41 2041 2041 HOH HOH B . X 7 HOH 42 2042 2042 HOH HOH B . X 7 HOH 43 2043 2043 HOH HOH B . X 7 HOH 44 2044 2044 HOH HOH B . X 7 HOH 45 2045 2045 HOH HOH B . X 7 HOH 46 2046 2046 HOH HOH B . X 7 HOH 47 2047 2047 HOH HOH B . X 7 HOH 48 2048 2048 HOH HOH B . X 7 HOH 49 2049 2049 HOH HOH B . X 7 HOH 50 2050 2050 HOH HOH B . X 7 HOH 51 2051 2051 HOH HOH B . X 7 HOH 52 2052 2052 HOH HOH B . X 7 HOH 53 2053 2053 HOH HOH B . Y 7 HOH 1 2001 2001 HOH HOH C . Y 7 HOH 2 2002 2002 HOH HOH C . Y 7 HOH 3 2003 2003 HOH HOH C . Y 7 HOH 4 2004 2004 HOH HOH C . Y 7 HOH 5 2005 2005 HOH HOH C . Y 7 HOH 6 2006 2006 HOH HOH C . Y 7 HOH 7 2007 2007 HOH HOH C . Y 7 HOH 8 2008 2008 HOH HOH C . Y 7 HOH 9 2009 2009 HOH HOH C . Y 7 HOH 10 2010 2010 HOH HOH C . Y 7 HOH 11 2011 2011 HOH HOH C . Y 7 HOH 12 2012 2012 HOH HOH C . Y 7 HOH 13 2013 2013 HOH HOH C . Y 7 HOH 14 2014 2014 HOH HOH C . Y 7 HOH 15 2015 2015 HOH HOH C . Y 7 HOH 16 2016 2016 HOH HOH C . Y 7 HOH 17 2017 2017 HOH HOH C . Y 7 HOH 18 2018 2018 HOH HOH C . Y 7 HOH 19 2019 2019 HOH HOH C . Y 7 HOH 20 2020 2020 HOH HOH C . Y 7 HOH 21 2021 2021 HOH HOH C . Y 7 HOH 22 2022 2022 HOH HOH C . Y 7 HOH 23 2023 2023 HOH HOH C . Y 7 HOH 24 2024 2024 HOH HOH C . Y 7 HOH 25 2025 2025 HOH HOH C . Y 7 HOH 26 2026 2026 HOH HOH C . Y 7 HOH 27 2027 2027 HOH HOH C . Y 7 HOH 28 2028 2028 HOH HOH C . Y 7 HOH 29 2029 2029 HOH HOH C . Y 7 HOH 30 2030 2030 HOH HOH C . Y 7 HOH 31 2031 2031 HOH HOH C . Y 7 HOH 32 2032 2032 HOH HOH C . Y 7 HOH 33 2033 2033 HOH HOH C . Y 7 HOH 34 2034 2034 HOH HOH C . Y 7 HOH 35 2035 2035 HOH HOH C . Y 7 HOH 36 2036 2036 HOH HOH C . Y 7 HOH 37 2037 2037 HOH HOH C . Y 7 HOH 38 2038 2038 HOH HOH C . Y 7 HOH 39 2039 2039 HOH HOH C . Y 7 HOH 40 2040 2040 HOH HOH C . Y 7 HOH 41 2041 2041 HOH HOH C . Y 7 HOH 42 2042 2042 HOH HOH C . Y 7 HOH 43 2043 2043 HOH HOH C . Y 7 HOH 44 2044 2044 HOH HOH C . Y 7 HOH 45 2045 2045 HOH HOH C . Y 7 HOH 46 2046 2046 HOH HOH C . Y 7 HOH 47 2047 2047 HOH HOH C . Y 7 HOH 48 2048 2048 HOH HOH C . Y 7 HOH 49 2049 2049 HOH HOH C . Y 7 HOH 50 2050 2050 HOH HOH C . Y 7 HOH 51 2051 2051 HOH HOH C . Y 7 HOH 52 2052 2052 HOH HOH C . Y 7 HOH 53 2053 2053 HOH HOH C . Y 7 HOH 54 2054 2054 HOH HOH C . Y 7 HOH 55 2055 2055 HOH HOH C . Y 7 HOH 56 2056 2056 HOH HOH C . Y 7 HOH 57 2057 2057 HOH HOH C . Y 7 HOH 58 2058 2058 HOH HOH C . Y 7 HOH 59 2059 2059 HOH HOH C . Y 7 HOH 60 2060 2060 HOH HOH C . Y 7 HOH 61 2061 2061 HOH HOH C . Y 7 HOH 62 2062 2062 HOH HOH C . Y 7 HOH 63 2063 2063 HOH HOH C . Y 7 HOH 64 2064 2064 HOH HOH C . Y 7 HOH 65 2065 2065 HOH HOH C . Y 7 HOH 66 2066 2066 HOH HOH C . Y 7 HOH 67 2067 2067 HOH HOH C . Y 7 HOH 68 2068 2068 HOH HOH C . Y 7 HOH 69 2069 2069 HOH HOH C . Y 7 HOH 70 2070 2070 HOH HOH C . Y 7 HOH 71 2071 2071 HOH HOH C . Y 7 HOH 72 2072 2072 HOH HOH C . Y 7 HOH 73 2073 2073 HOH HOH C . Y 7 HOH 74 2074 2074 HOH HOH C . Y 7 HOH 75 2075 2075 HOH HOH C . Y 7 HOH 76 2076 2076 HOH HOH C . Y 7 HOH 77 2077 2077 HOH HOH C . Y 7 HOH 78 2078 2078 HOH HOH C . Y 7 HOH 79 2079 2079 HOH HOH C . Y 7 HOH 80 2080 2080 HOH HOH C . Y 7 HOH 81 2081 2081 HOH HOH C . Y 7 HOH 82 2082 2082 HOH HOH C . Y 7 HOH 83 2083 2083 HOH HOH C . Y 7 HOH 84 2084 2084 HOH HOH C . Y 7 HOH 85 2085 2085 HOH HOH C . Y 7 HOH 86 2086 2086 HOH HOH C . Y 7 HOH 87 2087 2087 HOH HOH C . Y 7 HOH 88 2088 2088 HOH HOH C . Y 7 HOH 89 2089 2089 HOH HOH C . Y 7 HOH 90 2090 2090 HOH HOH C . Y 7 HOH 91 2091 2091 HOH HOH C . Y 7 HOH 92 2092 2092 HOH HOH C . Y 7 HOH 93 2093 2093 HOH HOH C . Y 7 HOH 94 2094 2094 HOH HOH C . Y 7 HOH 95 2095 2095 HOH HOH C . Y 7 HOH 96 2096 2096 HOH HOH C . Y 7 HOH 97 2097 2097 HOH HOH C . Y 7 HOH 98 2098 2098 HOH HOH C . Y 7 HOH 99 2099 2099 HOH HOH C . Y 7 HOH 100 2100 2100 HOH HOH C . Y 7 HOH 101 2101 2101 HOH HOH C . Y 7 HOH 102 2102 2102 HOH HOH C . Y 7 HOH 103 2103 2103 HOH HOH C . Y 7 HOH 104 2104 2104 HOH HOH C . Y 7 HOH 105 2105 2105 HOH HOH C . Y 7 HOH 106 2106 2106 HOH HOH C . Y 7 HOH 107 2107 2107 HOH HOH C . Y 7 HOH 108 2108 2108 HOH HOH C . Y 7 HOH 109 2109 2109 HOH HOH C . Y 7 HOH 110 2110 2110 HOH HOH C . Y 7 HOH 111 2111 2111 HOH HOH C . Y 7 HOH 112 2112 2112 HOH HOH C . Y 7 HOH 113 2113 2113 HOH HOH C . Y 7 HOH 114 2114 2114 HOH HOH C . Y 7 HOH 115 2115 2115 HOH HOH C . Y 7 HOH 116 2116 2116 HOH HOH C . Y 7 HOH 117 2117 2117 HOH HOH C . Y 7 HOH 118 2118 2118 HOH HOH C . Y 7 HOH 119 2119 2119 HOH HOH C . Y 7 HOH 120 2120 2120 HOH HOH C . Y 7 HOH 121 2121 2121 HOH HOH C . Y 7 HOH 122 2122 2122 HOH HOH C . Y 7 HOH 123 2123 2123 HOH HOH C . Y 7 HOH 124 2124 2124 HOH HOH C . Y 7 HOH 125 2125 2125 HOH HOH C . Y 7 HOH 126 2126 2126 HOH HOH C . Y 7 HOH 127 2127 2127 HOH HOH C . Y 7 HOH 128 2128 2128 HOH HOH C . Y 7 HOH 129 2129 2129 HOH HOH C . Y 7 HOH 130 2130 2130 HOH HOH C . Y 7 HOH 131 2131 2131 HOH HOH C . Y 7 HOH 132 2132 2132 HOH HOH C . Y 7 HOH 133 2133 2133 HOH HOH C . Y 7 HOH 134 2134 2134 HOH HOH C . Y 7 HOH 135 2135 2135 HOH HOH C . Y 7 HOH 136 2136 2136 HOH HOH C . Y 7 HOH 137 2137 2137 HOH HOH C . Y 7 HOH 138 2138 2138 HOH HOH C . Y 7 HOH 139 2139 2139 HOH HOH C . Y 7 HOH 140 2140 2140 HOH HOH C . Y 7 HOH 141 2141 2141 HOH HOH C . Y 7 HOH 142 2142 2142 HOH HOH C . Y 7 HOH 143 2143 2143 HOH HOH C . Y 7 HOH 144 2144 2144 HOH HOH C . Y 7 HOH 145 2145 2145 HOH HOH C . Y 7 HOH 146 2146 2146 HOH HOH C . Y 7 HOH 147 2147 2147 HOH HOH C . Y 7 HOH 148 2148 2148 HOH HOH C . Y 7 HOH 149 2149 2149 HOH HOH C . Y 7 HOH 150 2150 2150 HOH HOH C . Y 7 HOH 151 2151 2151 HOH HOH C . Y 7 HOH 152 2152 2152 HOH HOH C . Y 7 HOH 153 2153 2153 HOH HOH C . Y 7 HOH 154 2154 2154 HOH HOH C . Y 7 HOH 155 2155 2155 HOH HOH C . Y 7 HOH 156 2156 2156 HOH HOH C . Y 7 HOH 157 2157 2157 HOH HOH C . Y 7 HOH 158 2158 2158 HOH HOH C . Y 7 HOH 159 2159 2159 HOH HOH C . Y 7 HOH 160 2160 2160 HOH HOH C . Y 7 HOH 161 2161 2161 HOH HOH C . Y 7 HOH 162 2162 2162 HOH HOH C . Y 7 HOH 163 2163 2163 HOH HOH C . Y 7 HOH 164 2164 2164 HOH HOH C . Y 7 HOH 165 2165 2165 HOH HOH C . Y 7 HOH 166 2166 2166 HOH HOH C . Y 7 HOH 167 2167 2167 HOH HOH C . Y 7 HOH 168 2168 2168 HOH HOH C . Y 7 HOH 169 2169 2169 HOH HOH C . Y 7 HOH 170 2170 2170 HOH HOH C . Y 7 HOH 171 2171 2171 HOH HOH C . Y 7 HOH 172 2172 2172 HOH HOH C . Y 7 HOH 173 2173 2173 HOH HOH C . Y 7 HOH 174 2174 2174 HOH HOH C . Y 7 HOH 175 2175 2175 HOH HOH C . Y 7 HOH 176 2176 2176 HOH HOH C . Y 7 HOH 177 2177 2177 HOH HOH C . Y 7 HOH 178 2178 2178 HOH HOH C . Y 7 HOH 179 2179 2179 HOH HOH C . Y 7 HOH 180 2180 2180 HOH HOH C . Y 7 HOH 181 2181 2181 HOH HOH C . Y 7 HOH 182 2182 2182 HOH HOH C . Y 7 HOH 183 2183 2183 HOH HOH C . Y 7 HOH 184 2184 2184 HOH HOH C . Y 7 HOH 185 2185 2185 HOH HOH C . Y 7 HOH 186 2186 2186 HOH HOH C . Y 7 HOH 187 2187 2187 HOH HOH C . Y 7 HOH 188 2188 2188 HOH HOH C . Y 7 HOH 189 2189 2189 HOH HOH C . Y 7 HOH 190 2190 2190 HOH HOH C . Y 7 HOH 191 2191 2191 HOH HOH C . Y 7 HOH 192 2192 2192 HOH HOH C . Y 7 HOH 193 2193 2193 HOH HOH C . Y 7 HOH 194 2194 2194 HOH HOH C . Y 7 HOH 195 2195 2195 HOH HOH C . Y 7 HOH 196 2196 2196 HOH HOH C . Y 7 HOH 197 2197 2197 HOH HOH C . Y 7 HOH 198 2198 2198 HOH HOH C . Y 7 HOH 199 2199 2199 HOH HOH C . Y 7 HOH 200 2200 2200 HOH HOH C . Y 7 HOH 201 2201 2201 HOH HOH C . Y 7 HOH 202 2202 2202 HOH HOH C . Y 7 HOH 203 2203 2203 HOH HOH C . Y 7 HOH 204 2204 2204 HOH HOH C . Y 7 HOH 205 2205 2205 HOH HOH C . Y 7 HOH 206 2206 2206 HOH HOH C . Y 7 HOH 207 2207 2207 HOH HOH C . Y 7 HOH 208 2208 2208 HOH HOH C . Z 7 HOH 1 2001 2001 HOH HOH D . Z 7 HOH 2 2002 2002 HOH HOH D . Z 7 HOH 3 2003 2003 HOH HOH D . Z 7 HOH 4 2004 2004 HOH HOH D . Z 7 HOH 5 2005 2005 HOH HOH D . Z 7 HOH 6 2006 2006 HOH HOH D . Z 7 HOH 7 2007 2007 HOH HOH D . Z 7 HOH 8 2008 2008 HOH HOH D . Z 7 HOH 9 2009 2009 HOH HOH D . Z 7 HOH 10 2010 2010 HOH HOH D . Z 7 HOH 11 2011 2011 HOH HOH D . Z 7 HOH 12 2012 2012 HOH HOH D . Z 7 HOH 13 2013 2013 HOH HOH D . Z 7 HOH 14 2014 2014 HOH HOH D . Z 7 HOH 15 2015 2015 HOH HOH D . Z 7 HOH 16 2016 2016 HOH HOH D . Z 7 HOH 17 2017 2017 HOH HOH D . Z 7 HOH 18 2018 2018 HOH HOH D . Z 7 HOH 19 2019 2019 HOH HOH D . Z 7 HOH 20 2020 2020 HOH HOH D . Z 7 HOH 21 2021 2021 HOH HOH D . Z 7 HOH 22 2022 2022 HOH HOH D . Z 7 HOH 23 2023 2023 HOH HOH D . Z 7 HOH 24 2024 2024 HOH HOH D . Z 7 HOH 25 2025 2025 HOH HOH D . Z 7 HOH 26 2026 2026 HOH HOH D . Z 7 HOH 27 2027 2027 HOH HOH D . Z 7 HOH 28 2028 2028 HOH HOH D . Z 7 HOH 29 2029 2029 HOH HOH D . Z 7 HOH 30 2030 2030 HOH HOH D . Z 7 HOH 31 2031 2031 HOH HOH D . Z 7 HOH 32 2032 2032 HOH HOH D . Z 7 HOH 33 2033 2033 HOH HOH D . Z 7 HOH 34 2034 2034 HOH HOH D . Z 7 HOH 35 2035 2035 HOH HOH D . Z 7 HOH 36 2036 2036 HOH HOH D . Z 7 HOH 37 2037 2037 HOH HOH D . Z 7 HOH 38 2038 2038 HOH HOH D . Z 7 HOH 39 2039 2039 HOH HOH D . Z 7 HOH 40 2040 2040 HOH HOH D . Z 7 HOH 41 2041 2041 HOH HOH D . Z 7 HOH 42 2042 2042 HOH HOH D . Z 7 HOH 43 2043 2043 HOH HOH D . Z 7 HOH 44 2044 2044 HOH HOH D . AA 7 HOH 1 2001 2001 HOH HOH E . AA 7 HOH 2 2002 2002 HOH HOH E . AA 7 HOH 3 2003 2003 HOH HOH E . AA 7 HOH 4 2004 2004 HOH HOH E . AA 7 HOH 5 2005 2005 HOH HOH E . AA 7 HOH 6 2006 2006 HOH HOH E . AA 7 HOH 7 2007 2007 HOH HOH E . AA 7 HOH 8 2008 2008 HOH HOH E . AA 7 HOH 9 2009 2009 HOH HOH E . AA 7 HOH 10 2010 2010 HOH HOH E . AA 7 HOH 11 2011 2011 HOH HOH E . AA 7 HOH 12 2012 2012 HOH HOH E . AA 7 HOH 13 2013 2013 HOH HOH E . AA 7 HOH 14 2014 2014 HOH HOH E . AA 7 HOH 15 2015 2015 HOH HOH E . AA 7 HOH 16 2016 2016 HOH HOH E . AA 7 HOH 17 2017 2017 HOH HOH E . AA 7 HOH 18 2018 2018 HOH HOH E . AA 7 HOH 19 2019 2019 HOH HOH E . AA 7 HOH 20 2020 2020 HOH HOH E . AA 7 HOH 21 2021 2021 HOH HOH E . AA 7 HOH 22 2022 2022 HOH HOH E . AA 7 HOH 23 2023 2023 HOH HOH E . AA 7 HOH 24 2024 2024 HOH HOH E . AA 7 HOH 25 2025 2025 HOH HOH E . AA 7 HOH 26 2026 2026 HOH HOH E . AA 7 HOH 27 2027 2027 HOH HOH E . AA 7 HOH 28 2028 2028 HOH HOH E . AA 7 HOH 29 2029 2029 HOH HOH E . AA 7 HOH 30 2030 2030 HOH HOH E . AA 7 HOH 31 2031 2031 HOH HOH E . AA 7 HOH 32 2032 2032 HOH HOH E . AA 7 HOH 33 2033 2033 HOH HOH E . AA 7 HOH 34 2034 2034 HOH HOH E . AA 7 HOH 35 2035 2035 HOH HOH E . AA 7 HOH 36 2036 2036 HOH HOH E . AA 7 HOH 37 2037 2037 HOH HOH E . AA 7 HOH 38 2038 2038 HOH HOH E . AA 7 HOH 39 2039 2039 HOH HOH E . AA 7 HOH 40 2040 2040 HOH HOH E . AA 7 HOH 41 2041 2041 HOH HOH E . AA 7 HOH 42 2042 2042 HOH HOH E . AA 7 HOH 43 2043 2043 HOH HOH E . AA 7 HOH 44 2044 2044 HOH HOH E . AA 7 HOH 45 2045 2045 HOH HOH E . AA 7 HOH 46 2046 2046 HOH HOH E . AA 7 HOH 47 2047 2047 HOH HOH E . AA 7 HOH 48 2048 2048 HOH HOH E . AA 7 HOH 49 2049 2049 HOH HOH E . AA 7 HOH 50 2050 2050 HOH HOH E . AA 7 HOH 51 2051 2051 HOH HOH E . AA 7 HOH 52 2052 2052 HOH HOH E . AA 7 HOH 53 2053 2053 HOH HOH E . AA 7 HOH 54 2054 2054 HOH HOH E . AA 7 HOH 55 2055 2055 HOH HOH E . AA 7 HOH 56 2056 2056 HOH HOH E . AA 7 HOH 57 2057 2057 HOH HOH E . AA 7 HOH 58 2058 2058 HOH HOH E . AA 7 HOH 59 2059 2059 HOH HOH E . AA 7 HOH 60 2060 2060 HOH HOH E . AA 7 HOH 61 2061 2061 HOH HOH E . AA 7 HOH 62 2062 2062 HOH HOH E . AA 7 HOH 63 2063 2063 HOH HOH E . AA 7 HOH 64 2064 2064 HOH HOH E . AA 7 HOH 65 2065 2065 HOH HOH E . AA 7 HOH 66 2066 2066 HOH HOH E . AA 7 HOH 67 2067 2067 HOH HOH E . AA 7 HOH 68 2068 2068 HOH HOH E . AA 7 HOH 69 2069 2069 HOH HOH E . AA 7 HOH 70 2070 2070 HOH HOH E . AA 7 HOH 71 2071 2071 HOH HOH E . AA 7 HOH 72 2072 2072 HOH HOH E . AA 7 HOH 73 2073 2073 HOH HOH E . AA 7 HOH 74 2074 2074 HOH HOH E . AA 7 HOH 75 2075 2075 HOH HOH E . AA 7 HOH 76 2076 2076 HOH HOH E . AA 7 HOH 77 2077 2077 HOH HOH E . AA 7 HOH 78 2078 2078 HOH HOH E . AA 7 HOH 79 2079 2079 HOH HOH E . AA 7 HOH 80 2080 2080 HOH HOH E . AA 7 HOH 81 2081 2081 HOH HOH E . AA 7 HOH 82 2082 2082 HOH HOH E . AA 7 HOH 83 2083 2083 HOH HOH E . AA 7 HOH 84 2084 2084 HOH HOH E . AA 7 HOH 85 2085 2085 HOH HOH E . AA 7 HOH 86 2086 2086 HOH HOH E . AA 7 HOH 87 2087 2087 HOH HOH E . AA 7 HOH 88 2088 2088 HOH HOH E . AA 7 HOH 89 2089 2089 HOH HOH E . AA 7 HOH 90 2090 2090 HOH HOH E . AA 7 HOH 91 2091 2091 HOH HOH E . AA 7 HOH 92 2092 2092 HOH HOH E . AA 7 HOH 93 2093 2093 HOH HOH E . AA 7 HOH 94 2094 2094 HOH HOH E . AA 7 HOH 95 2095 2095 HOH HOH E . AA 7 HOH 96 2096 2096 HOH HOH E . AA 7 HOH 97 2097 2097 HOH HOH E . AA 7 HOH 98 2098 2098 HOH HOH E . AA 7 HOH 99 2099 2099 HOH HOH E . AA 7 HOH 100 2100 2100 HOH HOH E . AA 7 HOH 101 2101 2101 HOH HOH E . AA 7 HOH 102 2102 2102 HOH HOH E . AA 7 HOH 103 2103 2103 HOH HOH E . AA 7 HOH 104 2104 2104 HOH HOH E . AA 7 HOH 105 2105 2105 HOH HOH E . AA 7 HOH 106 2106 2106 HOH HOH E . AA 7 HOH 107 2107 2107 HOH HOH E . AA 7 HOH 108 2108 2108 HOH HOH E . AA 7 HOH 109 2109 2109 HOH HOH E . AA 7 HOH 110 2110 2110 HOH HOH E . AA 7 HOH 111 2111 2111 HOH HOH E . AA 7 HOH 112 2112 2112 HOH HOH E . AA 7 HOH 113 2113 2113 HOH HOH E . AA 7 HOH 114 2114 2114 HOH HOH E . AA 7 HOH 115 2115 2115 HOH HOH E . AA 7 HOH 116 2116 2116 HOH HOH E . AA 7 HOH 117 2117 2117 HOH HOH E . AA 7 HOH 118 2118 2118 HOH HOH E . AA 7 HOH 119 2119 2119 HOH HOH E . AA 7 HOH 120 2120 2120 HOH HOH E . AA 7 HOH 121 2121 2121 HOH HOH E . AA 7 HOH 122 2122 2122 HOH HOH E . AA 7 HOH 123 2123 2123 HOH HOH E . AA 7 HOH 124 2124 2124 HOH HOH E . AA 7 HOH 125 2125 2125 HOH HOH E . AA 7 HOH 126 2126 2126 HOH HOH E . AA 7 HOH 127 2127 2127 HOH HOH E . AA 7 HOH 128 2128 2128 HOH HOH E . AA 7 HOH 129 2129 2129 HOH HOH E . AA 7 HOH 130 2130 2130 HOH HOH E . AA 7 HOH 131 2131 2131 HOH HOH E . AA 7 HOH 132 2132 2132 HOH HOH E . AA 7 HOH 133 2133 2133 HOH HOH E . AA 7 HOH 134 2134 2134 HOH HOH E . AA 7 HOH 135 2135 2135 HOH HOH E . AA 7 HOH 136 2136 2136 HOH HOH E . AA 7 HOH 137 2137 2137 HOH HOH E . AA 7 HOH 138 2138 2138 HOH HOH E . AA 7 HOH 139 2139 2139 HOH HOH E . AA 7 HOH 140 2140 2140 HOH HOH E . AA 7 HOH 141 2141 2141 HOH HOH E . AA 7 HOH 142 2142 2142 HOH HOH E . AA 7 HOH 143 2143 2143 HOH HOH E . AA 7 HOH 144 2144 2144 HOH HOH E . AA 7 HOH 145 2145 2145 HOH HOH E . AA 7 HOH 146 2146 2146 HOH HOH E . AA 7 HOH 147 2147 2147 HOH HOH E . AA 7 HOH 148 2148 2148 HOH HOH E . AA 7 HOH 149 2149 2149 HOH HOH E . AA 7 HOH 150 2150 2150 HOH HOH E . AA 7 HOH 151 2151 2151 HOH HOH E . AA 7 HOH 152 2152 2152 HOH HOH E . AA 7 HOH 153 2153 2153 HOH HOH E . AA 7 HOH 154 2154 2154 HOH HOH E . AA 7 HOH 155 2155 2155 HOH HOH E . AA 7 HOH 156 2156 2156 HOH HOH E . AA 7 HOH 157 2157 2157 HOH HOH E . AA 7 HOH 158 2158 2158 HOH HOH E . AA 7 HOH 159 2159 2159 HOH HOH E . AA 7 HOH 160 2160 2160 HOH HOH E . AA 7 HOH 161 2161 2161 HOH HOH E . AA 7 HOH 162 2162 2162 HOH HOH E . AA 7 HOH 163 2163 2163 HOH HOH E . AA 7 HOH 164 2164 2164 HOH HOH E . AA 7 HOH 165 2165 2165 HOH HOH E . AA 7 HOH 166 2166 2166 HOH HOH E . AA 7 HOH 167 2167 2167 HOH HOH E . AA 7 HOH 168 2168 2168 HOH HOH E . AA 7 HOH 169 2169 2169 HOH HOH E . AA 7 HOH 170 2170 2170 HOH HOH E . AA 7 HOH 171 2171 2171 HOH HOH E . AA 7 HOH 172 2172 2172 HOH HOH E . AA 7 HOH 173 2173 2173 HOH HOH E . AA 7 HOH 174 2174 2174 HOH HOH E . AA 7 HOH 175 2175 2175 HOH HOH E . AA 7 HOH 176 2176 2176 HOH HOH E . BA 7 HOH 1 2001 2001 HOH HOH F . BA 7 HOH 2 2002 2002 HOH HOH F . BA 7 HOH 3 2003 2003 HOH HOH F . BA 7 HOH 4 2004 2004 HOH HOH F . BA 7 HOH 5 2005 2005 HOH HOH F . BA 7 HOH 6 2006 2006 HOH HOH F . BA 7 HOH 7 2007 2007 HOH HOH F . BA 7 HOH 8 2008 2008 HOH HOH F . BA 7 HOH 9 2009 2009 HOH HOH F . BA 7 HOH 10 2010 2010 HOH HOH F . BA 7 HOH 11 2011 2011 HOH HOH F . BA 7 HOH 12 2012 2012 HOH HOH F . BA 7 HOH 13 2013 2013 HOH HOH F . BA 7 HOH 14 2014 2014 HOH HOH F . BA 7 HOH 15 2015 2015 HOH HOH F . BA 7 HOH 16 2016 2016 HOH HOH F . BA 7 HOH 17 2017 2017 HOH HOH F . BA 7 HOH 18 2018 2018 HOH HOH F . BA 7 HOH 19 2019 2019 HOH HOH F . BA 7 HOH 20 2020 2020 HOH HOH F . BA 7 HOH 21 2021 2021 HOH HOH F . BA 7 HOH 22 2022 2022 HOH HOH F . BA 7 HOH 23 2023 2023 HOH HOH F . BA 7 HOH 24 2024 2024 HOH HOH F . BA 7 HOH 25 2025 2025 HOH HOH F . BA 7 HOH 26 2026 2026 HOH HOH F . BA 7 HOH 27 2027 2027 HOH HOH F . BA 7 HOH 28 2028 2028 HOH HOH F . BA 7 HOH 29 2029 2029 HOH HOH F . BA 7 HOH 30 2030 2030 HOH HOH F . BA 7 HOH 31 2031 2031 HOH HOH F . BA 7 HOH 32 2032 2032 HOH HOH F . BA 7 HOH 33 2033 2033 HOH HOH F . BA 7 HOH 34 2034 2034 HOH HOH F . BA 7 HOH 35 2035 2035 HOH HOH F . BA 7 HOH 36 2036 2036 HOH HOH F . BA 7 HOH 37 2037 2037 HOH HOH F . BA 7 HOH 38 2038 2038 HOH HOH F . BA 7 HOH 39 2039 2039 HOH HOH F . BA 7 HOH 40 2040 2040 HOH HOH F . BA 7 HOH 41 2041 2041 HOH HOH F . BA 7 HOH 42 2042 2042 HOH HOH F . BA 7 HOH 43 2043 2043 HOH HOH F . BA 7 HOH 44 2044 2044 HOH HOH F . BA 7 HOH 45 2045 2045 HOH HOH F . BA 7 HOH 46 2046 2046 HOH HOH F . BA 7 HOH 47 2047 2047 HOH HOH F . BA 7 HOH 48 2048 2048 HOH HOH F . BA 7 HOH 49 2049 2049 HOH HOH F . BA 7 HOH 50 2050 2050 HOH HOH F . BA 7 HOH 51 2051 2051 HOH HOH F . # 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 165 ? ASN 'GLYCOSYLATION SITE' 2 C ASN 166 C ASN 165 ? ASN 'GLYCOSYLATION SITE' 3 E ASN 166 E ASN 165 ? 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 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA # 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)' 29680 ? 1 MORE -132.8 ? 1 'SSA (A^2)' 58080 ? # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2013-04-24 2 'Structure model' 1 1 2013-05-08 3 'Structure model' 1 2 2013-05-15 4 'Structure model' 1 3 2013-05-22 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Database references' 2 3 'Structure model' 'Database references' 3 4 'Structure model' 'Database references' # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] 'X-RAY DIFFRACTION' 1 ? refined 11.9885 -33.5965 -7.6191 1.2464 1.1035 0.8685 -0.3126 -0.1256 -0.5988 0.4316 16.6519 1.0936 2.6451 0.6025 3.7048 -0.2745 -0.1142 0.3033 -1.8105 -0.3254 2.0188 0.1030 -0.3725 0.5999 'X-RAY DIFFRACTION' 2 ? refined 20.4053 19.3256 22.7420 0.1022 0.1484 0.1181 0.0326 -0.0079 0.0604 1.9367 2.2204 2.3867 0.8673 0.6243 1.1535 -0.0559 0.3712 0.2969 -0.1723 0.0155 0.1148 -0.4706 -0.0196 0.0404 'X-RAY DIFFRACTION' 3 ? refined 12.2119 -5.7170 7.9396 0.1911 0.3228 0.1998 -0.0447 -0.1084 -0.0365 1.7183 3.8936 4.3200 -1.6371 -1.1819 3.9503 0.1247 0.1807 -0.2877 0.4255 -0.1770 0.2342 0.6428 -0.2206 0.0523 'X-RAY DIFFRACTION' 4 ? refined 16.0659 -29.0057 -2.3268 0.6166 0.5299 0.7425 0.0525 -0.2200 -0.3271 1.5312 17.9208 5.1600 4.7281 1.4530 7.3888 -0.1896 0.4596 -0.3897 -0.5608 0.6475 -0.4362 0.3373 -0.0805 -0.4579 'X-RAY DIFFRACTION' 5 ? refined -0.3249 -48.5558 -13.9871 1.6791 1.8981 1.6184 -0.3902 -0.5641 -0.5933 1.2219 0.0195 1.0203 -0.1528 1.1020 -0.1368 0.2620 -0.3977 -0.5052 -0.0486 0.0459 0.0560 0.1255 -0.5093 -0.3079 'X-RAY DIFFRACTION' 6 ? refined 4.6574 -34.6112 5.0523 1.0985 1.2632 0.9138 0.0002 0.0446 -0.1816 19.5342 22.2236 3.7945 19.4008 8.2616 8.6830 0.0180 0.6091 0.4886 -0.7721 -0.3369 1.4397 -0.4316 -0.0871 0.3189 'X-RAY DIFFRACTION' 7 ? refined 27.6740 -6.5087 17.9941 0.0786 0.1285 0.0781 0.0268 -0.0162 -0.0100 11.3863 5.7574 7.3119 3.9898 4.8709 3.5003 0.1507 0.1624 0.2217 -0.4451 -0.2579 0.4077 -0.0178 -0.6901 0.1072 'X-RAY DIFFRACTION' 8 ? refined 8.7923 -45.7558 -1.6071 1.0160 0.8322 1.0383 -0.3311 -0.0804 -0.3298 5.3034 11.7319 6.0569 7.2473 5.0405 7.2436 0.1287 0.2628 -0.6229 0.0760 0.1735 0.4490 1.1922 -0.2856 -0.3022 'X-RAY DIFFRACTION' 9 ? refined 48.7302 -21.8283 16.4168 0.2886 0.1745 0.2831 0.0977 0.0220 -0.0508 1.9247 3.5136 1.6752 1.3190 -0.0394 1.4395 -0.0772 0.1168 -0.6881 0.1662 0.0750 -0.4527 0.6006 0.1831 0.0022 'X-RAY DIFFRACTION' 10 ? refined 54.2909 12.8387 26.4091 0.0864 0.2369 0.0937 -0.0242 0.0126 -0.0656 1.3733 2.0199 2.8655 -0.3672 0.8619 -0.2837 -0.1548 -0.3258 0.1767 -0.1230 0.1386 -0.1379 -0.4441 0.1317 0.0162 'X-RAY DIFFRACTION' 11 ? refined 49.3876 -20.5368 13.8434 0.1641 0.3535 0.4036 0.0073 0.1089 -0.1747 0.6814 7.7788 2.0588 2.1413 -0.1727 -1.0754 -0.0860 0.2019 -0.2106 -0.1251 0.1994 -0.1416 0.4272 0.3358 -0.1134 'X-RAY DIFFRACTION' 12 ? refined 37.2914 -37.8030 11.6348 0.8077 0.3101 0.5482 -0.1102 0.1088 -0.1832 3.2909 14.9744 0.9844 5.1025 1.1740 3.7353 -0.7487 0.5724 -0.5894 -0.7531 0.8027 -0.1148 0.0056 0.1853 -0.0540 'X-RAY DIFFRACTION' 13 ? refined 34.0327 -63.4728 -5.9901 1.4676 1.9636 2.1672 -0.4817 0.7833 -0.5439 8.9854 1.7852 5.3694 -3.9697 -6.6378 2.8701 -0.6188 0.9399 0.1054 0.6220 -0.1773 0.0613 0.7891 -0.0081 0.7961 'X-RAY DIFFRACTION' 14 ? refined 32.1228 -42.2856 -2.4613 1.2301 1.2408 0.9706 -0.0864 0.1026 -0.2693 2.0529 0.1581 0.7687 -0.2309 0.3088 -0.3424 -0.5747 0.2323 -0.6324 -0.0716 0.3584 -0.0667 0.2942 -0.7626 0.2162 'X-RAY DIFFRACTION' 15 ? refined 30.0328 -31.5049 14.2410 0.4930 0.2585 0.3771 -0.0300 0.0347 -0.2164 1.5858 13.9653 4.6985 2.4284 0.9505 7.1425 -0.1333 0.5548 -0.6179 -0.2756 0.3302 -0.4232 0.5276 0.0586 -0.1968 'X-RAY DIFFRACTION' 16 ? refined 23.8341 -68.5565 -13.3225 2.1957 1.6742 1.6684 -0.6319 0.4505 -0.9853 0.2233 0.6599 0.4749 0.3718 0.2951 0.5481 -0.1793 0.1743 -0.1364 -0.2076 0.1022 -0.0244 -0.0447 -0.1080 0.0771 'X-RAY DIFFRACTION' 17 ? refined 15.7201 -28.9269 38.7412 0.6994 0.2421 0.3773 -0.2656 0.1559 -0.0768 0.9365 6.3193 2.2105 1.8564 1.1710 3.5745 0.0865 0.0140 -0.1232 0.3458 -0.3457 0.6039 0.4917 -0.3098 0.2592 'X-RAY DIFFRACTION' 18 ? refined 32.0240 -3.8084 50.7226 0.4464 0.1034 0.0339 0.0739 0.0828 0.0141 2.6291 3.9997 0.3740 0.3914 0.4366 0.5508 -0.1596 -0.2344 -0.2013 0.3190 0.1511 -0.1238 0.3307 0.0206 0.0085 'X-RAY DIFFRACTION' 19 ? refined 34.2528 6.0500 52.4562 0.0260 0.1057 0.0115 0.0115 -0.0095 -0.0230 2.3717 1.2042 2.2954 -0.4498 -0.4780 0.5085 -0.0808 -0.2195 0.0592 0.1493 0.1121 -0.0715 0.0938 0.3547 -0.0313 'X-RAY DIFFRACTION' 20 ? refined 16.0288 -30.5776 35.4413 0.4996 0.1978 0.5093 -0.1560 0.2093 -0.1392 1.9561 6.0372 5.5409 2.7065 2.9664 3.9284 0.1092 0.0939 -0.4365 0.2951 0.0785 -0.0574 0.6577 -0.1443 -0.1878 'X-RAY DIFFRACTION' 21 ? refined 12.8025 -60.2465 21.0152 1.1381 0.5749 1.4075 -0.0056 -0.0154 -0.3271 5.1953 6.3960 0.9925 5.4841 1.1729 1.0635 0.1446 0.4814 -0.1208 0.6119 0.3090 -0.6682 0.2364 0.6423 -0.4535 'X-RAY DIFFRACTION' 22 ? refined 24.3600 -13.2184 28.3837 0.0763 0.1582 0.1374 -0.0120 0.0137 0.0058 2.6231 17.7172 4.6356 2.5740 -0.0268 0.3459 0.1219 -0.0187 -0.5043 0.4032 -0.3313 0.1677 0.5470 -0.1983 0.2094 'X-RAY DIFFRACTION' 23 ? refined 15.4069 -48.5860 13.4543 0.8887 0.2736 0.8772 -0.1645 0.1651 -0.1769 1.1189 18.4897 1.1603 4.4687 1.0499 4.2016 -0.0958 0.1209 -0.3163 -0.3592 0.3191 -0.5685 0.3003 0.0803 -0.2232 'X-RAY DIFFRACTION' 24 ? refined 11.8856 -77.7682 12.9390 0.6947 0.2428 0.7211 0.0027 0.0659 -0.1491 2.2834 18.0357 12.4922 3.0100 -3.6916 1.5674 0.1980 -0.2896 0.2337 -0.4003 0.2563 -1.0486 0.2624 0.5707 -0.4543 # 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 39 ? ? ? ? 'X-RAY DIFFRACTION' 2 2 A 40 ? ? A 255 ? ? ? ? 'X-RAY DIFFRACTION' 3 3 A 256 ? ? A 305 ? ? ? ? 'X-RAY DIFFRACTION' 4 4 A 306 ? ? A 321 ? ? ? ? 'X-RAY DIFFRACTION' 5 5 B 1 ? ? B 37 ? ? ? ? 'X-RAY DIFFRACTION' 6 6 B 38 ? ? B 59 ? ? ? ? 'X-RAY DIFFRACTION' 7 7 B 60 ? ? B 82 ? ? ? ? 'X-RAY DIFFRACTION' 8 8 B 83 ? ? B 162 ? ? ? ? 'X-RAY DIFFRACTION' 9 9 C -1 ? ? C 104 ? ? ? ? 'X-RAY DIFFRACTION' 10 10 C 105 ? ? C 257 ? ? ? ? 'X-RAY DIFFRACTION' 11 11 C 258 ? ? C 300 ? ? ? ? 'X-RAY DIFFRACTION' 12 12 C 301 ? ? C 321 ? ? ? ? 'X-RAY DIFFRACTION' 13 13 D 1 ? ? D 31 ? ? ? ? 'X-RAY DIFFRACTION' 14 14 D 32 ? ? D 61 ? ? ? ? 'X-RAY DIFFRACTION' 15 15 D 62 ? ? D 124 ? ? ? ? 'X-RAY DIFFRACTION' 16 16 D 125 ? ? D 157 ? ? ? ? 'X-RAY DIFFRACTION' 17 17 E -1 ? ? E 85 ? ? ? ? 'X-RAY DIFFRACTION' 18 18 E 86 ? ? E 123 ? ? ? ? 'X-RAY DIFFRACTION' 19 19 E 124 ? ? E 267 ? ? ? ? 'X-RAY DIFFRACTION' 20 20 E 268 ? ? E 321 ? ? ? ? 'X-RAY DIFFRACTION' 21 21 F 1 ? ? F 57 ? ? ? ? 'X-RAY DIFFRACTION' 22 22 F 58 ? ? F 83 ? ? ? ? 'X-RAY DIFFRACTION' 23 23 F 84 ? ? F 136 ? ? ? ? 'X-RAY DIFFRACTION' 24 24 F 137 ? ? F 157 ? ? ? ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.7.0032 ? 1 XDS 'data reduction' . ? 2 SCALA 'data scaling' . ? 3 PHASER phasing . ? 4 # _pdbx_entry_details.entry_id 4BH0 _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details 'MULTIBASIC SITE REMOVED' # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 NE2 C GLN 169 ? ? O C HOH 2137 ? ? 2.08 2 1 O1 A PO4 1325 ? ? O A HOH 2180 ? ? 2.14 # _pdbx_validate_rmsd_angle.id 1 _pdbx_validate_rmsd_angle.PDB_model_num 1 _pdbx_validate_rmsd_angle.auth_atom_id_1 NE _pdbx_validate_rmsd_angle.auth_asym_id_1 E _pdbx_validate_rmsd_angle.auth_comp_id_1 ARG _pdbx_validate_rmsd_angle.auth_seq_id_1 216 _pdbx_validate_rmsd_angle.PDB_ins_code_1 ? _pdbx_validate_rmsd_angle.label_alt_id_1 ? _pdbx_validate_rmsd_angle.auth_atom_id_2 CZ _pdbx_validate_rmsd_angle.auth_asym_id_2 E _pdbx_validate_rmsd_angle.auth_comp_id_2 ARG _pdbx_validate_rmsd_angle.auth_seq_id_2 216 _pdbx_validate_rmsd_angle.PDB_ins_code_2 ? _pdbx_validate_rmsd_angle.label_alt_id_2 ? _pdbx_validate_rmsd_angle.auth_atom_id_3 NH2 _pdbx_validate_rmsd_angle.auth_asym_id_3 E _pdbx_validate_rmsd_angle.auth_comp_id_3 ARG _pdbx_validate_rmsd_angle.auth_seq_id_3 216 _pdbx_validate_rmsd_angle.PDB_ins_code_3 ? _pdbx_validate_rmsd_angle.label_alt_id_3 ? _pdbx_validate_rmsd_angle.angle_value 117.23 _pdbx_validate_rmsd_angle.angle_target_value 120.30 _pdbx_validate_rmsd_angle.angle_deviation -3.07 _pdbx_validate_rmsd_angle.angle_standard_deviation 0.50 _pdbx_validate_rmsd_angle.linker_flag N # 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 ASN A 11 ? ? -100.69 52.81 2 1 THR A 13 ? ? 66.40 -27.26 3 1 ASN A 23 ? ? 50.90 70.39 4 1 ASP A 45 ? ? 38.67 45.76 5 1 ARG A 53 ? ? 57.75 -113.04 6 1 ASP A 88 ? ? -106.95 -112.81 7 1 CYS A 135 ? ? -117.18 69.37 8 1 TYR A 137 ? ? -166.52 115.75 9 1 SER A 142 ? ? -146.43 -156.97 10 1 GLN A 192 ? ? 75.84 -48.93 11 1 THR A 202 ? ? -127.40 -156.35 12 1 ASN A 206 ? ? -152.55 86.60 13 1 THR B 61 ? ? -111.44 52.19 14 1 ARG B 127 ? ? -94.02 -71.24 15 1 LEU B 133 ? ? -93.22 -63.16 16 1 ASN B 135 ? ? -99.98 31.38 17 1 ARG C 53 ? ? 61.12 -103.47 18 1 ASP C 88 ? ? -113.76 -109.91 19 1 TYR C 137 ? ? -160.05 114.98 20 1 SER C 142 ? ? -143.29 -153.20 21 1 ASN C 166 ? ? -65.22 92.56 22 1 GLN C 192 ? ? 67.43 -57.63 23 1 THR C 202 ? ? -128.07 -161.82 24 1 ASN C 206 ? ? -150.95 80.87 25 1 SER C 243 ? ? -172.11 143.75 26 1 GLU C 251 ? ? -120.27 -59.49 27 1 THR C 315 ? ? -130.71 -49.92 28 1 ALA D 35 ? ? -163.07 116.92 29 1 LEU D 133 ? ? -90.97 -64.82 30 1 ASN D 135 ? ? -94.60 32.76 31 1 ASN E 10 ? ? -161.52 -158.27 32 1 ASN E 23 ? ? 36.67 67.34 33 1 ARG E 53 ? ? 58.00 -109.70 34 1 ASP E 88 ? ? -128.67 -121.39 35 1 SER E 142 ? ? -146.12 -155.35 36 1 GLN E 192 ? ? 66.42 -54.49 37 1 THR E 202 ? ? -132.37 -146.79 38 1 ASN E 236 ? ? 73.21 -0.36 # loop_ _pdbx_distant_solvent_atoms.id _pdbx_distant_solvent_atoms.PDB_model_num _pdbx_distant_solvent_atoms.auth_atom_id _pdbx_distant_solvent_atoms.label_alt_id _pdbx_distant_solvent_atoms.auth_asym_id _pdbx_distant_solvent_atoms.auth_comp_id _pdbx_distant_solvent_atoms.auth_seq_id _pdbx_distant_solvent_atoms.PDB_ins_code _pdbx_distant_solvent_atoms.neighbor_macromolecule_distance _pdbx_distant_solvent_atoms.neighbor_ligand_distance 1 1 O ? C HOH 2013 ? 5.87 . 2 1 O ? C HOH 2028 ? 6.25 . 3 1 O ? C HOH 2055 ? 6.21 . 4 1 O ? E HOH 2024 ? 6.80 . 5 1 O ? F HOH 2027 ? 7.29 . 6 1 O ? F HOH 2028 ? 6.62 . 7 1 O ? F HOH 2029 ? 6.97 . 8 1 O ? F HOH 2030 ? . 5.91 9 1 O ? F HOH 2031 ? 7.90 . 10 1 O ? F HOH 2032 ? 9.28 . 11 1 O ? F HOH 2033 ? 7.19 . 12 1 O ? F HOH 2034 ? . 9.01 13 1 O ? F HOH 2037 ? . 7.80 14 1 O ? F HOH 2038 ? 6.78 . 15 1 O ? F HOH 2039 ? 6.25 . 16 1 O ? F HOH 2040 ? 7.06 . 17 1 O ? F HOH 2041 ? 7.70 . 18 1 O ? F HOH 2044 ? 7.42 . 19 1 O ? F HOH 2045 ? 7.03 . 20 1 O ? F HOH 2046 ? 8.79 . 21 1 O ? F HOH 2047 ? 7.69 . 22 1 O ? F HOH 2048 ? 6.72 . 23 1 O ? F HOH 2049 ? 6.56 . 24 1 O ? F HOH 2050 ? 8.72 . 25 1 O ? F HOH 2051 ? 8.84 . # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 A LYS 22 ? CG ? A LYS 23 CG 2 1 Y 1 A LYS 22 ? CD ? A LYS 23 CD 3 1 Y 1 A LYS 22 ? CE ? A LYS 23 CE 4 1 Y 1 A LYS 22 ? NZ ? A LYS 23 NZ 5 1 Y 1 B GLU 11 ? CG ? B GLU 11 CG 6 1 Y 1 B GLU 11 ? CD ? B GLU 11 CD 7 1 Y 1 B GLU 11 ? OE1 ? B GLU 11 OE1 8 1 Y 1 B GLU 11 ? OE2 ? B GLU 11 OE2 9 1 Y 1 B VAL 18 ? CG1 ? B VAL 18 CG1 10 1 Y 1 B VAL 18 ? CG2 ? B VAL 18 CG2 11 1 Y 1 B LYS 38 ? CD ? B LYS 38 CD 12 1 Y 1 B LYS 38 ? CE ? B LYS 38 CE 13 1 Y 1 B LYS 38 ? NZ ? B LYS 38 NZ 14 1 Y 1 B GLU 39 ? CG ? B GLU 39 CG 15 1 Y 1 B GLU 39 ? CD ? B GLU 39 CD 16 1 Y 1 B GLU 39 ? OE1 ? B GLU 39 OE1 17 1 Y 1 B GLU 39 ? OE2 ? B GLU 39 OE2 18 1 Y 1 B GLN 42 ? CG ? B GLN 42 CG 19 1 Y 1 B GLN 42 ? CD ? B GLN 42 CD 20 1 Y 1 B GLN 42 ? OE1 ? B GLN 42 OE1 21 1 Y 1 B GLN 42 ? NE2 ? B GLN 42 NE2 22 1 Y 1 B LYS 43 ? CD ? B LYS 43 CD 23 1 Y 1 B LYS 43 ? CE ? B LYS 43 CE 24 1 Y 1 B LYS 43 ? NZ ? B LYS 43 NZ 25 1 Y 1 B LYS 58 ? CG ? B LYS 58 CG 26 1 Y 1 B LYS 58 ? CD ? B LYS 58 CD 27 1 Y 1 B LYS 58 ? CE ? B LYS 58 CE 28 1 Y 1 B LYS 58 ? NZ ? B LYS 58 NZ 29 1 Y 1 B GLU 103 ? CG ? B GLU 103 CG 30 1 Y 1 B GLU 103 ? CD ? B GLU 103 CD 31 1 Y 1 B GLU 103 ? OE1 ? B GLU 103 OE1 32 1 Y 1 B GLU 103 ? OE2 ? B GLU 103 OE2 33 1 Y 1 B LYS 116 ? CG ? B LYS 116 CG 34 1 Y 1 B LYS 116 ? CD ? B LYS 116 CD 35 1 Y 1 B LYS 116 ? CE ? B LYS 116 CE 36 1 Y 1 B LYS 116 ? NZ ? B LYS 116 NZ 37 1 Y 1 B ARG 123 ? CG ? B ARG 123 CG 38 1 Y 1 B ARG 123 ? CD ? B ARG 123 CD 39 1 Y 1 B ARG 123 ? NE ? B ARG 123 NE 40 1 Y 1 B ARG 123 ? CZ ? B ARG 123 CZ 41 1 Y 1 B ARG 123 ? NH1 ? B ARG 123 NH1 42 1 Y 1 B ARG 123 ? NH2 ? B ARG 123 NH2 43 1 Y 1 B LEU 124 ? CG ? B LEU 124 CG 44 1 Y 1 B LEU 124 ? CD1 ? B LEU 124 CD1 45 1 Y 1 B LEU 124 ? CD2 ? B LEU 124 CD2 46 1 Y 1 B LEU 126 ? CG ? B LEU 126 CG 47 1 Y 1 B LEU 126 ? CD1 ? B LEU 126 CD1 48 1 Y 1 B LEU 126 ? CD2 ? B LEU 126 CD2 49 1 Y 1 B ARG 127 ? CG ? B ARG 127 CG 50 1 Y 1 B ARG 127 ? CD ? B ARG 127 CD 51 1 Y 1 B ARG 127 ? NE ? B ARG 127 NE 52 1 Y 1 B ARG 127 ? CZ ? B ARG 127 CZ 53 1 Y 1 B ARG 127 ? NH1 ? B ARG 127 NH1 54 1 Y 1 B ARG 127 ? NH2 ? B ARG 127 NH2 55 1 Y 1 B ASP 128 ? CG ? B ASP 128 CG 56 1 Y 1 B ASP 128 ? OD1 ? B ASP 128 OD1 57 1 Y 1 B ASP 128 ? OD2 ? B ASP 128 OD2 58 1 Y 1 B ASN 129 ? CG ? B ASN 129 CG 59 1 Y 1 B ASN 129 ? OD1 ? B ASN 129 OD1 60 1 Y 1 B ASN 129 ? ND2 ? B ASN 129 ND2 61 1 Y 1 C LYS 22 ? CG ? C LYS 23 CG 62 1 Y 1 C LYS 22 ? CD ? C LYS 23 CD 63 1 Y 1 C LYS 22 ? CE ? C LYS 23 CE 64 1 Y 1 C LYS 22 ? NZ ? C LYS 23 NZ 65 1 Y 1 C GLU 270 ? CG ? C GLU 271 CG 66 1 Y 1 C GLU 270 ? CD ? C GLU 271 CD 67 1 Y 1 C GLU 270 ? OE1 ? C GLU 271 OE1 68 1 Y 1 C GLU 270 ? OE2 ? C GLU 271 OE2 69 1 Y 1 C GLU 301 ? CD ? C GLU 302 CD 70 1 Y 1 C GLU 301 ? OE1 ? C GLU 302 OE1 71 1 Y 1 C GLU 301 ? OE2 ? C GLU 302 OE2 72 1 Y 1 D GLU 11 ? CG ? D GLU 11 CG 73 1 Y 1 D GLU 11 ? CD ? D GLU 11 CD 74 1 Y 1 D GLU 11 ? OE1 ? D GLU 11 OE1 75 1 Y 1 D GLU 11 ? OE2 ? D GLU 11 OE2 76 1 Y 1 D VAL 18 ? CG1 ? D VAL 18 CG1 77 1 Y 1 D VAL 18 ? CG2 ? D VAL 18 CG2 78 1 Y 1 D LYS 38 ? CD ? D LYS 38 CD 79 1 Y 1 D LYS 38 ? CE ? D LYS 38 CE 80 1 Y 1 D LYS 38 ? NZ ? D LYS 38 NZ 81 1 Y 1 D GLU 39 ? CG ? D GLU 39 CG 82 1 Y 1 D GLU 39 ? CD ? D GLU 39 CD 83 1 Y 1 D GLU 39 ? OE1 ? D GLU 39 OE1 84 1 Y 1 D GLU 39 ? OE2 ? D GLU 39 OE2 85 1 Y 1 D GLN 42 ? CG ? D GLN 42 CG 86 1 Y 1 D GLN 42 ? CD ? D GLN 42 CD 87 1 Y 1 D GLN 42 ? OE1 ? D GLN 42 OE1 88 1 Y 1 D GLN 42 ? NE2 ? D GLN 42 NE2 89 1 Y 1 D LYS 43 ? CD ? D LYS 43 CD 90 1 Y 1 D LYS 43 ? CE ? D LYS 43 CE 91 1 Y 1 D LYS 43 ? NZ ? D LYS 43 NZ 92 1 Y 1 D LYS 83 ? CD ? D LYS 83 CD 93 1 Y 1 D LYS 83 ? CE ? D LYS 83 CE 94 1 Y 1 D LYS 83 ? NZ ? D LYS 83 NZ 95 1 Y 1 D GLU 103 ? CG ? D GLU 103 CG 96 1 Y 1 D GLU 103 ? CD ? D GLU 103 CD 97 1 Y 1 D GLU 103 ? OE1 ? D GLU 103 OE1 98 1 Y 1 D GLU 103 ? OE2 ? D GLU 103 OE2 99 1 Y 1 D ARG 106 ? CG ? D ARG 106 CG 100 1 Y 1 D ARG 106 ? CD ? D ARG 106 CD 101 1 Y 1 D ARG 106 ? NE ? D ARG 106 NE 102 1 Y 1 D ARG 106 ? CZ ? D ARG 106 CZ 103 1 Y 1 D ARG 106 ? NH1 ? D ARG 106 NH1 104 1 Y 1 D ARG 106 ? NH2 ? D ARG 106 NH2 105 1 Y 1 D LEU 126 ? CG ? D LEU 126 CG 106 1 Y 1 D LEU 126 ? CD1 ? D LEU 126 CD1 107 1 Y 1 D LEU 126 ? CD2 ? D LEU 126 CD2 108 1 Y 1 D ARG 127 ? CG ? D ARG 127 CG 109 1 Y 1 D ARG 127 ? CD ? D ARG 127 CD 110 1 Y 1 D ARG 127 ? NE ? D ARG 127 NE 111 1 Y 1 D ARG 127 ? CZ ? D ARG 127 CZ 112 1 Y 1 D ARG 127 ? NH1 ? D ARG 127 NH1 113 1 Y 1 D ARG 127 ? NH2 ? D ARG 127 NH2 114 1 Y 1 D ASP 128 ? CG ? D ASP 128 CG 115 1 Y 1 D ASP 128 ? OD1 ? D ASP 128 OD1 116 1 Y 1 D ASP 128 ? OD2 ? D ASP 128 OD2 117 1 Y 1 D THR 156 ? OG1 ? D THR 156 OG1 118 1 Y 1 D THR 156 ? CG2 ? D THR 156 CG2 119 1 Y 1 E LYS 22 ? CG ? E LYS 23 CG 120 1 Y 1 E LYS 22 ? CD ? E LYS 23 CD 121 1 Y 1 E LYS 22 ? CE ? E LYS 23 CE 122 1 Y 1 E LYS 22 ? NZ ? E LYS 23 NZ 123 1 Y 1 E GLU 270 ? CG ? E GLU 271 CG 124 1 Y 1 E GLU 270 ? CD ? E GLU 271 CD 125 1 Y 1 E GLU 270 ? OE1 ? E GLU 271 OE1 126 1 Y 1 E GLU 270 ? OE2 ? E GLU 271 OE2 127 1 Y 1 E GLU 301 ? CD ? E GLU 302 CD 128 1 Y 1 E GLU 301 ? OE1 ? E GLU 302 OE1 129 1 Y 1 E GLU 301 ? OE2 ? E GLU 302 OE2 130 1 Y 1 E LEU 317 ? CG ? E LEU 318 CG 131 1 Y 1 E LEU 317 ? CD1 ? E LEU 318 CD1 132 1 Y 1 E LEU 317 ? CD2 ? E LEU 318 CD2 133 1 Y 1 F GLU 11 ? CG ? F GLU 11 CG 134 1 Y 1 F GLU 11 ? CD ? F GLU 11 CD 135 1 Y 1 F GLU 11 ? OE1 ? F GLU 11 OE1 136 1 Y 1 F GLU 11 ? OE2 ? F GLU 11 OE2 137 1 Y 1 F VAL 18 ? CG1 ? F VAL 18 CG1 138 1 Y 1 F VAL 18 ? CG2 ? F VAL 18 CG2 139 1 Y 1 F LYS 38 ? CD ? F LYS 38 CD 140 1 Y 1 F LYS 38 ? CE ? F LYS 38 CE 141 1 Y 1 F LYS 38 ? NZ ? F LYS 38 NZ 142 1 Y 1 F GLU 39 ? CG ? F GLU 39 CG 143 1 Y 1 F GLU 39 ? CD ? F GLU 39 CD 144 1 Y 1 F GLU 39 ? OE1 ? F GLU 39 OE1 145 1 Y 1 F GLU 39 ? OE2 ? F GLU 39 OE2 146 1 Y 1 F GLN 42 ? CG ? F GLN 42 CG 147 1 Y 1 F GLN 42 ? CD ? F GLN 42 CD 148 1 Y 1 F GLN 42 ? OE1 ? F GLN 42 OE1 149 1 Y 1 F GLN 42 ? NE2 ? F GLN 42 NE2 150 1 Y 1 F LYS 43 ? CD ? F LYS 43 CD 151 1 Y 1 F LYS 43 ? CE ? F LYS 43 CE 152 1 Y 1 F LYS 43 ? NZ ? F LYS 43 NZ 153 1 Y 1 F GLU 103 ? CG ? F GLU 103 CG 154 1 Y 1 F GLU 103 ? CD ? F GLU 103 CD 155 1 Y 1 F GLU 103 ? OE1 ? F GLU 103 OE1 156 1 Y 1 F GLU 103 ? OE2 ? F GLU 103 OE2 157 1 Y 1 F LEU 124 ? CG ? F LEU 124 CG 158 1 Y 1 F LEU 124 ? CD1 ? F LEU 124 CD1 159 1 Y 1 F LEU 124 ? CD2 ? F LEU 124 CD2 160 1 Y 1 F ARG 127 ? CG ? F ARG 127 CG 161 1 Y 1 F ARG 127 ? CD ? F ARG 127 CD 162 1 Y 1 F ARG 127 ? NE ? F ARG 127 NE 163 1 Y 1 F ARG 127 ? CZ ? F ARG 127 CZ 164 1 Y 1 F ARG 127 ? NH1 ? F ARG 127 NH1 165 1 Y 1 F ARG 127 ? NH2 ? F ARG 127 NH2 166 1 Y 1 F GLU 132 ? CG ? F GLU 132 CG 167 1 Y 1 F GLU 132 ? CD ? F GLU 132 CD 168 1 Y 1 F GLU 132 ? OE1 ? F GLU 132 OE1 169 1 Y 1 F GLU 132 ? OE2 ? F GLU 132 OE2 170 1 Y 1 F PHE 138 ? CG ? F PHE 138 CG 171 1 Y 1 F PHE 138 ? CD1 ? F PHE 138 CD1 172 1 Y 1 F PHE 138 ? CD2 ? F PHE 138 CD2 173 1 Y 1 F PHE 138 ? CE1 ? F PHE 138 CE1 174 1 Y 1 F PHE 138 ? CE2 ? F PHE 138 CE2 175 1 Y 1 F PHE 138 ? CZ ? F PHE 138 CZ 176 1 Y 1 F THR 156 ? OG1 ? F THR 156 OG1 177 1 Y 1 F THR 156 ? CG2 ? F THR 156 CG2 # 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 PRO 0 ? A PRO 1 2 1 Y 1 A SER 320 ? A SER 321 3 1 Y 1 A PRO 321 ? A PRO 322 4 1 Y 1 A GLN 322 ? A GLN 323 5 1 Y 1 A ARG 323 ? A ARG 324 6 1 Y 1 A GLU 324 ? A GLU 325 7 1 Y 1 A THR 325 ? A THR 326 8 1 Y 1 A ARG 326 ? A ARG 327 9 1 Y 1 B GLY 1 ? B GLY 1 10 1 Y 1 B LEU 2 ? B LEU 2 11 1 Y 1 B PHE 3 ? B PHE 3 12 1 Y 1 B GLY 4 ? B GLY 4 13 1 Y 1 B ALA 5 ? B ALA 5 14 1 Y 1 B ILE 6 ? B ILE 6 15 1 Y 1 B ALA 7 ? B ALA 7 16 1 Y 1 B GLY 8 ? B GLY 8 17 1 Y 1 B PHE 9 ? B PHE 9 18 1 Y 1 B THR 156 ? B THR 156 19 1 Y 1 B TYR 157 ? B TYR 157 20 1 Y 1 B ASP 158 ? B ASP 158 21 1 Y 1 B TYR 159 ? B TYR 159 22 1 Y 1 B PRO 160 ? B PRO 160 23 1 Y 1 B GLN 161 ? B GLN 161 24 1 Y 1 B TYR 162 ? B TYR 162 25 1 Y 1 B SER 163 ? B SER 163 26 1 Y 1 B GLU 164 ? B GLU 164 27 1 Y 1 B GLU 165 ? B GLU 165 28 1 Y 1 B ALA 166 ? B ALA 166 29 1 Y 1 C PRO 0 ? C PRO 1 30 1 Y 1 C SER 320 ? C SER 321 31 1 Y 1 C PRO 321 ? C PRO 322 32 1 Y 1 C GLN 322 ? C GLN 323 33 1 Y 1 C ARG 323 ? C ARG 324 34 1 Y 1 C GLU 324 ? C GLU 325 35 1 Y 1 C THR 325 ? C THR 326 36 1 Y 1 C ARG 326 ? C ARG 327 37 1 Y 1 D GLY 1 ? D GLY 1 38 1 Y 1 D LEU 2 ? D LEU 2 39 1 Y 1 D PHE 3 ? D PHE 3 40 1 Y 1 D GLY 4 ? D GLY 4 41 1 Y 1 D ALA 5 ? D ALA 5 42 1 Y 1 D ILE 6 ? D ILE 6 43 1 Y 1 D ALA 7 ? D ALA 7 44 1 Y 1 D GLY 8 ? D GLY 8 45 1 Y 1 D PHE 9 ? D PHE 9 46 1 Y 1 D ASP 158 ? D ASP 158 47 1 Y 1 D TYR 159 ? D TYR 159 48 1 Y 1 D PRO 160 ? D PRO 160 49 1 Y 1 D GLN 161 ? D GLN 161 50 1 Y 1 D TYR 162 ? D TYR 162 51 1 Y 1 D SER 163 ? D SER 163 52 1 Y 1 D GLU 164 ? D GLU 164 53 1 Y 1 D GLU 165 ? D GLU 165 54 1 Y 1 D ALA 166 ? D ALA 166 55 1 Y 1 E SER 320 ? E SER 321 56 1 Y 1 E PRO 321 ? E PRO 322 57 1 Y 1 E GLN 322 ? E GLN 323 58 1 Y 1 E ARG 323 ? E ARG 324 59 1 Y 1 E GLU 324 ? E GLU 325 60 1 Y 1 E THR 325 ? E THR 326 61 1 Y 1 E ARG 326 ? E ARG 327 62 1 Y 1 F GLY 1 ? F GLY 1 63 1 Y 1 F LEU 2 ? F LEU 2 64 1 Y 1 F PHE 3 ? F PHE 3 65 1 Y 1 F GLY 4 ? F GLY 4 66 1 Y 1 F ALA 5 ? F ALA 5 67 1 Y 1 F ILE 6 ? F ILE 6 68 1 Y 1 F ALA 7 ? F ALA 7 69 1 Y 1 F GLY 8 ? F GLY 8 70 1 Y 1 F PHE 9 ? F PHE 9 71 1 Y 1 F ASP 158 ? F ASP 158 72 1 Y 1 F TYR 159 ? F TYR 159 73 1 Y 1 F PRO 160 ? F PRO 160 74 1 Y 1 F GLN 161 ? F GLN 161 75 1 Y 1 F TYR 162 ? F TYR 162 76 1 Y 1 F SER 163 ? F SER 163 77 1 Y 1 F GLU 164 ? F GLU 164 78 1 Y 1 F GLU 165 ? F GLU 165 79 1 Y 1 F ALA 166 ? F ALA 166 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 3 N-ACETYL-D-GLUCOSAMINE NAG 4 'O-SIALIC ACID' SIA 5 BETA-D-GALACTOSE GAL 6 'PHOSPHATE ION' PO4 7 water HOH #